doc_id	sent_index	relation_id	relation	trigger	trigger_offset	arg_num	arg_head	arg_protein	arg_domain	arg_site	arg_sugar	arg_head_offset	arg_base_np	arg_base_np_offset	arg_np	arg_np_offset	sent_text
29932112	5	0	theme	cell-surface	745:756	arg1	biotinylation					758:770	cell-surface biotinylation	745:770	cell-surface biotinylation	745:770	We used site-directed mutagenesis, enzymatic de-glycosylation, cell-surface biotinylation, co-immunoprecipitation, and confocal microscopy.
29932112	1	1	gly	glycoproteins	147:159	arg1	glycoproteins					147:159	channel-forming glycoproteins	131:159	channel-forming glycoproteins expressed in mammalian tissues	131:190	Pannexins (Panx1, 2, 3) are channel-forming glycoproteins expressed in mammalian tissues.
29932112	1	1	gly	glycoproteins	147:159	arg1	Pannexins					103:111	Pannexins	103:111	Pannexins (Panx1, 2, 3)	103:125	Pannexins (Panx1, 2, 3) are channel-forming glycoproteins expressed in mammalian tissues.
29932112	8	2	theme	N86Q	1091:1094	arg1	glycosylation-deficient					1106:1128	glycosylation-deficient	1106:1128	glycosylation-deficient	1106:1128	The Panx2 N86Q mutant is glycosylation-deficient and tends to aggregate in the ER reducing its cell surface trafficking but it can still interact with Panx1.
29932112	8	2	theme	N86Q	1091:1094	arg1	mutant					1096:1101	The Panx2 N86Q mutant	1081:1101	The Panx2 N86Q mutant	1081:1101	The Panx2 N86Q mutant is glycosylation-deficient and tends to aggregate in the ER reducing its cell surface trafficking but it can still interact with Panx1.
29932112	3	3	theme	cell	474:477	arg1	death					479:483	neuronal cell death	465:483	neuronal cell death after ischemia	465:498	Panx1 and Panx2 intermixing can regulate channel properties, and both pannexins have been implicated in neuronal cell death after ischemia.
29932112	7	4	theme	endoplasmic	954:964	arg1	ER					977:978	ER	977:978	ER	977:978	Panx2 and the N86Q mutant are predominantly localized to the endoplasmic reticulum (ER) and cis-Golgi matrix with limited cell surface localization was seen only in the presence of Panx1.
29932112	7	4	theme	endoplasmic	954:964	arg1	reticulum					966:974	the endoplasmic reticulum	950:974	the endoplasmic reticulum (ER)	950:979	Panx2 and the N86Q mutant are predominantly localized to the endoplasmic reticulum (ER) and cis-Golgi matrix with limited cell surface localization was seen only in the presence of Panx1.
29932112	2	5	dep	localization	264:275	arg1	the					260:262	the	260:262	the	260:262	We previously reported that N-glycosylation acts as a regulator of the localization and intermixing of Panx1 and Panx3, but its effects on Panx2 are currently unknown.
29932112	4	6	theme	N-glycosylation	547:561	arg1	Panx2					571:575	Panx2	571:575	Panx2	571:575	Our objectives were to validate the predicted N-glycosylation site of Panx2 and to study the effects of Panx2 glycosylation on localization and its capacity to interact with Panx1.
29932112	4	6	theme	N-glycosylation	547:561	arg1	site					563:566	the predicted N-glycosylation site	533:566	the predicted N-glycosylation site of Panx2	533:575	Our objectives were to validate the predicted N-glycosylation site of Panx2 and to study the effects of Panx2 glycosylation on localization and its capacity to interact with Panx1.
29932112	5	7	theme	site-directed	690:702	arg1	mutagenesis					704:714	site-directed mutagenesis	690:714	site-directed mutagenesis	690:714	We used site-directed mutagenesis, enzymatic de-glycosylation, cell-surface biotinylation, co-immunoprecipitation, and confocal microscopy.
29932112	10	8	theme	2	1388:1388	arg1	forms					1369:1373	the un-glycosylated forms	1349:1373	the un-glycosylated forms of Panx1 and 2	1349:1388	We found that the un-glycosylated forms of Panx1 and 2 can readily interact, regulating their localization and potentially their channel function in cells where they are co-expressed.
29932112	4	9	theme	Panx2	571:575	arg1	Panx2					571:575	Panx2	571:575	Panx2	571:575	Our objectives were to validate the predicted N-glycosylation site of Panx2 and to study the effects of Panx2 glycosylation on localization and its capacity to interact with Panx1.
29932112	4	9	theme	Panx2	571:575	arg1	site					563:566	the predicted N-glycosylation site	533:566	the predicted N-glycosylation site of Panx2	533:575	Our objectives were to validate the predicted N-glycosylation site of Panx2 and to study the effects of Panx2 glycosylation on localization and its capacity to interact with Panx1.
29932112	10	10	theme	un-glycosylated	1353:1367	arg1	forms					1369:1373	the un-glycosylated forms	1349:1373	the un-glycosylated forms of Panx1 and 2	1349:1388	We found that the un-glycosylated forms of Panx1 and 2 can readily interact, regulating their localization and potentially their channel function in cells where they are co-expressed.
29932112	2	11	theme	localization	264:275	arg1	N-glycosylation					221:235	N-glycosylation	221:235	N-glycosylation	221:235	We previously reported that N-glycosylation acts as a regulator of the localization and intermixing of Panx1 and Panx3, but its effects on Panx2 are currently unknown.
29932112	2	11	theme	localization	264:275	arg1	regulator					247:255	a regulator	245:255	a regulator of the localization and intermixing of Panx1 and Panx3	245:310	We previously reported that N-glycosylation acts as a regulator of the localization and intermixing of Panx1 and Panx3, but its effects on Panx2 are currently unknown.
29932112	9	12	gly	N-glycosylation	1264:1278	arg1	Panx2					1328:1332	Panx2	1328:1332	Panx2	1328:1332	Our study indicates that N-glycosylation may be important for folding and trafficking of Panx2.
29932112	6	13	theme	Panx2	886:890	arg1	Panx2					886:890	Panx2	886:890	Panx2	886:890	Our results showed that N86 is the only N-glycosylation site of Panx2.
29932112	6	13	theme	Panx2	886:890	arg1	site					878:881	the only N-glycosylation site	853:881	the only N-glycosylation site of Panx2	853:890	Our results showed that N86 is the only N-glycosylation site of Panx2.
29932112	6	13	theme	Panx2	886:890	arg1	N86					846:848	N86	846:848	N86	846:848	Our results showed that N86 is the only N-glycosylation site of Panx2.
29932112	7	14	theme	Panx1	1074:1078	arg1	presence					1062:1069	the presence	1058:1069	the presence of Panx1	1058:1078	Panx2 and the N86Q mutant are predominantly localized to the endoplasmic reticulum (ER) and cis-Golgi matrix with limited cell surface localization was seen only in the presence of Panx1.
29932112	1	15	theme	channel-forming	131:145	arg1	glycoproteins					147:159	channel-forming glycoproteins	131:159	channel-forming glycoproteins expressed in mammalian tissues	131:190	Pannexins (Panx1, 2, 3) are channel-forming glycoproteins expressed in mammalian tissues.
29932112	1	15	theme	channel-forming	131:145	arg1	Pannexins					103:111	Pannexins	103:111	Pannexins (Panx1, 2, 3)	103:125	Pannexins (Panx1, 2, 3) are channel-forming glycoproteins expressed in mammalian tissues.
29932112	5	16	theme	enzymatic	717:725	arg1	de-glycosylation					727:742	enzymatic de-glycosylation	717:742	enzymatic de-glycosylation	717:742	We used site-directed mutagenesis, enzymatic de-glycosylation, cell-surface biotinylation, co-immunoprecipitation, and confocal microscopy.
29932112	4	17	gly	N-glycosylation	547:561	arg1	Panx2					571:575	Panx2	571:575	Panx2	571:575	Our objectives were to validate the predicted N-glycosylation site of Panx2 and to study the effects of Panx2 glycosylation on localization and its capacity to interact with Panx1.
29932112	4	17	gly	N-glycosylation	547:561	arg2	Panx2					571:575	Panx2	571:575	Panx2	571:575	Our objectives were to validate the predicted N-glycosylation site of Panx2 and to study the effects of Panx2 glycosylation on localization and its capacity to interact with Panx1.
29932112	4	17	gly	N-glycosylation	547:561	arg2	site					563:566	the predicted N-glycosylation site	533:566	the predicted N-glycosylation site of Panx2	533:575	Our objectives were to validate the predicted N-glycosylation site of Panx2 and to study the effects of Panx2 glycosylation on localization and its capacity to interact with Panx1.
29932112	5	18	theme	confocal	801:808	arg1	microscopy					810:819	confocal microscopy	801:819	confocal microscopy	801:819	We used site-directed mutagenesis, enzymatic de-glycosylation, cell-surface biotinylation, co-immunoprecipitation, and confocal microscopy.
29932112	2	19	from	effects	321:327	arg1	Panx2					332:336	Panx2	332:336	Panx2	332:336	We previously reported that N-glycosylation acts as a regulator of the localization and intermixing of Panx1 and Panx3, but its effects on Panx2 are currently unknown.
29932112	10	20	gly	un-glycosylated	1353:1367	arg1	forms					1369:1373	the un-glycosylated forms	1349:1373	the un-glycosylated forms of Panx1 and 2	1349:1388	We found that the un-glycosylated forms of Panx1 and 2 can readily interact, regulating their localization and potentially their channel function in cells where they are co-expressed.
29932112	10	20	gly	un-glycosylated	1353:1367	arg1	Panx1					1378:1382	Panx1	1378:1382	Panx1	1378:1382	We found that the un-glycosylated forms of Panx1 and 2 can readily interact, regulating their localization and potentially their channel function in cells where they are co-expressed.
29932112	2	21	theme	Panx1	296:300	arg1	localization					264:275	localization	264:275	localization	264:275	We previously reported that N-glycosylation acts as a regulator of the localization and intermixing of Panx1 and Panx3, but its effects on Panx2 are currently unknown.
29932112	2	21	theme	Panx1	296:300	arg1	intermixing					281:291	intermixing	281:291	intermixing	281:291	We previously reported that N-glycosylation acts as a regulator of the localization and intermixing of Panx1 and Panx3, but its effects on Panx2 are currently unknown.
29932112	3	22	theme	channel	402:408	arg1	properties					410:419	channel properties	402:419	channel properties	402:419	Panx1 and Panx2 intermixing can regulate channel properties, and both pannexins have been implicated in neuronal cell death after ischemia.
29932112	8	23	theme	cell	1176:1179	arg1	trafficking					1189:1199	its cell surface trafficking	1172:1199	its cell surface trafficking	1172:1199	The Panx2 N86Q mutant is glycosylation-deficient and tends to aggregate in the ER reducing its cell surface trafficking but it can still interact with Panx1.
29932112	10	24	theme	Panx1	1378:1382	arg1	forms					1369:1373	the un-glycosylated forms	1349:1373	the un-glycosylated forms of Panx1 and 2	1349:1388	We found that the un-glycosylated forms of Panx1 and 2 can readily interact, regulating their localization and potentially their channel function in cells where they are co-expressed.
29932112	6	25	gly	N-glycosylation	862:876	arg1	Panx2					886:890	Panx2	886:890	Panx2	886:890	Our results showed that N86 is the only N-glycosylation site of Panx2.
29932112	6	25	gly	N-glycosylation	862:876	arg2	site					878:881	the only N-glycosylation site	853:881	the only N-glycosylation site of Panx2	853:890	Our results showed that N86 is the only N-glycosylation site of Panx2.
29932112	6	25	gly	N-glycosylation	862:876	arg2	N86					846:848	N86	846:848	N86	846:848	Our results showed that N86 is the only N-glycosylation site of Panx2.
29932112	6	25	gly	N-glycosylation	862:876	arg2	Panx2					886:890	Panx2	886:890	Panx2	886:890	Our results showed that N86 is the only N-glycosylation site of Panx2.
29932112	1	26	theme	mammalian	174:182	arg1	tissues					184:190	mammalian tissues	174:190	mammalian tissues	174:190	Pannexins (Panx1, 2, 3) are channel-forming glycoproteins expressed in mammalian tissues.
29932112	0	27	theme	Pannexin	26:33	arg1	Localization					37:48	Pannexin 2 Localization	26:48	Pannexin 2 Localization	26:48	N-Glycosylation Regulates Pannexin 2 Localization but Is Not Required for Interacting with Pannexin 1.
29932112	4	28	theme	predicted	537:545	arg1	Panx2					571:575	Panx2	571:575	Panx2	571:575	Our objectives were to validate the predicted N-glycosylation site of Panx2 and to study the effects of Panx2 glycosylation on localization and its capacity to interact with Panx1.
29932112	4	28	theme	predicted	537:545	arg1	site					563:566	the predicted N-glycosylation site	533:566	the predicted N-glycosylation site of Panx2	533:575	Our objectives were to validate the predicted N-glycosylation site of Panx2 and to study the effects of Panx2 glycosylation on localization and its capacity to interact with Panx1.
29932112	6	29	theme	N-glycosylation	862:876	arg1	Panx2					886:890	Panx2	886:890	Panx2	886:890	Our results showed that N86 is the only N-glycosylation site of Panx2.
29932112	6	29	theme	N-glycosylation	862:876	arg1	site					878:881	the only N-glycosylation site	853:881	the only N-glycosylation site of Panx2	853:890	Our results showed that N86 is the only N-glycosylation site of Panx2.
29932112	6	29	theme	N-glycosylation	862:876	arg1	N86					846:848	N86	846:848	N86	846:848	Our results showed that N86 is the only N-glycosylation site of Panx2.
29932112	2	30	theme	intermixing	281:291	arg1	N-glycosylation					221:235	N-glycosylation	221:235	N-glycosylation	221:235	We previously reported that N-glycosylation acts as a regulator of the localization and intermixing of Panx1 and Panx3, but its effects on Panx2 are currently unknown.
29932112	2	30	theme	intermixing	281:291	arg1	regulator					247:255	a regulator	245:255	a regulator of the localization and intermixing of Panx1 and Panx3	245:310	We previously reported that N-glycosylation acts as a regulator of the localization and intermixing of Panx1 and Panx3, but its effects on Panx2 are currently unknown.
29932112	5	31	used	used	685:688	arg2	We					682:683	We	682:683	We	682:683	We used site-directed mutagenesis, enzymatic de-glycosylation, cell-surface biotinylation, co-immunoprecipitation, and confocal microscopy.
29932112	9	32	theme	Panx2	1328:1332	arg1	trafficking					1313:1323	trafficking	1313:1323	trafficking	1313:1323	Our study indicates that N-glycosylation may be important for folding and trafficking of Panx2.
29932112	9	32	theme	Panx2	1328:1332	arg1	folding					1301:1307	folding	1301:1307	folding	1301:1307	Our study indicates that N-glycosylation may be important for folding and trafficking of Panx2.
29932112	10	33	theme	channel	1464:1470	arg1	function					1472:1479	their channel function	1458:1479	their channel function in cells where they are co-expressed	1458:1516	We found that the un-glycosylated forms of Panx1 and 2 can readily interact, regulating their localization and potentially their channel function in cells where they are co-expressed.
29932112	6	34	theme	only	857:860	arg1	Panx2					886:890	Panx2	886:890	Panx2	886:890	Our results showed that N86 is the only N-glycosylation site of Panx2.
29932112	6	34	theme	only	857:860	arg1	site					878:881	the only N-glycosylation site	853:881	the only N-glycosylation site of Panx2	853:890	Our results showed that N86 is the only N-glycosylation site of Panx2.
29932112	6	34	theme	only	857:860	arg1	N86					846:848	N86	846:848	N86	846:848	Our results showed that N86 is the only N-glycosylation site of Panx2.
29932112	4	35	from	effects	594:600	arg1	localization					628:639	localization	628:639	localization	628:639	Our objectives were to validate the predicted N-glycosylation site of Panx2 and to study the effects of Panx2 glycosylation on localization and its capacity to interact with Panx1.
29932112	4	35	from	effects	594:600	arg1	capacity					649:656	its capacity to interact with Panx1	645:679	its capacity to interact with Panx1	645:679	Our objectives were to validate the predicted N-glycosylation site of Panx2 and to study the effects of Panx2 glycosylation on localization and its capacity to interact with Panx1.
29932112	4	36	theme	glycosylation	611:623	arg1	effects					594:600	the effects	590:600	the effects of Panx2 glycosylation on localization and its capacity to interact with Panx1	590:679	Our objectives were to validate the predicted N-glycosylation site of Panx2 and to study the effects of Panx2 glycosylation on localization and its capacity to interact with Panx1.
29932112	8	37	theme	surface	1181:1187	arg1	trafficking					1189:1199	its cell surface trafficking	1172:1199	its cell surface trafficking	1172:1199	The Panx2 N86Q mutant is glycosylation-deficient and tends to aggregate in the ER reducing its cell surface trafficking but it can still interact with Panx1.
29932112	10	38	from	localization	1429:1440	arg1	cells					1484:1488	cells	1484:1488	cells where they are co-expressed	1484:1516	We found that the un-glycosylated forms of Panx1 and 2 can readily interact, regulating their localization and potentially their channel function in cells where they are co-expressed.
29932112	4	39	theme	Panx2	605:609	arg1	glycosylation					611:623	Panx2 glycosylation	605:623	Panx2 glycosylation	605:623	Our objectives were to validate the predicted N-glycosylation site of Panx2 and to study the effects of Panx2 glycosylation on localization and its capacity to interact with Panx1.
29932112	8	40	theme	Panx2	1085:1089	arg1	glycosylation-deficient					1106:1128	glycosylation-deficient	1106:1128	glycosylation-deficient	1106:1128	The Panx2 N86Q mutant is glycosylation-deficient and tends to aggregate in the ER reducing its cell surface trafficking but it can still interact with Panx1.
29932112	8	40	theme	Panx2	1085:1089	arg1	mutant					1096:1101	The Panx2 N86Q mutant	1081:1101	The Panx2 N86Q mutant	1081:1101	The Panx2 N86Q mutant is glycosylation-deficient and tends to aggregate in the ER reducing its cell surface trafficking but it can still interact with Panx1.
29932112	7	41	theme	limited	1007:1013	arg1	localization					1028:1039	limited cell surface localization	1007:1039	limited cell surface localization	1007:1039	Panx2 and the N86Q mutant are predominantly localized to the endoplasmic reticulum (ER) and cis-Golgi matrix with limited cell surface localization was seen only in the presence of Panx1.
29932112	3	42	theme	Panx2	371:375	arg1	intermixing					377:387	Panx2 intermixing	371:387	Panx2 intermixing	371:387	Panx1 and Panx2 intermixing can regulate channel properties, and both pannexins have been implicated in neuronal cell death after ischemia.
29932112	3	43	theme	neuronal	465:472	arg1	death					479:483	neuronal cell death	465:483	neuronal cell death after ischemia	465:498	Panx1 and Panx2 intermixing can regulate channel properties, and both pannexins have been implicated in neuronal cell death after ischemia.
29932112	7	44	theme	cell	1015:1018	arg1	localization					1028:1039	limited cell surface localization	1007:1039	limited cell surface localization	1007:1039	Panx2 and the N86Q mutant are predominantly localized to the endoplasmic reticulum (ER) and cis-Golgi matrix with limited cell surface localization was seen only in the presence of Panx1.
29932112	7	45	theme	N86Q	907:910	arg1	mutant					912:917	the N86Q mutant	903:917	the N86Q mutant	903:917	Panx2 and the N86Q mutant are predominantly localized to the endoplasmic reticulum (ER) and cis-Golgi matrix with limited cell surface localization was seen only in the presence of Panx1.
29932112	7	45	theme	N86Q	907:910	arg1	localized					937:945	localized	937:945	localized	937:945	Panx2 and the N86Q mutant are predominantly localized to the endoplasmic reticulum (ER) and cis-Golgi matrix with limited cell surface localization was seen only in the presence of Panx1.
29932112	7	46	theme	surface	1020:1026	arg1	localization					1028:1039	limited cell surface localization	1007:1039	limited cell surface localization	1007:1039	Panx2 and the N86Q mutant are predominantly localized to the endoplasmic reticulum (ER) and cis-Golgi matrix with limited cell surface localization was seen only in the presence of Panx1.
29932112	8	47	from	aggregate	1143:1151	arg1	ER					1160:1161	the ER	1156:1161	the ER	1156:1161	The Panx2 N86Q mutant is glycosylation-deficient and tends to aggregate in the ER reducing its cell surface trafficking but it can still interact with Panx1.
29932112	2	48	theme	Panx3	306:310	arg1	localization					264:275	localization	264:275	localization	264:275	We previously reported that N-glycosylation acts as a regulator of the localization and intermixing of Panx1 and Panx3, but its effects on Panx2 are currently unknown.
29932112	2	48	theme	Panx3	306:310	arg1	intermixing					281:291	intermixing	281:291	intermixing	281:291	We previously reported that N-glycosylation acts as a regulator of the localization and intermixing of Panx1 and Panx3, but its effects on Panx2 are currently unknown.
29932112	7	49	dep	reticulum	966:974	arg1	matrix					995:1000	matrix	995:1000	matrix	995:1000	Panx2 and the N86Q mutant are predominantly localized to the endoplasmic reticulum (ER) and cis-Golgi matrix with limited cell surface localization was seen only in the presence of Panx1.
29932112	1	50	dep	Pannexins	103:111	arg1	2					121:121	2	121:121	2	121:121	Pannexins (Panx1, 2, 3) are channel-forming glycoproteins expressed in mammalian tissues.
29932112	1	50	dep	Pannexins	103:111	arg1	Panx1					114:118	Panx1	114:118	Panx1	114:118	Pannexins (Panx1, 2, 3) are channel-forming glycoproteins expressed in mammalian tissues.
29932112	10	51	from	function	1472:1479	arg1	cells					1484:1488	cells	1484:1488	cells where they are co-expressed	1484:1516	We found that the un-glycosylated forms of Panx1 and 2 can readily interact, regulating their localization and potentially their channel function in cells where they are co-expressed.
18533687	1	0	theme	family	243:248	arg1	receptor					143:150	The relaxin receptor	131:150	The relaxin receptor	131:150	The relaxin receptor, RXFP1, is a member of the leucine-rich repeat-containing G-protein-coupled receptor (LGR) family.
18533687	1	0	theme	family	243:248	arg1	member					165:170	a member	163:170	a member of the leucine-rich repeat-containing G-protein-coupled receptor (LGR) family	163:248	The relaxin receptor, RXFP1, is a member of the leucine-rich repeat-containing G-protein-coupled receptor (LGR) family.
18533687	6	1	theme	site	988:991	arg1	mutants					993:999	single- or multiple-glycosylation site mutants	954:999	single- or multiple-glycosylation site mutants of FLAG-tagged human RXFP1 which were then transiently expressed in HEK-293T cells	954:1082	Site-directed mutagenesis was utilized to generate single- or multiple-glycosylation site mutants of FLAG-tagged human RXFP1 which were then transiently expressed in HEK-293T cells.
18533687	3	2	contain	contains	406:413	arg1	RXFP1					400:404	RXFP1	400:404	RXFP1	400:404	RXFP1 contains six putative Asn-linked glycosylation sites in the ectodomain at positions Asn-14, Asn-105, Asn-242, Asn-250, Asn-303, and Asn-346, which are highly conserved across species.
18533687	3	2	contain	contains	406:413	arg2	sites					453:457	six putative Asn-linked glycosylation sites	415:457	six putative Asn-linked glycosylation sites	415:457	RXFP1 contains six putative Asn-linked glycosylation sites in the ectodomain at positions Asn-14, Asn-105, Asn-242, Asn-250, Asn-303, and Asn-346, which are highly conserved across species.
18533687	4	3	theme	N-Linked	590:597	arg1	modification					651:662	the most common post-translational modification	616:662	the most common post-translational modification of G-protein-coupled receptors	616:693	N-Linked glycosylation is the most common post-translational modification of G-protein-coupled receptors, although its role in modulating receptor function differs.
18533687	4	3	theme	N-Linked	590:597	arg1	glycosylation					599:611	N-Linked glycosylation	590:611	N-Linked glycosylation	590:611	N-Linked glycosylation is the most common post-translational modification of G-protein-coupled receptors, although its role in modulating receptor function differs.
18533687	11	4	theme	LGR	1754:1756	arg1	members					1765:1771	other LGR family members	1748:1771	other LGR family members	1748:1771	Hence, as is the case for other LGR family members, N-glycosylation is essential for the transport of the receptor to the cell surface.
18533687	8	5	used	utilized	1341:1348	arg2	sites					1321:1325	the potential N-glycosylation sites	1291:1325	the potential N-glycosylation sites of RXFP1	1291:1334	All of the potential N-glycosylation sites of RXFP1 were utilized in HEK-293T cells, and importantly, disruption of glycosylation at individual or combinations of double and triple sites had little effect on relaxin binding.
18533687	8	5	used	utilized	1341:1348	arg2	RXFP1					1330:1334	RXFP1	1330:1334	RXFP1	1330:1334	All of the potential N-glycosylation sites of RXFP1 were utilized in HEK-293T cells, and importantly, disruption of glycosylation at individual or combinations of double and triple sites had little effect on relaxin binding.
18533687	8	5	used	utilized	1341:1348	arg2	All					1284:1286	All	1284:1286	All	1284:1286	All of the potential N-glycosylation sites of RXFP1 were utilized in HEK-293T cells, and importantly, disruption of glycosylation at individual or combinations of double and triple sites had little effect on relaxin binding.
18533687	4	6	theme	receptors	685:693	arg1	modification					651:662	the most common post-translational modification	616:662	the most common post-translational modification of G-protein-coupled receptors	616:693	N-Linked glycosylation is the most common post-translational modification of G-protein-coupled receptors, although its role in modulating receptor function differs.
18533687	4	6	theme	receptors	685:693	arg1	glycosylation					599:611	N-Linked glycosylation	590:611	N-Linked glycosylation	590:611	N-Linked glycosylation is the most common post-translational modification of G-protein-coupled receptors, although its role in modulating receptor function differs.
18533687	7	7	theme	activity	1262:1269	arg1	measurement					1271:1281	cAMP activity measurement	1257:1281	cAMP activity measurement	1257:1281	Glycosylation status was analyzed by immunoprecipitation and Western blot and receptor function analyzed with an anti-FLAG ELISA, (33)P-H2 relaxin competition binding, and cAMP activity measurement.
18533687	10	8	theme	intracellular	1692:1704	arg1	signaling					1711:1719	optimal intracellular cAMP signaling	1684:1719	optimal intracellular cAMP signaling	1684:1719	In particular, N-glycosylation at Asn-303 of RXFP1 was required for optimal intracellular cAMP signaling.
18533687	8	9	gly	N-glycosylation	1305:1319	arg2	sites					1321:1325	the potential N-glycosylation sites	1291:1325	the potential N-glycosylation sites of RXFP1	1291:1334	All of the potential N-glycosylation sites of RXFP1 were utilized in HEK-293T cells, and importantly, disruption of glycosylation at individual or combinations of double and triple sites had little effect on relaxin binding.
18533687	8	9	gly	N-glycosylation	1305:1319	arg1	RXFP1					1330:1334	RXFP1	1330:1334	RXFP1	1330:1334	All of the potential N-glycosylation sites of RXFP1 were utilized in HEK-293T cells, and importantly, disruption of glycosylation at individual or combinations of double and triple sites had little effect on relaxin binding.
18533687	8	9	gly	N-glycosylation	1305:1319	arg2	RXFP1					1330:1334	RXFP1	1330:1334	RXFP1	1330:1334	All of the potential N-glycosylation sites of RXFP1 were utilized in HEK-293T cells, and importantly, disruption of glycosylation at individual or combinations of double and triple sites had little effect on relaxin binding.
18533687	2	10	theme	extracellular	296:308	arg1	ectodomain					310:319	a large extracellular ectodomain	288:319	a large extracellular ectodomain containing leucine-rich repeats which contain the primary ligand binding site	288:397	These receptors are characterized by a large extracellular ectodomain containing leucine-rich repeats which contain the primary ligand binding site.
18533687	9	11	theme	sites	1548:1552	arg1	combinations					1518:1529	combinations	1518:1529	combinations of glycosylation sites	1518:1552	However, combinations of glycosylation sites were required for cell surface expression and cAMP signaling.
18533687	8	12	theme	HEK-293T	1353:1360	arg1	cells					1362:1366	HEK-293T cells	1353:1366	HEK-293T cells	1353:1366	All of the potential N-glycosylation sites of RXFP1 were utilized in HEK-293T cells, and importantly, disruption of glycosylation at individual or combinations of double and triple sites had little effect on relaxin binding.
18533687	0	13	theme	receptor	112:119	arg1	function					121:128	receptor function	112:128	receptor function	112:128	Identification of the N-linked glycosylation sites of the human relaxin receptor and effect of glycosylation on receptor function.
18533687	5	14	link	N-linked	788:795	arg1	status					811:816	the actual N-linked glycosylation status	777:816	the actual N-linked glycosylation status of RXFP1 and the functional ramifications of these post-translational modifications	777:900	We herein investigate the actual N-linked glycosylation status of RXFP1 and the functional ramifications of these post-translational modifications.
18533687	5	15	theme	modifications	888:900	arg1	ramifications					846:858	the functional ramifications	831:858	the functional ramifications of these post-translational modifications	831:900	We herein investigate the actual N-linked glycosylation status of RXFP1 and the functional ramifications of these post-translational modifications.
18533687	5	15	theme	modifications	888:900	arg1	RXFP1					821:825	RXFP1	821:825	RXFP1	821:825	We herein investigate the actual N-linked glycosylation status of RXFP1 and the functional ramifications of these post-translational modifications.
18533687	8	16	theme	potential	1295:1303	arg1	RXFP1					1330:1334	RXFP1	1330:1334	RXFP1	1330:1334	All of the potential N-glycosylation sites of RXFP1 were utilized in HEK-293T cells, and importantly, disruption of glycosylation at individual or combinations of double and triple sites had little effect on relaxin binding.
18533687	8	16	theme	potential	1295:1303	arg1	sites					1321:1325	the potential N-glycosylation sites	1291:1325	the potential N-glycosylation sites of RXFP1	1291:1334	All of the potential N-glycosylation sites of RXFP1 were utilized in HEK-293T cells, and importantly, disruption of glycosylation at individual or combinations of double and triple sites had little effect on relaxin binding.
18533687	7	17	theme	receptor	1163:1170	arg1	function					1172:1179	receptor function	1163:1179	receptor function	1163:1179	Glycosylation status was analyzed by immunoprecipitation and Western blot and receptor function analyzed with an anti-FLAG ELISA, (33)P-H2 relaxin competition binding, and cAMP activity measurement.
18533687	1	18	theme	repeat-containing	192:208	arg1	family					243:248	the leucine-rich repeat-containing G-protein-coupled receptor (LGR) family	175:248	the leucine-rich repeat-containing G-protein-coupled receptor (LGR) family	175:248	The relaxin receptor, RXFP1, is a member of the leucine-rich repeat-containing G-protein-coupled receptor (LGR) family.
18533687	9	19	gly	glycosylation	1534:1546	arg2	sites					1548:1552	glycosylation sites	1534:1552	glycosylation sites	1534:1552	However, combinations of glycosylation sites were required for cell surface expression and cAMP signaling.
18533687	3	20	link	Asn-linked	428:437	arg1	sites					453:457	six putative Asn-linked glycosylation sites	415:457	six putative Asn-linked glycosylation sites	415:457	RXFP1 contains six putative Asn-linked glycosylation sites in the ectodomain at positions Asn-14, Asn-105, Asn-242, Asn-250, Asn-303, and Asn-346, which are highly conserved across species.
18533687	6	21	theme	human	1016:1020	arg1	RXFP1					1022:1026	FLAG-tagged human RXFP1	1004:1026	FLAG-tagged human RXFP1	1004:1026	Site-directed mutagenesis was utilized to generate single- or multiple-glycosylation site mutants of FLAG-tagged human RXFP1 which were then transiently expressed in HEK-293T cells.
18533687	11	22	theme	receptor	1828:1835	arg1	transport					1811:1819	the transport	1807:1819	the transport of the receptor to the cell surface	1807:1855	Hence, as is the case for other LGR family members, N-glycosylation is essential for the transport of the receptor to the cell surface.
18533687	9	23	theme	cAMP	1600:1603	arg1	signaling					1605:1613	cAMP signaling	1600:1613	cAMP signaling	1600:1613	However, combinations of glycosylation sites were required for cell surface expression and cAMP signaling.
18533687	0	24	from	effect	85:90	arg1	function					121:128	receptor function	112:128	receptor function	112:128	Identification of the N-linked glycosylation sites of the human relaxin receptor and effect of glycosylation on receptor function.
18533687	8	25	theme	glycosylation	1400:1412	arg1	disruption					1386:1395	disruption	1386:1395	disruption of glycosylation at individual or combinations of double and triple sites	1386:1469	All of the potential N-glycosylation sites of RXFP1 were utilized in HEK-293T cells, and importantly, disruption of glycosylation at individual or combinations of double and triple sites had little effect on relaxin binding.
18533687	5	26	theme	N-linked	788:795	arg1	status					811:816	the actual N-linked glycosylation status	777:816	the actual N-linked glycosylation status of RXFP1 and the functional ramifications of these post-translational modifications	777:900	We herein investigate the actual N-linked glycosylation status of RXFP1 and the functional ramifications of these post-translational modifications.
18533687	2	27	contain	containing	321:330	arg2	repeats					345:351	leucine-rich repeats	332:351	leucine-rich repeats which contain the primary ligand binding site	332:397	These receptors are characterized by a large extracellular ectodomain containing leucine-rich repeats which contain the primary ligand binding site.
18533687	2	27	contain	containing	321:330	arg1	ectodomain					310:319	a large extracellular ectodomain	288:319	a large extracellular ectodomain containing leucine-rich repeats which contain the primary ligand binding site	288:397	These receptors are characterized by a large extracellular ectodomain containing leucine-rich repeats which contain the primary ligand binding site.
18533687	10	28	gly	N-glycosylation	1631:1645	arg1	Asn-303					1650:1656	Asn-303	1650:1656	Asn-303 of RXFP1	1650:1665	In particular, N-glycosylation at Asn-303 of RXFP1 was required for optimal intracellular cAMP signaling.
18533687	10	28	gly	N-glycosylation	1631:1645	arg1	cAMP					1706:1709	optimal intracellular cAMP signaling	1684:1719	optimal intracellular cAMP signaling	1684:1719	In particular, N-glycosylation at Asn-303 of RXFP1 was required for optimal intracellular cAMP signaling.
18533687	10	28	gly	N-glycosylation	1631:1645	arg2	Asn-303					1650:1656	Asn-303	1650:1656	Asn-303 of RXFP1	1650:1665	In particular, N-glycosylation at Asn-303 of RXFP1 was required for optimal intracellular cAMP signaling.
18533687	10	28	gly	N-glycosylation	1631:1645	arg1	particular					1619:1628	particular	1619:1628	particular	1619:1628	In particular, N-glycosylation at Asn-303 of RXFP1 was required for optimal intracellular cAMP signaling.
18533687	0	29	theme	receptor	72:79	arg1	receptor					72:79	the human relaxin receptor	54:79	the human relaxin receptor	54:79	Identification of the N-linked glycosylation sites of the human relaxin receptor and effect of glycosylation on receptor function.
18533687	0	29	theme	receptor	72:79	arg1	sites					45:49	the N-linked glycosylation sites	18:49	the N-linked glycosylation sites of the human relaxin receptor	18:79	Identification of the N-linked glycosylation sites of the human relaxin receptor and effect of glycosylation on receptor function.
18533687	12	30	theme	cAMP	2000:2003	arg1	signaling					2005:2013	subsequent cAMP signaling	1989:2013	subsequent cAMP signaling	1989:2013	Additionally, it is likely that glycosylation is also essential for the conformational changes required for G-protein coupling and subsequent cAMP signaling.
18533687	0	31	from	Identification	0:13	arg1	function					121:128	receptor function	112:128	receptor function	112:128	Identification of the N-linked glycosylation sites of the human relaxin receptor and effect of glycosylation on receptor function.
18533687	2	32	contain	contain	359:365	arg1	repeats					345:351	leucine-rich repeats	332:351	leucine-rich repeats which contain the primary ligand binding site	332:397	These receptors are characterized by a large extracellular ectodomain containing leucine-rich repeats which contain the primary ligand binding site.
18533687	2	32	contain	contain	359:365	arg2	site					394:397	the primary ligand binding site	367:397	the primary ligand binding site	367:397	These receptors are characterized by a large extracellular ectodomain containing leucine-rich repeats which contain the primary ligand binding site.
18533687	6	33	theme	HEK-293T	1069:1076	arg1	cells					1078:1082	HEK-293T cells	1069:1082	HEK-293T cells	1069:1082	Site-directed mutagenesis was utilized to generate single- or multiple-glycosylation site mutants of FLAG-tagged human RXFP1 which were then transiently expressed in HEK-293T cells.
18533687	8	34	theme	double	1447:1452	arg1	sites					1465:1469	double and triple sites	1447:1469	double and triple sites	1447:1469	All of the potential N-glycosylation sites of RXFP1 were utilized in HEK-293T cells, and importantly, disruption of glycosylation at individual or combinations of double and triple sites had little effect on relaxin binding.
18533687	0	35	theme	glycosylation	95:107	arg1	Identification					0:13	Identification	0:13	Identification of the N-linked glycosylation sites of the human relaxin receptor	0:79	Identification of the N-linked glycosylation sites of the human relaxin receptor and effect of glycosylation on receptor function.
18533687	0	35	theme	glycosylation	95:107	arg1	effect					85:90	effect	85:90	effect of glycosylation on receptor function	85:128	Identification of the N-linked glycosylation sites of the human relaxin receptor and effect of glycosylation on receptor function.
18533687	0	36	theme	sites	45:49	arg1	Identification					0:13	Identification	0:13	Identification of the N-linked glycosylation sites of the human relaxin receptor	0:79	Identification of the N-linked glycosylation sites of the human relaxin receptor and effect of glycosylation on receptor function.
18533687	0	36	theme	sites	45:49	arg1	effect					85:90	effect	85:90	effect of glycosylation on receptor function	85:128	Identification of the N-linked glycosylation sites of the human relaxin receptor and effect of glycosylation on receptor function.
18533687	8	37	from	individual	1417:1426	arg1	disruption					1386:1395	disruption	1386:1395	disruption of glycosylation at individual or combinations of double and triple sites	1386:1469	All of the potential N-glycosylation sites of RXFP1 were utilized in HEK-293T cells, and importantly, disruption of glycosylation at individual or combinations of double and triple sites had little effect on relaxin binding.
18533687	0	38	theme	relaxin	64:70	arg1	receptor					72:79	the human relaxin receptor	54:79	the human relaxin receptor	54:79	Identification of the N-linked glycosylation sites of the human relaxin receptor and effect of glycosylation on receptor function.
18533687	8	39	theme	triple	1458:1463	arg1	sites					1465:1469	double and triple sites	1447:1469	double and triple sites	1447:1469	All of the potential N-glycosylation sites of RXFP1 were utilized in HEK-293T cells, and importantly, disruption of glycosylation at individual or combinations of double and triple sites had little effect on relaxin binding.
18533687	3	40	theme	glycosylation	439:451	arg1	sites					453:457	six putative Asn-linked glycosylation sites	415:457	six putative Asn-linked glycosylation sites	415:457	RXFP1 contains six putative Asn-linked glycosylation sites in the ectodomain at positions Asn-14, Asn-105, Asn-242, Asn-250, Asn-303, and Asn-346, which are highly conserved across species.
18533687	5	41	theme	ramifications	846:858	arg1	status					811:816	the actual N-linked glycosylation status	777:816	the actual N-linked glycosylation status of RXFP1 and the functional ramifications of these post-translational modifications	777:900	We herein investigate the actual N-linked glycosylation status of RXFP1 and the functional ramifications of these post-translational modifications.
18533687	7	42	theme	Glycosylation	1085:1097	arg1	status					1099:1104	Glycosylation status	1085:1104	Glycosylation status	1085:1104	Glycosylation status was analyzed by immunoprecipitation and Western blot and receptor function analyzed with an anti-FLAG ELISA, (33)P-H2 relaxin competition binding, and cAMP activity measurement.
18533687	12	43	theme	conformational	1930:1943	arg1	changes					1945:1951	the conformational changes	1926:1951	the conformational changes required for G-protein coupling and subsequent cAMP signaling	1926:2013	Additionally, it is likely that glycosylation is also essential for the conformational changes required for G-protein coupling and subsequent cAMP signaling.
18533687	3	44	theme	putative	419:426	arg1	sites					453:457	six putative Asn-linked glycosylation sites	415:457	six putative Asn-linked glycosylation sites	415:457	RXFP1 contains six putative Asn-linked glycosylation sites in the ectodomain at positions Asn-14, Asn-105, Asn-242, Asn-250, Asn-303, and Asn-346, which are highly conserved across species.
18533687	5	45	theme	RXFP1	821:825	arg1	status					811:816	the actual N-linked glycosylation status	777:816	the actual N-linked glycosylation status of RXFP1 and the functional ramifications of these post-translational modifications	777:900	We herein investigate the actual N-linked glycosylation status of RXFP1 and the functional ramifications of these post-translational modifications.
18533687	0	46	theme	glycosylation	31:43	arg1	receptor					72:79	the human relaxin receptor	54:79	the human relaxin receptor	54:79	Identification of the N-linked glycosylation sites of the human relaxin receptor and effect of glycosylation on receptor function.
18533687	0	46	theme	glycosylation	31:43	arg1	sites					45:49	the N-linked glycosylation sites	18:49	the N-linked glycosylation sites of the human relaxin receptor	18:79	Identification of the N-linked glycosylation sites of the human relaxin receptor and effect of glycosylation on receptor function.
18533687	10	47	from	Asn-303	1650:1656	arg1	N-glycosylation					1631:1645	N-glycosylation	1631:1645	N-glycosylation at Asn-303 of RXFP1	1631:1665	In particular, N-glycosylation at Asn-303 of RXFP1 was required for optimal intracellular cAMP signaling.
18533687	0	48	theme	human	58:62	arg1	receptor					72:79	the human relaxin receptor	54:79	the human relaxin receptor	54:79	Identification of the N-linked glycosylation sites of the human relaxin receptor and effect of glycosylation on receptor function.
18533687	8	49	theme	relaxin	1492:1498	arg1	binding					1500:1506	relaxin binding	1492:1506	relaxin binding	1492:1506	All of the potential N-glycosylation sites of RXFP1 were utilized in HEK-293T cells, and importantly, disruption of glycosylation at individual or combinations of double and triple sites had little effect on relaxin binding.
18533687	7	50	theme	relaxin	1224:1230	arg1	binding					1244:1250	(33)P-H2 relaxin competition binding	1215:1250	(33)P-H2 relaxin competition binding	1215:1250	Glycosylation status was analyzed by immunoprecipitation and Western blot and receptor function analyzed with an anti-FLAG ELISA, (33)P-H2 relaxin competition binding, and cAMP activity measurement.
18533687	6	51	theme	Site-directed	903:915	arg1	mutagenesis					917:927	Site-directed mutagenesis	903:927	Site-directed mutagenesis	903:927	Site-directed mutagenesis was utilized to generate single- or multiple-glycosylation site mutants of FLAG-tagged human RXFP1 which were then transiently expressed in HEK-293T cells.
18533687	2	52	theme	leucine-rich	332:343	arg1	repeats					345:351	leucine-rich repeats	332:351	leucine-rich repeats which contain the primary ligand binding site	332:397	These receptors are characterized by a large extracellular ectodomain containing leucine-rich repeats which contain the primary ligand binding site.
18533687	1	53	theme	G-protein-coupled	210:226	arg1	family					243:248	the leucine-rich repeat-containing G-protein-coupled receptor (LGR) family	175:248	the leucine-rich repeat-containing G-protein-coupled receptor (LGR) family	175:248	The relaxin receptor, RXFP1, is a member of the leucine-rich repeat-containing G-protein-coupled receptor (LGR) family.
18533687	3	54	from	sites	453:457	arg1	positions					480:488	positions Asn-14, Asn-105, Asn-242, Asn-250, Asn-303, and Asn-346	480:544	positions Asn-14, Asn-105, Asn-242, Asn-250, Asn-303, and Asn-346	480:544	RXFP1 contains six putative Asn-linked glycosylation sites in the ectodomain at positions Asn-14, Asn-105, Asn-242, Asn-250, Asn-303, and Asn-346, which are highly conserved across species.
18533687	3	54	from	sites	453:457	arg1	ectodomain					466:475	the ectodomain	462:475	the ectodomain at positions Asn-14, Asn-105, Asn-242, Asn-250, Asn-303, and Asn-346	462:544	RXFP1 contains six putative Asn-linked glycosylation sites in the ectodomain at positions Asn-14, Asn-105, Asn-242, Asn-250, Asn-303, and Asn-346, which are highly conserved across species.
18533687	2	55	theme	ligand	379:384	arg1	site					394:397	the primary ligand binding site	367:397	the primary ligand binding site	367:397	These receptors are characterized by a large extracellular ectodomain containing leucine-rich repeats which contain the primary ligand binding site.
18533687	6	56	used	utilized	933:940	arg2	mutagenesis					917:927	Site-directed mutagenesis	903:927	Site-directed mutagenesis	903:927	Site-directed mutagenesis was utilized to generate single- or multiple-glycosylation site mutants of FLAG-tagged human RXFP1 which were then transiently expressed in HEK-293T cells.
18533687	6	57	theme	FLAG-tagged	1004:1014	arg1	RXFP1					1022:1026	FLAG-tagged human RXFP1	1004:1026	FLAG-tagged human RXFP1	1004:1026	Site-directed mutagenesis was utilized to generate single- or multiple-glycosylation site mutants of FLAG-tagged human RXFP1 which were then transiently expressed in HEK-293T cells.
18533687	7	58	theme	33	1216:1217	arg1	P-H2					1219:1222	P-H2	1219:1222	P-H2	1219:1222	Glycosylation status was analyzed by immunoprecipitation and Western blot and receptor function analyzed with an anti-FLAG ELISA, (33)P-H2 relaxin competition binding, and cAMP activity measurement.
18533687	0	59	link	N-linked	22:29	arg1	receptor					72:79	the human relaxin receptor	54:79	the human relaxin receptor	54:79	Identification of the N-linked glycosylation sites of the human relaxin receptor and effect of glycosylation on receptor function.
18533687	0	59	link	N-linked	22:29	arg1	sites					45:49	the N-linked glycosylation sites	18:49	the N-linked glycosylation sites of the human relaxin receptor	18:79	Identification of the N-linked glycosylation sites of the human relaxin receptor and effect of glycosylation on receptor function.
18533687	6	60	theme	multiple-glycosylation	965:986	arg1	mutants					993:999	single- or multiple-glycosylation site mutants	954:999	single- or multiple-glycosylation site mutants of FLAG-tagged human RXFP1 which were then transiently expressed in HEK-293T cells	954:1082	Site-directed mutagenesis was utilized to generate single- or multiple-glycosylation site mutants of FLAG-tagged human RXFP1 which were then transiently expressed in HEK-293T cells.
18533687	10	61	theme	RXFP1	1661:1665	arg1	Asn-303					1650:1656	Asn-303	1650:1656	Asn-303 of RXFP1	1650:1665	In particular, N-glycosylation at Asn-303 of RXFP1 was required for optimal intracellular cAMP signaling.
18533687	11	62	theme	family	1758:1763	arg1	members					1765:1771	other LGR family members	1748:1771	other LGR family members	1748:1771	Hence, as is the case for other LGR family members, N-glycosylation is essential for the transport of the receptor to the cell surface.
18533687	7	63	theme	anti-FLAG	1198:1206	arg1	ELISA					1208:1212	an anti-FLAG ELISA	1195:1212	an anti-FLAG ELISA	1195:1212	Glycosylation status was analyzed by immunoprecipitation and Western blot and receptor function analyzed with an anti-FLAG ELISA, (33)P-H2 relaxin competition binding, and cAMP activity measurement.
18533687	6	64	theme	single-	954:960	arg1	mutants					993:999	single- or multiple-glycosylation site mutants	954:999	single- or multiple-glycosylation site mutants of FLAG-tagged human RXFP1 which were then transiently expressed in HEK-293T cells	954:1082	Site-directed mutagenesis was utilized to generate single- or multiple-glycosylation site mutants of FLAG-tagged human RXFP1 which were then transiently expressed in HEK-293T cells.
18533687	4	65	theme	G-protein-coupled	667:683	arg1	receptors					685:693	G-protein-coupled receptors	667:693	G-protein-coupled receptors	667:693	N-Linked glycosylation is the most common post-translational modification of G-protein-coupled receptors, although its role in modulating receptor function differs.
18533687	10	66	theme	cAMP	1706:1709	arg1	signaling					1711:1719	optimal intracellular cAMP signaling	1684:1719	optimal intracellular cAMP signaling	1684:1719	In particular, N-glycosylation at Asn-303 of RXFP1 was required for optimal intracellular cAMP signaling.
18533687	11	67	theme	other	1748:1752	arg1	members					1765:1771	other LGR family members	1748:1771	other LGR family members	1748:1771	Hence, as is the case for other LGR family members, N-glycosylation is essential for the transport of the receptor to the cell surface.
18533687	9	68	theme	glycosylation	1534:1546	arg1	sites					1548:1552	glycosylation sites	1534:1552	glycosylation sites	1534:1552	However, combinations of glycosylation sites were required for cell surface expression and cAMP signaling.
18533687	10	69	theme	optimal	1684:1690	arg1	signaling					1711:1719	optimal intracellular cAMP signaling	1684:1719	optimal intracellular cAMP signaling	1684:1719	In particular, N-glycosylation at Asn-303 of RXFP1 was required for optimal intracellular cAMP signaling.
18533687	2	70	theme	large	290:294	arg1	ectodomain					310:319	a large extracellular ectodomain	288:319	a large extracellular ectodomain containing leucine-rich repeats which contain the primary ligand binding site	288:397	These receptors are characterized by a large extracellular ectodomain containing leucine-rich repeats which contain the primary ligand binding site.
18533687	5	71	theme	post-translational	869:886	arg1	modifications					888:900	these post-translational modifications	863:900	these post-translational modifications	863:900	We herein investigate the actual N-linked glycosylation status of RXFP1 and the functional ramifications of these post-translational modifications.
18533687	4	72	theme	common	625:630	arg1	modification					651:662	the most common post-translational modification	616:662	the most common post-translational modification of G-protein-coupled receptors	616:693	N-Linked glycosylation is the most common post-translational modification of G-protein-coupled receptors, although its role in modulating receptor function differs.
18533687	4	72	theme	common	625:630	arg1	glycosylation					599:611	N-Linked glycosylation	590:611	N-Linked glycosylation	590:611	N-Linked glycosylation is the most common post-translational modification of G-protein-coupled receptors, although its role in modulating receptor function differs.
18533687	1	73	theme	leucine-rich	179:190	arg1	family					243:248	the leucine-rich repeat-containing G-protein-coupled receptor (LGR) family	175:248	the leucine-rich repeat-containing G-protein-coupled receptor (LGR) family	175:248	The relaxin receptor, RXFP1, is a member of the leucine-rich repeat-containing G-protein-coupled receptor (LGR) family.
18533687	7	74	theme	Western	1146:1152	arg1	blot					1154:1157	Western blot	1146:1157	Western blot	1146:1157	Glycosylation status was analyzed by immunoprecipitation and Western blot and receptor function analyzed with an anti-FLAG ELISA, (33)P-H2 relaxin competition binding, and cAMP activity measurement.
18533687	9	75	theme	surface	1577:1583	arg1	expression					1585:1594	cell surface expression	1572:1594	cell surface expression	1572:1594	However, combinations of glycosylation sites were required for cell surface expression and cAMP signaling.
18533687	8	76	theme	N-glycosylation	1305:1319	arg1	RXFP1					1330:1334	RXFP1	1330:1334	RXFP1	1330:1334	All of the potential N-glycosylation sites of RXFP1 were utilized in HEK-293T cells, and importantly, disruption of glycosylation at individual or combinations of double and triple sites had little effect on relaxin binding.
18533687	8	76	theme	N-glycosylation	1305:1319	arg1	sites					1321:1325	the potential N-glycosylation sites	1291:1325	the potential N-glycosylation sites of RXFP1	1291:1334	All of the potential N-glycosylation sites of RXFP1 were utilized in HEK-293T cells, and importantly, disruption of glycosylation at individual or combinations of double and triple sites had little effect on relaxin binding.
18533687	6	77	theme	RXFP1	1022:1026	arg1	mutants					993:999	single- or multiple-glycosylation site mutants	954:999	single- or multiple-glycosylation site mutants of FLAG-tagged human RXFP1 which were then transiently expressed in HEK-293T cells	954:1082	Site-directed mutagenesis was utilized to generate single- or multiple-glycosylation site mutants of FLAG-tagged human RXFP1 which were then transiently expressed in HEK-293T cells.
18533687	4	78	theme	receptor	728:735	arg1	function					737:744	receptor function	728:744	receptor function	728:744	N-Linked glycosylation is the most common post-translational modification of G-protein-coupled receptors, although its role in modulating receptor function differs.
18533687	5	79	theme	actual	781:786	arg1	status					811:816	the actual N-linked glycosylation status	777:816	the actual N-linked glycosylation status of RXFP1 and the functional ramifications of these post-translational modifications	777:900	We herein investigate the actual N-linked glycosylation status of RXFP1 and the functional ramifications of these post-translational modifications.
18533687	4	80	theme	post-translational	632:649	arg1	modification					651:662	the most common post-translational modification	616:662	the most common post-translational modification of G-protein-coupled receptors	616:693	N-Linked glycosylation is the most common post-translational modification of G-protein-coupled receptors, although its role in modulating receptor function differs.
18533687	4	80	theme	post-translational	632:649	arg1	glycosylation					599:611	N-Linked glycosylation	590:611	N-Linked glycosylation	590:611	N-Linked glycosylation is the most common post-translational modification of G-protein-coupled receptors, although its role in modulating receptor function differs.
18533687	1	81	theme	relaxin	135:141	arg1	receptor					143:150	The relaxin receptor	131:150	The relaxin receptor	131:150	The relaxin receptor, RXFP1, is a member of the leucine-rich repeat-containing G-protein-coupled receptor (LGR) family.
18533687	1	81	theme	relaxin	135:141	arg1	member					165:170	a member	163:170	a member of the leucine-rich repeat-containing G-protein-coupled receptor (LGR) family	163:248	The relaxin receptor, RXFP1, is a member of the leucine-rich repeat-containing G-protein-coupled receptor (LGR) family.
18533687	1	81	theme	relaxin	135:141	arg1	RXFP1					153:157	RXFP1	153:157	RXFP1	153:157	The relaxin receptor, RXFP1, is a member of the leucine-rich repeat-containing G-protein-coupled receptor (LGR) family.
18533687	8	82	contain	had	1471:1473	arg1	disruption					1386:1395	disruption	1386:1395	disruption of glycosylation at individual or combinations of double and triple sites	1386:1469	All of the potential N-glycosylation sites of RXFP1 were utilized in HEK-293T cells, and importantly, disruption of glycosylation at individual or combinations of double and triple sites had little effect on relaxin binding.
18533687	8	82	contain	had	1471:1473	arg2	effect					1482:1487	little effect	1475:1487	little effect	1475:1487	All of the potential N-glycosylation sites of RXFP1 were utilized in HEK-293T cells, and importantly, disruption of glycosylation at individual or combinations of double and triple sites had little effect on relaxin binding.
18533687	11	83	gly	N-glycosylation	1774:1788	arg1	receptor					1828:1835	the receptor	1824:1835	the receptor	1824:1835	Hence, as is the case for other LGR family members, N-glycosylation is essential for the transport of the receptor to the cell surface.
18533687	5	84	theme	glycosylation	797:809	arg1	status					811:816	the actual N-linked glycosylation status	777:816	the actual N-linked glycosylation status of RXFP1 and the functional ramifications of these post-translational modifications	777:900	We herein investigate the actual N-linked glycosylation status of RXFP1 and the functional ramifications of these post-translational modifications.
18533687	11	85	theme	cell	1844:1847	arg1	surface					1849:1855	the cell surface	1840:1855	the cell surface	1840:1855	Hence, as is the case for other LGR family members, N-glycosylation is essential for the transport of the receptor to the cell surface.
18533687	5	86	gly	glycosylation	797:809	arg1	ramifications					846:858	the functional ramifications	831:858	the functional ramifications of these post-translational modifications	831:900	We herein investigate the actual N-linked glycosylation status of RXFP1 and the functional ramifications of these post-translational modifications.
18533687	5	86	gly	glycosylation	797:809	arg1	RXFP1					821:825	RXFP1	821:825	RXFP1	821:825	We herein investigate the actual N-linked glycosylation status of RXFP1 and the functional ramifications of these post-translational modifications.
18533687	5	87	theme	functional	835:844	arg1	ramifications					846:858	the functional ramifications	831:858	the functional ramifications of these post-translational modifications	831:900	We herein investigate the actual N-linked glycosylation status of RXFP1 and the functional ramifications of these post-translational modifications.
18533687	12	88	theme	subsequent	1989:1998	arg1	signaling					2005:2013	subsequent cAMP signaling	1989:2013	subsequent cAMP signaling	1989:2013	Additionally, it is likely that glycosylation is also essential for the conformational changes required for G-protein coupling and subsequent cAMP signaling.
18533687	8	89	theme	RXFP1	1330:1334	arg1	RXFP1					1330:1334	RXFP1	1330:1334	RXFP1	1330:1334	All of the potential N-glycosylation sites of RXFP1 were utilized in HEK-293T cells, and importantly, disruption of glycosylation at individual or combinations of double and triple sites had little effect on relaxin binding.
18533687	8	89	theme	RXFP1	1330:1334	arg1	sites					1321:1325	the potential N-glycosylation sites	1291:1325	the potential N-glycosylation sites of RXFP1	1291:1334	All of the potential N-glycosylation sites of RXFP1 were utilized in HEK-293T cells, and importantly, disruption of glycosylation at individual or combinations of double and triple sites had little effect on relaxin binding.
18533687	2	90	theme	binding	386:392	arg1	site					394:397	the primary ligand binding site	367:397	the primary ligand binding site	367:397	These receptors are characterized by a large extracellular ectodomain containing leucine-rich repeats which contain the primary ligand binding site.
18533687	0	91	theme	N-linked	22:29	arg1	receptor					72:79	the human relaxin receptor	54:79	the human relaxin receptor	54:79	Identification of the N-linked glycosylation sites of the human relaxin receptor and effect of glycosylation on receptor function.
18533687	0	91	theme	N-linked	22:29	arg1	sites					45:49	the N-linked glycosylation sites	18:49	the N-linked glycosylation sites of the human relaxin receptor	18:79	Identification of the N-linked glycosylation sites of the human relaxin receptor and effect of glycosylation on receptor function.
18533687	0	92	gly	glycosylation	95:107	arg1	receptor					112:119	receptor function	112:128	receptor function	112:128	Identification of the N-linked glycosylation sites of the human relaxin receptor and effect of glycosylation on receptor function.
18533687	8	93	theme	sites	1465:1469	arg1	individual					1417:1426	individual	1417:1426	individual	1417:1426	All of the potential N-glycosylation sites of RXFP1 were utilized in HEK-293T cells, and importantly, disruption of glycosylation at individual or combinations of double and triple sites had little effect on relaxin binding.
18533687	7	94	theme	competition	1232:1242	arg1	binding					1244:1250	(33)P-H2 relaxin competition binding	1215:1250	(33)P-H2 relaxin competition binding	1215:1250	Glycosylation status was analyzed by immunoprecipitation and Western blot and receptor function analyzed with an anti-FLAG ELISA, (33)P-H2 relaxin competition binding, and cAMP activity measurement.
18533687	3	95	theme	Asn-linked	428:437	arg1	sites					453:457	six putative Asn-linked glycosylation sites	415:457	six putative Asn-linked glycosylation sites	415:457	RXFP1 contains six putative Asn-linked glycosylation sites in the ectodomain at positions Asn-14, Asn-105, Asn-242, Asn-250, Asn-303, and Asn-346, which are highly conserved across species.
18533687	8	96	theme	little	1475:1480	arg1	effect					1482:1487	little effect	1475:1487	little effect	1475:1487	All of the potential N-glycosylation sites of RXFP1 were utilized in HEK-293T cells, and importantly, disruption of glycosylation at individual or combinations of double and triple sites had little effect on relaxin binding.
18533687	7	97	theme	P-H2	1219:1222	arg1	binding					1244:1250	(33)P-H2 relaxin competition binding	1215:1250	(33)P-H2 relaxin competition binding	1215:1250	Glycosylation status was analyzed by immunoprecipitation and Western blot and receptor function analyzed with an anti-FLAG ELISA, (33)P-H2 relaxin competition binding, and cAMP activity measurement.
18533687	12	98	theme	G-protein	1966:1974	arg1	coupling					1976:1983	G-protein coupling	1966:1983	G-protein coupling	1966:1983	Additionally, it is likely that glycosylation is also essential for the conformational changes required for G-protein coupling and subsequent cAMP signaling.
18533687	3	99	from	positions	480:488	arg1	sites					453:457	six putative Asn-linked glycosylation sites	415:457	six putative Asn-linked glycosylation sites	415:457	RXFP1 contains six putative Asn-linked glycosylation sites in the ectodomain at positions Asn-14, Asn-105, Asn-242, Asn-250, Asn-303, and Asn-346, which are highly conserved across species.
18533687	3	99	from	positions	480:488	arg1	ectodomain					466:475	the ectodomain	462:475	the ectodomain at positions Asn-14, Asn-105, Asn-242, Asn-250, Asn-303, and Asn-346	462:544	RXFP1 contains six putative Asn-linked glycosylation sites in the ectodomain at positions Asn-14, Asn-105, Asn-242, Asn-250, Asn-303, and Asn-346, which are highly conserved across species.
18533687	0	100	gly	glycosylation	31:43	arg1	receptor					72:79	the human relaxin receptor	54:79	the human relaxin receptor	54:79	Identification of the N-linked glycosylation sites of the human relaxin receptor and effect of glycosylation on receptor function.
18533687	0	100	gly	glycosylation	31:43	arg2	sites					45:49	the N-linked glycosylation sites	18:49	the N-linked glycosylation sites of the human relaxin receptor	18:79	Identification of the N-linked glycosylation sites of the human relaxin receptor and effect of glycosylation on receptor function.
18533687	0	100	gly	glycosylation	31:43	arg2	receptor					72:79	the human relaxin receptor	54:79	the human relaxin receptor	54:79	Identification of the N-linked glycosylation sites of the human relaxin receptor and effect of glycosylation on receptor function.
18533687	2	101	theme	primary	371:377	arg1	site					394:397	the primary ligand binding site	367:397	the primary ligand binding site	367:397	These receptors are characterized by a large extracellular ectodomain containing leucine-rich repeats which contain the primary ligand binding site.
18533687	8	102	from	combinations	1431:1442	arg1	disruption					1386:1395	disruption	1386:1395	disruption of glycosylation at individual or combinations of double and triple sites	1386:1469	All of the potential N-glycosylation sites of RXFP1 were utilized in HEK-293T cells, and importantly, disruption of glycosylation at individual or combinations of double and triple sites had little effect on relaxin binding.
18533687	1	103	theme	receptor	228:235	arg1	family					243:248	the leucine-rich repeat-containing G-protein-coupled receptor (LGR) family	175:248	the leucine-rich repeat-containing G-protein-coupled receptor (LGR) family	175:248	The relaxin receptor, RXFP1, is a member of the leucine-rich repeat-containing G-protein-coupled receptor (LGR) family.
18533687	9	104	theme	cell	1572:1575	arg1	expression					1585:1594	cell surface expression	1572:1594	cell surface expression	1572:1594	However, combinations of glycosylation sites were required for cell surface expression and cAMP signaling.
18533687	3	105	gly	glycosylation	439:451	arg2	six					415:417	six	415:417	six	415:417	RXFP1 contains six putative Asn-linked glycosylation sites in the ectodomain at positions Asn-14, Asn-105, Asn-242, Asn-250, Asn-303, and Asn-346, which are highly conserved across species.
18533687	3	105	gly	glycosylation	439:451	arg2	positions					480:488	positions Asn-14, Asn-105, Asn-242, Asn-250, Asn-303, and Asn-346	480:544	positions Asn-14, Asn-105, Asn-242, Asn-250, Asn-303, and Asn-346	480:544	RXFP1 contains six putative Asn-linked glycosylation sites in the ectodomain at positions Asn-14, Asn-105, Asn-242, Asn-250, Asn-303, and Asn-346, which are highly conserved across species.
18533687	3	105	gly	glycosylation	439:451	arg2	sites					453:457	six putative Asn-linked glycosylation sites	415:457	six putative Asn-linked glycosylation sites	415:457	RXFP1 contains six putative Asn-linked glycosylation sites in the ectodomain at positions Asn-14, Asn-105, Asn-242, Asn-250, Asn-303, and Asn-346, which are highly conserved across species.
18533687	7	106	theme	cAMP	1257:1260	arg1	measurement					1271:1281	cAMP activity measurement	1257:1281	cAMP activity measurement	1257:1281	Glycosylation status was analyzed by immunoprecipitation and Western blot and receptor function analyzed with an anti-FLAG ELISA, (33)P-H2 relaxin competition binding, and cAMP activity measurement.
18533687	1	107	theme	LGR	238:240	arg1	family					243:248	the leucine-rich repeat-containing G-protein-coupled receptor (LGR) family	175:248	the leucine-rich repeat-containing G-protein-coupled receptor (LGR) family	175:248	The relaxin receptor, RXFP1, is a member of the leucine-rich repeat-containing G-protein-coupled receptor (LGR) family.
26853155	3	0	theme	non-synonymous	781:794	arg1	SNPs					796:799	another 10 non-synonymous SNPs	770:799	another 10 non-synonymous SNPs located within important functional domains	770:843	We constructed expression plasmids of wild-type and 21 single-amino-acid substitution mutants of syncytin-2, including 10 N-glycosylation sites individually silenced by mutagenizing N to Q, 1 naturally occurring single-nucleotide polymorphism (SNP) N118S that introduced an N-glycosylation site, and another 10 non-synonymous SNPs located within important functional domains.
26853155	10	1	theme	fusogenic	2051:2059	arg1	function					2061:2068	the fusogenic function	2047:2068	the fusogenic function of syncytin-2	2047:2082	Taken together, our results suggest that N-glycans at residues 133, 312, 332 and 443 of syncytin-2 are required for optimal fusion induction, and that SNPs C46R, N118S, T367M, R417H, V483I and T522M can alter the fusogenic function of syncytin-2.
26853155	2	2	theme	important	397:405	arg1	player					407:412	the most important player	388:412	the most important player in mediating trophoblast cell-cell fusion as a fusogen	388:467	The human endogenous retrovirus envelope glycoprotein syncytin-2 is the most important player in mediating trophoblast cell-cell fusion as a fusogen.
26853155	2	2	theme	important	397:405	arg1	syncytin-2					374:383	The human endogenous retrovirus envelope glycoprotein syncytin-2	320:383	The human endogenous retrovirus envelope glycoprotein syncytin-2	320:383	The human endogenous retrovirus envelope glycoprotein syncytin-2 is the most important player in mediating trophoblast cell-cell fusion as a fusogen.
26853155	5	3	theme	cytoplasmic	1230:1240	arg1	domain					1242:1247	the cytoplasmic domain	1226:1247	the cytoplasmic domain	1226:1247	Of the 21 mutants, N133Q, N312Q, N443Q, C46R (in the CXXC motif) and R417H (in the heptad repeat region and immunosuppressive domain) lost their fusogenicity, whereas N332Q, N118S, T367M (in the fusion peptide), V483I (in the transmembrane domain) and T522M (in the cytoplasmic domain) enhanced the fusogenic activity.
26853155	4	4	contain	had	916:918	arg1	mutants					908:914	the mutants	904:914	the mutants	904:914	We observed that syncytin-2 was highly fusogenic and that the mutants had different capacities in merging 293T cells.
26853155	4	4	contain	had	916:918	arg2	capacities					930:939	different capacities	920:939	different capacities	920:939	We observed that syncytin-2 was highly fusogenic and that the mutants had different capacities in merging 293T cells.
26853155	6	5	gly	glycosylated	1368:1379	arg1	N133					1303:1306	N133	1303:1306	N133	1303:1306	We also proved that N133, N146, N177, N220, N241, N247, N312, N332 and N443 were all glycosylated in 293T cells.
26853155	6	5	gly	glycosylated	1368:1379	arg1	N332					1345:1348	N332	1345:1348	N332	1345:1348	We also proved that N133, N146, N177, N220, N241, N247, N312, N332 and N443 were all glycosylated in 293T cells.
26853155	6	5	gly	glycosylated	1368:1379	arg2	N177					1315:1318	N177	1315:1318	N177	1315:1318	We also proved that N133, N146, N177, N220, N241, N247, N312, N332 and N443 were all glycosylated in 293T cells.
26853155	6	5	gly	glycosylated	1368:1379	arg1	N146					1309:1312	N146	1309:1312	N146	1309:1312	We also proved that N133, N146, N177, N220, N241, N247, N312, N332 and N443 were all glycosylated in 293T cells.
26853155	6	5	gly	glycosylated	1368:1379	arg1	N241					1327:1330	N241	1327:1330	N241	1327:1330	We also proved that N133, N146, N177, N220, N241, N247, N312, N332 and N443 were all glycosylated in 293T cells.
26853155	6	5	gly	glycosylated	1368:1379	arg2	N133					1303:1306	N133	1303:1306	N133	1303:1306	We also proved that N133, N146, N177, N220, N241, N247, N312, N332 and N443 were all glycosylated in 293T cells.
26853155	6	5	gly	glycosylated	1368:1379	arg1	cells					1389:1393	293T cells	1384:1393	293T cells	1384:1393	We also proved that N133, N146, N177, N220, N241, N247, N312, N332 and N443 were all glycosylated in 293T cells.
26853155	6	5	gly	glycosylated	1368:1379	arg2	N312					1339:1342	N312	1339:1342	N312	1339:1342	We also proved that N133, N146, N177, N220, N241, N247, N312, N332 and N443 were all glycosylated in 293T cells.
26853155	6	5	gly	glycosylated	1368:1379	arg2	N146					1309:1312	N146	1309:1312	N146	1309:1312	We also proved that N133, N146, N177, N220, N241, N247, N312, N332 and N443 were all glycosylated in 293T cells.
26853155	6	5	gly	glycosylated	1368:1379	arg1	N443					1354:1357	N443	1354:1357	N443	1354:1357	We also proved that N133, N146, N177, N220, N241, N247, N312, N332 and N443 were all glycosylated in 293T cells.
26853155	6	5	gly	glycosylated	1368:1379	arg2	N241					1327:1330	N241	1327:1330	N241	1327:1330	We also proved that N133, N146, N177, N220, N241, N247, N312, N332 and N443 were all glycosylated in 293T cells.
26853155	6	5	gly	glycosylated	1368:1379	arg2	N332					1345:1348	N332	1345:1348	N332	1345:1348	We also proved that N133, N146, N177, N220, N241, N247, N312, N332 and N443 were all glycosylated in 293T cells.
26853155	6	5	gly	glycosylated	1368:1379	arg1	N177					1315:1318	N177	1315:1318	N177	1315:1318	We also proved that N133, N146, N177, N220, N241, N247, N312, N332 and N443 were all glycosylated in 293T cells.
26853155	6	5	gly	glycosylated	1368:1379	arg2	N443					1354:1357	N443	1354:1357	N443	1354:1357	We also proved that N133, N146, N177, N220, N241, N247, N312, N332 and N443 were all glycosylated in 293T cells.
26853155	6	5	gly	glycosylated	1368:1379	arg1	N312					1339:1342	N312	1339:1342	N312	1339:1342	We also proved that N133, N146, N177, N220, N241, N247, N312, N332 and N443 were all glycosylated in 293T cells.
26853155	10	6	dep	SNPs	1989:1992	arg1	SNPs					1989:1992	SNPs C46R, N118S, T367M, R417H, V483I and T522M	1989:2035	SNPs C46R, N118S, T367M, R417H, V483I and T522M	1989:2035	Taken together, our results suggest that N-glycans at residues 133, 312, 332 and 443 of syncytin-2 are required for optimal fusion induction, and that SNPs C46R, N118S, T367M, R417H, V483I and T522M can alter the fusogenic function of syncytin-2.
26853155	10	6	dep	SNPs	1989:1992	arg1	N118S					2000:2004	N118S	2000:2004	N118S	2000:2004	Taken together, our results suggest that N-glycans at residues 133, 312, 332 and 443 of syncytin-2 are required for optimal fusion induction, and that SNPs C46R, N118S, T367M, R417H, V483I and T522M can alter the fusogenic function of syncytin-2.
26853155	10	6	dep	SNPs	1989:1992	arg1	V483I					2021:2025	V483I	2021:2025	V483I	2021:2025	Taken together, our results suggest that N-glycans at residues 133, 312, 332 and 443 of syncytin-2 are required for optimal fusion induction, and that SNPs C46R, N118S, T367M, R417H, V483I and T522M can alter the fusogenic function of syncytin-2.
26853155	10	6	dep	SNPs	1989:1992	arg1	T522M					2031:2035	T522M	2031:2035	T522M	2031:2035	Taken together, our results suggest that N-glycans at residues 133, 312, 332 and 443 of syncytin-2 are required for optimal fusion induction, and that SNPs C46R, N118S, T367M, R417H, V483I and T522M can alter the fusogenic function of syncytin-2.
26853155	10	6	dep	SNPs	1989:1992	arg1	R417H					2014:2018	R417H	2014:2018	R417H	2014:2018	Taken together, our results suggest that N-glycans at residues 133, 312, 332 and 443 of syncytin-2 are required for optimal fusion induction, and that SNPs C46R, N118S, T367M, R417H, V483I and T522M can alter the fusogenic function of syncytin-2.
26853155	10	7	from	residues	1892:1899	arg1	N-glycans					1879:1887	N-glycans	1879:1887	N-glycans at residues 133, 312, 332 and 443 of syncytin-2	1879:1935	Taken together, our results suggest that N-glycans at residues 133, 312, 332 and 443 of syncytin-2 are required for optimal fusion induction, and that SNPs C46R, N118S, T367M, R417H, V483I and T522M can alter the fusogenic function of syncytin-2.
26853155	5	8	theme	transmembrane	1190:1202	arg1	domain					1204:1209	the transmembrane domain	1186:1209	the transmembrane domain	1186:1209	Of the 21 mutants, N133Q, N312Q, N443Q, C46R (in the CXXC motif) and R417H (in the heptad repeat region and immunosuppressive domain) lost their fusogenicity, whereas N332Q, N118S, T367M (in the fusion peptide), V483I (in the transmembrane domain) and T522M (in the cytoplasmic domain) enhanced the fusogenic activity.
26853155	0	9	from	Effects	0:6	arg1	function					123:130	the fusogenic function	109:130	the fusogenic function of human syncytin-2	109:150	Effects of individually silenced N-glycosylation sites and non-synonymous single-nucleotide polymorphisms on the fusogenic function of human syncytin-2.
26853155	5	10	theme	repeat	1054:1059	arg1	region					1061:1066	the heptad repeat region	1043:1066	the heptad repeat region	1043:1066	Of the 21 mutants, N133Q, N312Q, N443Q, C46R (in the CXXC motif) and R417H (in the heptad repeat region and immunosuppressive domain) lost their fusogenicity, whereas N332Q, N118S, T367M (in the fusion peptide), V483I (in the transmembrane domain) and T522M (in the cytoplasmic domain) enhanced the fusogenic activity.
26853155	3	11	gly	10 N-glycosylation	589:606	arg2	sites					608:612	10 N-glycosylation sites	589:612	10 N-glycosylation sites individually silenced by mutagenizing N to Q, 1 naturally occurring single-nucleotide polymorphism (SNP) N118S that introduced an N-glycosylation site, and another 10 non-synonymous SNPs located within important functional domains	589:843	We constructed expression plasmids of wild-type and 21 single-amino-acid substitution mutants of syncytin-2, including 10 N-glycosylation sites individually silenced by mutagenizing N to Q, 1 naturally occurring single-nucleotide polymorphism (SNP) N118S that introduced an N-glycosylation site, and another 10 non-synonymous SNPs located within important functional domains.
26853155	0	12	theme	fusogenic	113:121	arg1	function					123:130	the fusogenic function	109:130	the fusogenic function of human syncytin-2	109:150	Effects of individually silenced N-glycosylation sites and non-synonymous single-nucleotide polymorphisms on the fusogenic function of human syncytin-2.
26853155	5	13	theme	CXXC	1017:1020	arg1	motif					1022:1026	the CXXC motif	1013:1026	the CXXC motif	1013:1026	Of the 21 mutants, N133Q, N312Q, N443Q, C46R (in the CXXC motif) and R417H (in the heptad repeat region and immunosuppressive domain) lost their fusogenicity, whereas N332Q, N118S, T367M (in the fusion peptide), V483I (in the transmembrane domain) and T522M (in the cytoplasmic domain) enhanced the fusogenic activity.
26853155	3	14	theme	syncytin-2	567:576	arg1	mutants					556:562	21 single-amino-acid substitution mutants	522:562	21 single-amino-acid substitution mutants	522:562	We constructed expression plasmids of wild-type and 21 single-amino-acid substitution mutants of syncytin-2, including 10 N-glycosylation sites individually silenced by mutagenizing N to Q, 1 naturally occurring single-nucleotide polymorphism (SNP) N118S that introduced an N-glycosylation site, and another 10 non-synonymous SNPs located within important functional domains.
26853155	3	14	theme	syncytin-2	567:576	arg1	wild-type					508:516	wild-type	508:516	wild-type	508:516	We constructed expression plasmids of wild-type and 21 single-amino-acid substitution mutants of syncytin-2, including 10 N-glycosylation sites individually silenced by mutagenizing N to Q, 1 naturally occurring single-nucleotide polymorphism (SNP) N118S that introduced an N-glycosylation site, and another 10 non-synonymous SNPs located within important functional domains.
26853155	3	14	theme	syncytin-2	567:576	arg1	sites					608:612	10 N-glycosylation sites	589:612	10 N-glycosylation sites individually silenced by mutagenizing N to Q, 1 naturally occurring single-nucleotide polymorphism (SNP) N118S that introduced an N-glycosylation site, and another 10 non-synonymous SNPs located within important functional domains	589:843	We constructed expression plasmids of wild-type and 21 single-amino-acid substitution mutants of syncytin-2, including 10 N-glycosylation sites individually silenced by mutagenizing N to Q, 1 naturally occurring single-nucleotide polymorphism (SNP) N118S that introduced an N-glycosylation site, and another 10 non-synonymous SNPs located within important functional domains.
26853155	1	15	theme	placental	157:165	arg1	indispensable					247:259	indispensable	247:259	indispensable	247:259	The placental syncytiotrophoblast, which is formed by the fusion of cytotrophoblast cells, is indispensable for the establishment and maintenance of normal pregnancy.
26853155	1	15	theme	placental	157:165	arg1	syncytiotrophoblast					167:185	The placental syncytiotrophoblast	153:185	The placental syncytiotrophoblast	153:185	The placental syncytiotrophoblast, which is formed by the fusion of cytotrophoblast cells, is indispensable for the establishment and maintenance of normal pregnancy.
26853155	0	16	theme	human	135:139	arg1	syncytin-2					141:150	human syncytin-2	135:150	human syncytin-2	135:150	Effects of individually silenced N-glycosylation sites and non-synonymous single-nucleotide polymorphisms on the fusogenic function of human syncytin-2.
26853155	3	17	theme	important	816:824	arg1	domains					837:843	important functional domains	816:843	important functional domains	816:843	We constructed expression plasmids of wild-type and 21 single-amino-acid substitution mutants of syncytin-2, including 10 N-glycosylation sites individually silenced by mutagenizing N to Q, 1 naturally occurring single-nucleotide polymorphism (SNP) N118S that introduced an N-glycosylation site, and another 10 non-synonymous SNPs located within important functional domains.
26853155	6	18	theme	293T	1384:1387	arg1	cells					1389:1393	293T cells	1384:1393	293T cells	1384:1393	We also proved that N133, N146, N177, N220, N241, N247, N312, N332 and N443 were all glycosylated in 293T cells.
26853155	8	19	theme	syncytin-2	1616:1625	arg1	sequence					1604:1611	the coding sequence	1593:1611	the coding sequence of syncytin-2 in 125 severe pre-eclamptic patients and 272 normal pregnant Chinese women	1593:1700	We also sequenced the coding sequence of syncytin-2 in 125 severe pre-eclamptic patients and 272 normal pregnant Chinese women.
26853155	3	20	theme	expression	485:494	arg1	plasmids					496:503	expression plasmids	485:503	expression plasmids of wild-type and 21 single-amino-acid substitution mutants of syncytin-2, including 10 N-glycosylation sites individually silenced by mutagenizing N to Q, 1 naturally occurring single-nucleotide polymorphism (SNP) N118S that introduced an N-glycosylation site, and another 10 non-synonymous SNPs located within important functional domains	485:843	We constructed expression plasmids of wild-type and 21 single-amino-acid substitution mutants of syncytin-2, including 10 N-glycosylation sites individually silenced by mutagenizing N to Q, 1 naturally occurring single-nucleotide polymorphism (SNP) N118S that introduced an N-glycosylation site, and another 10 non-synonymous SNPs located within important functional domains.
26853155	9	21	theme	heterozygous	1782:1793	arg1	carriers					1795:1802	heterozygous carriers	1782:1802	heterozygous carriers	1782:1802	Surprisingly, only 1 non-synonymous SNP T522M was found and the frequencies of heterozygous carriers were not significantly different.
26853155	10	22	theme	optimal	1954:1960	arg1	induction					1969:1977	optimal fusion induction	1954:1977	optimal fusion induction	1954:1977	Taken together, our results suggest that N-glycans at residues 133, 312, 332 and 443 of syncytin-2 are required for optimal fusion induction, and that SNPs C46R, N118S, T367M, R417H, V483I and T522M can alter the fusogenic function of syncytin-2.
26853155	8	23	theme	severe	1634:1639	arg1	patients					1655:1662	125 severe pre-eclamptic patients	1630:1662	125 severe pre-eclamptic patients	1630:1662	We also sequenced the coding sequence of syncytin-2 in 125 severe pre-eclamptic patients and 272 normal pregnant Chinese women.
26853155	2	24	theme	cell-cell	439:447	arg1	fusion					449:454	trophoblast cell-cell fusion	427:454	trophoblast cell-cell fusion	427:454	The human endogenous retrovirus envelope glycoprotein syncytin-2 is the most important player in mediating trophoblast cell-cell fusion as a fusogen.
26853155	2	24	theme	cell-cell	439:447	arg1	fusogen					461:467	a fusogen	459:467	a fusogen	459:467	The human endogenous retrovirus envelope glycoprotein syncytin-2 is the most important player in mediating trophoblast cell-cell fusion as a fusogen.
26853155	3	25	theme	located	801:807	arg1	SNPs					796:799	another 10 non-synonymous SNPs	770:799	another 10 non-synonymous SNPs located within important functional domains	770:843	We constructed expression plasmids of wild-type and 21 single-amino-acid substitution mutants of syncytin-2, including 10 N-glycosylation sites individually silenced by mutagenizing N to Q, 1 naturally occurring single-nucleotide polymorphism (SNP) N118S that introduced an N-glycosylation site, and another 10 non-synonymous SNPs located within important functional domains.
26853155	4	26	theme	293T	952:955	arg1	cells					957:961	merging 293T cells	944:961	merging 293T cells	944:961	We observed that syncytin-2 was highly fusogenic and that the mutants had different capacities in merging 293T cells.
26853155	7	27	theme	more	1559:1562	arg1	receptors					1564:1572	more receptors	1559:1572	more receptors	1559:1572	A co-immunoprecipitation assay showed compromised interaction between mutants N443Q, C46R, T367M, R417H and the receptor MFSD2A, whereas N118S was associated with more receptors.
26853155	2	28	theme	envelope	352:359	arg1	player					407:412	the most important player	388:412	the most important player in mediating trophoblast cell-cell fusion as a fusogen	388:467	The human endogenous retrovirus envelope glycoprotein syncytin-2 is the most important player in mediating trophoblast cell-cell fusion as a fusogen.
26853155	2	28	theme	envelope	352:359	arg1	syncytin-2					374:383	The human endogenous retrovirus envelope glycoprotein syncytin-2	320:383	The human endogenous retrovirus envelope glycoprotein syncytin-2	320:383	The human endogenous retrovirus envelope glycoprotein syncytin-2 is the most important player in mediating trophoblast cell-cell fusion as a fusogen.
26853155	2	29	theme	trophoblast	427:437	arg1	fusion					449:454	trophoblast cell-cell fusion	427:454	trophoblast cell-cell fusion	427:454	The human endogenous retrovirus envelope glycoprotein syncytin-2 is the most important player in mediating trophoblast cell-cell fusion as a fusogen.
26853155	2	29	theme	trophoblast	427:437	arg1	fusogen					461:467	a fusogen	459:467	a fusogen	459:467	The human endogenous retrovirus envelope glycoprotein syncytin-2 is the most important player in mediating trophoblast cell-cell fusion as a fusogen.
26853155	9	30	theme	non-synonymous	1724:1737	arg1	SNP					1739:1741	only 1 non-synonymous SNP	1717:1741	only 1 non-synonymous SNP T522M	1717:1747	Surprisingly, only 1 non-synonymous SNP T522M was found and the frequencies of heterozygous carriers were not significantly different.
26853155	1	31	theme	normal	302:307	arg1	pregnancy					309:317	normal pregnancy	302:317	normal pregnancy	302:317	The placental syncytiotrophoblast, which is formed by the fusion of cytotrophoblast cells, is indispensable for the establishment and maintenance of normal pregnancy.
26853155	4	32	theme	merging	944:950	arg1	cells					957:961	merging 293T cells	944:961	merging 293T cells	944:961	We observed that syncytin-2 was highly fusogenic and that the mutants had different capacities in merging 293T cells.
26853155	2	33	theme	retrovirus	341:350	arg1	player					407:412	the most important player	388:412	the most important player in mediating trophoblast cell-cell fusion as a fusogen	388:467	The human endogenous retrovirus envelope glycoprotein syncytin-2 is the most important player in mediating trophoblast cell-cell fusion as a fusogen.
26853155	2	33	theme	retrovirus	341:350	arg1	syncytin-2					374:383	The human endogenous retrovirus envelope glycoprotein syncytin-2	320:383	The human endogenous retrovirus envelope glycoprotein syncytin-2	320:383	The human endogenous retrovirus envelope glycoprotein syncytin-2 is the most important player in mediating trophoblast cell-cell fusion as a fusogen.
26853155	0	34	theme	silenced	24:31	arg1	sites					49:53	individually silenced N-glycosylation sites	11:53	individually silenced N-glycosylation sites	11:53	Effects of individually silenced N-glycosylation sites and non-synonymous single-nucleotide polymorphisms on the fusogenic function of human syncytin-2.
26853155	1	35	theme	pregnancy	309:317	arg1	maintenance					287:297	maintenance	287:297	maintenance	287:297	The placental syncytiotrophoblast, which is formed by the fusion of cytotrophoblast cells, is indispensable for the establishment and maintenance of normal pregnancy.
26853155	1	35	theme	pregnancy	309:317	arg1	establishment					269:281	establishment	269:281	establishment	269:281	The placental syncytiotrophoblast, which is formed by the fusion of cytotrophoblast cells, is indispensable for the establishment and maintenance of normal pregnancy.
26853155	9	36	theme	SNP	1739:1741	arg1	T522M					1743:1747	only 1 non-synonymous SNP T522M	1717:1747	only 1 non-synonymous SNP T522M	1717:1747	Surprisingly, only 1 non-synonymous SNP T522M was found and the frequencies of heterozygous carriers were not significantly different.
26853155	2	37	theme	endogenous	330:339	arg1	player					407:412	the most important player	388:412	the most important player in mediating trophoblast cell-cell fusion as a fusogen	388:467	The human endogenous retrovirus envelope glycoprotein syncytin-2 is the most important player in mediating trophoblast cell-cell fusion as a fusogen.
26853155	2	37	theme	endogenous	330:339	arg1	syncytin-2					374:383	The human endogenous retrovirus envelope glycoprotein syncytin-2	320:383	The human endogenous retrovirus envelope glycoprotein syncytin-2	320:383	The human endogenous retrovirus envelope glycoprotein syncytin-2 is the most important player in mediating trophoblast cell-cell fusion as a fusogen.
26853155	8	38	theme	pre-eclamptic	1641:1653	arg1	patients					1655:1662	125 severe pre-eclamptic patients	1630:1662	125 severe pre-eclamptic patients	1630:1662	We also sequenced the coding sequence of syncytin-2 in 125 severe pre-eclamptic patients and 272 normal pregnant Chinese women.
26853155	8	39	from	sequence	1604:1611	arg1	patients					1655:1662	125 severe pre-eclamptic patients	1630:1662	125 severe pre-eclamptic patients	1630:1662	We also sequenced the coding sequence of syncytin-2 in 125 severe pre-eclamptic patients and 272 normal pregnant Chinese women.
26853155	8	39	from	sequence	1604:1611	arg1	women					1696:1700	272 normal pregnant Chinese women	1668:1700	272 normal pregnant Chinese women	1668:1700	We also sequenced the coding sequence of syncytin-2 in 125 severe pre-eclamptic patients and 272 normal pregnant Chinese women.
26853155	3	40	theme	functional	826:835	arg1	domains					837:843	important functional domains	816:843	important functional domains	816:843	We constructed expression plasmids of wild-type and 21 single-amino-acid substitution mutants of syncytin-2, including 10 N-glycosylation sites individually silenced by mutagenizing N to Q, 1 naturally occurring single-nucleotide polymorphism (SNP) N118S that introduced an N-glycosylation site, and another 10 non-synonymous SNPs located within important functional domains.
26853155	0	41	theme	syncytin-2	141:150	arg1	function					123:130	the fusogenic function	109:130	the fusogenic function of human syncytin-2	109:150	Effects of individually silenced N-glycosylation sites and non-synonymous single-nucleotide polymorphisms on the fusogenic function of human syncytin-2.
26853155	2	42	theme	human	324:328	arg1	player					407:412	the most important player	388:412	the most important player in mediating trophoblast cell-cell fusion as a fusogen	388:467	The human endogenous retrovirus envelope glycoprotein syncytin-2 is the most important player in mediating trophoblast cell-cell fusion as a fusogen.
26853155	2	42	theme	human	324:328	arg1	syncytin-2					374:383	The human endogenous retrovirus envelope glycoprotein syncytin-2	320:383	The human endogenous retrovirus envelope glycoprotein syncytin-2	320:383	The human endogenous retrovirus envelope glycoprotein syncytin-2 is the most important player in mediating trophoblast cell-cell fusion as a fusogen.
26853155	1	43	theme	cytotrophoblast	221:235	arg1	cells					237:241	cytotrophoblast cells	221:241	cytotrophoblast cells	221:241	The placental syncytiotrophoblast, which is formed by the fusion of cytotrophoblast cells, is indispensable for the establishment and maintenance of normal pregnancy.
26853155	0	44	theme	sites	49:53	arg1	Effects					0:6	Effects	0:6	Effects of individually silenced N-glycosylation sites and non-synonymous single-nucleotide polymorphisms on the fusogenic function of human syncytin-2.	0:151	Effects of individually silenced N-glycosylation sites and non-synonymous single-nucleotide polymorphisms on the fusogenic function of human syncytin-2.
26853155	10	45	theme	fusion	1962:1967	arg1	induction					1969:1977	optimal fusion induction	1954:1977	optimal fusion induction	1954:1977	Taken together, our results suggest that N-glycans at residues 133, 312, 332 and 443 of syncytin-2 are required for optimal fusion induction, and that SNPs C46R, N118S, T367M, R417H, V483I and T522M can alter the fusogenic function of syncytin-2.
26853155	9	46	theme	carriers	1795:1802	arg1	frequencies					1767:1777	the frequencies	1763:1777	the frequencies of heterozygous carriers	1763:1802	Surprisingly, only 1 non-synonymous SNP T522M was found and the frequencies of heterozygous carriers were not significantly different.
26853155	9	46	theme	carriers	1795:1802	arg1	different					1827:1835	different	1827:1835	different	1827:1835	Surprisingly, only 1 non-synonymous SNP T522M was found and the frequencies of heterozygous carriers were not significantly different.
26853155	1	47	theme	cells	237:241	arg1	fusion					211:216	the fusion	207:216	the fusion of cytotrophoblast cells	207:241	The placental syncytiotrophoblast, which is formed by the fusion of cytotrophoblast cells, is indispensable for the establishment and maintenance of normal pregnancy.
26853155	0	48	theme	N-glycosylation	33:47	arg1	sites					49:53	individually silenced N-glycosylation sites	11:53	individually silenced N-glycosylation sites	11:53	Effects of individually silenced N-glycosylation sites and non-synonymous single-nucleotide polymorphisms on the fusogenic function of human syncytin-2.
26853155	3	49	theme	occurring	672:680	arg1	N118S					719:723	1 naturally occurring single-nucleotide polymorphism (SNP) N118S	660:723	1 naturally occurring single-nucleotide polymorphism (SNP) N118S that introduced an N-glycosylation site, and another 10 non-synonymous SNPs located within important functional domains	660:843	We constructed expression plasmids of wild-type and 21 single-amino-acid substitution mutants of syncytin-2, including 10 N-glycosylation sites individually silenced by mutagenizing N to Q, 1 naturally occurring single-nucleotide polymorphism (SNP) N118S that introduced an N-glycosylation site, and another 10 non-synonymous SNPs located within important functional domains.
26853155	3	49	theme	occurring	672:680	arg1	Q					657:657	Q	657:657	Q	657:657	We constructed expression plasmids of wild-type and 21 single-amino-acid substitution mutants of syncytin-2, including 10 N-glycosylation sites individually silenced by mutagenizing N to Q, 1 naturally occurring single-nucleotide polymorphism (SNP) N118S that introduced an N-glycosylation site, and another 10 non-synonymous SNPs located within important functional domains.
26853155	8	50	theme	pregnant	1679:1686	arg1	women					1696:1700	272 normal pregnant Chinese women	1668:1700	272 normal pregnant Chinese women	1668:1700	We also sequenced the coding sequence of syncytin-2 in 125 severe pre-eclamptic patients and 272 normal pregnant Chinese women.
26853155	3	51	theme	wild-type	508:516	arg1	plasmids					496:503	expression plasmids	485:503	expression plasmids of wild-type and 21 single-amino-acid substitution mutants of syncytin-2, including 10 N-glycosylation sites individually silenced by mutagenizing N to Q, 1 naturally occurring single-nucleotide polymorphism (SNP) N118S that introduced an N-glycosylation site, and another 10 non-synonymous SNPs located within important functional domains	485:843	We constructed expression plasmids of wild-type and 21 single-amino-acid substitution mutants of syncytin-2, including 10 N-glycosylation sites individually silenced by mutagenizing N to Q, 1 naturally occurring single-nucleotide polymorphism (SNP) N118S that introduced an N-glycosylation site, and another 10 non-synonymous SNPs located within important functional domains.
26853155	0	52	theme	non-synonymous	59:72	arg1	polymorphisms					92:104	non-synonymous single-nucleotide polymorphisms	59:104	non-synonymous single-nucleotide polymorphisms	59:104	Effects of individually silenced N-glycosylation sites and non-synonymous single-nucleotide polymorphisms on the fusogenic function of human syncytin-2.
26853155	5	53	theme	fusion	1159:1164	arg1	peptide					1166:1172	the fusion peptide	1155:1172	the fusion peptide	1155:1172	Of the 21 mutants, N133Q, N312Q, N443Q, C46R (in the CXXC motif) and R417H (in the heptad repeat region and immunosuppressive domain) lost their fusogenicity, whereas N332Q, N118S, T367M (in the fusion peptide), V483I (in the transmembrane domain) and T522M (in the cytoplasmic domain) enhanced the fusogenic activity.
26853155	7	54	dep	mutants	1466:1472	arg1	R417H					1494:1498	R417H	1494:1498	R417H	1494:1498	A co-immunoprecipitation assay showed compromised interaction between mutants N443Q, C46R, T367M, R417H and the receptor MFSD2A, whereas N118S was associated with more receptors.
26853155	7	54	dep	mutants	1466:1472	arg1	T367M					1487:1491	T367M	1487:1491	T367M	1487:1491	A co-immunoprecipitation assay showed compromised interaction between mutants N443Q, C46R, T367M, R417H and the receptor MFSD2A, whereas N118S was associated with more receptors.
26853155	7	54	dep	mutants	1466:1472	arg1	C46R					1481:1484	C46R	1481:1484	C46R	1481:1484	A co-immunoprecipitation assay showed compromised interaction between mutants N443Q, C46R, T367M, R417H and the receptor MFSD2A, whereas N118S was associated with more receptors.
26853155	4	55	theme	different	920:928	arg1	capacities					930:939	different capacities	920:939	different capacities	920:939	We observed that syncytin-2 was highly fusogenic and that the mutants had different capacities in merging 293T cells.
26853155	8	56	theme	normal	1672:1677	arg1	women					1696:1700	272 normal pregnant Chinese women	1668:1700	272 normal pregnant Chinese women	1668:1700	We also sequenced the coding sequence of syncytin-2 in 125 severe pre-eclamptic patients and 272 normal pregnant Chinese women.
26853155	3	57	theme	mutants	556:562	arg1	plasmids					496:503	expression plasmids	485:503	expression plasmids of wild-type and 21 single-amino-acid substitution mutants of syncytin-2, including 10 N-glycosylation sites individually silenced by mutagenizing N to Q, 1 naturally occurring single-nucleotide polymorphism (SNP) N118S that introduced an N-glycosylation site, and another 10 non-synonymous SNPs located within important functional domains	485:843	We constructed expression plasmids of wild-type and 21 single-amino-acid substitution mutants of syncytin-2, including 10 N-glycosylation sites individually silenced by mutagenizing N to Q, 1 naturally occurring single-nucleotide polymorphism (SNP) N118S that introduced an N-glycosylation site, and another 10 non-synonymous SNPs located within important functional domains.
26853155	2	58	gly	glycoprotein	361:372	arg1	glycoprotein					361:372	The human endogenous retrovirus envelope glycoprotein syncytin-2	320:383	The human endogenous retrovirus envelope glycoprotein syncytin-2	320:383	The human endogenous retrovirus envelope glycoprotein syncytin-2 is the most important player in mediating trophoblast cell-cell fusion as a fusogen.
26853155	5	59	theme	immunosuppressive	1072:1088	arg1	domain					1090:1095	immunosuppressive domain	1072:1095	immunosuppressive domain	1072:1095	Of the 21 mutants, N133Q, N312Q, N443Q, C46R (in the CXXC motif) and R417H (in the heptad repeat region and immunosuppressive domain) lost their fusogenicity, whereas N332Q, N118S, T367M (in the fusion peptide), V483I (in the transmembrane domain) and T522M (in the cytoplasmic domain) enhanced the fusogenic activity.
26853155	0	60	gly	N-glycosylation	33:47	arg2	sites					49:53	individually silenced N-glycosylation sites	11:53	individually silenced N-glycosylation sites	11:53	Effects of individually silenced N-glycosylation sites and non-synonymous single-nucleotide polymorphisms on the fusogenic function of human syncytin-2.
26853155	5	61	theme	heptad	1047:1052	arg1	region					1061:1066	the heptad repeat region	1043:1066	the heptad repeat region	1043:1066	Of the 21 mutants, N133Q, N312Q, N443Q, C46R (in the CXXC motif) and R417H (in the heptad repeat region and immunosuppressive domain) lost their fusogenicity, whereas N332Q, N118S, T367M (in the fusion peptide), V483I (in the transmembrane domain) and T522M (in the cytoplasmic domain) enhanced the fusogenic activity.
26853155	3	62	theme	single-amino-acid	525:541	arg1	mutants					556:562	21 single-amino-acid substitution mutants	522:562	21 single-amino-acid substitution mutants	522:562	We constructed expression plasmids of wild-type and 21 single-amino-acid substitution mutants of syncytin-2, including 10 N-glycosylation sites individually silenced by mutagenizing N to Q, 1 naturally occurring single-nucleotide polymorphism (SNP) N118S that introduced an N-glycosylation site, and another 10 non-synonymous SNPs located within important functional domains.
26853155	3	62	theme	single-amino-acid	525:541	arg1	sites					608:612	10 N-glycosylation sites	589:612	10 N-glycosylation sites individually silenced by mutagenizing N to Q, 1 naturally occurring single-nucleotide polymorphism (SNP) N118S that introduced an N-glycosylation site, and another 10 non-synonymous SNPs located within important functional domains	589:843	We constructed expression plasmids of wild-type and 21 single-amino-acid substitution mutants of syncytin-2, including 10 N-glycosylation sites individually silenced by mutagenizing N to Q, 1 naturally occurring single-nucleotide polymorphism (SNP) N118S that introduced an N-glycosylation site, and another 10 non-synonymous SNPs located within important functional domains.
26853155	3	63	theme	mutagenizing	639:650	arg1	N					652:652	mutagenizing N	639:652	mutagenizing N to Q, 1 naturally occurring single-nucleotide polymorphism (SNP) N118S that introduced an N-glycosylation site, and another 10 non-synonymous SNPs located within important functional domains	639:843	We constructed expression plasmids of wild-type and 21 single-amino-acid substitution mutants of syncytin-2, including 10 N-glycosylation sites individually silenced by mutagenizing N to Q, 1 naturally occurring single-nucleotide polymorphism (SNP) N118S that introduced an N-glycosylation site, and another 10 non-synonymous SNPs located within important functional domains.
26853155	7	64	theme	receptor	1508:1515	arg1	MFSD2A					1517:1522	the receptor MFSD2A	1504:1522	the receptor MFSD2A	1504:1522	A co-immunoprecipitation assay showed compromised interaction between mutants N443Q, C46R, T367M, R417H and the receptor MFSD2A, whereas N118S was associated with more receptors.
26853155	8	65	theme	Chinese	1688:1694	arg1	women					1696:1700	272 normal pregnant Chinese women	1668:1700	272 normal pregnant Chinese women	1668:1700	We also sequenced the coding sequence of syncytin-2 in 125 severe pre-eclamptic patients and 272 normal pregnant Chinese women.
26853155	10	66	theme	syncytin-2	1926:1935	arg1	residues					1892:1899	residues 133, 312, 332 and 443	1892:1921	residues 133, 312, 332 and 443 of syncytin-2	1892:1935	Taken together, our results suggest that N-glycans at residues 133, 312, 332 and 443 of syncytin-2 are required for optimal fusion induction, and that SNPs C46R, N118S, T367M, R417H, V483I and T522M can alter the fusogenic function of syncytin-2.
26853155	10	66	theme	syncytin-2	1926:1935	arg1	syncytin-2					1926:1935	syncytin-2	1926:1935	syncytin-2	1926:1935	Taken together, our results suggest that N-glycans at residues 133, 312, 332 and 443 of syncytin-2 are required for optimal fusion induction, and that SNPs C46R, N118S, T367M, R417H, V483I and T522M can alter the fusogenic function of syncytin-2.
26853155	10	67	theme	syncytin-2	2073:2082	arg1	function					2061:2068	the fusogenic function	2047:2068	the fusogenic function of syncytin-2	2047:2082	Taken together, our results suggest that N-glycans at residues 133, 312, 332 and 443 of syncytin-2 are required for optimal fusion induction, and that SNPs C46R, N118S, T367M, R417H, V483I and T522M can alter the fusogenic function of syncytin-2.
26853155	2	68	theme	glycoprotein	361:372	arg1	player					407:412	the most important player	388:412	the most important player in mediating trophoblast cell-cell fusion as a fusogen	388:467	The human endogenous retrovirus envelope glycoprotein syncytin-2 is the most important player in mediating trophoblast cell-cell fusion as a fusogen.
26853155	2	68	theme	glycoprotein	361:372	arg1	syncytin-2					374:383	The human endogenous retrovirus envelope glycoprotein syncytin-2	320:383	The human endogenous retrovirus envelope glycoprotein syncytin-2	320:383	The human endogenous retrovirus envelope glycoprotein syncytin-2 is the most important player in mediating trophoblast cell-cell fusion as a fusogen.
26853155	5	69	theme	fusogenic	1263:1271	arg1	activity					1273:1280	the fusogenic activity	1259:1280	the fusogenic activity	1259:1280	Of the 21 mutants, N133Q, N312Q, N443Q, C46R (in the CXXC motif) and R417H (in the heptad repeat region and immunosuppressive domain) lost their fusogenicity, whereas N332Q, N118S, T367M (in the fusion peptide), V483I (in the transmembrane domain) and T522M (in the cytoplasmic domain) enhanced the fusogenic activity.
26853155	0	70	theme	polymorphisms	92:104	arg1	Effects					0:6	Effects	0:6	Effects of individually silenced N-glycosylation sites and non-synonymous single-nucleotide polymorphisms on the fusogenic function of human syncytin-2.	0:151	Effects of individually silenced N-glycosylation sites and non-synonymous single-nucleotide polymorphisms on the fusogenic function of human syncytin-2.
26853155	3	71	theme	N-glycosylation	744:758	arg1	site					760:763	an N-glycosylation site	741:763	an N-glycosylation site	741:763	We constructed expression plasmids of wild-type and 21 single-amino-acid substitution mutants of syncytin-2, including 10 N-glycosylation sites individually silenced by mutagenizing N to Q, 1 naturally occurring single-nucleotide polymorphism (SNP) N118S that introduced an N-glycosylation site, and another 10 non-synonymous SNPs located within important functional domains.
26853155	3	72	theme	single-nucleotide	682:698	arg1	polymorphism					700:711	single-nucleotide polymorphism	682:711	1 naturally occurring single-nucleotide polymorphism (SNP) N118S that introduced an N-glycosylation site, and another 10 non-synonymous SNPs located within important functional domains	660:843	We constructed expression plasmids of wild-type and 21 single-amino-acid substitution mutants of syncytin-2, including 10 N-glycosylation sites individually silenced by mutagenizing N to Q, 1 naturally occurring single-nucleotide polymorphism (SNP) N118S that introduced an N-glycosylation site, and another 10 non-synonymous SNPs located within important functional domains.
26853155	3	72	theme	single-nucleotide	682:698	arg1	SNP					714:716	SNP	714:716	SNP	714:716	We constructed expression plasmids of wild-type and 21 single-amino-acid substitution mutants of syncytin-2, including 10 N-glycosylation sites individually silenced by mutagenizing N to Q, 1 naturally occurring single-nucleotide polymorphism (SNP) N118S that introduced an N-glycosylation site, and another 10 non-synonymous SNPs located within important functional domains.
26853155	3	73	theme	substitution	543:554	arg1	mutants					556:562	21 single-amino-acid substitution mutants	522:562	21 single-amino-acid substitution mutants	522:562	We constructed expression plasmids of wild-type and 21 single-amino-acid substitution mutants of syncytin-2, including 10 N-glycosylation sites individually silenced by mutagenizing N to Q, 1 naturally occurring single-nucleotide polymorphism (SNP) N118S that introduced an N-glycosylation site, and another 10 non-synonymous SNPs located within important functional domains.
26853155	3	73	theme	substitution	543:554	arg1	sites					608:612	10 N-glycosylation sites	589:612	10 N-glycosylation sites individually silenced by mutagenizing N to Q, 1 naturally occurring single-nucleotide polymorphism (SNP) N118S that introduced an N-glycosylation site, and another 10 non-synonymous SNPs located within important functional domains	589:843	We constructed expression plasmids of wild-type and 21 single-amino-acid substitution mutants of syncytin-2, including 10 N-glycosylation sites individually silenced by mutagenizing N to Q, 1 naturally occurring single-nucleotide polymorphism (SNP) N118S that introduced an N-glycosylation site, and another 10 non-synonymous SNPs located within important functional domains.
26853155	3	74	gly	N-glycosylation	744:758	arg2	site					760:763	an N-glycosylation site	741:763	an N-glycosylation site	741:763	We constructed expression plasmids of wild-type and 21 single-amino-acid substitution mutants of syncytin-2, including 10 N-glycosylation sites individually silenced by mutagenizing N to Q, 1 naturally occurring single-nucleotide polymorphism (SNP) N118S that introduced an N-glycosylation site, and another 10 non-synonymous SNPs located within important functional domains.
26853155	0	75	theme	single-nucleotide	74:90	arg1	polymorphisms					92:104	non-synonymous single-nucleotide polymorphisms	59:104	non-synonymous single-nucleotide polymorphisms	59:104	Effects of individually silenced N-glycosylation sites and non-synonymous single-nucleotide polymorphisms on the fusogenic function of human syncytin-2.
26853155	7	76	theme	co-immunoprecipitation	1398:1419	arg1	assay					1421:1425	A co-immunoprecipitation assay	1396:1425	A co-immunoprecipitation assay	1396:1425	A co-immunoprecipitation assay showed compromised interaction between mutants N443Q, C46R, T367M, R417H and the receptor MFSD2A, whereas N118S was associated with more receptors.
26853155	3	77	theme	polymorphism	700:711	arg1	N118S					719:723	1 naturally occurring single-nucleotide polymorphism (SNP) N118S	660:723	1 naturally occurring single-nucleotide polymorphism (SNP) N118S that introduced an N-glycosylation site, and another 10 non-synonymous SNPs located within important functional domains	660:843	We constructed expression plasmids of wild-type and 21 single-amino-acid substitution mutants of syncytin-2, including 10 N-glycosylation sites individually silenced by mutagenizing N to Q, 1 naturally occurring single-nucleotide polymorphism (SNP) N118S that introduced an N-glycosylation site, and another 10 non-synonymous SNPs located within important functional domains.
26853155	3	77	theme	polymorphism	700:711	arg1	Q					657:657	Q	657:657	Q	657:657	We constructed expression plasmids of wild-type and 21 single-amino-acid substitution mutants of syncytin-2, including 10 N-glycosylation sites individually silenced by mutagenizing N to Q, 1 naturally occurring single-nucleotide polymorphism (SNP) N118S that introduced an N-glycosylation site, and another 10 non-synonymous SNPs located within important functional domains.
26853155	3	78	theme	10 N-glycosylation	589:606	arg1	sites					608:612	10 N-glycosylation sites	589:612	10 N-glycosylation sites individually silenced by mutagenizing N to Q, 1 naturally occurring single-nucleotide polymorphism (SNP) N118S that introduced an N-glycosylation site, and another 10 non-synonymous SNPs located within important functional domains	589:843	We constructed expression plasmids of wild-type and 21 single-amino-acid substitution mutants of syncytin-2, including 10 N-glycosylation sites individually silenced by mutagenizing N to Q, 1 naturally occurring single-nucleotide polymorphism (SNP) N118S that introduced an N-glycosylation site, and another 10 non-synonymous SNPs located within important functional domains.
26853155	8	79	theme	coding	1597:1602	arg1	sequence					1604:1611	the coding sequence	1593:1611	the coding sequence of syncytin-2 in 125 severe pre-eclamptic patients and 272 normal pregnant Chinese women	1593:1700	We also sequenced the coding sequence of syncytin-2 in 125 severe pre-eclamptic patients and 272 normal pregnant Chinese women.
26853155	7	80	theme	compromised	1434:1444	arg1	interaction					1446:1456	compromised interaction	1434:1456	compromised interaction between mutants N443Q, C46R, T367M, R417H and the receptor MFSD2A	1434:1522	A co-immunoprecipitation assay showed compromised interaction between mutants N443Q, C46R, T367M, R417H and the receptor MFSD2A, whereas N118S was associated with more receptors.
27314333	8	0	from	positions	1378:1386	arg1	importance					1335:1344	the importance	1331:1344	the importance of N-glycosylation at these two positions	1331:1386	The results highlight the importance of N-glycosylation at these two positions in efficient folding and secretion of Rspo family.
27314333	4	1	from	N160	807:810	arg1	N-glycosylated					789:802	N-glycosylated	789:802	N-glycosylated	789:802	Using chemical inhibitors, deglycosylase and site-directed mutagenesis, we found that human Rspo1 and Rspo3 are both N-glycosylated at N137, a site near the C-terminus of the furin repeat 2 domain, and Rspo2 is N-glycosylated at N160, a position near the N-terminus of TSR1 domain.
27314333	11	2	from	role	1728:1731	arg1	biogenesis					1759:1768	the biogenesis	1755:1768	the biogenesis of Rspo1	1755:1777	Our findings provide evidence for the critical role of N-glycosylation in the biogenesis of Rspo1.
27314333	4	3	theme	human	664:668	arg1	Rspo1					670:674	human Rspo1	664:674	human Rspo1	664:674	Using chemical inhibitors, deglycosylase and site-directed mutagenesis, we found that human Rspo1 and Rspo3 are both N-glycosylated at N137, a site near the C-terminus of the furin repeat 2 domain, and Rspo2 is N-glycosylated at N160, a position near the N-terminus of TSR1 domain.
27314333	1	4	theme	signaling	213:221	arg1	activity					223:230	Wnt signaling activity	209:230	Wnt signaling activity	209:230	R-spondin 1 (Rspo1) plays an essential role in stem cell biology by potentiating Wnt signaling activity.
27314333	8	5	theme	Rspo	1426:1429	arg1	family					1431:1436	Rspo family	1426:1436	Rspo family	1426:1436	The results highlight the importance of N-glycosylation at these two positions in efficient folding and secretion of Rspo family.
27314333	7	6	theme	Similar	1200:1206	arg1	effect					1208:1213	Similar effect	1200:1213	Similar effect	1200:1213	Similar effect can be observed in the N137 Rspo1 or Rspo3 mutant engineered with Rspo2 N-glycosylation site.
27314333	6	7	theme	N-glycosylation	1013:1027	arg1	site					1029:1032	the N-glycosylation site	1009:1032	the N-glycosylation site	1009:1032	Introduction of the N-glycosylation site to Rspo2 mutant at the position homologous to N137 in Rspo1 restored full glycosylation and rescued the accumulation defect of nonglycosylated Rspo2 mutant in media.
27314333	7	8	theme	N-glycosylation	1287:1301	arg1	site					1303:1306	Rspo2 N-glycosylation site	1281:1306	Rspo2 N-glycosylation site	1281:1306	Similar effect can be observed in the N137 Rspo1 or Rspo3 mutant engineered with Rspo2 N-glycosylation site.
27314333	6	9	theme	full	1103:1106	arg1	glycosylation					1108:1120	full glycosylation	1103:1120	full glycosylation	1103:1120	Introduction of the N-glycosylation site to Rspo2 mutant at the position homologous to N137 in Rspo1 restored full glycosylation and rescued the accumulation defect of nonglycosylated Rspo2 mutant in media.
27314333	4	10	theme	site-directed	623:635	arg1	mutagenesis					637:647	site-directed mutagenesis	623:647	site-directed mutagenesis	623:647	Using chemical inhibitors, deglycosylase and site-directed mutagenesis, we found that human Rspo1 and Rspo3 are both N-glycosylated at N137, a site near the C-terminus of the furin repeat 2 domain, and Rspo2 is N-glycosylated at N160, a position near the N-terminus of TSR1 domain.
27314333	4	10	theme	site-directed	623:635	arg1	inhibitors					593:602	chemical inhibitors	584:602	chemical inhibitors	584:602	Using chemical inhibitors, deglycosylase and site-directed mutagenesis, we found that human Rspo1 and Rspo3 are both N-glycosylated at N137, a site near the C-terminus of the furin repeat 2 domain, and Rspo2 is N-glycosylated at N160, a position near the N-terminus of TSR1 domain.
27314333	6	11	theme	nonglycosylated	1161:1175	arg1	mutant					1183:1188	nonglycosylated Rspo2 mutant	1161:1188	nonglycosylated Rspo2 mutant	1161:1188	Introduction of the N-glycosylation site to Rspo2 mutant at the position homologous to N137 in Rspo1 restored full glycosylation and rescued the accumulation defect of nonglycosylated Rspo2 mutant in media.
27314333	4	12	gly	N-glycosylated	695:708	arg2	N137					713:716	N137	713:716	N137	713:716	Using chemical inhibitors, deglycosylase and site-directed mutagenesis, we found that human Rspo1 and Rspo3 are both N-glycosylated at N137, a site near the C-terminus of the furin repeat 2 domain, and Rspo2 is N-glycosylated at N160, a position near the N-terminus of TSR1 domain.
27314333	4	12	gly	N-glycosylated	695:708	arg2	site					721:724	a site	719:724	a site near the C-terminus of the furin repeat 2 domain	719:773	Using chemical inhibitors, deglycosylase and site-directed mutagenesis, we found that human Rspo1 and Rspo3 are both N-glycosylated at N137, a site near the C-terminus of the furin repeat 2 domain, and Rspo2 is N-glycosylated at N160, a position near the N-terminus of TSR1 domain.
27314333	4	12	gly	N-glycosylated	695:708	arg1	Rspo3					680:684	Rspo3	680:684	Rspo3	680:684	Using chemical inhibitors, deglycosylase and site-directed mutagenesis, we found that human Rspo1 and Rspo3 are both N-glycosylated at N137, a site near the C-terminus of the furin repeat 2 domain, and Rspo2 is N-glycosylated at N160, a position near the N-terminus of TSR1 domain.
27314333	4	12	gly	N-glycosylated	695:708	arg1	Rspo1					670:674	human Rspo1	664:674	human Rspo1	664:674	Using chemical inhibitors, deglycosylase and site-directed mutagenesis, we found that human Rspo1 and Rspo3 are both N-glycosylated at N137, a site near the C-terminus of the furin repeat 2 domain, and Rspo2 is N-glycosylated at N160, a position near the N-terminus of TSR1 domain.
27314333	9	13	theme	reticulum	1511:1519	arg1	control					1534:1540	endoplasmic reticulum (ER) quality control	1499:1540	endoplasmic reticulum (ER) quality control in N-glycan-dependent manner	1499:1569	Finally, we further showed that human Rspo1 is subjected to endoplasmic reticulum (ER) quality control in N-glycan-dependent manner.
27314333	6	14	gly	N-glycosylation	1013:1027	arg2	site					1029:1032	the N-glycosylation site	1009:1032	the N-glycosylation site	1009:1032	Introduction of the N-glycosylation site to Rspo2 mutant at the position homologous to N137 in Rspo1 restored full glycosylation and rescued the accumulation defect of nonglycosylated Rspo2 mutant in media.
27314333	3	15	theme	TSR1	500:503	arg1	domain					506:511	a thrombospondin type 1 (TSR1) domain	475:511	a thrombospondin type 1 (TSR1) domain that can provide affinity towards heparan sulfate proteoglycans	475:575	All Rspo proteins feature two amino-terminal furin-like repeats, which are responsible for Wnt signal potentiation, and a thrombospondin type 1 (TSR1) domain that can provide affinity towards heparan sulfate proteoglycans.
27314333	4	16	dep	both	690:693	arg1	N-glycosylated					695:708	N-glycosylated	695:708	N-glycosylated	695:708	Using chemical inhibitors, deglycosylase and site-directed mutagenesis, we found that human Rspo1 and Rspo3 are both N-glycosylated at N137, a site near the C-terminus of the furin repeat 2 domain, and Rspo2 is N-glycosylated at N160, a position near the N-terminus of TSR1 domain.
27314333	6	17	gly	nonglycosylated	1161:1175	arg1	mutant					1183:1188	nonglycosylated Rspo2 mutant	1161:1188	nonglycosylated Rspo2 mutant	1161:1188	Introduction of the N-glycosylation site to Rspo2 mutant at the position homologous to N137 in Rspo1 restored full glycosylation and rescued the accumulation defect of nonglycosylated Rspo2 mutant in media.
27314333	2	18	theme	diseases	305:312	arg1	number					295:300	a number	293:300	a number of diseases	293:312	Despite the fact that Rspo1 holds therapeutic potential for a number of diseases, its biogenesis is not fully elucidated.
27314333	6	19	from	position	1057:1064	arg1	Introduction					993:1004	Introduction	993:1004	Introduction of the N-glycosylation site to Rspo2 mutant at the position homologous to N137 in Rspo1	993:1092	Introduction of the N-glycosylation site to Rspo2 mutant at the position homologous to N137 in Rspo1 restored full glycosylation and rescued the accumulation defect of nonglycosylated Rspo2 mutant in media.
27314333	3	20	theme	type	492:495	arg1	domain					506:511	a thrombospondin type 1 (TSR1) domain	475:511	a thrombospondin type 1 (TSR1) domain that can provide affinity towards heparan sulfate proteoglycans	475:575	All Rspo proteins feature two amino-terminal furin-like repeats, which are responsible for Wnt signal potentiation, and a thrombospondin type 1 (TSR1) domain that can provide affinity towards heparan sulfate proteoglycans.
27314333	3	21	theme	furin-like	400:409	arg1	repeats					411:417	two amino-terminal furin-like repeats	381:417	two amino-terminal furin-like repeats	381:417	All Rspo proteins feature two amino-terminal furin-like repeats, which are responsible for Wnt signal potentiation, and a thrombospondin type 1 (TSR1) domain that can provide affinity towards heparan sulfate proteoglycans.
27314333	7	22	gly	N-glycosylation	1287:1301	arg2	site					1303:1306	Rspo2 N-glycosylation site	1281:1306	Rspo2 N-glycosylation site	1281:1306	Similar effect can be observed in the N137 Rspo1 or Rspo3 mutant engineered with Rspo2 N-glycosylation site.
27314333	10	23	theme	secreted	1665:1672	arg1	Rspo1					1674:1678	secreted Rspo1	1665:1678	secreted Rspo1	1665:1678	While N-glycan of Rspo1 plays a role in its intracellular stability, it had little effect on secreted Rspo1.
27314333	6	24	theme	homologous	1066:1075	arg1	position					1057:1064	the position	1053:1064	the position homologous to N137 in Rspo1	1053:1092	Introduction of the N-glycosylation site to Rspo2 mutant at the position homologous to N137 in Rspo1 restored full glycosylation and rescued the accumulation defect of nonglycosylated Rspo2 mutant in media.
27314333	4	25	from	N137	713:716	arg1	N-glycosylated					695:708	N-glycosylated	695:708	N-glycosylated	695:708	Using chemical inhibitors, deglycosylase and site-directed mutagenesis, we found that human Rspo1 and Rspo3 are both N-glycosylated at N137, a site near the C-terminus of the furin repeat 2 domain, and Rspo2 is N-glycosylated at N160, a position near the N-terminus of TSR1 domain.
27314333	9	26	from	control	1534:1540	arg1	manner					1564:1569	N-glycan-dependent manner	1545:1569	N-glycan-dependent manner	1545:1569	Finally, we further showed that human Rspo1 is subjected to endoplasmic reticulum (ER) quality control in N-glycan-dependent manner.
27314333	7	27	theme	Rspo3	1252:1256	arg1	mutant					1258:1263	the N137 Rspo1 or Rspo3 mutant	1234:1263	mutant	1258:1263	Similar effect can be observed in the N137 Rspo1 or Rspo3 mutant engineered with Rspo2 N-glycosylation site.
27314333	6	28	theme	mutant	1183:1188	arg1	defect					1151:1156	the accumulation defect	1134:1156	the accumulation defect of nonglycosylated Rspo2 mutant in media	1134:1197	Introduction of the N-glycosylation site to Rspo2 mutant at the position homologous to N137 in Rspo1 restored full glycosylation and rescued the accumulation defect of nonglycosylated Rspo2 mutant in media.
27314333	5	29	from	accumulation	920:931	arg1	media					936:940	media	936:940	media	936:940	Elimination of N-glycosylation at these sites affects their accumulation in media but have no effect on the ability towards heparin.
27314333	7	30	theme	N137	1238:1241	arg1	Rspo1					1243:1247	the N137 Rspo1 or Rspo3 mutant	1234:1263	Rspo1	1243:1247	Similar effect can be observed in the N137 Rspo1 or Rspo3 mutant engineered with Rspo2 N-glycosylation site.
27314333	6	31	theme	Rspo2	1177:1181	arg1	mutant					1183:1188	nonglycosylated Rspo2 mutant	1161:1188	nonglycosylated Rspo2 mutant	1161:1188	Introduction of the N-glycosylation site to Rspo2 mutant at the position homologous to N137 in Rspo1 restored full glycosylation and rescued the accumulation defect of nonglycosylated Rspo2 mutant in media.
27314333	3	32	theme	amino-terminal	385:398	arg1	repeats					411:417	two amino-terminal furin-like repeats	381:417	two amino-terminal furin-like repeats	381:417	All Rspo proteins feature two amino-terminal furin-like repeats, which are responsible for Wnt signal potentiation, and a thrombospondin type 1 (TSR1) domain that can provide affinity towards heparan sulfate proteoglycans.
27314333	0	33	theme	R-Spondin	25:33	arg1	N-Glycosylation					0:14	N-Glycosylation	0:14	N-Glycosylation of Human R-Spondin 1	0:35	N-Glycosylation of Human R-Spondin 1 Is Required for Efficient Secretion and Stability but Not for Its Heparin Binding Ability.
27314333	9	34	theme	N-glycan-dependent	1545:1562	arg1	manner					1564:1569	N-glycan-dependent manner	1545:1569	N-glycan-dependent manner	1545:1569	Finally, we further showed that human Rspo1 is subjected to endoplasmic reticulum (ER) quality control in N-glycan-dependent manner.
27314333	0	35	theme	Binding	111:117	arg1	Ability					119:125	Its Heparin Binding Ability	99:125	Its Heparin Binding Ability	99:125	N-Glycosylation of Human R-Spondin 1 Is Required for Efficient Secretion and Stability but Not for Its Heparin Binding Ability.
27314333	9	36	theme	quality	1526:1532	arg1	control					1534:1540	endoplasmic reticulum (ER) quality control	1499:1540	endoplasmic reticulum (ER) quality control in N-glycan-dependent manner	1499:1569	Finally, we further showed that human Rspo1 is subjected to endoplasmic reticulum (ER) quality control in N-glycan-dependent manner.
27314333	2	37	theme	therapeutic	267:277	arg1	potential					279:287	therapeutic potential	267:287	therapeutic potential for a number of diseases	267:312	Despite the fact that Rspo1 holds therapeutic potential for a number of diseases, its biogenesis is not fully elucidated.
27314333	4	38	theme	repeat	759:764	arg1	domain					768:773	the furin repeat 2 domain	749:773	the furin repeat 2 domain	749:773	Using chemical inhibitors, deglycosylase and site-directed mutagenesis, we found that human Rspo1 and Rspo3 are both N-glycosylated at N137, a site near the C-terminus of the furin repeat 2 domain, and Rspo2 is N-glycosylated at N160, a position near the N-terminus of TSR1 domain.
27314333	10	39	theme	Rspo1	1590:1594	arg1	N-glycan					1578:1585	N-glycan	1578:1585	N-glycan of Rspo1	1578:1594	While N-glycan of Rspo1 plays a role in its intracellular stability, it had little effect on secreted Rspo1.
27314333	0	40	theme	Human	19:23	arg1	R-Spondin					25:33	Human R-Spondin 1	19:35	Human R-Spondin 1	19:35	N-Glycosylation of Human R-Spondin 1 Is Required for Efficient Secretion and Stability but Not for Its Heparin Binding Ability.
27314333	0	41	theme	Heparin	103:109	arg1	Ability					119:125	Its Heparin Binding Ability	99:125	Its Heparin Binding Ability	99:125	N-Glycosylation of Human R-Spondin 1 Is Required for Efficient Secretion and Stability but Not for Its Heparin Binding Ability.
27314333	5	42	theme	N-glycosylation	875:889	arg1	Elimination					860:870	Elimination	860:870	Elimination of N-glycosylation at these sites	860:904	Elimination of N-glycosylation at these sites affects their accumulation in media but have no effect on the ability towards heparin.
27314333	6	43	from	N137	1080:1083	arg1	Rspo1					1088:1092	Rspo1	1088:1092	Rspo1	1088:1092	Introduction of the N-glycosylation site to Rspo2 mutant at the position homologous to N137 in Rspo1 restored full glycosylation and rescued the accumulation defect of nonglycosylated Rspo2 mutant in media.
27314333	4	44	theme	chemical	584:591	arg1	deglycosylase					605:617	deglycosylase	605:617	deglycosylase	605:617	Using chemical inhibitors, deglycosylase and site-directed mutagenesis, we found that human Rspo1 and Rspo3 are both N-glycosylated at N137, a site near the C-terminus of the furin repeat 2 domain, and Rspo2 is N-glycosylated at N160, a position near the N-terminus of TSR1 domain.
27314333	4	44	theme	chemical	584:591	arg1	mutagenesis					637:647	site-directed mutagenesis	623:647	site-directed mutagenesis	623:647	Using chemical inhibitors, deglycosylase and site-directed mutagenesis, we found that human Rspo1 and Rspo3 are both N-glycosylated at N137, a site near the C-terminus of the furin repeat 2 domain, and Rspo2 is N-glycosylated at N160, a position near the N-terminus of TSR1 domain.
27314333	4	44	theme	chemical	584:591	arg1	inhibitors					593:602	chemical inhibitors	584:602	chemical inhibitors	584:602	Using chemical inhibitors, deglycosylase and site-directed mutagenesis, we found that human Rspo1 and Rspo3 are both N-glycosylated at N137, a site near the C-terminus of the furin repeat 2 domain, and Rspo2 is N-glycosylated at N160, a position near the N-terminus of TSR1 domain.
27314333	10	45	theme	intracellular	1616:1628	arg1	stability					1630:1638	its intracellular stability	1612:1638	its intracellular stability	1612:1638	While N-glycan of Rspo1 plays a role in its intracellular stability, it had little effect on secreted Rspo1.
27314333	4	46	theme	domain	852:857	arg1	N-terminus					833:842	the N-terminus	829:842	the N-terminus of TSR1 domain	829:857	Using chemical inhibitors, deglycosylase and site-directed mutagenesis, we found that human Rspo1 and Rspo3 are both N-glycosylated at N137, a site near the C-terminus of the furin repeat 2 domain, and Rspo2 is N-glycosylated at N160, a position near the N-terminus of TSR1 domain.
27314333	0	47	gly	N-Glycosylation	0:14	arg1	R-Spondin					25:33	Human R-Spondin 1	19:35	Human R-Spondin 1	19:35	N-Glycosylation of Human R-Spondin 1 Is Required for Efficient Secretion and Stability but Not for Its Heparin Binding Ability.
27314333	1	48	theme	essential	157:165	arg1	role					167:170	an essential role	154:170	an essential role	154:170	R-spondin 1 (Rspo1) plays an essential role in stem cell biology by potentiating Wnt signaling activity.
27314333	1	49	theme	stem	175:178	arg1	biology					185:191	stem cell biology	175:191	stem cell biology	175:191	R-spondin 1 (Rspo1) plays an essential role in stem cell biology by potentiating Wnt signaling activity.
27314333	4	50	gly	N-glycosylated	789:802	arg1	Rspo2					780:784	Rspo2	780:784	Rspo2	780:784	Using chemical inhibitors, deglycosylase and site-directed mutagenesis, we found that human Rspo1 and Rspo3 are both N-glycosylated at N137, a site near the C-terminus of the furin repeat 2 domain, and Rspo2 is N-glycosylated at N160, a position near the N-terminus of TSR1 domain.
27314333	4	50	gly	N-glycosylated	789:802	arg2	N160					807:810	N160	807:810	N160	807:810	Using chemical inhibitors, deglycosylase and site-directed mutagenesis, we found that human Rspo1 and Rspo3 are both N-glycosylated at N137, a site near the C-terminus of the furin repeat 2 domain, and Rspo2 is N-glycosylated at N160, a position near the N-terminus of TSR1 domain.
27314333	4	50	gly	N-glycosylated	789:802	arg2	position					815:822	a position	813:822	a position near the N-terminus of TSR1 domain	813:857	Using chemical inhibitors, deglycosylase and site-directed mutagenesis, we found that human Rspo1 and Rspo3 are both N-glycosylated at N137, a site near the C-terminus of the furin repeat 2 domain, and Rspo2 is N-glycosylated at N160, a position near the N-terminus of TSR1 domain.
27314333	11	51	theme	N-glycosylation	1736:1750	arg1	role					1728:1731	the critical role	1715:1731	the critical role of N-glycosylation in the biogenesis of Rspo1	1715:1777	Our findings provide evidence for the critical role of N-glycosylation in the biogenesis of Rspo1.
27314333	4	52	theme	TSR1	847:850	arg1	domain					852:857	TSR1 domain	847:857	TSR1 domain	847:857	Using chemical inhibitors, deglycosylase and site-directed mutagenesis, we found that human Rspo1 and Rspo3 are both N-glycosylated at N137, a site near the C-terminus of the furin repeat 2 domain, and Rspo2 is N-glycosylated at N160, a position near the N-terminus of TSR1 domain.
27314333	7	53	located	observed	1222:1229	arg1	Rspo1					1243:1247	the N137 Rspo1 or Rspo3 mutant	1234:1263	Rspo1	1243:1247	Similar effect can be observed in the N137 Rspo1 or Rspo3 mutant engineered with Rspo2 N-glycosylation site.
27314333	7	53	located	observed	1222:1229	arg1	mutant					1258:1263	the N137 Rspo1 or Rspo3 mutant	1234:1263	mutant	1258:1263	Similar effect can be observed in the N137 Rspo1 or Rspo3 mutant engineered with Rspo2 N-glycosylation site.
27314333	7	53	located	observed	1222:1229	arg2	effect					1208:1213	Similar effect	1200:1213	Similar effect	1200:1213	Similar effect can be observed in the N137 Rspo1 or Rspo3 mutant engineered with Rspo2 N-glycosylation site.
27314333	3	54	theme	heparan	547:553	arg1	proteoglycans					563:575	heparan sulfate proteoglycans	547:575	heparan sulfate proteoglycans	547:575	All Rspo proteins feature two amino-terminal furin-like repeats, which are responsible for Wnt signal potentiation, and a thrombospondin type 1 (TSR1) domain that can provide affinity towards heparan sulfate proteoglycans.
27314333	11	55	gly	N-glycosylation	1736:1750	arg1	Rspo1					1773:1777	Rspo1	1773:1777	Rspo1	1773:1777	Our findings provide evidence for the critical role of N-glycosylation in the biogenesis of Rspo1.
27314333	1	56	theme	cell	180:183	arg1	biology					185:191	stem cell biology	175:191	stem cell biology	175:191	R-spondin 1 (Rspo1) plays an essential role in stem cell biology by potentiating Wnt signaling activity.
27314333	11	57	theme	critical	1719:1726	arg1	role					1728:1731	the critical role	1715:1731	the critical role of N-glycosylation in the biogenesis of Rspo1	1715:1777	Our findings provide evidence for the critical role of N-glycosylation in the biogenesis of Rspo1.
27314333	4	58	theme	domain	768:773	arg1	C-terminus					735:744	the C-terminus	731:744	the C-terminus of the furin repeat 2 domain	731:773	Using chemical inhibitors, deglycosylase and site-directed mutagenesis, we found that human Rspo1 and Rspo3 are both N-glycosylated at N137, a site near the C-terminus of the furin repeat 2 domain, and Rspo2 is N-glycosylated at N160, a position near the N-terminus of TSR1 domain.
27314333	3	59	theme	signal	450:455	arg1	potentiation					457:468	Wnt signal potentiation	446:468	Wnt signal potentiation	446:468	All Rspo proteins feature two amino-terminal furin-like repeats, which are responsible for Wnt signal potentiation, and a thrombospondin type 1 (TSR1) domain that can provide affinity towards heparan sulfate proteoglycans.
27314333	3	60	theme	Rspo	359:362	arg1	proteins					364:371	All Rspo proteins	355:371	All Rspo proteins	355:371	All Rspo proteins feature two amino-terminal furin-like repeats, which are responsible for Wnt signal potentiation, and a thrombospondin type 1 (TSR1) domain that can provide affinity towards heparan sulfate proteoglycans.
27314333	6	61	theme	accumulation	1138:1149	arg1	defect					1151:1156	the accumulation defect	1134:1156	the accumulation defect of nonglycosylated Rspo2 mutant in media	1134:1197	Introduction of the N-glycosylation site to Rspo2 mutant at the position homologous to N137 in Rspo1 restored full glycosylation and rescued the accumulation defect of nonglycosylated Rspo2 mutant in media.
27314333	8	62	theme	efficient	1391:1399	arg1	folding					1401:1407	efficient folding	1391:1407	efficient folding	1391:1407	The results highlight the importance of N-glycosylation at these two positions in efficient folding and secretion of Rspo family.
27314333	6	63	from	defect	1151:1156	arg1	media					1193:1197	media	1193:1197	media	1193:1197	Introduction of the N-glycosylation site to Rspo2 mutant at the position homologous to N137 in Rspo1 restored full glycosylation and rescued the accumulation defect of nonglycosylated Rspo2 mutant in media.
27314333	11	64	theme	Rspo1	1773:1777	arg1	biogenesis					1759:1768	the biogenesis	1755:1768	the biogenesis of Rspo1	1755:1777	Our findings provide evidence for the critical role of N-glycosylation in the biogenesis of Rspo1.
27314333	10	65	contain	had	1644:1646	arg1	it					1641:1642	it	1641:1642	it	1641:1642	While N-glycan of Rspo1 plays a role in its intracellular stability, it had little effect on secreted Rspo1.
27314333	10	65	contain	had	1644:1646	arg2	effect					1655:1660	little effect	1648:1660	little effect	1648:1660	While N-glycan of Rspo1 plays a role in its intracellular stability, it had little effect on secreted Rspo1.
27314333	8	66	theme	N-glycosylation	1349:1363	arg1	importance					1335:1344	the importance	1331:1344	the importance of N-glycosylation at these two positions	1331:1386	The results highlight the importance of N-glycosylation at these two positions in efficient folding and secretion of Rspo family.
27314333	4	67	theme	furin	753:757	arg1	domain					768:773	the furin repeat 2 domain	749:773	the furin repeat 2 domain	749:773	Using chemical inhibitors, deglycosylase and site-directed mutagenesis, we found that human Rspo1 and Rspo3 are both N-glycosylated at N137, a site near the C-terminus of the furin repeat 2 domain, and Rspo2 is N-glycosylated at N160, a position near the N-terminus of TSR1 domain.
27314333	6	68	theme	Rspo2	1037:1041	arg1	mutant					1043:1048	Rspo2 mutant	1037:1048	Rspo2 mutant	1037:1048	Introduction of the N-glycosylation site to Rspo2 mutant at the position homologous to N137 in Rspo1 restored full glycosylation and rescued the accumulation defect of nonglycosylated Rspo2 mutant in media.
27314333	7	69	theme	Rspo2	1281:1285	arg1	site					1303:1306	Rspo2 N-glycosylation site	1281:1306	Rspo2 N-glycosylation site	1281:1306	Similar effect can be observed in the N137 Rspo1 or Rspo3 mutant engineered with Rspo2 N-glycosylation site.
27314333	3	70	theme	Wnt	446:448	arg1	potentiation					457:468	Wnt signal potentiation	446:468	Wnt signal potentiation	446:468	All Rspo proteins feature two amino-terminal furin-like repeats, which are responsible for Wnt signal potentiation, and a thrombospondin type 1 (TSR1) domain that can provide affinity towards heparan sulfate proteoglycans.
27314333	5	71	contain	have	946:949	arg2	effect					954:959	no effect	951:959	no effect	951:959	Elimination of N-glycosylation at these sites affects their accumulation in media but have no effect on the ability towards heparin.
27314333	5	71	contain	have	946:949	arg1	Elimination					860:870	Elimination	860:870	Elimination of N-glycosylation at these sites	860:904	Elimination of N-glycosylation at these sites affects their accumulation in media but have no effect on the ability towards heparin.
27314333	6	72	theme	site	1029:1032	arg1	Introduction					993:1004	Introduction	993:1004	Introduction of the N-glycosylation site to Rspo2 mutant at the position homologous to N137 in Rspo1	993:1092	Introduction of the N-glycosylation site to Rspo2 mutant at the position homologous to N137 in Rspo1 restored full glycosylation and rescued the accumulation defect of nonglycosylated Rspo2 mutant in media.
27314333	3	73	theme	sulfate	555:561	arg1	proteoglycans					563:575	heparan sulfate proteoglycans	547:575	heparan sulfate proteoglycans	547:575	All Rspo proteins feature two amino-terminal furin-like repeats, which are responsible for Wnt signal potentiation, and a thrombospondin type 1 (TSR1) domain that can provide affinity towards heparan sulfate proteoglycans.
27314333	10	74	theme	little	1648:1653	arg1	effect					1655:1660	little effect	1648:1660	little effect	1648:1660	While N-glycan of Rspo1 plays a role in its intracellular stability, it had little effect on secreted Rspo1.
27314333	9	75	theme	human	1471:1475	arg1	Rspo1					1477:1481	human Rspo1	1471:1481	human Rspo1	1471:1481	Finally, we further showed that human Rspo1 is subjected to endoplasmic reticulum (ER) quality control in N-glycan-dependent manner.
27314333	0	76	theme	Efficient	53:61	arg1	Secretion					63:71	Efficient Secretion	53:71	Efficient Secretion	53:71	N-Glycosylation of Human R-Spondin 1 Is Required for Efficient Secretion and Stability but Not for Its Heparin Binding Ability.
27314333	8	77	theme	family	1431:1436	arg1	secretion					1413:1421	secretion	1413:1421	secretion	1413:1421	The results highlight the importance of N-glycosylation at these two positions in efficient folding and secretion of Rspo family.
27314333	8	77	theme	family	1431:1436	arg1	folding					1401:1407	efficient folding	1391:1407	efficient folding	1391:1407	The results highlight the importance of N-glycosylation at these two positions in efficient folding and secretion of Rspo family.
27314333	9	78	theme	endoplasmic	1499:1509	arg1	ER					1522:1523	ER	1522:1523	ER	1522:1523	Finally, we further showed that human Rspo1 is subjected to endoplasmic reticulum (ER) quality control in N-glycan-dependent manner.
27314333	9	78	theme	endoplasmic	1499:1509	arg1	reticulum					1511:1519	endoplasmic reticulum	1499:1519	endoplasmic reticulum (ER) quality control in N-glycan-dependent manner	1499:1569	Finally, we further showed that human Rspo1 is subjected to endoplasmic reticulum (ER) quality control in N-glycan-dependent manner.
27314333	3	79	theme	thrombospondin	477:490	arg1	domain					506:511	a thrombospondin type 1 (TSR1) domain	475:511	a thrombospondin type 1 (TSR1) domain that can provide affinity towards heparan sulfate proteoglycans	475:575	All Rspo proteins feature two amino-terminal furin-like repeats, which are responsible for Wnt signal potentiation, and a thrombospondin type 1 (TSR1) domain that can provide affinity towards heparan sulfate proteoglycans.
27314333	5	80	from	sites	900:904	arg1	Elimination					860:870	Elimination	860:870	Elimination of N-glycosylation at these sites	860:904	Elimination of N-glycosylation at these sites affects their accumulation in media but have no effect on the ability towards heparin.
27314333	1	81	theme	Wnt	209:211	arg1	activity					223:230	Wnt signaling activity	209:230	Wnt signaling activity	209:230	R-spondin 1 (Rspo1) plays an essential role in stem cell biology by potentiating Wnt signaling activity.
21920023	9	0	from	Introduction	1383:1394	arg1	mutant					1447:1452	a non-glycosylated human CTRC mutant	1417:1452	a non-glycosylated human CTRC mutant	1417:1452	Introduction of the Asn90 site in a non-glycosylated human CTRC mutant restored full glycosylation but only partially rescued the secretion defect.
21920023	6	1	theme	CTRC	1033:1036	arg1	activity					1038:1045	CTRC activity	1033:1045	CTRC activity	1033:1045	Elimination of N-glycosylation by mutation of Asn52 (N52S) reduced CTRC secretion about 10-fold from HEK 293T cells but had no effect on CTRC activity or inhibitor binding.
21920023	3	2	from	role	493:496	arg1	folding					527:533	CTRC folding	522:533	CTRC folding	522:533	The aim of the present study was to determine whether human CTRC undergoes asparagine-linked (N-linked) glycosylation and to examine the role of this modification in CTRC folding and function.
21920023	3	2	from	role	493:496	arg1	function					539:546	function	539:546	function	539:546	The aim of the present study was to determine whether human CTRC undergoes asparagine-linked (N-linked) glycosylation and to examine the role of this modification in CTRC folding and function.
21920023	8	3	gly	monoglycosylated	1356:1371	arg1	rat					1343:1345	the rat	1339:1345	the rat which is monoglycosylated on Asn90	1339:1380	Despite its important role, Asn52 is poorly conserved in other mammalian CTRC orthologs, including the rat which is monoglycosylated on Asn90.
21920023	8	3	gly	monoglycosylated	1356:1371	arg2	Asn90					1376:1380	Asn90	1376:1380	Asn90	1376:1380	Despite its important role, Asn52 is poorly conserved in other mammalian CTRC orthologs, including the rat which is monoglycosylated on Asn90.
21920023	8	3	gly	monoglycosylated	1356:1371	arg2	rat					1343:1345	the rat	1339:1345	the rat which is monoglycosylated on Asn90	1339:1380	Despite its important role, Asn52 is poorly conserved in other mammalian CTRC orthologs, including the rat which is monoglycosylated on Asn90.
21920023	8	3	gly	monoglycosylated	1356:1371	arg1	Asn90					1376:1380	Asn90	1376:1380	Asn90	1376:1380	Despite its important role, Asn52 is poorly conserved in other mammalian CTRC orthologs, including the rat which is monoglycosylated on Asn90.
21920023	4	4	theme	N-linked	581:588	arg1	Asn-Xaa-Ser/Thr					605:619	Asn-Xaa-Ser/Thr	605:619	Asn-Xaa-Ser/Thr	605:619	We abolished potential sites of N-linked glycosylation (Asn-Xaa-Ser/Thr) in human CTRC by mutating the Asn residues to Ser individually or in combination, expressed the CTRC mutants in HEK 293T cells and determined their glycosylation state using PNGase F and endo H digestion.
21920023	4	4	theme	N-linked	581:588	arg1	glycosylation					590:602	N-linked glycosylation	581:602	N-linked glycosylation (Asn-Xaa-Ser/Thr) in human CTRC	581:634	We abolished potential sites of N-linked glycosylation (Asn-Xaa-Ser/Thr) in human CTRC by mutating the Asn residues to Ser individually or in combination, expressed the CTRC mutants in HEK 293T cells and determined their glycosylation state using PNGase F and endo H digestion.
21920023	8	5	theme	CTRC	1313:1316	arg1	rat					1343:1345	the rat	1339:1345	the rat which is monoglycosylated on Asn90	1339:1380	Despite its important role, Asn52 is poorly conserved in other mammalian CTRC orthologs, including the rat which is monoglycosylated on Asn90.
21920023	8	5	theme	CTRC	1313:1316	arg1	orthologs					1318:1326	other mammalian CTRC orthologs	1297:1326	other mammalian CTRC orthologs	1297:1326	Despite its important role, Asn52 is poorly conserved in other mammalian CTRC orthologs, including the rat which is monoglycosylated on Asn90.
21920023	10	6	theme	inhibitor	1701:1709	arg1	binding					1711:1717	inhibitor binding	1701:1717	inhibitor binding	1701:1717	We conclude that N-linked glycosylation of human CTRC is required for efficient folding and secretion; however, the N-linked glycan is unimportant for enzyme activity or inhibitor binding.
21920023	5	7	theme	N-linked	870:877	arg1	glycan					879:884	a single N-linked glycan	861:884	a single N-linked glycan on Asn52	861:893	We found that human CTRC contains a single N-linked glycan on Asn52.
21920023	4	8	theme	H	814:814	arg1	digestion					816:824	endo H digestion	809:824	endo H digestion	809:824	We abolished potential sites of N-linked glycosylation (Asn-Xaa-Ser/Thr) in human CTRC by mutating the Asn residues to Ser individually or in combination, expressed the CTRC mutants in HEK 293T cells and determined their glycosylation state using PNGase F and endo H digestion.
21920023	0	9	link	Asparagine-linked	0:16	arg1	glycosylation					18:30	Asparagine-linked glycosylation	0:30	Asparagine-linked glycosylation of human chymotrypsin C	0:54	Asparagine-linked glycosylation of human chymotrypsin C is required for folding and secretion but not for enzyme activity.
21920023	3	10	theme	CTRC	522:525	arg1	folding					527:533	CTRC folding	522:533	CTRC folding	522:533	The aim of the present study was to determine whether human CTRC undergoes asparagine-linked (N-linked) glycosylation and to examine the role of this modification in CTRC folding and function.
21920023	10	11	theme	N-linked	1548:1555	arg1	glycosylation					1557:1569	N-linked glycosylation	1548:1569	N-linked glycosylation of human CTRC	1548:1583	We conclude that N-linked glycosylation of human CTRC is required for efficient folding and secretion; however, the N-linked glycan is unimportant for enzyme activity or inhibitor binding.
21920023	11	12	theme	glycan	1749:1754	arg1	position					1724:1731	The position	1720:1731	The position of the N-linked glycan	1720:1754	The position of the N-linked glycan is critical for optimal folding, and it may vary among the otherwise highly homologous mammalian CTRC sequences.
21920023	11	12	theme	glycan	1749:1754	arg1	critical					1759:1766	critical	1759:1766	critical	1759:1766	The position of the N-linked glycan is critical for optimal folding, and it may vary among the otherwise highly homologous mammalian CTRC sequences.
21920023	2	13	theme	CTRC	307:310	arg1	activity					282:289	activity	282:289	activity	282:289	Mutations that abolish activity or secretion of CTRC increase the risk for chronic pancreatitis.
21920023	2	13	theme	CTRC	307:310	arg1	secretion					294:302	secretion	294:302	secretion	294:302	Mutations that abolish activity or secretion of CTRC increase the risk for chronic pancreatitis.
21920023	5	14	theme	human	841:845	arg1	CTRC					847:850	human CTRC	841:850	human CTRC	841:850	We found that human CTRC contains a single N-linked glycan on Asn52.
21920023	4	15	theme	human	625:629	arg1	CTRC					631:634	human CTRC	625:634	human CTRC	625:634	We abolished potential sites of N-linked glycosylation (Asn-Xaa-Ser/Thr) in human CTRC by mutating the Asn residues to Ser individually or in combination, expressed the CTRC mutants in HEK 293T cells and determined their glycosylation state using PNGase F and endo H digestion.
21920023	9	16	theme	site	1409:1412	arg1	Introduction					1383:1394	Introduction	1383:1394	Introduction of the Asn90 site in a non-glycosylated human CTRC mutant	1383:1452	Introduction of the Asn90 site in a non-glycosylated human CTRC mutant restored full glycosylation but only partially rescued the secretion defect.
21920023	10	17	theme	CTRC	1580:1583	arg1	glycosylation					1557:1569	N-linked glycosylation	1548:1569	N-linked glycosylation of human CTRC	1548:1583	We conclude that N-linked glycosylation of human CTRC is required for efficient folding and secretion; however, the N-linked glycan is unimportant for enzyme activity or inhibitor binding.
21920023	11	18	theme	optimal	1772:1778	arg1	folding					1780:1786	optimal folding	1772:1786	optimal folding	1772:1786	The position of the N-linked glycan is critical for optimal folding, and it may vary among the otherwise highly homologous mammalian CTRC sequences.
21920023	7	19	theme	mutant	1101:1106	arg1	Overexpression					1069:1082	Overexpression	1069:1082	Overexpression of the N52S CTRC mutant	1069:1106	Overexpression of the N52S CTRC mutant elicited endoplasmic reticulum stress in AR42J acinar cells, indicating that N-glycosylation is required for folding of human CTRC.
21920023	9	20	theme	human	1436:1440	arg1	mutant					1447:1452	a non-glycosylated human CTRC mutant	1417:1452	a non-glycosylated human CTRC mutant	1417:1452	Introduction of the Asn90 site in a non-glycosylated human CTRC mutant restored full glycosylation but only partially rescued the secretion defect.
21920023	8	21	theme	important	1252:1260	arg1	role					1262:1265	its important role	1248:1265	its important role	1248:1265	Despite its important role, Asn52 is poorly conserved in other mammalian CTRC orthologs, including the rat which is monoglycosylated on Asn90.
21920023	1	22	theme	chymotrypsin	129:140	arg1	CTRC					145:148	CTRC	145:148	CTRC	145:148	Human chymotrypsin C (CTRC) plays a protective role in the pancreas by mitigating premature trypsinogen activation through degradation.
21920023	1	22	theme	chymotrypsin	129:140	arg1	C					142:142	Human chymotrypsin C	123:142	Human chymotrypsin C (CTRC)	123:149	Human chymotrypsin C (CTRC) plays a protective role in the pancreas by mitigating premature trypsinogen activation through degradation.
21920023	1	23	theme	Human	123:127	arg1	CTRC					145:148	CTRC	145:148	CTRC	145:148	Human chymotrypsin C (CTRC) plays a protective role in the pancreas by mitigating premature trypsinogen activation through degradation.
21920023	1	23	theme	Human	123:127	arg1	C					142:142	Human chymotrypsin C	123:142	Human chymotrypsin C (CTRC)	123:149	Human chymotrypsin C (CTRC) plays a protective role in the pancreas by mitigating premature trypsinogen activation through degradation.
21920023	11	24	link	N-linked	1740:1747	arg1	glycan					1749:1754	the N-linked glycan	1736:1754	the N-linked glycan	1736:1754	The position of the N-linked glycan is critical for optimal folding, and it may vary among the otherwise highly homologous mammalian CTRC sequences.
21920023	9	25	theme	full	1463:1466	arg1	glycosylation					1468:1480	full glycosylation	1463:1480	full glycosylation	1463:1480	Introduction of the Asn90 site in a non-glycosylated human CTRC mutant restored full glycosylation but only partially rescued the secretion defect.
21920023	6	26	theme	CTRC	963:966	arg1	secretion					968:976	CTRC secretion	963:976	CTRC secretion	963:976	Elimination of N-glycosylation by mutation of Asn52 (N52S) reduced CTRC secretion about 10-fold from HEK 293T cells but had no effect on CTRC activity or inhibitor binding.
21920023	6	27	contain	had	1016:1018	arg2	effect					1023:1028	no effect	1020:1028	no effect	1020:1028	Elimination of N-glycosylation by mutation of Asn52 (N52S) reduced CTRC secretion about 10-fold from HEK 293T cells but had no effect on CTRC activity or inhibitor binding.
21920023	6	27	contain	had	1016:1018	arg1	Elimination					896:906	Elimination	896:906	Elimination of N-glycosylation by mutation of Asn52 (N52S)	896:953	Elimination of N-glycosylation by mutation of Asn52 (N52S) reduced CTRC secretion about 10-fold from HEK 293T cells but had no effect on CTRC activity or inhibitor binding.
21920023	4	28	from	glycosylation	590:602	arg1	CTRC					631:634	human CTRC	625:634	human CTRC	625:634	We abolished potential sites of N-linked glycosylation (Asn-Xaa-Ser/Thr) in human CTRC by mutating the Asn residues to Ser individually or in combination, expressed the CTRC mutants in HEK 293T cells and determined their glycosylation state using PNGase F and endo H digestion.
21920023	4	29	gly	glycosylation	590:602	arg1	CTRC					631:634	human CTRC	625:634	human CTRC	625:634	We abolished potential sites of N-linked glycosylation (Asn-Xaa-Ser/Thr) in human CTRC by mutating the Asn residues to Ser individually or in combination, expressed the CTRC mutants in HEK 293T cells and determined their glycosylation state using PNGase F and endo H digestion.
21920023	4	29	gly	glycosylation	590:602	arg2	glycosylation					590:602	N-linked glycosylation	581:602	N-linked glycosylation (Asn-Xaa-Ser/Thr) in human CTRC	581:634	We abolished potential sites of N-linked glycosylation (Asn-Xaa-Ser/Thr) in human CTRC by mutating the Asn residues to Ser individually or in combination, expressed the CTRC mutants in HEK 293T cells and determined their glycosylation state using PNGase F and endo H digestion.
21920023	4	29	gly	glycosylation	590:602	arg2	sites					572:576	potential sites	562:576	potential sites of N-linked glycosylation (Asn-Xaa-Ser/Thr) in human CTRC	562:634	We abolished potential sites of N-linked glycosylation (Asn-Xaa-Ser/Thr) in human CTRC by mutating the Asn residues to Ser individually or in combination, expressed the CTRC mutants in HEK 293T cells and determined their glycosylation state using PNGase F and endo H digestion.
21920023	5	30	theme	single	863:868	arg1	glycan					879:884	a single N-linked glycan	861:884	a single N-linked glycan on Asn52	861:893	We found that human CTRC contains a single N-linked glycan on Asn52.
21920023	4	31	theme	293T	738:741	arg1	cells					743:747	HEK 293T cells	734:747	HEK 293T cells	734:747	We abolished potential sites of N-linked glycosylation (Asn-Xaa-Ser/Thr) in human CTRC by mutating the Asn residues to Ser individually or in combination, expressed the CTRC mutants in HEK 293T cells and determined their glycosylation state using PNGase F and endo H digestion.
21920023	7	32	theme	acinar	1155:1160	arg1	cells					1162:1166	AR42J acinar cells	1149:1166	AR42J acinar cells	1149:1166	Overexpression of the N52S CTRC mutant elicited endoplasmic reticulum stress in AR42J acinar cells, indicating that N-glycosylation is required for folding of human CTRC.
21920023	8	33	theme	other	1297:1301	arg1	rat					1343:1345	the rat	1339:1345	the rat which is monoglycosylated on Asn90	1339:1380	Despite its important role, Asn52 is poorly conserved in other mammalian CTRC orthologs, including the rat which is monoglycosylated on Asn90.
21920023	8	33	theme	other	1297:1301	arg1	orthologs					1318:1326	other mammalian CTRC orthologs	1297:1326	other mammalian CTRC orthologs	1297:1326	Despite its important role, Asn52 is poorly conserved in other mammalian CTRC orthologs, including the rat which is monoglycosylated on Asn90.
21920023	11	34	theme	mammalian	1843:1851	arg1	sequences					1858:1866	the otherwise highly homologous mammalian CTRC sequences	1811:1866	the otherwise highly homologous mammalian CTRC sequences	1811:1866	The position of the N-linked glycan is critical for optimal folding, and it may vary among the otherwise highly homologous mammalian CTRC sequences.
21920023	0	35	theme	C	54:54	arg1	glycosylation					18:30	Asparagine-linked glycosylation	0:30	Asparagine-linked glycosylation of human chymotrypsin C	0:54	Asparagine-linked glycosylation of human chymotrypsin C is required for folding and secretion but not for enzyme activity.
21920023	3	36	theme	present	371:377	arg1	study					379:383	the present study	367:383	the present study	367:383	The aim of the present study was to determine whether human CTRC undergoes asparagine-linked (N-linked) glycosylation and to examine the role of this modification in CTRC folding and function.
21920023	10	37	gly	glycosylation	1557:1569	arg1	CTRC					1580:1583	human CTRC	1574:1583	human CTRC	1574:1583	We conclude that N-linked glycosylation of human CTRC is required for efficient folding and secretion; however, the N-linked glycan is unimportant for enzyme activity or inhibitor binding.
21920023	4	38	theme	CTRC	718:721	arg1	mutants					723:729	the CTRC mutants	714:729	the CTRC mutants	714:729	We abolished potential sites of N-linked glycosylation (Asn-Xaa-Ser/Thr) in human CTRC by mutating the Asn residues to Ser individually or in combination, expressed the CTRC mutants in HEK 293T cells and determined their glycosylation state using PNGase F and endo H digestion.
21920023	3	39	theme	human	410:414	arg1	CTRC					416:419	human CTRC	410:419	human CTRC	410:419	The aim of the present study was to determine whether human CTRC undergoes asparagine-linked (N-linked) glycosylation and to examine the role of this modification in CTRC folding and function.
21920023	0	40	theme	Asparagine-linked	0:16	arg1	glycosylation					18:30	Asparagine-linked glycosylation	0:30	Asparagine-linked glycosylation of human chymotrypsin C	0:54	Asparagine-linked glycosylation of human chymotrypsin C is required for folding and secretion but not for enzyme activity.
21920023	3	41	gly	glycosylation	460:472	arg1	CTRC					416:419	human CTRC	410:419	human CTRC	410:419	The aim of the present study was to determine whether human CTRC undergoes asparagine-linked (N-linked) glycosylation and to examine the role of this modification in CTRC folding and function.
21920023	6	42	theme	293T	1001:1004	arg1	cells					1006:1010	HEK 293T cells	997:1010	HEK 293T cells	997:1010	Elimination of N-glycosylation by mutation of Asn52 (N52S) reduced CTRC secretion about 10-fold from HEK 293T cells but had no effect on CTRC activity or inhibitor binding.
21920023	7	43	theme	reticulum	1129:1137	arg1	stress					1139:1144	endoplasmic reticulum stress	1117:1144	endoplasmic reticulum stress in AR42J acinar cells	1117:1166	Overexpression of the N52S CTRC mutant elicited endoplasmic reticulum stress in AR42J acinar cells, indicating that N-glycosylation is required for folding of human CTRC.
21920023	4	44	theme	PNGase	796:801	arg1	F					803:803	PNGase F	796:803	PNGase F	796:803	We abolished potential sites of N-linked glycosylation (Asn-Xaa-Ser/Thr) in human CTRC by mutating the Asn residues to Ser individually or in combination, expressed the CTRC mutants in HEK 293T cells and determined their glycosylation state using PNGase F and endo H digestion.
21920023	7	45	theme	CTRC	1096:1099	arg1	mutant					1101:1106	the N52S CTRC mutant	1087:1106	the N52S CTRC mutant	1087:1106	Overexpression of the N52S CTRC mutant elicited endoplasmic reticulum stress in AR42J acinar cells, indicating that N-glycosylation is required for folding of human CTRC.
21920023	0	46	theme	chymotrypsin	41:52	arg1	C					54:54	human chymotrypsin C	35:54	human chymotrypsin C	35:54	Asparagine-linked glycosylation of human chymotrypsin C is required for folding and secretion but not for enzyme activity.
21920023	0	47	gly	glycosylation	18:30	arg1	C					54:54	human chymotrypsin C	35:54	human chymotrypsin C	35:54	Asparagine-linked glycosylation of human chymotrypsin C is required for folding and secretion but not for enzyme activity.
21920023	0	47	gly	glycosylation	18:30	arg1	enzyme					106:111	enzyme activity	106:120	enzyme activity	106:120	Asparagine-linked glycosylation of human chymotrypsin C is required for folding and secretion but not for enzyme activity.
21920023	2	48	theme	chronic	334:340	arg1	pancreatitis					342:353	chronic pancreatitis	334:353	chronic pancreatitis	334:353	Mutations that abolish activity or secretion of CTRC increase the risk for chronic pancreatitis.
21920023	7	49	gly	N-glycosylation	1185:1199	arg1	CTRC					1234:1237	human CTRC	1228:1237	human CTRC	1228:1237	Overexpression of the N52S CTRC mutant elicited endoplasmic reticulum stress in AR42J acinar cells, indicating that N-glycosylation is required for folding of human CTRC.
21920023	4	50	link	N-linked	581:588	arg1	Asn-Xaa-Ser/Thr					605:619	Asn-Xaa-Ser/Thr	605:619	Asn-Xaa-Ser/Thr	605:619	We abolished potential sites of N-linked glycosylation (Asn-Xaa-Ser/Thr) in human CTRC by mutating the Asn residues to Ser individually or in combination, expressed the CTRC mutants in HEK 293T cells and determined their glycosylation state using PNGase F and endo H digestion.
21920023	4	50	link	N-linked	581:588	arg1	glycosylation					590:602	N-linked glycosylation	581:602	N-linked glycosylation (Asn-Xaa-Ser/Thr) in human CTRC	581:634	We abolished potential sites of N-linked glycosylation (Asn-Xaa-Ser/Thr) in human CTRC by mutating the Asn residues to Ser individually or in combination, expressed the CTRC mutants in HEK 293T cells and determined their glycosylation state using PNGase F and endo H digestion.
21920023	7	51	theme	CTRC	1234:1237	arg1	folding					1217:1223	folding	1217:1223	folding of human CTRC	1217:1237	Overexpression of the N52S CTRC mutant elicited endoplasmic reticulum stress in AR42J acinar cells, indicating that N-glycosylation is required for folding of human CTRC.
21920023	4	52	from	sites	572:576	arg1	CTRC					631:634	human CTRC	625:634	human CTRC	625:634	We abolished potential sites of N-linked glycosylation (Asn-Xaa-Ser/Thr) in human CTRC by mutating the Asn residues to Ser individually or in combination, expressed the CTRC mutants in HEK 293T cells and determined their glycosylation state using PNGase F and endo H digestion.
21920023	6	53	theme	inhibitor	1050:1058	arg1	binding					1060:1066	inhibitor binding	1050:1066	inhibitor binding	1050:1066	Elimination of N-glycosylation by mutation of Asn52 (N52S) reduced CTRC secretion about 10-fold from HEK 293T cells but had no effect on CTRC activity or inhibitor binding.
21920023	4	54	theme	glycosylation	590:602	arg1	sites					572:576	potential sites	562:576	potential sites of N-linked glycosylation (Asn-Xaa-Ser/Thr) in human CTRC	562:634	We abolished potential sites of N-linked glycosylation (Asn-Xaa-Ser/Thr) in human CTRC by mutating the Asn residues to Ser individually or in combination, expressed the CTRC mutants in HEK 293T cells and determined their glycosylation state using PNGase F and endo H digestion.
21920023	4	54	theme	glycosylation	590:602	arg1	glycosylation					590:602	N-linked glycosylation	581:602	N-linked glycosylation (Asn-Xaa-Ser/Thr) in human CTRC	581:634	We abolished potential sites of N-linked glycosylation (Asn-Xaa-Ser/Thr) in human CTRC by mutating the Asn residues to Ser individually or in combination, expressed the CTRC mutants in HEK 293T cells and determined their glycosylation state using PNGase F and endo H digestion.
21920023	10	55	theme	enzyme	1682:1687	arg1	activity					1689:1696	enzyme activity	1682:1696	enzyme activity	1682:1696	We conclude that N-linked glycosylation of human CTRC is required for efficient folding and secretion; however, the N-linked glycan is unimportant for enzyme activity or inhibitor binding.
21920023	1	56	theme	trypsinogen	215:225	arg1	activation					227:236	premature trypsinogen activation	205:236	premature trypsinogen activation	205:236	Human chymotrypsin C (CTRC) plays a protective role in the pancreas by mitigating premature trypsinogen activation through degradation.
21920023	9	57	gly	non-glycosylated	1419:1434	arg1	mutant					1447:1452	a non-glycosylated human CTRC mutant	1417:1452	a non-glycosylated human CTRC mutant	1417:1452	Introduction of the Asn90 site in a non-glycosylated human CTRC mutant restored full glycosylation but only partially rescued the secretion defect.
21920023	3	58	link	N-linked	450:457	arg1	glycosylation					460:472	asparagine-linked (N-linked) glycosylation	431:472	asparagine-linked (N-linked) glycosylation	431:472	The aim of the present study was to determine whether human CTRC undergoes asparagine-linked (N-linked) glycosylation and to examine the role of this modification in CTRC folding and function.
21920023	4	59	theme	potential	562:570	arg1	sites					572:576	potential sites	562:576	potential sites of N-linked glycosylation (Asn-Xaa-Ser/Thr) in human CTRC	562:634	We abolished potential sites of N-linked glycosylation (Asn-Xaa-Ser/Thr) in human CTRC by mutating the Asn residues to Ser individually or in combination, expressed the CTRC mutants in HEK 293T cells and determined their glycosylation state using PNGase F and endo H digestion.
21920023	4	59	theme	potential	562:570	arg1	glycosylation					590:602	N-linked glycosylation	581:602	N-linked glycosylation (Asn-Xaa-Ser/Thr) in human CTRC	581:634	We abolished potential sites of N-linked glycosylation (Asn-Xaa-Ser/Thr) in human CTRC by mutating the Asn residues to Ser individually or in combination, expressed the CTRC mutants in HEK 293T cells and determined their glycosylation state using PNGase F and endo H digestion.
21920023	10	60	link	N-linked	1647:1654	arg1	unimportant					1666:1676	unimportant	1666:1676	unimportant	1666:1676	We conclude that N-linked glycosylation of human CTRC is required for efficient folding and secretion; however, the N-linked glycan is unimportant for enzyme activity or inhibitor binding.
21920023	10	60	link	N-linked	1647:1654	arg1	glycan					1656:1661	the N-linked glycan	1643:1661	the N-linked glycan	1643:1661	We conclude that N-linked glycosylation of human CTRC is required for efficient folding and secretion; however, the N-linked glycan is unimportant for enzyme activity or inhibitor binding.
21920023	11	61	theme	CTRC	1853:1856	arg1	sequences					1858:1866	the otherwise highly homologous mammalian CTRC sequences	1811:1866	the otherwise highly homologous mammalian CTRC sequences	1811:1866	The position of the N-linked glycan is critical for optimal folding, and it may vary among the otherwise highly homologous mammalian CTRC sequences.
21920023	10	62	link	N-linked	1548:1555	arg1	glycosylation					1557:1569	N-linked glycosylation	1548:1569	N-linked glycosylation of human CTRC	1548:1583	We conclude that N-linked glycosylation of human CTRC is required for efficient folding and secretion; however, the N-linked glycan is unimportant for enzyme activity or inhibitor binding.
21920023	1	63	theme	protective	159:168	arg1	role					170:173	a protective role	157:173	a protective role	157:173	Human chymotrypsin C (CTRC) plays a protective role in the pancreas by mitigating premature trypsinogen activation through degradation.
21920023	4	64	theme	endo	809:812	arg1	digestion					816:824	endo H digestion	809:824	endo H digestion	809:824	We abolished potential sites of N-linked glycosylation (Asn-Xaa-Ser/Thr) in human CTRC by mutating the Asn residues to Ser individually or in combination, expressed the CTRC mutants in HEK 293T cells and determined their glycosylation state using PNGase F and endo H digestion.
21920023	3	65	mod	modification	506:517	arg1	CTRC					522:525	CTRC folding	522:533	CTRC folding	522:533	The aim of the present study was to determine whether human CTRC undergoes asparagine-linked (N-linked) glycosylation and to examine the role of this modification in CTRC folding and function.
21920023	6	66	theme	Asn52	942:946	arg1	mutation					930:937	mutation	930:937	mutation of Asn52 (N52S)	930:953	Elimination of N-glycosylation by mutation of Asn52 (N52S) reduced CTRC secretion about 10-fold from HEK 293T cells but had no effect on CTRC activity or inhibitor binding.
21920023	3	67	link	asparagine-linked	431:447	arg1	glycosylation					460:472	asparagine-linked (N-linked) glycosylation	431:472	asparagine-linked (N-linked) glycosylation	431:472	The aim of the present study was to determine whether human CTRC undergoes asparagine-linked (N-linked) glycosylation and to examine the role of this modification in CTRC folding and function.
21920023	4	68	theme	Asn	652:654	arg1	residues					656:663	the Asn residues	648:663	the Asn residues	648:663	We abolished potential sites of N-linked glycosylation (Asn-Xaa-Ser/Thr) in human CTRC by mutating the Asn residues to Ser individually or in combination, expressed the CTRC mutants in HEK 293T cells and determined their glycosylation state using PNGase F and endo H digestion.
21920023	4	69	from	CTRC	631:634	arg1	sites					572:576	potential sites	562:576	potential sites of N-linked glycosylation (Asn-Xaa-Ser/Thr) in human CTRC	562:634	We abolished potential sites of N-linked glycosylation (Asn-Xaa-Ser/Thr) in human CTRC by mutating the Asn residues to Ser individually or in combination, expressed the CTRC mutants in HEK 293T cells and determined their glycosylation state using PNGase F and endo H digestion.
21920023	4	69	from	CTRC	631:634	arg1	glycosylation					590:602	N-linked glycosylation	581:602	N-linked glycosylation (Asn-Xaa-Ser/Thr) in human CTRC	581:634	We abolished potential sites of N-linked glycosylation (Asn-Xaa-Ser/Thr) in human CTRC by mutating the Asn residues to Ser individually or in combination, expressed the CTRC mutants in HEK 293T cells and determined their glycosylation state using PNGase F and endo H digestion.
21920023	9	70	theme	Asn90	1403:1407	arg1	site					1409:1412	the Asn90 site	1399:1412	the Asn90 site	1399:1412	Introduction of the Asn90 site in a non-glycosylated human CTRC mutant restored full glycosylation but only partially rescued the secretion defect.
21920023	7	71	from	stress	1139:1144	arg1	cells					1162:1166	AR42J acinar cells	1149:1166	AR42J acinar cells	1149:1166	Overexpression of the N52S CTRC mutant elicited endoplasmic reticulum stress in AR42J acinar cells, indicating that N-glycosylation is required for folding of human CTRC.
21920023	11	72	theme	N-linked	1740:1747	arg1	glycan					1749:1754	the N-linked glycan	1736:1754	the N-linked glycan	1736:1754	The position of the N-linked glycan is critical for optimal folding, and it may vary among the otherwise highly homologous mammalian CTRC sequences.
21920023	6	73	theme	N-glycosylation	911:925	arg1	Elimination					896:906	Elimination	896:906	Elimination of N-glycosylation by mutation of Asn52 (N52S)	896:953	Elimination of N-glycosylation by mutation of Asn52 (N52S) reduced CTRC secretion about 10-fold from HEK 293T cells but had no effect on CTRC activity or inhibitor binding.
21920023	10	74	theme	human	1574:1578	arg1	CTRC					1580:1583	human CTRC	1574:1583	human CTRC	1574:1583	We conclude that N-linked glycosylation of human CTRC is required for efficient folding and secretion; however, the N-linked glycan is unimportant for enzyme activity or inhibitor binding.
21920023	9	75	theme	non-glycosylated	1419:1434	arg1	mutant					1447:1452	a non-glycosylated human CTRC mutant	1417:1452	a non-glycosylated human CTRC mutant	1417:1452	Introduction of the Asn90 site in a non-glycosylated human CTRC mutant restored full glycosylation but only partially rescued the secretion defect.
21920023	9	76	theme	CTRC	1442:1445	arg1	mutant					1447:1452	a non-glycosylated human CTRC mutant	1417:1452	a non-glycosylated human CTRC mutant	1417:1452	Introduction of the Asn90 site in a non-glycosylated human CTRC mutant restored full glycosylation but only partially rescued the secretion defect.
21920023	5	77	contain	contains	852:859	arg1	CTRC					847:850	human CTRC	841:850	human CTRC	841:850	We found that human CTRC contains a single N-linked glycan on Asn52.
21920023	5	77	contain	contains	852:859	arg2	glycan					879:884	a single N-linked glycan	861:884	a single N-linked glycan on Asn52	861:893	We found that human CTRC contains a single N-linked glycan on Asn52.
21920023	7	78	theme	AR42J	1149:1153	arg1	cells					1162:1166	AR42J acinar cells	1149:1166	AR42J acinar cells	1149:1166	Overexpression of the N52S CTRC mutant elicited endoplasmic reticulum stress in AR42J acinar cells, indicating that N-glycosylation is required for folding of human CTRC.
21920023	4	79	theme	HEK	734:736	arg1	cells					743:747	HEK 293T cells	734:747	HEK 293T cells	734:747	We abolished potential sites of N-linked glycosylation (Asn-Xaa-Ser/Thr) in human CTRC by mutating the Asn residues to Ser individually or in combination, expressed the CTRC mutants in HEK 293T cells and determined their glycosylation state using PNGase F and endo H digestion.
21920023	0	80	theme	enzyme	106:111	arg1	activity					113:120	enzyme activity	106:120	enzyme activity	106:120	Asparagine-linked glycosylation of human chymotrypsin C is required for folding and secretion but not for enzyme activity.
21920023	3	81	theme	asparagine-linked	431:447	arg1	glycosylation					460:472	asparagine-linked (N-linked) glycosylation	431:472	asparagine-linked (N-linked) glycosylation	431:472	The aim of the present study was to determine whether human CTRC undergoes asparagine-linked (N-linked) glycosylation and to examine the role of this modification in CTRC folding and function.
21920023	7	82	theme	endoplasmic	1117:1127	arg1	reticulum					1129:1137	endoplasmic reticulum	1117:1137	endoplasmic reticulum stress in AR42J acinar cells	1117:1166	Overexpression of the N52S CTRC mutant elicited endoplasmic reticulum stress in AR42J acinar cells, indicating that N-glycosylation is required for folding of human CTRC.
21920023	9	83	theme	secretion	1513:1521	arg1	defect					1523:1528	the secretion defect	1509:1528	the secretion defect	1509:1528	Introduction of the Asn90 site in a non-glycosylated human CTRC mutant restored full glycosylation but only partially rescued the secretion defect.
21920023	3	84	theme	study	379:383	arg1	aim					360:362	The aim	356:362	The aim of the present study	356:383	The aim of the present study was to determine whether human CTRC undergoes asparagine-linked (N-linked) glycosylation and to examine the role of this modification in CTRC folding and function.
21920023	8	85	theme	mammalian	1303:1311	arg1	rat					1343:1345	the rat	1339:1345	the rat which is monoglycosylated on Asn90	1339:1380	Despite its important role, Asn52 is poorly conserved in other mammalian CTRC orthologs, including the rat which is monoglycosylated on Asn90.
21920023	8	85	theme	mammalian	1303:1311	arg1	orthologs					1318:1326	other mammalian CTRC orthologs	1297:1326	other mammalian CTRC orthologs	1297:1326	Despite its important role, Asn52 is poorly conserved in other mammalian CTRC orthologs, including the rat which is monoglycosylated on Asn90.
21920023	11	86	theme	homologous	1832:1841	arg1	sequences					1858:1866	the otherwise highly homologous mammalian CTRC sequences	1811:1866	the otherwise highly homologous mammalian CTRC sequences	1811:1866	The position of the N-linked glycan is critical for optimal folding, and it may vary among the otherwise highly homologous mammalian CTRC sequences.
21920023	0	87	theme	human	35:39	arg1	C					54:54	human chymotrypsin C	35:54	human chymotrypsin C	35:54	Asparagine-linked glycosylation of human chymotrypsin C is required for folding and secretion but not for enzyme activity.
21920023	5	88	from	glycan	879:884	arg1	Asn52					889:893	Asn52	889:893	Asn52	889:893	We found that human CTRC contains a single N-linked glycan on Asn52.
21920023	7	89	theme	N52S	1091:1094	arg1	mutant					1101:1106	the N52S CTRC mutant	1087:1106	the N52S CTRC mutant	1087:1106	Overexpression of the N52S CTRC mutant elicited endoplasmic reticulum stress in AR42J acinar cells, indicating that N-glycosylation is required for folding of human CTRC.
21920023	6	90	theme	HEK	997:999	arg1	cells					1006:1010	HEK 293T cells	997:1010	HEK 293T cells	997:1010	Elimination of N-glycosylation by mutation of Asn52 (N52S) reduced CTRC secretion about 10-fold from HEK 293T cells but had no effect on CTRC activity or inhibitor binding.
21920023	3	91	theme	N-linked	450:457	arg1	glycosylation					460:472	asparagine-linked (N-linked) glycosylation	431:472	asparagine-linked (N-linked) glycosylation	431:472	The aim of the present study was to determine whether human CTRC undergoes asparagine-linked (N-linked) glycosylation and to examine the role of this modification in CTRC folding and function.
21920023	7	92	theme	human	1228:1232	arg1	CTRC					1234:1237	human CTRC	1228:1237	human CTRC	1228:1237	Overexpression of the N52S CTRC mutant elicited endoplasmic reticulum stress in AR42J acinar cells, indicating that N-glycosylation is required for folding of human CTRC.
21920023	10	93	theme	N-linked	1647:1654	arg1	unimportant					1666:1676	unimportant	1666:1676	unimportant	1666:1676	We conclude that N-linked glycosylation of human CTRC is required for efficient folding and secretion; however, the N-linked glycan is unimportant for enzyme activity or inhibitor binding.
21920023	10	93	theme	N-linked	1647:1654	arg1	glycan					1656:1661	the N-linked glycan	1643:1661	the N-linked glycan	1643:1661	We conclude that N-linked glycosylation of human CTRC is required for efficient folding and secretion; however, the N-linked glycan is unimportant for enzyme activity or inhibitor binding.
21920023	5	94	link	N-linked	870:877	arg1	glycan					879:884	a single N-linked glycan	861:884	a single N-linked glycan on Asn52	861:893	We found that human CTRC contains a single N-linked glycan on Asn52.
21920023	1	95	theme	premature	205:213	arg1	activation					227:236	premature trypsinogen activation	205:236	premature trypsinogen activation	205:236	Human chymotrypsin C (CTRC) plays a protective role in the pancreas by mitigating premature trypsinogen activation through degradation.
21920023	10	96	theme	efficient	1601:1609	arg1	folding					1611:1617	efficient folding	1601:1617	efficient folding	1601:1617	We conclude that N-linked glycosylation of human CTRC is required for efficient folding and secretion; however, the N-linked glycan is unimportant for enzyme activity or inhibitor binding.
21920023	4	97	theme	glycosylation	770:782	arg1	state					784:788	their glycosylation state	764:788	their glycosylation state	764:788	We abolished potential sites of N-linked glycosylation (Asn-Xaa-Ser/Thr) in human CTRC by mutating the Asn residues to Ser individually or in combination, expressed the CTRC mutants in HEK 293T cells and determined their glycosylation state using PNGase F and endo H digestion.
21920023	3	98	theme	modification	506:517	arg1	role					493:496	the role	489:496	the role of this modification in CTRC folding and function	489:546	The aim of the present study was to determine whether human CTRC undergoes asparagine-linked (N-linked) glycosylation and to examine the role of this modification in CTRC folding and function.
20450227	10	0	theme	receptor	1878:1885	arg1	trafficking					1887:1897	receptor trafficking	1878:1897	receptor trafficking	1878:1897	This is the first report to map human P2X(7) glycosylation sites and reveal residue N187 is critical for receptor trafficking and function.
20450227	6	1	theme	pore	1097:1100	arg1	formation					1102:1110	pore formation	1097:1110	pore formation	1097:1110	Mutation of N187 results in weakened P2X(7) agonist-induced phosphorylation of ERK1/2, CREB, and p90 ribosomal S6 kinase, as well as a decreased level of pore formation.
20450227	3	2	theme	transcription	445:457	arg1	enzymes					472:478	enzymes	472:478	enzymes linked to the production of reactive oxygen species and interleukin-1 isoforms	472:557	Ligand binding to P2X(7) can stimulate ERK1/2, the transcription factor CREB, enzymes linked to the production of reactive oxygen species and interleukin-1 isoforms, and the formation of a nonspecific pore.
20450227	3	2	theme	transcription	445:457	arg1	CREB					466:469	the transcription factor CREB	441:469	the transcription factor CREB	441:469	Ligand binding to P2X(7) can stimulate ERK1/2, the transcription factor CREB, enzymes linked to the production of reactive oxygen species and interleukin-1 isoforms, and the formation of a nonspecific pore.
20450227	6	3	theme	CREB	1030:1033	arg1	phosphorylation					1003:1017	weakened P2X(7) agonist-induced phosphorylation	971:1017	weakened P2X(7) agonist-induced phosphorylation of ERK1/2, CREB, and p90 ribosomal S6 kinase, as well as a decreased level of pore formation	971:1110	Mutation of N187 results in weakened P2X(7) agonist-induced phosphorylation of ERK1/2, CREB, and p90 ribosomal S6 kinase, as well as a decreased level of pore formation.
20450227	9	4	theme	cell	1732:1735	arg1	expression					1745:1754	altered cell surface expression	1724:1754	altered cell surface expression of P2X(7) N187A	1724:1770	To address the mechanism whereby N187 mutation attenuates receptor activity, we developed a live cell proteinase K digestion assay that demonstrated altered cell surface expression of P2X(7) N187A.
20450227	6	5	theme	level	1088:1092	arg1	phosphorylation					1003:1017	weakened P2X(7) agonist-induced phosphorylation	971:1017	weakened P2X(7) agonist-induced phosphorylation of ERK1/2, CREB, and p90 ribosomal S6 kinase, as well as a decreased level of pore formation	971:1110	Mutation of N187 results in weakened P2X(7) agonist-induced phosphorylation of ERK1/2, CREB, and p90 ribosomal S6 kinase, as well as a decreased level of pore formation.
20450227	8	6	located	found	1455:1459	arg1	six					1464:1466	six	1464:1466	six	1464:1466	Interestingly, residue N187 belongs to an N-linked glycosylation consensus sequence found in six of the seven P2X family members, suggesting this site is fundamentally important to P2X receptor function.
20450227	8	6	located	found	1455:1459	arg1	members					1492:1498	the seven P2X family members	1471:1498	the seven P2X family members	1471:1498	Interestingly, residue N187 belongs to an N-linked glycosylation consensus sequence found in six of the seven P2X family members, suggesting this site is fundamentally important to P2X receptor function.
20450227	8	6	located	found	1455:1459	arg2	sequence					1446:1453	an N-linked glycosylation consensus sequence	1410:1453	an N-linked glycosylation consensus sequence found in six of the seven P2X family members	1410:1498	Interestingly, residue N187 belongs to an N-linked glycosylation consensus sequence found in six of the seven P2X family members, suggesting this site is fundamentally important to P2X receptor function.
20450227	7	7	theme	N-linked	1226:1233	arg1	tunicamycin					1269:1279	the N-linked glycosylation synthesis inhibitor tunicamycin	1222:1279	the N-linked glycosylation synthesis inhibitor tunicamycin	1222:1279	In further support of a role for glycosylation in receptor function, treatment of RAW 264.7 macrophages with the N-linked glycosylation synthesis inhibitor tunicamycin attenuates P2X(7) agonist-induced, but not phorbol ester-induced, ERK1/2 phosphorylation.
20450227	8	8	link	N-linked	1413:1420	arg1	sequence					1446:1453	an N-linked glycosylation consensus sequence	1410:1453	an N-linked glycosylation consensus sequence found in six of the seven P2X family members	1410:1498	Interestingly, residue N187 belongs to an N-linked glycosylation consensus sequence found in six of the seven P2X family members, suggesting this site is fundamentally important to P2X receptor function.
20450227	9	9	theme	P2X	1759:1761	arg1	expression					1745:1754	altered cell surface expression	1724:1754	altered cell surface expression of P2X(7) N187A	1724:1770	To address the mechanism whereby N187 mutation attenuates receptor activity, we developed a live cell proteinase K digestion assay that demonstrated altered cell surface expression of P2X(7) N187A.
20450227	2	10	theme	immune	271:276	arg1	monocytes					292:300	monocytes	292:300	monocytes	292:300	P2X(7) is expressed in immune cells such as monocytes and macrophages and is activated by extracellular ATP following tissue injury or infection.
20450227	2	10	theme	immune	271:276	arg1	macrophages					306:316	macrophages	306:316	macrophages	306:316	P2X(7) is expressed in immune cells such as monocytes and macrophages and is activated by extracellular ATP following tissue injury or infection.
20450227	2	10	theme	immune	271:276	arg1	cells					278:282	immune cells	271:282	immune cells such as monocytes and macrophages	271:316	P2X(7) is expressed in immune cells such as monocytes and macrophages and is activated by extracellular ATP following tissue injury or infection.
20450227	8	11	theme	receptor	1556:1563	arg1	function					1565:1572	P2X receptor function	1552:1572	P2X receptor function	1552:1572	Interestingly, residue N187 belongs to an N-linked glycosylation consensus sequence found in six of the seven P2X family members, suggesting this site is fundamentally important to P2X receptor function.
20450227	5	12	dep	appears	885:891	arg1	glycosylated					893:904	glycosylated	893:904	appears glycosylated at N187, N202, N213, N241, and N284	885:940	Here we provide evidence that P2X(7) is sensitive to the glycosidases EndoH and PNGase F and that the human receptor appears glycosylated at N187, N202, N213, N241, and N284.
20450227	0	13	theme	important	110:118	arg1	residue					102:108	a key residue	96:108	a key residue important for receptor function	96:140	Mutation of putative N-linked glycosylation sites on the human nucleotide receptor P2X7 reveals a key residue important for receptor function.
20450227	1	14	dep	potential	218:226	arg1	therapeutic					228:238	therapeutic	228:238	therapeutic	228:238	The nucleotide receptor P2X(7) is an immunomodulatory cation channel and a potential therapeutic target.
20450227	0	15	theme	receptor	124:131	arg1	function					133:140	receptor function	124:140	receptor function	124:140	Mutation of putative N-linked glycosylation sites on the human nucleotide receptor P2X7 reveals a key residue important for receptor function.
20450227	3	16	theme	interleukin-1	536:548	arg1	isoforms					550:557	interleukin-1 isoforms	536:557	interleukin-1 isoforms	536:557	Ligand binding to P2X(7) can stimulate ERK1/2, the transcription factor CREB, enzymes linked to the production of reactive oxygen species and interleukin-1 isoforms, and the formation of a nonspecific pore.
20450227	1	17	theme	cation	197:202	arg1	channel					204:210	an immunomodulatory cation channel	177:210	an immunomodulatory cation channel	177:210	The nucleotide receptor P2X(7) is an immunomodulatory cation channel and a potential therapeutic target.
20450227	1	17	theme	cation	197:202	arg1	P2X					167:169	The nucleotide receptor P2X	143:169	The nucleotide receptor P2X(7)	143:172	The nucleotide receptor P2X(7) is an immunomodulatory cation channel and a potential therapeutic target.
20450227	6	18	theme	kinase	1057:1062	arg1	phosphorylation					1003:1017	weakened P2X(7) agonist-induced phosphorylation	971:1017	weakened P2X(7) agonist-induced phosphorylation of ERK1/2, CREB, and p90 ribosomal S6 kinase, as well as a decreased level of pore formation	971:1110	Mutation of N187 results in weakened P2X(7) agonist-induced phosphorylation of ERK1/2, CREB, and p90 ribosomal S6 kinase, as well as a decreased level of pore formation.
20450227	3	19	theme	species	524:530	arg1	production					494:503	the production	490:503	the production of reactive oxygen species and interleukin-1 isoforms	490:557	Ligand binding to P2X(7) can stimulate ERK1/2, the transcription factor CREB, enzymes linked to the production of reactive oxygen species and interleukin-1 isoforms, and the formation of a nonspecific pore.
20450227	7	20	theme	receptor	1163:1170	arg1	function					1172:1179	receptor function	1163:1179	receptor function	1163:1179	In further support of a role for glycosylation in receptor function, treatment of RAW 264.7 macrophages with the N-linked glycosylation synthesis inhibitor tunicamycin attenuates P2X(7) agonist-induced, but not phorbol ester-induced, ERK1/2 phosphorylation.
20450227	6	21	theme	ribosomal	1044:1052	arg1	kinase					1057:1062	p90 ribosomal S6 kinase	1040:1062	p90 ribosomal S6 kinase	1040:1062	Mutation of N187 results in weakened P2X(7) agonist-induced phosphorylation of ERK1/2, CREB, and p90 ribosomal S6 kinase, as well as a decreased level of pore formation.
20450227	4	22	theme	P2X	652:654	arg1	biochemistry					636:647	the biochemistry	632:647	the biochemistry of P2X(7)	632:657	However, little is known about the biochemistry of P2X(7), including whether the receptor is N-linked glycosylated and if this modification affects receptor function.
20450227	7	23	theme	synthesis	1249:1257	arg1	tunicamycin					1269:1279	the N-linked glycosylation synthesis inhibitor tunicamycin	1222:1279	the N-linked glycosylation synthesis inhibitor tunicamycin	1222:1279	In further support of a role for glycosylation in receptor function, treatment of RAW 264.7 macrophages with the N-linked glycosylation synthesis inhibitor tunicamycin attenuates P2X(7) agonist-induced, but not phorbol ester-induced, ERK1/2 phosphorylation.
20450227	10	24	theme	P2X	1811:1813	arg1	sites					1832:1836	human P2X(7) glycosylation sites	1805:1836	human P2X(7) glycosylation sites	1805:1836	This is the first report to map human P2X(7) glycosylation sites and reveal residue N187 is critical for receptor trafficking and function.
20450227	0	25	theme	human	57:61	arg1	P2X7					83:86	the human nucleotide receptor P2X7	53:86	the human nucleotide receptor P2X7	53:86	Mutation of putative N-linked glycosylation sites on the human nucleotide receptor P2X7 reveals a key residue important for receptor function.
20450227	5	26	dep	glycosidases	825:836	arg1	glycosidases					825:836	the glycosidases EndoH and PNGase F	821:855	the glycosidases EndoH and PNGase F	821:855	Here we provide evidence that P2X(7) is sensitive to the glycosidases EndoH and PNGase F and that the human receptor appears glycosylated at N187, N202, N213, N241, and N284.
20450227	5	26	dep	glycosidases	825:836	arg1	EndoH					838:842	EndoH	838:842	EndoH	838:842	Here we provide evidence that P2X(7) is sensitive to the glycosidases EndoH and PNGase F and that the human receptor appears glycosylated at N187, N202, N213, N241, and N284.
20450227	5	26	dep	glycosidases	825:836	arg1	F					855:855	PNGase F	848:855	PNGase F	848:855	Here we provide evidence that P2X(7) is sensitive to the glycosidases EndoH and PNGase F and that the human receptor appears glycosylated at N187, N202, N213, N241, and N284.
20450227	0	27	theme	receptor	74:81	arg1	P2X7					83:86	the human nucleotide receptor P2X7	53:86	the human nucleotide receptor P2X7	53:86	Mutation of putative N-linked glycosylation sites on the human nucleotide receptor P2X7 reveals a key residue important for receptor function.
20450227	1	28	theme	receptor	158:165	arg1	7					171:171	7	171:171	7	171:171	The nucleotide receptor P2X(7) is an immunomodulatory cation channel and a potential therapeutic target.
20450227	1	28	theme	receptor	158:165	arg1	P2X					167:169	The nucleotide receptor P2X	143:169	The nucleotide receptor P2X(7)	143:172	The nucleotide receptor P2X(7) is an immunomodulatory cation channel and a potential therapeutic target.
20450227	1	28	theme	receptor	158:165	arg1	channel					204:210	an immunomodulatory cation channel	177:210	an immunomodulatory cation channel	177:210	The nucleotide receptor P2X(7) is an immunomodulatory cation channel and a potential therapeutic target.
20450227	7	29	link	N-linked	1226:1233	arg1	tunicamycin					1269:1279	the N-linked glycosylation synthesis inhibitor tunicamycin	1222:1279	the N-linked glycosylation synthesis inhibitor tunicamycin	1222:1279	In further support of a role for glycosylation in receptor function, treatment of RAW 264.7 macrophages with the N-linked glycosylation synthesis inhibitor tunicamycin attenuates P2X(7) agonist-induced, but not phorbol ester-induced, ERK1/2 phosphorylation.
20450227	0	30	from	Mutation	0:7	arg1	P2X7					83:86	the human nucleotide receptor P2X7	53:86	the human nucleotide receptor P2X7	53:86	Mutation of putative N-linked glycosylation sites on the human nucleotide receptor P2X7 reveals a key residue important for receptor function.
20450227	10	31	theme	glycosylation	1818:1830	arg1	sites					1832:1836	human P2X(7) glycosylation sites	1805:1836	human P2X(7) glycosylation sites	1805:1836	This is the first report to map human P2X(7) glycosylation sites and reveal residue N187 is critical for receptor trafficking and function.
20450227	7	32	with	treatment	1182:1190	arg1	tunicamycin					1269:1279	the N-linked glycosylation synthesis inhibitor tunicamycin	1222:1279	the N-linked glycosylation synthesis inhibitor tunicamycin	1222:1279	In further support of a role for glycosylation in receptor function, treatment of RAW 264.7 macrophages with the N-linked glycosylation synthesis inhibitor tunicamycin attenuates P2X(7) agonist-induced, but not phorbol ester-induced, ERK1/2 phosphorylation.
20450227	0	33	theme	key	98:100	arg1	residue					102:108	a key residue	96:108	a key residue important for receptor function	96:140	Mutation of putative N-linked glycosylation sites on the human nucleotide receptor P2X7 reveals a key residue important for receptor function.
20450227	9	34	theme	receptor	1633:1640	arg1	activity					1642:1649	receptor activity	1633:1649	receptor activity	1633:1649	To address the mechanism whereby N187 mutation attenuates receptor activity, we developed a live cell proteinase K digestion assay that demonstrated altered cell surface expression of P2X(7) N187A.
20450227	2	35	theme	extracellular	338:350	arg1	ATP					352:354	extracellular ATP	338:354	extracellular ATP	338:354	P2X(7) is expressed in immune cells such as monocytes and macrophages and is activated by extracellular ATP following tissue injury or infection.
20450227	0	36	theme	putative	12:19	arg1	sites					44:48	putative N-linked glycosylation sites	12:48	putative N-linked glycosylation sites	12:48	Mutation of putative N-linked glycosylation sites on the human nucleotide receptor P2X7 reveals a key residue important for receptor function.
20450227	6	37	theme	ERK1/2	1022:1027	arg1	phosphorylation					1003:1017	weakened P2X(7) agonist-induced phosphorylation	971:1017	weakened P2X(7) agonist-induced phosphorylation of ERK1/2, CREB, and p90 ribosomal S6 kinase, as well as a decreased level of pore formation	971:1110	Mutation of N187 results in weakened P2X(7) agonist-induced phosphorylation of ERK1/2, CREB, and p90 ribosomal S6 kinase, as well as a decreased level of pore formation.
20450227	5	38	theme	PNGase	848:853	arg1	glycosidases					825:836	the glycosidases EndoH and PNGase F	821:855	the glycosidases EndoH and PNGase F	821:855	Here we provide evidence that P2X(7) is sensitive to the glycosidases EndoH and PNGase F and that the human receptor appears glycosylated at N187, N202, N213, N241, and N284.
20450227	5	38	theme	PNGase	848:853	arg1	F					855:855	PNGase F	848:855	PNGase F	848:855	Here we provide evidence that P2X(7) is sensitive to the glycosidases EndoH and PNGase F and that the human receptor appears glycosylated at N187, N202, N213, N241, and N284.
20450227	3	39	theme	nonspecific	583:593	arg1	pore					595:598	a nonspecific pore	581:598	a nonspecific pore	581:598	Ligand binding to P2X(7) can stimulate ERK1/2, the transcription factor CREB, enzymes linked to the production of reactive oxygen species and interleukin-1 isoforms, and the formation of a nonspecific pore.
20450227	0	40	theme	glycosylation	30:42	arg1	sites					44:48	putative N-linked glycosylation sites	12:48	putative N-linked glycosylation sites	12:48	Mutation of putative N-linked glycosylation sites on the human nucleotide receptor P2X7 reveals a key residue important for receptor function.
20450227	5	41	gly	glycosylated	893:904	arg2	N202					915:918	N202	915:918	N202	915:918	Here we provide evidence that P2X(7) is sensitive to the glycosidases EndoH and PNGase F and that the human receptor appears glycosylated at N187, N202, N213, N241, and N284.
20450227	5	41	gly	glycosylated	893:904	arg2	N187					909:912	N187	909:912	N187	909:912	Here we provide evidence that P2X(7) is sensitive to the glycosidases EndoH and PNGase F and that the human receptor appears glycosylated at N187, N202, N213, N241, and N284.
20450227	5	41	gly	glycosylated	893:904	arg2	N284					937:940	N284	937:940	N284	937:940	Here we provide evidence that P2X(7) is sensitive to the glycosidases EndoH and PNGase F and that the human receptor appears glycosylated at N187, N202, N213, N241, and N284.
20450227	5	41	gly	glycosylated	893:904	arg2	N241					927:930	N241	927:930	N241	927:930	Here we provide evidence that P2X(7) is sensitive to the glycosidases EndoH and PNGase F and that the human receptor appears glycosylated at N187, N202, N213, N241, and N284.
20450227	5	41	gly	glycosylated	893:904	arg2	N213					921:924	N213	921:924	N213	921:924	Here we provide evidence that P2X(7) is sensitive to the glycosidases EndoH and PNGase F and that the human receptor appears glycosylated at N187, N202, N213, N241, and N284.
20450227	10	42	gly	glycosylation	1818:1830	arg2	sites					1832:1836	human P2X(7) glycosylation sites	1805:1836	human P2X(7) glycosylation sites	1805:1836	This is the first report to map human P2X(7) glycosylation sites and reveal residue N187 is critical for receptor trafficking and function.
20450227	6	43	theme	P2X	980:982	arg1	phosphorylation					1003:1017	weakened P2X(7) agonist-induced phosphorylation	971:1017	weakened P2X(7) agonist-induced phosphorylation of ERK1/2, CREB, and p90 ribosomal S6 kinase, as well as a decreased level of pore formation	971:1110	Mutation of N187 results in weakened P2X(7) agonist-induced phosphorylation of ERK1/2, CREB, and p90 ribosomal S6 kinase, as well as a decreased level of pore formation.
20450227	9	44	theme	proteinase	1677:1686	arg1	assay					1700:1704	a live cell proteinase K digestion assay	1665:1704	a live cell proteinase K digestion assay that demonstrated altered cell surface expression of P2X(7) N187A	1665:1770	To address the mechanism whereby N187 mutation attenuates receptor activity, we developed a live cell proteinase K digestion assay that demonstrated altered cell surface expression of P2X(7) N187A.
20450227	9	45	theme	digestion	1690:1698	arg1	assay					1700:1704	a live cell proteinase K digestion assay	1665:1704	a live cell proteinase K digestion assay that demonstrated altered cell surface expression of P2X(7) N187A	1665:1770	To address the mechanism whereby N187 mutation attenuates receptor activity, we developed a live cell proteinase K digestion assay that demonstrated altered cell surface expression of P2X(7) N187A.
20450227	8	46	theme	glycosylation	1422:1434	arg1	sequence					1446:1453	an N-linked glycosylation consensus sequence	1410:1453	an N-linked glycosylation consensus sequence found in six of the seven P2X family members	1410:1498	Interestingly, residue N187 belongs to an N-linked glycosylation consensus sequence found in six of the seven P2X family members, suggesting this site is fundamentally important to P2X receptor function.
20450227	3	47	theme	factor	459:464	arg1	enzymes					472:478	enzymes	472:478	enzymes linked to the production of reactive oxygen species and interleukin-1 isoforms	472:557	Ligand binding to P2X(7) can stimulate ERK1/2, the transcription factor CREB, enzymes linked to the production of reactive oxygen species and interleukin-1 isoforms, and the formation of a nonspecific pore.
20450227	3	47	theme	factor	459:464	arg1	CREB					466:469	the transcription factor CREB	441:469	the transcription factor CREB	441:469	Ligand binding to P2X(7) can stimulate ERK1/2, the transcription factor CREB, enzymes linked to the production of reactive oxygen species and interleukin-1 isoforms, and the formation of a nonspecific pore.
20450227	8	48	theme	family	1485:1490	arg1	members					1492:1498	the seven P2X family members	1471:1498	the seven P2X family members	1471:1498	Interestingly, residue N187 belongs to an N-linked glycosylation consensus sequence found in six of the seven P2X family members, suggesting this site is fundamentally important to P2X receptor function.
20450227	9	49	theme	live	1667:1670	arg1	assay					1700:1704	a live cell proteinase K digestion assay	1665:1704	a live cell proteinase K digestion assay that demonstrated altered cell surface expression of P2X(7) N187A	1665:1770	To address the mechanism whereby N187 mutation attenuates receptor activity, we developed a live cell proteinase K digestion assay that demonstrated altered cell surface expression of P2X(7) N187A.
20450227	7	50	theme	agonist-induced	1299:1313	arg1	phosphorylation					1354:1368	P2X(7) agonist-induced, but not phorbol ester-induced, ERK1/2 phosphorylation	1292:1368	P2X(7) agonist-induced, but not phorbol ester-induced, ERK1/2 phosphorylation	1292:1368	In further support of a role for glycosylation in receptor function, treatment of RAW 264.7 macrophages with the N-linked glycosylation synthesis inhibitor tunicamycin attenuates P2X(7) agonist-induced, but not phorbol ester-induced, ERK1/2 phosphorylation.
20450227	7	51	from	role	1137:1140	arg1	function					1172:1179	receptor function	1163:1179	receptor function	1163:1179	In further support of a role for glycosylation in receptor function, treatment of RAW 264.7 macrophages with the N-linked glycosylation synthesis inhibitor tunicamycin attenuates P2X(7) agonist-induced, but not phorbol ester-induced, ERK1/2 phosphorylation.
20450227	6	52	theme	N187	955:958	arg1	Mutation					943:950	Mutation	943:950	Mutation of N187	943:958	Mutation of N187 results in weakened P2X(7) agonist-induced phosphorylation of ERK1/2, CREB, and p90 ribosomal S6 kinase, as well as a decreased level of pore formation.
20450227	6	53	theme	formation	1102:1110	arg1	ERK1/2					1022:1027	ERK1/2	1022:1027	ERK1/2	1022:1027	Mutation of N187 results in weakened P2X(7) agonist-induced phosphorylation of ERK1/2, CREB, and p90 ribosomal S6 kinase, as well as a decreased level of pore formation.
20450227	6	53	theme	formation	1102:1110	arg1	CREB					1030:1033	CREB	1030:1033	CREB	1030:1033	Mutation of N187 results in weakened P2X(7) agonist-induced phosphorylation of ERK1/2, CREB, and p90 ribosomal S6 kinase, as well as a decreased level of pore formation.
20450227	6	53	theme	formation	1102:1110	arg1	level					1088:1092	a decreased level	1076:1092	a decreased level of pore formation	1076:1110	Mutation of N187 results in weakened P2X(7) agonist-induced phosphorylation of ERK1/2, CREB, and p90 ribosomal S6 kinase, as well as a decreased level of pore formation.
20450227	6	53	theme	formation	1102:1110	arg1	kinase					1057:1062	p90 ribosomal S6 kinase	1040:1062	p90 ribosomal S6 kinase	1040:1062	Mutation of N187 results in weakened P2X(7) agonist-induced phosphorylation of ERK1/2, CREB, and p90 ribosomal S6 kinase, as well as a decreased level of pore formation.
20450227	0	54	link	N-linked	21:28	arg1	sites					44:48	putative N-linked glycosylation sites	12:48	putative N-linked glycosylation sites	12:48	Mutation of putative N-linked glycosylation sites on the human nucleotide receptor P2X7 reveals a key residue important for receptor function.
20450227	9	55	theme	altered	1724:1730	arg1	expression					1745:1754	altered cell surface expression	1724:1754	altered cell surface expression of P2X(7) N187A	1724:1770	To address the mechanism whereby N187 mutation attenuates receptor activity, we developed a live cell proteinase K digestion assay that demonstrated altered cell surface expression of P2X(7) N187A.
20450227	7	56	theme	inhibitor	1259:1267	arg1	tunicamycin					1269:1279	the N-linked glycosylation synthesis inhibitor tunicamycin	1222:1279	the N-linked glycosylation synthesis inhibitor tunicamycin	1222:1279	In further support of a role for glycosylation in receptor function, treatment of RAW 264.7 macrophages with the N-linked glycosylation synthesis inhibitor tunicamycin attenuates P2X(7) agonist-induced, but not phorbol ester-induced, ERK1/2 phosphorylation.
20450227	9	57	theme	surface	1737:1743	arg1	expression					1745:1754	altered cell surface expression	1724:1754	altered cell surface expression of P2X(7) N187A	1724:1770	To address the mechanism whereby N187 mutation attenuates receptor activity, we developed a live cell proteinase K digestion assay that demonstrated altered cell surface expression of P2X(7) N187A.
20450227	6	58	theme	decreased	1078:1086	arg1	level					1088:1092	a decreased level	1076:1092	a decreased level of pore formation	1076:1110	Mutation of N187 results in weakened P2X(7) agonist-induced phosphorylation of ERK1/2, CREB, and p90 ribosomal S6 kinase, as well as a decreased level of pore formation.
20450227	4	59	theme	receptor	749:756	arg1	function					758:765	receptor function	749:765	receptor function	749:765	However, little is known about the biochemistry of P2X(7), including whether the receptor is N-linked glycosylated and if this modification affects receptor function.
20450227	7	60	theme	glycosylation	1235:1247	arg1	tunicamycin					1269:1279	the N-linked glycosylation synthesis inhibitor tunicamycin	1222:1279	the N-linked glycosylation synthesis inhibitor tunicamycin	1222:1279	In further support of a role for glycosylation in receptor function, treatment of RAW 264.7 macrophages with the N-linked glycosylation synthesis inhibitor tunicamycin attenuates P2X(7) agonist-induced, but not phorbol ester-induced, ERK1/2 phosphorylation.
20450227	6	61	theme	agonist-induced	987:1001	arg1	phosphorylation					1003:1017	weakened P2X(7) agonist-induced phosphorylation	971:1017	weakened P2X(7) agonist-induced phosphorylation of ERK1/2, CREB, and p90 ribosomal S6 kinase, as well as a decreased level of pore formation	971:1110	Mutation of N187 results in weakened P2X(7) agonist-induced phosphorylation of ERK1/2, CREB, and p90 ribosomal S6 kinase, as well as a decreased level of pore formation.
20450227	8	62	theme	P2X	1552:1554	arg1	function					1565:1572	P2X receptor function	1552:1572	P2X receptor function	1552:1572	Interestingly, residue N187 belongs to an N-linked glycosylation consensus sequence found in six of the seven P2X family members, suggesting this site is fundamentally important to P2X receptor function.
20450227	3	63	theme	reactive	508:515	arg1	species					524:530	reactive oxygen species	508:530	reactive oxygen species	508:530	Ligand binding to P2X(7) can stimulate ERK1/2, the transcription factor CREB, enzymes linked to the production of reactive oxygen species and interleukin-1 isoforms, and the formation of a nonspecific pore.
20450227	7	64	theme	macrophages	1205:1215	arg1	treatment					1182:1190	treatment	1182:1190	treatment of RAW 264.7 macrophages with the N-linked glycosylation synthesis inhibitor tunicamycin	1182:1279	In further support of a role for glycosylation in receptor function, treatment of RAW 264.7 macrophages with the N-linked glycosylation synthesis inhibitor tunicamycin attenuates P2X(7) agonist-induced, but not phorbol ester-induced, ERK1/2 phosphorylation.
20450227	1	65	theme	immunomodulatory	180:195	arg1	channel					204:210	an immunomodulatory cation channel	177:210	an immunomodulatory cation channel	177:210	The nucleotide receptor P2X(7) is an immunomodulatory cation channel and a potential therapeutic target.
20450227	1	65	theme	immunomodulatory	180:195	arg1	P2X					167:169	The nucleotide receptor P2X	143:169	The nucleotide receptor P2X(7)	143:172	The nucleotide receptor P2X(7) is an immunomodulatory cation channel and a potential therapeutic target.
20450227	7	66	theme	RAW	1195:1197	arg1	macrophages					1205:1215	RAW 264.7 macrophages	1195:1215	RAW 264.7 macrophages	1195:1215	In further support of a role for glycosylation in receptor function, treatment of RAW 264.7 macrophages with the N-linked glycosylation synthesis inhibitor tunicamycin attenuates P2X(7) agonist-induced, but not phorbol ester-induced, ERK1/2 phosphorylation.
20450227	3	67	theme	oxygen	517:522	arg1	species					524:530	reactive oxygen species	508:530	reactive oxygen species	508:530	Ligand binding to P2X(7) can stimulate ERK1/2, the transcription factor CREB, enzymes linked to the production of reactive oxygen species and interleukin-1 isoforms, and the formation of a nonspecific pore.
20450227	6	68	theme	S6	1054:1055	arg1	kinase					1057:1062	p90 ribosomal S6 kinase	1040:1062	p90 ribosomal S6 kinase	1040:1062	Mutation of N187 results in weakened P2X(7) agonist-induced phosphorylation of ERK1/2, CREB, and p90 ribosomal S6 kinase, as well as a decreased level of pore formation.
20450227	10	69	theme	first	1785:1789	arg1	report					1791:1796	the first report	1781:1796	the first report to map human P2X(7) glycosylation sites and reveal residue N187 is critical for receptor trafficking and function	1781:1910	This is the first report to map human P2X(7) glycosylation sites and reveal residue N187 is critical for receptor trafficking and function.
20450227	10	69	theme	first	1785:1789	arg1	This					1773:1776	This	1773:1776	This	1773:1776	This is the first report to map human P2X(7) glycosylation sites and reveal residue N187 is critical for receptor trafficking and function.
20450227	0	70	gly	glycosylation	30:42	arg2	sites					44:48	putative N-linked glycosylation sites	12:48	putative N-linked glycosylation sites	12:48	Mutation of putative N-linked glycosylation sites on the human nucleotide receptor P2X7 reveals a key residue important for receptor function.
20450227	6	71	theme	p90	1040:1042	arg1	kinase					1057:1062	p90 ribosomal S6 kinase	1040:1062	p90 ribosomal S6 kinase	1040:1062	Mutation of N187 results in weakened P2X(7) agonist-induced phosphorylation of ERK1/2, CREB, and p90 ribosomal S6 kinase, as well as a decreased level of pore formation.
20450227	0	72	theme	nucleotide	63:72	arg1	P2X7					83:86	the human nucleotide receptor P2X7	53:86	the human nucleotide receptor P2X7	53:86	Mutation of putative N-linked glycosylation sites on the human nucleotide receptor P2X7 reveals a key residue important for receptor function.
20450227	3	73	theme	isoforms	550:557	arg1	production					494:503	the production	490:503	the production of reactive oxygen species and interleukin-1 isoforms	490:557	Ligand binding to P2X(7) can stimulate ERK1/2, the transcription factor CREB, enzymes linked to the production of reactive oxygen species and interleukin-1 isoforms, and the formation of a nonspecific pore.
20450227	10	74	dep	report	1791:1796	arg1	reveal					1842:1847	reveal	1842:1847	reveal residue N187 is critical for receptor trafficking and function	1842:1910	This is the first report to map human P2X(7) glycosylation sites and reveal residue N187 is critical for receptor trafficking and function.
20450227	10	74	dep	report	1791:1796	arg1	map					1801:1803	map	1801:1803	to map human P2X(7) glycosylation sites	1798:1836	This is the first report to map human P2X(7) glycosylation sites and reveal residue N187 is critical for receptor trafficking and function.
20450227	10	75	theme	human	1805:1809	arg1	7					1815:1815	7	1815:1815	7	1815:1815	This is the first report to map human P2X(7) glycosylation sites and reveal residue N187 is critical for receptor trafficking and function.
20450227	10	75	theme	human	1805:1809	arg1	P2X					1811:1813	human P2X	1805:1813	human P2X(7) glycosylation sites	1805:1836	This is the first report to map human P2X(7) glycosylation sites and reveal residue N187 is critical for receptor trafficking and function.
20450227	1	76	theme	nucleotide	147:156	arg1	7					171:171	7	171:171	7	171:171	The nucleotide receptor P2X(7) is an immunomodulatory cation channel and a potential therapeutic target.
20450227	1	76	theme	nucleotide	147:156	arg1	P2X					167:169	The nucleotide receptor P2X	143:169	The nucleotide receptor P2X(7)	143:172	The nucleotide receptor P2X(7) is an immunomodulatory cation channel and a potential therapeutic target.
20450227	1	76	theme	nucleotide	147:156	arg1	channel					204:210	an immunomodulatory cation channel	177:210	an immunomodulatory cation channel	177:210	The nucleotide receptor P2X(7) is an immunomodulatory cation channel and a potential therapeutic target.
20450227	9	77	theme	N187	1608:1611	arg1	mutation					1613:1620	N187 mutation	1608:1620	N187 mutation	1608:1620	To address the mechanism whereby N187 mutation attenuates receptor activity, we developed a live cell proteinase K digestion assay that demonstrated altered cell surface expression of P2X(7) N187A.
20450227	7	78	theme	role	1137:1140	arg1	support					1124:1130	further support	1116:1130	further support of a role for glycosylation in receptor function	1116:1179	In further support of a role for glycosylation in receptor function, treatment of RAW 264.7 macrophages with the N-linked glycosylation synthesis inhibitor tunicamycin attenuates P2X(7) agonist-induced, but not phorbol ester-induced, ERK1/2 phosphorylation.
20450227	7	79	from	function	1172:1179	arg1	support					1124:1130	further support	1116:1130	further support of a role for glycosylation in receptor function	1116:1179	In further support of a role for glycosylation in receptor function, treatment of RAW 264.7 macrophages with the N-linked glycosylation synthesis inhibitor tunicamycin attenuates P2X(7) agonist-induced, but not phorbol ester-induced, ERK1/2 phosphorylation.
20450227	3	80	theme	Ligand	394:399	arg1	binding					401:407	Ligand binding	394:407	Ligand binding to P2X(7)	394:417	Ligand binding to P2X(7) can stimulate ERK1/2, the transcription factor CREB, enzymes linked to the production of reactive oxygen species and interleukin-1 isoforms, and the formation of a nonspecific pore.
20450227	0	81	theme	N-linked	21:28	arg1	sites					44:48	putative N-linked glycosylation sites	12:48	putative N-linked glycosylation sites	12:48	Mutation of putative N-linked glycosylation sites on the human nucleotide receptor P2X7 reveals a key residue important for receptor function.
20450227	3	82	attach	linked	480:485	arg2	CREB					466:469	the transcription factor CREB	441:469	the transcription factor CREB	441:469	Ligand binding to P2X(7) can stimulate ERK1/2, the transcription factor CREB, enzymes linked to the production of reactive oxygen species and interleukin-1 isoforms, and the formation of a nonspecific pore.
20450227	3	82	attach	linked	480:485	arg1	production					494:503	the production	490:503	the production of reactive oxygen species and interleukin-1 isoforms	490:557	Ligand binding to P2X(7) can stimulate ERK1/2, the transcription factor CREB, enzymes linked to the production of reactive oxygen species and interleukin-1 isoforms, and the formation of a nonspecific pore.
20450227	3	82	attach	linked	480:485	arg2	enzymes					472:478	enzymes	472:478	enzymes linked to the production of reactive oxygen species and interleukin-1 isoforms	472:557	Ligand binding to P2X(7) can stimulate ERK1/2, the transcription factor CREB, enzymes linked to the production of reactive oxygen species and interleukin-1 isoforms, and the formation of a nonspecific pore.
20450227	7	83	theme	further	1116:1122	arg1	support					1124:1130	further support	1116:1130	further support of a role for glycosylation in receptor function	1116:1179	In further support of a role for glycosylation in receptor function, treatment of RAW 264.7 macrophages with the N-linked glycosylation synthesis inhibitor tunicamycin attenuates P2X(7) agonist-induced, but not phorbol ester-induced, ERK1/2 phosphorylation.
20450227	0	84	theme	sites	44:48	arg1	Mutation					0:7	Mutation	0:7	Mutation of putative N-linked glycosylation sites on the human nucleotide receptor P2X7	0:86	Mutation of putative N-linked glycosylation sites on the human nucleotide receptor P2X7 reveals a key residue important for receptor function.
20450227	2	85	theme	tissue	366:371	arg1	injury					373:378	tissue injury	366:378	tissue injury	366:378	P2X(7) is expressed in immune cells such as monocytes and macrophages and is activated by extracellular ATP following tissue injury or infection.
20450227	4	86	gly	glycosylated	703:714	arg1	receptor					682:689	the receptor	678:689	the receptor	678:689	However, little is known about the biochemistry of P2X(7), including whether the receptor is N-linked glycosylated and if this modification affects receptor function.
20450227	7	87	theme	ERK1/2	1347:1352	arg1	phosphorylation					1354:1368	P2X(7) agonist-induced, but not phorbol ester-induced, ERK1/2 phosphorylation	1292:1368	P2X(7) agonist-induced, but not phorbol ester-induced, ERK1/2 phosphorylation	1292:1368	In further support of a role for glycosylation in receptor function, treatment of RAW 264.7 macrophages with the N-linked glycosylation synthesis inhibitor tunicamycin attenuates P2X(7) agonist-induced, but not phorbol ester-induced, ERK1/2 phosphorylation.
20450227	9	88	theme	cell	1672:1675	arg1	assay					1700:1704	a live cell proteinase K digestion assay	1665:1704	a live cell proteinase K digestion assay that demonstrated altered cell surface expression of P2X(7) N187A	1665:1770	To address the mechanism whereby N187 mutation attenuates receptor activity, we developed a live cell proteinase K digestion assay that demonstrated altered cell surface expression of P2X(7) N187A.
20450227	8	89	theme	N-linked	1413:1420	arg1	sequence					1446:1453	an N-linked glycosylation consensus sequence	1410:1453	an N-linked glycosylation consensus sequence found in six of the seven P2X family members	1410:1498	Interestingly, residue N187 belongs to an N-linked glycosylation consensus sequence found in six of the seven P2X family members, suggesting this site is fundamentally important to P2X receptor function.
20450227	8	90	theme	P2X	1481:1483	arg1	members					1492:1498	the seven P2X family members	1471:1498	the seven P2X family members	1471:1498	Interestingly, residue N187 belongs to an N-linked glycosylation consensus sequence found in six of the seven P2X family members, suggesting this site is fundamentally important to P2X receptor function.
20450227	7	91	theme	ester-induced	1332:1344	arg1	phosphorylation					1354:1368	P2X(7) agonist-induced, but not phorbol ester-induced, ERK1/2 phosphorylation	1292:1368	P2X(7) agonist-induced, but not phorbol ester-induced, ERK1/2 phosphorylation	1292:1368	In further support of a role for glycosylation in receptor function, treatment of RAW 264.7 macrophages with the N-linked glycosylation synthesis inhibitor tunicamycin attenuates P2X(7) agonist-induced, but not phorbol ester-induced, ERK1/2 phosphorylation.
20450227	5	92	theme	human	870:874	arg1	receptor					876:883	the human receptor	866:883	the human receptor	866:883	Here we provide evidence that P2X(7) is sensitive to the glycosidases EndoH and PNGase F and that the human receptor appears glycosylated at N187, N202, N213, N241, and N284.
20450227	7	93	from	support	1124:1130	arg1	function					1172:1179	receptor function	1163:1179	receptor function	1163:1179	In further support of a role for glycosylation in receptor function, treatment of RAW 264.7 macrophages with the N-linked glycosylation synthesis inhibitor tunicamycin attenuates P2X(7) agonist-induced, but not phorbol ester-induced, ERK1/2 phosphorylation.
20450227	6	94	theme	weakened	971:978	arg1	phosphorylation					1003:1017	weakened P2X(7) agonist-induced phosphorylation	971:1017	weakened P2X(7) agonist-induced phosphorylation of ERK1/2, CREB, and p90 ribosomal S6 kinase, as well as a decreased level of pore formation	971:1110	Mutation of N187 results in weakened P2X(7) agonist-induced phosphorylation of ERK1/2, CREB, and p90 ribosomal S6 kinase, as well as a decreased level of pore formation.
20450227	9	95	theme	K	1688:1688	arg1	assay					1700:1704	a live cell proteinase K digestion assay	1665:1704	a live cell proteinase K digestion assay that demonstrated altered cell surface expression of P2X(7) N187A	1665:1770	To address the mechanism whereby N187 mutation attenuates receptor activity, we developed a live cell proteinase K digestion assay that demonstrated altered cell surface expression of P2X(7) N187A.
20450227	8	96	theme	consensus	1436:1444	arg1	sequence					1446:1453	an N-linked glycosylation consensus sequence	1410:1453	an N-linked glycosylation consensus sequence found in six of the seven P2X family members	1410:1498	Interestingly, residue N187 belongs to an N-linked glycosylation consensus sequence found in six of the seven P2X family members, suggesting this site is fundamentally important to P2X receptor function.
20450227	3	97	theme	pore	595:598	arg1	ERK1/2					433:438	ERK1/2	433:438	ERK1/2	433:438	Ligand binding to P2X(7) can stimulate ERK1/2, the transcription factor CREB, enzymes linked to the production of reactive oxygen species and interleukin-1 isoforms, and the formation of a nonspecific pore.
20450227	3	97	theme	pore	595:598	arg1	formation					568:576	the formation	564:576	the formation of a nonspecific pore	564:598	Ligand binding to P2X(7) can stimulate ERK1/2, the transcription factor CREB, enzymes linked to the production of reactive oxygen species and interleukin-1 isoforms, and the formation of a nonspecific pore.
20450227	3	97	theme	pore	595:598	arg1	enzymes					472:478	enzymes	472:478	enzymes linked to the production of reactive oxygen species and interleukin-1 isoforms	472:557	Ligand binding to P2X(7) can stimulate ERK1/2, the transcription factor CREB, enzymes linked to the production of reactive oxygen species and interleukin-1 isoforms, and the formation of a nonspecific pore.
20450227	3	97	theme	pore	595:598	arg1	CREB					466:469	the transcription factor CREB	441:469	the transcription factor CREB	441:469	Ligand binding to P2X(7) can stimulate ERK1/2, the transcription factor CREB, enzymes linked to the production of reactive oxygen species and interleukin-1 isoforms, and the formation of a nonspecific pore.
20450227	8	98	theme	members	1492:1498	arg1	six					1464:1466	six	1464:1466	six	1464:1466	Interestingly, residue N187 belongs to an N-linked glycosylation consensus sequence found in six of the seven P2X family members, suggesting this site is fundamentally important to P2X receptor function.
20450227	8	98	theme	members	1492:1498	arg1	members					1492:1498	the seven P2X family members	1471:1498	the seven P2X family members	1471:1498	Interestingly, residue N187 belongs to an N-linked glycosylation consensus sequence found in six of the seven P2X family members, suggesting this site is fundamentally important to P2X receptor function.
20450227	1	99	theme	potential	218:226	arg1	target					240:245	a potential therapeutic target	216:245	a potential therapeutic target	216:245	The nucleotide receptor P2X(7) is an immunomodulatory cation channel and a potential therapeutic target.
25153361	0	0	theme	glycosylation	38:50	arg1	assignment					10:19	Confident assignment	0:19	Confident assignment of site-specific glycosylation in complex glycoproteins in a single step	0:92	Confident assignment of site-specific glycosylation in complex glycoproteins in a single step.
25153361	2	1	theme	searching	372:380	arg1	workflows					382:390	typical reversed-phase LC-MS and bottom-up proteomics database searching workflows	309:390	typical reversed-phase LC-MS and bottom-up proteomics database searching workflows	309:390	As a consequence of glycoform diversity and signal suppression from nonglycosylated peptides that ionize more efficiently, typical reversed-phase LC-MS and bottom-up proteomics database searching workflows do not perform well for identification of site-specific glycosylation for complex glycoproteins.
25153361	7	2	theme	product	1149:1155	arg1	ions					1157:1160	product ions	1149:1160	product ions from both glycan and peptide backbone dissociation for a majority of the glycopeptides tested using collisionally activated dissociation that served to confidently assign site-specific glycosylation	1149:1359	The tandem mass spectra exhibited product ions from both glycan and peptide backbone dissociation for a majority of the glycopeptides tested using collisionally activated dissociation that served to confidently assign site-specific glycosylation.
25153361	3	3	from	analysis	548:555	arg1	glycoproteins					587:599	complex glycoproteins	579:599	complex glycoproteins (>4 N-glycosylation sequons) in a single step	579:645	We present an LC-MS system for enrichment, separation, and analysis of glycopeptides from complex glycoproteins (>4 N-glycosylation sequons) in a single step.
25153361	3	3	from	analysis	548:555	arg1	sequons					621:627	>4 N-glycosylation sequons	602:627	>4 N-glycosylation sequons	602:627	We present an LC-MS system for enrichment, separation, and analysis of glycopeptides from complex glycoproteins (>4 N-glycosylation sequons) in a single step.
25153361	3	4	gly	glycoproteins	587:599	arg1	glycoproteins					587:599	complex glycoproteins	579:599	complex glycoproteins (>4 N-glycosylation sequons) in a single step	579:645	We present an LC-MS system for enrichment, separation, and analysis of glycopeptides from complex glycoproteins (>4 N-glycosylation sequons) in a single step.
25153361	3	4	gly	glycoproteins	587:599	arg1	sequons					621:627	>4 N-glycosylation sequons	602:627	>4 N-glycosylation sequons	602:627	We present an LC-MS system for enrichment, separation, and analysis of glycopeptides from complex glycoproteins (>4 N-glycosylation sequons) in a single step.
25153361	6	5	gly	glycopeptides	980:992	arg2	glycopeptides					980:992	glycopeptides the most abundant ions	980:1015	glycopeptides the most abundant ions detected	980:1024	The online enrichment renders glycopeptides the most abundant ions detected, thereby facilitating the generation of high-quality data-dependent tandem mass spectra.
25153361	7	6	theme	tandem	1119:1124	arg1	spectra					1131:1137	The tandem mass spectra	1115:1137	The tandem mass spectra	1115:1137	The tandem mass spectra exhibited product ions from both glycan and peptide backbone dissociation for a majority of the glycopeptides tested using collisionally activated dissociation that served to confidently assign site-specific glycosylation.
25153361	2	7	theme	reversed-phase	317:330	arg1	LC-MS					332:336	typical reversed-phase LC-MS	309:336	typical reversed-phase LC-MS	309:336	As a consequence of glycoform diversity and signal suppression from nonglycosylated peptides that ionize more efficiently, typical reversed-phase LC-MS and bottom-up proteomics database searching workflows do not perform well for identification of site-specific glycosylation for complex glycoproteins.
25153361	5	8	theme	alpha-1-acid	862:873	arg1	glycoprotein					875:886	human alpha-1-acid glycoprotein	856:886	human alpha-1-acid glycoprotein (5 sequons)	856:898	We demonstrated the effectiveness of the system using a set of glycoproteins including human transferrin (2 sequons), human alpha-1-acid glycoprotein (5 sequons), and influenza A virus hemagglutinin (9 sequons).
25153361	5	8	theme	alpha-1-acid	862:873	arg1	sequons					891:897	5 sequons	889:897	5 sequons	889:897	We demonstrated the effectiveness of the system using a set of glycoproteins including human transferrin (2 sequons), human alpha-1-acid glycoprotein (5 sequons), and influenza A virus hemagglutinin (9 sequons).
25153361	4	9	theme	HILIC	675:679	arg1	trap					692:695	an online HILIC enrichment trap	665:695	an online HILIC enrichment trap prior to reversed-phase C18-MS analysis	665:735	This system uses an online HILIC enrichment trap prior to reversed-phase C18-MS analysis.
25153361	3	10	theme	single	635:640	arg1	step					642:645	a single step	633:645	a single step	633:645	We present an LC-MS system for enrichment, separation, and analysis of glycopeptides from complex glycoproteins (>4 N-glycosylation sequons) in a single step.
25153361	1	11	gly	glycosylation	139:151	arg2	glycosylation					139:151	glycosylation	139:151	glycosylation	139:151	A glycoprotein may contain several sites of glycosylation, each of which is heterogeneous.
25153361	1	11	gly	glycosylation	139:151	arg2	sites					130:134	several sites	122:134	several sites	122:134	A glycoprotein may contain several sites of glycosylation, each of which is heterogeneous.
25153361	2	12	theme	glycoform	206:214	arg1	diversity					216:224	glycoform diversity	206:224	glycoform diversity	206:224	As a consequence of glycoform diversity and signal suppression from nonglycosylated peptides that ionize more efficiently, typical reversed-phase LC-MS and bottom-up proteomics database searching workflows do not perform well for identification of site-specific glycosylation for complex glycoproteins.
25153361	1	13	theme	several	122:128	arg1	sites					130:134	several sites	122:134	several sites	122:134	A glycoprotein may contain several sites of glycosylation, each of which is heterogeneous.
25153361	1	13	theme	several	122:128	arg1	glycosylation					139:151	glycosylation	139:151	glycosylation	139:151	A glycoprotein may contain several sites of glycosylation, each of which is heterogeneous.
25153361	2	14	theme	nonglycosylated	254:268	arg1	peptides					270:277	nonglycosylated peptides	254:277	nonglycosylated peptides that ionize more efficiently	254:306	As a consequence of glycoform diversity and signal suppression from nonglycosylated peptides that ionize more efficiently, typical reversed-phase LC-MS and bottom-up proteomics database searching workflows do not perform well for identification of site-specific glycosylation for complex glycoproteins.
25153361	6	15	dep	glycopeptides	980:992	arg1	ions					1012:1015	the most abundant ions	994:1015	glycopeptides the most abundant ions detected	980:1024	The online enrichment renders glycopeptides the most abundant ions detected, thereby facilitating the generation of high-quality data-dependent tandem mass spectra.
25153361	4	16	theme	C18-MS	721:726	arg1	analysis					728:735	reversed-phase C18-MS analysis	706:735	reversed-phase C18-MS analysis	706:735	This system uses an online HILIC enrichment trap prior to reversed-phase C18-MS analysis.
25153361	7	17	theme	activated	1276:1284	arg1	dissociation					1286:1297	collisionally activated dissociation	1262:1297	collisionally activated dissociation that served to confidently assign site-specific glycosylation	1262:1359	The tandem mass spectra exhibited product ions from both glycan and peptide backbone dissociation for a majority of the glycopeptides tested using collisionally activated dissociation that served to confidently assign site-specific glycosylation.
25153361	2	18	theme	suppression	237:247	arg1	consequence					191:201	a consequence	189:201	a consequence of glycoform diversity and signal suppression from nonglycosylated peptides that ionize more efficiently	189:306	As a consequence of glycoform diversity and signal suppression from nonglycosylated peptides that ionize more efficiently, typical reversed-phase LC-MS and bottom-up proteomics database searching workflows do not perform well for identification of site-specific glycosylation for complex glycoproteins.
25153361	5	19	theme	influenza	905:913	arg1	hemagglutinin					923:935	influenza A virus hemagglutinin	905:935	influenza A virus hemagglutinin (9 sequons)	905:947	We demonstrated the effectiveness of the system using a set of glycoproteins including human transferrin (2 sequons), human alpha-1-acid glycoprotein (5 sequons), and influenza A virus hemagglutinin (9 sequons).
25153361	5	19	theme	influenza	905:913	arg1	sequons					940:946	9 sequons	938:946	9 sequons	938:946	We demonstrated the effectiveness of the system using a set of glycoproteins including human transferrin (2 sequons), human alpha-1-acid glycoprotein (5 sequons), and influenza A virus hemagglutinin (9 sequons).
25153361	7	20	from	glycan	1172:1177	arg1	ions					1157:1160	product ions	1149:1160	product ions from both glycan and peptide backbone dissociation for a majority of the glycopeptides tested using collisionally activated dissociation that served to confidently assign site-specific glycosylation	1149:1359	The tandem mass spectra exhibited product ions from both glycan and peptide backbone dissociation for a majority of the glycopeptides tested using collisionally activated dissociation that served to confidently assign site-specific glycosylation.
25153361	8	21	theme	system	1395:1400	arg1	value					1382:1386	the value	1378:1386	the value of our system to define site-specific glycosylation	1378:1438	We demonstrated the value of our system to define site-specific glycosylation using a hemagglutinin containing 9 N-glycosylation sequons from a single HILIC-C18-MS acquisition.
25153361	0	22	theme	single	82:87	arg1	step					89:92	a single step	80:92	a single step	80:92	Confident assignment of site-specific glycosylation in complex glycoproteins in a single step.
25153361	5	23	theme	virus	917:921	arg1	hemagglutinin					923:935	influenza A virus hemagglutinin	905:935	influenza A virus hemagglutinin (9 sequons)	905:947	We demonstrated the effectiveness of the system using a set of glycoproteins including human transferrin (2 sequons), human alpha-1-acid glycoprotein (5 sequons), and influenza A virus hemagglutinin (9 sequons).
25153361	5	23	theme	virus	917:921	arg1	sequons					940:946	9 sequons	938:946	9 sequons	938:946	We demonstrated the effectiveness of the system using a set of glycoproteins including human transferrin (2 sequons), human alpha-1-acid glycoprotein (5 sequons), and influenza A virus hemagglutinin (9 sequons).
25153361	7	24	gly	glycopeptides	1235:1247	arg2	glycopeptides					1235:1247	the glycopeptides	1231:1247	the glycopeptides tested using collisionally activated dissociation that served to confidently assign site-specific glycosylation	1231:1359	The tandem mass spectra exhibited product ions from both glycan and peptide backbone dissociation for a majority of the glycopeptides tested using collisionally activated dissociation that served to confidently assign site-specific glycosylation.
25153361	3	25	from	glycoproteins	587:599	arg1	glycopeptides					560:572	glycopeptides	560:572	glycopeptides from complex glycoproteins (>4 N-glycosylation sequons) in a single step	560:645	We present an LC-MS system for enrichment, separation, and analysis of glycopeptides from complex glycoproteins (>4 N-glycosylation sequons) in a single step.
25153361	3	25	from	glycoproteins	587:599	arg1	separation					532:541	separation	532:541	separation	532:541	We present an LC-MS system for enrichment, separation, and analysis of glycopeptides from complex glycoproteins (>4 N-glycosylation sequons) in a single step.
25153361	3	25	from	glycoproteins	587:599	arg1	analysis					548:555	analysis	548:555	analysis of glycopeptides from complex glycoproteins (>4 N-glycosylation sequons) in a single step	548:645	We present an LC-MS system for enrichment, separation, and analysis of glycopeptides from complex glycoproteins (>4 N-glycosylation sequons) in a single step.
25153361	3	25	from	glycoproteins	587:599	arg1	enrichment					520:529	enrichment	520:529	enrichment	520:529	We present an LC-MS system for enrichment, separation, and analysis of glycopeptides from complex glycoproteins (>4 N-glycosylation sequons) in a single step.
25153361	3	25	from	glycoproteins	587:599	arg1	step					642:645	a single step	633:645	a single step	633:645	We present an LC-MS system for enrichment, separation, and analysis of glycopeptides from complex glycoproteins (>4 N-glycosylation sequons) in a single step.
25153361	7	26	theme	glycopeptides	1235:1247	arg1	majority					1219:1226	a majority	1217:1226	a majority of the glycopeptides tested using collisionally activated dissociation that served to confidently assign site-specific glycosylation	1217:1359	The tandem mass spectra exhibited product ions from both glycan and peptide backbone dissociation for a majority of the glycopeptides tested using collisionally activated dissociation that served to confidently assign site-specific glycosylation.
25153361	5	27	gly	glycoproteins	801:813	arg1	glycoprotein					875:886	human alpha-1-acid glycoprotein	856:886	human alpha-1-acid glycoprotein (5 sequons)	856:898	We demonstrated the effectiveness of the system using a set of glycoproteins including human transferrin (2 sequons), human alpha-1-acid glycoprotein (5 sequons), and influenza A virus hemagglutinin (9 sequons).
25153361	5	27	gly	glycoproteins	801:813	arg1	transferrin					831:841	human transferrin	825:841	human transferrin (2 sequons)	825:853	We demonstrated the effectiveness of the system using a set of glycoproteins including human transferrin (2 sequons), human alpha-1-acid glycoprotein (5 sequons), and influenza A virus hemagglutinin (9 sequons).
25153361	5	27	gly	glycoproteins	801:813	arg1	hemagglutinin					923:935	influenza A virus hemagglutinin	905:935	influenza A virus hemagglutinin (9 sequons)	905:947	We demonstrated the effectiveness of the system using a set of glycoproteins including human transferrin (2 sequons), human alpha-1-acid glycoprotein (5 sequons), and influenza A virus hemagglutinin (9 sequons).
25153361	5	27	gly	glycoproteins	801:813	arg1	glycoproteins					801:813	glycoproteins	801:813	glycoproteins including human transferrin (2 sequons), human alpha-1-acid glycoprotein (5 sequons), and influenza A virus hemagglutinin (9 sequons)	801:947	We demonstrated the effectiveness of the system using a set of glycoproteins including human transferrin (2 sequons), human alpha-1-acid glycoprotein (5 sequons), and influenza A virus hemagglutinin (9 sequons).
25153361	1	28	gly	glycoprotein	97:108	arg1	glycoprotein					97:108	A glycoprotein	95:108	A glycoprotein	95:108	A glycoprotein may contain several sites of glycosylation, each of which is heterogeneous.
25153361	6	29	theme	spectra	1106:1112	arg1	generation					1052:1061	the generation	1048:1061	the generation of high-quality data-dependent tandem mass spectra	1048:1112	The online enrichment renders glycopeptides the most abundant ions detected, thereby facilitating the generation of high-quality data-dependent tandem mass spectra.
25153361	0	30	theme	Confident	0:8	arg1	assignment					10:19	Confident assignment	0:19	Confident assignment of site-specific glycosylation in complex glycoproteins in a single step	0:92	Confident assignment of site-specific glycosylation in complex glycoproteins in a single step.
25153361	6	31	theme	tandem	1094:1099	arg1	spectra					1106:1112	high-quality data-dependent tandem mass spectra	1066:1112	high-quality data-dependent tandem mass spectra	1066:1112	The online enrichment renders glycopeptides the most abundant ions detected, thereby facilitating the generation of high-quality data-dependent tandem mass spectra.
25153361	3	32	theme	LC-MS	503:507	arg1	system					509:514	an LC-MS system	500:514	an LC-MS system for enrichment, separation, and analysis of glycopeptides from complex glycoproteins (>4 N-glycosylation sequons) in a single step	500:645	We present an LC-MS system for enrichment, separation, and analysis of glycopeptides from complex glycoproteins (>4 N-glycosylation sequons) in a single step.
25153361	2	33	from	peptides	270:277	arg1	consequence					191:201	a consequence	189:201	a consequence of glycoform diversity and signal suppression from nonglycosylated peptides that ionize more efficiently	189:306	As a consequence of glycoform diversity and signal suppression from nonglycosylated peptides that ionize more efficiently, typical reversed-phase LC-MS and bottom-up proteomics database searching workflows do not perform well for identification of site-specific glycosylation for complex glycoproteins.
25153361	2	33	from	peptides	270:277	arg1	diversity					216:224	glycoform diversity	206:224	glycoform diversity	206:224	As a consequence of glycoform diversity and signal suppression from nonglycosylated peptides that ionize more efficiently, typical reversed-phase LC-MS and bottom-up proteomics database searching workflows do not perform well for identification of site-specific glycosylation for complex glycoproteins.
25153361	2	33	from	peptides	270:277	arg1	suppression					237:247	signal suppression	230:247	signal suppression	230:247	As a consequence of glycoform diversity and signal suppression from nonglycosylated peptides that ionize more efficiently, typical reversed-phase LC-MS and bottom-up proteomics database searching workflows do not perform well for identification of site-specific glycosylation for complex glycoproteins.
25153361	6	34	theme	high-quality	1066:1077	arg1	spectra					1106:1112	high-quality data-dependent tandem mass spectra	1066:1112	high-quality data-dependent tandem mass spectra	1066:1112	The online enrichment renders glycopeptides the most abundant ions detected, thereby facilitating the generation of high-quality data-dependent tandem mass spectra.
25153361	8	35	theme	N-glycosylation	1475:1489	arg1	sequons					1491:1497	9 N-glycosylation sequons	1473:1497	9 N-glycosylation sequons	1473:1497	We demonstrated the value of our system to define site-specific glycosylation using a hemagglutinin containing 9 N-glycosylation sequons from a single HILIC-C18-MS acquisition.
25153361	2	36	theme	site-specific	434:446	arg1	glycosylation					448:460	site-specific glycosylation	434:460	site-specific glycosylation for complex glycoproteins	434:486	As a consequence of glycoform diversity and signal suppression from nonglycosylated peptides that ionize more efficiently, typical reversed-phase LC-MS and bottom-up proteomics database searching workflows do not perform well for identification of site-specific glycosylation for complex glycoproteins.
25153361	5	37	theme	human	825:829	arg1	transferrin					831:841	human transferrin	825:841	human transferrin (2 sequons)	825:853	We demonstrated the effectiveness of the system using a set of glycoproteins including human transferrin (2 sequons), human alpha-1-acid glycoprotein (5 sequons), and influenza A virus hemagglutinin (9 sequons).
25153361	5	37	theme	human	825:829	arg1	sequons					846:852	2 sequons	844:852	2 sequons	844:852	We demonstrated the effectiveness of the system using a set of glycoproteins including human transferrin (2 sequons), human alpha-1-acid glycoprotein (5 sequons), and influenza A virus hemagglutinin (9 sequons).
25153361	7	38	theme	peptide	1183:1189	arg1	backbone					1191:1198	peptide backbone	1183:1198	peptide backbone	1183:1198	The tandem mass spectra exhibited product ions from both glycan and peptide backbone dissociation for a majority of the glycopeptides tested using collisionally activated dissociation that served to confidently assign site-specific glycosylation.
25153361	2	39	theme	database	363:370	arg1	searching					372:380	bottom-up proteomics database searching	342:380	bottom-up proteomics database searching	342:380	As a consequence of glycoform diversity and signal suppression from nonglycosylated peptides that ionize more efficiently, typical reversed-phase LC-MS and bottom-up proteomics database searching workflows do not perform well for identification of site-specific glycosylation for complex glycoproteins.
25153361	0	40	theme	complex	55:61	arg1	glycoproteins					63:75	complex glycoproteins	55:75	complex glycoproteins in a single step	55:92	Confident assignment of site-specific glycosylation in complex glycoproteins in a single step.
25153361	8	41	theme	single	1506:1511	arg1	acquisition					1526:1536	a single HILIC-C18-MS acquisition	1504:1536	a single HILIC-C18-MS acquisition	1504:1536	We demonstrated the value of our system to define site-specific glycosylation using a hemagglutinin containing 9 N-glycosylation sequons from a single HILIC-C18-MS acquisition.
25153361	2	42	theme	bottom-up	342:350	arg1	searching					372:380	bottom-up proteomics database searching	342:380	bottom-up proteomics database searching	342:380	As a consequence of glycoform diversity and signal suppression from nonglycosylated peptides that ionize more efficiently, typical reversed-phase LC-MS and bottom-up proteomics database searching workflows do not perform well for identification of site-specific glycosylation for complex glycoproteins.
25153361	0	43	gly	glycoproteins	63:75	arg1	glycoproteins					63:75	complex glycoproteins	55:75	complex glycoproteins in a single step	55:92	Confident assignment of site-specific glycosylation in complex glycoproteins in a single step.
25153361	1	44	contain	contain	114:120	arg1	glycoprotein					97:108	A glycoprotein	95:108	A glycoprotein	95:108	A glycoprotein may contain several sites of glycosylation, each of which is heterogeneous.
25153361	1	44	contain	contain	114:120	arg2	glycosylation					139:151	glycosylation	139:151	glycosylation	139:151	A glycoprotein may contain several sites of glycosylation, each of which is heterogeneous.
25153361	1	44	contain	contain	114:120	arg2	sites					130:134	several sites	122:134	several sites	122:134	A glycoprotein may contain several sites of glycosylation, each of which is heterogeneous.
25153361	3	45	theme	complex	579:585	arg1	glycoproteins					587:599	complex glycoproteins	579:599	complex glycoproteins (>4 N-glycosylation sequons) in a single step	579:645	We present an LC-MS system for enrichment, separation, and analysis of glycopeptides from complex glycoproteins (>4 N-glycosylation sequons) in a single step.
25153361	3	45	theme	complex	579:585	arg1	sequons					621:627	>4 N-glycosylation sequons	602:627	>4 N-glycosylation sequons	602:627	We present an LC-MS system for enrichment, separation, and analysis of glycopeptides from complex glycoproteins (>4 N-glycosylation sequons) in a single step.
25153361	2	46	theme	LC-MS	332:336	arg1	workflows					382:390	typical reversed-phase LC-MS and bottom-up proteomics database searching workflows	309:390	typical reversed-phase LC-MS and bottom-up proteomics database searching workflows	309:390	As a consequence of glycoform diversity and signal suppression from nonglycosylated peptides that ionize more efficiently, typical reversed-phase LC-MS and bottom-up proteomics database searching workflows do not perform well for identification of site-specific glycosylation for complex glycoproteins.
25153361	7	47	theme	mass	1126:1129	arg1	spectra					1131:1137	The tandem mass spectra	1115:1137	The tandem mass spectra	1115:1137	The tandem mass spectra exhibited product ions from both glycan and peptide backbone dissociation for a majority of the glycopeptides tested using collisionally activated dissociation that served to confidently assign site-specific glycosylation.
25153361	3	48	theme	glycopeptides	560:572	arg1	separation					532:541	separation	532:541	separation	532:541	We present an LC-MS system for enrichment, separation, and analysis of glycopeptides from complex glycoproteins (>4 N-glycosylation sequons) in a single step.
25153361	3	48	theme	glycopeptides	560:572	arg1	analysis					548:555	analysis	548:555	analysis of glycopeptides from complex glycoproteins (>4 N-glycosylation sequons) in a single step	548:645	We present an LC-MS system for enrichment, separation, and analysis of glycopeptides from complex glycoproteins (>4 N-glycosylation sequons) in a single step.
25153361	3	48	theme	glycopeptides	560:572	arg1	enrichment					520:529	enrichment	520:529	enrichment	520:529	We present an LC-MS system for enrichment, separation, and analysis of glycopeptides from complex glycoproteins (>4 N-glycosylation sequons) in a single step.
25153361	2	49	from	consequence	191:201	arg1	peptides					270:277	nonglycosylated peptides	254:277	nonglycosylated peptides that ionize more efficiently	254:306	As a consequence of glycoform diversity and signal suppression from nonglycosylated peptides that ionize more efficiently, typical reversed-phase LC-MS and bottom-up proteomics database searching workflows do not perform well for identification of site-specific glycosylation for complex glycoproteins.
25153361	4	50	theme	enrichment	681:690	arg1	trap					692:695	an online HILIC enrichment trap	665:695	an online HILIC enrichment trap prior to reversed-phase C18-MS analysis	665:735	This system uses an online HILIC enrichment trap prior to reversed-phase C18-MS analysis.
25153361	2	51	gly	nonglycosylated	254:268	arg1	peptides					270:277	nonglycosylated peptides	254:277	nonglycosylated peptides that ionize more efficiently	254:306	As a consequence of glycoform diversity and signal suppression from nonglycosylated peptides that ionize more efficiently, typical reversed-phase LC-MS and bottom-up proteomics database searching workflows do not perform well for identification of site-specific glycosylation for complex glycoproteins.
25153361	5	52	theme	glycoproteins	801:813	arg1	glycoprotein					875:886	human alpha-1-acid glycoprotein	856:886	human alpha-1-acid glycoprotein (5 sequons)	856:898	We demonstrated the effectiveness of the system using a set of glycoproteins including human transferrin (2 sequons), human alpha-1-acid glycoprotein (5 sequons), and influenza A virus hemagglutinin (9 sequons).
25153361	5	52	theme	glycoproteins	801:813	arg1	set					794:796	a set	792:796	a set of glycoproteins including human transferrin (2 sequons), human alpha-1-acid glycoprotein (5 sequons), and influenza A virus hemagglutinin (9 sequons)	792:947	We demonstrated the effectiveness of the system using a set of glycoproteins including human transferrin (2 sequons), human alpha-1-acid glycoprotein (5 sequons), and influenza A virus hemagglutinin (9 sequons).
25153361	5	52	theme	glycoproteins	801:813	arg1	transferrin					831:841	human transferrin	825:841	human transferrin (2 sequons)	825:853	We demonstrated the effectiveness of the system using a set of glycoproteins including human transferrin (2 sequons), human alpha-1-acid glycoprotein (5 sequons), and influenza A virus hemagglutinin (9 sequons).
25153361	5	52	theme	glycoproteins	801:813	arg1	hemagglutinin					923:935	influenza A virus hemagglutinin	905:935	influenza A virus hemagglutinin (9 sequons)	905:947	We demonstrated the effectiveness of the system using a set of glycoproteins including human transferrin (2 sequons), human alpha-1-acid glycoprotein (5 sequons), and influenza A virus hemagglutinin (9 sequons).
25153361	5	52	theme	glycoproteins	801:813	arg1	glycoproteins					801:813	glycoproteins	801:813	glycoproteins including human transferrin (2 sequons), human alpha-1-acid glycoprotein (5 sequons), and influenza A virus hemagglutinin (9 sequons)	801:947	We demonstrated the effectiveness of the system using a set of glycoproteins including human transferrin (2 sequons), human alpha-1-acid glycoprotein (5 sequons), and influenza A virus hemagglutinin (9 sequons).
25153361	3	53	from	enrichment	520:529	arg1	glycoproteins					587:599	complex glycoproteins	579:599	complex glycoproteins (>4 N-glycosylation sequons) in a single step	579:645	We present an LC-MS system for enrichment, separation, and analysis of glycopeptides from complex glycoproteins (>4 N-glycosylation sequons) in a single step.
25153361	3	53	from	enrichment	520:529	arg1	sequons					621:627	>4 N-glycosylation sequons	602:627	>4 N-glycosylation sequons	602:627	We present an LC-MS system for enrichment, separation, and analysis of glycopeptides from complex glycoproteins (>4 N-glycosylation sequons) in a single step.
25153361	3	54	theme	N-glycosylation	605:619	arg1	glycoproteins					587:599	complex glycoproteins	579:599	complex glycoproteins (>4 N-glycosylation sequons) in a single step	579:645	We present an LC-MS system for enrichment, separation, and analysis of glycopeptides from complex glycoproteins (>4 N-glycosylation sequons) in a single step.
25153361	3	54	theme	N-glycosylation	605:619	arg1	sequons					621:627	>4 N-glycosylation sequons	602:627	>4 N-glycosylation sequons	602:627	We present an LC-MS system for enrichment, separation, and analysis of glycopeptides from complex glycoproteins (>4 N-glycosylation sequons) in a single step.
25153361	5	55	gly	glycoprotein	875:886	arg1	glycoprotein					875:886	human alpha-1-acid glycoprotein	856:886	human alpha-1-acid glycoprotein (5 sequons)	856:898	We demonstrated the effectiveness of the system using a set of glycoproteins including human transferrin (2 sequons), human alpha-1-acid glycoprotein (5 sequons), and influenza A virus hemagglutinin (9 sequons).
25153361	5	55	gly	glycoprotein	875:886	arg1	sequons					891:897	5 sequons	889:897	5 sequons	889:897	We demonstrated the effectiveness of the system using a set of glycoproteins including human transferrin (2 sequons), human alpha-1-acid glycoprotein (5 sequons), and influenza A virus hemagglutinin (9 sequons).
25153361	4	56	theme	prior	697:701	arg1	trap					692:695	an online HILIC enrichment trap	665:695	an online HILIC enrichment trap prior to reversed-phase C18-MS analysis	665:735	This system uses an online HILIC enrichment trap prior to reversed-phase C18-MS analysis.
25153361	3	57	from	separation	532:541	arg1	glycoproteins					587:599	complex glycoproteins	579:599	complex glycoproteins (>4 N-glycosylation sequons) in a single step	579:645	We present an LC-MS system for enrichment, separation, and analysis of glycopeptides from complex glycoproteins (>4 N-glycosylation sequons) in a single step.
25153361	3	57	from	separation	532:541	arg1	sequons					621:627	>4 N-glycosylation sequons	602:627	>4 N-glycosylation sequons	602:627	We present an LC-MS system for enrichment, separation, and analysis of glycopeptides from complex glycoproteins (>4 N-glycosylation sequons) in a single step.
25153361	2	58	theme	typical	309:315	arg1	LC-MS					332:336	typical reversed-phase LC-MS	309:336	typical reversed-phase LC-MS	309:336	As a consequence of glycoform diversity and signal suppression from nonglycosylated peptides that ionize more efficiently, typical reversed-phase LC-MS and bottom-up proteomics database searching workflows do not perform well for identification of site-specific glycosylation for complex glycoproteins.
25153361	5	59	theme	human	856:860	arg1	glycoprotein					875:886	human alpha-1-acid glycoprotein	856:886	human alpha-1-acid glycoprotein (5 sequons)	856:898	We demonstrated the effectiveness of the system using a set of glycoproteins including human transferrin (2 sequons), human alpha-1-acid glycoprotein (5 sequons), and influenza A virus hemagglutinin (9 sequons).
25153361	5	59	theme	human	856:860	arg1	sequons					891:897	5 sequons	889:897	5 sequons	889:897	We demonstrated the effectiveness of the system using a set of glycoproteins including human transferrin (2 sequons), human alpha-1-acid glycoprotein (5 sequons), and influenza A virus hemagglutinin (9 sequons).
25153361	2	60	theme	signal	230:235	arg1	suppression					237:247	signal suppression	230:247	signal suppression	230:247	As a consequence of glycoform diversity and signal suppression from nonglycosylated peptides that ionize more efficiently, typical reversed-phase LC-MS and bottom-up proteomics database searching workflows do not perform well for identification of site-specific glycosylation for complex glycoproteins.
25153361	6	61	theme	online	954:959	arg1	enrichment					961:970	The online enrichment	950:970	The online enrichment	950:970	The online enrichment renders glycopeptides the most abundant ions detected, thereby facilitating the generation of high-quality data-dependent tandem mass spectra.
25153361	4	62	theme	online	668:673	arg1	trap					692:695	an online HILIC enrichment trap	665:695	an online HILIC enrichment trap prior to reversed-phase C18-MS analysis	665:735	This system uses an online HILIC enrichment trap prior to reversed-phase C18-MS analysis.
25153361	2	63	theme	diversity	216:224	arg1	consequence					191:201	a consequence	189:201	a consequence of glycoform diversity and signal suppression from nonglycosylated peptides that ionize more efficiently	189:306	As a consequence of glycoform diversity and signal suppression from nonglycosylated peptides that ionize more efficiently, typical reversed-phase LC-MS and bottom-up proteomics database searching workflows do not perform well for identification of site-specific glycosylation for complex glycoproteins.
25153361	3	64	gly	N-glycosylation	605:619	arg2	sequons					621:627	>4 N-glycosylation sequons	602:627	>4 N-glycosylation sequons	602:627	We present an LC-MS system for enrichment, separation, and analysis of glycopeptides from complex glycoproteins (>4 N-glycosylation sequons) in a single step.
25153361	3	64	gly	N-glycosylation	605:619	arg2	glycoproteins					587:599	complex glycoproteins	579:599	complex glycoproteins (>4 N-glycosylation sequons) in a single step	579:645	We present an LC-MS system for enrichment, separation, and analysis of glycopeptides from complex glycoproteins (>4 N-glycosylation sequons) in a single step.
25153361	1	65	theme	glycosylation	139:151	arg1	sites					130:134	several sites	122:134	several sites	122:134	A glycoprotein may contain several sites of glycosylation, each of which is heterogeneous.
25153361	1	65	theme	glycosylation	139:151	arg1	glycosylation					139:151	glycosylation	139:151	glycosylation	139:151	A glycoprotein may contain several sites of glycosylation, each of which is heterogeneous.
25153361	8	66	contain	containing	1462:1471	arg1	hemagglutinin					1448:1460	a hemagglutinin	1446:1460	a hemagglutinin containing 9 N-glycosylation sequons from a single HILIC-C18-MS acquisition	1446:1536	We demonstrated the value of our system to define site-specific glycosylation using a hemagglutinin containing 9 N-glycosylation sequons from a single HILIC-C18-MS acquisition.
25153361	8	66	contain	containing	1462:1471	arg2	sequons					1491:1497	9 N-glycosylation sequons	1473:1497	9 N-glycosylation sequons	1473:1497	We demonstrated the value of our system to define site-specific glycosylation using a hemagglutinin containing 9 N-glycosylation sequons from a single HILIC-C18-MS acquisition.
25153361	4	67	theme	reversed-phase	706:719	arg1	analysis					728:735	reversed-phase C18-MS analysis	706:735	reversed-phase C18-MS analysis	706:735	This system uses an online HILIC enrichment trap prior to reversed-phase C18-MS analysis.
25153361	5	68	theme	A	915:915	arg1	hemagglutinin					923:935	influenza A virus hemagglutinin	905:935	influenza A virus hemagglutinin (9 sequons)	905:947	We demonstrated the effectiveness of the system using a set of glycoproteins including human transferrin (2 sequons), human alpha-1-acid glycoprotein (5 sequons), and influenza A virus hemagglutinin (9 sequons).
25153361	5	68	theme	A	915:915	arg1	sequons					940:946	9 sequons	938:946	9 sequons	938:946	We demonstrated the effectiveness of the system using a set of glycoproteins including human transferrin (2 sequons), human alpha-1-acid glycoprotein (5 sequons), and influenza A virus hemagglutinin (9 sequons).
25153361	0	69	from	glycoproteins	63:75	arg1	step					89:92	a single step	80:92	a single step	80:92	Confident assignment of site-specific glycosylation in complex glycoproteins in a single step.
25153361	0	70	from	assignment	10:19	arg1	glycoproteins					63:75	complex glycoproteins	55:75	complex glycoproteins in a single step	55:92	Confident assignment of site-specific glycosylation in complex glycoproteins in a single step.
25153361	3	71	gly	glycopeptides	560:572	arg2	glycopeptides					560:572	glycopeptides	560:572	glycopeptides from complex glycoproteins (>4 N-glycosylation sequons) in a single step	560:645	We present an LC-MS system for enrichment, separation, and analysis of glycopeptides from complex glycoproteins (>4 N-glycosylation sequons) in a single step.
25153361	3	71	gly	glycopeptides	560:572	arg1	glycoproteins					587:599	complex glycoproteins	579:599	complex glycoproteins (>4 N-glycosylation sequons) in a single step	579:645	We present an LC-MS system for enrichment, separation, and analysis of glycopeptides from complex glycoproteins (>4 N-glycosylation sequons) in a single step.
25153361	3	71	gly	glycopeptides	560:572	arg1	sequons					621:627	>4 N-glycosylation sequons	602:627	>4 N-glycosylation sequons	602:627	We present an LC-MS system for enrichment, separation, and analysis of glycopeptides from complex glycoproteins (>4 N-glycosylation sequons) in a single step.
25153361	6	72	theme	abundant	1003:1010	arg1	ions					1012:1015	the most abundant ions	994:1015	glycopeptides the most abundant ions detected	980:1024	The online enrichment renders glycopeptides the most abundant ions detected, thereby facilitating the generation of high-quality data-dependent tandem mass spectra.
25153361	7	73	from	backbone	1191:1198	arg1	ions					1157:1160	product ions	1149:1160	product ions from both glycan and peptide backbone dissociation for a majority of the glycopeptides tested using collisionally activated dissociation that served to confidently assign site-specific glycosylation	1149:1359	The tandem mass spectra exhibited product ions from both glycan and peptide backbone dissociation for a majority of the glycopeptides tested using collisionally activated dissociation that served to confidently assign site-specific glycosylation.
25153361	5	74	theme	system	779:784	arg1	effectiveness					758:770	the effectiveness	754:770	the effectiveness of the system	754:784	We demonstrated the effectiveness of the system using a set of glycoproteins including human transferrin (2 sequons), human alpha-1-acid glycoprotein (5 sequons), and influenza A virus hemagglutinin (9 sequons).
25153361	7	75	dep	glycan	1172:1177	arg1	dissociation					1200:1211	dissociation	1200:1211	dissociation	1200:1211	The tandem mass spectra exhibited product ions from both glycan and peptide backbone dissociation for a majority of the glycopeptides tested using collisionally activated dissociation that served to confidently assign site-specific glycosylation.
25153361	8	76	theme	site-specific	1412:1424	arg1	glycosylation					1426:1438	site-specific glycosylation	1412:1438	site-specific glycosylation	1412:1438	We demonstrated the value of our system to define site-specific glycosylation using a hemagglutinin containing 9 N-glycosylation sequons from a single HILIC-C18-MS acquisition.
25153361	6	77	theme	mass	1101:1104	arg1	spectra					1106:1112	high-quality data-dependent tandem mass spectra	1066:1112	high-quality data-dependent tandem mass spectra	1066:1112	The online enrichment renders glycopeptides the most abundant ions detected, thereby facilitating the generation of high-quality data-dependent tandem mass spectra.
25153361	0	78	theme	site-specific	24:36	arg1	glycosylation					38:50	site-specific glycosylation	24:50	site-specific glycosylation	24:50	Confident assignment of site-specific glycosylation in complex glycoproteins in a single step.
25153361	6	79	theme	data-dependent	1079:1092	arg1	spectra					1106:1112	high-quality data-dependent tandem mass spectra	1066:1112	high-quality data-dependent tandem mass spectra	1066:1112	The online enrichment renders glycopeptides the most abundant ions detected, thereby facilitating the generation of high-quality data-dependent tandem mass spectra.
25153361	2	80	theme	complex	466:472	arg1	glycoproteins					474:486	complex glycoproteins	466:486	complex glycoproteins	466:486	As a consequence of glycoform diversity and signal suppression from nonglycosylated peptides that ionize more efficiently, typical reversed-phase LC-MS and bottom-up proteomics database searching workflows do not perform well for identification of site-specific glycosylation for complex glycoproteins.
25153361	2	81	theme	glycosylation	448:460	arg1	identification					416:429	identification	416:429	identification of site-specific glycosylation for complex glycoproteins	416:486	As a consequence of glycoform diversity and signal suppression from nonglycosylated peptides that ionize more efficiently, typical reversed-phase LC-MS and bottom-up proteomics database searching workflows do not perform well for identification of site-specific glycosylation for complex glycoproteins.
25153361	7	82	theme	site-specific	1333:1345	arg1	glycosylation					1347:1359	site-specific glycosylation	1333:1359	site-specific glycosylation	1333:1359	The tandem mass spectra exhibited product ions from both glycan and peptide backbone dissociation for a majority of the glycopeptides tested using collisionally activated dissociation that served to confidently assign site-specific glycosylation.
25153361	2	83	theme	proteomics	352:361	arg1	searching					372:380	bottom-up proteomics database searching	342:380	bottom-up proteomics database searching	342:380	As a consequence of glycoform diversity and signal suppression from nonglycosylated peptides that ionize more efficiently, typical reversed-phase LC-MS and bottom-up proteomics database searching workflows do not perform well for identification of site-specific glycosylation for complex glycoproteins.
25153361	2	84	gly	glycoproteins	474:486	arg1	glycoproteins					474:486	complex glycoproteins	466:486	complex glycoproteins	466:486	As a consequence of glycoform diversity and signal suppression from nonglycosylated peptides that ionize more efficiently, typical reversed-phase LC-MS and bottom-up proteomics database searching workflows do not perform well for identification of site-specific glycosylation for complex glycoproteins.
25153361	8	85	gly	N-glycosylation	1475:1489	arg2	sequons					1491:1497	9 N-glycosylation sequons	1473:1497	9 N-glycosylation sequons	1473:1497	We demonstrated the value of our system to define site-specific glycosylation using a hemagglutinin containing 9 N-glycosylation sequons from a single HILIC-C18-MS acquisition.
25153361	8	86	theme	HILIC-C18-MS	1513:1524	arg1	acquisition					1526:1536	a single HILIC-C18-MS acquisition	1504:1536	a single HILIC-C18-MS acquisition	1504:1536	We demonstrated the value of our system to define site-specific glycosylation using a hemagglutinin containing 9 N-glycosylation sequons from a single HILIC-C18-MS acquisition.
21570947	0	0	theme	sodium-dependent	80:95	arg1	transporter					110:120	the human sodium-dependent multivitamin transporter	70:120	the human sodium-dependent multivitamin transporter (hSMVT)	70:128	Role of the putative N-glycosylation and PKC-phosphorylation sites of the human sodium-dependent multivitamin transporter (hSMVT) in function and regulation.
21570947	0	0	theme	sodium-dependent	80:95	arg1	hSMVT					123:127	hSMVT	123:127	hSMVT	123:127	Role of the putative N-glycosylation and PKC-phosphorylation sites of the human sodium-dependent multivitamin transporter (hSMVT) in function and regulation.
21570947	6	1	theme	mRNA	1147:1150	arg1	expression					1111:1120	expression	1111:1120	expression of the hSMVT protein and mRNA	1111:1150	The latter effect was not mediated via changes in the level of expression of the hSMVT protein and mRNA or in its level of expression at the cell membrane.
21570947	2	2	dep	function	444:451	arg1	the					440:442	the	440:442	the	440:442	The human SMVT (hSMVT) polypeptide is predicted to have four N-glycosylation sites and two putative PKC phosphorylation sites but their role in the function and regulation of the protein is not known and was examined in this investigation.
21570947	0	3	theme	human	74:78	arg1	transporter					110:120	the human sodium-dependent multivitamin transporter	70:120	the human sodium-dependent multivitamin transporter (hSMVT)	70:128	Role of the putative N-glycosylation and PKC-phosphorylation sites of the human sodium-dependent multivitamin transporter (hSMVT) in function and regulation.
21570947	0	3	theme	human	74:78	arg1	hSMVT					123:127	hSMVT	123:127	hSMVT	123:127	Role of the putative N-glycosylation and PKC-phosphorylation sites of the human sodium-dependent multivitamin transporter (hSMVT) in function and regulation.
21570947	6	4	theme	expression	1171:1180	arg1	level					1162:1166	its level	1158:1166	its level of expression at the cell membrane	1158:1201	The latter effect was not mediated via changes in the level of expression of the hSMVT protein and mRNA or in its level of expression at the cell membrane.
21570947	1	5	theme	sodium-dependent	162:177	arg1	SMVT					205:208	SMVT	205:208	SMVT	205:208	The sodium-dependent multivitamin transporter (SMVT) is a major biotin transporter in a variety of tissues including the small intestine.
21570947	1	5	theme	sodium-dependent	162:177	arg1	transporter					192:202	The sodium-dependent multivitamin transporter	158:202	The sodium-dependent multivitamin transporter (SMVT)	158:209	The sodium-dependent multivitamin transporter (SMVT) is a major biotin transporter in a variety of tissues including the small intestine.
21570947	1	5	theme	sodium-dependent	162:177	arg1	transporter					229:239	a major biotin transporter	214:239	a major biotin transporter in a variety of tissues including the small intestine	214:293	The sodium-dependent multivitamin transporter (SMVT) is a major biotin transporter in a variety of tissues including the small intestine.
21570947	2	6	from	role	432:435	arg1	function					444:451	function	444:451	function	444:451	The human SMVT (hSMVT) polypeptide is predicted to have four N-glycosylation sites and two putative PKC phosphorylation sites but their role in the function and regulation of the protein is not known and was examined in this investigation.
21570947	2	6	from	role	432:435	arg1	regulation					457:466	regulation	457:466	regulation	457:466	The human SMVT (hSMVT) polypeptide is predicted to have four N-glycosylation sites and two putative PKC phosphorylation sites but their role in the function and regulation of the protein is not known and was examined in this investigation.
21570947	8	7	dep	site	1398:1401	arg1	286					1407:1409	286	1407:1409	286	1407:1409	Furthermore, the study shows a role for the putative PKC-phosphorylation site Thr(286) of hSMVT in the PKC-mediated regulation of biotin uptake.
21570947	8	7	dep	site	1398:1401	arg1	Thr					1403:1405	Thr	1403:1405	the putative PKC-phosphorylation site Thr(286) of hSMVT in the PKC-mediated regulation of biotin uptake	1365:1467	Furthermore, the study shows a role for the putative PKC-phosphorylation site Thr(286) of hSMVT in the PKC-mediated regulation of biotin uptake.
21570947	0	8	theme	transporter	110:120	arg1	transporter					110:120	the human sodium-dependent multivitamin transporter	70:120	the human sodium-dependent multivitamin transporter (hSMVT)	70:128	Role of the putative N-glycosylation and PKC-phosphorylation sites of the human sodium-dependent multivitamin transporter (hSMVT) in function and regulation.
21570947	0	8	theme	transporter	110:120	arg1	N-glycosylation					21:35	the putative N-glycosylation and PKC-phosphorylation sites	8:65	N-glycosylation	21:35	Role of the putative N-glycosylation and PKC-phosphorylation sites of the human sodium-dependent multivitamin transporter (hSMVT) in function and regulation.
21570947	0	8	theme	transporter	110:120	arg1	sites					61:65	the putative N-glycosylation and PKC-phosphorylation sites	8:65	sites	61:65	Role of the putative N-glycosylation and PKC-phosphorylation sites of the human sodium-dependent multivitamin transporter (hSMVT) in function and regulation.
21570947	0	9	from	Role	0:3	arg1	function					133:140	function	133:140	function	133:140	Role of the putative N-glycosylation and PKC-phosphorylation sites of the human sodium-dependent multivitamin transporter (hSMVT) in function and regulation.
21570947	0	9	from	Role	0:3	arg1	regulation					146:155	regulation	146:155	regulation	146:155	Role of the putative N-glycosylation and PKC-phosphorylation sites of the human sodium-dependent multivitamin transporter (hSMVT) in function and regulation.
21570947	1	10	theme	tissues	257:263	arg1	intestine					285:293	the small intestine	275:293	the small intestine	275:293	The sodium-dependent multivitamin transporter (SMVT) is a major biotin transporter in a variety of tissues including the small intestine.
21570947	1	10	theme	tissues	257:263	arg1	tissues					257:263	tissues	257:263	tissues including the small intestine	257:293	The sodium-dependent multivitamin transporter (SMVT) is a major biotin transporter in a variety of tissues including the small intestine.
21570947	1	10	theme	tissues	257:263	arg1	variety					246:252	a variety	244:252	a variety of tissues including the small intestine	244:293	The sodium-dependent multivitamin transporter (SMVT) is a major biotin transporter in a variety of tissues including the small intestine.
21570947	0	11	theme	multivitamin	97:108	arg1	transporter					110:120	the human sodium-dependent multivitamin transporter	70:120	the human sodium-dependent multivitamin transporter (hSMVT)	70:128	Role of the putative N-glycosylation and PKC-phosphorylation sites of the human sodium-dependent multivitamin transporter (hSMVT) in function and regulation.
21570947	0	11	theme	multivitamin	97:108	arg1	hSMVT					123:127	hSMVT	123:127	hSMVT	123:127	Role of the putative N-glycosylation and PKC-phosphorylation sites of the human sodium-dependent multivitamin transporter (hSMVT) in function and regulation.
21570947	5	12	theme	PMA-induced	1007:1017	arg1	inhibition					1019:1028	the PMA-induced inhibition	1003:1028	the PMA-induced inhibition in biotin uptake	1003:1045	Mutating the putative PKC phosphorylation site Thr(286) of hSMVT led to a significant decrease in the PMA-induced inhibition in biotin uptake.
21570947	6	13	theme	expression	1111:1120	arg1	level					1102:1106	the level	1098:1106	the level of expression of the hSMVT protein and mRNA	1098:1150	The latter effect was not mediated via changes in the level of expression of the hSMVT protein and mRNA or in its level of expression at the cell membrane.
21570947	6	14	from	changes	1087:1093	arg1	level					1102:1106	the level	1098:1106	the level of expression of the hSMVT protein and mRNA	1098:1150	The latter effect was not mediated via changes in the level of expression of the hSMVT protein and mRNA or in its level of expression at the cell membrane.
21570947	6	14	from	changes	1087:1093	arg1	level					1162:1166	its level	1158:1166	its level of expression at the cell membrane	1158:1201	The latter effect was not mediated via changes in the level of expression of the hSMVT protein and mRNA or in its level of expression at the cell membrane.
21570947	4	15	theme	process	896:902	arg1	max					870:872	max	870:872	max	870:872	Studies utilizing site-directed mutagenesis revealed that the N-glycosylation sites at positions Asn(138) and Asn(489) are important for the function of hSMVT and that mutating these sites significantly reduces the V(max) of the biotin uptake process.
21570947	4	15	theme	process	896:902	arg1	V					868:868	the V	864:868	the V(max) of the biotin uptake process	864:902	Studies utilizing site-directed mutagenesis revealed that the N-glycosylation sites at positions Asn(138) and Asn(489) are important for the function of hSMVT and that mutating these sites significantly reduces the V(max) of the biotin uptake process.
21570947	1	16	theme	multivitamin	179:190	arg1	SMVT					205:208	SMVT	205:208	SMVT	205:208	The sodium-dependent multivitamin transporter (SMVT) is a major biotin transporter in a variety of tissues including the small intestine.
21570947	1	16	theme	multivitamin	179:190	arg1	transporter					192:202	The sodium-dependent multivitamin transporter	158:202	The sodium-dependent multivitamin transporter (SMVT)	158:209	The sodium-dependent multivitamin transporter (SMVT) is a major biotin transporter in a variety of tissues including the small intestine.
21570947	1	16	theme	multivitamin	179:190	arg1	transporter					229:239	a major biotin transporter	214:239	a major biotin transporter in a variety of tissues including the small intestine	214:293	The sodium-dependent multivitamin transporter (SMVT) is a major biotin transporter in a variety of tissues including the small intestine.
21570947	4	17	theme	uptake	889:894	arg1	process					896:902	the biotin uptake process	878:902	the biotin uptake process	878:902	Studies utilizing site-directed mutagenesis revealed that the N-glycosylation sites at positions Asn(138) and Asn(489) are important for the function of hSMVT and that mutating these sites significantly reduces the V(max) of the biotin uptake process.
21570947	2	18	contain	have	347:350	arg1	polypeptide					319:329	The human SMVT (hSMVT) polypeptide	296:329	The human SMVT (hSMVT) polypeptide	296:329	The human SMVT (hSMVT) polypeptide is predicted to have four N-glycosylation sites and two putative PKC phosphorylation sites but their role in the function and regulation of the protein is not known and was examined in this investigation.
21570947	2	18	contain	have	347:350	arg2	sites					416:420	two putative PKC phosphorylation sites	383:420	two putative PKC phosphorylation sites	383:420	The human SMVT (hSMVT) polypeptide is predicted to have four N-glycosylation sites and two putative PKC phosphorylation sites but their role in the function and regulation of the protein is not known and was examined in this investigation.
21570947	2	18	contain	have	347:350	arg2	sites					373:377	four N-glycosylation sites	352:377	four N-glycosylation sites	352:377	The human SMVT (hSMVT) polypeptide is predicted to have four N-glycosylation sites and two putative PKC phosphorylation sites but their role in the function and regulation of the protein is not known and was examined in this investigation.
21570947	5	19	from	decrease	991:998	arg1	inhibition					1019:1028	the PMA-induced inhibition	1003:1028	the PMA-induced inhibition in biotin uptake	1003:1045	Mutating the putative PKC phosphorylation site Thr(286) of hSMVT led to a significant decrease in the PMA-induced inhibition in biotin uptake.
21570947	5	20	theme	putative	918:925	arg1	site					947:950	the putative PKC phosphorylation site	914:950	the putative PKC phosphorylation site Thr(286) of hSMVT	914:968	Mutating the putative PKC phosphorylation site Thr(286) of hSMVT led to a significant decrease in the PMA-induced inhibition in biotin uptake.
21570947	5	20	theme	putative	918:925	arg1	hSMVT					964:968	hSMVT	964:968	hSMVT	964:968	Mutating the putative PKC phosphorylation site Thr(286) of hSMVT led to a significant decrease in the PMA-induced inhibition in biotin uptake.
21570947	7	21	gly	glycosylated	1257:1268	arg1	protein					1246:1252	the hSMVT protein	1236:1252	the hSMVT protein	1236:1252	These findings demonstrate that the hSMVT protein is glycosylated, and that glycosylation is important for its function.
21570947	5	22	theme	biotin	1033:1038	arg1	uptake					1040:1045	biotin uptake	1033:1045	biotin uptake	1033:1045	Mutating the putative PKC phosphorylation site Thr(286) of hSMVT led to a significant decrease in the PMA-induced inhibition in biotin uptake.
21570947	2	23	gly	N-glycosylation	357:371	arg2	four					352:355	four	352:355	four	352:355	The human SMVT (hSMVT) polypeptide is predicted to have four N-glycosylation sites and two putative PKC phosphorylation sites but their role in the function and regulation of the protein is not known and was examined in this investigation.
21570947	2	23	gly	N-glycosylation	357:371	arg2	sites					373:377	four N-glycosylation sites	352:377	four N-glycosylation sites	352:377	The human SMVT (hSMVT) polypeptide is predicted to have four N-glycosylation sites and two putative PKC phosphorylation sites but their role in the function and regulation of the protein is not known and was examined in this investigation.
21570947	4	24	from	positions	740:748	arg1	important					776:784	important	776:784	important	776:784	Studies utilizing site-directed mutagenesis revealed that the N-glycosylation sites at positions Asn(138) and Asn(489) are important for the function of hSMVT and that mutating these sites significantly reduces the V(max) of the biotin uptake process.
21570947	4	24	from	positions	740:748	arg1	sites					731:735	the N-glycosylation sites	711:735	the N-glycosylation sites at positions Asn(138) and Asn(489)	711:770	Studies utilizing site-directed mutagenesis revealed that the N-glycosylation sites at positions Asn(138) and Asn(489) are important for the function of hSMVT and that mutating these sites significantly reduces the V(max) of the biotin uptake process.
21570947	3	25	gly	glycosylated	581:592	arg1	protein					570:576	the hSMVT protein	560:576	the hSMVT protein	560:576	Our results showed that the hSMVT protein is glycosylated and that this glycosylation is important for its function.
21570947	8	26	from	site	1398:1401	arg1	regulation					1441:1450	the PKC-mediated regulation	1424:1450	the PKC-mediated regulation of biotin uptake	1424:1467	Furthermore, the study shows a role for the putative PKC-phosphorylation site Thr(286) of hSMVT in the PKC-mediated regulation of biotin uptake.
21570947	4	27	theme	hSMVT	806:810	arg1	function					794:801	the function	790:801	the function of hSMVT	790:810	Studies utilizing site-directed mutagenesis revealed that the N-glycosylation sites at positions Asn(138) and Asn(489) are important for the function of hSMVT and that mutating these sites significantly reduces the V(max) of the biotin uptake process.
21570947	2	28	theme	SMVT	306:309	arg1	polypeptide					319:329	The human SMVT (hSMVT) polypeptide	296:329	The human SMVT (hSMVT) polypeptide	296:329	The human SMVT (hSMVT) polypeptide is predicted to have four N-glycosylation sites and two putative PKC phosphorylation sites but their role in the function and regulation of the protein is not known and was examined in this investigation.
21570947	2	29	theme	N-glycosylation	357:371	arg1	sites					373:377	four N-glycosylation sites	352:377	four N-glycosylation sites	352:377	The human SMVT (hSMVT) polypeptide is predicted to have four N-glycosylation sites and two putative PKC phosphorylation sites but their role in the function and regulation of the protein is not known and was examined in this investigation.
21570947	0	30	theme	putative	12:19	arg1	N-glycosylation					21:35	the putative N-glycosylation and PKC-phosphorylation sites	8:65	N-glycosylation	21:35	Role of the putative N-glycosylation and PKC-phosphorylation sites of the human sodium-dependent multivitamin transporter (hSMVT) in function and regulation.
21570947	1	31	theme	small	279:283	arg1	intestine					285:293	the small intestine	275:293	the small intestine	275:293	The sodium-dependent multivitamin transporter (SMVT) is a major biotin transporter in a variety of tissues including the small intestine.
21570947	2	32	theme	human	300:304	arg1	polypeptide					319:329	The human SMVT (hSMVT) polypeptide	296:329	The human SMVT (hSMVT) polypeptide	296:329	The human SMVT (hSMVT) polypeptide is predicted to have four N-glycosylation sites and two putative PKC phosphorylation sites but their role in the function and regulation of the protein is not known and was examined in this investigation.
21570947	5	33	dep	site	947:950	arg1	Thr					952:954	Thr(286)	952:959	the putative PKC phosphorylation site Thr(286) of hSMVT	914:968	Mutating the putative PKC phosphorylation site Thr(286) of hSMVT led to a significant decrease in the PMA-induced inhibition in biotin uptake.
21570947	5	34	from	inhibition	1019:1028	arg1	uptake					1040:1045	biotin uptake	1033:1045	biotin uptake	1033:1045	Mutating the putative PKC phosphorylation site Thr(286) of hSMVT led to a significant decrease in the PMA-induced inhibition in biotin uptake.
21570947	8	35	theme	PKC-mediated	1428:1439	arg1	regulation					1441:1450	the PKC-mediated regulation	1424:1450	the PKC-mediated regulation of biotin uptake	1424:1467	Furthermore, the study shows a role for the putative PKC-phosphorylation site Thr(286) of hSMVT in the PKC-mediated regulation of biotin uptake.
21570947	5	36	theme	significant	979:989	arg1	decrease					991:998	a significant decrease	977:998	a significant decrease in the PMA-induced inhibition in biotin uptake	977:1045	Mutating the putative PKC phosphorylation site Thr(286) of hSMVT led to a significant decrease in the PMA-induced inhibition in biotin uptake.
21570947	4	37	theme	site-directed	671:683	arg1	mutagenesis					685:695	site-directed mutagenesis	671:695	site-directed mutagenesis	671:695	Studies utilizing site-directed mutagenesis revealed that the N-glycosylation sites at positions Asn(138) and Asn(489) are important for the function of hSMVT and that mutating these sites significantly reduces the V(max) of the biotin uptake process.
21570947	2	38	theme	phosphorylation	400:414	arg1	sites					416:420	two putative PKC phosphorylation sites	383:420	two putative PKC phosphorylation sites	383:420	The human SMVT (hSMVT) polypeptide is predicted to have four N-glycosylation sites and two putative PKC phosphorylation sites but their role in the function and regulation of the protein is not known and was examined in this investigation.
21570947	8	39	theme	biotin	1455:1460	arg1	uptake					1462:1467	biotin uptake	1455:1467	biotin uptake	1455:1467	Furthermore, the study shows a role for the putative PKC-phosphorylation site Thr(286) of hSMVT in the PKC-mediated regulation of biotin uptake.
21570947	3	40	theme	hSMVT	564:568	arg1	protein					570:576	the hSMVT protein	560:576	the hSMVT protein	560:576	Our results showed that the hSMVT protein is glycosylated and that this glycosylation is important for its function.
21570947	2	41	theme	PKC	396:398	arg1	sites					416:420	two putative PKC phosphorylation sites	383:420	two putative PKC phosphorylation sites	383:420	The human SMVT (hSMVT) polypeptide is predicted to have four N-glycosylation sites and two putative PKC phosphorylation sites but their role in the function and regulation of the protein is not known and was examined in this investigation.
21570947	0	42	theme	N-glycosylation	21:35	arg1	Role					0:3	Role	0:3	Role of the putative N-glycosylation and PKC-phosphorylation sites of the human sodium-dependent multivitamin transporter (hSMVT) in function and regulation.	0:156	Role of the putative N-glycosylation and PKC-phosphorylation sites of the human sodium-dependent multivitamin transporter (hSMVT) in function and regulation.
21570947	4	43	gly	N-glycosylation	715:729	arg2	sites					731:735	the N-glycosylation sites	711:735	the N-glycosylation sites at positions Asn(138) and Asn(489)	711:770	Studies utilizing site-directed mutagenesis revealed that the N-glycosylation sites at positions Asn(138) and Asn(489) are important for the function of hSMVT and that mutating these sites significantly reduces the V(max) of the biotin uptake process.
21570947	4	43	gly	N-glycosylation	715:729	arg2	important					776:784	important	776:784	important	776:784	Studies utilizing site-directed mutagenesis revealed that the N-glycosylation sites at positions Asn(138) and Asn(489) are important for the function of hSMVT and that mutating these sites significantly reduces the V(max) of the biotin uptake process.
21570947	4	43	gly	N-glycosylation	715:729	arg2	Asn					750:752	Asn(138)	750:757	Asn(138)	750:757	Studies utilizing site-directed mutagenesis revealed that the N-glycosylation sites at positions Asn(138) and Asn(489) are important for the function of hSMVT and that mutating these sites significantly reduces the V(max) of the biotin uptake process.
21570947	4	43	gly	N-glycosylation	715:729	arg2	Asn					763:765	Asn(489)	763:770	Asn(489)	763:770	Studies utilizing site-directed mutagenesis revealed that the N-glycosylation sites at positions Asn(138) and Asn(489) are important for the function of hSMVT and that mutating these sites significantly reduces the V(max) of the biotin uptake process.
21570947	4	43	gly	N-glycosylation	715:729	arg2	positions					740:748	positions Asn(138) and Asn(489)	740:770	positions Asn(138) and Asn(489)	740:770	Studies utilizing site-directed mutagenesis revealed that the N-glycosylation sites at positions Asn(138) and Asn(489) are important for the function of hSMVT and that mutating these sites significantly reduces the V(max) of the biotin uptake process.
21570947	6	44	theme	protein	1135:1141	arg1	expression					1111:1120	expression	1111:1120	expression of the hSMVT protein and mRNA	1111:1150	The latter effect was not mediated via changes in the level of expression of the hSMVT protein and mRNA or in its level of expression at the cell membrane.
21570947	1	45	theme	major	216:220	arg1	transporter					229:239	a major biotin transporter	214:239	a major biotin transporter in a variety of tissues including the small intestine	214:293	The sodium-dependent multivitamin transporter (SMVT) is a major biotin transporter in a variety of tissues including the small intestine.
21570947	1	45	theme	major	216:220	arg1	transporter					192:202	The sodium-dependent multivitamin transporter	158:202	The sodium-dependent multivitamin transporter (SMVT)	158:209	The sodium-dependent multivitamin transporter (SMVT) is a major biotin transporter in a variety of tissues including the small intestine.
21570947	0	46	theme	sites	61:65	arg1	Role					0:3	Role	0:3	Role of the putative N-glycosylation and PKC-phosphorylation sites of the human sodium-dependent multivitamin transporter (hSMVT) in function and regulation.	0:156	Role of the putative N-glycosylation and PKC-phosphorylation sites of the human sodium-dependent multivitamin transporter (hSMVT) in function and regulation.
21570947	4	47	theme	biotin	882:887	arg1	process					896:902	the biotin uptake process	878:902	the biotin uptake process	878:902	Studies utilizing site-directed mutagenesis revealed that the N-glycosylation sites at positions Asn(138) and Asn(489) are important for the function of hSMVT and that mutating these sites significantly reduces the V(max) of the biotin uptake process.
21570947	8	48	theme	hSMVT	1415:1419	arg1	site					1398:1401	the putative PKC-phosphorylation site Thr(286)	1365:1410	the putative PKC-phosphorylation site Thr(286) of hSMVT in the PKC-mediated regulation of biotin uptake	1365:1467	Furthermore, the study shows a role for the putative PKC-phosphorylation site Thr(286) of hSMVT in the PKC-mediated regulation of biotin uptake.
21570947	8	48	theme	hSMVT	1415:1419	arg1	hSMVT					1415:1419	hSMVT	1415:1419	hSMVT	1415:1419	Furthermore, the study shows a role for the putative PKC-phosphorylation site Thr(286) of hSMVT in the PKC-mediated regulation of biotin uptake.
21570947	6	49	theme	hSMVT	1129:1133	arg1	protein					1135:1141	the hSMVT protein	1125:1141	the hSMVT protein	1125:1141	The latter effect was not mediated via changes in the level of expression of the hSMVT protein and mRNA or in its level of expression at the cell membrane.
21570947	6	50	theme	latter	1052:1057	arg1	effect					1059:1064	The latter effect	1048:1064	The latter effect	1048:1064	The latter effect was not mediated via changes in the level of expression of the hSMVT protein and mRNA or in its level of expression at the cell membrane.
21570947	0	51	theme	PKC-phosphorylation	41:59	arg1	transporter					110:120	the human sodium-dependent multivitamin transporter	70:120	the human sodium-dependent multivitamin transporter (hSMVT)	70:128	Role of the putative N-glycosylation and PKC-phosphorylation sites of the human sodium-dependent multivitamin transporter (hSMVT) in function and regulation.
21570947	0	51	theme	PKC-phosphorylation	41:59	arg1	sites					61:65	the putative N-glycosylation and PKC-phosphorylation sites	8:65	sites	61:65	Role of the putative N-glycosylation and PKC-phosphorylation sites of the human sodium-dependent multivitamin transporter (hSMVT) in function and regulation.
21570947	8	52	theme	uptake	1462:1467	arg1	regulation					1441:1450	the PKC-mediated regulation	1424:1450	the PKC-mediated regulation of biotin uptake	1424:1467	Furthermore, the study shows a role for the putative PKC-phosphorylation site Thr(286) of hSMVT in the PKC-mediated regulation of biotin uptake.
21570947	5	53	theme	hSMVT	964:968	arg1	site					947:950	the putative PKC phosphorylation site	914:950	the putative PKC phosphorylation site Thr(286) of hSMVT	914:968	Mutating the putative PKC phosphorylation site Thr(286) of hSMVT led to a significant decrease in the PMA-induced inhibition in biotin uptake.
21570947	5	53	theme	hSMVT	964:968	arg1	hSMVT					964:968	hSMVT	964:968	hSMVT	964:968	Mutating the putative PKC phosphorylation site Thr(286) of hSMVT led to a significant decrease in the PMA-induced inhibition in biotin uptake.
21570947	4	54	dep	positions	740:748	arg1	positions					740:748	positions Asn(138) and Asn(489)	740:770	positions Asn(138) and Asn(489)	740:770	Studies utilizing site-directed mutagenesis revealed that the N-glycosylation sites at positions Asn(138) and Asn(489) are important for the function of hSMVT and that mutating these sites significantly reduces the V(max) of the biotin uptake process.
21570947	4	54	dep	positions	740:748	arg1	Asn					763:765	Asn(489)	763:770	Asn(489)	763:770	Studies utilizing site-directed mutagenesis revealed that the N-glycosylation sites at positions Asn(138) and Asn(489) are important for the function of hSMVT and that mutating these sites significantly reduces the V(max) of the biotin uptake process.
21570947	4	54	dep	positions	740:748	arg1	Asn					750:752	Asn(138)	750:757	Asn(138)	750:757	Studies utilizing site-directed mutagenesis revealed that the N-glycosylation sites at positions Asn(138) and Asn(489) are important for the function of hSMVT and that mutating these sites significantly reduces the V(max) of the biotin uptake process.
21570947	6	55	from	membrane	1194:1201	arg1	expression					1171:1180	expression	1171:1180	expression at the cell membrane	1171:1201	The latter effect was not mediated via changes in the level of expression of the hSMVT protein and mRNA or in its level of expression at the cell membrane.
21570947	6	55	from	membrane	1194:1201	arg1	level					1162:1166	its level	1158:1166	its level of expression at the cell membrane	1158:1201	The latter effect was not mediated via changes in the level of expression of the hSMVT protein and mRNA or in its level of expression at the cell membrane.
21570947	6	56	theme	cell	1189:1192	arg1	membrane					1194:1201	the cell membrane	1185:1201	the cell membrane	1185:1201	The latter effect was not mediated via changes in the level of expression of the hSMVT protein and mRNA or in its level of expression at the cell membrane.
21570947	5	57	theme	PKC	927:929	arg1	site					947:950	the putative PKC phosphorylation site	914:950	the putative PKC phosphorylation site Thr(286) of hSMVT	914:968	Mutating the putative PKC phosphorylation site Thr(286) of hSMVT led to a significant decrease in the PMA-induced inhibition in biotin uptake.
21570947	5	57	theme	PKC	927:929	arg1	hSMVT					964:968	hSMVT	964:968	hSMVT	964:968	Mutating the putative PKC phosphorylation site Thr(286) of hSMVT led to a significant decrease in the PMA-induced inhibition in biotin uptake.
21570947	0	58	gly	N-glycosylation	21:35	arg1	transporter					110:120	the human sodium-dependent multivitamin transporter	70:120	the human sodium-dependent multivitamin transporter (hSMVT)	70:128	Role of the putative N-glycosylation and PKC-phosphorylation sites of the human sodium-dependent multivitamin transporter (hSMVT) in function and regulation.
21570947	0	58	gly	N-glycosylation	21:35	arg1	hSMVT					123:127	hSMVT	123:127	hSMVT	123:127	Role of the putative N-glycosylation and PKC-phosphorylation sites of the human sodium-dependent multivitamin transporter (hSMVT) in function and regulation.
21570947	4	59	theme	N-glycosylation	715:729	arg1	important					776:784	important	776:784	important	776:784	Studies utilizing site-directed mutagenesis revealed that the N-glycosylation sites at positions Asn(138) and Asn(489) are important for the function of hSMVT and that mutating these sites significantly reduces the V(max) of the biotin uptake process.
21570947	4	59	theme	N-glycosylation	715:729	arg1	sites					731:735	the N-glycosylation sites	711:735	the N-glycosylation sites at positions Asn(138) and Asn(489)	711:770	Studies utilizing site-directed mutagenesis revealed that the N-glycosylation sites at positions Asn(138) and Asn(489) are important for the function of hSMVT and that mutating these sites significantly reduces the V(max) of the biotin uptake process.
21570947	1	60	theme	biotin	222:227	arg1	transporter					229:239	a major biotin transporter	214:239	a major biotin transporter in a variety of tissues including the small intestine	214:293	The sodium-dependent multivitamin transporter (SMVT) is a major biotin transporter in a variety of tissues including the small intestine.
21570947	1	60	theme	biotin	222:227	arg1	transporter					192:202	The sodium-dependent multivitamin transporter	158:202	The sodium-dependent multivitamin transporter (SMVT)	158:209	The sodium-dependent multivitamin transporter (SMVT) is a major biotin transporter in a variety of tissues including the small intestine.
21570947	1	61	from	transporter	229:239	arg1	intestine					285:293	the small intestine	275:293	the small intestine	275:293	The sodium-dependent multivitamin transporter (SMVT) is a major biotin transporter in a variety of tissues including the small intestine.
21570947	1	61	from	transporter	229:239	arg1	tissues					257:263	tissues	257:263	tissues including the small intestine	257:293	The sodium-dependent multivitamin transporter (SMVT) is a major biotin transporter in a variety of tissues including the small intestine.
21570947	1	61	from	transporter	229:239	arg1	variety					246:252	a variety	244:252	a variety of tissues including the small intestine	244:293	The sodium-dependent multivitamin transporter (SMVT) is a major biotin transporter in a variety of tissues including the small intestine.
21570947	5	62	theme	phosphorylation	931:945	arg1	site					947:950	the putative PKC phosphorylation site	914:950	the putative PKC phosphorylation site Thr(286) of hSMVT	914:968	Mutating the putative PKC phosphorylation site Thr(286) of hSMVT led to a significant decrease in the PMA-induced inhibition in biotin uptake.
21570947	5	62	theme	phosphorylation	931:945	arg1	hSMVT					964:968	hSMVT	964:968	hSMVT	964:968	Mutating the putative PKC phosphorylation site Thr(286) of hSMVT led to a significant decrease in the PMA-induced inhibition in biotin uptake.
21570947	8	63	theme	putative	1369:1376	arg1	site					1398:1401	the putative PKC-phosphorylation site Thr(286)	1365:1410	the putative PKC-phosphorylation site Thr(286) of hSMVT in the PKC-mediated regulation of biotin uptake	1365:1467	Furthermore, the study shows a role for the putative PKC-phosphorylation site Thr(286) of hSMVT in the PKC-mediated regulation of biotin uptake.
21570947	8	63	theme	putative	1369:1376	arg1	hSMVT					1415:1419	hSMVT	1415:1419	hSMVT	1415:1419	Furthermore, the study shows a role for the putative PKC-phosphorylation site Thr(286) of hSMVT in the PKC-mediated regulation of biotin uptake.
21570947	2	64	theme	hSMVT	312:316	arg1	polypeptide					319:329	The human SMVT (hSMVT) polypeptide	296:329	The human SMVT (hSMVT) polypeptide	296:329	The human SMVT (hSMVT) polypeptide is predicted to have four N-glycosylation sites and two putative PKC phosphorylation sites but their role in the function and regulation of the protein is not known and was examined in this investigation.
21570947	6	65	from	level	1162:1166	arg1	membrane					1194:1201	the cell membrane	1185:1201	the cell membrane	1185:1201	The latter effect was not mediated via changes in the level of expression of the hSMVT protein and mRNA or in its level of expression at the cell membrane.
21570947	2	66	theme	putative	387:394	arg1	sites					416:420	two putative PKC phosphorylation sites	383:420	two putative PKC phosphorylation sites	383:420	The human SMVT (hSMVT) polypeptide is predicted to have four N-glycosylation sites and two putative PKC phosphorylation sites but their role in the function and regulation of the protein is not known and was examined in this investigation.
21570947	2	67	theme	protein	475:481	arg1	function					444:451	function	444:451	function	444:451	The human SMVT (hSMVT) polypeptide is predicted to have four N-glycosylation sites and two putative PKC phosphorylation sites but their role in the function and regulation of the protein is not known and was examined in this investigation.
21570947	2	67	theme	protein	475:481	arg1	regulation					457:466	regulation	457:466	regulation	457:466	The human SMVT (hSMVT) polypeptide is predicted to have four N-glycosylation sites and two putative PKC phosphorylation sites but their role in the function and regulation of the protein is not known and was examined in this investigation.
21570947	8	68	theme	PKC-phosphorylation	1378:1396	arg1	site					1398:1401	the putative PKC-phosphorylation site Thr(286)	1365:1410	the putative PKC-phosphorylation site Thr(286) of hSMVT in the PKC-mediated regulation of biotin uptake	1365:1467	Furthermore, the study shows a role for the putative PKC-phosphorylation site Thr(286) of hSMVT in the PKC-mediated regulation of biotin uptake.
21570947	8	68	theme	PKC-phosphorylation	1378:1396	arg1	hSMVT					1415:1419	hSMVT	1415:1419	hSMVT	1415:1419	Furthermore, the study shows a role for the putative PKC-phosphorylation site Thr(286) of hSMVT in the PKC-mediated regulation of biotin uptake.
21570947	7	69	theme	hSMVT	1240:1244	arg1	protein					1246:1252	the hSMVT protein	1236:1252	the hSMVT protein	1236:1252	These findings demonstrate that the hSMVT protein is glycosylated, and that glycosylation is important for its function.
23234360	6	0	theme	future	1300:1305	arg1	studies					1307:1313	future studies	1300:1313	future studies addressing the biological and diagnostic importance of specific protein glycosylations in relation to human disease	1300:1429	The characterization of glycans and glycosylation sites in glycoproteins from human clinical samples provides a basis for future studies addressing the biological and diagnostic importance of specific protein glycosylations in relation to human disease.
23234360	4	1	used	used	786:789	arg2	We					783:784	We	783:784	We	783:784	We used electron-capture and -transfer dissociation (ECD/ETD) to pinpoint the glycosylation site(s) of the glycopeptides, identified as predominantly core-1-like HexHexNAc-O- structure attached to one to four Ser/Thr residues.
23234360	4	2	theme	core-1-like	933:943	arg1	structure					958:966	predominantly core-1-like HexHexNAc-O- structure	919:966	predominantly core-1-like HexHexNAc-O- structure attached to one to four Ser/Thr residues	919:1007	We used electron-capture and -transfer dissociation (ECD/ETD) to pinpoint the glycosylation site(s) of the glycopeptides, identified as predominantly core-1-like HexHexNAc-O- structure attached to one to four Ser/Thr residues.
23234360	2	3	from	fluid	385:389	arg1	O-glycopeptides					344:358	O-glycopeptides	344:358	O-glycopeptides from human cerebrospinal fluid	344:389	We previously reported a sialic acid capture-and-release protocol to enrich tryptic N- and O-glycopeptides from human cerebrospinal fluid glycoproteins using nano-LC-ESI-MS/MS with collision-induced dissociation (CID) for glycopeptide characterization.
23234360	2	3	from	fluid	385:389	arg1	N-					337:338	tryptic N-	329:338	tryptic N-	329:338	We previously reported a sialic acid capture-and-release protocol to enrich tryptic N- and O-glycopeptides from human cerebrospinal fluid glycoproteins using nano-LC-ESI-MS/MS with collision-induced dissociation (CID) for glycopeptide characterization.
23234360	6	4	gly	glycoproteins	1237:1249	arg1	glycoproteins					1237:1249	glycoproteins	1237:1249	glycoproteins from human clinical samples	1237:1277	The characterization of glycans and glycosylation sites in glycoproteins from human clinical samples provides a basis for future studies addressing the biological and diagnostic importance of specific protein glycosylations in relation to human disease.
23234360	3	5	theme	glycopeptide	754:765	arg1	identification					767:780	glycopeptide identification	754:780	glycopeptide identification	754:780	Here, we have introduced peptide N-glycosidase F (PNGase F) pretreatment of CSF samples to remove the N-glycans facilitating the selective characterization of O-glycopeptides and enabling the use of an automated CID-MS(2)/MS(3) search protocol for glycopeptide identification.
23234360	6	6	theme	clinical	1262:1269	arg1	samples					1271:1277	human clinical samples	1256:1277	human clinical samples	1256:1277	The characterization of glycans and glycosylation sites in glycoproteins from human clinical samples provides a basis for future studies addressing the biological and diagnostic importance of specific protein glycosylations in relation to human disease.
23234360	2	7	theme	O-glycopeptides	344:358	arg1	glycoproteins					391:403	tryptic N- and O-glycopeptides from human cerebrospinal fluid glycoproteins	329:403	tryptic N- and O-glycopeptides from human cerebrospinal fluid glycoproteins using nano-LC-ESI-MS/MS with collision-induced dissociation (CID) for glycopeptide characterization	329:503	We previously reported a sialic acid capture-and-release protocol to enrich tryptic N- and O-glycopeptides from human cerebrospinal fluid glycoproteins using nano-LC-ESI-MS/MS with collision-induced dissociation (CID) for glycopeptide characterization.
23234360	1	8	gly	O-glycosylation	128:142	arg1	residues					155:162	Ser/Thr residues	147:162	Ser/Thr residues of extracellular proteins	147:188	The GalNAc O-glycosylation on Ser/Thr residues of extracellular proteins has not been well characterized from a proteomics perspective.
23234360	1	8	gly	O-glycosylation	128:142	arg1	proteins					181:188	extracellular proteins	167:188	extracellular proteins	167:188	The GalNAc O-glycosylation on Ser/Thr residues of extracellular proteins has not been well characterized from a proteomics perspective.
23234360	2	9	theme	N-	337:338	arg1	glycoproteins					391:403	tryptic N- and O-glycopeptides from human cerebrospinal fluid glycoproteins	329:403	tryptic N- and O-glycopeptides from human cerebrospinal fluid glycoproteins using nano-LC-ESI-MS/MS with collision-induced dissociation (CID) for glycopeptide characterization	329:503	We previously reported a sialic acid capture-and-release protocol to enrich tryptic N- and O-glycopeptides from human cerebrospinal fluid glycoproteins using nano-LC-ESI-MS/MS with collision-induced dissociation (CID) for glycopeptide characterization.
23234360	4	10	theme	Ser/Thr	992:998	arg1	residues					1000:1007	one to four Ser/Thr residues	980:1007	one to four Ser/Thr residues	980:1007	We used electron-capture and -transfer dissociation (ECD/ETD) to pinpoint the glycosylation site(s) of the glycopeptides, identified as predominantly core-1-like HexHexNAc-O- structure attached to one to four Ser/Thr residues.
23234360	6	11	theme	human	1256:1260	arg1	samples					1271:1277	human clinical samples	1256:1277	human clinical samples	1256:1277	The characterization of glycans and glycosylation sites in glycoproteins from human clinical samples provides a basis for future studies addressing the biological and diagnostic importance of specific protein glycosylations in relation to human disease.
23234360	3	12	gly	O-glycopeptides	665:679	arg2	O-glycopeptides					665:679	O-glycopeptides	665:679	O-glycopeptides	665:679	Here, we have introduced peptide N-glycosidase F (PNGase F) pretreatment of CSF samples to remove the N-glycans facilitating the selective characterization of O-glycopeptides and enabling the use of an automated CID-MS(2)/MS(3) search protocol for glycopeptide identification.
23234360	6	13	theme	diagnostic	1345:1354	arg1	importance					1356:1365	the biological and diagnostic importance	1326:1365	the biological and diagnostic importance of specific protein glycosylations in relation to human disease	1326:1429	The characterization of glycans and glycosylation sites in glycoproteins from human clinical samples provides a basis for future studies addressing the biological and diagnostic importance of specific protein glycosylations in relation to human disease.
23234360	6	14	theme	biological	1330:1339	arg1	importance					1356:1365	the biological and diagnostic importance	1326:1365	the biological and diagnostic importance of specific protein glycosylations in relation to human disease	1326:1429	The characterization of glycans and glycosylation sites in glycoproteins from human clinical samples provides a basis for future studies addressing the biological and diagnostic importance of specific protein glycosylations in relation to human disease.
23234360	3	15	theme	O-glycopeptides	665:679	arg1	characterization					645:660	the selective characterization	631:660	the selective characterization of O-glycopeptides	631:679	Here, we have introduced peptide N-glycosidase F (PNGase F) pretreatment of CSF samples to remove the N-glycans facilitating the selective characterization of O-glycopeptides and enabling the use of an automated CID-MS(2)/MS(3) search protocol for glycopeptide identification.
23234360	6	16	theme	sites	1228:1232	arg1	characterization					1182:1197	The characterization	1178:1197	The characterization of glycans and glycosylation sites in glycoproteins from human clinical samples	1178:1277	The characterization of glycans and glycosylation sites in glycoproteins from human clinical samples provides a basis for future studies addressing the biological and diagnostic importance of specific protein glycosylations in relation to human disease.
23234360	2	17	theme	acid	285:288	arg1	protocol					310:317	a sialic acid capture-and-release protocol	276:317	a sialic acid capture-and-release protocol to enrich tryptic N- and O-glycopeptides from human cerebrospinal fluid glycoproteins using nano-LC-ESI-MS/MS with collision-induced dissociation (CID) for glycopeptide characterization	276:503	We previously reported a sialic acid capture-and-release protocol to enrich tryptic N- and O-glycopeptides from human cerebrospinal fluid glycoproteins using nano-LC-ESI-MS/MS with collision-induced dissociation (CID) for glycopeptide characterization.
23234360	3	18	dep	N-glycans	608:616	arg1	enabling					685:692	enabling	685:692	enabling the use of an automated CID-MS(2)/MS(3) search protocol for glycopeptide identification	685:780	Here, we have introduced peptide N-glycosidase F (PNGase F) pretreatment of CSF samples to remove the N-glycans facilitating the selective characterization of O-glycopeptides and enabling the use of an automated CID-MS(2)/MS(3) search protocol for glycopeptide identification.
23234360	3	18	dep	N-glycans	608:616	arg1	facilitating					618:629	facilitating	618:629	facilitating the selective characterization of O-glycopeptides	618:679	Here, we have introduced peptide N-glycosidase F (PNGase F) pretreatment of CSF samples to remove the N-glycans facilitating the selective characterization of O-glycopeptides and enabling the use of an automated CID-MS(2)/MS(3) search protocol for glycopeptide identification.
23234360	1	19	theme	extracellular	167:179	arg1	proteins					181:188	extracellular proteins	167:188	extracellular proteins	167:188	The GalNAc O-glycosylation on Ser/Thr residues of extracellular proteins has not been well characterized from a proteomics perspective.
23234360	6	20	from	glycans	1202:1208	arg1	glycoproteins					1237:1249	glycoproteins	1237:1249	glycoproteins from human clinical samples	1237:1277	The characterization of glycans and glycosylation sites in glycoproteins from human clinical samples provides a basis for future studies addressing the biological and diagnostic importance of specific protein glycosylations in relation to human disease.
23234360	6	20	from	glycans	1202:1208	arg1	samples					1271:1277	human clinical samples	1256:1277	human clinical samples	1256:1277	The characterization of glycans and glycosylation sites in glycoproteins from human clinical samples provides a basis for future studies addressing the biological and diagnostic importance of specific protein glycosylations in relation to human disease.
23234360	0	21	theme	cerebrospinal	82:94	arg1	fluid					96:100	human cerebrospinal fluid	76:100	human cerebrospinal fluid glycoproteins	76:114	LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins.
23234360	5	22	theme	Ser/Thr	1149:1155	arg1	n					1174:1174	n	1174:1174	n	1174:1174	We characterized 106 O-glycosylations and found Pro residues preferentially in the n - 1, n + 1, and/or n + 3 positions in relation to the Ser/Thr attachment site (n).
23234360	5	22	theme	Ser/Thr	1149:1155	arg1	site					1168:1171	the Ser/Thr attachment site	1145:1171	the Ser/Thr attachment site (n)	1145:1175	We characterized 106 O-glycosylations and found Pro residues preferentially in the n - 1, n + 1, and/or n + 3 positions in relation to the Ser/Thr attachment site (n).
23234360	0	23	theme	glycoproteins	102:114	arg1	glycoproteins					102:114	human cerebrospinal fluid glycoproteins	76:114	human cerebrospinal fluid glycoproteins	76:114	LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins.
23234360	0	23	theme	glycoproteins	102:114	arg1	sites					45:49	O-glycosylation sites	29:49	O-glycosylation sites	29:49	LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins.
23234360	0	23	theme	glycoproteins	102:114	arg1	structures					62:71	glycan structures	55:71	glycan structures	55:71	LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins.
23234360	6	24	theme	protein	1379:1385	arg1	glycosylations					1387:1400	specific protein glycosylations	1370:1400	specific protein glycosylations	1370:1400	The characterization of glycans and glycosylation sites in glycoproteins from human clinical samples provides a basis for future studies addressing the biological and diagnostic importance of specific protein glycosylations in relation to human disease.
23234360	4	25	theme	electron-capture	791:806	arg1	ECD/ETD					836:842	ECD/ETD	836:842	ECD/ETD	836:842	We used electron-capture and -transfer dissociation (ECD/ETD) to pinpoint the glycosylation site(s) of the glycopeptides, identified as predominantly core-1-like HexHexNAc-O- structure attached to one to four Ser/Thr residues.
23234360	4	25	theme	electron-capture	791:806	arg1	dissociation					822:833	electron-capture and -transfer dissociation	791:833	electron-capture and -transfer dissociation (ECD/ETD)	791:843	We used electron-capture and -transfer dissociation (ECD/ETD) to pinpoint the glycosylation site(s) of the glycopeptides, identified as predominantly core-1-like HexHexNAc-O- structure attached to one to four Ser/Thr residues.
23234360	6	26	from	characterization	1182:1197	arg1	glycoproteins					1237:1249	glycoproteins	1237:1249	glycoproteins from human clinical samples	1237:1277	The characterization of glycans and glycosylation sites in glycoproteins from human clinical samples provides a basis for future studies addressing the biological and diagnostic importance of specific protein glycosylations in relation to human disease.
23234360	0	27	theme	LC-MS/MS	0:7	arg1	characterization					9:24	LC-MS/MS characterization	0:24	LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins.	0:115	LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins.
23234360	6	28	from	importance	1356:1365	arg1	relation					1405:1412	relation	1405:1412	relation to human disease	1405:1429	The characterization of glycans and glycosylation sites in glycoproteins from human clinical samples provides a basis for future studies addressing the biological and diagnostic importance of specific protein glycosylations in relation to human disease.
23234360	1	29	from	O-glycosylation	128:142	arg1	residues					155:162	Ser/Thr residues	147:162	Ser/Thr residues of extracellular proteins	147:188	The GalNAc O-glycosylation on Ser/Thr residues of extracellular proteins has not been well characterized from a proteomics perspective.
23234360	1	29	from	O-glycosylation	128:142	arg1	proteins					181:188	extracellular proteins	167:188	extracellular proteins	167:188	The GalNAc O-glycosylation on Ser/Thr residues of extracellular proteins has not been well characterized from a proteomics perspective.
23234360	4	30	theme	-transfer	812:820	arg1	ECD/ETD					836:842	ECD/ETD	836:842	ECD/ETD	836:842	We used electron-capture and -transfer dissociation (ECD/ETD) to pinpoint the glycosylation site(s) of the glycopeptides, identified as predominantly core-1-like HexHexNAc-O- structure attached to one to four Ser/Thr residues.
23234360	4	30	theme	-transfer	812:820	arg1	dissociation					822:833	electron-capture and -transfer dissociation	791:833	electron-capture and -transfer dissociation (ECD/ETD)	791:843	We used electron-capture and -transfer dissociation (ECD/ETD) to pinpoint the glycosylation site(s) of the glycopeptides, identified as predominantly core-1-like HexHexNAc-O- structure attached to one to four Ser/Thr residues.
23234360	3	31	theme	N-glycosidase	539:551	arg1	F					563:563	PNGase F	556:563	PNGase F	556:563	Here, we have introduced peptide N-glycosidase F (PNGase F) pretreatment of CSF samples to remove the N-glycans facilitating the selective characterization of O-glycopeptides and enabling the use of an automated CID-MS(2)/MS(3) search protocol for glycopeptide identification.
23234360	3	31	theme	N-glycosidase	539:551	arg1	F					553:553	peptide N-glycosidase F	531:553	peptide N-glycosidase F (PNGase F) pretreatment of CSF samples	531:592	Here, we have introduced peptide N-glycosidase F (PNGase F) pretreatment of CSF samples to remove the N-glycans facilitating the selective characterization of O-glycopeptides and enabling the use of an automated CID-MS(2)/MS(3) search protocol for glycopeptide identification.
23234360	5	32	from	positions	1120:1128	arg1	relation					1133:1140	relation	1133:1140	relation to the Ser/Thr attachment site (n)	1133:1175	We characterized 106 O-glycosylations and found Pro residues preferentially in the n - 1, n + 1, and/or n + 3 positions in relation to the Ser/Thr attachment site (n).
23234360	1	33	theme	GalNAc	121:126	arg1	O-glycosylation					128:142	The GalNAc O-glycosylation	117:142	The GalNAc O-glycosylation on Ser/Thr residues of extracellular proteins	117:188	The GalNAc O-glycosylation on Ser/Thr residues of extracellular proteins has not been well characterized from a proteomics perspective.
23234360	4	34	attach	attached	968:975	arg1	residues					1000:1007	one to four Ser/Thr residues	980:1007	one to four Ser/Thr residues	980:1007	We used electron-capture and -transfer dissociation (ECD/ETD) to pinpoint the glycosylation site(s) of the glycopeptides, identified as predominantly core-1-like HexHexNAc-O- structure attached to one to four Ser/Thr residues.
23234360	4	34	attach	attached	968:975	arg2	structure					958:966	predominantly core-1-like HexHexNAc-O- structure	919:966	predominantly core-1-like HexHexNAc-O- structure attached to one to four Ser/Thr residues	919:1007	We used electron-capture and -transfer dissociation (ECD/ETD) to pinpoint the glycosylation site(s) of the glycopeptides, identified as predominantly core-1-like HexHexNAc-O- structure attached to one to four Ser/Thr residues.
23234360	3	35	gly	glycopeptide	754:765	arg2	glycopeptide					754:765	glycopeptide identification	754:780	glycopeptide identification	754:780	Here, we have introduced peptide N-glycosidase F (PNGase F) pretreatment of CSF samples to remove the N-glycans facilitating the selective characterization of O-glycopeptides and enabling the use of an automated CID-MS(2)/MS(3) search protocol for glycopeptide identification.
23234360	2	36	theme	glycopeptide	475:486	arg1	characterization					488:503	glycopeptide characterization	475:503	glycopeptide characterization	475:503	We previously reported a sialic acid capture-and-release protocol to enrich tryptic N- and O-glycopeptides from human cerebrospinal fluid glycoproteins using nano-LC-ESI-MS/MS with collision-induced dissociation (CID) for glycopeptide characterization.
23234360	0	37	theme	sites	45:49	arg1	characterization					9:24	LC-MS/MS characterization	0:24	LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins.	0:115	LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins.
23234360	3	38	theme	CID-MS	718:723	arg1	protocol					741:748	an automated CID-MS(2)/MS(3) search protocol	705:748	an automated CID-MS(2)/MS(3) search protocol for glycopeptide identification	705:780	Here, we have introduced peptide N-glycosidase F (PNGase F) pretreatment of CSF samples to remove the N-glycans facilitating the selective characterization of O-glycopeptides and enabling the use of an automated CID-MS(2)/MS(3) search protocol for glycopeptide identification.
23234360	4	39	gly	glycosylation	861:873	arg1	glycopeptides					890:902	the glycopeptides	886:902	the glycopeptides	886:902	We used electron-capture and -transfer dissociation (ECD/ETD) to pinpoint the glycosylation site(s) of the glycopeptides, identified as predominantly core-1-like HexHexNAc-O- structure attached to one to four Ser/Thr residues.
23234360	4	39	gly	glycosylation	861:873	arg2	s					880:880	s	880:880	s	880:880	We used electron-capture and -transfer dissociation (ECD/ETD) to pinpoint the glycosylation site(s) of the glycopeptides, identified as predominantly core-1-like HexHexNAc-O- structure attached to one to four Ser/Thr residues.
23234360	4	39	gly	glycosylation	861:873	arg2	site					875:878	the glycosylation site	857:878	the glycosylation site(s)	857:881	We used electron-capture and -transfer dissociation (ECD/ETD) to pinpoint the glycosylation site(s) of the glycopeptides, identified as predominantly core-1-like HexHexNAc-O- structure attached to one to four Ser/Thr residues.
23234360	4	39	gly	glycosylation	861:873	arg2	glycopeptides					890:902	the glycopeptides	886:902	the glycopeptides	886:902	We used electron-capture and -transfer dissociation (ECD/ETD) to pinpoint the glycosylation site(s) of the glycopeptides, identified as predominantly core-1-like HexHexNAc-O- structure attached to one to four Ser/Thr residues.
23234360	2	40	with	nano-LC-ESI-MS/MS	411:427	arg1	CID					466:468	CID	466:468	CID	466:468	We previously reported a sialic acid capture-and-release protocol to enrich tryptic N- and O-glycopeptides from human cerebrospinal fluid glycoproteins using nano-LC-ESI-MS/MS with collision-induced dissociation (CID) for glycopeptide characterization.
23234360	2	40	with	nano-LC-ESI-MS/MS	411:427	arg1	dissociation					452:463	collision-induced dissociation	434:463	collision-induced dissociation (CID)	434:469	We previously reported a sialic acid capture-and-release protocol to enrich tryptic N- and O-glycopeptides from human cerebrospinal fluid glycoproteins using nano-LC-ESI-MS/MS with collision-induced dissociation (CID) for glycopeptide characterization.
23234360	0	41	gly	O-glycosylation	29:43	arg2	sites					45:49	O-glycosylation sites	29:49	O-glycosylation sites	29:49	LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins.
23234360	0	41	gly	O-glycosylation	29:43	arg1	glycoproteins					102:114	human cerebrospinal fluid glycoproteins	76:114	human cerebrospinal fluid glycoproteins	76:114	LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins.
23234360	0	41	gly	O-glycosylation	29:43	arg2	glycoproteins					102:114	human cerebrospinal fluid glycoproteins	76:114	human cerebrospinal fluid glycoproteins	76:114	LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins.
23234360	2	42	theme	cerebrospinal	371:383	arg1	fluid					385:389	human cerebrospinal fluid	365:389	human cerebrospinal fluid	365:389	We previously reported a sialic acid capture-and-release protocol to enrich tryptic N- and O-glycopeptides from human cerebrospinal fluid glycoproteins using nano-LC-ESI-MS/MS with collision-induced dissociation (CID) for glycopeptide characterization.
23234360	6	43	gly	glycosylation	1214:1226	arg2	sites					1228:1232	glycosylation sites	1214:1232	glycosylation sites in glycoproteins from human clinical samples	1214:1277	The characterization of glycans and glycosylation sites in glycoproteins from human clinical samples provides a basis for future studies addressing the biological and diagnostic importance of specific protein glycosylations in relation to human disease.
23234360	6	43	gly	glycosylation	1214:1226	arg2	samples					1271:1277	human clinical samples	1256:1277	human clinical samples	1256:1277	The characterization of glycans and glycosylation sites in glycoproteins from human clinical samples provides a basis for future studies addressing the biological and diagnostic importance of specific protein glycosylations in relation to human disease.
23234360	3	44	theme	/MS	727:729	arg1	protocol					741:748	an automated CID-MS(2)/MS(3) search protocol	705:748	an automated CID-MS(2)/MS(3) search protocol for glycopeptide identification	705:780	Here, we have introduced peptide N-glycosidase F (PNGase F) pretreatment of CSF samples to remove the N-glycans facilitating the selective characterization of O-glycopeptides and enabling the use of an automated CID-MS(2)/MS(3) search protocol for glycopeptide identification.
23234360	4	45	theme	glycosylation	861:873	arg1	glycopeptides					890:902	the glycopeptides	886:902	the glycopeptides	886:902	We used electron-capture and -transfer dissociation (ECD/ETD) to pinpoint the glycosylation site(s) of the glycopeptides, identified as predominantly core-1-like HexHexNAc-O- structure attached to one to four Ser/Thr residues.
23234360	4	45	theme	glycosylation	861:873	arg1	s					880:880	s	880:880	s	880:880	We used electron-capture and -transfer dissociation (ECD/ETD) to pinpoint the glycosylation site(s) of the glycopeptides, identified as predominantly core-1-like HexHexNAc-O- structure attached to one to four Ser/Thr residues.
23234360	4	45	theme	glycosylation	861:873	arg1	site					875:878	the glycosylation site	857:878	the glycosylation site(s)	857:881	We used electron-capture and -transfer dissociation (ECD/ETD) to pinpoint the glycosylation site(s) of the glycopeptides, identified as predominantly core-1-like HexHexNAc-O- structure attached to one to four Ser/Thr residues.
23234360	3	46	theme	CSF	582:584	arg1	samples					586:592	CSF samples	582:592	CSF samples	582:592	Here, we have introduced peptide N-glycosidase F (PNGase F) pretreatment of CSF samples to remove the N-glycans facilitating the selective characterization of O-glycopeptides and enabling the use of an automated CID-MS(2)/MS(3) search protocol for glycopeptide identification.
23234360	6	47	theme	human	1417:1421	arg1	disease					1423:1429	human disease	1417:1429	human disease	1417:1429	The characterization of glycans and glycosylation sites in glycoproteins from human clinical samples provides a basis for future studies addressing the biological and diagnostic importance of specific protein glycosylations in relation to human disease.
23234360	6	48	from	samples	1271:1277	arg1	glycoproteins					1237:1249	glycoproteins	1237:1249	glycoproteins from human clinical samples	1237:1277	The characterization of glycans and glycosylation sites in glycoproteins from human clinical samples provides a basis for future studies addressing the biological and diagnostic importance of specific protein glycosylations in relation to human disease.
23234360	6	48	from	samples	1271:1277	arg1	glycans					1202:1208	glycans	1202:1208	glycans	1202:1208	The characterization of glycans and glycosylation sites in glycoproteins from human clinical samples provides a basis for future studies addressing the biological and diagnostic importance of specific protein glycosylations in relation to human disease.
23234360	6	48	from	samples	1271:1277	arg1	sites					1228:1232	glycosylation sites	1214:1232	glycosylation sites in glycoproteins from human clinical samples	1214:1277	The characterization of glycans and glycosylation sites in glycoproteins from human clinical samples provides a basis for future studies addressing the biological and diagnostic importance of specific protein glycosylations in relation to human disease.
23234360	3	49	theme	search	734:739	arg1	protocol					741:748	an automated CID-MS(2)/MS(3) search protocol	705:748	an automated CID-MS(2)/MS(3) search protocol for glycopeptide identification	705:780	Here, we have introduced peptide N-glycosidase F (PNGase F) pretreatment of CSF samples to remove the N-glycans facilitating the selective characterization of O-glycopeptides and enabling the use of an automated CID-MS(2)/MS(3) search protocol for glycopeptide identification.
23234360	2	50	theme	tryptic	329:335	arg1	N-					337:338	tryptic N-	329:338	tryptic N-	329:338	We previously reported a sialic acid capture-and-release protocol to enrich tryptic N- and O-glycopeptides from human cerebrospinal fluid glycoproteins using nano-LC-ESI-MS/MS with collision-induced dissociation (CID) for glycopeptide characterization.
23234360	0	51	theme	glycan	55:60	arg1	structures					62:71	glycan structures	55:71	glycan structures	55:71	LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins.
23234360	3	52	theme	selective	635:643	arg1	characterization					645:660	the selective characterization	631:660	the selective characterization of O-glycopeptides	631:679	Here, we have introduced peptide N-glycosidase F (PNGase F) pretreatment of CSF samples to remove the N-glycans facilitating the selective characterization of O-glycopeptides and enabling the use of an automated CID-MS(2)/MS(3) search protocol for glycopeptide identification.
23234360	4	53	theme	glycopeptides	890:902	arg1	glycopeptides					890:902	the glycopeptides	886:902	the glycopeptides	886:902	We used electron-capture and -transfer dissociation (ECD/ETD) to pinpoint the glycosylation site(s) of the glycopeptides, identified as predominantly core-1-like HexHexNAc-O- structure attached to one to four Ser/Thr residues.
23234360	4	53	theme	glycopeptides	890:902	arg1	s					880:880	s	880:880	s	880:880	We used electron-capture and -transfer dissociation (ECD/ETD) to pinpoint the glycosylation site(s) of the glycopeptides, identified as predominantly core-1-like HexHexNAc-O- structure attached to one to four Ser/Thr residues.
23234360	4	53	theme	glycopeptides	890:902	arg1	site					875:878	the glycosylation site	857:878	the glycosylation site(s)	857:881	We used electron-capture and -transfer dissociation (ECD/ETD) to pinpoint the glycosylation site(s) of the glycopeptides, identified as predominantly core-1-like HexHexNAc-O- structure attached to one to four Ser/Thr residues.
23234360	6	54	theme	specific	1370:1377	arg1	glycosylations					1387:1400	specific protein glycosylations	1370:1400	specific protein glycosylations	1370:1400	The characterization of glycans and glycosylation sites in glycoproteins from human clinical samples provides a basis for future studies addressing the biological and diagnostic importance of specific protein glycosylations in relation to human disease.
23234360	2	55	theme	collision-induced	434:450	arg1	CID					466:468	CID	466:468	CID	466:468	We previously reported a sialic acid capture-and-release protocol to enrich tryptic N- and O-glycopeptides from human cerebrospinal fluid glycoproteins using nano-LC-ESI-MS/MS with collision-induced dissociation (CID) for glycopeptide characterization.
23234360	2	55	theme	collision-induced	434:450	arg1	dissociation					452:463	collision-induced dissociation	434:463	collision-induced dissociation (CID)	434:469	We previously reported a sialic acid capture-and-release protocol to enrich tryptic N- and O-glycopeptides from human cerebrospinal fluid glycoproteins using nano-LC-ESI-MS/MS with collision-induced dissociation (CID) for glycopeptide characterization.
23234360	4	56	gly	glycopeptides	890:902	arg2	glycopeptides					890:902	the glycopeptides	886:902	the glycopeptides	886:902	We used electron-capture and -transfer dissociation (ECD/ETD) to pinpoint the glycosylation site(s) of the glycopeptides, identified as predominantly core-1-like HexHexNAc-O- structure attached to one to four Ser/Thr residues.
23234360	4	57	theme	HexHexNAc-O-	945:956	arg1	structure					958:966	predominantly core-1-like HexHexNAc-O- structure	919:966	predominantly core-1-like HexHexNAc-O- structure attached to one to four Ser/Thr residues	919:1007	We used electron-capture and -transfer dissociation (ECD/ETD) to pinpoint the glycosylation site(s) of the glycopeptides, identified as predominantly core-1-like HexHexNAc-O- structure attached to one to four Ser/Thr residues.
23234360	6	58	from	glycoproteins	1237:1249	arg1	characterization					1182:1197	The characterization	1178:1197	The characterization of glycans and glycosylation sites in glycoproteins from human clinical samples	1178:1277	The characterization of glycans and glycosylation sites in glycoproteins from human clinical samples provides a basis for future studies addressing the biological and diagnostic importance of specific protein glycosylations in relation to human disease.
23234360	2	59	theme	capture-and-release	290:308	arg1	protocol					310:317	a sialic acid capture-and-release protocol	276:317	a sialic acid capture-and-release protocol to enrich tryptic N- and O-glycopeptides from human cerebrospinal fluid glycoproteins using nano-LC-ESI-MS/MS with collision-induced dissociation (CID) for glycopeptide characterization	276:503	We previously reported a sialic acid capture-and-release protocol to enrich tryptic N- and O-glycopeptides from human cerebrospinal fluid glycoproteins using nano-LC-ESI-MS/MS with collision-induced dissociation (CID) for glycopeptide characterization.
23234360	1	60	theme	Ser/Thr	147:153	arg1	residues					155:162	Ser/Thr residues	147:162	Ser/Thr residues of extracellular proteins	147:188	The GalNAc O-glycosylation on Ser/Thr residues of extracellular proteins has not been well characterized from a proteomics perspective.
23234360	1	60	theme	Ser/Thr	147:153	arg1	proteins					181:188	extracellular proteins	167:188	extracellular proteins	167:188	The GalNAc O-glycosylation on Ser/Thr residues of extracellular proteins has not been well characterized from a proteomics perspective.
23234360	6	61	theme	glycosylation	1214:1226	arg1	sites					1228:1232	glycosylation sites	1214:1232	glycosylation sites in glycoproteins from human clinical samples	1214:1277	The characterization of glycans and glycosylation sites in glycoproteins from human clinical samples provides a basis for future studies addressing the biological and diagnostic importance of specific protein glycosylations in relation to human disease.
23234360	0	62	theme	human	76:80	arg1	fluid					96:100	human cerebrospinal fluid	76:100	human cerebrospinal fluid glycoproteins	76:114	LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins.
23234360	2	63	theme	sialic	278:283	arg1	protocol					310:317	a sialic acid capture-and-release protocol	276:317	a sialic acid capture-and-release protocol to enrich tryptic N- and O-glycopeptides from human cerebrospinal fluid glycoproteins using nano-LC-ESI-MS/MS with collision-induced dissociation (CID) for glycopeptide characterization	276:503	We previously reported a sialic acid capture-and-release protocol to enrich tryptic N- and O-glycopeptides from human cerebrospinal fluid glycoproteins using nano-LC-ESI-MS/MS with collision-induced dissociation (CID) for glycopeptide characterization.
23234360	6	64	theme	glycans	1202:1208	arg1	characterization					1182:1197	The characterization	1178:1197	The characterization of glycans and glycosylation sites in glycoproteins from human clinical samples	1178:1277	The characterization of glycans and glycosylation sites in glycoproteins from human clinical samples provides a basis for future studies addressing the biological and diagnostic importance of specific protein glycosylations in relation to human disease.
23234360	4	65	dep	four	987:990	arg1	to					984:985	to	984:985	to	984:985	We used electron-capture and -transfer dissociation (ECD/ETD) to pinpoint the glycosylation site(s) of the glycopeptides, identified as predominantly core-1-like HexHexNAc-O- structure attached to one to four Ser/Thr residues.
23234360	0	66	theme	fluid	96:100	arg1	glycoproteins					102:114	human cerebrospinal fluid glycoproteins	76:114	human cerebrospinal fluid glycoproteins	76:114	LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins.
23234360	1	67	theme	proteins	181:188	arg1	residues					155:162	Ser/Thr residues	147:162	Ser/Thr residues of extracellular proteins	147:188	The GalNAc O-glycosylation on Ser/Thr residues of extracellular proteins has not been well characterized from a proteomics perspective.
23234360	1	67	theme	proteins	181:188	arg1	proteins					181:188	extracellular proteins	167:188	extracellular proteins	167:188	The GalNAc O-glycosylation on Ser/Thr residues of extracellular proteins has not been well characterized from a proteomics perspective.
23234360	6	68	from	sites	1228:1232	arg1	glycoproteins					1237:1249	glycoproteins	1237:1249	glycoproteins from human clinical samples	1237:1277	The characterization of glycans and glycosylation sites in glycoproteins from human clinical samples provides a basis for future studies addressing the biological and diagnostic importance of specific protein glycosylations in relation to human disease.
23234360	6	68	from	sites	1228:1232	arg1	samples					1271:1277	human clinical samples	1256:1277	human clinical samples	1256:1277	The characterization of glycans and glycosylation sites in glycoproteins from human clinical samples provides a basis for future studies addressing the biological and diagnostic importance of specific protein glycosylations in relation to human disease.
23234360	5	69	theme	attachment	1157:1166	arg1	n					1174:1174	n	1174:1174	n	1174:1174	We characterized 106 O-glycosylations and found Pro residues preferentially in the n - 1, n + 1, and/or n + 3 positions in relation to the Ser/Thr attachment site (n).
23234360	5	69	theme	attachment	1157:1166	arg1	site					1168:1171	the Ser/Thr attachment site	1145:1171	the Ser/Thr attachment site (n)	1145:1175	We characterized 106 O-glycosylations and found Pro residues preferentially in the n - 1, n + 1, and/or n + 3 positions in relation to the Ser/Thr attachment site (n).
23234360	2	70	gly	glycopeptide	475:486	arg2	glycopeptide					475:486	glycopeptide	475:486	glycopeptide	475:486	We previously reported a sialic acid capture-and-release protocol to enrich tryptic N- and O-glycopeptides from human cerebrospinal fluid glycoproteins using nano-LC-ESI-MS/MS with collision-induced dissociation (CID) for glycopeptide characterization.
23234360	2	71	theme	human	365:369	arg1	fluid					385:389	human cerebrospinal fluid	365:389	human cerebrospinal fluid	365:389	We previously reported a sialic acid capture-and-release protocol to enrich tryptic N- and O-glycopeptides from human cerebrospinal fluid glycoproteins using nano-LC-ESI-MS/MS with collision-induced dissociation (CID) for glycopeptide characterization.
23234360	6	72	theme	glycosylations	1387:1400	arg1	importance					1356:1365	the biological and diagnostic importance	1326:1365	the biological and diagnostic importance of specific protein glycosylations in relation to human disease	1326:1429	The characterization of glycans and glycosylation sites in glycoproteins from human clinical samples provides a basis for future studies addressing the biological and diagnostic importance of specific protein glycosylations in relation to human disease.
23234360	2	73	gly	O-glycopeptides	344:358	arg1	fluid					385:389	human cerebrospinal fluid	365:389	human cerebrospinal fluid	365:389	We previously reported a sialic acid capture-and-release protocol to enrich tryptic N- and O-glycopeptides from human cerebrospinal fluid glycoproteins using nano-LC-ESI-MS/MS with collision-induced dissociation (CID) for glycopeptide characterization.
23234360	2	73	gly	O-glycopeptides	344:358	arg2	O-glycopeptides					344:358	O-glycopeptides	344:358	O-glycopeptides from human cerebrospinal fluid	344:389	We previously reported a sialic acid capture-and-release protocol to enrich tryptic N- and O-glycopeptides from human cerebrospinal fluid glycoproteins using nano-LC-ESI-MS/MS with collision-induced dissociation (CID) for glycopeptide characterization.
23234360	0	74	gly	glycoproteins	102:114	arg1	glycoproteins					102:114	human cerebrospinal fluid glycoproteins	76:114	human cerebrospinal fluid glycoproteins	76:114	LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins.
23234360	0	75	theme	O-glycosylation	29:43	arg1	glycoproteins					102:114	human cerebrospinal fluid glycoproteins	76:114	human cerebrospinal fluid glycoproteins	76:114	LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins.
23234360	0	75	theme	O-glycosylation	29:43	arg1	sites					45:49	O-glycosylation sites	29:49	O-glycosylation sites	29:49	LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins.
23234360	3	76	theme	F	553:553	arg1	pretreatment					566:577	peptide N-glycosidase F (PNGase F) pretreatment	531:577	peptide N-glycosidase F (PNGase F) pretreatment of CSF samples	531:592	Here, we have introduced peptide N-glycosidase F (PNGase F) pretreatment of CSF samples to remove the N-glycans facilitating the selective characterization of O-glycopeptides and enabling the use of an automated CID-MS(2)/MS(3) search protocol for glycopeptide identification.
23234360	1	77	theme	proteomics	229:238	arg1	perspective					240:250	a proteomics perspective	227:250	a proteomics perspective	227:250	The GalNAc O-glycosylation on Ser/Thr residues of extracellular proteins has not been well characterized from a proteomics perspective.
23234360	3	78	theme	automated	708:716	arg1	protocol					741:748	an automated CID-MS(2)/MS(3) search protocol	705:748	an automated CID-MS(2)/MS(3) search protocol for glycopeptide identification	705:780	Here, we have introduced peptide N-glycosidase F (PNGase F) pretreatment of CSF samples to remove the N-glycans facilitating the selective characterization of O-glycopeptides and enabling the use of an automated CID-MS(2)/MS(3) search protocol for glycopeptide identification.
23234360	3	79	theme	peptide	531:537	arg1	F					563:563	PNGase F	556:563	PNGase F	556:563	Here, we have introduced peptide N-glycosidase F (PNGase F) pretreatment of CSF samples to remove the N-glycans facilitating the selective characterization of O-glycopeptides and enabling the use of an automated CID-MS(2)/MS(3) search protocol for glycopeptide identification.
23234360	3	79	theme	peptide	531:537	arg1	F					553:553	peptide N-glycosidase F	531:553	peptide N-glycosidase F (PNGase F) pretreatment of CSF samples	531:592	Here, we have introduced peptide N-glycosidase F (PNGase F) pretreatment of CSF samples to remove the N-glycans facilitating the selective characterization of O-glycopeptides and enabling the use of an automated CID-MS(2)/MS(3) search protocol for glycopeptide identification.
23234360	0	80	theme	structures	62:71	arg1	characterization					9:24	LC-MS/MS characterization	0:24	LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins.	0:115	LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins.
23234360	2	81	gly	glycoproteins	391:403	arg1	glycoproteins					391:403	tryptic N- and O-glycopeptides from human cerebrospinal fluid glycoproteins	329:403	tryptic N- and O-glycopeptides from human cerebrospinal fluid glycoproteins using nano-LC-ESI-MS/MS with collision-induced dissociation (CID) for glycopeptide characterization	329:503	We previously reported a sialic acid capture-and-release protocol to enrich tryptic N- and O-glycopeptides from human cerebrospinal fluid glycoproteins using nano-LC-ESI-MS/MS with collision-induced dissociation (CID) for glycopeptide characterization.
23234360	5	82	theme	Pro	1058:1060	arg1	residues					1062:1069	Pro residues	1058:1069	Pro residues	1058:1069	We characterized 106 O-glycosylations and found Pro residues preferentially in the n - 1, n + 1, and/or n + 3 positions in relation to the Ser/Thr attachment site (n).
23234360	3	83	theme	PNGase	556:561	arg1	F					563:563	PNGase F	556:563	PNGase F	556:563	Here, we have introduced peptide N-glycosidase F (PNGase F) pretreatment of CSF samples to remove the N-glycans facilitating the selective characterization of O-glycopeptides and enabling the use of an automated CID-MS(2)/MS(3) search protocol for glycopeptide identification.
23234360	3	83	theme	PNGase	556:561	arg1	F					553:553	peptide N-glycosidase F	531:553	peptide N-glycosidase F (PNGase F) pretreatment of CSF samples	531:592	Here, we have introduced peptide N-glycosidase F (PNGase F) pretreatment of CSF samples to remove the N-glycans facilitating the selective characterization of O-glycopeptides and enabling the use of an automated CID-MS(2)/MS(3) search protocol for glycopeptide identification.
23234360	3	84	theme	protocol	741:748	arg1	use					698:700	the use	694:700	the use of an automated CID-MS(2)/MS(3) search protocol for glycopeptide identification	694:780	Here, we have introduced peptide N-glycosidase F (PNGase F) pretreatment of CSF samples to remove the N-glycans facilitating the selective characterization of O-glycopeptides and enabling the use of an automated CID-MS(2)/MS(3) search protocol for glycopeptide identification.
23234360	3	85	theme	samples	586:592	arg1	pretreatment					566:577	peptide N-glycosidase F (PNGase F) pretreatment	531:577	peptide N-glycosidase F (PNGase F) pretreatment of CSF samples	531:592	Here, we have introduced peptide N-glycosidase F (PNGase F) pretreatment of CSF samples to remove the N-glycans facilitating the selective characterization of O-glycopeptides and enabling the use of an automated CID-MS(2)/MS(3) search protocol for glycopeptide identification.
25802287	10	0	with	scanning	1488:1495	arg1	desorption/ionization-time-of-flight-MS					1557:1595	low-resolution matrix assisted laser desorption/ionization-time-of-flight-MS	1520:1595	low-resolution matrix assisted laser desorption/ionization-time-of-flight-MS	1520:1595	By scanning the treated spots with low-resolution matrix assisted laser desorption/ionization-time-of-flight-MS, we observed all five deglycosylated peptides, including the one originating from the secretory chain.
25802287	12	1	theme	comprehensive	1953:1965	arg1	analysis					1986:1993	the first detailed and comprehensive mass spectrometric analysis	1930:1993	the first detailed and comprehensive mass spectrometric analysis on the glycopeptide level for human polyclonal IgM with high mass accuracy	1930:2068	We present the first detailed and comprehensive mass spectrometric analysis on the glycopeptide level for human polyclonal IgM with high mass accuracy.
25802287	7	2	theme	glycopeptide	1188:1199	arg1	clusters					1201:1208	the "intact" glycopeptide clusters	1175:1208	the "intact" glycopeptide clusters	1175:1208	An identified peptide then leads directly to the position of the "intact" glycopeptide clusters, which are located in the adjacent spots.
25802287	7	2	theme	glycopeptide	1188:1199	arg1	located					1221:1227	located	1221:1227	located	1221:1227	An identified peptide then leads directly to the position of the "intact" glycopeptide clusters, which are located in the adjacent spots.
25802287	6	3	gly	glycosites	1013:1022	arg2	glycosites					1013:1022	distinct glycosites	1004:1022	distinct glycosites	1004:1022	Mining for distinct glycosites is performed by searching for the predicted deglycosylated peptides in the treated trace.
25802287	11	4	with	spots	1790:1794	arg1	accuracy					1836:1843	high mass accuracy	1826:1843	high mass accuracy	1826:1843	A detailed glycopeptide characterization was then accomplished on the adjacent, untreated spots with high mass resolution and high mass accuracy using a matrix assisted laser desorption ionization-Fourier transform-MS.
25802287	11	4	with	spots	1790:1794	arg1	resolution					1811:1820	high mass resolution	1801:1820	high mass resolution	1801:1820	A detailed glycopeptide characterization was then accomplished on the adjacent, untreated spots with high mass resolution and high mass accuracy using a matrix assisted laser desorption ionization-Fourier transform-MS.
25802287	4	5	theme	reaction	671:678	arg1	cavities					680:687	nanoliter reaction cavities	661:687	nanoliter reaction cavities	661:687	In this way, a short separation run is archived into thousands of nanoliter reaction cavities, and chromatographic peaks are spread over multiple array spots.
25802287	7	6	theme	intact	1180:1185	arg1	clusters					1201:1208	the "intact" glycopeptide clusters	1175:1208	the "intact" glycopeptide clusters	1175:1208	An identified peptide then leads directly to the position of the "intact" glycopeptide clusters, which are located in the adjacent spots.
25802287	7	6	theme	intact	1180:1185	arg1	located					1221:1227	located	1221:1227	located	1221:1227	An identified peptide then leads directly to the position of the "intact" glycopeptide clusters, which are located in the adjacent spots.
25802287	4	7	theme	array	741:745	arg1	spots					747:751	multiple array spots	732:751	multiple array spots	732:751	In this way, a short separation run is archived into thousands of nanoliter reaction cavities, and chromatographic peaks are spread over multiple array spots.
25802287	11	8	theme	high	1801:1804	arg1	resolution					1811:1820	high mass resolution	1801:1820	high mass resolution	1801:1820	A detailed glycopeptide characterization was then accomplished on the adjacent, untreated spots with high mass resolution and high mass accuracy using a matrix assisted laser desorption ionization-Fourier transform-MS.
25802287	13	9	theme	Asn	2260:2262	arg1	171					2264:2266	the glycosite Asn 171	2246:2266	the glycosite Asn 171	2246:2266	Besides complex type glycans on Asn 395, 332, 171, and on the J chain, we observed oligomannosidic glycans on Asn 563, Asn 402 and minor amounts of oligomannosidic glycans on the glycosite Asn 171.
25802287	3	10	from	frequency	566:574	arg1	microarray					583:592	the microarray	579:592	the microarray	579:592	A chromatographic separation of a proteolytic digest is deposited at a high frequency on the microarray.
25802287	7	11	theme	adjacent	1236:1243	arg1	spots					1245:1249	the adjacent spots	1232:1249	the adjacent spots	1232:1249	An identified peptide then leads directly to the position of the "intact" glycopeptide clusters, which are located in the adjacent spots.
25802287	14	12	located	found	2307:2311	arg2	glycans					2294:2300	hybrid type glycans	2282:2300	hybrid type glycans	2282:2300	Furthermore, hybrid type glycans were found on Asn 402, Asn 171 and in traces Asn 332.
25802287	14	12	located	found	2307:2311	arg1	Asn					2316:2318	Asn 402	2316:2322	Asn 402	2316:2322	Furthermore, hybrid type glycans were found on Asn 402, Asn 171 and in traces Asn 332.
25802287	14	12	located	found	2307:2311	arg1	Asn					2347:2349	in traces Asn 332	2337:2353	in traces Asn 332	2337:2353	Furthermore, hybrid type glycans were found on Asn 402, Asn 171 and in traces Asn 332.
25802287	14	12	located	found	2307:2311	arg1	Asn					2325:2327	Asn 171	2325:2331	Asn 171	2325:2331	Furthermore, hybrid type glycans were found on Asn 402, Asn 171 and in traces Asn 332.
25802287	13	13	gly	glycosite	2250:2258	arg2	glycosite					2250:2258	the glycosite Asn 171	2246:2266	the glycosite Asn 171	2246:2266	Besides complex type glycans on Asn 395, 332, 171, and on the J chain, we observed oligomannosidic glycans on Asn 563, Asn 402 and minor amounts of oligomannosidic glycans on the glycosite Asn 171.
25802287	14	14	theme	type	2289:2292	arg1	glycans					2294:2300	hybrid type glycans	2282:2300	hybrid type glycans	2282:2300	Furthermore, hybrid type glycans were found on Asn 402, Asn 171 and in traces Asn 332.
25802287	10	15	theme	treated	1501:1507	arg1	spots					1509:1513	the treated spots	1497:1513	the treated spots	1497:1513	By scanning the treated spots with low-resolution matrix assisted laser desorption/ionization-time-of-flight-MS, we observed all five deglycosylated peptides, including the one originating from the secretory chain.
25802287	2	16	theme	assisted	370:377	arg1	platform					410:417	a nano-liquid chromatography microarray-matrix assisted laser desorption/ionization-MS platform	323:417	a nano-liquid chromatography microarray-matrix assisted laser desorption/ionization-MS platform	323:417	It is based on a nano-liquid chromatography microarray-matrix assisted laser desorption/ionization-MS platform, which employs droplet microfluidics for on-plate nanoliter reactions.
25802287	5	17	gly	glycopeptides	978:990	arg2	glycopeptides					978:990	the intact glycopeptides	967:990	the intact glycopeptides	967:990	After fractionation, each other spot is treated with PNGaseF to generate two correlated traces within one run, one with treated spots where glycans are enzymatically released from the peptides, and one containing the intact glycopeptides.
25802287	8	18	theme	simple	1326:1331	arg1	experiment					1367:1376	a simple collision-induced dissociation-MS experiment	1324:1376	a simple collision-induced dissociation-MS experiment	1324:1376	Furthermore, the deglycosylated peptide can be sequenced efficiently in a simple collision-induced dissociation-MS experiment.
25802287	0	19	theme	Serum	162:166	arg1	M					183:183	Human Serum Immunoglobulin M	156:183	Human Serum Immunoglobulin M (IgM)	156:189	A Microarray-Matrix-assisted Laser Desorption/Ionization-Mass Spectrometry Approach for Site-specific Protein N-glycosylation Analysis, as Demonstrated for Human Serum Immunoglobulin M (IgM).
25802287	0	19	theme	Serum	162:166	arg1	IgM					186:188	IgM	186:188	IgM	186:188	A Microarray-Matrix-assisted Laser Desorption/Ionization-Mass Spectrometry Approach for Site-specific Protein N-glycosylation Analysis, as Demonstrated for Human Serum Immunoglobulin M (IgM).
25802287	13	20	theme	glycans	2235:2241	arg1	Asn					2181:2183	Asn 563	2181:2187	Asn 563	2181:2187	Besides complex type glycans on Asn 395, 332, 171, and on the J chain, we observed oligomannosidic glycans on Asn 563, Asn 402 and minor amounts of oligomannosidic glycans on the glycosite Asn 171.
25802287	13	20	theme	glycans	2235:2241	arg1	Asn					2190:2192	Asn 402	2190:2196	Asn 402	2190:2196	Besides complex type glycans on Asn 395, 332, 171, and on the J chain, we observed oligomannosidic glycans on Asn 563, Asn 402 and minor amounts of oligomannosidic glycans on the glycosite Asn 171.
25802287	13	20	theme	glycans	2235:2241	arg1	amounts					2208:2214	minor amounts	2202:2214	minor amounts of oligomannosidic glycans	2202:2241	Besides complex type glycans on Asn 395, 332, 171, and on the J chain, we observed oligomannosidic glycans on Asn 563, Asn 402 and minor amounts of oligomannosidic glycans on the glycosite Asn 171.
25802287	13	20	theme	glycans	2235:2241	arg1	glycans					2235:2241	oligomannosidic glycans	2219:2241	oligomannosidic glycans	2219:2241	Besides complex type glycans on Asn 395, 332, 171, and on the J chain, we observed oligomannosidic glycans on Asn 563, Asn 402 and minor amounts of oligomannosidic glycans on the glycosite Asn 171.
25802287	2	21	theme	chromatography	337:350	arg1	platform					410:417	a nano-liquid chromatography microarray-matrix assisted laser desorption/ionization-MS platform	323:417	a nano-liquid chromatography microarray-matrix assisted laser desorption/ionization-MS platform	323:417	It is based on a nano-liquid chromatography microarray-matrix assisted laser desorption/ionization-MS platform, which employs droplet microfluidics for on-plate nanoliter reactions.
25802287	8	22	theme	deglycosylated	1269:1282	arg1	peptide					1284:1290	the deglycosylated peptide	1265:1290	the deglycosylated peptide	1265:1290	Furthermore, the deglycosylated peptide can be sequenced efficiently in a simple collision-induced dissociation-MS experiment.
25802287	3	23	theme	proteolytic	524:534	arg1	digest					536:541	a proteolytic digest	522:541	a proteolytic digest	522:541	A chromatographic separation of a proteolytic digest is deposited at a high frequency on the microarray.
25802287	8	24	theme	dissociation-MS	1351:1365	arg1	experiment					1367:1376	a simple collision-induced dissociation-MS experiment	1324:1376	a simple collision-induced dissociation-MS experiment	1324:1376	Furthermore, the deglycosylated peptide can be sequenced efficiently in a simple collision-induced dissociation-MS experiment.
25802287	13	25	theme	minor	2202:2206	arg1	amounts					2208:2214	minor amounts	2202:2214	minor amounts of oligomannosidic glycans	2202:2241	Besides complex type glycans on Asn 395, 332, 171, and on the J chain, we observed oligomannosidic glycans on Asn 563, Asn 402 and minor amounts of oligomannosidic glycans on the glycosite Asn 171.
25802287	13	25	theme	minor	2202:2206	arg1	glycans					2235:2241	oligomannosidic glycans	2219:2241	oligomannosidic glycans	2219:2241	Besides complex type glycans on Asn 395, 332, 171, and on the J chain, we observed oligomannosidic glycans on Asn 563, Asn 402 and minor amounts of oligomannosidic glycans on the glycosite Asn 171.
25802287	13	26	theme	type	2087:2090	arg1	glycans					2092:2098	complex type glycans	2079:2098	complex type glycans on Asn 395, 332, 171, and on the J chain	2079:2139	Besides complex type glycans on Asn 395, 332, 171, and on the J chain, we observed oligomannosidic glycans on Asn 563, Asn 402 and minor amounts of oligomannosidic glycans on the glycosite Asn 171.
25802287	6	27	theme	treated	1099:1105	arg1	trace					1107:1111	the treated trace	1095:1111	the treated trace	1095:1111	Mining for distinct glycosites is performed by searching for the predicted deglycosylated peptides in the treated trace.
25802287	5	28	contain	containing	956:965	arg2	glycopeptides					978:990	the intact glycopeptides	967:990	the intact glycopeptides	967:990	After fractionation, each other spot is treated with PNGaseF to generate two correlated traces within one run, one with treated spots where glycans are enzymatically released from the peptides, and one containing the intact glycopeptides.
25802287	5	28	contain	containing	956:965	arg1	one					952:954	one	952:954	one	952:954	After fractionation, each other spot is treated with PNGaseF to generate two correlated traces within one run, one with treated spots where glycans are enzymatically released from the peptides, and one containing the intact glycopeptides.
25802287	5	28	contain	containing	956:965	arg1	run					860:862	one run	856:862	one run	856:862	After fractionation, each other spot is treated with PNGaseF to generate two correlated traces within one run, one with treated spots where glycans are enzymatically released from the peptides, and one containing the intact glycopeptides.
25802287	11	29	theme	desorption	1875:1884	arg1	transform-MS					1905:1916	a matrix assisted laser desorption ionization-Fourier transform-MS	1851:1916	a matrix assisted laser desorption ionization-Fourier transform-MS	1851:1916	A detailed glycopeptide characterization was then accomplished on the adjacent, untreated spots with high mass resolution and high mass accuracy using a matrix assisted laser desorption ionization-Fourier transform-MS.
25802287	5	30	theme	correlated	831:840	arg1	traces					842:847	two correlated traces	827:847	two correlated traces	827:847	After fractionation, each other spot is treated with PNGaseF to generate two correlated traces within one run, one with treated spots where glycans are enzymatically released from the peptides, and one containing the intact glycopeptides.
25802287	10	31	theme	laser	1551:1555	arg1	desorption/ionization-time-of-flight-MS					1557:1595	low-resolution matrix assisted laser desorption/ionization-time-of-flight-MS	1520:1595	low-resolution matrix assisted laser desorption/ionization-time-of-flight-MS	1520:1595	By scanning the treated spots with low-resolution matrix assisted laser desorption/ionization-time-of-flight-MS, we observed all five deglycosylated peptides, including the one originating from the secretory chain.
25802287	6	32	theme	deglycosylated	1068:1081	arg1	peptides					1083:1090	the predicted deglycosylated peptides	1054:1090	the predicted deglycosylated peptides	1054:1090	Mining for distinct glycosites is performed by searching for the predicted deglycosylated peptides in the treated trace.
25802287	10	33	theme	matrix	1535:1540	arg1	desorption/ionization-time-of-flight-MS					1557:1595	low-resolution matrix assisted laser desorption/ionization-time-of-flight-MS	1520:1595	low-resolution matrix assisted laser desorption/ionization-time-of-flight-MS	1520:1595	By scanning the treated spots with low-resolution matrix assisted laser desorption/ionization-time-of-flight-MS, we observed all five deglycosylated peptides, including the one originating from the secretory chain.
25802287	9	34	gly	glycosylation	1442:1454	arg1	IgM					1480:1482	human serum IgM	1468:1482	human serum IgM	1468:1482	We applied the microarray approach to a detailed site-specific glycosylation analysis of human serum IgM.
25802287	3	35	theme	digest	536:541	arg1	separation					508:517	A chromatographic separation	490:517	A chromatographic separation of a proteolytic digest	490:541	A chromatographic separation of a proteolytic digest is deposited at a high frequency on the microarray.
25802287	12	36	theme	mass	2056:2059	arg1	accuracy					2061:2068	high mass accuracy	2051:2068	high mass accuracy	2051:2068	We present the first detailed and comprehensive mass spectrometric analysis on the glycopeptide level for human polyclonal IgM with high mass accuracy.
25802287	2	37	theme	nanoliter	469:477	arg1	reactions					479:487	on-plate nanoliter reactions	460:487	on-plate nanoliter reactions	460:487	It is based on a nano-liquid chromatography microarray-matrix assisted laser desorption/ionization-MS platform, which employs droplet microfluidics for on-plate nanoliter reactions.
25802287	5	38	theme	treated	874:880	arg1	spots					882:886	treated spots	874:886	treated spots where glycans are enzymatically released from the peptides	874:945	After fractionation, each other spot is treated with PNGaseF to generate two correlated traces within one run, one with treated spots where glycans are enzymatically released from the peptides, and one containing the intact glycopeptides.
25802287	14	39	theme	traces	2340:2345	arg1	Asn					2347:2349	in traces Asn 332	2337:2353	in traces Asn 332	2337:2353	Furthermore, hybrid type glycans were found on Asn 402, Asn 171 and in traces Asn 332.
25802287	0	40	theme	Laser	29:33	arg1	Spectrometry					62:73	A Microarray-Matrix-assisted Laser Desorption/Ionization-Mass Spectrometry	0:73	A Microarray-Matrix-assisted Laser Desorption/Ionization-Mass Spectrometry	0:73	A Microarray-Matrix-assisted Laser Desorption/Ionization-Mass Spectrometry Approach for Site-specific Protein N-glycosylation Analysis, as Demonstrated for Human Serum Immunoglobulin M (IgM).
25802287	9	41	theme	site-specific	1428:1440	arg1	analysis					1456:1463	a detailed site-specific glycosylation analysis	1417:1463	a detailed site-specific glycosylation analysis of human serum IgM	1417:1482	We applied the microarray approach to a detailed site-specific glycosylation analysis of human serum IgM.
25802287	12	42	theme	polyclonal	2031:2040	arg1	IgM					2042:2044	human polyclonal IgM	2025:2044	human polyclonal IgM with high mass accuracy	2025:2068	We present the first detailed and comprehensive mass spectrometric analysis on the glycopeptide level for human polyclonal IgM with high mass accuracy.
25802287	0	43	theme	Protein	102:108	arg1	Analysis					126:133	Site-specific Protein N-glycosylation Analysis	88:133	Site-specific Protein N-glycosylation Analysis	88:133	A Microarray-Matrix-assisted Laser Desorption/Ionization-Mass Spectrometry Approach for Site-specific Protein N-glycosylation Analysis, as Demonstrated for Human Serum Immunoglobulin M (IgM).
25802287	11	44	gly	glycopeptide	1711:1722	arg2	glycopeptide					1711:1722	A detailed glycopeptide characterization	1700:1739	A detailed glycopeptide characterization	1700:1739	A detailed glycopeptide characterization was then accomplished on the adjacent, untreated spots with high mass resolution and high mass accuracy using a matrix assisted laser desorption ionization-Fourier transform-MS.
25802287	9	45	theme	human	1468:1472	arg1	IgM					1480:1482	human serum IgM	1468:1482	human serum IgM	1468:1482	We applied the microarray approach to a detailed site-specific glycosylation analysis of human serum IgM.
25802287	12	46	theme	glycopeptide	2002:2013	arg1	level					2015:2019	the glycopeptide level	1998:2019	the glycopeptide level for human polyclonal IgM with high mass accuracy	1998:2068	We present the first detailed and comprehensive mass spectrometric analysis on the glycopeptide level for human polyclonal IgM with high mass accuracy.
25802287	4	47	theme	short	610:614	arg1	run					627:629	a short separation run	608:629	a short separation run	608:629	In this way, a short separation run is archived into thousands of nanoliter reaction cavities, and chromatographic peaks are spread over multiple array spots.
25802287	11	48	theme	laser	1869:1873	arg1	transform-MS					1905:1916	a matrix assisted laser desorption ionization-Fourier transform-MS	1851:1916	a matrix assisted laser desorption ionization-Fourier transform-MS	1851:1916	A detailed glycopeptide characterization was then accomplished on the adjacent, untreated spots with high mass resolution and high mass accuracy using a matrix assisted laser desorption ionization-Fourier transform-MS.
25802287	13	49	theme	oligomannosidic	2154:2168	arg1	glycans					2170:2176	oligomannosidic glycans	2154:2176	oligomannosidic glycans on Asn 563, Asn 402 and minor amounts of oligomannosidic glycans on the glycosite Asn 171	2154:2266	Besides complex type glycans on Asn 395, 332, 171, and on the J chain, we observed oligomannosidic glycans on Asn 563, Asn 402 and minor amounts of oligomannosidic glycans on the glycosite Asn 171.
25802287	9	50	theme	IgM	1480:1482	arg1	analysis					1456:1463	a detailed site-specific glycosylation analysis	1417:1463	a detailed site-specific glycosylation analysis of human serum IgM	1417:1482	We applied the microarray approach to a detailed site-specific glycosylation analysis of human serum IgM.
25802287	5	51	attach	released	920:927	arg2	glycans					894:900	glycans	894:900	glycans	894:900	After fractionation, each other spot is treated with PNGaseF to generate two correlated traces within one run, one with treated spots where glycans are enzymatically released from the peptides, and one containing the intact glycopeptides.
25802287	5	51	attach	released	920:927	arg1	peptides					938:945	the peptides	934:945	the peptides	934:945	After fractionation, each other spot is treated with PNGaseF to generate two correlated traces within one run, one with treated spots where glycans are enzymatically released from the peptides, and one containing the intact glycopeptides.
25802287	4	52	theme	cavities	680:687	arg1	thousands					648:656	thousands	648:656	thousands of nanoliter reaction cavities	648:687	In this way, a short separation run is archived into thousands of nanoliter reaction cavities, and chromatographic peaks are spread over multiple array spots.
25802287	10	53	theme	secretory	1683:1691	arg1	chain					1693:1697	the secretory chain	1679:1697	the secretory chain	1679:1697	By scanning the treated spots with low-resolution matrix assisted laser desorption/ionization-time-of-flight-MS, we observed all five deglycosylated peptides, including the one originating from the secretory chain.
25802287	11	54	theme	matrix	1853:1858	arg1	transform-MS					1905:1916	a matrix assisted laser desorption ionization-Fourier transform-MS	1851:1916	a matrix assisted laser desorption ionization-Fourier transform-MS	1851:1916	A detailed glycopeptide characterization was then accomplished on the adjacent, untreated spots with high mass resolution and high mass accuracy using a matrix assisted laser desorption ionization-Fourier transform-MS.
25802287	11	55	theme	adjacent	1770:1777	arg1	spots					1790:1794	the adjacent, untreated spots	1766:1794	the adjacent, untreated spots with high mass resolution and high mass accuracy using a matrix assisted laser desorption ionization-Fourier transform-MS	1766:1916	A detailed glycopeptide characterization was then accomplished on the adjacent, untreated spots with high mass resolution and high mass accuracy using a matrix assisted laser desorption ionization-Fourier transform-MS.
25802287	12	56	with	IgM	2042:2044	arg1	accuracy					2061:2068	high mass accuracy	2051:2068	high mass accuracy	2051:2068	We present the first detailed and comprehensive mass spectrometric analysis on the glycopeptide level for human polyclonal IgM with high mass accuracy.
25802287	0	57	theme	Site-specific	88:100	arg1	Analysis					126:133	Site-specific Protein N-glycosylation Analysis	88:133	Site-specific Protein N-glycosylation Analysis	88:133	A Microarray-Matrix-assisted Laser Desorption/Ionization-Mass Spectrometry Approach for Site-specific Protein N-glycosylation Analysis, as Demonstrated for Human Serum Immunoglobulin M (IgM).
25802287	12	58	theme	mass	1967:1970	arg1	analysis					1986:1993	the first detailed and comprehensive mass spectrometric analysis	1930:1993	the first detailed and comprehensive mass spectrometric analysis on the glycopeptide level for human polyclonal IgM with high mass accuracy	1930:2068	We present the first detailed and comprehensive mass spectrometric analysis on the glycopeptide level for human polyclonal IgM with high mass accuracy.
25802287	7	59	theme	"	1186:1186	arg1	clusters					1201:1208	the "intact" glycopeptide clusters	1175:1208	the "intact" glycopeptide clusters	1175:1208	An identified peptide then leads directly to the position of the "intact" glycopeptide clusters, which are located in the adjacent spots.
25802287	7	59	theme	"	1186:1186	arg1	located					1221:1227	located	1221:1227	located	1221:1227	An identified peptide then leads directly to the position of the "intact" glycopeptide clusters, which are located in the adjacent spots.
25802287	2	60	theme	droplet	434:440	arg1	microfluidics					442:454	droplet microfluidics	434:454	droplet microfluidics for on-plate nanoliter reactions	434:487	It is based on a nano-liquid chromatography microarray-matrix assisted laser desorption/ionization-MS platform, which employs droplet microfluidics for on-plate nanoliter reactions.
25802287	1	61	theme	N-glycosylation	291:305	arg1	characterization					263:278	characterization	263:278	characterization	263:278	We demonstrate a new approach for the site-specific identification and characterization of protein N-glycosylation.
25802287	1	61	theme	N-glycosylation	291:305	arg1	identification					244:257	site-specific identification	230:257	site-specific identification	230:257	We demonstrate a new approach for the site-specific identification and characterization of protein N-glycosylation.
25802287	11	62	theme	mass	1831:1834	arg1	accuracy					1836:1843	high mass accuracy	1826:1843	high mass accuracy	1826:1843	A detailed glycopeptide characterization was then accomplished on the adjacent, untreated spots with high mass resolution and high mass accuracy using a matrix assisted laser desorption ionization-Fourier transform-MS.
25802287	11	63	theme	detailed	1702:1709	arg1	characterization					1724:1739	A detailed glycopeptide characterization	1700:1739	A detailed glycopeptide characterization	1700:1739	A detailed glycopeptide characterization was then accomplished on the adjacent, untreated spots with high mass resolution and high mass accuracy using a matrix assisted laser desorption ionization-Fourier transform-MS.
25802287	13	64	theme	171	2117:2119	arg1	Asn					2103:2105	Asn 395, 332	2103:2114	Asn	2103:2105	Besides complex type glycans on Asn 395, 332, 171, and on the J chain, we observed oligomannosidic glycans on Asn 563, Asn 402 and minor amounts of oligomannosidic glycans on the glycosite Asn 171.
25802287	2	65	theme	nano-liquid	325:335	arg1	platform					410:417	a nano-liquid chromatography microarray-matrix assisted laser desorption/ionization-MS platform	323:417	a nano-liquid chromatography microarray-matrix assisted laser desorption/ionization-MS platform	323:417	It is based on a nano-liquid chromatography microarray-matrix assisted laser desorption/ionization-MS platform, which employs droplet microfluidics for on-plate nanoliter reactions.
25802287	12	66	theme	first	1934:1938	arg1	analysis					1986:1993	the first detailed and comprehensive mass spectrometric analysis	1930:1993	the first detailed and comprehensive mass spectrometric analysis on the glycopeptide level for human polyclonal IgM with high mass accuracy	1930:2068	We present the first detailed and comprehensive mass spectrometric analysis on the glycopeptide level for human polyclonal IgM with high mass accuracy.
25802287	4	67	theme	nanoliter	661:669	arg1	cavities					680:687	nanoliter reaction cavities	661:687	nanoliter reaction cavities	661:687	In this way, a short separation run is archived into thousands of nanoliter reaction cavities, and chromatographic peaks are spread over multiple array spots.
25802287	4	68	theme	multiple	732:739	arg1	spots					747:751	multiple array spots	732:751	multiple array spots	732:751	In this way, a short separation run is archived into thousands of nanoliter reaction cavities, and chromatographic peaks are spread over multiple array spots.
25802287	11	69	theme	mass	1806:1809	arg1	resolution					1811:1820	high mass resolution	1801:1820	high mass resolution	1801:1820	A detailed glycopeptide characterization was then accomplished on the adjacent, untreated spots with high mass resolution and high mass accuracy using a matrix assisted laser desorption ionization-Fourier transform-MS.
25802287	8	70	gly	deglycosylated	1269:1282	arg1	peptide					1284:1290	the deglycosylated peptide	1265:1290	the deglycosylated peptide	1265:1290	Furthermore, the deglycosylated peptide can be sequenced efficiently in a simple collision-induced dissociation-MS experiment.
25802287	2	71	theme	laser	379:383	arg1	platform					410:417	a nano-liquid chromatography microarray-matrix assisted laser desorption/ionization-MS platform	323:417	a nano-liquid chromatography microarray-matrix assisted laser desorption/ionization-MS platform	323:417	It is based on a nano-liquid chromatography microarray-matrix assisted laser desorption/ionization-MS platform, which employs droplet microfluidics for on-plate nanoliter reactions.
25802287	1	72	theme	new	209:211	arg1	approach					213:220	a new approach	207:220	a new approach for the site-specific identification and characterization of protein N-glycosylation	207:305	We demonstrate a new approach for the site-specific identification and characterization of protein N-glycosylation.
25802287	10	73	gly	deglycosylated	1619:1632	arg1	peptides					1634:1641	all five deglycosylated peptides	1610:1641	all five deglycosylated peptides	1610:1641	By scanning the treated spots with low-resolution matrix assisted laser desorption/ionization-time-of-flight-MS, we observed all five deglycosylated peptides, including the one originating from the secretory chain.
25802287	10	73	gly	deglycosylated	1619:1632	arg1	one					1658:1660	the one	1654:1660	the one originating from the secretory chain	1654:1697	By scanning the treated spots with low-resolution matrix assisted laser desorption/ionization-time-of-flight-MS, we observed all five deglycosylated peptides, including the one originating from the secretory chain.
25802287	13	74	from	glycans	2170:2176	arg1	Asn					2181:2183	Asn 563	2181:2187	Asn 563	2181:2187	Besides complex type glycans on Asn 395, 332, 171, and on the J chain, we observed oligomannosidic glycans on Asn 563, Asn 402 and minor amounts of oligomannosidic glycans on the glycosite Asn 171.
25802287	13	74	from	glycans	2170:2176	arg1	Asn					2190:2192	Asn 402	2190:2196	Asn 402	2190:2196	Besides complex type glycans on Asn 395, 332, 171, and on the J chain, we observed oligomannosidic glycans on Asn 563, Asn 402 and minor amounts of oligomannosidic glycans on the glycosite Asn 171.
25802287	13	74	from	glycans	2170:2176	arg1	171					2264:2266	the glycosite Asn 171	2246:2266	the glycosite Asn 171	2246:2266	Besides complex type glycans on Asn 395, 332, 171, and on the J chain, we observed oligomannosidic glycans on Asn 563, Asn 402 and minor amounts of oligomannosidic glycans on the glycosite Asn 171.
25802287	13	74	from	glycans	2170:2176	arg1	glycans					2235:2241	oligomannosidic glycans	2219:2241	oligomannosidic glycans	2219:2241	Besides complex type glycans on Asn 395, 332, 171, and on the J chain, we observed oligomannosidic glycans on Asn 563, Asn 402 and minor amounts of oligomannosidic glycans on the glycosite Asn 171.
25802287	13	74	from	glycans	2170:2176	arg1	amounts					2208:2214	minor amounts	2202:2214	minor amounts of oligomannosidic glycans	2202:2241	Besides complex type glycans on Asn 395, 332, 171, and on the J chain, we observed oligomannosidic glycans on Asn 563, Asn 402 and minor amounts of oligomannosidic glycans on the glycosite Asn 171.
25802287	0	75	theme	Immunoglobulin	168:181	arg1	M					183:183	Human Serum Immunoglobulin M	156:183	Human Serum Immunoglobulin M (IgM)	156:189	A Microarray-Matrix-assisted Laser Desorption/Ionization-Mass Spectrometry Approach for Site-specific Protein N-glycosylation Analysis, as Demonstrated for Human Serum Immunoglobulin M (IgM).
25802287	0	75	theme	Immunoglobulin	168:181	arg1	IgM					186:188	IgM	186:188	IgM	186:188	A Microarray-Matrix-assisted Laser Desorption/Ionization-Mass Spectrometry Approach for Site-specific Protein N-glycosylation Analysis, as Demonstrated for Human Serum Immunoglobulin M (IgM).
25802287	7	76	located	located	1221:1227	arg2	clusters					1201:1208	the "intact" glycopeptide clusters	1175:1208	the "intact" glycopeptide clusters	1175:1208	An identified peptide then leads directly to the position of the "intact" glycopeptide clusters, which are located in the adjacent spots.
25802287	7	76	located	located	1221:1227	arg1	spots					1245:1249	the adjacent spots	1232:1249	the adjacent spots	1232:1249	An identified peptide then leads directly to the position of the "intact" glycopeptide clusters, which are located in the adjacent spots.
25802287	7	76	located	located	1221:1227	arg2	located					1221:1227	located	1221:1227	located	1221:1227	An identified peptide then leads directly to the position of the "intact" glycopeptide clusters, which are located in the adjacent spots.
25802287	2	77	theme	microarray-matrix	352:368	arg1	platform					410:417	a nano-liquid chromatography microarray-matrix assisted laser desorption/ionization-MS platform	323:417	a nano-liquid chromatography microarray-matrix assisted laser desorption/ionization-MS platform	323:417	It is based on a nano-liquid chromatography microarray-matrix assisted laser desorption/ionization-MS platform, which employs droplet microfluidics for on-plate nanoliter reactions.
25802287	7	78	from	spots	1245:1249	arg1	clusters					1201:1208	the "intact" glycopeptide clusters	1175:1208	the "intact" glycopeptide clusters	1175:1208	An identified peptide then leads directly to the position of the "intact" glycopeptide clusters, which are located in the adjacent spots.
25802287	7	78	from	spots	1245:1249	arg1	located					1221:1227	located	1221:1227	located	1221:1227	An identified peptide then leads directly to the position of the "intact" glycopeptide clusters, which are located in the adjacent spots.
25802287	1	79	theme	site-specific	230:242	arg1	identification					244:257	site-specific identification	230:257	site-specific identification	230:257	We demonstrate a new approach for the site-specific identification and characterization of protein N-glycosylation.
25802287	14	80	theme	hybrid	2282:2287	arg1	glycans					2294:2300	hybrid type glycans	2282:2300	hybrid type glycans	2282:2300	Furthermore, hybrid type glycans were found on Asn 402, Asn 171 and in traces Asn 332.
25802287	8	81	theme	collision-induced	1333:1349	arg1	experiment					1367:1376	a simple collision-induced dissociation-MS experiment	1324:1376	a simple collision-induced dissociation-MS experiment	1324:1376	Furthermore, the deglycosylated peptide can be sequenced efficiently in a simple collision-induced dissociation-MS experiment.
25802287	7	82	theme	identified	1117:1126	arg1	peptide					1128:1134	An identified peptide	1114:1134	An identified peptide	1114:1134	An identified peptide then leads directly to the position of the "intact" glycopeptide clusters, which are located in the adjacent spots.
25802287	13	83	theme	glycosite	2250:2258	arg1	171					2264:2266	the glycosite Asn 171	2246:2266	the glycosite Asn 171	2246:2266	Besides complex type glycans on Asn 395, 332, 171, and on the J chain, we observed oligomannosidic glycans on Asn 563, Asn 402 and minor amounts of oligomannosidic glycans on the glycosite Asn 171.
25802287	5	84	theme	intact	971:976	arg1	glycopeptides					978:990	the intact glycopeptides	967:990	the intact glycopeptides	967:990	After fractionation, each other spot is treated with PNGaseF to generate two correlated traces within one run, one with treated spots where glycans are enzymatically released from the peptides, and one containing the intact glycopeptides.
25802287	6	85	theme	distinct	1004:1011	arg1	glycosites					1013:1022	distinct glycosites	1004:1022	distinct glycosites	1004:1022	Mining for distinct glycosites is performed by searching for the predicted deglycosylated peptides in the treated trace.
25802287	5	86	theme	other	780:784	arg1	spot					786:789	each other spot	775:789	each other spot	775:789	After fractionation, each other spot is treated with PNGaseF to generate two correlated traces within one run, one with treated spots where glycans are enzymatically released from the peptides, and one containing the intact glycopeptides.
25802287	13	87	theme	complex	2079:2085	arg1	glycans					2092:2098	complex type glycans	2079:2098	complex type glycans on Asn 395, 332, 171, and on the J chain	2079:2139	Besides complex type glycans on Asn 395, 332, 171, and on the J chain, we observed oligomannosidic glycans on Asn 563, Asn 402 and minor amounts of oligomannosidic glycans on the glycosite Asn 171.
25802287	0	88	theme	N-glycosylation	110:124	arg1	Analysis					126:133	Site-specific Protein N-glycosylation Analysis	88:133	Site-specific Protein N-glycosylation Analysis	88:133	A Microarray-Matrix-assisted Laser Desorption/Ionization-Mass Spectrometry Approach for Site-specific Protein N-glycosylation Analysis, as Demonstrated for Human Serum Immunoglobulin M (IgM).
25802287	13	89	theme	oligomannosidic	2219:2233	arg1	glycans					2235:2241	oligomannosidic glycans	2219:2241	oligomannosidic glycans	2219:2241	Besides complex type glycans on Asn 395, 332, 171, and on the J chain, we observed oligomannosidic glycans on Asn 563, Asn 402 and minor amounts of oligomannosidic glycans on the glycosite Asn 171.
25802287	7	90	gly	glycopeptide	1188:1199	arg2	glycopeptide					1188:1199	the "intact" glycopeptide clusters	1175:1208	the "intact" glycopeptide clusters	1175:1208	An identified peptide then leads directly to the position of the "intact" glycopeptide clusters, which are located in the adjacent spots.
25802287	11	91	theme	ionization-Fourier	1886:1903	arg1	transform-MS					1905:1916	a matrix assisted laser desorption ionization-Fourier transform-MS	1851:1916	a matrix assisted laser desorption ionization-Fourier transform-MS	1851:1916	A detailed glycopeptide characterization was then accomplished on the adjacent, untreated spots with high mass resolution and high mass accuracy using a matrix assisted laser desorption ionization-Fourier transform-MS.
25802287	10	92	theme	assisted	1542:1549	arg1	desorption/ionization-time-of-flight-MS					1557:1595	low-resolution matrix assisted laser desorption/ionization-time-of-flight-MS	1520:1595	low-resolution matrix assisted laser desorption/ionization-time-of-flight-MS	1520:1595	By scanning the treated spots with low-resolution matrix assisted laser desorption/ionization-time-of-flight-MS, we observed all five deglycosylated peptides, including the one originating from the secretory chain.
25802287	6	93	theme	predicted	1058:1066	arg1	peptides					1083:1090	the predicted deglycosylated peptides	1054:1090	the predicted deglycosylated peptides	1054:1090	Mining for distinct glycosites is performed by searching for the predicted deglycosylated peptides in the treated trace.
25802287	7	94	from	located	1221:1227	arg1	spots					1245:1249	the adjacent spots	1232:1249	the adjacent spots	1232:1249	An identified peptide then leads directly to the position of the "intact" glycopeptide clusters, which are located in the adjacent spots.
25802287	10	95	theme	low-resolution	1520:1533	arg1	desorption/ionization-time-of-flight-MS					1557:1595	low-resolution matrix assisted laser desorption/ionization-time-of-flight-MS	1520:1595	low-resolution matrix assisted laser desorption/ionization-time-of-flight-MS	1520:1595	By scanning the treated spots with low-resolution matrix assisted laser desorption/ionization-time-of-flight-MS, we observed all five deglycosylated peptides, including the one originating from the secretory chain.
25802287	0	96	theme	Human	156:160	arg1	M					183:183	Human Serum Immunoglobulin M	156:183	Human Serum Immunoglobulin M (IgM)	156:189	A Microarray-Matrix-assisted Laser Desorption/Ionization-Mass Spectrometry Approach for Site-specific Protein N-glycosylation Analysis, as Demonstrated for Human Serum Immunoglobulin M (IgM).
25802287	0	96	theme	Human	156:160	arg1	IgM					186:188	IgM	186:188	IgM	186:188	A Microarray-Matrix-assisted Laser Desorption/Ionization-Mass Spectrometry Approach for Site-specific Protein N-glycosylation Analysis, as Demonstrated for Human Serum Immunoglobulin M (IgM).
25802287	9	97	theme	microarray	1394:1403	arg1	approach					1405:1412	the microarray approach	1390:1412	the microarray approach	1390:1412	We applied the microarray approach to a detailed site-specific glycosylation analysis of human serum IgM.
25802287	0	98	theme	Microarray-Matrix-assisted	2:27	arg1	Spectrometry					62:73	A Microarray-Matrix-assisted Laser Desorption/Ionization-Mass Spectrometry	0:73	A Microarray-Matrix-assisted Laser Desorption/Ionization-Mass Spectrometry	0:73	A Microarray-Matrix-assisted Laser Desorption/Ionization-Mass Spectrometry Approach for Site-specific Protein N-glycosylation Analysis, as Demonstrated for Human Serum Immunoglobulin M (IgM).
25802287	13	99	from	glycans	2092:2098	arg1	Asn					2103:2105	Asn 395, 332	2103:2114	Asn	2103:2105	Besides complex type glycans on Asn 395, 332, 171, and on the J chain, we observed oligomannosidic glycans on Asn 563, Asn 402 and minor amounts of oligomannosidic glycans on the glycosite Asn 171.
25802287	13	99	from	glycans	2092:2098	arg1	chain					2135:2139	the J chain	2129:2139	the J chain	2129:2139	Besides complex type glycans on Asn 395, 332, 171, and on the J chain, we observed oligomannosidic glycans on Asn 563, Asn 402 and minor amounts of oligomannosidic glycans on the glycosite Asn 171.
25802287	12	100	gly	glycopeptide	2002:2013	arg2	glycopeptide					2002:2013	glycopeptide	2002:2013	glycopeptide	2002:2013	We present the first detailed and comprehensive mass spectrometric analysis on the glycopeptide level for human polyclonal IgM with high mass accuracy.
25802287	2	101	theme	on-plate	460:467	arg1	reactions					479:487	on-plate nanoliter reactions	460:487	on-plate nanoliter reactions	460:487	It is based on a nano-liquid chromatography microarray-matrix assisted laser desorption/ionization-MS platform, which employs droplet microfluidics for on-plate nanoliter reactions.
25802287	0	102	theme	Desorption/Ionization-Mass	35:60	arg1	Spectrometry					62:73	A Microarray-Matrix-assisted Laser Desorption/Ionization-Mass Spectrometry	0:73	A Microarray-Matrix-assisted Laser Desorption/Ionization-Mass Spectrometry	0:73	A Microarray-Matrix-assisted Laser Desorption/Ionization-Mass Spectrometry Approach for Site-specific Protein N-glycosylation Analysis, as Demonstrated for Human Serum Immunoglobulin M (IgM).
25802287	9	103	theme	detailed	1419:1426	arg1	analysis					1456:1463	a detailed site-specific glycosylation analysis	1417:1463	a detailed site-specific glycosylation analysis of human serum IgM	1417:1482	We applied the microarray approach to a detailed site-specific glycosylation analysis of human serum IgM.
25802287	10	104	theme	deglycosylated	1619:1632	arg1	peptides					1634:1641	all five deglycosylated peptides	1610:1641	all five deglycosylated peptides	1610:1641	By scanning the treated spots with low-resolution matrix assisted laser desorption/ionization-time-of-flight-MS, we observed all five deglycosylated peptides, including the one originating from the secretory chain.
25802287	10	104	theme	deglycosylated	1619:1632	arg1	one					1658:1660	the one	1654:1660	the one originating from the secretory chain	1654:1697	By scanning the treated spots with low-resolution matrix assisted laser desorption/ionization-time-of-flight-MS, we observed all five deglycosylated peptides, including the one originating from the secretory chain.
25802287	11	105	dep	adjacent	1770:1777	arg1	untreated					1780:1788	untreated	1780:1788	untreated	1780:1788	A detailed glycopeptide characterization was then accomplished on the adjacent, untreated spots with high mass resolution and high mass accuracy using a matrix assisted laser desorption ionization-Fourier transform-MS.
25802287	14	106	theme	in	2337:2338	arg1	Asn					2347:2349	in traces Asn 332	2337:2353	in traces Asn 332	2337:2353	Furthermore, hybrid type glycans were found on Asn 402, Asn 171 and in traces Asn 332.
25802287	3	107	theme	high	561:564	arg1	frequency					566:574	a high frequency	559:574	a high frequency on the microarray	559:592	A chromatographic separation of a proteolytic digest is deposited at a high frequency on the microarray.
25802287	9	108	theme	glycosylation	1442:1454	arg1	analysis					1456:1463	a detailed site-specific glycosylation analysis	1417:1463	a detailed site-specific glycosylation analysis of human serum IgM	1417:1482	We applied the microarray approach to a detailed site-specific glycosylation analysis of human serum IgM.
25802287	12	109	theme	high	2051:2054	arg1	accuracy					2061:2068	high mass accuracy	2051:2068	high mass accuracy	2051:2068	We present the first detailed and comprehensive mass spectrometric analysis on the glycopeptide level for human polyclonal IgM with high mass accuracy.
25802287	11	110	theme	high	1826:1829	arg1	accuracy					1836:1843	high mass accuracy	1826:1843	high mass accuracy	1826:1843	A detailed glycopeptide characterization was then accomplished on the adjacent, untreated spots with high mass resolution and high mass accuracy using a matrix assisted laser desorption ionization-Fourier transform-MS.
25802287	6	111	gly	deglycosylated	1068:1081	arg1	peptides					1083:1090	the predicted deglycosylated peptides	1054:1090	the predicted deglycosylated peptides	1054:1090	Mining for distinct glycosites is performed by searching for the predicted deglycosylated peptides in the treated trace.
25802287	7	112	theme	clusters	1201:1208	arg1	position					1163:1170	the position	1159:1170	the position of the "intact" glycopeptide clusters, which are located in the adjacent spots	1159:1249	An identified peptide then leads directly to the position of the "intact" glycopeptide clusters, which are located in the adjacent spots.
25802287	12	113	theme	spectrometric	1972:1984	arg1	analysis					1986:1993	the first detailed and comprehensive mass spectrometric analysis	1930:1993	the first detailed and comprehensive mass spectrometric analysis on the glycopeptide level for human polyclonal IgM with high mass accuracy	1930:2068	We present the first detailed and comprehensive mass spectrometric analysis on the glycopeptide level for human polyclonal IgM with high mass accuracy.
25802287	3	114	theme	chromatographic	492:506	arg1	separation					508:517	A chromatographic separation	490:517	A chromatographic separation of a proteolytic digest	490:541	A chromatographic separation of a proteolytic digest is deposited at a high frequency on the microarray.
25802287	4	115	theme	separation	616:625	arg1	run					627:629	a short separation run	608:629	a short separation run	608:629	In this way, a short separation run is archived into thousands of nanoliter reaction cavities, and chromatographic peaks are spread over multiple array spots.
25802287	11	116	theme	assisted	1860:1867	arg1	transform-MS					1905:1916	a matrix assisted laser desorption ionization-Fourier transform-MS	1851:1916	a matrix assisted laser desorption ionization-Fourier transform-MS	1851:1916	A detailed glycopeptide characterization was then accomplished on the adjacent, untreated spots with high mass resolution and high mass accuracy using a matrix assisted laser desorption ionization-Fourier transform-MS.
25802287	11	117	theme	glycopeptide	1711:1722	arg1	characterization					1724:1739	A detailed glycopeptide characterization	1700:1739	A detailed glycopeptide characterization	1700:1739	A detailed glycopeptide characterization was then accomplished on the adjacent, untreated spots with high mass resolution and high mass accuracy using a matrix assisted laser desorption ionization-Fourier transform-MS.
25802287	9	118	theme	serum	1474:1478	arg1	IgM					1480:1482	human serum IgM	1468:1482	human serum IgM	1468:1482	We applied the microarray approach to a detailed site-specific glycosylation analysis of human serum IgM.
25802287	12	119	theme	human	2025:2029	arg1	IgM					2042:2044	human polyclonal IgM	2025:2044	human polyclonal IgM with high mass accuracy	2025:2068	We present the first detailed and comprehensive mass spectrometric analysis on the glycopeptide level for human polyclonal IgM with high mass accuracy.
25802287	12	120	from	analysis	1986:1993	arg1	level					2015:2019	the glycopeptide level	1998:2019	the glycopeptide level for human polyclonal IgM with high mass accuracy	1998:2068	We present the first detailed and comprehensive mass spectrometric analysis on the glycopeptide level for human polyclonal IgM with high mass accuracy.
25802287	1	121	dep	identification	244:257	arg1	the					226:228	the	226:228	the	226:228	We demonstrate a new approach for the site-specific identification and characterization of protein N-glycosylation.
25802287	2	122	theme	desorption/ionization-MS	385:408	arg1	platform					410:417	a nano-liquid chromatography microarray-matrix assisted laser desorption/ionization-MS platform	323:417	a nano-liquid chromatography microarray-matrix assisted laser desorption/ionization-MS platform	323:417	It is based on a nano-liquid chromatography microarray-matrix assisted laser desorption/ionization-MS platform, which employs droplet microfluidics for on-plate nanoliter reactions.
25802287	12	123	theme	detailed	1940:1947	arg1	analysis					1986:1993	the first detailed and comprehensive mass spectrometric analysis	1930:1993	the first detailed and comprehensive mass spectrometric analysis on the glycopeptide level for human polyclonal IgM with high mass accuracy	1930:2068	We present the first detailed and comprehensive mass spectrometric analysis on the glycopeptide level for human polyclonal IgM with high mass accuracy.
25802287	4	124	theme	chromatographic	694:708	arg1	peaks					710:714	chromatographic peaks	694:714	chromatographic peaks	694:714	In this way, a short separation run is archived into thousands of nanoliter reaction cavities, and chromatographic peaks are spread over multiple array spots.
25802287	13	125	theme	J	2133:2133	arg1	chain					2135:2139	the J chain	2129:2139	the J chain	2129:2139	Besides complex type glycans on Asn 395, 332, 171, and on the J chain, we observed oligomannosidic glycans on Asn 563, Asn 402 and minor amounts of oligomannosidic glycans on the glycosite Asn 171.
25802287	1	126	theme	protein	283:289	arg1	N-glycosylation					291:305	protein N-glycosylation	283:305	protein N-glycosylation	283:305	We demonstrate a new approach for the site-specific identification and characterization of protein N-glycosylation.
25944660	3	0	theme	O-GlcNAcylation	334:348	arg1	sites					350:354	Four O-GlcNAcylation sites	329:354	Four O-GlcNAcylation sites	329:354	Four O-GlcNAcylation sites were identified in human FOXO1 but directed mutagenesis of each site individually had modest (T317) or no effect (S550, T648, S654) on its O-GlcNAcylation status and transcriptional activity.
25944660	0	1	from	sites	27:31	arg1	FoxO1					36:40	FoxO1	36:40	FoxO1	36:40	Regulatory O-GlcNAcylation sites on FoxO1 are yet to be identified.
25944660	6	2	theme	tryptic	973:979	arg1	peptides					988:995	the tryptic digest peptides	969:995	the tryptic digest peptides	969:995	In an attempt to identify other O-GlcNAcylation sites, we immunoprecipitated wild-type O-GlcNAcylated Foxo1 and analysed the tryptic digest peptides by mass spectrometry using High-energy Collisional Dissociation.
25944660	5	3	theme	sites	728:732	arg1	mutation					707:714	mutation	707:714	mutation of all four sites	707:732	In the present work, we mutated these sites in the mouse Foxo1 and found that mutation of all four sites did not decrease Foxo1 O-GlcNAcylation status and transcriptional activity, and would even tend to increase them.
25944660	5	4	theme	present	636:642	arg1	work					644:647	the present work	632:647	the present work	632:647	In the present work, we mutated these sites in the mouse Foxo1 and found that mutation of all four sites did not decrease Foxo1 O-GlcNAcylation status and transcriptional activity, and would even tend to increase them.
25944660	7	5	theme	O-GlcNAcylation	1090:1104	arg1	site					1106:1109	a new O-GlcNAcylation site	1084:1109	a new O-GlcNAcylation site on Foxo1	1084:1118	We identified T646 as a new O-GlcNAcylation site on Foxo1.
25944660	7	5	theme	O-GlcNAcylation	1090:1104	arg1	T646					1076:1079	T646	1076:1079	T646	1076:1079	We identified T646 as a new O-GlcNAcylation site on Foxo1.
25944660	7	6	theme	new	1086:1088	arg1	site					1106:1109	a new O-GlcNAcylation site	1084:1109	a new O-GlcNAcylation site on Foxo1	1084:1118	We identified T646 as a new O-GlcNAcylation site on Foxo1.
25944660	7	6	theme	new	1086:1088	arg1	T646					1076:1079	T646	1076:1079	T646	1076:1079	We identified T646 as a new O-GlcNAcylation site on Foxo1.
25944660	3	7	theme	transcriptional	522:536	arg1	activity					538:545	transcriptional activity	522:545	transcriptional activity	522:545	Four O-GlcNAcylation sites were identified in human FOXO1 but directed mutagenesis of each site individually had modest (T317) or no effect (S550, T648, S654) on its O-GlcNAcylation status and transcriptional activity.
25944660	2	8	theme	transcriptional	303:317	arg1	activity					319:326	its transcriptional activity	299:326	its transcriptional activity	299:326	We and others previously demonstrated that FoxO1 is O-GlcNAcylated in different cell types, resulting in an increase in its transcriptional activity.
25944660	8	9	theme	directed	1135:1142	arg1	mutagenesis					1144:1154	site directed mutagenesis	1130:1154	site directed mutagenesis of this site individually or together with all four previously identified residues	1130:1237	However, site directed mutagenesis of this site individually or together with all four previously identified residues did not impair Foxo1 O-GlcNAcylation and transcriptional activity.
25944660	9	10	theme	Foxo1	1371:1375	arg1	activity					1377:1384	Foxo1 activity	1371:1384	Foxo1 activity	1371:1384	These results suggest that residues important for the control of Foxo1 activity by O-GlcNAcylation still remain to be identified.
25944660	3	11	contain	had	438:440	arg2	modest					442:447	modest	442:447	modest	442:447	Four O-GlcNAcylation sites were identified in human FOXO1 but directed mutagenesis of each site individually had modest (T317) or no effect (S550, T648, S654) on its O-GlcNAcylation status and transcriptional activity.
25944660	3	11	contain	had	438:440	arg2	effect					462:467	no effect	459:467	no effect (S550, T648, S654)	459:486	Four O-GlcNAcylation sites were identified in human FOXO1 but directed mutagenesis of each site individually had modest (T317) or no effect (S550, T648, S654) on its O-GlcNAcylation status and transcriptional activity.
25944660	3	11	contain	had	438:440	arg1	mutagenesis					400:410	directed mutagenesis	391:410	directed mutagenesis of each site	391:423	Four O-GlcNAcylation sites were identified in human FOXO1 but directed mutagenesis of each site individually had modest (T317) or no effect (S550, T648, S654) on its O-GlcNAcylation status and transcriptional activity.
25944660	3	11	contain	had	438:440	arg2	T317					450:453	T317	450:453	T317	450:453	Four O-GlcNAcylation sites were identified in human FOXO1 but directed mutagenesis of each site individually had modest (T317) or no effect (S550, T648, S654) on its O-GlcNAcylation status and transcriptional activity.
25944660	2	12	from	O-GlcNAcylated	231:244	arg1	types					264:268	different cell types	249:268	different cell types	249:268	We and others previously demonstrated that FoxO1 is O-GlcNAcylated in different cell types, resulting in an increase in its transcriptional activity.
25944660	3	13	theme	human	375:379	arg1	FOXO1					381:385	human FOXO1	375:385	human FOXO1	375:385	Four O-GlcNAcylation sites were identified in human FOXO1 but directed mutagenesis of each site individually had modest (T317) or no effect (S550, T648, S654) on its O-GlcNAcylation status and transcriptional activity.
25944660	5	14	theme	O-GlcNAcylation	757:771	arg1	status					773:778	Foxo1 O-GlcNAcylation status	751:778	Foxo1 O-GlcNAcylation status	751:778	In the present work, we mutated these sites in the mouse Foxo1 and found that mutation of all four sites did not decrease Foxo1 O-GlcNAcylation status and transcriptional activity, and would even tend to increase them.
25944660	8	15	theme	site	1164:1167	arg1	mutagenesis					1144:1154	site directed mutagenesis	1130:1154	site directed mutagenesis of this site individually or together with all four previously identified residues	1130:1237	However, site directed mutagenesis of this site individually or together with all four previously identified residues did not impair Foxo1 O-GlcNAcylation and transcriptional activity.
25944660	8	16	theme	identified	1219:1228	arg1	residues					1230:1237	all four previously identified residues	1199:1237	all four previously identified residues	1199:1237	However, site directed mutagenesis of this site individually or together with all four previously identified residues did not impair Foxo1 O-GlcNAcylation and transcriptional activity.
25944660	0	17	theme	O-GlcNAcylation	11:25	arg1	sites					27:31	Regulatory O-GlcNAcylation sites	0:31	Regulatory O-GlcNAcylation sites on FoxO1	0:40	Regulatory O-GlcNAcylation sites on FoxO1 are yet to be identified.
25944660	0	18	theme	Regulatory	0:9	arg1	sites					27:31	Regulatory O-GlcNAcylation sites	0:31	Regulatory O-GlcNAcylation sites on FoxO1	0:40	Regulatory O-GlcNAcylation sites on FoxO1 are yet to be identified.
25944660	9	19	theme	important	1342:1350	arg1	residues					1333:1340	residues	1333:1340	residues important for the control of Foxo1 activity by O-GlcNAcylation	1333:1403	These results suggest that residues important for the control of Foxo1 activity by O-GlcNAcylation still remain to be identified.
25944660	8	20	theme	site	1130:1133	arg1	mutagenesis					1144:1154	site directed mutagenesis	1130:1154	site directed mutagenesis of this site individually or together with all four previously identified residues	1130:1237	However, site directed mutagenesis of this site individually or together with all four previously identified residues did not impair Foxo1 O-GlcNAcylation and transcriptional activity.
25944660	3	21	theme	directed	391:398	arg1	mutagenesis					400:410	directed mutagenesis	391:410	directed mutagenesis of each site	391:423	Four O-GlcNAcylation sites were identified in human FOXO1 but directed mutagenesis of each site individually had modest (T317) or no effect (S550, T648, S654) on its O-GlcNAcylation status and transcriptional activity.
25944660	6	22	theme	O-GlcNAcylated	935:948	arg1	Foxo1					950:954	wild-type O-GlcNAcylated Foxo1	925:954	wild-type O-GlcNAcylated Foxo1	925:954	In an attempt to identify other O-GlcNAcylation sites, we immunoprecipitated wild-type O-GlcNAcylated Foxo1 and analysed the tryptic digest peptides by mass spectrometry using High-energy Collisional Dissociation.
25944660	1	23	theme	reversible	89:98	arg1	modification					119:130	a reversible post-translational modification	87:130	a reversible post-translational modification that regulates cytosolic and nuclear proteins	87:176	O-GlcNAcylation is a reversible post-translational modification that regulates cytosolic and nuclear proteins.
25944660	1	23	theme	reversible	89:98	arg1	O-GlcNAcylation					68:82	O-GlcNAcylation	68:82	O-GlcNAcylation	68:82	O-GlcNAcylation is a reversible post-translational modification that regulates cytosolic and nuclear proteins.
25944660	2	24	from	types	264:268	arg1	O-GlcNAcylated					231:244	O-GlcNAcylated	231:244	O-GlcNAcylated	231:244	We and others previously demonstrated that FoxO1 is O-GlcNAcylated in different cell types, resulting in an increase in its transcriptional activity.
25944660	6	25	theme	Collisional	1036:1046	arg1	Dissociation					1048:1059	High-energy Collisional Dissociation	1024:1059	High-energy Collisional Dissociation	1024:1059	In an attempt to identify other O-GlcNAcylation sites, we immunoprecipitated wild-type O-GlcNAcylated Foxo1 and analysed the tryptic digest peptides by mass spectrometry using High-energy Collisional Dissociation.
25944660	5	26	theme	transcriptional	784:798	arg1	activity					800:807	transcriptional activity	784:807	transcriptional activity	784:807	In the present work, we mutated these sites in the mouse Foxo1 and found that mutation of all four sites did not decrease Foxo1 O-GlcNAcylation status and transcriptional activity, and would even tend to increase them.
25944660	6	27	theme	wild-type	925:933	arg1	Foxo1					950:954	wild-type O-GlcNAcylated Foxo1	925:954	wild-type O-GlcNAcylated Foxo1	925:954	In an attempt to identify other O-GlcNAcylation sites, we immunoprecipitated wild-type O-GlcNAcylated Foxo1 and analysed the tryptic digest peptides by mass spectrometry using High-energy Collisional Dissociation.
25944660	1	28	theme	post-translational	100:117	arg1	modification					119:130	a reversible post-translational modification	87:130	a reversible post-translational modification that regulates cytosolic and nuclear proteins	87:176	O-GlcNAcylation is a reversible post-translational modification that regulates cytosolic and nuclear proteins.
25944660	1	28	theme	post-translational	100:117	arg1	O-GlcNAcylation					68:82	O-GlcNAcylation	68:82	O-GlcNAcylation	68:82	O-GlcNAcylation is a reversible post-translational modification that regulates cytosolic and nuclear proteins.
25944660	6	29	theme	High-energy	1024:1034	arg1	Dissociation					1048:1059	High-energy Collisional Dissociation	1024:1059	High-energy Collisional Dissociation	1024:1059	In an attempt to identify other O-GlcNAcylation sites, we immunoprecipitated wild-type O-GlcNAcylated Foxo1 and analysed the tryptic digest peptides by mass spectrometry using High-energy Collisional Dissociation.
25944660	5	30	theme	mouse	680:684	arg1	Foxo1					686:690	the mouse Foxo1	676:690	the mouse Foxo1	676:690	In the present work, we mutated these sites in the mouse Foxo1 and found that mutation of all four sites did not decrease Foxo1 O-GlcNAcylation status and transcriptional activity, and would even tend to increase them.
25944660	2	31	theme	cell	259:262	arg1	types					264:268	different cell types	249:268	different cell types	249:268	We and others previously demonstrated that FoxO1 is O-GlcNAcylated in different cell types, resulting in an increase in its transcriptional activity.
25944660	2	32	theme	different	249:257	arg1	types					264:268	different cell types	249:268	different cell types	249:268	We and others previously demonstrated that FoxO1 is O-GlcNAcylated in different cell types, resulting in an increase in its transcriptional activity.
25944660	3	33	theme	site	420:423	arg1	mutagenesis					400:410	directed mutagenesis	391:410	directed mutagenesis of each site	391:423	Four O-GlcNAcylation sites were identified in human FOXO1 but directed mutagenesis of each site individually had modest (T317) or no effect (S550, T648, S654) on its O-GlcNAcylation status and transcriptional activity.
25944660	7	34	from	site	1106:1109	arg1	Foxo1					1114:1118	Foxo1	1114:1118	Foxo1	1114:1118	We identified T646 as a new O-GlcNAcylation site on Foxo1.
25944660	5	35	theme	Foxo1	751:755	arg1	status					773:778	Foxo1 O-GlcNAcylation status	751:778	Foxo1 O-GlcNAcylation status	751:778	In the present work, we mutated these sites in the mouse Foxo1 and found that mutation of all four sites did not decrease Foxo1 O-GlcNAcylation status and transcriptional activity, and would even tend to increase them.
25944660	9	36	theme	activity	1377:1384	arg1	control					1360:1366	the control	1356:1366	the control of Foxo1 activity by O-GlcNAcylation	1356:1403	These results suggest that residues important for the control of Foxo1 activity by O-GlcNAcylation still remain to be identified.
25944660	1	37	theme	nuclear	161:167	arg1	proteins					169:176	cytosolic and nuclear proteins	147:176	cytosolic and nuclear proteins	147:176	O-GlcNAcylation is a reversible post-translational modification that regulates cytosolic and nuclear proteins.
25944660	8	38	theme	transcriptional	1280:1294	arg1	activity					1296:1303	transcriptional activity	1280:1303	transcriptional activity	1280:1303	However, site directed mutagenesis of this site individually or together with all four previously identified residues did not impair Foxo1 O-GlcNAcylation and transcriptional activity.
25944660	2	39	from	increase	287:294	arg1	activity					319:326	its transcriptional activity	299:326	its transcriptional activity	299:326	We and others previously demonstrated that FoxO1 is O-GlcNAcylated in different cell types, resulting in an increase in its transcriptional activity.
25944660	6	40	theme	O-GlcNAcylation	880:894	arg1	sites					896:900	other O-GlcNAcylation sites	874:900	other O-GlcNAcylation sites	874:900	In an attempt to identify other O-GlcNAcylation sites, we immunoprecipitated wild-type O-GlcNAcylated Foxo1 and analysed the tryptic digest peptides by mass spectrometry using High-energy Collisional Dissociation.
25944660	6	41	theme	mass	1000:1003	arg1	spectrometry					1005:1016	mass spectrometry	1000:1016	mass spectrometry using High-energy Collisional Dissociation	1000:1059	In an attempt to identify other O-GlcNAcylation sites, we immunoprecipitated wild-type O-GlcNAcylated Foxo1 and analysed the tryptic digest peptides by mass spectrometry using High-energy Collisional Dissociation.
25944660	3	42	dep	effect	462:467	arg1	S654					482:485	S654	482:485	S654	482:485	Four O-GlcNAcylation sites were identified in human FOXO1 but directed mutagenesis of each site individually had modest (T317) or no effect (S550, T648, S654) on its O-GlcNAcylation status and transcriptional activity.
25944660	3	42	dep	effect	462:467	arg1	T648					476:479	T648	476:479	T648	476:479	Four O-GlcNAcylation sites were identified in human FOXO1 but directed mutagenesis of each site individually had modest (T317) or no effect (S550, T648, S654) on its O-GlcNAcylation status and transcriptional activity.
25944660	3	42	dep	effect	462:467	arg1	S550					470:473	S550	470:473	S550	470:473	Four O-GlcNAcylation sites were identified in human FOXO1 but directed mutagenesis of each site individually had modest (T317) or no effect (S550, T648, S654) on its O-GlcNAcylation status and transcriptional activity.
25944660	1	43	theme	cytosolic	147:155	arg1	proteins					169:176	cytosolic and nuclear proteins	147:176	cytosolic and nuclear proteins	147:176	O-GlcNAcylation is a reversible post-translational modification that regulates cytosolic and nuclear proteins.
25944660	8	44	theme	Foxo1	1254:1258	arg1	O-GlcNAcylation					1260:1274	Foxo1 O-GlcNAcylation	1254:1274	Foxo1 O-GlcNAcylation	1254:1274	However, site directed mutagenesis of this site individually or together with all four previously identified residues did not impair Foxo1 O-GlcNAcylation and transcriptional activity.
25944660	6	45	theme	other	874:878	arg1	sites					896:900	other O-GlcNAcylation sites	874:900	other O-GlcNAcylation sites	874:900	In an attempt to identify other O-GlcNAcylation sites, we immunoprecipitated wild-type O-GlcNAcylated Foxo1 and analysed the tryptic digest peptides by mass spectrometry using High-energy Collisional Dissociation.
25944660	3	46	theme	O-GlcNAcylation	495:509	arg1	status					511:516	its O-GlcNAcylation status	491:516	its O-GlcNAcylation status	491:516	Four O-GlcNAcylation sites were identified in human FOXO1 but directed mutagenesis of each site individually had modest (T317) or no effect (S550, T648, S654) on its O-GlcNAcylation status and transcriptional activity.
25944660	6	47	theme	digest	981:986	arg1	peptides					988:995	the tryptic digest peptides	969:995	the tryptic digest peptides	969:995	In an attempt to identify other O-GlcNAcylation sites, we immunoprecipitated wild-type O-GlcNAcylated Foxo1 and analysed the tryptic digest peptides by mass spectrometry using High-energy Collisional Dissociation.
20622017	8	0	theme	unique	1156:1161	arg1	structures					1163:1172	12 unique structures	1153:1172	12 unique structures	1153:1172	However, analysis of hepatic GGT glycopeptides revealed 11 glycan compositions, with 12 unique structures, none of which were observed on kidney GGT.
20622017	11	1	theme	In	1384:1385	arg1	modeling					1394:1401	In silico modeling	1384:1401	In silico modeling of GGT	1384:1408	In silico modeling of GGT predicts that these two glycans are located in clefts on the surface of the protein facing the cell membrane, and their synthesis may be subject to steric constraints.
20622017	1	2	theme	normal	261:266	arg1	tissue					274:279	normal human tissue	261:279	normal human tissue	261:279	The cell surface glycoprotein γ-glutamyl transpeptidase (GGT) was isolated from healthy human kidney and liver to characterize its glycosylation in normal human tissue in vivo.
20622017	6	3	theme	single	897:902	arg1	site					904:907	a single site	895:907	a single site	895:907	Up to 15 different glycans were observed at a single site, with site-specific variation in glycan composition.
20622017	12	4	theme	novel	1725:1729	arg1	insights					1731:1738	novel insights	1725:1738	novel insights into tissue-specific and site-specific glycosylation in normal human tissues	1725:1815	This is the first analysis at the level of individual glycopeptides of a human glycoprotein produced by two different tissues in vivo and provides novel insights into tissue-specific and site-specific glycosylation in normal human tissues.
20622017	4	5	from	advances	486:493	arg1	spectrometry					503:514	mass spectrometry	498:514	mass spectrometry	498:514	Recent advances in mass spectrometry enabled us to identify the microheterogeneity and relative abundance of glycans on specific glycopeptides and revealed a broader spectrum of glycans than was observed among glycans enzymatically released from isolated GGT.
20622017	9	6	from	variation	1221:1229	arg1	glycosylation					1234:1246	glycosylation	1234:1246	glycosylation	1234:1246	No variation in glycosylation was observed among multiple kidney and liver donors.
20622017	2	7	from	type	324:327	arg1	kidney					336:341	the kidney	332:341	the kidney	332:341	GGT is expressed by a single cell type in the kidney.
20622017	11	8	theme	GGT	1406:1408	arg1	modeling					1394:1401	In silico modeling	1384:1401	In silico modeling of GGT	1384:1408	In silico modeling of GGT predicts that these two glycans are located in clefts on the surface of the protein facing the cell membrane, and their synthesis may be subject to steric constraints.
20622017	12	9	from	level	1612:1616	arg1	analysis					1596:1603	the first analysis	1586:1603	the first analysis	1586:1603	This is the first analysis at the level of individual glycopeptides of a human glycoprotein produced by two different tissues in vivo and provides novel insights into tissue-specific and site-specific glycosylation in normal human tissues.
20622017	12	9	from	level	1612:1616	arg1	This					1578:1581	This	1578:1581	This	1578:1581	This is the first analysis at the level of individual glycopeptides of a human glycoprotein produced by two different tissues in vivo and provides novel insights into tissue-specific and site-specific glycosylation in normal human tissues.
20622017	1	10	theme	healthy	193:199	arg1	kidney					207:212	healthy human kidney	193:212	healthy human kidney	193:212	The cell surface glycoprotein γ-glutamyl transpeptidase (GGT) was isolated from healthy human kidney and liver to characterize its glycosylation in normal human tissue in vivo.
20622017	4	11	theme	broader	637:643	arg1	spectrum					645:652	a broader spectrum	635:652	a broader spectrum of glycans	635:663	Recent advances in mass spectrometry enabled us to identify the microheterogeneity and relative abundance of glycans on specific glycopeptides and revealed a broader spectrum of glycans than was observed among glycans enzymatically released from isolated GGT.
20622017	1	12	gly	glycoprotein	130:141	arg1	glycoprotein					130:141	The cell surface glycoprotein γ-glutamyl transpeptidase	113:167	The cell surface glycoprotein γ-glutamyl transpeptidase (GGT)	113:173	The cell surface glycoprotein γ-glutamyl transpeptidase (GGT) was isolated from healthy human kidney and liver to characterize its glycosylation in normal human tissue in vivo.
20622017	4	13	from	microheterogeneity	543:560	arg1	glycopeptides					608:620	specific glycopeptides	599:620	specific glycopeptides	599:620	Recent advances in mass spectrometry enabled us to identify the microheterogeneity and relative abundance of glycans on specific glycopeptides and revealed a broader spectrum of glycans than was observed among glycans enzymatically released from isolated GGT.
20622017	4	14	theme	isolated	725:732	arg1	GGT					734:736	isolated GGT	725:736	isolated GGT	725:736	Recent advances in mass spectrometry enabled us to identify the microheterogeneity and relative abundance of glycans on specific glycopeptides and revealed a broader spectrum of glycans than was observed among glycans enzymatically released from isolated GGT.
20622017	1	15	from	glycosylation	244:256	arg1	tissue					274:279	normal human tissue	261:279	normal human tissue	261:279	The cell surface glycoprotein γ-glutamyl transpeptidase (GGT) was isolated from healthy human kidney and liver to characterize its glycosylation in normal human tissue in vivo.
20622017	1	16	theme	surface	122:128	arg1	GGT					170:172	GGT	170:172	GGT	170:172	The cell surface glycoprotein γ-glutamyl transpeptidase (GGT) was isolated from healthy human kidney and liver to characterize its glycosylation in normal human tissue in vivo.
20622017	1	16	theme	surface	122:128	arg1	transpeptidase					154:167	The cell surface glycoprotein γ-glutamyl transpeptidase	113:167	The cell surface glycoprotein γ-glutamyl transpeptidase (GGT)	113:173	The cell surface glycoprotein γ-glutamyl transpeptidase (GGT) was isolated from healthy human kidney and liver to characterize its glycosylation in normal human tissue in vivo.
20622017	6	17	theme	site-specific	915:927	arg1	variation					929:937	site-specific variation	915:937	site-specific variation in glycan composition	915:959	Up to 15 different glycans were observed at a single site, with site-specific variation in glycan composition.
20622017	9	18	theme	multiple	1267:1274	arg1	donors					1293:1298	multiple kidney and liver donors	1267:1298	multiple kidney and liver donors	1267:1298	No variation in glycosylation was observed among multiple kidney and liver donors.
20622017	7	19	theme	membrane	992:999	arg1	glycoproteins					1001:1013	liver membrane glycoproteins	986:1013	liver membrane glycoproteins	986:1013	N-Glycans released from liver membrane glycoproteins included many glycans also identified in the kidney.
20622017	1	20	theme	γ-glutamyl	143:152	arg1	GGT					170:172	GGT	170:172	GGT	170:172	The cell surface glycoprotein γ-glutamyl transpeptidase (GGT) was isolated from healthy human kidney and liver to characterize its glycosylation in normal human tissue in vivo.
20622017	1	20	theme	γ-glutamyl	143:152	arg1	transpeptidase					154:167	The cell surface glycoprotein γ-glutamyl transpeptidase	113:167	The cell surface glycoprotein γ-glutamyl transpeptidase (GGT)	113:173	The cell surface glycoprotein γ-glutamyl transpeptidase (GGT) was isolated from healthy human kidney and liver to characterize its glycosylation in normal human tissue in vivo.
20622017	5	21	theme	compositions	760:771	arg1	total					741:745	A total	739:745	A total	739:745	A total of 36 glycan compositions, with 40 unique structures, were identified by site-specific glycan analysis.
20622017	5	22	theme	site-specific	820:832	arg1	analysis					841:848	site-specific glycan analysis	820:848	site-specific glycan analysis	820:848	A total of 36 glycan compositions, with 40 unique structures, were identified by site-specific glycan analysis.
20622017	12	23	theme	human	1651:1655	arg1	glycoprotein					1657:1668	a human glycoprotein	1649:1668	a human glycoprotein produced by two different tissues in vivo	1649:1710	This is the first analysis at the level of individual glycopeptides of a human glycoprotein produced by two different tissues in vivo and provides novel insights into tissue-specific and site-specific glycosylation in normal human tissues.
20622017	11	24	theme	cell	1505:1508	arg1	membrane					1510:1517	the cell membrane	1501:1517	the cell membrane	1501:1517	In silico modeling of GGT predicts that these two glycans are located in clefts on the surface of the protein facing the cell membrane, and their synthesis may be subject to steric constraints.
20622017	4	25	theme	mass	498:501	arg1	spectrometry					503:514	mass spectrometry	498:514	mass spectrometry	498:514	Recent advances in mass spectrometry enabled us to identify the microheterogeneity and relative abundance of glycans on specific glycopeptides and revealed a broader spectrum of glycans than was observed among glycans enzymatically released from isolated GGT.
20622017	0	26	theme	human	99:103	arg1	tissue					105:110	normal human tissue	92:110	normal human tissue	92:110	Analysis of site-specific glycosylation of renal and hepatic γ-glutamyl transpeptidase from normal human tissue.
20622017	1	27	gly	glycosylation	244:256	arg1	tissue					274:279	normal human tissue	261:279	normal human tissue	261:279	The cell surface glycoprotein γ-glutamyl transpeptidase (GGT) was isolated from healthy human kidney and liver to characterize its glycosylation in normal human tissue in vivo.
20622017	12	28	theme	individual	1621:1630	arg1	glycopeptides					1632:1644	individual glycopeptides	1621:1644	individual glycopeptides of a human glycoprotein produced by two different tissues in vivo	1621:1710	This is the first analysis at the level of individual glycopeptides of a human glycoprotein produced by two different tissues in vivo and provides novel insights into tissue-specific and site-specific glycosylation in normal human tissues.
20622017	4	29	from	abundance	575:583	arg1	glycopeptides					608:620	specific glycopeptides	599:620	specific glycopeptides	599:620	Recent advances in mass spectrometry enabled us to identify the microheterogeneity and relative abundance of glycans on specific glycopeptides and revealed a broader spectrum of glycans than was observed among glycans enzymatically released from isolated GGT.
20622017	4	30	dep	microheterogeneity	543:560	arg1	the					539:541	the	539:541	the	539:541	Recent advances in mass spectrometry enabled us to identify the microheterogeneity and relative abundance of glycans on specific glycopeptides and revealed a broader spectrum of glycans than was observed among glycans enzymatically released from isolated GGT.
20622017	3	31	theme	N-glycans	360:368	arg1	spectrum					348:355	The spectrum	344:355	The spectrum of N-glycans released from kidney GGT	344:393	The spectrum of N-glycans released from kidney GGT constituted a subset of the N-glycans identified from renal membrane glycoproteins.
20622017	12	32	gly	glycoprotein	1657:1668	arg1	glycoprotein					1657:1668	a human glycoprotein	1649:1668	a human glycoprotein produced by two different tissues in vivo	1649:1710	This is the first analysis at the level of individual glycopeptides of a human glycoprotein produced by two different tissues in vivo and provides novel insights into tissue-specific and site-specific glycosylation in normal human tissues.
20622017	0	33	theme	transpeptidase	72:85	arg1	glycosylation					26:38	site-specific glycosylation	12:38	site-specific glycosylation of renal and hepatic γ-glutamyl transpeptidase from normal human tissue	12:110	Analysis of site-specific glycosylation of renal and hepatic γ-glutamyl transpeptidase from normal human tissue.
20622017	8	34	gly	glycopeptides	1101:1113	arg2	glycopeptides					1101:1113	hepatic GGT glycopeptides	1089:1113	hepatic GGT glycopeptides	1089:1113	However, analysis of hepatic GGT glycopeptides revealed 11 glycan compositions, with 12 unique structures, none of which were observed on kidney GGT.
20622017	3	35	gly	glycoproteins	464:476	arg1	glycoproteins					464:476	renal membrane glycoproteins	449:476	renal membrane glycoproteins	449:476	The spectrum of N-glycans released from kidney GGT constituted a subset of the N-glycans identified from renal membrane glycoproteins.
20622017	0	36	theme	site-specific	12:24	arg1	glycosylation					26:38	site-specific glycosylation	12:38	site-specific glycosylation of renal and hepatic γ-glutamyl transpeptidase from normal human tissue	12:110	Analysis of site-specific glycosylation of renal and hepatic γ-glutamyl transpeptidase from normal human tissue.
20622017	7	37	attach	released	972:979	arg2	N-Glycans					962:970	N-Glycans	962:970	N-Glycans released from liver membrane glycoproteins	962:1013	N-Glycans released from liver membrane glycoproteins included many glycans also identified in the kidney.
20622017	7	37	attach	released	972:979	arg1	glycoproteins					1001:1013	liver membrane glycoproteins	986:1013	liver membrane glycoproteins	986:1013	N-Glycans released from liver membrane glycoproteins included many glycans also identified in the kidney.
20622017	12	38	gly	glycopeptides	1632:1644	arg1	glycoprotein					1657:1668	a human glycoprotein	1649:1668	a human glycoprotein produced by two different tissues in vivo	1649:1710	This is the first analysis at the level of individual glycopeptides of a human glycoprotein produced by two different tissues in vivo and provides novel insights into tissue-specific and site-specific glycosylation in normal human tissues.
20622017	12	38	gly	glycopeptides	1632:1644	arg2	glycopeptides					1632:1644	individual glycopeptides	1621:1644	individual glycopeptides of a human glycoprotein produced by two different tissues in vivo	1621:1710	This is the first analysis at the level of individual glycopeptides of a human glycoprotein produced by two different tissues in vivo and provides novel insights into tissue-specific and site-specific glycosylation in normal human tissues.
20622017	3	39	theme	N-glycans	423:431	arg1	subset					409:414	a subset	407:414	a subset of the N-glycans identified from renal membrane glycoproteins	407:476	The spectrum of N-glycans released from kidney GGT constituted a subset of the N-glycans identified from renal membrane glycoproteins.
20622017	5	40	theme	unique	782:787	arg1	structures					789:798	40 unique structures	779:798	40 unique structures	779:798	A total of 36 glycan compositions, with 40 unique structures, were identified by site-specific glycan analysis.
20622017	8	41	theme	GGT	1097:1099	arg1	glycopeptides					1101:1113	hepatic GGT glycopeptides	1089:1113	hepatic GGT glycopeptides	1089:1113	However, analysis of hepatic GGT glycopeptides revealed 11 glycan compositions, with 12 unique structures, none of which were observed on kidney GGT.
20622017	12	42	theme	human	1803:1807	arg1	tissues					1809:1815	normal human tissues	1796:1815	normal human tissues	1796:1815	This is the first analysis at the level of individual glycopeptides of a human glycoprotein produced by two different tissues in vivo and provides novel insights into tissue-specific and site-specific glycosylation in normal human tissues.
20622017	6	43	from	variation	929:937	arg1	composition					949:959	glycan composition	942:959	glycan composition	942:959	Up to 15 different glycans were observed at a single site, with site-specific variation in glycan composition.
20622017	0	44	theme	γ-glutamyl	61:70	arg1	transpeptidase					72:85	renal and hepatic γ-glutamyl transpeptidase	43:85	renal and hepatic γ-glutamyl transpeptidase from normal human tissue	43:110	Analysis of site-specific glycosylation of renal and hepatic γ-glutamyl transpeptidase from normal human tissue.
20622017	8	45	located	observed	1194:1201	arg1	GGT					1213:1215	kidney GGT	1206:1215	kidney GGT	1206:1215	However, analysis of hepatic GGT glycopeptides revealed 11 glycan compositions, with 12 unique structures, none of which were observed on kidney GGT.
20622017	8	45	located	observed	1194:1201	arg2	none					1175:1178	none	1175:1178	none	1175:1178	However, analysis of hepatic GGT glycopeptides revealed 11 glycan compositions, with 12 unique structures, none of which were observed on kidney GGT.
20622017	0	46	gly	glycosylation	26:38	arg1	transpeptidase					72:85	renal and hepatic γ-glutamyl transpeptidase	43:85	renal and hepatic γ-glutamyl transpeptidase from normal human tissue	43:110	Analysis of site-specific glycosylation of renal and hepatic γ-glutamyl transpeptidase from normal human tissue.
20622017	10	47	theme	renal	1328:1332	arg1	GGT					1334:1336	renal GGT	1328:1336	renal GGT	1328:1336	Two glycosylation sites on renal GGT were modified exclusively by neutral glycans.
20622017	3	48	theme	membrane	455:462	arg1	glycoproteins					464:476	renal membrane glycoproteins	449:476	renal membrane glycoproteins	449:476	The spectrum of N-glycans released from kidney GGT constituted a subset of the N-glycans identified from renal membrane glycoproteins.
20622017	8	49	theme	glycan	1127:1132	arg1	compositions					1134:1145	11 glycan compositions	1124:1145	11 glycan compositions	1124:1145	However, analysis of hepatic GGT glycopeptides revealed 11 glycan compositions, with 12 unique structures, none of which were observed on kidney GGT.
20622017	12	50	theme	site-specific	1765:1777	arg1	glycosylation					1779:1791	tissue-specific and site-specific glycosylation	1745:1791	tissue-specific and site-specific glycosylation in normal human tissues	1745:1815	This is the first analysis at the level of individual glycopeptides of a human glycoprotein produced by two different tissues in vivo and provides novel insights into tissue-specific and site-specific glycosylation in normal human tissues.
20622017	4	51	theme	specific	599:606	arg1	glycopeptides					608:620	specific glycopeptides	599:620	specific glycopeptides	599:620	Recent advances in mass spectrometry enabled us to identify the microheterogeneity and relative abundance of glycans on specific glycopeptides and revealed a broader spectrum of glycans than was observed among glycans enzymatically released from isolated GGT.
20622017	10	52	theme	neutral	1367:1373	arg1	glycans					1375:1381	neutral glycans	1367:1381	neutral glycans	1367:1381	Two glycosylation sites on renal GGT were modified exclusively by neutral glycans.
20622017	12	53	from	glycosylation	1779:1791	arg1	tissues					1809:1815	normal human tissues	1796:1815	normal human tissues	1796:1815	This is the first analysis at the level of individual glycopeptides of a human glycoprotein produced by two different tissues in vivo and provides novel insights into tissue-specific and site-specific glycosylation in normal human tissues.
20622017	8	54	with	compositions	1134:1145	arg1	structures					1163:1172	12 unique structures	1153:1172	12 unique structures	1153:1172	However, analysis of hepatic GGT glycopeptides revealed 11 glycan compositions, with 12 unique structures, none of which were observed on kidney GGT.
20622017	4	55	from	glycopeptides	608:620	arg1	microheterogeneity					543:560	microheterogeneity	543:560	microheterogeneity	543:560	Recent advances in mass spectrometry enabled us to identify the microheterogeneity and relative abundance of glycans on specific glycopeptides and revealed a broader spectrum of glycans than was observed among glycans enzymatically released from isolated GGT.
20622017	4	55	from	glycopeptides	608:620	arg1	abundance					575:583	relative abundance	566:583	relative abundance	566:583	Recent advances in mass spectrometry enabled us to identify the microheterogeneity and relative abundance of glycans on specific glycopeptides and revealed a broader spectrum of glycans than was observed among glycans enzymatically released from isolated GGT.
20622017	11	56	located	located	1446:1452	arg1	clefts					1457:1462	clefts	1457:1462	clefts on the surface of the protein facing the cell membrane	1457:1517	In silico modeling of GGT predicts that these two glycans are located in clefts on the surface of the protein facing the cell membrane, and their synthesis may be subject to steric constraints.
20622017	11	56	located	located	1446:1452	arg2	glycans					1434:1440	these two glycans	1424:1440	these two glycans	1424:1440	In silico modeling of GGT predicts that these two glycans are located in clefts on the surface of the protein facing the cell membrane, and their synthesis may be subject to steric constraints.
20622017	1	57	theme	human	268:272	arg1	tissue					274:279	normal human tissue	261:279	normal human tissue	261:279	The cell surface glycoprotein γ-glutamyl transpeptidase (GGT) was isolated from healthy human kidney and liver to characterize its glycosylation in normal human tissue in vivo.
20622017	12	58	theme	tissue-specific	1745:1759	arg1	glycosylation					1779:1791	tissue-specific and site-specific glycosylation	1745:1791	tissue-specific and site-specific glycosylation in normal human tissues	1745:1815	This is the first analysis at the level of individual glycopeptides of a human glycoprotein produced by two different tissues in vivo and provides novel insights into tissue-specific and site-specific glycosylation in normal human tissues.
20622017	4	59	theme	glycans	588:594	arg1	microheterogeneity					543:560	microheterogeneity	543:560	microheterogeneity	543:560	Recent advances in mass spectrometry enabled us to identify the microheterogeneity and relative abundance of glycans on specific glycopeptides and revealed a broader spectrum of glycans than was observed among glycans enzymatically released from isolated GGT.
20622017	4	59	theme	glycans	588:594	arg1	abundance					575:583	relative abundance	566:583	relative abundance	566:583	Recent advances in mass spectrometry enabled us to identify the microheterogeneity and relative abundance of glycans on specific glycopeptides and revealed a broader spectrum of glycans than was observed among glycans enzymatically released from isolated GGT.
20622017	12	60	gly	glycosylation	1779:1791	arg1	tissues					1809:1815	normal human tissues	1796:1815	normal human tissues	1796:1815	This is the first analysis at the level of individual glycopeptides of a human glycoprotein produced by two different tissues in vivo and provides novel insights into tissue-specific and site-specific glycosylation in normal human tissues.
20622017	4	61	theme	glycans	657:663	arg1	spectrum					645:652	a broader spectrum	635:652	a broader spectrum of glycans	635:663	Recent advances in mass spectrometry enabled us to identify the microheterogeneity and relative abundance of glycans on specific glycopeptides and revealed a broader spectrum of glycans than was observed among glycans enzymatically released from isolated GGT.
20622017	4	62	attach	released	711:718	arg1	GGT					734:736	isolated GGT	725:736	isolated GGT	725:736	Recent advances in mass spectrometry enabled us to identify the microheterogeneity and relative abundance of glycans on specific glycopeptides and revealed a broader spectrum of glycans than was observed among glycans enzymatically released from isolated GGT.
20622017	4	62	attach	released	711:718	arg2	glycans					689:695	glycans	689:695	glycans enzymatically released from isolated GGT	689:736	Recent advances in mass spectrometry enabled us to identify the microheterogeneity and relative abundance of glycans on specific glycopeptides and revealed a broader spectrum of glycans than was observed among glycans enzymatically released from isolated GGT.
20622017	6	63	located	observed	883:890	arg2	glycans					870:876	Up to 15 different glycans	851:876	Up to 15 different glycans	851:876	Up to 15 different glycans were observed at a single site, with site-specific variation in glycan composition.
20622017	6	63	located	observed	883:890	arg1	site					904:907	a single site	895:907	a single site	895:907	Up to 15 different glycans were observed at a single site, with site-specific variation in glycan composition.
20622017	5	64	theme	glycan	834:839	arg1	analysis					841:848	site-specific glycan analysis	820:848	site-specific glycan analysis	820:848	A total of 36 glycan compositions, with 40 unique structures, were identified by site-specific glycan analysis.
20622017	12	65	theme	first	1590:1594	arg1	analysis					1596:1603	the first analysis	1586:1603	the first analysis	1586:1603	This is the first analysis at the level of individual glycopeptides of a human glycoprotein produced by two different tissues in vivo and provides novel insights into tissue-specific and site-specific glycosylation in normal human tissues.
20622017	12	65	theme	first	1590:1594	arg1	This					1578:1581	This	1578:1581	This	1578:1581	This is the first analysis at the level of individual glycopeptides of a human glycoprotein produced by two different tissues in vivo and provides novel insights into tissue-specific and site-specific glycosylation in normal human tissues.
20622017	11	66	dep	In	1384:1385	arg1	silico					1387:1392	silico	1387:1392	silico	1387:1392	In silico modeling of GGT predicts that these two glycans are located in clefts on the surface of the protein facing the cell membrane, and their synthesis may be subject to steric constraints.
20622017	8	67	theme	kidney	1206:1211	arg1	GGT					1213:1215	kidney GGT	1206:1215	kidney GGT	1206:1215	However, analysis of hepatic GGT glycopeptides revealed 11 glycan compositions, with 12 unique structures, none of which were observed on kidney GGT.
20622017	6	68	theme	glycan	942:947	arg1	composition					949:959	glycan composition	942:959	glycan composition	942:959	Up to 15 different glycans were observed at a single site, with site-specific variation in glycan composition.
20622017	10	69	gly	glycosylation	1305:1317	arg2	sites					1319:1323	Two glycosylation sites	1301:1323	Two glycosylation sites on renal GGT	1301:1336	Two glycosylation sites on renal GGT were modified exclusively by neutral glycans.
20622017	10	69	gly	glycosylation	1305:1317	arg2	Two					1301:1303	Two	1301:1303	Two	1301:1303	Two glycosylation sites on renal GGT were modified exclusively by neutral glycans.
20622017	4	70	gly	microheterogeneity	543:560	arg1	glycans					588:594	glycans	588:594	glycans on specific glycopeptides	588:620	Recent advances in mass spectrometry enabled us to identify the microheterogeneity and relative abundance of glycans on specific glycopeptides and revealed a broader spectrum of glycans than was observed among glycans enzymatically released from isolated GGT.
20622017	1	71	theme	cell	117:120	arg1	GGT					170:172	GGT	170:172	GGT	170:172	The cell surface glycoprotein γ-glutamyl transpeptidase (GGT) was isolated from healthy human kidney and liver to characterize its glycosylation in normal human tissue in vivo.
20622017	1	71	theme	cell	117:120	arg1	transpeptidase					154:167	The cell surface glycoprotein γ-glutamyl transpeptidase	113:167	The cell surface glycoprotein γ-glutamyl transpeptidase (GGT)	113:173	The cell surface glycoprotein γ-glutamyl transpeptidase (GGT) was isolated from healthy human kidney and liver to characterize its glycosylation in normal human tissue in vivo.
20622017	3	72	attach	released	370:377	arg1	GGT					391:393	kidney GGT	384:393	kidney GGT	384:393	The spectrum of N-glycans released from kidney GGT constituted a subset of the N-glycans identified from renal membrane glycoproteins.
20622017	3	72	attach	released	370:377	arg2	N-glycans					360:368	N-glycans	360:368	N-glycans released from kidney GGT	360:393	The spectrum of N-glycans released from kidney GGT constituted a subset of the N-glycans identified from renal membrane glycoproteins.
20622017	5	73	with	total	741:745	arg1	structures					789:798	40 unique structures	779:798	40 unique structures	779:798	A total of 36 glycan compositions, with 40 unique structures, were identified by site-specific glycan analysis.
20622017	7	74	theme	many	1024:1027	arg1	glycans					1029:1035	many glycans	1024:1035	many glycans also identified in the kidney	1024:1065	N-Glycans released from liver membrane glycoproteins included many glycans also identified in the kidney.
20622017	1	75	theme	glycoprotein	130:141	arg1	GGT					170:172	GGT	170:172	GGT	170:172	The cell surface glycoprotein γ-glutamyl transpeptidase (GGT) was isolated from healthy human kidney and liver to characterize its glycosylation in normal human tissue in vivo.
20622017	1	75	theme	glycoprotein	130:141	arg1	transpeptidase					154:167	The cell surface glycoprotein γ-glutamyl transpeptidase	113:167	The cell surface glycoprotein γ-glutamyl transpeptidase (GGT)	113:173	The cell surface glycoprotein γ-glutamyl transpeptidase (GGT) was isolated from healthy human kidney and liver to characterize its glycosylation in normal human tissue in vivo.
20622017	11	76	theme	steric	1558:1563	arg1	constraints					1565:1575	steric constraints	1558:1575	steric constraints	1558:1575	In silico modeling of GGT predicts that these two glycans are located in clefts on the surface of the protein facing the cell membrane, and their synthesis may be subject to steric constraints.
20622017	0	77	from	tissue	105:110	arg1	glycosylation					26:38	site-specific glycosylation	12:38	site-specific glycosylation of renal and hepatic γ-glutamyl transpeptidase from normal human tissue	12:110	Analysis of site-specific glycosylation of renal and hepatic γ-glutamyl transpeptidase from normal human tissue.
20622017	0	77	from	tissue	105:110	arg1	transpeptidase					72:85	renal and hepatic γ-glutamyl transpeptidase	43:85	renal and hepatic γ-glutamyl transpeptidase from normal human tissue	43:110	Analysis of site-specific glycosylation of renal and hepatic γ-glutamyl transpeptidase from normal human tissue.
20622017	2	78	theme	cell	319:322	arg1	type					324:327	a single cell type	310:327	a single cell type in the kidney	310:341	GGT is expressed by a single cell type in the kidney.
20622017	5	79	theme	glycan	753:758	arg1	compositions					760:771	36 glycan compositions	750:771	36 glycan compositions	750:771	A total of 36 glycan compositions, with 40 unique structures, were identified by site-specific glycan analysis.
20622017	9	80	theme	kidney	1276:1281	arg1	donors					1293:1298	multiple kidney and liver donors	1267:1298	multiple kidney and liver donors	1267:1298	No variation in glycosylation was observed among multiple kidney and liver donors.
20622017	1	81	theme	human	201:205	arg1	kidney					207:212	healthy human kidney	193:212	healthy human kidney	193:212	The cell surface glycoprotein γ-glutamyl transpeptidase (GGT) was isolated from healthy human kidney and liver to characterize its glycosylation in normal human tissue in vivo.
20622017	12	82	theme	different	1686:1694	arg1	tissues					1696:1702	two different tissues	1682:1702	two different tissues	1682:1702	This is the first analysis at the level of individual glycopeptides of a human glycoprotein produced by two different tissues in vivo and provides novel insights into tissue-specific and site-specific glycosylation in normal human tissues.
20622017	0	83	from	glycosylation	26:38	arg1	tissue					105:110	normal human tissue	92:110	normal human tissue	92:110	Analysis of site-specific glycosylation of renal and hepatic γ-glutamyl transpeptidase from normal human tissue.
20622017	10	84	from	sites	1319:1323	arg1	GGT					1334:1336	renal GGT	1328:1336	renal GGT	1328:1336	Two glycosylation sites on renal GGT were modified exclusively by neutral glycans.
20622017	4	85	from	glycans	588:594	arg1	glycopeptides					608:620	specific glycopeptides	599:620	specific glycopeptides	599:620	Recent advances in mass spectrometry enabled us to identify the microheterogeneity and relative abundance of glycans on specific glycopeptides and revealed a broader spectrum of glycans than was observed among glycans enzymatically released from isolated GGT.
20622017	0	86	theme	normal	92:97	arg1	tissue					105:110	normal human tissue	92:110	normal human tissue	92:110	Analysis of site-specific glycosylation of renal and hepatic γ-glutamyl transpeptidase from normal human tissue.
20622017	9	87	theme	liver	1287:1291	arg1	donors					1293:1298	multiple kidney and liver donors	1267:1298	multiple kidney and liver donors	1267:1298	No variation in glycosylation was observed among multiple kidney and liver donors.
20622017	7	88	theme	liver	986:990	arg1	glycoproteins					1001:1013	liver membrane glycoproteins	986:1013	liver membrane glycoproteins	986:1013	N-Glycans released from liver membrane glycoproteins included many glycans also identified in the kidney.
20622017	11	89	theme	protein	1486:1492	arg1	surface					1471:1477	the surface	1467:1477	the surface of the protein facing the cell membrane	1467:1517	In silico modeling of GGT predicts that these two glycans are located in clefts on the surface of the protein facing the cell membrane, and their synthesis may be subject to steric constraints.
20622017	4	90	gly	glycopeptides	608:620	arg2	glycopeptides					608:620	specific glycopeptides	599:620	specific glycopeptides	599:620	Recent advances in mass spectrometry enabled us to identify the microheterogeneity and relative abundance of glycans on specific glycopeptides and revealed a broader spectrum of glycans than was observed among glycans enzymatically released from isolated GGT.
20622017	12	91	theme	glycoprotein	1657:1668	arg1	glycopeptides					1632:1644	individual glycopeptides	1621:1644	individual glycopeptides of a human glycoprotein produced by two different tissues in vivo	1621:1710	This is the first analysis at the level of individual glycopeptides of a human glycoprotein produced by two different tissues in vivo and provides novel insights into tissue-specific and site-specific glycosylation in normal human tissues.
20622017	10	92	mod	modified	1343:1350	arg3	glycans					1375:1381	neutral glycans	1367:1381	neutral glycans	1367:1381	Two glycosylation sites on renal GGT were modified exclusively by neutral glycans.
20622017	10	92	mod	modified	1343:1350	arg1	sites					1319:1323	Two glycosylation sites	1301:1323	Two glycosylation sites on renal GGT	1301:1336	Two glycosylation sites on renal GGT were modified exclusively by neutral glycans.
20622017	4	93	theme	Recent	479:484	arg1	advances					486:493	Recent advances	479:493	Recent advances in mass spectrometry	479:514	Recent advances in mass spectrometry enabled us to identify the microheterogeneity and relative abundance of glycans on specific glycopeptides and revealed a broader spectrum of glycans than was observed among glycans enzymatically released from isolated GGT.
20622017	12	94	theme	glycopeptides	1632:1644	arg1	level					1612:1616	the level	1608:1616	the level of individual glycopeptides of a human glycoprotein produced by two different tissues in vivo	1608:1710	This is the first analysis at the level of individual glycopeptides of a human glycoprotein produced by two different tissues in vivo and provides novel insights into tissue-specific and site-specific glycosylation in normal human tissues.
20622017	7	95	gly	glycoproteins	1001:1013	arg1	glycoproteins					1001:1013	liver membrane glycoproteins	986:1013	liver membrane glycoproteins	986:1013	N-Glycans released from liver membrane glycoproteins included many glycans also identified in the kidney.
20622017	0	96	theme	glycosylation	26:38	arg1	Analysis					0:7	Analysis	0:7	Analysis of site-specific glycosylation of renal and hepatic γ-glutamyl transpeptidase from normal human tissue.	0:111	Analysis of site-specific glycosylation of renal and hepatic γ-glutamyl transpeptidase from normal human tissue.
20622017	8	97	theme	hepatic	1089:1095	arg1	glycopeptides					1101:1113	hepatic GGT glycopeptides	1089:1113	hepatic GGT glycopeptides	1089:1113	However, analysis of hepatic GGT glycopeptides revealed 11 glycan compositions, with 12 unique structures, none of which were observed on kidney GGT.
20622017	4	98	theme	relative	566:573	arg1	abundance					575:583	relative abundance	566:583	relative abundance	566:583	Recent advances in mass spectrometry enabled us to identify the microheterogeneity and relative abundance of glycans on specific glycopeptides and revealed a broader spectrum of glycans than was observed among glycans enzymatically released from isolated GGT.
20622017	1	99	attach	isolated	179:186	arg1	kidney					207:212	healthy human kidney	193:212	healthy human kidney	193:212	The cell surface glycoprotein γ-glutamyl transpeptidase (GGT) was isolated from healthy human kidney and liver to characterize its glycosylation in normal human tissue in vivo.
20622017	1	99	attach	isolated	179:186	arg2	GGT					170:172	GGT	170:172	GGT	170:172	The cell surface glycoprotein γ-glutamyl transpeptidase (GGT) was isolated from healthy human kidney and liver to characterize its glycosylation in normal human tissue in vivo.
20622017	1	99	attach	isolated	179:186	arg2	transpeptidase					154:167	The cell surface glycoprotein γ-glutamyl transpeptidase	113:167	The cell surface glycoprotein γ-glutamyl transpeptidase (GGT)	113:173	The cell surface glycoprotein γ-glutamyl transpeptidase (GGT) was isolated from healthy human kidney and liver to characterize its glycosylation in normal human tissue in vivo.
20622017	1	99	attach	isolated	179:186	arg1	liver					218:222	liver	218:222	liver	218:222	The cell surface glycoprotein γ-glutamyl transpeptidase (GGT) was isolated from healthy human kidney and liver to characterize its glycosylation in normal human tissue in vivo.
20622017	10	100	theme	glycosylation	1305:1317	arg1	sites					1319:1323	Two glycosylation sites	1301:1323	Two glycosylation sites on renal GGT	1301:1336	Two glycosylation sites on renal GGT were modified exclusively by neutral glycans.
20622017	3	101	theme	renal	449:453	arg1	glycoproteins					464:476	renal membrane glycoproteins	449:476	renal membrane glycoproteins	449:476	The spectrum of N-glycans released from kidney GGT constituted a subset of the N-glycans identified from renal membrane glycoproteins.
20622017	0	102	theme	renal	43:47	arg1	transpeptidase					72:85	renal and hepatic γ-glutamyl transpeptidase	43:85	renal and hepatic γ-glutamyl transpeptidase from normal human tissue	43:110	Analysis of site-specific glycosylation of renal and hepatic γ-glutamyl transpeptidase from normal human tissue.
20622017	8	103	theme	glycopeptides	1101:1113	arg1	analysis					1077:1084	analysis	1077:1084	analysis of hepatic GGT glycopeptides	1077:1113	However, analysis of hepatic GGT glycopeptides revealed 11 glycan compositions, with 12 unique structures, none of which were observed on kidney GGT.
20622017	6	104	theme	different	860:868	arg1	glycans					870:876	Up to 15 different glycans	851:876	Up to 15 different glycans	851:876	Up to 15 different glycans were observed at a single site, with site-specific variation in glycan composition.
20622017	11	105	from	located	1446:1452	arg1	clefts					1457:1462	clefts	1457:1462	clefts on the surface of the protein facing the cell membrane	1457:1517	In silico modeling of GGT predicts that these two glycans are located in clefts on the surface of the protein facing the cell membrane, and their synthesis may be subject to steric constraints.
20622017	6	106	dep	15	857:858	arg1	to					854:855	to	854:855	to	854:855	Up to 15 different glycans were observed at a single site, with site-specific variation in glycan composition.
20622017	0	107	theme	hepatic	53:59	arg1	transpeptidase					72:85	renal and hepatic γ-glutamyl transpeptidase	43:85	renal and hepatic γ-glutamyl transpeptidase from normal human tissue	43:110	Analysis of site-specific glycosylation of renal and hepatic γ-glutamyl transpeptidase from normal human tissue.
20622017	11	108	from	clefts	1457:1462	arg1	surface					1471:1477	the surface	1467:1477	the surface of the protein facing the cell membrane	1467:1517	In silico modeling of GGT predicts that these two glycans are located in clefts on the surface of the protein facing the cell membrane, and their synthesis may be subject to steric constraints.
20622017	11	108	from	clefts	1457:1462	arg1	located					1446:1452	located	1446:1452	located	1446:1452	In silico modeling of GGT predicts that these two glycans are located in clefts on the surface of the protein facing the cell membrane, and their synthesis may be subject to steric constraints.
20622017	12	109	theme	normal	1796:1801	arg1	tissues					1809:1815	normal human tissues	1796:1815	normal human tissues	1796:1815	This is the first analysis at the level of individual glycopeptides of a human glycoprotein produced by two different tissues in vivo and provides novel insights into tissue-specific and site-specific glycosylation in normal human tissues.
20622017	3	110	theme	kidney	384:389	arg1	GGT					391:393	kidney GGT	384:393	kidney GGT	384:393	The spectrum of N-glycans released from kidney GGT constituted a subset of the N-glycans identified from renal membrane glycoproteins.
20622017	2	111	theme	single	312:317	arg1	type					324:327	a single cell type	310:327	a single cell type in the kidney	310:341	GGT is expressed by a single cell type in the kidney.
23269669	2	0	theme	fluid-ion	357:365	arg1	homeostasis					367:377	fluid-ion homeostasis	357:377	fluid-ion homeostasis	357:377	GC-C is primarily expressed in the gastrointestinal tract, where it mediates fluid-ion homeostasis, intestinal inflammation, and cell proliferation in a cGMP-dependent manner, following activation by its ligands guanylin, uroguanylin, or the heat-stable enterotoxin peptide (ST).
23269669	1	1	theme	guanylyl	262:269	arg1	cyclase					271:277	membrane-associated receptor guanylyl cyclase	233:277	membrane-associated receptor guanylyl cyclase	233:277	Guanylyl cyclase C (GC-C) is a multidomain, membrane-associated receptor guanylyl cyclase.
23269669	1	1	theme	guanylyl	262:269	arg1	multidomain					220:230	a multidomain	218:230	a multidomain	218:230	Guanylyl cyclase C (GC-C) is a multidomain, membrane-associated receptor guanylyl cyclase.
23269669	9	2	theme	many	1601:1604	arg1	diseases					1606:1613	many diseases	1601:1613	many diseases	1601:1613	Because glycosylation of proteins is altered in many diseases and in a tissue-dependent manner, the activity and/or glycan-mediated interactions of GC-C may have a crucial role to play in its functions in different cell types.
23269669	6	3	theme	glycosylation	1148:1160	arg1	sites					1139:1143	the 10 sites	1132:1143	the 10 sites of glycosylation in GC-C	1132:1168	Systematic mutagenesis of each of the 10 sites of glycosylation in GC-C, either singly or in combination, identified two sites that were critical for ligand binding and two that regulated ST-mediated activation.
23269669	6	3	theme	glycosylation	1148:1160	arg1	glycosylation					1148:1160	glycosylation	1148:1160	glycosylation	1148:1160	Systematic mutagenesis of each of the 10 sites of glycosylation in GC-C, either singly or in combination, identified two sites that were critical for ligand binding and two that regulated ST-mediated activation.
23269669	9	4	contain	have	1710:1713	arg2	role					1725:1728	a crucial role	1715:1728	a crucial role	1715:1728	Because glycosylation of proteins is altered in many diseases and in a tissue-dependent manner, the activity and/or glycan-mediated interactions of GC-C may have a crucial role to play in its functions in different cell types.
23269669	9	4	contain	have	1710:1713	arg1	activity					1653:1660	activity	1653:1660	activity	1653:1660	Because glycosylation of proteins is altered in many diseases and in a tissue-dependent manner, the activity and/or glycan-mediated interactions of GC-C may have a crucial role to play in its functions in different cell types.
23269669	9	4	contain	have	1710:1713	arg1	interactions					1685:1696	glycan-mediated interactions	1669:1696	glycan-mediated interactions	1669:1696	Because glycosylation of proteins is altered in many diseases and in a tissue-dependent manner, the activity and/or glycan-mediated interactions of GC-C may have a crucial role to play in its functions in different cell types.
23269669	7	5	theme	protein	1425:1431	arg1	GC-C					1328:1331	GC-C	1328:1331	GC-C	1328:1331	We also show that GC-C is the first identified receptor client of the lectin chaperone vesicular integral membrane protein, VIP36.
23269669	7	5	theme	protein	1425:1431	arg1	client					1366:1371	the first identified receptor client	1336:1371	the first identified receptor client of the lectin chaperone vesicular integral membrane protein, VIP36	1336:1438	We also show that GC-C is the first identified receptor client of the lectin chaperone vesicular integral membrane protein, VIP36.
23269669	0	6	with	interaction	125:135	arg1	protein					170:176	vesicular integral membrane protein 36	142:179	vesicular integral membrane protein 36	142:179	Site-specific N-linked glycosylation of receptor guanylyl cyclase C regulates ligand binding, ligand-mediated activation and interaction with vesicular integral membrane protein 36, VIP36.
23269669	0	6	with	interaction	125:135	arg1	VIP36					182:186	VIP36	182:186	VIP36	182:186	Site-specific N-linked glycosylation of receptor guanylyl cyclase C regulates ligand binding, ligand-mediated activation and interaction with vesicular integral membrane protein 36, VIP36.
23269669	1	7	theme	Guanylyl	189:196	arg1	GC-C					209:212	GC-C	209:212	GC-C	209:212	Guanylyl cyclase C (GC-C) is a multidomain, membrane-associated receptor guanylyl cyclase.
23269669	1	7	theme	Guanylyl	189:196	arg1	C					206:206	Guanylyl cyclase C	189:206	Guanylyl cyclase C (GC-C)	189:213	Guanylyl cyclase C (GC-C) is a multidomain, membrane-associated receptor guanylyl cyclase.
23269669	1	7	theme	Guanylyl	189:196	arg1	multidomain					220:230	a multidomain	218:230	a multidomain	218:230	Guanylyl cyclase C (GC-C) is a multidomain, membrane-associated receptor guanylyl cyclase.
23269669	7	8	theme	integral	1407:1414	arg1	VIP36					1434:1438	VIP36	1434:1438	VIP36	1434:1438	We also show that GC-C is the first identified receptor client of the lectin chaperone vesicular integral membrane protein, VIP36.
23269669	7	8	theme	integral	1407:1414	arg1	protein					1425:1431	the lectin chaperone vesicular integral membrane protein	1376:1431	the lectin chaperone vesicular integral membrane protein	1376:1431	We also show that GC-C is the first identified receptor client of the lectin chaperone vesicular integral membrane protein, VIP36.
23269669	7	9	theme	receptor	1357:1364	arg1	GC-C					1328:1331	GC-C	1328:1331	GC-C	1328:1331	We also show that GC-C is the first identified receptor client of the lectin chaperone vesicular integral membrane protein, VIP36.
23269669	7	9	theme	receptor	1357:1364	arg1	client					1366:1371	the first identified receptor client	1336:1371	the first identified receptor client of the lectin chaperone vesicular integral membrane protein, VIP36	1336:1438	We also show that GC-C is the first identified receptor client of the lectin chaperone vesicular integral membrane protein, VIP36.
23269669	9	10	theme	glycan-mediated	1669:1683	arg1	interactions					1685:1696	glycan-mediated interactions	1669:1696	glycan-mediated interactions	1669:1696	Because glycosylation of proteins is altered in many diseases and in a tissue-dependent manner, the activity and/or glycan-mediated interactions of GC-C may have a crucial role to play in its functions in different cell types.
23269669	0	11	with	activation	110:119	arg1	protein					170:176	vesicular integral membrane protein 36	142:179	vesicular integral membrane protein 36	142:179	Site-specific N-linked glycosylation of receptor guanylyl cyclase C regulates ligand binding, ligand-mediated activation and interaction with vesicular integral membrane protein 36, VIP36.
23269669	0	11	with	activation	110:119	arg1	VIP36					182:186	VIP36	182:186	VIP36	182:186	Site-specific N-linked glycosylation of receptor guanylyl cyclase C regulates ligand binding, ligand-mediated activation and interaction with vesicular integral membrane protein 36, VIP36.
23269669	2	12	theme	gastrointestinal	315:330	arg1	tract					332:336	the gastrointestinal tract	311:336	the gastrointestinal tract	311:336	GC-C is primarily expressed in the gastrointestinal tract, where it mediates fluid-ion homeostasis, intestinal inflammation, and cell proliferation in a cGMP-dependent manner, following activation by its ligands guanylin, uroguanylin, or the heat-stable enterotoxin peptide (ST).
23269669	6	13	theme	each	1124:1127	arg1	mutagenesis					1109:1119	Systematic mutagenesis	1098:1119	Systematic mutagenesis	1098:1119	Systematic mutagenesis of each of the 10 sites of glycosylation in GC-C, either singly or in combination, identified two sites that were critical for ligand binding and two that regulated ST-mediated activation.
23269669	6	14	theme	ST-mediated	1286:1296	arg1	activation					1298:1307	ST-mediated activation	1286:1307	ST-mediated activation	1286:1307	Systematic mutagenesis of each of the 10 sites of glycosylation in GC-C, either singly or in combination, identified two sites that were critical for ligand binding and two that regulated ST-mediated activation.
23269669	5	15	gly	glycosylation	902:914	arg1	GC-C					925:928	human GC-C	919:928	human GC-C	919:928	When glycosylation of human GC-C was prevented, either by pharmacological intervention or by mutation of all of the 10 predicted glycosylation sites, ST binding and surface localization was abolished.
23269669	6	16	gly	glycosylation	1148:1160	arg2	glycosylation					1148:1160	glycosylation	1148:1160	glycosylation	1148:1160	Systematic mutagenesis of each of the 10 sites of glycosylation in GC-C, either singly or in combination, identified two sites that were critical for ligand binding and two that regulated ST-mediated activation.
23269669	6	16	gly	glycosylation	1148:1160	arg2	sites					1139:1143	the 10 sites	1132:1143	the 10 sites of glycosylation in GC-C	1132:1168	Systematic mutagenesis of each of the 10 sites of glycosylation in GC-C, either singly or in combination, identified two sites that were critical for ligand binding and two that regulated ST-mediated activation.
23269669	6	16	gly	glycosylation	1148:1160	arg1	GC-C					1165:1168	GC-C	1165:1168	GC-C	1165:1168	Systematic mutagenesis of each of the 10 sites of glycosylation in GC-C, either singly or in combination, identified two sites that were critical for ligand binding and two that regulated ST-mediated activation.
23269669	0	17	theme	integral	152:159	arg1	protein					170:176	vesicular integral membrane protein 36	142:179	vesicular integral membrane protein 36	142:179	Site-specific N-linked glycosylation of receptor guanylyl cyclase C regulates ligand binding, ligand-mediated activation and interaction with vesicular integral membrane protein 36, VIP36.
23269669	0	17	theme	integral	152:159	arg1	VIP36					182:186	VIP36	182:186	VIP36	182:186	Site-specific N-linked glycosylation of receptor guanylyl cyclase C regulates ligand binding, ligand-mediated activation and interaction with vesicular integral membrane protein 36, VIP36.
23269669	5	18	theme	ST	1047:1048	arg1	binding					1050:1056	ST binding	1047:1056	ST binding	1047:1056	When glycosylation of human GC-C was prevented, either by pharmacological intervention or by mutation of all of the 10 predicted glycosylation sites, ST binding and surface localization was abolished.
23269669	4	19	gly	glycosylated	685:696	arg2	GC-C					677:680	GC-C	677:680	GC-C	677:680	GC-C is glycosylated in the extracellular domain, and differentially glycosylated forms that are resident in the endoplasmic reticulum (130 kDa) and the plasma membrane (145 kDa) bind the ST peptide with equal affinity.
23269669	4	19	gly	glycosylated	685:696	arg1	domain					719:724	the extracellular domain	701:724	the extracellular domain	701:724	GC-C is glycosylated in the extracellular domain, and differentially glycosylated forms that are resident in the endoplasmic reticulum (130 kDa) and the plasma membrane (145 kDa) bind the ST peptide with equal affinity.
23269669	4	19	gly	glycosylated	685:696	arg1	GC-C					677:680	GC-C	677:680	GC-C	677:680	GC-C is glycosylated in the extracellular domain, and differentially glycosylated forms that are resident in the endoplasmic reticulum (130 kDa) and the plasma membrane (145 kDa) bind the ST peptide with equal affinity.
23269669	4	20	theme	equal	881:885	arg1	affinity					887:894	equal affinity	881:894	equal affinity	881:894	GC-C is glycosylated in the extracellular domain, and differentially glycosylated forms that are resident in the endoplasmic reticulum (130 kDa) and the plasma membrane (145 kDa) bind the ST peptide with equal affinity.
23269669	6	21	dep	either	1171:1176	arg1	singly					1178:1183	singly	1178:1183	singly	1178:1183	Systematic mutagenesis of each of the 10 sites of glycosylation in GC-C, either singly or in combination, identified two sites that were critical for ligand binding and two that regulated ST-mediated activation.
23269669	6	22	theme	ligand	1248:1253	arg1	binding					1255:1261	ligand binding	1248:1261	ligand binding	1248:1261	Systematic mutagenesis of each of the 10 sites of glycosylation in GC-C, either singly or in combination, identified two sites that were critical for ligand binding and two that regulated ST-mediated activation.
23269669	5	23	theme	predicted	1016:1024	arg1	sites					1040:1044	the 10 predicted glycosylation sites	1009:1044	the 10 predicted glycosylation sites	1009:1044	When glycosylation of human GC-C was prevented, either by pharmacological intervention or by mutation of all of the 10 predicted glycosylation sites, ST binding and surface localization was abolished.
23269669	7	24	theme	lectin	1380:1385	arg1	VIP36					1434:1438	VIP36	1434:1438	VIP36	1434:1438	We also show that GC-C is the first identified receptor client of the lectin chaperone vesicular integral membrane protein, VIP36.
23269669	7	24	theme	lectin	1380:1385	arg1	protein					1425:1431	the lectin chaperone vesicular integral membrane protein	1376:1431	the lectin chaperone vesicular integral membrane protein	1376:1431	We also show that GC-C is the first identified receptor client of the lectin chaperone vesicular integral membrane protein, VIP36.
23269669	9	25	theme	GC-C	1701:1704	arg1	activity					1653:1660	activity	1653:1660	activity	1653:1660	Because glycosylation of proteins is altered in many diseases and in a tissue-dependent manner, the activity and/or glycan-mediated interactions of GC-C may have a crucial role to play in its functions in different cell types.
23269669	9	26	dep	activity	1653:1660	arg1	the					1649:1651	the	1649:1651	the	1649:1651	Because glycosylation of proteins is altered in many diseases and in a tissue-dependent manner, the activity and/or glycan-mediated interactions of GC-C may have a crucial role to play in its functions in different cell types.
23269669	4	27	from	reticulum	802:810	arg1	resident					774:781	resident	774:781	resident	774:781	GC-C is glycosylated in the extracellular domain, and differentially glycosylated forms that are resident in the endoplasmic reticulum (130 kDa) and the plasma membrane (145 kDa) bind the ST peptide with equal affinity.
23269669	8	28	gly	glycosylation	1480:1492	arg1	sites					1506:1510	the same sites	1497:1510	the same sites that allow GC-C to fold and bind ligand	1497:1550	Interaction with VIP36 is dependent on glycosylation at the same sites that allow GC-C to fold and bind ligand.
23269669	8	28	gly	glycosylation	1480:1492	arg2	sites					1506:1510	the same sites	1497:1510	the same sites that allow GC-C to fold and bind ligand	1497:1550	Interaction with VIP36 is dependent on glycosylation at the same sites that allow GC-C to fold and bind ligand.
23269669	7	29	theme	membrane	1416:1423	arg1	VIP36					1434:1438	VIP36	1434:1438	VIP36	1434:1438	We also show that GC-C is the first identified receptor client of the lectin chaperone vesicular integral membrane protein, VIP36.
23269669	7	29	theme	membrane	1416:1423	arg1	protein					1425:1431	the lectin chaperone vesicular integral membrane protein	1376:1431	the lectin chaperone vesicular integral membrane protein	1376:1431	We also show that GC-C is the first identified receptor client of the lectin chaperone vesicular integral membrane protein, VIP36.
23269669	9	30	theme	crucial	1717:1723	arg1	role					1725:1728	a crucial role	1715:1728	a crucial role	1715:1728	Because glycosylation of proteins is altered in many diseases and in a tissue-dependent manner, the activity and/or glycan-mediated interactions of GC-C may have a crucial role to play in its functions in different cell types.
23269669	4	31	gly	glycosylated	746:757	arg1	forms					759:763	differentially glycosylated forms	731:763	differentially glycosylated forms that are resident in the endoplasmic reticulum (130 kDa) and the plasma membrane (145 kDa)	731:854	GC-C is glycosylated in the extracellular domain, and differentially glycosylated forms that are resident in the endoplasmic reticulum (130 kDa) and the plasma membrane (145 kDa) bind the ST peptide with equal affinity.
23269669	2	32	dep	ligands	484:490	arg1	peptide					546:552	the heat-stable enterotoxin peptide	518:552	the heat-stable enterotoxin peptide (ST)	518:557	GC-C is primarily expressed in the gastrointestinal tract, where it mediates fluid-ion homeostasis, intestinal inflammation, and cell proliferation in a cGMP-dependent manner, following activation by its ligands guanylin, uroguanylin, or the heat-stable enterotoxin peptide (ST).
23269669	2	32	dep	ligands	484:490	arg1	ligands					484:490	its ligands	480:490	its ligands guanylin, uroguanylin, or the heat-stable enterotoxin peptide (ST)	480:557	GC-C is primarily expressed in the gastrointestinal tract, where it mediates fluid-ion homeostasis, intestinal inflammation, and cell proliferation in a cGMP-dependent manner, following activation by its ligands guanylin, uroguanylin, or the heat-stable enterotoxin peptide (ST).
23269669	2	32	dep	ligands	484:490	arg1	uroguanylin					502:512	uroguanylin	502:512	uroguanylin	502:512	GC-C is primarily expressed in the gastrointestinal tract, where it mediates fluid-ion homeostasis, intestinal inflammation, and cell proliferation in a cGMP-dependent manner, following activation by its ligands guanylin, uroguanylin, or the heat-stable enterotoxin peptide (ST).
23269669	2	32	dep	ligands	484:490	arg1	guanylin					492:499	guanylin	492:499	guanylin	492:499	GC-C is primarily expressed in the gastrointestinal tract, where it mediates fluid-ion homeostasis, intestinal inflammation, and cell proliferation in a cGMP-dependent manner, following activation by its ligands guanylin, uroguanylin, or the heat-stable enterotoxin peptide (ST).
23269669	4	33	from	resident	774:781	arg1	kDa					851:853	145 kDa	847:853	145 kDa	847:853	GC-C is glycosylated in the extracellular domain, and differentially glycosylated forms that are resident in the endoplasmic reticulum (130 kDa) and the plasma membrane (145 kDa) bind the ST peptide with equal affinity.
23269669	4	33	from	resident	774:781	arg1	reticulum					802:810	the endoplasmic reticulum	786:810	the endoplasmic reticulum (130 kDa)	786:820	GC-C is glycosylated in the extracellular domain, and differentially glycosylated forms that are resident in the endoplasmic reticulum (130 kDa) and the plasma membrane (145 kDa) bind the ST peptide with equal affinity.
23269669	4	33	from	resident	774:781	arg1	kDa					817:819	130 kDa	813:819	130 kDa	813:819	GC-C is glycosylated in the extracellular domain, and differentially glycosylated forms that are resident in the endoplasmic reticulum (130 kDa) and the plasma membrane (145 kDa) bind the ST peptide with equal affinity.
23269669	4	33	from	resident	774:781	arg1	membrane					837:844	the plasma membrane	826:844	the plasma membrane (145 kDa)	826:854	GC-C is glycosylated in the extracellular domain, and differentially glycosylated forms that are resident in the endoplasmic reticulum (130 kDa) and the plasma membrane (145 kDa) bind the ST peptide with equal affinity.
23269669	2	34	theme	heat-stable	522:532	arg1	enterotoxin					534:544	the heat-stable enterotoxin	518:544	the heat-stable enterotoxin peptide (ST)	518:557	GC-C is primarily expressed in the gastrointestinal tract, where it mediates fluid-ion homeostasis, intestinal inflammation, and cell proliferation in a cGMP-dependent manner, following activation by its ligands guanylin, uroguanylin, or the heat-stable enterotoxin peptide (ST).
23269669	2	35	theme	cell	409:412	arg1	proliferation					414:426	cell proliferation	409:426	cell proliferation	409:426	GC-C is primarily expressed in the gastrointestinal tract, where it mediates fluid-ion homeostasis, intestinal inflammation, and cell proliferation in a cGMP-dependent manner, following activation by its ligands guanylin, uroguanylin, or the heat-stable enterotoxin peptide (ST).
23269669	4	36	from	membrane	837:844	arg1	resident					774:781	resident	774:781	resident	774:781	GC-C is glycosylated in the extracellular domain, and differentially glycosylated forms that are resident in the endoplasmic reticulum (130 kDa) and the plasma membrane (145 kDa) bind the ST peptide with equal affinity.
23269669	4	37	theme	glycosylated	746:757	arg1	forms					759:763	differentially glycosylated forms	731:763	differentially glycosylated forms that are resident in the endoplasmic reticulum (130 kDa) and the plasma membrane (145 kDa)	731:854	GC-C is glycosylated in the extracellular domain, and differentially glycosylated forms that are resident in the endoplasmic reticulum (130 kDa) and the plasma membrane (145 kDa) bind the ST peptide with equal affinity.
23269669	0	38	theme	Site-specific	0:12	arg1	glycosylation					23:35	Site-specific N-linked glycosylation	0:35	Site-specific N-linked glycosylation of receptor guanylyl cyclase C	0:66	Site-specific N-linked glycosylation of receptor guanylyl cyclase C regulates ligand binding, ligand-mediated activation and interaction with vesicular integral membrane protein 36, VIP36.
23269669	5	39	theme	human	919:923	arg1	GC-C					925:928	human GC-C	919:928	human GC-C	919:928	When glycosylation of human GC-C was prevented, either by pharmacological intervention or by mutation of all of the 10 predicted glycosylation sites, ST binding and surface localization was abolished.
23269669	8	40	theme	same	1501:1504	arg1	sites					1506:1510	the same sites	1497:1510	the same sites that allow GC-C to fold and bind ligand	1497:1550	Interaction with VIP36 is dependent on glycosylation at the same sites that allow GC-C to fold and bind ligand.
23269669	2	41	theme	cGMP-dependent	433:446	arg1	manner					448:453	a cGMP-dependent manner	431:453	a cGMP-dependent manner	431:453	GC-C is primarily expressed in the gastrointestinal tract, where it mediates fluid-ion homeostasis, intestinal inflammation, and cell proliferation in a cGMP-dependent manner, following activation by its ligands guanylin, uroguanylin, or the heat-stable enterotoxin peptide (ST).
23269669	4	42	with	peptide	868:874	arg1	affinity					887:894	equal affinity	881:894	equal affinity	881:894	GC-C is glycosylated in the extracellular domain, and differentially glycosylated forms that are resident in the endoplasmic reticulum (130 kDa) and the plasma membrane (145 kDa) bind the ST peptide with equal affinity.
23269669	9	43	theme	different	1758:1766	arg1	types					1773:1777	different cell types	1758:1777	different cell types	1758:1777	Because glycosylation of proteins is altered in many diseases and in a tissue-dependent manner, the activity and/or glycan-mediated interactions of GC-C may have a crucial role to play in its functions in different cell types.
23269669	0	44	theme	receptor	40:47	arg1	C					66:66	receptor guanylyl cyclase C	40:66	receptor guanylyl cyclase C	40:66	Site-specific N-linked glycosylation of receptor guanylyl cyclase C regulates ligand binding, ligand-mediated activation and interaction with vesicular integral membrane protein 36, VIP36.
23269669	0	45	theme	cyclase	58:64	arg1	C					66:66	receptor guanylyl cyclase C	40:66	receptor guanylyl cyclase C	40:66	Site-specific N-linked glycosylation of receptor guanylyl cyclase C regulates ligand binding, ligand-mediated activation and interaction with vesicular integral membrane protein 36, VIP36.
23269669	6	46	theme	Systematic	1098:1107	arg1	mutagenesis					1109:1119	Systematic mutagenesis	1098:1119	Systematic mutagenesis	1098:1119	Systematic mutagenesis of each of the 10 sites of glycosylation in GC-C, either singly or in combination, identified two sites that were critical for ligand binding and two that regulated ST-mediated activation.
23269669	6	47	dep	mutagenesis	1109:1119	arg1	either					1171:1176	either	1171:1176	either	1171:1176	Systematic mutagenesis of each of the 10 sites of glycosylation in GC-C, either singly or in combination, identified two sites that were critical for ligand binding and two that regulated ST-mediated activation.
23269669	6	47	dep	mutagenesis	1109:1119	arg1	combination					1191:1201	combination	1191:1201	combination	1191:1201	Systematic mutagenesis of each of the 10 sites of glycosylation in GC-C, either singly or in combination, identified two sites that were critical for ligand binding and two that regulated ST-mediated activation.
23269669	8	48	with	Interaction	1441:1451	arg1	VIP36					1458:1462	VIP36	1458:1462	VIP36	1458:1462	Interaction with VIP36 is dependent on glycosylation at the same sites that allow GC-C to fold and bind ligand.
23269669	1	49	theme	receptor	253:260	arg1	cyclase					271:277	membrane-associated receptor guanylyl cyclase	233:277	membrane-associated receptor guanylyl cyclase	233:277	Guanylyl cyclase C (GC-C) is a multidomain, membrane-associated receptor guanylyl cyclase.
23269669	1	49	theme	receptor	253:260	arg1	multidomain					220:230	a multidomain	218:230	a multidomain	218:230	Guanylyl cyclase C (GC-C) is a multidomain, membrane-associated receptor guanylyl cyclase.
23269669	5	50	gly	glycosylation	1026:1038	arg2	sites					1040:1044	the 10 predicted glycosylation sites	1009:1044	the 10 predicted glycosylation sites	1009:1044	When glycosylation of human GC-C was prevented, either by pharmacological intervention or by mutation of all of the 10 predicted glycosylation sites, ST binding and surface localization was abolished.
23269669	5	50	gly	glycosylation	1026:1038	arg2	10					1013:1014	10	1013:1014	10	1013:1014	When glycosylation of human GC-C was prevented, either by pharmacological intervention or by mutation of all of the 10 predicted glycosylation sites, ST binding and surface localization was abolished.
23269669	9	51	gly	glycosylation	1561:1573	arg1	manner					1641:1646	a tissue-dependent manner	1622:1646	a tissue-dependent manner	1622:1646	Because glycosylation of proteins is altered in many diseases and in a tissue-dependent manner, the activity and/or glycan-mediated interactions of GC-C may have a crucial role to play in its functions in different cell types.
23269669	9	51	gly	glycosylation	1561:1573	arg1	diseases					1606:1613	many diseases	1601:1613	many diseases	1601:1613	Because glycosylation of proteins is altered in many diseases and in a tissue-dependent manner, the activity and/or glycan-mediated interactions of GC-C may have a crucial role to play in its functions in different cell types.
23269669	9	51	gly	glycosylation	1561:1573	arg1	proteins					1578:1585	proteins	1578:1585	proteins	1578:1585	Because glycosylation of proteins is altered in many diseases and in a tissue-dependent manner, the activity and/or glycan-mediated interactions of GC-C may have a crucial role to play in its functions in different cell types.
23269669	8	52	from	sites	1506:1510	arg1	glycosylation					1480:1492	glycosylation	1480:1492	glycosylation at the same sites that allow GC-C to fold and bind ligand	1480:1550	Interaction with VIP36 is dependent on glycosylation at the same sites that allow GC-C to fold and bind ligand.
23269669	0	53	with	binding	85:91	arg1	protein					170:176	vesicular integral membrane protein 36	142:179	vesicular integral membrane protein 36	142:179	Site-specific N-linked glycosylation of receptor guanylyl cyclase C regulates ligand binding, ligand-mediated activation and interaction with vesicular integral membrane protein 36, VIP36.
23269669	0	53	with	binding	85:91	arg1	VIP36					182:186	VIP36	182:186	VIP36	182:186	Site-specific N-linked glycosylation of receptor guanylyl cyclase C regulates ligand binding, ligand-mediated activation and interaction with vesicular integral membrane protein 36, VIP36.
23269669	9	54	from	functions	1745:1753	arg1	types					1773:1777	different cell types	1758:1777	different cell types	1758:1777	Because glycosylation of proteins is altered in many diseases and in a tissue-dependent manner, the activity and/or glycan-mediated interactions of GC-C may have a crucial role to play in its functions in different cell types.
23269669	0	55	link	N-linked	14:21	arg1	glycosylation					23:35	Site-specific N-linked glycosylation	0:35	Site-specific N-linked glycosylation of receptor guanylyl cyclase C	0:66	Site-specific N-linked glycosylation of receptor guanylyl cyclase C regulates ligand binding, ligand-mediated activation and interaction with vesicular integral membrane protein 36, VIP36.
23269669	7	56	theme	chaperone	1387:1395	arg1	VIP36					1434:1438	VIP36	1434:1438	VIP36	1434:1438	We also show that GC-C is the first identified receptor client of the lectin chaperone vesicular integral membrane protein, VIP36.
23269669	7	56	theme	chaperone	1387:1395	arg1	protein					1425:1431	the lectin chaperone vesicular integral membrane protein	1376:1431	the lectin chaperone vesicular integral membrane protein	1376:1431	We also show that GC-C is the first identified receptor client of the lectin chaperone vesicular integral membrane protein, VIP36.
23269669	7	57	theme	vesicular	1397:1405	arg1	VIP36					1434:1438	VIP36	1434:1438	VIP36	1434:1438	We also show that GC-C is the first identified receptor client of the lectin chaperone vesicular integral membrane protein, VIP36.
23269669	7	57	theme	vesicular	1397:1405	arg1	protein					1425:1431	the lectin chaperone vesicular integral membrane protein	1376:1431	the lectin chaperone vesicular integral membrane protein	1376:1431	We also show that GC-C is the first identified receptor client of the lectin chaperone vesicular integral membrane protein, VIP36.
23269669	4	58	theme	plasma	830:835	arg1	membrane					837:844	the plasma membrane	826:844	the plasma membrane (145 kDa)	826:854	GC-C is glycosylated in the extracellular domain, and differentially glycosylated forms that are resident in the endoplasmic reticulum (130 kDa) and the plasma membrane (145 kDa) bind the ST peptide with equal affinity.
23269669	4	58	theme	plasma	830:835	arg1	kDa					851:853	145 kDa	847:853	145 kDa	847:853	GC-C is glycosylated in the extracellular domain, and differentially glycosylated forms that are resident in the endoplasmic reticulum (130 kDa) and the plasma membrane (145 kDa) bind the ST peptide with equal affinity.
23269669	1	59	theme	cyclase	198:204	arg1	GC-C					209:212	GC-C	209:212	GC-C	209:212	Guanylyl cyclase C (GC-C) is a multidomain, membrane-associated receptor guanylyl cyclase.
23269669	1	59	theme	cyclase	198:204	arg1	C					206:206	Guanylyl cyclase C	189:206	Guanylyl cyclase C (GC-C)	189:213	Guanylyl cyclase C (GC-C) is a multidomain, membrane-associated receptor guanylyl cyclase.
23269669	1	59	theme	cyclase	198:204	arg1	multidomain					220:230	a multidomain	218:230	a multidomain	218:230	Guanylyl cyclase C (GC-C) is a multidomain, membrane-associated receptor guanylyl cyclase.
23269669	9	60	theme	tissue-dependent	1624:1639	arg1	manner					1641:1646	a tissue-dependent manner	1622:1646	a tissue-dependent manner	1622:1646	Because glycosylation of proteins is altered in many diseases and in a tissue-dependent manner, the activity and/or glycan-mediated interactions of GC-C may have a crucial role to play in its functions in different cell types.
23269669	0	61	theme	vesicular	142:150	arg1	protein					170:176	vesicular integral membrane protein 36	142:179	vesicular integral membrane protein 36	142:179	Site-specific N-linked glycosylation of receptor guanylyl cyclase C regulates ligand binding, ligand-mediated activation and interaction with vesicular integral membrane protein 36, VIP36.
23269669	0	61	theme	vesicular	142:150	arg1	VIP36					182:186	VIP36	182:186	VIP36	182:186	Site-specific N-linked glycosylation of receptor guanylyl cyclase C regulates ligand binding, ligand-mediated activation and interaction with vesicular integral membrane protein 36, VIP36.
23269669	7	62	theme	identified	1346:1355	arg1	GC-C					1328:1331	GC-C	1328:1331	GC-C	1328:1331	We also show that GC-C is the first identified receptor client of the lectin chaperone vesicular integral membrane protein, VIP36.
23269669	7	62	theme	identified	1346:1355	arg1	client					1366:1371	the first identified receptor client	1336:1371	the first identified receptor client of the lectin chaperone vesicular integral membrane protein, VIP36	1336:1438	We also show that GC-C is the first identified receptor client of the lectin chaperone vesicular integral membrane protein, VIP36.
23269669	5	63	theme	all	1002:1004	arg1	mutation					990:997	mutation	990:997	mutation of all of the 10 predicted glycosylation sites	990:1044	When glycosylation of human GC-C was prevented, either by pharmacological intervention or by mutation of all of the 10 predicted glycosylation sites, ST binding and surface localization was abolished.
23269669	0	64	theme	membrane	161:168	arg1	protein					170:176	vesicular integral membrane protein 36	142:179	vesicular integral membrane protein 36	142:179	Site-specific N-linked glycosylation of receptor guanylyl cyclase C regulates ligand binding, ligand-mediated activation and interaction with vesicular integral membrane protein 36, VIP36.
23269669	0	64	theme	membrane	161:168	arg1	VIP36					182:186	VIP36	182:186	VIP36	182:186	Site-specific N-linked glycosylation of receptor guanylyl cyclase C regulates ligand binding, ligand-mediated activation and interaction with vesicular integral membrane protein 36, VIP36.
23269669	4	65	theme	ST	865:866	arg1	peptide					868:874	the ST peptide	861:874	the ST peptide with equal affinity	861:894	GC-C is glycosylated in the extracellular domain, and differentially glycosylated forms that are resident in the endoplasmic reticulum (130 kDa) and the plasma membrane (145 kDa) bind the ST peptide with equal affinity.
23269669	4	66	theme	extracellular	705:717	arg1	domain					719:724	the extracellular domain	701:724	the extracellular domain	701:724	GC-C is glycosylated in the extracellular domain, and differentially glycosylated forms that are resident in the endoplasmic reticulum (130 kDa) and the plasma membrane (145 kDa) bind the ST peptide with equal affinity.
23269669	0	67	theme	ligand	78:83	arg1	binding					85:91	ligand binding	78:91	ligand binding	78:91	Site-specific N-linked glycosylation of receptor guanylyl cyclase C regulates ligand binding, ligand-mediated activation and interaction with vesicular integral membrane protein 36, VIP36.
23269669	5	68	theme	glycosylation	1026:1038	arg1	sites					1040:1044	the 10 predicted glycosylation sites	1009:1044	the 10 predicted glycosylation sites	1009:1044	When glycosylation of human GC-C was prevented, either by pharmacological intervention or by mutation of all of the 10 predicted glycosylation sites, ST binding and surface localization was abolished.
23269669	0	69	theme	ligand-mediated	94:108	arg1	activation					110:119	ligand-mediated activation	94:119	ligand-mediated activation	94:119	Site-specific N-linked glycosylation of receptor guanylyl cyclase C regulates ligand binding, ligand-mediated activation and interaction with vesicular integral membrane protein 36, VIP36.
23269669	2	70	theme	enterotoxin	534:544	arg1	ligands					484:490	its ligands	480:490	its ligands guanylin, uroguanylin, or the heat-stable enterotoxin peptide (ST)	480:557	GC-C is primarily expressed in the gastrointestinal tract, where it mediates fluid-ion homeostasis, intestinal inflammation, and cell proliferation in a cGMP-dependent manner, following activation by its ligands guanylin, uroguanylin, or the heat-stable enterotoxin peptide (ST).
23269669	2	70	theme	enterotoxin	534:544	arg1	peptide					546:552	the heat-stable enterotoxin peptide	518:552	the heat-stable enterotoxin peptide (ST)	518:557	GC-C is primarily expressed in the gastrointestinal tract, where it mediates fluid-ion homeostasis, intestinal inflammation, and cell proliferation in a cGMP-dependent manner, following activation by its ligands guanylin, uroguanylin, or the heat-stable enterotoxin peptide (ST).
23269669	6	71	from	sites	1139:1143	arg1	GC-C					1165:1168	GC-C	1165:1168	GC-C	1165:1168	Systematic mutagenesis of each of the 10 sites of glycosylation in GC-C, either singly or in combination, identified two sites that were critical for ligand binding and two that regulated ST-mediated activation.
23269669	5	72	theme	surface	1062:1068	arg1	localization					1070:1081	surface localization	1062:1081	surface localization	1062:1081	When glycosylation of human GC-C was prevented, either by pharmacological intervention or by mutation of all of the 10 predicted glycosylation sites, ST binding and surface localization was abolished.
23269669	0	73	theme	N-linked	14:21	arg1	glycosylation					23:35	Site-specific N-linked glycosylation	0:35	Site-specific N-linked glycosylation of receptor guanylyl cyclase C	0:66	Site-specific N-linked glycosylation of receptor guanylyl cyclase C regulates ligand binding, ligand-mediated activation and interaction with vesicular integral membrane protein 36, VIP36.
23269669	5	74	theme	GC-C	925:928	arg1	glycosylation					902:914	glycosylation	902:914	glycosylation of human GC-C	902:928	When glycosylation of human GC-C was prevented, either by pharmacological intervention or by mutation of all of the 10 predicted glycosylation sites, ST binding and surface localization was abolished.
23269669	2	75	theme	intestinal	380:389	arg1	inflammation					391:402	intestinal inflammation	380:402	intestinal inflammation	380:402	GC-C is primarily expressed in the gastrointestinal tract, where it mediates fluid-ion homeostasis, intestinal inflammation, and cell proliferation in a cGMP-dependent manner, following activation by its ligands guanylin, uroguanylin, or the heat-stable enterotoxin peptide (ST).
23269669	0	76	theme	guanylyl	49:56	arg1	C					66:66	receptor guanylyl cyclase C	40:66	receptor guanylyl cyclase C	40:66	Site-specific N-linked glycosylation of receptor guanylyl cyclase C regulates ligand binding, ligand-mediated activation and interaction with vesicular integral membrane protein 36, VIP36.
23269669	2	77	dep	peptide	546:552	arg1	ST					555:556	ST	555:556	ST	555:556	GC-C is primarily expressed in the gastrointestinal tract, where it mediates fluid-ion homeostasis, intestinal inflammation, and cell proliferation in a cGMP-dependent manner, following activation by its ligands guanylin, uroguanylin, or the heat-stable enterotoxin peptide (ST).
23269669	9	78	theme	cell	1768:1771	arg1	types					1773:1777	different cell types	1758:1777	different cell types	1758:1777	Because glycosylation of proteins is altered in many diseases and in a tissue-dependent manner, the activity and/or glycan-mediated interactions of GC-C may have a crucial role to play in its functions in different cell types.
23269669	0	79	theme	C	66:66	arg1	glycosylation					23:35	Site-specific N-linked glycosylation	0:35	Site-specific N-linked glycosylation of receptor guanylyl cyclase C	0:66	Site-specific N-linked glycosylation of receptor guanylyl cyclase C regulates ligand binding, ligand-mediated activation and interaction with vesicular integral membrane protein 36, VIP36.
23269669	0	80	gly	glycosylation	23:35	arg1	C					66:66	receptor guanylyl cyclase C	40:66	receptor guanylyl cyclase C	40:66	Site-specific N-linked glycosylation of receptor guanylyl cyclase C regulates ligand binding, ligand-mediated activation and interaction with vesicular integral membrane protein 36, VIP36.
23269669	5	81	theme	pharmacological	955:969	arg1	intervention					971:982	pharmacological intervention	955:982	pharmacological intervention	955:982	When glycosylation of human GC-C was prevented, either by pharmacological intervention or by mutation of all of the 10 predicted glycosylation sites, ST binding and surface localization was abolished.
23269669	3	82	theme	deficiency/hyperactive	644:665	arg1	behavior					667:674	deficiency/hyperactive behavior	644:674	deficiency/hyperactive behavior	644:674	GC-C is also expressed in neurons, where it plays a role in satiation and attention deficiency/hyperactive behavior.
23269669	4	83	theme	endoplasmic	790:800	arg1	reticulum					802:810	the endoplasmic reticulum	786:810	the endoplasmic reticulum (130 kDa)	786:820	GC-C is glycosylated in the extracellular domain, and differentially glycosylated forms that are resident in the endoplasmic reticulum (130 kDa) and the plasma membrane (145 kDa) bind the ST peptide with equal affinity.
23269669	4	83	theme	endoplasmic	790:800	arg1	kDa					817:819	130 kDa	813:819	130 kDa	813:819	GC-C is glycosylated in the extracellular domain, and differentially glycosylated forms that are resident in the endoplasmic reticulum (130 kDa) and the plasma membrane (145 kDa) bind the ST peptide with equal affinity.
23269669	3	84	dep	satiation	620:628	arg1	behavior					667:674	deficiency/hyperactive behavior	644:674	deficiency/hyperactive behavior	644:674	GC-C is also expressed in neurons, where it plays a role in satiation and attention deficiency/hyperactive behavior.
23269669	9	85	theme	proteins	1578:1585	arg1	glycosylation					1561:1573	glycosylation	1561:1573	glycosylation of proteins	1561:1585	Because glycosylation of proteins is altered in many diseases and in a tissue-dependent manner, the activity and/or glycan-mediated interactions of GC-C may have a crucial role to play in its functions in different cell types.
23269669	1	86	theme	membrane-associated	233:251	arg1	cyclase					271:277	membrane-associated receptor guanylyl cyclase	233:277	membrane-associated receptor guanylyl cyclase	233:277	Guanylyl cyclase C (GC-C) is a multidomain, membrane-associated receptor guanylyl cyclase.
23269669	1	86	theme	membrane-associated	233:251	arg1	multidomain					220:230	a multidomain	218:230	a multidomain	218:230	Guanylyl cyclase C (GC-C) is a multidomain, membrane-associated receptor guanylyl cyclase.
27865927	1	0	theme	non-excitable	255:267	arg1	cells					280:284	both excitable and non-excitable eukaryotic cells	236:284	both excitable and non-excitable eukaryotic cells	236:284	A major intracellular calcium (Ca2+) uptake pathway in both excitable and non-excitable eukaryotic cells is store-operated Ca2+ entry (SOCE).
27865927	2	1	theme	immune	579:584	arg1	response					586:593	the immune response	575:593	the immune response to platelet aggregation	575:617	SOCE is the process by which endoplasmic reticulum (ER)-stored Ca2+ depletion leads to activation of plasma membrane Ca2+ channels to provide a sustained increase in cytosolic Ca2+ levels that mediate a plethora of physiological processes ranging from the immune response to platelet aggregation.
27865927	8	2	theme	robust	1921:1926	arg1	regulator					1935:1943	a robust ON/OFF regulator	1919:1943	a robust ON/OFF regulator of SOCE	1919:1951	Collectively, our data suggests that N-glycosylation enhances the EFSAM destabilization-coupled oligomerization in response to ER Ca2+ depletion thereby augmenting the role of STIM1 as a robust ON/OFF regulator of SOCE.
27865927	8	2	theme	robust	1921:1926	arg1	role					1902:1905	the role	1898:1905	the role of STIM1	1898:1914	Collectively, our data suggests that N-glycosylation enhances the EFSAM destabilization-coupled oligomerization in response to ER Ca2+ depletion thereby augmenting the role of STIM1 as a robust ON/OFF regulator of SOCE.
27865927	6	3	theme	enhanced	1530:1537	arg1	oligomerization					1539:1553	enhanced oligomerization	1530:1553	enhanced oligomerization	1530:1553	This augmentation occurs through changes in structure localized near the Asn131 and Asn171 sites that together permeate through the protein core and lead to decreased Ca2+ binding affinity, reduced stability and enhanced oligomerization.
27865927	1	4	theme	major	183:187	arg1	Ca2+					212:215	Ca2+	212:215	Ca2+	212:215	A major intracellular calcium (Ca2+) uptake pathway in both excitable and non-excitable eukaryotic cells is store-operated Ca2+ entry (SOCE).
27865927	1	4	theme	major	183:187	arg1	calcium					203:209	major intracellular calcium	183:209	A major intracellular calcium (Ca2+) uptake pathway in both excitable and non-excitable eukaryotic cells	181:284	A major intracellular calcium (Ca2+) uptake pathway in both excitable and non-excitable eukaryotic cells is store-operated Ca2+ entry (SOCE).
27865927	1	5	theme	calcium	203:209	arg1	pathway					225:231	A major intracellular calcium (Ca2+) uptake pathway	181:231	A major intracellular calcium (Ca2+) uptake pathway in both excitable and non-excitable eukaryotic cells	181:284	A major intracellular calcium (Ca2+) uptake pathway in both excitable and non-excitable eukaryotic cells is store-operated Ca2+ entry (SOCE).
27865927	1	5	theme	calcium	203:209	arg1	entry					309:313	store-operated Ca2+ entry	289:313	store-operated Ca2+ entry (SOCE)	289:320	A major intracellular calcium (Ca2+) uptake pathway in both excitable and non-excitable eukaryotic cells is store-operated Ca2+ entry (SOCE).
27865927	3	6	theme	ER	721:722	arg1	Ca2+					731:734	ER stored Ca2+	721:734	ER stored Ca2+ through luminal sensing machinery composed of EF-hand and SAM domains (EFSAM)	721:812	Stromal interaction molecule-1 (STIM1) is the principal regulator of SOCE and responds to changes in ER stored Ca2+ through luminal sensing machinery composed of EF-hand and SAM domains (EFSAM).
27865927	0	7	theme	interaction	119:129	arg1	molecule-1					131:140	stromal interaction molecule-1	111:140	stromal interaction molecule-1 mediated store operated calcium entry	111:178	Structural perturbations induced by Asn131 and Asn171 glycosylation converge within the EFSAM core and enhance stromal interaction molecule-1 mediated store operated calcium entry.
27865927	8	8	from	oligomerization	1830:1844	arg1	response					1849:1856	response	1849:1856	response to ER Ca2+ depletion	1849:1877	Collectively, our data suggests that N-glycosylation enhances the EFSAM destabilization-coupled oligomerization in response to ER Ca2+ depletion thereby augmenting the role of STIM1 as a robust ON/OFF regulator of SOCE.
27865927	1	9	theme	uptake	218:223	arg1	pathway					225:231	A major intracellular calcium (Ca2+) uptake pathway	181:231	A major intracellular calcium (Ca2+) uptake pathway in both excitable and non-excitable eukaryotic cells	181:284	A major intracellular calcium (Ca2+) uptake pathway in both excitable and non-excitable eukaryotic cells is store-operated Ca2+ entry (SOCE).
27865927	1	9	theme	uptake	218:223	arg1	entry					309:313	store-operated Ca2+ entry	289:313	store-operated Ca2+ entry (SOCE)	289:320	A major intracellular calcium (Ca2+) uptake pathway in both excitable and non-excitable eukaryotic cells is store-operated Ca2+ entry (SOCE).
27865927	2	10	from	increase	477:484	arg1	levels					504:509	cytosolic Ca2+ levels	489:509	cytosolic Ca2+ levels that mediate a plethora of physiological processes ranging from the immune response to platelet aggregation	489:617	SOCE is the process by which endoplasmic reticulum (ER)-stored Ca2+ depletion leads to activation of plasma membrane Ca2+ channels to provide a sustained increase in cytosolic Ca2+ levels that mediate a plethora of physiological processes ranging from the immune response to platelet aggregation.
27865927	9	11	theme	Issue	1988:1992	arg1	part					1970:1973	part	1970:1973	part of a Special Issue entitled	1970:2001	This article is part of a Special Issue entitled: ECS Meeting edited by Claus Heizmann, Joachim Krebs and Jacques Haiech.
27865927	3	12	theme	luminal	744:750	arg1	machinery					760:768	luminal sensing machinery	744:768	luminal sensing machinery composed of EF-hand and SAM domains (EFSAM)	744:812	Stromal interaction molecule-1 (STIM1) is the principal regulator of SOCE and responds to changes in ER stored Ca2+ through luminal sensing machinery composed of EF-hand and SAM domains (EFSAM).
27865927	0	13	theme	operated	157:164	arg1	entry					174:178	store operated calcium entry	151:178	store operated calcium entry	151:178	Structural perturbations induced by Asn131 and Asn171 glycosylation converge within the EFSAM core and enhance stromal interaction molecule-1 mediated store operated calcium entry.
27865927	8	14	theme	EFSAM	1800:1804	arg1	oligomerization					1830:1844	the EFSAM destabilization-coupled oligomerization	1796:1844	the EFSAM destabilization-coupled oligomerization in response to ER Ca2+ depletion	1796:1877	Collectively, our data suggests that N-glycosylation enhances the EFSAM destabilization-coupled oligomerization in response to ER Ca2+ depletion thereby augmenting the role of STIM1 as a robust ON/OFF regulator of SOCE.
27865927	2	15	theme	processes	552:560	arg1	plethora					526:533	a plethora	524:533	a plethora of physiological processes ranging from the immune response to platelet aggregation	524:617	SOCE is the process by which endoplasmic reticulum (ER)-stored Ca2+ depletion leads to activation of plasma membrane Ca2+ channels to provide a sustained increase in cytosolic Ca2+ levels that mediate a plethora of physiological processes ranging from the immune response to platelet aggregation.
27865927	9	16	dep	Claus	2026:2030	arg1	Joachim					2042:2048	Joachim	2042:2048	Joachim	2042:2048	This article is part of a Special Issue entitled: ECS Meeting edited by Claus Heizmann, Joachim Krebs and Jacques Haiech.
27865927	9	16	dep	Claus	2026:2030	arg1	Haiech					2068:2073	Haiech	2068:2073	Haiech	2068:2073	This article is part of a Special Issue entitled: ECS Meeting edited by Claus Heizmann, Joachim Krebs and Jacques Haiech.
27865927	5	17	theme	site-specific	1008:1020	arg1	approach					1031:1038	a site-specific chemical approach	1006:1038	a site-specific chemical approach to covalently linking glucose to EFSAM	1006:1077	By establishing a site-specific chemical approach to covalently linking glucose to EFSAM and examining α-helicity, thermal stability, three dimensional atomic-resolution structure, Ca2+ binding affinity and oligomerization, we show that N-glycosylation of the EFSAM domain enhances the properties that promote STIM1 activation.
27865927	3	18	theme	Stromal	620:626	arg1	regulator					676:684	the principal regulator	662:684	the principal regulator of SOCE	662:692	Stromal interaction molecule-1 (STIM1) is the principal regulator of SOCE and responds to changes in ER stored Ca2+ through luminal sensing machinery composed of EF-hand and SAM domains (EFSAM).
27865927	3	18	theme	Stromal	620:626	arg1	STIM1					652:656	STIM1	652:656	STIM1	652:656	Stromal interaction molecule-1 (STIM1) is the principal regulator of SOCE and responds to changes in ER stored Ca2+ through luminal sensing machinery composed of EF-hand and SAM domains (EFSAM).
27865927	3	18	theme	Stromal	620:626	arg1	molecule-1					640:649	Stromal interaction molecule-1	620:649	Stromal interaction molecule-1 (STIM1)	620:657	Stromal interaction molecule-1 (STIM1) is the principal regulator of SOCE and responds to changes in ER stored Ca2+ through luminal sensing machinery composed of EF-hand and SAM domains (EFSAM).
27865927	7	19	theme	HEK293	1593:1598	arg1	cells					1600:1604	HEK293 cells	1593:1604	HEK293 cells co-expressing Orai1 and STIM1	1593:1634	Congruently, Ca2+ influx via SOCE in HEK293 cells co-expressing Orai1 and STIM1 was diminished when N-glycosylation was blocked by introducing Asn131Gln and Asn171Gln mutations.
27865927	4	20	from	role	909:912	arg1	mechanism					959:967	the Ca2+ sensing mechanism	942:967	the Ca2+ sensing mechanism of STIM1	942:976	The EFSAM domain can undergo N-glycosylation at Asn131 and Asn171 sites; however, the precise role of EFSAM N-glycosylation in the Ca2+ sensing mechanism of STIM1 is unclear.
27865927	2	21	theme	sustained	467:475	arg1	increase					477:484	a sustained increase	465:484	a sustained increase in cytosolic Ca2+ levels that mediate a plethora of physiological processes ranging from the immune response to platelet aggregation	465:617	SOCE is the process by which endoplasmic reticulum (ER)-stored Ca2+ depletion leads to activation of plasma membrane Ca2+ channels to provide a sustained increase in cytosolic Ca2+ levels that mediate a plethora of physiological processes ranging from the immune response to platelet aggregation.
27865927	4	22	dep	Asn131	863:868	arg1	sites					881:885	sites	881:885	sites	881:885	The EFSAM domain can undergo N-glycosylation at Asn131 and Asn171 sites; however, the precise role of EFSAM N-glycosylation in the Ca2+ sensing mechanism of STIM1 is unclear.
27865927	8	23	theme	ER	1861:1862	arg1	depletion					1869:1877	ER Ca2+ depletion	1861:1877	ER Ca2+ depletion	1861:1877	Collectively, our data suggests that N-glycosylation enhances the EFSAM destabilization-coupled oligomerization in response to ER Ca2+ depletion thereby augmenting the role of STIM1 as a robust ON/OFF regulator of SOCE.
27865927	5	24	theme	EFSAM	1250:1254	arg1	domain					1256:1261	the EFSAM domain	1246:1261	the EFSAM domain	1246:1261	By establishing a site-specific chemical approach to covalently linking glucose to EFSAM and examining α-helicity, thermal stability, three dimensional atomic-resolution structure, Ca2+ binding affinity and oligomerization, we show that N-glycosylation of the EFSAM domain enhances the properties that promote STIM1 activation.
27865927	6	25	from	changes	1351:1357	arg1	structure					1362:1370	structure	1362:1370	structure localized near the Asn131 and Asn171 sites that together permeate through the protein core and lead to decreased Ca2+ binding affinity, reduced stability and enhanced oligomerization	1362:1553	This augmentation occurs through changes in structure localized near the Asn131 and Asn171 sites that together permeate through the protein core and lead to decreased Ca2+ binding affinity, reduced stability and enhanced oligomerization.
27865927	4	26	theme	EFSAM	917:921	arg1	N-glycosylation					923:937	EFSAM N-glycosylation	917:937	EFSAM N-glycosylation	917:937	The EFSAM domain can undergo N-glycosylation at Asn131 and Asn171 sites; however, the precise role of EFSAM N-glycosylation in the Ca2+ sensing mechanism of STIM1 is unclear.
27865927	2	27	theme	-stored	378:384	arg1	depletion					391:399	endoplasmic reticulum (ER)-stored Ca2+ depletion	352:399	endoplasmic reticulum (ER)-stored Ca2+ depletion	352:399	SOCE is the process by which endoplasmic reticulum (ER)-stored Ca2+ depletion leads to activation of plasma membrane Ca2+ channels to provide a sustained increase in cytosolic Ca2+ levels that mediate a plethora of physiological processes ranging from the immune response to platelet aggregation.
27865927	2	28	theme	membrane	431:438	arg1	channels					445:452	plasma membrane Ca2+ channels	424:452	plasma membrane Ca2+ channels	424:452	SOCE is the process by which endoplasmic reticulum (ER)-stored Ca2+ depletion leads to activation of plasma membrane Ca2+ channels to provide a sustained increase in cytosolic Ca2+ levels that mediate a plethora of physiological processes ranging from the immune response to platelet aggregation.
27865927	0	29	theme	Structural	0:9	arg1	perturbations					11:23	Structural perturbations	0:23	Structural perturbations induced by Asn131 and Asn171 glycosylation	0:66	Structural perturbations induced by Asn131 and Asn171 glycosylation converge within the EFSAM core and enhance stromal interaction molecule-1 mediated store operated calcium entry.
27865927	5	30	theme	atomic-resolution	1142:1158	arg1	structure					1160:1168	three dimensional atomic-resolution structure	1124:1168	three dimensional atomic-resolution structure	1124:1168	By establishing a site-specific chemical approach to covalently linking glucose to EFSAM and examining α-helicity, thermal stability, three dimensional atomic-resolution structure, Ca2+ binding affinity and oligomerization, we show that N-glycosylation of the EFSAM domain enhances the properties that promote STIM1 activation.
27865927	5	30	theme	atomic-resolution	1142:1158	arg1	oligomerization					1197:1211	oligomerization	1197:1211	oligomerization	1197:1211	By establishing a site-specific chemical approach to covalently linking glucose to EFSAM and examining α-helicity, thermal stability, three dimensional atomic-resolution structure, Ca2+ binding affinity and oligomerization, we show that N-glycosylation of the EFSAM domain enhances the properties that promote STIM1 activation.
27865927	5	30	theme	atomic-resolution	1142:1158	arg1	affinity					1184:1191	Ca2+ binding affinity	1171:1191	Ca2+ binding affinity	1171:1191	By establishing a site-specific chemical approach to covalently linking glucose to EFSAM and examining α-helicity, thermal stability, three dimensional atomic-resolution structure, Ca2+ binding affinity and oligomerization, we show that N-glycosylation of the EFSAM domain enhances the properties that promote STIM1 activation.
27865927	5	30	theme	atomic-resolution	1142:1158	arg1	α-helicity					1093:1102	α-helicity	1093:1102	α-helicity	1093:1102	By establishing a site-specific chemical approach to covalently linking glucose to EFSAM and examining α-helicity, thermal stability, three dimensional atomic-resolution structure, Ca2+ binding affinity and oligomerization, we show that N-glycosylation of the EFSAM domain enhances the properties that promote STIM1 activation.
27865927	1	31	theme	Ca2+	304:307	arg1	SOCE					316:319	SOCE	316:319	SOCE	316:319	A major intracellular calcium (Ca2+) uptake pathway in both excitable and non-excitable eukaryotic cells is store-operated Ca2+ entry (SOCE).
27865927	1	31	theme	Ca2+	304:307	arg1	pathway					225:231	A major intracellular calcium (Ca2+) uptake pathway	181:231	A major intracellular calcium (Ca2+) uptake pathway in both excitable and non-excitable eukaryotic cells	181:284	A major intracellular calcium (Ca2+) uptake pathway in both excitable and non-excitable eukaryotic cells is store-operated Ca2+ entry (SOCE).
27865927	1	31	theme	Ca2+	304:307	arg1	entry					309:313	store-operated Ca2+ entry	289:313	store-operated Ca2+ entry (SOCE)	289:320	A major intracellular calcium (Ca2+) uptake pathway in both excitable and non-excitable eukaryotic cells is store-operated Ca2+ entry (SOCE).
27865927	7	32	from	influx	1574:1579	arg1	cells					1600:1604	HEK293 cells	1593:1604	HEK293 cells co-expressing Orai1 and STIM1	1593:1634	Congruently, Ca2+ influx via SOCE in HEK293 cells co-expressing Orai1 and STIM1 was diminished when N-glycosylation was blocked by introducing Asn131Gln and Asn171Gln mutations.
27865927	4	33	theme	STIM1	972:976	arg1	mechanism					959:967	the Ca2+ sensing mechanism	942:967	the Ca2+ sensing mechanism of STIM1	942:976	The EFSAM domain can undergo N-glycosylation at Asn131 and Asn171 sites; however, the precise role of EFSAM N-glycosylation in the Ca2+ sensing mechanism of STIM1 is unclear.
27865927	0	34	theme	Asn171	47:52	arg1	glycosylation					54:66	Asn171 glycosylation	47:66	Asn171 glycosylation	47:66	Structural perturbations induced by Asn131 and Asn171 glycosylation converge within the EFSAM core and enhance stromal interaction molecule-1 mediated store operated calcium entry.
27865927	5	35	gly	N-glycosylation	1227:1241	arg1	domain					1256:1261	the EFSAM domain	1246:1261	the EFSAM domain	1246:1261	By establishing a site-specific chemical approach to covalently linking glucose to EFSAM and examining α-helicity, thermal stability, three dimensional atomic-resolution structure, Ca2+ binding affinity and oligomerization, we show that N-glycosylation of the EFSAM domain enhances the properties that promote STIM1 activation.
27865927	6	36	theme	Ca2+	1485:1488	arg1	affinity					1498:1505	decreased Ca2+ binding affinity	1475:1505	decreased Ca2+ binding affinity	1475:1505	This augmentation occurs through changes in structure localized near the Asn131 and Asn171 sites that together permeate through the protein core and lead to decreased Ca2+ binding affinity, reduced stability and enhanced oligomerization.
27865927	2	37	theme	reticulum	364:372	arg1	depletion					391:399	endoplasmic reticulum (ER)-stored Ca2+ depletion	352:399	endoplasmic reticulum (ER)-stored Ca2+ depletion	352:399	SOCE is the process by which endoplasmic reticulum (ER)-stored Ca2+ depletion leads to activation of plasma membrane Ca2+ channels to provide a sustained increase in cytosolic Ca2+ levels that mediate a plethora of physiological processes ranging from the immune response to platelet aggregation.
27865927	2	38	theme	channels	445:452	arg1	activation					410:419	activation	410:419	activation of plasma membrane Ca2+ channels	410:452	SOCE is the process by which endoplasmic reticulum (ER)-stored Ca2+ depletion leads to activation of plasma membrane Ca2+ channels to provide a sustained increase in cytosolic Ca2+ levels that mediate a plethora of physiological processes ranging from the immune response to platelet aggregation.
27865927	4	39	theme	Ca2+	946:949	arg1	mechanism					959:967	the Ca2+ sensing mechanism	942:967	the Ca2+ sensing mechanism of STIM1	942:976	The EFSAM domain can undergo N-glycosylation at Asn131 and Asn171 sites; however, the precise role of EFSAM N-glycosylation in the Ca2+ sensing mechanism of STIM1 is unclear.
27865927	8	40	theme	STIM1	1910:1914	arg1	regulator					1935:1943	a robust ON/OFF regulator	1919:1943	a robust ON/OFF regulator of SOCE	1919:1951	Collectively, our data suggests that N-glycosylation enhances the EFSAM destabilization-coupled oligomerization in response to ER Ca2+ depletion thereby augmenting the role of STIM1 as a robust ON/OFF regulator of SOCE.
27865927	8	40	theme	STIM1	1910:1914	arg1	role					1902:1905	the role	1898:1905	the role of STIM1	1898:1914	Collectively, our data suggests that N-glycosylation enhances the EFSAM destabilization-coupled oligomerization in response to ER Ca2+ depletion thereby augmenting the role of STIM1 as a robust ON/OFF regulator of SOCE.
27865927	5	41	theme	binding	1176:1182	arg1	structure					1160:1168	three dimensional atomic-resolution structure	1124:1168	three dimensional atomic-resolution structure	1124:1168	By establishing a site-specific chemical approach to covalently linking glucose to EFSAM and examining α-helicity, thermal stability, three dimensional atomic-resolution structure, Ca2+ binding affinity and oligomerization, we show that N-glycosylation of the EFSAM domain enhances the properties that promote STIM1 activation.
27865927	5	41	theme	binding	1176:1182	arg1	affinity					1184:1191	Ca2+ binding affinity	1171:1191	Ca2+ binding affinity	1171:1191	By establishing a site-specific chemical approach to covalently linking glucose to EFSAM and examining α-helicity, thermal stability, three dimensional atomic-resolution structure, Ca2+ binding affinity and oligomerization, we show that N-glycosylation of the EFSAM domain enhances the properties that promote STIM1 activation.
27865927	6	42	theme	protein	1450:1456	arg1	core					1458:1461	the protein core	1446:1461	the protein core	1446:1461	This augmentation occurs through changes in structure localized near the Asn131 and Asn171 sites that together permeate through the protein core and lead to decreased Ca2+ binding affinity, reduced stability and enhanced oligomerization.
27865927	1	43	theme	eukaryotic	269:278	arg1	cells					280:284	both excitable and non-excitable eukaryotic cells	236:284	both excitable and non-excitable eukaryotic cells	236:284	A major intracellular calcium (Ca2+) uptake pathway in both excitable and non-excitable eukaryotic cells is store-operated Ca2+ entry (SOCE).
27865927	8	44	theme	ON/OFF	1928:1933	arg1	regulator					1935:1943	a robust ON/OFF regulator	1919:1943	a robust ON/OFF regulator of SOCE	1919:1951	Collectively, our data suggests that N-glycosylation enhances the EFSAM destabilization-coupled oligomerization in response to ER Ca2+ depletion thereby augmenting the role of STIM1 as a robust ON/OFF regulator of SOCE.
27865927	8	44	theme	ON/OFF	1928:1933	arg1	role					1902:1905	the role	1898:1905	the role of STIM1	1898:1914	Collectively, our data suggests that N-glycosylation enhances the EFSAM destabilization-coupled oligomerization in response to ER Ca2+ depletion thereby augmenting the role of STIM1 as a robust ON/OFF regulator of SOCE.
27865927	1	45	theme	intracellular	189:201	arg1	Ca2+					212:215	Ca2+	212:215	Ca2+	212:215	A major intracellular calcium (Ca2+) uptake pathway in both excitable and non-excitable eukaryotic cells is store-operated Ca2+ entry (SOCE).
27865927	1	45	theme	intracellular	189:201	arg1	calcium					203:209	major intracellular calcium	183:209	A major intracellular calcium (Ca2+) uptake pathway in both excitable and non-excitable eukaryotic cells	181:284	A major intracellular calcium (Ca2+) uptake pathway in both excitable and non-excitable eukaryotic cells is store-operated Ca2+ entry (SOCE).
27865927	4	46	gly	N-glycosylation	844:858	arg1	Asn171					874:879	Asn171	874:879	Asn171	874:879	The EFSAM domain can undergo N-glycosylation at Asn131 and Asn171 sites; however, the precise role of EFSAM N-glycosylation in the Ca2+ sensing mechanism of STIM1 is unclear.
27865927	4	46	gly	N-glycosylation	844:858	arg1	Asn131					863:868	Asn131	863:868	Asn131	863:868	The EFSAM domain can undergo N-glycosylation at Asn131 and Asn171 sites; however, the precise role of EFSAM N-glycosylation in the Ca2+ sensing mechanism of STIM1 is unclear.
27865927	4	46	gly	N-glycosylation	844:858	arg1	domain					825:830	The EFSAM domain	815:830	The EFSAM domain	815:830	The EFSAM domain can undergo N-glycosylation at Asn131 and Asn171 sites; however, the precise role of EFSAM N-glycosylation in the Ca2+ sensing mechanism of STIM1 is unclear.
27865927	2	47	theme	platelet	598:605	arg1	aggregation					607:617	platelet aggregation	598:617	platelet aggregation	598:617	SOCE is the process by which endoplasmic reticulum (ER)-stored Ca2+ depletion leads to activation of plasma membrane Ca2+ channels to provide a sustained increase in cytosolic Ca2+ levels that mediate a plethora of physiological processes ranging from the immune response to platelet aggregation.
27865927	3	48	from	changes	710:716	arg1	Ca2+					731:734	ER stored Ca2+	721:734	ER stored Ca2+ through luminal sensing machinery composed of EF-hand and SAM domains (EFSAM)	721:812	Stromal interaction molecule-1 (STIM1) is the principal regulator of SOCE and responds to changes in ER stored Ca2+ through luminal sensing machinery composed of EF-hand and SAM domains (EFSAM).
27865927	6	49	theme	reduced	1508:1514	arg1	stability					1516:1524	reduced stability	1508:1524	reduced stability	1508:1524	This augmentation occurs through changes in structure localized near the Asn131 and Asn171 sites that together permeate through the protein core and lead to decreased Ca2+ binding affinity, reduced stability and enhanced oligomerization.
27865927	3	50	theme	stored	724:729	arg1	Ca2+					731:734	ER stored Ca2+	721:734	ER stored Ca2+ through luminal sensing machinery composed of EF-hand and SAM domains (EFSAM)	721:812	Stromal interaction molecule-1 (STIM1) is the principal regulator of SOCE and responds to changes in ER stored Ca2+ through luminal sensing machinery composed of EF-hand and SAM domains (EFSAM).
27865927	0	51	theme	store	151:155	arg1	entry					174:178	store operated calcium entry	151:178	store operated calcium entry	151:178	Structural perturbations induced by Asn131 and Asn171 glycosylation converge within the EFSAM core and enhance stromal interaction molecule-1 mediated store operated calcium entry.
27865927	9	52	theme	Special	1980:1986	arg1	Issue					1988:1992	a Special Issue	1978:1992	a Special Issue entitled	1978:2001	This article is part of a Special Issue entitled: ECS Meeting edited by Claus Heizmann, Joachim Krebs and Jacques Haiech.
27865927	0	53	theme	calcium	166:172	arg1	entry					174:178	store operated calcium entry	151:178	store operated calcium entry	151:178	Structural perturbations induced by Asn131 and Asn171 glycosylation converge within the EFSAM core and enhance stromal interaction molecule-1 mediated store operated calcium entry.
27865927	5	54	theme	linking	1054:1060	arg1	glucose					1062:1068	covalently linking glucose	1043:1068	covalently linking glucose	1043:1068	By establishing a site-specific chemical approach to covalently linking glucose to EFSAM and examining α-helicity, thermal stability, three dimensional atomic-resolution structure, Ca2+ binding affinity and oligomerization, we show that N-glycosylation of the EFSAM domain enhances the properties that promote STIM1 activation.
27865927	3	55	theme	principal	666:674	arg1	regulator					676:684	the principal regulator	662:684	the principal regulator of SOCE	662:692	Stromal interaction molecule-1 (STIM1) is the principal regulator of SOCE and responds to changes in ER stored Ca2+ through luminal sensing machinery composed of EF-hand and SAM domains (EFSAM).
27865927	3	55	theme	principal	666:674	arg1	molecule-1					640:649	Stromal interaction molecule-1	620:649	Stromal interaction molecule-1 (STIM1)	620:657	Stromal interaction molecule-1 (STIM1) is the principal regulator of SOCE and responds to changes in ER stored Ca2+ through luminal sensing machinery composed of EF-hand and SAM domains (EFSAM).
27865927	5	56	theme	domain	1256:1261	arg1	N-glycosylation					1227:1241	N-glycosylation	1227:1241	N-glycosylation of the EFSAM domain	1227:1261	By establishing a site-specific chemical approach to covalently linking glucose to EFSAM and examining α-helicity, thermal stability, three dimensional atomic-resolution structure, Ca2+ binding affinity and oligomerization, we show that N-glycosylation of the EFSAM domain enhances the properties that promote STIM1 activation.
27865927	3	57	theme	sensing	752:758	arg1	machinery					760:768	luminal sensing machinery	744:768	luminal sensing machinery composed of EF-hand and SAM domains (EFSAM)	744:812	Stromal interaction molecule-1 (STIM1) is the principal regulator of SOCE and responds to changes in ER stored Ca2+ through luminal sensing machinery composed of EF-hand and SAM domains (EFSAM).
27865927	1	58	from	pathway	225:231	arg1	cells					280:284	both excitable and non-excitable eukaryotic cells	236:284	both excitable and non-excitable eukaryotic cells	236:284	A major intracellular calcium (Ca2+) uptake pathway in both excitable and non-excitable eukaryotic cells is store-operated Ca2+ entry (SOCE).
27865927	2	59	theme	physiological	538:550	arg1	processes					552:560	physiological processes	538:560	physiological processes ranging from the immune response to platelet aggregation	538:617	SOCE is the process by which endoplasmic reticulum (ER)-stored Ca2+ depletion leads to activation of plasma membrane Ca2+ channels to provide a sustained increase in cytosolic Ca2+ levels that mediate a plethora of physiological processes ranging from the immune response to platelet aggregation.
27865927	3	60	theme	SAM	794:796	arg1	EFSAM					807:811	EFSAM	807:811	EFSAM	807:811	Stromal interaction molecule-1 (STIM1) is the principal regulator of SOCE and responds to changes in ER stored Ca2+ through luminal sensing machinery composed of EF-hand and SAM domains (EFSAM).
27865927	3	60	theme	SAM	794:796	arg1	domains					798:804	EF-hand and SAM domains	782:804	EF-hand and SAM domains (EFSAM)	782:812	Stromal interaction molecule-1 (STIM1) is the principal regulator of SOCE and responds to changes in ER stored Ca2+ through luminal sensing machinery composed of EF-hand and SAM domains (EFSAM).
27865927	6	61	theme	Asn131	1391:1396	arg1	sites					1409:1413	the Asn131 and Asn171 sites	1387:1413	sites	1409:1413	This augmentation occurs through changes in structure localized near the Asn131 and Asn171 sites that together permeate through the protein core and lead to decreased Ca2+ binding affinity, reduced stability and enhanced oligomerization.
27865927	5	62	theme	chemical	1022:1029	arg1	approach					1031:1038	a site-specific chemical approach	1006:1038	a site-specific chemical approach to covalently linking glucose to EFSAM	1006:1077	By establishing a site-specific chemical approach to covalently linking glucose to EFSAM and examining α-helicity, thermal stability, three dimensional atomic-resolution structure, Ca2+ binding affinity and oligomerization, we show that N-glycosylation of the EFSAM domain enhances the properties that promote STIM1 activation.
27865927	8	63	theme	destabilization-coupled	1806:1828	arg1	oligomerization					1830:1844	the EFSAM destabilization-coupled oligomerization	1796:1844	the EFSAM destabilization-coupled oligomerization in response to ER Ca2+ depletion	1796:1877	Collectively, our data suggests that N-glycosylation enhances the EFSAM destabilization-coupled oligomerization in response to ER Ca2+ depletion thereby augmenting the role of STIM1 as a robust ON/OFF regulator of SOCE.
27865927	9	64	dep	Joachim	2042:2048	arg1	Krebs					2050:2054	Krebs	2050:2054	Krebs	2050:2054	This article is part of a Special Issue entitled: ECS Meeting edited by Claus Heizmann, Joachim Krebs and Jacques Haiech.
27865927	4	65	theme	N-glycosylation	923:937	arg1	unclear					981:987	unclear	981:987	unclear	981:987	The EFSAM domain can undergo N-glycosylation at Asn131 and Asn171 sites; however, the precise role of EFSAM N-glycosylation in the Ca2+ sensing mechanism of STIM1 is unclear.
27865927	4	65	theme	N-glycosylation	923:937	arg1	role					909:912	the precise role	897:912	the precise role of EFSAM N-glycosylation in the Ca2+ sensing mechanism of STIM1	897:976	The EFSAM domain can undergo N-glycosylation at Asn131 and Asn171 sites; however, the precise role of EFSAM N-glycosylation in the Ca2+ sensing mechanism of STIM1 is unclear.
27865927	3	66	theme	EF-hand	782:788	arg1	EFSAM					807:811	EFSAM	807:811	EFSAM	807:811	Stromal interaction molecule-1 (STIM1) is the principal regulator of SOCE and responds to changes in ER stored Ca2+ through luminal sensing machinery composed of EF-hand and SAM domains (EFSAM).
27865927	3	66	theme	EF-hand	782:788	arg1	domains					798:804	EF-hand and SAM domains	782:804	EF-hand and SAM domains (EFSAM)	782:812	Stromal interaction molecule-1 (STIM1) is the principal regulator of SOCE and responds to changes in ER stored Ca2+ through luminal sensing machinery composed of EF-hand and SAM domains (EFSAM).
27865927	0	67	theme	EFSAM	88:92	arg1	core					94:97	the EFSAM core	84:97	the EFSAM core	84:97	Structural perturbations induced by Asn131 and Asn171 glycosylation converge within the EFSAM core and enhance stromal interaction molecule-1 mediated store operated calcium entry.
27865927	7	68	theme	Ca2+	1569:1572	arg1	influx					1574:1579	Ca2+ influx	1569:1579	Ca2+ influx via SOCE in HEK293 cells co-expressing Orai1 and STIM1	1569:1634	Congruently, Ca2+ influx via SOCE in HEK293 cells co-expressing Orai1 and STIM1 was diminished when N-glycosylation was blocked by introducing Asn131Gln and Asn171Gln mutations.
27865927	8	69	theme	SOCE	1948:1951	arg1	regulator					1935:1943	a robust ON/OFF regulator	1919:1943	a robust ON/OFF regulator of SOCE	1919:1951	Collectively, our data suggests that N-glycosylation enhances the EFSAM destabilization-coupled oligomerization in response to ER Ca2+ depletion thereby augmenting the role of STIM1 as a robust ON/OFF regulator of SOCE.
27865927	8	69	theme	SOCE	1948:1951	arg1	role					1902:1905	the role	1898:1905	the role of STIM1	1898:1914	Collectively, our data suggests that N-glycosylation enhances the EFSAM destabilization-coupled oligomerization in response to ER Ca2+ depletion thereby augmenting the role of STIM1 as a robust ON/OFF regulator of SOCE.
27865927	5	70	theme	thermal	1105:1111	arg1	α-helicity					1093:1102	α-helicity	1093:1102	α-helicity	1093:1102	By establishing a site-specific chemical approach to covalently linking glucose to EFSAM and examining α-helicity, thermal stability, three dimensional atomic-resolution structure, Ca2+ binding affinity and oligomerization, we show that N-glycosylation of the EFSAM domain enhances the properties that promote STIM1 activation.
27865927	5	70	theme	thermal	1105:1111	arg1	stability					1113:1121	thermal stability	1105:1121	thermal stability	1105:1121	By establishing a site-specific chemical approach to covalently linking glucose to EFSAM and examining α-helicity, thermal stability, three dimensional atomic-resolution structure, Ca2+ binding affinity and oligomerization, we show that N-glycosylation of the EFSAM domain enhances the properties that promote STIM1 activation.
27865927	4	71	gly	N-glycosylation	923:937	arg1	STIM1					972:976	STIM1	972:976	STIM1	972:976	The EFSAM domain can undergo N-glycosylation at Asn131 and Asn171 sites; however, the precise role of EFSAM N-glycosylation in the Ca2+ sensing mechanism of STIM1 is unclear.
27865927	4	71	gly	N-glycosylation	923:937	arg1	Ca2+					946:949	the Ca2+ sensing mechanism	942:967	the Ca2+ sensing mechanism of STIM1	942:976	The EFSAM domain can undergo N-glycosylation at Asn131 and Asn171 sites; however, the precise role of EFSAM N-glycosylation in the Ca2+ sensing mechanism of STIM1 is unclear.
27865927	4	72	theme	precise	901:907	arg1	unclear					981:987	unclear	981:987	unclear	981:987	The EFSAM domain can undergo N-glycosylation at Asn131 and Asn171 sites; however, the precise role of EFSAM N-glycosylation in the Ca2+ sensing mechanism of STIM1 is unclear.
27865927	4	72	theme	precise	901:907	arg1	role					909:912	the precise role	897:912	the precise role of EFSAM N-glycosylation in the Ca2+ sensing mechanism of STIM1	897:976	The EFSAM domain can undergo N-glycosylation at Asn131 and Asn171 sites; however, the precise role of EFSAM N-glycosylation in the Ca2+ sensing mechanism of STIM1 is unclear.
27865927	0	73	theme	stromal	111:117	arg1	molecule-1					131:140	stromal interaction molecule-1	111:140	stromal interaction molecule-1 mediated store operated calcium entry	111:178	Structural perturbations induced by Asn131 and Asn171 glycosylation converge within the EFSAM core and enhance stromal interaction molecule-1 mediated store operated calcium entry.
27865927	8	74	theme	Ca2+	1864:1867	arg1	depletion					1869:1877	ER Ca2+ depletion	1861:1877	ER Ca2+ depletion	1861:1877	Collectively, our data suggests that N-glycosylation enhances the EFSAM destabilization-coupled oligomerization in response to ER Ca2+ depletion thereby augmenting the role of STIM1 as a robust ON/OFF regulator of SOCE.
27865927	7	75	theme	Asn171Gln	1713:1721	arg1	mutations					1723:1731	Asn131Gln and Asn171Gln mutations	1699:1731	Asn131Gln and Asn171Gln mutations	1699:1731	Congruently, Ca2+ influx via SOCE in HEK293 cells co-expressing Orai1 and STIM1 was diminished when N-glycosylation was blocked by introducing Asn131Gln and Asn171Gln mutations.
27865927	2	76	theme	cytosolic	489:497	arg1	levels					504:509	cytosolic Ca2+ levels	489:509	cytosolic Ca2+ levels that mediate a plethora of physiological processes ranging from the immune response to platelet aggregation	489:617	SOCE is the process by which endoplasmic reticulum (ER)-stored Ca2+ depletion leads to activation of plasma membrane Ca2+ channels to provide a sustained increase in cytosolic Ca2+ levels that mediate a plethora of physiological processes ranging from the immune response to platelet aggregation.
27865927	2	77	theme	Ca2+	499:502	arg1	levels					504:509	cytosolic Ca2+ levels	489:509	cytosolic Ca2+ levels that mediate a plethora of physiological processes ranging from the immune response to platelet aggregation	489:617	SOCE is the process by which endoplasmic reticulum (ER)-stored Ca2+ depletion leads to activation of plasma membrane Ca2+ channels to provide a sustained increase in cytosolic Ca2+ levels that mediate a plethora of physiological processes ranging from the immune response to platelet aggregation.
27865927	7	78	theme	Asn131Gln	1699:1707	arg1	mutations					1723:1731	Asn131Gln and Asn171Gln mutations	1699:1731	Asn131Gln and Asn171Gln mutations	1699:1731	Congruently, Ca2+ influx via SOCE in HEK293 cells co-expressing Orai1 and STIM1 was diminished when N-glycosylation was blocked by introducing Asn131Gln and Asn171Gln mutations.
27865927	2	79	theme	plasma	424:429	arg1	channels					445:452	plasma membrane Ca2+ channels	424:452	plasma membrane Ca2+ channels	424:452	SOCE is the process by which endoplasmic reticulum (ER)-stored Ca2+ depletion leads to activation of plasma membrane Ca2+ channels to provide a sustained increase in cytosolic Ca2+ levels that mediate a plethora of physiological processes ranging from the immune response to platelet aggregation.
27865927	1	80	theme	store-operated	289:302	arg1	SOCE					316:319	SOCE	316:319	SOCE	316:319	A major intracellular calcium (Ca2+) uptake pathway in both excitable and non-excitable eukaryotic cells is store-operated Ca2+ entry (SOCE).
27865927	1	80	theme	store-operated	289:302	arg1	pathway					225:231	A major intracellular calcium (Ca2+) uptake pathway	181:231	A major intracellular calcium (Ca2+) uptake pathway in both excitable and non-excitable eukaryotic cells	181:284	A major intracellular calcium (Ca2+) uptake pathway in both excitable and non-excitable eukaryotic cells is store-operated Ca2+ entry (SOCE).
27865927	1	80	theme	store-operated	289:302	arg1	entry					309:313	store-operated Ca2+ entry	289:313	store-operated Ca2+ entry (SOCE)	289:320	A major intracellular calcium (Ca2+) uptake pathway in both excitable and non-excitable eukaryotic cells is store-operated Ca2+ entry (SOCE).
27865927	5	81	theme	STIM1	1300:1304	arg1	activation					1306:1315	STIM1 activation	1300:1315	STIM1 activation	1300:1315	By establishing a site-specific chemical approach to covalently linking glucose to EFSAM and examining α-helicity, thermal stability, three dimensional atomic-resolution structure, Ca2+ binding affinity and oligomerization, we show that N-glycosylation of the EFSAM domain enhances the properties that promote STIM1 activation.
27865927	5	82	theme	Ca2+	1171:1174	arg1	structure					1160:1168	three dimensional atomic-resolution structure	1124:1168	three dimensional atomic-resolution structure	1124:1168	By establishing a site-specific chemical approach to covalently linking glucose to EFSAM and examining α-helicity, thermal stability, three dimensional atomic-resolution structure, Ca2+ binding affinity and oligomerization, we show that N-glycosylation of the EFSAM domain enhances the properties that promote STIM1 activation.
27865927	5	82	theme	Ca2+	1171:1174	arg1	affinity					1184:1191	Ca2+ binding affinity	1171:1191	Ca2+ binding affinity	1171:1191	By establishing a site-specific chemical approach to covalently linking glucose to EFSAM and examining α-helicity, thermal stability, three dimensional atomic-resolution structure, Ca2+ binding affinity and oligomerization, we show that N-glycosylation of the EFSAM domain enhances the properties that promote STIM1 activation.
27865927	4	83	theme	sensing	951:957	arg1	mechanism					959:967	the Ca2+ sensing mechanism	942:967	the Ca2+ sensing mechanism of STIM1	942:976	The EFSAM domain can undergo N-glycosylation at Asn131 and Asn171 sites; however, the precise role of EFSAM N-glycosylation in the Ca2+ sensing mechanism of STIM1 is unclear.
27865927	3	84	theme	interaction	628:638	arg1	regulator					676:684	the principal regulator	662:684	the principal regulator of SOCE	662:692	Stromal interaction molecule-1 (STIM1) is the principal regulator of SOCE and responds to changes in ER stored Ca2+ through luminal sensing machinery composed of EF-hand and SAM domains (EFSAM).
27865927	3	84	theme	interaction	628:638	arg1	STIM1					652:656	STIM1	652:656	STIM1	652:656	Stromal interaction molecule-1 (STIM1) is the principal regulator of SOCE and responds to changes in ER stored Ca2+ through luminal sensing machinery composed of EF-hand and SAM domains (EFSAM).
27865927	3	84	theme	interaction	628:638	arg1	molecule-1					640:649	Stromal interaction molecule-1	620:649	Stromal interaction molecule-1 (STIM1)	620:657	Stromal interaction molecule-1 (STIM1) is the principal regulator of SOCE and responds to changes in ER stored Ca2+ through luminal sensing machinery composed of EF-hand and SAM domains (EFSAM).
27865927	2	85	theme	Ca2+	386:389	arg1	depletion					391:399	endoplasmic reticulum (ER)-stored Ca2+ depletion	352:399	endoplasmic reticulum (ER)-stored Ca2+ depletion	352:399	SOCE is the process by which endoplasmic reticulum (ER)-stored Ca2+ depletion leads to activation of plasma membrane Ca2+ channels to provide a sustained increase in cytosolic Ca2+ levels that mediate a plethora of physiological processes ranging from the immune response to platelet aggregation.
27865927	6	86	theme	Asn171	1402:1407	arg1	sites					1409:1413	the Asn131 and Asn171 sites	1387:1413	sites	1409:1413	This augmentation occurs through changes in structure localized near the Asn131 and Asn171 sites that together permeate through the protein core and lead to decreased Ca2+ binding affinity, reduced stability and enhanced oligomerization.
27865927	4	87	theme	EFSAM	819:823	arg1	domain					825:830	The EFSAM domain	815:830	The EFSAM domain	815:830	The EFSAM domain can undergo N-glycosylation at Asn131 and Asn171 sites; however, the precise role of EFSAM N-glycosylation in the Ca2+ sensing mechanism of STIM1 is unclear.
27865927	2	88	theme	Ca2+	440:443	arg1	channels					445:452	plasma membrane Ca2+ channels	424:452	plasma membrane Ca2+ channels	424:452	SOCE is the process by which endoplasmic reticulum (ER)-stored Ca2+ depletion leads to activation of plasma membrane Ca2+ channels to provide a sustained increase in cytosolic Ca2+ levels that mediate a plethora of physiological processes ranging from the immune response to platelet aggregation.
27865927	6	89	theme	binding	1490:1496	arg1	affinity					1498:1505	decreased Ca2+ binding affinity	1475:1505	decreased Ca2+ binding affinity	1475:1505	This augmentation occurs through changes in structure localized near the Asn131 and Asn171 sites that together permeate through the protein core and lead to decreased Ca2+ binding affinity, reduced stability and enhanced oligomerization.
27865927	5	90	theme	dimensional	1130:1140	arg1	structure					1160:1168	three dimensional atomic-resolution structure	1124:1168	three dimensional atomic-resolution structure	1124:1168	By establishing a site-specific chemical approach to covalently linking glucose to EFSAM and examining α-helicity, thermal stability, three dimensional atomic-resolution structure, Ca2+ binding affinity and oligomerization, we show that N-glycosylation of the EFSAM domain enhances the properties that promote STIM1 activation.
27865927	5	90	theme	dimensional	1130:1140	arg1	oligomerization					1197:1211	oligomerization	1197:1211	oligomerization	1197:1211	By establishing a site-specific chemical approach to covalently linking glucose to EFSAM and examining α-helicity, thermal stability, three dimensional atomic-resolution structure, Ca2+ binding affinity and oligomerization, we show that N-glycosylation of the EFSAM domain enhances the properties that promote STIM1 activation.
27865927	5	90	theme	dimensional	1130:1140	arg1	affinity					1184:1191	Ca2+ binding affinity	1171:1191	Ca2+ binding affinity	1171:1191	By establishing a site-specific chemical approach to covalently linking glucose to EFSAM and examining α-helicity, thermal stability, three dimensional atomic-resolution structure, Ca2+ binding affinity and oligomerization, we show that N-glycosylation of the EFSAM domain enhances the properties that promote STIM1 activation.
27865927	5	90	theme	dimensional	1130:1140	arg1	α-helicity					1093:1102	α-helicity	1093:1102	α-helicity	1093:1102	By establishing a site-specific chemical approach to covalently linking glucose to EFSAM and examining α-helicity, thermal stability, three dimensional atomic-resolution structure, Ca2+ binding affinity and oligomerization, we show that N-glycosylation of the EFSAM domain enhances the properties that promote STIM1 activation.
27865927	6	91	theme	decreased	1475:1483	arg1	affinity					1498:1505	decreased Ca2+ binding affinity	1475:1505	decreased Ca2+ binding affinity	1475:1505	This augmentation occurs through changes in structure localized near the Asn131 and Asn171 sites that together permeate through the protein core and lead to decreased Ca2+ binding affinity, reduced stability and enhanced oligomerization.
27865927	3	92	theme	SOCE	689:692	arg1	regulator					676:684	the principal regulator	662:684	the principal regulator of SOCE	662:692	Stromal interaction molecule-1 (STIM1) is the principal regulator of SOCE and responds to changes in ER stored Ca2+ through luminal sensing machinery composed of EF-hand and SAM domains (EFSAM).
27865927	3	92	theme	SOCE	689:692	arg1	molecule-1					640:649	Stromal interaction molecule-1	620:649	Stromal interaction molecule-1 (STIM1)	620:657	Stromal interaction molecule-1 (STIM1) is the principal regulator of SOCE and responds to changes in ER stored Ca2+ through luminal sensing machinery composed of EF-hand and SAM domains (EFSAM).
27865927	2	93	theme	endoplasmic	352:362	arg1	ER					375:376	ER	375:376	ER	375:376	SOCE is the process by which endoplasmic reticulum (ER)-stored Ca2+ depletion leads to activation of plasma membrane Ca2+ channels to provide a sustained increase in cytosolic Ca2+ levels that mediate a plethora of physiological processes ranging from the immune response to platelet aggregation.
27865927	2	93	theme	endoplasmic	352:362	arg1	reticulum					364:372	endoplasmic reticulum	352:372	endoplasmic reticulum (ER)-stored Ca2+ depletion	352:399	SOCE is the process by which endoplasmic reticulum (ER)-stored Ca2+ depletion leads to activation of plasma membrane Ca2+ channels to provide a sustained increase in cytosolic Ca2+ levels that mediate a plethora of physiological processes ranging from the immune response to platelet aggregation.
27865927	1	94	theme	excitable	241:249	arg1	cells					280:284	both excitable and non-excitable eukaryotic cells	236:284	both excitable and non-excitable eukaryotic cells	236:284	A major intracellular calcium (Ca2+) uptake pathway in both excitable and non-excitable eukaryotic cells is store-operated Ca2+ entry (SOCE).
21550978	3	0	theme	rat	691:693	arg1	cells					702:706	Kirsten murine sarcoma virus-transformed rat kidney cells	650:706	Kirsten murine sarcoma virus-transformed rat kidney cells	650:706	In this study, epitope-tagged wild-type human PAR(1) (hPAR(1)) and a panel of N-linked glycosylation-deficient mutant receptors were permanently expressed in epithelial cells (Kirsten murine sarcoma virus-transformed rat kidney cells and CHO cells).
21550978	7	1	theme	optimal	1541:1547	arg1	expression					1571:1580	optimal receptor cell surface expression	1541:1580	optimal receptor cell surface expression	1541:1580	Removing these N-linked glycosylation sequons affected hPAR(1) cell surface expression to varying degrees, and N-linked glycosylation at extracellular loop 2 (especially Asn(250)) of hPAR(1) is essential for optimal receptor cell surface expression and receptor stability.
21550978	3	2	theme	wild-type	504:512	arg1	hPAR					528:531	hPAR(1)	528:534	hPAR(1)	528:534	In this study, epitope-tagged wild-type human PAR(1) (hPAR(1)) and a panel of N-linked glycosylation-deficient mutant receptors were permanently expressed in epithelial cells (Kirsten murine sarcoma virus-transformed rat kidney cells and CHO cells).
21550978	3	2	theme	wild-type	504:512	arg1	PAR					520:522	epitope-tagged wild-type human PAR(1)	489:525	epitope-tagged wild-type human PAR(1) (hPAR(1))	489:535	In this study, epitope-tagged wild-type human PAR(1) (hPAR(1)) and a panel of N-linked glycosylation-deficient mutant receptors were permanently expressed in epithelial cells (Kirsten murine sarcoma virus-transformed rat kidney cells and CHO cells).
21550978	5	3	theme	cathepsin	1112:1120	arg1	G					1122:1122	cathepsin G	1112:1122	the neutrophil proteinases elastase and proteinase 3 but not cathepsin G	1051:1122	We reported for the first time that glycosylation in the N terminus of hPAR(1) downstream of the tethered ligand (especially Asn(75)) governs receptor disarming to trypsin, thermolysin, and the neutrophil proteinases elastase and proteinase 3 but not cathepsin G.
21550978	5	4	theme	first	881:885	arg1	time					887:890	the first time	877:890	the first time	877:890	We reported for the first time that glycosylation in the N terminus of hPAR(1) downstream of the tethered ligand (especially Asn(75)) governs receptor disarming to trypsin, thermolysin, and the neutrophil proteinases elastase and proteinase 3 but not cathepsin G.
21550978	3	5	theme	murine	658:663	arg1	cells					702:706	Kirsten murine sarcoma virus-transformed rat kidney cells	650:706	Kirsten murine sarcoma virus-transformed rat kidney cells	650:706	In this study, epitope-tagged wild-type human PAR(1) (hPAR(1)) and a panel of N-linked glycosylation-deficient mutant receptors were permanently expressed in epithelial cells (Kirsten murine sarcoma virus-transformed rat kidney cells and CHO cells).
21550978	4	6	theme	hPAR	852:855	arg1	expression					838:847	proteinase activation/disarming and cell global expression	790:847	proteinase activation/disarming and cell global expression of hPAR(1)	790:858	We have analyzed the role of N-linked glycosylation in regulating proteinase activation/disarming and cell global expression of hPAR(1).
21550978	7	7	dep	Asn	1503:1505	arg1	especially					1492:1501	especially	1492:1501	especially	1492:1501	Removing these N-linked glycosylation sequons affected hPAR(1) cell surface expression to varying degrees, and N-linked glycosylation at extracellular loop 2 (especially Asn(250)) of hPAR(1) is essential for optimal receptor cell surface expression and receptor stability.
21550978	3	8	theme	human	514:518	arg1	hPAR					528:531	hPAR(1)	528:534	hPAR(1)	528:534	In this study, epitope-tagged wild-type human PAR(1) (hPAR(1)) and a panel of N-linked glycosylation-deficient mutant receptors were permanently expressed in epithelial cells (Kirsten murine sarcoma virus-transformed rat kidney cells and CHO cells).
21550978	3	8	theme	human	514:518	arg1	PAR					520:522	epitope-tagged wild-type human PAR(1)	489:525	epitope-tagged wild-type human PAR(1) (hPAR(1))	489:535	In this study, epitope-tagged wild-type human PAR(1) (hPAR(1)) and a panel of N-linked glycosylation-deficient mutant receptors were permanently expressed in epithelial cells (Kirsten murine sarcoma virus-transformed rat kidney cells and CHO cells).
21550978	3	9	dep	cells	643:647	arg1	cells					702:706	Kirsten murine sarcoma virus-transformed rat kidney cells	650:706	Kirsten murine sarcoma virus-transformed rat kidney cells	650:706	In this study, epitope-tagged wild-type human PAR(1) (hPAR(1)) and a panel of N-linked glycosylation-deficient mutant receptors were permanently expressed in epithelial cells (Kirsten murine sarcoma virus-transformed rat kidney cells and CHO cells).
21550978	3	9	dep	cells	643:647	arg1	cells					716:720	CHO cells	712:720	CHO cells	712:720	In this study, epitope-tagged wild-type human PAR(1) (hPAR(1)) and a panel of N-linked glycosylation-deficient mutant receptors were permanently expressed in epithelial cells (Kirsten murine sarcoma virus-transformed rat kidney cells and CHO cells).
21550978	6	10	theme	consensus	1257:1265	arg1	Asn					1323:1325	Asn(259)	1323:1330	Asn(259)	1323:1330	In addition, hPAR(1) is heavily N-linked glycosylated and sialylated in epithelial cell lines, and glycosylation occurs at all five consensus sites, namely, Asn(35), Asn(62), Asn(75), Asn(250), and Asn(259).
21550978	6	10	theme	consensus	1257:1265	arg1	sites					1267:1271	all five consensus sites	1248:1271	all five consensus sites	1248:1271	In addition, hPAR(1) is heavily N-linked glycosylated and sialylated in epithelial cell lines, and glycosylation occurs at all five consensus sites, namely, Asn(35), Asn(62), Asn(75), Asn(250), and Asn(259).
21550978	6	10	theme	consensus	1257:1265	arg1	Asn					1300:1302	Asn(75)	1300:1306	Asn(75)	1300:1306	In addition, hPAR(1) is heavily N-linked glycosylated and sialylated in epithelial cell lines, and glycosylation occurs at all five consensus sites, namely, Asn(35), Asn(62), Asn(75), Asn(250), and Asn(259).
21550978	6	10	theme	consensus	1257:1265	arg1	Asn					1291:1293	Asn(62)	1291:1297	Asn(62)	1291:1297	In addition, hPAR(1) is heavily N-linked glycosylated and sialylated in epithelial cell lines, and glycosylation occurs at all five consensus sites, namely, Asn(35), Asn(62), Asn(75), Asn(250), and Asn(259).
21550978	6	10	theme	consensus	1257:1265	arg1	Asn					1282:1284	Asn(35)	1282:1288	Asn(35)	1282:1288	In addition, hPAR(1) is heavily N-linked glycosylated and sialylated in epithelial cell lines, and glycosylation occurs at all five consensus sites, namely, Asn(35), Asn(62), Asn(75), Asn(250), and Asn(259).
21550978	6	10	theme	consensus	1257:1265	arg1	Asn					1309:1311	Asn(250)	1309:1316	Asn(250)	1309:1316	In addition, hPAR(1) is heavily N-linked glycosylated and sialylated in epithelial cell lines, and glycosylation occurs at all five consensus sites, namely, Asn(35), Asn(62), Asn(75), Asn(250), and Asn(259).
21550978	3	11	theme	sarcoma	665:671	arg1	cells					702:706	Kirsten murine sarcoma virus-transformed rat kidney cells	650:706	Kirsten murine sarcoma virus-transformed rat kidney cells	650:706	In this study, epitope-tagged wild-type human PAR(1) (hPAR(1)) and a panel of N-linked glycosylation-deficient mutant receptors were permanently expressed in epithelial cells (Kirsten murine sarcoma virus-transformed rat kidney cells and CHO cells).
21550978	7	12	from	loop	1484:1487	arg1	glycosylation					1453:1465	N-linked glycosylation	1444:1465	N-linked glycosylation at extracellular loop 2 (especially Asn(250)) of hPAR(1)	1444:1522	Removing these N-linked glycosylation sequons affected hPAR(1) cell surface expression to varying degrees, and N-linked glycosylation at extracellular loop 2 (especially Asn(250)) of hPAR(1) is essential for optimal receptor cell surface expression and receptor stability.
21550978	1	13	theme	extracellular	278:290	arg1	terminus					294:301	its extracellular N terminus	274:301	its extracellular N terminus	274:301	Proteinase-activated receptor 1 (PAR(1)) induces activation of platelet and vascular cells after proteolytic cleavage of its extracellular N terminus by thrombin.
21550978	0	14	theme	neutrophil	113:122	arg1	proteinases					124:134	neutrophil proteinases	113:134	neutrophil proteinases	113:134	N-linked glycosylation regulates human proteinase-activated receptor-1 cell surface expression and disarming via neutrophil proteinases and thermolysin.
21550978	7	15	link	N-linked	1444:1451	arg1	glycosylation					1453:1465	N-linked glycosylation	1444:1465	N-linked glycosylation at extracellular loop 2 (especially Asn(250)) of hPAR(1)	1444:1522	Removing these N-linked glycosylation sequons affected hPAR(1) cell surface expression to varying degrees, and N-linked glycosylation at extracellular loop 2 (especially Asn(250)) of hPAR(1) is essential for optimal receptor cell surface expression and receptor stability.
21550978	7	16	theme	receptor	1586:1593	arg1	stability					1595:1603	receptor stability	1586:1603	receptor stability	1586:1603	Removing these N-linked glycosylation sequons affected hPAR(1) cell surface expression to varying degrees, and N-linked glycosylation at extracellular loop 2 (especially Asn(250)) of hPAR(1) is essential for optimal receptor cell surface expression and receptor stability.
21550978	7	17	theme	varying	1423:1429	arg1	degrees					1431:1437	varying degrees	1423:1437	varying degrees	1423:1437	Removing these N-linked glycosylation sequons affected hPAR(1) cell surface expression to varying degrees, and N-linked glycosylation at extracellular loop 2 (especially Asn(250)) of hPAR(1) is essential for optimal receptor cell surface expression and receptor stability.
21550978	1	18	theme	N	292:292	arg1	terminus					294:301	its extracellular N terminus	274:301	its extracellular N terminus	274:301	Proteinase-activated receptor 1 (PAR(1)) induces activation of platelet and vascular cells after proteolytic cleavage of its extracellular N terminus by thrombin.
21550978	3	19	theme	CHO	712:714	arg1	cells					716:720	CHO cells	712:720	CHO cells	712:720	In this study, epitope-tagged wild-type human PAR(1) (hPAR(1)) and a panel of N-linked glycosylation-deficient mutant receptors were permanently expressed in epithelial cells (Kirsten murine sarcoma virus-transformed rat kidney cells and CHO cells).
21550978	4	20	theme	global	831:836	arg1	expression					838:847	proteinase activation/disarming and cell global expression	790:847	proteinase activation/disarming and cell global expression of hPAR(1)	790:858	We have analyzed the role of N-linked glycosylation in regulating proteinase activation/disarming and cell global expression of hPAR(1).
21550978	2	21	theme	PAR	432:434	arg1	responses					419:427	the responses	415:427	the responses of PAR(1)	415:437	In pathological situations, other proteinases may be generated in the circulation and might modify the responses of PAR(1) by cleaving extracellular domains.
21550978	5	22	theme	hPAR	932:935	arg1	terminus					920:927	the N terminus	914:927	the N terminus of hPAR(1) downstream of the tethered ligand (especially Asn(75))	914:993	We reported for the first time that glycosylation in the N terminus of hPAR(1) downstream of the tethered ligand (especially Asn(75)) governs receptor disarming to trypsin, thermolysin, and the neutrophil proteinases elastase and proteinase 3 but not cathepsin G.
21550978	7	23	theme	extracellular	1470:1482	arg1	loop					1484:1487	extracellular loop 2	1470:1489	extracellular loop 2 (especially Asn(250)) of hPAR(1)	1470:1522	Removing these N-linked glycosylation sequons affected hPAR(1) cell surface expression to varying degrees, and N-linked glycosylation at extracellular loop 2 (especially Asn(250)) of hPAR(1) is essential for optimal receptor cell surface expression and receptor stability.
21550978	7	23	theme	extracellular	1470:1482	arg1	Asn					1503:1505	Asn(250)	1503:1510	Asn(250)	1503:1510	Removing these N-linked glycosylation sequons affected hPAR(1) cell surface expression to varying degrees, and N-linked glycosylation at extracellular loop 2 (especially Asn(250)) of hPAR(1) is essential for optimal receptor cell surface expression and receptor stability.
21550978	5	24	dep	ligand	967:972	arg1	75					990:991	75	990:991	75	990:991	We reported for the first time that glycosylation in the N terminus of hPAR(1) downstream of the tethered ligand (especially Asn(75)) governs receptor disarming to trypsin, thermolysin, and the neutrophil proteinases elastase and proteinase 3 but not cathepsin G.
21550978	5	24	dep	ligand	967:972	arg1	Asn					986:988	Asn	986:988	especially Asn(75)	975:992	We reported for the first time that glycosylation in the N terminus of hPAR(1) downstream of the tethered ligand (especially Asn(75)) governs receptor disarming to trypsin, thermolysin, and the neutrophil proteinases elastase and proteinase 3 but not cathepsin G.
21550978	2	25	theme	extracellular	451:463	arg1	domains					465:471	extracellular domains	451:471	extracellular domains	451:471	In pathological situations, other proteinases may be generated in the circulation and might modify the responses of PAR(1) by cleaving extracellular domains.
21550978	3	26	theme	kidney	695:700	arg1	cells					702:706	Kirsten murine sarcoma virus-transformed rat kidney cells	650:706	Kirsten murine sarcoma virus-transformed rat kidney cells	650:706	In this study, epitope-tagged wild-type human PAR(1) (hPAR(1)) and a panel of N-linked glycosylation-deficient mutant receptors were permanently expressed in epithelial cells (Kirsten murine sarcoma virus-transformed rat kidney cells and CHO cells).
21550978	6	27	gly	glycosylated	1166:1177	arg1	hPAR					1138:1141	hPAR(1)	1138:1144	hPAR(1)	1138:1144	In addition, hPAR(1) is heavily N-linked glycosylated and sialylated in epithelial cell lines, and glycosylation occurs at all five consensus sites, namely, Asn(35), Asn(62), Asn(75), Asn(250), and Asn(259).
21550978	7	28	link	N-linked	1348:1355	arg1	sequons					1371:1377	these N-linked glycosylation sequons	1342:1377	these N-linked glycosylation sequons	1342:1377	Removing these N-linked glycosylation sequons affected hPAR(1) cell surface expression to varying degrees, and N-linked glycosylation at extracellular loop 2 (especially Asn(250)) of hPAR(1) is essential for optimal receptor cell surface expression and receptor stability.
21550978	6	29	from	N-linked	1157:1164	arg1	addition					1128:1135	addition	1128:1135	addition	1128:1135	In addition, hPAR(1) is heavily N-linked glycosylated and sialylated in epithelial cell lines, and glycosylation occurs at all five consensus sites, namely, Asn(35), Asn(62), Asn(75), Asn(250), and Asn(259).
21550978	7	30	theme	N-linked	1444:1451	arg1	glycosylation					1453:1465	N-linked glycosylation	1444:1465	N-linked glycosylation at extracellular loop 2 (especially Asn(250)) of hPAR(1)	1444:1522	Removing these N-linked glycosylation sequons affected hPAR(1) cell surface expression to varying degrees, and N-linked glycosylation at extracellular loop 2 (especially Asn(250)) of hPAR(1) is essential for optimal receptor cell surface expression and receptor stability.
21550978	7	31	theme	hPAR	1388:1391	arg1	expression					1409:1418	hPAR(1) cell surface expression	1388:1418	hPAR(1) cell surface expression to varying degrees	1388:1437	Removing these N-linked glycosylation sequons affected hPAR(1) cell surface expression to varying degrees, and N-linked glycosylation at extracellular loop 2 (especially Asn(250)) of hPAR(1) is essential for optimal receptor cell surface expression and receptor stability.
21550978	3	32	link	N-linked	552:559	arg1	receptors					592:600	N-linked glycosylation-deficient mutant receptors	552:600	N-linked glycosylation-deficient mutant receptors	552:600	In this study, epitope-tagged wild-type human PAR(1) (hPAR(1)) and a panel of N-linked glycosylation-deficient mutant receptors were permanently expressed in epithelial cells (Kirsten murine sarcoma virus-transformed rat kidney cells and CHO cells).
21550978	5	33	dep	proteinases	1066:1076	arg1	elastase					1078:1085	elastase	1078:1085	elastase	1078:1085	We reported for the first time that glycosylation in the N terminus of hPAR(1) downstream of the tethered ligand (especially Asn(75)) governs receptor disarming to trypsin, thermolysin, and the neutrophil proteinases elastase and proteinase 3 but not cathepsin G.
21550978	5	33	dep	proteinases	1066:1076	arg1	G					1122:1122	cathepsin G	1112:1122	the neutrophil proteinases elastase and proteinase 3 but not cathepsin G	1051:1122	We reported for the first time that glycosylation in the N terminus of hPAR(1) downstream of the tethered ligand (especially Asn(75)) governs receptor disarming to trypsin, thermolysin, and the neutrophil proteinases elastase and proteinase 3 but not cathepsin G.
21550978	5	33	dep	proteinases	1066:1076	arg1	proteinase					1091:1100	proteinase 3	1091:1102	proteinase 3	1091:1102	We reported for the first time that glycosylation in the N terminus of hPAR(1) downstream of the tethered ligand (especially Asn(75)) governs receptor disarming to trypsin, thermolysin, and the neutrophil proteinases elastase and proteinase 3 but not cathepsin G.
21550978	5	33	dep	proteinases	1066:1076	arg1	proteinases					1066:1076	the neutrophil proteinases elastase and proteinase 3 but not cathepsin G	1051:1122	the neutrophil proteinases elastase and proteinase 3 but not cathepsin G	1051:1122	We reported for the first time that glycosylation in the N terminus of hPAR(1) downstream of the tethered ligand (especially Asn(75)) governs receptor disarming to trypsin, thermolysin, and the neutrophil proteinases elastase and proteinase 3 but not cathepsin G.
21550978	7	34	theme	N-linked	1348:1355	arg1	sequons					1371:1377	these N-linked glycosylation sequons	1342:1377	these N-linked glycosylation sequons	1342:1377	Removing these N-linked glycosylation sequons affected hPAR(1) cell surface expression to varying degrees, and N-linked glycosylation at extracellular loop 2 (especially Asn(250)) of hPAR(1) is essential for optimal receptor cell surface expression and receptor stability.
21550978	0	35	theme	N-linked	0:7	arg1	glycosylation					9:21	N-linked glycosylation	0:21	N-linked glycosylation	0:21	N-linked glycosylation regulates human proteinase-activated receptor-1 cell surface expression and disarming via neutrophil proteinases and thermolysin.
21550978	1	36	theme	terminus	294:301	arg1	cleavage					262:269	proteolytic cleavage	250:269	proteolytic cleavage of its extracellular N terminus by thrombin	250:313	Proteinase-activated receptor 1 (PAR(1)) induces activation of platelet and vascular cells after proteolytic cleavage of its extracellular N terminus by thrombin.
21550978	7	37	gly	glycosylation	1357:1369	arg2	sequons					1371:1377	these N-linked glycosylation sequons	1342:1377	these N-linked glycosylation sequons	1342:1377	Removing these N-linked glycosylation sequons affected hPAR(1) cell surface expression to varying degrees, and N-linked glycosylation at extracellular loop 2 (especially Asn(250)) of hPAR(1) is essential for optimal receptor cell surface expression and receptor stability.
21550978	7	38	theme	hPAR	1516:1519	arg1	loop					1484:1487	extracellular loop 2	1470:1489	extracellular loop 2 (especially Asn(250)) of hPAR(1)	1470:1522	Removing these N-linked glycosylation sequons affected hPAR(1) cell surface expression to varying degrees, and N-linked glycosylation at extracellular loop 2 (especially Asn(250)) of hPAR(1) is essential for optimal receptor cell surface expression and receptor stability.
21550978	7	38	theme	hPAR	1516:1519	arg1	Asn					1503:1505	Asn(250)	1503:1510	Asn(250)	1503:1510	Removing these N-linked glycosylation sequons affected hPAR(1) cell surface expression to varying degrees, and N-linked glycosylation at extracellular loop 2 (especially Asn(250)) of hPAR(1) is essential for optimal receptor cell surface expression and receptor stability.
21550978	0	39	theme	human	33:37	arg1	receptor-1					60:69	human proteinase-activated receptor-1	33:69	human proteinase-activated receptor-1 cell surface expression	33:93	N-linked glycosylation regulates human proteinase-activated receptor-1 cell surface expression and disarming via neutrophil proteinases and thermolysin.
21550978	7	40	theme	surface	1401:1407	arg1	expression					1409:1418	hPAR(1) cell surface expression	1388:1418	hPAR(1) cell surface expression to varying degrees	1388:1437	Removing these N-linked glycosylation sequons affected hPAR(1) cell surface expression to varying degrees, and N-linked glycosylation at extracellular loop 2 (especially Asn(250)) of hPAR(1) is essential for optimal receptor cell surface expression and receptor stability.
21550978	0	41	link	N-linked	0:7	arg1	glycosylation					9:21	N-linked glycosylation	0:21	N-linked glycosylation	0:21	N-linked glycosylation regulates human proteinase-activated receptor-1 cell surface expression and disarming via neutrophil proteinases and thermolysin.
21550978	2	42	theme	pathological	319:330	arg1	situations					332:341	pathological situations	319:341	pathological situations	319:341	In pathological situations, other proteinases may be generated in the circulation and might modify the responses of PAR(1) by cleaving extracellular domains.
21550978	6	43	gly	glycosylation	1224:1236	arg2	Asn					1309:1311	Asn(250)	1309:1316	Asn(250)	1309:1316	In addition, hPAR(1) is heavily N-linked glycosylated and sialylated in epithelial cell lines, and glycosylation occurs at all five consensus sites, namely, Asn(35), Asn(62), Asn(75), Asn(250), and Asn(259).
21550978	6	43	gly	glycosylation	1224:1236	arg2	Asn					1323:1325	Asn(259)	1323:1330	Asn(259)	1323:1330	In addition, hPAR(1) is heavily N-linked glycosylated and sialylated in epithelial cell lines, and glycosylation occurs at all five consensus sites, namely, Asn(35), Asn(62), Asn(75), Asn(250), and Asn(259).
21550978	6	43	gly	glycosylation	1224:1236	arg2	Asn					1282:1284	Asn(35)	1282:1288	Asn(35)	1282:1288	In addition, hPAR(1) is heavily N-linked glycosylated and sialylated in epithelial cell lines, and glycosylation occurs at all five consensus sites, namely, Asn(35), Asn(62), Asn(75), Asn(250), and Asn(259).
21550978	6	43	gly	glycosylation	1224:1236	arg2	sites					1267:1271	all five consensus sites	1248:1271	all five consensus sites	1248:1271	In addition, hPAR(1) is heavily N-linked glycosylated and sialylated in epithelial cell lines, and glycosylation occurs at all five consensus sites, namely, Asn(35), Asn(62), Asn(75), Asn(250), and Asn(259).
21550978	6	43	gly	glycosylation	1224:1236	arg2	Asn					1291:1293	Asn(62)	1291:1297	Asn(62)	1291:1297	In addition, hPAR(1) is heavily N-linked glycosylated and sialylated in epithelial cell lines, and glycosylation occurs at all five consensus sites, namely, Asn(35), Asn(62), Asn(75), Asn(250), and Asn(259).
21550978	6	43	gly	glycosylation	1224:1236	arg2	Asn					1300:1302	Asn(75)	1300:1306	Asn(75)	1300:1306	In addition, hPAR(1) is heavily N-linked glycosylated and sialylated in epithelial cell lines, and glycosylation occurs at all five consensus sites, namely, Asn(35), Asn(62), Asn(75), Asn(250), and Asn(259).
21550978	7	44	theme	cell	1396:1399	arg1	expression					1409:1418	hPAR(1) cell surface expression	1388:1418	hPAR(1) cell surface expression to varying degrees	1388:1437	Removing these N-linked glycosylation sequons affected hPAR(1) cell surface expression to varying degrees, and N-linked glycosylation at extracellular loop 2 (especially Asn(250)) of hPAR(1) is essential for optimal receptor cell surface expression and receptor stability.
21550978	5	45	theme	N	918:918	arg1	terminus					920:927	the N terminus	914:927	the N terminus of hPAR(1) downstream of the tethered ligand (especially Asn(75))	914:993	We reported for the first time that glycosylation in the N terminus of hPAR(1) downstream of the tethered ligand (especially Asn(75)) governs receptor disarming to trypsin, thermolysin, and the neutrophil proteinases elastase and proteinase 3 but not cathepsin G.
21550978	6	46	attach	N-linked	1157:1164	arg3	addition					1128:1135	addition	1128:1135	addition	1128:1135	In addition, hPAR(1) is heavily N-linked glycosylated and sialylated in epithelial cell lines, and glycosylation occurs at all five consensus sites, namely, Asn(35), Asn(62), Asn(75), Asn(250), and Asn(259).
21550978	1	47	theme	platelet	216:223	arg1	cells					238:242	platelet and vascular cells	216:242	cells	238:242	Proteinase-activated receptor 1 (PAR(1)) induces activation of platelet and vascular cells after proteolytic cleavage of its extracellular N terminus by thrombin.
21550978	0	48	theme	receptor-1	60:69	arg1	expression					84:93	human proteinase-activated receptor-1 cell surface expression	33:93	human proteinase-activated receptor-1 cell surface expression	33:93	N-linked glycosylation regulates human proteinase-activated receptor-1 cell surface expression and disarming via neutrophil proteinases and thermolysin.
21550978	3	49	theme	epitope-tagged	489:502	arg1	hPAR					528:531	hPAR(1)	528:534	hPAR(1)	528:534	In this study, epitope-tagged wild-type human PAR(1) (hPAR(1)) and a panel of N-linked glycosylation-deficient mutant receptors were permanently expressed in epithelial cells (Kirsten murine sarcoma virus-transformed rat kidney cells and CHO cells).
21550978	3	49	theme	epitope-tagged	489:502	arg1	PAR					520:522	epitope-tagged wild-type human PAR(1)	489:525	epitope-tagged wild-type human PAR(1) (hPAR(1))	489:535	In this study, epitope-tagged wild-type human PAR(1) (hPAR(1)) and a panel of N-linked glycosylation-deficient mutant receptors were permanently expressed in epithelial cells (Kirsten murine sarcoma virus-transformed rat kidney cells and CHO cells).
21550978	4	50	link	N-linked	753:760	arg1	glycosylation					762:774	N-linked glycosylation	753:774	N-linked glycosylation	753:774	We have analyzed the role of N-linked glycosylation in regulating proteinase activation/disarming and cell global expression of hPAR(1).
21550978	0	51	theme	proteinase-activated	39:58	arg1	receptor-1					60:69	human proteinase-activated receptor-1	33:69	human proteinase-activated receptor-1 cell surface expression	33:93	N-linked glycosylation regulates human proteinase-activated receptor-1 cell surface expression and disarming via neutrophil proteinases and thermolysin.
21550978	5	52	theme	neutrophil	1055:1064	arg1	elastase					1078:1085	elastase	1078:1085	elastase	1078:1085	We reported for the first time that glycosylation in the N terminus of hPAR(1) downstream of the tethered ligand (especially Asn(75)) governs receptor disarming to trypsin, thermolysin, and the neutrophil proteinases elastase and proteinase 3 but not cathepsin G.
21550978	5	52	theme	neutrophil	1055:1064	arg1	proteinases					1066:1076	the neutrophil proteinases elastase and proteinase 3 but not cathepsin G	1051:1122	the neutrophil proteinases elastase and proteinase 3 but not cathepsin G	1051:1122	We reported for the first time that glycosylation in the N terminus of hPAR(1) downstream of the tethered ligand (especially Asn(75)) governs receptor disarming to trypsin, thermolysin, and the neutrophil proteinases elastase and proteinase 3 but not cathepsin G.
21550978	5	52	theme	neutrophil	1055:1064	arg1	proteinase					1091:1100	proteinase 3	1091:1102	proteinase 3	1091:1102	We reported for the first time that glycosylation in the N terminus of hPAR(1) downstream of the tethered ligand (especially Asn(75)) governs receptor disarming to trypsin, thermolysin, and the neutrophil proteinases elastase and proteinase 3 but not cathepsin G.
21550978	7	53	theme	glycosylation	1357:1369	arg1	sequons					1371:1377	these N-linked glycosylation sequons	1342:1377	these N-linked glycosylation sequons	1342:1377	Removing these N-linked glycosylation sequons affected hPAR(1) cell surface expression to varying degrees, and N-linked glycosylation at extracellular loop 2 (especially Asn(250)) of hPAR(1) is essential for optimal receptor cell surface expression and receptor stability.
21550978	5	54	theme	tethered	958:965	arg1	ligand					967:972	the tethered ligand	954:972	the tethered ligand (especially Asn(75))	954:993	We reported for the first time that glycosylation in the N terminus of hPAR(1) downstream of the tethered ligand (especially Asn(75)) governs receptor disarming to trypsin, thermolysin, and the neutrophil proteinases elastase and proteinase 3 but not cathepsin G.
21550978	1	55	theme	vascular	229:236	arg1	cells					238:242	platelet and vascular cells	216:242	cells	238:242	Proteinase-activated receptor 1 (PAR(1)) induces activation of platelet and vascular cells after proteolytic cleavage of its extracellular N terminus by thrombin.
21550978	0	56	theme	surface	76:82	arg1	expression					84:93	human proteinase-activated receptor-1 cell surface expression	33:93	human proteinase-activated receptor-1 cell surface expression	33:93	N-linked glycosylation regulates human proteinase-activated receptor-1 cell surface expression and disarming via neutrophil proteinases and thermolysin.
21550978	5	57	theme	receptor	1003:1010	arg1	disarming					1012:1020	receptor disarming	1003:1020	receptor disarming	1003:1020	We reported for the first time that glycosylation in the N terminus of hPAR(1) downstream of the tethered ligand (especially Asn(75)) governs receptor disarming to trypsin, thermolysin, and the neutrophil proteinases elastase and proteinase 3 but not cathepsin G.
21550978	7	58	gly	glycosylation	1453:1465	arg1	receptor					1549:1556	optimal receptor cell surface expression	1541:1580	optimal receptor cell surface expression	1541:1580	Removing these N-linked glycosylation sequons affected hPAR(1) cell surface expression to varying degrees, and N-linked glycosylation at extracellular loop 2 (especially Asn(250)) of hPAR(1) is essential for optimal receptor cell surface expression and receptor stability.
21550978	7	58	gly	glycosylation	1453:1465	arg2	loop					1484:1487	extracellular loop 2	1470:1489	extracellular loop 2 (especially Asn(250)) of hPAR(1)	1470:1522	Removing these N-linked glycosylation sequons affected hPAR(1) cell surface expression to varying degrees, and N-linked glycosylation at extracellular loop 2 (especially Asn(250)) of hPAR(1) is essential for optimal receptor cell surface expression and receptor stability.
21550978	7	58	gly	glycosylation	1453:1465	arg1	cell					1558:1561	optimal receptor cell surface expression	1541:1580	optimal receptor cell surface expression	1541:1580	Removing these N-linked glycosylation sequons affected hPAR(1) cell surface expression to varying degrees, and N-linked glycosylation at extracellular loop 2 (especially Asn(250)) of hPAR(1) is essential for optimal receptor cell surface expression and receptor stability.
21550978	7	58	gly	glycosylation	1453:1465	arg1	loop					1484:1487	extracellular loop 2	1470:1489	extracellular loop 2 (especially Asn(250)) of hPAR(1)	1470:1522	Removing these N-linked glycosylation sequons affected hPAR(1) cell surface expression to varying degrees, and N-linked glycosylation at extracellular loop 2 (especially Asn(250)) of hPAR(1) is essential for optimal receptor cell surface expression and receptor stability.
21550978	7	58	gly	glycosylation	1453:1465	arg2	Asn					1503:1505	Asn(250)	1503:1510	Asn(250)	1503:1510	Removing these N-linked glycosylation sequons affected hPAR(1) cell surface expression to varying degrees, and N-linked glycosylation at extracellular loop 2 (especially Asn(250)) of hPAR(1) is essential for optimal receptor cell surface expression and receptor stability.
21550978	7	58	gly	glycosylation	1453:1465	arg1	surface					1563:1569	optimal receptor cell surface expression	1541:1580	optimal receptor cell surface expression	1541:1580	Removing these N-linked glycosylation sequons affected hPAR(1) cell surface expression to varying degrees, and N-linked glycosylation at extracellular loop 2 (especially Asn(250)) of hPAR(1) is essential for optimal receptor cell surface expression and receptor stability.
21550978	7	58	gly	glycosylation	1453:1465	arg1	receptor					1586:1593	receptor stability	1586:1603	receptor stability	1586:1603	Removing these N-linked glycosylation sequons affected hPAR(1) cell surface expression to varying degrees, and N-linked glycosylation at extracellular loop 2 (especially Asn(250)) of hPAR(1) is essential for optimal receptor cell surface expression and receptor stability.
21550978	7	58	gly	glycosylation	1453:1465	arg1	Asn					1503:1505	Asn(250)	1503:1510	Asn(250)	1503:1510	Removing these N-linked glycosylation sequons affected hPAR(1) cell surface expression to varying degrees, and N-linked glycosylation at extracellular loop 2 (especially Asn(250)) of hPAR(1) is essential for optimal receptor cell surface expression and receptor stability.
21550978	0	59	theme	cell	71:74	arg1	expression					84:93	human proteinase-activated receptor-1 cell surface expression	33:93	human proteinase-activated receptor-1 cell surface expression	33:93	N-linked glycosylation regulates human proteinase-activated receptor-1 cell surface expression and disarming via neutrophil proteinases and thermolysin.
21550978	6	60	dep	N-linked	1157:1164	arg1	glycosylated					1166:1177	glycosylated	1166:1177	glycosylated	1166:1177	In addition, hPAR(1) is heavily N-linked glycosylated and sialylated in epithelial cell lines, and glycosylation occurs at all five consensus sites, namely, Asn(35), Asn(62), Asn(75), Asn(250), and Asn(259).
21550978	6	60	dep	N-linked	1157:1164	arg1	sialylated					1183:1192	sialylated	1183:1192	sialylated in epithelial cell lines	1183:1217	In addition, hPAR(1) is heavily N-linked glycosylated and sialylated in epithelial cell lines, and glycosylation occurs at all five consensus sites, namely, Asn(35), Asn(62), Asn(75), Asn(250), and Asn(259).
21550978	6	61	theme	cell	1208:1211	arg1	lines					1213:1217	epithelial cell lines	1197:1217	epithelial cell lines	1197:1217	In addition, hPAR(1) is heavily N-linked glycosylated and sialylated in epithelial cell lines, and glycosylation occurs at all five consensus sites, namely, Asn(35), Asn(62), Asn(75), Asn(250), and Asn(259).
21550978	4	62	theme	activation/disarming	801:820	arg1	expression					838:847	proteinase activation/disarming and cell global expression	790:847	proteinase activation/disarming and cell global expression of hPAR(1)	790:858	We have analyzed the role of N-linked glycosylation in regulating proteinase activation/disarming and cell global expression of hPAR(1).
21550978	7	63	theme	surface	1563:1569	arg1	expression					1571:1580	optimal receptor cell surface expression	1541:1580	optimal receptor cell surface expression	1541:1580	Removing these N-linked glycosylation sequons affected hPAR(1) cell surface expression to varying degrees, and N-linked glycosylation at extracellular loop 2 (especially Asn(250)) of hPAR(1) is essential for optimal receptor cell surface expression and receptor stability.
21550978	1	64	theme	Proteinase-activated	153:172	arg1	receptor					174:181	Proteinase-activated receptor 1	153:183	Proteinase-activated receptor 1 (PAR(1))	153:192	Proteinase-activated receptor 1 (PAR(1)) induces activation of platelet and vascular cells after proteolytic cleavage of its extracellular N terminus by thrombin.
21550978	1	64	theme	Proteinase-activated	153:172	arg1	PAR					186:188	PAR(1)	186:191	PAR(1)	186:191	Proteinase-activated receptor 1 (PAR(1)) induces activation of platelet and vascular cells after proteolytic cleavage of its extracellular N terminus by thrombin.
21550978	4	65	theme	glycosylation	762:774	arg1	role					745:748	the role	741:748	the role of N-linked glycosylation in regulating proteinase activation/disarming and cell global expression of hPAR(1)	741:858	We have analyzed the role of N-linked glycosylation in regulating proteinase activation/disarming and cell global expression of hPAR(1).
21550978	6	66	theme	epithelial	1197:1206	arg1	lines					1213:1217	epithelial cell lines	1197:1217	epithelial cell lines	1197:1217	In addition, hPAR(1) is heavily N-linked glycosylated and sialylated in epithelial cell lines, and glycosylation occurs at all five consensus sites, namely, Asn(35), Asn(62), Asn(75), Asn(250), and Asn(259).
21550978	3	67	theme	Kirsten	650:656	arg1	cells					702:706	Kirsten murine sarcoma virus-transformed rat kidney cells	650:706	Kirsten murine sarcoma virus-transformed rat kidney cells	650:706	In this study, epitope-tagged wild-type human PAR(1) (hPAR(1)) and a panel of N-linked glycosylation-deficient mutant receptors were permanently expressed in epithelial cells (Kirsten murine sarcoma virus-transformed rat kidney cells and CHO cells).
21550978	3	68	theme	mutant	585:590	arg1	receptors					592:600	N-linked glycosylation-deficient mutant receptors	552:600	N-linked glycosylation-deficient mutant receptors	552:600	In this study, epitope-tagged wild-type human PAR(1) (hPAR(1)) and a panel of N-linked glycosylation-deficient mutant receptors were permanently expressed in epithelial cells (Kirsten murine sarcoma virus-transformed rat kidney cells and CHO cells).
21550978	6	69	from	addition	1128:1135	arg1	N-linked					1157:1164	N-linked	1157:1164	N-linked	1157:1164	In addition, hPAR(1) is heavily N-linked glycosylated and sialylated in epithelial cell lines, and glycosylation occurs at all five consensus sites, namely, Asn(35), Asn(62), Asn(75), Asn(250), and Asn(259).
21550978	1	70	theme	cells	238:242	arg1	activation					202:211	activation	202:211	activation of platelet and vascular cells	202:242	Proteinase-activated receptor 1 (PAR(1)) induces activation of platelet and vascular cells after proteolytic cleavage of its extracellular N terminus by thrombin.
21550978	3	71	theme	epithelial	632:641	arg1	cells					643:647	epithelial cells	632:647	epithelial cells (Kirsten murine sarcoma virus-transformed rat kidney cells and CHO cells)	632:721	In this study, epitope-tagged wild-type human PAR(1) (hPAR(1)) and a panel of N-linked glycosylation-deficient mutant receptors were permanently expressed in epithelial cells (Kirsten murine sarcoma virus-transformed rat kidney cells and CHO cells).
21550978	3	72	theme	receptors	592:600	arg1	panel					543:547	a panel	541:547	a panel of N-linked glycosylation-deficient mutant receptors	541:600	In this study, epitope-tagged wild-type human PAR(1) (hPAR(1)) and a panel of N-linked glycosylation-deficient mutant receptors were permanently expressed in epithelial cells (Kirsten murine sarcoma virus-transformed rat kidney cells and CHO cells).
21550978	3	72	theme	receptors	592:600	arg1	hPAR					528:531	hPAR(1)	528:534	hPAR(1)	528:534	In this study, epitope-tagged wild-type human PAR(1) (hPAR(1)) and a panel of N-linked glycosylation-deficient mutant receptors were permanently expressed in epithelial cells (Kirsten murine sarcoma virus-transformed rat kidney cells and CHO cells).
21550978	3	72	theme	receptors	592:600	arg1	PAR					520:522	epitope-tagged wild-type human PAR(1)	489:525	epitope-tagged wild-type human PAR(1) (hPAR(1))	489:535	In this study, epitope-tagged wild-type human PAR(1) (hPAR(1)) and a panel of N-linked glycosylation-deficient mutant receptors were permanently expressed in epithelial cells (Kirsten murine sarcoma virus-transformed rat kidney cells and CHO cells).
21550978	7	73	theme	receptor	1549:1556	arg1	expression					1571:1580	optimal receptor cell surface expression	1541:1580	optimal receptor cell surface expression	1541:1580	Removing these N-linked glycosylation sequons affected hPAR(1) cell surface expression to varying degrees, and N-linked glycosylation at extracellular loop 2 (especially Asn(250)) of hPAR(1) is essential for optimal receptor cell surface expression and receptor stability.
21550978	2	74	theme	other	344:348	arg1	proteinases					350:360	other proteinases	344:360	other proteinases	344:360	In pathological situations, other proteinases may be generated in the circulation and might modify the responses of PAR(1) by cleaving extracellular domains.
21550978	5	75	from	glycosylation	897:909	arg1	terminus					920:927	the N terminus	914:927	the N terminus of hPAR(1) downstream of the tethered ligand (especially Asn(75))	914:993	We reported for the first time that glycosylation in the N terminus of hPAR(1) downstream of the tethered ligand (especially Asn(75)) governs receptor disarming to trypsin, thermolysin, and the neutrophil proteinases elastase and proteinase 3 but not cathepsin G.
21550978	4	76	theme	N-linked	753:760	arg1	glycosylation					762:774	N-linked glycosylation	753:774	N-linked glycosylation	753:774	We have analyzed the role of N-linked glycosylation in regulating proteinase activation/disarming and cell global expression of hPAR(1).
21550978	3	77	theme	N-linked	552:559	arg1	receptors					592:600	N-linked glycosylation-deficient mutant receptors	552:600	N-linked glycosylation-deficient mutant receptors	552:600	In this study, epitope-tagged wild-type human PAR(1) (hPAR(1)) and a panel of N-linked glycosylation-deficient mutant receptors were permanently expressed in epithelial cells (Kirsten murine sarcoma virus-transformed rat kidney cells and CHO cells).
21550978	7	78	theme	cell	1558:1561	arg1	expression					1571:1580	optimal receptor cell surface expression	1541:1580	optimal receptor cell surface expression	1541:1580	Removing these N-linked glycosylation sequons affected hPAR(1) cell surface expression to varying degrees, and N-linked glycosylation at extracellular loop 2 (especially Asn(250)) of hPAR(1) is essential for optimal receptor cell surface expression and receptor stability.
21550978	1	79	theme	proteolytic	250:260	arg1	cleavage					262:269	proteolytic cleavage	250:269	proteolytic cleavage of its extracellular N terminus by thrombin	250:313	Proteinase-activated receptor 1 (PAR(1)) induces activation of platelet and vascular cells after proteolytic cleavage of its extracellular N terminus by thrombin.
21550978	4	80	gly	glycosylation	762:774	arg1	hPAR					852:855	hPAR(1)	852:858	hPAR(1)	852:858	We have analyzed the role of N-linked glycosylation in regulating proteinase activation/disarming and cell global expression of hPAR(1).
21550978	3	81	theme	virus-transformed	673:689	arg1	cells					702:706	Kirsten murine sarcoma virus-transformed rat kidney cells	650:706	Kirsten murine sarcoma virus-transformed rat kidney cells	650:706	In this study, epitope-tagged wild-type human PAR(1) (hPAR(1)) and a panel of N-linked glycosylation-deficient mutant receptors were permanently expressed in epithelial cells (Kirsten murine sarcoma virus-transformed rat kidney cells and CHO cells).
21550978	3	82	theme	glycosylation-deficient	561:583	arg1	receptors					592:600	N-linked glycosylation-deficient mutant receptors	552:600	N-linked glycosylation-deficient mutant receptors	552:600	In this study, epitope-tagged wild-type human PAR(1) (hPAR(1)) and a panel of N-linked glycosylation-deficient mutant receptors were permanently expressed in epithelial cells (Kirsten murine sarcoma virus-transformed rat kidney cells and CHO cells).
21550978	6	83	gly	sialylated	1183:1192	arg1	hPAR					1138:1141	hPAR(1)	1138:1144	hPAR(1)	1138:1144	In addition, hPAR(1) is heavily N-linked glycosylated and sialylated in epithelial cell lines, and glycosylation occurs at all five consensus sites, namely, Asn(35), Asn(62), Asn(75), Asn(250), and Asn(259).
21550978	5	84	gly	glycosylation	897:909	arg1	terminus					920:927	the N terminus	914:927	the N terminus of hPAR(1) downstream of the tethered ligand (especially Asn(75))	914:993	We reported for the first time that glycosylation in the N terminus of hPAR(1) downstream of the tethered ligand (especially Asn(75)) governs receptor disarming to trypsin, thermolysin, and the neutrophil proteinases elastase and proteinase 3 but not cathepsin G.
21053369	6	0	theme	deglycosylated	921:934	arg1	forms					936:940	their corresponding deglycosylated forms	901:940	their corresponding deglycosylated forms in each collected HPLC fraction	901:972	Both the glycopeptides and their corresponding deglycosylated forms in each collected HPLC fraction were studied by liquid chromatography-tandem mass spectrometry (LC-MS/MS) (LTQ-Orbitrap) for glycosylation site profiling.
21053369	4	1	theme	glycosylation	591:603	arg1	occupancy					605:613	glycosylation occupancy	591:613	glycosylation occupancy of each site	591:626	In this work, glycosylation profiles of soluble recombinant human IL-23r (rhIL-23r) were established using mass spectrometry (MS), which included defining glycosylation sites, degree of glycosylation occupancy of each site and structure of attached oligosaccharides.
21053369	7	2	theme	dissociation	1165:1176	arg1	fragmentation					1184:1196	collision-induced dissociation (CID) fragmentation	1147:1196	collision-induced dissociation (CID) fragmentation of target glycopeptides in combination with accurate mass measurement	1147:1266	The attached glycan structures were elucidated by collision-induced dissociation (CID) fragmentation of target glycopeptides in combination with accurate mass measurement.
21053369	4	3	theme	glycosylation	419:431	arg1	profiles					433:440	glycosylation profiles	419:440	glycosylation profiles of soluble recombinant human IL-23r (rhIL-23r)	419:487	In this work, glycosylation profiles of soluble recombinant human IL-23r (rhIL-23r) were established using mass spectrometry (MS), which included defining glycosylation sites, degree of glycosylation occupancy of each site and structure of attached oligosaccharides.
21053369	6	4	from	glycopeptides	883:895	arg1	fraction					965:972	each collected HPLC fraction	945:972	each collected HPLC fraction	945:972	Both the glycopeptides and their corresponding deglycosylated forms in each collected HPLC fraction were studied by liquid chromatography-tandem mass spectrometry (LC-MS/MS) (LTQ-Orbitrap) for glycosylation site profiling.
21053369	0	5	theme	Glycosylation	0:12	arg1	analysis					14:21	Glycosylation analysis	0:21	Glycosylation analysis of interleukin-23 receptor: elucidation of glycosylation sites and characterization of attached glycan structures.	0:136	Glycosylation analysis of interleukin-23 receptor: elucidation of glycosylation sites and characterization of attached glycan structures.
21053369	13	6	located	observed	1784:1791	arg2	glycans					1766:1772	hybrid type glycans	1754:1772	hybrid type glycans	1754:1772	High mannose and hybrid type glycans were only observed on Asn157.
21053369	13	6	located	observed	1784:1791	arg2	mannose					1742:1748	High mannose	1737:1748	High mannose	1737:1748	High mannose and hybrid type glycans were only observed on Asn157.
21053369	13	6	located	observed	1784:1791	arg1	Asn157					1796:1801	Asn157	1796:1801	Asn157	1796:1801	High mannose and hybrid type glycans were only observed on Asn157.
21053369	12	7	theme	tetra-antennary	1668:1682	arg1	structures					1697:1706	tetra-antennary complex type structures	1668:1706	tetra-antennary complex type structures	1668:1706	Most of them were bi-, tri- or tetra-antennary complex type structures with fucose and sialic acid.
21053369	13	8	theme	type	1761:1764	arg1	glycans					1766:1772	hybrid type glycans	1754:1772	hybrid type glycans	1754:1772	High mannose and hybrid type glycans were only observed on Asn157.
21053369	7	9	theme	glycan	1110:1115	arg1	structures					1117:1126	The attached glycan structures	1097:1126	The attached glycan structures	1097:1126	The attached glycan structures were elucidated by collision-induced dissociation (CID) fragmentation of target glycopeptides in combination with accurate mass measurement.
21053369	1	10	theme	central	192:198	arg1	cytokine					180:187	a heterodimeric cytokine	164:187	a heterodimeric cytokine	164:187	Interleukin-23 (IL-23) is a heterodimeric cytokine, a central factor in chronic/autoimmune inflammation.
21053369	1	10	theme	central	192:198	arg1	factor					200:205	a central factor	190:205	a central factor in chronic/autoimmune inflammation	190:240	Interleukin-23 (IL-23) is a heterodimeric cytokine, a central factor in chronic/autoimmune inflammation.
21053369	12	11	theme	type	1692:1695	arg1	structures					1697:1706	tetra-antennary complex type structures	1668:1706	tetra-antennary complex type structures	1668:1706	Most of them were bi-, tri- or tetra-antennary complex type structures with fucose and sialic acid.
21053369	4	12	theme	attached	645:652	arg1	oligosaccharides					654:669	attached oligosaccharides	645:669	attached oligosaccharides	645:669	In this work, glycosylation profiles of soluble recombinant human IL-23r (rhIL-23r) were established using mass spectrometry (MS), which included defining glycosylation sites, degree of glycosylation occupancy of each site and structure of attached oligosaccharides.
21053369	14	13	theme	IL-23r	1839:1844	arg1	glycosylation					1846:1858	IL-23r glycosylation	1839:1858	IL-23r glycosylation	1839:1858	The structural characterization on IL-23r glycosylation provides useful information for better understanding of the biological function of IL-23r.
21053369	4	14	theme	IL-23r	471:476	arg1	profiles					433:440	glycosylation profiles	419:440	glycosylation profiles of soluble recombinant human IL-23r (rhIL-23r)	419:487	In this work, glycosylation profiles of soluble recombinant human IL-23r (rhIL-23r) were established using mass spectrometry (MS), which included defining glycosylation sites, degree of glycosylation occupancy of each site and structure of attached oligosaccharides.
21053369	7	15	with	combination	1225:1235	arg1	measurement					1256:1266	accurate mass measurement	1242:1266	accurate mass measurement	1242:1266	The attached glycan structures were elucidated by collision-induced dissociation (CID) fragmentation of target glycopeptides in combination with accurate mass measurement.
21053369	10	16	theme	LysC	1576:1579	arg1	digestion					1581:1589	LysC digestion	1576:1589	LysC digestion	1576:1589	Those two sites were 88% and 45% occupied by estimation from trypsin digestion and were 55% and 42% occupied from LysC digestion.
21053369	5	17	theme	MS	813:814	arg1	instrument					816:825	a triple quadrupole MS instrument	793:825	a triple quadrupole MS instrument to locate the retention time of glycopeptides	793:871	Specifically, precursor ion scan of oxonium ion protonated N-acetylglucosamine (GlcNAc(+)) (m/z 204) was performed using a triple quadrupole MS instrument to locate the retention time of glycopeptides.
21053369	4	18	gly	glycosylation	560:572	arg1	occupancy					605:613	glycosylation occupancy	591:613	glycosylation occupancy of each site	591:626	In this work, glycosylation profiles of soluble recombinant human IL-23r (rhIL-23r) were established using mass spectrometry (MS), which included defining glycosylation sites, degree of glycosylation occupancy of each site and structure of attached oligosaccharides.
21053369	4	18	gly	glycosylation	560:572	arg1	oligosaccharides					654:669	attached oligosaccharides	645:669	attached oligosaccharides	645:669	In this work, glycosylation profiles of soluble recombinant human IL-23r (rhIL-23r) were established using mass spectrometry (MS), which included defining glycosylation sites, degree of glycosylation occupancy of each site and structure of attached oligosaccharides.
21053369	4	18	gly	glycosylation	560:572	arg2	sites					574:578	glycosylation sites	560:578	glycosylation sites	560:578	In this work, glycosylation profiles of soluble recombinant human IL-23r (rhIL-23r) were established using mass spectrometry (MS), which included defining glycosylation sites, degree of glycosylation occupancy of each site and structure of attached oligosaccharides.
21053369	4	18	gly	glycosylation	560:572	arg2	oligosaccharides					654:669	attached oligosaccharides	645:669	attached oligosaccharides	645:669	In this work, glycosylation profiles of soluble recombinant human IL-23r (rhIL-23r) were established using mass spectrometry (MS), which included defining glycosylation sites, degree of glycosylation occupancy of each site and structure of attached oligosaccharides.
21053369	4	18	gly	glycosylation	560:572	arg2	occupancy					605:613	glycosylation occupancy	591:613	glycosylation occupancy of each site	591:626	In this work, glycosylation profiles of soluble recombinant human IL-23r (rhIL-23r) were established using mass spectrometry (MS), which included defining glycosylation sites, degree of glycosylation occupancy of each site and structure of attached oligosaccharides.
21053369	5	19	theme	retention	841:849	arg1	time					851:854	the retention time	837:854	the retention time of glycopeptides	837:871	Specifically, precursor ion scan of oxonium ion protonated N-acetylglucosamine (GlcNAc(+)) (m/z 204) was performed using a triple quadrupole MS instrument to locate the retention time of glycopeptides.
21053369	8	20	theme	glycosylation	1275:1287	arg1	sites					1289:1293	Eight glycosylation sites	1269:1293	Eight glycosylation sites	1269:1293	Eight glycosylation sites were identified on IL-23r (Asn24, Asn209, Asn239, Asn157, Asn118, Asn250, Asn58 and Asn6).
21053369	6	21	theme	collected	950:958	arg1	fraction					965:972	each collected HPLC fraction	945:972	each collected HPLC fraction	945:972	Both the glycopeptides and their corresponding deglycosylated forms in each collected HPLC fraction were studied by liquid chromatography-tandem mass spectrometry (LC-MS/MS) (LTQ-Orbitrap) for glycosylation site profiling.
21053369	1	22	from	factor	200:205	arg1	inflammation					229:240	chronic/autoimmune inflammation	210:240	chronic/autoimmune inflammation	210:240	Interleukin-23 (IL-23) is a heterodimeric cytokine, a central factor in chronic/autoimmune inflammation.
21053369	5	23	theme	ion	716:718	arg1	N-acetylglucosamine					731:749	oxonium ion protonated N-acetylglucosamine	708:749	oxonium ion protonated N-acetylglucosamine (GlcNAc(+)) (m/z 204)	708:771	Specifically, precursor ion scan of oxonium ion protonated N-acetylglucosamine (GlcNAc(+)) (m/z 204) was performed using a triple quadrupole MS instrument to locate the retention time of glycopeptides.
21053369	5	23	theme	ion	716:718	arg1	GlcNAc					752:757	GlcNAc(+)	752:760	GlcNAc	752:757	Specifically, precursor ion scan of oxonium ion protonated N-acetylglucosamine (GlcNAc(+)) (m/z 204) was performed using a triple quadrupole MS instrument to locate the retention time of glycopeptides.
21053369	5	23	theme	ion	716:718	arg1	m/z					764:766	m/z 204	764:770	m/z 204	764:770	Specifically, precursor ion scan of oxonium ion protonated N-acetylglucosamine (GlcNAc(+)) (m/z 204) was performed using a triple quadrupole MS instrument to locate the retention time of glycopeptides.
21053369	4	24	theme	recombinant	453:463	arg1	rhIL-23r					479:486	rhIL-23r	479:486	rhIL-23r	479:486	In this work, glycosylation profiles of soluble recombinant human IL-23r (rhIL-23r) were established using mass spectrometry (MS), which included defining glycosylation sites, degree of glycosylation occupancy of each site and structure of attached oligosaccharides.
21053369	4	24	theme	recombinant	453:463	arg1	IL-23r					471:476	soluble recombinant human IL-23r	445:476	soluble recombinant human IL-23r (rhIL-23r)	445:487	In this work, glycosylation profiles of soluble recombinant human IL-23r (rhIL-23r) were established using mass spectrometry (MS), which included defining glycosylation sites, degree of glycosylation occupancy of each site and structure of attached oligosaccharides.
21053369	11	25	located	observed	1617:1624	arg1	IL-23r					1629:1634	IL-23r	1629:1634	IL-23r	1629:1634	Multiple glycoforms were observed in IL-23r.
21053369	11	25	located	observed	1617:1624	arg2	glycoforms					1601:1610	Multiple glycoforms	1592:1610	Multiple glycoforms	1592:1610	Multiple glycoforms were observed in IL-23r.
21053369	0	26	theme	glycosylation	66:78	arg1	sites					80:84	glycosylation sites	66:84	glycosylation sites	66:84	Glycosylation analysis of interleukin-23 receptor: elucidation of glycosylation sites and characterization of attached glycan structures.
21053369	1	27	theme	heterodimeric	166:178	arg1	cytokine					180:187	a heterodimeric cytokine	164:187	a heterodimeric cytokine	164:187	Interleukin-23 (IL-23) is a heterodimeric cytokine, a central factor in chronic/autoimmune inflammation.
21053369	1	27	theme	heterodimeric	166:178	arg1	Interleukin-23					138:151	Interleukin-23	138:151	Interleukin-23 (IL-23)	138:159	Interleukin-23 (IL-23) is a heterodimeric cytokine, a central factor in chronic/autoimmune inflammation.
21053369	1	27	theme	heterodimeric	166:178	arg1	factor					200:205	a central factor	190:205	a central factor in chronic/autoimmune inflammation	190:240	Interleukin-23 (IL-23) is a heterodimeric cytokine, a central factor in chronic/autoimmune inflammation.
21053369	6	28	theme	mass	1019:1022	arg1	LC-MS/MS					1038:1045	LC-MS/MS	1038:1045	LC-MS/MS	1038:1045	Both the glycopeptides and their corresponding deglycosylated forms in each collected HPLC fraction were studied by liquid chromatography-tandem mass spectrometry (LC-MS/MS) (LTQ-Orbitrap) for glycosylation site profiling.
21053369	6	28	theme	mass	1019:1022	arg1	LTQ-Orbitrap					1049:1060	LTQ-Orbitrap	1049:1060	LTQ-Orbitrap	1049:1060	Both the glycopeptides and their corresponding deglycosylated forms in each collected HPLC fraction were studied by liquid chromatography-tandem mass spectrometry (LC-MS/MS) (LTQ-Orbitrap) for glycosylation site profiling.
21053369	6	28	theme	mass	1019:1022	arg1	spectrometry					1024:1035	liquid chromatography-tandem mass spectrometry	990:1035	liquid chromatography-tandem mass spectrometry (LC-MS/MS) (LTQ-Orbitrap) for glycosylation site profiling	990:1094	Both the glycopeptides and their corresponding deglycosylated forms in each collected HPLC fraction were studied by liquid chromatography-tandem mass spectrometry (LC-MS/MS) (LTQ-Orbitrap) for glycosylation site profiling.
21053369	7	29	from	fragmentation	1184:1196	arg1	combination					1225:1235	combination	1225:1235	combination with accurate mass measurement	1225:1266	The attached glycan structures were elucidated by collision-induced dissociation (CID) fragmentation of target glycopeptides in combination with accurate mass measurement.
21053369	7	30	theme	mass	1251:1254	arg1	measurement					1256:1266	accurate mass measurement	1242:1266	accurate mass measurement	1242:1266	The attached glycan structures were elucidated by collision-induced dissociation (CID) fragmentation of target glycopeptides in combination with accurate mass measurement.
21053369	12	31	with	tri-	1660:1663	arg1	fucose					1713:1718	fucose	1713:1718	fucose	1713:1718	Most of them were bi-, tri- or tetra-antennary complex type structures with fucose and sialic acid.
21053369	12	31	with	tri-	1660:1663	arg1	acid					1731:1734	sialic acid	1724:1734	sialic acid	1724:1734	Most of them were bi-, tri- or tetra-antennary complex type structures with fucose and sialic acid.
21053369	6	32	theme	liquid	990:995	arg1	LC-MS/MS					1038:1045	LC-MS/MS	1038:1045	LC-MS/MS	1038:1045	Both the glycopeptides and their corresponding deglycosylated forms in each collected HPLC fraction were studied by liquid chromatography-tandem mass spectrometry (LC-MS/MS) (LTQ-Orbitrap) for glycosylation site profiling.
21053369	6	32	theme	liquid	990:995	arg1	LTQ-Orbitrap					1049:1060	LTQ-Orbitrap	1049:1060	LTQ-Orbitrap	1049:1060	Both the glycopeptides and their corresponding deglycosylated forms in each collected HPLC fraction were studied by liquid chromatography-tandem mass spectrometry (LC-MS/MS) (LTQ-Orbitrap) for glycosylation site profiling.
21053369	6	32	theme	liquid	990:995	arg1	spectrometry					1024:1035	liquid chromatography-tandem mass spectrometry	990:1035	liquid chromatography-tandem mass spectrometry (LC-MS/MS) (LTQ-Orbitrap) for glycosylation site profiling	990:1094	Both the glycopeptides and their corresponding deglycosylated forms in each collected HPLC fraction were studied by liquid chromatography-tandem mass spectrometry (LC-MS/MS) (LTQ-Orbitrap) for glycosylation site profiling.
21053369	3	33	theme	IL-23r	375:380	arg1	characterization					355:370	The structural characterization	340:370	The structural characterization of IL-23r	340:380	The structural characterization of IL-23r has not been reported.
21053369	0	34	theme	glycan	119:124	arg1	structures					126:135	attached glycan structures	110:135	attached glycan structures	110:135	Glycosylation analysis of interleukin-23 receptor: elucidation of glycosylation sites and characterization of attached glycan structures.
21053369	12	35	with	bi-	1655:1657	arg1	fucose					1713:1718	fucose	1713:1718	fucose	1713:1718	Most of them were bi-, tri- or tetra-antennary complex type structures with fucose and sialic acid.
21053369	12	35	with	bi-	1655:1657	arg1	acid					1731:1734	sialic acid	1724:1734	sialic acid	1724:1734	Most of them were bi-, tri- or tetra-antennary complex type structures with fucose and sialic acid.
21053369	5	36	theme	quadrupole	802:811	arg1	instrument					816:825	a triple quadrupole MS instrument	793:825	a triple quadrupole MS instrument to locate the retention time of glycopeptides	793:871	Specifically, precursor ion scan of oxonium ion protonated N-acetylglucosamine (GlcNAc(+)) (m/z 204) was performed using a triple quadrupole MS instrument to locate the retention time of glycopeptides.
21053369	4	37	gly	occupancy	605:613	arg2	site					623:626	each site	618:626	each site	618:626	In this work, glycosylation profiles of soluble recombinant human IL-23r (rhIL-23r) were established using mass spectrometry (MS), which included defining glycosylation sites, degree of glycosylation occupancy of each site and structure of attached oligosaccharides.
21053369	8	38	dep	identified	1300:1309	arg1	Asn58					1369:1373	Asn58	1369:1373	Asn58	1369:1373	Eight glycosylation sites were identified on IL-23r (Asn24, Asn209, Asn239, Asn157, Asn118, Asn250, Asn58 and Asn6).
21053369	8	38	dep	identified	1300:1309	arg1	Asn250					1361:1366	Asn250	1361:1366	Asn250	1361:1366	Eight glycosylation sites were identified on IL-23r (Asn24, Asn209, Asn239, Asn157, Asn118, Asn250, Asn58 and Asn6).
21053369	8	38	dep	identified	1300:1309	arg1	Asn209					1329:1334	Asn209	1329:1334	Asn209	1329:1334	Eight glycosylation sites were identified on IL-23r (Asn24, Asn209, Asn239, Asn157, Asn118, Asn250, Asn58 and Asn6).
21053369	8	38	dep	identified	1300:1309	arg1	Asn6					1379:1382	Asn6	1379:1382	Asn6	1379:1382	Eight glycosylation sites were identified on IL-23r (Asn24, Asn209, Asn239, Asn157, Asn118, Asn250, Asn58 and Asn6).
21053369	8	38	dep	identified	1300:1309	arg1	Asn157					1345:1350	Asn157	1345:1350	Asn157	1345:1350	Eight glycosylation sites were identified on IL-23r (Asn24, Asn209, Asn239, Asn157, Asn118, Asn250, Asn58 and Asn6).
21053369	6	39	theme	site	1081:1084	arg1	profiling					1086:1094	glycosylation site profiling	1067:1094	glycosylation site profiling	1067:1094	Both the glycopeptides and their corresponding deglycosylated forms in each collected HPLC fraction were studied by liquid chromatography-tandem mass spectrometry (LC-MS/MS) (LTQ-Orbitrap) for glycosylation site profiling.
21053369	4	40	theme	glycosylation	560:572	arg1	occupancy					605:613	glycosylation occupancy	591:613	glycosylation occupancy of each site	591:626	In this work, glycosylation profiles of soluble recombinant human IL-23r (rhIL-23r) were established using mass spectrometry (MS), which included defining glycosylation sites, degree of glycosylation occupancy of each site and structure of attached oligosaccharides.
21053369	4	40	theme	glycosylation	560:572	arg1	sites					574:578	glycosylation sites	560:578	glycosylation sites	560:578	In this work, glycosylation profiles of soluble recombinant human IL-23r (rhIL-23r) were established using mass spectrometry (MS), which included defining glycosylation sites, degree of glycosylation occupancy of each site and structure of attached oligosaccharides.
21053369	4	40	theme	glycosylation	560:572	arg1	oligosaccharides					654:669	attached oligosaccharides	645:669	attached oligosaccharides	645:669	In this work, glycosylation profiles of soluble recombinant human IL-23r (rhIL-23r) were established using mass spectrometry (MS), which included defining glycosylation sites, degree of glycosylation occupancy of each site and structure of attached oligosaccharides.
21053369	7	41	theme	target	1201:1206	arg1	glycopeptides					1208:1220	target glycopeptides	1201:1220	target glycopeptides	1201:1220	The attached glycan structures were elucidated by collision-induced dissociation (CID) fragmentation of target glycopeptides in combination with accurate mass measurement.
21053369	0	42	theme	receptor	41:48	arg1	analysis					14:21	Glycosylation analysis	0:21	Glycosylation analysis of interleukin-23 receptor: elucidation of glycosylation sites and characterization of attached glycan structures.	0:136	Glycosylation analysis of interleukin-23 receptor: elucidation of glycosylation sites and characterization of attached glycan structures.
21053369	14	43	theme	biological	1920:1929	arg1	function					1931:1938	the biological function	1916:1938	the biological function of IL-23r	1916:1948	The structural characterization on IL-23r glycosylation provides useful information for better understanding of the biological function of IL-23r.
21053369	10	44	theme	trypsin	1523:1529	arg1	digestion					1531:1539	trypsin digestion	1523:1539	trypsin digestion	1523:1539	Those two sites were 88% and 45% occupied by estimation from trypsin digestion and were 55% and 42% occupied from LysC digestion.
21053369	9	45	theme	glycosylation	1398:1410	arg1	sites					1412:1416	the glycosylation sites	1394:1416	the glycosylation sites	1394:1416	Most of the glycosylation sites were > 95% occupied except Asn250 and Asn6.
21053369	14	46	theme	better	1892:1897	arg1	understanding					1899:1911	better understanding	1892:1911	better understanding of the biological function of IL-23r	1892:1948	The structural characterization on IL-23r glycosylation provides useful information for better understanding of the biological function of IL-23r.
21053369	6	47	from	forms	936:940	arg1	fraction					965:972	each collected HPLC fraction	945:972	each collected HPLC fraction	945:972	Both the glycopeptides and their corresponding deglycosylated forms in each collected HPLC fraction were studied by liquid chromatography-tandem mass spectrometry (LC-MS/MS) (LTQ-Orbitrap) for glycosylation site profiling.
21053369	7	48	theme	collision-induced	1147:1163	arg1	CID					1179:1181	CID	1179:1181	CID	1179:1181	The attached glycan structures were elucidated by collision-induced dissociation (CID) fragmentation of target glycopeptides in combination with accurate mass measurement.
21053369	7	48	theme	collision-induced	1147:1163	arg1	dissociation					1165:1176	collision-induced dissociation	1147:1176	collision-induced dissociation (CID) fragmentation of target glycopeptides in combination with accurate mass measurement	1147:1266	The attached glycan structures were elucidated by collision-induced dissociation (CID) fragmentation of target glycopeptides in combination with accurate mass measurement.
21053369	6	49	theme	corresponding	907:919	arg1	forms					936:940	their corresponding deglycosylated forms	901:940	their corresponding deglycosylated forms in each collected HPLC fraction	901:972	Both the glycopeptides and their corresponding deglycosylated forms in each collected HPLC fraction were studied by liquid chromatography-tandem mass spectrometry (LC-MS/MS) (LTQ-Orbitrap) for glycosylation site profiling.
21053369	11	50	theme	Multiple	1592:1599	arg1	glycoforms					1601:1610	Multiple glycoforms	1592:1610	Multiple glycoforms	1592:1610	Multiple glycoforms were observed in IL-23r.
21053369	5	51	theme	precursor	686:694	arg1	ion					696:698	precursor ion	686:698	precursor ion scan of oxonium ion protonated N-acetylglucosamine (GlcNAc(+)) (m/z 204)	686:771	Specifically, precursor ion scan of oxonium ion protonated N-acetylglucosamine (GlcNAc(+)) (m/z 204) was performed using a triple quadrupole MS instrument to locate the retention time of glycopeptides.
21053369	5	52	gly	glycopeptides	859:871	arg2	glycopeptides					859:871	glycopeptides	859:871	glycopeptides	859:871	Specifically, precursor ion scan of oxonium ion protonated N-acetylglucosamine (GlcNAc(+)) (m/z 204) was performed using a triple quadrupole MS instrument to locate the retention time of glycopeptides.
21053369	12	53	theme	sialic	1724:1729	arg1	acid					1731:1734	sialic acid	1724:1734	sialic acid	1724:1734	Most of them were bi-, tri- or tetra-antennary complex type structures with fucose and sialic acid.
21053369	4	54	theme	occupancy	605:613	arg1	occupancy					605:613	glycosylation occupancy	591:613	glycosylation occupancy of each site	591:626	In this work, glycosylation profiles of soluble recombinant human IL-23r (rhIL-23r) were established using mass spectrometry (MS), which included defining glycosylation sites, degree of glycosylation occupancy of each site and structure of attached oligosaccharides.
21053369	4	54	theme	occupancy	605:613	arg1	sites					574:578	glycosylation sites	560:578	glycosylation sites	560:578	In this work, glycosylation profiles of soluble recombinant human IL-23r (rhIL-23r) were established using mass spectrometry (MS), which included defining glycosylation sites, degree of glycosylation occupancy of each site and structure of attached oligosaccharides.
21053369	4	54	theme	occupancy	605:613	arg1	oligosaccharides					654:669	attached oligosaccharides	645:669	attached oligosaccharides	645:669	In this work, glycosylation profiles of soluble recombinant human IL-23r (rhIL-23r) were established using mass spectrometry (MS), which included defining glycosylation sites, degree of glycosylation occupancy of each site and structure of attached oligosaccharides.
21053369	4	54	theme	occupancy	605:613	arg1	structure					632:640	structure	632:640	structure of attached oligosaccharides	632:669	In this work, glycosylation profiles of soluble recombinant human IL-23r (rhIL-23r) were established using mass spectrometry (MS), which included defining glycosylation sites, degree of glycosylation occupancy of each site and structure of attached oligosaccharides.
21053369	4	54	theme	occupancy	605:613	arg1	degree					581:586	degree	581:586	degree of glycosylation occupancy of each site	581:626	In this work, glycosylation profiles of soluble recombinant human IL-23r (rhIL-23r) were established using mass spectrometry (MS), which included defining glycosylation sites, degree of glycosylation occupancy of each site and structure of attached oligosaccharides.
21053369	13	55	theme	High	1737:1740	arg1	mannose					1742:1748	High mannose	1737:1748	High mannose	1737:1748	High mannose and hybrid type glycans were only observed on Asn157.
21053369	14	56	theme	useful	1869:1874	arg1	information					1876:1886	useful information	1869:1886	useful information for better understanding of the biological function of IL-23r	1869:1948	The structural characterization on IL-23r glycosylation provides useful information for better understanding of the biological function of IL-23r.
21053369	12	57	theme	complex	1684:1690	arg1	structures					1697:1706	tetra-antennary complex type structures	1668:1706	tetra-antennary complex type structures	1668:1706	Most of them were bi-, tri- or tetra-antennary complex type structures with fucose and sialic acid.
21053369	7	58	theme	attached	1101:1108	arg1	structures					1117:1126	The attached glycan structures	1097:1126	The attached glycan structures	1097:1126	The attached glycan structures were elucidated by collision-induced dissociation (CID) fragmentation of target glycopeptides in combination with accurate mass measurement.
21053369	5	59	theme	glycopeptides	859:871	arg1	time					851:854	the retention time	837:854	the retention time of glycopeptides	837:871	Specifically, precursor ion scan of oxonium ion protonated N-acetylglucosamine (GlcNAc(+)) (m/z 204) was performed using a triple quadrupole MS instrument to locate the retention time of glycopeptides.
21053369	5	60	theme	protonated	720:729	arg1	N-acetylglucosamine					731:749	oxonium ion protonated N-acetylglucosamine	708:749	oxonium ion protonated N-acetylglucosamine (GlcNAc(+)) (m/z 204)	708:771	Specifically, precursor ion scan of oxonium ion protonated N-acetylglucosamine (GlcNAc(+)) (m/z 204) was performed using a triple quadrupole MS instrument to locate the retention time of glycopeptides.
21053369	5	60	theme	protonated	720:729	arg1	GlcNAc					752:757	GlcNAc(+)	752:760	GlcNAc	752:757	Specifically, precursor ion scan of oxonium ion protonated N-acetylglucosamine (GlcNAc(+)) (m/z 204) was performed using a triple quadrupole MS instrument to locate the retention time of glycopeptides.
21053369	5	60	theme	protonated	720:729	arg1	m/z					764:766	m/z 204	764:770	m/z 204	764:770	Specifically, precursor ion scan of oxonium ion protonated N-acetylglucosamine (GlcNAc(+)) (m/z 204) was performed using a triple quadrupole MS instrument to locate the retention time of glycopeptides.
21053369	8	61	gly	glycosylation	1275:1287	arg2	sites					1289:1293	Eight glycosylation sites	1269:1293	Eight glycosylation sites	1269:1293	Eight glycosylation sites were identified on IL-23r (Asn24, Asn209, Asn239, Asn157, Asn118, Asn250, Asn58 and Asn6).
21053369	8	61	gly	glycosylation	1275:1287	arg2	Eight					1269:1273	Eight	1269:1273	Eight	1269:1273	Eight glycosylation sites were identified on IL-23r (Asn24, Asn209, Asn239, Asn157, Asn118, Asn250, Asn58 and Asn6).
21053369	14	62	from	characterization	1819:1834	arg1	glycosylation					1846:1858	IL-23r glycosylation	1839:1858	IL-23r glycosylation	1839:1858	The structural characterization on IL-23r glycosylation provides useful information for better understanding of the biological function of IL-23r.
21053369	1	63	theme	chronic/autoimmune	210:227	arg1	inflammation					229:240	chronic/autoimmune inflammation	210:240	chronic/autoimmune inflammation	210:240	Interleukin-23 (IL-23) is a heterodimeric cytokine, a central factor in chronic/autoimmune inflammation.
21053369	6	64	theme	HPLC	960:963	arg1	fraction					965:972	each collected HPLC fraction	945:972	each collected HPLC fraction	945:972	Both the glycopeptides and their corresponding deglycosylated forms in each collected HPLC fraction were studied by liquid chromatography-tandem mass spectrometry (LC-MS/MS) (LTQ-Orbitrap) for glycosylation site profiling.
21053369	4	65	theme	oligosaccharides	654:669	arg1	occupancy					605:613	glycosylation occupancy	591:613	glycosylation occupancy of each site	591:626	In this work, glycosylation profiles of soluble recombinant human IL-23r (rhIL-23r) were established using mass spectrometry (MS), which included defining glycosylation sites, degree of glycosylation occupancy of each site and structure of attached oligosaccharides.
21053369	4	65	theme	oligosaccharides	654:669	arg1	sites					574:578	glycosylation sites	560:578	glycosylation sites	560:578	In this work, glycosylation profiles of soluble recombinant human IL-23r (rhIL-23r) were established using mass spectrometry (MS), which included defining glycosylation sites, degree of glycosylation occupancy of each site and structure of attached oligosaccharides.
21053369	4	65	theme	oligosaccharides	654:669	arg1	oligosaccharides					654:669	attached oligosaccharides	645:669	attached oligosaccharides	645:669	In this work, glycosylation profiles of soluble recombinant human IL-23r (rhIL-23r) were established using mass spectrometry (MS), which included defining glycosylation sites, degree of glycosylation occupancy of each site and structure of attached oligosaccharides.
21053369	4	65	theme	oligosaccharides	654:669	arg1	structure					632:640	structure	632:640	structure of attached oligosaccharides	632:669	In this work, glycosylation profiles of soluble recombinant human IL-23r (rhIL-23r) were established using mass spectrometry (MS), which included defining glycosylation sites, degree of glycosylation occupancy of each site and structure of attached oligosaccharides.
21053369	4	65	theme	oligosaccharides	654:669	arg1	degree					581:586	degree	581:586	degree of glycosylation occupancy of each site	581:626	In this work, glycosylation profiles of soluble recombinant human IL-23r (rhIL-23r) were established using mass spectrometry (MS), which included defining glycosylation sites, degree of glycosylation occupancy of each site and structure of attached oligosaccharides.
21053369	7	66	theme	accurate	1242:1249	arg1	measurement					1256:1266	accurate mass measurement	1242:1266	accurate mass measurement	1242:1266	The attached glycan structures were elucidated by collision-induced dissociation (CID) fragmentation of target glycopeptides in combination with accurate mass measurement.
21053369	14	67	theme	structural	1808:1817	arg1	characterization					1819:1834	The structural characterization	1804:1834	The structural characterization on IL-23r glycosylation	1804:1858	The structural characterization on IL-23r glycosylation provides useful information for better understanding of the biological function of IL-23r.
21053369	4	68	theme	soluble	445:451	arg1	rhIL-23r					479:486	rhIL-23r	479:486	rhIL-23r	479:486	In this work, glycosylation profiles of soluble recombinant human IL-23r (rhIL-23r) were established using mass spectrometry (MS), which included defining glycosylation sites, degree of glycosylation occupancy of each site and structure of attached oligosaccharides.
21053369	4	68	theme	soluble	445:451	arg1	IL-23r					471:476	soluble recombinant human IL-23r	445:476	soluble recombinant human IL-23r (rhIL-23r)	445:487	In this work, glycosylation profiles of soluble recombinant human IL-23r (rhIL-23r) were established using mass spectrometry (MS), which included defining glycosylation sites, degree of glycosylation occupancy of each site and structure of attached oligosaccharides.
21053369	6	69	gly	glycopeptides	883:895	arg2	glycopeptides					883:895	the glycopeptides	879:895	the glycopeptides	879:895	Both the glycopeptides and their corresponding deglycosylated forms in each collected HPLC fraction were studied by liquid chromatography-tandem mass spectrometry (LC-MS/MS) (LTQ-Orbitrap) for glycosylation site profiling.
21053369	5	70	theme	oxonium	708:714	arg1	N-acetylglucosamine					731:749	oxonium ion protonated N-acetylglucosamine	708:749	oxonium ion protonated N-acetylglucosamine (GlcNAc(+)) (m/z 204)	708:771	Specifically, precursor ion scan of oxonium ion protonated N-acetylglucosamine (GlcNAc(+)) (m/z 204) was performed using a triple quadrupole MS instrument to locate the retention time of glycopeptides.
21053369	5	70	theme	oxonium	708:714	arg1	GlcNAc					752:757	GlcNAc(+)	752:760	GlcNAc	752:757	Specifically, precursor ion scan of oxonium ion protonated N-acetylglucosamine (GlcNAc(+)) (m/z 204) was performed using a triple quadrupole MS instrument to locate the retention time of glycopeptides.
21053369	5	70	theme	oxonium	708:714	arg1	m/z					764:766	m/z 204	764:770	m/z 204	764:770	Specifically, precursor ion scan of oxonium ion protonated N-acetylglucosamine (GlcNAc(+)) (m/z 204) was performed using a triple quadrupole MS instrument to locate the retention time of glycopeptides.
21053369	4	71	theme	human	465:469	arg1	rhIL-23r					479:486	rhIL-23r	479:486	rhIL-23r	479:486	In this work, glycosylation profiles of soluble recombinant human IL-23r (rhIL-23r) were established using mass spectrometry (MS), which included defining glycosylation sites, degree of glycosylation occupancy of each site and structure of attached oligosaccharides.
21053369	4	71	theme	human	465:469	arg1	IL-23r					471:476	soluble recombinant human IL-23r	445:476	soluble recombinant human IL-23r (rhIL-23r)	445:487	In this work, glycosylation profiles of soluble recombinant human IL-23r (rhIL-23r) were established using mass spectrometry (MS), which included defining glycosylation sites, degree of glycosylation occupancy of each site and structure of attached oligosaccharides.
21053369	0	72	theme	sites	80:84	arg1	characterization					90:105	characterization	90:105	characterization of attached glycan structures	90:135	Glycosylation analysis of interleukin-23 receptor: elucidation of glycosylation sites and characterization of attached glycan structures.
21053369	0	72	theme	sites	80:84	arg1	elucidation					51:61	elucidation	51:61	elucidation of glycosylation sites	51:84	Glycosylation analysis of interleukin-23 receptor: elucidation of glycosylation sites and characterization of attached glycan structures.
21053369	2	73	theme	heterodimeric	264:276	arg1	receptor					278:285	a heterodimeric receptor	262:285	a heterodimeric receptor	262:285	It signals through a heterodimeric receptor consisting of IL-23r, which is heavily glycosylated.
21053369	12	74	with	structures	1697:1706	arg1	fucose					1713:1718	fucose	1713:1718	fucose	1713:1718	Most of them were bi-, tri- or tetra-antennary complex type structures with fucose and sialic acid.
21053369	12	74	with	structures	1697:1706	arg1	acid					1731:1734	sialic acid	1724:1734	sialic acid	1724:1734	Most of them were bi-, tri- or tetra-antennary complex type structures with fucose and sialic acid.
21053369	4	75	gly	glycosylation	419:431	arg1	rhIL-23r					479:486	rhIL-23r	479:486	rhIL-23r	479:486	In this work, glycosylation profiles of soluble recombinant human IL-23r (rhIL-23r) were established using mass spectrometry (MS), which included defining glycosylation sites, degree of glycosylation occupancy of each site and structure of attached oligosaccharides.
21053369	4	75	gly	glycosylation	419:431	arg1	IL-23r					471:476	soluble recombinant human IL-23r	445:476	soluble recombinant human IL-23r (rhIL-23r)	445:487	In this work, glycosylation profiles of soluble recombinant human IL-23r (rhIL-23r) were established using mass spectrometry (MS), which included defining glycosylation sites, degree of glycosylation occupancy of each site and structure of attached oligosaccharides.
21053369	6	76	gly	deglycosylated	921:934	arg1	forms					936:940	their corresponding deglycosylated forms	901:940	their corresponding deglycosylated forms in each collected HPLC fraction	901:972	Both the glycopeptides and their corresponding deglycosylated forms in each collected HPLC fraction were studied by liquid chromatography-tandem mass spectrometry (LC-MS/MS) (LTQ-Orbitrap) for glycosylation site profiling.
21053369	3	77	theme	structural	344:353	arg1	characterization					355:370	The structural characterization	340:370	The structural characterization of IL-23r	340:380	The structural characterization of IL-23r has not been reported.
21053369	0	78	theme	attached	110:117	arg1	structures					126:135	attached glycan structures	110:135	attached glycan structures	110:135	Glycosylation analysis of interleukin-23 receptor: elucidation of glycosylation sites and characterization of attached glycan structures.
21053369	0	79	gly	glycosylation	66:78	arg2	sites					80:84	glycosylation sites	66:84	glycosylation sites	66:84	Glycosylation analysis of interleukin-23 receptor: elucidation of glycosylation sites and characterization of attached glycan structures.
21053369	6	80	theme	chromatography-tandem	997:1017	arg1	LC-MS/MS					1038:1045	LC-MS/MS	1038:1045	LC-MS/MS	1038:1045	Both the glycopeptides and their corresponding deglycosylated forms in each collected HPLC fraction were studied by liquid chromatography-tandem mass spectrometry (LC-MS/MS) (LTQ-Orbitrap) for glycosylation site profiling.
21053369	6	80	theme	chromatography-tandem	997:1017	arg1	LTQ-Orbitrap					1049:1060	LTQ-Orbitrap	1049:1060	LTQ-Orbitrap	1049:1060	Both the glycopeptides and their corresponding deglycosylated forms in each collected HPLC fraction were studied by liquid chromatography-tandem mass spectrometry (LC-MS/MS) (LTQ-Orbitrap) for glycosylation site profiling.
21053369	6	80	theme	chromatography-tandem	997:1017	arg1	spectrometry					1024:1035	liquid chromatography-tandem mass spectrometry	990:1035	liquid chromatography-tandem mass spectrometry (LC-MS/MS) (LTQ-Orbitrap) for glycosylation site profiling	990:1094	Both the glycopeptides and their corresponding deglycosylated forms in each collected HPLC fraction were studied by liquid chromatography-tandem mass spectrometry (LC-MS/MS) (LTQ-Orbitrap) for glycosylation site profiling.
21053369	0	81	theme	structures	126:135	arg1	characterization					90:105	characterization	90:105	characterization of attached glycan structures	90:135	Glycosylation analysis of interleukin-23 receptor: elucidation of glycosylation sites and characterization of attached glycan structures.
21053369	0	81	theme	structures	126:135	arg1	elucidation					51:61	elucidation	51:61	elucidation of glycosylation sites	51:84	Glycosylation analysis of interleukin-23 receptor: elucidation of glycosylation sites and characterization of attached glycan structures.
21053369	4	82	theme	mass	512:515	arg1	MS					531:532	MS	531:532	MS	531:532	In this work, glycosylation profiles of soluble recombinant human IL-23r (rhIL-23r) were established using mass spectrometry (MS), which included defining glycosylation sites, degree of glycosylation occupancy of each site and structure of attached oligosaccharides.
21053369	4	82	theme	mass	512:515	arg1	spectrometry					517:528	mass spectrometry	512:528	mass spectrometry (MS)	512:533	In this work, glycosylation profiles of soluble recombinant human IL-23r (rhIL-23r) were established using mass spectrometry (MS), which included defining glycosylation sites, degree of glycosylation occupancy of each site and structure of attached oligosaccharides.
21053369	5	83	theme	triple	795:800	arg1	instrument					816:825	a triple quadrupole MS instrument	793:825	a triple quadrupole MS instrument to locate the retention time of glycopeptides	793:871	Specifically, precursor ion scan of oxonium ion protonated N-acetylglucosamine (GlcNAc(+)) (m/z 204) was performed using a triple quadrupole MS instrument to locate the retention time of glycopeptides.
21053369	2	84	gly	glycosylated	326:337	arg1	receptor					278:285	a heterodimeric receptor	262:285	a heterodimeric receptor	262:285	It signals through a heterodimeric receptor consisting of IL-23r, which is heavily glycosylated.
21053369	5	85	dep	ion	696:698	arg1	scan					700:703	scan	700:703	scan of oxonium ion protonated N-acetylglucosamine (GlcNAc(+)) (m/z 204)	700:771	Specifically, precursor ion scan of oxonium ion protonated N-acetylglucosamine (GlcNAc(+)) (m/z 204) was performed using a triple quadrupole MS instrument to locate the retention time of glycopeptides.
21053369	0	86	theme	interleukin-23	26:39	arg1	receptor					41:48	interleukin-23 receptor	26:48	interleukin-23 receptor	26:48	Glycosylation analysis of interleukin-23 receptor: elucidation of glycosylation sites and characterization of attached glycan structures.
21053369	6	87	theme	glycosylation	1067:1079	arg1	profiling					1086:1094	glycosylation site profiling	1067:1094	glycosylation site profiling	1067:1094	Both the glycopeptides and their corresponding deglycosylated forms in each collected HPLC fraction were studied by liquid chromatography-tandem mass spectrometry (LC-MS/MS) (LTQ-Orbitrap) for glycosylation site profiling.
21053369	6	88	gly	glycosylation	1067:1079	arg2	profiling					1086:1094	glycosylation site profiling	1067:1094	glycosylation site profiling	1067:1094	Both the glycopeptides and their corresponding deglycosylated forms in each collected HPLC fraction were studied by liquid chromatography-tandem mass spectrometry (LC-MS/MS) (LTQ-Orbitrap) for glycosylation site profiling.
21053369	6	88	gly	glycosylation	1067:1079	arg2	site					1081:1084	glycosylation site profiling	1067:1094	glycosylation site profiling	1067:1094	Both the glycopeptides and their corresponding deglycosylated forms in each collected HPLC fraction were studied by liquid chromatography-tandem mass spectrometry (LC-MS/MS) (LTQ-Orbitrap) for glycosylation site profiling.
21053369	14	89	theme	IL-23r	1943:1948	arg1	function					1931:1938	the biological function	1916:1938	the biological function of IL-23r	1916:1948	The structural characterization on IL-23r glycosylation provides useful information for better understanding of the biological function of IL-23r.
21053369	14	90	theme	function	1931:1938	arg1	understanding					1899:1911	better understanding	1892:1911	better understanding of the biological function of IL-23r	1892:1948	The structural characterization on IL-23r glycosylation provides useful information for better understanding of the biological function of IL-23r.
21053369	9	91	gly	glycosylation	1398:1410	arg2	sites					1412:1416	the glycosylation sites	1394:1416	the glycosylation sites	1394:1416	Most of the glycosylation sites were > 95% occupied except Asn250 and Asn6.
21053369	10	92	from	digestion	1531:1539	arg1	estimation					1507:1516	estimation	1507:1516	estimation from trypsin digestion	1507:1539	Those two sites were 88% and 45% occupied by estimation from trypsin digestion and were 55% and 42% occupied from LysC digestion.
21053369	4	93	theme	site	623:626	arg1	occupancy					605:613	glycosylation occupancy	591:613	glycosylation occupancy of each site	591:626	In this work, glycosylation profiles of soluble recombinant human IL-23r (rhIL-23r) were established using mass spectrometry (MS), which included defining glycosylation sites, degree of glycosylation occupancy of each site and structure of attached oligosaccharides.
21053369	7	94	gly	glycopeptides	1208:1220	arg2	glycopeptides					1208:1220	target glycopeptides	1201:1220	target glycopeptides	1201:1220	The attached glycan structures were elucidated by collision-induced dissociation (CID) fragmentation of target glycopeptides in combination with accurate mass measurement.
21053369	0	95	dep	analysis	14:21	arg1	characterization					90:105	characterization	90:105	characterization of attached glycan structures	90:135	Glycosylation analysis of interleukin-23 receptor: elucidation of glycosylation sites and characterization of attached glycan structures.
21053369	0	95	dep	analysis	14:21	arg1	elucidation					51:61	elucidation	51:61	elucidation of glycosylation sites	51:84	Glycosylation analysis of interleukin-23 receptor: elucidation of glycosylation sites and characterization of attached glycan structures.
21053369	13	96	theme	hybrid	1754:1759	arg1	glycans					1766:1772	hybrid type glycans	1754:1772	hybrid type glycans	1754:1772	High mannose and hybrid type glycans were only observed on Asn157.
21053369	7	97	theme	glycopeptides	1208:1220	arg1	fragmentation					1184:1196	collision-induced dissociation (CID) fragmentation	1147:1196	collision-induced dissociation (CID) fragmentation of target glycopeptides in combination with accurate mass measurement	1147:1266	The attached glycan structures were elucidated by collision-induced dissociation (CID) fragmentation of target glycopeptides in combination with accurate mass measurement.
23829323	9	0	link	plasma-derived	1861:1874	arg1	haptoglobin					1876:1886	plasma-derived haptoglobin	1861:1886	plasma-derived haptoglobin	1861:1886	We further demonstrate the effectiveness of this approach by analyzing plasma-derived haptoglobin, identifying 136 N-linked glycopeptide spectra at a false discovery rate of 0.4%, representing 15 distinct glycopeptides on at least three of the four N-linked glycosylation sites.
23829323	9	1	theme	glycosylation	2048:2060	arg1	sites					2062:2066	the four N-linked glycosylation sites	2030:2066	the four N-linked glycosylation sites	2030:2066	We further demonstrate the effectiveness of this approach by analyzing plasma-derived haptoglobin, identifying 136 N-linked glycopeptide spectra at a false discovery rate of 0.4%, representing 15 distinct glycopeptides on at least three of the four N-linked glycosylation sites.
23829323	2	2	theme	Direct	399:404	arg1	analysis					406:413	Direct analysis	399:413	Direct analysis of protein N-glycosylation by tandem mass spectrometry of glycopeptides	399:485	Direct analysis of protein N-glycosylation by tandem mass spectrometry of glycopeptides promises site-specific elucidation of N-glycan microheterogeneity, something that detached N-glycan and deglycosylated peptide analyses cannot provide.
23829323	3	3	theme	successful	648:657	arg1	implementation					659:672	successful implementation	648:672	successful implementation of direct N-glycopeptide analysis by tandem mass spectrometry	648:734	However, successful implementation of direct N-glycopeptide analysis by tandem mass spectrometry remains a challenge.
23829323	3	4	gly	N-glycopeptide	684:697	arg2	N-glycopeptide					684:697	direct N-glycopeptide analysis	677:706	direct N-glycopeptide analysis	677:706	However, successful implementation of direct N-glycopeptide analysis by tandem mass spectrometry remains a challenge.
23829323	1	5	theme	significant	199:209	arg1	role					211:214	a significant role	197:214	a significant role in many vital cellular processes and human diseases	197:266	Glycosylation is a common protein modification with a significant role in many vital cellular processes and human diseases, making the characterization of protein-attached glycan structures important for understanding cell biology and disease processes.
23829323	4	6	theme	algorithmic	783:793	arg1	techniques					795:804	algorithmic techniques	783:804	algorithmic techniques	783:804	In this work, we consider algorithmic techniques for the analysis of LC-MS/MS data acquired from glycopeptide-enriched fractions of enzymatic digests of purified proteins.
23829323	3	7	theme	N-glycopeptide	684:697	arg1	analysis					699:706	direct N-glycopeptide analysis	677:706	direct N-glycopeptide analysis	677:706	However, successful implementation of direct N-glycopeptide analysis by tandem mass spectrometry remains a challenge.
23829323	5	8	theme	fragmentation	1013:1025	arg1	spectra					1027:1033	CID fragmentation spectra	1009:1033	CID fragmentation spectra of N-glycopeptides	1009:1052	We implement a computational strategy that takes advantage of the properties of CID fragmentation spectra of N-glycopeptides, matching the MS/MS spectra to peptide-glycan pairs from protein sequences and glycan structure databases.
23829323	9	9	theme	plasma-derived	1861:1874	arg1	haptoglobin					1876:1886	plasma-derived haptoglobin	1861:1886	plasma-derived haptoglobin	1861:1886	We further demonstrate the effectiveness of this approach by analyzing plasma-derived haptoglobin, identifying 136 N-linked glycopeptide spectra at a false discovery rate of 0.4%, representing 15 distinct glycopeptides on at least three of the four N-linked glycosylation sites.
23829323	2	10	gly	deglycosylated	591:604	arg1	analyses					614:621	deglycosylated peptide analyses	591:621	deglycosylated peptide analyses	591:621	Direct analysis of protein N-glycosylation by tandem mass spectrometry of glycopeptides promises site-specific elucidation of N-glycan microheterogeneity, something that detached N-glycan and deglycosylated peptide analyses cannot provide.
23829323	1	11	theme	vital	224:228	arg1	processes					239:247	many vital cellular processes	219:247	many vital cellular processes	219:247	Glycosylation is a common protein modification with a significant role in many vital cellular processes and human diseases, making the characterization of protein-attached glycan structures important for understanding cell biology and disease processes.
23829323	3	12	theme	mass	718:721	arg1	spectrometry					723:734	tandem mass spectrometry	711:734	tandem mass spectrometry	711:734	However, successful implementation of direct N-glycopeptide analysis by tandem mass spectrometry remains a challenge.
23829323	4	13	theme	LC-MS/MS	826:833	arg1	data					835:838	LC-MS/MS data	826:838	LC-MS/MS data acquired from glycopeptide-enriched fractions of enzymatic digests of purified proteins	826:926	In this work, we consider algorithmic techniques for the analysis of LC-MS/MS data acquired from glycopeptide-enriched fractions of enzymatic digests of purified proteins.
23829323	9	14	theme	glycopeptide	1914:1925	arg1	spectra					1927:1933	136 N-linked glycopeptide spectra	1901:1933	136 N-linked glycopeptide spectra	1901:1933	We further demonstrate the effectiveness of this approach by analyzing plasma-derived haptoglobin, identifying 136 N-linked glycopeptide spectra at a false discovery rate of 0.4%, representing 15 distinct glycopeptides on at least three of the four N-linked glycosylation sites.
23829323	8	15	theme	spectra	1627:1633	arg1	246					1616:1618	246	1616:1618	246	1616:1618	Our software, GlycoPeptideSearch (GPS), assigned glycopeptide identifications to 246 of the spectra at a false discovery rate of 5.58%, identifying 42 distinct haptoglobin peptide-glycan pairs at each of the four haptoglobin N-linked glycosylation sites.
23829323	8	15	theme	spectra	1627:1633	arg1	spectra					1627:1633	the spectra	1623:1633	the spectra	1623:1633	Our software, GlycoPeptideSearch (GPS), assigned glycopeptide identifications to 246 of the spectra at a false discovery rate of 5.58%, identifying 42 distinct haptoglobin peptide-glycan pairs at each of the four haptoglobin N-linked glycosylation sites.
23829323	1	16	from	role	211:214	arg1	diseases					259:266	human diseases	253:266	human diseases	253:266	Glycosylation is a common protein modification with a significant role in many vital cellular processes and human diseases, making the characterization of protein-attached glycan structures important for understanding cell biology and disease processes.
23829323	1	16	from	role	211:214	arg1	processes					239:247	many vital cellular processes	219:247	many vital cellular processes	219:247	Glycosylation is a common protein modification with a significant role in many vital cellular processes and human diseases, making the characterization of protein-attached glycan structures important for understanding cell biology and disease processes.
23829323	2	17	theme	deglycosylated	591:604	arg1	analyses					614:621	deglycosylated peptide analyses	591:621	deglycosylated peptide analyses	591:621	Direct analysis of protein N-glycosylation by tandem mass spectrometry of glycopeptides promises site-specific elucidation of N-glycan microheterogeneity, something that detached N-glycan and deglycosylated peptide analyses cannot provide.
23829323	0	18	theme	CID	93:95	arg1	spectra					109:115	glycopeptide CID tandem mass spectra	80:115	glycopeptide CID tandem mass spectra	80:115	Exploring site-specific N-glycosylation microheterogeneity of haptoglobin using glycopeptide CID tandem mass spectra and glycan database search.
23829323	9	19	theme	distinct	1986:1993	arg1	glycopeptides					1995:2007	15 distinct glycopeptides	1983:2007	15 distinct glycopeptides	1983:2007	We further demonstrate the effectiveness of this approach by analyzing plasma-derived haptoglobin, identifying 136 N-linked glycopeptide spectra at a false discovery rate of 0.4%, representing 15 distinct glycopeptides on at least three of the four N-linked glycosylation sites.
23829323	1	20	theme	protein	171:177	arg1	modification					179:190	a common protein modification	162:190	a common protein modification with a significant role in many vital cellular processes and human diseases	162:266	Glycosylation is a common protein modification with a significant role in many vital cellular processes and human diseases, making the characterization of protein-attached glycan structures important for understanding cell biology and disease processes.
23829323	1	20	theme	protein	171:177	arg1	Glycosylation					145:157	Glycosylation	145:157	Glycosylation	145:157	Glycosylation is a common protein modification with a significant role in many vital cellular processes and human diseases, making the characterization of protein-attached glycan structures important for understanding cell biology and disease processes.
23829323	9	21	theme	false	1940:1944	arg1	rate					1956:1959	a false discovery rate	1938:1959	a false discovery rate of 0.4%	1938:1967	We further demonstrate the effectiveness of this approach by analyzing plasma-derived haptoglobin, identifying 136 N-linked glycopeptide spectra at a false discovery rate of 0.4%, representing 15 distinct glycopeptides on at least three of the four N-linked glycosylation sites.
23829323	8	22	theme	discovery	1646:1654	arg1	rate					1656:1659	a false discovery rate	1638:1659	a false discovery rate of 5.58%	1638:1668	Our software, GlycoPeptideSearch (GPS), assigned glycopeptide identifications to 246 of the spectra at a false discovery rate of 5.58%, identifying 42 distinct haptoglobin peptide-glycan pairs at each of the four haptoglobin N-linked glycosylation sites.
23829323	2	23	gly	glycopeptides	473:485	arg2	glycopeptides					473:485	glycopeptides	473:485	glycopeptides	473:485	Direct analysis of protein N-glycosylation by tandem mass spectrometry of glycopeptides promises site-specific elucidation of N-glycan microheterogeneity, something that detached N-glycan and deglycosylated peptide analyses cannot provide.
23829323	0	24	theme	mass	104:107	arg1	spectra					109:115	glycopeptide CID tandem mass spectra	80:115	glycopeptide CID tandem mass spectra	80:115	Exploring site-specific N-glycosylation microheterogeneity of haptoglobin using glycopeptide CID tandem mass spectra and glycan database search.
23829323	4	25	theme	digests	899:905	arg1	fractions					876:884	glycopeptide-enriched fractions	854:884	glycopeptide-enriched fractions of enzymatic digests of purified proteins	854:926	In this work, we consider algorithmic techniques for the analysis of LC-MS/MS data acquired from glycopeptide-enriched fractions of enzymatic digests of purified proteins.
23829323	10	26	from	http	2134:2137	arg1	download					2120:2127	download	2120:2127	download from http://edwardslab.bmcb.georgetown.edu/GPS	2120:2174	The software, GlycoPeptideSearch, is available for download from http://edwardslab.bmcb.georgetown.edu/GPS .
23829323	8	27	theme	%	1668:1668	arg1	rate					1656:1659	a false discovery rate	1638:1659	a false discovery rate of 5.58%	1638:1668	Our software, GlycoPeptideSearch (GPS), assigned glycopeptide identifications to 246 of the spectra at a false discovery rate of 5.58%, identifying 42 distinct haptoglobin peptide-glycan pairs at each of the four haptoglobin N-linked glycosylation sites.
23829323	4	28	theme	purified	910:917	arg1	proteins					919:926	purified proteins	910:926	purified proteins	910:926	In this work, we consider algorithmic techniques for the analysis of LC-MS/MS data acquired from glycopeptide-enriched fractions of enzymatic digests of purified proteins.
23829323	2	29	theme	mass	452:455	arg1	spectrometry					457:468	tandem mass spectrometry	445:468	tandem mass spectrometry of glycopeptides	445:485	Direct analysis of protein N-glycosylation by tandem mass spectrometry of glycopeptides promises site-specific elucidation of N-glycan microheterogeneity, something that detached N-glycan and deglycosylated peptide analyses cannot provide.
23829323	0	30	theme	database	128:135	arg1	search					137:142	glycan database search	121:142	glycan database search	121:142	Exploring site-specific N-glycosylation microheterogeneity of haptoglobin using glycopeptide CID tandem mass spectra and glycan database search.
23829323	5	31	theme	glycan	1133:1138	arg1	databases					1150:1158	glycan structure databases	1133:1158	glycan structure databases	1133:1158	We implement a computational strategy that takes advantage of the properties of CID fragmentation spectra of N-glycopeptides, matching the MS/MS spectra to peptide-glycan pairs from protein sequences and glycan structure databases.
23829323	2	32	theme	N-glycan	525:532	arg1	something					554:562	something	554:562	something that detached N-glycan and deglycosylated peptide analyses	554:621	Direct analysis of protein N-glycosylation by tandem mass spectrometry of glycopeptides promises site-specific elucidation of N-glycan microheterogeneity, something that detached N-glycan and deglycosylated peptide analyses cannot provide.
23829323	2	32	theme	N-glycan	525:532	arg1	microheterogeneity					534:551	N-glycan microheterogeneity	525:551	N-glycan microheterogeneity	525:551	Direct analysis of protein N-glycosylation by tandem mass spectrometry of glycopeptides promises site-specific elucidation of N-glycan microheterogeneity, something that detached N-glycan and deglycosylated peptide analyses cannot provide.
23829323	4	33	theme	glycopeptide-enriched	854:874	arg1	fractions					876:884	glycopeptide-enriched fractions	854:884	glycopeptide-enriched fractions of enzymatic digests of purified proteins	854:926	In this work, we consider algorithmic techniques for the analysis of LC-MS/MS data acquired from glycopeptide-enriched fractions of enzymatic digests of purified proteins.
23829323	5	34	theme	computational	944:956	arg1	strategy					958:965	a computational strategy	942:965	a computational strategy that takes advantage of the properties of CID fragmentation spectra of N-glycopeptides, matching the MS/MS spectra to peptide-glycan pairs from protein sequences and glycan structure databases	942:1158	We implement a computational strategy that takes advantage of the properties of CID fragmentation spectra of N-glycopeptides, matching the MS/MS spectra to peptide-glycan pairs from protein sequences and glycan structure databases.
23829323	1	35	theme	protein-attached	300:315	arg1	structures					324:333	protein-attached glycan structures	300:333	protein-attached glycan structures important for understanding cell biology and disease processes	300:396	Glycosylation is a common protein modification with a significant role in many vital cellular processes and human diseases, making the characterization of protein-attached glycan structures important for understanding cell biology and disease processes.
23829323	5	36	theme	peptide-glycan	1085:1098	arg1	pairs					1100:1104	peptide-glycan pairs	1085:1104	peptide-glycan pairs from protein sequences and glycan structure databases	1085:1158	We implement a computational strategy that takes advantage of the properties of CID fragmentation spectra of N-glycopeptides, matching the MS/MS spectra to peptide-glycan pairs from protein sequences and glycan structure databases.
23829323	6	37	theme	rate	1216:1219	arg1	technique					1232:1240	a novel false discovery rate estimation technique	1192:1240	a novel false discovery rate estimation technique to estimate and manage the number of false identifications	1192:1299	Significantly, we also propose a novel false discovery rate estimation technique to estimate and manage the number of false identifications.
23829323	8	38	theme	distinct	1686:1693	arg1	pairs					1722:1726	42 distinct haptoglobin peptide-glycan pairs	1683:1726	42 distinct haptoglobin peptide-glycan pairs	1683:1726	Our software, GlycoPeptideSearch (GPS), assigned glycopeptide identifications to 246 of the spectra at a false discovery rate of 5.58%, identifying 42 distinct haptoglobin peptide-glycan pairs at each of the four haptoglobin N-linked glycosylation sites.
23829323	0	39	theme	N-glycosylation	24:38	arg1	microheterogeneity					40:57	site-specific N-glycosylation microheterogeneity	10:57	site-specific N-glycosylation microheterogeneity of haptoglobin	10:72	Exploring site-specific N-glycosylation microheterogeneity of haptoglobin using glycopeptide CID tandem mass spectra and glycan database search.
23829323	1	40	theme	structures	324:333	arg1	characterization					280:295	the characterization	276:295	the characterization of protein-attached glycan structures important for understanding cell biology and disease processes	276:396	Glycosylation is a common protein modification with a significant role in many vital cellular processes and human diseases, making the characterization of protein-attached glycan structures important for understanding cell biology and disease processes.
23829323	7	41	gly	glycopeptides	1398:1410	arg2	glycopeptides					1398:1410	glycopeptides	1398:1410	glycopeptides using HILIC chromatography	1398:1437	We use a human glycoprotein standard, haptoglobin, digested with trypsin and GluC, enriched for glycopeptides using HILIC chromatography, and analyzed by LC-MS/MS to demonstrate our algorithmic strategy and evaluate its performance.
23829323	6	42	theme	false	1200:1204	arg1	technique					1232:1240	a novel false discovery rate estimation technique	1192:1240	a novel false discovery rate estimation technique to estimate and manage the number of false identifications	1192:1299	Significantly, we also propose a novel false discovery rate estimation technique to estimate and manage the number of false identifications.
23829323	8	43	theme	peptide-glycan	1707:1720	arg1	pairs					1722:1726	42 distinct haptoglobin peptide-glycan pairs	1683:1726	42 distinct haptoglobin peptide-glycan pairs	1683:1726	Our software, GlycoPeptideSearch (GPS), assigned glycopeptide identifications to 246 of the spectra at a false discovery rate of 5.58%, identifying 42 distinct haptoglobin peptide-glycan pairs at each of the four haptoglobin N-linked glycosylation sites.
23829323	9	44	link	N-linked	2039:2046	arg1	sites					2062:2066	the four N-linked glycosylation sites	2030:2066	the four N-linked glycosylation sites	2030:2066	We further demonstrate the effectiveness of this approach by analyzing plasma-derived haptoglobin, identifying 136 N-linked glycopeptide spectra at a false discovery rate of 0.4%, representing 15 distinct glycopeptides on at least three of the four N-linked glycosylation sites.
23829323	1	45	theme	cell	363:366	arg1	biology					368:374	cell biology	363:374	cell biology	363:374	Glycosylation is a common protein modification with a significant role in many vital cellular processes and human diseases, making the characterization of protein-attached glycan structures important for understanding cell biology and disease processes.
23829323	8	46	gly	glycosylation	1769:1781	arg2	four					1743:1746	four	1743:1746	four	1743:1746	Our software, GlycoPeptideSearch (GPS), assigned glycopeptide identifications to 246 of the spectra at a false discovery rate of 5.58%, identifying 42 distinct haptoglobin peptide-glycan pairs at each of the four haptoglobin N-linked glycosylation sites.
23829323	8	46	gly	glycosylation	1769:1781	arg2	sites					1783:1787	the four haptoglobin N-linked glycosylation sites	1739:1787	the four haptoglobin N-linked glycosylation sites	1739:1787	Our software, GlycoPeptideSearch (GPS), assigned glycopeptide identifications to 246 of the spectra at a false discovery rate of 5.58%, identifying 42 distinct haptoglobin peptide-glycan pairs at each of the four haptoglobin N-linked glycosylation sites.
23829323	6	47	theme	false	1279:1283	arg1	identifications					1285:1299	false identifications	1279:1299	false identifications	1279:1299	Significantly, we also propose a novel false discovery rate estimation technique to estimate and manage the number of false identifications.
23829323	9	48	link	N-linked	1905:1912	arg1	spectra					1927:1933	136 N-linked glycopeptide spectra	1901:1933	136 N-linked glycopeptide spectra	1901:1933	We further demonstrate the effectiveness of this approach by analyzing plasma-derived haptoglobin, identifying 136 N-linked glycopeptide spectra at a false discovery rate of 0.4%, representing 15 distinct glycopeptides on at least three of the four N-linked glycosylation sites.
23829323	7	49	gly	glycoprotein	1317:1328	arg1	glycoprotein					1317:1328	a human glycoprotein standard	1309:1337	a human glycoprotein standard	1309:1337	We use a human glycoprotein standard, haptoglobin, digested with trypsin and GluC, enriched for glycopeptides using HILIC chromatography, and analyzed by LC-MS/MS to demonstrate our algorithmic strategy and evaluate its performance.
23829323	7	49	gly	glycoprotein	1317:1328	arg1	haptoglobin					1340:1350	haptoglobin	1340:1350	haptoglobin	1340:1350	We use a human glycoprotein standard, haptoglobin, digested with trypsin and GluC, enriched for glycopeptides using HILIC chromatography, and analyzed by LC-MS/MS to demonstrate our algorithmic strategy and evaluate its performance.
23829323	2	50	theme	protein	418:424	arg1	N-glycosylation					426:440	protein N-glycosylation	418:440	protein N-glycosylation	418:440	Direct analysis of protein N-glycosylation by tandem mass spectrometry of glycopeptides promises site-specific elucidation of N-glycan microheterogeneity, something that detached N-glycan and deglycosylated peptide analyses cannot provide.
23829323	0	51	gly	glycopeptide	80:91	arg2	glycopeptide					80:91	glycopeptide CID tandem mass spectra	80:115	glycopeptide CID tandem mass spectra	80:115	Exploring site-specific N-glycosylation microheterogeneity of haptoglobin using glycopeptide CID tandem mass spectra and glycan database search.
23829323	9	52	theme	N-linked	2039:2046	arg1	sites					2062:2066	the four N-linked glycosylation sites	2030:2066	the four N-linked glycosylation sites	2030:2066	We further demonstrate the effectiveness of this approach by analyzing plasma-derived haptoglobin, identifying 136 N-linked glycopeptide spectra at a false discovery rate of 0.4%, representing 15 distinct glycopeptides on at least three of the four N-linked glycosylation sites.
23829323	8	53	theme	N-linked	1760:1767	arg1	sites					1783:1787	the four haptoglobin N-linked glycosylation sites	1739:1787	the four haptoglobin N-linked glycosylation sites	1739:1787	Our software, GlycoPeptideSearch (GPS), assigned glycopeptide identifications to 246 of the spectra at a false discovery rate of 5.58%, identifying 42 distinct haptoglobin peptide-glycan pairs at each of the four haptoglobin N-linked glycosylation sites.
23829323	9	54	theme	sites	2062:2066	arg1	three					2021:2025	three	2021:2025	three	2021:2025	We further demonstrate the effectiveness of this approach by analyzing plasma-derived haptoglobin, identifying 136 N-linked glycopeptide spectra at a false discovery rate of 0.4%, representing 15 distinct glycopeptides on at least three of the four N-linked glycosylation sites.
23829323	9	54	theme	sites	2062:2066	arg1	sites					2062:2066	the four N-linked glycosylation sites	2030:2066	the four N-linked glycosylation sites	2030:2066	We further demonstrate the effectiveness of this approach by analyzing plasma-derived haptoglobin, identifying 136 N-linked glycopeptide spectra at a false discovery rate of 0.4%, representing 15 distinct glycopeptides on at least three of the four N-linked glycosylation sites.
23829323	5	55	from	sequences	1119:1127	arg1	pairs					1100:1104	peptide-glycan pairs	1085:1104	peptide-glycan pairs from protein sequences and glycan structure databases	1085:1158	We implement a computational strategy that takes advantage of the properties of CID fragmentation spectra of N-glycopeptides, matching the MS/MS spectra to peptide-glycan pairs from protein sequences and glycan structure databases.
23829323	8	56	gly	glycopeptide	1584:1595	arg2	glycopeptide					1584:1595	glycopeptide identifications	1584:1611	glycopeptide identifications	1584:1611	Our software, GlycoPeptideSearch (GPS), assigned glycopeptide identifications to 246 of the spectra at a false discovery rate of 5.58%, identifying 42 distinct haptoglobin peptide-glycan pairs at each of the four haptoglobin N-linked glycosylation sites.
23829323	9	57	gly	glycosylation	2048:2060	arg2	sites					2062:2066	the four N-linked glycosylation sites	2030:2066	the four N-linked glycosylation sites	2030:2066	We further demonstrate the effectiveness of this approach by analyzing plasma-derived haptoglobin, identifying 136 N-linked glycopeptide spectra at a false discovery rate of 0.4%, representing 15 distinct glycopeptides on at least three of the four N-linked glycosylation sites.
23829323	9	57	gly	glycosylation	2048:2060	arg2	four					2034:2037	four	2034:2037	four	2034:2037	We further demonstrate the effectiveness of this approach by analyzing plasma-derived haptoglobin, identifying 136 N-linked glycopeptide spectra at a false discovery rate of 0.4%, representing 15 distinct glycopeptides on at least three of the four N-linked glycosylation sites.
23829323	5	58	theme	properties	995:1004	arg1	advantage					978:986	advantage	978:986	advantage of the properties of CID fragmentation spectra of N-glycopeptides	978:1052	We implement a computational strategy that takes advantage of the properties of CID fragmentation spectra of N-glycopeptides, matching the MS/MS spectra to peptide-glycan pairs from protein sequences and glycan structure databases.
23829323	9	59	theme	approach	1839:1846	arg1	effectiveness					1817:1829	the effectiveness	1813:1829	the effectiveness of this approach	1813:1846	We further demonstrate the effectiveness of this approach by analyzing plasma-derived haptoglobin, identifying 136 N-linked glycopeptide spectra at a false discovery rate of 0.4%, representing 15 distinct glycopeptides on at least three of the four N-linked glycosylation sites.
23829323	3	60	theme	direct	677:682	arg1	analysis					699:706	direct N-glycopeptide analysis	677:706	direct N-glycopeptide analysis	677:706	However, successful implementation of direct N-glycopeptide analysis by tandem mass spectrometry remains a challenge.
23829323	5	61	from	databases	1150:1158	arg1	pairs					1100:1104	peptide-glycan pairs	1085:1104	peptide-glycan pairs from protein sequences and glycan structure databases	1085:1158	We implement a computational strategy that takes advantage of the properties of CID fragmentation spectra of N-glycopeptides, matching the MS/MS spectra to peptide-glycan pairs from protein sequences and glycan structure databases.
23829323	5	62	theme	CID	1009:1011	arg1	spectra					1027:1033	CID fragmentation spectra	1009:1033	CID fragmentation spectra of N-glycopeptides	1009:1052	We implement a computational strategy that takes advantage of the properties of CID fragmentation spectra of N-glycopeptides, matching the MS/MS spectra to peptide-glycan pairs from protein sequences and glycan structure databases.
23829323	0	63	gly	microheterogeneity	40:57	arg1	haptoglobin					62:72	haptoglobin	62:72	haptoglobin	62:72	Exploring site-specific N-glycosylation microheterogeneity of haptoglobin using glycopeptide CID tandem mass spectra and glycan database search.
23829323	1	64	theme	many	219:222	arg1	processes					239:247	many vital cellular processes	219:247	many vital cellular processes	219:247	Glycosylation is a common protein modification with a significant role in many vital cellular processes and human diseases, making the characterization of protein-attached glycan structures important for understanding cell biology and disease processes.
23829323	1	65	theme	common	164:169	arg1	modification					179:190	a common protein modification	162:190	a common protein modification with a significant role in many vital cellular processes and human diseases	162:266	Glycosylation is a common protein modification with a significant role in many vital cellular processes and human diseases, making the characterization of protein-attached glycan structures important for understanding cell biology and disease processes.
23829323	1	65	theme	common	164:169	arg1	Glycosylation					145:157	Glycosylation	145:157	Glycosylation	145:157	Glycosylation is a common protein modification with a significant role in many vital cellular processes and human diseases, making the characterization of protein-attached glycan structures important for understanding cell biology and disease processes.
23829323	3	66	theme	tandem	711:716	arg1	spectrometry					723:734	tandem mass spectrometry	711:734	tandem mass spectrometry	711:734	However, successful implementation of direct N-glycopeptide analysis by tandem mass spectrometry remains a challenge.
23829323	9	67	gly	glycopeptide	1914:1925	arg2	glycopeptide					1914:1925	136 N-linked glycopeptide spectra	1901:1933	136 N-linked glycopeptide spectra	1901:1933	We further demonstrate the effectiveness of this approach by analyzing plasma-derived haptoglobin, identifying 136 N-linked glycopeptide spectra at a false discovery rate of 0.4%, representing 15 distinct glycopeptides on at least three of the four N-linked glycosylation sites.
23829323	1	68	theme	cellular	230:237	arg1	processes					239:247	many vital cellular processes	219:247	many vital cellular processes	219:247	Glycosylation is a common protein modification with a significant role in many vital cellular processes and human diseases, making the characterization of protein-attached glycan structures important for understanding cell biology and disease processes.
23829323	8	69	link	N-linked	1760:1767	arg1	sites					1783:1787	the four haptoglobin N-linked glycosylation sites	1739:1787	the four haptoglobin N-linked glycosylation sites	1739:1787	Our software, GlycoPeptideSearch (GPS), assigned glycopeptide identifications to 246 of the spectra at a false discovery rate of 5.58%, identifying 42 distinct haptoglobin peptide-glycan pairs at each of the four haptoglobin N-linked glycosylation sites.
23829323	3	70	theme	analysis	699:706	arg1	implementation					659:672	successful implementation	648:672	successful implementation of direct N-glycopeptide analysis by tandem mass spectrometry	648:734	However, successful implementation of direct N-glycopeptide analysis by tandem mass spectrometry remains a challenge.
23829323	9	71	theme	N-linked	1905:1912	arg1	spectra					1927:1933	136 N-linked glycopeptide spectra	1901:1933	136 N-linked glycopeptide spectra	1901:1933	We further demonstrate the effectiveness of this approach by analyzing plasma-derived haptoglobin, identifying 136 N-linked glycopeptide spectra at a false discovery rate of 0.4%, representing 15 distinct glycopeptides on at least three of the four N-linked glycosylation sites.
23829323	5	72	theme	MS/MS	1068:1072	arg1	spectra					1074:1080	the MS/MS spectra	1064:1080	the MS/MS spectra	1064:1080	We implement a computational strategy that takes advantage of the properties of CID fragmentation spectra of N-glycopeptides, matching the MS/MS spectra to peptide-glycan pairs from protein sequences and glycan structure databases.
23829323	5	73	gly	N-glycopeptides	1038:1052	arg2	N-glycopeptides					1038:1052	N-glycopeptides	1038:1052	N-glycopeptides	1038:1052	We implement a computational strategy that takes advantage of the properties of CID fragmentation spectra of N-glycopeptides, matching the MS/MS spectra to peptide-glycan pairs from protein sequences and glycan structure databases.
23829323	8	74	theme	false	1640:1644	arg1	rate					1656:1659	a false discovery rate	1638:1659	a false discovery rate of 5.58%	1638:1668	Our software, GlycoPeptideSearch (GPS), assigned glycopeptide identifications to 246 of the spectra at a false discovery rate of 5.58%, identifying 42 distinct haptoglobin peptide-glycan pairs at each of the four haptoglobin N-linked glycosylation sites.
23829323	4	75	theme	data	835:838	arg1	analysis					814:821	the analysis	810:821	the analysis of LC-MS/MS data acquired from glycopeptide-enriched fractions of enzymatic digests of purified proteins	810:926	In this work, we consider algorithmic techniques for the analysis of LC-MS/MS data acquired from glycopeptide-enriched fractions of enzymatic digests of purified proteins.
23829323	0	76	theme	tandem	97:102	arg1	spectra					109:115	glycopeptide CID tandem mass spectra	80:115	glycopeptide CID tandem mass spectra	80:115	Exploring site-specific N-glycosylation microheterogeneity of haptoglobin using glycopeptide CID tandem mass spectra and glycan database search.
23829323	5	77	theme	spectra	1027:1033	arg1	properties					995:1004	the properties	991:1004	the properties of CID fragmentation spectra of N-glycopeptides	991:1052	We implement a computational strategy that takes advantage of the properties of CID fragmentation spectra of N-glycopeptides, matching the MS/MS spectra to peptide-glycan pairs from protein sequences and glycan structure databases.
23829323	1	78	theme	disease	380:386	arg1	processes					388:396	disease processes	380:396	disease processes	380:396	Glycosylation is a common protein modification with a significant role in many vital cellular processes and human diseases, making the characterization of protein-attached glycan structures important for understanding cell biology and disease processes.
23829323	1	79	with	modification	179:190	arg1	role					211:214	a significant role	197:214	a significant role in many vital cellular processes and human diseases	197:266	Glycosylation is a common protein modification with a significant role in many vital cellular processes and human diseases, making the characterization of protein-attached glycan structures important for understanding cell biology and disease processes.
23829323	5	80	theme	N-glycopeptides	1038:1052	arg1	spectra					1027:1033	CID fragmentation spectra	1009:1033	CID fragmentation spectra of N-glycopeptides	1009:1052	We implement a computational strategy that takes advantage of the properties of CID fragmentation spectra of N-glycopeptides, matching the MS/MS spectra to peptide-glycan pairs from protein sequences and glycan structure databases.
23829323	9	81	theme	discovery	1946:1954	arg1	rate					1956:1959	a false discovery rate	1938:1959	a false discovery rate of 0.4%	1938:1967	We further demonstrate the effectiveness of this approach by analyzing plasma-derived haptoglobin, identifying 136 N-linked glycopeptide spectra at a false discovery rate of 0.4%, representing 15 distinct glycopeptides on at least three of the four N-linked glycosylation sites.
23829323	7	82	dep	glycoprotein	1317:1328	arg1	digested					1353:1360	digested	1353:1360	digested with trypsin and GluC	1353:1382	We use a human glycoprotein standard, haptoglobin, digested with trypsin and GluC, enriched for glycopeptides using HILIC chromatography, and analyzed by LC-MS/MS to demonstrate our algorithmic strategy and evaluate its performance.
23829323	7	82	dep	glycoprotein	1317:1328	arg1	enriched					1385:1392	enriched	1385:1392	enriched for glycopeptides using HILIC chromatography	1385:1437	We use a human glycoprotein standard, haptoglobin, digested with trypsin and GluC, enriched for glycopeptides using HILIC chromatography, and analyzed by LC-MS/MS to demonstrate our algorithmic strategy and evaluate its performance.
23829323	7	82	dep	glycoprotein	1317:1328	arg1	analyzed					1444:1451	analyzed	1444:1451	analyzed by LC-MS/MS	1444:1463	We use a human glycoprotein standard, haptoglobin, digested with trypsin and GluC, enriched for glycopeptides using HILIC chromatography, and analyzed by LC-MS/MS to demonstrate our algorithmic strategy and evaluate its performance.
23829323	0	83	theme	glycan	121:126	arg1	search					137:142	glycan database search	121:142	glycan database search	121:142	Exploring site-specific N-glycosylation microheterogeneity of haptoglobin using glycopeptide CID tandem mass spectra and glycan database search.
23829323	5	84	theme	protein	1111:1117	arg1	sequences					1119:1127	protein sequences	1111:1127	protein sequences	1111:1127	We implement a computational strategy that takes advantage of the properties of CID fragmentation spectra of N-glycopeptides, matching the MS/MS spectra to peptide-glycan pairs from protein sequences and glycan structure databases.
23829323	4	85	theme	enzymatic	889:897	arg1	digests					899:905	enzymatic digests	889:905	enzymatic digests of purified proteins	889:926	In this work, we consider algorithmic techniques for the analysis of LC-MS/MS data acquired from glycopeptide-enriched fractions of enzymatic digests of purified proteins.
23829323	7	86	theme	algorithmic	1484:1494	arg1	strategy					1496:1503	our algorithmic strategy	1480:1503	our algorithmic strategy	1480:1503	We use a human glycoprotein standard, haptoglobin, digested with trypsin and GluC, enriched for glycopeptides using HILIC chromatography, and analyzed by LC-MS/MS to demonstrate our algorithmic strategy and evaluate its performance.
23829323	2	87	theme	peptide	606:612	arg1	analyses					614:621	deglycosylated peptide analyses	591:621	deglycosylated peptide analyses	591:621	Direct analysis of protein N-glycosylation by tandem mass spectrometry of glycopeptides promises site-specific elucidation of N-glycan microheterogeneity, something that detached N-glycan and deglycosylated peptide analyses cannot provide.
23829323	2	88	theme	tandem	445:450	arg1	spectrometry					457:468	tandem mass spectrometry	445:468	tandem mass spectrometry of glycopeptides	445:485	Direct analysis of protein N-glycosylation by tandem mass spectrometry of glycopeptides promises site-specific elucidation of N-glycan microheterogeneity, something that detached N-glycan and deglycosylated peptide analyses cannot provide.
23829323	0	89	theme	site-specific	10:22	arg1	microheterogeneity					40:57	site-specific N-glycosylation microheterogeneity	10:57	site-specific N-glycosylation microheterogeneity of haptoglobin	10:72	Exploring site-specific N-glycosylation microheterogeneity of haptoglobin using glycopeptide CID tandem mass spectra and glycan database search.
23829323	9	90	gly	glycopeptides	1995:2007	arg2	glycopeptides					1995:2007	15 distinct glycopeptides	1983:2007	15 distinct glycopeptides	1983:2007	We further demonstrate the effectiveness of this approach by analyzing plasma-derived haptoglobin, identifying 136 N-linked glycopeptide spectra at a false discovery rate of 0.4%, representing 15 distinct glycopeptides on at least three of the four N-linked glycosylation sites.
23829323	6	91	theme	estimation	1221:1230	arg1	technique					1232:1240	a novel false discovery rate estimation technique	1192:1240	a novel false discovery rate estimation technique to estimate and manage the number of false identifications	1192:1299	Significantly, we also propose a novel false discovery rate estimation technique to estimate and manage the number of false identifications.
23829323	8	92	theme	haptoglobin	1695:1705	arg1	pairs					1722:1726	42 distinct haptoglobin peptide-glycan pairs	1683:1726	42 distinct haptoglobin peptide-glycan pairs	1683:1726	Our software, GlycoPeptideSearch (GPS), assigned glycopeptide identifications to 246 of the spectra at a false discovery rate of 5.58%, identifying 42 distinct haptoglobin peptide-glycan pairs at each of the four haptoglobin N-linked glycosylation sites.
23829323	2	93	theme	N-glycosylation	426:440	arg1	analysis					406:413	Direct analysis	399:413	Direct analysis of protein N-glycosylation by tandem mass spectrometry of glycopeptides	399:485	Direct analysis of protein N-glycosylation by tandem mass spectrometry of glycopeptides promises site-specific elucidation of N-glycan microheterogeneity, something that detached N-glycan and deglycosylated peptide analyses cannot provide.
23829323	7	94	theme	human	1311:1315	arg1	glycoprotein					1317:1328	a human glycoprotein standard	1309:1337	a human glycoprotein standard	1309:1337	We use a human glycoprotein standard, haptoglobin, digested with trypsin and GluC, enriched for glycopeptides using HILIC chromatography, and analyzed by LC-MS/MS to demonstrate our algorithmic strategy and evaluate its performance.
23829323	7	94	theme	human	1311:1315	arg1	haptoglobin					1340:1350	haptoglobin	1340:1350	haptoglobin	1340:1350	We use a human glycoprotein standard, haptoglobin, digested with trypsin and GluC, enriched for glycopeptides using HILIC chromatography, and analyzed by LC-MS/MS to demonstrate our algorithmic strategy and evaluate its performance.
23829323	1	95	theme	glycan	317:322	arg1	structures					324:333	protein-attached glycan structures	300:333	protein-attached glycan structures important for understanding cell biology and disease processes	300:396	Glycosylation is a common protein modification with a significant role in many vital cellular processes and human diseases, making the characterization of protein-attached glycan structures important for understanding cell biology and disease processes.
23829323	6	96	theme	discovery	1206:1214	arg1	technique					1232:1240	a novel false discovery rate estimation technique	1192:1240	a novel false discovery rate estimation technique to estimate and manage the number of false identifications	1192:1299	Significantly, we also propose a novel false discovery rate estimation technique to estimate and manage the number of false identifications.
23829323	2	97	theme	site-specific	496:508	arg1	elucidation					510:520	site-specific elucidation	496:520	site-specific elucidation of N-glycan microheterogeneity, something that detached N-glycan and deglycosylated peptide analyses	496:621	Direct analysis of protein N-glycosylation by tandem mass spectrometry of glycopeptides promises site-specific elucidation of N-glycan microheterogeneity, something that detached N-glycan and deglycosylated peptide analyses cannot provide.
23829323	2	98	theme	glycopeptides	473:485	arg1	spectrometry					457:468	tandem mass spectrometry	445:468	tandem mass spectrometry of glycopeptides	445:485	Direct analysis of protein N-glycosylation by tandem mass spectrometry of glycopeptides promises site-specific elucidation of N-glycan microheterogeneity, something that detached N-glycan and deglycosylated peptide analyses cannot provide.
23829323	0	99	theme	haptoglobin	62:72	arg1	microheterogeneity					40:57	site-specific N-glycosylation microheterogeneity	10:57	site-specific N-glycosylation microheterogeneity of haptoglobin	10:72	Exploring site-specific N-glycosylation microheterogeneity of haptoglobin using glycopeptide CID tandem mass spectra and glycan database search.
23829323	1	100	theme	important	335:343	arg1	structures					324:333	protein-attached glycan structures	300:333	protein-attached glycan structures important for understanding cell biology and disease processes	300:396	Glycosylation is a common protein modification with a significant role in many vital cellular processes and human diseases, making the characterization of protein-attached glycan structures important for understanding cell biology and disease processes.
23829323	6	101	theme	novel	1194:1198	arg1	technique					1232:1240	a novel false discovery rate estimation technique	1192:1240	a novel false discovery rate estimation technique to estimate and manage the number of false identifications	1192:1299	Significantly, we also propose a novel false discovery rate estimation technique to estimate and manage the number of false identifications.
23829323	9	102	theme	%	1967:1967	arg1	rate					1956:1959	a false discovery rate	1938:1959	a false discovery rate of 0.4%	1938:1967	We further demonstrate the effectiveness of this approach by analyzing plasma-derived haptoglobin, identifying 136 N-linked glycopeptide spectra at a false discovery rate of 0.4%, representing 15 distinct glycopeptides on at least three of the four N-linked glycosylation sites.
23829323	0	103	theme	glycopeptide	80:91	arg1	spectra					109:115	glycopeptide CID tandem mass spectra	80:115	glycopeptide CID tandem mass spectra	80:115	Exploring site-specific N-glycosylation microheterogeneity of haptoglobin using glycopeptide CID tandem mass spectra and glycan database search.
23829323	0	104	gly	N-glycosylation	24:38	arg1	haptoglobin					62:72	haptoglobin	62:72	haptoglobin	62:72	Exploring site-specific N-glycosylation microheterogeneity of haptoglobin using glycopeptide CID tandem mass spectra and glycan database search.
23829323	6	105	theme	identifications	1285:1299	arg1	number					1269:1274	the number	1265:1274	the number of false identifications	1265:1299	Significantly, we also propose a novel false discovery rate estimation technique to estimate and manage the number of false identifications.
23829323	2	106	theme	microheterogeneity	534:551	arg1	elucidation					510:520	site-specific elucidation	496:520	site-specific elucidation of N-glycan microheterogeneity, something that detached N-glycan and deglycosylated peptide analyses	496:621	Direct analysis of protein N-glycosylation by tandem mass spectrometry of glycopeptides promises site-specific elucidation of N-glycan microheterogeneity, something that detached N-glycan and deglycosylated peptide analyses cannot provide.
23829323	5	107	theme	structure	1140:1148	arg1	databases					1150:1158	glycan structure databases	1133:1158	glycan structure databases	1133:1158	We implement a computational strategy that takes advantage of the properties of CID fragmentation spectra of N-glycopeptides, matching the MS/MS spectra to peptide-glycan pairs from protein sequences and glycan structure databases.
23829323	7	108	theme	HILIC	1418:1422	arg1	chromatography					1424:1437	HILIC chromatography	1418:1437	HILIC chromatography	1418:1437	We use a human glycoprotein standard, haptoglobin, digested with trypsin and GluC, enriched for glycopeptides using HILIC chromatography, and analyzed by LC-MS/MS to demonstrate our algorithmic strategy and evaluate its performance.
23829323	8	109	theme	haptoglobin	1748:1758	arg1	sites					1783:1787	the four haptoglobin N-linked glycosylation sites	1739:1787	the four haptoglobin N-linked glycosylation sites	1739:1787	Our software, GlycoPeptideSearch (GPS), assigned glycopeptide identifications to 246 of the spectra at a false discovery rate of 5.58%, identifying 42 distinct haptoglobin peptide-glycan pairs at each of the four haptoglobin N-linked glycosylation sites.
23829323	4	110	theme	proteins	919:926	arg1	digests					899:905	enzymatic digests	889:905	enzymatic digests of purified proteins	889:926	In this work, we consider algorithmic techniques for the analysis of LC-MS/MS data acquired from glycopeptide-enriched fractions of enzymatic digests of purified proteins.
23829323	1	111	theme	human	253:257	arg1	diseases					259:266	human diseases	253:266	human diseases	253:266	Glycosylation is a common protein modification with a significant role in many vital cellular processes and human diseases, making the characterization of protein-attached glycan structures important for understanding cell biology and disease processes.
23829323	8	112	theme	glycosylation	1769:1781	arg1	sites					1783:1787	the four haptoglobin N-linked glycosylation sites	1739:1787	the four haptoglobin N-linked glycosylation sites	1739:1787	Our software, GlycoPeptideSearch (GPS), assigned glycopeptide identifications to 246 of the spectra at a false discovery rate of 5.58%, identifying 42 distinct haptoglobin peptide-glycan pairs at each of the four haptoglobin N-linked glycosylation sites.
23829323	8	113	theme	glycopeptide	1584:1595	arg1	identifications					1597:1611	glycopeptide identifications	1584:1611	glycopeptide identifications	1584:1611	Our software, GlycoPeptideSearch (GPS), assigned glycopeptide identifications to 246 of the spectra at a false discovery rate of 5.58%, identifying 42 distinct haptoglobin peptide-glycan pairs at each of the four haptoglobin N-linked glycosylation sites.
23829323	7	114	theme	standard	1330:1337	arg1	glycoprotein					1317:1328	a human glycoprotein standard	1309:1337	a human glycoprotein standard	1309:1337	We use a human glycoprotein standard, haptoglobin, digested with trypsin and GluC, enriched for glycopeptides using HILIC chromatography, and analyzed by LC-MS/MS to demonstrate our algorithmic strategy and evaluate its performance.
23829323	7	114	theme	standard	1330:1337	arg1	haptoglobin					1340:1350	haptoglobin	1340:1350	haptoglobin	1340:1350	We use a human glycoprotein standard, haptoglobin, digested with trypsin and GluC, enriched for glycopeptides using HILIC chromatography, and analyzed by LC-MS/MS to demonstrate our algorithmic strategy and evaluate its performance.
27127844	0	0	theme	a4	70:71	arg1	Stability					81:89	Vacuolar H+ -ATPase (V-ATPase) a4 Subunit Stability	39:89	Vacuolar H+ -ATPase (V-ATPase) a4 Subunit Stability	39:89	N-Linked Glycosylation Is Required for Vacuolar H+ -ATPase (V-ATPase) a4 Subunit Stability, Assembly, and Cell Surface Expression.
27127844	6	1	theme	putative	818:825	arg1	site					841:844	the putative glycosylation site	814:844	the putative glycosylation site	814:844	We transfected HEK 293 cells, using the pCDNA3.1 expression-vector system, to express cDNA constructs of epitope-tagged human a4 subunit, with or without mutations to eliminate the putative glycosylation site.
27127844	4	2	contain	has	440:442	arg1	subunit					432:438	The subunit	428:438	The subunit	428:438	The subunit has conserved, predicted N-glycosylation sites, and the a3 isoform has been directly shown to be N-glycosylated.
27127844	4	2	contain	has	440:442	arg2	sites					481:485	conserved, predicted N-glycosylation sites	444:485	sites	481:485	The subunit has conserved, predicted N-glycosylation sites, and the a3 isoform has been directly shown to be N-glycosylated.
27127844	6	3	gly	glycosylation	827:839	arg2	site					841:844	the putative glycosylation site	814:844	the putative glycosylation site	814:844	We transfected HEK 293 cells, using the pCDNA3.1 expression-vector system, to express cDNA constructs of epitope-tagged human a4 subunit, with or without mutations to eliminate the putative glycosylation site.
27127844	1	4	theme	V-ATPase	202:209	arg1	complex					211:217	the V-ATPase complex	198:217	the V-ATPase complex	198:217	The a subunit is the largest of 14 different subunits that make up the V-ATPase complex.
27127844	4	5	theme	predicted	455:463	arg1	sites					481:485	conserved, predicted N-glycosylation sites	444:485	sites	481:485	The subunit has conserved, predicted N-glycosylation sites, and the a3 isoform has been directly shown to be N-glycosylated.
27127844	13	6	theme	Co-immunoprecipitation	1660:1681	arg1	studies					1683:1689	Co-immunoprecipitation studies	1660:1689	Co-immunoprecipitation studies	1660:1689	Co-immunoprecipitation studies suggested that a4N489D does not assemble with the V-ATPase V1 domain.
27127844	6	7	theme	cDNA	723:726	arg1	constructs					728:737	cDNA constructs	723:737	cDNA constructs of epitope-tagged human a4 subunit	723:772	We transfected HEK 293 cells, using the pCDNA3.1 expression-vector system, to express cDNA constructs of epitope-tagged human a4 subunit, with or without mutations to eliminate the putative glycosylation site.
27127844	1	8	theme	a	135:135	arg1	subunit					137:143	The a subunit	131:143	The a subunit	131:143	The a subunit is the largest of 14 different subunits that make up the V-ATPase complex.
27127844	1	8	theme	a	135:135	arg1	largest					152:158	largest	152:158	largest	152:158	The a subunit is the largest of 14 different subunits that make up the V-ATPase complex.
27127844	3	9	theme	a	312:312	arg1	isoforms					322:329	a subunit isoforms	312:329	a subunit isoforms	312:329	Clinically, a subunit isoforms are implicated in diverse diseases; however, little is known about their structure and function.
27127844	4	10	gly	N-glycosylated	537:550	arg1	N-glycosylated					537:550	N-glycosylated	537:550	N-glycosylated	537:550	The subunit has conserved, predicted N-glycosylation sites, and the a3 isoform has been directly shown to be N-glycosylated.
27127844	4	10	gly	N-glycosylated	537:550	arg1	isoform					499:505	the a3 isoform	492:505	the a3 isoform	492:505	The subunit has conserved, predicted N-glycosylation sites, and the a3 isoform has been directly shown to be N-glycosylated.
27127844	2	11	theme	membrane	246:253	arg1	protein					255:261	this membrane protein	241:261	this membrane protein	241:261	In mammalian species this membrane protein has four paralogous isoforms, a1-a4.
27127844	13	12	theme	V1	1750:1751	arg1	domain					1753:1758	the V-ATPase V1 domain	1737:1758	the V-ATPase V1 domain	1737:1758	Co-immunoprecipitation studies suggested that a4N489D does not assemble with the V-ATPase V1 domain.
27127844	3	13	theme	subunit	314:320	arg1	isoforms					322:329	a subunit isoforms	312:329	a subunit isoforms	312:329	Clinically, a subunit isoforms are implicated in diverse diseases; however, little is known about their structure and function.
27127844	9	14	theme	relative	1133:1140	arg1	mobility					1142:1149	This relative mobility	1128:1149	This relative mobility	1128:1149	This relative mobility was identical to that of unglycosylated mutant a4N489D , demonstrating that the a4 subunit is glycosylated.
27127844	12	15	theme	membrane	1624:1631	arg1	trafficking					1633:1643	plasma membrane trafficking	1617:1643	plasma membrane trafficking	1617:1643	Immunofluorescence colocalization data showed that unglycosylated a4 was mostly retained in the ER, and that plasma membrane trafficking was defective.
27127844	5	16	from	site	623:626	arg1	N-glycosylated					591:604	N-glycosylated	591:604	N-glycosylated	591:604	Here we ask if human a4 (ATP6V0A4) is N-glycosylated at the predicted site, Asn489.
27127844	11	17	theme	Unglycosylated	1392:1405	arg1	a4					1407:1408	Unglycosylated a4	1392:1408	Unglycosylated a4	1392:1408	Unglycosylated a4 was degraded mostly in the proteasomal pathway, but also, in part, through the lysosomal pathway.
27127844	8	18	theme	Endoglycosidase-treated	1004:1026	arg1	WT					1039:1040	WT	1039:1040	WT	1039:1040	Endoglycosidase-treated wild type (WT) a4 showed increased relative mobility on immunoblots, compared with untreated WT a4.
27127844	8	18	theme	Endoglycosidase-treated	1004:1026	arg1	type					1033:1036	Endoglycosidase-treated wild type	1004:1036	Endoglycosidase-treated wild type (WT) a4	1004:1044	Endoglycosidase-treated wild type (WT) a4 showed increased relative mobility on immunoblots, compared with untreated WT a4.
27127844	10	19	theme	higher	1350:1355	arg1	rate					1357:1360	a higher rate	1348:1360	a higher rate than the N-glycosylated form	1348:1389	Cycloheximide pulse-chase experiments showed that the unglycosylated subunit degraded at a higher rate than the N-glycosylated form.
27127844	12	20	theme	plasma	1617:1622	arg1	trafficking					1633:1643	plasma membrane trafficking	1617:1643	plasma membrane trafficking	1617:1643	Immunofluorescence colocalization data showed that unglycosylated a4 was mostly retained in the ER, and that plasma membrane trafficking was defective.
27127844	9	21	gly	unglycosylated	1176:1189	arg1	a4N489D					1198:1204	unglycosylated mutant a4N489D	1176:1204	unglycosylated mutant a4N489D	1176:1204	This relative mobility was identical to that of unglycosylated mutant a4N489D , demonstrating that the a4 subunit is glycosylated.
27127844	8	22	theme	WT	1121:1122	arg1	a4					1124:1125	untreated WT a4	1111:1125	untreated WT a4	1111:1125	Endoglycosidase-treated wild type (WT) a4 showed increased relative mobility on immunoblots, compared with untreated WT a4.
27127844	8	23	from	mobility	1072:1079	arg1	immunoblots					1084:1094	immunoblots	1084:1094	immunoblots	1084:1094	Endoglycosidase-treated wild type (WT) a4 showed increased relative mobility on immunoblots, compared with untreated WT a4.
27127844	2	24	theme	mammalian	223:231	arg1	species					233:239	mammalian species	223:239	mammalian species	223:239	In mammalian species this membrane protein has four paralogous isoforms, a1-a4.
27127844	10	25	gly	unglycosylated	1313:1326	arg1	subunit					1328:1334	the unglycosylated subunit	1309:1334	the unglycosylated subunit	1309:1334	Cycloheximide pulse-chase experiments showed that the unglycosylated subunit degraded at a higher rate than the N-glycosylated form.
27127844	13	26	theme	V-ATPase	1741:1748	arg1	domain					1753:1758	the V-ATPase V1 domain	1737:1758	the V-ATPase V1 domain	1737:1758	Co-immunoprecipitation studies suggested that a4N489D does not assemble with the V-ATPase V1 domain.
27127844	8	27	theme	type	1033:1036	arg1	a4					1043:1044	Endoglycosidase-treated wild type (WT) a4	1004:1044	Endoglycosidase-treated wild type (WT) a4	1004:1044	Endoglycosidase-treated wild type (WT) a4 showed increased relative mobility on immunoblots, compared with untreated WT a4.
27127844	6	28	theme	expression-vector	686:702	arg1	system					704:709	the pCDNA3.1 expression-vector system	673:709	the pCDNA3.1 expression-vector system	673:709	We transfected HEK 293 cells, using the pCDNA3.1 expression-vector system, to express cDNA constructs of epitope-tagged human a4 subunit, with or without mutations to eliminate the putative glycosylation site.
27127844	2	29	theme	paralogous	272:281	arg1	a1-a4					293:297	a1-a4	293:297	a1-a4	293:297	In mammalian species this membrane protein has four paralogous isoforms, a1-a4.
27127844	2	29	theme	paralogous	272:281	arg1	isoforms					283:290	four paralogous isoforms	267:290	four paralogous isoforms	267:290	In mammalian species this membrane protein has four paralogous isoforms, a1-a4.
27127844	18	30	dep	©	1957:1957	arg1	Inc.					1983:1986	Inc.	1983:1986	Inc.	1983:1986	© 2016 Wiley Periodicals, Inc.
27127844	0	31	theme	N-Linked	0:7	arg1	Glycosylation					9:21	N-Linked Glycosylation	0:21	N-Linked Glycosylation	0:21	N-Linked Glycosylation Is Required for Vacuolar H+ -ATPase (V-ATPase) a4 Subunit Stability, Assembly, and Cell Surface Expression.
27127844	4	32	theme	a3	496:497	arg1	N-glycosylated					537:550	N-glycosylated	537:550	N-glycosylated	537:550	The subunit has conserved, predicted N-glycosylation sites, and the a3 isoform has been directly shown to be N-glycosylated.
27127844	4	32	theme	a3	496:497	arg1	isoform					499:505	the a3 isoform	492:505	the a3 isoform	492:505	The subunit has conserved, predicted N-glycosylation sites, and the a3 isoform has been directly shown to be N-glycosylated.
27127844	5	33	theme	human	568:572	arg1	ATP6V0A4					578:585	ATP6V0A4	578:585	ATP6V0A4	578:585	Here we ask if human a4 (ATP6V0A4) is N-glycosylated at the predicted site, Asn489.
27127844	5	33	theme	human	568:572	arg1	a4					574:575	human a4	568:575	human a4 (ATP6V0A4)	568:586	Here we ask if human a4 (ATP6V0A4) is N-glycosylated at the predicted site, Asn489.
27127844	6	34	theme	pCDNA3.1	677:684	arg1	system					704:709	the pCDNA3.1 expression-vector system	673:709	the pCDNA3.1 expression-vector system	673:709	We transfected HEK 293 cells, using the pCDNA3.1 expression-vector system, to express cDNA constructs of epitope-tagged human a4 subunit, with or without mutations to eliminate the putative glycosylation site.
27127844	12	35	gly	unglycosylated	1559:1572	arg1	a4					1574:1575	unglycosylated a4	1559:1575	unglycosylated a4	1559:1575	Immunofluorescence colocalization data showed that unglycosylated a4 was mostly retained in the ER, and that plasma membrane trafficking was defective.
27127844	11	36	theme	proteasomal	1437:1447	arg1	pathway					1449:1455	the proteasomal pathway	1433:1455	the proteasomal pathway	1433:1455	Unglycosylated a4 was degraded mostly in the proteasomal pathway, but also, in part, through the lysosomal pathway.
27127844	10	37	gly	N-glycosylated	1371:1384	arg1	form					1386:1389	the N-glycosylated form	1367:1389	the N-glycosylated form	1367:1389	Cycloheximide pulse-chase experiments showed that the unglycosylated subunit degraded at a higher rate than the N-glycosylated form.
27127844	6	38	theme	HEK	652:654	arg1	cells					660:664	HEK 293 cells	652:664	HEK 293 cells	652:664	We transfected HEK 293 cells, using the pCDNA3.1 expression-vector system, to express cDNA constructs of epitope-tagged human a4 subunit, with or without mutations to eliminate the putative glycosylation site.
27127844	5	39	theme	predicted	613:621	arg1	site					623:626	the predicted site	609:626	the predicted site	609:626	Here we ask if human a4 (ATP6V0A4) is N-glycosylated at the predicted site, Asn489.
27127844	5	39	theme	predicted	613:621	arg1	Asn489					629:634	Asn489	629:634	Asn489	629:634	Here we ask if human a4 (ATP6V0A4) is N-glycosylated at the predicted site, Asn489.
27127844	10	40	theme	N-glycosylated	1371:1384	arg1	form					1386:1389	the N-glycosylated form	1367:1389	the N-glycosylated form	1367:1389	Cycloheximide pulse-chase experiments showed that the unglycosylated subunit degraded at a higher rate than the N-glycosylated form.
27127844	10	41	theme	pulse-chase	1273:1283	arg1	experiments					1285:1295	Cycloheximide pulse-chase experiments	1259:1295	Cycloheximide pulse-chase experiments	1259:1295	Cycloheximide pulse-chase experiments showed that the unglycosylated subunit degraded at a higher rate than the N-glycosylated form.
27127844	10	42	theme	Cycloheximide	1259:1271	arg1	experiments					1285:1295	Cycloheximide pulse-chase experiments	1259:1295	Cycloheximide pulse-chase experiments	1259:1295	Cycloheximide pulse-chase experiments showed that the unglycosylated subunit degraded at a higher rate than the N-glycosylated form.
27127844	9	43	theme	a4	1231:1232	arg1	subunit					1234:1240	the a4 subunit	1227:1240	the a4 subunit	1227:1240	This relative mobility was identical to that of unglycosylated mutant a4N489D , demonstrating that the a4 subunit is glycosylated.
27127844	0	44	theme	Vacuolar	39:46	arg1	V-ATPase					60:67	V-ATPase	60:67	V-ATPase	60:67	N-Linked Glycosylation Is Required for Vacuolar H+ -ATPase (V-ATPase) a4 Subunit Stability, Assembly, and Cell Surface Expression.
27127844	0	44	theme	Vacuolar	39:46	arg1	-ATPase					51:57	Vacuolar H+ -ATPase	39:57	Vacuolar H+ -ATPase (V-ATPase) a4 Subunit Stability	39:89	N-Linked Glycosylation Is Required for Vacuolar H+ -ATPase (V-ATPase) a4 Subunit Stability, Assembly, and Cell Surface Expression.
27127844	14	45	theme	a4	1838:1839	arg1	stability					1841:1849	a4 stability	1838:1849	a4 stability	1838:1849	Taken together, these data show that N-glycosylation plays a crucial role in a4 stability, and in V-ATPase assembly and trafficking to the plasma membrane.
27127844	0	46	theme	Surface	111:117	arg1	Expression					119:128	Cell Surface Expression	106:128	Cell Surface Expression	106:128	N-Linked Glycosylation Is Required for Vacuolar H+ -ATPase (V-ATPase) a4 Subunit Stability, Assembly, and Cell Surface Expression.
27127844	9	47	theme	unglycosylated	1176:1189	arg1	a4N489D					1198:1204	unglycosylated mutant a4N489D	1176:1204	unglycosylated mutant a4N489D	1176:1204	This relative mobility was identical to that of unglycosylated mutant a4N489D , demonstrating that the a4 subunit is glycosylated.
27127844	17	48	dep	2757-2768	1940:1948	arg1	117					1935:1937	117	1935:1937	117	1935:1937	117: 2757-2768, 2016.
27127844	1	49	theme	different	166:174	arg1	subunits					176:183	14 different subunits	163:183	14 different subunits that make up the V-ATPase complex	163:217	The a subunit is the largest of 14 different subunits that make up the V-ATPase complex.
27127844	12	50	theme	unglycosylated	1559:1572	arg1	a4					1574:1575	unglycosylated a4	1559:1575	unglycosylated a4	1559:1575	Immunofluorescence colocalization data showed that unglycosylated a4 was mostly retained in the ER, and that plasma membrane trafficking was defective.
27127844	0	51	theme	Cell	106:109	arg1	Expression					119:128	Cell Surface Expression	106:128	Cell Surface Expression	106:128	N-Linked Glycosylation Is Required for Vacuolar H+ -ATPase (V-ATPase) a4 Subunit Stability, Assembly, and Cell Surface Expression.
27127844	6	52	theme	subunit	766:772	arg1	constructs					728:737	cDNA constructs	723:737	cDNA constructs of epitope-tagged human a4 subunit	723:772	We transfected HEK 293 cells, using the pCDNA3.1 expression-vector system, to express cDNA constructs of epitope-tagged human a4 subunit, with or without mutations to eliminate the putative glycosylation site.
27127844	10	53	theme	unglycosylated	1313:1326	arg1	subunit					1328:1334	the unglycosylated subunit	1309:1334	the unglycosylated subunit	1309:1334	Cycloheximide pulse-chase experiments showed that the unglycosylated subunit degraded at a higher rate than the N-glycosylated form.
27127844	0	54	theme	-ATPase	51:57	arg1	Stability					81:89	Vacuolar H+ -ATPase (V-ATPase) a4 Subunit Stability	39:89	Vacuolar H+ -ATPase (V-ATPase) a4 Subunit Stability	39:89	N-Linked Glycosylation Is Required for Vacuolar H+ -ATPase (V-ATPase) a4 Subunit Stability, Assembly, and Cell Surface Expression.
27127844	4	55	theme	N-glycosylation	465:479	arg1	sites					481:485	conserved, predicted N-glycosylation sites	444:485	sites	481:485	The subunit has conserved, predicted N-glycosylation sites, and the a3 isoform has been directly shown to be N-glycosylated.
27127844	8	56	theme	increased	1053:1061	arg1	mobility					1072:1079	increased relative mobility	1053:1079	increased relative mobility on immunoblots	1053:1094	Endoglycosidase-treated wild type (WT) a4 showed increased relative mobility on immunoblots, compared with untreated WT a4.
27127844	6	57	theme	a4	763:764	arg1	subunit					766:772	epitope-tagged human a4 subunit	742:772	epitope-tagged human a4 subunit	742:772	We transfected HEK 293 cells, using the pCDNA3.1 expression-vector system, to express cDNA constructs of epitope-tagged human a4 subunit, with or without mutations to eliminate the putative glycosylation site.
27127844	2	58	contain	has	263:265	arg2	isoforms					283:290	four paralogous isoforms	267:290	four paralogous isoforms	267:290	In mammalian species this membrane protein has four paralogous isoforms, a1-a4.
27127844	2	58	contain	has	263:265	arg1	protein					255:261	this membrane protein	241:261	this membrane protein	241:261	In mammalian species this membrane protein has four paralogous isoforms, a1-a4.
27127844	2	58	contain	has	263:265	arg2	a1-a4					293:297	a1-a4	293:297	a1-a4	293:297	In mammalian species this membrane protein has four paralogous isoforms, a1-a4.
27127844	0	59	theme	H+	48:49	arg1	V-ATPase					60:67	V-ATPase	60:67	V-ATPase	60:67	N-Linked Glycosylation Is Required for Vacuolar H+ -ATPase (V-ATPase) a4 Subunit Stability, Assembly, and Cell Surface Expression.
27127844	0	59	theme	H+	48:49	arg1	-ATPase					51:57	Vacuolar H+ -ATPase	39:57	Vacuolar H+ -ATPase (V-ATPase) a4 Subunit Stability	39:89	N-Linked Glycosylation Is Required for Vacuolar H+ -ATPase (V-ATPase) a4 Subunit Stability, Assembly, and Cell Surface Expression.
27127844	14	60	theme	V-ATPase	1859:1866	arg1	assembly					1868:1875	V-ATPase assembly	1859:1875	V-ATPase assembly	1859:1875	Taken together, these data show that N-glycosylation plays a crucial role in a4 stability, and in V-ATPase assembly and trafficking to the plasma membrane.
27127844	6	61	theme	glycosylation	827:839	arg1	site					841:844	the putative glycosylation site	814:844	the putative glycosylation site	814:844	We transfected HEK 293 cells, using the pCDNA3.1 expression-vector system, to express cDNA constructs of epitope-tagged human a4 subunit, with or without mutations to eliminate the putative glycosylation site.
27127844	6	62	theme	human	757:761	arg1	subunit					766:772	epitope-tagged human a4 subunit	742:772	epitope-tagged human a4 subunit	742:772	We transfected HEK 293 cells, using the pCDNA3.1 expression-vector system, to express cDNA constructs of epitope-tagged human a4 subunit, with or without mutations to eliminate the putative glycosylation site.
27127844	11	63	theme	lysosomal	1489:1497	arg1	pathway					1499:1505	the lysosomal pathway	1485:1505	the lysosomal pathway	1485:1505	Unglycosylated a4 was degraded mostly in the proteasomal pathway, but also, in part, through the lysosomal pathway.
27127844	9	64	theme	mutant	1191:1196	arg1	a4N489D					1198:1204	unglycosylated mutant a4N489D	1176:1204	unglycosylated mutant a4N489D	1176:1204	This relative mobility was identical to that of unglycosylated mutant a4N489D , demonstrating that the a4 subunit is glycosylated.
27127844	7	65	with	treatment	887:895	arg1	endoglycosidases					902:917	endoglycosidases	902:917	endoglycosidases	902:917	Glycosylation was characterized also by treatment with endoglycosidases; expression and localization were assessed by immunoblotting and immunofluorescence.
27127844	6	66	theme	epitope-tagged	742:755	arg1	subunit					766:772	epitope-tagged human a4 subunit	742:772	epitope-tagged human a4 subunit	742:772	We transfected HEK 293 cells, using the pCDNA3.1 expression-vector system, to express cDNA constructs of epitope-tagged human a4 subunit, with or without mutations to eliminate the putative glycosylation site.
27127844	9	67	gly	glycosylated	1245:1256	arg1	subunit					1234:1240	the a4 subunit	1227:1240	the a4 subunit	1227:1240	This relative mobility was identical to that of unglycosylated mutant a4N489D , demonstrating that the a4 subunit is glycosylated.
27127844	8	68	theme	untreated	1111:1119	arg1	a4					1124:1125	untreated WT a4	1111:1125	untreated WT a4	1111:1125	Endoglycosidase-treated wild type (WT) a4 showed increased relative mobility on immunoblots, compared with untreated WT a4.
27127844	8	69	theme	relative	1063:1070	arg1	mobility					1072:1079	increased relative mobility	1053:1079	increased relative mobility on immunoblots	1053:1094	Endoglycosidase-treated wild type (WT) a4 showed increased relative mobility on immunoblots, compared with untreated WT a4.
27127844	4	70	gly	N-glycosylation	465:479	arg2	sites					481:485	conserved, predicted N-glycosylation sites	444:485	sites	481:485	The subunit has conserved, predicted N-glycosylation sites, and the a3 isoform has been directly shown to be N-glycosylated.
27127844	14	71	theme	crucial	1822:1828	arg1	role					1830:1833	a crucial role	1820:1833	a crucial role	1820:1833	Taken together, these data show that N-glycosylation plays a crucial role in a4 stability, and in V-ATPase assembly and trafficking to the plasma membrane.
27127844	12	72	theme	Immunofluorescence	1508:1525	arg1	data					1542:1545	Immunofluorescence colocalization data	1508:1545	Immunofluorescence colocalization data	1508:1545	Immunofluorescence colocalization data showed that unglycosylated a4 was mostly retained in the ER, and that plasma membrane trafficking was defective.
27127844	8	73	theme	wild	1028:1031	arg1	WT					1039:1040	WT	1039:1040	WT	1039:1040	Endoglycosidase-treated wild type (WT) a4 showed increased relative mobility on immunoblots, compared with untreated WT a4.
27127844	8	73	theme	wild	1028:1031	arg1	type					1033:1036	Endoglycosidase-treated wild type	1004:1036	Endoglycosidase-treated wild type (WT) a4	1004:1044	Endoglycosidase-treated wild type (WT) a4 showed increased relative mobility on immunoblots, compared with untreated WT a4.
27127844	11	74	gly	Unglycosylated	1392:1405	arg1	a4					1407:1408	Unglycosylated a4	1392:1408	Unglycosylated a4	1392:1408	Unglycosylated a4 was degraded mostly in the proteasomal pathway, but also, in part, through the lysosomal pathway.
27127844	5	75	gly	N-glycosylated	591:604	arg2	Asn489					629:634	Asn489	629:634	Asn489	629:634	Here we ask if human a4 (ATP6V0A4) is N-glycosylated at the predicted site, Asn489.
27127844	5	75	gly	N-glycosylated	591:604	arg2	site					623:626	the predicted site	609:626	the predicted site	609:626	Here we ask if human a4 (ATP6V0A4) is N-glycosylated at the predicted site, Asn489.
27127844	5	75	gly	N-glycosylated	591:604	arg1	ATP6V0A4					578:585	ATP6V0A4	578:585	ATP6V0A4	578:585	Here we ask if human a4 (ATP6V0A4) is N-glycosylated at the predicted site, Asn489.
27127844	5	75	gly	N-glycosylated	591:604	arg1	a4					574:575	human a4	568:575	human a4 (ATP6V0A4)	568:586	Here we ask if human a4 (ATP6V0A4) is N-glycosylated at the predicted site, Asn489.
27127844	3	76	theme	diverse	349:355	arg1	diseases					357:364	diverse diseases	349:364	diverse diseases	349:364	Clinically, a subunit isoforms are implicated in diverse diseases; however, little is known about their structure and function.
27127844	4	77	theme	conserved	444:452	arg1	sites					481:485	conserved, predicted N-glycosylation sites	444:485	sites	481:485	The subunit has conserved, predicted N-glycosylation sites, and the a3 isoform has been directly shown to be N-glycosylated.
27127844	14	78	theme	plasma	1900:1905	arg1	membrane					1907:1914	the plasma membrane	1896:1914	the plasma membrane	1896:1914	Taken together, these data show that N-glycosylation plays a crucial role in a4 stability, and in V-ATPase assembly and trafficking to the plasma membrane.
27127844	12	79	theme	colocalization	1527:1540	arg1	data					1542:1545	Immunofluorescence colocalization data	1508:1545	Immunofluorescence colocalization data	1508:1545	Immunofluorescence colocalization data showed that unglycosylated a4 was mostly retained in the ER, and that plasma membrane trafficking was defective.
27127844	0	80	theme	Subunit	73:79	arg1	Stability					81:89	Vacuolar H+ -ATPase (V-ATPase) a4 Subunit Stability	39:89	Vacuolar H+ -ATPase (V-ATPase) a4 Subunit Stability	39:89	N-Linked Glycosylation Is Required for Vacuolar H+ -ATPase (V-ATPase) a4 Subunit Stability, Assembly, and Cell Surface Expression.
25495042	5	0	gly	glycosylation	812:824	arg1	receptor					863:870	AMPA receptor	858:870	AMPA receptor surface expression	858:889	We next examine the effect of TARP glycosylation on TARP trafficking and also on AMPA receptor surface expression.
25495042	5	0	gly	glycosylation	812:824	arg1	surface					872:878	AMPA receptor surface expression	858:889	AMPA receptor surface expression	858:889	We next examine the effect of TARP glycosylation on TARP trafficking and also on AMPA receptor surface expression.
25495042	5	0	gly	glycosylation	812:824	arg1	TARP					829:832	TARP trafficking	829:844	TARP trafficking	829:844	We next examine the effect of TARP glycosylation on TARP trafficking and also on AMPA receptor surface expression.
25495042	9	1	theme	large	1301:1305	arg1	pool					1307:1310	a large pool	1299:1310	a large pool of immature GluA1	1299:1328	Furthermore, when the maturation of TARP γ-8 is impaired, a large pool of immature GluA1 is retained intracellularly.
25495042	3	2	theme	TARP	486:489	arg1	glycosylation					491:503	TARP glycosylation	486:503	TARP glycosylation	486:503	In the present study, we examined the effect of TARP glycosylation on AMPA receptor trafficking.
25495042	9	3	theme	immature	1315:1322	arg1	GluA1					1324:1328	immature GluA1	1315:1328	immature GluA1	1315:1328	Furthermore, when the maturation of TARP γ-8 is impaired, a large pool of immature GluA1 is retained intracellularly.
25495042	4	4	gly	glycosylation	679:691	arg1	γ-2					701:703	TARP γ-2	696:703	TARP γ-2	696:703	We first showed that TARP γ-8 is an N-glycosylated protein, which contains two glycosylation sites, Asn53 and Asn56, and compared this with the glycosylation of TARP γ-2 and the AMPA receptor auxiliary protein CNIH-2 (cornichon homologue 2).
25495042	6	5	theme	heterologous	993:1004	arg1	cells					1006:1010	heterologous cells	993:1010	heterologous cells	993:1010	We find that TARP γ-8 glycosylation is critical for surface expression of both TARP γ-8 and GluA1 in heterologous cells and neurons.
25495042	3	6	theme	glycosylation	491:503	arg1	effect					476:481	the effect	472:481	the effect of TARP glycosylation on AMPA receptor trafficking	472:532	In the present study, we examined the effect of TARP glycosylation on AMPA receptor trafficking.
25495042	6	7	theme	surface	944:950	arg1	expression					952:961	surface expression	944:961	surface expression of both TARP γ-8 and GluA1 in heterologous cells and neurons	944:1022	We find that TARP γ-8 glycosylation is critical for surface expression of both TARP γ-8 and GluA1 in heterologous cells and neurons.
25495042	7	8	theme	TARP	1052:1055	arg1	γ-8					1057:1059	TARP γ-8	1052:1059	TARP γ-8	1052:1059	Specifically, knockdown of TARP γ-8 causes a decrease in both total and surface AMPA receptors.
25495042	2	9	theme	TARP	300:303	arg1	γ-8					305:307	TARP γ-8	300:307	TARP γ-8	300:307	It has been shown that TARP γ-8 promotes surface expression of AMPA receptors; however, how TARP γ-8 regulates the expression of AMPA receptors remains unclear.
25495042	6	10	theme	GluA1	984:988	arg1	expression					952:961	surface expression	944:961	surface expression of both TARP γ-8 and GluA1 in heterologous cells and neurons	944:1022	We find that TARP γ-8 glycosylation is critical for surface expression of both TARP γ-8 and GluA1 in heterologous cells and neurons.
25495042	4	11	theme	N-glycosylated	571:584	arg1	protein					586:592	an N-glycosylated protein	568:592	an N-glycosylated protein	568:592	We first showed that TARP γ-8 is an N-glycosylated protein, which contains two glycosylation sites, Asn53 and Asn56, and compared this with the glycosylation of TARP γ-2 and the AMPA receptor auxiliary protein CNIH-2 (cornichon homologue 2).
25495042	4	11	theme	N-glycosylated	571:584	arg1	TARP					556:559	TARP γ-8	556:563	TARP γ-8	556:563	We first showed that TARP γ-8 is an N-glycosylated protein, which contains two glycosylation sites, Asn53 and Asn56, and compared this with the glycosylation of TARP γ-2 and the AMPA receptor auxiliary protein CNIH-2 (cornichon homologue 2).
25495042	10	12	theme	complex	1493:1499	arg1	function					1463:1470	function	1463:1470	function	1463:1470	Taken together, our data reveal an important role for the maturation of TARP γ-8 in the trafficking and function of the AMPA receptor complex.
25495042	10	12	theme	complex	1493:1499	arg1	trafficking					1447:1457	trafficking	1447:1457	trafficking	1447:1457	Taken together, our data reveal an important role for the maturation of TARP γ-8 in the trafficking and function of the AMPA receptor complex.
25495042	10	13	from	role	1404:1407	arg1	function					1463:1470	function	1463:1470	function	1463:1470	Taken together, our data reveal an important role for the maturation of TARP γ-8 in the trafficking and function of the AMPA receptor complex.
25495042	10	13	from	role	1404:1407	arg1	trafficking					1447:1457	trafficking	1447:1457	trafficking	1447:1457	Taken together, our data reveal an important role for the maturation of TARP γ-8 in the trafficking and function of the AMPA receptor complex.
25495042	4	14	theme	receptor	718:725	arg1	homologue					763:771	cornichon homologue 2	753:773	cornichon homologue 2	753:773	We first showed that TARP γ-8 is an N-glycosylated protein, which contains two glycosylation sites, Asn53 and Asn56, and compared this with the glycosylation of TARP γ-2 and the AMPA receptor auxiliary protein CNIH-2 (cornichon homologue 2).
25495042	4	14	theme	receptor	718:725	arg1	CNIH-2					745:750	the AMPA receptor auxiliary protein CNIH-2	709:750	the AMPA receptor auxiliary protein CNIH-2 (cornichon homologue 2)	709:774	We first showed that TARP γ-8 is an N-glycosylated protein, which contains two glycosylation sites, Asn53 and Asn56, and compared this with the glycosylation of TARP γ-2 and the AMPA receptor auxiliary protein CNIH-2 (cornichon homologue 2).
25495042	4	15	theme	TARP	696:699	arg1	γ-2					701:703	TARP γ-2	696:703	TARP γ-2	696:703	We first showed that TARP γ-8 is an N-glycosylated protein, which contains two glycosylation sites, Asn53 and Asn56, and compared this with the glycosylation of TARP γ-2 and the AMPA receptor auxiliary protein CNIH-2 (cornichon homologue 2).
25495042	5	16	theme	AMPA	858:861	arg1	receptor					863:870	AMPA receptor	858:870	AMPA receptor surface expression	858:889	We next examine the effect of TARP glycosylation on TARP trafficking and also on AMPA receptor surface expression.
25495042	1	17	theme	receptors	220:228	arg1	subunit					204:210	an auxiliary subunit	191:210	an auxiliary subunit of AMPA receptors that is widely distributed in the hippocampus	191:274	TARP [transmembrane AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor regulatory protein] γ-8 is an auxiliary subunit of AMPA receptors that is widely distributed in the hippocampus.
25495042	1	17	theme	receptors	220:228	arg1	γ-8					184:186	TARP [transmembrane AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor regulatory protein] γ-8	75:186	TARP [transmembrane AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor regulatory protein] γ-8	75:186	TARP [transmembrane AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor regulatory protein] γ-8 is an auxiliary subunit of AMPA receptors that is widely distributed in the hippocampus.
25495042	3	18	gly	glycosylation	491:503	arg1	receptor					513:520	AMPA receptor trafficking	508:532	AMPA receptor trafficking	508:532	In the present study, we examined the effect of TARP glycosylation on AMPA receptor trafficking.
25495042	3	18	gly	glycosylation	491:503	arg1	AMPA					508:511	AMPA receptor trafficking	508:532	AMPA receptor trafficking	508:532	In the present study, we examined the effect of TARP glycosylation on AMPA receptor trafficking.
25495042	5	19	theme	surface	872:878	arg1	expression					880:889	AMPA receptor surface expression	858:889	AMPA receptor surface expression	858:889	We next examine the effect of TARP glycosylation on TARP trafficking and also on AMPA receptor surface expression.
25495042	5	20	theme	TARP	807:810	arg1	glycosylation					812:824	TARP glycosylation	807:824	TARP glycosylation	807:824	We next examine the effect of TARP glycosylation on TARP trafficking and also on AMPA receptor surface expression.
25495042	8	21	from	expression	1138:1147	arg1	neurons					1188:1194	cultured neurons	1179:1194	cultured neurons	1179:1194	We find that the expression of unglycosylated TARP γ-8 in cultured neurons is unable to restore GluA1 expression fully.
25495042	4	22	gly	glycosylation	614:626	arg2	two					610:612	two	610:612	two	610:612	We first showed that TARP γ-8 is an N-glycosylated protein, which contains two glycosylation sites, Asn53 and Asn56, and compared this with the glycosylation of TARP γ-2 and the AMPA receptor auxiliary protein CNIH-2 (cornichon homologue 2).
25495042	4	22	gly	glycosylation	614:626	arg2	Asn56					645:649	Asn56	645:649	Asn56	645:649	We first showed that TARP γ-8 is an N-glycosylated protein, which contains two glycosylation sites, Asn53 and Asn56, and compared this with the glycosylation of TARP γ-2 and the AMPA receptor auxiliary protein CNIH-2 (cornichon homologue 2).
25495042	4	22	gly	glycosylation	614:626	arg2	Asn53					635:639	Asn53	635:639	Asn53	635:639	We first showed that TARP γ-8 is an N-glycosylated protein, which contains two glycosylation sites, Asn53 and Asn56, and compared this with the glycosylation of TARP γ-2 and the AMPA receptor auxiliary protein CNIH-2 (cornichon homologue 2).
25495042	4	22	gly	glycosylation	614:626	arg2	sites					628:632	two glycosylation sites	610:632	two glycosylation sites	610:632	We first showed that TARP γ-8 is an N-glycosylated protein, which contains two glycosylation sites, Asn53 and Asn56, and compared this with the glycosylation of TARP γ-2 and the AMPA receptor auxiliary protein CNIH-2 (cornichon homologue 2).
25495042	6	23	gly	glycosylation	914:926	arg1	surface					944:950	surface expression	944:961	surface expression of both TARP γ-8 and GluA1 in heterologous cells and neurons	944:1022	We find that TARP γ-8 glycosylation is critical for surface expression of both TARP γ-8 and GluA1 in heterologous cells and neurons.
25495042	6	23	gly	glycosylation	914:926	arg1	GluA1					984:988	GluA1	984:988	GluA1	984:988	We find that TARP γ-8 glycosylation is critical for surface expression of both TARP γ-8 and GluA1 in heterologous cells and neurons.
25495042	6	23	gly	glycosylation	914:926	arg1	γ-8					976:978	TARP γ-8	971:978	TARP γ-8	971:978	We find that TARP γ-8 glycosylation is critical for surface expression of both TARP γ-8 and GluA1 in heterologous cells and neurons.
25495042	1	24	theme	TARP	75:78	arg1	subunit					204:210	an auxiliary subunit	191:210	an auxiliary subunit of AMPA receptors that is widely distributed in the hippocampus	191:274	TARP [transmembrane AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor regulatory protein] γ-8 is an auxiliary subunit of AMPA receptors that is widely distributed in the hippocampus.
25495042	1	24	theme	TARP	75:78	arg1	γ-8					184:186	TARP [transmembrane AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor regulatory protein] γ-8	75:186	TARP [transmembrane AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor regulatory protein] γ-8	75:186	TARP [transmembrane AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor regulatory protein] γ-8 is an auxiliary subunit of AMPA receptors that is widely distributed in the hippocampus.
25495042	1	25	theme	auxiliary	194:202	arg1	subunit					204:210	an auxiliary subunit	191:210	an auxiliary subunit of AMPA receptors that is widely distributed in the hippocampus	191:274	TARP [transmembrane AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor regulatory protein] γ-8 is an auxiliary subunit of AMPA receptors that is widely distributed in the hippocampus.
25495042	1	25	theme	auxiliary	194:202	arg1	γ-8					184:186	TARP [transmembrane AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor regulatory protein] γ-8	75:186	TARP [transmembrane AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor regulatory protein] γ-8	75:186	TARP [transmembrane AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor regulatory protein] γ-8 is an auxiliary subunit of AMPA receptors that is widely distributed in the hippocampus.
25495042	7	26	theme	AMPA	1105:1108	arg1	receptors					1110:1118	surface AMPA receptors	1097:1118	surface AMPA receptors	1097:1118	Specifically, knockdown of TARP γ-8 causes a decrease in both total and surface AMPA receptors.
25495042	6	27	theme	TARP	905:908	arg1	glycosylation					914:926	TARP γ-8 glycosylation	905:926	TARP γ-8 glycosylation	905:926	We find that TARP γ-8 glycosylation is critical for surface expression of both TARP γ-8 and GluA1 in heterologous cells and neurons.
25495042	6	28	from	expression	952:961	arg1	neurons					1016:1022	neurons	1016:1022	neurons	1016:1022	We find that TARP γ-8 glycosylation is critical for surface expression of both TARP γ-8 and GluA1 in heterologous cells and neurons.
25495042	6	28	from	expression	952:961	arg1	cells					1006:1010	heterologous cells	993:1010	heterologous cells	993:1010	We find that TARP γ-8 glycosylation is critical for surface expression of both TARP γ-8 and GluA1 in heterologous cells and neurons.
25495042	1	29	theme	[transmembrane	80:93	arg1	subunit					204:210	an auxiliary subunit	191:210	an auxiliary subunit of AMPA receptors that is widely distributed in the hippocampus	191:274	TARP [transmembrane AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor regulatory protein] γ-8 is an auxiliary subunit of AMPA receptors that is widely distributed in the hippocampus.
25495042	1	29	theme	[transmembrane	80:93	arg1	γ-8					184:186	TARP [transmembrane AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor regulatory protein] γ-8	75:186	TARP [transmembrane AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor regulatory protein] γ-8	75:186	TARP [transmembrane AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor regulatory protein] γ-8 is an auxiliary subunit of AMPA receptors that is widely distributed in the hippocampus.
25495042	8	30	theme	cultured	1179:1186	arg1	neurons					1188:1194	cultured neurons	1179:1194	cultured neurons	1179:1194	We find that the expression of unglycosylated TARP γ-8 in cultured neurons is unable to restore GluA1 expression fully.
25495042	0	31	theme	TARP	0:3	arg1	glycosylation					9:21	TARP γ-8 glycosylation	0:21	TARP γ-8 glycosylation	0:21	TARP γ-8 glycosylation regulates the surface expression of AMPA receptors.
25495042	8	32	theme	γ-8	1172:1174	arg1	expression					1138:1147	the expression	1134:1147	the expression of unglycosylated TARP γ-8 in cultured neurons	1134:1194	We find that the expression of unglycosylated TARP γ-8 in cultured neurons is unable to restore GluA1 expression fully.
25495042	8	32	theme	γ-8	1172:1174	arg1	unable					1199:1204	unable	1199:1204	unable	1199:1204	We find that the expression of unglycosylated TARP γ-8 in cultured neurons is unable to restore GluA1 expression fully.
25495042	3	33	from	effect	476:481	arg1	trafficking					522:532	AMPA receptor trafficking	508:532	AMPA receptor trafficking	508:532	In the present study, we examined the effect of TARP glycosylation on AMPA receptor trafficking.
25495042	1	34	theme	AMPA	95:98	arg1	subunit					204:210	an auxiliary subunit	191:210	an auxiliary subunit of AMPA receptors that is widely distributed in the hippocampus	191:274	TARP [transmembrane AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor regulatory protein] γ-8 is an auxiliary subunit of AMPA receptors that is widely distributed in the hippocampus.
25495042	1	34	theme	AMPA	95:98	arg1	γ-8					184:186	TARP [transmembrane AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor regulatory protein] γ-8	75:186	TARP [transmembrane AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor regulatory protein] γ-8	75:186	TARP [transmembrane AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor regulatory protein] γ-8 is an auxiliary subunit of AMPA receptors that is widely distributed in the hippocampus.
25495042	4	35	theme	auxiliary	727:735	arg1	homologue					763:771	cornichon homologue 2	753:773	cornichon homologue 2	753:773	We first showed that TARP γ-8 is an N-glycosylated protein, which contains two glycosylation sites, Asn53 and Asn56, and compared this with the glycosylation of TARP γ-2 and the AMPA receptor auxiliary protein CNIH-2 (cornichon homologue 2).
25495042	4	35	theme	auxiliary	727:735	arg1	CNIH-2					745:750	the AMPA receptor auxiliary protein CNIH-2	709:750	the AMPA receptor auxiliary protein CNIH-2 (cornichon homologue 2)	709:774	We first showed that TARP γ-8 is an N-glycosylated protein, which contains two glycosylation sites, Asn53 and Asn56, and compared this with the glycosylation of TARP γ-2 and the AMPA receptor auxiliary protein CNIH-2 (cornichon homologue 2).
25495042	5	36	theme	TARP	829:832	arg1	trafficking					834:844	TARP trafficking	829:844	TARP trafficking	829:844	We next examine the effect of TARP glycosylation on TARP trafficking and also on AMPA receptor surface expression.
25495042	10	37	theme	receptor	1484:1491	arg1	complex					1493:1499	the AMPA receptor complex	1475:1499	the AMPA receptor complex	1475:1499	Taken together, our data reveal an important role for the maturation of TARP γ-8 in the trafficking and function of the AMPA receptor complex.
25495042	4	38	theme	γ-2	701:703	arg1	homologue					763:771	cornichon homologue 2	753:773	cornichon homologue 2	753:773	We first showed that TARP γ-8 is an N-glycosylated protein, which contains two glycosylation sites, Asn53 and Asn56, and compared this with the glycosylation of TARP γ-2 and the AMPA receptor auxiliary protein CNIH-2 (cornichon homologue 2).
25495042	4	38	theme	γ-2	701:703	arg1	glycosylation					679:691	the glycosylation	675:691	the glycosylation of TARP γ-2	675:703	We first showed that TARP γ-8 is an N-glycosylated protein, which contains two glycosylation sites, Asn53 and Asn56, and compared this with the glycosylation of TARP γ-2 and the AMPA receptor auxiliary protein CNIH-2 (cornichon homologue 2).
25495042	4	38	theme	γ-2	701:703	arg1	CNIH-2					745:750	the AMPA receptor auxiliary protein CNIH-2	709:750	the AMPA receptor auxiliary protein CNIH-2 (cornichon homologue 2)	709:774	We first showed that TARP γ-8 is an N-glycosylated protein, which contains two glycosylation sites, Asn53 and Asn56, and compared this with the glycosylation of TARP γ-2 and the AMPA receptor auxiliary protein CNIH-2 (cornichon homologue 2).
25495042	4	39	gly	N-glycosylated	571:584	arg1	protein					586:592	an N-glycosylated protein	568:592	an N-glycosylated protein	568:592	We first showed that TARP γ-8 is an N-glycosylated protein, which contains two glycosylation sites, Asn53 and Asn56, and compared this with the glycosylation of TARP γ-2 and the AMPA receptor auxiliary protein CNIH-2 (cornichon homologue 2).
25495042	4	39	gly	N-glycosylated	571:584	arg1	TARP					556:559	TARP γ-8	556:563	TARP γ-8	556:563	We first showed that TARP γ-8 is an N-glycosylated protein, which contains two glycosylation sites, Asn53 and Asn56, and compared this with the glycosylation of TARP γ-2 and the AMPA receptor auxiliary protein CNIH-2 (cornichon homologue 2).
25495042	4	40	theme	AMPA	713:716	arg1	homologue					763:771	cornichon homologue 2	753:773	cornichon homologue 2	753:773	We first showed that TARP γ-8 is an N-glycosylated protein, which contains two glycosylation sites, Asn53 and Asn56, and compared this with the glycosylation of TARP γ-2 and the AMPA receptor auxiliary protein CNIH-2 (cornichon homologue 2).
25495042	4	40	theme	AMPA	713:716	arg1	CNIH-2					745:750	the AMPA receptor auxiliary protein CNIH-2	709:750	the AMPA receptor auxiliary protein CNIH-2 (cornichon homologue 2)	709:774	We first showed that TARP γ-8 is an N-glycosylated protein, which contains two glycosylation sites, Asn53 and Asn56, and compared this with the glycosylation of TARP γ-2 and the AMPA receptor auxiliary protein CNIH-2 (cornichon homologue 2).
25495042	1	41	theme	AMPA	215:218	arg1	receptors					220:228	AMPA receptors	215:228	AMPA receptors	215:228	TARP [transmembrane AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor regulatory protein] γ-8 is an auxiliary subunit of AMPA receptors that is widely distributed in the hippocampus.
25495042	2	42	theme	surface	318:324	arg1	expression					326:335	surface expression	318:335	surface expression of AMPA receptors	318:353	It has been shown that TARP γ-8 promotes surface expression of AMPA receptors; however, how TARP γ-8 regulates the expression of AMPA receptors remains unclear.
25495042	3	43	theme	receptor	513:520	arg1	trafficking					522:532	AMPA receptor trafficking	508:532	AMPA receptor trafficking	508:532	In the present study, we examined the effect of TARP glycosylation on AMPA receptor trafficking.
25495042	1	44	theme	α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic	101:147	arg1	protein					175:181	α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor regulatory protein	101:181	TARP [transmembrane AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor regulatory protein] γ-8	75:186	TARP [transmembrane AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor regulatory protein] γ-8 is an auxiliary subunit of AMPA receptors that is widely distributed in the hippocampus.
25495042	2	45	theme	receptors	411:419	arg1	expression					392:401	the expression	388:401	the expression of AMPA receptors	388:419	It has been shown that TARP γ-8 promotes surface expression of AMPA receptors; however, how TARP γ-8 regulates the expression of AMPA receptors remains unclear.
25495042	0	46	theme	surface	37:43	arg1	expression					45:54	the surface expression	33:54	the surface expression of AMPA receptors	33:72	TARP γ-8 glycosylation regulates the surface expression of AMPA receptors.
25495042	5	47	theme	receptor	863:870	arg1	expression					880:889	AMPA receptor surface expression	858:889	AMPA receptor surface expression	858:889	We next examine the effect of TARP glycosylation on TARP trafficking and also on AMPA receptor surface expression.
25495042	10	48	theme	important	1394:1402	arg1	role					1404:1407	an important role	1391:1407	an important role for the maturation of TARP γ-8 in the trafficking and function of the AMPA receptor complex	1391:1499	Taken together, our data reveal an important role for the maturation of TARP γ-8 in the trafficking and function of the AMPA receptor complex.
25495042	3	49	theme	present	445:451	arg1	study					453:457	the present study	441:457	the present study	441:457	In the present study, we examined the effect of TARP glycosylation on AMPA receptor trafficking.
25495042	9	50	theme	TARP	1277:1280	arg1	impaired					1289:1296	impaired	1289:1296	impaired	1289:1296	Furthermore, when the maturation of TARP γ-8 is impaired, a large pool of immature GluA1 is retained intracellularly.
25495042	9	50	theme	TARP	1277:1280	arg1	maturation					1263:1272	the maturation	1259:1272	the maturation of TARP γ-8	1259:1284	Furthermore, when the maturation of TARP γ-8 is impaired, a large pool of immature GluA1 is retained intracellularly.
25495042	2	51	theme	AMPA	406:409	arg1	receptors					411:419	AMPA receptors	406:419	AMPA receptors	406:419	It has been shown that TARP γ-8 promotes surface expression of AMPA receptors; however, how TARP γ-8 regulates the expression of AMPA receptors remains unclear.
25495042	8	52	theme	TARP	1167:1170	arg1	γ-8					1172:1174	unglycosylated TARP γ-8	1152:1174	unglycosylated TARP γ-8	1152:1174	We find that the expression of unglycosylated TARP γ-8 in cultured neurons is unable to restore GluA1 expression fully.
25495042	9	53	theme	GluA1	1324:1328	arg1	pool					1307:1310	a large pool	1299:1310	a large pool of immature GluA1	1299:1328	Furthermore, when the maturation of TARP γ-8 is impaired, a large pool of immature GluA1 is retained intracellularly.
25495042	5	54	from	effect	797:802	arg1	trafficking					834:844	TARP trafficking	829:844	TARP trafficking	829:844	We next examine the effect of TARP glycosylation on TARP trafficking and also on AMPA receptor surface expression.
25495042	5	54	from	effect	797:802	arg1	expression					880:889	AMPA receptor surface expression	858:889	AMPA receptor surface expression	858:889	We next examine the effect of TARP glycosylation on TARP trafficking and also on AMPA receptor surface expression.
25495042	8	55	theme	GluA1	1217:1221	arg1	expression					1223:1232	GluA1 expression	1217:1232	GluA1 expression	1217:1232	We find that the expression of unglycosylated TARP γ-8 in cultured neurons is unable to restore GluA1 expression fully.
25495042	10	56	theme	TARP	1431:1434	arg1	maturation					1417:1426	the maturation	1413:1426	the maturation of TARP γ-8	1413:1438	Taken together, our data reveal an important role for the maturation of TARP γ-8 in the trafficking and function of the AMPA receptor complex.
25495042	1	57	theme	acid	149:152	arg1	protein					175:181	α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor regulatory protein	101:181	TARP [transmembrane AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor regulatory protein] γ-8	75:186	TARP [transmembrane AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor regulatory protein] γ-8 is an auxiliary subunit of AMPA receptors that is widely distributed in the hippocampus.
25495042	2	58	theme	receptors	345:353	arg1	expression					326:335	surface expression	318:335	surface expression of AMPA receptors	318:353	It has been shown that TARP γ-8 promotes surface expression of AMPA receptors; however, how TARP γ-8 regulates the expression of AMPA receptors remains unclear.
25495042	8	59	gly	unglycosylated	1152:1165	arg1	γ-8					1172:1174	unglycosylated TARP γ-8	1152:1174	unglycosylated TARP γ-8	1152:1174	We find that the expression of unglycosylated TARP γ-8 in cultured neurons is unable to restore GluA1 expression fully.
25495042	1	60	theme	protein	175:181	arg1	subunit					204:210	an auxiliary subunit	191:210	an auxiliary subunit of AMPA receptors that is widely distributed in the hippocampus	191:274	TARP [transmembrane AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor regulatory protein] γ-8 is an auxiliary subunit of AMPA receptors that is widely distributed in the hippocampus.
25495042	1	60	theme	protein	175:181	arg1	γ-8					184:186	TARP [transmembrane AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor regulatory protein] γ-8	75:186	TARP [transmembrane AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor regulatory protein] γ-8	75:186	TARP [transmembrane AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor regulatory protein] γ-8 is an auxiliary subunit of AMPA receptors that is widely distributed in the hippocampus.
25495042	4	61	theme	cornichon	753:761	arg1	homologue					763:771	cornichon homologue 2	753:773	cornichon homologue 2	753:773	We first showed that TARP γ-8 is an N-glycosylated protein, which contains two glycosylation sites, Asn53 and Asn56, and compared this with the glycosylation of TARP γ-2 and the AMPA receptor auxiliary protein CNIH-2 (cornichon homologue 2).
25495042	4	61	theme	cornichon	753:761	arg1	CNIH-2					745:750	the AMPA receptor auxiliary protein CNIH-2	709:750	the AMPA receptor auxiliary protein CNIH-2 (cornichon homologue 2)	709:774	We first showed that TARP γ-8 is an N-glycosylated protein, which contains two glycosylation sites, Asn53 and Asn56, and compared this with the glycosylation of TARP γ-2 and the AMPA receptor auxiliary protein CNIH-2 (cornichon homologue 2).
25495042	6	62	theme	TARP	971:974	arg1	γ-8					976:978	TARP γ-8	971:978	TARP γ-8	971:978	We find that TARP γ-8 glycosylation is critical for surface expression of both TARP γ-8 and GluA1 in heterologous cells and neurons.
25495042	1	63	theme	receptor	155:162	arg1	protein					175:181	α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor regulatory protein	101:181	TARP [transmembrane AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor regulatory protein] γ-8	75:186	TARP [transmembrane AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor regulatory protein] γ-8 is an auxiliary subunit of AMPA receptors that is widely distributed in the hippocampus.
25495042	6	64	theme	γ-8	976:978	arg1	expression					952:961	surface expression	944:961	surface expression of both TARP γ-8 and GluA1 in heterologous cells and neurons	944:1022	We find that TARP γ-8 glycosylation is critical for surface expression of both TARP γ-8 and GluA1 in heterologous cells and neurons.
25495042	4	65	theme	protein	737:743	arg1	homologue					763:771	cornichon homologue 2	753:773	cornichon homologue 2	753:773	We first showed that TARP γ-8 is an N-glycosylated protein, which contains two glycosylation sites, Asn53 and Asn56, and compared this with the glycosylation of TARP γ-2 and the AMPA receptor auxiliary protein CNIH-2 (cornichon homologue 2).
25495042	4	65	theme	protein	737:743	arg1	CNIH-2					745:750	the AMPA receptor auxiliary protein CNIH-2	709:750	the AMPA receptor auxiliary protein CNIH-2 (cornichon homologue 2)	709:774	We first showed that TARP γ-8 is an N-glycosylated protein, which contains two glycosylation sites, Asn53 and Asn56, and compared this with the glycosylation of TARP γ-2 and the AMPA receptor auxiliary protein CNIH-2 (cornichon homologue 2).
25495042	4	66	contain	contains	601:608	arg2	Asn56					645:649	Asn56	645:649	Asn56	645:649	We first showed that TARP γ-8 is an N-glycosylated protein, which contains two glycosylation sites, Asn53 and Asn56, and compared this with the glycosylation of TARP γ-2 and the AMPA receptor auxiliary protein CNIH-2 (cornichon homologue 2).
25495042	4	66	contain	contains	601:608	arg1	TARP					556:559	TARP γ-8	556:563	TARP γ-8	556:563	We first showed that TARP γ-8 is an N-glycosylated protein, which contains two glycosylation sites, Asn53 and Asn56, and compared this with the glycosylation of TARP γ-2 and the AMPA receptor auxiliary protein CNIH-2 (cornichon homologue 2).
25495042	4	66	contain	contains	601:608	arg2	Asn53					635:639	Asn53	635:639	Asn53	635:639	We first showed that TARP γ-8 is an N-glycosylated protein, which contains two glycosylation sites, Asn53 and Asn56, and compared this with the glycosylation of TARP γ-2 and the AMPA receptor auxiliary protein CNIH-2 (cornichon homologue 2).
25495042	4	66	contain	contains	601:608	arg1	protein					586:592	an N-glycosylated protein	568:592	an N-glycosylated protein	568:592	We first showed that TARP γ-8 is an N-glycosylated protein, which contains two glycosylation sites, Asn53 and Asn56, and compared this with the glycosylation of TARP γ-2 and the AMPA receptor auxiliary protein CNIH-2 (cornichon homologue 2).
25495042	4	66	contain	contains	601:608	arg2	sites					628:632	two glycosylation sites	610:632	two glycosylation sites	610:632	We first showed that TARP γ-8 is an N-glycosylated protein, which contains two glycosylation sites, Asn53 and Asn56, and compared this with the glycosylation of TARP γ-2 and the AMPA receptor auxiliary protein CNIH-2 (cornichon homologue 2).
25495042	1	67	theme	regulatory	164:173	arg1	protein					175:181	α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor regulatory protein	101:181	TARP [transmembrane AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor regulatory protein] γ-8	75:186	TARP [transmembrane AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor regulatory protein] γ-8 is an auxiliary subunit of AMPA receptors that is widely distributed in the hippocampus.
25495042	8	68	theme	unglycosylated	1152:1165	arg1	γ-8					1172:1174	unglycosylated TARP γ-8	1152:1174	unglycosylated TARP γ-8	1152:1174	We find that the expression of unglycosylated TARP γ-8 in cultured neurons is unable to restore GluA1 expression fully.
25495042	2	69	theme	AMPA	340:343	arg1	receptors					345:353	AMPA receptors	340:353	AMPA receptors	340:353	It has been shown that TARP γ-8 promotes surface expression of AMPA receptors; however, how TARP γ-8 regulates the expression of AMPA receptors remains unclear.
25495042	0	70	theme	receptors	64:72	arg1	expression					45:54	the surface expression	33:54	the surface expression of AMPA receptors	33:72	TARP γ-8 glycosylation regulates the surface expression of AMPA receptors.
25495042	4	71	theme	glycosylation	614:626	arg1	sites					628:632	two glycosylation sites	610:632	two glycosylation sites	610:632	We first showed that TARP γ-8 is an N-glycosylated protein, which contains two glycosylation sites, Asn53 and Asn56, and compared this with the glycosylation of TARP γ-2 and the AMPA receptor auxiliary protein CNIH-2 (cornichon homologue 2).
25495042	4	71	theme	glycosylation	614:626	arg1	Asn56					645:649	Asn56	645:649	Asn56	645:649	We first showed that TARP γ-8 is an N-glycosylated protein, which contains two glycosylation sites, Asn53 and Asn56, and compared this with the glycosylation of TARP γ-2 and the AMPA receptor auxiliary protein CNIH-2 (cornichon homologue 2).
25495042	4	71	theme	glycosylation	614:626	arg1	Asn53					635:639	Asn53	635:639	Asn53	635:639	We first showed that TARP γ-8 is an N-glycosylated protein, which contains two glycosylation sites, Asn53 and Asn56, and compared this with the glycosylation of TARP γ-2 and the AMPA receptor auxiliary protein CNIH-2 (cornichon homologue 2).
25495042	2	72	theme	TARP	369:372	arg1	γ-8					374:376	TARP γ-8	369:376	TARP γ-8	369:376	It has been shown that TARP γ-8 promotes surface expression of AMPA receptors; however, how TARP γ-8 regulates the expression of AMPA receptors remains unclear.
25495042	5	73	theme	glycosylation	812:824	arg1	effect					797:802	the effect	793:802	the effect of TARP glycosylation on TARP trafficking and also on AMPA receptor surface expression	793:889	We next examine the effect of TARP glycosylation on TARP trafficking and also on AMPA receptor surface expression.
25495042	0	74	theme	AMPA	59:62	arg1	receptors					64:72	AMPA receptors	59:72	AMPA receptors	59:72	TARP γ-8 glycosylation regulates the surface expression of AMPA receptors.
25495042	7	75	from	decrease	1070:1077	arg1	total					1087:1091	total	1087:1091	total	1087:1091	Specifically, knockdown of TARP γ-8 causes a decrease in both total and surface AMPA receptors.
25495042	7	75	from	decrease	1070:1077	arg1	receptors					1110:1118	surface AMPA receptors	1097:1118	surface AMPA receptors	1097:1118	Specifically, knockdown of TARP γ-8 causes a decrease in both total and surface AMPA receptors.
25495042	7	76	theme	surface	1097:1103	arg1	receptors					1110:1118	surface AMPA receptors	1097:1118	surface AMPA receptors	1097:1118	Specifically, knockdown of TARP γ-8 causes a decrease in both total and surface AMPA receptors.
25495042	10	77	theme	AMPA	1479:1482	arg1	complex					1493:1499	the AMPA receptor complex	1475:1499	the AMPA receptor complex	1475:1499	Taken together, our data reveal an important role for the maturation of TARP γ-8 in the trafficking and function of the AMPA receptor complex.
25495042	3	78	theme	AMPA	508:511	arg1	trafficking					522:532	AMPA receptor trafficking	508:532	AMPA receptor trafficking	508:532	In the present study, we examined the effect of TARP glycosylation on AMPA receptor trafficking.
25495042	7	79	theme	γ-8	1057:1059	arg1	knockdown					1039:1047	knockdown	1039:1047	knockdown of TARP γ-8	1039:1059	Specifically, knockdown of TARP γ-8 causes a decrease in both total and surface AMPA receptors.
24142515	2	0	link	N-linked	297:304	arg1	sites					320:324	three putative N-linked glycosylation sites	282:324	three putative N-linked glycosylation sites	282:324	The first luminal loop of ABCA3 contains three putative N-linked glycosylation sites at residues 53, 124, and 140.
24142515	0	1	link	N-linked	14:21	arg1	glycosylation					23:35	N-linked glycosylation	14:35	N-linked glycosylation	14:35	Disruption of N-linked glycosylation promotes proteasomal degradation of the human ATP-binding cassette transporter ABCA3.
24142515	4	2	with	constructs	670:679	arg1	cDNAs					719:723	either wild-type or mutant ABCA3 cDNAs	686:723	either wild-type or mutant ABCA3 cDNAs that contained glutamine for asparagine substitutions at the putative glycosylation motifs	686:814	To understand its role in ABCA3 biosynthesis, we utilized EGFP-tagged fusion constructs with either wild-type or mutant ABCA3 cDNAs that contained glutamine for asparagine substitutions at the putative glycosylation motifs.
24142515	8	3	dep	resulted	1467:1474	arg1	accompanied					1555:1565	accompanied	1555:1565	accompanied by reduced overall expression levels	1555:1602	In contrast, substitutions at N124 or N140, as well a N124/N140 double mutation, resulted in increased electrophoretic mobility indicative of a glycosylation deficiency accompanied by reduced overall expression levels.
24142515	3	4	link	N-linked	395:402	arg1	modification					381:392	A common cotranslational modification	356:392	A common cotranslational modification	356:392	A common cotranslational modification, N-linked glycosylation, is critical for the proper expression of glycoproteins by enhancing folding, trafficking, and stability through augmentation of the endoplasmic reticulum (ER) folding cycle.
24142515	3	4	link	N-linked	395:402	arg1	glycosylation					404:416	N-linked glycosylation	395:416	N-linked glycosylation	395:416	A common cotranslational modification, N-linked glycosylation, is critical for the proper expression of glycoproteins by enhancing folding, trafficking, and stability through augmentation of the endoplasmic reticulum (ER) folding cycle.
24142515	10	5	link	N-linked	1777:1784	arg1	glycosylation					1786:1798	cotranslational N-linked glycosylation	1761:1798	cotranslational N-linked glycosylation at N124 and N140	1761:1815	These results suggest that cotranslational N-linked glycosylation at N124 and N140 is critical for ABCA3 stability, and its disruption results in protein destabilization and proteasomal degradation.
24142515	2	6	theme	luminal	251:257	arg1	loop					259:262	The first luminal loop	241:262	The first luminal loop of ABCA3	241:271	The first luminal loop of ABCA3 contains three putative N-linked glycosylation sites at residues 53, 124, and 140.
24142515	1	7	theme	type	181:184	arg1	cells					194:198	alveolar type 2 (AT2) cells	172:198	alveolar type 2 (AT2) cells	172:198	The lipid transport protein, ABCA3, expressed in alveolar type 2 (AT2) cells, is critical for surfactant homeostasis.
24142515	9	8	theme	proteasome	1706:1715	arg1	MG132					1727:1731	the proteasome inhibitor MG132	1702:1731	the proteasome inhibitor MG132	1702:1731	Diminished steady-state levels of glycan-deficient ABCA3 isoforms were rescued by treatment with the proteasome inhibitor MG132.
24142515	2	9	theme	putative	288:295	arg1	sites					320:324	three putative N-linked glycosylation sites	282:324	three putative N-linked glycosylation sites	282:324	The first luminal loop of ABCA3 contains three putative N-linked glycosylation sites at residues 53, 124, and 140.
24142515	8	10	from	N140	1424:1427	arg1	substitutions					1399:1411	substitutions	1399:1411	substitutions at N124 or N140	1399:1427	In contrast, substitutions at N124 or N140, as well a N124/N140 double mutation, resulted in increased electrophoretic mobility indicative of a glycosylation deficiency accompanied by reduced overall expression levels.
24142515	8	10	from	N140	1424:1427	arg1	mutation					1457:1464	a N124/N140 double mutation	1438:1464	a N124/N140 double mutation	1438:1464	In contrast, substitutions at N124 or N140, as well a N124/N140 double mutation, resulted in increased electrophoretic mobility indicative of a glycosylation deficiency accompanied by reduced overall expression levels.
24142515	6	11	theme	residues	1218:1225	arg1	mutation					1192:1199	mutation	1192:1199	mutation of N124 and N140 residues	1192:1225	Fluorescence imaging of transiently transfected A549 or primary human AT2 cells showed that although single motif mutants exhibited a vesicular distribution pattern similar to wild-type ABCA3, mutation of N124 and N140 residues resulted in a shift toward an ER-predominant distribution.
24142515	4	12	theme	mutant	706:711	arg1	cDNAs					719:723	either wild-type or mutant ABCA3 cDNAs	686:723	either wild-type or mutant ABCA3 cDNAs that contained glutamine for asparagine substitutions at the putative glycosylation motifs	686:814	To understand its role in ABCA3 biosynthesis, we utilized EGFP-tagged fusion constructs with either wild-type or mutant ABCA3 cDNAs that contained glutamine for asparagine substitutions at the putative glycosylation motifs.
24142515	8	13	from	N124	1416:1419	arg1	substitutions					1399:1411	substitutions	1399:1411	substitutions at N124 or N140	1399:1427	In contrast, substitutions at N124 or N140, as well a N124/N140 double mutation, resulted in increased electrophoretic mobility indicative of a glycosylation deficiency accompanied by reduced overall expression levels.
24142515	8	13	from	N124	1416:1419	arg1	mutation					1457:1464	a N124/N140 double mutation	1438:1464	a N124/N140 double mutation	1438:1464	In contrast, substitutions at N124 or N140, as well a N124/N140 double mutation, resulted in increased electrophoretic mobility indicative of a glycosylation deficiency accompanied by reduced overall expression levels.
24142515	7	14	theme	ABCA3	1362:1366	arg1	level					1379:1383	ABCA3 expression level	1362:1383	ABCA3 expression level	1362:1383	By immunoblotting, the N53 mutation exhibited no effect on either the Mr or ABCA3 expression level.
24142515	4	15	contain	contained	730:738	arg1	cDNAs					719:723	either wild-type or mutant ABCA3 cDNAs	686:723	either wild-type or mutant ABCA3 cDNAs that contained glutamine for asparagine substitutions at the putative glycosylation motifs	686:814	To understand its role in ABCA3 biosynthesis, we utilized EGFP-tagged fusion constructs with either wild-type or mutant ABCA3 cDNAs that contained glutamine for asparagine substitutions at the putative glycosylation motifs.
24142515	4	15	contain	contained	730:738	arg2	glutamine					740:748	glutamine	740:748	glutamine for asparagine substitutions at the putative glycosylation motifs	740:814	To understand its role in ABCA3 biosynthesis, we utilized EGFP-tagged fusion constructs with either wild-type or mutant ABCA3 cDNAs that contained glutamine for asparagine substitutions at the putative glycosylation motifs.
24142515	10	16	theme	ABCA3	1833:1837	arg1	stability					1839:1847	ABCA3 stability	1833:1847	ABCA3 stability	1833:1847	These results suggest that cotranslational N-linked glycosylation at N124 and N140 is critical for ABCA3 stability, and its disruption results in protein destabilization and proteasomal degradation.
24142515	4	17	from	motifs	809:814	arg1	substitutions					765:777	asparagine substitutions	754:777	asparagine substitutions at the putative glycosylation motifs	754:814	To understand its role in ABCA3 biosynthesis, we utilized EGFP-tagged fusion constructs with either wild-type or mutant ABCA3 cDNAs that contained glutamine for asparagine substitutions at the putative glycosylation motifs.
24142515	1	18	theme	transport	133:141	arg1	protein					143:149	The lipid transport protein	123:149	The lipid transport protein	123:149	The lipid transport protein, ABCA3, expressed in alveolar type 2 (AT2) cells, is critical for surfactant homeostasis.
24142515	1	18	theme	transport	133:141	arg1	critical					204:211	critical	204:211	critical	204:211	The lipid transport protein, ABCA3, expressed in alveolar type 2 (AT2) cells, is critical for surfactant homeostasis.
24142515	1	18	theme	transport	133:141	arg1	ABCA3					152:156	ABCA3	152:156	ABCA3	152:156	The lipid transport protein, ABCA3, expressed in alveolar type 2 (AT2) cells, is critical for surfactant homeostasis.
24142515	8	19	theme	N124/N140	1440:1448	arg1	mutation					1457:1464	a N124/N140 double mutation	1438:1464	a N124/N140 double mutation	1438:1464	In contrast, substitutions at N124 or N140, as well a N124/N140 double mutation, resulted in increased electrophoretic mobility indicative of a glycosylation deficiency accompanied by reduced overall expression levels.
24142515	6	20	theme	primary	1055:1061	arg1	cells					1073:1077	transiently transfected A549 or primary human AT2 cells	1023:1077	cells	1073:1077	Fluorescence imaging of transiently transfected A549 or primary human AT2 cells showed that although single motif mutants exhibited a vesicular distribution pattern similar to wild-type ABCA3, mutation of N124 and N140 residues resulted in a shift toward an ER-predominant distribution.
24142515	4	21	theme	EGFP-tagged	651:661	arg1	constructs					670:679	EGFP-tagged fusion constructs	651:679	EGFP-tagged fusion constructs with either wild-type or mutant ABCA3 cDNAs that contained glutamine for asparagine substitutions at the putative glycosylation motifs	651:814	To understand its role in ABCA3 biosynthesis, we utilized EGFP-tagged fusion constructs with either wild-type or mutant ABCA3 cDNAs that contained glutamine for asparagine substitutions at the putative glycosylation motifs.
24142515	3	22	theme	cycle	586:590	arg1	augmentation					531:542	augmentation	531:542	augmentation of the endoplasmic reticulum (ER) folding cycle	531:590	A common cotranslational modification, N-linked glycosylation, is critical for the proper expression of glycoproteins by enhancing folding, trafficking, and stability through augmentation of the endoplasmic reticulum (ER) folding cycle.
24142515	6	23	theme	Fluorescence	999:1010	arg1	imaging					1012:1018	Fluorescence imaging	999:1018	Fluorescence imaging of transiently transfected A549 or primary human AT2 cells	999:1077	Fluorescence imaging of transiently transfected A549 or primary human AT2 cells showed that although single motif mutants exhibited a vesicular distribution pattern similar to wild-type ABCA3, mutation of N124 and N140 residues resulted in a shift toward an ER-predominant distribution.
24142515	0	24	theme	ATP-binding	83:93	arg1	transporter					104:114	the human ATP-binding cassette transporter ABCA3	73:120	the human ATP-binding cassette transporter ABCA3	73:120	Disruption of N-linked glycosylation promotes proteasomal degradation of the human ATP-binding cassette transporter ABCA3.
24142515	8	25	theme	increased	1479:1487	arg1	mobility					1505:1512	increased electrophoretic mobility	1479:1512	increased electrophoretic mobility indicative of a glycosylation deficiency	1479:1553	In contrast, substitutions at N124 or N140, as well a N124/N140 double mutation, resulted in increased electrophoretic mobility indicative of a glycosylation deficiency accompanied by reduced overall expression levels.
24142515	0	26	theme	transporter	104:114	arg1	degradation					58:68	proteasomal degradation	46:68	proteasomal degradation of the human ATP-binding cassette transporter ABCA3	46:120	Disruption of N-linked glycosylation promotes proteasomal degradation of the human ATP-binding cassette transporter ABCA3.
24142515	5	27	theme	wild-type	955:963	arg1	ABCA3					965:969	wild-type ABCA3	955:969	wild-type ABCA3	955:969	In A549 cells, inhibition of glycosylation by tunicamycin increased the electrophoretic mobility (Mr) and reduced the expression level of wild-type ABCA3 in a dose-dependent manner.
24142515	4	28	theme	asparagine	754:763	arg1	substitutions					765:777	asparagine substitutions	754:777	asparagine substitutions at the putative glycosylation motifs	754:814	To understand its role in ABCA3 biosynthesis, we utilized EGFP-tagged fusion constructs with either wild-type or mutant ABCA3 cDNAs that contained glutamine for asparagine substitutions at the putative glycosylation motifs.
24142515	6	29	theme	cells	1073:1077	arg1	imaging					1012:1018	Fluorescence imaging	999:1018	Fluorescence imaging of transiently transfected A549 or primary human AT2 cells	999:1077	Fluorescence imaging of transiently transfected A549 or primary human AT2 cells showed that although single motif mutants exhibited a vesicular distribution pattern similar to wild-type ABCA3, mutation of N124 and N140 residues resulted in a shift toward an ER-predominant distribution.
24142515	4	30	theme	ABCA3	713:717	arg1	cDNAs					719:723	either wild-type or mutant ABCA3 cDNAs	686:723	either wild-type or mutant ABCA3 cDNAs that contained glutamine for asparagine substitutions at the putative glycosylation motifs	686:814	To understand its role in ABCA3 biosynthesis, we utilized EGFP-tagged fusion constructs with either wild-type or mutant ABCA3 cDNAs that contained glutamine for asparagine substitutions at the putative glycosylation motifs.
24142515	3	31	theme	N-linked	395:402	arg1	modification					381:392	A common cotranslational modification	356:392	A common cotranslational modification	356:392	A common cotranslational modification, N-linked glycosylation, is critical for the proper expression of glycoproteins by enhancing folding, trafficking, and stability through augmentation of the endoplasmic reticulum (ER) folding cycle.
24142515	3	31	theme	N-linked	395:402	arg1	glycosylation					404:416	N-linked glycosylation	395:416	N-linked glycosylation	395:416	A common cotranslational modification, N-linked glycosylation, is critical for the proper expression of glycoproteins by enhancing folding, trafficking, and stability through augmentation of the endoplasmic reticulum (ER) folding cycle.
24142515	4	32	used	utilized	642:649	arg2	we					639:640	we	639:640	we	639:640	To understand its role in ABCA3 biosynthesis, we utilized EGFP-tagged fusion constructs with either wild-type or mutant ABCA3 cDNAs that contained glutamine for asparagine substitutions at the putative glycosylation motifs.
24142515	6	33	theme	human	1063:1067	arg1	cells					1073:1077	transiently transfected A549 or primary human AT2 cells	1023:1077	cells	1073:1077	Fluorescence imaging of transiently transfected A549 or primary human AT2 cells showed that although single motif mutants exhibited a vesicular distribution pattern similar to wild-type ABCA3, mutation of N124 and N140 residues resulted in a shift toward an ER-predominant distribution.
24142515	8	34	theme	glycosylation	1530:1542	arg1	deficiency					1544:1553	a glycosylation deficiency	1528:1553	a glycosylation deficiency	1528:1553	In contrast, substitutions at N124 or N140, as well a N124/N140 double mutation, resulted in increased electrophoretic mobility indicative of a glycosylation deficiency accompanied by reduced overall expression levels.
24142515	0	35	theme	N-linked	14:21	arg1	glycosylation					23:35	N-linked glycosylation	14:35	N-linked glycosylation	14:35	Disruption of N-linked glycosylation promotes proteasomal degradation of the human ATP-binding cassette transporter ABCA3.
24142515	2	36	contain	contains	273:280	arg2	loop					259:262	The first luminal loop	241:262	The first luminal loop of ABCA3	241:271	The first luminal loop of ABCA3 contains three putative N-linked glycosylation sites at residues 53, 124, and 140.
24142515	2	36	contain	contains	273:280	arg1	residues					329:336	residues 53, 124, and 140	329:353	residues 53, 124, and 140	329:353	The first luminal loop of ABCA3 contains three putative N-linked glycosylation sites at residues 53, 124, and 140.
24142515	2	36	contain	contains	273:280	arg1	loop					259:262	The first luminal loop	241:262	The first luminal loop of ABCA3	241:271	The first luminal loop of ABCA3 contains three putative N-linked glycosylation sites at residues 53, 124, and 140.
24142515	2	36	contain	contains	273:280	arg2	sites					320:324	three putative N-linked glycosylation sites	282:324	three putative N-linked glycosylation sites	282:324	The first luminal loop of ABCA3 contains three putative N-linked glycosylation sites at residues 53, 124, and 140.
24142515	9	37	theme	Diminished	1605:1614	arg1	levels					1629:1634	Diminished steady-state levels	1605:1634	Diminished steady-state levels of glycan-deficient ABCA3 isoforms	1605:1669	Diminished steady-state levels of glycan-deficient ABCA3 isoforms were rescued by treatment with the proteasome inhibitor MG132.
24142515	6	38	theme	transfected	1035:1045	arg1	A549					1047:1050	transiently transfected A549 or primary human AT2 cells	1023:1077	A549	1047:1050	Fluorescence imaging of transiently transfected A549 or primary human AT2 cells showed that although single motif mutants exhibited a vesicular distribution pattern similar to wild-type ABCA3, mutation of N124 and N140 residues resulted in a shift toward an ER-predominant distribution.
24142515	3	39	theme	common	358:363	arg1	modification					381:392	A common cotranslational modification	356:392	A common cotranslational modification	356:392	A common cotranslational modification, N-linked glycosylation, is critical for the proper expression of glycoproteins by enhancing folding, trafficking, and stability through augmentation of the endoplasmic reticulum (ER) folding cycle.
24142515	3	39	theme	common	358:363	arg1	glycosylation					404:416	N-linked glycosylation	395:416	N-linked glycosylation	395:416	A common cotranslational modification, N-linked glycosylation, is critical for the proper expression of glycoproteins by enhancing folding, trafficking, and stability through augmentation of the endoplasmic reticulum (ER) folding cycle.
24142515	3	39	theme	common	358:363	arg1	critical					422:429	critical	422:429	critical	422:429	A common cotranslational modification, N-linked glycosylation, is critical for the proper expression of glycoproteins by enhancing folding, trafficking, and stability through augmentation of the endoplasmic reticulum (ER) folding cycle.
24142515	8	40	theme	reduced	1570:1576	arg1	levels					1597:1602	reduced overall expression levels	1570:1602	reduced overall expression levels	1570:1602	In contrast, substitutions at N124 or N140, as well a N124/N140 double mutation, resulted in increased electrophoretic mobility indicative of a glycosylation deficiency accompanied by reduced overall expression levels.
24142515	10	41	theme	protein	1880:1886	arg1	destabilization					1888:1902	protein destabilization	1880:1902	protein destabilization	1880:1902	These results suggest that cotranslational N-linked glycosylation at N124 and N140 is critical for ABCA3 stability, and its disruption results in protein destabilization and proteasomal degradation.
24142515	3	42	theme	glycoproteins	460:472	arg1	expression					446:455	the proper expression	435:455	the proper expression of glycoproteins	435:472	A common cotranslational modification, N-linked glycosylation, is critical for the proper expression of glycoproteins by enhancing folding, trafficking, and stability through augmentation of the endoplasmic reticulum (ER) folding cycle.
24142515	10	43	gly	glycosylation	1786:1798	arg1	N124					1803:1806	N124	1803:1806	N124	1803:1806	These results suggest that cotranslational N-linked glycosylation at N124 and N140 is critical for ABCA3 stability, and its disruption results in protein destabilization and proteasomal degradation.
24142515	10	43	gly	glycosylation	1786:1798	arg1	ABCA3					1833:1837	ABCA3 stability	1833:1847	ABCA3 stability	1833:1847	These results suggest that cotranslational N-linked glycosylation at N124 and N140 is critical for ABCA3 stability, and its disruption results in protein destabilization and proteasomal degradation.
24142515	10	43	gly	glycosylation	1786:1798	arg2	N140					1812:1815	N140	1812:1815	N140	1812:1815	These results suggest that cotranslational N-linked glycosylation at N124 and N140 is critical for ABCA3 stability, and its disruption results in protein destabilization and proteasomal degradation.
24142515	10	43	gly	glycosylation	1786:1798	arg1	N140					1812:1815	N140	1812:1815	N140	1812:1815	These results suggest that cotranslational N-linked glycosylation at N124 and N140 is critical for ABCA3 stability, and its disruption results in protein destabilization and proteasomal degradation.
24142515	10	43	gly	glycosylation	1786:1798	arg2	N124					1803:1806	N124	1803:1806	N124	1803:1806	These results suggest that cotranslational N-linked glycosylation at N124 and N140 is critical for ABCA3 stability, and its disruption results in protein destabilization and proteasomal degradation.
24142515	8	44	theme	expression	1586:1595	arg1	levels					1597:1602	reduced overall expression levels	1570:1602	reduced overall expression levels	1570:1602	In contrast, substitutions at N124 or N140, as well a N124/N140 double mutation, resulted in increased electrophoretic mobility indicative of a glycosylation deficiency accompanied by reduced overall expression levels.
24142515	2	45	gly	glycosylation	306:318	arg2	three					282:286	three	282:286	three	282:286	The first luminal loop of ABCA3 contains three putative N-linked glycosylation sites at residues 53, 124, and 140.
24142515	2	45	gly	glycosylation	306:318	arg2	sites					320:324	three putative N-linked glycosylation sites	282:324	three putative N-linked glycosylation sites	282:324	The first luminal loop of ABCA3 contains three putative N-linked glycosylation sites at residues 53, 124, and 140.
24142515	5	46	from	level	946:950	arg1	manner					991:996	a dose-dependent manner	974:996	a dose-dependent manner	974:996	In A549 cells, inhibition of glycosylation by tunicamycin increased the electrophoretic mobility (Mr) and reduced the expression level of wild-type ABCA3 in a dose-dependent manner.
24142515	5	47	theme	dose-dependent	976:989	arg1	manner					991:996	a dose-dependent manner	974:996	a dose-dependent manner	974:996	In A549 cells, inhibition of glycosylation by tunicamycin increased the electrophoretic mobility (Mr) and reduced the expression level of wild-type ABCA3 in a dose-dependent manner.
24142515	4	48	theme	putative	786:793	arg1	motifs					809:814	the putative glycosylation motifs	782:814	the putative glycosylation motifs	782:814	To understand its role in ABCA3 biosynthesis, we utilized EGFP-tagged fusion constructs with either wild-type or mutant ABCA3 cDNAs that contained glutamine for asparagine substitutions at the putative glycosylation motifs.
24142515	10	49	theme	N-linked	1777:1784	arg1	glycosylation					1786:1798	cotranslational N-linked glycosylation	1761:1798	cotranslational N-linked glycosylation at N124 and N140	1761:1815	These results suggest that cotranslational N-linked glycosylation at N124 and N140 is critical for ABCA3 stability, and its disruption results in protein destabilization and proteasomal degradation.
24142515	5	50	theme	glycosylation	846:858	arg1	inhibition					832:841	inhibition	832:841	inhibition of glycosylation by tunicamycin	832:873	In A549 cells, inhibition of glycosylation by tunicamycin increased the electrophoretic mobility (Mr) and reduced the expression level of wild-type ABCA3 in a dose-dependent manner.
24142515	9	51	theme	isoforms	1662:1669	arg1	levels					1629:1634	Diminished steady-state levels	1605:1634	Diminished steady-state levels of glycan-deficient ABCA3 isoforms	1605:1669	Diminished steady-state levels of glycan-deficient ABCA3 isoforms were rescued by treatment with the proteasome inhibitor MG132.
24142515	6	52	theme	single	1100:1105	arg1	mutants					1113:1119	single motif mutants	1100:1119	single motif mutants	1100:1119	Fluorescence imaging of transiently transfected A549 or primary human AT2 cells showed that although single motif mutants exhibited a vesicular distribution pattern similar to wild-type ABCA3, mutation of N124 and N140 residues resulted in a shift toward an ER-predominant distribution.
24142515	2	53	theme	ABCA3	267:271	arg1	loop					259:262	The first luminal loop	241:262	The first luminal loop of ABCA3	241:271	The first luminal loop of ABCA3 contains three putative N-linked glycosylation sites at residues 53, 124, and 140.
24142515	6	54	theme	ER-predominant	1257:1270	arg1	distribution					1272:1283	an ER-predominant distribution	1254:1283	an ER-predominant distribution	1254:1283	Fluorescence imaging of transiently transfected A549 or primary human AT2 cells showed that although single motif mutants exhibited a vesicular distribution pattern similar to wild-type ABCA3, mutation of N124 and N140 residues resulted in a shift toward an ER-predominant distribution.
24142515	1	55	theme	alveolar	172:179	arg1	type					181:184	alveolar type 2	172:186	alveolar type 2 (AT2) cells	172:198	The lipid transport protein, ABCA3, expressed in alveolar type 2 (AT2) cells, is critical for surfactant homeostasis.
24142515	1	55	theme	alveolar	172:179	arg1	AT2					189:191	AT2	189:191	AT2	189:191	The lipid transport protein, ABCA3, expressed in alveolar type 2 (AT2) cells, is critical for surfactant homeostasis.
24142515	6	56	theme	wild-type	1175:1183	arg1	ABCA3					1185:1189	wild-type ABCA3	1175:1189	wild-type ABCA3	1175:1189	Fluorescence imaging of transiently transfected A549 or primary human AT2 cells showed that although single motif mutants exhibited a vesicular distribution pattern similar to wild-type ABCA3, mutation of N124 and N140 residues resulted in a shift toward an ER-predominant distribution.
24142515	4	57	theme	ABCA3	619:623	arg1	biosynthesis					625:636	ABCA3 biosynthesis	619:636	ABCA3 biosynthesis	619:636	To understand its role in ABCA3 biosynthesis, we utilized EGFP-tagged fusion constructs with either wild-type or mutant ABCA3 cDNAs that contained glutamine for asparagine substitutions at the putative glycosylation motifs.
24142515	2	58	theme	N-linked	297:304	arg1	sites					320:324	three putative N-linked glycosylation sites	282:324	three putative N-linked glycosylation sites	282:324	The first luminal loop of ABCA3 contains three putative N-linked glycosylation sites at residues 53, 124, and 140.
24142515	9	59	theme	inhibitor	1717:1725	arg1	MG132					1727:1731	the proteasome inhibitor MG132	1702:1731	the proteasome inhibitor MG132	1702:1731	Diminished steady-state levels of glycan-deficient ABCA3 isoforms were rescued by treatment with the proteasome inhibitor MG132.
24142515	6	60	theme	similar	1164:1170	arg1	pattern					1156:1162	a vesicular distribution pattern	1131:1162	a vesicular distribution pattern similar to wild-type ABCA3	1131:1189	Fluorescence imaging of transiently transfected A549 or primary human AT2 cells showed that although single motif mutants exhibited a vesicular distribution pattern similar to wild-type ABCA3, mutation of N124 and N140 residues resulted in a shift toward an ER-predominant distribution.
24142515	4	61	from	role	611:614	arg1	biosynthesis					625:636	ABCA3 biosynthesis	619:636	ABCA3 biosynthesis	619:636	To understand its role in ABCA3 biosynthesis, we utilized EGFP-tagged fusion constructs with either wild-type or mutant ABCA3 cDNAs that contained glutamine for asparagine substitutions at the putative glycosylation motifs.
24142515	5	62	theme	A549	820:823	arg1	cells					825:829	A549 cells	820:829	A549 cells	820:829	In A549 cells, inhibition of glycosylation by tunicamycin increased the electrophoretic mobility (Mr) and reduced the expression level of wild-type ABCA3 in a dose-dependent manner.
24142515	3	63	theme	endoplasmic	551:561	arg1	ER					574:575	ER	574:575	ER	574:575	A common cotranslational modification, N-linked glycosylation, is critical for the proper expression of glycoproteins by enhancing folding, trafficking, and stability through augmentation of the endoplasmic reticulum (ER) folding cycle.
24142515	3	63	theme	endoplasmic	551:561	arg1	reticulum					563:571	the endoplasmic reticulum	547:571	the endoplasmic reticulum (ER) folding cycle	547:590	A common cotranslational modification, N-linked glycosylation, is critical for the proper expression of glycoproteins by enhancing folding, trafficking, and stability through augmentation of the endoplasmic reticulum (ER) folding cycle.
24142515	6	64	theme	distribution	1143:1154	arg1	pattern					1156:1162	a vesicular distribution pattern	1131:1162	a vesicular distribution pattern similar to wild-type ABCA3	1131:1189	Fluorescence imaging of transiently transfected A549 or primary human AT2 cells showed that although single motif mutants exhibited a vesicular distribution pattern similar to wild-type ABCA3, mutation of N124 and N140 residues resulted in a shift toward an ER-predominant distribution.
24142515	3	65	theme	reticulum	563:571	arg1	cycle					586:590	the endoplasmic reticulum (ER) folding cycle	547:590	the endoplasmic reticulum (ER) folding cycle	547:590	A common cotranslational modification, N-linked glycosylation, is critical for the proper expression of glycoproteins by enhancing folding, trafficking, and stability through augmentation of the endoplasmic reticulum (ER) folding cycle.
24142515	1	66	theme	lipid	127:131	arg1	protein					143:149	The lipid transport protein	123:149	The lipid transport protein	123:149	The lipid transport protein, ABCA3, expressed in alveolar type 2 (AT2) cells, is critical for surfactant homeostasis.
24142515	1	66	theme	lipid	127:131	arg1	critical					204:211	critical	204:211	critical	204:211	The lipid transport protein, ABCA3, expressed in alveolar type 2 (AT2) cells, is critical for surfactant homeostasis.
24142515	1	66	theme	lipid	127:131	arg1	ABCA3					152:156	ABCA3	152:156	ABCA3	152:156	The lipid transport protein, ABCA3, expressed in alveolar type 2 (AT2) cells, is critical for surfactant homeostasis.
24142515	10	67	theme	cotranslational	1761:1775	arg1	glycosylation					1786:1798	cotranslational N-linked glycosylation	1761:1798	cotranslational N-linked glycosylation at N124 and N140	1761:1815	These results suggest that cotranslational N-linked glycosylation at N124 and N140 is critical for ABCA3 stability, and its disruption results in protein destabilization and proteasomal degradation.
24142515	8	68	theme	double	1450:1455	arg1	mutation					1457:1464	a N124/N140 double mutation	1438:1464	a N124/N140 double mutation	1438:1464	In contrast, substitutions at N124 or N140, as well a N124/N140 double mutation, resulted in increased electrophoretic mobility indicative of a glycosylation deficiency accompanied by reduced overall expression levels.
24142515	7	69	theme	expression	1368:1377	arg1	level					1379:1383	ABCA3 expression level	1362:1383	ABCA3 expression level	1362:1383	By immunoblotting, the N53 mutation exhibited no effect on either the Mr or ABCA3 expression level.
24142515	2	70	theme	first	245:249	arg1	loop					259:262	The first luminal loop	241:262	The first luminal loop of ABCA3	241:271	The first luminal loop of ABCA3 contains three putative N-linked glycosylation sites at residues 53, 124, and 140.
24142515	4	71	theme	wild-type	693:701	arg1	cDNAs					719:723	either wild-type or mutant ABCA3 cDNAs	686:723	either wild-type or mutant ABCA3 cDNAs that contained glutamine for asparagine substitutions at the putative glycosylation motifs	686:814	To understand its role in ABCA3 biosynthesis, we utilized EGFP-tagged fusion constructs with either wild-type or mutant ABCA3 cDNAs that contained glutamine for asparagine substitutions at the putative glycosylation motifs.
24142515	0	72	theme	human	77:81	arg1	transporter					104:114	the human ATP-binding cassette transporter ABCA3	73:120	the human ATP-binding cassette transporter ABCA3	73:120	Disruption of N-linked glycosylation promotes proteasomal degradation of the human ATP-binding cassette transporter ABCA3.
24142515	3	73	theme	folding	578:584	arg1	cycle					586:590	the endoplasmic reticulum (ER) folding cycle	547:590	the endoplasmic reticulum (ER) folding cycle	547:590	A common cotranslational modification, N-linked glycosylation, is critical for the proper expression of glycoproteins by enhancing folding, trafficking, and stability through augmentation of the endoplasmic reticulum (ER) folding cycle.
24142515	10	74	from	N124	1803:1806	arg1	glycosylation					1786:1798	cotranslational N-linked glycosylation	1761:1798	cotranslational N-linked glycosylation at N124 and N140	1761:1815	These results suggest that cotranslational N-linked glycosylation at N124 and N140 is critical for ABCA3 stability, and its disruption results in protein destabilization and proteasomal degradation.
24142515	0	75	theme	cassette	95:102	arg1	transporter					104:114	the human ATP-binding cassette transporter ABCA3	73:120	the human ATP-binding cassette transporter ABCA3	73:120	Disruption of N-linked glycosylation promotes proteasomal degradation of the human ATP-binding cassette transporter ABCA3.
24142515	5	76	theme	electrophoretic	889:903	arg1	Mr					915:916	Mr	915:916	Mr	915:916	In A549 cells, inhibition of glycosylation by tunicamycin increased the electrophoretic mobility (Mr) and reduced the expression level of wild-type ABCA3 in a dose-dependent manner.
24142515	5	76	theme	electrophoretic	889:903	arg1	mobility					905:912	the electrophoretic mobility	885:912	the electrophoretic mobility (Mr)	885:917	In A549 cells, inhibition of glycosylation by tunicamycin increased the electrophoretic mobility (Mr) and reduced the expression level of wild-type ABCA3 in a dose-dependent manner.
24142515	10	77	from	N140	1812:1815	arg1	glycosylation					1786:1798	cotranslational N-linked glycosylation	1761:1798	cotranslational N-linked glycosylation at N124 and N140	1761:1815	These results suggest that cotranslational N-linked glycosylation at N124 and N140 is critical for ABCA3 stability, and its disruption results in protein destabilization and proteasomal degradation.
24142515	8	78	theme	electrophoretic	1489:1503	arg1	mobility					1505:1512	increased electrophoretic mobility	1479:1512	increased electrophoretic mobility indicative of a glycosylation deficiency	1479:1553	In contrast, substitutions at N124 or N140, as well a N124/N140 double mutation, resulted in increased electrophoretic mobility indicative of a glycosylation deficiency accompanied by reduced overall expression levels.
24142515	4	79	theme	fusion	663:668	arg1	constructs					670:679	EGFP-tagged fusion constructs	651:679	EGFP-tagged fusion constructs with either wild-type or mutant ABCA3 cDNAs that contained glutamine for asparagine substitutions at the putative glycosylation motifs	651:814	To understand its role in ABCA3 biosynthesis, we utilized EGFP-tagged fusion constructs with either wild-type or mutant ABCA3 cDNAs that contained glutamine for asparagine substitutions at the putative glycosylation motifs.
24142515	9	80	theme	glycan-deficient	1639:1654	arg1	isoforms					1662:1669	glycan-deficient ABCA3 isoforms	1639:1669	glycan-deficient ABCA3 isoforms	1639:1669	Diminished steady-state levels of glycan-deficient ABCA3 isoforms were rescued by treatment with the proteasome inhibitor MG132.
24142515	8	81	theme	indicative	1514:1523	arg1	mobility					1505:1512	increased electrophoretic mobility	1479:1512	increased electrophoretic mobility indicative of a glycosylation deficiency	1479:1553	In contrast, substitutions at N124 or N140, as well a N124/N140 double mutation, resulted in increased electrophoretic mobility indicative of a glycosylation deficiency accompanied by reduced overall expression levels.
24142515	5	82	theme	ABCA3	965:969	arg1	level					946:950	the expression level	931:950	the expression level of wild-type ABCA3 in a dose-dependent manner	931:996	In A549 cells, inhibition of glycosylation by tunicamycin increased the electrophoretic mobility (Mr) and reduced the expression level of wild-type ABCA3 in a dose-dependent manner.
24142515	4	83	gly	glycosylation	795:807	arg2	motifs					809:814	the putative glycosylation motifs	782:814	the putative glycosylation motifs	782:814	To understand its role in ABCA3 biosynthesis, we utilized EGFP-tagged fusion constructs with either wild-type or mutant ABCA3 cDNAs that contained glutamine for asparagine substitutions at the putative glycosylation motifs.
24142515	6	84	theme	AT2	1069:1071	arg1	cells					1073:1077	transiently transfected A549 or primary human AT2 cells	1023:1077	cells	1073:1077	Fluorescence imaging of transiently transfected A549 or primary human AT2 cells showed that although single motif mutants exhibited a vesicular distribution pattern similar to wild-type ABCA3, mutation of N124 and N140 residues resulted in a shift toward an ER-predominant distribution.
24142515	8	85	theme	deficiency	1544:1553	arg1	indicative					1514:1523	indicative	1514:1523	indicative	1514:1523	In contrast, substitutions at N124 or N140, as well a N124/N140 double mutation, resulted in increased electrophoretic mobility indicative of a glycosylation deficiency accompanied by reduced overall expression levels.
24142515	3	86	gly	glycoproteins	460:472	arg1	glycoproteins					460:472	glycoproteins	460:472	glycoproteins	460:472	A common cotranslational modification, N-linked glycosylation, is critical for the proper expression of glycoproteins by enhancing folding, trafficking, and stability through augmentation of the endoplasmic reticulum (ER) folding cycle.
24142515	0	87	theme	glycosylation	23:35	arg1	Disruption					0:9	Disruption	0:9	Disruption of N-linked glycosylation	0:35	Disruption of N-linked glycosylation promotes proteasomal degradation of the human ATP-binding cassette transporter ABCA3.
24142515	5	88	theme	expression	935:944	arg1	level					946:950	the expression level	931:950	the expression level of wild-type ABCA3 in a dose-dependent manner	931:996	In A549 cells, inhibition of glycosylation by tunicamycin increased the electrophoretic mobility (Mr) and reduced the expression level of wild-type ABCA3 in a dose-dependent manner.
24142515	7	89	theme	N53	1309:1311	arg1	mutation					1313:1320	the N53 mutation	1305:1320	the N53 mutation	1305:1320	By immunoblotting, the N53 mutation exhibited no effect on either the Mr or ABCA3 expression level.
24142515	10	90	theme	proteasomal	1908:1918	arg1	degradation					1920:1930	proteasomal degradation	1908:1930	proteasomal degradation	1908:1930	These results suggest that cotranslational N-linked glycosylation at N124 and N140 is critical for ABCA3 stability, and its disruption results in protein destabilization and proteasomal degradation.
24142515	3	91	theme	proper	439:444	arg1	expression					446:455	the proper expression	435:455	the proper expression of glycoproteins	435:472	A common cotranslational modification, N-linked glycosylation, is critical for the proper expression of glycoproteins by enhancing folding, trafficking, and stability through augmentation of the endoplasmic reticulum (ER) folding cycle.
24142515	0	92	theme	proteasomal	46:56	arg1	degradation					58:68	proteasomal degradation	46:68	proteasomal degradation of the human ATP-binding cassette transporter ABCA3	46:120	Disruption of N-linked glycosylation promotes proteasomal degradation of the human ATP-binding cassette transporter ABCA3.
24142515	6	93	theme	A549	1047:1050	arg1	imaging					1012:1018	Fluorescence imaging	999:1018	Fluorescence imaging of transiently transfected A549 or primary human AT2 cells	999:1077	Fluorescence imaging of transiently transfected A549 or primary human AT2 cells showed that although single motif mutants exhibited a vesicular distribution pattern similar to wild-type ABCA3, mutation of N124 and N140 residues resulted in a shift toward an ER-predominant distribution.
24142515	8	94	theme	overall	1578:1584	arg1	levels					1597:1602	reduced overall expression levels	1570:1602	reduced overall expression levels	1570:1602	In contrast, substitutions at N124 or N140, as well a N124/N140 double mutation, resulted in increased electrophoretic mobility indicative of a glycosylation deficiency accompanied by reduced overall expression levels.
24142515	4	95	theme	glycosylation	795:807	arg1	motifs					809:814	the putative glycosylation motifs	782:814	the putative glycosylation motifs	782:814	To understand its role in ABCA3 biosynthesis, we utilized EGFP-tagged fusion constructs with either wild-type or mutant ABCA3 cDNAs that contained glutamine for asparagine substitutions at the putative glycosylation motifs.
24142515	9	96	theme	steady-state	1616:1627	arg1	levels					1629:1634	Diminished steady-state levels	1605:1634	Diminished steady-state levels of glycan-deficient ABCA3 isoforms	1605:1669	Diminished steady-state levels of glycan-deficient ABCA3 isoforms were rescued by treatment with the proteasome inhibitor MG132.
24142515	6	97	theme	vesicular	1133:1141	arg1	pattern					1156:1162	a vesicular distribution pattern	1131:1162	a vesicular distribution pattern similar to wild-type ABCA3	1131:1189	Fluorescence imaging of transiently transfected A549 or primary human AT2 cells showed that although single motif mutants exhibited a vesicular distribution pattern similar to wild-type ABCA3, mutation of N124 and N140 residues resulted in a shift toward an ER-predominant distribution.
24142515	3	98	theme	cotranslational	365:379	arg1	modification					381:392	A common cotranslational modification	356:392	A common cotranslational modification	356:392	A common cotranslational modification, N-linked glycosylation, is critical for the proper expression of glycoproteins by enhancing folding, trafficking, and stability through augmentation of the endoplasmic reticulum (ER) folding cycle.
24142515	3	98	theme	cotranslational	365:379	arg1	glycosylation					404:416	N-linked glycosylation	395:416	N-linked glycosylation	395:416	A common cotranslational modification, N-linked glycosylation, is critical for the proper expression of glycoproteins by enhancing folding, trafficking, and stability through augmentation of the endoplasmic reticulum (ER) folding cycle.
24142515	3	98	theme	cotranslational	365:379	arg1	critical					422:429	critical	422:429	critical	422:429	A common cotranslational modification, N-linked glycosylation, is critical for the proper expression of glycoproteins by enhancing folding, trafficking, and stability through augmentation of the endoplasmic reticulum (ER) folding cycle.
24142515	2	99	theme	glycosylation	306:318	arg1	sites					320:324	three putative N-linked glycosylation sites	282:324	three putative N-linked glycosylation sites	282:324	The first luminal loop of ABCA3 contains three putative N-linked glycosylation sites at residues 53, 124, and 140.
24142515	9	100	theme	ABCA3	1656:1660	arg1	isoforms					1662:1669	glycan-deficient ABCA3 isoforms	1639:1669	glycan-deficient ABCA3 isoforms	1639:1669	Diminished steady-state levels of glycan-deficient ABCA3 isoforms were rescued by treatment with the proteasome inhibitor MG132.
24142515	6	101	theme	motif	1107:1111	arg1	mutants					1113:1119	single motif mutants	1100:1119	single motif mutants	1100:1119	Fluorescence imaging of transiently transfected A549 or primary human AT2 cells showed that although single motif mutants exhibited a vesicular distribution pattern similar to wild-type ABCA3, mutation of N124 and N140 residues resulted in a shift toward an ER-predominant distribution.
24142515	9	102	with	treatment	1687:1695	arg1	MG132					1727:1731	the proteasome inhibitor MG132	1702:1731	the proteasome inhibitor MG132	1702:1731	Diminished steady-state levels of glycan-deficient ABCA3 isoforms were rescued by treatment with the proteasome inhibitor MG132.
24142515	1	103	theme	surfactant	217:226	arg1	homeostasis					228:238	surfactant homeostasis	217:238	surfactant homeostasis	217:238	The lipid transport protein, ABCA3, expressed in alveolar type 2 (AT2) cells, is critical for surfactant homeostasis.
24058541	5	0	theme	certain	672:678	arg1	sites					680:684	certain sites	672:684	certain sites (N179, N252, N304, or N320)	672:712	Additionally, localization studies showed that the lack of N-glycosylation on certain sites (N179, N252, N304, or N320) caused CLN5 retention in the endoplasmic reticulum, indicating that glycosylation is important for protein folding.
24058541	5	0	theme	certain	672:678	arg1	N304					699:702	N304	699:702	N304	699:702	Additionally, localization studies showed that the lack of N-glycosylation on certain sites (N179, N252, N304, or N320) caused CLN5 retention in the endoplasmic reticulum, indicating that glycosylation is important for protein folding.
24058541	5	0	theme	certain	672:678	arg1	N320					708:711	N320	708:711	N320	708:711	Additionally, localization studies showed that the lack of N-glycosylation on certain sites (N179, N252, N304, or N320) caused CLN5 retention in the endoplasmic reticulum, indicating that glycosylation is important for protein folding.
24058541	5	0	theme	certain	672:678	arg1	N252					693:696	N252	693:696	N252	693:696	Additionally, localization studies showed that the lack of N-glycosylation on certain sites (N179, N252, N304, or N320) caused CLN5 retention in the endoplasmic reticulum, indicating that glycosylation is important for protein folding.
24058541	5	0	theme	certain	672:678	arg1	N179					687:690	N179	687:690	N179	687:690	Additionally, localization studies showed that the lack of N-glycosylation on certain sites (N179, N252, N304, or N320) caused CLN5 retention in the endoplasmic reticulum, indicating that glycosylation is important for protein folding.
24058541	8	1	from	defect	1200:1205	arg1	lysosome					1214:1221	the lysosome	1210:1221	the lysosome	1210:1221	The N192S patient mutant is localized to the lysosome, indicating that this mutant has a functional defect in the lysosome.
24058541	6	2	theme	CLN5	981:984	arg1	trafficking					986:996	CLN5 trafficking	981:996	CLN5 trafficking to the lysosome	981:1012	Interestingly, one particular mutant, N401Q, is mislocalized to the Golgi, suggesting that N401 is not important for protein folding but essential for CLN5 trafficking to the lysosome.
24058541	2	3	from	Mutations	157:165	arg1	CLN5					170:173	CLN5	170:173	CLN5	170:173	Mutations in CLN5 lead to neuronal ceroid lipofuscinosis, a group of inherited neurodegenerative disorders that mainly affect children.
24058541	0	4	from	role	4:7	arg1	functionality					57:69	functionality	57:69	functionality	57:69	The role of N-glycosylation in folding, trafficking, and functionality of lysosomal protein CLN5.
24058541	0	4	from	role	4:7	arg1	folding					31:37	folding	31:37	folding	31:37	The role of N-glycosylation in folding, trafficking, and functionality of lysosomal protein CLN5.
24058541	0	4	from	role	4:7	arg1	trafficking					40:50	trafficking	40:50	trafficking	40:50	The role of N-glycosylation in folding, trafficking, and functionality of lysosomal protein CLN5.
24058541	1	5	theme	unknown	139:145	arg1	function					147:154	unknown function	139:154	unknown function	139:154	CLN5 is a soluble lysosomal protein with unknown function.
24058541	0	6	theme	protein	84:90	arg1	functionality					57:69	functionality	57:69	functionality	57:69	The role of N-glycosylation in folding, trafficking, and functionality of lysosomal protein CLN5.
24058541	0	6	theme	protein	84:90	arg1	folding					31:37	folding	31:37	folding	31:37	The role of N-glycosylation in folding, trafficking, and functionality of lysosomal protein CLN5.
24058541	0	6	theme	protein	84:90	arg1	trafficking					40:50	trafficking	40:50	trafficking	40:50	The role of N-glycosylation in folding, trafficking, and functionality of lysosomal protein CLN5.
24058541	4	7	theme	site-directed	395:407	arg1	mutagenesis					409:419	site-directed mutagenesis	395:419	site-directed mutagenesis of individual asparagine residues to glutamine on each of the N-glycosylation consensus sites	395:513	Through site-directed mutagenesis of individual asparagine residues to glutamine on each of the N-glycosylation consensus sites, we showed that all eight putative N-glycosylation sites are utilized in vivo.
24058541	3	8	theme	Asn-X-Thr/Ser	353:365	arg1	sequence					377:384	the Asn-X-Thr/Ser consensus sequence	349:384	the Asn-X-Thr/Ser consensus sequence	349:384	CLN5 has eight potential N-glycosylation sites based on the Asn-X-Thr/Ser consensus sequence.
24058541	4	9	theme	consensus	499:507	arg1	sites					509:513	the N-glycosylation consensus sites	479:513	the N-glycosylation consensus sites	479:513	Through site-directed mutagenesis of individual asparagine residues to glutamine on each of the N-glycosylation consensus sites, we showed that all eight putative N-glycosylation sites are utilized in vivo.
24058541	1	10	with	protein	126:132	arg1	function					147:154	unknown function	139:154	unknown function	139:154	CLN5 is a soluble lysosomal protein with unknown function.
24058541	4	11	theme	individual	424:433	arg1	residues					446:453	individual asparagine residues	424:453	individual asparagine residues	424:453	Through site-directed mutagenesis of individual asparagine residues to glutamine on each of the N-glycosylation consensus sites, we showed that all eight putative N-glycosylation sites are utilized in vivo.
24058541	8	12	theme	patient	1110:1116	arg1	localized					1128:1136	localized	1128:1136	localized	1128:1136	The N192S patient mutant is localized to the lysosome, indicating that this mutant has a functional defect in the lysosome.
24058541	8	12	theme	patient	1110:1116	arg1	mutant					1118:1123	The N192S patient mutant	1100:1123	The N192S patient mutant	1100:1123	The N192S patient mutant is localized to the lysosome, indicating that this mutant has a functional defect in the lysosome.
24058541	4	13	theme	N-glycosylation	483:497	arg1	sites					509:513	the N-glycosylation consensus sites	479:513	the N-glycosylation consensus sites	479:513	Through site-directed mutagenesis of individual asparagine residues to glutamine on each of the N-glycosylation consensus sites, we showed that all eight putative N-glycosylation sites are utilized in vivo.
24058541	9	14	theme	N-glycosylation	1293:1307	arg1	CLN5					1318:1321	CLN5	1318:1321	CLN5	1318:1321	Our results suggest that there are functional differences in various N-glycosylation sites of CLN5 which affect folding, trafficking, and lysosomal function of CLN5.
24058541	9	14	theme	N-glycosylation	1293:1307	arg1	sites					1309:1313	various N-glycosylation sites	1285:1313	various N-glycosylation sites of CLN5	1285:1321	Our results suggest that there are functional differences in various N-glycosylation sites of CLN5 which affect folding, trafficking, and lysosomal function of CLN5.
24058541	9	15	theme	CLN5	1384:1387	arg1	function					1372:1379	lysosomal function	1362:1379	lysosomal function	1362:1379	Our results suggest that there are functional differences in various N-glycosylation sites of CLN5 which affect folding, trafficking, and lysosomal function of CLN5.
24058541	9	15	theme	CLN5	1384:1387	arg1	trafficking					1345:1355	trafficking	1345:1355	trafficking	1345:1355	Our results suggest that there are functional differences in various N-glycosylation sites of CLN5 which affect folding, trafficking, and lysosomal function of CLN5.
24058541	9	15	theme	CLN5	1384:1387	arg1	folding					1336:1342	folding	1336:1342	folding	1336:1342	Our results suggest that there are functional differences in various N-glycosylation sites of CLN5 which affect folding, trafficking, and lysosomal function of CLN5.
24058541	2	16	theme	disorders	254:262	arg1	disorders					254:262	inherited neurodegenerative disorders	226:262	inherited neurodegenerative disorders that mainly affect children	226:290	Mutations in CLN5 lead to neuronal ceroid lipofuscinosis, a group of inherited neurodegenerative disorders that mainly affect children.
24058541	2	16	theme	disorders	254:262	arg1	lipofuscinosis					199:212	neuronal ceroid lipofuscinosis	183:212	neuronal ceroid lipofuscinosis	183:212	Mutations in CLN5 lead to neuronal ceroid lipofuscinosis, a group of inherited neurodegenerative disorders that mainly affect children.
24058541	2	16	theme	disorders	254:262	arg1	group					217:221	a group	215:221	a group of inherited neurodegenerative disorders that mainly affect children	215:290	Mutations in CLN5 lead to neuronal ceroid lipofuscinosis, a group of inherited neurodegenerative disorders that mainly affect children.
24058541	3	17	contain	has	298:300	arg2	sites					334:338	eight potential N-glycosylation sites	302:338	eight potential N-glycosylation sites	302:338	CLN5 has eight potential N-glycosylation sites based on the Asn-X-Thr/Ser consensus sequence.
24058541	3	17	contain	has	298:300	arg1	CLN5					293:296	CLN5	293:296	CLN5	293:296	CLN5 has eight potential N-glycosylation sites based on the Asn-X-Thr/Ser consensus sequence.
24058541	7	18	gly	N-glycosylation	1071:1085	arg1	mutations					1052:1060	several patient mutations	1036:1060	several patient mutations in which N-glycosylation is affected	1036:1097	Finally, we analyzed several patient mutations in which N-glycosylation is affected.
24058541	3	19	theme	potential	308:316	arg1	sites					334:338	eight potential N-glycosylation sites	302:338	eight potential N-glycosylation sites	302:338	CLN5 has eight potential N-glycosylation sites based on the Asn-X-Thr/Ser consensus sequence.
24058541	5	20	theme	N-glycosylation	653:667	arg1	lack					645:648	the lack	641:648	the lack of N-glycosylation on certain sites (N179, N252, N304, or N320)	641:712	Additionally, localization studies showed that the lack of N-glycosylation on certain sites (N179, N252, N304, or N320) caused CLN5 retention in the endoplasmic reticulum, indicating that glycosylation is important for protein folding.
24058541	9	21	theme	various	1285:1291	arg1	CLN5					1318:1321	CLN5	1318:1321	CLN5	1318:1321	Our results suggest that there are functional differences in various N-glycosylation sites of CLN5 which affect folding, trafficking, and lysosomal function of CLN5.
24058541	9	21	theme	various	1285:1291	arg1	sites					1309:1313	various N-glycosylation sites	1285:1313	various N-glycosylation sites of CLN5	1285:1321	Our results suggest that there are functional differences in various N-glycosylation sites of CLN5 which affect folding, trafficking, and lysosomal function of CLN5.
24058541	9	22	theme	CLN5	1318:1321	arg1	CLN5					1318:1321	CLN5	1318:1321	CLN5	1318:1321	Our results suggest that there are functional differences in various N-glycosylation sites of CLN5 which affect folding, trafficking, and lysosomal function of CLN5.
24058541	9	22	theme	CLN5	1318:1321	arg1	sites					1309:1313	various N-glycosylation sites	1285:1313	various N-glycosylation sites of CLN5	1285:1321	Our results suggest that there are functional differences in various N-glycosylation sites of CLN5 which affect folding, trafficking, and lysosomal function of CLN5.
24058541	4	23	theme	residues	446:453	arg1	mutagenesis					409:419	site-directed mutagenesis	395:419	site-directed mutagenesis of individual asparagine residues to glutamine on each of the N-glycosylation consensus sites	395:513	Through site-directed mutagenesis of individual asparagine residues to glutamine on each of the N-glycosylation consensus sites, we showed that all eight putative N-glycosylation sites are utilized in vivo.
24058541	4	24	gly	N-glycosylation	483:497	arg2	sites					509:513	the N-glycosylation consensus sites	479:513	the N-glycosylation consensus sites	479:513	Through site-directed mutagenesis of individual asparagine residues to glutamine on each of the N-glycosylation consensus sites, we showed that all eight putative N-glycosylation sites are utilized in vivo.
24058541	3	25	theme	consensus	367:375	arg1	sequence					377:384	the Asn-X-Thr/Ser consensus sequence	349:384	the Asn-X-Thr/Ser consensus sequence	349:384	CLN5 has eight potential N-glycosylation sites based on the Asn-X-Thr/Ser consensus sequence.
24058541	6	26	theme	protein	947:953	arg1	folding					955:961	protein folding	947:961	protein folding	947:961	Interestingly, one particular mutant, N401Q, is mislocalized to the Golgi, suggesting that N401 is not important for protein folding but essential for CLN5 trafficking to the lysosome.
24058541	7	27	theme	patient	1044:1050	arg1	mutations					1052:1060	several patient mutations	1036:1060	several patient mutations in which N-glycosylation is affected	1036:1097	Finally, we analyzed several patient mutations in which N-glycosylation is affected.
24058541	0	28	gly	N-glycosylation	12:26	arg1	protein					84:90	lysosomal protein CLN5	74:95	lysosomal protein CLN5	74:95	The role of N-glycosylation in folding, trafficking, and functionality of lysosomal protein CLN5.
24058541	5	29	dep	sites	680:684	arg1	sites					680:684	certain sites	672:684	certain sites (N179, N252, N304, or N320)	672:712	Additionally, localization studies showed that the lack of N-glycosylation on certain sites (N179, N252, N304, or N320) caused CLN5 retention in the endoplasmic reticulum, indicating that glycosylation is important for protein folding.
24058541	5	29	dep	sites	680:684	arg1	N304					699:702	N304	699:702	N304	699:702	Additionally, localization studies showed that the lack of N-glycosylation on certain sites (N179, N252, N304, or N320) caused CLN5 retention in the endoplasmic reticulum, indicating that glycosylation is important for protein folding.
24058541	5	29	dep	sites	680:684	arg1	N320					708:711	N320	708:711	N320	708:711	Additionally, localization studies showed that the lack of N-glycosylation on certain sites (N179, N252, N304, or N320) caused CLN5 retention in the endoplasmic reticulum, indicating that glycosylation is important for protein folding.
24058541	5	29	dep	sites	680:684	arg1	N252					693:696	N252	693:696	N252	693:696	Additionally, localization studies showed that the lack of N-glycosylation on certain sites (N179, N252, N304, or N320) caused CLN5 retention in the endoplasmic reticulum, indicating that glycosylation is important for protein folding.
24058541	5	29	dep	sites	680:684	arg1	N179					687:690	N179	687:690	N179	687:690	Additionally, localization studies showed that the lack of N-glycosylation on certain sites (N179, N252, N304, or N320) caused CLN5 retention in the endoplasmic reticulum, indicating that glycosylation is important for protein folding.
24058541	5	30	from	lack	645:648	arg1	sites					680:684	certain sites	672:684	certain sites (N179, N252, N304, or N320)	672:712	Additionally, localization studies showed that the lack of N-glycosylation on certain sites (N179, N252, N304, or N320) caused CLN5 retention in the endoplasmic reticulum, indicating that glycosylation is important for protein folding.
24058541	5	30	from	lack	645:648	arg1	N304					699:702	N304	699:702	N304	699:702	Additionally, localization studies showed that the lack of N-glycosylation on certain sites (N179, N252, N304, or N320) caused CLN5 retention in the endoplasmic reticulum, indicating that glycosylation is important for protein folding.
24058541	5	30	from	lack	645:648	arg1	N320					708:711	N320	708:711	N320	708:711	Additionally, localization studies showed that the lack of N-glycosylation on certain sites (N179, N252, N304, or N320) caused CLN5 retention in the endoplasmic reticulum, indicating that glycosylation is important for protein folding.
24058541	5	30	from	lack	645:648	arg1	N252					693:696	N252	693:696	N252	693:696	Additionally, localization studies showed that the lack of N-glycosylation on certain sites (N179, N252, N304, or N320) caused CLN5 retention in the endoplasmic reticulum, indicating that glycosylation is important for protein folding.
24058541	5	30	from	lack	645:648	arg1	N179					687:690	N179	687:690	N179	687:690	Additionally, localization studies showed that the lack of N-glycosylation on certain sites (N179, N252, N304, or N320) caused CLN5 retention in the endoplasmic reticulum, indicating that glycosylation is important for protein folding.
24058541	9	31	gly	N-glycosylation	1293:1307	arg2	sites					1309:1313	various N-glycosylation sites	1285:1313	various N-glycosylation sites of CLN5	1285:1321	Our results suggest that there are functional differences in various N-glycosylation sites of CLN5 which affect folding, trafficking, and lysosomal function of CLN5.
24058541	9	31	gly	N-glycosylation	1293:1307	arg1	CLN5					1318:1321	CLN5	1318:1321	CLN5	1318:1321	Our results suggest that there are functional differences in various N-glycosylation sites of CLN5 which affect folding, trafficking, and lysosomal function of CLN5.
24058541	9	31	gly	N-glycosylation	1293:1307	arg2	CLN5					1318:1321	CLN5	1318:1321	CLN5	1318:1321	Our results suggest that there are functional differences in various N-glycosylation sites of CLN5 which affect folding, trafficking, and lysosomal function of CLN5.
24058541	5	32	theme	localization	608:619	arg1	studies					621:627	localization studies	608:627	localization studies	608:627	Additionally, localization studies showed that the lack of N-glycosylation on certain sites (N179, N252, N304, or N320) caused CLN5 retention in the endoplasmic reticulum, indicating that glycosylation is important for protein folding.
24058541	9	33	from	differences	1270:1280	arg1	CLN5					1318:1321	CLN5	1318:1321	CLN5	1318:1321	Our results suggest that there are functional differences in various N-glycosylation sites of CLN5 which affect folding, trafficking, and lysosomal function of CLN5.
24058541	9	33	from	differences	1270:1280	arg1	sites					1309:1313	various N-glycosylation sites	1285:1313	various N-glycosylation sites of CLN5	1285:1321	Our results suggest that there are functional differences in various N-glycosylation sites of CLN5 which affect folding, trafficking, and lysosomal function of CLN5.
24058541	4	34	theme	putative	541:548	arg1	sites					566:570	all eight putative N-glycosylation sites	531:570	all eight putative N-glycosylation sites	531:570	Through site-directed mutagenesis of individual asparagine residues to glutamine on each of the N-glycosylation consensus sites, we showed that all eight putative N-glycosylation sites are utilized in vivo.
24058541	7	35	theme	several	1036:1042	arg1	mutations					1052:1060	several patient mutations	1036:1060	several patient mutations in which N-glycosylation is affected	1036:1097	Finally, we analyzed several patient mutations in which N-glycosylation is affected.
24058541	5	36	theme	CLN5	721:724	arg1	retention					726:734	CLN5 retention	721:734	CLN5 retention	721:734	Additionally, localization studies showed that the lack of N-glycosylation on certain sites (N179, N252, N304, or N320) caused CLN5 retention in the endoplasmic reticulum, indicating that glycosylation is important for protein folding.
24058541	0	37	theme	N-glycosylation	12:26	arg1	role					4:7	The role	0:7	The role of N-glycosylation in folding, trafficking, and functionality of lysosomal protein CLN5.	0:96	The role of N-glycosylation in folding, trafficking, and functionality of lysosomal protein CLN5.
24058541	5	38	theme	protein	813:819	arg1	folding					821:827	protein folding	813:827	protein folding	813:827	Additionally, localization studies showed that the lack of N-glycosylation on certain sites (N179, N252, N304, or N320) caused CLN5 retention in the endoplasmic reticulum, indicating that glycosylation is important for protein folding.
24058541	4	39	from	glutamine	458:466	arg1	sites					509:513	the N-glycosylation consensus sites	479:513	the N-glycosylation consensus sites	479:513	Through site-directed mutagenesis of individual asparagine residues to glutamine on each of the N-glycosylation consensus sites, we showed that all eight putative N-glycosylation sites are utilized in vivo.
24058541	4	39	from	glutamine	458:466	arg1	each					471:474	each	471:474	each	471:474	Through site-directed mutagenesis of individual asparagine residues to glutamine on each of the N-glycosylation consensus sites, we showed that all eight putative N-glycosylation sites are utilized in vivo.
24058541	6	40	theme	particular	849:858	arg1	mutant					860:865	one particular mutant	845:865	one particular mutant	845:865	Interestingly, one particular mutant, N401Q, is mislocalized to the Golgi, suggesting that N401 is not important for protein folding but essential for CLN5 trafficking to the lysosome.
24058541	6	40	theme	particular	849:858	arg1	N401Q					868:872	N401Q	868:872	N401Q	868:872	Interestingly, one particular mutant, N401Q, is mislocalized to the Golgi, suggesting that N401 is not important for protein folding but essential for CLN5 trafficking to the lysosome.
24058541	8	41	contain	has	1183:1185	arg2	defect					1200:1205	a functional defect	1187:1205	a functional defect in the lysosome	1187:1221	The N192S patient mutant is localized to the lysosome, indicating that this mutant has a functional defect in the lysosome.
24058541	8	41	contain	has	1183:1185	arg1	mutant					1176:1181	this mutant	1171:1181	this mutant	1171:1181	The N192S patient mutant is localized to the lysosome, indicating that this mutant has a functional defect in the lysosome.
24058541	8	42	theme	functional	1189:1198	arg1	defect					1200:1205	a functional defect	1187:1205	a functional defect in the lysosome	1187:1221	The N192S patient mutant is localized to the lysosome, indicating that this mutant has a functional defect in the lysosome.
24058541	3	43	gly	N-glycosylation	318:332	arg2	eight					302:306	eight	302:306	eight	302:306	CLN5 has eight potential N-glycosylation sites based on the Asn-X-Thr/Ser consensus sequence.
24058541	3	43	gly	N-glycosylation	318:332	arg2	sites					334:338	eight potential N-glycosylation sites	302:338	eight potential N-glycosylation sites	302:338	CLN5 has eight potential N-glycosylation sites based on the Asn-X-Thr/Ser consensus sequence.
24058541	2	44	theme	neuronal	183:190	arg1	disorders					254:262	inherited neurodegenerative disorders	226:262	inherited neurodegenerative disorders that mainly affect children	226:290	Mutations in CLN5 lead to neuronal ceroid lipofuscinosis, a group of inherited neurodegenerative disorders that mainly affect children.
24058541	2	44	theme	neuronal	183:190	arg1	lipofuscinosis					199:212	neuronal ceroid lipofuscinosis	183:212	neuronal ceroid lipofuscinosis	183:212	Mutations in CLN5 lead to neuronal ceroid lipofuscinosis, a group of inherited neurodegenerative disorders that mainly affect children.
24058541	2	44	theme	neuronal	183:190	arg1	group					217:221	a group	215:221	a group of inherited neurodegenerative disorders that mainly affect children	215:290	Mutations in CLN5 lead to neuronal ceroid lipofuscinosis, a group of inherited neurodegenerative disorders that mainly affect children.
24058541	2	45	theme	ceroid	192:197	arg1	disorders					254:262	inherited neurodegenerative disorders	226:262	inherited neurodegenerative disorders that mainly affect children	226:290	Mutations in CLN5 lead to neuronal ceroid lipofuscinosis, a group of inherited neurodegenerative disorders that mainly affect children.
24058541	2	45	theme	ceroid	192:197	arg1	lipofuscinosis					199:212	neuronal ceroid lipofuscinosis	183:212	neuronal ceroid lipofuscinosis	183:212	Mutations in CLN5 lead to neuronal ceroid lipofuscinosis, a group of inherited neurodegenerative disorders that mainly affect children.
24058541	2	45	theme	ceroid	192:197	arg1	group					217:221	a group	215:221	a group of inherited neurodegenerative disorders that mainly affect children	215:290	Mutations in CLN5 lead to neuronal ceroid lipofuscinosis, a group of inherited neurodegenerative disorders that mainly affect children.
24058541	4	46	theme	N-glycosylation	550:564	arg1	sites					566:570	all eight putative N-glycosylation sites	531:570	all eight putative N-glycosylation sites	531:570	Through site-directed mutagenesis of individual asparagine residues to glutamine on each of the N-glycosylation consensus sites, we showed that all eight putative N-glycosylation sites are utilized in vivo.
24058541	8	47	theme	N192S	1104:1108	arg1	localized					1128:1136	localized	1128:1136	localized	1128:1136	The N192S patient mutant is localized to the lysosome, indicating that this mutant has a functional defect in the lysosome.
24058541	8	47	theme	N192S	1104:1108	arg1	mutant					1118:1123	The N192S patient mutant	1100:1123	The N192S patient mutant	1100:1123	The N192S patient mutant is localized to the lysosome, indicating that this mutant has a functional defect in the lysosome.
24058541	4	48	theme	asparagine	435:444	arg1	residues					446:453	individual asparagine residues	424:453	individual asparagine residues	424:453	Through site-directed mutagenesis of individual asparagine residues to glutamine on each of the N-glycosylation consensus sites, we showed that all eight putative N-glycosylation sites are utilized in vivo.
24058541	2	49	theme	neurodegenerative	236:252	arg1	disorders					254:262	inherited neurodegenerative disorders	226:262	inherited neurodegenerative disorders that mainly affect children	226:290	Mutations in CLN5 lead to neuronal ceroid lipofuscinosis, a group of inherited neurodegenerative disorders that mainly affect children.
24058541	2	50	theme	inherited	226:234	arg1	disorders					254:262	inherited neurodegenerative disorders	226:262	inherited neurodegenerative disorders that mainly affect children	226:290	Mutations in CLN5 lead to neuronal ceroid lipofuscinosis, a group of inherited neurodegenerative disorders that mainly affect children.
24058541	1	51	theme	soluble	108:114	arg1	protein					126:132	a soluble lysosomal protein	106:132	a soluble lysosomal protein with unknown function	106:154	CLN5 is a soluble lysosomal protein with unknown function.
24058541	1	51	theme	soluble	108:114	arg1	CLN5					98:101	CLN5	98:101	CLN5	98:101	CLN5 is a soluble lysosomal protein with unknown function.
24058541	9	52	theme	lysosomal	1362:1370	arg1	function					1372:1379	lysosomal function	1362:1379	lysosomal function	1362:1379	Our results suggest that there are functional differences in various N-glycosylation sites of CLN5 which affect folding, trafficking, and lysosomal function of CLN5.
24058541	3	53	theme	N-glycosylation	318:332	arg1	sites					334:338	eight potential N-glycosylation sites	302:338	eight potential N-glycosylation sites	302:338	CLN5 has eight potential N-glycosylation sites based on the Asn-X-Thr/Ser consensus sequence.
24058541	1	54	theme	lysosomal	116:124	arg1	protein					126:132	a soluble lysosomal protein	106:132	a soluble lysosomal protein with unknown function	106:154	CLN5 is a soluble lysosomal protein with unknown function.
24058541	1	54	theme	lysosomal	116:124	arg1	CLN5					98:101	CLN5	98:101	CLN5	98:101	CLN5 is a soluble lysosomal protein with unknown function.
24058541	4	55	used	utilized	576:583	arg2	sites					566:570	all eight putative N-glycosylation sites	531:570	all eight putative N-glycosylation sites	531:570	Through site-directed mutagenesis of individual asparagine residues to glutamine on each of the N-glycosylation consensus sites, we showed that all eight putative N-glycosylation sites are utilized in vivo.
24058541	5	56	theme	endoplasmic	743:753	arg1	reticulum					755:763	the endoplasmic reticulum	739:763	the endoplasmic reticulum	739:763	Additionally, localization studies showed that the lack of N-glycosylation on certain sites (N179, N252, N304, or N320) caused CLN5 retention in the endoplasmic reticulum, indicating that glycosylation is important for protein folding.
24058541	9	57	theme	functional	1259:1268	arg1	differences					1270:1280	functional differences	1259:1280	functional differences in various N-glycosylation sites of CLN5 which affect folding, trafficking, and lysosomal function of CLN5	1259:1387	Our results suggest that there are functional differences in various N-glycosylation sites of CLN5 which affect folding, trafficking, and lysosomal function of CLN5.
24058541	5	58	gly	glycosylation	782:794	arg1	protein					813:819	protein folding	813:827	protein folding	813:827	Additionally, localization studies showed that the lack of N-glycosylation on certain sites (N179, N252, N304, or N320) caused CLN5 retention in the endoplasmic reticulum, indicating that glycosylation is important for protein folding.
24058541	4	59	gly	N-glycosylation	550:564	arg2	eight					535:539	eight	535:539	eight	535:539	Through site-directed mutagenesis of individual asparagine residues to glutamine on each of the N-glycosylation consensus sites, we showed that all eight putative N-glycosylation sites are utilized in vivo.
24058541	4	59	gly	N-glycosylation	550:564	arg2	sites					566:570	all eight putative N-glycosylation sites	531:570	all eight putative N-glycosylation sites	531:570	Through site-directed mutagenesis of individual asparagine residues to glutamine on each of the N-glycosylation consensus sites, we showed that all eight putative N-glycosylation sites are utilized in vivo.
24058541	0	60	theme	lysosomal	74:82	arg1	protein					84:90	lysosomal protein CLN5	74:95	lysosomal protein CLN5	74:95	The role of N-glycosylation in folding, trafficking, and functionality of lysosomal protein CLN5.
23069765	7	0	theme	characteristic	1200:1213	arg1	pattern					1215:1221	its characteristic pattern	1196:1221	its characteristic pattern of N-glycosylation	1196:1240	Therefore, the kidney host cell line not only imposed its characteristic pattern of N-glycosylation on recombinant IL-17A but additionally created an O-glycosylation not known to be present in the T cell-derived cytokine.
23069765	2	1	gly	N-glycosylation	323:337	arg2	Asn68					347:351	Asn68	347:351	Asn68	347:351	Its polypeptide monomer contains one canonical N-glycosylation site at Asn68, and human recombinant IL-17A was partly N-glycosylated when expressed in human kidney (HEK293) cells as a fusion protein with a melittin signal sequence and an N-terminal hexahistidine tag.
23069765	2	1	gly	N-glycosylation	323:337	arg2	site					339:342	one canonical N-glycosylation site	309:342	one canonical N-glycosylation site at Asn68	309:351	Its polypeptide monomer contains one canonical N-glycosylation site at Asn68, and human recombinant IL-17A was partly N-glycosylated when expressed in human kidney (HEK293) cells as a fusion protein with a melittin signal sequence and an N-terminal hexahistidine tag.
23069765	2	1	gly	N-glycosylation	323:337	arg2	one					309:311	one	309:311	one	309:311	Its polypeptide monomer contains one canonical N-glycosylation site at Asn68, and human recombinant IL-17A was partly N-glycosylated when expressed in human kidney (HEK293) cells as a fusion protein with a melittin signal sequence and an N-terminal hexahistidine tag.
23069765	2	2	theme	canonical	313:321	arg1	site					339:342	one canonical N-glycosylation site	309:342	one canonical N-glycosylation site at Asn68	309:351	Its polypeptide monomer contains one canonical N-glycosylation site at Asn68, and human recombinant IL-17A was partly N-glycosylated when expressed in human kidney (HEK293) cells as a fusion protein with a melittin signal sequence and an N-terminal hexahistidine tag.
23069765	5	3	theme	Thr26	926:930	arg1	O-glycosylation					907:921	unpredicted partial O-glycosylation	887:921	unpredicted partial O-glycosylation of Thr26 with the mucin-like structure -GalNAc(-NeuNAc)-Gal-NeuNAc	887:988	These were caused by unpredicted partial O-glycosylation of Thr26 with the mucin-like structure -GalNAc(-NeuNAc)-Gal-NeuNAc.
23069765	5	4	gly	O-glycosylation	907:921	arg1	Thr26					926:930	Thr26	926:930	Thr26	926:930	These were caused by unpredicted partial O-glycosylation of Thr26 with the mucin-like structure -GalNAc(-NeuNAc)-Gal-NeuNAc.
23069765	4	5	theme	mass	717:720	arg1	spectrum					722:729	The mass spectrum	713:729	The mass spectrum of IL-17A monomer	713:747	The mass spectrum of IL-17A monomer also included peaks shifted by +948 Da from the respective masses of unglycosylated and N-glycosylated polypeptides.
23069765	7	6	theme	cell	1169:1172	arg1	line					1174:1177	the kidney host cell line	1153:1177	the kidney host cell line	1153:1177	Therefore, the kidney host cell line not only imposed its characteristic pattern of N-glycosylation on recombinant IL-17A but additionally created an O-glycosylation not known to be present in the T cell-derived cytokine.
23069765	8	7	gly	O-glycosylate	1567:1579	arg1	protein					1583:1589	a protein	1581:1589	a protein that is probably not normally O-glycosylated	1581:1634	Mammalian host cell lines for recombinant protein expression generally impose their characteristic patterns of N-glycosylation on the product, but this work exemplifies how a host may also unpredictably O-glycosylate a protein that is probably not normally O-glycosylated.
23069765	8	7	gly	O-glycosylate	1567:1579	arg1	O-glycosylated					1621:1634	O-glycosylated	1621:1634	O-glycosylated	1621:1634	Mammalian host cell lines for recombinant protein expression generally impose their characteristic patterns of N-glycosylation on the product, but this work exemplifies how a host may also unpredictably O-glycosylate a protein that is probably not normally O-glycosylated.
23069765	6	8	theme	recombinant	1050:1060	arg1	IL-17A					1062:1067	commercially sourced recombinant IL-17A	1029:1067	commercially sourced recombinant IL-17A also expressed in HEK293 cells but with a different N-terminal sequence	1029:1139	Identical O-glycosylation occurred in commercially sourced recombinant IL-17A also expressed in HEK293 cells but with a different N-terminal sequence.
23069765	7	9	theme	kidney	1157:1162	arg1	line					1174:1177	the kidney host cell line	1153:1177	the kidney host cell line	1153:1177	Therefore, the kidney host cell line not only imposed its characteristic pattern of N-glycosylation on recombinant IL-17A but additionally created an O-glycosylation not known to be present in the T cell-derived cytokine.
23069765	3	10	theme	N-glycopeptide	582:595	arg1	63-69					597:601	the tryptic N-glycopeptide 63-69	570:601	the tryptic N-glycopeptide 63-69	570:601	Orbitrap mass analyses of the tryptic N-glycopeptide 63-69 indicated that the N-glycosylation was of the GalNAc-terminated type characteristic of cultured kidney cells.
23069765	5	11	theme	unpredicted	887:897	arg1	O-glycosylation					907:921	unpredicted partial O-glycosylation	887:921	unpredicted partial O-glycosylation of Thr26 with the mucin-like structure -GalNAc(-NeuNAc)-Gal-NeuNAc	887:988	These were caused by unpredicted partial O-glycosylation of Thr26 with the mucin-like structure -GalNAc(-NeuNAc)-Gal-NeuNAc.
23069765	8	12	theme	host	1374:1377	arg1	lines					1384:1388	Mammalian host cell lines	1364:1388	Mammalian host cell lines for recombinant protein expression	1364:1423	Mammalian host cell lines for recombinant protein expression generally impose their characteristic patterns of N-glycosylation on the product, but this work exemplifies how a host may also unpredictably O-glycosylate a protein that is probably not normally O-glycosylated.
23069765	1	13	theme	disulfide-linked	235:250	arg1	homodimer					252:260	a variably glycosylated disulfide-linked homodimer	211:260	a variably glycosylated disulfide-linked homodimer of 34-38 kDa	211:273	The T helper cell-derived cytokine interleukin-17A (IL-17A) is a variably glycosylated disulfide-linked homodimer of 34-38 kDa.
23069765	1	13	theme	disulfide-linked	235:250	arg1	interleukin-17A					183:197	The T helper cell-derived cytokine interleukin-17A	148:197	The T helper cell-derived cytokine interleukin-17A (IL-17A)	148:206	The T helper cell-derived cytokine interleukin-17A (IL-17A) is a variably glycosylated disulfide-linked homodimer of 34-38 kDa.
23069765	2	14	with	protein	467:473	arg1	sequence					498:505	a melittin signal sequence	480:505	a melittin signal sequence	480:505	Its polypeptide monomer contains one canonical N-glycosylation site at Asn68, and human recombinant IL-17A was partly N-glycosylated when expressed in human kidney (HEK293) cells as a fusion protein with a melittin signal sequence and an N-terminal hexahistidine tag.
23069765	6	15	theme	Identical	991:999	arg1	O-glycosylation					1001:1015	Identical O-glycosylation	991:1015	Identical O-glycosylation	991:1015	Identical O-glycosylation occurred in commercially sourced recombinant IL-17A also expressed in HEK293 cells but with a different N-terminal sequence.
23069765	3	16	gly	N-glycopeptide	582:595	arg2	N-glycopeptide					582:595	the tryptic N-glycopeptide 63-69	570:601	the tryptic N-glycopeptide 63-69	570:601	Orbitrap mass analyses of the tryptic N-glycopeptide 63-69 indicated that the N-glycosylation was of the GalNAc-terminated type characteristic of cultured kidney cells.
23069765	2	17	theme	polypeptide	280:290	arg1	monomer					292:298	Its polypeptide monomer	276:298	Its polypeptide monomer	276:298	Its polypeptide monomer contains one canonical N-glycosylation site at Asn68, and human recombinant IL-17A was partly N-glycosylated when expressed in human kidney (HEK293) cells as a fusion protein with a melittin signal sequence and an N-terminal hexahistidine tag.
23069765	1	18	theme	T	152:152	arg1	homodimer					252:260	a variably glycosylated disulfide-linked homodimer	211:260	a variably glycosylated disulfide-linked homodimer of 34-38 kDa	211:273	The T helper cell-derived cytokine interleukin-17A (IL-17A) is a variably glycosylated disulfide-linked homodimer of 34-38 kDa.
23069765	1	18	theme	T	152:152	arg1	IL-17A					200:205	IL-17A	200:205	IL-17A	200:205	The T helper cell-derived cytokine interleukin-17A (IL-17A) is a variably glycosylated disulfide-linked homodimer of 34-38 kDa.
23069765	1	18	theme	T	152:152	arg1	interleukin-17A					183:197	The T helper cell-derived cytokine interleukin-17A	148:197	The T helper cell-derived cytokine interleukin-17A (IL-17A)	148:206	The T helper cell-derived cytokine interleukin-17A (IL-17A) is a variably glycosylated disulfide-linked homodimer of 34-38 kDa.
23069765	8	19	theme	recombinant	1394:1404	arg1	expression					1414:1423	recombinant protein expression	1394:1423	recombinant protein expression	1394:1423	Mammalian host cell lines for recombinant protein expression generally impose their characteristic patterns of N-glycosylation on the product, but this work exemplifies how a host may also unpredictably O-glycosylate a protein that is probably not normally O-glycosylated.
23069765	2	20	theme	N-terminal	514:523	arg1	tag					539:541	an N-terminal hexahistidine tag	511:541	an N-terminal hexahistidine tag	511:541	Its polypeptide monomer contains one canonical N-glycosylation site at Asn68, and human recombinant IL-17A was partly N-glycosylated when expressed in human kidney (HEK293) cells as a fusion protein with a melittin signal sequence and an N-terminal hexahistidine tag.
23069765	7	21	from	present	1324:1330	arg1	cytokine					1354:1361	the T cell-derived cytokine	1335:1361	the T cell-derived cytokine	1335:1361	Therefore, the kidney host cell line not only imposed its characteristic pattern of N-glycosylation on recombinant IL-17A but additionally created an O-glycosylation not known to be present in the T cell-derived cytokine.
23069765	0	22	theme	recombinant	81:91	arg1	interleukin-17A					93:107	human recombinant interleukin-17A	75:107	human recombinant interleukin-17A	75:107	Unexpected mucin-type O-glycosylation and host-specific N-glycosylation of human recombinant interleukin-17A expressed in a human kidney cell line.
23069765	5	23	theme	structure	952:960	arg1	-Gal-NeuNAc					978:988	the mucin-like structure -GalNAc(-NeuNAc)-Gal-NeuNAc	937:988	the mucin-like structure -GalNAc(-NeuNAc)-Gal-NeuNAc	937:988	These were caused by unpredicted partial O-glycosylation of Thr26 with the mucin-like structure -GalNAc(-NeuNAc)-Gal-NeuNAc.
23069765	4	24	theme	monomer	741:747	arg1	spectrum					722:729	The mass spectrum	713:729	The mass spectrum of IL-17A monomer	713:747	The mass spectrum of IL-17A monomer also included peaks shifted by +948 Da from the respective masses of unglycosylated and N-glycosylated polypeptides.
23069765	3	25	theme	type	667:670	arg1	characteristic					672:685	the GalNAc-terminated type characteristic	645:685	the GalNAc-terminated type characteristic of cultured kidney cells	645:710	Orbitrap mass analyses of the tryptic N-glycopeptide 63-69 indicated that the N-glycosylation was of the GalNAc-terminated type characteristic of cultured kidney cells.
23069765	4	26	theme	respective	797:806	arg1	masses					808:813	the respective masses	793:813	the respective masses of unglycosylated and N-glycosylated polypeptides	793:863	The mass spectrum of IL-17A monomer also included peaks shifted by +948 Da from the respective masses of unglycosylated and N-glycosylated polypeptides.
23069765	8	27	gly	O-glycosylated	1621:1634	arg1	protein					1583:1589	a protein	1581:1589	a protein that is probably not normally O-glycosylated	1581:1634	Mammalian host cell lines for recombinant protein expression generally impose their characteristic patterns of N-glycosylation on the product, but this work exemplifies how a host may also unpredictably O-glycosylate a protein that is probably not normally O-glycosylated.
23069765	8	27	gly	O-glycosylated	1621:1634	arg1	O-glycosylated					1621:1634	O-glycosylated	1621:1634	O-glycosylated	1621:1634	Mammalian host cell lines for recombinant protein expression generally impose their characteristic patterns of N-glycosylation on the product, but this work exemplifies how a host may also unpredictably O-glycosylate a protein that is probably not normally O-glycosylated.
23069765	2	28	theme	kidney	433:438	arg1	cells					449:453	human kidney (HEK293) cells	427:453	human kidney (HEK293) cells as a fusion protein with a melittin signal sequence and an N-terminal hexahistidine tag	427:541	Its polypeptide monomer contains one canonical N-glycosylation site at Asn68, and human recombinant IL-17A was partly N-glycosylated when expressed in human kidney (HEK293) cells as a fusion protein with a melittin signal sequence and an N-terminal hexahistidine tag.
23069765	0	29	theme	kidney	130:135	arg1	line					142:145	a human kidney cell line	122:145	a human kidney cell line	122:145	Unexpected mucin-type O-glycosylation and host-specific N-glycosylation of human recombinant interleukin-17A expressed in a human kidney cell line.
23069765	4	30	gly	unglycosylated	818:831	arg1	polypeptides					852:863	unglycosylated and N-glycosylated polypeptides	818:863	unglycosylated and N-glycosylated polypeptides	818:863	The mass spectrum of IL-17A monomer also included peaks shifted by +948 Da from the respective masses of unglycosylated and N-glycosylated polypeptides.
23069765	2	31	with	tag	539:541	arg1	sequence					498:505	a melittin signal sequence	480:505	a melittin signal sequence	480:505	Its polypeptide monomer contains one canonical N-glycosylation site at Asn68, and human recombinant IL-17A was partly N-glycosylated when expressed in human kidney (HEK293) cells as a fusion protein with a melittin signal sequence and an N-terminal hexahistidine tag.
23069765	0	32	theme	Unexpected	0:9	arg1	O-glycosylation					22:36	Unexpected mucin-type O-glycosylation	0:36	Unexpected mucin-type O-glycosylation	0:36	Unexpected mucin-type O-glycosylation and host-specific N-glycosylation of human recombinant interleukin-17A expressed in a human kidney cell line.
23069765	2	33	contain	contains	300:307	arg2	site					339:342	one canonical N-glycosylation site	309:342	one canonical N-glycosylation site at Asn68	309:351	Its polypeptide monomer contains one canonical N-glycosylation site at Asn68, and human recombinant IL-17A was partly N-glycosylated when expressed in human kidney (HEK293) cells as a fusion protein with a melittin signal sequence and an N-terminal hexahistidine tag.
23069765	2	33	contain	contains	300:307	arg1	monomer					292:298	Its polypeptide monomer	276:298	Its polypeptide monomer	276:298	Its polypeptide monomer contains one canonical N-glycosylation site at Asn68, and human recombinant IL-17A was partly N-glycosylated when expressed in human kidney (HEK293) cells as a fusion protein with a melittin signal sequence and an N-terminal hexahistidine tag.
23069765	2	34	gly	N-glycosylated	394:407	arg1	IL-17A					376:381	human recombinant IL-17A	358:381	human recombinant IL-17A	358:381	Its polypeptide monomer contains one canonical N-glycosylation site at Asn68, and human recombinant IL-17A was partly N-glycosylated when expressed in human kidney (HEK293) cells as a fusion protein with a melittin signal sequence and an N-terminal hexahistidine tag.
23069765	1	35	theme	helper	154:159	arg1	homodimer					252:260	a variably glycosylated disulfide-linked homodimer	211:260	a variably glycosylated disulfide-linked homodimer of 34-38 kDa	211:273	The T helper cell-derived cytokine interleukin-17A (IL-17A) is a variably glycosylated disulfide-linked homodimer of 34-38 kDa.
23069765	1	35	theme	helper	154:159	arg1	IL-17A					200:205	IL-17A	200:205	IL-17A	200:205	The T helper cell-derived cytokine interleukin-17A (IL-17A) is a variably glycosylated disulfide-linked homodimer of 34-38 kDa.
23069765	1	35	theme	helper	154:159	arg1	interleukin-17A					183:197	The T helper cell-derived cytokine interleukin-17A	148:197	The T helper cell-derived cytokine interleukin-17A (IL-17A)	148:206	The T helper cell-derived cytokine interleukin-17A (IL-17A) is a variably glycosylated disulfide-linked homodimer of 34-38 kDa.
23069765	2	36	theme	signal	491:496	arg1	sequence					498:505	a melittin signal sequence	480:505	a melittin signal sequence	480:505	Its polypeptide monomer contains one canonical N-glycosylation site at Asn68, and human recombinant IL-17A was partly N-glycosylated when expressed in human kidney (HEK293) cells as a fusion protein with a melittin signal sequence and an N-terminal hexahistidine tag.
23069765	3	37	theme	kidney	699:704	arg1	cells					706:710	cultured kidney cells	690:710	cultured kidney cells	690:710	Orbitrap mass analyses of the tryptic N-glycopeptide 63-69 indicated that the N-glycosylation was of the GalNAc-terminated type characteristic of cultured kidney cells.
23069765	0	38	theme	host-specific	42:54	arg1	N-glycosylation					56:70	host-specific N-glycosylation	42:70	host-specific N-glycosylation	42:70	Unexpected mucin-type O-glycosylation and host-specific N-glycosylation of human recombinant interleukin-17A expressed in a human kidney cell line.
23069765	6	39	theme	different	1111:1119	arg1	sequence					1132:1139	a different N-terminal sequence	1109:1139	a different N-terminal sequence	1109:1139	Identical O-glycosylation occurred in commercially sourced recombinant IL-17A also expressed in HEK293 cells but with a different N-terminal sequence.
23069765	2	40	theme	human	358:362	arg1	IL-17A					376:381	human recombinant IL-17A	358:381	human recombinant IL-17A	358:381	Its polypeptide monomer contains one canonical N-glycosylation site at Asn68, and human recombinant IL-17A was partly N-glycosylated when expressed in human kidney (HEK293) cells as a fusion protein with a melittin signal sequence and an N-terminal hexahistidine tag.
23069765	0	41	gly	N-glycosylation	56:70	arg1	interleukin-17A					93:107	human recombinant interleukin-17A	75:107	human recombinant interleukin-17A	75:107	Unexpected mucin-type O-glycosylation and host-specific N-glycosylation of human recombinant interleukin-17A expressed in a human kidney cell line.
23069765	1	42	theme	cell-derived	161:172	arg1	homodimer					252:260	a variably glycosylated disulfide-linked homodimer	211:260	a variably glycosylated disulfide-linked homodimer of 34-38 kDa	211:273	The T helper cell-derived cytokine interleukin-17A (IL-17A) is a variably glycosylated disulfide-linked homodimer of 34-38 kDa.
23069765	1	42	theme	cell-derived	161:172	arg1	IL-17A					200:205	IL-17A	200:205	IL-17A	200:205	The T helper cell-derived cytokine interleukin-17A (IL-17A) is a variably glycosylated disulfide-linked homodimer of 34-38 kDa.
23069765	1	42	theme	cell-derived	161:172	arg1	interleukin-17A					183:197	The T helper cell-derived cytokine interleukin-17A	148:197	The T helper cell-derived cytokine interleukin-17A (IL-17A)	148:206	The T helper cell-derived cytokine interleukin-17A (IL-17A) is a variably glycosylated disulfide-linked homodimer of 34-38 kDa.
23069765	4	43	theme	polypeptides	852:863	arg1	masses					808:813	the respective masses	793:813	the respective masses of unglycosylated and N-glycosylated polypeptides	793:863	The mass spectrum of IL-17A monomer also included peaks shifted by +948 Da from the respective masses of unglycosylated and N-glycosylated polypeptides.
23069765	0	44	theme	human	75:79	arg1	interleukin-17A					93:107	human recombinant interleukin-17A	75:107	human recombinant interleukin-17A	75:107	Unexpected mucin-type O-glycosylation and host-specific N-glycosylation of human recombinant interleukin-17A expressed in a human kidney cell line.
23069765	7	45	theme	cell-derived	1341:1352	arg1	cytokine					1354:1361	the T cell-derived cytokine	1335:1361	the T cell-derived cytokine	1335:1361	Therefore, the kidney host cell line not only imposed its characteristic pattern of N-glycosylation on recombinant IL-17A but additionally created an O-glycosylation not known to be present in the T cell-derived cytokine.
23069765	2	46	theme	N-glycosylation	323:337	arg1	site					339:342	one canonical N-glycosylation site	309:342	one canonical N-glycosylation site at Asn68	309:351	Its polypeptide monomer contains one canonical N-glycosylation site at Asn68, and human recombinant IL-17A was partly N-glycosylated when expressed in human kidney (HEK293) cells as a fusion protein with a melittin signal sequence and an N-terminal hexahistidine tag.
23069765	5	47	theme	-GalNAc	962:968	arg1	-Gal-NeuNAc					978:988	the mucin-like structure -GalNAc(-NeuNAc)-Gal-NeuNAc	937:988	the mucin-like structure -GalNAc(-NeuNAc)-Gal-NeuNAc	937:988	These were caused by unpredicted partial O-glycosylation of Thr26 with the mucin-like structure -GalNAc(-NeuNAc)-Gal-NeuNAc.
23069765	6	48	gly	O-glycosylation	1001:1015	arg2	IL-17A					1062:1067	commercially sourced recombinant IL-17A	1029:1067	commercially sourced recombinant IL-17A also expressed in HEK293 cells but with a different N-terminal sequence	1029:1139	Identical O-glycosylation occurred in commercially sourced recombinant IL-17A also expressed in HEK293 cells but with a different N-terminal sequence.
23069765	3	49	theme	mass	553:556	arg1	analyses					558:565	Orbitrap mass analyses	544:565	Orbitrap mass analyses of the tryptic N-glycopeptide 63-69	544:601	Orbitrap mass analyses of the tryptic N-glycopeptide 63-69 indicated that the N-glycosylation was of the GalNAc-terminated type characteristic of cultured kidney cells.
23069765	7	50	from	cytokine	1354:1361	arg1	present					1324:1330	present	1324:1330	present	1324:1330	Therefore, the kidney host cell line not only imposed its characteristic pattern of N-glycosylation on recombinant IL-17A but additionally created an O-glycosylation not known to be present in the T cell-derived cytokine.
23069765	7	51	theme	host	1164:1167	arg1	line					1174:1177	the kidney host cell line	1153:1177	the kidney host cell line	1153:1177	Therefore, the kidney host cell line not only imposed its characteristic pattern of N-glycosylation on recombinant IL-17A but additionally created an O-glycosylation not known to be present in the T cell-derived cytokine.
23069765	3	52	theme	63-69	597:601	arg1	analyses					558:565	Orbitrap mass analyses	544:565	Orbitrap mass analyses of the tryptic N-glycopeptide 63-69	544:601	Orbitrap mass analyses of the tryptic N-glycopeptide 63-69 indicated that the N-glycosylation was of the GalNAc-terminated type characteristic of cultured kidney cells.
23069765	1	53	gly	glycosylated	222:233	arg1	homodimer					252:260	a variably glycosylated disulfide-linked homodimer	211:260	a variably glycosylated disulfide-linked homodimer of 34-38 kDa	211:273	The T helper cell-derived cytokine interleukin-17A (IL-17A) is a variably glycosylated disulfide-linked homodimer of 34-38 kDa.
23069765	1	53	gly	glycosylated	222:233	arg1	interleukin-17A					183:197	The T helper cell-derived cytokine interleukin-17A	148:197	The T helper cell-derived cytokine interleukin-17A (IL-17A)	148:206	The T helper cell-derived cytokine interleukin-17A (IL-17A) is a variably glycosylated disulfide-linked homodimer of 34-38 kDa.
23069765	3	54	theme	tryptic	574:580	arg1	63-69					597:601	the tryptic N-glycopeptide 63-69	570:601	the tryptic N-glycopeptide 63-69	570:601	Orbitrap mass analyses of the tryptic N-glycopeptide 63-69 indicated that the N-glycosylation was of the GalNAc-terminated type characteristic of cultured kidney cells.
23069765	6	55	theme	sourced	1042:1048	arg1	IL-17A					1062:1067	commercially sourced recombinant IL-17A	1029:1067	commercially sourced recombinant IL-17A also expressed in HEK293 cells but with a different N-terminal sequence	1029:1139	Identical O-glycosylation occurred in commercially sourced recombinant IL-17A also expressed in HEK293 cells but with a different N-terminal sequence.
23069765	5	56	theme	partial	899:905	arg1	O-glycosylation					907:921	unpredicted partial O-glycosylation	887:921	unpredicted partial O-glycosylation of Thr26 with the mucin-like structure -GalNAc(-NeuNAc)-Gal-NeuNAc	887:988	These were caused by unpredicted partial O-glycosylation of Thr26 with the mucin-like structure -GalNAc(-NeuNAc)-Gal-NeuNAc.
23069765	7	57	link	cell-derived	1341:1352	arg1	cytokine					1354:1361	the T cell-derived cytokine	1335:1361	the T cell-derived cytokine	1335:1361	Therefore, the kidney host cell line not only imposed its characteristic pattern of N-glycosylation on recombinant IL-17A but additionally created an O-glycosylation not known to be present in the T cell-derived cytokine.
23069765	8	58	theme	Mammalian	1364:1372	arg1	lines					1384:1388	Mammalian host cell lines	1364:1388	Mammalian host cell lines for recombinant protein expression	1364:1423	Mammalian host cell lines for recombinant protein expression generally impose their characteristic patterns of N-glycosylation on the product, but this work exemplifies how a host may also unpredictably O-glycosylate a protein that is probably not normally O-glycosylated.
23069765	5	59	theme	-NeuNAc	970:976	arg1	-Gal-NeuNAc					978:988	the mucin-like structure -GalNAc(-NeuNAc)-Gal-NeuNAc	937:988	the mucin-like structure -GalNAc(-NeuNAc)-Gal-NeuNAc	937:988	These were caused by unpredicted partial O-glycosylation of Thr26 with the mucin-like structure -GalNAc(-NeuNAc)-Gal-NeuNAc.
23069765	8	60	theme	cell	1379:1382	arg1	lines					1384:1388	Mammalian host cell lines	1364:1388	Mammalian host cell lines for recombinant protein expression	1364:1423	Mammalian host cell lines for recombinant protein expression generally impose their characteristic patterns of N-glycosylation on the product, but this work exemplifies how a host may also unpredictably O-glycosylate a protein that is probably not normally O-glycosylated.
23069765	3	61	theme	GalNAc-terminated	649:665	arg1	characteristic					672:685	the GalNAc-terminated type characteristic	645:685	the GalNAc-terminated type characteristic of cultured kidney cells	645:710	Orbitrap mass analyses of the tryptic N-glycopeptide 63-69 indicated that the N-glycosylation was of the GalNAc-terminated type characteristic of cultured kidney cells.
23069765	8	62	theme	characteristic	1448:1461	arg1	patterns					1463:1470	their characteristic patterns	1442:1470	their characteristic patterns of N-glycosylation	1442:1489	Mammalian host cell lines for recombinant protein expression generally impose their characteristic patterns of N-glycosylation on the product, but this work exemplifies how a host may also unpredictably O-glycosylate a protein that is probably not normally O-glycosylated.
23069765	0	63	theme	interleukin-17A	93:107	arg1	O-glycosylation					22:36	Unexpected mucin-type O-glycosylation	0:36	Unexpected mucin-type O-glycosylation	0:36	Unexpected mucin-type O-glycosylation and host-specific N-glycosylation of human recombinant interleukin-17A expressed in a human kidney cell line.
23069765	0	63	theme	interleukin-17A	93:107	arg1	N-glycosylation					56:70	host-specific N-glycosylation	42:70	host-specific N-glycosylation	42:70	Unexpected mucin-type O-glycosylation and host-specific N-glycosylation of human recombinant interleukin-17A expressed in a human kidney cell line.
23069765	5	64	theme	mucin-like	941:950	arg1	-Gal-NeuNAc					978:988	the mucin-like structure -GalNAc(-NeuNAc)-Gal-NeuNAc	937:988	the mucin-like structure -GalNAc(-NeuNAc)-Gal-NeuNAc	937:988	These were caused by unpredicted partial O-glycosylation of Thr26 with the mucin-like structure -GalNAc(-NeuNAc)-Gal-NeuNAc.
23069765	8	65	theme	protein	1406:1412	arg1	expression					1414:1423	recombinant protein expression	1394:1423	recombinant protein expression	1394:1423	Mammalian host cell lines for recombinant protein expression generally impose their characteristic patterns of N-glycosylation on the product, but this work exemplifies how a host may also unpredictably O-glycosylate a protein that is probably not normally O-glycosylated.
23069765	1	66	theme	cytokine	174:181	arg1	homodimer					252:260	a variably glycosylated disulfide-linked homodimer	211:260	a variably glycosylated disulfide-linked homodimer of 34-38 kDa	211:273	The T helper cell-derived cytokine interleukin-17A (IL-17A) is a variably glycosylated disulfide-linked homodimer of 34-38 kDa.
23069765	1	66	theme	cytokine	174:181	arg1	IL-17A					200:205	IL-17A	200:205	IL-17A	200:205	The T helper cell-derived cytokine interleukin-17A (IL-17A) is a variably glycosylated disulfide-linked homodimer of 34-38 kDa.
23069765	1	66	theme	cytokine	174:181	arg1	interleukin-17A					183:197	The T helper cell-derived cytokine interleukin-17A	148:197	The T helper cell-derived cytokine interleukin-17A (IL-17A)	148:206	The T helper cell-derived cytokine interleukin-17A (IL-17A) is a variably glycosylated disulfide-linked homodimer of 34-38 kDa.
23069765	6	67	theme	HEK293	1087:1092	arg1	cells					1094:1098	HEK293 cells	1087:1098	HEK293 cells	1087:1098	Identical O-glycosylation occurred in commercially sourced recombinant IL-17A also expressed in HEK293 cells but with a different N-terminal sequence.
23069765	1	68	link	disulfide-linked	235:250	arg1	homodimer					252:260	a variably glycosylated disulfide-linked homodimer	211:260	a variably glycosylated disulfide-linked homodimer of 34-38 kDa	211:273	The T helper cell-derived cytokine interleukin-17A (IL-17A) is a variably glycosylated disulfide-linked homodimer of 34-38 kDa.
23069765	1	68	link	disulfide-linked	235:250	arg1	interleukin-17A					183:197	The T helper cell-derived cytokine interleukin-17A	148:197	The T helper cell-derived cytokine interleukin-17A (IL-17A)	148:206	The T helper cell-derived cytokine interleukin-17A (IL-17A) is a variably glycosylated disulfide-linked homodimer of 34-38 kDa.
23069765	4	69	theme	IL-17A	734:739	arg1	monomer					741:747	IL-17A monomer	734:747	IL-17A monomer	734:747	The mass spectrum of IL-17A monomer also included peaks shifted by +948 Da from the respective masses of unglycosylated and N-glycosylated polypeptides.
23069765	0	70	theme	human	124:128	arg1	line					142:145	a human kidney cell line	122:145	a human kidney cell line	122:145	Unexpected mucin-type O-glycosylation and host-specific N-glycosylation of human recombinant interleukin-17A expressed in a human kidney cell line.
23069765	2	71	from	Asn68	347:351	arg1	site					339:342	one canonical N-glycosylation site	309:342	one canonical N-glycosylation site at Asn68	309:351	Its polypeptide monomer contains one canonical N-glycosylation site at Asn68, and human recombinant IL-17A was partly N-glycosylated when expressed in human kidney (HEK293) cells as a fusion protein with a melittin signal sequence and an N-terminal hexahistidine tag.
23069765	0	72	theme	cell	137:140	arg1	line					142:145	a human kidney cell line	122:145	a human kidney cell line	122:145	Unexpected mucin-type O-glycosylation and host-specific N-glycosylation of human recombinant interleukin-17A expressed in a human kidney cell line.
23069765	2	73	theme	hexahistidine	525:537	arg1	tag					539:541	an N-terminal hexahistidine tag	511:541	an N-terminal hexahistidine tag	511:541	Its polypeptide monomer contains one canonical N-glycosylation site at Asn68, and human recombinant IL-17A was partly N-glycosylated when expressed in human kidney (HEK293) cells as a fusion protein with a melittin signal sequence and an N-terminal hexahistidine tag.
23069765	2	74	theme	human	427:431	arg1	HEK293					441:446	HEK293	441:446	HEK293	441:446	Its polypeptide monomer contains one canonical N-glycosylation site at Asn68, and human recombinant IL-17A was partly N-glycosylated when expressed in human kidney (HEK293) cells as a fusion protein with a melittin signal sequence and an N-terminal hexahistidine tag.
23069765	2	74	theme	human	427:431	arg1	kidney					433:438	human kidney	427:438	human kidney (HEK293) cells as a fusion protein with a melittin signal sequence and an N-terminal hexahistidine tag	427:541	Its polypeptide monomer contains one canonical N-glycosylation site at Asn68, and human recombinant IL-17A was partly N-glycosylated when expressed in human kidney (HEK293) cells as a fusion protein with a melittin signal sequence and an N-terminal hexahistidine tag.
23069765	0	75	theme	mucin-type	11:20	arg1	O-glycosylation					22:36	Unexpected mucin-type O-glycosylation	0:36	Unexpected mucin-type O-glycosylation	0:36	Unexpected mucin-type O-glycosylation and host-specific N-glycosylation of human recombinant interleukin-17A expressed in a human kidney cell line.
23069765	2	76	theme	fusion	460:465	arg1	protein					467:473	a fusion protein	458:473	a fusion protein with a melittin signal sequence	458:505	Its polypeptide monomer contains one canonical N-glycosylation site at Asn68, and human recombinant IL-17A was partly N-glycosylated when expressed in human kidney (HEK293) cells as a fusion protein with a melittin signal sequence and an N-terminal hexahistidine tag.
23069765	8	77	theme	N-glycosylation	1475:1489	arg1	patterns					1463:1470	their characteristic patterns	1442:1470	their characteristic patterns of N-glycosylation	1442:1489	Mammalian host cell lines for recombinant protein expression generally impose their characteristic patterns of N-glycosylation on the product, but this work exemplifies how a host may also unpredictably O-glycosylate a protein that is probably not normally O-glycosylated.
23069765	7	78	theme	recombinant	1245:1255	arg1	IL-17A					1257:1262	recombinant IL-17A	1245:1262	recombinant IL-17A	1245:1262	Therefore, the kidney host cell line not only imposed its characteristic pattern of N-glycosylation on recombinant IL-17A but additionally created an O-glycosylation not known to be present in the T cell-derived cytokine.
23069765	5	79	with	O-glycosylation	907:921	arg1	-Gal-NeuNAc					978:988	the mucin-like structure -GalNAc(-NeuNAc)-Gal-NeuNAc	937:988	the mucin-like structure -GalNAc(-NeuNAc)-Gal-NeuNAc	937:988	These were caused by unpredicted partial O-glycosylation of Thr26 with the mucin-like structure -GalNAc(-NeuNAc)-Gal-NeuNAc.
23069765	3	80	theme	cultured	690:697	arg1	cells					706:710	cultured kidney cells	690:710	cultured kidney cells	690:710	Orbitrap mass analyses of the tryptic N-glycopeptide 63-69 indicated that the N-glycosylation was of the GalNAc-terminated type characteristic of cultured kidney cells.
23069765	7	81	theme	N-glycosylation	1226:1240	arg1	pattern					1215:1221	its characteristic pattern	1196:1221	its characteristic pattern of N-glycosylation	1196:1240	Therefore, the kidney host cell line not only imposed its characteristic pattern of N-glycosylation on recombinant IL-17A but additionally created an O-glycosylation not known to be present in the T cell-derived cytokine.
23069765	1	82	theme	glycosylated	222:233	arg1	homodimer					252:260	a variably glycosylated disulfide-linked homodimer	211:260	a variably glycosylated disulfide-linked homodimer of 34-38 kDa	211:273	The T helper cell-derived cytokine interleukin-17A (IL-17A) is a variably glycosylated disulfide-linked homodimer of 34-38 kDa.
23069765	1	82	theme	glycosylated	222:233	arg1	interleukin-17A					183:197	The T helper cell-derived cytokine interleukin-17A	148:197	The T helper cell-derived cytokine interleukin-17A (IL-17A)	148:206	The T helper cell-derived cytokine interleukin-17A (IL-17A) is a variably glycosylated disulfide-linked homodimer of 34-38 kDa.
23069765	6	83	theme	N-terminal	1121:1130	arg1	sequence					1132:1139	a different N-terminal sequence	1109:1139	a different N-terminal sequence	1109:1139	Identical O-glycosylation occurred in commercially sourced recombinant IL-17A also expressed in HEK293 cells but with a different N-terminal sequence.
23069765	2	84	theme	melittin	482:489	arg1	sequence					498:505	a melittin signal sequence	480:505	a melittin signal sequence	480:505	Its polypeptide monomer contains one canonical N-glycosylation site at Asn68, and human recombinant IL-17A was partly N-glycosylated when expressed in human kidney (HEK293) cells as a fusion protein with a melittin signal sequence and an N-terminal hexahistidine tag.
23069765	1	85	link	cell-derived	161:172	arg1	homodimer					252:260	a variably glycosylated disulfide-linked homodimer	211:260	a variably glycosylated disulfide-linked homodimer of 34-38 kDa	211:273	The T helper cell-derived cytokine interleukin-17A (IL-17A) is a variably glycosylated disulfide-linked homodimer of 34-38 kDa.
23069765	1	85	link	cell-derived	161:172	arg1	IL-17A					200:205	IL-17A	200:205	IL-17A	200:205	The T helper cell-derived cytokine interleukin-17A (IL-17A) is a variably glycosylated disulfide-linked homodimer of 34-38 kDa.
23069765	1	85	link	cell-derived	161:172	arg1	interleukin-17A					183:197	The T helper cell-derived cytokine interleukin-17A	148:197	The T helper cell-derived cytokine interleukin-17A (IL-17A)	148:206	The T helper cell-derived cytokine interleukin-17A (IL-17A) is a variably glycosylated disulfide-linked homodimer of 34-38 kDa.
23069765	4	86	gly	N-glycosylated	837:850	arg1	polypeptides					852:863	unglycosylated and N-glycosylated polypeptides	818:863	unglycosylated and N-glycosylated polypeptides	818:863	The mass spectrum of IL-17A monomer also included peaks shifted by +948 Da from the respective masses of unglycosylated and N-glycosylated polypeptides.
23069765	0	87	gly	O-glycosylation	22:36	arg1	interleukin-17A					93:107	human recombinant interleukin-17A	75:107	human recombinant interleukin-17A	75:107	Unexpected mucin-type O-glycosylation and host-specific N-glycosylation of human recombinant interleukin-17A expressed in a human kidney cell line.
23069765	2	88	theme	recombinant	364:374	arg1	IL-17A					376:381	human recombinant IL-17A	358:381	human recombinant IL-17A	358:381	Its polypeptide monomer contains one canonical N-glycosylation site at Asn68, and human recombinant IL-17A was partly N-glycosylated when expressed in human kidney (HEK293) cells as a fusion protein with a melittin signal sequence and an N-terminal hexahistidine tag.
23069765	3	89	theme	cells	706:710	arg1	characteristic					672:685	the GalNAc-terminated type characteristic	645:685	the GalNAc-terminated type characteristic of cultured kidney cells	645:710	Orbitrap mass analyses of the tryptic N-glycopeptide 63-69 indicated that the N-glycosylation was of the GalNAc-terminated type characteristic of cultured kidney cells.
23069765	4	90	theme	unglycosylated	818:831	arg1	polypeptides					852:863	unglycosylated and N-glycosylated polypeptides	818:863	unglycosylated and N-glycosylated polypeptides	818:863	The mass spectrum of IL-17A monomer also included peaks shifted by +948 Da from the respective masses of unglycosylated and N-glycosylated polypeptides.
23069765	7	91	theme	T	1339:1339	arg1	cytokine					1354:1361	the T cell-derived cytokine	1335:1361	the T cell-derived cytokine	1335:1361	Therefore, the kidney host cell line not only imposed its characteristic pattern of N-glycosylation on recombinant IL-17A but additionally created an O-glycosylation not known to be present in the T cell-derived cytokine.
23069765	4	92	theme	N-glycosylated	837:850	arg1	polypeptides					852:863	unglycosylated and N-glycosylated polypeptides	818:863	unglycosylated and N-glycosylated polypeptides	818:863	The mass spectrum of IL-17A monomer also included peaks shifted by +948 Da from the respective masses of unglycosylated and N-glycosylated polypeptides.
23069765	3	93	theme	Orbitrap	544:551	arg1	analyses					558:565	Orbitrap mass analyses	544:565	Orbitrap mass analyses of the tryptic N-glycopeptide 63-69	544:601	Orbitrap mass analyses of the tryptic N-glycopeptide 63-69 indicated that the N-glycosylation was of the GalNAc-terminated type characteristic of cultured kidney cells.
23069765	1	94	theme	kDa	271:273	arg1	homodimer					252:260	a variably glycosylated disulfide-linked homodimer	211:260	a variably glycosylated disulfide-linked homodimer of 34-38 kDa	211:273	The T helper cell-derived cytokine interleukin-17A (IL-17A) is a variably glycosylated disulfide-linked homodimer of 34-38 kDa.
23069765	1	94	theme	kDa	271:273	arg1	interleukin-17A					183:197	The T helper cell-derived cytokine interleukin-17A	148:197	The T helper cell-derived cytokine interleukin-17A (IL-17A)	148:206	The T helper cell-derived cytokine interleukin-17A (IL-17A) is a variably glycosylated disulfide-linked homodimer of 34-38 kDa.
23662732	3	0	from	preparation	411:421	arg1	advanced					392:399	advanced	392:399	advanced	392:399	While the field has advanced in sample preparation and detection, automated data analysis remains an important goal.
23662732	4	1	theme	liquid	763:768	arg1	LC/MS/MS					811:818	LC/MS/MS	811:818	LC/MS/MS	811:818	A new bioinformatics approach implemented in software called GP Finder automatically distinguishes correct assignments from random matches and complements experimental techniques that are optimal for glycopeptides, including nonspecific proteolysis and high mass resolution liquid chromatography/tandem mass spectrometry (LC/MS/MS).
23662732	4	1	theme	liquid	763:768	arg1	spectrometry					797:808	high mass resolution liquid chromatography/tandem mass spectrometry	742:808	high mass resolution liquid chromatography/tandem mass spectrometry (LC/MS/MS)	742:819	A new bioinformatics approach implemented in software called GP Finder automatically distinguishes correct assignments from random matches and complements experimental techniques that are optimal for glycopeptides, including nonspecific proteolysis and high mass resolution liquid chromatography/tandem mass spectrometry (LC/MS/MS).
23662732	1	2	theme	glycoproteins	161:173	arg1	SSG					153:155	SSG	153:155	SSG	153:155	Site-specific glycosylation (SSG) of glycoproteins remains a considerable challenge and limits further progress in the areas of proteomics and glycomics.
23662732	1	2	theme	glycoproteins	161:173	arg1	glycosylation					138:150	Site-specific glycosylation	124:150	Site-specific glycosylation (SSG) of glycoproteins	124:173	Site-specific glycosylation (SSG) of glycoproteins remains a considerable challenge and limits further progress in the areas of proteomics and glycomics.
23662732	6	3	gly	N-glycoproteins	1241:1255	arg1	N-glycoproteins					1241:1255	N-glycoproteins	1241:1255	N-glycoproteins from unprocessed human milk and O-glycoproteins from very-low-density-lipoprotein (vLDL) particles	1241:1354	The approach was further applied to a mixture of N-glycoproteins from unprocessed human milk and O-glycoproteins from very-low-density-lipoprotein (vLDL) particles.
23662732	0	4	theme	glycan	77:82	arg1	heterogeneity					84:96	extensive glycan heterogeneity	67:96	extensive glycan heterogeneity of glycoprotein mixtures	67:121	Automated assignments of N- and O-site specific glycosylation with extensive glycan heterogeneity of glycoprotein mixtures.
23662732	5	5	theme	5	973:973	arg1	%					974:974	%	974:974	%	974:974	SSG for multiple N- and O-glycosylation sites, including extensive glycan heterogeneity, was annotated for single proteins and protein mixtures with a 5% false-discovery rate, generating hundreds of nonrandom glycopeptide matches and demonstrating the proof-of-concept for a self-consistency scoring algorithm shown to be compliant with the target-decoy approach (TDA).
23662732	4	6	theme	resolution	752:761	arg1	LC/MS/MS					811:818	LC/MS/MS	811:818	LC/MS/MS	811:818	A new bioinformatics approach implemented in software called GP Finder automatically distinguishes correct assignments from random matches and complements experimental techniques that are optimal for glycopeptides, including nonspecific proteolysis and high mass resolution liquid chromatography/tandem mass spectrometry (LC/MS/MS).
23662732	4	6	theme	resolution	752:761	arg1	spectrometry					797:808	high mass resolution liquid chromatography/tandem mass spectrometry	742:808	high mass resolution liquid chromatography/tandem mass spectrometry (LC/MS/MS)	742:819	A new bioinformatics approach implemented in software called GP Finder automatically distinguishes correct assignments from random matches and complements experimental techniques that are optimal for glycopeptides, including nonspecific proteolysis and high mass resolution liquid chromatography/tandem mass spectrometry (LC/MS/MS).
23662732	1	7	theme	glycomics	267:275	arg1	areas					243:247	the areas	239:247	the areas of proteomics and glycomics	239:275	Site-specific glycosylation (SSG) of glycoproteins remains a considerable challenge and limits further progress in the areas of proteomics and glycomics.
23662732	0	8	theme	glycoprotein	101:112	arg1	mixtures					114:121	glycoprotein mixtures	101:121	glycoprotein mixtures	101:121	Automated assignments of N- and O-site specific glycosylation with extensive glycan heterogeneity of glycoprotein mixtures.
23662732	3	9	from	detection	427:435	arg1	advanced					392:399	advanced	392:399	advanced	392:399	While the field has advanced in sample preparation and detection, automated data analysis remains an important goal.
23662732	6	10	gly	O-glycoproteins	1289:1303	arg1	O-glycoproteins					1289:1303	O-glycoproteins	1289:1303	O-glycoproteins	1289:1303	The approach was further applied to a mixture of N-glycoproteins from unprocessed human milk and O-glycoproteins from very-low-density-lipoprotein (vLDL) particles.
23662732	5	11	theme	matches	1044:1050	arg1	hundreds					1009:1016	hundreds	1009:1016	hundreds of nonrandom glycopeptide matches	1009:1050	SSG for multiple N- and O-glycosylation sites, including extensive glycan heterogeneity, was annotated for single proteins and protein mixtures with a 5% false-discovery rate, generating hundreds of nonrandom glycopeptide matches and demonstrating the proof-of-concept for a self-consistency scoring algorithm shown to be compliant with the target-decoy approach (TDA).
23662732	5	12	dep	N-	839:840	arg1	sites					862:866	sites	862:866	sites	862:866	SSG for multiple N- and O-glycosylation sites, including extensive glycan heterogeneity, was annotated for single proteins and protein mixtures with a 5% false-discovery rate, generating hundreds of nonrandom glycopeptide matches and demonstrating the proof-of-concept for a self-consistency scoring algorithm shown to be compliant with the target-decoy approach (TDA).
23662732	5	13	with	proteins	936:943	arg1	rate					992:995	a 5% false-discovery rate	971:995	a 5% false-discovery rate	971:995	SSG for multiple N- and O-glycosylation sites, including extensive glycan heterogeneity, was annotated for single proteins and protein mixtures with a 5% false-discovery rate, generating hundreds of nonrandom glycopeptide matches and demonstrating the proof-of-concept for a self-consistency scoring algorithm shown to be compliant with the target-decoy approach (TDA).
23662732	6	14	theme	human	1274:1278	arg1	milk					1280:1283	unprocessed human milk	1262:1283	unprocessed human milk	1262:1283	The approach was further applied to a mixture of N-glycoproteins from unprocessed human milk and O-glycoproteins from very-low-density-lipoprotein (vLDL) particles.
23662732	2	15	theme	new	304:306	arg1	approaches					308:317	new approaches	304:317	new approaches in sample preparation, detection, and data analysis	304:369	Effective methods require new approaches in sample preparation, detection, and data analysis.
23662732	5	16	gly	glycopeptide	1031:1042	arg2	glycopeptide					1031:1042	nonrandom glycopeptide matches	1021:1050	nonrandom glycopeptide matches	1021:1050	SSG for multiple N- and O-glycosylation sites, including extensive glycan heterogeneity, was annotated for single proteins and protein mixtures with a 5% false-discovery rate, generating hundreds of nonrandom glycopeptide matches and demonstrating the proof-of-concept for a self-consistency scoring algorithm shown to be compliant with the target-decoy approach (TDA).
23662732	2	17	theme	data	357:360	arg1	analysis					362:369	data analysis	357:369	data analysis	357:369	Effective methods require new approaches in sample preparation, detection, and data analysis.
23662732	6	18	theme	unprocessed	1262:1272	arg1	milk					1280:1283	unprocessed human milk	1262:1283	unprocessed human milk	1262:1283	The approach was further applied to a mixture of N-glycoproteins from unprocessed human milk and O-glycoproteins from very-low-density-lipoprotein (vLDL) particles.
23662732	6	19	from	particles	1346:1354	arg1	O-glycoproteins					1289:1303	O-glycoproteins	1289:1303	O-glycoproteins	1289:1303	The approach was further applied to a mixture of N-glycoproteins from unprocessed human milk and O-glycoproteins from very-low-density-lipoprotein (vLDL) particles.
23662732	6	19	from	particles	1346:1354	arg1	milk					1280:1283	unprocessed human milk	1262:1283	unprocessed human milk	1262:1283	The approach was further applied to a mixture of N-glycoproteins from unprocessed human milk and O-glycoproteins from very-low-density-lipoprotein (vLDL) particles.
23662732	3	20	theme	data	448:451	arg1	analysis					453:460	automated data analysis	438:460	automated data analysis	438:460	While the field has advanced in sample preparation and detection, automated data analysis remains an important goal.
23662732	0	21	theme	mixtures	114:121	arg1	heterogeneity					84:96	extensive glycan heterogeneity	67:96	extensive glycan heterogeneity of glycoprotein mixtures	67:121	Automated assignments of N- and O-site specific glycosylation with extensive glycan heterogeneity of glycoprotein mixtures.
23662732	3	22	from	advanced	392:399	arg1	preparation					411:421	sample preparation	404:421	sample preparation	404:421	While the field has advanced in sample preparation and detection, automated data analysis remains an important goal.
23662732	3	22	from	advanced	392:399	arg1	detection					427:435	detection	427:435	detection	427:435	While the field has advanced in sample preparation and detection, automated data analysis remains an important goal.
23662732	0	23	gly	heterogeneity	84:96	arg1	mixtures					114:121	glycoprotein mixtures	101:121	glycoprotein mixtures	101:121	Automated assignments of N- and O-site specific glycosylation with extensive glycan heterogeneity of glycoprotein mixtures.
23662732	6	24	from	milk	1280:1283	arg1	N-glycoproteins					1241:1255	N-glycoproteins	1241:1255	N-glycoproteins from unprocessed human milk and O-glycoproteins from very-low-density-lipoprotein (vLDL) particles	1241:1354	The approach was further applied to a mixture of N-glycoproteins from unprocessed human milk and O-glycoproteins from very-low-density-lipoprotein (vLDL) particles.
23662732	6	24	from	milk	1280:1283	arg1	mixture					1230:1236	a mixture	1228:1236	a mixture of N-glycoproteins from unprocessed human milk and O-glycoproteins from very-low-density-lipoprotein (vLDL) particles	1228:1354	The approach was further applied to a mixture of N-glycoproteins from unprocessed human milk and O-glycoproteins from very-low-density-lipoprotein (vLDL) particles.
23662732	1	25	theme	considerable	185:196	arg1	challenge					198:206	a considerable challenge	183:206	a considerable challenge	183:206	Site-specific glycosylation (SSG) of glycoproteins remains a considerable challenge and limits further progress in the areas of proteomics and glycomics.
23662732	5	26	theme	extensive	879:887	arg1	heterogeneity					896:908	extensive glycan heterogeneity	879:908	extensive glycan heterogeneity	879:908	SSG for multiple N- and O-glycosylation sites, including extensive glycan heterogeneity, was annotated for single proteins and protein mixtures with a 5% false-discovery rate, generating hundreds of nonrandom glycopeptide matches and demonstrating the proof-of-concept for a self-consistency scoring algorithm shown to be compliant with the target-decoy approach (TDA).
23662732	4	27	theme	new	491:493	arg1	approach					510:517	A new bioinformatics approach	489:517	A new bioinformatics approach implemented in software called GP Finder	489:558	A new bioinformatics approach implemented in software called GP Finder automatically distinguishes correct assignments from random matches and complements experimental techniques that are optimal for glycopeptides, including nonspecific proteolysis and high mass resolution liquid chromatography/tandem mass spectrometry (LC/MS/MS).
23662732	4	28	gly	glycopeptides	689:701	arg2	spectrometry					797:808	high mass resolution liquid chromatography/tandem mass spectrometry	742:808	high mass resolution liquid chromatography/tandem mass spectrometry (LC/MS/MS)	742:819	A new bioinformatics approach implemented in software called GP Finder automatically distinguishes correct assignments from random matches and complements experimental techniques that are optimal for glycopeptides, including nonspecific proteolysis and high mass resolution liquid chromatography/tandem mass spectrometry (LC/MS/MS).
23662732	4	28	gly	glycopeptides	689:701	arg2	proteolysis					726:736	nonspecific proteolysis	714:736	nonspecific proteolysis	714:736	A new bioinformatics approach implemented in software called GP Finder automatically distinguishes correct assignments from random matches and complements experimental techniques that are optimal for glycopeptides, including nonspecific proteolysis and high mass resolution liquid chromatography/tandem mass spectrometry (LC/MS/MS).
23662732	4	28	gly	glycopeptides	689:701	arg2	glycopeptides					689:701	glycopeptides	689:701	glycopeptides	689:701	A new bioinformatics approach implemented in software called GP Finder automatically distinguishes correct assignments from random matches and complements experimental techniques that are optimal for glycopeptides, including nonspecific proteolysis and high mass resolution liquid chromatography/tandem mass spectrometry (LC/MS/MS).
23662732	6	29	theme	N-glycoproteins	1241:1255	arg1	mixture					1230:1236	a mixture	1228:1236	a mixture of N-glycoproteins from unprocessed human milk and O-glycoproteins from very-low-density-lipoprotein (vLDL) particles	1228:1354	The approach was further applied to a mixture of N-glycoproteins from unprocessed human milk and O-glycoproteins from very-low-density-lipoprotein (vLDL) particles.
23662732	5	30	with	compliant	1144:1152	arg1	approach					1176:1183	the target-decoy approach	1159:1183	the target-decoy approach (TDA)	1159:1189	SSG for multiple N- and O-glycosylation sites, including extensive glycan heterogeneity, was annotated for single proteins and protein mixtures with a 5% false-discovery rate, generating hundreds of nonrandom glycopeptide matches and demonstrating the proof-of-concept for a self-consistency scoring algorithm shown to be compliant with the target-decoy approach (TDA).
23662732	5	30	with	compliant	1144:1152	arg1	TDA					1186:1188	TDA	1186:1188	TDA	1186:1188	SSG for multiple N- and O-glycosylation sites, including extensive glycan heterogeneity, was annotated for single proteins and protein mixtures with a 5% false-discovery rate, generating hundreds of nonrandom glycopeptide matches and demonstrating the proof-of-concept for a self-consistency scoring algorithm shown to be compliant with the target-decoy approach (TDA).
23662732	5	31	theme	protein	949:955	arg1	mixtures					957:964	protein mixtures	949:964	protein mixtures with a 5% false-discovery rate	949:995	SSG for multiple N- and O-glycosylation sites, including extensive glycan heterogeneity, was annotated for single proteins and protein mixtures with a 5% false-discovery rate, generating hundreds of nonrandom glycopeptide matches and demonstrating the proof-of-concept for a self-consistency scoring algorithm shown to be compliant with the target-decoy approach (TDA).
23662732	0	32	theme	Automated	0:8	arg1	assignments					10:20	Automated assignments	0:20	Automated assignments of N- and O-site specific glycosylation with extensive glycan heterogeneity of glycoprotein mixtures.	0:122	Automated assignments of N- and O-site specific glycosylation with extensive glycan heterogeneity of glycoprotein mixtures.
23662732	4	33	theme	correct	588:594	arg1	assignments					596:606	correct assignments	588:606	correct assignments	588:606	A new bioinformatics approach implemented in software called GP Finder automatically distinguishes correct assignments from random matches and complements experimental techniques that are optimal for glycopeptides, including nonspecific proteolysis and high mass resolution liquid chromatography/tandem mass spectrometry (LC/MS/MS).
23662732	0	34	gly	glycoprotein	101:112	arg1	glycoprotein					101:112	glycoprotein mixtures	101:121	glycoprotein mixtures	101:121	Automated assignments of N- and O-site specific glycosylation with extensive glycan heterogeneity of glycoprotein mixtures.
23662732	6	35	from	mixture	1230:1236	arg1	O-glycoproteins					1289:1303	O-glycoproteins	1289:1303	O-glycoproteins	1289:1303	The approach was further applied to a mixture of N-glycoproteins from unprocessed human milk and O-glycoproteins from very-low-density-lipoprotein (vLDL) particles.
23662732	6	35	from	mixture	1230:1236	arg1	milk					1280:1283	unprocessed human milk	1262:1283	unprocessed human milk	1262:1283	The approach was further applied to a mixture of N-glycoproteins from unprocessed human milk and O-glycoproteins from very-low-density-lipoprotein (vLDL) particles.
23662732	3	36	theme	automated	438:446	arg1	analysis					453:460	automated data analysis	438:460	automated data analysis	438:460	While the field has advanced in sample preparation and detection, automated data analysis remains an important goal.
23662732	0	37	theme	N-	25:26	arg1	assignments					10:20	Automated assignments	0:20	Automated assignments of N- and O-site specific glycosylation with extensive glycan heterogeneity of glycoprotein mixtures.	0:122	Automated assignments of N- and O-site specific glycosylation with extensive glycan heterogeneity of glycoprotein mixtures.
23662732	5	38	theme	glycan	889:894	arg1	heterogeneity					896:908	extensive glycan heterogeneity	879:908	extensive glycan heterogeneity	879:908	SSG for multiple N- and O-glycosylation sites, including extensive glycan heterogeneity, was annotated for single proteins and protein mixtures with a 5% false-discovery rate, generating hundreds of nonrandom glycopeptide matches and demonstrating the proof-of-concept for a self-consistency scoring algorithm shown to be compliant with the target-decoy approach (TDA).
23662732	1	39	gly	glycosylation	138:150	arg1	glycoproteins					161:173	glycoproteins	161:173	glycoproteins	161:173	Site-specific glycosylation (SSG) of glycoproteins remains a considerable challenge and limits further progress in the areas of proteomics and glycomics.
23662732	2	40	theme	sample	322:327	arg1	preparation					329:339	sample preparation	322:339	sample preparation	322:339	Effective methods require new approaches in sample preparation, detection, and data analysis.
23662732	3	41	theme	important	473:481	arg1	goal					483:486	an important goal	470:486	an important goal	470:486	While the field has advanced in sample preparation and detection, automated data analysis remains an important goal.
23662732	5	42	theme	target-decoy	1163:1174	arg1	approach					1176:1183	the target-decoy approach	1159:1183	the target-decoy approach (TDA)	1159:1189	SSG for multiple N- and O-glycosylation sites, including extensive glycan heterogeneity, was annotated for single proteins and protein mixtures with a 5% false-discovery rate, generating hundreds of nonrandom glycopeptide matches and demonstrating the proof-of-concept for a self-consistency scoring algorithm shown to be compliant with the target-decoy approach (TDA).
23662732	5	42	theme	target-decoy	1163:1174	arg1	TDA					1186:1188	TDA	1186:1188	TDA	1186:1188	SSG for multiple N- and O-glycosylation sites, including extensive glycan heterogeneity, was annotated for single proteins and protein mixtures with a 5% false-discovery rate, generating hundreds of nonrandom glycopeptide matches and demonstrating the proof-of-concept for a self-consistency scoring algorithm shown to be compliant with the target-decoy approach (TDA).
23662732	5	43	theme	glycopeptide	1031:1042	arg1	matches					1044:1050	nonrandom glycopeptide matches	1021:1050	nonrandom glycopeptide matches	1021:1050	SSG for multiple N- and O-glycosylation sites, including extensive glycan heterogeneity, was annotated for single proteins and protein mixtures with a 5% false-discovery rate, generating hundreds of nonrandom glycopeptide matches and demonstrating the proof-of-concept for a self-consistency scoring algorithm shown to be compliant with the target-decoy approach (TDA).
23662732	1	44	theme	further	219:225	arg1	progress					227:234	further progress	219:234	further progress in the areas of proteomics and glycomics	219:275	Site-specific glycosylation (SSG) of glycoproteins remains a considerable challenge and limits further progress in the areas of proteomics and glycomics.
23662732	0	45	theme	O-site	32:37	arg1	glycosylation					48:60	O-site specific glycosylation	32:60	O-site specific glycosylation	32:60	Automated assignments of N- and O-site specific glycosylation with extensive glycan heterogeneity of glycoprotein mixtures.
23662732	6	46	theme	vLDL	1340:1343	arg1	particles					1346:1354	very-low-density-lipoprotein (vLDL) particles	1310:1354	very-low-density-lipoprotein (vLDL) particles	1310:1354	The approach was further applied to a mixture of N-glycoproteins from unprocessed human milk and O-glycoproteins from very-low-density-lipoprotein (vLDL) particles.
23662732	5	47	theme	scoring	1114:1120	arg1	algorithm					1122:1130	a self-consistency scoring algorithm	1095:1130	a self-consistency scoring algorithm shown to be compliant with the target-decoy approach (TDA)	1095:1189	SSG for multiple N- and O-glycosylation sites, including extensive glycan heterogeneity, was annotated for single proteins and protein mixtures with a 5% false-discovery rate, generating hundreds of nonrandom glycopeptide matches and demonstrating the proof-of-concept for a self-consistency scoring algorithm shown to be compliant with the target-decoy approach (TDA).
23662732	4	48	theme	nonspecific	714:724	arg1	proteolysis					726:736	nonspecific proteolysis	714:736	nonspecific proteolysis	714:736	A new bioinformatics approach implemented in software called GP Finder automatically distinguishes correct assignments from random matches and complements experimental techniques that are optimal for glycopeptides, including nonspecific proteolysis and high mass resolution liquid chromatography/tandem mass spectrometry (LC/MS/MS).
23662732	4	49	theme	GP	550:551	arg1	Finder					553:558	software called GP Finder	534:558	software called GP Finder	534:558	A new bioinformatics approach implemented in software called GP Finder automatically distinguishes correct assignments from random matches and complements experimental techniques that are optimal for glycopeptides, including nonspecific proteolysis and high mass resolution liquid chromatography/tandem mass spectrometry (LC/MS/MS).
23662732	4	50	theme	random	613:618	arg1	matches					620:626	random matches	613:626	random matches	613:626	A new bioinformatics approach implemented in software called GP Finder automatically distinguishes correct assignments from random matches and complements experimental techniques that are optimal for glycopeptides, including nonspecific proteolysis and high mass resolution liquid chromatography/tandem mass spectrometry (LC/MS/MS).
23662732	1	51	from	progress	227:234	arg1	areas					243:247	the areas	239:247	the areas of proteomics and glycomics	239:275	Site-specific glycosylation (SSG) of glycoproteins remains a considerable challenge and limits further progress in the areas of proteomics and glycomics.
23662732	5	52	theme	single	929:934	arg1	proteins					936:943	single proteins	929:943	single proteins	929:943	SSG for multiple N- and O-glycosylation sites, including extensive glycan heterogeneity, was annotated for single proteins and protein mixtures with a 5% false-discovery rate, generating hundreds of nonrandom glycopeptide matches and demonstrating the proof-of-concept for a self-consistency scoring algorithm shown to be compliant with the target-decoy approach (TDA).
23662732	0	53	theme	glycosylation	48:60	arg1	assignments					10:20	Automated assignments	0:20	Automated assignments of N- and O-site specific glycosylation with extensive glycan heterogeneity of glycoprotein mixtures.	0:122	Automated assignments of N- and O-site specific glycosylation with extensive glycan heterogeneity of glycoprotein mixtures.
23662732	4	54	theme	called	543:548	arg1	Finder					553:558	software called GP Finder	534:558	software called GP Finder	534:558	A new bioinformatics approach implemented in software called GP Finder automatically distinguishes correct assignments from random matches and complements experimental techniques that are optimal for glycopeptides, including nonspecific proteolysis and high mass resolution liquid chromatography/tandem mass spectrometry (LC/MS/MS).
23662732	5	55	theme	multiple	830:837	arg1	N-					839:840	multiple N-	830:840	multiple N-	830:840	SSG for multiple N- and O-glycosylation sites, including extensive glycan heterogeneity, was annotated for single proteins and protein mixtures with a 5% false-discovery rate, generating hundreds of nonrandom glycopeptide matches and demonstrating the proof-of-concept for a self-consistency scoring algorithm shown to be compliant with the target-decoy approach (TDA).
23662732	5	56	dep	proteins	936:943	arg1	demonstrating					1056:1068	demonstrating	1056:1068	demonstrating the proof-of-concept for a self-consistency scoring algorithm shown to be compliant with the target-decoy approach (TDA)	1056:1189	SSG for multiple N- and O-glycosylation sites, including extensive glycan heterogeneity, was annotated for single proteins and protein mixtures with a 5% false-discovery rate, generating hundreds of nonrandom glycopeptide matches and demonstrating the proof-of-concept for a self-consistency scoring algorithm shown to be compliant with the target-decoy approach (TDA).
23662732	5	56	dep	proteins	936:943	arg1	generating					998:1007	generating	998:1007	generating hundreds of nonrandom glycopeptide matches	998:1050	SSG for multiple N- and O-glycosylation sites, including extensive glycan heterogeneity, was annotated for single proteins and protein mixtures with a 5% false-discovery rate, generating hundreds of nonrandom glycopeptide matches and demonstrating the proof-of-concept for a self-consistency scoring algorithm shown to be compliant with the target-decoy approach (TDA).
23662732	4	57	theme	bioinformatics	495:508	arg1	approach					510:517	A new bioinformatics approach	489:517	A new bioinformatics approach implemented in software called GP Finder	489:558	A new bioinformatics approach implemented in software called GP Finder automatically distinguishes correct assignments from random matches and complements experimental techniques that are optimal for glycopeptides, including nonspecific proteolysis and high mass resolution liquid chromatography/tandem mass spectrometry (LC/MS/MS).
23662732	1	58	theme	Site-specific	124:136	arg1	SSG					153:155	SSG	153:155	SSG	153:155	Site-specific glycosylation (SSG) of glycoproteins remains a considerable challenge and limits further progress in the areas of proteomics and glycomics.
23662732	1	58	theme	Site-specific	124:136	arg1	glycosylation					138:150	Site-specific glycosylation	124:150	Site-specific glycosylation (SSG) of glycoproteins	124:173	Site-specific glycosylation (SSG) of glycoproteins remains a considerable challenge and limits further progress in the areas of proteomics and glycomics.
23662732	0	59	theme	specific	39:46	arg1	glycosylation					48:60	O-site specific glycosylation	32:60	O-site specific glycosylation	32:60	Automated assignments of N- and O-site specific glycosylation with extensive glycan heterogeneity of glycoprotein mixtures.
23662732	5	60	with	mixtures	957:964	arg1	rate					992:995	a 5% false-discovery rate	971:995	a 5% false-discovery rate	971:995	SSG for multiple N- and O-glycosylation sites, including extensive glycan heterogeneity, was annotated for single proteins and protein mixtures with a 5% false-discovery rate, generating hundreds of nonrandom glycopeptide matches and demonstrating the proof-of-concept for a self-consistency scoring algorithm shown to be compliant with the target-decoy approach (TDA).
23662732	0	61	with	assignments	10:20	arg1	heterogeneity					84:96	extensive glycan heterogeneity	67:96	extensive glycan heterogeneity of glycoprotein mixtures	67:121	Automated assignments of N- and O-site specific glycosylation with extensive glycan heterogeneity of glycoprotein mixtures.
23662732	4	62	theme	chromatography/tandem	770:790	arg1	LC/MS/MS					811:818	LC/MS/MS	811:818	LC/MS/MS	811:818	A new bioinformatics approach implemented in software called GP Finder automatically distinguishes correct assignments from random matches and complements experimental techniques that are optimal for glycopeptides, including nonspecific proteolysis and high mass resolution liquid chromatography/tandem mass spectrometry (LC/MS/MS).
23662732	4	62	theme	chromatography/tandem	770:790	arg1	spectrometry					797:808	high mass resolution liquid chromatography/tandem mass spectrometry	742:808	high mass resolution liquid chromatography/tandem mass spectrometry (LC/MS/MS)	742:819	A new bioinformatics approach implemented in software called GP Finder automatically distinguishes correct assignments from random matches and complements experimental techniques that are optimal for glycopeptides, including nonspecific proteolysis and high mass resolution liquid chromatography/tandem mass spectrometry (LC/MS/MS).
23662732	4	63	theme	mass	792:795	arg1	LC/MS/MS					811:818	LC/MS/MS	811:818	LC/MS/MS	811:818	A new bioinformatics approach implemented in software called GP Finder automatically distinguishes correct assignments from random matches and complements experimental techniques that are optimal for glycopeptides, including nonspecific proteolysis and high mass resolution liquid chromatography/tandem mass spectrometry (LC/MS/MS).
23662732	4	63	theme	mass	792:795	arg1	spectrometry					797:808	high mass resolution liquid chromatography/tandem mass spectrometry	742:808	high mass resolution liquid chromatography/tandem mass spectrometry (LC/MS/MS)	742:819	A new bioinformatics approach implemented in software called GP Finder automatically distinguishes correct assignments from random matches and complements experimental techniques that are optimal for glycopeptides, including nonspecific proteolysis and high mass resolution liquid chromatography/tandem mass spectrometry (LC/MS/MS).
23662732	6	64	theme	very-low-density-lipoprotein	1310:1337	arg1	particles					1346:1354	very-low-density-lipoprotein (vLDL) particles	1310:1354	very-low-density-lipoprotein (vLDL) particles	1310:1354	The approach was further applied to a mixture of N-glycoproteins from unprocessed human milk and O-glycoproteins from very-low-density-lipoprotein (vLDL) particles.
23662732	2	65	theme	Effective	278:286	arg1	methods					288:294	Effective methods	278:294	Effective methods	278:294	Effective methods require new approaches in sample preparation, detection, and data analysis.
23662732	5	66	theme	%	974:974	arg1	rate					992:995	a 5% false-discovery rate	971:995	a 5% false-discovery rate	971:995	SSG for multiple N- and O-glycosylation sites, including extensive glycan heterogeneity, was annotated for single proteins and protein mixtures with a 5% false-discovery rate, generating hundreds of nonrandom glycopeptide matches and demonstrating the proof-of-concept for a self-consistency scoring algorithm shown to be compliant with the target-decoy approach (TDA).
23662732	5	67	theme	nonrandom	1021:1029	arg1	matches					1044:1050	nonrandom glycopeptide matches	1021:1050	nonrandom glycopeptide matches	1021:1050	SSG for multiple N- and O-glycosylation sites, including extensive glycan heterogeneity, was annotated for single proteins and protein mixtures with a 5% false-discovery rate, generating hundreds of nonrandom glycopeptide matches and demonstrating the proof-of-concept for a self-consistency scoring algorithm shown to be compliant with the target-decoy approach (TDA).
23662732	1	68	gly	glycoproteins	161:173	arg1	glycoproteins					161:173	glycoproteins	161:173	glycoproteins	161:173	Site-specific glycosylation (SSG) of glycoproteins remains a considerable challenge and limits further progress in the areas of proteomics and glycomics.
23662732	5	69	theme	false-discovery	976:990	arg1	rate					992:995	a 5% false-discovery rate	971:995	a 5% false-discovery rate	971:995	SSG for multiple N- and O-glycosylation sites, including extensive glycan heterogeneity, was annotated for single proteins and protein mixtures with a 5% false-discovery rate, generating hundreds of nonrandom glycopeptide matches and demonstrating the proof-of-concept for a self-consistency scoring algorithm shown to be compliant with the target-decoy approach (TDA).
23662732	2	70	from	approaches	308:317	arg1	detection					342:350	detection	342:350	detection	342:350	Effective methods require new approaches in sample preparation, detection, and data analysis.
23662732	2	70	from	approaches	308:317	arg1	preparation					329:339	sample preparation	322:339	sample preparation	322:339	Effective methods require new approaches in sample preparation, detection, and data analysis.
23662732	2	70	from	approaches	308:317	arg1	analysis					362:369	data analysis	357:369	data analysis	357:369	Effective methods require new approaches in sample preparation, detection, and data analysis.
23662732	4	71	theme	experimental	644:655	arg1	techniques					657:666	experimental techniques	644:666	experimental techniques that are optimal for glycopeptides, including nonspecific proteolysis and high mass resolution liquid chromatography/tandem mass spectrometry (LC/MS/MS)	644:819	A new bioinformatics approach implemented in software called GP Finder automatically distinguishes correct assignments from random matches and complements experimental techniques that are optimal for glycopeptides, including nonspecific proteolysis and high mass resolution liquid chromatography/tandem mass spectrometry (LC/MS/MS).
23662732	0	72	theme	extensive	67:75	arg1	heterogeneity					84:96	extensive glycan heterogeneity	67:96	extensive glycan heterogeneity of glycoprotein mixtures	67:121	Automated assignments of N- and O-site specific glycosylation with extensive glycan heterogeneity of glycoprotein mixtures.
23662732	4	73	theme	mass	747:750	arg1	LC/MS/MS					811:818	LC/MS/MS	811:818	LC/MS/MS	811:818	A new bioinformatics approach implemented in software called GP Finder automatically distinguishes correct assignments from random matches and complements experimental techniques that are optimal for glycopeptides, including nonspecific proteolysis and high mass resolution liquid chromatography/tandem mass spectrometry (LC/MS/MS).
23662732	4	73	theme	mass	747:750	arg1	spectrometry					797:808	high mass resolution liquid chromatography/tandem mass spectrometry	742:808	high mass resolution liquid chromatography/tandem mass spectrometry (LC/MS/MS)	742:819	A new bioinformatics approach implemented in software called GP Finder automatically distinguishes correct assignments from random matches and complements experimental techniques that are optimal for glycopeptides, including nonspecific proteolysis and high mass resolution liquid chromatography/tandem mass spectrometry (LC/MS/MS).
23662732	3	74	theme	sample	404:409	arg1	preparation					411:421	sample preparation	404:421	sample preparation	404:421	While the field has advanced in sample preparation and detection, automated data analysis remains an important goal.
23662732	5	75	theme	self-consistency	1097:1112	arg1	algorithm					1122:1130	a self-consistency scoring algorithm	1095:1130	a self-consistency scoring algorithm shown to be compliant with the target-decoy approach (TDA)	1095:1189	SSG for multiple N- and O-glycosylation sites, including extensive glycan heterogeneity, was annotated for single proteins and protein mixtures with a 5% false-discovery rate, generating hundreds of nonrandom glycopeptide matches and demonstrating the proof-of-concept for a self-consistency scoring algorithm shown to be compliant with the target-decoy approach (TDA).
23662732	4	76	theme	high	742:745	arg1	LC/MS/MS					811:818	LC/MS/MS	811:818	LC/MS/MS	811:818	A new bioinformatics approach implemented in software called GP Finder automatically distinguishes correct assignments from random matches and complements experimental techniques that are optimal for glycopeptides, including nonspecific proteolysis and high mass resolution liquid chromatography/tandem mass spectrometry (LC/MS/MS).
23662732	4	76	theme	high	742:745	arg1	spectrometry					797:808	high mass resolution liquid chromatography/tandem mass spectrometry	742:808	high mass resolution liquid chromatography/tandem mass spectrometry (LC/MS/MS)	742:819	A new bioinformatics approach implemented in software called GP Finder automatically distinguishes correct assignments from random matches and complements experimental techniques that are optimal for glycopeptides, including nonspecific proteolysis and high mass resolution liquid chromatography/tandem mass spectrometry (LC/MS/MS).
23662732	6	77	from	O-glycoproteins	1289:1303	arg1	N-glycoproteins					1241:1255	N-glycoproteins	1241:1255	N-glycoproteins from unprocessed human milk and O-glycoproteins from very-low-density-lipoprotein (vLDL) particles	1241:1354	The approach was further applied to a mixture of N-glycoproteins from unprocessed human milk and O-glycoproteins from very-low-density-lipoprotein (vLDL) particles.
23662732	6	77	from	O-glycoproteins	1289:1303	arg1	mixture					1230:1236	a mixture	1228:1236	a mixture of N-glycoproteins from unprocessed human milk and O-glycoproteins from very-low-density-lipoprotein (vLDL) particles	1228:1354	The approach was further applied to a mixture of N-glycoproteins from unprocessed human milk and O-glycoproteins from very-low-density-lipoprotein (vLDL) particles.
23662732	1	78	theme	proteomics	252:261	arg1	areas					243:247	the areas	239:247	the areas of proteomics and glycomics	239:275	Site-specific glycosylation (SSG) of glycoproteins remains a considerable challenge and limits further progress in the areas of proteomics and glycomics.
16401092	2	0	theme	glycoprotein	327:338	arg1	mZP3					351:354	the mZP glycoprotein designated mZP3	319:354	the mZP glycoprotein designated mZP3	319:354	O-Glycans occupying two highly conserved vicinal glycosylation sites (Ser-332 and Ser-334) on the mZP glycoprotein designated mZP3 were previously implicated in this interaction.
16401092	2	1	theme	glycosylation	274:286	arg1	Ser-332					295:301	Ser-332	295:301	Ser-332	295:301	O-Glycans occupying two highly conserved vicinal glycosylation sites (Ser-332 and Ser-334) on the mZP glycoprotein designated mZP3 were previously implicated in this interaction.
16401092	2	1	theme	glycosylation	274:286	arg1	sites					288:292	two highly conserved vicinal glycosylation sites	245:292	two highly conserved vicinal glycosylation sites (Ser-332 and Ser-334) on the mZP glycoprotein designated mZP3	245:354	O-Glycans occupying two highly conserved vicinal glycosylation sites (Ser-332 and Ser-334) on the mZP glycoprotein designated mZP3 were previously implicated in this interaction.
16401092	2	1	theme	glycosylation	274:286	arg1	Ser-334					307:313	Ser-334	307:313	Ser-334	307:313	O-Glycans occupying two highly conserved vicinal glycosylation sites (Ser-332 and Ser-334) on the mZP glycoprotein designated mZP3 were previously implicated in this interaction.
16401092	8	2	theme	rescue	1240:1245	arg1	mice					1247:1250	rescue mice	1240:1250	rescue mice	1240:1250	However, in huZP3 derived from rescue mice, the O-glycans associated with Thr-156 (analogous to Thr-155 in mZP3) are exclusively core 1 and related Tn sequences, whereas core 2 O-glycans predominate at the other conserved site.
16401092	2	3	theme	conserved	256:264	arg1	Ser-332					295:301	Ser-332	295:301	Ser-332	295:301	O-Glycans occupying two highly conserved vicinal glycosylation sites (Ser-332 and Ser-334) on the mZP glycoprotein designated mZP3 were previously implicated in this interaction.
16401092	2	3	theme	conserved	256:264	arg1	sites					288:292	two highly conserved vicinal glycosylation sites	245:292	two highly conserved vicinal glycosylation sites (Ser-332 and Ser-334) on the mZP glycoprotein designated mZP3	245:354	O-Glycans occupying two highly conserved vicinal glycosylation sites (Ser-332 and Ser-334) on the mZP glycoprotein designated mZP3 were previously implicated in this interaction.
16401092	2	3	theme	conserved	256:264	arg1	Ser-334					307:313	Ser-334	307:313	Ser-334	307:313	O-Glycans occupying two highly conserved vicinal glycosylation sites (Ser-332 and Ser-334) on the mZP glycoprotein designated mZP3 were previously implicated in this interaction.
16401092	8	4	attach	derived	1227:1233	arg1	mice					1247:1250	rescue mice	1240:1250	rescue mice	1240:1250	However, in huZP3 derived from rescue mice, the O-glycans associated with Thr-156 (analogous to Thr-155 in mZP3) are exclusively core 1 and related Tn sequences, whereas core 2 O-glycans predominate at the other conserved site.
16401092	8	4	attach	derived	1227:1233	arg2	huZP3					1221:1225	huZP3	1221:1225	huZP3 derived from rescue mice	1221:1250	However, in huZP3 derived from rescue mice, the O-glycans associated with Thr-156 (analogous to Thr-155 in mZP3) are exclusively core 1 and related Tn sequences, whereas core 2 O-glycans predominate at the other conserved site.
16401092	8	5	from	sequences	1360:1368	arg1	huZP3					1221:1225	huZP3	1221:1225	huZP3 derived from rescue mice	1221:1250	However, in huZP3 derived from rescue mice, the O-glycans associated with Thr-156 (analogous to Thr-155 in mZP3) are exclusively core 1 and related Tn sequences, whereas core 2 O-glycans predominate at the other conserved site.
16401092	3	6	theme	alternate	497:505	arg1	operational					537:547	operational	537:547	operational	537:547	However, recent biophysical analyses confirm that neither site is occupied, implying that an alternate O-glycosylation domain may be operational in native mZP3.
16401092	3	6	theme	alternate	497:505	arg1	domain					523:528	an alternate O-glycosylation domain	494:528	an alternate O-glycosylation domain	494:528	However, recent biophysical analyses confirm that neither site is occupied, implying that an alternate O-glycosylation domain may be operational in native mZP3.
16401092	1	7	theme	extracellular	178:190	arg1	pellucida					145:153	the zona pellucida	136:153	the zona pellucida (mZP)	136:159	Murine sperm initiate fertilization by binding to the zona pellucida (mZP), the specialized extracellular matrix of their homologous eggs.
16401092	1	7	theme	extracellular	178:190	arg1	matrix					192:197	the specialized extracellular matrix	162:197	the specialized extracellular matrix of their homologous eggs	162:222	Murine sperm initiate fertilization by binding to the zona pellucida (mZP), the specialized extracellular matrix of their homologous eggs.
16401092	9	8	theme	core	1656:1659	arg1	sequence					1663:1670	the core 1 sequence	1652:1670	the core 1 sequence	1652:1670	This unique restriction of O-glycan expression suggests that sequence differences in the conserved O-glycosylation domains of mZP3 and huZP3 affect the ability of core 2 N-acetylglucosaminyltransferase(s) to extend the core 1 sequence.
16401092	8	9	theme	core	1379:1382	arg1	O-glycans					1386:1394	core 2 O-glycans	1379:1394	core 2 O-glycans	1379:1394	However, in huZP3 derived from rescue mice, the O-glycans associated with Thr-156 (analogous to Thr-155 in mZP3) are exclusively core 1 and related Tn sequences, whereas core 2 O-glycans predominate at the other conserved site.
16401092	4	10	theme	O-glycosylation	678:692	arg1	specificity					663:673	the site specificity	654:673	the site specificity of O-glycosylation in both native mZP3 and huZP3	654:722	Since human ZP3 (huZP3) can substitute for mZP3 in rescue mice to mediate sperm binding, the site specificity of O-glycosylation in both native mZP3 and huZP3 was analyzed using ultrasensitive mass spectrometric techniques.
16401092	6	11	gly	glycoprotein	1135:1146	arg1	glycoprotein					1135:1146	an evolutionarily related glycoprotein	1109:1146	an evolutionarily related glycoprotein	1109:1146	Thus, there is a specific O-glycosylation domain within native mZP3 expressing two closely spaced O-glycans that is very well conserved in an evolutionarily related glycoprotein.
16401092	5	12	gly	glycopeptide	871:882	arg2	glycopeptide					871:882	the glycopeptide	867:882	the glycopeptide	867:882	Two O-glycosylation sites in native mZP3, one at Thr-155 and the other within the glycopeptide at positions 161-168 (ATVSSEEK), are conserved in huZP3 derived from transgenic mice.
16401092	3	13	from	mZP3	559:562	arg1	operational					537:547	operational	537:547	operational	537:547	However, recent biophysical analyses confirm that neither site is occupied, implying that an alternate O-glycosylation domain may be operational in native mZP3.
16401092	3	13	from	mZP3	559:562	arg1	domain					523:528	an alternate O-glycosylation domain	494:528	an alternate O-glycosylation domain	494:528	However, recent biophysical analyses confirm that neither site is occupied, implying that an alternate O-glycosylation domain may be operational in native mZP3.
16401092	2	14	from	sites	288:292	arg1	mZP3					351:354	the mZP glycoprotein designated mZP3	319:354	the mZP glycoprotein designated mZP3	319:354	O-Glycans occupying two highly conserved vicinal glycosylation sites (Ser-332 and Ser-334) on the mZP glycoprotein designated mZP3 were previously implicated in this interaction.
16401092	0	15	theme	murine	64:69	arg1	ZP3					81:83	murine and human ZP3	64:83	murine and human ZP3	64:83	Differential O-glycosylation of a conserved domain expressed in murine and human ZP3.
16401092	8	16	dep	core	1338:1341	arg1	whereas					1371:1377	whereas	1371:1377	whereas	1371:1377	However, in huZP3 derived from rescue mice, the O-glycans associated with Thr-156 (analogous to Thr-155 in mZP3) are exclusively core 1 and related Tn sequences, whereas core 2 O-glycans predominate at the other conserved site.
16401092	8	17	theme	other	1415:1419	arg1	site					1431:1434	the other conserved site	1411:1434	the other conserved site	1411:1434	However, in huZP3 derived from rescue mice, the O-glycans associated with Thr-156 (analogous to Thr-155 in mZP3) are exclusively core 1 and related Tn sequences, whereas core 2 O-glycans predominate at the other conserved site.
16401092	2	18	dep	sites	288:292	arg1	Ser-332					295:301	Ser-332	295:301	Ser-332	295:301	O-Glycans occupying two highly conserved vicinal glycosylation sites (Ser-332 and Ser-334) on the mZP glycoprotein designated mZP3 were previously implicated in this interaction.
16401092	2	18	dep	sites	288:292	arg1	sites					288:292	two highly conserved vicinal glycosylation sites	245:292	two highly conserved vicinal glycosylation sites (Ser-332 and Ser-334) on the mZP glycoprotein designated mZP3	245:354	O-Glycans occupying two highly conserved vicinal glycosylation sites (Ser-332 and Ser-334) on the mZP glycoprotein designated mZP3 were previously implicated in this interaction.
16401092	2	18	dep	sites	288:292	arg1	Ser-334					307:313	Ser-334	307:313	Ser-334	307:313	O-Glycans occupying two highly conserved vicinal glycosylation sites (Ser-332 and Ser-334) on the mZP glycoprotein designated mZP3 were previously implicated in this interaction.
16401092	0	19	theme	human	75:79	arg1	ZP3					81:83	murine and human ZP3	64:83	murine and human ZP3	64:83	Differential O-glycosylation of a conserved domain expressed in murine and human ZP3.
16401092	10	20	from	Thr-156	1720:1726	arg1	O-glycosylation					1701:1715	O-glycosylation	1701:1715	O-glycosylation at Thr-156	1701:1726	However, this difference in O-glycosylation at Thr-156 does not affect the fertility or the sperm binding phenotype of eggs derived from female huZP3 rescue mice.
16401092	10	20	from	Thr-156	1720:1726	arg1	difference					1687:1696	this difference	1682:1696	this difference in O-glycosylation at Thr-156	1682:1726	However, this difference in O-glycosylation at Thr-156 does not affect the fertility or the sperm binding phenotype of eggs derived from female huZP3 rescue mice.
16401092	7	21	theme	core	1165:1168	arg1	O-glycans					1172:1180	core 2 O-glycans	1165:1180	core 2 O-glycans	1165:1180	In native mZP3, core 2 O-glycans predominate at both sites.
16401092	5	22	from	sites	809:813	arg1	mZP3					825:828	native mZP3	818:828	native mZP3	818:828	Two O-glycosylation sites in native mZP3, one at Thr-155 and the other within the glycopeptide at positions 161-168 (ATVSSEEK), are conserved in huZP3 derived from transgenic mice.
16401092	9	23	theme	expression	1473:1482	arg1	restriction					1449:1459	This unique restriction	1437:1459	This unique restriction of O-glycan expression	1437:1482	This unique restriction of O-glycan expression suggests that sequence differences in the conserved O-glycosylation domains of mZP3 and huZP3 affect the ability of core 2 N-acetylglucosaminyltransferase(s) to extend the core 1 sequence.
16401092	4	24	theme	ultrasensitive	743:756	arg1	techniques					777:786	ultrasensitive mass spectrometric techniques	743:786	ultrasensitive mass spectrometric techniques	743:786	Since human ZP3 (huZP3) can substitute for mZP3 in rescue mice to mediate sperm binding, the site specificity of O-glycosylation in both native mZP3 and huZP3 was analyzed using ultrasensitive mass spectrometric techniques.
16401092	10	25	from	difference	1687:1696	arg1	O-glycosylation					1701:1715	O-glycosylation	1701:1715	O-glycosylation at Thr-156	1701:1726	However, this difference in O-glycosylation at Thr-156 does not affect the fertility or the sperm binding phenotype of eggs derived from female huZP3 rescue mice.
16401092	10	25	from	difference	1687:1696	arg1	Thr-156					1720:1726	Thr-156	1720:1726	Thr-156	1720:1726	However, this difference in O-glycosylation at Thr-156 does not affect the fertility or the sperm binding phenotype of eggs derived from female huZP3 rescue mice.
16401092	3	26	theme	recent	413:418	arg1	analyses					432:439	recent biophysical analyses	413:439	recent biophysical analyses	413:439	However, recent biophysical analyses confirm that neither site is occupied, implying that an alternate O-glycosylation domain may be operational in native mZP3.
16401092	0	27	theme	Differential	0:11	arg1	O-glycosylation					13:27	Differential O-glycosylation	0:27	Differential O-glycosylation of a conserved domain	0:49	Differential O-glycosylation of a conserved domain expressed in murine and human ZP3.
16401092	1	28	theme	Murine	86:91	arg1	sperm					93:97	Murine sperm	86:97	Murine sperm	86:97	Murine sperm initiate fertilization by binding to the zona pellucida (mZP), the specialized extracellular matrix of their homologous eggs.
16401092	6	29	theme	O-glycosylation	996:1010	arg1	domain					1012:1017	a specific O-glycosylation domain	985:1017	a specific O-glycosylation domain within native mZP3 expressing two closely spaced O-glycans that is very well conserved in an evolutionarily related glycoprotein	985:1146	Thus, there is a specific O-glycosylation domain within native mZP3 expressing two closely spaced O-glycans that is very well conserved in an evolutionarily related glycoprotein.
16401092	2	30	gly	glycoprotein	327:338	arg1	glycoprotein					327:338	the mZP glycoprotein designated mZP3	319:354	the mZP glycoprotein designated mZP3	319:354	O-Glycans occupying two highly conserved vicinal glycosylation sites (Ser-332 and Ser-334) on the mZP glycoprotein designated mZP3 were previously implicated in this interaction.
16401092	5	31	gly	O-glycosylation	793:807	arg2	other					854:858	other	854:858	other	854:858	Two O-glycosylation sites in native mZP3, one at Thr-155 and the other within the glycopeptide at positions 161-168 (ATVSSEEK), are conserved in huZP3 derived from transgenic mice.
16401092	5	31	gly	O-glycosylation	793:807	arg2	sites					809:813	Two O-glycosylation sites	789:813	Two O-glycosylation sites in native mZP3	789:828	Two O-glycosylation sites in native mZP3, one at Thr-155 and the other within the glycopeptide at positions 161-168 (ATVSSEEK), are conserved in huZP3 derived from transgenic mice.
16401092	5	31	gly	O-glycosylation	793:807	arg2	one					831:833	one	831:833	one	831:833	Two O-glycosylation sites in native mZP3, one at Thr-155 and the other within the glycopeptide at positions 161-168 (ATVSSEEK), are conserved in huZP3 derived from transgenic mice.
16401092	5	31	gly	O-glycosylation	793:807	arg2	Two					789:791	Two	789:791	Two	789:791	Two O-glycosylation sites in native mZP3, one at Thr-155 and the other within the glycopeptide at positions 161-168 (ATVSSEEK), are conserved in huZP3 derived from transgenic mice.
16401092	0	32	theme	conserved	34:42	arg1	domain					44:49	a conserved domain	32:49	a conserved domain	32:49	Differential O-glycosylation of a conserved domain expressed in murine and human ZP3.
16401092	9	33	theme	O-glycosylation	1536:1550	arg1	domains					1552:1558	the conserved O-glycosylation domains	1522:1558	the conserved O-glycosylation domains of mZP3 and huZP3	1522:1576	This unique restriction of O-glycan expression suggests that sequence differences in the conserved O-glycosylation domains of mZP3 and huZP3 affect the ability of core 2 N-acetylglucosaminyltransferase(s) to extend the core 1 sequence.
16401092	9	33	theme	O-glycosylation	1536:1550	arg1	huZP3					1572:1576	huZP3	1572:1576	huZP3	1572:1576	This unique restriction of O-glycan expression suggests that sequence differences in the conserved O-glycosylation domains of mZP3 and huZP3 affect the ability of core 2 N-acetylglucosaminyltransferase(s) to extend the core 1 sequence.
16401092	9	33	theme	O-glycosylation	1536:1550	arg1	mZP3					1563:1566	mZP3	1563:1566	mZP3	1563:1566	This unique restriction of O-glycan expression suggests that sequence differences in the conserved O-glycosylation domains of mZP3 and huZP3 affect the ability of core 2 N-acetylglucosaminyltransferase(s) to extend the core 1 sequence.
16401092	10	34	theme	binding	1771:1777	arg1	phenotype					1779:1787	the sperm binding phenotype	1761:1787	the sperm binding phenotype	1761:1787	However, this difference in O-glycosylation at Thr-156 does not affect the fertility or the sperm binding phenotype of eggs derived from female huZP3 rescue mice.
16401092	2	35	theme	mZP	323:325	arg1	mZP3					351:354	the mZP glycoprotein designated mZP3	319:354	the mZP glycoprotein designated mZP3	319:354	O-Glycans occupying two highly conserved vicinal glycosylation sites (Ser-332 and Ser-334) on the mZP glycoprotein designated mZP3 were previously implicated in this interaction.
16401092	10	36	theme	female	1810:1815	arg1	mice					1830:1833	female huZP3 rescue mice	1810:1833	female huZP3 rescue mice	1810:1833	However, this difference in O-glycosylation at Thr-156 does not affect the fertility or the sperm binding phenotype of eggs derived from female huZP3 rescue mice.
16401092	8	37	theme	related	1349:1355	arg1	sequences					1360:1368	related Tn sequences	1349:1368	related Tn sequences	1349:1368	However, in huZP3 derived from rescue mice, the O-glycans associated with Thr-156 (analogous to Thr-155 in mZP3) are exclusively core 1 and related Tn sequences, whereas core 2 O-glycans predominate at the other conserved site.
16401092	0	38	gly	O-glycosylation	13:27	arg1	domain					44:49	a conserved domain	32:49	a conserved domain	32:49	Differential O-glycosylation of a conserved domain expressed in murine and human ZP3.
16401092	5	39	theme	transgenic	953:962	arg1	mice					964:967	transgenic mice	953:967	transgenic mice	953:967	Two O-glycosylation sites in native mZP3, one at Thr-155 and the other within the glycopeptide at positions 161-168 (ATVSSEEK), are conserved in huZP3 derived from transgenic mice.
16401092	9	40	theme	unique	1442:1447	arg1	restriction					1449:1459	This unique restriction	1437:1459	This unique restriction of O-glycan expression	1437:1482	This unique restriction of O-glycan expression suggests that sequence differences in the conserved O-glycosylation domains of mZP3 and huZP3 affect the ability of core 2 N-acetylglucosaminyltransferase(s) to extend the core 1 sequence.
16401092	3	41	theme	O-glycosylation	507:521	arg1	operational					537:547	operational	537:547	operational	537:547	However, recent biophysical analyses confirm that neither site is occupied, implying that an alternate O-glycosylation domain may be operational in native mZP3.
16401092	3	41	theme	O-glycosylation	507:521	arg1	domain					523:528	an alternate O-glycosylation domain	494:528	an alternate O-glycosylation domain	494:528	However, recent biophysical analyses confirm that neither site is occupied, implying that an alternate O-glycosylation domain may be operational in native mZP3.
16401092	1	42	theme	eggs	219:222	arg1	pellucida					145:153	the zona pellucida	136:153	the zona pellucida (mZP)	136:159	Murine sperm initiate fertilization by binding to the zona pellucida (mZP), the specialized extracellular matrix of their homologous eggs.
16401092	1	42	theme	eggs	219:222	arg1	matrix					192:197	the specialized extracellular matrix	162:197	the specialized extracellular matrix of their homologous eggs	162:222	Murine sperm initiate fertilization by binding to the zona pellucida (mZP), the specialized extracellular matrix of their homologous eggs.
16401092	6	43	theme	spaced	1061:1066	arg1	O-glycans					1068:1076	two closely spaced O-glycans	1049:1076	two closely spaced O-glycans that is very well conserved in an evolutionarily related glycoprotein	1049:1146	Thus, there is a specific O-glycosylation domain within native mZP3 expressing two closely spaced O-glycans that is very well conserved in an evolutionarily related glycoprotein.
16401092	2	44	theme	designated	340:349	arg1	mZP3					351:354	the mZP glycoprotein designated mZP3	319:354	the mZP glycoprotein designated mZP3	319:354	O-Glycans occupying two highly conserved vicinal glycosylation sites (Ser-332 and Ser-334) on the mZP glycoprotein designated mZP3 were previously implicated in this interaction.
16401092	4	45	theme	human	571:575	arg1	huZP3					582:586	huZP3	582:586	huZP3	582:586	Since human ZP3 (huZP3) can substitute for mZP3 in rescue mice to mediate sperm binding, the site specificity of O-glycosylation in both native mZP3 and huZP3 was analyzed using ultrasensitive mass spectrometric techniques.
16401092	4	45	theme	human	571:575	arg1	ZP3					577:579	human ZP3	571:579	human ZP3 (huZP3)	571:587	Since human ZP3 (huZP3) can substitute for mZP3 in rescue mice to mediate sperm binding, the site specificity of O-glycosylation in both native mZP3 and huZP3 was analyzed using ultrasensitive mass spectrometric techniques.
16401092	2	46	gly	glycosylation	274:286	arg2	Ser-334					307:313	Ser-334	307:313	Ser-334	307:313	O-Glycans occupying two highly conserved vicinal glycosylation sites (Ser-332 and Ser-334) on the mZP glycoprotein designated mZP3 were previously implicated in this interaction.
16401092	2	46	gly	glycosylation	274:286	arg2	Ser-332					295:301	Ser-332	295:301	Ser-332	295:301	O-Glycans occupying two highly conserved vicinal glycosylation sites (Ser-332 and Ser-334) on the mZP glycoprotein designated mZP3 were previously implicated in this interaction.
16401092	2	46	gly	glycosylation	274:286	arg2	two					245:247	two	245:247	two	245:247	O-Glycans occupying two highly conserved vicinal glycosylation sites (Ser-332 and Ser-334) on the mZP glycoprotein designated mZP3 were previously implicated in this interaction.
16401092	2	46	gly	glycosylation	274:286	arg2	sites					288:292	two highly conserved vicinal glycosylation sites	245:292	two highly conserved vicinal glycosylation sites (Ser-332 and Ser-334) on the mZP glycoprotein designated mZP3	245:354	O-Glycans occupying two highly conserved vicinal glycosylation sites (Ser-332 and Ser-334) on the mZP glycoprotein designated mZP3 were previously implicated in this interaction.
16401092	10	47	theme	rescue	1823:1828	arg1	mice					1830:1833	female huZP3 rescue mice	1810:1833	female huZP3 rescue mice	1810:1833	However, this difference in O-glycosylation at Thr-156 does not affect the fertility or the sperm binding phenotype of eggs derived from female huZP3 rescue mice.
16401092	8	48	from	Thr-155	1305:1311	arg1	mZP3					1316:1319	mZP3	1316:1319	mZP3	1316:1319	However, in huZP3 derived from rescue mice, the O-glycans associated with Thr-156 (analogous to Thr-155 in mZP3) are exclusively core 1 and related Tn sequences, whereas core 2 O-glycans predominate at the other conserved site.
16401092	9	49	theme	core	1600:1603	arg1	N-acetylglucosaminyltransferase					1607:1637	core 2 N-acetylglucosaminyltransferase	1600:1637	core 2 N-acetylglucosaminyltransferase(s)	1600:1640	This unique restriction of O-glycan expression suggests that sequence differences in the conserved O-glycosylation domains of mZP3 and huZP3 affect the ability of core 2 N-acetylglucosaminyltransferase(s) to extend the core 1 sequence.
16401092	9	49	theme	core	1600:1603	arg1	s					1639:1639	s	1639:1639	s	1639:1639	This unique restriction of O-glycan expression suggests that sequence differences in the conserved O-glycosylation domains of mZP3 and huZP3 affect the ability of core 2 N-acetylglucosaminyltransferase(s) to extend the core 1 sequence.
16401092	2	50	theme	vicinal	266:272	arg1	Ser-332					295:301	Ser-332	295:301	Ser-332	295:301	O-Glycans occupying two highly conserved vicinal glycosylation sites (Ser-332 and Ser-334) on the mZP glycoprotein designated mZP3 were previously implicated in this interaction.
16401092	2	50	theme	vicinal	266:272	arg1	sites					288:292	two highly conserved vicinal glycosylation sites	245:292	two highly conserved vicinal glycosylation sites (Ser-332 and Ser-334) on the mZP glycoprotein designated mZP3	245:354	O-Glycans occupying two highly conserved vicinal glycosylation sites (Ser-332 and Ser-334) on the mZP glycoprotein designated mZP3 were previously implicated in this interaction.
16401092	2	50	theme	vicinal	266:272	arg1	Ser-334					307:313	Ser-334	307:313	Ser-334	307:313	O-Glycans occupying two highly conserved vicinal glycosylation sites (Ser-332 and Ser-334) on the mZP glycoprotein designated mZP3 were previously implicated in this interaction.
16401092	8	51	from	core	1338:1341	arg1	huZP3					1221:1225	huZP3	1221:1225	huZP3 derived from rescue mice	1221:1250	However, in huZP3 derived from rescue mice, the O-glycans associated with Thr-156 (analogous to Thr-155 in mZP3) are exclusively core 1 and related Tn sequences, whereas core 2 O-glycans predominate at the other conserved site.
16401092	9	52	theme	N-acetylglucosaminyltransferase	1607:1637	arg1	ability					1589:1595	the ability	1585:1595	the ability of core 2 N-acetylglucosaminyltransferase(s) to extend the core 1 sequence	1585:1670	This unique restriction of O-glycan expression suggests that sequence differences in the conserved O-glycosylation domains of mZP3 and huZP3 affect the ability of core 2 N-acetylglucosaminyltransferase(s) to extend the core 1 sequence.
16401092	6	53	theme	related	1127:1133	arg1	glycoprotein					1135:1146	an evolutionarily related glycoprotein	1109:1146	an evolutionarily related glycoprotein	1109:1146	Thus, there is a specific O-glycosylation domain within native mZP3 expressing two closely spaced O-glycans that is very well conserved in an evolutionarily related glycoprotein.
16401092	10	54	dep	fertility	1748:1756	arg1	the					1744:1746	the	1744:1746	the	1744:1746	However, this difference in O-glycosylation at Thr-156 does not affect the fertility or the sperm binding phenotype of eggs derived from female huZP3 rescue mice.
16401092	4	55	theme	sperm	639:643	arg1	binding					645:651	sperm binding	639:651	sperm binding	639:651	Since human ZP3 (huZP3) can substitute for mZP3 in rescue mice to mediate sperm binding, the site specificity of O-glycosylation in both native mZP3 and huZP3 was analyzed using ultrasensitive mass spectrometric techniques.
16401092	3	56	theme	native	552:557	arg1	mZP3					559:562	native mZP3	552:562	native mZP3	552:562	However, recent biophysical analyses confirm that neither site is occupied, implying that an alternate O-glycosylation domain may be operational in native mZP3.
16401092	1	57	theme	specialized	166:176	arg1	pellucida					145:153	the zona pellucida	136:153	the zona pellucida (mZP)	136:159	Murine sperm initiate fertilization by binding to the zona pellucida (mZP), the specialized extracellular matrix of their homologous eggs.
16401092	1	57	theme	specialized	166:176	arg1	matrix					192:197	the specialized extracellular matrix	162:197	the specialized extracellular matrix of their homologous eggs	162:222	Murine sperm initiate fertilization by binding to the zona pellucida (mZP), the specialized extracellular matrix of their homologous eggs.
16401092	5	58	attach	derived	940:946	arg1	mice					964:967	transgenic mice	953:967	transgenic mice	953:967	Two O-glycosylation sites in native mZP3, one at Thr-155 and the other within the glycopeptide at positions 161-168 (ATVSSEEK), are conserved in huZP3 derived from transgenic mice.
16401092	5	58	attach	derived	940:946	arg2	huZP3					934:938	huZP3	934:938	huZP3 derived from transgenic mice	934:967	Two O-glycosylation sites in native mZP3, one at Thr-155 and the other within the glycopeptide at positions 161-168 (ATVSSEEK), are conserved in huZP3 derived from transgenic mice.
16401092	4	59	from	mZP3	608:611	arg1	mice					623:626	rescue mice	616:626	rescue mice	616:626	Since human ZP3 (huZP3) can substitute for mZP3 in rescue mice to mediate sperm binding, the site specificity of O-glycosylation in both native mZP3 and huZP3 was analyzed using ultrasensitive mass spectrometric techniques.
16401092	4	60	theme	rescue	616:621	arg1	mice					623:626	rescue mice	616:626	rescue mice	616:626	Since human ZP3 (huZP3) can substitute for mZP3 in rescue mice to mediate sperm binding, the site specificity of O-glycosylation in both native mZP3 and huZP3 was analyzed using ultrasensitive mass spectrometric techniques.
16401092	4	61	theme	spectrometric	763:775	arg1	techniques					777:786	ultrasensitive mass spectrometric techniques	743:786	ultrasensitive mass spectrometric techniques	743:786	Since human ZP3 (huZP3) can substitute for mZP3 in rescue mice to mediate sperm binding, the site specificity of O-glycosylation in both native mZP3 and huZP3 was analyzed using ultrasensitive mass spectrometric techniques.
16401092	10	62	theme	sperm	1765:1769	arg1	phenotype					1779:1787	the sperm binding phenotype	1761:1787	the sperm binding phenotype	1761:1787	However, this difference in O-glycosylation at Thr-156 does not affect the fertility or the sperm binding phenotype of eggs derived from female huZP3 rescue mice.
16401092	10	63	attach	derived	1797:1803	arg2	eggs					1792:1795	eggs	1792:1795	eggs derived from female huZP3 rescue mice	1792:1833	However, this difference in O-glycosylation at Thr-156 does not affect the fertility or the sperm binding phenotype of eggs derived from female huZP3 rescue mice.
16401092	10	63	attach	derived	1797:1803	arg1	mice					1830:1833	female huZP3 rescue mice	1810:1833	female huZP3 rescue mice	1810:1833	However, this difference in O-glycosylation at Thr-156 does not affect the fertility or the sperm binding phenotype of eggs derived from female huZP3 rescue mice.
16401092	5	64	theme	native	818:823	arg1	mZP3					825:828	native mZP3	818:828	native mZP3	818:828	Two O-glycosylation sites in native mZP3, one at Thr-155 and the other within the glycopeptide at positions 161-168 (ATVSSEEK), are conserved in huZP3 derived from transgenic mice.
16401092	9	65	from	differences	1507:1517	arg1	domains					1552:1558	the conserved O-glycosylation domains	1522:1558	the conserved O-glycosylation domains of mZP3 and huZP3	1522:1576	This unique restriction of O-glycan expression suggests that sequence differences in the conserved O-glycosylation domains of mZP3 and huZP3 affect the ability of core 2 N-acetylglucosaminyltransferase(s) to extend the core 1 sequence.
16401092	9	65	from	differences	1507:1517	arg1	huZP3					1572:1576	huZP3	1572:1576	huZP3	1572:1576	This unique restriction of O-glycan expression suggests that sequence differences in the conserved O-glycosylation domains of mZP3 and huZP3 affect the ability of core 2 N-acetylglucosaminyltransferase(s) to extend the core 1 sequence.
16401092	9	65	from	differences	1507:1517	arg1	mZP3					1563:1566	mZP3	1563:1566	mZP3	1563:1566	This unique restriction of O-glycan expression suggests that sequence differences in the conserved O-glycosylation domains of mZP3 and huZP3 affect the ability of core 2 N-acetylglucosaminyltransferase(s) to extend the core 1 sequence.
16401092	8	66	theme	conserved	1421:1429	arg1	site					1431:1434	the other conserved site	1411:1434	the other conserved site	1411:1434	However, in huZP3 derived from rescue mice, the O-glycans associated with Thr-156 (analogous to Thr-155 in mZP3) are exclusively core 1 and related Tn sequences, whereas core 2 O-glycans predominate at the other conserved site.
16401092	5	67	from	Thr-155	838:844	arg1	one					831:833	one	831:833	one	831:833	Two O-glycosylation sites in native mZP3, one at Thr-155 and the other within the glycopeptide at positions 161-168 (ATVSSEEK), are conserved in huZP3 derived from transgenic mice.
16401092	5	67	from	Thr-155	838:844	arg1	sites					809:813	Two O-glycosylation sites	789:813	Two O-glycosylation sites in native mZP3	789:828	Two O-glycosylation sites in native mZP3, one at Thr-155 and the other within the glycopeptide at positions 161-168 (ATVSSEEK), are conserved in huZP3 derived from transgenic mice.
16401092	4	68	theme	site	658:661	arg1	specificity					663:673	the site specificity	654:673	the site specificity of O-glycosylation in both native mZP3 and huZP3	654:722	Since human ZP3 (huZP3) can substitute for mZP3 in rescue mice to mediate sperm binding, the site specificity of O-glycosylation in both native mZP3 and huZP3 was analyzed using ultrasensitive mass spectrometric techniques.
16401092	3	69	from	operational	537:547	arg1	mZP3					559:562	native mZP3	552:562	native mZP3	552:562	However, recent biophysical analyses confirm that neither site is occupied, implying that an alternate O-glycosylation domain may be operational in native mZP3.
16401092	9	70	theme	O-glycan	1464:1471	arg1	expression					1473:1482	O-glycan expression	1464:1482	O-glycan expression	1464:1482	This unique restriction of O-glycan expression suggests that sequence differences in the conserved O-glycosylation domains of mZP3 and huZP3 affect the ability of core 2 N-acetylglucosaminyltransferase(s) to extend the core 1 sequence.
16401092	7	71	theme	native	1152:1157	arg1	mZP3					1159:1162	native mZP3	1152:1162	native mZP3	1152:1162	In native mZP3, core 2 O-glycans predominate at both sites.
16401092	8	72	theme	analogous	1292:1300	arg1	Thr-156					1283:1289	Thr-156	1283:1289	Thr-156 (analogous to Thr-155 in mZP3)	1283:1320	However, in huZP3 derived from rescue mice, the O-glycans associated with Thr-156 (analogous to Thr-155 in mZP3) are exclusively core 1 and related Tn sequences, whereas core 2 O-glycans predominate at the other conserved site.
16401092	9	73	theme	sequence	1498:1505	arg1	differences					1507:1517	sequence differences	1498:1517	sequence differences in the conserved O-glycosylation domains of mZP3 and huZP3	1498:1576	This unique restriction of O-glycan expression suggests that sequence differences in the conserved O-glycosylation domains of mZP3 and huZP3 affect the ability of core 2 N-acetylglucosaminyltransferase(s) to extend the core 1 sequence.
16401092	6	74	theme	native	1026:1031	arg1	mZP3					1033:1036	native mZP3	1026:1036	native mZP3 expressing two closely spaced O-glycans that is very well conserved in an evolutionarily related glycoprotein	1026:1146	Thus, there is a specific O-glycosylation domain within native mZP3 expressing two closely spaced O-glycans that is very well conserved in an evolutionarily related glycoprotein.
16401092	4	75	theme	native	702:707	arg1	mZP3					709:712	native mZP3	702:712	native mZP3	702:712	Since human ZP3 (huZP3) can substitute for mZP3 in rescue mice to mediate sperm binding, the site specificity of O-glycosylation in both native mZP3 and huZP3 was analyzed using ultrasensitive mass spectrometric techniques.
16401092	3	76	theme	biophysical	420:430	arg1	analyses					432:439	recent biophysical analyses	413:439	recent biophysical analyses	413:439	However, recent biophysical analyses confirm that neither site is occupied, implying that an alternate O-glycosylation domain may be operational in native mZP3.
16401092	5	77	theme	O-glycosylation	793:807	arg1	other					854:858	other	854:858	other	854:858	Two O-glycosylation sites in native mZP3, one at Thr-155 and the other within the glycopeptide at positions 161-168 (ATVSSEEK), are conserved in huZP3 derived from transgenic mice.
16401092	5	77	theme	O-glycosylation	793:807	arg1	one					831:833	one	831:833	one	831:833	Two O-glycosylation sites in native mZP3, one at Thr-155 and the other within the glycopeptide at positions 161-168 (ATVSSEEK), are conserved in huZP3 derived from transgenic mice.
16401092	5	77	theme	O-glycosylation	793:807	arg1	sites					809:813	Two O-glycosylation sites	789:813	Two O-glycosylation sites in native mZP3	789:828	Two O-glycosylation sites in native mZP3, one at Thr-155 and the other within the glycopeptide at positions 161-168 (ATVSSEEK), are conserved in huZP3 derived from transgenic mice.
16401092	5	78	from	positions	887:895	arg1	other					854:858	other	854:858	other	854:858	Two O-glycosylation sites in native mZP3, one at Thr-155 and the other within the glycopeptide at positions 161-168 (ATVSSEEK), are conserved in huZP3 derived from transgenic mice.
16401092	5	78	from	positions	887:895	arg1	sites					809:813	Two O-glycosylation sites	789:813	Two O-glycosylation sites in native mZP3	789:828	Two O-glycosylation sites in native mZP3, one at Thr-155 and the other within the glycopeptide at positions 161-168 (ATVSSEEK), are conserved in huZP3 derived from transgenic mice.
16401092	10	79	theme	eggs	1792:1795	arg1	phenotype					1779:1787	the sperm binding phenotype	1761:1787	the sperm binding phenotype	1761:1787	However, this difference in O-glycosylation at Thr-156 does not affect the fertility or the sperm binding phenotype of eggs derived from female huZP3 rescue mice.
16401092	10	79	theme	eggs	1792:1795	arg1	fertility					1748:1756	fertility	1748:1756	fertility	1748:1756	However, this difference in O-glycosylation at Thr-156 does not affect the fertility or the sperm binding phenotype of eggs derived from female huZP3 rescue mice.
16401092	0	80	theme	domain	44:49	arg1	O-glycosylation					13:27	Differential O-glycosylation	0:27	Differential O-glycosylation of a conserved domain	0:49	Differential O-glycosylation of a conserved domain expressed in murine and human ZP3.
16401092	10	81	gly	O-glycosylation	1701:1715	arg2	Thr-156					1720:1726	Thr-156	1720:1726	Thr-156	1720:1726	However, this difference in O-glycosylation at Thr-156 does not affect the fertility or the sperm binding phenotype of eggs derived from female huZP3 rescue mice.
16401092	10	81	gly	O-glycosylation	1701:1715	arg1	Thr-156					1720:1726	Thr-156	1720:1726	Thr-156	1720:1726	However, this difference in O-glycosylation at Thr-156 does not affect the fertility or the sperm binding phenotype of eggs derived from female huZP3 rescue mice.
16401092	9	82	theme	conserved	1526:1534	arg1	domains					1552:1558	the conserved O-glycosylation domains	1522:1558	the conserved O-glycosylation domains of mZP3 and huZP3	1522:1576	This unique restriction of O-glycan expression suggests that sequence differences in the conserved O-glycosylation domains of mZP3 and huZP3 affect the ability of core 2 N-acetylglucosaminyltransferase(s) to extend the core 1 sequence.
16401092	9	82	theme	conserved	1526:1534	arg1	huZP3					1572:1576	huZP3	1572:1576	huZP3	1572:1576	This unique restriction of O-glycan expression suggests that sequence differences in the conserved O-glycosylation domains of mZP3 and huZP3 affect the ability of core 2 N-acetylglucosaminyltransferase(s) to extend the core 1 sequence.
16401092	9	82	theme	conserved	1526:1534	arg1	mZP3					1563:1566	mZP3	1563:1566	mZP3	1563:1566	This unique restriction of O-glycan expression suggests that sequence differences in the conserved O-glycosylation domains of mZP3 and huZP3 affect the ability of core 2 N-acetylglucosaminyltransferase(s) to extend the core 1 sequence.
16401092	6	83	theme	specific	987:994	arg1	domain					1012:1017	a specific O-glycosylation domain	985:1017	a specific O-glycosylation domain within native mZP3 expressing two closely spaced O-glycans that is very well conserved in an evolutionarily related glycoprotein	985:1146	Thus, there is a specific O-glycosylation domain within native mZP3 expressing two closely spaced O-glycans that is very well conserved in an evolutionarily related glycoprotein.
16401092	3	84	used	occupied	470:477	arg2	site					462:465	neither site	454:465	neither site	454:465	However, recent biophysical analyses confirm that neither site is occupied, implying that an alternate O-glycosylation domain may be operational in native mZP3.
16401092	10	85	theme	huZP3	1817:1821	arg1	mice					1830:1833	female huZP3 rescue mice	1810:1833	female huZP3 rescue mice	1810:1833	However, this difference in O-glycosylation at Thr-156 does not affect the fertility or the sperm binding phenotype of eggs derived from female huZP3 rescue mice.
16401092	1	86	theme	zona	140:143	arg1	matrix					192:197	the specialized extracellular matrix	162:197	the specialized extracellular matrix of their homologous eggs	162:222	Murine sperm initiate fertilization by binding to the zona pellucida (mZP), the specialized extracellular matrix of their homologous eggs.
16401092	1	86	theme	zona	140:143	arg1	mZP					156:158	mZP	156:158	mZP	156:158	Murine sperm initiate fertilization by binding to the zona pellucida (mZP), the specialized extracellular matrix of their homologous eggs.
16401092	1	86	theme	zona	140:143	arg1	pellucida					145:153	the zona pellucida	136:153	the zona pellucida (mZP)	136:159	Murine sperm initiate fertilization by binding to the zona pellucida (mZP), the specialized extracellular matrix of their homologous eggs.
16401092	9	87	theme	mZP3	1563:1566	arg1	domains					1552:1558	the conserved O-glycosylation domains	1522:1558	the conserved O-glycosylation domains of mZP3 and huZP3	1522:1576	This unique restriction of O-glycan expression suggests that sequence differences in the conserved O-glycosylation domains of mZP3 and huZP3 affect the ability of core 2 N-acetylglucosaminyltransferase(s) to extend the core 1 sequence.
16401092	9	87	theme	mZP3	1563:1566	arg1	huZP3					1572:1576	huZP3	1572:1576	huZP3	1572:1576	This unique restriction of O-glycan expression suggests that sequence differences in the conserved O-glycosylation domains of mZP3 and huZP3 affect the ability of core 2 N-acetylglucosaminyltransferase(s) to extend the core 1 sequence.
16401092	9	87	theme	mZP3	1563:1566	arg1	mZP3					1563:1566	mZP3	1563:1566	mZP3	1563:1566	This unique restriction of O-glycan expression suggests that sequence differences in the conserved O-glycosylation domains of mZP3 and huZP3 affect the ability of core 2 N-acetylglucosaminyltransferase(s) to extend the core 1 sequence.
16401092	5	88	dep	positions	887:895	arg1	ATVSSEEK					906:913	ATVSSEEK	906:913	ATVSSEEK	906:913	Two O-glycosylation sites in native mZP3, one at Thr-155 and the other within the glycopeptide at positions 161-168 (ATVSSEEK), are conserved in huZP3 derived from transgenic mice.
16401092	5	88	dep	positions	887:895	arg1	161-168					897:903	161-168	897:903	161-168	897:903	Two O-glycosylation sites in native mZP3, one at Thr-155 and the other within the glycopeptide at positions 161-168 (ATVSSEEK), are conserved in huZP3 derived from transgenic mice.
16401092	4	89	theme	mass	758:761	arg1	techniques					777:786	ultrasensitive mass spectrometric techniques	743:786	ultrasensitive mass spectrometric techniques	743:786	Since human ZP3 (huZP3) can substitute for mZP3 in rescue mice to mediate sperm binding, the site specificity of O-glycosylation in both native mZP3 and huZP3 was analyzed using ultrasensitive mass spectrometric techniques.
16401092	1	90	theme	homologous	208:217	arg1	eggs					219:222	their homologous eggs	202:222	their homologous eggs	202:222	Murine sperm initiate fertilization by binding to the zona pellucida (mZP), the specialized extracellular matrix of their homologous eggs.
16401092	9	91	theme	huZP3	1572:1576	arg1	domains					1552:1558	the conserved O-glycosylation domains	1522:1558	the conserved O-glycosylation domains of mZP3 and huZP3	1522:1576	This unique restriction of O-glycan expression suggests that sequence differences in the conserved O-glycosylation domains of mZP3 and huZP3 affect the ability of core 2 N-acetylglucosaminyltransferase(s) to extend the core 1 sequence.
16401092	9	91	theme	huZP3	1572:1576	arg1	huZP3					1572:1576	huZP3	1572:1576	huZP3	1572:1576	This unique restriction of O-glycan expression suggests that sequence differences in the conserved O-glycosylation domains of mZP3 and huZP3 affect the ability of core 2 N-acetylglucosaminyltransferase(s) to extend the core 1 sequence.
16401092	9	91	theme	huZP3	1572:1576	arg1	mZP3					1563:1566	mZP3	1563:1566	mZP3	1563:1566	This unique restriction of O-glycan expression suggests that sequence differences in the conserved O-glycosylation domains of mZP3 and huZP3 affect the ability of core 2 N-acetylglucosaminyltransferase(s) to extend the core 1 sequence.
16401092	8	92	theme	Tn	1357:1358	arg1	sequences					1360:1368	related Tn sequences	1349:1368	related Tn sequences	1349:1368	However, in huZP3 derived from rescue mice, the O-glycans associated with Thr-156 (analogous to Thr-155 in mZP3) are exclusively core 1 and related Tn sequences, whereas core 2 O-glycans predominate at the other conserved site.
16401092	4	93	from	specificity	663:673	arg1	huZP3					718:722	huZP3	718:722	huZP3	718:722	Since human ZP3 (huZP3) can substitute for mZP3 in rescue mice to mediate sperm binding, the site specificity of O-glycosylation in both native mZP3 and huZP3 was analyzed using ultrasensitive mass spectrometric techniques.
16401092	4	93	from	specificity	663:673	arg1	mZP3					709:712	native mZP3	702:712	native mZP3	702:712	Since human ZP3 (huZP3) can substitute for mZP3 in rescue mice to mediate sperm binding, the site specificity of O-glycosylation in both native mZP3 and huZP3 was analyzed using ultrasensitive mass spectrometric techniques.
23001782	9	0	theme	charge	1601:1606	arg1	heterogeneity					1608:1620	charge heterogeneity	1601:1620	charge heterogeneity	1601:1620	Electrophoretic analysis of intact hSHBG revealed size and charge heterogeneity of the isoforms circulating in blood serum.
23001782	2	1	theme	hSHBG	343:347	arg1	action					333:338	action	333:338	action of hSHBG	333:347	Several molecular mechanisms of action of hSHBG, including the function of its attached glycans remain unknown.
23001782	1	2	theme	targeted	237:244	arg1	delivery					246:253	targeted delivery	237:253	targeted delivery	237:253	Human sex hormone binding globulin (hSHBG) is a serum glycoprotein central to the transport and targeted delivery of sex hormones to steroid-sensitive tissues.
23001782	9	3	theme	isoforms	1629:1636	arg1	size					1592:1595	size	1592:1595	size	1592:1595	Electrophoretic analysis of intact hSHBG revealed size and charge heterogeneity of the isoforms circulating in blood serum.
23001782	9	3	theme	isoforms	1629:1636	arg1	heterogeneity					1608:1620	charge heterogeneity	1601:1620	charge heterogeneity	1601:1620	Electrophoretic analysis of intact hSHBG revealed size and charge heterogeneity of the isoforms circulating in blood serum.
23001782	6	4	used	occupied	999:1006	arg2	sites					989:993	Both sites	984:993	Both sites	984:993	Both sites are occupied by the same six sialylated and partly core fucosylated bi- and triantennary N-Glycoforms with lactosamine-type antennas of the form (±NeuAcα6)Galβ4GlcNAc.
23001782	4	5	from	sites	684:688	arg1	hSHBG					832:836	intact hSHBG	825:836	intact hSHBG	825:836	MS-driven glycoproteomics and glycomics combined with exoglycosidase treatment were used in a bottom-up and top-down manner to determine glycosylation sites, site-specific occupancies and monosaccharide compositions, detailed glycan structures, and the higher level arrangement of glycans on intact hSHBG.
23001782	5	6	gly	N-glycosylated	880:893	arg2	351					902:904	351	902:904	351	902:904	It was found that serum-derived hSHBG is N-glycosylated at Asn(351) and Asn(367) with average molar occupancies of 85.1 and 95.3%, respectively.
23001782	5	6	gly	N-glycosylated	880:893	arg2	367					915:917	367	915:917	367	915:917	It was found that serum-derived hSHBG is N-glycosylated at Asn(351) and Asn(367) with average molar occupancies of 85.1 and 95.3%, respectively.
23001782	5	6	gly	N-glycosylated	880:893	arg2	Asn					898:900	Asn	898:900	Asn(351)	898:905	It was found that serum-derived hSHBG is N-glycosylated at Asn(351) and Asn(367) with average molar occupancies of 85.1 and 95.3%, respectively.
23001782	5	6	gly	N-glycosylated	880:893	arg1	hSHBG					871:875	serum-derived hSHBG	857:875	serum-derived hSHBG	857:875	It was found that serum-derived hSHBG is N-glycosylated at Asn(351) and Asn(367) with average molar occupancies of 85.1 and 95.3%, respectively.
23001782	5	6	gly	N-glycosylated	880:893	arg2	Asn					911:913	Asn	911:913	Asn(367)	911:918	It was found that serum-derived hSHBG is N-glycosylated at Asn(351) and Asn(367) with average molar occupancies of 85.1 and 95.3%, respectively.
23001782	4	7	theme	site-specific	691:703	arg1	occupancies					705:715	site-specific occupancies	691:715	site-specific occupancies	691:715	MS-driven glycoproteomics and glycomics combined with exoglycosidase treatment were used in a bottom-up and top-down manner to determine glycosylation sites, site-specific occupancies and monosaccharide compositions, detailed glycan structures, and the higher level arrangement of glycans on intact hSHBG.
23001782	2	8	theme	Several	301:307	arg1	mechanisms					319:328	Several molecular mechanisms	301:328	Several molecular mechanisms	301:328	Several molecular mechanisms of action of hSHBG, including the function of its attached glycans remain unknown.
23001782	2	8	theme	Several	301:307	arg1	function					364:371	the function	360:371	the function of its attached glycans	360:395	Several molecular mechanisms of action of hSHBG, including the function of its attached glycans remain unknown.
23001782	8	9	theme	N-terminal	1327:1336	arg1	7					1342:1342	7	1342:1342	7	1342:1342	The N-terminal Thr(7) was fully occupied by the two O-linked glycans NeuAcα3Galβ3(NeuAcα6)GalNAc (where NeuAc is N-acetylneuraminic acid and GalNAc is N-acetylgalactosamine) and NeuAcα3Galβ3GalNAc in a 1:6 molar ratio.
23001782	8	9	theme	N-terminal	1327:1336	arg1	Thr					1338:1340	The N-terminal Thr	1323:1340	The N-terminal Thr(7)	1323:1343	The N-terminal Thr(7) was fully occupied by the two O-linked glycans NeuAcα3Galβ3(NeuAcα6)GalNAc (where NeuAc is N-acetylneuraminic acid and GalNAc is N-acetylgalactosamine) and NeuAcα3Galβ3GalNAc in a 1:6 molar ratio.
23001782	3	10	link	O-linked	486:493	arg1	glycosylation					495:507	the N- and O-linked glycosylation	475:507	the N- and O-linked glycosylation of serum-derived hSHBG	475:530	Here, we perform a detailed site-specific characterization of the N- and O-linked glycosylation of serum-derived hSHBG.
23001782	0	11	theme	circulating	119:129	arg1	globulin					110:117	human sex hormone binding globulin circulating	84:129	human sex hormone binding globulin circulating in serum	84:138	Micro- and macroheterogeneity of N-glycosylation yields size and charge isoforms of human sex hormone binding globulin circulating in serum.
23001782	3	12	theme	glycosylation	495:507	arg1	characterization					455:470	a detailed site-specific characterization	430:470	a detailed site-specific characterization of the N- and O-linked glycosylation of serum-derived hSHBG	430:530	Here, we perform a detailed site-specific characterization of the N- and O-linked glycosylation of serum-derived hSHBG.
23001782	11	13	theme	functional	2013:2022	arg1	aspects					2024:2030	the functional aspects	2009:2030	the functional aspects of the hSHBG glycans	2009:2051	To date, this work represents the most detailed structural map of the heterogeneous hSHBG glycosylation, which is a prerequisite for investigating the functional aspects of the hSHBG glycans.
23001782	1	14	dep	transport	223:231	arg1	the					219:221	the	219:221	the	219:221	Human sex hormone binding globulin (hSHBG) is a serum glycoprotein central to the transport and targeted delivery of sex hormones to steroid-sensitive tissues.
23001782	8	15	from	glycans	1384:1390	arg1	ratio					1535:1539	a 1:6 molar ratio	1523:1539	a 1:6 molar ratio	1523:1539	The N-terminal Thr(7) was fully occupied by the two O-linked glycans NeuAcα3Galβ3(NeuAcα6)GalNAc (where NeuAc is N-acetylneuraminic acid and GalNAc is N-acetylgalactosamine) and NeuAcα3Galβ3GalNAc in a 1:6 molar ratio.
23001782	4	16	theme	detailed	750:757	arg1	structures					766:775	detailed glycan structures	750:775	detailed glycan structures	750:775	MS-driven glycoproteomics and glycomics combined with exoglycosidase treatment were used in a bottom-up and top-down manner to determine glycosylation sites, site-specific occupancies and monosaccharide compositions, detailed glycan structures, and the higher level arrangement of glycans on intact hSHBG.
23001782	4	17	used	used	617:620	arg2	glycomics					563:571	glycomics	563:571	glycomics	563:571	MS-driven glycoproteomics and glycomics combined with exoglycosidase treatment were used in a bottom-up and top-down manner to determine glycosylation sites, site-specific occupancies and monosaccharide compositions, detailed glycan structures, and the higher level arrangement of glycans on intact hSHBG.
23001782	4	17	used	used	617:620	arg2	glycoproteomics					543:557	MS-driven glycoproteomics	533:557	MS-driven glycoproteomics	533:557	MS-driven glycoproteomics and glycomics combined with exoglycosidase treatment were used in a bottom-up and top-down manner to determine glycosylation sites, site-specific occupancies and monosaccharide compositions, detailed glycan structures, and the higher level arrangement of glycans on intact hSHBG.
23001782	10	18	theme	Asn	1771:1773	arg1	occupancies					1787:1797	differential Asn(351) glycan occupancies	1758:1797	differential Asn(351) glycan occupancies	1758:1797	Interestingly, the size and charge heterogeneity were shown to originate predominantly from differential Asn(351) glycan occupancies and N-glycan sialylation that may modulate the hSHBG activity.
23001782	11	19	theme	hSHBG	2039:2043	arg1	glycans					2045:2051	the hSHBG glycans	2035:2051	the hSHBG glycans	2035:2051	To date, this work represents the most detailed structural map of the heterogeneous hSHBG glycosylation, which is a prerequisite for investigating the functional aspects of the hSHBG glycans.
23001782	11	20	theme	hSHBG	1946:1950	arg1	prerequisite					1978:1989	a prerequisite	1976:1989	a prerequisite for investigating the functional aspects of the hSHBG glycans	1976:2051	To date, this work represents the most detailed structural map of the heterogeneous hSHBG glycosylation, which is a prerequisite for investigating the functional aspects of the hSHBG glycans.
23001782	11	20	theme	hSHBG	1946:1950	arg1	glycosylation					1952:1964	the heterogeneous hSHBG glycosylation	1928:1964	the heterogeneous hSHBG glycosylation	1928:1964	To date, this work represents the most detailed structural map of the heterogeneous hSHBG glycosylation, which is a prerequisite for investigating the functional aspects of the hSHBG glycans.
23001782	6	21	dep	bi-	1063:1065	arg1	N-Glycoforms					1084:1095	N-Glycoforms	1084:1095	N-Glycoforms	1084:1095	Both sites are occupied by the same six sialylated and partly core fucosylated bi- and triantennary N-Glycoforms with lactosamine-type antennas of the form (±NeuAcα6)Galβ4GlcNAc.
23001782	11	22	theme	glycosylation	1952:1964	arg1	map					1921:1923	the most detailed structural map	1892:1923	the most detailed structural map of the heterogeneous hSHBG glycosylation, which is a prerequisite for investigating the functional aspects of the hSHBG glycans	1892:2051	To date, this work represents the most detailed structural map of the heterogeneous hSHBG glycosylation, which is a prerequisite for investigating the functional aspects of the hSHBG glycans.
23001782	5	23	theme	average	925:931	arg1	occupancies					939:949	average molar occupancies	925:949	average molar occupancies of 85.1 and 95.3%, respectively	925:981	It was found that serum-derived hSHBG is N-glycosylated at Asn(351) and Asn(367) with average molar occupancies of 85.1 and 95.3%, respectively.
23001782	0	24	theme	charge	65:70	arg1	isoforms					72:79	size and charge isoforms	56:79	size and charge isoforms of human sex hormone binding globulin circulating in serum	56:138	Micro- and macroheterogeneity of N-glycosylation yields size and charge isoforms of human sex hormone binding globulin circulating in serum.
23001782	10	25	theme	glycan	1780:1785	arg1	occupancies					1787:1797	differential Asn(351) glycan occupancies	1758:1797	differential Asn(351) glycan occupancies	1758:1797	Interestingly, the size and charge heterogeneity were shown to originate predominantly from differential Asn(351) glycan occupancies and N-glycan sialylation that may modulate the hSHBG activity.
23001782	1	26	theme	sex	147:149	arg1	hSHBG					177:181	hSHBG	177:181	hSHBG	177:181	Human sex hormone binding globulin (hSHBG) is a serum glycoprotein central to the transport and targeted delivery of sex hormones to steroid-sensitive tissues.
23001782	1	26	theme	sex	147:149	arg1	globulin					167:174	Human sex hormone binding globulin	141:174	Human sex hormone binding globulin (hSHBG)	141:182	Human sex hormone binding globulin (hSHBG) is a serum glycoprotein central to the transport and targeted delivery of sex hormones to steroid-sensitive tissues.
23001782	1	26	theme	sex	147:149	arg1	glycoprotein					195:206	a serum glycoprotein	187:206	a serum glycoprotein central to the transport and targeted delivery of sex hormones to steroid-sensitive tissues	187:298	Human sex hormone binding globulin (hSHBG) is a serum glycoprotein central to the transport and targeted delivery of sex hormones to steroid-sensitive tissues.
23001782	11	27	theme	glycans	2045:2051	arg1	aspects					2024:2030	the functional aspects	2009:2030	the functional aspects of the hSHBG glycans	2009:2051	To date, this work represents the most detailed structural map of the heterogeneous hSHBG glycosylation, which is a prerequisite for investigating the functional aspects of the hSHBG glycans.
23001782	4	28	from	glycans	814:820	arg1	hSHBG					832:836	intact hSHBG	825:836	intact hSHBG	825:836	MS-driven glycoproteomics and glycomics combined with exoglycosidase treatment were used in a bottom-up and top-down manner to determine glycosylation sites, site-specific occupancies and monosaccharide compositions, detailed glycan structures, and the higher level arrangement of glycans on intact hSHBG.
23001782	1	29	theme	binding	159:165	arg1	hSHBG					177:181	hSHBG	177:181	hSHBG	177:181	Human sex hormone binding globulin (hSHBG) is a serum glycoprotein central to the transport and targeted delivery of sex hormones to steroid-sensitive tissues.
23001782	1	29	theme	binding	159:165	arg1	globulin					167:174	Human sex hormone binding globulin	141:174	Human sex hormone binding globulin (hSHBG)	141:182	Human sex hormone binding globulin (hSHBG) is a serum glycoprotein central to the transport and targeted delivery of sex hormones to steroid-sensitive tissues.
23001782	1	29	theme	binding	159:165	arg1	glycoprotein					195:206	a serum glycoprotein	187:206	a serum glycoprotein central to the transport and targeted delivery of sex hormones to steroid-sensitive tissues	187:298	Human sex hormone binding globulin (hSHBG) is a serum glycoprotein central to the transport and targeted delivery of sex hormones to steroid-sensitive tissues.
23001782	8	30	link	O-linked	1375:1382	arg1	NeuAcα6					1405:1411	NeuAcα6	1405:1411	NeuAcα6	1405:1411	The N-terminal Thr(7) was fully occupied by the two O-linked glycans NeuAcα3Galβ3(NeuAcα6)GalNAc (where NeuAc is N-acetylneuraminic acid and GalNAc is N-acetylgalactosamine) and NeuAcα3Galβ3GalNAc in a 1:6 molar ratio.
23001782	8	30	link	O-linked	1375:1382	arg1	NeuAcα3Galβ3GalNAc					1501:1518	NeuAcα3Galβ3GalNAc	1501:1518	NeuAcα3Galβ3GalNAc	1501:1518	The N-terminal Thr(7) was fully occupied by the two O-linked glycans NeuAcα3Galβ3(NeuAcα6)GalNAc (where NeuAc is N-acetylneuraminic acid and GalNAc is N-acetylgalactosamine) and NeuAcα3Galβ3GalNAc in a 1:6 molar ratio.
23001782	8	30	link	O-linked	1375:1382	arg1	glycans					1384:1390	the two O-linked glycans NeuAcα3Galβ3(NeuAcα6)GalNAc (where NeuAc is N-acetylneuraminic acid and GalNAc is N-acetylgalactosamine) and NeuAcα3Galβ3GalNAc	1367:1518	the two O-linked glycans NeuAcα3Galβ3(NeuAcα6)GalNAc (where NeuAc is N-acetylneuraminic acid and GalNAc is N-acetylgalactosamine) and NeuAcα3Galβ3GalNAc in a 1:6 molar ratio	1367:1539	The N-terminal Thr(7) was fully occupied by the two O-linked glycans NeuAcα3Galβ3(NeuAcα6)GalNAc (where NeuAc is N-acetylneuraminic acid and GalNAc is N-acetylgalactosamine) and NeuAcα3Galβ3GalNAc in a 1:6 molar ratio.
23001782	5	31	gly	occupancies	939:949	arg2	%					967:967	85.1 and 95.3%	954:967	%	967:967	It was found that serum-derived hSHBG is N-glycosylated at Asn(351) and Asn(367) with average molar occupancies of 85.1 and 95.3%, respectively.
23001782	0	32	theme	sex	90:92	arg1	globulin					110:117	human sex hormone binding globulin circulating	84:129	human sex hormone binding globulin circulating in serum	84:138	Micro- and macroheterogeneity of N-glycosylation yields size and charge isoforms of human sex hormone binding globulin circulating in serum.
23001782	7	33	gly	N-glycoforms	1251:1262	arg1	Asn					1242:1244	Asn(351) N-glycoforms	1242:1262	Asn(351) N-glycoforms	1242:1262	N-Glycoforms of Asn(367) were slightly more branched and core fucosylated than Asn(351) N-glycoforms due probably to a more surface-exposed glycosylation site.
23001782	4	34	from	arrangement	799:809	arg1	hSHBG					832:836	intact hSHBG	825:836	intact hSHBG	825:836	MS-driven glycoproteomics and glycomics combined with exoglycosidase treatment were used in a bottom-up and top-down manner to determine glycosylation sites, site-specific occupancies and monosaccharide compositions, detailed glycan structures, and the higher level arrangement of glycans on intact hSHBG.
23001782	5	35	theme	95.3	963:966	arg1	%					967:967	85.1 and 95.3%	954:967	%	967:967	It was found that serum-derived hSHBG is N-glycosylated at Asn(351) and Asn(367) with average molar occupancies of 85.1 and 95.3%, respectively.
23001782	3	36	gly	glycosylation	495:507	arg1	hSHBG					526:530	serum-derived hSHBG	512:530	serum-derived hSHBG	512:530	Here, we perform a detailed site-specific characterization of the N- and O-linked glycosylation of serum-derived hSHBG.
23001782	2	37	theme	attached	380:387	arg1	glycans					389:395	its attached glycans	376:395	its attached glycans	376:395	Several molecular mechanisms of action of hSHBG, including the function of its attached glycans remain unknown.
23001782	0	38	theme	binding	102:108	arg1	globulin					110:117	human sex hormone binding globulin circulating	84:129	human sex hormone binding globulin circulating in serum	84:138	Micro- and macroheterogeneity of N-glycosylation yields size and charge isoforms of human sex hormone binding globulin circulating in serum.
23001782	6	39	theme	fucosylated	1051:1061	arg1	bi-					1063:1065	the same six sialylated and partly core fucosylated bi-	1011:1065	the same six sialylated and partly core fucosylated bi-	1011:1065	Both sites are occupied by the same six sialylated and partly core fucosylated bi- and triantennary N-Glycoforms with lactosamine-type antennas of the form (±NeuAcα6)Galβ4GlcNAc.
23001782	1	40	theme	sex	258:260	arg1	hormones					262:269	sex hormones	258:269	sex hormones	258:269	Human sex hormone binding globulin (hSHBG) is a serum glycoprotein central to the transport and targeted delivery of sex hormones to steroid-sensitive tissues.
23001782	6	41	gly	sialylated	1024:1033	arg1	bi-					1063:1065	the same six sialylated and partly core fucosylated bi-	1011:1065	the same six sialylated and partly core fucosylated bi-	1011:1065	Both sites are occupied by the same six sialylated and partly core fucosylated bi- and triantennary N-Glycoforms with lactosamine-type antennas of the form (±NeuAcα6)Galβ4GlcNAc.
23001782	4	42	theme	higher	786:791	arg1	arrangement					799:809	the higher level arrangement	782:809	the higher level arrangement of glycans on intact hSHBG	782:836	MS-driven glycoproteomics and glycomics combined with exoglycosidase treatment were used in a bottom-up and top-down manner to determine glycosylation sites, site-specific occupancies and monosaccharide compositions, detailed glycan structures, and the higher level arrangement of glycans on intact hSHBG.
23001782	3	43	theme	site-specific	441:453	arg1	characterization					455:470	a detailed site-specific characterization	430:470	a detailed site-specific characterization of the N- and O-linked glycosylation of serum-derived hSHBG	430:530	Here, we perform a detailed site-specific characterization of the N- and O-linked glycosylation of serum-derived hSHBG.
23001782	5	44	theme	85.1	954:957	arg1	%					967:967	85.1 and 95.3%	954:967	%	967:967	It was found that serum-derived hSHBG is N-glycosylated at Asn(351) and Asn(367) with average molar occupancies of 85.1 and 95.3%, respectively.
23001782	6	45	theme	sialylated	1024:1033	arg1	bi-					1063:1065	the same six sialylated and partly core fucosylated bi-	1011:1065	the same six sialylated and partly core fucosylated bi-	1011:1065	Both sites are occupied by the same six sialylated and partly core fucosylated bi- and triantennary N-Glycoforms with lactosamine-type antennas of the form (±NeuAcα6)Galβ4GlcNAc.
23001782	0	46	theme	N-glycosylation	33:47	arg1	macroheterogeneity					11:28	macroheterogeneity	11:28	macroheterogeneity	11:28	Micro- and macroheterogeneity of N-glycosylation yields size and charge isoforms of human sex hormone binding globulin circulating in serum.
23001782	0	46	theme	N-glycosylation	33:47	arg1	Micro-					0:5	Micro-	0:5	Micro-	0:5	Micro- and macroheterogeneity of N-glycosylation yields size and charge isoforms of human sex hormone binding globulin circulating in serum.
23001782	6	47	theme	same	1015:1018	arg1	bi-					1063:1065	the same six sialylated and partly core fucosylated bi-	1011:1065	the same six sialylated and partly core fucosylated bi-	1011:1065	Both sites are occupied by the same six sialylated and partly core fucosylated bi- and triantennary N-Glycoforms with lactosamine-type antennas of the form (±NeuAcα6)Galβ4GlcNAc.
23001782	8	48	theme	1:6	1525:1527	arg1	ratio					1535:1539	a 1:6 molar ratio	1523:1539	a 1:6 molar ratio	1523:1539	The N-terminal Thr(7) was fully occupied by the two O-linked glycans NeuAcα3Galβ3(NeuAcα6)GalNAc (where NeuAc is N-acetylneuraminic acid and GalNAc is N-acetylgalactosamine) and NeuAcα3Galβ3GalNAc in a 1:6 molar ratio.
23001782	6	49	gly	fucosylated	1051:1061	arg1	bi-					1063:1065	the same six sialylated and partly core fucosylated bi-	1011:1065	the same six sialylated and partly core fucosylated bi-	1011:1065	Both sites are occupied by the same six sialylated and partly core fucosylated bi- and triantennary N-Glycoforms with lactosamine-type antennas of the form (±NeuAcα6)Galβ4GlcNAc.
23001782	3	50	theme	N-	479:480	arg1	glycosylation					495:507	the N- and O-linked glycosylation	475:507	the N- and O-linked glycosylation of serum-derived hSHBG	475:530	Here, we perform a detailed site-specific characterization of the N- and O-linked glycosylation of serum-derived hSHBG.
23001782	0	51	theme	size	56:59	arg1	isoforms					72:79	size and charge isoforms	56:79	size and charge isoforms of human sex hormone binding globulin circulating in serum	56:138	Micro- and macroheterogeneity of N-glycosylation yields size and charge isoforms of human sex hormone binding globulin circulating in serum.
23001782	9	52	theme	intact	1570:1575	arg1	hSHBG					1577:1581	intact hSHBG	1570:1581	intact hSHBG	1570:1581	Electrophoretic analysis of intact hSHBG revealed size and charge heterogeneity of the isoforms circulating in blood serum.
23001782	4	53	theme	MS-driven	533:541	arg1	glycoproteomics					543:557	MS-driven glycoproteomics	533:557	MS-driven glycoproteomics	533:557	MS-driven glycoproteomics and glycomics combined with exoglycosidase treatment were used in a bottom-up and top-down manner to determine glycosylation sites, site-specific occupancies and monosaccharide compositions, detailed glycan structures, and the higher level arrangement of glycans on intact hSHBG.
23001782	4	54	theme	intact	825:830	arg1	hSHBG					832:836	intact hSHBG	825:836	intact hSHBG	825:836	MS-driven glycoproteomics and glycomics combined with exoglycosidase treatment were used in a bottom-up and top-down manner to determine glycosylation sites, site-specific occupancies and monosaccharide compositions, detailed glycan structures, and the higher level arrangement of glycans on intact hSHBG.
23001782	1	55	theme	central	208:214	arg1	globulin					167:174	Human sex hormone binding globulin	141:174	Human sex hormone binding globulin (hSHBG)	141:182	Human sex hormone binding globulin (hSHBG) is a serum glycoprotein central to the transport and targeted delivery of sex hormones to steroid-sensitive tissues.
23001782	1	55	theme	central	208:214	arg1	glycoprotein					195:206	a serum glycoprotein	187:206	a serum glycoprotein central to the transport and targeted delivery of sex hormones to steroid-sensitive tissues	187:298	Human sex hormone binding globulin (hSHBG) is a serum glycoprotein central to the transport and targeted delivery of sex hormones to steroid-sensitive tissues.
23001782	6	56	theme	lactosamine-type	1102:1117	arg1	antennas					1119:1126	lactosamine-type antennas	1102:1126	lactosamine-type antennas of the form (±NeuAcα6)Galβ4GlcNAc	1102:1160	Both sites are occupied by the same six sialylated and partly core fucosylated bi- and triantennary N-Glycoforms with lactosamine-type antennas of the form (±NeuAcα6)Galβ4GlcNAc.
23001782	0	57	from	serum	134:138	arg1	isoforms					72:79	size and charge isoforms	56:79	size and charge isoforms of human sex hormone binding globulin circulating in serum	56:138	Micro- and macroheterogeneity of N-glycosylation yields size and charge isoforms of human sex hormone binding globulin circulating in serum.
23001782	3	58	theme	detailed	432:439	arg1	characterization					455:470	a detailed site-specific characterization	430:470	a detailed site-specific characterization of the N- and O-linked glycosylation of serum-derived hSHBG	430:530	Here, we perform a detailed site-specific characterization of the N- and O-linked glycosylation of serum-derived hSHBG.
23001782	10	59	theme	charge	1694:1699	arg1	heterogeneity					1701:1713	charge heterogeneity	1694:1713	charge heterogeneity	1694:1713	Interestingly, the size and charge heterogeneity were shown to originate predominantly from differential Asn(351) glycan occupancies and N-glycan sialylation that may modulate the hSHBG activity.
23001782	4	60	theme	bottom-up	627:635	arg1	manner					650:655	a bottom-up and top-down manner	625:655	manner	650:655	MS-driven glycoproteomics and glycomics combined with exoglycosidase treatment were used in a bottom-up and top-down manner to determine glycosylation sites, site-specific occupancies and monosaccharide compositions, detailed glycan structures, and the higher level arrangement of glycans on intact hSHBG.
23001782	4	61	gly	glycosylation	670:682	arg2	glycans					814:820	glycans	814:820	glycans on intact hSHBG	814:836	MS-driven glycoproteomics and glycomics combined with exoglycosidase treatment were used in a bottom-up and top-down manner to determine glycosylation sites, site-specific occupancies and monosaccharide compositions, detailed glycan structures, and the higher level arrangement of glycans on intact hSHBG.
23001782	4	61	gly	glycosylation	670:682	arg2	sites					684:688	glycosylation sites	670:688	glycosylation sites	670:688	MS-driven glycoproteomics and glycomics combined with exoglycosidase treatment were used in a bottom-up and top-down manner to determine glycosylation sites, site-specific occupancies and monosaccharide compositions, detailed glycan structures, and the higher level arrangement of glycans on intact hSHBG.
23001782	4	61	gly	glycosylation	670:682	arg1	glycans					814:820	glycans	814:820	glycans on intact hSHBG	814:836	MS-driven glycoproteomics and glycomics combined with exoglycosidase treatment were used in a bottom-up and top-down manner to determine glycosylation sites, site-specific occupancies and monosaccharide compositions, detailed glycan structures, and the higher level arrangement of glycans on intact hSHBG.
23001782	4	61	gly	glycosylation	670:682	arg2	hSHBG					832:836	intact hSHBG	825:836	intact hSHBG	825:836	MS-driven glycoproteomics and glycomics combined with exoglycosidase treatment were used in a bottom-up and top-down manner to determine glycosylation sites, site-specific occupancies and monosaccharide compositions, detailed glycan structures, and the higher level arrangement of glycans on intact hSHBG.
23001782	3	62	theme	O-linked	486:493	arg1	glycosylation					495:507	the N- and O-linked glycosylation	475:507	the N- and O-linked glycosylation of serum-derived hSHBG	475:530	Here, we perform a detailed site-specific characterization of the N- and O-linked glycosylation of serum-derived hSHBG.
23001782	4	63	theme	exoglycosidase	587:600	arg1	treatment					602:610	exoglycosidase treatment	587:610	exoglycosidase treatment	587:610	MS-driven glycoproteomics and glycomics combined with exoglycosidase treatment were used in a bottom-up and top-down manner to determine glycosylation sites, site-specific occupancies and monosaccharide compositions, detailed glycan structures, and the higher level arrangement of glycans on intact hSHBG.
23001782	4	64	from	occupancies	705:715	arg1	hSHBG					832:836	intact hSHBG	825:836	intact hSHBG	825:836	MS-driven glycoproteomics and glycomics combined with exoglycosidase treatment were used in a bottom-up and top-down manner to determine glycosylation sites, site-specific occupancies and monosaccharide compositions, detailed glycan structures, and the higher level arrangement of glycans on intact hSHBG.
23001782	10	65	theme	differential	1758:1769	arg1	occupancies					1787:1797	differential Asn(351) glycan occupancies	1758:1797	differential Asn(351) glycan occupancies	1758:1797	Interestingly, the size and charge heterogeneity were shown to originate predominantly from differential Asn(351) glycan occupancies and N-glycan sialylation that may modulate the hSHBG activity.
23001782	8	66	used	occupied	1355:1362	arg2	7					1342:1342	7	1342:1342	7	1342:1342	The N-terminal Thr(7) was fully occupied by the two O-linked glycans NeuAcα3Galβ3(NeuAcα6)GalNAc (where NeuAc is N-acetylneuraminic acid and GalNAc is N-acetylgalactosamine) and NeuAcα3Galβ3GalNAc in a 1:6 molar ratio.
23001782	8	66	used	occupied	1355:1362	arg2	Thr					1338:1340	The N-terminal Thr	1323:1340	The N-terminal Thr(7)	1323:1343	The N-terminal Thr(7) was fully occupied by the two O-linked glycans NeuAcα3Galβ3(NeuAcα6)GalNAc (where NeuAc is N-acetylneuraminic acid and GalNAc is N-acetylgalactosamine) and NeuAcα3Galβ3GalNAc in a 1:6 molar ratio.
23001782	3	67	theme	hSHBG	526:530	arg1	glycosylation					495:507	the N- and O-linked glycosylation	475:507	the N- and O-linked glycosylation of serum-derived hSHBG	475:530	Here, we perform a detailed site-specific characterization of the N- and O-linked glycosylation of serum-derived hSHBG.
23001782	11	68	dep	detailed	1901:1908	arg1	structural					1910:1919	structural	1910:1919	structural	1910:1919	To date, this work represents the most detailed structural map of the heterogeneous hSHBG glycosylation, which is a prerequisite for investigating the functional aspects of the hSHBG glycans.
23001782	11	69	theme	heterogeneous	1932:1944	arg1	prerequisite					1978:1989	a prerequisite	1976:1989	a prerequisite for investigating the functional aspects of the hSHBG glycans	1976:2051	To date, this work represents the most detailed structural map of the heterogeneous hSHBG glycosylation, which is a prerequisite for investigating the functional aspects of the hSHBG glycans.
23001782	11	69	theme	heterogeneous	1932:1944	arg1	glycosylation					1952:1964	the heterogeneous hSHBG glycosylation	1928:1964	the heterogeneous hSHBG glycosylation	1928:1964	To date, this work represents the most detailed structural map of the heterogeneous hSHBG glycosylation, which is a prerequisite for investigating the functional aspects of the hSHBG glycans.
23001782	6	70	theme	Galβ4GlcNAc	1150:1160	arg1	antennas					1119:1126	lactosamine-type antennas	1102:1126	lactosamine-type antennas of the form (±NeuAcα6)Galβ4GlcNAc	1102:1160	Both sites are occupied by the same six sialylated and partly core fucosylated bi- and triantennary N-Glycoforms with lactosamine-type antennas of the form (±NeuAcα6)Galβ4GlcNAc.
23001782	4	71	theme	glycosylation	670:682	arg1	sites					684:688	glycosylation sites	670:688	glycosylation sites	670:688	MS-driven glycoproteomics and glycomics combined with exoglycosidase treatment were used in a bottom-up and top-down manner to determine glycosylation sites, site-specific occupancies and monosaccharide compositions, detailed glycan structures, and the higher level arrangement of glycans on intact hSHBG.
23001782	4	71	theme	glycosylation	670:682	arg1	glycans					814:820	glycans	814:820	glycans on intact hSHBG	814:836	MS-driven glycoproteomics and glycomics combined with exoglycosidase treatment were used in a bottom-up and top-down manner to determine glycosylation sites, site-specific occupancies and monosaccharide compositions, detailed glycan structures, and the higher level arrangement of glycans on intact hSHBG.
23001782	1	72	gly	glycoprotein	195:206	arg1	globulin					167:174	Human sex hormone binding globulin	141:174	Human sex hormone binding globulin (hSHBG)	141:182	Human sex hormone binding globulin (hSHBG) is a serum glycoprotein central to the transport and targeted delivery of sex hormones to steroid-sensitive tissues.
23001782	1	72	gly	glycoprotein	195:206	arg1	glycoprotein					195:206	a serum glycoprotein	187:206	a serum glycoprotein central to the transport and targeted delivery of sex hormones to steroid-sensitive tissues	187:298	Human sex hormone binding globulin (hSHBG) is a serum glycoprotein central to the transport and targeted delivery of sex hormones to steroid-sensitive tissues.
23001782	2	73	theme	molecular	309:317	arg1	mechanisms					319:328	Several molecular mechanisms	301:328	Several molecular mechanisms	301:328	Several molecular mechanisms of action of hSHBG, including the function of its attached glycans remain unknown.
23001782	2	73	theme	molecular	309:317	arg1	function					364:371	the function	360:371	the function of its attached glycans	360:395	Several molecular mechanisms of action of hSHBG, including the function of its attached glycans remain unknown.
23001782	9	74	theme	blood	1653:1657	arg1	serum					1659:1663	blood serum	1653:1663	blood serum	1653:1663	Electrophoretic analysis of intact hSHBG revealed size and charge heterogeneity of the isoforms circulating in blood serum.
23001782	6	75	theme	±NeuAcα6	1141:1148	arg1	Galβ4GlcNAc					1150:1160	the form (±NeuAcα6)Galβ4GlcNAc	1131:1160	the form (±NeuAcα6)Galβ4GlcNAc	1131:1160	Both sites are occupied by the same six sialylated and partly core fucosylated bi- and triantennary N-Glycoforms with lactosamine-type antennas of the form (±NeuAcα6)Galβ4GlcNAc.
23001782	5	76	from	Asn	911:913	arg1	N-glycosylated					880:893	N-glycosylated	880:893	N-glycosylated	880:893	It was found that serum-derived hSHBG is N-glycosylated at Asn(351) and Asn(367) with average molar occupancies of 85.1 and 95.3%, respectively.
23001782	5	77	theme	serum-derived	857:869	arg1	hSHBG					871:875	serum-derived hSHBG	857:875	serum-derived hSHBG	857:875	It was found that serum-derived hSHBG is N-glycosylated at Asn(351) and Asn(367) with average molar occupancies of 85.1 and 95.3%, respectively.
23001782	6	78	theme	form	1135:1138	arg1	Galβ4GlcNAc					1150:1160	the form (±NeuAcα6)Galβ4GlcNAc	1131:1160	the form (±NeuAcα6)Galβ4GlcNAc	1131:1160	Both sites are occupied by the same six sialylated and partly core fucosylated bi- and triantennary N-Glycoforms with lactosamine-type antennas of the form (±NeuAcα6)Galβ4GlcNAc.
23001782	4	79	theme	top-down	641:648	arg1	manner					650:655	a bottom-up and top-down manner	625:655	manner	650:655	MS-driven glycoproteomics and glycomics combined with exoglycosidase treatment were used in a bottom-up and top-down manner to determine glycosylation sites, site-specific occupancies and monosaccharide compositions, detailed glycan structures, and the higher level arrangement of glycans on intact hSHBG.
23001782	1	80	theme	serum	189:193	arg1	globulin					167:174	Human sex hormone binding globulin	141:174	Human sex hormone binding globulin (hSHBG)	141:182	Human sex hormone binding globulin (hSHBG) is a serum glycoprotein central to the transport and targeted delivery of sex hormones to steroid-sensitive tissues.
23001782	1	80	theme	serum	189:193	arg1	glycoprotein					195:206	a serum glycoprotein	187:206	a serum glycoprotein central to the transport and targeted delivery of sex hormones to steroid-sensitive tissues	187:298	Human sex hormone binding globulin (hSHBG) is a serum glycoprotein central to the transport and targeted delivery of sex hormones to steroid-sensitive tissues.
23001782	9	81	gly	heterogeneity	1608:1620	arg1	isoforms					1629:1636	the isoforms	1625:1636	the isoforms circulating in blood serum	1625:1663	Electrophoretic analysis of intact hSHBG revealed size and charge heterogeneity of the isoforms circulating in blood serum.
23001782	3	82	link	serum-derived	512:524	arg1	hSHBG					526:530	serum-derived hSHBG	512:530	serum-derived hSHBG	512:530	Here, we perform a detailed site-specific characterization of the N- and O-linked glycosylation of serum-derived hSHBG.
23001782	0	83	from	isoforms	72:79	arg1	serum					134:138	serum	134:138	serum	134:138	Micro- and macroheterogeneity of N-glycosylation yields size and charge isoforms of human sex hormone binding globulin circulating in serum.
23001782	4	84	gly	occupancies	705:715	arg2	glycans					814:820	glycans	814:820	glycans on intact hSHBG	814:836	MS-driven glycoproteomics and glycomics combined with exoglycosidase treatment were used in a bottom-up and top-down manner to determine glycosylation sites, site-specific occupancies and monosaccharide compositions, detailed glycan structures, and the higher level arrangement of glycans on intact hSHBG.
23001782	11	85	theme	detailed	1901:1908	arg1	map					1921:1923	the most detailed structural map	1892:1923	the most detailed structural map of the heterogeneous hSHBG glycosylation, which is a prerequisite for investigating the functional aspects of the hSHBG glycans	1892:2051	To date, this work represents the most detailed structural map of the heterogeneous hSHBG glycosylation, which is a prerequisite for investigating the functional aspects of the hSHBG glycans.
23001782	8	86	dep	glycans	1384:1390	arg1	NeuAcα6					1405:1411	NeuAcα6	1405:1411	NeuAcα6	1405:1411	The N-terminal Thr(7) was fully occupied by the two O-linked glycans NeuAcα3Galβ3(NeuAcα6)GalNAc (where NeuAc is N-acetylneuraminic acid and GalNAc is N-acetylgalactosamine) and NeuAcα3Galβ3GalNAc in a 1:6 molar ratio.
23001782	8	86	dep	glycans	1384:1390	arg1	NeuAcα3Galβ3GalNAc					1501:1518	NeuAcα3Galβ3GalNAc	1501:1518	NeuAcα3Galβ3GalNAc	1501:1518	The N-terminal Thr(7) was fully occupied by the two O-linked glycans NeuAcα3Galβ3(NeuAcα6)GalNAc (where NeuAc is N-acetylneuraminic acid and GalNAc is N-acetylgalactosamine) and NeuAcα3Galβ3GalNAc in a 1:6 molar ratio.
23001782	8	86	dep	glycans	1384:1390	arg1	glycans					1384:1390	the two O-linked glycans NeuAcα3Galβ3(NeuAcα6)GalNAc (where NeuAc is N-acetylneuraminic acid and GalNAc is N-acetylgalactosamine) and NeuAcα3Galβ3GalNAc	1367:1518	the two O-linked glycans NeuAcα3Galβ3(NeuAcα6)GalNAc (where NeuAc is N-acetylneuraminic acid and GalNAc is N-acetylgalactosamine) and NeuAcα3Galβ3GalNAc in a 1:6 molar ratio	1367:1539	The N-terminal Thr(7) was fully occupied by the two O-linked glycans NeuAcα3Galβ3(NeuAcα6)GalNAc (where NeuAc is N-acetylneuraminic acid and GalNAc is N-acetylgalactosamine) and NeuAcα3Galβ3GalNAc in a 1:6 molar ratio.
23001782	0	87	from	globulin	110:117	arg1	serum					134:138	serum	134:138	serum	134:138	Micro- and macroheterogeneity of N-glycosylation yields size and charge isoforms of human sex hormone binding globulin circulating in serum.
23001782	10	88	theme	N-glycan	1803:1810	arg1	sialylation					1812:1822	N-glycan sialylation	1803:1822	N-glycan sialylation that may modulate the hSHBG activity	1803:1859	Interestingly, the size and charge heterogeneity were shown to originate predominantly from differential Asn(351) glycan occupancies and N-glycan sialylation that may modulate the hSHBG activity.
23001782	4	89	theme	glycans	814:820	arg1	structures					766:775	detailed glycan structures	750:775	detailed glycan structures	750:775	MS-driven glycoproteomics and glycomics combined with exoglycosidase treatment were used in a bottom-up and top-down manner to determine glycosylation sites, site-specific occupancies and monosaccharide compositions, detailed glycan structures, and the higher level arrangement of glycans on intact hSHBG.
23001782	4	89	theme	glycans	814:820	arg1	arrangement					799:809	the higher level arrangement	782:809	the higher level arrangement of glycans on intact hSHBG	782:836	MS-driven glycoproteomics and glycomics combined with exoglycosidase treatment were used in a bottom-up and top-down manner to determine glycosylation sites, site-specific occupancies and monosaccharide compositions, detailed glycan structures, and the higher level arrangement of glycans on intact hSHBG.
23001782	4	89	theme	glycans	814:820	arg1	occupancies					705:715	site-specific occupancies	691:715	site-specific occupancies	691:715	MS-driven glycoproteomics and glycomics combined with exoglycosidase treatment were used in a bottom-up and top-down manner to determine glycosylation sites, site-specific occupancies and monosaccharide compositions, detailed glycan structures, and the higher level arrangement of glycans on intact hSHBG.
23001782	4	89	theme	glycans	814:820	arg1	glycans					814:820	glycans	814:820	glycans on intact hSHBG	814:836	MS-driven glycoproteomics and glycomics combined with exoglycosidase treatment were used in a bottom-up and top-down manner to determine glycosylation sites, site-specific occupancies and monosaccharide compositions, detailed glycan structures, and the higher level arrangement of glycans on intact hSHBG.
23001782	4	89	theme	glycans	814:820	arg1	compositions					736:747	monosaccharide compositions	721:747	monosaccharide compositions	721:747	MS-driven glycoproteomics and glycomics combined with exoglycosidase treatment were used in a bottom-up and top-down manner to determine glycosylation sites, site-specific occupancies and monosaccharide compositions, detailed glycan structures, and the higher level arrangement of glycans on intact hSHBG.
23001782	4	89	theme	glycans	814:820	arg1	sites					684:688	glycosylation sites	670:688	glycosylation sites	670:688	MS-driven glycoproteomics and glycomics combined with exoglycosidase treatment were used in a bottom-up and top-down manner to determine glycosylation sites, site-specific occupancies and monosaccharide compositions, detailed glycan structures, and the higher level arrangement of glycans on intact hSHBG.
23001782	4	90	theme	glycan	759:764	arg1	structures					766:775	detailed glycan structures	750:775	detailed glycan structures	750:775	MS-driven glycoproteomics and glycomics combined with exoglycosidase treatment were used in a bottom-up and top-down manner to determine glycosylation sites, site-specific occupancies and monosaccharide compositions, detailed glycan structures, and the higher level arrangement of glycans on intact hSHBG.
23001782	4	91	from	hSHBG	832:836	arg1	structures					766:775	detailed glycan structures	750:775	detailed glycan structures	750:775	MS-driven glycoproteomics and glycomics combined with exoglycosidase treatment were used in a bottom-up and top-down manner to determine glycosylation sites, site-specific occupancies and monosaccharide compositions, detailed glycan structures, and the higher level arrangement of glycans on intact hSHBG.
23001782	4	91	from	hSHBG	832:836	arg1	arrangement					799:809	the higher level arrangement	782:809	the higher level arrangement of glycans on intact hSHBG	782:836	MS-driven glycoproteomics and glycomics combined with exoglycosidase treatment were used in a bottom-up and top-down manner to determine glycosylation sites, site-specific occupancies and monosaccharide compositions, detailed glycan structures, and the higher level arrangement of glycans on intact hSHBG.
23001782	4	91	from	hSHBG	832:836	arg1	occupancies					705:715	site-specific occupancies	691:715	site-specific occupancies	691:715	MS-driven glycoproteomics and glycomics combined with exoglycosidase treatment were used in a bottom-up and top-down manner to determine glycosylation sites, site-specific occupancies and monosaccharide compositions, detailed glycan structures, and the higher level arrangement of glycans on intact hSHBG.
23001782	4	91	from	hSHBG	832:836	arg1	glycans					814:820	glycans	814:820	glycans on intact hSHBG	814:836	MS-driven glycoproteomics and glycomics combined with exoglycosidase treatment were used in a bottom-up and top-down manner to determine glycosylation sites, site-specific occupancies and monosaccharide compositions, detailed glycan structures, and the higher level arrangement of glycans on intact hSHBG.
23001782	4	91	from	hSHBG	832:836	arg1	compositions					736:747	monosaccharide compositions	721:747	monosaccharide compositions	721:747	MS-driven glycoproteomics and glycomics combined with exoglycosidase treatment were used in a bottom-up and top-down manner to determine glycosylation sites, site-specific occupancies and monosaccharide compositions, detailed glycan structures, and the higher level arrangement of glycans on intact hSHBG.
23001782	4	91	from	hSHBG	832:836	arg1	sites					684:688	glycosylation sites	670:688	glycosylation sites	670:688	MS-driven glycoproteomics and glycomics combined with exoglycosidase treatment were used in a bottom-up and top-down manner to determine glycosylation sites, site-specific occupancies and monosaccharide compositions, detailed glycan structures, and the higher level arrangement of glycans on intact hSHBG.
23001782	1	92	theme	Human	141:145	arg1	hSHBG					177:181	hSHBG	177:181	hSHBG	177:181	Human sex hormone binding globulin (hSHBG) is a serum glycoprotein central to the transport and targeted delivery of sex hormones to steroid-sensitive tissues.
23001782	1	92	theme	Human	141:145	arg1	globulin					167:174	Human sex hormone binding globulin	141:174	Human sex hormone binding globulin (hSHBG)	141:182	Human sex hormone binding globulin (hSHBG) is a serum glycoprotein central to the transport and targeted delivery of sex hormones to steroid-sensitive tissues.
23001782	1	92	theme	Human	141:145	arg1	glycoprotein					195:206	a serum glycoprotein	187:206	a serum glycoprotein central to the transport and targeted delivery of sex hormones to steroid-sensitive tissues	187:298	Human sex hormone binding globulin (hSHBG) is a serum glycoprotein central to the transport and targeted delivery of sex hormones to steroid-sensitive tissues.
23001782	8	93	theme	N-acetylneuraminic	1436:1453	arg1	acid					1455:1458	N-acetylneuraminic acid	1436:1458	N-acetylneuraminic acid	1436:1458	The N-terminal Thr(7) was fully occupied by the two O-linked glycans NeuAcα3Galβ3(NeuAcα6)GalNAc (where NeuAc is N-acetylneuraminic acid and GalNAc is N-acetylgalactosamine) and NeuAcα3Galβ3GalNAc in a 1:6 molar ratio.
23001782	0	94	theme	human	84:88	arg1	globulin					110:117	human sex hormone binding globulin circulating	84:129	human sex hormone binding globulin circulating in serum	84:138	Micro- and macroheterogeneity of N-glycosylation yields size and charge isoforms of human sex hormone binding globulin circulating in serum.
23001782	5	95	from	Asn	898:900	arg1	N-glycosylated					880:893	N-glycosylated	880:893	N-glycosylated	880:893	It was found that serum-derived hSHBG is N-glycosylated at Asn(351) and Asn(367) with average molar occupancies of 85.1 and 95.3%, respectively.
23001782	1	96	theme	hormone	151:157	arg1	hSHBG					177:181	hSHBG	177:181	hSHBG	177:181	Human sex hormone binding globulin (hSHBG) is a serum glycoprotein central to the transport and targeted delivery of sex hormones to steroid-sensitive tissues.
23001782	1	96	theme	hormone	151:157	arg1	globulin					167:174	Human sex hormone binding globulin	141:174	Human sex hormone binding globulin (hSHBG)	141:182	Human sex hormone binding globulin (hSHBG) is a serum glycoprotein central to the transport and targeted delivery of sex hormones to steroid-sensitive tissues.
23001782	1	96	theme	hormone	151:157	arg1	glycoprotein					195:206	a serum glycoprotein	187:206	a serum glycoprotein central to the transport and targeted delivery of sex hormones to steroid-sensitive tissues	187:298	Human sex hormone binding globulin (hSHBG) is a serum glycoprotein central to the transport and targeted delivery of sex hormones to steroid-sensitive tissues.
23001782	4	97	theme	monosaccharide	721:734	arg1	compositions					736:747	monosaccharide compositions	721:747	monosaccharide compositions	721:747	MS-driven glycoproteomics and glycomics combined with exoglycosidase treatment were used in a bottom-up and top-down manner to determine glycosylation sites, site-specific occupancies and monosaccharide compositions, detailed glycan structures, and the higher level arrangement of glycans on intact hSHBG.
23001782	0	98	theme	hormone	94:100	arg1	globulin					110:117	human sex hormone binding globulin circulating	84:129	human sex hormone binding globulin circulating in serum	84:138	Micro- and macroheterogeneity of N-glycosylation yields size and charge isoforms of human sex hormone binding globulin circulating in serum.
23001782	5	99	link	serum-derived	857:869	arg1	hSHBG					871:875	serum-derived hSHBG	857:875	serum-derived hSHBG	857:875	It was found that serum-derived hSHBG is N-glycosylated at Asn(351) and Asn(367) with average molar occupancies of 85.1 and 95.3%, respectively.
23001782	4	100	theme	level	793:797	arg1	arrangement					799:809	the higher level arrangement	782:809	the higher level arrangement of glycans on intact hSHBG	782:836	MS-driven glycoproteomics and glycomics combined with exoglycosidase treatment were used in a bottom-up and top-down manner to determine glycosylation sites, site-specific occupancies and monosaccharide compositions, detailed glycan structures, and the higher level arrangement of glycans on intact hSHBG.
23001782	0	101	theme	globulin	110:117	arg1	isoforms					72:79	size and charge isoforms	56:79	size and charge isoforms of human sex hormone binding globulin circulating in serum	56:138	Micro- and macroheterogeneity of N-glycosylation yields size and charge isoforms of human sex hormone binding globulin circulating in serum.
23001782	7	102	gly	glycosylation	1303:1315	arg2	site					1317:1320	a more surface-exposed glycosylation site	1280:1320	a more surface-exposed glycosylation site	1280:1320	N-Glycoforms of Asn(367) were slightly more branched and core fucosylated than Asn(351) N-glycoforms due probably to a more surface-exposed glycosylation site.
23001782	5	103	theme	%	967:967	arg1	occupancies					939:949	average molar occupancies	925:949	average molar occupancies of 85.1 and 95.3%, respectively	925:981	It was found that serum-derived hSHBG is N-glycosylated at Asn(351) and Asn(367) with average molar occupancies of 85.1 and 95.3%, respectively.
23001782	7	104	theme	surface-exposed	1287:1301	arg1	site					1317:1320	a more surface-exposed glycosylation site	1280:1320	a more surface-exposed glycosylation site	1280:1320	N-Glycoforms of Asn(367) were slightly more branched and core fucosylated than Asn(351) N-glycoforms due probably to a more surface-exposed glycosylation site.
23001782	6	105	dep	sialylated	1024:1033	arg1	six					1020:1022	six	1020:1022	six	1020:1022	Both sites are occupied by the same six sialylated and partly core fucosylated bi- and triantennary N-Glycoforms with lactosamine-type antennas of the form (±NeuAcα6)Galβ4GlcNAc.
23001782	7	106	theme	Asn	1179:1181	arg1	N-Glycoforms					1163:1174	N-Glycoforms	1163:1174	N-Glycoforms of Asn(367)	1163:1186	N-Glycoforms of Asn(367) were slightly more branched and core fucosylated than Asn(351) N-glycoforms due probably to a more surface-exposed glycosylation site.
23001782	5	107	theme	molar	933:937	arg1	occupancies					939:949	average molar occupancies	925:949	average molar occupancies of 85.1 and 95.3%, respectively	925:981	It was found that serum-derived hSHBG is N-glycosylated at Asn(351) and Asn(367) with average molar occupancies of 85.1 and 95.3%, respectively.
23001782	1	108	theme	hormones	262:269	arg1	transport					223:231	transport	223:231	transport	223:231	Human sex hormone binding globulin (hSHBG) is a serum glycoprotein central to the transport and targeted delivery of sex hormones to steroid-sensitive tissues.
23001782	1	108	theme	hormones	262:269	arg1	delivery					246:253	targeted delivery	237:253	targeted delivery	237:253	Human sex hormone binding globulin (hSHBG) is a serum glycoprotein central to the transport and targeted delivery of sex hormones to steroid-sensitive tissues.
23001782	5	109	with	N-glycosylated	880:893	arg1	occupancies					939:949	average molar occupancies	925:949	average molar occupancies of 85.1 and 95.3%, respectively	925:981	It was found that serum-derived hSHBG is N-glycosylated at Asn(351) and Asn(367) with average molar occupancies of 85.1 and 95.3%, respectively.
23001782	1	110	theme	steroid-sensitive	274:290	arg1	tissues					292:298	steroid-sensitive tissues	274:298	steroid-sensitive tissues	274:298	Human sex hormone binding globulin (hSHBG) is a serum glycoprotein central to the transport and targeted delivery of sex hormones to steroid-sensitive tissues.
23001782	9	111	theme	Electrophoretic	1542:1556	arg1	analysis					1558:1565	Electrophoretic analysis	1542:1565	Electrophoretic analysis of intact hSHBG	1542:1581	Electrophoretic analysis of intact hSHBG revealed size and charge heterogeneity of the isoforms circulating in blood serum.
23001782	8	112	theme	molar	1529:1533	arg1	ratio					1535:1539	a 1:6 molar ratio	1523:1539	a 1:6 molar ratio	1523:1539	The N-terminal Thr(7) was fully occupied by the two O-linked glycans NeuAcα3Galβ3(NeuAcα6)GalNAc (where NeuAc is N-acetylneuraminic acid and GalNAc is N-acetylgalactosamine) and NeuAcα3Galβ3GalNAc in a 1:6 molar ratio.
23001782	2	113	theme	glycans	389:395	arg1	function					364:371	the function	360:371	the function of its attached glycans	360:395	Several molecular mechanisms of action of hSHBG, including the function of its attached glycans remain unknown.
23001782	8	114	dep	NeuAcα6	1405:1411	arg1	GalNAc					1413:1418	GalNAc	1413:1418	NeuAcα3Galβ3(NeuAcα6)GalNAc (where NeuAc is N-acetylneuraminic acid and GalNAc is N-acetylgalactosamine)	1392:1495	The N-terminal Thr(7) was fully occupied by the two O-linked glycans NeuAcα3Galβ3(NeuAcα6)GalNAc (where NeuAc is N-acetylneuraminic acid and GalNAc is N-acetylgalactosamine) and NeuAcα3Galβ3GalNAc in a 1:6 molar ratio.
23001782	0	115	gly	macroheterogeneity	11:28	arg1	N-glycosylation					33:47	N-glycosylation	33:47	N-glycosylation	33:47	Micro- and macroheterogeneity of N-glycosylation yields size and charge isoforms of human sex hormone binding globulin circulating in serum.
23001782	2	116	theme	action	333:338	arg1	mechanisms					319:328	Several molecular mechanisms	301:328	Several molecular mechanisms	301:328	Several molecular mechanisms of action of hSHBG, including the function of its attached glycans remain unknown.
23001782	2	116	theme	action	333:338	arg1	function					364:371	the function	360:371	the function of its attached glycans	360:395	Several molecular mechanisms of action of hSHBG, including the function of its attached glycans remain unknown.
23001782	4	117	from	structures	766:775	arg1	hSHBG					832:836	intact hSHBG	825:836	intact hSHBG	825:836	MS-driven glycoproteomics and glycomics combined with exoglycosidase treatment were used in a bottom-up and top-down manner to determine glycosylation sites, site-specific occupancies and monosaccharide compositions, detailed glycan structures, and the higher level arrangement of glycans on intact hSHBG.
23001782	9	118	theme	hSHBG	1577:1581	arg1	analysis					1558:1565	Electrophoretic analysis	1542:1565	Electrophoretic analysis of intact hSHBG	1542:1581	Electrophoretic analysis of intact hSHBG revealed size and charge heterogeneity of the isoforms circulating in blood serum.
23001782	7	119	theme	Asn	1242:1244	arg1	N-glycoforms					1251:1262	Asn(351) N-glycoforms	1242:1262	Asn(351) N-glycoforms	1242:1262	N-Glycoforms of Asn(367) were slightly more branched and core fucosylated than Asn(351) N-glycoforms due probably to a more surface-exposed glycosylation site.
23001782	10	120	theme	hSHBG	1846:1850	arg1	activity					1852:1859	the hSHBG activity	1842:1859	the hSHBG activity	1842:1859	Interestingly, the size and charge heterogeneity were shown to originate predominantly from differential Asn(351) glycan occupancies and N-glycan sialylation that may modulate the hSHBG activity.
23001782	7	121	theme	glycosylation	1303:1315	arg1	site					1317:1320	a more surface-exposed glycosylation site	1280:1320	a more surface-exposed glycosylation site	1280:1320	N-Glycoforms of Asn(367) were slightly more branched and core fucosylated than Asn(351) N-glycoforms due probably to a more surface-exposed glycosylation site.
23001782	8	122	theme	O-linked	1375:1382	arg1	NeuAcα6					1405:1411	NeuAcα6	1405:1411	NeuAcα6	1405:1411	The N-terminal Thr(7) was fully occupied by the two O-linked glycans NeuAcα3Galβ3(NeuAcα6)GalNAc (where NeuAc is N-acetylneuraminic acid and GalNAc is N-acetylgalactosamine) and NeuAcα3Galβ3GalNAc in a 1:6 molar ratio.
23001782	8	122	theme	O-linked	1375:1382	arg1	NeuAcα3Galβ3GalNAc					1501:1518	NeuAcα3Galβ3GalNAc	1501:1518	NeuAcα3Galβ3GalNAc	1501:1518	The N-terminal Thr(7) was fully occupied by the two O-linked glycans NeuAcα3Galβ3(NeuAcα6)GalNAc (where NeuAc is N-acetylneuraminic acid and GalNAc is N-acetylgalactosamine) and NeuAcα3Galβ3GalNAc in a 1:6 molar ratio.
23001782	8	122	theme	O-linked	1375:1382	arg1	glycans					1384:1390	the two O-linked glycans NeuAcα3Galβ3(NeuAcα6)GalNAc (where NeuAc is N-acetylneuraminic acid and GalNAc is N-acetylgalactosamine) and NeuAcα3Galβ3GalNAc	1367:1518	the two O-linked glycans NeuAcα3Galβ3(NeuAcα6)GalNAc (where NeuAc is N-acetylneuraminic acid and GalNAc is N-acetylgalactosamine) and NeuAcα3Galβ3GalNAc in a 1:6 molar ratio	1367:1539	The N-terminal Thr(7) was fully occupied by the two O-linked glycans NeuAcα3Galβ3(NeuAcα6)GalNAc (where NeuAc is N-acetylneuraminic acid and GalNAc is N-acetylgalactosamine) and NeuAcα3Galβ3GalNAc in a 1:6 molar ratio.
23001782	3	123	theme	serum-derived	512:524	arg1	hSHBG					526:530	serum-derived hSHBG	512:530	serum-derived hSHBG	512:530	Here, we perform a detailed site-specific characterization of the N- and O-linked glycosylation of serum-derived hSHBG.
23001782	4	124	from	compositions	736:747	arg1	hSHBG					832:836	intact hSHBG	825:836	intact hSHBG	825:836	MS-driven glycoproteomics and glycomics combined with exoglycosidase treatment were used in a bottom-up and top-down manner to determine glycosylation sites, site-specific occupancies and monosaccharide compositions, detailed glycan structures, and the higher level arrangement of glycans on intact hSHBG.
28467637	5	0	theme	G-protein-dependent	633:651	arg1	signaling					653:661	isoproterenol-promoted G-protein-dependent signaling	610:661	isoproterenol-promoted G-protein-dependent signaling	610:661	Deletion of the N-glycan at the N-terminus rather than Asn187 showed decreased effects on isoproterenol-promoted G-protein-dependent signaling, β-arrestin2 recruitment, and receptor internalization.
28467637	7	1	theme	receptor	1007:1014	arg1	dimerization					1016:1027	receptor dimerization	1007:1027	receptor dimerization	1007:1027	As decreased β2 AR homodimer accompanied with reduced efficiency for receptor function, we proposed that the N-glycosylation of β2 AR regulated receptor function by influencing receptor dimerization.
28467637	9	2	dep	showed	1242:1247	arg1	similar					1321:1327	similar	1321:1327	similar	1321:1327	Studies of Lys60 and Glu338, two residues at the receptor dimerization interface, exhibited that the K60A/E338A showed decreased β2 AR dimerization and its effects on receptor signaling were similar to N6Q and N15Q, which further supported the importance of receptor dimerization for receptor function.
28467637	4	3	theme	receptor	480:487	arg1	expression					489:498	receptor expression	480:498	receptor expression	480:498	Here, we show that deletion of the N-glycan did not affect receptor expression and ligand binding.
28467637	9	4	theme	dimerization	1188:1199	arg1	interface					1201:1209	the receptor dimerization interface	1175:1209	the receptor dimerization interface	1175:1209	Studies of Lys60 and Glu338, two residues at the receptor dimerization interface, exhibited that the K60A/E338A showed decreased β2 AR dimerization and its effects on receptor signaling were similar to N6Q and N15Q, which further supported the importance of receptor dimerization for receptor function.
28467637	9	5	from	interface	1201:1209	arg1	Studies					1130:1136	Studies	1130:1136	Studies of Lys60 and Glu338	1130:1156	Studies of Lys60 and Glu338, two residues at the receptor dimerization interface, exhibited that the K60A/E338A showed decreased β2 AR dimerization and its effects on receptor signaling were similar to N6Q and N15Q, which further supported the importance of receptor dimerization for receptor function.
28467637	9	5	from	interface	1201:1209	arg1	residues					1163:1170	two residues	1159:1170	two residues at the receptor dimerization interface	1159:1209	Studies of Lys60 and Glu338, two residues at the receptor dimerization interface, exhibited that the K60A/E338A showed decreased β2 AR dimerization and its effects on receptor signaling were similar to N6Q and N15Q, which further supported the importance of receptor dimerization for receptor function.
28467637	9	6	theme	receptor	1179:1186	arg1	interface					1201:1209	the receptor dimerization interface	1175:1209	the receptor dimerization interface	1175:1209	Studies of Lys60 and Glu338, two residues at the receptor dimerization interface, exhibited that the K60A/E338A showed decreased β2 AR dimerization and its effects on receptor signaling were similar to N6Q and N15Q, which further supported the importance of receptor dimerization for receptor function.
28467637	7	7	theme	receptor	899:906	arg1	function					908:915	receptor function	899:915	receptor function	899:915	As decreased β2 AR homodimer accompanied with reduced efficiency for receptor function, we proposed that the N-glycosylation of β2 AR regulated receptor function by influencing receptor dimerization.
28467637	9	8	from	dimerization	1265:1276	arg1	signaling					1306:1314	receptor signaling	1297:1314	receptor signaling	1297:1314	Studies of Lys60 and Glu338, two residues at the receptor dimerization interface, exhibited that the K60A/E338A showed decreased β2 AR dimerization and its effects on receptor signaling were similar to N6Q and N15Q, which further supported the importance of receptor dimerization for receptor function.
28467637	5	9	theme	β-arrestin2	664:674	arg1	recruitment					676:686	β-arrestin2 recruitment	664:686	β-arrestin2 recruitment	664:686	Deletion of the N-glycan at the N-terminus rather than Asn187 showed decreased effects on isoproterenol-promoted G-protein-dependent signaling, β-arrestin2 recruitment, and receptor internalization.
28467637	7	10	theme	reduced	876:882	arg1	efficiency					884:893	reduced efficiency	876:893	reduced efficiency for receptor function	876:915	As decreased β2 AR homodimer accompanied with reduced efficiency for receptor function, we proposed that the N-glycosylation of β2 AR regulated receptor function by influencing receptor dimerization.
28467637	3	11	theme	adrenergic	277:286	arg1	AR					301:302	β2 AR	298:302	β2 AR	298:302	β2 adrenergic receptor (β2 AR) has three N-glycosylation sites: Asn6, Asn15 at the N-terminus, and Asn187 at the second extracellular loop (ECL2).
28467637	3	11	theme	adrenergic	277:286	arg1	receptor					288:295	β2 adrenergic receptor	274:295	β2 adrenergic receptor (β2 AR)	274:303	β2 adrenergic receptor (β2 AR) has three N-glycosylation sites: Asn6, Asn15 at the N-terminus, and Asn187 at the second extracellular loop (ECL2).
28467637	6	12	theme	receptor	807:814	arg1	dimerization					816:827	receptor dimerization	807:827	receptor dimerization	807:827	Both N6Q and N15Q showed decreased receptor dimerization, while N187Q did not influence receptor dimerization.
28467637	11	13	dep	F	1567:1567	arg1	A					1625:1625	endo-β-N-acetylglucosaminidase A	1594:1625	Peptide-N-glycosidase F (PNGase F, EC 3.2.2.11); endo-β-N-acetylglucosaminidase A (Endo-A, EC 3.2.1.96).	1545:1648	Peptide-N-glycosidase F (PNGase F, EC 3.2.2.11); endo-β-N-acetylglucosaminidase A (Endo-A, EC 3.2.1.96).
28467637	11	13	dep	F	1567:1567	arg1	EC					1580:1581	EC 3.2.2.11	1580:1590	EC 3.2.2.11	1580:1590	Peptide-N-glycosidase F (PNGase F, EC 3.2.2.11); endo-β-N-acetylglucosaminidase A (Endo-A, EC 3.2.1.96).
28467637	11	13	dep	F	1567:1567	arg1	F					1577:1577	PNGase F	1570:1577	PNGase F	1570:1577	Peptide-N-glycosidase F (PNGase F, EC 3.2.2.11); endo-β-N-acetylglucosaminidase A (Endo-A, EC 3.2.1.96).
28467637	3	14	contain	has	305:307	arg1	AR					301:302	β2 AR	298:302	β2 AR	298:302	β2 adrenergic receptor (β2 AR) has three N-glycosylation sites: Asn6, Asn15 at the N-terminus, and Asn187 at the second extracellular loop (ECL2).
28467637	3	14	contain	has	305:307	arg2	Asn6					338:341	Asn6	338:341	Asn6	338:341	β2 adrenergic receptor (β2 AR) has three N-glycosylation sites: Asn6, Asn15 at the N-terminus, and Asn187 at the second extracellular loop (ECL2).
28467637	3	14	contain	has	305:307	arg2	Asn15					344:348	Asn15	344:348	Asn15 at the N-terminus	344:366	β2 adrenergic receptor (β2 AR) has three N-glycosylation sites: Asn6, Asn15 at the N-terminus, and Asn187 at the second extracellular loop (ECL2).
28467637	3	14	contain	has	305:307	arg2	Asn187					373:378	Asn187	373:378	Asn187	373:378	β2 adrenergic receptor (β2 AR) has three N-glycosylation sites: Asn6, Asn15 at the N-terminus, and Asn187 at the second extracellular loop (ECL2).
28467637	3	14	contain	has	305:307	arg2	sites					331:335	three N-glycosylation sites	309:335	three N-glycosylation sites: Asn6, Asn15 at the N-terminus, and Asn187	309:378	β2 adrenergic receptor (β2 AR) has three N-glycosylation sites: Asn6, Asn15 at the N-terminus, and Asn187 at the second extracellular loop (ECL2).
28467637	3	14	contain	has	305:307	arg1	receptor					288:295	β2 adrenergic receptor	274:295	β2 adrenergic receptor (β2 AR)	274:303	β2 adrenergic receptor (β2 AR) has three N-glycosylation sites: Asn6, Asn15 at the N-terminus, and Asn187 at the second extracellular loop (ECL2).
28467637	3	15	dep	sites	331:335	arg1	Asn15					344:348	Asn15	344:348	Asn15 at the N-terminus	344:366	β2 adrenergic receptor (β2 AR) has three N-glycosylation sites: Asn6, Asn15 at the N-terminus, and Asn187 at the second extracellular loop (ECL2).
28467637	3	15	dep	sites	331:335	arg1	Asn187					373:378	Asn187	373:378	Asn187	373:378	β2 adrenergic receptor (β2 AR) has three N-glycosylation sites: Asn6, Asn15 at the N-terminus, and Asn187 at the second extracellular loop (ECL2).
28467637	3	15	dep	sites	331:335	arg1	sites					331:335	three N-glycosylation sites	309:335	three N-glycosylation sites: Asn6, Asn15 at the N-terminus, and Asn187	309:378	β2 adrenergic receptor (β2 AR) has three N-glycosylation sites: Asn6, Asn15 at the N-terminus, and Asn187 at the second extracellular loop (ECL2).
28467637	3	15	dep	sites	331:335	arg1	Asn6					338:341	Asn6	338:341	Asn6	338:341	β2 adrenergic receptor (β2 AR) has three N-glycosylation sites: Asn6, Asn15 at the N-terminus, and Asn187 at the second extracellular loop (ECL2).
28467637	4	16	theme	N-glycan	456:463	arg1	deletion					440:447	deletion	440:447	deletion of the N-glycan	440:463	Here, we show that deletion of the N-glycan did not affect receptor expression and ligand binding.
28467637	5	17	theme	N-glycan	536:543	arg1	Deletion					520:527	Deletion	520:527	Deletion of the N-glycan at the N-terminus rather than Asn187	520:580	Deletion of the N-glycan at the N-terminus rather than Asn187 showed decreased effects on isoproterenol-promoted G-protein-dependent signaling, β-arrestin2 recruitment, and receptor internalization.
28467637	9	18	theme	AR	1262:1263	arg1	dimerization					1265:1276	decreased β2 AR dimerization	1249:1276	decreased β2 AR dimerization	1249:1276	Studies of Lys60 and Glu338, two residues at the receptor dimerization interface, exhibited that the K60A/E338A showed decreased β2 AR dimerization and its effects on receptor signaling were similar to N6Q and N15Q, which further supported the importance of receptor dimerization for receptor function.
28467637	5	19	from	effects	599:605	arg1	signaling					653:661	isoproterenol-promoted G-protein-dependent signaling	610:661	isoproterenol-promoted G-protein-dependent signaling	610:661	Deletion of the N-glycan at the N-terminus rather than Asn187 showed decreased effects on isoproterenol-promoted G-protein-dependent signaling, β-arrestin2 recruitment, and receptor internalization.
28467637	5	19	from	effects	599:605	arg1	recruitment					676:686	β-arrestin2 recruitment	664:686	β-arrestin2 recruitment	664:686	Deletion of the N-glycan at the N-terminus rather than Asn187 showed decreased effects on isoproterenol-promoted G-protein-dependent signaling, β-arrestin2 recruitment, and receptor internalization.
28467637	5	19	from	effects	599:605	arg1	internalization					702:716	receptor internalization	693:716	receptor internalization	693:716	Deletion of the N-glycan at the N-terminus rather than Asn187 showed decreased effects on isoproterenol-promoted G-protein-dependent signaling, β-arrestin2 recruitment, and receptor internalization.
28467637	7	20	theme	AR	961:962	arg1	N-glycosylation					939:953	the N-glycosylation	935:953	the N-glycosylation of β2 AR	935:962	As decreased β2 AR homodimer accompanied with reduced efficiency for receptor function, we proposed that the N-glycosylation of β2 AR regulated receptor function by influencing receptor dimerization.
28467637	11	21	theme	endo-β-N-acetylglucosaminidase	1594:1623	arg1	A					1625:1625	endo-β-N-acetylglucosaminidase A	1594:1625	Peptide-N-glycosidase F (PNGase F, EC 3.2.2.11); endo-β-N-acetylglucosaminidase A (Endo-A, EC 3.2.1.96).	1545:1648	Peptide-N-glycosidase F (PNGase F, EC 3.2.2.11); endo-β-N-acetylglucosaminidase A (Endo-A, EC 3.2.1.96).
28467637	10	22	theme	new	1452:1454	arg1	insights					1456:1463	new insights	1452:1463	new insights into the relationship among glycosylation, dimerization, and function of GPCRs	1452:1542	This work provides new insights into the relationship among glycosylation, dimerization, and function of GPCRs.
28467637	3	23	theme	β2	274:275	arg1	AR					301:302	β2 AR	298:302	β2 AR	298:302	β2 adrenergic receptor (β2 AR) has three N-glycosylation sites: Asn6, Asn15 at the N-terminus, and Asn187 at the second extracellular loop (ECL2).
28467637	3	23	theme	β2	274:275	arg1	receptor					288:295	β2 adrenergic receptor	274:295	β2 adrenergic receptor (β2 AR)	274:303	β2 adrenergic receptor (β2 AR) has three N-glycosylation sites: Asn6, Asn15 at the N-terminus, and Asn187 at the second extracellular loop (ECL2).
28467637	5	24	theme	decreased	589:597	arg1	effects					599:605	decreased effects	589:605	decreased effects on isoproterenol-promoted G-protein-dependent signaling, β-arrestin2 recruitment, and receptor internalization	589:716	Deletion of the N-glycan at the N-terminus rather than Asn187 showed decreased effects on isoproterenol-promoted G-protein-dependent signaling, β-arrestin2 recruitment, and receptor internalization.
28467637	7	25	theme	AR	846:847	arg1	homodimer					849:857	decreased β2 AR homodimer	833:857	decreased β2 AR homodimer accompanied with reduced efficiency for receptor function	833:915	As decreased β2 AR homodimer accompanied with reduced efficiency for receptor function, we proposed that the N-glycosylation of β2 AR regulated receptor function by influencing receptor dimerization.
28467637	0	26	theme	β2	23:24	arg1	receptor					37:44	the β2 adrenergic receptor	19:44	the β2 adrenergic receptor	19:44	N-glycosylation of the β2 adrenergic receptor regulates receptor function by modulating dimerization.
28467637	7	27	theme	receptor	974:981	arg1	function					983:990	receptor function	974:990	receptor function	974:990	As decreased β2 AR homodimer accompanied with reduced efficiency for receptor function, we proposed that the N-glycosylation of β2 AR regulated receptor function by influencing receptor dimerization.
28467637	11	28	theme	PNGase	1570:1575	arg1	EC					1580:1581	EC 3.2.2.11	1580:1590	EC 3.2.2.11	1580:1590	Peptide-N-glycosidase F (PNGase F, EC 3.2.2.11); endo-β-N-acetylglucosaminidase A (Endo-A, EC 3.2.1.96).
28467637	11	28	theme	PNGase	1570:1575	arg1	F					1577:1577	PNGase F	1570:1577	PNGase F	1570:1577	Peptide-N-glycosidase F (PNGase F, EC 3.2.2.11); endo-β-N-acetylglucosaminidase A (Endo-A, EC 3.2.1.96).
28467637	11	29	theme	Peptide-N-glycosidase	1545:1565	arg1	F					1567:1567	Peptide-N-glycosidase F	1545:1567	Peptide-N-glycosidase F (PNGase F, EC 3.2.2.11); endo-β-N-acetylglucosaminidase A (Endo-A, EC 3.2.1.96).	1545:1648	Peptide-N-glycosidase F (PNGase F, EC 3.2.2.11); endo-β-N-acetylglucosaminidase A (Endo-A, EC 3.2.1.96).
28467637	9	30	theme	decreased	1249:1257	arg1	dimerization					1265:1276	decreased β2 AR dimerization	1249:1276	decreased β2 AR dimerization	1249:1276	Studies of Lys60 and Glu338, two residues at the receptor dimerization interface, exhibited that the K60A/E338A showed decreased β2 AR dimerization and its effects on receptor signaling were similar to N6Q and N15Q, which further supported the importance of receptor dimerization for receptor function.
28467637	9	31	theme	Lys60	1141:1145	arg1	Studies					1130:1136	Studies	1130:1136	Studies of Lys60 and Glu338	1130:1156	Studies of Lys60 and Glu338, two residues at the receptor dimerization interface, exhibited that the K60A/E338A showed decreased β2 AR dimerization and its effects on receptor signaling were similar to N6Q and N15Q, which further supported the importance of receptor dimerization for receptor function.
28467637	9	31	theme	Lys60	1141:1145	arg1	residues					1163:1170	two residues	1159:1170	two residues at the receptor dimerization interface	1159:1209	Studies of Lys60 and Glu338, two residues at the receptor dimerization interface, exhibited that the K60A/E338A showed decreased β2 AR dimerization and its effects on receptor signaling were similar to N6Q and N15Q, which further supported the importance of receptor dimerization for receptor function.
28467637	7	32	theme	decreased	833:841	arg1	homodimer					849:857	decreased β2 AR homodimer	833:857	decreased β2 AR homodimer accompanied with reduced efficiency for receptor function	833:915	As decreased β2 AR homodimer accompanied with reduced efficiency for receptor function, we proposed that the N-glycosylation of β2 AR regulated receptor function by influencing receptor dimerization.
28467637	5	33	from	Asn187	575:580	arg1	Deletion					520:527	Deletion	520:527	Deletion of the N-glycan at the N-terminus rather than Asn187	520:580	Deletion of the N-glycan at the N-terminus rather than Asn187 showed decreased effects on isoproterenol-promoted G-protein-dependent signaling, β-arrestin2 recruitment, and receptor internalization.
28467637	0	34	theme	receptor	37:44	arg1	N-glycosylation					0:14	N-glycosylation	0:14	N-glycosylation of the β2 adrenergic receptor	0:44	N-glycosylation of the β2 adrenergic receptor regulates receptor function by modulating dimerization.
28467637	5	35	from	N-terminus	552:561	arg1	Deletion					520:527	Deletion	520:527	Deletion of the N-glycan at the N-terminus rather than Asn187	520:580	Deletion of the N-glycan at the N-terminus rather than Asn187 showed decreased effects on isoproterenol-promoted G-protein-dependent signaling, β-arrestin2 recruitment, and receptor internalization.
28467637	9	36	theme	β2	1259:1260	arg1	dimerization					1265:1276	decreased β2 AR dimerization	1249:1276	decreased β2 AR dimerization	1249:1276	Studies of Lys60 and Glu338, two residues at the receptor dimerization interface, exhibited that the K60A/E338A showed decreased β2 AR dimerization and its effects on receptor signaling were similar to N6Q and N15Q, which further supported the importance of receptor dimerization for receptor function.
28467637	0	37	gly	N-glycosylation	0:14	arg1	receptor					37:44	the β2 adrenergic receptor	19:44	the β2 adrenergic receptor	19:44	N-glycosylation of the β2 adrenergic receptor regulates receptor function by modulating dimerization.
28467637	7	38	theme	β2	843:844	arg1	homodimer					849:857	decreased β2 AR homodimer	833:857	decreased β2 AR homodimer accompanied with reduced efficiency for receptor function	833:915	As decreased β2 AR homodimer accompanied with reduced efficiency for receptor function, we proposed that the N-glycosylation of β2 AR regulated receptor function by influencing receptor dimerization.
28467637	0	39	theme	adrenergic	26:35	arg1	receptor					37:44	the β2 adrenergic receptor	19:44	the β2 adrenergic receptor	19:44	N-glycosylation of the β2 adrenergic receptor regulates receptor function by modulating dimerization.
28467637	8	40	theme	dimerization	1106:1117	arg1	interface					1119:1127	the dimerization interface	1102:1127	the dimerization interface	1102:1127	To verify this hypothesis, we further paid attention to the residues at the dimerization interface.
28467637	3	41	from	N-terminus	357:366	arg1	Asn15					344:348	Asn15	344:348	Asn15 at the N-terminus	344:366	β2 adrenergic receptor (β2 AR) has three N-glycosylation sites: Asn6, Asn15 at the N-terminus, and Asn187 at the second extracellular loop (ECL2).
28467637	3	41	from	N-terminus	357:366	arg1	Asn6					338:341	Asn6	338:341	Asn6	338:341	β2 adrenergic receptor (β2 AR) has three N-glycosylation sites: Asn6, Asn15 at the N-terminus, and Asn187 at the second extracellular loop (ECL2).
28467637	3	41	from	N-terminus	357:366	arg1	sites					331:335	three N-glycosylation sites	309:335	three N-glycosylation sites: Asn6, Asn15 at the N-terminus, and Asn187	309:378	β2 adrenergic receptor (β2 AR) has three N-glycosylation sites: Asn6, Asn15 at the N-terminus, and Asn187 at the second extracellular loop (ECL2).
28467637	3	41	from	N-terminus	357:366	arg1	Asn187					373:378	Asn187	373:378	Asn187	373:378	β2 adrenergic receptor (β2 AR) has three N-glycosylation sites: Asn6, Asn15 at the N-terminus, and Asn187 at the second extracellular loop (ECL2).
28467637	2	42	theme	GPCR	258:261	arg1	signaling					263:271	GPCR signaling	258:271	GPCR signaling	258:271	However, it remains unknown how N-glycosylation affects GPCR signaling.
28467637	9	43	theme	receptor	1388:1395	arg1	dimerization					1397:1408	receptor dimerization	1388:1408	receptor dimerization	1388:1408	Studies of Lys60 and Glu338, two residues at the receptor dimerization interface, exhibited that the K60A/E338A showed decreased β2 AR dimerization and its effects on receptor signaling were similar to N6Q and N15Q, which further supported the importance of receptor dimerization for receptor function.
28467637	3	44	theme	second	387:392	arg1	ECL2					414:417	ECL2	414:417	ECL2	414:417	β2 adrenergic receptor (β2 AR) has three N-glycosylation sites: Asn6, Asn15 at the N-terminus, and Asn187 at the second extracellular loop (ECL2).
28467637	3	44	theme	second	387:392	arg1	loop					408:411	the second extracellular loop	383:411	the second extracellular loop (ECL2)	383:418	β2 adrenergic receptor (β2 AR) has three N-glycosylation sites: Asn6, Asn15 at the N-terminus, and Asn187 at the second extracellular loop (ECL2).
28467637	3	45	theme	N-glycosylation	315:329	arg1	Asn6					338:341	Asn6	338:341	Asn6	338:341	β2 adrenergic receptor (β2 AR) has three N-glycosylation sites: Asn6, Asn15 at the N-terminus, and Asn187 at the second extracellular loop (ECL2).
28467637	3	45	theme	N-glycosylation	315:329	arg1	Asn15					344:348	Asn15	344:348	Asn15 at the N-terminus	344:366	β2 adrenergic receptor (β2 AR) has three N-glycosylation sites: Asn6, Asn15 at the N-terminus, and Asn187 at the second extracellular loop (ECL2).
28467637	3	45	theme	N-glycosylation	315:329	arg1	Asn187					373:378	Asn187	373:378	Asn187	373:378	β2 adrenergic receptor (β2 AR) has three N-glycosylation sites: Asn6, Asn15 at the N-terminus, and Asn187 at the second extracellular loop (ECL2).
28467637	3	45	theme	N-glycosylation	315:329	arg1	sites					331:335	three N-glycosylation sites	309:335	three N-glycosylation sites: Asn6, Asn15 at the N-terminus, and Asn187	309:378	β2 adrenergic receptor (β2 AR) has three N-glycosylation sites: Asn6, Asn15 at the N-terminus, and Asn187 at the second extracellular loop (ECL2).
28467637	3	46	gly	N-glycosylation	315:329	arg2	sites					331:335	three N-glycosylation sites	309:335	three N-glycosylation sites: Asn6, Asn15 at the N-terminus, and Asn187	309:378	β2 adrenergic receptor (β2 AR) has three N-glycosylation sites: Asn6, Asn15 at the N-terminus, and Asn187 at the second extracellular loop (ECL2).
28467637	3	46	gly	N-glycosylation	315:329	arg2	three					309:313	three	309:313	three	309:313	β2 adrenergic receptor (β2 AR) has three N-glycosylation sites: Asn6, Asn15 at the N-terminus, and Asn187 at the second extracellular loop (ECL2).
28467637	3	46	gly	N-glycosylation	315:329	arg2	Asn15					344:348	Asn15	344:348	Asn15 at the N-terminus	344:366	β2 adrenergic receptor (β2 AR) has three N-glycosylation sites: Asn6, Asn15 at the N-terminus, and Asn187 at the second extracellular loop (ECL2).
28467637	3	46	gly	N-glycosylation	315:329	arg2	Asn6					338:341	Asn6	338:341	Asn6	338:341	β2 adrenergic receptor (β2 AR) has three N-glycosylation sites: Asn6, Asn15 at the N-terminus, and Asn187 at the second extracellular loop (ECL2).
28467637	3	46	gly	N-glycosylation	315:329	arg2	Asn187					373:378	Asn187	373:378	Asn187	373:378	β2 adrenergic receptor (β2 AR) has three N-glycosylation sites: Asn6, Asn15 at the N-terminus, and Asn187 at the second extracellular loop (ECL2).
28467637	9	47	theme	Glu338	1151:1156	arg1	Studies					1130:1136	Studies	1130:1136	Studies of Lys60 and Glu338	1130:1156	Studies of Lys60 and Glu338, two residues at the receptor dimerization interface, exhibited that the K60A/E338A showed decreased β2 AR dimerization and its effects on receptor signaling were similar to N6Q and N15Q, which further supported the importance of receptor dimerization for receptor function.
28467637	9	47	theme	Glu338	1151:1156	arg1	residues					1163:1170	two residues	1159:1170	two residues at the receptor dimerization interface	1159:1209	Studies of Lys60 and Glu338, two residues at the receptor dimerization interface, exhibited that the K60A/E338A showed decreased β2 AR dimerization and its effects on receptor signaling were similar to N6Q and N15Q, which further supported the importance of receptor dimerization for receptor function.
28467637	1	48	theme	common	123:128	arg1	modification					149:160	a common post-translational modification	121:160	a common post-translational modification of G-protein-coupled receptors (GPCRs)	121:199	N-glycosylation is a common post-translational modification of G-protein-coupled receptors (GPCRs).
28467637	1	48	theme	common	123:128	arg1	N-glycosylation					102:116	N-glycosylation	102:116	N-glycosylation	102:116	N-glycosylation is a common post-translational modification of G-protein-coupled receptors (GPCRs).
28467637	3	49	theme	extracellular	394:406	arg1	ECL2					414:417	ECL2	414:417	ECL2	414:417	β2 adrenergic receptor (β2 AR) has three N-glycosylation sites: Asn6, Asn15 at the N-terminus, and Asn187 at the second extracellular loop (ECL2).
28467637	3	49	theme	extracellular	394:406	arg1	loop					408:411	the second extracellular loop	383:411	the second extracellular loop (ECL2)	383:418	β2 adrenergic receptor (β2 AR) has three N-glycosylation sites: Asn6, Asn15 at the N-terminus, and Asn187 at the second extracellular loop (ECL2).
28467637	1	50	theme	post-translational	130:147	arg1	modification					149:160	a common post-translational modification	121:160	a common post-translational modification of G-protein-coupled receptors (GPCRs)	121:199	N-glycosylation is a common post-translational modification of G-protein-coupled receptors (GPCRs).
28467637	1	50	theme	post-translational	130:147	arg1	N-glycosylation					102:116	N-glycosylation	102:116	N-glycosylation	102:116	N-glycosylation is a common post-translational modification of G-protein-coupled receptors (GPCRs).
28467637	10	51	gly	glycosylation	1493:1505	arg1	GPCRs					1538:1542	GPCRs	1538:1542	GPCRs	1538:1542	This work provides new insights into the relationship among glycosylation, dimerization, and function of GPCRs.
28467637	4	52	theme	ligand	504:509	arg1	binding					511:517	ligand binding	504:517	ligand binding	504:517	Here, we show that deletion of the N-glycan did not affect receptor expression and ligand binding.
28467637	10	53	theme	GPCRs	1538:1542	arg1	dimerization					1508:1519	dimerization	1508:1519	dimerization	1508:1519	This work provides new insights into the relationship among glycosylation, dimerization, and function of GPCRs.
28467637	10	53	theme	GPCRs	1538:1542	arg1	function					1526:1533	function	1526:1533	function	1526:1533	This work provides new insights into the relationship among glycosylation, dimerization, and function of GPCRs.
28467637	10	53	theme	GPCRs	1538:1542	arg1	glycosylation					1493:1505	glycosylation	1493:1505	glycosylation	1493:1505	This work provides new insights into the relationship among glycosylation, dimerization, and function of GPCRs.
28467637	7	54	theme	β2	958:959	arg1	AR					961:962	β2 AR	958:962	β2 AR	958:962	As decreased β2 AR homodimer accompanied with reduced efficiency for receptor function, we proposed that the N-glycosylation of β2 AR regulated receptor function by influencing receptor dimerization.
28467637	6	55	theme	receptor	754:761	arg1	dimerization					763:774	receptor dimerization	754:774	receptor dimerization	754:774	Both N6Q and N15Q showed decreased receptor dimerization, while N187Q did not influence receptor dimerization.
28467637	9	56	theme	dimerization	1397:1408	arg1	importance					1374:1383	the importance	1370:1383	the importance of receptor dimerization for receptor function	1370:1430	Studies of Lys60 and Glu338, two residues at the receptor dimerization interface, exhibited that the K60A/E338A showed decreased β2 AR dimerization and its effects on receptor signaling were similar to N6Q and N15Q, which further supported the importance of receptor dimerization for receptor function.
28467637	8	57	from	interface	1119:1127	arg1	residues					1090:1097	the residues	1086:1097	the residues at the dimerization interface	1086:1127	To verify this hypothesis, we further paid attention to the residues at the dimerization interface.
28467637	5	58	theme	receptor	693:700	arg1	internalization					702:716	receptor internalization	693:716	receptor internalization	693:716	Deletion of the N-glycan at the N-terminus rather than Asn187 showed decreased effects on isoproterenol-promoted G-protein-dependent signaling, β-arrestin2 recruitment, and receptor internalization.
28467637	11	59	dep	A	1625:1625	arg1	EC					1636:1637	EC 3.2.1.96	1636:1646	EC 3.2.1.96	1636:1646	Peptide-N-glycosidase F (PNGase F, EC 3.2.2.11); endo-β-N-acetylglucosaminidase A (Endo-A, EC 3.2.1.96).
28467637	11	59	dep	A	1625:1625	arg1	Endo-A					1628:1633	Endo-A	1628:1633	Endo-A	1628:1633	Peptide-N-glycosidase F (PNGase F, EC 3.2.2.11); endo-β-N-acetylglucosaminidase A (Endo-A, EC 3.2.1.96).
28467637	9	60	from	effects	1286:1292	arg1	signaling					1306:1314	receptor signaling	1297:1314	receptor signaling	1297:1314	Studies of Lys60 and Glu338, two residues at the receptor dimerization interface, exhibited that the K60A/E338A showed decreased β2 AR dimerization and its effects on receptor signaling were similar to N6Q and N15Q, which further supported the importance of receptor dimerization for receptor function.
28467637	1	61	theme	G-protein-coupled	165:181	arg1	receptors					183:191	G-protein-coupled receptors	165:191	G-protein-coupled receptors (GPCRs)	165:199	N-glycosylation is a common post-translational modification of G-protein-coupled receptors (GPCRs).
28467637	1	61	theme	G-protein-coupled	165:181	arg1	GPCRs					194:198	GPCRs	194:198	GPCRs	194:198	N-glycosylation is a common post-translational modification of G-protein-coupled receptors (GPCRs).
28467637	6	62	dep	showed	737:742	arg1	decreased					744:752	decreased	744:752	decreased	744:752	Both N6Q and N15Q showed decreased receptor dimerization, while N187Q did not influence receptor dimerization.
28467637	9	63	theme	receptor	1414:1421	arg1	function					1423:1430	receptor function	1414:1430	receptor function	1414:1430	Studies of Lys60 and Glu338, two residues at the receptor dimerization interface, exhibited that the K60A/E338A showed decreased β2 AR dimerization and its effects on receptor signaling were similar to N6Q and N15Q, which further supported the importance of receptor dimerization for receptor function.
28467637	0	64	theme	receptor	56:63	arg1	function					65:72	receptor function	56:72	receptor function	56:72	N-glycosylation of the β2 adrenergic receptor regulates receptor function by modulating dimerization.
28467637	9	65	theme	receptor	1297:1304	arg1	signaling					1306:1314	receptor signaling	1297:1314	receptor signaling	1297:1314	Studies of Lys60 and Glu338, two residues at the receptor dimerization interface, exhibited that the K60A/E338A showed decreased β2 AR dimerization and its effects on receptor signaling were similar to N6Q and N15Q, which further supported the importance of receptor dimerization for receptor function.
28467637	2	66	gly	N-glycosylation	234:248	arg1	GPCR					258:261	GPCR signaling	258:271	GPCR signaling	258:271	However, it remains unknown how N-glycosylation affects GPCR signaling.
28467637	1	67	theme	receptors	183:191	arg1	modification					149:160	a common post-translational modification	121:160	a common post-translational modification of G-protein-coupled receptors (GPCRs)	121:199	N-glycosylation is a common post-translational modification of G-protein-coupled receptors (GPCRs).
28467637	1	67	theme	receptors	183:191	arg1	N-glycosylation					102:116	N-glycosylation	102:116	N-glycosylation	102:116	N-glycosylation is a common post-translational modification of G-protein-coupled receptors (GPCRs).
28467637	5	68	theme	isoproterenol-promoted	610:631	arg1	signaling					653:661	isoproterenol-promoted G-protein-dependent signaling	610:661	isoproterenol-promoted G-protein-dependent signaling	610:661	Deletion of the N-glycan at the N-terminus rather than Asn187 showed decreased effects on isoproterenol-promoted G-protein-dependent signaling, β-arrestin2 recruitment, and receptor internalization.
28467637	7	69	gly	N-glycosylation	939:953	arg1	AR					961:962	β2 AR	958:962	β2 AR	958:962	As decreased β2 AR homodimer accompanied with reduced efficiency for receptor function, we proposed that the N-glycosylation of β2 AR regulated receptor function by influencing receptor dimerization.
18061361	9	0	theme	protein	1657:1663	arg1	MW					1632:1633	approximately the predicted MW	1604:1633	approximately the predicted MW of the unglycosylated protein	1604:1663	PNGase F reduces the molecular weight (MW) of natural NCBE in mouse brain or human NCBE expressed in oocytes to approximately the predicted MW of the unglycosylated protein.
18061361	8	1	theme	rat	1432:1434	arg1	brain					1436:1440	mouse and rat brain	1422:1440	brain	1436:1440	By Western blot, nearly all NCBE in mouse and rat brain is highly N-glycosylated (approximately 150 kDa).
18061361	2	2	theme	human	514:518	arg1	NCBE					520:523	human NCBE	514:523	human NCBE	514:523	Here we characterize a new antibody that was generated in rabbit against a fusion protein consisting of maltose-binding protein and the first 135 amino acids (aa) of the N-terminus of human NCBE.
18061361	6	3	attach	present	1161:1167	arg1	plexus					1247:1252	the basolateral membrane of embryonic day 18 (E18) fetal and adult choroid plexus	1172:1252	the basolateral membrane of embryonic day 18 (E18) fetal and adult choroid plexus	1172:1252	Immunocytochemistry shows that NCBE is present at the basolateral membrane of embryonic day 18 (E18) fetal and adult choroid plexus.
18061361	6	3	attach	present	1161:1167	arg2	NCBE					1153:1156	NCBE	1153:1156	NCBE	1153:1156	Immunocytochemistry shows that NCBE is present at the basolateral membrane of embryonic day 18 (E18) fetal and adult choroid plexus.
18061361	7	4	from	neurons	1358:1364	arg1	present					1271:1277	present	1271:1277	present	1271:1277	NCBE protein is present by Western blot and immunocytochemistry in cultured and freshly dissociated HC neurons but not astrocytes.
18061361	3	5	theme	full-length	643:653	arg1	transporters					655:666	full-length transporters	643:666	full-length transporters expressed in Xenopus	643:687	Western blotting--both of purified peptides representing the initial approximately 120 aa of the transporters and of full-length transporters expressed in Xenopus oocytes--demonstrated that the antibody is specific for NCBE versus the two most closely related proteins, NDCBE (SLC4A8) and NBCn1 (SLC4A7).
18061361	9	6	gly	unglycosylated	1642:1655	arg1	protein					1657:1663	the unglycosylated protein	1638:1663	the unglycosylated protein	1638:1663	PNGase F reduces the molecular weight (MW) of natural NCBE in mouse brain or human NCBE expressed in oocytes to approximately the predicted MW of the unglycosylated protein.
18061361	8	7	gly	N-glycosylated	1452:1465	arg1	NCBE					1414:1417	nearly all NCBE	1403:1417	nearly all NCBE in mouse and rat brain	1403:1440	By Western blot, nearly all NCBE in mouse and rat brain is highly N-glycosylated (approximately 150 kDa).
18061361	7	8	from	present	1271:1277	arg1	neurons					1358:1364	freshly dissociated HC neurons	1335:1364	freshly dissociated HC neurons	1335:1364	NCBE protein is present by Western blot and immunocytochemistry in cultured and freshly dissociated HC neurons but not astrocytes.
18061361	7	8	from	present	1271:1277	arg1	astrocytes					1374:1383	astrocytes	1374:1383	astrocytes	1374:1383	NCBE protein is present by Western blot and immunocytochemistry in cultured and freshly dissociated HC neurons but not astrocytes.
18061361	7	8	from	present	1271:1277	arg1	cultured					1322:1329	cultured	1322:1329	cultured	1322:1329	NCBE protein is present by Western blot and immunocytochemistry in cultured and freshly dissociated HC neurons but not astrocytes.
18061361	9	9	theme	PNGase	1492:1497	arg1	F					1499:1499	PNGase F	1492:1499	PNGase F	1492:1499	PNGase F reduces the molecular weight (MW) of natural NCBE in mouse brain or human NCBE expressed in oocytes to approximately the predicted MW of the unglycosylated protein.
18061361	10	10	theme	N-glycosylation	1718:1732	arg1	sites					1734:1738	the three consensus N-glycosylation sites	1698:1738	the three consensus N-glycosylation sites	1698:1738	In oocytes, mutating any one of the three consensus N-glycosylation sites reduces glycosylation of the other two, and the triple mutant exhibits negligible functional expression.
18061361	0	11	theme	transporter	111:121	arg1	NCBE					123:126	the sodium-coupled bicarbonate transporter NCBE	80:126	the sodium-coupled bicarbonate transporter NCBE	80:126	Use of a new polyclonal antibody to study the distribution and glycosylation of the sodium-coupled bicarbonate transporter NCBE in rodent brain.
18061361	6	12	from	plexus	1247:1252	arg1	present					1161:1167	present	1161:1167	present	1161:1167	Immunocytochemistry shows that NCBE is present at the basolateral membrane of embryonic day 18 (E18) fetal and adult choroid plexus.
18061361	1	13	theme	SLC4	179:182	arg1	family					184:189	the SLC4 family	175:189	the SLC4 family of bicarbonate transporters, several of which play important roles in intracellular-pH regulation and transepithelial HCO(3)(-) transport	175:327	NCBE (SLC4A10) is a member of the SLC4 family of bicarbonate transporters, several of which play important roles in intracellular-pH regulation and transepithelial HCO(3)(-) transport.
18061361	9	14	theme	molecular	1513:1521	arg1	weight					1523:1528	the molecular weight	1509:1528	the molecular weight (MW) of natural NCBE	1509:1549	PNGase F reduces the molecular weight (MW) of natural NCBE in mouse brain or human NCBE expressed in oocytes to approximately the predicted MW of the unglycosylated protein.
18061361	9	14	theme	molecular	1513:1521	arg1	MW					1531:1532	MW	1531:1532	MW	1531:1532	PNGase F reduces the molecular weight (MW) of natural NCBE in mouse brain or human NCBE expressed in oocytes to approximately the predicted MW of the unglycosylated protein.
18061361	7	15	located	present	1271:1277	arg2	protein					1260:1266	NCBE protein	1255:1266	NCBE protein	1255:1266	NCBE protein is present by Western blot and immunocytochemistry in cultured and freshly dissociated HC neurons but not astrocytes.
18061361	7	15	located	present	1271:1277	arg1	neurons					1358:1364	freshly dissociated HC neurons	1335:1364	freshly dissociated HC neurons	1335:1364	NCBE protein is present by Western blot and immunocytochemistry in cultured and freshly dissociated HC neurons but not astrocytes.
18061361	7	15	located	present	1271:1277	arg1	astrocytes					1374:1383	astrocytes	1374:1383	astrocytes	1374:1383	NCBE protein is present by Western blot and immunocytochemistry in cultured and freshly dissociated HC neurons but not astrocytes.
18061361	7	15	located	present	1271:1277	arg1	cultured					1322:1329	cultured	1322:1329	cultured	1322:1329	NCBE protein is present by Western blot and immunocytochemistry in cultured and freshly dissociated HC neurons but not astrocytes.
18061361	4	16	theme	Western	831:837	arg1	blotting					839:846	Western blotting	831:846	Western blotting of tissue in four regions of adult mouse brain	831:893	Western blotting of tissue in four regions of adult mouse brain indicates that NCBE is expressed most abundantly in cerebral cortex (CX), cerebellum (CB) and hippocampus (HC), and less so in subcortex (SCX).
18061361	5	17	theme	choroid	1106:1112	arg1	plexus					1114:1119	choroid plexus	1106:1119	choroid plexus	1106:1119	NCBE protein was present in CX, CB, and HC microdissected to avoid choroid plexus.
18061361	3	18	theme	purified	552:559	arg1	peptides					561:568	purified peptides	552:568	purified peptides representing the initial approximately 120 aa	552:614	Western blotting--both of purified peptides representing the initial approximately 120 aa of the transporters and of full-length transporters expressed in Xenopus oocytes--demonstrated that the antibody is specific for NCBE versus the two most closely related proteins, NDCBE (SLC4A8) and NBCn1 (SLC4A7).
18061361	4	19	theme	brain	889:893	arg1	regions					866:872	four regions	861:872	four regions of adult mouse brain	861:893	Western blotting of tissue in four regions of adult mouse brain indicates that NCBE is expressed most abundantly in cerebral cortex (CX), cerebellum (CB) and hippocampus (HC), and less so in subcortex (SCX).
18061361	1	20	theme	HCO	309:311	arg1	transport					319:327	transepithelial HCO(3)(-) transport	293:327	transepithelial HCO(3)(-) transport	293:327	NCBE (SLC4A10) is a member of the SLC4 family of bicarbonate transporters, several of which play important roles in intracellular-pH regulation and transepithelial HCO(3)(-) transport.
18061361	9	21	theme	natural	1538:1544	arg1	NCBE					1546:1549	natural NCBE	1538:1549	natural NCBE	1538:1549	PNGase F reduces the molecular weight (MW) of natural NCBE in mouse brain or human NCBE expressed in oocytes to approximately the predicted MW of the unglycosylated protein.
18061361	10	22	theme	two	1775:1777	arg1	glycosylation					1748:1760	glycosylation	1748:1760	glycosylation of the other two	1748:1777	In oocytes, mutating any one of the three consensus N-glycosylation sites reduces glycosylation of the other two, and the triple mutant exhibits negligible functional expression.
18061361	3	23	theme	related	778:784	arg1	NBCn1					815:819	NBCn1	815:819	NBCn1 (SLC4A7)	815:828	Western blotting--both of purified peptides representing the initial approximately 120 aa of the transporters and of full-length transporters expressed in Xenopus oocytes--demonstrated that the antibody is specific for NCBE versus the two most closely related proteins, NDCBE (SLC4A8) and NBCn1 (SLC4A7).
18061361	3	23	theme	related	778:784	arg1	NDCBE					796:800	NDCBE	796:800	NDCBE (SLC4A8)	796:809	Western blotting--both of purified peptides representing the initial approximately 120 aa of the transporters and of full-length transporters expressed in Xenopus oocytes--demonstrated that the antibody is specific for NCBE versus the two most closely related proteins, NDCBE (SLC4A8) and NBCn1 (SLC4A7).
18061361	3	23	theme	related	778:784	arg1	proteins					786:793	the two most closely related proteins	757:793	the two most closely related proteins	757:793	Western blotting--both of purified peptides representing the initial approximately 120 aa of the transporters and of full-length transporters expressed in Xenopus oocytes--demonstrated that the antibody is specific for NCBE versus the two most closely related proteins, NDCBE (SLC4A8) and NBCn1 (SLC4A7).
18061361	6	24	theme	day	1210:1212	arg1	membrane					1188:1195	the basolateral membrane	1172:1195	the basolateral membrane of embryonic day 18	1172:1215	Immunocytochemistry shows that NCBE is present at the basolateral membrane of embryonic day 18 (E18) fetal and adult choroid plexus.
18061361	4	25	theme	adult	877:881	arg1	brain					889:893	adult mouse brain	877:893	adult mouse brain	877:893	Western blotting of tissue in four regions of adult mouse brain indicates that NCBE is expressed most abundantly in cerebral cortex (CX), cerebellum (CB) and hippocampus (HC), and less so in subcortex (SCX).
18061361	0	26	theme	sodium-coupled	84:97	arg1	NCBE					123:126	the sodium-coupled bicarbonate transporter NCBE	80:126	the sodium-coupled bicarbonate transporter NCBE	80:126	Use of a new polyclonal antibody to study the distribution and glycosylation of the sodium-coupled bicarbonate transporter NCBE in rodent brain.
18061361	0	27	theme	antibody	24:31	arg1	Use					0:2	Use	0:2	Use of a new polyclonal antibody to study the distribution and glycosylation of the sodium-coupled bicarbonate transporter NCBE in rodent brain.	0:143	Use of a new polyclonal antibody to study the distribution and glycosylation of the sodium-coupled bicarbonate transporter NCBE in rodent brain.
18061361	0	28	gly	glycosylation	63:75	arg1	NCBE					123:126	the sodium-coupled bicarbonate transporter NCBE	80:126	the sodium-coupled bicarbonate transporter NCBE	80:126	Use of a new polyclonal antibody to study the distribution and glycosylation of the sodium-coupled bicarbonate transporter NCBE in rodent brain.
18061361	0	28	gly	glycosylation	63:75	arg1	brain					138:142	rodent brain	131:142	rodent brain	131:142	Use of a new polyclonal antibody to study the distribution and glycosylation of the sodium-coupled bicarbonate transporter NCBE in rodent brain.
18061361	9	29	theme	human	1569:1573	arg1	NCBE					1575:1578	human NCBE	1569:1578	human NCBE	1569:1578	PNGase F reduces the molecular weight (MW) of natural NCBE in mouse brain or human NCBE expressed in oocytes to approximately the predicted MW of the unglycosylated protein.
18061361	6	30	theme	choroid	1239:1245	arg1	plexus					1247:1252	the basolateral membrane of embryonic day 18 (E18) fetal and adult choroid plexus	1172:1252	the basolateral membrane of embryonic day 18 (E18) fetal and adult choroid plexus	1172:1252	Immunocytochemistry shows that NCBE is present at the basolateral membrane of embryonic day 18 (E18) fetal and adult choroid plexus.
18061361	7	31	from	astrocytes	1374:1383	arg1	present					1271:1277	present	1271:1277	present	1271:1277	NCBE protein is present by Western blot and immunocytochemistry in cultured and freshly dissociated HC neurons but not astrocytes.
18061361	10	32	gly	N-glycosylation	1718:1732	arg2	three					1702:1706	three	1702:1706	three	1702:1706	In oocytes, mutating any one of the three consensus N-glycosylation sites reduces glycosylation of the other two, and the triple mutant exhibits negligible functional expression.
18061361	10	32	gly	N-glycosylation	1718:1732	arg2	sites					1734:1738	the three consensus N-glycosylation sites	1698:1738	the three consensus N-glycosylation sites	1698:1738	In oocytes, mutating any one of the three consensus N-glycosylation sites reduces glycosylation of the other two, and the triple mutant exhibits negligible functional expression.
18061361	3	33	theme	initial	587:593	arg1	aa					613:614	the initial approximately 120 aa	583:614	the initial approximately 120 aa	583:614	Western blotting--both of purified peptides representing the initial approximately 120 aa of the transporters and of full-length transporters expressed in Xenopus oocytes--demonstrated that the antibody is specific for NCBE versus the two most closely related proteins, NDCBE (SLC4A8) and NBCn1 (SLC4A7).
18061361	2	34	theme	new	353:355	arg1	antibody					357:364	a new antibody	351:364	a new antibody that was generated in rabbit against a fusion protein consisting of maltose-binding protein and the first 135 amino acids (aa) of the N-terminus of human NCBE	351:523	Here we characterize a new antibody that was generated in rabbit against a fusion protein consisting of maltose-binding protein and the first 135 amino acids (aa) of the N-terminus of human NCBE.
18061361	0	35	theme	polyclonal	13:22	arg1	antibody					24:31	a new polyclonal antibody	7:31	a new polyclonal antibody to study the distribution and glycosylation of the sodium-coupled bicarbonate transporter NCBE in rodent brain	7:142	Use of a new polyclonal antibody to study the distribution and glycosylation of the sodium-coupled bicarbonate transporter NCBE in rodent brain.
18061361	1	36	theme	intracellular-pH	261:276	arg1	regulation					278:287	intracellular-pH regulation	261:287	intracellular-pH regulation	261:287	NCBE (SLC4A10) is a member of the SLC4 family of bicarbonate transporters, several of which play important roles in intracellular-pH regulation and transepithelial HCO(3)(-) transport.
18061361	7	37	theme	dissociated	1343:1353	arg1	neurons					1358:1364	freshly dissociated HC neurons	1335:1364	freshly dissociated HC neurons	1335:1364	NCBE protein is present by Western blot and immunocytochemistry in cultured and freshly dissociated HC neurons but not astrocytes.
18061361	8	38	theme	Western	1389:1395	arg1	blot					1397:1400	Western blot	1389:1400	Western blot	1389:1400	By Western blot, nearly all NCBE in mouse and rat brain is highly N-glycosylated (approximately 150 kDa).
18061361	2	39	theme	maltose-binding	434:448	arg1	protein					450:456	maltose-binding protein	434:456	maltose-binding protein	434:456	Here we characterize a new antibody that was generated in rabbit against a fusion protein consisting of maltose-binding protein and the first 135 amino acids (aa) of the N-terminus of human NCBE.
18061361	9	40	theme	predicted	1622:1630	arg1	MW					1632:1633	approximately the predicted MW	1604:1633	approximately the predicted MW of the unglycosylated protein	1604:1663	PNGase F reduces the molecular weight (MW) of natural NCBE in mouse brain or human NCBE expressed in oocytes to approximately the predicted MW of the unglycosylated protein.
18061361	1	41	theme	family	184:189	arg1	NCBE					145:148	NCBE	145:148	NCBE (SLC4A10)	145:158	NCBE (SLC4A10) is a member of the SLC4 family of bicarbonate transporters, several of which play important roles in intracellular-pH regulation and transepithelial HCO(3)(-) transport.
18061361	1	41	theme	family	184:189	arg1	member					165:170	a member	163:170	a member of the SLC4 family of bicarbonate transporters, several of which play important roles in intracellular-pH regulation and transepithelial HCO(3)(-) transport	163:327	NCBE (SLC4A10) is a member of the SLC4 family of bicarbonate transporters, several of which play important roles in intracellular-pH regulation and transepithelial HCO(3)(-) transport.
18061361	8	42	theme	all	1410:1412	arg1	NCBE					1414:1417	nearly all NCBE	1403:1417	nearly all NCBE in mouse and rat brain	1403:1440	By Western blot, nearly all NCBE in mouse and rat brain is highly N-glycosylated (approximately 150 kDa).
18061361	1	43	theme	bicarbonate	194:204	arg1	transporters					206:217	bicarbonate transporters	194:217	bicarbonate transporters	194:217	NCBE (SLC4A10) is a member of the SLC4 family of bicarbonate transporters, several of which play important roles in intracellular-pH regulation and transepithelial HCO(3)(-) transport.
18061361	7	44	from	cultured	1322:1329	arg1	present					1271:1277	present	1271:1277	present	1271:1277	NCBE protein is present by Western blot and immunocytochemistry in cultured and freshly dissociated HC neurons but not astrocytes.
18061361	5	45	located	present	1056:1062	arg2	protein					1044:1050	NCBE protein	1039:1050	NCBE protein	1039:1050	NCBE protein was present in CX, CB, and HC microdissected to avoid choroid plexus.
18061361	5	45	located	present	1056:1062	arg1	CB					1071:1072	CB	1071:1072	CB	1071:1072	NCBE protein was present in CX, CB, and HC microdissected to avoid choroid plexus.
18061361	5	45	located	present	1056:1062	arg1	HC					1079:1080	HC	1079:1080	HC	1079:1080	NCBE protein was present in CX, CB, and HC microdissected to avoid choroid plexus.
18061361	5	45	located	present	1056:1062	arg1	CX					1067:1068	CX	1067:1068	CX	1067:1068	NCBE protein was present in CX, CB, and HC microdissected to avoid choroid plexus.
18061361	9	46	theme	unglycosylated	1642:1655	arg1	protein					1657:1663	the unglycosylated protein	1638:1663	the unglycosylated protein	1638:1663	PNGase F reduces the molecular weight (MW) of natural NCBE in mouse brain or human NCBE expressed in oocytes to approximately the predicted MW of the unglycosylated protein.
18061361	7	47	theme	Western	1282:1288	arg1	blot					1290:1293	Western blot	1282:1293	Western blot	1282:1293	NCBE protein is present by Western blot and immunocytochemistry in cultured and freshly dissociated HC neurons but not astrocytes.
18061361	2	48	theme	NCBE	520:523	arg1	N-terminus					500:509	the N-terminus	496:509	the N-terminus of human NCBE	496:523	Here we characterize a new antibody that was generated in rabbit against a fusion protein consisting of maltose-binding protein and the first 135 amino acids (aa) of the N-terminus of human NCBE.
18061361	3	49	theme	transporters	623:634	arg1	blotting--both					534:547	Western blotting--both	526:547	Western blotting--both of purified peptides representing the initial approximately 120 aa of the transporters and of full-length transporters expressed in Xenopus	526:687	Western blotting--both of purified peptides representing the initial approximately 120 aa of the transporters and of full-length transporters expressed in Xenopus oocytes--demonstrated that the antibody is specific for NCBE versus the two most closely related proteins, NDCBE (SLC4A8) and NBCn1 (SLC4A7).
18061361	4	50	from	regions	866:872	arg1	blotting					839:846	Western blotting	831:846	Western blotting of tissue in four regions of adult mouse brain	831:893	Western blotting of tissue in four regions of adult mouse brain indicates that NCBE is expressed most abundantly in cerebral cortex (CX), cerebellum (CB) and hippocampus (HC), and less so in subcortex (SCX).
18061361	7	51	theme	NCBE	1255:1258	arg1	protein					1260:1266	NCBE protein	1255:1266	NCBE protein	1255:1266	NCBE protein is present by Western blot and immunocytochemistry in cultured and freshly dissociated HC neurons but not astrocytes.
18061361	10	52	theme	negligible	1811:1820	arg1	expression					1833:1842	negligible functional expression	1811:1842	negligible functional expression	1811:1842	In oocytes, mutating any one of the three consensus N-glycosylation sites reduces glycosylation of the other two, and the triple mutant exhibits negligible functional expression.
18061361	5	53	from	HC	1079:1080	arg1	present					1056:1062	present	1056:1062	present	1056:1062	NCBE protein was present in CX, CB, and HC microdissected to avoid choroid plexus.
18061361	3	54	theme	transporters	655:666	arg1	blotting--both					534:547	Western blotting--both	526:547	Western blotting--both of purified peptides representing the initial approximately 120 aa of the transporters and of full-length transporters expressed in Xenopus	526:687	Western blotting--both of purified peptides representing the initial approximately 120 aa of the transporters and of full-length transporters expressed in Xenopus oocytes--demonstrated that the antibody is specific for NCBE versus the two most closely related proteins, NDCBE (SLC4A8) and NBCn1 (SLC4A7).
18061361	10	55	theme	sites	1734:1738	arg1	sites					1734:1738	the three consensus N-glycosylation sites	1698:1738	the three consensus N-glycosylation sites	1698:1738	In oocytes, mutating any one of the three consensus N-glycosylation sites reduces glycosylation of the other two, and the triple mutant exhibits negligible functional expression.
18061361	10	55	theme	sites	1734:1738	arg1	one					1691:1693	one	1691:1693	one	1691:1693	In oocytes, mutating any one of the three consensus N-glycosylation sites reduces glycosylation of the other two, and the triple mutant exhibits negligible functional expression.
18061361	0	56	theme	NCBE	123:126	arg1	glycosylation					63:75	glycosylation	63:75	glycosylation	63:75	Use of a new polyclonal antibody to study the distribution and glycosylation of the sodium-coupled bicarbonate transporter NCBE in rodent brain.
18061361	0	56	theme	NCBE	123:126	arg1	distribution					46:57	distribution	46:57	distribution	46:57	Use of a new polyclonal antibody to study the distribution and glycosylation of the sodium-coupled bicarbonate transporter NCBE in rodent brain.
18061361	0	57	from	glycosylation	63:75	arg1	brain					138:142	rodent brain	131:142	rodent brain	131:142	Use of a new polyclonal antibody to study the distribution and glycosylation of the sodium-coupled bicarbonate transporter NCBE in rodent brain.
18061361	10	58	theme	consensus	1708:1716	arg1	sites					1734:1738	the three consensus N-glycosylation sites	1698:1738	the three consensus N-glycosylation sites	1698:1738	In oocytes, mutating any one of the three consensus N-glycosylation sites reduces glycosylation of the other two, and the triple mutant exhibits negligible functional expression.
18061361	8	59	from	NCBE	1414:1417	arg1	brain					1436:1440	mouse and rat brain	1422:1440	brain	1436:1440	By Western blot, nearly all NCBE in mouse and rat brain is highly N-glycosylated (approximately 150 kDa).
18061361	4	60	from	tissue	851:856	arg1	regions					866:872	four regions	861:872	four regions of adult mouse brain	861:893	Western blotting of tissue in four regions of adult mouse brain indicates that NCBE is expressed most abundantly in cerebral cortex (CX), cerebellum (CB) and hippocampus (HC), and less so in subcortex (SCX).
18061361	4	61	theme	tissue	851:856	arg1	blotting					839:846	Western blotting	831:846	Western blotting of tissue in four regions of adult mouse brain	831:893	Western blotting of tissue in four regions of adult mouse brain indicates that NCBE is expressed most abundantly in cerebral cortex (CX), cerebellum (CB) and hippocampus (HC), and less so in subcortex (SCX).
18061361	0	62	from	distribution	46:57	arg1	brain					138:142	rodent brain	131:142	rodent brain	131:142	Use of a new polyclonal antibody to study the distribution and glycosylation of the sodium-coupled bicarbonate transporter NCBE in rodent brain.
18061361	5	63	from	CB	1071:1072	arg1	present					1056:1062	present	1056:1062	present	1056:1062	NCBE protein was present in CX, CB, and HC microdissected to avoid choroid plexus.
18061361	4	64	from	blotting	839:846	arg1	regions					866:872	four regions	861:872	four regions of adult mouse brain	861:893	Western blotting of tissue in four regions of adult mouse brain indicates that NCBE is expressed most abundantly in cerebral cortex (CX), cerebellum (CB) and hippocampus (HC), and less so in subcortex (SCX).
18061361	5	65	from	present	1056:1062	arg1	CB					1071:1072	CB	1071:1072	CB	1071:1072	NCBE protein was present in CX, CB, and HC microdissected to avoid choroid plexus.
18061361	5	65	from	present	1056:1062	arg1	HC					1079:1080	HC	1079:1080	HC	1079:1080	NCBE protein was present in CX, CB, and HC microdissected to avoid choroid plexus.
18061361	5	65	from	present	1056:1062	arg1	CX					1067:1068	CX	1067:1068	CX	1067:1068	NCBE protein was present in CX, CB, and HC microdissected to avoid choroid plexus.
18061361	5	66	from	CX	1067:1068	arg1	present					1056:1062	present	1056:1062	present	1056:1062	NCBE protein was present in CX, CB, and HC microdissected to avoid choroid plexus.
18061361	3	67	theme	Western	526:532	arg1	blotting--both					534:547	Western blotting--both	526:547	Western blotting--both of purified peptides representing the initial approximately 120 aa of the transporters and of full-length transporters expressed in Xenopus	526:687	Western blotting--both of purified peptides representing the initial approximately 120 aa of the transporters and of full-length transporters expressed in Xenopus oocytes--demonstrated that the antibody is specific for NCBE versus the two most closely related proteins, NDCBE (SLC4A8) and NBCn1 (SLC4A7).
18061361	4	68	theme	mouse	883:887	arg1	brain					889:893	adult mouse brain	877:893	adult mouse brain	877:893	Western blotting of tissue in four regions of adult mouse brain indicates that NCBE is expressed most abundantly in cerebral cortex (CX), cerebellum (CB) and hippocampus (HC), and less so in subcortex (SCX).
18061361	5	69	attach	present	1056:1062	arg2	protein					1044:1050	NCBE protein	1039:1050	NCBE protein	1039:1050	NCBE protein was present in CX, CB, and HC microdissected to avoid choroid plexus.
18061361	5	69	attach	present	1056:1062	arg1	CB					1071:1072	CB	1071:1072	CB	1071:1072	NCBE protein was present in CX, CB, and HC microdissected to avoid choroid plexus.
18061361	5	69	attach	present	1056:1062	arg1	HC					1079:1080	HC	1079:1080	HC	1079:1080	NCBE protein was present in CX, CB, and HC microdissected to avoid choroid plexus.
18061361	5	69	attach	present	1056:1062	arg1	CX					1067:1068	CX	1067:1068	CX	1067:1068	NCBE protein was present in CX, CB, and HC microdissected to avoid choroid plexus.
18061361	8	70	dep	N-glycosylated	1452:1465	arg1	kDa					1486:1488	approximately 150 kDa	1468:1488	approximately 150 kDa	1468:1488	By Western blot, nearly all NCBE in mouse and rat brain is highly N-glycosylated (approximately 150 kDa).
18061361	2	71	theme	first	466:470	arg1	aa					489:490	aa	489:490	aa	489:490	Here we characterize a new antibody that was generated in rabbit against a fusion protein consisting of maltose-binding protein and the first 135 amino acids (aa) of the N-terminus of human NCBE.
18061361	2	71	theme	first	466:470	arg1	acids					482:486	the first 135 amino acids	462:486	the first 135 amino acids (aa)	462:491	Here we characterize a new antibody that was generated in rabbit against a fusion protein consisting of maltose-binding protein and the first 135 amino acids (aa) of the N-terminus of human NCBE.
18061361	9	72	theme	NCBE	1546:1549	arg1	weight					1523:1528	the molecular weight	1509:1528	the molecular weight (MW) of natural NCBE	1509:1549	PNGase F reduces the molecular weight (MW) of natural NCBE in mouse brain or human NCBE expressed in oocytes to approximately the predicted MW of the unglycosylated protein.
18061361	9	72	theme	NCBE	1546:1549	arg1	MW					1531:1532	MW	1531:1532	MW	1531:1532	PNGase F reduces the molecular weight (MW) of natural NCBE in mouse brain or human NCBE expressed in oocytes to approximately the predicted MW of the unglycosylated protein.
18061361	6	73	theme	embryonic	1200:1208	arg1	day					1210:1212	embryonic day 18	1200:1215	embryonic day 18	1200:1215	Immunocytochemistry shows that NCBE is present at the basolateral membrane of embryonic day 18 (E18) fetal and adult choroid plexus.
18061361	6	74	located	present	1161:1167	arg1	plexus					1247:1252	the basolateral membrane of embryonic day 18 (E18) fetal and adult choroid plexus	1172:1252	the basolateral membrane of embryonic day 18 (E18) fetal and adult choroid plexus	1172:1252	Immunocytochemistry shows that NCBE is present at the basolateral membrane of embryonic day 18 (E18) fetal and adult choroid plexus.
18061361	6	74	located	present	1161:1167	arg2	NCBE					1153:1156	NCBE	1153:1156	NCBE	1153:1156	Immunocytochemistry shows that NCBE is present at the basolateral membrane of embryonic day 18 (E18) fetal and adult choroid plexus.
18061361	9	75	theme	mouse	1554:1558	arg1	brain					1560:1564	mouse brain	1554:1564	mouse brain	1554:1564	PNGase F reduces the molecular weight (MW) of natural NCBE in mouse brain or human NCBE expressed in oocytes to approximately the predicted MW of the unglycosylated protein.
18061361	10	76	theme	triple	1788:1793	arg1	mutant					1795:1800	the triple mutant	1784:1800	the triple mutant	1784:1800	In oocytes, mutating any one of the three consensus N-glycosylation sites reduces glycosylation of the other two, and the triple mutant exhibits negligible functional expression.
18061361	0	77	theme	bicarbonate	99:109	arg1	NCBE					123:126	the sodium-coupled bicarbonate transporter NCBE	80:126	the sodium-coupled bicarbonate transporter NCBE	80:126	Use of a new polyclonal antibody to study the distribution and glycosylation of the sodium-coupled bicarbonate transporter NCBE in rodent brain.
18061361	10	78	gly	glycosylation	1748:1760	arg1	oocytes					1669:1675	oocytes	1669:1675	oocytes	1669:1675	In oocytes, mutating any one of the three consensus N-glycosylation sites reduces glycosylation of the other two, and the triple mutant exhibits negligible functional expression.
18061361	10	78	gly	glycosylation	1748:1760	arg1	two					1775:1777	two	1775:1777	two	1775:1777	In oocytes, mutating any one of the three consensus N-glycosylation sites reduces glycosylation of the other two, and the triple mutant exhibits negligible functional expression.
18061361	0	79	theme	rodent	131:136	arg1	brain					138:142	rodent brain	131:142	rodent brain	131:142	Use of a new polyclonal antibody to study the distribution and glycosylation of the sodium-coupled bicarbonate transporter NCBE in rodent brain.
18061361	0	80	theme	new	9:11	arg1	antibody					24:31	a new polyclonal antibody	7:31	a new polyclonal antibody to study the distribution and glycosylation of the sodium-coupled bicarbonate transporter NCBE in rodent brain	7:142	Use of a new polyclonal antibody to study the distribution and glycosylation of the sodium-coupled bicarbonate transporter NCBE in rodent brain.
18061361	1	81	theme	important	242:250	arg1	roles					252:256	important roles	242:256	important roles	242:256	NCBE (SLC4A10) is a member of the SLC4 family of bicarbonate transporters, several of which play important roles in intracellular-pH regulation and transepithelial HCO(3)(-) transport.
18061361	6	82	dep	fetal	1223:1227	arg1	membrane					1188:1195	the basolateral membrane	1172:1195	the basolateral membrane of embryonic day 18	1172:1215	Immunocytochemistry shows that NCBE is present at the basolateral membrane of embryonic day 18 (E18) fetal and adult choroid plexus.
18061361	0	83	dep	distribution	46:57	arg1	the					42:44	the	42:44	the	42:44	Use of a new polyclonal antibody to study the distribution and glycosylation of the sodium-coupled bicarbonate transporter NCBE in rodent brain.
18061361	4	84	theme	cerebral	947:954	arg1	CX					964:965	CX	964:965	CX	964:965	Western blotting of tissue in four regions of adult mouse brain indicates that NCBE is expressed most abundantly in cerebral cortex (CX), cerebellum (CB) and hippocampus (HC), and less so in subcortex (SCX).
18061361	4	84	theme	cerebral	947:954	arg1	cortex					956:961	cerebral cortex	947:961	cerebral cortex (CX)	947:966	Western blotting of tissue in four regions of adult mouse brain indicates that NCBE is expressed most abundantly in cerebral cortex (CX), cerebellum (CB) and hippocampus (HC), and less so in subcortex (SCX).
18061361	6	85	theme	adult	1233:1237	arg1	plexus					1247:1252	the basolateral membrane of embryonic day 18 (E18) fetal and adult choroid plexus	1172:1252	the basolateral membrane of embryonic day 18 (E18) fetal and adult choroid plexus	1172:1252	Immunocytochemistry shows that NCBE is present at the basolateral membrane of embryonic day 18 (E18) fetal and adult choroid plexus.
18061361	5	86	theme	NCBE	1039:1042	arg1	protein					1044:1050	NCBE protein	1039:1050	NCBE protein	1039:1050	NCBE protein was present in CX, CB, and HC microdissected to avoid choroid plexus.
18061361	2	87	theme	fusion	405:410	arg1	protein					412:418	a fusion protein	403:418	a fusion protein consisting of maltose-binding protein and the first 135 amino acids (aa) of the N-terminus of human NCBE	403:523	Here we characterize a new antibody that was generated in rabbit against a fusion protein consisting of maltose-binding protein and the first 135 amino acids (aa) of the N-terminus of human NCBE.
18061361	3	88	theme	peptides	561:568	arg1	blotting--both					534:547	Western blotting--both	526:547	Western blotting--both of purified peptides representing the initial approximately 120 aa of the transporters and of full-length transporters expressed in Xenopus	526:687	Western blotting--both of purified peptides representing the initial approximately 120 aa of the transporters and of full-length transporters expressed in Xenopus oocytes--demonstrated that the antibody is specific for NCBE versus the two most closely related proteins, NDCBE (SLC4A8) and NBCn1 (SLC4A7).
18061361	6	89	theme	basolateral	1176:1186	arg1	membrane					1188:1195	the basolateral membrane	1172:1195	the basolateral membrane of embryonic day 18	1172:1215	Immunocytochemistry shows that NCBE is present at the basolateral membrane of embryonic day 18 (E18) fetal and adult choroid plexus.
18061361	6	90	theme	fetal	1223:1227	arg1	plexus					1247:1252	the basolateral membrane of embryonic day 18 (E18) fetal and adult choroid plexus	1172:1252	the basolateral membrane of embryonic day 18 (E18) fetal and adult choroid plexus	1172:1252	Immunocytochemistry shows that NCBE is present at the basolateral membrane of embryonic day 18 (E18) fetal and adult choroid plexus.
18061361	7	91	theme	HC	1355:1356	arg1	neurons					1358:1364	freshly dissociated HC neurons	1335:1364	freshly dissociated HC neurons	1335:1364	NCBE protein is present by Western blot and immunocytochemistry in cultured and freshly dissociated HC neurons but not astrocytes.
18061361	0	92	dep	antibody	24:31	arg1	study					36:40	study	36:40	to study the distribution and glycosylation of the sodium-coupled bicarbonate transporter NCBE in rodent brain	33:142	Use of a new polyclonal antibody to study the distribution and glycosylation of the sodium-coupled bicarbonate transporter NCBE in rodent brain.
18061361	2	93	theme	amino	476:480	arg1	aa					489:490	aa	489:490	aa	489:490	Here we characterize a new antibody that was generated in rabbit against a fusion protein consisting of maltose-binding protein and the first 135 amino acids (aa) of the N-terminus of human NCBE.
18061361	2	93	theme	amino	476:480	arg1	acids					482:486	the first 135 amino acids	462:486	the first 135 amino acids (aa)	462:491	Here we characterize a new antibody that was generated in rabbit against a fusion protein consisting of maltose-binding protein and the first 135 amino acids (aa) of the N-terminus of human NCBE.
18061361	7	94	attach	present	1271:1277	arg2	protein					1260:1266	NCBE protein	1255:1266	NCBE protein	1255:1266	NCBE protein is present by Western blot and immunocytochemistry in cultured and freshly dissociated HC neurons but not astrocytes.
18061361	7	94	attach	present	1271:1277	arg1	neurons					1358:1364	freshly dissociated HC neurons	1335:1364	freshly dissociated HC neurons	1335:1364	NCBE protein is present by Western blot and immunocytochemistry in cultured and freshly dissociated HC neurons but not astrocytes.
18061361	7	94	attach	present	1271:1277	arg1	astrocytes					1374:1383	astrocytes	1374:1383	astrocytes	1374:1383	NCBE protein is present by Western blot and immunocytochemistry in cultured and freshly dissociated HC neurons but not astrocytes.
18061361	7	94	attach	present	1271:1277	arg1	cultured					1322:1329	cultured	1322:1329	cultured	1322:1329	NCBE protein is present by Western blot and immunocytochemistry in cultured and freshly dissociated HC neurons but not astrocytes.
18061361	1	95	theme	transepithelial	293:307	arg1	transport					319:327	transepithelial HCO(3)(-) transport	293:327	transepithelial HCO(3)(-) transport	293:327	NCBE (SLC4A10) is a member of the SLC4 family of bicarbonate transporters, several of which play important roles in intracellular-pH regulation and transepithelial HCO(3)(-) transport.
18061361	10	96	theme	functional	1822:1831	arg1	expression					1833:1842	negligible functional expression	1811:1842	negligible functional expression	1811:1842	In oocytes, mutating any one of the three consensus N-glycosylation sites reduces glycosylation of the other two, and the triple mutant exhibits negligible functional expression.
18061361	8	97	theme	mouse	1422:1426	arg1	brain					1436:1440	mouse and rat brain	1422:1440	brain	1436:1440	By Western blot, nearly all NCBE in mouse and rat brain is highly N-glycosylated (approximately 150 kDa).
18061361	1	98	theme	transporters	206:217	arg1	several					220:226	several	220:226	several	220:226	NCBE (SLC4A10) is a member of the SLC4 family of bicarbonate transporters, several of which play important roles in intracellular-pH regulation and transepithelial HCO(3)(-) transport.
18061361	1	98	theme	transporters	206:217	arg1	family					184:189	the SLC4 family	175:189	the SLC4 family of bicarbonate transporters, several of which play important roles in intracellular-pH regulation and transepithelial HCO(3)(-) transport	175:327	NCBE (SLC4A10) is a member of the SLC4 family of bicarbonate transporters, several of which play important roles in intracellular-pH regulation and transepithelial HCO(3)(-) transport.
20729838	2	0	from	Mutations	195:203	arg1	K8					208:209	K8	208:209	K8	208:209	Mutations in K8 and K18 predispose the affected individual to liver disease as they protect hepatocytes from apoptosis.
20729838	2	0	from	Mutations	195:203	arg1	K18					215:217	K18	215:217	K18	215:217	Mutations in K8 and K18 predispose the affected individual to liver disease as they protect hepatocytes from apoptosis.
20729838	3	1	theme	dynamic	329:335	arg1	glycosylation					366:378	dynamic O-linked N-acetylglucosamine glycosylation	329:378	dynamic O-linked N-acetylglucosamine glycosylation	329:378	K18 undergoes dynamic O-linked N-acetylglucosamine glycosylation at Ser 30, 31 and 49.
20729838	6	2	theme	Akt1	973:976	arg1	inactivation					957:968	the inactivation	953:968	the inactivation of Akt1 and protein kinase Ctheta	953:1002	The enhanced apoptosis in the livers of mice that express K18-Gly(-) involves the inactivation of Akt1 and protein kinase Ctheta as a result of their site-specific hypophosphorylation.
20729838	6	2	theme	Akt1	973:976	arg1	result					1009:1014	a result	1007:1014	a result of their site-specific hypophosphorylation	1007:1057	The enhanced apoptosis in the livers of mice that express K18-Gly(-) involves the inactivation of Akt1 and protein kinase Ctheta as a result of their site-specific hypophosphorylation.
20729838	5	3	theme	K18-Gly	674:680	arg1	mice					685:688	K18-Gly(-) mice	674:688	K18-Gly(-) mice	674:688	K18-Gly(-) mice are more susceptible to liver and pancreatic injury and apoptosis induced by streptozotocin or to liver injury by combined N-acetyl-D-glucosaminidase inhibition and Fas administration.
20729838	6	4	theme	kinase	990:995	arg1	Ctheta					997:1002	protein kinase Ctheta	982:1002	protein kinase Ctheta	982:1002	The enhanced apoptosis in the livers of mice that express K18-Gly(-) involves the inactivation of Akt1 and protein kinase Ctheta as a result of their site-specific hypophosphorylation.
20729838	3	5	theme	O-linked	337:344	arg1	N-acetylglucosamine					346:364	O-linked N-acetylglucosamine	337:364	dynamic O-linked N-acetylglucosamine glycosylation	329:378	K18 undergoes dynamic O-linked N-acetylglucosamine glycosylation at Ser 30, 31 and 49.
20729838	6	6	theme	mice	915:918	arg1	livers					905:910	the livers	901:910	the livers of mice that express K18-Gly(-)	901:942	The enhanced apoptosis in the livers of mice that express K18-Gly(-) involves the inactivation of Akt1 and protein kinase Ctheta as a result of their site-specific hypophosphorylation.
20729838	7	7	theme	reciprocal	1112:1121	arg1	hyperglycosylation					1123:1140	reciprocal hyperglycosylation	1112:1140	reciprocal hyperglycosylation	1112:1140	Akt1 binds to K8, which probably contributes to the reciprocal hyperglycosylation and hypophosphorylation of Akt1 that occurs on K18 hypoglycosylation, and leads to decreased Akt1 kinase activity.
20729838	8	8	from	role	1315:1318	arg1	injury					1334:1339	epithelial injury	1323:1339	epithelial injury	1323:1339	Therefore, K18 glycosylation provides a unique protective role in epithelial injury by promoting the phosphorylation and activation of cell-survival kinases.
20729838	6	9	theme	protein	982:988	arg1	Ctheta					997:1002	protein kinase Ctheta	982:1002	protein kinase Ctheta	982:1002	The enhanced apoptosis in the livers of mice that express K18-Gly(-) involves the inactivation of Akt1 and protein kinase Ctheta as a result of their site-specific hypophosphorylation.
20729838	4	10	dep	glycosylated	545:556	arg1	K18-Gly					559:565	K18-Gly	559:565	K18-Gly	559:565	We investigated the function of K18 glycosylation by generating mice that overexpress human K18 S30/31/49A substitution mutants that cannot be glycosylated (K18-Gly(-)), and compared the susceptibility of these mice to injury with wild-type and other keratin-mutant mice.
20729838	4	11	theme	keratin-mutant	653:666	arg1	mice					668:671	wild-type and other keratin-mutant mice	633:671	wild-type and other keratin-mutant mice	633:671	We investigated the function of K18 glycosylation by generating mice that overexpress human K18 S30/31/49A substitution mutants that cannot be glycosylated (K18-Gly(-)), and compared the susceptibility of these mice to injury with wild-type and other keratin-mutant mice.
20729838	6	12	from	apoptosis	888:896	arg1	livers					905:910	the livers	901:910	the livers of mice that express K18-Gly(-)	901:942	The enhanced apoptosis in the livers of mice that express K18-Gly(-) involves the inactivation of Akt1 and protein kinase Ctheta as a result of their site-specific hypophosphorylation.
20729838	4	13	theme	K18	494:496	arg1	mutants					522:528	human K18 S30/31/49A substitution mutants	488:528	human K18 S30/31/49A substitution mutants that cannot be glycosylated (K18-Gly(-))	488:569	We investigated the function of K18 glycosylation by generating mice that overexpress human K18 S30/31/49A substitution mutants that cannot be glycosylated (K18-Gly(-)), and compared the susceptibility of these mice to injury with wild-type and other keratin-mutant mice.
20729838	7	14	theme	kinase	1240:1245	arg1	activity					1247:1254	decreased Akt1 kinase activity	1225:1254	decreased Akt1 kinase activity	1225:1254	Akt1 binds to K8, which probably contributes to the reciprocal hyperglycosylation and hypophosphorylation of Akt1 that occurs on K18 hypoglycosylation, and leads to decreased Akt1 kinase activity.
20729838	1	15	dep	Keratins	75:82	arg1	K18					101:103	K18	101:103	K18	101:103	Keratins 8 and 18 (K8 and K18) are heteropolymeric intermediate filament phosphoglycoproteins of simple-type epithelia.
20729838	1	15	dep	Keratins	75:82	arg1	K8					94:95	K8	94:95	K8	94:95	Keratins 8 and 18 (K8 and K18) are heteropolymeric intermediate filament phosphoglycoproteins of simple-type epithelia.
20729838	1	15	dep	Keratins	75:82	arg1	Keratins					75:82	Keratins 8 and 18	75:91	Keratins	75:82	Keratins 8 and 18 (K8 and K18) are heteropolymeric intermediate filament phosphoglycoproteins of simple-type epithelia.
20729838	7	16	theme	K18	1189:1191	arg1	hypoglycosylation					1193:1209	K18 hypoglycosylation	1189:1209	K18 hypoglycosylation	1189:1209	Akt1 binds to K8, which probably contributes to the reciprocal hyperglycosylation and hypophosphorylation of Akt1 that occurs on K18 hypoglycosylation, and leads to decreased Akt1 kinase activity.
20729838	4	17	theme	human	488:492	arg1	mutants					522:528	human K18 S30/31/49A substitution mutants	488:528	human K18 S30/31/49A substitution mutants that cannot be glycosylated (K18-Gly(-))	488:569	We investigated the function of K18 glycosylation by generating mice that overexpress human K18 S30/31/49A substitution mutants that cannot be glycosylated (K18-Gly(-)), and compared the susceptibility of these mice to injury with wild-type and other keratin-mutant mice.
20729838	7	18	dep	hyperglycosylation	1123:1140	arg1	the					1108:1110	the	1108:1110	the	1108:1110	Akt1 binds to K8, which probably contributes to the reciprocal hyperglycosylation and hypophosphorylation of Akt1 that occurs on K18 hypoglycosylation, and leads to decreased Akt1 kinase activity.
20729838	5	19	theme	liver	788:792	arg1	injury					794:799	liver injury	788:799	liver injury by combined N-acetyl-D-glucosaminidase inhibition and Fas administration	788:872	K18-Gly(-) mice are more susceptible to liver and pancreatic injury and apoptosis induced by streptozotocin or to liver injury by combined N-acetyl-D-glucosaminidase inhibition and Fas administration.
20729838	8	20	theme	K18	1268:1270	arg1	glycosylation					1272:1284	K18 glycosylation	1268:1284	K18 glycosylation	1268:1284	Therefore, K18 glycosylation provides a unique protective role in epithelial injury by promoting the phosphorylation and activation of cell-survival kinases.
20729838	1	21	theme	simple-type	172:182	arg1	epithelia					184:192	simple-type epithelia	172:192	simple-type epithelia	172:192	Keratins 8 and 18 (K8 and K18) are heteropolymeric intermediate filament phosphoglycoproteins of simple-type epithelia.
20729838	5	22	theme	pancreatic	724:733	arg1	injury					735:740	pancreatic injury	724:740	pancreatic injury	724:740	K18-Gly(-) mice are more susceptible to liver and pancreatic injury and apoptosis induced by streptozotocin or to liver injury by combined N-acetyl-D-glucosaminidase inhibition and Fas administration.
20729838	4	23	theme	substitution	509:520	arg1	mutants					522:528	human K18 S30/31/49A substitution mutants	488:528	human K18 S30/31/49A substitution mutants that cannot be glycosylated (K18-Gly(-))	488:569	We investigated the function of K18 glycosylation by generating mice that overexpress human K18 S30/31/49A substitution mutants that cannot be glycosylated (K18-Gly(-)), and compared the susceptibility of these mice to injury with wild-type and other keratin-mutant mice.
20729838	1	24	theme	epithelia	184:192	arg1	phosphoglycoproteins					148:167	heteropolymeric intermediate filament phosphoglycoproteins	110:167	heteropolymeric intermediate filament phosphoglycoproteins of simple-type epithelia	110:192	Keratins 8 and 18 (K8 and K18) are heteropolymeric intermediate filament phosphoglycoproteins of simple-type epithelia.
20729838	1	24	theme	epithelia	184:192	arg1	Keratins					75:82	Keratins 8 and 18	75:91	Keratins	75:82	Keratins 8 and 18 (K8 and K18) are heteropolymeric intermediate filament phosphoglycoproteins of simple-type epithelia.
20729838	1	24	theme	epithelia	184:192	arg1	18					90:91	18	90:91	18	90:91	Keratins 8 and 18 (K8 and K18) are heteropolymeric intermediate filament phosphoglycoproteins of simple-type epithelia.
20729838	0	25	theme	keratin	13:19	arg1	glycosylation					21:33	Cytoskeletal keratin glycosylation	0:33	Cytoskeletal keratin glycosylation	0:33	Cytoskeletal keratin glycosylation protects epithelial tissue from injury.
20729838	4	26	theme	S30/31/49A	498:507	arg1	mutants					522:528	human K18 S30/31/49A substitution mutants	488:528	human K18 S30/31/49A substitution mutants that cannot be glycosylated (K18-Gly(-))	488:569	We investigated the function of K18 glycosylation by generating mice that overexpress human K18 S30/31/49A substitution mutants that cannot be glycosylated (K18-Gly(-)), and compared the susceptibility of these mice to injury with wild-type and other keratin-mutant mice.
20729838	7	27	theme	decreased	1225:1233	arg1	activity					1247:1254	decreased Akt1 kinase activity	1225:1254	decreased Akt1 kinase activity	1225:1254	Akt1 binds to K8, which probably contributes to the reciprocal hyperglycosylation and hypophosphorylation of Akt1 that occurs on K18 hypoglycosylation, and leads to decreased Akt1 kinase activity.
20729838	0	28	theme	Cytoskeletal	0:11	arg1	glycosylation					21:33	Cytoskeletal keratin glycosylation	0:33	Cytoskeletal keratin glycosylation	0:33	Cytoskeletal keratin glycosylation protects epithelial tissue from injury.
20729838	3	29	link	O-linked	337:344	arg1	N-acetylglucosamine					346:364	O-linked N-acetylglucosamine	337:364	dynamic O-linked N-acetylglucosamine glycosylation	329:378	K18 undergoes dynamic O-linked N-acetylglucosamine glycosylation at Ser 30, 31 and 49.
20729838	7	30	theme	Akt1	1169:1172	arg1	hypophosphorylation					1146:1164	hypophosphorylation	1146:1164	hypophosphorylation	1146:1164	Akt1 binds to K8, which probably contributes to the reciprocal hyperglycosylation and hypophosphorylation of Akt1 that occurs on K18 hypoglycosylation, and leads to decreased Akt1 kinase activity.
20729838	7	30	theme	Akt1	1169:1172	arg1	hyperglycosylation					1123:1140	reciprocal hyperglycosylation	1112:1140	reciprocal hyperglycosylation	1112:1140	Akt1 binds to K8, which probably contributes to the reciprocal hyperglycosylation and hypophosphorylation of Akt1 that occurs on K18 hypoglycosylation, and leads to decreased Akt1 kinase activity.
20729838	8	31	theme	protective	1304:1313	arg1	role					1315:1318	a unique protective role	1295:1318	a unique protective role in epithelial injury	1295:1339	Therefore, K18 glycosylation provides a unique protective role in epithelial injury by promoting the phosphorylation and activation of cell-survival kinases.
20729838	8	32	theme	kinases	1406:1412	arg1	phosphorylation					1358:1372	phosphorylation	1358:1372	phosphorylation	1358:1372	Therefore, K18 glycosylation provides a unique protective role in epithelial injury by promoting the phosphorylation and activation of cell-survival kinases.
20729838	8	32	theme	kinases	1406:1412	arg1	activation					1378:1387	activation	1378:1387	activation	1378:1387	Therefore, K18 glycosylation provides a unique protective role in epithelial injury by promoting the phosphorylation and activation of cell-survival kinases.
20729838	5	33	theme	N-acetyl-D-glucosaminidase	813:838	arg1	inhibition					840:849	combined N-acetyl-D-glucosaminidase inhibition	804:849	combined N-acetyl-D-glucosaminidase inhibition	804:849	K18-Gly(-) mice are more susceptible to liver and pancreatic injury and apoptosis induced by streptozotocin or to liver injury by combined N-acetyl-D-glucosaminidase inhibition and Fas administration.
20729838	5	34	theme	combined	804:811	arg1	inhibition					840:849	combined N-acetyl-D-glucosaminidase inhibition	804:849	combined N-acetyl-D-glucosaminidase inhibition	804:849	K18-Gly(-) mice are more susceptible to liver and pancreatic injury and apoptosis induced by streptozotocin or to liver injury by combined N-acetyl-D-glucosaminidase inhibition and Fas administration.
20729838	6	35	theme	enhanced	879:886	arg1	apoptosis					888:896	The enhanced apoptosis	875:896	The enhanced apoptosis in the livers of mice that express K18-Gly(-)	875:942	The enhanced apoptosis in the livers of mice that express K18-Gly(-) involves the inactivation of Akt1 and protein kinase Ctheta as a result of their site-specific hypophosphorylation.
20729838	8	36	theme	cell-survival	1392:1404	arg1	kinases					1406:1412	cell-survival kinases	1392:1412	cell-survival kinases	1392:1412	Therefore, K18 glycosylation provides a unique protective role in epithelial injury by promoting the phosphorylation and activation of cell-survival kinases.
20729838	6	37	theme	site-specific	1025:1037	arg1	hypophosphorylation					1039:1057	their site-specific hypophosphorylation	1019:1057	their site-specific hypophosphorylation	1019:1057	The enhanced apoptosis in the livers of mice that express K18-Gly(-) involves the inactivation of Akt1 and protein kinase Ctheta as a result of their site-specific hypophosphorylation.
20729838	6	38	dep	K18-Gly	933:939	arg1	-					941:941	-	941:941	-	941:941	The enhanced apoptosis in the livers of mice that express K18-Gly(-) involves the inactivation of Akt1 and protein kinase Ctheta as a result of their site-specific hypophosphorylation.
20729838	0	39	theme	epithelial	44:53	arg1	tissue					55:60	epithelial tissue	44:60	epithelial tissue	44:60	Cytoskeletal keratin glycosylation protects epithelial tissue from injury.
20729838	8	40	dep	phosphorylation	1358:1372	arg1	the					1354:1356	the	1354:1356	the	1354:1356	Therefore, K18 glycosylation provides a unique protective role in epithelial injury by promoting the phosphorylation and activation of cell-survival kinases.
20729838	2	41	theme	affected	234:241	arg1	individual					243:252	the affected individual	230:252	the affected individual to liver disease	230:269	Mutations in K8 and K18 predispose the affected individual to liver disease as they protect hepatocytes from apoptosis.
20729838	5	42	theme	Fas	855:857	arg1	administration					859:872	Fas administration	855:872	Fas administration	855:872	K18-Gly(-) mice are more susceptible to liver and pancreatic injury and apoptosis induced by streptozotocin or to liver injury by combined N-acetyl-D-glucosaminidase inhibition and Fas administration.
20729838	4	43	theme	wild-type	633:641	arg1	mice					668:671	wild-type and other keratin-mutant mice	633:671	wild-type and other keratin-mutant mice	633:671	We investigated the function of K18 glycosylation by generating mice that overexpress human K18 S30/31/49A substitution mutants that cannot be glycosylated (K18-Gly(-)), and compared the susceptibility of these mice to injury with wild-type and other keratin-mutant mice.
20729838	3	44	gly	glycosylation	366:378	arg1	49					398:399	49	398:399	49	398:399	K18 undergoes dynamic O-linked N-acetylglucosamine glycosylation at Ser 30, 31 and 49.
20729838	3	44	gly	glycosylation	366:378	arg1	Ser					383:385	Ser 30	383:388	Ser 30	383:388	K18 undergoes dynamic O-linked N-acetylglucosamine glycosylation at Ser 30, 31 and 49.
20729838	3	44	gly	glycosylation	366:378	arg1	31					391:392	31	391:392	31	391:392	K18 undergoes dynamic O-linked N-acetylglucosamine glycosylation at Ser 30, 31 and 49.
20729838	3	44	gly	glycosylation	366:378	arg1	K18					315:317	K18	315:317	K18	315:317	K18 undergoes dynamic O-linked N-acetylglucosamine glycosylation at Ser 30, 31 and 49.
20729838	8	45	theme	unique	1297:1302	arg1	role					1315:1318	a unique protective role	1295:1318	a unique protective role in epithelial injury	1295:1339	Therefore, K18 glycosylation provides a unique protective role in epithelial injury by promoting the phosphorylation and activation of cell-survival kinases.
20729838	4	46	theme	K18	434:436	arg1	glycosylation					438:450	K18 glycosylation	434:450	K18 glycosylation	434:450	We investigated the function of K18 glycosylation by generating mice that overexpress human K18 S30/31/49A substitution mutants that cannot be glycosylated (K18-Gly(-)), and compared the susceptibility of these mice to injury with wild-type and other keratin-mutant mice.
20729838	7	47	gly	hyperglycosylation	1123:1140	arg2	hypoglycosylation					1193:1209	K18 hypoglycosylation	1189:1209	K18 hypoglycosylation	1189:1209	Akt1 binds to K8, which probably contributes to the reciprocal hyperglycosylation and hypophosphorylation of Akt1 that occurs on K18 hypoglycosylation, and leads to decreased Akt1 kinase activity.
20729838	7	47	gly	hyperglycosylation	1123:1140	arg1	Akt1					1169:1172	Akt1	1169:1172	Akt1	1169:1172	Akt1 binds to K8, which probably contributes to the reciprocal hyperglycosylation and hypophosphorylation of Akt1 that occurs on K18 hypoglycosylation, and leads to decreased Akt1 kinase activity.
20729838	1	48	gly	phosphoglycoproteins	148:167	arg1	phosphoglycoproteins					148:167	heteropolymeric intermediate filament phosphoglycoproteins	110:167	heteropolymeric intermediate filament phosphoglycoproteins of simple-type epithelia	110:192	Keratins 8 and 18 (K8 and K18) are heteropolymeric intermediate filament phosphoglycoproteins of simple-type epithelia.
20729838	1	48	gly	phosphoglycoproteins	148:167	arg1	Keratins					75:82	Keratins 8 and 18	75:91	Keratins	75:82	Keratins 8 and 18 (K8 and K18) are heteropolymeric intermediate filament phosphoglycoproteins of simple-type epithelia.
20729838	1	48	gly	phosphoglycoproteins	148:167	arg1	18					90:91	18	90:91	18	90:91	Keratins 8 and 18 (K8 and K18) are heteropolymeric intermediate filament phosphoglycoproteins of simple-type epithelia.
20729838	8	49	theme	epithelial	1323:1332	arg1	injury					1334:1339	epithelial injury	1323:1339	epithelial injury	1323:1339	Therefore, K18 glycosylation provides a unique protective role in epithelial injury by promoting the phosphorylation and activation of cell-survival kinases.
20729838	4	50	gly	glycosylated	545:556	arg1	mutants					522:528	human K18 S30/31/49A substitution mutants	488:528	human K18 S30/31/49A substitution mutants that cannot be glycosylated (K18-Gly(-))	488:569	We investigated the function of K18 glycosylation by generating mice that overexpress human K18 S30/31/49A substitution mutants that cannot be glycosylated (K18-Gly(-)), and compared the susceptibility of these mice to injury with wild-type and other keratin-mutant mice.
20729838	1	51	theme	heteropolymeric	110:124	arg1	phosphoglycoproteins					148:167	heteropolymeric intermediate filament phosphoglycoproteins	110:167	heteropolymeric intermediate filament phosphoglycoproteins of simple-type epithelia	110:192	Keratins 8 and 18 (K8 and K18) are heteropolymeric intermediate filament phosphoglycoproteins of simple-type epithelia.
20729838	1	51	theme	heteropolymeric	110:124	arg1	Keratins					75:82	Keratins 8 and 18	75:91	Keratins	75:82	Keratins 8 and 18 (K8 and K18) are heteropolymeric intermediate filament phosphoglycoproteins of simple-type epithelia.
20729838	1	51	theme	heteropolymeric	110:124	arg1	18					90:91	18	90:91	18	90:91	Keratins 8 and 18 (K8 and K18) are heteropolymeric intermediate filament phosphoglycoproteins of simple-type epithelia.
20729838	3	52	theme	N-acetylglucosamine	346:364	arg1	glycosylation					366:378	dynamic O-linked N-acetylglucosamine glycosylation	329:378	dynamic O-linked N-acetylglucosamine glycosylation	329:378	K18 undergoes dynamic O-linked N-acetylglucosamine glycosylation at Ser 30, 31 and 49.
20729838	4	53	theme	glycosylation	438:450	arg1	function					422:429	the function	418:429	the function of K18 glycosylation	418:450	We investigated the function of K18 glycosylation by generating mice that overexpress human K18 S30/31/49A substitution mutants that cannot be glycosylated (K18-Gly(-)), and compared the susceptibility of these mice to injury with wild-type and other keratin-mutant mice.
20729838	2	54	theme	liver	257:261	arg1	disease					263:269	liver disease	257:269	liver disease	257:269	Mutations in K8 and K18 predispose the affected individual to liver disease as they protect hepatocytes from apoptosis.
20729838	6	55	theme	hypophosphorylation	1039:1057	arg1	inactivation					957:968	the inactivation	953:968	the inactivation of Akt1 and protein kinase Ctheta	953:1002	The enhanced apoptosis in the livers of mice that express K18-Gly(-) involves the inactivation of Akt1 and protein kinase Ctheta as a result of their site-specific hypophosphorylation.
20729838	6	55	theme	hypophosphorylation	1039:1057	arg1	result					1009:1014	a result	1007:1014	a result of their site-specific hypophosphorylation	1007:1057	The enhanced apoptosis in the livers of mice that express K18-Gly(-) involves the inactivation of Akt1 and protein kinase Ctheta as a result of their site-specific hypophosphorylation.
20729838	1	56	theme	intermediate	126:137	arg1	phosphoglycoproteins					148:167	heteropolymeric intermediate filament phosphoglycoproteins	110:167	heteropolymeric intermediate filament phosphoglycoproteins of simple-type epithelia	110:192	Keratins 8 and 18 (K8 and K18) are heteropolymeric intermediate filament phosphoglycoproteins of simple-type epithelia.
20729838	1	56	theme	intermediate	126:137	arg1	Keratins					75:82	Keratins 8 and 18	75:91	Keratins	75:82	Keratins 8 and 18 (K8 and K18) are heteropolymeric intermediate filament phosphoglycoproteins of simple-type epithelia.
20729838	1	56	theme	intermediate	126:137	arg1	18					90:91	18	90:91	18	90:91	Keratins 8 and 18 (K8 and K18) are heteropolymeric intermediate filament phosphoglycoproteins of simple-type epithelia.
20729838	7	57	theme	Akt1	1235:1238	arg1	activity					1247:1254	decreased Akt1 kinase activity	1225:1254	decreased Akt1 kinase activity	1225:1254	Akt1 binds to K8, which probably contributes to the reciprocal hyperglycosylation and hypophosphorylation of Akt1 that occurs on K18 hypoglycosylation, and leads to decreased Akt1 kinase activity.
20729838	6	58	theme	Ctheta	997:1002	arg1	inactivation					957:968	the inactivation	953:968	the inactivation of Akt1 and protein kinase Ctheta	953:1002	The enhanced apoptosis in the livers of mice that express K18-Gly(-) involves the inactivation of Akt1 and protein kinase Ctheta as a result of their site-specific hypophosphorylation.
20729838	6	58	theme	Ctheta	997:1002	arg1	result					1009:1014	a result	1007:1014	a result of their site-specific hypophosphorylation	1007:1057	The enhanced apoptosis in the livers of mice that express K18-Gly(-) involves the inactivation of Akt1 and protein kinase Ctheta as a result of their site-specific hypophosphorylation.
20729838	1	59	theme	filament	139:146	arg1	phosphoglycoproteins					148:167	heteropolymeric intermediate filament phosphoglycoproteins	110:167	heteropolymeric intermediate filament phosphoglycoproteins of simple-type epithelia	110:192	Keratins 8 and 18 (K8 and K18) are heteropolymeric intermediate filament phosphoglycoproteins of simple-type epithelia.
20729838	1	59	theme	filament	139:146	arg1	Keratins					75:82	Keratins 8 and 18	75:91	Keratins	75:82	Keratins 8 and 18 (K8 and K18) are heteropolymeric intermediate filament phosphoglycoproteins of simple-type epithelia.
20729838	1	59	theme	filament	139:146	arg1	18					90:91	18	90:91	18	90:91	Keratins 8 and 18 (K8 and K18) are heteropolymeric intermediate filament phosphoglycoproteins of simple-type epithelia.
20729838	4	60	theme	mice	613:616	arg1	susceptibility					589:602	the susceptibility	585:602	the susceptibility of these mice to injury	585:626	We investigated the function of K18 glycosylation by generating mice that overexpress human K18 S30/31/49A substitution mutants that cannot be glycosylated (K18-Gly(-)), and compared the susceptibility of these mice to injury with wild-type and other keratin-mutant mice.
23556518	12	0	theme	N-linked	1651:1658	arg1	glycosylation					1660:1672	N-linked glycosylation	1651:1672	N-linked glycosylation	1651:1672	On the basis of our analyses, we conclude that unlike TfR1, N-linked glycosylation is dispensable for the cell surface expression and holo-Tf binding, but it is required for efficient intersubunit disulfide bond formation and holo-Tf-induced stabilization of TfR2.
23556518	0	1	theme	cell	154:157	arg1	surface					159:165	the cell surface	150:165	the cell surface	150:165	N-linked glycosylation is required for transferrin-induced stabilization of transferrin receptor 2, but not for transferrin binding or trafficking to the cell surface.
23556518	4	2	theme	Asn-linked	528:537	arg1	sites					564:568	four potential Asn-linked (N-linked) glycosylation sites	513:568	four potential Asn-linked (N-linked) glycosylation sites on its ectodomain	513:586	Human TfR2 (hTfR2) contains four potential Asn-linked (N-linked) glycosylation sites on its ectodomain.
23556518	3	3	theme	hormone	466:472	arg1	hepcidin					475:482	the iron regulatory hormone, hepcidin	446:482	hepcidin	475:482	TfR2 is proposed to sense body iron levels and increase the level of expression of the iron regulatory hormone, hepcidin.
23556518	1	4	theme	family	243:248	arg1	member					203:208	a member	201:208	a member of the transferrin receptor-like family of proteins	201:260	Transferrin receptor 2 (TfR2) is a member of the transferrin receptor-like family of proteins.
23556518	1	4	theme	family	243:248	arg1	receptor					180:187	Transferrin receptor 2	168:189	Transferrin receptor 2 (TfR2)	168:196	Transferrin receptor 2 (TfR2) is a member of the transferrin receptor-like family of proteins.
23556518	4	5	theme	N-linked	540:547	arg1	sites					564:568	four potential Asn-linked (N-linked) glycosylation sites	513:568	four potential Asn-linked (N-linked) glycosylation sites on its ectodomain	513:586	Human TfR2 (hTfR2) contains four potential Asn-linked (N-linked) glycosylation sites on its ectodomain.
23556518	7	6	theme	oligosaccharides	1035:1050	arg1	absence					1015:1021	the absence	1011:1021	the absence of N-linked oligosaccharides	1011:1050	Cell surface protein biotinylation and biotin-labeled Tf indicated that in the absence of N-linked oligosaccharides, hTfR2 still moved to the plasma membrane and bound its ligand, holo-Tf.
23556518	3	7	theme	regulatory	455:464	arg1	hepcidin					475:482	the iron regulatory hormone, hepcidin	446:482	hepcidin	475:482	TfR2 is proposed to sense body iron levels and increase the level of expression of the iron regulatory hormone, hepcidin.
23556518	1	8	theme	proteins	253:260	arg1	family					243:248	the transferrin receptor-like family	213:248	the transferrin receptor-like family of proteins	213:260	Transferrin receptor 2 (TfR2) is a member of the transferrin receptor-like family of proteins.
23556518	0	9	link	N-linked	0:7	arg1	glycosylation					9:21	N-linked glycosylation	0:21	N-linked glycosylation	0:21	N-linked glycosylation is required for transferrin-induced stabilization of transferrin receptor 2, but not for transferrin binding or trafficking to the cell surface.
23556518	6	10	used	utilized	926:933	arg2	sequence					871:878	the consensus sequence	857:878	the consensus sequence for N-linked glycosylation at Asn 540	857:916	In this study, by employing site-directed mutagenesis to remove glycosylation sites of hTfR2 individually or in combination, we found that hTfR2 was glycosylated at Asn 240, 339, and 754, while the consensus sequence for N-linked glycosylation at Asn 540 was not utilized.
23556518	6	10	used	utilized	926:933	arg2	Asn					910:912	Asn 540	910:916	Asn 540	910:916	In this study, by employing site-directed mutagenesis to remove glycosylation sites of hTfR2 individually or in combination, we found that hTfR2 was glycosylated at Asn 240, 339, and 754, while the consensus sequence for N-linked glycosylation at Asn 540 was not utilized.
23556518	12	11	theme	TfR2	1850:1853	arg1	formation					1803:1811	efficient intersubunit disulfide bond formation	1765:1811	efficient intersubunit disulfide bond formation	1765:1811	On the basis of our analyses, we conclude that unlike TfR1, N-linked glycosylation is dispensable for the cell surface expression and holo-Tf binding, but it is required for efficient intersubunit disulfide bond formation and holo-Tf-induced stabilization of TfR2.
23556518	12	11	theme	TfR2	1850:1853	arg1	stabilization					1833:1845	holo-Tf-induced stabilization	1817:1845	holo-Tf-induced stabilization of TfR2	1817:1853	On the basis of our analyses, we conclude that unlike TfR1, N-linked glycosylation is dispensable for the cell surface expression and holo-Tf binding, but it is required for efficient intersubunit disulfide bond formation and holo-Tf-induced stabilization of TfR2.
23556518	6	12	theme	glycosylation	727:739	arg1	sites					741:745	glycosylation sites	727:745	glycosylation sites of hTfR2	727:754	In this study, by employing site-directed mutagenesis to remove glycosylation sites of hTfR2 individually or in combination, we found that hTfR2 was glycosylated at Asn 240, 339, and 754, while the consensus sequence for N-linked glycosylation at Asn 540 was not utilized.
23556518	6	12	theme	glycosylation	727:739	arg1	hTfR2					750:754	hTfR2	750:754	hTfR2	750:754	In this study, by employing site-directed mutagenesis to remove glycosylation sites of hTfR2 individually or in combination, we found that hTfR2 was glycosylated at Asn 240, 339, and 754, while the consensus sequence for N-linked glycosylation at Asn 540 was not utilized.
23556518	6	13	theme	N-linked	884:891	arg1	glycosylation					893:905	N-linked glycosylation	884:905	N-linked glycosylation	884:905	In this study, by employing site-directed mutagenesis to remove glycosylation sites of hTfR2 individually or in combination, we found that hTfR2 was glycosylated at Asn 240, 339, and 754, while the consensus sequence for N-linked glycosylation at Asn 540 was not utilized.
23556518	2	14	theme	iron	312:315	arg1	disease					326:332	the iron overload disease	308:332	the iron overload disease	308:332	Mutations in TfR2 can lead to a rare form of the iron overload disease, hereditary hemochromatosis.
23556518	2	14	theme	iron	312:315	arg1	hemochromatosis					346:360	hereditary hemochromatosis	335:360	hereditary hemochromatosis	335:360	Mutations in TfR2 can lead to a rare form of the iron overload disease, hereditary hemochromatosis.
23556518	6	15	gly	glycosylation	727:739	arg2	hTfR2					750:754	hTfR2	750:754	hTfR2	750:754	In this study, by employing site-directed mutagenesis to remove glycosylation sites of hTfR2 individually or in combination, we found that hTfR2 was glycosylated at Asn 240, 339, and 754, while the consensus sequence for N-linked glycosylation at Asn 540 was not utilized.
23556518	6	15	gly	glycosylation	727:739	arg1	hTfR2					750:754	hTfR2	750:754	hTfR2	750:754	In this study, by employing site-directed mutagenesis to remove glycosylation sites of hTfR2 individually or in combination, we found that hTfR2 was glycosylated at Asn 240, 339, and 754, while the consensus sequence for N-linked glycosylation at Asn 540 was not utilized.
23556518	6	15	gly	glycosylation	727:739	arg2	sites					741:745	glycosylation sites	727:745	glycosylation sites of hTfR2	727:754	In this study, by employing site-directed mutagenesis to remove glycosylation sites of hTfR2 individually or in combination, we found that hTfR2 was glycosylated at Asn 240, 339, and 754, while the consensus sequence for N-linked glycosylation at Asn 540 was not utilized.
23556518	3	16	theme	iron	394:397	arg1	levels					399:404	sense body iron levels	383:404	sense body iron levels	383:404	TfR2 is proposed to sense body iron levels and increase the level of expression of the iron regulatory hormone, hepcidin.
23556518	8	17	theme	disulfide	1202:1210	arg1	bonds					1212:1216	the intersubunit disulfide bonds	1185:1216	the intersubunit disulfide bonds as efficiently as the wild type (WT)	1185:1253	However, without N-linked glycosylation, hTfR2 did not form the intersubunit disulfide bonds as efficiently as the wild type (WT).
23556518	6	18	link	N-linked	884:891	arg1	glycosylation					893:905	N-linked glycosylation	884:905	N-linked glycosylation	884:905	In this study, by employing site-directed mutagenesis to remove glycosylation sites of hTfR2 individually or in combination, we found that hTfR2 was glycosylated at Asn 240, 339, and 754, while the consensus sequence for N-linked glycosylation at Asn 540 was not utilized.
23556518	7	19	theme	N-linked	1026:1033	arg1	oligosaccharides					1035:1050	N-linked oligosaccharides	1026:1050	N-linked oligosaccharides	1026:1050	Cell surface protein biotinylation and biotin-labeled Tf indicated that in the absence of N-linked oligosaccharides, hTfR2 still moved to the plasma membrane and bound its ligand, holo-Tf.
23556518	2	20	from	Mutations	263:271	arg1	TfR2					276:279	TfR2	276:279	TfR2	276:279	Mutations in TfR2 can lead to a rare form of the iron overload disease, hereditary hemochromatosis.
23556518	12	21	dep	analyses	1611:1618	arg1	the					1594:1596	the	1594:1596	the	1594:1596	On the basis of our analyses, we conclude that unlike TfR1, N-linked glycosylation is dispensable for the cell surface expression and holo-Tf binding, but it is required for efficient intersubunit disulfide bond formation and holo-Tf-induced stabilization of TfR2.
23556518	12	21	dep	analyses	1611:1618	arg1	basis					1598:1602	basis	1598:1602	basis	1598:1602	On the basis of our analyses, we conclude that unlike TfR1, N-linked glycosylation is dispensable for the cell surface expression and holo-Tf binding, but it is required for efficient intersubunit disulfide bond formation and holo-Tf-induced stabilization of TfR2.
23556518	7	22	theme	protein	949:955	arg1	biotinylation					957:969	Cell surface protein biotinylation	936:969	Cell surface protein biotinylation	936:969	Cell surface protein biotinylation and biotin-labeled Tf indicated that in the absence of N-linked oligosaccharides, hTfR2 still moved to the plasma membrane and bound its ligand, holo-Tf.
23556518	4	23	from	sites	564:568	arg1	ectodomain					577:586	its ectodomain	573:586	its ectodomain	573:586	Human TfR2 (hTfR2) contains four potential Asn-linked (N-linked) glycosylation sites on its ectodomain.
23556518	8	24	theme	wild	1240:1243	arg1	WT					1251:1252	WT	1251:1252	WT	1251:1252	However, without N-linked glycosylation, hTfR2 did not form the intersubunit disulfide bonds as efficiently as the wild type (WT).
23556518	8	24	theme	wild	1240:1243	arg1	type					1245:1248	the wild type	1236:1248	the intersubunit disulfide bonds as efficiently as the wild type (WT)	1185:1253	However, without N-linked glycosylation, hTfR2 did not form the intersubunit disulfide bonds as efficiently as the wild type (WT).
23556518	12	25	theme	efficient	1765:1773	arg1	formation					1803:1811	efficient intersubunit disulfide bond formation	1765:1811	efficient intersubunit disulfide bond formation	1765:1811	On the basis of our analyses, we conclude that unlike TfR1, N-linked glycosylation is dispensable for the cell surface expression and holo-Tf binding, but it is required for efficient intersubunit disulfide bond formation and holo-Tf-induced stabilization of TfR2.
23556518	12	26	theme	disulfide	1788:1796	arg1	formation					1803:1811	efficient intersubunit disulfide bond formation	1765:1811	efficient intersubunit disulfide bond formation	1765:1811	On the basis of our analyses, we conclude that unlike TfR1, N-linked glycosylation is dispensable for the cell surface expression and holo-Tf binding, but it is required for efficient intersubunit disulfide bond formation and holo-Tf-induced stabilization of TfR2.
23556518	6	27	from	Asn	910:912	arg1	sequence					871:878	the consensus sequence	857:878	the consensus sequence for N-linked glycosylation at Asn 540	857:916	In this study, by employing site-directed mutagenesis to remove glycosylation sites of hTfR2 individually or in combination, we found that hTfR2 was glycosylated at Asn 240, 339, and 754, while the consensus sequence for N-linked glycosylation at Asn 540 was not utilized.
23556518	3	28	theme	body	389:392	arg1	levels					399:404	sense body iron levels	383:404	sense body iron levels	383:404	TfR2 is proposed to sense body iron levels and increase the level of expression of the iron regulatory hormone, hepcidin.
23556518	0	29	theme	N-linked	0:7	arg1	glycosylation					9:21	N-linked glycosylation	0:21	N-linked glycosylation	0:21	N-linked glycosylation is required for transferrin-induced stabilization of transferrin receptor 2, but not for transferrin binding or trafficking to the cell surface.
23556518	6	30	gly	glycosylated	812:823	arg1	hTfR2					802:806	hTfR2	802:806	hTfR2	802:806	In this study, by employing site-directed mutagenesis to remove glycosylation sites of hTfR2 individually or in combination, we found that hTfR2 was glycosylated at Asn 240, 339, and 754, while the consensus sequence for N-linked glycosylation at Asn 540 was not utilized.
23556518	6	30	gly	glycosylated	812:823	arg2	Asn					828:830	Asn	828:830	Asn 240, 339, and 754	828:848	In this study, by employing site-directed mutagenesis to remove glycosylation sites of hTfR2 individually or in combination, we found that hTfR2 was glycosylated at Asn 240, 339, and 754, while the consensus sequence for N-linked glycosylation at Asn 540 was not utilized.
23556518	7	31	link	N-linked	1026:1033	arg1	oligosaccharides					1035:1050	N-linked oligosaccharides	1026:1050	N-linked oligosaccharides	1026:1050	Cell surface protein biotinylation and biotin-labeled Tf indicated that in the absence of N-linked oligosaccharides, hTfR2 still moved to the plasma membrane and bound its ligand, holo-Tf.
23556518	12	32	theme	holo-Tf	1725:1731	arg1	binding					1733:1739	holo-Tf binding	1725:1739	holo-Tf binding	1725:1739	On the basis of our analyses, we conclude that unlike TfR1, N-linked glycosylation is dispensable for the cell surface expression and holo-Tf binding, but it is required for efficient intersubunit disulfide bond formation and holo-Tf-induced stabilization of TfR2.
23556518	10	33	theme	unglycosylated	1372:1385	arg1	hTfR2					1387:1391	the unglycosylated hTfR2	1368:1391	the unglycosylated hTfR2	1368:1391	We further provide evidence that the unglycosylated hTfR2 behaved in manner different from that of the WT in response to holo-Tf treatment.
23556518	11	34	theme	oligosaccharides	1573:1588	arg1	absence					1553:1559	the absence	1549:1559	the absence of N-linked oligosaccharides	1549:1588	Thus, the putative iron-sensing function of TfR2 could not be achieved in the absence of N-linked oligosaccharides.
23556518	12	35	link	N-linked	1651:1658	arg1	glycosylation					1660:1672	N-linked glycosylation	1651:1672	N-linked glycosylation	1651:1672	On the basis of our analyses, we conclude that unlike TfR1, N-linked glycosylation is dispensable for the cell surface expression and holo-Tf binding, but it is required for efficient intersubunit disulfide bond formation and holo-Tf-induced stabilization of TfR2.
23556518	10	36	from	WT	1438:1439	arg1	response					1444:1451	response	1444:1451	response to holo-Tf treatment	1444:1472	We further provide evidence that the unglycosylated hTfR2 behaved in manner different from that of the WT in response to holo-Tf treatment.
23556518	0	37	gly	glycosylation	9:21	arg1	receptor					88:95	transferrin receptor 2	76:97	transferrin receptor 2	76:97	N-linked glycosylation is required for transferrin-induced stabilization of transferrin receptor 2, but not for transferrin binding or trafficking to the cell surface.
23556518	0	37	gly	glycosylation	9:21	arg1	transferrin					112:122	transferrin binding or trafficking	112:145	transferrin	112:122	N-linked glycosylation is required for transferrin-induced stabilization of transferrin receptor 2, but not for transferrin binding or trafficking to the cell surface.
23556518	0	38	theme	transferrin	76:86	arg1	receptor					88:95	transferrin receptor 2	76:97	transferrin receptor 2	76:97	N-linked glycosylation is required for transferrin-induced stabilization of transferrin receptor 2, but not for transferrin binding or trafficking to the cell surface.
23556518	5	39	from	importance	593:602	arg1	function					629:636	TfR2 function	624:636	TfR2 function	624:636	The importance of glycosylation in TfR2 function has not been elucidated.
23556518	12	40	theme	cell	1697:1700	arg1	expression					1710:1719	the cell surface expression	1693:1719	the cell surface expression	1693:1719	On the basis of our analyses, we conclude that unlike TfR1, N-linked glycosylation is dispensable for the cell surface expression and holo-Tf binding, but it is required for efficient intersubunit disulfide bond formation and holo-Tf-induced stabilization of TfR2.
23556518	4	41	link	N-linked	540:547	arg1	sites					564:568	four potential Asn-linked (N-linked) glycosylation sites	513:568	four potential Asn-linked (N-linked) glycosylation sites on its ectodomain	513:586	Human TfR2 (hTfR2) contains four potential Asn-linked (N-linked) glycosylation sites on its ectodomain.
23556518	8	42	dep	efficiently	1221:1231	arg1	as					1233:1234	as	1233:1234	as	1233:1234	However, without N-linked glycosylation, hTfR2 did not form the intersubunit disulfide bonds as efficiently as the wild type (WT).
23556518	3	43	theme	expression	432:441	arg1	level					423:427	the level	419:427	the level of expression of the iron regulatory hormone, hepcidin	419:482	TfR2 is proposed to sense body iron levels and increase the level of expression of the iron regulatory hormone, hepcidin.
23556518	9	44	theme	unglycosylated	1270:1283	arg1	form					1285:1288	the unglycosylated form	1266:1288	the unglycosylated form of hTfR2	1266:1297	Moreover, the unglycosylated form of hTfR2 could not be stabilized by holo-Tf.
23556518	4	45	link	Asn-linked	528:537	arg1	sites					564:568	four potential Asn-linked (N-linked) glycosylation sites	513:568	four potential Asn-linked (N-linked) glycosylation sites on its ectodomain	513:586	Human TfR2 (hTfR2) contains four potential Asn-linked (N-linked) glycosylation sites on its ectodomain.
23556518	11	46	theme	putative	1485:1492	arg1	function					1507:1514	the putative iron-sensing function	1481:1514	the putative iron-sensing function of TfR2	1481:1522	Thus, the putative iron-sensing function of TfR2 could not be achieved in the absence of N-linked oligosaccharides.
23556518	2	47	theme	overload	317:324	arg1	disease					326:332	the iron overload disease	308:332	the iron overload disease	308:332	Mutations in TfR2 can lead to a rare form of the iron overload disease, hereditary hemochromatosis.
23556518	2	47	theme	overload	317:324	arg1	hemochromatosis					346:360	hereditary hemochromatosis	335:360	hereditary hemochromatosis	335:360	Mutations in TfR2 can lead to a rare form of the iron overload disease, hereditary hemochromatosis.
23556518	1	48	theme	receptor-like	229:241	arg1	family					243:248	the transferrin receptor-like family	213:248	the transferrin receptor-like family of proteins	213:260	Transferrin receptor 2 (TfR2) is a member of the transferrin receptor-like family of proteins.
23556518	11	49	link	N-linked	1564:1571	arg1	oligosaccharides					1573:1588	N-linked oligosaccharides	1564:1588	N-linked oligosaccharides	1564:1588	Thus, the putative iron-sensing function of TfR2 could not be achieved in the absence of N-linked oligosaccharides.
23556518	4	50	theme	potential	518:526	arg1	sites					564:568	four potential Asn-linked (N-linked) glycosylation sites	513:568	four potential Asn-linked (N-linked) glycosylation sites on its ectodomain	513:586	Human TfR2 (hTfR2) contains four potential Asn-linked (N-linked) glycosylation sites on its ectodomain.
23556518	10	51	theme	holo-Tf	1456:1462	arg1	treatment					1464:1472	holo-Tf treatment	1456:1472	holo-Tf treatment	1456:1472	We further provide evidence that the unglycosylated hTfR2 behaved in manner different from that of the WT in response to holo-Tf treatment.
23556518	11	52	theme	TfR2	1519:1522	arg1	function					1507:1514	the putative iron-sensing function	1481:1514	the putative iron-sensing function of TfR2	1481:1522	Thus, the putative iron-sensing function of TfR2 could not be achieved in the absence of N-linked oligosaccharides.
23556518	5	53	theme	glycosylation	607:619	arg1	importance					593:602	The importance	589:602	The importance of glycosylation in TfR2 function	589:636	The importance of glycosylation in TfR2 function has not been elucidated.
23556518	6	54	theme	hTfR2	750:754	arg1	sites					741:745	glycosylation sites	727:745	glycosylation sites of hTfR2	727:754	In this study, by employing site-directed mutagenesis to remove glycosylation sites of hTfR2 individually or in combination, we found that hTfR2 was glycosylated at Asn 240, 339, and 754, while the consensus sequence for N-linked glycosylation at Asn 540 was not utilized.
23556518	6	54	theme	hTfR2	750:754	arg1	hTfR2					750:754	hTfR2	750:754	hTfR2	750:754	In this study, by employing site-directed mutagenesis to remove glycosylation sites of hTfR2 individually or in combination, we found that hTfR2 was glycosylated at Asn 240, 339, and 754, while the consensus sequence for N-linked glycosylation at Asn 540 was not utilized.
23556518	1	55	theme	Transferrin	168:178	arg1	member					203:208	a member	201:208	a member of the transferrin receptor-like family of proteins	201:260	Transferrin receptor 2 (TfR2) is a member of the transferrin receptor-like family of proteins.
23556518	1	55	theme	Transferrin	168:178	arg1	receptor					180:187	Transferrin receptor 2	168:189	Transferrin receptor 2 (TfR2)	168:196	Transferrin receptor 2 (TfR2) is a member of the transferrin receptor-like family of proteins.
23556518	1	55	theme	Transferrin	168:178	arg1	TfR2					192:195	TfR2	192:195	TfR2	192:195	Transferrin receptor 2 (TfR2) is a member of the transferrin receptor-like family of proteins.
23556518	8	56	theme	N-linked	1142:1149	arg1	glycosylation					1151:1163	N-linked glycosylation	1142:1163	N-linked glycosylation	1142:1163	However, without N-linked glycosylation, hTfR2 did not form the intersubunit disulfide bonds as efficiently as the wild type (WT).
23556518	4	57	contain	contains	504:511	arg1	TfR2					491:494	Human TfR2	485:494	Human TfR2 (hTfR2)	485:502	Human TfR2 (hTfR2) contains four potential Asn-linked (N-linked) glycosylation sites on its ectodomain.
23556518	4	57	contain	contains	504:511	arg2	sites					564:568	four potential Asn-linked (N-linked) glycosylation sites	513:568	four potential Asn-linked (N-linked) glycosylation sites on its ectodomain	513:586	Human TfR2 (hTfR2) contains four potential Asn-linked (N-linked) glycosylation sites on its ectodomain.
23556518	4	57	contain	contains	504:511	arg1	hTfR2					497:501	hTfR2	497:501	hTfR2	497:501	Human TfR2 (hTfR2) contains four potential Asn-linked (N-linked) glycosylation sites on its ectodomain.
23556518	7	58	theme	biotin-labeled	975:988	arg1	Tf					990:991	biotin-labeled Tf	975:991	biotin-labeled Tf	975:991	Cell surface protein biotinylation and biotin-labeled Tf indicated that in the absence of N-linked oligosaccharides, hTfR2 still moved to the plasma membrane and bound its ligand, holo-Tf.
23556518	6	59	theme	consensus	861:869	arg1	sequence					871:878	the consensus sequence	857:878	the consensus sequence for N-linked glycosylation at Asn 540	857:916	In this study, by employing site-directed mutagenesis to remove glycosylation sites of hTfR2 individually or in combination, we found that hTfR2 was glycosylated at Asn 240, 339, and 754, while the consensus sequence for N-linked glycosylation at Asn 540 was not utilized.
23556518	5	60	theme	TfR2	624:627	arg1	function					629:636	TfR2 function	624:636	TfR2 function	624:636	The importance of glycosylation in TfR2 function has not been elucidated.
23556518	7	61	theme	Cell	936:939	arg1	biotinylation					957:969	Cell surface protein biotinylation	936:969	Cell surface protein biotinylation	936:969	Cell surface protein biotinylation and biotin-labeled Tf indicated that in the absence of N-linked oligosaccharides, hTfR2 still moved to the plasma membrane and bound its ligand, holo-Tf.
23556518	12	62	theme	holo-Tf-induced	1817:1831	arg1	stabilization					1833:1845	holo-Tf-induced stabilization	1817:1845	holo-Tf-induced stabilization of TfR2	1817:1853	On the basis of our analyses, we conclude that unlike TfR1, N-linked glycosylation is dispensable for the cell surface expression and holo-Tf binding, but it is required for efficient intersubunit disulfide bond formation and holo-Tf-induced stabilization of TfR2.
23556518	8	63	theme	intersubunit	1189:1200	arg1	bonds					1212:1216	the intersubunit disulfide bonds	1185:1216	the intersubunit disulfide bonds as efficiently as the wild type (WT)	1185:1253	However, without N-linked glycosylation, hTfR2 did not form the intersubunit disulfide bonds as efficiently as the wild type (WT).
23556518	7	64	theme	surface	941:947	arg1	biotinylation					957:969	Cell surface protein biotinylation	936:969	Cell surface protein biotinylation	936:969	Cell surface protein biotinylation and biotin-labeled Tf indicated that in the absence of N-linked oligosaccharides, hTfR2 still moved to the plasma membrane and bound its ligand, holo-Tf.
23556518	0	65	theme	receptor	88:95	arg1	stabilization					59:71	transferrin-induced stabilization	39:71	transferrin-induced stabilization of transferrin receptor 2	39:97	N-linked glycosylation is required for transferrin-induced stabilization of transferrin receptor 2, but not for transferrin binding or trafficking to the cell surface.
23556518	12	66	theme	intersubunit	1775:1786	arg1	formation					1803:1811	efficient intersubunit disulfide bond formation	1765:1811	efficient intersubunit disulfide bond formation	1765:1811	On the basis of our analyses, we conclude that unlike TfR1, N-linked glycosylation is dispensable for the cell surface expression and holo-Tf binding, but it is required for efficient intersubunit disulfide bond formation and holo-Tf-induced stabilization of TfR2.
23556518	12	67	theme	bond	1798:1801	arg1	formation					1803:1811	efficient intersubunit disulfide bond formation	1765:1811	efficient intersubunit disulfide bond formation	1765:1811	On the basis of our analyses, we conclude that unlike TfR1, N-linked glycosylation is dispensable for the cell surface expression and holo-Tf binding, but it is required for efficient intersubunit disulfide bond formation and holo-Tf-induced stabilization of TfR2.
23556518	4	68	gly	glycosylation	550:562	arg2	four					513:516	four	513:516	four	513:516	Human TfR2 (hTfR2) contains four potential Asn-linked (N-linked) glycosylation sites on its ectodomain.
23556518	4	68	gly	glycosylation	550:562	arg2	sites					564:568	four potential Asn-linked (N-linked) glycosylation sites	513:568	four potential Asn-linked (N-linked) glycosylation sites on its ectodomain	513:586	Human TfR2 (hTfR2) contains four potential Asn-linked (N-linked) glycosylation sites on its ectodomain.
23556518	0	69	theme	transferrin	112:122	arg1	binding					124:130	transferrin binding or trafficking	112:145	binding	124:130	N-linked glycosylation is required for transferrin-induced stabilization of transferrin receptor 2, but not for transferrin binding or trafficking to the cell surface.
23556518	2	70	theme	hereditary	335:344	arg1	disease					326:332	the iron overload disease	308:332	the iron overload disease	308:332	Mutations in TfR2 can lead to a rare form of the iron overload disease, hereditary hemochromatosis.
23556518	2	70	theme	hereditary	335:344	arg1	hemochromatosis					346:360	hereditary hemochromatosis	335:360	hereditary hemochromatosis	335:360	Mutations in TfR2 can lead to a rare form of the iron overload disease, hereditary hemochromatosis.
23556518	7	71	theme	plasma	1078:1083	arg1	membrane					1085:1092	the plasma membrane	1074:1092	the plasma membrane	1074:1092	Cell surface protein biotinylation and biotin-labeled Tf indicated that in the absence of N-linked oligosaccharides, hTfR2 still moved to the plasma membrane and bound its ligand, holo-Tf.
23556518	11	72	theme	N-linked	1564:1571	arg1	oligosaccharides					1573:1588	N-linked oligosaccharides	1564:1588	N-linked oligosaccharides	1564:1588	Thus, the putative iron-sensing function of TfR2 could not be achieved in the absence of N-linked oligosaccharides.
23556518	10	73	gly	unglycosylated	1372:1385	arg1	hTfR2					1387:1391	the unglycosylated hTfR2	1368:1391	the unglycosylated hTfR2	1368:1391	We further provide evidence that the unglycosylated hTfR2 behaved in manner different from that of the WT in response to holo-Tf treatment.
23556518	0	74	theme	transferrin-induced	39:57	arg1	stabilization					59:71	transferrin-induced stabilization	39:71	transferrin-induced stabilization of transferrin receptor 2	39:97	N-linked glycosylation is required for transferrin-induced stabilization of transferrin receptor 2, but not for transferrin binding or trafficking to the cell surface.
23556518	10	75	from	that	1426:1429	arg1	different					1411:1419	different	1411:1419	different	1411:1419	We further provide evidence that the unglycosylated hTfR2 behaved in manner different from that of the WT in response to holo-Tf treatment.
23556518	3	76	theme	sense	383:387	arg1	levels					399:404	sense body iron levels	383:404	sense body iron levels	383:404	TfR2 is proposed to sense body iron levels and increase the level of expression of the iron regulatory hormone, hepcidin.
23556518	4	77	theme	Human	485:489	arg1	TfR2					491:494	Human TfR2	485:494	Human TfR2 (hTfR2)	485:502	Human TfR2 (hTfR2) contains four potential Asn-linked (N-linked) glycosylation sites on its ectodomain.
23556518	4	77	theme	Human	485:489	arg1	hTfR2					497:501	hTfR2	497:501	hTfR2	497:501	Human TfR2 (hTfR2) contains four potential Asn-linked (N-linked) glycosylation sites on its ectodomain.
23556518	9	78	gly	unglycosylated	1270:1283	arg1	hTfR2					1293:1297	hTfR2	1293:1297	hTfR2	1293:1297	Moreover, the unglycosylated form of hTfR2 could not be stabilized by holo-Tf.
23556518	9	78	gly	unglycosylated	1270:1283	arg1	form					1285:1288	the unglycosylated form	1266:1288	the unglycosylated form of hTfR2	1266:1297	Moreover, the unglycosylated form of hTfR2 could not be stabilized by holo-Tf.
23556518	12	79	theme	surface	1702:1708	arg1	expression					1710:1719	the cell surface expression	1693:1719	the cell surface expression	1693:1719	On the basis of our analyses, we conclude that unlike TfR1, N-linked glycosylation is dispensable for the cell surface expression and holo-Tf binding, but it is required for efficient intersubunit disulfide bond formation and holo-Tf-induced stabilization of TfR2.
23556518	8	80	link	N-linked	1142:1149	arg1	glycosylation					1151:1163	N-linked glycosylation	1142:1163	N-linked glycosylation	1142:1163	However, without N-linked glycosylation, hTfR2 did not form the intersubunit disulfide bonds as efficiently as the wild type (WT).
23556518	2	81	theme	disease	326:332	arg1	form					300:303	a rare form	293:303	a rare form of the iron overload disease, hereditary hemochromatosis	293:360	Mutations in TfR2 can lead to a rare form of the iron overload disease, hereditary hemochromatosis.
23556518	10	82	theme	different	1411:1419	arg1	manner					1404:1409	manner	1404:1409	manner different from that of the WT in response to holo-Tf treatment	1404:1472	We further provide evidence that the unglycosylated hTfR2 behaved in manner different from that of the WT in response to holo-Tf treatment.
23556518	6	83	theme	site-directed	691:703	arg1	mutagenesis					705:715	site-directed mutagenesis	691:715	site-directed mutagenesis	691:715	In this study, by employing site-directed mutagenesis to remove glycosylation sites of hTfR2 individually or in combination, we found that hTfR2 was glycosylated at Asn 240, 339, and 754, while the consensus sequence for N-linked glycosylation at Asn 540 was not utilized.
23556518	3	84	theme	iron	450:453	arg1	hepcidin					475:482	the iron regulatory hormone, hepcidin	446:482	hepcidin	475:482	TfR2 is proposed to sense body iron levels and increase the level of expression of the iron regulatory hormone, hepcidin.
23556518	4	85	theme	glycosylation	550:562	arg1	sites					564:568	four potential Asn-linked (N-linked) glycosylation sites	513:568	four potential Asn-linked (N-linked) glycosylation sites on its ectodomain	513:586	Human TfR2 (hTfR2) contains four potential Asn-linked (N-linked) glycosylation sites on its ectodomain.
23556518	11	86	theme	iron-sensing	1494:1505	arg1	function					1507:1514	the putative iron-sensing function	1481:1514	the putative iron-sensing function of TfR2	1481:1522	Thus, the putative iron-sensing function of TfR2 could not be achieved in the absence of N-linked oligosaccharides.
23556518	2	87	theme	rare	295:298	arg1	form					300:303	a rare form	293:303	a rare form of the iron overload disease, hereditary hemochromatosis	293:360	Mutations in TfR2 can lead to a rare form of the iron overload disease, hereditary hemochromatosis.
23556518	1	88	theme	transferrin	217:227	arg1	family					243:248	the transferrin receptor-like family	213:248	the transferrin receptor-like family of proteins	213:260	Transferrin receptor 2 (TfR2) is a member of the transferrin receptor-like family of proteins.
23556518	3	89	theme	hepcidin	475:482	arg1	expression					432:441	expression	432:441	expression of the iron regulatory hormone, hepcidin	432:482	TfR2 is proposed to sense body iron levels and increase the level of expression of the iron regulatory hormone, hepcidin.
23556518	9	90	theme	hTfR2	1293:1297	arg1	form					1285:1288	the unglycosylated form	1266:1288	the unglycosylated form of hTfR2	1266:1297	Moreover, the unglycosylated form of hTfR2 could not be stabilized by holo-Tf.
23503728	0	0	theme	asparagine-linked	84:100	arg1	glycosylation					102:114	asparagine-linked glycosylation	84:114	asparagine-linked glycosylation	84:114	Surface expression and function of Cav3.2 T-type calcium channels are controlled by asparagine-linked glycosylation.
23503728	7	1	theme	aberrant	1300:1307	arg1	upregulation					1309:1320	aberrant upregulation	1300:1320	aberrant upregulation of T-type channel activity	1300:1347	Our data suggest that N-linked glycosylation of T-type channels may play an important role in aberrant upregulation of T-type channel activity in response to glucose elevations.
23503728	3	2	link	-linked	480:486	arg1	glycosylation					488:500	asparagine (N)-linked glycosylation	466:500	asparagine (N)-linked glycosylation	466:500	In the present study, we looked at the role of asparagine (N)-linked glycosylation on human Cav3.2 T-type channel expression and function.
23503728	1	3	theme	neuronal	187:194	arg1	physiology					196:205	neuronal physiology	187:205	neuronal physiology where they control cellular excitability and synaptic transmission	187:272	Low-voltage-activated T-type calcium channels play important roles in neuronal physiology where they control cellular excitability and synaptic transmission.
23503728	3	4	from	role	458:461	arg1	expression					533:542	human Cav3.2 T-type channel expression	505:542	human Cav3.2 T-type channel expression	505:542	In the present study, we looked at the role of asparagine (N)-linked glycosylation on human Cav3.2 T-type channel expression and function.
23503728	3	4	from	role	458:461	arg1	function					548:555	function	548:555	function	548:555	In the present study, we looked at the role of asparagine (N)-linked glycosylation on human Cav3.2 T-type channel expression and function.
23503728	4	5	from	Manipulation	558:569	arg1	cells					587:591	cells	587:591	cells expressing a recombinant Cav3.2 channel	587:631	Manipulation of N-glycans on cells expressing a recombinant Cav3.2 channel revealed that N-linked glycosylation is critical for proper functional expression of the channel.
23503728	5	6	theme	channel	984:990	arg1	activity					992:999	channel activity	984:999	channel activity	984:999	Using site-directed mutagenesis to disrupt the canonical N-linked glycosylation sites of Cav3.2 channel, we show that glycosylation at asparagine N192 is critical for channel expression at the surface, whereas glycosylation at asparagine N1466 controls channel activity.
23503728	5	7	link	N-linked	788:795	arg1	channel					827:833	Cav3.2 channel	820:833	Cav3.2 channel	820:833	Using site-directed mutagenesis to disrupt the canonical N-linked glycosylation sites of Cav3.2 channel, we show that glycosylation at asparagine N192 is critical for channel expression at the surface, whereas glycosylation at asparagine N1466 controls channel activity.
23503728	5	7	link	N-linked	788:795	arg1	sites					811:815	the canonical N-linked glycosylation sites	774:815	the canonical N-linked glycosylation sites of Cav3.2 channel	774:833	Using site-directed mutagenesis to disrupt the canonical N-linked glycosylation sites of Cav3.2 channel, we show that glycosylation at asparagine N192 is critical for channel expression at the surface, whereas glycosylation at asparagine N1466 controls channel activity.
23503728	5	8	gly	glycosylation	941:953	arg2	N1466					969:973	asparagine N1466	958:973	asparagine N1466	958:973	Using site-directed mutagenesis to disrupt the canonical N-linked glycosylation sites of Cav3.2 channel, we show that glycosylation at asparagine N192 is critical for channel expression at the surface, whereas glycosylation at asparagine N1466 controls channel activity.
23503728	5	8	gly	glycosylation	941:953	arg1	N1466					969:973	asparagine N1466	958:973	asparagine N1466	958:973	Using site-directed mutagenesis to disrupt the canonical N-linked glycosylation sites of Cav3.2 channel, we show that glycosylation at asparagine N192 is critical for channel expression at the surface, whereas glycosylation at asparagine N1466 controls channel activity.
23503728	7	9	theme	T-type	1254:1259	arg1	channels					1261:1268	T-type channels	1254:1268	T-type channels	1254:1268	Our data suggest that N-linked glycosylation of T-type channels may play an important role in aberrant upregulation of T-type channel activity in response to glucose elevations.
23503728	6	10	gly	glycosylation	1041:1053	arg1	Cav3.2					1058:1063	Cav3.2	1058:1063	Cav3.2	1058:1063	Moreover, we demonstrate that N-linked glycosylation of Cav3.2 not only controls surface expression and activity of the channel but also underlies glucose-dependent potentiation of T-type Ca(2+) current.
23503728	2	11	theme	pathophysiological	342:359	arg1	conditions					361:370	various pathophysiological conditions	334:370	various pathophysiological conditions such as pain arising from diabetic neuropathy	334:416	Alteration in T-type channel expression has been linked to various pathophysiological conditions such as pain arising from diabetic neuropathy.
23503728	2	11	theme	pathophysiological	342:359	arg1	pain					380:383	pain	380:383	pain arising from diabetic neuropathy	380:416	Alteration in T-type channel expression has been linked to various pathophysiological conditions such as pain arising from diabetic neuropathy.
23503728	6	12	theme	surface	1083:1089	arg1	expression					1091:1100	surface expression	1083:1100	surface expression	1083:1100	Moreover, we demonstrate that N-linked glycosylation of Cav3.2 not only controls surface expression and activity of the channel but also underlies glucose-dependent potentiation of T-type Ca(2+) current.
23503728	3	13	theme	present	426:432	arg1	study					434:438	the present study	422:438	the present study	422:438	In the present study, we looked at the role of asparagine (N)-linked glycosylation on human Cav3.2 T-type channel expression and function.
23503728	5	14	theme	site-directed	737:749	arg1	mutagenesis					751:761	site-directed mutagenesis	737:761	site-directed mutagenesis	737:761	Using site-directed mutagenesis to disrupt the canonical N-linked glycosylation sites of Cav3.2 channel, we show that glycosylation at asparagine N192 is critical for channel expression at the surface, whereas glycosylation at asparagine N1466 controls channel activity.
23503728	5	15	from	N1466	969:973	arg1	glycosylation					941:953	glycosylation	941:953	glycosylation at asparagine N1466	941:973	Using site-directed mutagenesis to disrupt the canonical N-linked glycosylation sites of Cav3.2 channel, we show that glycosylation at asparagine N192 is critical for channel expression at the surface, whereas glycosylation at asparagine N1466 controls channel activity.
23503728	2	16	theme	various	334:340	arg1	conditions					361:370	various pathophysiological conditions	334:370	various pathophysiological conditions such as pain arising from diabetic neuropathy	334:416	Alteration in T-type channel expression has been linked to various pathophysiological conditions such as pain arising from diabetic neuropathy.
23503728	2	16	theme	various	334:340	arg1	pain					380:383	pain	380:383	pain arising from diabetic neuropathy	380:416	Alteration in T-type channel expression has been linked to various pathophysiological conditions such as pain arising from diabetic neuropathy.
23503728	2	17	from	Alteration	275:284	arg1	expression					304:313	T-type channel expression	289:313	T-type channel expression	289:313	Alteration in T-type channel expression has been linked to various pathophysiological conditions such as pain arising from diabetic neuropathy.
23503728	3	18	theme	channel	525:531	arg1	expression					533:542	human Cav3.2 T-type channel expression	505:542	human Cav3.2 T-type channel expression	505:542	In the present study, we looked at the role of asparagine (N)-linked glycosylation on human Cav3.2 T-type channel expression and function.
23503728	5	19	theme	channel	827:833	arg1	channel					827:833	Cav3.2 channel	820:833	Cav3.2 channel	820:833	Using site-directed mutagenesis to disrupt the canonical N-linked glycosylation sites of Cav3.2 channel, we show that glycosylation at asparagine N192 is critical for channel expression at the surface, whereas glycosylation at asparagine N1466 controls channel activity.
23503728	5	19	theme	channel	827:833	arg1	sites					811:815	the canonical N-linked glycosylation sites	774:815	the canonical N-linked glycosylation sites of Cav3.2 channel	774:833	Using site-directed mutagenesis to disrupt the canonical N-linked glycosylation sites of Cav3.2 channel, we show that glycosylation at asparagine N192 is critical for channel expression at the surface, whereas glycosylation at asparagine N1466 controls channel activity.
23503728	4	20	theme	functional	693:702	arg1	expression					704:713	proper functional expression	686:713	proper functional expression of the channel	686:728	Manipulation of N-glycans on cells expressing a recombinant Cav3.2 channel revealed that N-linked glycosylation is critical for proper functional expression of the channel.
23503728	5	21	gly	glycosylation	849:861	arg1	N192					877:880	asparagine N192	866:880	asparagine N192	866:880	Using site-directed mutagenesis to disrupt the canonical N-linked glycosylation sites of Cav3.2 channel, we show that glycosylation at asparagine N192 is critical for channel expression at the surface, whereas glycosylation at asparagine N1466 controls channel activity.
23503728	5	21	gly	glycosylation	849:861	arg1	channel					898:904	channel expression	898:915	channel expression at the surface	898:930	Using site-directed mutagenesis to disrupt the canonical N-linked glycosylation sites of Cav3.2 channel, we show that glycosylation at asparagine N192 is critical for channel expression at the surface, whereas glycosylation at asparagine N1466 controls channel activity.
23503728	5	21	gly	glycosylation	849:861	arg2	N192					877:880	asparagine N192	866:880	asparagine N192	866:880	Using site-directed mutagenesis to disrupt the canonical N-linked glycosylation sites of Cav3.2 channel, we show that glycosylation at asparagine N192 is critical for channel expression at the surface, whereas glycosylation at asparagine N1466 controls channel activity.
23503728	6	22	theme	Ca	1190:1191	arg1	current					1197:1203	T-type Ca(2+) current	1183:1203	T-type Ca(2+) current	1183:1203	Moreover, we demonstrate that N-linked glycosylation of Cav3.2 not only controls surface expression and activity of the channel but also underlies glucose-dependent potentiation of T-type Ca(2+) current.
23503728	4	23	theme	N-linked	647:654	arg1	glycosylation					656:668	N-linked glycosylation	647:668	N-linked glycosylation	647:668	Manipulation of N-glycans on cells expressing a recombinant Cav3.2 channel revealed that N-linked glycosylation is critical for proper functional expression of the channel.
23503728	4	24	theme	channel	722:728	arg1	expression					704:713	proper functional expression	686:713	proper functional expression of the channel	686:728	Manipulation of N-glycans on cells expressing a recombinant Cav3.2 channel revealed that N-linked glycosylation is critical for proper functional expression of the channel.
23503728	7	25	theme	glucose	1364:1370	arg1	elevations					1372:1381	glucose elevations	1364:1381	glucose elevations	1364:1381	Our data suggest that N-linked glycosylation of T-type channels may play an important role in aberrant upregulation of T-type channel activity in response to glucose elevations.
23503728	0	26	theme	Surface	0:6	arg1	expression					8:17	Surface expression	0:17	Surface expression	0:17	Surface expression and function of Cav3.2 T-type calcium channels are controlled by asparagine-linked glycosylation.
23503728	4	27	theme	recombinant	606:616	arg1	channel					625:631	a recombinant Cav3.2 channel	604:631	a recombinant Cav3.2 channel	604:631	Manipulation of N-glycans on cells expressing a recombinant Cav3.2 channel revealed that N-linked glycosylation is critical for proper functional expression of the channel.
23503728	1	28	theme	cellular	226:233	arg1	excitability					235:246	cellular excitability	226:246	cellular excitability	226:246	Low-voltage-activated T-type calcium channels play important roles in neuronal physiology where they control cellular excitability and synaptic transmission.
23503728	5	29	theme	channel	898:904	arg1	expression					906:915	channel expression	898:915	channel expression at the surface	898:930	Using site-directed mutagenesis to disrupt the canonical N-linked glycosylation sites of Cav3.2 channel, we show that glycosylation at asparagine N192 is critical for channel expression at the surface, whereas glycosylation at asparagine N1466 controls channel activity.
23503728	5	30	theme	canonical	778:786	arg1	channel					827:833	Cav3.2 channel	820:833	Cav3.2 channel	820:833	Using site-directed mutagenesis to disrupt the canonical N-linked glycosylation sites of Cav3.2 channel, we show that glycosylation at asparagine N192 is critical for channel expression at the surface, whereas glycosylation at asparagine N1466 controls channel activity.
23503728	5	30	theme	canonical	778:786	arg1	sites					811:815	the canonical N-linked glycosylation sites	774:815	the canonical N-linked glycosylation sites of Cav3.2 channel	774:833	Using site-directed mutagenesis to disrupt the canonical N-linked glycosylation sites of Cav3.2 channel, we show that glycosylation at asparagine N192 is critical for channel expression at the surface, whereas glycosylation at asparagine N1466 controls channel activity.
23503728	4	31	gly	glycosylation	656:668	arg1	channel					722:728	the channel	718:728	the channel	718:728	Manipulation of N-glycans on cells expressing a recombinant Cav3.2 channel revealed that N-linked glycosylation is critical for proper functional expression of the channel.
23503728	1	32	theme	Low-voltage-activated	117:137	arg1	channels					154:161	Low-voltage-activated T-type calcium channels	117:161	Low-voltage-activated T-type calcium channels	117:161	Low-voltage-activated T-type calcium channels play important roles in neuronal physiology where they control cellular excitability and synaptic transmission.
23503728	6	33	theme	glucose-dependent	1149:1165	arg1	potentiation					1167:1178	glucose-dependent potentiation	1149:1178	glucose-dependent potentiation of T-type Ca(2+) current	1149:1203	Moreover, we demonstrate that N-linked glycosylation of Cav3.2 not only controls surface expression and activity of the channel but also underlies glucose-dependent potentiation of T-type Ca(2+) current.
23503728	7	34	theme	channels	1261:1268	arg1	glycosylation					1237:1249	N-linked glycosylation	1228:1249	N-linked glycosylation of T-type channels	1228:1268	Our data suggest that N-linked glycosylation of T-type channels may play an important role in aberrant upregulation of T-type channel activity in response to glucose elevations.
23503728	6	35	theme	Cav3.2	1058:1063	arg1	glycosylation					1041:1053	N-linked glycosylation	1032:1053	N-linked glycosylation of Cav3.2	1032:1063	Moreover, we demonstrate that N-linked glycosylation of Cav3.2 not only controls surface expression and activity of the channel but also underlies glucose-dependent potentiation of T-type Ca(2+) current.
23503728	5	36	theme	N-linked	788:795	arg1	channel					827:833	Cav3.2 channel	820:833	Cav3.2 channel	820:833	Using site-directed mutagenesis to disrupt the canonical N-linked glycosylation sites of Cav3.2 channel, we show that glycosylation at asparagine N192 is critical for channel expression at the surface, whereas glycosylation at asparagine N1466 controls channel activity.
23503728	5	36	theme	N-linked	788:795	arg1	sites					811:815	the canonical N-linked glycosylation sites	774:815	the canonical N-linked glycosylation sites of Cav3.2 channel	774:833	Using site-directed mutagenesis to disrupt the canonical N-linked glycosylation sites of Cav3.2 channel, we show that glycosylation at asparagine N192 is critical for channel expression at the surface, whereas glycosylation at asparagine N1466 controls channel activity.
23503728	1	37	theme	T-type	139:144	arg1	channels					154:161	Low-voltage-activated T-type calcium channels	117:161	Low-voltage-activated T-type calcium channels	117:161	Low-voltage-activated T-type calcium channels play important roles in neuronal physiology where they control cellular excitability and synaptic transmission.
23503728	3	38	theme	human	505:509	arg1	expression					533:542	human Cav3.2 T-type channel expression	505:542	human Cav3.2 T-type channel expression	505:542	In the present study, we looked at the role of asparagine (N)-linked glycosylation on human Cav3.2 T-type channel expression and function.
23503728	0	39	theme	Cav3.2 T-type	35:47	arg1	channels					57:64	Cav3.2 T-type calcium channels	35:64	Cav3.2 T-type calcium channels	35:64	Surface expression and function of Cav3.2 T-type calcium channels are controlled by asparagine-linked glycosylation.
23503728	4	40	theme	Cav3.2	618:623	arg1	channel					625:631	a recombinant Cav3.2 channel	604:631	a recombinant Cav3.2 channel	604:631	Manipulation of N-glycans on cells expressing a recombinant Cav3.2 channel revealed that N-linked glycosylation is critical for proper functional expression of the channel.
23503728	5	41	theme	glycosylation	797:809	arg1	channel					827:833	Cav3.2 channel	820:833	Cav3.2 channel	820:833	Using site-directed mutagenesis to disrupt the canonical N-linked glycosylation sites of Cav3.2 channel, we show that glycosylation at asparagine N192 is critical for channel expression at the surface, whereas glycosylation at asparagine N1466 controls channel activity.
23503728	5	41	theme	glycosylation	797:809	arg1	sites					811:815	the canonical N-linked glycosylation sites	774:815	the canonical N-linked glycosylation sites of Cav3.2 channel	774:833	Using site-directed mutagenesis to disrupt the canonical N-linked glycosylation sites of Cav3.2 channel, we show that glycosylation at asparagine N192 is critical for channel expression at the surface, whereas glycosylation at asparagine N1466 controls channel activity.
23503728	3	42	theme	-linked	480:486	arg1	glycosylation					488:500	asparagine (N)-linked glycosylation	466:500	asparagine (N)-linked glycosylation	466:500	In the present study, we looked at the role of asparagine (N)-linked glycosylation on human Cav3.2 T-type channel expression and function.
23503728	2	43	theme	T-type	289:294	arg1	expression					304:313	T-type channel expression	289:313	T-type channel expression	289:313	Alteration in T-type channel expression has been linked to various pathophysiological conditions such as pain arising from diabetic neuropathy.
23503728	5	44	theme	asparagine	958:967	arg1	N1466					969:973	asparagine N1466	958:973	asparagine N1466	958:973	Using site-directed mutagenesis to disrupt the canonical N-linked glycosylation sites of Cav3.2 channel, we show that glycosylation at asparagine N192 is critical for channel expression at the surface, whereas glycosylation at asparagine N1466 controls channel activity.
23503728	1	45	theme	synaptic	252:259	arg1	transmission					261:272	synaptic transmission	252:272	synaptic transmission	252:272	Low-voltage-activated T-type calcium channels play important roles in neuronal physiology where they control cellular excitability and synaptic transmission.
23503728	5	46	theme	asparagine	866:875	arg1	N192					877:880	asparagine N192	866:880	asparagine N192	866:880	Using site-directed mutagenesis to disrupt the canonical N-linked glycosylation sites of Cav3.2 channel, we show that glycosylation at asparagine N192 is critical for channel expression at the surface, whereas glycosylation at asparagine N1466 controls channel activity.
23503728	7	47	gly	glycosylation	1237:1249	arg1	channels					1261:1268	T-type channels	1254:1268	T-type channels	1254:1268	Our data suggest that N-linked glycosylation of T-type channels may play an important role in aberrant upregulation of T-type channel activity in response to glucose elevations.
23503728	0	48	link	asparagine-linked	84:100	arg1	glycosylation					102:114	asparagine-linked glycosylation	84:114	asparagine-linked glycosylation	84:114	Surface expression and function of Cav3.2 T-type calcium channels are controlled by asparagine-linked glycosylation.
23503728	3	49	theme	glycosylation	488:500	arg1	role					458:461	the role	454:461	the role of asparagine (N)-linked glycosylation on human Cav3.2 T-type channel expression and function	454:555	In the present study, we looked at the role of asparagine (N)-linked glycosylation on human Cav3.2 T-type channel expression and function.
23503728	0	50	theme	channels	57:64	arg1	function					23:30	function	23:30	function	23:30	Surface expression and function of Cav3.2 T-type calcium channels are controlled by asparagine-linked glycosylation.
23503728	0	50	theme	channels	57:64	arg1	expression					8:17	Surface expression	0:17	Surface expression	0:17	Surface expression and function of Cav3.2 T-type calcium channels are controlled by asparagine-linked glycosylation.
23503728	4	51	theme	N-glycans	574:582	arg1	Manipulation					558:569	Manipulation	558:569	Manipulation of N-glycans on cells expressing a recombinant Cav3.2 channel	558:631	Manipulation of N-glycans on cells expressing a recombinant Cav3.2 channel revealed that N-linked glycosylation is critical for proper functional expression of the channel.
23503728	1	52	theme	calcium	146:152	arg1	channels					154:161	Low-voltage-activated T-type calcium channels	117:161	Low-voltage-activated T-type calcium channels	117:161	Low-voltage-activated T-type calcium channels play important roles in neuronal physiology where they control cellular excitability and synaptic transmission.
23503728	0	53	theme	calcium	49:55	arg1	channels					57:64	Cav3.2 T-type calcium channels	35:64	Cav3.2 T-type calcium channels	35:64	Surface expression and function of Cav3.2 T-type calcium channels are controlled by asparagine-linked glycosylation.
23503728	2	54	attach	linked	324:329	arg1	conditions					361:370	various pathophysiological conditions	334:370	various pathophysiological conditions such as pain arising from diabetic neuropathy	334:416	Alteration in T-type channel expression has been linked to various pathophysiological conditions such as pain arising from diabetic neuropathy.
23503728	2	54	attach	linked	324:329	arg2	Alteration					275:284	Alteration	275:284	Alteration in T-type channel expression	275:313	Alteration in T-type channel expression has been linked to various pathophysiological conditions such as pain arising from diabetic neuropathy.
23503728	2	54	attach	linked	324:329	arg1	pain					380:383	pain	380:383	pain arising from diabetic neuropathy	380:416	Alteration in T-type channel expression has been linked to various pathophysiological conditions such as pain arising from diabetic neuropathy.
23503728	7	55	theme	important	1282:1290	arg1	role					1292:1295	an important role	1279:1295	an important role	1279:1295	Our data suggest that N-linked glycosylation of T-type channels may play an important role in aberrant upregulation of T-type channel activity in response to glucose elevations.
23503728	7	56	theme	activity	1340:1347	arg1	upregulation					1309:1320	aberrant upregulation	1300:1320	aberrant upregulation of T-type channel activity	1300:1347	Our data suggest that N-linked glycosylation of T-type channels may play an important role in aberrant upregulation of T-type channel activity in response to glucose elevations.
23503728	2	57	theme	diabetic	398:405	arg1	neuropathy					407:416	diabetic neuropathy	398:416	diabetic neuropathy	398:416	Alteration in T-type channel expression has been linked to various pathophysiological conditions such as pain arising from diabetic neuropathy.
23503728	6	58	link	N-linked	1032:1039	arg1	glycosylation					1041:1053	N-linked glycosylation	1032:1053	N-linked glycosylation of Cav3.2	1032:1063	Moreover, we demonstrate that N-linked glycosylation of Cav3.2 not only controls surface expression and activity of the channel but also underlies glucose-dependent potentiation of T-type Ca(2+) current.
23503728	4	59	link	N-linked	647:654	arg1	glycosylation					656:668	N-linked glycosylation	647:668	N-linked glycosylation	647:668	Manipulation of N-glycans on cells expressing a recombinant Cav3.2 channel revealed that N-linked glycosylation is critical for proper functional expression of the channel.
23503728	7	60	theme	N-linked	1228:1235	arg1	glycosylation					1237:1249	N-linked glycosylation	1228:1249	N-linked glycosylation of T-type channels	1228:1268	Our data suggest that N-linked glycosylation of T-type channels may play an important role in aberrant upregulation of T-type channel activity in response to glucose elevations.
23503728	7	61	link	N-linked	1228:1235	arg1	glycosylation					1237:1249	N-linked glycosylation	1228:1249	N-linked glycosylation of T-type channels	1228:1268	Our data suggest that N-linked glycosylation of T-type channels may play an important role in aberrant upregulation of T-type channel activity in response to glucose elevations.
23503728	3	62	theme	Cav3.2 T-type	511:523	arg1	expression					533:542	human Cav3.2 T-type channel expression	505:542	human Cav3.2 T-type channel expression	505:542	In the present study, we looked at the role of asparagine (N)-linked glycosylation on human Cav3.2 T-type channel expression and function.
23503728	6	63	theme	channel	1122:1128	arg1	expression					1091:1100	surface expression	1083:1100	surface expression	1083:1100	Moreover, we demonstrate that N-linked glycosylation of Cav3.2 not only controls surface expression and activity of the channel but also underlies glucose-dependent potentiation of T-type Ca(2+) current.
23503728	6	63	theme	channel	1122:1128	arg1	activity					1106:1113	activity	1106:1113	activity	1106:1113	Moreover, we demonstrate that N-linked glycosylation of Cav3.2 not only controls surface expression and activity of the channel but also underlies glucose-dependent potentiation of T-type Ca(2+) current.
23503728	5	64	from	surface	924:930	arg1	expression					906:915	channel expression	898:915	channel expression at the surface	898:930	Using site-directed mutagenesis to disrupt the canonical N-linked glycosylation sites of Cav3.2 channel, we show that glycosylation at asparagine N192 is critical for channel expression at the surface, whereas glycosylation at asparagine N1466 controls channel activity.
23503728	1	65	theme	important	168:176	arg1	roles					178:182	important roles	168:182	important roles	168:182	Low-voltage-activated T-type calcium channels play important roles in neuronal physiology where they control cellular excitability and synaptic transmission.
23503728	7	66	dep	elevations	1372:1381	arg1	response					1352:1359	response	1352:1359	response	1352:1359	Our data suggest that N-linked glycosylation of T-type channels may play an important role in aberrant upregulation of T-type channel activity in response to glucose elevations.
23503728	5	67	gly	glycosylation	797:809	arg2	sites					811:815	the canonical N-linked glycosylation sites	774:815	the canonical N-linked glycosylation sites of Cav3.2 channel	774:833	Using site-directed mutagenesis to disrupt the canonical N-linked glycosylation sites of Cav3.2 channel, we show that glycosylation at asparagine N192 is critical for channel expression at the surface, whereas glycosylation at asparagine N1466 controls channel activity.
23503728	5	67	gly	glycosylation	797:809	arg1	channel					827:833	Cav3.2 channel	820:833	Cav3.2 channel	820:833	Using site-directed mutagenesis to disrupt the canonical N-linked glycosylation sites of Cav3.2 channel, we show that glycosylation at asparagine N192 is critical for channel expression at the surface, whereas glycosylation at asparagine N1466 controls channel activity.
23503728	5	67	gly	glycosylation	797:809	arg2	channel					827:833	Cav3.2 channel	820:833	Cav3.2 channel	820:833	Using site-directed mutagenesis to disrupt the canonical N-linked glycosylation sites of Cav3.2 channel, we show that glycosylation at asparagine N192 is critical for channel expression at the surface, whereas glycosylation at asparagine N1466 controls channel activity.
23503728	6	68	theme	current	1197:1203	arg1	potentiation					1167:1178	glucose-dependent potentiation	1149:1178	glucose-dependent potentiation of T-type Ca(2+) current	1149:1203	Moreover, we demonstrate that N-linked glycosylation of Cav3.2 not only controls surface expression and activity of the channel but also underlies glucose-dependent potentiation of T-type Ca(2+) current.
23503728	6	69	theme	T-type	1183:1188	arg1	current					1197:1203	T-type Ca(2+) current	1183:1203	T-type Ca(2+) current	1183:1203	Moreover, we demonstrate that N-linked glycosylation of Cav3.2 not only controls surface expression and activity of the channel but also underlies glucose-dependent potentiation of T-type Ca(2+) current.
23503728	4	70	theme	proper	686:691	arg1	expression					704:713	proper functional expression	686:713	proper functional expression of the channel	686:728	Manipulation of N-glycans on cells expressing a recombinant Cav3.2 channel revealed that N-linked glycosylation is critical for proper functional expression of the channel.
23503728	7	71	theme	T-type	1325:1330	arg1	activity					1340:1347	T-type channel activity	1325:1347	T-type channel activity	1325:1347	Our data suggest that N-linked glycosylation of T-type channels may play an important role in aberrant upregulation of T-type channel activity in response to glucose elevations.
23503728	5	72	from	N192	877:880	arg1	glycosylation					849:861	glycosylation	849:861	glycosylation at asparagine N192	849:880	Using site-directed mutagenesis to disrupt the canonical N-linked glycosylation sites of Cav3.2 channel, we show that glycosylation at asparagine N192 is critical for channel expression at the surface, whereas glycosylation at asparagine N1466 controls channel activity.
23503728	2	73	theme	channel	296:302	arg1	expression					304:313	T-type channel expression	289:313	T-type channel expression	289:313	Alteration in T-type channel expression has been linked to various pathophysiological conditions such as pain arising from diabetic neuropathy.
23503728	7	74	theme	channel	1332:1338	arg1	activity					1340:1347	T-type channel activity	1325:1347	T-type channel activity	1325:1347	Our data suggest that N-linked glycosylation of T-type channels may play an important role in aberrant upregulation of T-type channel activity in response to glucose elevations.
23503728	6	75	theme	N-linked	1032:1039	arg1	glycosylation					1041:1053	N-linked glycosylation	1032:1053	N-linked glycosylation of Cav3.2	1032:1063	Moreover, we demonstrate that N-linked glycosylation of Cav3.2 not only controls surface expression and activity of the channel but also underlies glucose-dependent potentiation of T-type Ca(2+) current.
21669976	2	0	gly	O-glycosylated	252:265	arg1	subunit					241:247	the KCNE1 regulatory subunit	220:247	the KCNE1 regulatory subunit	220:247	Here, we show the KCNE1 regulatory subunit is O-glycosylated with mucin-type glycans in vivo.
21669976	2	0	gly	O-glycosylated	252:265	arg1	O-glycosylated					252:265	O-glycosylated	252:265	O-glycosylated	252:265	Here, we show the KCNE1 regulatory subunit is O-glycosylated with mucin-type glycans in vivo.
21669976	3	1	theme	glycan	459:464	arg1	content					466:472	their glycan content	453:472	their glycan content	453:472	As O-linked glycosylation sites are not recognizable by sequence gazing, we designed a novel set of glycosylation mutants and KCNE chimeras and analysed their glycan content using deglycosylation enzymes.
21669976	5	2	theme	type	635:638	arg1	KCNE1					640:644	wild type KCNE1	630:644	wild type KCNE1	630:644	For wild type KCNE1, the overlapping N- and O-glycosylation sites are innocuous for subunit biogenesis; however, mutation of Thr-7 to a non-hydroxylated residue yielded mostly unglycosylated protein and a small fraction of mono-N-glycosylated protein.
21669976	5	3	dep	N-	663:664	arg1	sites					686:690	sites	686:690	sites	686:690	For wild type KCNE1, the overlapping N- and O-glycosylation sites are innocuous for subunit biogenesis; however, mutation of Thr-7 to a non-hydroxylated residue yielded mostly unglycosylated protein and a small fraction of mono-N-glycosylated protein.
21669976	6	4	theme	compounded	882:891	arg1	hypoglycosylation					893:909	The compounded hypoglycosylation	878:909	The compounded hypoglycosylation	878:909	The compounded hypoglycosylation was equally deleterious for KCNQ1–KCNE1 cell surface expression, demonstrating that KCNE1 O-glycosylation is a post-translational modification that is integral for the proper biogenesis and anterograde trafficking of the cardiac IKs complex.
21669976	6	4	theme	compounded	882:891	arg1	deleterious					923:933	deleterious	923:933	deleterious	923:933	The compounded hypoglycosylation was equally deleterious for KCNQ1–KCNE1 cell surface expression, demonstrating that KCNE1 O-glycosylation is a post-translational modification that is integral for the proper biogenesis and anterograde trafficking of the cardiac IKs complex.
21669976	6	5	theme	anterograde	1101:1111	arg1	trafficking					1113:1123	anterograde trafficking	1101:1123	anterograde trafficking	1101:1123	The compounded hypoglycosylation was equally deleterious for KCNQ1–KCNE1 cell surface expression, demonstrating that KCNE1 O-glycosylation is a post-translational modification that is integral for the proper biogenesis and anterograde trafficking of the cardiac IKs complex.
21669976	2	6	with	O-glycosylated	252:265	arg1	glycans					283:289	mucin-type glycans	272:289	mucin-type glycans	272:289	Here, we show the KCNE1 regulatory subunit is O-glycosylated with mucin-type glycans in vivo.
21669976	4	7	from	Thr-7	566:570	arg1	O-glycosylated					548:561	O-glycosylated	548:561	O-glycosylated	548:561	Our results show that KCNE1 is exclusively O-glycosylated at Thr-7, which is also required for N-glycosylation at Asn-5.
21669976	7	8	from	glycoforms	1272:1281	arg1	cells					1293:1297	native cells	1286:1297	native cells	1286:1297	The enzymatic assays and panel of glycosylation mutants used here will be valuable for identifying the different KCNE1 glycoforms in native cells and determining the roles N- and O-glycosylation play in KCNQ1–KCNE1 function and localization in cardiomyocytes,
21669976	3	9	link	O-linked	303:310	arg1	sites					326:330	O-linked glycosylation sites	303:330	O-linked glycosylation sites	303:330	As O-linked glycosylation sites are not recognizable by sequence gazing, we designed a novel set of glycosylation mutants and KCNE chimeras and analysed their glycan content using deglycosylation enzymes.
21669976	7	10	theme	native	1286:1291	arg1	cells					1293:1297	native cells	1286:1297	native cells	1286:1297	The enzymatic assays and panel of glycosylation mutants used here will be valuable for identifying the different KCNE1 glycoforms in native cells and determining the roles N- and O-glycosylation play in KCNQ1–KCNE1 function and localization in cardiomyocytes,
21669976	5	11	theme	wild	630:633	arg1	KCNE1					640:644	wild type KCNE1	630:644	wild type KCNE1	630:644	For wild type KCNE1, the overlapping N- and O-glycosylation sites are innocuous for subunit biogenesis; however, mutation of Thr-7 to a non-hydroxylated residue yielded mostly unglycosylated protein and a small fraction of mono-N-glycosylated protein.
21669976	7	12	theme	KCNE1	1266:1270	arg1	glycoforms					1272:1281	the different KCNE1 glycoforms	1252:1281	the different KCNE1 glycoforms in native cells	1252:1297	The enzymatic assays and panel of glycosylation mutants used here will be valuable for identifying the different KCNE1 glycoforms in native cells and determining the roles N- and O-glycosylation play in KCNQ1–KCNE1 function and localization in cardiomyocytes,
21669976	5	13	theme	protein	869:875	arg1	protein					817:823	mostly unglycosylated protein	795:823	mostly unglycosylated protein	795:823	For wild type KCNE1, the overlapping N- and O-glycosylation sites are innocuous for subunit biogenesis; however, mutation of Thr-7 to a non-hydroxylated residue yielded mostly unglycosylated protein and a small fraction of mono-N-glycosylated protein.
21669976	5	13	theme	protein	869:875	arg1	fraction					837:844	a small fraction	829:844	a small fraction of mono-N-glycosylated protein	829:875	For wild type KCNE1, the overlapping N- and O-glycosylation sites are innocuous for subunit biogenesis; however, mutation of Thr-7 to a non-hydroxylated residue yielded mostly unglycosylated protein and a small fraction of mono-N-glycosylated protein.
21669976	5	14	theme	mono-N-glycosylated	849:867	arg1	protein					869:875	mono-N-glycosylated protein	849:875	mono-N-glycosylated protein	849:875	For wild type KCNE1, the overlapping N- and O-glycosylation sites are innocuous for subunit biogenesis; however, mutation of Thr-7 to a non-hydroxylated residue yielded mostly unglycosylated protein and a small fraction of mono-N-glycosylated protein.
21669976	6	15	theme	cardiac	1132:1138	arg1	complex					1144:1150	the cardiac IKs complex	1128:1150	the cardiac IKs complex	1128:1150	The compounded hypoglycosylation was equally deleterious for KCNQ1–KCNE1 cell surface expression, demonstrating that KCNE1 O-glycosylation is a post-translational modification that is integral for the proper biogenesis and anterograde trafficking of the cardiac IKs complex.
21669976	3	16	theme	O-linked	303:310	arg1	sites					326:330	O-linked glycosylation sites	303:330	O-linked glycosylation sites	303:330	As O-linked glycosylation sites are not recognizable by sequence gazing, we designed a novel set of glycosylation mutants and KCNE chimeras and analysed their glycan content using deglycosylation enzymes.
21669976	7	17	from	function	1368:1375	arg1	cardiomyocytes					1397:1410	cardiomyocytes	1397:1410	cardiomyocytes	1397:1410	The enzymatic assays and panel of glycosylation mutants used here will be valuable for identifying the different KCNE1 glycoforms in native cells and determining the roles N- and O-glycosylation play in KCNQ1–KCNE1 function and localization in cardiomyocytes,
21669976	3	18	theme	KCNE	426:429	arg1	chimeras					431:438	KCNE chimeras	426:438	KCNE chimeras	426:438	As O-linked glycosylation sites are not recognizable by sequence gazing, we designed a novel set of glycosylation mutants and KCNE chimeras and analysed their glycan content using deglycosylation enzymes.
21669976	1	19	theme	Post-translational	46:63	arg1	modifications					65:77	Post-translational modifications	46:77	Post-translational modifications of the KCNQ1–KCNE1 (Kv7) K+ channel complex	46:121	Post-translational modifications of the KCNQ1–KCNE1 (Kv7) K+ channel complex are vital for regulation of the cardiac IKs current and action potential duration.
21669976	6	20	theme	proper	1079:1084	arg1	biogenesis					1086:1095	proper biogenesis	1079:1095	proper biogenesis	1079:1095	The compounded hypoglycosylation was equally deleterious for KCNQ1–KCNE1 cell surface expression, demonstrating that KCNE1 O-glycosylation is a post-translational modification that is integral for the proper biogenesis and anterograde trafficking of the cardiac IKs complex.
21669976	3	21	theme	glycosylation	312:324	arg1	sites					326:330	O-linked glycosylation sites	303:330	O-linked glycosylation sites	303:330	As O-linked glycosylation sites are not recognizable by sequence gazing, we designed a novel set of glycosylation mutants and KCNE chimeras and analysed their glycan content using deglycosylation enzymes.
21669976	6	22	theme	IKs	1140:1142	arg1	complex					1144:1150	the cardiac IKs complex	1128:1150	the cardiac IKs complex	1128:1150	The compounded hypoglycosylation was equally deleterious for KCNQ1–KCNE1 cell surface expression, demonstrating that KCNE1 O-glycosylation is a post-translational modification that is integral for the proper biogenesis and anterograde trafficking of the cardiac IKs complex.
21669976	2	23	theme	KCNE1	224:228	arg1	subunit					241:247	the KCNE1 regulatory subunit	220:247	the KCNE1 regulatory subunit	220:247	Here, we show the KCNE1 regulatory subunit is O-glycosylated with mucin-type glycans in vivo.
21669976	2	23	theme	KCNE1	224:228	arg1	O-glycosylated					252:265	O-glycosylated	252:265	O-glycosylated	252:265	Here, we show the KCNE1 regulatory subunit is O-glycosylated with mucin-type glycans in vivo.
21669976	7	24	from	localization	1381:1392	arg1	cardiomyocytes					1397:1410	cardiomyocytes	1397:1410	cardiomyocytes	1397:1410	The enzymatic assays and panel of glycosylation mutants used here will be valuable for identifying the different KCNE1 glycoforms in native cells and determining the roles N- and O-glycosylation play in KCNQ1–KCNE1 function and localization in cardiomyocytes,
21669976	7	25	gly	glycoforms	1272:1281	arg2	cells					1293:1297	native cells	1286:1297	native cells	1286:1297	The enzymatic assays and panel of glycosylation mutants used here will be valuable for identifying the different KCNE1 glycoforms in native cells and determining the roles N- and O-glycosylation play in KCNQ1–KCNE1 function and localization in cardiomyocytes,
21669976	7	25	gly	glycoforms	1272:1281	arg1	KCNE1					1266:1270	the different KCNE1 glycoforms	1252:1281	the different KCNE1 glycoforms in native cells	1252:1297	The enzymatic assays and panel of glycosylation mutants used here will be valuable for identifying the different KCNE1 glycoforms in native cells and determining the roles N- and O-glycosylation play in KCNQ1–KCNE1 function and localization in cardiomyocytes,
21669976	7	26	theme	glycosylation	1187:1199	arg1	mutants					1201:1207	glycosylation mutants	1187:1207	glycosylation mutants	1187:1207	The enzymatic assays and panel of glycosylation mutants used here will be valuable for identifying the different KCNE1 glycoforms in native cells and determining the roles N- and O-glycosylation play in KCNQ1–KCNE1 function and localization in cardiomyocytes,
21669976	4	27	gly	N-glycosylation	600:614	arg2	Asn-5					619:623	Asn-5	619:623	Asn-5	619:623	Our results show that KCNE1 is exclusively O-glycosylated at Thr-7, which is also required for N-glycosylation at Asn-5.
21669976	4	27	gly	N-glycosylation	600:614	arg1	Asn-5					619:623	Asn-5	619:623	Asn-5	619:623	Our results show that KCNE1 is exclusively O-glycosylated at Thr-7, which is also required for N-glycosylation at Asn-5.
21669976	4	28	gly	O-glycosylated	548:561	arg2	Thr-7					566:570	Thr-7	566:570	Thr-7	566:570	Our results show that KCNE1 is exclusively O-glycosylated at Thr-7, which is also required for N-glycosylation at Asn-5.
21669976	4	28	gly	O-glycosylated	548:561	arg1	KCNE1					527:531	KCNE1	527:531	KCNE1	527:531	Our results show that KCNE1 is exclusively O-glycosylated at Thr-7, which is also required for N-glycosylation at Asn-5.
21669976	4	29	from	Asn-5	619:623	arg1	N-glycosylation					600:614	N-glycosylation	600:614	N-glycosylation at Asn-5	600:623	Our results show that KCNE1 is exclusively O-glycosylated at Thr-7, which is also required for N-glycosylation at Asn-5.
21669976	5	30	theme	small	831:835	arg1	fraction					837:844	a small fraction	829:844	a small fraction of mono-N-glycosylated protein	829:875	For wild type KCNE1, the overlapping N- and O-glycosylation sites are innocuous for subunit biogenesis; however, mutation of Thr-7 to a non-hydroxylated residue yielded mostly unglycosylated protein and a small fraction of mono-N-glycosylated protein.
21669976	3	31	theme	sequence	356:363	arg1	gazing					365:370	sequence gazing	356:370	sequence gazing	356:370	As O-linked glycosylation sites are not recognizable by sequence gazing, we designed a novel set of glycosylation mutants and KCNE chimeras and analysed their glycan content using deglycosylation enzymes.
21669976	7	32	theme	different	1256:1264	arg1	glycoforms					1272:1281	the different KCNE1 glycoforms	1252:1281	the different KCNE1 glycoforms in native cells	1252:1297	The enzymatic assays and panel of glycosylation mutants used here will be valuable for identifying the different KCNE1 glycoforms in native cells and determining the roles N- and O-glycosylation play in KCNQ1–KCNE1 function and localization in cardiomyocytes,
21669976	5	33	gly	unglycosylated	802:815	arg1	protein					817:823	mostly unglycosylated protein	795:823	mostly unglycosylated protein	795:823	For wild type KCNE1, the overlapping N- and O-glycosylation sites are innocuous for subunit biogenesis; however, mutation of Thr-7 to a non-hydroxylated residue yielded mostly unglycosylated protein and a small fraction of mono-N-glycosylated protein.
21669976	2	34	theme	mucin-type	272:281	arg1	glycans					283:289	mucin-type glycans	272:289	mucin-type glycans	272:289	Here, we show the KCNE1 regulatory subunit is O-glycosylated with mucin-type glycans in vivo.
21669976	1	35	theme	cardiac	155:161	arg1	current					167:173	the cardiac IKs current	151:173	the cardiac IKs current	151:173	Post-translational modifications of the KCNQ1–KCNE1 (Kv7) K+ channel complex are vital for regulation of the cardiac IKs current and action potential duration.
21669976	0	36	theme	cardiac	23:29	arg1	Ks					33:34	Ks	33:34	Ks	33:34	O-glycosylation of the cardiac I(Ks) complex.
21669976	0	36	theme	cardiac	23:29	arg1	I					31:31	cardiac I	23:31	the cardiac I(Ks) complex	19:43	O-glycosylation of the cardiac I(Ks) complex.
21669976	5	37	theme	overlapping	651:661	arg1	innocuous					696:704	innocuous	696:704	innocuous	696:704	For wild type KCNE1, the overlapping N- and O-glycosylation sites are innocuous for subunit biogenesis; however, mutation of Thr-7 to a non-hydroxylated residue yielded mostly unglycosylated protein and a small fraction of mono-N-glycosylated protein.
21669976	5	37	theme	overlapping	651:661	arg1	N-					663:664	the overlapping N-	647:664	the overlapping N-	647:664	For wild type KCNE1, the overlapping N- and O-glycosylation sites are innocuous for subunit biogenesis; however, mutation of Thr-7 to a non-hydroxylated residue yielded mostly unglycosylated protein and a small fraction of mono-N-glycosylated protein.
21669976	1	38	theme	KCNQ1–KCNE1	86:96	arg1	complex					115:121	the KCNQ1–KCNE1 (Kv7) K+ channel complex	82:121	the KCNQ1–KCNE1 (Kv7) K+ channel complex	82:121	Post-translational modifications of the KCNQ1–KCNE1 (Kv7) K+ channel complex are vital for regulation of the cardiac IKs current and action potential duration.
21669976	1	39	theme	IKs	163:165	arg1	current					167:173	the cardiac IKs current	151:173	the cardiac IKs current	151:173	Post-translational modifications of the KCNQ1–KCNE1 (Kv7) K+ channel complex are vital for regulation of the cardiac IKs current and action potential duration.
21669976	6	40	theme	surface	956:962	arg1	expression					964:973	KCNQ1–KCNE1 cell surface expression	939:973	KCNQ1–KCNE1 cell surface expression	939:973	The compounded hypoglycosylation was equally deleterious for KCNQ1–KCNE1 cell surface expression, demonstrating that KCNE1 O-glycosylation is a post-translational modification that is integral for the proper biogenesis and anterograde trafficking of the cardiac IKs complex.
21669976	2	41	theme	regulatory	230:239	arg1	subunit					241:247	the KCNE1 regulatory subunit	220:247	the KCNE1 regulatory subunit	220:247	Here, we show the KCNE1 regulatory subunit is O-glycosylated with mucin-type glycans in vivo.
21669976	2	41	theme	regulatory	230:239	arg1	O-glycosylated					252:265	O-glycosylated	252:265	O-glycosylated	252:265	Here, we show the KCNE1 regulatory subunit is O-glycosylated with mucin-type glycans in vivo.
21669976	6	42	dep	biogenesis	1086:1095	arg1	the					1075:1077	the	1075:1077	the	1075:1077	The compounded hypoglycosylation was equally deleterious for KCNQ1–KCNE1 cell surface expression, demonstrating that KCNE1 O-glycosylation is a post-translational modification that is integral for the proper biogenesis and anterograde trafficking of the cardiac IKs complex.
21669976	1	43	theme	current	167:173	arg1	regulation					137:146	regulation	137:146	regulation of the cardiac IKs current and action potential duration	137:203	Post-translational modifications of the KCNQ1–KCNE1 (Kv7) K+ channel complex are vital for regulation of the cardiac IKs current and action potential duration.
21669976	6	44	theme	cell	951:954	arg1	expression					964:973	KCNQ1–KCNE1 cell surface expression	939:973	KCNQ1–KCNE1 cell surface expression	939:973	The compounded hypoglycosylation was equally deleterious for KCNQ1–KCNE1 cell surface expression, demonstrating that KCNE1 O-glycosylation is a post-translational modification that is integral for the proper biogenesis and anterograde trafficking of the cardiac IKs complex.
21669976	3	45	gly	glycosylation	312:324	arg2	sites					326:330	O-linked glycosylation sites	303:330	O-linked glycosylation sites	303:330	As O-linked glycosylation sites are not recognizable by sequence gazing, we designed a novel set of glycosylation mutants and KCNE chimeras and analysed their glycan content using deglycosylation enzymes.
21669976	5	46	theme	unglycosylated	802:815	arg1	protein					817:823	mostly unglycosylated protein	795:823	mostly unglycosylated protein	795:823	For wild type KCNE1, the overlapping N- and O-glycosylation sites are innocuous for subunit biogenesis; however, mutation of Thr-7 to a non-hydroxylated residue yielded mostly unglycosylated protein and a small fraction of mono-N-glycosylated protein.
21669976	0	47	gly	O-glycosylation	0:14	arg1	complex					37:43	the cardiac I(Ks) complex	19:43	the cardiac I(Ks) complex	19:43	O-glycosylation of the cardiac I(Ks) complex.
21669976	3	48	theme	novel	387:391	arg1	set					393:395	a novel set	385:395	a novel set of glycosylation mutants and KCNE chimeras	385:438	As O-linked glycosylation sites are not recognizable by sequence gazing, we designed a novel set of glycosylation mutants and KCNE chimeras and analysed their glycan content using deglycosylation enzymes.
21669976	3	48	theme	novel	387:391	arg1	mutants					414:420	glycosylation mutants	400:420	glycosylation mutants	400:420	As O-linked glycosylation sites are not recognizable by sequence gazing, we designed a novel set of glycosylation mutants and KCNE chimeras and analysed their glycan content using deglycosylation enzymes.
21669976	3	48	theme	novel	387:391	arg1	chimeras					431:438	KCNE chimeras	426:438	KCNE chimeras	426:438	As O-linked glycosylation sites are not recognizable by sequence gazing, we designed a novel set of glycosylation mutants and KCNE chimeras and analysed their glycan content using deglycosylation enzymes.
21669976	3	49	theme	glycosylation	400:412	arg1	mutants					414:420	glycosylation mutants	400:420	glycosylation mutants	400:420	As O-linked glycosylation sites are not recognizable by sequence gazing, we designed a novel set of glycosylation mutants and KCNE chimeras and analysed their glycan content using deglycosylation enzymes.
21669976	0	50	theme	I	31:31	arg1	complex					37:43	the cardiac I(Ks) complex	19:43	the cardiac I(Ks) complex	19:43	O-glycosylation of the cardiac I(Ks) complex.
21669976	6	51	theme	KCNQ1–KCNE1	939:949	arg1	expression					964:973	KCNQ1–KCNE1 cell surface expression	939:973	KCNQ1–KCNE1 cell surface expression	939:973	The compounded hypoglycosylation was equally deleterious for KCNQ1–KCNE1 cell surface expression, demonstrating that KCNE1 O-glycosylation is a post-translational modification that is integral for the proper biogenesis and anterograde trafficking of the cardiac IKs complex.
21669976	6	52	theme	KCNE1	995:999	arg1	integral					1062:1069	integral	1062:1069	integral	1062:1069	The compounded hypoglycosylation was equally deleterious for KCNQ1–KCNE1 cell surface expression, demonstrating that KCNE1 O-glycosylation is a post-translational modification that is integral for the proper biogenesis and anterograde trafficking of the cardiac IKs complex.
21669976	6	52	theme	KCNE1	995:999	arg1	O-glycosylation					1001:1015	KCNE1 O-glycosylation	995:1015	KCNE1 O-glycosylation	995:1015	The compounded hypoglycosylation was equally deleterious for KCNQ1–KCNE1 cell surface expression, demonstrating that KCNE1 O-glycosylation is a post-translational modification that is integral for the proper biogenesis and anterograde trafficking of the cardiac IKs complex.
21669976	6	52	theme	KCNE1	995:999	arg1	modification					1041:1052	a post-translational modification	1020:1052	a post-translational modification that is integral for the proper biogenesis and anterograde trafficking of the cardiac IKs complex	1020:1150	The compounded hypoglycosylation was equally deleterious for KCNQ1–KCNE1 cell surface expression, demonstrating that KCNE1 O-glycosylation is a post-translational modification that is integral for the proper biogenesis and anterograde trafficking of the cardiac IKs complex.
21669976	5	53	theme	non-hydroxylated	762:777	arg1	residue					779:785	a non-hydroxylated residue	760:785	a non-hydroxylated residue	760:785	For wild type KCNE1, the overlapping N- and O-glycosylation sites are innocuous for subunit biogenesis; however, mutation of Thr-7 to a non-hydroxylated residue yielded mostly unglycosylated protein and a small fraction of mono-N-glycosylated protein.
21669976	1	54	theme	action	179:184	arg1	duration					196:203	action potential duration	179:203	action potential duration	179:203	Post-translational modifications of the KCNQ1–KCNE1 (Kv7) K+ channel complex are vital for regulation of the cardiac IKs current and action potential duration.
21669976	5	55	gly	mono-N-glycosylated	849:867	arg1	protein					869:875	mono-N-glycosylated protein	849:875	mono-N-glycosylated protein	849:875	For wild type KCNE1, the overlapping N- and O-glycosylation sites are innocuous for subunit biogenesis; however, mutation of Thr-7 to a non-hydroxylated residue yielded mostly unglycosylated protein and a small fraction of mono-N-glycosylated protein.
21669976	1	56	theme	Kv7	99:101	arg1	complex					115:121	the KCNQ1–KCNE1 (Kv7) K+ channel complex	82:121	the KCNQ1–KCNE1 (Kv7) K+ channel complex	82:121	Post-translational modifications of the KCNQ1–KCNE1 (Kv7) K+ channel complex are vital for regulation of the cardiac IKs current and action potential duration.
21669976	5	57	theme	Thr-7	751:755	arg1	mutation					739:746	mutation	739:746	mutation of Thr-7 to a non-hydroxylated residue	739:785	For wild type KCNE1, the overlapping N- and O-glycosylation sites are innocuous for subunit biogenesis; however, mutation of Thr-7 to a non-hydroxylated residue yielded mostly unglycosylated protein and a small fraction of mono-N-glycosylated protein.
21669976	3	58	theme	chimeras	431:438	arg1	set					393:395	a novel set	385:395	a novel set of glycosylation mutants and KCNE chimeras	385:438	As O-linked glycosylation sites are not recognizable by sequence gazing, we designed a novel set of glycosylation mutants and KCNE chimeras and analysed their glycan content using deglycosylation enzymes.
21669976	3	58	theme	chimeras	431:438	arg1	mutants					414:420	glycosylation mutants	400:420	glycosylation mutants	400:420	As O-linked glycosylation sites are not recognizable by sequence gazing, we designed a novel set of glycosylation mutants and KCNE chimeras and analysed their glycan content using deglycosylation enzymes.
21669976	3	58	theme	chimeras	431:438	arg1	chimeras					431:438	KCNE chimeras	426:438	KCNE chimeras	426:438	As O-linked glycosylation sites are not recognizable by sequence gazing, we designed a novel set of glycosylation mutants and KCNE chimeras and analysed their glycan content using deglycosylation enzymes.
21669976	6	59	theme	complex	1144:1150	arg1	biogenesis					1086:1095	proper biogenesis	1079:1095	proper biogenesis	1079:1095	The compounded hypoglycosylation was equally deleterious for KCNQ1–KCNE1 cell surface expression, demonstrating that KCNE1 O-glycosylation is a post-translational modification that is integral for the proper biogenesis and anterograde trafficking of the cardiac IKs complex.
21669976	6	59	theme	complex	1144:1150	arg1	trafficking					1113:1123	anterograde trafficking	1101:1123	anterograde trafficking	1101:1123	The compounded hypoglycosylation was equally deleterious for KCNQ1–KCNE1 cell surface expression, demonstrating that KCNE1 O-glycosylation is a post-translational modification that is integral for the proper biogenesis and anterograde trafficking of the cardiac IKs complex.
21669976	7	60	theme	enzymatic	1157:1165	arg1	assays					1167:1172	The enzymatic assays	1153:1172	The enzymatic assays	1153:1172	The enzymatic assays and panel of glycosylation mutants used here will be valuable for identifying the different KCNE1 glycoforms in native cells and determining the roles N- and O-glycosylation play in KCNQ1–KCNE1 function and localization in cardiomyocytes,
21669976	7	60	theme	enzymatic	1157:1165	arg1	valuable					1227:1234	valuable	1227:1234	valuable	1227:1234	The enzymatic assays and panel of glycosylation mutants used here will be valuable for identifying the different KCNE1 glycoforms in native cells and determining the roles N- and O-glycosylation play in KCNQ1–KCNE1 function and localization in cardiomyocytes,
21669976	6	61	theme	post-translational	1022:1039	arg1	integral					1062:1069	integral	1062:1069	integral	1062:1069	The compounded hypoglycosylation was equally deleterious for KCNQ1–KCNE1 cell surface expression, demonstrating that KCNE1 O-glycosylation is a post-translational modification that is integral for the proper biogenesis and anterograde trafficking of the cardiac IKs complex.
21669976	6	61	theme	post-translational	1022:1039	arg1	O-glycosylation					1001:1015	KCNE1 O-glycosylation	995:1015	KCNE1 O-glycosylation	995:1015	The compounded hypoglycosylation was equally deleterious for KCNQ1–KCNE1 cell surface expression, demonstrating that KCNE1 O-glycosylation is a post-translational modification that is integral for the proper biogenesis and anterograde trafficking of the cardiac IKs complex.
21669976	6	61	theme	post-translational	1022:1039	arg1	modification					1041:1052	a post-translational modification	1020:1052	a post-translational modification that is integral for the proper biogenesis and anterograde trafficking of the cardiac IKs complex	1020:1150	The compounded hypoglycosylation was equally deleterious for KCNQ1–KCNE1 cell surface expression, demonstrating that KCNE1 O-glycosylation is a post-translational modification that is integral for the proper biogenesis and anterograde trafficking of the cardiac IKs complex.
21669976	1	62	theme	K+	104:105	arg1	complex					115:121	the KCNQ1–KCNE1 (Kv7) K+ channel complex	82:121	the KCNQ1–KCNE1 (Kv7) K+ channel complex	82:121	Post-translational modifications of the KCNQ1–KCNE1 (Kv7) K+ channel complex are vital for regulation of the cardiac IKs current and action potential duration.
21669976	1	63	theme	potential	186:194	arg1	duration					196:203	action potential duration	179:203	action potential duration	179:203	Post-translational modifications of the KCNQ1–KCNE1 (Kv7) K+ channel complex are vital for regulation of the cardiac IKs current and action potential duration.
21669976	7	64	dep	roles	1319:1323	arg1	play					1348:1351	play	1348:1351	play in KCNQ1–KCNE1 function and localization in cardiomyocytes	1348:1410	The enzymatic assays and panel of glycosylation mutants used here will be valuable for identifying the different KCNE1 glycoforms in native cells and determining the roles N- and O-glycosylation play in KCNQ1–KCNE1 function and localization in cardiomyocytes,
21669976	1	65	theme	channel	107:113	arg1	complex					115:121	the KCNQ1–KCNE1 (Kv7) K+ channel complex	82:121	the KCNQ1–KCNE1 (Kv7) K+ channel complex	82:121	Post-translational modifications of the KCNQ1–KCNE1 (Kv7) K+ channel complex are vital for regulation of the cardiac IKs current and action potential duration.
21669976	1	66	theme	duration	196:203	arg1	regulation					137:146	regulation	137:146	regulation of the cardiac IKs current and action potential duration	137:203	Post-translational modifications of the KCNQ1–KCNE1 (Kv7) K+ channel complex are vital for regulation of the cardiac IKs current and action potential duration.
21669976	5	67	theme	subunit	710:716	arg1	biogenesis					718:727	subunit biogenesis	710:727	subunit biogenesis	710:727	For wild type KCNE1, the overlapping N- and O-glycosylation sites are innocuous for subunit biogenesis; however, mutation of Thr-7 to a non-hydroxylated residue yielded mostly unglycosylated protein and a small fraction of mono-N-glycosylated protein.
21669976	3	68	theme	mutants	414:420	arg1	set					393:395	a novel set	385:395	a novel set of glycosylation mutants and KCNE chimeras	385:438	As O-linked glycosylation sites are not recognizable by sequence gazing, we designed a novel set of glycosylation mutants and KCNE chimeras and analysed their glycan content using deglycosylation enzymes.
21669976	3	68	theme	mutants	414:420	arg1	mutants					414:420	glycosylation mutants	400:420	glycosylation mutants	400:420	As O-linked glycosylation sites are not recognizable by sequence gazing, we designed a novel set of glycosylation mutants and KCNE chimeras and analysed their glycan content using deglycosylation enzymes.
21669976	3	68	theme	mutants	414:420	arg1	chimeras					431:438	KCNE chimeras	426:438	KCNE chimeras	426:438	As O-linked glycosylation sites are not recognizable by sequence gazing, we designed a novel set of glycosylation mutants and KCNE chimeras and analysed their glycan content using deglycosylation enzymes.
21669976	1	69	theme	complex	115:121	arg1	modifications					65:77	Post-translational modifications	46:77	Post-translational modifications of the KCNQ1–KCNE1 (Kv7) K+ channel complex	46:121	Post-translational modifications of the KCNQ1–KCNE1 (Kv7) K+ channel complex are vital for regulation of the cardiac IKs current and action potential duration.
21669976	7	70	theme	KCNQ1–KCNE1	1356:1366	arg1	function					1368:1375	KCNQ1–KCNE1 function	1356:1375	KCNQ1–KCNE1 function	1356:1375	The enzymatic assays and panel of glycosylation mutants used here will be valuable for identifying the different KCNE1 glycoforms in native cells and determining the roles N- and O-glycosylation play in KCNQ1–KCNE1 function and localization in cardiomyocytes,
21669976	0	71	theme	complex	37:43	arg1	O-glycosylation					0:14	O-glycosylation	0:14	O-glycosylation of the cardiac I(Ks) complex	0:43	O-glycosylation of the cardiac I(Ks) complex.
21669976	3	72	theme	deglycosylation	480:494	arg1	enzymes					496:502	deglycosylation enzymes	480:502	deglycosylation enzymes	480:502	As O-linked glycosylation sites are not recognizable by sequence gazing, we designed a novel set of glycosylation mutants and KCNE chimeras and analysed their glycan content using deglycosylation enzymes.
21669976	7	73	theme	mutants	1201:1207	arg1	assays					1167:1172	The enzymatic assays	1153:1172	The enzymatic assays	1153:1172	The enzymatic assays and panel of glycosylation mutants used here will be valuable for identifying the different KCNE1 glycoforms in native cells and determining the roles N- and O-glycosylation play in KCNQ1–KCNE1 function and localization in cardiomyocytes,
21669976	7	73	theme	mutants	1201:1207	arg1	valuable					1227:1234	valuable	1227:1234	valuable	1227:1234	The enzymatic assays and panel of glycosylation mutants used here will be valuable for identifying the different KCNE1 glycoforms in native cells and determining the roles N- and O-glycosylation play in KCNQ1–KCNE1 function and localization in cardiomyocytes,
21669976	7	73	theme	mutants	1201:1207	arg1	panel					1178:1182	panel	1178:1182	panel of glycosylation mutants	1178:1207	The enzymatic assays and panel of glycosylation mutants used here will be valuable for identifying the different KCNE1 glycoforms in native cells and determining the roles N- and O-glycosylation play in KCNQ1–KCNE1 function and localization in cardiomyocytes,
19369259	3	0	from	role	651:654	arg1	function					675:682	function	675:682	function	675:682	CD36 is heavily modified post-translationally by N-linked glycosylation, and 10 putative glycosylation sites situated in the large extracellular loop of the protein have been identified; however, their utilization and role in the folding and function of the protein have not been characterized.
19369259	3	0	from	role	651:654	arg1	folding					663:669	folding	663:669	folding	663:669	CD36 is heavily modified post-translationally by N-linked glycosylation, and 10 putative glycosylation sites situated in the large extracellular loop of the protein have been identified; however, their utilization and role in the folding and function of the protein have not been characterized.
19369259	6	1	theme	sites	1281:1285	arg1	importance					1249:1258	the importance	1245:1258	the importance of carboxyl-terminal sites Asn-247, Asn-321, and Asn-417	1245:1315	Minimally glycosylated mutants that supported trafficking were identified and indicated the importance of carboxyl-terminal sites Asn-247, Asn-321, and Asn-417.
19369259	8	2	theme	glycosylated	1447:1458	arg1	mutants					1460:1466	these minimally glycosylated mutants	1431:1466	these minimally glycosylated mutants	1431:1466	Surprisingly, these minimally glycosylated mutants appear to be predominantly core-glycosylated, indicating that mature glycosylation is not necessary for surface expression in mammalian cells.
19369259	1	3	theme	scavenger	122:130	arg1	CD36					104:107	Human CD36	98:107	Human CD36	98:107	Human CD36 is a class B scavenger receptor expressed in a variety of cell types such as macrophage and adipocytes.
19369259	1	3	theme	scavenger	122:130	arg1	receptor					132:139	a class B scavenger receptor	112:139	a class B scavenger receptor expressed in a variety of cell types such as macrophage and adipocytes	112:210	Human CD36 is a class B scavenger receptor expressed in a variety of cell types such as macrophage and adipocytes.
19369259	3	4	theme	protein	691:697	arg1	function					675:682	function	675:682	function	675:682	CD36 is heavily modified post-translationally by N-linked glycosylation, and 10 putative glycosylation sites situated in the large extracellular loop of the protein have been identified; however, their utilization and role in the folding and function of the protein have not been characterized.
19369259	3	4	theme	protein	691:697	arg1	folding					663:669	folding	663:669	folding	663:669	CD36 is heavily modified post-translationally by N-linked glycosylation, and 10 putative glycosylation sites situated in the large extracellular loop of the protein have been identified; however, their utilization and role in the folding and function of the protein have not been characterized.
19369259	4	5	mod	modified	953:960	arg3	glycosylation					965:977	glycosylation	965:977	glycosylation	965:977	Using mass spectrometry on purified and peptide N-glycosidase F-deglycosylated CD36 and also by comparing the electrophoretic mobility of different glycosylation site mutants, we have determined that 9 of the 10 sites can be modified by glycosylation.
19369259	4	5	mod	modified	953:960	arg1	sites					940:944	the 10 sites	933:944	the 10 sites	933:944	Using mass spectrometry on purified and peptide N-glycosidase F-deglycosylated CD36 and also by comparing the electrophoretic mobility of different glycosylation site mutants, we have determined that 9 of the 10 sites can be modified by glycosylation.
19369259	4	5	mod	modified	953:960	arg1	9					928:928	9	928:928	9	928:928	Using mass spectrometry on purified and peptide N-glycosidase F-deglycosylated CD36 and also by comparing the electrophoretic mobility of different glycosylation site mutants, we have determined that 9 of the 10 sites can be modified by glycosylation.
19369259	9	6	theme	density	1726:1732	arg1	lipoprotein					1734:1744	modified low density lipoprotein	1713:1744	modified low density lipoprotein	1713:1744	The data also show that neither the nature nor the pattern of glycosylation is relevant to binding of modified low density lipoprotein.
19369259	9	7	theme	glycosylation	1673:1685	arg1	relevant					1690:1697	relevant	1690:1697	relevant	1690:1697	The data also show that neither the nature nor the pattern of glycosylation is relevant to binding of modified low density lipoprotein.
19369259	9	7	theme	glycosylation	1673:1685	arg1	pattern					1662:1668	the pattern	1658:1668	the pattern of glycosylation	1658:1685	The data also show that neither the nature nor the pattern of glycosylation is relevant to binding of modified low density lipoprotein.
19369259	4	8	theme	purified	755:762	arg1	CD36					807:810	purified and peptide N-glycosidase F-deglycosylated CD36	755:810	purified and peptide N-glycosidase F-deglycosylated CD36	755:810	Using mass spectrometry on purified and peptide N-glycosidase F-deglycosylated CD36 and also by comparing the electrophoretic mobility of different glycosylation site mutants, we have determined that 9 of the 10 sites can be modified by glycosylation.
19369259	4	9	gly	F-deglycosylated	790:805	arg1	CD36					807:810	purified and peptide N-glycosidase F-deglycosylated CD36	755:810	purified and peptide N-glycosidase F-deglycosylated CD36	755:810	Using mass spectrometry on purified and peptide N-glycosidase F-deglycosylated CD36 and also by comparing the electrophoretic mobility of different glycosylation site mutants, we have determined that 9 of the 10 sites can be modified by glycosylation.
19369259	3	10	theme	large	558:562	arg1	loop					578:581	the large extracellular loop	554:581	the large extracellular loop of the protein	554:596	CD36 is heavily modified post-translationally by N-linked glycosylation, and 10 putative glycosylation sites situated in the large extracellular loop of the protein have been identified; however, their utilization and role in the folding and function of the protein have not been characterized.
19369259	4	11	from	spectrometry	739:750	arg1	CD36					807:810	purified and peptide N-glycosidase F-deglycosylated CD36	755:810	purified and peptide N-glycosidase F-deglycosylated CD36	755:810	Using mass spectrometry on purified and peptide N-glycosidase F-deglycosylated CD36 and also by comparing the electrophoretic mobility of different glycosylation site mutants, we have determined that 9 of the 10 sites can be modified by glycosylation.
19369259	2	12	theme	wide	253:256	arg1	acids					339:343	long chain fatty acids	322:343	long chain fatty acids	322:343	This plasma membrane glycoprotein has a wide range of ligands including oxidized low density lipoprotein and long chain fatty acids which involves the receptor in diseases such as atherosclerosis and insulin resistance.
19369259	2	12	theme	wide	253:256	arg1	lipoprotein					306:316	oxidized low density lipoprotein	285:316	oxidized low density lipoprotein	285:316	This plasma membrane glycoprotein has a wide range of ligands including oxidized low density lipoprotein and long chain fatty acids which involves the receptor in diseases such as atherosclerosis and insulin resistance.
19369259	2	12	theme	wide	253:256	arg1	range					258:262	a wide range	251:262	a wide range of ligands including oxidized low density lipoprotein and long chain fatty acids which involves the receptor in diseases such as atherosclerosis and insulin resistance	251:430	This plasma membrane glycoprotein has a wide range of ligands including oxidized low density lipoprotein and long chain fatty acids which involves the receptor in diseases such as atherosclerosis and insulin resistance.
19369259	6	13	theme	carboxyl-terminal	1263:1279	arg1	sites					1281:1285	carboxyl-terminal sites Asn-247, Asn-321, and Asn-417	1263:1315	carboxyl-terminal sites Asn-247, Asn-321, and Asn-417	1263:1315	Minimally glycosylated mutants that supported trafficking were identified and indicated the importance of carboxyl-terminal sites Asn-247, Asn-321, and Asn-417.
19369259	6	13	theme	carboxyl-terminal	1263:1279	arg1	Asn-321					1296:1302	Asn-321	1296:1302	Asn-321	1296:1302	Minimally glycosylated mutants that supported trafficking were identified and indicated the importance of carboxyl-terminal sites Asn-247, Asn-321, and Asn-417.
19369259	6	13	theme	carboxyl-terminal	1263:1279	arg1	Asn-417					1309:1315	Asn-417	1309:1315	Asn-417	1309:1315	Minimally glycosylated mutants that supported trafficking were identified and indicated the importance of carboxyl-terminal sites Asn-247, Asn-321, and Asn-417.
19369259	6	13	theme	carboxyl-terminal	1263:1279	arg1	Asn-247					1287:1293	Asn-247	1287:1293	Asn-247	1287:1293	Minimally glycosylated mutants that supported trafficking were identified and indicated the importance of carboxyl-terminal sites Asn-247, Asn-321, and Asn-417.
19369259	0	14	from	status	49:54	arg1	function					88:95	function	88:95	function	88:95	The Human Scavenger Receptor CD36: glycosylation status and its role in trafficking and function.
19369259	0	14	from	status	49:54	arg1	trafficking					72:82	trafficking	72:82	trafficking	72:82	The Human Scavenger Receptor CD36: glycosylation status and its role in trafficking and function.
19369259	4	15	theme	different	866:874	arg1	mutants					895:901	different glycosylation site mutants	866:901	different glycosylation site mutants	866:901	Using mass spectrometry on purified and peptide N-glycosidase F-deglycosylated CD36 and also by comparing the electrophoretic mobility of different glycosylation site mutants, we have determined that 9 of the 10 sites can be modified by glycosylation.
19369259	8	16	from	expression	1580:1589	arg1	cells					1604:1608	mammalian cells	1594:1608	mammalian cells	1594:1608	Surprisingly, these minimally glycosylated mutants appear to be predominantly core-glycosylated, indicating that mature glycosylation is not necessary for surface expression in mammalian cells.
19369259	2	17	theme	long	322:325	arg1	acids					339:343	long chain fatty acids	322:343	long chain fatty acids	322:343	This plasma membrane glycoprotein has a wide range of ligands including oxidized low density lipoprotein and long chain fatty acids which involves the receptor in diseases such as atherosclerosis and insulin resistance.
19369259	2	18	theme	oxidized	285:292	arg1	lipoprotein					306:316	oxidized low density lipoprotein	285:316	oxidized low density lipoprotein	285:316	This plasma membrane glycoprotein has a wide range of ligands including oxidized low density lipoprotein and long chain fatty acids which involves the receptor in diseases such as atherosclerosis and insulin resistance.
19369259	2	19	gly	glycoprotein	234:245	arg1	glycoprotein					234:245	This plasma membrane glycoprotein	213:245	This plasma membrane glycoprotein	213:245	This plasma membrane glycoprotein has a wide range of ligands including oxidized low density lipoprotein and long chain fatty acids which involves the receptor in diseases such as atherosclerosis and insulin resistance.
19369259	7	20	theme	proper	1389:1394	arg1	trafficking					1396:1406	proper trafficking	1389:1406	proper trafficking of CD36	1389:1414	However, unlike SRBI, no individual site was found to be essential for proper trafficking of CD36.
19369259	8	21	gly	core-glycosylated	1495:1511	arg1	mutants					1460:1466	these minimally glycosylated mutants	1431:1466	these minimally glycosylated mutants	1431:1466	Surprisingly, these minimally glycosylated mutants appear to be predominantly core-glycosylated, indicating that mature glycosylation is not necessary for surface expression in mammalian cells.
19369259	7	22	theme	individual	1343:1352	arg1	site					1354:1357	no individual site	1340:1357	no individual site	1340:1357	However, unlike SRBI, no individual site was found to be essential for proper trafficking of CD36.
19369259	8	23	gly	glycosylated	1447:1458	arg1	mutants					1460:1466	these minimally glycosylated mutants	1431:1466	these minimally glycosylated mutants	1431:1466	Surprisingly, these minimally glycosylated mutants appear to be predominantly core-glycosylated, indicating that mature glycosylation is not necessary for surface expression in mammalian cells.
19369259	8	24	theme	surface	1572:1578	arg1	expression					1580:1589	surface expression	1572:1589	surface expression in mammalian cells	1572:1608	Surprisingly, these minimally glycosylated mutants appear to be predominantly core-glycosylated, indicating that mature glycosylation is not necessary for surface expression in mammalian cells.
19369259	3	25	theme	putative	513:520	arg1	sites					536:540	10 putative glycosylation sites	510:540	10 putative glycosylation sites situated in the large extracellular loop of the protein	510:596	CD36 is heavily modified post-translationally by N-linked glycosylation, and 10 putative glycosylation sites situated in the large extracellular loop of the protein have been identified; however, their utilization and role in the folding and function of the protein have not been characterized.
19369259	4	26	theme	sites	940:944	arg1	sites					940:944	the 10 sites	933:944	the 10 sites	933:944	Using mass spectrometry on purified and peptide N-glycosidase F-deglycosylated CD36 and also by comparing the electrophoretic mobility of different glycosylation site mutants, we have determined that 9 of the 10 sites can be modified by glycosylation.
19369259	4	26	theme	sites	940:944	arg1	9					928:928	9	928:928	9	928:928	Using mass spectrometry on purified and peptide N-glycosidase F-deglycosylated CD36 and also by comparing the electrophoretic mobility of different glycosylation site mutants, we have determined that 9 of the 10 sites can be modified by glycosylation.
19369259	2	27	theme	insulin	413:419	arg1	resistance					421:430	insulin resistance	413:430	insulin resistance	413:430	This plasma membrane glycoprotein has a wide range of ligands including oxidized low density lipoprotein and long chain fatty acids which involves the receptor in diseases such as atherosclerosis and insulin resistance.
19369259	4	28	theme	electrophoretic	838:852	arg1	mobility					854:861	the electrophoretic mobility	834:861	the electrophoretic mobility of different glycosylation site mutants	834:901	Using mass spectrometry on purified and peptide N-glycosidase F-deglycosylated CD36 and also by comparing the electrophoretic mobility of different glycosylation site mutants, we have determined that 9 of the 10 sites can be modified by glycosylation.
19369259	5	29	theme	Flow	980:983	arg1	analysis					996:1003	Flow cytometric analysis	980:1003	Flow cytometric analysis of the different glycosylation mutants expressed in mammalian cells	980:1071	Flow cytometric analysis of the different glycosylation mutants expressed in mammalian cells established that glycosylation is necessary for trafficking to the plasma membrane.
19369259	6	30	theme	glycosylated	1167:1178	arg1	mutants					1180:1186	Minimally glycosylated mutants	1157:1186	Minimally glycosylated mutants that supported trafficking	1157:1213	Minimally glycosylated mutants that supported trafficking were identified and indicated the importance of carboxyl-terminal sites Asn-247, Asn-321, and Asn-417.
19369259	6	31	gly	glycosylated	1167:1178	arg1	mutants					1180:1186	Minimally glycosylated mutants	1157:1186	Minimally glycosylated mutants that supported trafficking	1157:1213	Minimally glycosylated mutants that supported trafficking were identified and indicated the importance of carboxyl-terminal sites Asn-247, Asn-321, and Asn-417.
19369259	5	32	theme	plasma	1140:1145	arg1	membrane					1147:1154	the plasma membrane	1136:1154	the plasma membrane	1136:1154	Flow cytometric analysis of the different glycosylation mutants expressed in mammalian cells established that glycosylation is necessary for trafficking to the plasma membrane.
19369259	2	33	theme	ligands	267:273	arg1	acids					339:343	long chain fatty acids	322:343	long chain fatty acids	322:343	This plasma membrane glycoprotein has a wide range of ligands including oxidized low density lipoprotein and long chain fatty acids which involves the receptor in diseases such as atherosclerosis and insulin resistance.
19369259	2	33	theme	ligands	267:273	arg1	lipoprotein					306:316	oxidized low density lipoprotein	285:316	oxidized low density lipoprotein	285:316	This plasma membrane glycoprotein has a wide range of ligands including oxidized low density lipoprotein and long chain fatty acids which involves the receptor in diseases such as atherosclerosis and insulin resistance.
19369259	2	33	theme	ligands	267:273	arg1	range					258:262	a wide range	251:262	a wide range of ligands including oxidized low density lipoprotein and long chain fatty acids which involves the receptor in diseases such as atherosclerosis and insulin resistance	251:430	This plasma membrane glycoprotein has a wide range of ligands including oxidized low density lipoprotein and long chain fatty acids which involves the receptor in diseases such as atherosclerosis and insulin resistance.
19369259	4	34	theme	mass	734:737	arg1	spectrometry					739:750	mass spectrometry	734:750	mass spectrometry on purified and peptide N-glycosidase F-deglycosylated CD36	734:810	Using mass spectrometry on purified and peptide N-glycosidase F-deglycosylated CD36 and also by comparing the electrophoretic mobility of different glycosylation site mutants, we have determined that 9 of the 10 sites can be modified by glycosylation.
19369259	3	35	gly	glycosylation	522:534	arg2	10					510:511	10	510:511	10	510:511	CD36 is heavily modified post-translationally by N-linked glycosylation, and 10 putative glycosylation sites situated in the large extracellular loop of the protein have been identified; however, their utilization and role in the folding and function of the protein have not been characterized.
19369259	3	35	gly	glycosylation	522:534	arg2	sites					536:540	10 putative glycosylation sites	510:540	10 putative glycosylation sites situated in the large extracellular loop of the protein	510:596	CD36 is heavily modified post-translationally by N-linked glycosylation, and 10 putative glycosylation sites situated in the large extracellular loop of the protein have been identified; however, their utilization and role in the folding and function of the protein have not been characterized.
19369259	0	36	theme	Receptor	20:27	arg1	CD36					29:32	The Human Scavenger Receptor CD36	0:32	The Human Scavenger Receptor CD36	0:32	The Human Scavenger Receptor CD36: glycosylation status and its role in trafficking and function.
19369259	2	37	contain	has	247:249	arg2	acids					339:343	long chain fatty acids	322:343	long chain fatty acids	322:343	This plasma membrane glycoprotein has a wide range of ligands including oxidized low density lipoprotein and long chain fatty acids which involves the receptor in diseases such as atherosclerosis and insulin resistance.
19369259	2	37	contain	has	247:249	arg1	glycoprotein					234:245	This plasma membrane glycoprotein	213:245	This plasma membrane glycoprotein	213:245	This plasma membrane glycoprotein has a wide range of ligands including oxidized low density lipoprotein and long chain fatty acids which involves the receptor in diseases such as atherosclerosis and insulin resistance.
19369259	2	37	contain	has	247:249	arg2	lipoprotein					306:316	oxidized low density lipoprotein	285:316	oxidized low density lipoprotein	285:316	This plasma membrane glycoprotein has a wide range of ligands including oxidized low density lipoprotein and long chain fatty acids which involves the receptor in diseases such as atherosclerosis and insulin resistance.
19369259	2	37	contain	has	247:249	arg2	range					258:262	a wide range	251:262	a wide range of ligands including oxidized low density lipoprotein and long chain fatty acids which involves the receptor in diseases such as atherosclerosis and insulin resistance	251:430	This plasma membrane glycoprotein has a wide range of ligands including oxidized low density lipoprotein and long chain fatty acids which involves the receptor in diseases such as atherosclerosis and insulin resistance.
19369259	3	38	link	N-linked	482:489	arg1	glycosylation					491:503	N-linked glycosylation	482:503	N-linked glycosylation	482:503	CD36 is heavily modified post-translationally by N-linked glycosylation, and 10 putative glycosylation sites situated in the large extracellular loop of the protein have been identified; however, their utilization and role in the folding and function of the protein have not been characterized.
19369259	9	39	theme	modified	1713:1720	arg1	lipoprotein					1734:1744	modified low density lipoprotein	1713:1744	modified low density lipoprotein	1713:1744	The data also show that neither the nature nor the pattern of glycosylation is relevant to binding of modified low density lipoprotein.
19369259	3	40	theme	situated	542:549	arg1	sites					536:540	10 putative glycosylation sites	510:540	10 putative glycosylation sites situated in the large extracellular loop of the protein	510:596	CD36 is heavily modified post-translationally by N-linked glycosylation, and 10 putative glycosylation sites situated in the large extracellular loop of the protein have been identified; however, their utilization and role in the folding and function of the protein have not been characterized.
19369259	3	41	from	loop	578:581	arg1	situated					542:549	situated	542:549	situated	542:549	CD36 is heavily modified post-translationally by N-linked glycosylation, and 10 putative glycosylation sites situated in the large extracellular loop of the protein have been identified; however, their utilization and role in the folding and function of the protein have not been characterized.
19369259	3	42	mod	modified	449:456	arg1	CD36					433:436	CD36	433:436	CD36	433:436	CD36 is heavily modified post-translationally by N-linked glycosylation, and 10 putative glycosylation sites situated in the large extracellular loop of the protein have been identified; however, their utilization and role in the folding and function of the protein have not been characterized.
19369259	3	42	mod	modified	449:456	arg3	glycosylation					491:503	N-linked glycosylation	482:503	N-linked glycosylation	482:503	CD36 is heavily modified post-translationally by N-linked glycosylation, and 10 putative glycosylation sites situated in the large extracellular loop of the protein have been identified; however, their utilization and role in the folding and function of the protein have not been characterized.
19369259	0	43	theme	Scavenger	10:18	arg1	CD36					29:32	The Human Scavenger Receptor CD36	0:32	The Human Scavenger Receptor CD36	0:32	The Human Scavenger Receptor CD36: glycosylation status and its role in trafficking and function.
19369259	2	44	theme	fatty	333:337	arg1	acids					339:343	long chain fatty acids	322:343	long chain fatty acids	322:343	This plasma membrane glycoprotein has a wide range of ligands including oxidized low density lipoprotein and long chain fatty acids which involves the receptor in diseases such as atherosclerosis and insulin resistance.
19369259	5	45	theme	mammalian	1057:1065	arg1	cells					1067:1071	mammalian cells	1057:1071	mammalian cells	1057:1071	Flow cytometric analysis of the different glycosylation mutants expressed in mammalian cells established that glycosylation is necessary for trafficking to the plasma membrane.
19369259	7	46	theme	CD36	1411:1414	arg1	trafficking					1396:1406	proper trafficking	1389:1406	proper trafficking of CD36	1389:1414	However, unlike SRBI, no individual site was found to be essential for proper trafficking of CD36.
19369259	1	47	theme	cell	167:170	arg1	adipocytes					201:210	adipocytes	201:210	adipocytes	201:210	Human CD36 is a class B scavenger receptor expressed in a variety of cell types such as macrophage and adipocytes.
19369259	1	47	theme	cell	167:170	arg1	types					172:176	cell types	167:176	cell types such as macrophage and adipocytes	167:210	Human CD36 is a class B scavenger receptor expressed in a variety of cell types such as macrophage and adipocytes.
19369259	1	47	theme	cell	167:170	arg1	macrophage					186:195	macrophage	186:195	macrophage	186:195	Human CD36 is a class B scavenger receptor expressed in a variety of cell types such as macrophage and adipocytes.
19369259	3	48	theme	N-linked	482:489	arg1	glycosylation					491:503	N-linked glycosylation	482:503	N-linked glycosylation	482:503	CD36 is heavily modified post-translationally by N-linked glycosylation, and 10 putative glycosylation sites situated in the large extracellular loop of the protein have been identified; however, their utilization and role in the folding and function of the protein have not been characterized.
19369259	8	49	theme	mammalian	1594:1602	arg1	cells					1604:1608	mammalian cells	1594:1608	mammalian cells	1594:1608	Surprisingly, these minimally glycosylated mutants appear to be predominantly core-glycosylated, indicating that mature glycosylation is not necessary for surface expression in mammalian cells.
19369259	9	50	theme	lipoprotein	1734:1744	arg1	binding					1702:1708	binding	1702:1708	binding of modified low density lipoprotein	1702:1744	The data also show that neither the nature nor the pattern of glycosylation is relevant to binding of modified low density lipoprotein.
19369259	0	51	from	role	64:67	arg1	function					88:95	function	88:95	function	88:95	The Human Scavenger Receptor CD36: glycosylation status and its role in trafficking and function.
19369259	0	51	from	role	64:67	arg1	trafficking					72:82	trafficking	72:82	trafficking	72:82	The Human Scavenger Receptor CD36: glycosylation status and its role in trafficking and function.
19369259	0	52	dep	status	49:54	arg1	CD36					29:32	The Human Scavenger Receptor CD36	0:32	The Human Scavenger Receptor CD36	0:32	The Human Scavenger Receptor CD36: glycosylation status and its role in trafficking and function.
19369259	4	53	gly	glycosylation	876:888	arg2	site					890:893	different glycosylation site mutants	866:901	different glycosylation site mutants	866:901	Using mass spectrometry on purified and peptide N-glycosidase F-deglycosylated CD36 and also by comparing the electrophoretic mobility of different glycosylation site mutants, we have determined that 9 of the 10 sites can be modified by glycosylation.
19369259	4	53	gly	glycosylation	876:888	arg2	mutants					895:901	different glycosylation site mutants	866:901	different glycosylation site mutants	866:901	Using mass spectrometry on purified and peptide N-glycosidase F-deglycosylated CD36 and also by comparing the electrophoretic mobility of different glycosylation site mutants, we have determined that 9 of the 10 sites can be modified by glycosylation.
19369259	1	54	theme	types	172:176	arg1	variety					156:162	a variety	154:162	a variety of cell types such as macrophage and adipocytes	154:210	Human CD36 is a class B scavenger receptor expressed in a variety of cell types such as macrophage and adipocytes.
19369259	1	54	theme	types	172:176	arg1	types					172:176	cell types	167:176	cell types such as macrophage and adipocytes	167:210	Human CD36 is a class B scavenger receptor expressed in a variety of cell types such as macrophage and adipocytes.
19369259	1	54	theme	types	172:176	arg1	macrophage					186:195	macrophage	186:195	macrophage	186:195	Human CD36 is a class B scavenger receptor expressed in a variety of cell types such as macrophage and adipocytes.
19369259	1	54	theme	types	172:176	arg1	adipocytes					201:210	adipocytes	201:210	adipocytes	201:210	Human CD36 is a class B scavenger receptor expressed in a variety of cell types such as macrophage and adipocytes.
19369259	4	55	theme	F-deglycosylated	790:805	arg1	CD36					807:810	purified and peptide N-glycosidase F-deglycosylated CD36	755:810	purified and peptide N-glycosidase F-deglycosylated CD36	755:810	Using mass spectrometry on purified and peptide N-glycosidase F-deglycosylated CD36 and also by comparing the electrophoretic mobility of different glycosylation site mutants, we have determined that 9 of the 10 sites can be modified by glycosylation.
19369259	4	56	theme	glycosylation	876:888	arg1	mutants					895:901	different glycosylation site mutants	866:901	different glycosylation site mutants	866:901	Using mass spectrometry on purified and peptide N-glycosidase F-deglycosylated CD36 and also by comparing the electrophoretic mobility of different glycosylation site mutants, we have determined that 9 of the 10 sites can be modified by glycosylation.
19369259	3	57	dep	folding	663:669	arg1	the					659:661	the	659:661	the	659:661	CD36 is heavily modified post-translationally by N-linked glycosylation, and 10 putative glycosylation sites situated in the large extracellular loop of the protein have been identified; however, their utilization and role in the folding and function of the protein have not been characterized.
19369259	3	58	theme	extracellular	564:576	arg1	loop					578:581	the large extracellular loop	554:581	the large extracellular loop of the protein	554:596	CD36 is heavily modified post-translationally by N-linked glycosylation, and 10 putative glycosylation sites situated in the large extracellular loop of the protein have been identified; however, their utilization and role in the folding and function of the protein have not been characterized.
19369259	8	59	theme	mature	1530:1535	arg1	glycosylation					1537:1549	mature glycosylation	1530:1549	mature glycosylation	1530:1549	Surprisingly, these minimally glycosylated mutants appear to be predominantly core-glycosylated, indicating that mature glycosylation is not necessary for surface expression in mammalian cells.
19369259	1	60	theme	Human	98:102	arg1	CD36					104:107	Human CD36	98:107	Human CD36	98:107	Human CD36 is a class B scavenger receptor expressed in a variety of cell types such as macrophage and adipocytes.
19369259	1	60	theme	Human	98:102	arg1	receptor					132:139	a class B scavenger receptor	112:139	a class B scavenger receptor expressed in a variety of cell types such as macrophage and adipocytes	112:210	Human CD36 is a class B scavenger receptor expressed in a variety of cell types such as macrophage and adipocytes.
19369259	0	61	theme	glycosylation	35:47	arg1	status					49:54	glycosylation status	35:54	glycosylation status	35:54	The Human Scavenger Receptor CD36: glycosylation status and its role in trafficking and function.
19369259	4	62	theme	mutants	895:901	arg1	mobility					854:861	the electrophoretic mobility	834:861	the electrophoretic mobility of different glycosylation site mutants	834:901	Using mass spectrometry on purified and peptide N-glycosidase F-deglycosylated CD36 and also by comparing the electrophoretic mobility of different glycosylation site mutants, we have determined that 9 of the 10 sites can be modified by glycosylation.
19369259	4	63	theme	site	890:893	arg1	mutants					895:901	different glycosylation site mutants	866:901	different glycosylation site mutants	866:901	Using mass spectrometry on purified and peptide N-glycosidase F-deglycosylated CD36 and also by comparing the electrophoretic mobility of different glycosylation site mutants, we have determined that 9 of the 10 sites can be modified by glycosylation.
19369259	5	64	theme	glycosylation	1022:1034	arg1	mutants					1036:1042	the different glycosylation mutants	1008:1042	the different glycosylation mutants expressed in mammalian cells	1008:1071	Flow cytometric analysis of the different glycosylation mutants expressed in mammalian cells established that glycosylation is necessary for trafficking to the plasma membrane.
19369259	5	65	theme	different	1012:1020	arg1	mutants					1036:1042	the different glycosylation mutants	1008:1042	the different glycosylation mutants expressed in mammalian cells	1008:1071	Flow cytometric analysis of the different glycosylation mutants expressed in mammalian cells established that glycosylation is necessary for trafficking to the plasma membrane.
19369259	2	66	theme	density	298:304	arg1	lipoprotein					306:316	oxidized low density lipoprotein	285:316	oxidized low density lipoprotein	285:316	This plasma membrane glycoprotein has a wide range of ligands including oxidized low density lipoprotein and long chain fatty acids which involves the receptor in diseases such as atherosclerosis and insulin resistance.
19369259	3	67	from	situated	542:549	arg1	loop					578:581	the large extracellular loop	554:581	the large extracellular loop of the protein	554:596	CD36 is heavily modified post-translationally by N-linked glycosylation, and 10 putative glycosylation sites situated in the large extracellular loop of the protein have been identified; however, their utilization and role in the folding and function of the protein have not been characterized.
19369259	9	68	theme	low	1722:1724	arg1	lipoprotein					1734:1744	modified low density lipoprotein	1713:1744	modified low density lipoprotein	1713:1744	The data also show that neither the nature nor the pattern of glycosylation is relevant to binding of modified low density lipoprotein.
19369259	5	69	theme	mutants	1036:1042	arg1	analysis					996:1003	Flow cytometric analysis	980:1003	Flow cytometric analysis of the different glycosylation mutants expressed in mammalian cells	980:1071	Flow cytometric analysis of the different glycosylation mutants expressed in mammalian cells established that glycosylation is necessary for trafficking to the plasma membrane.
19369259	2	70	theme	membrane	225:232	arg1	glycoprotein					234:245	This plasma membrane glycoprotein	213:245	This plasma membrane glycoprotein	213:245	This plasma membrane glycoprotein has a wide range of ligands including oxidized low density lipoprotein and long chain fatty acids which involves the receptor in diseases such as atherosclerosis and insulin resistance.
19369259	2	71	theme	low	294:296	arg1	lipoprotein					306:316	oxidized low density lipoprotein	285:316	oxidized low density lipoprotein	285:316	This plasma membrane glycoprotein has a wide range of ligands including oxidized low density lipoprotein and long chain fatty acids which involves the receptor in diseases such as atherosclerosis and insulin resistance.
19369259	2	72	theme	plasma	218:223	arg1	glycoprotein					234:245	This plasma membrane glycoprotein	213:245	This plasma membrane glycoprotein	213:245	This plasma membrane glycoprotein has a wide range of ligands including oxidized low density lipoprotein and long chain fatty acids which involves the receptor in diseases such as atherosclerosis and insulin resistance.
19369259	1	73	theme	B	120:120	arg1	CD36					104:107	Human CD36	98:107	Human CD36	98:107	Human CD36 is a class B scavenger receptor expressed in a variety of cell types such as macrophage and adipocytes.
19369259	1	73	theme	B	120:120	arg1	receptor					132:139	a class B scavenger receptor	112:139	a class B scavenger receptor expressed in a variety of cell types such as macrophage and adipocytes	112:210	Human CD36 is a class B scavenger receptor expressed in a variety of cell types such as macrophage and adipocytes.
19369259	3	74	from	utilization	635:645	arg1	function					675:682	function	675:682	function	675:682	CD36 is heavily modified post-translationally by N-linked glycosylation, and 10 putative glycosylation sites situated in the large extracellular loop of the protein have been identified; however, their utilization and role in the folding and function of the protein have not been characterized.
19369259	3	74	from	utilization	635:645	arg1	folding					663:669	folding	663:669	folding	663:669	CD36 is heavily modified post-translationally by N-linked glycosylation, and 10 putative glycosylation sites situated in the large extracellular loop of the protein have been identified; however, their utilization and role in the folding and function of the protein have not been characterized.
19369259	3	75	theme	protein	590:596	arg1	loop					578:581	the large extracellular loop	554:581	the large extracellular loop of the protein	554:596	CD36 is heavily modified post-translationally by N-linked glycosylation, and 10 putative glycosylation sites situated in the large extracellular loop of the protein have been identified; however, their utilization and role in the folding and function of the protein have not been characterized.
19369259	2	76	from	receptor	364:371	arg1	diseases					376:383	diseases	376:383	diseases such as atherosclerosis and insulin resistance	376:430	This plasma membrane glycoprotein has a wide range of ligands including oxidized low density lipoprotein and long chain fatty acids which involves the receptor in diseases such as atherosclerosis and insulin resistance.
19369259	2	76	from	receptor	364:371	arg1	atherosclerosis					393:407	atherosclerosis	393:407	atherosclerosis	393:407	This plasma membrane glycoprotein has a wide range of ligands including oxidized low density lipoprotein and long chain fatty acids which involves the receptor in diseases such as atherosclerosis and insulin resistance.
19369259	2	76	from	receptor	364:371	arg1	resistance					421:430	insulin resistance	413:430	insulin resistance	413:430	This plasma membrane glycoprotein has a wide range of ligands including oxidized low density lipoprotein and long chain fatty acids which involves the receptor in diseases such as atherosclerosis and insulin resistance.
19369259	1	77	theme	class	114:118	arg1	CD36					104:107	Human CD36	98:107	Human CD36	98:107	Human CD36 is a class B scavenger receptor expressed in a variety of cell types such as macrophage and adipocytes.
19369259	1	77	theme	class	114:118	arg1	receptor					132:139	a class B scavenger receptor	112:139	a class B scavenger receptor expressed in a variety of cell types such as macrophage and adipocytes	112:210	Human CD36 is a class B scavenger receptor expressed in a variety of cell types such as macrophage and adipocytes.
19369259	6	78	dep	sites	1281:1285	arg1	sites					1281:1285	carboxyl-terminal sites Asn-247, Asn-321, and Asn-417	1263:1315	carboxyl-terminal sites Asn-247, Asn-321, and Asn-417	1263:1315	Minimally glycosylated mutants that supported trafficking were identified and indicated the importance of carboxyl-terminal sites Asn-247, Asn-321, and Asn-417.
19369259	6	78	dep	sites	1281:1285	arg1	Asn-321					1296:1302	Asn-321	1296:1302	Asn-321	1296:1302	Minimally glycosylated mutants that supported trafficking were identified and indicated the importance of carboxyl-terminal sites Asn-247, Asn-321, and Asn-417.
19369259	6	78	dep	sites	1281:1285	arg1	Asn-417					1309:1315	Asn-417	1309:1315	Asn-417	1309:1315	Minimally glycosylated mutants that supported trafficking were identified and indicated the importance of carboxyl-terminal sites Asn-247, Asn-321, and Asn-417.
19369259	6	78	dep	sites	1281:1285	arg1	Asn-247					1287:1293	Asn-247	1287:1293	Asn-247	1287:1293	Minimally glycosylated mutants that supported trafficking were identified and indicated the importance of carboxyl-terminal sites Asn-247, Asn-321, and Asn-417.
19369259	3	79	theme	glycosylation	522:534	arg1	sites					536:540	10 putative glycosylation sites	510:540	10 putative glycosylation sites situated in the large extracellular loop of the protein	510:596	CD36 is heavily modified post-translationally by N-linked glycosylation, and 10 putative glycosylation sites situated in the large extracellular loop of the protein have been identified; however, their utilization and role in the folding and function of the protein have not been characterized.
19369259	5	80	theme	cytometric	985:994	arg1	analysis					996:1003	Flow cytometric analysis	980:1003	Flow cytometric analysis of the different glycosylation mutants expressed in mammalian cells	980:1071	Flow cytometric analysis of the different glycosylation mutants expressed in mammalian cells established that glycosylation is necessary for trafficking to the plasma membrane.
19369259	2	81	theme	chain	327:331	arg1	acids					339:343	long chain fatty acids	322:343	long chain fatty acids	322:343	This plasma membrane glycoprotein has a wide range of ligands including oxidized low density lipoprotein and long chain fatty acids which involves the receptor in diseases such as atherosclerosis and insulin resistance.
19369259	0	82	theme	Human	4:8	arg1	CD36					29:32	The Human Scavenger Receptor CD36	0:32	The Human Scavenger Receptor CD36	0:32	The Human Scavenger Receptor CD36: glycosylation status and its role in trafficking and function.
20356926	0	0	theme	factor	102:107	arg1	activation					59:68	optimal proteolytic activation	39:68	optimal proteolytic activation of membrane-bound transcription factor CREB-H	39:114	N-linked glycosylation is required for optimal proteolytic activation of membrane-bound transcription factor CREB-H.
20356926	6	1	theme	sites	568:572	arg1	Disruption					544:553	Disruption	544:553	Disruption of all three sites by site-directed mutagenesis	544:601	Disruption of all three sites by site-directed mutagenesis completely abrogated N-linked glycosylation of CREB-H.
20356926	9	2	link	N-linked	1138:1145	arg1	glycosylation					1147:1159	N-linked glycosylation	1138:1159	N-linked glycosylation	1138:1159	Taken together, our findings suggest that N-linked glycosylation is required for full activation of CREB-H through intramembrane proteolysis.
20356926	9	3	theme	N-linked	1138:1145	arg1	glycosylation					1147:1159	N-linked glycosylation	1138:1159	N-linked glycosylation	1138:1159	Taken together, our findings suggest that N-linked glycosylation is required for full activation of CREB-H through intramembrane proteolysis.
20356926	0	4	theme	transcription	88:100	arg1	factor					102:107	membrane-bound transcription factor CREB-H	73:114	membrane-bound transcription factor CREB-H	73:114	N-linked glycosylation is required for optimal proteolytic activation of membrane-bound transcription factor CREB-H.
20356926	7	5	theme	CREB-H	687:692	arg1	mutant					677:682	The unglycosylated mutant	658:682	The unglycosylated mutant of CREB-H	658:692	The unglycosylated mutant of CREB-H was not unstable, unfolded or aggregated.
20356926	7	5	theme	CREB-H	687:692	arg1	unstable					702:709	unstable	702:709	unstable	702:709	The unglycosylated mutant of CREB-H was not unstable, unfolded or aggregated.
20356926	8	6	gly	deglycosylated	871:884	arg1	CREB-H					886:891	unglycosylated or deglycosylated CREB-H	853:891	unglycosylated or deglycosylated CREB-H	853:891	Upon stimulation with an activator of intramembrane proteolysis such as brefeldin A and KDEL-tailed site 1 protease, unglycosylated or deglycosylated CREB-H was largely uncleaved, retained in an inactive form in the endoplasmic reticulum, and less capable of activating transcription driven by unfolded protein response element or C-reactive protein promoter.
20356926	8	7	theme	unfolded	1030:1037	arg1	element					1056:1062	unfolded protein response element	1030:1062	unfolded protein response element	1030:1062	Upon stimulation with an activator of intramembrane proteolysis such as brefeldin A and KDEL-tailed site 1 protease, unglycosylated or deglycosylated CREB-H was largely uncleaved, retained in an inactive form in the endoplasmic reticulum, and less capable of activating transcription driven by unfolded protein response element or C-reactive protein promoter.
20356926	1	8	theme	CREB3	177:181	arg1	subfamily					183:191	the CREB3 subfamily	173:191	the CREB3 subfamily	173:191	CREB-H is a liver-enriched bZIP transcription factor of the CREB3 subfamily.
20356926	4	9	theme	luminal	423:429	arg1	domain					431:436	the luminal domain	419:436	the luminal domain at the C-terminus	419:454	In this study we characterized N-linked glycosylation of CREB-H in the luminal domain at the C-terminus.
20356926	8	10	theme	unglycosylated	853:866	arg1	CREB-H					886:891	unglycosylated or deglycosylated CREB-H	853:891	unglycosylated or deglycosylated CREB-H	853:891	Upon stimulation with an activator of intramembrane proteolysis such as brefeldin A and KDEL-tailed site 1 protease, unglycosylated or deglycosylated CREB-H was largely uncleaved, retained in an inactive form in the endoplasmic reticulum, and less capable of activating transcription driven by unfolded protein response element or C-reactive protein promoter.
20356926	8	11	theme	response	1047:1054	arg1	element					1056:1062	unfolded protein response element	1030:1062	unfolded protein response element	1030:1062	Upon stimulation with an activator of intramembrane proteolysis such as brefeldin A and KDEL-tailed site 1 protease, unglycosylated or deglycosylated CREB-H was largely uncleaved, retained in an inactive form in the endoplasmic reticulum, and less capable of activating transcription driven by unfolded protein response element or C-reactive protein promoter.
20356926	9	12	theme	full	1177:1180	arg1	activation					1182:1191	full activation	1177:1191	full activation of CREB-H through intramembrane proteolysis	1177:1235	Taken together, our findings suggest that N-linked glycosylation is required for full activation of CREB-H through intramembrane proteolysis.
20356926	0	13	link	N-linked	0:7	arg1	glycosylation					9:21	N-linked glycosylation	0:21	N-linked glycosylation	0:21	N-linked glycosylation is required for optimal proteolytic activation of membrane-bound transcription factor CREB-H.
20356926	4	14	link	N-linked	383:390	arg1	glycosylation					392:404	N-linked glycosylation	383:404	N-linked glycosylation of CREB-H in the luminal domain at the C-terminus	383:454	In this study we characterized N-linked glycosylation of CREB-H in the luminal domain at the C-terminus.
20356926	1	15	theme	subfamily	183:191	arg1	CREB-H					117:122	CREB-H	117:122	CREB-H	117:122	CREB-H is a liver-enriched bZIP transcription factor of the CREB3 subfamily.
20356926	1	15	theme	subfamily	183:191	arg1	factor					163:168	a liver-enriched bZIP transcription factor	127:168	a liver-enriched bZIP transcription factor of the CREB3 subfamily	127:191	CREB-H is a liver-enriched bZIP transcription factor of the CREB3 subfamily.
20356926	8	16	theme	C-reactive	1067:1076	arg1	promoter					1086:1093	C-reactive protein promoter	1067:1093	C-reactive protein promoter	1067:1093	Upon stimulation with an activator of intramembrane proteolysis such as brefeldin A and KDEL-tailed site 1 protease, unglycosylated or deglycosylated CREB-H was largely uncleaved, retained in an inactive form in the endoplasmic reticulum, and less capable of activating transcription driven by unfolded protein response element or C-reactive protein promoter.
20356926	5	17	gly	glycosylation	508:520	arg2	sites					522:526	three N-linked glycosylation sites	493:526	three N-linked glycosylation sites in this region	493:541	We found that CREB-H is modified at three N-linked glycosylation sites in this region.
20356926	5	17	gly	glycosylation	508:520	arg2	three					493:497	three	493:497	three	493:497	We found that CREB-H is modified at three N-linked glycosylation sites in this region.
20356926	3	18	theme	Aberrant	291:298	arg1	expression					300:309	Aberrant expression	291:309	Aberrant expression of CREB-H	291:319	Aberrant expression of CREB-H is implicated in liver cancer.
20356926	4	19	theme	CREB-H	409:414	arg1	glycosylation					392:404	N-linked glycosylation	383:404	N-linked glycosylation of CREB-H in the luminal domain at the C-terminus	383:454	In this study we characterized N-linked glycosylation of CREB-H in the luminal domain at the C-terminus.
20356926	6	20	theme	CREB-H	650:655	arg1	glycosylation					633:645	N-linked glycosylation	624:645	N-linked glycosylation of CREB-H	624:655	Disruption of all three sites by site-directed mutagenesis completely abrogated N-linked glycosylation of CREB-H.
20356926	7	21	gly	unglycosylated	662:675	arg1	mutant					677:682	The unglycosylated mutant	658:682	The unglycosylated mutant of CREB-H	658:692	The unglycosylated mutant of CREB-H was not unstable, unfolded or aggregated.
20356926	7	21	gly	unglycosylated	662:675	arg1	unstable					702:709	unstable	702:709	unstable	702:709	The unglycosylated mutant of CREB-H was not unstable, unfolded or aggregated.
20356926	7	22	theme	unglycosylated	662:675	arg1	mutant					677:682	The unglycosylated mutant	658:682	The unglycosylated mutant of CREB-H	658:692	The unglycosylated mutant of CREB-H was not unstable, unfolded or aggregated.
20356926	7	22	theme	unglycosylated	662:675	arg1	unstable					702:709	unstable	702:709	unstable	702:709	The unglycosylated mutant of CREB-H was not unstable, unfolded or aggregated.
20356926	6	23	theme	site-directed	577:589	arg1	mutagenesis					591:601	site-directed mutagenesis	577:601	site-directed mutagenesis	577:601	Disruption of all three sites by site-directed mutagenesis completely abrogated N-linked glycosylation of CREB-H.
20356926	8	24	theme	inactive	931:938	arg1	form					940:943	an inactive form	928:943	an inactive form in the endoplasmic reticulum	928:972	Upon stimulation with an activator of intramembrane proteolysis such as brefeldin A and KDEL-tailed site 1 protease, unglycosylated or deglycosylated CREB-H was largely uncleaved, retained in an inactive form in the endoplasmic reticulum, and less capable of activating transcription driven by unfolded protein response element or C-reactive protein promoter.
20356926	0	25	theme	N-linked	0:7	arg1	glycosylation					9:21	N-linked glycosylation	0:21	N-linked glycosylation	0:21	N-linked glycosylation is required for optimal proteolytic activation of membrane-bound transcription factor CREB-H.
20356926	8	26	theme	protein	1078:1084	arg1	promoter					1086:1093	C-reactive protein promoter	1067:1093	C-reactive protein promoter	1067:1093	Upon stimulation with an activator of intramembrane proteolysis such as brefeldin A and KDEL-tailed site 1 protease, unglycosylated or deglycosylated CREB-H was largely uncleaved, retained in an inactive form in the endoplasmic reticulum, and less capable of activating transcription driven by unfolded protein response element or C-reactive protein promoter.
20356926	3	27	theme	CREB-H	314:319	arg1	expression					300:309	Aberrant expression	291:309	Aberrant expression of CREB-H	291:319	Aberrant expression of CREB-H is implicated in liver cancer.
20356926	8	28	theme	protein	1039:1045	arg1	element					1056:1062	unfolded protein response element	1030:1062	unfolded protein response element	1030:1062	Upon stimulation with an activator of intramembrane proteolysis such as brefeldin A and KDEL-tailed site 1 protease, unglycosylated or deglycosylated CREB-H was largely uncleaved, retained in an inactive form in the endoplasmic reticulum, and less capable of activating transcription driven by unfolded protein response element or C-reactive protein promoter.
20356926	6	29	gly	glycosylation	633:645	arg1	CREB-H					650:655	CREB-H	650:655	CREB-H	650:655	Disruption of all three sites by site-directed mutagenesis completely abrogated N-linked glycosylation of CREB-H.
20356926	4	30	from	glycosylation	392:404	arg1	domain					431:436	the luminal domain	419:436	the luminal domain at the C-terminus	419:454	In this study we characterized N-linked glycosylation of CREB-H in the luminal domain at the C-terminus.
20356926	4	30	from	glycosylation	392:404	arg1	C-terminus					445:454	the C-terminus	441:454	the C-terminus	441:454	In this study we characterized N-linked glycosylation of CREB-H in the luminal domain at the C-terminus.
20356926	8	31	theme	intramembrane	774:786	arg1	proteolysis					788:798	intramembrane proteolysis	774:798	intramembrane proteolysis	774:798	Upon stimulation with an activator of intramembrane proteolysis such as brefeldin A and KDEL-tailed site 1 protease, unglycosylated or deglycosylated CREB-H was largely uncleaved, retained in an inactive form in the endoplasmic reticulum, and less capable of activating transcription driven by unfolded protein response element or C-reactive protein promoter.
20356926	8	32	theme	endoplasmic	952:962	arg1	reticulum					964:972	the endoplasmic reticulum	948:972	the endoplasmic reticulum	948:972	Upon stimulation with an activator of intramembrane proteolysis such as brefeldin A and KDEL-tailed site 1 protease, unglycosylated or deglycosylated CREB-H was largely uncleaved, retained in an inactive form in the endoplasmic reticulum, and less capable of activating transcription driven by unfolded protein response element or C-reactive protein promoter.
20356926	5	33	theme	N-linked	499:506	arg1	sites					522:526	three N-linked glycosylation sites	493:526	three N-linked glycosylation sites in this region	493:541	We found that CREB-H is modified at three N-linked glycosylation sites in this region.
20356926	8	34	with	stimulation	741:751	arg1	activator					761:769	an activator	758:769	an activator of intramembrane proteolysis such as brefeldin A and KDEL-tailed site 1 protease	758:850	Upon stimulation with an activator of intramembrane proteolysis such as brefeldin A and KDEL-tailed site 1 protease, unglycosylated or deglycosylated CREB-H was largely uncleaved, retained in an inactive form in the endoplasmic reticulum, and less capable of activating transcription driven by unfolded protein response element or C-reactive protein promoter.
20356926	0	35	theme	optimal	39:45	arg1	activation					59:68	optimal proteolytic activation	39:68	optimal proteolytic activation of membrane-bound transcription factor CREB-H	39:114	N-linked glycosylation is required for optimal proteolytic activation of membrane-bound transcription factor CREB-H.
20356926	4	36	gly	glycosylation	392:404	arg1	domain					431:436	the luminal domain	419:436	the luminal domain at the C-terminus	419:454	In this study we characterized N-linked glycosylation of CREB-H in the luminal domain at the C-terminus.
20356926	4	36	gly	glycosylation	392:404	arg1	study					360:364	this study	355:364	this study	355:364	In this study we characterized N-linked glycosylation of CREB-H in the luminal domain at the C-terminus.
20356926	4	36	gly	glycosylation	392:404	arg1	CREB-H					409:414	CREB-H	409:414	CREB-H	409:414	In this study we characterized N-linked glycosylation of CREB-H in the luminal domain at the C-terminus.
20356926	2	37	theme	C-terminal	258:267	arg1	domain					283:288	a C-terminal transmembrane domain	256:288	a C-terminal transmembrane domain	256:288	CREB-H is activated by intramembrane proteolysis that removes a C-terminal transmembrane domain.
20356926	5	38	theme	glycosylation	508:520	arg1	sites					522:526	three N-linked glycosylation sites	493:526	three N-linked glycosylation sites in this region	493:541	We found that CREB-H is modified at three N-linked glycosylation sites in this region.
20356926	9	39	theme	intramembrane	1211:1223	arg1	proteolysis					1225:1235	intramembrane proteolysis	1211:1235	intramembrane proteolysis	1211:1235	Taken together, our findings suggest that N-linked glycosylation is required for full activation of CREB-H through intramembrane proteolysis.
20356926	8	40	theme	deglycosylated	871:884	arg1	CREB-H					886:891	unglycosylated or deglycosylated CREB-H	853:891	unglycosylated or deglycosylated CREB-H	853:891	Upon stimulation with an activator of intramembrane proteolysis such as brefeldin A and KDEL-tailed site 1 protease, unglycosylated or deglycosylated CREB-H was largely uncleaved, retained in an inactive form in the endoplasmic reticulum, and less capable of activating transcription driven by unfolded protein response element or C-reactive protein promoter.
20356926	9	41	gly	glycosylation	1147:1159	arg1	CREB-H					1196:1201	CREB-H	1196:1201	CREB-H	1196:1201	Taken together, our findings suggest that N-linked glycosylation is required for full activation of CREB-H through intramembrane proteolysis.
20356926	8	42	from	form	940:943	arg1	reticulum					964:972	the endoplasmic reticulum	948:972	the endoplasmic reticulum	948:972	Upon stimulation with an activator of intramembrane proteolysis such as brefeldin A and KDEL-tailed site 1 protease, unglycosylated or deglycosylated CREB-H was largely uncleaved, retained in an inactive form in the endoplasmic reticulum, and less capable of activating transcription driven by unfolded protein response element or C-reactive protein promoter.
20356926	0	43	gly	glycosylation	9:21	arg1	factor					102:107	membrane-bound transcription factor CREB-H	73:114	membrane-bound transcription factor CREB-H	73:114	N-linked glycosylation is required for optimal proteolytic activation of membrane-bound transcription factor CREB-H.
20356926	8	44	theme	proteolysis	788:798	arg1	activator					761:769	an activator	758:769	an activator of intramembrane proteolysis such as brefeldin A and KDEL-tailed site 1 protease	758:850	Upon stimulation with an activator of intramembrane proteolysis such as brefeldin A and KDEL-tailed site 1 protease, unglycosylated or deglycosylated CREB-H was largely uncleaved, retained in an inactive form in the endoplasmic reticulum, and less capable of activating transcription driven by unfolded protein response element or C-reactive protein promoter.
20356926	3	45	theme	liver	338:342	arg1	cancer					344:349	liver cancer	338:349	liver cancer	338:349	Aberrant expression of CREB-H is implicated in liver cancer.
20356926	9	46	theme	CREB-H	1196:1201	arg1	activation					1182:1191	full activation	1177:1191	full activation of CREB-H through intramembrane proteolysis	1177:1235	Taken together, our findings suggest that N-linked glycosylation is required for full activation of CREB-H through intramembrane proteolysis.
20356926	0	47	theme	proteolytic	47:57	arg1	activation					59:68	optimal proteolytic activation	39:68	optimal proteolytic activation of membrane-bound transcription factor CREB-H	39:114	N-linked glycosylation is required for optimal proteolytic activation of membrane-bound transcription factor CREB-H.
20356926	8	48	theme	brefeldin	808:816	arg1	A					818:818	brefeldin A	808:818	brefeldin A	808:818	Upon stimulation with an activator of intramembrane proteolysis such as brefeldin A and KDEL-tailed site 1 protease, unglycosylated or deglycosylated CREB-H was largely uncleaved, retained in an inactive form in the endoplasmic reticulum, and less capable of activating transcription driven by unfolded protein response element or C-reactive protein promoter.
20356926	1	49	theme	liver-enriched	129:142	arg1	CREB-H					117:122	CREB-H	117:122	CREB-H	117:122	CREB-H is a liver-enriched bZIP transcription factor of the CREB3 subfamily.
20356926	1	49	theme	liver-enriched	129:142	arg1	factor					163:168	a liver-enriched bZIP transcription factor	127:168	a liver-enriched bZIP transcription factor of the CREB3 subfamily	127:191	CREB-H is a liver-enriched bZIP transcription factor of the CREB3 subfamily.
20356926	6	50	theme	N-linked	624:631	arg1	glycosylation					633:645	N-linked glycosylation	624:645	N-linked glycosylation of CREB-H	624:655	Disruption of all three sites by site-directed mutagenesis completely abrogated N-linked glycosylation of CREB-H.
20356926	8	51	gly	unglycosylated	853:866	arg1	CREB-H					886:891	unglycosylated or deglycosylated CREB-H	853:891	unglycosylated or deglycosylated CREB-H	853:891	Upon stimulation with an activator of intramembrane proteolysis such as brefeldin A and KDEL-tailed site 1 protease, unglycosylated or deglycosylated CREB-H was largely uncleaved, retained in an inactive form in the endoplasmic reticulum, and less capable of activating transcription driven by unfolded protein response element or C-reactive protein promoter.
20356926	2	52	theme	intramembrane	217:229	arg1	proteolysis					231:241	intramembrane proteolysis	217:241	intramembrane proteolysis that removes a C-terminal transmembrane domain	217:288	CREB-H is activated by intramembrane proteolysis that removes a C-terminal transmembrane domain.
20356926	4	53	theme	N-linked	383:390	arg1	glycosylation					392:404	N-linked glycosylation	383:404	N-linked glycosylation of CREB-H in the luminal domain at the C-terminus	383:454	In this study we characterized N-linked glycosylation of CREB-H in the luminal domain at the C-terminus.
20356926	1	54	theme	bZIP	144:147	arg1	CREB-H					117:122	CREB-H	117:122	CREB-H	117:122	CREB-H is a liver-enriched bZIP transcription factor of the CREB3 subfamily.
20356926	1	54	theme	bZIP	144:147	arg1	factor					163:168	a liver-enriched bZIP transcription factor	127:168	a liver-enriched bZIP transcription factor of the CREB3 subfamily	127:191	CREB-H is a liver-enriched bZIP transcription factor of the CREB3 subfamily.
20356926	10	55	theme	transcription	1317:1329	arg1	regulation					1286:1295	the regulation	1282:1295	the regulation of CREB-H-dependent transcription	1282:1329	Our work also reveals a novel mechanism for the regulation of CREB-H-dependent transcription.
20356926	10	56	theme	novel	1262:1266	arg1	mechanism					1268:1276	a novel mechanism	1260:1276	a novel mechanism for the regulation of CREB-H-dependent transcription	1260:1329	Our work also reveals a novel mechanism for the regulation of CREB-H-dependent transcription.
20356926	4	57	from	C-terminus	445:454	arg1	domain					431:436	the luminal domain	419:436	the luminal domain at the C-terminus	419:454	In this study we characterized N-linked glycosylation of CREB-H in the luminal domain at the C-terminus.
20356926	4	57	from	C-terminus	445:454	arg1	glycosylation					392:404	N-linked glycosylation	383:404	N-linked glycosylation of CREB-H in the luminal domain at the C-terminus	383:454	In this study we characterized N-linked glycosylation of CREB-H in the luminal domain at the C-terminus.
20356926	1	58	theme	transcription	149:161	arg1	CREB-H					117:122	CREB-H	117:122	CREB-H	117:122	CREB-H is a liver-enriched bZIP transcription factor of the CREB3 subfamily.
20356926	1	58	theme	transcription	149:161	arg1	factor					163:168	a liver-enriched bZIP transcription factor	127:168	a liver-enriched bZIP transcription factor of the CREB3 subfamily	127:191	CREB-H is a liver-enriched bZIP transcription factor of the CREB3 subfamily.
20356926	10	59	theme	CREB-H-dependent	1300:1315	arg1	transcription					1317:1329	CREB-H-dependent transcription	1300:1329	CREB-H-dependent transcription	1300:1329	Our work also reveals a novel mechanism for the regulation of CREB-H-dependent transcription.
20356926	8	60	theme	A	818:818	arg1	protease					843:850	brefeldin A and KDEL-tailed site 1 protease	808:850	brefeldin A and KDEL-tailed site 1 protease	808:850	Upon stimulation with an activator of intramembrane proteolysis such as brefeldin A and KDEL-tailed site 1 protease, unglycosylated or deglycosylated CREB-H was largely uncleaved, retained in an inactive form in the endoplasmic reticulum, and less capable of activating transcription driven by unfolded protein response element or C-reactive protein promoter.
20356926	0	61	theme	membrane-bound	73:86	arg1	factor					102:107	membrane-bound transcription factor CREB-H	73:114	membrane-bound transcription factor CREB-H	73:114	N-linked glycosylation is required for optimal proteolytic activation of membrane-bound transcription factor CREB-H.
20356926	5	62	from	sites	522:526	arg1	region					536:541	this region	531:541	this region	531:541	We found that CREB-H is modified at three N-linked glycosylation sites in this region.
20356926	8	63	theme	site	836:839	arg1	protease					843:850	brefeldin A and KDEL-tailed site 1 protease	808:850	brefeldin A and KDEL-tailed site 1 protease	808:850	Upon stimulation with an activator of intramembrane proteolysis such as brefeldin A and KDEL-tailed site 1 protease, unglycosylated or deglycosylated CREB-H was largely uncleaved, retained in an inactive form in the endoplasmic reticulum, and less capable of activating transcription driven by unfolded protein response element or C-reactive protein promoter.
20356926	5	64	link	N-linked	499:506	arg1	sites					522:526	three N-linked glycosylation sites	493:526	three N-linked glycosylation sites in this region	493:541	We found that CREB-H is modified at three N-linked glycosylation sites in this region.
20356926	2	65	theme	transmembrane	269:281	arg1	domain					283:288	a C-terminal transmembrane domain	256:288	a C-terminal transmembrane domain	256:288	CREB-H is activated by intramembrane proteolysis that removes a C-terminal transmembrane domain.
20356926	6	66	link	N-linked	624:631	arg1	glycosylation					633:645	N-linked glycosylation	624:645	N-linked glycosylation of CREB-H	624:655	Disruption of all three sites by site-directed mutagenesis completely abrogated N-linked glycosylation of CREB-H.
20356926	8	67	theme	KDEL-tailed	824:834	arg1	site					836:839	KDEL-tailed site 1	824:841	KDEL-tailed site 1	824:841	Upon stimulation with an activator of intramembrane proteolysis such as brefeldin A and KDEL-tailed site 1 protease, unglycosylated or deglycosylated CREB-H was largely uncleaved, retained in an inactive form in the endoplasmic reticulum, and less capable of activating transcription driven by unfolded protein response element or C-reactive protein promoter.
23167757	3	0	theme	PDIA2	619:623	arg1	function					570:577	function	570:577	function	570:577	PDI family A member 2 (PDIA2, previously known as PDIp) has a similar domain structure to prototypical PDI (also known as PDIA1), but the function and post-translational modifications of PDIA2 remain poorly understood.
23167757	3	0	theme	PDIA2	619:623	arg1	modifications					602:614	post-translational modifications	583:614	post-translational modifications	583:614	PDI family A member 2 (PDIA2, previously known as PDIp) has a similar domain structure to prototypical PDI (also known as PDIA1), but the function and post-translational modifications of PDIA2 remain poorly understood.
23167757	8	1	theme	described	1578:1586	arg1	roles					1588:1592	its previously described roles	1563:1592	its previously described roles in autoimmunity and Parkinson's disease	1563:1632	Finally, we identified human major histocompatibility complex class 1 antigens (HLA-A,B,C) as potential binding partners of PDIA2, suggesting an involvement for PDIA2 in antigen presentation in addition to its previously described roles in autoimmunity and Parkinson's disease.
23167757	5	2	theme	potential	856:864	arg1	PDIA2					904:908	human PDIA2	898:908	human PDIA2 (N127, N284 and N516)	898:930	By site-directed mutagenesis and enzymatic deglycosylation, we show here that all three Asn residues within the potential N-linked glycosylation sites of human PDIA2 (N127, N284 and N516) are glycosylated in human cells.
23167757	5	2	theme	potential	856:864	arg1	sites					889:893	the potential N-linked glycosylation sites	852:893	the potential N-linked glycosylation sites of human PDIA2 (N127, N284 and N516)	852:930	By site-directed mutagenesis and enzymatic deglycosylation, we show here that all three Asn residues within the potential N-linked glycosylation sites of human PDIA2 (N127, N284 and N516) are glycosylated in human cells.
23167757	0	3	link	N-linked	0:7	arg1	glycosylation					9:21	N-linked glycosylation	0:21	N-linked glycosylation	0:21	N-linked glycosylation modulates dimerization of protein disulfide isomerase family A member 2 (PDIA2).
23167757	1	4	theme	important	157:165	arg1	enzymes					167:173	important enzymes	157:173	important enzymes for the correct folding and maturation of proteins that transit or reside in the endoplasmic reticulum (ER)	157:281	Protein disulfide isomerase (PDI) family members are important enzymes for the correct folding and maturation of proteins that transit or reside in the endoplasmic reticulum (ER).
23167757	1	4	theme	important	157:165	arg1	members					145:151	Protein disulfide isomerase (PDI) family members	104:151	Protein disulfide isomerase (PDI) family members	104:151	Protein disulfide isomerase (PDI) family members are important enzymes for the correct folding and maturation of proteins that transit or reside in the endoplasmic reticulum (ER).
23167757	8	5	from	involvement	1502:1512	arg1	presentation					1535:1546	antigen presentation	1527:1546	antigen presentation in addition to its previously described roles in autoimmunity and Parkinson's disease	1527:1632	Finally, we identified human major histocompatibility complex class 1 antigens (HLA-A,B,C) as potential binding partners of PDIA2, suggesting an involvement for PDIA2 in antigen presentation in addition to its previously described roles in autoimmunity and Parkinson's disease.
23167757	3	6	theme	domain	502:507	arg1	structure					509:517	a similar domain structure	492:517	a similar domain structure	492:517	PDI family A member 2 (PDIA2, previously known as PDIp) has a similar domain structure to prototypical PDI (also known as PDIA1), but the function and post-translational modifications of PDIA2 remain poorly understood.
23167757	1	7	theme	correct	183:189	arg1	folding					191:197	folding	191:197	folding	191:197	Protein disulfide isomerase (PDI) family members are important enzymes for the correct folding and maturation of proteins that transit or reside in the endoplasmic reticulum (ER).
23167757	1	8	theme	disulfide	112:120	arg1	isomerase					122:130	Protein disulfide isomerase	104:130	Protein disulfide isomerase (PDI) family members	104:151	Protein disulfide isomerase (PDI) family members are important enzymes for the correct folding and maturation of proteins that transit or reside in the endoplasmic reticulum (ER).
23167757	1	8	theme	disulfide	112:120	arg1	PDI					133:135	PDI	133:135	PDI	133:135	Protein disulfide isomerase (PDI) family members are important enzymes for the correct folding and maturation of proteins that transit or reside in the endoplasmic reticulum (ER).
23167757	8	9	theme	complex	1411:1417	arg1	class					1419:1423	major histocompatibility complex class 1	1386:1425	human major histocompatibility complex class 1 antigens (HLA-A,B,C)	1380:1446	Finally, we identified human major histocompatibility complex class 1 antigens (HLA-A,B,C) as potential binding partners of PDIA2, suggesting an involvement for PDIA2 in antigen presentation in addition to its previously described roles in autoimmunity and Parkinson's disease.
23167757	7	10	theme	subcellular	1331:1341	arg1	localization					1343:1354	subcellular localization	1331:1354	PDIA2 protein-protein interactions but not subcellular localization	1288:1354	Nevertheless, in HeLa cells, both wild-type and N127/284/516Q mutant PDIA2 proteins localize to the ER, but not the ER-Golgi intermediate compartment, suggesting that glycosylation is important for PDIA2 protein-protein interactions but not subcellular localization.
23167757	4	11	contain	contains	689:696	arg1	PDIA2					683:687	PDIA2	683:687	PDIA2	683:687	Unlike most PDI family members, PDIA2 contains three predicted N-linked glycosylation sites.
23167757	4	11	contain	contains	689:696	arg2	sites					737:741	three predicted N-linked glycosylation sites	698:741	three predicted N-linked glycosylation sites	698:741	Unlike most PDI family members, PDIA2 contains three predicted N-linked glycosylation sites.
23167757	5	12	theme	N-linked	866:873	arg1	PDIA2					904:908	human PDIA2	898:908	human PDIA2 (N127, N284 and N516)	898:930	By site-directed mutagenesis and enzymatic deglycosylation, we show here that all three Asn residues within the potential N-linked glycosylation sites of human PDIA2 (N127, N284 and N516) are glycosylated in human cells.
23167757	5	12	theme	N-linked	866:873	arg1	sites					889:893	the potential N-linked glycosylation sites	852:893	the potential N-linked glycosylation sites of human PDIA2 (N127, N284 and N516)	852:930	By site-directed mutagenesis and enzymatic deglycosylation, we show here that all three Asn residues within the potential N-linked glycosylation sites of human PDIA2 (N127, N284 and N516) are glycosylated in human cells.
23167757	9	13	theme	defined	1682:1688	arg1	member					1690:1695	this poorly defined member	1670:1695	this poorly defined member of the PDI family	1670:1713	These results further characterize this poorly defined member of the PDI family.
23167757	7	14	theme	protein-protein	1294:1308	arg1	interactions					1310:1321	PDIA2 protein-protein interactions	1288:1321	PDIA2 protein-protein interactions but not subcellular localization	1288:1354	Nevertheless, in HeLa cells, both wild-type and N127/284/516Q mutant PDIA2 proteins localize to the ER, but not the ER-Golgi intermediate compartment, suggesting that glycosylation is important for PDIA2 protein-protein interactions but not subcellular localization.
23167757	4	15	theme	PDI	663:665	arg1	members					674:680	most PDI family members	658:680	most PDI family members	658:680	Unlike most PDI family members, PDIA2 contains three predicted N-linked glycosylation sites.
23167757	1	16	theme	isomerase	122:130	arg1	enzymes					167:173	important enzymes	157:173	important enzymes for the correct folding and maturation of proteins that transit or reside in the endoplasmic reticulum (ER)	157:281	Protein disulfide isomerase (PDI) family members are important enzymes for the correct folding and maturation of proteins that transit or reside in the endoplasmic reticulum (ER).
23167757	1	16	theme	isomerase	122:130	arg1	members					145:151	Protein disulfide isomerase (PDI) family members	104:151	Protein disulfide isomerase (PDI) family members	104:151	Protein disulfide isomerase (PDI) family members are important enzymes for the correct folding and maturation of proteins that transit or reside in the endoplasmic reticulum (ER).
23167757	3	17	theme	family	436:441	arg1	member					445:450	PDI family A member 2	432:452	PDI family A member 2 (PDIA2, previously known as PDIp)	432:486	PDI family A member 2 (PDIA2, previously known as PDIp) has a similar domain structure to prototypical PDI (also known as PDIA1), but the function and post-translational modifications of PDIA2 remain poorly understood.
23167757	5	18	dep	PDIA2	904:908	arg1	N516					926:929	N516	926:929	N516	926:929	By site-directed mutagenesis and enzymatic deglycosylation, we show here that all three Asn residues within the potential N-linked glycosylation sites of human PDIA2 (N127, N284 and N516) are glycosylated in human cells.
23167757	5	18	dep	PDIA2	904:908	arg1	N284					917:920	N284	917:920	N284	917:920	By site-directed mutagenesis and enzymatic deglycosylation, we show here that all three Asn residues within the potential N-linked glycosylation sites of human PDIA2 (N127, N284 and N516) are glycosylated in human cells.
23167757	5	18	dep	PDIA2	904:908	arg1	N127					911:914	N127	911:914	N127	911:914	By site-directed mutagenesis and enzymatic deglycosylation, we show here that all three Asn residues within the potential N-linked glycosylation sites of human PDIA2 (N127, N284 and N516) are glycosylated in human cells.
23167757	0	19	theme	family	77:82	arg1	member					86:91	family A member 2	77:93	protein disulfide isomerase family A member 2 (PDIA2)	49:101	N-linked glycosylation modulates dimerization of protein disulfide isomerase family A member 2 (PDIA2).
23167757	0	19	theme	family	77:82	arg1	PDIA2					96:100	PDIA2	96:100	PDIA2	96:100	N-linked glycosylation modulates dimerization of protein disulfide isomerase family A member 2 (PDIA2).
23167757	7	20	theme	HeLa	1107:1110	arg1	cells					1112:1116	HeLa cells	1107:1116	HeLa cells	1107:1116	Nevertheless, in HeLa cells, both wild-type and N127/284/516Q mutant PDIA2 proteins localize to the ER, but not the ER-Golgi intermediate compartment, suggesting that glycosylation is important for PDIA2 protein-protein interactions but not subcellular localization.
23167757	9	21	theme	PDI	1704:1706	arg1	family					1708:1713	the PDI family	1700:1713	the PDI family	1700:1713	These results further characterize this poorly defined member of the PDI family.
23167757	7	22	theme	PDIA2	1159:1163	arg1	proteins					1165:1172	both wild-type and N127/284/516Q mutant PDIA2 proteins	1119:1172	both wild-type and N127/284/516Q mutant PDIA2 proteins	1119:1172	Nevertheless, in HeLa cells, both wild-type and N127/284/516Q mutant PDIA2 proteins localize to the ER, but not the ER-Golgi intermediate compartment, suggesting that glycosylation is important for PDIA2 protein-protein interactions but not subcellular localization.
23167757	8	23	theme	potential	1451:1459	arg1	antigens					1427:1434	human major histocompatibility complex class 1 antigens	1380:1434	human major histocompatibility complex class 1 antigens (HLA-A,B,C)	1380:1446	Finally, we identified human major histocompatibility complex class 1 antigens (HLA-A,B,C) as potential binding partners of PDIA2, suggesting an involvement for PDIA2 in antigen presentation in addition to its previously described roles in autoimmunity and Parkinson's disease.
23167757	8	23	theme	potential	1451:1459	arg1	partners					1469:1476	potential binding partners	1451:1476	potential binding partners of PDIA2	1451:1485	Finally, we identified human major histocompatibility complex class 1 antigens (HLA-A,B,C) as potential binding partners of PDIA2, suggesting an involvement for PDIA2 in antigen presentation in addition to its previously described roles in autoimmunity and Parkinson's disease.
23167757	4	24	theme	N-linked	714:721	arg1	sites					737:741	three predicted N-linked glycosylation sites	698:741	three predicted N-linked glycosylation sites	698:741	Unlike most PDI family members, PDIA2 contains three predicted N-linked glycosylation sites.
23167757	2	25	theme	cell	350:353	arg1	expression					360:369	cell type expression	350:369	cell type expression	350:369	The human PDI family comprises at least 19 members that differ in cell type expression, substrate specificity and post-translational modifications.
23167757	7	26	theme	wild-type	1124:1132	arg1	proteins					1165:1172	both wild-type and N127/284/516Q mutant PDIA2 proteins	1119:1172	both wild-type and N127/284/516Q mutant PDIA2 proteins	1119:1172	Nevertheless, in HeLa cells, both wild-type and N127/284/516Q mutant PDIA2 proteins localize to the ER, but not the ER-Golgi intermediate compartment, suggesting that glycosylation is important for PDIA2 protein-protein interactions but not subcellular localization.
23167757	0	27	theme	protein	49:55	arg1	isomerase					67:75	protein disulfide isomerase family A member 2 (PDIA2)	49:101	protein disulfide isomerase family A member 2 (PDIA2)	49:101	N-linked glycosylation modulates dimerization of protein disulfide isomerase family A member 2 (PDIA2).
23167757	6	28	theme	glycosylation-null	998:1015	arg1	Gln					1017:1019	glycosylation-null Gln	998:1019	glycosylation-null Gln	998:1019	Furthermore, mutation of N284 to glycosylation-null Gln increases formation of a highly stable disulfide-bonded PDIA2 dimer.
23167757	0	29	theme	N-linked	0:7	arg1	glycosylation					9:21	N-linked glycosylation	0:21	N-linked glycosylation	0:21	N-linked glycosylation modulates dimerization of protein disulfide isomerase family A member 2 (PDIA2).
23167757	5	30	theme	human	898:902	arg1	PDIA2					904:908	human PDIA2	898:908	human PDIA2 (N127, N284 and N516)	898:930	By site-directed mutagenesis and enzymatic deglycosylation, we show here that all three Asn residues within the potential N-linked glycosylation sites of human PDIA2 (N127, N284 and N516) are glycosylated in human cells.
23167757	6	31	theme	N284	990:993	arg1	mutation					978:985	mutation	978:985	mutation of N284 to glycosylation-null Gln	978:1019	Furthermore, mutation of N284 to glycosylation-null Gln increases formation of a highly stable disulfide-bonded PDIA2 dimer.
23167757	8	32	theme	PDIA2	1481:1485	arg1	antigens					1427:1434	human major histocompatibility complex class 1 antigens	1380:1434	human major histocompatibility complex class 1 antigens (HLA-A,B,C)	1380:1446	Finally, we identified human major histocompatibility complex class 1 antigens (HLA-A,B,C) as potential binding partners of PDIA2, suggesting an involvement for PDIA2 in antigen presentation in addition to its previously described roles in autoimmunity and Parkinson's disease.
23167757	8	32	theme	PDIA2	1481:1485	arg1	partners					1469:1476	potential binding partners	1451:1476	potential binding partners of PDIA2	1451:1485	Finally, we identified human major histocompatibility complex class 1 antigens (HLA-A,B,C) as potential binding partners of PDIA2, suggesting an involvement for PDIA2 in antigen presentation in addition to its previously described roles in autoimmunity and Parkinson's disease.
23167757	2	33	theme	substrate	372:380	arg1	specificity					382:392	substrate specificity	372:392	substrate specificity	372:392	The human PDI family comprises at least 19 members that differ in cell type expression, substrate specificity and post-translational modifications.
23167757	5	34	theme	enzymatic	777:785	arg1	deglycosylation					787:801	enzymatic deglycosylation	777:801	enzymatic deglycosylation	777:801	By site-directed mutagenesis and enzymatic deglycosylation, we show here that all three Asn residues within the potential N-linked glycosylation sites of human PDIA2 (N127, N284 and N516) are glycosylated in human cells.
23167757	8	35	dep	antigens	1427:1434	arg1	HLA-A					1437:1441	HLA-A	1437:1441	HLA-A	1437:1441	Finally, we identified human major histocompatibility complex class 1 antigens (HLA-A,B,C) as potential binding partners of PDIA2, suggesting an involvement for PDIA2 in antigen presentation in addition to its previously described roles in autoimmunity and Parkinson's disease.
23167757	8	35	dep	antigens	1427:1434	arg1	C					1445:1445	C	1445:1445	C	1445:1445	Finally, we identified human major histocompatibility complex class 1 antigens (HLA-A,B,C) as potential binding partners of PDIA2, suggesting an involvement for PDIA2 in antigen presentation in addition to its previously described roles in autoimmunity and Parkinson's disease.
23167757	8	35	dep	antigens	1427:1434	arg1	B					1443:1443	B	1443:1443	B	1443:1443	Finally, we identified human major histocompatibility complex class 1 antigens (HLA-A,B,C) as potential binding partners of PDIA2, suggesting an involvement for PDIA2 in antigen presentation in addition to its previously described roles in autoimmunity and Parkinson's disease.
23167757	5	36	theme	human	952:956	arg1	cells					958:962	human cells	952:962	human cells	952:962	By site-directed mutagenesis and enzymatic deglycosylation, we show here that all three Asn residues within the potential N-linked glycosylation sites of human PDIA2 (N127, N284 and N516) are glycosylated in human cells.
23167757	5	37	gly	glycosylated	936:947	arg1	cells					958:962	human cells	952:962	human cells	952:962	By site-directed mutagenesis and enzymatic deglycosylation, we show here that all three Asn residues within the potential N-linked glycosylation sites of human PDIA2 (N127, N284 and N516) are glycosylated in human cells.
23167757	5	37	gly	glycosylated	936:947	arg1	residues					836:843	all three Asn residues	822:843	all three Asn residues within the potential N-linked glycosylation sites of human PDIA2 (N127, N284 and N516)	822:930	By site-directed mutagenesis and enzymatic deglycosylation, we show here that all three Asn residues within the potential N-linked glycosylation sites of human PDIA2 (N127, N284 and N516) are glycosylated in human cells.
23167757	5	37	gly	glycosylated	936:947	arg2	residues					836:843	all three Asn residues	822:843	all three Asn residues within the potential N-linked glycosylation sites of human PDIA2 (N127, N284 and N516)	822:930	By site-directed mutagenesis and enzymatic deglycosylation, we show here that all three Asn residues within the potential N-linked glycosylation sites of human PDIA2 (N127, N284 and N516) are glycosylated in human cells.
23167757	0	38	theme	disulfide	57:65	arg1	isomerase					67:75	protein disulfide isomerase family A member 2 (PDIA2)	49:101	protein disulfide isomerase family A member 2 (PDIA2)	49:101	N-linked glycosylation modulates dimerization of protein disulfide isomerase family A member 2 (PDIA2).
23167757	6	39	theme	disulfide-bonded	1060:1075	arg1	dimer					1083:1087	a highly stable disulfide-bonded PDIA2 dimer	1044:1087	a highly stable disulfide-bonded PDIA2 dimer	1044:1087	Furthermore, mutation of N284 to glycosylation-null Gln increases formation of a highly stable disulfide-bonded PDIA2 dimer.
23167757	3	40	contain	has	488:490	arg1	member					445:450	PDI family A member 2	432:452	PDI family A member 2 (PDIA2, previously known as PDIp)	432:486	PDI family A member 2 (PDIA2, previously known as PDIp) has a similar domain structure to prototypical PDI (also known as PDIA1), but the function and post-translational modifications of PDIA2 remain poorly understood.
23167757	3	40	contain	has	488:490	arg2	structure					509:517	a similar domain structure	492:517	a similar domain structure	492:517	PDI family A member 2 (PDIA2, previously known as PDIp) has a similar domain structure to prototypical PDI (also known as PDIA1), but the function and post-translational modifications of PDIA2 remain poorly understood.
23167757	8	41	theme	human	1380:1384	arg1	antigens					1427:1434	human major histocompatibility complex class 1 antigens	1380:1434	human major histocompatibility complex class 1 antigens (HLA-A,B,C)	1380:1446	Finally, we identified human major histocompatibility complex class 1 antigens (HLA-A,B,C) as potential binding partners of PDIA2, suggesting an involvement for PDIA2 in antigen presentation in addition to its previously described roles in autoimmunity and Parkinson's disease.
23167757	8	41	theme	human	1380:1384	arg1	partners					1469:1476	potential binding partners	1451:1476	potential binding partners of PDIA2	1451:1485	Finally, we identified human major histocompatibility complex class 1 antigens (HLA-A,B,C) as potential binding partners of PDIA2, suggesting an involvement for PDIA2 in antigen presentation in addition to its previously described roles in autoimmunity and Parkinson's disease.
23167757	2	42	theme	PDI	294:296	arg1	family					298:303	The human PDI family	284:303	The human PDI family	284:303	The human PDI family comprises at least 19 members that differ in cell type expression, substrate specificity and post-translational modifications.
23167757	5	43	link	N-linked	866:873	arg1	PDIA2					904:908	human PDIA2	898:908	human PDIA2 (N127, N284 and N516)	898:930	By site-directed mutagenesis and enzymatic deglycosylation, we show here that all three Asn residues within the potential N-linked glycosylation sites of human PDIA2 (N127, N284 and N516) are glycosylated in human cells.
23167757	5	43	link	N-linked	866:873	arg1	sites					889:893	the potential N-linked glycosylation sites	852:893	the potential N-linked glycosylation sites of human PDIA2 (N127, N284 and N516)	852:930	By site-directed mutagenesis and enzymatic deglycosylation, we show here that all three Asn residues within the potential N-linked glycosylation sites of human PDIA2 (N127, N284 and N516) are glycosylated in human cells.
23167757	8	44	theme	antigen	1527:1533	arg1	presentation					1535:1546	antigen presentation	1527:1546	antigen presentation in addition to its previously described roles in autoimmunity and Parkinson's disease	1527:1632	Finally, we identified human major histocompatibility complex class 1 antigens (HLA-A,B,C) as potential binding partners of PDIA2, suggesting an involvement for PDIA2 in antigen presentation in addition to its previously described roles in autoimmunity and Parkinson's disease.
23167757	3	45	theme	post-translational	583:600	arg1	modifications					602:614	post-translational modifications	583:614	post-translational modifications	583:614	PDI family A member 2 (PDIA2, previously known as PDIp) has a similar domain structure to prototypical PDI (also known as PDIA1), but the function and post-translational modifications of PDIA2 remain poorly understood.
23167757	8	46	theme	histocompatibility	1392:1409	arg1	class					1419:1423	major histocompatibility complex class 1	1386:1425	human major histocompatibility complex class 1 antigens (HLA-A,B,C)	1380:1446	Finally, we identified human major histocompatibility complex class 1 antigens (HLA-A,B,C) as potential binding partners of PDIA2, suggesting an involvement for PDIA2 in antigen presentation in addition to its previously described roles in autoimmunity and Parkinson's disease.
23167757	3	47	dep	PDI	535:537	arg1	known					545:549	known	545:549	known as PDIA1	545:558	PDI family A member 2 (PDIA2, previously known as PDIp) has a similar domain structure to prototypical PDI (also known as PDIA1), but the function and post-translational modifications of PDIA2 remain poorly understood.
23167757	1	48	theme	proteins	217:224	arg1	maturation					203:212	maturation	203:212	maturation	203:212	Protein disulfide isomerase (PDI) family members are important enzymes for the correct folding and maturation of proteins that transit or reside in the endoplasmic reticulum (ER).
23167757	1	48	theme	proteins	217:224	arg1	folding					191:197	folding	191:197	folding	191:197	Protein disulfide isomerase (PDI) family members are important enzymes for the correct folding and maturation of proteins that transit or reside in the endoplasmic reticulum (ER).
23167757	3	49	theme	PDI	432:434	arg1	member					445:450	PDI family A member 2	432:452	PDI family A member 2 (PDIA2, previously known as PDIp)	432:486	PDI family A member 2 (PDIA2, previously known as PDIp) has a similar domain structure to prototypical PDI (also known as PDIA1), but the function and post-translational modifications of PDIA2 remain poorly understood.
23167757	6	50	theme	PDIA2	1077:1081	arg1	dimer					1083:1087	a highly stable disulfide-bonded PDIA2 dimer	1044:1087	a highly stable disulfide-bonded PDIA2 dimer	1044:1087	Furthermore, mutation of N284 to glycosylation-null Gln increases formation of a highly stable disulfide-bonded PDIA2 dimer.
23167757	3	51	theme	similar	494:500	arg1	structure					509:517	a similar domain structure	492:517	a similar domain structure	492:517	PDI family A member 2 (PDIA2, previously known as PDIp) has a similar domain structure to prototypical PDI (also known as PDIA1), but the function and post-translational modifications of PDIA2 remain poorly understood.
23167757	3	52	dep	known	545:549	arg1	also					540:543	also	540:543	also	540:543	PDI family A member 2 (PDIA2, previously known as PDIp) has a similar domain structure to prototypical PDI (also known as PDIA1), but the function and post-translational modifications of PDIA2 remain poorly understood.
23167757	8	53	theme	class	1419:1423	arg1	antigens					1427:1434	human major histocompatibility complex class 1 antigens	1380:1434	human major histocompatibility complex class 1 antigens (HLA-A,B,C)	1380:1446	Finally, we identified human major histocompatibility complex class 1 antigens (HLA-A,B,C) as potential binding partners of PDIA2, suggesting an involvement for PDIA2 in antigen presentation in addition to its previously described roles in autoimmunity and Parkinson's disease.
23167757	8	53	theme	class	1419:1423	arg1	partners					1469:1476	potential binding partners	1451:1476	potential binding partners of PDIA2	1451:1485	Finally, we identified human major histocompatibility complex class 1 antigens (HLA-A,B,C) as potential binding partners of PDIA2, suggesting an involvement for PDIA2 in antigen presentation in addition to its previously described roles in autoimmunity and Parkinson's disease.
23167757	6	54	theme	dimer	1083:1087	arg1	formation					1031:1039	formation	1031:1039	formation of a highly stable disulfide-bonded PDIA2 dimer	1031:1087	Furthermore, mutation of N284 to glycosylation-null Gln increases formation of a highly stable disulfide-bonded PDIA2 dimer.
23167757	7	55	theme	ER-Golgi	1206:1213	arg1	compartment					1228:1238	the ER-Golgi intermediate compartment	1202:1238	the ER-Golgi intermediate compartment	1202:1238	Nevertheless, in HeLa cells, both wild-type and N127/284/516Q mutant PDIA2 proteins localize to the ER, but not the ER-Golgi intermediate compartment, suggesting that glycosylation is important for PDIA2 protein-protein interactions but not subcellular localization.
23167757	5	56	gly	glycosylation	875:887	arg2	sites					889:893	the potential N-linked glycosylation sites	852:893	the potential N-linked glycosylation sites of human PDIA2 (N127, N284 and N516)	852:930	By site-directed mutagenesis and enzymatic deglycosylation, we show here that all three Asn residues within the potential N-linked glycosylation sites of human PDIA2 (N127, N284 and N516) are glycosylated in human cells.
23167757	5	56	gly	glycosylation	875:887	arg1	PDIA2					904:908	human PDIA2	898:908	human PDIA2 (N127, N284 and N516)	898:930	By site-directed mutagenesis and enzymatic deglycosylation, we show here that all three Asn residues within the potential N-linked glycosylation sites of human PDIA2 (N127, N284 and N516) are glycosylated in human cells.
23167757	5	56	gly	glycosylation	875:887	arg2	PDIA2					904:908	human PDIA2	898:908	human PDIA2 (N127, N284 and N516)	898:930	By site-directed mutagenesis and enzymatic deglycosylation, we show here that all three Asn residues within the potential N-linked glycosylation sites of human PDIA2 (N127, N284 and N516) are glycosylated in human cells.
23167757	3	57	theme	prototypical	522:533	arg1	PDI					535:537	prototypical PDI	522:537	prototypical PDI (also known as PDIA1)	522:559	PDI family A member 2 (PDIA2, previously known as PDIp) has a similar domain structure to prototypical PDI (also known as PDIA1), but the function and post-translational modifications of PDIA2 remain poorly understood.
23167757	1	58	theme	Protein	104:110	arg1	isomerase					122:130	Protein disulfide isomerase	104:130	Protein disulfide isomerase (PDI) family members	104:151	Protein disulfide isomerase (PDI) family members are important enzymes for the correct folding and maturation of proteins that transit or reside in the endoplasmic reticulum (ER).
23167757	1	58	theme	Protein	104:110	arg1	PDI					133:135	PDI	133:135	PDI	133:135	Protein disulfide isomerase (PDI) family members are important enzymes for the correct folding and maturation of proteins that transit or reside in the endoplasmic reticulum (ER).
23167757	1	59	dep	folding	191:197	arg1	the					179:181	the	179:181	the	179:181	Protein disulfide isomerase (PDI) family members are important enzymes for the correct folding and maturation of proteins that transit or reside in the endoplasmic reticulum (ER).
23167757	5	60	theme	glycosylation	875:887	arg1	PDIA2					904:908	human PDIA2	898:908	human PDIA2 (N127, N284 and N516)	898:930	By site-directed mutagenesis and enzymatic deglycosylation, we show here that all three Asn residues within the potential N-linked glycosylation sites of human PDIA2 (N127, N284 and N516) are glycosylated in human cells.
23167757	5	60	theme	glycosylation	875:887	arg1	sites					889:893	the potential N-linked glycosylation sites	852:893	the potential N-linked glycosylation sites of human PDIA2 (N127, N284 and N516)	852:930	By site-directed mutagenesis and enzymatic deglycosylation, we show here that all three Asn residues within the potential N-linked glycosylation sites of human PDIA2 (N127, N284 and N516) are glycosylated in human cells.
23167757	4	61	theme	most	658:661	arg1	members					674:680	most PDI family members	658:680	most PDI family members	658:680	Unlike most PDI family members, PDIA2 contains three predicted N-linked glycosylation sites.
23167757	0	62	theme	A	84:84	arg1	member					86:91	family A member 2	77:93	protein disulfide isomerase family A member 2 (PDIA2)	49:101	N-linked glycosylation modulates dimerization of protein disulfide isomerase family A member 2 (PDIA2).
23167757	0	62	theme	A	84:84	arg1	PDIA2					96:100	PDIA2	96:100	PDIA2	96:100	N-linked glycosylation modulates dimerization of protein disulfide isomerase family A member 2 (PDIA2).
23167757	5	63	theme	Asn	832:834	arg1	residues					836:843	all three Asn residues	822:843	all three Asn residues within the potential N-linked glycosylation sites of human PDIA2 (N127, N284 and N516)	822:930	By site-directed mutagenesis and enzymatic deglycosylation, we show here that all three Asn residues within the potential N-linked glycosylation sites of human PDIA2 (N127, N284 and N516) are glycosylated in human cells.
23167757	7	64	theme	PDIA2	1288:1292	arg1	interactions					1310:1321	PDIA2 protein-protein interactions	1288:1321	PDIA2 protein-protein interactions but not subcellular localization	1288:1354	Nevertheless, in HeLa cells, both wild-type and N127/284/516Q mutant PDIA2 proteins localize to the ER, but not the ER-Golgi intermediate compartment, suggesting that glycosylation is important for PDIA2 protein-protein interactions but not subcellular localization.
23167757	7	65	theme	mutant	1152:1157	arg1	proteins					1165:1172	both wild-type and N127/284/516Q mutant PDIA2 proteins	1119:1172	both wild-type and N127/284/516Q mutant PDIA2 proteins	1119:1172	Nevertheless, in HeLa cells, both wild-type and N127/284/516Q mutant PDIA2 proteins localize to the ER, but not the ER-Golgi intermediate compartment, suggesting that glycosylation is important for PDIA2 protein-protein interactions but not subcellular localization.
23167757	1	66	theme	family	138:143	arg1	enzymes					167:173	important enzymes	157:173	important enzymes for the correct folding and maturation of proteins that transit or reside in the endoplasmic reticulum (ER)	157:281	Protein disulfide isomerase (PDI) family members are important enzymes for the correct folding and maturation of proteins that transit or reside in the endoplasmic reticulum (ER).
23167757	1	66	theme	family	138:143	arg1	members					145:151	Protein disulfide isomerase (PDI) family members	104:151	Protein disulfide isomerase (PDI) family members	104:151	Protein disulfide isomerase (PDI) family members are important enzymes for the correct folding and maturation of proteins that transit or reside in the endoplasmic reticulum (ER).
23167757	9	67	theme	family	1708:1713	arg1	member					1690:1695	this poorly defined member	1670:1695	this poorly defined member of the PDI family	1670:1713	These results further characterize this poorly defined member of the PDI family.
23167757	3	68	dep	member	445:450	arg1	PDIA2					455:459	PDIA2	455:459	PDIA2	455:459	PDI family A member 2 (PDIA2, previously known as PDIp) has a similar domain structure to prototypical PDI (also known as PDIA1), but the function and post-translational modifications of PDIA2 remain poorly understood.
23167757	8	69	theme	binding	1461:1467	arg1	antigens					1427:1434	human major histocompatibility complex class 1 antigens	1380:1434	human major histocompatibility complex class 1 antigens (HLA-A,B,C)	1380:1446	Finally, we identified human major histocompatibility complex class 1 antigens (HLA-A,B,C) as potential binding partners of PDIA2, suggesting an involvement for PDIA2 in antigen presentation in addition to its previously described roles in autoimmunity and Parkinson's disease.
23167757	8	69	theme	binding	1461:1467	arg1	partners					1469:1476	potential binding partners	1451:1476	potential binding partners of PDIA2	1451:1485	Finally, we identified human major histocompatibility complex class 1 antigens (HLA-A,B,C) as potential binding partners of PDIA2, suggesting an involvement for PDIA2 in antigen presentation in addition to its previously described roles in autoimmunity and Parkinson's disease.
23167757	8	70	from	roles	1588:1592	arg1	autoimmunity					1597:1608	autoimmunity	1597:1608	autoimmunity	1597:1608	Finally, we identified human major histocompatibility complex class 1 antigens (HLA-A,B,C) as potential binding partners of PDIA2, suggesting an involvement for PDIA2 in antigen presentation in addition to its previously described roles in autoimmunity and Parkinson's disease.
23167757	8	70	from	roles	1588:1592	arg1	disease					1626:1632	Parkinson's disease	1614:1632	Parkinson's disease	1614:1632	Finally, we identified human major histocompatibility complex class 1 antigens (HLA-A,B,C) as potential binding partners of PDIA2, suggesting an involvement for PDIA2 in antigen presentation in addition to its previously described roles in autoimmunity and Parkinson's disease.
23167757	5	71	theme	site-directed	747:759	arg1	mutagenesis					761:771	site-directed mutagenesis	747:771	site-directed mutagenesis	747:771	By site-directed mutagenesis and enzymatic deglycosylation, we show here that all three Asn residues within the potential N-linked glycosylation sites of human PDIA2 (N127, N284 and N516) are glycosylated in human cells.
23167757	7	72	gly	glycosylation	1257:1269	arg1	PDIA2					1288:1292	PDIA2 protein-protein interactions	1288:1321	PDIA2 protein-protein interactions but not subcellular localization	1288:1354	Nevertheless, in HeLa cells, both wild-type and N127/284/516Q mutant PDIA2 proteins localize to the ER, but not the ER-Golgi intermediate compartment, suggesting that glycosylation is important for PDIA2 protein-protein interactions but not subcellular localization.
23167757	2	73	theme	post-translational	398:415	arg1	modifications					417:429	post-translational modifications	398:429	post-translational modifications	398:429	The human PDI family comprises at least 19 members that differ in cell type expression, substrate specificity and post-translational modifications.
23167757	4	74	theme	family	667:672	arg1	members					674:680	most PDI family members	658:680	most PDI family members	658:680	Unlike most PDI family members, PDIA2 contains three predicted N-linked glycosylation sites.
23167757	1	75	theme	endoplasmic	256:266	arg1	reticulum					268:276	the endoplasmic reticulum	252:276	the endoplasmic reticulum (ER)	252:281	Protein disulfide isomerase (PDI) family members are important enzymes for the correct folding and maturation of proteins that transit or reside in the endoplasmic reticulum (ER).
23167757	1	75	theme	endoplasmic	256:266	arg1	ER					279:280	ER	279:280	ER	279:280	Protein disulfide isomerase (PDI) family members are important enzymes for the correct folding and maturation of proteins that transit or reside in the endoplasmic reticulum (ER).
23167757	5	76	theme	PDIA2	904:908	arg1	PDIA2					904:908	human PDIA2	898:908	human PDIA2 (N127, N284 and N516)	898:930	By site-directed mutagenesis and enzymatic deglycosylation, we show here that all three Asn residues within the potential N-linked glycosylation sites of human PDIA2 (N127, N284 and N516) are glycosylated in human cells.
23167757	5	76	theme	PDIA2	904:908	arg1	sites					889:893	the potential N-linked glycosylation sites	852:893	the potential N-linked glycosylation sites of human PDIA2 (N127, N284 and N516)	852:930	By site-directed mutagenesis and enzymatic deglycosylation, we show here that all three Asn residues within the potential N-linked glycosylation sites of human PDIA2 (N127, N284 and N516) are glycosylated in human cells.
23167757	3	77	theme	A	443:443	arg1	member					445:450	PDI family A member 2	432:452	PDI family A member 2 (PDIA2, previously known as PDIp)	432:486	PDI family A member 2 (PDIA2, previously known as PDIp) has a similar domain structure to prototypical PDI (also known as PDIA1), but the function and post-translational modifications of PDIA2 remain poorly understood.
23167757	4	78	gly	glycosylation	723:735	arg2	three					698:702	three	698:702	three	698:702	Unlike most PDI family members, PDIA2 contains three predicted N-linked glycosylation sites.
23167757	4	78	gly	glycosylation	723:735	arg2	sites					737:741	three predicted N-linked glycosylation sites	698:741	three predicted N-linked glycosylation sites	698:741	Unlike most PDI family members, PDIA2 contains three predicted N-linked glycosylation sites.
23167757	0	79	dep	isomerase	67:75	arg1	member					86:91	family A member 2	77:93	protein disulfide isomerase family A member 2 (PDIA2)	49:101	N-linked glycosylation modulates dimerization of protein disulfide isomerase family A member 2 (PDIA2).
23167757	0	79	dep	isomerase	67:75	arg1	PDIA2					96:100	PDIA2	96:100	PDIA2	96:100	N-linked glycosylation modulates dimerization of protein disulfide isomerase family A member 2 (PDIA2).
23167757	7	80	theme	intermediate	1215:1226	arg1	compartment					1228:1238	the ER-Golgi intermediate compartment	1202:1238	the ER-Golgi intermediate compartment	1202:1238	Nevertheless, in HeLa cells, both wild-type and N127/284/516Q mutant PDIA2 proteins localize to the ER, but not the ER-Golgi intermediate compartment, suggesting that glycosylation is important for PDIA2 protein-protein interactions but not subcellular localization.
23167757	2	81	theme	type	355:358	arg1	expression					360:369	cell type expression	350:369	cell type expression	350:369	The human PDI family comprises at least 19 members that differ in cell type expression, substrate specificity and post-translational modifications.
23167757	0	82	theme	isomerase	67:75	arg1	dimerization					33:44	dimerization	33:44	dimerization of protein disulfide isomerase family A member 2 (PDIA2)	33:101	N-linked glycosylation modulates dimerization of protein disulfide isomerase family A member 2 (PDIA2).
23167757	4	83	link	N-linked	714:721	arg1	sites					737:741	three predicted N-linked glycosylation sites	698:741	three predicted N-linked glycosylation sites	698:741	Unlike most PDI family members, PDIA2 contains three predicted N-linked glycosylation sites.
23167757	6	84	theme	stable	1053:1058	arg1	dimer					1083:1087	a highly stable disulfide-bonded PDIA2 dimer	1044:1087	a highly stable disulfide-bonded PDIA2 dimer	1044:1087	Furthermore, mutation of N284 to glycosylation-null Gln increases formation of a highly stable disulfide-bonded PDIA2 dimer.
23167757	4	85	theme	predicted	704:712	arg1	sites					737:741	three predicted N-linked glycosylation sites	698:741	three predicted N-linked glycosylation sites	698:741	Unlike most PDI family members, PDIA2 contains three predicted N-linked glycosylation sites.
23167757	4	86	theme	glycosylation	723:735	arg1	sites					737:741	three predicted N-linked glycosylation sites	698:741	three predicted N-linked glycosylation sites	698:741	Unlike most PDI family members, PDIA2 contains three predicted N-linked glycosylation sites.
23167757	2	87	theme	human	288:292	arg1	family					298:303	The human PDI family	284:303	The human PDI family	284:303	The human PDI family comprises at least 19 members that differ in cell type expression, substrate specificity and post-translational modifications.
23167757	8	88	theme	major	1386:1390	arg1	class					1419:1423	major histocompatibility complex class 1	1386:1425	human major histocompatibility complex class 1 antigens (HLA-A,B,C)	1380:1446	Finally, we identified human major histocompatibility complex class 1 antigens (HLA-A,B,C) as potential binding partners of PDIA2, suggesting an involvement for PDIA2 in antigen presentation in addition to its previously described roles in autoimmunity and Parkinson's disease.
23167757	3	89	dep	function	570:577	arg1	the					566:568	the	566:568	the	566:568	PDI family A member 2 (PDIA2, previously known as PDIp) has a similar domain structure to prototypical PDI (also known as PDIA1), but the function and post-translational modifications of PDIA2 remain poorly understood.
22516225	7	0	theme	Several	1199:1205	arg1	residues					1233:1240	Several conserved phosphorylation residues	1199:1240	Several conserved phosphorylation residues	1199:1240	Several conserved phosphorylation residues and kinases that can alter the ability of occludin to regulate the integrity of TJs were identified.
22516225	10	1	theme	Yin	1800:1802	arg1	Yang					1804:1807	Yin Yang	1800:1807	the two Yin Yang sites (Ser408 and Ser490)	1792:1833	Furthermore, based on findings from this study, a potential novel interplay between phosphorylation and O-β-glycosylation at the two Yin Yang sites (Ser408 and Ser490) is also proposed.
22516225	4	2	theme	detailed	657:664	arg1	information					666:676	detailed information	657:676	detailed information of the posttranslational modifications (PTMs) of occludin	657:734	However, detailed information of the posttranslational modifications (PTMs) of occludin still remains largely unknown.
22516225	2	3	dep	attachment	277:286	arg1	the					273:275	the	273:275	the	273:275	Several host factors that facilitate the attachment and entry of HCV have been discovered, of which human occludin seems to be the most promising.
22516225	0	4	theme	occludin	97:104	arg1	phosphorylation					50:64	phosphorylation	50:64	phosphorylation	50:64	Computational identification of interplay between phosphorylation and O-β-glycosylation of human occludin as potential mechanism to impair hepatitis C virus entry.
22516225	0	4	theme	occludin	97:104	arg1	O-β-glycosylation					70:86	O-β-glycosylation	70:86	O-β-glycosylation	70:86	Computational identification of interplay between phosphorylation and O-β-glycosylation of human occludin as potential mechanism to impair hepatitis C virus entry.
22516225	6	5	dep	identify	977:984	arg1	exploited					1089:1097	exploited	1089:1097	can be exploited for the inhibition of HCV entry	1082:1129	To identify the O-β-glycosylation potential and how interplay between phosphorylation and O-β-glycosylation can be exploited for the inhibition of HCV entry, here we report a computational analysis of PTMs of human occludin.
22516225	9	6	dep	ERK	1595:1597	arg1	Ser8					1600:1603	Ser8	1600:1603	Ser8	1600:1603	To our knowledge, this is the first study to report the O-β-GlcNAc potential of occludin and target sites of ERK (Ser8, Ser310, and Thr345), GSK-3 (Ser8, Ser341) and Cdk5 (Thr376).
22516225	9	6	dep	ERK	1595:1597	arg1	Ser310					1606:1611	Ser310	1606:1611	Ser310	1606:1611	To our knowledge, this is the first study to report the O-β-GlcNAc potential of occludin and target sites of ERK (Ser8, Ser310, and Thr345), GSK-3 (Ser8, Ser341) and Cdk5 (Thr376).
22516225	9	6	dep	ERK	1595:1597	arg1	Thr345					1618:1623	Thr345	1618:1623	Thr345	1618:1623	To our knowledge, this is the first study to report the O-β-GlcNAc potential of occludin and target sites of ERK (Ser8, Ser310, and Thr345), GSK-3 (Ser8, Ser341) and Cdk5 (Thr376).
22516225	5	7	theme	unique	869:874	arg1	type					876:879	a unique type	867:879	a unique type of modification known as O-β-glycosylation	867:922	In addition to phosphorylation, serine/threonine residues of several proteins are also regulated by a unique type of modification known as O-β-glycosylation and this crosstalk serves as a functional switch.
22516225	10	8	dep	sites	1809:1813	arg1	Ser490					1827:1832	Ser490	1827:1832	Ser490	1827:1832	Furthermore, based on findings from this study, a potential novel interplay between phosphorylation and O-β-glycosylation at the two Yin Yang sites (Ser408 and Ser490) is also proposed.
22516225	10	8	dep	sites	1809:1813	arg1	Ser408					1816:1821	Ser408	1816:1821	Ser408	1816:1821	Furthermore, based on findings from this study, a potential novel interplay between phosphorylation and O-β-glycosylation at the two Yin Yang sites (Ser408 and Ser490) is also proposed.
22516225	10	8	dep	sites	1809:1813	arg1	sites					1809:1813	the two Yin Yang sites	1792:1813	the two Yin Yang sites (Ser408 and Ser490)	1792:1833	Furthermore, based on findings from this study, a potential novel interplay between phosphorylation and O-β-glycosylation at the two Yin Yang sites (Ser408 and Ser490) is also proposed.
22516225	9	9	theme	ERK	1595:1597	arg1	potential					1553:1561	the O-β-GlcNAc potential	1538:1561	the O-β-GlcNAc potential of occludin and target sites of ERK (Ser8, Ser310, and Thr345), GSK-3 (Ser8, Ser341) and Cdk5 (Thr376)	1538:1664	To our knowledge, this is the first study to report the O-β-GlcNAc potential of occludin and target sites of ERK (Ser8, Ser310, and Thr345), GSK-3 (Ser8, Ser341) and Cdk5 (Thr376).
22516225	2	10	theme	host	244:247	arg1	factors					249:255	Several host factors	236:255	Several host factors that facilitate the attachment and entry of HCV	236:303	Several host factors that facilitate the attachment and entry of HCV have been discovered, of which human occludin seems to be the most promising.
22516225	4	11	theme	occludin	727:734	arg1	PTMs					718:721	PTMs	718:721	PTMs	718:721	However, detailed information of the posttranslational modifications (PTMs) of occludin still remains largely unknown.
22516225	4	11	theme	occludin	727:734	arg1	modifications					703:715	the posttranslational modifications	681:715	the posttranslational modifications (PTMs) of occludin	681:734	However, detailed information of the posttranslational modifications (PTMs) of occludin still remains largely unknown.
22516225	8	12	theme	reported	1369:1376	arg1	residues					1382:1389	previously reported Tyr residues	1358:1389	previously reported Tyr residues	1358:1389	In addition to previously reported Tyr residues, two additional Tyr residues (Tyr29 and Tyr287) were identified as target sites of Src kinase.
22516225	0	13	theme	potential	109:117	arg1	mechanism					119:127	potential mechanism	109:127	potential mechanism	109:127	Computational identification of interplay between phosphorylation and O-β-glycosylation of human occludin as potential mechanism to impair hepatitis C virus entry.
22516225	10	14	from	sites	1809:1813	arg1	O-β-glycosylation					1771:1787	O-β-glycosylation	1771:1787	O-β-glycosylation	1771:1787	Furthermore, based on findings from this study, a potential novel interplay between phosphorylation and O-β-glycosylation at the two Yin Yang sites (Ser408 and Ser490) is also proposed.
22516225	10	14	from	sites	1809:1813	arg1	phosphorylation					1751:1765	phosphorylation	1751:1765	phosphorylation	1751:1765	Furthermore, based on findings from this study, a potential novel interplay between phosphorylation and O-β-glycosylation at the two Yin Yang sites (Ser408 and Ser490) is also proposed.
22516225	6	15	theme	occludin	1189:1196	arg1	PTMs					1175:1178	PTMs	1175:1178	PTMs of human occludin	1175:1196	To identify the O-β-glycosylation potential and how interplay between phosphorylation and O-β-glycosylation can be exploited for the inhibition of HCV entry, here we report a computational analysis of PTMs of human occludin.
22516225	1	16	theme	C	174:174	arg1	HCV					183:185	HCV	183:185	HCV	183:185	Hepatitis C virus (HCV) is one of the leading causes of liver diseases.
22516225	1	16	theme	C	174:174	arg1	virus					176:180	Hepatitis C virus	164:180	Hepatitis C virus (HCV)	164:186	Hepatitis C virus (HCV) is one of the leading causes of liver diseases.
22516225	3	17	theme	HCV	490:492	arg1	infection					494:502	HCV infection	490:502	HCV infection	490:502	Studies have shown that activity of occludin is dependent upon its phosphorylation status, and that during HCV infection deregulation of phosphorylated occludin collectively leads to a reduction in tight junction (TJ) integrity of hepatocytes and favors HCV entry.
22516225	5	18	theme	proteins	836:843	arg1	residues					816:823	serine/threonine residues	799:823	serine/threonine residues of several proteins	799:843	In addition to phosphorylation, serine/threonine residues of several proteins are also regulated by a unique type of modification known as O-β-glycosylation and this crosstalk serves as a functional switch.
22516225	5	18	theme	proteins	836:843	arg1	proteins					836:843	several proteins	828:843	several proteins	828:843	In addition to phosphorylation, serine/threonine residues of several proteins are also regulated by a unique type of modification known as O-β-glycosylation and this crosstalk serves as a functional switch.
22516225	8	19	dep	residues	1411:1418	arg1	residues					1411:1418	two additional Tyr residues	1392:1418	two additional Tyr residues (Tyr29 and Tyr287)	1392:1437	In addition to previously reported Tyr residues, two additional Tyr residues (Tyr29 and Tyr287) were identified as target sites of Src kinase.
22516225	8	19	dep	residues	1411:1418	arg1	Tyr287					1431:1436	Tyr287	1431:1436	Tyr287	1431:1436	In addition to previously reported Tyr residues, two additional Tyr residues (Tyr29 and Tyr287) were identified as target sites of Src kinase.
22516225	8	19	dep	residues	1411:1418	arg1	Tyr29					1421:1425	Tyr29	1421:1425	Tyr29	1421:1425	In addition to previously reported Tyr residues, two additional Tyr residues (Tyr29 and Tyr287) were identified as target sites of Src kinase.
22516225	5	20	theme	functional	955:964	arg1	switch					966:971	a functional switch	953:971	a functional switch	953:971	In addition to phosphorylation, serine/threonine residues of several proteins are also regulated by a unique type of modification known as O-β-glycosylation and this crosstalk serves as a functional switch.
22516225	5	20	theme	functional	955:964	arg1	crosstalk					933:941	this crosstalk	928:941	this crosstalk	928:941	In addition to phosphorylation, serine/threonine residues of several proteins are also regulated by a unique type of modification known as O-β-glycosylation and this crosstalk serves as a functional switch.
22516225	9	21	theme	first	1516:1520	arg1	this					1504:1507	this	1504:1507	this	1504:1507	To our knowledge, this is the first study to report the O-β-GlcNAc potential of occludin and target sites of ERK (Ser8, Ser310, and Thr345), GSK-3 (Ser8, Ser341) and Cdk5 (Thr376).
22516225	9	21	theme	first	1516:1520	arg1	study					1522:1526	the first study	1512:1526	the first study to report the O-β-GlcNAc potential of occludin and target sites of ERK (Ser8, Ser310, and Thr345), GSK-3 (Ser8, Ser341) and Cdk5 (Thr376)	1512:1664	To our knowledge, this is the first study to report the O-β-GlcNAc potential of occludin and target sites of ERK (Ser8, Ser310, and Thr345), GSK-3 (Ser8, Ser341) and Cdk5 (Thr376).
22516225	7	22	theme	conserved	1207:1215	arg1	residues					1233:1240	Several conserved phosphorylation residues	1199:1240	Several conserved phosphorylation residues	1199:1240	Several conserved phosphorylation residues and kinases that can alter the ability of occludin to regulate the integrity of TJs were identified.
22516225	7	23	theme	phosphorylation	1217:1231	arg1	residues					1233:1240	Several conserved phosphorylation residues	1199:1240	Several conserved phosphorylation residues	1199:1240	Several conserved phosphorylation residues and kinases that can alter the ability of occludin to regulate the integrity of TJs were identified.
22516225	2	24	theme	HCV	301:303	arg1	entry					292:296	entry	292:296	entry	292:296	Several host factors that facilitate the attachment and entry of HCV have been discovered, of which human occludin seems to be the most promising.
22516225	2	24	theme	HCV	301:303	arg1	attachment					277:286	attachment	277:286	attachment	277:286	Several host factors that facilitate the attachment and entry of HCV have been discovered, of which human occludin seems to be the most promising.
22516225	9	25	theme	sites	1586:1590	arg1	potential					1553:1561	the O-β-GlcNAc potential	1538:1561	the O-β-GlcNAc potential of occludin and target sites of ERK (Ser8, Ser310, and Thr345), GSK-3 (Ser8, Ser341) and Cdk5 (Thr376)	1538:1664	To our knowledge, this is the first study to report the O-β-GlcNAc potential of occludin and target sites of ERK (Ser8, Ser310, and Thr345), GSK-3 (Ser8, Ser341) and Cdk5 (Thr376).
22516225	0	26	theme	Computational	0:12	arg1	identification					14:27	Computational identification	0:27	Computational identification of interplay between phosphorylation and O-β-glycosylation of human occludin as potential mechanism	0:127	Computational identification of interplay between phosphorylation and O-β-glycosylation of human occludin as potential mechanism to impair hepatitis C virus entry.
22516225	6	27	theme	human	1183:1187	arg1	occludin					1189:1196	human occludin	1183:1196	human occludin	1183:1196	To identify the O-β-glycosylation potential and how interplay between phosphorylation and O-β-glycosylation can be exploited for the inhibition of HCV entry, here we report a computational analysis of PTMs of human occludin.
22516225	8	28	theme	target	1458:1463	arg1	kinase					1478:1483	Src kinase	1474:1483	Src kinase	1474:1483	In addition to previously reported Tyr residues, two additional Tyr residues (Tyr29 and Tyr287) were identified as target sites of Src kinase.
22516225	8	28	theme	target	1458:1463	arg1	residues					1411:1418	two additional Tyr residues	1392:1418	two additional Tyr residues (Tyr29 and Tyr287)	1392:1437	In addition to previously reported Tyr residues, two additional Tyr residues (Tyr29 and Tyr287) were identified as target sites of Src kinase.
22516225	8	28	theme	target	1458:1463	arg1	sites					1465:1469	target sites	1458:1469	target sites of Src kinase	1458:1483	In addition to previously reported Tyr residues, two additional Tyr residues (Tyr29 and Tyr287) were identified as target sites of Src kinase.
22516225	4	29	theme	modifications	703:715	arg1	information					666:676	detailed information	657:676	detailed information of the posttranslational modifications (PTMs) of occludin	657:734	However, detailed information of the posttranslational modifications (PTMs) of occludin still remains largely unknown.
22516225	8	30	theme	Tyr	1407:1409	arg1	kinase					1478:1483	Src kinase	1474:1483	Src kinase	1474:1483	In addition to previously reported Tyr residues, two additional Tyr residues (Tyr29 and Tyr287) were identified as target sites of Src kinase.
22516225	8	30	theme	Tyr	1407:1409	arg1	residues					1411:1418	two additional Tyr residues	1392:1418	two additional Tyr residues (Tyr29 and Tyr287)	1392:1437	In addition to previously reported Tyr residues, two additional Tyr residues (Tyr29 and Tyr287) were identified as target sites of Src kinase.
22516225	8	30	theme	Tyr	1407:1409	arg1	Tyr29					1421:1425	Tyr29	1421:1425	Tyr29	1421:1425	In addition to previously reported Tyr residues, two additional Tyr residues (Tyr29 and Tyr287) were identified as target sites of Src kinase.
22516225	8	30	theme	Tyr	1407:1409	arg1	Tyr287					1431:1436	Tyr287	1431:1436	Tyr287	1431:1436	In addition to previously reported Tyr residues, two additional Tyr residues (Tyr29 and Tyr287) were identified as target sites of Src kinase.
22516225	8	30	theme	Tyr	1407:1409	arg1	sites					1465:1469	target sites	1458:1469	target sites of Src kinase	1458:1483	In addition to previously reported Tyr residues, two additional Tyr residues (Tyr29 and Tyr287) were identified as target sites of Src kinase.
22516225	0	31	theme	interplay	32:40	arg1	identification					14:27	Computational identification	0:27	Computational identification of interplay between phosphorylation and O-β-glycosylation of human occludin as potential mechanism	0:127	Computational identification of interplay between phosphorylation and O-β-glycosylation of human occludin as potential mechanism to impair hepatitis C virus entry.
22516225	3	32	theme	tight	581:585	arg1	integrity					601:609	tight junction (TJ) integrity	581:609	tight junction (TJ) integrity of hepatocytes	581:624	Studies have shown that activity of occludin is dependent upon its phosphorylation status, and that during HCV infection deregulation of phosphorylated occludin collectively leads to a reduction in tight junction (TJ) integrity of hepatocytes and favors HCV entry.
22516225	0	33	theme	C	149:149	arg1	virus					151:155	hepatitis C virus	139:155	hepatitis C virus entry	139:161	Computational identification of interplay between phosphorylation and O-β-glycosylation of human occludin as potential mechanism to impair hepatitis C virus entry.
22516225	3	34	theme	phosphorylated	520:533	arg1	occludin					535:542	phosphorylated occludin	520:542	phosphorylated occludin	520:542	Studies have shown that activity of occludin is dependent upon its phosphorylation status, and that during HCV infection deregulation of phosphorylated occludin collectively leads to a reduction in tight junction (TJ) integrity of hepatocytes and favors HCV entry.
22516225	5	35	theme	serine/threonine	799:814	arg1	residues					816:823	serine/threonine residues	799:823	serine/threonine residues of several proteins	799:843	In addition to phosphorylation, serine/threonine residues of several proteins are also regulated by a unique type of modification known as O-β-glycosylation and this crosstalk serves as a functional switch.
22516225	5	35	theme	serine/threonine	799:814	arg1	proteins					836:843	several proteins	828:843	several proteins	828:843	In addition to phosphorylation, serine/threonine residues of several proteins are also regulated by a unique type of modification known as O-β-glycosylation and this crosstalk serves as a functional switch.
22516225	9	36	theme	target	1579:1584	arg1	sites					1586:1590	target sites	1579:1590	target sites	1579:1590	To our knowledge, this is the first study to report the O-β-GlcNAc potential of occludin and target sites of ERK (Ser8, Ser310, and Thr345), GSK-3 (Ser8, Ser341) and Cdk5 (Thr376).
22516225	0	37	theme	hepatitis	139:147	arg1	virus					151:155	hepatitis C virus	139:155	hepatitis C virus entry	139:161	Computational identification of interplay between phosphorylation and O-β-glycosylation of human occludin as potential mechanism to impair hepatitis C virus entry.
22516225	6	38	theme	PTMs	1175:1178	arg1	analysis					1163:1170	a computational analysis	1147:1170	a computational analysis of PTMs of human occludin	1147:1196	To identify the O-β-glycosylation potential and how interplay between phosphorylation and O-β-glycosylation can be exploited for the inhibition of HCV entry, here we report a computational analysis of PTMs of human occludin.
22516225	3	39	theme	occludin	535:542	arg1	deregulation					504:515	deregulation	504:515	deregulation of phosphorylated occludin	504:542	Studies have shown that activity of occludin is dependent upon its phosphorylation status, and that during HCV infection deregulation of phosphorylated occludin collectively leads to a reduction in tight junction (TJ) integrity of hepatocytes and favors HCV entry.
22516225	3	40	from	reduction	568:576	arg1	integrity					601:609	tight junction (TJ) integrity	581:609	tight junction (TJ) integrity of hepatocytes	581:624	Studies have shown that activity of occludin is dependent upon its phosphorylation status, and that during HCV infection deregulation of phosphorylated occludin collectively leads to a reduction in tight junction (TJ) integrity of hepatocytes and favors HCV entry.
22516225	10	41	from	study	1708:1712	arg1	findings					1689:1696	findings	1689:1696	findings from this study	1689:1712	Furthermore, based on findings from this study, a potential novel interplay between phosphorylation and O-β-glycosylation at the two Yin Yang sites (Ser408 and Ser490) is also proposed.
22516225	6	42	theme	entry	1125:1129	arg1	inhibition					1107:1116	the inhibition	1103:1116	the inhibition of HCV entry	1103:1129	To identify the O-β-glycosylation potential and how interplay between phosphorylation and O-β-glycosylation can be exploited for the inhibition of HCV entry, here we report a computational analysis of PTMs of human occludin.
22516225	9	43	theme	GSK-3	1627:1631	arg1	potential					1553:1561	the O-β-GlcNAc potential	1538:1561	the O-β-GlcNAc potential of occludin and target sites of ERK (Ser8, Ser310, and Thr345), GSK-3 (Ser8, Ser341) and Cdk5 (Thr376)	1538:1664	To our knowledge, this is the first study to report the O-β-GlcNAc potential of occludin and target sites of ERK (Ser8, Ser310, and Thr345), GSK-3 (Ser8, Ser341) and Cdk5 (Thr376).
22516225	3	44	theme	hepatocytes	614:624	arg1	integrity					601:609	tight junction (TJ) integrity	581:609	tight junction (TJ) integrity of hepatocytes	581:624	Studies have shown that activity of occludin is dependent upon its phosphorylation status, and that during HCV infection deregulation of phosphorylated occludin collectively leads to a reduction in tight junction (TJ) integrity of hepatocytes and favors HCV entry.
22516225	9	45	theme	O-β-GlcNAc	1542:1551	arg1	potential					1553:1561	the O-β-GlcNAc potential	1538:1561	the O-β-GlcNAc potential of occludin and target sites of ERK (Ser8, Ser310, and Thr345), GSK-3 (Ser8, Ser341) and Cdk5 (Thr376)	1538:1664	To our knowledge, this is the first study to report the O-β-GlcNAc potential of occludin and target sites of ERK (Ser8, Ser310, and Thr345), GSK-3 (Ser8, Ser341) and Cdk5 (Thr376).
22516225	7	46	theme	occludin	1284:1291	arg1	ability					1273:1279	the ability	1269:1279	the ability of occludin to regulate the integrity of TJs	1269:1324	Several conserved phosphorylation residues and kinases that can alter the ability of occludin to regulate the integrity of TJs were identified.
22516225	7	47	theme	TJs	1322:1324	arg1	integrity					1309:1317	the integrity	1305:1317	the integrity of TJs	1305:1324	Several conserved phosphorylation residues and kinases that can alter the ability of occludin to regulate the integrity of TJs were identified.
22516225	0	48	theme	virus	151:155	arg1	entry					157:161	hepatitis C virus entry	139:161	hepatitis C virus entry	139:161	Computational identification of interplay between phosphorylation and O-β-glycosylation of human occludin as potential mechanism to impair hepatitis C virus entry.
22516225	10	49	theme	novel	1727:1731	arg1	interplay					1733:1741	a potential novel interplay	1715:1741	a potential novel interplay between phosphorylation and O-β-glycosylation at the two Yin Yang sites (Ser408 and Ser490)	1715:1833	Furthermore, based on findings from this study, a potential novel interplay between phosphorylation and O-β-glycosylation at the two Yin Yang sites (Ser408 and Ser490) is also proposed.
22516225	6	50	theme	O-β-glycosylation	990:1006	arg1	potential					1008:1016	the O-β-glycosylation potential	986:1016	the O-β-glycosylation potential	986:1016	To identify the O-β-glycosylation potential and how interplay between phosphorylation and O-β-glycosylation can be exploited for the inhibition of HCV entry, here we report a computational analysis of PTMs of human occludin.
22516225	5	51	theme	several	828:834	arg1	proteins					836:843	several proteins	828:843	several proteins	828:843	In addition to phosphorylation, serine/threonine residues of several proteins are also regulated by a unique type of modification known as O-β-glycosylation and this crosstalk serves as a functional switch.
22516225	1	52	theme	leading	202:208	arg1	causes					210:215	the leading causes	198:215	the leading causes of liver diseases	198:233	Hepatitis C virus (HCV) is one of the leading causes of liver diseases.
22516225	10	53	theme	potential	1717:1725	arg1	interplay					1733:1741	a potential novel interplay	1715:1741	a potential novel interplay between phosphorylation and O-β-glycosylation at the two Yin Yang sites (Ser408 and Ser490)	1715:1833	Furthermore, based on findings from this study, a potential novel interplay between phosphorylation and O-β-glycosylation at the two Yin Yang sites (Ser408 and Ser490) is also proposed.
22516225	8	54	theme	additional	1396:1405	arg1	kinase					1478:1483	Src kinase	1474:1483	Src kinase	1474:1483	In addition to previously reported Tyr residues, two additional Tyr residues (Tyr29 and Tyr287) were identified as target sites of Src kinase.
22516225	8	54	theme	additional	1396:1405	arg1	residues					1411:1418	two additional Tyr residues	1392:1418	two additional Tyr residues (Tyr29 and Tyr287)	1392:1437	In addition to previously reported Tyr residues, two additional Tyr residues (Tyr29 and Tyr287) were identified as target sites of Src kinase.
22516225	8	54	theme	additional	1396:1405	arg1	Tyr29					1421:1425	Tyr29	1421:1425	Tyr29	1421:1425	In addition to previously reported Tyr residues, two additional Tyr residues (Tyr29 and Tyr287) were identified as target sites of Src kinase.
22516225	8	54	theme	additional	1396:1405	arg1	Tyr287					1431:1436	Tyr287	1431:1436	Tyr287	1431:1436	In addition to previously reported Tyr residues, two additional Tyr residues (Tyr29 and Tyr287) were identified as target sites of Src kinase.
22516225	8	54	theme	additional	1396:1405	arg1	sites					1465:1469	target sites	1458:1469	target sites of Src kinase	1458:1483	In addition to previously reported Tyr residues, two additional Tyr residues (Tyr29 and Tyr287) were identified as target sites of Src kinase.
22516225	3	55	theme	phosphorylation	450:464	arg1	status					466:471	its phosphorylation status	446:471	its phosphorylation status	446:471	Studies have shown that activity of occludin is dependent upon its phosphorylation status, and that during HCV infection deregulation of phosphorylated occludin collectively leads to a reduction in tight junction (TJ) integrity of hepatocytes and favors HCV entry.
22516225	8	56	theme	kinase	1478:1483	arg1	kinase					1478:1483	Src kinase	1474:1483	Src kinase	1474:1483	In addition to previously reported Tyr residues, two additional Tyr residues (Tyr29 and Tyr287) were identified as target sites of Src kinase.
22516225	8	56	theme	kinase	1478:1483	arg1	residues					1411:1418	two additional Tyr residues	1392:1418	two additional Tyr residues (Tyr29 and Tyr287)	1392:1437	In addition to previously reported Tyr residues, two additional Tyr residues (Tyr29 and Tyr287) were identified as target sites of Src kinase.
22516225	8	56	theme	kinase	1478:1483	arg1	sites					1465:1469	target sites	1458:1469	target sites of Src kinase	1458:1483	In addition to previously reported Tyr residues, two additional Tyr residues (Tyr29 and Tyr287) were identified as target sites of Src kinase.
22516225	10	57	theme	Yang	1804:1807	arg1	Ser490					1827:1832	Ser490	1827:1832	Ser490	1827:1832	Furthermore, based on findings from this study, a potential novel interplay between phosphorylation and O-β-glycosylation at the two Yin Yang sites (Ser408 and Ser490) is also proposed.
22516225	10	57	theme	Yang	1804:1807	arg1	Ser408					1816:1821	Ser408	1816:1821	Ser408	1816:1821	Furthermore, based on findings from this study, a potential novel interplay between phosphorylation and O-β-glycosylation at the two Yin Yang sites (Ser408 and Ser490) is also proposed.
22516225	10	57	theme	Yang	1804:1807	arg1	sites					1809:1813	the two Yin Yang sites	1792:1813	the two Yin Yang sites (Ser408 and Ser490)	1792:1833	Furthermore, based on findings from this study, a potential novel interplay between phosphorylation and O-β-glycosylation at the two Yin Yang sites (Ser408 and Ser490) is also proposed.
22516225	3	58	theme	HCV	637:639	arg1	entry					641:645	HCV entry	637:645	HCV entry	637:645	Studies have shown that activity of occludin is dependent upon its phosphorylation status, and that during HCV infection deregulation of phosphorylated occludin collectively leads to a reduction in tight junction (TJ) integrity of hepatocytes and favors HCV entry.
22516225	9	59	theme	occludin	1566:1573	arg1	potential					1553:1561	the O-β-GlcNAc potential	1538:1561	the O-β-GlcNAc potential of occludin and target sites of ERK (Ser8, Ser310, and Thr345), GSK-3 (Ser8, Ser341) and Cdk5 (Thr376)	1538:1664	To our knowledge, this is the first study to report the O-β-GlcNAc potential of occludin and target sites of ERK (Ser8, Ser310, and Thr345), GSK-3 (Ser8, Ser341) and Cdk5 (Thr376).
22516225	5	60	theme	modification	884:895	arg1	type					876:879	a unique type	867:879	a unique type of modification known as O-β-glycosylation	867:922	In addition to phosphorylation, serine/threonine residues of several proteins are also regulated by a unique type of modification known as O-β-glycosylation and this crosstalk serves as a functional switch.
22516225	3	61	theme	junction	587:594	arg1	integrity					601:609	tight junction (TJ) integrity	581:609	tight junction (TJ) integrity of hepatocytes	581:624	Studies have shown that activity of occludin is dependent upon its phosphorylation status, and that during HCV infection deregulation of phosphorylated occludin collectively leads to a reduction in tight junction (TJ) integrity of hepatocytes and favors HCV entry.
22516225	4	62	theme	posttranslational	685:701	arg1	PTMs					718:721	PTMs	718:721	PTMs	718:721	However, detailed information of the posttranslational modifications (PTMs) of occludin still remains largely unknown.
22516225	4	62	theme	posttranslational	685:701	arg1	modifications					703:715	the posttranslational modifications	681:715	the posttranslational modifications (PTMs) of occludin	681:734	However, detailed information of the posttranslational modifications (PTMs) of occludin still remains largely unknown.
22516225	8	63	theme	Tyr	1378:1380	arg1	residues					1382:1389	previously reported Tyr residues	1358:1389	previously reported Tyr residues	1358:1389	In addition to previously reported Tyr residues, two additional Tyr residues (Tyr29 and Tyr287) were identified as target sites of Src kinase.
22516225	1	64	theme	causes	210:215	arg1	causes					210:215	the leading causes	198:215	the leading causes of liver diseases	198:233	Hepatitis C virus (HCV) is one of the leading causes of liver diseases.
22516225	1	64	theme	causes	210:215	arg1	one					191:193	one	191:193	one	191:193	Hepatitis C virus (HCV) is one of the leading causes of liver diseases.
22516225	6	65	theme	computational	1149:1161	arg1	analysis					1163:1170	a computational analysis	1147:1170	a computational analysis of PTMs of human occludin	1147:1196	To identify the O-β-glycosylation potential and how interplay between phosphorylation and O-β-glycosylation can be exploited for the inhibition of HCV entry, here we report a computational analysis of PTMs of human occludin.
22516225	3	66	theme	TJ	597:598	arg1	integrity					601:609	tight junction (TJ) integrity	581:609	tight junction (TJ) integrity of hepatocytes	581:624	Studies have shown that activity of occludin is dependent upon its phosphorylation status, and that during HCV infection deregulation of phosphorylated occludin collectively leads to a reduction in tight junction (TJ) integrity of hepatocytes and favors HCV entry.
22516225	1	67	theme	Hepatitis	164:172	arg1	HCV					183:185	HCV	183:185	HCV	183:185	Hepatitis C virus (HCV) is one of the leading causes of liver diseases.
22516225	1	67	theme	Hepatitis	164:172	arg1	virus					176:180	Hepatitis C virus	164:180	Hepatitis C virus (HCV)	164:186	Hepatitis C virus (HCV) is one of the leading causes of liver diseases.
22516225	6	68	theme	HCV	1121:1123	arg1	entry					1125:1129	HCV entry	1121:1129	HCV entry	1121:1129	To identify the O-β-glycosylation potential and how interplay between phosphorylation and O-β-glycosylation can be exploited for the inhibition of HCV entry, here we report a computational analysis of PTMs of human occludin.
22516225	0	69	theme	human	91:95	arg1	occludin					97:104	human occludin	91:104	human occludin	91:104	Computational identification of interplay between phosphorylation and O-β-glycosylation of human occludin as potential mechanism to impair hepatitis C virus entry.
22516225	3	70	theme	occludin	419:426	arg1	activity					407:414	activity	407:414	activity of occludin	407:426	Studies have shown that activity of occludin is dependent upon its phosphorylation status, and that during HCV infection deregulation of phosphorylated occludin collectively leads to a reduction in tight junction (TJ) integrity of hepatocytes and favors HCV entry.
22516225	2	71	theme	Several	236:242	arg1	factors					249:255	Several host factors	236:255	Several host factors that facilitate the attachment and entry of HCV	236:303	Several host factors that facilitate the attachment and entry of HCV have been discovered, of which human occludin seems to be the most promising.
22516225	1	72	theme	liver	220:224	arg1	diseases					226:233	liver diseases	220:233	liver diseases	220:233	Hepatitis C virus (HCV) is one of the leading causes of liver diseases.
22516225	9	73	theme	Cdk5	1652:1655	arg1	potential					1553:1561	the O-β-GlcNAc potential	1538:1561	the O-β-GlcNAc potential of occludin and target sites of ERK (Ser8, Ser310, and Thr345), GSK-3 (Ser8, Ser341) and Cdk5 (Thr376)	1538:1664	To our knowledge, this is the first study to report the O-β-GlcNAc potential of occludin and target sites of ERK (Ser8, Ser310, and Thr345), GSK-3 (Ser8, Ser341) and Cdk5 (Thr376).
22516225	8	74	theme	Src	1474:1476	arg1	kinase					1478:1483	Src kinase	1474:1483	Src kinase	1474:1483	In addition to previously reported Tyr residues, two additional Tyr residues (Tyr29 and Tyr287) were identified as target sites of Src kinase.
22516225	0	75	gly	O-β-glycosylation	70:86	arg1	occludin					97:104	human occludin	91:104	human occludin	91:104	Computational identification of interplay between phosphorylation and O-β-glycosylation of human occludin as potential mechanism to impair hepatitis C virus entry.
22516225	2	76	theme	human	336:340	arg1	promising					372:380	promising	372:380	promising	372:380	Several host factors that facilitate the attachment and entry of HCV have been discovered, of which human occludin seems to be the most promising.
22516225	2	76	theme	human	336:340	arg1	occludin					342:349	human occludin	336:349	human occludin	336:349	Several host factors that facilitate the attachment and entry of HCV have been discovered, of which human occludin seems to be the most promising.
22516225	10	77	gly	O-β-glycosylation	1771:1787	arg1	Ser408					1816:1821	Ser408	1816:1821	Ser408	1816:1821	Furthermore, based on findings from this study, a potential novel interplay between phosphorylation and O-β-glycosylation at the two Yin Yang sites (Ser408 and Ser490) is also proposed.
22516225	10	77	gly	O-β-glycosylation	1771:1787	arg2	Ser490					1827:1832	Ser490	1827:1832	Ser490	1827:1832	Furthermore, based on findings from this study, a potential novel interplay between phosphorylation and O-β-glycosylation at the two Yin Yang sites (Ser408 and Ser490) is also proposed.
22516225	10	77	gly	O-β-glycosylation	1771:1787	arg2	sites					1809:1813	the two Yin Yang sites	1792:1813	the two Yin Yang sites (Ser408 and Ser490)	1792:1833	Furthermore, based on findings from this study, a potential novel interplay between phosphorylation and O-β-glycosylation at the two Yin Yang sites (Ser408 and Ser490) is also proposed.
22516225	10	77	gly	O-β-glycosylation	1771:1787	arg1	Ser490					1827:1832	Ser490	1827:1832	Ser490	1827:1832	Furthermore, based on findings from this study, a potential novel interplay between phosphorylation and O-β-glycosylation at the two Yin Yang sites (Ser408 and Ser490) is also proposed.
22516225	10	77	gly	O-β-glycosylation	1771:1787	arg2	Ser408					1816:1821	Ser408	1816:1821	Ser408	1816:1821	Furthermore, based on findings from this study, a potential novel interplay between phosphorylation and O-β-glycosylation at the two Yin Yang sites (Ser408 and Ser490) is also proposed.
22516225	10	77	gly	O-β-glycosylation	1771:1787	arg1	sites					1809:1813	the two Yin Yang sites	1792:1813	the two Yin Yang sites (Ser408 and Ser490)	1792:1833	Furthermore, based on findings from this study, a potential novel interplay between phosphorylation and O-β-glycosylation at the two Yin Yang sites (Ser408 and Ser490) is also proposed.
22516225	1	78	theme	diseases	226:233	arg1	causes					210:215	the leading causes	198:215	the leading causes of liver diseases	198:233	Hepatitis C virus (HCV) is one of the leading causes of liver diseases.
20563614	13	0	theme	synaptic	1841:1848	arg1	expression					1867:1876	synaptic specific protein expression	1841:1876	synaptic specific protein expression including Synapsin II	1841:1898	Using iTRAQ, abnormal synaptic expression levels of several proteins previously implicated in AD pathology were observed in addition to novel changes in synaptic specific protein expression including Synapsin II.
20563614	9	1	theme	phosphorylation	1176:1190	arg1	implication					1233:1243	possible implication	1224:1243	possible implication of those sites in synaptic plasticity in normal versus AD states	1224:1308	The potential interplay of phosphorylation with mapped O-GlcNAc sites, and possible implication of those sites in synaptic plasticity in normal versus AD states is discussed.
20563614	9	1	theme	phosphorylation	1176:1190	arg1	interplay					1163:1171	The potential interplay	1149:1171	The potential interplay of phosphorylation with mapped O-GlcNAc sites	1149:1217	The potential interplay of phosphorylation with mapped O-GlcNAc sites, and possible implication of those sites in synaptic plasticity in normal versus AD states is discussed.
20563614	10	2	theme	isotopic	1357:1364	arg1	approach					1379:1386	a powerful differential isotopic quantitative approach	1333:1386	a powerful differential isotopic quantitative approach in proteomics	1333:1400	iTRAQ is a powerful differential isotopic quantitative approach in proteomics.
20563614	10	2	theme	isotopic	1357:1364	arg1	iTRAQ					1324:1328	iTRAQ	1324:1328	iTRAQ	1324:1328	iTRAQ is a powerful differential isotopic quantitative approach in proteomics.
20563614	4	3	theme	lectin	587:592	arg1	enrichment					594:603	lectin enrichment	587:603	lectin enrichment	587:603	Using lectin enrichment and mass spectrometry, we mapped several human cortical synaptic O-GlcNAc modification sites.
20563614	11	4	theme	ion	1537:1539	arg1	spectrometry					1551:1562	ion trap mass spectrometry	1537:1562	ion trap mass spectrometry	1537:1562	Pulsed Q dissociation (PQD) is a recently introduced fragmentation strategy that enables detection of low mass iTRAQ reporter ions in ion trap mass spectrometry.
20563614	9	5	from	implication	1233:1243	arg1	plasticity					1272:1281	synaptic plasticity	1263:1281	synaptic plasticity in normal versus AD states	1263:1308	The potential interplay of phosphorylation with mapped O-GlcNAc sites, and possible implication of those sites in synaptic plasticity in normal versus AD states is discussed.
20563614	4	6	theme	cortical	652:659	arg1	sites					692:696	several human cortical synaptic O-GlcNAc modification sites	638:696	several human cortical synaptic O-GlcNAc modification sites	638:696	Using lectin enrichment and mass spectrometry, we mapped several human cortical synaptic O-GlcNAc modification sites.
20563614	1	7	attach	linked	164:169	arg1	learning					183:190	impaired learning	174:190	impaired learning	174:190	Neuronal synaptic functional deficits are linked to impaired learning and memory in Alzheimer's disease (AD).
20563614	1	7	attach	linked	164:169	arg2	deficits					151:158	Neuronal synaptic functional deficits	122:158	Neuronal synaptic functional deficits	122:158	Neuronal synaptic functional deficits are linked to impaired learning and memory in Alzheimer's disease (AD).
20563614	1	7	attach	linked	164:169	arg1	memory					196:201	memory	196:201	memory	196:201	Neuronal synaptic functional deficits are linked to impaired learning and memory in Alzheimer's disease (AD).
20563614	0	8	theme	Human	0:4	arg1	disease					18:24	Human Alzheimer's disease	0:24	Human Alzheimer's disease	0:24	Human Alzheimer's disease synaptic O-GlcNAc site mapping and iTRAQ expression proteomics with ion trap mass spectrometry.
20563614	1	9	theme	impaired	174:181	arg1	learning					183:190	impaired learning	174:190	impaired learning	174:190	Neuronal synaptic functional deficits are linked to impaired learning and memory in Alzheimer's disease (AD).
20563614	4	10	theme	O-GlcNAc	670:677	arg1	sites					692:696	several human cortical synaptic O-GlcNAc modification sites	638:696	several human cortical synaptic O-GlcNAc modification sites	638:696	Using lectin enrichment and mass spectrometry, we mapped several human cortical synaptic O-GlcNAc modification sites.
20563614	13	11	theme	AD	1782:1783	arg1	pathology					1785:1793	AD pathology	1782:1793	AD pathology	1782:1793	Using iTRAQ, abnormal synaptic expression levels of several proteins previously implicated in AD pathology were observed in addition to novel changes in synaptic specific protein expression including Synapsin II.
20563614	13	12	theme	novel	1824:1828	arg1	changes					1830:1836	novel changes	1824:1836	novel changes in synaptic specific protein expression including Synapsin II	1824:1898	Using iTRAQ, abnormal synaptic expression levels of several proteins previously implicated in AD pathology were observed in addition to novel changes in synaptic specific protein expression including Synapsin II.
20563614	3	13	theme	synaptic	560:567	arg1	plasticity					569:578	synaptic plasticity	560:578	synaptic plasticity	560:578	Reduced levels of O-GlcNAc have been observed in AD, suggesting a possible link to deficits in synaptic plasticity.
20563614	12	14	theme	PQD-based	1604:1612	arg1	quantitation					1620:1631	PQD-based iTRAQ quantitation	1604:1631	PQD-based iTRAQ quantitation	1604:1631	We optimized LTQ ion trap settings for PQD-based iTRAQ quantitation and demonstrated its utility in O-GlcNAc site mapping.
20563614	11	15	theme	mass	1546:1549	arg1	spectrometry					1551:1562	ion trap mass spectrometry	1537:1562	ion trap mass spectrometry	1537:1562	Pulsed Q dissociation (PQD) is a recently introduced fragmentation strategy that enables detection of low mass iTRAQ reporter ions in ion trap mass spectrometry.
20563614	7	16	theme	synaptic	1067:1074	arg1	plasticity					1076:1085	synaptic plasticity	1067:1085	synaptic plasticity	1067:1085	Mek2 is a signaling component of the Erk 1/2 pathway involved in synaptic plasticity.
20563614	2	17	theme	novel	274:278	arg1	modification					334:345	a novel cytosolic and nuclear carbohydrate post-translational modification	272:345	a novel cytosolic and nuclear carbohydrate post-translational modification	272:345	We recently demonstrated that O-GlcNAc, a novel cytosolic and nuclear carbohydrate post-translational modification, is enriched at neuronal synapses and positively regulates synaptic plasticity linked to learning and memory in mice.
20563614	2	17	theme	novel	274:278	arg1	O-GlcNAc					262:269	O-GlcNAc	262:269	O-GlcNAc	262:269	We recently demonstrated that O-GlcNAc, a novel cytosolic and nuclear carbohydrate post-translational modification, is enriched at neuronal synapses and positively regulates synaptic plasticity linked to learning and memory in mice.
20563614	4	18	theme	several	638:644	arg1	sites					692:696	several human cortical synaptic O-GlcNAc modification sites	638:696	several human cortical synaptic O-GlcNAc modification sites	638:696	Using lectin enrichment and mass spectrometry, we mapped several human cortical synaptic O-GlcNAc modification sites.
20563614	13	19	theme	proteins	1748:1755	arg1	levels					1730:1735	abnormal synaptic expression levels	1701:1735	abnormal synaptic expression levels of several proteins previously implicated in AD pathology	1701:1793	Using iTRAQ, abnormal synaptic expression levels of several proteins previously implicated in AD pathology were observed in addition to novel changes in synaptic specific protein expression including Synapsin II.
20563614	5	20	theme	O-GlcNAcation	722:734	arg1	patterns					710:717	patterns	710:717	patterns of O-GlcNAcation	710:734	Overlap in patterns of O-GlcNAcation between mouse and human appears to be high, as previously mapped mouse synaptic O-GlcNAc sites in Bassoon, Piccolo, and tubulin polymerization promoting protein p25 were identified in human.
20563614	7	21	theme	signaling	1012:1020	arg1	Mek2					1002:1005	Mek2	1002:1005	Mek2	1002:1005	Mek2 is a signaling component of the Erk 1/2 pathway involved in synaptic plasticity.
20563614	7	21	theme	signaling	1012:1020	arg1	component					1022:1030	a signaling component	1010:1030	a signaling component of the Erk 1/2 pathway involved in synaptic plasticity	1010:1085	Mek2 is a signaling component of the Erk 1/2 pathway involved in synaptic plasticity.
20563614	6	22	theme	modification	942:953	arg1	sites					955:959	Novel O-GlcNAc modification sites	927:959	Novel O-GlcNAc modification sites	927:959	Novel O-GlcNAc modification sites were identified on Mek2 and RPN13/ADRM1.
20563614	1	23	from	memory	196:201	arg1	AD					227:228	AD	227:228	AD	227:228	Neuronal synaptic functional deficits are linked to impaired learning and memory in Alzheimer's disease (AD).
20563614	1	23	from	memory	196:201	arg1	disease					218:224	Alzheimer's disease	206:224	Alzheimer's disease (AD)	206:229	Neuronal synaptic functional deficits are linked to impaired learning and memory in Alzheimer's disease (AD).
20563614	6	24	theme	Novel	927:931	arg1	sites					955:959	Novel O-GlcNAc modification sites	927:959	Novel O-GlcNAc modification sites	927:959	Novel O-GlcNAc modification sites were identified on Mek2 and RPN13/ADRM1.
20563614	11	25	theme	mass	1509:1512	arg1	ions					1529:1532	low mass iTRAQ reporter ions	1505:1532	low mass iTRAQ reporter ions in ion trap mass spectrometry	1505:1562	Pulsed Q dissociation (PQD) is a recently introduced fragmentation strategy that enables detection of low mass iTRAQ reporter ions in ion trap mass spectrometry.
20563614	1	26	from	learning	183:190	arg1	AD					227:228	AD	227:228	AD	227:228	Neuronal synaptic functional deficits are linked to impaired learning and memory in Alzheimer's disease (AD).
20563614	1	26	from	learning	183:190	arg1	disease					218:224	Alzheimer's disease	206:224	Alzheimer's disease (AD)	206:229	Neuronal synaptic functional deficits are linked to impaired learning and memory in Alzheimer's disease (AD).
20563614	1	27	theme	synaptic	131:138	arg1	deficits					151:158	Neuronal synaptic functional deficits	122:158	Neuronal synaptic functional deficits	122:158	Neuronal synaptic functional deficits are linked to impaired learning and memory in Alzheimer's disease (AD).
20563614	3	28	from	deficits	548:555	arg1	plasticity					569:578	synaptic plasticity	560:578	synaptic plasticity	560:578	Reduced levels of O-GlcNAc have been observed in AD, suggesting a possible link to deficits in synaptic plasticity.
20563614	5	29	theme	protein	889:895	arg1	p25					897:899	protein p25	889:899	protein p25	889:899	Overlap in patterns of O-GlcNAcation between mouse and human appears to be high, as previously mapped mouse synaptic O-GlcNAc sites in Bassoon, Piccolo, and tubulin polymerization promoting protein p25 were identified in human.
20563614	2	30	from	learning	436:443	arg1	mice					459:462	mice	459:462	mice	459:462	We recently demonstrated that O-GlcNAc, a novel cytosolic and nuclear carbohydrate post-translational modification, is enriched at neuronal synapses and positively regulates synaptic plasticity linked to learning and memory in mice.
20563614	13	31	theme	synaptic	1710:1717	arg1	levels					1730:1735	abnormal synaptic expression levels	1701:1735	abnormal synaptic expression levels of several proteins previously implicated in AD pathology	1701:1793	Using iTRAQ, abnormal synaptic expression levels of several proteins previously implicated in AD pathology were observed in addition to novel changes in synaptic specific protein expression including Synapsin II.
20563614	0	32	theme	expression	67:76	arg1	proteomics					78:87	O-GlcNAc site mapping and iTRAQ expression proteomics	35:87	proteomics	78:87	Human Alzheimer's disease synaptic O-GlcNAc site mapping and iTRAQ expression proteomics with ion trap mass spectrometry.
20563614	11	33	from	spectrometry	1551:1562	arg1	detection					1492:1500	detection	1492:1500	detection of low mass iTRAQ reporter ions in ion trap mass spectrometry	1492:1562	Pulsed Q dissociation (PQD) is a recently introduced fragmentation strategy that enables detection of low mass iTRAQ reporter ions in ion trap mass spectrometry.
20563614	2	34	from	memory	449:454	arg1	mice					459:462	mice	459:462	mice	459:462	We recently demonstrated that O-GlcNAc, a novel cytosolic and nuclear carbohydrate post-translational modification, is enriched at neuronal synapses and positively regulates synaptic plasticity linked to learning and memory in mice.
20563614	9	35	theme	mapped	1197:1202	arg1	sites					1213:1217	mapped O-GlcNAc sites	1197:1217	mapped O-GlcNAc sites	1197:1217	The potential interplay of phosphorylation with mapped O-GlcNAc sites, and possible implication of those sites in synaptic plasticity in normal versus AD states is discussed.
20563614	11	36	theme	reporter	1520:1527	arg1	ions					1529:1532	low mass iTRAQ reporter ions	1505:1532	low mass iTRAQ reporter ions in ion trap mass spectrometry	1505:1562	Pulsed Q dissociation (PQD) is a recently introduced fragmentation strategy that enables detection of low mass iTRAQ reporter ions in ion trap mass spectrometry.
20563614	9	37	with	implication	1233:1243	arg1	sites					1213:1217	mapped O-GlcNAc sites	1197:1217	mapped O-GlcNAc sites	1197:1217	The potential interplay of phosphorylation with mapped O-GlcNAc sites, and possible implication of those sites in synaptic plasticity in normal versus AD states is discussed.
20563614	12	38	theme	site	1674:1677	arg1	mapping					1679:1685	O-GlcNAc site mapping	1665:1685	O-GlcNAc site mapping	1665:1685	We optimized LTQ ion trap settings for PQD-based iTRAQ quantitation and demonstrated its utility in O-GlcNAc site mapping.
20563614	11	39	theme	introduced	1445:1454	arg1	strategy					1470:1477	a recently introduced fragmentation strategy	1434:1477	a recently introduced fragmentation strategy that enables detection of low mass iTRAQ reporter ions in ion trap mass spectrometry	1434:1562	Pulsed Q dissociation (PQD) is a recently introduced fragmentation strategy that enables detection of low mass iTRAQ reporter ions in ion trap mass spectrometry.
20563614	11	39	theme	introduced	1445:1454	arg1	dissociation					1412:1423	Pulsed Q dissociation	1403:1423	Pulsed Q dissociation (PQD)	1403:1429	Pulsed Q dissociation (PQD) is a recently introduced fragmentation strategy that enables detection of low mass iTRAQ reporter ions in ion trap mass spectrometry.
20563614	0	40	theme	trap	98:101	arg1	spectrometry					108:119	ion trap mass spectrometry	94:119	ion trap mass spectrometry	94:119	Human Alzheimer's disease synaptic O-GlcNAc site mapping and iTRAQ expression proteomics with ion trap mass spectrometry.
20563614	5	41	theme	synaptic	807:814	arg1	sites					825:829	previously mapped mouse synaptic O-GlcNAc sites	783:829	previously mapped mouse synaptic O-GlcNAc sites in Bassoon, Piccolo, and tubulin polymerization promoting protein p25	783:899	Overlap in patterns of O-GlcNAcation between mouse and human appears to be high, as previously mapped mouse synaptic O-GlcNAc sites in Bassoon, Piccolo, and tubulin polymerization promoting protein p25 were identified in human.
20563614	9	42	theme	O-GlcNAc	1204:1211	arg1	sites					1213:1217	mapped O-GlcNAc sites	1197:1217	mapped O-GlcNAc sites	1197:1217	The potential interplay of phosphorylation with mapped O-GlcNAc sites, and possible implication of those sites in synaptic plasticity in normal versus AD states is discussed.
20563614	13	43	theme	protein	1859:1865	arg1	expression					1867:1876	synaptic specific protein expression	1841:1876	synaptic specific protein expression including Synapsin II	1841:1898	Using iTRAQ, abnormal synaptic expression levels of several proteins previously implicated in AD pathology were observed in addition to novel changes in synaptic specific protein expression including Synapsin II.
20563614	3	44	theme	Reduced	465:471	arg1	levels					473:478	Reduced levels	465:478	Reduced levels of O-GlcNAc	465:490	Reduced levels of O-GlcNAc have been observed in AD, suggesting a possible link to deficits in synaptic plasticity.
20563614	2	45	attach	linked	426:431	arg1	memory					449:454	memory	449:454	memory	449:454	We recently demonstrated that O-GlcNAc, a novel cytosolic and nuclear carbohydrate post-translational modification, is enriched at neuronal synapses and positively regulates synaptic plasticity linked to learning and memory in mice.
20563614	2	45	attach	linked	426:431	arg2	plasticity					415:424	synaptic plasticity	406:424	synaptic plasticity linked to learning and memory in mice	406:462	We recently demonstrated that O-GlcNAc, a novel cytosolic and nuclear carbohydrate post-translational modification, is enriched at neuronal synapses and positively regulates synaptic plasticity linked to learning and memory in mice.
20563614	2	45	attach	linked	426:431	arg1	learning					436:443	learning	436:443	learning	436:443	We recently demonstrated that O-GlcNAc, a novel cytosolic and nuclear carbohydrate post-translational modification, is enriched at neuronal synapses and positively regulates synaptic plasticity linked to learning and memory in mice.
20563614	9	46	from	interplay	1163:1171	arg1	plasticity					1272:1281	synaptic plasticity	1263:1281	synaptic plasticity in normal versus AD states	1263:1308	The potential interplay of phosphorylation with mapped O-GlcNAc sites, and possible implication of those sites in synaptic plasticity in normal versus AD states is discussed.
20563614	10	47	from	approach	1379:1386	arg1	proteomics					1391:1400	proteomics	1391:1400	proteomics	1391:1400	iTRAQ is a powerful differential isotopic quantitative approach in proteomics.
20563614	10	48	theme	powerful	1335:1342	arg1	approach					1379:1386	a powerful differential isotopic quantitative approach	1333:1386	a powerful differential isotopic quantitative approach in proteomics	1333:1400	iTRAQ is a powerful differential isotopic quantitative approach in proteomics.
20563614	10	48	theme	powerful	1335:1342	arg1	iTRAQ					1324:1328	iTRAQ	1324:1328	iTRAQ	1324:1328	iTRAQ is a powerful differential isotopic quantitative approach in proteomics.
20563614	5	49	theme	mapped	794:799	arg1	sites					825:829	previously mapped mouse synaptic O-GlcNAc sites	783:829	previously mapped mouse synaptic O-GlcNAc sites in Bassoon, Piccolo, and tubulin polymerization promoting protein p25	783:899	Overlap in patterns of O-GlcNAcation between mouse and human appears to be high, as previously mapped mouse synaptic O-GlcNAc sites in Bassoon, Piccolo, and tubulin polymerization promoting protein p25 were identified in human.
20563614	2	50	theme	post-translational	315:332	arg1	modification					334:345	a novel cytosolic and nuclear carbohydrate post-translational modification	272:345	a novel cytosolic and nuclear carbohydrate post-translational modification	272:345	We recently demonstrated that O-GlcNAc, a novel cytosolic and nuclear carbohydrate post-translational modification, is enriched at neuronal synapses and positively regulates synaptic plasticity linked to learning and memory in mice.
20563614	2	50	theme	post-translational	315:332	arg1	O-GlcNAc					262:269	O-GlcNAc	262:269	O-GlcNAc	262:269	We recently demonstrated that O-GlcNAc, a novel cytosolic and nuclear carbohydrate post-translational modification, is enriched at neuronal synapses and positively regulates synaptic plasticity linked to learning and memory in mice.
20563614	9	51	with	interplay	1163:1171	arg1	sites					1213:1217	mapped O-GlcNAc sites	1197:1217	mapped O-GlcNAc sites	1197:1217	The potential interplay of phosphorylation with mapped O-GlcNAc sites, and possible implication of those sites in synaptic plasticity in normal versus AD states is discussed.
20563614	11	52	theme	Pulsed	1403:1408	arg1	strategy					1470:1477	a recently introduced fragmentation strategy	1434:1477	a recently introduced fragmentation strategy that enables detection of low mass iTRAQ reporter ions in ion trap mass spectrometry	1434:1562	Pulsed Q dissociation (PQD) is a recently introduced fragmentation strategy that enables detection of low mass iTRAQ reporter ions in ion trap mass spectrometry.
20563614	11	52	theme	Pulsed	1403:1408	arg1	PQD					1426:1428	PQD	1426:1428	PQD	1426:1428	Pulsed Q dissociation (PQD) is a recently introduced fragmentation strategy that enables detection of low mass iTRAQ reporter ions in ion trap mass spectrometry.
20563614	11	52	theme	Pulsed	1403:1408	arg1	dissociation					1412:1423	Pulsed Q dissociation	1403:1423	Pulsed Q dissociation (PQD)	1403:1429	Pulsed Q dissociation (PQD) is a recently introduced fragmentation strategy that enables detection of low mass iTRAQ reporter ions in ion trap mass spectrometry.
20563614	9	53	theme	potential	1153:1161	arg1	interplay					1163:1171	The potential interplay	1149:1171	The potential interplay of phosphorylation with mapped O-GlcNAc sites	1149:1217	The potential interplay of phosphorylation with mapped O-GlcNAc sites, and possible implication of those sites in synaptic plasticity in normal versus AD states is discussed.
20563614	2	54	theme	neuronal	363:370	arg1	synapses					372:379	neuronal synapses	363:379	neuronal synapses	363:379	We recently demonstrated that O-GlcNAc, a novel cytosolic and nuclear carbohydrate post-translational modification, is enriched at neuronal synapses and positively regulates synaptic plasticity linked to learning and memory in mice.
20563614	8	55	theme	proteasomal	1116:1126	arg1	pathway					1140:1146	the proteasomal degradation pathway	1112:1146	the proteasomal degradation pathway	1112:1146	RPN13 is a component of the proteasomal degradation pathway.
20563614	4	56	theme	mass	609:612	arg1	spectrometry					614:625	mass spectrometry	609:625	mass spectrometry	609:625	Using lectin enrichment and mass spectrometry, we mapped several human cortical synaptic O-GlcNAc modification sites.
20563614	0	57	with	synaptic	26:33	arg1	spectrometry					108:119	ion trap mass spectrometry	94:119	ion trap mass spectrometry	94:119	Human Alzheimer's disease synaptic O-GlcNAc site mapping and iTRAQ expression proteomics with ion trap mass spectrometry.
20563614	8	58	theme	pathway	1140:1146	arg1	RPN13					1088:1092	RPN13	1088:1092	RPN13	1088:1092	RPN13 is a component of the proteasomal degradation pathway.
20563614	8	58	theme	pathway	1140:1146	arg1	component					1099:1107	a component	1097:1107	a component of the proteasomal degradation pathway	1097:1146	RPN13 is a component of the proteasomal degradation pathway.
20563614	3	59	theme	possible	531:538	arg1	link					540:543	a possible link	529:543	a possible link to deficits in synaptic plasticity	529:578	Reduced levels of O-GlcNAc have been observed in AD, suggesting a possible link to deficits in synaptic plasticity.
20563614	11	60	theme	trap	1541:1544	arg1	spectrometry					1551:1562	ion trap mass spectrometry	1537:1562	ion trap mass spectrometry	1537:1562	Pulsed Q dissociation (PQD) is a recently introduced fragmentation strategy that enables detection of low mass iTRAQ reporter ions in ion trap mass spectrometry.
20563614	0	61	theme	site	44:47	arg1	mapping					49:55	O-GlcNAc site mapping and iTRAQ expression proteomics	35:87	mapping	49:55	Human Alzheimer's disease synaptic O-GlcNAc site mapping and iTRAQ expression proteomics with ion trap mass spectrometry.
20563614	4	62	theme	human	646:650	arg1	sites					692:696	several human cortical synaptic O-GlcNAc modification sites	638:696	several human cortical synaptic O-GlcNAc modification sites	638:696	Using lectin enrichment and mass spectrometry, we mapped several human cortical synaptic O-GlcNAc modification sites.
20563614	2	63	theme	nuclear	294:300	arg1	modification					334:345	a novel cytosolic and nuclear carbohydrate post-translational modification	272:345	a novel cytosolic and nuclear carbohydrate post-translational modification	272:345	We recently demonstrated that O-GlcNAc, a novel cytosolic and nuclear carbohydrate post-translational modification, is enriched at neuronal synapses and positively regulates synaptic plasticity linked to learning and memory in mice.
20563614	2	63	theme	nuclear	294:300	arg1	O-GlcNAc					262:269	O-GlcNAc	262:269	O-GlcNAc	262:269	We recently demonstrated that O-GlcNAc, a novel cytosolic and nuclear carbohydrate post-translational modification, is enriched at neuronal synapses and positively regulates synaptic plasticity linked to learning and memory in mice.
20563614	5	64	theme	tubulin	856:862	arg1	polymerization					864:877	tubulin polymerization	856:877	tubulin polymerization	856:877	Overlap in patterns of O-GlcNAcation between mouse and human appears to be high, as previously mapped mouse synaptic O-GlcNAc sites in Bassoon, Piccolo, and tubulin polymerization promoting protein p25 were identified in human.
20563614	12	65	theme	iTRAQ	1614:1618	arg1	quantitation					1620:1631	PQD-based iTRAQ quantitation	1604:1631	PQD-based iTRAQ quantitation	1604:1631	We optimized LTQ ion trap settings for PQD-based iTRAQ quantitation and demonstrated its utility in O-GlcNAc site mapping.
20563614	4	66	theme	synaptic	661:668	arg1	sites					692:696	several human cortical synaptic O-GlcNAc modification sites	638:696	several human cortical synaptic O-GlcNAc modification sites	638:696	Using lectin enrichment and mass spectrometry, we mapped several human cortical synaptic O-GlcNAc modification sites.
20563614	9	67	theme	possible	1224:1231	arg1	implication					1233:1243	possible implication	1224:1243	possible implication of those sites in synaptic plasticity in normal versus AD states	1224:1308	The potential interplay of phosphorylation with mapped O-GlcNAc sites, and possible implication of those sites in synaptic plasticity in normal versus AD states is discussed.
20563614	2	68	theme	cytosolic	280:288	arg1	modification					334:345	a novel cytosolic and nuclear carbohydrate post-translational modification	272:345	a novel cytosolic and nuclear carbohydrate post-translational modification	272:345	We recently demonstrated that O-GlcNAc, a novel cytosolic and nuclear carbohydrate post-translational modification, is enriched at neuronal synapses and positively regulates synaptic plasticity linked to learning and memory in mice.
20563614	2	68	theme	cytosolic	280:288	arg1	O-GlcNAc					262:269	O-GlcNAc	262:269	O-GlcNAc	262:269	We recently demonstrated that O-GlcNAc, a novel cytosolic and nuclear carbohydrate post-translational modification, is enriched at neuronal synapses and positively regulates synaptic plasticity linked to learning and memory in mice.
20563614	13	69	theme	several	1740:1746	arg1	proteins					1748:1755	several proteins	1740:1755	several proteins previously implicated in AD pathology	1740:1793	Using iTRAQ, abnormal synaptic expression levels of several proteins previously implicated in AD pathology were observed in addition to novel changes in synaptic specific protein expression including Synapsin II.
20563614	7	70	theme	pathway	1047:1053	arg1	Mek2					1002:1005	Mek2	1002:1005	Mek2	1002:1005	Mek2 is a signaling component of the Erk 1/2 pathway involved in synaptic plasticity.
20563614	7	70	theme	pathway	1047:1053	arg1	component					1022:1030	a signaling component	1010:1030	a signaling component of the Erk 1/2 pathway involved in synaptic plasticity	1010:1085	Mek2 is a signaling component of the Erk 1/2 pathway involved in synaptic plasticity.
20563614	12	71	theme	trap	1586:1589	arg1	settings					1591:1598	LTQ ion trap settings	1578:1598	LTQ ion trap settings for PQD-based iTRAQ quantitation	1578:1631	We optimized LTQ ion trap settings for PQD-based iTRAQ quantitation and demonstrated its utility in O-GlcNAc site mapping.
20563614	7	72	theme	Erk	1039:1041	arg1	pathway					1047:1053	the Erk 1/2 pathway	1035:1053	the Erk 1/2 pathway involved in synaptic plasticity	1035:1085	Mek2 is a signaling component of the Erk 1/2 pathway involved in synaptic plasticity.
20563614	9	73	theme	sites	1254:1258	arg1	implication					1233:1243	possible implication	1224:1243	possible implication of those sites in synaptic plasticity in normal versus AD states	1224:1308	The potential interplay of phosphorylation with mapped O-GlcNAc sites, and possible implication of those sites in synaptic plasticity in normal versus AD states is discussed.
20563614	9	73	theme	sites	1254:1258	arg1	interplay					1163:1171	The potential interplay	1149:1171	The potential interplay of phosphorylation with mapped O-GlcNAc sites	1149:1217	The potential interplay of phosphorylation with mapped O-GlcNAc sites, and possible implication of those sites in synaptic plasticity in normal versus AD states is discussed.
20563614	6	74	theme	O-GlcNAc	933:940	arg1	sites					955:959	Novel O-GlcNAc modification sites	927:959	Novel O-GlcNAc modification sites	927:959	Novel O-GlcNAc modification sites were identified on Mek2 and RPN13/ADRM1.
20563614	11	75	theme	low	1505:1507	arg1	ions					1529:1532	low mass iTRAQ reporter ions	1505:1532	low mass iTRAQ reporter ions in ion trap mass spectrometry	1505:1562	Pulsed Q dissociation (PQD) is a recently introduced fragmentation strategy that enables detection of low mass iTRAQ reporter ions in ion trap mass spectrometry.
20563614	9	76	theme	synaptic	1263:1270	arg1	plasticity					1272:1281	synaptic plasticity	1263:1281	synaptic plasticity in normal versus AD states	1263:1308	The potential interplay of phosphorylation with mapped O-GlcNAc sites, and possible implication of those sites in synaptic plasticity in normal versus AD states is discussed.
20563614	3	77	located	observed	502:509	arg2	levels					473:478	Reduced levels	465:478	Reduced levels of O-GlcNAc	465:490	Reduced levels of O-GlcNAc have been observed in AD, suggesting a possible link to deficits in synaptic plasticity.
20563614	3	77	located	observed	502:509	arg1	AD					514:515	AD	514:515	AD	514:515	Reduced levels of O-GlcNAc have been observed in AD, suggesting a possible link to deficits in synaptic plasticity.
20563614	1	78	theme	Neuronal	122:129	arg1	deficits					151:158	Neuronal synaptic functional deficits	122:158	Neuronal synaptic functional deficits	122:158	Neuronal synaptic functional deficits are linked to impaired learning and memory in Alzheimer's disease (AD).
20563614	0	79	theme	iTRAQ	61:65	arg1	proteomics					78:87	O-GlcNAc site mapping and iTRAQ expression proteomics	35:87	proteomics	78:87	Human Alzheimer's disease synaptic O-GlcNAc site mapping and iTRAQ expression proteomics with ion trap mass spectrometry.
20563614	13	80	from	changes	1830:1836	arg1	expression					1867:1876	synaptic specific protein expression	1841:1876	synaptic specific protein expression including Synapsin II	1841:1898	Using iTRAQ, abnormal synaptic expression levels of several proteins previously implicated in AD pathology were observed in addition to novel changes in synaptic specific protein expression including Synapsin II.
20563614	1	81	theme	functional	140:149	arg1	deficits					151:158	Neuronal synaptic functional deficits	122:158	Neuronal synaptic functional deficits	122:158	Neuronal synaptic functional deficits are linked to impaired learning and memory in Alzheimer's disease (AD).
20563614	12	82	theme	LTQ	1578:1580	arg1	settings					1591:1598	LTQ ion trap settings	1578:1598	LTQ ion trap settings for PQD-based iTRAQ quantitation	1578:1631	We optimized LTQ ion trap settings for PQD-based iTRAQ quantitation and demonstrated its utility in O-GlcNAc site mapping.
20563614	4	83	theme	modification	679:690	arg1	sites					692:696	several human cortical synaptic O-GlcNAc modification sites	638:696	several human cortical synaptic O-GlcNAc modification sites	638:696	Using lectin enrichment and mass spectrometry, we mapped several human cortical synaptic O-GlcNAc modification sites.
20563614	11	84	theme	ions	1529:1532	arg1	detection					1492:1500	detection	1492:1500	detection of low mass iTRAQ reporter ions in ion trap mass spectrometry	1492:1562	Pulsed Q dissociation (PQD) is a recently introduced fragmentation strategy that enables detection of low mass iTRAQ reporter ions in ion trap mass spectrometry.
20563614	13	85	theme	expression	1719:1728	arg1	levels					1730:1735	abnormal synaptic expression levels	1701:1735	abnormal synaptic expression levels of several proteins previously implicated in AD pathology	1701:1793	Using iTRAQ, abnormal synaptic expression levels of several proteins previously implicated in AD pathology were observed in addition to novel changes in synaptic specific protein expression including Synapsin II.
20563614	11	86	theme	iTRAQ	1514:1518	arg1	ions					1529:1532	low mass iTRAQ reporter ions	1505:1532	low mass iTRAQ reporter ions in ion trap mass spectrometry	1505:1562	Pulsed Q dissociation (PQD) is a recently introduced fragmentation strategy that enables detection of low mass iTRAQ reporter ions in ion trap mass spectrometry.
20563614	0	87	theme	ion	94:96	arg1	spectrometry					108:119	ion trap mass spectrometry	94:119	ion trap mass spectrometry	94:119	Human Alzheimer's disease synaptic O-GlcNAc site mapping and iTRAQ expression proteomics with ion trap mass spectrometry.
20563614	3	88	theme	O-GlcNAc	483:490	arg1	levels					473:478	Reduced levels	465:478	Reduced levels of O-GlcNAc	465:490	Reduced levels of O-GlcNAc have been observed in AD, suggesting a possible link to deficits in synaptic plasticity.
20563614	0	89	theme	mass	103:106	arg1	spectrometry					108:119	ion trap mass spectrometry	94:119	ion trap mass spectrometry	94:119	Human Alzheimer's disease synaptic O-GlcNAc site mapping and iTRAQ expression proteomics with ion trap mass spectrometry.
20563614	5	90	from	sites	825:829	arg1	Piccolo					843:849	Piccolo	843:849	Piccolo	843:849	Overlap in patterns of O-GlcNAcation between mouse and human appears to be high, as previously mapped mouse synaptic O-GlcNAc sites in Bassoon, Piccolo, and tubulin polymerization promoting protein p25 were identified in human.
20563614	5	90	from	sites	825:829	arg1	polymerization					864:877	tubulin polymerization	856:877	tubulin polymerization	856:877	Overlap in patterns of O-GlcNAcation between mouse and human appears to be high, as previously mapped mouse synaptic O-GlcNAc sites in Bassoon, Piccolo, and tubulin polymerization promoting protein p25 were identified in human.
20563614	11	91	from	ions	1529:1532	arg1	spectrometry					1551:1562	ion trap mass spectrometry	1537:1562	ion trap mass spectrometry	1537:1562	Pulsed Q dissociation (PQD) is a recently introduced fragmentation strategy that enables detection of low mass iTRAQ reporter ions in ion trap mass spectrometry.
20563614	12	92	theme	O-GlcNAc	1665:1672	arg1	mapping					1679:1685	O-GlcNAc site mapping	1665:1685	O-GlcNAc site mapping	1665:1685	We optimized LTQ ion trap settings for PQD-based iTRAQ quantitation and demonstrated its utility in O-GlcNAc site mapping.
20563614	5	93	theme	mouse	801:805	arg1	sites					825:829	previously mapped mouse synaptic O-GlcNAc sites	783:829	previously mapped mouse synaptic O-GlcNAc sites in Bassoon, Piccolo, and tubulin polymerization promoting protein p25	783:899	Overlap in patterns of O-GlcNAcation between mouse and human appears to be high, as previously mapped mouse synaptic O-GlcNAc sites in Bassoon, Piccolo, and tubulin polymerization promoting protein p25 were identified in human.
20563614	9	94	from	plasticity	1272:1281	arg1	AD					1300:1301	AD	1300:1301	AD	1300:1301	The potential interplay of phosphorylation with mapped O-GlcNAc sites, and possible implication of those sites in synaptic plasticity in normal versus AD states is discussed.
20563614	9	94	from	plasticity	1272:1281	arg1	normal					1286:1291	normal	1286:1291	normal	1286:1291	The potential interplay of phosphorylation with mapped O-GlcNAc sites, and possible implication of those sites in synaptic plasticity in normal versus AD states is discussed.
20563614	11	95	from	detection	1492:1500	arg1	spectrometry					1551:1562	ion trap mass spectrometry	1537:1562	ion trap mass spectrometry	1537:1562	Pulsed Q dissociation (PQD) is a recently introduced fragmentation strategy that enables detection of low mass iTRAQ reporter ions in ion trap mass spectrometry.
20563614	13	96	theme	abnormal	1701:1708	arg1	levels					1730:1735	abnormal synaptic expression levels	1701:1735	abnormal synaptic expression levels of several proteins previously implicated in AD pathology	1701:1793	Using iTRAQ, abnormal synaptic expression levels of several proteins previously implicated in AD pathology were observed in addition to novel changes in synaptic specific protein expression including Synapsin II.
20563614	13	97	theme	specific	1850:1857	arg1	expression					1867:1876	synaptic specific protein expression	1841:1876	synaptic specific protein expression including Synapsin II	1841:1898	Using iTRAQ, abnormal synaptic expression levels of several proteins previously implicated in AD pathology were observed in addition to novel changes in synaptic specific protein expression including Synapsin II.
20563614	5	98	theme	O-GlcNAc	816:823	arg1	sites					825:829	previously mapped mouse synaptic O-GlcNAc sites	783:829	previously mapped mouse synaptic O-GlcNAc sites in Bassoon, Piccolo, and tubulin polymerization promoting protein p25	783:899	Overlap in patterns of O-GlcNAcation between mouse and human appears to be high, as previously mapped mouse synaptic O-GlcNAc sites in Bassoon, Piccolo, and tubulin polymerization promoting protein p25 were identified in human.
20563614	9	99	dep	normal	1286:1291	arg1	states					1303:1308	states	1303:1308	states	1303:1308	The potential interplay of phosphorylation with mapped O-GlcNAc sites, and possible implication of those sites in synaptic plasticity in normal versus AD states is discussed.
20563614	11	100	theme	fragmentation	1456:1468	arg1	strategy					1470:1477	a recently introduced fragmentation strategy	1434:1477	a recently introduced fragmentation strategy that enables detection of low mass iTRAQ reporter ions in ion trap mass spectrometry	1434:1562	Pulsed Q dissociation (PQD) is a recently introduced fragmentation strategy that enables detection of low mass iTRAQ reporter ions in ion trap mass spectrometry.
20563614	11	100	theme	fragmentation	1456:1468	arg1	dissociation					1412:1423	Pulsed Q dissociation	1403:1423	Pulsed Q dissociation (PQD)	1403:1429	Pulsed Q dissociation (PQD) is a recently introduced fragmentation strategy that enables detection of low mass iTRAQ reporter ions in ion trap mass spectrometry.
20563614	0	101	theme	O-GlcNAc	35:42	arg1	mapping					49:55	O-GlcNAc site mapping and iTRAQ expression proteomics	35:87	mapping	49:55	Human Alzheimer's disease synaptic O-GlcNAc site mapping and iTRAQ expression proteomics with ion trap mass spectrometry.
20563614	10	102	theme	differential	1344:1355	arg1	approach					1379:1386	a powerful differential isotopic quantitative approach	1333:1386	a powerful differential isotopic quantitative approach in proteomics	1333:1400	iTRAQ is a powerful differential isotopic quantitative approach in proteomics.
20563614	10	102	theme	differential	1344:1355	arg1	iTRAQ					1324:1328	iTRAQ	1324:1328	iTRAQ	1324:1328	iTRAQ is a powerful differential isotopic quantitative approach in proteomics.
20563614	2	103	theme	synaptic	406:413	arg1	plasticity					415:424	synaptic plasticity	406:424	synaptic plasticity linked to learning and memory in mice	406:462	We recently demonstrated that O-GlcNAc, a novel cytosolic and nuclear carbohydrate post-translational modification, is enriched at neuronal synapses and positively regulates synaptic plasticity linked to learning and memory in mice.
20563614	2	104	theme	carbohydrate	302:313	arg1	modification					334:345	a novel cytosolic and nuclear carbohydrate post-translational modification	272:345	a novel cytosolic and nuclear carbohydrate post-translational modification	272:345	We recently demonstrated that O-GlcNAc, a novel cytosolic and nuclear carbohydrate post-translational modification, is enriched at neuronal synapses and positively regulates synaptic plasticity linked to learning and memory in mice.
20563614	2	104	theme	carbohydrate	302:313	arg1	O-GlcNAc					262:269	O-GlcNAc	262:269	O-GlcNAc	262:269	We recently demonstrated that O-GlcNAc, a novel cytosolic and nuclear carbohydrate post-translational modification, is enriched at neuronal synapses and positively regulates synaptic plasticity linked to learning and memory in mice.
20563614	8	105	theme	degradation	1128:1138	arg1	pathway					1140:1146	the proteasomal degradation pathway	1112:1146	the proteasomal degradation pathway	1112:1146	RPN13 is a component of the proteasomal degradation pathway.
20563614	11	106	theme	Q	1410:1410	arg1	strategy					1470:1477	a recently introduced fragmentation strategy	1434:1477	a recently introduced fragmentation strategy that enables detection of low mass iTRAQ reporter ions in ion trap mass spectrometry	1434:1562	Pulsed Q dissociation (PQD) is a recently introduced fragmentation strategy that enables detection of low mass iTRAQ reporter ions in ion trap mass spectrometry.
20563614	11	106	theme	Q	1410:1410	arg1	PQD					1426:1428	PQD	1426:1428	PQD	1426:1428	Pulsed Q dissociation (PQD) is a recently introduced fragmentation strategy that enables detection of low mass iTRAQ reporter ions in ion trap mass spectrometry.
20563614	11	106	theme	Q	1410:1410	arg1	dissociation					1412:1423	Pulsed Q dissociation	1403:1423	Pulsed Q dissociation (PQD)	1403:1429	Pulsed Q dissociation (PQD) is a recently introduced fragmentation strategy that enables detection of low mass iTRAQ reporter ions in ion trap mass spectrometry.
20563614	10	107	theme	quantitative	1366:1377	arg1	approach					1379:1386	a powerful differential isotopic quantitative approach	1333:1386	a powerful differential isotopic quantitative approach in proteomics	1333:1400	iTRAQ is a powerful differential isotopic quantitative approach in proteomics.
20563614	10	107	theme	quantitative	1366:1377	arg1	iTRAQ					1324:1328	iTRAQ	1324:1328	iTRAQ	1324:1328	iTRAQ is a powerful differential isotopic quantitative approach in proteomics.
20563614	12	108	theme	ion	1582:1584	arg1	settings					1591:1598	LTQ ion trap settings	1578:1598	LTQ ion trap settings for PQD-based iTRAQ quantitation	1578:1631	We optimized LTQ ion trap settings for PQD-based iTRAQ quantitation and demonstrated its utility in O-GlcNAc site mapping.
19684018	8	0	theme	amino	1254:1258	arg1	acids					1260:1264	as few as 5 amino acids	1242:1264	as few as 5 amino acids	1242:1264	Moving the cleavage site away from the Thr(27) polysaccharide by insertion of as few as 5 amino acids allows cleavage to occur in the presence of glycosylation.
19684018	9	1	theme	protein-tagged	1416:1429	arg1	transporter					1437:1447	a functional green fluorescent protein-tagged hCTR1 transporter	1385:1447	a functional green fluorescent protein-tagged hCTR1 transporter in live cells	1385:1461	Imaging studies using immunofluorescence in fixed cells and a functional green fluorescent protein-tagged hCTR1 transporter in live cells showed that the cleaved peptide accumulates in punctate structures in the cytoplasm.
19684018	4	2	theme	cleavage	604:611	arg1	site					591:594	the site	587:594	the site	587:594	We have now investigated (i) the site of this cleavage, determining which peptide bonds are cleaved, (ii) the mechanism by which glycosylation prevents cleavage, and (iii) where in the cell the proteolytic cleavage takes place.
19684018	4	2	theme	cleavage	604:611	arg1	cleavage					604:611	this cleavage	599:611	this cleavage	599:611	We have now investigated (i) the site of this cleavage, determining which peptide bonds are cleaved, (ii) the mechanism by which glycosylation prevents cleavage, and (iii) where in the cell the proteolytic cleavage takes place.
19684018	4	2	theme	cleavage	604:611	arg1	mechanism					668:676	the mechanism by which glycosylation prevents cleavage, and (iii) where in the cell the proteolytic cleavage takes place	664:783	(ii) the mechanism by which glycosylation prevents cleavage, and (iii) where in the cell the proteolytic cleavage takes place	659:783	We have now investigated (i) the site of this cleavage, determining which peptide bonds are cleaved, (ii) the mechanism by which glycosylation prevents cleavage, and (iii) where in the cell the proteolytic cleavage takes place.
19684018	5	3	dep	residues	839:846	arg1	29-33					848:852	29-33	848:852	29-33	848:852	Cleavage occurs in the sequence Ala-Ser-His-Ser-His (residues 29-33), which does not contain previously recognized protease cleavage sites.
19684018	9	4	theme	hCTR1	1431:1435	arg1	transporter					1437:1447	a functional green fluorescent protein-tagged hCTR1 transporter	1385:1447	a functional green fluorescent protein-tagged hCTR1 transporter in live cells	1385:1461	Imaging studies using immunofluorescence in fixed cells and a functional green fluorescent protein-tagged hCTR1 transporter in live cells showed that the cleaved peptide accumulates in punctate structures in the cytoplasm.
19684018	1	5	theme	transmembrane	255:267	arg1	segments					269:276	three transmembrane segments	249:276	three transmembrane segments	249:276	The human copper transporter hCTR1 is a homotrimer composed of a plasma membrane protein of 190 amino acids that contains three transmembrane segments.
19684018	0	6	theme	endosomal	104:112	arg1	compartment					114:124	a Rab9-positive endosomal compartment	88:124	a Rab9-positive endosomal compartment	88:124	Human copper transporter 1 lacking O-linked glycosylation is proteolytically cleaved in a Rab9-positive endosomal compartment.
19684018	2	7	link	N-linked	349:356	arg1	glycosylation					406:418	glycosylation	406:418	glycosylation	406:418	The extracellular 65-amino acid amino terminus of hCTR1 contains both N-linked (at Asn(15)) and O-linked (at Thr(27)) sites of glycosylation.
19684018	2	7	link	N-linked	349:356	arg1	sites					397:401	both N-linked (at Asn(15)) and O-linked (at Thr(27)) sites	344:401	both N-linked (at Asn(15)) and O-linked (at Thr(27)) sites of glycosylation	344:418	The extracellular 65-amino acid amino terminus of hCTR1 contains both N-linked (at Asn(15)) and O-linked (at Thr(27)) sites of glycosylation.
19684018	10	8	theme	transporter	1699:1709	arg1	delivery					1683:1690	delivery	1683:1690	delivery of the transporter to the plasma membrane	1683:1732	These puncta overlap compartments were stained by Rab9, indicating that hCTR1 cleavage occurs in a late endosomal compartment prior to delivery of the transporter to the plasma membrane.
19684018	2	9	theme	acid	306:309	arg1	terminus					317:324	The extracellular 65-amino acid amino terminus	279:324	The extracellular 65-amino acid amino terminus of hCTR1	279:333	The extracellular 65-amino acid amino terminus of hCTR1 contains both N-linked (at Asn(15)) and O-linked (at Thr(27)) sites of glycosylation.
19684018	2	10	dep	N-linked	349:356	arg1	Asn					362:364	Asn	362:364	Asn(15)	362:368	The extracellular 65-amino acid amino terminus of hCTR1 contains both N-linked (at Asn(15)) and O-linked (at Thr(27)) sites of glycosylation.
19684018	2	10	dep	N-linked	349:356	arg1	15					366:367	15	366:367	15	366:367	The extracellular 65-amino acid amino terminus of hCTR1 contains both N-linked (at Asn(15)) and O-linked (at Thr(27)) sites of glycosylation.
19684018	0	11	theme	Rab9-positive	90:102	arg1	compartment					114:124	a Rab9-positive endosomal compartment	88:124	a Rab9-positive endosomal compartment	88:124	Human copper transporter 1 lacking O-linked glycosylation is proteolytically cleaved in a Rab9-positive endosomal compartment.
19684018	2	12	theme	65-amino	297:304	arg1	terminus					317:324	The extracellular 65-amino acid amino terminus	279:324	The extracellular 65-amino acid amino terminus of hCTR1	279:333	The extracellular 65-amino acid amino terminus of hCTR1 contains both N-linked (at Asn(15)) and O-linked (at Thr(27)) sites of glycosylation.
19684018	8	13	theme	glycosylation	1310:1322	arg1	presence					1298:1305	the presence	1294:1305	the presence of glycosylation	1294:1322	Moving the cleavage site away from the Thr(27) polysaccharide by insertion of as few as 5 amino acids allows cleavage to occur in the presence of glycosylation.
19684018	10	14	theme	plasma	1718:1723	arg1	membrane					1725:1732	the plasma membrane	1714:1732	the plasma membrane	1714:1732	These puncta overlap compartments were stained by Rab9, indicating that hCTR1 cleavage occurs in a late endosomal compartment prior to delivery of the transporter to the plasma membrane.
19684018	9	15	theme	live	1452:1455	arg1	cells					1457:1461	live cells	1452:1461	live cells	1452:1461	Imaging studies using immunofluorescence in fixed cells and a functional green fluorescent protein-tagged hCTR1 transporter in live cells showed that the cleaved peptide accumulates in punctate structures in the cytoplasm.
19684018	9	16	from	immunofluorescence	1347:1364	arg1	cells					1375:1379	fixed cells	1369:1379	fixed cells	1369:1379	Imaging studies using immunofluorescence in fixed cells and a functional green fluorescent protein-tagged hCTR1 transporter in live cells showed that the cleaved peptide accumulates in punctate structures in the cytoplasm.
19684018	9	16	from	immunofluorescence	1347:1364	arg1	cells					1457:1461	live cells	1452:1461	live cells	1452:1461	Imaging studies using immunofluorescence in fixed cells and a functional green fluorescent protein-tagged hCTR1 transporter in live cells showed that the cleaved peptide accumulates in punctate structures in the cytoplasm.
19684018	2	17	theme	extracellular	283:295	arg1	terminus					317:324	The extracellular 65-amino acid amino terminus	279:324	The extracellular 65-amino acid amino terminus of hCTR1	279:333	The extracellular 65-amino acid amino terminus of hCTR1 contains both N-linked (at Asn(15)) and O-linked (at Thr(27)) sites of glycosylation.
19684018	2	18	theme	O-linked	375:382	arg1	glycosylation					406:418	glycosylation	406:418	glycosylation	406:418	The extracellular 65-amino acid amino terminus of hCTR1 contains both N-linked (at Asn(15)) and O-linked (at Thr(27)) sites of glycosylation.
19684018	2	18	theme	O-linked	375:382	arg1	sites					397:401	both N-linked (at Asn(15)) and O-linked (at Thr(27)) sites	344:401	both N-linked (at Asn(15)) and O-linked (at Thr(27)) sites of glycosylation	344:418	The extracellular 65-amino acid amino terminus of hCTR1 contains both N-linked (at Asn(15)) and O-linked (at Thr(27)) sites of glycosylation.
19684018	7	19	from	Thr	1094:1096	arg1	polysaccharide					1076:1089	the O-linked polysaccharide	1063:1089	the O-linked polysaccharide at Thr(27)	1063:1100	We also show that the O-linked polysaccharide at Thr(27) blocks proteolysis due to its proximity to the cleavage site.
19684018	4	20	dep	site	591:594	arg1	i					584:584	i	584:584	i	584:584	We have now investigated (i) the site of this cleavage, determining which peptide bonds are cleaved, (ii) the mechanism by which glycosylation prevents cleavage, and (iii) where in the cell the proteolytic cleavage takes place.
19684018	4	20	dep	site	591:594	arg1	determining					614:624	determining	614:624	determining which peptide bonds are cleaved	614:656	We have now investigated (i) the site of this cleavage, determining which peptide bonds are cleaved, (ii) the mechanism by which glycosylation prevents cleavage, and (iii) where in the cell the proteolytic cleavage takes place.
19684018	6	21	theme	hCTR1	944:948	arg1	mutants					950:956	hCTR1 mutants	944:956	hCTR1 mutants	944:956	Using a series of hCTR1 mutants, we show that cleavage occurs preferentially between residues Ala(29)-Ser(30)-His(31).
19684018	0	22	theme	copper	6:11	arg1	transporter					13:23	Human copper transporter 1	0:25	Human copper transporter 1 lacking O-linked glycosylation	0:56	Human copper transporter 1 lacking O-linked glycosylation is proteolytically cleaved in a Rab9-positive endosomal compartment.
19684018	8	23	theme	Thr	1203:1205	arg1	polysaccharide					1211:1224	the Thr(27) polysaccharide	1199:1224	the Thr(27) polysaccharide	1199:1224	Moving the cleavage site away from the Thr(27) polysaccharide by insertion of as few as 5 amino acids allows cleavage to occur in the presence of glycosylation.
19684018	2	24	theme	hCTR1	329:333	arg1	terminus					317:324	The extracellular 65-amino acid amino terminus	279:324	The extracellular 65-amino acid amino terminus of hCTR1	279:333	The extracellular 65-amino acid amino terminus of hCTR1 contains both N-linked (at Asn(15)) and O-linked (at Thr(27)) sites of glycosylation.
19684018	9	25	theme	punctate	1510:1517	arg1	structures					1519:1528	punctate structures	1510:1528	punctate structures in the cytoplasm	1510:1545	Imaging studies using immunofluorescence in fixed cells and a functional green fluorescent protein-tagged hCTR1 transporter in live cells showed that the cleaved peptide accumulates in punctate structures in the cytoplasm.
19684018	0	26	theme	Human	0:4	arg1	transporter					13:23	Human copper transporter 1	0:25	Human copper transporter 1 lacking O-linked glycosylation	0:56	Human copper transporter 1 lacking O-linked glycosylation is proteolytically cleaved in a Rab9-positive endosomal compartment.
19684018	9	27	theme	Imaging	1325:1331	arg1	studies					1333:1339	Imaging studies	1325:1339	Imaging studies using immunofluorescence in fixed cells and a functional green fluorescent protein-tagged hCTR1 transporter in live cells	1325:1461	Imaging studies using immunofluorescence in fixed cells and a functional green fluorescent protein-tagged hCTR1 transporter in live cells showed that the cleaved peptide accumulates in punctate structures in the cytoplasm.
19684018	9	28	theme	functional	1387:1396	arg1	transporter					1437:1447	a functional green fluorescent protein-tagged hCTR1 transporter	1385:1447	a functional green fluorescent protein-tagged hCTR1 transporter in live cells	1385:1461	Imaging studies using immunofluorescence in fixed cells and a functional green fluorescent protein-tagged hCTR1 transporter in live cells showed that the cleaved peptide accumulates in punctate structures in the cytoplasm.
19684018	0	29	link	O-linked	35:42	arg1	glycosylation					44:56	O-linked glycosylation	35:56	O-linked glycosylation	35:56	Human copper transporter 1 lacking O-linked glycosylation is proteolytically cleaved in a Rab9-positive endosomal compartment.
19684018	5	30	theme	sequence	809:816	arg1	Ala-Ser-His-Ser-His					818:836	the sequence Ala-Ser-His-Ser-His	805:836	the sequence Ala-Ser-His-Ser-His (residues 29-33)	805:853	Cleavage occurs in the sequence Ala-Ser-His-Ser-His (residues 29-33), which does not contain previously recognized protease cleavage sites.
19684018	5	30	theme	sequence	809:816	arg1	residues					839:846	residues 29-33	839:852	residues 29-33	839:852	Cleavage occurs in the sequence Ala-Ser-His-Ser-His (residues 29-33), which does not contain previously recognized protease cleavage sites.
19684018	1	31	theme	plasma	192:197	arg1	protein					208:214	a plasma membrane protein	190:214	a plasma membrane protein of 190 amino acids	190:233	The human copper transporter hCTR1 is a homotrimer composed of a plasma membrane protein of 190 amino acids that contains three transmembrane segments.
19684018	3	32	from	Thr	443:445	arg1	O-glycosylation					424:438	O-glycosylation	424:438	O-glycosylation at Thr(27)	424:449	If O-glycosylation at Thr(27) is prevented, hCTR1 is efficiently cleaved, removing approximately 30 amino acids from the amino terminus.
19684018	3	33	theme	amino	521:525	arg1	acids					527:531	approximately 30 amino acids	504:531	approximately 30 amino acids	504:531	If O-glycosylation at Thr(27) is prevented, hCTR1 is efficiently cleaved, removing approximately 30 amino acids from the amino terminus.
19684018	6	34	theme	Ala	1020:1022	arg1	-Ser					1027:1030	Ala(29)-Ser(30)	1020:1034	residues Ala(29)-Ser(30)-His(31)	1011:1042	Using a series of hCTR1 mutants, we show that cleavage occurs preferentially between residues Ala(29)-Ser(30)-His(31).
19684018	8	35	theme	acids	1260:1264	arg1	insertion					1229:1237	insertion	1229:1237	insertion of as few as 5 amino acids	1229:1264	Moving the cleavage site away from the Thr(27) polysaccharide by insertion of as few as 5 amino acids allows cleavage to occur in the presence of glycosylation.
19684018	1	36	theme	membrane	199:206	arg1	protein					208:214	a plasma membrane protein	190:214	a plasma membrane protein of 190 amino acids	190:233	The human copper transporter hCTR1 is a homotrimer composed of a plasma membrane protein of 190 amino acids that contains three transmembrane segments.
19684018	9	37	theme	cleaved	1479:1485	arg1	peptide					1487:1493	the cleaved peptide	1475:1493	the cleaved peptide	1475:1493	Imaging studies using immunofluorescence in fixed cells and a functional green fluorescent protein-tagged hCTR1 transporter in live cells showed that the cleaved peptide accumulates in punctate structures in the cytoplasm.
19684018	10	38	theme	late	1647:1650	arg1	compartment					1662:1672	a late endosomal compartment	1645:1672	a late endosomal compartment prior to delivery of the transporter to the plasma membrane	1645:1732	These puncta overlap compartments were stained by Rab9, indicating that hCTR1 cleavage occurs in a late endosomal compartment prior to delivery of the transporter to the plasma membrane.
19684018	2	39	theme	amino	311:315	arg1	terminus					317:324	The extracellular 65-amino acid amino terminus	279:324	The extracellular 65-amino acid amino terminus of hCTR1	279:333	The extracellular 65-amino acid amino terminus of hCTR1 contains both N-linked (at Asn(15)) and O-linked (at Thr(27)) sites of glycosylation.
19684018	3	40	gly	O-glycosylation	424:438	arg1	Thr					443:445	Thr	443:445	Thr(27)	443:449	If O-glycosylation at Thr(27) is prevented, hCTR1 is efficiently cleaved, removing approximately 30 amino acids from the amino terminus.
19684018	3	40	gly	O-glycosylation	424:438	arg2	27					447:448	27	447:448	27	447:448	If O-glycosylation at Thr(27) is prevented, hCTR1 is efficiently cleaved, removing approximately 30 amino acids from the amino terminus.
19684018	3	40	gly	O-glycosylation	424:438	arg1	27					447:448	27	447:448	27	447:448	If O-glycosylation at Thr(27) is prevented, hCTR1 is efficiently cleaved, removing approximately 30 amino acids from the amino terminus.
19684018	3	40	gly	O-glycosylation	424:438	arg2	Thr					443:445	Thr	443:445	Thr(27)	443:449	If O-glycosylation at Thr(27) is prevented, hCTR1 is efficiently cleaved, removing approximately 30 amino acids from the amino terminus.
19684018	0	41	theme	O-linked	35:42	arg1	glycosylation					44:56	O-linked glycosylation	35:56	O-linked glycosylation	35:56	Human copper transporter 1 lacking O-linked glycosylation is proteolytically cleaved in a Rab9-positive endosomal compartment.
19684018	2	42	theme	N-linked	349:356	arg1	glycosylation					406:418	glycosylation	406:418	glycosylation	406:418	The extracellular 65-amino acid amino terminus of hCTR1 contains both N-linked (at Asn(15)) and O-linked (at Thr(27)) sites of glycosylation.
19684018	2	42	theme	N-linked	349:356	arg1	sites					397:401	both N-linked (at Asn(15)) and O-linked (at Thr(27)) sites	344:401	both N-linked (at Asn(15)) and O-linked (at Thr(27)) sites of glycosylation	344:418	The extracellular 65-amino acid amino terminus of hCTR1 contains both N-linked (at Asn(15)) and O-linked (at Thr(27)) sites of glycosylation.
19684018	1	43	contain	contains	240:247	arg2	segments					269:276	three transmembrane segments	249:276	three transmembrane segments	249:276	The human copper transporter hCTR1 is a homotrimer composed of a plasma membrane protein of 190 amino acids that contains three transmembrane segments.
19684018	1	43	contain	contains	240:247	arg1	hCTR1					156:160	The human copper transporter hCTR1	127:160	The human copper transporter hCTR1	127:160	The human copper transporter hCTR1 is a homotrimer composed of a plasma membrane protein of 190 amino acids that contains three transmembrane segments.
19684018	1	43	contain	contains	240:247	arg1	homotrimer					167:176	a homotrimer	165:176	a homotrimer composed of a plasma membrane protein of 190 amino acids that contains three transmembrane segments	165:276	The human copper transporter hCTR1 is a homotrimer composed of a plasma membrane protein of 190 amino acids that contains three transmembrane segments.
19684018	4	44	dep	mechanism	668:676	arg1	ii					660:661	ii	660:661	ii	660:661	We have now investigated (i) the site of this cleavage, determining which peptide bonds are cleaved, (ii) the mechanism by which glycosylation prevents cleavage, and (iii) where in the cell the proteolytic cleavage takes place.
19684018	6	45	theme	mutants	950:956	arg1	series					934:939	a series	932:939	a series of hCTR1 mutants	932:956	Using a series of hCTR1 mutants, we show that cleavage occurs preferentially between residues Ala(29)-Ser(30)-His(31).
19684018	9	46	from	transporter	1437:1447	arg1	cells					1375:1379	fixed cells	1369:1379	fixed cells	1369:1379	Imaging studies using immunofluorescence in fixed cells and a functional green fluorescent protein-tagged hCTR1 transporter in live cells showed that the cleaved peptide accumulates in punctate structures in the cytoplasm.
19684018	9	46	from	transporter	1437:1447	arg1	cells					1457:1461	live cells	1452:1461	live cells	1452:1461	Imaging studies using immunofluorescence in fixed cells and a functional green fluorescent protein-tagged hCTR1 transporter in live cells showed that the cleaved peptide accumulates in punctate structures in the cytoplasm.
19684018	7	47	link	O-linked	1067:1074	arg1	polysaccharide					1076:1089	the O-linked polysaccharide	1063:1089	the O-linked polysaccharide at Thr(27)	1063:1100	We also show that the O-linked polysaccharide at Thr(27) blocks proteolysis due to its proximity to the cleavage site.
19684018	2	48	link	O-linked	375:382	arg1	glycosylation					406:418	glycosylation	406:418	glycosylation	406:418	The extracellular 65-amino acid amino terminus of hCTR1 contains both N-linked (at Asn(15)) and O-linked (at Thr(27)) sites of glycosylation.
19684018	2	48	link	O-linked	375:382	arg1	sites					397:401	both N-linked (at Asn(15)) and O-linked (at Thr(27)) sites	344:401	both N-linked (at Asn(15)) and O-linked (at Thr(27)) sites of glycosylation	344:418	The extracellular 65-amino acid amino terminus of hCTR1 contains both N-linked (at Asn(15)) and O-linked (at Thr(27)) sites of glycosylation.
19684018	5	49	theme	recognized	890:899	arg1	sites					919:923	previously recognized protease cleavage sites	879:923	previously recognized protease cleavage sites	879:923	Cleavage occurs in the sequence Ala-Ser-His-Ser-His (residues 29-33), which does not contain previously recognized protease cleavage sites.
19684018	9	50	theme	green	1398:1402	arg1	transporter					1437:1447	a functional green fluorescent protein-tagged hCTR1 transporter	1385:1447	a functional green fluorescent protein-tagged hCTR1 transporter in live cells	1385:1461	Imaging studies using immunofluorescence in fixed cells and a functional green fluorescent protein-tagged hCTR1 transporter in live cells showed that the cleaved peptide accumulates in punctate structures in the cytoplasm.
19684018	2	51	theme	glycosylation	406:418	arg1	glycosylation					406:418	glycosylation	406:418	glycosylation	406:418	The extracellular 65-amino acid amino terminus of hCTR1 contains both N-linked (at Asn(15)) and O-linked (at Thr(27)) sites of glycosylation.
19684018	2	51	theme	glycosylation	406:418	arg1	sites					397:401	both N-linked (at Asn(15)) and O-linked (at Thr(27)) sites	344:401	both N-linked (at Asn(15)) and O-linked (at Thr(27)) sites of glycosylation	344:418	The extracellular 65-amino acid amino terminus of hCTR1 contains both N-linked (at Asn(15)) and O-linked (at Thr(27)) sites of glycosylation.
19684018	5	52	theme	protease	901:908	arg1	sites					919:923	previously recognized protease cleavage sites	879:923	previously recognized protease cleavage sites	879:923	Cleavage occurs in the sequence Ala-Ser-His-Ser-His (residues 29-33), which does not contain previously recognized protease cleavage sites.
19684018	4	53	theme	proteolytic	752:762	arg1	cleavage					764:771	the proteolytic cleavage	748:771	the proteolytic cleavage	748:771	We have now investigated (i) the site of this cleavage, determining which peptide bonds are cleaved, (ii) the mechanism by which glycosylation prevents cleavage, and (iii) where in the cell the proteolytic cleavage takes place.
19684018	5	54	theme	cleavage	910:917	arg1	sites					919:923	previously recognized protease cleavage sites	879:923	previously recognized protease cleavage sites	879:923	Cleavage occurs in the sequence Ala-Ser-His-Ser-His (residues 29-33), which does not contain previously recognized protease cleavage sites.
19684018	2	55	gly	glycosylation	406:418	arg2	glycosylation					406:418	glycosylation	406:418	glycosylation	406:418	The extracellular 65-amino acid amino terminus of hCTR1 contains both N-linked (at Asn(15)) and O-linked (at Thr(27)) sites of glycosylation.
19684018	2	55	gly	glycosylation	406:418	arg2	sites					397:401	both N-linked (at Asn(15)) and O-linked (at Thr(27)) sites	344:401	both N-linked (at Asn(15)) and O-linked (at Thr(27)) sites of glycosylation	344:418	The extracellular 65-amino acid amino terminus of hCTR1 contains both N-linked (at Asn(15)) and O-linked (at Thr(27)) sites of glycosylation.
19684018	9	56	from	structures	1519:1528	arg1	cytoplasm					1537:1545	the cytoplasm	1533:1545	the cytoplasm	1533:1545	Imaging studies using immunofluorescence in fixed cells and a functional green fluorescent protein-tagged hCTR1 transporter in live cells showed that the cleaved peptide accumulates in punctate structures in the cytoplasm.
19684018	1	57	theme	human	131:135	arg1	hCTR1					156:160	The human copper transporter hCTR1	127:160	The human copper transporter hCTR1	127:160	The human copper transporter hCTR1 is a homotrimer composed of a plasma membrane protein of 190 amino acids that contains three transmembrane segments.
19684018	1	57	theme	human	131:135	arg1	homotrimer					167:176	a homotrimer	165:176	a homotrimer composed of a plasma membrane protein of 190 amino acids that contains three transmembrane segments	165:276	The human copper transporter hCTR1 is a homotrimer composed of a plasma membrane protein of 190 amino acids that contains three transmembrane segments.
19684018	9	58	theme	fluorescent	1404:1414	arg1	transporter					1437:1447	a functional green fluorescent protein-tagged hCTR1 transporter	1385:1447	a functional green fluorescent protein-tagged hCTR1 transporter in live cells	1385:1461	Imaging studies using immunofluorescence in fixed cells and a functional green fluorescent protein-tagged hCTR1 transporter in live cells showed that the cleaved peptide accumulates in punctate structures in the cytoplasm.
19684018	10	59	theme	prior	1674:1678	arg1	compartment					1662:1672	a late endosomal compartment	1645:1672	a late endosomal compartment prior to delivery of the transporter to the plasma membrane	1645:1732	These puncta overlap compartments were stained by Rab9, indicating that hCTR1 cleavage occurs in a late endosomal compartment prior to delivery of the transporter to the plasma membrane.
19684018	7	60	theme	cleavage	1149:1156	arg1	site					1158:1161	the cleavage site	1145:1161	the cleavage site	1145:1161	We also show that the O-linked polysaccharide at Thr(27) blocks proteolysis due to its proximity to the cleavage site.
19684018	9	61	theme	fixed	1369:1373	arg1	cells					1375:1379	fixed cells	1369:1379	fixed cells	1369:1379	Imaging studies using immunofluorescence in fixed cells and a functional green fluorescent protein-tagged hCTR1 transporter in live cells showed that the cleaved peptide accumulates in punctate structures in the cytoplasm.
19684018	1	62	theme	copper	137:142	arg1	hCTR1					156:160	The human copper transporter hCTR1	127:160	The human copper transporter hCTR1	127:160	The human copper transporter hCTR1 is a homotrimer composed of a plasma membrane protein of 190 amino acids that contains three transmembrane segments.
19684018	1	62	theme	copper	137:142	arg1	homotrimer					167:176	a homotrimer	165:176	a homotrimer composed of a plasma membrane protein of 190 amino acids that contains three transmembrane segments	165:276	The human copper transporter hCTR1 is a homotrimer composed of a plasma membrane protein of 190 amino acids that contains three transmembrane segments.
19684018	8	63	theme	cleavage	1175:1182	arg1	site					1184:1187	the cleavage site	1171:1187	the cleavage site	1171:1187	Moving the cleavage site away from the Thr(27) polysaccharide by insertion of as few as 5 amino acids allows cleavage to occur in the presence of glycosylation.
19684018	1	64	theme	amino	223:227	arg1	acids					229:233	190 amino acids	219:233	190 amino acids	219:233	The human copper transporter hCTR1 is a homotrimer composed of a plasma membrane protein of 190 amino acids that contains three transmembrane segments.
19684018	4	65	theme	peptide	632:638	arg1	bonds					640:644	peptide bonds	632:644	peptide bonds	632:644	We have now investigated (i) the site of this cleavage, determining which peptide bonds are cleaved, (ii) the mechanism by which glycosylation prevents cleavage, and (iii) where in the cell the proteolytic cleavage takes place.
19684018	1	66	theme	transporter	144:154	arg1	hCTR1					156:160	The human copper transporter hCTR1	127:160	The human copper transporter hCTR1	127:160	The human copper transporter hCTR1 is a homotrimer composed of a plasma membrane protein of 190 amino acids that contains three transmembrane segments.
19684018	1	66	theme	transporter	144:154	arg1	homotrimer					167:176	a homotrimer	165:176	a homotrimer composed of a plasma membrane protein of 190 amino acids that contains three transmembrane segments	165:276	The human copper transporter hCTR1 is a homotrimer composed of a plasma membrane protein of 190 amino acids that contains three transmembrane segments.
19684018	1	67	theme	acids	229:233	arg1	protein					208:214	a plasma membrane protein	190:214	a plasma membrane protein of 190 amino acids	190:233	The human copper transporter hCTR1 is a homotrimer composed of a plasma membrane protein of 190 amino acids that contains three transmembrane segments.
19684018	10	68	theme	endosomal	1652:1660	arg1	compartment					1662:1672	a late endosomal compartment	1645:1672	a late endosomal compartment prior to delivery of the transporter to the plasma membrane	1645:1732	These puncta overlap compartments were stained by Rab9, indicating that hCTR1 cleavage occurs in a late endosomal compartment prior to delivery of the transporter to the plasma membrane.
19684018	2	69	dep	O-linked	375:382	arg1	27					392:393	27	392:393	27	392:393	The extracellular 65-amino acid amino terminus of hCTR1 contains both N-linked (at Asn(15)) and O-linked (at Thr(27)) sites of glycosylation.
19684018	2	69	dep	O-linked	375:382	arg1	Thr					388:390	Thr	388:390	Thr(27)	388:394	The extracellular 65-amino acid amino terminus of hCTR1 contains both N-linked (at Asn(15)) and O-linked (at Thr(27)) sites of glycosylation.
19684018	6	70	dep	-Ser	1027:1030	arg1	-His					1035:1038	-His(31)	1035:1042	residues Ala(29)-Ser(30)-His(31)	1011:1042	Using a series of hCTR1 mutants, we show that cleavage occurs preferentially between residues Ala(29)-Ser(30)-His(31).
19684018	6	71	dep	residues	1011:1018	arg1	-Ser					1027:1030	Ala(29)-Ser(30)	1020:1034	residues Ala(29)-Ser(30)-His(31)	1011:1042	Using a series of hCTR1 mutants, we show that cleavage occurs preferentially between residues Ala(29)-Ser(30)-His(31).
19684018	4	72	dep	takes	773:777	arg1	iii					725:727	iii	725:727	iii	725:727	We have now investigated (i) the site of this cleavage, determining which peptide bonds are cleaved, (ii) the mechanism by which glycosylation prevents cleavage, and (iii) where in the cell the proteolytic cleavage takes place.
19684018	2	73	contain	contains	335:342	arg1	terminus					317:324	The extracellular 65-amino acid amino terminus	279:324	The extracellular 65-amino acid amino terminus of hCTR1	279:333	The extracellular 65-amino acid amino terminus of hCTR1 contains both N-linked (at Asn(15)) and O-linked (at Thr(27)) sites of glycosylation.
19684018	2	73	contain	contains	335:342	arg2	glycosylation					406:418	glycosylation	406:418	glycosylation	406:418	The extracellular 65-amino acid amino terminus of hCTR1 contains both N-linked (at Asn(15)) and O-linked (at Thr(27)) sites of glycosylation.
19684018	2	73	contain	contains	335:342	arg2	sites					397:401	both N-linked (at Asn(15)) and O-linked (at Thr(27)) sites	344:401	both N-linked (at Asn(15)) and O-linked (at Thr(27)) sites of glycosylation	344:418	The extracellular 65-amino acid amino terminus of hCTR1 contains both N-linked (at Asn(15)) and O-linked (at Thr(27)) sites of glycosylation.
19684018	3	74	theme	amino	542:546	arg1	terminus					548:555	the amino terminus	538:555	the amino terminus	538:555	If O-glycosylation at Thr(27) is prevented, hCTR1 is efficiently cleaved, removing approximately 30 amino acids from the amino terminus.
19684018	7	75	theme	O-linked	1067:1074	arg1	polysaccharide					1076:1089	the O-linked polysaccharide	1063:1089	the O-linked polysaccharide at Thr(27)	1063:1100	We also show that the O-linked polysaccharide at Thr(27) blocks proteolysis due to its proximity to the cleavage site.
19684018	5	76	contain	contain	871:877	arg1	Ala-Ser-His-Ser-His					818:836	the sequence Ala-Ser-His-Ser-His	805:836	the sequence Ala-Ser-His-Ser-His (residues 29-33)	805:853	Cleavage occurs in the sequence Ala-Ser-His-Ser-His (residues 29-33), which does not contain previously recognized protease cleavage sites.
19684018	5	76	contain	contain	871:877	arg2	sites					919:923	previously recognized protease cleavage sites	879:923	previously recognized protease cleavage sites	879:923	Cleavage occurs in the sequence Ala-Ser-His-Ser-His (residues 29-33), which does not contain previously recognized protease cleavage sites.
19684018	5	76	contain	contain	871:877	arg1	residues					839:846	residues 29-33	839:852	residues 29-33	839:852	Cleavage occurs in the sequence Ala-Ser-His-Ser-His (residues 29-33), which does not contain previously recognized protease cleavage sites.
19684018	10	77	theme	hCTR1	1620:1624	arg1	cleavage					1626:1633	hCTR1 cleavage	1620:1633	hCTR1 cleavage	1620:1633	These puncta overlap compartments were stained by Rab9, indicating that hCTR1 cleavage occurs in a late endosomal compartment prior to delivery of the transporter to the plasma membrane.
22159084	1	0	from	intestine	221:229	arg1	Cl					195:196	Cl	195:196	Cl	195:196	SLC26A3 is a Cl(-)/HCO(3)(-) exchanger that plays a major role in Cl(-) absorption from the intestine.
22159084	10	1	theme	cell	1334:1337	arg1	expression					1347:1356	decreased cell surface expression	1324:1356	decreased cell surface expression	1324:1356	Deglycosylation of SLC26A3 causes a defect in cell surface processing with decreased cell surface expression.
22159084	6	2	link	N-linked	797:804	arg1	carbohydrates					806:818	the N-linked carbohydrates	793:818	the N-linked carbohydrates	793:818	Deglycosylation experiments with glycosidases indicated that the mature glycosylated form of SLC26A3 exists at the plasma membrane, and a putative large second extracellular loop contains all of the N-linked carbohydrates.
22159084	1	3	theme	major	181:185	arg1	role					187:190	a major role	179:190	a major role	179:190	SLC26A3 is a Cl(-)/HCO(3)(-) exchanger that plays a major role in Cl(-) absorption from the intestine.
22159084	6	4	contain	contains	777:784	arg2	all					786:788	all	786:788	all	786:788	Deglycosylation experiments with glycosidases indicated that the mature glycosylated form of SLC26A3 exists at the plasma membrane, and a putative large second extracellular loop contains all of the N-linked carbohydrates.
22159084	6	4	contain	contains	777:784	arg1	loop					772:775	a putative large second extracellular loop	734:775	a putative large second extracellular loop	734:775	Deglycosylation experiments with glycosidases indicated that the mature glycosylated form of SLC26A3 exists at the plasma membrane, and a putative large second extracellular loop contains all of the N-linked carbohydrates.
22159084	6	4	contain	contains	777:784	arg2	carbohydrates					806:818	the N-linked carbohydrates	793:818	the N-linked carbohydrates	793:818	Deglycosylation experiments with glycosidases indicated that the mature glycosylated form of SLC26A3 exists at the plasma membrane, and a putative large second extracellular loop contains all of the N-linked carbohydrates.
22159084	3	5	gly	glycosylated	324:335	arg1	SLC26A3					312:318	SLC26A3	312:318	SLC26A3	312:318	It has been shown that SLC26A3 are glycosylated, with the attached carbohydrate being extracellular and perhaps modulating function.
22159084	2	6	theme	chloride-losing	263:277	arg1	diarrhea					279:286	congenital chloride-losing diarrhea	252:286	congenital chloride-losing diarrhea	252:286	Its mutation causes congenital chloride-losing diarrhea.
22159084	7	7	theme	SLC26A3	840:846	arg1	Deglycosylation					821:835	Deglycosylation	821:835	Deglycosylation of SLC26A3	821:846	Deglycosylation of SLC26A3 causes depression of transport activity compared with wild-type, although robust intracellular pH changes were still observed, suggesting that N-glycosylation is not absolutely necessary for transport activity.
22159084	10	8	theme	surface	1339:1345	arg1	expression					1347:1356	decreased cell surface expression	1324:1356	decreased cell surface expression	1324:1356	Deglycosylation of SLC26A3 causes a defect in cell surface processing with decreased cell surface expression.
22159084	0	9	theme	intestinal	93:102	arg1	SLC26A3					120:126	the intestinal anion exchanger SLC26A3	89:126	the intestinal anion exchanger SLC26A3	89:126	Role of N-glycosylation in cell surface expression and protection against proteolysis of the intestinal anion exchanger SLC26A3.
22159084	0	10	from	Role	0:3	arg1	expression					40:49	cell surface expression	27:49	cell surface expression	27:49	Role of N-glycosylation in cell surface expression and protection against proteolysis of the intestinal anion exchanger SLC26A3.
22159084	6	11	with	experiments	614:624	arg1	glycosidases					631:642	glycosidases	631:642	glycosidases	631:642	Deglycosylation experiments with glycosidases indicated that the mature glycosylated form of SLC26A3 exists at the plasma membrane, and a putative large second extracellular loop contains all of the N-linked carbohydrates.
22159084	5	12	theme	biochemical	517:527	arg1	modification					529:540	biochemical modification	517:540	biochemical modification	517:540	We used the approaches of biochemical modification and site-directed mutagenesis to prevent glycosylation.
22159084	10	13	with	processing	1308:1317	arg1	expression					1347:1356	decreased cell surface expression	1324:1356	decreased cell surface expression	1324:1356	Deglycosylation of SLC26A3 causes a defect in cell surface processing with decreased cell surface expression.
22159084	12	14	theme	increased	1554:1562	arg1	susceptibility					1564:1577	increased susceptibility	1554:1577	increased susceptibility to trypsin	1554:1588	While the mature glycosylated SLC26A3 showed little breakdown after treatment with trypsin, deglycosylated SLC26A3 exhibited increased susceptibility to trypsin, suggesting that the oligosaccharides protect SLC26A3 from tryptic digestion.
22159084	13	15	theme	cell	1750:1753	arg1	expression					1763:1772	cell surface expression	1750:1772	cell surface expression	1750:1772	In conclusion, our data indicate that N-glycosylation of SLC26A3 is important for cell surface expression and for protection from proteolytic degradation that may contribute to the understanding of pathogenesis of congenital disorders of glycosylation.
22159084	5	16	theme	modification	529:540	arg1	approaches					503:512	the approaches	499:512	the approaches of biochemical modification and site-directed mutagenesis	499:570	We used the approaches of biochemical modification and site-directed mutagenesis to prevent glycosylation.
22159084	8	17	gly	glycosylation	1071:1083	arg2	sites					1085:1089	glycosylation sites	1071:1089	glycosylation sites	1071:1089	To localize glycosylation sites, we mutated the five consensus sites by replacing asparagine (N) with glutamine.
22159084	0	18	theme	exchanger	110:118	arg1	SLC26A3					120:126	the intestinal anion exchanger SLC26A3	89:126	the intestinal anion exchanger SLC26A3	89:126	Role of N-glycosylation in cell surface expression and protection against proteolysis of the intestinal anion exchanger SLC26A3.
22159084	7	19	gly	Deglycosylation	821:835	arg1	SLC26A3					840:846	SLC26A3	840:846	SLC26A3	840:846	Deglycosylation of SLC26A3 causes depression of transport activity compared with wild-type, although robust intracellular pH changes were still observed, suggesting that N-glycosylation is not absolutely necessary for transport activity.
22159084	5	20	theme	site-directed	546:558	arg1	mutagenesis					560:570	site-directed mutagenesis	546:570	site-directed mutagenesis	546:570	We used the approaches of biochemical modification and site-directed mutagenesis to prevent glycosylation.
22159084	6	21	theme	second	751:756	arg1	loop					772:775	a putative large second extracellular loop	734:775	a putative large second extracellular loop	734:775	Deglycosylation experiments with glycosidases indicated that the mature glycosylated form of SLC26A3 exists at the plasma membrane, and a putative large second extracellular loop contains all of the N-linked carbohydrates.
22159084	6	22	theme	glycosylated	670:681	arg1	form					683:686	the mature glycosylated form	659:686	the mature glycosylated form of SLC26A3	659:697	Deglycosylation experiments with glycosidases indicated that the mature glycosylated form of SLC26A3 exists at the plasma membrane, and a putative large second extracellular loop contains all of the N-linked carbohydrates.
22159084	3	23	theme	attached	347:354	arg1	extracellular					375:387	extracellular	375:387	extracellular	375:387	It has been shown that SLC26A3 are glycosylated, with the attached carbohydrate being extracellular and perhaps modulating function.
22159084	3	23	theme	attached	347:354	arg1	carbohydrate					356:367	the attached carbohydrate	343:367	the attached carbohydrate	343:367	It has been shown that SLC26A3 are glycosylated, with the attached carbohydrate being extracellular and perhaps modulating function.
22159084	0	24	theme	anion	104:108	arg1	SLC26A3					120:126	the intestinal anion exchanger SLC26A3	89:126	the intestinal anion exchanger SLC26A3	89:126	Role of N-glycosylation in cell surface expression and protection against proteolysis of the intestinal anion exchanger SLC26A3.
22159084	5	25	theme	mutagenesis	560:570	arg1	approaches					503:512	the approaches	499:512	the approaches of biochemical modification and site-directed mutagenesis	499:570	We used the approaches of biochemical modification and site-directed mutagenesis to prevent glycosylation.
22159084	6	26	theme	large	745:749	arg1	loop					772:775	a putative large second extracellular loop	734:775	a putative large second extracellular loop	734:775	Deglycosylation experiments with glycosidases indicated that the mature glycosylated form of SLC26A3 exists at the plasma membrane, and a putative large second extracellular loop contains all of the N-linked carbohydrates.
22159084	5	27	used	used	494:497	arg2	We					491:492	We	491:492	We	491:492	We used the approaches of biochemical modification and site-directed mutagenesis to prevent glycosylation.
22159084	1	28	theme	/HCO	147:150	arg1	SLC26A3					129:135	SLC26A3	129:135	SLC26A3	129:135	SLC26A3 is a Cl(-)/HCO(3)(-) exchanger that plays a major role in Cl(-) absorption from the intestine.
22159084	1	28	theme	/HCO	147:150	arg1	exchanger					158:166	a Cl(-)/HCO(3)(-) exchanger	140:166	a Cl(-)/HCO(3)(-) exchanger that plays a major role in Cl(-) absorption from the intestine	140:229	SLC26A3 is a Cl(-)/HCO(3)(-) exchanger that plays a major role in Cl(-) absorption from the intestine.
22159084	7	29	theme	intracellular	929:941	arg1	changes					946:952	robust intracellular pH changes	922:952	robust intracellular pH changes	922:952	Deglycosylation of SLC26A3 causes depression of transport activity compared with wild-type, although robust intracellular pH changes were still observed, suggesting that N-glycosylation is not absolutely necessary for transport activity.
22159084	12	30	with	treatment	1497:1505	arg1	trypsin					1512:1518	trypsin	1512:1518	trypsin	1512:1518	While the mature glycosylated SLC26A3 showed little breakdown after treatment with trypsin, deglycosylated SLC26A3 exhibited increased susceptibility to trypsin, suggesting that the oligosaccharides protect SLC26A3 from tryptic digestion.
22159084	6	31	theme	putative	736:743	arg1	loop					772:775	a putative large second extracellular loop	734:775	a putative large second extracellular loop	734:775	Deglycosylation experiments with glycosidases indicated that the mature glycosylated form of SLC26A3 exists at the plasma membrane, and a putative large second extracellular loop contains all of the N-linked carbohydrates.
22159084	13	32	from	degradation	1810:1820	arg1	protection					1782:1791	protection	1782:1791	protection from proteolytic degradation that may contribute to the understanding of pathogenesis of congenital disorders of glycosylation	1782:1918	In conclusion, our data indicate that N-glycosylation of SLC26A3 is important for cell surface expression and for protection from proteolytic degradation that may contribute to the understanding of pathogenesis of congenital disorders of glycosylation.
22159084	12	33	theme	little	1474:1479	arg1	breakdown					1481:1489	little breakdown	1474:1489	little breakdown	1474:1489	While the mature glycosylated SLC26A3 showed little breakdown after treatment with trypsin, deglycosylated SLC26A3 exhibited increased susceptibility to trypsin, suggesting that the oligosaccharides protect SLC26A3 from tryptic digestion.
22159084	13	34	theme	SLC26A3	1725:1731	arg1	N-glycosylation					1706:1720	N-glycosylation	1706:1720	N-glycosylation of SLC26A3	1706:1731	In conclusion, our data indicate that N-glycosylation of SLC26A3 is important for cell surface expression and for protection from proteolytic degradation that may contribute to the understanding of pathogenesis of congenital disorders of glycosylation.
22159084	13	35	theme	surface	1755:1761	arg1	expression					1763:1772	cell surface expression	1750:1772	cell surface expression	1750:1772	In conclusion, our data indicate that N-glycosylation of SLC26A3 is important for cell surface expression and for protection from proteolytic degradation that may contribute to the understanding of pathogenesis of congenital disorders of glycosylation.
22159084	6	36	theme	N-linked	797:804	arg1	carbohydrates					806:818	the N-linked carbohydrates	793:818	the N-linked carbohydrates	793:818	Deglycosylation experiments with glycosidases indicated that the mature glycosylated form of SLC26A3 exists at the plasma membrane, and a putative large second extracellular loop contains all of the N-linked carbohydrates.
22159084	10	37	theme	cell	1295:1298	arg1	processing					1308:1317	cell surface processing	1295:1317	cell surface processing with decreased cell surface expression	1295:1356	Deglycosylation of SLC26A3 causes a defect in cell surface processing with decreased cell surface expression.
22159084	13	38	theme	proteolytic	1798:1808	arg1	degradation					1810:1820	proteolytic degradation	1798:1820	proteolytic degradation that may contribute to the understanding of pathogenesis of congenital disorders of glycosylation	1798:1918	In conclusion, our data indicate that N-glycosylation of SLC26A3 is important for cell surface expression and for protection from proteolytic degradation that may contribute to the understanding of pathogenesis of congenital disorders of glycosylation.
22159084	7	39	theme	pH	943:944	arg1	changes					946:952	robust intracellular pH changes	922:952	robust intracellular pH changes	922:952	Deglycosylation of SLC26A3 causes depression of transport activity compared with wild-type, although robust intracellular pH changes were still observed, suggesting that N-glycosylation is not absolutely necessary for transport activity.
22159084	13	40	theme	congenital	1882:1891	arg1	disorders					1893:1901	congenital disorders	1882:1901	congenital disorders of glycosylation	1882:1918	In conclusion, our data indicate that N-glycosylation of SLC26A3 is important for cell surface expression and for protection from proteolytic degradation that may contribute to the understanding of pathogenesis of congenital disorders of glycosylation.
22159084	0	41	theme	N-glycosylation	8:22	arg1	Role					0:3	Role	0:3	Role of N-glycosylation in cell surface expression	0:49	Role of N-glycosylation in cell surface expression and protection against proteolysis of the intestinal anion exchanger SLC26A3.
22159084	0	41	theme	N-glycosylation	8:22	arg1	protection					55:64	protection	55:64	protection against proteolysis of the intestinal anion exchanger SLC26A3	55:126	Role of N-glycosylation in cell surface expression and protection against proteolysis of the intestinal anion exchanger SLC26A3.
22159084	12	42	theme	tryptic	1649:1655	arg1	digestion					1657:1665	tryptic digestion	1649:1665	tryptic digestion	1649:1665	While the mature glycosylated SLC26A3 showed little breakdown after treatment with trypsin, deglycosylated SLC26A3 exhibited increased susceptibility to trypsin, suggesting that the oligosaccharides protect SLC26A3 from tryptic digestion.
22159084	0	43	theme	SLC26A3	120:126	arg1	proteolysis					74:84	proteolysis	74:84	proteolysis of the intestinal anion exchanger SLC26A3	74:126	Role of N-glycosylation in cell surface expression and protection against proteolysis of the intestinal anion exchanger SLC26A3.
22159084	11	44	theme	tryptic	1410:1416	arg1	digestion					1418:1426	tryptic digestion	1410:1426	tryptic digestion	1410:1426	We also assessed whether SLC26A3 is protected from tryptic digestion.
22159084	13	45	theme	disorders	1893:1901	arg1	pathogenesis					1866:1877	pathogenesis	1866:1877	pathogenesis of congenital disorders of glycosylation	1866:1918	In conclusion, our data indicate that N-glycosylation of SLC26A3 is important for cell surface expression and for protection from proteolytic degradation that may contribute to the understanding of pathogenesis of congenital disorders of glycosylation.
22159084	0	46	theme	surface	32:38	arg1	expression					40:49	cell surface expression	27:49	cell surface expression	27:49	Role of N-glycosylation in cell surface expression and protection against proteolysis of the intestinal anion exchanger SLC26A3.
22159084	10	47	theme	SLC26A3	1268:1274	arg1	Deglycosylation					1249:1263	Deglycosylation	1249:1263	Deglycosylation of SLC26A3	1249:1274	Deglycosylation of SLC26A3 causes a defect in cell surface processing with decreased cell surface expression.
22159084	13	48	theme	pathogenesis	1866:1877	arg1	understanding					1849:1861	the understanding	1845:1861	the understanding of pathogenesis of congenital disorders of glycosylation	1845:1918	In conclusion, our data indicate that N-glycosylation of SLC26A3 is important for cell surface expression and for protection from proteolytic degradation that may contribute to the understanding of pathogenesis of congenital disorders of glycosylation.
22159084	8	49	theme	glycosylation	1071:1083	arg1	sites					1085:1089	glycosylation sites	1071:1089	glycosylation sites	1071:1089	To localize glycosylation sites, we mutated the five consensus sites by replacing asparagine (N) with glutamine.
22159084	0	50	theme	cell	27:30	arg1	expression					40:49	cell surface expression	27:49	cell surface expression	27:49	Role of N-glycosylation in cell surface expression and protection against proteolysis of the intestinal anion exchanger SLC26A3.
22159084	12	51	theme	deglycosylated	1521:1534	arg1	SLC26A3					1536:1542	deglycosylated SLC26A3	1521:1542	deglycosylated SLC26A3	1521:1542	While the mature glycosylated SLC26A3 showed little breakdown after treatment with trypsin, deglycosylated SLC26A3 exhibited increased susceptibility to trypsin, suggesting that the oligosaccharides protect SLC26A3 from tryptic digestion.
22159084	10	52	theme	decreased	1324:1332	arg1	expression					1347:1356	decreased cell surface expression	1324:1356	decreased cell surface expression	1324:1356	Deglycosylation of SLC26A3 causes a defect in cell surface processing with decreased cell surface expression.
22159084	9	53	gly	glycosylated	1211:1222	arg1	SLC26A3					1200:1206	SLC26A3	1200:1206	SLC26A3	1200:1206	Immnoblotting suggests that SLC26A3 is glycosylated at N153, N161, and N165.
22159084	9	53	gly	glycosylated	1211:1222	arg2	N165					1243:1246	N165	1243:1246	N165	1243:1246	Immnoblotting suggests that SLC26A3 is glycosylated at N153, N161, and N165.
22159084	9	53	gly	glycosylated	1211:1222	arg2	N161					1233:1236	N161	1233:1236	N161	1233:1236	Immnoblotting suggests that SLC26A3 is glycosylated at N153, N161, and N165.
22159084	9	53	gly	glycosylated	1211:1222	arg2	N153					1227:1230	N153	1227:1230	N153	1227:1230	Immnoblotting suggests that SLC26A3 is glycosylated at N153, N161, and N165.
22159084	4	54	theme	glycosylation	443:455	arg1	role					435:438	the role	431:438	the role of glycosylation	431:455	However, the role of glycosylation has yet to be clearly determined.
22159084	6	55	theme	extracellular	758:770	arg1	loop					772:775	a putative large second extracellular loop	734:775	a putative large second extracellular loop	734:775	Deglycosylation experiments with glycosidases indicated that the mature glycosylated form of SLC26A3 exists at the plasma membrane, and a putative large second extracellular loop contains all of the N-linked carbohydrates.
22159084	0	56	from	protection	55:64	arg1	expression					40:49	cell surface expression	27:49	cell surface expression	27:49	Role of N-glycosylation in cell surface expression and protection against proteolysis of the intestinal anion exchanger SLC26A3.
22159084	0	57	gly	N-glycosylation	8:22	arg1	surface					32:38	cell surface expression	27:49	cell surface expression	27:49	Role of N-glycosylation in cell surface expression and protection against proteolysis of the intestinal anion exchanger SLC26A3.
22159084	0	57	gly	N-glycosylation	8:22	arg1	cell					27:30	cell surface expression	27:49	cell surface expression	27:49	Role of N-glycosylation in cell surface expression and protection against proteolysis of the intestinal anion exchanger SLC26A3.
22159084	10	58	gly	Deglycosylation	1249:1263	arg1	SLC26A3					1268:1274	SLC26A3	1268:1274	SLC26A3	1268:1274	Deglycosylation of SLC26A3 causes a defect in cell surface processing with decreased cell surface expression.
22159084	2	59	theme	congenital	252:261	arg1	diarrhea					279:286	congenital chloride-losing diarrhea	252:286	congenital chloride-losing diarrhea	252:286	Its mutation causes congenital chloride-losing diarrhea.
22159084	12	60	theme	glycosylated	1446:1457	arg1	SLC26A3					1459:1465	the mature glycosylated SLC26A3	1435:1465	the mature glycosylated SLC26A3	1435:1465	While the mature glycosylated SLC26A3 showed little breakdown after treatment with trypsin, deglycosylated SLC26A3 exhibited increased susceptibility to trypsin, suggesting that the oligosaccharides protect SLC26A3 from tryptic digestion.
22159084	7	61	theme	transport	1039:1047	arg1	activity					1049:1056	transport activity	1039:1056	transport activity	1039:1056	Deglycosylation of SLC26A3 causes depression of transport activity compared with wild-type, although robust intracellular pH changes were still observed, suggesting that N-glycosylation is not absolutely necessary for transport activity.
22159084	6	62	gly	glycosylated	670:681	arg1	SLC26A3					691:697	SLC26A3	691:697	SLC26A3	691:697	Deglycosylation experiments with glycosidases indicated that the mature glycosylated form of SLC26A3 exists at the plasma membrane, and a putative large second extracellular loop contains all of the N-linked carbohydrates.
22159084	6	62	gly	glycosylated	670:681	arg1	form					683:686	the mature glycosylated form	659:686	the mature glycosylated form of SLC26A3	659:697	Deglycosylation experiments with glycosidases indicated that the mature glycosylated form of SLC26A3 exists at the plasma membrane, and a putative large second extracellular loop contains all of the N-linked carbohydrates.
22159084	6	63	theme	plasma	713:718	arg1	membrane					720:727	the plasma membrane	709:727	the plasma membrane	709:727	Deglycosylation experiments with glycosidases indicated that the mature glycosylated form of SLC26A3 exists at the plasma membrane, and a putative large second extracellular loop contains all of the N-linked carbohydrates.
22159084	8	64	theme	consensus	1112:1120	arg1	sites					1122:1126	the five consensus sites	1103:1126	the five consensus sites	1103:1126	To localize glycosylation sites, we mutated the five consensus sites by replacing asparagine (N) with glutamine.
22159084	12	65	gly	deglycosylated	1521:1534	arg1	SLC26A3					1536:1542	deglycosylated SLC26A3	1521:1542	deglycosylated SLC26A3	1521:1542	While the mature glycosylated SLC26A3 showed little breakdown after treatment with trypsin, deglycosylated SLC26A3 exhibited increased susceptibility to trypsin, suggesting that the oligosaccharides protect SLC26A3 from tryptic digestion.
22159084	10	66	from	defect	1285:1290	arg1	processing					1308:1317	cell surface processing	1295:1317	cell surface processing with decreased cell surface expression	1295:1356	Deglycosylation of SLC26A3 causes a defect in cell surface processing with decreased cell surface expression.
22159084	10	67	theme	surface	1300:1306	arg1	processing					1308:1317	cell surface processing	1295:1317	cell surface processing with decreased cell surface expression	1295:1356	Deglycosylation of SLC26A3 causes a defect in cell surface processing with decreased cell surface expression.
22159084	12	68	gly	glycosylated	1446:1457	arg1	SLC26A3					1459:1465	the mature glycosylated SLC26A3	1435:1465	the mature glycosylated SLC26A3	1435:1465	While the mature glycosylated SLC26A3 showed little breakdown after treatment with trypsin, deglycosylated SLC26A3 exhibited increased susceptibility to trypsin, suggesting that the oligosaccharides protect SLC26A3 from tryptic digestion.
22159084	6	69	theme	Deglycosylation	598:612	arg1	experiments					614:624	Deglycosylation experiments	598:624	Deglycosylation experiments with glycosidases	598:642	Deglycosylation experiments with glycosidases indicated that the mature glycosylated form of SLC26A3 exists at the plasma membrane, and a putative large second extracellular loop contains all of the N-linked carbohydrates.
22159084	13	70	theme	glycosylation	1906:1918	arg1	disorders					1893:1901	congenital disorders	1882:1901	congenital disorders of glycosylation	1882:1918	In conclusion, our data indicate that N-glycosylation of SLC26A3 is important for cell surface expression and for protection from proteolytic degradation that may contribute to the understanding of pathogenesis of congenital disorders of glycosylation.
22159084	7	71	theme	transport	869:877	arg1	activity					879:886	transport activity	869:886	transport activity	869:886	Deglycosylation of SLC26A3 causes depression of transport activity compared with wild-type, although robust intracellular pH changes were still observed, suggesting that N-glycosylation is not absolutely necessary for transport activity.
22159084	6	72	theme	mature	663:668	arg1	form					683:686	the mature glycosylated form	659:686	the mature glycosylated form of SLC26A3	659:697	Deglycosylation experiments with glycosidases indicated that the mature glycosylated form of SLC26A3 exists at the plasma membrane, and a putative large second extracellular loop contains all of the N-linked carbohydrates.
22159084	7	73	theme	activity	879:886	arg1	depression					855:864	depression	855:864	depression of transport activity	855:886	Deglycosylation of SLC26A3 causes depression of transport activity compared with wild-type, although robust intracellular pH changes were still observed, suggesting that N-glycosylation is not absolutely necessary for transport activity.
22159084	7	74	theme	robust	922:927	arg1	changes					946:952	robust intracellular pH changes	922:952	robust intracellular pH changes	922:952	Deglycosylation of SLC26A3 causes depression of transport activity compared with wild-type, although robust intracellular pH changes were still observed, suggesting that N-glycosylation is not absolutely necessary for transport activity.
22159084	12	75	theme	mature	1439:1444	arg1	SLC26A3					1459:1465	the mature glycosylated SLC26A3	1435:1465	the mature glycosylated SLC26A3	1435:1465	While the mature glycosylated SLC26A3 showed little breakdown after treatment with trypsin, deglycosylated SLC26A3 exhibited increased susceptibility to trypsin, suggesting that the oligosaccharides protect SLC26A3 from tryptic digestion.
22159084	6	76	theme	SLC26A3	691:697	arg1	form					683:686	the mature glycosylated form	659:686	the mature glycosylated form of SLC26A3	659:697	Deglycosylation experiments with glycosidases indicated that the mature glycosylated form of SLC26A3 exists at the plasma membrane, and a putative large second extracellular loop contains all of the N-linked carbohydrates.
22159084	1	77	theme	Cl	142:143	arg1	SLC26A3					129:135	SLC26A3	129:135	SLC26A3	129:135	SLC26A3 is a Cl(-)/HCO(3)(-) exchanger that plays a major role in Cl(-) absorption from the intestine.
22159084	1	77	theme	Cl	142:143	arg1	exchanger					158:166	a Cl(-)/HCO(3)(-) exchanger	140:166	a Cl(-)/HCO(3)(-) exchanger that plays a major role in Cl(-) absorption from the intestine	140:229	SLC26A3 is a Cl(-)/HCO(3)(-) exchanger that plays a major role in Cl(-) absorption from the intestine.
22159084	13	78	gly	N-glycosylation	1706:1720	arg1	surface					1755:1761	cell surface expression	1750:1772	cell surface expression	1750:1772	In conclusion, our data indicate that N-glycosylation of SLC26A3 is important for cell surface expression and for protection from proteolytic degradation that may contribute to the understanding of pathogenesis of congenital disorders of glycosylation.
22159084	13	78	gly	N-glycosylation	1706:1720	arg1	SLC26A3					1725:1731	SLC26A3	1725:1731	SLC26A3	1725:1731	In conclusion, our data indicate that N-glycosylation of SLC26A3 is important for cell surface expression and for protection from proteolytic degradation that may contribute to the understanding of pathogenesis of congenital disorders of glycosylation.
22159084	13	78	gly	N-glycosylation	1706:1720	arg1	cell					1750:1753	cell surface expression	1750:1772	cell surface expression	1750:1772	In conclusion, our data indicate that N-glycosylation of SLC26A3 is important for cell surface expression and for protection from proteolytic degradation that may contribute to the understanding of pathogenesis of congenital disorders of glycosylation.
25187573	14	0	theme	joint	2442:2446	arg1	movement					2448:2455	natural joint movement	2434:2455	natural joint movement	2434:2455	The identification of these unique properties of lubricin may provide insight into the important low-friction lubricating functions of lubricin during natural joint movement.
25187573	7	1	theme	N-acetylgalactosaminyltransferase	1245:1277	arg1	genes					1279:1283	polypeptide N-acetylgalactosaminyltransferase genes	1233:1283	polypeptide N-acetylgalactosaminyltransferase genes	1233:1283	Investigation of the expression of polypeptide N-acetylgalactosaminyltransferase genes was carried out using cultured primary fibroblast-like synoviocytes, a cell type that expresses lubricin in vivo.
25187573	1	2	gly	glycoprotein	186:197	arg1	glycoprotein					186:197	The lubricative, heavily glycosylated mucin-like synovial glycoprotein lubricin	128:206	The lubricative, heavily glycosylated mucin-like synovial glycoprotein lubricin	128:206	The lubricative, heavily glycosylated mucin-like synovial glycoprotein lubricin has previously been observed to contain glycosylation changes related to rheumatoid and osteoarthritis.
25187573	10	3	theme	glycopeptide	1764:1775	arg1	analysis					1777:1784	The site-specific glycopeptide analysis	1746:1784	The site-specific glycopeptide analysis	1746:1784	The site-specific glycopeptide analysis covered 82% of the protein sequence and showed that lubricin glycosylation displays both micro- and macroheterogeneity.
25187573	1	4	theme	synovial	177:184	arg1	lubricin					199:206	The lubricative, heavily glycosylated mucin-like synovial glycoprotein lubricin	128:206	The lubricative, heavily glycosylated mucin-like synovial glycoprotein lubricin	128:206	The lubricative, heavily glycosylated mucin-like synovial glycoprotein lubricin has previously been observed to contain glycosylation changes related to rheumatoid and osteoarthritis.
25187573	14	5	theme	lubricating	2393:2403	arg1	functions					2405:2413	the important low-friction lubricating functions	2366:2413	the important low-friction lubricating functions of lubricin	2366:2425	The identification of these unique properties of lubricin may provide insight into the important low-friction lubricating functions of lubricin during natural joint movement.
25187573	13	6	theme	charged	2158:2164	arg1	residues					2186:2193	The more positively charged lysine and arginine residues	2138:2193	The more positively charged lysine and arginine residues in the N and C termini	2138:2216	The more positively charged lysine and arginine residues in the N and C termini suggest that synovial lubricin exists as an amphoteric molecule.
25187573	5	7	gly	glycosylated	1013:1024	arg1	residues					925:932	adjacent threonine residues	906:932	adjacent threonine residues within the central STP-rich region	906:967	This showed that adjacent threonine residues within the central STP-rich region could be simultaneously and/or individually glycosylated.
25187573	4	8	theme	liquid	652:657	arg1	spectrometry					686:697	liquid chromatography-tandem mass spectrometry	652:697	a liquid chromatography-tandem mass spectrometry approach	650:706	In this study, using a liquid chromatography-tandem mass spectrometry approach, employing both collision-induced and electron-transfer dissociation fragmentation methods, we identified 185 O-glycopeptides within the STP-rich domain of human synovial lubricin.
25187573	14	9	theme	important	2370:2378	arg1	functions					2405:2413	the important low-friction lubricating functions	2366:2413	the important low-friction lubricating functions of lubricin	2366:2425	The identification of these unique properties of lubricin may provide insight into the important low-friction lubricating functions of lubricin during natural joint movement.
25187573	0	10	theme	glycopeptide	105:116	arg1	analysis					118:125	site-specific glycopeptide analysis	91:125	site-specific glycopeptide analysis	91:125	The O-glycomap of lubricin, a novel mucin responsible for joint lubrication, identified by site-specific glycopeptide analysis.
25187573	5	11	theme	threonine	915:923	arg1	residues					925:932	adjacent threonine residues	906:932	adjacent threonine residues within the central STP-rich region	906:967	This showed that adjacent threonine residues within the central STP-rich region could be simultaneously and/or individually glycosylated.
25187573	4	12	theme	dissociation	764:775	arg1	methods					791:797	both collision-induced and electron-transfer dissociation fragmentation methods	719:797	methods	791:797	In this study, using a liquid chromatography-tandem mass spectrometry approach, employing both collision-induced and electron-transfer dissociation fragmentation methods, we identified 185 O-glycopeptides within the STP-rich domain of human synovial lubricin.
25187573	4	13	theme	mass	681:684	arg1	spectrometry					686:697	liquid chromatography-tandem mass spectrometry	652:697	a liquid chromatography-tandem mass spectrometry approach	650:706	In this study, using a liquid chromatography-tandem mass spectrometry approach, employing both collision-induced and electron-transfer dissociation fragmentation methods, we identified 185 O-glycopeptides within the STP-rich domain of human synovial lubricin.
25187573	6	14	theme	core	1042:1045	arg1	structures					1049:1058	core 1 structures	1042:1058	core 1 structures responsible for biolubrication	1042:1089	In addition to core 1 structures responsible for biolubrication, core 2 O-glycopeptides were also identified, indicating that lubricin glycosylation may have other roles.
25187573	4	15	theme	fragmentation	777:789	arg1	methods					791:797	both collision-induced and electron-transfer dissociation fragmentation methods	719:797	methods	791:797	In this study, using a liquid chromatography-tandem mass spectrometry approach, employing both collision-induced and electron-transfer dissociation fragmentation methods, we identified 185 O-glycopeptides within the STP-rich domain of human synovial lubricin.
25187573	10	16	theme	sequence	1813:1820	arg1	%					1796:1796	82%	1794:1796	82% of the protein sequence	1794:1820	The site-specific glycopeptide analysis covered 82% of the protein sequence and showed that lubricin glycosylation displays both micro- and macroheterogeneity.
25187573	10	16	theme	sequence	1813:1820	arg1	sequence					1813:1820	the protein sequence	1801:1820	the protein sequence	1801:1820	The site-specific glycopeptide analysis covered 82% of the protein sequence and showed that lubricin glycosylation displays both micro- and macroheterogeneity.
25187573	9	17	theme	transferase	1681:1691	arg1	genes					1693:1697	transferase genes	1681:1697	transferase genes important for the O-glycosylation of lubricin	1681:1743	This suggests that there is a unique combination of transferase genes important for the O-glycosylation of lubricin.
25187573	6	18	dep	structures	1049:1058	arg1	addition					1030:1037	addition	1030:1037	addition	1030:1037	In addition to core 1 structures responsible for biolubrication, core 2 O-glycopeptides were also identified, indicating that lubricin glycosylation may have other roles.
25187573	9	19	theme	important	1699:1707	arg1	genes					1693:1697	transferase genes	1681:1697	transferase genes important for the O-glycosylation of lubricin	1681:1743	This suggests that there is a unique combination of transferase genes important for the O-glycosylation of lubricin.
25187573	8	20	theme	understood	1460:1469	arg1	N-acetylgalactosaminyltransferase					1483:1515	the less understood polypeptide N-acetylgalactosaminyltransferase 15 and 5	1451:1524	N-acetylgalactosaminyltransferase	1483:1515	This analysis showed high mRNA expression levels of the less understood polypeptide N-acetylgalactosaminyltransferase 15 and 5 in addition to the ubiquitously expressed polypeptide N-acetylgalactosaminyltransferase 1 and 2 genes.
25187573	0	21	theme	responsible	42:52	arg1	lubricin					18:25	lubricin	18:25	lubricin	18:25	The O-glycomap of lubricin, a novel mucin responsible for joint lubrication, identified by site-specific glycopeptide analysis.
25187573	0	21	theme	responsible	42:52	arg1	mucin					36:40	a novel mucin	28:40	a novel mucin responsible for joint lubrication	28:74	The O-glycomap of lubricin, a novel mucin responsible for joint lubrication, identified by site-specific glycopeptide analysis.
25187573	13	22	theme	amphoteric	2262:2271	arg1	molecule					2273:2280	an amphoteric molecule	2259:2280	an amphoteric molecule	2259:2280	The more positively charged lysine and arginine residues in the N and C termini suggest that synovial lubricin exists as an amphoteric molecule.
25187573	6	23	contain	have	1180:1183	arg2	roles					1191:1195	other roles	1185:1195	other roles	1185:1195	In addition to core 1 structures responsible for biolubrication, core 2 O-glycopeptides were also identified, indicating that lubricin glycosylation may have other roles.
25187573	6	23	contain	have	1180:1183	arg1	glycosylation					1162:1174	lubricin glycosylation	1153:1174	lubricin glycosylation	1153:1174	In addition to core 1 structures responsible for biolubrication, core 2 O-glycopeptides were also identified, indicating that lubricin glycosylation may have other roles.
25187573	4	24	theme	electron-transfer	746:762	arg1	methods					791:797	both collision-induced and electron-transfer dissociation fragmentation methods	719:797	methods	791:797	In this study, using a liquid chromatography-tandem mass spectrometry approach, employing both collision-induced and electron-transfer dissociation fragmentation methods, we identified 185 O-glycopeptides within the STP-rich domain of human synovial lubricin.
25187573	0	25	theme	joint	58:62	arg1	lubrication					64:74	joint lubrication	58:74	joint lubrication	58:74	The O-glycomap of lubricin, a novel mucin responsible for joint lubrication, identified by site-specific glycopeptide analysis.
25187573	12	26	theme	negative	2121:2128	arg1	charge					2130:2135	the domain a negative charge	2108:2135	the domain a negative charge	2108:2135	These glycosylation sites were focused in the central STP-rich region, giving the domain a negative charge.
25187573	7	27	theme	cell	1356:1359	arg1	synoviocytes					1340:1351	cultured primary fibroblast-like synoviocytes	1307:1351	cultured primary fibroblast-like synoviocytes	1307:1351	Investigation of the expression of polypeptide N-acetylgalactosaminyltransferase genes was carried out using cultured primary fibroblast-like synoviocytes, a cell type that expresses lubricin in vivo.
25187573	7	27	theme	cell	1356:1359	arg1	type					1361:1364	a cell type	1354:1364	a cell type that expresses lubricin in vivo	1354:1396	Investigation of the expression of polypeptide N-acetylgalactosaminyltransferase genes was carried out using cultured primary fibroblast-like synoviocytes, a cell type that expresses lubricin in vivo.
25187573	14	28	theme	unique	2311:2316	arg1	properties					2318:2327	these unique properties	2305:2327	these unique properties of lubricin	2305:2339	The identification of these unique properties of lubricin may provide insight into the important low-friction lubricating functions of lubricin during natural joint movement.
25187573	11	29	gly	O-glycosylation	1970:1984	arg2	O-glycosylation					1970:1984	O-glycosylation	1970:1984	O-glycosylation	1970:1984	The density of glycosylation was shown to be high: 168 sites of O-glycosylation, predominately sialylated, were identified.
25187573	11	29	gly	O-glycosylation	1970:1984	arg2	sites					1961:1965	168 sites	1957:1965	168 sites	1957:1965	The density of glycosylation was shown to be high: 168 sites of O-glycosylation, predominately sialylated, were identified.
25187573	4	30	gly	O-glycopeptides	818:832	arg2	O-glycopeptides					818:832	185 O-glycopeptides	814:832	185 O-glycopeptides	814:832	In this study, using a liquid chromatography-tandem mass spectrometry approach, employing both collision-induced and electron-transfer dissociation fragmentation methods, we identified 185 O-glycopeptides within the STP-rich domain of human synovial lubricin.
25187573	6	31	theme	other	1185:1189	arg1	roles					1191:1195	other roles	1185:1195	other roles	1185:1195	In addition to core 1 structures responsible for biolubrication, core 2 O-glycopeptides were also identified, indicating that lubricin glycosylation may have other roles.
25187573	9	32	gly	O-glycosylation	1717:1731	arg1	lubricin					1736:1743	lubricin	1736:1743	lubricin	1736:1743	This suggests that there is a unique combination of transferase genes important for the O-glycosylation of lubricin.
25187573	7	33	theme	fibroblast-like	1324:1338	arg1	synoviocytes					1340:1351	cultured primary fibroblast-like synoviocytes	1307:1351	cultured primary fibroblast-like synoviocytes	1307:1351	Investigation of the expression of polypeptide N-acetylgalactosaminyltransferase genes was carried out using cultured primary fibroblast-like synoviocytes, a cell type that expresses lubricin in vivo.
25187573	7	33	theme	fibroblast-like	1324:1338	arg1	type					1361:1364	a cell type	1354:1364	a cell type that expresses lubricin in vivo	1354:1396	Investigation of the expression of polypeptide N-acetylgalactosaminyltransferase genes was carried out using cultured primary fibroblast-like synoviocytes, a cell type that expresses lubricin in vivo.
25187573	12	34	theme	domain	2112:2117	arg1	charge					2130:2135	the domain a negative charge	2108:2135	the domain a negative charge	2108:2135	These glycosylation sites were focused in the central STP-rich region, giving the domain a negative charge.
25187573	1	35	dep	lubricative	132:142	arg1	glycosylated					153:164	glycosylated	153:164	glycosylated	153:164	The lubricative, heavily glycosylated mucin-like synovial glycoprotein lubricin has previously been observed to contain glycosylation changes related to rheumatoid and osteoarthritis.
25187573	7	36	theme	cultured	1307:1314	arg1	synoviocytes					1340:1351	cultured primary fibroblast-like synoviocytes	1307:1351	cultured primary fibroblast-like synoviocytes	1307:1351	Investigation of the expression of polypeptide N-acetylgalactosaminyltransferase genes was carried out using cultured primary fibroblast-like synoviocytes, a cell type that expresses lubricin in vivo.
25187573	7	36	theme	cultured	1307:1314	arg1	type					1361:1364	a cell type	1354:1364	a cell type that expresses lubricin in vivo	1354:1396	Investigation of the expression of polypeptide N-acetylgalactosaminyltransferase genes was carried out using cultured primary fibroblast-like synoviocytes, a cell type that expresses lubricin in vivo.
25187573	12	37	theme	central	2076:2082	arg1	region					2093:2098	the central STP-rich region	2072:2098	the central STP-rich region	2072:2098	These glycosylation sites were focused in the central STP-rich region, giving the domain a negative charge.
25187573	6	38	theme	lubricin	1153:1160	arg1	glycosylation					1162:1174	lubricin glycosylation	1153:1174	lubricin glycosylation	1153:1174	In addition to core 1 structures responsible for biolubrication, core 2 O-glycopeptides were also identified, indicating that lubricin glycosylation may have other roles.
25187573	11	39	theme	glycosylation	1921:1933	arg1	high					1951:1954	high	1951:1954	high	1951:1954	The density of glycosylation was shown to be high: 168 sites of O-glycosylation, predominately sialylated, were identified.
25187573	11	39	theme	glycosylation	1921:1933	arg1	density					1910:1916	The density	1906:1916	The density of glycosylation	1906:1933	The density of glycosylation was shown to be high: 168 sites of O-glycosylation, predominately sialylated, were identified.
25187573	8	40	theme	polypeptide	1568:1578	arg1	N-acetylgalactosaminyltransferase					1580:1612	polypeptide N-acetylgalactosaminyltransferase 1 and 2	1568:1620	N-acetylgalactosaminyltransferase	1580:1612	This analysis showed high mRNA expression levels of the less understood polypeptide N-acetylgalactosaminyltransferase 15 and 5 in addition to the ubiquitously expressed polypeptide N-acetylgalactosaminyltransferase 1 and 2 genes.
25187573	2	41	theme	pathological	432:443	arg1	mechanisms					445:454	the pathological mechanisms	428:454	the pathological mechanisms involved in these diseases	428:481	Thus, a site-specific investigation of the glycosylation of lubricin was undertaken, in order to further understand the pathological mechanisms involved in these diseases.
25187573	6	42	gly	O-glycopeptides	1099:1113	arg2	O-glycopeptides					1099:1113	core 2 O-glycopeptides	1092:1113	core 2 O-glycopeptides	1092:1113	In addition to core 1 structures responsible for biolubrication, core 2 O-glycopeptides were also identified, indicating that lubricin glycosylation may have other roles.
25187573	2	43	theme	lubricin	372:379	arg1	glycosylation					355:367	the glycosylation	351:367	the glycosylation of lubricin	351:379	Thus, a site-specific investigation of the glycosylation of lubricin was undertaken, in order to further understand the pathological mechanisms involved in these diseases.
25187573	0	44	theme	novel	30:34	arg1	lubricin					18:25	lubricin	18:25	lubricin	18:25	The O-glycomap of lubricin, a novel mucin responsible for joint lubrication, identified by site-specific glycopeptide analysis.
25187573	0	44	theme	novel	30:34	arg1	mucin					36:40	a novel mucin	28:40	a novel mucin responsible for joint lubrication	28:74	The O-glycomap of lubricin, a novel mucin responsible for joint lubrication, identified by site-specific glycopeptide analysis.
25187573	8	45	theme	2	1620:1620	arg1	genes					1622:1626	the ubiquitously expressed polypeptide N-acetylgalactosaminyltransferase 1 and 2 genes	1541:1626	the ubiquitously expressed polypeptide N-acetylgalactosaminyltransferase 1 and 2 genes	1541:1626	This analysis showed high mRNA expression levels of the less understood polypeptide N-acetylgalactosaminyltransferase 15 and 5 in addition to the ubiquitously expressed polypeptide N-acetylgalactosaminyltransferase 1 and 2 genes.
25187573	13	46	theme	synovial	2231:2238	arg1	lubricin					2240:2247	synovial lubricin	2231:2247	synovial lubricin	2231:2247	The more positively charged lysine and arginine residues in the N and C termini suggest that synovial lubricin exists as an amphoteric molecule.
25187573	2	47	theme	glycosylation	355:367	arg1	investigation					334:346	a site-specific investigation	318:346	a site-specific investigation of the glycosylation of lubricin	318:379	Thus, a site-specific investigation of the glycosylation of lubricin was undertaken, in order to further understand the pathological mechanisms involved in these diseases.
25187573	10	48	theme	site-specific	1750:1762	arg1	analysis					1777:1784	The site-specific glycopeptide analysis	1746:1784	The site-specific glycopeptide analysis	1746:1784	The site-specific glycopeptide analysis covered 82% of the protein sequence and showed that lubricin glycosylation displays both micro- and macroheterogeneity.
25187573	4	49	theme	lubricin	879:886	arg1	lubricin					879:886	human synovial lubricin	864:886	human synovial lubricin	864:886	In this study, using a liquid chromatography-tandem mass spectrometry approach, employing both collision-induced and electron-transfer dissociation fragmentation methods, we identified 185 O-glycopeptides within the STP-rich domain of human synovial lubricin.
25187573	4	49	theme	lubricin	879:886	arg1	domain					854:859	the STP-rich domain	841:859	the STP-rich domain of human synovial lubricin	841:886	In this study, using a liquid chromatography-tandem mass spectrometry approach, employing both collision-induced and electron-transfer dissociation fragmentation methods, we identified 185 O-glycopeptides within the STP-rich domain of human synovial lubricin.
25187573	13	50	theme	N	2202:2202	arg1	termini					2210:2216	the N and C termini	2198:2216	termini	2210:2216	The more positively charged lysine and arginine residues in the N and C termini suggest that synovial lubricin exists as an amphoteric molecule.
25187573	5	51	theme	central	945:951	arg1	region					962:967	the central STP-rich region	941:967	the central STP-rich region	941:967	This showed that adjacent threonine residues within the central STP-rich region could be simultaneously and/or individually glycosylated.
25187573	1	52	theme	glycosylation	248:260	arg1	changes					262:268	glycosylation changes	248:268	glycosylation changes related to rheumatoid and osteoarthritis	248:309	The lubricative, heavily glycosylated mucin-like synovial glycoprotein lubricin has previously been observed to contain glycosylation changes related to rheumatoid and osteoarthritis.
25187573	12	53	gly	glycosylation	2036:2048	arg2	sites					2050:2054	These glycosylation sites	2030:2054	These glycosylation sites	2030:2054	These glycosylation sites were focused in the central STP-rich region, giving the domain a negative charge.
25187573	7	54	theme	polypeptide	1233:1243	arg1	genes					1279:1283	polypeptide N-acetylgalactosaminyltransferase genes	1233:1283	polypeptide N-acetylgalactosaminyltransferase genes	1233:1283	Investigation of the expression of polypeptide N-acetylgalactosaminyltransferase genes was carried out using cultured primary fibroblast-like synoviocytes, a cell type that expresses lubricin in vivo.
25187573	13	55	theme	C	2208:2208	arg1	termini					2210:2216	the N and C termini	2198:2216	termini	2210:2216	The more positively charged lysine and arginine residues in the N and C termini suggest that synovial lubricin exists as an amphoteric molecule.
25187573	1	56	theme	related	270:276	arg1	changes					262:268	glycosylation changes	248:268	glycosylation changes related to rheumatoid and osteoarthritis	248:309	The lubricative, heavily glycosylated mucin-like synovial glycoprotein lubricin has previously been observed to contain glycosylation changes related to rheumatoid and osteoarthritis.
25187573	14	57	theme	natural	2434:2440	arg1	movement					2448:2455	natural joint movement	2434:2455	natural joint movement	2434:2455	The identification of these unique properties of lubricin may provide insight into the important low-friction lubricating functions of lubricin during natural joint movement.
25187573	7	58	theme	expression	1219:1228	arg1	Investigation					1198:1210	Investigation	1198:1210	Investigation of the expression of polypeptide N-acetylgalactosaminyltransferase genes	1198:1283	Investigation of the expression of polypeptide N-acetylgalactosaminyltransferase genes was carried out using cultured primary fibroblast-like synoviocytes, a cell type that expresses lubricin in vivo.
25187573	13	59	theme	arginine	2177:2184	arg1	residues					2186:2193	The more positively charged lysine and arginine residues	2138:2193	The more positively charged lysine and arginine residues in the N and C termini	2138:2216	The more positively charged lysine and arginine residues in the N and C termini suggest that synovial lubricin exists as an amphoteric molecule.
25187573	8	60	theme	N-acetylgalactosaminyltransferase	1483:1515	arg1	levels					1441:1446	high mRNA expression levels	1420:1446	high mRNA expression levels of the less understood polypeptide N-acetylgalactosaminyltransferase 15 and 5	1420:1524	This analysis showed high mRNA expression levels of the less understood polypeptide N-acetylgalactosaminyltransferase 15 and 5 in addition to the ubiquitously expressed polypeptide N-acetylgalactosaminyltransferase 1 and 2 genes.
25187573	14	61	theme	lubricin	2418:2425	arg1	functions					2405:2413	the important low-friction lubricating functions	2366:2413	the important low-friction lubricating functions of lubricin	2366:2425	The identification of these unique properties of lubricin may provide insight into the important low-friction lubricating functions of lubricin during natural joint movement.
25187573	3	62	theme	tandem	570:575	arg1	EPAPTTPK					586:593	EPAPTTPK	586:593	EPAPTTPK	586:593	Lubricin contains an serine/threonine/proline (STP)-rich domain composed of imperfect tandem repeats (EPAPTTPK), the target for O-glycosylation.
25187573	3	62	theme	tandem	570:575	arg1	repeats					577:583	imperfect tandem repeats	560:583	imperfect tandem repeats (EPAPTTPK)	560:594	Lubricin contains an serine/threonine/proline (STP)-rich domain composed of imperfect tandem repeats (EPAPTTPK), the target for O-glycosylation.
25187573	1	63	theme	glycoprotein	186:197	arg1	lubricin					199:206	The lubricative, heavily glycosylated mucin-like synovial glycoprotein lubricin	128:206	The lubricative, heavily glycosylated mucin-like synovial glycoprotein lubricin	128:206	The lubricative, heavily glycosylated mucin-like synovial glycoprotein lubricin has previously been observed to contain glycosylation changes related to rheumatoid and osteoarthritis.
25187573	1	64	theme	mucin-like	166:175	arg1	lubricin					199:206	The lubricative, heavily glycosylated mucin-like synovial glycoprotein lubricin	128:206	The lubricative, heavily glycosylated mucin-like synovial glycoprotein lubricin	128:206	The lubricative, heavily glycosylated mucin-like synovial glycoprotein lubricin has previously been observed to contain glycosylation changes related to rheumatoid and osteoarthritis.
25187573	4	65	theme	spectrometry	686:697	arg1	approach					699:706	a liquid chromatography-tandem mass spectrometry approach	650:706	a liquid chromatography-tandem mass spectrometry approach	650:706	In this study, using a liquid chromatography-tandem mass spectrometry approach, employing both collision-induced and electron-transfer dissociation fragmentation methods, we identified 185 O-glycopeptides within the STP-rich domain of human synovial lubricin.
25187573	10	66	theme	protein	1805:1811	arg1	sequence					1813:1820	the protein sequence	1801:1820	the protein sequence	1801:1820	The site-specific glycopeptide analysis covered 82% of the protein sequence and showed that lubricin glycosylation displays both micro- and macroheterogeneity.
25187573	5	67	theme	STP-rich	953:960	arg1	region					962:967	the central STP-rich region	941:967	the central STP-rich region	941:967	This showed that adjacent threonine residues within the central STP-rich region could be simultaneously and/or individually glycosylated.
25187573	14	68	theme	low-friction	2380:2391	arg1	functions					2405:2413	the important low-friction lubricating functions	2366:2413	the important low-friction lubricating functions of lubricin	2366:2425	The identification of these unique properties of lubricin may provide insight into the important low-friction lubricating functions of lubricin during natural joint movement.
25187573	13	69	theme	lysine	2166:2171	arg1	residues					2186:2193	The more positively charged lysine and arginine residues	2138:2193	The more positively charged lysine and arginine residues in the N and C termini	2138:2216	The more positively charged lysine and arginine residues in the N and C termini suggest that synovial lubricin exists as an amphoteric molecule.
25187573	2	70	theme	site-specific	320:332	arg1	investigation					334:346	a site-specific investigation	318:346	a site-specific investigation of the glycosylation of lubricin	318:379	Thus, a site-specific investigation of the glycosylation of lubricin was undertaken, in order to further understand the pathological mechanisms involved in these diseases.
25187573	5	71	theme	adjacent	906:913	arg1	residues					925:932	adjacent threonine residues	906:932	adjacent threonine residues within the central STP-rich region	906:967	This showed that adjacent threonine residues within the central STP-rich region could be simultaneously and/or individually glycosylated.
25187573	6	72	theme	responsible	1060:1070	arg1	structures					1049:1058	core 1 structures	1042:1058	core 1 structures responsible for biolubrication	1042:1089	In addition to core 1 structures responsible for biolubrication, core 2 O-glycopeptides were also identified, indicating that lubricin glycosylation may have other roles.
25187573	3	73	contain	contains	493:500	arg2	target					601:606	the target	597:606	the target for O-glycosylation	597:626	Lubricin contains an serine/threonine/proline (STP)-rich domain composed of imperfect tandem repeats (EPAPTTPK), the target for O-glycosylation.
25187573	3	73	contain	contains	493:500	arg2	domain					541:546	an serine/threonine/proline (STP)-rich domain	502:546	an serine/threonine/proline (STP)-rich domain composed of imperfect tandem repeats (EPAPTTPK)	502:594	Lubricin contains an serine/threonine/proline (STP)-rich domain composed of imperfect tandem repeats (EPAPTTPK), the target for O-glycosylation.
25187573	3	73	contain	contains	493:500	arg1	Lubricin					484:491	Lubricin	484:491	Lubricin	484:491	Lubricin contains an serine/threonine/proline (STP)-rich domain composed of imperfect tandem repeats (EPAPTTPK), the target for O-glycosylation.
25187573	13	74	from	residues	2186:2193	arg1	termini					2210:2216	the N and C termini	2198:2216	termini	2210:2216	The more positively charged lysine and arginine residues in the N and C termini suggest that synovial lubricin exists as an amphoteric molecule.
25187573	9	75	theme	unique	1659:1664	arg1	combination					1666:1676	a unique combination	1657:1676	a unique combination of transferase genes important for the O-glycosylation of lubricin	1657:1743	This suggests that there is a unique combination of transferase genes important for the O-glycosylation of lubricin.
25187573	4	76	theme	chromatography-tandem	659:679	arg1	spectrometry					686:697	liquid chromatography-tandem mass spectrometry	652:697	a liquid chromatography-tandem mass spectrometry approach	650:706	In this study, using a liquid chromatography-tandem mass spectrometry approach, employing both collision-induced and electron-transfer dissociation fragmentation methods, we identified 185 O-glycopeptides within the STP-rich domain of human synovial lubricin.
25187573	1	77	contain	contain	240:246	arg1	lubricin					199:206	The lubricative, heavily glycosylated mucin-like synovial glycoprotein lubricin	128:206	The lubricative, heavily glycosylated mucin-like synovial glycoprotein lubricin	128:206	The lubricative, heavily glycosylated mucin-like synovial glycoprotein lubricin has previously been observed to contain glycosylation changes related to rheumatoid and osteoarthritis.
25187573	1	77	contain	contain	240:246	arg2	changes					262:268	glycosylation changes	248:268	glycosylation changes related to rheumatoid and osteoarthritis	248:309	The lubricative, heavily glycosylated mucin-like synovial glycoprotein lubricin has previously been observed to contain glycosylation changes related to rheumatoid and osteoarthritis.
25187573	0	78	gly	glycopeptide	105:116	arg2	glycopeptide					105:116	site-specific glycopeptide analysis	91:125	site-specific glycopeptide analysis	91:125	The O-glycomap of lubricin, a novel mucin responsible for joint lubrication, identified by site-specific glycopeptide analysis.
25187573	10	79	gly	glycopeptide	1764:1775	arg2	glycopeptide					1764:1775	The site-specific glycopeptide analysis	1746:1784	The site-specific glycopeptide analysis	1746:1784	The site-specific glycopeptide analysis covered 82% of the protein sequence and showed that lubricin glycosylation displays both micro- and macroheterogeneity.
25187573	8	80	theme	expression	1430:1439	arg1	levels					1441:1446	high mRNA expression levels	1420:1446	high mRNA expression levels of the less understood polypeptide N-acetylgalactosaminyltransferase 15 and 5	1420:1524	This analysis showed high mRNA expression levels of the less understood polypeptide N-acetylgalactosaminyltransferase 15 and 5 in addition to the ubiquitously expressed polypeptide N-acetylgalactosaminyltransferase 1 and 2 genes.
25187573	4	81	theme	human	864:868	arg1	lubricin					879:886	human synovial lubricin	864:886	human synovial lubricin	864:886	In this study, using a liquid chromatography-tandem mass spectrometry approach, employing both collision-induced and electron-transfer dissociation fragmentation methods, we identified 185 O-glycopeptides within the STP-rich domain of human synovial lubricin.
25187573	9	82	theme	genes	1693:1697	arg1	combination					1666:1676	a unique combination	1657:1676	a unique combination of transferase genes important for the O-glycosylation of lubricin	1657:1743	This suggests that there is a unique combination of transferase genes important for the O-glycosylation of lubricin.
25187573	1	83	theme	lubricative	132:142	arg1	lubricin					199:206	The lubricative, heavily glycosylated mucin-like synovial glycoprotein lubricin	128:206	The lubricative, heavily glycosylated mucin-like synovial glycoprotein lubricin	128:206	The lubricative, heavily glycosylated mucin-like synovial glycoprotein lubricin has previously been observed to contain glycosylation changes related to rheumatoid and osteoarthritis.
25187573	2	84	gly	glycosylation	355:367	arg1	lubricin					372:379	lubricin	372:379	lubricin	372:379	Thus, a site-specific investigation of the glycosylation of lubricin was undertaken, in order to further understand the pathological mechanisms involved in these diseases.
25187573	14	85	theme	lubricin	2332:2339	arg1	properties					2318:2327	these unique properties	2305:2327	these unique properties of lubricin	2305:2339	The identification of these unique properties of lubricin may provide insight into the important low-friction lubricating functions of lubricin during natural joint movement.
25187573	8	86	theme	polypeptide	1471:1481	arg1	N-acetylgalactosaminyltransferase					1483:1515	the less understood polypeptide N-acetylgalactosaminyltransferase 15 and 5	1451:1524	N-acetylgalactosaminyltransferase	1483:1515	This analysis showed high mRNA expression levels of the less understood polypeptide N-acetylgalactosaminyltransferase 15 and 5 in addition to the ubiquitously expressed polypeptide N-acetylgalactosaminyltransferase 1 and 2 genes.
25187573	9	87	theme	lubricin	1736:1743	arg1	O-glycosylation					1717:1731	the O-glycosylation	1713:1731	the O-glycosylation of lubricin	1713:1743	This suggests that there is a unique combination of transferase genes important for the O-glycosylation of lubricin.
25187573	6	88	theme	core	1092:1095	arg1	O-glycopeptides					1099:1113	core 2 O-glycopeptides	1092:1113	core 2 O-glycopeptides	1092:1113	In addition to core 1 structures responsible for biolubrication, core 2 O-glycopeptides were also identified, indicating that lubricin glycosylation may have other roles.
25187573	14	89	theme	properties	2318:2327	arg1	identification					2287:2300	The identification	2283:2300	The identification of these unique properties of lubricin	2283:2339	The identification of these unique properties of lubricin may provide insight into the important low-friction lubricating functions of lubricin during natural joint movement.
25187573	11	90	theme	O-glycosylation	1970:1984	arg1	O-glycosylation					1970:1984	O-glycosylation	1970:1984	O-glycosylation	1970:1984	The density of glycosylation was shown to be high: 168 sites of O-glycosylation, predominately sialylated, were identified.
25187573	11	90	theme	O-glycosylation	1970:1984	arg1	sites					1961:1965	168 sites	1957:1965	168 sites	1957:1965	The density of glycosylation was shown to be high: 168 sites of O-glycosylation, predominately sialylated, were identified.
25187573	0	91	theme	site-specific	91:103	arg1	analysis					118:125	site-specific glycopeptide analysis	91:125	site-specific glycopeptide analysis	91:125	The O-glycomap of lubricin, a novel mucin responsible for joint lubrication, identified by site-specific glycopeptide analysis.
25187573	8	92	theme	5	1524:1524	arg1	levels					1441:1446	high mRNA expression levels	1420:1446	high mRNA expression levels of the less understood polypeptide N-acetylgalactosaminyltransferase 15 and 5	1420:1524	This analysis showed high mRNA expression levels of the less understood polypeptide N-acetylgalactosaminyltransferase 15 and 5 in addition to the ubiquitously expressed polypeptide N-acetylgalactosaminyltransferase 1 and 2 genes.
25187573	7	93	theme	primary	1316:1322	arg1	synoviocytes					1340:1351	cultured primary fibroblast-like synoviocytes	1307:1351	cultured primary fibroblast-like synoviocytes	1307:1351	Investigation of the expression of polypeptide N-acetylgalactosaminyltransferase genes was carried out using cultured primary fibroblast-like synoviocytes, a cell type that expresses lubricin in vivo.
25187573	7	93	theme	primary	1316:1322	arg1	type					1361:1364	a cell type	1354:1364	a cell type that expresses lubricin in vivo	1354:1396	Investigation of the expression of polypeptide N-acetylgalactosaminyltransferase genes was carried out using cultured primary fibroblast-like synoviocytes, a cell type that expresses lubricin in vivo.
25187573	12	94	theme	a	2119:2119	arg1	charge					2130:2135	the domain a negative charge	2108:2135	the domain a negative charge	2108:2135	These glycosylation sites were focused in the central STP-rich region, giving the domain a negative charge.
25187573	10	95	theme	lubricin	1838:1845	arg1	glycosylation					1847:1859	lubricin glycosylation	1838:1859	lubricin glycosylation	1838:1859	The site-specific glycopeptide analysis covered 82% of the protein sequence and showed that lubricin glycosylation displays both micro- and macroheterogeneity.
25187573	0	96	theme	lubricin	18:25	arg1	O-glycomap					4:13	The O-glycomap	0:13	The O-glycomap of lubricin, a novel mucin responsible for joint lubrication,	0:75	The O-glycomap of lubricin, a novel mucin responsible for joint lubrication, identified by site-specific glycopeptide analysis.
25187573	2	97	dep	understand	417:426	arg1	to					406:407	to	406:407	to	406:407	Thus, a site-specific investigation of the glycosylation of lubricin was undertaken, in order to further understand the pathological mechanisms involved in these diseases.
25187573	12	98	theme	STP-rich	2084:2091	arg1	region					2093:2098	the central STP-rich region	2072:2098	the central STP-rich region	2072:2098	These glycosylation sites were focused in the central STP-rich region, giving the domain a negative charge.
25187573	8	99	theme	mRNA	1425:1428	arg1	levels					1441:1446	high mRNA expression levels	1420:1446	high mRNA expression levels of the less understood polypeptide N-acetylgalactosaminyltransferase 15 and 5	1420:1524	This analysis showed high mRNA expression levels of the less understood polypeptide N-acetylgalactosaminyltransferase 15 and 5 in addition to the ubiquitously expressed polypeptide N-acetylgalactosaminyltransferase 1 and 2 genes.
25187573	8	100	theme	expressed	1558:1566	arg1	genes					1622:1626	the ubiquitously expressed polypeptide N-acetylgalactosaminyltransferase 1 and 2 genes	1541:1626	the ubiquitously expressed polypeptide N-acetylgalactosaminyltransferase 1 and 2 genes	1541:1626	This analysis showed high mRNA expression levels of the less understood polypeptide N-acetylgalactosaminyltransferase 15 and 5 in addition to the ubiquitously expressed polypeptide N-acetylgalactosaminyltransferase 1 and 2 genes.
25187573	7	101	theme	genes	1279:1283	arg1	expression					1219:1228	the expression	1215:1228	the expression of polypeptide N-acetylgalactosaminyltransferase genes	1215:1283	Investigation of the expression of polypeptide N-acetylgalactosaminyltransferase genes was carried out using cultured primary fibroblast-like synoviocytes, a cell type that expresses lubricin in vivo.
25187573	8	102	theme	N-acetylgalactosaminyltransferase	1580:1612	arg1	genes					1622:1626	the ubiquitously expressed polypeptide N-acetylgalactosaminyltransferase 1 and 2 genes	1541:1626	the ubiquitously expressed polypeptide N-acetylgalactosaminyltransferase 1 and 2 genes	1541:1626	This analysis showed high mRNA expression levels of the less understood polypeptide N-acetylgalactosaminyltransferase 15 and 5 in addition to the ubiquitously expressed polypeptide N-acetylgalactosaminyltransferase 1 and 2 genes.
25187573	3	103	theme	-rich	535:539	arg1	domain					541:546	an serine/threonine/proline (STP)-rich domain	502:546	an serine/threonine/proline (STP)-rich domain composed of imperfect tandem repeats (EPAPTTPK)	502:594	Lubricin contains an serine/threonine/proline (STP)-rich domain composed of imperfect tandem repeats (EPAPTTPK), the target for O-glycosylation.
25187573	3	103	theme	-rich	535:539	arg1	target					601:606	the target	597:606	the target for O-glycosylation	597:626	Lubricin contains an serine/threonine/proline (STP)-rich domain composed of imperfect tandem repeats (EPAPTTPK), the target for O-glycosylation.
25187573	4	104	theme	synovial	870:877	arg1	lubricin					879:886	human synovial lubricin	864:886	human synovial lubricin	864:886	In this study, using a liquid chromatography-tandem mass spectrometry approach, employing both collision-induced and electron-transfer dissociation fragmentation methods, we identified 185 O-glycopeptides within the STP-rich domain of human synovial lubricin.
25187573	12	105	theme	glycosylation	2036:2048	arg1	sites					2050:2054	These glycosylation sites	2030:2054	These glycosylation sites	2030:2054	These glycosylation sites were focused in the central STP-rich region, giving the domain a negative charge.
25187573	4	106	theme	STP-rich	845:852	arg1	lubricin					879:886	human synovial lubricin	864:886	human synovial lubricin	864:886	In this study, using a liquid chromatography-tandem mass spectrometry approach, employing both collision-induced and electron-transfer dissociation fragmentation methods, we identified 185 O-glycopeptides within the STP-rich domain of human synovial lubricin.
25187573	4	106	theme	STP-rich	845:852	arg1	domain					854:859	the STP-rich domain	841:859	the STP-rich domain of human synovial lubricin	841:886	In this study, using a liquid chromatography-tandem mass spectrometry approach, employing both collision-induced and electron-transfer dissociation fragmentation methods, we identified 185 O-glycopeptides within the STP-rich domain of human synovial lubricin.
25187573	8	107	theme	high	1420:1423	arg1	levels					1441:1446	high mRNA expression levels	1420:1446	high mRNA expression levels of the less understood polypeptide N-acetylgalactosaminyltransferase 15 and 5	1420:1524	This analysis showed high mRNA expression levels of the less understood polypeptide N-acetylgalactosaminyltransferase 15 and 5 in addition to the ubiquitously expressed polypeptide N-acetylgalactosaminyltransferase 1 and 2 genes.
25187573	11	108	gly	sialylated	2001:2010	arg1	O-glycosylation					1970:1984	O-glycosylation	1970:1984	O-glycosylation	1970:1984	The density of glycosylation was shown to be high: 168 sites of O-glycosylation, predominately sialylated, were identified.
25187573	11	108	gly	sialylated	2001:2010	arg1	sites					1961:1965	168 sites	1957:1965	168 sites	1957:1965	The density of glycosylation was shown to be high: 168 sites of O-glycosylation, predominately sialylated, were identified.
25187573	3	109	theme	imperfect	560:568	arg1	EPAPTTPK					586:593	EPAPTTPK	586:593	EPAPTTPK	586:593	Lubricin contains an serine/threonine/proline (STP)-rich domain composed of imperfect tandem repeats (EPAPTTPK), the target for O-glycosylation.
25187573	3	109	theme	imperfect	560:568	arg1	repeats					577:583	imperfect tandem repeats	560:583	imperfect tandem repeats (EPAPTTPK)	560:594	Lubricin contains an serine/threonine/proline (STP)-rich domain composed of imperfect tandem repeats (EPAPTTPK), the target for O-glycosylation.
22649382	2	0	theme	each	352:355	arg1	role					344:347	the role	340:347	the role of each of the four extracellular domain putative N-glycosylation sites for cell surface localization and function of the receptor	340:478	We probed the role of each of the four extracellular domain putative N-glycosylation sites for cell surface localization and function of the receptor.
22649382	9	1	theme	domain	1446:1451	arg1	sites					1469:1473	extracellular domain N-glycosylation sites	1432:1473	extracellular domain N-glycosylation sites	1432:1473	Our data indicate that extracellular domain N-glycosylation sites regulate in a combinatorial manner cell surface localization of TpoR.
22649382	8	2	theme	receptor	1271:1278	arg1	mutants					1280:1286	N-glycosylation receptor mutants	1255:1286	N-glycosylation receptor mutants	1255:1286	N-glycosylation receptor mutants are not misfolded as, once localized on the cell surface in overexpression conditions, they can bind and respond to Tpo.
22649382	7	3	theme	membrane	1197:1204	arg1	localization					1206:1217	plasma membrane localization	1190:1217	plasma membrane localization	1190:1217	The TpoR mutant defective in all four N-glycosylation sites was severely impaired in plasma membrane localization and was degraded by the proteasome.
22649382	10	4	theme	inefficient	1624:1634	arg1	receptor					1636:1643	inefficient receptor traffic	1624:1651	inefficient receptor traffic	1624:1651	We discuss how mutations around TpoR N-glycosylation sites might contribute to inefficient receptor traffic and disease.
22649382	3	5	theme	mature	562:567	arg1	pattern					584:590	the mature N-glycosylated pattern	558:590	the mature N-glycosylated pattern	558:590	Single N-glycosylation mutants at any of the four sites were able to acquire the mature N-glycosylated pattern, but exhibited a decreased Tpo-dependent JAK2-STAT response in stably transduced Ba/F3 or Ba/F3-JAK2 cell lines.
22649382	1	6	theme	thrombopoietin	207:220	arg1	functions					194:202	the signaling functions	180:202	the signaling functions of thrombopoietin (Tpo)	180:226	The thrombopoietin receptor (TpoR) is a type I transmembrane protein that mediates the signaling functions of thrombopoietin (Tpo) in regulating megakaryocyte differentiation, platelet formation, and hematopoietic stem cell renewal.
22649382	9	7	gly	N-glycosylation	1453:1467	arg2	sites					1469:1473	extracellular domain N-glycosylation sites	1432:1473	extracellular domain N-glycosylation sites	1432:1473	Our data indicate that extracellular domain N-glycosylation sites regulate in a combinatorial manner cell surface localization of TpoR.
22649382	5	8	theme	third	851:855	arg1	site					873:876	the third N-glycosylation site	847:876	the third N-glycosylation site (Asn298)	847:885	In contrast, the third N-glycosylation site (Asn298) decreased receptor maturation and stability.
22649382	5	8	theme	third	851:855	arg1	Asn298					879:884	Asn298	879:884	Asn298	879:884	In contrast, the third N-glycosylation site (Asn298) decreased receptor maturation and stability.
22649382	4	9	theme	cell	736:739	arg1	localization					749:760	cell surface localization	736:760	cell surface localization	736:760	The ability of JAK2 to promote cell surface localization and stability of TpoR required the first N-glycosylation site (Asn117).
22649382	9	10	theme	TpoR	1539:1542	arg1	localization					1523:1534	cell surface localization	1510:1534	cell surface localization of TpoR	1510:1542	Our data indicate that extracellular domain N-glycosylation sites regulate in a combinatorial manner cell surface localization of TpoR.
22649382	6	11	theme	single	1038:1043	arg1	site					1055:1058	the single remaining site	1034:1058	the single remaining site	1034:1058	TpoR mutants lacking three N-glycosylation sites were defective in maturation, but N-glycosylation on the single remaining site could be detected by sensitivity to PNGaseF.
22649382	10	12	gly	N-glycosylation	1582:1596	arg2	sites					1598:1602	TpoR N-glycosylation sites	1577:1602	TpoR N-glycosylation sites	1577:1602	We discuss how mutations around TpoR N-glycosylation sites might contribute to inefficient receptor traffic and disease.
22649382	1	13	theme	platelet	273:280	arg1	formation					282:290	platelet formation	273:290	platelet formation	273:290	The thrombopoietin receptor (TpoR) is a type I transmembrane protein that mediates the signaling functions of thrombopoietin (Tpo) in regulating megakaryocyte differentiation, platelet formation, and hematopoietic stem cell renewal.
22649382	3	14	theme	Tpo-dependent	619:631	arg1	response					643:650	a decreased Tpo-dependent JAK2-STAT response	607:650	a decreased Tpo-dependent JAK2-STAT response	607:650	Single N-glycosylation mutants at any of the four sites were able to acquire the mature N-glycosylated pattern, but exhibited a decreased Tpo-dependent JAK2-STAT response in stably transduced Ba/F3 or Ba/F3-JAK2 cell lines.
22649382	1	15	theme	transmembrane	144:156	arg1	receptor					116:123	The thrombopoietin receptor	97:123	The thrombopoietin receptor (TpoR)	97:130	The thrombopoietin receptor (TpoR) is a type I transmembrane protein that mediates the signaling functions of thrombopoietin (Tpo) in regulating megakaryocyte differentiation, platelet formation, and hematopoietic stem cell renewal.
22649382	1	15	theme	transmembrane	144:156	arg1	protein					158:164	a type I transmembrane protein	135:164	a type I transmembrane protein that mediates the signaling functions of thrombopoietin (Tpo) in regulating megakaryocyte differentiation, platelet formation, and hematopoietic stem cell renewal	135:327	The thrombopoietin receptor (TpoR) is a type I transmembrane protein that mediates the signaling functions of thrombopoietin (Tpo) in regulating megakaryocyte differentiation, platelet formation, and hematopoietic stem cell renewal.
22649382	7	16	from	sites	1159:1163	arg1	defective					1121:1129	defective	1121:1129	defective	1121:1129	The TpoR mutant defective in all four N-glycosylation sites was severely impaired in plasma membrane localization and was degraded by the proteasome.
22649382	8	17	theme	overexpression	1348:1361	arg1	conditions					1363:1372	overexpression conditions	1348:1372	overexpression conditions	1348:1372	N-glycosylation receptor mutants are not misfolded as, once localized on the cell surface in overexpression conditions, they can bind and respond to Tpo.
22649382	4	18	theme	TpoR	779:782	arg1	stability					766:774	stability	766:774	stability of TpoR	766:782	The ability of JAK2 to promote cell surface localization and stability of TpoR required the first N-glycosylation site (Asn117).
22649382	4	18	theme	TpoR	779:782	arg1	localization					749:760	cell surface localization	736:760	cell surface localization	736:760	The ability of JAK2 to promote cell surface localization and stability of TpoR required the first N-glycosylation site (Asn117).
22649382	1	19	theme	type	137:140	arg1	receptor					116:123	The thrombopoietin receptor	97:123	The thrombopoietin receptor (TpoR)	97:130	The thrombopoietin receptor (TpoR) is a type I transmembrane protein that mediates the signaling functions of thrombopoietin (Tpo) in regulating megakaryocyte differentiation, platelet formation, and hematopoietic stem cell renewal.
22649382	1	19	theme	type	137:140	arg1	protein					158:164	a type I transmembrane protein	135:164	a type I transmembrane protein that mediates the signaling functions of thrombopoietin (Tpo) in regulating megakaryocyte differentiation, platelet formation, and hematopoietic stem cell renewal	135:327	The thrombopoietin receptor (TpoR) is a type I transmembrane protein that mediates the signaling functions of thrombopoietin (Tpo) in regulating megakaryocyte differentiation, platelet formation, and hematopoietic stem cell renewal.
22649382	3	20	theme	Single	481:486	arg1	mutants					504:510	Single N-glycosylation mutants	481:510	Single N-glycosylation mutants at any of the four sites	481:535	Single N-glycosylation mutants at any of the four sites were able to acquire the mature N-glycosylated pattern, but exhibited a decreased Tpo-dependent JAK2-STAT response in stably transduced Ba/F3 or Ba/F3-JAK2 cell lines.
22649382	2	21	theme	N-glycosylation	399:413	arg1	sites					415:419	the four extracellular domain putative N-glycosylation sites	360:419	the four extracellular domain putative N-glycosylation sites for cell surface localization and function of the receptor	360:478	We probed the role of each of the four extracellular domain putative N-glycosylation sites for cell surface localization and function of the receptor.
22649382	6	22	from	N-glycosylation	1015:1029	arg1	site					1055:1058	the single remaining site	1034:1058	the single remaining site	1034:1058	TpoR mutants lacking three N-glycosylation sites were defective in maturation, but N-glycosylation on the single remaining site could be detected by sensitivity to PNGaseF.
22649382	2	23	theme	domain	383:388	arg1	sites					415:419	the four extracellular domain putative N-glycosylation sites	360:419	the four extracellular domain putative N-glycosylation sites for cell surface localization and function of the receptor	360:478	We probed the role of each of the four extracellular domain putative N-glycosylation sites for cell surface localization and function of the receptor.
22649382	0	24	theme	Extracellular	0:12	arg1	N-glycosylation					21:35	Extracellular domain N-glycosylation	0:35	Extracellular domain N-glycosylation	0:35	Extracellular domain N-glycosylation controls human thrombopoietin receptor cell surface levels.
22649382	8	25	from	surface	1337:1343	arg1	conditions					1363:1372	overexpression conditions	1348:1372	overexpression conditions	1348:1372	N-glycosylation receptor mutants are not misfolded as, once localized on the cell surface in overexpression conditions, they can bind and respond to Tpo.
22649382	10	26	dep	receptor	1636:1643	arg1	traffic					1645:1651	traffic	1645:1651	traffic	1645:1651	We discuss how mutations around TpoR N-glycosylation sites might contribute to inefficient receptor traffic and disease.
22649382	2	27	theme	surface	430:436	arg1	localization					438:449	cell surface localization	425:449	cell surface localization	425:449	We probed the role of each of the four extracellular domain putative N-glycosylation sites for cell surface localization and function of the receptor.
22649382	1	28	theme	hematopoietic	297:309	arg1	renewal					321:327	hematopoietic stem cell renewal	297:327	hematopoietic stem cell renewal	297:327	The thrombopoietin receptor (TpoR) is a type I transmembrane protein that mediates the signaling functions of thrombopoietin (Tpo) in regulating megakaryocyte differentiation, platelet formation, and hematopoietic stem cell renewal.
22649382	9	29	theme	N-glycosylation	1453:1467	arg1	sites					1469:1473	extracellular domain N-glycosylation sites	1432:1473	extracellular domain N-glycosylation sites	1432:1473	Our data indicate that extracellular domain N-glycosylation sites regulate in a combinatorial manner cell surface localization of TpoR.
22649382	1	30	theme	cell	316:319	arg1	renewal					321:327	hematopoietic stem cell renewal	297:327	hematopoietic stem cell renewal	297:327	The thrombopoietin receptor (TpoR) is a type I transmembrane protein that mediates the signaling functions of thrombopoietin (Tpo) in regulating megakaryocyte differentiation, platelet formation, and hematopoietic stem cell renewal.
22649382	0	31	theme	human	46:50	arg1	levels					89:94	human thrombopoietin receptor cell surface levels	46:94	human thrombopoietin receptor cell surface levels	46:94	Extracellular domain N-glycosylation controls human thrombopoietin receptor cell surface levels.
22649382	2	32	theme	receptor	471:478	arg1	function					455:462	function	455:462	function	455:462	We probed the role of each of the four extracellular domain putative N-glycosylation sites for cell surface localization and function of the receptor.
22649382	2	32	theme	receptor	471:478	arg1	localization					438:449	cell surface localization	425:449	cell surface localization	425:449	We probed the role of each of the four extracellular domain putative N-glycosylation sites for cell surface localization and function of the receptor.
22649382	0	33	theme	surface	81:87	arg1	levels					89:94	human thrombopoietin receptor cell surface levels	46:94	human thrombopoietin receptor cell surface levels	46:94	Extracellular domain N-glycosylation controls human thrombopoietin receptor cell surface levels.
22649382	6	34	gly	N-glycosylation	1015:1029	arg1	site					1055:1058	the single remaining site	1034:1058	the single remaining site	1034:1058	TpoR mutants lacking three N-glycosylation sites were defective in maturation, but N-glycosylation on the single remaining site could be detected by sensitivity to PNGaseF.
22649382	0	35	theme	receptor	67:74	arg1	levels					89:94	human thrombopoietin receptor cell surface levels	46:94	human thrombopoietin receptor cell surface levels	46:94	Extracellular domain N-glycosylation controls human thrombopoietin receptor cell surface levels.
22649382	4	36	theme	N-glycosylation	803:817	arg1	site					819:822	the first N-glycosylation site	793:822	the first N-glycosylation site (Asn117)	793:831	The ability of JAK2 to promote cell surface localization and stability of TpoR required the first N-glycosylation site (Asn117).
22649382	4	36	theme	N-glycosylation	803:817	arg1	Asn117					825:830	Asn117	825:830	Asn117	825:830	The ability of JAK2 to promote cell surface localization and stability of TpoR required the first N-glycosylation site (Asn117).
22649382	3	37	theme	N-glycosylation	488:502	arg1	mutants					504:510	Single N-glycosylation mutants	481:510	Single N-glycosylation mutants at any of the four sites	481:535	Single N-glycosylation mutants at any of the four sites were able to acquire the mature N-glycosylated pattern, but exhibited a decreased Tpo-dependent JAK2-STAT response in stably transduced Ba/F3 or Ba/F3-JAK2 cell lines.
22649382	10	38	theme	N-glycosylation	1582:1596	arg1	sites					1598:1602	TpoR N-glycosylation sites	1577:1602	TpoR N-glycosylation sites	1577:1602	We discuss how mutations around TpoR N-glycosylation sites might contribute to inefficient receptor traffic and disease.
22649382	3	39	theme	Ba/F3-JAK2	682:691	arg1	lines					698:702	stably transduced Ba/F3 or Ba/F3-JAK2 cell lines	655:702	lines	698:702	Single N-glycosylation mutants at any of the four sites were able to acquire the mature N-glycosylated pattern, but exhibited a decreased Tpo-dependent JAK2-STAT response in stably transduced Ba/F3 or Ba/F3-JAK2 cell lines.
22649382	8	40	theme	N-glycosylation	1255:1269	arg1	mutants					1280:1286	N-glycosylation receptor mutants	1255:1286	N-glycosylation receptor mutants	1255:1286	N-glycosylation receptor mutants are not misfolded as, once localized on the cell surface in overexpression conditions, they can bind and respond to Tpo.
22649382	0	41	theme	cell	76:79	arg1	levels					89:94	human thrombopoietin receptor cell surface levels	46:94	human thrombopoietin receptor cell surface levels	46:94	Extracellular domain N-glycosylation controls human thrombopoietin receptor cell surface levels.
22649382	6	42	theme	TpoR	932:935	arg1	mutants					937:943	TpoR mutants	932:943	TpoR mutants lacking three N-glycosylation sites	932:979	TpoR mutants lacking three N-glycosylation sites were defective in maturation, but N-glycosylation on the single remaining site could be detected by sensitivity to PNGaseF.
22649382	5	43	gly	N-glycosylation	857:871	arg2	Asn298					879:884	Asn298	879:884	Asn298	879:884	In contrast, the third N-glycosylation site (Asn298) decreased receptor maturation and stability.
22649382	5	43	gly	N-glycosylation	857:871	arg2	site					873:876	the third N-glycosylation site	847:876	the third N-glycosylation site (Asn298)	847:885	In contrast, the third N-glycosylation site (Asn298) decreased receptor maturation and stability.
22649382	7	44	theme	defective	1121:1129	arg1	mutant					1114:1119	The TpoR mutant	1105:1119	The TpoR mutant defective in all four N-glycosylation sites	1105:1163	The TpoR mutant defective in all four N-glycosylation sites was severely impaired in plasma membrane localization and was degraded by the proteasome.
22649382	7	44	theme	defective	1121:1129	arg1	impaired					1178:1185	impaired	1178:1185	impaired	1178:1185	The TpoR mutant defective in all four N-glycosylation sites was severely impaired in plasma membrane localization and was degraded by the proteasome.
22649382	6	45	gly	N-glycosylation	959:973	arg2	sites					975:979	three N-glycosylation sites	953:979	three N-glycosylation sites	953:979	TpoR mutants lacking three N-glycosylation sites were defective in maturation, but N-glycosylation on the single remaining site could be detected by sensitivity to PNGaseF.
22649382	6	45	gly	N-glycosylation	959:973	arg2	three					953:957	three	953:957	three	953:957	TpoR mutants lacking three N-glycosylation sites were defective in maturation, but N-glycosylation on the single remaining site could be detected by sensitivity to PNGaseF.
22649382	9	46	theme	extracellular	1432:1444	arg1	sites					1469:1473	extracellular domain N-glycosylation sites	1432:1473	extracellular domain N-glycosylation sites	1432:1473	Our data indicate that extracellular domain N-glycosylation sites regulate in a combinatorial manner cell surface localization of TpoR.
22649382	7	47	theme	TpoR	1109:1112	arg1	mutant					1114:1119	The TpoR mutant	1105:1119	The TpoR mutant defective in all four N-glycosylation sites	1105:1163	The TpoR mutant defective in all four N-glycosylation sites was severely impaired in plasma membrane localization and was degraded by the proteasome.
22649382	7	47	theme	TpoR	1109:1112	arg1	impaired					1178:1185	impaired	1178:1185	impaired	1178:1185	The TpoR mutant defective in all four N-glycosylation sites was severely impaired in plasma membrane localization and was degraded by the proteasome.
22649382	5	48	theme	N-glycosylation	857:871	arg1	site					873:876	the third N-glycosylation site	847:876	the third N-glycosylation site (Asn298)	847:885	In contrast, the third N-glycosylation site (Asn298) decreased receptor maturation and stability.
22649382	5	48	theme	N-glycosylation	857:871	arg1	Asn298					879:884	Asn298	879:884	Asn298	879:884	In contrast, the third N-glycosylation site (Asn298) decreased receptor maturation and stability.
22649382	6	49	from	maturation	999:1008	arg1	defective					986:994	defective	986:994	defective	986:994	TpoR mutants lacking three N-glycosylation sites were defective in maturation, but N-glycosylation on the single remaining site could be detected by sensitivity to PNGaseF.
22649382	3	50	theme	N-glycosylated	569:582	arg1	pattern					584:590	the mature N-glycosylated pattern	558:590	the mature N-glycosylated pattern	558:590	Single N-glycosylation mutants at any of the four sites were able to acquire the mature N-glycosylated pattern, but exhibited a decreased Tpo-dependent JAK2-STAT response in stably transduced Ba/F3 or Ba/F3-JAK2 cell lines.
22649382	1	51	theme	signaling	184:192	arg1	functions					194:202	the signaling functions	180:202	the signaling functions of thrombopoietin (Tpo)	180:226	The thrombopoietin receptor (TpoR) is a type I transmembrane protein that mediates the signaling functions of thrombopoietin (Tpo) in regulating megakaryocyte differentiation, platelet formation, and hematopoietic stem cell renewal.
22649382	3	52	from	any	515:517	arg1	mutants					504:510	Single N-glycosylation mutants	481:510	Single N-glycosylation mutants at any of the four sites	481:535	Single N-glycosylation mutants at any of the four sites were able to acquire the mature N-glycosylated pattern, but exhibited a decreased Tpo-dependent JAK2-STAT response in stably transduced Ba/F3 or Ba/F3-JAK2 cell lines.
22649382	7	53	from	localization	1206:1217	arg1	mutant					1114:1119	The TpoR mutant	1105:1119	The TpoR mutant defective in all four N-glycosylation sites	1105:1163	The TpoR mutant defective in all four N-glycosylation sites was severely impaired in plasma membrane localization and was degraded by the proteasome.
22649382	7	53	from	localization	1206:1217	arg1	impaired					1178:1185	impaired	1178:1185	impaired	1178:1185	The TpoR mutant defective in all four N-glycosylation sites was severely impaired in plasma membrane localization and was degraded by the proteasome.
22649382	6	54	theme	N-glycosylation	959:973	arg1	sites					975:979	three N-glycosylation sites	953:979	three N-glycosylation sites	953:979	TpoR mutants lacking three N-glycosylation sites were defective in maturation, but N-glycosylation on the single remaining site could be detected by sensitivity to PNGaseF.
22649382	9	55	theme	surface	1515:1521	arg1	localization					1523:1534	cell surface localization	1510:1534	cell surface localization of TpoR	1510:1542	Our data indicate that extracellular domain N-glycosylation sites regulate in a combinatorial manner cell surface localization of TpoR.
22649382	4	56	theme	JAK2	720:723	arg1	ability					709:715	The ability	705:715	The ability of JAK2 to promote cell surface localization and stability of TpoR	705:782	The ability of JAK2 to promote cell surface localization and stability of TpoR required the first N-glycosylation site (Asn117).
22649382	3	57	theme	JAK2-STAT	633:641	arg1	response					643:650	a decreased Tpo-dependent JAK2-STAT response	607:650	a decreased Tpo-dependent JAK2-STAT response	607:650	Single N-glycosylation mutants at any of the four sites were able to acquire the mature N-glycosylated pattern, but exhibited a decreased Tpo-dependent JAK2-STAT response in stably transduced Ba/F3 or Ba/F3-JAK2 cell lines.
22649382	6	58	theme	remaining	1045:1053	arg1	site					1055:1058	the single remaining site	1034:1058	the single remaining site	1034:1058	TpoR mutants lacking three N-glycosylation sites were defective in maturation, but N-glycosylation on the single remaining site could be detected by sensitivity to PNGaseF.
22649382	3	59	theme	decreased	609:617	arg1	response					643:650	a decreased Tpo-dependent JAK2-STAT response	607:650	a decreased Tpo-dependent JAK2-STAT response	607:650	Single N-glycosylation mutants at any of the four sites were able to acquire the mature N-glycosylated pattern, but exhibited a decreased Tpo-dependent JAK2-STAT response in stably transduced Ba/F3 or Ba/F3-JAK2 cell lines.
22649382	1	60	theme	I	142:142	arg1	receptor					116:123	The thrombopoietin receptor	97:123	The thrombopoietin receptor (TpoR)	97:130	The thrombopoietin receptor (TpoR) is a type I transmembrane protein that mediates the signaling functions of thrombopoietin (Tpo) in regulating megakaryocyte differentiation, platelet formation, and hematopoietic stem cell renewal.
22649382	1	60	theme	I	142:142	arg1	protein					158:164	a type I transmembrane protein	135:164	a type I transmembrane protein that mediates the signaling functions of thrombopoietin (Tpo) in regulating megakaryocyte differentiation, platelet formation, and hematopoietic stem cell renewal	135:327	The thrombopoietin receptor (TpoR) is a type I transmembrane protein that mediates the signaling functions of thrombopoietin (Tpo) in regulating megakaryocyte differentiation, platelet formation, and hematopoietic stem cell renewal.
22649382	8	61	theme	cell	1332:1335	arg1	surface					1337:1343	the cell surface	1328:1343	the cell surface in overexpression conditions	1328:1372	N-glycosylation receptor mutants are not misfolded as, once localized on the cell surface in overexpression conditions, they can bind and respond to Tpo.
22649382	5	62	theme	receptor	897:904	arg1	maturation					906:915	receptor maturation	897:915	receptor maturation	897:915	In contrast, the third N-glycosylation site (Asn298) decreased receptor maturation and stability.
22649382	4	63	gly	N-glycosylation	803:817	arg2	Asn117					825:830	Asn117	825:830	Asn117	825:830	The ability of JAK2 to promote cell surface localization and stability of TpoR required the first N-glycosylation site (Asn117).
22649382	4	63	gly	N-glycosylation	803:817	arg2	site					819:822	the first N-glycosylation site	793:822	the first N-glycosylation site (Asn117)	793:831	The ability of JAK2 to promote cell surface localization and stability of TpoR required the first N-glycosylation site (Asn117).
22649382	7	64	from	impaired	1178:1185	arg1	localization					1206:1217	plasma membrane localization	1190:1217	plasma membrane localization	1190:1217	The TpoR mutant defective in all four N-glycosylation sites was severely impaired in plasma membrane localization and was degraded by the proteasome.
22649382	9	65	theme	combinatorial	1489:1501	arg1	manner					1503:1508	a combinatorial manner	1487:1508	a combinatorial manner	1487:1508	Our data indicate that extracellular domain N-glycosylation sites regulate in a combinatorial manner cell surface localization of TpoR.
22649382	2	66	gly	N-glycosylation	399:413	arg2	four					364:367	four	364:367	four	364:367	We probed the role of each of the four extracellular domain putative N-glycosylation sites for cell surface localization and function of the receptor.
22649382	2	66	gly	N-glycosylation	399:413	arg2	sites					415:419	the four extracellular domain putative N-glycosylation sites	360:419	the four extracellular domain putative N-glycosylation sites for cell surface localization and function of the receptor	360:478	We probed the role of each of the four extracellular domain putative N-glycosylation sites for cell surface localization and function of the receptor.
22649382	2	67	theme	putative	390:397	arg1	sites					415:419	the four extracellular domain putative N-glycosylation sites	360:419	the four extracellular domain putative N-glycosylation sites for cell surface localization and function of the receptor	360:478	We probed the role of each of the four extracellular domain putative N-glycosylation sites for cell surface localization and function of the receptor.
22649382	0	68	theme	domain	14:19	arg1	N-glycosylation					21:35	Extracellular domain N-glycosylation	0:35	Extracellular domain N-glycosylation	0:35	Extracellular domain N-glycosylation controls human thrombopoietin receptor cell surface levels.
22649382	1	69	theme	thrombopoietin	101:114	arg1	receptor					116:123	The thrombopoietin receptor	97:123	The thrombopoietin receptor (TpoR)	97:130	The thrombopoietin receptor (TpoR) is a type I transmembrane protein that mediates the signaling functions of thrombopoietin (Tpo) in regulating megakaryocyte differentiation, platelet formation, and hematopoietic stem cell renewal.
22649382	1	69	theme	thrombopoietin	101:114	arg1	protein					158:164	a type I transmembrane protein	135:164	a type I transmembrane protein that mediates the signaling functions of thrombopoietin (Tpo) in regulating megakaryocyte differentiation, platelet formation, and hematopoietic stem cell renewal	135:327	The thrombopoietin receptor (TpoR) is a type I transmembrane protein that mediates the signaling functions of thrombopoietin (Tpo) in regulating megakaryocyte differentiation, platelet formation, and hematopoietic stem cell renewal.
22649382	1	69	theme	thrombopoietin	101:114	arg1	TpoR					126:129	TpoR	126:129	TpoR	126:129	The thrombopoietin receptor (TpoR) is a type I transmembrane protein that mediates the signaling functions of thrombopoietin (Tpo) in regulating megakaryocyte differentiation, platelet formation, and hematopoietic stem cell renewal.
22649382	4	70	theme	surface	741:747	arg1	localization					749:760	cell surface localization	736:760	cell surface localization	736:760	The ability of JAK2 to promote cell surface localization and stability of TpoR required the first N-glycosylation site (Asn117).
22649382	2	71	theme	extracellular	369:381	arg1	sites					415:419	the four extracellular domain putative N-glycosylation sites	360:419	the four extracellular domain putative N-glycosylation sites for cell surface localization and function of the receptor	360:478	We probed the role of each of the four extracellular domain putative N-glycosylation sites for cell surface localization and function of the receptor.
22649382	3	72	theme	transduced	662:671	arg1	Ba/F3					673:677	stably transduced Ba/F3 or Ba/F3-JAK2 cell lines	655:702	Ba/F3	673:677	Single N-glycosylation mutants at any of the four sites were able to acquire the mature N-glycosylated pattern, but exhibited a decreased Tpo-dependent JAK2-STAT response in stably transduced Ba/F3 or Ba/F3-JAK2 cell lines.
22649382	2	73	theme	cell	425:428	arg1	localization					438:449	cell surface localization	425:449	cell surface localization	425:449	We probed the role of each of the four extracellular domain putative N-glycosylation sites for cell surface localization and function of the receptor.
22649382	0	74	theme	thrombopoietin	52:65	arg1	levels					89:94	human thrombopoietin receptor cell surface levels	46:94	human thrombopoietin receptor cell surface levels	46:94	Extracellular domain N-glycosylation controls human thrombopoietin receptor cell surface levels.
22649382	1	75	theme	stem	311:314	arg1	renewal					321:327	hematopoietic stem cell renewal	297:327	hematopoietic stem cell renewal	297:327	The thrombopoietin receptor (TpoR) is a type I transmembrane protein that mediates the signaling functions of thrombopoietin (Tpo) in regulating megakaryocyte differentiation, platelet formation, and hematopoietic stem cell renewal.
22649382	7	76	from	defective	1121:1129	arg1	sites					1159:1163	all four N-glycosylation sites	1134:1163	all four N-glycosylation sites	1134:1163	The TpoR mutant defective in all four N-glycosylation sites was severely impaired in plasma membrane localization and was degraded by the proteasome.
22649382	6	77	from	defective	986:994	arg1	maturation					999:1008	maturation	999:1008	maturation	999:1008	TpoR mutants lacking three N-glycosylation sites were defective in maturation, but N-glycosylation on the single remaining site could be detected by sensitivity to PNGaseF.
22649382	7	78	theme	N-glycosylation	1143:1157	arg1	sites					1159:1163	all four N-glycosylation sites	1134:1163	all four N-glycosylation sites	1134:1163	The TpoR mutant defective in all four N-glycosylation sites was severely impaired in plasma membrane localization and was degraded by the proteasome.
22649382	3	79	theme	cell	693:696	arg1	lines					698:702	stably transduced Ba/F3 or Ba/F3-JAK2 cell lines	655:702	lines	698:702	Single N-glycosylation mutants at any of the four sites were able to acquire the mature N-glycosylated pattern, but exhibited a decreased Tpo-dependent JAK2-STAT response in stably transduced Ba/F3 or Ba/F3-JAK2 cell lines.
22649382	7	80	gly	N-glycosylation	1143:1157	arg2	four					1138:1141	four	1138:1141	four	1138:1141	The TpoR mutant defective in all four N-glycosylation sites was severely impaired in plasma membrane localization and was degraded by the proteasome.
22649382	7	80	gly	N-glycosylation	1143:1157	arg2	sites					1159:1163	all four N-glycosylation sites	1134:1163	all four N-glycosylation sites	1134:1163	The TpoR mutant defective in all four N-glycosylation sites was severely impaired in plasma membrane localization and was degraded by the proteasome.
22649382	4	81	theme	first	797:801	arg1	site					819:822	the first N-glycosylation site	793:822	the first N-glycosylation site (Asn117)	793:831	The ability of JAK2 to promote cell surface localization and stability of TpoR required the first N-glycosylation site (Asn117).
22649382	4	81	theme	first	797:801	arg1	Asn117					825:830	Asn117	825:830	Asn117	825:830	The ability of JAK2 to promote cell surface localization and stability of TpoR required the first N-glycosylation site (Asn117).
22649382	9	82	theme	cell	1510:1513	arg1	localization					1523:1534	cell surface localization	1510:1534	cell surface localization of TpoR	1510:1542	Our data indicate that extracellular domain N-glycosylation sites regulate in a combinatorial manner cell surface localization of TpoR.
22649382	10	83	theme	TpoR	1577:1580	arg1	sites					1598:1602	TpoR N-glycosylation sites	1577:1602	TpoR N-glycosylation sites	1577:1602	We discuss how mutations around TpoR N-glycosylation sites might contribute to inefficient receptor traffic and disease.
22649382	7	84	theme	plasma	1190:1195	arg1	localization					1206:1217	plasma membrane localization	1190:1217	plasma membrane localization	1190:1217	The TpoR mutant defective in all four N-glycosylation sites was severely impaired in plasma membrane localization and was degraded by the proteasome.
22649382	1	85	theme	megakaryocyte	242:254	arg1	differentiation					256:270	megakaryocyte differentiation	242:270	megakaryocyte differentiation	242:270	The thrombopoietin receptor (TpoR) is a type I transmembrane protein that mediates the signaling functions of thrombopoietin (Tpo) in regulating megakaryocyte differentiation, platelet formation, and hematopoietic stem cell renewal.
29237092	1	0	theme	various	194:200	arg1	proteins					202:209	various proteins	194:209	various proteins	194:209	The unexpected, non-enzymatic S-glycosylation of cysteine residues in various proteins by per-O-acetylated monosaccharides is described.
29237092	3	1	from	list	599:602	arg1	cells					658:662	HeLa cells	653:662	HeLa cells	653:662	It is demonstrated that the use of unacetylated unnatural sugars can avoid the artifact formation and a corrected list of O-GlcNAcylated proteins and O-GlcNAc sites in HeLa cells has been assembled by using N-azidoacetylgalactosamine (GalNAz).
29237092	0	2	theme	Glycan	107:112	arg1	Labeling					114:121	Metabolic Glycan Labeling	97:121	Metabolic Glycan Labeling	97:121	Artificial Cysteine S-Glycosylation Induced by Per-O-Acetylated Unnatural Monosaccharides during Metabolic Glycan Labeling.
29237092	1	3	from	proteins	202:209	arg1	S-glycosylation					154:168	The unexpected, non-enzymatic S-glycosylation	124:168	The unexpected, non-enzymatic S-glycosylation of cysteine residues in various proteins by per-O-acetylated monosaccharides	124:245	The unexpected, non-enzymatic S-glycosylation of cysteine residues in various proteins by per-O-acetylated monosaccharides is described.
29237092	3	4	theme	O-GlcNAc	635:642	arg1	sites					644:648	O-GlcNAc sites	635:648	O-GlcNAc sites	635:648	It is demonstrated that the use of unacetylated unnatural sugars can avoid the artifact formation and a corrected list of O-GlcNAcylated proteins and O-GlcNAc sites in HeLa cells has been assembled by using N-azidoacetylgalactosamine (GalNAz).
29237092	3	5	theme	O-GlcNAcylated	607:620	arg1	proteins					622:629	O-GlcNAcylated proteins	607:629	O-GlcNAcylated proteins	607:629	It is demonstrated that the use of unacetylated unnatural sugars can avoid the artifact formation and a corrected list of O-GlcNAcylated proteins and O-GlcNAc sites in HeLa cells has been assembled by using N-azidoacetylgalactosamine (GalNAz).
29237092	1	6	from	residues	182:189	arg1	proteins					202:209	various proteins	194:209	various proteins	194:209	The unexpected, non-enzymatic S-glycosylation of cysteine residues in various proteins by per-O-acetylated monosaccharides is described.
29237092	2	7	theme	labeling	362:369	arg1	validity					333:340	validity	333:340	validity	333:340	This artificial S-glycosylation greatly compromises the specificity and validity of metabolic glycan labeling in living cells by per-O-acetylated azido and alkynyl sugars, which has been overlooked in the field for decades.
29237092	2	7	theme	labeling	362:369	arg1	specificity					317:327	specificity	317:327	specificity	317:327	This artificial S-glycosylation greatly compromises the specificity and validity of metabolic glycan labeling in living cells by per-O-acetylated azido and alkynyl sugars, which has been overlooked in the field for decades.
29237092	2	8	theme	azido	407:411	arg1	sugars					425:430	per-O-acetylated azido and alkynyl sugars	390:430	per-O-acetylated azido and alkynyl sugars	390:430	This artificial S-glycosylation greatly compromises the specificity and validity of metabolic glycan labeling in living cells by per-O-acetylated azido and alkynyl sugars, which has been overlooked in the field for decades.
29237092	3	9	theme	unnatural	533:541	arg1	sugars					543:548	unacetylated unnatural sugars	520:548	unacetylated unnatural sugars	520:548	It is demonstrated that the use of unacetylated unnatural sugars can avoid the artifact formation and a corrected list of O-GlcNAcylated proteins and O-GlcNAc sites in HeLa cells has been assembled by using N-azidoacetylgalactosamine (GalNAz).
29237092	2	10	theme	glycan	355:360	arg1	labeling					362:369	metabolic glycan labeling	345:369	metabolic glycan labeling	345:369	This artificial S-glycosylation greatly compromises the specificity and validity of metabolic glycan labeling in living cells by per-O-acetylated azido and alkynyl sugars, which has been overlooked in the field for decades.
29237092	2	11	theme	metabolic	345:353	arg1	labeling					362:369	metabolic glycan labeling	345:369	metabolic glycan labeling	345:369	This artificial S-glycosylation greatly compromises the specificity and validity of metabolic glycan labeling in living cells by per-O-acetylated azido and alkynyl sugars, which has been overlooked in the field for decades.
29237092	1	12	theme	per-O-acetylated	214:229	arg1	monosaccharides					231:245	per-O-acetylated monosaccharides	214:245	per-O-acetylated monosaccharides	214:245	The unexpected, non-enzymatic S-glycosylation of cysteine residues in various proteins by per-O-acetylated monosaccharides is described.
29237092	0	13	theme	Cysteine	11:18	arg1	S-Glycosylation					20:34	Artificial Cysteine S-Glycosylation	0:34	Artificial Cysteine S-Glycosylation	0:34	Artificial Cysteine S-Glycosylation Induced by Per-O-Acetylated Unnatural Monosaccharides during Metabolic Glycan Labeling.
29237092	2	14	theme	per-O-acetylated	390:405	arg1	sugars					425:430	per-O-acetylated azido and alkynyl sugars	390:430	per-O-acetylated azido and alkynyl sugars	390:430	This artificial S-glycosylation greatly compromises the specificity and validity of metabolic glycan labeling in living cells by per-O-acetylated azido and alkynyl sugars, which has been overlooked in the field for decades.
29237092	0	15	theme	Artificial	0:9	arg1	S-Glycosylation					20:34	Artificial Cysteine S-Glycosylation	0:34	Artificial Cysteine S-Glycosylation	0:34	Artificial Cysteine S-Glycosylation Induced by Per-O-Acetylated Unnatural Monosaccharides during Metabolic Glycan Labeling.
29237092	3	16	theme	sites	644:648	arg1	list					599:602	a corrected list	587:602	a corrected list of O-GlcNAcylated proteins and O-GlcNAc sites in HeLa cells	587:662	It is demonstrated that the use of unacetylated unnatural sugars can avoid the artifact formation and a corrected list of O-GlcNAcylated proteins and O-GlcNAc sites in HeLa cells has been assembled by using N-azidoacetylgalactosamine (GalNAz).
29237092	1	17	gly	S-glycosylation	154:168	arg1	residues					182:189	cysteine residues	173:189	cysteine residues in various proteins	173:209	The unexpected, non-enzymatic S-glycosylation of cysteine residues in various proteins by per-O-acetylated monosaccharides is described.
29237092	1	18	from	S-glycosylation	154:168	arg1	proteins					202:209	various proteins	194:209	various proteins	194:209	The unexpected, non-enzymatic S-glycosylation of cysteine residues in various proteins by per-O-acetylated monosaccharides is described.
29237092	1	19	theme	unexpected	128:137	arg1	S-glycosylation					154:168	The unexpected, non-enzymatic S-glycosylation	124:168	The unexpected, non-enzymatic S-glycosylation of cysteine residues in various proteins by per-O-acetylated monosaccharides	124:245	The unexpected, non-enzymatic S-glycosylation of cysteine residues in various proteins by per-O-acetylated monosaccharides is described.
29237092	2	20	from	specificity	317:327	arg1	cells					381:385	living cells	374:385	living cells	374:385	This artificial S-glycosylation greatly compromises the specificity and validity of metabolic glycan labeling in living cells by per-O-acetylated azido and alkynyl sugars, which has been overlooked in the field for decades.
29237092	3	21	theme	unacetylated	520:531	arg1	sugars					543:548	unacetylated unnatural sugars	520:548	unacetylated unnatural sugars	520:548	It is demonstrated that the use of unacetylated unnatural sugars can avoid the artifact formation and a corrected list of O-GlcNAcylated proteins and O-GlcNAc sites in HeLa cells has been assembled by using N-azidoacetylgalactosamine (GalNAz).
29237092	3	22	theme	corrected	589:597	arg1	list					599:602	a corrected list	587:602	a corrected list of O-GlcNAcylated proteins and O-GlcNAc sites in HeLa cells	587:662	It is demonstrated that the use of unacetylated unnatural sugars can avoid the artifact formation and a corrected list of O-GlcNAcylated proteins and O-GlcNAc sites in HeLa cells has been assembled by using N-azidoacetylgalactosamine (GalNAz).
29237092	2	23	theme	living	374:379	arg1	cells					381:385	living cells	374:385	living cells	374:385	This artificial S-glycosylation greatly compromises the specificity and validity of metabolic glycan labeling in living cells by per-O-acetylated azido and alkynyl sugars, which has been overlooked in the field for decades.
29237092	1	24	theme	residues	182:189	arg1	S-glycosylation					154:168	The unexpected, non-enzymatic S-glycosylation	124:168	The unexpected, non-enzymatic S-glycosylation of cysteine residues in various proteins by per-O-acetylated monosaccharides	124:245	The unexpected, non-enzymatic S-glycosylation of cysteine residues in various proteins by per-O-acetylated monosaccharides is described.
29237092	0	25	theme	Per-O-Acetylated	47:62	arg1	Monosaccharides					74:88	Per-O-Acetylated Unnatural Monosaccharides	47:88	Per-O-Acetylated Unnatural Monosaccharides	47:88	Artificial Cysteine S-Glycosylation Induced by Per-O-Acetylated Unnatural Monosaccharides during Metabolic Glycan Labeling.
29237092	2	26	from	validity	333:340	arg1	cells					381:385	living cells	374:385	living cells	374:385	This artificial S-glycosylation greatly compromises the specificity and validity of metabolic glycan labeling in living cells by per-O-acetylated azido and alkynyl sugars, which has been overlooked in the field for decades.
29237092	3	27	theme	artifact	564:571	arg1	formation					573:581	the artifact formation	560:581	the artifact formation	560:581	It is demonstrated that the use of unacetylated unnatural sugars can avoid the artifact formation and a corrected list of O-GlcNAcylated proteins and O-GlcNAc sites in HeLa cells has been assembled by using N-azidoacetylgalactosamine (GalNAz).
29237092	0	28	theme	Unnatural	64:72	arg1	Monosaccharides					74:88	Per-O-Acetylated Unnatural Monosaccharides	47:88	Per-O-Acetylated Unnatural Monosaccharides	47:88	Artificial Cysteine S-Glycosylation Induced by Per-O-Acetylated Unnatural Monosaccharides during Metabolic Glycan Labeling.
29237092	2	29	theme	artificial	266:275	arg1	S-glycosylation					277:291	This artificial S-glycosylation	261:291	This artificial S-glycosylation	261:291	This artificial S-glycosylation greatly compromises the specificity and validity of metabolic glycan labeling in living cells by per-O-acetylated azido and alkynyl sugars, which has been overlooked in the field for decades.
29237092	3	30	theme	HeLa	653:656	arg1	cells					658:662	HeLa cells	653:662	HeLa cells	653:662	It is demonstrated that the use of unacetylated unnatural sugars can avoid the artifact formation and a corrected list of O-GlcNAcylated proteins and O-GlcNAc sites in HeLa cells has been assembled by using N-azidoacetylgalactosamine (GalNAz).
29237092	2	31	theme	alkynyl	417:423	arg1	sugars					425:430	per-O-acetylated azido and alkynyl sugars	390:430	per-O-acetylated azido and alkynyl sugars	390:430	This artificial S-glycosylation greatly compromises the specificity and validity of metabolic glycan labeling in living cells by per-O-acetylated azido and alkynyl sugars, which has been overlooked in the field for decades.
29237092	3	32	theme	sugars	543:548	arg1	use					513:515	the use	509:515	the use of unacetylated unnatural sugars	509:548	It is demonstrated that the use of unacetylated unnatural sugars can avoid the artifact formation and a corrected list of O-GlcNAcylated proteins and O-GlcNAc sites in HeLa cells has been assembled by using N-azidoacetylgalactosamine (GalNAz).
29237092	3	33	theme	proteins	622:629	arg1	list					599:602	a corrected list	587:602	a corrected list of O-GlcNAcylated proteins and O-GlcNAc sites in HeLa cells	587:662	It is demonstrated that the use of unacetylated unnatural sugars can avoid the artifact formation and a corrected list of O-GlcNAcylated proteins and O-GlcNAc sites in HeLa cells has been assembled by using N-azidoacetylgalactosamine (GalNAz).
29237092	1	34	theme	cysteine	173:180	arg1	residues					182:189	cysteine residues	173:189	cysteine residues in various proteins	173:209	The unexpected, non-enzymatic S-glycosylation of cysteine residues in various proteins by per-O-acetylated monosaccharides is described.
29237092	0	35	theme	Metabolic	97:105	arg1	Labeling					114:121	Metabolic Glycan Labeling	97:121	Metabolic Glycan Labeling	97:121	Artificial Cysteine S-Glycosylation Induced by Per-O-Acetylated Unnatural Monosaccharides during Metabolic Glycan Labeling.
29237092	1	36	dep	unexpected	128:137	arg1	non-enzymatic					140:152	non-enzymatic	140:152	non-enzymatic	140:152	The unexpected, non-enzymatic S-glycosylation of cysteine residues in various proteins by per-O-acetylated monosaccharides is described.
29237092	2	37	dep	specificity	317:327	arg1	the					313:315	the	313:315	the	313:315	This artificial S-glycosylation greatly compromises the specificity and validity of metabolic glycan labeling in living cells by per-O-acetylated azido and alkynyl sugars, which has been overlooked in the field for decades.
22240840	5	0	with	treatment	872:880	arg1	endoglycosidase					890:904	an endoglycosidase	887:904	an endoglycosidase	887:904	An immunoblot analysis of whole cell lysate (S9) fractions with or without treatment with an endoglycosidase revealed that UGT2B7 was N-glycosylated at Asn-68 and Asn-315 but not Asn-67.
22240840	3	1	contain	has	355:357	arg2	sites					391:395	three potential N-glycosylation sites	359:395	three potential N-glycosylation sites (asparagine at positions 67, 68 and 315)	359:436	Although this enzyme has three potential N-glycosylation sites (asparagine at positions 67, 68 and 315), no information is available on the actual glycosylated sites and the effects of N-glycosylation on its enzymatic functions.
22240840	3	1	contain	has	355:357	arg1	enzyme					348:353	this enzyme	343:353	this enzyme	343:353	Although this enzyme has three potential N-glycosylation sites (asparagine at positions 67, 68 and 315), no information is available on the actual glycosylated sites and the effects of N-glycosylation on its enzymatic functions.
22240840	6	2	theme	Kinetic	984:990	arg1	analysis					992:999	Kinetic analysis	984:999	Kinetic analysis employing the S9 fractions as enzyme sources and zidovudine (AZT) and morphine as typical substrates	984:1100	Kinetic analysis employing the S9 fractions as enzyme sources and zidovudine (AZT) and morphine as typical substrates demonstrated that the abolition of N-glycosylation decreased the affinity for AZT but increased that for morphine without affecting reaction velocities, while it decreased the affinity for UDPGA as a cofactor regardless of the substrate used.
22240840	0	3	theme	morphine	72:79	arg1	glucuronidation					38:52	the glucuronidation	34:52	the glucuronidation of zidovudine and morphine by UGT2B7	34:89	The effects of N-glycosylation on the glucuronidation of zidovudine and morphine by UGT2B7 expressed in HEK293 cells.
22240840	0	4	from	effects	4:10	arg1	glucuronidation					38:52	the glucuronidation	34:52	the glucuronidation of zidovudine and morphine by UGT2B7	34:89	The effects of N-glycosylation on the glucuronidation of zidovudine and morphine by UGT2B7 expressed in HEK293 cells.
22240840	5	5	from	Asn-68	949:954	arg1	N-glycosylated					931:944	N-glycosylated	931:944	N-glycosylated	931:944	An immunoblot analysis of whole cell lysate (S9) fractions with or without treatment with an endoglycosidase revealed that UGT2B7 was N-glycosylated at Asn-68 and Asn-315 but not Asn-67.
22240840	4	6	theme	HEK293	583:588	arg1	cells					590:594	HEK293 cells	583:594	HEK293 cells expressing wild-type UGT2B7 and five mutants (N67Q, N68Q, N315Q, N68Q/N315Q and N67Q/N68Q/N315Q) in which an asparagine at one or more potential N-glycosylation sites was substituted with a glutamine	583:794	We thus constructed HEK293 cells expressing wild-type UGT2B7 and five mutants (N67Q, N68Q, N315Q, N68Q/N315Q and N67Q/N68Q/N315Q) in which an asparagine at one or more potential N-glycosylation sites was substituted with a glutamine.
22240840	1	7	from	glycoproteins	158:170	arg1	membranes					197:205	endoplasmic reticulum membranes	175:205	endoplasmic reticulum membranes	175:205	UDP-glucuronosyltransferases (UGTs) are glycoproteins in endoplasmic reticulum membranes.
22240840	3	8	gly	N-glycosylation	519:533	arg2	N-glycosylation					519:533	N-glycosylation	519:533	N-glycosylation	519:533	Although this enzyme has three potential N-glycosylation sites (asparagine at positions 67, 68 and 315), no information is available on the actual glycosylated sites and the effects of N-glycosylation on its enzymatic functions.
22240840	3	8	gly	N-glycosylation	519:533	arg2	sites					494:498	the actual glycosylated sites	470:498	the actual glycosylated sites	470:498	Although this enzyme has three potential N-glycosylation sites (asparagine at positions 67, 68 and 315), no information is available on the actual glycosylated sites and the effects of N-glycosylation on its enzymatic functions.
22240840	4	9	theme	wild-type	607:615	arg1	UGT2B7					617:622	wild-type UGT2B7	607:622	wild-type UGT2B7	607:622	We thus constructed HEK293 cells expressing wild-type UGT2B7 and five mutants (N67Q, N68Q, N315Q, N68Q/N315Q and N67Q/N68Q/N315Q) in which an asparagine at one or more potential N-glycosylation sites was substituted with a glutamine.
22240840	4	10	theme	N-glycosylation	741:755	arg1	sites					757:761	one or more potential N-glycosylation sites	719:761	one or more potential N-glycosylation sites	719:761	We thus constructed HEK293 cells expressing wild-type UGT2B7 and five mutants (N67Q, N68Q, N315Q, N68Q/N315Q and N67Q/N68Q/N315Q) in which an asparagine at one or more potential N-glycosylation sites was substituted with a glutamine.
22240840	4	11	from	sites	757:761	arg1	asparagine					705:714	an asparagine	702:714	an asparagine at one or more potential N-glycosylation sites	702:761	We thus constructed HEK293 cells expressing wild-type UGT2B7 and five mutants (N67Q, N68Q, N315Q, N68Q/N315Q and N67Q/N68Q/N315Q) in which an asparagine at one or more potential N-glycosylation sites was substituted with a glutamine.
22240840	2	12	theme	endogenous	297:306	arg1	substances					322:331	various endogenous and exogenous substances	289:331	various endogenous and exogenous substances	289:331	UGT2B7 is an important UGT isoenzyme expressed in human liver and glucuronidates various endogenous and exogenous substances.
22240840	6	13	theme	typical	1083:1089	arg1	substrates					1091:1100	typical substrates	1083:1100	typical substrates	1083:1100	Kinetic analysis employing the S9 fractions as enzyme sources and zidovudine (AZT) and morphine as typical substrates demonstrated that the abolition of N-glycosylation decreased the affinity for AZT but increased that for morphine without affecting reaction velocities, while it decreased the affinity for UDPGA as a cofactor regardless of the substrate used.
22240840	6	13	theme	typical	1083:1089	arg1	fractions					1018:1026	the S9 fractions	1011:1026	the S9 fractions	1011:1026	Kinetic analysis employing the S9 fractions as enzyme sources and zidovudine (AZT) and morphine as typical substrates demonstrated that the abolition of N-glycosylation decreased the affinity for AZT but increased that for morphine without affecting reaction velocities, while it decreased the affinity for UDPGA as a cofactor regardless of the substrate used.
22240840	0	14	theme	HEK293	104:109	arg1	cells					111:115	HEK293 cells	104:115	HEK293 cells	104:115	The effects of N-glycosylation on the glucuronidation of zidovudine and morphine by UGT2B7 expressed in HEK293 cells.
22240840	6	15	theme	enzyme	1031:1036	arg1	fractions					1018:1026	the S9 fractions	1011:1026	the S9 fractions	1011:1026	Kinetic analysis employing the S9 fractions as enzyme sources and zidovudine (AZT) and morphine as typical substrates demonstrated that the abolition of N-glycosylation decreased the affinity for AZT but increased that for morphine without affecting reaction velocities, while it decreased the affinity for UDPGA as a cofactor regardless of the substrate used.
22240840	6	15	theme	enzyme	1031:1036	arg1	sources					1038:1044	enzyme sources	1031:1044	enzyme sources	1031:1044	Kinetic analysis employing the S9 fractions as enzyme sources and zidovudine (AZT) and morphine as typical substrates demonstrated that the abolition of N-glycosylation decreased the affinity for AZT but increased that for morphine without affecting reaction velocities, while it decreased the affinity for UDPGA as a cofactor regardless of the substrate used.
22240840	2	16	theme	various	289:295	arg1	substances					322:331	various endogenous and exogenous substances	289:331	various endogenous and exogenous substances	289:331	UGT2B7 is an important UGT isoenzyme expressed in human liver and glucuronidates various endogenous and exogenous substances.
22240840	5	17	theme	fractions	846:854	arg1	analysis					811:818	An immunoblot analysis	797:818	An immunoblot analysis of whole cell lysate (S9) fractions with or without treatment with an endoglycosidase	797:904	An immunoblot analysis of whole cell lysate (S9) fractions with or without treatment with an endoglycosidase revealed that UGT2B7 was N-glycosylated at Asn-68 and Asn-315 but not Asn-67.
22240840	3	18	theme	N-glycosylation	375:389	arg1	sites					391:395	three potential N-glycosylation sites	359:395	three potential N-glycosylation sites (asparagine at positions 67, 68 and 315)	359:436	Although this enzyme has three potential N-glycosylation sites (asparagine at positions 67, 68 and 315), no information is available on the actual glycosylated sites and the effects of N-glycosylation on its enzymatic functions.
22240840	3	19	from	positions	412:420	arg1	asparagine					398:407	asparagine	398:407	asparagine at positions 67, 68 and 315	398:435	Although this enzyme has three potential N-glycosylation sites (asparagine at positions 67, 68 and 315), no information is available on the actual glycosylated sites and the effects of N-glycosylation on its enzymatic functions.
22240840	7	20	theme	AZT	1434:1436	arg1	glucuronidation					1415:1429	the glucuronidation	1411:1429	the glucuronidation of AZT and morphine by human UGT2B7	1411:1465	These results suggest that N-glycosylation differentially affects the glucuronidation of AZT and morphine by human UGT2B7.
22240840	1	21	theme	endoplasmic	175:185	arg1	membranes					197:205	endoplasmic reticulum membranes	175:205	endoplasmic reticulum membranes	175:205	UDP-glucuronosyltransferases (UGTs) are glycoproteins in endoplasmic reticulum membranes.
22240840	7	22	theme	human	1454:1458	arg1	UGT2B7					1460:1465	human UGT2B7	1454:1465	human UGT2B7	1454:1465	These results suggest that N-glycosylation differentially affects the glucuronidation of AZT and morphine by human UGT2B7.
22240840	6	23	theme	N-glycosylation	1137:1151	arg1	abolition					1124:1132	the abolition	1120:1132	the abolition of N-glycosylation	1120:1151	Kinetic analysis employing the S9 fractions as enzyme sources and zidovudine (AZT) and morphine as typical substrates demonstrated that the abolition of N-glycosylation decreased the affinity for AZT but increased that for morphine without affecting reaction velocities, while it decreased the affinity for UDPGA as a cofactor regardless of the substrate used.
22240840	5	24	from	Asn-67	976:981	arg1	N-glycosylated					931:944	N-glycosylated	931:944	N-glycosylated	931:944	An immunoblot analysis of whole cell lysate (S9) fractions with or without treatment with an endoglycosidase revealed that UGT2B7 was N-glycosylated at Asn-68 and Asn-315 but not Asn-67.
22240840	1	25	theme	reticulum	187:195	arg1	membranes					197:205	endoplasmic reticulum membranes	175:205	endoplasmic reticulum membranes	175:205	UDP-glucuronosyltransferases (UGTs) are glycoproteins in endoplasmic reticulum membranes.
22240840	5	26	theme	immunoblot	800:809	arg1	analysis					811:818	An immunoblot analysis	797:818	An immunoblot analysis of whole cell lysate (S9) fractions with or without treatment with an endoglycosidase	797:904	An immunoblot analysis of whole cell lysate (S9) fractions with or without treatment with an endoglycosidase revealed that UGT2B7 was N-glycosylated at Asn-68 and Asn-315 but not Asn-67.
22240840	6	27	theme	reaction	1234:1241	arg1	velocities					1243:1252	reaction velocities	1234:1252	reaction velocities	1234:1252	Kinetic analysis employing the S9 fractions as enzyme sources and zidovudine (AZT) and morphine as typical substrates demonstrated that the abolition of N-glycosylation decreased the affinity for AZT but increased that for morphine without affecting reaction velocities, while it decreased the affinity for UDPGA as a cofactor regardless of the substrate used.
22240840	3	28	from	sites	494:498	arg1	functions					552:560	its enzymatic functions	538:560	its enzymatic functions	538:560	Although this enzyme has three potential N-glycosylation sites (asparagine at positions 67, 68 and 315), no information is available on the actual glycosylated sites and the effects of N-glycosylation on its enzymatic functions.
22240840	0	29	theme	N-glycosylation	15:29	arg1	effects					4:10	The effects	0:10	The effects of N-glycosylation on the glucuronidation of zidovudine and morphine by UGT2B7	0:89	The effects of N-glycosylation on the glucuronidation of zidovudine and morphine by UGT2B7 expressed in HEK293 cells.
22240840	0	30	gly	N-glycosylation	15:29	arg1	morphine					72:79	morphine	72:79	morphine by UGT2B7	72:89	The effects of N-glycosylation on the glucuronidation of zidovudine and morphine by UGT2B7 expressed in HEK293 cells.
22240840	0	30	gly	N-glycosylation	15:29	arg1	zidovudine					57:66	zidovudine	57:66	zidovudine	57:66	The effects of N-glycosylation on the glucuronidation of zidovudine and morphine by UGT2B7 expressed in HEK293 cells.
22240840	3	31	gly	glycosylated	481:492	arg1	sites					494:498	the actual glycosylated sites	470:498	the actual glycosylated sites	470:498	Although this enzyme has three potential N-glycosylation sites (asparagine at positions 67, 68 and 315), no information is available on the actual glycosylated sites and the effects of N-glycosylation on its enzymatic functions.
22240840	3	31	gly	glycosylated	481:492	arg1	N-glycosylation					519:533	N-glycosylation	519:533	N-glycosylation	519:533	Although this enzyme has three potential N-glycosylation sites (asparagine at positions 67, 68 and 315), no information is available on the actual glycosylated sites and the effects of N-glycosylation on its enzymatic functions.
22240840	5	32	theme	whole	823:827	arg1	lysate					834:839	whole cell lysate	823:839	whole cell lysate (S9) fractions with or without treatment with an endoglycosidase	823:904	An immunoblot analysis of whole cell lysate (S9) fractions with or without treatment with an endoglycosidase revealed that UGT2B7 was N-glycosylated at Asn-68 and Asn-315 but not Asn-67.
22240840	5	32	theme	whole	823:827	arg1	S9					842:843	S9	842:843	S9	842:843	An immunoblot analysis of whole cell lysate (S9) fractions with or without treatment with an endoglycosidase revealed that UGT2B7 was N-glycosylated at Asn-68 and Asn-315 but not Asn-67.
22240840	3	33	theme	potential	365:373	arg1	sites					391:395	three potential N-glycosylation sites	359:395	three potential N-glycosylation sites (asparagine at positions 67, 68 and 315)	359:436	Although this enzyme has three potential N-glycosylation sites (asparagine at positions 67, 68 and 315), no information is available on the actual glycosylated sites and the effects of N-glycosylation on its enzymatic functions.
22240840	2	34	theme	exogenous	312:320	arg1	substances					322:331	various endogenous and exogenous substances	289:331	various endogenous and exogenous substances	289:331	UGT2B7 is an important UGT isoenzyme expressed in human liver and glucuronidates various endogenous and exogenous substances.
22240840	5	35	theme	cell	829:832	arg1	lysate					834:839	whole cell lysate	823:839	whole cell lysate (S9) fractions with or without treatment with an endoglycosidase	823:904	An immunoblot analysis of whole cell lysate (S9) fractions with or without treatment with an endoglycosidase revealed that UGT2B7 was N-glycosylated at Asn-68 and Asn-315 but not Asn-67.
22240840	5	35	theme	cell	829:832	arg1	S9					842:843	S9	842:843	S9	842:843	An immunoblot analysis of whole cell lysate (S9) fractions with or without treatment with an endoglycosidase revealed that UGT2B7 was N-glycosylated at Asn-68 and Asn-315 but not Asn-67.
22240840	7	36	gly	N-glycosylation	1372:1386	arg1	AZT					1434:1436	AZT	1434:1436	AZT	1434:1436	These results suggest that N-glycosylation differentially affects the glucuronidation of AZT and morphine by human UGT2B7.
22240840	7	36	gly	N-glycosylation	1372:1386	arg1	morphine					1442:1449	morphine	1442:1449	morphine	1442:1449	These results suggest that N-glycosylation differentially affects the glucuronidation of AZT and morphine by human UGT2B7.
22240840	3	37	gly	N-glycosylation	375:389	arg2	sites					391:395	three potential N-glycosylation sites	359:395	three potential N-glycosylation sites (asparagine at positions 67, 68 and 315)	359:436	Although this enzyme has three potential N-glycosylation sites (asparagine at positions 67, 68 and 315), no information is available on the actual glycosylated sites and the effects of N-glycosylation on its enzymatic functions.
22240840	3	37	gly	N-glycosylation	375:389	arg2	three					359:363	three	359:363	three	359:363	Although this enzyme has three potential N-glycosylation sites (asparagine at positions 67, 68 and 315), no information is available on the actual glycosylated sites and the effects of N-glycosylation on its enzymatic functions.
22240840	5	38	theme	lysate	834:839	arg1	fractions					846:854	whole cell lysate (S9) fractions	823:854	whole cell lysate (S9) fractions with or without treatment with an endoglycosidase	823:904	An immunoblot analysis of whole cell lysate (S9) fractions with or without treatment with an endoglycosidase revealed that UGT2B7 was N-glycosylated at Asn-68 and Asn-315 but not Asn-67.
22240840	5	39	gly	N-glycosylated	931:944	arg1	UGT2B7					920:925	UGT2B7	920:925	UGT2B7	920:925	An immunoblot analysis of whole cell lysate (S9) fractions with or without treatment with an endoglycosidase revealed that UGT2B7 was N-glycosylated at Asn-68 and Asn-315 but not Asn-67.
22240840	5	39	gly	N-glycosylated	931:944	arg2	Asn-315					960:966	Asn-315	960:966	Asn-315	960:966	An immunoblot analysis of whole cell lysate (S9) fractions with or without treatment with an endoglycosidase revealed that UGT2B7 was N-glycosylated at Asn-68 and Asn-315 but not Asn-67.
22240840	5	39	gly	N-glycosylated	931:944	arg2	Asn-68					949:954	Asn-68	949:954	Asn-68	949:954	An immunoblot analysis of whole cell lysate (S9) fractions with or without treatment with an endoglycosidase revealed that UGT2B7 was N-glycosylated at Asn-68 and Asn-315 but not Asn-67.
22240840	5	39	gly	N-glycosylated	931:944	arg2	Asn-67					976:981	Asn-67	976:981	Asn-67	976:981	An immunoblot analysis of whole cell lysate (S9) fractions with or without treatment with an endoglycosidase revealed that UGT2B7 was N-glycosylated at Asn-68 and Asn-315 but not Asn-67.
22240840	2	40	theme	UGT	231:233	arg1	isoenzyme					235:243	an important UGT isoenzyme	218:243	an important UGT isoenzyme expressed in human liver	218:268	UGT2B7 is an important UGT isoenzyme expressed in human liver and glucuronidates various endogenous and exogenous substances.
22240840	2	40	theme	UGT	231:233	arg1	UGT2B7					208:213	UGT2B7	208:213	UGT2B7	208:213	UGT2B7 is an important UGT isoenzyme expressed in human liver and glucuronidates various endogenous and exogenous substances.
22240840	3	41	dep	sites	391:395	arg1	asparagine					398:407	asparagine	398:407	asparagine at positions 67, 68 and 315	398:435	Although this enzyme has three potential N-glycosylation sites (asparagine at positions 67, 68 and 315), no information is available on the actual glycosylated sites and the effects of N-glycosylation on its enzymatic functions.
22240840	4	42	dep	mutants	633:639	arg1	N68Q					648:651	N68Q	648:651	N68Q	648:651	We thus constructed HEK293 cells expressing wild-type UGT2B7 and five mutants (N67Q, N68Q, N315Q, N68Q/N315Q and N67Q/N68Q/N315Q) in which an asparagine at one or more potential N-glycosylation sites was substituted with a glutamine.
22240840	4	42	dep	mutants	633:639	arg1	mutants					633:639	five mutants	628:639	five mutants (N67Q, N68Q, N315Q, N68Q/N315Q and N67Q/N68Q/N315Q) in which an asparagine at one or more potential N-glycosylation sites was substituted with a glutamine	628:794	We thus constructed HEK293 cells expressing wild-type UGT2B7 and five mutants (N67Q, N68Q, N315Q, N68Q/N315Q and N67Q/N68Q/N315Q) in which an asparagine at one or more potential N-glycosylation sites was substituted with a glutamine.
22240840	4	42	dep	mutants	633:639	arg1	N67Q/N68Q/N315Q					676:690	N67Q/N68Q/N315Q	676:690	N67Q/N68Q/N315Q	676:690	We thus constructed HEK293 cells expressing wild-type UGT2B7 and five mutants (N67Q, N68Q, N315Q, N68Q/N315Q and N67Q/N68Q/N315Q) in which an asparagine at one or more potential N-glycosylation sites was substituted with a glutamine.
22240840	4	42	dep	mutants	633:639	arg1	N68Q/N315Q					661:670	N68Q/N315Q	661:670	N68Q/N315Q	661:670	We thus constructed HEK293 cells expressing wild-type UGT2B7 and five mutants (N67Q, N68Q, N315Q, N68Q/N315Q and N67Q/N68Q/N315Q) in which an asparagine at one or more potential N-glycosylation sites was substituted with a glutamine.
22240840	2	43	theme	important	221:229	arg1	isoenzyme					235:243	an important UGT isoenzyme	218:243	an important UGT isoenzyme expressed in human liver	218:268	UGT2B7 is an important UGT isoenzyme expressed in human liver and glucuronidates various endogenous and exogenous substances.
22240840	2	43	theme	important	221:229	arg1	UGT2B7					208:213	UGT2B7	208:213	UGT2B7	208:213	UGT2B7 is an important UGT isoenzyme expressed in human liver and glucuronidates various endogenous and exogenous substances.
22240840	1	44	gly	glycoproteins	158:170	arg1	UDP-glucuronosyltransferases					118:145	UDP-glucuronosyltransferases	118:145	UDP-glucuronosyltransferases (UGTs)	118:152	UDP-glucuronosyltransferases (UGTs) are glycoproteins in endoplasmic reticulum membranes.
22240840	1	44	gly	glycoproteins	158:170	arg1	glycoproteins					158:170	glycoproteins	158:170	glycoproteins in endoplasmic reticulum membranes	158:205	UDP-glucuronosyltransferases (UGTs) are glycoproteins in endoplasmic reticulum membranes.
22240840	3	45	from	effects	508:514	arg1	functions					552:560	its enzymatic functions	538:560	its enzymatic functions	538:560	Although this enzyme has three potential N-glycosylation sites (asparagine at positions 67, 68 and 315), no information is available on the actual glycosylated sites and the effects of N-glycosylation on its enzymatic functions.
22240840	3	46	theme	actual	474:479	arg1	sites					494:498	the actual glycosylated sites	470:498	the actual glycosylated sites	470:498	Although this enzyme has three potential N-glycosylation sites (asparagine at positions 67, 68 and 315), no information is available on the actual glycosylated sites and the effects of N-glycosylation on its enzymatic functions.
22240840	3	46	theme	actual	474:479	arg1	N-glycosylation					519:533	N-glycosylation	519:533	N-glycosylation	519:533	Although this enzyme has three potential N-glycosylation sites (asparagine at positions 67, 68 and 315), no information is available on the actual glycosylated sites and the effects of N-glycosylation on its enzymatic functions.
22240840	4	47	theme	potential	731:739	arg1	sites					757:761	one or more potential N-glycosylation sites	719:761	one or more potential N-glycosylation sites	719:761	We thus constructed HEK293 cells expressing wild-type UGT2B7 and five mutants (N67Q, N68Q, N315Q, N68Q/N315Q and N67Q/N68Q/N315Q) in which an asparagine at one or more potential N-glycosylation sites was substituted with a glutamine.
22240840	6	48	theme	S9	1015:1016	arg1	substrates					1091:1100	typical substrates	1083:1100	typical substrates	1083:1100	Kinetic analysis employing the S9 fractions as enzyme sources and zidovudine (AZT) and morphine as typical substrates demonstrated that the abolition of N-glycosylation decreased the affinity for AZT but increased that for morphine without affecting reaction velocities, while it decreased the affinity for UDPGA as a cofactor regardless of the substrate used.
22240840	6	48	theme	S9	1015:1016	arg1	fractions					1018:1026	the S9 fractions	1011:1026	the S9 fractions	1011:1026	Kinetic analysis employing the S9 fractions as enzyme sources and zidovudine (AZT) and morphine as typical substrates demonstrated that the abolition of N-glycosylation decreased the affinity for AZT but increased that for morphine without affecting reaction velocities, while it decreased the affinity for UDPGA as a cofactor regardless of the substrate used.
22240840	6	48	theme	S9	1015:1016	arg1	sources					1038:1044	enzyme sources	1031:1044	enzyme sources	1031:1044	Kinetic analysis employing the S9 fractions as enzyme sources and zidovudine (AZT) and morphine as typical substrates demonstrated that the abolition of N-glycosylation decreased the affinity for AZT but increased that for morphine without affecting reaction velocities, while it decreased the affinity for UDPGA as a cofactor regardless of the substrate used.
22240840	3	49	theme	enzymatic	542:550	arg1	functions					552:560	its enzymatic functions	538:560	its enzymatic functions	538:560	Although this enzyme has three potential N-glycosylation sites (asparagine at positions 67, 68 and 315), no information is available on the actual glycosylated sites and the effects of N-glycosylation on its enzymatic functions.
22240840	3	50	theme	glycosylated	481:492	arg1	sites					494:498	the actual glycosylated sites	470:498	the actual glycosylated sites	470:498	Although this enzyme has three potential N-glycosylation sites (asparagine at positions 67, 68 and 315), no information is available on the actual glycosylated sites and the effects of N-glycosylation on its enzymatic functions.
22240840	3	50	theme	glycosylated	481:492	arg1	N-glycosylation					519:533	N-glycosylation	519:533	N-glycosylation	519:533	Although this enzyme has three potential N-glycosylation sites (asparagine at positions 67, 68 and 315), no information is available on the actual glycosylated sites and the effects of N-glycosylation on its enzymatic functions.
22240840	4	51	gly	N-glycosylation	741:755	arg2	one					719:721	one	719:721	one	719:721	We thus constructed HEK293 cells expressing wild-type UGT2B7 and five mutants (N67Q, N68Q, N315Q, N68Q/N315Q and N67Q/N68Q/N315Q) in which an asparagine at one or more potential N-glycosylation sites was substituted with a glutamine.
22240840	4	51	gly	N-glycosylation	741:755	arg2	sites					757:761	one or more potential N-glycosylation sites	719:761	one or more potential N-glycosylation sites	719:761	We thus constructed HEK293 cells expressing wild-type UGT2B7 and five mutants (N67Q, N68Q, N315Q, N68Q/N315Q and N67Q/N68Q/N315Q) in which an asparagine at one or more potential N-glycosylation sites was substituted with a glutamine.
22240840	4	51	gly	N-glycosylation	741:755	arg2	more					726:729	more	726:729	more	726:729	We thus constructed HEK293 cells expressing wild-type UGT2B7 and five mutants (N67Q, N68Q, N315Q, N68Q/N315Q and N67Q/N68Q/N315Q) in which an asparagine at one or more potential N-glycosylation sites was substituted with a glutamine.
22240840	7	52	theme	morphine	1442:1449	arg1	glucuronidation					1415:1429	the glucuronidation	1411:1429	the glucuronidation of AZT and morphine by human UGT2B7	1411:1465	These results suggest that N-glycosylation differentially affects the glucuronidation of AZT and morphine by human UGT2B7.
22240840	2	53	theme	human	258:262	arg1	liver					264:268	human liver	258:268	human liver	258:268	UGT2B7 is an important UGT isoenzyme expressed in human liver and glucuronidates various endogenous and exogenous substances.
22240840	0	54	theme	zidovudine	57:66	arg1	glucuronidation					38:52	the glucuronidation	34:52	the glucuronidation of zidovudine and morphine by UGT2B7	34:89	The effects of N-glycosylation on the glucuronidation of zidovudine and morphine by UGT2B7 expressed in HEK293 cells.
22240840	3	55	theme	N-glycosylation	519:533	arg1	sites					494:498	the actual glycosylated sites	470:498	the actual glycosylated sites	470:498	Although this enzyme has three potential N-glycosylation sites (asparagine at positions 67, 68 and 315), no information is available on the actual glycosylated sites and the effects of N-glycosylation on its enzymatic functions.
22240840	3	55	theme	N-glycosylation	519:533	arg1	effects					508:514	the effects	504:514	the effects of N-glycosylation on its enzymatic functions	504:560	Although this enzyme has three potential N-glycosylation sites (asparagine at positions 67, 68 and 315), no information is available on the actual glycosylated sites and the effects of N-glycosylation on its enzymatic functions.
22240840	3	55	theme	N-glycosylation	519:533	arg1	N-glycosylation					519:533	N-glycosylation	519:533	N-glycosylation	519:533	Although this enzyme has three potential N-glycosylation sites (asparagine at positions 67, 68 and 315), no information is available on the actual glycosylated sites and the effects of N-glycosylation on its enzymatic functions.
22240840	5	56	from	Asn-315	960:966	arg1	N-glycosylated					931:944	N-glycosylated	931:944	N-glycosylated	931:944	An immunoblot analysis of whole cell lysate (S9) fractions with or without treatment with an endoglycosidase revealed that UGT2B7 was N-glycosylated at Asn-68 and Asn-315 but not Asn-67.
21606357	1	0	theme	processes	342:350	arg1	regulator					315:323	a general regulator	305:323	a general regulator of many cellular processes, including signal transduction, cell division, and transcription	305:415	The monosaccharide addition of an N-acetylglucosamine to serine and threonine residues of nuclear and cytosolic proteins (O-GlcNAc) is a posttranslational modification emerging as a general regulator of many cellular processes, including signal transduction, cell division, and transcription.
21606357	0	1	theme	O-GlcNAc	72:79	arg1	distribution					81:92	the normal site-specific O-GlcNAc distribution	47:92	the normal site-specific O-GlcNAc distribution in mouse embryonic stem cells	47:122	Polycomb repressive complex 2 is necessary for the normal site-specific O-GlcNAc distribution in mouse embryonic stem cells.
21606357	1	2	theme	N-acetylglucosamine	159:177	arg1	modification					280:291	a posttranslational modification	260:291	a posttranslational modification emerging as a general regulator of many cellular processes, including signal transduction, cell division, and transcription	260:415	The monosaccharide addition of an N-acetylglucosamine to serine and threonine residues of nuclear and cytosolic proteins (O-GlcNAc) is a posttranslational modification emerging as a general regulator of many cellular processes, including signal transduction, cell division, and transcription.
21606357	1	2	theme	N-acetylglucosamine	159:177	arg1	addition					144:151	The monosaccharide addition	125:151	The monosaccharide addition of an N-acetylglucosamine to serine and threonine residues of nuclear and cytosolic proteins (O-GlcNAc)	125:255	The monosaccharide addition of an N-acetylglucosamine to serine and threonine residues of nuclear and cytosolic proteins (O-GlcNAc) is a posttranslational modification emerging as a general regulator of many cellular processes, including signal transduction, cell division, and transcription.
21606357	0	3	theme	mouse	97:101	arg1	cells					118:122	mouse embryonic stem cells	97:122	mouse embryonic stem cells	97:122	Polycomb repressive complex 2 is necessary for the normal site-specific O-GlcNAc distribution in mouse embryonic stem cells.
21606357	4	4	theme	ESC	767:769	arg1	maintenance					776:786	mouse ESC cell maintenance	761:786	mouse ESC cell maintenance	761:786	Here, we unambiguously identify over 60 nuclear proteins as O-GlcNAcylated, several of which are crucial for mouse ESC cell maintenance.
21606357	5	5	from	flies	869:873	arg1	connection					816:825	the connection	812:825	the connection between OGT and Polycomb group genes from flies to mammals	812:884	Furthermore, we extend the connection between OGT and Polycomb group genes from flies to mammals, showing Polycomb repressive complex 2 is necessary to maintain normal levels of OGT and for the correct cellular distribution of O-GlcNAc.
21606357	3	6	theme	mouse	533:537	arg1	development					539:549	mouse development	533:549	mouse development	533:549	To understand the role of OGT in mouse development better, we mapped sites of O-GlcNAcylation of nuclear proteins in mouse embryonic stem cells (ESCs).
21606357	5	7	theme	Polycomb	895:902	arg1	complex					915:921	Polycomb repressive complex 2	895:923	Polycomb repressive complex 2	895:923	Furthermore, we extend the connection between OGT and Polycomb group genes from flies to mammals, showing Polycomb repressive complex 2 is necessary to maintain normal levels of OGT and for the correct cellular distribution of O-GlcNAc.
21606357	1	8	theme	signal	363:368	arg1	transduction					370:381	signal transduction	363:381	signal transduction	363:381	The monosaccharide addition of an N-acetylglucosamine to serine and threonine residues of nuclear and cytosolic proteins (O-GlcNAc) is a posttranslational modification emerging as a general regulator of many cellular processes, including signal transduction, cell division, and transcription.
21606357	3	9	from	role	518:521	arg1	development					539:549	mouse development	533:549	mouse development	533:549	To understand the role of OGT in mouse development better, we mapped sites of O-GlcNAcylation of nuclear proteins in mouse embryonic stem cells (ESCs).
21606357	1	10	theme	posttranslational	262:278	arg1	modification					280:291	a posttranslational modification	260:291	a posttranslational modification emerging as a general regulator of many cellular processes, including signal transduction, cell division, and transcription	260:415	The monosaccharide addition of an N-acetylglucosamine to serine and threonine residues of nuclear and cytosolic proteins (O-GlcNAc) is a posttranslational modification emerging as a general regulator of many cellular processes, including signal transduction, cell division, and transcription.
21606357	1	10	theme	posttranslational	262:278	arg1	addition					144:151	The monosaccharide addition	125:151	The monosaccharide addition of an N-acetylglucosamine to serine and threonine residues of nuclear and cytosolic proteins (O-GlcNAc)	125:255	The monosaccharide addition of an N-acetylglucosamine to serine and threonine residues of nuclear and cytosolic proteins (O-GlcNAc) is a posttranslational modification emerging as a general regulator of many cellular processes, including signal transduction, cell division, and transcription.
21606357	0	11	theme	stem	113:116	arg1	cells					118:122	mouse embryonic stem cells	97:122	mouse embryonic stem cells	97:122	Polycomb repressive complex 2 is necessary for the normal site-specific O-GlcNAc distribution in mouse embryonic stem cells.
21606357	3	12	theme	OGT	526:528	arg1	role					518:521	the role	514:521	the role of OGT in mouse development	514:549	To understand the role of OGT in mouse development better, we mapped sites of O-GlcNAcylation of nuclear proteins in mouse embryonic stem cells (ESCs).
21606357	3	13	from	proteins	605:612	arg1	cells					638:642	mouse embryonic stem cells	617:642	mouse embryonic stem cells (ESCs)	617:649	To understand the role of OGT in mouse development better, we mapped sites of O-GlcNAcylation of nuclear proteins in mouse embryonic stem cells (ESCs).
21606357	3	13	from	proteins	605:612	arg1	ESCs					645:648	ESCs	645:648	ESCs	645:648	To understand the role of OGT in mouse development better, we mapped sites of O-GlcNAcylation of nuclear proteins in mouse embryonic stem cells (ESCs).
21606357	0	14	theme	embryonic	103:111	arg1	cells					118:122	mouse embryonic stem cells	97:122	mouse embryonic stem cells	97:122	Polycomb repressive complex 2 is necessary for the normal site-specific O-GlcNAc distribution in mouse embryonic stem cells.
21606357	2	15	theme	embryonic	477:485	arg1	development					487:497	embryonic development	477:497	embryonic development	477:497	The sole mouse O-GlcNAc transferase (OGT) is essential for embryonic development.
21606357	3	16	from	cells	638:642	arg1	O-GlcNAcylation					578:592	O-GlcNAcylation	578:592	O-GlcNAcylation of nuclear proteins in mouse embryonic stem cells (ESCs)	578:649	To understand the role of OGT in mouse development better, we mapped sites of O-GlcNAcylation of nuclear proteins in mouse embryonic stem cells (ESCs).
21606357	0	17	theme	repressive	9:18	arg1	complex					20:26	Polycomb repressive complex 2	0:28	Polycomb repressive complex 2	0:28	Polycomb repressive complex 2 is necessary for the normal site-specific O-GlcNAc distribution in mouse embryonic stem cells.
21606357	1	18	theme	cell	384:387	arg1	division					389:396	cell division	384:396	cell division	384:396	The monosaccharide addition of an N-acetylglucosamine to serine and threonine residues of nuclear and cytosolic proteins (O-GlcNAc) is a posttranslational modification emerging as a general regulator of many cellular processes, including signal transduction, cell division, and transcription.
21606357	4	19	theme	O-GlcNAcylated	712:725	arg1	several					728:734	several	728:734	several	728:734	Here, we unambiguously identify over 60 nuclear proteins as O-GlcNAcylated, several of which are crucial for mouse ESC cell maintenance.
21606357	0	20	theme	Polycomb	0:7	arg1	complex					20:26	Polycomb repressive complex 2	0:28	Polycomb repressive complex 2	0:28	Polycomb repressive complex 2 is necessary for the normal site-specific O-GlcNAc distribution in mouse embryonic stem cells.
21606357	6	21	theme	important	1159:1167	arg1	proteins					1150:1157	proteins	1150:1157	proteins important to maintain the ESC transcriptional repertoire	1150:1214	Together, these results provide insight into how OGT may regulate transcription in early development, possibly by modifying proteins important to maintain the ESC transcriptional repertoire.
21606357	4	22	theme	nuclear	692:698	arg1	proteins					700:707	over 60 nuclear proteins	684:707	over 60 nuclear proteins	684:707	Here, we unambiguously identify over 60 nuclear proteins as O-GlcNAcylated, several of which are crucial for mouse ESC cell maintenance.
21606357	5	23	theme	repressive	904:913	arg1	complex					915:921	Polycomb repressive complex 2	895:923	Polycomb repressive complex 2	895:923	Furthermore, we extend the connection between OGT and Polycomb group genes from flies to mammals, showing Polycomb repressive complex 2 is necessary to maintain normal levels of OGT and for the correct cellular distribution of O-GlcNAc.
21606357	5	24	theme	Polycomb	843:850	arg1	genes					858:862	Polycomb group genes	843:862	Polycomb group genes	843:862	Furthermore, we extend the connection between OGT and Polycomb group genes from flies to mammals, showing Polycomb repressive complex 2 is necessary to maintain normal levels of OGT and for the correct cellular distribution of O-GlcNAc.
21606357	4	25	theme	cell	771:774	arg1	maintenance					776:786	mouse ESC cell maintenance	761:786	mouse ESC cell maintenance	761:786	Here, we unambiguously identify over 60 nuclear proteins as O-GlcNAcylated, several of which are crucial for mouse ESC cell maintenance.
21606357	5	26	theme	correct	983:989	arg1	distribution					1000:1011	the correct cellular distribution	979:1011	the correct cellular distribution of O-GlcNAc	979:1023	Furthermore, we extend the connection between OGT and Polycomb group genes from flies to mammals, showing Polycomb repressive complex 2 is necessary to maintain normal levels of OGT and for the correct cellular distribution of O-GlcNAc.
21606357	2	27	theme	mouse	427:431	arg1	OGT					455:457	OGT	455:457	OGT	455:457	The sole mouse O-GlcNAc transferase (OGT) is essential for embryonic development.
21606357	2	27	theme	mouse	427:431	arg1	essential					463:471	essential	463:471	essential	463:471	The sole mouse O-GlcNAc transferase (OGT) is essential for embryonic development.
21606357	2	27	theme	mouse	427:431	arg1	transferase					442:452	The sole mouse O-GlcNAc transferase	418:452	The sole mouse O-GlcNAc transferase (OGT)	418:458	The sole mouse O-GlcNAc transferase (OGT) is essential for embryonic development.
21606357	2	28	theme	O-GlcNAc	433:440	arg1	OGT					455:457	OGT	455:457	OGT	455:457	The sole mouse O-GlcNAc transferase (OGT) is essential for embryonic development.
21606357	2	28	theme	O-GlcNAc	433:440	arg1	essential					463:471	essential	463:471	essential	463:471	The sole mouse O-GlcNAc transferase (OGT) is essential for embryonic development.
21606357	2	28	theme	O-GlcNAc	433:440	arg1	transferase					442:452	The sole mouse O-GlcNAc transferase	418:452	The sole mouse O-GlcNAc transferase (OGT)	418:458	The sole mouse O-GlcNAc transferase (OGT) is essential for embryonic development.
21606357	0	29	from	distribution	81:92	arg1	cells					118:122	mouse embryonic stem cells	97:122	mouse embryonic stem cells	97:122	Polycomb repressive complex 2 is necessary for the normal site-specific O-GlcNAc distribution in mouse embryonic stem cells.
21606357	3	30	from	O-GlcNAcylation	578:592	arg1	cells					638:642	mouse embryonic stem cells	617:642	mouse embryonic stem cells (ESCs)	617:649	To understand the role of OGT in mouse development better, we mapped sites of O-GlcNAcylation of nuclear proteins in mouse embryonic stem cells (ESCs).
21606357	3	30	from	O-GlcNAcylation	578:592	arg1	ESCs					645:648	ESCs	645:648	ESCs	645:648	To understand the role of OGT in mouse development better, we mapped sites of O-GlcNAcylation of nuclear proteins in mouse embryonic stem cells (ESCs).
21606357	2	31	theme	sole	422:425	arg1	OGT					455:457	OGT	455:457	OGT	455:457	The sole mouse O-GlcNAc transferase (OGT) is essential for embryonic development.
21606357	2	31	theme	sole	422:425	arg1	essential					463:471	essential	463:471	essential	463:471	The sole mouse O-GlcNAc transferase (OGT) is essential for embryonic development.
21606357	2	31	theme	sole	422:425	arg1	transferase					442:452	The sole mouse O-GlcNAc transferase	418:452	The sole mouse O-GlcNAc transferase (OGT)	418:458	The sole mouse O-GlcNAc transferase (OGT) is essential for embryonic development.
21606357	5	32	theme	OGT	967:969	arg1	levels					957:962	normal levels	950:962	normal levels of OGT and for the correct cellular distribution of O-GlcNAc	950:1023	Furthermore, we extend the connection between OGT and Polycomb group genes from flies to mammals, showing Polycomb repressive complex 2 is necessary to maintain normal levels of OGT and for the correct cellular distribution of O-GlcNAc.
21606357	3	33	theme	O-GlcNAcylation	578:592	arg1	O-GlcNAcylation					578:592	O-GlcNAcylation	578:592	O-GlcNAcylation of nuclear proteins in mouse embryonic stem cells (ESCs)	578:649	To understand the role of OGT in mouse development better, we mapped sites of O-GlcNAcylation of nuclear proteins in mouse embryonic stem cells (ESCs).
21606357	3	33	theme	O-GlcNAcylation	578:592	arg1	sites					569:573	sites	569:573	sites of O-GlcNAcylation of nuclear proteins in mouse embryonic stem cells (ESCs)	569:649	To understand the role of OGT in mouse development better, we mapped sites of O-GlcNAcylation of nuclear proteins in mouse embryonic stem cells (ESCs).
21606357	1	34	theme	nuclear	215:221	arg1	O-GlcNAc					247:254	O-GlcNAc	247:254	O-GlcNAc	247:254	The monosaccharide addition of an N-acetylglucosamine to serine and threonine residues of nuclear and cytosolic proteins (O-GlcNAc) is a posttranslational modification emerging as a general regulator of many cellular processes, including signal transduction, cell division, and transcription.
21606357	1	34	theme	nuclear	215:221	arg1	proteins					237:244	nuclear and cytosolic proteins	215:244	nuclear and cytosolic proteins (O-GlcNAc)	215:255	The monosaccharide addition of an N-acetylglucosamine to serine and threonine residues of nuclear and cytosolic proteins (O-GlcNAc) is a posttranslational modification emerging as a general regulator of many cellular processes, including signal transduction, cell division, and transcription.
21606357	1	35	theme	general	307:313	arg1	regulator					315:323	a general regulator	305:323	a general regulator of many cellular processes, including signal transduction, cell division, and transcription	305:415	The monosaccharide addition of an N-acetylglucosamine to serine and threonine residues of nuclear and cytosolic proteins (O-GlcNAc) is a posttranslational modification emerging as a general regulator of many cellular processes, including signal transduction, cell division, and transcription.
21606357	3	36	theme	embryonic	623:631	arg1	cells					638:642	mouse embryonic stem cells	617:642	mouse embryonic stem cells (ESCs)	617:649	To understand the role of OGT in mouse development better, we mapped sites of O-GlcNAcylation of nuclear proteins in mouse embryonic stem cells (ESCs).
21606357	3	36	theme	embryonic	623:631	arg1	ESCs					645:648	ESCs	645:648	ESCs	645:648	To understand the role of OGT in mouse development better, we mapped sites of O-GlcNAcylation of nuclear proteins in mouse embryonic stem cells (ESCs).
21606357	6	37	theme	transcriptional	1189:1203	arg1	repertoire					1205:1214	the ESC transcriptional repertoire	1181:1214	the ESC transcriptional repertoire	1181:1214	Together, these results provide insight into how OGT may regulate transcription in early development, possibly by modifying proteins important to maintain the ESC transcriptional repertoire.
21606357	3	38	theme	stem	633:636	arg1	cells					638:642	mouse embryonic stem cells	617:642	mouse embryonic stem cells (ESCs)	617:649	To understand the role of OGT in mouse development better, we mapped sites of O-GlcNAcylation of nuclear proteins in mouse embryonic stem cells (ESCs).
21606357	3	38	theme	stem	633:636	arg1	ESCs					645:648	ESCs	645:648	ESCs	645:648	To understand the role of OGT in mouse development better, we mapped sites of O-GlcNAcylation of nuclear proteins in mouse embryonic stem cells (ESCs).
21606357	6	39	theme	ESC	1185:1187	arg1	repertoire					1205:1214	the ESC transcriptional repertoire	1181:1214	the ESC transcriptional repertoire	1181:1214	Together, these results provide insight into how OGT may regulate transcription in early development, possibly by modifying proteins important to maintain the ESC transcriptional repertoire.
21606357	5	40	theme	cellular	991:998	arg1	distribution					1000:1011	the correct cellular distribution	979:1011	the correct cellular distribution of O-GlcNAc	979:1023	Furthermore, we extend the connection between OGT and Polycomb group genes from flies to mammals, showing Polycomb repressive complex 2 is necessary to maintain normal levels of OGT and for the correct cellular distribution of O-GlcNAc.
21606357	1	41	dep	serine	182:187	arg1	residues					203:210	residues	203:210	residues	203:210	The monosaccharide addition of an N-acetylglucosamine to serine and threonine residues of nuclear and cytosolic proteins (O-GlcNAc) is a posttranslational modification emerging as a general regulator of many cellular processes, including signal transduction, cell division, and transcription.
21606357	1	42	theme	many	328:331	arg1	transduction					370:381	signal transduction	363:381	signal transduction	363:381	The monosaccharide addition of an N-acetylglucosamine to serine and threonine residues of nuclear and cytosolic proteins (O-GlcNAc) is a posttranslational modification emerging as a general regulator of many cellular processes, including signal transduction, cell division, and transcription.
21606357	1	42	theme	many	328:331	arg1	division					389:396	cell division	384:396	cell division	384:396	The monosaccharide addition of an N-acetylglucosamine to serine and threonine residues of nuclear and cytosolic proteins (O-GlcNAc) is a posttranslational modification emerging as a general regulator of many cellular processes, including signal transduction, cell division, and transcription.
21606357	1	42	theme	many	328:331	arg1	transcription					403:415	transcription	403:415	transcription	403:415	The monosaccharide addition of an N-acetylglucosamine to serine and threonine residues of nuclear and cytosolic proteins (O-GlcNAc) is a posttranslational modification emerging as a general regulator of many cellular processes, including signal transduction, cell division, and transcription.
21606357	1	42	theme	many	328:331	arg1	processes					342:350	many cellular processes	328:350	many cellular processes	328:350	The monosaccharide addition of an N-acetylglucosamine to serine and threonine residues of nuclear and cytosolic proteins (O-GlcNAc) is a posttranslational modification emerging as a general regulator of many cellular processes, including signal transduction, cell division, and transcription.
21606357	5	43	theme	normal	950:955	arg1	levels					957:962	normal levels	950:962	normal levels of OGT and for the correct cellular distribution of O-GlcNAc	950:1023	Furthermore, we extend the connection between OGT and Polycomb group genes from flies to mammals, showing Polycomb repressive complex 2 is necessary to maintain normal levels of OGT and for the correct cellular distribution of O-GlcNAc.
21606357	4	44	theme	mouse	761:765	arg1	maintenance					776:786	mouse ESC cell maintenance	761:786	mouse ESC cell maintenance	761:786	Here, we unambiguously identify over 60 nuclear proteins as O-GlcNAcylated, several of which are crucial for mouse ESC cell maintenance.
21606357	1	45	theme	cytosolic	227:235	arg1	O-GlcNAc					247:254	O-GlcNAc	247:254	O-GlcNAc	247:254	The monosaccharide addition of an N-acetylglucosamine to serine and threonine residues of nuclear and cytosolic proteins (O-GlcNAc) is a posttranslational modification emerging as a general regulator of many cellular processes, including signal transduction, cell division, and transcription.
21606357	1	45	theme	cytosolic	227:235	arg1	proteins					237:244	nuclear and cytosolic proteins	215:244	nuclear and cytosolic proteins (O-GlcNAc)	215:255	The monosaccharide addition of an N-acetylglucosamine to serine and threonine residues of nuclear and cytosolic proteins (O-GlcNAc) is a posttranslational modification emerging as a general regulator of many cellular processes, including signal transduction, cell division, and transcription.
21606357	3	46	theme	mouse	617:621	arg1	cells					638:642	mouse embryonic stem cells	617:642	mouse embryonic stem cells (ESCs)	617:649	To understand the role of OGT in mouse development better, we mapped sites of O-GlcNAcylation of nuclear proteins in mouse embryonic stem cells (ESCs).
21606357	3	46	theme	mouse	617:621	arg1	ESCs					645:648	ESCs	645:648	ESCs	645:648	To understand the role of OGT in mouse development better, we mapped sites of O-GlcNAcylation of nuclear proteins in mouse embryonic stem cells (ESCs).
21606357	1	47	theme	monosaccharide	129:142	arg1	modification					280:291	a posttranslational modification	260:291	a posttranslational modification emerging as a general regulator of many cellular processes, including signal transduction, cell division, and transcription	260:415	The monosaccharide addition of an N-acetylglucosamine to serine and threonine residues of nuclear and cytosolic proteins (O-GlcNAc) is a posttranslational modification emerging as a general regulator of many cellular processes, including signal transduction, cell division, and transcription.
21606357	1	47	theme	monosaccharide	129:142	arg1	addition					144:151	The monosaccharide addition	125:151	The monosaccharide addition of an N-acetylglucosamine to serine and threonine residues of nuclear and cytosolic proteins (O-GlcNAc)	125:255	The monosaccharide addition of an N-acetylglucosamine to serine and threonine residues of nuclear and cytosolic proteins (O-GlcNAc) is a posttranslational modification emerging as a general regulator of many cellular processes, including signal transduction, cell division, and transcription.
21606357	1	48	theme	proteins	237:244	arg1	threonine					193:201	threonine	193:201	threonine	193:201	The monosaccharide addition of an N-acetylglucosamine to serine and threonine residues of nuclear and cytosolic proteins (O-GlcNAc) is a posttranslational modification emerging as a general regulator of many cellular processes, including signal transduction, cell division, and transcription.
21606357	1	48	theme	proteins	237:244	arg1	serine					182:187	serine	182:187	serine	182:187	The monosaccharide addition of an N-acetylglucosamine to serine and threonine residues of nuclear and cytosolic proteins (O-GlcNAc) is a posttranslational modification emerging as a general regulator of many cellular processes, including signal transduction, cell division, and transcription.
21606357	0	49	theme	site-specific	58:70	arg1	distribution					81:92	the normal site-specific O-GlcNAc distribution	47:92	the normal site-specific O-GlcNAc distribution in mouse embryonic stem cells	47:122	Polycomb repressive complex 2 is necessary for the normal site-specific O-GlcNAc distribution in mouse embryonic stem cells.
21606357	5	50	theme	O-GlcNAc	1016:1023	arg1	distribution					1000:1011	the correct cellular distribution	979:1011	the correct cellular distribution of O-GlcNAc	979:1023	Furthermore, we extend the connection between OGT and Polycomb group genes from flies to mammals, showing Polycomb repressive complex 2 is necessary to maintain normal levels of OGT and for the correct cellular distribution of O-GlcNAc.
21606357	3	51	theme	nuclear	597:603	arg1	proteins					605:612	nuclear proteins	597:612	nuclear proteins in mouse embryonic stem cells (ESCs)	597:649	To understand the role of OGT in mouse development better, we mapped sites of O-GlcNAcylation of nuclear proteins in mouse embryonic stem cells (ESCs).
21606357	5	52	theme	group	852:856	arg1	genes					858:862	Polycomb group genes	843:862	Polycomb group genes	843:862	Furthermore, we extend the connection between OGT and Polycomb group genes from flies to mammals, showing Polycomb repressive complex 2 is necessary to maintain normal levels of OGT and for the correct cellular distribution of O-GlcNAc.
21606357	6	53	theme	early	1109:1113	arg1	development					1115:1125	early development	1109:1125	early development	1109:1125	Together, these results provide insight into how OGT may regulate transcription in early development, possibly by modifying proteins important to maintain the ESC transcriptional repertoire.
21606357	0	54	theme	normal	51:56	arg1	distribution					81:92	the normal site-specific O-GlcNAc distribution	47:92	the normal site-specific O-GlcNAc distribution in mouse embryonic stem cells	47:122	Polycomb repressive complex 2 is necessary for the normal site-specific O-GlcNAc distribution in mouse embryonic stem cells.
21606357	1	55	theme	cellular	333:340	arg1	transduction					370:381	signal transduction	363:381	signal transduction	363:381	The monosaccharide addition of an N-acetylglucosamine to serine and threonine residues of nuclear and cytosolic proteins (O-GlcNAc) is a posttranslational modification emerging as a general regulator of many cellular processes, including signal transduction, cell division, and transcription.
21606357	1	55	theme	cellular	333:340	arg1	division					389:396	cell division	384:396	cell division	384:396	The monosaccharide addition of an N-acetylglucosamine to serine and threonine residues of nuclear and cytosolic proteins (O-GlcNAc) is a posttranslational modification emerging as a general regulator of many cellular processes, including signal transduction, cell division, and transcription.
21606357	1	55	theme	cellular	333:340	arg1	transcription					403:415	transcription	403:415	transcription	403:415	The monosaccharide addition of an N-acetylglucosamine to serine and threonine residues of nuclear and cytosolic proteins (O-GlcNAc) is a posttranslational modification emerging as a general regulator of many cellular processes, including signal transduction, cell division, and transcription.
21606357	1	55	theme	cellular	333:340	arg1	processes					342:350	many cellular processes	328:350	many cellular processes	328:350	The monosaccharide addition of an N-acetylglucosamine to serine and threonine residues of nuclear and cytosolic proteins (O-GlcNAc) is a posttranslational modification emerging as a general regulator of many cellular processes, including signal transduction, cell division, and transcription.
21606357	3	56	theme	proteins	605:612	arg1	O-GlcNAcylation					578:592	O-GlcNAcylation	578:592	O-GlcNAcylation of nuclear proteins in mouse embryonic stem cells (ESCs)	578:649	To understand the role of OGT in mouse development better, we mapped sites of O-GlcNAcylation of nuclear proteins in mouse embryonic stem cells (ESCs).
22245433	0	0	theme	certain	74:80	arg1	inhibitors					88:97	certain COX-2 inhibitors	74:97	certain COX-2 inhibitors	74:97	Glycosylation of human cyclooxygenase-2 (COX-2) decreases the efficacy of certain COX-2 inhibitors.
22245433	4	1	theme	COX-2	517:521	arg1	genes					523:527	the mutant and wild-type COX-2 genes	492:527	the mutant and wild-type COX-2 genes	492:527	In this study, Asn(580) was mutated, and the mutant and wild-type COX-2 genes were expressed in COS-1 cells to determine how glycosylation affects the inhibition of COX-2 activity by aspirin, flurbiprofen, ibuprofen, celecoxib, and etoricoxib.
22245433	4	2	theme	wild-type	507:515	arg1	genes					523:527	the mutant and wild-type COX-2 genes	492:527	the mutant and wild-type COX-2 genes	492:527	In this study, Asn(580) was mutated, and the mutant and wild-type COX-2 genes were expressed in COS-1 cells to determine how glycosylation affects the inhibition of COX-2 activity by aspirin, flurbiprofen, ibuprofen, celecoxib, and etoricoxib.
22245433	0	3	theme	inhibitors	88:97	arg1	efficacy					62:69	the efficacy	58:69	the efficacy of certain COX-2 inhibitors	58:97	Glycosylation of human cyclooxygenase-2 (COX-2) decreases the efficacy of certain COX-2 inhibitors.
22245433	3	4	gly	glycosylation	424:436	arg2	580					445:447	580	445:447	580	445:447	COX-2 exists as two glycoforms, 72 and 74 kDa, the latter resulting from an additional glycosylation at Asn(580).
22245433	3	4	gly	glycosylation	424:436	arg1	580					445:447	580	445:447	580	445:447	COX-2 exists as two glycoforms, 72 and 74 kDa, the latter resulting from an additional glycosylation at Asn(580).
22245433	3	4	gly	glycosylation	424:436	arg2	Asn					441:443	Asn	441:443	Asn(580)	441:448	COX-2 exists as two glycoforms, 72 and 74 kDa, the latter resulting from an additional glycosylation at Asn(580).
22245433	3	4	gly	glycosylation	424:436	arg1	Asn					441:443	Asn	441:443	Asn(580)	441:448	COX-2 exists as two glycoforms, 72 and 74 kDa, the latter resulting from an additional glycosylation at Asn(580).
22245433	0	5	theme	COX-2	82:86	arg1	inhibitors					88:97	certain COX-2 inhibitors	74:97	certain COX-2 inhibitors	74:97	Glycosylation of human cyclooxygenase-2 (COX-2) decreases the efficacy of certain COX-2 inhibitors.
22245433	5	6	gly	glycosylation	804:816	arg2	site					818:821	the glycosylation site	800:821	the glycosylation site	800:821	Results indicate that certain inhibitors were 2-5 times more effective at inhibiting COX-2 activity when the glycosylation site was eliminated, indicating that glycosylation of COX-2 at Asn(580) decreases the efficacy of some inhibitors.
22245433	5	7	theme	glycosylation	804:816	arg1	site					818:821	the glycosylation site	800:821	the glycosylation site	800:821	Results indicate that certain inhibitors were 2-5 times more effective at inhibiting COX-2 activity when the glycosylation site was eliminated, indicating that glycosylation of COX-2 at Asn(580) decreases the efficacy of some inhibitors.
22245433	1	8	theme	physiological	151:163	arg1	inflammation					208:219	inflammation	208:219	inflammation	208:219	Prostanoids play an important role in a variety of physiological and pathophysiological processes including inflammation and cancer.
22245433	1	8	theme	physiological	151:163	arg1	processes					188:196	physiological and pathophysiological processes	151:196	physiological and pathophysiological processes including inflammation and cancer	151:230	Prostanoids play an important role in a variety of physiological and pathophysiological processes including inflammation and cancer.
22245433	1	8	theme	physiological	151:163	arg1	cancer					225:230	cancer	225:230	cancer	225:230	Prostanoids play an important role in a variety of physiological and pathophysiological processes including inflammation and cancer.
22245433	2	9	from	step	251:254	arg1	pathway					287:293	the prostanoid biosynthesis pathway	259:293	the prostanoid biosynthesis pathway	259:293	The rate-limiting step in the prostanoid biosynthesis pathway is catalyzed by cyclooxygenase-2 (COX-2).
22245433	1	10	theme	pathophysiological	169:186	arg1	inflammation					208:219	inflammation	208:219	inflammation	208:219	Prostanoids play an important role in a variety of physiological and pathophysiological processes including inflammation and cancer.
22245433	1	10	theme	pathophysiological	169:186	arg1	processes					188:196	physiological and pathophysiological processes	151:196	physiological and pathophysiological processes including inflammation and cancer	151:230	Prostanoids play an important role in a variety of physiological and pathophysiological processes including inflammation and cancer.
22245433	1	10	theme	pathophysiological	169:186	arg1	cancer					225:230	cancer	225:230	cancer	225:230	Prostanoids play an important role in a variety of physiological and pathophysiological processes including inflammation and cancer.
22245433	4	11	gly	glycosylation	576:588	arg1	activity					622:629	COX-2 activity	616:629	COX-2 activity	616:629	In this study, Asn(580) was mutated, and the mutant and wild-type COX-2 genes were expressed in COS-1 cells to determine how glycosylation affects the inhibition of COX-2 activity by aspirin, flurbiprofen, ibuprofen, celecoxib, and etoricoxib.
22245433	3	12	theme	additional	413:422	arg1	glycosylation					424:436	an additional glycosylation	410:436	an additional glycosylation at Asn(580)	410:448	COX-2 exists as two glycoforms, 72 and 74 kDa, the latter resulting from an additional glycosylation at Asn(580).
22245433	0	13	theme	cyclooxygenase-2	23:38	arg1	Glycosylation					0:12	Glycosylation	0:12	Glycosylation of human cyclooxygenase-2 (COX-2)	0:46	Glycosylation of human cyclooxygenase-2 (COX-2) decreases the efficacy of certain COX-2 inhibitors.
22245433	5	14	gly	glycosylation	855:867	arg1	580					885:887	580	885:887	580	885:887	Results indicate that certain inhibitors were 2-5 times more effective at inhibiting COX-2 activity when the glycosylation site was eliminated, indicating that glycosylation of COX-2 at Asn(580) decreases the efficacy of some inhibitors.
22245433	5	14	gly	glycosylation	855:867	arg2	580					885:887	580	885:887	580	885:887	Results indicate that certain inhibitors were 2-5 times more effective at inhibiting COX-2 activity when the glycosylation site was eliminated, indicating that glycosylation of COX-2 at Asn(580) decreases the efficacy of some inhibitors.
22245433	5	14	gly	glycosylation	855:867	arg1	Asn					881:883	Asn	881:883	Asn(580)	881:888	Results indicate that certain inhibitors were 2-5 times more effective at inhibiting COX-2 activity when the glycosylation site was eliminated, indicating that glycosylation of COX-2 at Asn(580) decreases the efficacy of some inhibitors.
22245433	5	14	gly	glycosylation	855:867	arg2	Asn					881:883	Asn	881:883	Asn(580)	881:888	Results indicate that certain inhibitors were 2-5 times more effective at inhibiting COX-2 activity when the glycosylation site was eliminated, indicating that glycosylation of COX-2 at Asn(580) decreases the efficacy of some inhibitors.
22245433	5	14	gly	glycosylation	855:867	arg1	COX-2					872:876	COX-2	872:876	COX-2	872:876	Results indicate that certain inhibitors were 2-5 times more effective at inhibiting COX-2 activity when the glycosylation site was eliminated, indicating that glycosylation of COX-2 at Asn(580) decreases the efficacy of some inhibitors.
22245433	0	15	theme	human	17:21	arg1	COX-2					41:45	COX-2	41:45	COX-2	41:45	Glycosylation of human cyclooxygenase-2 (COX-2) decreases the efficacy of certain COX-2 inhibitors.
22245433	0	15	theme	human	17:21	arg1	cyclooxygenase-2					23:38	human cyclooxygenase-2	17:38	human cyclooxygenase-2 (COX-2)	17:46	Glycosylation of human cyclooxygenase-2 (COX-2) decreases the efficacy of certain COX-2 inhibitors.
22245433	4	16	theme	mutant	496:501	arg1	genes					523:527	the mutant and wild-type COX-2 genes	492:527	the mutant and wild-type COX-2 genes	492:527	In this study, Asn(580) was mutated, and the mutant and wild-type COX-2 genes were expressed in COS-1 cells to determine how glycosylation affects the inhibition of COX-2 activity by aspirin, flurbiprofen, ibuprofen, celecoxib, and etoricoxib.
22245433	0	17	gly	Glycosylation	0:12	arg1	COX-2					41:45	COX-2	41:45	COX-2	41:45	Glycosylation of human cyclooxygenase-2 (COX-2) decreases the efficacy of certain COX-2 inhibitors.
22245433	0	17	gly	Glycosylation	0:12	arg1	cyclooxygenase-2					23:38	human cyclooxygenase-2	17:38	human cyclooxygenase-2 (COX-2)	17:46	Glycosylation of human cyclooxygenase-2 (COX-2) decreases the efficacy of certain COX-2 inhibitors.
22245433	1	18	theme	processes	188:196	arg1	inflammation					208:219	inflammation	208:219	inflammation	208:219	Prostanoids play an important role in a variety of physiological and pathophysiological processes including inflammation and cancer.
22245433	1	18	theme	processes	188:196	arg1	processes					188:196	physiological and pathophysiological processes	151:196	physiological and pathophysiological processes including inflammation and cancer	151:230	Prostanoids play an important role in a variety of physiological and pathophysiological processes including inflammation and cancer.
22245433	1	18	theme	processes	188:196	arg1	variety					140:146	a variety	138:146	a variety of physiological and pathophysiological processes including inflammation and cancer	138:230	Prostanoids play an important role in a variety of physiological and pathophysiological processes including inflammation and cancer.
22245433	1	18	theme	processes	188:196	arg1	cancer					225:230	cancer	225:230	cancer	225:230	Prostanoids play an important role in a variety of physiological and pathophysiological processes including inflammation and cancer.
22245433	5	19	theme	COX-2	780:784	arg1	activity					786:793	COX-2 activity	780:793	COX-2 activity	780:793	Results indicate that certain inhibitors were 2-5 times more effective at inhibiting COX-2 activity when the glycosylation site was eliminated, indicating that glycosylation of COX-2 at Asn(580) decreases the efficacy of some inhibitors.
22245433	5	20	theme	certain	717:723	arg1	inhibitors					725:734	certain inhibitors	717:734	certain inhibitors	717:734	Results indicate that certain inhibitors were 2-5 times more effective at inhibiting COX-2 activity when the glycosylation site was eliminated, indicating that glycosylation of COX-2 at Asn(580) decreases the efficacy of some inhibitors.
22245433	2	21	theme	rate-limiting	237:249	arg1	step					251:254	The rate-limiting step	233:254	The rate-limiting step in the prostanoid biosynthesis pathway	233:293	The rate-limiting step in the prostanoid biosynthesis pathway is catalyzed by cyclooxygenase-2 (COX-2).
22245433	3	22	from	Asn	441:443	arg1	glycosylation					424:436	an additional glycosylation	410:436	an additional glycosylation at Asn(580)	410:448	COX-2 exists as two glycoforms, 72 and 74 kDa, the latter resulting from an additional glycosylation at Asn(580).
22245433	2	23	theme	biosynthesis	274:285	arg1	pathway					287:293	the prostanoid biosynthesis pathway	259:293	the prostanoid biosynthesis pathway	259:293	The rate-limiting step in the prostanoid biosynthesis pathway is catalyzed by cyclooxygenase-2 (COX-2).
22245433	1	24	theme	important	120:128	arg1	role					130:133	an important role	117:133	an important role	117:133	Prostanoids play an important role in a variety of physiological and pathophysiological processes including inflammation and cancer.
22245433	2	25	theme	prostanoid	263:272	arg1	pathway					287:293	the prostanoid biosynthesis pathway	259:293	the prostanoid biosynthesis pathway	259:293	The rate-limiting step in the prostanoid biosynthesis pathway is catalyzed by cyclooxygenase-2 (COX-2).
22245433	5	26	theme	COX-2	872:876	arg1	glycosylation					855:867	glycosylation	855:867	glycosylation of COX-2 at Asn(580)	855:888	Results indicate that certain inhibitors were 2-5 times more effective at inhibiting COX-2 activity when the glycosylation site was eliminated, indicating that glycosylation of COX-2 at Asn(580) decreases the efficacy of some inhibitors.
22245433	5	27	theme	inhibitors	921:930	arg1	efficacy					904:911	the efficacy	900:911	the efficacy of some inhibitors	900:930	Results indicate that certain inhibitors were 2-5 times more effective at inhibiting COX-2 activity when the glycosylation site was eliminated, indicating that glycosylation of COX-2 at Asn(580) decreases the efficacy of some inhibitors.
22245433	4	28	theme	activity	622:629	arg1	inhibition					602:611	the inhibition	598:611	the inhibition of COX-2 activity by aspirin, flurbiprofen, ibuprofen, celecoxib, and etoricoxib	598:692	In this study, Asn(580) was mutated, and the mutant and wild-type COX-2 genes were expressed in COS-1 cells to determine how glycosylation affects the inhibition of COX-2 activity by aspirin, flurbiprofen, ibuprofen, celecoxib, and etoricoxib.
22245433	5	29	from	Asn	881:883	arg1	glycosylation					855:867	glycosylation	855:867	glycosylation of COX-2 at Asn(580)	855:888	Results indicate that certain inhibitors were 2-5 times more effective at inhibiting COX-2 activity when the glycosylation site was eliminated, indicating that glycosylation of COX-2 at Asn(580) decreases the efficacy of some inhibitors.
22245433	5	30	theme	effective	756:764	arg1	times					745:749	2-5 times	741:749	2-5 times more effective	741:764	Results indicate that certain inhibitors were 2-5 times more effective at inhibiting COX-2 activity when the glycosylation site was eliminated, indicating that glycosylation of COX-2 at Asn(580) decreases the efficacy of some inhibitors.
22245433	4	31	theme	COX-2	616:620	arg1	activity					622:629	COX-2 activity	616:629	COX-2 activity	616:629	In this study, Asn(580) was mutated, and the mutant and wild-type COX-2 genes were expressed in COS-1 cells to determine how glycosylation affects the inhibition of COX-2 activity by aspirin, flurbiprofen, ibuprofen, celecoxib, and etoricoxib.
22245433	4	32	theme	COS-1	547:551	arg1	cells					553:557	COS-1 cells	547:557	COS-1 cells	547:557	In this study, Asn(580) was mutated, and the mutant and wild-type COX-2 genes were expressed in COS-1 cells to determine how glycosylation affects the inhibition of COX-2 activity by aspirin, flurbiprofen, ibuprofen, celecoxib, and etoricoxib.
20706749	0	0	theme	O-GlcNAc	77:84	arg1	antibody					90:97	a site-specific O-GlcNAc tau antibody	61:97	a site-specific O-GlcNAc tau antibody	61:97	Mapping O-GlcNAc modification sites on tau and generation of a site-specific O-GlcNAc tau antibody.
20706749	5	1	theme	IgG	858:860	arg1	3925					872:875	3925	872:875	3925	872:875	Using this information we have raised a rabbit polyclonal IgG antibody (3925) that detects tau O-GlcNAc modified at Ser-400.
20706749	5	1	theme	IgG	858:860	arg1	antibody					862:869	a rabbit polyclonal IgG antibody	838:869	a rabbit polyclonal IgG antibody (3925) that detects tau O-GlcNAc modified at Ser-400	838:922	Using this information we have raised a rabbit polyclonal IgG antibody (3925) that detects tau O-GlcNAc modified at Ser-400.
20706749	7	2	dep	in	1183:1184	arg1	vitro					1186:1190	vitro	1186:1190	vitro	1186:1190	The identification of these O-GlcNAc sites on tau and this antibody will enable both in vivo and in vitro experiments designed to understand the possible functional roles of O-GlcNAc on tau.
20706749	0	3	theme	site-specific	63:75	arg1	antibody					90:97	a site-specific O-GlcNAc tau antibody	61:97	a site-specific O-GlcNAc tau antibody	61:97	Mapping O-GlcNAc modification sites on tau and generation of a site-specific O-GlcNAc tau antibody.
20706749	7	4	theme	in	1171:1172	arg1	experiments					1192:1202	both in vivo and in vitro experiments	1166:1202	both in vivo and in vitro experiments designed to understand the possible functional roles of O-GlcNAc on tau	1166:1274	The identification of these O-GlcNAc sites on tau and this antibody will enable both in vivo and in vitro experiments designed to understand the possible functional roles of O-GlcNAc on tau.
20706749	1	5	theme	threonine	266:274	arg1	residues					276:283	certain serine and threonine residues	247:283	certain serine and threonine residues	247:283	The microtubule-associated protein tau is known to be post-translationally modified by the addition of N-acetyl-D: -glucosamine monosaccharides to certain serine and threonine residues.
20706749	0	6	theme	antibody	90:97	arg1	tau					39:41	tau	39:41	tau	39:41	Mapping O-GlcNAc modification sites on tau and generation of a site-specific O-GlcNAc tau antibody.
20706749	0	6	theme	antibody	90:97	arg1	generation					47:56	generation	47:56	generation	47:56	Mapping O-GlcNAc modification sites on tau and generation of a site-specific O-GlcNAc tau antibody.
20706749	4	7	from	presence	726:733	arg1	Ser-409					770:776	Ser-409	770:776	Ser-409	770:776	We have also detected the presence of a third O-GlcNAc site on either Ser-409, Ser-412, or Ser-413.
20706749	4	7	from	presence	726:733	arg1	Ser-412					779:785	Ser-412	779:785	Ser-412	779:785	We have also detected the presence of a third O-GlcNAc site on either Ser-409, Ser-412, or Ser-413.
20706749	4	7	from	presence	726:733	arg1	Ser-413					791:797	Ser-413	791:797	Ser-413	791:797	We have also detected the presence of a third O-GlcNAc site on either Ser-409, Ser-412, or Ser-413.
20706749	4	8	theme	third	740:744	arg1	site					755:758	a third O-GlcNAc site	738:758	a third O-GlcNAc site	738:758	We have also detected the presence of a third O-GlcNAc site on either Ser-409, Ser-412, or Ser-413.
20706749	5	9	from	Ser-400	916:922	arg1	modified					904:911	modified	904:911	modified	904:911	Using this information we have raised a rabbit polyclonal IgG antibody (3925) that detects tau O-GlcNAc modified at Ser-400.
20706749	0	10	theme	tau	86:88	arg1	antibody					90:97	a site-specific O-GlcNAc tau antibody	61:97	a site-specific O-GlcNAc tau antibody	61:97	Mapping O-GlcNAc modification sites on tau and generation of a site-specific O-GlcNAc tau antibody.
20706749	7	11	from	identification	1090:1103	arg1	tau					1132:1134	tau	1132:1134	tau	1132:1134	The identification of these O-GlcNAc sites on tau and this antibody will enable both in vivo and in vitro experiments designed to understand the possible functional roles of O-GlcNAc on tau.
20706749	7	11	from	identification	1090:1103	arg1	antibody					1145:1152	this antibody	1140:1152	this antibody	1140:1152	The identification of these O-GlcNAc sites on tau and this antibody will enable both in vivo and in vitro experiments designed to understand the possible functional roles of O-GlcNAc on tau.
20706749	3	12	theme	recombinant	557:567	arg1	tau					587:589	recombinant O-GlcNAc modified tau	557:589	recombinant O-GlcNAc modified tau	557:589	Here, we describe a method for the production of recombinant O-GlcNAc modified tau and, using this tau, we have mapped sites of O-GlcNAc on tau at Thr-123 and Ser-400 using mass spectrometry.
20706749	2	13	theme	modification	301:312	arg1	sites					314:318	These O-GlcNAc modification sites	286:318	These O-GlcNAc modification sites on tau	286:325	These O-GlcNAc modification sites on tau have been challenging to identify due to the inherent complexity of tau from mammalian brains and the fact that the O-GlcNAc modification typically has substoichiometric occupancy.
20706749	7	14	theme	sites	1123:1127	arg1	identification					1090:1103	The identification	1086:1103	The identification of these O-GlcNAc sites on tau and this antibody	1086:1152	The identification of these O-GlcNAc sites on tau and this antibody will enable both in vivo and in vitro experiments designed to understand the possible functional roles of O-GlcNAc on tau.
20706749	6	15	theme	O-GlcNAc	987:994	arg1	modification					996:1007	the Ser-400 tau O-GlcNAc modification	971:1007	the Ser-400 tau O-GlcNAc modification	971:1007	Further, using this antibody we have detected the Ser-400 tau O-GlcNAc modification in rat brain, which confirms the validity of this in vitro mapping approach.
20706749	2	16	theme	O-GlcNAc	292:299	arg1	sites					314:318	These O-GlcNAc modification sites	286:318	These O-GlcNAc modification sites on tau	286:325	These O-GlcNAc modification sites on tau have been challenging to identify due to the inherent complexity of tau from mammalian brains and the fact that the O-GlcNAc modification typically has substoichiometric occupancy.
20706749	6	17	theme	rat	1012:1014	arg1	brain					1016:1020	rat brain	1012:1020	rat brain	1012:1020	Further, using this antibody we have detected the Ser-400 tau O-GlcNAc modification in rat brain, which confirms the validity of this in vitro mapping approach.
20706749	2	18	theme	mammalian	404:412	arg1	brains					414:419	mammalian brains	404:419	mammalian brains	404:419	These O-GlcNAc modification sites on tau have been challenging to identify due to the inherent complexity of tau from mammalian brains and the fact that the O-GlcNAc modification typically has substoichiometric occupancy.
20706749	7	19	theme	possible	1231:1238	arg1	roles					1251:1255	the possible functional roles	1227:1255	the possible functional roles of O-GlcNAc on tau	1227:1274	The identification of these O-GlcNAc sites on tau and this antibody will enable both in vivo and in vitro experiments designed to understand the possible functional roles of O-GlcNAc on tau.
20706749	4	20	theme	O-GlcNAc	746:753	arg1	site					755:758	a third O-GlcNAc site	738:758	a third O-GlcNAc site	738:758	We have also detected the presence of a third O-GlcNAc site on either Ser-409, Ser-412, or Ser-413.
20706749	7	21	theme	O-GlcNAc	1260:1267	arg1	roles					1251:1255	the possible functional roles	1227:1255	the possible functional roles of O-GlcNAc on tau	1227:1274	The identification of these O-GlcNAc sites on tau and this antibody will enable both in vivo and in vitro experiments designed to understand the possible functional roles of O-GlcNAc on tau.
20706749	0	22	theme	O-GlcNAc	8:15	arg1	sites					30:34	O-GlcNAc modification sites	8:34	O-GlcNAc modification sites on tau and generation of a site-specific O-GlcNAc tau antibody	8:97	Mapping O-GlcNAc modification sites on tau and generation of a site-specific O-GlcNAc tau antibody.
20706749	6	23	dep	detected	962:969	arg1	using					934:938	using	934:938	using this antibody	934:952	Further, using this antibody we have detected the Ser-400 tau O-GlcNAc modification in rat brain, which confirms the validity of this in vitro mapping approach.
20706749	2	24	contain	has	475:477	arg2	occupancy					497:505	substoichiometric occupancy	479:505	substoichiometric occupancy	479:505	These O-GlcNAc modification sites on tau have been challenging to identify due to the inherent complexity of tau from mammalian brains and the fact that the O-GlcNAc modification typically has substoichiometric occupancy.
20706749	2	24	contain	has	475:477	arg1	modification					452:463	the O-GlcNAc modification	439:463	the O-GlcNAc modification	439:463	These O-GlcNAc modification sites on tau have been challenging to identify due to the inherent complexity of tau from mammalian brains and the fact that the O-GlcNAc modification typically has substoichiometric occupancy.
20706749	3	25	theme	tau	587:589	arg1	production					543:552	the production	539:552	the production of recombinant O-GlcNAc modified tau	539:589	Here, we describe a method for the production of recombinant O-GlcNAc modified tau and, using this tau, we have mapped sites of O-GlcNAc on tau at Thr-123 and Ser-400 using mass spectrometry.
20706749	2	26	theme	tau	395:397	arg1	fact					429:432	the fact that the O-GlcNAc modification typically has substoichiometric occupancy	425:505	the fact that the O-GlcNAc modification typically has substoichiometric occupancy	425:505	These O-GlcNAc modification sites on tau have been challenging to identify due to the inherent complexity of tau from mammalian brains and the fact that the O-GlcNAc modification typically has substoichiometric occupancy.
20706749	2	26	theme	tau	395:397	arg1	complexity					381:390	the inherent complexity	368:390	the inherent complexity of tau from mammalian brains	368:419	These O-GlcNAc modification sites on tau have been challenging to identify due to the inherent complexity of tau from mammalian brains and the fact that the O-GlcNAc modification typically has substoichiometric occupancy.
20706749	2	27	theme	O-GlcNAc	443:450	arg1	modification					452:463	the O-GlcNAc modification	439:463	the O-GlcNAc modification	439:463	These O-GlcNAc modification sites on tau have been challenging to identify due to the inherent complexity of tau from mammalian brains and the fact that the O-GlcNAc modification typically has substoichiometric occupancy.
20706749	2	28	from	complexity	381:390	arg1	brains					414:419	mammalian brains	404:419	mammalian brains	404:419	These O-GlcNAc modification sites on tau have been challenging to identify due to the inherent complexity of tau from mammalian brains and the fact that the O-GlcNAc modification typically has substoichiometric occupancy.
20706749	7	29	dep	in	1171:1172	arg1	vivo					1174:1177	vivo	1174:1177	vivo	1174:1177	The identification of these O-GlcNAc sites on tau and this antibody will enable both in vivo and in vitro experiments designed to understand the possible functional roles of O-GlcNAc on tau.
20706749	6	30	from	modification	996:1007	arg1	brain					1016:1020	rat brain	1012:1020	rat brain	1012:1020	Further, using this antibody we have detected the Ser-400 tau O-GlcNAc modification in rat brain, which confirms the validity of this in vitro mapping approach.
20706749	6	31	theme	mapping	1068:1074	arg1	approach					1076:1083	this in vitro mapping approach	1054:1083	this in vitro mapping approach	1054:1083	Further, using this antibody we have detected the Ser-400 tau O-GlcNAc modification in rat brain, which confirms the validity of this in vitro mapping approach.
20706749	6	32	theme	approach	1076:1083	arg1	validity					1042:1049	the validity	1038:1049	the validity of this in vitro mapping approach	1038:1083	Further, using this antibody we have detected the Ser-400 tau O-GlcNAc modification in rat brain, which confirms the validity of this in vitro mapping approach.
20706749	7	33	theme	functional	1240:1249	arg1	roles					1251:1255	the possible functional roles	1227:1255	the possible functional roles of O-GlcNAc on tau	1227:1274	The identification of these O-GlcNAc sites on tau and this antibody will enable both in vivo and in vitro experiments designed to understand the possible functional roles of O-GlcNAc on tau.
20706749	0	34	theme	modification	17:28	arg1	sites					30:34	O-GlcNAc modification sites	8:34	O-GlcNAc modification sites on tau and generation of a site-specific O-GlcNAc tau antibody	8:97	Mapping O-GlcNAc modification sites on tau and generation of a site-specific O-GlcNAc tau antibody.
20706749	4	35	theme	site	755:758	arg1	presence					726:733	the presence	722:733	the presence of a third O-GlcNAc site on either Ser-409, Ser-412, or Ser-413	722:797	We have also detected the presence of a third O-GlcNAc site on either Ser-409, Ser-412, or Ser-413.
20706749	3	36	theme	O-GlcNAc	636:643	arg1	O-GlcNAc					636:643	O-GlcNAc	636:643	O-GlcNAc	636:643	Here, we describe a method for the production of recombinant O-GlcNAc modified tau and, using this tau, we have mapped sites of O-GlcNAc on tau at Thr-123 and Ser-400 using mass spectrometry.
20706749	3	36	theme	O-GlcNAc	636:643	arg1	sites					627:631	sites	627:631	sites of O-GlcNAc on tau	627:650	Here, we describe a method for the production of recombinant O-GlcNAc modified tau and, using this tau, we have mapped sites of O-GlcNAc on tau at Thr-123 and Ser-400 using mass spectrometry.
20706749	3	37	theme	modified	578:585	arg1	tau					587:589	recombinant O-GlcNAc modified tau	557:589	recombinant O-GlcNAc modified tau	557:589	Here, we describe a method for the production of recombinant O-GlcNAc modified tau and, using this tau, we have mapped sites of O-GlcNAc on tau at Thr-123 and Ser-400 using mass spectrometry.
20706749	1	38	theme	N-acetyl-D	203:212	arg1	monosaccharides					228:242	N-acetyl-D: -glucosamine monosaccharides	203:242	N-acetyl-D: -glucosamine monosaccharides	203:242	The microtubule-associated protein tau is known to be post-translationally modified by the addition of N-acetyl-D: -glucosamine monosaccharides to certain serine and threonine residues.
20706749	6	39	theme	in	1059:1060	arg1	approach					1076:1083	this in vitro mapping approach	1054:1083	this in vitro mapping approach	1054:1083	Further, using this antibody we have detected the Ser-400 tau O-GlcNAc modification in rat brain, which confirms the validity of this in vitro mapping approach.
20706749	7	40	theme	O-GlcNAc	1114:1121	arg1	sites					1123:1127	these O-GlcNAc sites	1108:1127	these O-GlcNAc sites on tau and this antibody	1108:1152	The identification of these O-GlcNAc sites on tau and this antibody will enable both in vivo and in vitro experiments designed to understand the possible functional roles of O-GlcNAc on tau.
20706749	5	41	dep	raised	831:836	arg1	Using					800:804	Using	800:804	Using this information	800:821	Using this information we have raised a rabbit polyclonal IgG antibody (3925) that detects tau O-GlcNAc modified at Ser-400.
20706749	6	42	theme	tau	983:985	arg1	modification					996:1007	the Ser-400 tau O-GlcNAc modification	971:1007	the Ser-400 tau O-GlcNAc modification	971:1007	Further, using this antibody we have detected the Ser-400 tau O-GlcNAc modification in rat brain, which confirms the validity of this in vitro mapping approach.
20706749	2	43	theme	substoichiometric	479:495	arg1	occupancy					497:505	substoichiometric occupancy	479:505	substoichiometric occupancy	479:505	These O-GlcNAc modification sites on tau have been challenging to identify due to the inherent complexity of tau from mammalian brains and the fact that the O-GlcNAc modification typically has substoichiometric occupancy.
20706749	7	44	from	tau	1132:1134	arg1	identification					1090:1103	The identification	1086:1103	The identification of these O-GlcNAc sites on tau and this antibody	1086:1152	The identification of these O-GlcNAc sites on tau and this antibody will enable both in vivo and in vitro experiments designed to understand the possible functional roles of O-GlcNAc on tau.
20706749	1	45	theme	-glucosamine	215:226	arg1	monosaccharides					228:242	N-acetyl-D: -glucosamine monosaccharides	203:242	N-acetyl-D: -glucosamine monosaccharides	203:242	The microtubule-associated protein tau is known to be post-translationally modified by the addition of N-acetyl-D: -glucosamine monosaccharides to certain serine and threonine residues.
20706749	3	46	from	sites	627:631	arg1	tau					648:650	tau	648:650	tau	648:650	Here, we describe a method for the production of recombinant O-GlcNAc modified tau and, using this tau, we have mapped sites of O-GlcNAc on tau at Thr-123 and Ser-400 using mass spectrometry.
20706749	6	47	theme	Ser-400	975:981	arg1	modification					996:1007	the Ser-400 tau O-GlcNAc modification	971:1007	the Ser-400 tau O-GlcNAc modification	971:1007	Further, using this antibody we have detected the Ser-400 tau O-GlcNAc modification in rat brain, which confirms the validity of this in vitro mapping approach.
20706749	1	48	theme	microtubule-associated	104:125	arg1	tau					135:137	The microtubule-associated protein tau	100:137	The microtubule-associated protein tau	100:137	The microtubule-associated protein tau is known to be post-translationally modified by the addition of N-acetyl-D: -glucosamine monosaccharides to certain serine and threonine residues.
20706749	7	49	from	roles	1251:1255	arg1	tau					1272:1274	tau	1272:1274	tau	1272:1274	The identification of these O-GlcNAc sites on tau and this antibody will enable both in vivo and in vitro experiments designed to understand the possible functional roles of O-GlcNAc on tau.
20706749	4	50	attach	presence	726:733	arg2	site					755:758	a third O-GlcNAc site	738:758	a third O-GlcNAc site	738:758	We have also detected the presence of a third O-GlcNAc site on either Ser-409, Ser-412, or Ser-413.
20706749	4	50	attach	presence	726:733	arg1	Ser-409					770:776	Ser-409	770:776	Ser-409	770:776	We have also detected the presence of a third O-GlcNAc site on either Ser-409, Ser-412, or Ser-413.
20706749	4	50	attach	presence	726:733	arg1	Ser-412					779:785	Ser-412	779:785	Ser-412	779:785	We have also detected the presence of a third O-GlcNAc site on either Ser-409, Ser-412, or Ser-413.
20706749	4	50	attach	presence	726:733	arg1	Ser-413					791:797	Ser-413	791:797	Ser-413	791:797	We have also detected the presence of a third O-GlcNAc site on either Ser-409, Ser-412, or Ser-413.
20706749	3	51	theme	mass	681:684	arg1	spectrometry					686:697	mass spectrometry	681:697	mass spectrometry	681:697	Here, we describe a method for the production of recombinant O-GlcNAc modified tau and, using this tau, we have mapped sites of O-GlcNAc on tau at Thr-123 and Ser-400 using mass spectrometry.
20706749	1	52	theme	protein	127:133	arg1	tau					135:137	The microtubule-associated protein tau	100:137	The microtubule-associated protein tau	100:137	The microtubule-associated protein tau is known to be post-translationally modified by the addition of N-acetyl-D: -glucosamine monosaccharides to certain serine and threonine residues.
20706749	7	53	from	antibody	1145:1152	arg1	identification					1090:1103	The identification	1086:1103	The identification of these O-GlcNAc sites on tau and this antibody	1086:1152	The identification of these O-GlcNAc sites on tau and this antibody will enable both in vivo and in vitro experiments designed to understand the possible functional roles of O-GlcNAc on tau.
20706749	7	54	theme	in	1183:1184	arg1	experiments					1192:1202	both in vivo and in vitro experiments	1166:1202	both in vivo and in vitro experiments designed to understand the possible functional roles of O-GlcNAc on tau	1166:1274	The identification of these O-GlcNAc sites on tau and this antibody will enable both in vivo and in vitro experiments designed to understand the possible functional roles of O-GlcNAc on tau.
20706749	1	55	theme	monosaccharides	228:242	arg1	addition					191:198	the addition	187:198	the addition of N-acetyl-D: -glucosamine monosaccharides to certain serine and threonine residues	187:283	The microtubule-associated protein tau is known to be post-translationally modified by the addition of N-acetyl-D: -glucosamine monosaccharides to certain serine and threonine residues.
20706749	7	56	from	sites	1123:1127	arg1	tau					1132:1134	tau	1132:1134	tau	1132:1134	The identification of these O-GlcNAc sites on tau and this antibody will enable both in vivo and in vitro experiments designed to understand the possible functional roles of O-GlcNAc on tau.
20706749	7	56	from	sites	1123:1127	arg1	antibody					1145:1152	this antibody	1140:1152	this antibody	1140:1152	The identification of these O-GlcNAc sites on tau and this antibody will enable both in vivo and in vitro experiments designed to understand the possible functional roles of O-GlcNAc on tau.
20706749	1	57	mod	modified	175:182	arg1	tau					135:137	The microtubule-associated protein tau	100:137	The microtubule-associated protein tau	100:137	The microtubule-associated protein tau is known to be post-translationally modified by the addition of N-acetyl-D: -glucosamine monosaccharides to certain serine and threonine residues.
20706749	1	57	mod	modified	175:182	arg3	addition					191:198	the addition	187:198	the addition of N-acetyl-D: -glucosamine monosaccharides to certain serine and threonine residues	187:283	The microtubule-associated protein tau is known to be post-translationally modified by the addition of N-acetyl-D: -glucosamine monosaccharides to certain serine and threonine residues.
20706749	2	58	from	sites	314:318	arg1	tau					323:325	tau	323:325	tau	323:325	These O-GlcNAc modification sites on tau have been challenging to identify due to the inherent complexity of tau from mammalian brains and the fact that the O-GlcNAc modification typically has substoichiometric occupancy.
20706749	5	59	theme	polyclonal	847:856	arg1	3925					872:875	3925	872:875	3925	872:875	Using this information we have raised a rabbit polyclonal IgG antibody (3925) that detects tau O-GlcNAc modified at Ser-400.
20706749	5	59	theme	polyclonal	847:856	arg1	antibody					862:869	a rabbit polyclonal IgG antibody	838:869	a rabbit polyclonal IgG antibody (3925) that detects tau O-GlcNAc modified at Ser-400	838:922	Using this information we have raised a rabbit polyclonal IgG antibody (3925) that detects tau O-GlcNAc modified at Ser-400.
20706749	2	60	from	brains	414:419	arg1	fact					429:432	the fact that the O-GlcNAc modification typically has substoichiometric occupancy	425:505	the fact that the O-GlcNAc modification typically has substoichiometric occupancy	425:505	These O-GlcNAc modification sites on tau have been challenging to identify due to the inherent complexity of tau from mammalian brains and the fact that the O-GlcNAc modification typically has substoichiometric occupancy.
20706749	2	60	from	brains	414:419	arg1	tau					395:397	tau	395:397	tau from mammalian brains	395:419	These O-GlcNAc modification sites on tau have been challenging to identify due to the inherent complexity of tau from mammalian brains and the fact that the O-GlcNAc modification typically has substoichiometric occupancy.
20706749	2	60	from	brains	414:419	arg1	complexity					381:390	the inherent complexity	368:390	the inherent complexity of tau from mammalian brains	368:419	These O-GlcNAc modification sites on tau have been challenging to identify due to the inherent complexity of tau from mammalian brains and the fact that the O-GlcNAc modification typically has substoichiometric occupancy.
20706749	5	61	theme	rabbit	840:845	arg1	3925					872:875	3925	872:875	3925	872:875	Using this information we have raised a rabbit polyclonal IgG antibody (3925) that detects tau O-GlcNAc modified at Ser-400.
20706749	5	61	theme	rabbit	840:845	arg1	antibody					862:869	a rabbit polyclonal IgG antibody	838:869	a rabbit polyclonal IgG antibody (3925) that detects tau O-GlcNAc modified at Ser-400	838:922	Using this information we have raised a rabbit polyclonal IgG antibody (3925) that detects tau O-GlcNAc modified at Ser-400.
20706749	1	62	theme	certain	247:253	arg1	residues					276:283	certain serine and threonine residues	247:283	certain serine and threonine residues	247:283	The microtubule-associated protein tau is known to be post-translationally modified by the addition of N-acetyl-D: -glucosamine monosaccharides to certain serine and threonine residues.
20706749	0	63	from	sites	30:34	arg1	tau					39:41	tau	39:41	tau	39:41	Mapping O-GlcNAc modification sites on tau and generation of a site-specific O-GlcNAc tau antibody.
20706749	0	63	from	sites	30:34	arg1	generation					47:56	generation	47:56	generation	47:56	Mapping O-GlcNAc modification sites on tau and generation of a site-specific O-GlcNAc tau antibody.
20706749	6	64	dep	in	1059:1060	arg1	vitro					1062:1066	vitro	1062:1066	vitro	1062:1066	Further, using this antibody we have detected the Ser-400 tau O-GlcNAc modification in rat brain, which confirms the validity of this in vitro mapping approach.
20706749	2	65	from	fact	429:432	arg1	brains					414:419	mammalian brains	404:419	mammalian brains	404:419	These O-GlcNAc modification sites on tau have been challenging to identify due to the inherent complexity of tau from mammalian brains and the fact that the O-GlcNAc modification typically has substoichiometric occupancy.
20706749	2	66	theme	inherent	372:379	arg1	complexity					381:390	the inherent complexity	368:390	the inherent complexity of tau from mammalian brains	368:419	These O-GlcNAc modification sites on tau have been challenging to identify due to the inherent complexity of tau from mammalian brains and the fact that the O-GlcNAc modification typically has substoichiometric occupancy.
20706749	1	67	theme	serine	255:260	arg1	residues					276:283	certain serine and threonine residues	247:283	certain serine and threonine residues	247:283	The microtubule-associated protein tau is known to be post-translationally modified by the addition of N-acetyl-D: -glucosamine monosaccharides to certain serine and threonine residues.
19343721	7	0	from	tissues	1468:1474	arg1	uniform					1446:1452	uniform	1446:1452	uniform	1446:1452	The N-glycan structures found for tg-PC are very similar to those reported for a recombinant Factor IX produced in transgenic pig milk, and similar to the endogenous milk protein lactoferrin, which may indicate that N-glycan processing in the porcine mammary epithelial cells is more uniform than in other tissues.
19343721	3	1	theme	sialylated	716:725	arg1	N-glycans					630:638	The N-glycans	626:638	The N-glycans of tg-PC	626:647	The N-glycans of tg-PC are complex sialylated structures, but less branched and partially sialylated.
19343721	3	1	theme	sialylated	716:725	arg1	structures					672:681	complex sialylated structures	653:681	complex sialylated structures	653:681	The N-glycans of tg-PC are complex sialylated structures, but less branched and partially sialylated.
19343721	1	2	theme	different	459:467	arg1	levels					480:485	approximately tenfold different expression levels	437:485	approximately tenfold different expression levels	437:485	We have characterized the micro- and macro-heterogeneity of plasma-derived hPC and compared the glycosylation features with recombinant protein C (tg-PC) produced in a transgenic pig bioreactor from two animals having approximately tenfold different expression levels.
19343721	7	3	theme	N-glycan	1378:1385	arg1	processing					1387:1396	N-glycan processing	1378:1396	N-glycan processing in the porcine mammary epithelial cells	1378:1436	The N-glycan structures found for tg-PC are very similar to those reported for a recombinant Factor IX produced in transgenic pig milk, and similar to the endogenous milk protein lactoferrin, which may indicate that N-glycan processing in the porcine mammary epithelial cells is more uniform than in other tissues.
19343721	7	4	theme	mammary	1413:1419	arg1	cells					1432:1436	the porcine mammary epithelial cells	1401:1436	the porcine mammary epithelial cells	1401:1436	The N-glycan structures found for tg-PC are very similar to those reported for a recombinant Factor IX produced in transgenic pig milk, and similar to the endogenous milk protein lactoferrin, which may indicate that N-glycan processing in the porcine mammary epithelial cells is more uniform than in other tissues.
19343721	4	5	theme	high	859:862	arg1	levels					875:880	these high expression levels	853:880	these high expression levels	853:880	The porcine mammary epithelial cells glycosylate the Asn-X-Cys sequon with a similar efficiency as human hepatocytes even at these high expression levels, and site occupancy at this sequon was not affected by expression level.
19343721	2	6	theme	site	576:579	arg1	occupancy					581:589	78% site occupancy	572:589	78% site occupancy	572:589	The N-glycans of hPC are complex di- and tri-sialylated structures, and we measured 78% site occupancy at Asn-329 (the Asn-X-Cys sequon).
19343721	0	7	gly	occupancy	44:52	arg2	sequon					70:75	an Asn-X-Cys sequon	57:75	an Asn-X-Cys sequon	57:75	N-glycosylation microheterogeneity and site occupancy of an Asn-X-Cys sequon in plasma-derived and recombinant protein C. Human protein C (hPC) is glycosylated at three Asn-X-Ser/Thr and one atypical Asn-X-Cys sequons.
19343721	0	7	gly	occupancy	44:52	arg1	sequon					70:75	an Asn-X-Cys sequon	57:75	an Asn-X-Cys sequon	57:75	N-glycosylation microheterogeneity and site occupancy of an Asn-X-Cys sequon in plasma-derived and recombinant protein C. Human protein C (hPC) is glycosylated at three Asn-X-Ser/Thr and one atypical Asn-X-Cys sequons.
19343721	0	7	gly	occupancy	44:52	arg2	site					39:42	site occupancy	39:52	site occupancy	39:52	N-glycosylation microheterogeneity and site occupancy of an Asn-X-Cys sequon in plasma-derived and recombinant protein C. Human protein C (hPC) is glycosylated at three Asn-X-Ser/Thr and one atypical Asn-X-Cys sequons.
19343721	0	8	theme	protein	128:134	arg1	hPC					139:141	hPC	139:141	hPC	139:141	N-glycosylation microheterogeneity and site occupancy of an Asn-X-Cys sequon in plasma-derived and recombinant protein C. Human protein C (hPC) is glycosylated at three Asn-X-Ser/Thr and one atypical Asn-X-Cys sequons.
19343721	0	8	theme	protein	128:134	arg1	C					136:136	plasma-derived and recombinant protein C. Human protein C	80:136	plasma-derived and recombinant protein C. Human protein C (hPC)	80:142	N-glycosylation microheterogeneity and site occupancy of an Asn-X-Cys sequon in plasma-derived and recombinant protein C. Human protein C (hPC) is glycosylated at three Asn-X-Ser/Thr and one atypical Asn-X-Cys sequons.
19343721	1	9	theme	pig	398:400	arg1	bioreactor					402:411	a transgenic pig bioreactor	385:411	a transgenic pig bioreactor	385:411	We have characterized the micro- and macro-heterogeneity of plasma-derived hPC and compared the glycosylation features with recombinant protein C (tg-PC) produced in a transgenic pig bioreactor from two animals having approximately tenfold different expression levels.
19343721	7	10	from	uniform	1446:1452	arg1	tissues					1468:1474	other tissues	1462:1474	other tissues	1462:1474	The N-glycan structures found for tg-PC are very similar to those reported for a recombinant Factor IX produced in transgenic pig milk, and similar to the endogenous milk protein lactoferrin, which may indicate that N-glycan processing in the porcine mammary epithelial cells is more uniform than in other tissues.
19343721	7	11	theme	milk	1328:1331	arg1	lactoferrin					1341:1351	the endogenous milk protein lactoferrin	1313:1351	the endogenous milk protein lactoferrin	1313:1351	The N-glycan structures found for tg-PC are very similar to those reported for a recombinant Factor IX produced in transgenic pig milk, and similar to the endogenous milk protein lactoferrin, which may indicate that N-glycan processing in the porcine mammary epithelial cells is more uniform than in other tissues.
19343721	2	12	theme	%	574:574	arg1	occupancy					581:589	78% site occupancy	572:589	78% site occupancy	572:589	The N-glycans of hPC are complex di- and tri-sialylated structures, and we measured 78% site occupancy at Asn-329 (the Asn-X-Cys sequon).
19343721	6	13	attach	predominant	1129:1139	arg1	site					1156:1159	the Asn-329 site	1144:1159	the Asn-329 site	1144:1159	Interestingly, glycans with GalNAc in the antennae were predominant at the Asn-329 site.
19343721	6	13	attach	predominant	1129:1139	arg2	glycans					1088:1094	glycans	1088:1094	glycans with GalNAc in the antennae	1088:1122	Interestingly, glycans with GalNAc in the antennae were predominant at the Asn-329 site.
19343721	2	14	theme	complex	513:519	arg1	N-glycans					492:500	The N-glycans	488:500	The N-glycans of hPC	488:507	The N-glycans of hPC are complex di- and tri-sialylated structures, and we measured 78% site occupancy at Asn-329 (the Asn-X-Cys sequon).
19343721	2	14	theme	complex	513:519	arg1	structures					544:553	complex di- and tri-sialylated structures	513:553	complex di- and tri-sialylated structures	513:553	The N-glycans of hPC are complex di- and tri-sialylated structures, and we measured 78% site occupancy at Asn-329 (the Asn-X-Cys sequon).
19343721	4	15	gly	glycosylate	765:775	arg1	sequon					791:796	the Asn-X-Cys sequon	777:796	the Asn-X-Cys sequon	777:796	The porcine mammary epithelial cells glycosylate the Asn-X-Cys sequon with a similar efficiency as human hepatocytes even at these high expression levels, and site occupancy at this sequon was not affected by expression level.
19343721	1	16	theme	recombinant	343:353	arg1	C					363:363	recombinant protein C	343:363	recombinant protein C (tg-PC) produced in a transgenic pig bioreactor from two animals having approximately tenfold different expression levels	343:485	We have characterized the micro- and macro-heterogeneity of plasma-derived hPC and compared the glycosylation features with recombinant protein C (tg-PC) produced in a transgenic pig bioreactor from two animals having approximately tenfold different expression levels.
19343721	1	16	theme	recombinant	343:353	arg1	tg-PC					366:370	tg-PC	366:370	tg-PC	366:370	We have characterized the micro- and macro-heterogeneity of plasma-derived hPC and compared the glycosylation features with recombinant protein C (tg-PC) produced in a transgenic pig bioreactor from two animals having approximately tenfold different expression levels.
19343721	2	17	theme	hPC	505:507	arg1	structures					544:553	complex di- and tri-sialylated structures	513:553	complex di- and tri-sialylated structures	513:553	The N-glycans of hPC are complex di- and tri-sialylated structures, and we measured 78% site occupancy at Asn-329 (the Asn-X-Cys sequon).
19343721	2	17	theme	hPC	505:507	arg1	N-glycans					492:500	The N-glycans	488:500	The N-glycans of hPC	488:507	The N-glycans of hPC are complex di- and tri-sialylated structures, and we measured 78% site occupancy at Asn-329 (the Asn-X-Cys sequon).
19343721	0	18	theme	plasma-derived	80:93	arg1	hPC					139:141	hPC	139:141	hPC	139:141	N-glycosylation microheterogeneity and site occupancy of an Asn-X-Cys sequon in plasma-derived and recombinant protein C. Human protein C (hPC) is glycosylated at three Asn-X-Ser/Thr and one atypical Asn-X-Cys sequons.
19343721	0	18	theme	plasma-derived	80:93	arg1	C					136:136	plasma-derived and recombinant protein C. Human protein C	80:136	plasma-derived and recombinant protein C. Human protein C (hPC)	80:142	N-glycosylation microheterogeneity and site occupancy of an Asn-X-Cys sequon in plasma-derived and recombinant protein C. Human protein C (hPC) is glycosylated at three Asn-X-Ser/Thr and one atypical Asn-X-Cys sequons.
19343721	4	19	theme	expression	937:946	arg1	level					948:952	expression level	937:952	expression level	937:952	The porcine mammary epithelial cells glycosylate the Asn-X-Cys sequon with a similar efficiency as human hepatocytes even at these high expression levels, and site occupancy at this sequon was not affected by expression level.
19343721	0	20	theme	recombinant	99:109	arg1	hPC					139:141	hPC	139:141	hPC	139:141	N-glycosylation microheterogeneity and site occupancy of an Asn-X-Cys sequon in plasma-derived and recombinant protein C. Human protein C (hPC) is glycosylated at three Asn-X-Ser/Thr and one atypical Asn-X-Cys sequons.
19343721	0	20	theme	recombinant	99:109	arg1	C					136:136	plasma-derived and recombinant protein C. Human protein C	80:136	plasma-derived and recombinant protein C. Human protein C (hPC)	80:142	N-glycosylation microheterogeneity and site occupancy of an Asn-X-Cys sequon in plasma-derived and recombinant protein C. Human protein C (hPC) is glycosylated at three Asn-X-Ser/Thr and one atypical Asn-X-Cys sequons.
19343721	5	21	theme	distinct	957:964	arg1	present					1001:1007	present	1001:1007	present	1001:1007	A distinct bias for particular structures was present at each of the four glycosylation sites for both hPC and tg-PC.
19343721	5	21	theme	distinct	957:964	arg1	bias					966:969	A distinct bias	955:969	A distinct bias for particular structures	955:995	A distinct bias for particular structures was present at each of the four glycosylation sites for both hPC and tg-PC.
19343721	4	22	theme	Asn-X-Cys	781:789	arg1	sequon					791:796	the Asn-X-Cys sequon	777:796	the Asn-X-Cys sequon	777:796	The porcine mammary epithelial cells glycosylate the Asn-X-Cys sequon with a similar efficiency as human hepatocytes even at these high expression levels, and site occupancy at this sequon was not affected by expression level.
19343721	7	23	theme	N-glycan	1166:1173	arg1	structures					1175:1184	The N-glycan structures	1162:1184	The N-glycan structures found for tg-PC	1162:1200	The N-glycan structures found for tg-PC are very similar to those reported for a recombinant Factor IX produced in transgenic pig milk, and similar to the endogenous milk protein lactoferrin, which may indicate that N-glycan processing in the porcine mammary epithelial cells is more uniform than in other tissues.
19343721	7	23	theme	N-glycan	1166:1173	arg1	similar					1211:1217	similar	1211:1217	similar	1211:1217	The N-glycan structures found for tg-PC are very similar to those reported for a recombinant Factor IX produced in transgenic pig milk, and similar to the endogenous milk protein lactoferrin, which may indicate that N-glycan processing in the porcine mammary epithelial cells is more uniform than in other tissues.
19343721	0	24	from	occupancy	44:52	arg1	hPC					139:141	hPC	139:141	hPC	139:141	N-glycosylation microheterogeneity and site occupancy of an Asn-X-Cys sequon in plasma-derived and recombinant protein C. Human protein C (hPC) is glycosylated at three Asn-X-Ser/Thr and one atypical Asn-X-Cys sequons.
19343721	0	24	from	occupancy	44:52	arg1	C					136:136	plasma-derived and recombinant protein C. Human protein C	80:136	plasma-derived and recombinant protein C. Human protein C (hPC)	80:142	N-glycosylation microheterogeneity and site occupancy of an Asn-X-Cys sequon in plasma-derived and recombinant protein C. Human protein C (hPC) is glycosylated at three Asn-X-Ser/Thr and one atypical Asn-X-Cys sequons.
19343721	4	25	theme	porcine	732:738	arg1	cells					759:763	The porcine mammary epithelial cells	728:763	The porcine mammary epithelial cells	728:763	The porcine mammary epithelial cells glycosylate the Asn-X-Cys sequon with a similar efficiency as human hepatocytes even at these high expression levels, and site occupancy at this sequon was not affected by expression level.
19343721	6	26	from	site	1156:1159	arg1	predominant					1129:1139	predominant	1129:1139	predominant	1129:1139	Interestingly, glycans with GalNAc in the antennae were predominant at the Asn-329 site.
19343721	0	27	theme	N-glycosylation	0:14	arg1	microheterogeneity					16:33	N-glycosylation microheterogeneity	0:33	N-glycosylation microheterogeneity	0:33	N-glycosylation microheterogeneity and site occupancy of an Asn-X-Cys sequon in plasma-derived and recombinant protein C. Human protein C (hPC) is glycosylated at three Asn-X-Ser/Thr and one atypical Asn-X-Cys sequons.
19343721	1	28	theme	plasma-derived	279:292	arg1	hPC					294:296	plasma-derived hPC	279:296	plasma-derived hPC	279:296	We have characterized the micro- and macro-heterogeneity of plasma-derived hPC and compared the glycosylation features with recombinant protein C (tg-PC) produced in a transgenic pig bioreactor from two animals having approximately tenfold different expression levels.
19343721	3	29	gly	sialylated	716:725	arg1	N-glycans					630:638	The N-glycans	626:638	The N-glycans of tg-PC	626:647	The N-glycans of tg-PC are complex sialylated structures, but less branched and partially sialylated.
19343721	3	29	gly	sialylated	716:725	arg1	structures					672:681	complex sialylated structures	653:681	complex sialylated structures	653:681	The N-glycans of tg-PC are complex sialylated structures, but less branched and partially sialylated.
19343721	4	30	theme	epithelial	748:757	arg1	cells					759:763	The porcine mammary epithelial cells	728:763	The porcine mammary epithelial cells	728:763	The porcine mammary epithelial cells glycosylate the Asn-X-Cys sequon with a similar efficiency as human hepatocytes even at these high expression levels, and site occupancy at this sequon was not affected by expression level.
19343721	1	31	contain	having	430:435	arg1	animals					422:428	two animals	418:428	two animals having approximately tenfold different expression levels	418:485	We have characterized the micro- and macro-heterogeneity of plasma-derived hPC and compared the glycosylation features with recombinant protein C (tg-PC) produced in a transgenic pig bioreactor from two animals having approximately tenfold different expression levels.
19343721	1	31	contain	having	430:435	arg2	levels					480:485	approximately tenfold different expression levels	437:485	approximately tenfold different expression levels	437:485	We have characterized the micro- and macro-heterogeneity of plasma-derived hPC and compared the glycosylation features with recombinant protein C (tg-PC) produced in a transgenic pig bioreactor from two animals having approximately tenfold different expression levels.
19343721	6	32	theme	Asn-329	1148:1154	arg1	site					1156:1159	the Asn-329 site	1144:1159	the Asn-329 site	1144:1159	Interestingly, glycans with GalNAc in the antennae were predominant at the Asn-329 site.
19343721	7	33	theme	transgenic	1277:1286	arg1	milk					1292:1295	transgenic pig milk	1277:1295	transgenic pig milk	1277:1295	The N-glycan structures found for tg-PC are very similar to those reported for a recombinant Factor IX produced in transgenic pig milk, and similar to the endogenous milk protein lactoferrin, which may indicate that N-glycan processing in the porcine mammary epithelial cells is more uniform than in other tissues.
19343721	3	34	theme	tg-PC	643:647	arg1	N-glycans					630:638	The N-glycans	626:638	The N-glycans of tg-PC	626:647	The N-glycans of tg-PC are complex sialylated structures, but less branched and partially sialylated.
19343721	3	34	theme	tg-PC	643:647	arg1	structures					672:681	complex sialylated structures	653:681	complex sialylated structures	653:681	The N-glycans of tg-PC are complex sialylated structures, but less branched and partially sialylated.
19343721	0	35	gly	microheterogeneity	16:33	arg1	sequon					70:75	an Asn-X-Cys sequon	57:75	an Asn-X-Cys sequon	57:75	N-glycosylation microheterogeneity and site occupancy of an Asn-X-Cys sequon in plasma-derived and recombinant protein C. Human protein C (hPC) is glycosylated at three Asn-X-Ser/Thr and one atypical Asn-X-Cys sequons.
19343721	0	36	theme	sequon	70:75	arg1	microheterogeneity					16:33	N-glycosylation microheterogeneity	0:33	N-glycosylation microheterogeneity	0:33	N-glycosylation microheterogeneity and site occupancy of an Asn-X-Cys sequon in plasma-derived and recombinant protein C. Human protein C (hPC) is glycosylated at three Asn-X-Ser/Thr and one atypical Asn-X-Cys sequons.
19343721	0	36	theme	sequon	70:75	arg1	occupancy					44:52	site occupancy	39:52	site occupancy	39:52	N-glycosylation microheterogeneity and site occupancy of an Asn-X-Cys sequon in plasma-derived and recombinant protein C. Human protein C (hPC) is glycosylated at three Asn-X-Ser/Thr and one atypical Asn-X-Cys sequons.
19343721	6	37	with	glycans	1088:1094	arg1	GalNAc					1101:1106	GalNAc	1101:1106	GalNAc	1101:1106	Interestingly, glycans with GalNAc in the antennae were predominant at the Asn-329 site.
19343721	7	38	theme	Factor	1255:1260	arg1	IX					1262:1263	a recombinant Factor IX	1241:1263	a recombinant Factor IX produced in transgenic pig milk	1241:1295	The N-glycan structures found for tg-PC are very similar to those reported for a recombinant Factor IX produced in transgenic pig milk, and similar to the endogenous milk protein lactoferrin, which may indicate that N-glycan processing in the porcine mammary epithelial cells is more uniform than in other tissues.
19343721	3	39	gly	sialylated	661:670	arg1	N-glycans					630:638	The N-glycans	626:638	The N-glycans of tg-PC	626:647	The N-glycans of tg-PC are complex sialylated structures, but less branched and partially sialylated.
19343721	3	39	gly	sialylated	661:670	arg1	structures					672:681	complex sialylated structures	653:681	complex sialylated structures	653:681	The N-glycans of tg-PC are complex sialylated structures, but less branched and partially sialylated.
19343721	3	40	theme	complex	653:659	arg1	N-glycans					630:638	The N-glycans	626:638	The N-glycans of tg-PC	626:647	The N-glycans of tg-PC are complex sialylated structures, but less branched and partially sialylated.
19343721	3	40	theme	complex	653:659	arg1	structures					672:681	complex sialylated structures	653:681	complex sialylated structures	653:681	The N-glycans of tg-PC are complex sialylated structures, but less branched and partially sialylated.
19343721	4	41	theme	similar	805:811	arg1	efficiency					813:822	a similar efficiency	803:822	a similar efficiency as human hepatocytes	803:843	The porcine mammary epithelial cells glycosylate the Asn-X-Cys sequon with a similar efficiency as human hepatocytes even at these high expression levels, and site occupancy at this sequon was not affected by expression level.
19343721	5	42	gly	glycosylation	1029:1041	arg2	four					1024:1027	four	1024:1027	four	1024:1027	A distinct bias for particular structures was present at each of the four glycosylation sites for both hPC and tg-PC.
19343721	5	42	gly	glycosylation	1029:1041	arg2	sites					1043:1047	the four glycosylation sites	1020:1047	the four glycosylation sites for both hPC and tg-PC	1020:1070	A distinct bias for particular structures was present at each of the four glycosylation sites for both hPC and tg-PC.
19343721	3	43	theme	branched	693:700	arg1	N-glycans					630:638	The N-glycans	626:638	The N-glycans of tg-PC	626:647	The N-glycans of tg-PC are complex sialylated structures, but less branched and partially sialylated.
19343721	3	43	theme	branched	693:700	arg1	structures					672:681	complex sialylated structures	653:681	complex sialylated structures	653:681	The N-glycans of tg-PC are complex sialylated structures, but less branched and partially sialylated.
19343721	4	44	theme	expression	864:873	arg1	levels					875:880	these high expression levels	853:880	these high expression levels	853:880	The porcine mammary epithelial cells glycosylate the Asn-X-Cys sequon with a similar efficiency as human hepatocytes even at these high expression levels, and site occupancy at this sequon was not affected by expression level.
19343721	1	45	with	features	329:336	arg1	C					363:363	recombinant protein C	343:363	recombinant protein C (tg-PC) produced in a transgenic pig bioreactor from two animals having approximately tenfold different expression levels	343:485	We have characterized the micro- and macro-heterogeneity of plasma-derived hPC and compared the glycosylation features with recombinant protein C (tg-PC) produced in a transgenic pig bioreactor from two animals having approximately tenfold different expression levels.
19343721	1	45	with	features	329:336	arg1	tg-PC					366:370	tg-PC	366:370	tg-PC	366:370	We have characterized the micro- and macro-heterogeneity of plasma-derived hPC and compared the glycosylation features with recombinant protein C (tg-PC) produced in a transgenic pig bioreactor from two animals having approximately tenfold different expression levels.
19343721	1	46	theme	tenfold	451:457	arg1	levels					480:485	approximately tenfold different expression levels	437:485	approximately tenfold different expression levels	437:485	We have characterized the micro- and macro-heterogeneity of plasma-derived hPC and compared the glycosylation features with recombinant protein C (tg-PC) produced in a transgenic pig bioreactor from two animals having approximately tenfold different expression levels.
19343721	5	47	located	present	1001:1007	arg1	sites					1043:1047	the four glycosylation sites	1020:1047	the four glycosylation sites for both hPC and tg-PC	1020:1070	A distinct bias for particular structures was present at each of the four glycosylation sites for both hPC and tg-PC.
19343721	5	47	located	present	1001:1007	arg1	each					1012:1015	each	1012:1015	each	1012:1015	A distinct bias for particular structures was present at each of the four glycosylation sites for both hPC and tg-PC.
19343721	5	47	located	present	1001:1007	arg2	bias					966:969	A distinct bias	955:969	A distinct bias for particular structures	955:995	A distinct bias for particular structures was present at each of the four glycosylation sites for both hPC and tg-PC.
19343721	5	47	located	present	1001:1007	arg2	present					1001:1007	present	1001:1007	present	1001:1007	A distinct bias for particular structures was present at each of the four glycosylation sites for both hPC and tg-PC.
19343721	7	48	theme	epithelial	1421:1430	arg1	cells					1432:1436	the porcine mammary epithelial cells	1401:1436	the porcine mammary epithelial cells	1401:1436	The N-glycan structures found for tg-PC are very similar to those reported for a recombinant Factor IX produced in transgenic pig milk, and similar to the endogenous milk protein lactoferrin, which may indicate that N-glycan processing in the porcine mammary epithelial cells is more uniform than in other tissues.
19343721	1	49	theme	expression	469:478	arg1	levels					480:485	approximately tenfold different expression levels	437:485	approximately tenfold different expression levels	437:485	We have characterized the micro- and macro-heterogeneity of plasma-derived hPC and compared the glycosylation features with recombinant protein C (tg-PC) produced in a transgenic pig bioreactor from two animals having approximately tenfold different expression levels.
19343721	7	50	theme	porcine	1405:1411	arg1	cells					1432:1436	the porcine mammary epithelial cells	1401:1436	the porcine mammary epithelial cells	1401:1436	The N-glycan structures found for tg-PC are very similar to those reported for a recombinant Factor IX produced in transgenic pig milk, and similar to the endogenous milk protein lactoferrin, which may indicate that N-glycan processing in the porcine mammary epithelial cells is more uniform than in other tissues.
19343721	2	51	theme	Asn-X-Cys	607:615	arg1	sequon					617:622	the Asn-X-Cys sequon	603:622	the Asn-X-Cys sequon	603:622	The N-glycans of hPC are complex di- and tri-sialylated structures, and we measured 78% site occupancy at Asn-329 (the Asn-X-Cys sequon).
19343721	2	51	theme	Asn-X-Cys	607:615	arg1	Asn-329					594:600	Asn-329	594:600	Asn-329 (the Asn-X-Cys sequon)	594:623	The N-glycans of hPC are complex di- and tri-sialylated structures, and we measured 78% site occupancy at Asn-329 (the Asn-X-Cys sequon).
19343721	1	52	theme	transgenic	387:396	arg1	bioreactor					402:411	a transgenic pig bioreactor	385:411	a transgenic pig bioreactor	385:411	We have characterized the micro- and macro-heterogeneity of plasma-derived hPC and compared the glycosylation features with recombinant protein C (tg-PC) produced in a transgenic pig bioreactor from two animals having approximately tenfold different expression levels.
19343721	5	53	from	each	1012:1015	arg1	present					1001:1007	present	1001:1007	present	1001:1007	A distinct bias for particular structures was present at each of the four glycosylation sites for both hPC and tg-PC.
19343721	5	53	from	each	1012:1015	arg1	bias					966:969	A distinct bias	955:969	A distinct bias for particular structures	955:995	A distinct bias for particular structures was present at each of the four glycosylation sites for both hPC and tg-PC.
19343721	0	54	dep	Asn-X-Ser/Thr	169:181	arg1	sequons					210:216	sequons	210:216	sequons	210:216	N-glycosylation microheterogeneity and site occupancy of an Asn-X-Cys sequon in plasma-derived and recombinant protein C. Human protein C (hPC) is glycosylated at three Asn-X-Ser/Thr and one atypical Asn-X-Cys sequons.
19343721	4	55	from	sequon	910:915	arg1	occupancy					892:900	site occupancy	887:900	site occupancy at this sequon	887:915	The porcine mammary epithelial cells glycosylate the Asn-X-Cys sequon with a similar efficiency as human hepatocytes even at these high expression levels, and site occupancy at this sequon was not affected by expression level.
19343721	4	56	theme	site	887:890	arg1	occupancy					892:900	site occupancy	887:900	site occupancy at this sequon	887:915	The porcine mammary epithelial cells glycosylate the Asn-X-Cys sequon with a similar efficiency as human hepatocytes even at these high expression levels, and site occupancy at this sequon was not affected by expression level.
19343721	7	57	theme	protein	1333:1339	arg1	lactoferrin					1341:1351	the endogenous milk protein lactoferrin	1313:1351	the endogenous milk protein lactoferrin	1313:1351	The N-glycan structures found for tg-PC are very similar to those reported for a recombinant Factor IX produced in transgenic pig milk, and similar to the endogenous milk protein lactoferrin, which may indicate that N-glycan processing in the porcine mammary epithelial cells is more uniform than in other tissues.
19343721	5	58	theme	glycosylation	1029:1041	arg1	sites					1043:1047	the four glycosylation sites	1020:1047	the four glycosylation sites for both hPC and tg-PC	1020:1070	A distinct bias for particular structures was present at each of the four glycosylation sites for both hPC and tg-PC.
19343721	2	59	theme	78	572:573	arg1	%					574:574	%	574:574	%	574:574	The N-glycans of hPC are complex di- and tri-sialylated structures, and we measured 78% site occupancy at Asn-329 (the Asn-X-Cys sequon).
19343721	1	60	dep	micro-	245:250	arg1	the					241:243	the	241:243	the	241:243	We have characterized the micro- and macro-heterogeneity of plasma-derived hPC and compared the glycosylation features with recombinant protein C (tg-PC) produced in a transgenic pig bioreactor from two animals having approximately tenfold different expression levels.
19343721	7	61	theme	endogenous	1317:1326	arg1	lactoferrin					1341:1351	the endogenous milk protein lactoferrin	1313:1351	the endogenous milk protein lactoferrin	1313:1351	The N-glycan structures found for tg-PC are very similar to those reported for a recombinant Factor IX produced in transgenic pig milk, and similar to the endogenous milk protein lactoferrin, which may indicate that N-glycan processing in the porcine mammary epithelial cells is more uniform than in other tissues.
19343721	1	62	theme	protein	355:361	arg1	C					363:363	recombinant protein C	343:363	recombinant protein C (tg-PC) produced in a transgenic pig bioreactor from two animals having approximately tenfold different expression levels	343:485	We have characterized the micro- and macro-heterogeneity of plasma-derived hPC and compared the glycosylation features with recombinant protein C (tg-PC) produced in a transgenic pig bioreactor from two animals having approximately tenfold different expression levels.
19343721	1	62	theme	protein	355:361	arg1	tg-PC					366:370	tg-PC	366:370	tg-PC	366:370	We have characterized the micro- and macro-heterogeneity of plasma-derived hPC and compared the glycosylation features with recombinant protein C (tg-PC) produced in a transgenic pig bioreactor from two animals having approximately tenfold different expression levels.
19343721	0	63	gly	glycosylated	147:158	arg2	Asn-X-Cys					200:208	Asn-X-Cys	200:208	Asn-X-Cys	200:208	N-glycosylation microheterogeneity and site occupancy of an Asn-X-Cys sequon in plasma-derived and recombinant protein C. Human protein C (hPC) is glycosylated at three Asn-X-Ser/Thr and one atypical Asn-X-Cys sequons.
19343721	0	63	gly	glycosylated	147:158	arg2	Asn-X-Ser/Thr					169:181	Asn-X-Ser/Thr	169:181	Asn-X-Ser/Thr	169:181	N-glycosylation microheterogeneity and site occupancy of an Asn-X-Cys sequon in plasma-derived and recombinant protein C. Human protein C (hPC) is glycosylated at three Asn-X-Ser/Thr and one atypical Asn-X-Cys sequons.
19343721	0	63	gly	glycosylated	147:158	arg1	microheterogeneity					16:33	N-glycosylation microheterogeneity	0:33	N-glycosylation microheterogeneity	0:33	N-glycosylation microheterogeneity and site occupancy of an Asn-X-Cys sequon in plasma-derived and recombinant protein C. Human protein C (hPC) is glycosylated at three Asn-X-Ser/Thr and one atypical Asn-X-Cys sequons.
19343721	0	63	gly	glycosylated	147:158	arg1	occupancy					44:52	site occupancy	39:52	site occupancy	39:52	N-glycosylation microheterogeneity and site occupancy of an Asn-X-Cys sequon in plasma-derived and recombinant protein C. Human protein C (hPC) is glycosylated at three Asn-X-Ser/Thr and one atypical Asn-X-Cys sequons.
19343721	7	64	from	processing	1387:1396	arg1	cells					1432:1436	the porcine mammary epithelial cells	1401:1436	the porcine mammary epithelial cells	1401:1436	The N-glycan structures found for tg-PC are very similar to those reported for a recombinant Factor IX produced in transgenic pig milk, and similar to the endogenous milk protein lactoferrin, which may indicate that N-glycan processing in the porcine mammary epithelial cells is more uniform than in other tissues.
19343721	0	65	from	microheterogeneity	16:33	arg1	hPC					139:141	hPC	139:141	hPC	139:141	N-glycosylation microheterogeneity and site occupancy of an Asn-X-Cys sequon in plasma-derived and recombinant protein C. Human protein C (hPC) is glycosylated at three Asn-X-Ser/Thr and one atypical Asn-X-Cys sequons.
19343721	0	65	from	microheterogeneity	16:33	arg1	C					136:136	plasma-derived and recombinant protein C. Human protein C	80:136	plasma-derived and recombinant protein C. Human protein C (hPC)	80:142	N-glycosylation microheterogeneity and site occupancy of an Asn-X-Cys sequon in plasma-derived and recombinant protein C. Human protein C (hPC) is glycosylated at three Asn-X-Ser/Thr and one atypical Asn-X-Cys sequons.
19343721	0	66	theme	protein	111:117	arg1	hPC					139:141	hPC	139:141	hPC	139:141	N-glycosylation microheterogeneity and site occupancy of an Asn-X-Cys sequon in plasma-derived and recombinant protein C. Human protein C (hPC) is glycosylated at three Asn-X-Ser/Thr and one atypical Asn-X-Cys sequons.
19343721	0	66	theme	protein	111:117	arg1	C					136:136	plasma-derived and recombinant protein C. Human protein C	80:136	plasma-derived and recombinant protein C. Human protein C (hPC)	80:142	N-glycosylation microheterogeneity and site occupancy of an Asn-X-Cys sequon in plasma-derived and recombinant protein C. Human protein C (hPC) is glycosylated at three Asn-X-Ser/Thr and one atypical Asn-X-Cys sequons.
19343721	2	67	gly	tri-sialylated	529:542	arg1	N-glycans					492:500	The N-glycans	488:500	The N-glycans of hPC	488:507	The N-glycans of hPC are complex di- and tri-sialylated structures, and we measured 78% site occupancy at Asn-329 (the Asn-X-Cys sequon).
19343721	2	67	gly	tri-sialylated	529:542	arg1	structures					544:553	complex di- and tri-sialylated structures	513:553	complex di- and tri-sialylated structures	513:553	The N-glycans of hPC are complex di- and tri-sialylated structures, and we measured 78% site occupancy at Asn-329 (the Asn-X-Cys sequon).
19343721	5	68	attach	present	1001:1007	arg1	sites					1043:1047	the four glycosylation sites	1020:1047	the four glycosylation sites for both hPC and tg-PC	1020:1070	A distinct bias for particular structures was present at each of the four glycosylation sites for both hPC and tg-PC.
19343721	5	68	attach	present	1001:1007	arg1	each					1012:1015	each	1012:1015	each	1012:1015	A distinct bias for particular structures was present at each of the four glycosylation sites for both hPC and tg-PC.
19343721	5	68	attach	present	1001:1007	arg2	bias					966:969	A distinct bias	955:969	A distinct bias for particular structures	955:995	A distinct bias for particular structures was present at each of the four glycosylation sites for both hPC and tg-PC.
19343721	5	68	attach	present	1001:1007	arg2	present					1001:1007	present	1001:1007	present	1001:1007	A distinct bias for particular structures was present at each of the four glycosylation sites for both hPC and tg-PC.
19343721	2	69	theme	tri-sialylated	529:542	arg1	N-glycans					492:500	The N-glycans	488:500	The N-glycans of hPC	488:507	The N-glycans of hPC are complex di- and tri-sialylated structures, and we measured 78% site occupancy at Asn-329 (the Asn-X-Cys sequon).
19343721	2	69	theme	tri-sialylated	529:542	arg1	structures					544:553	complex di- and tri-sialylated structures	513:553	complex di- and tri-sialylated structures	513:553	The N-glycans of hPC are complex di- and tri-sialylated structures, and we measured 78% site occupancy at Asn-329 (the Asn-X-Cys sequon).
19343721	0	70	theme	Human	122:126	arg1	hPC					139:141	hPC	139:141	hPC	139:141	N-glycosylation microheterogeneity and site occupancy of an Asn-X-Cys sequon in plasma-derived and recombinant protein C. Human protein C (hPC) is glycosylated at three Asn-X-Ser/Thr and one atypical Asn-X-Cys sequons.
19343721	0	70	theme	Human	122:126	arg1	C					136:136	plasma-derived and recombinant protein C. Human protein C	80:136	plasma-derived and recombinant protein C. Human protein C (hPC)	80:142	N-glycosylation microheterogeneity and site occupancy of an Asn-X-Cys sequon in plasma-derived and recombinant protein C. Human protein C (hPC) is glycosylated at three Asn-X-Ser/Thr and one atypical Asn-X-Cys sequons.
19343721	2	71	theme	di-	521:523	arg1	N-glycans					492:500	The N-glycans	488:500	The N-glycans of hPC	488:507	The N-glycans of hPC are complex di- and tri-sialylated structures, and we measured 78% site occupancy at Asn-329 (the Asn-X-Cys sequon).
19343721	2	71	theme	di-	521:523	arg1	structures					544:553	complex di- and tri-sialylated structures	513:553	complex di- and tri-sialylated structures	513:553	The N-glycans of hPC are complex di- and tri-sialylated structures, and we measured 78% site occupancy at Asn-329 (the Asn-X-Cys sequon).
19343721	7	72	theme	pig	1288:1290	arg1	milk					1292:1295	transgenic pig milk	1277:1295	transgenic pig milk	1277:1295	The N-glycan structures found for tg-PC are very similar to those reported for a recombinant Factor IX produced in transgenic pig milk, and similar to the endogenous milk protein lactoferrin, which may indicate that N-glycan processing in the porcine mammary epithelial cells is more uniform than in other tissues.
19343721	0	73	theme	site	39:42	arg1	occupancy					44:52	site occupancy	39:52	site occupancy	39:52	N-glycosylation microheterogeneity and site occupancy of an Asn-X-Cys sequon in plasma-derived and recombinant protein C. Human protein C (hPC) is glycosylated at three Asn-X-Ser/Thr and one atypical Asn-X-Cys sequons.
19343721	1	74	theme	hPC	294:296	arg1	macro-heterogeneity					256:274	macro-heterogeneity	256:274	macro-heterogeneity	256:274	We have characterized the micro- and macro-heterogeneity of plasma-derived hPC and compared the glycosylation features with recombinant protein C (tg-PC) produced in a transgenic pig bioreactor from two animals having approximately tenfold different expression levels.
19343721	1	74	theme	hPC	294:296	arg1	micro-					245:250	micro-	245:250	micro-	245:250	We have characterized the micro- and macro-heterogeneity of plasma-derived hPC and compared the glycosylation features with recombinant protein C (tg-PC) produced in a transgenic pig bioreactor from two animals having approximately tenfold different expression levels.
19343721	1	75	gly	macro-heterogeneity	256:274	arg1	hPC					294:296	plasma-derived hPC	279:296	plasma-derived hPC	279:296	We have characterized the micro- and macro-heterogeneity of plasma-derived hPC and compared the glycosylation features with recombinant protein C (tg-PC) produced in a transgenic pig bioreactor from two animals having approximately tenfold different expression levels.
19343721	4	76	theme	mammary	740:746	arg1	cells					759:763	The porcine mammary epithelial cells	728:763	The porcine mammary epithelial cells	728:763	The porcine mammary epithelial cells glycosylate the Asn-X-Cys sequon with a similar efficiency as human hepatocytes even at these high expression levels, and site occupancy at this sequon was not affected by expression level.
19343721	0	77	gly	N-glycosylation	0:14	arg1	sequon					70:75	an Asn-X-Cys sequon	57:75	an Asn-X-Cys sequon	57:75	N-glycosylation microheterogeneity and site occupancy of an Asn-X-Cys sequon in plasma-derived and recombinant protein C. Human protein C (hPC) is glycosylated at three Asn-X-Ser/Thr and one atypical Asn-X-Cys sequons.
19343721	0	77	gly	N-glycosylation	0:14	arg2	hPC					139:141	hPC	139:141	hPC	139:141	N-glycosylation microheterogeneity and site occupancy of an Asn-X-Cys sequon in plasma-derived and recombinant protein C. Human protein C (hPC) is glycosylated at three Asn-X-Ser/Thr and one atypical Asn-X-Cys sequons.
19343721	0	77	gly	N-glycosylation	0:14	arg2	C					136:136	plasma-derived and recombinant protein C. Human protein C	80:136	plasma-derived and recombinant protein C. Human protein C (hPC)	80:142	N-glycosylation microheterogeneity and site occupancy of an Asn-X-Cys sequon in plasma-derived and recombinant protein C. Human protein C (hPC) is glycosylated at three Asn-X-Ser/Thr and one atypical Asn-X-Cys sequons.
19343721	0	78	theme	C.	119:120	arg1	hPC					139:141	hPC	139:141	hPC	139:141	N-glycosylation microheterogeneity and site occupancy of an Asn-X-Cys sequon in plasma-derived and recombinant protein C. Human protein C (hPC) is glycosylated at three Asn-X-Ser/Thr and one atypical Asn-X-Cys sequons.
19343721	0	78	theme	C.	119:120	arg1	C					136:136	plasma-derived and recombinant protein C. Human protein C	80:136	plasma-derived and recombinant protein C. Human protein C (hPC)	80:142	N-glycosylation microheterogeneity and site occupancy of an Asn-X-Cys sequon in plasma-derived and recombinant protein C. Human protein C (hPC) is glycosylated at three Asn-X-Ser/Thr and one atypical Asn-X-Cys sequons.
19343721	0	79	theme	Asn-X-Cys	60:68	arg1	sequon					70:75	an Asn-X-Cys sequon	57:75	an Asn-X-Cys sequon	57:75	N-glycosylation microheterogeneity and site occupancy of an Asn-X-Cys sequon in plasma-derived and recombinant protein C. Human protein C (hPC) is glycosylated at three Asn-X-Ser/Thr and one atypical Asn-X-Cys sequons.
19343721	1	80	theme	glycosylation	315:327	arg1	features					329:336	the glycosylation features	311:336	the glycosylation features with recombinant protein C (tg-PC) produced in a transgenic pig bioreactor from two animals having approximately tenfold different expression levels	311:485	We have characterized the micro- and macro-heterogeneity of plasma-derived hPC and compared the glycosylation features with recombinant protein C (tg-PC) produced in a transgenic pig bioreactor from two animals having approximately tenfold different expression levels.
19343721	0	81	link	plasma-derived	80:93	arg1	hPC					139:141	hPC	139:141	hPC	139:141	N-glycosylation microheterogeneity and site occupancy of an Asn-X-Cys sequon in plasma-derived and recombinant protein C. Human protein C (hPC) is glycosylated at three Asn-X-Ser/Thr and one atypical Asn-X-Cys sequons.
19343721	0	81	link	plasma-derived	80:93	arg1	C					136:136	plasma-derived and recombinant protein C. Human protein C	80:136	plasma-derived and recombinant protein C. Human protein C (hPC)	80:142	N-glycosylation microheterogeneity and site occupancy of an Asn-X-Cys sequon in plasma-derived and recombinant protein C. Human protein C (hPC) is glycosylated at three Asn-X-Ser/Thr and one atypical Asn-X-Cys sequons.
19343721	7	82	theme	recombinant	1243:1253	arg1	IX					1262:1263	a recombinant Factor IX	1241:1263	a recombinant Factor IX produced in transgenic pig milk	1241:1295	The N-glycan structures found for tg-PC are very similar to those reported for a recombinant Factor IX produced in transgenic pig milk, and similar to the endogenous milk protein lactoferrin, which may indicate that N-glycan processing in the porcine mammary epithelial cells is more uniform than in other tissues.
19343721	3	83	theme	sialylated	661:670	arg1	N-glycans					630:638	The N-glycans	626:638	The N-glycans of tg-PC	626:647	The N-glycans of tg-PC are complex sialylated structures, but less branched and partially sialylated.
19343721	3	83	theme	sialylated	661:670	arg1	structures					672:681	complex sialylated structures	653:681	complex sialylated structures	653:681	The N-glycans of tg-PC are complex sialylated structures, but less branched and partially sialylated.
19343721	4	84	theme	human	827:831	arg1	hepatocytes					833:843	human hepatocytes	827:843	human hepatocytes	827:843	The porcine mammary epithelial cells glycosylate the Asn-X-Cys sequon with a similar efficiency as human hepatocytes even at these high expression levels, and site occupancy at this sequon was not affected by expression level.
19343721	5	85	theme	particular	975:984	arg1	structures					986:995	particular structures	975:995	particular structures	975:995	A distinct bias for particular structures was present at each of the four glycosylation sites for both hPC and tg-PC.
19343721	1	86	link	plasma-derived	279:292	arg1	hPC					294:296	plasma-derived hPC	279:296	plasma-derived hPC	279:296	We have characterized the micro- and macro-heterogeneity of plasma-derived hPC and compared the glycosylation features with recombinant protein C (tg-PC) produced in a transgenic pig bioreactor from two animals having approximately tenfold different expression levels.
19343721	7	87	theme	other	1462:1466	arg1	tissues					1468:1474	other tissues	1462:1474	other tissues	1462:1474	The N-glycan structures found for tg-PC are very similar to those reported for a recombinant Factor IX produced in transgenic pig milk, and similar to the endogenous milk protein lactoferrin, which may indicate that N-glycan processing in the porcine mammary epithelial cells is more uniform than in other tissues.
19343721	6	88	from	glycans	1088:1094	arg1	antennae					1115:1122	the antennae	1111:1122	the antennae	1111:1122	Interestingly, glycans with GalNAc in the antennae were predominant at the Asn-329 site.
17563389	9	0	theme	receptors	1719:1727	arg1	elucidation					1615:1625	the ongoing elucidation	1603:1625	the ongoing elucidation of the role of glycosylation in G protein-coupled receptors	1603:1685	These results contribute to the ongoing elucidation of the role of glycosylation in G protein-coupled receptors and the study of the neurokinin receptors in particular.
17563389	9	0	theme	receptors	1719:1727	arg1	study					1695:1699	the study	1691:1699	the study of the neurokinin receptors in particular	1691:1741	These results contribute to the ongoing elucidation of the role of glycosylation in G protein-coupled receptors and the study of the neurokinin receptors in particular.
17563389	3	1	theme	nontransformed	617:630	arg1	line					662:665	nontransformed human colonic epithelial cell line	617:665	a nontransformed human colonic epithelial cell line	615:665	Using a lentiviral transfection system, the mutants were stably transfected into NCM 460 cells, a nontransformed human colonic epithelial cell line.
17563389	3	1	theme	nontransformed	617:630	arg1	cells					608:612	NCM 460 cells	600:612	NCM 460 cells	600:612	Using a lentiviral transfection system, the mutants were stably transfected into NCM 460 cells, a nontransformed human colonic epithelial cell line.
17563389	1	2	link	N-linked	243:250	arg1	Asn-14					273:278	Asn-14	273:278	Asn-14	273:278	The neurokinin 1 receptor (NK1R), a G protein-coupled receptor involved in diverse functions including pain and inflammation, has two putative N-linked glycosylation sites, Asn-14 and Asn-18.
17563389	1	2	link	N-linked	243:250	arg1	sites					266:270	two putative N-linked glycosylation sites	230:270	two putative N-linked glycosylation sites	230:270	The neurokinin 1 receptor (NK1R), a G protein-coupled receptor involved in diverse functions including pain and inflammation, has two putative N-linked glycosylation sites, Asn-14 and Asn-18.
17563389	1	2	link	N-linked	243:250	arg1	Asn-18					284:289	Asn-18	284:289	Asn-18	284:289	The neurokinin 1 receptor (NK1R), a G protein-coupled receptor involved in diverse functions including pain and inflammation, has two putative N-linked glycosylation sites, Asn-14 and Asn-18.
17563389	2	3	theme	glycosylation	324:336	arg1	role					307:310	the role	303:310	the role of N-linked glycosylation in the functioning of the NK1R	303:367	We studied the role of N-linked glycosylation in the functioning of the NK1R by constructing three receptor mutants: two single mutants (Asn --> Gln-14 and Asn --> Gln-18) and a double mutant, lacking both glycosylation sites.
17563389	1	4	theme	putative	234:241	arg1	Asn-14					273:278	Asn-14	273:278	Asn-14	273:278	The neurokinin 1 receptor (NK1R), a G protein-coupled receptor involved in diverse functions including pain and inflammation, has two putative N-linked glycosylation sites, Asn-14 and Asn-18.
17563389	1	4	theme	putative	234:241	arg1	sites					266:270	two putative N-linked glycosylation sites	230:270	two putative N-linked glycosylation sites	230:270	The neurokinin 1 receptor (NK1R), a G protein-coupled receptor involved in diverse functions including pain and inflammation, has two putative N-linked glycosylation sites, Asn-14 and Asn-18.
17563389	1	4	theme	putative	234:241	arg1	Asn-18					284:289	Asn-18	284:289	Asn-18	284:289	The neurokinin 1 receptor (NK1R), a G protein-coupled receptor involved in diverse functions including pain and inflammation, has two putative N-linked glycosylation sites, Asn-14 and Asn-18.
17563389	6	5	theme	sites	1168:1172	arg1	ablation					1128:1135	the ablation	1124:1135	the ablation of both N-linked glycosylation sites	1124:1172	In terms of receptor function, the ablation of both N-linked glycosylation sites did not have a profound effect on the receptors' abilities to activate the MAP kinase families (p42/p44, JNK, and p38), but did affect SP-induced IL-8 secretion.
17563389	1	6	theme	glycosylation	252:264	arg1	Asn-14					273:278	Asn-14	273:278	Asn-14	273:278	The neurokinin 1 receptor (NK1R), a G protein-coupled receptor involved in diverse functions including pain and inflammation, has two putative N-linked glycosylation sites, Asn-14 and Asn-18.
17563389	1	6	theme	glycosylation	252:264	arg1	sites					266:270	two putative N-linked glycosylation sites	230:270	two putative N-linked glycosylation sites	230:270	The neurokinin 1 receptor (NK1R), a G protein-coupled receptor involved in diverse functions including pain and inflammation, has two putative N-linked glycosylation sites, Asn-14 and Asn-18.
17563389	1	6	theme	glycosylation	252:264	arg1	Asn-18					284:289	Asn-18	284:289	Asn-18	284:289	The neurokinin 1 receptor (NK1R), a G protein-coupled receptor involved in diverse functions including pain and inflammation, has two putative N-linked glycosylation sites, Asn-14 and Asn-18.
17563389	3	7	theme	cell	657:660	arg1	line					662:665	nontransformed human colonic epithelial cell line	617:665	a nontransformed human colonic epithelial cell line	615:665	Using a lentiviral transfection system, the mutants were stably transfected into NCM 460 cells, a nontransformed human colonic epithelial cell line.
17563389	3	7	theme	cell	657:660	arg1	cells					608:612	NCM 460 cells	600:612	NCM 460 cells	600:612	Using a lentiviral transfection system, the mutants were stably transfected into NCM 460 cells, a nontransformed human colonic epithelial cell line.
17563389	6	8	theme	N-linked	1145:1152	arg1	sites					1168:1172	both N-linked glycosylation sites	1140:1172	both N-linked glycosylation sites	1140:1172	In terms of receptor function, the ablation of both N-linked glycosylation sites did not have a profound effect on the receptors' abilities to activate the MAP kinase families (p42/p44, JNK, and p38), but did affect SP-induced IL-8 secretion.
17563389	4	9	theme	sites	796:800	arg1	number					772:777	the number	768:777	the number of glycosylation sites available	768:810	We observed that the magnitude of glycosylation as estimated by changes in gel migration depends on the number of glycosylation sites available, with the wild-type receptor containing the greatest amount of glycosylation.
17563389	2	10	link	N-linked	315:322	arg1	glycosylation					324:336	N-linked glycosylation	315:336	N-linked glycosylation	315:336	We studied the role of N-linked glycosylation in the functioning of the NK1R by constructing three receptor mutants: two single mutants (Asn --> Gln-14 and Asn --> Gln-18) and a double mutant, lacking both glycosylation sites.
17563389	4	11	theme	glycosylation	875:887	arg1	amount					865:870	the greatest amount	852:870	the greatest amount of glycosylation	852:887	We observed that the magnitude of glycosylation as estimated by changes in gel migration depends on the number of glycosylation sites available, with the wild-type receptor containing the greatest amount of glycosylation.
17563389	4	11	theme	glycosylation	875:887	arg1	glycosylation					875:887	glycosylation	875:887	glycosylation	875:887	We observed that the magnitude of glycosylation as estimated by changes in gel migration depends on the number of glycosylation sites available, with the wild-type receptor containing the greatest amount of glycosylation.
17563389	6	12	link	N-linked	1145:1152	arg1	sites					1168:1172	both N-linked glycosylation sites	1140:1172	both N-linked glycosylation sites	1140:1172	In terms of receptor function, the ablation of both N-linked glycosylation sites did not have a profound effect on the receptors' abilities to activate the MAP kinase families (p42/p44, JNK, and p38), but did affect SP-induced IL-8 secretion.
17563389	5	13	theme	double	1006:1011	arg1	NK1R					1037:1040	nonglycosylated NK1R	1021:1040	nonglycosylated NK1R	1021:1040	All mutant receptors were able to bind to substance P and neurokinin A ligand with similar affinities; however, the double mutant, nonglycosylated NK1R showed only half the B(max) of the wild-type NK1R.
17563389	5	13	theme	double	1006:1011	arg1	mutant					1013:1018	the double mutant	1002:1018	the double mutant	1002:1018	All mutant receptors were able to bind to substance P and neurokinin A ligand with similar affinities; however, the double mutant, nonglycosylated NK1R showed only half the B(max) of the wild-type NK1R.
17563389	5	14	theme	similar	973:979	arg1	affinities					981:990	similar affinities	973:990	similar affinities	973:990	All mutant receptors were able to bind to substance P and neurokinin A ligand with similar affinities; however, the double mutant, nonglycosylated NK1R showed only half the B(max) of the wild-type NK1R.
17563389	3	15	theme	lentiviral	527:536	arg1	system					551:556	a lentiviral transfection system	525:556	a lentiviral transfection system	525:556	Using a lentiviral transfection system, the mutants were stably transfected into NCM 460 cells, a nontransformed human colonic epithelial cell line.
17563389	6	16	gly	glycosylation	1154:1166	arg2	sites					1168:1172	both N-linked glycosylation sites	1140:1172	both N-linked glycosylation sites	1140:1172	In terms of receptor function, the ablation of both N-linked glycosylation sites did not have a profound effect on the receptors' abilities to activate the MAP kinase families (p42/p44, JNK, and p38), but did affect SP-induced IL-8 secretion.
17563389	6	17	theme	receptor	1105:1112	arg1	function					1114:1121	receptor function	1105:1121	receptor function	1105:1121	In terms of receptor function, the ablation of both N-linked glycosylation sites did not have a profound effect on the receptors' abilities to activate the MAP kinase families (p42/p44, JNK, and p38), but did affect SP-induced IL-8 secretion.
17563389	5	18	theme	only	1049:1052	arg1	half					1054:1057	only half the B(max)	1049:1068	only half the B(max) of the wild-type NK1R	1049:1090	All mutant receptors were able to bind to substance P and neurokinin A ligand with similar affinities; however, the double mutant, nonglycosylated NK1R showed only half the B(max) of the wild-type NK1R.
17563389	4	19	from	changes	732:738	arg1	migration					747:755	gel migration	743:755	gel migration	743:755	We observed that the magnitude of glycosylation as estimated by changes in gel migration depends on the number of glycosylation sites available, with the wild-type receptor containing the greatest amount of glycosylation.
17563389	7	20	theme	mutant	1424:1429	arg1	receptor					1431:1438	the double mutant receptor	1413:1438	the double mutant receptor	1413:1438	All mutants were able to internalize, but the kinetics of internalization of the double mutant receptor was more rapid, when compared with wild-type NK1R.
17563389	2	21	theme	Asn	448:450	arg1	mutants					420:426	two single mutants	409:426	two single mutants (Asn --> Gln-14 and Asn --> Gln-18)	409:462	We studied the role of N-linked glycosylation in the functioning of the NK1R by constructing three receptor mutants: two single mutants (Asn --> Gln-14 and Asn --> Gln-18) and a double mutant, lacking both glycosylation sites.
17563389	2	21	theme	Asn	448:450	arg1	Gln-18					456:461	Asn --> Gln-18	448:461	Asn --> Gln-18	448:461	We studied the role of N-linked glycosylation in the functioning of the NK1R by constructing three receptor mutants: two single mutants (Asn --> Gln-14 and Asn --> Gln-18) and a double mutant, lacking both glycosylation sites.
17563389	0	22	theme	neurokinin	77:86	arg1	receptor					90:97	the neurokinin 1 receptor	73:97	the neurokinin 1 receptor	73:97	Functional consequences of alteration of N-linked glycosylation sites on the neurokinin 1 receptor.
17563389	2	23	theme	double	470:475	arg1	mutant					477:482	a double mutant	468:482	a double mutant	468:482	We studied the role of N-linked glycosylation in the functioning of the NK1R by constructing three receptor mutants: two single mutants (Asn --> Gln-14 and Asn --> Gln-18) and a double mutant, lacking both glycosylation sites.
17563389	4	24	theme	glycosylation	702:714	arg1	magnitude					689:697	the magnitude	685:697	the magnitude of glycosylation as estimated by changes in gel migration	685:755	We observed that the magnitude of glycosylation as estimated by changes in gel migration depends on the number of glycosylation sites available, with the wild-type receptor containing the greatest amount of glycosylation.
17563389	4	25	contain	containing	841:850	arg2	glycosylation					875:887	glycosylation	875:887	glycosylation	875:887	We observed that the magnitude of glycosylation as estimated by changes in gel migration depends on the number of glycosylation sites available, with the wild-type receptor containing the greatest amount of glycosylation.
17563389	4	25	contain	containing	841:850	arg2	amount					865:870	the greatest amount	852:870	the greatest amount of glycosylation	852:887	We observed that the magnitude of glycosylation as estimated by changes in gel migration depends on the number of glycosylation sites available, with the wild-type receptor containing the greatest amount of glycosylation.
17563389	4	25	contain	containing	841:850	arg1	receptor					832:839	the wild-type receptor	818:839	the wild-type receptor containing the greatest amount of glycosylation	818:887	We observed that the magnitude of glycosylation as estimated by changes in gel migration depends on the number of glycosylation sites available, with the wild-type receptor containing the greatest amount of glycosylation.
17563389	7	26	theme	internalization	1394:1408	arg1	rapid					1449:1453	rapid	1449:1453	rapid	1449:1453	All mutants were able to internalize, but the kinetics of internalization of the double mutant receptor was more rapid, when compared with wild-type NK1R.
17563389	7	26	theme	internalization	1394:1408	arg1	kinetics					1382:1389	the kinetics	1378:1389	the kinetics of internalization of the double mutant receptor	1378:1438	All mutants were able to internalize, but the kinetics of internalization of the double mutant receptor was more rapid, when compared with wild-type NK1R.
17563389	9	27	theme	role	1634:1637	arg1	elucidation					1615:1625	the ongoing elucidation	1603:1625	the ongoing elucidation of the role of glycosylation in G protein-coupled receptors	1603:1685	These results contribute to the ongoing elucidation of the role of glycosylation in G protein-coupled receptors and the study of the neurokinin receptors in particular.
17563389	9	27	theme	role	1634:1637	arg1	study					1695:1699	the study	1691:1699	the study of the neurokinin receptors in particular	1691:1741	These results contribute to the ongoing elucidation of the role of glycosylation in G protein-coupled receptors and the study of the neurokinin receptors in particular.
17563389	0	28	theme	Functional	0:9	arg1	consequences					11:22	Functional consequences	0:22	Functional consequences of alteration of N-linked glycosylation sites on the neurokinin 1 receptor	0:97	Functional consequences of alteration of N-linked glycosylation sites on the neurokinin 1 receptor.
17563389	1	29	gly	glycosylation	252:264	arg2	sites					266:270	two putative N-linked glycosylation sites	230:270	two putative N-linked glycosylation sites	230:270	The neurokinin 1 receptor (NK1R), a G protein-coupled receptor involved in diverse functions including pain and inflammation, has two putative N-linked glycosylation sites, Asn-14 and Asn-18.
17563389	1	29	gly	glycosylation	252:264	arg2	Asn-18					284:289	Asn-18	284:289	Asn-18	284:289	The neurokinin 1 receptor (NK1R), a G protein-coupled receptor involved in diverse functions including pain and inflammation, has two putative N-linked glycosylation sites, Asn-14 and Asn-18.
17563389	1	29	gly	glycosylation	252:264	arg2	two					230:232	two	230:232	two	230:232	The neurokinin 1 receptor (NK1R), a G protein-coupled receptor involved in diverse functions including pain and inflammation, has two putative N-linked glycosylation sites, Asn-14 and Asn-18.
17563389	1	29	gly	glycosylation	252:264	arg2	Asn-14					273:278	Asn-14	273:278	Asn-14	273:278	The neurokinin 1 receptor (NK1R), a G protein-coupled receptor involved in diverse functions including pain and inflammation, has two putative N-linked glycosylation sites, Asn-14 and Asn-18.
17563389	9	30	theme	glycosylation	1642:1654	arg1	role					1634:1637	the role	1630:1637	the role of glycosylation in G protein-coupled receptors	1630:1685	These results contribute to the ongoing elucidation of the role of glycosylation in G protein-coupled receptors and the study of the neurokinin receptors in particular.
17563389	5	31	theme	NK1R	1087:1090	arg1	half					1054:1057	only half the B(max)	1049:1068	only half the B(max) of the wild-type NK1R	1049:1090	All mutant receptors were able to bind to substance P and neurokinin A ligand with similar affinities; however, the double mutant, nonglycosylated NK1R showed only half the B(max) of the wild-type NK1R.
17563389	1	32	theme	neurokinin	104:113	arg1	NK1R					127:130	NK1R	127:130	NK1R	127:130	The neurokinin 1 receptor (NK1R), a G protein-coupled receptor involved in diverse functions including pain and inflammation, has two putative N-linked glycosylation sites, Asn-14 and Asn-18.
17563389	1	32	theme	neurokinin	104:113	arg1	receptor					117:124	neurokinin 1 receptor	104:124	The neurokinin 1 receptor (NK1R)	100:131	The neurokinin 1 receptor (NK1R), a G protein-coupled receptor involved in diverse functions including pain and inflammation, has two putative N-linked glycosylation sites, Asn-14 and Asn-18.
17563389	1	32	theme	neurokinin	104:113	arg1	receptor					154:161	a G protein-coupled receptor	134:161	a G protein-coupled receptor involved in diverse functions including pain and inflammation	134:223	The neurokinin 1 receptor (NK1R), a G protein-coupled receptor involved in diverse functions including pain and inflammation, has two putative N-linked glycosylation sites, Asn-14 and Asn-18.
17563389	5	33	dep	half	1054:1057	arg1	max					1065:1067	max	1065:1067	max	1065:1067	All mutant receptors were able to bind to substance P and neurokinin A ligand with similar affinities; however, the double mutant, nonglycosylated NK1R showed only half the B(max) of the wild-type NK1R.
17563389	5	33	dep	half	1054:1057	arg1	B					1063:1063	the B	1059:1063	only half the B(max) of the wild-type NK1R	1049:1090	All mutant receptors were able to bind to substance P and neurokinin A ligand with similar affinities; however, the double mutant, nonglycosylated NK1R showed only half the B(max) of the wild-type NK1R.
17563389	2	34	gly	glycosylation	324:336	arg1	NK1R					364:367	the NK1R	360:367	the NK1R	360:367	We studied the role of N-linked glycosylation in the functioning of the NK1R by constructing three receptor mutants: two single mutants (Asn --> Gln-14 and Asn --> Gln-18) and a double mutant, lacking both glycosylation sites.
17563389	3	35	theme	NCM	600:602	arg1	cells					608:612	NCM 460 cells	600:612	NCM 460 cells	600:612	Using a lentiviral transfection system, the mutants were stably transfected into NCM 460 cells, a nontransformed human colonic epithelial cell line.
17563389	3	35	theme	NCM	600:602	arg1	line					662:665	nontransformed human colonic epithelial cell line	617:665	a nontransformed human colonic epithelial cell line	615:665	Using a lentiviral transfection system, the mutants were stably transfected into NCM 460 cells, a nontransformed human colonic epithelial cell line.
17563389	9	36	theme	protein-coupled	1661:1675	arg1	receptors					1677:1685	G protein-coupled receptors	1659:1685	G protein-coupled receptors	1659:1685	These results contribute to the ongoing elucidation of the role of glycosylation in G protein-coupled receptors and the study of the neurokinin receptors in particular.
17563389	2	37	theme	Asn	429:431	arg1	mutants					420:426	two single mutants	409:426	two single mutants (Asn --> Gln-14 and Asn --> Gln-18)	409:462	We studied the role of N-linked glycosylation in the functioning of the NK1R by constructing three receptor mutants: two single mutants (Asn --> Gln-14 and Asn --> Gln-18) and a double mutant, lacking both glycosylation sites.
17563389	2	37	theme	Asn	429:431	arg1	Gln-14					437:442	Asn --> Gln-14	429:442	Asn --> Gln-14	429:442	We studied the role of N-linked glycosylation in the functioning of the NK1R by constructing three receptor mutants: two single mutants (Asn --> Gln-14 and Asn --> Gln-18) and a double mutant, lacking both glycosylation sites.
17563389	2	38	theme	N-linked	315:322	arg1	glycosylation					324:336	N-linked glycosylation	315:336	N-linked glycosylation	315:336	We studied the role of N-linked glycosylation in the functioning of the NK1R by constructing three receptor mutants: two single mutants (Asn --> Gln-14 and Asn --> Gln-18) and a double mutant, lacking both glycosylation sites.
17563389	0	39	theme	glycosylation	50:62	arg1	sites					64:68	N-linked glycosylation sites	41:68	N-linked glycosylation sites	41:68	Functional consequences of alteration of N-linked glycosylation sites on the neurokinin 1 receptor.
17563389	4	40	theme	gel	743:745	arg1	migration					747:755	gel migration	743:755	gel migration	743:755	We observed that the magnitude of glycosylation as estimated by changes in gel migration depends on the number of glycosylation sites available, with the wild-type receptor containing the greatest amount of glycosylation.
17563389	9	41	from	receptors	1677:1685	arg1	elucidation					1615:1625	the ongoing elucidation	1603:1625	the ongoing elucidation of the role of glycosylation in G protein-coupled receptors	1603:1685	These results contribute to the ongoing elucidation of the role of glycosylation in G protein-coupled receptors and the study of the neurokinin receptors in particular.
17563389	9	41	from	receptors	1677:1685	arg1	study					1695:1699	the study	1691:1699	the study of the neurokinin receptors in particular	1691:1741	These results contribute to the ongoing elucidation of the role of glycosylation in G protein-coupled receptors and the study of the neurokinin receptors in particular.
17563389	9	42	theme	neurokinin	1708:1717	arg1	receptors					1719:1727	the neurokinin receptors	1704:1727	the neurokinin receptors in particular	1704:1741	These results contribute to the ongoing elucidation of the role of glycosylation in G protein-coupled receptors and the study of the neurokinin receptors in particular.
17563389	3	43	theme	epithelial	646:655	arg1	line					662:665	nontransformed human colonic epithelial cell line	617:665	a nontransformed human colonic epithelial cell line	615:665	Using a lentiviral transfection system, the mutants were stably transfected into NCM 460 cells, a nontransformed human colonic epithelial cell line.
17563389	3	43	theme	epithelial	646:655	arg1	cells					608:612	NCM 460 cells	600:612	NCM 460 cells	600:612	Using a lentiviral transfection system, the mutants were stably transfected into NCM 460 cells, a nontransformed human colonic epithelial cell line.
17563389	6	44	theme	SP-induced	1309:1318	arg1	secretion					1325:1333	SP-induced IL-8 secretion	1309:1333	SP-induced IL-8 secretion	1309:1333	In terms of receptor function, the ablation of both N-linked glycosylation sites did not have a profound effect on the receptors' abilities to activate the MAP kinase families (p42/p44, JNK, and p38), but did affect SP-induced IL-8 secretion.
17563389	4	45	theme	available	802:810	arg1	sites					796:800	glycosylation sites	782:800	glycosylation sites available	782:810	We observed that the magnitude of glycosylation as estimated by changes in gel migration depends on the number of glycosylation sites available, with the wild-type receptor containing the greatest amount of glycosylation.
17563389	2	46	from	role	307:310	arg1	the					341:343	the	341:343	the	341:343	We studied the role of N-linked glycosylation in the functioning of the NK1R by constructing three receptor mutants: two single mutants (Asn --> Gln-14 and Asn --> Gln-18) and a double mutant, lacking both glycosylation sites.
17563389	5	47	with	ligand	961:966	arg1	affinities					981:990	similar affinities	973:990	similar affinities	973:990	All mutant receptors were able to bind to substance P and neurokinin A ligand with similar affinities; however, the double mutant, nonglycosylated NK1R showed only half the B(max) of the wild-type NK1R.
17563389	3	48	theme	human	632:636	arg1	line					662:665	nontransformed human colonic epithelial cell line	617:665	a nontransformed human colonic epithelial cell line	615:665	Using a lentiviral transfection system, the mutants were stably transfected into NCM 460 cells, a nontransformed human colonic epithelial cell line.
17563389	3	48	theme	human	632:636	arg1	cells					608:612	NCM 460 cells	600:612	NCM 460 cells	600:612	Using a lentiviral transfection system, the mutants were stably transfected into NCM 460 cells, a nontransformed human colonic epithelial cell line.
17563389	1	49	theme	N-linked	243:250	arg1	Asn-14					273:278	Asn-14	273:278	Asn-14	273:278	The neurokinin 1 receptor (NK1R), a G protein-coupled receptor involved in diverse functions including pain and inflammation, has two putative N-linked glycosylation sites, Asn-14 and Asn-18.
17563389	1	49	theme	N-linked	243:250	arg1	sites					266:270	two putative N-linked glycosylation sites	230:270	two putative N-linked glycosylation sites	230:270	The neurokinin 1 receptor (NK1R), a G protein-coupled receptor involved in diverse functions including pain and inflammation, has two putative N-linked glycosylation sites, Asn-14 and Asn-18.
17563389	1	49	theme	N-linked	243:250	arg1	Asn-18					284:289	Asn-18	284:289	Asn-18	284:289	The neurokinin 1 receptor (NK1R), a G protein-coupled receptor involved in diverse functions including pain and inflammation, has two putative N-linked glycosylation sites, Asn-14 and Asn-18.
17563389	8	50	gly	glycosylation	1502:1514	arg1	NK1R					1519:1522	NK1R	1519:1522	NK1R	1519:1522	Therefore, glycosylation of NK1R may stabilize the receptor in the plasma membrane.
17563389	9	51	from	particular	1732:1741	arg1	elucidation					1615:1625	the ongoing elucidation	1603:1625	the ongoing elucidation of the role of glycosylation in G protein-coupled receptors	1603:1685	These results contribute to the ongoing elucidation of the role of glycosylation in G protein-coupled receptors and the study of the neurokinin receptors in particular.
17563389	9	51	from	particular	1732:1741	arg1	study					1695:1699	the study	1691:1699	the study of the neurokinin receptors in particular	1691:1741	These results contribute to the ongoing elucidation of the role of glycosylation in G protein-coupled receptors and the study of the neurokinin receptors in particular.
17563389	6	52	theme	glycosylation	1154:1166	arg1	sites					1168:1172	both N-linked glycosylation sites	1140:1172	both N-linked glycosylation sites	1140:1172	In terms of receptor function, the ablation of both N-linked glycosylation sites did not have a profound effect on the receptors' abilities to activate the MAP kinase families (p42/p44, JNK, and p38), but did affect SP-induced IL-8 secretion.
17563389	1	53	theme	protein-coupled	138:152	arg1	receptor					154:161	a G protein-coupled receptor	134:161	a G protein-coupled receptor involved in diverse functions including pain and inflammation	134:223	The neurokinin 1 receptor (NK1R), a G protein-coupled receptor involved in diverse functions including pain and inflammation, has two putative N-linked glycosylation sites, Asn-14 and Asn-18.
17563389	1	53	theme	protein-coupled	138:152	arg1	receptor					117:124	neurokinin 1 receptor	104:124	The neurokinin 1 receptor (NK1R)	100:131	The neurokinin 1 receptor (NK1R), a G protein-coupled receptor involved in diverse functions including pain and inflammation, has two putative N-linked glycosylation sites, Asn-14 and Asn-18.
17563389	9	54	from	role	1634:1637	arg1	receptors					1677:1685	G protein-coupled receptors	1659:1685	G protein-coupled receptors	1659:1685	These results contribute to the ongoing elucidation of the role of glycosylation in G protein-coupled receptors and the study of the neurokinin receptors in particular.
17563389	9	55	from	receptors	1719:1727	arg1	particular					1732:1741	particular	1732:1741	particular	1732:1741	These results contribute to the ongoing elucidation of the role of glycosylation in G protein-coupled receptors and the study of the neurokinin receptors in particular.
17563389	6	56	theme	kinase	1253:1258	arg1	families					1260:1267	the MAP kinase families	1245:1267	the MAP kinase families (p42/p44, JNK, and p38)	1245:1291	In terms of receptor function, the ablation of both N-linked glycosylation sites did not have a profound effect on the receptors' abilities to activate the MAP kinase families (p42/p44, JNK, and p38), but did affect SP-induced IL-8 secretion.
17563389	6	56	theme	kinase	1253:1258	arg1	JNK					1279:1281	JNK	1279:1281	JNK	1279:1281	In terms of receptor function, the ablation of both N-linked glycosylation sites did not have a profound effect on the receptors' abilities to activate the MAP kinase families (p42/p44, JNK, and p38), but did affect SP-induced IL-8 secretion.
17563389	6	56	theme	kinase	1253:1258	arg1	p38					1288:1290	p38	1288:1290	p38	1288:1290	In terms of receptor function, the ablation of both N-linked glycosylation sites did not have a profound effect on the receptors' abilities to activate the MAP kinase families (p42/p44, JNK, and p38), but did affect SP-induced IL-8 secretion.
17563389	6	56	theme	kinase	1253:1258	arg1	p42/p44					1270:1276	p42/p44	1270:1276	p42/p44	1270:1276	In terms of receptor function, the ablation of both N-linked glycosylation sites did not have a profound effect on the receptors' abilities to activate the MAP kinase families (p42/p44, JNK, and p38), but did affect SP-induced IL-8 secretion.
17563389	7	57	theme	wild-type	1475:1483	arg1	NK1R					1485:1488	wild-type NK1R	1475:1488	wild-type NK1R	1475:1488	All mutants were able to internalize, but the kinetics of internalization of the double mutant receptor was more rapid, when compared with wild-type NK1R.
17563389	4	58	theme	glycosylation	782:794	arg1	sites					796:800	glycosylation sites	782:800	glycosylation sites available	782:810	We observed that the magnitude of glycosylation as estimated by changes in gel migration depends on the number of glycosylation sites available, with the wild-type receptor containing the greatest amount of glycosylation.
17563389	0	59	link	N-linked	41:48	arg1	sites					64:68	N-linked glycosylation sites	41:68	N-linked glycosylation sites	41:68	Functional consequences of alteration of N-linked glycosylation sites on the neurokinin 1 receptor.
17563389	5	60	gly	nonglycosylated	1021:1035	arg1	NK1R					1037:1040	nonglycosylated NK1R	1021:1040	nonglycosylated NK1R	1021:1040	All mutant receptors were able to bind to substance P and neurokinin A ligand with similar affinities; however, the double mutant, nonglycosylated NK1R showed only half the B(max) of the wild-type NK1R.
17563389	5	60	gly	nonglycosylated	1021:1035	arg1	mutant					1013:1018	the double mutant	1002:1018	the double mutant	1002:1018	All mutant receptors were able to bind to substance P and neurokinin A ligand with similar affinities; however, the double mutant, nonglycosylated NK1R showed only half the B(max) of the wild-type NK1R.
17563389	8	61	theme	plasma	1558:1563	arg1	membrane					1565:1572	the plasma membrane	1554:1572	the plasma membrane	1554:1572	Therefore, glycosylation of NK1R may stabilize the receptor in the plasma membrane.
17563389	1	62	theme	diverse	175:181	arg1	functions					183:191	diverse functions	175:191	diverse functions including pain and inflammation	175:223	The neurokinin 1 receptor (NK1R), a G protein-coupled receptor involved in diverse functions including pain and inflammation, has two putative N-linked glycosylation sites, Asn-14 and Asn-18.
17563389	1	62	theme	diverse	175:181	arg1	inflammation					212:223	inflammation	212:223	inflammation	212:223	The neurokinin 1 receptor (NK1R), a G protein-coupled receptor involved in diverse functions including pain and inflammation, has two putative N-linked glycosylation sites, Asn-14 and Asn-18.
17563389	1	62	theme	diverse	175:181	arg1	pain					203:206	pain	203:206	pain	203:206	The neurokinin 1 receptor (NK1R), a G protein-coupled receptor involved in diverse functions including pain and inflammation, has two putative N-linked glycosylation sites, Asn-14 and Asn-18.
17563389	4	63	theme	greatest	856:863	arg1	amount					865:870	the greatest amount	852:870	the greatest amount of glycosylation	852:887	We observed that the magnitude of glycosylation as estimated by changes in gel migration depends on the number of glycosylation sites available, with the wild-type receptor containing the greatest amount of glycosylation.
17563389	4	63	theme	greatest	856:863	arg1	glycosylation					875:887	glycosylation	875:887	glycosylation	875:887	We observed that the magnitude of glycosylation as estimated by changes in gel migration depends on the number of glycosylation sites available, with the wild-type receptor containing the greatest amount of glycosylation.
17563389	9	64	from	study	1695:1699	arg1	receptors					1677:1685	G protein-coupled receptors	1659:1685	G protein-coupled receptors	1659:1685	These results contribute to the ongoing elucidation of the role of glycosylation in G protein-coupled receptors and the study of the neurokinin receptors in particular.
17563389	9	64	from	study	1695:1699	arg1	particular					1732:1741	particular	1732:1741	particular	1732:1741	These results contribute to the ongoing elucidation of the role of glycosylation in G protein-coupled receptors and the study of the neurokinin receptors in particular.
17563389	1	65	contain	has	226:228	arg2	sites					266:270	two putative N-linked glycosylation sites	230:270	two putative N-linked glycosylation sites	230:270	The neurokinin 1 receptor (NK1R), a G protein-coupled receptor involved in diverse functions including pain and inflammation, has two putative N-linked glycosylation sites, Asn-14 and Asn-18.
17563389	1	65	contain	has	226:228	arg2	Asn-14					273:278	Asn-14	273:278	Asn-14	273:278	The neurokinin 1 receptor (NK1R), a G protein-coupled receptor involved in diverse functions including pain and inflammation, has two putative N-linked glycosylation sites, Asn-14 and Asn-18.
17563389	1	65	contain	has	226:228	arg2	Asn-18					284:289	Asn-18	284:289	Asn-18	284:289	The neurokinin 1 receptor (NK1R), a G protein-coupled receptor involved in diverse functions including pain and inflammation, has two putative N-linked glycosylation sites, Asn-14 and Asn-18.
17563389	1	65	contain	has	226:228	arg1	receptor					117:124	neurokinin 1 receptor	104:124	The neurokinin 1 receptor (NK1R)	100:131	The neurokinin 1 receptor (NK1R), a G protein-coupled receptor involved in diverse functions including pain and inflammation, has two putative N-linked glycosylation sites, Asn-14 and Asn-18.
17563389	1	65	contain	has	226:228	arg1	NK1R					127:130	NK1R	127:130	NK1R	127:130	The neurokinin 1 receptor (NK1R), a G protein-coupled receptor involved in diverse functions including pain and inflammation, has two putative N-linked glycosylation sites, Asn-14 and Asn-18.
17563389	1	65	contain	has	226:228	arg1	receptor					154:161	a G protein-coupled receptor	134:161	a G protein-coupled receptor involved in diverse functions including pain and inflammation	134:223	The neurokinin 1 receptor (NK1R), a G protein-coupled receptor involved in diverse functions including pain and inflammation, has two putative N-linked glycosylation sites, Asn-14 and Asn-18.
17563389	4	66	gly	glycosylation	782:794	arg2	sites					796:800	glycosylation sites	782:800	glycosylation sites available	782:810	We observed that the magnitude of glycosylation as estimated by changes in gel migration depends on the number of glycosylation sites available, with the wild-type receptor containing the greatest amount of glycosylation.
17563389	5	67	dep	substance	932:940	arg1	P					942:942	P	942:942	P	942:942	All mutant receptors were able to bind to substance P and neurokinin A ligand with similar affinities; however, the double mutant, nonglycosylated NK1R showed only half the B(max) of the wild-type NK1R.
17563389	9	68	theme	ongoing	1607:1613	arg1	elucidation					1615:1625	the ongoing elucidation	1603:1625	the ongoing elucidation of the role of glycosylation in G protein-coupled receptors	1603:1685	These results contribute to the ongoing elucidation of the role of glycosylation in G protein-coupled receptors and the study of the neurokinin receptors in particular.
17563389	4	69	dep	magnitude	689:697	arg1	estimated					719:727	estimated	719:727	estimated by changes in gel migration	719:755	We observed that the magnitude of glycosylation as estimated by changes in gel migration depends on the number of glycosylation sites available, with the wild-type receptor containing the greatest amount of glycosylation.
17563389	4	70	theme	wild-type	822:830	arg1	receptor					832:839	the wild-type receptor	818:839	the wild-type receptor containing the greatest amount of glycosylation	818:887	We observed that the magnitude of glycosylation as estimated by changes in gel migration depends on the number of glycosylation sites available, with the wild-type receptor containing the greatest amount of glycosylation.
17563389	6	71	theme	function	1114:1121	arg1	terms					1096:1100	terms	1096:1100	terms of receptor function	1096:1121	In terms of receptor function, the ablation of both N-linked glycosylation sites did not have a profound effect on the receptors' abilities to activate the MAP kinase families (p42/p44, JNK, and p38), but did affect SP-induced IL-8 secretion.
17563389	6	72	theme	profound	1189:1196	arg1	effect					1198:1203	a profound effect	1187:1203	a profound effect	1187:1203	In terms of receptor function, the ablation of both N-linked glycosylation sites did not have a profound effect on the receptors' abilities to activate the MAP kinase families (p42/p44, JNK, and p38), but did affect SP-induced IL-8 secretion.
17563389	2	73	gly	glycosylation	498:510	arg2	sites					512:516	both glycosylation sites	493:516	both glycosylation sites	493:516	We studied the role of N-linked glycosylation in the functioning of the NK1R by constructing three receptor mutants: two single mutants (Asn --> Gln-14 and Asn --> Gln-18) and a double mutant, lacking both glycosylation sites.
17563389	7	74	theme	receptor	1431:1438	arg1	internalization					1394:1408	internalization	1394:1408	internalization of the double mutant receptor	1394:1438	All mutants were able to internalize, but the kinetics of internalization of the double mutant receptor was more rapid, when compared with wild-type NK1R.
17563389	2	75	theme	glycosylation	498:510	arg1	sites					512:516	both glycosylation sites	493:516	both glycosylation sites	493:516	We studied the role of N-linked glycosylation in the functioning of the NK1R by constructing three receptor mutants: two single mutants (Asn --> Gln-14 and Asn --> Gln-18) and a double mutant, lacking both glycosylation sites.
17563389	7	76	theme	double	1417:1422	arg1	receptor					1431:1438	the double mutant receptor	1413:1438	the double mutant receptor	1413:1438	All mutants were able to internalize, but the kinetics of internalization of the double mutant receptor was more rapid, when compared with wild-type NK1R.
17563389	2	77	theme	-->	452:454	arg1	mutants					420:426	two single mutants	409:426	two single mutants (Asn --> Gln-14 and Asn --> Gln-18)	409:462	We studied the role of N-linked glycosylation in the functioning of the NK1R by constructing three receptor mutants: two single mutants (Asn --> Gln-14 and Asn --> Gln-18) and a double mutant, lacking both glycosylation sites.
17563389	2	77	theme	-->	452:454	arg1	Gln-18					456:461	Asn --> Gln-18	448:461	Asn --> Gln-18	448:461	We studied the role of N-linked glycosylation in the functioning of the NK1R by constructing three receptor mutants: two single mutants (Asn --> Gln-14 and Asn --> Gln-18) and a double mutant, lacking both glycosylation sites.
17563389	0	78	from	consequences	11:22	arg1	receptor					90:97	the neurokinin 1 receptor	73:97	the neurokinin 1 receptor	73:97	Functional consequences of alteration of N-linked glycosylation sites on the neurokinin 1 receptor.
17563389	6	79	theme	MAP	1249:1251	arg1	families					1260:1267	the MAP kinase families	1245:1267	the MAP kinase families (p42/p44, JNK, and p38)	1245:1291	In terms of receptor function, the ablation of both N-linked glycosylation sites did not have a profound effect on the receptors' abilities to activate the MAP kinase families (p42/p44, JNK, and p38), but did affect SP-induced IL-8 secretion.
17563389	6	79	theme	MAP	1249:1251	arg1	JNK					1279:1281	JNK	1279:1281	JNK	1279:1281	In terms of receptor function, the ablation of both N-linked glycosylation sites did not have a profound effect on the receptors' abilities to activate the MAP kinase families (p42/p44, JNK, and p38), but did affect SP-induced IL-8 secretion.
17563389	6	79	theme	MAP	1249:1251	arg1	p38					1288:1290	p38	1288:1290	p38	1288:1290	In terms of receptor function, the ablation of both N-linked glycosylation sites did not have a profound effect on the receptors' abilities to activate the MAP kinase families (p42/p44, JNK, and p38), but did affect SP-induced IL-8 secretion.
17563389	6	79	theme	MAP	1249:1251	arg1	p42/p44					1270:1276	p42/p44	1270:1276	p42/p44	1270:1276	In terms of receptor function, the ablation of both N-linked glycosylation sites did not have a profound effect on the receptors' abilities to activate the MAP kinase families (p42/p44, JNK, and p38), but did affect SP-induced IL-8 secretion.
17563389	5	80	theme	nonglycosylated	1021:1035	arg1	NK1R					1037:1040	nonglycosylated NK1R	1021:1040	nonglycosylated NK1R	1021:1040	All mutant receptors were able to bind to substance P and neurokinin A ligand with similar affinities; however, the double mutant, nonglycosylated NK1R showed only half the B(max) of the wild-type NK1R.
17563389	5	80	theme	nonglycosylated	1021:1035	arg1	mutant					1013:1018	the double mutant	1002:1018	the double mutant	1002:1018	All mutant receptors were able to bind to substance P and neurokinin A ligand with similar affinities; however, the double mutant, nonglycosylated NK1R showed only half the B(max) of the wild-type NK1R.
17563389	6	81	dep	families	1260:1267	arg1	families					1260:1267	the MAP kinase families	1245:1267	the MAP kinase families (p42/p44, JNK, and p38)	1245:1291	In terms of receptor function, the ablation of both N-linked glycosylation sites did not have a profound effect on the receptors' abilities to activate the MAP kinase families (p42/p44, JNK, and p38), but did affect SP-induced IL-8 secretion.
17563389	6	81	dep	families	1260:1267	arg1	JNK					1279:1281	JNK	1279:1281	JNK	1279:1281	In terms of receptor function, the ablation of both N-linked glycosylation sites did not have a profound effect on the receptors' abilities to activate the MAP kinase families (p42/p44, JNK, and p38), but did affect SP-induced IL-8 secretion.
17563389	6	81	dep	families	1260:1267	arg1	p38					1288:1290	p38	1288:1290	p38	1288:1290	In terms of receptor function, the ablation of both N-linked glycosylation sites did not have a profound effect on the receptors' abilities to activate the MAP kinase families (p42/p44, JNK, and p38), but did affect SP-induced IL-8 secretion.
17563389	6	81	dep	families	1260:1267	arg1	p42/p44					1270:1276	p42/p44	1270:1276	p42/p44	1270:1276	In terms of receptor function, the ablation of both N-linked glycosylation sites did not have a profound effect on the receptors' abilities to activate the MAP kinase families (p42/p44, JNK, and p38), but did affect SP-induced IL-8 secretion.
17563389	2	82	dep	mutants	420:426	arg1	mutants					420:426	two single mutants	409:426	two single mutants (Asn --> Gln-14 and Asn --> Gln-18)	409:462	We studied the role of N-linked glycosylation in the functioning of the NK1R by constructing three receptor mutants: two single mutants (Asn --> Gln-14 and Asn --> Gln-18) and a double mutant, lacking both glycosylation sites.
17563389	2	82	dep	mutants	420:426	arg1	Gln-18					456:461	Asn --> Gln-18	448:461	Asn --> Gln-18	448:461	We studied the role of N-linked glycosylation in the functioning of the NK1R by constructing three receptor mutants: two single mutants (Asn --> Gln-14 and Asn --> Gln-18) and a double mutant, lacking both glycosylation sites.
17563389	2	82	dep	mutants	420:426	arg1	Gln-14					437:442	Asn --> Gln-14	429:442	Asn --> Gln-14	429:442	We studied the role of N-linked glycosylation in the functioning of the NK1R by constructing three receptor mutants: two single mutants (Asn --> Gln-14 and Asn --> Gln-18) and a double mutant, lacking both glycosylation sites.
17563389	6	83	contain	have	1182:1185	arg2	effect					1198:1203	a profound effect	1187:1203	a profound effect	1187:1203	In terms of receptor function, the ablation of both N-linked glycosylation sites did not have a profound effect on the receptors' abilities to activate the MAP kinase families (p42/p44, JNK, and p38), but did affect SP-induced IL-8 secretion.
17563389	6	83	contain	have	1182:1185	arg1	ablation					1128:1135	the ablation	1124:1135	the ablation of both N-linked glycosylation sites	1124:1172	In terms of receptor function, the ablation of both N-linked glycosylation sites did not have a profound effect on the receptors' abilities to activate the MAP kinase families (p42/p44, JNK, and p38), but did affect SP-induced IL-8 secretion.
17563389	2	84	theme	single	413:418	arg1	Gln-18					456:461	Asn --> Gln-18	448:461	Asn --> Gln-18	448:461	We studied the role of N-linked glycosylation in the functioning of the NK1R by constructing three receptor mutants: two single mutants (Asn --> Gln-14 and Asn --> Gln-18) and a double mutant, lacking both glycosylation sites.
17563389	2	84	theme	single	413:418	arg1	mutants					420:426	two single mutants	409:426	two single mutants (Asn --> Gln-14 and Asn --> Gln-18)	409:462	We studied the role of N-linked glycosylation in the functioning of the NK1R by constructing three receptor mutants: two single mutants (Asn --> Gln-14 and Asn --> Gln-18) and a double mutant, lacking both glycosylation sites.
17563389	2	84	theme	single	413:418	arg1	Gln-14					437:442	Asn --> Gln-14	429:442	Asn --> Gln-14	429:442	We studied the role of N-linked glycosylation in the functioning of the NK1R by constructing three receptor mutants: two single mutants (Asn --> Gln-14 and Asn --> Gln-18) and a double mutant, lacking both glycosylation sites.
17563389	0	85	theme	alteration	27:36	arg1	consequences					11:22	Functional consequences	0:22	Functional consequences of alteration of N-linked glycosylation sites on the neurokinin 1 receptor	0:97	Functional consequences of alteration of N-linked glycosylation sites on the neurokinin 1 receptor.
17563389	5	86	theme	wild-type	1077:1085	arg1	NK1R					1087:1090	the wild-type NK1R	1073:1090	the wild-type NK1R	1073:1090	All mutant receptors were able to bind to substance P and neurokinin A ligand with similar affinities; however, the double mutant, nonglycosylated NK1R showed only half the B(max) of the wild-type NK1R.
17563389	5	87	theme	mutant	894:899	arg1	receptors					901:909	All mutant receptors	890:909	All mutant receptors	890:909	All mutant receptors were able to bind to substance P and neurokinin A ligand with similar affinities; however, the double mutant, nonglycosylated NK1R showed only half the B(max) of the wild-type NK1R.
17563389	3	88	theme	transfection	538:549	arg1	system					551:556	a lentiviral transfection system	525:556	a lentiviral transfection system	525:556	Using a lentiviral transfection system, the mutants were stably transfected into NCM 460 cells, a nontransformed human colonic epithelial cell line.
17563389	2	89	theme	receptor	391:398	arg1	mutants					400:406	three receptor mutants	385:406	three receptor mutants	385:406	We studied the role of N-linked glycosylation in the functioning of the NK1R by constructing three receptor mutants: two single mutants (Asn --> Gln-14 and Asn --> Gln-18) and a double mutant, lacking both glycosylation sites.
17563389	0	90	theme	N-linked	41:48	arg1	sites					64:68	N-linked glycosylation sites	41:68	N-linked glycosylation sites	41:68	Functional consequences of alteration of N-linked glycosylation sites on the neurokinin 1 receptor.
17563389	2	91	theme	-->	433:435	arg1	mutants					420:426	two single mutants	409:426	two single mutants (Asn --> Gln-14 and Asn --> Gln-18)	409:462	We studied the role of N-linked glycosylation in the functioning of the NK1R by constructing three receptor mutants: two single mutants (Asn --> Gln-14 and Asn --> Gln-18) and a double mutant, lacking both glycosylation sites.
17563389	2	91	theme	-->	433:435	arg1	Gln-14					437:442	Asn --> Gln-14	429:442	Asn --> Gln-14	429:442	We studied the role of N-linked glycosylation in the functioning of the NK1R by constructing three receptor mutants: two single mutants (Asn --> Gln-14 and Asn --> Gln-18) and a double mutant, lacking both glycosylation sites.
17563389	0	92	theme	sites	64:68	arg1	alteration					27:36	alteration	27:36	alteration of N-linked glycosylation sites	27:68	Functional consequences of alteration of N-linked glycosylation sites on the neurokinin 1 receptor.
17563389	9	93	from	elucidation	1615:1625	arg1	receptors					1677:1685	G protein-coupled receptors	1659:1685	G protein-coupled receptors	1659:1685	These results contribute to the ongoing elucidation of the role of glycosylation in G protein-coupled receptors and the study of the neurokinin receptors in particular.
17563389	9	93	from	elucidation	1615:1625	arg1	particular					1732:1741	particular	1732:1741	particular	1732:1741	These results contribute to the ongoing elucidation of the role of glycosylation in G protein-coupled receptors and the study of the neurokinin receptors in particular.
17563389	0	94	gly	glycosylation	50:62	arg2	sites					64:68	N-linked glycosylation sites	41:68	N-linked glycosylation sites	41:68	Functional consequences of alteration of N-linked glycosylation sites on the neurokinin 1 receptor.
17563389	6	95	theme	IL-8	1320:1323	arg1	secretion					1325:1333	SP-induced IL-8 secretion	1309:1333	SP-induced IL-8 secretion	1309:1333	In terms of receptor function, the ablation of both N-linked glycosylation sites did not have a profound effect on the receptors' abilities to activate the MAP kinase families (p42/p44, JNK, and p38), but did affect SP-induced IL-8 secretion.
17563389	3	96	theme	colonic	638:644	arg1	line					662:665	nontransformed human colonic epithelial cell line	617:665	a nontransformed human colonic epithelial cell line	615:665	Using a lentiviral transfection system, the mutants were stably transfected into NCM 460 cells, a nontransformed human colonic epithelial cell line.
17563389	3	96	theme	colonic	638:644	arg1	cells					608:612	NCM 460 cells	600:612	NCM 460 cells	600:612	Using a lentiviral transfection system, the mutants were stably transfected into NCM 460 cells, a nontransformed human colonic epithelial cell line.
17563389	8	97	theme	NK1R	1519:1522	arg1	glycosylation					1502:1514	glycosylation	1502:1514	glycosylation of NK1R	1502:1522	Therefore, glycosylation of NK1R may stabilize the receptor in the plasma membrane.
23285087	5	0	theme	additional	1128:1137	arg1	asparagine					1139:1148	an additional asparagine	1125:1148	an additional asparagine at position 503	1125:1164	Our results showed that Asn134 and Asn516 are used for glycosylation under normal conditions; however, when Asn134 was mutagenized, an additional asparagine at position 503 is involved in the glycosylation process.
23285087	3	1	theme	experimental	490:501	arg1	evidence					503:510	experimental evidence	490:510	experimental evidence	490:510	However, experimental evidence is still lacking on how such a post-translational modification affect the transport activity of OATPs and which of the putative glycosylation sites are utilized in these transporter proteins.
23285087	2	2	gly	N-glycosylation	303:317	arg2	sites					319:323	Putative N-glycosylation sites	294:323	Putative N-glycosylation sites located in the extracellular loops 2 and 5	294:366	Putative N-glycosylation sites located in the extracellular loops 2 and 5 is considered a common feature of all OATPs and some members have been demonstrated to be glycosylated proteins.
23285087	3	3	theme	transporter	682:692	arg1	proteins					694:701	these transporter proteins	676:701	these transporter proteins	676:701	However, experimental evidence is still lacking on how such a post-translational modification affect the transport activity of OATPs and which of the putative glycosylation sites are utilized in these transporter proteins.
23285087	1	4	theme	key	174:176	arg1	determinants					178:189	key determinants	174:189	key determinants of absorption, distribution, metabolism and excretion (ADME) of various drugs, xenobiotics and toxins	174:291	Organic anion transporting polypeptides (OATPs) have been extensively recognized as key determinants of absorption, distribution, metabolism and excretion (ADME) of various drugs, xenobiotics and toxins.
23285087	1	4	theme	key	174:176	arg1	polypeptides					117:128	Organic anion transporting polypeptides	90:128	Organic anion transporting polypeptides (OATPs)	90:136	Organic anion transporting polypeptides (OATPs) have been extensively recognized as key determinants of absorption, distribution, metabolism and excretion (ADME) of various drugs, xenobiotics and toxins.
23285087	2	5	from	located	325:331	arg1	loops					354:358	the extracellular loops 2 and 5	336:366	the extracellular loops 2 and 5	336:366	Putative N-glycosylation sites located in the extracellular loops 2 and 5 is considered a common feature of all OATPs and some members have been demonstrated to be glycosylated proteins.
23285087	1	6	theme	various	255:261	arg1	drugs					263:267	various drugs	255:267	various drugs	255:267	Organic anion transporting polypeptides (OATPs) have been extensively recognized as key determinants of absorption, distribution, metabolism and excretion (ADME) of various drugs, xenobiotics and toxins.
23285087	7	7	theme	protein	1440:1446	arg1	stability					1411:1419	stability	1411:1419	stability of the transporter protein	1411:1446	Further studies revealed that glycosylation affected stability of the transporter protein and the unglycosylated mutant was retained within endoplasmic reticulum.
23285087	3	8	theme	post-translational	543:560	arg1	modification					562:573	such a post-translational modification	536:573	such a post-translational modification	536:573	However, experimental evidence is still lacking on how such a post-translational modification affect the transport activity of OATPs and which of the putative glycosylation sites are utilized in these transporter proteins.
23285087	1	9	theme	drugs	263:267	arg1	absorption					194:203	absorption	194:203	absorption	194:203	Organic anion transporting polypeptides (OATPs) have been extensively recognized as key determinants of absorption, distribution, metabolism and excretion (ADME) of various drugs, xenobiotics and toxins.
23285087	1	9	theme	drugs	263:267	arg1	ADME					246:249	ADME	246:249	ADME	246:249	Organic anion transporting polypeptides (OATPs) have been extensively recognized as key determinants of absorption, distribution, metabolism and excretion (ADME) of various drugs, xenobiotics and toxins.
23285087	1	9	theme	drugs	263:267	arg1	excretion					235:243	excretion	235:243	excretion	235:243	Organic anion transporting polypeptides (OATPs) have been extensively recognized as key determinants of absorption, distribution, metabolism and excretion (ADME) of various drugs, xenobiotics and toxins.
23285087	1	9	theme	drugs	263:267	arg1	metabolism					220:229	metabolism	220:229	metabolism	220:229	Organic anion transporting polypeptides (OATPs) have been extensively recognized as key determinants of absorption, distribution, metabolism and excretion (ADME) of various drugs, xenobiotics and toxins.
23285087	1	9	theme	drugs	263:267	arg1	distribution					206:217	distribution	206:217	distribution	206:217	Organic anion transporting polypeptides (OATPs) have been extensively recognized as key determinants of absorption, distribution, metabolism and excretion (ADME) of various drugs, xenobiotics and toxins.
23285087	2	10	theme	located	325:331	arg1	sites					319:323	Putative N-glycosylation sites	294:323	Putative N-glycosylation sites located in the extracellular loops 2 and 5	294:366	Putative N-glycosylation sites located in the extracellular loops 2 and 5 is considered a common feature of all OATPs and some members have been demonstrated to be glycosylated proteins.
23285087	2	11	from	loops	354:358	arg1	located					325:331	located	325:331	located	325:331	Putative N-glycosylation sites located in the extracellular loops 2 and 5 is considered a common feature of all OATPs and some members have been demonstrated to be glycosylated proteins.
23285087	5	12	theme	glycosylation	1185:1197	arg1	process					1199:1205	the glycosylation process	1181:1205	the glycosylation process	1181:1205	Our results showed that Asn134 and Asn516 are used for glycosylation under normal conditions; however, when Asn134 was mutagenized, an additional asparagine at position 503 is involved in the glycosylation process.
23285087	6	13	theme	transport	1338:1346	arg1	activity					1348:1355	transport activity	1338:1355	transport activity	1338:1355	Simultaneously replacement of all three asparagines with glutamines led to significantly reduced protein level as well as loss of transport activity.
23285087	6	14	theme	asparagines	1248:1258	arg1	replacement					1223:1233	replacement	1223:1233	replacement of all three asparagines with glutamines	1223:1274	Simultaneously replacement of all three asparagines with glutamines led to significantly reduced protein level as well as loss of transport activity.
23285087	5	15	theme	normal	1068:1073	arg1	conditions					1075:1084	normal conditions	1068:1084	normal conditions	1068:1084	Our results showed that Asn134 and Asn516 are used for glycosylation under normal conditions; however, when Asn134 was mutagenized, an additional asparagine at position 503 is involved in the glycosylation process.
23285087	2	16	theme	glycosylated	458:469	arg1	proteins					471:478	glycosylated proteins	458:478	glycosylated proteins	458:478	Putative N-glycosylation sites located in the extracellular loops 2 and 5 is considered a common feature of all OATPs and some members have been demonstrated to be glycosylated proteins.
23285087	1	17	theme	Organic	90:96	arg1	OATPs					131:135	OATPs	131:135	OATPs	131:135	Organic anion transporting polypeptides (OATPs) have been extensively recognized as key determinants of absorption, distribution, metabolism and excretion (ADME) of various drugs, xenobiotics and toxins.
23285087	1	17	theme	Organic	90:96	arg1	polypeptides					117:128	Organic anion transporting polypeptides	90:128	Organic anion transporting polypeptides (OATPs)	90:136	Organic anion transporting polypeptides (OATPs) have been extensively recognized as key determinants of absorption, distribution, metabolism and excretion (ADME) of various drugs, xenobiotics and toxins.
23285087	1	17	theme	Organic	90:96	arg1	determinants					178:189	key determinants	174:189	key determinants of absorption, distribution, metabolism and excretion (ADME) of various drugs, xenobiotics and toxins	174:291	Organic anion transporting polypeptides (OATPs) have been extensively recognized as key determinants of absorption, distribution, metabolism and excretion (ADME) of various drugs, xenobiotics and toxins.
23285087	7	18	gly	unglycosylated	1456:1469	arg1	mutant					1471:1476	the unglycosylated mutant	1452:1476	the unglycosylated mutant	1452:1476	Further studies revealed that glycosylation affected stability of the transporter protein and the unglycosylated mutant was retained within endoplasmic reticulum.
23285087	2	19	theme	common	384:389	arg1	feature					391:397	a common feature	382:397	a common feature of all OATPs	382:410	Putative N-glycosylation sites located in the extracellular loops 2 and 5 is considered a common feature of all OATPs and some members have been demonstrated to be glycosylated proteins.
23285087	7	20	gly	glycosylation	1388:1400	arg1	protein					1440:1446	the transporter protein	1424:1446	the transporter protein	1424:1446	Further studies revealed that glycosylation affected stability of the transporter protein and the unglycosylated mutant was retained within endoplasmic reticulum.
23285087	5	21	used	used	1039:1042	arg2	Asn134					1017:1022	Asn134	1017:1022	Asn134	1017:1022	Our results showed that Asn134 and Asn516 are used for glycosylation under normal conditions; however, when Asn134 was mutagenized, an additional asparagine at position 503 is involved in the glycosylation process.
23285087	5	21	used	used	1039:1042	arg2	Asn516					1028:1033	Asn516	1028:1033	Asn516	1028:1033	Our results showed that Asn134 and Asn516 are used for glycosylation under normal conditions; however, when Asn134 was mutagenized, an additional asparagine at position 503 is involved in the glycosylation process.
23285087	1	22	theme	anion	98:102	arg1	OATPs					131:135	OATPs	131:135	OATPs	131:135	Organic anion transporting polypeptides (OATPs) have been extensively recognized as key determinants of absorption, distribution, metabolism and excretion (ADME) of various drugs, xenobiotics and toxins.
23285087	1	22	theme	anion	98:102	arg1	polypeptides					117:128	Organic anion transporting polypeptides	90:128	Organic anion transporting polypeptides (OATPs)	90:136	Organic anion transporting polypeptides (OATPs) have been extensively recognized as key determinants of absorption, distribution, metabolism and excretion (ADME) of various drugs, xenobiotics and toxins.
23285087	1	22	theme	anion	98:102	arg1	determinants					178:189	key determinants	174:189	key determinants of absorption, distribution, metabolism and excretion (ADME) of various drugs, xenobiotics and toxins	174:291	Organic anion transporting polypeptides (OATPs) have been extensively recognized as key determinants of absorption, distribution, metabolism and excretion (ADME) of various drugs, xenobiotics and toxins.
23285087	1	23	theme	absorption	194:203	arg1	determinants					178:189	key determinants	174:189	key determinants of absorption, distribution, metabolism and excretion (ADME) of various drugs, xenobiotics and toxins	174:291	Organic anion transporting polypeptides (OATPs) have been extensively recognized as key determinants of absorption, distribution, metabolism and excretion (ADME) of various drugs, xenobiotics and toxins.
23285087	1	23	theme	absorption	194:203	arg1	polypeptides					117:128	Organic anion transporting polypeptides	90:128	Organic anion transporting polypeptides (OATPs)	90:136	Organic anion transporting polypeptides (OATPs) have been extensively recognized as key determinants of absorption, distribution, metabolism and excretion (ADME) of various drugs, xenobiotics and toxins.
23285087	1	24	theme	xenobiotics	270:280	arg1	absorption					194:203	absorption	194:203	absorption	194:203	Organic anion transporting polypeptides (OATPs) have been extensively recognized as key determinants of absorption, distribution, metabolism and excretion (ADME) of various drugs, xenobiotics and toxins.
23285087	1	24	theme	xenobiotics	270:280	arg1	ADME					246:249	ADME	246:249	ADME	246:249	Organic anion transporting polypeptides (OATPs) have been extensively recognized as key determinants of absorption, distribution, metabolism and excretion (ADME) of various drugs, xenobiotics and toxins.
23285087	1	24	theme	xenobiotics	270:280	arg1	excretion					235:243	excretion	235:243	excretion	235:243	Organic anion transporting polypeptides (OATPs) have been extensively recognized as key determinants of absorption, distribution, metabolism and excretion (ADME) of various drugs, xenobiotics and toxins.
23285087	1	24	theme	xenobiotics	270:280	arg1	metabolism					220:229	metabolism	220:229	metabolism	220:229	Organic anion transporting polypeptides (OATPs) have been extensively recognized as key determinants of absorption, distribution, metabolism and excretion (ADME) of various drugs, xenobiotics and toxins.
23285087	1	24	theme	xenobiotics	270:280	arg1	distribution					206:217	distribution	206:217	distribution	206:217	Organic anion transporting polypeptides (OATPs) have been extensively recognized as key determinants of absorption, distribution, metabolism and excretion (ADME) of various drugs, xenobiotics and toxins.
23285087	5	25	from	position	1153:1160	arg1	asparagine					1139:1148	an additional asparagine	1125:1148	an additional asparagine at position 503	1125:1164	Our results showed that Asn134 and Asn516 are used for glycosylation under normal conditions; however, when Asn134 was mutagenized, an additional asparagine at position 503 is involved in the glycosylation process.
23285087	1	26	theme	transporting	104:115	arg1	OATPs					131:135	OATPs	131:135	OATPs	131:135	Organic anion transporting polypeptides (OATPs) have been extensively recognized as key determinants of absorption, distribution, metabolism and excretion (ADME) of various drugs, xenobiotics and toxins.
23285087	1	26	theme	transporting	104:115	arg1	polypeptides					117:128	Organic anion transporting polypeptides	90:128	Organic anion transporting polypeptides (OATPs)	90:136	Organic anion transporting polypeptides (OATPs) have been extensively recognized as key determinants of absorption, distribution, metabolism and excretion (ADME) of various drugs, xenobiotics and toxins.
23285087	1	26	theme	transporting	104:115	arg1	determinants					178:189	key determinants	174:189	key determinants of absorption, distribution, metabolism and excretion (ADME) of various drugs, xenobiotics and toxins	174:291	Organic anion transporting polypeptides (OATPs) have been extensively recognized as key determinants of absorption, distribution, metabolism and excretion (ADME) of various drugs, xenobiotics and toxins.
23285087	4	27	dep	sites	866:870	arg1	Asn503					881:886	Asn503	881:886	Asn503	881:886	In the present study, we substituted asparagine residues that are possibly involved in N-glycosylation with glutamine residues and identified three glycosylation sites (Asn134, Asn503 and Asn516) within the structure of OATP1B1, an OATP member that is mainly expressed in the human liver.
23285087	4	27	dep	sites	866:870	arg1	Asn134					873:878	Asn134	873:878	Asn134	873:878	In the present study, we substituted asparagine residues that are possibly involved in N-glycosylation with glutamine residues and identified three glycosylation sites (Asn134, Asn503 and Asn516) within the structure of OATP1B1, an OATP member that is mainly expressed in the human liver.
23285087	4	27	dep	sites	866:870	arg1	sites					866:870	three glycosylation sites	846:870	three glycosylation sites (Asn134, Asn503 and Asn516) within the structure of OATP1B1, an OATP member that is mainly expressed in the human liver	846:990	In the present study, we substituted asparagine residues that are possibly involved in N-glycosylation with glutamine residues and identified three glycosylation sites (Asn134, Asn503 and Asn516) within the structure of OATP1B1, an OATP member that is mainly expressed in the human liver.
23285087	4	27	dep	sites	866:870	arg1	Asn516					892:897	Asn516	892:897	Asn516	892:897	In the present study, we substituted asparagine residues that are possibly involved in N-glycosylation with glutamine residues and identified three glycosylation sites (Asn134, Asn503 and Asn516) within the structure of OATP1B1, an OATP member that is mainly expressed in the human liver.
23285087	4	28	theme	glutamine	812:820	arg1	residues					822:829	glutamine residues	812:829	glutamine residues	812:829	In the present study, we substituted asparagine residues that are possibly involved in N-glycosylation with glutamine residues and identified three glycosylation sites (Asn134, Asn503 and Asn516) within the structure of OATP1B1, an OATP member that is mainly expressed in the human liver.
23285087	4	29	theme	OATP1B1	924:930	arg1	structure					911:919	the structure	907:919	the structure of OATP1B1, an OATP member that is mainly expressed in the human liver	907:990	In the present study, we substituted asparagine residues that are possibly involved in N-glycosylation with glutamine residues and identified three glycosylation sites (Asn134, Asn503 and Asn516) within the structure of OATP1B1, an OATP member that is mainly expressed in the human liver.
23285087	2	30	theme	N-glycosylation	303:317	arg1	sites					319:323	Putative N-glycosylation sites	294:323	Putative N-glycosylation sites located in the extracellular loops 2 and 5	294:366	Putative N-glycosylation sites located in the extracellular loops 2 and 5 is considered a common feature of all OATPs and some members have been demonstrated to be glycosylated proteins.
23285087	1	31	theme	distribution	206:217	arg1	determinants					178:189	key determinants	174:189	key determinants of absorption, distribution, metabolism and excretion (ADME) of various drugs, xenobiotics and toxins	174:291	Organic anion transporting polypeptides (OATPs) have been extensively recognized as key determinants of absorption, distribution, metabolism and excretion (ADME) of various drugs, xenobiotics and toxins.
23285087	1	31	theme	distribution	206:217	arg1	polypeptides					117:128	Organic anion transporting polypeptides	90:128	Organic anion transporting polypeptides (OATPs)	90:136	Organic anion transporting polypeptides (OATPs) have been extensively recognized as key determinants of absorption, distribution, metabolism and excretion (ADME) of various drugs, xenobiotics and toxins.
23285087	0	32	theme	proper	25:30	arg1	processing					32:41	proper processing	25:41	proper processing of organic anion transporting polypeptide 1B1	25:87	N-Glycosylation dictates proper processing of organic anion transporting polypeptide 1B1.
23285087	1	33	theme	toxins	286:291	arg1	absorption					194:203	absorption	194:203	absorption	194:203	Organic anion transporting polypeptides (OATPs) have been extensively recognized as key determinants of absorption, distribution, metabolism and excretion (ADME) of various drugs, xenobiotics and toxins.
23285087	1	33	theme	toxins	286:291	arg1	ADME					246:249	ADME	246:249	ADME	246:249	Organic anion transporting polypeptides (OATPs) have been extensively recognized as key determinants of absorption, distribution, metabolism and excretion (ADME) of various drugs, xenobiotics and toxins.
23285087	1	33	theme	toxins	286:291	arg1	excretion					235:243	excretion	235:243	excretion	235:243	Organic anion transporting polypeptides (OATPs) have been extensively recognized as key determinants of absorption, distribution, metabolism and excretion (ADME) of various drugs, xenobiotics and toxins.
23285087	1	33	theme	toxins	286:291	arg1	metabolism					220:229	metabolism	220:229	metabolism	220:229	Organic anion transporting polypeptides (OATPs) have been extensively recognized as key determinants of absorption, distribution, metabolism and excretion (ADME) of various drugs, xenobiotics and toxins.
23285087	1	33	theme	toxins	286:291	arg1	distribution					206:217	distribution	206:217	distribution	206:217	Organic anion transporting polypeptides (OATPs) have been extensively recognized as key determinants of absorption, distribution, metabolism and excretion (ADME) of various drugs, xenobiotics and toxins.
23285087	3	34	theme	glycosylation	640:652	arg1	sites					654:658	the putative glycosylation sites	627:658	the putative glycosylation sites	627:658	However, experimental evidence is still lacking on how such a post-translational modification affect the transport activity of OATPs and which of the putative glycosylation sites are utilized in these transporter proteins.
23285087	2	35	theme	Putative	294:301	arg1	sites					319:323	Putative N-glycosylation sites	294:323	Putative N-glycosylation sites located in the extracellular loops 2 and 5	294:366	Putative N-glycosylation sites located in the extracellular loops 2 and 5 is considered a common feature of all OATPs and some members have been demonstrated to be glycosylated proteins.
23285087	2	36	theme	OATPs	406:410	arg1	feature					391:397	a common feature	382:397	a common feature of all OATPs	382:410	Putative N-glycosylation sites located in the extracellular loops 2 and 5 is considered a common feature of all OATPs and some members have been demonstrated to be glycosylated proteins.
23285087	0	37	theme	organic	46:52	arg1	polypeptide					73:83	organic anion transporting polypeptide	46:83	organic anion transporting polypeptide 1B1	46:87	N-Glycosylation dictates proper processing of organic anion transporting polypeptide 1B1.
23285087	1	38	theme	metabolism	220:229	arg1	determinants					178:189	key determinants	174:189	key determinants of absorption, distribution, metabolism and excretion (ADME) of various drugs, xenobiotics and toxins	174:291	Organic anion transporting polypeptides (OATPs) have been extensively recognized as key determinants of absorption, distribution, metabolism and excretion (ADME) of various drugs, xenobiotics and toxins.
23285087	1	38	theme	metabolism	220:229	arg1	polypeptides					117:128	Organic anion transporting polypeptides	90:128	Organic anion transporting polypeptides (OATPs)	90:136	Organic anion transporting polypeptides (OATPs) have been extensively recognized as key determinants of absorption, distribution, metabolism and excretion (ADME) of various drugs, xenobiotics and toxins.
23285087	4	39	theme	human	980:984	arg1	liver					986:990	the human liver	976:990	the human liver	976:990	In the present study, we substituted asparagine residues that are possibly involved in N-glycosylation with glutamine residues and identified three glycosylation sites (Asn134, Asn503 and Asn516) within the structure of OATP1B1, an OATP member that is mainly expressed in the human liver.
23285087	3	40	used	utilized	664:671	arg2	which					618:622	which	618:622	which	618:622	However, experimental evidence is still lacking on how such a post-translational modification affect the transport activity of OATPs and which of the putative glycosylation sites are utilized in these transporter proteins.
23285087	3	41	gly	glycosylation	640:652	arg2	sites					654:658	the putative glycosylation sites	627:658	the putative glycosylation sites	627:658	However, experimental evidence is still lacking on how such a post-translational modification affect the transport activity of OATPs and which of the putative glycosylation sites are utilized in these transporter proteins.
23285087	2	42	gly	glycosylated	458:469	arg1	proteins					471:478	glycosylated proteins	458:478	glycosylated proteins	458:478	Putative N-glycosylation sites located in the extracellular loops 2 and 5 is considered a common feature of all OATPs and some members have been demonstrated to be glycosylated proteins.
23285087	0	43	theme	transporting	60:71	arg1	polypeptide					73:83	organic anion transporting polypeptide	46:83	organic anion transporting polypeptide 1B1	46:87	N-Glycosylation dictates proper processing of organic anion transporting polypeptide 1B1.
23285087	3	44	theme	putative	631:638	arg1	sites					654:658	the putative glycosylation sites	627:658	the putative glycosylation sites	627:658	However, experimental evidence is still lacking on how such a post-translational modification affect the transport activity of OATPs and which of the putative glycosylation sites are utilized in these transporter proteins.
23285087	7	45	theme	Further	1358:1364	arg1	studies					1366:1372	Further studies	1358:1372	Further studies	1358:1372	Further studies revealed that glycosylation affected stability of the transporter protein and the unglycosylated mutant was retained within endoplasmic reticulum.
23285087	4	46	theme	present	711:717	arg1	study					719:723	the present study	707:723	the present study	707:723	In the present study, we substituted asparagine residues that are possibly involved in N-glycosylation with glutamine residues and identified three glycosylation sites (Asn134, Asn503 and Asn516) within the structure of OATP1B1, an OATP member that is mainly expressed in the human liver.
23285087	0	47	theme	anion	54:58	arg1	polypeptide					73:83	organic anion transporting polypeptide	46:83	organic anion transporting polypeptide 1B1	46:87	N-Glycosylation dictates proper processing of organic anion transporting polypeptide 1B1.
23285087	4	48	theme	glycosylation	852:864	arg1	Asn503					881:886	Asn503	881:886	Asn503	881:886	In the present study, we substituted asparagine residues that are possibly involved in N-glycosylation with glutamine residues and identified three glycosylation sites (Asn134, Asn503 and Asn516) within the structure of OATP1B1, an OATP member that is mainly expressed in the human liver.
23285087	4	48	theme	glycosylation	852:864	arg1	Asn134					873:878	Asn134	873:878	Asn134	873:878	In the present study, we substituted asparagine residues that are possibly involved in N-glycosylation with glutamine residues and identified three glycosylation sites (Asn134, Asn503 and Asn516) within the structure of OATP1B1, an OATP member that is mainly expressed in the human liver.
23285087	4	48	theme	glycosylation	852:864	arg1	sites					866:870	three glycosylation sites	846:870	three glycosylation sites (Asn134, Asn503 and Asn516) within the structure of OATP1B1, an OATP member that is mainly expressed in the human liver	846:990	In the present study, we substituted asparagine residues that are possibly involved in N-glycosylation with glutamine residues and identified three glycosylation sites (Asn134, Asn503 and Asn516) within the structure of OATP1B1, an OATP member that is mainly expressed in the human liver.
23285087	4	48	theme	glycosylation	852:864	arg1	Asn516					892:897	Asn516	892:897	Asn516	892:897	In the present study, we substituted asparagine residues that are possibly involved in N-glycosylation with glutamine residues and identified three glycosylation sites (Asn134, Asn503 and Asn516) within the structure of OATP1B1, an OATP member that is mainly expressed in the human liver.
23285087	6	49	theme	protein	1305:1311	arg1	level					1313:1317	significantly reduced protein level	1283:1317	significantly reduced protein level as well as loss of transport activity	1283:1355	Simultaneously replacement of all three asparagines with glutamines led to significantly reduced protein level as well as loss of transport activity.
23285087	3	50	theme	transport	586:594	arg1	activity					596:603	the transport activity	582:603	the transport activity of OATPs	582:612	However, experimental evidence is still lacking on how such a post-translational modification affect the transport activity of OATPs and which of the putative glycosylation sites are utilized in these transporter proteins.
23285087	2	51	theme	extracellular	340:352	arg1	loops					354:358	the extracellular loops 2 and 5	336:366	the extracellular loops 2 and 5	336:366	Putative N-glycosylation sites located in the extracellular loops 2 and 5 is considered a common feature of all OATPs and some members have been demonstrated to be glycosylated proteins.
23285087	6	52	theme	reduced	1297:1303	arg1	level					1313:1317	significantly reduced protein level	1283:1317	significantly reduced protein level as well as loss of transport activity	1283:1355	Simultaneously replacement of all three asparagines with glutamines led to significantly reduced protein level as well as loss of transport activity.
23285087	2	53	dep	loops	354:358	arg1	5					366:366	5	366:366	5	366:366	Putative N-glycosylation sites located in the extracellular loops 2 and 5 is considered a common feature of all OATPs and some members have been demonstrated to be glycosylated proteins.
23285087	2	53	dep	loops	354:358	arg1	2					360:360	2	360:360	2	360:360	Putative N-glycosylation sites located in the extracellular loops 2 and 5 is considered a common feature of all OATPs and some members have been demonstrated to be glycosylated proteins.
23285087	1	54	theme	excretion	235:243	arg1	determinants					178:189	key determinants	174:189	key determinants of absorption, distribution, metabolism and excretion (ADME) of various drugs, xenobiotics and toxins	174:291	Organic anion transporting polypeptides (OATPs) have been extensively recognized as key determinants of absorption, distribution, metabolism and excretion (ADME) of various drugs, xenobiotics and toxins.
23285087	1	54	theme	excretion	235:243	arg1	polypeptides					117:128	Organic anion transporting polypeptides	90:128	Organic anion transporting polypeptides (OATPs)	90:136	Organic anion transporting polypeptides (OATPs) have been extensively recognized as key determinants of absorption, distribution, metabolism and excretion (ADME) of various drugs, xenobiotics and toxins.
23285087	7	55	theme	transporter	1428:1438	arg1	protein					1440:1446	the transporter protein	1424:1446	the transporter protein	1424:1446	Further studies revealed that glycosylation affected stability of the transporter protein and the unglycosylated mutant was retained within endoplasmic reticulum.
23285087	4	56	with	N-glycosylation	791:805	arg1	residues					822:829	glutamine residues	812:829	glutamine residues	812:829	In the present study, we substituted asparagine residues that are possibly involved in N-glycosylation with glutamine residues and identified three glycosylation sites (Asn134, Asn503 and Asn516) within the structure of OATP1B1, an OATP member that is mainly expressed in the human liver.
23285087	4	57	theme	asparagine	741:750	arg1	residues					752:759	asparagine residues	741:759	asparagine residues that are possibly involved in N-glycosylation with glutamine residues	741:829	In the present study, we substituted asparagine residues that are possibly involved in N-glycosylation with glutamine residues and identified three glycosylation sites (Asn134, Asn503 and Asn516) within the structure of OATP1B1, an OATP member that is mainly expressed in the human liver.
23285087	6	58	theme	activity	1348:1355	arg1	level					1313:1317	significantly reduced protein level	1283:1317	significantly reduced protein level as well as loss of transport activity	1283:1355	Simultaneously replacement of all three asparagines with glutamines led to significantly reduced protein level as well as loss of transport activity.
23285087	6	58	theme	activity	1348:1355	arg1	loss					1330:1333	loss	1330:1333	significantly reduced protein level as well as loss of transport activity	1283:1355	Simultaneously replacement of all three asparagines with glutamines led to significantly reduced protein level as well as loss of transport activity.
23285087	0	59	theme	1B1	85:87	arg1	processing					32:41	proper processing	25:41	proper processing of organic anion transporting polypeptide 1B1	25:87	N-Glycosylation dictates proper processing of organic anion transporting polypeptide 1B1.
23285087	3	60	theme	OATPs	608:612	arg1	activity					596:603	the transport activity	582:603	the transport activity of OATPs	582:612	However, experimental evidence is still lacking on how such a post-translational modification affect the transport activity of OATPs and which of the putative glycosylation sites are utilized in these transporter proteins.
23285087	4	61	gly	glycosylation	852:864	arg2	three					846:850	three	846:850	three	846:850	In the present study, we substituted asparagine residues that are possibly involved in N-glycosylation with glutamine residues and identified three glycosylation sites (Asn134, Asn503 and Asn516) within the structure of OATP1B1, an OATP member that is mainly expressed in the human liver.
23285087	4	61	gly	glycosylation	852:864	arg2	Asn516					892:897	Asn516	892:897	Asn516	892:897	In the present study, we substituted asparagine residues that are possibly involved in N-glycosylation with glutamine residues and identified three glycosylation sites (Asn134, Asn503 and Asn516) within the structure of OATP1B1, an OATP member that is mainly expressed in the human liver.
23285087	4	61	gly	glycosylation	852:864	arg2	Asn503					881:886	Asn503	881:886	Asn503	881:886	In the present study, we substituted asparagine residues that are possibly involved in N-glycosylation with glutamine residues and identified three glycosylation sites (Asn134, Asn503 and Asn516) within the structure of OATP1B1, an OATP member that is mainly expressed in the human liver.
23285087	4	61	gly	glycosylation	852:864	arg2	Asn134					873:878	Asn134	873:878	Asn134	873:878	In the present study, we substituted asparagine residues that are possibly involved in N-glycosylation with glutamine residues and identified three glycosylation sites (Asn134, Asn503 and Asn516) within the structure of OATP1B1, an OATP member that is mainly expressed in the human liver.
23285087	4	61	gly	glycosylation	852:864	arg2	sites					866:870	three glycosylation sites	846:870	three glycosylation sites (Asn134, Asn503 and Asn516) within the structure of OATP1B1, an OATP member that is mainly expressed in the human liver	846:990	In the present study, we substituted asparagine residues that are possibly involved in N-glycosylation with glutamine residues and identified three glycosylation sites (Asn134, Asn503 and Asn516) within the structure of OATP1B1, an OATP member that is mainly expressed in the human liver.
23285087	6	62	with	replacement	1223:1233	arg1	glutamines					1265:1274	glutamines	1265:1274	glutamines	1265:1274	Simultaneously replacement of all three asparagines with glutamines led to significantly reduced protein level as well as loss of transport activity.
23285087	0	63	theme	polypeptide	73:83	arg1	1B1					85:87	organic anion transporting polypeptide 1B1	46:87	organic anion transporting polypeptide 1B1	46:87	N-Glycosylation dictates proper processing of organic anion transporting polypeptide 1B1.
23285087	7	64	theme	endoplasmic	1498:1508	arg1	reticulum					1510:1518	endoplasmic reticulum	1498:1518	endoplasmic reticulum	1498:1518	Further studies revealed that glycosylation affected stability of the transporter protein and the unglycosylated mutant was retained within endoplasmic reticulum.
23285087	7	65	theme	unglycosylated	1456:1469	arg1	mutant					1471:1476	the unglycosylated mutant	1452:1476	the unglycosylated mutant	1452:1476	Further studies revealed that glycosylation affected stability of the transporter protein and the unglycosylated mutant was retained within endoplasmic reticulum.
23285087	4	66	theme	OATP	936:939	arg1	OATP1B1					924:930	OATP1B1	924:930	OATP1B1	924:930	In the present study, we substituted asparagine residues that are possibly involved in N-glycosylation with glutamine residues and identified three glycosylation sites (Asn134, Asn503 and Asn516) within the structure of OATP1B1, an OATP member that is mainly expressed in the human liver.
23285087	4	66	theme	OATP	936:939	arg1	member					941:946	an OATP member	933:946	an OATP member that is mainly expressed in the human liver	933:990	In the present study, we substituted asparagine residues that are possibly involved in N-glycosylation with glutamine residues and identified three glycosylation sites (Asn134, Asn503 and Asn516) within the structure of OATP1B1, an OATP member that is mainly expressed in the human liver.
22722744	0	0	theme	multiple	80:87	arg1	techniques					113:122	multiple mass spectrometry-based techniques	80:122	multiple mass spectrometry-based techniques	80:122	Comprehensive characterization of the N-glycosylation status of CD44s by use of multiple mass spectrometry-based techniques.
22722744	8	1	theme	glycosite	1468:1476	arg1	N100					1478:1481	glycosite N100	1468:1481	glycosite N100	1468:1481	Furthermore, the site-specific N-glycan distributions profiled by LC-ESI-MS(E) indicated that most glycosites bore complex-type glycans, except for glycosite N100, which was occupied by high-mannose-type N-glycans.
22722744	5	2	theme	N-glycosites	909:920	arg1	ratios					895:900	the occupation ratios	880:900	the occupation ratios of the N-glycosites	880:920	Specifically, the occupation ratios of the N-glycosites were first determined by MS with (18)O labeling; the results revealed five glycosites with different occupation ratios.
22722744	4	3	theme	CD44s	859:863	arg1	N-glycosylation					828:842	the N-glycosylation	824:842	the N-glycosylation of recombinant CD44s	824:863	In this work, an integrated strategy combining stable isotope labeling, chemical derivatization, hydrophilic-interaction liquid chromatographic (HILIC) separation, and mass spectrometric (MS) identification was used to perform a comprehensive qualitative and quantitative survey of the N-glycosylation of recombinant CD44s.
22722744	6	4	theme	chemical	1075:1082	arg1	derivatization					1084:1097	chemical derivatization	1075:1097	chemical derivatization	1075:1097	Next, N-glycans were profiled by chemical derivatization and exoglycosidase digestion, followed by MALDI-TOF-MS and HILIC-ESI-MS-MS analysis.
22722744	3	5	theme	prolific	494:501	arg1	type					528:531	CD44 standard type	514:531	CD44 standard type (CD44s)	514:539	In the CD44 family, the most prolific isoform is CD44 standard type (CD44s).
22722744	3	5	theme	prolific	494:501	arg1	isoform					503:509	the most prolific isoform	485:509	the most prolific isoform	485:509	In the CD44 family, the most prolific isoform is CD44 standard type (CD44s).
22722744	3	6	from	type	528:531	arg1	family					477:482	the CD44 family	468:482	the CD44 family	468:482	In the CD44 family, the most prolific isoform is CD44 standard type (CD44s).
22722744	5	7	theme	O	959:959	arg1	labeling					961:968	(18)O labeling	955:968	(18)O labeling	955:968	Specifically, the occupation ratios of the N-glycosites were first determined by MS with (18)O labeling; the results revealed five glycosites with different occupation ratios.
22722744	0	8	theme	spectrometry-based	94:111	arg1	techniques					113:122	multiple mass spectrometry-based techniques	80:122	multiple mass spectrometry-based techniques	80:122	Comprehensive characterization of the N-glycosylation status of CD44s by use of multiple mass spectrometry-based techniques.
22722744	9	9	theme	comprehensive	1553:1565	arg1	report					1567:1572	the first comprehensive report	1543:1572	the first comprehensive report of the N-glycosylation of CD44s	1543:1604	This is the first comprehensive report of the N-glycosylation of CD44s.
22722744	9	9	theme	comprehensive	1553:1565	arg1	This					1535:1538	This	1535:1538	This	1535:1538	This is the first comprehensive report of the N-glycosylation of CD44s.
22722744	6	10	theme	HILIC-ESI-MS-MS	1158:1172	arg1	analysis					1174:1181	HILIC-ESI-MS-MS analysis	1158:1181	HILIC-ESI-MS-MS analysis	1158:1181	Next, N-glycans were profiled by chemical derivatization and exoglycosidase digestion, followed by MALDI-TOF-MS and HILIC-ESI-MS-MS analysis.
22722744	5	11	theme	occupation	884:893	arg1	ratios					895:900	the occupation ratios	880:900	the occupation ratios of the N-glycosites	880:920	Specifically, the occupation ratios of the N-glycosites were first determined by MS with (18)O labeling; the results revealed five glycosites with different occupation ratios.
22722744	10	12	theme	status	1669:1674	arg1	characterization					1629:1644	characterization	1629:1644	characterization of the N-glycosylation status of CD44s	1629:1683	Figure Strategies for characterization of the N-glycosylation status of CD44s.
22722744	7	13	theme	complex-type	1265:1276	arg1	glycans					1278:1284	non-sialylated, fucosylated complex-type glycans	1237:1284	non-sialylated, fucosylated complex-type glycans	1237:1284	Interestingly, the quantitative analysis showed that non-sialylated, fucosylated complex-type glycans dominated the N-glycans of CD44s.
22722744	9	14	theme	N-glycosylation	1581:1595	arg1	report					1567:1572	the first comprehensive report	1543:1572	the first comprehensive report of the N-glycosylation of CD44s	1543:1604	This is the first comprehensive report of the N-glycosylation of CD44s.
22722744	9	14	theme	N-glycosylation	1581:1595	arg1	This					1535:1538	This	1535:1538	This	1535:1538	This is the first comprehensive report of the N-glycosylation of CD44s.
22722744	1	15	theme	growth	286:291	arg1	regulation					272:281	regulation	272:281	regulation of growth, survival, differentiation, and motility	272:332	The CD44 family are type-1 transmembrane glycoproteins which are important in mediating the response of cells to their microenvironment, including regulation of growth, survival, differentiation, and motility.
22722744	4	16	theme	HILIC	687:691	arg1	separation					694:703	hydrophilic-interaction liquid chromatographic (HILIC) separation	639:703	hydrophilic-interaction liquid chromatographic (HILIC) separation	639:703	In this work, an integrated strategy combining stable isotope labeling, chemical derivatization, hydrophilic-interaction liquid chromatographic (HILIC) separation, and mass spectrometric (MS) identification was used to perform a comprehensive qualitative and quantitative survey of the N-glycosylation of recombinant CD44s.
22722744	4	17	theme	N-glycosylation	828:842	arg1	survey					814:819	a comprehensive qualitative and quantitative survey	769:819	a comprehensive qualitative and quantitative survey of the N-glycosylation of recombinant CD44s	769:863	In this work, an integrated strategy combining stable isotope labeling, chemical derivatization, hydrophilic-interaction liquid chromatographic (HILIC) separation, and mass spectrometric (MS) identification was used to perform a comprehensive qualitative and quantitative survey of the N-glycosylation of recombinant CD44s.
22722744	4	18	theme	isotope	596:602	arg1	labeling					604:611	stable isotope labeling	589:611	stable isotope labeling	589:611	In this work, an integrated strategy combining stable isotope labeling, chemical derivatization, hydrophilic-interaction liquid chromatographic (HILIC) separation, and mass spectrometric (MS) identification was used to perform a comprehensive qualitative and quantitative survey of the N-glycosylation of recombinant CD44s.
22722744	3	19	theme	CD44	514:517	arg1	type					528:531	CD44 standard type	514:531	CD44 standard type (CD44s)	514:539	In the CD44 family, the most prolific isoform is CD44 standard type (CD44s).
22722744	3	19	theme	CD44	514:517	arg1	isoform					503:509	the most prolific isoform	485:509	the most prolific isoform	485:509	In the CD44 family, the most prolific isoform is CD44 standard type (CD44s).
22722744	3	19	theme	CD44	514:517	arg1	CD44s					534:538	CD44s	534:538	CD44s	534:538	In the CD44 family, the most prolific isoform is CD44 standard type (CD44s).
22722744	0	20	theme	techniques	113:122	arg1	use					73:75	use	73:75	use of multiple mass spectrometry-based techniques	73:122	Comprehensive characterization of the N-glycosylation status of CD44s by use of multiple mass spectrometry-based techniques.
22722744	6	21	theme	exoglycosidase	1103:1116	arg1	digestion					1118:1126	exoglycosidase digestion	1103:1126	exoglycosidase digestion	1103:1126	Next, N-glycans were profiled by chemical derivatization and exoglycosidase digestion, followed by MALDI-TOF-MS and HILIC-ESI-MS-MS analysis.
22722744	7	22	theme	quantitative	1203:1214	arg1	analysis					1216:1223	the quantitative analysis	1199:1223	the quantitative analysis	1199:1223	Interestingly, the quantitative analysis showed that non-sialylated, fucosylated complex-type glycans dominated the N-glycans of CD44s.
22722744	3	23	theme	standard	519:526	arg1	type					528:531	CD44 standard type	514:531	CD44 standard type (CD44s)	514:539	In the CD44 family, the most prolific isoform is CD44 standard type (CD44s).
22722744	3	23	theme	standard	519:526	arg1	isoform					503:509	the most prolific isoform	485:509	the most prolific isoform	485:509	In the CD44 family, the most prolific isoform is CD44 standard type (CD44s).
22722744	3	23	theme	standard	519:526	arg1	CD44s					534:538	CD44s	534:538	CD44s	534:538	In the CD44 family, the most prolific isoform is CD44 standard type (CD44s).
22722744	8	24	used	occupied	1494:1501	arg2	N100					1478:1481	glycosite N100	1468:1481	glycosite N100	1468:1481	Furthermore, the site-specific N-glycan distributions profiled by LC-ESI-MS(E) indicated that most glycosites bore complex-type glycans, except for glycosite N100, which was occupied by high-mannose-type N-glycans.
22722744	10	25	theme	N-glycosylation	1653:1667	arg1	status					1669:1674	the N-glycosylation status	1649:1674	the N-glycosylation status of CD44s	1649:1683	Figure Strategies for characterization of the N-glycosylation status of CD44s.
22722744	4	26	theme	recombinant	847:857	arg1	CD44s					859:863	recombinant CD44s	847:863	recombinant CD44s	847:863	In this work, an integrated strategy combining stable isotope labeling, chemical derivatization, hydrophilic-interaction liquid chromatographic (HILIC) separation, and mass spectrometric (MS) identification was used to perform a comprehensive qualitative and quantitative survey of the N-glycosylation of recombinant CD44s.
22722744	9	27	theme	CD44s	1600:1604	arg1	N-glycosylation					1581:1595	the N-glycosylation	1577:1595	the N-glycosylation of CD44s	1577:1604	This is the first comprehensive report of the N-glycosylation of CD44s.
22722744	8	28	contain	bore	1430:1433	arg1	glycosites					1419:1428	most glycosites	1414:1428	most glycosites	1414:1428	Furthermore, the site-specific N-glycan distributions profiled by LC-ESI-MS(E) indicated that most glycosites bore complex-type glycans, except for glycosite N100, which was occupied by high-mannose-type N-glycans.
22722744	8	28	contain	bore	1430:1433	arg2	glycans					1448:1454	complex-type glycans	1435:1454	complex-type glycans	1435:1454	Furthermore, the site-specific N-glycan distributions profiled by LC-ESI-MS(E) indicated that most glycosites bore complex-type glycans, except for glycosite N100, which was occupied by high-mannose-type N-glycans.
22722744	4	29	theme	liquid	663:668	arg1	separation					694:703	hydrophilic-interaction liquid chromatographic (HILIC) separation	639:703	hydrophilic-interaction liquid chromatographic (HILIC) separation	639:703	In this work, an integrated strategy combining stable isotope labeling, chemical derivatization, hydrophilic-interaction liquid chromatographic (HILIC) separation, and mass spectrometric (MS) identification was used to perform a comprehensive qualitative and quantitative survey of the N-glycosylation of recombinant CD44s.
22722744	0	30	theme	Comprehensive	0:12	arg1	characterization					14:29	Comprehensive characterization	0:29	Comprehensive characterization of the N-glycosylation status of CD44s by use of multiple mass spectrometry-based techniques.	0:123	Comprehensive characterization of the N-glycosylation status of CD44s by use of multiple mass spectrometry-based techniques.
22722744	9	31	gly	N-glycosylation	1581:1595	arg1	CD44s					1600:1604	CD44s	1600:1604	CD44s	1600:1604	This is the first comprehensive report of the N-glycosylation of CD44s.
22722744	8	32	theme	high-mannose-type	1506:1522	arg1	N-glycans					1524:1532	high-mannose-type N-glycans	1506:1532	high-mannose-type N-glycans	1506:1532	Furthermore, the site-specific N-glycan distributions profiled by LC-ESI-MS(E) indicated that most glycosites bore complex-type glycans, except for glycosite N100, which was occupied by high-mannose-type N-glycans.
22722744	4	33	theme	spectrometric	715:727	arg1	identification					734:747	mass spectrometric (MS) identification	710:747	mass spectrometric (MS) identification	710:747	In this work, an integrated strategy combining stable isotope labeling, chemical derivatization, hydrophilic-interaction liquid chromatographic (HILIC) separation, and mass spectrometric (MS) identification was used to perform a comprehensive qualitative and quantitative survey of the N-glycosylation of recombinant CD44s.
22722744	4	34	theme	hydrophilic-interaction	639:661	arg1	separation					694:703	hydrophilic-interaction liquid chromatographic (HILIC) separation	639:703	hydrophilic-interaction liquid chromatographic (HILIC) separation	639:703	In this work, an integrated strategy combining stable isotope labeling, chemical derivatization, hydrophilic-interaction liquid chromatographic (HILIC) separation, and mass spectrometric (MS) identification was used to perform a comprehensive qualitative and quantitative survey of the N-glycosylation of recombinant CD44s.
22722744	1	35	theme	survival	294:301	arg1	regulation					272:281	regulation	272:281	regulation of growth, survival, differentiation, and motility	272:332	The CD44 family are type-1 transmembrane glycoproteins which are important in mediating the response of cells to their microenvironment, including regulation of growth, survival, differentiation, and motility.
22722744	5	36	gly	N-glycosites	909:920	arg2	N-glycosites					909:920	the N-glycosites	905:920	the N-glycosites	905:920	Specifically, the occupation ratios of the N-glycosites were first determined by MS with (18)O labeling; the results revealed five glycosites with different occupation ratios.
22722744	8	37	theme	most	1414:1417	arg1	glycosites					1419:1428	most glycosites	1414:1428	most glycosites	1414:1428	Furthermore, the site-specific N-glycan distributions profiled by LC-ESI-MS(E) indicated that most glycosites bore complex-type glycans, except for glycosite N100, which was occupied by high-mannose-type N-glycans.
22722744	5	38	gly	glycosites	997:1006	arg2	glycosites					997:1006	five glycosites	992:1006	five glycosites with different occupation ratios	992:1039	Specifically, the occupation ratios of the N-glycosites were first determined by MS with (18)O labeling; the results revealed five glycosites with different occupation ratios.
22722744	10	39	gly	N-glycosylation	1653:1667	arg1	CD44s					1679:1683	CD44s	1679:1683	CD44s	1679:1683	Figure Strategies for characterization of the N-glycosylation status of CD44s.
22722744	4	40	theme	MS	730:731	arg1	identification					734:747	mass spectrometric (MS) identification	710:747	mass spectrometric (MS) identification	710:747	In this work, an integrated strategy combining stable isotope labeling, chemical derivatization, hydrophilic-interaction liquid chromatographic (HILIC) separation, and mass spectrometric (MS) identification was used to perform a comprehensive qualitative and quantitative survey of the N-glycosylation of recombinant CD44s.
22722744	4	41	gly	N-glycosylation	828:842	arg1	CD44s					859:863	recombinant CD44s	847:863	recombinant CD44s	847:863	In this work, an integrated strategy combining stable isotope labeling, chemical derivatization, hydrophilic-interaction liquid chromatographic (HILIC) separation, and mass spectrometric (MS) identification was used to perform a comprehensive qualitative and quantitative survey of the N-glycosylation of recombinant CD44s.
22722744	0	42	theme	status	54:59	arg1	characterization					14:29	Comprehensive characterization	0:29	Comprehensive characterization of the N-glycosylation status of CD44s by use of multiple mass spectrometry-based techniques.	0:123	Comprehensive characterization of the N-glycosylation status of CD44s by use of multiple mass spectrometry-based techniques.
22722744	1	43	theme	differentiation	304:318	arg1	regulation					272:281	regulation	272:281	regulation of growth, survival, differentiation, and motility	272:332	The CD44 family are type-1 transmembrane glycoproteins which are important in mediating the response of cells to their microenvironment, including regulation of growth, survival, differentiation, and motility.
22722744	7	44	dep	non-sialylated	1237:1250	arg1	fucosylated					1253:1263	fucosylated	1253:1263	fucosylated	1253:1263	Interestingly, the quantitative analysis showed that non-sialylated, fucosylated complex-type glycans dominated the N-glycans of CD44s.
22722744	4	45	theme	quantitative	801:812	arg1	survey					814:819	a comprehensive qualitative and quantitative survey	769:819	a comprehensive qualitative and quantitative survey of the N-glycosylation of recombinant CD44s	769:863	In this work, an integrated strategy combining stable isotope labeling, chemical derivatization, hydrophilic-interaction liquid chromatographic (HILIC) separation, and mass spectrometric (MS) identification was used to perform a comprehensive qualitative and quantitative survey of the N-glycosylation of recombinant CD44s.
22722744	4	46	theme	chemical	614:621	arg1	derivatization					623:636	chemical derivatization	614:636	chemical derivatization	614:636	In this work, an integrated strategy combining stable isotope labeling, chemical derivatization, hydrophilic-interaction liquid chromatographic (HILIC) separation, and mass spectrometric (MS) identification was used to perform a comprehensive qualitative and quantitative survey of the N-glycosylation of recombinant CD44s.
22722744	0	47	theme	N-glycosylation	38:52	arg1	status					54:59	the N-glycosylation status	34:59	the N-glycosylation status of CD44s	34:68	Comprehensive characterization of the N-glycosylation status of CD44s by use of multiple mass spectrometry-based techniques.
22722744	10	48	theme	CD44s	1679:1683	arg1	status					1669:1674	the N-glycosylation status	1649:1674	the N-glycosylation status of CD44s	1649:1683	Figure Strategies for characterization of the N-glycosylation status of CD44s.
22722744	8	49	gly	glycosite	1468:1476	arg2	glycosite					1468:1476	glycosite N100	1468:1481	glycosite N100	1468:1481	Furthermore, the site-specific N-glycan distributions profiled by LC-ESI-MS(E) indicated that most glycosites bore complex-type glycans, except for glycosite N100, which was occupied by high-mannose-type N-glycans.
22722744	6	50	dep	profiled	1063:1070	arg1	followed					1129:1136	followed	1129:1136	followed by MALDI-TOF-MS and HILIC-ESI-MS-MS analysis	1129:1181	Next, N-glycans were profiled by chemical derivatization and exoglycosidase digestion, followed by MALDI-TOF-MS and HILIC-ESI-MS-MS analysis.
22722744	1	51	theme	cells	229:233	arg1	response					217:224	the response	213:224	the response of cells to their microenvironment	213:259	The CD44 family are type-1 transmembrane glycoproteins which are important in mediating the response of cells to their microenvironment, including regulation of growth, survival, differentiation, and motility.
22722744	0	52	theme	CD44s	64:68	arg1	status					54:59	the N-glycosylation status	34:59	the N-glycosylation status of CD44s	34:68	Comprehensive characterization of the N-glycosylation status of CD44s by use of multiple mass spectrometry-based techniques.
22722744	5	53	with	glycosites	997:1006	arg1	ratios					1034:1039	different occupation ratios	1013:1039	different occupation ratios	1013:1039	Specifically, the occupation ratios of the N-glycosites were first determined by MS with (18)O labeling; the results revealed five glycosites with different occupation ratios.
22722744	8	54	theme	site-specific	1337:1349	arg1	distributions					1360:1372	the site-specific N-glycan distributions	1333:1372	the site-specific N-glycan distributions profiled by LC-ESI-MS(E)	1333:1397	Furthermore, the site-specific N-glycan distributions profiled by LC-ESI-MS(E) indicated that most glycosites bore complex-type glycans, except for glycosite N100, which was occupied by high-mannose-type N-glycans.
22722744	4	55	theme	integrated	559:568	arg1	strategy					570:577	an integrated strategy	556:577	an integrated strategy combining stable isotope labeling, chemical derivatization, hydrophilic-interaction liquid chromatographic (HILIC) separation, and mass spectrometric (MS) identification	556:747	In this work, an integrated strategy combining stable isotope labeling, chemical derivatization, hydrophilic-interaction liquid chromatographic (HILIC) separation, and mass spectrometric (MS) identification was used to perform a comprehensive qualitative and quantitative survey of the N-glycosylation of recombinant CD44s.
22722744	1	56	theme	motility	325:332	arg1	regulation					272:281	regulation	272:281	regulation of growth, survival, differentiation, and motility	272:332	The CD44 family are type-1 transmembrane glycoproteins which are important in mediating the response of cells to their microenvironment, including regulation of growth, survival, differentiation, and motility.
22722744	5	57	theme	different	1013:1021	arg1	ratios					1034:1039	different occupation ratios	1013:1039	different occupation ratios	1013:1039	Specifically, the occupation ratios of the N-glycosites were first determined by MS with (18)O labeling; the results revealed five glycosites with different occupation ratios.
22722744	8	58	theme	complex-type	1435:1446	arg1	glycans					1448:1454	complex-type glycans	1435:1454	complex-type glycans	1435:1454	Furthermore, the site-specific N-glycan distributions profiled by LC-ESI-MS(E) indicated that most glycosites bore complex-type glycans, except for glycosite N100, which was occupied by high-mannose-type N-glycans.
22722744	1	59	theme	CD44	129:132	arg1	family					134:139	The CD44 family	125:139	The CD44 family	125:139	The CD44 family are type-1 transmembrane glycoproteins which are important in mediating the response of cells to their microenvironment, including regulation of growth, survival, differentiation, and motility.
22722744	1	59	theme	CD44	129:132	arg1	regulation					272:281	regulation	272:281	regulation of growth, survival, differentiation, and motility	272:332	The CD44 family are type-1 transmembrane glycoproteins which are important in mediating the response of cells to their microenvironment, including regulation of growth, survival, differentiation, and motility.
22722744	1	59	theme	CD44	129:132	arg1	glycoproteins					166:178	type-1 transmembrane glycoproteins	145:178	type-1 transmembrane glycoproteins	145:178	The CD44 family are type-1 transmembrane glycoproteins which are important in mediating the response of cells to their microenvironment, including regulation of growth, survival, differentiation, and motility.
22722744	4	60	used	used	753:756	arg2	strategy					570:577	an integrated strategy	556:577	an integrated strategy combining stable isotope labeling, chemical derivatization, hydrophilic-interaction liquid chromatographic (HILIC) separation, and mass spectrometric (MS) identification	556:747	In this work, an integrated strategy combining stable isotope labeling, chemical derivatization, hydrophilic-interaction liquid chromatographic (HILIC) separation, and mass spectrometric (MS) identification was used to perform a comprehensive qualitative and quantitative survey of the N-glycosylation of recombinant CD44s.
22722744	5	61	theme	occupation	1023:1032	arg1	ratios					1034:1039	different occupation ratios	1013:1039	different occupation ratios	1013:1039	Specifically, the occupation ratios of the N-glycosites were first determined by MS with (18)O labeling; the results revealed five glycosites with different occupation ratios.
22722744	0	62	gly	N-glycosylation	38:52	arg1	CD44s					64:68	CD44s	64:68	CD44s	64:68	Comprehensive characterization of the N-glycosylation status of CD44s by use of multiple mass spectrometry-based techniques.
22722744	3	63	theme	CD44	472:475	arg1	family					477:482	the CD44 family	468:482	the CD44 family	468:482	In the CD44 family, the most prolific isoform is CD44 standard type (CD44s).
22722744	8	64	gly	glycosites	1419:1428	arg2	glycosites					1419:1428	most glycosites	1414:1428	most glycosites	1414:1428	Furthermore, the site-specific N-glycan distributions profiled by LC-ESI-MS(E) indicated that most glycosites bore complex-type glycans, except for glycosite N100, which was occupied by high-mannose-type N-glycans.
22722744	1	65	gly	glycoproteins	166:178	arg1	family					134:139	The CD44 family	125:139	The CD44 family	125:139	The CD44 family are type-1 transmembrane glycoproteins which are important in mediating the response of cells to their microenvironment, including regulation of growth, survival, differentiation, and motility.
22722744	1	65	gly	glycoproteins	166:178	arg1	regulation					272:281	regulation	272:281	regulation of growth, survival, differentiation, and motility	272:332	The CD44 family are type-1 transmembrane glycoproteins which are important in mediating the response of cells to their microenvironment, including regulation of growth, survival, differentiation, and motility.
22722744	1	65	gly	glycoproteins	166:178	arg1	glycoproteins					166:178	type-1 transmembrane glycoproteins	145:178	type-1 transmembrane glycoproteins	145:178	The CD44 family are type-1 transmembrane glycoproteins which are important in mediating the response of cells to their microenvironment, including regulation of growth, survival, differentiation, and motility.
22722744	7	66	theme	CD44s	1313:1317	arg1	N-glycans					1300:1308	the N-glycans	1296:1308	the N-glycans of CD44s	1296:1317	Interestingly, the quantitative analysis showed that non-sialylated, fucosylated complex-type glycans dominated the N-glycans of CD44s.
22722744	8	67	theme	N-glycan	1351:1358	arg1	distributions					1360:1372	the site-specific N-glycan distributions	1333:1372	the site-specific N-glycan distributions profiled by LC-ESI-MS(E)	1333:1397	Furthermore, the site-specific N-glycan distributions profiled by LC-ESI-MS(E) indicated that most glycosites bore complex-type glycans, except for glycosite N100, which was occupied by high-mannose-type N-glycans.
22722744	4	68	theme	chromatographic	670:684	arg1	separation					694:703	hydrophilic-interaction liquid chromatographic (HILIC) separation	639:703	hydrophilic-interaction liquid chromatographic (HILIC) separation	639:703	In this work, an integrated strategy combining stable isotope labeling, chemical derivatization, hydrophilic-interaction liquid chromatographic (HILIC) separation, and mass spectrometric (MS) identification was used to perform a comprehensive qualitative and quantitative survey of the N-glycosylation of recombinant CD44s.
22722744	4	69	theme	mass	710:713	arg1	identification					734:747	mass spectrometric (MS) identification	710:747	mass spectrometric (MS) identification	710:747	In this work, an integrated strategy combining stable isotope labeling, chemical derivatization, hydrophilic-interaction liquid chromatographic (HILIC) separation, and mass spectrometric (MS) identification was used to perform a comprehensive qualitative and quantitative survey of the N-glycosylation of recombinant CD44s.
22722744	7	70	theme	non-sialylated	1237:1250	arg1	glycans					1278:1284	non-sialylated, fucosylated complex-type glycans	1237:1284	non-sialylated, fucosylated complex-type glycans	1237:1284	Interestingly, the quantitative analysis showed that non-sialylated, fucosylated complex-type glycans dominated the N-glycans of CD44s.
22722744	2	71	theme	important	345:353	arg1	functions					355:363	All these important functions	335:363	All these important functions	335:363	All these important functions have been reported to be regulated by N-glycosylation; however, little is known about this process.
22722744	4	72	theme	qualitative	785:795	arg1	survey					814:819	a comprehensive qualitative and quantitative survey	769:819	a comprehensive qualitative and quantitative survey of the N-glycosylation of recombinant CD44s	769:863	In this work, an integrated strategy combining stable isotope labeling, chemical derivatization, hydrophilic-interaction liquid chromatographic (HILIC) separation, and mass spectrometric (MS) identification was used to perform a comprehensive qualitative and quantitative survey of the N-glycosylation of recombinant CD44s.
22722744	9	73	theme	first	1547:1551	arg1	report					1567:1572	the first comprehensive report	1543:1572	the first comprehensive report of the N-glycosylation of CD44s	1543:1604	This is the first comprehensive report of the N-glycosylation of CD44s.
22722744	9	73	theme	first	1547:1551	arg1	This					1535:1538	This	1535:1538	This	1535:1538	This is the first comprehensive report of the N-glycosylation of CD44s.
22722744	1	74	theme	type-1	145:150	arg1	family					134:139	The CD44 family	125:139	The CD44 family	125:139	The CD44 family are type-1 transmembrane glycoproteins which are important in mediating the response of cells to their microenvironment, including regulation of growth, survival, differentiation, and motility.
22722744	1	74	theme	type-1	145:150	arg1	regulation					272:281	regulation	272:281	regulation of growth, survival, differentiation, and motility	272:332	The CD44 family are type-1 transmembrane glycoproteins which are important in mediating the response of cells to their microenvironment, including regulation of growth, survival, differentiation, and motility.
22722744	1	74	theme	type-1	145:150	arg1	glycoproteins					166:178	type-1 transmembrane glycoproteins	145:178	type-1 transmembrane glycoproteins	145:178	The CD44 family are type-1 transmembrane glycoproteins which are important in mediating the response of cells to their microenvironment, including regulation of growth, survival, differentiation, and motility.
22722744	4	75	theme	stable	589:594	arg1	labeling					604:611	stable isotope labeling	589:611	stable isotope labeling	589:611	In this work, an integrated strategy combining stable isotope labeling, chemical derivatization, hydrophilic-interaction liquid chromatographic (HILIC) separation, and mass spectrometric (MS) identification was used to perform a comprehensive qualitative and quantitative survey of the N-glycosylation of recombinant CD44s.
22722744	7	76	gly	non-sialylated	1237:1250	arg1	glycans					1278:1284	non-sialylated, fucosylated complex-type glycans	1237:1284	non-sialylated, fucosylated complex-type glycans	1237:1284	Interestingly, the quantitative analysis showed that non-sialylated, fucosylated complex-type glycans dominated the N-glycans of CD44s.
22722744	4	77	theme	comprehensive	771:783	arg1	survey					814:819	a comprehensive qualitative and quantitative survey	769:819	a comprehensive qualitative and quantitative survey of the N-glycosylation of recombinant CD44s	769:863	In this work, an integrated strategy combining stable isotope labeling, chemical derivatization, hydrophilic-interaction liquid chromatographic (HILIC) separation, and mass spectrometric (MS) identification was used to perform a comprehensive qualitative and quantitative survey of the N-glycosylation of recombinant CD44s.
22722744	1	78	theme	transmembrane	152:164	arg1	family					134:139	The CD44 family	125:139	The CD44 family	125:139	The CD44 family are type-1 transmembrane glycoproteins which are important in mediating the response of cells to their microenvironment, including regulation of growth, survival, differentiation, and motility.
22722744	1	78	theme	transmembrane	152:164	arg1	regulation					272:281	regulation	272:281	regulation of growth, survival, differentiation, and motility	272:332	The CD44 family are type-1 transmembrane glycoproteins which are important in mediating the response of cells to their microenvironment, including regulation of growth, survival, differentiation, and motility.
22722744	1	78	theme	transmembrane	152:164	arg1	glycoproteins					166:178	type-1 transmembrane glycoproteins	145:178	type-1 transmembrane glycoproteins	145:178	The CD44 family are type-1 transmembrane glycoproteins which are important in mediating the response of cells to their microenvironment, including regulation of growth, survival, differentiation, and motility.
23661698	5	0	dep	cell	820:823	arg1	proliferation					839:851	proliferation	839:851	proliferation	839:851	We found that deglycosylated ephrin-A1 does not efficiently induce EphA2 receptor internalization and degradation, and does not activate the downstream signaling pathways involved in cell migration and proliferation.
23661698	5	0	dep	cell	820:823	arg1	migration					825:833	migration	825:833	migration	825:833	We found that deglycosylated ephrin-A1 does not efficiently induce EphA2 receptor internalization and degradation, and does not activate the downstream signaling pathways involved in cell migration and proliferation.
23661698	3	1	theme	ephrin-A1	479:487	arg1	biology					458:464	the biology	454:464	the biology of EphA2 and ephrin-A1	454:487	Here we report for the first time the significance of the glycosylation in the biology of EphA2 and ephrin-A1.
23661698	4	2	theme	several	568:574	arg1	assays					576:581	several assays	568:581	several assays using glioblastoma (GBM) cells and recombinant EphA2	568:634	Ephrin-A1 was enzymatically deglycosylated, and its activity was evaluated in several assays using glioblastoma (GBM) cells and recombinant EphA2.
23661698	0	3	theme	preferred	76:84	arg1	ligand					86:91	a preferred ligand	74:91	a preferred ligand for EphA2 receptor tyrosine kinase	74:126	Biological and structural characterization of glycosylation on ephrin-A1, a preferred ligand for EphA2 receptor tyrosine kinase.
23661698	0	3	theme	preferred	76:84	arg1	ephrin-A1					63:71	ephrin-A1	63:71	ephrin-A1	63:71	Biological and structural characterization of glycosylation on ephrin-A1, a preferred ligand for EphA2 receptor tyrosine kinase.
23661698	0	4	theme	EphA2	97:101	arg1	kinase					121:126	EphA2 receptor tyrosine kinase	97:126	EphA2 receptor tyrosine kinase	97:126	Biological and structural characterization of glycosylation on ephrin-A1, a preferred ligand for EphA2 receptor tyrosine kinase.
23661698	2	5	theme	crystal	277:283	arg1	structure					285:293	The crystal structure	273:293	The crystal structure of the ligand-receptor complex	273:324	The crystal structure of the ligand-receptor complex revealed a glycosylation on the Asn-26 of ephrin-A1.
23661698	8	6	theme	EphA2	1196:1200	arg1	residues					1184:1191	two residues	1180:1191	two residues	1180:1191	Analysis of Eph/ephrin crystal structures reveals an interaction between the ligand's carbohydrates and two residues of EphA2: Asp-78 and Lys-136.
23661698	8	6	theme	EphA2	1196:1200	arg1	Lys-136					1214:1220	Lys-136	1214:1220	Lys-136	1214:1220	Analysis of Eph/ephrin crystal structures reveals an interaction between the ligand's carbohydrates and two residues of EphA2: Asp-78 and Lys-136.
23661698	8	6	theme	EphA2	1196:1200	arg1	Asp-78					1203:1208	Asp-78	1203:1208	Asp-78	1203:1208	Analysis of Eph/ephrin crystal structures reveals an interaction between the ligand's carbohydrates and two residues of EphA2: Asp-78 and Lys-136.
23661698	8	6	theme	EphA2	1196:1200	arg1	EphA2					1196:1200	EphA2	1196:1200	EphA2	1196:1200	Analysis of Eph/ephrin crystal structures reveals an interaction between the ligand's carbohydrates and two residues of EphA2: Asp-78 and Lys-136.
23661698	8	6	theme	EphA2	1196:1200	arg1	carbohydrates					1162:1174	the ligand's carbohydrates	1149:1174	the ligand's carbohydrates	1149:1174	Analysis of Eph/ephrin crystal structures reveals an interaction between the ligand's carbohydrates and two residues of EphA2: Asp-78 and Lys-136.
23661698	6	7	theme	deglycosylated	911:924	arg1	ephrin-A1					926:934	deglycosylated ephrin-A1	911:934	deglycosylated ephrin-A1	911:934	Data obtained by surface plasmon resonance confirms that deglycosylated ephrin-A1 does not bind EphA2 with high affinity.
23661698	7	8	from	Mutations	976:984	arg1	ephrin-A1					1015:1023	ephrin-A1	1015:1023	ephrin-A1	1015:1023	Mutations in the glycosylation site on ephrin-A1 result in protein aggregation and mislocalization.
23661698	7	8	from	Mutations	976:984	arg1	site					1007:1010	the glycosylation site	989:1010	the glycosylation site on ephrin-A1	989:1023	Mutations in the glycosylation site on ephrin-A1 result in protein aggregation and mislocalization.
23661698	2	9	from	glycosylation	337:349	arg1	Asn-26					358:363	the Asn-26	354:363	the Asn-26 of ephrin-A1	354:376	The crystal structure of the ligand-receptor complex revealed a glycosylation on the Asn-26 of ephrin-A1.
23661698	2	10	theme	complex	318:324	arg1	structure					285:293	The crystal structure	273:293	The crystal structure of the ligand-receptor complex	273:324	The crystal structure of the ligand-receptor complex revealed a glycosylation on the Asn-26 of ephrin-A1.
23661698	0	11	theme	tyrosine	112:119	arg1	kinase					121:126	EphA2 receptor tyrosine kinase	97:126	EphA2 receptor tyrosine kinase	97:126	Biological and structural characterization of glycosylation on ephrin-A1, a preferred ligand for EphA2 receptor tyrosine kinase.
23661698	9	12	theme	EphA2	1341:1345	arg1	receptor					1347:1354	the EphA2 receptor	1337:1354	the EphA2 receptor	1337:1354	These findings suggest that the glycosylation on ephrin-A1 plays a critical role in the binding and activation of the EphA2 receptor.
23661698	8	13	theme	Eph/ephrin	1088:1097	arg1	structures					1107:1116	Eph/ephrin crystal structures	1088:1116	Eph/ephrin crystal structures	1088:1116	Analysis of Eph/ephrin crystal structures reveals an interaction between the ligand's carbohydrates and two residues of EphA2: Asp-78 and Lys-136.
23661698	5	14	theme	downstream	778:787	arg1	pathways					799:806	the downstream signaling pathways	774:806	the downstream signaling pathways involved in cell migration and proliferation	774:851	We found that deglycosylated ephrin-A1 does not efficiently induce EphA2 receptor internalization and degradation, and does not activate the downstream signaling pathways involved in cell migration and proliferation.
23661698	0	15	theme	receptor	103:110	arg1	kinase					121:126	EphA2 receptor tyrosine kinase	97:126	EphA2 receptor tyrosine kinase	97:126	Biological and structural characterization of glycosylation on ephrin-A1, a preferred ligand for EphA2 receptor tyrosine kinase.
23661698	9	16	theme	receptor	1347:1354	arg1	activation					1323:1332	activation	1323:1332	activation	1323:1332	These findings suggest that the glycosylation on ephrin-A1 plays a critical role in the binding and activation of the EphA2 receptor.
23661698	9	16	theme	receptor	1347:1354	arg1	binding					1311:1317	binding	1311:1317	binding	1311:1317	These findings suggest that the glycosylation on ephrin-A1 plays a critical role in the binding and activation of the EphA2 receptor.
23661698	7	17	from	site	1007:1010	arg1	ephrin-A1					1015:1023	ephrin-A1	1015:1023	ephrin-A1	1015:1023	Mutations in the glycosylation site on ephrin-A1 result in protein aggregation and mislocalization.
23661698	8	18	dep	carbohydrates	1162:1174	arg1	Lys-136					1214:1220	Lys-136	1214:1220	Lys-136	1214:1220	Analysis of Eph/ephrin crystal structures reveals an interaction between the ligand's carbohydrates and two residues of EphA2: Asp-78 and Lys-136.
23661698	8	18	dep	carbohydrates	1162:1174	arg1	Asp-78					1203:1208	Asp-78	1203:1208	Asp-78	1203:1208	Analysis of Eph/ephrin crystal structures reveals an interaction between the ligand's carbohydrates and two residues of EphA2: Asp-78 and Lys-136.
23661698	8	18	dep	carbohydrates	1162:1174	arg1	carbohydrates					1162:1174	the ligand's carbohydrates	1149:1174	the ligand's carbohydrates	1149:1174	Analysis of Eph/ephrin crystal structures reveals an interaction between the ligand's carbohydrates and two residues of EphA2: Asp-78 and Lys-136.
23661698	8	19	theme	structures	1107:1116	arg1	Analysis					1076:1083	Analysis	1076:1083	Analysis of Eph/ephrin crystal structures	1076:1116	Analysis of Eph/ephrin crystal structures reveals an interaction between the ligand's carbohydrates and two residues of EphA2: Asp-78 and Lys-136.
23661698	2	20	theme	ligand-receptor	302:316	arg1	complex					318:324	the ligand-receptor complex	298:324	the ligand-receptor complex	298:324	The crystal structure of the ligand-receptor complex revealed a glycosylation on the Asn-26 of ephrin-A1.
23661698	0	21	theme	Biological	0:9	arg1	characterization					26:41	Biological and structural characterization	0:41	Biological and structural characterization of glycosylation on ephrin-A1, a preferred ligand for EphA2 receptor tyrosine kinase.	0:127	Biological and structural characterization of glycosylation on ephrin-A1, a preferred ligand for EphA2 receptor tyrosine kinase.
23661698	8	22	theme	crystal	1099:1105	arg1	structures					1107:1116	Eph/ephrin crystal structures	1088:1116	Eph/ephrin crystal structures	1088:1116	Analysis of Eph/ephrin crystal structures reveals an interaction between the ligand's carbohydrates and two residues of EphA2: Asp-78 and Lys-136.
23661698	2	23	theme	ephrin-A1	368:376	arg1	Asn-26					358:363	the Asn-26	354:363	the Asn-26 of ephrin-A1	354:376	The crystal structure of the ligand-receptor complex revealed a glycosylation on the Asn-26 of ephrin-A1.
23661698	0	24	theme	structural	15:24	arg1	characterization					26:41	Biological and structural characterization	0:41	Biological and structural characterization of glycosylation on ephrin-A1, a preferred ligand for EphA2 receptor tyrosine kinase.	0:127	Biological and structural characterization of glycosylation on ephrin-A1, a preferred ligand for EphA2 receptor tyrosine kinase.
23661698	7	25	theme	glycosylation	993:1005	arg1	site					1007:1010	the glycosylation site	989:1010	the glycosylation site on ephrin-A1	989:1023	Mutations in the glycosylation site on ephrin-A1 result in protein aggregation and mislocalization.
23661698	6	26	theme	plasmon	879:885	arg1	resonance					887:895	surface plasmon resonance	871:895	surface plasmon resonance	871:895	Data obtained by surface plasmon resonance confirms that deglycosylated ephrin-A1 does not bind EphA2 with high affinity.
23661698	1	27	theme	malignancies	196:207	arg1	number					186:191	a number	184:191	a number of malignancies	184:207	The EphA2 receptor tyrosine kinase is overexpressed in a number of malignancies and is activated by ephrin ligands, most commonly by ephrin-A1.
23661698	0	28	theme	glycosylation	46:58	arg1	characterization					26:41	Biological and structural characterization	0:41	Biological and structural characterization of glycosylation on ephrin-A1, a preferred ligand for EphA2 receptor tyrosine kinase.	0:127	Biological and structural characterization of glycosylation on ephrin-A1, a preferred ligand for EphA2 receptor tyrosine kinase.
23661698	7	29	gly	glycosylation	993:1005	arg2	site					1007:1010	the glycosylation site	989:1010	the glycosylation site on ephrin-A1	989:1023	Mutations in the glycosylation site on ephrin-A1 result in protein aggregation and mislocalization.
23661698	5	30	theme	EphA2	704:708	arg1	internalization					719:733	EphA2 receptor internalization	704:733	EphA2 receptor internalization	704:733	We found that deglycosylated ephrin-A1 does not efficiently induce EphA2 receptor internalization and degradation, and does not activate the downstream signaling pathways involved in cell migration and proliferation.
23661698	6	31	theme	surface	871:877	arg1	resonance					887:895	surface plasmon resonance	871:895	surface plasmon resonance	871:895	Data obtained by surface plasmon resonance confirms that deglycosylated ephrin-A1 does not bind EphA2 with high affinity.
23661698	7	32	from	ephrin-A1	1015:1023	arg1	Mutations					976:984	Mutations	976:984	Mutations in the glycosylation site on ephrin-A1	976:1023	Mutations in the glycosylation site on ephrin-A1 result in protein aggregation and mislocalization.
23661698	3	33	theme	first	402:406	arg1	time					408:411	the first time	398:411	the first time	398:411	Here we report for the first time the significance of the glycosylation in the biology of EphA2 and ephrin-A1.
23661698	5	34	theme	receptor	710:717	arg1	internalization					719:733	EphA2 receptor internalization	704:733	EphA2 receptor internalization	704:733	We found that deglycosylated ephrin-A1 does not efficiently induce EphA2 receptor internalization and degradation, and does not activate the downstream signaling pathways involved in cell migration and proliferation.
23661698	7	35	theme	protein	1035:1041	arg1	aggregation					1043:1053	protein aggregation	1035:1053	protein aggregation	1035:1053	Mutations in the glycosylation site on ephrin-A1 result in protein aggregation and mislocalization.
23661698	3	36	theme	glycosylation	437:449	arg1	significance					417:428	the significance	413:428	the significance of the glycosylation in the biology of EphA2 and ephrin-A1	413:487	Here we report for the first time the significance of the glycosylation in the biology of EphA2 and ephrin-A1.
23661698	5	37	theme	signaling	789:797	arg1	pathways					799:806	the downstream signaling pathways	774:806	the downstream signaling pathways involved in cell migration and proliferation	774:851	We found that deglycosylated ephrin-A1 does not efficiently induce EphA2 receptor internalization and degradation, and does not activate the downstream signaling pathways involved in cell migration and proliferation.
23661698	6	38	theme	high	961:964	arg1	affinity					966:973	high affinity	961:973	high affinity	961:973	Data obtained by surface plasmon resonance confirms that deglycosylated ephrin-A1 does not bind EphA2 with high affinity.
23661698	5	39	theme	deglycosylated	651:664	arg1	ephrin-A1					666:674	deglycosylated ephrin-A1	651:674	deglycosylated ephrin-A1	651:674	We found that deglycosylated ephrin-A1 does not efficiently induce EphA2 receptor internalization and degradation, and does not activate the downstream signaling pathways involved in cell migration and proliferation.
23661698	3	40	theme	EphA2	469:473	arg1	biology					458:464	the biology	454:464	the biology of EphA2 and ephrin-A1	454:487	Here we report for the first time the significance of the glycosylation in the biology of EphA2 and ephrin-A1.
23661698	2	41	gly	glycosylation	337:349	arg1	Asn-26					358:363	the Asn-26	354:363	the Asn-26 of ephrin-A1	354:376	The crystal structure of the ligand-receptor complex revealed a glycosylation on the Asn-26 of ephrin-A1.
23661698	9	42	theme	critical	1290:1297	arg1	role					1299:1302	a critical role	1288:1302	a critical role	1288:1302	These findings suggest that the glycosylation on ephrin-A1 plays a critical role in the binding and activation of the EphA2 receptor.
23661698	9	43	from	glycosylation	1255:1267	arg1	ephrin-A1					1272:1280	ephrin-A1	1272:1280	ephrin-A1	1272:1280	These findings suggest that the glycosylation on ephrin-A1 plays a critical role in the binding and activation of the EphA2 receptor.
23661698	6	44	gly	deglycosylated	911:924	arg1	ephrin-A1					926:934	deglycosylated ephrin-A1	911:934	deglycosylated ephrin-A1	911:934	Data obtained by surface plasmon resonance confirms that deglycosylated ephrin-A1 does not bind EphA2 with high affinity.
23661698	1	45	theme	EphA2	133:137	arg1	kinase					157:162	The EphA2 receptor tyrosine kinase	129:162	The EphA2 receptor tyrosine kinase	129:162	The EphA2 receptor tyrosine kinase is overexpressed in a number of malignancies and is activated by ephrin ligands, most commonly by ephrin-A1.
23661698	4	46	theme	glioblastoma	589:600	arg1	cells					608:612	glioblastoma (GBM) cells	589:612	glioblastoma (GBM) cells	589:612	Ephrin-A1 was enzymatically deglycosylated, and its activity was evaluated in several assays using glioblastoma (GBM) cells and recombinant EphA2.
23661698	4	47	theme	recombinant	618:628	arg1	EphA2					630:634	recombinant EphA2	618:634	recombinant EphA2	618:634	Ephrin-A1 was enzymatically deglycosylated, and its activity was evaluated in several assays using glioblastoma (GBM) cells and recombinant EphA2.
23661698	4	48	gly	deglycosylated	518:531	arg1	Ephrin-A1					490:498	Ephrin-A1	490:498	Ephrin-A1	490:498	Ephrin-A1 was enzymatically deglycosylated, and its activity was evaluated in several assays using glioblastoma (GBM) cells and recombinant EphA2.
23661698	1	49	theme	receptor	139:146	arg1	kinase					157:162	The EphA2 receptor tyrosine kinase	129:162	The EphA2 receptor tyrosine kinase	129:162	The EphA2 receptor tyrosine kinase is overexpressed in a number of malignancies and is activated by ephrin ligands, most commonly by ephrin-A1.
23661698	5	50	gly	deglycosylated	651:664	arg1	ephrin-A1					666:674	deglycosylated ephrin-A1	651:674	deglycosylated ephrin-A1	651:674	We found that deglycosylated ephrin-A1 does not efficiently induce EphA2 receptor internalization and degradation, and does not activate the downstream signaling pathways involved in cell migration and proliferation.
23661698	1	51	theme	ephrin	229:234	arg1	ligands					236:242	ephrin ligands	229:242	ephrin ligands	229:242	The EphA2 receptor tyrosine kinase is overexpressed in a number of malignancies and is activated by ephrin ligands, most commonly by ephrin-A1.
23661698	9	52	gly	glycosylation	1255:1267	arg1	ephrin-A1					1272:1280	ephrin-A1	1272:1280	ephrin-A1	1272:1280	These findings suggest that the glycosylation on ephrin-A1 plays a critical role in the binding and activation of the EphA2 receptor.
23661698	0	53	from	characterization	26:41	arg1	ligand					86:91	a preferred ligand	74:91	a preferred ligand for EphA2 receptor tyrosine kinase	74:126	Biological and structural characterization of glycosylation on ephrin-A1, a preferred ligand for EphA2 receptor tyrosine kinase.
23661698	0	53	from	characterization	26:41	arg1	ephrin-A1					63:71	ephrin-A1	63:71	ephrin-A1	63:71	Biological and structural characterization of glycosylation on ephrin-A1, a preferred ligand for EphA2 receptor tyrosine kinase.
23661698	3	54	from	significance	417:428	arg1	biology					458:464	the biology	454:464	the biology of EphA2 and ephrin-A1	454:487	Here we report for the first time the significance of the glycosylation in the biology of EphA2 and ephrin-A1.
23661698	1	55	theme	tyrosine	148:155	arg1	kinase					157:162	The EphA2 receptor tyrosine kinase	129:162	The EphA2 receptor tyrosine kinase	129:162	The EphA2 receptor tyrosine kinase is overexpressed in a number of malignancies and is activated by ephrin ligands, most commonly by ephrin-A1.
23661698	4	56	theme	GBM	603:605	arg1	cells					608:612	glioblastoma (GBM) cells	589:612	glioblastoma (GBM) cells	589:612	Ephrin-A1 was enzymatically deglycosylated, and its activity was evaluated in several assays using glioblastoma (GBM) cells and recombinant EphA2.
22967898	5	0	from	secretion	648:656	arg1	cells					682:686	HT1080 cells	675:686	HT1080 cells	675:686	N-glycosylation of cathepsin V was important for transportation to lysosome, secretion, and activity in HT1080 cells.
22967898	4	1	theme	cathepsin	456:464	arg1	V					466:466	cathepsin V	456:466	cathepsin V	456:466	We demonstrated that cathepsin V is N-glycosylated at both Asn(221) and Asn(292) using mass spectrometry and site-directed mutagenesis.
22967898	5	2	theme	cathepsin	590:598	arg1	V					600:600	cathepsin V	590:600	cathepsin V	590:600	N-glycosylation of cathepsin V was important for transportation to lysosome, secretion, and activity in HT1080 cells.
22967898	6	3	theme	V	741:741	arg1	functions					718:726	functions	718:726	functions of cathepsin V	718:741	These data demonstrated that functions of cathepsin V are controlled by N-glycosylation.
22967898	2	4	contain	contains	226:233	arg1	V					224:224	Cathepsin V	214:224	Cathepsin V	214:224	Cathepsin V contains two predicted N-glycosylation sites, but it has not been reported whether cathepsin V is glycosylated or not.
22967898	2	4	contain	contains	226:233	arg2	sites					265:269	two predicted N-glycosylation sites	235:269	two predicted N-glycosylation sites	235:269	Cathepsin V contains two predicted N-glycosylation sites, but it has not been reported whether cathepsin V is glycosylated or not.
22967898	5	5	theme	V	600:600	arg1	N-glycosylation					571:585	N-glycosylation	571:585	N-glycosylation of cathepsin V	571:600	N-glycosylation of cathepsin V was important for transportation to lysosome, secretion, and activity in HT1080 cells.
22967898	6	6	theme	cathepsin	731:739	arg1	V					741:741	cathepsin V	731:741	cathepsin V	731:741	These data demonstrated that functions of cathepsin V are controlled by N-glycosylation.
22967898	5	7	from	lysosome	638:645	arg1	cells					682:686	HT1080 cells	675:686	HT1080 cells	675:686	N-glycosylation of cathepsin V was important for transportation to lysosome, secretion, and activity in HT1080 cells.
22967898	4	8	from	Asn	507:509	arg1	N-glycosylated					471:484	N-glycosylated	471:484	N-glycosylated	471:484	We demonstrated that cathepsin V is N-glycosylated at both Asn(221) and Asn(292) using mass spectrometry and site-directed mutagenesis.
22967898	2	9	theme	N-glycosylation	249:263	arg1	sites					265:269	two predicted N-glycosylation sites	235:269	two predicted N-glycosylation sites	235:269	Cathepsin V contains two predicted N-glycosylation sites, but it has not been reported whether cathepsin V is glycosylated or not.
22967898	2	10	gly	N-glycosylation	249:263	arg2	two					235:237	two	235:237	two	235:237	Cathepsin V contains two predicted N-glycosylation sites, but it has not been reported whether cathepsin V is glycosylated or not.
22967898	2	10	gly	N-glycosylation	249:263	arg2	sites					265:269	two predicted N-glycosylation sites	235:269	two predicted N-glycosylation sites	235:269	Cathepsin V contains two predicted N-glycosylation sites, but it has not been reported whether cathepsin V is glycosylated or not.
22967898	4	11	theme	site-directed	544:556	arg1	mutagenesis					558:568	site-directed mutagenesis	544:568	site-directed mutagenesis	544:568	We demonstrated that cathepsin V is N-glycosylated at both Asn(221) and Asn(292) using mass spectrometry and site-directed mutagenesis.
22967898	1	12	theme	Cathepsin	88:96	arg1	member					142:147	a member	140:147	a member	140:147	Cathepsin V (L2), a lysosomal cysteine protease, is a member of cathepsin family, relating to cancer invasion and metastasis.
22967898	1	12	theme	Cathepsin	88:96	arg1	L2					101:102	L2	101:102	L2	101:102	Cathepsin V (L2), a lysosomal cysteine protease, is a member of cathepsin family, relating to cancer invasion and metastasis.
22967898	1	12	theme	Cathepsin	88:96	arg1	protease					127:134	a lysosomal cysteine protease	106:134	a lysosomal cysteine protease	106:134	Cathepsin V (L2), a lysosomal cysteine protease, is a member of cathepsin family, relating to cancer invasion and metastasis.
22967898	1	12	theme	Cathepsin	88:96	arg1	V					98:98	Cathepsin V	88:98	Cathepsin V (L2)	88:103	Cathepsin V (L2), a lysosomal cysteine protease, is a member of cathepsin family, relating to cancer invasion and metastasis.
22967898	3	13	theme	N-glycosylation	385:399	arg1	role					377:380	the role	373:380	the role of N-glycosylation of cathepsin V for its functions	373:432	In this study, we clarified the role of N-glycosylation of cathepsin V for its functions.
22967898	1	14	theme	cathepsin	152:160	arg1	family					162:167	cathepsin family	152:167	cathepsin family	152:167	Cathepsin V (L2), a lysosomal cysteine protease, is a member of cathepsin family, relating to cancer invasion and metastasis.
22967898	1	15	theme	family	162:167	arg1	member					142:147	a member	140:147	a member	140:147	Cathepsin V (L2), a lysosomal cysteine protease, is a member of cathepsin family, relating to cancer invasion and metastasis.
22967898	1	15	theme	family	162:167	arg1	V					98:98	Cathepsin V	88:98	Cathepsin V (L2)	88:103	Cathepsin V (L2), a lysosomal cysteine protease, is a member of cathepsin family, relating to cancer invasion and metastasis.
22967898	0	16	theme	V	27:27	arg1	activity					29:36	cathepsin V activity	17:36	cathepsin V activity	17:36	Determination of cathepsin V activity and intracellular trafficking by N-glycosylation.
22967898	2	17	gly	glycosylated	324:335	arg1	V					319:319	cathepsin V	309:319	cathepsin V	309:319	Cathepsin V contains two predicted N-glycosylation sites, but it has not been reported whether cathepsin V is glycosylated or not.
22967898	3	18	theme	V	414:414	arg1	N-glycosylation					385:399	N-glycosylation	385:399	N-glycosylation of cathepsin V	385:414	In this study, we clarified the role of N-glycosylation of cathepsin V for its functions.
22967898	0	19	theme	cathepsin	17:25	arg1	activity					29:36	cathepsin V activity	17:36	cathepsin V activity	17:36	Determination of cathepsin V activity and intracellular trafficking by N-glycosylation.
22967898	5	20	from	activity	663:670	arg1	cells					682:686	HT1080 cells	675:686	HT1080 cells	675:686	N-glycosylation of cathepsin V was important for transportation to lysosome, secretion, and activity in HT1080 cells.
22967898	0	21	theme	activity	29:36	arg1	Determination					0:12	Determination	0:12	Determination of cathepsin V activity and intracellular trafficking by N-glycosylation	0:85	Determination of cathepsin V activity and intracellular trafficking by N-glycosylation.
22967898	3	22	theme	cathepsin	404:412	arg1	V					414:414	cathepsin V	404:414	cathepsin V	404:414	In this study, we clarified the role of N-glycosylation of cathepsin V for its functions.
22967898	0	23	theme	trafficking	56:66	arg1	Determination					0:12	Determination	0:12	Determination of cathepsin V activity and intracellular trafficking by N-glycosylation	0:85	Determination of cathepsin V activity and intracellular trafficking by N-glycosylation.
22967898	2	24	theme	cathepsin	309:317	arg1	V					319:319	cathepsin V	309:319	cathepsin V	309:319	Cathepsin V contains two predicted N-glycosylation sites, but it has not been reported whether cathepsin V is glycosylated or not.
22967898	0	25	theme	intracellular	42:54	arg1	trafficking					56:66	intracellular trafficking	42:66	intracellular trafficking	42:66	Determination of cathepsin V activity and intracellular trafficking by N-glycosylation.
22967898	3	26	gly	N-glycosylation	385:399	arg1	V					414:414	cathepsin V	404:414	cathepsin V	404:414	In this study, we clarified the role of N-glycosylation of cathepsin V for its functions.
22967898	1	27	theme	lysosomal	108:116	arg1	V					98:98	Cathepsin V	88:98	Cathepsin V (L2)	88:103	Cathepsin V (L2), a lysosomal cysteine protease, is a member of cathepsin family, relating to cancer invasion and metastasis.
22967898	1	27	theme	lysosomal	108:116	arg1	protease					127:134	a lysosomal cysteine protease	106:134	a lysosomal cysteine protease	106:134	Cathepsin V (L2), a lysosomal cysteine protease, is a member of cathepsin family, relating to cancer invasion and metastasis.
22967898	2	28	theme	predicted	239:247	arg1	sites					265:269	two predicted N-glycosylation sites	235:269	two predicted N-glycosylation sites	235:269	Cathepsin V contains two predicted N-glycosylation sites, but it has not been reported whether cathepsin V is glycosylated or not.
22967898	4	29	from	Asn	494:496	arg1	N-glycosylated					471:484	N-glycosylated	471:484	N-glycosylated	471:484	We demonstrated that cathepsin V is N-glycosylated at both Asn(221) and Asn(292) using mass spectrometry and site-directed mutagenesis.
22967898	1	30	theme	cysteine	118:125	arg1	V					98:98	Cathepsin V	88:98	Cathepsin V (L2)	88:103	Cathepsin V (L2), a lysosomal cysteine protease, is a member of cathepsin family, relating to cancer invasion and metastasis.
22967898	1	30	theme	cysteine	118:125	arg1	protease					127:134	a lysosomal cysteine protease	106:134	a lysosomal cysteine protease	106:134	Cathepsin V (L2), a lysosomal cysteine protease, is a member of cathepsin family, relating to cancer invasion and metastasis.
22967898	5	31	theme	HT1080	675:680	arg1	cells					682:686	HT1080 cells	675:686	HT1080 cells	675:686	N-glycosylation of cathepsin V was important for transportation to lysosome, secretion, and activity in HT1080 cells.
22967898	1	32	theme	cancer	182:187	arg1	invasion					189:196	cancer invasion	182:196	cancer invasion	182:196	Cathepsin V (L2), a lysosomal cysteine protease, is a member of cathepsin family, relating to cancer invasion and metastasis.
22967898	4	33	gly	N-glycosylated	471:484	arg2	221					498:500	221	498:500	221	498:500	We demonstrated that cathepsin V is N-glycosylated at both Asn(221) and Asn(292) using mass spectrometry and site-directed mutagenesis.
22967898	4	33	gly	N-glycosylated	471:484	arg2	292					511:513	292	511:513	292	511:513	We demonstrated that cathepsin V is N-glycosylated at both Asn(221) and Asn(292) using mass spectrometry and site-directed mutagenesis.
22967898	4	33	gly	N-glycosylated	471:484	arg2	Asn					494:496	Asn	494:496	Asn(221)	494:501	We demonstrated that cathepsin V is N-glycosylated at both Asn(221) and Asn(292) using mass spectrometry and site-directed mutagenesis.
22967898	4	33	gly	N-glycosylated	471:484	arg2	Asn					507:509	Asn	507:509	Asn(292)	507:514	We demonstrated that cathepsin V is N-glycosylated at both Asn(221) and Asn(292) using mass spectrometry and site-directed mutagenesis.
22967898	4	33	gly	N-glycosylated	471:484	arg1	V					466:466	cathepsin V	456:466	cathepsin V	456:466	We demonstrated that cathepsin V is N-glycosylated at both Asn(221) and Asn(292) using mass spectrometry and site-directed mutagenesis.
22967898	5	34	gly	N-glycosylation	571:585	arg1	V					600:600	cathepsin V	590:600	cathepsin V	590:600	N-glycosylation of cathepsin V was important for transportation to lysosome, secretion, and activity in HT1080 cells.
22967898	2	35	theme	Cathepsin	214:222	arg1	V					224:224	Cathepsin V	214:224	Cathepsin V	214:224	Cathepsin V contains two predicted N-glycosylation sites, but it has not been reported whether cathepsin V is glycosylated or not.
22967898	4	36	theme	mass	522:525	arg1	spectrometry					527:538	mass spectrometry	522:538	mass spectrometry	522:538	We demonstrated that cathepsin V is N-glycosylated at both Asn(221) and Asn(292) using mass spectrometry and site-directed mutagenesis.
23982206	0	0	theme	O-GlcNAc	73:80	arg1	glycosylation					82:94	O-GlcNAc glycosylation	73:94	O-GlcNAc glycosylation	73:94	Activation of the transcriptional function of the NF-κB protein c-Rel by O-GlcNAc glycosylation.
23982206	7	1	theme	T	1479:1479	arg1	cytokines					1493:1501	T helper cell cytokines	1479:1501	T helper cell cytokines	1479:1501	Our findings suggest a stimulus-specific role for hyperglycemia-induced O-GlcNAcylation of c-Rel in promoting T cell-mediated autoimmunity in conditions such as type 1 diabetes by enhancing the production of T helper cell cytokines.
23982206	5	2	from	expression	841:850	arg1	response					906:913	response	906:913	response to T cell receptor (TCR) activation	906:949	Blocking the O-GlcNAcylation of this residue abrogated c-Rel-mediated expression of the cytokine-encoding genes IL2, IFNG, and CSF2 in response to T cell receptor (TCR) activation, whereas increasing the extent of O-GlcNAcylation of cellular proteins enhanced the expression of these genes.
23982206	7	3	theme	helper	1481:1486	arg1	cytokines					1493:1501	T helper cell cytokines	1479:1501	T helper cell cytokines	1479:1501	Our findings suggest a stimulus-specific role for hyperglycemia-induced O-GlcNAcylation of c-Rel in promoting T cell-mediated autoimmunity in conditions such as type 1 diabetes by enhancing the production of T helper cell cytokines.
23982206	5	4	theme	T	918:918	arg1	receptor					925:932	T cell receptor	918:932	T cell receptor (TCR) activation	918:949	Blocking the O-GlcNAcylation of this residue abrogated c-Rel-mediated expression of the cytokine-encoding genes IL2, IFNG, and CSF2 in response to T cell receptor (TCR) activation, whereas increasing the extent of O-GlcNAcylation of cellular proteins enhanced the expression of these genes.
23982206	5	4	theme	T	918:918	arg1	TCR					935:937	TCR	935:937	TCR	935:937	Blocking the O-GlcNAcylation of this residue abrogated c-Rel-mediated expression of the cytokine-encoding genes IL2, IFNG, and CSF2 in response to T cell receptor (TCR) activation, whereas increasing the extent of O-GlcNAcylation of cellular proteins enhanced the expression of these genes.
23982206	5	5	theme	residue	808:814	arg1	O-GlcNAcylation					784:798	the O-GlcNAcylation	780:798	the O-GlcNAcylation of this residue	780:814	Blocking the O-GlcNAcylation of this residue abrogated c-Rel-mediated expression of the cytokine-encoding genes IL2, IFNG, and CSF2 in response to T cell receptor (TCR) activation, whereas increasing the extent of O-GlcNAcylation of cellular proteins enhanced the expression of these genes.
23982206	3	6	theme	subunit	575:581	arg1	c-Rel					583:587	the NF-κB subunit c-Rel	565:587	the NF-κB subunit c-Rel	565:587	We report that the NF-κB subunit c-Rel is modified and activated by O-GlcNAcylation.
23982206	7	7	theme	type	1432:1435	arg1	diabetes					1439:1446	type 1 diabetes	1432:1446	type 1 diabetes	1432:1446	Our findings suggest a stimulus-specific role for hyperglycemia-induced O-GlcNAcylation of c-Rel in promoting T cell-mediated autoimmunity in conditions such as type 1 diabetes by enhancing the production of T helper cell cytokines.
23982206	1	8	theme	several	248:254	arg1	methylation					316:326	methylation	316:326	methylation	316:326	The transcription factor nuclear factor κB (NF-κB) rapidly reprograms gene expression in response to various stimuli, and its activity is regulated by several posttranslational modifications, including phosphorylation, methylation, and acetylation.
23982206	1	8	theme	several	248:254	arg1	modifications					274:286	several posttranslational modifications	248:286	several posttranslational modifications	248:286	The transcription factor nuclear factor κB (NF-κB) rapidly reprograms gene expression in response to various stimuli, and its activity is regulated by several posttranslational modifications, including phosphorylation, methylation, and acetylation.
23982206	1	8	theme	several	248:254	arg1	phosphorylation					299:313	phosphorylation	299:313	phosphorylation	299:313	The transcription factor nuclear factor κB (NF-κB) rapidly reprograms gene expression in response to various stimuli, and its activity is regulated by several posttranslational modifications, including phosphorylation, methylation, and acetylation.
23982206	1	8	theme	several	248:254	arg1	acetylation					333:343	acetylation	333:343	acetylation	333:343	The transcription factor nuclear factor κB (NF-κB) rapidly reprograms gene expression in response to various stimuli, and its activity is regulated by several posttranslational modifications, including phosphorylation, methylation, and acetylation.
23982206	2	9	theme	cellular	533:540	arg1	stress					542:547	cellular stress	533:547	cellular stress	533:547	The addition of O-linked β-N-acetylglucosamine (a process known as O-GlcNAcylation) is an abundant posttranslational modification that is enhanced in conditions such as hyperglycemia and cellular stress.
23982206	4	10	theme	DNA	719:721	arg1	binding					723:729	DNA binding	719:729	DNA binding	719:729	We identified serine 350 as the site of O-GlcNAcylation, which was required for the DNA binding and transactivation functions of c-Rel.
23982206	2	11	dep	β-N-acetylglucosamine	371:391	arg1	process					396:402	a process	394:402	a process known as O-GlcNAcylation	394:427	The addition of O-linked β-N-acetylglucosamine (a process known as O-GlcNAcylation) is an abundant posttranslational modification that is enhanced in conditions such as hyperglycemia and cellular stress.
23982206	7	12	from	autoimmunity	1397:1408	arg1	diabetes					1439:1446	type 1 diabetes	1432:1446	type 1 diabetes	1432:1446	Our findings suggest a stimulus-specific role for hyperglycemia-induced O-GlcNAcylation of c-Rel in promoting T cell-mediated autoimmunity in conditions such as type 1 diabetes by enhancing the production of T helper cell cytokines.
23982206	7	12	from	autoimmunity	1397:1408	arg1	conditions					1413:1422	conditions	1413:1422	conditions such as type 1 diabetes	1413:1446	Our findings suggest a stimulus-specific role for hyperglycemia-induced O-GlcNAcylation of c-Rel in promoting T cell-mediated autoimmunity in conditions such as type 1 diabetes by enhancing the production of T helper cell cytokines.
23982206	1	13	theme	gene	167:170	arg1	expression					172:181	gene expression	167:181	gene expression	167:181	The transcription factor nuclear factor κB (NF-κB) rapidly reprograms gene expression in response to various stimuli, and its activity is regulated by several posttranslational modifications, including phosphorylation, methylation, and acetylation.
23982206	5	14	theme	c-Rel-mediated	826:839	arg1	expression					841:850	c-Rel-mediated expression	826:850	c-Rel-mediated expression of the cytokine-encoding genes IL2, IFNG, and CSF2 in response to T cell receptor (TCR) activation	826:949	Blocking the O-GlcNAcylation of this residue abrogated c-Rel-mediated expression of the cytokine-encoding genes IL2, IFNG, and CSF2 in response to T cell receptor (TCR) activation, whereas increasing the extent of O-GlcNAcylation of cellular proteins enhanced the expression of these genes.
23982206	2	15	link	O-linked	362:369	arg1	β-N-acetylglucosamine					371:391	O-linked β-N-acetylglucosamine	362:391	O-linked β-N-acetylglucosamine (a process known as O-GlcNAcylation)	362:428	The addition of O-linked β-N-acetylglucosamine (a process known as O-GlcNAcylation) is an abundant posttranslational modification that is enhanced in conditions such as hyperglycemia and cellular stress.
23982206	6	16	theme	tumor	1070:1074	arg1	TNF					1093:1095	TNF	1093:1095	TNF	1093:1095	TCR- or tumor necrosis factor (TNF)-induced expression of other NF-κB target genes, such as NFKBIA (which encodes IκBα) and TNFAIP3 (which encodes A20), occurred independently of the O-GlcNAcylation of c-Rel.
23982206	6	16	theme	tumor	1070:1074	arg1	factor					1085:1090	tumor necrosis factor	1070:1090	tumor necrosis factor (TNF)	1070:1096	TCR- or tumor necrosis factor (TNF)-induced expression of other NF-κB target genes, such as NFKBIA (which encodes IκBα) and TNFAIP3 (which encodes A20), occurred independently of the O-GlcNAcylation of c-Rel.
23982206	2	17	theme	posttranslational	445:461	arg1	modification					463:474	an abundant posttranslational modification	433:474	an abundant posttranslational modification that is enhanced in conditions such as hyperglycemia and cellular stress	433:547	The addition of O-linked β-N-acetylglucosamine (a process known as O-GlcNAcylation) is an abundant posttranslational modification that is enhanced in conditions such as hyperglycemia and cellular stress.
23982206	2	17	theme	posttranslational	445:461	arg1	addition					350:357	The addition	346:357	The addition of O-linked β-N-acetylglucosamine (a process known as O-GlcNAcylation)	346:428	The addition of O-linked β-N-acetylglucosamine (a process known as O-GlcNAcylation) is an abundant posttranslational modification that is enhanced in conditions such as hyperglycemia and cellular stress.
23982206	1	18	theme	posttranslational	256:272	arg1	methylation					316:326	methylation	316:326	methylation	316:326	The transcription factor nuclear factor κB (NF-κB) rapidly reprograms gene expression in response to various stimuli, and its activity is regulated by several posttranslational modifications, including phosphorylation, methylation, and acetylation.
23982206	1	18	theme	posttranslational	256:272	arg1	modifications					274:286	several posttranslational modifications	248:286	several posttranslational modifications	248:286	The transcription factor nuclear factor κB (NF-κB) rapidly reprograms gene expression in response to various stimuli, and its activity is regulated by several posttranslational modifications, including phosphorylation, methylation, and acetylation.
23982206	1	18	theme	posttranslational	256:272	arg1	phosphorylation					299:313	phosphorylation	299:313	phosphorylation	299:313	The transcription factor nuclear factor κB (NF-κB) rapidly reprograms gene expression in response to various stimuli, and its activity is regulated by several posttranslational modifications, including phosphorylation, methylation, and acetylation.
23982206	1	18	theme	posttranslational	256:272	arg1	acetylation					333:343	acetylation	333:343	acetylation	333:343	The transcription factor nuclear factor κB (NF-κB) rapidly reprograms gene expression in response to various stimuli, and its activity is regulated by several posttranslational modifications, including phosphorylation, methylation, and acetylation.
23982206	4	19	theme	transactivation	735:749	arg1	functions					751:759	transactivation functions	735:759	transactivation functions	735:759	We identified serine 350 as the site of O-GlcNAcylation, which was required for the DNA binding and transactivation functions of c-Rel.
23982206	4	20	theme	O-GlcNAcylation	675:689	arg1	serine					649:654	serine 350	649:658	serine 350	649:658	We identified serine 350 as the site of O-GlcNAcylation, which was required for the DNA binding and transactivation functions of c-Rel.
23982206	4	20	theme	O-GlcNAcylation	675:689	arg1	O-GlcNAcylation					675:689	O-GlcNAcylation	675:689	O-GlcNAcylation	675:689	We identified serine 350 as the site of O-GlcNAcylation, which was required for the DNA binding and transactivation functions of c-Rel.
23982206	4	20	theme	O-GlcNAcylation	675:689	arg1	site					667:670	the site	663:670	the site	663:670	We identified serine 350 as the site of O-GlcNAcylation, which was required for the DNA binding and transactivation functions of c-Rel.
23982206	2	21	theme	abundant	436:443	arg1	modification					463:474	an abundant posttranslational modification	433:474	an abundant posttranslational modification that is enhanced in conditions such as hyperglycemia and cellular stress	433:547	The addition of O-linked β-N-acetylglucosamine (a process known as O-GlcNAcylation) is an abundant posttranslational modification that is enhanced in conditions such as hyperglycemia and cellular stress.
23982206	2	21	theme	abundant	436:443	arg1	addition					350:357	The addition	346:357	The addition of O-linked β-N-acetylglucosamine (a process known as O-GlcNAcylation)	346:428	The addition of O-linked β-N-acetylglucosamine (a process known as O-GlcNAcylation) is an abundant posttranslational modification that is enhanced in conditions such as hyperglycemia and cellular stress.
23982206	7	22	theme	c-Rel	1362:1366	arg1	O-GlcNAcylation					1343:1357	hyperglycemia-induced O-GlcNAcylation	1321:1357	hyperglycemia-induced O-GlcNAcylation of c-Rel	1321:1366	Our findings suggest a stimulus-specific role for hyperglycemia-induced O-GlcNAcylation of c-Rel in promoting T cell-mediated autoimmunity in conditions such as type 1 diabetes by enhancing the production of T helper cell cytokines.
23982206	3	23	theme	NF-κB	569:573	arg1	c-Rel					583:587	the NF-κB subunit c-Rel	565:587	the NF-κB subunit c-Rel	565:587	We report that the NF-κB subunit c-Rel is modified and activated by O-GlcNAcylation.
23982206	5	24	theme	cytokine-encoding	859:875	arg1	IL2					883:885	IL2	883:885	IL2	883:885	Blocking the O-GlcNAcylation of this residue abrogated c-Rel-mediated expression of the cytokine-encoding genes IL2, IFNG, and CSF2 in response to T cell receptor (TCR) activation, whereas increasing the extent of O-GlcNAcylation of cellular proteins enhanced the expression of these genes.
23982206	5	24	theme	cytokine-encoding	859:875	arg1	genes					877:881	the cytokine-encoding genes IL2, IFNG, and CSF2	855:901	the cytokine-encoding genes IL2, IFNG, and CSF2	855:901	Blocking the O-GlcNAcylation of this residue abrogated c-Rel-mediated expression of the cytokine-encoding genes IL2, IFNG, and CSF2 in response to T cell receptor (TCR) activation, whereas increasing the extent of O-GlcNAcylation of cellular proteins enhanced the expression of these genes.
23982206	5	24	theme	cytokine-encoding	859:875	arg1	IFNG					888:891	IFNG	888:891	IFNG	888:891	Blocking the O-GlcNAcylation of this residue abrogated c-Rel-mediated expression of the cytokine-encoding genes IL2, IFNG, and CSF2 in response to T cell receptor (TCR) activation, whereas increasing the extent of O-GlcNAcylation of cellular proteins enhanced the expression of these genes.
23982206	5	24	theme	cytokine-encoding	859:875	arg1	CSF2					898:901	CSF2	898:901	CSF2	898:901	Blocking the O-GlcNAcylation of this residue abrogated c-Rel-mediated expression of the cytokine-encoding genes IL2, IFNG, and CSF2 in response to T cell receptor (TCR) activation, whereas increasing the extent of O-GlcNAcylation of cellular proteins enhanced the expression of these genes.
23982206	4	25	dep	binding	723:729	arg1	the					715:717	the	715:717	the	715:717	We identified serine 350 as the site of O-GlcNAcylation, which was required for the DNA binding and transactivation functions of c-Rel.
23982206	1	26	theme	transcription	101:113	arg1	factor					130:135	The transcription factor nuclear factor κB	97:138	The transcription factor nuclear factor κB (NF-κB)	97:146	The transcription factor nuclear factor κB (NF-κB) rapidly reprograms gene expression in response to various stimuli, and its activity is regulated by several posttranslational modifications, including phosphorylation, methylation, and acetylation.
23982206	1	26	theme	transcription	101:113	arg1	NF-κB					141:145	NF-κB	141:145	NF-κB	141:145	The transcription factor nuclear factor κB (NF-κB) rapidly reprograms gene expression in response to various stimuli, and its activity is regulated by several posttranslational modifications, including phosphorylation, methylation, and acetylation.
23982206	5	27	theme	genes	877:881	arg1	expression					841:850	c-Rel-mediated expression	826:850	c-Rel-mediated expression of the cytokine-encoding genes IL2, IFNG, and CSF2 in response to T cell receptor (TCR) activation	826:949	Blocking the O-GlcNAcylation of this residue abrogated c-Rel-mediated expression of the cytokine-encoding genes IL2, IFNG, and CSF2 in response to T cell receptor (TCR) activation, whereas increasing the extent of O-GlcNAcylation of cellular proteins enhanced the expression of these genes.
23982206	5	28	theme	receptor	925:932	arg1	activation					940:949	T cell receptor (TCR) activation	918:949	T cell receptor (TCR) activation	918:949	Blocking the O-GlcNAcylation of this residue abrogated c-Rel-mediated expression of the cytokine-encoding genes IL2, IFNG, and CSF2 in response to T cell receptor (TCR) activation, whereas increasing the extent of O-GlcNAcylation of cellular proteins enhanced the expression of these genes.
23982206	6	29	theme	other	1120:1124	arg1	NFKBIA					1154:1159	NFKBIA	1154:1159	NFKBIA (which encodes IκBα)	1154:1180	TCR- or tumor necrosis factor (TNF)-induced expression of other NF-κB target genes, such as NFKBIA (which encodes IκBα) and TNFAIP3 (which encodes A20), occurred independently of the O-GlcNAcylation of c-Rel.
23982206	6	29	theme	other	1120:1124	arg1	genes					1139:1143	other NF-κB target genes	1120:1143	other NF-κB target genes	1120:1143	TCR- or tumor necrosis factor (TNF)-induced expression of other NF-κB target genes, such as NFKBIA (which encodes IκBα) and TNFAIP3 (which encodes A20), occurred independently of the O-GlcNAcylation of c-Rel.
23982206	6	29	theme	other	1120:1124	arg1	TNFAIP3					1186:1192	TNFAIP3	1186:1192	TNFAIP3 (which encodes A20)	1186:1212	TCR- or tumor necrosis factor (TNF)-induced expression of other NF-κB target genes, such as NFKBIA (which encodes IκBα) and TNFAIP3 (which encodes A20), occurred independently of the O-GlcNAcylation of c-Rel.
23982206	1	30	theme	various	198:204	arg1	stimuli					206:212	various stimuli	198:212	various stimuli	198:212	The transcription factor nuclear factor κB (NF-κB) rapidly reprograms gene expression in response to various stimuli, and its activity is regulated by several posttranslational modifications, including phosphorylation, methylation, and acetylation.
23982206	0	31	theme	function	34:41	arg1	Activation					0:9	Activation	0:9	Activation of the transcriptional function of the NF-κB protein c-Rel by O-GlcNAc glycosylation.	0:95	Activation of the transcriptional function of the NF-κB protein c-Rel by O-GlcNAc glycosylation.
23982206	0	32	theme	transcriptional	18:32	arg1	function					34:41	the transcriptional function	14:41	the transcriptional function of the NF-κB protein c-Rel	14:68	Activation of the transcriptional function of the NF-κB protein c-Rel by O-GlcNAc glycosylation.
23982206	0	33	theme	NF-κB	50:54	arg1	c-Rel					64:68	the NF-κB protein c-Rel	46:68	the NF-κB protein c-Rel	46:68	Activation of the transcriptional function of the NF-κB protein c-Rel by O-GlcNAc glycosylation.
23982206	7	34	theme	hyperglycemia-induced	1321:1341	arg1	O-GlcNAcylation					1343:1357	hyperglycemia-induced O-GlcNAcylation	1321:1357	hyperglycemia-induced O-GlcNAcylation of c-Rel	1321:1366	Our findings suggest a stimulus-specific role for hyperglycemia-induced O-GlcNAcylation of c-Rel in promoting T cell-mediated autoimmunity in conditions such as type 1 diabetes by enhancing the production of T helper cell cytokines.
23982206	6	35	theme	-induced	1097:1104	arg1	expression					1106:1115	TCR- or tumor necrosis factor (TNF)-induced expression	1062:1115	TCR- or tumor necrosis factor (TNF)-induced expression of other NF-κB target genes, such as NFKBIA (which encodes IκBα) and TNFAIP3 (which encodes A20),	1062:1213	TCR- or tumor necrosis factor (TNF)-induced expression of other NF-κB target genes, such as NFKBIA (which encodes IκBα) and TNFAIP3 (which encodes A20), occurred independently of the O-GlcNAcylation of c-Rel.
23982206	1	36	theme	factor	115:120	arg1	factor					130:135	The transcription factor nuclear factor κB	97:138	The transcription factor nuclear factor κB (NF-κB)	97:146	The transcription factor nuclear factor κB (NF-κB) rapidly reprograms gene expression in response to various stimuli, and its activity is regulated by several posttranslational modifications, including phosphorylation, methylation, and acetylation.
23982206	1	36	theme	factor	115:120	arg1	NF-κB					141:145	NF-κB	141:145	NF-κB	141:145	The transcription factor nuclear factor κB (NF-κB) rapidly reprograms gene expression in response to various stimuli, and its activity is regulated by several posttranslational modifications, including phosphorylation, methylation, and acetylation.
23982206	7	37	theme	cytokines	1493:1501	arg1	production					1465:1474	the production	1461:1474	the production of T helper cell cytokines	1461:1501	Our findings suggest a stimulus-specific role for hyperglycemia-induced O-GlcNAcylation of c-Rel in promoting T cell-mediated autoimmunity in conditions such as type 1 diabetes by enhancing the production of T helper cell cytokines.
23982206	6	38	theme	genes	1139:1143	arg1	expression					1106:1115	TCR- or tumor necrosis factor (TNF)-induced expression	1062:1115	TCR- or tumor necrosis factor (TNF)-induced expression of other NF-κB target genes, such as NFKBIA (which encodes IκBα) and TNFAIP3 (which encodes A20),	1062:1213	TCR- or tumor necrosis factor (TNF)-induced expression of other NF-κB target genes, such as NFKBIA (which encodes IκBα) and TNFAIP3 (which encodes A20), occurred independently of the O-GlcNAcylation of c-Rel.
23982206	7	39	theme	stimulus-specific	1294:1310	arg1	role					1312:1315	a stimulus-specific role	1292:1315	a stimulus-specific role for hyperglycemia-induced O-GlcNAcylation of c-Rel in promoting T cell-mediated autoimmunity in conditions such as type 1 diabetes by enhancing the production of T helper cell cytokines	1292:1501	Our findings suggest a stimulus-specific role for hyperglycemia-induced O-GlcNAcylation of c-Rel in promoting T cell-mediated autoimmunity in conditions such as type 1 diabetes by enhancing the production of T helper cell cytokines.
23982206	1	40	theme	nuclear	122:128	arg1	factor					130:135	The transcription factor nuclear factor κB	97:138	The transcription factor nuclear factor κB (NF-κB)	97:146	The transcription factor nuclear factor κB (NF-κB) rapidly reprograms gene expression in response to various stimuli, and its activity is regulated by several posttranslational modifications, including phosphorylation, methylation, and acetylation.
23982206	1	40	theme	nuclear	122:128	arg1	NF-κB					141:145	NF-κB	141:145	NF-κB	141:145	The transcription factor nuclear factor κB (NF-κB) rapidly reprograms gene expression in response to various stimuli, and its activity is regulated by several posttranslational modifications, including phosphorylation, methylation, and acetylation.
23982206	5	41	dep	genes	877:881	arg1	IL2					883:885	IL2	883:885	IL2	883:885	Blocking the O-GlcNAcylation of this residue abrogated c-Rel-mediated expression of the cytokine-encoding genes IL2, IFNG, and CSF2 in response to T cell receptor (TCR) activation, whereas increasing the extent of O-GlcNAcylation of cellular proteins enhanced the expression of these genes.
23982206	5	41	dep	genes	877:881	arg1	genes					877:881	the cytokine-encoding genes IL2, IFNG, and CSF2	855:901	the cytokine-encoding genes IL2, IFNG, and CSF2	855:901	Blocking the O-GlcNAcylation of this residue abrogated c-Rel-mediated expression of the cytokine-encoding genes IL2, IFNG, and CSF2 in response to T cell receptor (TCR) activation, whereas increasing the extent of O-GlcNAcylation of cellular proteins enhanced the expression of these genes.
23982206	5	41	dep	genes	877:881	arg1	IFNG					888:891	IFNG	888:891	IFNG	888:891	Blocking the O-GlcNAcylation of this residue abrogated c-Rel-mediated expression of the cytokine-encoding genes IL2, IFNG, and CSF2 in response to T cell receptor (TCR) activation, whereas increasing the extent of O-GlcNAcylation of cellular proteins enhanced the expression of these genes.
23982206	5	41	dep	genes	877:881	arg1	CSF2					898:901	CSF2	898:901	CSF2	898:901	Blocking the O-GlcNAcylation of this residue abrogated c-Rel-mediated expression of the cytokine-encoding genes IL2, IFNG, and CSF2 in response to T cell receptor (TCR) activation, whereas increasing the extent of O-GlcNAcylation of cellular proteins enhanced the expression of these genes.
23982206	6	42	theme	c-Rel	1264:1268	arg1	O-GlcNAcylation					1245:1259	the O-GlcNAcylation	1241:1259	the O-GlcNAcylation of c-Rel	1241:1268	TCR- or tumor necrosis factor (TNF)-induced expression of other NF-κB target genes, such as NFKBIA (which encodes IκBα) and TNFAIP3 (which encodes A20), occurred independently of the O-GlcNAcylation of c-Rel.
23982206	5	43	theme	genes	1055:1059	arg1	expression					1035:1044	the expression	1031:1044	the expression of these genes	1031:1059	Blocking the O-GlcNAcylation of this residue abrogated c-Rel-mediated expression of the cytokine-encoding genes IL2, IFNG, and CSF2 in response to T cell receptor (TCR) activation, whereas increasing the extent of O-GlcNAcylation of cellular proteins enhanced the expression of these genes.
23982206	5	44	theme	O-GlcNAcylation	985:999	arg1	extent					975:980	the extent	971:980	increasing the extent of O-GlcNAcylation of cellular proteins	960:1020	Blocking the O-GlcNAcylation of this residue abrogated c-Rel-mediated expression of the cytokine-encoding genes IL2, IFNG, and CSF2 in response to T cell receptor (TCR) activation, whereas increasing the extent of O-GlcNAcylation of cellular proteins enhanced the expression of these genes.
23982206	4	45	theme	c-Rel	764:768	arg1	binding					723:729	DNA binding	719:729	DNA binding	719:729	We identified serine 350 as the site of O-GlcNAcylation, which was required for the DNA binding and transactivation functions of c-Rel.
23982206	4	45	theme	c-Rel	764:768	arg1	functions					751:759	transactivation functions	735:759	transactivation functions	735:759	We identified serine 350 as the site of O-GlcNAcylation, which was required for the DNA binding and transactivation functions of c-Rel.
23982206	7	46	theme	cell-mediated	1383:1395	arg1	autoimmunity					1397:1408	T cell-mediated autoimmunity	1381:1408	T cell-mediated autoimmunity in conditions such as type 1 diabetes	1381:1446	Our findings suggest a stimulus-specific role for hyperglycemia-induced O-GlcNAcylation of c-Rel in promoting T cell-mediated autoimmunity in conditions such as type 1 diabetes by enhancing the production of T helper cell cytokines.
23982206	5	47	theme	cell	920:923	arg1	receptor					925:932	T cell receptor	918:932	T cell receptor (TCR) activation	918:949	Blocking the O-GlcNAcylation of this residue abrogated c-Rel-mediated expression of the cytokine-encoding genes IL2, IFNG, and CSF2 in response to T cell receptor (TCR) activation, whereas increasing the extent of O-GlcNAcylation of cellular proteins enhanced the expression of these genes.
23982206	5	47	theme	cell	920:923	arg1	TCR					935:937	TCR	935:937	TCR	935:937	Blocking the O-GlcNAcylation of this residue abrogated c-Rel-mediated expression of the cytokine-encoding genes IL2, IFNG, and CSF2 in response to T cell receptor (TCR) activation, whereas increasing the extent of O-GlcNAcylation of cellular proteins enhanced the expression of these genes.
23982206	5	48	theme	increasing	960:969	arg1	extent					975:980	the extent	971:980	increasing the extent of O-GlcNAcylation of cellular proteins	960:1020	Blocking the O-GlcNAcylation of this residue abrogated c-Rel-mediated expression of the cytokine-encoding genes IL2, IFNG, and CSF2 in response to T cell receptor (TCR) activation, whereas increasing the extent of O-GlcNAcylation of cellular proteins enhanced the expression of these genes.
23982206	6	49	theme	NF-κB	1126:1130	arg1	NFKBIA					1154:1159	NFKBIA	1154:1159	NFKBIA (which encodes IκBα)	1154:1180	TCR- or tumor necrosis factor (TNF)-induced expression of other NF-κB target genes, such as NFKBIA (which encodes IκBα) and TNFAIP3 (which encodes A20), occurred independently of the O-GlcNAcylation of c-Rel.
23982206	6	49	theme	NF-κB	1126:1130	arg1	genes					1139:1143	other NF-κB target genes	1120:1143	other NF-κB target genes	1120:1143	TCR- or tumor necrosis factor (TNF)-induced expression of other NF-κB target genes, such as NFKBIA (which encodes IκBα) and TNFAIP3 (which encodes A20), occurred independently of the O-GlcNAcylation of c-Rel.
23982206	6	49	theme	NF-κB	1126:1130	arg1	TNFAIP3					1186:1192	TNFAIP3	1186:1192	TNFAIP3 (which encodes A20)	1186:1212	TCR- or tumor necrosis factor (TNF)-induced expression of other NF-κB target genes, such as NFKBIA (which encodes IκBα) and TNFAIP3 (which encodes A20), occurred independently of the O-GlcNAcylation of c-Rel.
23982206	0	50	theme	c-Rel	64:68	arg1	function					34:41	the transcriptional function	14:41	the transcriptional function of the NF-κB protein c-Rel	14:68	Activation of the transcriptional function of the NF-κB protein c-Rel by O-GlcNAc glycosylation.
23982206	7	51	theme	cell	1488:1491	arg1	cytokines					1493:1501	T helper cell cytokines	1479:1501	T helper cell cytokines	1479:1501	Our findings suggest a stimulus-specific role for hyperglycemia-induced O-GlcNAcylation of c-Rel in promoting T cell-mediated autoimmunity in conditions such as type 1 diabetes by enhancing the production of T helper cell cytokines.
23982206	5	52	theme	cellular	1004:1011	arg1	proteins					1013:1020	cellular proteins	1004:1020	cellular proteins	1004:1020	Blocking the O-GlcNAcylation of this residue abrogated c-Rel-mediated expression of the cytokine-encoding genes IL2, IFNG, and CSF2 in response to T cell receptor (TCR) activation, whereas increasing the extent of O-GlcNAcylation of cellular proteins enhanced the expression of these genes.
23982206	6	53	theme	TCR-	1062:1065	arg1	expression					1106:1115	TCR- or tumor necrosis factor (TNF)-induced expression	1062:1115	TCR- or tumor necrosis factor (TNF)-induced expression of other NF-κB target genes, such as NFKBIA (which encodes IκBα) and TNFAIP3 (which encodes A20),	1062:1213	TCR- or tumor necrosis factor (TNF)-induced expression of other NF-κB target genes, such as NFKBIA (which encodes IκBα) and TNFAIP3 (which encodes A20), occurred independently of the O-GlcNAcylation of c-Rel.
23982206	2	54	theme	β-N-acetylglucosamine	371:391	arg1	modification					463:474	an abundant posttranslational modification	433:474	an abundant posttranslational modification that is enhanced in conditions such as hyperglycemia and cellular stress	433:547	The addition of O-linked β-N-acetylglucosamine (a process known as O-GlcNAcylation) is an abundant posttranslational modification that is enhanced in conditions such as hyperglycemia and cellular stress.
23982206	2	54	theme	β-N-acetylglucosamine	371:391	arg1	addition					350:357	The addition	346:357	The addition of O-linked β-N-acetylglucosamine (a process known as O-GlcNAcylation)	346:428	The addition of O-linked β-N-acetylglucosamine (a process known as O-GlcNAcylation) is an abundant posttranslational modification that is enhanced in conditions such as hyperglycemia and cellular stress.
23982206	6	55	theme	necrosis	1076:1083	arg1	TNF					1093:1095	TNF	1093:1095	TNF	1093:1095	TCR- or tumor necrosis factor (TNF)-induced expression of other NF-κB target genes, such as NFKBIA (which encodes IκBα) and TNFAIP3 (which encodes A20), occurred independently of the O-GlcNAcylation of c-Rel.
23982206	6	55	theme	necrosis	1076:1083	arg1	factor					1085:1090	tumor necrosis factor	1070:1090	tumor necrosis factor (TNF)	1070:1096	TCR- or tumor necrosis factor (TNF)-induced expression of other NF-κB target genes, such as NFKBIA (which encodes IκBα) and TNFAIP3 (which encodes A20), occurred independently of the O-GlcNAcylation of c-Rel.
23982206	0	56	theme	protein	56:62	arg1	c-Rel					64:68	the NF-κB protein c-Rel	46:68	the NF-κB protein c-Rel	46:68	Activation of the transcriptional function of the NF-κB protein c-Rel by O-GlcNAc glycosylation.
23982206	6	57	theme	target	1132:1137	arg1	NFKBIA					1154:1159	NFKBIA	1154:1159	NFKBIA (which encodes IκBα)	1154:1180	TCR- or tumor necrosis factor (TNF)-induced expression of other NF-κB target genes, such as NFKBIA (which encodes IκBα) and TNFAIP3 (which encodes A20), occurred independently of the O-GlcNAcylation of c-Rel.
23982206	6	57	theme	target	1132:1137	arg1	genes					1139:1143	other NF-κB target genes	1120:1143	other NF-κB target genes	1120:1143	TCR- or tumor necrosis factor (TNF)-induced expression of other NF-κB target genes, such as NFKBIA (which encodes IκBα) and TNFAIP3 (which encodes A20), occurred independently of the O-GlcNAcylation of c-Rel.
23982206	6	57	theme	target	1132:1137	arg1	TNFAIP3					1186:1192	TNFAIP3	1186:1192	TNFAIP3 (which encodes A20)	1186:1212	TCR- or tumor necrosis factor (TNF)-induced expression of other NF-κB target genes, such as NFKBIA (which encodes IκBα) and TNFAIP3 (which encodes A20), occurred independently of the O-GlcNAcylation of c-Rel.
23982206	5	58	theme	proteins	1013:1020	arg1	O-GlcNAcylation					985:999	O-GlcNAcylation	985:999	O-GlcNAcylation of cellular proteins	985:1020	Blocking the O-GlcNAcylation of this residue abrogated c-Rel-mediated expression of the cytokine-encoding genes IL2, IFNG, and CSF2 in response to T cell receptor (TCR) activation, whereas increasing the extent of O-GlcNAcylation of cellular proteins enhanced the expression of these genes.
23982206	2	59	theme	O-linked	362:369	arg1	β-N-acetylglucosamine					371:391	O-linked β-N-acetylglucosamine	362:391	O-linked β-N-acetylglucosamine (a process known as O-GlcNAcylation)	362:428	The addition of O-linked β-N-acetylglucosamine (a process known as O-GlcNAcylation) is an abundant posttranslational modification that is enhanced in conditions such as hyperglycemia and cellular stress.
19951703	4	0	theme	N-glycosylation	402:416	arg1	sites					418:422	the potential N-glycosylation sites	388:422	the potential N-glycosylation sites at residues 71, 292, and 344	388:451	Mutation analysis at the potential N-glycosylation sites at residues 71, 292, and 344 (from asparagine to glutamine) revealed that all of them were glycosylated, but the extent of glycosylation and/or size of the glycan differed.
19951703	1	1	theme	xeno/endobiotics	146:161	arg1	xeno/endobiotics					146:161	xeno/endobiotics	146:161	xeno/endobiotics	146:161	UDP-glucuronosyltransferases (UGTs) catalyze the glucuronidation of a variety of xeno/endobiotics.
19951703	1	1	theme	xeno/endobiotics	146:161	arg1	variety					135:141	a variety	133:141	a variety of xeno/endobiotics	133:161	UDP-glucuronosyltransferases (UGTs) catalyze the glucuronidation of a variety of xeno/endobiotics.
19951703	8	2	theme	Endo	1118:1121	arg1	H					1123:1123	Endo H	1118:1123	Endo H under the non-denaturing condition	1118:1158	To the contrary, the deglycosylated UGT1A9, which was produced by the treatment with Endo H under the non-denaturing condition, showed the same enzyme kinetics as the control.
19951703	6	3	theme	unglycosylated	826:839	arg1	UGT1A9					841:846	unglycosylated UGT1A9	826:846	unglycosylated UGT1A9	826:846	To evaluate the role of glycosylation in the enzyme activity, we produced unglycosylated UGT1A9 by treating HEK293 cells transiently transfected with expression plasmid with tunicamycin.
19951703	10	4	theme	the	1359:1361	arg1	analysis					1347:1354	The thermal stability analysis	1325:1354	The thermal stability analysis of the mutated and deglycosylated UGT1A9 proteins	1325:1404	The thermal stability analysis of the mutated and deglycosylated UGT1A9 proteins supported the findings.
19951703	4	5	theme	Mutation	367:374	arg1	analysis					376:383	Mutation analysis	367:383	Mutation analysis at the potential N-glycosylation sites at residues 71, 292, and 344 (from asparagine to glutamine)	367:482	Mutation analysis at the potential N-glycosylation sites at residues 71, 292, and 344 (from asparagine to glutamine) revealed that all of them were glycosylated, but the extent of glycosylation and/or size of the glycan differed.
19951703	4	6	gly	N-glycosylation	402:416	arg2	residues					427:434	residues 71, 292, and 344	427:451	residues 71, 292, and 344	427:451	Mutation analysis at the potential N-glycosylation sites at residues 71, 292, and 344 (from asparagine to glutamine) revealed that all of them were glycosylated, but the extent of glycosylation and/or size of the glycan differed.
19951703	4	6	gly	N-glycosylation	402:416	arg2	sites					418:422	the potential N-glycosylation sites	388:422	the potential N-glycosylation sites at residues 71, 292, and 344	388:451	Mutation analysis at the potential N-glycosylation sites at residues 71, 292, and 344 (from asparagine to glutamine) revealed that all of them were glycosylated, but the extent of glycosylation and/or size of the glycan differed.
19951703	5	7	theme	enzyme	662:667	arg1	activities					669:678	decreased enzyme activities	652:678	decreased enzyme activities	652:678	In comparison with the wild-type, these mutants showed decreased enzyme activities in parallel with the extent of the band shift in Western blot analysis.
19951703	4	8	dep	glutamine	473:481	arg1	asparagine					459:468	asparagine	459:468	asparagine	459:468	Mutation analysis at the potential N-glycosylation sites at residues 71, 292, and 344 (from asparagine to glutamine) revealed that all of them were glycosylated, but the extent of glycosylation and/or size of the glycan differed.
19951703	6	9	gly	unglycosylated	826:839	arg1	UGT1A9					841:846	unglycosylated UGT1A9	826:846	unglycosylated UGT1A9	826:846	To evaluate the role of glycosylation in the enzyme activity, we produced unglycosylated UGT1A9 by treating HEK293 cells transiently transfected with expression plasmid with tunicamycin.
19951703	5	10	from	analysis	742:749	arg1	extent					701:706	the extent	697:706	the extent of the band shift in Western blot analysis	697:749	In comparison with the wild-type, these mutants showed decreased enzyme activities in parallel with the extent of the band shift in Western blot analysis.
19951703	4	11	gly	glycosylation	547:559	arg1	glycan					580:585	the glycan	576:585	the glycan	576:585	Mutation analysis at the potential N-glycosylation sites at residues 71, 292, and 344 (from asparagine to glutamine) revealed that all of them were glycosylated, but the extent of glycosylation and/or size of the glycan differed.
19951703	9	12	gly	glycosylation	1240:1252	arg1	UGT1A9					1317:1322	UGT1A9	1317:1322	UGT1A9	1317:1322	These results suggest that the glycosylation that occurs during translation is important for the folding of UGT1A9.
19951703	11	13	theme	important	1486:1494	arg1	role					1496:1499	an important role	1483:1499	an important role	1483:1499	In conclusion, we found that the N-glycosylation has an important role in the folding of UGT1A9.
19951703	10	14	theme	thermal	1329:1335	arg1	stability					1337:1345	The thermal stability	1325:1345	The thermal stability analysis of the mutated and deglycosylated UGT1A9 proteins	1325:1404	The thermal stability analysis of the mutated and deglycosylated UGT1A9 proteins supported the findings.
19951703	7	15	theme	stress	1025:1030	arg1	which					986:990	which	986:990	which	986:990	The unglycosylated UGT1A9 was almost inactive, which was not an indirect effect of ER stress.
19951703	7	15	theme	stress	1025:1030	arg1	effect					1012:1017	an indirect effect	1000:1017	an indirect effect of ER stress	1000:1030	The unglycosylated UGT1A9 was almost inactive, which was not an indirect effect of ER stress.
19951703	4	16	theme	size	568:571	arg1	extent					537:542	the extent	533:542	the extent of glycosylation and/or size of the glycan	533:585	Mutation analysis at the potential N-glycosylation sites at residues 71, 292, and 344 (from asparagine to glutamine) revealed that all of them were glycosylated, but the extent of glycosylation and/or size of the glycan differed.
19951703	6	17	with	plasmid	913:919	arg1	tunicamycin					926:936	tunicamycin	926:936	tunicamycin	926:936	To evaluate the role of glycosylation in the enzyme activity, we produced unglycosylated UGT1A9 by treating HEK293 cells transiently transfected with expression plasmid with tunicamycin.
19951703	3	18	theme	N-glycosylation	318:332	arg1	role					310:313	the role	306:313	the role of N-glycosylation in the function of human UGT1A9	306:364	In the present study, we investigated the role of N-glycosylation in the function of human UGT1A9.
19951703	10	19	theme	UGT1A9	1390:1395	arg1	proteins					1397:1404	deglycosylated UGT1A9 proteins	1375:1404	deglycosylated UGT1A9 proteins	1375:1404	The thermal stability analysis of the mutated and deglycosylated UGT1A9 proteins supported the findings.
19951703	4	20	gly	glycosylated	515:526	arg1	them					505:508	them	505:508	them	505:508	Mutation analysis at the potential N-glycosylation sites at residues 71, 292, and 344 (from asparagine to glutamine) revealed that all of them were glycosylated, but the extent of glycosylation and/or size of the glycan differed.
19951703	4	20	gly	glycosylated	515:526	arg1	all					498:500	all	498:500	all	498:500	Mutation analysis at the potential N-glycosylation sites at residues 71, 292, and 344 (from asparagine to glutamine) revealed that all of them were glycosylated, but the extent of glycosylation and/or size of the glycan differed.
19951703	2	21	theme	luminal	252:258	arg1	domain					260:265	a glycosylated luminal domain	237:265	a glycosylated luminal domain	237:265	UGTs are type I membrane proteins of the endoplasmic reticulum (ER) with a glycosylated luminal domain.
19951703	6	22	theme	HEK293	860:865	arg1	cells					867:871	HEK293 cells	860:871	HEK293 cells transiently transfected with expression plasmid with tunicamycin	860:936	To evaluate the role of glycosylation in the enzyme activity, we produced unglycosylated UGT1A9 by treating HEK293 cells transiently transfected with expression plasmid with tunicamycin.
19951703	3	23	theme	human	353:357	arg1	UGT1A9					359:364	human UGT1A9	353:364	human UGT1A9	353:364	In the present study, we investigated the role of N-glycosylation in the function of human UGT1A9.
19951703	6	24	theme	enzyme	797:802	arg1	activity					804:811	the enzyme activity	793:811	the enzyme activity	793:811	To evaluate the role of glycosylation in the enzyme activity, we produced unglycosylated UGT1A9 by treating HEK293 cells transiently transfected with expression plasmid with tunicamycin.
19951703	10	25	theme	deglycosylated	1375:1388	arg1	proteins					1397:1404	deglycosylated UGT1A9 proteins	1375:1404	deglycosylated UGT1A9 proteins	1375:1404	The thermal stability analysis of the mutated and deglycosylated UGT1A9 proteins supported the findings.
19951703	8	26	theme	deglycosylated	1054:1067	arg1	UGT1A9					1069:1074	the deglycosylated UGT1A9	1050:1074	the deglycosylated UGT1A9	1050:1074	To the contrary, the deglycosylated UGT1A9, which was produced by the treatment with Endo H under the non-denaturing condition, showed the same enzyme kinetics as the control.
19951703	4	27	from	residues	427:434	arg1	sites					418:422	the potential N-glycosylation sites	388:422	the potential N-glycosylation sites at residues 71, 292, and 344	388:451	Mutation analysis at the potential N-glycosylation sites at residues 71, 292, and 344 (from asparagine to glutamine) revealed that all of them were glycosylated, but the extent of glycosylation and/or size of the glycan differed.
19951703	3	28	theme	UGT1A9	359:364	arg1	function					341:348	the function	337:348	the function of human UGT1A9	337:364	In the present study, we investigated the role of N-glycosylation in the function of human UGT1A9.
19951703	3	29	from	role	310:313	arg1	function					341:348	the function	337:348	the function of human UGT1A9	337:364	In the present study, we investigated the role of N-glycosylation in the function of human UGT1A9.
19951703	2	30	gly	glycosylated	239:250	arg1	domain					260:265	a glycosylated luminal domain	237:265	a glycosylated luminal domain	237:265	UGTs are type I membrane proteins of the endoplasmic reticulum (ER) with a glycosylated luminal domain.
19951703	8	31	theme	same	1172:1175	arg1	kinetics					1184:1191	the same enzyme kinetics	1168:1191	the same enzyme kinetics	1168:1191	To the contrary, the deglycosylated UGT1A9, which was produced by the treatment with Endo H under the non-denaturing condition, showed the same enzyme kinetics as the control.
19951703	8	31	theme	same	1172:1175	arg1	control					1200:1206	the control	1196:1206	the control	1196:1206	To the contrary, the deglycosylated UGT1A9, which was produced by the treatment with Endo H under the non-denaturing condition, showed the same enzyme kinetics as the control.
19951703	6	32	from	role	768:771	arg1	activity					804:811	the enzyme activity	793:811	the enzyme activity	793:811	To evaluate the role of glycosylation in the enzyme activity, we produced unglycosylated UGT1A9 by treating HEK293 cells transiently transfected with expression plasmid with tunicamycin.
19951703	5	33	theme	blot	737:740	arg1	analysis					742:749	Western blot analysis	729:749	Western blot analysis	729:749	In comparison with the wild-type, these mutants showed decreased enzyme activities in parallel with the extent of the band shift in Western blot analysis.
19951703	7	34	theme	indirect	1003:1010	arg1	which					986:990	which	986:990	which	986:990	The unglycosylated UGT1A9 was almost inactive, which was not an indirect effect of ER stress.
19951703	7	34	theme	indirect	1003:1010	arg1	effect					1012:1017	an indirect effect	1000:1017	an indirect effect of ER stress	1000:1030	The unglycosylated UGT1A9 was almost inactive, which was not an indirect effect of ER stress.
19951703	8	35	theme	enzyme	1177:1182	arg1	kinetics					1184:1191	the same enzyme kinetics	1168:1191	the same enzyme kinetics	1168:1191	To the contrary, the deglycosylated UGT1A9, which was produced by the treatment with Endo H under the non-denaturing condition, showed the same enzyme kinetics as the control.
19951703	8	35	theme	enzyme	1177:1182	arg1	control					1200:1206	the control	1196:1206	the control	1196:1206	To the contrary, the deglycosylated UGT1A9, which was produced by the treatment with Endo H under the non-denaturing condition, showed the same enzyme kinetics as the control.
19951703	8	36	with	treatment	1103:1111	arg1	H					1123:1123	Endo H	1118:1123	Endo H under the non-denaturing condition	1118:1158	To the contrary, the deglycosylated UGT1A9, which was produced by the treatment with Endo H under the non-denaturing condition, showed the same enzyme kinetics as the control.
19951703	2	37	theme	I	178:178	arg1	proteins					189:196	type I membrane proteins	173:196	type I membrane proteins of the endoplasmic reticulum (ER) with a glycosylated luminal domain	173:265	UGTs are type I membrane proteins of the endoplasmic reticulum (ER) with a glycosylated luminal domain.
19951703	2	37	theme	I	178:178	arg1	UGTs					164:167	UGTs	164:167	UGTs	164:167	UGTs are type I membrane proteins of the endoplasmic reticulum (ER) with a glycosylated luminal domain.
19951703	2	38	with	proteins	189:196	arg1	domain					260:265	a glycosylated luminal domain	237:265	a glycosylated luminal domain	237:265	UGTs are type I membrane proteins of the endoplasmic reticulum (ER) with a glycosylated luminal domain.
19951703	0	39	theme	protein	32:38	arg1	folding					40:46	protein folding	32:46	protein folding of human UGT1A9	32:62	N-Glycosylation plays a role in protein folding of human UGT1A9.
19951703	3	40	gly	N-glycosylation	318:332	arg1	UGT1A9					359:364	human UGT1A9	353:364	human UGT1A9	353:364	In the present study, we investigated the role of N-glycosylation in the function of human UGT1A9.
19951703	2	41	theme	type	173:176	arg1	proteins					189:196	type I membrane proteins	173:196	type I membrane proteins of the endoplasmic reticulum (ER) with a glycosylated luminal domain	173:265	UGTs are type I membrane proteins of the endoplasmic reticulum (ER) with a glycosylated luminal domain.
19951703	2	41	theme	type	173:176	arg1	UGTs					164:167	UGTs	164:167	UGTs	164:167	UGTs are type I membrane proteins of the endoplasmic reticulum (ER) with a glycosylated luminal domain.
19951703	6	42	gly	glycosylation	776:788	arg1	enzyme					797:802	the enzyme activity	793:811	the enzyme activity	793:811	To evaluate the role of glycosylation in the enzyme activity, we produced unglycosylated UGT1A9 by treating HEK293 cells transiently transfected with expression plasmid with tunicamycin.
19951703	4	43	theme	glycan	580:585	arg1	glycosylation					547:559	glycosylation	547:559	glycosylation	547:559	Mutation analysis at the potential N-glycosylation sites at residues 71, 292, and 344 (from asparagine to glutamine) revealed that all of them were glycosylated, but the extent of glycosylation and/or size of the glycan differed.
19951703	5	44	theme	band	715:718	arg1	shift					720:724	the band shift	711:724	the band shift in Western blot analysis	711:749	In comparison with the wild-type, these mutants showed decreased enzyme activities in parallel with the extent of the band shift in Western blot analysis.
19951703	5	45	theme	decreased	652:660	arg1	activities					669:678	decreased enzyme activities	652:678	decreased enzyme activities	652:678	In comparison with the wild-type, these mutants showed decreased enzyme activities in parallel with the extent of the band shift in Western blot analysis.
19951703	6	46	theme	glycosylation	776:788	arg1	role					768:771	the role	764:771	the role of glycosylation in the enzyme activity	764:811	To evaluate the role of glycosylation in the enzyme activity, we produced unglycosylated UGT1A9 by treating HEK293 cells transiently transfected with expression plasmid with tunicamycin.
19951703	5	47	with	parallel	683:690	arg1	extent					701:706	the extent	697:706	the extent of the band shift in Western blot analysis	697:749	In comparison with the wild-type, these mutants showed decreased enzyme activities in parallel with the extent of the band shift in Western blot analysis.
19951703	5	48	theme	shift	720:724	arg1	extent					701:706	the extent	697:706	the extent of the band shift in Western blot analysis	697:749	In comparison with the wild-type, these mutants showed decreased enzyme activities in parallel with the extent of the band shift in Western blot analysis.
19951703	4	49	from	sites	418:422	arg1	analysis					376:383	Mutation analysis	367:383	Mutation analysis at the potential N-glycosylation sites at residues 71, 292, and 344 (from asparagine to glutamine)	367:482	Mutation analysis at the potential N-glycosylation sites at residues 71, 292, and 344 (from asparagine to glutamine) revealed that all of them were glycosylated, but the extent of glycosylation and/or size of the glycan differed.
19951703	6	50	theme	expression	902:911	arg1	plasmid					913:919	expression plasmid	902:919	expression plasmid with tunicamycin	902:936	To evaluate the role of glycosylation in the enzyme activity, we produced unglycosylated UGT1A9 by treating HEK293 cells transiently transfected with expression plasmid with tunicamycin.
19951703	2	51	theme	reticulum	217:225	arg1	proteins					189:196	type I membrane proteins	173:196	type I membrane proteins of the endoplasmic reticulum (ER) with a glycosylated luminal domain	173:265	UGTs are type I membrane proteins of the endoplasmic reticulum (ER) with a glycosylated luminal domain.
19951703	2	51	theme	reticulum	217:225	arg1	UGTs					164:167	UGTs	164:167	UGTs	164:167	UGTs are type I membrane proteins of the endoplasmic reticulum (ER) with a glycosylated luminal domain.
19951703	8	52	gly	deglycosylated	1054:1067	arg1	UGT1A9					1069:1074	the deglycosylated UGT1A9	1050:1074	the deglycosylated UGT1A9	1050:1074	To the contrary, the deglycosylated UGT1A9, which was produced by the treatment with Endo H under the non-denaturing condition, showed the same enzyme kinetics as the control.
19951703	5	53	from	extent	701:706	arg1	analysis					742:749	Western blot analysis	729:749	Western blot analysis	729:749	In comparison with the wild-type, these mutants showed decreased enzyme activities in parallel with the extent of the band shift in Western blot analysis.
19951703	4	54	theme	potential	392:400	arg1	sites					418:422	the potential N-glycosylation sites	388:422	the potential N-glycosylation sites at residues 71, 292, and 344	388:451	Mutation analysis at the potential N-glycosylation sites at residues 71, 292, and 344 (from asparagine to glutamine) revealed that all of them were glycosylated, but the extent of glycosylation and/or size of the glycan differed.
19951703	2	55	theme	endoplasmic	205:215	arg1	ER					228:229	ER	228:229	ER	228:229	UGTs are type I membrane proteins of the endoplasmic reticulum (ER) with a glycosylated luminal domain.
19951703	2	55	theme	endoplasmic	205:215	arg1	reticulum					217:225	the endoplasmic reticulum	201:225	the endoplasmic reticulum (ER)	201:230	UGTs are type I membrane proteins of the endoplasmic reticulum (ER) with a glycosylated luminal domain.
19951703	7	56	theme	unglycosylated	943:956	arg1	UGT1A9					958:963	The unglycosylated UGT1A9	939:963	The unglycosylated UGT1A9	939:963	The unglycosylated UGT1A9 was almost inactive, which was not an indirect effect of ER stress.
19951703	7	56	theme	unglycosylated	943:956	arg1	inactive					976:983	inactive	976:983	inactive	976:983	The unglycosylated UGT1A9 was almost inactive, which was not an indirect effect of ER stress.
19951703	7	57	gly	unglycosylated	943:956	arg1	UGT1A9					958:963	The unglycosylated UGT1A9	939:963	The unglycosylated UGT1A9	939:963	The unglycosylated UGT1A9 was almost inactive, which was not an indirect effect of ER stress.
19951703	7	57	gly	unglycosylated	943:956	arg1	inactive					976:983	inactive	976:983	inactive	976:983	The unglycosylated UGT1A9 was almost inactive, which was not an indirect effect of ER stress.
19951703	10	58	theme	stability	1337:1345	arg1	analysis					1347:1354	The thermal stability analysis	1325:1354	The thermal stability analysis of the mutated and deglycosylated UGT1A9 proteins	1325:1404	The thermal stability analysis of the mutated and deglycosylated UGT1A9 proteins supported the findings.
19951703	2	59	theme	glycosylated	239:250	arg1	domain					260:265	a glycosylated luminal domain	237:265	a glycosylated luminal domain	237:265	UGTs are type I membrane proteins of the endoplasmic reticulum (ER) with a glycosylated luminal domain.
19951703	11	60	contain	has	1479:1481	arg2	role					1496:1499	an important role	1483:1499	an important role	1483:1499	In conclusion, we found that the N-glycosylation has an important role in the folding of UGT1A9.
19951703	11	60	contain	has	1479:1481	arg1	N-glycosylation					1463:1477	the N-glycosylation	1459:1477	the N-glycosylation	1459:1477	In conclusion, we found that the N-glycosylation has an important role in the folding of UGT1A9.
19951703	3	61	theme	present	275:281	arg1	study					283:287	the present study	271:287	the present study	271:287	In the present study, we investigated the role of N-glycosylation in the function of human UGT1A9.
19951703	10	62	theme	proteins	1397:1404	arg1	analysis					1347:1354	The thermal stability analysis	1325:1354	The thermal stability analysis of the mutated and deglycosylated UGT1A9 proteins	1325:1404	The thermal stability analysis of the mutated and deglycosylated UGT1A9 proteins supported the findings.
19951703	5	63	with	comparison	600:609	arg1	wild-type					620:628	wild-type	620:628	wild-type	620:628	In comparison with the wild-type, these mutants showed decreased enzyme activities in parallel with the extent of the band shift in Western blot analysis.
19951703	8	64	theme	non-denaturing	1135:1148	arg1	condition					1150:1158	the non-denaturing condition	1131:1158	the non-denaturing condition	1131:1158	To the contrary, the deglycosylated UGT1A9, which was produced by the treatment with Endo H under the non-denaturing condition, showed the same enzyme kinetics as the control.
19951703	7	65	theme	ER	1022:1023	arg1	stress					1025:1030	ER stress	1022:1030	ER stress	1022:1030	The unglycosylated UGT1A9 was almost inactive, which was not an indirect effect of ER stress.
19951703	0	66	theme	UGT1A9	57:62	arg1	folding					40:46	protein folding	32:46	protein folding of human UGT1A9	32:62	N-Glycosylation plays a role in protein folding of human UGT1A9.
19951703	2	67	theme	membrane	180:187	arg1	proteins					189:196	type I membrane proteins	173:196	type I membrane proteins of the endoplasmic reticulum (ER) with a glycosylated luminal domain	173:265	UGTs are type I membrane proteins of the endoplasmic reticulum (ER) with a glycosylated luminal domain.
19951703	2	67	theme	membrane	180:187	arg1	UGTs					164:167	UGTs	164:167	UGTs	164:167	UGTs are type I membrane proteins of the endoplasmic reticulum (ER) with a glycosylated luminal domain.
19951703	1	68	theme	variety	135:141	arg1	glucuronidation					114:128	the glucuronidation	110:128	the glucuronidation of a variety of xeno/endobiotics	110:161	UDP-glucuronosyltransferases (UGTs) catalyze the glucuronidation of a variety of xeno/endobiotics.
19951703	10	69	gly	deglycosylated	1375:1388	arg1	proteins					1397:1404	deglycosylated UGT1A9 proteins	1375:1404	deglycosylated UGT1A9 proteins	1375:1404	The thermal stability analysis of the mutated and deglycosylated UGT1A9 proteins supported the findings.
19951703	0	70	theme	human	51:55	arg1	UGT1A9					57:62	human UGT1A9	51:62	human UGT1A9	51:62	N-Glycosylation plays a role in protein folding of human UGT1A9.
19951703	5	71	from	shift	720:724	arg1	analysis					742:749	Western blot analysis	729:749	Western blot analysis	729:749	In comparison with the wild-type, these mutants showed decreased enzyme activities in parallel with the extent of the band shift in Western blot analysis.
19951703	9	72	theme	UGT1A9	1317:1322	arg1	folding					1306:1312	the folding	1302:1312	the folding of UGT1A9	1302:1322	These results suggest that the glycosylation that occurs during translation is important for the folding of UGT1A9.
19951703	11	73	theme	UGT1A9	1519:1524	arg1	folding					1508:1514	the folding	1504:1514	the folding of UGT1A9	1504:1524	In conclusion, we found that the N-glycosylation has an important role in the folding of UGT1A9.
19951703	5	74	theme	Western	729:735	arg1	analysis					742:749	Western blot analysis	729:749	Western blot analysis	729:749	In comparison with the wild-type, these mutants showed decreased enzyme activities in parallel with the extent of the band shift in Western blot analysis.
19951703	4	75	theme	glycosylation	547:559	arg1	extent					537:542	the extent	533:542	the extent of glycosylation and/or size of the glycan	533:585	Mutation analysis at the potential N-glycosylation sites at residues 71, 292, and 344 (from asparagine to glutamine) revealed that all of them were glycosylated, but the extent of glycosylation and/or size of the glycan differed.
19379732	4	0	theme	degrees	1102:1108	arg1	C					1110:1110	28 degrees C	1099:1110	28 degrees C	1099:1110	However, the N138Q/N144Q double mutant displayed barely detectable membrane expression at approximately 65 kDa, no apparent glycosylation and minimal AA uptake (<10%) with no discernible improvement in expression or activity when cultured at 28 degrees C or 37 degrees C. Marker protein immunocytochemistry with N138Q/N144Q identified intracellular aggregates with hSVCT1 localised at the nuclear membrane but absent at the plasma membrane thus implicating its role as a possible intracellular transporter and suggesting N-glycosylation is required for hSVCT1 membrane targeting.
19379732	2	1	theme	hSVCT2	319:324	arg1	N-					274:275	N-	274:275	N-	274:275	Antibodies to N- and C-termini of hSVCT1 and C-terminus of hSVCT2 identified positive immunofluorescence only after permeabilisation, suggesting these regions are intracellular.
19379732	2	1	theme	hSVCT2	319:324	arg1	C-terminus					305:314	C-terminus	305:314	C-terminus of hSVCT2	305:324	Antibodies to N- and C-termini of hSVCT1 and C-terminus of hSVCT2 identified positive immunofluorescence only after permeabilisation, suggesting these regions are intracellular.
19379732	3	2	theme	WT	843:844	arg1	activity					846:853	WT activity	843:853	WT activity	843:853	PNGase F treatment confirmed that WT hSVCT1 (approximately 70-100 kDa) is glycosylated and site-directed mutagenesis of the three putative N-glycosylation sites, Asn138, Asn144, Asn230, demonstrated that mutants N138Q and N144Q were glycosylated (approximately 68-90 kDa) with only 31-65% of WT l-ascorbic acid (AA) uptake while the glycosylation profile of N230Q remained unaltered (approximately 98% of WT activity).
19379732	1	3	theme	COS-1	219:223	arg1	cells					225:229	COS-1 cells	219:229	COS-1 cells	219:229	The Na(+)-dependent transporters, hSVCT1 and hSVCT2, were assessed in COS-1 cells for their membrane topology.
19379732	5	4	theme	same	1457:1460	arg1	loop					1483:1486	the same putative hydrophilic loop	1453:1486	the same putative hydrophilic loop as Asn230	1453:1496	Also, Lys242 on the same putative hydrophilic loop as Asn230 after biotinylation was inaccessible from the extracellular side when analysed by MALDI-TOF MS. A new hSVCT1 secondary structure model supporting these findings is proposed.
19379732	3	5	gly	glycosylated	512:523	arg1	kDa					504:506	approximately 70-100 kDa	483:506	approximately 70-100 kDa	483:506	PNGase F treatment confirmed that WT hSVCT1 (approximately 70-100 kDa) is glycosylated and site-directed mutagenesis of the three putative N-glycosylation sites, Asn138, Asn144, Asn230, demonstrated that mutants N138Q and N144Q were glycosylated (approximately 68-90 kDa) with only 31-65% of WT l-ascorbic acid (AA) uptake while the glycosylation profile of N230Q remained unaltered (approximately 98% of WT activity).
19379732	3	5	gly	glycosylated	512:523	arg1	hSVCT1					475:480	WT hSVCT1	472:480	WT hSVCT1 (approximately 70-100 kDa)	472:507	PNGase F treatment confirmed that WT hSVCT1 (approximately 70-100 kDa) is glycosylated and site-directed mutagenesis of the three putative N-glycosylation sites, Asn138, Asn144, Asn230, demonstrated that mutants N138Q and N144Q were glycosylated (approximately 68-90 kDa) with only 31-65% of WT l-ascorbic acid (AA) uptake while the glycosylation profile of N230Q remained unaltered (approximately 98% of WT activity).
19379732	4	6	dep	identified	1181:1190	arg1	implicating					1302:1312	implicating	1302:1312	implicating its role as a possible intracellular transporter	1302:1361	However, the N138Q/N144Q double mutant displayed barely detectable membrane expression at approximately 65 kDa, no apparent glycosylation and minimal AA uptake (<10%) with no discernible improvement in expression or activity when cultured at 28 degrees C or 37 degrees C. Marker protein immunocytochemistry with N138Q/N144Q identified intracellular aggregates with hSVCT1 localised at the nuclear membrane but absent at the plasma membrane thus implicating its role as a possible intracellular transporter and suggesting N-glycosylation is required for hSVCT1 membrane targeting.
19379732	4	6	dep	identified	1181:1190	arg1	suggesting					1367:1376	suggesting	1367:1376	suggesting N-glycosylation is required for hSVCT1 membrane targeting	1367:1434	However, the N138Q/N144Q double mutant displayed barely detectable membrane expression at approximately 65 kDa, no apparent glycosylation and minimal AA uptake (<10%) with no discernible improvement in expression or activity when cultured at 28 degrees C or 37 degrees C. Marker protein immunocytochemistry with N138Q/N144Q identified intracellular aggregates with hSVCT1 localised at the nuclear membrane but absent at the plasma membrane thus implicating its role as a possible intracellular transporter and suggesting N-glycosylation is required for hSVCT1 membrane targeting.
19379732	3	7	theme	N230Q	796:800	arg1	profile					785:791	the glycosylation profile	767:791	the glycosylation profile of N230Q	767:800	PNGase F treatment confirmed that WT hSVCT1 (approximately 70-100 kDa) is glycosylated and site-directed mutagenesis of the three putative N-glycosylation sites, Asn138, Asn144, Asn230, demonstrated that mutants N138Q and N144Q were glycosylated (approximately 68-90 kDa) with only 31-65% of WT l-ascorbic acid (AA) uptake while the glycosylation profile of N230Q remained unaltered (approximately 98% of WT activity).
19379732	4	8	theme	Marker	1129:1134	arg1	immunocytochemistry					1144:1162	Marker protein immunocytochemistry	1129:1162	Marker protein immunocytochemistry with N138Q/N144Q	1129:1179	However, the N138Q/N144Q double mutant displayed barely detectable membrane expression at approximately 65 kDa, no apparent glycosylation and minimal AA uptake (<10%) with no discernible improvement in expression or activity when cultured at 28 degrees C or 37 degrees C. Marker protein immunocytochemistry with N138Q/N144Q identified intracellular aggregates with hSVCT1 localised at the nuclear membrane but absent at the plasma membrane thus implicating its role as a possible intracellular transporter and suggesting N-glycosylation is required for hSVCT1 membrane targeting.
19379732	5	9	theme	putative	1462:1469	arg1	loop					1483:1486	the same putative hydrophilic loop	1453:1486	the same putative hydrophilic loop as Asn230	1453:1496	Also, Lys242 on the same putative hydrophilic loop as Asn230 after biotinylation was inaccessible from the extracellular side when analysed by MALDI-TOF MS. A new hSVCT1 secondary structure model supporting these findings is proposed.
19379732	3	10	dep	unaltered	811:819	arg1	%					838:838	approximately 98%	822:838	approximately 98% of WT activity	822:853	PNGase F treatment confirmed that WT hSVCT1 (approximately 70-100 kDa) is glycosylated and site-directed mutagenesis of the three putative N-glycosylation sites, Asn138, Asn144, Asn230, demonstrated that mutants N138Q and N144Q were glycosylated (approximately 68-90 kDa) with only 31-65% of WT l-ascorbic acid (AA) uptake while the glycosylation profile of N230Q remained unaltered (approximately 98% of WT activity).
19379732	3	10	dep	unaltered	811:819	arg1	activity					846:853	WT activity	843:853	WT activity	843:853	PNGase F treatment confirmed that WT hSVCT1 (approximately 70-100 kDa) is glycosylated and site-directed mutagenesis of the three putative N-glycosylation sites, Asn138, Asn144, Asn230, demonstrated that mutants N138Q and N144Q were glycosylated (approximately 68-90 kDa) with only 31-65% of WT l-ascorbic acid (AA) uptake while the glycosylation profile of N230Q remained unaltered (approximately 98% of WT activity).
19379732	3	11	theme	site-directed	529:541	arg1	mutagenesis					543:553	site-directed mutagenesis	529:553	site-directed mutagenesis of the three putative N-glycosylation sites	529:597	PNGase F treatment confirmed that WT hSVCT1 (approximately 70-100 kDa) is glycosylated and site-directed mutagenesis of the three putative N-glycosylation sites, Asn138, Asn144, Asn230, demonstrated that mutants N138Q and N144Q were glycosylated (approximately 68-90 kDa) with only 31-65% of WT l-ascorbic acid (AA) uptake while the glycosylation profile of N230Q remained unaltered (approximately 98% of WT activity).
19379732	3	12	theme	glycosylation	771:783	arg1	profile					785:791	the glycosylation profile	767:791	the glycosylation profile of N230Q	767:800	PNGase F treatment confirmed that WT hSVCT1 (approximately 70-100 kDa) is glycosylated and site-directed mutagenesis of the three putative N-glycosylation sites, Asn138, Asn144, Asn230, demonstrated that mutants N138Q and N144Q were glycosylated (approximately 68-90 kDa) with only 31-65% of WT l-ascorbic acid (AA) uptake while the glycosylation profile of N230Q remained unaltered (approximately 98% of WT activity).
19379732	5	13	theme	extracellular	1544:1556	arg1	side					1558:1561	the extracellular side	1540:1561	the extracellular side	1540:1561	Also, Lys242 on the same putative hydrophilic loop as Asn230 after biotinylation was inaccessible from the extracellular side when analysed by MALDI-TOF MS. A new hSVCT1 secondary structure model supporting these findings is proposed.
19379732	4	14	theme	apparent	972:979	arg1	glycosylation					981:993	no apparent glycosylation	969:993	no apparent glycosylation	969:993	However, the N138Q/N144Q double mutant displayed barely detectable membrane expression at approximately 65 kDa, no apparent glycosylation and minimal AA uptake (<10%) with no discernible improvement in expression or activity when cultured at 28 degrees C or 37 degrees C. Marker protein immunocytochemistry with N138Q/N144Q identified intracellular aggregates with hSVCT1 localised at the nuclear membrane but absent at the plasma membrane thus implicating its role as a possible intracellular transporter and suggesting N-glycosylation is required for hSVCT1 membrane targeting.
19379732	5	15	from	side	1558:1561	arg1	inaccessible					1522:1533	inaccessible	1522:1533	inaccessible	1522:1533	Also, Lys242 on the same putative hydrophilic loop as Asn230 after biotinylation was inaccessible from the extracellular side when analysed by MALDI-TOF MS. A new hSVCT1 secondary structure model supporting these findings is proposed.
19379732	4	16	dep	C	1110:1110	arg1	C.					1126:1127	C.	1126:1127	C.	1126:1127	However, the N138Q/N144Q double mutant displayed barely detectable membrane expression at approximately 65 kDa, no apparent glycosylation and minimal AA uptake (<10%) with no discernible improvement in expression or activity when cultured at 28 degrees C or 37 degrees C. Marker protein immunocytochemistry with N138Q/N144Q identified intracellular aggregates with hSVCT1 localised at the nuclear membrane but absent at the plasma membrane thus implicating its role as a possible intracellular transporter and suggesting N-glycosylation is required for hSVCT1 membrane targeting.
19379732	4	17	from	membrane	1288:1295	arg1	absent					1267:1272	absent	1267:1272	absent	1267:1272	However, the N138Q/N144Q double mutant displayed barely detectable membrane expression at approximately 65 kDa, no apparent glycosylation and minimal AA uptake (<10%) with no discernible improvement in expression or activity when cultured at 28 degrees C or 37 degrees C. Marker protein immunocytochemistry with N138Q/N144Q identified intracellular aggregates with hSVCT1 localised at the nuclear membrane but absent at the plasma membrane thus implicating its role as a possible intracellular transporter and suggesting N-glycosylation is required for hSVCT1 membrane targeting.
19379732	0	18	theme	N-glycosylation	101:115	arg1	transporter					68:78	the human sodium-dependent vitamin C transporter	31:78	the human sodium-dependent vitamin C transporter	31:78	Topological studies of hSVCT1, the human sodium-dependent vitamin C transporter and the influence of N-glycosylation on its intracellular targeting.
19379732	0	18	theme	N-glycosylation	101:115	arg1	influence					88:96	the influence	84:96	the influence of N-glycosylation on its intracellular targeting	84:146	Topological studies of hSVCT1, the human sodium-dependent vitamin C transporter and the influence of N-glycosylation on its intracellular targeting.
19379732	0	18	theme	N-glycosylation	101:115	arg1	hSVCT1					23:28	hSVCT1	23:28	hSVCT1	23:28	Topological studies of hSVCT1, the human sodium-dependent vitamin C transporter and the influence of N-glycosylation on its intracellular targeting.
19379732	4	19	theme	AA	1007:1008	arg1	uptake					1010:1015	minimal AA uptake	999:1015	minimal AA uptake (<10%)	999:1022	However, the N138Q/N144Q double mutant displayed barely detectable membrane expression at approximately 65 kDa, no apparent glycosylation and minimal AA uptake (<10%) with no discernible improvement in expression or activity when cultured at 28 degrees C or 37 degrees C. Marker protein immunocytochemistry with N138Q/N144Q identified intracellular aggregates with hSVCT1 localised at the nuclear membrane but absent at the plasma membrane thus implicating its role as a possible intracellular transporter and suggesting N-glycosylation is required for hSVCT1 membrane targeting.
19379732	4	19	theme	AA	1007:1008	arg1	%					1021:1021	<10%	1018:1021	<10%	1018:1021	However, the N138Q/N144Q double mutant displayed barely detectable membrane expression at approximately 65 kDa, no apparent glycosylation and minimal AA uptake (<10%) with no discernible improvement in expression or activity when cultured at 28 degrees C or 37 degrees C. Marker protein immunocytochemistry with N138Q/N144Q identified intracellular aggregates with hSVCT1 localised at the nuclear membrane but absent at the plasma membrane thus implicating its role as a possible intracellular transporter and suggesting N-glycosylation is required for hSVCT1 membrane targeting.
19379732	4	20	dep	hSVCT1	1222:1227	arg1	localised					1229:1237	localised	1229:1237	localised at the nuclear membrane	1229:1261	However, the N138Q/N144Q double mutant displayed barely detectable membrane expression at approximately 65 kDa, no apparent glycosylation and minimal AA uptake (<10%) with no discernible improvement in expression or activity when cultured at 28 degrees C or 37 degrees C. Marker protein immunocytochemistry with N138Q/N144Q identified intracellular aggregates with hSVCT1 localised at the nuclear membrane but absent at the plasma membrane thus implicating its role as a possible intracellular transporter and suggesting N-glycosylation is required for hSVCT1 membrane targeting.
19379732	4	20	dep	hSVCT1	1222:1227	arg1	absent					1267:1272	absent	1267:1272	absent	1267:1272	However, the N138Q/N144Q double mutant displayed barely detectable membrane expression at approximately 65 kDa, no apparent glycosylation and minimal AA uptake (<10%) with no discernible improvement in expression or activity when cultured at 28 degrees C or 37 degrees C. Marker protein immunocytochemistry with N138Q/N144Q identified intracellular aggregates with hSVCT1 localised at the nuclear membrane but absent at the plasma membrane thus implicating its role as a possible intracellular transporter and suggesting N-glycosylation is required for hSVCT1 membrane targeting.
19379732	5	21	theme	secondary	1607:1615	arg1	model					1627:1631	A new hSVCT1 secondary structure model	1594:1631	A new hSVCT1 secondary structure model supporting these findings	1594:1657	Also, Lys242 on the same putative hydrophilic loop as Asn230 after biotinylation was inaccessible from the extracellular side when analysed by MALDI-TOF MS. A new hSVCT1 secondary structure model supporting these findings is proposed.
19379732	4	22	theme	plasma	1281:1286	arg1	membrane					1288:1295	the plasma membrane	1277:1295	the plasma membrane	1277:1295	However, the N138Q/N144Q double mutant displayed barely detectable membrane expression at approximately 65 kDa, no apparent glycosylation and minimal AA uptake (<10%) with no discernible improvement in expression or activity when cultured at 28 degrees C or 37 degrees C. Marker protein immunocytochemistry with N138Q/N144Q identified intracellular aggregates with hSVCT1 localised at the nuclear membrane but absent at the plasma membrane thus implicating its role as a possible intracellular transporter and suggesting N-glycosylation is required for hSVCT1 membrane targeting.
19379732	4	23	gly	N-glycosylation	1378:1392	arg1	membrane					1417:1424	hSVCT1 membrane targeting	1410:1434	hSVCT1 membrane targeting	1410:1434	However, the N138Q/N144Q double mutant displayed barely detectable membrane expression at approximately 65 kDa, no apparent glycosylation and minimal AA uptake (<10%) with no discernible improvement in expression or activity when cultured at 28 degrees C or 37 degrees C. Marker protein immunocytochemistry with N138Q/N144Q identified intracellular aggregates with hSVCT1 localised at the nuclear membrane but absent at the plasma membrane thus implicating its role as a possible intracellular transporter and suggesting N-glycosylation is required for hSVCT1 membrane targeting.
19379732	4	23	gly	N-glycosylation	1378:1392	arg1	hSVCT1					1410:1415	hSVCT1 membrane targeting	1410:1434	hSVCT1 membrane targeting	1410:1434	However, the N138Q/N144Q double mutant displayed barely detectable membrane expression at approximately 65 kDa, no apparent glycosylation and minimal AA uptake (<10%) with no discernible improvement in expression or activity when cultured at 28 degrees C or 37 degrees C. Marker protein immunocytochemistry with N138Q/N144Q identified intracellular aggregates with hSVCT1 localised at the nuclear membrane but absent at the plasma membrane thus implicating its role as a possible intracellular transporter and suggesting N-glycosylation is required for hSVCT1 membrane targeting.
19379732	4	24	theme	hSVCT1	1410:1415	arg1	targeting					1426:1434	hSVCT1 membrane targeting	1410:1434	hSVCT1 membrane targeting	1410:1434	However, the N138Q/N144Q double mutant displayed barely detectable membrane expression at approximately 65 kDa, no apparent glycosylation and minimal AA uptake (<10%) with no discernible improvement in expression or activity when cultured at 28 degrees C or 37 degrees C. Marker protein immunocytochemistry with N138Q/N144Q identified intracellular aggregates with hSVCT1 localised at the nuclear membrane but absent at the plasma membrane thus implicating its role as a possible intracellular transporter and suggesting N-glycosylation is required for hSVCT1 membrane targeting.
19379732	3	25	theme	activity	846:853	arg1	%					838:838	approximately 98%	822:838	approximately 98% of WT activity	822:853	PNGase F treatment confirmed that WT hSVCT1 (approximately 70-100 kDa) is glycosylated and site-directed mutagenesis of the three putative N-glycosylation sites, Asn138, Asn144, Asn230, demonstrated that mutants N138Q and N144Q were glycosylated (approximately 68-90 kDa) with only 31-65% of WT l-ascorbic acid (AA) uptake while the glycosylation profile of N230Q remained unaltered (approximately 98% of WT activity).
19379732	3	25	theme	activity	846:853	arg1	activity					846:853	WT activity	843:853	WT activity	843:853	PNGase F treatment confirmed that WT hSVCT1 (approximately 70-100 kDa) is glycosylated and site-directed mutagenesis of the three putative N-glycosylation sites, Asn138, Asn144, Asn230, demonstrated that mutants N138Q and N144Q were glycosylated (approximately 68-90 kDa) with only 31-65% of WT l-ascorbic acid (AA) uptake while the glycosylation profile of N230Q remained unaltered (approximately 98% of WT activity).
19379732	3	26	theme	PNGase	438:443	arg1	treatment					447:455	PNGase F treatment	438:455	PNGase F treatment	438:455	PNGase F treatment confirmed that WT hSVCT1 (approximately 70-100 kDa) is glycosylated and site-directed mutagenesis of the three putative N-glycosylation sites, Asn138, Asn144, Asn230, demonstrated that mutants N138Q and N144Q were glycosylated (approximately 68-90 kDa) with only 31-65% of WT l-ascorbic acid (AA) uptake while the glycosylation profile of N230Q remained unaltered (approximately 98% of WT activity).
19379732	4	27	with	aggregates	1206:1215	arg1	hSVCT1					1222:1227	hSVCT1	1222:1227	hSVCT1 localised at the nuclear membrane but absent at the plasma membrane	1222:1295	However, the N138Q/N144Q double mutant displayed barely detectable membrane expression at approximately 65 kDa, no apparent glycosylation and minimal AA uptake (<10%) with no discernible improvement in expression or activity when cultured at 28 degrees C or 37 degrees C. Marker protein immunocytochemistry with N138Q/N144Q identified intracellular aggregates with hSVCT1 localised at the nuclear membrane but absent at the plasma membrane thus implicating its role as a possible intracellular transporter and suggesting N-glycosylation is required for hSVCT1 membrane targeting.
19379732	5	28	theme	hSVCT1	1600:1605	arg1	model					1627:1631	A new hSVCT1 secondary structure model	1594:1631	A new hSVCT1 secondary structure model supporting these findings	1594:1657	Also, Lys242 on the same putative hydrophilic loop as Asn230 after biotinylation was inaccessible from the extracellular side when analysed by MALDI-TOF MS. A new hSVCT1 secondary structure model supporting these findings is proposed.
19379732	3	29	dep	glycosylated	671:682	arg1	kDa					705:707	approximately 68-90 kDa	685:707	approximately 68-90 kDa	685:707	PNGase F treatment confirmed that WT hSVCT1 (approximately 70-100 kDa) is glycosylated and site-directed mutagenesis of the three putative N-glycosylation sites, Asn138, Asn144, Asn230, demonstrated that mutants N138Q and N144Q were glycosylated (approximately 68-90 kDa) with only 31-65% of WT l-ascorbic acid (AA) uptake while the glycosylation profile of N230Q remained unaltered (approximately 98% of WT activity).
19379732	1	30	theme	-dependent	158:167	arg1	hSVCT1					183:188	hSVCT1	183:188	hSVCT1	183:188	The Na(+)-dependent transporters, hSVCT1 and hSVCT2, were assessed in COS-1 cells for their membrane topology.
19379732	1	30	theme	-dependent	158:167	arg1	transporters					169:180	The Na(+)-dependent transporters	149:180	The Na(+)-dependent transporters	149:180	The Na(+)-dependent transporters, hSVCT1 and hSVCT2, were assessed in COS-1 cells for their membrane topology.
19379732	1	30	theme	-dependent	158:167	arg1	hSVCT2					194:199	hSVCT2	194:199	hSVCT2	194:199	The Na(+)-dependent transporters, hSVCT1 and hSVCT2, were assessed in COS-1 cells for their membrane topology.
19379732	0	31	theme	Topological	0:10	arg1	studies					12:18	Topological studies	0:18	Topological studies of hSVCT1, the human sodium-dependent vitamin C transporter and the influence of N-glycosylation on its intracellular targeting.	0:147	Topological studies of hSVCT1, the human sodium-dependent vitamin C transporter and the influence of N-glycosylation on its intracellular targeting.
19379732	1	32	theme	membrane	241:248	arg1	topology					250:257	their membrane topology	235:257	their membrane topology	235:257	The Na(+)-dependent transporters, hSVCT1 and hSVCT2, were assessed in COS-1 cells for their membrane topology.
19379732	3	33	theme	putative	568:575	arg1	sites					593:597	the three putative N-glycosylation sites	558:597	the three putative N-glycosylation sites	558:597	PNGase F treatment confirmed that WT hSVCT1 (approximately 70-100 kDa) is glycosylated and site-directed mutagenesis of the three putative N-glycosylation sites, Asn138, Asn144, Asn230, demonstrated that mutants N138Q and N144Q were glycosylated (approximately 68-90 kDa) with only 31-65% of WT l-ascorbic acid (AA) uptake while the glycosylation profile of N230Q remained unaltered (approximately 98% of WT activity).
19379732	4	34	dep	C.	1126:1127	arg1	identified					1181:1190	identified	1181:1190	identified intracellular aggregates with hSVCT1 localised at the nuclear membrane but absent at the plasma membrane thus implicating its role as a possible intracellular transporter and suggesting N-glycosylation is required for hSVCT1 membrane targeting	1181:1434	However, the N138Q/N144Q double mutant displayed barely detectable membrane expression at approximately 65 kDa, no apparent glycosylation and minimal AA uptake (<10%) with no discernible improvement in expression or activity when cultured at 28 degrees C or 37 degrees C. Marker protein immunocytochemistry with N138Q/N144Q identified intracellular aggregates with hSVCT1 localised at the nuclear membrane but absent at the plasma membrane thus implicating its role as a possible intracellular transporter and suggesting N-glycosylation is required for hSVCT1 membrane targeting.
19379732	0	35	theme	hSVCT1	23:28	arg1	studies					12:18	Topological studies	0:18	Topological studies of hSVCT1, the human sodium-dependent vitamin C transporter and the influence of N-glycosylation on its intracellular targeting.	0:147	Topological studies of hSVCT1, the human sodium-dependent vitamin C transporter and the influence of N-glycosylation on its intracellular targeting.
19379732	3	36	theme	WT	730:731	arg1	uptake					754:759	WT l-ascorbic acid (AA) uptake	730:759	WT l-ascorbic acid (AA) uptake while the glycosylation profile of N230Q remained unaltered (approximately 98% of WT activity)	730:854	PNGase F treatment confirmed that WT hSVCT1 (approximately 70-100 kDa) is glycosylated and site-directed mutagenesis of the three putative N-glycosylation sites, Asn138, Asn144, Asn230, demonstrated that mutants N138Q and N144Q were glycosylated (approximately 68-90 kDa) with only 31-65% of WT l-ascorbic acid (AA) uptake while the glycosylation profile of N230Q remained unaltered (approximately 98% of WT activity).
19379732	4	37	theme	intracellular	1192:1204	arg1	aggregates					1206:1215	intracellular aggregates	1192:1215	intracellular aggregates with hSVCT1 localised at the nuclear membrane but absent at the plasma membrane	1192:1295	However, the N138Q/N144Q double mutant displayed barely detectable membrane expression at approximately 65 kDa, no apparent glycosylation and minimal AA uptake (<10%) with no discernible improvement in expression or activity when cultured at 28 degrees C or 37 degrees C. Marker protein immunocytochemistry with N138Q/N144Q identified intracellular aggregates with hSVCT1 localised at the nuclear membrane but absent at the plasma membrane thus implicating its role as a possible intracellular transporter and suggesting N-glycosylation is required for hSVCT1 membrane targeting.
19379732	4	38	theme	discernible	1032:1042	arg1	improvement					1044:1054	no discernible improvement	1029:1054	no discernible improvement in expression or activity	1029:1080	However, the N138Q/N144Q double mutant displayed barely detectable membrane expression at approximately 65 kDa, no apparent glycosylation and minimal AA uptake (<10%) with no discernible improvement in expression or activity when cultured at 28 degrees C or 37 degrees C. Marker protein immunocytochemistry with N138Q/N144Q identified intracellular aggregates with hSVCT1 localised at the nuclear membrane but absent at the plasma membrane thus implicating its role as a possible intracellular transporter and suggesting N-glycosylation is required for hSVCT1 membrane targeting.
19379732	5	39	theme	new	1596:1598	arg1	model					1627:1631	A new hSVCT1 secondary structure model	1594:1631	A new hSVCT1 secondary structure model supporting these findings	1594:1657	Also, Lys242 on the same putative hydrophilic loop as Asn230 after biotinylation was inaccessible from the extracellular side when analysed by MALDI-TOF MS. A new hSVCT1 secondary structure model supporting these findings is proposed.
19379732	4	40	theme	N138Q/N144Q	870:880	arg1	mutant					889:894	the N138Q/N144Q double mutant	866:894	the N138Q/N144Q double mutant	866:894	However, the N138Q/N144Q double mutant displayed barely detectable membrane expression at approximately 65 kDa, no apparent glycosylation and minimal AA uptake (<10%) with no discernible improvement in expression or activity when cultured at 28 degrees C or 37 degrees C. Marker protein immunocytochemistry with N138Q/N144Q identified intracellular aggregates with hSVCT1 localised at the nuclear membrane but absent at the plasma membrane thus implicating its role as a possible intracellular transporter and suggesting N-glycosylation is required for hSVCT1 membrane targeting.
19379732	5	41	theme	hydrophilic	1471:1481	arg1	loop					1483:1486	the same putative hydrophilic loop	1453:1486	the same putative hydrophilic loop as Asn230	1453:1496	Also, Lys242 on the same putative hydrophilic loop as Asn230 after biotinylation was inaccessible from the extracellular side when analysed by MALDI-TOF MS. A new hSVCT1 secondary structure model supporting these findings is proposed.
19379732	4	42	theme	double	882:887	arg1	mutant					889:894	the N138Q/N144Q double mutant	866:894	the N138Q/N144Q double mutant	866:894	However, the N138Q/N144Q double mutant displayed barely detectable membrane expression at approximately 65 kDa, no apparent glycosylation and minimal AA uptake (<10%) with no discernible improvement in expression or activity when cultured at 28 degrees C or 37 degrees C. Marker protein immunocytochemistry with N138Q/N144Q identified intracellular aggregates with hSVCT1 localised at the nuclear membrane but absent at the plasma membrane thus implicating its role as a possible intracellular transporter and suggesting N-glycosylation is required for hSVCT1 membrane targeting.
19379732	0	43	from	transporter	68:78	arg1	targeting					138:146	its intracellular targeting	120:146	its intracellular targeting	120:146	Topological studies of hSVCT1, the human sodium-dependent vitamin C transporter and the influence of N-glycosylation on its intracellular targeting.
19379732	4	44	theme	minimal	999:1005	arg1	uptake					1010:1015	minimal AA uptake	999:1015	minimal AA uptake (<10%)	999:1022	However, the N138Q/N144Q double mutant displayed barely detectable membrane expression at approximately 65 kDa, no apparent glycosylation and minimal AA uptake (<10%) with no discernible improvement in expression or activity when cultured at 28 degrees C or 37 degrees C. Marker protein immunocytochemistry with N138Q/N144Q identified intracellular aggregates with hSVCT1 localised at the nuclear membrane but absent at the plasma membrane thus implicating its role as a possible intracellular transporter and suggesting N-glycosylation is required for hSVCT1 membrane targeting.
19379732	4	44	theme	minimal	999:1005	arg1	%					1021:1021	<10%	1018:1021	<10%	1018:1021	However, the N138Q/N144Q double mutant displayed barely detectable membrane expression at approximately 65 kDa, no apparent glycosylation and minimal AA uptake (<10%) with no discernible improvement in expression or activity when cultured at 28 degrees C or 37 degrees C. Marker protein immunocytochemistry with N138Q/N144Q identified intracellular aggregates with hSVCT1 localised at the nuclear membrane but absent at the plasma membrane thus implicating its role as a possible intracellular transporter and suggesting N-glycosylation is required for hSVCT1 membrane targeting.
19379732	3	45	theme	F	445:445	arg1	treatment					447:455	PNGase F treatment	438:455	PNGase F treatment	438:455	PNGase F treatment confirmed that WT hSVCT1 (approximately 70-100 kDa) is glycosylated and site-directed mutagenesis of the three putative N-glycosylation sites, Asn138, Asn144, Asn230, demonstrated that mutants N138Q and N144Q were glycosylated (approximately 68-90 kDa) with only 31-65% of WT l-ascorbic acid (AA) uptake while the glycosylation profile of N230Q remained unaltered (approximately 98% of WT activity).
19379732	4	46	with	immunocytochemistry	1144:1162	arg1	N138Q/N144Q					1169:1179	N138Q/N144Q	1169:1179	N138Q/N144Q	1169:1179	However, the N138Q/N144Q double mutant displayed barely detectable membrane expression at approximately 65 kDa, no apparent glycosylation and minimal AA uptake (<10%) with no discernible improvement in expression or activity when cultured at 28 degrees C or 37 degrees C. Marker protein immunocytochemistry with N138Q/N144Q identified intracellular aggregates with hSVCT1 localised at the nuclear membrane but absent at the plasma membrane thus implicating its role as a possible intracellular transporter and suggesting N-glycosylation is required for hSVCT1 membrane targeting.
19379732	4	47	from	kDa	964:966	arg1	expression					933:942	barely detectable membrane expression	906:942	barely detectable membrane expression at approximately 65 kDa	906:966	However, the N138Q/N144Q double mutant displayed barely detectable membrane expression at approximately 65 kDa, no apparent glycosylation and minimal AA uptake (<10%) with no discernible improvement in expression or activity when cultured at 28 degrees C or 37 degrees C. Marker protein immunocytochemistry with N138Q/N144Q identified intracellular aggregates with hSVCT1 localised at the nuclear membrane but absent at the plasma membrane thus implicating its role as a possible intracellular transporter and suggesting N-glycosylation is required for hSVCT1 membrane targeting.
19379732	4	47	from	kDa	964:966	arg1	uptake					1010:1015	minimal AA uptake	999:1015	minimal AA uptake (<10%)	999:1022	However, the N138Q/N144Q double mutant displayed barely detectable membrane expression at approximately 65 kDa, no apparent glycosylation and minimal AA uptake (<10%) with no discernible improvement in expression or activity when cultured at 28 degrees C or 37 degrees C. Marker protein immunocytochemistry with N138Q/N144Q identified intracellular aggregates with hSVCT1 localised at the nuclear membrane but absent at the plasma membrane thus implicating its role as a possible intracellular transporter and suggesting N-glycosylation is required for hSVCT1 membrane targeting.
19379732	4	47	from	kDa	964:966	arg1	%					1021:1021	<10%	1018:1021	<10%	1018:1021	However, the N138Q/N144Q double mutant displayed barely detectable membrane expression at approximately 65 kDa, no apparent glycosylation and minimal AA uptake (<10%) with no discernible improvement in expression or activity when cultured at 28 degrees C or 37 degrees C. Marker protein immunocytochemistry with N138Q/N144Q identified intracellular aggregates with hSVCT1 localised at the nuclear membrane but absent at the plasma membrane thus implicating its role as a possible intracellular transporter and suggesting N-glycosylation is required for hSVCT1 membrane targeting.
19379732	4	47	from	kDa	964:966	arg1	glycosylation					981:993	no apparent glycosylation	969:993	no apparent glycosylation	969:993	However, the N138Q/N144Q double mutant displayed barely detectable membrane expression at approximately 65 kDa, no apparent glycosylation and minimal AA uptake (<10%) with no discernible improvement in expression or activity when cultured at 28 degrees C or 37 degrees C. Marker protein immunocytochemistry with N138Q/N144Q identified intracellular aggregates with hSVCT1 localised at the nuclear membrane but absent at the plasma membrane thus implicating its role as a possible intracellular transporter and suggesting N-glycosylation is required for hSVCT1 membrane targeting.
19379732	0	48	theme	intracellular	124:136	arg1	targeting					138:146	its intracellular targeting	120:146	its intracellular targeting	120:146	Topological studies of hSVCT1, the human sodium-dependent vitamin C transporter and the influence of N-glycosylation on its intracellular targeting.
19379732	4	49	gly	glycosylation	981:993	arg1	kDa					964:966	approximately 65 kDa	947:966	approximately 65 kDa	947:966	However, the N138Q/N144Q double mutant displayed barely detectable membrane expression at approximately 65 kDa, no apparent glycosylation and minimal AA uptake (<10%) with no discernible improvement in expression or activity when cultured at 28 degrees C or 37 degrees C. Marker protein immunocytochemistry with N138Q/N144Q identified intracellular aggregates with hSVCT1 localised at the nuclear membrane but absent at the plasma membrane thus implicating its role as a possible intracellular transporter and suggesting N-glycosylation is required for hSVCT1 membrane targeting.
19379732	4	49	gly	glycosylation	981:993	arg2	kDa					964:966	approximately 65 kDa	947:966	approximately 65 kDa	947:966	However, the N138Q/N144Q double mutant displayed barely detectable membrane expression at approximately 65 kDa, no apparent glycosylation and minimal AA uptake (<10%) with no discernible improvement in expression or activity when cultured at 28 degrees C or 37 degrees C. Marker protein immunocytochemistry with N138Q/N144Q identified intracellular aggregates with hSVCT1 localised at the nuclear membrane but absent at the plasma membrane thus implicating its role as a possible intracellular transporter and suggesting N-glycosylation is required for hSVCT1 membrane targeting.
19379732	3	50	gly	N-glycosylation	577:591	arg2	three					562:566	three	562:566	three	562:566	PNGase F treatment confirmed that WT hSVCT1 (approximately 70-100 kDa) is glycosylated and site-directed mutagenesis of the three putative N-glycosylation sites, Asn138, Asn144, Asn230, demonstrated that mutants N138Q and N144Q were glycosylated (approximately 68-90 kDa) with only 31-65% of WT l-ascorbic acid (AA) uptake while the glycosylation profile of N230Q remained unaltered (approximately 98% of WT activity).
19379732	3	50	gly	N-glycosylation	577:591	arg2	sites					593:597	the three putative N-glycosylation sites	558:597	the three putative N-glycosylation sites	558:597	PNGase F treatment confirmed that WT hSVCT1 (approximately 70-100 kDa) is glycosylated and site-directed mutagenesis of the three putative N-glycosylation sites, Asn138, Asn144, Asn230, demonstrated that mutants N138Q and N144Q were glycosylated (approximately 68-90 kDa) with only 31-65% of WT l-ascorbic acid (AA) uptake while the glycosylation profile of N230Q remained unaltered (approximately 98% of WT activity).
19379732	0	51	theme	sodium-dependent	41:56	arg1	transporter					68:78	the human sodium-dependent vitamin C transporter	31:78	the human sodium-dependent vitamin C transporter	31:78	Topological studies of hSVCT1, the human sodium-dependent vitamin C transporter and the influence of N-glycosylation on its intracellular targeting.
19379732	0	51	theme	sodium-dependent	41:56	arg1	hSVCT1					23:28	hSVCT1	23:28	hSVCT1	23:28	Topological studies of hSVCT1, the human sodium-dependent vitamin C transporter and the influence of N-glycosylation on its intracellular targeting.
19379732	3	52	theme	AA	750:751	arg1	uptake					754:759	WT l-ascorbic acid (AA) uptake	730:759	WT l-ascorbic acid (AA) uptake while the glycosylation profile of N230Q remained unaltered (approximately 98% of WT activity)	730:854	PNGase F treatment confirmed that WT hSVCT1 (approximately 70-100 kDa) is glycosylated and site-directed mutagenesis of the three putative N-glycosylation sites, Asn138, Asn144, Asn230, demonstrated that mutants N138Q and N144Q were glycosylated (approximately 68-90 kDa) with only 31-65% of WT l-ascorbic acid (AA) uptake while the glycosylation profile of N230Q remained unaltered (approximately 98% of WT activity).
19379732	4	53	theme	possible	1328:1335	arg1	transporter					1351:1361	a possible intracellular transporter	1326:1361	a possible intracellular transporter	1326:1361	However, the N138Q/N144Q double mutant displayed barely detectable membrane expression at approximately 65 kDa, no apparent glycosylation and minimal AA uptake (<10%) with no discernible improvement in expression or activity when cultured at 28 degrees C or 37 degrees C. Marker protein immunocytochemistry with N138Q/N144Q identified intracellular aggregates with hSVCT1 localised at the nuclear membrane but absent at the plasma membrane thus implicating its role as a possible intracellular transporter and suggesting N-glycosylation is required for hSVCT1 membrane targeting.
19379732	4	53	theme	possible	1328:1335	arg1	role					1318:1321	its role	1314:1321	its role	1314:1321	However, the N138Q/N144Q double mutant displayed barely detectable membrane expression at approximately 65 kDa, no apparent glycosylation and minimal AA uptake (<10%) with no discernible improvement in expression or activity when cultured at 28 degrees C or 37 degrees C. Marker protein immunocytochemistry with N138Q/N144Q identified intracellular aggregates with hSVCT1 localised at the nuclear membrane but absent at the plasma membrane thus implicating its role as a possible intracellular transporter and suggesting N-glycosylation is required for hSVCT1 membrane targeting.
19379732	3	54	gly	glycosylation	771:783	arg1	N230Q					796:800	N230Q	796:800	N230Q	796:800	PNGase F treatment confirmed that WT hSVCT1 (approximately 70-100 kDa) is glycosylated and site-directed mutagenesis of the three putative N-glycosylation sites, Asn138, Asn144, Asn230, demonstrated that mutants N138Q and N144Q were glycosylated (approximately 68-90 kDa) with only 31-65% of WT l-ascorbic acid (AA) uptake while the glycosylation profile of N230Q remained unaltered (approximately 98% of WT activity).
19379732	3	55	theme	N-glycosylation	577:591	arg1	sites					593:597	the three putative N-glycosylation sites	558:597	the three putative N-glycosylation sites	558:597	PNGase F treatment confirmed that WT hSVCT1 (approximately 70-100 kDa) is glycosylated and site-directed mutagenesis of the three putative N-glycosylation sites, Asn138, Asn144, Asn230, demonstrated that mutants N138Q and N144Q were glycosylated (approximately 68-90 kDa) with only 31-65% of WT l-ascorbic acid (AA) uptake while the glycosylation profile of N230Q remained unaltered (approximately 98% of WT activity).
19379732	3	56	dep	glycosylated	512:523	arg1	and					525:527	and	525:527	and	525:527	PNGase F treatment confirmed that WT hSVCT1 (approximately 70-100 kDa) is glycosylated and site-directed mutagenesis of the three putative N-glycosylation sites, Asn138, Asn144, Asn230, demonstrated that mutants N138Q and N144Q were glycosylated (approximately 68-90 kDa) with only 31-65% of WT l-ascorbic acid (AA) uptake while the glycosylation profile of N230Q remained unaltered (approximately 98% of WT activity).
19379732	0	57	theme	human	35:39	arg1	transporter					68:78	the human sodium-dependent vitamin C transporter	31:78	the human sodium-dependent vitamin C transporter	31:78	Topological studies of hSVCT1, the human sodium-dependent vitamin C transporter and the influence of N-glycosylation on its intracellular targeting.
19379732	0	57	theme	human	35:39	arg1	hSVCT1					23:28	hSVCT1	23:28	hSVCT1	23:28	Topological studies of hSVCT1, the human sodium-dependent vitamin C transporter and the influence of N-glycosylation on its intracellular targeting.
19379732	3	58	theme	l-ascorbic	733:742	arg1	uptake					754:759	WT l-ascorbic acid (AA) uptake	730:759	WT l-ascorbic acid (AA) uptake while the glycosylation profile of N230Q remained unaltered (approximately 98% of WT activity)	730:854	PNGase F treatment confirmed that WT hSVCT1 (approximately 70-100 kDa) is glycosylated and site-directed mutagenesis of the three putative N-glycosylation sites, Asn138, Asn144, Asn230, demonstrated that mutants N138Q and N144Q were glycosylated (approximately 68-90 kDa) with only 31-65% of WT l-ascorbic acid (AA) uptake while the glycosylation profile of N230Q remained unaltered (approximately 98% of WT activity).
19379732	3	59	theme	sites	593:597	arg1	mutagenesis					543:553	site-directed mutagenesis	529:553	site-directed mutagenesis of the three putative N-glycosylation sites	529:597	PNGase F treatment confirmed that WT hSVCT1 (approximately 70-100 kDa) is glycosylated and site-directed mutagenesis of the three putative N-glycosylation sites, Asn138, Asn144, Asn230, demonstrated that mutants N138Q and N144Q were glycosylated (approximately 68-90 kDa) with only 31-65% of WT l-ascorbic acid (AA) uptake while the glycosylation profile of N230Q remained unaltered (approximately 98% of WT activity).
19379732	3	60	dep	and	525:527	arg1	Asn138					600:605	Asn138	600:605	Asn138	600:605	PNGase F treatment confirmed that WT hSVCT1 (approximately 70-100 kDa) is glycosylated and site-directed mutagenesis of the three putative N-glycosylation sites, Asn138, Asn144, Asn230, demonstrated that mutants N138Q and N144Q were glycosylated (approximately 68-90 kDa) with only 31-65% of WT l-ascorbic acid (AA) uptake while the glycosylation profile of N230Q remained unaltered (approximately 98% of WT activity).
19379732	3	60	dep	and	525:527	arg1	mutagenesis					543:553	site-directed mutagenesis	529:553	site-directed mutagenesis of the three putative N-glycosylation sites	529:597	PNGase F treatment confirmed that WT hSVCT1 (approximately 70-100 kDa) is glycosylated and site-directed mutagenesis of the three putative N-glycosylation sites, Asn138, Asn144, Asn230, demonstrated that mutants N138Q and N144Q were glycosylated (approximately 68-90 kDa) with only 31-65% of WT l-ascorbic acid (AA) uptake while the glycosylation profile of N230Q remained unaltered (approximately 98% of WT activity).
19379732	3	60	dep	and	525:527	arg1	Asn230					616:621	Asn230	616:621	Asn230	616:621	PNGase F treatment confirmed that WT hSVCT1 (approximately 70-100 kDa) is glycosylated and site-directed mutagenesis of the three putative N-glycosylation sites, Asn138, Asn144, Asn230, demonstrated that mutants N138Q and N144Q were glycosylated (approximately 68-90 kDa) with only 31-65% of WT l-ascorbic acid (AA) uptake while the glycosylation profile of N230Q remained unaltered (approximately 98% of WT activity).
19379732	3	60	dep	and	525:527	arg1	demonstrated					624:635	demonstrated	624:635	demonstrated that mutants N138Q and N144Q were glycosylated (approximately 68-90 kDa) with only 31-65% of WT l-ascorbic acid (AA) uptake while the glycosylation profile of N230Q remained unaltered (approximately 98% of WT activity)	624:854	PNGase F treatment confirmed that WT hSVCT1 (approximately 70-100 kDa) is glycosylated and site-directed mutagenesis of the three putative N-glycosylation sites, Asn138, Asn144, Asn230, demonstrated that mutants N138Q and N144Q were glycosylated (approximately 68-90 kDa) with only 31-65% of WT l-ascorbic acid (AA) uptake while the glycosylation profile of N230Q remained unaltered (approximately 98% of WT activity).
19379732	3	60	dep	and	525:527	arg1	Asn144					608:613	Asn144	608:613	Asn144	608:613	PNGase F treatment confirmed that WT hSVCT1 (approximately 70-100 kDa) is glycosylated and site-directed mutagenesis of the three putative N-glycosylation sites, Asn138, Asn144, Asn230, demonstrated that mutants N138Q and N144Q were glycosylated (approximately 68-90 kDa) with only 31-65% of WT l-ascorbic acid (AA) uptake while the glycosylation profile of N230Q remained unaltered (approximately 98% of WT activity).
19379732	4	61	theme	detectable	913:922	arg1	expression					933:942	barely detectable membrane expression	906:942	barely detectable membrane expression at approximately 65 kDa	906:966	However, the N138Q/N144Q double mutant displayed barely detectable membrane expression at approximately 65 kDa, no apparent glycosylation and minimal AA uptake (<10%) with no discernible improvement in expression or activity when cultured at 28 degrees C or 37 degrees C. Marker protein immunocytochemistry with N138Q/N144Q identified intracellular aggregates with hSVCT1 localised at the nuclear membrane but absent at the plasma membrane thus implicating its role as a possible intracellular transporter and suggesting N-glycosylation is required for hSVCT1 membrane targeting.
19379732	3	62	gly	glycosylated	671:682	arg1	mutants					642:648	mutants	642:648	mutants N138Q and N144Q	642:664	PNGase F treatment confirmed that WT hSVCT1 (approximately 70-100 kDa) is glycosylated and site-directed mutagenesis of the three putative N-glycosylation sites, Asn138, Asn144, Asn230, demonstrated that mutants N138Q and N144Q were glycosylated (approximately 68-90 kDa) with only 31-65% of WT l-ascorbic acid (AA) uptake while the glycosylation profile of N230Q remained unaltered (approximately 98% of WT activity).
19379732	3	62	gly	glycosylated	671:682	arg1	N144Q					660:664	N144Q	660:664	N144Q	660:664	PNGase F treatment confirmed that WT hSVCT1 (approximately 70-100 kDa) is glycosylated and site-directed mutagenesis of the three putative N-glycosylation sites, Asn138, Asn144, Asn230, demonstrated that mutants N138Q and N144Q were glycosylated (approximately 68-90 kDa) with only 31-65% of WT l-ascorbic acid (AA) uptake while the glycosylation profile of N230Q remained unaltered (approximately 98% of WT activity).
19379732	3	62	gly	glycosylated	671:682	arg1	N138Q					650:654	N138Q	650:654	N138Q	650:654	PNGase F treatment confirmed that WT hSVCT1 (approximately 70-100 kDa) is glycosylated and site-directed mutagenesis of the three putative N-glycosylation sites, Asn138, Asn144, Asn230, demonstrated that mutants N138Q and N144Q were glycosylated (approximately 68-90 kDa) with only 31-65% of WT l-ascorbic acid (AA) uptake while the glycosylation profile of N230Q remained unaltered (approximately 98% of WT activity).
19379732	4	63	theme	protein	1136:1142	arg1	immunocytochemistry					1144:1162	Marker protein immunocytochemistry	1129:1162	Marker protein immunocytochemistry with N138Q/N144Q	1129:1179	However, the N138Q/N144Q double mutant displayed barely detectable membrane expression at approximately 65 kDa, no apparent glycosylation and minimal AA uptake (<10%) with no discernible improvement in expression or activity when cultured at 28 degrees C or 37 degrees C. Marker protein immunocytochemistry with N138Q/N144Q identified intracellular aggregates with hSVCT1 localised at the nuclear membrane but absent at the plasma membrane thus implicating its role as a possible intracellular transporter and suggesting N-glycosylation is required for hSVCT1 membrane targeting.
19379732	2	64	theme	hSVCT1	294:299	arg1	N-					274:275	N-	274:275	N-	274:275	Antibodies to N- and C-termini of hSVCT1 and C-terminus of hSVCT2 identified positive immunofluorescence only after permeabilisation, suggesting these regions are intracellular.
19379732	2	64	theme	hSVCT1	294:299	arg1	C-terminus					305:314	C-terminus	305:314	C-terminus of hSVCT2	305:324	Antibodies to N- and C-termini of hSVCT1 and C-terminus of hSVCT2 identified positive immunofluorescence only after permeabilisation, suggesting these regions are intracellular.
19379732	4	65	theme	membrane	1417:1424	arg1	targeting					1426:1434	hSVCT1 membrane targeting	1410:1434	hSVCT1 membrane targeting	1410:1434	However, the N138Q/N144Q double mutant displayed barely detectable membrane expression at approximately 65 kDa, no apparent glycosylation and minimal AA uptake (<10%) with no discernible improvement in expression or activity when cultured at 28 degrees C or 37 degrees C. Marker protein immunocytochemistry with N138Q/N144Q identified intracellular aggregates with hSVCT1 localised at the nuclear membrane but absent at the plasma membrane thus implicating its role as a possible intracellular transporter and suggesting N-glycosylation is required for hSVCT1 membrane targeting.
19379732	3	66	theme	acid	744:747	arg1	uptake					754:759	WT l-ascorbic acid (AA) uptake	730:759	WT l-ascorbic acid (AA) uptake while the glycosylation profile of N230Q remained unaltered (approximately 98% of WT activity)	730:854	PNGase F treatment confirmed that WT hSVCT1 (approximately 70-100 kDa) is glycosylated and site-directed mutagenesis of the three putative N-glycosylation sites, Asn138, Asn144, Asn230, demonstrated that mutants N138Q and N144Q were glycosylated (approximately 68-90 kDa) with only 31-65% of WT l-ascorbic acid (AA) uptake while the glycosylation profile of N230Q remained unaltered (approximately 98% of WT activity).
19379732	0	67	from	influence	88:96	arg1	targeting					138:146	its intracellular targeting	120:146	its intracellular targeting	120:146	Topological studies of hSVCT1, the human sodium-dependent vitamin C transporter and the influence of N-glycosylation on its intracellular targeting.
19379732	4	68	theme	intracellular	1337:1349	arg1	transporter					1351:1361	a possible intracellular transporter	1326:1361	a possible intracellular transporter	1326:1361	However, the N138Q/N144Q double mutant displayed barely detectable membrane expression at approximately 65 kDa, no apparent glycosylation and minimal AA uptake (<10%) with no discernible improvement in expression or activity when cultured at 28 degrees C or 37 degrees C. Marker protein immunocytochemistry with N138Q/N144Q identified intracellular aggregates with hSVCT1 localised at the nuclear membrane but absent at the plasma membrane thus implicating its role as a possible intracellular transporter and suggesting N-glycosylation is required for hSVCT1 membrane targeting.
19379732	4	68	theme	intracellular	1337:1349	arg1	role					1318:1321	its role	1314:1321	its role	1314:1321	However, the N138Q/N144Q double mutant displayed barely detectable membrane expression at approximately 65 kDa, no apparent glycosylation and minimal AA uptake (<10%) with no discernible improvement in expression or activity when cultured at 28 degrees C or 37 degrees C. Marker protein immunocytochemistry with N138Q/N144Q identified intracellular aggregates with hSVCT1 localised at the nuclear membrane but absent at the plasma membrane thus implicating its role as a possible intracellular transporter and suggesting N-glycosylation is required for hSVCT1 membrane targeting.
19379732	4	69	theme	nuclear	1246:1252	arg1	membrane					1254:1261	the nuclear membrane	1242:1261	the nuclear membrane	1242:1261	However, the N138Q/N144Q double mutant displayed barely detectable membrane expression at approximately 65 kDa, no apparent glycosylation and minimal AA uptake (<10%) with no discernible improvement in expression or activity when cultured at 28 degrees C or 37 degrees C. Marker protein immunocytochemistry with N138Q/N144Q identified intracellular aggregates with hSVCT1 localised at the nuclear membrane but absent at the plasma membrane thus implicating its role as a possible intracellular transporter and suggesting N-glycosylation is required for hSVCT1 membrane targeting.
19379732	3	70	theme	WT	472:473	arg1	kDa					504:506	approximately 70-100 kDa	483:506	approximately 70-100 kDa	483:506	PNGase F treatment confirmed that WT hSVCT1 (approximately 70-100 kDa) is glycosylated and site-directed mutagenesis of the three putative N-glycosylation sites, Asn138, Asn144, Asn230, demonstrated that mutants N138Q and N144Q were glycosylated (approximately 68-90 kDa) with only 31-65% of WT l-ascorbic acid (AA) uptake while the glycosylation profile of N230Q remained unaltered (approximately 98% of WT activity).
19379732	3	70	theme	WT	472:473	arg1	hSVCT1					475:480	WT hSVCT1	472:480	WT hSVCT1 (approximately 70-100 kDa)	472:507	PNGase F treatment confirmed that WT hSVCT1 (approximately 70-100 kDa) is glycosylated and site-directed mutagenesis of the three putative N-glycosylation sites, Asn138, Asn144, Asn230, demonstrated that mutants N138Q and N144Q were glycosylated (approximately 68-90 kDa) with only 31-65% of WT l-ascorbic acid (AA) uptake while the glycosylation profile of N230Q remained unaltered (approximately 98% of WT activity).
19379732	0	71	theme	C	66:66	arg1	transporter					68:78	the human sodium-dependent vitamin C transporter	31:78	the human sodium-dependent vitamin C transporter	31:78	Topological studies of hSVCT1, the human sodium-dependent vitamin C transporter and the influence of N-glycosylation on its intracellular targeting.
19379732	0	71	theme	C	66:66	arg1	hSVCT1					23:28	hSVCT1	23:28	hSVCT1	23:28	Topological studies of hSVCT1, the human sodium-dependent vitamin C transporter and the influence of N-glycosylation on its intracellular targeting.
19379732	5	72	from	Lys242	1443:1448	arg1	loop					1483:1486	the same putative hydrophilic loop	1453:1486	the same putative hydrophilic loop as Asn230	1453:1496	Also, Lys242 on the same putative hydrophilic loop as Asn230 after biotinylation was inaccessible from the extracellular side when analysed by MALDI-TOF MS. A new hSVCT1 secondary structure model supporting these findings is proposed.
19379732	2	73	theme	positive	337:344	arg1	immunofluorescence					346:363	positive immunofluorescence	337:363	positive immunofluorescence	337:363	Antibodies to N- and C-termini of hSVCT1 and C-terminus of hSVCT2 identified positive immunofluorescence only after permeabilisation, suggesting these regions are intracellular.
19379732	4	74	from	improvement	1044:1054	arg1	activity					1073:1080	activity	1073:1080	activity	1073:1080	However, the N138Q/N144Q double mutant displayed barely detectable membrane expression at approximately 65 kDa, no apparent glycosylation and minimal AA uptake (<10%) with no discernible improvement in expression or activity when cultured at 28 degrees C or 37 degrees C. Marker protein immunocytochemistry with N138Q/N144Q identified intracellular aggregates with hSVCT1 localised at the nuclear membrane but absent at the plasma membrane thus implicating its role as a possible intracellular transporter and suggesting N-glycosylation is required for hSVCT1 membrane targeting.
19379732	4	74	from	improvement	1044:1054	arg1	expression					1059:1068	expression	1059:1068	expression	1059:1068	However, the N138Q/N144Q double mutant displayed barely detectable membrane expression at approximately 65 kDa, no apparent glycosylation and minimal AA uptake (<10%) with no discernible improvement in expression or activity when cultured at 28 degrees C or 37 degrees C. Marker protein immunocytochemistry with N138Q/N144Q identified intracellular aggregates with hSVCT1 localised at the nuclear membrane but absent at the plasma membrane thus implicating its role as a possible intracellular transporter and suggesting N-glycosylation is required for hSVCT1 membrane targeting.
19379732	4	75	theme	membrane	924:931	arg1	expression					933:942	barely detectable membrane expression	906:942	barely detectable membrane expression at approximately 65 kDa	906:966	However, the N138Q/N144Q double mutant displayed barely detectable membrane expression at approximately 65 kDa, no apparent glycosylation and minimal AA uptake (<10%) with no discernible improvement in expression or activity when cultured at 28 degrees C or 37 degrees C. Marker protein immunocytochemistry with N138Q/N144Q identified intracellular aggregates with hSVCT1 localised at the nuclear membrane but absent at the plasma membrane thus implicating its role as a possible intracellular transporter and suggesting N-glycosylation is required for hSVCT1 membrane targeting.
19379732	0	76	theme	vitamin	58:64	arg1	transporter					68:78	the human sodium-dependent vitamin C transporter	31:78	the human sodium-dependent vitamin C transporter	31:78	Topological studies of hSVCT1, the human sodium-dependent vitamin C transporter and the influence of N-glycosylation on its intracellular targeting.
19379732	0	76	theme	vitamin	58:64	arg1	hSVCT1					23:28	hSVCT1	23:28	hSVCT1	23:28	Topological studies of hSVCT1, the human sodium-dependent vitamin C transporter and the influence of N-glycosylation on its intracellular targeting.
19379732	3	77	dep	mutants	642:648	arg1	mutants					642:648	mutants	642:648	mutants N138Q and N144Q	642:664	PNGase F treatment confirmed that WT hSVCT1 (approximately 70-100 kDa) is glycosylated and site-directed mutagenesis of the three putative N-glycosylation sites, Asn138, Asn144, Asn230, demonstrated that mutants N138Q and N144Q were glycosylated (approximately 68-90 kDa) with only 31-65% of WT l-ascorbic acid (AA) uptake while the glycosylation profile of N230Q remained unaltered (approximately 98% of WT activity).
19379732	3	77	dep	mutants	642:648	arg1	N144Q					660:664	N144Q	660:664	N144Q	660:664	PNGase F treatment confirmed that WT hSVCT1 (approximately 70-100 kDa) is glycosylated and site-directed mutagenesis of the three putative N-glycosylation sites, Asn138, Asn144, Asn230, demonstrated that mutants N138Q and N144Q were glycosylated (approximately 68-90 kDa) with only 31-65% of WT l-ascorbic acid (AA) uptake while the glycosylation profile of N230Q remained unaltered (approximately 98% of WT activity).
19379732	3	77	dep	mutants	642:648	arg1	N138Q					650:654	N138Q	650:654	N138Q	650:654	PNGase F treatment confirmed that WT hSVCT1 (approximately 70-100 kDa) is glycosylated and site-directed mutagenesis of the three putative N-glycosylation sites, Asn138, Asn144, Asn230, demonstrated that mutants N138Q and N144Q were glycosylated (approximately 68-90 kDa) with only 31-65% of WT l-ascorbic acid (AA) uptake while the glycosylation profile of N230Q remained unaltered (approximately 98% of WT activity).
19379732	5	78	theme	structure	1617:1625	arg1	model					1627:1631	A new hSVCT1 secondary structure model	1594:1631	A new hSVCT1 secondary structure model supporting these findings	1594:1657	Also, Lys242 on the same putative hydrophilic loop as Asn230 after biotinylation was inaccessible from the extracellular side when analysed by MALDI-TOF MS. A new hSVCT1 secondary structure model supporting these findings is proposed.
19379732	3	79	theme	uptake	754:759	arg1	%					725:725	only 31-65%	715:725	only 31-65% of WT l-ascorbic acid (AA) uptake while the glycosylation profile of N230Q remained unaltered (approximately 98% of WT activity)	715:854	PNGase F treatment confirmed that WT hSVCT1 (approximately 70-100 kDa) is glycosylated and site-directed mutagenesis of the three putative N-glycosylation sites, Asn138, Asn144, Asn230, demonstrated that mutants N138Q and N144Q were glycosylated (approximately 68-90 kDa) with only 31-65% of WT l-ascorbic acid (AA) uptake while the glycosylation profile of N230Q remained unaltered (approximately 98% of WT activity).
19379732	3	79	theme	uptake	754:759	arg1	uptake					754:759	WT l-ascorbic acid (AA) uptake	730:759	WT l-ascorbic acid (AA) uptake while the glycosylation profile of N230Q remained unaltered (approximately 98% of WT activity)	730:854	PNGase F treatment confirmed that WT hSVCT1 (approximately 70-100 kDa) is glycosylated and site-directed mutagenesis of the three putative N-glycosylation sites, Asn138, Asn144, Asn230, demonstrated that mutants N138Q and N144Q were glycosylated (approximately 68-90 kDa) with only 31-65% of WT l-ascorbic acid (AA) uptake while the glycosylation profile of N230Q remained unaltered (approximately 98% of WT activity).
22067045	5	0	from	distribution	579:590	arg1	site					619:622	each site	614:622	each site within the context of adjacent sites in this clustered region	614:684	The range and distribution of O-glycan chains at each site within the context of adjacent sites in this clustered region create a complex heterogeneity of surface epitopes that is incompletely defined.
22067045	5	1	from	range	569:573	arg1	site					619:622	each site	614:622	each site within the context of adjacent sites in this clustered region	614:684	The range and distribution of O-glycan chains at each site within the context of adjacent sites in this clustered region create a complex heterogeneity of surface epitopes that is incompletely defined.
22067045	5	2	theme	surface	720:726	arg1	epitopes					728:735	surface epitopes	720:735	surface epitopes	720:735	The range and distribution of O-glycan chains at each site within the context of adjacent sites in this clustered region create a complex heterogeneity of surface epitopes that is incompletely defined.
22067045	5	3	gly	heterogeneity	703:715	arg1	epitopes					728:735	surface epitopes	720:735	surface epitopes	720:735	The range and distribution of O-glycan chains at each site within the context of adjacent sites in this clustered region create a complex heterogeneity of surface epitopes that is incompletely defined.
22067045	8	4	from	present	1275:1281	arg1	protein					1314:1320	a model IgA1 (Mce1) myeloma protein	1286:1320	a model IgA1 (Mce1) myeloma protein	1286:1320	These isomers are present in a model IgA1 (Mce1) myeloma protein and occur naturally in normal human serum IgA1.
22067045	9	5	theme	positional	1462:1471	arg1	isomers					1473:1479	the predominant positional isomers	1446:1479	the predominant positional isomers	1446:1479	Variable O-glycan chains attached to Ser(230), Thr(233) or Thr(236) produce the predominant positional isomers, including O-glycans composed of a single GalNAc residue.
22067045	9	5	theme	positional	1462:1471	arg1	O-glycans					1492:1500	O-glycans	1492:1500	O-glycans composed of a single GalNAc residue	1492:1536	Variable O-glycan chains attached to Ser(230), Thr(233) or Thr(236) produce the predominant positional isomers, including O-glycans composed of a single GalNAc residue.
22067045	7	6	theme	glycan	1240:1245	arg1	sites					1233:1237	individual sites	1222:1237	individual sites (glycan isomers)	1222:1254	Here, we report the identification and elucidation of IgA1 O-glycopeptide structural isomers that occur based on amino acid position of the attached glycans (positional isomers) and the structure of the O-glycan chains at individual sites (glycan isomers).
22067045	7	6	theme	glycan	1240:1245	arg1	isomers					1247:1253	glycan isomers	1240:1253	glycan isomers	1240:1253	Here, we report the identification and elucidation of IgA1 O-glycopeptide structural isomers that occur based on amino acid position of the attached glycans (positional isomers) and the structure of the O-glycan chains at individual sites (glycan isomers).
22067045	10	7	theme	single-site	1653:1663	arg1	heterogeneity					1665:1677	the single-site heterogeneity	1649:1677	the single-site heterogeneity for all O-glycan sites in a single sample	1649:1719	These findings represent the first definitive identification of structural isomeric IgA1 O-glycoforms, define the single-site heterogeneity for all O-glycan sites in a single sample, and have implications for defining epitopes based on clustered O-glycan variability.
22067045	6	8	theme	heterogeneity	821:833	arg1	analysis					795:802	the analysis	791:802	the analysis of IgA1 O-glycan heterogeneity by use of high resolution LC-MS and electron capture dissociation tandem MS to unambiguously localize all amino acid attachment sites in IgA1 (Ale) myeloma protein	791:997	We previously described the analysis of IgA1 O-glycan heterogeneity by use of high resolution LC-MS and electron capture dissociation tandem MS to unambiguously localize all amino acid attachment sites in IgA1 (Ale) myeloma protein.
22067045	3	9	theme	major	234:238	arg1	difference					251:260	The major structural difference	230:260	The major structural difference between these two subclasses	230:289	The major structural difference between these two subclasses is the presence of nine potential sites of O-glycosylation in the hinge region between the first and second constant region domains of the heavy chain.
22067045	3	9	theme	major	234:238	arg1	presence					298:305	the presence	294:305	the presence of nine potential sites of O-glycosylation in the hinge region between the first and second constant region domains of the heavy chain	294:440	The major structural difference between these two subclasses is the presence of nine potential sites of O-glycosylation in the hinge region between the first and second constant region domains of the heavy chain.
22067045	10	10	contain	have	1726:1729	arg1	findings					1545:1552	These findings	1539:1552	These findings	1539:1552	These findings represent the first definitive identification of structural isomeric IgA1 O-glycoforms, define the single-site heterogeneity for all O-glycan sites in a single sample, and have implications for defining epitopes based on clustered O-glycan variability.
22067045	10	10	contain	have	1726:1729	arg2	implications					1731:1742	implications	1731:1742	implications for defining epitopes based on clustered O-glycan variability	1731:1804	These findings represent the first definitive identification of structural isomeric IgA1 O-glycoforms, define the single-site heterogeneity for all O-glycan sites in a single sample, and have implications for defining epitopes based on clustered O-glycan variability.
22067045	10	11	theme	O-glycan	1785:1792	arg1	variability					1794:1804	clustered O-glycan variability	1775:1804	clustered O-glycan variability	1775:1804	These findings represent the first definitive identification of structural isomeric IgA1 O-glycoforms, define the single-site heterogeneity for all O-glycan sites in a single sample, and have implications for defining epitopes based on clustered O-glycan variability.
22067045	6	12	theme	IgA1	807:810	arg1	heterogeneity					821:833	IgA1 O-glycan heterogeneity	807:833	IgA1 O-glycan heterogeneity	807:833	We previously described the analysis of IgA1 O-glycan heterogeneity by use of high resolution LC-MS and electron capture dissociation tandem MS to unambiguously localize all amino acid attachment sites in IgA1 (Ale) myeloma protein.
22067045	8	13	theme	model	1288:1292	arg1	protein					1314:1320	a model IgA1 (Mce1) myeloma protein	1286:1320	a model IgA1 (Mce1) myeloma protein	1286:1320	These isomers are present in a model IgA1 (Mce1) myeloma protein and occur naturally in normal human serum IgA1.
22067045	10	14	theme	first	1568:1572	arg1	identification					1585:1598	the first definitive identification	1564:1598	the first definitive identification of structural isomeric IgA1 O-glycoforms	1564:1639	These findings represent the first definitive identification of structural isomeric IgA1 O-glycoforms, define the single-site heterogeneity for all O-glycan sites in a single sample, and have implications for defining epitopes based on clustered O-glycan variability.
22067045	7	15	theme	O-glycan	1203:1210	arg1	chains					1212:1217	the O-glycan chains	1199:1217	the O-glycan chains	1199:1217	Here, we report the identification and elucidation of IgA1 O-glycopeptide structural isomers that occur based on amino acid position of the attached glycans (positional isomers) and the structure of the O-glycan chains at individual sites (glycan isomers).
22067045	10	16	theme	IgA1	1623:1626	arg1	O-glycoforms					1628:1639	structural isomeric IgA1 O-glycoforms	1603:1639	structural isomeric IgA1 O-glycoforms	1603:1639	These findings represent the first definitive identification of structural isomeric IgA1 O-glycoforms, define the single-site heterogeneity for all O-glycan sites in a single sample, and have implications for defining epitopes based on clustered O-glycan variability.
22067045	1	17	theme	important	128:136	arg1	role					138:141	an important role	125:141	an important role	125:141	IgA is the most abundantly produced antibody and plays an important role in the mucosal immune system.
22067045	6	18	theme	dissociation	888:899	arg1	use					838:840	use	838:840	use of high resolution LC-MS and electron capture dissociation tandem MS to unambiguously localize all amino acid attachment sites in IgA1 (Ale) myeloma protein	838:997	We previously described the analysis of IgA1 O-glycan heterogeneity by use of high resolution LC-MS and electron capture dissociation tandem MS to unambiguously localize all amino acid attachment sites in IgA1 (Ale) myeloma protein.
22067045	9	19	theme	single	1516:1521	arg1	residue					1530:1536	a single GalNAc residue	1514:1536	a single GalNAc residue	1514:1536	Variable O-glycan chains attached to Ser(230), Thr(233) or Thr(236) produce the predominant positional isomers, including O-glycans composed of a single GalNAc residue.
22067045	4	20	theme	O-glycan	544:551	arg1	attachment					553:562	O-glycan attachment	544:562	O-glycan attachment	544:562	Thr(225), Thr(228), Ser(230), Ser(232) and Thr(236) have been identified as the predominant sites of O-glycan attachment.
22067045	8	21	from	protein	1314:1320	arg1	present					1275:1281	present	1275:1281	present	1275:1281	These isomers are present in a model IgA1 (Mce1) myeloma protein and occur naturally in normal human serum IgA1.
22067045	6	22	theme	electron	871:878	arg1	dissociation					888:899	electron capture dissociation	871:899	electron capture dissociation	871:899	We previously described the analysis of IgA1 O-glycan heterogeneity by use of high resolution LC-MS and electron capture dissociation tandem MS to unambiguously localize all amino acid attachment sites in IgA1 (Ale) myeloma protein.
22067045	7	23	theme	isomers	1085:1091	arg1	elucidation					1039:1049	elucidation	1039:1049	elucidation	1039:1049	Here, we report the identification and elucidation of IgA1 O-glycopeptide structural isomers that occur based on amino acid position of the attached glycans (positional isomers) and the structure of the O-glycan chains at individual sites (glycan isomers).
22067045	7	23	theme	isomers	1085:1091	arg1	identification					1020:1033	identification	1020:1033	identification	1020:1033	Here, we report the identification and elucidation of IgA1 O-glycopeptide structural isomers that occur based on amino acid position of the attached glycans (positional isomers) and the structure of the O-glycan chains at individual sites (glycan isomers).
22067045	5	24	from	context	635:641	arg1	region					679:684	this clustered region	664:684	this clustered region	664:684	The range and distribution of O-glycan chains at each site within the context of adjacent sites in this clustered region create a complex heterogeneity of surface epitopes that is incompletely defined.
22067045	1	25	theme	mucosal	150:156	arg1	system					165:170	the mucosal immune system	146:170	the mucosal immune system	146:170	IgA is the most abundantly produced antibody and plays an important role in the mucosal immune system.
22067045	6	26	theme	LC-MS	861:865	arg1	use					838:840	use	838:840	use of high resolution LC-MS and electron capture dissociation tandem MS to unambiguously localize all amino acid attachment sites in IgA1 (Ale) myeloma protein	838:997	We previously described the analysis of IgA1 O-glycan heterogeneity by use of high resolution LC-MS and electron capture dissociation tandem MS to unambiguously localize all amino acid attachment sites in IgA1 (Ale) myeloma protein.
22067045	6	27	dep	LC-MS	861:865	arg1	MS					908:909	tandem MS	901:909	tandem MS	901:909	We previously described the analysis of IgA1 O-glycan heterogeneity by use of high resolution LC-MS and electron capture dissociation tandem MS to unambiguously localize all amino acid attachment sites in IgA1 (Ale) myeloma protein.
22067045	7	28	dep	identification	1020:1033	arg1	the					1016:1018	the	1016:1018	the	1016:1018	Here, we report the identification and elucidation of IgA1 O-glycopeptide structural isomers that occur based on amino acid position of the attached glycans (positional isomers) and the structure of the O-glycan chains at individual sites (glycan isomers).
22067045	7	29	gly	O-glycopeptide	1059:1072	arg2	O-glycopeptide					1059:1072	IgA1 O-glycopeptide structural isomers	1054:1091	IgA1 O-glycopeptide structural isomers that occur based on amino acid position of the attached glycans (positional isomers) and the structure of the O-glycan chains at individual sites (glycan isomers)	1054:1254	Here, we report the identification and elucidation of IgA1 O-glycopeptide structural isomers that occur based on amino acid position of the attached glycans (positional isomers) and the structure of the O-glycan chains at individual sites (glycan isomers).
22067045	7	30	theme	O-glycopeptide	1059:1072	arg1	isomers					1085:1091	IgA1 O-glycopeptide structural isomers	1054:1091	IgA1 O-glycopeptide structural isomers that occur based on amino acid position of the attached glycans (positional isomers) and the structure of the O-glycan chains at individual sites (glycan isomers)	1054:1254	Here, we report the identification and elucidation of IgA1 O-glycopeptide structural isomers that occur based on amino acid position of the attached glycans (positional isomers) and the structure of the O-glycan chains at individual sites (glycan isomers).
22067045	6	31	theme	high	845:848	arg1	LC-MS					861:865	high resolution LC-MS	845:865	high resolution LC-MS	845:865	We previously described the analysis of IgA1 O-glycan heterogeneity by use of high resolution LC-MS and electron capture dissociation tandem MS to unambiguously localize all amino acid attachment sites in IgA1 (Ale) myeloma protein.
22067045	3	32	theme	potential	315:323	arg1	sites					325:329	nine potential sites	310:329	nine potential sites of O-glycosylation	310:348	The major structural difference between these two subclasses is the presence of nine potential sites of O-glycosylation in the hinge region between the first and second constant region domains of the heavy chain.
22067045	3	32	theme	potential	315:323	arg1	O-glycosylation					334:348	O-glycosylation	334:348	O-glycosylation	334:348	The major structural difference between these two subclasses is the presence of nine potential sites of O-glycosylation in the hinge region between the first and second constant region domains of the heavy chain.
22067045	3	33	theme	region	408:413	arg1	domains					415:421	the first and second constant region domains	378:421	the first and second constant region domains of the heavy chain	378:440	The major structural difference between these two subclasses is the presence of nine potential sites of O-glycosylation in the hinge region between the first and second constant region domains of the heavy chain.
22067045	3	33	theme	region	408:413	arg1	chain					436:440	the heavy chain	426:440	the heavy chain	426:440	The major structural difference between these two subclasses is the presence of nine potential sites of O-glycosylation in the hinge region between the first and second constant region domains of the heavy chain.
22067045	9	34	theme	O-glycan	1379:1386	arg1	chains					1388:1393	Variable O-glycan chains	1370:1393	Variable O-glycan chains attached to Ser(230), Thr(233) or Thr(236)	1370:1436	Variable O-glycan chains attached to Ser(230), Thr(233) or Thr(236) produce the predominant positional isomers, including O-glycans composed of a single GalNAc residue.
22067045	6	35	theme	acid	947:950	arg1	sites					963:967	all amino acid attachment sites	937:967	all amino acid attachment sites in IgA1 (Ale) myeloma protein	937:997	We previously described the analysis of IgA1 O-glycan heterogeneity by use of high resolution LC-MS and electron capture dissociation tandem MS to unambiguously localize all amino acid attachment sites in IgA1 (Ale) myeloma protein.
22067045	3	36	theme	hinge	357:361	arg1	region					363:368	the hinge region	353:368	the hinge region between the first and second constant region domains of the heavy chain	353:440	The major structural difference between these two subclasses is the presence of nine potential sites of O-glycosylation in the hinge region between the first and second constant region domains of the heavy chain.
22067045	8	37	theme	human	1352:1356	arg1	IgA1					1364:1367	normal human serum IgA1	1345:1367	normal human serum IgA1	1345:1367	These isomers are present in a model IgA1 (Mce1) myeloma protein and occur naturally in normal human serum IgA1.
22067045	3	38	theme	second	392:397	arg1	domains					415:421	the first and second constant region domains	378:421	the first and second constant region domains of the heavy chain	378:440	The major structural difference between these two subclasses is the presence of nine potential sites of O-glycosylation in the hinge region between the first and second constant region domains of the heavy chain.
22067045	3	38	theme	second	392:397	arg1	chain					436:440	the heavy chain	426:440	the heavy chain	426:440	The major structural difference between these two subclasses is the presence of nine potential sites of O-glycosylation in the hinge region between the first and second constant region domains of the heavy chain.
22067045	3	39	theme	heavy	430:434	arg1	chain					436:440	the heavy chain	426:440	the heavy chain	426:440	The major structural difference between these two subclasses is the presence of nine potential sites of O-glycosylation in the hinge region between the first and second constant region domains of the heavy chain.
22067045	0	40	theme	structural	20:29	arg1	isomers					31:37	Naturally occurring structural isomers	0:37	Naturally occurring structural isomers in serum IgA1 o-glycosylation	0:67	Naturally occurring structural isomers in serum IgA1 o-glycosylation.
22067045	7	41	from	sites	1233:1237	arg1	position					1124:1131	amino acid position	1113:1131	amino acid position of the attached glycans (positional isomers)	1113:1176	Here, we report the identification and elucidation of IgA1 O-glycopeptide structural isomers that occur based on amino acid position of the attached glycans (positional isomers) and the structure of the O-glycan chains at individual sites (glycan isomers).
22067045	7	41	from	sites	1233:1237	arg1	structure					1186:1194	the structure	1182:1194	the structure of the O-glycan chains at individual sites (glycan isomers)	1182:1254	Here, we report the identification and elucidation of IgA1 O-glycopeptide structural isomers that occur based on amino acid position of the attached glycans (positional isomers) and the structure of the O-glycan chains at individual sites (glycan isomers).
22067045	3	42	theme	first	382:386	arg1	domains					415:421	the first and second constant region domains	378:421	the first and second constant region domains of the heavy chain	378:440	The major structural difference between these two subclasses is the presence of nine potential sites of O-glycosylation in the hinge region between the first and second constant region domains of the heavy chain.
22067045	3	42	theme	first	382:386	arg1	chain					436:440	the heavy chain	426:440	the heavy chain	426:440	The major structural difference between these two subclasses is the presence of nine potential sites of O-glycosylation in the hinge region between the first and second constant region domains of the heavy chain.
22067045	8	43	attach	present	1275:1281	arg2	isomers					1263:1269	These isomers	1257:1269	These isomers	1257:1269	These isomers are present in a model IgA1 (Mce1) myeloma protein and occur naturally in normal human serum IgA1.
22067045	8	43	attach	present	1275:1281	arg1	protein					1314:1320	a model IgA1 (Mce1) myeloma protein	1286:1320	a model IgA1 (Mce1) myeloma protein	1286:1320	These isomers are present in a model IgA1 (Mce1) myeloma protein and occur naturally in normal human serum IgA1.
22067045	6	44	theme	myeloma	983:989	arg1	protein					991:997	IgA1 (Ale) myeloma protein	972:997	IgA1 (Ale) myeloma protein	972:997	We previously described the analysis of IgA1 O-glycan heterogeneity by use of high resolution LC-MS and electron capture dissociation tandem MS to unambiguously localize all amino acid attachment sites in IgA1 (Ale) myeloma protein.
22067045	10	45	theme	structural	1603:1612	arg1	O-glycoforms					1628:1639	structural isomeric IgA1 O-glycoforms	1603:1639	structural isomeric IgA1 O-glycoforms	1603:1639	These findings represent the first definitive identification of structural isomeric IgA1 O-glycoforms, define the single-site heterogeneity for all O-glycan sites in a single sample, and have implications for defining epitopes based on clustered O-glycan variability.
22067045	6	46	theme	Ale	978:980	arg1	protein					991:997	IgA1 (Ale) myeloma protein	972:997	IgA1 (Ale) myeloma protein	972:997	We previously described the analysis of IgA1 O-glycan heterogeneity by use of high resolution LC-MS and electron capture dissociation tandem MS to unambiguously localize all amino acid attachment sites in IgA1 (Ale) myeloma protein.
22067045	6	47	from	sites	963:967	arg1	protein					991:997	IgA1 (Ale) myeloma protein	972:997	IgA1 (Ale) myeloma protein	972:997	We previously described the analysis of IgA1 O-glycan heterogeneity by use of high resolution LC-MS and electron capture dissociation tandem MS to unambiguously localize all amino acid attachment sites in IgA1 (Ale) myeloma protein.
22067045	6	48	theme	IgA1	972:975	arg1	protein					991:997	IgA1 (Ale) myeloma protein	972:997	IgA1 (Ale) myeloma protein	972:997	We previously described the analysis of IgA1 O-glycan heterogeneity by use of high resolution LC-MS and electron capture dissociation tandem MS to unambiguously localize all amino acid attachment sites in IgA1 (Ale) myeloma protein.
22067045	9	49	attach	attached	1395:1402	arg1	Thr					1429:1431	Thr	1429:1431	Thr(236)	1429:1436	Variable O-glycan chains attached to Ser(230), Thr(233) or Thr(236) produce the predominant positional isomers, including O-glycans composed of a single GalNAc residue.
22067045	9	49	attach	attached	1395:1402	arg1	236					1433:1435	236	1433:1435	236	1433:1435	Variable O-glycan chains attached to Ser(230), Thr(233) or Thr(236) produce the predominant positional isomers, including O-glycans composed of a single GalNAc residue.
22067045	9	49	attach	attached	1395:1402	arg1	Thr					1417:1419	Thr(233)	1417:1424	Thr(233)	1417:1424	Variable O-glycan chains attached to Ser(230), Thr(233) or Thr(236) produce the predominant positional isomers, including O-glycans composed of a single GalNAc residue.
22067045	9	49	attach	attached	1395:1402	arg1	Ser					1407:1409	Ser	1407:1409	Ser(230)	1407:1414	Variable O-glycan chains attached to Ser(230), Thr(233) or Thr(236) produce the predominant positional isomers, including O-glycans composed of a single GalNAc residue.
22067045	9	49	attach	attached	1395:1402	arg2	chains					1388:1393	Variable O-glycan chains	1370:1393	Variable O-glycan chains attached to Ser(230), Thr(233) or Thr(236)	1370:1436	Variable O-glycan chains attached to Ser(230), Thr(233) or Thr(236) produce the predominant positional isomers, including O-glycans composed of a single GalNAc residue.
22067045	9	49	attach	attached	1395:1402	arg1	230					1411:1413	230	1411:1413	230	1411:1413	Variable O-glycan chains attached to Ser(230), Thr(233) or Thr(236) produce the predominant positional isomers, including O-glycans composed of a single GalNAc residue.
22067045	1	50	theme	immune	158:163	arg1	system					165:170	the mucosal immune system	146:170	the mucosal immune system	146:170	IgA is the most abundantly produced antibody and plays an important role in the mucosal immune system.
22067045	5	51	theme	sites	655:659	arg1	context					635:641	the context	631:641	the context of adjacent sites in this clustered region	631:684	The range and distribution of O-glycan chains at each site within the context of adjacent sites in this clustered region create a complex heterogeneity of surface epitopes that is incompletely defined.
22067045	5	52	theme	epitopes	728:735	arg1	heterogeneity					703:715	a complex heterogeneity	693:715	a complex heterogeneity of surface epitopes that is incompletely defined	693:764	The range and distribution of O-glycan chains at each site within the context of adjacent sites in this clustered region create a complex heterogeneity of surface epitopes that is incompletely defined.
22067045	10	53	from	sites	1696:1700	arg1	sample					1714:1719	a single sample	1705:1719	a single sample	1705:1719	These findings represent the first definitive identification of structural isomeric IgA1 O-glycoforms, define the single-site heterogeneity for all O-glycan sites in a single sample, and have implications for defining epitopes based on clustered O-glycan variability.
22067045	9	54	theme	predominant	1450:1460	arg1	isomers					1473:1479	the predominant positional isomers	1446:1479	the predominant positional isomers	1446:1479	Variable O-glycan chains attached to Ser(230), Thr(233) or Thr(236) produce the predominant positional isomers, including O-glycans composed of a single GalNAc residue.
22067045	9	54	theme	predominant	1450:1460	arg1	O-glycans					1492:1500	O-glycans	1492:1500	O-glycans composed of a single GalNAc residue	1492:1536	Variable O-glycan chains attached to Ser(230), Thr(233) or Thr(236) produce the predominant positional isomers, including O-glycans composed of a single GalNAc residue.
22067045	0	55	theme	IgA1	48:51	arg1	o-glycosylation					53:67	serum IgA1 o-glycosylation	42:67	serum IgA1 o-glycosylation	42:67	Naturally occurring structural isomers in serum IgA1 o-glycosylation.
22067045	4	56	theme	predominant	523:533	arg1	Thr					453:455	Thr(228)	453:460	Thr(228)	453:460	Thr(225), Thr(228), Ser(230), Ser(232) and Thr(236) have been identified as the predominant sites of O-glycan attachment.
22067045	4	56	theme	predominant	523:533	arg1	Thr					443:445	Thr	443:445	Thr(225)	443:450	Thr(225), Thr(228), Ser(230), Ser(232) and Thr(236) have been identified as the predominant sites of O-glycan attachment.
22067045	4	56	theme	predominant	523:533	arg1	attachment					553:562	O-glycan attachment	544:562	O-glycan attachment	544:562	Thr(225), Thr(228), Ser(230), Ser(232) and Thr(236) have been identified as the predominant sites of O-glycan attachment.
22067045	4	56	theme	predominant	523:533	arg1	Thr					486:488	Thr	486:488	Thr(236)	486:493	Thr(225), Thr(228), Ser(230), Ser(232) and Thr(236) have been identified as the predominant sites of O-glycan attachment.
22067045	4	56	theme	predominant	523:533	arg1	Ser					473:475	Ser(232)	473:480	Ser(232)	473:480	Thr(225), Thr(228), Ser(230), Ser(232) and Thr(236) have been identified as the predominant sites of O-glycan attachment.
22067045	4	56	theme	predominant	523:533	arg1	Ser					463:465	Ser(230)	463:470	Ser(230)	463:470	Thr(225), Thr(228), Ser(230), Ser(232) and Thr(236) have been identified as the predominant sites of O-glycan attachment.
22067045	4	56	theme	predominant	523:533	arg1	sites					535:539	the predominant sites	519:539	the predominant sites of O-glycan attachment	519:562	Thr(225), Thr(228), Ser(230), Ser(232) and Thr(236) have been identified as the predominant sites of O-glycan attachment.
22067045	7	57	theme	attached	1140:1147	arg1	glycans					1149:1155	the attached glycans	1136:1155	the attached glycans (positional isomers)	1136:1176	Here, we report the identification and elucidation of IgA1 O-glycopeptide structural isomers that occur based on amino acid position of the attached glycans (positional isomers) and the structure of the O-glycan chains at individual sites (glycan isomers).
22067045	7	57	theme	attached	1140:1147	arg1	isomers					1169:1175	positional isomers	1158:1175	positional isomers	1158:1175	Here, we report the identification and elucidation of IgA1 O-glycopeptide structural isomers that occur based on amino acid position of the attached glycans (positional isomers) and the structure of the O-glycan chains at individual sites (glycan isomers).
22067045	5	58	theme	complex	695:701	arg1	heterogeneity					703:715	a complex heterogeneity	693:715	a complex heterogeneity of surface epitopes that is incompletely defined	693:764	The range and distribution of O-glycan chains at each site within the context of adjacent sites in this clustered region create a complex heterogeneity of surface epitopes that is incompletely defined.
22067045	6	59	theme	O-glycan	812:819	arg1	heterogeneity					821:833	IgA1 O-glycan heterogeneity	807:833	IgA1 O-glycan heterogeneity	807:833	We previously described the analysis of IgA1 O-glycan heterogeneity by use of high resolution LC-MS and electron capture dissociation tandem MS to unambiguously localize all amino acid attachment sites in IgA1 (Ale) myeloma protein.
22067045	3	60	theme	structural	240:249	arg1	difference					251:260	The major structural difference	230:260	The major structural difference between these two subclasses	230:289	The major structural difference between these two subclasses is the presence of nine potential sites of O-glycosylation in the hinge region between the first and second constant region domains of the heavy chain.
22067045	3	60	theme	structural	240:249	arg1	presence					298:305	the presence	294:305	the presence of nine potential sites of O-glycosylation in the hinge region between the first and second constant region domains of the heavy chain	294:440	The major structural difference between these two subclasses is the presence of nine potential sites of O-glycosylation in the hinge region between the first and second constant region domains of the heavy chain.
22067045	8	61	theme	IgA1	1294:1297	arg1	protein					1314:1320	a model IgA1 (Mce1) myeloma protein	1286:1320	a model IgA1 (Mce1) myeloma protein	1286:1320	These isomers are present in a model IgA1 (Mce1) myeloma protein and occur naturally in normal human serum IgA1.
22067045	10	62	theme	clustered	1775:1783	arg1	variability					1794:1804	clustered O-glycan variability	1775:1804	clustered O-glycan variability	1775:1804	These findings represent the first definitive identification of structural isomeric IgA1 O-glycoforms, define the single-site heterogeneity for all O-glycan sites in a single sample, and have implications for defining epitopes based on clustered O-glycan variability.
22067045	10	63	theme	definitive	1574:1583	arg1	identification					1585:1598	the first definitive identification	1564:1598	the first definitive identification of structural isomeric IgA1 O-glycoforms	1564:1639	These findings represent the first definitive identification of structural isomeric IgA1 O-glycoforms, define the single-site heterogeneity for all O-glycan sites in a single sample, and have implications for defining epitopes based on clustered O-glycan variability.
22067045	8	64	located	present	1275:1281	arg1	protein					1314:1320	a model IgA1 (Mce1) myeloma protein	1286:1320	a model IgA1 (Mce1) myeloma protein	1286:1320	These isomers are present in a model IgA1 (Mce1) myeloma protein and occur naturally in normal human serum IgA1.
22067045	8	64	located	present	1275:1281	arg2	isomers					1263:1269	These isomers	1257:1269	These isomers	1257:1269	These isomers are present in a model IgA1 (Mce1) myeloma protein and occur naturally in normal human serum IgA1.
22067045	8	65	theme	Mce1	1300:1303	arg1	protein					1314:1320	a model IgA1 (Mce1) myeloma protein	1286:1320	a model IgA1 (Mce1) myeloma protein	1286:1320	These isomers are present in a model IgA1 (Mce1) myeloma protein and occur naturally in normal human serum IgA1.
22067045	7	66	theme	individual	1222:1231	arg1	sites					1233:1237	individual sites	1222:1237	individual sites (glycan isomers)	1222:1254	Here, we report the identification and elucidation of IgA1 O-glycopeptide structural isomers that occur based on amino acid position of the attached glycans (positional isomers) and the structure of the O-glycan chains at individual sites (glycan isomers).
22067045	7	66	theme	individual	1222:1231	arg1	isomers					1247:1253	glycan isomers	1240:1253	glycan isomers	1240:1253	Here, we report the identification and elucidation of IgA1 O-glycopeptide structural isomers that occur based on amino acid position of the attached glycans (positional isomers) and the structure of the O-glycan chains at individual sites (glycan isomers).
22067045	3	67	from	presence	298:305	arg1	region					363:368	the hinge region	353:368	the hinge region between the first and second constant region domains of the heavy chain	353:440	The major structural difference between these two subclasses is the presence of nine potential sites of O-glycosylation in the hinge region between the first and second constant region domains of the heavy chain.
22067045	10	68	theme	O-glycoforms	1628:1639	arg1	identification					1585:1598	the first definitive identification	1564:1598	the first definitive identification of structural isomeric IgA1 O-glycoforms	1564:1639	These findings represent the first definitive identification of structural isomeric IgA1 O-glycoforms, define the single-site heterogeneity for all O-glycan sites in a single sample, and have implications for defining epitopes based on clustered O-glycan variability.
22067045	6	69	theme	tandem	901:906	arg1	MS					908:909	tandem MS	901:909	tandem MS	901:909	We previously described the analysis of IgA1 O-glycan heterogeneity by use of high resolution LC-MS and electron capture dissociation tandem MS to unambiguously localize all amino acid attachment sites in IgA1 (Ale) myeloma protein.
22067045	8	70	theme	myeloma	1306:1312	arg1	protein					1314:1320	a model IgA1 (Mce1) myeloma protein	1286:1320	a model IgA1 (Mce1) myeloma protein	1286:1320	These isomers are present in a model IgA1 (Mce1) myeloma protein and occur naturally in normal human serum IgA1.
22067045	7	71	theme	chains	1212:1217	arg1	position					1124:1131	amino acid position	1113:1131	amino acid position of the attached glycans (positional isomers)	1113:1176	Here, we report the identification and elucidation of IgA1 O-glycopeptide structural isomers that occur based on amino acid position of the attached glycans (positional isomers) and the structure of the O-glycan chains at individual sites (glycan isomers).
22067045	7	71	theme	chains	1212:1217	arg1	structure					1186:1194	the structure	1182:1194	the structure of the O-glycan chains at individual sites (glycan isomers)	1182:1254	Here, we report the identification and elucidation of IgA1 O-glycopeptide structural isomers that occur based on amino acid position of the attached glycans (positional isomers) and the structure of the O-glycan chains at individual sites (glycan isomers).
22067045	5	72	from	site	619:622	arg1	chains					604:609	O-glycan chains	595:609	O-glycan chains at each site within the context of adjacent sites in this clustered region	595:684	The range and distribution of O-glycan chains at each site within the context of adjacent sites in this clustered region create a complex heterogeneity of surface epitopes that is incompletely defined.
22067045	5	72	from	site	619:622	arg1	range					569:573	range	569:573	range	569:573	The range and distribution of O-glycan chains at each site within the context of adjacent sites in this clustered region create a complex heterogeneity of surface epitopes that is incompletely defined.
22067045	5	72	from	site	619:622	arg1	distribution					579:590	distribution	579:590	distribution	579:590	The range and distribution of O-glycan chains at each site within the context of adjacent sites in this clustered region create a complex heterogeneity of surface epitopes that is incompletely defined.
22067045	10	73	theme	isomeric	1614:1621	arg1	O-glycoforms					1628:1639	structural isomeric IgA1 O-glycoforms	1603:1639	structural isomeric IgA1 O-glycoforms	1603:1639	These findings represent the first definitive identification of structural isomeric IgA1 O-glycoforms, define the single-site heterogeneity for all O-glycan sites in a single sample, and have implications for defining epitopes based on clustered O-glycan variability.
22067045	6	74	theme	capture	880:886	arg1	dissociation					888:899	electron capture dissociation	871:899	electron capture dissociation	871:899	We previously described the analysis of IgA1 O-glycan heterogeneity by use of high resolution LC-MS and electron capture dissociation tandem MS to unambiguously localize all amino acid attachment sites in IgA1 (Ale) myeloma protein.
22067045	9	75	theme	GalNAc	1523:1528	arg1	residue					1530:1536	a single GalNAc residue	1514:1536	a single GalNAc residue	1514:1536	Variable O-glycan chains attached to Ser(230), Thr(233) or Thr(236) produce the predominant positional isomers, including O-glycans composed of a single GalNAc residue.
22067045	0	76	from	isomers	31:37	arg1	o-glycosylation					53:67	serum IgA1 o-glycosylation	42:67	serum IgA1 o-glycosylation	42:67	Naturally occurring structural isomers in serum IgA1 o-glycosylation.
22067045	5	77	theme	O-glycan	595:602	arg1	chains					604:609	O-glycan chains	595:609	O-glycan chains at each site within the context of adjacent sites in this clustered region	595:684	The range and distribution of O-glycan chains at each site within the context of adjacent sites in this clustered region create a complex heterogeneity of surface epitopes that is incompletely defined.
22067045	7	78	theme	structural	1074:1083	arg1	isomers					1085:1091	IgA1 O-glycopeptide structural isomers	1054:1091	IgA1 O-glycopeptide structural isomers that occur based on amino acid position of the attached glycans (positional isomers) and the structure of the O-glycan chains at individual sites (glycan isomers)	1054:1254	Here, we report the identification and elucidation of IgA1 O-glycopeptide structural isomers that occur based on amino acid position of the attached glycans (positional isomers) and the structure of the O-glycan chains at individual sites (glycan isomers).
22067045	5	79	from	sites	655:659	arg1	region					679:684	this clustered region	664:684	this clustered region	664:684	The range and distribution of O-glycan chains at each site within the context of adjacent sites in this clustered region create a complex heterogeneity of surface epitopes that is incompletely defined.
22067045	5	80	dep	range	569:573	arg1	The					565:567	The	565:567	The	565:567	The range and distribution of O-glycan chains at each site within the context of adjacent sites in this clustered region create a complex heterogeneity of surface epitopes that is incompletely defined.
22067045	4	81	theme	attachment	553:562	arg1	Thr					453:455	Thr(228)	453:460	Thr(228)	453:460	Thr(225), Thr(228), Ser(230), Ser(232) and Thr(236) have been identified as the predominant sites of O-glycan attachment.
22067045	4	81	theme	attachment	553:562	arg1	Thr					443:445	Thr	443:445	Thr(225)	443:450	Thr(225), Thr(228), Ser(230), Ser(232) and Thr(236) have been identified as the predominant sites of O-glycan attachment.
22067045	4	81	theme	attachment	553:562	arg1	attachment					553:562	O-glycan attachment	544:562	O-glycan attachment	544:562	Thr(225), Thr(228), Ser(230), Ser(232) and Thr(236) have been identified as the predominant sites of O-glycan attachment.
22067045	4	81	theme	attachment	553:562	arg1	Thr					486:488	Thr	486:488	Thr(236)	486:493	Thr(225), Thr(228), Ser(230), Ser(232) and Thr(236) have been identified as the predominant sites of O-glycan attachment.
22067045	4	81	theme	attachment	553:562	arg1	Ser					473:475	Ser(232)	473:480	Ser(232)	473:480	Thr(225), Thr(228), Ser(230), Ser(232) and Thr(236) have been identified as the predominant sites of O-glycan attachment.
22067045	4	81	theme	attachment	553:562	arg1	Ser					463:465	Ser(230)	463:470	Ser(230)	463:470	Thr(225), Thr(228), Ser(230), Ser(232) and Thr(236) have been identified as the predominant sites of O-glycan attachment.
22067045	4	81	theme	attachment	553:562	arg1	sites					535:539	the predominant sites	519:539	the predominant sites of O-glycan attachment	519:562	Thr(225), Thr(228), Ser(230), Ser(232) and Thr(236) have been identified as the predominant sites of O-glycan attachment.
22067045	7	82	theme	IgA1	1054:1057	arg1	isomers					1085:1091	IgA1 O-glycopeptide structural isomers	1054:1091	IgA1 O-glycopeptide structural isomers that occur based on amino acid position of the attached glycans (positional isomers) and the structure of the O-glycan chains at individual sites (glycan isomers)	1054:1254	Here, we report the identification and elucidation of IgA1 O-glycopeptide structural isomers that occur based on amino acid position of the attached glycans (positional isomers) and the structure of the O-glycan chains at individual sites (glycan isomers).
22067045	6	83	theme	resolution	850:859	arg1	LC-MS					861:865	high resolution LC-MS	845:865	high resolution LC-MS	845:865	We previously described the analysis of IgA1 O-glycan heterogeneity by use of high resolution LC-MS and electron capture dissociation tandem MS to unambiguously localize all amino acid attachment sites in IgA1 (Ale) myeloma protein.
22067045	3	84	theme	O-glycosylation	334:348	arg1	sites					325:329	nine potential sites	310:329	nine potential sites of O-glycosylation	310:348	The major structural difference between these two subclasses is the presence of nine potential sites of O-glycosylation in the hinge region between the first and second constant region domains of the heavy chain.
22067045	3	84	theme	O-glycosylation	334:348	arg1	O-glycosylation					334:348	O-glycosylation	334:348	O-glycosylation	334:348	The major structural difference between these two subclasses is the presence of nine potential sites of O-glycosylation in the hinge region between the first and second constant region domains of the heavy chain.
22067045	8	85	theme	normal	1345:1350	arg1	IgA1					1364:1367	normal human serum IgA1	1345:1367	normal human serum IgA1	1345:1367	These isomers are present in a model IgA1 (Mce1) myeloma protein and occur naturally in normal human serum IgA1.
22067045	5	86	theme	chains	604:609	arg1	range					569:573	range	569:573	range	569:573	The range and distribution of O-glycan chains at each site within the context of adjacent sites in this clustered region create a complex heterogeneity of surface epitopes that is incompletely defined.
22067045	5	86	theme	chains	604:609	arg1	distribution					579:590	distribution	579:590	distribution	579:590	The range and distribution of O-glycan chains at each site within the context of adjacent sites in this clustered region create a complex heterogeneity of surface epitopes that is incompletely defined.
22067045	5	87	from	region	679:684	arg1	context					635:641	the context	631:641	the context of adjacent sites in this clustered region	631:684	The range and distribution of O-glycan chains at each site within the context of adjacent sites in this clustered region create a complex heterogeneity of surface epitopes that is incompletely defined.
22067045	9	88	theme	Variable	1370:1377	arg1	chains					1388:1393	Variable O-glycan chains	1370:1393	Variable O-glycan chains attached to Ser(230), Thr(233) or Thr(236)	1370:1436	Variable O-glycan chains attached to Ser(230), Thr(233) or Thr(236) produce the predominant positional isomers, including O-glycans composed of a single GalNAc residue.
22067045	6	89	theme	attachment	952:961	arg1	sites					963:967	all amino acid attachment sites	937:967	all amino acid attachment sites in IgA1 (Ale) myeloma protein	937:997	We previously described the analysis of IgA1 O-glycan heterogeneity by use of high resolution LC-MS and electron capture dissociation tandem MS to unambiguously localize all amino acid attachment sites in IgA1 (Ale) myeloma protein.
22067045	3	90	theme	sites	325:329	arg1	difference					251:260	The major structural difference	230:260	The major structural difference between these two subclasses	230:289	The major structural difference between these two subclasses is the presence of nine potential sites of O-glycosylation in the hinge region between the first and second constant region domains of the heavy chain.
22067045	3	90	theme	sites	325:329	arg1	presence					298:305	the presence	294:305	the presence of nine potential sites of O-glycosylation in the hinge region between the first and second constant region domains of the heavy chain	294:440	The major structural difference between these two subclasses is the presence of nine potential sites of O-glycosylation in the hinge region between the first and second constant region domains of the heavy chain.
22067045	3	91	attach	presence	298:305	arg2	O-glycosylation					334:348	O-glycosylation	334:348	O-glycosylation	334:348	The major structural difference between these two subclasses is the presence of nine potential sites of O-glycosylation in the hinge region between the first and second constant region domains of the heavy chain.
22067045	3	91	attach	presence	298:305	arg2	sites					325:329	nine potential sites	310:329	nine potential sites of O-glycosylation	310:348	The major structural difference between these two subclasses is the presence of nine potential sites of O-glycosylation in the hinge region between the first and second constant region domains of the heavy chain.
22067045	3	91	attach	presence	298:305	arg1	region					363:368	the hinge region	353:368	the hinge region between the first and second constant region domains of the heavy chain	353:440	The major structural difference between these two subclasses is the presence of nine potential sites of O-glycosylation in the hinge region between the first and second constant region domains of the heavy chain.
22067045	0	92	theme	occurring	10:18	arg1	isomers					31:37	Naturally occurring structural isomers	0:37	Naturally occurring structural isomers in serum IgA1 o-glycosylation	0:67	Naturally occurring structural isomers in serum IgA1 o-glycosylation.
22067045	6	93	theme	amino	941:945	arg1	sites					963:967	all amino acid attachment sites	937:967	all amino acid attachment sites in IgA1 (Ale) myeloma protein	937:997	We previously described the analysis of IgA1 O-glycan heterogeneity by use of high resolution LC-MS and electron capture dissociation tandem MS to unambiguously localize all amino acid attachment sites in IgA1 (Ale) myeloma protein.
22067045	3	94	theme	constant	399:406	arg1	domains					415:421	the first and second constant region domains	378:421	the first and second constant region domains of the heavy chain	378:440	The major structural difference between these two subclasses is the presence of nine potential sites of O-glycosylation in the hinge region between the first and second constant region domains of the heavy chain.
22067045	3	94	theme	constant	399:406	arg1	chain					436:440	the heavy chain	426:440	the heavy chain	426:440	The major structural difference between these two subclasses is the presence of nine potential sites of O-glycosylation in the hinge region between the first and second constant region domains of the heavy chain.
22067045	5	95	theme	clustered	669:677	arg1	region					679:684	this clustered region	664:684	this clustered region	664:684	The range and distribution of O-glycan chains at each site within the context of adjacent sites in this clustered region create a complex heterogeneity of surface epitopes that is incompletely defined.
22067045	3	96	gly	O-glycosylation	334:348	arg2	O-glycosylation					334:348	O-glycosylation	334:348	O-glycosylation	334:348	The major structural difference between these two subclasses is the presence of nine potential sites of O-glycosylation in the hinge region between the first and second constant region domains of the heavy chain.
22067045	3	96	gly	O-glycosylation	334:348	arg2	sites					325:329	nine potential sites	310:329	nine potential sites of O-glycosylation	310:348	The major structural difference between these two subclasses is the presence of nine potential sites of O-glycosylation in the hinge region between the first and second constant region domains of the heavy chain.
22067045	7	97	theme	positional	1158:1167	arg1	glycans					1149:1155	the attached glycans	1136:1155	the attached glycans (positional isomers)	1136:1176	Here, we report the identification and elucidation of IgA1 O-glycopeptide structural isomers that occur based on amino acid position of the attached glycans (positional isomers) and the structure of the O-glycan chains at individual sites (glycan isomers).
22067045	7	97	theme	positional	1158:1167	arg1	isomers					1169:1175	positional isomers	1158:1175	positional isomers	1158:1175	Here, we report the identification and elucidation of IgA1 O-glycopeptide structural isomers that occur based on amino acid position of the attached glycans (positional isomers) and the structure of the O-glycan chains at individual sites (glycan isomers).
22067045	2	98	theme	Human	173:177	arg1	IgA					179:181	Human IgA	173:181	Human IgA	173:181	Human IgA is represented by two isotypes, IgA1 and IgA2.
22067045	3	99	theme	chain	436:440	arg1	domains					415:421	the first and second constant region domains	378:421	the first and second constant region domains of the heavy chain	378:440	The major structural difference between these two subclasses is the presence of nine potential sites of O-glycosylation in the hinge region between the first and second constant region domains of the heavy chain.
22067045	3	99	theme	chain	436:440	arg1	chain					436:440	the heavy chain	426:440	the heavy chain	426:440	The major structural difference between these two subclasses is the presence of nine potential sites of O-glycosylation in the hinge region between the first and second constant region domains of the heavy chain.
22067045	0	100	theme	serum	42:46	arg1	o-glycosylation					53:67	serum IgA1 o-glycosylation	42:67	serum IgA1 o-glycosylation	42:67	Naturally occurring structural isomers in serum IgA1 o-glycosylation.
22067045	7	101	theme	glycans	1149:1155	arg1	position					1124:1131	amino acid position	1113:1131	amino acid position of the attached glycans (positional isomers)	1113:1176	Here, we report the identification and elucidation of IgA1 O-glycopeptide structural isomers that occur based on amino acid position of the attached glycans (positional isomers) and the structure of the O-glycan chains at individual sites (glycan isomers).
22067045	7	101	theme	glycans	1149:1155	arg1	structure					1186:1194	the structure	1182:1194	the structure of the O-glycan chains at individual sites (glycan isomers)	1182:1254	Here, we report the identification and elucidation of IgA1 O-glycopeptide structural isomers that occur based on amino acid position of the attached glycans (positional isomers) and the structure of the O-glycan chains at individual sites (glycan isomers).
22067045	5	102	theme	adjacent	646:653	arg1	sites					655:659	adjacent sites	646:659	adjacent sites in this clustered region	646:684	The range and distribution of O-glycan chains at each site within the context of adjacent sites in this clustered region create a complex heterogeneity of surface epitopes that is incompletely defined.
22067045	8	103	theme	serum	1358:1362	arg1	IgA1					1364:1367	normal human serum IgA1	1345:1367	normal human serum IgA1	1345:1367	These isomers are present in a model IgA1 (Mce1) myeloma protein and occur naturally in normal human serum IgA1.
22067045	10	104	theme	O-glycan	1687:1694	arg1	sites					1696:1700	all O-glycan sites	1683:1700	all O-glycan sites in a single sample	1683:1719	These findings represent the first definitive identification of structural isomeric IgA1 O-glycoforms, define the single-site heterogeneity for all O-glycan sites in a single sample, and have implications for defining epitopes based on clustered O-glycan variability.
22067045	7	105	theme	acid	1119:1122	arg1	position					1124:1131	amino acid position	1113:1131	amino acid position of the attached glycans (positional isomers)	1113:1176	Here, we report the identification and elucidation of IgA1 O-glycopeptide structural isomers that occur based on amino acid position of the attached glycans (positional isomers) and the structure of the O-glycan chains at individual sites (glycan isomers).
22067045	10	106	gly	O-glycoforms	1628:1639	arg1	IgA1					1623:1626	structural isomeric IgA1 O-glycoforms	1603:1639	structural isomeric IgA1 O-glycoforms	1603:1639	These findings represent the first definitive identification of structural isomeric IgA1 O-glycoforms, define the single-site heterogeneity for all O-glycan sites in a single sample, and have implications for defining epitopes based on clustered O-glycan variability.
22067045	7	107	theme	amino	1113:1117	arg1	position					1124:1131	amino acid position	1113:1131	amino acid position of the attached glycans (positional isomers)	1113:1176	Here, we report the identification and elucidation of IgA1 O-glycopeptide structural isomers that occur based on amino acid position of the attached glycans (positional isomers) and the structure of the O-glycan chains at individual sites (glycan isomers).
22067045	10	108	theme	single	1707:1712	arg1	sample					1714:1719	a single sample	1705:1719	a single sample	1705:1719	These findings represent the first definitive identification of structural isomeric IgA1 O-glycoforms, define the single-site heterogeneity for all O-glycan sites in a single sample, and have implications for defining epitopes based on clustered O-glycan variability.
24085305	12	0	theme	anti-inflammatory	1926:1942	arg1	LILRA3					1900:1905	LILRA3	1900:1905	LILRA3	1900:1905	Overall, our data demonstrated for the first time that LILRA3 is a potential new anti-inflammatory protein, and optimal glycosylation is required for its functions.
24085305	12	0	theme	anti-inflammatory	1926:1942	arg1	protein					1944:1950	a potential new anti-inflammatory protein	1910:1950	a potential new anti-inflammatory protein	1910:1950	Overall, our data demonstrated for the first time that LILRA3 is a potential new anti-inflammatory protein, and optimal glycosylation is required for its functions.
24085305	7	1	theme	larger	1088:1093	arg1	times					1082:1086	2-4 times	1078:1086	2-4 times larger than the unprocessed protein	1078:1122	In contrast, rLILRA3 produced in E. coli was similar in size to the unprocessed protein, but yeast-produced protein was 2-4 times larger than the unprocessed protein.
24085305	11	2	theme	glycosylated	1774:1785	arg1	LILRA3					1787:1792	optimally glycosylated LILRA3	1764:1792	optimally glycosylated LILRA3	1764:1792	Binding to monocytes was partially blocked by β-lactose, indicating that optimally glycosylated LILRA3 might be critical for ligand binding and function.
24085305	1	3	theme	inhibitory	257:266	arg1	receptors					268:276	the highly homologous activating and inhibitory receptors	220:276	the highly homologous activating and inhibitory receptors expressed on leukocytes	220:300	The leukocyte immunoglobulin-like receptor (LILR) A3 is a member of the highly homologous activating and inhibitory receptors expressed on leukocytes.
24085305	3	4	theme	knowledge	556:564	arg1	lack					487:490	the lack	483:490	the lack of high quality functional recombinant protein and insufficient knowledge regarding its ligand(s)	483:588	Functions of LILRA3 are unclear primarily because of the lack of high quality functional recombinant protein and insufficient knowledge regarding its ligand(s).
24085305	8	5	theme	peptide-N-glycosidase	1140:1160	arg1	F					1162:1162	peptide-N-glycosidase F	1140:1162	peptide-N-glycosidase F	1140:1162	Treatment with peptide-N-glycosidase F reduced the size of the mammalian cell- and yeast-produced rLILRA3 to 50 kDa, suggesting that most modifications are due to glycosylation.
24085305	8	6	theme	yeast-produced	1208:1221	arg1	rLILRA3					1223:1229	the mammalian cell- and yeast-produced rLILRA3	1184:1229	the mammalian cell- and yeast-produced rLILRA3 to 50 kDa	1184:1239	Treatment with peptide-N-glycosidase F reduced the size of the mammalian cell- and yeast-produced rLILRA3 to 50 kDa, suggesting that most modifications are due to glycosylation.
24085305	5	7	theme	native	827:832	arg1	LILRA3					845:850	a 70-kDa native macrophage LILRA3	818:850	a 70-kDa native macrophage LILRA3	818:850	We found that the purified rLILRA3 produced in the mammalian system was the same size as a 70-kDa native macrophage LILRA3.
24085305	9	8	with	Consistent	1303:1312	arg1	this					1319:1322	this	1319:1322	this	1319:1322	Consistent with this, mass spectrometric analysis of the mammalian rLILRA3 revealed canonical N-glycosylation at the predicted Asn(140), Asn(281), Asn(302), Asn(341), and Asn(431) sites.
24085305	2	9	theme	soluble	315:321	arg1	LILRA3					303:308	LILRA3	303:308	LILRA3	303:308	LILRA3 is a soluble receptor of unknown functions but is predicted to act as a broad antagonist to other membrane-bound LILRs.
24085305	2	9	theme	soluble	315:321	arg1	receptor					323:330	a soluble receptor	313:330	a soluble receptor of unknown functions	313:351	LILRA3 is a soluble receptor of unknown functions but is predicted to act as a broad antagonist to other membrane-bound LILRs.
24085305	12	10	theme	first	1884:1888	arg1	time					1890:1893	the first time	1880:1893	the first time	1880:1893	Overall, our data demonstrated for the first time that LILRA3 is a potential new anti-inflammatory protein, and optimal glycosylation is required for its functions.
24085305	4	11	theme	recombinant	628:638	arg1	proteins					657:664	recombinant LILRA3 (rLILRA3) proteins	628:664	recombinant LILRA3 (rLILRA3) proteins produced in 293T cells, Escherichia coli, and Pichia pastoris	628:726	Here, we expressed and characterized recombinant LILRA3 (rLILRA3) proteins produced in 293T cells, Escherichia coli, and Pichia pastoris.
24085305	0	12	theme	receptor	131:138	arg1	protein					143:149	functionally active leukocyte immunoglobulin-like receptor A3 protein	81:149	functionally active leukocyte immunoglobulin-like receptor A3 protein	81:149	Glycosylation in a mammalian expression system is critical for the production of functionally active leukocyte immunoglobulin-like receptor A3 protein.
24085305	10	13	theme	TNFα	1661:1664	arg1	production					1666:1675	LPS-induced TNFα production	1649:1675	LPS-induced TNFα production by monocytes	1649:1688	Functionally, only mammalian cell-expressed rLILRA3 bound onto the surface of monocytes with high affinity, and importantly, only this significantly abrogated LPS-induced TNFα production by monocytes.
24085305	6	14	theme	significant	912:922	arg1	modifications					943:955	significant post-translational modifications	912:955	significant post-translational modifications	912:955	This is 20 kDa larger than the calculated size, suggesting significant post-translational modifications.
24085305	0	15	theme	protein	143:149	arg1	production					67:76	the production	63:76	the production of functionally active leukocyte immunoglobulin-like receptor A3 protein	63:149	Glycosylation in a mammalian expression system is critical for the production of functionally active leukocyte immunoglobulin-like receptor A3 protein.
24085305	8	16	theme	cell-	1198:1202	arg1	rLILRA3					1223:1229	the mammalian cell- and yeast-produced rLILRA3	1184:1229	the mammalian cell- and yeast-produced rLILRA3 to 50 kDa	1184:1239	Treatment with peptide-N-glycosidase F reduced the size of the mammalian cell- and yeast-produced rLILRA3 to 50 kDa, suggesting that most modifications are due to glycosylation.
24085305	8	17	theme	most	1258:1261	arg1	modifications					1263:1275	most modifications	1258:1275	most modifications	1258:1275	Treatment with peptide-N-glycosidase F reduced the size of the mammalian cell- and yeast-produced rLILRA3 to 50 kDa, suggesting that most modifications are due to glycosylation.
24085305	6	18	theme	calculated	884:893	arg1	size					895:898	the calculated size	880:898	the calculated size	880:898	This is 20 kDa larger than the calculated size, suggesting significant post-translational modifications.
24085305	10	19	theme	LPS-induced	1649:1659	arg1	production					1666:1675	LPS-induced TNFα production	1649:1675	LPS-induced TNFα production by monocytes	1649:1688	Functionally, only mammalian cell-expressed rLILRA3 bound onto the surface of monocytes with high affinity, and importantly, only this significantly abrogated LPS-induced TNFα production by monocytes.
24085305	9	20	theme	Asn	1450:1452	arg1	sites					1483:1487	the predicted Asn(140), Asn(281), Asn(302), Asn(341), and Asn(431) sites	1416:1487	the predicted Asn(140), Asn(281), Asn(302), Asn(341), and Asn(431) sites	1416:1487	Consistent with this, mass spectrometric analysis of the mammalian rLILRA3 revealed canonical N-glycosylation at the predicted Asn(140), Asn(281), Asn(302), Asn(341), and Asn(431) sites.
24085305	4	21	theme	293T	678:681	arg1	cells					683:687	293T cells	678:687	293T cells	678:687	Here, we expressed and characterized recombinant LILRA3 (rLILRA3) proteins produced in 293T cells, Escherichia coli, and Pichia pastoris.
24085305	4	21	theme	293T	678:681	arg1	coli					702:705	Escherichia coli	690:705	Escherichia coli	690:705	Here, we expressed and characterized recombinant LILRA3 (rLILRA3) proteins produced in 293T cells, Escherichia coli, and Pichia pastoris.
24085305	4	21	theme	293T	678:681	arg1	pastoris					719:726	Pichia pastoris	712:726	Pichia pastoris	712:726	Here, we expressed and characterized recombinant LILRA3 (rLILRA3) proteins produced in 293T cells, Escherichia coli, and Pichia pastoris.
24085305	1	22	theme	leukocyte	156:164	arg1	A3					202:203	The leukocyte immunoglobulin-like receptor (LILR) A3	152:203	The leukocyte immunoglobulin-like receptor (LILR) A3	152:203	The leukocyte immunoglobulin-like receptor (LILR) A3 is a member of the highly homologous activating and inhibitory receptors expressed on leukocytes.
24085305	1	22	theme	leukocyte	156:164	arg1	member					210:215	a member	208:215	a member of the highly homologous activating and inhibitory receptors expressed on leukocytes	208:300	The leukocyte immunoglobulin-like receptor (LILR) A3 is a member of the highly homologous activating and inhibitory receptors expressed on leukocytes.
24085305	12	23	theme	optimal	1957:1963	arg1	glycosylation					1965:1977	optimal glycosylation	1957:1977	optimal glycosylation	1957:1977	Overall, our data demonstrated for the first time that LILRA3 is a potential new anti-inflammatory protein, and optimal glycosylation is required for its functions.
24085305	5	24	theme	purified	747:754	arg1	rLILRA3					756:762	the purified rLILRA3	743:762	the purified rLILRA3 produced in the mammalian system	743:795	We found that the purified rLILRA3 produced in the mammalian system was the same size as a 70-kDa native macrophage LILRA3.
24085305	5	24	theme	purified	747:754	arg1	size					810:813	the same size	801:813	the same size	801:813	We found that the purified rLILRA3 produced in the mammalian system was the same size as a 70-kDa native macrophage LILRA3.
24085305	1	25	theme	receptor	186:193	arg1	A3					202:203	The leukocyte immunoglobulin-like receptor (LILR) A3	152:203	The leukocyte immunoglobulin-like receptor (LILR) A3	152:203	The leukocyte immunoglobulin-like receptor (LILR) A3 is a member of the highly homologous activating and inhibitory receptors expressed on leukocytes.
24085305	1	25	theme	receptor	186:193	arg1	member					210:215	a member	208:215	a member of the highly homologous activating and inhibitory receptors expressed on leukocytes	208:300	The leukocyte immunoglobulin-like receptor (LILR) A3 is a member of the highly homologous activating and inhibitory receptors expressed on leukocytes.
24085305	0	26	from	Glycosylation	0:12	arg1	system					40:45	a mammalian expression system	17:45	a mammalian expression system	17:45	Glycosylation in a mammalian expression system is critical for the production of functionally active leukocyte immunoglobulin-like receptor A3 protein.
24085305	2	27	theme	broad	382:386	arg1	LILRA3					303:308	LILRA3	303:308	LILRA3	303:308	LILRA3 is a soluble receptor of unknown functions but is predicted to act as a broad antagonist to other membrane-bound LILRs.
24085305	2	27	theme	broad	382:386	arg1	antagonist					388:397	a broad antagonist	380:397	a broad antagonist to other membrane-bound LILRs	380:427	LILRA3 is a soluble receptor of unknown functions but is predicted to act as a broad antagonist to other membrane-bound LILRs.
24085305	0	28	theme	leukocyte	101:109	arg1	protein					143:149	functionally active leukocyte immunoglobulin-like receptor A3 protein	81:149	functionally active leukocyte immunoglobulin-like receptor A3 protein	81:149	Glycosylation in a mammalian expression system is critical for the production of functionally active leukocyte immunoglobulin-like receptor A3 protein.
24085305	9	29	from	sites	1483:1487	arg1	N-glycosylation					1397:1411	canonical N-glycosylation	1387:1411	canonical N-glycosylation at the predicted Asn(140), Asn(281), Asn(302), Asn(341), and Asn(431) sites	1387:1487	Consistent with this, mass spectrometric analysis of the mammalian rLILRA3 revealed canonical N-glycosylation at the predicted Asn(140), Asn(281), Asn(302), Asn(341), and Asn(431) sites.
24085305	10	30	theme	monocytes	1568:1576	arg1	surface					1557:1563	the surface	1553:1563	the surface of monocytes with high affinity	1553:1595	Functionally, only mammalian cell-expressed rLILRA3 bound onto the surface of monocytes with high affinity, and importantly, only this significantly abrogated LPS-induced TNFα production by monocytes.
24085305	2	31	theme	other	402:406	arg1	LILRs					423:427	other membrane-bound LILRs	402:427	other membrane-bound LILRs	402:427	LILRA3 is a soluble receptor of unknown functions but is predicted to act as a broad antagonist to other membrane-bound LILRs.
24085305	9	32	theme	predicted	1420:1428	arg1	sites					1483:1487	the predicted Asn(140), Asn(281), Asn(302), Asn(341), and Asn(431) sites	1416:1487	the predicted Asn(140), Asn(281), Asn(302), Asn(341), and Asn(431) sites	1416:1487	Consistent with this, mass spectrometric analysis of the mammalian rLILRA3 revealed canonical N-glycosylation at the predicted Asn(140), Asn(281), Asn(302), Asn(341), and Asn(431) sites.
24085305	9	33	theme	mass	1325:1328	arg1	analysis					1344:1351	mass spectrometric analysis	1325:1351	mass spectrometric analysis of the mammalian rLILRA3	1325:1376	Consistent with this, mass spectrometric analysis of the mammalian rLILRA3 revealed canonical N-glycosylation at the predicted Asn(140), Asn(281), Asn(302), Asn(341), and Asn(431) sites.
24085305	0	34	theme	expression	29:38	arg1	system					40:45	a mammalian expression system	17:45	a mammalian expression system	17:45	Glycosylation in a mammalian expression system is critical for the production of functionally active leukocyte immunoglobulin-like receptor A3 protein.
24085305	9	35	theme	Asn	1430:1432	arg1	sites					1483:1487	the predicted Asn(140), Asn(281), Asn(302), Asn(341), and Asn(431) sites	1416:1487	the predicted Asn(140), Asn(281), Asn(302), Asn(341), and Asn(431) sites	1416:1487	Consistent with this, mass spectrometric analysis of the mammalian rLILRA3 revealed canonical N-glycosylation at the predicted Asn(140), Asn(281), Asn(302), Asn(341), and Asn(431) sites.
24085305	9	36	gly	N-glycosylation	1397:1411	arg1	sites					1483:1487	the predicted Asn(140), Asn(281), Asn(302), Asn(341), and Asn(431) sites	1416:1487	the predicted Asn(140), Asn(281), Asn(302), Asn(341), and Asn(431) sites	1416:1487	Consistent with this, mass spectrometric analysis of the mammalian rLILRA3 revealed canonical N-glycosylation at the predicted Asn(140), Asn(281), Asn(302), Asn(341), and Asn(431) sites.
24085305	9	36	gly	N-glycosylation	1397:1411	arg2	sites					1483:1487	the predicted Asn(140), Asn(281), Asn(302), Asn(341), and Asn(431) sites	1416:1487	the predicted Asn(140), Asn(281), Asn(302), Asn(341), and Asn(431) sites	1416:1487	Consistent with this, mass spectrometric analysis of the mammalian rLILRA3 revealed canonical N-glycosylation at the predicted Asn(140), Asn(281), Asn(302), Asn(341), and Asn(431) sites.
24085305	10	37	theme	high	1583:1586	arg1	affinity					1588:1595	high affinity	1583:1595	high affinity	1583:1595	Functionally, only mammalian cell-expressed rLILRA3 bound onto the surface of monocytes with high affinity, and importantly, only this significantly abrogated LPS-induced TNFα production by monocytes.
24085305	7	38	from	similar	1003:1009	arg1	size					1014:1017	size	1014:1017	size	1014:1017	In contrast, rLILRA3 produced in E. coli was similar in size to the unprocessed protein, but yeast-produced protein was 2-4 times larger than the unprocessed protein.
24085305	7	38	from	similar	1003:1009	arg1	contrast					961:968	contrast	961:968	contrast	961:968	In contrast, rLILRA3 produced in E. coli was similar in size to the unprocessed protein, but yeast-produced protein was 2-4 times larger than the unprocessed protein.
24085305	3	39	theme	functional	508:517	arg1	protein					531:537	high quality functional recombinant protein	495:537	high quality functional recombinant protein	495:537	Functions of LILRA3 are unclear primarily because of the lack of high quality functional recombinant protein and insufficient knowledge regarding its ligand(s).
24085305	1	40	theme	LILR	196:199	arg1	A3					202:203	The leukocyte immunoglobulin-like receptor (LILR) A3	152:203	The leukocyte immunoglobulin-like receptor (LILR) A3	152:203	The leukocyte immunoglobulin-like receptor (LILR) A3 is a member of the highly homologous activating and inhibitory receptors expressed on leukocytes.
24085305	1	40	theme	LILR	196:199	arg1	member					210:215	a member	208:215	a member of the highly homologous activating and inhibitory receptors expressed on leukocytes	208:300	The leukocyte immunoglobulin-like receptor (LILR) A3 is a member of the highly homologous activating and inhibitory receptors expressed on leukocytes.
24085305	9	41	theme	rLILRA3	1370:1376	arg1	analysis					1344:1351	mass spectrometric analysis	1325:1351	mass spectrometric analysis of the mammalian rLILRA3	1325:1376	Consistent with this, mass spectrometric analysis of the mammalian rLILRA3 revealed canonical N-glycosylation at the predicted Asn(140), Asn(281), Asn(302), Asn(341), and Asn(431) sites.
24085305	7	42	from	size	1014:1017	arg1	similar					1003:1009	similar	1003:1009	similar	1003:1009	In contrast, rLILRA3 produced in E. coli was similar in size to the unprocessed protein, but yeast-produced protein was 2-4 times larger than the unprocessed protein.
24085305	3	43	theme	high	495:498	arg1	protein					531:537	high quality functional recombinant protein	495:537	high quality functional recombinant protein	495:537	Functions of LILRA3 are unclear primarily because of the lack of high quality functional recombinant protein and insufficient knowledge regarding its ligand(s).
24085305	9	44	theme	canonical	1387:1395	arg1	N-glycosylation					1397:1411	canonical N-glycosylation	1387:1411	canonical N-glycosylation at the predicted Asn(140), Asn(281), Asn(302), Asn(341), and Asn(431) sites	1387:1487	Consistent with this, mass spectrometric analysis of the mammalian rLILRA3 revealed canonical N-glycosylation at the predicted Asn(140), Asn(281), Asn(302), Asn(341), and Asn(431) sites.
24085305	12	45	theme	new	1922:1924	arg1	LILRA3					1900:1905	LILRA3	1900:1905	LILRA3	1900:1905	Overall, our data demonstrated for the first time that LILRA3 is a potential new anti-inflammatory protein, and optimal glycosylation is required for its functions.
24085305	12	45	theme	new	1922:1924	arg1	protein					1944:1950	a potential new anti-inflammatory protein	1910:1950	a potential new anti-inflammatory protein	1910:1950	Overall, our data demonstrated for the first time that LILRA3 is a potential new anti-inflammatory protein, and optimal glycosylation is required for its functions.
24085305	3	46	theme	insufficient	543:554	arg1	knowledge					556:564	insufficient knowledge	543:564	insufficient knowledge regarding its ligand(s)	543:588	Functions of LILRA3 are unclear primarily because of the lack of high quality functional recombinant protein and insufficient knowledge regarding its ligand(s).
24085305	1	47	theme	receptors	268:276	arg1	A3					202:203	The leukocyte immunoglobulin-like receptor (LILR) A3	152:203	The leukocyte immunoglobulin-like receptor (LILR) A3	152:203	The leukocyte immunoglobulin-like receptor (LILR) A3 is a member of the highly homologous activating and inhibitory receptors expressed on leukocytes.
24085305	1	47	theme	receptors	268:276	arg1	member					210:215	a member	208:215	a member of the highly homologous activating and inhibitory receptors expressed on leukocytes	208:300	The leukocyte immunoglobulin-like receptor (LILR) A3 is a member of the highly homologous activating and inhibitory receptors expressed on leukocytes.
24085305	7	48	theme	yeast-produced	1051:1064	arg1	protein					1066:1072	yeast-produced protein	1051:1072	yeast-produced protein	1051:1072	In contrast, rLILRA3 produced in E. coli was similar in size to the unprocessed protein, but yeast-produced protein was 2-4 times larger than the unprocessed protein.
24085305	3	49	theme	protein	531:537	arg1	lack					487:490	the lack	483:490	the lack of high quality functional recombinant protein and insufficient knowledge regarding its ligand(s)	483:588	Functions of LILRA3 are unclear primarily because of the lack of high quality functional recombinant protein and insufficient knowledge regarding its ligand(s).
24085305	5	50	theme	70-kDa	820:825	arg1	LILRA3					845:850	a 70-kDa native macrophage LILRA3	818:850	a 70-kDa native macrophage LILRA3	818:850	We found that the purified rLILRA3 produced in the mammalian system was the same size as a 70-kDa native macrophage LILRA3.
24085305	10	51	with	monocytes	1568:1576	arg1	affinity					1588:1595	high affinity	1583:1595	high affinity	1583:1595	Functionally, only mammalian cell-expressed rLILRA3 bound onto the surface of monocytes with high affinity, and importantly, only this significantly abrogated LPS-induced TNFα production by monocytes.
24085305	7	52	from	contrast	961:968	arg1	similar					1003:1009	similar	1003:1009	similar	1003:1009	In contrast, rLILRA3 produced in E. coli was similar in size to the unprocessed protein, but yeast-produced protein was 2-4 times larger than the unprocessed protein.
24085305	4	53	theme	rLILRA3	648:654	arg1	proteins					657:664	recombinant LILRA3 (rLILRA3) proteins	628:664	recombinant LILRA3 (rLILRA3) proteins produced in 293T cells, Escherichia coli, and Pichia pastoris	628:726	Here, we expressed and characterized recombinant LILRA3 (rLILRA3) proteins produced in 293T cells, Escherichia coli, and Pichia pastoris.
24085305	5	54	theme	macrophage	834:843	arg1	LILRA3					845:850	a 70-kDa native macrophage LILRA3	818:850	a 70-kDa native macrophage LILRA3	818:850	We found that the purified rLILRA3 produced in the mammalian system was the same size as a 70-kDa native macrophage LILRA3.
24085305	8	55	theme	rLILRA3	1223:1229	arg1	size					1176:1179	the size	1172:1179	the size of the mammalian cell- and yeast-produced rLILRA3 to 50 kDa	1172:1239	Treatment with peptide-N-glycosidase F reduced the size of the mammalian cell- and yeast-produced rLILRA3 to 50 kDa, suggesting that most modifications are due to glycosylation.
24085305	0	56	theme	A3	140:141	arg1	protein					143:149	functionally active leukocyte immunoglobulin-like receptor A3 protein	81:149	functionally active leukocyte immunoglobulin-like receptor A3 protein	81:149	Glycosylation in a mammalian expression system is critical for the production of functionally active leukocyte immunoglobulin-like receptor A3 protein.
24085305	5	57	theme	same	805:808	arg1	rLILRA3					756:762	the purified rLILRA3	743:762	the purified rLILRA3 produced in the mammalian system	743:795	We found that the purified rLILRA3 produced in the mammalian system was the same size as a 70-kDa native macrophage LILRA3.
24085305	5	57	theme	same	805:808	arg1	size					810:813	the same size	801:813	the same size	801:813	We found that the purified rLILRA3 produced in the mammalian system was the same size as a 70-kDa native macrophage LILRA3.
24085305	6	58	theme	post-translational	924:941	arg1	modifications					943:955	significant post-translational modifications	912:955	significant post-translational modifications	912:955	This is 20 kDa larger than the calculated size, suggesting significant post-translational modifications.
24085305	10	59	theme	mammalian	1509:1517	arg1	rLILRA3					1534:1540	only mammalian cell-expressed rLILRA3	1504:1540	only mammalian cell-expressed rLILRA3	1504:1540	Functionally, only mammalian cell-expressed rLILRA3 bound onto the surface of monocytes with high affinity, and importantly, only this significantly abrogated LPS-induced TNFα production by monocytes.
24085305	9	60	theme	Asn	1440:1442	arg1	sites					1483:1487	the predicted Asn(140), Asn(281), Asn(302), Asn(341), and Asn(431) sites	1416:1487	the predicted Asn(140), Asn(281), Asn(302), Asn(341), and Asn(431) sites	1416:1487	Consistent with this, mass spectrometric analysis of the mammalian rLILRA3 revealed canonical N-glycosylation at the predicted Asn(140), Asn(281), Asn(302), Asn(341), and Asn(431) sites.
24085305	11	61	gly	glycosylated	1774:1785	arg1	LILRA3					1787:1792	optimally glycosylated LILRA3	1764:1792	optimally glycosylated LILRA3	1764:1792	Binding to monocytes was partially blocked by β-lactose, indicating that optimally glycosylated LILRA3 might be critical for ligand binding and function.
24085305	4	62	theme	LILRA3	640:645	arg1	proteins					657:664	recombinant LILRA3 (rLILRA3) proteins	628:664	recombinant LILRA3 (rLILRA3) proteins produced in 293T cells, Escherichia coli, and Pichia pastoris	628:726	Here, we expressed and characterized recombinant LILRA3 (rLILRA3) proteins produced in 293T cells, Escherichia coli, and Pichia pastoris.
24085305	8	63	theme	mammalian	1188:1196	arg1	rLILRA3					1223:1229	the mammalian cell- and yeast-produced rLILRA3	1184:1229	the mammalian cell- and yeast-produced rLILRA3 to 50 kDa	1184:1239	Treatment with peptide-N-glycosidase F reduced the size of the mammalian cell- and yeast-produced rLILRA3 to 50 kDa, suggesting that most modifications are due to glycosylation.
24085305	7	64	theme	unprocessed	1026:1036	arg1	protein					1038:1044	the unprocessed protein	1022:1044	the unprocessed protein	1022:1044	In contrast, rLILRA3 produced in E. coli was similar in size to the unprocessed protein, but yeast-produced protein was 2-4 times larger than the unprocessed protein.
24085305	2	65	theme	unknown	335:341	arg1	functions					343:351	unknown functions	335:351	unknown functions	335:351	LILRA3 is a soluble receptor of unknown functions but is predicted to act as a broad antagonist to other membrane-bound LILRs.
24085305	1	66	theme	immunoglobulin-like	166:184	arg1	A3					202:203	The leukocyte immunoglobulin-like receptor (LILR) A3	152:203	The leukocyte immunoglobulin-like receptor (LILR) A3	152:203	The leukocyte immunoglobulin-like receptor (LILR) A3 is a member of the highly homologous activating and inhibitory receptors expressed on leukocytes.
24085305	1	66	theme	immunoglobulin-like	166:184	arg1	member					210:215	a member	208:215	a member of the highly homologous activating and inhibitory receptors expressed on leukocytes	208:300	The leukocyte immunoglobulin-like receptor (LILR) A3 is a member of the highly homologous activating and inhibitory receptors expressed on leukocytes.
24085305	0	67	theme	active	94:99	arg1	protein					143:149	functionally active leukocyte immunoglobulin-like receptor A3 protein	81:149	functionally active leukocyte immunoglobulin-like receptor A3 protein	81:149	Glycosylation in a mammalian expression system is critical for the production of functionally active leukocyte immunoglobulin-like receptor A3 protein.
24085305	9	68	theme	Asn	1460:1462	arg1	sites					1483:1487	the predicted Asn(140), Asn(281), Asn(302), Asn(341), and Asn(431) sites	1416:1487	the predicted Asn(140), Asn(281), Asn(302), Asn(341), and Asn(431) sites	1416:1487	Consistent with this, mass spectrometric analysis of the mammalian rLILRA3 revealed canonical N-glycosylation at the predicted Asn(140), Asn(281), Asn(302), Asn(341), and Asn(431) sites.
24085305	0	69	theme	immunoglobulin-like	111:129	arg1	protein					143:149	functionally active leukocyte immunoglobulin-like receptor A3 protein	81:149	functionally active leukocyte immunoglobulin-like receptor A3 protein	81:149	Glycosylation in a mammalian expression system is critical for the production of functionally active leukocyte immunoglobulin-like receptor A3 protein.
24085305	11	70	theme	ligand	1816:1821	arg1	binding					1823:1829	ligand binding	1816:1829	ligand binding	1816:1829	Binding to monocytes was partially blocked by β-lactose, indicating that optimally glycosylated LILRA3 might be critical for ligand binding and function.
24085305	5	71	theme	mammalian	780:788	arg1	system					790:795	the mammalian system	776:795	the mammalian system	776:795	We found that the purified rLILRA3 produced in the mammalian system was the same size as a 70-kDa native macrophage LILRA3.
24085305	8	72	with	Treatment	1125:1133	arg1	F					1162:1162	peptide-N-glycosidase F	1140:1162	peptide-N-glycosidase F	1140:1162	Treatment with peptide-N-glycosidase F reduced the size of the mammalian cell- and yeast-produced rLILRA3 to 50 kDa, suggesting that most modifications are due to glycosylation.
24085305	10	73	theme	cell-expressed	1519:1532	arg1	rLILRA3					1534:1540	only mammalian cell-expressed rLILRA3	1504:1540	only mammalian cell-expressed rLILRA3	1504:1540	Functionally, only mammalian cell-expressed rLILRA3 bound onto the surface of monocytes with high affinity, and importantly, only this significantly abrogated LPS-induced TNFα production by monocytes.
24085305	0	74	theme	mammalian	19:27	arg1	system					40:45	a mammalian expression system	17:45	a mammalian expression system	17:45	Glycosylation in a mammalian expression system is critical for the production of functionally active leukocyte immunoglobulin-like receptor A3 protein.
24085305	9	75	theme	Asn	1474:1476	arg1	sites					1483:1487	the predicted Asn(140), Asn(281), Asn(302), Asn(341), and Asn(431) sites	1416:1487	the predicted Asn(140), Asn(281), Asn(302), Asn(341), and Asn(431) sites	1416:1487	Consistent with this, mass spectrometric analysis of the mammalian rLILRA3 revealed canonical N-glycosylation at the predicted Asn(140), Asn(281), Asn(302), Asn(341), and Asn(431) sites.
24085305	2	76	theme	membrane-bound	408:421	arg1	LILRs					423:427	other membrane-bound LILRs	402:427	other membrane-bound LILRs	402:427	LILRA3 is a soluble receptor of unknown functions but is predicted to act as a broad antagonist to other membrane-bound LILRs.
24085305	7	77	theme	unprocessed	1104:1114	arg1	protein					1116:1122	the unprocessed protein	1100:1122	the unprocessed protein	1100:1122	In contrast, rLILRA3 produced in E. coli was similar in size to the unprocessed protein, but yeast-produced protein was 2-4 times larger than the unprocessed protein.
24085305	1	78	theme	homologous	231:240	arg1	receptors					268:276	the highly homologous activating and inhibitory receptors	220:276	the highly homologous activating and inhibitory receptors expressed on leukocytes	220:300	The leukocyte immunoglobulin-like receptor (LILR) A3 is a member of the highly homologous activating and inhibitory receptors expressed on leukocytes.
24085305	9	79	theme	spectrometric	1330:1342	arg1	analysis					1344:1351	mass spectrometric analysis	1325:1351	mass spectrometric analysis of the mammalian rLILRA3	1325:1376	Consistent with this, mass spectrometric analysis of the mammalian rLILRA3 revealed canonical N-glycosylation at the predicted Asn(140), Asn(281), Asn(302), Asn(341), and Asn(431) sites.
24085305	3	80	theme	quality	500:506	arg1	protein					531:537	high quality functional recombinant protein	495:537	high quality functional recombinant protein	495:537	Functions of LILRA3 are unclear primarily because of the lack of high quality functional recombinant protein and insufficient knowledge regarding its ligand(s).
24085305	2	81	theme	functions	343:351	arg1	LILRA3					303:308	LILRA3	303:308	LILRA3	303:308	LILRA3 is a soluble receptor of unknown functions but is predicted to act as a broad antagonist to other membrane-bound LILRs.
24085305	2	81	theme	functions	343:351	arg1	receptor					323:330	a soluble receptor	313:330	a soluble receptor of unknown functions	313:351	LILRA3 is a soluble receptor of unknown functions but is predicted to act as a broad antagonist to other membrane-bound LILRs.
24085305	9	82	theme	mammalian	1360:1368	arg1	rLILRA3					1370:1376	the mammalian rLILRA3	1356:1376	the mammalian rLILRA3	1356:1376	Consistent with this, mass spectrometric analysis of the mammalian rLILRA3 revealed canonical N-glycosylation at the predicted Asn(140), Asn(281), Asn(302), Asn(341), and Asn(431) sites.
24085305	12	83	theme	potential	1912:1920	arg1	LILRA3					1900:1905	LILRA3	1900:1905	LILRA3	1900:1905	Overall, our data demonstrated for the first time that LILRA3 is a potential new anti-inflammatory protein, and optimal glycosylation is required for its functions.
24085305	12	83	theme	potential	1912:1920	arg1	protein					1944:1950	a potential new anti-inflammatory protein	1910:1950	a potential new anti-inflammatory protein	1910:1950	Overall, our data demonstrated for the first time that LILRA3 is a potential new anti-inflammatory protein, and optimal glycosylation is required for its functions.
24085305	3	84	theme	LILRA3	443:448	arg1	Functions					430:438	Functions	430:438	Functions of LILRA3	430:448	Functions of LILRA3 are unclear primarily because of the lack of high quality functional recombinant protein and insufficient knowledge regarding its ligand(s).
24085305	3	85	theme	recombinant	519:529	arg1	protein					531:537	high quality functional recombinant protein	495:537	high quality functional recombinant protein	495:537	Functions of LILRA3 are unclear primarily because of the lack of high quality functional recombinant protein and insufficient knowledge regarding its ligand(s).
24085305	1	86	theme	activating	242:251	arg1	receptors					268:276	the highly homologous activating and inhibitory receptors	220:276	the highly homologous activating and inhibitory receptors expressed on leukocytes	220:300	The leukocyte immunoglobulin-like receptor (LILR) A3 is a member of the highly homologous activating and inhibitory receptors expressed on leukocytes.
16263699	6	0	theme	acid	927:930	arg1	oxidation					932:940	periodic acid oxidation	918:940	periodic acid oxidation	918:940	Therefore, concanavalin A was used for specific interaction with carbohydrate species along with periodic acid oxidation and hydrazide bead trapping of glycosylated proteins.
16263699	10	1	theme	Ras-mitogen-activated	1591:1611	arg1	pathway					1628:1634	the Ras-mitogen-activated protein kinase pathway	1587:1634	the Ras-mitogen-activated protein kinase pathway in the immune system	1587:1655	With this approach including hydrazide bead affinity trapping, the immunoglobulin receptor G6f, which is known to couple to the Ras-mitogen-activated protein kinase pathway in the immune system, was shown here for the first time to be present in human platelets.
16263699	7	2	theme	modification	1147:1158	arg1	proteins					1119:1126	proteins	1119:1126	proteins	1119:1126	Derivatization by peptide:N-glycosidase F yielded deglycosylated peptides, which provided the basis for the elucidation of proteins and their sites of modification.
16263699	7	2	theme	modification	1147:1158	arg1	sites					1138:1142	their sites	1132:1142	their sites of modification	1132:1158	Derivatization by peptide:N-glycosidase F yielded deglycosylated peptides, which provided the basis for the elucidation of proteins and their sites of modification.
16263699	7	2	theme	modification	1147:1158	arg1	modification					1147:1158	modification	1147:1158	modification	1147:1158	Derivatization by peptide:N-glycosidase F yielded deglycosylated peptides, which provided the basis for the elucidation of proteins and their sites of modification.
16263699	2	3	gly	glycoprotein	304:315	arg1	glycoprotein					304:315	glycoprotein VI	304:318	glycoprotein VI	304:318	They account e.g. for secretory proteins and plasma membrane receptors including integrins and glycoprotein VI as well as intracellular components of cytosol and organelles including storage proteins (multimerin 1 etc.).
16263699	7	4	theme	sites	1138:1142	arg1	elucidation					1104:1114	the elucidation	1100:1114	the elucidation of proteins and their sites of modification	1100:1158	Derivatization by peptide:N-glycosidase F yielded deglycosylated peptides, which provided the basis for the elucidation of proteins and their sites of modification.
16263699	8	5	theme	nano-LC-ESI-MS/MS	1200:1216	arg1	analysis					1218:1225	nano-LC-ESI-MS/MS analysis	1200:1225	nano-LC-ESI-MS/MS analysis	1200:1225	Using both methods in combination with nano-LC-ESI-MS/MS analysis 70 different glycosylation sites within 41 different proteins were identified.
16263699	10	6	theme	hydrazide	1492:1500	arg1	trapping					1516:1523	hydrazide bead affinity trapping	1492:1523	hydrazide bead affinity trapping	1492:1523	With this approach including hydrazide bead affinity trapping, the immunoglobulin receptor G6f, which is known to couple to the Ras-mitogen-activated protein kinase pathway in the immune system, was shown here for the first time to be present in human platelets.
16263699	3	7	theme	little	525:530	arg1	attention					532:540	little attention	525:540	little attention	525:540	Although many of those proteins have been studied for some time with regard to their function, little attention has been paid with respect to their glycosylation sites.
16263699	4	8	theme	platelet	661:668	arg1	proteins					670:677	human platelet proteins	655:677	human platelet proteins	655:677	Here we report the analysis of N-glycosylation sites of human platelet proteins.
16263699	4	9	gly	N-glycosylation	630:644	arg2	proteins					670:677	human platelet proteins	655:677	human platelet proteins	655:677	Here we report the analysis of N-glycosylation sites of human platelet proteins.
16263699	4	9	gly	N-glycosylation	630:644	arg1	proteins					670:677	human platelet proteins	655:677	human platelet proteins	655:677	Here we report the analysis of N-glycosylation sites of human platelet proteins.
16263699	4	9	gly	N-glycosylation	630:644	arg2	sites					646:650	N-glycosylation sites	630:650	N-glycosylation sites of human platelet proteins	630:677	Here we report the analysis of N-glycosylation sites of human platelet proteins.
16263699	1	10	theme	glycoprotein	186:197	arg1	isoforms					199:206	glycoprotein isoforms	186:206	glycoprotein isoforms	186:206	Among known platelet proteins, a prominent and functionally important group is represented by glycoprotein isoforms.
16263699	8	11	theme	glycosylation	1240:1252	arg1	sites					1254:1258	70 different glycosylation sites	1227:1258	70 different glycosylation sites within 41 different proteins	1227:1287	Using both methods in combination with nano-LC-ESI-MS/MS analysis 70 different glycosylation sites within 41 different proteins were identified.
16263699	6	12	theme	proteins	986:993	arg1	trapping					961:968	hydrazide bead trapping	946:968	hydrazide bead trapping	946:968	Therefore, concanavalin A was used for specific interaction with carbohydrate species along with periodic acid oxidation and hydrazide bead trapping of glycosylated proteins.
16263699	6	12	theme	proteins	986:993	arg1	oxidation					932:940	periodic acid oxidation	918:940	periodic acid oxidation	918:940	Therefore, concanavalin A was used for specific interaction with carbohydrate species along with periodic acid oxidation and hydrazide bead trapping of glycosylated proteins.
16263699	8	13	dep	identified	1294:1303	arg1	Using					1161:1165	Using	1161:1165	Using both methods in combination with nano-LC-ESI-MS/MS analysis	1161:1225	Using both methods in combination with nano-LC-ESI-MS/MS analysis 70 different glycosylation sites within 41 different proteins were identified.
16263699	4	14	theme	N-glycosylation	630:644	arg1	proteins					670:677	human platelet proteins	655:677	human platelet proteins	655:677	Here we report the analysis of N-glycosylation sites of human platelet proteins.
16263699	4	14	theme	N-glycosylation	630:644	arg1	sites					646:650	N-glycosylation sites	630:650	N-glycosylation sites of human platelet proteins	630:677	Here we report the analysis of N-glycosylation sites of human platelet proteins.
16263699	10	15	theme	first	1681:1685	arg1	time					1687:1690	the first time	1677:1690	the first time	1677:1690	With this approach including hydrazide bead affinity trapping, the immunoglobulin receptor G6f, which is known to couple to the Ras-mitogen-activated protein kinase pathway in the immune system, was shown here for the first time to be present in human platelets.
16263699	2	16	theme	secretory	231:239	arg1	glycoprotein					304:315	glycoprotein VI	304:318	glycoprotein VI	304:318	They account e.g. for secretory proteins and plasma membrane receptors including integrins and glycoprotein VI as well as intracellular components of cytosol and organelles including storage proteins (multimerin 1 etc.).
16263699	2	16	theme	secretory	231:239	arg1	proteins					241:248	secretory proteins	231:248	secretory proteins	231:248	They account e.g. for secretory proteins and plasma membrane receptors including integrins and glycoprotein VI as well as intracellular components of cytosol and organelles including storage proteins (multimerin 1 etc.).
16263699	2	16	theme	secretory	231:239	arg1	integrins					290:298	integrins	290:298	integrins	290:298	They account e.g. for secretory proteins and plasma membrane receptors including integrins and glycoprotein VI as well as intracellular components of cytosol and organelles including storage proteins (multimerin 1 etc.).
16263699	8	17	theme	different	1270:1278	arg1	proteins					1280:1287	41 different proteins	1267:1287	41 different proteins	1267:1287	Using both methods in combination with nano-LC-ESI-MS/MS analysis 70 different glycosylation sites within 41 different proteins were identified.
16263699	6	18	theme	bead	956:959	arg1	trapping					961:968	hydrazide bead trapping	946:968	hydrazide bead trapping	946:968	Therefore, concanavalin A was used for specific interaction with carbohydrate species along with periodic acid oxidation and hydrazide bead trapping of glycosylated proteins.
16263699	7	19	theme	N-glycosidase	1022:1034	arg1	F					1036:1036	peptide:N-glycosidase F	1014:1036	peptide:N-glycosidase F	1014:1036	Derivatization by peptide:N-glycosidase F yielded deglycosylated peptides, which provided the basis for the elucidation of proteins and their sites of modification.
16263699	2	20	theme	membrane	261:268	arg1	glycoprotein					304:315	glycoprotein VI	304:318	glycoprotein VI	304:318	They account e.g. for secretory proteins and plasma membrane receptors including integrins and glycoprotein VI as well as intracellular components of cytosol and organelles including storage proteins (multimerin 1 etc.).
16263699	2	20	theme	membrane	261:268	arg1	integrins					290:298	integrins	290:298	integrins	290:298	They account e.g. for secretory proteins and plasma membrane receptors including integrins and glycoprotein VI as well as intracellular components of cytosol and organelles including storage proteins (multimerin 1 etc.).
16263699	2	20	theme	membrane	261:268	arg1	receptors					270:278	plasma membrane receptors	254:278	plasma membrane receptors	254:278	They account e.g. for secretory proteins and plasma membrane receptors including integrins and glycoprotein VI as well as intracellular components of cytosol and organelles including storage proteins (multimerin 1 etc.).
16263699	7	21	theme	peptide	1014:1020	arg1	F					1036:1036	peptide:N-glycosidase F	1014:1036	peptide:N-glycosidase F	1014:1036	Derivatization by peptide:N-glycosidase F yielded deglycosylated peptides, which provided the basis for the elucidation of proteins and their sites of modification.
16263699	1	22	theme	prominent	125:133	arg1	group					162:166	a prominent and functionally important group	123:166	a prominent and functionally important group	123:166	Among known platelet proteins, a prominent and functionally important group is represented by glycoprotein isoforms.
16263699	10	23	theme	immune	1643:1648	arg1	system					1650:1655	the immune system	1639:1655	the immune system	1639:1655	With this approach including hydrazide bead affinity trapping, the immunoglobulin receptor G6f, which is known to couple to the Ras-mitogen-activated protein kinase pathway in the immune system, was shown here for the first time to be present in human platelets.
16263699	2	24	dep	glycoprotein	304:315	arg1	VI					317:318	VI	317:318	VI	317:318	They account e.g. for secretory proteins and plasma membrane receptors including integrins and glycoprotein VI as well as intracellular components of cytosol and organelles including storage proteins (multimerin 1 etc.).
16263699	0	25	theme	glycoproteomic	67:80	arg1	approach					82:89	a glycoproteomic approach	65:89	a glycoproteomic approach	65:89	Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach.
16263699	0	26	from	Elucidation	0:10	arg1	proteins					55:62	human platelet proteins	40:62	human platelet proteins	40:62	Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach.
16263699	10	27	theme	affinity	1507:1514	arg1	trapping					1516:1523	hydrazide bead affinity trapping	1492:1523	hydrazide bead affinity trapping	1492:1523	With this approach including hydrazide bead affinity trapping, the immunoglobulin receptor G6f, which is known to couple to the Ras-mitogen-activated protein kinase pathway in the immune system, was shown here for the first time to be present in human platelets.
16263699	5	28	theme	affinity	724:731	arg1	chromatography					733:746	lectin affinity chromatography	717:746	lectin affinity chromatography as well as chemical trapping of protein bound oligosaccharides	717:809	For the enrichment of glycopeptides, lectin affinity chromatography as well as chemical trapping of protein bound oligosaccharides was used.
16263699	10	29	attach	present	1698:1704	arg2	G6f					1554:1556	the immunoglobulin receptor G6f	1526:1556	the immunoglobulin receptor G6f	1526:1556	With this approach including hydrazide bead affinity trapping, the immunoglobulin receptor G6f, which is known to couple to the Ras-mitogen-activated protein kinase pathway in the immune system, was shown here for the first time to be present in human platelets.
16263699	10	29	attach	present	1698:1704	arg1	platelets					1715:1723	human platelets	1709:1723	human platelets	1709:1723	With this approach including hydrazide bead affinity trapping, the immunoglobulin receptor G6f, which is known to couple to the Ras-mitogen-activated protein kinase pathway in the immune system, was shown here for the first time to be present in human platelets.
16263699	10	29	attach	present	1698:1704	arg2	present					1698:1704	present	1698:1704	present	1698:1704	With this approach including hydrazide bead affinity trapping, the immunoglobulin receptor G6f, which is known to couple to the Ras-mitogen-activated protein kinase pathway in the immune system, was shown here for the first time to be present in human platelets.
16263699	0	30	theme	human	40:44	arg1	proteins					55:62	human platelet proteins	40:62	human platelet proteins	40:62	Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach.
16263699	10	31	theme	immunoglobulin	1530:1543	arg1	present					1698:1704	present	1698:1704	present	1698:1704	With this approach including hydrazide bead affinity trapping, the immunoglobulin receptor G6f, which is known to couple to the Ras-mitogen-activated protein kinase pathway in the immune system, was shown here for the first time to be present in human platelets.
16263699	10	31	theme	immunoglobulin	1530:1543	arg1	G6f					1554:1556	the immunoglobulin receptor G6f	1526:1556	the immunoglobulin receptor G6f	1526:1556	With this approach including hydrazide bead affinity trapping, the immunoglobulin receptor G6f, which is known to couple to the Ras-mitogen-activated protein kinase pathway in the immune system, was shown here for the first time to be present in human platelets.
16263699	9	32	theme	sites	1388:1392	arg1	majority					1367:1374	the majority	1363:1374	the majority of these 70 sites	1363:1392	Comparison with the Swiss-Prot database established that the majority of these 70 sites have not been specifically determined by previous research projects.
16263699	10	33	located	present	1698:1704	arg2	G6f					1554:1556	the immunoglobulin receptor G6f	1526:1556	the immunoglobulin receptor G6f	1526:1556	With this approach including hydrazide bead affinity trapping, the immunoglobulin receptor G6f, which is known to couple to the Ras-mitogen-activated protein kinase pathway in the immune system, was shown here for the first time to be present in human platelets.
16263699	10	33	located	present	1698:1704	arg1	platelets					1715:1723	human platelets	1709:1723	human platelets	1709:1723	With this approach including hydrazide bead affinity trapping, the immunoglobulin receptor G6f, which is known to couple to the Ras-mitogen-activated protein kinase pathway in the immune system, was shown here for the first time to be present in human platelets.
16263699	10	33	located	present	1698:1704	arg2	present					1698:1704	present	1698:1704	present	1698:1704	With this approach including hydrazide bead affinity trapping, the immunoglobulin receptor G6f, which is known to couple to the Ras-mitogen-activated protein kinase pathway in the immune system, was shown here for the first time to be present in human platelets.
16263699	0	34	theme	N-glycosylation	15:29	arg1	sites					31:35	N-glycosylation sites	15:35	N-glycosylation sites	15:35	Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach.
16263699	1	35	theme	platelet	104:111	arg1	proteins					113:120	known platelet proteins	98:120	known platelet proteins	98:120	Among known platelet proteins, a prominent and functionally important group is represented by glycoprotein isoforms.
16263699	3	36	theme	proteins	453:460	arg1	many					439:442	many	439:442	many	439:442	Although many of those proteins have been studied for some time with regard to their function, little attention has been paid with respect to their glycosylation sites.
16263699	3	36	theme	proteins	453:460	arg1	proteins					453:460	those proteins	447:460	those proteins	447:460	Although many of those proteins have been studied for some time with regard to their function, little attention has been paid with respect to their glycosylation sites.
16263699	5	37	theme	protein	780:786	arg1	oligosaccharides					794:809	protein bound oligosaccharides	780:809	protein bound oligosaccharides	780:809	For the enrichment of glycopeptides, lectin affinity chromatography as well as chemical trapping of protein bound oligosaccharides was used.
16263699	10	38	from	pathway	1628:1634	arg1	system					1650:1655	the immune system	1639:1655	the immune system	1639:1655	With this approach including hydrazide bead affinity trapping, the immunoglobulin receptor G6f, which is known to couple to the Ras-mitogen-activated protein kinase pathway in the immune system, was shown here for the first time to be present in human platelets.
16263699	2	39	theme	cytosol	359:365	arg1	integrins					290:298	integrins	290:298	integrins	290:298	They account e.g. for secretory proteins and plasma membrane receptors including integrins and glycoprotein VI as well as intracellular components of cytosol and organelles including storage proteins (multimerin 1 etc.).
16263699	2	39	theme	cytosol	359:365	arg1	glycoprotein					304:315	glycoprotein VI	304:318	glycoprotein VI	304:318	They account e.g. for secretory proteins and plasma membrane receptors including integrins and glycoprotein VI as well as intracellular components of cytosol and organelles including storage proteins (multimerin 1 etc.).
16263699	2	39	theme	cytosol	359:365	arg1	proteins					241:248	secretory proteins	231:248	secretory proteins	231:248	They account e.g. for secretory proteins and plasma membrane receptors including integrins and glycoprotein VI as well as intracellular components of cytosol and organelles including storage proteins (multimerin 1 etc.).
16263699	2	39	theme	cytosol	359:365	arg1	components					345:354	intracellular components	331:354	secretory proteins and plasma membrane receptors including integrins and glycoprotein VI as well as intracellular components of cytosol and organelles including storage proteins (multimerin 1 etc.)	231:427	They account e.g. for secretory proteins and plasma membrane receptors including integrins and glycoprotein VI as well as intracellular components of cytosol and organelles including storage proteins (multimerin 1 etc.).
16263699	2	39	theme	cytosol	359:365	arg1	receptors					270:278	plasma membrane receptors	254:278	plasma membrane receptors	254:278	They account e.g. for secretory proteins and plasma membrane receptors including integrins and glycoprotein VI as well as intracellular components of cytosol and organelles including storage proteins (multimerin 1 etc.).
16263699	5	40	theme	oligosaccharides	794:809	arg1	chromatography					733:746	lectin affinity chromatography	717:746	lectin affinity chromatography as well as chemical trapping of protein bound oligosaccharides	717:809	For the enrichment of glycopeptides, lectin affinity chromatography as well as chemical trapping of protein bound oligosaccharides was used.
16263699	5	40	theme	oligosaccharides	794:809	arg1	trapping					768:775	chemical trapping	759:775	lectin affinity chromatography as well as chemical trapping of protein bound oligosaccharides	717:809	For the enrichment of glycopeptides, lectin affinity chromatography as well as chemical trapping of protein bound oligosaccharides was used.
16263699	9	41	theme	research	1444:1451	arg1	projects					1453:1460	previous research projects	1435:1460	previous research projects	1435:1460	Comparison with the Swiss-Prot database established that the majority of these 70 sites have not been specifically determined by previous research projects.
16263699	6	42	theme	concanavalin	832:843	arg1	A					845:845	concanavalin A	832:845	concanavalin A	832:845	Therefore, concanavalin A was used for specific interaction with carbohydrate species along with periodic acid oxidation and hydrazide bead trapping of glycosylated proteins.
16263699	10	43	from	platelets	1715:1723	arg1	present					1698:1704	present	1698:1704	present	1698:1704	With this approach including hydrazide bead affinity trapping, the immunoglobulin receptor G6f, which is known to couple to the Ras-mitogen-activated protein kinase pathway in the immune system, was shown here for the first time to be present in human platelets.
16263699	10	43	from	platelets	1715:1723	arg1	G6f					1554:1556	the immunoglobulin receptor G6f	1526:1556	the immunoglobulin receptor G6f	1526:1556	With this approach including hydrazide bead affinity trapping, the immunoglobulin receptor G6f, which is known to couple to the Ras-mitogen-activated protein kinase pathway in the immune system, was shown here for the first time to be present in human platelets.
16263699	2	44	theme	storage	392:398	arg1	proteins					400:407	storage proteins	392:407	storage proteins (multimerin 1 etc.)	392:427	They account e.g. for secretory proteins and plasma membrane receptors including integrins and glycoprotein VI as well as intracellular components of cytosol and organelles including storage proteins (multimerin 1 etc.).
16263699	10	45	theme	protein	1613:1619	arg1	pathway					1628:1634	the Ras-mitogen-activated protein kinase pathway	1587:1634	the Ras-mitogen-activated protein kinase pathway in the immune system	1587:1655	With this approach including hydrazide bead affinity trapping, the immunoglobulin receptor G6f, which is known to couple to the Ras-mitogen-activated protein kinase pathway in the immune system, was shown here for the first time to be present in human platelets.
16263699	2	46	theme	organelles	371:380	arg1	integrins					290:298	integrins	290:298	integrins	290:298	They account e.g. for secretory proteins and plasma membrane receptors including integrins and glycoprotein VI as well as intracellular components of cytosol and organelles including storage proteins (multimerin 1 etc.).
16263699	2	46	theme	organelles	371:380	arg1	glycoprotein					304:315	glycoprotein VI	304:318	glycoprotein VI	304:318	They account e.g. for secretory proteins and plasma membrane receptors including integrins and glycoprotein VI as well as intracellular components of cytosol and organelles including storage proteins (multimerin 1 etc.).
16263699	2	46	theme	organelles	371:380	arg1	proteins					241:248	secretory proteins	231:248	secretory proteins	231:248	They account e.g. for secretory proteins and plasma membrane receptors including integrins and glycoprotein VI as well as intracellular components of cytosol and organelles including storage proteins (multimerin 1 etc.).
16263699	2	46	theme	organelles	371:380	arg1	components					345:354	intracellular components	331:354	secretory proteins and plasma membrane receptors including integrins and glycoprotein VI as well as intracellular components of cytosol and organelles including storage proteins (multimerin 1 etc.)	231:427	They account e.g. for secretory proteins and plasma membrane receptors including integrins and glycoprotein VI as well as intracellular components of cytosol and organelles including storage proteins (multimerin 1 etc.).
16263699	2	46	theme	organelles	371:380	arg1	receptors					270:278	plasma membrane receptors	254:278	plasma membrane receptors	254:278	They account e.g. for secretory proteins and plasma membrane receptors including integrins and glycoprotein VI as well as intracellular components of cytosol and organelles including storage proteins (multimerin 1 etc.).
16263699	6	47	theme	periodic	918:925	arg1	oxidation					932:940	periodic acid oxidation	918:940	periodic acid oxidation	918:940	Therefore, concanavalin A was used for specific interaction with carbohydrate species along with periodic acid oxidation and hydrazide bead trapping of glycosylated proteins.
16263699	1	48	gly	glycoprotein	186:197	arg1	glycoprotein					186:197	glycoprotein isoforms	186:206	glycoprotein isoforms	186:206	Among known platelet proteins, a prominent and functionally important group is represented by glycoprotein isoforms.
16263699	7	49	theme	proteins	1119:1126	arg1	elucidation					1104:1114	the elucidation	1100:1114	the elucidation of proteins and their sites of modification	1100:1158	Derivatization by peptide:N-glycosidase F yielded deglycosylated peptides, which provided the basis for the elucidation of proteins and their sites of modification.
16263699	8	50	gly	glycosylation	1240:1252	arg2	sites					1254:1258	70 different glycosylation sites	1227:1258	70 different glycosylation sites within 41 different proteins	1227:1287	Using both methods in combination with nano-LC-ESI-MS/MS analysis 70 different glycosylation sites within 41 different proteins were identified.
16263699	8	50	gly	glycosylation	1240:1252	arg2	70					1227:1228	70	1227:1228	70	1227:1228	Using both methods in combination with nano-LC-ESI-MS/MS analysis 70 different glycosylation sites within 41 different proteins were identified.
16263699	0	51	theme	platelet	46:53	arg1	proteins					55:62	human platelet proteins	40:62	human platelet proteins	40:62	Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach.
16263699	6	52	theme	carbohydrate	886:897	arg1	species					899:905	carbohydrate species	886:905	carbohydrate species along with periodic acid oxidation and hydrazide bead trapping of glycosylated proteins	886:993	Therefore, concanavalin A was used for specific interaction with carbohydrate species along with periodic acid oxidation and hydrazide bead trapping of glycosylated proteins.
16263699	4	53	theme	sites	646:650	arg1	analysis					618:625	the analysis	614:625	the analysis of N-glycosylation sites of human platelet proteins	614:677	Here we report the analysis of N-glycosylation sites of human platelet proteins.
16263699	4	54	theme	human	655:659	arg1	proteins					670:677	human platelet proteins	655:677	human platelet proteins	655:677	Here we report the analysis of N-glycosylation sites of human platelet proteins.
16263699	6	55	gly	glycosylated	973:984	arg1	proteins					986:993	glycosylated proteins	973:993	glycosylated proteins	973:993	Therefore, concanavalin A was used for specific interaction with carbohydrate species along with periodic acid oxidation and hydrazide bead trapping of glycosylated proteins.
16263699	8	56	theme	different	1230:1238	arg1	sites					1254:1258	70 different glycosylation sites	1227:1258	70 different glycosylation sites within 41 different proteins	1227:1287	Using both methods in combination with nano-LC-ESI-MS/MS analysis 70 different glycosylation sites within 41 different proteins were identified.
16263699	6	57	theme	glycosylated	973:984	arg1	proteins					986:993	glycosylated proteins	973:993	glycosylated proteins	973:993	Therefore, concanavalin A was used for specific interaction with carbohydrate species along with periodic acid oxidation and hydrazide bead trapping of glycosylated proteins.
16263699	3	58	gly	glycosylation	578:590	arg2	sites					592:596	their glycosylation sites	572:596	their glycosylation sites	572:596	Although many of those proteins have been studied for some time with regard to their function, little attention has been paid with respect to their glycosylation sites.
16263699	5	59	theme	glycopeptides	702:714	arg1	enrichment					688:697	the enrichment	684:697	the enrichment of glycopeptides	684:714	For the enrichment of glycopeptides, lectin affinity chromatography as well as chemical trapping of protein bound oligosaccharides was used.
16263699	3	60	theme	glycosylation	578:590	arg1	sites					592:596	their glycosylation sites	572:596	their glycosylation sites	572:596	Although many of those proteins have been studied for some time with regard to their function, little attention has been paid with respect to their glycosylation sites.
16263699	7	61	theme	deglycosylated	1046:1059	arg1	peptides					1061:1068	deglycosylated peptides	1046:1068	deglycosylated peptides	1046:1068	Derivatization by peptide:N-glycosidase F yielded deglycosylated peptides, which provided the basis for the elucidation of proteins and their sites of modification.
16263699	6	62	theme	hydrazide	946:954	arg1	trapping					961:968	hydrazide bead trapping	946:968	hydrazide bead trapping	946:968	Therefore, concanavalin A was used for specific interaction with carbohydrate species along with periodic acid oxidation and hydrazide bead trapping of glycosylated proteins.
16263699	5	63	gly	glycopeptides	702:714	arg2	glycopeptides					702:714	glycopeptides	702:714	glycopeptides	702:714	For the enrichment of glycopeptides, lectin affinity chromatography as well as chemical trapping of protein bound oligosaccharides was used.
16263699	9	64	theme	Swiss-Prot	1326:1335	arg1	database					1337:1344	the Swiss-Prot database	1322:1344	the Swiss-Prot database	1322:1344	Comparison with the Swiss-Prot database established that the majority of these 70 sites have not been specifically determined by previous research projects.
16263699	2	65	theme	plasma	254:259	arg1	glycoprotein					304:315	glycoprotein VI	304:318	glycoprotein VI	304:318	They account e.g. for secretory proteins and plasma membrane receptors including integrins and glycoprotein VI as well as intracellular components of cytosol and organelles including storage proteins (multimerin 1 etc.).
16263699	2	65	theme	plasma	254:259	arg1	integrins					290:298	integrins	290:298	integrins	290:298	They account e.g. for secretory proteins and plasma membrane receptors including integrins and glycoprotein VI as well as intracellular components of cytosol and organelles including storage proteins (multimerin 1 etc.).
16263699	2	65	theme	plasma	254:259	arg1	receptors					270:278	plasma membrane receptors	254:278	plasma membrane receptors	254:278	They account e.g. for secretory proteins and plasma membrane receptors including integrins and glycoprotein VI as well as intracellular components of cytosol and organelles including storage proteins (multimerin 1 etc.).
16263699	4	66	theme	proteins	670:677	arg1	proteins					670:677	human platelet proteins	655:677	human platelet proteins	655:677	Here we report the analysis of N-glycosylation sites of human platelet proteins.
16263699	4	66	theme	proteins	670:677	arg1	sites					646:650	N-glycosylation sites	630:650	N-glycosylation sites of human platelet proteins	630:677	Here we report the analysis of N-glycosylation sites of human platelet proteins.
16263699	5	67	theme	chemical	759:766	arg1	trapping					768:775	chemical trapping	759:775	lectin affinity chromatography as well as chemical trapping of protein bound oligosaccharides	717:809	For the enrichment of glycopeptides, lectin affinity chromatography as well as chemical trapping of protein bound oligosaccharides was used.
16263699	1	68	theme	important	152:160	arg1	group					162:166	a prominent and functionally important group	123:166	a prominent and functionally important group	123:166	Among known platelet proteins, a prominent and functionally important group is represented by glycoprotein isoforms.
16263699	5	69	theme	lectin	717:722	arg1	chromatography					733:746	lectin affinity chromatography	717:746	lectin affinity chromatography as well as chemical trapping of protein bound oligosaccharides	717:809	For the enrichment of glycopeptides, lectin affinity chromatography as well as chemical trapping of protein bound oligosaccharides was used.
16263699	10	70	theme	bead	1502:1505	arg1	trapping					1516:1523	hydrazide bead affinity trapping	1492:1523	hydrazide bead affinity trapping	1492:1523	With this approach including hydrazide bead affinity trapping, the immunoglobulin receptor G6f, which is known to couple to the Ras-mitogen-activated protein kinase pathway in the immune system, was shown here for the first time to be present in human platelets.
16263699	10	71	theme	receptor	1545:1552	arg1	present					1698:1704	present	1698:1704	present	1698:1704	With this approach including hydrazide bead affinity trapping, the immunoglobulin receptor G6f, which is known to couple to the Ras-mitogen-activated protein kinase pathway in the immune system, was shown here for the first time to be present in human platelets.
16263699	10	71	theme	receptor	1545:1552	arg1	G6f					1554:1556	the immunoglobulin receptor G6f	1526:1556	the immunoglobulin receptor G6f	1526:1556	With this approach including hydrazide bead affinity trapping, the immunoglobulin receptor G6f, which is known to couple to the Ras-mitogen-activated protein kinase pathway in the immune system, was shown here for the first time to be present in human platelets.
16263699	9	72	with	Comparison	1306:1315	arg1	database					1337:1344	the Swiss-Prot database	1322:1344	the Swiss-Prot database	1322:1344	Comparison with the Swiss-Prot database established that the majority of these 70 sites have not been specifically determined by previous research projects.
16263699	0	73	dep	approach	82:89	arg1	Elucidation					0:10	Elucidation	0:10	Elucidation of N-glycosylation sites on human platelet proteins	0:62	Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach.
16263699	6	74	with	interaction	869:879	arg1	species					899:905	carbohydrate species	886:905	carbohydrate species along with periodic acid oxidation and hydrazide bead trapping of glycosylated proteins	886:993	Therefore, concanavalin A was used for specific interaction with carbohydrate species along with periodic acid oxidation and hydrazide bead trapping of glycosylated proteins.
16263699	6	74	with	interaction	869:879	arg1	oxidation					932:940	periodic acid oxidation	918:940	periodic acid oxidation	918:940	Therefore, concanavalin A was used for specific interaction with carbohydrate species along with periodic acid oxidation and hydrazide bead trapping of glycosylated proteins.
16263699	8	75	with	combination	1183:1193	arg1	analysis					1218:1225	nano-LC-ESI-MS/MS analysis	1200:1225	nano-LC-ESI-MS/MS analysis	1200:1225	Using both methods in combination with nano-LC-ESI-MS/MS analysis 70 different glycosylation sites within 41 different proteins were identified.
16263699	0	76	theme	sites	31:35	arg1	Elucidation					0:10	Elucidation	0:10	Elucidation of N-glycosylation sites on human platelet proteins	0:62	Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach.
16263699	1	77	theme	known	98:102	arg1	proteins					113:120	known platelet proteins	98:120	known platelet proteins	98:120	Among known platelet proteins, a prominent and functionally important group is represented by glycoprotein isoforms.
16263699	6	78	used	used	851:854	arg2	A					845:845	concanavalin A	832:845	concanavalin A	832:845	Therefore, concanavalin A was used for specific interaction with carbohydrate species along with periodic acid oxidation and hydrazide bead trapping of glycosylated proteins.
16263699	6	79	theme	specific	860:867	arg1	interaction					869:879	specific interaction	860:879	specific interaction with carbohydrate species along with periodic acid oxidation and hydrazide bead trapping of glycosylated proteins	860:993	Therefore, concanavalin A was used for specific interaction with carbohydrate species along with periodic acid oxidation and hydrazide bead trapping of glycosylated proteins.
16263699	7	80	gly	deglycosylated	1046:1059	arg1	peptides					1061:1068	deglycosylated peptides	1046:1068	deglycosylated peptides	1046:1068	Derivatization by peptide:N-glycosidase F yielded deglycosylated peptides, which provided the basis for the elucidation of proteins and their sites of modification.
16263699	10	81	theme	human	1709:1713	arg1	platelets					1715:1723	human platelets	1709:1723	human platelets	1709:1723	With this approach including hydrazide bead affinity trapping, the immunoglobulin receptor G6f, which is known to couple to the Ras-mitogen-activated protein kinase pathway in the immune system, was shown here for the first time to be present in human platelets.
16263699	5	82	theme	bound	788:792	arg1	oligosaccharides					794:809	protein bound oligosaccharides	780:809	protein bound oligosaccharides	780:809	For the enrichment of glycopeptides, lectin affinity chromatography as well as chemical trapping of protein bound oligosaccharides was used.
16263699	0	83	gly	N-glycosylation	15:29	arg2	sites					31:35	N-glycosylation sites	15:35	N-glycosylation sites	15:35	Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach.
16263699	9	84	theme	previous	1435:1442	arg1	projects					1453:1460	previous research projects	1435:1460	previous research projects	1435:1460	Comparison with the Swiss-Prot database established that the majority of these 70 sites have not been specifically determined by previous research projects.
16263699	5	85	used	used	815:818	arg2	trapping					768:775	chemical trapping	759:775	lectin affinity chromatography as well as chemical trapping of protein bound oligosaccharides	717:809	For the enrichment of glycopeptides, lectin affinity chromatography as well as chemical trapping of protein bound oligosaccharides was used.
16263699	5	85	used	used	815:818	arg2	chromatography					733:746	lectin affinity chromatography	717:746	lectin affinity chromatography as well as chemical trapping of protein bound oligosaccharides	717:809	For the enrichment of glycopeptides, lectin affinity chromatography as well as chemical trapping of protein bound oligosaccharides was used.
16263699	10	86	from	present	1698:1704	arg1	platelets					1715:1723	human platelets	1709:1723	human platelets	1709:1723	With this approach including hydrazide bead affinity trapping, the immunoglobulin receptor G6f, which is known to couple to the Ras-mitogen-activated protein kinase pathway in the immune system, was shown here for the first time to be present in human platelets.
16263699	2	87	dep	proteins	400:407	arg1	multimerin					410:419	multimerin	410:419	multimerin 1 etc.	410:426	They account e.g. for secretory proteins and plasma membrane receptors including integrins and glycoprotein VI as well as intracellular components of cytosol and organelles including storage proteins (multimerin 1 etc.).
16263699	2	88	theme	intracellular	331:343	arg1	glycoprotein					304:315	glycoprotein VI	304:318	glycoprotein VI	304:318	They account e.g. for secretory proteins and plasma membrane receptors including integrins and glycoprotein VI as well as intracellular components of cytosol and organelles including storage proteins (multimerin 1 etc.).
16263699	2	88	theme	intracellular	331:343	arg1	components					345:354	intracellular components	331:354	secretory proteins and plasma membrane receptors including integrins and glycoprotein VI as well as intracellular components of cytosol and organelles including storage proteins (multimerin 1 etc.)	231:427	They account e.g. for secretory proteins and plasma membrane receptors including integrins and glycoprotein VI as well as intracellular components of cytosol and organelles including storage proteins (multimerin 1 etc.).
16263699	2	88	theme	intracellular	331:343	arg1	integrins					290:298	integrins	290:298	integrins	290:298	They account e.g. for secretory proteins and plasma membrane receptors including integrins and glycoprotein VI as well as intracellular components of cytosol and organelles including storage proteins (multimerin 1 etc.).
16263699	6	89	dep	along	907:911	arg1	with					913:916	with	913:916	with	913:916	Therefore, concanavalin A was used for specific interaction with carbohydrate species along with periodic acid oxidation and hydrazide bead trapping of glycosylated proteins.
16263699	10	90	theme	kinase	1621:1626	arg1	pathway					1628:1634	the Ras-mitogen-activated protein kinase pathway	1587:1634	the Ras-mitogen-activated protein kinase pathway in the immune system	1587:1655	With this approach including hydrazide bead affinity trapping, the immunoglobulin receptor G6f, which is known to couple to the Ras-mitogen-activated protein kinase pathway in the immune system, was shown here for the first time to be present in human platelets.
16263699	2	91	dep	multimerin	410:419	arg1	etc					423:425	1 etc	421:425	multimerin 1 etc.	410:426	They account e.g. for secretory proteins and plasma membrane receptors including integrins and glycoprotein VI as well as intracellular components of cytosol and organelles including storage proteins (multimerin 1 etc.).
15737642	0	0	theme	biological	70:79	arg1	function					81:88	the biological function	66:88	the biological function of beta1,3-N-acetylglucosaminyltransferase 2 and its secretion	66:151	The effects of N-glycosylation sites and the N-terminal region on the biological function of beta1,3-N-acetylglucosaminyltransferase 2 and its secretion.
15737642	2	1	theme	site-directed	502:514	arg1	mutagenesis					516:526	site-directed mutagenesis	502:526	site-directed mutagenesis of potential N-glycosylation sites	502:561	To obtain insight into the structure of beta3GnT2, the effects of N-glycosylation on its biological function were evaluated using the addition of inhibitors, site-directed mutagenesis of potential N-glycosylation sites, and deletion of its N-terminal region using a fusion protein with GFP(uv) in a baculovirus expression system.
15737642	4	2	theme	beta3GnT	919:926	arg1	activity					928:935	the beta3GnT activity	915:935	the beta3GnT activity	915:935	The N-glycosylation at Asn219 was necessary for the beta3GnT activity; moreover, N-glycosylation at Asn127 and Asn219 was critical for efficient protein secretion.
15737642	6	3	theme	uv	1298:1299	arg1	-beta3GnT2Delta83					1301:1317	GFP(uv)-beta3GnT2Delta83	1294:1317	GFP(uv)-beta3GnT2Delta83	1294:1317	The truncated protein consisting of amino acids 82-397 (GFP(uv)-beta3GnT2Delta83), which lacked both one N-glycosylation site at Asn79 and the stem region of glycosyltransferase, was expressed as only a small form and showed no beta3GnT activity.
15737642	6	3	theme	uv	1298:1299	arg1	82-397					1286:1291	82-397	1286:1291	82-397	1286:1291	The truncated protein consisting of amino acids 82-397 (GFP(uv)-beta3GnT2Delta83), which lacked both one N-glycosylation site at Asn79 and the stem region of glycosyltransferase, was expressed as only a small form and showed no beta3GnT activity.
15737642	5	4	gly	glycosylation	1213:1225	arg2	Asn219					1230:1235	Asn219	1230:1235	Asn219	1230:1235	When Ser221 was replaced with Thr, fusion protein was expressed as a single band, indicating that the double band of the expressed fusion protein was due to the heterogeneity of the glycosylation at Asn219.
15737642	5	4	gly	glycosylation	1213:1225	arg1	Asn219					1230:1235	Asn219	1230:1235	Asn219	1230:1235	When Ser221 was replaced with Thr, fusion protein was expressed as a single band, indicating that the double band of the expressed fusion protein was due to the heterogeneity of the glycosylation at Asn219.
15737642	1	5	theme	acceptor	274:281	arg1	chains					283:288	the polylactosamine acceptor chains	254:288	the polylactosamine acceptor chains	254:288	Human beta1,3-N-acetylglucosaminyltransferase 2 (beta3GnT2) is thought to be an enzyme that extends the polylactosamine acceptor chains, but its function and structure analysis are unknown.
15737642	6	6	theme	N-glycosylation	1343:1357	arg1	site					1359:1362	one N-glycosylation site	1339:1362	one N-glycosylation site at Asn79	1339:1371	The truncated protein consisting of amino acids 82-397 (GFP(uv)-beta3GnT2Delta83), which lacked both one N-glycosylation site at Asn79 and the stem region of glycosyltransferase, was expressed as only a small form and showed no beta3GnT activity.
15737642	6	6	theme	N-glycosylation	1343:1357	arg1	glycosyltransferase					1396:1414	glycosyltransferase	1396:1414	glycosyltransferase	1396:1414	The truncated protein consisting of amino acids 82-397 (GFP(uv)-beta3GnT2Delta83), which lacked both one N-glycosylation site at Asn79 and the stem region of glycosyltransferase, was expressed as only a small form and showed no beta3GnT activity.
15737642	0	7	from	effects	4:10	arg1	function					81:88	the biological function	66:88	the biological function of beta1,3-N-acetylglucosaminyltransferase 2 and its secretion	66:151	The effects of N-glycosylation sites and the N-terminal region on the biological function of beta1,3-N-acetylglucosaminyltransferase 2 and its secretion.
15737642	4	8	theme	at	887:888	arg1	Asn219					890:895	The N-glycosylation at Asn219	867:895	The N-glycosylation at Asn219	867:895	The N-glycosylation at Asn219 was necessary for the beta3GnT activity; moreover, N-glycosylation at Asn127 and Asn219 was critical for efficient protein secretion.
15737642	4	8	theme	at	887:888	arg1	necessary					901:909	necessary	901:909	necessary	901:909	The N-glycosylation at Asn219 was necessary for the beta3GnT activity; moreover, N-glycosylation at Asn127 and Asn219 was critical for efficient protein secretion.
15737642	8	9	theme	active	1820:1825	arg1	structure					1835:1843	the active protein structure	1816:1843	the active protein structure	1816:1843	The N-terminal region, which belongs to a stem region of glycosyltransferase, might also be important to the active protein structure.
15737642	2	10	theme	potential	531:539	arg1	sites					557:561	potential N-glycosylation sites	531:561	potential N-glycosylation sites	531:561	To obtain insight into the structure of beta3GnT2, the effects of N-glycosylation on its biological function were evaluated using the addition of inhibitors, site-directed mutagenesis of potential N-glycosylation sites, and deletion of its N-terminal region using a fusion protein with GFP(uv) in a baculovirus expression system.
15737642	3	11	theme	N-glycosylation	697:711	arg1	sites					713:717	Four of five potential N-glycosylation sites	674:717	Four of five potential N-glycosylation sites	674:717	Four of five potential N-glycosylation sites were found to be occupied, and their biological function and secretion were inhibited with the treatment of N-glycosylation inhibitor, tunicamycin.
15737642	6	12	theme	amino	1274:1278	arg1	acids					1280:1284	amino acids 82-397 (GFP(uv)-beta3GnT2Delta83)	1274:1318	amino acids 82-397 (GFP(uv)-beta3GnT2Delta83)	1274:1318	The truncated protein consisting of amino acids 82-397 (GFP(uv)-beta3GnT2Delta83), which lacked both one N-glycosylation site at Asn79 and the stem region of glycosyltransferase, was expressed as only a small form and showed no beta3GnT activity.
15737642	2	13	theme	expression	655:664	arg1	system					666:671	a baculovirus expression system	641:671	a baculovirus expression system	641:671	To obtain insight into the structure of beta3GnT2, the effects of N-glycosylation on its biological function were evaluated using the addition of inhibitors, site-directed mutagenesis of potential N-glycosylation sites, and deletion of its N-terminal region using a fusion protein with GFP(uv) in a baculovirus expression system.
15737642	3	14	used	occupied	736:743	arg2	sites					713:717	Four of five potential N-glycosylation sites	674:717	Four of five potential N-glycosylation sites	674:717	Four of five potential N-glycosylation sites were found to be occupied, and their biological function and secretion were inhibited with the treatment of N-glycosylation inhibitor, tunicamycin.
15737642	2	15	theme	sites	557:561	arg1	mutagenesis					516:526	site-directed mutagenesis	502:526	site-directed mutagenesis of potential N-glycosylation sites	502:561	To obtain insight into the structure of beta3GnT2, the effects of N-glycosylation on its biological function were evaluated using the addition of inhibitors, site-directed mutagenesis of potential N-glycosylation sites, and deletion of its N-terminal region using a fusion protein with GFP(uv) in a baculovirus expression system.
15737642	2	15	theme	sites	557:561	arg1	addition					478:485	the addition	474:485	the addition of inhibitors	474:499	To obtain insight into the structure of beta3GnT2, the effects of N-glycosylation on its biological function were evaluated using the addition of inhibitors, site-directed mutagenesis of potential N-glycosylation sites, and deletion of its N-terminal region using a fusion protein with GFP(uv) in a baculovirus expression system.
15737642	2	15	theme	sites	557:561	arg1	deletion					568:575	deletion	568:575	deletion of its N-terminal region using a fusion protein with GFP(uv) in a baculovirus expression system	568:671	To obtain insight into the structure of beta3GnT2, the effects of N-glycosylation on its biological function were evaluated using the addition of inhibitors, site-directed mutagenesis of potential N-glycosylation sites, and deletion of its N-terminal region using a fusion protein with GFP(uv) in a baculovirus expression system.
15737642	5	16	theme	single	1100:1105	arg1	protein					1073:1079	fusion protein	1066:1079	fusion protein	1066:1079	When Ser221 was replaced with Thr, fusion protein was expressed as a single band, indicating that the double band of the expressed fusion protein was due to the heterogeneity of the glycosylation at Asn219.
15737642	5	16	theme	single	1100:1105	arg1	band					1107:1110	a single band	1098:1110	a single band	1098:1110	When Ser221 was replaced with Thr, fusion protein was expressed as a single band, indicating that the double band of the expressed fusion protein was due to the heterogeneity of the glycosylation at Asn219.
15737642	2	17	theme	fusion	610:615	arg1	protein					617:623	a fusion protein	608:623	a fusion protein with GFP(uv) in a baculovirus expression system	608:671	To obtain insight into the structure of beta3GnT2, the effects of N-glycosylation on its biological function were evaluated using the addition of inhibitors, site-directed mutagenesis of potential N-glycosylation sites, and deletion of its N-terminal region using a fusion protein with GFP(uv) in a baculovirus expression system.
15737642	2	18	theme	baculovirus	643:653	arg1	system					666:671	a baculovirus expression system	641:671	a baculovirus expression system	641:671	To obtain insight into the structure of beta3GnT2, the effects of N-glycosylation on its biological function were evaluated using the addition of inhibitors, site-directed mutagenesis of potential N-glycosylation sites, and deletion of its N-terminal region using a fusion protein with GFP(uv) in a baculovirus expression system.
15737642	2	19	with	protein	617:623	arg1	uv					634:635	uv	634:635	uv	634:635	To obtain insight into the structure of beta3GnT2, the effects of N-glycosylation on its biological function were evaluated using the addition of inhibitors, site-directed mutagenesis of potential N-glycosylation sites, and deletion of its N-terminal region using a fusion protein with GFP(uv) in a baculovirus expression system.
15737642	2	19	with	protein	617:623	arg1	GFP					630:632	GFP	630:632	GFP(uv) in a baculovirus expression system	630:671	To obtain insight into the structure of beta3GnT2, the effects of N-glycosylation on its biological function were evaluated using the addition of inhibitors, site-directed mutagenesis of potential N-glycosylation sites, and deletion of its N-terminal region using a fusion protein with GFP(uv) in a baculovirus expression system.
15737642	3	20	theme	N-glycosylation	827:841	arg1	tunicamycin					854:864	N-glycosylation inhibitor, tunicamycin	827:864	tunicamycin	854:864	Four of five potential N-glycosylation sites were found to be occupied, and their biological function and secretion were inhibited with the treatment of N-glycosylation inhibitor, tunicamycin.
15737642	2	21	theme	N-glycosylation	541:555	arg1	sites					557:561	potential N-glycosylation sites	531:561	potential N-glycosylation sites	531:561	To obtain insight into the structure of beta3GnT2, the effects of N-glycosylation on its biological function were evaluated using the addition of inhibitors, site-directed mutagenesis of potential N-glycosylation sites, and deletion of its N-terminal region using a fusion protein with GFP(uv) in a baculovirus expression system.
15737642	7	22	theme	biological	1663:1672	arg1	function					1674:1681	its biological function	1659:1681	its biological function	1659:1681	These results suggest that the N-glycosylation site at Asn219, which is conserved throughout the beta1,3-glycosyltransferase family, is indispensable not only with regard to its biological function, but also to its secretion.
15737642	8	23	theme	glycosyltransferase	1768:1786	arg1	region					1758:1763	a stem region	1751:1763	a stem region of glycosyltransferase	1751:1786	The N-terminal region, which belongs to a stem region of glycosyltransferase, might also be important to the active protein structure.
15737642	0	24	theme	beta1,3-N-acetylglucosaminyltransferase	93:131	arg1	function					81:88	the biological function	66:88	the biological function of beta1,3-N-acetylglucosaminyltransferase 2 and its secretion	66:151	The effects of N-glycosylation sites and the N-terminal region on the biological function of beta1,3-N-acetylglucosaminyltransferase 2 and its secretion.
15737642	3	25	theme	inhibitor	843:851	arg1	tunicamycin					854:864	N-glycosylation inhibitor, tunicamycin	827:864	tunicamycin	854:864	Four of five potential N-glycosylation sites were found to be occupied, and their biological function and secretion were inhibited with the treatment of N-glycosylation inhibitor, tunicamycin.
15737642	5	26	gly	heterogeneity	1192:1204	arg1	glycosylation					1213:1225	the glycosylation	1209:1225	the glycosylation at Asn219	1209:1235	When Ser221 was replaced with Thr, fusion protein was expressed as a single band, indicating that the double band of the expressed fusion protein was due to the heterogeneity of the glycosylation at Asn219.
15737642	2	27	gly	N-glycosylation	541:555	arg2	sites					557:561	potential N-glycosylation sites	531:561	potential N-glycosylation sites	531:561	To obtain insight into the structure of beta3GnT2, the effects of N-glycosylation on its biological function were evaluated using the addition of inhibitors, site-directed mutagenesis of potential N-glycosylation sites, and deletion of its N-terminal region using a fusion protein with GFP(uv) in a baculovirus expression system.
15737642	7	28	from	Asn219	1540:1545	arg1	site					1532:1535	the N-glycosylation site	1512:1535	the N-glycosylation site	1512:1535	These results suggest that the N-glycosylation site at Asn219, which is conserved throughout the beta1,3-glycosyltransferase family, is indispensable not only with regard to its biological function, but also to its secretion.
15737642	7	28	from	Asn219	1540:1545	arg1	indispensable					1621:1633	indispensable	1621:1633	indispensable	1621:1633	These results suggest that the N-glycosylation site at Asn219, which is conserved throughout the beta1,3-glycosyltransferase family, is indispensable not only with regard to its biological function, but also to its secretion.
15737642	5	29	theme	expressed	1152:1160	arg1	protein					1169:1175	the expressed fusion protein	1148:1175	the expressed fusion protein	1148:1175	When Ser221 was replaced with Thr, fusion protein was expressed as a single band, indicating that the double band of the expressed fusion protein was due to the heterogeneity of the glycosylation at Asn219.
15737642	4	30	theme	N-glycosylation	871:885	arg1	Asn219					890:895	The N-glycosylation at Asn219	867:895	The N-glycosylation at Asn219	867:895	The N-glycosylation at Asn219 was necessary for the beta3GnT activity; moreover, N-glycosylation at Asn127 and Asn219 was critical for efficient protein secretion.
15737642	4	30	theme	N-glycosylation	871:885	arg1	necessary					901:909	necessary	901:909	necessary	901:909	The N-glycosylation at Asn219 was necessary for the beta3GnT activity; moreover, N-glycosylation at Asn127 and Asn219 was critical for efficient protein secretion.
15737642	5	31	theme	protein	1169:1175	arg1	due					1181:1183	due	1181:1183	due	1181:1183	When Ser221 was replaced with Thr, fusion protein was expressed as a single band, indicating that the double band of the expressed fusion protein was due to the heterogeneity of the glycosylation at Asn219.
15737642	5	31	theme	protein	1169:1175	arg1	band					1140:1143	the double band	1129:1143	the double band of the expressed fusion protein	1129:1175	When Ser221 was replaced with Thr, fusion protein was expressed as a single band, indicating that the double band of the expressed fusion protein was due to the heterogeneity of the glycosylation at Asn219.
15737642	3	32	theme	potential	687:695	arg1	sites					713:717	Four of five potential N-glycosylation sites	674:717	Four of five potential N-glycosylation sites	674:717	Four of five potential N-glycosylation sites were found to be occupied, and their biological function and secretion were inhibited with the treatment of N-glycosylation inhibitor, tunicamycin.
15737642	4	33	from	Asn219	978:983	arg1	N-glycosylation					948:962	N-glycosylation	948:962	N-glycosylation at Asn127 and Asn219	948:983	The N-glycosylation at Asn219 was necessary for the beta3GnT activity; moreover, N-glycosylation at Asn127 and Asn219 was critical for efficient protein secretion.
15737642	5	34	theme	double	1133:1138	arg1	due					1181:1183	due	1181:1183	due	1181:1183	When Ser221 was replaced with Thr, fusion protein was expressed as a single band, indicating that the double band of the expressed fusion protein was due to the heterogeneity of the glycosylation at Asn219.
15737642	5	34	theme	double	1133:1138	arg1	band					1140:1143	the double band	1129:1143	the double band of the expressed fusion protein	1129:1175	When Ser221 was replaced with Thr, fusion protein was expressed as a single band, indicating that the double band of the expressed fusion protein was due to the heterogeneity of the glycosylation at Asn219.
15737642	0	35	theme	N-glycosylation	15:29	arg1	sites					31:35	N-glycosylation sites	15:35	N-glycosylation sites	15:35	The effects of N-glycosylation sites and the N-terminal region on the biological function of beta1,3-N-acetylglucosaminyltransferase 2 and its secretion.
15737642	3	36	theme	biological	756:765	arg1	function					767:774	their biological function	750:774	their biological function	750:774	Four of five potential N-glycosylation sites were found to be occupied, and their biological function and secretion were inhibited with the treatment of N-glycosylation inhibitor, tunicamycin.
15737642	6	37	from	Asn79	1367:1371	arg1	site					1359:1362	one N-glycosylation site	1339:1362	one N-glycosylation site at Asn79	1339:1371	The truncated protein consisting of amino acids 82-397 (GFP(uv)-beta3GnT2Delta83), which lacked both one N-glycosylation site at Asn79 and the stem region of glycosyltransferase, was expressed as only a small form and showed no beta3GnT activity.
15737642	6	37	from	Asn79	1367:1371	arg1	region					1386:1391	the stem region	1377:1391	the stem region of glycosyltransferase	1377:1414	The truncated protein consisting of amino acids 82-397 (GFP(uv)-beta3GnT2Delta83), which lacked both one N-glycosylation site at Asn79 and the stem region of glycosyltransferase, was expressed as only a small form and showed no beta3GnT activity.
15737642	6	37	from	Asn79	1367:1371	arg1	glycosyltransferase					1396:1414	glycosyltransferase	1396:1414	glycosyltransferase	1396:1414	The truncated protein consisting of amino acids 82-397 (GFP(uv)-beta3GnT2Delta83), which lacked both one N-glycosylation site at Asn79 and the stem region of glycosyltransferase, was expressed as only a small form and showed no beta3GnT activity.
15737642	7	38	theme	N-glycosylation	1516:1530	arg1	site					1532:1535	the N-glycosylation site	1512:1535	the N-glycosylation site	1512:1535	These results suggest that the N-glycosylation site at Asn219, which is conserved throughout the beta1,3-glycosyltransferase family, is indispensable not only with regard to its biological function, but also to its secretion.
15737642	7	38	theme	N-glycosylation	1516:1530	arg1	indispensable					1621:1633	indispensable	1621:1633	indispensable	1621:1633	These results suggest that the N-glycosylation site at Asn219, which is conserved throughout the beta1,3-glycosyltransferase family, is indispensable not only with regard to its biological function, but also to its secretion.
15737642	2	39	theme	biological	433:442	arg1	function					444:451	its biological function	429:451	its biological function	429:451	To obtain insight into the structure of beta3GnT2, the effects of N-glycosylation on its biological function were evaluated using the addition of inhibitors, site-directed mutagenesis of potential N-glycosylation sites, and deletion of its N-terminal region using a fusion protein with GFP(uv) in a baculovirus expression system.
15737642	2	40	from	GFP	630:632	arg1	system					666:671	a baculovirus expression system	641:671	a baculovirus expression system	641:671	To obtain insight into the structure of beta3GnT2, the effects of N-glycosylation on its biological function were evaluated using the addition of inhibitors, site-directed mutagenesis of potential N-glycosylation sites, and deletion of its N-terminal region using a fusion protein with GFP(uv) in a baculovirus expression system.
15737642	6	41	theme	stem	1381:1384	arg1	region					1386:1391	the stem region	1377:1391	the stem region of glycosyltransferase	1377:1414	The truncated protein consisting of amino acids 82-397 (GFP(uv)-beta3GnT2Delta83), which lacked both one N-glycosylation site at Asn79 and the stem region of glycosyltransferase, was expressed as only a small form and showed no beta3GnT activity.
15737642	6	42	theme	beta3GnT	1466:1473	arg1	activity					1475:1482	no beta3GnT activity	1463:1482	no beta3GnT activity	1463:1482	The truncated protein consisting of amino acids 82-397 (GFP(uv)-beta3GnT2Delta83), which lacked both one N-glycosylation site at Asn79 and the stem region of glycosyltransferase, was expressed as only a small form and showed no beta3GnT activity.
15737642	6	42	theme	beta3GnT	1466:1473	arg1	form					1447:1450	only a small form	1434:1450	only a small form	1434:1450	The truncated protein consisting of amino acids 82-397 (GFP(uv)-beta3GnT2Delta83), which lacked both one N-glycosylation site at Asn79 and the stem region of glycosyltransferase, was expressed as only a small form and showed no beta3GnT activity.
15737642	6	42	theme	beta3GnT	1466:1473	arg1	protein					1252:1258	The truncated protein	1238:1258	The truncated protein	1238:1258	The truncated protein consisting of amino acids 82-397 (GFP(uv)-beta3GnT2Delta83), which lacked both one N-glycosylation site at Asn79 and the stem region of glycosyltransferase, was expressed as only a small form and showed no beta3GnT activity.
15737642	1	43	theme	Human	154:158	arg1	beta1,3-N-acetylglucosaminyltransferase					160:198	Human beta1,3-N-acetylglucosaminyltransferase 2	154:200	Human beta1,3-N-acetylglucosaminyltransferase 2 (beta3GnT2)	154:212	Human beta1,3-N-acetylglucosaminyltransferase 2 (beta3GnT2) is thought to be an enzyme that extends the polylactosamine acceptor chains, but its function and structure analysis are unknown.
15737642	1	43	theme	Human	154:158	arg1	beta3GnT2					203:211	beta3GnT2	203:211	beta3GnT2	203:211	Human beta1,3-N-acetylglucosaminyltransferase 2 (beta3GnT2) is thought to be an enzyme that extends the polylactosamine acceptor chains, but its function and structure analysis are unknown.
15737642	1	43	theme	Human	154:158	arg1	enzyme					234:239	an enzyme	231:239	an enzyme that extends the polylactosamine acceptor chains	231:288	Human beta1,3-N-acetylglucosaminyltransferase 2 (beta3GnT2) is thought to be an enzyme that extends the polylactosamine acceptor chains, but its function and structure analysis are unknown.
15737642	2	44	theme	inhibitors	490:499	arg1	mutagenesis					516:526	site-directed mutagenesis	502:526	site-directed mutagenesis of potential N-glycosylation sites	502:561	To obtain insight into the structure of beta3GnT2, the effects of N-glycosylation on its biological function were evaluated using the addition of inhibitors, site-directed mutagenesis of potential N-glycosylation sites, and deletion of its N-terminal region using a fusion protein with GFP(uv) in a baculovirus expression system.
15737642	2	44	theme	inhibitors	490:499	arg1	addition					478:485	the addition	474:485	the addition of inhibitors	474:499	To obtain insight into the structure of beta3GnT2, the effects of N-glycosylation on its biological function were evaluated using the addition of inhibitors, site-directed mutagenesis of potential N-glycosylation sites, and deletion of its N-terminal region using a fusion protein with GFP(uv) in a baculovirus expression system.
15737642	2	44	theme	inhibitors	490:499	arg1	deletion					568:575	deletion	568:575	deletion of its N-terminal region using a fusion protein with GFP(uv) in a baculovirus expression system	568:671	To obtain insight into the structure of beta3GnT2, the effects of N-glycosylation on its biological function were evaluated using the addition of inhibitors, site-directed mutagenesis of potential N-glycosylation sites, and deletion of its N-terminal region using a fusion protein with GFP(uv) in a baculovirus expression system.
15737642	1	45	theme	structure	312:320	arg1	analysis					322:329	structure analysis	312:329	structure analysis	312:329	Human beta1,3-N-acetylglucosaminyltransferase 2 (beta3GnT2) is thought to be an enzyme that extends the polylactosamine acceptor chains, but its function and structure analysis are unknown.
15737642	6	46	theme	truncated	1242:1250	arg1	protein					1252:1258	The truncated protein	1238:1258	The truncated protein	1238:1258	The truncated protein consisting of amino acids 82-397 (GFP(uv)-beta3GnT2Delta83), which lacked both one N-glycosylation site at Asn79 and the stem region of glycosyltransferase, was expressed as only a small form and showed no beta3GnT activity.
15737642	6	46	theme	truncated	1242:1250	arg1	form					1447:1450	only a small form	1434:1450	only a small form	1434:1450	The truncated protein consisting of amino acids 82-397 (GFP(uv)-beta3GnT2Delta83), which lacked both one N-glycosylation site at Asn79 and the stem region of glycosyltransferase, was expressed as only a small form and showed no beta3GnT activity.
15737642	6	46	theme	truncated	1242:1250	arg1	activity					1475:1482	no beta3GnT activity	1463:1482	no beta3GnT activity	1463:1482	The truncated protein consisting of amino acids 82-397 (GFP(uv)-beta3GnT2Delta83), which lacked both one N-glycosylation site at Asn79 and the stem region of glycosyltransferase, was expressed as only a small form and showed no beta3GnT activity.
15737642	0	47	theme	sites	31:35	arg1	effects					4:10	The effects	0:10	The effects of N-glycosylation sites and the N-terminal region on the biological function of beta1,3-N-acetylglucosaminyltransferase 2 and its secretion	0:151	The effects of N-glycosylation sites and the N-terminal region on the biological function of beta1,3-N-acetylglucosaminyltransferase 2 and its secretion.
15737642	0	48	theme	secretion	143:151	arg1	function					81:88	the biological function	66:88	the biological function of beta1,3-N-acetylglucosaminyltransferase 2 and its secretion	66:151	The effects of N-glycosylation sites and the N-terminal region on the biological function of beta1,3-N-acetylglucosaminyltransferase 2 and its secretion.
15737642	6	49	theme	glycosyltransferase	1396:1414	arg1	site					1359:1362	one N-glycosylation site	1339:1362	one N-glycosylation site at Asn79	1339:1371	The truncated protein consisting of amino acids 82-397 (GFP(uv)-beta3GnT2Delta83), which lacked both one N-glycosylation site at Asn79 and the stem region of glycosyltransferase, was expressed as only a small form and showed no beta3GnT activity.
15737642	6	49	theme	glycosyltransferase	1396:1414	arg1	region					1386:1391	the stem region	1377:1391	the stem region of glycosyltransferase	1377:1414	The truncated protein consisting of amino acids 82-397 (GFP(uv)-beta3GnT2Delta83), which lacked both one N-glycosylation site at Asn79 and the stem region of glycosyltransferase, was expressed as only a small form and showed no beta3GnT activity.
15737642	6	49	theme	glycosyltransferase	1396:1414	arg1	glycosyltransferase					1396:1414	glycosyltransferase	1396:1414	glycosyltransferase	1396:1414	The truncated protein consisting of amino acids 82-397 (GFP(uv)-beta3GnT2Delta83), which lacked both one N-glycosylation site at Asn79 and the stem region of glycosyltransferase, was expressed as only a small form and showed no beta3GnT activity.
15737642	2	50	theme	N-glycosylation	410:424	arg1	effects					399:405	the effects	395:405	the effects of N-glycosylation on its biological function	395:451	To obtain insight into the structure of beta3GnT2, the effects of N-glycosylation on its biological function were evaluated using the addition of inhibitors, site-directed mutagenesis of potential N-glycosylation sites, and deletion of its N-terminal region using a fusion protein with GFP(uv) in a baculovirus expression system.
15737642	0	51	theme	N-terminal	45:54	arg1	region					56:61	the N-terminal region	41:61	the N-terminal region	41:61	The effects of N-glycosylation sites and the N-terminal region on the biological function of beta1,3-N-acetylglucosaminyltransferase 2 and its secretion.
15737642	7	52	theme	beta1,3-glycosyltransferase	1582:1608	arg1	family					1610:1615	the beta1,3-glycosyltransferase family	1578:1615	the beta1,3-glycosyltransferase family	1578:1615	These results suggest that the N-glycosylation site at Asn219, which is conserved throughout the beta1,3-glycosyltransferase family, is indispensable not only with regard to its biological function, but also to its secretion.
15737642	5	53	from	Asn219	1230:1235	arg1	heterogeneity					1192:1204	the heterogeneity	1188:1204	the heterogeneity of the glycosylation at Asn219	1188:1235	When Ser221 was replaced with Thr, fusion protein was expressed as a single band, indicating that the double band of the expressed fusion protein was due to the heterogeneity of the glycosylation at Asn219.
15737642	5	53	from	Asn219	1230:1235	arg1	glycosylation					1213:1225	the glycosylation	1209:1225	the glycosylation at Asn219	1209:1235	When Ser221 was replaced with Thr, fusion protein was expressed as a single band, indicating that the double band of the expressed fusion protein was due to the heterogeneity of the glycosylation at Asn219.
15737642	6	54	theme	GFP	1294:1296	arg1	-beta3GnT2Delta83					1301:1317	GFP(uv)-beta3GnT2Delta83	1294:1317	GFP(uv)-beta3GnT2Delta83	1294:1317	The truncated protein consisting of amino acids 82-397 (GFP(uv)-beta3GnT2Delta83), which lacked both one N-glycosylation site at Asn79 and the stem region of glycosyltransferase, was expressed as only a small form and showed no beta3GnT activity.
15737642	6	54	theme	GFP	1294:1296	arg1	82-397					1286:1291	82-397	1286:1291	82-397	1286:1291	The truncated protein consisting of amino acids 82-397 (GFP(uv)-beta3GnT2Delta83), which lacked both one N-glycosylation site at Asn79 and the stem region of glycosyltransferase, was expressed as only a small form and showed no beta3GnT activity.
15737642	4	55	from	Asn219	890:895	arg1	N-glycosylation					871:885	The N-glycosylation at Asn219	867:895	The N-glycosylation at Asn219	867:895	The N-glycosylation at Asn219 was necessary for the beta3GnT activity; moreover, N-glycosylation at Asn127 and Asn219 was critical for efficient protein secretion.
15737642	4	55	from	Asn219	890:895	arg1	at					887:888	The N-glycosylation at Asn219	867:895	The N-glycosylation at Asn219	867:895	The N-glycosylation at Asn219 was necessary for the beta3GnT activity; moreover, N-glycosylation at Asn127 and Asn219 was critical for efficient protein secretion.
15737642	5	56	from	heterogeneity	1192:1204	arg1	Asn219					1230:1235	Asn219	1230:1235	Asn219	1230:1235	When Ser221 was replaced with Thr, fusion protein was expressed as a single band, indicating that the double band of the expressed fusion protein was due to the heterogeneity of the glycosylation at Asn219.
15737642	3	57	gly	N-glycosylation	697:711	arg2	five					682:685	five	682:685	five	682:685	Four of five potential N-glycosylation sites were found to be occupied, and their biological function and secretion were inhibited with the treatment of N-glycosylation inhibitor, tunicamycin.
15737642	3	57	gly	N-glycosylation	697:711	arg2	sites					713:717	Four of five potential N-glycosylation sites	674:717	Four of five potential N-glycosylation sites	674:717	Four of five potential N-glycosylation sites were found to be occupied, and their biological function and secretion were inhibited with the treatment of N-glycosylation inhibitor, tunicamycin.
15737642	0	58	gly	N-glycosylation	15:29	arg2	sites					31:35	N-glycosylation sites	15:35	N-glycosylation sites	15:35	The effects of N-glycosylation sites and the N-terminal region on the biological function of beta1,3-N-acetylglucosaminyltransferase 2 and its secretion.
15737642	8	59	theme	protein	1827:1833	arg1	structure					1835:1843	the active protein structure	1816:1843	the active protein structure	1816:1843	The N-terminal region, which belongs to a stem region of glycosyltransferase, might also be important to the active protein structure.
15737642	5	60	theme	fusion	1162:1167	arg1	protein					1169:1175	the expressed fusion protein	1148:1175	the expressed fusion protein	1148:1175	When Ser221 was replaced with Thr, fusion protein was expressed as a single band, indicating that the double band of the expressed fusion protein was due to the heterogeneity of the glycosylation at Asn219.
15737642	2	61	theme	region	595:600	arg1	mutagenesis					516:526	site-directed mutagenesis	502:526	site-directed mutagenesis of potential N-glycosylation sites	502:561	To obtain insight into the structure of beta3GnT2, the effects of N-glycosylation on its biological function were evaluated using the addition of inhibitors, site-directed mutagenesis of potential N-glycosylation sites, and deletion of its N-terminal region using a fusion protein with GFP(uv) in a baculovirus expression system.
15737642	2	61	theme	region	595:600	arg1	addition					478:485	the addition	474:485	the addition of inhibitors	474:499	To obtain insight into the structure of beta3GnT2, the effects of N-glycosylation on its biological function were evaluated using the addition of inhibitors, site-directed mutagenesis of potential N-glycosylation sites, and deletion of its N-terminal region using a fusion protein with GFP(uv) in a baculovirus expression system.
15737642	2	61	theme	region	595:600	arg1	deletion					568:575	deletion	568:575	deletion of its N-terminal region using a fusion protein with GFP(uv) in a baculovirus expression system	568:671	To obtain insight into the structure of beta3GnT2, the effects of N-glycosylation on its biological function were evaluated using the addition of inhibitors, site-directed mutagenesis of potential N-glycosylation sites, and deletion of its N-terminal region using a fusion protein with GFP(uv) in a baculovirus expression system.
15737642	4	62	from	Asn127	967:972	arg1	N-glycosylation					948:962	N-glycosylation	948:962	N-glycosylation at Asn127 and Asn219	948:983	The N-glycosylation at Asn219 was necessary for the beta3GnT activity; moreover, N-glycosylation at Asn127 and Asn219 was critical for efficient protein secretion.
15737642	2	63	from	effects	399:405	arg1	function					444:451	its biological function	429:451	its biological function	429:451	To obtain insight into the structure of beta3GnT2, the effects of N-glycosylation on its biological function were evaluated using the addition of inhibitors, site-directed mutagenesis of potential N-glycosylation sites, and deletion of its N-terminal region using a fusion protein with GFP(uv) in a baculovirus expression system.
15737642	6	64	dep	acids	1280:1284	arg1	-beta3GnT2Delta83					1301:1317	GFP(uv)-beta3GnT2Delta83	1294:1317	GFP(uv)-beta3GnT2Delta83	1294:1317	The truncated protein consisting of amino acids 82-397 (GFP(uv)-beta3GnT2Delta83), which lacked both one N-glycosylation site at Asn79 and the stem region of glycosyltransferase, was expressed as only a small form and showed no beta3GnT activity.
15737642	6	64	dep	acids	1280:1284	arg1	82-397					1286:1291	82-397	1286:1291	82-397	1286:1291	The truncated protein consisting of amino acids 82-397 (GFP(uv)-beta3GnT2Delta83), which lacked both one N-glycosylation site at Asn79 and the stem region of glycosyltransferase, was expressed as only a small form and showed no beta3GnT activity.
15737642	5	65	theme	glycosylation	1213:1225	arg1	heterogeneity					1192:1204	the heterogeneity	1188:1204	the heterogeneity of the glycosylation at Asn219	1188:1235	When Ser221 was replaced with Thr, fusion protein was expressed as a single band, indicating that the double band of the expressed fusion protein was due to the heterogeneity of the glycosylation at Asn219.
15737642	2	66	theme	N-terminal	584:593	arg1	region					595:600	its N-terminal region	580:600	its N-terminal region using a fusion protein with GFP(uv) in a baculovirus expression system	580:671	To obtain insight into the structure of beta3GnT2, the effects of N-glycosylation on its biological function were evaluated using the addition of inhibitors, site-directed mutagenesis of potential N-glycosylation sites, and deletion of its N-terminal region using a fusion protein with GFP(uv) in a baculovirus expression system.
15737642	5	67	theme	fusion	1066:1071	arg1	protein					1073:1079	fusion protein	1066:1079	fusion protein	1066:1079	When Ser221 was replaced with Thr, fusion protein was expressed as a single band, indicating that the double band of the expressed fusion protein was due to the heterogeneity of the glycosylation at Asn219.
15737642	5	67	theme	fusion	1066:1071	arg1	band					1107:1110	a single band	1098:1110	a single band	1098:1110	When Ser221 was replaced with Thr, fusion protein was expressed as a single band, indicating that the double band of the expressed fusion protein was due to the heterogeneity of the glycosylation at Asn219.
15737642	7	68	gly	N-glycosylation	1516:1530	arg2	indispensable					1621:1633	indispensable	1621:1633	indispensable	1621:1633	These results suggest that the N-glycosylation site at Asn219, which is conserved throughout the beta1,3-glycosyltransferase family, is indispensable not only with regard to its biological function, but also to its secretion.
15737642	7	68	gly	N-glycosylation	1516:1530	arg2	Asn219					1540:1545	Asn219	1540:1545	Asn219	1540:1545	These results suggest that the N-glycosylation site at Asn219, which is conserved throughout the beta1,3-glycosyltransferase family, is indispensable not only with regard to its biological function, but also to its secretion.
15737642	7	68	gly	N-glycosylation	1516:1530	arg2	site					1532:1535	the N-glycosylation site	1512:1535	the N-glycosylation site	1512:1535	These results suggest that the N-glycosylation site at Asn219, which is conserved throughout the beta1,3-glycosyltransferase family, is indispensable not only with regard to its biological function, but also to its secretion.
15737642	4	69	gly	N-glycosylation	948:962	arg1	protein					1012:1018	efficient protein secretion	1002:1028	efficient protein secretion	1002:1028	The N-glycosylation at Asn219 was necessary for the beta3GnT activity; moreover, N-glycosylation at Asn127 and Asn219 was critical for efficient protein secretion.
15737642	4	69	gly	N-glycosylation	948:962	arg1	Asn219					978:983	Asn219	978:983	Asn219	978:983	The N-glycosylation at Asn219 was necessary for the beta3GnT activity; moreover, N-glycosylation at Asn127 and Asn219 was critical for efficient protein secretion.
15737642	4	69	gly	N-glycosylation	948:962	arg2	Asn219					978:983	Asn219	978:983	Asn219	978:983	The N-glycosylation at Asn219 was necessary for the beta3GnT activity; moreover, N-glycosylation at Asn127 and Asn219 was critical for efficient protein secretion.
15737642	4	69	gly	N-glycosylation	948:962	arg1	Asn127					967:972	Asn127	967:972	Asn127	967:972	The N-glycosylation at Asn219 was necessary for the beta3GnT activity; moreover, N-glycosylation at Asn127 and Asn219 was critical for efficient protein secretion.
15737642	4	69	gly	N-glycosylation	948:962	arg2	Asn127					967:972	Asn127	967:972	Asn127	967:972	The N-glycosylation at Asn219 was necessary for the beta3GnT activity; moreover, N-glycosylation at Asn127 and Asn219 was critical for efficient protein secretion.
15737642	3	70	theme	tunicamycin	854:864	arg1	treatment					814:822	the treatment	810:822	the treatment of N-glycosylation inhibitor, tunicamycin	810:864	Four of five potential N-glycosylation sites were found to be occupied, and their biological function and secretion were inhibited with the treatment of N-glycosylation inhibitor, tunicamycin.
15737642	4	71	gly	N-glycosylation	871:885	arg2	necessary					901:909	necessary	901:909	necessary	901:909	The N-glycosylation at Asn219 was necessary for the beta3GnT activity; moreover, N-glycosylation at Asn127 and Asn219 was critical for efficient protein secretion.
15737642	4	71	gly	N-glycosylation	871:885	arg1	Asn219					890:895	The N-glycosylation at Asn219	867:895	The N-glycosylation at Asn219	867:895	The N-glycosylation at Asn219 was necessary for the beta3GnT activity; moreover, N-glycosylation at Asn127 and Asn219 was critical for efficient protein secretion.
15737642	4	71	gly	N-glycosylation	871:885	arg2	Asn219					890:895	The N-glycosylation at Asn219	867:895	The N-glycosylation at Asn219	867:895	The N-glycosylation at Asn219 was necessary for the beta3GnT activity; moreover, N-glycosylation at Asn127 and Asn219 was critical for efficient protein secretion.
15737642	4	71	gly	N-glycosylation	871:885	arg1	necessary					901:909	necessary	901:909	necessary	901:909	The N-glycosylation at Asn219 was necessary for the beta3GnT activity; moreover, N-glycosylation at Asn127 and Asn219 was critical for efficient protein secretion.
15737642	6	72	gly	N-glycosylation	1343:1357	arg2	Asn79					1367:1371	Asn79	1367:1371	Asn79	1367:1371	The truncated protein consisting of amino acids 82-397 (GFP(uv)-beta3GnT2Delta83), which lacked both one N-glycosylation site at Asn79 and the stem region of glycosyltransferase, was expressed as only a small form and showed no beta3GnT activity.
15737642	6	72	gly	N-glycosylation	1343:1357	arg1	glycosyltransferase					1396:1414	glycosyltransferase	1396:1414	glycosyltransferase	1396:1414	The truncated protein consisting of amino acids 82-397 (GFP(uv)-beta3GnT2Delta83), which lacked both one N-glycosylation site at Asn79 and the stem region of glycosyltransferase, was expressed as only a small form and showed no beta3GnT activity.
15737642	6	72	gly	N-glycosylation	1343:1357	arg2	site					1359:1362	one N-glycosylation site	1339:1362	one N-glycosylation site at Asn79	1339:1371	The truncated protein consisting of amino acids 82-397 (GFP(uv)-beta3GnT2Delta83), which lacked both one N-glycosylation site at Asn79 and the stem region of glycosyltransferase, was expressed as only a small form and showed no beta3GnT activity.
15737642	6	72	gly	N-glycosylation	1343:1357	arg2	one					1339:1341	one	1339:1341	one	1339:1341	The truncated protein consisting of amino acids 82-397 (GFP(uv)-beta3GnT2Delta83), which lacked both one N-glycosylation site at Asn79 and the stem region of glycosyltransferase, was expressed as only a small form and showed no beta3GnT activity.
15737642	6	72	gly	N-glycosylation	1343:1357	arg2	glycosyltransferase					1396:1414	glycosyltransferase	1396:1414	glycosyltransferase	1396:1414	The truncated protein consisting of amino acids 82-397 (GFP(uv)-beta3GnT2Delta83), which lacked both one N-glycosylation site at Asn79 and the stem region of glycosyltransferase, was expressed as only a small form and showed no beta3GnT activity.
15737642	2	73	theme	beta3GnT2	384:392	arg1	structure					371:379	the structure	367:379	the structure of beta3GnT2	367:392	To obtain insight into the structure of beta3GnT2, the effects of N-glycosylation on its biological function were evaluated using the addition of inhibitors, site-directed mutagenesis of potential N-glycosylation sites, and deletion of its N-terminal region using a fusion protein with GFP(uv) in a baculovirus expression system.
15737642	6	74	theme	small	1441:1445	arg1	protein					1252:1258	The truncated protein	1238:1258	The truncated protein	1238:1258	The truncated protein consisting of amino acids 82-397 (GFP(uv)-beta3GnT2Delta83), which lacked both one N-glycosylation site at Asn79 and the stem region of glycosyltransferase, was expressed as only a small form and showed no beta3GnT activity.
15737642	6	74	theme	small	1441:1445	arg1	form					1447:1450	only a small form	1434:1450	only a small form	1434:1450	The truncated protein consisting of amino acids 82-397 (GFP(uv)-beta3GnT2Delta83), which lacked both one N-glycosylation site at Asn79 and the stem region of glycosyltransferase, was expressed as only a small form and showed no beta3GnT activity.
15737642	6	74	theme	small	1441:1445	arg1	activity					1475:1482	no beta3GnT activity	1463:1482	no beta3GnT activity	1463:1482	The truncated protein consisting of amino acids 82-397 (GFP(uv)-beta3GnT2Delta83), which lacked both one N-glycosylation site at Asn79 and the stem region of glycosyltransferase, was expressed as only a small form and showed no beta3GnT activity.
15737642	0	75	theme	region	56:61	arg1	effects					4:10	The effects	0:10	The effects of N-glycosylation sites and the N-terminal region on the biological function of beta1,3-N-acetylglucosaminyltransferase 2 and its secretion	0:151	The effects of N-glycosylation sites and the N-terminal region on the biological function of beta1,3-N-acetylglucosaminyltransferase 2 and its secretion.
15737642	4	76	theme	efficient	1002:1010	arg1	secretion					1020:1028	efficient protein secretion	1002:1028	efficient protein secretion	1002:1028	The N-glycosylation at Asn219 was necessary for the beta3GnT activity; moreover, N-glycosylation at Asn127 and Asn219 was critical for efficient protein secretion.
15737642	4	77	theme	protein	1012:1018	arg1	secretion					1020:1028	efficient protein secretion	1002:1028	efficient protein secretion	1002:1028	The N-glycosylation at Asn219 was necessary for the beta3GnT activity; moreover, N-glycosylation at Asn127 and Asn219 was critical for efficient protein secretion.
15737642	8	78	theme	stem	1753:1756	arg1	region					1758:1763	a stem region	1751:1763	a stem region of glycosyltransferase	1751:1786	The N-terminal region, which belongs to a stem region of glycosyltransferase, might also be important to the active protein structure.
15737642	8	79	theme	N-terminal	1715:1724	arg1	region					1726:1731	The N-terminal region	1711:1731	The N-terminal region	1711:1731	The N-terminal region, which belongs to a stem region of glycosyltransferase, might also be important to the active protein structure.
15737642	8	79	theme	N-terminal	1715:1724	arg1	important					1803:1811	important	1803:1811	important	1803:1811	The N-terminal region, which belongs to a stem region of glycosyltransferase, might also be important to the active protein structure.
15737642	1	80	theme	polylactosamine	258:272	arg1	chains					283:288	the polylactosamine acceptor chains	254:288	the polylactosamine acceptor chains	254:288	Human beta1,3-N-acetylglucosaminyltransferase 2 (beta3GnT2) is thought to be an enzyme that extends the polylactosamine acceptor chains, but its function and structure analysis are unknown.
20618438	7	0	dep	deficient	1144:1152	arg1	reminiscent					1251:1261	reminiscent	1251:1261	reminiscent of the HFE-C282Y variant	1251:1286	We also observed that the triple mutant was functionally deficient in beta2-microglobulin interactions and incapable of regulating transferrin binding, once again, reminiscent of the HFE-C282Y variant.
20618438	7	0	dep	deficient	1144:1152	arg1	mutant					1120:1125	the triple mutant	1109:1125	the triple mutant	1109:1125	We also observed that the triple mutant was functionally deficient in beta2-microglobulin interactions and incapable of regulating transferrin binding, once again, reminiscent of the HFE-C282Y variant.
20618438	7	0	dep	deficient	1144:1152	arg1	deficient					1144:1152	deficient	1144:1152	deficient	1144:1152	We also observed that the triple mutant was functionally deficient in beta2-microglobulin interactions and incapable of regulating transferrin binding, once again, reminiscent of the HFE-C282Y variant.
20618438	4	1	theme	putative	523:530	arg1	sites					548:552	putative N-glycosylation sites	523:552	putative N-glycosylation sites	523:552	Here we employed bioinformatics to identify putative N-glycosylation sites at residues N110, N130 and N234 of the human HFE protein, and used site-directed mutagenesis to create combinations of single, double or triple mutants.
20618438	7	2	theme	beta2-microglobulin	1157:1175	arg1	interactions					1177:1188	beta2-microglobulin interactions	1157:1188	beta2-microglobulin interactions	1157:1188	We also observed that the triple mutant was functionally deficient in beta2-microglobulin interactions and incapable of regulating transferrin binding, once again, reminiscent of the HFE-C282Y variant.
20618438	11	3	dep	trafficking	1936:1946	arg1	the					1911:1913	the	1911:1913	the	1911:1913	We conclude that glycosylation is important for the normal intracellular trafficking and functional activity of HFE.
20618438	4	4	theme	HFE	599:601	arg1	protein					603:609	the human HFE protein	589:609	the human HFE protein	589:609	Here we employed bioinformatics to identify putative N-glycosylation sites at residues N110, N130 and N234 of the human HFE protein, and used site-directed mutagenesis to create combinations of single, double or triple mutants.
20618438	5	5	theme	transferrin	779:789	arg1	receptor					791:798	the type 1 transferrin receptor	768:798	the type 1 transferrin receptor	768:798	Compared with the wild-type protein, which co-localizes with the type 1 transferrin receptor in the endosomal recycling compartment and on distributed punctae, the triple mutant co-localized with BiP in the endoplasmic reticulum.
20618438	2	6	theme	transferrin	365:375	arg1	receptors					377:385	transferrin receptors	365:385	transferrin receptors	365:385	It influences cellular iron concentrations through multiple mechanisms, including regulation of transferrin binding to transferrin receptors.
20618438	4	7	theme	human	593:597	arg1	protein					603:609	the human HFE protein	589:609	the human HFE protein	589:609	Here we employed bioinformatics to identify putative N-glycosylation sites at residues N110, N130 and N234 of the human HFE protein, and used site-directed mutagenesis to create combinations of single, double or triple mutants.
20618438	4	8	dep	residues	557:564	arg1	N110					566:569	N110	566:569	N110	566:569	Here we employed bioinformatics to identify putative N-glycosylation sites at residues N110, N130 and N234 of the human HFE protein, and used site-directed mutagenesis to create combinations of single, double or triple mutants.
20618438	2	9	theme	multiple	297:304	arg1	mechanisms					306:315	multiple mechanisms	297:315	multiple mechanisms	297:315	It influences cellular iron concentrations through multiple mechanisms, including regulation of transferrin binding to transferrin receptors.
20618438	2	9	theme	multiple	297:304	arg1	regulation					328:337	regulation	328:337	regulation of transferrin binding to transferrin receptors	328:385	It influences cellular iron concentrations through multiple mechanisms, including regulation of transferrin binding to transferrin receptors.
20618438	10	10	theme	decreased	1776:1784	arg1	binding					1794:1800	decreased surface binding	1776:1800	decreased surface binding of transferrin	1776:1815	Furthermore, although the majority of cells expressing these single and double mutants showed decreased surface binding of transferrin, a number appeared to have lost this ability.
20618438	6	11	theme	misfolding	1011:1020	arg1	mutant					1032:1037	the misfolding HFE-C282Y mutant	1007:1037	the misfolding HFE-C282Y mutant that causes type 1 hereditary haemachromatosis	1007:1084	This was similar to the localization pattern described previously for the misfolding HFE-C282Y mutant that causes type 1 hereditary haemachromatosis.
20618438	3	12	from	importance	392:401	arg1	localization					427:438	localization	427:438	localization	427:438	The importance of glycosylation in HFE localization and function has not yet been studied.
20618438	3	12	from	importance	392:401	arg1	HFE					423:425	HFE localization and function	423:451	HFE localization and function	423:451	The importance of glycosylation in HFE localization and function has not yet been studied.
20618438	3	12	from	importance	392:401	arg1	function					444:451	function	444:451	function	444:451	The importance of glycosylation in HFE localization and function has not yet been studied.
20618438	11	13	theme	HFE	1975:1977	arg1	trafficking					1936:1946	intracellular trafficking	1922:1946	intracellular trafficking	1922:1946	We conclude that glycosylation is important for the normal intracellular trafficking and functional activity of HFE.
20618438	11	13	theme	HFE	1975:1977	arg1	activity					1963:1970	functional activity	1952:1970	functional activity	1952:1970	We conclude that glycosylation is important for the normal intracellular trafficking and functional activity of HFE.
20618438	9	14	theme	additional	1647:1656	arg1	localization					1668:1679	additional reticular localization	1647:1679	additional reticular localization	1647:1679	Therefore, although they displayed an endosomal recycling compartment/punctate localization like the wild-type protein, many cells simultaneously displayed additional reticular localization.
20618438	8	15	from	protein	1482:1488	arg1	characteristics					1391:1405	characteristics	1391:1405	characteristics primarily of the wild-type, but also some from the glycosylation-deficient protein	1391:1488	Single and double mutants that undergo limited glycosylation appeared to have a mixed phenotype, with characteristics primarily of the wild-type, but also some from the glycosylation-deficient protein.
20618438	4	16	theme	protein	603:609	arg1	protein					603:609	the human HFE protein	589:609	the human HFE protein	589:609	Here we employed bioinformatics to identify putative N-glycosylation sites at residues N110, N130 and N234 of the human HFE protein, and used site-directed mutagenesis to create combinations of single, double or triple mutants.
20618438	4	16	theme	protein	603:609	arg1	residues					557:564	residues	557:564	residues	557:564	Here we employed bioinformatics to identify putative N-glycosylation sites at residues N110, N130 and N234 of the human HFE protein, and used site-directed mutagenesis to create combinations of single, double or triple mutants.
20618438	0	17	theme	cell	107:110	arg1	binding					132:138	cell surface transferrin binding	107:138	cell surface transferrin binding	107:138	N-glycosylation is important for the correct intracellular localization of HFE and its ability to decrease cell surface transferrin binding.
20618438	3	18	dep	HFE	423:425	arg1	localization					427:438	localization	427:438	localization	427:438	The importance of glycosylation in HFE localization and function has not yet been studied.
20618438	3	18	dep	HFE	423:425	arg1	HFE					423:425	HFE localization and function	423:451	HFE localization and function	423:451	The importance of glycosylation in HFE localization and function has not yet been studied.
20618438	3	18	dep	HFE	423:425	arg1	function					444:451	function	444:451	function	444:451	The importance of glycosylation in HFE localization and function has not yet been studied.
20618438	5	19	theme	recycling	817:825	arg1	compartment					827:837	the endosomal recycling compartment	803:837	the endosomal recycling compartment	803:837	Compared with the wild-type protein, which co-localizes with the type 1 transferrin receptor in the endosomal recycling compartment and on distributed punctae, the triple mutant co-localized with BiP in the endoplasmic reticulum.
20618438	9	20	theme	reticular	1658:1666	arg1	localization					1668:1679	additional reticular localization	1647:1679	additional reticular localization	1647:1679	Therefore, although they displayed an endosomal recycling compartment/punctate localization like the wild-type protein, many cells simultaneously displayed additional reticular localization.
20618438	4	21	gly	N-glycosylation	532:546	arg2	sites					548:552	putative N-glycosylation sites	523:552	putative N-glycosylation sites	523:552	Here we employed bioinformatics to identify putative N-glycosylation sites at residues N110, N130 and N234 of the human HFE protein, and used site-directed mutagenesis to create combinations of single, double or triple mutants.
20618438	5	22	theme	triple	871:876	arg1	mutant					878:883	the triple mutant	867:883	the triple mutant	867:883	Compared with the wild-type protein, which co-localizes with the type 1 transferrin receptor in the endosomal recycling compartment and on distributed punctae, the triple mutant co-localized with BiP in the endoplasmic reticulum.
20618438	5	23	theme	endosomal	807:815	arg1	compartment					827:837	the endosomal recycling compartment	803:837	the endosomal recycling compartment	803:837	Compared with the wild-type protein, which co-localizes with the type 1 transferrin receptor in the endosomal recycling compartment and on distributed punctae, the triple mutant co-localized with BiP in the endoplasmic reticulum.
20618438	5	24	theme	endoplasmic	914:924	arg1	reticulum					926:934	the endoplasmic reticulum	910:934	the endoplasmic reticulum	910:934	Compared with the wild-type protein, which co-localizes with the type 1 transferrin receptor in the endosomal recycling compartment and on distributed punctae, the triple mutant co-localized with BiP in the endoplasmic reticulum.
20618438	2	25	theme	iron	269:272	arg1	concentrations					274:287	cellular iron concentrations	260:287	cellular iron concentrations	260:287	It influences cellular iron concentrations through multiple mechanisms, including regulation of transferrin binding to transferrin receptors.
20618438	10	26	theme	double	1754:1759	arg1	mutants					1761:1767	these single and double mutants	1737:1767	these single and double mutants	1737:1767	Furthermore, although the majority of cells expressing these single and double mutants showed decreased surface binding of transferrin, a number appeared to have lost this ability.
20618438	1	27	theme	transmembrane	157:169	arg1	protein					171:177	a type 1 transmembrane protein	148:177	a type 1 transmembrane protein that becomes N-glycosylated during transport to the cell membrane	148:243	HFE is a type 1 transmembrane protein that becomes N-glycosylated during transport to the cell membrane.
20618438	1	27	theme	transmembrane	157:169	arg1	HFE					141:143	HFE	141:143	HFE	141:143	HFE is a type 1 transmembrane protein that becomes N-glycosylated during transport to the cell membrane.
20618438	3	28	theme	glycosylation	406:418	arg1	importance					392:401	The importance	388:401	The importance of glycosylation in HFE localization and function	388:451	The importance of glycosylation in HFE localization and function has not yet been studied.
20618438	7	29	theme	triple	1113:1118	arg1	reminiscent					1251:1261	reminiscent	1251:1261	reminiscent of the HFE-C282Y variant	1251:1286	We also observed that the triple mutant was functionally deficient in beta2-microglobulin interactions and incapable of regulating transferrin binding, once again, reminiscent of the HFE-C282Y variant.
20618438	7	29	theme	triple	1113:1118	arg1	mutant					1120:1125	the triple mutant	1109:1125	the triple mutant	1109:1125	We also observed that the triple mutant was functionally deficient in beta2-microglobulin interactions and incapable of regulating transferrin binding, once again, reminiscent of the HFE-C282Y variant.
20618438	7	29	theme	triple	1113:1118	arg1	deficient					1144:1152	deficient	1144:1152	deficient	1144:1152	We also observed that the triple mutant was functionally deficient in beta2-microglobulin interactions and incapable of regulating transferrin binding, once again, reminiscent of the HFE-C282Y variant.
20618438	7	30	theme	variant	1280:1286	arg1	reminiscent					1251:1261	reminiscent	1251:1261	reminiscent of the HFE-C282Y variant	1251:1286	We also observed that the triple mutant was functionally deficient in beta2-microglobulin interactions and incapable of regulating transferrin binding, once again, reminiscent of the HFE-C282Y variant.
20618438	7	30	theme	variant	1280:1286	arg1	mutant					1120:1125	the triple mutant	1109:1125	the triple mutant	1109:1125	We also observed that the triple mutant was functionally deficient in beta2-microglobulin interactions and incapable of regulating transferrin binding, once again, reminiscent of the HFE-C282Y variant.
20618438	7	30	theme	variant	1280:1286	arg1	deficient					1144:1152	deficient	1144:1152	deficient	1144:1152	We also observed that the triple mutant was functionally deficient in beta2-microglobulin interactions and incapable of regulating transferrin binding, once again, reminiscent of the HFE-C282Y variant.
20618438	11	31	gly	glycosylation	1880:1892	arg1	HFE					1975:1977	HFE	1975:1977	HFE	1975:1977	We conclude that glycosylation is important for the normal intracellular trafficking and functional activity of HFE.
20618438	11	32	theme	normal	1915:1920	arg1	trafficking					1936:1946	intracellular trafficking	1922:1946	intracellular trafficking	1922:1946	We conclude that glycosylation is important for the normal intracellular trafficking and functional activity of HFE.
20618438	8	33	theme	wild-type	1424:1432	arg1	characteristics					1391:1405	characteristics	1391:1405	characteristics primarily of the wild-type, but also some from the glycosylation-deficient protein	1391:1488	Single and double mutants that undergo limited glycosylation appeared to have a mixed phenotype, with characteristics primarily of the wild-type, but also some from the glycosylation-deficient protein.
20618438	4	34	theme	double	681:686	arg1	mutants					698:704	single, double or triple mutants	673:704	single, double or triple mutants	673:704	Here we employed bioinformatics to identify putative N-glycosylation sites at residues N110, N130 and N234 of the human HFE protein, and used site-directed mutagenesis to create combinations of single, double or triple mutants.
20618438	7	35	theme	transferrin	1218:1228	arg1	binding					1230:1236	transferrin binding	1218:1236	transferrin binding	1218:1236	We also observed that the triple mutant was functionally deficient in beta2-microglobulin interactions and incapable of regulating transferrin binding, once again, reminiscent of the HFE-C282Y variant.
20618438	10	36	theme	transferrin	1805:1815	arg1	binding					1794:1800	decreased surface binding	1776:1800	decreased surface binding of transferrin	1776:1815	Furthermore, although the majority of cells expressing these single and double mutants showed decreased surface binding of transferrin, a number appeared to have lost this ability.
20618438	0	37	theme	transferrin	120:130	arg1	binding					132:138	cell surface transferrin binding	107:138	cell surface transferrin binding	107:138	N-glycosylation is important for the correct intracellular localization of HFE and its ability to decrease cell surface transferrin binding.
20618438	11	38	theme	functional	1952:1961	arg1	activity					1963:1970	functional activity	1952:1970	functional activity	1952:1970	We conclude that glycosylation is important for the normal intracellular trafficking and functional activity of HFE.
20618438	5	39	theme	distributed	846:856	arg1	punctae					858:864	distributed punctae	846:864	distributed punctae	846:864	Compared with the wild-type protein, which co-localizes with the type 1 transferrin receptor in the endosomal recycling compartment and on distributed punctae, the triple mutant co-localized with BiP in the endoplasmic reticulum.
20618438	0	40	theme	surface	112:118	arg1	binding					132:138	cell surface transferrin binding	107:138	cell surface transferrin binding	107:138	N-glycosylation is important for the correct intracellular localization of HFE and its ability to decrease cell surface transferrin binding.
20618438	1	41	theme	type	150:153	arg1	protein					171:177	a type 1 transmembrane protein	148:177	a type 1 transmembrane protein that becomes N-glycosylated during transport to the cell membrane	148:243	HFE is a type 1 transmembrane protein that becomes N-glycosylated during transport to the cell membrane.
20618438	1	41	theme	type	150:153	arg1	HFE					141:143	HFE	141:143	HFE	141:143	HFE is a type 1 transmembrane protein that becomes N-glycosylated during transport to the cell membrane.
20618438	9	42	theme	recycling	1539:1547	arg1	localization					1570:1581	an endosomal recycling compartment/punctate localization	1526:1581	an endosomal recycling compartment/punctate localization	1526:1581	Therefore, although they displayed an endosomal recycling compartment/punctate localization like the wild-type protein, many cells simultaneously displayed additional reticular localization.
20618438	0	43	theme	correct	37:43	arg1	localization					59:70	the correct intracellular localization	33:70	the correct intracellular localization of HFE	33:77	N-glycosylation is important for the correct intracellular localization of HFE and its ability to decrease cell surface transferrin binding.
20618438	5	44	theme	wild-type	725:733	arg1	protein					735:741	the wild-type protein	721:741	the wild-type protein	721:741	Compared with the wild-type protein, which co-localizes with the type 1 transferrin receptor in the endosomal recycling compartment and on distributed punctae, the triple mutant co-localized with BiP in the endoplasmic reticulum.
20618438	0	45	gly	N-glycosylation	0:14	arg1	HFE					75:77	HFE	75:77	HFE	75:77	N-glycosylation is important for the correct intracellular localization of HFE and its ability to decrease cell surface transferrin binding.
20618438	8	46	theme	double	1300:1305	arg1	mutants					1307:1313	Single and double mutants	1289:1313	Single and double mutants that undergo limited glycosylation	1289:1348	Single and double mutants that undergo limited glycosylation appeared to have a mixed phenotype, with characteristics primarily of the wild-type, but also some from the glycosylation-deficient protein.
20618438	9	47	theme	compartment/punctate	1549:1568	arg1	localization					1570:1581	an endosomal recycling compartment/punctate localization	1526:1581	an endosomal recycling compartment/punctate localization	1526:1581	Therefore, although they displayed an endosomal recycling compartment/punctate localization like the wild-type protein, many cells simultaneously displayed additional reticular localization.
20618438	8	48	theme	Single	1289:1294	arg1	mutants					1307:1313	Single and double mutants	1289:1313	Single and double mutants that undergo limited glycosylation	1289:1348	Single and double mutants that undergo limited glycosylation appeared to have a mixed phenotype, with characteristics primarily of the wild-type, but also some from the glycosylation-deficient protein.
20618438	6	49	theme	localization	961:972	arg1	pattern					974:980	the localization pattern	957:980	the localization pattern described previously for the misfolding HFE-C282Y mutant that causes type 1 hereditary haemachromatosis	957:1084	This was similar to the localization pattern described previously for the misfolding HFE-C282Y mutant that causes type 1 hereditary haemachromatosis.
20618438	4	50	used	used	616:619	arg2	we					484:485	we	484:485	we	484:485	Here we employed bioinformatics to identify putative N-glycosylation sites at residues N110, N130 and N234 of the human HFE protein, and used site-directed mutagenesis to create combinations of single, double or triple mutants.
20618438	6	51	theme	HFE-C282Y	1022:1030	arg1	mutant					1032:1037	the misfolding HFE-C282Y mutant	1007:1037	the misfolding HFE-C282Y mutant that causes type 1 hereditary haemachromatosis	1007:1084	This was similar to the localization pattern described previously for the misfolding HFE-C282Y mutant that causes type 1 hereditary haemachromatosis.
20618438	8	52	theme	some	1444:1447	arg1	characteristics					1391:1405	characteristics	1391:1405	characteristics primarily of the wild-type, but also some from the glycosylation-deficient protein	1391:1488	Single and double mutants that undergo limited glycosylation appeared to have a mixed phenotype, with characteristics primarily of the wild-type, but also some from the glycosylation-deficient protein.
20618438	6	53	theme	hereditary	1058:1067	arg1	haemachromatosis					1069:1084	type 1 hereditary haemachromatosis	1051:1084	type 1 hereditary haemachromatosis	1051:1084	This was similar to the localization pattern described previously for the misfolding HFE-C282Y mutant that causes type 1 hereditary haemachromatosis.
20618438	7	54	from	deficient	1144:1152	arg1	interactions					1177:1188	beta2-microglobulin interactions	1157:1188	beta2-microglobulin interactions	1157:1188	We also observed that the triple mutant was functionally deficient in beta2-microglobulin interactions and incapable of regulating transferrin binding, once again, reminiscent of the HFE-C282Y variant.
20618438	8	55	contain	have	1362:1365	arg2	phenotype					1375:1383	a mixed phenotype	1367:1383	a mixed phenotype	1367:1383	Single and double mutants that undergo limited glycosylation appeared to have a mixed phenotype, with characteristics primarily of the wild-type, but also some from the glycosylation-deficient protein.
20618438	8	55	contain	have	1362:1365	arg1	mutants					1307:1313	Single and double mutants	1289:1313	Single and double mutants that undergo limited glycosylation	1289:1348	Single and double mutants that undergo limited glycosylation appeared to have a mixed phenotype, with characteristics primarily of the wild-type, but also some from the glycosylation-deficient protein.
20618438	11	56	theme	intracellular	1922:1934	arg1	trafficking					1936:1946	intracellular trafficking	1922:1946	intracellular trafficking	1922:1946	We conclude that glycosylation is important for the normal intracellular trafficking and functional activity of HFE.
20618438	8	57	theme	glycosylation-deficient	1458:1480	arg1	protein					1482:1488	the glycosylation-deficient protein	1454:1488	the glycosylation-deficient protein	1454:1488	Single and double mutants that undergo limited glycosylation appeared to have a mixed phenotype, with characteristics primarily of the wild-type, but also some from the glycosylation-deficient protein.
20618438	0	58	theme	intracellular	45:57	arg1	localization					59:70	the correct intracellular localization	33:70	the correct intracellular localization of HFE	33:77	N-glycosylation is important for the correct intracellular localization of HFE and its ability to decrease cell surface transferrin binding.
20618438	9	59	theme	wild-type	1592:1600	arg1	protein					1602:1608	the wild-type protein	1588:1608	the wild-type protein	1588:1608	Therefore, although they displayed an endosomal recycling compartment/punctate localization like the wild-type protein, many cells simultaneously displayed additional reticular localization.
20618438	8	60	from	characteristics	1391:1405	arg1	protein					1482:1488	the glycosylation-deficient protein	1454:1488	the glycosylation-deficient protein	1454:1488	Single and double mutants that undergo limited glycosylation appeared to have a mixed phenotype, with characteristics primarily of the wild-type, but also some from the glycosylation-deficient protein.
20618438	2	61	theme	binding	354:360	arg1	regulation					328:337	regulation	328:337	regulation of transferrin binding to transferrin receptors	328:385	It influences cellular iron concentrations through multiple mechanisms, including regulation of transferrin binding to transferrin receptors.
20618438	7	62	from	interactions	1177:1188	arg1	reminiscent					1251:1261	reminiscent	1251:1261	reminiscent of the HFE-C282Y variant	1251:1286	We also observed that the triple mutant was functionally deficient in beta2-microglobulin interactions and incapable of regulating transferrin binding, once again, reminiscent of the HFE-C282Y variant.
20618438	7	62	from	interactions	1177:1188	arg1	mutant					1120:1125	the triple mutant	1109:1125	the triple mutant	1109:1125	We also observed that the triple mutant was functionally deficient in beta2-microglobulin interactions and incapable of regulating transferrin binding, once again, reminiscent of the HFE-C282Y variant.
20618438	7	62	from	interactions	1177:1188	arg1	deficient					1144:1152	deficient	1144:1152	deficient	1144:1152	We also observed that the triple mutant was functionally deficient in beta2-microglobulin interactions and incapable of regulating transferrin binding, once again, reminiscent of the HFE-C282Y variant.
20618438	2	63	theme	cellular	260:267	arg1	concentrations					274:287	cellular iron concentrations	260:287	cellular iron concentrations	260:287	It influences cellular iron concentrations through multiple mechanisms, including regulation of transferrin binding to transferrin receptors.
20618438	9	64	theme	many	1611:1614	arg1	cells					1616:1620	many cells	1611:1620	many cells	1611:1620	Therefore, although they displayed an endosomal recycling compartment/punctate localization like the wild-type protein, many cells simultaneously displayed additional reticular localization.
20618438	2	65	theme	transferrin	342:352	arg1	binding					354:360	transferrin binding	342:360	transferrin binding to transferrin receptors	342:385	It influences cellular iron concentrations through multiple mechanisms, including regulation of transferrin binding to transferrin receptors.
20618438	8	66	theme	limited	1328:1334	arg1	glycosylation					1336:1348	limited glycosylation	1328:1348	limited glycosylation	1328:1348	Single and double mutants that undergo limited glycosylation appeared to have a mixed phenotype, with characteristics primarily of the wild-type, but also some from the glycosylation-deficient protein.
20618438	10	67	theme	surface	1786:1792	arg1	binding					1794:1800	decreased surface binding	1776:1800	decreased surface binding of transferrin	1776:1815	Furthermore, although the majority of cells expressing these single and double mutants showed decreased surface binding of transferrin, a number appeared to have lost this ability.
20618438	8	68	theme	mixed	1369:1373	arg1	phenotype					1375:1383	a mixed phenotype	1367:1383	a mixed phenotype	1367:1383	Single and double mutants that undergo limited glycosylation appeared to have a mixed phenotype, with characteristics primarily of the wild-type, but also some from the glycosylation-deficient protein.
20618438	6	69	theme	type	1051:1054	arg1	haemachromatosis					1069:1084	type 1 hereditary haemachromatosis	1051:1084	type 1 hereditary haemachromatosis	1051:1084	This was similar to the localization pattern described previously for the misfolding HFE-C282Y mutant that causes type 1 hereditary haemachromatosis.
20618438	0	70	theme	HFE	75:77	arg1	ability					87:93	its ability to decrease cell surface transferrin binding	83:138	its ability to decrease cell surface transferrin binding	83:138	N-glycosylation is important for the correct intracellular localization of HFE and its ability to decrease cell surface transferrin binding.
20618438	0	70	theme	HFE	75:77	arg1	localization					59:70	the correct intracellular localization	33:70	the correct intracellular localization of HFE	33:77	N-glycosylation is important for the correct intracellular localization of HFE and its ability to decrease cell surface transferrin binding.
20618438	8	71	gly	glycosylation	1336:1348	arg1	mutants					1307:1313	Single and double mutants	1289:1313	Single and double mutants that undergo limited glycosylation	1289:1348	Single and double mutants that undergo limited glycosylation appeared to have a mixed phenotype, with characteristics primarily of the wild-type, but also some from the glycosylation-deficient protein.
20618438	9	72	theme	endosomal	1529:1537	arg1	localization					1570:1581	an endosomal recycling compartment/punctate localization	1526:1581	an endosomal recycling compartment/punctate localization	1526:1581	Therefore, although they displayed an endosomal recycling compartment/punctate localization like the wild-type protein, many cells simultaneously displayed additional reticular localization.
20618438	4	73	theme	mutants	698:704	arg1	combinations					657:668	combinations	657:668	combinations of single, double or triple mutants	657:704	Here we employed bioinformatics to identify putative N-glycosylation sites at residues N110, N130 and N234 of the human HFE protein, and used site-directed mutagenesis to create combinations of single, double or triple mutants.
20618438	4	74	theme	single	673:678	arg1	mutants					698:704	single, double or triple mutants	673:704	single, double or triple mutants	673:704	Here we employed bioinformatics to identify putative N-glycosylation sites at residues N110, N130 and N234 of the human HFE protein, and used site-directed mutagenesis to create combinations of single, double or triple mutants.
20618438	1	75	theme	cell	231:234	arg1	membrane					236:243	the cell membrane	227:243	the cell membrane	227:243	HFE is a type 1 transmembrane protein that becomes N-glycosylated during transport to the cell membrane.
20618438	5	76	theme	type	772:775	arg1	receptor					791:798	the type 1 transferrin receptor	768:798	the type 1 transferrin receptor	768:798	Compared with the wild-type protein, which co-localizes with the type 1 transferrin receptor in the endosomal recycling compartment and on distributed punctae, the triple mutant co-localized with BiP in the endoplasmic reticulum.
20618438	4	77	theme	N-glycosylation	532:546	arg1	sites					548:552	putative N-glycosylation sites	523:552	putative N-glycosylation sites	523:552	Here we employed bioinformatics to identify putative N-glycosylation sites at residues N110, N130 and N234 of the human HFE protein, and used site-directed mutagenesis to create combinations of single, double or triple mutants.
20618438	10	78	theme	cells	1720:1724	arg1	majority					1708:1715	the majority	1704:1715	the majority of cells expressing these single and double mutants	1704:1767	Furthermore, although the majority of cells expressing these single and double mutants showed decreased surface binding of transferrin, a number appeared to have lost this ability.
20618438	4	79	theme	triple	691:696	arg1	mutants					698:704	single, double or triple mutants	673:704	single, double or triple mutants	673:704	Here we employed bioinformatics to identify putative N-glycosylation sites at residues N110, N130 and N234 of the human HFE protein, and used site-directed mutagenesis to create combinations of single, double or triple mutants.
20618438	10	80	theme	single	1743:1748	arg1	mutants					1761:1767	these single and double mutants	1737:1767	these single and double mutants	1737:1767	Furthermore, although the majority of cells expressing these single and double mutants showed decreased surface binding of transferrin, a number appeared to have lost this ability.
20618438	4	81	theme	site-directed	621:633	arg1	mutagenesis					635:645	site-directed mutagenesis	621:645	site-directed mutagenesis	621:645	Here we employed bioinformatics to identify putative N-glycosylation sites at residues N110, N130 and N234 of the human HFE protein, and used site-directed mutagenesis to create combinations of single, double or triple mutants.
15702487	2	0	theme	glycans	350:356	arg1	study					341:345	the study	337:345	the study of glycans and their impact on protein folding	337:392	As protein tridimensional structures are related to function, the study of glycans and their impact on protein folding can provide important information to the field of proteomics.
15702487	6	1	theme	functionalities	1212:1226	arg1	advantage					1176:1184	advantage	1176:1184	advantage of the StrOligo algorithm functionalities	1176:1226	This article describes parallel experiments involving both approaches, designed to take advantage of the StrOligo algorithm functionalities with the aim of characterizing glycosylation microheterogeneity on a specific site.
15702487	2	2	theme	tridimensional	286:299	arg1	structures					301:310	protein tridimensional structures	278:310	protein tridimensional structures	278:310	As protein tridimensional structures are related to function, the study of glycans and their impact on protein folding can provide important information to the field of proteomics.
15702487	2	3	from	study	341:345	arg1	folding					386:392	protein folding	378:392	protein folding	378:392	As protein tridimensional structures are related to function, the study of glycans and their impact on protein folding can provide important information to the field of proteomics.
15702487	2	4	from	glycans	350:356	arg1	folding					386:392	protein folding	378:392	protein folding	378:392	As protein tridimensional structures are related to function, the study of glycans and their impact on protein folding can provide important information to the field of proteomics.
15702487	5	5	theme	such	869:872	arg1	details					874:880	such details	869:880	such details	869:880	In order to obtain such details by mass spectrometry (MS), either whole glycoproteins must be digested and analyzed as mixtures of peptides and glycopeptides, or glycans must be isolated from glycopeptide fractions and analyzed as pools.
15702487	9	6	theme	tandem	1715:1720	arg1	spectrometry					1727:1738	tandem mass spectrometry	1715:1738	tandem mass spectrometry (MS/MS)	1715:1746	The sample was divided in two aliquots, and glycans from the first aliquot were released enzymatically, labelled with 2-aminobenzamide, and identified using tandem mass spectrometry (MS/MS) and the StrOligo program.
15702487	9	6	theme	tandem	1715:1720	arg1	MS/MS					1741:1745	MS/MS	1741:1745	MS/MS	1741:1745	The sample was divided in two aliquots, and glycans from the first aliquot were released enzymatically, labelled with 2-aminobenzamide, and identified using tandem mass spectrometry (MS/MS) and the StrOligo program.
15702487	6	7	theme	algorithm	1202:1210	arg1	functionalities					1212:1226	the StrOligo algorithm functionalities	1189:1226	the StrOligo algorithm functionalities	1189:1226	This article describes parallel experiments involving both approaches, designed to take advantage of the StrOligo algorithm functionalities with the aim of characterizing glycosylation microheterogeneity on a specific site.
15702487	12	8	theme	peptide	2113:2119	arg1	sequence					2121:2128	peptide sequence	2113:2128	peptide sequence	2113:2128	These spectra allowed, by comparison, detection of a glycopeptide (several glycoforms) and elucidation of peptide sequence.
15702487	10	9	theme	other	1778:1782	arg1	aliquot					1784:1790	The other aliquot	1774:1790	The other aliquot	1774:1790	The other aliquot was digested with trypsin and the resulting peptides separated by reversed-phase high-performance liquid chromatography (HPLC).
15702487	8	10	theme	alpha	1479:1483	arg1	beta					1487:1490	alpha 5 beta 1	1479:1492	alpha 5 beta 1 subunits of human integrin	1479:1519	Glycosylation of alpha 5 beta 1 subunits of human integrin was studied to test the methodology.
15702487	7	11	theme	desorption/ionization	1415:1435	arg1	source					1445:1450	a matrix-assisted laser desorption/ionization (MALDI) source	1391:1450	a matrix-assisted laser desorption/ionization (MALDI) source	1391:1450	A hybrid quadrupole-quadrupole-time-of-flight (QqTOF) instrument equipped with a matrix-assisted laser desorption/ionization (MALDI) source was used.
15702487	4	12	gly	glycosylation	706:718	arg2	sites					720:724	glycosylation sites	706:724	glycosylation sites	706:724	Glycomics studies most often aim at identifying glycosylation sites, and thus are performed on deglycosylated proteins resulting in loss of site-specific details concerning the glycosylation.
15702487	13	13	theme	glycans	2147:2153	arg1	Compositions					2131:2142	Compositions	2131:2142	Compositions of glycans present	2131:2161	Compositions of glycans present were proposed, and identification of possible glycan structures was conducted using MS/MS and StrOligo.
15702487	8	14	theme	beta	1487:1490	arg1	subunits					1494:1501	alpha 5 beta 1 subunits	1479:1501	alpha 5 beta 1 subunits of human integrin	1479:1519	Glycosylation of alpha 5 beta 1 subunits of human integrin was studied to test the methodology.
15702487	7	15	theme	matrix-assisted	1393:1407	arg1	MALDI					1438:1442	MALDI	1438:1442	MALDI	1438:1442	A hybrid quadrupole-quadrupole-time-of-flight (QqTOF) instrument equipped with a matrix-assisted laser desorption/ionization (MALDI) source was used.
15702487	7	15	theme	matrix-assisted	1393:1407	arg1	desorption/ionization					1415:1435	matrix-assisted laser desorption/ionization	1393:1435	a matrix-assisted laser desorption/ionization (MALDI) source	1391:1450	A hybrid quadrupole-quadrupole-time-of-flight (QqTOF) instrument equipped with a matrix-assisted laser desorption/ionization (MALDI) source was used.
15702487	8	16	theme	subunits	1494:1501	arg1	Glycosylation					1462:1474	Glycosylation	1462:1474	Glycosylation of alpha 5 beta 1 subunits of human integrin	1462:1519	Glycosylation of alpha 5 beta 1 subunits of human integrin was studied to test the methodology.
15702487	6	17	theme	StrOligo	1193:1200	arg1	functionalities					1212:1226	the StrOligo algorithm functionalities	1189:1226	the StrOligo algorithm functionalities	1189:1226	This article describes parallel experiments involving both approaches, designed to take advantage of the StrOligo algorithm functionalities with the aim of characterizing glycosylation microheterogeneity on a specific site.
15702487	4	18	theme	glycosylation	706:718	arg1	sites					720:724	glycosylation sites	706:724	glycosylation sites	706:724	Glycomics studies most often aim at identifying glycosylation sites, and thus are performed on deglycosylated proteins resulting in loss of site-specific details concerning the glycosylation.
15702487	9	19	theme	StrOligo	1756:1763	arg1	program					1765:1771	the StrOligo program	1752:1771	the StrOligo program	1752:1771	The sample was divided in two aliquots, and glycans from the first aliquot were released enzymatically, labelled with 2-aminobenzamide, and identified using tandem mass spectrometry (MS/MS) and the StrOligo program.
15702487	8	20	theme	human	1506:1510	arg1	integrin					1512:1519	human integrin	1506:1519	human integrin	1506:1519	Glycosylation of alpha 5 beta 1 subunits of human integrin was studied to test the methodology.
15702487	12	21	theme	glycopeptide	2060:2071	arg1	detection					2045:2053	detection	2045:2053	detection of a glycopeptide (several glycoforms)	2045:2092	These spectra allowed, by comparison, detection of a glycopeptide (several glycoforms) and elucidation of peptide sequence.
15702487	12	21	theme	glycopeptide	2060:2071	arg1	elucidation					2098:2108	elucidation	2098:2108	elucidation of peptide sequence	2098:2128	These spectra allowed, by comparison, detection of a glycopeptide (several glycoforms) and elucidation of peptide sequence.
15702487	8	22	gly	Glycosylation	1462:1474	arg1	subunits					1494:1501	alpha 5 beta 1 subunits	1479:1501	alpha 5 beta 1 subunits of human integrin	1479:1519	Glycosylation of alpha 5 beta 1 subunits of human integrin was studied to test the methodology.
15702487	10	23	theme	resulting	1826:1834	arg1	peptides					1836:1843	the resulting peptides	1822:1843	the resulting peptides separated by reversed-phase high-performance liquid chromatography (HPLC)	1822:1917	The other aliquot was digested with trypsin and the resulting peptides separated by reversed-phase high-performance liquid chromatography (HPLC).
15702487	12	24	theme	several	2074:2080	arg1	glycopeptide					2060:2071	a glycopeptide	2058:2071	a glycopeptide (several glycoforms)	2058:2092	These spectra allowed, by comparison, detection of a glycopeptide (several glycoforms) and elucidation of peptide sequence.
15702487	12	24	theme	several	2074:2080	arg1	glycoforms					2082:2091	several glycoforms	2074:2091	several glycoforms	2074:2091	These spectra allowed, by comparison, detection of a glycopeptide (several glycoforms) and elucidation of peptide sequence.
15702487	4	25	gly	deglycosylated	753:766	arg1	proteins					768:775	deglycosylated proteins	753:775	deglycosylated proteins resulting in loss of site-specific details concerning the glycosylation	753:847	Glycomics studies most often aim at identifying glycosylation sites, and thus are performed on deglycosylated proteins resulting in loss of site-specific details concerning the glycosylation.
15702487	3	26	from	glycans	544:550	arg1	proteins					555:562	proteins	555:562	proteins	555:562	The subdiscipline of glycomics (or glycoproteomics) is rapidly growing in importance as glycans in proteins have shown to be involved in protein-protein or protein-(drug, virus, antibody) interactions.
15702487	4	27	theme	deglycosylated	753:766	arg1	proteins					768:775	deglycosylated proteins	753:775	deglycosylated proteins resulting in loss of site-specific details concerning the glycosylation	753:847	Glycomics studies most often aim at identifying glycosylation sites, and thus are performed on deglycosylated proteins resulting in loss of site-specific details concerning the glycosylation.
15702487	11	28	theme	collected	1931:1939	arg1	fraction					1941:1948	A specific collected fraction	1920:1948	A specific collected fraction	1920:1948	A specific collected fraction was then analyzed by MS before and after glycan release.
15702487	0	29	theme	mass	95:98	arg1	spectrometry					100:111	tandem mass spectrometry	88:111	tandem mass spectrometry	88:111	Global and site-specific detection of human integrin alpha 5 beta 1 glycosylation using tandem mass spectrometry and the StrOligo algorithm.
15702487	9	30	from	aliquot	1625:1631	arg1	glycans					1602:1608	glycans	1602:1608	glycans from the first aliquot	1602:1631	The sample was divided in two aliquots, and glycans from the first aliquot were released enzymatically, labelled with 2-aminobenzamide, and identified using tandem mass spectrometry (MS/MS) and the StrOligo program.
15702487	5	31	gly	glycopeptides	994:1006	arg2	glycopeptides					994:1006	glycopeptides	994:1006	glycopeptides	994:1006	In order to obtain such details by mass spectrometry (MS), either whole glycoproteins must be digested and analyzed as mixtures of peptides and glycopeptides, or glycans must be isolated from glycopeptide fractions and analyzed as pools.
15702487	2	32	theme	protein	378:384	arg1	folding					386:392	protein folding	378:392	protein folding	378:392	As protein tridimensional structures are related to function, the study of glycans and their impact on protein folding can provide important information to the field of proteomics.
15702487	0	33	theme	Global	0:5	arg1	detection					25:33	Global and site-specific detection	0:33	Global and site-specific detection of human integrin alpha 5 beta 1 glycosylation	0:80	Global and site-specific detection of human integrin alpha 5 beta 1 glycosylation using tandem mass spectrometry and the StrOligo algorithm.
15702487	5	34	theme	whole	916:920	arg1	glycoproteins					922:934	either whole glycoproteins	909:934	either whole glycoproteins	909:934	In order to obtain such details by mass spectrometry (MS), either whole glycoproteins must be digested and analyzed as mixtures of peptides and glycopeptides, or glycans must be isolated from glycopeptide fractions and analyzed as pools.
15702487	5	34	theme	whole	916:920	arg1	mixtures					969:976	mixtures	969:976	mixtures of peptides and glycopeptides	969:1006	In order to obtain such details by mass spectrometry (MS), either whole glycoproteins must be digested and analyzed as mixtures of peptides and glycopeptides, or glycans must be isolated from glycopeptide fractions and analyzed as pools.
15702487	3	35	theme	protein-protein	593:607	arg1	interactions					644:655	protein-protein or protein-(drug, virus, antibody) interactions	593:655	interactions	644:655	The subdiscipline of glycomics (or glycoproteomics) is rapidly growing in importance as glycans in proteins have shown to be involved in protein-protein or protein-(drug, virus, antibody) interactions.
15702487	0	36	theme	site-specific	11:23	arg1	detection					25:33	Global and site-specific detection	0:33	Global and site-specific detection of human integrin alpha 5 beta 1 glycosylation	0:80	Global and site-specific detection of human integrin alpha 5 beta 1 glycosylation using tandem mass spectrometry and the StrOligo algorithm.
15702487	7	37	theme	hybrid	1314:1319	arg1	instrument					1366:1375	A hybrid quadrupole-quadrupole-time-of-flight (QqTOF) instrument	1312:1375	A hybrid quadrupole-quadrupole-time-of-flight (QqTOF) instrument equipped with a matrix-assisted laser desorption/ionization (MALDI) source	1312:1450	A hybrid quadrupole-quadrupole-time-of-flight (QqTOF) instrument equipped with a matrix-assisted laser desorption/ionization (MALDI) source was used.
15702487	10	38	theme	liquid	1890:1895	arg1	HPLC					1913:1916	HPLC	1913:1916	HPLC	1913:1916	The other aliquot was digested with trypsin and the resulting peptides separated by reversed-phase high-performance liquid chromatography (HPLC).
15702487	10	38	theme	liquid	1890:1895	arg1	chromatography					1897:1910	reversed-phase high-performance liquid chromatography	1858:1910	reversed-phase high-performance liquid chromatography (HPLC)	1858:1917	The other aliquot was digested with trypsin and the resulting peptides separated by reversed-phase high-performance liquid chromatography (HPLC).
15702487	4	39	theme	site-specific	798:810	arg1	details					812:818	site-specific details	798:818	site-specific details concerning the glycosylation	798:847	Glycomics studies most often aim at identifying glycosylation sites, and thus are performed on deglycosylated proteins resulting in loss of site-specific details concerning the glycosylation.
15702487	2	40	theme	important	406:414	arg1	information					416:426	important information	406:426	important information to the field of proteomics	406:453	As protein tridimensional structures are related to function, the study of glycans and their impact on protein folding can provide important information to the field of proteomics.
15702487	13	41	theme	structures	2216:2225	arg1	identification					2182:2195	identification	2182:2195	identification of possible glycan structures	2182:2225	Compositions of glycans present were proposed, and identification of possible glycan structures was conducted using MS/MS and StrOligo.
15702487	5	42	theme	glycopeptides	994:1006	arg1	glycoproteins					922:934	either whole glycoproteins	909:934	either whole glycoproteins	909:934	In order to obtain such details by mass spectrometry (MS), either whole glycoproteins must be digested and analyzed as mixtures of peptides and glycopeptides, or glycans must be isolated from glycopeptide fractions and analyzed as pools.
15702487	5	42	theme	glycopeptides	994:1006	arg1	mixtures					969:976	mixtures	969:976	mixtures of peptides and glycopeptides	969:1006	In order to obtain such details by mass spectrometry (MS), either whole glycoproteins must be digested and analyzed as mixtures of peptides and glycopeptides, or glycans must be isolated from glycopeptide fractions and analyzed as pools.
15702487	10	43	theme	reversed-phase	1858:1871	arg1	HPLC					1913:1916	HPLC	1913:1916	HPLC	1913:1916	The other aliquot was digested with trypsin and the resulting peptides separated by reversed-phase high-performance liquid chromatography (HPLC).
15702487	10	43	theme	reversed-phase	1858:1871	arg1	chromatography					1897:1910	reversed-phase high-performance liquid chromatography	1858:1910	reversed-phase high-performance liquid chromatography (HPLC)	1858:1917	The other aliquot was digested with trypsin and the resulting peptides separated by reversed-phase high-performance liquid chromatography (HPLC).
15702487	0	44	theme	integrin	44:51	arg1	beta					61:64	human integrin alpha 5 beta 1	38:66	human integrin alpha 5 beta 1 glycosylation	38:80	Global and site-specific detection of human integrin alpha 5 beta 1 glycosylation using tandem mass spectrometry and the StrOligo algorithm.
15702487	9	45	theme	first	1619:1623	arg1	aliquot					1625:1631	the first aliquot	1615:1631	the first aliquot	1615:1631	The sample was divided in two aliquots, and glycans from the first aliquot were released enzymatically, labelled with 2-aminobenzamide, and identified using tandem mass spectrometry (MS/MS) and the StrOligo program.
15702487	10	46	theme	high-performance	1873:1888	arg1	HPLC					1913:1916	HPLC	1913:1916	HPLC	1913:1916	The other aliquot was digested with trypsin and the resulting peptides separated by reversed-phase high-performance liquid chromatography (HPLC).
15702487	10	46	theme	high-performance	1873:1888	arg1	chromatography					1897:1910	reversed-phase high-performance liquid chromatography	1858:1910	reversed-phase high-performance liquid chromatography (HPLC)	1858:1917	The other aliquot was digested with trypsin and the resulting peptides separated by reversed-phase high-performance liquid chromatography (HPLC).
15702487	5	47	gly	glycopeptide	1042:1053	arg2	glycopeptide					1042:1053	glycopeptide	1042:1053	glycopeptide	1042:1053	In order to obtain such details by mass spectrometry (MS), either whole glycoproteins must be digested and analyzed as mixtures of peptides and glycopeptides, or glycans must be isolated from glycopeptide fractions and analyzed as pools.
15702487	3	48	theme	glycomics	477:485	arg1	subdiscipline					460:472	The subdiscipline	456:472	The subdiscipline of glycomics (or glycoproteomics)	456:506	The subdiscipline of glycomics (or glycoproteomics) is rapidly growing in importance as glycans in proteins have shown to be involved in protein-protein or protein-(drug, virus, antibody) interactions.
15702487	2	49	theme	impact	368:373	arg1	study					341:345	the study	337:345	the study of glycans and their impact on protein folding	337:392	As protein tridimensional structures are related to function, the study of glycans and their impact on protein folding can provide important information to the field of proteomics.
15702487	13	50	theme	possible	2200:2207	arg1	structures					2216:2225	possible glycan structures	2200:2225	possible glycan structures	2200:2225	Compositions of glycans present were proposed, and identification of possible glycan structures was conducted using MS/MS and StrOligo.
15702487	5	51	theme	peptides	981:988	arg1	glycoproteins					922:934	either whole glycoproteins	909:934	either whole glycoproteins	909:934	In order to obtain such details by mass spectrometry (MS), either whole glycoproteins must be digested and analyzed as mixtures of peptides and glycopeptides, or glycans must be isolated from glycopeptide fractions and analyzed as pools.
15702487	5	51	theme	peptides	981:988	arg1	mixtures					969:976	mixtures	969:976	mixtures of peptides and glycopeptides	969:1006	In order to obtain such details by mass spectrometry (MS), either whole glycoproteins must be digested and analyzed as mixtures of peptides and glycopeptides, or glycans must be isolated from glycopeptide fractions and analyzed as pools.
15702487	6	52	theme	specific	1297:1304	arg1	site					1306:1309	a specific site	1295:1309	a specific site	1295:1309	This article describes parallel experiments involving both approaches, designed to take advantage of the StrOligo algorithm functionalities with the aim of characterizing glycosylation microheterogeneity on a specific site.
15702487	3	53	dep	interactions	644:655	arg1	virus					627:631	protein-protein or protein-(drug, virus, antibody) interactions	593:655	virus	627:631	The subdiscipline of glycomics (or glycoproteomics) is rapidly growing in importance as glycans in proteins have shown to be involved in protein-protein or protein-(drug, virus, antibody) interactions.
15702487	3	53	dep	interactions	644:655	arg1	antibody					634:641	protein-protein or protein-(drug, virus, antibody) interactions	593:655	antibody	634:641	The subdiscipline of glycomics (or glycoproteomics) is rapidly growing in importance as glycans in proteins have shown to be involved in protein-protein or protein-(drug, virus, antibody) interactions.
15702487	6	54	theme	glycosylation	1259:1271	arg1	microheterogeneity					1273:1290	glycosylation microheterogeneity	1259:1290	glycosylation microheterogeneity	1259:1290	This article describes parallel experiments involving both approaches, designed to take advantage of the StrOligo algorithm functionalities with the aim of characterizing glycosylation microheterogeneity on a specific site.
15702487	2	55	theme	protein	278:284	arg1	structures					301:310	protein tridimensional structures	278:310	protein tridimensional structures	278:310	As protein tridimensional structures are related to function, the study of glycans and their impact on protein folding can provide important information to the field of proteomics.
15702487	7	56	used	used	1456:1459	arg2	instrument					1366:1375	A hybrid quadrupole-quadrupole-time-of-flight (QqTOF) instrument	1312:1375	A hybrid quadrupole-quadrupole-time-of-flight (QqTOF) instrument equipped with a matrix-assisted laser desorption/ionization (MALDI) source	1312:1450	A hybrid quadrupole-quadrupole-time-of-flight (QqTOF) instrument equipped with a matrix-assisted laser desorption/ionization (MALDI) source was used.
15702487	2	57	from	impact	368:373	arg1	folding					386:392	protein folding	378:392	protein folding	378:392	As protein tridimensional structures are related to function, the study of glycans and their impact on protein folding can provide important information to the field of proteomics.
15702487	9	58	theme	mass	1722:1725	arg1	spectrometry					1727:1738	tandem mass spectrometry	1715:1738	tandem mass spectrometry (MS/MS)	1715:1746	The sample was divided in two aliquots, and glycans from the first aliquot were released enzymatically, labelled with 2-aminobenzamide, and identified using tandem mass spectrometry (MS/MS) and the StrOligo program.
15702487	9	58	theme	mass	1722:1725	arg1	MS/MS					1741:1745	MS/MS	1741:1745	MS/MS	1741:1745	The sample was divided in two aliquots, and glycans from the first aliquot were released enzymatically, labelled with 2-aminobenzamide, and identified using tandem mass spectrometry (MS/MS) and the StrOligo program.
15702487	5	59	theme	glycopeptide	1042:1053	arg1	fractions					1055:1063	glycopeptide fractions	1042:1063	glycopeptide fractions	1042:1063	In order to obtain such details by mass spectrometry (MS), either whole glycoproteins must be digested and analyzed as mixtures of peptides and glycopeptides, or glycans must be isolated from glycopeptide fractions and analyzed as pools.
15702487	12	60	theme	sequence	2121:2128	arg1	detection					2045:2053	detection	2045:2053	detection of a glycopeptide (several glycoforms)	2045:2092	These spectra allowed, by comparison, detection of a glycopeptide (several glycoforms) and elucidation of peptide sequence.
15702487	12	60	theme	sequence	2121:2128	arg1	elucidation					2098:2108	elucidation	2098:2108	elucidation of peptide sequence	2098:2128	These spectra allowed, by comparison, detection of a glycopeptide (several glycoforms) and elucidation of peptide sequence.
15702487	13	61	theme	present	2155:2161	arg1	glycans					2147:2153	glycans	2147:2153	glycans present	2147:2161	Compositions of glycans present were proposed, and identification of possible glycan structures was conducted using MS/MS and StrOligo.
15702487	7	62	theme	laser	1409:1413	arg1	MALDI					1438:1442	MALDI	1438:1442	MALDI	1438:1442	A hybrid quadrupole-quadrupole-time-of-flight (QqTOF) instrument equipped with a matrix-assisted laser desorption/ionization (MALDI) source was used.
15702487	7	62	theme	laser	1409:1413	arg1	desorption/ionization					1415:1435	matrix-assisted laser desorption/ionization	1393:1435	a matrix-assisted laser desorption/ionization (MALDI) source	1391:1450	A hybrid quadrupole-quadrupole-time-of-flight (QqTOF) instrument equipped with a matrix-assisted laser desorption/ionization (MALDI) source was used.
15702487	3	63	theme	protein-	612:619	arg1	interactions					644:655	protein-protein or protein-(drug, virus, antibody) interactions	593:655	interactions	644:655	The subdiscipline of glycomics (or glycoproteomics) is rapidly growing in importance as glycans in proteins have shown to be involved in protein-protein or protein-(drug, virus, antibody) interactions.
15702487	8	64	theme	integrin	1512:1519	arg1	subunits					1494:1501	alpha 5 beta 1 subunits	1479:1501	alpha 5 beta 1 subunits of human integrin	1479:1519	Glycosylation of alpha 5 beta 1 subunits of human integrin was studied to test the methodology.
15702487	0	65	theme	beta	61:64	arg1	glycosylation					68:80	human integrin alpha 5 beta 1 glycosylation	38:80	human integrin alpha 5 beta 1 glycosylation	38:80	Global and site-specific detection of human integrin alpha 5 beta 1 glycosylation using tandem mass spectrometry and the StrOligo algorithm.
15702487	11	66	theme	glycan	1991:1996	arg1	release					1998:2004	glycan release	1991:2004	glycan release	1991:2004	A specific collected fraction was then analyzed by MS before and after glycan release.
15702487	4	67	theme	Glycomics	658:666	arg1	studies					668:674	Glycomics studies	658:674	Glycomics studies	658:674	Glycomics studies most often aim at identifying glycosylation sites, and thus are performed on deglycosylated proteins resulting in loss of site-specific details concerning the glycosylation.
15702487	0	68	theme	glycosylation	68:80	arg1	detection					25:33	Global and site-specific detection	0:33	Global and site-specific detection of human integrin alpha 5 beta 1 glycosylation	0:80	Global and site-specific detection of human integrin alpha 5 beta 1 glycosylation using tandem mass spectrometry and the StrOligo algorithm.
15702487	5	69	theme	mass	885:888	arg1	MS					904:905	MS	904:905	MS	904:905	In order to obtain such details by mass spectrometry (MS), either whole glycoproteins must be digested and analyzed as mixtures of peptides and glycopeptides, or glycans must be isolated from glycopeptide fractions and analyzed as pools.
15702487	5	69	theme	mass	885:888	arg1	spectrometry					890:901	mass spectrometry	885:901	mass spectrometry (MS)	885:906	In order to obtain such details by mass spectrometry (MS), either whole glycoproteins must be digested and analyzed as mixtures of peptides and glycopeptides, or glycans must be isolated from glycopeptide fractions and analyzed as pools.
15702487	0	70	theme	tandem	88:93	arg1	spectrometry					100:111	tandem mass spectrometry	88:111	tandem mass spectrometry	88:111	Global and site-specific detection of human integrin alpha 5 beta 1 glycosylation using tandem mass spectrometry and the StrOligo algorithm.
15702487	12	71	gly	glycopeptide	2060:2071	arg2	glycoforms					2082:2091	several glycoforms	2074:2091	several glycoforms	2074:2091	These spectra allowed, by comparison, detection of a glycopeptide (several glycoforms) and elucidation of peptide sequence.
15702487	12	71	gly	glycopeptide	2060:2071	arg2	glycopeptide					2060:2071	a glycopeptide	2058:2071	a glycopeptide (several glycoforms)	2058:2092	These spectra allowed, by comparison, detection of a glycopeptide (several glycoforms) and elucidation of peptide sequence.
15702487	7	72	theme	QqTOF	1359:1363	arg1	instrument					1366:1375	A hybrid quadrupole-quadrupole-time-of-flight (QqTOF) instrument	1312:1375	A hybrid quadrupole-quadrupole-time-of-flight (QqTOF) instrument equipped with a matrix-assisted laser desorption/ionization (MALDI) source	1312:1450	A hybrid quadrupole-quadrupole-time-of-flight (QqTOF) instrument equipped with a matrix-assisted laser desorption/ionization (MALDI) source was used.
15702487	5	73	gly	glycoproteins	922:934	arg1	glycoproteins					922:934	either whole glycoproteins	909:934	either whole glycoproteins	909:934	In order to obtain such details by mass spectrometry (MS), either whole glycoproteins must be digested and analyzed as mixtures of peptides and glycopeptides, or glycans must be isolated from glycopeptide fractions and analyzed as pools.
15702487	5	73	gly	glycoproteins	922:934	arg1	mixtures					969:976	mixtures	969:976	mixtures of peptides and glycopeptides	969:1006	In order to obtain such details by mass spectrometry (MS), either whole glycoproteins must be digested and analyzed as mixtures of peptides and glycopeptides, or glycans must be isolated from glycopeptide fractions and analyzed as pools.
15702487	7	74	theme	quadrupole-quadrupole-time-of-flight	1321:1356	arg1	instrument					1366:1375	A hybrid quadrupole-quadrupole-time-of-flight (QqTOF) instrument	1312:1375	A hybrid quadrupole-quadrupole-time-of-flight (QqTOF) instrument equipped with a matrix-assisted laser desorption/ionization (MALDI) source	1312:1450	A hybrid quadrupole-quadrupole-time-of-flight (QqTOF) instrument equipped with a matrix-assisted laser desorption/ionization (MALDI) source was used.
15702487	11	75	theme	specific	1922:1929	arg1	fraction					1941:1948	A specific collected fraction	1920:1948	A specific collected fraction	1920:1948	A specific collected fraction was then analyzed by MS before and after glycan release.
15702487	1	76	gly	glycoproteins	260:272	arg1	glycoproteins					260:272	glycoproteins	260:272	glycoproteins	260:272	Glycans are oligosaccharides associated with proteins, and are known to confer specific functions and conformations on glycoproteins.
15702487	0	77	theme	human	38:42	arg1	beta					61:64	human integrin alpha 5 beta 1	38:66	human integrin alpha 5 beta 1 glycosylation	38:80	Global and site-specific detection of human integrin alpha 5 beta 1 glycosylation using tandem mass spectrometry and the StrOligo algorithm.
15702487	5	78	attach	isolated	1028:1035	arg2	glycans					1012:1018	glycans	1012:1018	glycans	1012:1018	In order to obtain such details by mass spectrometry (MS), either whole glycoproteins must be digested and analyzed as mixtures of peptides and glycopeptides, or glycans must be isolated from glycopeptide fractions and analyzed as pools.
15702487	5	78	attach	isolated	1028:1035	arg1	fractions					1055:1063	glycopeptide fractions	1042:1063	glycopeptide fractions	1042:1063	In order to obtain such details by mass spectrometry (MS), either whole glycoproteins must be digested and analyzed as mixtures of peptides and glycopeptides, or glycans must be isolated from glycopeptide fractions and analyzed as pools.
15702487	5	78	attach	isolated	1028:1035	arg2	pools					1081:1085	pools	1081:1085	pools	1081:1085	In order to obtain such details by mass spectrometry (MS), either whole glycoproteins must be digested and analyzed as mixtures of peptides and glycopeptides, or glycans must be isolated from glycopeptide fractions and analyzed as pools.
15702487	3	79	theme	drug	621:624	arg1	interactions					644:655	protein-protein or protein-(drug, virus, antibody) interactions	593:655	interactions	644:655	The subdiscipline of glycomics (or glycoproteomics) is rapidly growing in importance as glycans in proteins have shown to be involved in protein-protein or protein-(drug, virus, antibody) interactions.
15702487	0	80	theme	alpha	53:57	arg1	beta					61:64	human integrin alpha 5 beta 1	38:66	human integrin alpha 5 beta 1 glycosylation	38:80	Global and site-specific detection of human integrin alpha 5 beta 1 glycosylation using tandem mass spectrometry and the StrOligo algorithm.
15702487	6	81	theme	parallel	1111:1118	arg1	experiments					1120:1130	parallel experiments	1111:1130	parallel experiments	1111:1130	This article describes parallel experiments involving both approaches, designed to take advantage of the StrOligo algorithm functionalities with the aim of characterizing glycosylation microheterogeneity on a specific site.
15702487	0	82	theme	StrOligo	121:128	arg1	algorithm					130:138	the StrOligo algorithm	117:138	the StrOligo algorithm	117:138	Global and site-specific detection of human integrin alpha 5 beta 1 glycosylation using tandem mass spectrometry and the StrOligo algorithm.
15702487	4	83	theme	details	812:818	arg1	loss					790:793	loss	790:793	loss of site-specific details concerning the glycosylation	790:847	Glycomics studies most often aim at identifying glycosylation sites, and thus are performed on deglycosylated proteins resulting in loss of site-specific details concerning the glycosylation.
15702487	2	84	from	folding	386:392	arg1	study					341:345	the study	337:345	the study of glycans and their impact on protein folding	337:392	As protein tridimensional structures are related to function, the study of glycans and their impact on protein folding can provide important information to the field of proteomics.
15702487	1	85	theme	specific	220:227	arg1	functions					229:237	specific functions	220:237	specific functions	220:237	Glycans are oligosaccharides associated with proteins, and are known to confer specific functions and conformations on glycoproteins.
15702487	2	86	theme	proteomics	444:453	arg1	field					435:439	the field	431:439	the field of proteomics	431:453	As protein tridimensional structures are related to function, the study of glycans and their impact on protein folding can provide important information to the field of proteomics.
15702487	13	87	theme	glycan	2209:2214	arg1	structures					2216:2225	possible glycan structures	2200:2225	possible glycan structures	2200:2225	Compositions of glycans present were proposed, and identification of possible glycan structures was conducted using MS/MS and StrOligo.
23335398	0	0	theme	essential	74:82	arg1	breakthrough					61:72	the mass spectrometric breakthrough	38:72	Electron transfer dissociation (ETD): the mass spectrometric breakthrough essential for O-GlcNAc protein site assignments-a study of the O-GlcNAcylated protein host cell factor C1.	0:179	Electron transfer dissociation (ETD): the mass spectrometric breakthrough essential for O-GlcNAc protein site assignments-a study of the O-GlcNAcylated protein host cell factor C1.
23335398	2	1	theme	signaling	478:486	arg1	field					415:419	The field	411:419	The field of intracellular O-GlcNAc (O-linked N-acetylglucosamine) signaling	411:486	The field of intracellular O-GlcNAc (O-linked N-acetylglucosamine) signaling has especially advanced with the advent of ETD MS. Only within the last five years have proteomic-scale experiments utilizing ETD allowed the assignment of hundreds of O-GlcNAc sites within cells and subcellular structures.
23335398	0	2	theme	C1	177:178	arg1	study					124:128	O-GlcNAc protein site assignments-a study	88:128	O-GlcNAc protein site assignments-a study of the O-GlcNAcylated protein host cell factor C1	88:178	Electron transfer dissociation (ETD): the mass spectrometric breakthrough essential for O-GlcNAc protein site assignments-a study of the O-GlcNAcylated protein host cell factor C1.
23335398	6	3	theme	protein	1339:1345	arg1	PTMs					1321:1324	the PTMs	1317:1324	the PTMs of the HCF-1 protein isolated from HEK293T cells	1317:1373	ETD, along with higher energy collisional dissociation (HCD) MS, was employed to assign the PTMs of the HCF-1 protein isolated from HEK293T cells.
23335398	4	4	theme	O-GlcNAcylated	1047:1060	arg1	C1					1087:1088	the extensively O-GlcNAcylated protein Host Cell Factor C1	1031:1088	the extensively O-GlcNAcylated protein Host Cell Factor C1 (HCF-1)	1031:1096	Here, we discuss the advantages of using ETD, complimented with collisional-activation MS, in a study of the extensively O-GlcNAcylated protein Host Cell Factor C1 (HCF-1).
23335398	4	4	theme	O-GlcNAcylated	1047:1060	arg1	HCF-1					1091:1095	HCF-1	1091:1095	HCF-1	1091:1095	Here, we discuss the advantages of using ETD, complimented with collisional-activation MS, in a study of the extensively O-GlcNAcylated protein Host Cell Factor C1 (HCF-1).
23335398	5	5	theme	transcriptional	1110:1124	arg1	HCF-1					1099:1103	HCF-1	1099:1103	HCF-1	1099:1103	HCF-1 is a transcriptional coregulator that forms a stable complex with O-GlcNAc transferase and controls cell cycle progression.
23335398	5	5	theme	transcriptional	1110:1124	arg1	coregulator					1126:1136	a transcriptional coregulator	1108:1136	a transcriptional coregulator that forms a stable complex with O-GlcNAc transferase and controls cell cycle progression	1108:1226	HCF-1 is a transcriptional coregulator that forms a stable complex with O-GlcNAc transferase and controls cell cycle progression.
23335398	3	6	with	interaction	897:907	arg1	PTMs					920:923	other PTMs	914:923	other PTMs	914:923	Our ability to identify and unambiguously assign the site of O-GlcNAc modifications using ETD is rapidly increasing our understanding of this regulatory glycosylation and its potential interaction with other PTMs.
23335398	0	7	theme	factor	170:175	arg1	C1					177:178	the O-GlcNAcylated protein host cell factor C1	133:178	the O-GlcNAcylated protein host cell factor C1	133:178	Electron transfer dissociation (ETD): the mass spectrometric breakthrough essential for O-GlcNAc protein site assignments-a study of the O-GlcNAcylated protein host cell factor C1.
23335398	4	8	theme	C1	1087:1088	arg1	study					1022:1026	a study	1020:1026	a study of the extensively O-GlcNAcylated protein Host Cell Factor C1 (HCF-1)	1020:1096	Here, we discuss the advantages of using ETD, complimented with collisional-activation MS, in a study of the extensively O-GlcNAcylated protein Host Cell Factor C1 (HCF-1).
23335398	4	9	theme	Cell	1075:1078	arg1	C1					1087:1088	the extensively O-GlcNAcylated protein Host Cell Factor C1	1031:1088	the extensively O-GlcNAcylated protein Host Cell Factor C1 (HCF-1)	1031:1096	Here, we discuss the advantages of using ETD, complimented with collisional-activation MS, in a study of the extensively O-GlcNAcylated protein Host Cell Factor C1 (HCF-1).
23335398	4	9	theme	Cell	1075:1078	arg1	HCF-1					1091:1095	HCF-1	1091:1095	HCF-1	1091:1095	Here, we discuss the advantages of using ETD, complimented with collisional-activation MS, in a study of the extensively O-GlcNAcylated protein Host Cell Factor C1 (HCF-1).
23335398	1	10	theme	electron	251:258	arg1	capture					260:266	electron capture and electron transfer dissociation	251:301	capture	260:266	The development of electron-based, unimolecular dissociation MS, i.e. electron capture and electron transfer dissociation (ECD and ETD, respectively), has greatly increased the speed and reliability of labile PTM site assignment.
23335398	0	11	theme	O-GlcNAc	88:95	arg1	study					124:128	O-GlcNAc protein site assignments-a study	88:128	O-GlcNAc protein site assignments-a study of the O-GlcNAcylated protein host cell factor C1	88:178	Electron transfer dissociation (ETD): the mass spectrometric breakthrough essential for O-GlcNAc protein site assignments-a study of the O-GlcNAcylated protein host cell factor C1.
23335398	2	12	theme	hundreds	644:651	arg1	assignment					630:639	the assignment	626:639	the assignment of hundreds of O-GlcNAc sites	626:669	The field of intracellular O-GlcNAc (O-linked N-acetylglucosamine) signaling has especially advanced with the advent of ETD MS. Only within the last five years have proteomic-scale experiments utilizing ETD allowed the assignment of hundreds of O-GlcNAc sites within cells and subcellular structures.
23335398	7	13	theme	O-GlcNAcylation	1402:1416	arg1	phosphorylation					1432:1446	phosphorylation	1432:1446	phosphorylation	1432:1446	These include 19 sites of O-GlcNAcylation, two sites of phosphorylation, and two sites bearing dimethylarginine, and showcase the residue-specific, PTM complexity of this regulator of cell proliferation.
23335398	7	13	theme	O-GlcNAcylation	1402:1416	arg1	O-GlcNAcylation					1402:1416	O-GlcNAcylation	1402:1416	O-GlcNAcylation	1402:1416	These include 19 sites of O-GlcNAcylation, two sites of phosphorylation, and two sites bearing dimethylarginine, and showcase the residue-specific, PTM complexity of this regulator of cell proliferation.
23335398	7	13	theme	O-GlcNAcylation	1402:1416	arg1	sites					1423:1427	two sites	1419:1427	two sites of phosphorylation	1419:1446	These include 19 sites of O-GlcNAcylation, two sites of phosphorylation, and two sites bearing dimethylarginine, and showcase the residue-specific, PTM complexity of this regulator of cell proliferation.
23335398	7	13	theme	O-GlcNAcylation	1402:1416	arg1	sites					1393:1397	19 sites	1390:1397	19 sites of O-GlcNAcylation	1390:1416	These include 19 sites of O-GlcNAcylation, two sites of phosphorylation, and two sites bearing dimethylarginine, and showcase the residue-specific, PTM complexity of this regulator of cell proliferation.
23335398	7	13	theme	O-GlcNAcylation	1402:1416	arg1	sites					1457:1461	two sites	1453:1461	two sites bearing dimethylarginine	1453:1486	These include 19 sites of O-GlcNAcylation, two sites of phosphorylation, and two sites bearing dimethylarginine, and showcase the residue-specific, PTM complexity of this regulator of cell proliferation.
23335398	3	14	theme	potential	887:895	arg1	interaction					897:907	its potential interaction	883:907	its potential interaction with other PTMs	883:923	Our ability to identify and unambiguously assign the site of O-GlcNAc modifications using ETD is rapidly increasing our understanding of this regulatory glycosylation and its potential interaction with other PTMs.
23335398	5	15	theme	cycle	1210:1214	arg1	progression					1216:1226	cell cycle progression	1205:1226	cell cycle progression	1205:1226	HCF-1 is a transcriptional coregulator that forms a stable complex with O-GlcNAc transferase and controls cell cycle progression.
23335398	6	16	theme	HCF-1	1333:1337	arg1	protein					1339:1345	the HCF-1 protein	1329:1345	the HCF-1 protein isolated from HEK293T cells	1329:1373	ETD, along with higher energy collisional dissociation (HCD) MS, was employed to assign the PTMs of the HCF-1 protein isolated from HEK293T cells.
23335398	6	17	theme	dissociation	1271:1282	arg1	MS					1290:1291	higher energy collisional dissociation (HCD) MS	1245:1291	higher energy collisional dissociation (HCD) MS	1245:1291	ETD, along with higher energy collisional dissociation (HCD) MS, was employed to assign the PTMs of the HCF-1 protein isolated from HEK293T cells.
23335398	6	18	dep	along	1234:1238	arg1	with					1240:1243	with	1240:1243	with	1240:1243	ETD, along with higher energy collisional dissociation (HCD) MS, was employed to assign the PTMs of the HCF-1 protein isolated from HEK293T cells.
23335398	0	19	theme	site	105:108	arg1	study					124:128	O-GlcNAc protein site assignments-a study	88:128	O-GlcNAc protein site assignments-a study of the O-GlcNAcylated protein host cell factor C1	88:178	Electron transfer dissociation (ETD): the mass spectrometric breakthrough essential for O-GlcNAc protein site assignments-a study of the O-GlcNAcylated protein host cell factor C1.
23335398	7	20	theme	phosphorylation	1432:1446	arg1	phosphorylation					1432:1446	phosphorylation	1432:1446	phosphorylation	1432:1446	These include 19 sites of O-GlcNAcylation, two sites of phosphorylation, and two sites bearing dimethylarginine, and showcase the residue-specific, PTM complexity of this regulator of cell proliferation.
23335398	7	20	theme	phosphorylation	1432:1446	arg1	O-GlcNAcylation					1402:1416	O-GlcNAcylation	1402:1416	O-GlcNAcylation	1402:1416	These include 19 sites of O-GlcNAcylation, two sites of phosphorylation, and two sites bearing dimethylarginine, and showcase the residue-specific, PTM complexity of this regulator of cell proliferation.
23335398	7	20	theme	phosphorylation	1432:1446	arg1	sites					1423:1427	two sites	1419:1427	two sites of phosphorylation	1419:1446	These include 19 sites of O-GlcNAcylation, two sites of phosphorylation, and two sites bearing dimethylarginine, and showcase the residue-specific, PTM complexity of this regulator of cell proliferation.
23335398	7	20	theme	phosphorylation	1432:1446	arg1	sites					1393:1397	19 sites	1390:1397	19 sites of O-GlcNAcylation	1390:1416	These include 19 sites of O-GlcNAcylation, two sites of phosphorylation, and two sites bearing dimethylarginine, and showcase the residue-specific, PTM complexity of this regulator of cell proliferation.
23335398	7	20	theme	phosphorylation	1432:1446	arg1	sites					1457:1461	two sites	1453:1461	two sites bearing dimethylarginine	1453:1486	These include 19 sites of O-GlcNAcylation, two sites of phosphorylation, and two sites bearing dimethylarginine, and showcase the residue-specific, PTM complexity of this regulator of cell proliferation.
23335398	6	21	theme	collisional	1259:1269	arg1	MS					1290:1291	higher energy collisional dissociation (HCD) MS	1245:1291	higher energy collisional dissociation (HCD) MS	1245:1291	ETD, along with higher energy collisional dissociation (HCD) MS, was employed to assign the PTMs of the HCF-1 protein isolated from HEK293T cells.
23335398	0	22	theme	protein	97:103	arg1	study					124:128	O-GlcNAc protein site assignments-a study	88:128	O-GlcNAc protein site assignments-a study of the O-GlcNAcylated protein host cell factor C1	88:178	Electron transfer dissociation (ETD): the mass spectrometric breakthrough essential for O-GlcNAc protein site assignments-a study of the O-GlcNAcylated protein host cell factor C1.
23335398	6	23	theme	energy	1252:1257	arg1	MS					1290:1291	higher energy collisional dissociation (HCD) MS	1245:1291	higher energy collisional dissociation (HCD) MS	1245:1291	ETD, along with higher energy collisional dissociation (HCD) MS, was employed to assign the PTMs of the HCF-1 protein isolated from HEK293T cells.
23335398	7	24	theme	proliferation	1565:1577	arg1	regulator					1547:1555	this regulator	1542:1555	this regulator of cell proliferation	1542:1577	These include 19 sites of O-GlcNAcylation, two sites of phosphorylation, and two sites bearing dimethylarginine, and showcase the residue-specific, PTM complexity of this regulator of cell proliferation.
23335398	3	25	theme	other	914:918	arg1	PTMs					920:923	other PTMs	914:923	other PTMs	914:923	Our ability to identify and unambiguously assign the site of O-GlcNAc modifications using ETD is rapidly increasing our understanding of this regulatory glycosylation and its potential interaction with other PTMs.
23335398	7	26	dep	residue-specific	1506:1521	arg1	PTM					1524:1526	PTM	1524:1526	PTM	1524:1526	These include 19 sites of O-GlcNAcylation, two sites of phosphorylation, and two sites bearing dimethylarginine, and showcase the residue-specific, PTM complexity of this regulator of cell proliferation.
23335398	0	27	theme	transfer	9:16	arg1	dissociation					18:29	Electron transfer dissociation	0:29	Electron transfer dissociation (ETD): the mass spectrometric breakthrough essential for O-GlcNAc protein site assignments-a study of the O-GlcNAcylated protein host cell factor C1.	0:179	Electron transfer dissociation (ETD): the mass spectrometric breakthrough essential for O-GlcNAc protein site assignments-a study of the O-GlcNAcylated protein host cell factor C1.
23335398	0	27	theme	transfer	9:16	arg1	ETD					32:34	ETD	32:34	ETD	32:34	Electron transfer dissociation (ETD): the mass spectrometric breakthrough essential for O-GlcNAc protein site assignments-a study of the O-GlcNAcylated protein host cell factor C1.
23335398	5	28	theme	O-GlcNAc	1171:1178	arg1	transferase					1180:1190	O-GlcNAc transferase	1171:1190	O-GlcNAc transferase	1171:1190	HCF-1 is a transcriptional coregulator that forms a stable complex with O-GlcNAc transferase and controls cell cycle progression.
23335398	2	29	with	advanced	503:510	arg1	advent					521:526	the advent	517:526	the advent of ETD MS. Only within the last five years have proteomic-scale experiments utilizing ETD allowed the assignment of hundreds of O-GlcNAc sites within cells and subcellular structures	517:709	The field of intracellular O-GlcNAc (O-linked N-acetylglucosamine) signaling has especially advanced with the advent of ETD MS. Only within the last five years have proteomic-scale experiments utilizing ETD allowed the assignment of hundreds of O-GlcNAc sites within cells and subcellular structures.
23335398	2	30	theme	last	555:558	arg1	years					565:569	the last five years	551:569	the last five years	551:569	The field of intracellular O-GlcNAc (O-linked N-acetylglucosamine) signaling has especially advanced with the advent of ETD MS. Only within the last five years have proteomic-scale experiments utilizing ETD allowed the assignment of hundreds of O-GlcNAc sites within cells and subcellular structures.
23335398	0	31	theme	Electron	0:7	arg1	dissociation					18:29	Electron transfer dissociation	0:29	Electron transfer dissociation (ETD): the mass spectrometric breakthrough essential for O-GlcNAc protein site assignments-a study of the O-GlcNAcylated protein host cell factor C1.	0:179	Electron transfer dissociation (ETD): the mass spectrometric breakthrough essential for O-GlcNAc protein site assignments-a study of the O-GlcNAcylated protein host cell factor C1.
23335398	0	31	theme	Electron	0:7	arg1	ETD					32:34	ETD	32:34	ETD	32:34	Electron transfer dissociation (ETD): the mass spectrometric breakthrough essential for O-GlcNAc protein site assignments-a study of the O-GlcNAcylated protein host cell factor C1.
23335398	1	32	theme	electron	272:279	arg1	dissociation					290:301	electron capture and electron transfer dissociation	251:301	dissociation	290:301	The development of electron-based, unimolecular dissociation MS, i.e. electron capture and electron transfer dissociation (ECD and ETD, respectively), has greatly increased the speed and reliability of labile PTM site assignment.
23335398	2	33	theme	sites	665:669	arg1	hundreds					644:651	hundreds	644:651	hundreds of O-GlcNAc sites	644:669	The field of intracellular O-GlcNAc (O-linked N-acetylglucosamine) signaling has especially advanced with the advent of ETD MS. Only within the last five years have proteomic-scale experiments utilizing ETD allowed the assignment of hundreds of O-GlcNAc sites within cells and subcellular structures.
23335398	1	34	dep	capture	260:266	arg1	ETD					312:314	ETD	312:314	ETD	312:314	The development of electron-based, unimolecular dissociation MS, i.e. electron capture and electron transfer dissociation (ECD and ETD, respectively), has greatly increased the speed and reliability of labile PTM site assignment.
23335398	1	34	dep	capture	260:266	arg1	i.e.					246:249	i.e.	246:249	i.e.	246:249	The development of electron-based, unimolecular dissociation MS, i.e. electron capture and electron transfer dissociation (ECD and ETD, respectively), has greatly increased the speed and reliability of labile PTM site assignment.
23335398	1	34	dep	capture	260:266	arg1	ECD					304:306	ECD	304:306	ECD	304:306	The development of electron-based, unimolecular dissociation MS, i.e. electron capture and electron transfer dissociation (ECD and ETD, respectively), has greatly increased the speed and reliability of labile PTM site assignment.
23335398	2	35	theme	proteomic-scale	576:590	arg1	experiments					592:602	proteomic-scale experiments	576:602	proteomic-scale experiments utilizing ETD	576:616	The field of intracellular O-GlcNAc (O-linked N-acetylglucosamine) signaling has especially advanced with the advent of ETD MS. Only within the last five years have proteomic-scale experiments utilizing ETD allowed the assignment of hundreds of O-GlcNAc sites within cells and subcellular structures.
23335398	1	36	theme	transfer	281:288	arg1	dissociation					290:301	electron capture and electron transfer dissociation	251:301	dissociation	290:301	The development of electron-based, unimolecular dissociation MS, i.e. electron capture and electron transfer dissociation (ECD and ETD, respectively), has greatly increased the speed and reliability of labile PTM site assignment.
23335398	6	37	theme	HCD	1285:1287	arg1	MS					1290:1291	higher energy collisional dissociation (HCD) MS	1245:1291	higher energy collisional dissociation (HCD) MS	1245:1291	ETD, along with higher energy collisional dissociation (HCD) MS, was employed to assign the PTMs of the HCF-1 protein isolated from HEK293T cells.
23335398	2	38	link	O-linked	448:455	arg1	N-acetylglucosamine					457:475	O-linked N-acetylglucosamine	448:475	intracellular O-GlcNAc (O-linked N-acetylglucosamine) signaling	424:486	The field of intracellular O-GlcNAc (O-linked N-acetylglucosamine) signaling has especially advanced with the advent of ETD MS. Only within the last five years have proteomic-scale experiments utilizing ETD allowed the assignment of hundreds of O-GlcNAc sites within cells and subcellular structures.
23335398	0	39	theme	assignments-a	110:122	arg1	study					124:128	O-GlcNAc protein site assignments-a study	88:128	O-GlcNAc protein site assignments-a study of the O-GlcNAcylated protein host cell factor C1	88:178	Electron transfer dissociation (ETD): the mass spectrometric breakthrough essential for O-GlcNAc protein site assignments-a study of the O-GlcNAcylated protein host cell factor C1.
23335398	7	40	theme	residue-specific	1506:1521	arg1	complexity					1528:1537	the residue-specific, PTM complexity	1502:1537	the residue-specific, PTM complexity of this regulator of cell proliferation	1502:1577	These include 19 sites of O-GlcNAcylation, two sites of phosphorylation, and two sites bearing dimethylarginine, and showcase the residue-specific, PTM complexity of this regulator of cell proliferation.
23335398	2	41	theme	N-acetylglucosamine	457:475	arg1	signaling					478:486	intracellular O-GlcNAc (O-linked N-acetylglucosamine) signaling	424:486	intracellular O-GlcNAc (O-linked N-acetylglucosamine) signaling	424:486	The field of intracellular O-GlcNAc (O-linked N-acetylglucosamine) signaling has especially advanced with the advent of ETD MS. Only within the last five years have proteomic-scale experiments utilizing ETD allowed the assignment of hundreds of O-GlcNAc sites within cells and subcellular structures.
23335398	2	42	theme	ETD	531:533	arg1	advent					521:526	the advent	517:526	the advent of ETD MS. Only within the last five years have proteomic-scale experiments utilizing ETD allowed the assignment of hundreds of O-GlcNAc sites within cells and subcellular structures	517:709	The field of intracellular O-GlcNAc (O-linked N-acetylglucosamine) signaling has especially advanced with the advent of ETD MS. Only within the last five years have proteomic-scale experiments utilizing ETD allowed the assignment of hundreds of O-GlcNAc sites within cells and subcellular structures.
23335398	6	43	theme	higher	1245:1250	arg1	MS					1290:1291	higher energy collisional dissociation (HCD) MS	1245:1291	higher energy collisional dissociation (HCD) MS	1245:1291	ETD, along with higher energy collisional dissociation (HCD) MS, was employed to assign the PTMs of the HCF-1 protein isolated from HEK293T cells.
23335398	1	44	theme	electron-based	200:213	arg1	MS					242:243	electron-based, unimolecular dissociation MS	200:243	electron-based, unimolecular dissociation MS	200:243	The development of electron-based, unimolecular dissociation MS, i.e. electron capture and electron transfer dissociation (ECD and ETD, respectively), has greatly increased the speed and reliability of labile PTM site assignment.
23335398	2	45	theme	O-linked	448:455	arg1	N-acetylglucosamine					457:475	O-linked N-acetylglucosamine	448:475	intracellular O-GlcNAc (O-linked N-acetylglucosamine) signaling	424:486	The field of intracellular O-GlcNAc (O-linked N-acetylglucosamine) signaling has especially advanced with the advent of ETD MS. Only within the last five years have proteomic-scale experiments utilizing ETD allowed the assignment of hundreds of O-GlcNAc sites within cells and subcellular structures.
23335398	3	46	theme	O-GlcNAc	773:780	arg1	modifications					782:794	O-GlcNAc modifications	773:794	O-GlcNAc modifications using ETD	773:804	Our ability to identify and unambiguously assign the site of O-GlcNAc modifications using ETD is rapidly increasing our understanding of this regulatory glycosylation and its potential interaction with other PTMs.
23335398	5	47	theme	cell	1205:1208	arg1	progression					1216:1226	cell cycle progression	1205:1226	cell cycle progression	1205:1226	HCF-1 is a transcriptional coregulator that forms a stable complex with O-GlcNAc transferase and controls cell cycle progression.
23335398	7	48	theme	regulator	1547:1555	arg1	complexity					1528:1537	the residue-specific, PTM complexity	1502:1537	the residue-specific, PTM complexity of this regulator of cell proliferation	1502:1577	These include 19 sites of O-GlcNAcylation, two sites of phosphorylation, and two sites bearing dimethylarginine, and showcase the residue-specific, PTM complexity of this regulator of cell proliferation.
23335398	1	49	dep	speed	358:362	arg1	the					354:356	the	354:356	the	354:356	The development of electron-based, unimolecular dissociation MS, i.e. electron capture and electron transfer dissociation (ECD and ETD, respectively), has greatly increased the speed and reliability of labile PTM site assignment.
23335398	0	50	theme	protein	152:158	arg1	C1					177:178	the O-GlcNAcylated protein host cell factor C1	133:178	the O-GlcNAcylated protein host cell factor C1	133:178	Electron transfer dissociation (ETD): the mass spectrometric breakthrough essential for O-GlcNAc protein site assignments-a study of the O-GlcNAcylated protein host cell factor C1.
23335398	1	51	theme	labile	383:388	arg1	assignment					399:408	labile PTM site assignment	383:408	labile PTM site assignment	383:408	The development of electron-based, unimolecular dissociation MS, i.e. electron capture and electron transfer dissociation (ECD and ETD, respectively), has greatly increased the speed and reliability of labile PTM site assignment.
23335398	3	52	with	understanding	832:844	arg1	PTMs					920:923	other PTMs	914:923	other PTMs	914:923	Our ability to identify and unambiguously assign the site of O-GlcNAc modifications using ETD is rapidly increasing our understanding of this regulatory glycosylation and its potential interaction with other PTMs.
23335398	2	53	theme	O-GlcNAc	438:445	arg1	signaling					478:486	intracellular O-GlcNAc (O-linked N-acetylglucosamine) signaling	424:486	intracellular O-GlcNAc (O-linked N-acetylglucosamine) signaling	424:486	The field of intracellular O-GlcNAc (O-linked N-acetylglucosamine) signaling has especially advanced with the advent of ETD MS. Only within the last five years have proteomic-scale experiments utilizing ETD allowed the assignment of hundreds of O-GlcNAc sites within cells and subcellular structures.
23335398	5	54	theme	stable	1151:1156	arg1	complex					1158:1164	a stable complex	1149:1164	a stable complex with O-GlcNAc transferase	1149:1190	HCF-1 is a transcriptional coregulator that forms a stable complex with O-GlcNAc transferase and controls cell cycle progression.
23335398	0	55	theme	O-GlcNAcylated	137:150	arg1	C1					177:178	the O-GlcNAcylated protein host cell factor C1	133:178	the O-GlcNAcylated protein host cell factor C1	133:178	Electron transfer dissociation (ETD): the mass spectrometric breakthrough essential for O-GlcNAc protein site assignments-a study of the O-GlcNAcylated protein host cell factor C1.
23335398	1	56	theme	PTM	390:392	arg1	assignment					399:408	labile PTM site assignment	383:408	labile PTM site assignment	383:408	The development of electron-based, unimolecular dissociation MS, i.e. electron capture and electron transfer dissociation (ECD and ETD, respectively), has greatly increased the speed and reliability of labile PTM site assignment.
23335398	2	57	theme	subcellular	688:698	arg1	structures					700:709	subcellular structures	688:709	subcellular structures	688:709	The field of intracellular O-GlcNAc (O-linked N-acetylglucosamine) signaling has especially advanced with the advent of ETD MS. Only within the last five years have proteomic-scale experiments utilizing ETD allowed the assignment of hundreds of O-GlcNAc sites within cells and subcellular structures.
23335398	3	58	theme	glycosylation	865:877	arg1	interaction					897:907	its potential interaction	883:907	its potential interaction with other PTMs	883:923	Our ability to identify and unambiguously assign the site of O-GlcNAc modifications using ETD is rapidly increasing our understanding of this regulatory glycosylation and its potential interaction with other PTMs.
23335398	3	58	theme	glycosylation	865:877	arg1	understanding					832:844	our understanding	828:844	our understanding of this regulatory glycosylation	828:877	Our ability to identify and unambiguously assign the site of O-GlcNAc modifications using ETD is rapidly increasing our understanding of this regulatory glycosylation and its potential interaction with other PTMs.
23335398	2	59	theme	O-GlcNAc	656:663	arg1	sites					665:669	O-GlcNAc sites	656:669	O-GlcNAc sites	656:669	The field of intracellular O-GlcNAc (O-linked N-acetylglucosamine) signaling has especially advanced with the advent of ETD MS. Only within the last five years have proteomic-scale experiments utilizing ETD allowed the assignment of hundreds of O-GlcNAc sites within cells and subcellular structures.
23335398	0	60	theme	cell	165:168	arg1	C1					177:178	the O-GlcNAcylated protein host cell factor C1	133:178	the O-GlcNAcylated protein host cell factor C1	133:178	Electron transfer dissociation (ETD): the mass spectrometric breakthrough essential for O-GlcNAc protein site assignments-a study of the O-GlcNAcylated protein host cell factor C1.
23335398	1	61	theme	site	394:397	arg1	assignment					399:408	labile PTM site assignment	383:408	labile PTM site assignment	383:408	The development of electron-based, unimolecular dissociation MS, i.e. electron capture and electron transfer dissociation (ECD and ETD, respectively), has greatly increased the speed and reliability of labile PTM site assignment.
23335398	1	62	dep	electron-based	200:213	arg1	unimolecular					216:227	unimolecular	216:227	unimolecular	216:227	The development of electron-based, unimolecular dissociation MS, i.e. electron capture and electron transfer dissociation (ECD and ETD, respectively), has greatly increased the speed and reliability of labile PTM site assignment.
23335398	5	63	with	complex	1158:1164	arg1	transferase					1180:1190	O-GlcNAc transferase	1171:1190	O-GlcNAc transferase	1171:1190	HCF-1 is a transcriptional coregulator that forms a stable complex with O-GlcNAc transferase and controls cell cycle progression.
23335398	4	64	theme	Factor	1080:1085	arg1	C1					1087:1088	the extensively O-GlcNAcylated protein Host Cell Factor C1	1031:1088	the extensively O-GlcNAcylated protein Host Cell Factor C1 (HCF-1)	1031:1096	Here, we discuss the advantages of using ETD, complimented with collisional-activation MS, in a study of the extensively O-GlcNAcylated protein Host Cell Factor C1 (HCF-1).
23335398	4	64	theme	Factor	1080:1085	arg1	HCF-1					1091:1095	HCF-1	1091:1095	HCF-1	1091:1095	Here, we discuss the advantages of using ETD, complimented with collisional-activation MS, in a study of the extensively O-GlcNAcylated protein Host Cell Factor C1 (HCF-1).
23335398	7	65	theme	cell	1560:1563	arg1	proliferation					1565:1577	cell proliferation	1560:1577	cell proliferation	1560:1577	These include 19 sites of O-GlcNAcylation, two sites of phosphorylation, and two sites bearing dimethylarginine, and showcase the residue-specific, PTM complexity of this regulator of cell proliferation.
23335398	0	66	theme	host	160:163	arg1	C1					177:178	the O-GlcNAcylated protein host cell factor C1	133:178	the O-GlcNAcylated protein host cell factor C1	133:178	Electron transfer dissociation (ETD): the mass spectrometric breakthrough essential for O-GlcNAc protein site assignments-a study of the O-GlcNAcylated protein host cell factor C1.
23335398	1	67	theme	assignment	399:408	arg1	reliability					368:378	reliability	368:378	reliability	368:378	The development of electron-based, unimolecular dissociation MS, i.e. electron capture and electron transfer dissociation (ECD and ETD, respectively), has greatly increased the speed and reliability of labile PTM site assignment.
23335398	1	67	theme	assignment	399:408	arg1	speed					358:362	speed	358:362	speed	358:362	The development of electron-based, unimolecular dissociation MS, i.e. electron capture and electron transfer dissociation (ECD and ETD, respectively), has greatly increased the speed and reliability of labile PTM site assignment.
23335398	0	68	dep	dissociation	18:29	arg1	breakthrough					61:72	the mass spectrometric breakthrough	38:72	Electron transfer dissociation (ETD): the mass spectrometric breakthrough essential for O-GlcNAc protein site assignments-a study of the O-GlcNAcylated protein host cell factor C1.	0:179	Electron transfer dissociation (ETD): the mass spectrometric breakthrough essential for O-GlcNAc protein site assignments-a study of the O-GlcNAcylated protein host cell factor C1.
23335398	1	69	theme	dissociation	229:240	arg1	MS					242:243	electron-based, unimolecular dissociation MS	200:243	electron-based, unimolecular dissociation MS	200:243	The development of electron-based, unimolecular dissociation MS, i.e. electron capture and electron transfer dissociation (ECD and ETD, respectively), has greatly increased the speed and reliability of labile PTM site assignment.
23335398	0	70	theme	spectrometric	47:59	arg1	breakthrough					61:72	the mass spectrometric breakthrough	38:72	Electron transfer dissociation (ETD): the mass spectrometric breakthrough essential for O-GlcNAc protein site assignments-a study of the O-GlcNAcylated protein host cell factor C1.	0:179	Electron transfer dissociation (ETD): the mass spectrometric breakthrough essential for O-GlcNAc protein site assignments-a study of the O-GlcNAcylated protein host cell factor C1.
23335398	4	71	theme	Host	1070:1073	arg1	C1					1087:1088	the extensively O-GlcNAcylated protein Host Cell Factor C1	1031:1088	the extensively O-GlcNAcylated protein Host Cell Factor C1 (HCF-1)	1031:1096	Here, we discuss the advantages of using ETD, complimented with collisional-activation MS, in a study of the extensively O-GlcNAcylated protein Host Cell Factor C1 (HCF-1).
23335398	4	71	theme	Host	1070:1073	arg1	HCF-1					1091:1095	HCF-1	1091:1095	HCF-1	1091:1095	Here, we discuss the advantages of using ETD, complimented with collisional-activation MS, in a study of the extensively O-GlcNAcylated protein Host Cell Factor C1 (HCF-1).
23335398	6	72	theme	HEK293T	1361:1367	arg1	cells					1369:1373	HEK293T cells	1361:1373	HEK293T cells	1361:1373	ETD, along with higher energy collisional dissociation (HCD) MS, was employed to assign the PTMs of the HCF-1 protein isolated from HEK293T cells.
23335398	3	73	theme	regulatory	854:863	arg1	glycosylation					865:877	this regulatory glycosylation	849:877	this regulatory glycosylation	849:877	Our ability to identify and unambiguously assign the site of O-GlcNAc modifications using ETD is rapidly increasing our understanding of this regulatory glycosylation and its potential interaction with other PTMs.
23335398	1	74	theme	MS	242:243	arg1	development					185:195	The development	181:195	The development	181:195	The development of electron-based, unimolecular dissociation MS, i.e. electron capture and electron transfer dissociation (ECD and ETD, respectively), has greatly increased the speed and reliability of labile PTM site assignment.
23335398	0	75	theme	mass	42:45	arg1	breakthrough					61:72	the mass spectrometric breakthrough	38:72	Electron transfer dissociation (ETD): the mass spectrometric breakthrough essential for O-GlcNAc protein site assignments-a study of the O-GlcNAcylated protein host cell factor C1.	0:179	Electron transfer dissociation (ETD): the mass spectrometric breakthrough essential for O-GlcNAc protein site assignments-a study of the O-GlcNAcylated protein host cell factor C1.
23335398	4	76	theme	collisional-activation	990:1011	arg1	MS					1013:1014	collisional-activation MS	990:1014	collisional-activation MS	990:1014	Here, we discuss the advantages of using ETD, complimented with collisional-activation MS, in a study of the extensively O-GlcNAcylated protein Host Cell Factor C1 (HCF-1).
23335398	6	77	attach	isolated	1347:1354	arg2	protein					1339:1345	the HCF-1 protein	1329:1345	the HCF-1 protein isolated from HEK293T cells	1329:1373	ETD, along with higher energy collisional dissociation (HCD) MS, was employed to assign the PTMs of the HCF-1 protein isolated from HEK293T cells.
23335398	6	77	attach	isolated	1347:1354	arg1	cells					1369:1373	HEK293T cells	1361:1373	HEK293T cells	1361:1373	ETD, along with higher energy collisional dissociation (HCD) MS, was employed to assign the PTMs of the HCF-1 protein isolated from HEK293T cells.
23335398	2	78	theme	intracellular	424:436	arg1	signaling					478:486	intracellular O-GlcNAc (O-linked N-acetylglucosamine) signaling	424:486	intracellular O-GlcNAc (O-linked N-acetylglucosamine) signaling	424:486	The field of intracellular O-GlcNAc (O-linked N-acetylglucosamine) signaling has especially advanced with the advent of ETD MS. Only within the last five years have proteomic-scale experiments utilizing ETD allowed the assignment of hundreds of O-GlcNAc sites within cells and subcellular structures.
23335398	4	79	theme	protein	1062:1068	arg1	C1					1087:1088	the extensively O-GlcNAcylated protein Host Cell Factor C1	1031:1088	the extensively O-GlcNAcylated protein Host Cell Factor C1 (HCF-1)	1031:1096	Here, we discuss the advantages of using ETD, complimented with collisional-activation MS, in a study of the extensively O-GlcNAcylated protein Host Cell Factor C1 (HCF-1).
23335398	4	79	theme	protein	1062:1068	arg1	HCF-1					1091:1095	HCF-1	1091:1095	HCF-1	1091:1095	Here, we discuss the advantages of using ETD, complimented with collisional-activation MS, in a study of the extensively O-GlcNAcylated protein Host Cell Factor C1 (HCF-1).
23335398	3	80	theme	modifications	782:794	arg1	site					765:768	the site	761:768	the site of O-GlcNAc modifications using ETD	761:804	Our ability to identify and unambiguously assign the site of O-GlcNAc modifications using ETD is rapidly increasing our understanding of this regulatory glycosylation and its potential interaction with other PTMs.
23335398	3	80	theme	modifications	782:794	arg1	modifications					782:794	O-GlcNAc modifications	773:794	O-GlcNAc modifications using ETD	773:804	Our ability to identify and unambiguously assign the site of O-GlcNAc modifications using ETD is rapidly increasing our understanding of this regulatory glycosylation and its potential interaction with other PTMs.
15009203	14	0	located	found	2201:2205	arg1	spectra					2220:2226	the MALDI spectra	2210:2226	the MALDI spectra of the desialylated glycoproteins	2210:2260	The major difference between both preparations was found in the MALDI spectra of the desialylated glycoproteins, revealing a higher proportion of forms with a single N-glycosylation site occupied in the preparation derived from suspension culture.
15009203	14	0	located	found	2201:2205	arg2	difference					2160:2169	The major difference	2150:2169	The major difference between both preparations	2150:2195	The major difference between both preparations was found in the MALDI spectra of the desialylated glycoproteins, revealing a higher proportion of forms with a single N-glycosylation site occupied in the preparation derived from suspension culture.
15009203	13	1	from	molecules	2101:2109	arg1	O-glycosylated					2134:2147	O-glycosylated	2134:2147	O-glycosylated	2134:2147	In the triply modified GM-CSF molecules, Ser5 was additionally O-glycosylated.
15009203	10	2	dep	found	1671:1675	arg1	sialylated					1686:1695	sialylated	1686:1695	sialylated with NeuNAc (93%) or NeuNGc (7%)	1686:1728	More than 90% of terminal galactose residues of the N-glycans were found alpha2-3 sialylated with NeuNAc (93%) or NeuNGc (7%).
15009203	3	3	theme	ovary	524:528	arg1	line					535:538	an engineered Chinese hamster ovary cell line	494:538	an engineered Chinese hamster ovary cell line	494:538	The purpose of this work was to characterize the recombinant human GM-CSF from an engineered Chinese hamster ovary cell line grown in suspension and as adherent culture for the identification of the glycosylation sites and the definition of the glycosidic moiety, including the degree of site occupancy.
15009203	0	4	link	O-linked	7:14	arg1	carbohydrates					16:28	O-linked carbohydrates	7:28	O-linked carbohydrates	7:28	N- and O-linked carbohydrates and glycosylation site occupancy in recombinant human granulocyte-macrophage colony-stimulating factor secreted by a Chinese hamster ovary cell line.
15009203	10	5	theme	galactose	1630:1638	arg1	N-glycans					1656:1664	the N-glycans	1652:1664	the N-glycans	1652:1664	More than 90% of terminal galactose residues of the N-glycans were found alpha2-3 sialylated with NeuNAc (93%) or NeuNGc (7%).
15009203	10	5	theme	galactose	1630:1638	arg1	residues					1640:1647	terminal galactose residues	1621:1647	terminal galactose residues of the N-glycans	1621:1664	More than 90% of terminal galactose residues of the N-glycans were found alpha2-3 sialylated with NeuNAc (93%) or NeuNGc (7%).
15009203	7	6	theme	365	1150:1152	arg1	units					1136:1140	Hex-HexNAc units	1125:1140	Hex-HexNAc units (Deltam 365 Da)	1125:1156	At least 16 glycoforms, differing in the number of Hex-HexNAc units (Deltam 365 Da), were detected in MALDI-TOF MS spectra of the desialylated GM-CSFs.
15009203	7	6	theme	365	1150:1152	arg1	Da					1154:1155	Deltam 365 Da	1143:1155	Deltam 365 Da	1143:1155	At least 16 glycoforms, differing in the number of Hex-HexNAc units (Deltam 365 Da), were detected in MALDI-TOF MS spectra of the desialylated GM-CSFs.
15009203	5	7	theme	molecular	893:901	arg1	forms					908:912	Minor low molecular mass forms	883:912	Minor low molecular mass forms	883:912	Minor low molecular mass forms completely lacked N-linked oligosaccharides but contained 1-3 O-linked glycans.
15009203	10	8	theme	N-glycans	1656:1664	arg1	N-glycans					1656:1664	the N-glycans	1652:1664	the N-glycans	1652:1664	More than 90% of terminal galactose residues of the N-glycans were found alpha2-3 sialylated with NeuNAc (93%) or NeuNGc (7%).
15009203	10	8	theme	N-glycans	1656:1664	arg1	residues					1640:1647	terminal galactose residues	1621:1647	terminal galactose residues of the N-glycans	1621:1664	More than 90% of terminal galactose residues of the N-glycans were found alpha2-3 sialylated with NeuNAc (93%) or NeuNGc (7%).
15009203	1	9	gly	glycoproteins	225:237	arg1	glycoproteins					225:237	several naturally occurring glycoproteins	197:237	several naturally occurring glycoproteins that regulate leukocyte production, migration and function	197:296	GM-CSF is one of several naturally occurring glycoproteins that regulate leukocyte production, migration and function.
15009203	2	10	theme	cell	333:336	arg1	types					338:342	different cell types	323:342	different cell types	323:342	It has been produced in different cell types, with different properties that depend on the production process used.
15009203	1	11	theme	several	197:203	arg1	glycoproteins					225:237	several naturally occurring glycoproteins	197:237	several naturally occurring glycoproteins that regulate leukocyte production, migration and function	197:296	GM-CSF is one of several naturally occurring glycoproteins that regulate leukocyte production, migration and function.
15009203	7	12	theme	Hex-HexNAc	1125:1134	arg1	units					1136:1140	Hex-HexNAc units	1125:1140	Hex-HexNAc units (Deltam 365 Da)	1125:1156	At least 16 glycoforms, differing in the number of Hex-HexNAc units (Deltam 365 Da), were detected in MALDI-TOF MS spectra of the desialylated GM-CSFs.
15009203	7	12	theme	Hex-HexNAc	1125:1134	arg1	Da					1154:1155	Deltam 365 Da	1143:1155	Deltam 365 Da	1143:1155	At least 16 glycoforms, differing in the number of Hex-HexNAc units (Deltam 365 Da), were detected in MALDI-TOF MS spectra of the desialylated GM-CSFs.
15009203	3	13	theme	adherent	567:574	arg1	culture					576:582	adherent culture	567:582	adherent culture for the identification of the glycosylation sites and the definition of the glycosidic moiety	567:676	The purpose of this work was to characterize the recombinant human GM-CSF from an engineered Chinese hamster ovary cell line grown in suspension and as adherent culture for the identification of the glycosylation sites and the definition of the glycosidic moiety, including the degree of site occupancy.
15009203	1	14	theme	occurring	215:223	arg1	glycoproteins					225:237	several naturally occurring glycoproteins	197:237	several naturally occurring glycoproteins that regulate leukocyte production, migration and function	197:296	GM-CSF is one of several naturally occurring glycoproteins that regulate leukocyte production, migration and function.
15009203	8	15	theme	HPAEC-PAD	1243:1251	arg1	analysis					1253:1260	MALDI-TOF MS and HPAEC-PAD analysis	1226:1260	analysis	1253:1260	MALDI-TOF MS and HPAEC-PAD analysis indicated the presence of predominantly tri- and tetraantennary N-linked oligosaccharide chains with and without N-acetyllactosamine repeat units and some 10% of biantennary oligosaccharides, all containing more than 90% proximal alpha1-6-linked fucose.
15009203	6	16	theme	charged	1013:1019	arg1	isoforms					1021:1028	Twelve differently charged isoforms	994:1028	Twelve differently charged isoforms	994:1028	Twelve differently charged isoforms were detected in isoelectric focusing gels.
15009203	8	17	theme	N-linked	1326:1333	arg1	all					1454:1456	all	1454:1456	all	1454:1456	MALDI-TOF MS and HPAEC-PAD analysis indicated the presence of predominantly tri- and tetraantennary N-linked oligosaccharide chains with and without N-acetyllactosamine repeat units and some 10% of biantennary oligosaccharides, all containing more than 90% proximal alpha1-6-linked fucose.
15009203	8	17	theme	N-linked	1326:1333	arg1	chains					1351:1356	predominantly tri- and tetraantennary N-linked oligosaccharide chains	1288:1356	predominantly tri- and tetraantennary N-linked oligosaccharide chains with and without N-acetyllactosamine repeat units	1288:1406	MALDI-TOF MS and HPAEC-PAD analysis indicated the presence of predominantly tri- and tetraantennary N-linked oligosaccharide chains with and without N-acetyllactosamine repeat units and some 10% of biantennary oligosaccharides, all containing more than 90% proximal alpha1-6-linked fucose.
15009203	11	18	theme	GM-CSF	1849:1854	arg1	form					1856:1859	the mono glycosylated GM-CSF form	1827:1859	the mono glycosylated GM-CSF form	1827:1859	Site specific glycosylation was analysed by electrospray ionization MS and it was found that in the mono glycosylated GM-CSF form more than 90% of the Asn37 were occupied by N-glycans.
15009203	0	19	theme	hamster	155:161	arg1	line					174:177	a Chinese hamster ovary cell line	145:177	a Chinese hamster ovary cell line	145:177	N- and O-linked carbohydrates and glycosylation site occupancy in recombinant human granulocyte-macrophage colony-stimulating factor secreted by a Chinese hamster ovary cell line.
15009203	13	20	gly	O-glycosylated	2134:2147	arg1	Ser5					2112:2115	Ser5	2112:2115	Ser5	2112:2115	In the triply modified GM-CSF molecules, Ser5 was additionally O-glycosylated.
15009203	13	20	gly	O-glycosylated	2134:2147	arg2	Ser5					2112:2115	Ser5	2112:2115	Ser5	2112:2115	In the triply modified GM-CSF molecules, Ser5 was additionally O-glycosylated.
15009203	13	20	gly	O-glycosylated	2134:2147	arg1	molecules					2101:2109	the triply modified GM-CSF molecules	2074:2109	the triply modified GM-CSF molecules	2074:2109	In the triply modified GM-CSF molecules, Ser5 was additionally O-glycosylated.
15009203	5	21	theme	Minor	883:887	arg1	forms					908:912	Minor low molecular mass forms	883:912	Minor low molecular mass forms	883:912	Minor low molecular mass forms completely lacked N-linked oligosaccharides but contained 1-3 O-linked glycans.
15009203	13	22	from	O-glycosylated	2134:2147	arg1	molecules					2101:2109	the triply modified GM-CSF molecules	2074:2109	the triply modified GM-CSF molecules	2074:2109	In the triply modified GM-CSF molecules, Ser5 was additionally O-glycosylated.
15009203	8	23	theme	chains	1351:1356	arg1	presence					1276:1283	the presence	1272:1283	the presence of predominantly tri- and tetraantennary N-linked oligosaccharide chains with and without N-acetyllactosamine repeat units and some 10% of biantennary oligosaccharides, all containing more than 90% proximal alpha1-6-linked fucose	1272:1513	MALDI-TOF MS and HPAEC-PAD analysis indicated the presence of predominantly tri- and tetraantennary N-linked oligosaccharide chains with and without N-acetyllactosamine repeat units and some 10% of biantennary oligosaccharides, all containing more than 90% proximal alpha1-6-linked fucose.
15009203	0	24	theme	cell	169:172	arg1	line					174:177	a Chinese hamster ovary cell line	145:177	a Chinese hamster ovary cell line	145:177	N- and O-linked carbohydrates and glycosylation site occupancy in recombinant human granulocyte-macrophage colony-stimulating factor secreted by a Chinese hamster ovary cell line.
15009203	13	25	theme	GM-CSF	2094:2099	arg1	molecules					2101:2109	the triply modified GM-CSF molecules	2074:2109	the triply modified GM-CSF molecules	2074:2109	In the triply modified GM-CSF molecules, Ser5 was additionally O-glycosylated.
15009203	15	26	theme	intact	2498:2503	arg1	glycoprotein					2505:2516	the intact glycoprotein	2494:2516	the intact glycoprotein	2494:2516	ESI-MS and MALDI-MS analysis of endoproteolytically cleaved peptides as well as MALDI-TOF MS of the intact glycoprotein demonstrated the N- and C-termini integrity of the GM-CSF preparations.
15009203	11	27	theme	electrospray	1775:1786	arg1	MS					1799:1800	electrospray ionization MS	1775:1800	electrospray ionization MS	1775:1800	Site specific glycosylation was analysed by electrospray ionization MS and it was found that in the mono glycosylated GM-CSF form more than 90% of the Asn37 were occupied by N-glycans.
15009203	5	28	theme	O-linked	976:983	arg1	glycans					985:991	1-3 O-linked glycans	972:991	1-3 O-linked glycans	972:991	Minor low molecular mass forms completely lacked N-linked oligosaccharides but contained 1-3 O-linked glycans.
15009203	8	29	dep	%	1481:1481	arg1	90					1479:1480	90	1479:1480	90	1479:1480	MALDI-TOF MS and HPAEC-PAD analysis indicated the presence of predominantly tri- and tetraantennary N-linked oligosaccharide chains with and without N-acetyllactosamine repeat units and some 10% of biantennary oligosaccharides, all containing more than 90% proximal alpha1-6-linked fucose.
15009203	8	30	theme	N-acetyllactosamine	1375:1393	arg1	units					1402:1406	N-acetyllactosamine repeat units	1375:1406	N-acetyllactosamine repeat units	1375:1406	MALDI-TOF MS and HPAEC-PAD analysis indicated the presence of predominantly tri- and tetraantennary N-linked oligosaccharide chains with and without N-acetyllactosamine repeat units and some 10% of biantennary oligosaccharides, all containing more than 90% proximal alpha1-6-linked fucose.
15009203	0	31	theme	O-linked	7:14	arg1	carbohydrates					16:28	O-linked carbohydrates	7:28	O-linked carbohydrates	7:28	N- and O-linked carbohydrates and glycosylation site occupancy in recombinant human granulocyte-macrophage colony-stimulating factor secreted by a Chinese hamster ovary cell line.
15009203	15	32	theme	MALDI-TOF	2478:2486	arg1	MS					2488:2489	MALDI-TOF MS	2478:2489	ESI-MS and MALDI-MS analysis of endoproteolytically cleaved peptides as well as MALDI-TOF MS of the intact glycoprotein	2398:2516	ESI-MS and MALDI-MS analysis of endoproteolytically cleaved peptides as well as MALDI-TOF MS of the intact glycoprotein demonstrated the N- and C-termini integrity of the GM-CSF preparations.
15009203	14	33	gly	N-glycosylation	2316:2330	arg2	site					2332:2335	a single N-glycosylation site	2307:2335	a single N-glycosylation site occupied in the preparation derived from suspension culture	2307:2395	The major difference between both preparations was found in the MALDI spectra of the desialylated glycoproteins, revealing a higher proportion of forms with a single N-glycosylation site occupied in the preparation derived from suspension culture.
15009203	14	34	theme	MALDI	2214:2218	arg1	spectra					2220:2226	the MALDI spectra	2210:2226	the MALDI spectra of the desialylated glycoproteins	2210:2260	The major difference between both preparations was found in the MALDI spectra of the desialylated glycoproteins, revealing a higher proportion of forms with a single N-glycosylation site occupied in the preparation derived from suspension culture.
15009203	13	35	theme	modified	2085:2092	arg1	molecules					2101:2109	the triply modified GM-CSF molecules	2074:2109	the triply modified GM-CSF molecules	2074:2109	In the triply modified GM-CSF molecules, Ser5 was additionally O-glycosylated.
15009203	14	36	theme	N-glycosylation	2316:2330	arg1	site					2332:2335	a single N-glycosylation site	2307:2335	a single N-glycosylation site occupied in the preparation derived from suspension culture	2307:2395	The major difference between both preparations was found in the MALDI spectra of the desialylated glycoproteins, revealing a higher proportion of forms with a single N-glycosylation site occupied in the preparation derived from suspension culture.
15009203	0	37	theme	human	78:82	arg1	factor					126:131	granulocyte-macrophage colony-stimulating factor	84:131	recombinant human granulocyte-macrophage colony-stimulating factor	66:131	N- and O-linked carbohydrates and glycosylation site occupancy in recombinant human granulocyte-macrophage colony-stimulating factor secreted by a Chinese hamster ovary cell line.
15009203	15	38	theme	peptides	2458:2465	arg1	analysis					2418:2425	ESI-MS and MALDI-MS analysis	2398:2425	ESI-MS and MALDI-MS analysis of endoproteolytically cleaved peptides as well as MALDI-TOF MS of the intact glycoprotein	2398:2516	ESI-MS and MALDI-MS analysis of endoproteolytically cleaved peptides as well as MALDI-TOF MS of the intact glycoprotein demonstrated the N- and C-termini integrity of the GM-CSF preparations.
15009203	15	38	theme	peptides	2458:2465	arg1	MS					2488:2489	MALDI-TOF MS	2478:2489	ESI-MS and MALDI-MS analysis of endoproteolytically cleaved peptides as well as MALDI-TOF MS of the intact glycoprotein	2398:2516	ESI-MS and MALDI-MS analysis of endoproteolytically cleaved peptides as well as MALDI-TOF MS of the intact glycoprotein demonstrated the N- and C-termini integrity of the GM-CSF preparations.
15009203	15	39	theme	GM-CSF	2569:2574	arg1	preparations					2576:2587	the GM-CSF preparations	2565:2587	the GM-CSF preparations	2565:2587	ESI-MS and MALDI-MS analysis of endoproteolytically cleaved peptides as well as MALDI-TOF MS of the intact glycoprotein demonstrated the N- and C-termini integrity of the GM-CSF preparations.
15009203	6	40	theme	focusing	1059:1066	arg1	gels					1068:1071	isoelectric focusing gels	1047:1071	isoelectric focusing gels	1047:1071	Twelve differently charged isoforms were detected in isoelectric focusing gels.
15009203	0	41	from	N-	0:1	arg1	factor					126:131	granulocyte-macrophage colony-stimulating factor	84:131	recombinant human granulocyte-macrophage colony-stimulating factor	66:131	N- and O-linked carbohydrates and glycosylation site occupancy in recombinant human granulocyte-macrophage colony-stimulating factor secreted by a Chinese hamster ovary cell line.
15009203	4	42	theme	multiple	783:790	arg1	bands					792:796	multiple bands	783:796	multiple bands containing glycoprotein forms with either two or one N-glycosylation sites occupied	783:880	Both preparations exhibited size heterogeneity in SDS/PAGE with multiple bands containing glycoprotein forms with either two or one N-glycosylation sites occupied.
15009203	0	43	theme	colony-stimulating	107:124	arg1	factor					126:131	granulocyte-macrophage colony-stimulating factor	84:131	recombinant human granulocyte-macrophage colony-stimulating factor	66:131	N- and O-linked carbohydrates and glycosylation site occupancy in recombinant human granulocyte-macrophage colony-stimulating factor secreted by a Chinese hamster ovary cell line.
15009203	12	44	gly	O-glycosylated	2037:2050	arg1	form					2065:2068	the predominantly doubly O-glycosylated glycoprotein form	2012:2068	the predominantly doubly O-glycosylated glycoprotein form	2012:2068	O-glycosylation at the N-terminus of the polypeptide was detected at Ser7 and Ser9 or Thr10, in the predominantly doubly O-glycosylated glycoprotein form.
15009203	8	45	theme	%	1419:1419	arg1	presence					1276:1283	the presence	1272:1283	the presence of predominantly tri- and tetraantennary N-linked oligosaccharide chains with and without N-acetyllactosamine repeat units and some 10% of biantennary oligosaccharides, all containing more than 90% proximal alpha1-6-linked fucose	1272:1513	MALDI-TOF MS and HPAEC-PAD analysis indicated the presence of predominantly tri- and tetraantennary N-linked oligosaccharide chains with and without N-acetyllactosamine repeat units and some 10% of biantennary oligosaccharides, all containing more than 90% proximal alpha1-6-linked fucose.
15009203	14	46	theme	forms	2296:2300	arg1	proportion					2282:2291	a higher proportion	2273:2291	a higher proportion of forms with a single N-glycosylation site occupied in the preparation derived from suspension culture	2273:2395	The major difference between both preparations was found in the MALDI spectra of the desialylated glycoproteins, revealing a higher proportion of forms with a single N-glycosylation site occupied in the preparation derived from suspension culture.
15009203	4	47	gly	glycoprotein	809:820	arg1	glycoprotein					809:820	glycoprotein forms	809:826	glycoprotein forms	809:826	Both preparations exhibited size heterogeneity in SDS/PAGE with multiple bands containing glycoprotein forms with either two or one N-glycosylation sites occupied.
15009203	8	48	theme	biantennary	1424:1434	arg1	oligosaccharides					1436:1451	biantennary oligosaccharides	1424:1451	biantennary oligosaccharides	1424:1451	MALDI-TOF MS and HPAEC-PAD analysis indicated the presence of predominantly tri- and tetraantennary N-linked oligosaccharide chains with and without N-acetyllactosamine repeat units and some 10% of biantennary oligosaccharides, all containing more than 90% proximal alpha1-6-linked fucose.
15009203	3	49	theme	work	435:438	arg1	purpose					419:425	The purpose	415:425	The purpose of this work	415:438	The purpose of this work was to characterize the recombinant human GM-CSF from an engineered Chinese hamster ovary cell line grown in suspension and as adherent culture for the identification of the glycosylation sites and the definition of the glycosidic moiety, including the degree of site occupancy.
15009203	7	50	theme	desialylated	1204:1215	arg1	GM-CSFs					1217:1223	the desialylated GM-CSFs	1200:1223	the desialylated GM-CSFs	1200:1223	At least 16 glycoforms, differing in the number of Hex-HexNAc units (Deltam 365 Da), were detected in MALDI-TOF MS spectra of the desialylated GM-CSFs.
15009203	4	51	from	heterogeneity	752:764	arg1	SDS/PAGE					769:776	SDS/PAGE	769:776	SDS/PAGE	769:776	Both preparations exhibited size heterogeneity in SDS/PAGE with multiple bands containing glycoprotein forms with either two or one N-glycosylation sites occupied.
15009203	3	52	theme	human	476:480	arg1	GM-CSF					482:487	the recombinant human GM-CSF	460:487	the recombinant human GM-CSF	460:487	The purpose of this work was to characterize the recombinant human GM-CSF from an engineered Chinese hamster ovary cell line grown in suspension and as adherent culture for the identification of the glycosylation sites and the definition of the glycosidic moiety, including the degree of site occupancy.
15009203	4	53	gly	N-glycosylation	851:865	arg2	sites					867:871	either two or one N-glycosylation sites	833:871	either two or one N-glycosylation sites occupied	833:880	Both preparations exhibited size heterogeneity in SDS/PAGE with multiple bands containing glycoprotein forms with either two or one N-glycosylation sites occupied.
15009203	4	53	gly	N-glycosylation	851:865	arg2	one					847:849	one	847:849	one	847:849	Both preparations exhibited size heterogeneity in SDS/PAGE with multiple bands containing glycoprotein forms with either two or one N-glycosylation sites occupied.
15009203	4	53	gly	N-glycosylation	851:865	arg2	two					840:842	two	840:842	two	840:842	Both preparations exhibited size heterogeneity in SDS/PAGE with multiple bands containing glycoprotein forms with either two or one N-glycosylation sites occupied.
15009203	12	54	theme	glycoprotein	2052:2063	arg1	form					2065:2068	the predominantly doubly O-glycosylated glycoprotein form	2012:2068	the predominantly doubly O-glycosylated glycoprotein form	2012:2068	O-glycosylation at the N-terminus of the polypeptide was detected at Ser7 and Ser9 or Thr10, in the predominantly doubly O-glycosylated glycoprotein form.
15009203	3	55	theme	glycosidic	660:669	arg1	moiety					671:676	the glycosidic moiety	656:676	the glycosidic moiety	656:676	The purpose of this work was to characterize the recombinant human GM-CSF from an engineered Chinese hamster ovary cell line grown in suspension and as adherent culture for the identification of the glycosylation sites and the definition of the glycosidic moiety, including the degree of site occupancy.
15009203	12	56	located	detected	1973:1980	arg1	form					2065:2068	the predominantly doubly O-glycosylated glycoprotein form	2012:2068	the predominantly doubly O-glycosylated glycoprotein form	2012:2068	O-glycosylation at the N-terminus of the polypeptide was detected at Ser7 and Ser9 or Thr10, in the predominantly doubly O-glycosylated glycoprotein form.
15009203	12	56	located	detected	1973:1980	arg1	Thr10					2002:2006	Thr10	2002:2006	Thr10	2002:2006	O-glycosylation at the N-terminus of the polypeptide was detected at Ser7 and Ser9 or Thr10, in the predominantly doubly O-glycosylated glycoprotein form.
15009203	12	56	located	detected	1973:1980	arg1	Ser9					1994:1997	Ser9	1994:1997	Ser9	1994:1997	O-glycosylation at the N-terminus of the polypeptide was detected at Ser7 and Ser9 or Thr10, in the predominantly doubly O-glycosylated glycoprotein form.
15009203	12	56	located	detected	1973:1980	arg1	Ser7					1985:1988	Ser7	1985:1988	Ser7	1985:1988	O-glycosylation at the N-terminus of the polypeptide was detected at Ser7 and Ser9 or Thr10, in the predominantly doubly O-glycosylated glycoprotein form.
15009203	12	56	located	detected	1973:1980	arg2	O-glycosylation					1916:1930	O-glycosylation	1916:1930	O-glycosylation at the N-terminus of the polypeptide	1916:1967	O-glycosylation at the N-terminus of the polypeptide was detected at Ser7 and Ser9 or Thr10, in the predominantly doubly O-glycosylated glycoprotein form.
15009203	7	57	theme	MS	1186:1187	arg1	spectra					1189:1195	MALDI-TOF MS spectra	1176:1195	MALDI-TOF MS spectra of the desialylated GM-CSFs	1176:1223	At least 16 glycoforms, differing in the number of Hex-HexNAc units (Deltam 365 Da), were detected in MALDI-TOF MS spectra of the desialylated GM-CSFs.
15009203	4	58	theme	N-glycosylation	851:865	arg1	sites					867:871	either two or one N-glycosylation sites	833:871	either two or one N-glycosylation sites occupied	833:880	Both preparations exhibited size heterogeneity in SDS/PAGE with multiple bands containing glycoprotein forms with either two or one N-glycosylation sites occupied.
15009203	3	59	theme	engineered	497:506	arg1	line					535:538	an engineered Chinese hamster ovary cell line	494:538	an engineered Chinese hamster ovary cell line	494:538	The purpose of this work was to characterize the recombinant human GM-CSF from an engineered Chinese hamster ovary cell line grown in suspension and as adherent culture for the identification of the glycosylation sites and the definition of the glycosidic moiety, including the degree of site occupancy.
15009203	0	60	theme	site	48:51	arg1	occupancy					53:61	glycosylation site occupancy	34:61	glycosylation site occupancy	34:61	N- and O-linked carbohydrates and glycosylation site occupancy in recombinant human granulocyte-macrophage colony-stimulating factor secreted by a Chinese hamster ovary cell line.
15009203	5	61	link	O-linked	976:983	arg1	glycans					985:991	1-3 O-linked glycans	972:991	1-3 O-linked glycans	972:991	Minor low molecular mass forms completely lacked N-linked oligosaccharides but contained 1-3 O-linked glycans.
15009203	8	62	link	N-linked	1326:1333	arg1	all					1454:1456	all	1454:1456	all	1454:1456	MALDI-TOF MS and HPAEC-PAD analysis indicated the presence of predominantly tri- and tetraantennary N-linked oligosaccharide chains with and without N-acetyllactosamine repeat units and some 10% of biantennary oligosaccharides, all containing more than 90% proximal alpha1-6-linked fucose.
15009203	8	62	link	N-linked	1326:1333	arg1	chains					1351:1356	predominantly tri- and tetraantennary N-linked oligosaccharide chains	1288:1356	predominantly tri- and tetraantennary N-linked oligosaccharide chains with and without N-acetyllactosamine repeat units	1288:1406	MALDI-TOF MS and HPAEC-PAD analysis indicated the presence of predominantly tri- and tetraantennary N-linked oligosaccharide chains with and without N-acetyllactosamine repeat units and some 10% of biantennary oligosaccharides, all containing more than 90% proximal alpha1-6-linked fucose.
15009203	3	63	theme	sites	628:632	arg1	definition					642:651	the definition	638:651	the definition of the glycosidic moiety	638:676	The purpose of this work was to characterize the recombinant human GM-CSF from an engineered Chinese hamster ovary cell line grown in suspension and as adherent culture for the identification of the glycosylation sites and the definition of the glycosidic moiety, including the degree of site occupancy.
15009203	3	63	theme	sites	628:632	arg1	identification					592:605	the identification	588:605	the identification of the glycosylation sites	588:632	The purpose of this work was to characterize the recombinant human GM-CSF from an engineered Chinese hamster ovary cell line grown in suspension and as adherent culture for the identification of the glycosylation sites and the definition of the glycosidic moiety, including the degree of site occupancy.
15009203	7	64	gly	desialylated	1204:1215	arg1	GM-CSFs					1217:1223	the desialylated GM-CSFs	1200:1223	the desialylated GM-CSFs	1200:1223	At least 16 glycoforms, differing in the number of Hex-HexNAc units (Deltam 365 Da), were detected in MALDI-TOF MS spectra of the desialylated GM-CSFs.
15009203	0	65	gly	glycosylation	34:46	arg2	occupancy					53:61	glycosylation site occupancy	34:61	glycosylation site occupancy	34:61	N- and O-linked carbohydrates and glycosylation site occupancy in recombinant human granulocyte-macrophage colony-stimulating factor secreted by a Chinese hamster ovary cell line.
15009203	0	65	gly	glycosylation	34:46	arg2	site					48:51	glycosylation site occupancy	34:61	glycosylation site occupancy	34:61	N- and O-linked carbohydrates and glycosylation site occupancy in recombinant human granulocyte-macrophage colony-stimulating factor secreted by a Chinese hamster ovary cell line.
15009203	14	66	theme	glycoproteins	2248:2260	arg1	spectra					2220:2226	the MALDI spectra	2210:2226	the MALDI spectra of the desialylated glycoproteins	2210:2260	The major difference between both preparations was found in the MALDI spectra of the desialylated glycoproteins, revealing a higher proportion of forms with a single N-glycosylation site occupied in the preparation derived from suspension culture.
15009203	11	67	theme	specific	1736:1743	arg1	glycosylation					1745:1757	Site specific glycosylation	1731:1757	Site specific glycosylation	1731:1757	Site specific glycosylation was analysed by electrospray ionization MS and it was found that in the mono glycosylated GM-CSF form more than 90% of the Asn37 were occupied by N-glycans.
15009203	8	68	theme	alpha1-6-linked	1492:1506	arg1	fucose					1508:1513	more than 90% proximal alpha1-6-linked fucose	1469:1513	more than 90% proximal alpha1-6-linked fucose	1469:1513	MALDI-TOF MS and HPAEC-PAD analysis indicated the presence of predominantly tri- and tetraantennary N-linked oligosaccharide chains with and without N-acetyllactosamine repeat units and some 10% of biantennary oligosaccharides, all containing more than 90% proximal alpha1-6-linked fucose.
15009203	3	69	theme	cell	530:533	arg1	line					535:538	an engineered Chinese hamster ovary cell line	494:538	an engineered Chinese hamster ovary cell line	494:538	The purpose of this work was to characterize the recombinant human GM-CSF from an engineered Chinese hamster ovary cell line grown in suspension and as adherent culture for the identification of the glycosylation sites and the definition of the glycosidic moiety, including the degree of site occupancy.
15009203	14	70	gly	glycoproteins	2248:2260	arg1	glycoproteins					2248:2260	the desialylated glycoproteins	2231:2260	the desialylated glycoproteins	2231:2260	The major difference between both preparations was found in the MALDI spectra of the desialylated glycoproteins, revealing a higher proportion of forms with a single N-glycosylation site occupied in the preparation derived from suspension culture.
15009203	3	71	theme	occupancy	708:716	arg1	degree					693:698	the degree	689:698	the degree of site occupancy	689:716	The purpose of this work was to characterize the recombinant human GM-CSF from an engineered Chinese hamster ovary cell line grown in suspension and as adherent culture for the identification of the glycosylation sites and the definition of the glycosidic moiety, including the degree of site occupancy.
15009203	3	72	theme	hamster	516:522	arg1	line					535:538	an engineered Chinese hamster ovary cell line	494:538	an engineered Chinese hamster ovary cell line	494:538	The purpose of this work was to characterize the recombinant human GM-CSF from an engineered Chinese hamster ovary cell line grown in suspension and as adherent culture for the identification of the glycosylation sites and the definition of the glycosidic moiety, including the degree of site occupancy.
15009203	10	73	theme	residues	1640:1647	arg1	N-glycans					1656:1664	the N-glycans	1652:1664	the N-glycans	1652:1664	More than 90% of terminal galactose residues of the N-glycans were found alpha2-3 sialylated with NeuNAc (93%) or NeuNGc (7%).
15009203	10	73	theme	residues	1640:1647	arg1	%					1616:1616	More than 90%	1604:1616	More than 90% of terminal galactose residues of the N-glycans	1604:1664	More than 90% of terminal galactose residues of the N-glycans were found alpha2-3 sialylated with NeuNAc (93%) or NeuNGc (7%).
15009203	10	73	theme	residues	1640:1647	arg1	residues					1640:1647	terminal galactose residues	1621:1647	terminal galactose residues of the N-glycans	1621:1664	More than 90% of terminal galactose residues of the N-glycans were found alpha2-3 sialylated with NeuNAc (93%) or NeuNGc (7%).
15009203	11	74	gly	glycosylated	1836:1847	arg1	form					1856:1859	the mono glycosylated GM-CSF form	1827:1859	the mono glycosylated GM-CSF form	1827:1859	Site specific glycosylation was analysed by electrospray ionization MS and it was found that in the mono glycosylated GM-CSF form more than 90% of the Asn37 were occupied by N-glycans.
15009203	10	75	theme	terminal	1621:1628	arg1	N-glycans					1656:1664	the N-glycans	1652:1664	the N-glycans	1652:1664	More than 90% of terminal galactose residues of the N-glycans were found alpha2-3 sialylated with NeuNAc (93%) or NeuNGc (7%).
15009203	10	75	theme	terminal	1621:1628	arg1	residues					1640:1647	terminal galactose residues	1621:1647	terminal galactose residues of the N-glycans	1621:1664	More than 90% of terminal galactose residues of the N-glycans were found alpha2-3 sialylated with NeuNAc (93%) or NeuNGc (7%).
15009203	7	76	theme	Deltam	1143:1148	arg1	units					1136:1140	Hex-HexNAc units	1125:1140	Hex-HexNAc units (Deltam 365 Da)	1125:1156	At least 16 glycoforms, differing in the number of Hex-HexNAc units (Deltam 365 Da), were detected in MALDI-TOF MS spectra of the desialylated GM-CSFs.
15009203	7	76	theme	Deltam	1143:1148	arg1	Da					1154:1155	Deltam 365 Da	1143:1155	Deltam 365 Da	1143:1155	At least 16 glycoforms, differing in the number of Hex-HexNAc units (Deltam 365 Da), were detected in MALDI-TOF MS spectra of the desialylated GM-CSFs.
15009203	7	77	located	detected	1164:1171	arg2	glycoforms					1086:1095	At least 16 glycoforms	1074:1095	At least 16 glycoforms	1074:1095	At least 16 glycoforms, differing in the number of Hex-HexNAc units (Deltam 365 Da), were detected in MALDI-TOF MS spectra of the desialylated GM-CSFs.
15009203	7	77	located	detected	1164:1171	arg1	spectra					1189:1195	MALDI-TOF MS spectra	1176:1195	MALDI-TOF MS spectra of the desialylated GM-CSFs	1176:1223	At least 16 glycoforms, differing in the number of Hex-HexNAc units (Deltam 365 Da), were detected in MALDI-TOF MS spectra of the desialylated GM-CSFs.
15009203	5	78	theme	low	889:891	arg1	forms					908:912	Minor low molecular mass forms	883:912	Minor low molecular mass forms	883:912	Minor low molecular mass forms completely lacked N-linked oligosaccharides but contained 1-3 O-linked glycans.
15009203	14	79	with	proportion	2282:2291	arg1	site					2332:2335	a single N-glycosylation site	2307:2335	a single N-glycosylation site occupied in the preparation derived from suspension culture	2307:2395	The major difference between both preparations was found in the MALDI spectra of the desialylated glycoproteins, revealing a higher proportion of forms with a single N-glycosylation site occupied in the preparation derived from suspension culture.
15009203	7	80	theme	units	1136:1140	arg1	number					1115:1120	the number	1111:1120	the number of Hex-HexNAc units (Deltam 365 Da)	1111:1156	At least 16 glycoforms, differing in the number of Hex-HexNAc units (Deltam 365 Da), were detected in MALDI-TOF MS spectra of the desialylated GM-CSFs.
15009203	14	81	theme	suspension	2378:2387	arg1	culture					2389:2395	suspension culture	2378:2395	suspension culture	2378:2395	The major difference between both preparations was found in the MALDI spectra of the desialylated glycoproteins, revealing a higher proportion of forms with a single N-glycosylation site occupied in the preparation derived from suspension culture.
15009203	5	82	theme	mass	903:906	arg1	forms					908:912	Minor low molecular mass forms	883:912	Minor low molecular mass forms	883:912	Minor low molecular mass forms completely lacked N-linked oligosaccharides but contained 1-3 O-linked glycans.
15009203	3	83	gly	glycosylation	614:626	arg2	sites					628:632	the glycosylation sites	610:632	the glycosylation sites	610:632	The purpose of this work was to characterize the recombinant human GM-CSF from an engineered Chinese hamster ovary cell line grown in suspension and as adherent culture for the identification of the glycosylation sites and the definition of the glycosidic moiety, including the degree of site occupancy.
15009203	0	84	theme	Chinese	147:153	arg1	line					174:177	a Chinese hamster ovary cell line	145:177	a Chinese hamster ovary cell line	145:177	N- and O-linked carbohydrates and glycosylation site occupancy in recombinant human granulocyte-macrophage colony-stimulating factor secreted by a Chinese hamster ovary cell line.
15009203	2	85	theme	different	323:331	arg1	types					338:342	different cell types	323:342	different cell types	323:342	It has been produced in different cell types, with different properties that depend on the production process used.
15009203	8	86	theme	MALDI-TOF	1226:1234	arg1	MS					1236:1237	MALDI-TOF MS and HPAEC-PAD analysis	1226:1260	MS	1236:1237	MALDI-TOF MS and HPAEC-PAD analysis indicated the presence of predominantly tri- and tetraantennary N-linked oligosaccharide chains with and without N-acetyllactosamine repeat units and some 10% of biantennary oligosaccharides, all containing more than 90% proximal alpha1-6-linked fucose.
15009203	8	87	theme	tri-	1302:1305	arg1	all					1454:1456	all	1454:1456	all	1454:1456	MALDI-TOF MS and HPAEC-PAD analysis indicated the presence of predominantly tri- and tetraantennary N-linked oligosaccharide chains with and without N-acetyllactosamine repeat units and some 10% of biantennary oligosaccharides, all containing more than 90% proximal alpha1-6-linked fucose.
15009203	8	87	theme	tri-	1302:1305	arg1	chains					1351:1356	predominantly tri- and tetraantennary N-linked oligosaccharide chains	1288:1356	predominantly tri- and tetraantennary N-linked oligosaccharide chains with and without N-acetyllactosamine repeat units	1288:1406	MALDI-TOF MS and HPAEC-PAD analysis indicated the presence of predominantly tri- and tetraantennary N-linked oligosaccharide chains with and without N-acetyllactosamine repeat units and some 10% of biantennary oligosaccharides, all containing more than 90% proximal alpha1-6-linked fucose.
15009203	2	88	theme	different	350:358	arg1	properties					360:369	different properties	350:369	different properties that depend on the production process used	350:412	It has been produced in different cell types, with different properties that depend on the production process used.
15009203	0	89	theme	ovary	163:167	arg1	line					174:177	a Chinese hamster ovary cell line	145:177	a Chinese hamster ovary cell line	145:177	N- and O-linked carbohydrates and glycosylation site occupancy in recombinant human granulocyte-macrophage colony-stimulating factor secreted by a Chinese hamster ovary cell line.
15009203	15	90	theme	MALDI-MS	2409:2416	arg1	analysis					2418:2425	ESI-MS and MALDI-MS analysis	2398:2425	ESI-MS and MALDI-MS analysis of endoproteolytically cleaved peptides as well as MALDI-TOF MS of the intact glycoprotein	2398:2516	ESI-MS and MALDI-MS analysis of endoproteolytically cleaved peptides as well as MALDI-TOF MS of the intact glycoprotein demonstrated the N- and C-termini integrity of the GM-CSF preparations.
15009203	9	91	theme	oligosaccharide	1520:1534	arg1	similar					1595:1601	similar	1595:1601	similar	1595:1601	The oligosaccharide patterns of both GM-CSF preparations were found to be very similar.
15009203	9	91	theme	oligosaccharide	1520:1534	arg1	patterns					1536:1543	The oligosaccharide patterns	1516:1543	The oligosaccharide patterns of both GM-CSF preparations	1516:1571	The oligosaccharide patterns of both GM-CSF preparations were found to be very similar.
15009203	1	92	theme	glycoproteins	225:237	arg1	glycoproteins					225:237	several naturally occurring glycoproteins	197:237	several naturally occurring glycoproteins that regulate leukocyte production, migration and function	197:296	GM-CSF is one of several naturally occurring glycoproteins that regulate leukocyte production, migration and function.
15009203	1	92	theme	glycoproteins	225:237	arg1	one					190:192	one	190:192	one	190:192	GM-CSF is one of several naturally occurring glycoproteins that regulate leukocyte production, migration and function.
15009203	8	93	theme	tetraantennary	1311:1324	arg1	all					1454:1456	all	1454:1456	all	1454:1456	MALDI-TOF MS and HPAEC-PAD analysis indicated the presence of predominantly tri- and tetraantennary N-linked oligosaccharide chains with and without N-acetyllactosamine repeat units and some 10% of biantennary oligosaccharides, all containing more than 90% proximal alpha1-6-linked fucose.
15009203	8	93	theme	tetraantennary	1311:1324	arg1	chains					1351:1356	predominantly tri- and tetraantennary N-linked oligosaccharide chains	1288:1356	predominantly tri- and tetraantennary N-linked oligosaccharide chains with and without N-acetyllactosamine repeat units	1288:1406	MALDI-TOF MS and HPAEC-PAD analysis indicated the presence of predominantly tri- and tetraantennary N-linked oligosaccharide chains with and without N-acetyllactosamine repeat units and some 10% of biantennary oligosaccharides, all containing more than 90% proximal alpha1-6-linked fucose.
15009203	14	94	theme	major	2154:2158	arg1	difference					2160:2169	The major difference	2150:2169	The major difference between both preparations	2150:2195	The major difference between both preparations was found in the MALDI spectra of the desialylated glycoproteins, revealing a higher proportion of forms with a single N-glycosylation site occupied in the preparation derived from suspension culture.
15009203	4	95	contain	containing	798:807	arg1	bands					792:796	multiple bands	783:796	multiple bands containing glycoprotein forms with either two or one N-glycosylation sites occupied	783:880	Both preparations exhibited size heterogeneity in SDS/PAGE with multiple bands containing glycoprotein forms with either two or one N-glycosylation sites occupied.
15009203	4	95	contain	containing	798:807	arg2	forms					822:826	glycoprotein forms	809:826	glycoprotein forms	809:826	Both preparations exhibited size heterogeneity in SDS/PAGE with multiple bands containing glycoprotein forms with either two or one N-glycosylation sites occupied.
15009203	15	96	theme	ESI-MS	2398:2403	arg1	analysis					2418:2425	ESI-MS and MALDI-MS analysis	2398:2425	ESI-MS and MALDI-MS analysis of endoproteolytically cleaved peptides as well as MALDI-TOF MS of the intact glycoprotein	2398:2516	ESI-MS and MALDI-MS analysis of endoproteolytically cleaved peptides as well as MALDI-TOF MS of the intact glycoprotein demonstrated the N- and C-termini integrity of the GM-CSF preparations.
15009203	9	97	theme	preparations	1560:1571	arg1	similar					1595:1601	similar	1595:1601	similar	1595:1601	The oligosaccharide patterns of both GM-CSF preparations were found to be very similar.
15009203	9	97	theme	preparations	1560:1571	arg1	patterns					1536:1543	The oligosaccharide patterns	1516:1543	The oligosaccharide patterns of both GM-CSF preparations	1516:1571	The oligosaccharide patterns of both GM-CSF preparations were found to be very similar.
15009203	12	98	theme	polypeptide	1957:1967	arg1	N-terminus					1939:1948	the N-terminus	1935:1948	the N-terminus of the polypeptide	1935:1967	O-glycosylation at the N-terminus of the polypeptide was detected at Ser7 and Ser9 or Thr10, in the predominantly doubly O-glycosylated glycoprotein form.
15009203	5	99	contain	contained	962:970	arg2	glycans					985:991	1-3 O-linked glycans	972:991	1-3 O-linked glycans	972:991	Minor low molecular mass forms completely lacked N-linked oligosaccharides but contained 1-3 O-linked glycans.
15009203	5	99	contain	contained	962:970	arg1	forms					908:912	Minor low molecular mass forms	883:912	Minor low molecular mass forms	883:912	Minor low molecular mass forms completely lacked N-linked oligosaccharides but contained 1-3 O-linked glycans.
15009203	8	100	theme	oligosaccharide	1335:1349	arg1	all					1454:1456	all	1454:1456	all	1454:1456	MALDI-TOF MS and HPAEC-PAD analysis indicated the presence of predominantly tri- and tetraantennary N-linked oligosaccharide chains with and without N-acetyllactosamine repeat units and some 10% of biantennary oligosaccharides, all containing more than 90% proximal alpha1-6-linked fucose.
15009203	8	100	theme	oligosaccharide	1335:1349	arg1	chains					1351:1356	predominantly tri- and tetraantennary N-linked oligosaccharide chains	1288:1356	predominantly tri- and tetraantennary N-linked oligosaccharide chains with and without N-acetyllactosamine repeat units	1288:1406	MALDI-TOF MS and HPAEC-PAD analysis indicated the presence of predominantly tri- and tetraantennary N-linked oligosaccharide chains with and without N-acetyllactosamine repeat units and some 10% of biantennary oligosaccharides, all containing more than 90% proximal alpha1-6-linked fucose.
15009203	12	101	gly	O-glycosylation	1916:1930	arg1	Thr10					2002:2006	Thr10	2002:2006	Thr10	2002:2006	O-glycosylation at the N-terminus of the polypeptide was detected at Ser7 and Ser9 or Thr10, in the predominantly doubly O-glycosylated glycoprotein form.
15009203	12	101	gly	O-glycosylation	1916:1930	arg1	N-terminus					1939:1948	the N-terminus	1935:1948	the N-terminus of the polypeptide	1935:1967	O-glycosylation at the N-terminus of the polypeptide was detected at Ser7 and Ser9 or Thr10, in the predominantly doubly O-glycosylated glycoprotein form.
15009203	12	101	gly	O-glycosylation	1916:1930	arg1	form					2065:2068	the predominantly doubly O-glycosylated glycoprotein form	2012:2068	the predominantly doubly O-glycosylated glycoprotein form	2012:2068	O-glycosylation at the N-terminus of the polypeptide was detected at Ser7 and Ser9 or Thr10, in the predominantly doubly O-glycosylated glycoprotein form.
15009203	12	101	gly	O-glycosylation	1916:1930	arg1	Ser7					1985:1988	Ser7	1985:1988	Ser7	1985:1988	O-glycosylation at the N-terminus of the polypeptide was detected at Ser7 and Ser9 or Thr10, in the predominantly doubly O-glycosylated glycoprotein form.
15009203	12	101	gly	O-glycosylation	1916:1930	arg2	N-terminus					1939:1948	the N-terminus	1935:1948	the N-terminus of the polypeptide	1935:1967	O-glycosylation at the N-terminus of the polypeptide was detected at Ser7 and Ser9 or Thr10, in the predominantly doubly O-glycosylated glycoprotein form.
15009203	12	101	gly	O-glycosylation	1916:1930	arg1	Ser9					1994:1997	Ser9	1994:1997	Ser9	1994:1997	O-glycosylation at the N-terminus of the polypeptide was detected at Ser7 and Ser9 or Thr10, in the predominantly doubly O-glycosylated glycoprotein form.
15009203	11	102	theme	glycosylated	1836:1847	arg1	form					1856:1859	the mono glycosylated GM-CSF form	1827:1859	the mono glycosylated GM-CSF form	1827:1859	Site specific glycosylation was analysed by electrospray ionization MS and it was found that in the mono glycosylated GM-CSF form more than 90% of the Asn37 were occupied by N-glycans.
15009203	15	103	theme	glycoprotein	2505:2516	arg1	analysis					2418:2425	ESI-MS and MALDI-MS analysis	2398:2425	ESI-MS and MALDI-MS analysis of endoproteolytically cleaved peptides as well as MALDI-TOF MS of the intact glycoprotein	2398:2516	ESI-MS and MALDI-MS analysis of endoproteolytically cleaved peptides as well as MALDI-TOF MS of the intact glycoprotein demonstrated the N- and C-termini integrity of the GM-CSF preparations.
15009203	15	103	theme	glycoprotein	2505:2516	arg1	MS					2488:2489	MALDI-TOF MS	2478:2489	ESI-MS and MALDI-MS analysis of endoproteolytically cleaved peptides as well as MALDI-TOF MS of the intact glycoprotein	2398:2516	ESI-MS and MALDI-MS analysis of endoproteolytically cleaved peptides as well as MALDI-TOF MS of the intact glycoprotein demonstrated the N- and C-termini integrity of the GM-CSF preparations.
15009203	0	104	theme	glycosylation	34:46	arg1	occupancy					53:61	glycosylation site occupancy	34:61	glycosylation site occupancy	34:61	N- and O-linked carbohydrates and glycosylation site occupancy in recombinant human granulocyte-macrophage colony-stimulating factor secreted by a Chinese hamster ovary cell line.
15009203	12	105	from	N-terminus	1939:1948	arg1	O-glycosylation					1916:1930	O-glycosylation	1916:1930	O-glycosylation at the N-terminus of the polypeptide	1916:1967	O-glycosylation at the N-terminus of the polypeptide was detected at Ser7 and Ser9 or Thr10, in the predominantly doubly O-glycosylated glycoprotein form.
15009203	11	106	theme	ionization	1788:1797	arg1	MS					1799:1800	electrospray ionization MS	1775:1800	electrospray ionization MS	1775:1800	Site specific glycosylation was analysed by electrospray ionization MS and it was found that in the mono glycosylated GM-CSF form more than 90% of the Asn37 were occupied by N-glycans.
15009203	0	107	theme	recombinant	66:76	arg1	factor					126:131	granulocyte-macrophage colony-stimulating factor	84:131	recombinant human granulocyte-macrophage colony-stimulating factor	66:131	N- and O-linked carbohydrates and glycosylation site occupancy in recombinant human granulocyte-macrophage colony-stimulating factor secreted by a Chinese hamster ovary cell line.
15009203	3	108	theme	glycosylation	614:626	arg1	sites					628:632	the glycosylation sites	610:632	the glycosylation sites	610:632	The purpose of this work was to characterize the recombinant human GM-CSF from an engineered Chinese hamster ovary cell line grown in suspension and as adherent culture for the identification of the glycosylation sites and the definition of the glycosidic moiety, including the degree of site occupancy.
15009203	0	109	from	carbohydrates	16:28	arg1	factor					126:131	granulocyte-macrophage colony-stimulating factor	84:131	recombinant human granulocyte-macrophage colony-stimulating factor	66:131	N- and O-linked carbohydrates and glycosylation site occupancy in recombinant human granulocyte-macrophage colony-stimulating factor secreted by a Chinese hamster ovary cell line.
15009203	12	110	theme	O-glycosylated	2037:2050	arg1	form					2065:2068	the predominantly doubly O-glycosylated glycoprotein form	2012:2068	the predominantly doubly O-glycosylated glycoprotein form	2012:2068	O-glycosylation at the N-terminus of the polypeptide was detected at Ser7 and Ser9 or Thr10, in the predominantly doubly O-glycosylated glycoprotein form.
15009203	15	111	dep	N-	2535:2536	arg1	integrity					2552:2560	integrity	2552:2560	integrity	2552:2560	ESI-MS and MALDI-MS analysis of endoproteolytically cleaved peptides as well as MALDI-TOF MS of the intact glycoprotein demonstrated the N- and C-termini integrity of the GM-CSF preparations.
15009203	15	111	dep	N-	2535:2536	arg1	the					2531:2533	the	2531:2533	the	2531:2533	ESI-MS and MALDI-MS analysis of endoproteolytically cleaved peptides as well as MALDI-TOF MS of the intact glycoprotein demonstrated the N- and C-termini integrity of the GM-CSF preparations.
15009203	0	112	theme	granulocyte-macrophage	84:105	arg1	factor					126:131	granulocyte-macrophage colony-stimulating factor	84:131	recombinant human granulocyte-macrophage colony-stimulating factor	66:131	N- and O-linked carbohydrates and glycosylation site occupancy in recombinant human granulocyte-macrophage colony-stimulating factor secreted by a Chinese hamster ovary cell line.
15009203	5	113	theme	N-linked	932:939	arg1	oligosaccharides					941:956	N-linked oligosaccharides	932:956	N-linked oligosaccharides	932:956	Minor low molecular mass forms completely lacked N-linked oligosaccharides but contained 1-3 O-linked glycans.
15009203	8	114	link	alpha1-6-linked	1492:1506	arg1	fucose					1508:1513	more than 90% proximal alpha1-6-linked fucose	1469:1513	more than 90% proximal alpha1-6-linked fucose	1469:1513	MALDI-TOF MS and HPAEC-PAD analysis indicated the presence of predominantly tri- and tetraantennary N-linked oligosaccharide chains with and without N-acetyllactosamine repeat units and some 10% of biantennary oligosaccharides, all containing more than 90% proximal alpha1-6-linked fucose.
15009203	10	115	gly	sialylated	1686:1695	arg1	N-glycans					1656:1664	the N-glycans	1652:1664	the N-glycans	1652:1664	More than 90% of terminal galactose residues of the N-glycans were found alpha2-3 sialylated with NeuNAc (93%) or NeuNGc (7%).
15009203	10	115	gly	sialylated	1686:1695	arg1	%					1616:1616	More than 90%	1604:1616	More than 90% of terminal galactose residues of the N-glycans	1604:1664	More than 90% of terminal galactose residues of the N-glycans were found alpha2-3 sialylated with NeuNAc (93%) or NeuNGc (7%).
15009203	10	115	gly	sialylated	1686:1695	arg1	residues					1640:1647	terminal galactose residues	1621:1647	terminal galactose residues of the N-glycans	1621:1664	More than 90% of terminal galactose residues of the N-glycans were found alpha2-3 sialylated with NeuNAc (93%) or NeuNGc (7%).
15009203	8	116	theme	repeat	1395:1400	arg1	units					1402:1406	N-acetyllactosamine repeat units	1375:1406	N-acetyllactosamine repeat units	1375:1406	MALDI-TOF MS and HPAEC-PAD analysis indicated the presence of predominantly tri- and tetraantennary N-linked oligosaccharide chains with and without N-acetyllactosamine repeat units and some 10% of biantennary oligosaccharides, all containing more than 90% proximal alpha1-6-linked fucose.
15009203	14	117	theme	single	2309:2314	arg1	site					2332:2335	a single N-glycosylation site	2307:2335	a single N-glycosylation site occupied in the preparation derived from suspension culture	2307:2395	The major difference between both preparations was found in the MALDI spectra of the desialylated glycoproteins, revealing a higher proportion of forms with a single N-glycosylation site occupied in the preparation derived from suspension culture.
15009203	6	118	located	detected	1035:1042	arg2	isoforms					1021:1028	Twelve differently charged isoforms	994:1028	Twelve differently charged isoforms	994:1028	Twelve differently charged isoforms were detected in isoelectric focusing gels.
15009203	6	118	located	detected	1035:1042	arg1	gels					1068:1071	isoelectric focusing gels	1047:1071	isoelectric focusing gels	1047:1071	Twelve differently charged isoforms were detected in isoelectric focusing gels.
15009203	14	119	attach	derived	2365:2371	arg2	preparation					2353:2363	the preparation	2349:2363	the preparation derived from suspension culture	2349:2395	The major difference between both preparations was found in the MALDI spectra of the desialylated glycoproteins, revealing a higher proportion of forms with a single N-glycosylation site occupied in the preparation derived from suspension culture.
15009203	14	119	attach	derived	2365:2371	arg1	culture					2389:2395	suspension culture	2378:2395	suspension culture	2378:2395	The major difference between both preparations was found in the MALDI spectra of the desialylated glycoproteins, revealing a higher proportion of forms with a single N-glycosylation site occupied in the preparation derived from suspension culture.
15009203	15	120	theme	preparations	2576:2587	arg1	N-					2535:2536	N-	2535:2536	N-	2535:2536	ESI-MS and MALDI-MS analysis of endoproteolytically cleaved peptides as well as MALDI-TOF MS of the intact glycoprotein demonstrated the N- and C-termini integrity of the GM-CSF preparations.
15009203	6	121	theme	isoelectric	1047:1057	arg1	gels					1068:1071	isoelectric focusing gels	1047:1071	isoelectric focusing gels	1047:1071	Twelve differently charged isoforms were detected in isoelectric focusing gels.
15009203	0	122	from	occupancy	53:61	arg1	factor					126:131	granulocyte-macrophage colony-stimulating factor	84:131	recombinant human granulocyte-macrophage colony-stimulating factor	66:131	N- and O-linked carbohydrates and glycosylation site occupancy in recombinant human granulocyte-macrophage colony-stimulating factor secreted by a Chinese hamster ovary cell line.
15009203	7	123	theme	GM-CSFs	1217:1223	arg1	spectra					1189:1195	MALDI-TOF MS spectra	1176:1195	MALDI-TOF MS spectra of the desialylated GM-CSFs	1176:1223	At least 16 glycoforms, differing in the number of Hex-HexNAc units (Deltam 365 Da), were detected in MALDI-TOF MS spectra of the desialylated GM-CSFs.
15009203	11	124	dep	glycosylated	1836:1847	arg1	mono					1831:1834	mono	1831:1834	mono	1831:1834	Site specific glycosylation was analysed by electrospray ionization MS and it was found that in the mono glycosylated GM-CSF form more than 90% of the Asn37 were occupied by N-glycans.
15009203	15	125	theme	cleaved	2450:2456	arg1	peptides					2458:2465	endoproteolytically cleaved peptides	2430:2465	endoproteolytically cleaved peptides	2430:2465	ESI-MS and MALDI-MS analysis of endoproteolytically cleaved peptides as well as MALDI-TOF MS of the intact glycoprotein demonstrated the N- and C-termini integrity of the GM-CSF preparations.
15009203	12	126	gly	glycoprotein	2052:2063	arg1	glycoprotein					2052:2063	the predominantly doubly O-glycosylated glycoprotein form	2012:2068	the predominantly doubly O-glycosylated glycoprotein form	2012:2068	O-glycosylation at the N-terminus of the polypeptide was detected at Ser7 and Ser9 or Thr10, in the predominantly doubly O-glycosylated glycoprotein form.
15009203	4	127	theme	size	747:750	arg1	heterogeneity					752:764	size heterogeneity	747:764	size heterogeneity in SDS/PAGE	747:776	Both preparations exhibited size heterogeneity in SDS/PAGE with multiple bands containing glycoprotein forms with either two or one N-glycosylation sites occupied.
15009203	14	128	theme	higher	2275:2280	arg1	proportion					2282:2291	a higher proportion	2273:2291	a higher proportion of forms with a single N-glycosylation site occupied in the preparation derived from suspension culture	2273:2395	The major difference between both preparations was found in the MALDI spectra of the desialylated glycoproteins, revealing a higher proportion of forms with a single N-glycosylation site occupied in the preparation derived from suspension culture.
15009203	2	129	theme	production	390:399	arg1	process					401:407	the production process	386:407	the production process used	386:412	It has been produced in different cell types, with different properties that depend on the production process used.
15009203	5	130	link	N-linked	932:939	arg1	oligosaccharides					941:956	N-linked oligosaccharides	932:956	N-linked oligosaccharides	932:956	Minor low molecular mass forms completely lacked N-linked oligosaccharides but contained 1-3 O-linked glycans.
15009203	8	131	theme	oligosaccharides	1436:1451	arg1	all					1454:1456	all	1454:1456	all	1454:1456	MALDI-TOF MS and HPAEC-PAD analysis indicated the presence of predominantly tri- and tetraantennary N-linked oligosaccharide chains with and without N-acetyllactosamine repeat units and some 10% of biantennary oligosaccharides, all containing more than 90% proximal alpha1-6-linked fucose.
15009203	8	131	theme	oligosaccharides	1436:1451	arg1	%					1419:1419	some 10%	1412:1419	some 10% of biantennary oligosaccharides	1412:1451	MALDI-TOF MS and HPAEC-PAD analysis indicated the presence of predominantly tri- and tetraantennary N-linked oligosaccharide chains with and without N-acetyllactosamine repeat units and some 10% of biantennary oligosaccharides, all containing more than 90% proximal alpha1-6-linked fucose.
15009203	8	131	theme	oligosaccharides	1436:1451	arg1	oligosaccharides					1436:1451	biantennary oligosaccharides	1424:1451	biantennary oligosaccharides	1424:1451	MALDI-TOF MS and HPAEC-PAD analysis indicated the presence of predominantly tri- and tetraantennary N-linked oligosaccharide chains with and without N-acetyllactosamine repeat units and some 10% of biantennary oligosaccharides, all containing more than 90% proximal alpha1-6-linked fucose.
15009203	8	131	theme	oligosaccharides	1436:1451	arg1	chains					1351:1356	predominantly tri- and tetraantennary N-linked oligosaccharide chains	1288:1356	predominantly tri- and tetraantennary N-linked oligosaccharide chains with and without N-acetyllactosamine repeat units	1288:1406	MALDI-TOF MS and HPAEC-PAD analysis indicated the presence of predominantly tri- and tetraantennary N-linked oligosaccharide chains with and without N-acetyllactosamine repeat units and some 10% of biantennary oligosaccharides, all containing more than 90% proximal alpha1-6-linked fucose.
15009203	11	132	theme	Asn37	1882:1886	arg1	%					1873:1873	more than 90%	1861:1873	more than 90% of the Asn37	1861:1886	Site specific glycosylation was analysed by electrospray ionization MS and it was found that in the mono glycosylated GM-CSF form more than 90% of the Asn37 were occupied by N-glycans.
15009203	11	132	theme	Asn37	1882:1886	arg1	Asn37					1882:1886	the Asn37	1878:1886	the Asn37	1878:1886	Site specific glycosylation was analysed by electrospray ionization MS and it was found that in the mono glycosylated GM-CSF form more than 90% of the Asn37 were occupied by N-glycans.
15009203	7	133	theme	MALDI-TOF	1176:1184	arg1	spectra					1189:1195	MALDI-TOF MS spectra	1176:1195	MALDI-TOF MS spectra of the desialylated GM-CSFs	1176:1223	At least 16 glycoforms, differing in the number of Hex-HexNAc units (Deltam 365 Da), were detected in MALDI-TOF MS spectra of the desialylated GM-CSFs.
15009203	3	134	theme	recombinant	464:474	arg1	GM-CSF					482:487	the recombinant human GM-CSF	460:487	the recombinant human GM-CSF	460:487	The purpose of this work was to characterize the recombinant human GM-CSF from an engineered Chinese hamster ovary cell line grown in suspension and as adherent culture for the identification of the glycosylation sites and the definition of the glycosidic moiety, including the degree of site occupancy.
15009203	11	135	used	occupied	1893:1900	arg2	Asn37					1882:1886	the Asn37	1878:1886	the Asn37	1878:1886	Site specific glycosylation was analysed by electrospray ionization MS and it was found that in the mono glycosylated GM-CSF form more than 90% of the Asn37 were occupied by N-glycans.
15009203	11	135	used	occupied	1893:1900	arg2	%					1873:1873	more than 90%	1861:1873	more than 90% of the Asn37	1861:1886	Site specific glycosylation was analysed by electrospray ionization MS and it was found that in the mono glycosylated GM-CSF form more than 90% of the Asn37 were occupied by N-glycans.
15009203	8	136	contain	containing	1458:1467	arg2	fucose					1508:1513	more than 90% proximal alpha1-6-linked fucose	1469:1513	more than 90% proximal alpha1-6-linked fucose	1469:1513	MALDI-TOF MS and HPAEC-PAD analysis indicated the presence of predominantly tri- and tetraantennary N-linked oligosaccharide chains with and without N-acetyllactosamine repeat units and some 10% of biantennary oligosaccharides, all containing more than 90% proximal alpha1-6-linked fucose.
15009203	8	136	contain	containing	1458:1467	arg1	all					1454:1456	all	1454:1456	all	1454:1456	MALDI-TOF MS and HPAEC-PAD analysis indicated the presence of predominantly tri- and tetraantennary N-linked oligosaccharide chains with and without N-acetyllactosamine repeat units and some 10% of biantennary oligosaccharides, all containing more than 90% proximal alpha1-6-linked fucose.
15009203	8	136	contain	containing	1458:1467	arg1	chains					1351:1356	predominantly tri- and tetraantennary N-linked oligosaccharide chains	1288:1356	predominantly tri- and tetraantennary N-linked oligosaccharide chains with and without N-acetyllactosamine repeat units	1288:1406	MALDI-TOF MS and HPAEC-PAD analysis indicated the presence of predominantly tri- and tetraantennary N-linked oligosaccharide chains with and without N-acetyllactosamine repeat units and some 10% of biantennary oligosaccharides, all containing more than 90% proximal alpha1-6-linked fucose.
15009203	15	137	gly	glycoprotein	2505:2516	arg1	glycoprotein					2505:2516	the intact glycoprotein	2494:2516	the intact glycoprotein	2494:2516	ESI-MS and MALDI-MS analysis of endoproteolytically cleaved peptides as well as MALDI-TOF MS of the intact glycoprotein demonstrated the N- and C-termini integrity of the GM-CSF preparations.
15009203	3	138	theme	Chinese	508:514	arg1	line					535:538	an engineered Chinese hamster ovary cell line	494:538	an engineered Chinese hamster ovary cell line	494:538	The purpose of this work was to characterize the recombinant human GM-CSF from an engineered Chinese hamster ovary cell line grown in suspension and as adherent culture for the identification of the glycosylation sites and the definition of the glycosidic moiety, including the degree of site occupancy.
15009203	8	139	dep	fucose	1508:1513	arg1	%					1481:1481	%	1481:1481	%	1481:1481	MALDI-TOF MS and HPAEC-PAD analysis indicated the presence of predominantly tri- and tetraantennary N-linked oligosaccharide chains with and without N-acetyllactosamine repeat units and some 10% of biantennary oligosaccharides, all containing more than 90% proximal alpha1-6-linked fucose.
15009203	3	140	theme	moiety	671:676	arg1	definition					642:651	the definition	638:651	the definition of the glycosidic moiety	638:676	The purpose of this work was to characterize the recombinant human GM-CSF from an engineered Chinese hamster ovary cell line grown in suspension and as adherent culture for the identification of the glycosylation sites and the definition of the glycosidic moiety, including the degree of site occupancy.
15009203	3	140	theme	moiety	671:676	arg1	identification					592:605	the identification	588:605	the identification of the glycosylation sites	588:632	The purpose of this work was to characterize the recombinant human GM-CSF from an engineered Chinese hamster ovary cell line grown in suspension and as adherent culture for the identification of the glycosylation sites and the definition of the glycosidic moiety, including the degree of site occupancy.
15009203	4	141	theme	glycoprotein	809:820	arg1	forms					822:826	glycoprotein forms	809:826	glycoprotein forms	809:826	Both preparations exhibited size heterogeneity in SDS/PAGE with multiple bands containing glycoprotein forms with either two or one N-glycosylation sites occupied.
15009203	1	142	theme	leukocyte	253:261	arg1	production					263:272	leukocyte production	253:272	leukocyte production	253:272	GM-CSF is one of several naturally occurring glycoproteins that regulate leukocyte production, migration and function.
15009203	9	143	theme	GM-CSF	1553:1558	arg1	preparations					1560:1571	both GM-CSF preparations	1548:1571	both GM-CSF preparations	1548:1571	The oligosaccharide patterns of both GM-CSF preparations were found to be very similar.
15009203	14	144	gly	desialylated	2235:2246	arg1	glycoproteins					2248:2260	the desialylated glycoproteins	2231:2260	the desialylated glycoproteins	2231:2260	The major difference between both preparations was found in the MALDI spectra of the desialylated glycoproteins, revealing a higher proportion of forms with a single N-glycosylation site occupied in the preparation derived from suspension culture.
15009203	14	145	theme	desialylated	2235:2246	arg1	glycoproteins					2248:2260	the desialylated glycoproteins	2231:2260	the desialylated glycoproteins	2231:2260	The major difference between both preparations was found in the MALDI spectra of the desialylated glycoproteins, revealing a higher proportion of forms with a single N-glycosylation site occupied in the preparation derived from suspension culture.
15009203	3	146	theme	site	703:706	arg1	occupancy					708:716	site occupancy	703:716	site occupancy	703:716	The purpose of this work was to characterize the recombinant human GM-CSF from an engineered Chinese hamster ovary cell line grown in suspension and as adherent culture for the identification of the glycosylation sites and the definition of the glycosidic moiety, including the degree of site occupancy.
15009203	8	147	theme	proximal	1483:1490	arg1	fucose					1508:1513	more than 90% proximal alpha1-6-linked fucose	1469:1513	more than 90% proximal alpha1-6-linked fucose	1469:1513	MALDI-TOF MS and HPAEC-PAD analysis indicated the presence of predominantly tri- and tetraantennary N-linked oligosaccharide chains with and without N-acetyllactosamine repeat units and some 10% of biantennary oligosaccharides, all containing more than 90% proximal alpha1-6-linked fucose.
15140192	4	0	theme	putative	560:567	arg1	sites					585:589	putative N-glycosylation sites	560:589	putative N-glycosylation sites	560:589	Therefore, the effects of N-glycosylation were investigated by producing single-point (N163Q and N166Q) or double-point mutations (NN163/166QQ and NN163/166AA) at putative N-glycosylation sites.
15140192	6	1	from	properties	895:904	arg1	cell-types					919:928	different cell-types	909:928	different cell-types	909:928	We determined the effects of these manipulations on prestin's cell surface expression, molecular mass, glycosylation pattern, and electrophysiological properties in different cell-types.
15140192	6	2	theme	surface	811:817	arg1	expression					819:828	prestin's cell surface expression	796:828	prestin's cell surface expression	796:828	We determined the effects of these manipulations on prestin's cell surface expression, molecular mass, glycosylation pattern, and electrophysiological properties in different cell-types.
15140192	5	3	from	glycosylation	708:720	arg1	prestin					735:741	wild-type prestin	725:741	wild-type prestin	725:741	Further, treatment with tunicamycin or glycopeptidase-F was used to determine the consequences of removing N-linked glycosylation in wild-type prestin.
15140192	5	4	used	used	652:655	arg2	treatment					601:609	treatment	601:609	treatment with tunicamycin or glycopeptidase-F	601:646	Further, treatment with tunicamycin or glycopeptidase-F was used to determine the consequences of removing N-linked glycosylation in wild-type prestin.
15140192	6	5	theme	different	909:917	arg1	cell-types					919:928	different cell-types	909:928	different cell-types	909:928	We determined the effects of these manipulations on prestin's cell surface expression, molecular mass, glycosylation pattern, and electrophysiological properties in different cell-types.
15140192	0	6	link	N-linked	0:7	arg1	sites					23:27	N-linked glycosylation sites	0:27	N-linked glycosylation sites of the motor protein prestin: effects on membrane targeting and electrophysiological function.	0:122	N-linked glycosylation sites of the motor protein prestin: effects on membrane targeting and electrophysiological function.
15140192	0	6	link	N-linked	0:7	arg1	prestin					50:56	the motor protein prestin	32:56	the motor protein prestin	32:56	N-linked glycosylation sites of the motor protein prestin: effects on membrane targeting and electrophysiological function.
15140192	13	7	theme	OHC	1685:1687	arg1	electromotility					1689:1703	OHC electromotility	1685:1703	OHC electromotility	1685:1703	These data suggest that glycosylation of prestin may quantitatively affect OHC electromotility.
15140192	1	8	theme	cells	165:169	arg1	protein					143:149	a motor protein	135:149	a motor protein of outer hair cells (OHC) that plays a crucial role in mammalian hearing	135:222	Prestin is a motor protein of outer hair cells (OHC) that plays a crucial role in mammalian hearing.
15140192	1	8	theme	cells	165:169	arg1	Prestin					124:130	Prestin	124:130	Prestin	124:130	Prestin is a motor protein of outer hair cells (OHC) that plays a crucial role in mammalian hearing.
15140192	12	9	from	transfer	1573:1580	arg1	change					1519:1524	a change	1517:1524	a change in membrane potential at most effective charge transfer to more depolarized values	1517:1607	Compared to glycosylated prestin, the fully de-glycosylated protein has altered electrophysiological function, with a change in membrane potential at most effective charge transfer to more depolarized values.
15140192	12	10	theme	electrophysiological	1481:1500	arg1	function					1502:1509	altered electrophysiological function	1473:1509	altered electrophysiological function	1473:1509	Compared to glycosylated prestin, the fully de-glycosylated protein has altered electrophysiological function, with a change in membrane potential at most effective charge transfer to more depolarized values.
15140192	12	11	theme	glycosylated	1413:1424	arg1	prestin					1426:1432	glycosylated prestin	1413:1432	glycosylated prestin	1413:1432	Compared to glycosylated prestin, the fully de-glycosylated protein has altered electrophysiological function, with a change in membrane potential at most effective charge transfer to more depolarized values.
15140192	6	12	from	pattern	861:867	arg1	cell-types					919:928	different cell-types	909:928	different cell-types	909:928	We determined the effects of these manipulations on prestin's cell surface expression, molecular mass, glycosylation pattern, and electrophysiological properties in different cell-types.
15140192	2	13	theme	N-linked	283:290	arg1	sites					306:310	three potential N-linked glycosylation sites	267:310	three potential N-linked glycosylation sites	267:310	Prestin is a putative N-glycoprotein with three potential N-linked glycosylation sites.
15140192	12	14	gly	de-glycosylated	1445:1459	arg1	protein					1461:1467	the fully de-glycosylated protein	1435:1467	the fully de-glycosylated protein	1435:1467	Compared to glycosylated prestin, the fully de-glycosylated protein has altered electrophysiological function, with a change in membrane potential at most effective charge transfer to more depolarized values.
15140192	13	15	theme	prestin	1651:1657	arg1	glycosylation					1634:1646	glycosylation	1634:1646	glycosylation of prestin	1634:1657	These data suggest that glycosylation of prestin may quantitatively affect OHC electromotility.
15140192	11	16	gly	deglycosylated	1301:1314	arg1	prestin					1316:1322	deglycosylated prestin	1301:1322	deglycosylated prestin	1301:1322	Both glycosylated and deglycosylated prestin demonstrate non-linear capacitance, a signature of prestin's motor function.
15140192	7	17	with	glycoprotein	963:974	arg1	sites					1004:1008	N-linked glycosylation sites	981:1008	N-linked glycosylation sites at N163 and N166	981:1025	Data indicate that prestin is a glycoprotein with N-linked glycosylation sites at N163 and N166.
15140192	5	18	theme	wild-type	725:733	arg1	prestin					735:741	wild-type prestin	725:741	wild-type prestin	725:741	Further, treatment with tunicamycin or glycopeptidase-F was used to determine the consequences of removing N-linked glycosylation in wild-type prestin.
15140192	5	19	with	treatment	601:609	arg1	glycopeptidase-F					631:646	glycopeptidase-F	631:646	glycopeptidase-F	631:646	Further, treatment with tunicamycin or glycopeptidase-F was used to determine the consequences of removing N-linked glycosylation in wild-type prestin.
15140192	5	19	with	treatment	601:609	arg1	tunicamycin					616:626	tunicamycin	616:626	tunicamycin	616:626	Further, treatment with tunicamycin or glycopeptidase-F was used to determine the consequences of removing N-linked glycosylation in wild-type prestin.
15140192	5	20	gly	glycosylation	708:720	arg1	prestin					735:741	wild-type prestin	725:741	wild-type prestin	725:741	Further, treatment with tunicamycin or glycopeptidase-F was used to determine the consequences of removing N-linked glycosylation in wild-type prestin.
15140192	11	21	theme	function	1391:1398	arg1	capacitance					1347:1357	non-linear capacitance	1336:1357	non-linear capacitance	1336:1357	Both glycosylated and deglycosylated prestin demonstrate non-linear capacitance, a signature of prestin's motor function.
15140192	11	21	theme	function	1391:1398	arg1	signature					1362:1370	a signature	1360:1370	a signature of prestin's motor function	1360:1398	Both glycosylated and deglycosylated prestin demonstrate non-linear capacitance, a signature of prestin's motor function.
15140192	10	22	gly	glycosylation	1207:1219	arg1	plasma					1241:1246	plasma membrane targeting	1241:1265	plasma membrane targeting of prestin	1241:1276	N-linked glycosylation is not required for plasma membrane targeting of prestin.
15140192	10	22	gly	glycosylation	1207:1219	arg1	membrane					1248:1255	plasma membrane targeting	1241:1265	plasma membrane targeting of prestin	1241:1276	N-linked glycosylation is not required for plasma membrane targeting of prestin.
15140192	10	22	gly	glycosylation	1207:1219	arg1	prestin					1270:1276	prestin	1270:1276	prestin	1270:1276	N-linked glycosylation is not required for plasma membrane targeting of prestin.
15140192	10	23	theme	plasma	1241:1246	arg1	targeting					1257:1265	plasma membrane targeting	1241:1265	plasma membrane targeting of prestin	1241:1276	N-linked glycosylation is not required for plasma membrane targeting of prestin.
15140192	2	24	with	N-glycoprotein	247:260	arg1	sites					306:310	three potential N-linked glycosylation sites	267:310	three potential N-linked glycosylation sites	267:310	Prestin is a putative N-glycoprotein with three potential N-linked glycosylation sites.
15140192	7	25	theme	glycosylation	990:1002	arg1	sites					1004:1008	N-linked glycosylation sites	981:1008	N-linked glycosylation sites at N163 and N166	981:1025	Data indicate that prestin is a glycoprotein with N-linked glycosylation sites at N163 and N166.
15140192	1	26	theme	outer	154:158	arg1	OHC					172:174	OHC	172:174	OHC	172:174	Prestin is a motor protein of outer hair cells (OHC) that plays a crucial role in mammalian hearing.
15140192	1	26	theme	outer	154:158	arg1	cells					165:169	outer hair cells	154:169	outer hair cells (OHC)	154:175	Prestin is a motor protein of outer hair cells (OHC) that plays a crucial role in mammalian hearing.
15140192	12	27	theme	effective	1556:1564	arg1	transfer					1573:1580	most effective charge transfer	1551:1580	most effective charge transfer to more depolarized values	1551:1607	Compared to glycosylated prestin, the fully de-glycosylated protein has altered electrophysiological function, with a change in membrane potential at most effective charge transfer to more depolarized values.
15140192	3	28	dep	function	363:370	arg1	the					359:361	the	359:361	the	359:361	It is not known whether glycosylation affects the function and activity of prestin.
15140192	10	29	theme	prestin	1270:1276	arg1	targeting					1257:1265	plasma membrane targeting	1241:1265	plasma membrane targeting of prestin	1241:1276	N-linked glycosylation is not required for plasma membrane targeting of prestin.
15140192	8	30	theme	differential	1051:1062	arg1	programs					1064:1071	differential programs	1051:1071	differential programs	1051:1071	N163 and N166 may have differential programs for synthesis and trimming of the glycans.
15140192	12	31	theme	depolarized	1590:1600	arg1	values					1602:1607	more depolarized values	1585:1607	more depolarized values	1585:1607	Compared to glycosylated prestin, the fully de-glycosylated protein has altered electrophysiological function, with a change in membrane potential at most effective charge transfer to more depolarized values.
15140192	0	32	theme	electrophysiological	93:112	arg1	function					114:121	electrophysiological function	93:121	electrophysiological function	93:121	N-linked glycosylation sites of the motor protein prestin: effects on membrane targeting and electrophysiological function.
15140192	11	33	theme	non-linear	1336:1345	arg1	capacitance					1347:1357	non-linear capacitance	1336:1357	non-linear capacitance	1336:1357	Both glycosylated and deglycosylated prestin demonstrate non-linear capacitance, a signature of prestin's motor function.
15140192	11	33	theme	non-linear	1336:1345	arg1	signature					1362:1370	a signature	1360:1370	a signature of prestin's motor function	1360:1398	Both glycosylated and deglycosylated prestin demonstrate non-linear capacitance, a signature of prestin's motor function.
15140192	0	34	theme	N-linked	0:7	arg1	sites					23:27	N-linked glycosylation sites	0:27	N-linked glycosylation sites of the motor protein prestin: effects on membrane targeting and electrophysiological function.	0:122	N-linked glycosylation sites of the motor protein prestin: effects on membrane targeting and electrophysiological function.
15140192	0	34	theme	N-linked	0:7	arg1	prestin					50:56	the motor protein prestin	32:56	the motor protein prestin	32:56	N-linked glycosylation sites of the motor protein prestin: effects on membrane targeting and electrophysiological function.
15140192	4	35	gly	N-glycosylation	569:583	arg2	sites					585:589	putative N-glycosylation sites	560:589	putative N-glycosylation sites	560:589	Therefore, the effects of N-glycosylation were investigated by producing single-point (N163Q and N166Q) or double-point mutations (NN163/166QQ and NN163/166AA) at putative N-glycosylation sites.
15140192	6	36	from	expression	819:828	arg1	cell-types					919:928	different cell-types	909:928	different cell-types	909:928	We determined the effects of these manipulations on prestin's cell surface expression, molecular mass, glycosylation pattern, and electrophysiological properties in different cell-types.
15140192	9	37	contain	have	1141:1144	arg2	extent					1154:1159	greater extent	1146:1159	greater extent of glycosylation than its companion	1146:1195	The N166 site appears to have greater extent of glycosylation than its companion.
15140192	9	37	contain	have	1141:1144	arg1	site					1125:1128	The N166 site	1116:1128	The N166 site	1116:1128	The N166 site appears to have greater extent of glycosylation than its companion.
15140192	6	38	theme	electrophysiological	874:893	arg1	properties					895:904	electrophysiological properties	874:904	electrophysiological properties	874:904	We determined the effects of these manipulations on prestin's cell surface expression, molecular mass, glycosylation pattern, and electrophysiological properties in different cell-types.
15140192	3	39	theme	prestin	388:394	arg1	function					363:370	function	363:370	function	363:370	It is not known whether glycosylation affects the function and activity of prestin.
15140192	3	39	theme	prestin	388:394	arg1	activity					376:383	activity	376:383	activity	376:383	It is not known whether glycosylation affects the function and activity of prestin.
15140192	8	40	theme	glycans	1107:1113	arg1	synthesis					1077:1085	synthesis	1077:1085	synthesis	1077:1085	N163 and N166 may have differential programs for synthesis and trimming of the glycans.
15140192	8	40	theme	glycans	1107:1113	arg1	trimming					1091:1098	trimming	1091:1098	trimming	1091:1098	N163 and N166 may have differential programs for synthesis and trimming of the glycans.
15140192	0	41	gly	glycosylation	9:21	arg2	prestin					50:56	the motor protein prestin	32:56	the motor protein prestin	32:56	N-linked glycosylation sites of the motor protein prestin: effects on membrane targeting and electrophysiological function.
15140192	0	41	gly	glycosylation	9:21	arg1	prestin					50:56	the motor protein prestin	32:56	the motor protein prestin	32:56	N-linked glycosylation sites of the motor protein prestin: effects on membrane targeting and electrophysiological function.
15140192	0	41	gly	glycosylation	9:21	arg2	sites					23:27	N-linked glycosylation sites	0:27	N-linked glycosylation sites of the motor protein prestin: effects on membrane targeting and electrophysiological function.	0:122	N-linked glycosylation sites of the motor protein prestin: effects on membrane targeting and electrophysiological function.
15140192	0	42	theme	protein	42:48	arg1	prestin					50:56	the motor protein prestin	32:56	the motor protein prestin	32:56	N-linked glycosylation sites of the motor protein prestin: effects on membrane targeting and electrophysiological function.
15140192	12	43	theme	membrane	1529:1536	arg1	potential					1538:1546	membrane potential	1529:1546	membrane potential	1529:1546	Compared to glycosylated prestin, the fully de-glycosylated protein has altered electrophysiological function, with a change in membrane potential at most effective charge transfer to more depolarized values.
15140192	10	44	link	N-linked	1198:1205	arg1	glycosylation					1207:1219	N-linked glycosylation	1198:1219	N-linked glycosylation	1198:1219	N-linked glycosylation is not required for plasma membrane targeting of prestin.
15140192	1	45	theme	crucial	190:196	arg1	role					198:201	a crucial role	188:201	a crucial role	188:201	Prestin is a motor protein of outer hair cells (OHC) that plays a crucial role in mammalian hearing.
15140192	0	46	dep	sites	23:27	arg1	effects					59:65	effects	59:65	N-linked glycosylation sites of the motor protein prestin: effects on membrane targeting and electrophysiological function.	0:122	N-linked glycosylation sites of the motor protein prestin: effects on membrane targeting and electrophysiological function.
15140192	9	47	theme	glycosylation	1164:1176	arg1	extent					1154:1159	greater extent	1146:1159	greater extent of glycosylation than its companion	1146:1195	The N166 site appears to have greater extent of glycosylation than its companion.
15140192	5	48	link	N-linked	699:706	arg1	glycosylation					708:720	N-linked glycosylation	699:720	N-linked glycosylation in wild-type prestin	699:741	Further, treatment with tunicamycin or glycopeptidase-F was used to determine the consequences of removing N-linked glycosylation in wild-type prestin.
15140192	7	49	gly	glycosylation	990:1002	arg2	sites					1004:1008	N-linked glycosylation sites	981:1008	N-linked glycosylation sites at N163 and N166	981:1025	Data indicate that prestin is a glycoprotein with N-linked glycosylation sites at N163 and N166.
15140192	7	49	gly	glycosylation	990:1002	arg2	N166					1022:1025	N166	1022:1025	N166	1022:1025	Data indicate that prestin is a glycoprotein with N-linked glycosylation sites at N163 and N166.
15140192	7	49	gly	glycosylation	990:1002	arg2	N163					1013:1016	N163	1013:1016	N163	1013:1016	Data indicate that prestin is a glycoprotein with N-linked glycosylation sites at N163 and N166.
15140192	2	50	gly	N-glycoprotein	247:260	arg1	N-glycoprotein					247:260	a putative N-glycoprotein	236:260	a putative N-glycoprotein with three potential N-linked glycosylation sites	236:310	Prestin is a putative N-glycoprotein with three potential N-linked glycosylation sites.
15140192	2	50	gly	N-glycoprotein	247:260	arg1	Prestin					225:231	Prestin	225:231	Prestin	225:231	Prestin is a putative N-glycoprotein with three potential N-linked glycosylation sites.
15140192	12	51	theme	altered	1473:1479	arg1	function					1502:1509	altered electrophysiological function	1473:1509	altered electrophysiological function	1473:1509	Compared to glycosylated prestin, the fully de-glycosylated protein has altered electrophysiological function, with a change in membrane potential at most effective charge transfer to more depolarized values.
15140192	4	52	theme	N-glycosylation	569:583	arg1	sites					585:589	putative N-glycosylation sites	560:589	putative N-glycosylation sites	560:589	Therefore, the effects of N-glycosylation were investigated by producing single-point (N163Q and N166Q) or double-point mutations (NN163/166QQ and NN163/166AA) at putative N-glycosylation sites.
15140192	6	53	theme	cell	806:809	arg1	expression					819:828	prestin's cell surface expression	796:828	prestin's cell surface expression	796:828	We determined the effects of these manipulations on prestin's cell surface expression, molecular mass, glycosylation pattern, and electrophysiological properties in different cell-types.
15140192	2	54	theme	putative	238:245	arg1	N-glycoprotein					247:260	a putative N-glycoprotein	236:260	a putative N-glycoprotein with three potential N-linked glycosylation sites	236:310	Prestin is a putative N-glycoprotein with three potential N-linked glycosylation sites.
15140192	2	54	theme	putative	238:245	arg1	Prestin					225:231	Prestin	225:231	Prestin	225:231	Prestin is a putative N-glycoprotein with three potential N-linked glycosylation sites.
15140192	1	55	theme	hair	160:163	arg1	OHC					172:174	OHC	172:174	OHC	172:174	Prestin is a motor protein of outer hair cells (OHC) that plays a crucial role in mammalian hearing.
15140192	1	55	theme	hair	160:163	arg1	cells					165:169	outer hair cells	154:169	outer hair cells (OHC)	154:175	Prestin is a motor protein of outer hair cells (OHC) that plays a crucial role in mammalian hearing.
15140192	12	56	theme	de-glycosylated	1445:1459	arg1	protein					1461:1467	the fully de-glycosylated protein	1435:1467	the fully de-glycosylated protein	1435:1467	Compared to glycosylated prestin, the fully de-glycosylated protein has altered electrophysiological function, with a change in membrane potential at most effective charge transfer to more depolarized values.
15140192	7	57	from	N163	1013:1016	arg1	sites					1004:1008	N-linked glycosylation sites	981:1008	N-linked glycosylation sites at N163 and N166	981:1025	Data indicate that prestin is a glycoprotein with N-linked glycosylation sites at N163 and N166.
15140192	2	58	theme	glycosylation	292:304	arg1	sites					306:310	three potential N-linked glycosylation sites	267:310	three potential N-linked glycosylation sites	267:310	Prestin is a putative N-glycoprotein with three potential N-linked glycosylation sites.
15140192	6	59	theme	glycosylation	847:859	arg1	pattern					861:867	glycosylation pattern	847:867	glycosylation pattern	847:867	We determined the effects of these manipulations on prestin's cell surface expression, molecular mass, glycosylation pattern, and electrophysiological properties in different cell-types.
15140192	7	60	from	N166	1022:1025	arg1	sites					1004:1008	N-linked glycosylation sites	981:1008	N-linked glycosylation sites at N163 and N166	981:1025	Data indicate that prestin is a glycoprotein with N-linked glycosylation sites at N163 and N166.
15140192	5	61	theme	N-linked	699:706	arg1	glycosylation					708:720	N-linked glycosylation	699:720	N-linked glycosylation in wild-type prestin	699:741	Further, treatment with tunicamycin or glycopeptidase-F was used to determine the consequences of removing N-linked glycosylation in wild-type prestin.
15140192	6	62	theme	manipulations	779:791	arg1	effects					762:768	the effects	758:768	the effects of these manipulations on prestin's cell surface expression, molecular mass, glycosylation pattern, and electrophysiological properties in different cell-types	758:928	We determined the effects of these manipulations on prestin's cell surface expression, molecular mass, glycosylation pattern, and electrophysiological properties in different cell-types.
15140192	2	63	theme	potential	273:281	arg1	sites					306:310	three potential N-linked glycosylation sites	267:310	three potential N-linked glycosylation sites	267:310	Prestin is a putative N-glycoprotein with three potential N-linked glycosylation sites.
15140192	4	64	theme	N-glycosylation	423:437	arg1	effects					412:418	the effects	408:418	the effects of N-glycosylation	408:437	Therefore, the effects of N-glycosylation were investigated by producing single-point (N163Q and N166Q) or double-point mutations (NN163/166QQ and NN163/166AA) at putative N-glycosylation sites.
15140192	6	65	from	mass	841:844	arg1	cell-types					919:928	different cell-types	909:928	different cell-types	909:928	We determined the effects of these manipulations on prestin's cell surface expression, molecular mass, glycosylation pattern, and electrophysiological properties in different cell-types.
15140192	13	66	gly	glycosylation	1634:1646	arg1	prestin					1651:1657	prestin	1651:1657	prestin	1651:1657	These data suggest that glycosylation of prestin may quantitatively affect OHC electromotility.
15140192	0	67	from	effects	59:65	arg1	targeting					79:87	membrane targeting	70:87	membrane targeting	70:87	N-linked glycosylation sites of the motor protein prestin: effects on membrane targeting and electrophysiological function.
15140192	0	67	from	effects	59:65	arg1	function					114:121	electrophysiological function	93:121	electrophysiological function	93:121	N-linked glycosylation sites of the motor protein prestin: effects on membrane targeting and electrophysiological function.
15140192	11	68	theme	motor	1385:1389	arg1	function					1391:1398	prestin's motor function	1375:1398	prestin's motor function	1375:1398	Both glycosylated and deglycosylated prestin demonstrate non-linear capacitance, a signature of prestin's motor function.
15140192	12	69	gly	glycosylated	1413:1424	arg1	prestin					1426:1432	glycosylated prestin	1413:1432	glycosylated prestin	1413:1432	Compared to glycosylated prestin, the fully de-glycosylated protein has altered electrophysiological function, with a change in membrane potential at most effective charge transfer to more depolarized values.
15140192	2	70	link	N-linked	283:290	arg1	sites					306:310	three potential N-linked glycosylation sites	267:310	three potential N-linked glycosylation sites	267:310	Prestin is a putative N-glycoprotein with three potential N-linked glycosylation sites.
15140192	10	71	theme	membrane	1248:1255	arg1	targeting					1257:1265	plasma membrane targeting	1241:1265	plasma membrane targeting of prestin	1241:1276	N-linked glycosylation is not required for plasma membrane targeting of prestin.
15140192	1	72	theme	motor	137:141	arg1	protein					143:149	a motor protein	135:149	a motor protein of outer hair cells (OHC) that plays a crucial role in mammalian hearing	135:222	Prestin is a motor protein of outer hair cells (OHC) that plays a crucial role in mammalian hearing.
15140192	1	72	theme	motor	137:141	arg1	Prestin					124:130	Prestin	124:130	Prestin	124:130	Prestin is a motor protein of outer hair cells (OHC) that plays a crucial role in mammalian hearing.
15140192	0	73	theme	membrane	70:77	arg1	targeting					79:87	membrane targeting	70:87	membrane targeting	70:87	N-linked glycosylation sites of the motor protein prestin: effects on membrane targeting and electrophysiological function.
15140192	4	74	dep	mutations	517:525	arg1	mutations					517:525	double-point mutations	504:525	double-point mutations (NN163/166QQ and NN163/166AA)	504:555	Therefore, the effects of N-glycosylation were investigated by producing single-point (N163Q and N166Q) or double-point mutations (NN163/166QQ and NN163/166AA) at putative N-glycosylation sites.
15140192	4	74	dep	mutations	517:525	arg1	NN163/166AA					544:554	NN163/166AA	544:554	NN163/166AA	544:554	Therefore, the effects of N-glycosylation were investigated by producing single-point (N163Q and N166Q) or double-point mutations (NN163/166QQ and NN163/166AA) at putative N-glycosylation sites.
15140192	4	74	dep	mutations	517:525	arg1	NN163/166QQ					528:538	NN163/166QQ	528:538	NN163/166QQ	528:538	Therefore, the effects of N-glycosylation were investigated by producing single-point (N163Q and N166Q) or double-point mutations (NN163/166QQ and NN163/166AA) at putative N-glycosylation sites.
15140192	7	75	link	N-linked	981:988	arg1	sites					1004:1008	N-linked glycosylation sites	981:1008	N-linked glycosylation sites at N163 and N166	981:1025	Data indicate that prestin is a glycoprotein with N-linked glycosylation sites at N163 and N166.
15140192	11	76	theme	deglycosylated	1301:1314	arg1	prestin					1316:1322	deglycosylated prestin	1301:1322	deglycosylated prestin	1301:1322	Both glycosylated and deglycosylated prestin demonstrate non-linear capacitance, a signature of prestin's motor function.
15140192	7	77	theme	N-linked	981:988	arg1	sites					1004:1008	N-linked glycosylation sites	981:1008	N-linked glycosylation sites at N163 and N166	981:1025	Data indicate that prestin is a glycoprotein with N-linked glycosylation sites at N163 and N166.
15140192	12	78	contain	has	1469:1471	arg2	function					1502:1509	altered electrophysiological function	1473:1509	altered electrophysiological function	1473:1509	Compared to glycosylated prestin, the fully de-glycosylated protein has altered electrophysiological function, with a change in membrane potential at most effective charge transfer to more depolarized values.
15140192	12	78	contain	has	1469:1471	arg1	protein					1461:1467	the fully de-glycosylated protein	1435:1467	the fully de-glycosylated protein	1435:1467	Compared to glycosylated prestin, the fully de-glycosylated protein has altered electrophysiological function, with a change in membrane potential at most effective charge transfer to more depolarized values.
15140192	0	79	theme	glycosylation	9:21	arg1	sites					23:27	N-linked glycosylation sites	0:27	N-linked glycosylation sites of the motor protein prestin: effects on membrane targeting and electrophysiological function.	0:122	N-linked glycosylation sites of the motor protein prestin: effects on membrane targeting and electrophysiological function.
15140192	0	79	theme	glycosylation	9:21	arg1	prestin					50:56	the motor protein prestin	32:56	the motor protein prestin	32:56	N-linked glycosylation sites of the motor protein prestin: effects on membrane targeting and electrophysiological function.
15140192	3	80	gly	glycosylation	337:349	arg1	prestin					388:394	prestin	388:394	prestin	388:394	It is not known whether glycosylation affects the function and activity of prestin.
15140192	0	81	theme	motor	36:40	arg1	prestin					50:56	the motor protein prestin	32:56	the motor protein prestin	32:56	N-linked glycosylation sites of the motor protein prestin: effects on membrane targeting and electrophysiological function.
15140192	4	82	theme	double-point	504:515	arg1	mutations					517:525	double-point mutations	504:525	double-point mutations (NN163/166QQ and NN163/166AA)	504:555	Therefore, the effects of N-glycosylation were investigated by producing single-point (N163Q and N166Q) or double-point mutations (NN163/166QQ and NN163/166AA) at putative N-glycosylation sites.
15140192	4	82	theme	double-point	504:515	arg1	NN163/166AA					544:554	NN163/166AA	544:554	NN163/166AA	544:554	Therefore, the effects of N-glycosylation were investigated by producing single-point (N163Q and N166Q) or double-point mutations (NN163/166QQ and NN163/166AA) at putative N-glycosylation sites.
15140192	4	82	theme	double-point	504:515	arg1	NN163/166QQ					528:538	NN163/166QQ	528:538	NN163/166QQ	528:538	Therefore, the effects of N-glycosylation were investigated by producing single-point (N163Q and N166Q) or double-point mutations (NN163/166QQ and NN163/166AA) at putative N-glycosylation sites.
15140192	8	83	contain	have	1046:1049	arg1	N163					1028:1031	N163	1028:1031	N163	1028:1031	N163 and N166 may have differential programs for synthesis and trimming of the glycans.
15140192	8	83	contain	have	1046:1049	arg2	programs					1064:1071	differential programs	1051:1071	differential programs	1051:1071	N163 and N166 may have differential programs for synthesis and trimming of the glycans.
15140192	8	83	contain	have	1046:1049	arg1	N166					1037:1040	N166	1037:1040	N166	1037:1040	N163 and N166 may have differential programs for synthesis and trimming of the glycans.
15140192	0	84	theme	prestin	50:56	arg1	sites					23:27	N-linked glycosylation sites	0:27	N-linked glycosylation sites of the motor protein prestin: effects on membrane targeting and electrophysiological function.	0:122	N-linked glycosylation sites of the motor protein prestin: effects on membrane targeting and electrophysiological function.
15140192	0	84	theme	prestin	50:56	arg1	prestin					50:56	the motor protein prestin	32:56	the motor protein prestin	32:56	N-linked glycosylation sites of the motor protein prestin: effects on membrane targeting and electrophysiological function.
15140192	12	85	theme	charge	1566:1571	arg1	transfer					1573:1580	most effective charge transfer	1551:1580	most effective charge transfer to more depolarized values	1551:1607	Compared to glycosylated prestin, the fully de-glycosylated protein has altered electrophysiological function, with a change in membrane potential at most effective charge transfer to more depolarized values.
15140192	6	86	from	effects	762:768	arg1	properties					895:904	electrophysiological properties	874:904	electrophysiological properties	874:904	We determined the effects of these manipulations on prestin's cell surface expression, molecular mass, glycosylation pattern, and electrophysiological properties in different cell-types.
15140192	6	86	from	effects	762:768	arg1	expression					819:828	prestin's cell surface expression	796:828	prestin's cell surface expression	796:828	We determined the effects of these manipulations on prestin's cell surface expression, molecular mass, glycosylation pattern, and electrophysiological properties in different cell-types.
15140192	6	86	from	effects	762:768	arg1	mass					841:844	molecular mass	831:844	molecular mass	831:844	We determined the effects of these manipulations on prestin's cell surface expression, molecular mass, glycosylation pattern, and electrophysiological properties in different cell-types.
15140192	6	86	from	effects	762:768	arg1	pattern					861:867	glycosylation pattern	847:867	glycosylation pattern	847:867	We determined the effects of these manipulations on prestin's cell surface expression, molecular mass, glycosylation pattern, and electrophysiological properties in different cell-types.
15140192	9	87	theme	greater	1146:1152	arg1	extent					1154:1159	greater extent	1146:1159	greater extent of glycosylation than its companion	1146:1195	The N166 site appears to have greater extent of glycosylation than its companion.
15140192	7	88	gly	glycoprotein	963:974	arg1	prestin					950:956	prestin	950:956	prestin	950:956	Data indicate that prestin is a glycoprotein with N-linked glycosylation sites at N163 and N166.
15140192	7	88	gly	glycoprotein	963:974	arg1	glycoprotein					963:974	a glycoprotein	961:974	a glycoprotein with N-linked glycosylation sites at N163 and N166	961:1025	Data indicate that prestin is a glycoprotein with N-linked glycosylation sites at N163 and N166.
15140192	10	89	theme	N-linked	1198:1205	arg1	glycosylation					1207:1219	N-linked glycosylation	1198:1219	N-linked glycosylation	1198:1219	N-linked glycosylation is not required for plasma membrane targeting of prestin.
15140192	12	90	from	change	1519:1524	arg1	potential					1538:1546	membrane potential	1529:1546	membrane potential	1529:1546	Compared to glycosylated prestin, the fully de-glycosylated protein has altered electrophysiological function, with a change in membrane potential at most effective charge transfer to more depolarized values.
15140192	6	91	theme	molecular	831:839	arg1	mass					841:844	molecular mass	831:844	molecular mass	831:844	We determined the effects of these manipulations on prestin's cell surface expression, molecular mass, glycosylation pattern, and electrophysiological properties in different cell-types.
15140192	2	92	gly	glycosylation	292:304	arg2	sites					306:310	three potential N-linked glycosylation sites	267:310	three potential N-linked glycosylation sites	267:310	Prestin is a putative N-glycoprotein with three potential N-linked glycosylation sites.
15140192	2	92	gly	glycosylation	292:304	arg2	three					267:271	three	267:271	three	267:271	Prestin is a putative N-glycoprotein with three potential N-linked glycosylation sites.
15140192	1	93	theme	mammalian	206:214	arg1	hearing					216:222	mammalian hearing	206:222	mammalian hearing	206:222	Prestin is a motor protein of outer hair cells (OHC) that plays a crucial role in mammalian hearing.
19167329	1	0	link	Asparagine-linked	106:122	arg1	glycosylation					124:136	Asparagine-linked glycosylation	106:136	Asparagine-linked glycosylation of polypeptides in the lumen of the endoplasmic reticulum	106:194	Asparagine-linked glycosylation of polypeptides in the lumen of the endoplasmic reticulum is catalyzed by the hetero-oligomeric oligosaccharyltransferase (OST).
19167329	1	1	theme	reticulum	186:194	arg1	lumen					161:165	the lumen	157:165	the lumen of the endoplasmic reticulum	157:194	Asparagine-linked glycosylation of polypeptides in the lumen of the endoplasmic reticulum is catalyzed by the hetero-oligomeric oligosaccharyltransferase (OST).
19167329	4	2	theme	polypeptide	650:660	arg1	glycosylation					621:633	cotranslational glycosylation	605:633	cotranslational glycosylation of the nascent polypeptide	605:660	The STT3A OST isoform is primarily responsible for cotranslational glycosylation of the nascent polypeptide as it enters the lumen of the endoplasmic reticulum.
19167329	5	3	theme	STT3B	719:723	arg1	isoform					725:731	The STT3B isoform	715:731	The STT3B isoform	715:731	The STT3B isoform is required for efficient cotranslational glycosylation of an acceptor site adjacent to the N-terminal signal sequence of a secreted protein.
19167329	5	4	theme	protein	866:872	arg1	sequence					843:850	the N-terminal signal sequence	821:850	the N-terminal signal sequence of a secreted protein	821:872	The STT3B isoform is required for efficient cotranslational glycosylation of an acceptor site adjacent to the N-terminal signal sequence of a secreted protein.
19167329	4	5	theme	nascent	642:648	arg1	polypeptide					650:660	the nascent polypeptide	638:660	the nascent polypeptide	638:660	The STT3A OST isoform is primarily responsible for cotranslational glycosylation of the nascent polypeptide as it enters the lumen of the endoplasmic reticulum.
19167329	1	6	gly	glycosylation	124:136	arg1	lumen					161:165	the lumen	157:165	the lumen of the endoplasmic reticulum	157:194	Asparagine-linked glycosylation of polypeptides in the lumen of the endoplasmic reticulum is catalyzed by the hetero-oligomeric oligosaccharyltransferase (OST).
19167329	1	6	gly	glycosylation	124:136	arg1	polypeptides					141:152	polypeptides	141:152	polypeptides	141:152	Asparagine-linked glycosylation of polypeptides in the lumen of the endoplasmic reticulum is catalyzed by the hetero-oligomeric oligosaccharyltransferase (OST).
19167329	4	7	theme	OST	564:566	arg1	responsible					589:599	responsible	589:599	responsible	589:599	The STT3A OST isoform is primarily responsible for cotranslational glycosylation of the nascent polypeptide as it enters the lumen of the endoplasmic reticulum.
19167329	4	7	theme	OST	564:566	arg1	isoform					568:574	The STT3A OST isoform	554:574	The STT3A OST isoform	554:574	The STT3A OST isoform is primarily responsible for cotranslational glycosylation of the nascent polypeptide as it enters the lumen of the endoplasmic reticulum.
19167329	5	8	theme	adjacent	809:816	arg1	site					804:807	an acceptor site	792:807	an acceptor site adjacent to the N-terminal signal sequence of a secreted protein	792:872	The STT3B isoform is required for efficient cotranslational glycosylation of an acceptor site adjacent to the N-terminal signal sequence of a secreted protein.
19167329	6	9	theme	unfolded	996:1003	arg1	protein					1005:1011	an unfolded protein	993:1011	an unfolded protein	993:1011	Unlike STT3A, STT3B efficiently mediates posttranslational glycosylation of a carboxyl-terminal glycosylation site in an unfolded protein.
19167329	7	10	theme	OST	1061:1063	arg1	isoforms					1065:1072	the OST isoforms	1057:1072	the OST isoforms	1057:1072	These distinct and complementary roles for the OST isoforms allow sequential scanning of polypeptides for acceptor sites to insure the maximal efficiency of N-glycosylation.
19167329	6	11	gly	glycosylation	934:946	arg1	site					985:988	a carboxyl-terminal glycosylation site	951:988	a carboxyl-terminal glycosylation site in an unfolded protein	951:1011	Unlike STT3A, STT3B efficiently mediates posttranslational glycosylation of a carboxyl-terminal glycosylation site in an unfolded protein.
19167329	3	12	theme	OST	474:476	arg1	isoforms					478:485	the OST isoforms	470:485	the OST isoforms	470:485	Using siRNA to achieve isoform-specific knockdowns, we show that the OST isoforms cooperate and act sequentially to mediate protein N-glycosylation.
19167329	3	13	theme	isoform-specific	428:443	arg1	knockdowns					445:454	isoform-specific knockdowns	428:454	isoform-specific knockdowns	428:454	Using siRNA to achieve isoform-specific knockdowns, we show that the OST isoforms cooperate and act sequentially to mediate protein N-glycosylation.
19167329	6	14	theme	site	985:988	arg1	glycosylation					934:946	posttranslational glycosylation	916:946	posttranslational glycosylation of a carboxyl-terminal glycosylation site in an unfolded protein	916:1011	Unlike STT3A, STT3B efficiently mediates posttranslational glycosylation of a carboxyl-terminal glycosylation site in an unfolded protein.
19167329	5	15	theme	N-terminal	825:834	arg1	sequence					843:850	the N-terminal signal sequence	821:850	the N-terminal signal sequence of a secreted protein	821:872	The STT3B isoform is required for efficient cotranslational glycosylation of an acceptor site adjacent to the N-terminal signal sequence of a secreted protein.
19167329	1	16	theme	Asparagine-linked	106:122	arg1	glycosylation					124:136	Asparagine-linked glycosylation	106:136	Asparagine-linked glycosylation of polypeptides in the lumen of the endoplasmic reticulum	106:194	Asparagine-linked glycosylation of polypeptides in the lumen of the endoplasmic reticulum is catalyzed by the hetero-oligomeric oligosaccharyltransferase (OST).
19167329	0	17	theme	Cotranslational	0:14	arg1	N-glycosylation					38:52	Cotranslational and posttranslational N-glycosylation	0:52	Cotranslational and posttranslational N-glycosylation of polypeptides by distinct mammalian OST isoforms.	0:104	Cotranslational and posttranslational N-glycosylation of polypeptides by distinct mammalian OST isoforms.
19167329	2	18	theme	enzymatic	348:356	arg1	properties					358:367	distinct enzymatic properties	339:367	distinct enzymatic properties	339:367	OST isoforms with different catalytic subunits (STT3A versus STT3B) and distinct enzymatic properties are coexpressed in mammalian cells.
19167329	1	19	theme	hetero-oligomeric	216:232	arg1	OST					261:263	OST	261:263	OST	261:263	Asparagine-linked glycosylation of polypeptides in the lumen of the endoplasmic reticulum is catalyzed by the hetero-oligomeric oligosaccharyltransferase (OST).
19167329	1	19	theme	hetero-oligomeric	216:232	arg1	oligosaccharyltransferase					234:258	the hetero-oligomeric oligosaccharyltransferase	212:258	the hetero-oligomeric oligosaccharyltransferase (OST)	212:264	Asparagine-linked glycosylation of polypeptides in the lumen of the endoplasmic reticulum is catalyzed by the hetero-oligomeric oligosaccharyltransferase (OST).
19167329	6	20	from	glycosylation	934:946	arg1	protein					1005:1011	an unfolded protein	993:1011	an unfolded protein	993:1011	Unlike STT3A, STT3B efficiently mediates posttranslational glycosylation of a carboxyl-terminal glycosylation site in an unfolded protein.
19167329	4	21	theme	cotranslational	605:619	arg1	glycosylation					621:633	cotranslational glycosylation	605:633	cotranslational glycosylation of the nascent polypeptide	605:660	The STT3A OST isoform is primarily responsible for cotranslational glycosylation of the nascent polypeptide as it enters the lumen of the endoplasmic reticulum.
19167329	7	22	theme	complementary	1033:1045	arg1	roles					1047:1051	These distinct and complementary roles	1014:1051	These distinct and complementary roles for the OST isoforms	1014:1072	These distinct and complementary roles for the OST isoforms allow sequential scanning of polypeptides for acceptor sites to insure the maximal efficiency of N-glycosylation.
19167329	2	23	theme	distinct	339:346	arg1	properties					358:367	distinct enzymatic properties	339:367	distinct enzymatic properties	339:367	OST isoforms with different catalytic subunits (STT3A versus STT3B) and distinct enzymatic properties are coexpressed in mammalian cells.
19167329	6	24	gly	glycosylation	971:983	arg2	site					985:988	a carboxyl-terminal glycosylation site	951:988	a carboxyl-terminal glycosylation site in an unfolded protein	951:1011	Unlike STT3A, STT3B efficiently mediates posttranslational glycosylation of a carboxyl-terminal glycosylation site in an unfolded protein.
19167329	4	25	theme	endoplasmic	692:702	arg1	reticulum					704:712	the endoplasmic reticulum	688:712	the endoplasmic reticulum	688:712	The STT3A OST isoform is primarily responsible for cotranslational glycosylation of the nascent polypeptide as it enters the lumen of the endoplasmic reticulum.
19167329	0	26	theme	posttranslational	20:36	arg1	N-glycosylation					38:52	Cotranslational and posttranslational N-glycosylation	0:52	Cotranslational and posttranslational N-glycosylation of polypeptides by distinct mammalian OST isoforms.	0:104	Cotranslational and posttranslational N-glycosylation of polypeptides by distinct mammalian OST isoforms.
19167329	6	27	theme	glycosylation	971:983	arg1	site					985:988	a carboxyl-terminal glycosylation site	951:988	a carboxyl-terminal glycosylation site in an unfolded protein	951:1011	Unlike STT3A, STT3B efficiently mediates posttranslational glycosylation of a carboxyl-terminal glycosylation site in an unfolded protein.
19167329	1	28	theme	polypeptides	141:152	arg1	glycosylation					124:136	Asparagine-linked glycosylation	106:136	Asparagine-linked glycosylation of polypeptides in the lumen of the endoplasmic reticulum	106:194	Asparagine-linked glycosylation of polypeptides in the lumen of the endoplasmic reticulum is catalyzed by the hetero-oligomeric oligosaccharyltransferase (OST).
19167329	0	29	theme	polypeptides	57:68	arg1	N-glycosylation					38:52	Cotranslational and posttranslational N-glycosylation	0:52	Cotranslational and posttranslational N-glycosylation of polypeptides by distinct mammalian OST isoforms.	0:104	Cotranslational and posttranslational N-glycosylation of polypeptides by distinct mammalian OST isoforms.
19167329	2	30	with	isoforms	271:278	arg1	subunits					305:312	different catalytic subunits	285:312	different catalytic subunits (STT3A versus STT3B)	285:333	OST isoforms with different catalytic subunits (STT3A versus STT3B) and distinct enzymatic properties are coexpressed in mammalian cells.
19167329	2	30	with	isoforms	271:278	arg1	properties					358:367	distinct enzymatic properties	339:367	distinct enzymatic properties	339:367	OST isoforms with different catalytic subunits (STT3A versus STT3B) and distinct enzymatic properties are coexpressed in mammalian cells.
19167329	6	31	theme	carboxyl-terminal	953:969	arg1	site					985:988	a carboxyl-terminal glycosylation site	951:988	a carboxyl-terminal glycosylation site in an unfolded protein	951:1011	Unlike STT3A, STT3B efficiently mediates posttranslational glycosylation of a carboxyl-terminal glycosylation site in an unfolded protein.
19167329	2	32	dep	subunits	305:312	arg1	STT3B					328:332	STT3B	328:332	STT3B	328:332	OST isoforms with different catalytic subunits (STT3A versus STT3B) and distinct enzymatic properties are coexpressed in mammalian cells.
19167329	2	32	dep	subunits	305:312	arg1	STT3A					315:319	STT3A	315:319	STT3A	315:319	OST isoforms with different catalytic subunits (STT3A versus STT3B) and distinct enzymatic properties are coexpressed in mammalian cells.
19167329	5	33	theme	secreted	857:864	arg1	protein					866:872	a secreted protein	855:872	a secreted protein	855:872	The STT3B isoform is required for efficient cotranslational glycosylation of an acceptor site adjacent to the N-terminal signal sequence of a secreted protein.
19167329	5	34	theme	acceptor	795:802	arg1	site					804:807	an acceptor site	792:807	an acceptor site adjacent to the N-terminal signal sequence of a secreted protein	792:872	The STT3B isoform is required for efficient cotranslational glycosylation of an acceptor site adjacent to the N-terminal signal sequence of a secreted protein.
19167329	4	35	theme	reticulum	704:712	arg1	lumen					679:683	the lumen	675:683	the lumen of the endoplasmic reticulum	675:712	The STT3A OST isoform is primarily responsible for cotranslational glycosylation of the nascent polypeptide as it enters the lumen of the endoplasmic reticulum.
19167329	0	36	theme	distinct	73:80	arg1	isoforms					96:103	distinct mammalian OST isoforms	73:103	distinct mammalian OST isoforms	73:103	Cotranslational and posttranslational N-glycosylation of polypeptides by distinct mammalian OST isoforms.
19167329	5	37	theme	site	804:807	arg1	glycosylation					775:787	efficient cotranslational glycosylation	749:787	efficient cotranslational glycosylation of an acceptor site adjacent to the N-terminal signal sequence of a secreted protein	749:872	The STT3B isoform is required for efficient cotranslational glycosylation of an acceptor site adjacent to the N-terminal signal sequence of a secreted protein.
19167329	7	38	theme	maximal	1149:1155	arg1	efficiency					1157:1166	the maximal efficiency	1145:1166	the maximal efficiency of N-glycosylation	1145:1185	These distinct and complementary roles for the OST isoforms allow sequential scanning of polypeptides for acceptor sites to insure the maximal efficiency of N-glycosylation.
19167329	5	39	theme	signal	836:841	arg1	sequence					843:850	the N-terminal signal sequence	821:850	the N-terminal signal sequence of a secreted protein	821:872	The STT3B isoform is required for efficient cotranslational glycosylation of an acceptor site adjacent to the N-terminal signal sequence of a secreted protein.
19167329	2	40	theme	OST	267:269	arg1	isoforms					271:278	OST isoforms	267:278	OST isoforms with different catalytic subunits (STT3A versus STT3B) and distinct enzymatic properties	267:367	OST isoforms with different catalytic subunits (STT3A versus STT3B) and distinct enzymatic properties are coexpressed in mammalian cells.
19167329	4	41	gly	glycosylation	621:633	arg1	polypeptide					650:660	the nascent polypeptide	638:660	the nascent polypeptide	638:660	The STT3A OST isoform is primarily responsible for cotranslational glycosylation of the nascent polypeptide as it enters the lumen of the endoplasmic reticulum.
19167329	2	42	theme	mammalian	388:396	arg1	cells					398:402	mammalian cells	388:402	mammalian cells	388:402	OST isoforms with different catalytic subunits (STT3A versus STT3B) and distinct enzymatic properties are coexpressed in mammalian cells.
19167329	7	43	theme	N-glycosylation	1171:1185	arg1	efficiency					1157:1166	the maximal efficiency	1145:1166	the maximal efficiency of N-glycosylation	1145:1185	These distinct and complementary roles for the OST isoforms allow sequential scanning of polypeptides for acceptor sites to insure the maximal efficiency of N-glycosylation.
19167329	0	44	gly	N-glycosylation	38:52	arg1	polypeptides					57:68	polypeptides	57:68	polypeptides	57:68	Cotranslational and posttranslational N-glycosylation of polypeptides by distinct mammalian OST isoforms.
19167329	5	45	gly	glycosylation	775:787	arg1	site					804:807	an acceptor site	792:807	an acceptor site adjacent to the N-terminal signal sequence of a secreted protein	792:872	The STT3B isoform is required for efficient cotranslational glycosylation of an acceptor site adjacent to the N-terminal signal sequence of a secreted protein.
19167329	6	46	from	protein	1005:1011	arg1	glycosylation					934:946	posttranslational glycosylation	916:946	posttranslational glycosylation of a carboxyl-terminal glycosylation site in an unfolded protein	916:1011	Unlike STT3A, STT3B efficiently mediates posttranslational glycosylation of a carboxyl-terminal glycosylation site in an unfolded protein.
19167329	5	47	theme	efficient	749:757	arg1	glycosylation					775:787	efficient cotranslational glycosylation	749:787	efficient cotranslational glycosylation of an acceptor site adjacent to the N-terminal signal sequence of a secreted protein	749:872	The STT3B isoform is required for efficient cotranslational glycosylation of an acceptor site adjacent to the N-terminal signal sequence of a secreted protein.
19167329	6	48	theme	posttranslational	916:932	arg1	glycosylation					934:946	posttranslational glycosylation	916:946	posttranslational glycosylation of a carboxyl-terminal glycosylation site in an unfolded protein	916:1011	Unlike STT3A, STT3B efficiently mediates posttranslational glycosylation of a carboxyl-terminal glycosylation site in an unfolded protein.
19167329	7	49	theme	acceptor	1120:1127	arg1	sites					1129:1133	acceptor sites	1120:1133	acceptor sites	1120:1133	These distinct and complementary roles for the OST isoforms allow sequential scanning of polypeptides for acceptor sites to insure the maximal efficiency of N-glycosylation.
19167329	7	50	theme	distinct	1020:1027	arg1	roles					1047:1051	These distinct and complementary roles	1014:1051	These distinct and complementary roles for the OST isoforms	1014:1072	These distinct and complementary roles for the OST isoforms allow sequential scanning of polypeptides for acceptor sites to insure the maximal efficiency of N-glycosylation.
19167329	5	51	theme	cotranslational	759:773	arg1	glycosylation					775:787	efficient cotranslational glycosylation	749:787	efficient cotranslational glycosylation of an acceptor site adjacent to the N-terminal signal sequence of a secreted protein	749:872	The STT3B isoform is required for efficient cotranslational glycosylation of an acceptor site adjacent to the N-terminal signal sequence of a secreted protein.
19167329	3	52	theme	protein	529:535	arg1	N-glycosylation					537:551	protein N-glycosylation	529:551	protein N-glycosylation	529:551	Using siRNA to achieve isoform-specific knockdowns, we show that the OST isoforms cooperate and act sequentially to mediate protein N-glycosylation.
19167329	0	53	theme	OST	92:94	arg1	isoforms					96:103	distinct mammalian OST isoforms	73:103	distinct mammalian OST isoforms	73:103	Cotranslational and posttranslational N-glycosylation of polypeptides by distinct mammalian OST isoforms.
19167329	2	54	theme	catalytic	295:303	arg1	subunits					305:312	different catalytic subunits	285:312	different catalytic subunits (STT3A versus STT3B)	285:333	OST isoforms with different catalytic subunits (STT3A versus STT3B) and distinct enzymatic properties are coexpressed in mammalian cells.
19167329	7	55	theme	polypeptides	1103:1114	arg1	scanning					1091:1098	sequential scanning	1080:1098	sequential scanning of polypeptides for acceptor sites	1080:1133	These distinct and complementary roles for the OST isoforms allow sequential scanning of polypeptides for acceptor sites to insure the maximal efficiency of N-glycosylation.
19167329	1	56	from	glycosylation	124:136	arg1	lumen					161:165	the lumen	157:165	the lumen of the endoplasmic reticulum	157:194	Asparagine-linked glycosylation of polypeptides in the lumen of the endoplasmic reticulum is catalyzed by the hetero-oligomeric oligosaccharyltransferase (OST).
19167329	0	57	theme	mammalian	82:90	arg1	isoforms					96:103	distinct mammalian OST isoforms	73:103	distinct mammalian OST isoforms	73:103	Cotranslational and posttranslational N-glycosylation of polypeptides by distinct mammalian OST isoforms.
19167329	4	58	theme	STT3A	558:562	arg1	responsible					589:599	responsible	589:599	responsible	589:599	The STT3A OST isoform is primarily responsible for cotranslational glycosylation of the nascent polypeptide as it enters the lumen of the endoplasmic reticulum.
19167329	4	58	theme	STT3A	558:562	arg1	isoform					568:574	The STT3A OST isoform	554:574	The STT3A OST isoform	554:574	The STT3A OST isoform is primarily responsible for cotranslational glycosylation of the nascent polypeptide as it enters the lumen of the endoplasmic reticulum.
19167329	2	59	theme	different	285:293	arg1	subunits					305:312	different catalytic subunits	285:312	different catalytic subunits (STT3A versus STT3B)	285:333	OST isoforms with different catalytic subunits (STT3A versus STT3B) and distinct enzymatic properties are coexpressed in mammalian cells.
19167329	7	60	theme	sequential	1080:1089	arg1	scanning					1091:1098	sequential scanning	1080:1098	sequential scanning of polypeptides for acceptor sites	1080:1133	These distinct and complementary roles for the OST isoforms allow sequential scanning of polypeptides for acceptor sites to insure the maximal efficiency of N-glycosylation.
19167329	1	61	theme	endoplasmic	174:184	arg1	reticulum					186:194	the endoplasmic reticulum	170:194	the endoplasmic reticulum	170:194	Asparagine-linked glycosylation of polypeptides in the lumen of the endoplasmic reticulum is catalyzed by the hetero-oligomeric oligosaccharyltransferase (OST).
19167329	6	62	from	site	985:988	arg1	protein					1005:1011	an unfolded protein	993:1011	an unfolded protein	993:1011	Unlike STT3A, STT3B efficiently mediates posttranslational glycosylation of a carboxyl-terminal glycosylation site in an unfolded protein.
16321355	0	0	theme	human	42:46	arg1	ceruloplasmin					55:67	human plasma ceruloplasmin	42:67	human plasma ceruloplasmin	42:67	Site-specific N-glycosylation analysis of human plasma ceruloplasmin using liquid chromatography with electrospray ionization tandem mass spectrometry.
16321355	8	1	theme	antennas	1542:1549	arg1	one					1531:1533	one	1531:1533	one	1531:1533	Exoglycosidase digestion suggested that fucose residues were linked to reducing end GlcNAc in biantennary oligosaccharides and to reducing end and/or alpha1-3 to outer arms GlcNAc in triantennary oligosaccharides and that roughly one of the antennas in triantennary oligosaccharides was alpha2-3 sialylated and occasionally alpha1-3 fucosylated at GlcNAc.
16321355	8	1	theme	antennas	1542:1549	arg1	antennas					1542:1549	the antennas	1538:1549	the antennas in triantennary oligosaccharides	1538:1582	Exoglycosidase digestion suggested that fucose residues were linked to reducing end GlcNAc in biantennary oligosaccharides and to reducing end and/or alpha1-3 to outer arms GlcNAc in triantennary oligosaccharides and that roughly one of the antennas in triantennary oligosaccharides was alpha2-3 sialylated and occasionally alpha1-3 fucosylated at GlcNAc.
16321355	6	2	theme	fucose	1197:1202	arg1	residues					1204:1211	fucose residues	1197:1211	fucose residues (0, 1, or 2)	1197:1224	Of the seven potential N-glycosylation sites, four (Asn119, Asn339, Asn378, and Asn743) were occupied by a sialylated biantennary or triantennary oligosaccharide with fucose residues (0, 1, or 2).
16321355	4	3	theme	carbohydrate	665:676	arg1	m/z					694:696	m/z 204	694:700	m/z 204 (HexNAc)	694:709	Product ion spectra acquired data-dependently were used for both distinction of the glycopeptides from the peptides using the carbohydrate B-ions, such as m/z 204 (HexNAc) and m/z 366 (HexHexNAc), and identification of the peptide moiety of the glycopeptide based on the presence of the b- and y-series ions derived from the peptide.
16321355	4	3	theme	carbohydrate	665:676	arg1	m/z					715:717	m/z 366	715:721	m/z 366 (HexHexNAc)	715:733	Product ion spectra acquired data-dependently were used for both distinction of the glycopeptides from the peptides using the carbohydrate B-ions, such as m/z 204 (HexNAc) and m/z 366 (HexHexNAc), and identification of the peptide moiety of the glycopeptide based on the presence of the b- and y-series ions derived from the peptide.
16321355	4	3	theme	carbohydrate	665:676	arg1	B-ions					678:683	the carbohydrate B-ions	661:683	the carbohydrate B-ions	661:683	Product ion spectra acquired data-dependently were used for both distinction of the glycopeptides from the peptides using the carbohydrate B-ions, such as m/z 204 (HexNAc) and m/z 366 (HexHexNAc), and identification of the peptide moiety of the glycopeptide based on the presence of the b- and y-series ions derived from the peptide.
16321355	8	4	theme	reducing	1372:1379	arg1	GlcNAc					1385:1390	reducing end GlcNAc	1372:1390	reducing end GlcNAc	1372:1390	Exoglycosidase digestion suggested that fucose residues were linked to reducing end GlcNAc in biantennary oligosaccharides and to reducing end and/or alpha1-3 to outer arms GlcNAc in triantennary oligosaccharides and that roughly one of the antennas in triantennary oligosaccharides was alpha2-3 sialylated and occasionally alpha1-3 fucosylated at GlcNAc.
16321355	6	5	dep	sialylated	1137:1146	arg1	biantennary					1148:1158	biantennary	1148:1158	biantennary	1148:1158	Of the seven potential N-glycosylation sites, four (Asn119, Asn339, Asn378, and Asn743) were occupied by a sialylated biantennary or triantennary oligosaccharide with fucose residues (0, 1, or 2).
16321355	6	5	dep	sialylated	1137:1146	arg1	triantennary					1163:1174	triantennary	1163:1174	triantennary	1163:1174	Of the seven potential N-glycosylation sites, four (Asn119, Asn339, Asn378, and Asn743) were occupied by a sialylated biantennary or triantennary oligosaccharide with fucose residues (0, 1, or 2).
16321355	2	6	theme	ceruloplasmin	302:314	arg1	analysis					284:291	a site-specific glycosylation analysis	254:291	a site-specific glycosylation analysis of human ceruloplasmin (CP)	254:319	In this study, a site-specific glycosylation analysis of human ceruloplasmin (CP) was carried out using reversed-phase high-performance liquid chromatography with electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS).
16321355	1	7	theme	iron	222:225	arg1	metabolism					227:236	iron metabolism	222:236	iron metabolism	222:236	Ceruloplasmin has ferroxidase activity and plays an essential role in iron metabolism.
16321355	6	8	theme	sialylated	1137:1146	arg1	oligosaccharide					1176:1190	a sialylated biantennary or triantennary oligosaccharide	1135:1190	a sialylated biantennary or triantennary oligosaccharide with fucose residues (0, 1, or 2)	1135:1224	Of the seven potential N-glycosylation sites, four (Asn119, Asn339, Asn378, and Asn743) were occupied by a sialylated biantennary or triantennary oligosaccharide with fucose residues (0, 1, or 2).
16321355	6	9	gly	sialylated	1137:1146	arg1	oligosaccharide					1176:1190	a sialylated biantennary or triantennary oligosaccharide	1135:1190	a sialylated biantennary or triantennary oligosaccharide with fucose residues (0, 1, or 2)	1135:1224	Of the seven potential N-glycosylation sites, four (Asn119, Asn339, Asn378, and Asn743) were occupied by a sialylated biantennary or triantennary oligosaccharide with fucose residues (0, 1, or 2).
16321355	8	10	theme	outer	1463:1467	arg1	GlcNAc					1474:1479	outer arms GlcNAc	1463:1479	outer arms GlcNAc in triantennary oligosaccharides	1463:1512	Exoglycosidase digestion suggested that fucose residues were linked to reducing end GlcNAc in biantennary oligosaccharides and to reducing end and/or alpha1-3 to outer arms GlcNAc in triantennary oligosaccharides and that roughly one of the antennas in triantennary oligosaccharides was alpha2-3 sialylated and occasionally alpha1-3 fucosylated at GlcNAc.
16321355	5	11	theme	observed	959:966	arg1	mass					968:971	the observed mass	955:971	the observed mass of the glycopeptide and theoretical mass of the peptide	955:1027	Oligosaccharide composition was deduced from the molecular weight calculated from the observed mass of the glycopeptide and theoretical mass of the peptide.
16321355	6	12	theme	potential	1043:1051	arg1	sites					1069:1073	the seven potential N-glycosylation sites	1033:1073	the seven potential N-glycosylation sites	1033:1073	Of the seven potential N-glycosylation sites, four (Asn119, Asn339, Asn378, and Asn743) were occupied by a sialylated biantennary or triantennary oligosaccharide with fucose residues (0, 1, or 2).
16321355	8	13	theme	triantennary	1484:1495	arg1	oligosaccharides					1497:1512	triantennary oligosaccharides	1484:1512	triantennary oligosaccharides	1484:1512	Exoglycosidase digestion suggested that fucose residues were linked to reducing end GlcNAc in biantennary oligosaccharides and to reducing end and/or alpha1-3 to outer arms GlcNAc in triantennary oligosaccharides and that roughly one of the antennas in triantennary oligosaccharides was alpha2-3 sialylated and occasionally alpha1-3 fucosylated at GlcNAc.
16321355	0	14	theme	liquid	75:80	arg1	chromatography					82:95	liquid chromatography	75:95	liquid chromatography	75:95	Site-specific N-glycosylation analysis of human plasma ceruloplasmin using liquid chromatography with electrospray ionization tandem mass spectrometry.
16321355	2	15	theme	glycosylation	270:282	arg1	analysis					284:291	a site-specific glycosylation analysis	254:291	a site-specific glycosylation analysis of human ceruloplasmin (CP)	254:319	In this study, a site-specific glycosylation analysis of human ceruloplasmin (CP) was carried out using reversed-phase high-performance liquid chromatography with electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS).
16321355	6	16	used	occupied	1123:1130	arg2	four					1076:1079	four	1076:1079	four	1076:1079	Of the seven potential N-glycosylation sites, four (Asn119, Asn339, Asn378, and Asn743) were occupied by a sialylated biantennary or triantennary oligosaccharide with fucose residues (0, 1, or 2).
16321355	8	17	attach	linked	1362:1367	arg1	alpha1-3					1451:1458	alpha1-3	1451:1458	alpha1-3	1451:1458	Exoglycosidase digestion suggested that fucose residues were linked to reducing end GlcNAc in biantennary oligosaccharides and to reducing end and/or alpha1-3 to outer arms GlcNAc in triantennary oligosaccharides and that roughly one of the antennas in triantennary oligosaccharides was alpha2-3 sialylated and occasionally alpha1-3 fucosylated at GlcNAc.
16321355	8	17	attach	linked	1362:1367	arg1	end					1440:1442	reducing end	1431:1442	reducing end	1431:1442	Exoglycosidase digestion suggested that fucose residues were linked to reducing end GlcNAc in biantennary oligosaccharides and to reducing end and/or alpha1-3 to outer arms GlcNAc in triantennary oligosaccharides and that roughly one of the antennas in triantennary oligosaccharides was alpha2-3 sialylated and occasionally alpha1-3 fucosylated at GlcNAc.
16321355	8	17	attach	linked	1362:1367	arg3	oligosaccharides					1407:1422	biantennary oligosaccharides	1395:1422	biantennary oligosaccharides	1395:1422	Exoglycosidase digestion suggested that fucose residues were linked to reducing end GlcNAc in biantennary oligosaccharides and to reducing end and/or alpha1-3 to outer arms GlcNAc in triantennary oligosaccharides and that roughly one of the antennas in triantennary oligosaccharides was alpha2-3 sialylated and occasionally alpha1-3 fucosylated at GlcNAc.
16321355	8	17	attach	linked	1362:1367	arg2	residues					1348:1355	fucose residues	1341:1355	fucose residues	1341:1355	Exoglycosidase digestion suggested that fucose residues were linked to reducing end GlcNAc in biantennary oligosaccharides and to reducing end and/or alpha1-3 to outer arms GlcNAc in triantennary oligosaccharides and that roughly one of the antennas in triantennary oligosaccharides was alpha2-3 sialylated and occasionally alpha1-3 fucosylated at GlcNAc.
16321355	8	17	attach	linked	1362:1367	arg1	GlcNAc					1385:1390	reducing end GlcNAc	1372:1390	reducing end GlcNAc	1372:1390	Exoglycosidase digestion suggested that fucose residues were linked to reducing end GlcNAc in biantennary oligosaccharides and to reducing end and/or alpha1-3 to outer arms GlcNAc in triantennary oligosaccharides and that roughly one of the antennas in triantennary oligosaccharides was alpha2-3 sialylated and occasionally alpha1-3 fucosylated at GlcNAc.
16321355	0	18	theme	ionization	115:124	arg1	spectrometry					138:149	electrospray ionization tandem mass spectrometry	102:149	electrospray ionization tandem mass spectrometry	102:149	Site-specific N-glycosylation analysis of human plasma ceruloplasmin using liquid chromatography with electrospray ionization tandem mass spectrometry.
16321355	5	19	theme	theoretical	997:1007	arg1	mass					1009:1012	the glycopeptide and theoretical mass	976:1012	the glycopeptide and theoretical mass of the peptide	976:1027	Oligosaccharide composition was deduced from the molecular weight calculated from the observed mass of the glycopeptide and theoretical mass of the peptide.
16321355	1	20	theme	ferroxidase	170:180	arg1	activity					182:189	ferroxidase activity	170:189	ferroxidase activity	170:189	Ceruloplasmin has ferroxidase activity and plays an essential role in iron metabolism.
16321355	5	21	gly	glycopeptide	980:991	arg2	glycopeptide					980:991	glycopeptide	980:991	glycopeptide	980:991	Oligosaccharide composition was deduced from the molecular weight calculated from the observed mass of the glycopeptide and theoretical mass of the peptide.
16321355	3	22	theme	carboxymethylated	487:503	arg1	CP					505:506	carboxymethylated CP	487:506	carboxymethylated CP	487:506	A tryptic digest of carboxymethylated CP was subjected to LC-ESI-MS/MS.
16321355	0	23	theme	mass	133:136	arg1	spectrometry					138:149	electrospray ionization tandem mass spectrometry	102:149	electrospray ionization tandem mass spectrometry	102:149	Site-specific N-glycosylation analysis of human plasma ceruloplasmin using liquid chromatography with electrospray ionization tandem mass spectrometry.
16321355	4	24	theme	ion	547:549	arg1	spectra					551:557	Product ion spectra	539:557	Product ion spectra acquired data-dependently	539:583	Product ion spectra acquired data-dependently were used for both distinction of the glycopeptides from the peptides using the carbohydrate B-ions, such as m/z 204 (HexNAc) and m/z 366 (HexHexNAc), and identification of the peptide moiety of the glycopeptide based on the presence of the b- and y-series ions derived from the peptide.
16321355	4	25	theme	moiety	770:775	arg1	identification					740:753	identification	740:753	identification of the peptide moiety of the glycopeptide based on the presence of the b- and y-series ions derived from the peptide	740:870	Product ion spectra acquired data-dependently were used for both distinction of the glycopeptides from the peptides using the carbohydrate B-ions, such as m/z 204 (HexNAc) and m/z 366 (HexHexNAc), and identification of the peptide moiety of the glycopeptide based on the presence of the b- and y-series ions derived from the peptide.
16321355	4	25	theme	moiety	770:775	arg1	m/z					694:696	m/z 204	694:700	m/z 204 (HexNAc)	694:709	Product ion spectra acquired data-dependently were used for both distinction of the glycopeptides from the peptides using the carbohydrate B-ions, such as m/z 204 (HexNAc) and m/z 366 (HexHexNAc), and identification of the peptide moiety of the glycopeptide based on the presence of the b- and y-series ions derived from the peptide.
16321355	4	25	theme	moiety	770:775	arg1	m/z					715:717	m/z 366	715:721	m/z 366 (HexHexNAc)	715:733	Product ion spectra acquired data-dependently were used for both distinction of the glycopeptides from the peptides using the carbohydrate B-ions, such as m/z 204 (HexNAc) and m/z 366 (HexHexNAc), and identification of the peptide moiety of the glycopeptide based on the presence of the b- and y-series ions derived from the peptide.
16321355	4	25	theme	moiety	770:775	arg1	B-ions					678:683	the carbohydrate B-ions	661:683	the carbohydrate B-ions	661:683	Product ion spectra acquired data-dependently were used for both distinction of the glycopeptides from the peptides using the carbohydrate B-ions, such as m/z 204 (HexNAc) and m/z 366 (HexHexNAc), and identification of the peptide moiety of the glycopeptide based on the presence of the b- and y-series ions derived from the peptide.
16321355	0	26	theme	Site-specific	0:12	arg1	analysis					30:37	Site-specific N-glycosylation analysis	0:37	Site-specific N-glycosylation analysis of human plasma ceruloplasmin	0:67	Site-specific N-glycosylation analysis of human plasma ceruloplasmin using liquid chromatography with electrospray ionization tandem mass spectrometry.
16321355	8	27	theme	triantennary	1554:1565	arg1	oligosaccharides					1567:1582	triantennary oligosaccharides	1554:1582	triantennary oligosaccharides	1554:1582	Exoglycosidase digestion suggested that fucose residues were linked to reducing end GlcNAc in biantennary oligosaccharides and to reducing end and/or alpha1-3 to outer arms GlcNAc in triantennary oligosaccharides and that roughly one of the antennas in triantennary oligosaccharides was alpha2-3 sialylated and occasionally alpha1-3 fucosylated at GlcNAc.
16321355	4	28	theme	y-series	833:840	arg1	ions					842:845	the b- and y-series ions	822:845	ions	842:845	Product ion spectra acquired data-dependently were used for both distinction of the glycopeptides from the peptides using the carbohydrate B-ions, such as m/z 204 (HexNAc) and m/z 366 (HexHexNAc), and identification of the peptide moiety of the glycopeptide based on the presence of the b- and y-series ions derived from the peptide.
16321355	5	29	theme	glycopeptide	980:991	arg1	mass					1009:1012	the glycopeptide and theoretical mass	976:1012	the glycopeptide and theoretical mass of the peptide	976:1027	Oligosaccharide composition was deduced from the molecular weight calculated from the observed mass of the glycopeptide and theoretical mass of the peptide.
16321355	8	30	theme	biantennary	1395:1405	arg1	oligosaccharides					1407:1422	biantennary oligosaccharides	1395:1422	biantennary oligosaccharides	1395:1422	Exoglycosidase digestion suggested that fucose residues were linked to reducing end GlcNAc in biantennary oligosaccharides and to reducing end and/or alpha1-3 to outer arms GlcNAc in triantennary oligosaccharides and that roughly one of the antennas in triantennary oligosaccharides was alpha2-3 sialylated and occasionally alpha1-3 fucosylated at GlcNAc.
16321355	4	31	from	distinction	604:614	arg1	peptides					646:653	the peptides	642:653	the peptides using the carbohydrate B-ions, such as m/z 204 (HexNAc) and m/z 366 (HexHexNAc), and identification of the peptide moiety of the glycopeptide based on the presence of the b- and y-series ions derived from the peptide	642:870	Product ion spectra acquired data-dependently were used for both distinction of the glycopeptides from the peptides using the carbohydrate B-ions, such as m/z 204 (HexNAc) and m/z 366 (HexHexNAc), and identification of the peptide moiety of the glycopeptide based on the presence of the b- and y-series ions derived from the peptide.
16321355	8	32	from	antennas	1542:1549	arg1	oligosaccharides					1567:1582	triantennary oligosaccharides	1554:1582	triantennary oligosaccharides	1554:1582	Exoglycosidase digestion suggested that fucose residues were linked to reducing end GlcNAc in biantennary oligosaccharides and to reducing end and/or alpha1-3 to outer arms GlcNAc in triantennary oligosaccharides and that roughly one of the antennas in triantennary oligosaccharides was alpha2-3 sialylated and occasionally alpha1-3 fucosylated at GlcNAc.
16321355	0	33	gly	N-glycosylation	14:28	arg1	ceruloplasmin					55:67	human plasma ceruloplasmin	42:67	human plasma ceruloplasmin	42:67	Site-specific N-glycosylation analysis of human plasma ceruloplasmin using liquid chromatography with electrospray ionization tandem mass spectrometry.
16321355	0	34	theme	ceruloplasmin	55:67	arg1	analysis					30:37	Site-specific N-glycosylation analysis	0:37	Site-specific N-glycosylation analysis of human plasma ceruloplasmin	0:67	Site-specific N-glycosylation analysis of human plasma ceruloplasmin using liquid chromatography with electrospray ionization tandem mass spectrometry.
16321355	7	35	gly	sialylated	1245:1254	arg1	oligosaccharide					1271:1285	sialylated tetraantennary oligosaccharide	1245:1285	sialylated tetraantennary oligosaccharide	1245:1285	A small amount of sialylated tetraantennary oligosaccharide was detected.
16321355	7	36	theme	tetraantennary	1256:1269	arg1	oligosaccharide					1271:1285	sialylated tetraantennary oligosaccharide	1245:1285	sialylated tetraantennary oligosaccharide	1245:1285	A small amount of sialylated tetraantennary oligosaccharide was detected.
16321355	8	37	theme	reducing	1431:1438	arg1	end					1440:1442	reducing end	1431:1442	reducing end	1431:1442	Exoglycosidase digestion suggested that fucose residues were linked to reducing end GlcNAc in biantennary oligosaccharides and to reducing end and/or alpha1-3 to outer arms GlcNAc in triantennary oligosaccharides and that roughly one of the antennas in triantennary oligosaccharides was alpha2-3 sialylated and occasionally alpha1-3 fucosylated at GlcNAc.
16321355	2	38	theme	high-performance	358:373	arg1	chromatography					382:395	reversed-phase high-performance liquid chromatography	343:395	reversed-phase high-performance liquid chromatography	343:395	In this study, a site-specific glycosylation analysis of human ceruloplasmin (CP) was carried out using reversed-phase high-performance liquid chromatography with electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS).
16321355	5	39	theme	peptide	1021:1027	arg1	mass					1009:1012	the glycopeptide and theoretical mass	976:1012	the glycopeptide and theoretical mass of the peptide	976:1027	Oligosaccharide composition was deduced from the molecular weight calculated from the observed mass of the glycopeptide and theoretical mass of the peptide.
16321355	4	40	theme	b-	826:827	arg1	ions					842:845	the b- and y-series ions	822:845	ions	842:845	Product ion spectra acquired data-dependently were used for both distinction of the glycopeptides from the peptides using the carbohydrate B-ions, such as m/z 204 (HexNAc) and m/z 366 (HexHexNAc), and identification of the peptide moiety of the glycopeptide based on the presence of the b- and y-series ions derived from the peptide.
16321355	6	41	gly	N-glycosylation	1053:1067	arg2	sites					1069:1073	the seven potential N-glycosylation sites	1033:1073	the seven potential N-glycosylation sites	1033:1073	Of the seven potential N-glycosylation sites, four (Asn119, Asn339, Asn378, and Asn743) were occupied by a sialylated biantennary or triantennary oligosaccharide with fucose residues (0, 1, or 2).
16321355	6	41	gly	N-glycosylation	1053:1067	arg2	seven					1037:1041	seven	1037:1041	seven	1037:1041	Of the seven potential N-glycosylation sites, four (Asn119, Asn339, Asn378, and Asn743) were occupied by a sialylated biantennary or triantennary oligosaccharide with fucose residues (0, 1, or 2).
16321355	2	42	theme	tandem	426:431	arg1	LC-ESI-MS/MS					452:463	LC-ESI-MS/MS	452:463	LC-ESI-MS/MS	452:463	In this study, a site-specific glycosylation analysis of human ceruloplasmin (CP) was carried out using reversed-phase high-performance liquid chromatography with electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS).
16321355	2	42	theme	tandem	426:431	arg1	spectrometry					438:449	electrospray ionization tandem mass spectrometry	402:449	electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS)	402:464	In this study, a site-specific glycosylation analysis of human ceruloplasmin (CP) was carried out using reversed-phase high-performance liquid chromatography with electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS).
16321355	7	43	theme	small	1229:1233	arg1	oligosaccharide					1271:1285	sialylated tetraantennary oligosaccharide	1245:1285	sialylated tetraantennary oligosaccharide	1245:1285	A small amount of sialylated tetraantennary oligosaccharide was detected.
16321355	7	43	theme	small	1229:1233	arg1	amount					1235:1240	A small amount	1227:1240	A small amount of sialylated tetraantennary oligosaccharide	1227:1285	A small amount of sialylated tetraantennary oligosaccharide was detected.
16321355	1	44	contain	has	166:168	arg1	Ceruloplasmin					152:164	Ceruloplasmin	152:164	Ceruloplasmin	152:164	Ceruloplasmin has ferroxidase activity and plays an essential role in iron metabolism.
16321355	1	44	contain	has	166:168	arg2	activity					182:189	ferroxidase activity	170:189	ferroxidase activity	170:189	Ceruloplasmin has ferroxidase activity and plays an essential role in iron metabolism.
16321355	2	45	theme	electrospray	402:413	arg1	LC-ESI-MS/MS					452:463	LC-ESI-MS/MS	452:463	LC-ESI-MS/MS	452:463	In this study, a site-specific glycosylation analysis of human ceruloplasmin (CP) was carried out using reversed-phase high-performance liquid chromatography with electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS).
16321355	2	45	theme	electrospray	402:413	arg1	spectrometry					438:449	electrospray ionization tandem mass spectrometry	402:449	electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS)	402:464	In this study, a site-specific glycosylation analysis of human ceruloplasmin (CP) was carried out using reversed-phase high-performance liquid chromatography with electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS).
16321355	1	46	theme	essential	204:212	arg1	role					214:217	an essential role	201:217	an essential role	201:217	Ceruloplasmin has ferroxidase activity and plays an essential role in iron metabolism.
16321355	6	47	with	oligosaccharide	1176:1190	arg1	residues					1204:1211	fucose residues	1197:1211	fucose residues (0, 1, or 2)	1197:1224	Of the seven potential N-glycosylation sites, four (Asn119, Asn339, Asn378, and Asn743) were occupied by a sialylated biantennary or triantennary oligosaccharide with fucose residues (0, 1, or 2).
16321355	2	48	gly	glycosylation	270:282	arg1	CP					317:318	CP	317:318	CP	317:318	In this study, a site-specific glycosylation analysis of human ceruloplasmin (CP) was carried out using reversed-phase high-performance liquid chromatography with electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS).
16321355	2	48	gly	glycosylation	270:282	arg1	ceruloplasmin					302:314	human ceruloplasmin	296:314	human ceruloplasmin (CP)	296:319	In this study, a site-specific glycosylation analysis of human ceruloplasmin (CP) was carried out using reversed-phase high-performance liquid chromatography with electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS).
16321355	4	49	used	used	590:593	arg2	spectra					551:557	Product ion spectra	539:557	Product ion spectra acquired data-dependently	539:583	Product ion spectra acquired data-dependently were used for both distinction of the glycopeptides from the peptides using the carbohydrate B-ions, such as m/z 204 (HexNAc) and m/z 366 (HexHexNAc), and identification of the peptide moiety of the glycopeptide based on the presence of the b- and y-series ions derived from the peptide.
16321355	2	50	theme	site-specific	256:268	arg1	analysis					284:291	a site-specific glycosylation analysis	254:291	a site-specific glycosylation analysis of human ceruloplasmin (CP)	254:319	In this study, a site-specific glycosylation analysis of human ceruloplasmin (CP) was carried out using reversed-phase high-performance liquid chromatography with electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS).
16321355	8	51	theme	arms	1469:1472	arg1	GlcNAc					1474:1479	outer arms GlcNAc	1463:1479	outer arms GlcNAc in triantennary oligosaccharides	1463:1512	Exoglycosidase digestion suggested that fucose residues were linked to reducing end GlcNAc in biantennary oligosaccharides and to reducing end and/or alpha1-3 to outer arms GlcNAc in triantennary oligosaccharides and that roughly one of the antennas in triantennary oligosaccharides was alpha2-3 sialylated and occasionally alpha1-3 fucosylated at GlcNAc.
16321355	8	52	dep	sialylated	1597:1606	arg1	fucosylated					1634:1644	fucosylated	1634:1644	fucosylated	1634:1644	Exoglycosidase digestion suggested that fucose residues were linked to reducing end GlcNAc in biantennary oligosaccharides and to reducing end and/or alpha1-3 to outer arms GlcNAc in triantennary oligosaccharides and that roughly one of the antennas in triantennary oligosaccharides was alpha2-3 sialylated and occasionally alpha1-3 fucosylated at GlcNAc.
16321355	8	52	dep	sialylated	1597:1606	arg1	alpha2-3					1588:1595	alpha2-3	1588:1595	alpha2-3	1588:1595	Exoglycosidase digestion suggested that fucose residues were linked to reducing end GlcNAc in biantennary oligosaccharides and to reducing end and/or alpha1-3 to outer arms GlcNAc in triantennary oligosaccharides and that roughly one of the antennas in triantennary oligosaccharides was alpha2-3 sialylated and occasionally alpha1-3 fucosylated at GlcNAc.
16321355	4	53	gly	glycopeptides	623:635	arg2	glycopeptides					623:635	the glycopeptides	619:635	the glycopeptides from the peptides using the carbohydrate B-ions, such as m/z 204 (HexNAc) and m/z 366 (HexHexNAc), and identification of the peptide moiety of the glycopeptide based on the presence of the b- and y-series ions derived from the peptide	619:870	Product ion spectra acquired data-dependently were used for both distinction of the glycopeptides from the peptides using the carbohydrate B-ions, such as m/z 204 (HexNAc) and m/z 366 (HexHexNAc), and identification of the peptide moiety of the glycopeptide based on the presence of the b- and y-series ions derived from the peptide.
16321355	4	53	gly	glycopeptides	623:635	arg1	peptides					646:653	the peptides	642:653	the peptides using the carbohydrate B-ions, such as m/z 204 (HexNAc) and m/z 366 (HexHexNAc), and identification of the peptide moiety of the glycopeptide based on the presence of the b- and y-series ions derived from the peptide	642:870	Product ion spectra acquired data-dependently were used for both distinction of the glycopeptides from the peptides using the carbohydrate B-ions, such as m/z 204 (HexNAc) and m/z 366 (HexHexNAc), and identification of the peptide moiety of the glycopeptide based on the presence of the b- and y-series ions derived from the peptide.
16321355	6	54	dep	residues	1204:1211	arg1	1					1217:1217	1	1217:1217	1	1217:1217	Of the seven potential N-glycosylation sites, four (Asn119, Asn339, Asn378, and Asn743) were occupied by a sialylated biantennary or triantennary oligosaccharide with fucose residues (0, 1, or 2).
16321355	6	54	dep	residues	1204:1211	arg1	2					1223:1223	2	1223:1223	2	1223:1223	Of the seven potential N-glycosylation sites, four (Asn119, Asn339, Asn378, and Asn743) were occupied by a sialylated biantennary or triantennary oligosaccharide with fucose residues (0, 1, or 2).
16321355	2	55	theme	human	296:300	arg1	CP					317:318	CP	317:318	CP	317:318	In this study, a site-specific glycosylation analysis of human ceruloplasmin (CP) was carried out using reversed-phase high-performance liquid chromatography with electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS).
16321355	2	55	theme	human	296:300	arg1	ceruloplasmin					302:314	human ceruloplasmin	296:314	human ceruloplasmin (CP)	296:319	In this study, a site-specific glycosylation analysis of human ceruloplasmin (CP) was carried out using reversed-phase high-performance liquid chromatography with electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS).
16321355	6	56	theme	N-glycosylation	1053:1067	arg1	sites					1069:1073	the seven potential N-glycosylation sites	1033:1073	the seven potential N-glycosylation sites	1033:1073	Of the seven potential N-glycosylation sites, four (Asn119, Asn339, Asn378, and Asn743) were occupied by a sialylated biantennary or triantennary oligosaccharide with fucose residues (0, 1, or 2).
16321355	4	57	gly	glycopeptide	784:795	arg2	glycopeptide					784:795	the glycopeptide	780:795	the glycopeptide	780:795	Product ion spectra acquired data-dependently were used for both distinction of the glycopeptides from the peptides using the carbohydrate B-ions, such as m/z 204 (HexNAc) and m/z 366 (HexHexNAc), and identification of the peptide moiety of the glycopeptide based on the presence of the b- and y-series ions derived from the peptide.
16321355	8	58	theme	Exoglycosidase	1301:1314	arg1	digestion					1316:1324	Exoglycosidase digestion	1301:1324	Exoglycosidase digestion	1301:1324	Exoglycosidase digestion suggested that fucose residues were linked to reducing end GlcNAc in biantennary oligosaccharides and to reducing end and/or alpha1-3 to outer arms GlcNAc in triantennary oligosaccharides and that roughly one of the antennas in triantennary oligosaccharides was alpha2-3 sialylated and occasionally alpha1-3 fucosylated at GlcNAc.
16321355	4	59	attach	derived	847:853	arg1	peptide					864:870	the peptide	860:870	the peptide	860:870	Product ion spectra acquired data-dependently were used for both distinction of the glycopeptides from the peptides using the carbohydrate B-ions, such as m/z 204 (HexNAc) and m/z 366 (HexHexNAc), and identification of the peptide moiety of the glycopeptide based on the presence of the b- and y-series ions derived from the peptide.
16321355	4	59	attach	derived	847:853	arg2	ions					842:845	the b- and y-series ions	822:845	ions	842:845	Product ion spectra acquired data-dependently were used for both distinction of the glycopeptides from the peptides using the carbohydrate B-ions, such as m/z 204 (HexNAc) and m/z 366 (HexHexNAc), and identification of the peptide moiety of the glycopeptide based on the presence of the b- and y-series ions derived from the peptide.
16321355	0	60	theme	electrospray	102:113	arg1	spectrometry					138:149	electrospray ionization tandem mass spectrometry	102:149	electrospray ionization tandem mass spectrometry	102:149	Site-specific N-glycosylation analysis of human plasma ceruloplasmin using liquid chromatography with electrospray ionization tandem mass spectrometry.
16321355	5	61	theme	molecular	922:930	arg1	weight					932:937	the molecular weight	918:937	the molecular weight calculated from the observed mass of the glycopeptide and theoretical mass of the peptide	918:1027	Oligosaccharide composition was deduced from the molecular weight calculated from the observed mass of the glycopeptide and theoretical mass of the peptide.
16321355	4	62	from	peptides	646:653	arg1	distinction					604:614	both distinction	599:614	both distinction of the glycopeptides from the peptides using the carbohydrate B-ions, such as m/z 204 (HexNAc) and m/z 366 (HexHexNAc), and identification of the peptide moiety of the glycopeptide based on the presence of the b- and y-series ions derived from the peptide	599:870	Product ion spectra acquired data-dependently were used for both distinction of the glycopeptides from the peptides using the carbohydrate B-ions, such as m/z 204 (HexNAc) and m/z 366 (HexHexNAc), and identification of the peptide moiety of the glycopeptide based on the presence of the b- and y-series ions derived from the peptide.
16321355	4	62	from	peptides	646:653	arg1	glycopeptides					623:635	the glycopeptides	619:635	the glycopeptides from the peptides using the carbohydrate B-ions, such as m/z 204 (HexNAc) and m/z 366 (HexHexNAc), and identification of the peptide moiety of the glycopeptide based on the presence of the b- and y-series ions derived from the peptide	619:870	Product ion spectra acquired data-dependently were used for both distinction of the glycopeptides from the peptides using the carbohydrate B-ions, such as m/z 204 (HexNAc) and m/z 366 (HexHexNAc), and identification of the peptide moiety of the glycopeptide based on the presence of the b- and y-series ions derived from the peptide.
16321355	0	63	theme	tandem	126:131	arg1	spectrometry					138:149	electrospray ionization tandem mass spectrometry	102:149	electrospray ionization tandem mass spectrometry	102:149	Site-specific N-glycosylation analysis of human plasma ceruloplasmin using liquid chromatography with electrospray ionization tandem mass spectrometry.
16321355	4	64	theme	Product	539:545	arg1	spectra					551:557	Product ion spectra	539:557	Product ion spectra acquired data-dependently	539:583	Product ion spectra acquired data-dependently were used for both distinction of the glycopeptides from the peptides using the carbohydrate B-ions, such as m/z 204 (HexNAc) and m/z 366 (HexHexNAc), and identification of the peptide moiety of the glycopeptide based on the presence of the b- and y-series ions derived from the peptide.
16321355	8	65	theme	fucose	1341:1346	arg1	residues					1348:1355	fucose residues	1341:1355	fucose residues	1341:1355	Exoglycosidase digestion suggested that fucose residues were linked to reducing end GlcNAc in biantennary oligosaccharides and to reducing end and/or alpha1-3 to outer arms GlcNAc in triantennary oligosaccharides and that roughly one of the antennas in triantennary oligosaccharides was alpha2-3 sialylated and occasionally alpha1-3 fucosylated at GlcNAc.
16321355	4	66	theme	glycopeptide	784:795	arg1	moiety					770:775	the peptide moiety	758:775	the peptide moiety of the glycopeptide based on the presence of the b- and y-series ions derived from the peptide	758:870	Product ion spectra acquired data-dependently were used for both distinction of the glycopeptides from the peptides using the carbohydrate B-ions, such as m/z 204 (HexNAc) and m/z 366 (HexHexNAc), and identification of the peptide moiety of the glycopeptide based on the presence of the b- and y-series ions derived from the peptide.
16321355	5	67	theme	Oligosaccharide	873:887	arg1	composition					889:899	Oligosaccharide composition	873:899	Oligosaccharide composition	873:899	Oligosaccharide composition was deduced from the molecular weight calculated from the observed mass of the glycopeptide and theoretical mass of the peptide.
16321355	5	68	theme	mass	1009:1012	arg1	mass					968:971	the observed mass	955:971	the observed mass of the glycopeptide and theoretical mass of the peptide	955:1027	Oligosaccharide composition was deduced from the molecular weight calculated from the observed mass of the glycopeptide and theoretical mass of the peptide.
16321355	6	69	dep	four	1076:1079	arg1	Asn378					1098:1103	Asn378	1098:1103	Asn378	1098:1103	Of the seven potential N-glycosylation sites, four (Asn119, Asn339, Asn378, and Asn743) were occupied by a sialylated biantennary or triantennary oligosaccharide with fucose residues (0, 1, or 2).
16321355	6	69	dep	four	1076:1079	arg1	Asn743					1110:1115	Asn743	1110:1115	Asn743	1110:1115	Of the seven potential N-glycosylation sites, four (Asn119, Asn339, Asn378, and Asn743) were occupied by a sialylated biantennary or triantennary oligosaccharide with fucose residues (0, 1, or 2).
16321355	6	69	dep	four	1076:1079	arg1	Asn339					1090:1095	Asn339	1090:1095	Asn339	1090:1095	Of the seven potential N-glycosylation sites, four (Asn119, Asn339, Asn378, and Asn743) were occupied by a sialylated biantennary or triantennary oligosaccharide with fucose residues (0, 1, or 2).
16321355	3	70	theme	CP	505:506	arg1	digest					477:482	A tryptic digest	467:482	A tryptic digest of carboxymethylated CP	467:506	A tryptic digest of carboxymethylated CP was subjected to LC-ESI-MS/MS.
16321355	0	71	theme	N-glycosylation	14:28	arg1	analysis					30:37	Site-specific N-glycosylation analysis	0:37	Site-specific N-glycosylation analysis of human plasma ceruloplasmin	0:67	Site-specific N-glycosylation analysis of human plasma ceruloplasmin using liquid chromatography with electrospray ionization tandem mass spectrometry.
16321355	8	72	gly	sialylated	1597:1606	arg1	one					1531:1533	one	1531:1533	one	1531:1533	Exoglycosidase digestion suggested that fucose residues were linked to reducing end GlcNAc in biantennary oligosaccharides and to reducing end and/or alpha1-3 to outer arms GlcNAc in triantennary oligosaccharides and that roughly one of the antennas in triantennary oligosaccharides was alpha2-3 sialylated and occasionally alpha1-3 fucosylated at GlcNAc.
16321355	8	72	gly	sialylated	1597:1606	arg1	antennas					1542:1549	the antennas	1538:1549	the antennas in triantennary oligosaccharides	1538:1582	Exoglycosidase digestion suggested that fucose residues were linked to reducing end GlcNAc in biantennary oligosaccharides and to reducing end and/or alpha1-3 to outer arms GlcNAc in triantennary oligosaccharides and that roughly one of the antennas in triantennary oligosaccharides was alpha2-3 sialylated and occasionally alpha1-3 fucosylated at GlcNAc.
16321355	8	72	gly	sialylated	1597:1606	arg2	GlcNAc					1649:1654	GlcNAc	1649:1654	GlcNAc	1649:1654	Exoglycosidase digestion suggested that fucose residues were linked to reducing end GlcNAc in biantennary oligosaccharides and to reducing end and/or alpha1-3 to outer arms GlcNAc in triantennary oligosaccharides and that roughly one of the antennas in triantennary oligosaccharides was alpha2-3 sialylated and occasionally alpha1-3 fucosylated at GlcNAc.
16321355	4	73	theme	glycopeptides	623:635	arg1	distinction					604:614	both distinction	599:614	both distinction of the glycopeptides from the peptides using the carbohydrate B-ions, such as m/z 204 (HexNAc) and m/z 366 (HexHexNAc), and identification of the peptide moiety of the glycopeptide based on the presence of the b- and y-series ions derived from the peptide	599:870	Product ion spectra acquired data-dependently were used for both distinction of the glycopeptides from the peptides using the carbohydrate B-ions, such as m/z 204 (HexNAc) and m/z 366 (HexHexNAc), and identification of the peptide moiety of the glycopeptide based on the presence of the b- and y-series ions derived from the peptide.
16321355	4	74	theme	peptide	762:768	arg1	moiety					770:775	the peptide moiety	758:775	the peptide moiety of the glycopeptide based on the presence of the b- and y-series ions derived from the peptide	758:870	Product ion spectra acquired data-dependently were used for both distinction of the glycopeptides from the peptides using the carbohydrate B-ions, such as m/z 204 (HexNAc) and m/z 366 (HexHexNAc), and identification of the peptide moiety of the glycopeptide based on the presence of the b- and y-series ions derived from the peptide.
16321355	2	75	theme	mass	433:436	arg1	LC-ESI-MS/MS					452:463	LC-ESI-MS/MS	452:463	LC-ESI-MS/MS	452:463	In this study, a site-specific glycosylation analysis of human ceruloplasmin (CP) was carried out using reversed-phase high-performance liquid chromatography with electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS).
16321355	2	75	theme	mass	433:436	arg1	spectrometry					438:449	electrospray ionization tandem mass spectrometry	402:449	electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS)	402:464	In this study, a site-specific glycosylation analysis of human ceruloplasmin (CP) was carried out using reversed-phase high-performance liquid chromatography with electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS).
16321355	8	76	theme	end	1381:1383	arg1	GlcNAc					1385:1390	reducing end GlcNAc	1372:1390	reducing end GlcNAc	1372:1390	Exoglycosidase digestion suggested that fucose residues were linked to reducing end GlcNAc in biantennary oligosaccharides and to reducing end and/or alpha1-3 to outer arms GlcNAc in triantennary oligosaccharides and that roughly one of the antennas in triantennary oligosaccharides was alpha2-3 sialylated and occasionally alpha1-3 fucosylated at GlcNAc.
16321355	0	77	theme	plasma	48:53	arg1	ceruloplasmin					55:67	human plasma ceruloplasmin	42:67	human plasma ceruloplasmin	42:67	Site-specific N-glycosylation analysis of human plasma ceruloplasmin using liquid chromatography with electrospray ionization tandem mass spectrometry.
16321355	7	78	theme	oligosaccharide	1271:1285	arg1	oligosaccharide					1271:1285	sialylated tetraantennary oligosaccharide	1245:1285	sialylated tetraantennary oligosaccharide	1245:1285	A small amount of sialylated tetraantennary oligosaccharide was detected.
16321355	7	78	theme	oligosaccharide	1271:1285	arg1	amount					1235:1240	A small amount	1227:1240	A small amount of sialylated tetraantennary oligosaccharide	1227:1285	A small amount of sialylated tetraantennary oligosaccharide was detected.
16321355	3	79	theme	tryptic	469:475	arg1	digest					477:482	A tryptic digest	467:482	A tryptic digest of carboxymethylated CP	467:506	A tryptic digest of carboxymethylated CP was subjected to LC-ESI-MS/MS.
16321355	8	80	from	GlcNAc	1474:1479	arg1	oligosaccharides					1497:1512	triantennary oligosaccharides	1484:1512	triantennary oligosaccharides	1484:1512	Exoglycosidase digestion suggested that fucose residues were linked to reducing end GlcNAc in biantennary oligosaccharides and to reducing end and/or alpha1-3 to outer arms GlcNAc in triantennary oligosaccharides and that roughly one of the antennas in triantennary oligosaccharides was alpha2-3 sialylated and occasionally alpha1-3 fucosylated at GlcNAc.
16321355	7	81	theme	sialylated	1245:1254	arg1	oligosaccharide					1271:1285	sialylated tetraantennary oligosaccharide	1245:1285	sialylated tetraantennary oligosaccharide	1245:1285	A small amount of sialylated tetraantennary oligosaccharide was detected.
16321355	4	82	theme	ions	842:845	arg1	presence					810:817	the presence	806:817	the presence of the b- and y-series ions derived from the peptide	806:870	Product ion spectra acquired data-dependently were used for both distinction of the glycopeptides from the peptides using the carbohydrate B-ions, such as m/z 204 (HexNAc) and m/z 366 (HexHexNAc), and identification of the peptide moiety of the glycopeptide based on the presence of the b- and y-series ions derived from the peptide.
16321355	2	83	theme	liquid	375:380	arg1	chromatography					382:395	reversed-phase high-performance liquid chromatography	343:395	reversed-phase high-performance liquid chromatography	343:395	In this study, a site-specific glycosylation analysis of human ceruloplasmin (CP) was carried out using reversed-phase high-performance liquid chromatography with electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS).
16321355	2	84	theme	reversed-phase	343:356	arg1	chromatography					382:395	reversed-phase high-performance liquid chromatography	343:395	reversed-phase high-performance liquid chromatography	343:395	In this study, a site-specific glycosylation analysis of human ceruloplasmin (CP) was carried out using reversed-phase high-performance liquid chromatography with electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS).
16321355	2	85	theme	ionization	415:424	arg1	LC-ESI-MS/MS					452:463	LC-ESI-MS/MS	452:463	LC-ESI-MS/MS	452:463	In this study, a site-specific glycosylation analysis of human ceruloplasmin (CP) was carried out using reversed-phase high-performance liquid chromatography with electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS).
16321355	2	85	theme	ionization	415:424	arg1	spectrometry					438:449	electrospray ionization tandem mass spectrometry	402:449	electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS)	402:464	In this study, a site-specific glycosylation analysis of human ceruloplasmin (CP) was carried out using reversed-phase high-performance liquid chromatography with electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS).
15454184	0	0	theme	hamster	94:100	arg1	cells					108:112	Chinese hamster ovary cells	86:112	Chinese hamster ovary cells	86:112	Analysis of site-specific glycosylation in recombinant human follistatin expressed in Chinese hamster ovary cells.
15454184	7	1	theme	oligosaccharide	908:922	arg1	profiling					924:932	mass spectrometric oligosaccharide profiling	889:932	mass spectrometric oligosaccharide profiling	889:932	This finding was supported by mass spectrometric oligosaccharide profiling, in which the m/z values and elution times of some of the oligosaccharides from rhFS were in good agreement with those of standard oligosaccharides.
15454184	6	2	theme	composition	740:750	arg1	analyses					752:759	Monosaccharide composition analyses	725:759	Monosaccharide composition analyses	725:759	Monosaccharide composition analyses suggested the linkages of fucosylated bi- and triantennary complex-type oligosaccharides on rhFS.
15454184	2	3	theme	FS	343:344	arg1	rhFS					347:350	recombinant human FS (rhFS)	325:351	recombinant human FS (rhFS) produced in Chinese hamster ovary cells	325:391	In this study, we analyzed the glycosylation of recombinant human FS (rhFS) produced in Chinese hamster ovary cells.
15454184	6	4	gly	fucosylated	787:797	arg1	bi-					799:801	fucosylated bi- and triantennary complex-type oligosaccharides	787:848	bi-	799:801	Monosaccharide composition analyses suggested the linkages of fucosylated bi- and triantennary complex-type oligosaccharides on rhFS.
15454184	0	5	theme	Chinese	86:92	arg1	cells					108:112	Chinese hamster ovary cells	86:112	Chinese hamster ovary cells	86:112	Analysis of site-specific glycosylation in recombinant human follistatin expressed in Chinese hamster ovary cells.
15454184	9	6	theme	major	1233:1237	arg1	oligosaccharides					1212:1227	biantennary oligosaccharides	1200:1227	biantennary oligosaccharides	1200:1227	It was suggested that biantennary oligosaccharides are major oligosaccharides located at both Asn95 and Asn259, whereas the triantennary structures are present mainly at Asn95.
15454184	9	6	theme	major	1233:1237	arg1	oligosaccharides					1239:1254	major oligosaccharides	1233:1254	major oligosaccharides located at both Asn95 and Asn259	1233:1287	It was suggested that biantennary oligosaccharides are major oligosaccharides located at both Asn95 and Asn259, whereas the triantennary structures are present mainly at Asn95.
15454184	2	7	theme	human	337:341	arg1	rhFS					347:350	recombinant human FS (rhFS)	325:351	recombinant human FS (rhFS) produced in Chinese hamster ovary cells	325:391	In this study, we analyzed the glycosylation of recombinant human FS (rhFS) produced in Chinese hamster ovary cells.
15454184	1	8	theme	biological	242:251	arg1	activities					253:262	the biological activities	238:262	the biological activities of activins	238:274	Follistatin (FS), a glycoprotein, plays an important role in cell growth and differentiation through the neutralization of the biological activities of activins.
15454184	0	9	from	Analysis	0:7	arg1	follistatin					61:71	recombinant human follistatin	43:71	recombinant human follistatin	43:71	Analysis of site-specific glycosylation in recombinant human follistatin expressed in Chinese hamster ovary cells.
15454184	5	10	theme	mass	579:582	arg1	mapping					619:625	mass spectrometric peptide/glycopeptide mapping	579:625	mass spectrometric peptide/glycopeptide mapping	579:625	Using mass spectrometric peptide/glycopeptide mapping and precursor-ion scanning, we found that both N-glycosylation sites were partially glycosylated.
15454184	4	11	contain	contains	509:516	arg2	Asn95					555:559	Asn95	555:559	Asn95	555:559	FS contains two potential N-glycosylation sites, Asn95 and Asn259.
15454184	4	11	contain	contains	509:516	arg2	sites					548:552	two potential N-glycosylation sites	518:552	two potential N-glycosylation sites	518:552	FS contains two potential N-glycosylation sites, Asn95 and Asn259.
15454184	4	11	contain	contains	509:516	arg1	FS					506:507	FS	506:507	FS	506:507	FS contains two potential N-glycosylation sites, Asn95 and Asn259.
15454184	4	11	contain	contains	509:516	arg2	Asn259					565:570	Asn259	565:570	Asn259	565:570	FS contains two potential N-glycosylation sites, Asn95 and Asn259.
15454184	9	12	attach	present	1330:1336	arg2	structures					1315:1324	the triantennary structures	1298:1324	the triantennary structures	1298:1324	It was suggested that biantennary oligosaccharides are major oligosaccharides located at both Asn95 and Asn259, whereas the triantennary structures are present mainly at Asn95.
15454184	9	12	attach	present	1330:1336	arg1	Asn95					1348:1352	Asn95	1348:1352	Asn95	1348:1352	It was suggested that biantennary oligosaccharides are major oligosaccharides located at both Asn95 and Asn259, whereas the triantennary structures are present mainly at Asn95.
15454184	1	13	theme	activities	253:262	arg1	neutralization					220:233	the neutralization	216:233	the neutralization of the biological activities of activins	216:274	Follistatin (FS), a glycoprotein, plays an important role in cell growth and differentiation through the neutralization of the biological activities of activins.
15454184	0	14	theme	ovary	102:106	arg1	cells					108:112	Chinese hamster ovary cells	86:112	Chinese hamster ovary cells	86:112	Analysis of site-specific glycosylation in recombinant human follistatin expressed in Chinese hamster ovary cells.
15454184	0	15	from	follistatin	61:71	arg1	Analysis					0:7	Analysis	0:7	Analysis of site-specific glycosylation in recombinant human follistatin	0:71	Analysis of site-specific glycosylation in recombinant human follistatin expressed in Chinese hamster ovary cells.
15454184	6	16	theme	fucosylated	787:797	arg1	bi-					799:801	fucosylated bi- and triantennary complex-type oligosaccharides	787:848	bi-	799:801	Monosaccharide composition analyses suggested the linkages of fucosylated bi- and triantennary complex-type oligosaccharides on rhFS.
15454184	5	17	theme	spectrometric	584:596	arg1	mapping					619:625	mass spectrometric peptide/glycopeptide mapping	579:625	mass spectrometric peptide/glycopeptide mapping	579:625	Using mass spectrometric peptide/glycopeptide mapping and precursor-ion scanning, we found that both N-glycosylation sites were partially glycosylated.
15454184	3	18	gly	glycosylated	486:497	arg1	forms					499:503	glycosylated forms	486:503	glycosylated forms	486:503	The results of SDS-PAGE and MALDI-TOF MS revealed the presence of both non-glycosylated and glycosylated forms.
15454184	6	19	theme	Monosaccharide	725:738	arg1	composition					740:750	Monosaccharide composition	725:750	Monosaccharide composition analyses	725:759	Monosaccharide composition analyses suggested the linkages of fucosylated bi- and triantennary complex-type oligosaccharides on rhFS.
15454184	7	20	theme	spectrometric	894:906	arg1	profiling					924:932	mass spectrometric oligosaccharide profiling	889:932	mass spectrometric oligosaccharide profiling	889:932	This finding was supported by mass spectrometric oligosaccharide profiling, in which the m/z values and elution times of some of the oligosaccharides from rhFS were in good agreement with those of standard oligosaccharides.
15454184	5	21	gly	glycosylated	711:722	arg1	sites					690:694	both N-glycosylation sites	669:694	both N-glycosylation sites	669:694	Using mass spectrometric peptide/glycopeptide mapping and precursor-ion scanning, we found that both N-glycosylation sites were partially glycosylated.
15454184	5	22	theme	peptide/glycopeptide	598:617	arg1	mapping					619:625	mass spectrometric peptide/glycopeptide mapping	579:625	mass spectrometric peptide/glycopeptide mapping	579:625	Using mass spectrometric peptide/glycopeptide mapping and precursor-ion scanning, we found that both N-glycosylation sites were partially glycosylated.
15454184	8	23	theme	spectra	1148:1154	arg1	basis					1130:1134	the basis	1126:1134	the basis of the mass spectra of the glycopeptides	1126:1175	Site-specific glycosylation was deduced on the basis of the mass spectra of the glycopeptides.
15454184	2	24	theme	Chinese	365:371	arg1	cells					387:391	Chinese hamster ovary cells	365:391	Chinese hamster ovary cells	365:391	In this study, we analyzed the glycosylation of recombinant human FS (rhFS) produced in Chinese hamster ovary cells.
15454184	8	25	theme	Site-specific	1083:1095	arg1	glycosylation					1097:1109	Site-specific glycosylation	1083:1109	Site-specific glycosylation	1083:1109	Site-specific glycosylation was deduced on the basis of the mass spectra of the glycopeptides.
15454184	9	26	theme	located	1256:1262	arg1	oligosaccharides					1212:1227	biantennary oligosaccharides	1200:1227	biantennary oligosaccharides	1200:1227	It was suggested that biantennary oligosaccharides are major oligosaccharides located at both Asn95 and Asn259, whereas the triantennary structures are present mainly at Asn95.
15454184	9	26	theme	located	1256:1262	arg1	oligosaccharides					1239:1254	major oligosaccharides	1233:1254	major oligosaccharides located at both Asn95 and Asn259	1233:1287	It was suggested that biantennary oligosaccharides are major oligosaccharides located at both Asn95 and Asn259, whereas the triantennary structures are present mainly at Asn95.
15454184	6	27	theme	complex-type	820:831	arg1	oligosaccharides					833:848	fucosylated bi- and triantennary complex-type oligosaccharides	787:848	oligosaccharides	833:848	Monosaccharide composition analyses suggested the linkages of fucosylated bi- and triantennary complex-type oligosaccharides on rhFS.
15454184	6	28	theme	oligosaccharides	833:848	arg1	linkages					775:782	the linkages	771:782	the linkages of fucosylated bi- and triantennary complex-type oligosaccharides on rhFS	771:856	Monosaccharide composition analyses suggested the linkages of fucosylated bi- and triantennary complex-type oligosaccharides on rhFS.
15454184	7	29	theme	mass	889:892	arg1	profiling					924:932	mass spectrometric oligosaccharide profiling	889:932	mass spectrometric oligosaccharide profiling	889:932	This finding was supported by mass spectrometric oligosaccharide profiling, in which the m/z values and elution times of some of the oligosaccharides from rhFS were in good agreement with those of standard oligosaccharides.
15454184	1	30	theme	important	158:166	arg1	role					168:171	an important role	155:171	an important role	155:171	Follistatin (FS), a glycoprotein, plays an important role in cell growth and differentiation through the neutralization of the biological activities of activins.
15454184	5	31	theme	precursor-ion	631:643	arg1	scanning					645:652	precursor-ion scanning	631:652	precursor-ion scanning	631:652	Using mass spectrometric peptide/glycopeptide mapping and precursor-ion scanning, we found that both N-glycosylation sites were partially glycosylated.
15454184	4	32	theme	N-glycosylation	532:546	arg1	Asn259					565:570	Asn259	565:570	Asn259	565:570	FS contains two potential N-glycosylation sites, Asn95 and Asn259.
15454184	4	32	theme	N-glycosylation	532:546	arg1	Asn95					555:559	Asn95	555:559	Asn95	555:559	FS contains two potential N-glycosylation sites, Asn95 and Asn259.
15454184	4	32	theme	N-glycosylation	532:546	arg1	sites					548:552	two potential N-glycosylation sites	518:552	two potential N-glycosylation sites	518:552	FS contains two potential N-glycosylation sites, Asn95 and Asn259.
15454184	5	33	theme	N-glycosylation	674:688	arg1	sites					690:694	both N-glycosylation sites	669:694	both N-glycosylation sites	669:694	Using mass spectrometric peptide/glycopeptide mapping and precursor-ion scanning, we found that both N-glycosylation sites were partially glycosylated.
15454184	1	34	theme	activins	267:274	arg1	activities					253:262	the biological activities	238:262	the biological activities of activins	238:274	Follistatin (FS), a glycoprotein, plays an important role in cell growth and differentiation through the neutralization of the biological activities of activins.
15454184	6	35	theme	triantennary	807:818	arg1	oligosaccharides					833:848	fucosylated bi- and triantennary complex-type oligosaccharides	787:848	oligosaccharides	833:848	Monosaccharide composition analyses suggested the linkages of fucosylated bi- and triantennary complex-type oligosaccharides on rhFS.
15454184	7	36	from	agreement	1032:1040	arg1	profiling					924:932	mass spectrometric oligosaccharide profiling	889:932	mass spectrometric oligosaccharide profiling	889:932	This finding was supported by mass spectrometric oligosaccharide profiling, in which the m/z values and elution times of some of the oligosaccharides from rhFS were in good agreement with those of standard oligosaccharides.
15454184	0	37	theme	glycosylation	26:38	arg1	Analysis					0:7	Analysis	0:7	Analysis of site-specific glycosylation in recombinant human follistatin	0:71	Analysis of site-specific glycosylation in recombinant human follistatin expressed in Chinese hamster ovary cells.
15454184	4	38	theme	potential	522:530	arg1	Asn259					565:570	Asn259	565:570	Asn259	565:570	FS contains two potential N-glycosylation sites, Asn95 and Asn259.
15454184	4	38	theme	potential	522:530	arg1	Asn95					555:559	Asn95	555:559	Asn95	555:559	FS contains two potential N-glycosylation sites, Asn95 and Asn259.
15454184	4	38	theme	potential	522:530	arg1	sites					548:552	two potential N-glycosylation sites	518:552	two potential N-glycosylation sites	518:552	FS contains two potential N-glycosylation sites, Asn95 and Asn259.
15454184	3	39	theme	MS	432:433	arg1	results					398:404	The results	394:404	The results of SDS-PAGE and MALDI-TOF MS	394:433	The results of SDS-PAGE and MALDI-TOF MS revealed the presence of both non-glycosylated and glycosylated forms.
15454184	0	40	theme	site-specific	12:24	arg1	glycosylation					26:38	site-specific glycosylation	12:38	site-specific glycosylation in recombinant human follistatin	12:71	Analysis of site-specific glycosylation in recombinant human follistatin expressed in Chinese hamster ovary cells.
15454184	7	41	from	rhFS	1014:1017	arg1	oligosaccharides					992:1007	the oligosaccharides	988:1007	the oligosaccharides from rhFS	988:1017	This finding was supported by mass spectrometric oligosaccharide profiling, in which the m/z values and elution times of some of the oligosaccharides from rhFS were in good agreement with those of standard oligosaccharides.
15454184	3	42	theme	glycosylated	486:497	arg1	forms					499:503	glycosylated forms	486:503	glycosylated forms	486:503	The results of SDS-PAGE and MALDI-TOF MS revealed the presence of both non-glycosylated and glycosylated forms.
15454184	0	43	theme	recombinant	43:53	arg1	follistatin					61:71	recombinant human follistatin	43:71	recombinant human follistatin	43:71	Analysis of site-specific glycosylation in recombinant human follistatin expressed in Chinese hamster ovary cells.
15454184	9	44	from	Asn259	1282:1287	arg1	located					1256:1262	located	1256:1262	located	1256:1262	It was suggested that biantennary oligosaccharides are major oligosaccharides located at both Asn95 and Asn259, whereas the triantennary structures are present mainly at Asn95.
15454184	8	45	theme	mass	1143:1146	arg1	spectra					1148:1154	the mass spectra	1139:1154	the mass spectra of the glycopeptides	1139:1175	Site-specific glycosylation was deduced on the basis of the mass spectra of the glycopeptides.
15454184	8	46	gly	glycosylation	1097:1109	arg1	basis					1130:1134	the basis	1126:1134	the basis of the mass spectra of the glycopeptides	1126:1175	Site-specific glycosylation was deduced on the basis of the mass spectra of the glycopeptides.
15454184	2	47	theme	ovary	381:385	arg1	cells					387:391	Chinese hamster ovary cells	365:391	Chinese hamster ovary cells	365:391	In this study, we analyzed the glycosylation of recombinant human FS (rhFS) produced in Chinese hamster ovary cells.
15454184	6	48	theme	bi-	799:801	arg1	linkages					775:782	the linkages	771:782	the linkages of fucosylated bi- and triantennary complex-type oligosaccharides on rhFS	771:856	Monosaccharide composition analyses suggested the linkages of fucosylated bi- and triantennary complex-type oligosaccharides on rhFS.
15454184	2	49	theme	hamster	373:379	arg1	cells					387:391	Chinese hamster ovary cells	365:391	Chinese hamster ovary cells	365:391	In this study, we analyzed the glycosylation of recombinant human FS (rhFS) produced in Chinese hamster ovary cells.
15454184	3	50	theme	non-glycosylated	465:480	arg1	presence					448:455	the presence	444:455	the presence of both non-glycosylated and glycosylated forms	444:503	The results of SDS-PAGE and MALDI-TOF MS revealed the presence of both non-glycosylated and glycosylated forms.
15454184	1	51	gly	glycoprotein	135:146	arg1	glycoprotein					135:146	a glycoprotein	133:146	a glycoprotein	133:146	Follistatin (FS), a glycoprotein, plays an important role in cell growth and differentiation through the neutralization of the biological activities of activins.
15454184	1	51	gly	glycoprotein	135:146	arg1	Follistatin					115:125	Follistatin	115:125	Follistatin (FS)	115:130	Follistatin (FS), a glycoprotein, plays an important role in cell growth and differentiation through the neutralization of the biological activities of activins.
15454184	9	52	theme	triantennary	1302:1313	arg1	structures					1315:1324	the triantennary structures	1298:1324	the triantennary structures	1298:1324	It was suggested that biantennary oligosaccharides are major oligosaccharides located at both Asn95 and Asn259, whereas the triantennary structures are present mainly at Asn95.
15454184	4	53	gly	N-glycosylation	532:546	arg2	Asn95					555:559	Asn95	555:559	Asn95	555:559	FS contains two potential N-glycosylation sites, Asn95 and Asn259.
15454184	4	53	gly	N-glycosylation	532:546	arg2	sites					548:552	two potential N-glycosylation sites	518:552	two potential N-glycosylation sites	518:552	FS contains two potential N-glycosylation sites, Asn95 and Asn259.
15454184	4	53	gly	N-glycosylation	532:546	arg2	two					518:520	two	518:520	two	518:520	FS contains two potential N-glycosylation sites, Asn95 and Asn259.
15454184	4	53	gly	N-glycosylation	532:546	arg2	Asn259					565:570	Asn259	565:570	Asn259	565:570	FS contains two potential N-glycosylation sites, Asn95 and Asn259.
15454184	2	54	theme	recombinant	325:335	arg1	rhFS					347:350	recombinant human FS (rhFS)	325:351	recombinant human FS (rhFS) produced in Chinese hamster ovary cells	325:391	In this study, we analyzed the glycosylation of recombinant human FS (rhFS) produced in Chinese hamster ovary cells.
15454184	0	55	theme	human	55:59	arg1	follistatin					61:71	recombinant human follistatin	43:71	recombinant human follistatin	43:71	Analysis of site-specific glycosylation in recombinant human follistatin expressed in Chinese hamster ovary cells.
15454184	5	56	gly	N-glycosylation	674:688	arg2	sites					690:694	both N-glycosylation sites	669:694	both N-glycosylation sites	669:694	Using mass spectrometric peptide/glycopeptide mapping and precursor-ion scanning, we found that both N-glycosylation sites were partially glycosylated.
15454184	0	57	gly	glycosylation	26:38	arg1	follistatin					61:71	recombinant human follistatin	43:71	recombinant human follistatin	43:71	Analysis of site-specific glycosylation in recombinant human follistatin expressed in Chinese hamster ovary cells.
15454184	6	58	from	linkages	775:782	arg1	rhFS					853:856	rhFS	853:856	rhFS	853:856	Monosaccharide composition analyses suggested the linkages of fucosylated bi- and triantennary complex-type oligosaccharides on rhFS.
15454184	9	59	dep	oligosaccharides	1239:1254	arg1	whereas					1290:1296	whereas	1290:1296	whereas	1290:1296	It was suggested that biantennary oligosaccharides are major oligosaccharides located at both Asn95 and Asn259, whereas the triantennary structures are present mainly at Asn95.
15454184	8	60	theme	glycopeptides	1163:1175	arg1	spectra					1148:1154	the mass spectra	1139:1154	the mass spectra of the glycopeptides	1139:1175	Site-specific glycosylation was deduced on the basis of the mass spectra of the glycopeptides.
15454184	7	61	theme	some	980:983	arg1	values					952:957	m/z values	948:957	m/z values	948:957	This finding was supported by mass spectrometric oligosaccharide profiling, in which the m/z values and elution times of some of the oligosaccharides from rhFS were in good agreement with those of standard oligosaccharides.
15454184	7	61	theme	some	980:983	arg1	times					971:975	elution times	963:975	elution times	963:975	This finding was supported by mass spectrometric oligosaccharide profiling, in which the m/z values and elution times of some of the oligosaccharides from rhFS were in good agreement with those of standard oligosaccharides.
15454184	8	62	gly	glycopeptides	1163:1175	arg2	glycopeptides					1163:1175	the glycopeptides	1159:1175	the glycopeptides	1159:1175	Site-specific glycosylation was deduced on the basis of the mass spectra of the glycopeptides.
15454184	7	63	dep	values	952:957	arg1	the					944:946	the	944:946	the	944:946	This finding was supported by mass spectrometric oligosaccharide profiling, in which the m/z values and elution times of some of the oligosaccharides from rhFS were in good agreement with those of standard oligosaccharides.
15454184	7	64	theme	elution	963:969	arg1	times					971:975	elution times	963:975	elution times	963:975	This finding was supported by mass spectrometric oligosaccharide profiling, in which the m/z values and elution times of some of the oligosaccharides from rhFS were in good agreement with those of standard oligosaccharides.
15454184	9	65	from	Asn95	1348:1352	arg1	present					1330:1336	present	1330:1336	present	1330:1336	It was suggested that biantennary oligosaccharides are major oligosaccharides located at both Asn95 and Asn259, whereas the triantennary structures are present mainly at Asn95.
15454184	2	66	gly	glycosylation	308:320	arg1	study					285:289	this study	280:289	this study	280:289	In this study, we analyzed the glycosylation of recombinant human FS (rhFS) produced in Chinese hamster ovary cells.
15454184	2	66	gly	glycosylation	308:320	arg1	rhFS					347:350	recombinant human FS (rhFS)	325:351	recombinant human FS (rhFS) produced in Chinese hamster ovary cells	325:391	In this study, we analyzed the glycosylation of recombinant human FS (rhFS) produced in Chinese hamster ovary cells.
15454184	7	67	theme	standard	1056:1063	arg1	oligosaccharides					1065:1080	standard oligosaccharides	1056:1080	standard oligosaccharides	1056:1080	This finding was supported by mass spectrometric oligosaccharide profiling, in which the m/z values and elution times of some of the oligosaccharides from rhFS were in good agreement with those of standard oligosaccharides.
15454184	7	68	theme	good	1027:1030	arg1	agreement					1032:1040	good agreement	1027:1040	good agreement with those of standard oligosaccharides	1027:1080	This finding was supported by mass spectrometric oligosaccharide profiling, in which the m/z values and elution times of some of the oligosaccharides from rhFS were in good agreement with those of standard oligosaccharides.
15454184	9	69	from	Asn95	1272:1276	arg1	located					1256:1262	located	1256:1262	located	1256:1262	It was suggested that biantennary oligosaccharides are major oligosaccharides located at both Asn95 and Asn259, whereas the triantennary structures are present mainly at Asn95.
15454184	7	70	theme	m/z	948:950	arg1	values					952:957	m/z values	948:957	m/z values	948:957	This finding was supported by mass spectrometric oligosaccharide profiling, in which the m/z values and elution times of some of the oligosaccharides from rhFS were in good agreement with those of standard oligosaccharides.
15454184	3	71	theme	MALDI-TOF	422:430	arg1	MS					432:433	MALDI-TOF MS	422:433	MALDI-TOF MS	422:433	The results of SDS-PAGE and MALDI-TOF MS revealed the presence of both non-glycosylated and glycosylated forms.
15454184	1	72	dep	cell	176:179	arg1	growth					181:186	growth	181:186	growth	181:186	Follistatin (FS), a glycoprotein, plays an important role in cell growth and differentiation through the neutralization of the biological activities of activins.
15454184	1	72	dep	cell	176:179	arg1	differentiation					192:206	differentiation	192:206	differentiation	192:206	Follistatin (FS), a glycoprotein, plays an important role in cell growth and differentiation through the neutralization of the biological activities of activins.
15454184	9	73	theme	biantennary	1200:1210	arg1	oligosaccharides					1212:1227	biantennary oligosaccharides	1200:1227	biantennary oligosaccharides	1200:1227	It was suggested that biantennary oligosaccharides are major oligosaccharides located at both Asn95 and Asn259, whereas the triantennary structures are present mainly at Asn95.
15454184	9	73	theme	biantennary	1200:1210	arg1	oligosaccharides					1239:1254	major oligosaccharides	1233:1254	major oligosaccharides located at both Asn95 and Asn259	1233:1287	It was suggested that biantennary oligosaccharides are major oligosaccharides located at both Asn95 and Asn259, whereas the triantennary structures are present mainly at Asn95.
15454184	2	74	theme	rhFS	347:350	arg1	glycosylation					308:320	the glycosylation	304:320	the glycosylation of recombinant human FS (rhFS) produced in Chinese hamster ovary cells	304:391	In this study, we analyzed the glycosylation of recombinant human FS (rhFS) produced in Chinese hamster ovary cells.
15454184	3	75	theme	SDS-PAGE	409:416	arg1	results					398:404	The results	394:404	The results of SDS-PAGE and MALDI-TOF MS	394:433	The results of SDS-PAGE and MALDI-TOF MS revealed the presence of both non-glycosylated and glycosylated forms.
15454184	5	76	gly	peptide/glycopeptide	598:617	arg2	peptide/glycopeptide					598:617	mass spectrometric peptide/glycopeptide mapping	579:625	mass spectrometric peptide/glycopeptide mapping	579:625	Using mass spectrometric peptide/glycopeptide mapping and precursor-ion scanning, we found that both N-glycosylation sites were partially glycosylated.
15454184	0	77	from	glycosylation	26:38	arg1	follistatin					61:71	recombinant human follistatin	43:71	recombinant human follistatin	43:71	Analysis of site-specific glycosylation in recombinant human follistatin expressed in Chinese hamster ovary cells.
15454184	3	78	theme	forms	499:503	arg1	presence					448:455	the presence	444:455	the presence of both non-glycosylated and glycosylated forms	444:503	The results of SDS-PAGE and MALDI-TOF MS revealed the presence of both non-glycosylated and glycosylated forms.
15454184	7	79	with	agreement	1032:1040	arg1	those					1047:1051	those	1047:1051	those	1047:1051	This finding was supported by mass spectrometric oligosaccharide profiling, in which the m/z values and elution times of some of the oligosaccharides from rhFS were in good agreement with those of standard oligosaccharides.
21511948	10	0	theme	mass	1290:1293	arg1	analysis					1308:1315	mass spectrometry analysis	1290:1315	mass spectrometry analysis	1290:1315	Using mass spectrometry analysis, we found that Asn(81) may or may not be glycosylated in WT RAGE, whereas in G82S RAGE, Asn(81) is always glycosylated.
21511948	1	1	theme	end	242:244	arg1	RAGE					256:259	RAGE	256:259	RAGE	256:259	Interaction between the receptor for advanced glycation end products (RAGE) and its ligands amplifies the proinflammatory response.
21511948	1	1	theme	end	242:244	arg1	products					246:253	advanced glycation end products	223:253	advanced glycation end products (RAGE)	223:260	Interaction between the receptor for advanced glycation end products (RAGE) and its ligands amplifies the proinflammatory response.
21511948	12	2	theme	RAGE	1789:1792	arg1	variant					1794:1800	the G82S polymorphic RAGE variant	1768:1800	the G82S polymorphic RAGE variant	1768:1800	Therefore, the G82S polymorphism promotes N-linked glycosylation of Asn(81), which has implications for the structure of the ligand binding region of RAGE and might explain the enhanced function associated with the G82S polymorphic RAGE variant.
21511948	6	3	theme	RAGE	841:844	arg1	protein					846:852	RAGE protein	841:852	RAGE protein	841:852	WT or various mutant forms of RAGE protein, including N25Q, N81Q, N25Q/G82S, and N25Q/N81Q, were produced by transfecting HEK293 cells.
21511948	0	4	theme	G82S	160:163	arg1	variant					177:183	the G82S polymorphic variant	156:183	the G82S polymorphic variant	156:183	The G82S polymorphism promotes glycosylation of the receptor for advanced glycation end products (RAGE) at asparagine 81: comparison of wild-type rage with the G82S polymorphic variant.
21511948	3	5	from	Asn	473:475	arg1	sites					424:428	Two potential sites	410:428	Two potential sites	410:428	Two potential sites for N-linked glycosylation, at Asn(25) and Asn(81), are implicated, one of which is potentially influenced by a naturally occurring polymorphism that substitutes Gly(82) with Ser.
21511948	12	6	theme	G82S	1572:1575	arg1	polymorphism					1577:1588	the G82S polymorphism	1568:1588	the G82S polymorphism	1568:1588	Therefore, the G82S polymorphism promotes N-linked glycosylation of Asn(81), which has implications for the structure of the ligand binding region of RAGE and might explain the enhanced function associated with the G82S polymorphic RAGE variant.
21511948	6	7	theme	various	817:823	arg1	forms					832:836	various mutant forms	817:836	various mutant forms	817:836	WT or various mutant forms of RAGE protein, including N25Q, N81Q, N25Q/G82S, and N25Q/N81Q, were produced by transfecting HEK293 cells.
21511948	6	7	theme	various	817:823	arg1	N81Q					871:874	N81Q	871:874	N81Q	871:874	WT or various mutant forms of RAGE protein, including N25Q, N81Q, N25Q/G82S, and N25Q/N81Q, were produced by transfecting HEK293 cells.
21511948	6	7	theme	various	817:823	arg1	N25Q/G82S					877:885	N25Q/G82S	877:885	N25Q/G82S	877:885	WT or various mutant forms of RAGE protein, including N25Q, N81Q, N25Q/G82S, and N25Q/N81Q, were produced by transfecting HEK293 cells.
21511948	6	7	theme	various	817:823	arg1	N25Q/N81Q					892:900	N25Q/N81Q	892:900	N25Q/N81Q	892:900	WT or various mutant forms of RAGE protein, including N25Q, N81Q, N25Q/G82S, and N25Q/N81Q, were produced by transfecting HEK293 cells.
21511948	12	8	theme	G82S	1772:1775	arg1	variant					1794:1800	the G82S polymorphic RAGE variant	1768:1800	the G82S polymorphic RAGE variant	1768:1800	Therefore, the G82S polymorphism promotes N-linked glycosylation of Asn(81), which has implications for the structure of the ligand binding region of RAGE and might explain the enhanced function associated with the G82S polymorphic RAGE variant.
21511948	10	9	gly	glycosylated	1358:1369	arg1	Asn					1332:1334	Asn	1332:1334	Asn(81)	1332:1338	Using mass spectrometry analysis, we found that Asn(81) may or may not be glycosylated in WT RAGE, whereas in G82S RAGE, Asn(81) is always glycosylated.
21511948	10	9	gly	glycosylated	1358:1369	arg1	RAGE					1377:1380	WT RAGE	1374:1380	WT RAGE	1374:1380	Using mass spectrometry analysis, we found that Asn(81) may or may not be glycosylated in WT RAGE, whereas in G82S RAGE, Asn(81) is always glycosylated.
21511948	10	9	gly	glycosylated	1358:1369	arg2	81					1336:1337	81	1336:1337	81	1336:1337	Using mass spectrometry analysis, we found that Asn(81) may or may not be glycosylated in WT RAGE, whereas in G82S RAGE, Asn(81) is always glycosylated.
21511948	10	9	gly	glycosylated	1358:1369	arg1	81					1336:1337	81	1336:1337	81	1336:1337	Using mass spectrometry analysis, we found that Asn(81) may or may not be glycosylated in WT RAGE, whereas in G82S RAGE, Asn(81) is always glycosylated.
21511948	10	9	gly	glycosylated	1358:1369	arg2	Asn					1332:1334	Asn	1332:1334	Asn(81)	1332:1338	Using mass spectrometry analysis, we found that Asn(81) may or may not be glycosylated in WT RAGE, whereas in G82S RAGE, Asn(81) is always glycosylated.
21511948	7	10	theme	proteins	987:994	arg1	patterns					965:972	The glycosylation patterns	947:972	The glycosylation patterns of expressed proteins	947:994	The glycosylation patterns of expressed proteins were compared.
21511948	9	11	theme	N25Q	1176:1179	arg1	glycosylation					1159:1171	N-linked glycosylation	1150:1171	N-linked glycosylation of N25Q and N81Q mutants	1150:1196	Our data also revealed N-linked glycosylation of N25Q and N81Q mutants, suggesting that both Asn(25) and Asn(81) can be utilized for N-linked glycosylation.
21511948	5	12	theme	ligand	795:800	arg1	binding					802:808	ligand binding	795:808	ligand binding	795:808	We hypothesized that the G82S polymorphism affects RAGE glycosylation and thereby affects ligand binding.
21511948	4	13	theme	RAGE	632:635	arg1	variant					637:643	This G82S polymorphic RAGE variant	610:643	This G82S polymorphic RAGE variant	610:643	This G82S polymorphic RAGE variant displays increased ligand binding and downstream signaling.
21511948	9	14	theme	N81Q	1185:1188	arg1	glycosylation					1159:1171	N-linked glycosylation	1150:1171	N-linked glycosylation of N25Q and N81Q mutants	1150:1196	Our data also revealed N-linked glycosylation of N25Q and N81Q mutants, suggesting that both Asn(25) and Asn(81) can be utilized for N-linked glycosylation.
21511948	7	15	gly	glycosylation	951:963	arg1	proteins					987:994	expressed proteins	977:994	expressed proteins	977:994	The glycosylation patterns of expressed proteins were compared.
21511948	7	16	theme	glycosylation	951:963	arg1	patterns					965:972	The glycosylation patterns	947:972	The glycosylation patterns of expressed proteins	947:994	The glycosylation patterns of expressed proteins were compared.
21511948	3	17	theme	occurring	552:560	arg1	polymorphism					562:573	a naturally occurring polymorphism	540:573	a naturally occurring polymorphism that substitutes Gly(82) with Ser	540:607	Two potential sites for N-linked glycosylation, at Asn(25) and Asn(81), are implicated, one of which is potentially influenced by a naturally occurring polymorphism that substitutes Gly(82) with Ser.
21511948	11	18	theme	NF-κB	1539:1543	arg1	activation					1545:1554	NF-κB activation	1539:1554	NF-κB activation	1539:1554	Furthermore, RAGE binding to S100B ligand is affected by Asn(81) glycosylation, with consequences for NF-κB activation.
21511948	0	19	theme	wild-type	136:144	arg1	rage					146:149	wild-type rage	136:149	wild-type rage	136:149	The G82S polymorphism promotes glycosylation of the receptor for advanced glycation end products (RAGE) at asparagine 81: comparison of wild-type rage with the G82S polymorphic variant.
21511948	4	20	theme	G82S	615:618	arg1	variant					637:643	This G82S polymorphic RAGE variant	610:643	This G82S polymorphic RAGE variant	610:643	This G82S polymorphic RAGE variant displays increased ligand binding and downstream signaling.
21511948	0	21	theme	glycation	74:82	arg1	RAGE					98:101	RAGE	98:101	RAGE	98:101	The G82S polymorphism promotes glycosylation of the receptor for advanced glycation end products (RAGE) at asparagine 81: comparison of wild-type rage with the G82S polymorphic variant.
21511948	0	21	theme	glycation	74:82	arg1	products					88:95	advanced glycation end products	65:95	advanced glycation end products (RAGE)	65:102	The G82S polymorphism promotes glycosylation of the receptor for advanced glycation end products (RAGE) at asparagine 81: comparison of wild-type rage with the G82S polymorphic variant.
21511948	0	22	with	comparison	122:131	arg1	variant					177:183	the G82S polymorphic variant	156:183	the G82S polymorphic variant	156:183	The G82S polymorphism promotes glycosylation of the receptor for advanced glycation end products (RAGE) at asparagine 81: comparison of wild-type rage with the G82S polymorphic variant.
21511948	3	23	theme	potential	414:422	arg1	sites					424:428	Two potential sites	410:428	Two potential sites	410:428	Two potential sites for N-linked glycosylation, at Asn(25) and Asn(81), are implicated, one of which is potentially influenced by a naturally occurring polymorphism that substitutes Gly(82) with Ser.
21511948	10	24	gly	glycosylated	1423:1434	arg2	81					1409:1410	81	1409:1410	81	1409:1410	Using mass spectrometry analysis, we found that Asn(81) may or may not be glycosylated in WT RAGE, whereas in G82S RAGE, Asn(81) is always glycosylated.
21511948	10	24	gly	glycosylated	1423:1434	arg1	Asn					1405:1407	Asn	1405:1407	Asn(81)	1405:1411	Using mass spectrometry analysis, we found that Asn(81) may or may not be glycosylated in WT RAGE, whereas in G82S RAGE, Asn(81) is always glycosylated.
21511948	10	24	gly	glycosylated	1423:1434	arg2	Asn					1405:1407	Asn	1405:1407	Asn(81)	1405:1411	Using mass spectrometry analysis, we found that Asn(81) may or may not be glycosylated in WT RAGE, whereas in G82S RAGE, Asn(81) is always glycosylated.
21511948	10	24	gly	glycosylated	1423:1434	arg1	RAGE					1399:1402	G82S RAGE	1394:1402	G82S RAGE	1394:1402	Using mass spectrometry analysis, we found that Asn(81) may or may not be glycosylated in WT RAGE, whereas in G82S RAGE, Asn(81) is always glycosylated.
21511948	10	24	gly	glycosylated	1423:1434	arg1	81					1409:1410	81	1409:1410	81	1409:1410	Using mass spectrometry analysis, we found that Asn(81) may or may not be glycosylated in WT RAGE, whereas in G82S RAGE, Asn(81) is always glycosylated.
21511948	4	25	theme	ligand	664:669	arg1	binding					671:677	increased ligand binding	654:677	increased ligand binding	654:677	This G82S polymorphic RAGE variant displays increased ligand binding and downstream signaling.
21511948	12	26	theme	binding	1689:1695	arg1	region					1697:1702	the ligand binding region	1678:1702	the ligand binding region of RAGE	1678:1710	Therefore, the G82S polymorphism promotes N-linked glycosylation of Asn(81), which has implications for the structure of the ligand binding region of RAGE and might explain the enhanced function associated with the G82S polymorphic RAGE variant.
21511948	2	27	theme	binding	401:407	arg1	regulation					380:389	the regulation	376:389	the regulation of ligand binding	376:407	N-Linked glycosylation of RAGE plays an important role in the regulation of ligand binding.
21511948	10	28	dep	may	1340:1342	arg1	whereas					1383:1389	whereas	1383:1389	whereas	1383:1389	Using mass spectrometry analysis, we found that Asn(81) may or may not be glycosylated in WT RAGE, whereas in G82S RAGE, Asn(81) is always glycosylated.
21511948	12	29	contain	has	1640:1642	arg1	glycosylation					1608:1620	N-linked glycosylation	1599:1620	N-linked glycosylation	1599:1620	Therefore, the G82S polymorphism promotes N-linked glycosylation of Asn(81), which has implications for the structure of the ligand binding region of RAGE and might explain the enhanced function associated with the G82S polymorphic RAGE variant.
21511948	12	29	contain	has	1640:1642	arg2	implications					1644:1655	implications	1644:1655	implications for the structure of the ligand binding region of RAGE	1644:1710	Therefore, the G82S polymorphism promotes N-linked glycosylation of Asn(81), which has implications for the structure of the ligand binding region of RAGE and might explain the enhanced function associated with the G82S polymorphic RAGE variant.
21511948	5	30	theme	G82S	730:733	arg1	polymorphism					735:746	the G82S polymorphism	726:746	the G82S polymorphism	726:746	We hypothesized that the G82S polymorphism affects RAGE glycosylation and thereby affects ligand binding.
21511948	10	31	theme	WT	1374:1375	arg1	RAGE					1377:1380	WT RAGE	1374:1380	WT RAGE	1374:1380	Using mass spectrometry analysis, we found that Asn(81) may or may not be glycosylated in WT RAGE, whereas in G82S RAGE, Asn(81) is always glycosylated.
21511948	12	32	theme	N-linked	1599:1606	arg1	glycosylation					1608:1620	N-linked glycosylation	1599:1620	N-linked glycosylation	1599:1620	Therefore, the G82S polymorphism promotes N-linked glycosylation of Asn(81), which has implications for the structure of the ligand binding region of RAGE and might explain the enhanced function associated with the G82S polymorphic RAGE variant.
21511948	9	33	link	N-linked	1150:1157	arg1	glycosylation					1159:1171	N-linked glycosylation	1150:1171	N-linked glycosylation of N25Q and N81Q mutants	1150:1196	Our data also revealed N-linked glycosylation of N25Q and N81Q mutants, suggesting that both Asn(25) and Asn(81) can be utilized for N-linked glycosylation.
21511948	11	34	theme	RAGE	1450:1453	arg1	binding					1455:1461	RAGE binding	1450:1461	RAGE binding to S100B ligand	1450:1477	Furthermore, RAGE binding to S100B ligand is affected by Asn(81) glycosylation, with consequences for NF-κB activation.
21511948	12	35	link	N-linked	1599:1606	arg1	glycosylation					1608:1620	N-linked glycosylation	1599:1620	N-linked glycosylation	1599:1620	Therefore, the G82S polymorphism promotes N-linked glycosylation of Asn(81), which has implications for the structure of the ligand binding region of RAGE and might explain the enhanced function associated with the G82S polymorphic RAGE variant.
21511948	2	36	theme	RAGE	344:347	arg1	glycosylation					327:339	N-Linked glycosylation	318:339	N-Linked glycosylation of RAGE	318:347	N-Linked glycosylation of RAGE plays an important role in the regulation of ligand binding.
21511948	1	37	theme	glycation	232:240	arg1	RAGE					256:259	RAGE	256:259	RAGE	256:259	Interaction between the receptor for advanced glycation end products (RAGE) and its ligands amplifies the proinflammatory response.
21511948	1	37	theme	glycation	232:240	arg1	products					246:253	advanced glycation end products	223:253	advanced glycation end products (RAGE)	223:260	Interaction between the receptor for advanced glycation end products (RAGE) and its ligands amplifies the proinflammatory response.
21511948	8	38	theme	polymorphic	1070:1080	arg1	variant					1082:1088	the G82S polymorphic variant	1061:1088	the G82S polymorphic variant	1061:1088	Enzymatic deglycosylation showed that WT RAGE and the G82S polymorphic variant are glycosylated to the same extent.
21511948	6	39	theme	protein	846:852	arg1	forms					832:836	various mutant forms	817:836	various mutant forms	817:836	WT or various mutant forms of RAGE protein, including N25Q, N81Q, N25Q/G82S, and N25Q/N81Q, were produced by transfecting HEK293 cells.
21511948	6	39	theme	protein	846:852	arg1	N81Q					871:874	N81Q	871:874	N81Q	871:874	WT or various mutant forms of RAGE protein, including N25Q, N81Q, N25Q/G82S, and N25Q/N81Q, were produced by transfecting HEK293 cells.
21511948	6	39	theme	protein	846:852	arg1	WT					811:812	WT	811:812	WT	811:812	WT or various mutant forms of RAGE protein, including N25Q, N81Q, N25Q/G82S, and N25Q/N81Q, were produced by transfecting HEK293 cells.
21511948	6	39	theme	protein	846:852	arg1	N25Q/G82S					877:885	N25Q/G82S	877:885	N25Q/G82S	877:885	WT or various mutant forms of RAGE protein, including N25Q, N81Q, N25Q/G82S, and N25Q/N81Q, were produced by transfecting HEK293 cells.
21511948	6	39	theme	protein	846:852	arg1	N25Q/N81Q					892:900	N25Q/N81Q	892:900	N25Q/N81Q	892:900	WT or various mutant forms of RAGE protein, including N25Q, N81Q, N25Q/G82S, and N25Q/N81Q, were produced by transfecting HEK293 cells.
21511948	3	40	link	N-linked	434:441	arg1	glycosylation					443:455	N-linked glycosylation	434:455	N-linked glycosylation	434:455	Two potential sites for N-linked glycosylation, at Asn(25) and Asn(81), are implicated, one of which is potentially influenced by a naturally occurring polymorphism that substitutes Gly(82) with Ser.
21511948	0	41	theme	polymorphic	165:175	arg1	variant					177:183	the G82S polymorphic variant	156:183	the G82S polymorphic variant	156:183	The G82S polymorphism promotes glycosylation of the receptor for advanced glycation end products (RAGE) at asparagine 81: comparison of wild-type rage with the G82S polymorphic variant.
21511948	12	42	theme	polymorphic	1777:1787	arg1	variant					1794:1800	the G82S polymorphic RAGE variant	1768:1800	the G82S polymorphic RAGE variant	1768:1800	Therefore, the G82S polymorphism promotes N-linked glycosylation of Asn(81), which has implications for the structure of the ligand binding region of RAGE and might explain the enhanced function associated with the G82S polymorphic RAGE variant.
21511948	9	43	link	N-linked	1260:1267	arg1	glycosylation					1269:1281	N-linked glycosylation	1260:1281	N-linked glycosylation	1260:1281	Our data also revealed N-linked glycosylation of N25Q and N81Q mutants, suggesting that both Asn(25) and Asn(81) can be utilized for N-linked glycosylation.
21511948	12	44	gly	glycosylation	1608:1620	arg1	81					1629:1630	81	1629:1630	81	1629:1630	Therefore, the G82S polymorphism promotes N-linked glycosylation of Asn(81), which has implications for the structure of the ligand binding region of RAGE and might explain the enhanced function associated with the G82S polymorphic RAGE variant.
21511948	12	44	gly	glycosylation	1608:1620	arg1	Asn					1625:1627	Asn	1625:1627	Asn(81)	1625:1631	Therefore, the G82S polymorphism promotes N-linked glycosylation of Asn(81), which has implications for the structure of the ligand binding region of RAGE and might explain the enhanced function associated with the G82S polymorphic RAGE variant.
21511948	11	45	theme	Asn	1494:1496	arg1	glycosylation					1502:1514	Asn(81) glycosylation	1494:1514	Asn(81) glycosylation	1494:1514	Furthermore, RAGE binding to S100B ligand is affected by Asn(81) glycosylation, with consequences for NF-κB activation.
21511948	6	46	theme	mutant	825:830	arg1	forms					832:836	various mutant forms	817:836	various mutant forms	817:836	WT or various mutant forms of RAGE protein, including N25Q, N81Q, N25Q/G82S, and N25Q/N81Q, were produced by transfecting HEK293 cells.
21511948	6	46	theme	mutant	825:830	arg1	N81Q					871:874	N81Q	871:874	N81Q	871:874	WT or various mutant forms of RAGE protein, including N25Q, N81Q, N25Q/G82S, and N25Q/N81Q, were produced by transfecting HEK293 cells.
21511948	6	46	theme	mutant	825:830	arg1	N25Q/G82S					877:885	N25Q/G82S	877:885	N25Q/G82S	877:885	WT or various mutant forms of RAGE protein, including N25Q, N81Q, N25Q/G82S, and N25Q/N81Q, were produced by transfecting HEK293 cells.
21511948	6	46	theme	mutant	825:830	arg1	N25Q/N81Q					892:900	N25Q/N81Q	892:900	N25Q/N81Q	892:900	WT or various mutant forms of RAGE protein, including N25Q, N81Q, N25Q/G82S, and N25Q/N81Q, were produced by transfecting HEK293 cells.
21511948	9	47	gly	glycosylation	1159:1171	arg1	N25Q					1176:1179	N25Q	1176:1179	N25Q	1176:1179	Our data also revealed N-linked glycosylation of N25Q and N81Q mutants, suggesting that both Asn(25) and Asn(81) can be utilized for N-linked glycosylation.
21511948	9	47	gly	glycosylation	1159:1171	arg1	N81Q					1185:1188	N81Q	1185:1188	N81Q	1185:1188	Our data also revealed N-linked glycosylation of N25Q and N81Q mutants, suggesting that both Asn(25) and Asn(81) can be utilized for N-linked glycosylation.
21511948	3	48	from	Asn	461:463	arg1	sites					424:428	Two potential sites	410:428	Two potential sites	410:428	Two potential sites for N-linked glycosylation, at Asn(25) and Asn(81), are implicated, one of which is potentially influenced by a naturally occurring polymorphism that substitutes Gly(82) with Ser.
21511948	8	49	theme	same	1114:1117	arg1	extent					1119:1124	the same extent	1110:1124	the same extent	1110:1124	Enzymatic deglycosylation showed that WT RAGE and the G82S polymorphic variant are glycosylated to the same extent.
21511948	10	50	theme	spectrometry	1295:1306	arg1	analysis					1308:1315	mass spectrometry analysis	1290:1315	mass spectrometry analysis	1290:1315	Using mass spectrometry analysis, we found that Asn(81) may or may not be glycosylated in WT RAGE, whereas in G82S RAGE, Asn(81) is always glycosylated.
21511948	7	51	theme	expressed	977:985	arg1	proteins					987:994	expressed proteins	977:994	expressed proteins	977:994	The glycosylation patterns of expressed proteins were compared.
21511948	9	52	used	utilized	1247:1254	arg2	Asn					1232:1234	Asn	1232:1234	Asn(81)	1232:1238	Our data also revealed N-linked glycosylation of N25Q and N81Q mutants, suggesting that both Asn(25) and Asn(81) can be utilized for N-linked glycosylation.
21511948	9	52	used	utilized	1247:1254	arg2	25					1224:1225	25	1224:1225	25	1224:1225	Our data also revealed N-linked glycosylation of N25Q and N81Q mutants, suggesting that both Asn(25) and Asn(81) can be utilized for N-linked glycosylation.
21511948	9	52	used	utilized	1247:1254	arg2	81					1236:1237	81	1236:1237	81	1236:1237	Our data also revealed N-linked glycosylation of N25Q and N81Q mutants, suggesting that both Asn(25) and Asn(81) can be utilized for N-linked glycosylation.
21511948	9	52	used	utilized	1247:1254	arg2	Asn					1220:1222	Asn	1220:1222	Asn(25)	1220:1226	Our data also revealed N-linked glycosylation of N25Q and N81Q mutants, suggesting that both Asn(25) and Asn(81) can be utilized for N-linked glycosylation.
21511948	1	53	theme	proinflammatory	292:306	arg1	response					308:315	the proinflammatory response	288:315	the proinflammatory response	288:315	Interaction between the receptor for advanced glycation end products (RAGE) and its ligands amplifies the proinflammatory response.
21511948	3	54	theme	which	505:509	arg1	which					505:509	which	505:509	which	505:509	Two potential sites for N-linked glycosylation, at Asn(25) and Asn(81), are implicated, one of which is potentially influenced by a naturally occurring polymorphism that substitutes Gly(82) with Ser.
21511948	3	54	theme	which	505:509	arg1	one					498:500	one	498:500	one	498:500	Two potential sites for N-linked glycosylation, at Asn(25) and Asn(81), are implicated, one of which is potentially influenced by a naturally occurring polymorphism that substitutes Gly(82) with Ser.
21511948	12	55	theme	enhanced	1734:1741	arg1	function					1743:1750	the enhanced function	1730:1750	the enhanced function associated with the G82S polymorphic RAGE variant	1730:1800	Therefore, the G82S polymorphism promotes N-linked glycosylation of Asn(81), which has implications for the structure of the ligand binding region of RAGE and might explain the enhanced function associated with the G82S polymorphic RAGE variant.
21511948	4	56	theme	polymorphic	620:630	arg1	variant					637:643	This G82S polymorphic RAGE variant	610:643	This G82S polymorphic RAGE variant	610:643	This G82S polymorphic RAGE variant displays increased ligand binding and downstream signaling.
21511948	9	57	theme	N-linked	1150:1157	arg1	glycosylation					1159:1171	N-linked glycosylation	1150:1171	N-linked glycosylation of N25Q and N81Q mutants	1150:1196	Our data also revealed N-linked glycosylation of N25Q and N81Q mutants, suggesting that both Asn(25) and Asn(81) can be utilized for N-linked glycosylation.
21511948	0	58	theme	rage	146:149	arg1	comparison					122:131	comparison	122:131	comparison of wild-type rage with the G82S polymorphic variant	122:183	The G82S polymorphism promotes glycosylation of the receptor for advanced glycation end products (RAGE) at asparagine 81: comparison of wild-type rage with the G82S polymorphic variant.
21511948	0	59	theme	advanced	65:72	arg1	RAGE					98:101	RAGE	98:101	RAGE	98:101	The G82S polymorphism promotes glycosylation of the receptor for advanced glycation end products (RAGE) at asparagine 81: comparison of wild-type rage with the G82S polymorphic variant.
21511948	0	59	theme	advanced	65:72	arg1	products					88:95	advanced glycation end products	65:95	advanced glycation end products (RAGE)	65:102	The G82S polymorphism promotes glycosylation of the receptor for advanced glycation end products (RAGE) at asparagine 81: comparison of wild-type rage with the G82S polymorphic variant.
21511948	6	60	theme	HEK293	933:938	arg1	cells					940:944	HEK293 cells	933:944	HEK293 cells	933:944	WT or various mutant forms of RAGE protein, including N25Q, N81Q, N25Q/G82S, and N25Q/N81Q, were produced by transfecting HEK293 cells.
21511948	0	61	theme	end	84:86	arg1	RAGE					98:101	RAGE	98:101	RAGE	98:101	The G82S polymorphism promotes glycosylation of the receptor for advanced glycation end products (RAGE) at asparagine 81: comparison of wild-type rage with the G82S polymorphic variant.
21511948	0	61	theme	end	84:86	arg1	products					88:95	advanced glycation end products	65:95	advanced glycation end products (RAGE)	65:102	The G82S polymorphism promotes glycosylation of the receptor for advanced glycation end products (RAGE) at asparagine 81: comparison of wild-type rage with the G82S polymorphic variant.
21511948	12	62	theme	RAGE	1707:1710	arg1	region					1697:1702	the ligand binding region	1678:1702	the ligand binding region of RAGE	1678:1710	Therefore, the G82S polymorphism promotes N-linked glycosylation of Asn(81), which has implications for the structure of the ligand binding region of RAGE and might explain the enhanced function associated with the G82S polymorphic RAGE variant.
21511948	4	63	theme	downstream	683:692	arg1	signaling					694:702	downstream signaling	683:702	downstream signaling	683:702	This G82S polymorphic RAGE variant displays increased ligand binding and downstream signaling.
21511948	12	64	theme	ligand	1682:1687	arg1	region					1697:1702	the ligand binding region	1678:1702	the ligand binding region of RAGE	1678:1710	Therefore, the G82S polymorphism promotes N-linked glycosylation of Asn(81), which has implications for the structure of the ligand binding region of RAGE and might explain the enhanced function associated with the G82S polymorphic RAGE variant.
21511948	0	65	theme	G82S	4:7	arg1	polymorphism					9:20	The G82S polymorphism	0:20	The G82S polymorphism	0:20	The G82S polymorphism promotes glycosylation of the receptor for advanced glycation end products (RAGE) at asparagine 81: comparison of wild-type rage with the G82S polymorphic variant.
21511948	12	66	theme	region	1697:1702	arg1	structure					1665:1673	the structure	1661:1673	the structure of the ligand binding region of RAGE	1661:1710	Therefore, the G82S polymorphism promotes N-linked glycosylation of Asn(81), which has implications for the structure of the ligand binding region of RAGE and might explain the enhanced function associated with the G82S polymorphic RAGE variant.
21511948	4	67	theme	increased	654:662	arg1	binding					671:677	increased ligand binding	654:677	increased ligand binding	654:677	This G82S polymorphic RAGE variant displays increased ligand binding and downstream signaling.
21511948	2	68	theme	important	358:366	arg1	role					368:371	an important role	355:371	an important role	355:371	N-Linked glycosylation of RAGE plays an important role in the regulation of ligand binding.
21511948	5	69	theme	RAGE	756:759	arg1	glycosylation					761:773	RAGE glycosylation	756:773	RAGE glycosylation	756:773	We hypothesized that the G82S polymorphism affects RAGE glycosylation and thereby affects ligand binding.
21511948	8	70	theme	Enzymatic	1011:1019	arg1	deglycosylation					1021:1035	Enzymatic deglycosylation	1011:1035	Enzymatic deglycosylation	1011:1035	Enzymatic deglycosylation showed that WT RAGE and the G82S polymorphic variant are glycosylated to the same extent.
21511948	8	71	gly	glycosylated	1094:1105	arg1	variant					1082:1088	the G82S polymorphic variant	1061:1088	the G82S polymorphic variant	1061:1088	Enzymatic deglycosylation showed that WT RAGE and the G82S polymorphic variant are glycosylated to the same extent.
21511948	8	71	gly	glycosylated	1094:1105	arg1	RAGE					1052:1055	WT RAGE	1049:1055	WT RAGE	1049:1055	Enzymatic deglycosylation showed that WT RAGE and the G82S polymorphic variant are glycosylated to the same extent.
21511948	2	72	theme	ligand	394:399	arg1	binding					401:407	ligand binding	394:407	ligand binding	394:407	N-Linked glycosylation of RAGE plays an important role in the regulation of ligand binding.
21511948	3	73	theme	N-linked	434:441	arg1	glycosylation					443:455	N-linked glycosylation	434:455	N-linked glycosylation	434:455	Two potential sites for N-linked glycosylation, at Asn(25) and Asn(81), are implicated, one of which is potentially influenced by a naturally occurring polymorphism that substitutes Gly(82) with Ser.
21511948	0	74	theme	receptor	52:59	arg1	glycosylation					31:43	glycosylation	31:43	glycosylation of the receptor for advanced glycation end products (RAGE)	31:102	The G82S polymorphism promotes glycosylation of the receptor for advanced glycation end products (RAGE) at asparagine 81: comparison of wild-type rage with the G82S polymorphic variant.
21511948	8	75	theme	WT	1049:1050	arg1	RAGE					1052:1055	WT RAGE	1049:1055	WT RAGE	1049:1055	Enzymatic deglycosylation showed that WT RAGE and the G82S polymorphic variant are glycosylated to the same extent.
21511948	12	76	theme	Asn	1625:1627	arg1	glycosylation					1608:1620	N-linked glycosylation	1599:1620	N-linked glycosylation	1599:1620	Therefore, the G82S polymorphism promotes N-linked glycosylation of Asn(81), which has implications for the structure of the ligand binding region of RAGE and might explain the enhanced function associated with the G82S polymorphic RAGE variant.
21511948	2	77	gly	glycosylation	327:339	arg1	RAGE					344:347	RAGE	344:347	RAGE	344:347	N-Linked glycosylation of RAGE plays an important role in the regulation of ligand binding.
21511948	2	78	theme	N-Linked	318:325	arg1	glycosylation					327:339	N-Linked glycosylation	318:339	N-Linked glycosylation of RAGE	318:347	N-Linked glycosylation of RAGE plays an important role in the regulation of ligand binding.
21511948	9	79	theme	N-linked	1260:1267	arg1	glycosylation					1269:1281	N-linked glycosylation	1260:1281	N-linked glycosylation	1260:1281	Our data also revealed N-linked glycosylation of N25Q and N81Q mutants, suggesting that both Asn(25) and Asn(81) can be utilized for N-linked glycosylation.
21511948	0	80	gly	glycosylation	31:43	arg1	asparagine					107:116	asparagine 81	107:119	asparagine 81	107:119	The G82S polymorphism promotes glycosylation of the receptor for advanced glycation end products (RAGE) at asparagine 81: comparison of wild-type rage with the G82S polymorphic variant.
21511948	0	80	gly	glycosylation	31:43	arg1	receptor					52:59	the receptor	48:59	the receptor for advanced glycation end products (RAGE)	48:102	The G82S polymorphism promotes glycosylation of the receptor for advanced glycation end products (RAGE) at asparagine 81: comparison of wild-type rage with the G82S polymorphic variant.
21511948	9	81	dep	N25Q	1176:1179	arg1	mutants					1190:1196	mutants	1190:1196	mutants	1190:1196	Our data also revealed N-linked glycosylation of N25Q and N81Q mutants, suggesting that both Asn(25) and Asn(81) can be utilized for N-linked glycosylation.
21511948	8	82	theme	G82S	1065:1068	arg1	variant					1082:1088	the G82S polymorphic variant	1061:1088	the G82S polymorphic variant	1061:1088	Enzymatic deglycosylation showed that WT RAGE and the G82S polymorphic variant are glycosylated to the same extent.
21511948	10	83	theme	G82S	1394:1397	arg1	RAGE					1399:1402	G82S RAGE	1394:1402	G82S RAGE	1394:1402	Using mass spectrometry analysis, we found that Asn(81) may or may not be glycosylated in WT RAGE, whereas in G82S RAGE, Asn(81) is always glycosylated.
21511948	11	84	theme	S100B	1466:1470	arg1	ligand					1472:1477	S100B ligand	1466:1477	S100B ligand	1466:1477	Furthermore, RAGE binding to S100B ligand is affected by Asn(81) glycosylation, with consequences for NF-κB activation.
21511948	1	85	theme	advanced	223:230	arg1	RAGE					256:259	RAGE	256:259	RAGE	256:259	Interaction between the receptor for advanced glycation end products (RAGE) and its ligands amplifies the proinflammatory response.
21511948	1	85	theme	advanced	223:230	arg1	products					246:253	advanced glycation end products	223:253	advanced glycation end products (RAGE)	223:260	Interaction between the receptor for advanced glycation end products (RAGE) and its ligands amplifies the proinflammatory response.
18025088	7	0	from	increases	1354:1362	arg1	levels					1380:1385	the relative levels	1367:1385	the relative levels of unglycosylated triadin-1	1367:1413	Besides substantial increases in the relative levels of unglycosylated triadin-1, proteasome inhibition led to an accumulation of two new modified forms of triadin-1 that were seen with triadin-1 only when it is not glycosylated on Asn(75).
18025088	2	1	theme	N-linked	341:348	arg1	glycans					350:356	N-linked glycans	341:356	N-linked glycans	341:356	Calsequestrin and triadin-1 both contain N-linked glycans, but about half of triadin-1 in the heart remains unglycosylated.
18025088	6	2	with	Treatment	1130:1138	arg1	MG-132					1183:1188	the proteasome inhibitor MG-132	1158:1188	the proteasome inhibitor MG-132	1158:1188	Treatment of triadin-1 with the proteasome inhibitor MG-132 led to striking changes in the relative levels of triadin-1 that indicated active breakdown of unglycosylated, but not glycosylated, triadin-1.
18025088	8	3	theme	novel	1641:1645	arg1	isoforms					1647:1654	these novel isoforms	1635:1654	these novel isoforms	1635:1654	Effects of tunicamycin and endoglycosidase H confirmed that these novel isoforms represent two alternative N-linked glycosylation sites, indicating that an alternative topology occurs infrequently leading to yet other glycoforms with short half-lives.
18025088	5	4	from	levels	1006:1011	arg1	type					1057:1060	the cell type	1048:1060	the cell type	1048:1060	Although triadin-1 appeared by SDS-PAGE analysis as a 35/40-kDa doublet in all cells, variations occurred in the relative levels of the two glycoforms depending on the cell type and whether overexpression involved a plasmid or adenoviral vector.
18025088	4	5	theme	characteristic	653:666	arg1	glycosylation					679:691	the characteristic incomplete glycosylation	649:691	the characteristic incomplete glycosylation stemmed from properties of the glycosylation sequence that are conserved among triadin splice variants, including the close proximity of Asn(75) to the sarcoplasmic reticulum inner membrane	649:881	We showed that the characteristic incomplete glycosylation stemmed from properties of the glycosylation sequence that are conserved among triadin splice variants, including the close proximity of Asn(75) to the sarcoplasmic reticulum inner membrane.
18025088	6	6	theme	active	1265:1270	arg1	breakdown					1272:1280	active breakdown	1265:1280	active breakdown of unglycosylated, but not glycosylated, triadin-1	1265:1331	Treatment of triadin-1 with the proteasome inhibitor MG-132 led to striking changes in the relative levels of triadin-1 that indicated active breakdown of unglycosylated, but not glycosylated, triadin-1.
18025088	3	7	theme	glycoform	527:535	arg1	variants					537:544	glycoform variants	527:544	glycoform variants in non-muscle cell lines and neonatal heart cells using plasmid and adenoviral vectors	527:631	To investigate mechanisms for this incomplete glycosylation, we overexpressed triadin-1 as a series of glycoform variants in non-muscle cell lines and neonatal heart cells using plasmid and adenoviral vectors.
18025088	8	8	theme	alternative	1731:1741	arg1	topology					1743:1750	an alternative topology	1728:1750	an alternative topology	1728:1750	Effects of tunicamycin and endoglycosidase H confirmed that these novel isoforms represent two alternative N-linked glycosylation sites, indicating that an alternative topology occurs infrequently leading to yet other glycoforms with short half-lives.
18025088	7	9	theme	modified	1472:1479	arg1	forms					1481:1485	two new modified forms	1464:1485	two new modified forms of triadin-1 that were seen with triadin-1 only when it is not glycosylated on Asn(75)	1464:1572	Besides substantial increases in the relative levels of unglycosylated triadin-1, proteasome inhibition led to an accumulation of two new modified forms of triadin-1 that were seen with triadin-1 only when it is not glycosylated on Asn(75).
18025088	4	10	theme	reticulum	858:866	arg1	membrane					874:881	the sarcoplasmic reticulum inner membrane	841:881	the sarcoplasmic reticulum inner membrane	841:881	We showed that the characteristic incomplete glycosylation stemmed from properties of the glycosylation sequence that are conserved among triadin splice variants, including the close proximity of Asn(75) to the sarcoplasmic reticulum inner membrane.
18025088	6	11	theme	proteasome	1162:1171	arg1	MG-132					1183:1188	the proteasome inhibitor MG-132	1158:1188	the proteasome inhibitor MG-132	1158:1188	Treatment of triadin-1 with the proteasome inhibitor MG-132 led to striking changes in the relative levels of triadin-1 that indicated active breakdown of unglycosylated, but not glycosylated, triadin-1.
18025088	5	12	from	glycoforms	1024:1033	arg1	type					1057:1060	the cell type	1048:1060	the cell type	1048:1060	Although triadin-1 appeared by SDS-PAGE analysis as a 35/40-kDa doublet in all cells, variations occurred in the relative levels of the two glycoforms depending on the cell type and whether overexpression involved a plasmid or adenoviral vector.
18025088	6	13	gly	glycosylated	1309:1320	arg1	triadin-1					1323:1331	unglycosylated, but not glycosylated, triadin-1	1285:1331	unglycosylated, but not glycosylated, triadin-1	1285:1331	Treatment of triadin-1 with the proteasome inhibitor MG-132 led to striking changes in the relative levels of triadin-1 that indicated active breakdown of unglycosylated, but not glycosylated, triadin-1.
18025088	6	14	theme	relative	1221:1228	arg1	levels					1230:1235	the relative levels	1217:1235	the relative levels of triadin-1	1217:1248	Treatment of triadin-1 with the proteasome inhibitor MG-132 led to striking changes in the relative levels of triadin-1 that indicated active breakdown of unglycosylated, but not glycosylated, triadin-1.
18025088	7	15	theme	proteasome	1416:1425	arg1	inhibition					1427:1436	proteasome inhibition	1416:1436	proteasome inhibition	1416:1436	Besides substantial increases in the relative levels of unglycosylated triadin-1, proteasome inhibition led to an accumulation of two new modified forms of triadin-1 that were seen with triadin-1 only when it is not glycosylated on Asn(75).
18025088	3	16	theme	cell	560:563	arg1	lines					565:569	non-muscle cell lines	549:569	non-muscle cell lines	549:569	To investigate mechanisms for this incomplete glycosylation, we overexpressed triadin-1 as a series of glycoform variants in non-muscle cell lines and neonatal heart cells using plasmid and adenoviral vectors.
18025088	7	17	theme	triadin-1	1405:1413	arg1	levels					1380:1385	the relative levels	1367:1385	the relative levels of unglycosylated triadin-1	1367:1413	Besides substantial increases in the relative levels of unglycosylated triadin-1, proteasome inhibition led to an accumulation of two new modified forms of triadin-1 that were seen with triadin-1 only when it is not glycosylated on Asn(75).
18025088	7	18	gly	unglycosylated	1390:1403	arg1	triadin-1					1405:1413	unglycosylated triadin-1	1390:1413	unglycosylated triadin-1	1390:1413	Besides substantial increases in the relative levels of unglycosylated triadin-1, proteasome inhibition led to an accumulation of two new modified forms of triadin-1 that were seen with triadin-1 only when it is not glycosylated on Asn(75).
18025088	4	19	theme	glycosylation	724:736	arg1	sequence					738:745	the glycosylation sequence	720:745	the glycosylation sequence that are conserved among triadin splice variants, including the close proximity of Asn(75) to the sarcoplasmic reticulum inner membrane	720:881	We showed that the characteristic incomplete glycosylation stemmed from properties of the glycosylation sequence that are conserved among triadin splice variants, including the close proximity of Asn(75) to the sarcoplasmic reticulum inner membrane.
18025088	3	20	theme	heart	584:588	arg1	cells					590:594	neonatal heart cells	575:594	neonatal heart cells	575:594	To investigate mechanisms for this incomplete glycosylation, we overexpressed triadin-1 as a series of glycoform variants in non-muscle cell lines and neonatal heart cells using plasmid and adenoviral vectors.
18025088	7	21	theme	relative	1371:1378	arg1	levels					1380:1385	the relative levels	1367:1385	the relative levels of unglycosylated triadin-1	1367:1413	Besides substantial increases in the relative levels of unglycosylated triadin-1, proteasome inhibition led to an accumulation of two new modified forms of triadin-1 that were seen with triadin-1 only when it is not glycosylated on Asn(75).
18025088	5	22	theme	cell	1052:1055	arg1	type					1057:1060	the cell type	1048:1060	the cell type	1048:1060	Although triadin-1 appeared by SDS-PAGE analysis as a 35/40-kDa doublet in all cells, variations occurred in the relative levels of the two glycoforms depending on the cell type and whether overexpression involved a plasmid or adenoviral vector.
18025088	8	23	theme	short	1809:1813	arg1	half-lives					1815:1824	short half-lives	1809:1824	short half-lives	1809:1824	Effects of tunicamycin and endoglycosidase H confirmed that these novel isoforms represent two alternative N-linked glycosylation sites, indicating that an alternative topology occurs infrequently leading to yet other glycoforms with short half-lives.
18025088	5	24	theme	35/40-kDa	938:946	arg1	doublet					948:954	a 35/40-kDa doublet	936:954	a 35/40-kDa doublet in all cells	936:967	Although triadin-1 appeared by SDS-PAGE analysis as a 35/40-kDa doublet in all cells, variations occurred in the relative levels of the two glycoforms depending on the cell type and whether overexpression involved a plasmid or adenoviral vector.
18025088	5	25	from	type	1057:1060	arg1	levels					1006:1011	the relative levels	993:1011	the relative levels of the two glycoforms depending on the cell type and whether overexpression involved a plasmid or adenoviral vector	993:1127	Although triadin-1 appeared by SDS-PAGE analysis as a 35/40-kDa doublet in all cells, variations occurred in the relative levels of the two glycoforms depending on the cell type and whether overexpression involved a plasmid or adenoviral vector.
18025088	7	26	gly	glycosylated	1550:1561	arg2	Asn					1566:1568	Asn	1566:1568	Asn(75)	1566:1572	Besides substantial increases in the relative levels of unglycosylated triadin-1, proteasome inhibition led to an accumulation of two new modified forms of triadin-1 that were seen with triadin-1 only when it is not glycosylated on Asn(75).
18025088	7	26	gly	glycosylated	1550:1561	arg2	75					1570:1571	75	1570:1571	75	1570:1571	Besides substantial increases in the relative levels of unglycosylated triadin-1, proteasome inhibition led to an accumulation of two new modified forms of triadin-1 that were seen with triadin-1 only when it is not glycosylated on Asn(75).
18025088	7	26	gly	glycosylated	1550:1561	arg2	it					1540:1541	it	1540:1541	it	1540:1541	Besides substantial increases in the relative levels of unglycosylated triadin-1, proteasome inhibition led to an accumulation of two new modified forms of triadin-1 that were seen with triadin-1 only when it is not glycosylated on Asn(75).
18025088	7	26	gly	glycosylated	1550:1561	arg1	Asn					1566:1568	Asn	1566:1568	Asn(75)	1566:1572	Besides substantial increases in the relative levels of unglycosylated triadin-1, proteasome inhibition led to an accumulation of two new modified forms of triadin-1 that were seen with triadin-1 only when it is not glycosylated on Asn(75).
18025088	7	26	gly	glycosylated	1550:1561	arg1	75					1570:1571	75	1570:1571	75	1570:1571	Besides substantial increases in the relative levels of unglycosylated triadin-1, proteasome inhibition led to an accumulation of two new modified forms of triadin-1 that were seen with triadin-1 only when it is not glycosylated on Asn(75).
18025088	7	26	gly	glycosylated	1550:1561	arg1	it					1540:1541	it	1540:1541	it	1540:1541	Besides substantial increases in the relative levels of unglycosylated triadin-1, proteasome inhibition led to an accumulation of two new modified forms of triadin-1 that were seen with triadin-1 only when it is not glycosylated on Asn(75).
18025088	0	27	theme	cardiac	82:88	arg1	triadin-1					90:98	actively degrading cardiac triadin-1	63:98	actively degrading cardiac triadin-1	63:98	Inefficient glycosylation leads to high steady-state levels of actively degrading cardiac triadin-1.
18025088	5	28	theme	SDS-PAGE	915:922	arg1	analysis					924:931	SDS-PAGE analysis	915:931	SDS-PAGE analysis	915:931	Although triadin-1 appeared by SDS-PAGE analysis as a 35/40-kDa doublet in all cells, variations occurred in the relative levels of the two glycoforms depending on the cell type and whether overexpression involved a plasmid or adenoviral vector.
18025088	2	29	theme	triadin-1	377:385	arg1	half					369:372	about half	363:372	about half of triadin-1 in the heart	363:398	Calsequestrin and triadin-1 both contain N-linked glycans, but about half of triadin-1 in the heart remains unglycosylated.
18025088	0	30	theme	Inefficient	0:10	arg1	glycosylation					12:24	Inefficient glycosylation	0:24	Inefficient glycosylation	0:24	Inefficient glycosylation leads to high steady-state levels of actively degrading cardiac triadin-1.
18025088	8	31	link	N-linked	1682:1689	arg1	sites					1705:1709	two alternative N-linked glycosylation sites	1666:1709	two alternative N-linked glycosylation sites	1666:1709	Effects of tunicamycin and endoglycosidase H confirmed that these novel isoforms represent two alternative N-linked glycosylation sites, indicating that an alternative topology occurs infrequently leading to yet other glycoforms with short half-lives.
18025088	4	32	theme	triadin	772:778	arg1	proximity					817:825	the close proximity	807:825	the close proximity of Asn(75) to the sarcoplasmic reticulum inner membrane	807:881	We showed that the characteristic incomplete glycosylation stemmed from properties of the glycosylation sequence that are conserved among triadin splice variants, including the close proximity of Asn(75) to the sarcoplasmic reticulum inner membrane.
18025088	4	32	theme	triadin	772:778	arg1	variants					787:794	triadin splice variants	772:794	triadin splice variants	772:794	We showed that the characteristic incomplete glycosylation stemmed from properties of the glycosylation sequence that are conserved among triadin splice variants, including the close proximity of Asn(75) to the sarcoplasmic reticulum inner membrane.
18025088	1	33	theme	sarcoplasmic	115:126	arg1	reticulum					128:136	junctional sarcoplasmic reticulum	104:136	junctional sarcoplasmic reticulum	104:136	In junctional sarcoplasmic reticulum, binding to cardiac triadin-1 provides a mechanism by which the Ca(2+)-release channel/ryanodine receptor may link with calsequestrin to regulate Ca(2+) release.
18025088	0	34	theme	high	35:38	arg1	levels					53:58	high steady-state levels	35:58	high steady-state levels of actively degrading cardiac triadin-1	35:98	Inefficient glycosylation leads to high steady-state levels of actively degrading cardiac triadin-1.
18025088	4	35	dep	showed	637:642	arg1	glycosylation					679:691	the characteristic incomplete glycosylation	649:691	the characteristic incomplete glycosylation stemmed from properties of the glycosylation sequence that are conserved among triadin splice variants, including the close proximity of Asn(75) to the sarcoplasmic reticulum inner membrane	649:881	We showed that the characteristic incomplete glycosylation stemmed from properties of the glycosylation sequence that are conserved among triadin splice variants, including the close proximity of Asn(75) to the sarcoplasmic reticulum inner membrane.
18025088	2	36	from	half	369:372	arg1	heart					394:398	the heart	390:398	the heart	390:398	Calsequestrin and triadin-1 both contain N-linked glycans, but about half of triadin-1 in the heart remains unglycosylated.
18025088	4	37	theme	close	811:815	arg1	proximity					817:825	the close proximity	807:825	the close proximity of Asn(75) to the sarcoplasmic reticulum inner membrane	807:881	We showed that the characteristic incomplete glycosylation stemmed from properties of the glycosylation sequence that are conserved among triadin splice variants, including the close proximity of Asn(75) to the sarcoplasmic reticulum inner membrane.
18025088	1	38	theme	-release	208:215	arg1	receptor					235:242	the Ca(2+)-release channel/ryanodine receptor	198:242	the Ca(2+)-release channel/ryanodine receptor	198:242	In junctional sarcoplasmic reticulum, binding to cardiac triadin-1 provides a mechanism by which the Ca(2+)-release channel/ryanodine receptor may link with calsequestrin to regulate Ca(2+) release.
18025088	5	39	theme	relative	997:1004	arg1	levels					1006:1011	the relative levels	993:1011	the relative levels of the two glycoforms depending on the cell type and whether overexpression involved a plasmid or adenoviral vector	993:1127	Although triadin-1 appeared by SDS-PAGE analysis as a 35/40-kDa doublet in all cells, variations occurred in the relative levels of the two glycoforms depending on the cell type and whether overexpression involved a plasmid or adenoviral vector.
18025088	8	40	theme	tunicamycin	1586:1596	arg1	Effects					1575:1581	Effects	1575:1581	Effects of tunicamycin and endoglycosidase H	1575:1618	Effects of tunicamycin and endoglycosidase H confirmed that these novel isoforms represent two alternative N-linked glycosylation sites, indicating that an alternative topology occurs infrequently leading to yet other glycoforms with short half-lives.
18025088	8	41	theme	endoglycosidase	1602:1616	arg1	H					1618:1618	endoglycosidase H	1602:1618	endoglycosidase H	1602:1618	Effects of tunicamycin and endoglycosidase H confirmed that these novel isoforms represent two alternative N-linked glycosylation sites, indicating that an alternative topology occurs infrequently leading to yet other glycoforms with short half-lives.
18025088	8	42	theme	N-linked	1682:1689	arg1	sites					1705:1709	two alternative N-linked glycosylation sites	1666:1709	two alternative N-linked glycosylation sites	1666:1709	Effects of tunicamycin and endoglycosidase H confirmed that these novel isoforms represent two alternative N-linked glycosylation sites, indicating that an alternative topology occurs infrequently leading to yet other glycoforms with short half-lives.
18025088	7	43	theme	triadin-1	1490:1498	arg1	forms					1481:1485	two new modified forms	1464:1485	two new modified forms of triadin-1 that were seen with triadin-1 only when it is not glycosylated on Asn(75)	1464:1572	Besides substantial increases in the relative levels of unglycosylated triadin-1, proteasome inhibition led to an accumulation of two new modified forms of triadin-1 that were seen with triadin-1 only when it is not glycosylated on Asn(75).
18025088	4	44	theme	inner	868:872	arg1	membrane					874:881	the sarcoplasmic reticulum inner membrane	841:881	the sarcoplasmic reticulum inner membrane	841:881	We showed that the characteristic incomplete glycosylation stemmed from properties of the glycosylation sequence that are conserved among triadin splice variants, including the close proximity of Asn(75) to the sarcoplasmic reticulum inner membrane.
18025088	6	45	theme	unglycosylated	1285:1298	arg1	triadin-1					1323:1331	unglycosylated, but not glycosylated, triadin-1	1285:1331	unglycosylated, but not glycosylated, triadin-1	1285:1331	Treatment of triadin-1 with the proteasome inhibitor MG-132 led to striking changes in the relative levels of triadin-1 that indicated active breakdown of unglycosylated, but not glycosylated, triadin-1.
18025088	3	46	theme	variants	537:544	arg1	triadin-1					502:510	triadin-1	502:510	triadin-1	502:510	To investigate mechanisms for this incomplete glycosylation, we overexpressed triadin-1 as a series of glycoform variants in non-muscle cell lines and neonatal heart cells using plasmid and adenoviral vectors.
18025088	3	46	theme	variants	537:544	arg1	series					517:522	a series	515:522	a series of glycoform variants in non-muscle cell lines and neonatal heart cells using plasmid and adenoviral vectors	515:631	To investigate mechanisms for this incomplete glycosylation, we overexpressed triadin-1 as a series of glycoform variants in non-muscle cell lines and neonatal heart cells using plasmid and adenoviral vectors.
18025088	7	47	theme	forms	1481:1485	arg1	accumulation					1448:1459	an accumulation	1445:1459	an accumulation of two new modified forms of triadin-1 that were seen with triadin-1 only when it is not glycosylated on Asn(75)	1445:1572	Besides substantial increases in the relative levels of unglycosylated triadin-1, proteasome inhibition led to an accumulation of two new modified forms of triadin-1 that were seen with triadin-1 only when it is not glycosylated on Asn(75).
18025088	2	48	link	N-linked	341:348	arg1	glycans					350:356	N-linked glycans	341:356	N-linked glycans	341:356	Calsequestrin and triadin-1 both contain N-linked glycans, but about half of triadin-1 in the heart remains unglycosylated.
18025088	3	49	from	series	517:522	arg1	cells					590:594	neonatal heart cells	575:594	neonatal heart cells	575:594	To investigate mechanisms for this incomplete glycosylation, we overexpressed triadin-1 as a series of glycoform variants in non-muscle cell lines and neonatal heart cells using plasmid and adenoviral vectors.
18025088	3	49	from	series	517:522	arg1	lines					565:569	non-muscle cell lines	549:569	non-muscle cell lines	549:569	To investigate mechanisms for this incomplete glycosylation, we overexpressed triadin-1 as a series of glycoform variants in non-muscle cell lines and neonatal heart cells using plasmid and adenoviral vectors.
18025088	7	50	theme	new	1468:1470	arg1	forms					1481:1485	two new modified forms	1464:1485	two new modified forms of triadin-1 that were seen with triadin-1 only when it is not glycosylated on Asn(75)	1464:1572	Besides substantial increases in the relative levels of unglycosylated triadin-1, proteasome inhibition led to an accumulation of two new modified forms of triadin-1 that were seen with triadin-1 only when it is not glycosylated on Asn(75).
18025088	8	51	gly	glycosylation	1691:1703	arg2	sites					1705:1709	two alternative N-linked glycosylation sites	1666:1709	two alternative N-linked glycosylation sites	1666:1709	Effects of tunicamycin and endoglycosidase H confirmed that these novel isoforms represent two alternative N-linked glycosylation sites, indicating that an alternative topology occurs infrequently leading to yet other glycoforms with short half-lives.
18025088	8	51	gly	glycosylation	1691:1703	arg2	two					1666:1668	two	1666:1668	two	1666:1668	Effects of tunicamycin and endoglycosidase H confirmed that these novel isoforms represent two alternative N-linked glycosylation sites, indicating that an alternative topology occurs infrequently leading to yet other glycoforms with short half-lives.
18025088	6	52	theme	inhibitor	1173:1181	arg1	MG-132					1183:1188	the proteasome inhibitor MG-132	1158:1188	the proteasome inhibitor MG-132	1158:1188	Treatment of triadin-1 with the proteasome inhibitor MG-132 led to striking changes in the relative levels of triadin-1 that indicated active breakdown of unglycosylated, but not glycosylated, triadin-1.
18025088	8	53	with	glycoforms	1793:1802	arg1	half-lives					1815:1824	short half-lives	1809:1824	short half-lives	1809:1824	Effects of tunicamycin and endoglycosidase H confirmed that these novel isoforms represent two alternative N-linked glycosylation sites, indicating that an alternative topology occurs infrequently leading to yet other glycoforms with short half-lives.
18025088	4	54	theme	sarcoplasmic	845:856	arg1	reticulum					858:866	the sarcoplasmic reticulum	841:866	the sarcoplasmic reticulum inner membrane	841:881	We showed that the characteristic incomplete glycosylation stemmed from properties of the glycosylation sequence that are conserved among triadin splice variants, including the close proximity of Asn(75) to the sarcoplasmic reticulum inner membrane.
18025088	4	55	theme	incomplete	668:677	arg1	glycosylation					679:691	the characteristic incomplete glycosylation	649:691	the characteristic incomplete glycosylation stemmed from properties of the glycosylation sequence that are conserved among triadin splice variants, including the close proximity of Asn(75) to the sarcoplasmic reticulum inner membrane	649:881	We showed that the characteristic incomplete glycosylation stemmed from properties of the glycosylation sequence that are conserved among triadin splice variants, including the close proximity of Asn(75) to the sarcoplasmic reticulum inner membrane.
18025088	3	56	theme	non-muscle	549:558	arg1	lines					565:569	non-muscle cell lines	549:569	non-muscle cell lines	549:569	To investigate mechanisms for this incomplete glycosylation, we overexpressed triadin-1 as a series of glycoform variants in non-muscle cell lines and neonatal heart cells using plasmid and adenoviral vectors.
18025088	6	57	gly	unglycosylated	1285:1298	arg1	triadin-1					1323:1331	unglycosylated, but not glycosylated, triadin-1	1285:1331	unglycosylated, but not glycosylated, triadin-1	1285:1331	Treatment of triadin-1 with the proteasome inhibitor MG-132 led to striking changes in the relative levels of triadin-1 that indicated active breakdown of unglycosylated, but not glycosylated, triadin-1.
18025088	6	58	theme	triadin-1	1323:1331	arg1	breakdown					1272:1280	active breakdown	1265:1280	active breakdown of unglycosylated, but not glycosylated, triadin-1	1265:1331	Treatment of triadin-1 with the proteasome inhibitor MG-132 led to striking changes in the relative levels of triadin-1 that indicated active breakdown of unglycosylated, but not glycosylated, triadin-1.
18025088	3	59	theme	neonatal	575:582	arg1	cells					590:594	neonatal heart cells	575:594	neonatal heart cells	575:594	To investigate mechanisms for this incomplete glycosylation, we overexpressed triadin-1 as a series of glycoform variants in non-muscle cell lines and neonatal heart cells using plasmid and adenoviral vectors.
18025088	7	60	theme	unglycosylated	1390:1403	arg1	triadin-1					1405:1413	unglycosylated triadin-1	1390:1413	unglycosylated triadin-1	1390:1413	Besides substantial increases in the relative levels of unglycosylated triadin-1, proteasome inhibition led to an accumulation of two new modified forms of triadin-1 that were seen with triadin-1 only when it is not glycosylated on Asn(75).
18025088	6	61	theme	glycosylated	1309:1320	arg1	triadin-1					1323:1331	unglycosylated, but not glycosylated, triadin-1	1285:1331	unglycosylated, but not glycosylated, triadin-1	1285:1331	Treatment of triadin-1 with the proteasome inhibitor MG-132 led to striking changes in the relative levels of triadin-1 that indicated active breakdown of unglycosylated, but not glycosylated, triadin-1.
18025088	3	62	theme	adenoviral	614:623	arg1	vectors					625:631	adenoviral vectors	614:631	adenoviral vectors	614:631	To investigate mechanisms for this incomplete glycosylation, we overexpressed triadin-1 as a series of glycoform variants in non-muscle cell lines and neonatal heart cells using plasmid and adenoviral vectors.
18025088	8	63	theme	other	1787:1791	arg1	glycoforms					1793:1802	yet other glycoforms	1783:1802	yet other glycoforms with short half-lives	1783:1824	Effects of tunicamycin and endoglycosidase H confirmed that these novel isoforms represent two alternative N-linked glycosylation sites, indicating that an alternative topology occurs infrequently leading to yet other glycoforms with short half-lives.
18025088	4	64	theme	sequence	738:745	arg1	properties					706:715	properties	706:715	properties of the glycosylation sequence that are conserved among triadin splice variants, including the close proximity of Asn(75) to the sarcoplasmic reticulum inner membrane	706:881	We showed that the characteristic incomplete glycosylation stemmed from properties of the glycosylation sequence that are conserved among triadin splice variants, including the close proximity of Asn(75) to the sarcoplasmic reticulum inner membrane.
18025088	3	65	from	lines	565:569	arg1	triadin-1					502:510	triadin-1	502:510	triadin-1	502:510	To investigate mechanisms for this incomplete glycosylation, we overexpressed triadin-1 as a series of glycoform variants in non-muscle cell lines and neonatal heart cells using plasmid and adenoviral vectors.
18025088	3	65	from	lines	565:569	arg1	series					517:522	a series	515:522	a series of glycoform variants in non-muscle cell lines and neonatal heart cells using plasmid and adenoviral vectors	515:631	To investigate mechanisms for this incomplete glycosylation, we overexpressed triadin-1 as a series of glycoform variants in non-muscle cell lines and neonatal heart cells using plasmid and adenoviral vectors.
18025088	0	66	theme	degrading	72:80	arg1	triadin-1					90:98	actively degrading cardiac triadin-1	63:98	actively degrading cardiac triadin-1	63:98	Inefficient glycosylation leads to high steady-state levels of actively degrading cardiac triadin-1.
18025088	1	67	theme	cardiac	150:156	arg1	triadin-1					158:166	cardiac triadin-1	150:166	cardiac triadin-1	150:166	In junctional sarcoplasmic reticulum, binding to cardiac triadin-1 provides a mechanism by which the Ca(2+)-release channel/ryanodine receptor may link with calsequestrin to regulate Ca(2+) release.
18025088	6	68	theme	striking	1197:1204	arg1	changes					1206:1212	striking changes	1197:1212	striking changes in the relative levels of triadin-1 that indicated active breakdown of unglycosylated, but not glycosylated, triadin-1	1197:1331	Treatment of triadin-1 with the proteasome inhibitor MG-132 led to striking changes in the relative levels of triadin-1 that indicated active breakdown of unglycosylated, but not glycosylated, triadin-1.
18025088	6	69	from	changes	1206:1212	arg1	levels					1230:1235	the relative levels	1217:1235	the relative levels of triadin-1	1217:1248	Treatment of triadin-1 with the proteasome inhibitor MG-132 led to striking changes in the relative levels of triadin-1 that indicated active breakdown of unglycosylated, but not glycosylated, triadin-1.
18025088	0	70	theme	triadin-1	90:98	arg1	levels					53:58	high steady-state levels	35:58	high steady-state levels of actively degrading cardiac triadin-1	35:98	Inefficient glycosylation leads to high steady-state levels of actively degrading cardiac triadin-1.
18025088	3	71	from	variants	537:544	arg1	cells					590:594	neonatal heart cells	575:594	neonatal heart cells	575:594	To investigate mechanisms for this incomplete glycosylation, we overexpressed triadin-1 as a series of glycoform variants in non-muscle cell lines and neonatal heart cells using plasmid and adenoviral vectors.
18025088	3	71	from	variants	537:544	arg1	lines					565:569	non-muscle cell lines	549:569	non-muscle cell lines	549:569	To investigate mechanisms for this incomplete glycosylation, we overexpressed triadin-1 as a series of glycoform variants in non-muscle cell lines and neonatal heart cells using plasmid and adenoviral vectors.
18025088	2	72	contain	contain	333:339	arg2	glycans					350:356	N-linked glycans	341:356	N-linked glycans	341:356	Calsequestrin and triadin-1 both contain N-linked glycans, but about half of triadin-1 in the heart remains unglycosylated.
18025088	2	72	contain	contain	333:339	arg1	triadin-1					318:326	triadin-1	318:326	triadin-1	318:326	Calsequestrin and triadin-1 both contain N-linked glycans, but about half of triadin-1 in the heart remains unglycosylated.
18025088	2	72	contain	contain	333:339	arg1	Calsequestrin					300:312	Calsequestrin	300:312	Calsequestrin	300:312	Calsequestrin and triadin-1 both contain N-linked glycans, but about half of triadin-1 in the heart remains unglycosylated.
18025088	6	73	theme	triadin-1	1143:1151	arg1	Treatment					1130:1138	Treatment	1130:1138	Treatment of triadin-1 with the proteasome inhibitor MG-132	1130:1188	Treatment of triadin-1 with the proteasome inhibitor MG-132 led to striking changes in the relative levels of triadin-1 that indicated active breakdown of unglycosylated, but not glycosylated, triadin-1.
18025088	4	74	theme	splice	780:785	arg1	proximity					817:825	the close proximity	807:825	the close proximity of Asn(75) to the sarcoplasmic reticulum inner membrane	807:881	We showed that the characteristic incomplete glycosylation stemmed from properties of the glycosylation sequence that are conserved among triadin splice variants, including the close proximity of Asn(75) to the sarcoplasmic reticulum inner membrane.
18025088	4	74	theme	splice	780:785	arg1	variants					787:794	triadin splice variants	772:794	triadin splice variants	772:794	We showed that the characteristic incomplete glycosylation stemmed from properties of the glycosylation sequence that are conserved among triadin splice variants, including the close proximity of Asn(75) to the sarcoplasmic reticulum inner membrane.
18025088	8	75	theme	alternative	1670:1680	arg1	sites					1705:1709	two alternative N-linked glycosylation sites	1666:1709	two alternative N-linked glycosylation sites	1666:1709	Effects of tunicamycin and endoglycosidase H confirmed that these novel isoforms represent two alternative N-linked glycosylation sites, indicating that an alternative topology occurs infrequently leading to yet other glycoforms with short half-lives.
18025088	7	76	theme	substantial	1342:1352	arg1	increases					1354:1362	substantial increases	1342:1362	substantial increases in the relative levels of unglycosylated triadin-1	1342:1413	Besides substantial increases in the relative levels of unglycosylated triadin-1, proteasome inhibition led to an accumulation of two new modified forms of triadin-1 that were seen with triadin-1 only when it is not glycosylated on Asn(75).
18025088	5	77	theme	adenoviral	1111:1120	arg1	vector					1122:1127	adenoviral vector	1111:1127	adenoviral vector	1111:1127	Although triadin-1 appeared by SDS-PAGE analysis as a 35/40-kDa doublet in all cells, variations occurred in the relative levels of the two glycoforms depending on the cell type and whether overexpression involved a plasmid or adenoviral vector.
18025088	1	78	theme	Ca	284:285	arg1	release					291:297	Ca(2+) release	284:297	Ca(2+) release	284:297	In junctional sarcoplasmic reticulum, binding to cardiac triadin-1 provides a mechanism by which the Ca(2+)-release channel/ryanodine receptor may link with calsequestrin to regulate Ca(2+) release.
18025088	1	79	theme	junctional	104:113	arg1	reticulum					128:136	junctional sarcoplasmic reticulum	104:136	junctional sarcoplasmic reticulum	104:136	In junctional sarcoplasmic reticulum, binding to cardiac triadin-1 provides a mechanism by which the Ca(2+)-release channel/ryanodine receptor may link with calsequestrin to regulate Ca(2+) release.
18025088	6	80	theme	triadin-1	1240:1248	arg1	levels					1230:1235	the relative levels	1217:1235	the relative levels of triadin-1	1217:1248	Treatment of triadin-1 with the proteasome inhibitor MG-132 led to striking changes in the relative levels of triadin-1 that indicated active breakdown of unglycosylated, but not glycosylated, triadin-1.
18025088	5	81	gly	glycoforms	1024:1033	arg2	type					1057:1060	the cell type	1048:1060	the cell type	1048:1060	Although triadin-1 appeared by SDS-PAGE analysis as a 35/40-kDa doublet in all cells, variations occurred in the relative levels of the two glycoforms depending on the cell type and whether overexpression involved a plasmid or adenoviral vector.
18025088	3	82	from	cells	590:594	arg1	triadin-1					502:510	triadin-1	502:510	triadin-1	502:510	To investigate mechanisms for this incomplete glycosylation, we overexpressed triadin-1 as a series of glycoform variants in non-muscle cell lines and neonatal heart cells using plasmid and adenoviral vectors.
18025088	3	82	from	cells	590:594	arg1	series					517:522	a series	515:522	a series of glycoform variants in non-muscle cell lines and neonatal heart cells using plasmid and adenoviral vectors	515:631	To investigate mechanisms for this incomplete glycosylation, we overexpressed triadin-1 as a series of glycoform variants in non-muscle cell lines and neonatal heart cells using plasmid and adenoviral vectors.
18025088	3	83	theme	incomplete	459:468	arg1	glycosylation					470:482	this incomplete glycosylation	454:482	this incomplete glycosylation	454:482	To investigate mechanisms for this incomplete glycosylation, we overexpressed triadin-1 as a series of glycoform variants in non-muscle cell lines and neonatal heart cells using plasmid and adenoviral vectors.
18025088	0	84	theme	steady-state	40:51	arg1	levels					53:58	high steady-state levels	35:58	high steady-state levels of actively degrading cardiac triadin-1	35:98	Inefficient glycosylation leads to high steady-state levels of actively degrading cardiac triadin-1.
18025088	4	85	theme	Asn	830:832	arg1	proximity					817:825	the close proximity	807:825	the close proximity of Asn(75) to the sarcoplasmic reticulum inner membrane	807:881	We showed that the characteristic incomplete glycosylation stemmed from properties of the glycosylation sequence that are conserved among triadin splice variants, including the close proximity of Asn(75) to the sarcoplasmic reticulum inner membrane.
18025088	5	86	theme	glycoforms	1024:1033	arg1	levels					1006:1011	the relative levels	993:1011	the relative levels of the two glycoforms depending on the cell type and whether overexpression involved a plasmid or adenoviral vector	993:1127	Although triadin-1 appeared by SDS-PAGE analysis as a 35/40-kDa doublet in all cells, variations occurred in the relative levels of the two glycoforms depending on the cell type and whether overexpression involved a plasmid or adenoviral vector.
18025088	5	87	from	doublet	948:954	arg1	cells					963:967	all cells	959:967	all cells	959:967	Although triadin-1 appeared by SDS-PAGE analysis as a 35/40-kDa doublet in all cells, variations occurred in the relative levels of the two glycoforms depending on the cell type and whether overexpression involved a plasmid or adenoviral vector.
18025088	1	88	theme	channel/ryanodine	217:233	arg1	receptor					235:242	the Ca(2+)-release channel/ryanodine receptor	198:242	the Ca(2+)-release channel/ryanodine receptor	198:242	In junctional sarcoplasmic reticulum, binding to cardiac triadin-1 provides a mechanism by which the Ca(2+)-release channel/ryanodine receptor may link with calsequestrin to regulate Ca(2+) release.
18025088	8	89	theme	H	1618:1618	arg1	Effects					1575:1581	Effects	1575:1581	Effects of tunicamycin and endoglycosidase H	1575:1618	Effects of tunicamycin and endoglycosidase H confirmed that these novel isoforms represent two alternative N-linked glycosylation sites, indicating that an alternative topology occurs infrequently leading to yet other glycoforms with short half-lives.
18025088	8	90	theme	glycosylation	1691:1703	arg1	sites					1705:1709	two alternative N-linked glycosylation sites	1666:1709	two alternative N-linked glycosylation sites	1666:1709	Effects of tunicamycin and endoglycosidase H confirmed that these novel isoforms represent two alternative N-linked glycosylation sites, indicating that an alternative topology occurs infrequently leading to yet other glycoforms with short half-lives.
23263199	4	0	theme	truncated	530:538	arg1	variants					540:547	truncated variants	530:547	truncated variants of human fucosyltransferase IX containing the soluble extracellular catalytic domain	530:632	We produced truncated variants of human fucosyltransferase IX containing the soluble extracellular catalytic domain.
23263199	5	1	theme	mutant	706:711	arg1	DNAs					713:716	several genomic mutant DNAs	690:716	several genomic mutant DNAs encoding a glutamine (Gln/Q) instead of the asparagine residue	690:779	To analyze the relevance of each N-glycosylation site, several genomic mutant DNAs encoding a glutamine (Gln/Q) instead of the asparagine residue were created prosperously using site-directed mutagenesis and subsequently expressed in Spodoptera frugiperda cells applying a baculovirus expression system.
23263199	9	2	gly	N-glycosylation	1542:1556	arg2	more					1528:1531	more	1528:1531	more	1528:1531	The same could be observed for variants missing two or more putative N-glycosylation sites, which indicated the importance of N-glycosylation for enzyme stability and activity.
23263199	9	2	gly	N-glycosylation	1542:1556	arg2	two					1521:1523	two	1521:1523	two	1521:1523	The same could be observed for variants missing two or more putative N-glycosylation sites, which indicated the importance of N-glycosylation for enzyme stability and activity.
23263199	9	2	gly	N-glycosylation	1542:1556	arg2	sites					1558:1562	two or more putative N-glycosylation sites	1521:1562	two or more putative N-glycosylation sites	1521:1562	The same could be observed for variants missing two or more putative N-glycosylation sites, which indicated the importance of N-glycosylation for enzyme stability and activity.
23263199	6	3	theme	IX	1005:1006	arg1	production					945:954	production	945:954	production	945:954	After production and purification of these variants of human FucT IX, the wild-type (wt) enzyme and the variants were characterized regarding their activity and kinetic properties.
23263199	6	3	theme	IX	1005:1006	arg1	purification					960:971	purification	960:971	purification	960:971	After production and purification of these variants of human FucT IX, the wild-type (wt) enzyme and the variants were characterized regarding their activity and kinetic properties.
23263199	4	4	theme	human	552:556	arg1	IX					577:578	human fucosyltransferase IX	552:578	human fucosyltransferase IX containing the soluble extracellular catalytic domain	552:632	We produced truncated variants of human fucosyltransferase IX containing the soluble extracellular catalytic domain.
23263199	7	5	theme	N-glycosylation	1196:1210	arg1	sites					1212:1216	the individual N-glycosylation sites	1181:1216	the individual N-glycosylation sites	1181:1216	The variants showed lower activity than the wt FucT, whereas the individual N-glycosylation sites had different effects on the enzyme activity and kinetic parameters.
23263199	1	6	from	diphosphate-β-L-fucose	175:196	arg1	transfer					139:146	the transfer	135:146	the transfer of l-fucose from guanosine diphosphate-β-L-fucose to N-acetyllactosamine	135:219	Human α1,3-fucosyltransferase IX catalyzes the transfer of l-fucose from guanosine diphosphate-β-L-fucose to N-acetyllactosamine, generating a Lewis X epitope, and is thereby involved in the synthesis of fucosylated cell surface glycoconjugates.
23263199	7	7	theme	individual	1185:1194	arg1	sites					1212:1216	the individual N-glycosylation sites	1181:1216	the individual N-glycosylation sites	1181:1216	The variants showed lower activity than the wt FucT, whereas the individual N-glycosylation sites had different effects on the enzyme activity and kinetic parameters.
23263199	6	8	theme	human	994:998	arg1	IX					1005:1006	human FucT IX	994:1006	human FucT IX	994:1006	After production and purification of these variants of human FucT IX, the wild-type (wt) enzyme and the variants were characterized regarding their activity and kinetic properties.
23263199	8	9	theme	single	1297:1302	arg1	N62Q					1312:1315	the single variant N62Q	1293:1315	the single variant N62Q	1293:1315	While the single variant N62Q still showed ∼60% of wt activity and N101Q retained ∼30% activity, replacement of Asn153 by glutamine led to an almost complete loss of enzymatic activity.
23263199	4	10	contain	containing	580:589	arg2	domain					627:632	the soluble extracellular catalytic domain	591:632	the soluble extracellular catalytic domain	591:632	We produced truncated variants of human fucosyltransferase IX containing the soluble extracellular catalytic domain.
23263199	4	10	contain	containing	580:589	arg1	IX					577:578	human fucosyltransferase IX	552:578	human fucosyltransferase IX containing the soluble extracellular catalytic domain	552:632	We produced truncated variants of human fucosyltransferase IX containing the soluble extracellular catalytic domain.
23263199	9	11	theme	enzyme	1619:1624	arg1	stability					1626:1634	enzyme stability	1619:1634	enzyme stability	1619:1634	The same could be observed for variants missing two or more putative N-glycosylation sites, which indicated the importance of N-glycosylation for enzyme stability and activity.
23263199	2	12	theme	putative	356:363	arg1	sites					381:385	three putative N-glycosylation sites	350:385	three putative N-glycosylation sites	350:385	It contains three putative N-glycosylation sites (Asn62, Asn101 and Asn153).
23263199	6	13	theme	variants	982:989	arg1	production					945:954	production	945:954	production	945:954	After production and purification of these variants of human FucT IX, the wild-type (wt) enzyme and the variants were characterized regarding their activity and kinetic properties.
23263199	6	13	theme	variants	982:989	arg1	purification					960:971	purification	960:971	purification	960:971	After production and purification of these variants of human FucT IX, the wild-type (wt) enzyme and the variants were characterized regarding their activity and kinetic properties.
23263199	5	14	theme	site	684:687	arg1	relevance					650:658	the relevance	646:658	the relevance of each N-glycosylation site	646:687	To analyze the relevance of each N-glycosylation site, several genomic mutant DNAs encoding a glutamine (Gln/Q) instead of the asparagine residue were created prosperously using site-directed mutagenesis and subsequently expressed in Spodoptera frugiperda cells applying a baculovirus expression system.
23263199	5	15	theme	expression	920:929	arg1	system					931:936	a baculovirus expression system	906:936	a baculovirus expression system	906:936	To analyze the relevance of each N-glycosylation site, several genomic mutant DNAs encoding a glutamine (Gln/Q) instead of the asparagine residue were created prosperously using site-directed mutagenesis and subsequently expressed in Spodoptera frugiperda cells applying a baculovirus expression system.
23263199	9	16	theme	N-glycosylation	1599:1613	arg1	importance					1585:1594	the importance	1581:1594	the importance of N-glycosylation for enzyme stability and activity	1581:1647	The same could be observed for variants missing two or more putative N-glycosylation sites, which indicated the importance of N-glycosylation for enzyme stability and activity.
23263199	7	17	gly	N-glycosylation	1196:1210	arg2	sites					1212:1216	the individual N-glycosylation sites	1181:1216	the individual N-glycosylation sites	1181:1216	The variants showed lower activity than the wt FucT, whereas the individual N-glycosylation sites had different effects on the enzyme activity and kinetic parameters.
23263199	7	18	theme	kinetic	1267:1273	arg1	parameters					1275:1284	kinetic parameters	1267:1284	kinetic parameters	1267:1284	The variants showed lower activity than the wt FucT, whereas the individual N-glycosylation sites had different effects on the enzyme activity and kinetic parameters.
23263199	6	19	theme	wild-type	1013:1021	arg1	enzyme					1028:1033	the wild-type (wt) enzyme and the variants	1009:1050	enzyme	1028:1033	After production and purification of these variants of human FucT IX, the wild-type (wt) enzyme and the variants were characterized regarding their activity and kinetic properties.
23263199	5	20	theme	frugiperda	880:889	arg1	cells					891:895	Spodoptera frugiperda cells	869:895	Spodoptera frugiperda cells applying a baculovirus expression system	869:936	To analyze the relevance of each N-glycosylation site, several genomic mutant DNAs encoding a glutamine (Gln/Q) instead of the asparagine residue were created prosperously using site-directed mutagenesis and subsequently expressed in Spodoptera frugiperda cells applying a baculovirus expression system.
23263199	4	21	theme	catalytic	617:625	arg1	domain					627:632	the soluble extracellular catalytic domain	591:632	the soluble extracellular catalytic domain	591:632	We produced truncated variants of human fucosyltransferase IX containing the soluble extracellular catalytic domain.
23263199	5	22	theme	several	690:696	arg1	DNAs					713:716	several genomic mutant DNAs	690:716	several genomic mutant DNAs encoding a glutamine (Gln/Q) instead of the asparagine residue	690:779	To analyze the relevance of each N-glycosylation site, several genomic mutant DNAs encoding a glutamine (Gln/Q) instead of the asparagine residue were created prosperously using site-directed mutagenesis and subsequently expressed in Spodoptera frugiperda cells applying a baculovirus expression system.
23263199	4	23	theme	extracellular	603:615	arg1	domain					627:632	the soluble extracellular catalytic domain	591:632	the soluble extracellular catalytic domain	591:632	We produced truncated variants of human fucosyltransferase IX containing the soluble extracellular catalytic domain.
23263199	1	24	theme	Human	92:96	arg1	IX					122:123	Human α1,3-fucosyltransferase IX	92:123	Human α1,3-fucosyltransferase IX	92:123	Human α1,3-fucosyltransferase IX catalyzes the transfer of l-fucose from guanosine diphosphate-β-L-fucose to N-acetyllactosamine, generating a Lewis X epitope, and is thereby involved in the synthesis of fucosylated cell surface glycoconjugates.
23263199	7	25	theme	enzyme	1247:1252	arg1	activity					1254:1261	the enzyme activity	1243:1261	the enzyme activity	1243:1261	The variants showed lower activity than the wt FucT, whereas the individual N-glycosylation sites had different effects on the enzyme activity and kinetic parameters.
23263199	3	26	theme	functional	447:456	arg1	role					458:461	the functional role	443:461	the functional role of these potential N-glycosylations within the enzyme	443:515	The current study considers the functional role of these potential N-glycosylations within the enzyme.
23263199	6	27	theme	FucT	1000:1003	arg1	IX					1005:1006	human FucT IX	994:1006	human FucT IX	994:1006	After production and purification of these variants of human FucT IX, the wild-type (wt) enzyme and the variants were characterized regarding their activity and kinetic properties.
23263199	1	28	theme	fucosylated	296:306	arg1	glycoconjugates					321:335	fucosylated cell surface glycoconjugates	296:335	fucosylated cell surface glycoconjugates	296:335	Human α1,3-fucosyltransferase IX catalyzes the transfer of l-fucose from guanosine diphosphate-β-L-fucose to N-acetyllactosamine, generating a Lewis X epitope, and is thereby involved in the synthesis of fucosylated cell surface glycoconjugates.
23263199	5	29	theme	genomic	698:704	arg1	DNAs					713:716	several genomic mutant DNAs	690:716	several genomic mutant DNAs encoding a glutamine (Gln/Q) instead of the asparagine residue	690:779	To analyze the relevance of each N-glycosylation site, several genomic mutant DNAs encoding a glutamine (Gln/Q) instead of the asparagine residue were created prosperously using site-directed mutagenesis and subsequently expressed in Spodoptera frugiperda cells applying a baculovirus expression system.
23263199	1	30	theme	α1,3-fucosyltransferase	98:120	arg1	IX					122:123	Human α1,3-fucosyltransferase IX	92:123	Human α1,3-fucosyltransferase IX	92:123	Human α1,3-fucosyltransferase IX catalyzes the transfer of l-fucose from guanosine diphosphate-β-L-fucose to N-acetyllactosamine, generating a Lewis X epitope, and is thereby involved in the synthesis of fucosylated cell surface glycoconjugates.
23263199	0	31	theme	α1,3-fucosyltransferase	26:48	arg1	IX					50:51	human α1,3-fucosyltransferase IX	20:51	human α1,3-fucosyltransferase IX	20:51	N-glycosylations of human α1,3-fucosyltransferase IX are required for full enzyme activity.
23263199	1	32	theme	cell	308:311	arg1	glycoconjugates					321:335	fucosylated cell surface glycoconjugates	296:335	fucosylated cell surface glycoconjugates	296:335	Human α1,3-fucosyltransferase IX catalyzes the transfer of l-fucose from guanosine diphosphate-β-L-fucose to N-acetyllactosamine, generating a Lewis X epitope, and is thereby involved in the synthesis of fucosylated cell surface glycoconjugates.
23263199	5	33	theme	N-glycosylation	668:682	arg1	site					684:687	each N-glycosylation site	663:687	each N-glycosylation site	663:687	To analyze the relevance of each N-glycosylation site, several genomic mutant DNAs encoding a glutamine (Gln/Q) instead of the asparagine residue were created prosperously using site-directed mutagenesis and subsequently expressed in Spodoptera frugiperda cells applying a baculovirus expression system.
23263199	7	34	contain	had	1218:1220	arg1	sites					1212:1216	the individual N-glycosylation sites	1181:1216	the individual N-glycosylation sites	1181:1216	The variants showed lower activity than the wt FucT, whereas the individual N-glycosylation sites had different effects on the enzyme activity and kinetic parameters.
23263199	7	34	contain	had	1218:1220	arg2	effects					1232:1238	different effects	1222:1238	different effects	1222:1238	The variants showed lower activity than the wt FucT, whereas the individual N-glycosylation sites had different effects on the enzyme activity and kinetic parameters.
23263199	1	35	theme	Lewis	235:239	arg1	epitope					243:249	a Lewis X epitope	233:249	a Lewis X epitope	233:249	Human α1,3-fucosyltransferase IX catalyzes the transfer of l-fucose from guanosine diphosphate-β-L-fucose to N-acetyllactosamine, generating a Lewis X epitope, and is thereby involved in the synthesis of fucosylated cell surface glycoconjugates.
23263199	0	36	theme	human	20:24	arg1	IX					50:51	human α1,3-fucosyltransferase IX	20:51	human α1,3-fucosyltransferase IX	20:51	N-glycosylations of human α1,3-fucosyltransferase IX are required for full enzyme activity.
23263199	1	37	theme	surface	313:319	arg1	glycoconjugates					321:335	fucosylated cell surface glycoconjugates	296:335	fucosylated cell surface glycoconjugates	296:335	Human α1,3-fucosyltransferase IX catalyzes the transfer of l-fucose from guanosine diphosphate-β-L-fucose to N-acetyllactosamine, generating a Lewis X epitope, and is thereby involved in the synthesis of fucosylated cell surface glycoconjugates.
23263199	9	38	theme	N-glycosylation	1542:1556	arg1	sites					1558:1562	two or more putative N-glycosylation sites	1521:1562	two or more putative N-glycosylation sites	1521:1562	The same could be observed for variants missing two or more putative N-glycosylation sites, which indicated the importance of N-glycosylation for enzyme stability and activity.
23263199	6	39	dep	wild-type	1013:1021	arg1	wt					1024:1025	wt	1024:1025	wt	1024:1025	After production and purification of these variants of human FucT IX, the wild-type (wt) enzyme and the variants were characterized regarding their activity and kinetic properties.
23263199	2	40	dep	contains	341:348	arg1	Asn153					406:411	Asn153	406:411	Asn153	406:411	It contains three putative N-glycosylation sites (Asn62, Asn101 and Asn153).
23263199	2	40	dep	contains	341:348	arg1	Asn101					395:400	Asn101	395:400	Asn101	395:400	It contains three putative N-glycosylation sites (Asn62, Asn101 and Asn153).
23263199	2	40	dep	contains	341:348	arg1	Asn62					388:392	Asn62	388:392	Asn62	388:392	It contains three putative N-glycosylation sites (Asn62, Asn101 and Asn153).
23263199	1	41	theme	X	241:241	arg1	epitope					243:249	a Lewis X epitope	233:249	a Lewis X epitope	233:249	Human α1,3-fucosyltransferase IX catalyzes the transfer of l-fucose from guanosine diphosphate-β-L-fucose to N-acetyllactosamine, generating a Lewis X epitope, and is thereby involved in the synthesis of fucosylated cell surface glycoconjugates.
23263199	7	42	theme	different	1222:1230	arg1	effects					1232:1238	different effects	1222:1238	different effects	1222:1238	The variants showed lower activity than the wt FucT, whereas the individual N-glycosylation sites had different effects on the enzyme activity and kinetic parameters.
23263199	1	43	theme	glycoconjugates	321:335	arg1	synthesis					283:291	the synthesis	279:291	the synthesis of fucosylated cell surface glycoconjugates	279:335	Human α1,3-fucosyltransferase IX catalyzes the transfer of l-fucose from guanosine diphosphate-β-L-fucose to N-acetyllactosamine, generating a Lewis X epitope, and is thereby involved in the synthesis of fucosylated cell surface glycoconjugates.
23263199	8	44	theme	activity	1341:1348	arg1	%					1333:1333	∼60%	1330:1333	∼60% of wt activity	1330:1348	While the single variant N62Q still showed ∼60% of wt activity and N101Q retained ∼30% activity, replacement of Asn153 by glutamine led to an almost complete loss of enzymatic activity.
23263199	8	44	theme	activity	1341:1348	arg1	activity					1341:1348	wt activity	1338:1348	wt activity	1338:1348	While the single variant N62Q still showed ∼60% of wt activity and N101Q retained ∼30% activity, replacement of Asn153 by glutamine led to an almost complete loss of enzymatic activity.
23263199	0	45	gly	N-glycosylations	0:15	arg1	IX					50:51	human α1,3-fucosyltransferase IX	20:51	human α1,3-fucosyltransferase IX	20:51	N-glycosylations of human α1,3-fucosyltransferase IX are required for full enzyme activity.
23263199	8	46	theme	∼30	1369:1371	arg1	%					1372:1372	%	1372:1372	%	1372:1372	While the single variant N62Q still showed ∼60% of wt activity and N101Q retained ∼30% activity, replacement of Asn153 by glutamine led to an almost complete loss of enzymatic activity.
23263199	3	47	theme	potential	472:480	arg1	N-glycosylations					482:497	these potential N-glycosylations	466:497	these potential N-glycosylations	466:497	The current study considers the functional role of these potential N-glycosylations within the enzyme.
23263199	0	48	theme	IX	50:51	arg1	N-glycosylations					0:15	N-glycosylations	0:15	N-glycosylations of human α1,3-fucosyltransferase IX	0:51	N-glycosylations of human α1,3-fucosyltransferase IX are required for full enzyme activity.
23263199	4	49	theme	IX	577:578	arg1	variants					540:547	truncated variants	530:547	truncated variants of human fucosyltransferase IX containing the soluble extracellular catalytic domain	530:632	We produced truncated variants of human fucosyltransferase IX containing the soluble extracellular catalytic domain.
23263199	5	50	theme	asparagine	762:771	arg1	residue					773:779	the asparagine residue	758:779	a glutamine (Gln/Q) instead of the asparagine residue	727:779	To analyze the relevance of each N-glycosylation site, several genomic mutant DNAs encoding a glutamine (Gln/Q) instead of the asparagine residue were created prosperously using site-directed mutagenesis and subsequently expressed in Spodoptera frugiperda cells applying a baculovirus expression system.
23263199	8	51	theme	%	1372:1372	arg1	activity					1374:1381	∼30% activity	1369:1381	∼30% activity	1369:1381	While the single variant N62Q still showed ∼60% of wt activity and N101Q retained ∼30% activity, replacement of Asn153 by glutamine led to an almost complete loss of enzymatic activity.
23263199	8	52	theme	complete	1436:1443	arg1	loss					1445:1448	an almost complete loss	1426:1448	an almost complete loss of enzymatic activity	1426:1470	While the single variant N62Q still showed ∼60% of wt activity and N101Q retained ∼30% activity, replacement of Asn153 by glutamine led to an almost complete loss of enzymatic activity.
23263199	3	53	theme	N-glycosylations	482:497	arg1	role					458:461	the functional role	443:461	the functional role of these potential N-glycosylations within the enzyme	443:515	The current study considers the functional role of these potential N-glycosylations within the enzyme.
23263199	3	54	theme	current	419:425	arg1	study					427:431	The current study	415:431	The current study	415:431	The current study considers the functional role of these potential N-glycosylations within the enzyme.
23263199	4	55	theme	fucosyltransferase	558:575	arg1	IX					577:578	human fucosyltransferase IX	552:578	human fucosyltransferase IX containing the soluble extracellular catalytic domain	552:632	We produced truncated variants of human fucosyltransferase IX containing the soluble extracellular catalytic domain.
23263199	8	56	theme	Asn153	1399:1404	arg1	replacement					1384:1394	replacement	1384:1394	replacement of Asn153 by glutamine	1384:1417	While the single variant N62Q still showed ∼60% of wt activity and N101Q retained ∼30% activity, replacement of Asn153 by glutamine led to an almost complete loss of enzymatic activity.
23263199	4	57	theme	soluble	595:601	arg1	domain					627:632	the soluble extracellular catalytic domain	591:632	the soluble extracellular catalytic domain	591:632	We produced truncated variants of human fucosyltransferase IX containing the soluble extracellular catalytic domain.
23263199	8	58	theme	enzymatic	1453:1461	arg1	activity					1463:1470	enzymatic activity	1453:1470	enzymatic activity	1453:1470	While the single variant N62Q still showed ∼60% of wt activity and N101Q retained ∼30% activity, replacement of Asn153 by glutamine led to an almost complete loss of enzymatic activity.
23263199	1	59	gly	fucosylated	296:306	arg1	glycoconjugates					321:335	fucosylated cell surface glycoconjugates	296:335	fucosylated cell surface glycoconjugates	296:335	Human α1,3-fucosyltransferase IX catalyzes the transfer of l-fucose from guanosine diphosphate-β-L-fucose to N-acetyllactosamine, generating a Lewis X epitope, and is thereby involved in the synthesis of fucosylated cell surface glycoconjugates.
23263199	7	60	theme	lower	1140:1144	arg1	activity					1146:1153	lower activity	1140:1153	lower activity	1140:1153	The variants showed lower activity than the wt FucT, whereas the individual N-glycosylation sites had different effects on the enzyme activity and kinetic parameters.
23263199	5	61	theme	Spodoptera	869:878	arg1	frugiperda					880:889	Spodoptera frugiperda	869:889	Spodoptera frugiperda cells applying a baculovirus expression system	869:936	To analyze the relevance of each N-glycosylation site, several genomic mutant DNAs encoding a glutamine (Gln/Q) instead of the asparagine residue were created prosperously using site-directed mutagenesis and subsequently expressed in Spodoptera frugiperda cells applying a baculovirus expression system.
23263199	2	62	contain	contains	341:348	arg1	It					338:339	It	338:339	It	338:339	It contains three putative N-glycosylation sites (Asn62, Asn101 and Asn153).
23263199	2	62	contain	contains	341:348	arg2	sites					381:385	three putative N-glycosylation sites	350:385	three putative N-glycosylation sites	350:385	It contains three putative N-glycosylation sites (Asn62, Asn101 and Asn153).
23263199	9	63	theme	putative	1533:1540	arg1	sites					1558:1562	two or more putative N-glycosylation sites	1521:1562	two or more putative N-glycosylation sites	1521:1562	The same could be observed for variants missing two or more putative N-glycosylation sites, which indicated the importance of N-glycosylation for enzyme stability and activity.
23263199	8	64	dep	showed	1323:1328	arg1	retained					1360:1367	retained	1360:1367	showed ∼60% of wt activity and N101Q retained ∼30% activity	1323:1381	While the single variant N62Q still showed ∼60% of wt activity and N101Q retained ∼30% activity, replacement of Asn153 by glutamine led to an almost complete loss of enzymatic activity.
23263199	5	65	theme	site-directed	813:825	arg1	mutagenesis					827:837	site-directed mutagenesis	813:837	site-directed mutagenesis	813:837	To analyze the relevance of each N-glycosylation site, several genomic mutant DNAs encoding a glutamine (Gln/Q) instead of the asparagine residue were created prosperously using site-directed mutagenesis and subsequently expressed in Spodoptera frugiperda cells applying a baculovirus expression system.
23263199	2	66	theme	N-glycosylation	365:379	arg1	sites					381:385	three putative N-glycosylation sites	350:385	three putative N-glycosylation sites	350:385	It contains three putative N-glycosylation sites (Asn62, Asn101 and Asn153).
23263199	6	67	theme	kinetic	1100:1106	arg1	properties					1108:1117	kinetic properties	1100:1117	kinetic properties	1100:1117	After production and purification of these variants of human FucT IX, the wild-type (wt) enzyme and the variants were characterized regarding their activity and kinetic properties.
23263199	2	68	gly	N-glycosylation	365:379	arg2	three					350:354	three	350:354	three	350:354	It contains three putative N-glycosylation sites (Asn62, Asn101 and Asn153).
23263199	2	68	gly	N-glycosylation	365:379	arg2	sites					381:385	three putative N-glycosylation sites	350:385	three putative N-glycosylation sites	350:385	It contains three putative N-glycosylation sites (Asn62, Asn101 and Asn153).
23263199	8	69	theme	activity	1463:1470	arg1	loss					1445:1448	an almost complete loss	1426:1448	an almost complete loss of enzymatic activity	1426:1470	While the single variant N62Q still showed ∼60% of wt activity and N101Q retained ∼30% activity, replacement of Asn153 by glutamine led to an almost complete loss of enzymatic activity.
23263199	1	70	theme	l-fucose	151:158	arg1	transfer					139:146	the transfer	135:146	the transfer of l-fucose from guanosine diphosphate-β-L-fucose to N-acetyllactosamine	135:219	Human α1,3-fucosyltransferase IX catalyzes the transfer of l-fucose from guanosine diphosphate-β-L-fucose to N-acetyllactosamine, generating a Lewis X epitope, and is thereby involved in the synthesis of fucosylated cell surface glycoconjugates.
23263199	8	71	theme	variant	1304:1310	arg1	N62Q					1312:1315	the single variant N62Q	1293:1315	the single variant N62Q	1293:1315	While the single variant N62Q still showed ∼60% of wt activity and N101Q retained ∼30% activity, replacement of Asn153 by glutamine led to an almost complete loss of enzymatic activity.
23263199	7	72	theme	wt	1164:1165	arg1	FucT					1167:1170	the wt FucT	1160:1170	the wt FucT	1160:1170	The variants showed lower activity than the wt FucT, whereas the individual N-glycosylation sites had different effects on the enzyme activity and kinetic parameters.
23263199	0	73	theme	enzyme	75:80	arg1	activity					82:89	full enzyme activity	70:89	full enzyme activity	70:89	N-glycosylations of human α1,3-fucosyltransferase IX are required for full enzyme activity.
23263199	8	74	theme	wt	1338:1339	arg1	activity					1341:1348	wt activity	1338:1348	wt activity	1338:1348	While the single variant N62Q still showed ∼60% of wt activity and N101Q retained ∼30% activity, replacement of Asn153 by glutamine led to an almost complete loss of enzymatic activity.
23263199	5	75	theme	baculovirus	908:918	arg1	system					931:936	a baculovirus expression system	906:936	a baculovirus expression system	906:936	To analyze the relevance of each N-glycosylation site, several genomic mutant DNAs encoding a glutamine (Gln/Q) instead of the asparagine residue were created prosperously using site-directed mutagenesis and subsequently expressed in Spodoptera frugiperda cells applying a baculovirus expression system.
23263199	5	76	gly	N-glycosylation	668:682	arg2	site					684:687	each N-glycosylation site	663:687	each N-glycosylation site	663:687	To analyze the relevance of each N-glycosylation site, several genomic mutant DNAs encoding a glutamine (Gln/Q) instead of the asparagine residue were created prosperously using site-directed mutagenesis and subsequently expressed in Spodoptera frugiperda cells applying a baculovirus expression system.
23263199	0	77	theme	full	70:73	arg1	activity					82:89	full enzyme activity	70:89	full enzyme activity	70:89	N-glycosylations of human α1,3-fucosyltransferase IX are required for full enzyme activity.
23263199	1	78	theme	guanosine	165:173	arg1	diphosphate-β-L-fucose					175:196	guanosine diphosphate-β-L-fucose	165:196	guanosine diphosphate-β-L-fucose	165:196	Human α1,3-fucosyltransferase IX catalyzes the transfer of l-fucose from guanosine diphosphate-β-L-fucose to N-acetyllactosamine, generating a Lewis X epitope, and is thereby involved in the synthesis of fucosylated cell surface glycoconjugates.
15869464	10	0	theme	rational	1969:1976	arg1	design					1991:1996	a rational experimental design	1967:1996	a rational experimental design of functional studies aimed at understanding the structural and functional interdependences in diverse biological processes in which OPN is a key molecule	1967:2151	Knowledge about the positions and nature of PTMs in OPN will allow a rational experimental design of functional studies aimed at understanding the structural and functional interdependences in diverse biological processes in which OPN is a key molecule.
15869464	9	1	contain	containing	1786:1795	arg1	devoid					1872:1877	devoid	1872:1877	devoid	1872:1877	The phosphorylations are arranged in clusters of three to five phosphoresidues and the regions containing the glycosylations and the RGD (Arg-Gly-Asp) integrin-binding sequence are devoid of phosphorylations.
15869464	9	1	contain	containing	1786:1795	arg1	regions					1778:1784	the regions	1774:1784	the regions containing the glycosylations and the RGD (Arg-Gly-Asp) integrin-binding sequence	1774:1866	The phosphorylations are arranged in clusters of three to five phosphoresidues and the regions containing the glycosylations and the RGD (Arg-Gly-Asp) integrin-binding sequence are devoid of phosphorylations.
15869464	9	1	contain	containing	1786:1795	arg2	sequence					1859:1866	the RGD (Arg-Gly-Asp) integrin-binding sequence	1820:1866	the RGD (Arg-Gly-Asp) integrin-binding sequence	1820:1866	The phosphorylations are arranged in clusters of three to five phosphoresidues and the regions containing the glycosylations and the RGD (Arg-Gly-Asp) integrin-binding sequence are devoid of phosphorylations.
15869464	9	1	contain	containing	1786:1795	arg2	glycosylations					1801:1814	the glycosylations	1797:1814	the glycosylations	1797:1814	The phosphorylations are arranged in clusters of three to five phosphoresidues and the regions containing the glycosylations and the RGD (Arg-Gly-Asp) integrin-binding sequence are devoid of phosphorylations.
15869464	3	2	theme	Edman	574:578	arg1	degradation					580:590	Edman degradation	574:590	Edman degradation	574:590	Using a combination of Edman degradation and MS analyses, we have characterized the complete phosphorylation and glycosylation pattern of native human OPN.
15869464	1	3	theme	key	288:290	arg1	molecule					292:299	a key molecule	286:299	a key molecule in a multitude of biological processes such as bone mineralization, cancer metastasis, cell-mediated immune response, inflammation and cell survival	286:448	OPN (osteopontin) is an integrin-binding highly phosphorylated glycoprotein, recognized as a key molecule in a multitude of biological processes such as bone mineralization, cancer metastasis, cell-mediated immune response, inflammation and cell survival.
15869464	10	4	theme	functional	2001:2010	arg1	studies					2012:2018	functional studies	2001:2018	functional studies aimed at understanding the structural and functional interdependences in diverse biological processes in which OPN is a key molecule	2001:2151	Knowledge about the positions and nature of PTMs in OPN will allow a rational experimental design of functional studies aimed at understanding the structural and functional interdependences in diverse biological processes in which OPN is a key molecule.
15869464	1	5	from	molecule	292:299	arg1	multitude					306:314	a multitude	304:314	a multitude of biological processes such as bone mineralization, cancer metastasis, cell-mediated immune response, inflammation and cell survival	304:448	OPN (osteopontin) is an integrin-binding highly phosphorylated glycoprotein, recognized as a key molecule in a multitude of biological processes such as bone mineralization, cancer metastasis, cell-mediated immune response, inflammation and cell survival.
15869464	6	6	theme	P	1297:1297	arg1	CKII					1262:1265	CKII	1262:1265	CKII (casein kinase II) [S-X-X-E/S(P)/D]	1262:1301	Six phosphorylations (Ser101, Ser107, Ser175, Ser199, Ser212 and Ser251) are located in the target sequence of CKII (casein kinase II) [S-X-X-E/S(P)/D] and a single phosphorylation, Ser203, is not positioned in the motif of either MGCK or CKII.
15869464	6	6	theme	P	1297:1297	arg1	/D					1299:1300	casein kinase II) [S-X-X-E/S(P)/D	1268:1300	casein kinase II) [S-X-X-E/S(P)/D	1268:1300	Six phosphorylations (Ser101, Ser107, Ser175, Ser199, Ser212 and Ser251) are located in the target sequence of CKII (casein kinase II) [S-X-X-E/S(P)/D] and a single phosphorylation, Ser203, is not positioned in the motif of either MGCK or CKII.
15869464	5	7	dep	phosphorylations	794:809	arg1	Ser287					1006:1011	Ser287	1006:1011	Ser287	1006:1011	There are 29 phosphorylations (Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254, Ser259, Ser264, Ser275, Ser287, Ser292 and Ser294) located in the target sequence of MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D).
15869464	5	7	dep	phosphorylations	794:809	arg1	Ser259					982:987	Ser259	982:987	Ser259	982:987	There are 29 phosphorylations (Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254, Ser259, Ser264, Ser275, Ser287, Ser292 and Ser294) located in the target sequence of MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D).
15869464	5	7	dep	phosphorylations	794:809	arg1	Ser264					990:995	Ser264	990:995	Ser264	990:995	There are 29 phosphorylations (Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254, Ser259, Ser264, Ser275, Ser287, Ser292 and Ser294) located in the target sequence of MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D).
15869464	5	7	dep	phosphorylations	794:809	arg1	Ser292					1014:1019	Ser292	1014:1019	Ser292	1014:1019	There are 29 phosphorylations (Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254, Ser259, Ser264, Ser275, Ser287, Ser292 and Ser294) located in the target sequence of MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D).
15869464	5	7	dep	phosphorylations	794:809	arg1	Ser294					1025:1030	Ser294	1025:1030	Ser294	1025:1030	There are 29 phosphorylations (Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254, Ser259, Ser264, Ser275, Ser287, Ser292 and Ser294) located in the target sequence of MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D).
15869464	5	7	dep	phosphorylations	794:809	arg1	phosphorylations					794:809	29 phosphorylations	791:809	29 phosphorylations (Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254, Ser259, Ser264, Ser275, Ser287, Ser292 and Ser294) located in the target sequence of MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D)	791:1148	There are 29 phosphorylations (Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254, Ser259, Ser264, Ser275, Ser287, Ser292 and Ser294) located in the target sequence of MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D).
15869464	5	7	dep	phosphorylations	794:809	arg1	Ser254					974:979	Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254	812:979	Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254	812:979	There are 29 phosphorylations (Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254, Ser259, Ser264, Ser275, Ser287, Ser292 and Ser294) located in the target sequence of MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D).
15869464	5	7	dep	phosphorylations	794:809	arg1	Ser275					998:1003	Ser275	998:1003	Ser275	998:1003	There are 29 phosphorylations (Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254, Ser259, Ser264, Ser275, Ser287, Ser292 and Ser294) located in the target sequence of MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D).
15869464	3	8	theme	analyses	599:606	arg1	combination					559:569	a combination	557:569	a combination of Edman degradation and MS analyses	557:606	Using a combination of Edman degradation and MS analyses, we have characterized the complete phosphorylation and glycosylation pattern of native human OPN.
15869464	6	9	theme	[S-X-X-E/S	1286:1295	arg1	CKII					1262:1265	CKII	1262:1265	CKII (casein kinase II) [S-X-X-E/S(P)/D]	1262:1301	Six phosphorylations (Ser101, Ser107, Ser175, Ser199, Ser212 and Ser251) are located in the target sequence of CKII (casein kinase II) [S-X-X-E/S(P)/D] and a single phosphorylation, Ser203, is not positioned in the motif of either MGCK or CKII.
15869464	6	9	theme	[S-X-X-E/S	1286:1295	arg1	/D					1299:1300	casein kinase II) [S-X-X-E/S(P)/D	1268:1300	casein kinase II) [S-X-X-E/S(P)/D	1268:1300	Six phosphorylations (Ser101, Ser107, Ser175, Ser199, Ser212 and Ser251) are located in the target sequence of CKII (casein kinase II) [S-X-X-E/S(P)/D] and a single phosphorylation, Ser203, is not positioned in the motif of either MGCK or CKII.
15869464	1	10	theme	immune	402:407	arg1	response					409:416	cell-mediated immune response	388:416	cell-mediated immune response	388:416	OPN (osteopontin) is an integrin-binding highly phosphorylated glycoprotein, recognized as a key molecule in a multitude of biological processes such as bone mineralization, cancer metastasis, cell-mediated immune response, inflammation and cell survival.
15869464	9	11	theme	phosphoresidues	1754:1768	arg1	clusters					1728:1735	clusters	1728:1735	clusters of three to five phosphoresidues	1728:1768	The phosphorylations are arranged in clusters of three to five phosphoresidues and the regions containing the glycosylations and the RGD (Arg-Gly-Asp) integrin-binding sequence are devoid of phosphorylations.
15869464	0	12	from	clusters	82:89	arg1	located					71:77	located	71:77	located	71:77	Post-translationally modified residues of native human osteopontin are located in clusters: identification of 36 phosphorylation and five O-glycosylation sites and their biological implications.
15869464	9	13	theme	phosphorylations	1882:1897	arg1	devoid					1872:1877	devoid	1872:1877	devoid	1872:1877	The phosphorylations are arranged in clusters of three to five phosphoresidues and the regions containing the glycosylations and the RGD (Arg-Gly-Asp) integrin-binding sequence are devoid of phosphorylations.
15869464	9	13	theme	phosphorylations	1882:1897	arg1	regions					1778:1784	the regions	1774:1784	the regions containing the glycosylations and the RGD (Arg-Gly-Asp) integrin-binding sequence	1774:1866	The phosphorylations are arranged in clusters of three to five phosphoresidues and the regions containing the glycosylations and the RGD (Arg-Gly-Asp) integrin-binding sequence are devoid of phosphorylations.
15869464	0	14	theme	O-glycosylation	138:152	arg1	sites					154:158	36 phosphorylation and five O-glycosylation sites	110:158	sites	154:158	Post-translationally modified residues of native human osteopontin are located in clusters: identification of 36 phosphorylation and five O-glycosylation sites and their biological implications.
15869464	6	15	from	located	1228:1234	arg1	sequence					1250:1257	the target sequence	1239:1257	the target sequence of CKII (casein kinase II) [S-X-X-E/S(P)/D]	1239:1301	Six phosphorylations (Ser101, Ser107, Ser175, Ser199, Ser212 and Ser251) are located in the target sequence of CKII (casein kinase II) [S-X-X-E/S(P)/D] and a single phosphorylation, Ser203, is not positioned in the motif of either MGCK or CKII.
15869464	0	16	located	located	71:77	arg1	clusters					82:89	clusters	82:89	clusters: identification of 36 phosphorylation and five O-glycosylation sites and their biological implications	82:192	Post-translationally modified residues of native human osteopontin are located in clusters: identification of 36 phosphorylation and five O-glycosylation sites and their biological implications.
15869464	0	16	located	located	71:77	arg2	osteopontin					55:65	native human osteopontin	42:65	native human osteopontin	42:65	Post-translationally modified residues of native human osteopontin are located in clusters: identification of 36 phosphorylation and five O-glycosylation sites and their biological implications.
15869464	0	16	located	located	71:77	arg2	residues					30:37	Post-translationally modified residues	0:37	Post-translationally modified residues of native human osteopontin	0:65	Post-translationally modified residues of native human osteopontin are located in clusters: identification of 36 phosphorylation and five O-glycosylation sites and their biological implications.
15869464	6	17	from	positioned	1348:1357	arg1	motif					1366:1370	the motif	1362:1370	the motif of either MGCK or CKII	1362:1393	Six phosphorylations (Ser101, Ser107, Ser175, Ser199, Ser212 and Ser251) are located in the target sequence of CKII (casein kinase II) [S-X-X-E/S(P)/D] and a single phosphorylation, Ser203, is not positioned in the motif of either MGCK or CKII.
15869464	10	18	theme	functional	2062:2071	arg1	interdependences					2073:2088	the structural and functional interdependences	2043:2088	the structural and functional interdependences in diverse biological processes in which OPN is a key molecule	2043:2151	Knowledge about the positions and nature of PTMs in OPN will allow a rational experimental design of functional studies aimed at understanding the structural and functional interdependences in diverse biological processes in which OPN is a key molecule.
15869464	0	19	from	located	71:77	arg1	clusters					82:89	clusters	82:89	clusters: identification of 36 phosphorylation and five O-glycosylation sites and their biological implications	82:192	Post-translationally modified residues of native human osteopontin are located in clusters: identification of 36 phosphorylation and five O-glycosylation sites and their biological implications.
15869464	10	20	from	positions	1920:1928	arg1	OPN					1952:1954	OPN	1952:1954	OPN	1952:1954	Knowledge about the positions and nature of PTMs in OPN will allow a rational experimental design of functional studies aimed at understanding the structural and functional interdependences in diverse biological processes in which OPN is a key molecule.
15869464	10	21	theme	structural	2047:2056	arg1	interdependences					2073:2088	the structural and functional interdependences	2043:2088	the structural and functional interdependences in diverse biological processes in which OPN is a key molecule	2043:2151	Knowledge about the positions and nature of PTMs in OPN will allow a rational experimental design of functional studies aimed at understanding the structural and functional interdependences in diverse biological processes in which OPN is a key molecule.
15869464	6	22	theme	CKII	1390:1393	arg1	motif					1366:1370	the motif	1362:1370	the motif of either MGCK or CKII	1362:1393	Six phosphorylations (Ser101, Ser107, Ser175, Ser199, Ser212 and Ser251) are located in the target sequence of CKII (casein kinase II) [S-X-X-E/S(P)/D] and a single phosphorylation, Ser203, is not positioned in the motif of either MGCK or CKII.
15869464	10	23	from	nature	1934:1939	arg1	OPN					1952:1954	OPN	1952:1954	OPN	1952:1954	Knowledge about the positions and nature of PTMs in OPN will allow a rational experimental design of functional studies aimed at understanding the structural and functional interdependences in diverse biological processes in which OPN is a key molecule.
15869464	5	24	theme	Golgi	1120:1124	arg1	kinase					1126:1131	the Golgi kinase	1116:1131	the Golgi kinase (S/T-X-E/S(P)/D)	1116:1148	There are 29 phosphorylations (Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254, Ser259, Ser264, Ser275, Ser287, Ser292 and Ser294) located in the target sequence of MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D).
15869464	5	24	theme	Golgi	1120:1124	arg1	/D					1146:1147	S/T-X-E/S(P)/D	1134:1147	S/T-X-E/S(P)/D	1134:1147	There are 29 phosphorylations (Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254, Ser259, Ser264, Ser275, Ser287, Ser292 and Ser294) located in the target sequence of MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D).
15869464	0	25	theme	biological	170:179	arg1	implications					181:192	their biological implications	164:192	their biological implications	164:192	Post-translationally modified residues of native human osteopontin are located in clusters: identification of 36 phosphorylation and five O-glycosylation sites and their biological implications.
15869464	6	26	theme	single	1309:1314	arg1	positioned					1348:1357	positioned	1348:1357	positioned	1348:1357	Six phosphorylations (Ser101, Ser107, Ser175, Ser199, Ser212 and Ser251) are located in the target sequence of CKII (casein kinase II) [S-X-X-E/S(P)/D] and a single phosphorylation, Ser203, is not positioned in the motif of either MGCK or CKII.
15869464	6	26	theme	single	1309:1314	arg1	Ser203					1333:1338	Ser203	1333:1338	Ser203	1333:1338	Six phosphorylations (Ser101, Ser107, Ser175, Ser199, Ser212 and Ser251) are located in the target sequence of CKII (casein kinase II) [S-X-X-E/S(P)/D] and a single phosphorylation, Ser203, is not positioned in the motif of either MGCK or CKII.
15869464	6	26	theme	single	1309:1314	arg1	phosphorylation					1316:1330	a single phosphorylation	1307:1330	a single phosphorylation	1307:1330	Six phosphorylations (Ser101, Ser107, Ser175, Ser199, Ser212 and Ser251) are located in the target sequence of CKII (casein kinase II) [S-X-X-E/S(P)/D] and a single phosphorylation, Ser203, is not positioned in the motif of either MGCK or CKII.
15869464	7	27	theme	modification	1451:1462	arg1	degree					1441:1446	the maximal degree	1429:1446	the maximal degree of modification	1429:1462	The 36 phosphoresidues represent the maximal degree of modification since variability at many sites was seen.
15869464	2	28	theme	post-translational	517:534	arg1	PTM					512:514	PTM	512:514	PTM (post-translational modification)	512:548	A significant regulation of OPN function is mediated through PTM (post-translational modification).
15869464	2	28	theme	post-translational	517:534	arg1	modification					536:547	post-translational modification	517:547	post-translational modification	517:547	A significant regulation of OPN function is mediated through PTM (post-translational modification).
15869464	6	29	theme	MGCK	1382:1385	arg1	motif					1366:1370	the motif	1362:1370	the motif of either MGCK or CKII	1362:1393	Six phosphorylations (Ser101, Ser107, Ser175, Ser199, Ser212 and Ser251) are located in the target sequence of CKII (casein kinase II) [S-X-X-E/S(P)/D] and a single phosphorylation, Ser203, is not positioned in the motif of either MGCK or CKII.
15869464	10	30	from	PTMs	1944:1947	arg1	OPN					1952:1954	OPN	1952:1954	OPN	1952:1954	Knowledge about the positions and nature of PTMs in OPN will allow a rational experimental design of functional studies aimed at understanding the structural and functional interdependences in diverse biological processes in which OPN is a key molecule.
15869464	3	31	theme	complete	635:642	arg1	phosphorylation					644:658	the complete phosphorylation and glycosylation pattern	631:684	phosphorylation	644:658	Using a combination of Edman degradation and MS analyses, we have characterized the complete phosphorylation and glycosylation pattern of native human OPN.
15869464	10	32	dep	positions	1920:1928	arg1	the					1916:1918	the	1916:1918	the	1916:1918	Knowledge about the positions and nature of PTMs in OPN will allow a rational experimental design of functional studies aimed at understanding the structural and functional interdependences in diverse biological processes in which OPN is a key molecule.
15869464	9	33	dep	five	1749:1752	arg1	to					1746:1747	to	1746:1747	to	1746:1747	The phosphorylations are arranged in clusters of three to five phosphoresidues and the regions containing the glycosylations and the RGD (Arg-Gly-Asp) integrin-binding sequence are devoid of phosphorylations.
15869464	8	34	used	occupied	1663:1670	arg2	sites					1611:1615	two potential sites	1597:1615	two potential sites for N-glycosylation (Asn63 and Asn90)	1597:1653	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	4	35	theme	phosphoresidues	721:735	arg1	total					709:713	A total	707:713	A total of 36 phosphoresidues	707:735	A total of 36 phosphoresidues have been localized in the sequence of OPN.
15869464	6	36	dep	phosphorylations	1155:1170	arg1	Ser212					1205:1210	Ser212	1205:1210	Ser212	1205:1210	Six phosphorylations (Ser101, Ser107, Ser175, Ser199, Ser212 and Ser251) are located in the target sequence of CKII (casein kinase II) [S-X-X-E/S(P)/D] and a single phosphorylation, Ser203, is not positioned in the motif of either MGCK or CKII.
15869464	6	36	dep	phosphorylations	1155:1170	arg1	Ser107					1181:1186	Ser107	1181:1186	Ser107	1181:1186	Six phosphorylations (Ser101, Ser107, Ser175, Ser199, Ser212 and Ser251) are located in the target sequence of CKII (casein kinase II) [S-X-X-E/S(P)/D] and a single phosphorylation, Ser203, is not positioned in the motif of either MGCK or CKII.
15869464	6	36	dep	phosphorylations	1155:1170	arg1	Ser175					1189:1194	Ser175	1189:1194	Ser175	1189:1194	Six phosphorylations (Ser101, Ser107, Ser175, Ser199, Ser212 and Ser251) are located in the target sequence of CKII (casein kinase II) [S-X-X-E/S(P)/D] and a single phosphorylation, Ser203, is not positioned in the motif of either MGCK or CKII.
15869464	6	36	dep	phosphorylations	1155:1170	arg1	Ser251					1216:1221	Ser251	1216:1221	Ser251	1216:1221	Six phosphorylations (Ser101, Ser107, Ser175, Ser199, Ser212 and Ser251) are located in the target sequence of CKII (casein kinase II) [S-X-X-E/S(P)/D] and a single phosphorylation, Ser203, is not positioned in the motif of either MGCK or CKII.
15869464	6	36	dep	phosphorylations	1155:1170	arg1	phosphorylations					1155:1170	Six phosphorylations	1151:1170	Six phosphorylations (Ser101, Ser107, Ser175, Ser199, Ser212 and Ser251)	1151:1222	Six phosphorylations (Ser101, Ser107, Ser175, Ser199, Ser212 and Ser251) are located in the target sequence of CKII (casein kinase II) [S-X-X-E/S(P)/D] and a single phosphorylation, Ser203, is not positioned in the motif of either MGCK or CKII.
15869464	6	36	dep	phosphorylations	1155:1170	arg1	Ser101					1173:1178	Ser101	1173:1178	Ser101	1173:1178	Six phosphorylations (Ser101, Ser107, Ser175, Ser199, Ser212 and Ser251) are located in the target sequence of CKII (casein kinase II) [S-X-X-E/S(P)/D] and a single phosphorylation, Ser203, is not positioned in the motif of either MGCK or CKII.
15869464	6	36	dep	phosphorylations	1155:1170	arg1	Ser199					1197:1202	Ser199	1197:1202	Ser199	1197:1202	Six phosphorylations (Ser101, Ser107, Ser175, Ser199, Ser212 and Ser251) are located in the target sequence of CKII (casein kinase II) [S-X-X-E/S(P)/D] and a single phosphorylation, Ser203, is not positioned in the motif of either MGCK or CKII.
15869464	0	37	theme	sites	154:158	arg1	identification					92:105	identification	92:105	identification of 36 phosphorylation and five O-glycosylation sites	92:158	Post-translationally modified residues of native human osteopontin are located in clusters: identification of 36 phosphorylation and five O-glycosylation sites and their biological implications.
15869464	0	37	theme	sites	154:158	arg1	implications					181:192	their biological implications	164:192	their biological implications	164:192	Post-translationally modified residues of native human osteopontin are located in clusters: identification of 36 phosphorylation and five O-glycosylation sites and their biological implications.
15869464	8	38	theme	human	1675:1679	arg1	OPN					1686:1688	human milk OPN	1675:1688	human milk OPN	1675:1688	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	1	39	theme	cancer	369:374	arg1	metastasis					376:385	cancer metastasis	369:385	cancer metastasis	369:385	OPN (osteopontin) is an integrin-binding highly phosphorylated glycoprotein, recognized as a key molecule in a multitude of biological processes such as bone mineralization, cancer metastasis, cell-mediated immune response, inflammation and cell survival.
15869464	10	40	theme	biological	2101:2110	arg1	processes					2112:2120	diverse biological processes	2093:2120	diverse biological processes in which OPN is a key molecule	2093:2151	Knowledge about the positions and nature of PTMs in OPN will allow a rational experimental design of functional studies aimed at understanding the structural and functional interdependences in diverse biological processes in which OPN is a key molecule.
15869464	5	41	dep	Ser65	867:871	arg1	Ser46					832:836	Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65	812:871	Ser46	832:836	There are 29 phosphorylations (Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254, Ser259, Ser264, Ser275, Ser287, Ser292 and Ser294) located in the target sequence of MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D).
15869464	5	41	dep	Ser65	867:871	arg1	Ser47					839:843	Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65	812:871	Ser47	839:843	There are 29 phosphorylations (Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254, Ser259, Ser264, Ser275, Ser287, Ser292 and Ser294) located in the target sequence of MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D).
15869464	5	41	dep	Ser65	867:871	arg1	Ser10					818:822	Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65	812:871	Ser10	818:822	There are 29 phosphorylations (Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254, Ser259, Ser264, Ser275, Ser287, Ser292 and Ser294) located in the target sequence of MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D).
15869464	5	41	dep	Ser65	867:871	arg1	Ser11					825:829	Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65	812:871	Ser11	825:829	There are 29 phosphorylations (Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254, Ser259, Ser264, Ser275, Ser287, Ser292 and Ser294) located in the target sequence of MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D).
15869464	5	41	dep	Ser65	867:871	arg1	Thr50					846:850	Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65	812:871	Thr50	846:850	There are 29 phosphorylations (Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254, Ser259, Ser264, Ser275, Ser287, Ser292 and Ser294) located in the target sequence of MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D).
15869464	5	41	dep	Ser65	867:871	arg1	Ser60					853:857	Ser60	853:857	Ser60	853:857	There are 29 phosphorylations (Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254, Ser259, Ser264, Ser275, Ser287, Ser292 and Ser294) located in the target sequence of MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D).
15869464	5	42	theme	located	1033:1039	arg1	Ser287					1006:1011	Ser287	1006:1011	Ser287	1006:1011	There are 29 phosphorylations (Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254, Ser259, Ser264, Ser275, Ser287, Ser292 and Ser294) located in the target sequence of MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D).
15869464	5	42	theme	located	1033:1039	arg1	Ser259					982:987	Ser259	982:987	Ser259	982:987	There are 29 phosphorylations (Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254, Ser259, Ser264, Ser275, Ser287, Ser292 and Ser294) located in the target sequence of MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D).
15869464	5	42	theme	located	1033:1039	arg1	Ser264					990:995	Ser264	990:995	Ser264	990:995	There are 29 phosphorylations (Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254, Ser259, Ser264, Ser275, Ser287, Ser292 and Ser294) located in the target sequence of MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D).
15869464	5	42	theme	located	1033:1039	arg1	Ser292					1014:1019	Ser292	1014:1019	Ser292	1014:1019	There are 29 phosphorylations (Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254, Ser259, Ser264, Ser275, Ser287, Ser292 and Ser294) located in the target sequence of MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D).
15869464	5	42	theme	located	1033:1039	arg1	Ser294					1025:1030	Ser294	1025:1030	Ser294	1025:1030	There are 29 phosphorylations (Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254, Ser259, Ser264, Ser275, Ser287, Ser292 and Ser294) located in the target sequence of MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D).
15869464	5	42	theme	located	1033:1039	arg1	phosphorylations					794:809	29 phosphorylations	791:809	29 phosphorylations (Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254, Ser259, Ser264, Ser275, Ser287, Ser292 and Ser294) located in the target sequence of MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D)	791:1148	There are 29 phosphorylations (Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254, Ser259, Ser264, Ser275, Ser287, Ser292 and Ser294) located in the target sequence of MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D).
15869464	5	42	theme	located	1033:1039	arg1	Ser254					974:979	Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254	812:979	Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254	812:979	There are 29 phosphorylations (Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254, Ser259, Ser264, Ser275, Ser287, Ser292 and Ser294) located in the target sequence of MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D).
15869464	5	42	theme	located	1033:1039	arg1	Ser275					998:1003	Ser275	998:1003	Ser275	998:1003	There are 29 phosphorylations (Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254, Ser259, Ser264, Ser275, Ser287, Ser292 and Ser294) located in the target sequence of MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D).
15869464	0	43	dep	clusters	82:89	arg1	identification					92:105	identification	92:105	identification of 36 phosphorylation and five O-glycosylation sites	92:158	Post-translationally modified residues of native human osteopontin are located in clusters: identification of 36 phosphorylation and five O-glycosylation sites and their biological implications.
15869464	0	43	dep	clusters	82:89	arg1	implications					181:192	their biological implications	164:192	their biological implications	164:192	Post-translationally modified residues of native human osteopontin are located in clusters: identification of 36 phosphorylation and five O-glycosylation sites and their biological implications.
15869464	2	44	theme	significant	453:463	arg1	regulation					465:474	A significant regulation	451:474	A significant regulation of OPN function	451:490	A significant regulation of OPN function is mediated through PTM (post-translational modification).
15869464	4	45	theme	OPN	776:778	arg1	sequence					764:771	the sequence	760:771	the sequence of OPN	760:778	A total of 36 phosphoresidues have been localized in the sequence of OPN.
15869464	10	46	theme	key	2140:2142	arg1	molecule					2144:2151	a key molecule	2138:2151	a key molecule	2138:2151	Knowledge about the positions and nature of PTMs in OPN will allow a rational experimental design of functional studies aimed at understanding the structural and functional interdependences in diverse biological processes in which OPN is a key molecule.
15869464	10	46	theme	key	2140:2142	arg1	OPN					2131:2133	OPN	2131:2133	OPN	2131:2133	Knowledge about the positions and nature of PTMs in OPN will allow a rational experimental design of functional studies aimed at understanding the structural and functional interdependences in diverse biological processes in which OPN is a key molecule.
15869464	3	47	theme	native	689:694	arg1	OPN					702:704	native human OPN	689:704	native human OPN	689:704	Using a combination of Edman degradation and MS analyses, we have characterized the complete phosphorylation and glycosylation pattern of native human OPN.
15869464	0	48	theme	native	42:47	arg1	osteopontin					55:65	native human osteopontin	42:65	native human osteopontin	42:65	Post-translationally modified residues of native human osteopontin are located in clusters: identification of 36 phosphorylation and five O-glycosylation sites and their biological implications.
15869464	2	49	theme	function	483:490	arg1	regulation					465:474	A significant regulation	451:474	A significant regulation of OPN function	451:490	A significant regulation of OPN function is mediated through PTM (post-translational modification).
15869464	0	50	theme	osteopontin	55:65	arg1	residues					30:37	Post-translationally modified residues	0:37	Post-translationally modified residues of native human osteopontin	0:65	Post-translationally modified residues of native human osteopontin are located in clusters: identification of 36 phosphorylation and five O-glycosylation sites and their biological implications.
15869464	0	50	theme	osteopontin	55:65	arg1	osteopontin					55:65	native human osteopontin	42:65	native human osteopontin	42:65	Post-translationally modified residues of native human osteopontin are located in clusters: identification of 36 phosphorylation and five O-glycosylation sites and their biological implications.
15869464	1	51	theme	processes	330:338	arg1	multitude					306:314	a multitude	304:314	a multitude of biological processes such as bone mineralization, cancer metastasis, cell-mediated immune response, inflammation and cell survival	304:448	OPN (osteopontin) is an integrin-binding highly phosphorylated glycoprotein, recognized as a key molecule in a multitude of biological processes such as bone mineralization, cancer metastasis, cell-mediated immune response, inflammation and cell survival.
15869464	7	52	from	sites	1490:1494	arg1	variability					1470:1480	variability	1470:1480	variability at many sites	1470:1494	The 36 phosphoresidues represent the maximal degree of modification since variability at many sites was seen.
15869464	5	53	theme	mammary	1073:1079	arg1	MGCK					1067:1070	MGCK	1067:1070	MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D)	1067:1148	There are 29 phosphorylations (Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254, Ser259, Ser264, Ser275, Ser287, Ser292 and Ser294) located in the target sequence of MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D).
15869464	5	53	theme	mammary	1073:1079	arg1	kinase					1094:1099	mammary gland casein kinase	1073:1099	mammary gland casein kinase	1073:1099	There are 29 phosphorylations (Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254, Ser259, Ser264, Ser275, Ser287, Ser292 and Ser294) located in the target sequence of MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D).
15869464	3	54	theme	OPN	702:704	arg1	phosphorylation					644:658	the complete phosphorylation and glycosylation pattern	631:684	phosphorylation	644:658	Using a combination of Edman degradation and MS analyses, we have characterized the complete phosphorylation and glycosylation pattern of native human OPN.
15869464	3	54	theme	OPN	702:704	arg1	pattern					678:684	the complete phosphorylation and glycosylation pattern	631:684	pattern	678:684	Using a combination of Edman degradation and MS analyses, we have characterized the complete phosphorylation and glycosylation pattern of native human OPN.
15869464	5	55	theme	casein	1087:1092	arg1	MGCK					1067:1070	MGCK	1067:1070	MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D)	1067:1148	There are 29 phosphorylations (Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254, Ser259, Ser264, Ser275, Ser287, Ser292 and Ser294) located in the target sequence of MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D).
15869464	5	55	theme	casein	1087:1092	arg1	kinase					1094:1099	mammary gland casein kinase	1073:1099	mammary gland casein kinase	1073:1099	There are 29 phosphorylations (Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254, Ser259, Ser264, Ser275, Ser287, Ser292 and Ser294) located in the target sequence of MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D).
15869464	6	56	theme	target	1243:1248	arg1	sequence					1250:1257	the target sequence	1239:1257	the target sequence of CKII (casein kinase II) [S-X-X-E/S(P)/D]	1239:1301	Six phosphorylations (Ser101, Ser107, Ser175, Ser199, Ser212 and Ser251) are located in the target sequence of CKII (casein kinase II) [S-X-X-E/S(P)/D] and a single phosphorylation, Ser203, is not positioned in the motif of either MGCK or CKII.
15869464	8	57	theme	potential	1601:1609	arg1	sites					1611:1615	two potential sites	1597:1615	two potential sites for N-glycosylation (Asn63 and Asn90)	1597:1653	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	9	58	theme	RGD	1824:1826	arg1	sequence					1859:1866	the RGD (Arg-Gly-Asp) integrin-binding sequence	1820:1866	the RGD (Arg-Gly-Asp) integrin-binding sequence	1820:1866	The phosphorylations are arranged in clusters of three to five phosphoresidues and the regions containing the glycosylations and the RGD (Arg-Gly-Asp) integrin-binding sequence are devoid of phosphorylations.
15869464	5	59	theme	MGCK	1067:1070	arg1	sequence					1055:1062	the target sequence	1044:1062	the target sequence of MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D)	1044:1148	There are 29 phosphorylations (Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254, Ser259, Ser264, Ser275, Ser287, Ser292 and Ser294) located in the target sequence of MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D).
15869464	10	60	from	OPN	1952:1954	arg1	nature					1934:1939	nature	1934:1939	nature	1934:1939	Knowledge about the positions and nature of PTMs in OPN will allow a rational experimental design of functional studies aimed at understanding the structural and functional interdependences in diverse biological processes in which OPN is a key molecule.
15869464	10	60	from	OPN	1952:1954	arg1	positions					1920:1928	positions	1920:1928	positions	1920:1928	Knowledge about the positions and nature of PTMs in OPN will allow a rational experimental design of functional studies aimed at understanding the structural and functional interdependences in diverse biological processes in which OPN is a key molecule.
15869464	3	61	gly	glycosylation	664:676	arg1	OPN					702:704	native human OPN	689:704	native human OPN	689:704	Using a combination of Edman degradation and MS analyses, we have characterized the complete phosphorylation and glycosylation pattern of native human OPN.
15869464	9	62	theme	Arg-Gly-Asp	1829:1839	arg1	sequence					1859:1866	the RGD (Arg-Gly-Asp) integrin-binding sequence	1820:1866	the RGD (Arg-Gly-Asp) integrin-binding sequence	1820:1866	The phosphorylations are arranged in clusters of three to five phosphoresidues and the regions containing the glycosylations and the RGD (Arg-Gly-Asp) integrin-binding sequence are devoid of phosphorylations.
15869464	6	63	from	motif	1366:1370	arg1	positioned					1348:1357	positioned	1348:1357	positioned	1348:1357	Six phosphorylations (Ser101, Ser107, Ser175, Ser199, Ser212 and Ser251) are located in the target sequence of CKII (casein kinase II) [S-X-X-E/S(P)/D] and a single phosphorylation, Ser203, is not positioned in the motif of either MGCK or CKII.
15869464	6	63	from	motif	1366:1370	arg1	phosphorylation					1316:1330	a single phosphorylation	1307:1330	a single phosphorylation	1307:1330	Six phosphorylations (Ser101, Ser107, Ser175, Ser199, Ser212 and Ser251) are located in the target sequence of CKII (casein kinase II) [S-X-X-E/S(P)/D] and a single phosphorylation, Ser203, is not positioned in the motif of either MGCK or CKII.
15869464	9	64	theme	integrin-binding	1842:1857	arg1	sequence					1859:1866	the RGD (Arg-Gly-Asp) integrin-binding sequence	1820:1866	the RGD (Arg-Gly-Asp) integrin-binding sequence	1820:1866	The phosphorylations are arranged in clusters of three to five phosphoresidues and the regions containing the glycosylations and the RGD (Arg-Gly-Asp) integrin-binding sequence are devoid of phosphorylations.
15869464	5	65	from	located	1033:1039	arg1	sequence					1055:1062	the target sequence	1044:1062	the target sequence of MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D)	1044:1148	There are 29 phosphorylations (Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254, Ser259, Ser264, Ser275, Ser287, Ser292 and Ser294) located in the target sequence of MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D).
15869464	3	66	theme	MS	596:597	arg1	analyses					599:606	MS analyses	596:606	MS analyses	596:606	Using a combination of Edman degradation and MS analyses, we have characterized the complete phosphorylation and glycosylation pattern of native human OPN.
15869464	10	67	from	molecule	2144:2151	arg1	processes					2112:2120	diverse biological processes	2093:2120	diverse biological processes in which OPN is a key molecule	2093:2151	Knowledge about the positions and nature of PTMs in OPN will allow a rational experimental design of functional studies aimed at understanding the structural and functional interdependences in diverse biological processes in which OPN is a key molecule.
15869464	10	68	theme	experimental	1978:1989	arg1	design					1991:1996	a rational experimental design	1967:1996	a rational experimental design of functional studies aimed at understanding the structural and functional interdependences in diverse biological processes in which OPN is a key molecule	1967:2151	Knowledge about the positions and nature of PTMs in OPN will allow a rational experimental design of functional studies aimed at understanding the structural and functional interdependences in diverse biological processes in which OPN is a key molecule.
15869464	7	69	theme	many	1485:1488	arg1	sites					1490:1494	many sites	1485:1494	many sites	1485:1494	The 36 phosphoresidues represent the maximal degree of modification since variability at many sites was seen.
15869464	3	70	theme	degradation	580:590	arg1	combination					559:569	a combination	557:569	a combination of Edman degradation and MS analyses	557:606	Using a combination of Edman degradation and MS analyses, we have characterized the complete phosphorylation and glycosylation pattern of native human OPN.
15869464	8	71	dep	O-glycosylated	1534:1547	arg1	Thr118					1550:1555	Thr118	1550:1555	Thr118	1550:1555	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	71	dep	O-glycosylated	1534:1547	arg1	Thr131					1574:1579	Thr131	1574:1579	Thr131	1574:1579	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	71	dep	O-glycosylated	1534:1547	arg1	Thr136					1585:1590	Thr136	1585:1590	Thr136	1585:1590	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	71	dep	O-glycosylated	1534:1547	arg1	residues					1521:1528	Five threonine residues	1506:1528	Five threonine residues	1506:1528	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	71	dep	O-glycosylated	1534:1547	arg1	Thr122					1558:1563	Thr122	1558:1563	Thr122	1558:1563	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	71	dep	O-glycosylated	1534:1547	arg1	Thr127					1566:1571	Thr127	1566:1571	Thr127	1566:1571	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	5	72	from	sequence	1055:1062	arg1	located					1033:1039	located	1033:1039	located	1033:1039	There are 29 phosphorylations (Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254, Ser259, Ser264, Ser275, Ser287, Ser292 and Ser294) located in the target sequence of MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D).
15869464	6	73	theme	kinase	1275:1280	arg1	CKII					1262:1265	CKII	1262:1265	CKII (casein kinase II) [S-X-X-E/S(P)/D]	1262:1301	Six phosphorylations (Ser101, Ser107, Ser175, Ser199, Ser212 and Ser251) are located in the target sequence of CKII (casein kinase II) [S-X-X-E/S(P)/D] and a single phosphorylation, Ser203, is not positioned in the motif of either MGCK or CKII.
15869464	6	73	theme	kinase	1275:1280	arg1	/D					1299:1300	casein kinase II) [S-X-X-E/S(P)/D	1268:1300	casein kinase II) [S-X-X-E/S(P)/D	1268:1300	Six phosphorylations (Ser101, Ser107, Ser175, Ser199, Ser212 and Ser251) are located in the target sequence of CKII (casein kinase II) [S-X-X-E/S(P)/D] and a single phosphorylation, Ser203, is not positioned in the motif of either MGCK or CKII.
15869464	10	74	theme	studies	2012:2018	arg1	design					1991:1996	a rational experimental design	1967:1996	a rational experimental design of functional studies aimed at understanding the structural and functional interdependences in diverse biological processes in which OPN is a key molecule	1967:2151	Knowledge about the positions and nature of PTMs in OPN will allow a rational experimental design of functional studies aimed at understanding the structural and functional interdependences in diverse biological processes in which OPN is a key molecule.
15869464	1	75	theme	cell	436:439	arg1	survival					441:448	cell survival	436:448	cell survival	436:448	OPN (osteopontin) is an integrin-binding highly phosphorylated glycoprotein, recognized as a key molecule in a multitude of biological processes such as bone mineralization, cancer metastasis, cell-mediated immune response, inflammation and cell survival.
15869464	0	76	gly	O-glycosylation	138:152	arg2	sites					154:158	36 phosphorylation and five O-glycosylation sites	110:158	sites	154:158	Post-translationally modified residues of native human osteopontin are located in clusters: identification of 36 phosphorylation and five O-glycosylation sites and their biological implications.
15869464	0	76	gly	O-glycosylation	138:152	arg2	five					133:136	five	133:136	five	133:136	Post-translationally modified residues of native human osteopontin are located in clusters: identification of 36 phosphorylation and five O-glycosylation sites and their biological implications.
15869464	10	77	theme	diverse	2093:2099	arg1	processes					2112:2120	diverse biological processes	2093:2120	diverse biological processes in which OPN is a key molecule	2093:2151	Knowledge about the positions and nature of PTMs in OPN will allow a rational experimental design of functional studies aimed at understanding the structural and functional interdependences in diverse biological processes in which OPN is a key molecule.
15869464	1	78	theme	bone	348:351	arg1	mineralization					353:366	bone mineralization	348:366	bone mineralization	348:366	OPN (osteopontin) is an integrin-binding highly phosphorylated glycoprotein, recognized as a key molecule in a multitude of biological processes such as bone mineralization, cancer metastasis, cell-mediated immune response, inflammation and cell survival.
15869464	8	79	theme	threonine	1511:1519	arg1	Thr118					1550:1555	Thr118	1550:1555	Thr118	1550:1555	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	79	theme	threonine	1511:1519	arg1	Thr131					1574:1579	Thr131	1574:1579	Thr131	1574:1579	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	79	theme	threonine	1511:1519	arg1	Thr136					1585:1590	Thr136	1585:1590	Thr136	1585:1590	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	79	theme	threonine	1511:1519	arg1	residues					1521:1528	Five threonine residues	1506:1528	Five threonine residues	1506:1528	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	79	theme	threonine	1511:1519	arg1	Thr122					1558:1563	Thr122	1558:1563	Thr122	1558:1563	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	79	theme	threonine	1511:1519	arg1	Thr127					1566:1571	Thr127	1566:1571	Thr127	1566:1571	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	5	80	theme	Ser65	867:871	arg1	phosphorylations					794:809	29 phosphorylations	791:809	29 phosphorylations (Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254, Ser259, Ser264, Ser275, Ser287, Ser292 and Ser294) located in the target sequence of MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D)	791:1148	There are 29 phosphorylations (Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254, Ser259, Ser264, Ser275, Ser287, Ser292 and Ser294) located in the target sequence of MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D).
15869464	5	80	theme	Ser65	867:871	arg1	Ser254					974:979	Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254	812:979	Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254	812:979	There are 29 phosphorylations (Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254, Ser259, Ser264, Ser275, Ser287, Ser292 and Ser294) located in the target sequence of MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D).
15869464	4	81	located	localized	747:755	arg2	total					709:713	A total	707:713	A total of 36 phosphoresidues	707:735	A total of 36 phosphoresidues have been localized in the sequence of OPN.
15869464	4	81	located	localized	747:755	arg1	sequence					764:771	the sequence	760:771	the sequence of OPN	760:778	A total of 36 phosphoresidues have been localized in the sequence of OPN.
15869464	8	82	theme	milk	1681:1684	arg1	OPN					1686:1688	human milk OPN	1675:1688	human milk OPN	1675:1688	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	7	83	theme	maximal	1433:1439	arg1	degree					1441:1446	the maximal degree	1429:1446	the maximal degree of modification	1429:1462	The 36 phosphoresidues represent the maximal degree of modification since variability at many sites was seen.
15869464	0	84	theme	phosphorylation	113:127	arg1	identification					92:105	identification	92:105	identification of 36 phosphorylation and five O-glycosylation sites	92:158	Post-translationally modified residues of native human osteopontin are located in clusters: identification of 36 phosphorylation and five O-glycosylation sites and their biological implications.
15869464	0	84	theme	phosphorylation	113:127	arg1	implications					181:192	their biological implications	164:192	their biological implications	164:192	Post-translationally modified residues of native human osteopontin are located in clusters: identification of 36 phosphorylation and five O-glycosylation sites and their biological implications.
15869464	1	85	gly	glycoprotein	258:269	arg1	glycoprotein					258:269	an integrin-binding highly phosphorylated glycoprotein	216:269	an integrin-binding highly phosphorylated glycoprotein	216:269	OPN (osteopontin) is an integrin-binding highly phosphorylated glycoprotein, recognized as a key molecule in a multitude of biological processes such as bone mineralization, cancer metastasis, cell-mediated immune response, inflammation and cell survival.
15869464	1	85	gly	glycoprotein	258:269	arg1	OPN					195:197	OPN	195:197	OPN (osteopontin)	195:211	OPN (osteopontin) is an integrin-binding highly phosphorylated glycoprotein, recognized as a key molecule in a multitude of biological processes such as bone mineralization, cancer metastasis, cell-mediated immune response, inflammation and cell survival.
15869464	1	86	theme	phosphorylated	243:256	arg1	glycoprotein					258:269	an integrin-binding highly phosphorylated glycoprotein	216:269	an integrin-binding highly phosphorylated glycoprotein	216:269	OPN (osteopontin) is an integrin-binding highly phosphorylated glycoprotein, recognized as a key molecule in a multitude of biological processes such as bone mineralization, cancer metastasis, cell-mediated immune response, inflammation and cell survival.
15869464	1	86	theme	phosphorylated	243:256	arg1	OPN					195:197	OPN	195:197	OPN (osteopontin)	195:211	OPN (osteopontin) is an integrin-binding highly phosphorylated glycoprotein, recognized as a key molecule in a multitude of biological processes such as bone mineralization, cancer metastasis, cell-mediated immune response, inflammation and cell survival.
15869464	0	87	theme	modified	21:28	arg1	residues					30:37	Post-translationally modified residues	0:37	Post-translationally modified residues of native human osteopontin	0:65	Post-translationally modified residues of native human osteopontin are located in clusters: identification of 36 phosphorylation and five O-glycosylation sites and their biological implications.
15869464	0	87	theme	modified	21:28	arg1	osteopontin					55:65	native human osteopontin	42:65	native human osteopontin	42:65	Post-translationally modified residues of native human osteopontin are located in clusters: identification of 36 phosphorylation and five O-glycosylation sites and their biological implications.
15869464	1	88	theme	cell-mediated	388:400	arg1	response					409:416	cell-mediated immune response	388:416	cell-mediated immune response	388:416	OPN (osteopontin) is an integrin-binding highly phosphorylated glycoprotein, recognized as a key molecule in a multitude of biological processes such as bone mineralization, cancer metastasis, cell-mediated immune response, inflammation and cell survival.
15869464	8	89	gly	O-glycosylated	1534:1547	arg1	Thr118					1550:1555	Thr118	1550:1555	Thr118	1550:1555	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	89	gly	O-glycosylated	1534:1547	arg1	Thr131					1574:1579	Thr131	1574:1579	Thr131	1574:1579	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	89	gly	O-glycosylated	1534:1547	arg1	Thr136					1585:1590	Thr136	1585:1590	Thr136	1585:1590	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	89	gly	O-glycosylated	1534:1547	arg1	residues					1521:1528	Five threonine residues	1506:1528	Five threonine residues	1506:1528	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	89	gly	O-glycosylated	1534:1547	arg1	Thr122					1558:1563	Thr122	1558:1563	Thr122	1558:1563	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	89	gly	O-glycosylated	1534:1547	arg1	Thr127					1566:1571	Thr127	1566:1571	Thr127	1566:1571	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	10	90	theme	PTMs	1944:1947	arg1	nature					1934:1939	nature	1934:1939	nature	1934:1939	Knowledge about the positions and nature of PTMs in OPN will allow a rational experimental design of functional studies aimed at understanding the structural and functional interdependences in diverse biological processes in which OPN is a key molecule.
15869464	10	90	theme	PTMs	1944:1947	arg1	positions					1920:1928	positions	1920:1928	positions	1920:1928	Knowledge about the positions and nature of PTMs in OPN will allow a rational experimental design of functional studies aimed at understanding the structural and functional interdependences in diverse biological processes in which OPN is a key molecule.
15869464	5	91	theme	S/T-X-E/S	1134:1142	arg1	kinase					1126:1131	the Golgi kinase	1116:1131	the Golgi kinase (S/T-X-E/S(P)/D)	1116:1148	There are 29 phosphorylations (Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254, Ser259, Ser264, Ser275, Ser287, Ser292 and Ser294) located in the target sequence of MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D).
15869464	5	91	theme	S/T-X-E/S	1134:1142	arg1	/D					1146:1147	S/T-X-E/S(P)/D	1134:1147	S/T-X-E/S(P)/D	1134:1147	There are 29 phosphorylations (Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254, Ser259, Ser264, Ser275, Ser287, Ser292 and Ser294) located in the target sequence of MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D).
15869464	10	92	from	interdependences	2073:2088	arg1	processes					2112:2120	diverse biological processes	2093:2120	diverse biological processes in which OPN is a key molecule	2093:2151	Knowledge about the positions and nature of PTMs in OPN will allow a rational experimental design of functional studies aimed at understanding the structural and functional interdependences in diverse biological processes in which OPN is a key molecule.
15869464	5	93	theme	P	1144:1144	arg1	kinase					1126:1131	the Golgi kinase	1116:1131	the Golgi kinase (S/T-X-E/S(P)/D)	1116:1148	There are 29 phosphorylations (Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254, Ser259, Ser264, Ser275, Ser287, Ser292 and Ser294) located in the target sequence of MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D).
15869464	5	93	theme	P	1144:1144	arg1	/D					1146:1147	S/T-X-E/S(P)/D	1134:1147	S/T-X-E/S(P)/D	1134:1147	There are 29 phosphorylations (Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254, Ser259, Ser264, Ser275, Ser287, Ser292 and Ser294) located in the target sequence of MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D).
15869464	0	94	theme	human	49:53	arg1	osteopontin					55:65	native human osteopontin	42:65	native human osteopontin	42:65	Post-translationally modified residues of native human osteopontin are located in clusters: identification of 36 phosphorylation and five O-glycosylation sites and their biological implications.
15869464	5	95	theme	target	1048:1053	arg1	sequence					1055:1062	the target sequence	1044:1062	the target sequence of MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D)	1044:1148	There are 29 phosphorylations (Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254, Ser259, Ser264, Ser275, Ser287, Ser292 and Ser294) located in the target sequence of MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D).
15869464	8	96	dep	N-glycosylation	1621:1635	arg1	Asn90					1648:1652	Asn90	1648:1652	Asn90	1648:1652	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	8	96	dep	N-glycosylation	1621:1635	arg1	Asn63					1638:1642	Asn63	1638:1642	Asn63	1638:1642	Five threonine residues are O-glycosylated (Thr118, Thr122, Thr127, Thr131 and Thr136) and two potential sites for N-glycosylation (Asn63 and Asn90) are not occupied in human milk OPN.
15869464	3	97	theme	glycosylation	664:676	arg1	pattern					678:684	the complete phosphorylation and glycosylation pattern	631:684	pattern	678:684	Using a combination of Edman degradation and MS analyses, we have characterized the complete phosphorylation and glycosylation pattern of native human OPN.
15869464	1	98	theme	biological	319:328	arg1	inflammation					419:430	inflammation	419:430	inflammation	419:430	OPN (osteopontin) is an integrin-binding highly phosphorylated glycoprotein, recognized as a key molecule in a multitude of biological processes such as bone mineralization, cancer metastasis, cell-mediated immune response, inflammation and cell survival.
15869464	1	98	theme	biological	319:328	arg1	processes					330:338	biological processes	319:338	biological processes such as bone mineralization, cancer metastasis, cell-mediated immune response, inflammation and cell survival	319:448	OPN (osteopontin) is an integrin-binding highly phosphorylated glycoprotein, recognized as a key molecule in a multitude of biological processes such as bone mineralization, cancer metastasis, cell-mediated immune response, inflammation and cell survival.
15869464	1	98	theme	biological	319:328	arg1	metastasis					376:385	cancer metastasis	369:385	cancer metastasis	369:385	OPN (osteopontin) is an integrin-binding highly phosphorylated glycoprotein, recognized as a key molecule in a multitude of biological processes such as bone mineralization, cancer metastasis, cell-mediated immune response, inflammation and cell survival.
15869464	1	98	theme	biological	319:328	arg1	survival					441:448	cell survival	436:448	cell survival	436:448	OPN (osteopontin) is an integrin-binding highly phosphorylated glycoprotein, recognized as a key molecule in a multitude of biological processes such as bone mineralization, cancer metastasis, cell-mediated immune response, inflammation and cell survival.
15869464	1	98	theme	biological	319:328	arg1	mineralization					353:366	bone mineralization	348:366	bone mineralization	348:366	OPN (osteopontin) is an integrin-binding highly phosphorylated glycoprotein, recognized as a key molecule in a multitude of biological processes such as bone mineralization, cancer metastasis, cell-mediated immune response, inflammation and cell survival.
15869464	1	98	theme	biological	319:328	arg1	response					409:416	cell-mediated immune response	388:416	cell-mediated immune response	388:416	OPN (osteopontin) is an integrin-binding highly phosphorylated glycoprotein, recognized as a key molecule in a multitude of biological processes such as bone mineralization, cancer metastasis, cell-mediated immune response, inflammation and cell survival.
15869464	2	99	theme	OPN	479:481	arg1	function					483:490	OPN function	479:490	OPN function	479:490	A significant regulation of OPN function is mediated through PTM (post-translational modification).
15869464	6	100	theme	casein	1268:1273	arg1	kinase					1275:1280	casein kinase II	1268:1283	casein kinase II) [S-X-X-E/S(P)/D	1268:1300	Six phosphorylations (Ser101, Ser107, Ser175, Ser199, Ser212 and Ser251) are located in the target sequence of CKII (casein kinase II) [S-X-X-E/S(P)/D] and a single phosphorylation, Ser203, is not positioned in the motif of either MGCK or CKII.
15869464	3	101	theme	human	696:700	arg1	OPN					702:704	native human OPN	689:704	native human OPN	689:704	Using a combination of Edman degradation and MS analyses, we have characterized the complete phosphorylation and glycosylation pattern of native human OPN.
15869464	6	102	theme	CKII	1262:1265	arg1	sequence					1250:1257	the target sequence	1239:1257	the target sequence of CKII (casein kinase II) [S-X-X-E/S(P)/D]	1239:1301	Six phosphorylations (Ser101, Ser107, Ser175, Ser199, Ser212 and Ser251) are located in the target sequence of CKII (casein kinase II) [S-X-X-E/S(P)/D] and a single phosphorylation, Ser203, is not positioned in the motif of either MGCK or CKII.
15869464	5	103	theme	gland	1081:1085	arg1	MGCK					1067:1070	MGCK	1067:1070	MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D)	1067:1148	There are 29 phosphorylations (Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254, Ser259, Ser264, Ser275, Ser287, Ser292 and Ser294) located in the target sequence of MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D).
15869464	5	103	theme	gland	1081:1085	arg1	kinase					1094:1099	mammary gland casein kinase	1073:1099	mammary gland casein kinase	1073:1099	There are 29 phosphorylations (Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254, Ser259, Ser264, Ser275, Ser287, Ser292 and Ser294) located in the target sequence of MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D).
15869464	1	104	theme	integrin-binding	219:234	arg1	glycoprotein					258:269	an integrin-binding highly phosphorylated glycoprotein	216:269	an integrin-binding highly phosphorylated glycoprotein	216:269	OPN (osteopontin) is an integrin-binding highly phosphorylated glycoprotein, recognized as a key molecule in a multitude of biological processes such as bone mineralization, cancer metastasis, cell-mediated immune response, inflammation and cell survival.
15869464	1	104	theme	integrin-binding	219:234	arg1	OPN					195:197	OPN	195:197	OPN (osteopontin)	195:211	OPN (osteopontin) is an integrin-binding highly phosphorylated glycoprotein, recognized as a key molecule in a multitude of biological processes such as bone mineralization, cancer metastasis, cell-mediated immune response, inflammation and cell survival.
15869464	6	105	from	sequence	1250:1257	arg1	located					1228:1234	located	1228:1234	located	1228:1234	Six phosphorylations (Ser101, Ser107, Ser175, Ser199, Ser212 and Ser251) are located in the target sequence of CKII (casein kinase II) [S-X-X-E/S(P)/D] and a single phosphorylation, Ser203, is not positioned in the motif of either MGCK or CKII.
15869464	6	106	located	located	1228:1234	arg2	phosphorylations					1155:1170	Six phosphorylations	1151:1170	Six phosphorylations (Ser101, Ser107, Ser175, Ser199, Ser212 and Ser251)	1151:1222	Six phosphorylations (Ser101, Ser107, Ser175, Ser199, Ser212 and Ser251) are located in the target sequence of CKII (casein kinase II) [S-X-X-E/S(P)/D] and a single phosphorylation, Ser203, is not positioned in the motif of either MGCK or CKII.
15869464	6	106	located	located	1228:1234	arg1	sequence					1250:1257	the target sequence	1239:1257	the target sequence of CKII (casein kinase II) [S-X-X-E/S(P)/D]	1239:1301	Six phosphorylations (Ser101, Ser107, Ser175, Ser199, Ser212 and Ser251) are located in the target sequence of CKII (casein kinase II) [S-X-X-E/S(P)/D] and a single phosphorylation, Ser203, is not positioned in the motif of either MGCK or CKII.
15869464	6	106	located	located	1228:1234	arg2	Ser101					1173:1178	Ser101	1173:1178	Ser101	1173:1178	Six phosphorylations (Ser101, Ser107, Ser175, Ser199, Ser212 and Ser251) are located in the target sequence of CKII (casein kinase II) [S-X-X-E/S(P)/D] and a single phosphorylation, Ser203, is not positioned in the motif of either MGCK or CKII.
15869464	6	106	located	located	1228:1234	arg2	Ser199					1197:1202	Ser199	1197:1202	Ser199	1197:1202	Six phosphorylations (Ser101, Ser107, Ser175, Ser199, Ser212 and Ser251) are located in the target sequence of CKII (casein kinase II) [S-X-X-E/S(P)/D] and a single phosphorylation, Ser203, is not positioned in the motif of either MGCK or CKII.
15869464	6	106	located	located	1228:1234	arg2	Ser107					1181:1186	Ser107	1181:1186	Ser107	1181:1186	Six phosphorylations (Ser101, Ser107, Ser175, Ser199, Ser212 and Ser251) are located in the target sequence of CKII (casein kinase II) [S-X-X-E/S(P)/D] and a single phosphorylation, Ser203, is not positioned in the motif of either MGCK or CKII.
15869464	6	106	located	located	1228:1234	arg2	Ser212					1205:1210	Ser212	1205:1210	Ser212	1205:1210	Six phosphorylations (Ser101, Ser107, Ser175, Ser199, Ser212 and Ser251) are located in the target sequence of CKII (casein kinase II) [S-X-X-E/S(P)/D] and a single phosphorylation, Ser203, is not positioned in the motif of either MGCK or CKII.
15869464	6	106	located	located	1228:1234	arg2	Ser175					1189:1194	Ser175	1189:1194	Ser175	1189:1194	Six phosphorylations (Ser101, Ser107, Ser175, Ser199, Ser212 and Ser251) are located in the target sequence of CKII (casein kinase II) [S-X-X-E/S(P)/D] and a single phosphorylation, Ser203, is not positioned in the motif of either MGCK or CKII.
15869464	6	106	located	located	1228:1234	arg2	Ser251					1216:1221	Ser251	1216:1221	Ser251	1216:1221	Six phosphorylations (Ser101, Ser107, Ser175, Ser199, Ser212 and Ser251) are located in the target sequence of CKII (casein kinase II) [S-X-X-E/S(P)/D] and a single phosphorylation, Ser203, is not positioned in the motif of either MGCK or CKII.
15869464	5	107	dep	Ser247	966:971	arg1	Thr169					926:931	Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247	881:971	Thr169	926:931	There are 29 phosphorylations (Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254, Ser259, Ser264, Ser275, Ser287, Ser292 and Ser294) located in the target sequence of MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D).
15869464	5	107	dep	Ser247	966:971	arg1	Ser218					950:955	Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247	881:971	Ser218	950:955	There are 29 phosphorylations (Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254, Ser259, Ser264, Ser275, Ser287, Ser292 and Ser294) located in the target sequence of MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D).
15869464	5	107	dep	Ser247	966:971	arg1	Ser104					902:907	Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247	881:971	Ser104	902:907	There are 29 phosphorylations (Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254, Ser259, Ser264, Ser275, Ser287, Ser292 and Ser294) located in the target sequence of MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D).
15869464	5	107	dep	Ser247	966:971	arg1	Ser238					958:963	Ser238	958:963	Ser238	958:963	There are 29 phosphorylations (Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254, Ser259, Ser264, Ser275, Ser287, Ser292 and Ser294) located in the target sequence of MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D).
15869464	5	107	dep	Ser247	966:971	arg1	Ser110					910:915	Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247	881:971	Ser110	910:915	There are 29 phosphorylations (Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254, Ser259, Ser264, Ser275, Ser287, Ser292 and Ser294) located in the target sequence of MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D).
15869464	5	107	dep	Ser247	966:971	arg1	Ser179					934:939	Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247	881:971	Ser179	934:939	There are 29 phosphorylations (Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254, Ser259, Ser264, Ser275, Ser287, Ser292 and Ser294) located in the target sequence of MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D).
15869464	5	107	dep	Ser247	966:971	arg1	Ser208					942:947	Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247	881:971	Ser208	942:947	There are 29 phosphorylations (Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254, Ser259, Ser264, Ser275, Ser287, Ser292 and Ser294) located in the target sequence of MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D).
15869464	5	107	dep	Ser247	966:971	arg1	Ser92					895:899	Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247	881:971	Ser92	895:899	There are 29 phosphorylations (Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254, Ser259, Ser264, Ser275, Ser287, Ser292 and Ser294) located in the target sequence of MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D).
15869464	5	107	dep	Ser247	966:971	arg1	Ser113					918:923	Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247	881:971	Ser113	918:923	There are 29 phosphorylations (Ser8, Ser10, Ser11, Ser46, Ser47, Thr50, Ser60, Ser62, Ser65, Ser83, Ser86, Ser89, Ser92, Ser104, Ser110, Ser113, Thr169, Ser179, Ser208, Ser218, Ser238, Ser247, Ser254, Ser259, Ser264, Ser275, Ser287, Ser292 and Ser294) located in the target sequence of MGCK (mammary gland casein kinase) also known as the Golgi kinase (S/T-X-E/S(P)/D).
24884609	6	0	theme	LC-MS/MS	863:870	arg1	analysis					872:879	glycosidase-assisted LC-MS/MS analysis	842:879	glycosidase-assisted LC-MS/MS analysis of ITIH4 trypsin-GluC glycopeptides enriched via hydrophilic interaction liquid chromatography	842:974	Next, we performed glycosidase-assisted LC-MS/MS analysis of ITIH4 trypsin-GluC glycopeptides enriched via hydrophilic interaction liquid chromatography to characterize ITIH4 N-glycoforms.
24884609	6	1	gly	N-glycoforms	998:1009	arg1	ITIH4					992:996	ITIH4 N-glycoforms	992:1009	ITIH4 N-glycoforms	992:1009	Next, we performed glycosidase-assisted LC-MS/MS analysis of ITIH4 trypsin-GluC glycopeptides enriched via hydrophilic interaction liquid chromatography to characterize ITIH4 N-glycoforms.
24884609	1	2	theme	acute-phase	155:165	arg1	H4					131:132	Inter-alpha-trypsin inhibitor heavy chain H4	89:132	Inter-alpha-trypsin inhibitor heavy chain H4 (ITIH4)	89:140	Inter-alpha-trypsin inhibitor heavy chain H4 (ITIH4) is a 120 kDa acute-phase glycoprotein produced primarily in the liver, secreted into the blood, and identified in serum.
24884609	1	2	theme	acute-phase	155:165	arg1	glycoprotein					167:178	a 120 kDa acute-phase glycoprotein	145:178	a 120 kDa acute-phase glycoprotein produced primarily in the liver, secreted into the blood, and identified in serum	145:260	Inter-alpha-trypsin inhibitor heavy chain H4 (ITIH4) is a 120 kDa acute-phase glycoprotein produced primarily in the liver, secreted into the blood, and identified in serum.
24884609	9	3	theme	N-linked	1317:1324	arg1	glycans					1326:1332	high-mannose N-linked glycans	1304:1332	high-mannose N-linked glycans	1304:1332	Site N274 contained high-mannose N-linked glycans in both serum and recombinant ITIH4.
24884609	8	4	theme	N-glycosylation	1202:1216	arg1	site					1218:1221	A fifth N-glycosylation site	1194:1221	A fifth N-glycosylation site	1194:1221	A fifth N-glycosylation site was discovered at N274 with the rare nonconsensus NVV motif.
24884609	6	5	theme	glycosidase-assisted	842:861	arg1	analysis					872:879	glycosidase-assisted LC-MS/MS analysis	842:879	glycosidase-assisted LC-MS/MS analysis of ITIH4 trypsin-GluC glycopeptides enriched via hydrophilic interaction liquid chromatography	842:974	Next, we performed glycosidase-assisted LC-MS/MS analysis of ITIH4 trypsin-GluC glycopeptides enriched via hydrophilic interaction liquid chromatography to characterize ITIH4 N-glycoforms.
24884609	9	6	contain	contained	1294:1302	arg2	glycans					1326:1332	high-mannose N-linked glycans	1304:1332	high-mannose N-linked glycans	1304:1332	Site N274 contained high-mannose N-linked glycans in both serum and recombinant ITIH4.
24884609	9	6	contain	contained	1294:1302	arg1	ITIH4					1364:1368	recombinant ITIH4	1352:1368	recombinant ITIH4	1352:1368	Site N274 contained high-mannose N-linked glycans in both serum and recombinant ITIH4.
24884609	9	6	contain	contained	1294:1302	arg1	N274					1289:1292	Site N274	1284:1292	Site N274	1284:1292	Site N274 contained high-mannose N-linked glycans in both serum and recombinant ITIH4.
24884609	9	6	contain	contained	1294:1302	arg1	serum					1342:1346	serum	1342:1346	serum	1342:1346	Site N274 contained high-mannose N-linked glycans in both serum and recombinant ITIH4.
24884609	9	6	contain	contained	1294:1302	arg2	N274					1289:1292	Site N274	1284:1292	Site N274	1284:1292	Site N274 contained high-mannose N-linked glycans in both serum and recombinant ITIH4.
24884609	3	7	theme	serum-derived	476:488	arg1	ITIH4					490:494	recombinant and serum-derived ITIH4	460:494	recombinant and serum-derived ITIH4 using analytical mass spectrometry	460:529	In this study, we aimed to characterize glycosylation of recombinant and serum-derived ITIH4 using analytical mass spectrometry.
24884609	7	8	attach	isolated	1122:1129	arg2	protein					1114:1120	protein	1114:1120	protein isolated from serum	1114:1140	While microheterogeneity of N-glycoforms differed between ITIH4 protein expressed in HEK293 cells and protein isolated from serum, occupancy of N-glycosylation sites did not differ.
24884609	7	8	attach	isolated	1122:1129	arg1	serum					1136:1140	serum	1136:1140	serum	1136:1140	While microheterogeneity of N-glycoforms differed between ITIH4 protein expressed in HEK293 cells and protein isolated from serum, occupancy of N-glycosylation sites did not differ.
24884609	9	9	theme	high-mannose	1304:1315	arg1	glycans					1326:1332	high-mannose N-linked glycans	1304:1332	high-mannose N-linked glycans	1304:1332	Site N274 contained high-mannose N-linked glycans in both serum and recombinant ITIH4.
24884609	10	10	theme	sites	1477:1481	arg1	utilization					1446:1456	utilization	1446:1456	utilization of O-glycosylation sites on ITIH4	1446:1490	We also identified isoform-specific ITIH4 O-glycoforms and documented that utilization of O-glycosylation sites on ITIH4 differed between the cell line and serum.
24884609	6	11	gly	glycopeptides	903:915	arg2	glycopeptides					903:915	ITIH4 trypsin-GluC glycopeptides	884:915	ITIH4 trypsin-GluC glycopeptides enriched via hydrophilic interaction liquid chromatography	884:974	Next, we performed glycosidase-assisted LC-MS/MS analysis of ITIH4 trypsin-GluC glycopeptides enriched via hydrophilic interaction liquid chromatography to characterize ITIH4 N-glycoforms.
24884609	5	12	theme	ITIH4	745:749	arg1	glycopeptides					764:776	ITIH4 tryptic/GluC glycopeptides	745:776	ITIH4 tryptic/GluC glycopeptides	745:776	First, we confirmed that the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577) were glycosylated by treating ITIH4 tryptic/GluC glycopeptides with PNGaseF in the presence of (18)O water.
24884609	5	13	dep	sequons	679:685	arg1	N81					688:690	N81	688:690	N81	688:690	First, we confirmed that the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577) were glycosylated by treating ITIH4 tryptic/GluC glycopeptides with PNGaseF in the presence of (18)O water.
24884609	5	13	dep	sequons	679:685	arg1	sequons					679:685	the four ITIH4 N-X-S/T sequons	656:685	the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577)	656:713	First, we confirmed that the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577) were glycosylated by treating ITIH4 tryptic/GluC glycopeptides with PNGaseF in the presence of (18)O water.
24884609	5	13	dep	sequons	679:685	arg1	N517					699:702	N517	699:702	N517	699:702	First, we confirmed that the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577) were glycosylated by treating ITIH4 tryptic/GluC glycopeptides with PNGaseF in the presence of (18)O water.
24884609	5	13	dep	sequons	679:685	arg1	N577					709:712	N577	709:712	N577	709:712	First, we confirmed that the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577) were glycosylated by treating ITIH4 tryptic/GluC glycopeptides with PNGaseF in the presence of (18)O water.
24884609	5	13	dep	sequons	679:685	arg1	N207					693:696	N207	693:696	N207	693:696	First, we confirmed that the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577) were glycosylated by treating ITIH4 tryptic/GluC glycopeptides with PNGaseF in the presence of (18)O water.
24884609	5	14	from	PNGaseF	783:789	arg1	presence					798:805	the presence	794:805	the presence of (18)O water	794:820	First, we confirmed that the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577) were glycosylated by treating ITIH4 tryptic/GluC glycopeptides with PNGaseF in the presence of (18)O water.
24884609	6	15	theme	liquid	954:959	arg1	chromatography					961:974	hydrophilic interaction liquid chromatography	930:974	hydrophilic interaction liquid chromatography	930:974	Next, we performed glycosidase-assisted LC-MS/MS analysis of ITIH4 trypsin-GluC glycopeptides enriched via hydrophilic interaction liquid chromatography to characterize ITIH4 N-glycoforms.
24884609	10	16	theme	ITIH4	1407:1411	arg1	O-glycoforms					1413:1424	isoform-specific ITIH4 O-glycoforms	1390:1424	isoform-specific ITIH4 O-glycoforms	1390:1424	We also identified isoform-specific ITIH4 O-glycoforms and documented that utilization of O-glycosylation sites on ITIH4 differed between the cell line and serum.
24884609	4	17	theme	glycopeptide	575:586	arg1	analyses					588:595	glycopeptide analyses	575:595	glycopeptide analyses	575:595	Recombinant ITIH4 was analyzed to optimize glycopeptide analyses, followed by serum-derived ITIH4.
24884609	10	18	theme	cell	1513:1516	arg1	line					1518:1521	the cell line	1509:1521	the cell line	1509:1521	We also identified isoform-specific ITIH4 O-glycoforms and documented that utilization of O-glycosylation sites on ITIH4 differed between the cell line and serum.
24884609	8	19	gly	N-glycosylation	1202:1216	arg2	site					1218:1221	A fifth N-glycosylation site	1194:1221	A fifth N-glycosylation site	1194:1221	A fifth N-glycosylation site was discovered at N274 with the rare nonconsensus NVV motif.
24884609	1	20	theme	Inter-alpha-trypsin	89:107	arg1	chain					125:129	Inter-alpha-trypsin inhibitor heavy chain	89:129	Inter-alpha-trypsin inhibitor heavy chain H4 (ITIH4)	89:140	Inter-alpha-trypsin inhibitor heavy chain H4 (ITIH4) is a 120 kDa acute-phase glycoprotein produced primarily in the liver, secreted into the blood, and identified in serum.
24884609	8	21	theme	rare	1255:1258	arg1	motif					1277:1281	the rare nonconsensus NVV motif	1251:1281	the rare nonconsensus NVV motif	1251:1281	A fifth N-glycosylation site was discovered at N274 with the rare nonconsensus NVV motif.
24884609	5	22	theme	tryptic/GluC	751:762	arg1	glycopeptides					764:776	ITIH4 tryptic/GluC glycopeptides	745:776	ITIH4 tryptic/GluC glycopeptides	745:776	First, we confirmed that the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577) were glycosylated by treating ITIH4 tryptic/GluC glycopeptides with PNGaseF in the presence of (18)O water.
24884609	10	23	gly	O-glycoforms	1413:1424	arg1	ITIH4					1407:1411	isoform-specific ITIH4 O-glycoforms	1390:1424	isoform-specific ITIH4 O-glycoforms	1390:1424	We also identified isoform-specific ITIH4 O-glycoforms and documented that utilization of O-glycosylation sites on ITIH4 differed between the cell line and serum.
24884609	1	24	theme	inhibitor	109:117	arg1	chain					125:129	Inter-alpha-trypsin inhibitor heavy chain	89:129	Inter-alpha-trypsin inhibitor heavy chain H4 (ITIH4)	89:140	Inter-alpha-trypsin inhibitor heavy chain H4 (ITIH4) is a 120 kDa acute-phase glycoprotein produced primarily in the liver, secreted into the blood, and identified in serum.
24884609	9	25	link	N-linked	1317:1324	arg1	glycans					1326:1332	high-mannose N-linked glycans	1304:1332	high-mannose N-linked glycans	1304:1332	Site N274 contained high-mannose N-linked glycans in both serum and recombinant ITIH4.
24884609	0	26	theme	glycan	14:19	arg1	microheterogeneity					21:38	Site-specific glycan microheterogeneity	0:38	Site-specific glycan microheterogeneity of inter-alpha-trypsin inhibitor heavy chain H4	0:86	Site-specific glycan microheterogeneity of inter-alpha-trypsin inhibitor heavy chain H4.
24884609	10	27	theme	O-glycosylation	1461:1475	arg1	sites					1477:1481	O-glycosylation sites	1461:1481	O-glycosylation sites	1461:1481	We also identified isoform-specific ITIH4 O-glycoforms and documented that utilization of O-glycosylation sites on ITIH4 differed between the cell line and serum.
24884609	1	28	theme	heavy	119:123	arg1	chain					125:129	Inter-alpha-trypsin inhibitor heavy chain	89:129	Inter-alpha-trypsin inhibitor heavy chain H4 (ITIH4)	89:140	Inter-alpha-trypsin inhibitor heavy chain H4 (ITIH4) is a 120 kDa acute-phase glycoprotein produced primarily in the liver, secreted into the blood, and identified in serum.
24884609	3	29	theme	analytical	502:511	arg1	spectrometry					518:529	analytical mass spectrometry	502:529	analytical mass spectrometry	502:529	In this study, we aimed to characterize glycosylation of recombinant and serum-derived ITIH4 using analytical mass spectrometry.
24884609	5	30	theme	O	814:814	arg1	water					816:820	(18)O water	810:820	(18)O water	810:820	First, we confirmed that the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577) were glycosylated by treating ITIH4 tryptic/GluC glycopeptides with PNGaseF in the presence of (18)O water.
24884609	0	31	theme	Site-specific	0:12	arg1	microheterogeneity					21:38	Site-specific glycan microheterogeneity	0:38	Site-specific glycan microheterogeneity of inter-alpha-trypsin inhibitor heavy chain H4	0:86	Site-specific glycan microheterogeneity of inter-alpha-trypsin inhibitor heavy chain H4.
24884609	6	32	theme	interaction	942:952	arg1	chromatography					961:974	hydrophilic interaction liquid chromatography	930:974	hydrophilic interaction liquid chromatography	930:974	Next, we performed glycosidase-assisted LC-MS/MS analysis of ITIH4 trypsin-GluC glycopeptides enriched via hydrophilic interaction liquid chromatography to characterize ITIH4 N-glycoforms.
24884609	7	33	theme	HEK293	1097:1102	arg1	cells					1104:1108	HEK293 cells	1097:1108	HEK293 cells	1097:1108	While microheterogeneity of N-glycoforms differed between ITIH4 protein expressed in HEK293 cells and protein isolated from serum, occupancy of N-glycosylation sites did not differ.
24884609	4	34	gly	glycopeptide	575:586	arg2	glycopeptide					575:586	glycopeptide analyses	575:595	glycopeptide analyses	575:595	Recombinant ITIH4 was analyzed to optimize glycopeptide analyses, followed by serum-derived ITIH4.
24884609	1	35	theme	chain	125:129	arg1	ITIH4					135:139	ITIH4	135:139	ITIH4	135:139	Inter-alpha-trypsin inhibitor heavy chain H4 (ITIH4) is a 120 kDa acute-phase glycoprotein produced primarily in the liver, secreted into the blood, and identified in serum.
24884609	1	35	theme	chain	125:129	arg1	H4					131:132	Inter-alpha-trypsin inhibitor heavy chain H4	89:132	Inter-alpha-trypsin inhibitor heavy chain H4 (ITIH4)	89:140	Inter-alpha-trypsin inhibitor heavy chain H4 (ITIH4) is a 120 kDa acute-phase glycoprotein produced primarily in the liver, secreted into the blood, and identified in serum.
24884609	1	35	theme	chain	125:129	arg1	glycoprotein					167:178	a 120 kDa acute-phase glycoprotein	145:178	a 120 kDa acute-phase glycoprotein produced primarily in the liver, secreted into the blood, and identified in serum	145:260	Inter-alpha-trypsin inhibitor heavy chain H4 (ITIH4) is a 120 kDa acute-phase glycoprotein produced primarily in the liver, secreted into the blood, and identified in serum.
24884609	8	36	theme	nonconsensus	1260:1271	arg1	motif					1277:1281	the rare nonconsensus NVV motif	1251:1281	the rare nonconsensus NVV motif	1251:1281	A fifth N-glycosylation site was discovered at N274 with the rare nonconsensus NVV motif.
24884609	5	37	theme	water	816:820	arg1	presence					798:805	the presence	794:805	the presence of (18)O water	794:820	First, we confirmed that the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577) were glycosylated by treating ITIH4 tryptic/GluC glycopeptides with PNGaseF in the presence of (18)O water.
24884609	7	38	theme	sites	1172:1176	arg1	occupancy					1143:1151	occupancy	1143:1151	occupancy of N-glycosylation sites	1143:1176	While microheterogeneity of N-glycoforms differed between ITIH4 protein expressed in HEK293 cells and protein isolated from serum, occupancy of N-glycosylation sites did not differ.
24884609	4	39	theme	Recombinant	532:542	arg1	ITIH4					544:548	Recombinant ITIH4	532:548	Recombinant ITIH4	532:548	Recombinant ITIH4 was analyzed to optimize glycopeptide analyses, followed by serum-derived ITIH4.
24884609	10	40	theme	isoform-specific	1390:1405	arg1	O-glycoforms					1413:1424	isoform-specific ITIH4 O-glycoforms	1390:1424	isoform-specific ITIH4 O-glycoforms	1390:1424	We also identified isoform-specific ITIH4 O-glycoforms and documented that utilization of O-glycosylation sites on ITIH4 differed between the cell line and serum.
24884609	3	41	gly	glycosylation	443:455	arg1	ITIH4					490:494	recombinant and serum-derived ITIH4	460:494	recombinant and serum-derived ITIH4 using analytical mass spectrometry	460:529	In this study, we aimed to characterize glycosylation of recombinant and serum-derived ITIH4 using analytical mass spectrometry.
24884609	8	42	theme	NVV	1273:1275	arg1	motif					1277:1281	the rare nonconsensus NVV motif	1251:1281	the rare nonconsensus NVV motif	1251:1281	A fifth N-glycosylation site was discovered at N274 with the rare nonconsensus NVV motif.
24884609	1	43	dep	glycoprotein	167:178	arg1	produced					180:187	produced	180:187	produced primarily in the liver	180:210	Inter-alpha-trypsin inhibitor heavy chain H4 (ITIH4) is a 120 kDa acute-phase glycoprotein produced primarily in the liver, secreted into the blood, and identified in serum.
24884609	1	43	dep	glycoprotein	167:178	arg1	secreted					213:220	secreted	213:220	secreted into the blood	213:235	Inter-alpha-trypsin inhibitor heavy chain H4 (ITIH4) is a 120 kDa acute-phase glycoprotein produced primarily in the liver, secreted into the blood, and identified in serum.
24884609	1	43	dep	glycoprotein	167:178	arg1	identified					242:251	identified	242:251	identified in serum	242:260	Inter-alpha-trypsin inhibitor heavy chain H4 (ITIH4) is a 120 kDa acute-phase glycoprotein produced primarily in the liver, secreted into the blood, and identified in serum.
24884609	9	44	theme	recombinant	1352:1362	arg1	ITIH4					1364:1368	recombinant ITIH4	1352:1368	recombinant ITIH4	1352:1368	Site N274 contained high-mannose N-linked glycans in both serum and recombinant ITIH4.
24884609	3	45	link	serum-derived	476:488	arg1	ITIH4					490:494	recombinant and serum-derived ITIH4	460:494	recombinant and serum-derived ITIH4 using analytical mass spectrometry	460:529	In this study, we aimed to characterize glycosylation of recombinant and serum-derived ITIH4 using analytical mass spectrometry.
24884609	4	46	link	serum-derived	610:622	arg1	ITIH4					624:628	serum-derived ITIH4	610:628	serum-derived ITIH4	610:628	Recombinant ITIH4 was analyzed to optimize glycopeptide analyses, followed by serum-derived ITIH4.
24884609	2	47	theme	liver	284:288	arg1	development					290:300	liver development	284:300	liver development	284:300	ITIH4 is involved in liver development and stabilization of the extracellular matrix (ECM), and its expression is altered in liver disease.
24884609	2	48	theme	liver	388:392	arg1	disease					394:400	liver disease	388:400	liver disease	388:400	ITIH4 is involved in liver development and stabilization of the extracellular matrix (ECM), and its expression is altered in liver disease.
24884609	0	49	theme	inhibitor	63:71	arg1	chain					79:83	inter-alpha-trypsin inhibitor heavy chain	43:83	inter-alpha-trypsin inhibitor heavy chain H4	43:86	Site-specific glycan microheterogeneity of inter-alpha-trypsin inhibitor heavy chain H4.
24884609	3	50	theme	recombinant	460:470	arg1	ITIH4					490:494	recombinant and serum-derived ITIH4	460:494	recombinant and serum-derived ITIH4 using analytical mass spectrometry	460:529	In this study, we aimed to characterize glycosylation of recombinant and serum-derived ITIH4 using analytical mass spectrometry.
24884609	10	51	gly	O-glycosylation	1461:1475	arg2	sites					1477:1481	O-glycosylation sites	1461:1481	O-glycosylation sites	1461:1481	We also identified isoform-specific ITIH4 O-glycoforms and documented that utilization of O-glycosylation sites on ITIH4 differed between the cell line and serum.
24884609	7	52	gly	N-glycosylation	1156:1170	arg2	sites					1172:1176	N-glycosylation sites	1156:1176	N-glycosylation sites	1156:1176	While microheterogeneity of N-glycoforms differed between ITIH4 protein expressed in HEK293 cells and protein isolated from serum, occupancy of N-glycosylation sites did not differ.
24884609	8	53	theme	fifth	1196:1200	arg1	site					1218:1221	A fifth N-glycosylation site	1194:1221	A fifth N-glycosylation site	1194:1221	A fifth N-glycosylation site was discovered at N274 with the rare nonconsensus NVV motif.
24884609	0	54	theme	inter-alpha-trypsin	43:61	arg1	chain					79:83	inter-alpha-trypsin inhibitor heavy chain	43:83	inter-alpha-trypsin inhibitor heavy chain H4	43:86	Site-specific glycan microheterogeneity of inter-alpha-trypsin inhibitor heavy chain H4.
24884609	6	55	theme	glycopeptides	903:915	arg1	analysis					872:879	glycosidase-assisted LC-MS/MS analysis	842:879	glycosidase-assisted LC-MS/MS analysis of ITIH4 trypsin-GluC glycopeptides enriched via hydrophilic interaction liquid chromatography	842:974	Next, we performed glycosidase-assisted LC-MS/MS analysis of ITIH4 trypsin-GluC glycopeptides enriched via hydrophilic interaction liquid chromatography to characterize ITIH4 N-glycoforms.
24884609	7	56	theme	N-glycosylation	1156:1170	arg1	sites					1172:1176	N-glycosylation sites	1156:1176	N-glycosylation sites	1156:1176	While microheterogeneity of N-glycoforms differed between ITIH4 protein expressed in HEK293 cells and protein isolated from serum, occupancy of N-glycosylation sites did not differ.
24884609	5	57	gly	glycopeptides	764:776	arg2	glycopeptides					764:776	ITIH4 tryptic/GluC glycopeptides	745:776	ITIH4 tryptic/GluC glycopeptides	745:776	First, we confirmed that the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577) were glycosylated by treating ITIH4 tryptic/GluC glycopeptides with PNGaseF in the presence of (18)O water.
24884609	10	58	from	utilization	1446:1456	arg1	ITIH4					1486:1490	ITIH4	1486:1490	ITIH4	1486:1490	We also identified isoform-specific ITIH4 O-glycoforms and documented that utilization of O-glycosylation sites on ITIH4 differed between the cell line and serum.
24884609	0	59	theme	chain	79:83	arg1	H4					85:86	inter-alpha-trypsin inhibitor heavy chain H4	43:86	inter-alpha-trypsin inhibitor heavy chain H4	43:86	Site-specific glycan microheterogeneity of inter-alpha-trypsin inhibitor heavy chain H4.
24884609	6	60	theme	trypsin-GluC	890:901	arg1	glycopeptides					903:915	ITIH4 trypsin-GluC glycopeptides	884:915	ITIH4 trypsin-GluC glycopeptides enriched via hydrophilic interaction liquid chromatography	884:974	Next, we performed glycosidase-assisted LC-MS/MS analysis of ITIH4 trypsin-GluC glycopeptides enriched via hydrophilic interaction liquid chromatography to characterize ITIH4 N-glycoforms.
24884609	7	61	theme	N-glycoforms	1040:1051	arg1	microheterogeneity					1018:1035	microheterogeneity	1018:1035	microheterogeneity of N-glycoforms	1018:1051	While microheterogeneity of N-glycoforms differed between ITIH4 protein expressed in HEK293 cells and protein isolated from serum, occupancy of N-glycosylation sites did not differ.
24884609	6	62	theme	hydrophilic	930:940	arg1	chromatography					961:974	hydrophilic interaction liquid chromatography	930:974	hydrophilic interaction liquid chromatography	930:974	Next, we performed glycosidase-assisted LC-MS/MS analysis of ITIH4 trypsin-GluC glycopeptides enriched via hydrophilic interaction liquid chromatography to characterize ITIH4 N-glycoforms.
24884609	0	63	gly	microheterogeneity	21:38	arg1	H4					85:86	inter-alpha-trypsin inhibitor heavy chain H4	43:86	inter-alpha-trypsin inhibitor heavy chain H4	43:86	Site-specific glycan microheterogeneity of inter-alpha-trypsin inhibitor heavy chain H4.
24884609	5	64	theme	N-X-S/T	671:677	arg1	N81					688:690	N81	688:690	N81	688:690	First, we confirmed that the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577) were glycosylated by treating ITIH4 tryptic/GluC glycopeptides with PNGaseF in the presence of (18)O water.
24884609	5	64	theme	N-X-S/T	671:677	arg1	sequons					679:685	the four ITIH4 N-X-S/T sequons	656:685	the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577)	656:713	First, we confirmed that the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577) were glycosylated by treating ITIH4 tryptic/GluC glycopeptides with PNGaseF in the presence of (18)O water.
24884609	5	64	theme	N-X-S/T	671:677	arg1	N517					699:702	N517	699:702	N517	699:702	First, we confirmed that the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577) were glycosylated by treating ITIH4 tryptic/GluC glycopeptides with PNGaseF in the presence of (18)O water.
24884609	5	64	theme	N-X-S/T	671:677	arg1	N577					709:712	N577	709:712	N577	709:712	First, we confirmed that the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577) were glycosylated by treating ITIH4 tryptic/GluC glycopeptides with PNGaseF in the presence of (18)O water.
24884609	5	64	theme	N-X-S/T	671:677	arg1	N207					693:696	N207	693:696	N207	693:696	First, we confirmed that the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577) were glycosylated by treating ITIH4 tryptic/GluC glycopeptides with PNGaseF in the presence of (18)O water.
24884609	2	65	theme	matrix	341:346	arg1	development					290:300	liver development	284:300	liver development	284:300	ITIH4 is involved in liver development and stabilization of the extracellular matrix (ECM), and its expression is altered in liver disease.
24884609	2	65	theme	matrix	341:346	arg1	stabilization					306:318	stabilization	306:318	stabilization of the extracellular matrix (ECM)	306:352	ITIH4 is involved in liver development and stabilization of the extracellular matrix (ECM), and its expression is altered in liver disease.
24884609	0	66	theme	heavy	73:77	arg1	chain					79:83	inter-alpha-trypsin inhibitor heavy chain	43:83	inter-alpha-trypsin inhibitor heavy chain H4	43:86	Site-specific glycan microheterogeneity of inter-alpha-trypsin inhibitor heavy chain H4.
24884609	6	67	theme	ITIH4	884:888	arg1	glycopeptides					903:915	ITIH4 trypsin-GluC glycopeptides	884:915	ITIH4 trypsin-GluC glycopeptides enriched via hydrophilic interaction liquid chromatography	884:974	Next, we performed glycosidase-assisted LC-MS/MS analysis of ITIH4 trypsin-GluC glycopeptides enriched via hydrophilic interaction liquid chromatography to characterize ITIH4 N-glycoforms.
24884609	5	68	theme	ITIH4	665:669	arg1	N81					688:690	N81	688:690	N81	688:690	First, we confirmed that the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577) were glycosylated by treating ITIH4 tryptic/GluC glycopeptides with PNGaseF in the presence of (18)O water.
24884609	5	68	theme	ITIH4	665:669	arg1	sequons					679:685	the four ITIH4 N-X-S/T sequons	656:685	the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577)	656:713	First, we confirmed that the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577) were glycosylated by treating ITIH4 tryptic/GluC glycopeptides with PNGaseF in the presence of (18)O water.
24884609	5	68	theme	ITIH4	665:669	arg1	N517					699:702	N517	699:702	N517	699:702	First, we confirmed that the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577) were glycosylated by treating ITIH4 tryptic/GluC glycopeptides with PNGaseF in the presence of (18)O water.
24884609	5	68	theme	ITIH4	665:669	arg1	N577					709:712	N577	709:712	N577	709:712	First, we confirmed that the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577) were glycosylated by treating ITIH4 tryptic/GluC glycopeptides with PNGaseF in the presence of (18)O water.
24884609	5	68	theme	ITIH4	665:669	arg1	N207					693:696	N207	693:696	N207	693:696	First, we confirmed that the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577) were glycosylated by treating ITIH4 tryptic/GluC glycopeptides with PNGaseF in the presence of (18)O water.
24884609	2	69	theme	extracellular	327:339	arg1	ECM					349:351	ECM	349:351	ECM	349:351	ITIH4 is involved in liver development and stabilization of the extracellular matrix (ECM), and its expression is altered in liver disease.
24884609	2	69	theme	extracellular	327:339	arg1	matrix					341:346	extracellular matrix	327:346	the extracellular matrix (ECM)	323:352	ITIH4 is involved in liver development and stabilization of the extracellular matrix (ECM), and its expression is altered in liver disease.
24884609	1	70	gly	glycoprotein	167:178	arg1	H4					131:132	Inter-alpha-trypsin inhibitor heavy chain H4	89:132	Inter-alpha-trypsin inhibitor heavy chain H4 (ITIH4)	89:140	Inter-alpha-trypsin inhibitor heavy chain H4 (ITIH4) is a 120 kDa acute-phase glycoprotein produced primarily in the liver, secreted into the blood, and identified in serum.
24884609	1	70	gly	glycoprotein	167:178	arg1	glycoprotein					167:178	a 120 kDa acute-phase glycoprotein	145:178	a 120 kDa acute-phase glycoprotein produced primarily in the liver, secreted into the blood, and identified in serum	145:260	Inter-alpha-trypsin inhibitor heavy chain H4 (ITIH4) is a 120 kDa acute-phase glycoprotein produced primarily in the liver, secreted into the blood, and identified in serum.
24884609	3	71	theme	mass	513:516	arg1	spectrometry					518:529	analytical mass spectrometry	502:529	analytical mass spectrometry	502:529	In this study, we aimed to characterize glycosylation of recombinant and serum-derived ITIH4 using analytical mass spectrometry.
24884609	7	72	gly	microheterogeneity	1018:1035	arg1	N-glycoforms					1040:1051	N-glycoforms	1040:1051	N-glycoforms	1040:1051	While microheterogeneity of N-glycoforms differed between ITIH4 protein expressed in HEK293 cells and protein isolated from serum, occupancy of N-glycosylation sites did not differ.
24884609	7	73	theme	ITIH4	1070:1074	arg1	protein					1076:1082	ITIH4 protein	1070:1082	ITIH4 protein expressed in HEK293 cells	1070:1108	While microheterogeneity of N-glycoforms differed between ITIH4 protein expressed in HEK293 cells and protein isolated from serum, occupancy of N-glycosylation sites did not differ.
24884609	3	74	theme	ITIH4	490:494	arg1	glycosylation					443:455	glycosylation	443:455	glycosylation of recombinant and serum-derived ITIH4 using analytical mass spectrometry	443:529	In this study, we aimed to characterize glycosylation of recombinant and serum-derived ITIH4 using analytical mass spectrometry.
24884609	4	75	theme	serum-derived	610:622	arg1	ITIH4					624:628	serum-derived ITIH4	610:628	serum-derived ITIH4	610:628	Recombinant ITIH4 was analyzed to optimize glycopeptide analyses, followed by serum-derived ITIH4.
24884609	0	76	theme	H4	85:86	arg1	microheterogeneity					21:38	Site-specific glycan microheterogeneity	0:38	Site-specific glycan microheterogeneity of inter-alpha-trypsin inhibitor heavy chain H4	0:86	Site-specific glycan microheterogeneity of inter-alpha-trypsin inhibitor heavy chain H4.
24884609	9	77	theme	Site	1284:1287	arg1	N274					1289:1292	Site N274	1284:1292	Site N274	1284:1292	Site N274 contained high-mannose N-linked glycans in both serum and recombinant ITIH4.
24884609	5	78	gly	glycosylated	720:731	arg1	N81					688:690	N81	688:690	N81	688:690	First, we confirmed that the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577) were glycosylated by treating ITIH4 tryptic/GluC glycopeptides with PNGaseF in the presence of (18)O water.
24884609	5	78	gly	glycosylated	720:731	arg1	sequons					679:685	the four ITIH4 N-X-S/T sequons	656:685	the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577)	656:713	First, we confirmed that the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577) were glycosylated by treating ITIH4 tryptic/GluC glycopeptides with PNGaseF in the presence of (18)O water.
24884609	5	78	gly	glycosylated	720:731	arg1	N517					699:702	N517	699:702	N517	699:702	First, we confirmed that the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577) were glycosylated by treating ITIH4 tryptic/GluC glycopeptides with PNGaseF in the presence of (18)O water.
24884609	5	78	gly	glycosylated	720:731	arg1	N577					709:712	N577	709:712	N577	709:712	First, we confirmed that the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577) were glycosylated by treating ITIH4 tryptic/GluC glycopeptides with PNGaseF in the presence of (18)O water.
24884609	5	78	gly	glycosylated	720:731	arg1	N207					693:696	N207	693:696	N207	693:696	First, we confirmed that the four ITIH4 N-X-S/T sequons (N81, N207, N517, and N577) were glycosylated by treating ITIH4 tryptic/GluC glycopeptides with PNGaseF in the presence of (18)O water.
24884609	7	79	gly	occupancy	1143:1151	arg2	sites					1172:1176	N-glycosylation sites	1156:1176	N-glycosylation sites	1156:1176	While microheterogeneity of N-glycoforms differed between ITIH4 protein expressed in HEK293 cells and protein isolated from serum, occupancy of N-glycosylation sites did not differ.
24884609	1	80	theme	kDa	151:153	arg1	H4					131:132	Inter-alpha-trypsin inhibitor heavy chain H4	89:132	Inter-alpha-trypsin inhibitor heavy chain H4 (ITIH4)	89:140	Inter-alpha-trypsin inhibitor heavy chain H4 (ITIH4) is a 120 kDa acute-phase glycoprotein produced primarily in the liver, secreted into the blood, and identified in serum.
24884609	1	80	theme	kDa	151:153	arg1	glycoprotein					167:178	a 120 kDa acute-phase glycoprotein	145:178	a 120 kDa acute-phase glycoprotein produced primarily in the liver, secreted into the blood, and identified in serum	145:260	Inter-alpha-trypsin inhibitor heavy chain H4 (ITIH4) is a 120 kDa acute-phase glycoprotein produced primarily in the liver, secreted into the blood, and identified in serum.
24884609	6	81	theme	ITIH4	992:996	arg1	N-glycoforms					998:1009	ITIH4 N-glycoforms	992:1009	ITIH4 N-glycoforms	992:1009	Next, we performed glycosidase-assisted LC-MS/MS analysis of ITIH4 trypsin-GluC glycopeptides enriched via hydrophilic interaction liquid chromatography to characterize ITIH4 N-glycoforms.
18514042	0	0	theme	mass	114:117	arg1	spectrometry					119:130	high-performance liquid chromatography/tandem mass spectrometry	68:130	high-performance liquid chromatography/tandem mass spectrometry	68:130	Simultaneous glycosylation analysis of human serum glycoproteins by high-performance liquid chromatography/tandem mass spectrometry.
18514042	5	1	from	heterogeneity	874:886	arg1	glycopeptides					904:916	the assigned glycopeptides	891:916	the assigned glycopeptides	891:916	Mass spectrometric carbohydrate heterogeneity in the assigned glycopeptides was analyzed by an additional LC/MS.
18514042	3	2	theme	MS/MS	542:546	arg1	spectra					548:554	MS/MS spectra	542:554	MS/MS spectra	542:554	The glycopeptide peaks on the chromatogram were basically assigned by database searching with modified peak-list text files of MS/MS spectra and then based on mass differences of glycan units from characterized glycopeptides.
18514042	0	3	theme	chromatography/tandem	92:112	arg1	spectrometry					119:130	high-performance liquid chromatography/tandem mass spectrometry	68:130	high-performance liquid chromatography/tandem mass spectrometry	68:130	Simultaneous glycosylation analysis of human serum glycoproteins by high-performance liquid chromatography/tandem mass spectrometry.
18514042	4	4	theme	values	765:770	arg1	comparison					721:730	a comparison	719:730	a comparison of their retention times and m/z values with those obtained by LC/MS of commercially available glycoproteins	719:839	Glycopeptide of IgG, haptoglobin and ceruloplasmin were confirmed by means of a comparison of their retention times and m/z values with those obtained by LC/MS of commercially available glycoproteins.
18514042	3	5	theme	spectra	548:554	arg1	files					533:537	modified peak-list text files	509:537	modified peak-list text files of MS/MS spectra	509:554	The glycopeptide peaks on the chromatogram were basically assigned by database searching with modified peak-list text files of MS/MS spectra and then based on mass differences of glycan units from characterized glycopeptides.
18514042	4	6	theme	glycoproteins	827:839	arg1	LC/MS					795:799	LC/MS	795:799	LC/MS of commercially available glycoproteins	795:839	Glycopeptide of IgG, haptoglobin and ceruloplasmin were confirmed by means of a comparison of their retention times and m/z values with those obtained by LC/MS of commercially available glycoproteins.
18514042	3	7	theme	glycopeptide	419:430	arg1	peaks					432:436	The glycopeptide peaks	415:436	The glycopeptide peaks on the chromatogram	415:456	The glycopeptide peaks on the chromatogram were basically assigned by database searching with modified peak-list text files of MS/MS spectra and then based on mass differences of glycan units from characterized glycopeptides.
18514042	2	8	theme	LC/Qq-TOF	336:344	arg1	MS					346:347	LC/Qq-TOF MS	336:347	LC/Qq-TOF MS of human serum tryptic digest, the albumin of which was depleted	336:412	In this study, we performed simultaneous site-specific glycosylation analysis of abundant serum glycoproteins by LC/Qq-TOF MS of human serum tryptic digest, the albumin of which was depleted.
18514042	3	9	from	differences	579:589	arg1	glycopeptides					626:638	characterized glycopeptides	612:638	characterized glycopeptides	612:638	The glycopeptide peaks on the chromatogram were basically assigned by database searching with modified peak-list text files of MS/MS spectra and then based on mass differences of glycan units from characterized glycopeptides.
18514042	3	10	theme	units	601:605	arg1	differences					579:589	mass differences	574:589	mass differences of glycan units from characterized glycopeptides	574:638	The glycopeptide peaks on the chromatogram were basically assigned by database searching with modified peak-list text files of MS/MS spectra and then based on mass differences of glycan units from characterized glycopeptides.
18514042	6	11	theme	site-specific	984:996	arg1	glycosylation					998:1010	site-specific glycosylation	984:1010	site-specific glycosylation of 23 sites in abundant serum glycoproteins	984:1054	We successfully demonstrated site-specific glycosylation of 23 sites in abundant serum glycoproteins.
18514042	4	12	theme	retention	741:749	arg1	times					751:755	their retention times	735:755	their retention times	735:755	Glycopeptide of IgG, haptoglobin and ceruloplasmin were confirmed by means of a comparison of their retention times and m/z values with those obtained by LC/MS of commercially available glycoproteins.
18514042	5	13	gly	glycopeptides	904:916	arg2	glycopeptides					904:916	the assigned glycopeptides	891:916	the assigned glycopeptides	891:916	Mass spectrometric carbohydrate heterogeneity in the assigned glycopeptides was analyzed by an additional LC/MS.
18514042	3	14	theme	text	528:531	arg1	files					533:537	modified peak-list text files	509:537	modified peak-list text files of MS/MS spectra	509:554	The glycopeptide peaks on the chromatogram were basically assigned by database searching with modified peak-list text files of MS/MS spectra and then based on mass differences of glycan units from characterized glycopeptides.
18514042	3	15	gly	glycopeptide	419:430	arg2	glycopeptide					419:430	glycopeptide	419:430	glycopeptide	419:430	The glycopeptide peaks on the chromatogram were basically assigned by database searching with modified peak-list text files of MS/MS spectra and then based on mass differences of glycan units from characterized glycopeptides.
18514042	5	16	theme	carbohydrate	861:872	arg1	heterogeneity					874:886	Mass spectrometric carbohydrate heterogeneity	842:886	Mass spectrometric carbohydrate heterogeneity in the assigned glycopeptides	842:916	Mass spectrometric carbohydrate heterogeneity in the assigned glycopeptides was analyzed by an additional LC/MS.
18514042	2	17	theme	glycoproteins	319:331	arg1	analysis					292:299	simultaneous site-specific glycosylation analysis	251:299	simultaneous site-specific glycosylation analysis of abundant serum glycoproteins	251:331	In this study, we performed simultaneous site-specific glycosylation analysis of abundant serum glycoproteins by LC/Qq-TOF MS of human serum tryptic digest, the albumin of which was depleted.
18514042	2	18	gly	glycoproteins	319:331	arg1	glycoproteins					319:331	abundant serum glycoproteins	304:331	abundant serum glycoproteins	304:331	In this study, we performed simultaneous site-specific glycosylation analysis of abundant serum glycoproteins by LC/Qq-TOF MS of human serum tryptic digest, the albumin of which was depleted.
18514042	4	19	gly	glycoproteins	827:839	arg1	glycoproteins					827:839	commercially available glycoproteins	804:839	commercially available glycoproteins	804:839	Glycopeptide of IgG, haptoglobin and ceruloplasmin were confirmed by means of a comparison of their retention times and m/z values with those obtained by LC/MS of commercially available glycoproteins.
18514042	2	20	theme	serum	313:317	arg1	glycoproteins					319:331	abundant serum glycoproteins	304:331	abundant serum glycoproteins	304:331	In this study, we performed simultaneous site-specific glycosylation analysis of abundant serum glycoproteins by LC/Qq-TOF MS of human serum tryptic digest, the albumin of which was depleted.
18514042	1	21	theme	certain	205:211	arg1	diseases					213:220	certain diseases	205:220	certain diseases	205:220	Changes in the glycosylation of some serum proteins are associated with certain diseases.
18514042	0	22	theme	glycosylation	13:25	arg1	analysis					27:34	Simultaneous glycosylation analysis	0:34	Simultaneous glycosylation analysis of human serum glycoproteins by high-performance liquid chromatography/tandem mass spectrometry.	0:131	Simultaneous glycosylation analysis of human serum glycoproteins by high-performance liquid chromatography/tandem mass spectrometry.
18514042	4	23	with	comparison	721:730	arg1	those					777:781	those	777:781	those	777:781	Glycopeptide of IgG, haptoglobin and ceruloplasmin were confirmed by means of a comparison of their retention times and m/z values with those obtained by LC/MS of commercially available glycoproteins.
18514042	6	24	from	glycosylation	998:1010	arg1	glycoproteins					1042:1054	abundant serum glycoproteins	1027:1054	abundant serum glycoproteins	1027:1054	We successfully demonstrated site-specific glycosylation of 23 sites in abundant serum glycoproteins.
18514042	2	25	theme	serum	358:362	arg1	digest					372:377	human serum tryptic digest	352:377	human serum tryptic digest	352:377	In this study, we performed simultaneous site-specific glycosylation analysis of abundant serum glycoproteins by LC/Qq-TOF MS of human serum tryptic digest, the albumin of which was depleted.
18514042	5	26	theme	additional	937:946	arg1	LC/MS					948:952	an additional LC/MS	934:952	an additional LC/MS	934:952	Mass spectrometric carbohydrate heterogeneity in the assigned glycopeptides was analyzed by an additional LC/MS.
18514042	0	27	theme	Simultaneous	0:11	arg1	analysis					27:34	Simultaneous glycosylation analysis	0:34	Simultaneous glycosylation analysis of human serum glycoproteins by high-performance liquid chromatography/tandem mass spectrometry.	0:131	Simultaneous glycosylation analysis of human serum glycoproteins by high-performance liquid chromatography/tandem mass spectrometry.
18514042	4	28	theme	m/z	761:763	arg1	values					765:770	m/z values	761:770	m/z values	761:770	Glycopeptide of IgG, haptoglobin and ceruloplasmin were confirmed by means of a comparison of their retention times and m/z values with those obtained by LC/MS of commercially available glycoproteins.
18514042	6	29	gly	glycoproteins	1042:1054	arg1	glycoproteins					1042:1054	abundant serum glycoproteins	1027:1054	abundant serum glycoproteins	1027:1054	We successfully demonstrated site-specific glycosylation of 23 sites in abundant serum glycoproteins.
18514042	2	30	theme	human	352:356	arg1	digest					372:377	human serum tryptic digest	352:377	human serum tryptic digest	352:377	In this study, we performed simultaneous site-specific glycosylation analysis of abundant serum glycoproteins by LC/Qq-TOF MS of human serum tryptic digest, the albumin of which was depleted.
18514042	2	31	gly	glycosylation	278:290	arg1	glycoproteins					319:331	abundant serum glycoproteins	304:331	abundant serum glycoproteins	304:331	In this study, we performed simultaneous site-specific glycosylation analysis of abundant serum glycoproteins by LC/Qq-TOF MS of human serum tryptic digest, the albumin of which was depleted.
18514042	1	32	gly	glycosylation	148:160	arg1	proteins					176:183	some serum proteins	165:183	some serum proteins	165:183	Changes in the glycosylation of some serum proteins are associated with certain diseases.
18514042	3	33	from	glycopeptides	626:638	arg1	differences					579:589	mass differences	574:589	mass differences of glycan units from characterized glycopeptides	574:638	The glycopeptide peaks on the chromatogram were basically assigned by database searching with modified peak-list text files of MS/MS spectra and then based on mass differences of glycan units from characterized glycopeptides.
18514042	3	33	from	glycopeptides	626:638	arg1	units					601:605	glycan units	594:605	glycan units from characterized glycopeptides	594:638	The glycopeptide peaks on the chromatogram were basically assigned by database searching with modified peak-list text files of MS/MS spectra and then based on mass differences of glycan units from characterized glycopeptides.
18514042	4	34	theme	ceruloplasmin	678:690	arg1	Glycopeptide					641:652	Glycopeptide	641:652	Glycopeptide of IgG, haptoglobin and ceruloplasmin	641:690	Glycopeptide of IgG, haptoglobin and ceruloplasmin were confirmed by means of a comparison of their retention times and m/z values with those obtained by LC/MS of commercially available glycoproteins.
18514042	3	35	with	searching	494:502	arg1	files					533:537	modified peak-list text files	509:537	modified peak-list text files of MS/MS spectra	509:554	The glycopeptide peaks on the chromatogram were basically assigned by database searching with modified peak-list text files of MS/MS spectra and then based on mass differences of glycan units from characterized glycopeptides.
18514042	3	36	theme	glycan	594:599	arg1	units					601:605	glycan units	594:605	glycan units from characterized glycopeptides	594:638	The glycopeptide peaks on the chromatogram were basically assigned by database searching with modified peak-list text files of MS/MS spectra and then based on mass differences of glycan units from characterized glycopeptides.
18514042	3	37	theme	modified	509:516	arg1	files					533:537	modified peak-list text files	509:537	modified peak-list text files of MS/MS spectra	509:554	The glycopeptide peaks on the chromatogram were basically assigned by database searching with modified peak-list text files of MS/MS spectra and then based on mass differences of glycan units from characterized glycopeptides.
18514042	0	38	theme	serum	45:49	arg1	glycoproteins					51:63	human serum glycoproteins	39:63	human serum glycoproteins	39:63	Simultaneous glycosylation analysis of human serum glycoproteins by high-performance liquid chromatography/tandem mass spectrometry.
18514042	3	39	theme	database	485:492	arg1	searching					494:502	database searching	485:502	database searching with modified peak-list text files of MS/MS spectra	485:554	The glycopeptide peaks on the chromatogram were basically assigned by database searching with modified peak-list text files of MS/MS spectra and then based on mass differences of glycan units from characterized glycopeptides.
18514042	2	40	theme	site-specific	264:276	arg1	analysis					292:299	simultaneous site-specific glycosylation analysis	251:299	simultaneous site-specific glycosylation analysis of abundant serum glycoproteins	251:331	In this study, we performed simultaneous site-specific glycosylation analysis of abundant serum glycoproteins by LC/Qq-TOF MS of human serum tryptic digest, the albumin of which was depleted.
18514042	3	41	gly	glycopeptides	626:638	arg2	glycopeptides					626:638	characterized glycopeptides	612:638	characterized glycopeptides	612:638	The glycopeptide peaks on the chromatogram were basically assigned by database searching with modified peak-list text files of MS/MS spectra and then based on mass differences of glycan units from characterized glycopeptides.
18514042	0	42	theme	human	39:43	arg1	glycoproteins					51:63	human serum glycoproteins	39:63	human serum glycoproteins	39:63	Simultaneous glycosylation analysis of human serum glycoproteins by high-performance liquid chromatography/tandem mass spectrometry.
18514042	6	43	theme	serum	1036:1040	arg1	glycoproteins					1042:1054	abundant serum glycoproteins	1027:1054	abundant serum glycoproteins	1027:1054	We successfully demonstrated site-specific glycosylation of 23 sites in abundant serum glycoproteins.
18514042	4	44	dep	comparison	721:730	arg1	means					710:714	means	710:714	means	710:714	Glycopeptide of IgG, haptoglobin and ceruloplasmin were confirmed by means of a comparison of their retention times and m/z values with those obtained by LC/MS of commercially available glycoproteins.
18514042	0	45	gly	glycosylation	13:25	arg1	glycoproteins					51:63	human serum glycoproteins	39:63	human serum glycoproteins	39:63	Simultaneous glycosylation analysis of human serum glycoproteins by high-performance liquid chromatography/tandem mass spectrometry.
18514042	5	46	theme	Mass	842:845	arg1	heterogeneity					874:886	Mass spectrometric carbohydrate heterogeneity	842:886	Mass spectrometric carbohydrate heterogeneity in the assigned glycopeptides	842:916	Mass spectrometric carbohydrate heterogeneity in the assigned glycopeptides was analyzed by an additional LC/MS.
18514042	6	47	theme	abundant	1027:1034	arg1	glycoproteins					1042:1054	abundant serum glycoproteins	1027:1054	abundant serum glycoproteins	1027:1054	We successfully demonstrated site-specific glycosylation of 23 sites in abundant serum glycoproteins.
18514042	5	48	theme	spectrometric	847:859	arg1	heterogeneity					874:886	Mass spectrometric carbohydrate heterogeneity	842:886	Mass spectrometric carbohydrate heterogeneity in the assigned glycopeptides	842:916	Mass spectrometric carbohydrate heterogeneity in the assigned glycopeptides was analyzed by an additional LC/MS.
18514042	3	49	theme	characterized	612:624	arg1	glycopeptides					626:638	characterized glycopeptides	612:638	characterized glycopeptides	612:638	The glycopeptide peaks on the chromatogram were basically assigned by database searching with modified peak-list text files of MS/MS spectra and then based on mass differences of glycan units from characterized glycopeptides.
18514042	0	50	theme	glycoproteins	51:63	arg1	analysis					27:34	Simultaneous glycosylation analysis	0:34	Simultaneous glycosylation analysis of human serum glycoproteins by high-performance liquid chromatography/tandem mass spectrometry.	0:131	Simultaneous glycosylation analysis of human serum glycoproteins by high-performance liquid chromatography/tandem mass spectrometry.
18514042	4	51	theme	times	751:755	arg1	comparison					721:730	a comparison	719:730	a comparison of their retention times and m/z values with those obtained by LC/MS of commercially available glycoproteins	719:839	Glycopeptide of IgG, haptoglobin and ceruloplasmin were confirmed by means of a comparison of their retention times and m/z values with those obtained by LC/MS of commercially available glycoproteins.
18514042	1	52	from	Changes	133:139	arg1	glycosylation					148:160	the glycosylation	144:160	the glycosylation of some serum proteins	144:183	Changes in the glycosylation of some serum proteins are associated with certain diseases.
18514042	6	53	theme	sites	1018:1022	arg1	glycosylation					998:1010	site-specific glycosylation	984:1010	site-specific glycosylation of 23 sites in abundant serum glycoproteins	984:1054	We successfully demonstrated site-specific glycosylation of 23 sites in abundant serum glycoproteins.
18514042	2	54	theme	abundant	304:311	arg1	glycoproteins					319:331	abundant serum glycoproteins	304:331	abundant serum glycoproteins	304:331	In this study, we performed simultaneous site-specific glycosylation analysis of abundant serum glycoproteins by LC/Qq-TOF MS of human serum tryptic digest, the albumin of which was depleted.
18514042	2	55	theme	simultaneous	251:262	arg1	analysis					292:299	simultaneous site-specific glycosylation analysis	251:299	simultaneous site-specific glycosylation analysis of abundant serum glycoproteins	251:331	In this study, we performed simultaneous site-specific glycosylation analysis of abundant serum glycoproteins by LC/Qq-TOF MS of human serum tryptic digest, the albumin of which was depleted.
18514042	2	56	theme	digest	372:377	arg1	albumin					384:390	the albumin	380:390	the albumin	380:390	In this study, we performed simultaneous site-specific glycosylation analysis of abundant serum glycoproteins by LC/Qq-TOF MS of human serum tryptic digest, the albumin of which was depleted.
18514042	2	56	theme	digest	372:377	arg1	MS					346:347	LC/Qq-TOF MS	336:347	LC/Qq-TOF MS of human serum tryptic digest, the albumin of which was depleted	336:412	In this study, we performed simultaneous site-specific glycosylation analysis of abundant serum glycoproteins by LC/Qq-TOF MS of human serum tryptic digest, the albumin of which was depleted.
18514042	4	57	theme	IgG	657:659	arg1	Glycopeptide					641:652	Glycopeptide	641:652	Glycopeptide of IgG, haptoglobin and ceruloplasmin	641:690	Glycopeptide of IgG, haptoglobin and ceruloplasmin were confirmed by means of a comparison of their retention times and m/z values with those obtained by LC/MS of commercially available glycoproteins.
18514042	4	58	theme	available	817:825	arg1	glycoproteins					827:839	commercially available glycoproteins	804:839	commercially available glycoproteins	804:839	Glycopeptide of IgG, haptoglobin and ceruloplasmin were confirmed by means of a comparison of their retention times and m/z values with those obtained by LC/MS of commercially available glycoproteins.
18514042	3	59	theme	mass	574:577	arg1	differences					579:589	mass differences	574:589	mass differences of glycan units from characterized glycopeptides	574:638	The glycopeptide peaks on the chromatogram were basically assigned by database searching with modified peak-list text files of MS/MS spectra and then based on mass differences of glycan units from characterized glycopeptides.
18514042	2	60	theme	tryptic	364:370	arg1	digest					372:377	human serum tryptic digest	352:377	human serum tryptic digest	352:377	In this study, we performed simultaneous site-specific glycosylation analysis of abundant serum glycoproteins by LC/Qq-TOF MS of human serum tryptic digest, the albumin of which was depleted.
18514042	3	61	theme	peak-list	518:526	arg1	files					533:537	modified peak-list text files	509:537	modified peak-list text files of MS/MS spectra	509:554	The glycopeptide peaks on the chromatogram were basically assigned by database searching with modified peak-list text files of MS/MS spectra and then based on mass differences of glycan units from characterized glycopeptides.
18514042	0	62	theme	liquid	85:90	arg1	spectrometry					119:130	high-performance liquid chromatography/tandem mass spectrometry	68:130	high-performance liquid chromatography/tandem mass spectrometry	68:130	Simultaneous glycosylation analysis of human serum glycoproteins by high-performance liquid chromatography/tandem mass spectrometry.
18514042	6	63	gly	glycosylation	998:1010	arg1	sites					1018:1022	23 sites	1015:1022	23 sites	1015:1022	We successfully demonstrated site-specific glycosylation of 23 sites in abundant serum glycoproteins.
18514042	6	63	gly	glycosylation	998:1010	arg1	glycoproteins					1042:1054	abundant serum glycoproteins	1027:1054	abundant serum glycoproteins	1027:1054	We successfully demonstrated site-specific glycosylation of 23 sites in abundant serum glycoproteins.
18514042	0	64	gly	glycoproteins	51:63	arg1	glycoproteins					51:63	human serum glycoproteins	39:63	human serum glycoproteins	39:63	Simultaneous glycosylation analysis of human serum glycoproteins by high-performance liquid chromatography/tandem mass spectrometry.
18514042	5	65	theme	assigned	895:902	arg1	glycopeptides					904:916	the assigned glycopeptides	891:916	the assigned glycopeptides	891:916	Mass spectrometric carbohydrate heterogeneity in the assigned glycopeptides was analyzed by an additional LC/MS.
18514042	1	66	theme	serum	170:174	arg1	proteins					176:183	some serum proteins	165:183	some serum proteins	165:183	Changes in the glycosylation of some serum proteins are associated with certain diseases.
18514042	4	67	theme	haptoglobin	662:672	arg1	Glycopeptide					641:652	Glycopeptide	641:652	Glycopeptide of IgG, haptoglobin and ceruloplasmin	641:690	Glycopeptide of IgG, haptoglobin and ceruloplasmin were confirmed by means of a comparison of their retention times and m/z values with those obtained by LC/MS of commercially available glycoproteins.
18514042	0	68	theme	high-performance	68:83	arg1	spectrometry					119:130	high-performance liquid chromatography/tandem mass spectrometry	68:130	high-performance liquid chromatography/tandem mass spectrometry	68:130	Simultaneous glycosylation analysis of human serum glycoproteins by high-performance liquid chromatography/tandem mass spectrometry.
18514042	3	69	from	peaks	432:436	arg1	chromatogram					445:456	the chromatogram	441:456	the chromatogram	441:456	The glycopeptide peaks on the chromatogram were basically assigned by database searching with modified peak-list text files of MS/MS spectra and then based on mass differences of glycan units from characterized glycopeptides.
18514042	2	70	theme	glycosylation	278:290	arg1	analysis					292:299	simultaneous site-specific glycosylation analysis	251:299	simultaneous site-specific glycosylation analysis of abundant serum glycoproteins	251:331	In this study, we performed simultaneous site-specific glycosylation analysis of abundant serum glycoproteins by LC/Qq-TOF MS of human serum tryptic digest, the albumin of which was depleted.
18514042	1	71	theme	proteins	176:183	arg1	glycosylation					148:160	the glycosylation	144:160	the glycosylation of some serum proteins	144:183	Changes in the glycosylation of some serum proteins are associated with certain diseases.
20657584	3	0	from	levels	455:460	arg1	proteins					476:483	endogenous proteins	465:483	endogenous proteins	465:483	This approach enables rapid quantification of in vivo glycosylation levels on endogenous proteins without the need for protein purification, advanced instrumentation or expensive radiolabels.
20657584	6	1	theme	post-translational	1168:1185	arg1	modifications					1187:1199	other post-translational modifications	1162:1199	other post-translational modifications	1162:1199	We anticipate that this mass-tagging strategy will advance our understanding of O-GlcNAc glycosylation, as well as other post-translational modifications and poorly understood glycosylation motifs.
20657584	6	2	theme	mass-tagging	1071:1082	arg1	strategy					1084:1091	this mass-tagging strategy	1066:1091	this mass-tagging strategy	1066:1091	We anticipate that this mass-tagging strategy will advance our understanding of O-GlcNAc glycosylation, as well as other post-translational modifications and poorly understood glycosylation motifs.
20657584	6	3	theme	glycosylation	1136:1148	arg1	modifications					1187:1199	other post-translational modifications	1162:1199	other post-translational modifications	1162:1199	We anticipate that this mass-tagging strategy will advance our understanding of O-GlcNAc glycosylation, as well as other post-translational modifications and poorly understood glycosylation motifs.
20657584	6	3	theme	glycosylation	1136:1148	arg1	understanding					1110:1122	our understanding	1106:1122	our understanding of O-GlcNAc glycosylation	1106:1148	We anticipate that this mass-tagging strategy will advance our understanding of O-GlcNAc glycosylation, as well as other post-translational modifications and poorly understood glycosylation motifs.
20657584	6	3	theme	glycosylation	1136:1148	arg1	motifs					1237:1242	poorly understood glycosylation motifs	1205:1242	poorly understood glycosylation motifs	1205:1242	We anticipate that this mass-tagging strategy will advance our understanding of O-GlcNAc glycosylation, as well as other post-translational modifications and poorly understood glycosylation motifs.
20657584	5	4	from	relationship	949:960	arg1	undetectable					1010:1021	undetectable	1010:1021	undetectable	1010:1021	Finally, we apply this strategy to rapidly assess the complex interplay between glycosylation and phosphorylation and discover an unexpected reverse 'yin-yang' relationship on the transcriptional repressor MeCP2 that was undetectable by traditional methods.
20657584	5	4	from	relationship	949:960	arg1	MeCP2					995:999	the transcriptional repressor MeCP2	965:999	the transcriptional repressor MeCP2 that was undetectable by traditional methods	965:1044	Finally, we apply this strategy to rapidly assess the complex interplay between glycosylation and phosphorylation and discover an unexpected reverse 'yin-yang' relationship on the transcriptional repressor MeCP2 that was undetectable by traditional methods.
20657584	6	5	theme	glycosylation	1223:1235	arg1	motifs					1237:1242	poorly understood glycosylation motifs	1205:1242	poorly understood glycosylation motifs	1205:1242	We anticipate that this mass-tagging strategy will advance our understanding of O-GlcNAc glycosylation, as well as other post-translational modifications and poorly understood glycosylation motifs.
20657584	3	6	dep	in	433:434	arg1	vivo					436:439	vivo	436:439	vivo	436:439	This approach enables rapid quantification of in vivo glycosylation levels on endogenous proteins without the need for protein purification, advanced instrumentation or expensive radiolabels.
20657584	2	7	theme	protein	317:323	arg1	subpopulation					325:337	the O-GlcNAc-modified protein subpopulation	295:337	the O-GlcNAc-modified protein subpopulation using resolvable polyethylene glycol mass tags	295:384	Here we describe a powerful method to visualize the O-GlcNAc-modified protein subpopulation using resolvable polyethylene glycol mass tags.
20657584	5	8	theme	traditional	1026:1036	arg1	methods					1038:1044	traditional methods	1026:1044	traditional methods	1026:1044	Finally, we apply this strategy to rapidly assess the complex interplay between glycosylation and phosphorylation and discover an unexpected reverse 'yin-yang' relationship on the transcriptional repressor MeCP2 that was undetectable by traditional methods.
20657584	3	9	theme	rapid	409:413	arg1	quantification					415:428	rapid quantification	409:428	rapid quantification of in vivo glycosylation levels on endogenous proteins	409:483	This approach enables rapid quantification of in vivo glycosylation levels on endogenous proteins without the need for protein purification, advanced instrumentation or expensive radiolabels.
20657584	3	10	from	quantification	415:428	arg1	proteins					476:483	endogenous proteins	465:483	endogenous proteins	465:483	This approach enables rapid quantification of in vivo glycosylation levels on endogenous proteins without the need for protein purification, advanced instrumentation or expensive radiolabels.
20657584	2	11	theme	O-GlcNAc-modified	299:315	arg1	subpopulation					325:337	the O-GlcNAc-modified protein subpopulation	295:337	the O-GlcNAc-modified protein subpopulation using resolvable polyethylene glycol mass tags	295:384	Here we describe a powerful method to visualize the O-GlcNAc-modified protein subpopulation using resolvable polyethylene glycol mass tags.
20657584	6	12	gly	glycosylation	1223:1235	arg2	motifs					1237:1242	poorly understood glycosylation motifs	1205:1242	poorly understood glycosylation motifs	1205:1242	We anticipate that this mass-tagging strategy will advance our understanding of O-GlcNAc glycosylation, as well as other post-translational modifications and poorly understood glycosylation motifs.
20657584	5	13	theme	complex	843:849	arg1	interplay					851:859	the complex interplay	839:859	the complex interplay between glycosylation and phosphorylation	839:901	Finally, we apply this strategy to rapidly assess the complex interplay between glycosylation and phosphorylation and discover an unexpected reverse 'yin-yang' relationship on the transcriptional repressor MeCP2 that was undetectable by traditional methods.
20657584	5	14	theme	repressor	985:993	arg1	undetectable					1010:1021	undetectable	1010:1021	undetectable	1010:1021	Finally, we apply this strategy to rapidly assess the complex interplay between glycosylation and phosphorylation and discover an unexpected reverse 'yin-yang' relationship on the transcriptional repressor MeCP2 that was undetectable by traditional methods.
20657584	5	14	theme	repressor	985:993	arg1	MeCP2					995:999	the transcriptional repressor MeCP2	965:999	the transcriptional repressor MeCP2 that was undetectable by traditional methods	965:1044	Finally, we apply this strategy to rapidly assess the complex interplay between glycosylation and phosphorylation and discover an unexpected reverse 'yin-yang' relationship on the transcriptional repressor MeCP2 that was undetectable by traditional methods.
20657584	4	15	dep	state	625:629	arg1	mono-					645:649	mono-	645:649	mono-	645:649	In addition, it establishes the glycosylation state (for example, mono-, di-, tri-) of proteins, providing information regarding overall O-GlcNAc site occupancy that cannot be obtained using mass spectrometry.
20657584	4	15	dep	state	625:629	arg1	tri-					657:660	tri-	657:660	tri-	657:660	In addition, it establishes the glycosylation state (for example, mono-, di-, tri-) of proteins, providing information regarding overall O-GlcNAc site occupancy that cannot be obtained using mass spectrometry.
20657584	4	15	dep	state	625:629	arg1	di-					652:654	di-	652:654	di-	652:654	In addition, it establishes the glycosylation state (for example, mono-, di-, tri-) of proteins, providing information regarding overall O-GlcNAc site occupancy that cannot be obtained using mass spectrometry.
20657584	6	16	theme	understood	1212:1221	arg1	motifs					1237:1242	poorly understood glycosylation motifs	1205:1242	poorly understood glycosylation motifs	1205:1242	We anticipate that this mass-tagging strategy will advance our understanding of O-GlcNAc glycosylation, as well as other post-translational modifications and poorly understood glycosylation motifs.
20657584	1	17	theme	Mechanistic	89:99	arg1	studies					101:107	Mechanistic studies	89:107	Mechanistic studies of O-GlcNAc glycosylation	89:133	Mechanistic studies of O-GlcNAc glycosylation have been limited by an inability to monitor the glycosylation stoichiometries of proteins obtained from cells.
20657584	6	18	theme	other	1162:1166	arg1	modifications					1187:1199	other post-translational modifications	1162:1199	other post-translational modifications	1162:1199	We anticipate that this mass-tagging strategy will advance our understanding of O-GlcNAc glycosylation, as well as other post-translational modifications and poorly understood glycosylation motifs.
20657584	1	19	theme	glycosylation	184:196	arg1	stoichiometries					198:212	the glycosylation stoichiometries	180:212	the glycosylation stoichiometries of proteins obtained from cells	180:244	Mechanistic studies of O-GlcNAc glycosylation have been limited by an inability to monitor the glycosylation stoichiometries of proteins obtained from cells.
20657584	3	20	theme	in	433:434	arg1	levels					455:460	in vivo glycosylation levels	433:460	in vivo glycosylation levels on endogenous proteins	433:483	This approach enables rapid quantification of in vivo glycosylation levels on endogenous proteins without the need for protein purification, advanced instrumentation or expensive radiolabels.
20657584	2	21	theme	polyethylene	356:367	arg1	glycol					369:374	polyethylene glycol	356:374	resolvable polyethylene glycol mass tags	345:384	Here we describe a powerful method to visualize the O-GlcNAc-modified protein subpopulation using resolvable polyethylene glycol mass tags.
20657584	4	22	theme	O-GlcNAc	716:723	arg1	occupancy					730:738	overall O-GlcNAc site occupancy	708:738	overall O-GlcNAc site occupancy that cannot be obtained using mass spectrometry	708:786	In addition, it establishes the glycosylation state (for example, mono-, di-, tri-) of proteins, providing information regarding overall O-GlcNAc site occupancy that cannot be obtained using mass spectrometry.
20657584	2	23	theme	resolvable	345:354	arg1	tags					381:384	resolvable polyethylene glycol mass tags	345:384	resolvable polyethylene glycol mass tags	345:384	Here we describe a powerful method to visualize the O-GlcNAc-modified protein subpopulation using resolvable polyethylene glycol mass tags.
20657584	4	24	theme	overall	708:714	arg1	occupancy					730:738	overall O-GlcNAc site occupancy	708:738	overall O-GlcNAc site occupancy that cannot be obtained using mass spectrometry	708:786	In addition, it establishes the glycosylation state (for example, mono-, di-, tri-) of proteins, providing information regarding overall O-GlcNAc site occupancy that cannot be obtained using mass spectrometry.
20657584	4	25	theme	glycosylation	611:623	arg1	state					625:629	the glycosylation state	607:629	the glycosylation state (for example, mono-, di-, tri-) of proteins	607:673	In addition, it establishes the glycosylation state (for example, mono-, di-, tri-) of proteins, providing information regarding overall O-GlcNAc site occupancy that cannot be obtained using mass spectrometry.
20657584	1	26	theme	O-GlcNAc	112:119	arg1	glycosylation					121:133	O-GlcNAc glycosylation	112:133	O-GlcNAc glycosylation	112:133	Mechanistic studies of O-GlcNAc glycosylation have been limited by an inability to monitor the glycosylation stoichiometries of proteins obtained from cells.
20657584	1	27	theme	proteins	217:224	arg1	stoichiometries					198:212	the glycosylation stoichiometries	180:212	the glycosylation stoichiometries of proteins obtained from cells	180:244	Mechanistic studies of O-GlcNAc glycosylation have been limited by an inability to monitor the glycosylation stoichiometries of proteins obtained from cells.
20657584	0	28	theme	O-glycosylation	18:32	arg1	Quantification					0:13	Quantification	0:13	Quantification of O-glycosylation stoichiometry and dynamics	0:59	Quantification of O-glycosylation stoichiometry and dynamics using resolvable mass tags.
20657584	1	29	theme	glycosylation	121:133	arg1	studies					101:107	Mechanistic studies	89:107	Mechanistic studies of O-GlcNAc glycosylation	89:133	Mechanistic studies of O-GlcNAc glycosylation have been limited by an inability to monitor the glycosylation stoichiometries of proteins obtained from cells.
20657584	6	30	theme	O-GlcNAc	1127:1134	arg1	glycosylation					1136:1148	O-GlcNAc glycosylation	1127:1148	O-GlcNAc glycosylation	1127:1148	We anticipate that this mass-tagging strategy will advance our understanding of O-GlcNAc glycosylation, as well as other post-translational modifications and poorly understood glycosylation motifs.
20657584	0	31	theme	dynamics	52:59	arg1	Quantification					0:13	Quantification	0:13	Quantification of O-glycosylation stoichiometry and dynamics	0:59	Quantification of O-glycosylation stoichiometry and dynamics using resolvable mass tags.
20657584	5	32	theme	transcriptional	969:983	arg1	undetectable					1010:1021	undetectable	1010:1021	undetectable	1010:1021	Finally, we apply this strategy to rapidly assess the complex interplay between glycosylation and phosphorylation and discover an unexpected reverse 'yin-yang' relationship on the transcriptional repressor MeCP2 that was undetectable by traditional methods.
20657584	5	32	theme	transcriptional	969:983	arg1	MeCP2					995:999	the transcriptional repressor MeCP2	965:999	the transcriptional repressor MeCP2 that was undetectable by traditional methods	965:1044	Finally, we apply this strategy to rapidly assess the complex interplay between glycosylation and phosphorylation and discover an unexpected reverse 'yin-yang' relationship on the transcriptional repressor MeCP2 that was undetectable by traditional methods.
20657584	3	33	theme	endogenous	465:474	arg1	proteins					476:483	endogenous proteins	465:483	endogenous proteins	465:483	This approach enables rapid quantification of in vivo glycosylation levels on endogenous proteins without the need for protein purification, advanced instrumentation or expensive radiolabels.
20657584	5	34	theme	reverse	930:936	arg1	relationship					949:960	an unexpected reverse 'yin-yang' relationship	916:960	an unexpected reverse 'yin-yang' relationship on the transcriptional repressor MeCP2 that was undetectable by traditional methods	916:1044	Finally, we apply this strategy to rapidly assess the complex interplay between glycosylation and phosphorylation and discover an unexpected reverse 'yin-yang' relationship on the transcriptional repressor MeCP2 that was undetectable by traditional methods.
20657584	4	35	gly	glycosylation	611:623	arg1	proteins					666:673	proteins	666:673	proteins	666:673	In addition, it establishes the glycosylation state (for example, mono-, di-, tri-) of proteins, providing information regarding overall O-GlcNAc site occupancy that cannot be obtained using mass spectrometry.
20657584	3	36	theme	protein	506:512	arg1	purification					514:525	protein purification	506:525	protein purification	506:525	This approach enables rapid quantification of in vivo glycosylation levels on endogenous proteins without the need for protein purification, advanced instrumentation or expensive radiolabels.
20657584	3	37	theme	glycosylation	441:453	arg1	levels					455:460	in vivo glycosylation levels	433:460	in vivo glycosylation levels on endogenous proteins	433:483	This approach enables rapid quantification of in vivo glycosylation levels on endogenous proteins without the need for protein purification, advanced instrumentation or expensive radiolabels.
20657584	0	38	theme	mass	78:81	arg1	tags					83:86	resolvable mass tags	67:86	resolvable mass tags	67:86	Quantification of O-glycosylation stoichiometry and dynamics using resolvable mass tags.
20657584	3	39	theme	levels	455:460	arg1	quantification					415:428	rapid quantification	409:428	rapid quantification of in vivo glycosylation levels on endogenous proteins	409:483	This approach enables rapid quantification of in vivo glycosylation levels on endogenous proteins without the need for protein purification, advanced instrumentation or expensive radiolabels.
20657584	3	40	theme	expensive	556:564	arg1	radiolabels					566:576	expensive radiolabels	556:576	expensive radiolabels	556:576	This approach enables rapid quantification of in vivo glycosylation levels on endogenous proteins without the need for protein purification, advanced instrumentation or expensive radiolabels.
20657584	4	41	theme	mass	770:773	arg1	spectrometry					775:786	mass spectrometry	770:786	mass spectrometry	770:786	In addition, it establishes the glycosylation state (for example, mono-, di-, tri-) of proteins, providing information regarding overall O-GlcNAc site occupancy that cannot be obtained using mass spectrometry.
20657584	2	42	theme	mass	376:379	arg1	tags					381:384	resolvable polyethylene glycol mass tags	345:384	resolvable polyethylene glycol mass tags	345:384	Here we describe a powerful method to visualize the O-GlcNAc-modified protein subpopulation using resolvable polyethylene glycol mass tags.
20657584	0	43	dep	O-glycosylation	18:32	arg1	stoichiometry					34:46	stoichiometry	34:46	stoichiometry	34:46	Quantification of O-glycosylation stoichiometry and dynamics using resolvable mass tags.
20657584	3	44	from	proteins	476:483	arg1	quantification					415:428	rapid quantification	409:428	rapid quantification of in vivo glycosylation levels on endogenous proteins	409:483	This approach enables rapid quantification of in vivo glycosylation levels on endogenous proteins without the need for protein purification, advanced instrumentation or expensive radiolabels.
20657584	2	45	theme	glycol	369:374	arg1	tags					381:384	resolvable polyethylene glycol mass tags	345:384	resolvable polyethylene glycol mass tags	345:384	Here we describe a powerful method to visualize the O-GlcNAc-modified protein subpopulation using resolvable polyethylene glycol mass tags.
20657584	3	46	theme	advanced	528:535	arg1	instrumentation					537:551	advanced instrumentation	528:551	advanced instrumentation	528:551	This approach enables rapid quantification of in vivo glycosylation levels on endogenous proteins without the need for protein purification, advanced instrumentation or expensive radiolabels.
20657584	2	47	theme	powerful	266:273	arg1	method					275:280	a powerful method	264:280	a powerful method to visualize the O-GlcNAc-modified protein subpopulation using resolvable polyethylene glycol mass tags	264:384	Here we describe a powerful method to visualize the O-GlcNAc-modified protein subpopulation using resolvable polyethylene glycol mass tags.
20657584	4	48	theme	proteins	666:673	arg1	state					625:629	the glycosylation state	607:629	the glycosylation state (for example, mono-, di-, tri-) of proteins	607:673	In addition, it establishes the glycosylation state (for example, mono-, di-, tri-) of proteins, providing information regarding overall O-GlcNAc site occupancy that cannot be obtained using mass spectrometry.
20657584	5	49	theme	yin-yang	939:946	arg1	relationship					949:960	an unexpected reverse 'yin-yang' relationship	916:960	an unexpected reverse 'yin-yang' relationship on the transcriptional repressor MeCP2 that was undetectable by traditional methods	916:1044	Finally, we apply this strategy to rapidly assess the complex interplay between glycosylation and phosphorylation and discover an unexpected reverse 'yin-yang' relationship on the transcriptional repressor MeCP2 that was undetectable by traditional methods.
20657584	5	50	theme	unexpected	919:928	arg1	relationship					949:960	an unexpected reverse 'yin-yang' relationship	916:960	an unexpected reverse 'yin-yang' relationship on the transcriptional repressor MeCP2 that was undetectable by traditional methods	916:1044	Finally, we apply this strategy to rapidly assess the complex interplay between glycosylation and phosphorylation and discover an unexpected reverse 'yin-yang' relationship on the transcriptional repressor MeCP2 that was undetectable by traditional methods.
20657584	0	51	theme	resolvable	67:76	arg1	tags					83:86	resolvable mass tags	67:86	resolvable mass tags	67:86	Quantification of O-glycosylation stoichiometry and dynamics using resolvable mass tags.
20657584	4	52	theme	site	725:728	arg1	occupancy					730:738	overall O-GlcNAc site occupancy	708:738	overall O-GlcNAc site occupancy that cannot be obtained using mass spectrometry	708:786	In addition, it establishes the glycosylation state (for example, mono-, di-, tri-) of proteins, providing information regarding overall O-GlcNAc site occupancy that cannot be obtained using mass spectrometry.
23584533	7	0	theme	O-glycoproteome	1245:1259	arg1	view					1233:1236	The greatly expanded view	1212:1236	The greatly expanded view of the O-glycoproteome	1212:1259	The greatly expanded view of the O-glycoproteome should facilitate the exploration of how site-specific O-glycosylation regulates protein function.
23584533	5	1	theme	human	907:911	arg1	O-glycoproteome					913:927	the human O-glycoproteome	903:927	the human O-glycoproteome	903:927	We implemented this on 12 human cell lines from different organs, and present a first map of the human O-glycoproteome with almost 3000 glycosites in over 600 O-glycoproteins as well as an improved NetOGlyc4.0 model for prediction of O-glycosylation.
23584533	5	2	theme	O-glycoproteome	913:927	arg1	map					896:898	a first map	888:898	a first map of the human O-glycoproteome	888:927	We implemented this on 12 human cell lines from different organs, and present a first map of the human O-glycoproteome with almost 3000 glycosites in over 600 O-glycoproteins as well as an improved NetOGlyc4.0 model for prediction of O-glycosylation.
23584533	6	3	theme	cell	1118:1121	arg1	line					1123:1126	each cell line	1113:1126	each cell line	1113:1126	The finding of unique subsets of O-glycoproteins in each cell line provides evidence that the O-glycoproteome is differentially regulated and dynamic.
23584533	5	4	theme	NetOGlyc4.0	1008:1018	arg1	model					1020:1024	an improved NetOGlyc4.0 model	996:1024	over 600 O-glycoproteins as well as an improved NetOGlyc4.0 model for prediction of O-glycosylation	960:1058	We implemented this on 12 human cell lines from different organs, and present a first map of the human O-glycoproteome with almost 3000 glycosites in over 600 O-glycoproteins as well as an improved NetOGlyc4.0 model for prediction of O-glycosylation.
23584533	5	5	theme	O-glycosylation	1044:1058	arg1	prediction					1030:1039	prediction	1030:1039	prediction of O-glycosylation	1030:1058	We implemented this on 12 human cell lines from different organs, and present a first map of the human O-glycoproteome with almost 3000 glycosites in over 600 O-glycoproteins as well as an improved NetOGlyc4.0 model for prediction of O-glycosylation.
23584533	4	6	theme	ETD-based	771:779	arg1	analysis					800:807	'bottom-up' ETD-based mass spectrometric analysis	759:807	'bottom-up' ETD-based mass spectrometric analysis	759:807	We have developed a genetic engineering approach using human cell lines to simplify O-glycosylation (SimpleCells) that enables proteome-wide discovery of O-glycan sites using 'bottom-up' ETD-based mass spectrometric analysis.
23584533	4	7	theme	engineering	612:622	arg1	approach					624:631	a genetic engineering approach	602:631	a genetic engineering approach	602:631	We have developed a genetic engineering approach using human cell lines to simplify O-glycosylation (SimpleCells) that enables proteome-wide discovery of O-glycan sites using 'bottom-up' ETD-based mass spectrometric analysis.
23584533	4	8	theme	spectrometric	786:798	arg1	analysis					800:807	'bottom-up' ETD-based mass spectrometric analysis	759:807	'bottom-up' ETD-based mass spectrometric analysis	759:807	We have developed a genetic engineering approach using human cell lines to simplify O-glycosylation (SimpleCells) that enables proteome-wide discovery of O-glycan sites using 'bottom-up' ETD-based mass spectrometric analysis.
23584533	2	9	theme	glycoproteomes	298:311	arg1	knowledge					279:287	substantial knowledge	267:287	substantial knowledge of these glycoproteomes	267:311	While several types of glycosylation can be predicted by the protein sequence context, and substantial knowledge of these glycoproteomes is available, our knowledge of the GalNAc-type O-glycosylation is highly limited.
23584533	4	10	theme	genetic	604:610	arg1	approach					624:631	a genetic engineering approach	602:631	a genetic engineering approach	602:631	We have developed a genetic engineering approach using human cell lines to simplify O-glycosylation (SimpleCells) that enables proteome-wide discovery of O-glycan sites using 'bottom-up' ETD-based mass spectrometric analysis.
23584533	5	11	gly	O-glycoproteins	969:983	arg1	O-glycoproteins					969:983	over 600 O-glycoproteins	960:983	over 600 O-glycoproteins as well as an improved NetOGlyc4.0 model for prediction of O-glycosylation	960:1058	We implemented this on 12 human cell lines from different organs, and present a first map of the human O-glycoproteome with almost 3000 glycosites in over 600 O-glycoproteins as well as an improved NetOGlyc4.0 model for prediction of O-glycosylation.
23584533	4	12	theme	sites	747:751	arg1	discovery					725:733	proteome-wide discovery	711:733	proteome-wide discovery of O-glycan sites	711:751	We have developed a genetic engineering approach using human cell lines to simplify O-glycosylation (SimpleCells) that enables proteome-wide discovery of O-glycan sites using 'bottom-up' ETD-based mass spectrometric analysis.
23584533	6	13	from	finding	1065:1071	arg1	line					1123:1126	each cell line	1113:1126	each cell line	1113:1126	The finding of unique subsets of O-glycoproteins in each cell line provides evidence that the O-glycoproteome is differentially regulated and dynamic.
23584533	0	14	theme	Precision	0:8	arg1	mapping					10:16	Precision mapping	0:16	Precision mapping of the human O-GalNAc	0:38	Precision mapping of the human O-GalNAc glycoproteome through SimpleCell technology.
23584533	3	15	theme	polypeptide	457:467	arg1	GalNAc-transferases					469:487	20 polypeptide GalNAc-transferases	454:487	20 polypeptide GalNAc-transferases attaching the initiating GalNAc monosaccharides to Ser and Thr (and likely some Tyr) residues	454:581	This type of glycosylation is unique in being regulated by 20 polypeptide GalNAc-transferases attaching the initiating GalNAc monosaccharides to Ser and Thr (and likely some Tyr) residues.
23584533	5	16	theme	human	836:840	arg1	lines					847:851	12 human cell lines	833:851	12 human cell lines from different organs	833:873	We implemented this on 12 human cell lines from different organs, and present a first map of the human O-glycoproteome with almost 3000 glycosites in over 600 O-glycoproteins as well as an improved NetOGlyc4.0 model for prediction of O-glycosylation.
23584533	5	17	from	glycosites	946:955	arg1	model					1020:1024	an improved NetOGlyc4.0 model	996:1024	over 600 O-glycoproteins as well as an improved NetOGlyc4.0 model for prediction of O-glycosylation	960:1058	We implemented this on 12 human cell lines from different organs, and present a first map of the human O-glycoproteome with almost 3000 glycosites in over 600 O-glycoproteins as well as an improved NetOGlyc4.0 model for prediction of O-glycosylation.
23584533	5	17	from	glycosites	946:955	arg1	O-glycoproteins					969:983	over 600 O-glycoproteins	960:983	over 600 O-glycoproteins as well as an improved NetOGlyc4.0 model for prediction of O-glycosylation	960:1058	We implemented this on 12 human cell lines from different organs, and present a first map of the human O-glycoproteome with almost 3000 glycosites in over 600 O-glycoproteins as well as an improved NetOGlyc4.0 model for prediction of O-glycosylation.
23584533	5	18	theme	first	890:894	arg1	map					896:898	a first map	888:898	a first map of the human O-glycoproteome	888:927	We implemented this on 12 human cell lines from different organs, and present a first map of the human O-glycoproteome with almost 3000 glycosites in over 600 O-glycoproteins as well as an improved NetOGlyc4.0 model for prediction of O-glycosylation.
23584533	3	19	theme	glycosylation	408:420	arg1	type					400:403	This type	395:403	This type of glycosylation	395:420	This type of glycosylation is unique in being regulated by 20 polypeptide GalNAc-transferases attaching the initiating GalNAc monosaccharides to Ser and Thr (and likely some Tyr) residues.
23584533	3	20	dep	Thr	548:550	arg1	Tyr					569:571	Tyr	569:571	Tyr	569:571	This type of glycosylation is unique in being regulated by 20 polypeptide GalNAc-transferases attaching the initiating GalNAc monosaccharides to Ser and Thr (and likely some Tyr) residues.
23584533	6	21	theme	subsets	1083:1089	arg1	finding					1065:1071	The finding	1061:1071	The finding of unique subsets of O-glycoproteins in each cell line	1061:1126	The finding of unique subsets of O-glycoproteins in each cell line provides evidence that the O-glycoproteome is differentially regulated and dynamic.
23584533	5	22	theme	cell	842:845	arg1	lines					847:851	12 human cell lines	833:851	12 human cell lines from different organs	833:873	We implemented this on 12 human cell lines from different organs, and present a first map of the human O-glycoproteome with almost 3000 glycosites in over 600 O-glycoproteins as well as an improved NetOGlyc4.0 model for prediction of O-glycosylation.
23584533	4	23	theme	mass	781:784	arg1	analysis					800:807	'bottom-up' ETD-based mass spectrometric analysis	759:807	'bottom-up' ETD-based mass spectrometric analysis	759:807	We have developed a genetic engineering approach using human cell lines to simplify O-glycosylation (SimpleCells) that enables proteome-wide discovery of O-glycan sites using 'bottom-up' ETD-based mass spectrometric analysis.
23584533	5	24	theme	different	858:866	arg1	organs					868:873	different organs	858:873	different organs	858:873	We implemented this on 12 human cell lines from different organs, and present a first map of the human O-glycoproteome with almost 3000 glycosites in over 600 O-glycoproteins as well as an improved NetOGlyc4.0 model for prediction of O-glycosylation.
23584533	2	25	theme	glycosylation	199:211	arg1	types					190:194	several types	182:194	several types of glycosylation	182:211	While several types of glycosylation can be predicted by the protein sequence context, and substantial knowledge of these glycoproteomes is available, our knowledge of the GalNAc-type O-glycosylation is highly limited.
23584533	1	26	theme	abundant	111:118	arg1	modification					150:161	the most abundant and diverse posttranslational modification	102:161	the most abundant and diverse posttranslational modification of proteins	102:173	Glycosylation is the most abundant and diverse posttranslational modification of proteins.
23584533	1	26	theme	abundant	111:118	arg1	Glycosylation					85:97	Glycosylation	85:97	Glycosylation	85:97	Glycosylation is the most abundant and diverse posttranslational modification of proteins.
23584533	3	27	theme	initiating	503:512	arg1	monosaccharides					521:535	the initiating GalNAc monosaccharides	499:535	the initiating GalNAc monosaccharides	499:535	This type of glycosylation is unique in being regulated by 20 polypeptide GalNAc-transferases attaching the initiating GalNAc monosaccharides to Ser and Thr (and likely some Tyr) residues.
23584533	0	28	theme	O-GalNAc	31:38	arg1	mapping					10:16	Precision mapping	0:16	Precision mapping of the human O-GalNAc	0:38	Precision mapping of the human O-GalNAc glycoproteome through SimpleCell technology.
23584533	2	29	theme	GalNAc-type	348:358	arg1	O-glycosylation					360:374	the GalNAc-type O-glycosylation	344:374	the GalNAc-type O-glycosylation	344:374	While several types of glycosylation can be predicted by the protein sequence context, and substantial knowledge of these glycoproteomes is available, our knowledge of the GalNAc-type O-glycosylation is highly limited.
23584533	5	30	gly	glycosites	946:955	arg2	glycosites					946:955	almost 3000 glycosites	934:955	almost 3000 glycosites in over 600 O-glycoproteins as well as an improved NetOGlyc4.0 model for prediction of O-glycosylation	934:1058	We implemented this on 12 human cell lines from different organs, and present a first map of the human O-glycoproteome with almost 3000 glycosites in over 600 O-glycoproteins as well as an improved NetOGlyc4.0 model for prediction of O-glycosylation.
23584533	0	31	theme	human	25:29	arg1	O-GalNAc					31:38	the human O-GalNAc	21:38	the human O-GalNAc	21:38	Precision mapping of the human O-GalNAc glycoproteome through SimpleCell technology.
23584533	2	32	theme	sequence	245:252	arg1	context					254:260	the protein sequence context	233:260	the protein sequence context	233:260	While several types of glycosylation can be predicted by the protein sequence context, and substantial knowledge of these glycoproteomes is available, our knowledge of the GalNAc-type O-glycosylation is highly limited.
23584533	6	33	gly	O-glycoproteins	1094:1108	arg1	O-glycoproteins					1094:1108	O-glycoproteins	1094:1108	O-glycoproteins	1094:1108	The finding of unique subsets of O-glycoproteins in each cell line provides evidence that the O-glycoproteome is differentially regulated and dynamic.
23584533	2	34	theme	several	182:188	arg1	types					190:194	several types	182:194	several types of glycosylation	182:211	While several types of glycosylation can be predicted by the protein sequence context, and substantial knowledge of these glycoproteomes is available, our knowledge of the GalNAc-type O-glycosylation is highly limited.
23584533	2	35	theme	protein	237:243	arg1	context					254:260	the protein sequence context	233:260	the protein sequence context	233:260	While several types of glycosylation can be predicted by the protein sequence context, and substantial knowledge of these glycoproteomes is available, our knowledge of the GalNAc-type O-glycosylation is highly limited.
23584533	2	36	theme	O-glycosylation	360:374	arg1	knowledge					331:339	our knowledge	327:339	our knowledge of the GalNAc-type O-glycosylation	327:374	While several types of glycosylation can be predicted by the protein sequence context, and substantial knowledge of these glycoproteomes is available, our knowledge of the GalNAc-type O-glycosylation is highly limited.
23584533	7	37	theme	protein	1342:1348	arg1	function					1350:1357	protein function	1342:1357	protein function	1342:1357	The greatly expanded view of the O-glycoproteome should facilitate the exploration of how site-specific O-glycosylation regulates protein function.
23584533	1	38	theme	diverse	124:130	arg1	modification					150:161	the most abundant and diverse posttranslational modification	102:161	the most abundant and diverse posttranslational modification of proteins	102:173	Glycosylation is the most abundant and diverse posttranslational modification of proteins.
23584533	1	38	theme	diverse	124:130	arg1	Glycosylation					85:97	Glycosylation	85:97	Glycosylation	85:97	Glycosylation is the most abundant and diverse posttranslational modification of proteins.
23584533	5	39	theme	improved	999:1006	arg1	model					1020:1024	an improved NetOGlyc4.0 model	996:1024	over 600 O-glycoproteins as well as an improved NetOGlyc4.0 model for prediction of O-glycosylation	960:1058	We implemented this on 12 human cell lines from different organs, and present a first map of the human O-glycoproteome with almost 3000 glycosites in over 600 O-glycoproteins as well as an improved NetOGlyc4.0 model for prediction of O-glycosylation.
23584533	5	40	from	organs	868:873	arg1	lines					847:851	12 human cell lines	833:851	12 human cell lines from different organs	833:873	We implemented this on 12 human cell lines from different organs, and present a first map of the human O-glycoproteome with almost 3000 glycosites in over 600 O-glycoproteins as well as an improved NetOGlyc4.0 model for prediction of O-glycosylation.
23584533	3	41	theme	GalNAc	514:519	arg1	monosaccharides					521:535	the initiating GalNAc monosaccharides	499:535	the initiating GalNAc monosaccharides	499:535	This type of glycosylation is unique in being regulated by 20 polypeptide GalNAc-transferases attaching the initiating GalNAc monosaccharides to Ser and Thr (and likely some Tyr) residues.
23584533	3	42	dep	Ser	540:542	arg1	residues					574:581	residues	574:581	residues	574:581	This type of glycosylation is unique in being regulated by 20 polypeptide GalNAc-transferases attaching the initiating GalNAc monosaccharides to Ser and Thr (and likely some Tyr) residues.
23584533	2	43	theme	substantial	267:277	arg1	knowledge					279:287	substantial knowledge	267:287	substantial knowledge of these glycoproteomes	267:311	While several types of glycosylation can be predicted by the protein sequence context, and substantial knowledge of these glycoproteomes is available, our knowledge of the GalNAc-type O-glycosylation is highly limited.
23584533	7	44	theme	site-specific	1302:1314	arg1	O-glycosylation					1316:1330	site-specific O-glycosylation	1302:1330	site-specific O-glycosylation	1302:1330	The greatly expanded view of the O-glycoproteome should facilitate the exploration of how site-specific O-glycosylation regulates protein function.
23584533	1	45	theme	posttranslational	132:148	arg1	modification					150:161	the most abundant and diverse posttranslational modification	102:161	the most abundant and diverse posttranslational modification of proteins	102:173	Glycosylation is the most abundant and diverse posttranslational modification of proteins.
23584533	1	45	theme	posttranslational	132:148	arg1	Glycosylation					85:97	Glycosylation	85:97	Glycosylation	85:97	Glycosylation is the most abundant and diverse posttranslational modification of proteins.
23584533	6	46	theme	unique	1076:1081	arg1	subsets					1083:1089	unique subsets	1076:1089	unique subsets of O-glycoproteins	1076:1108	The finding of unique subsets of O-glycoproteins in each cell line provides evidence that the O-glycoproteome is differentially regulated and dynamic.
23584533	4	47	theme	proteome-wide	711:723	arg1	discovery					725:733	proteome-wide discovery	711:733	proteome-wide discovery of O-glycan sites	711:751	We have developed a genetic engineering approach using human cell lines to simplify O-glycosylation (SimpleCells) that enables proteome-wide discovery of O-glycan sites using 'bottom-up' ETD-based mass spectrometric analysis.
23584533	6	48	theme	O-glycoproteins	1094:1108	arg1	subsets					1083:1089	unique subsets	1076:1089	unique subsets of O-glycoproteins	1076:1108	The finding of unique subsets of O-glycoproteins in each cell line provides evidence that the O-glycoproteome is differentially regulated and dynamic.
23584533	4	49	theme	cell	645:648	arg1	lines					650:654	human cell lines	639:654	human cell lines	639:654	We have developed a genetic engineering approach using human cell lines to simplify O-glycosylation (SimpleCells) that enables proteome-wide discovery of O-glycan sites using 'bottom-up' ETD-based mass spectrometric analysis.
23584533	0	50	theme	SimpleCell	62:71	arg1	technology					73:82	SimpleCell technology	62:82	SimpleCell technology	62:82	Precision mapping of the human O-GalNAc glycoproteome through SimpleCell technology.
23584533	7	51	theme	expanded	1224:1231	arg1	view					1233:1236	The greatly expanded view	1212:1236	The greatly expanded view of the O-glycoproteome	1212:1259	The greatly expanded view of the O-glycoproteome should facilitate the exploration of how site-specific O-glycosylation regulates protein function.
23584533	4	52	theme	human	639:643	arg1	lines					650:654	human cell lines	639:654	human cell lines	639:654	We have developed a genetic engineering approach using human cell lines to simplify O-glycosylation (SimpleCells) that enables proteome-wide discovery of O-glycan sites using 'bottom-up' ETD-based mass spectrometric analysis.
23584533	1	53	theme	proteins	166:173	arg1	modification					150:161	the most abundant and diverse posttranslational modification	102:161	the most abundant and diverse posttranslational modification of proteins	102:173	Glycosylation is the most abundant and diverse posttranslational modification of proteins.
23584533	1	53	theme	proteins	166:173	arg1	Glycosylation					85:97	Glycosylation	85:97	Glycosylation	85:97	Glycosylation is the most abundant and diverse posttranslational modification of proteins.
23584533	4	54	theme	O-glycan	738:745	arg1	sites					747:751	O-glycan sites	738:751	O-glycan sites	738:751	We have developed a genetic engineering approach using human cell lines to simplify O-glycosylation (SimpleCells) that enables proteome-wide discovery of O-glycan sites using 'bottom-up' ETD-based mass spectrometric analysis.
29405629	3	0	theme	transmembrane	303:315	arg1	protein					317:323	a multipass transmembrane protein	291:323	a multipass transmembrane protein that localizes to the endoplasmic reticulum (ER)	291:372	DPY19L3 is predicted to be a multipass transmembrane protein that localizes to the endoplasmic reticulum (ER); however, its structure is undetermined.
29405629	3	0	theme	transmembrane	303:315	arg1	DPY19L3					264:270	DPY19L3	264:270	DPY19L3	264:270	DPY19L3 is predicted to be a multipass transmembrane protein that localizes to the endoplasmic reticulum (ER); however, its structure is undetermined.
29405629	7	1	gly	N-glycosylations	1296:1311	arg1	DPY19L3					1316:1322	DPY19L3	1316:1322	DPY19L3	1316:1322	Isoform2 does not possess C-mannosyltransferase activity, indicating the importance of the C-terminal region; however, N-glycosylations of DPY19L3 do not have any roles for its enzymatic activity.
29405629	4	2	theme	in silico	479:487	arg1	analysis					489:496	in silico analysis	479:496	in silico analysis	479:496	In this study, we propose a topological structure of DPY19L3 by in silico analysis and experimental methods such as redox-sensitive luciferase assay and introduction of N-glycosylation sites, suggesting that DPY19L3 comprises 11 transmembrane regions and two re-entrant loops with the N- and C-terminal ends facing the cytoplasm and ER lumen, respectively.
29405629	6	3	theme	C-terminal	1139:1148	arg1	region					1158:1163	the C-terminal luminal region	1135:1163	the C-terminal luminal region of DPY19L3	1135:1174	By mass spectrometry, we measured the C-mannosyltransferase activity of N-glycosylation-defective mutants of DPY19L3 and isoform2, a splice variant, which lacks the C-terminal luminal region of DPY19L3.
29405629	4	4	gly	N-glycosylation	584:598	arg2	sites					600:604	N-glycosylation sites	584:604	N-glycosylation sites	584:604	In this study, we propose a topological structure of DPY19L3 by in silico analysis and experimental methods such as redox-sensitive luciferase assay and introduction of N-glycosylation sites, suggesting that DPY19L3 comprises 11 transmembrane regions and two re-entrant loops with the N- and C-terminal ends facing the cytoplasm and ER lumen, respectively.
29405629	3	5	theme	endoplasmic	347:357	arg1	ER					370:371	ER	370:371	ER	370:371	DPY19L3 is predicted to be a multipass transmembrane protein that localizes to the endoplasmic reticulum (ER); however, its structure is undetermined.
29405629	3	5	theme	endoplasmic	347:357	arg1	reticulum					359:367	the endoplasmic reticulum	343:367	the endoplasmic reticulum (ER)	343:372	DPY19L3 is predicted to be a multipass transmembrane protein that localizes to the endoplasmic reticulum (ER); however, its structure is undetermined.
29405629	5	6	from	Asn118	894:899	arg1	N-glycosylated					876:889	N-glycosylated	876:889	N-glycosylated	876:889	Furthermore, DPY19L3 has four predicted N-glycosylation sites, and we have demonstrated that DPY19L3 is N-glycosylated at Asn118 and Asn704 but not Asn319 and Asn439 , supporting our topological model.
29405629	4	7	dep	N-	700:701	arg1	the					696:698	the	696:698	the	696:698	In this study, we propose a topological structure of DPY19L3 by in silico analysis and experimental methods such as redox-sensitive luciferase assay and introduction of N-glycosylation sites, suggesting that DPY19L3 comprises 11 transmembrane regions and two re-entrant loops with the N- and C-terminal ends facing the cytoplasm and ER lumen, respectively.
29405629	8	8	theme	novel	1380:1384	arg1	findings					1386:1393	These novel findings	1374:1393	These novel findings on DPY19L3	1374:1404	These novel findings on DPY19L3 provide important insights into the mechanism of C-mannosylation.
29405629	1	9	dep	functions	125:133	arg1	the					121:123	the	121:123	the	121:123	C-mannosylation is a rare type of protein glycosylation, the functions and mechanisms of which remain unclear.
29405629	4	10	theme	ER	748:749	arg1	lumen					751:755	ER lumen	748:755	ER lumen	748:755	In this study, we propose a topological structure of DPY19L3 by in silico analysis and experimental methods such as redox-sensitive luciferase assay and introduction of N-glycosylation sites, suggesting that DPY19L3 comprises 11 transmembrane regions and two re-entrant loops with the N- and C-terminal ends facing the cytoplasm and ER lumen, respectively.
29405629	8	11	from	findings	1386:1393	arg1	DPY19L3					1398:1404	DPY19L3	1398:1404	DPY19L3	1398:1404	These novel findings on DPY19L3 provide important insights into the mechanism of C-mannosylation.
29405629	5	12	theme	topological	955:965	arg1	model					967:971	our topological model	951:971	our topological model	951:971	Furthermore, DPY19L3 has four predicted N-glycosylation sites, and we have demonstrated that DPY19L3 is N-glycosylated at Asn118 and Asn704 but not Asn319 and Asn439 , supporting our topological model.
29405629	6	13	theme	isoform2	1095:1102	arg1	mutants					1072:1078	N-glycosylation-defective mutants	1046:1078	N-glycosylation-defective mutants of DPY19L3 and isoform2, a splice variant, which lacks the C-terminal luminal region of DPY19L3	1046:1174	By mass spectrometry, we measured the C-mannosyltransferase activity of N-glycosylation-defective mutants of DPY19L3 and isoform2, a splice variant, which lacks the C-terminal luminal region of DPY19L3.
29405629	6	14	theme	DPY19L3	1168:1174	arg1	region					1158:1163	the C-terminal luminal region	1135:1163	the C-terminal luminal region of DPY19L3	1135:1174	By mass spectrometry, we measured the C-mannosyltransferase activity of N-glycosylation-defective mutants of DPY19L3 and isoform2, a splice variant, which lacks the C-terminal luminal region of DPY19L3.
29405629	4	15	theme	transmembrane	644:656	arg1	regions					658:664	11 transmembrane regions	641:664	11 transmembrane regions	641:664	In this study, we propose a topological structure of DPY19L3 by in silico analysis and experimental methods such as redox-sensitive luciferase assay and introduction of N-glycosylation sites, suggesting that DPY19L3 comprises 11 transmembrane regions and two re-entrant loops with the N- and C-terminal ends facing the cytoplasm and ER lumen, respectively.
29405629	4	16	theme	topological	443:453	arg1	structure					455:463	a topological structure	441:463	a topological structure of DPY19L3	441:474	In this study, we propose a topological structure of DPY19L3 by in silico analysis and experimental methods such as redox-sensitive luciferase assay and introduction of N-glycosylation sites, suggesting that DPY19L3 comprises 11 transmembrane regions and two re-entrant loops with the N- and C-terminal ends facing the cytoplasm and ER lumen, respectively.
29405629	7	17	theme	region	1279:1284	arg1	importance					1250:1259	the importance	1246:1259	the importance of the C-terminal region	1246:1284	Isoform2 does not possess C-mannosyltransferase activity, indicating the importance of the C-terminal region; however, N-glycosylations of DPY19L3 do not have any roles for its enzymatic activity.
29405629	1	18	theme	rare	85:88	arg1	type					90:93	a rare type	83:93	a rare type	83:93	C-mannosylation is a rare type of protein glycosylation, the functions and mechanisms of which remain unclear.
29405629	1	18	theme	rare	85:88	arg1	C-mannosylation					64:78	C-mannosylation	64:78	C-mannosylation	64:78	C-mannosylation is a rare type of protein glycosylation, the functions and mechanisms of which remain unclear.
29405629	2	19	from	C-mannosyltransferase	212:232	arg1	cells					257:261	human cells	251:261	human cells	251:261	Recently, we identified DPY19L3 as a C-mannosyltransferase of R-spondin1 in human cells.
29405629	6	20	theme	DPY19L3	1083:1089	arg1	mutants					1072:1078	N-glycosylation-defective mutants	1046:1078	N-glycosylation-defective mutants of DPY19L3 and isoform2, a splice variant, which lacks the C-terminal luminal region of DPY19L3	1046:1174	By mass spectrometry, we measured the C-mannosyltransferase activity of N-glycosylation-defective mutants of DPY19L3 and isoform2, a splice variant, which lacks the C-terminal luminal region of DPY19L3.
29405629	0	21	theme	Topological	0:10	arg1	analysis					12:19	Topological analysis	0:19	Topological analysis of DPY19L3	0:30	Topological analysis of DPY19L3, a human C-mannosyltransferase.
29405629	1	22	theme	type	90:93	arg1	mechanisms					139:148	mechanisms	139:148	mechanisms	139:148	C-mannosylation is a rare type of protein glycosylation, the functions and mechanisms of which remain unclear.
29405629	1	22	theme	type	90:93	arg1	functions					125:133	functions	125:133	functions	125:133	C-mannosylation is a rare type of protein glycosylation, the functions and mechanisms of which remain unclear.
29405629	0	23	theme	DPY19L3	24:30	arg1	analysis					12:19	Topological analysis	0:19	Topological analysis of DPY19L3	0:30	Topological analysis of DPY19L3, a human C-mannosyltransferase.
29405629	5	24	from	Asn704	905:910	arg1	N-glycosylated					876:889	N-glycosylated	876:889	N-glycosylated	876:889	Furthermore, DPY19L3 has four predicted N-glycosylation sites, and we have demonstrated that DPY19L3 is N-glycosylated at Asn118 and Asn704 but not Asn319 and Asn439 , supporting our topological model.
29405629	6	25	theme	luminal	1150:1156	arg1	region					1158:1163	the C-terminal luminal region	1135:1163	the C-terminal luminal region of DPY19L3	1135:1174	By mass spectrometry, we measured the C-mannosyltransferase activity of N-glycosylation-defective mutants of DPY19L3 and isoform2, a splice variant, which lacks the C-terminal luminal region of DPY19L3.
29405629	6	26	theme	mutants	1072:1078	arg1	activity					1034:1041	the C-mannosyltransferase activity	1008:1041	the C-mannosyltransferase activity of N-glycosylation-defective mutants of DPY19L3 and isoform2, a splice variant, which lacks the C-terminal luminal region of DPY19L3	1008:1174	By mass spectrometry, we measured the C-mannosyltransferase activity of N-glycosylation-defective mutants of DPY19L3 and isoform2, a splice variant, which lacks the C-terminal luminal region of DPY19L3.
29405629	5	27	theme	N-glycosylation	812:826	arg1	sites					828:832	four predicted N-glycosylation sites	797:832	four predicted N-glycosylation sites	797:832	Furthermore, DPY19L3 has four predicted N-glycosylation sites, and we have demonstrated that DPY19L3 is N-glycosylated at Asn118 and Asn704 but not Asn319 and Asn439 , supporting our topological model.
29405629	4	28	theme	luciferase	547:556	arg1	assay					558:562	redox-sensitive luciferase assay	531:562	redox-sensitive luciferase assay	531:562	In this study, we propose a topological structure of DPY19L3 by in silico analysis and experimental methods such as redox-sensitive luciferase assay and introduction of N-glycosylation sites, suggesting that DPY19L3 comprises 11 transmembrane regions and two re-entrant loops with the N- and C-terminal ends facing the cytoplasm and ER lumen, respectively.
29405629	1	29	theme	protein	98:104	arg1	glycosylation					106:118	protein glycosylation	98:118	protein glycosylation	98:118	C-mannosylation is a rare type of protein glycosylation, the functions and mechanisms of which remain unclear.
29405629	6	30	theme	N-glycosylation-defective	1046:1070	arg1	mutants					1072:1078	N-glycosylation-defective mutants	1046:1078	N-glycosylation-defective mutants of DPY19L3 and isoform2, a splice variant, which lacks the C-terminal luminal region of DPY19L3	1046:1174	By mass spectrometry, we measured the C-mannosyltransferase activity of N-glycosylation-defective mutants of DPY19L3 and isoform2, a splice variant, which lacks the C-terminal luminal region of DPY19L3.
29405629	4	31	theme	redox-sensitive	531:545	arg1	assay					558:562	redox-sensitive luciferase assay	531:562	redox-sensitive luciferase assay	531:562	In this study, we propose a topological structure of DPY19L3 by in silico analysis and experimental methods such as redox-sensitive luciferase assay and introduction of N-glycosylation sites, suggesting that DPY19L3 comprises 11 transmembrane regions and two re-entrant loops with the N- and C-terminal ends facing the cytoplasm and ER lumen, respectively.
29405629	8	32	theme	C-mannosylation	1455:1469	arg1	mechanism					1442:1450	the mechanism	1438:1450	the mechanism of C-mannosylation	1438:1469	These novel findings on DPY19L3 provide important insights into the mechanism of C-mannosylation.
29405629	0	33	dep	C-mannosyltransferase	41:61	arg1	analysis					12:19	Topological analysis	0:19	Topological analysis of DPY19L3	0:30	Topological analysis of DPY19L3, a human C-mannosyltransferase.
29405629	6	34	theme	C-mannosyltransferase	1012:1032	arg1	activity					1034:1041	the C-mannosyltransferase activity	1008:1041	the C-mannosyltransferase activity of N-glycosylation-defective mutants of DPY19L3 and isoform2, a splice variant, which lacks the C-terminal luminal region of DPY19L3	1008:1174	By mass spectrometry, we measured the C-mannosyltransferase activity of N-glycosylation-defective mutants of DPY19L3 and isoform2, a splice variant, which lacks the C-terminal luminal region of DPY19L3.
29405629	5	35	theme	predicted	802:810	arg1	sites					828:832	four predicted N-glycosylation sites	797:832	four predicted N-glycosylation sites	797:832	Furthermore, DPY19L3 has four predicted N-glycosylation sites, and we have demonstrated that DPY19L3 is N-glycosylated at Asn118 and Asn704 but not Asn319 and Asn439 , supporting our topological model.
29405629	7	36	contain	possess	1195:1201	arg2	activity					1225:1232	C-mannosyltransferase activity	1203:1232	C-mannosyltransferase activity	1203:1232	Isoform2 does not possess C-mannosyltransferase activity, indicating the importance of the C-terminal region; however, N-glycosylations of DPY19L3 do not have any roles for its enzymatic activity.
29405629	7	36	contain	possess	1195:1201	arg1	Isoform2					1177:1184	Isoform2	1177:1184	Isoform2	1177:1184	Isoform2 does not possess C-mannosyltransferase activity, indicating the importance of the C-terminal region; however, N-glycosylations of DPY19L3 do not have any roles for its enzymatic activity.
29405629	7	37	theme	DPY19L3	1316:1322	arg1	N-glycosylations					1296:1311	N-glycosylations	1296:1311	N-glycosylations of DPY19L3	1296:1322	Isoform2 does not possess C-mannosyltransferase activity, indicating the importance of the C-terminal region; however, N-glycosylations of DPY19L3 do not have any roles for its enzymatic activity.
29405629	7	38	theme	C-mannosyltransferase	1203:1223	arg1	activity					1225:1232	C-mannosyltransferase activity	1203:1232	C-mannosyltransferase activity	1203:1232	Isoform2 does not possess C-mannosyltransferase activity, indicating the importance of the C-terminal region; however, N-glycosylations of DPY19L3 do not have any roles for its enzymatic activity.
29405629	5	39	gly	N-glycosylated	876:889	arg2	Asn319					920:925	Asn319	920:925	Asn319	920:925	Furthermore, DPY19L3 has four predicted N-glycosylation sites, and we have demonstrated that DPY19L3 is N-glycosylated at Asn118 and Asn704 but not Asn319 and Asn439 , supporting our topological model.
29405629	5	39	gly	N-glycosylated	876:889	arg2	Asn704					905:910	Asn704	905:910	Asn704	905:910	Furthermore, DPY19L3 has four predicted N-glycosylation sites, and we have demonstrated that DPY19L3 is N-glycosylated at Asn118 and Asn704 but not Asn319 and Asn439 , supporting our topological model.
29405629	5	39	gly	N-glycosylated	876:889	arg2	Asn118					894:899	Asn118	894:899	Asn118	894:899	Furthermore, DPY19L3 has four predicted N-glycosylation sites, and we have demonstrated that DPY19L3 is N-glycosylated at Asn118 and Asn704 but not Asn319 and Asn439 , supporting our topological model.
29405629	5	39	gly	N-glycosylated	876:889	arg1	DPY19L3					865:871	DPY19L3	865:871	DPY19L3	865:871	Furthermore, DPY19L3 has four predicted N-glycosylation sites, and we have demonstrated that DPY19L3 is N-glycosylated at Asn118 and Asn704 but not Asn319 and Asn439 , supporting our topological model.
29405629	5	40	contain	has	793:795	arg2	sites					828:832	four predicted N-glycosylation sites	797:832	four predicted N-glycosylation sites	797:832	Furthermore, DPY19L3 has four predicted N-glycosylation sites, and we have demonstrated that DPY19L3 is N-glycosylated at Asn118 and Asn704 but not Asn319 and Asn439 , supporting our topological model.
29405629	5	40	contain	has	793:795	arg1	DPY19L3					785:791	DPY19L3	785:791	DPY19L3	785:791	Furthermore, DPY19L3 has four predicted N-glycosylation sites, and we have demonstrated that DPY19L3 is N-glycosylated at Asn118 and Asn704 but not Asn319 and Asn439 , supporting our topological model.
29405629	5	41	gly	N-glycosylation	812:826	arg2	sites					828:832	four predicted N-glycosylation sites	797:832	four predicted N-glycosylation sites	797:832	Furthermore, DPY19L3 has four predicted N-glycosylation sites, and we have demonstrated that DPY19L3 is N-glycosylated at Asn118 and Asn704 but not Asn319 and Asn439 , supporting our topological model.
29405629	5	41	gly	N-glycosylation	812:826	arg2	four					797:800	four	797:800	four	797:800	Furthermore, DPY19L3 has four predicted N-glycosylation sites, and we have demonstrated that DPY19L3 is N-glycosylated at Asn118 and Asn704 but not Asn319 and Asn439 , supporting our topological model.
29405629	1	42	theme	glycosylation	106:118	arg1	type					90:93	a rare type	83:93	a rare type	83:93	C-mannosylation is a rare type of protein glycosylation, the functions and mechanisms of which remain unclear.
29405629	1	42	theme	glycosylation	106:118	arg1	C-mannosylation					64:78	C-mannosylation	64:78	C-mannosylation	64:78	C-mannosylation is a rare type of protein glycosylation, the functions and mechanisms of which remain unclear.
29405629	0	43	theme	human	35:39	arg1	C-mannosyltransferase					41:61	a human C-mannosyltransferase	33:61	a human C-mannosyltransferase	33:61	Topological analysis of DPY19L3, a human C-mannosyltransferase.
29405629	3	44	theme	multipass	293:301	arg1	protein					317:323	a multipass transmembrane protein	291:323	a multipass transmembrane protein that localizes to the endoplasmic reticulum (ER)	291:372	DPY19L3 is predicted to be a multipass transmembrane protein that localizes to the endoplasmic reticulum (ER); however, its structure is undetermined.
29405629	3	44	theme	multipass	293:301	arg1	DPY19L3					264:270	DPY19L3	264:270	DPY19L3	264:270	DPY19L3 is predicted to be a multipass transmembrane protein that localizes to the endoplasmic reticulum (ER); however, its structure is undetermined.
29405629	8	45	theme	important	1414:1422	arg1	insights					1424:1431	important insights	1414:1431	important insights into the mechanism of C-mannosylation	1414:1469	These novel findings on DPY19L3 provide important insights into the mechanism of C-mannosylation.
29405629	4	46	theme	experimental	502:513	arg1	introduction					568:579	introduction	568:579	introduction of N-glycosylation sites	568:604	In this study, we propose a topological structure of DPY19L3 by in silico analysis and experimental methods such as redox-sensitive luciferase assay and introduction of N-glycosylation sites, suggesting that DPY19L3 comprises 11 transmembrane regions and two re-entrant loops with the N- and C-terminal ends facing the cytoplasm and ER lumen, respectively.
29405629	4	46	theme	experimental	502:513	arg1	assay					558:562	redox-sensitive luciferase assay	531:562	redox-sensitive luciferase assay	531:562	In this study, we propose a topological structure of DPY19L3 by in silico analysis and experimental methods such as redox-sensitive luciferase assay and introduction of N-glycosylation sites, suggesting that DPY19L3 comprises 11 transmembrane regions and two re-entrant loops with the N- and C-terminal ends facing the cytoplasm and ER lumen, respectively.
29405629	4	46	theme	experimental	502:513	arg1	methods					515:521	experimental methods	502:521	experimental methods such as redox-sensitive luciferase assay and introduction of N-glycosylation sites	502:604	In this study, we propose a topological structure of DPY19L3 by in silico analysis and experimental methods such as redox-sensitive luciferase assay and introduction of N-glycosylation sites, suggesting that DPY19L3 comprises 11 transmembrane regions and two re-entrant loops with the N- and C-terminal ends facing the cytoplasm and ER lumen, respectively.
29405629	7	47	contain	have	1331:1334	arg2	roles					1340:1344	any roles	1336:1344	any roles for its enzymatic activity	1336:1371	Isoform2 does not possess C-mannosyltransferase activity, indicating the importance of the C-terminal region; however, N-glycosylations of DPY19L3 do not have any roles for its enzymatic activity.
29405629	7	47	contain	have	1331:1334	arg1	N-glycosylations					1296:1311	N-glycosylations	1296:1311	N-glycosylations of DPY19L3	1296:1322	Isoform2 does not possess C-mannosyltransferase activity, indicating the importance of the C-terminal region; however, N-glycosylations of DPY19L3 do not have any roles for its enzymatic activity.
29405629	7	48	theme	enzymatic	1354:1362	arg1	activity					1364:1371	its enzymatic activity	1350:1371	its enzymatic activity	1350:1371	Isoform2 does not possess C-mannosyltransferase activity, indicating the importance of the C-terminal region; however, N-glycosylations of DPY19L3 do not have any roles for its enzymatic activity.
29405629	4	49	theme	sites	600:604	arg1	introduction					568:579	introduction	568:579	introduction of N-glycosylation sites	568:604	In this study, we propose a topological structure of DPY19L3 by in silico analysis and experimental methods such as redox-sensitive luciferase assay and introduction of N-glycosylation sites, suggesting that DPY19L3 comprises 11 transmembrane regions and two re-entrant loops with the N- and C-terminal ends facing the cytoplasm and ER lumen, respectively.
29405629	4	49	theme	sites	600:604	arg1	assay					558:562	redox-sensitive luciferase assay	531:562	redox-sensitive luciferase assay	531:562	In this study, we propose a topological structure of DPY19L3 by in silico analysis and experimental methods such as redox-sensitive luciferase assay and introduction of N-glycosylation sites, suggesting that DPY19L3 comprises 11 transmembrane regions and two re-entrant loops with the N- and C-terminal ends facing the cytoplasm and ER lumen, respectively.
29405629	2	50	theme	human	251:255	arg1	cells					257:261	human cells	251:261	human cells	251:261	Recently, we identified DPY19L3 as a C-mannosyltransferase of R-spondin1 in human cells.
29405629	4	51	theme	C-terminal	707:716	arg1	ends					718:721	C-terminal ends	707:721	C-terminal ends facing the cytoplasm and ER lumen, respectively	707:769	In this study, we propose a topological structure of DPY19L3 by in silico analysis and experimental methods such as redox-sensitive luciferase assay and introduction of N-glycosylation sites, suggesting that DPY19L3 comprises 11 transmembrane regions and two re-entrant loops with the N- and C-terminal ends facing the cytoplasm and ER lumen, respectively.
29405629	5	52	from	Asn319	920:925	arg1	N-glycosylated					876:889	N-glycosylated	876:889	N-glycosylated	876:889	Furthermore, DPY19L3 has four predicted N-glycosylation sites, and we have demonstrated that DPY19L3 is N-glycosylated at Asn118 and Asn704 but not Asn319 and Asn439 , supporting our topological model.
29405629	4	53	theme	N-glycosylation	584:598	arg1	sites					600:604	N-glycosylation sites	584:604	N-glycosylation sites	584:604	In this study, we propose a topological structure of DPY19L3 by in silico analysis and experimental methods such as redox-sensitive luciferase assay and introduction of N-glycosylation sites, suggesting that DPY19L3 comprises 11 transmembrane regions and two re-entrant loops with the N- and C-terminal ends facing the cytoplasm and ER lumen, respectively.
29405629	6	54	theme	splice	1107:1112	arg1	DPY19L3					1083:1089	DPY19L3	1083:1089	DPY19L3	1083:1089	By mass spectrometry, we measured the C-mannosyltransferase activity of N-glycosylation-defective mutants of DPY19L3 and isoform2, a splice variant, which lacks the C-terminal luminal region of DPY19L3.
29405629	6	54	theme	splice	1107:1112	arg1	variant					1114:1120	a splice variant	1105:1120	a splice variant	1105:1120	By mass spectrometry, we measured the C-mannosyltransferase activity of N-glycosylation-defective mutants of DPY19L3 and isoform2, a splice variant, which lacks the C-terminal luminal region of DPY19L3.
29405629	7	55	theme	C-terminal	1268:1277	arg1	region					1279:1284	the C-terminal region	1264:1284	the C-terminal region	1264:1284	Isoform2 does not possess C-mannosyltransferase activity, indicating the importance of the C-terminal region; however, N-glycosylations of DPY19L3 do not have any roles for its enzymatic activity.
29405629	4	56	theme	DPY19L3	468:474	arg1	structure					455:463	a topological structure	441:463	a topological structure of DPY19L3	441:474	In this study, we propose a topological structure of DPY19L3 by in silico analysis and experimental methods such as redox-sensitive luciferase assay and introduction of N-glycosylation sites, suggesting that DPY19L3 comprises 11 transmembrane regions and two re-entrant loops with the N- and C-terminal ends facing the cytoplasm and ER lumen, respectively.
29405629	2	57	theme	R-spondin1	237:246	arg1	C-mannosyltransferase					212:232	a C-mannosyltransferase	210:232	a C-mannosyltransferase of R-spondin1 in human cells	210:261	Recently, we identified DPY19L3 as a C-mannosyltransferase of R-spondin1 in human cells.
29405629	2	57	theme	R-spondin1	237:246	arg1	DPY19L3					199:205	DPY19L3	199:205	DPY19L3	199:205	Recently, we identified DPY19L3 as a C-mannosyltransferase of R-spondin1 in human cells.
29405629	4	58	theme	re-entrant	674:683	arg1	loops					685:689	two re-entrant loops	670:689	two re-entrant loops	670:689	In this study, we propose a topological structure of DPY19L3 by in silico analysis and experimental methods such as redox-sensitive luciferase assay and introduction of N-glycosylation sites, suggesting that DPY19L3 comprises 11 transmembrane regions and two re-entrant loops with the N- and C-terminal ends facing the cytoplasm and ER lumen, respectively.
12706347	2	0	theme	membrane-associated	384:402	arg1	related					431:437	related	431:437	related	431:437	NTPDase3 is a prototypical cell membrane-associated eNTPDase, which is equally related and enzymatically intermediate to the other two cell surface membrane NTPDases (NTPDase1 and 2).
12706347	2	0	theme	membrane-associated	384:402	arg1	eNTPDase					404:411	a prototypical cell membrane-associated eNTPDase	364:411	a prototypical cell membrane-associated eNTPDase	364:411	NTPDase3 is a prototypical cell membrane-associated eNTPDase, which is equally related and enzymatically intermediate to the other two cell surface membrane NTPDases (NTPDase1 and 2).
12706347	2	0	theme	membrane-associated	384:402	arg1	NTPDase3					352:359	NTPDase3	352:359	NTPDase3	352:359	NTPDase3 is a prototypical cell membrane-associated eNTPDase, which is equally related and enzymatically intermediate to the other two cell surface membrane NTPDases (NTPDase1 and 2).
12706347	9	1	theme	membrane	1715:1722	arg1	eNTPDases					1724:1732	cell membrane eNTPDases	1710:1732	cell membrane eNTPDases	1710:1732	Since this N-glycosylation site is invariant in cell membrane eNTPDases, it is postulated that glycosylation of this residue near ACR1 is crucial for full enzymatic activity of the cell membrane NTPDases.
12706347	1	2	gly	glycosylation	184:196	arg1	diphosphohydrolases					319:337	membrane-bound ecto-nucleoside triphosphate diphosphohydrolases	275:337	membrane-bound ecto-nucleoside triphosphate diphosphohydrolases (eNTPDases)	275:349	N-linked glycosylation is important for the function, cellular localization, and oligomerization of membrane-bound ecto-nucleoside triphosphate diphosphohydrolases (eNTPDases).
12706347	1	2	gly	glycosylation	184:196	arg1	eNTPDases					340:348	eNTPDases	340:348	eNTPDases	340:348	N-linked glycosylation is important for the function, cellular localization, and oligomerization of membrane-bound ecto-nucleoside triphosphate diphosphohydrolases (eNTPDases).
12706347	3	3	theme	putative	584:591	arg1	sites					609:613	seven putative N-glycosylation sites	578:613	seven putative N-glycosylation sites located in the ecto-domain	578:640	The protein sequence of NTPDase3 contains seven putative N-glycosylation sites located in the ecto-domain.
12706347	9	4	gly	glycosylation	1757:1769	arg1	residue					1779:1785	this residue	1774:1785	this residue	1774:1785	Since this N-glycosylation site is invariant in cell membrane eNTPDases, it is postulated that glycosylation of this residue near ACR1 is crucial for full enzymatic activity of the cell membrane NTPDases.
12706347	1	5	theme	membrane-bound	275:288	arg1	diphosphohydrolases					319:337	membrane-bound ecto-nucleoside triphosphate diphosphohydrolases	275:337	membrane-bound ecto-nucleoside triphosphate diphosphohydrolases (eNTPDases)	275:349	N-linked glycosylation is important for the function, cellular localization, and oligomerization of membrane-bound ecto-nucleoside triphosphate diphosphohydrolases (eNTPDases).
12706347	1	5	theme	membrane-bound	275:288	arg1	eNTPDases					340:348	eNTPDases	340:348	eNTPDases	340:348	N-linked glycosylation is important for the function, cellular localization, and oligomerization of membrane-bound ecto-nucleoside triphosphate diphosphohydrolases (eNTPDases).
12706347	9	6	theme	NTPDases	1857:1864	arg1	activity					1827:1834	full enzymatic activity	1812:1834	full enzymatic activity of the cell membrane NTPDases	1812:1864	Since this N-glycosylation site is invariant in cell membrane eNTPDases, it is postulated that glycosylation of this residue near ACR1 is crucial for full enzymatic activity of the cell membrane NTPDases.
12706347	1	7	theme	N-linked	175:182	arg1	glycosylation					184:196	N-linked glycosylation	175:196	N-linked glycosylation	175:196	N-linked glycosylation is important for the function, cellular localization, and oligomerization of membrane-bound ecto-nucleoside triphosphate diphosphohydrolases (eNTPDases).
12706347	7	8	gly	deglycosylation	1133:1147	arg1	site					1157:1160	this site	1152:1160	this site	1152:1160	Enzymatic deglycosylation of this site is shown to be responsible for the inactivation of the wild-type enzyme by treatment with peptide N-glycosidase-F.
12706347	4	9	from	asparagine	691:700	arg1	NTPDase3					708:715	NTPDase3	708:715	NTPDase3	708:715	Only one of these putative glycosylation sites, asparagine 81 in NTPDase3, which is located near apyrase conserved region 1 (ACR1), is invariant in all the cell surface membrane eNTPDases.
12706347	4	10	theme	sites	684:688	arg1	asparagine					691:700	asparagine 81	691:703	asparagine 81 in NTPDase3, which is located near apyrase conserved region 1 (ACR1)	691:772	Only one of these putative glycosylation sites, asparagine 81 in NTPDase3, which is located near apyrase conserved region 1 (ACR1), is invariant in all the cell surface membrane eNTPDases.
12706347	4	10	theme	sites	684:688	arg1	sites					684:688	these putative glycosylation sites	655:688	these putative glycosylation sites	655:688	Only one of these putative glycosylation sites, asparagine 81 in NTPDase3, which is located near apyrase conserved region 1 (ACR1), is invariant in all the cell surface membrane eNTPDases.
12706347	4	10	theme	sites	684:688	arg1	one					648:650	one	648:650	one	648:650	Only one of these putative glycosylation sites, asparagine 81 in NTPDase3, which is located near apyrase conserved region 1 (ACR1), is invariant in all the cell surface membrane eNTPDases.
12706347	0	11	theme	full	97:100	arg1	activity					112:119	full enzymatic activity	97:119	full enzymatic activity of ecto-nucleoside triphosphate diphosphohydrolase 3	97:172	Asparagine 81, an invariant glycosylation site near apyrase conserved region 1, is essential for full enzymatic activity of ecto-nucleoside triphosphate diphosphohydrolase 3.
12706347	3	12	theme	protein	540:546	arg1	sequence					548:555	The protein sequence	536:555	The protein sequence of NTPDase3	536:567	The protein sequence of NTPDase3 contains seven putative N-glycosylation sites located in the ecto-domain.
12706347	8	13	from	site	1485:1488	arg1	lack					1455:1458	lack	1455:1458	lack of glycosylation at this site	1455:1488	In addition, glycosylation of this conserved site is necessary for the stabilization/stimulation of nucleotidase activity upon treatment with the lectin concanavalin A. However, lack of glycosylation at this site did not result in large changes in tertiary or quaternary structure, as measured by Cibacron blue binding, chemical cross-linking, and native gel electrophoretic analysis.
12706347	8	14	gly	glycosylation	1290:1302	arg1	site					1322:1325	this conserved site	1307:1325	this conserved site	1307:1325	In addition, glycosylation of this conserved site is necessary for the stabilization/stimulation of nucleotidase activity upon treatment with the lectin concanavalin A. However, lack of glycosylation at this site did not result in large changes in tertiary or quaternary structure, as measured by Cibacron blue binding, chemical cross-linking, and native gel electrophoretic analysis.
12706347	9	15	from	eNTPDases	1724:1732	arg1	invariant					1697:1705	invariant	1697:1705	invariant	1697:1705	Since this N-glycosylation site is invariant in cell membrane eNTPDases, it is postulated that glycosylation of this residue near ACR1 is crucial for full enzymatic activity of the cell membrane NTPDases.
12706347	9	16	theme	residue	1779:1785	arg1	glycosylation					1757:1769	glycosylation	1757:1769	glycosylation of this residue near ACR1	1757:1795	Since this N-glycosylation site is invariant in cell membrane eNTPDases, it is postulated that glycosylation of this residue near ACR1 is crucial for full enzymatic activity of the cell membrane NTPDases.
12706347	8	17	theme	large	1508:1512	arg1	changes					1514:1520	large changes	1508:1520	large changes in tertiary or quaternary structure	1508:1556	In addition, glycosylation of this conserved site is necessary for the stabilization/stimulation of nucleotidase activity upon treatment with the lectin concanavalin A. However, lack of glycosylation at this site did not result in large changes in tertiary or quaternary structure, as measured by Cibacron blue binding, chemical cross-linking, and native gel electrophoretic analysis.
12706347	7	18	with	treatment	1237:1245	arg1	peptide					1252:1258	peptide N-glycosidase-F	1252:1274	peptide N-glycosidase-F	1252:1274	Enzymatic deglycosylation of this site is shown to be responsible for the inactivation of the wild-type enzyme by treatment with peptide N-glycosidase-F.
12706347	4	19	theme	conserved	748:756	arg1	region					758:763	apyrase conserved region 1	740:765	apyrase conserved region 1 (ACR1)	740:772	Only one of these putative glycosylation sites, asparagine 81 in NTPDase3, which is located near apyrase conserved region 1 (ACR1), is invariant in all the cell surface membrane eNTPDases.
12706347	4	19	theme	conserved	748:756	arg1	ACR1					768:771	ACR1	768:771	ACR1	768:771	Only one of these putative glycosylation sites, asparagine 81 in NTPDase3, which is located near apyrase conserved region 1 (ACR1), is invariant in all the cell surface membrane eNTPDases.
12706347	0	20	theme	ecto-nucleoside	124:138	arg1	diphosphohydrolase					153:170	ecto-nucleoside triphosphate diphosphohydrolase 3	124:172	ecto-nucleoside triphosphate diphosphohydrolase 3	124:172	Asparagine 81, an invariant glycosylation site near apyrase conserved region 1, is essential for full enzymatic activity of ecto-nucleoside triphosphate diphosphohydrolase 3.
12706347	4	21	from	eNTPDases	821:829	arg1	invariant					778:786	invariant	778:786	invariant	778:786	Only one of these putative glycosylation sites, asparagine 81 in NTPDase3, which is located near apyrase conserved region 1 (ACR1), is invariant in all the cell surface membrane eNTPDases.
12706347	8	22	theme	nucleotidase	1377:1388	arg1	activity					1390:1397	nucleotidase activity	1377:1397	nucleotidase activity	1377:1397	In addition, glycosylation of this conserved site is necessary for the stabilization/stimulation of nucleotidase activity upon treatment with the lectin concanavalin A. However, lack of glycosylation at this site did not result in large changes in tertiary or quaternary structure, as measured by Cibacron blue binding, chemical cross-linking, and native gel electrophoretic analysis.
12706347	0	23	theme	apyrase	52:58	arg1	region					70:75	apyrase conserved region 1	52:77	apyrase conserved region 1	52:77	Asparagine 81, an invariant glycosylation site near apyrase conserved region 1, is essential for full enzymatic activity of ecto-nucleoside triphosphate diphosphohydrolase 3.
12706347	5	24	theme	conserved	915:923	arg1	site					941:944	this highly conserved N-glycosylation site	903:944	this highly conserved N-glycosylation site in NTPDase3	903:956	Using site-directed mutagenesis, mutants were constructed to eliminate this highly conserved N-glycosylation site in NTPDase3.
12706347	9	25	theme	full	1812:1815	arg1	activity					1827:1834	full enzymatic activity	1812:1834	full enzymatic activity of the cell membrane NTPDases	1812:1864	Since this N-glycosylation site is invariant in cell membrane eNTPDases, it is postulated that glycosylation of this residue near ACR1 is crucial for full enzymatic activity of the cell membrane NTPDases.
12706347	0	26	theme	diphosphohydrolase	153:170	arg1	activity					112:119	full enzymatic activity	97:119	full enzymatic activity of ecto-nucleoside triphosphate diphosphohydrolase 3	97:172	Asparagine 81, an invariant glycosylation site near apyrase conserved region 1, is essential for full enzymatic activity of ecto-nucleoside triphosphate diphosphohydrolase 3.
12706347	6	27	theme	full	1033:1036	arg1	activity					1048:1055	full enzymatic activity	1033:1055	full enzymatic activity	1033:1055	The results indicate that glycosylation at this position is essential for full enzymatic activity, with mutant ATPase activity decreased more than ADPase activity.
12706347	4	28	from	invariant	778:786	arg1	eNTPDases					821:829	all the cell surface membrane eNTPDases	791:829	all the cell surface membrane eNTPDases	791:829	Only one of these putative glycosylation sites, asparagine 81 in NTPDase3, which is located near apyrase conserved region 1 (ACR1), is invariant in all the cell surface membrane eNTPDases.
12706347	8	29	theme	lectin	1423:1428	arg1	concanavalin					1430:1441	the lectin concanavalin	1419:1441	the lectin concanavalin	1419:1441	In addition, glycosylation of this conserved site is necessary for the stabilization/stimulation of nucleotidase activity upon treatment with the lectin concanavalin A. However, lack of glycosylation at this site did not result in large changes in tertiary or quaternary structure, as measured by Cibacron blue binding, chemical cross-linking, and native gel electrophoretic analysis.
12706347	2	30	theme	surface	492:498	arg1	NTPDases					509:516	the other two cell surface membrane NTPDases	473:516	the other two cell surface membrane NTPDases (NTPDase1 and 2)	473:533	NTPDase3 is a prototypical cell membrane-associated eNTPDase, which is equally related and enzymatically intermediate to the other two cell surface membrane NTPDases (NTPDase1 and 2).
12706347	8	31	theme	blue	1583:1586	arg1	binding					1588:1594	Cibacron blue binding	1574:1594	Cibacron blue binding	1574:1594	In addition, glycosylation of this conserved site is necessary for the stabilization/stimulation of nucleotidase activity upon treatment with the lectin concanavalin A. However, lack of glycosylation at this site did not result in large changes in tertiary or quaternary structure, as measured by Cibacron blue binding, chemical cross-linking, and native gel electrophoretic analysis.
12706347	0	32	theme	conserved	60:68	arg1	region					70:75	apyrase conserved region 1	52:77	apyrase conserved region 1	52:77	Asparagine 81, an invariant glycosylation site near apyrase conserved region 1, is essential for full enzymatic activity of ecto-nucleoside triphosphate diphosphohydrolase 3.
12706347	7	33	theme	wild-type	1217:1225	arg1	enzyme					1227:1232	the wild-type enzyme	1213:1232	the wild-type enzyme	1213:1232	Enzymatic deglycosylation of this site is shown to be responsible for the inactivation of the wild-type enzyme by treatment with peptide N-glycosidase-F.
12706347	1	34	theme	ecto-nucleoside	290:304	arg1	diphosphohydrolases					319:337	membrane-bound ecto-nucleoside triphosphate diphosphohydrolases	275:337	membrane-bound ecto-nucleoside triphosphate diphosphohydrolases (eNTPDases)	275:349	N-linked glycosylation is important for the function, cellular localization, and oligomerization of membrane-bound ecto-nucleoside triphosphate diphosphohydrolases (eNTPDases).
12706347	1	34	theme	ecto-nucleoside	290:304	arg1	eNTPDases					340:348	eNTPDases	340:348	eNTPDases	340:348	N-linked glycosylation is important for the function, cellular localization, and oligomerization of membrane-bound ecto-nucleoside triphosphate diphosphohydrolases (eNTPDases).
12706347	3	35	from	ecto-domain	630:640	arg1	located					615:621	located	615:621	located	615:621	The protein sequence of NTPDase3 contains seven putative N-glycosylation sites located in the ecto-domain.
12706347	5	36	theme	site-directed	838:850	arg1	mutagenesis					852:862	site-directed mutagenesis	838:862	site-directed mutagenesis	838:862	Using site-directed mutagenesis, mutants were constructed to eliminate this highly conserved N-glycosylation site in NTPDase3.
12706347	1	37	theme	diphosphohydrolases	319:337	arg1	localization					238:249	cellular localization	229:249	cellular localization	229:249	N-linked glycosylation is important for the function, cellular localization, and oligomerization of membrane-bound ecto-nucleoside triphosphate diphosphohydrolases (eNTPDases).
12706347	1	37	theme	diphosphohydrolases	319:337	arg1	oligomerization					256:270	oligomerization	256:270	oligomerization	256:270	N-linked glycosylation is important for the function, cellular localization, and oligomerization of membrane-bound ecto-nucleoside triphosphate diphosphohydrolases (eNTPDases).
12706347	1	37	theme	diphosphohydrolases	319:337	arg1	function					219:226	function	219:226	function	219:226	N-linked glycosylation is important for the function, cellular localization, and oligomerization of membrane-bound ecto-nucleoside triphosphate diphosphohydrolases (eNTPDases).
12706347	0	38	theme	invariant	18:26	arg1	Asparagine					0:9	Asparagine 81	0:12	Asparagine 81	0:12	Asparagine 81, an invariant glycosylation site near apyrase conserved region 1, is essential for full enzymatic activity of ecto-nucleoside triphosphate diphosphohydrolase 3.
12706347	0	38	theme	invariant	18:26	arg1	site					42:45	an invariant glycosylation site	15:45	an invariant glycosylation site near apyrase conserved region 1	15:77	Asparagine 81, an invariant glycosylation site near apyrase conserved region 1, is essential for full enzymatic activity of ecto-nucleoside triphosphate diphosphohydrolase 3.
12706347	6	39	theme	ATPase	1070:1075	arg1	activity					1077:1084	mutant ATPase activity	1063:1084	mutant ATPase activity	1063:1084	The results indicate that glycosylation at this position is essential for full enzymatic activity, with mutant ATPase activity decreased more than ADPase activity.
12706347	8	40	theme	native	1625:1630	arg1	analysis					1652:1659	native gel electrophoretic analysis	1625:1659	native gel electrophoretic analysis	1625:1659	In addition, glycosylation of this conserved site is necessary for the stabilization/stimulation of nucleotidase activity upon treatment with the lectin concanavalin A. However, lack of glycosylation at this site did not result in large changes in tertiary or quaternary structure, as measured by Cibacron blue binding, chemical cross-linking, and native gel electrophoretic analysis.
12706347	2	41	theme	cell	379:382	arg1	related					431:437	related	431:437	related	431:437	NTPDase3 is a prototypical cell membrane-associated eNTPDase, which is equally related and enzymatically intermediate to the other two cell surface membrane NTPDases (NTPDase1 and 2).
12706347	2	41	theme	cell	379:382	arg1	eNTPDase					404:411	a prototypical cell membrane-associated eNTPDase	364:411	a prototypical cell membrane-associated eNTPDase	364:411	NTPDase3 is a prototypical cell membrane-associated eNTPDase, which is equally related and enzymatically intermediate to the other two cell surface membrane NTPDases (NTPDase1 and 2).
12706347	2	41	theme	cell	379:382	arg1	NTPDase3					352:359	NTPDase3	352:359	NTPDase3	352:359	NTPDase3 is a prototypical cell membrane-associated eNTPDase, which is equally related and enzymatically intermediate to the other two cell surface membrane NTPDases (NTPDase1 and 2).
12706347	8	42	theme	gel	1632:1634	arg1	analysis					1652:1659	native gel electrophoretic analysis	1625:1659	native gel electrophoretic analysis	1625:1659	In addition, glycosylation of this conserved site is necessary for the stabilization/stimulation of nucleotidase activity upon treatment with the lectin concanavalin A. However, lack of glycosylation at this site did not result in large changes in tertiary or quaternary structure, as measured by Cibacron blue binding, chemical cross-linking, and native gel electrophoretic analysis.
12706347	4	43	theme	cell	799:802	arg1	eNTPDases					821:829	all the cell surface membrane eNTPDases	791:829	all the cell surface membrane eNTPDases	791:829	Only one of these putative glycosylation sites, asparagine 81 in NTPDase3, which is located near apyrase conserved region 1 (ACR1), is invariant in all the cell surface membrane eNTPDases.
12706347	0	44	gly	glycosylation	28:40	arg2	Asparagine					0:9	Asparagine 81	0:12	Asparagine 81	0:12	Asparagine 81, an invariant glycosylation site near apyrase conserved region 1, is essential for full enzymatic activity of ecto-nucleoside triphosphate diphosphohydrolase 3.
12706347	0	44	gly	glycosylation	28:40	arg2	site					42:45	an invariant glycosylation site	15:45	an invariant glycosylation site near apyrase conserved region 1	15:77	Asparagine 81, an invariant glycosylation site near apyrase conserved region 1, is essential for full enzymatic activity of ecto-nucleoside triphosphate diphosphohydrolase 3.
12706347	4	45	theme	membrane	812:819	arg1	eNTPDases					821:829	all the cell surface membrane eNTPDases	791:829	all the cell surface membrane eNTPDases	791:829	Only one of these putative glycosylation sites, asparagine 81 in NTPDase3, which is located near apyrase conserved region 1 (ACR1), is invariant in all the cell surface membrane eNTPDases.
12706347	8	46	dep	necessary	1330:1338	arg1	A.					1443:1444	A.	1443:1444	A.	1443:1444	In addition, glycosylation of this conserved site is necessary for the stabilization/stimulation of nucleotidase activity upon treatment with the lectin concanavalin A. However, lack of glycosylation at this site did not result in large changes in tertiary or quaternary structure, as measured by Cibacron blue binding, chemical cross-linking, and native gel electrophoretic analysis.
12706347	9	47	theme	cell	1710:1713	arg1	eNTPDases					1724:1732	cell membrane eNTPDases	1710:1732	cell membrane eNTPDases	1710:1732	Since this N-glycosylation site is invariant in cell membrane eNTPDases, it is postulated that glycosylation of this residue near ACR1 is crucial for full enzymatic activity of the cell membrane NTPDases.
12706347	9	48	gly	N-glycosylation	1673:1687	arg2	site					1689:1692	this N-glycosylation site	1668:1692	this N-glycosylation site	1668:1692	Since this N-glycosylation site is invariant in cell membrane eNTPDases, it is postulated that glycosylation of this residue near ACR1 is crucial for full enzymatic activity of the cell membrane NTPDases.
12706347	7	49	theme	site	1157:1160	arg1	deglycosylation					1133:1147	Enzymatic deglycosylation	1123:1147	Enzymatic deglycosylation of this site	1123:1160	Enzymatic deglycosylation of this site is shown to be responsible for the inactivation of the wild-type enzyme by treatment with peptide N-glycosidase-F.
12706347	6	50	gly	glycosylation	985:997	arg2	position					1007:1014	this position	1002:1014	this position	1002:1014	The results indicate that glycosylation at this position is essential for full enzymatic activity, with mutant ATPase activity decreased more than ADPase activity.
12706347	6	50	gly	glycosylation	985:997	arg1	position					1007:1014	this position	1002:1014	this position	1002:1014	The results indicate that glycosylation at this position is essential for full enzymatic activity, with mutant ATPase activity decreased more than ADPase activity.
12706347	4	51	gly	glycosylation	670:682	arg2	sites					684:688	these putative glycosylation sites	655:688	these putative glycosylation sites	655:688	Only one of these putative glycosylation sites, asparagine 81 in NTPDase3, which is located near apyrase conserved region 1 (ACR1), is invariant in all the cell surface membrane eNTPDases.
12706347	3	52	theme	NTPDase3	560:567	arg1	sequence					548:555	The protein sequence	536:555	The protein sequence of NTPDase3	536:567	The protein sequence of NTPDase3 contains seven putative N-glycosylation sites located in the ecto-domain.
12706347	7	53	theme	Enzymatic	1123:1131	arg1	deglycosylation					1133:1147	Enzymatic deglycosylation	1123:1147	Enzymatic deglycosylation of this site	1123:1160	Enzymatic deglycosylation of this site is shown to be responsible for the inactivation of the wild-type enzyme by treatment with peptide N-glycosidase-F.
12706347	3	54	theme	located	615:621	arg1	sites					609:613	seven putative N-glycosylation sites	578:613	seven putative N-glycosylation sites located in the ecto-domain	578:640	The protein sequence of NTPDase3 contains seven putative N-glycosylation sites located in the ecto-domain.
12706347	0	55	theme	enzymatic	102:110	arg1	activity					112:119	full enzymatic activity	97:119	full enzymatic activity of ecto-nucleoside triphosphate diphosphohydrolase 3	97:172	Asparagine 81, an invariant glycosylation site near apyrase conserved region 1, is essential for full enzymatic activity of ecto-nucleoside triphosphate diphosphohydrolase 3.
12706347	3	56	theme	N-glycosylation	593:607	arg1	sites					609:613	seven putative N-glycosylation sites	578:613	seven putative N-glycosylation sites located in the ecto-domain	578:640	The protein sequence of NTPDase3 contains seven putative N-glycosylation sites located in the ecto-domain.
12706347	4	57	theme	glycosylation	670:682	arg1	sites					684:688	these putative glycosylation sites	655:688	these putative glycosylation sites	655:688	Only one of these putative glycosylation sites, asparagine 81 in NTPDase3, which is located near apyrase conserved region 1 (ACR1), is invariant in all the cell surface membrane eNTPDases.
12706347	8	58	theme	site	1322:1325	arg1	glycosylation					1290:1302	glycosylation	1290:1302	glycosylation of this conserved site	1290:1325	In addition, glycosylation of this conserved site is necessary for the stabilization/stimulation of nucleotidase activity upon treatment with the lectin concanavalin A. However, lack of glycosylation at this site did not result in large changes in tertiary or quaternary structure, as measured by Cibacron blue binding, chemical cross-linking, and native gel electrophoretic analysis.
12706347	0	59	theme	triphosphate	140:151	arg1	diphosphohydrolase					153:170	ecto-nucleoside triphosphate diphosphohydrolase 3	124:172	ecto-nucleoside triphosphate diphosphohydrolase 3	124:172	Asparagine 81, an invariant glycosylation site near apyrase conserved region 1, is essential for full enzymatic activity of ecto-nucleoside triphosphate diphosphohydrolase 3.
12706347	8	60	theme	tertiary	1525:1532	arg1	structure					1548:1556	tertiary or quaternary structure	1525:1556	tertiary or quaternary structure	1525:1556	In addition, glycosylation of this conserved site is necessary for the stabilization/stimulation of nucleotidase activity upon treatment with the lectin concanavalin A. However, lack of glycosylation at this site did not result in large changes in tertiary or quaternary structure, as measured by Cibacron blue binding, chemical cross-linking, and native gel electrophoretic analysis.
12706347	4	61	theme	apyrase	740:746	arg1	region					758:763	apyrase conserved region 1	740:765	apyrase conserved region 1 (ACR1)	740:772	Only one of these putative glycosylation sites, asparagine 81 in NTPDase3, which is located near apyrase conserved region 1 (ACR1), is invariant in all the cell surface membrane eNTPDases.
12706347	4	61	theme	apyrase	740:746	arg1	ACR1					768:771	ACR1	768:771	ACR1	768:771	Only one of these putative glycosylation sites, asparagine 81 in NTPDase3, which is located near apyrase conserved region 1 (ACR1), is invariant in all the cell surface membrane eNTPDases.
12706347	8	62	from	addition	1280:1287	arg1	necessary					1330:1338	necessary	1330:1338	necessary	1330:1338	In addition, glycosylation of this conserved site is necessary for the stabilization/stimulation of nucleotidase activity upon treatment with the lectin concanavalin A. However, lack of glycosylation at this site did not result in large changes in tertiary or quaternary structure, as measured by Cibacron blue binding, chemical cross-linking, and native gel electrophoretic analysis.
12706347	6	63	theme	mutant	1063:1068	arg1	activity					1077:1084	mutant ATPase activity	1063:1084	mutant ATPase activity	1063:1084	The results indicate that glycosylation at this position is essential for full enzymatic activity, with mutant ATPase activity decreased more than ADPase activity.
12706347	5	64	gly	N-glycosylation	925:939	arg2	site					941:944	this highly conserved N-glycosylation site	903:944	this highly conserved N-glycosylation site in NTPDase3	903:956	Using site-directed mutagenesis, mutants were constructed to eliminate this highly conserved N-glycosylation site in NTPDase3.
12706347	8	65	theme	quaternary	1537:1546	arg1	structure					1548:1556	tertiary or quaternary structure	1525:1556	tertiary or quaternary structure	1525:1556	In addition, glycosylation of this conserved site is necessary for the stabilization/stimulation of nucleotidase activity upon treatment with the lectin concanavalin A. However, lack of glycosylation at this site did not result in large changes in tertiary or quaternary structure, as measured by Cibacron blue binding, chemical cross-linking, and native gel electrophoretic analysis.
12706347	3	66	gly	N-glycosylation	593:607	arg2	sites					609:613	seven putative N-glycosylation sites	578:613	seven putative N-glycosylation sites located in the ecto-domain	578:640	The protein sequence of NTPDase3 contains seven putative N-glycosylation sites located in the ecto-domain.
12706347	3	66	gly	N-glycosylation	593:607	arg2	seven					578:582	seven	578:582	seven	578:582	The protein sequence of NTPDase3 contains seven putative N-glycosylation sites located in the ecto-domain.
12706347	3	67	from	located	615:621	arg1	ecto-domain					630:640	the ecto-domain	626:640	the ecto-domain	626:640	The protein sequence of NTPDase3 contains seven putative N-glycosylation sites located in the ecto-domain.
12706347	8	68	from	changes	1514:1520	arg1	structure					1548:1556	tertiary or quaternary structure	1525:1556	tertiary or quaternary structure	1525:1556	In addition, glycosylation of this conserved site is necessary for the stabilization/stimulation of nucleotidase activity upon treatment with the lectin concanavalin A. However, lack of glycosylation at this site did not result in large changes in tertiary or quaternary structure, as measured by Cibacron blue binding, chemical cross-linking, and native gel electrophoretic analysis.
12706347	8	69	theme	conserved	1312:1320	arg1	site					1322:1325	this conserved site	1307:1325	this conserved site	1307:1325	In addition, glycosylation of this conserved site is necessary for the stabilization/stimulation of nucleotidase activity upon treatment with the lectin concanavalin A. However, lack of glycosylation at this site did not result in large changes in tertiary or quaternary structure, as measured by Cibacron blue binding, chemical cross-linking, and native gel electrophoretic analysis.
12706347	8	70	with	treatment	1404:1412	arg1	concanavalin					1430:1441	the lectin concanavalin	1419:1441	the lectin concanavalin	1419:1441	In addition, glycosylation of this conserved site is necessary for the stabilization/stimulation of nucleotidase activity upon treatment with the lectin concanavalin A. However, lack of glycosylation at this site did not result in large changes in tertiary or quaternary structure, as measured by Cibacron blue binding, chemical cross-linking, and native gel electrophoretic analysis.
12706347	2	71	dep	NTPDases	509:516	arg1	2					532:532	2	532:532	2	532:532	NTPDase3 is a prototypical cell membrane-associated eNTPDase, which is equally related and enzymatically intermediate to the other two cell surface membrane NTPDases (NTPDase1 and 2).
12706347	2	71	dep	NTPDases	509:516	arg1	NTPDase1					519:526	NTPDase1	519:526	NTPDase1	519:526	NTPDase3 is a prototypical cell membrane-associated eNTPDase, which is equally related and enzymatically intermediate to the other two cell surface membrane NTPDases (NTPDase1 and 2).
12706347	5	72	theme	N-glycosylation	925:939	arg1	site					941:944	this highly conserved N-glycosylation site	903:944	this highly conserved N-glycosylation site in NTPDase3	903:956	Using site-directed mutagenesis, mutants were constructed to eliminate this highly conserved N-glycosylation site in NTPDase3.
12706347	6	73	theme	enzymatic	1038:1046	arg1	activity					1048:1055	full enzymatic activity	1033:1055	full enzymatic activity	1033:1055	The results indicate that glycosylation at this position is essential for full enzymatic activity, with mutant ATPase activity decreased more than ADPase activity.
12706347	9	74	theme	enzymatic	1817:1825	arg1	activity					1827:1834	full enzymatic activity	1812:1834	full enzymatic activity of the cell membrane NTPDases	1812:1864	Since this N-glycosylation site is invariant in cell membrane eNTPDases, it is postulated that glycosylation of this residue near ACR1 is crucial for full enzymatic activity of the cell membrane NTPDases.
12706347	8	75	theme	activity	1390:1397	arg1	stabilization/stimulation					1348:1372	the stabilization/stimulation	1344:1372	the stabilization/stimulation of nucleotidase activity upon treatment with the lectin concanavalin	1344:1441	In addition, glycosylation of this conserved site is necessary for the stabilization/stimulation of nucleotidase activity upon treatment with the lectin concanavalin A. However, lack of glycosylation at this site did not result in large changes in tertiary or quaternary structure, as measured by Cibacron blue binding, chemical cross-linking, and native gel electrophoretic analysis.
12706347	5	76	from	site	941:944	arg1	NTPDase3					949:956	NTPDase3	949:956	NTPDase3	949:956	Using site-directed mutagenesis, mutants were constructed to eliminate this highly conserved N-glycosylation site in NTPDase3.
12706347	8	77	theme	Cibacron	1574:1581	arg1	binding					1588:1594	Cibacron blue binding	1574:1594	Cibacron blue binding	1574:1594	In addition, glycosylation of this conserved site is necessary for the stabilization/stimulation of nucleotidase activity upon treatment with the lectin concanavalin A. However, lack of glycosylation at this site did not result in large changes in tertiary or quaternary structure, as measured by Cibacron blue binding, chemical cross-linking, and native gel electrophoretic analysis.
12706347	7	78	theme	enzyme	1227:1232	arg1	inactivation					1197:1208	the inactivation	1193:1208	the inactivation of the wild-type enzyme by treatment with peptide N-glycosidase-F	1193:1274	Enzymatic deglycosylation of this site is shown to be responsible for the inactivation of the wild-type enzyme by treatment with peptide N-glycosidase-F.
12706347	8	79	from	necessary	1330:1338	arg1	addition					1280:1287	addition	1280:1287	addition	1280:1287	In addition, glycosylation of this conserved site is necessary for the stabilization/stimulation of nucleotidase activity upon treatment with the lectin concanavalin A. However, lack of glycosylation at this site did not result in large changes in tertiary or quaternary structure, as measured by Cibacron blue binding, chemical cross-linking, and native gel electrophoretic analysis.
12706347	9	80	from	invariant	1697:1705	arg1	eNTPDases					1724:1732	cell membrane eNTPDases	1710:1732	cell membrane eNTPDases	1710:1732	Since this N-glycosylation site is invariant in cell membrane eNTPDases, it is postulated that glycosylation of this residue near ACR1 is crucial for full enzymatic activity of the cell membrane NTPDases.
12706347	9	81	theme	cell	1843:1846	arg1	NTPDases					1857:1864	the cell membrane NTPDases	1839:1864	the cell membrane NTPDases	1839:1864	Since this N-glycosylation site is invariant in cell membrane eNTPDases, it is postulated that glycosylation of this residue near ACR1 is crucial for full enzymatic activity of the cell membrane NTPDases.
12706347	6	82	theme	ADPase	1106:1111	arg1	activity					1113:1120	ADPase activity	1106:1120	ADPase activity	1106:1120	The results indicate that glycosylation at this position is essential for full enzymatic activity, with mutant ATPase activity decreased more than ADPase activity.
12706347	2	83	theme	cell	487:490	arg1	NTPDases					509:516	the other two cell surface membrane NTPDases	473:516	the other two cell surface membrane NTPDases (NTPDase1 and 2)	473:533	NTPDase3 is a prototypical cell membrane-associated eNTPDase, which is equally related and enzymatically intermediate to the other two cell surface membrane NTPDases (NTPDase1 and 2).
12706347	8	84	theme	chemical	1597:1604	arg1	cross-linking					1606:1618	chemical cross-linking	1597:1618	chemical cross-linking	1597:1618	In addition, glycosylation of this conserved site is necessary for the stabilization/stimulation of nucleotidase activity upon treatment with the lectin concanavalin A. However, lack of glycosylation at this site did not result in large changes in tertiary or quaternary structure, as measured by Cibacron blue binding, chemical cross-linking, and native gel electrophoretic analysis.
12706347	1	85	link	N-linked	175:182	arg1	glycosylation					184:196	N-linked glycosylation	175:196	N-linked glycosylation	175:196	N-linked glycosylation is important for the function, cellular localization, and oligomerization of membrane-bound ecto-nucleoside triphosphate diphosphohydrolases (eNTPDases).
12706347	1	86	theme	triphosphate	306:317	arg1	diphosphohydrolases					319:337	membrane-bound ecto-nucleoside triphosphate diphosphohydrolases	275:337	membrane-bound ecto-nucleoside triphosphate diphosphohydrolases (eNTPDases)	275:349	N-linked glycosylation is important for the function, cellular localization, and oligomerization of membrane-bound ecto-nucleoside triphosphate diphosphohydrolases (eNTPDases).
12706347	1	86	theme	triphosphate	306:317	arg1	eNTPDases					340:348	eNTPDases	340:348	eNTPDases	340:348	N-linked glycosylation is important for the function, cellular localization, and oligomerization of membrane-bound ecto-nucleoside triphosphate diphosphohydrolases (eNTPDases).
12706347	2	87	theme	other	477:481	arg1	NTPDases					509:516	the other two cell surface membrane NTPDases	473:516	the other two cell surface membrane NTPDases (NTPDase1 and 2)	473:533	NTPDase3 is a prototypical cell membrane-associated eNTPDase, which is equally related and enzymatically intermediate to the other two cell surface membrane NTPDases (NTPDase1 and 2).
12706347	0	88	theme	glycosylation	28:40	arg1	Asparagine					0:9	Asparagine 81	0:12	Asparagine 81	0:12	Asparagine 81, an invariant glycosylation site near apyrase conserved region 1, is essential for full enzymatic activity of ecto-nucleoside triphosphate diphosphohydrolase 3.
12706347	0	88	theme	glycosylation	28:40	arg1	site					42:45	an invariant glycosylation site	15:45	an invariant glycosylation site near apyrase conserved region 1	15:77	Asparagine 81, an invariant glycosylation site near apyrase conserved region 1, is essential for full enzymatic activity of ecto-nucleoside triphosphate diphosphohydrolase 3.
12706347	3	89	contain	contains	569:576	arg2	sites					609:613	seven putative N-glycosylation sites	578:613	seven putative N-glycosylation sites located in the ecto-domain	578:640	The protein sequence of NTPDase3 contains seven putative N-glycosylation sites located in the ecto-domain.
12706347	3	89	contain	contains	569:576	arg1	sequence					548:555	The protein sequence	536:555	The protein sequence of NTPDase3	536:567	The protein sequence of NTPDase3 contains seven putative N-glycosylation sites located in the ecto-domain.
12706347	6	90	from	position	1007:1014	arg1	glycosylation					985:997	glycosylation	985:997	glycosylation at this position	985:1014	The results indicate that glycosylation at this position is essential for full enzymatic activity, with mutant ATPase activity decreased more than ADPase activity.
12706347	2	91	theme	membrane	500:507	arg1	NTPDases					509:516	the other two cell surface membrane NTPDases	473:516	the other two cell surface membrane NTPDases (NTPDase1 and 2)	473:533	NTPDase3 is a prototypical cell membrane-associated eNTPDase, which is equally related and enzymatically intermediate to the other two cell surface membrane NTPDases (NTPDase1 and 2).
12706347	8	92	theme	electrophoretic	1636:1650	arg1	analysis					1652:1659	native gel electrophoretic analysis	1625:1659	native gel electrophoretic analysis	1625:1659	In addition, glycosylation of this conserved site is necessary for the stabilization/stimulation of nucleotidase activity upon treatment with the lectin concanavalin A. However, lack of glycosylation at this site did not result in large changes in tertiary or quaternary structure, as measured by Cibacron blue binding, chemical cross-linking, and native gel electrophoretic analysis.
12706347	8	93	theme	glycosylation	1463:1475	arg1	lack					1455:1458	lack	1455:1458	lack of glycosylation at this site	1455:1488	In addition, glycosylation of this conserved site is necessary for the stabilization/stimulation of nucleotidase activity upon treatment with the lectin concanavalin A. However, lack of glycosylation at this site did not result in large changes in tertiary or quaternary structure, as measured by Cibacron blue binding, chemical cross-linking, and native gel electrophoretic analysis.
12706347	2	94	theme	prototypical	366:377	arg1	related					431:437	related	431:437	related	431:437	NTPDase3 is a prototypical cell membrane-associated eNTPDase, which is equally related and enzymatically intermediate to the other two cell surface membrane NTPDases (NTPDase1 and 2).
12706347	2	94	theme	prototypical	366:377	arg1	eNTPDase					404:411	a prototypical cell membrane-associated eNTPDase	364:411	a prototypical cell membrane-associated eNTPDase	364:411	NTPDase3 is a prototypical cell membrane-associated eNTPDase, which is equally related and enzymatically intermediate to the other two cell surface membrane NTPDases (NTPDase1 and 2).
12706347	2	94	theme	prototypical	366:377	arg1	NTPDase3					352:359	NTPDase3	352:359	NTPDase3	352:359	NTPDase3 is a prototypical cell membrane-associated eNTPDase, which is equally related and enzymatically intermediate to the other two cell surface membrane NTPDases (NTPDase1 and 2).
12706347	9	95	theme	N-glycosylation	1673:1687	arg1	site					1689:1692	this N-glycosylation site	1668:1692	this N-glycosylation site	1668:1692	Since this N-glycosylation site is invariant in cell membrane eNTPDases, it is postulated that glycosylation of this residue near ACR1 is crucial for full enzymatic activity of the cell membrane NTPDases.
12706347	1	96	dep	function	219:226	arg1	the					215:217	the	215:217	the	215:217	N-linked glycosylation is important for the function, cellular localization, and oligomerization of membrane-bound ecto-nucleoside triphosphate diphosphohydrolases (eNTPDases).
12706347	1	97	theme	cellular	229:236	arg1	localization					238:249	cellular localization	229:249	cellular localization	229:249	N-linked glycosylation is important for the function, cellular localization, and oligomerization of membrane-bound ecto-nucleoside triphosphate diphosphohydrolases (eNTPDases).
12706347	4	98	theme	putative	661:668	arg1	sites					684:688	these putative glycosylation sites	655:688	these putative glycosylation sites	655:688	Only one of these putative glycosylation sites, asparagine 81 in NTPDase3, which is located near apyrase conserved region 1 (ACR1), is invariant in all the cell surface membrane eNTPDases.
12706347	4	99	theme	surface	804:810	arg1	eNTPDases					821:829	all the cell surface membrane eNTPDases	791:829	all the cell surface membrane eNTPDases	791:829	Only one of these putative glycosylation sites, asparagine 81 in NTPDase3, which is located near apyrase conserved region 1 (ACR1), is invariant in all the cell surface membrane eNTPDases.
12706347	9	100	theme	membrane	1848:1855	arg1	NTPDases					1857:1864	the cell membrane NTPDases	1839:1864	the cell membrane NTPDases	1839:1864	Since this N-glycosylation site is invariant in cell membrane eNTPDases, it is postulated that glycosylation of this residue near ACR1 is crucial for full enzymatic activity of the cell membrane NTPDases.
17980170	2	0	gly	glycosylated	356:367	arg1	NAAA					348:351	NAAA	348:351	NAAA	348:351	Previously, we suggested that NAAA is glycosylated and proteolytically cleaved.
17980170	8	1	theme	p-chloromercuribenzoic	1071:1092	arg1	acid					1094:1097	p-chloromercuribenzoic acid	1071:1097	p-chloromercuribenzoic acid	1071:1097	However, the cleavage did not proceed at pH 7.4 or in the presence of p-chloromercuribenzoic acid.
17980170	9	2	theme	mutant	1104:1109	arg1	resistant					1121:1129	resistant	1121:1129	resistant	1121:1129	The mutant C126S was resistant to the cleavage and remained inactive.
17980170	9	2	theme	mutant	1104:1109	arg1	C126S					1111:1115	The mutant C126S	1100:1115	The mutant C126S	1100:1115	The mutant C126S was resistant to the cleavage and remained inactive.
17980170	0	3	theme	lysosomal	91:99	arg1	enzyme					101:106	a lysosomal enzyme	89:106	a lysosomal enzyme involved in the endocannabinoid metabolism	89:149	Proteolytic activation and glycosylation of N-acylethanolamine-hydrolyzing acid amidase, a lysosomal enzyme involved in the endocannabinoid metabolism.
17980170	0	3	theme	lysosomal	91:99	arg1	activation					12:21	activation	12:21	activation	12:21	Proteolytic activation and glycosylation of N-acylethanolamine-hydrolyzing acid amidase, a lysosomal enzyme involved in the endocannabinoid metabolism.
17980170	4	4	with	blotting	540:547	arg1	antibody					564:571	anti-NAAA antibody	554:571	anti-NAAA antibody	554:571	Western blotting with anti-NAAA antibody revealed that most of NAAA in the cell homogenate was the cleaved 30-kDa form.
17980170	4	5	theme	30-kDa	639:644	arg1	NAAA					595:598	NAAA	595:598	NAAA in the cell homogenate	595:621	Western blotting with anti-NAAA antibody revealed that most of NAAA in the cell homogenate was the cleaved 30-kDa form.
17980170	4	5	theme	30-kDa	639:644	arg1	most					587:590	most	587:590	most	587:590	Western blotting with anti-NAAA antibody revealed that most of NAAA in the cell homogenate was the cleaved 30-kDa form.
17980170	4	5	theme	30-kDa	639:644	arg1	form					646:649	the cleaved 30-kDa form	627:649	the cleaved 30-kDa form	627:649	Western blotting with anti-NAAA antibody revealed that most of NAAA in the cell homogenate was the cleaved 30-kDa form.
17980170	6	6	theme	30-kDa	853:858	arg1	form					860:863	the 30-kDa form	849:863	the 30-kDa form	849:863	When incubated at pH 4.5, the 48-kDa form was time-dependently converted to the 30-kDa form with concomitant increase in the N-palmitoylethanolamine-hydrolyzing activity.
17980170	7	7	theme	purified	948:955	arg1	form					964:967	The purified 48-kDa form	944:967	The purified 48-kDa form	944:967	The purified 48-kDa form was also cleaved and activated.
17980170	5	8	theme	extracellular	714:726	arg1	enzyme					728:733	the extracellular enzyme	710:733	the extracellular enzyme	710:733	However, some of NAAA were released outside the cells and the extracellular enzyme was mostly the uncleaved 48-kDa form.
17980170	5	8	theme	extracellular	714:726	arg1	form					767:770	the uncleaved 48-kDa form	746:770	the uncleaved 48-kDa form	746:770	However, some of NAAA were released outside the cells and the extracellular enzyme was mostly the uncleaved 48-kDa form.
17980170	11	9	gly	N-glycosylation	1396:1410	arg2	sites					1412:1416	six potential N-glycosylation sites	1382:1416	six potential N-glycosylation sites	1382:1416	We next determined N-glycosylation sites of human NAAA by site-directed mutagenesis addressed to asparagine residues in six potential N-glycosylation sites.
17980170	11	9	gly	N-glycosylation	1396:1410	arg2	six					1382:1384	six	1382:1384	six	1382:1384	We next determined N-glycosylation sites of human NAAA by site-directed mutagenesis addressed to asparagine residues in six potential N-glycosylation sites.
17980170	0	10	theme	endocannabinoid	124:138	arg1	metabolism					140:149	the endocannabinoid metabolism	120:149	the endocannabinoid metabolism	120:149	Proteolytic activation and glycosylation of N-acylethanolamine-hydrolyzing acid amidase, a lysosomal enzyme involved in the endocannabinoid metabolism.
17980170	12	11	theme	N-glycosylation	1495:1509	arg1	Asn-309					1463:1469	Asn-309	1463:1469	Asn-309	1463:1469	The results exhibited that Asn-37, Asn-107, Asn-309, and Asn-333 are actual N-glycosylation sites.
17980170	12	11	theme	N-glycosylation	1495:1509	arg1	Asn-333					1476:1482	Asn-333	1476:1482	Asn-333	1476:1482	The results exhibited that Asn-37, Asn-107, Asn-309, and Asn-333 are actual N-glycosylation sites.
17980170	12	11	theme	N-glycosylation	1495:1509	arg1	Asn-107					1454:1460	Asn-107	1454:1460	Asn-107	1454:1460	The results exhibited that Asn-37, Asn-107, Asn-309, and Asn-333 are actual N-glycosylation sites.
17980170	12	11	theme	N-glycosylation	1495:1509	arg1	Asn-37					1446:1451	Asn-37	1446:1451	Asn-37	1446:1451	The results exhibited that Asn-37, Asn-107, Asn-309, and Asn-333 are actual N-glycosylation sites.
17980170	12	11	theme	N-glycosylation	1495:1509	arg1	sites					1511:1515	actual N-glycosylation sites	1488:1515	actual N-glycosylation sites	1488:1515	The results exhibited that Asn-37, Asn-107, Asn-309, and Asn-333 are actual N-glycosylation sites.
17980170	11	12	theme	potential	1386:1394	arg1	sites					1412:1416	six potential N-glycosylation sites	1382:1416	six potential N-glycosylation sites	1382:1416	We next determined N-glycosylation sites of human NAAA by site-directed mutagenesis addressed to asparagine residues in six potential N-glycosylation sites.
17980170	13	13	theme	important	1556:1564	arg1	role					1566:1569	an important role	1553:1569	an important role	1553:1569	The glycosylation appeared to play an important role in stabilizing the enzyme protein.
17980170	12	14	theme	actual	1488:1493	arg1	Asn-309					1463:1469	Asn-309	1463:1469	Asn-309	1463:1469	The results exhibited that Asn-37, Asn-107, Asn-309, and Asn-333 are actual N-glycosylation sites.
17980170	12	14	theme	actual	1488:1493	arg1	Asn-333					1476:1482	Asn-333	1476:1482	Asn-333	1476:1482	The results exhibited that Asn-37, Asn-107, Asn-309, and Asn-333 are actual N-glycosylation sites.
17980170	12	14	theme	actual	1488:1493	arg1	Asn-107					1454:1460	Asn-107	1454:1460	Asn-107	1454:1460	The results exhibited that Asn-37, Asn-107, Asn-309, and Asn-333 are actual N-glycosylation sites.
17980170	12	14	theme	actual	1488:1493	arg1	Asn-37					1446:1451	Asn-37	1446:1451	Asn-37	1446:1451	The results exhibited that Asn-37, Asn-107, Asn-309, and Asn-333 are actual N-glycosylation sites.
17980170	12	14	theme	actual	1488:1493	arg1	sites					1511:1515	actual N-glycosylation sites	1488:1515	actual N-glycosylation sites	1488:1515	The results exhibited that Asn-37, Asn-107, Asn-309, and Asn-333 are actual N-glycosylation sites.
17980170	13	15	theme	enzyme	1590:1595	arg1	protein					1597:1603	the enzyme protein	1586:1603	the enzyme protein	1586:1603	The glycosylation appeared to play an important role in stabilizing the enzyme protein.
17980170	3	16	theme	embryonic	504:512	arg1	kidney					514:519	human embryonic kidney 293	498:523	human embryonic kidney 293 cells	498:529	Here, we investigated the mechanism and significance of the cleavage of human NAAA overexpressed in human embryonic kidney 293 cells.
17980170	0	17	theme	acid	75:78	arg1	amidase					80:86	N-acylethanolamine-hydrolyzing acid amidase	44:86	N-acylethanolamine-hydrolyzing acid amidase	44:86	Proteolytic activation and glycosylation of N-acylethanolamine-hydrolyzing acid amidase, a lysosomal enzyme involved in the endocannabinoid metabolism.
17980170	3	18	theme	NAAA	476:479	arg1	cleavage					458:465	the cleavage	454:465	the cleavage of human NAAA overexpressed in human embryonic kidney 293 cells	454:529	Here, we investigated the mechanism and significance of the cleavage of human NAAA overexpressed in human embryonic kidney 293 cells.
17980170	3	19	theme	cleavage	458:465	arg1	significance					438:449	significance	438:449	significance	438:449	Here, we investigated the mechanism and significance of the cleavage of human NAAA overexpressed in human embryonic kidney 293 cells.
17980170	3	19	theme	cleavage	458:465	arg1	mechanism					424:432	mechanism	424:432	mechanism	424:432	Here, we investigated the mechanism and significance of the cleavage of human NAAA overexpressed in human embryonic kidney 293 cells.
17980170	3	20	theme	kidney	514:519	arg1	cells					525:529	human embryonic kidney 293 cells	498:529	human embryonic kidney 293 cells	498:529	Here, we investigated the mechanism and significance of the cleavage of human NAAA overexpressed in human embryonic kidney 293 cells.
17980170	8	21	theme	acid	1094:1097	arg1	presence					1059:1066	the presence	1055:1066	the presence of p-chloromercuribenzoic acid	1055:1097	However, the cleavage did not proceed at pH 7.4 or in the presence of p-chloromercuribenzoic acid.
17980170	4	22	theme	anti-NAAA	554:562	arg1	antibody					564:571	anti-NAAA antibody	554:571	anti-NAAA antibody	554:571	Western blotting with anti-NAAA antibody revealed that most of NAAA in the cell homogenate was the cleaved 30-kDa form.
17980170	6	23	from	increase	882:889	arg1	activity					934:941	the N-palmitoylethanolamine-hydrolyzing activity	894:941	the N-palmitoylethanolamine-hydrolyzing activity	894:941	When incubated at pH 4.5, the 48-kDa form was time-dependently converted to the 30-kDa form with concomitant increase in the N-palmitoylethanolamine-hydrolyzing activity.
17980170	1	24	theme	lysosomal	208:216	arg1	enzyme					218:223	a lysosomal enzyme	206:223	a lysosomal enzyme hydrolyzing bioactive N-acylethanolamines, including anandamide and N-palmitoylethanolamine	206:315	N-acylethanolamine-hydrolyzing acid amidase (NAAA) is a lysosomal enzyme hydrolyzing bioactive N-acylethanolamines, including anandamide and N-palmitoylethanolamine.
17980170	1	24	theme	lysosomal	208:216	arg1	amidase					188:194	N-acylethanolamine-hydrolyzing acid amidase	152:194	N-acylethanolamine-hydrolyzing acid amidase (NAAA)	152:201	N-acylethanolamine-hydrolyzing acid amidase (NAAA) is a lysosomal enzyme hydrolyzing bioactive N-acylethanolamines, including anandamide and N-palmitoylethanolamine.
17980170	0	25	theme	Proteolytic	0:10	arg1	enzyme					101:106	a lysosomal enzyme	89:106	a lysosomal enzyme involved in the endocannabinoid metabolism	89:149	Proteolytic activation and glycosylation of N-acylethanolamine-hydrolyzing acid amidase, a lysosomal enzyme involved in the endocannabinoid metabolism.
17980170	0	25	theme	Proteolytic	0:10	arg1	activation					12:21	activation	12:21	activation	12:21	Proteolytic activation and glycosylation of N-acylethanolamine-hydrolyzing acid amidase, a lysosomal enzyme involved in the endocannabinoid metabolism.
17980170	3	26	theme	human	498:502	arg1	kidney					514:519	human embryonic kidney 293	498:523	human embryonic kidney 293 cells	498:529	Here, we investigated the mechanism and significance of the cleavage of human NAAA overexpressed in human embryonic kidney 293 cells.
17980170	5	27	theme	uncleaved	750:758	arg1	enzyme					728:733	the extracellular enzyme	710:733	the extracellular enzyme	710:733	However, some of NAAA were released outside the cells and the extracellular enzyme was mostly the uncleaved 48-kDa form.
17980170	5	27	theme	uncleaved	750:758	arg1	form					767:770	the uncleaved 48-kDa form	746:770	the uncleaved 48-kDa form	746:770	However, some of NAAA were released outside the cells and the extracellular enzyme was mostly the uncleaved 48-kDa form.
17980170	4	28	theme	cleaved	631:637	arg1	NAAA					595:598	NAAA	595:598	NAAA in the cell homogenate	595:621	Western blotting with anti-NAAA antibody revealed that most of NAAA in the cell homogenate was the cleaved 30-kDa form.
17980170	4	28	theme	cleaved	631:637	arg1	most					587:590	most	587:590	most	587:590	Western blotting with anti-NAAA antibody revealed that most of NAAA in the cell homogenate was the cleaved 30-kDa form.
17980170	4	28	theme	cleaved	631:637	arg1	form					646:649	the cleaved 30-kDa form	627:649	the cleaved 30-kDa form	627:649	Western blotting with anti-NAAA antibody revealed that most of NAAA in the cell homogenate was the cleaved 30-kDa form.
17980170	5	29	theme	48-kDa	760:765	arg1	enzyme					728:733	the extracellular enzyme	710:733	the extracellular enzyme	710:733	However, some of NAAA were released outside the cells and the extracellular enzyme was mostly the uncleaved 48-kDa form.
17980170	5	29	theme	48-kDa	760:765	arg1	form					767:770	the uncleaved 48-kDa form	746:770	the uncleaved 48-kDa form	746:770	However, some of NAAA were released outside the cells and the extracellular enzyme was mostly the uncleaved 48-kDa form.
17980170	1	30	theme	bioactive	237:245	arg1	N-palmitoylethanolamine					293:315	N-palmitoylethanolamine	293:315	N-palmitoylethanolamine	293:315	N-acylethanolamine-hydrolyzing acid amidase (NAAA) is a lysosomal enzyme hydrolyzing bioactive N-acylethanolamines, including anandamide and N-palmitoylethanolamine.
17980170	1	30	theme	bioactive	237:245	arg1	N-acylethanolamines					247:265	bioactive N-acylethanolamines	237:265	bioactive N-acylethanolamines	237:265	N-acylethanolamine-hydrolyzing acid amidase (NAAA) is a lysosomal enzyme hydrolyzing bioactive N-acylethanolamines, including anandamide and N-palmitoylethanolamine.
17980170	1	30	theme	bioactive	237:245	arg1	anandamide					278:287	anandamide	278:287	anandamide	278:287	N-acylethanolamine-hydrolyzing acid amidase (NAAA) is a lysosomal enzyme hydrolyzing bioactive N-acylethanolamines, including anandamide and N-palmitoylethanolamine.
17980170	0	31	theme	N-acylethanolamine-hydrolyzing	44:73	arg1	amidase					80:86	N-acylethanolamine-hydrolyzing acid amidase	44:86	N-acylethanolamine-hydrolyzing acid amidase	44:86	Proteolytic activation and glycosylation of N-acylethanolamine-hydrolyzing acid amidase, a lysosomal enzyme involved in the endocannabinoid metabolism.
17980170	11	32	theme	N-glycosylation	1281:1295	arg1	sites					1297:1301	N-glycosylation sites	1281:1301	N-glycosylation sites of human NAAA	1281:1315	We next determined N-glycosylation sites of human NAAA by site-directed mutagenesis addressed to asparagine residues in six potential N-glycosylation sites.
17980170	11	32	theme	N-glycosylation	1281:1295	arg1	NAAA					1312:1315	human NAAA	1306:1315	human NAAA	1306:1315	We next determined N-glycosylation sites of human NAAA by site-directed mutagenesis addressed to asparagine residues in six potential N-glycosylation sites.
17980170	10	33	theme	specific	1204:1211	arg1	step					1256:1259	a self-catalyzed activation step	1228:1259	a self-catalyzed activation step	1228:1259	These results suggested that this specific proteolysis is a self-catalyzed activation step.
17980170	10	33	theme	specific	1204:1211	arg1	proteolysis					1213:1223	this specific proteolysis	1199:1223	this specific proteolysis	1199:1223	These results suggested that this specific proteolysis is a self-catalyzed activation step.
17980170	4	34	theme	Western	532:538	arg1	blotting					540:547	Western blotting	532:547	Western blotting with anti-NAAA antibody	532:571	Western blotting with anti-NAAA antibody revealed that most of NAAA in the cell homogenate was the cleaved 30-kDa form.
17980170	11	35	theme	site-directed	1320:1332	arg1	mutagenesis					1334:1344	site-directed mutagenesis	1320:1344	site-directed mutagenesis addressed to asparagine residues in six potential N-glycosylation sites	1320:1416	We next determined N-glycosylation sites of human NAAA by site-directed mutagenesis addressed to asparagine residues in six potential N-glycosylation sites.
17980170	6	36	theme	48-kDa	803:808	arg1	form					810:813	the 48-kDa form	799:813	the 48-kDa form	799:813	When incubated at pH 4.5, the 48-kDa form was time-dependently converted to the 30-kDa form with concomitant increase in the N-palmitoylethanolamine-hydrolyzing activity.
17980170	0	37	theme	amidase	80:86	arg1	glycosylation					27:39	glycosylation	27:39	glycosylation	27:39	Proteolytic activation and glycosylation of N-acylethanolamine-hydrolyzing acid amidase, a lysosomal enzyme involved in the endocannabinoid metabolism.
17980170	0	37	theme	amidase	80:86	arg1	activation					12:21	activation	12:21	activation	12:21	Proteolytic activation and glycosylation of N-acylethanolamine-hydrolyzing acid amidase, a lysosomal enzyme involved in the endocannabinoid metabolism.
17980170	0	37	theme	amidase	80:86	arg1	enzyme					101:106	a lysosomal enzyme	89:106	a lysosomal enzyme involved in the endocannabinoid metabolism	89:149	Proteolytic activation and glycosylation of N-acylethanolamine-hydrolyzing acid amidase, a lysosomal enzyme involved in the endocannabinoid metabolism.
17980170	4	38	from	NAAA	595:598	arg1	homogenate					612:621	the cell homogenate	603:621	the cell homogenate	603:621	Western blotting with anti-NAAA antibody revealed that most of NAAA in the cell homogenate was the cleaved 30-kDa form.
17980170	11	39	theme	NAAA	1312:1315	arg1	sites					1297:1301	N-glycosylation sites	1281:1301	N-glycosylation sites of human NAAA	1281:1315	We next determined N-glycosylation sites of human NAAA by site-directed mutagenesis addressed to asparagine residues in six potential N-glycosylation sites.
17980170	11	39	theme	NAAA	1312:1315	arg1	NAAA					1312:1315	human NAAA	1306:1315	human NAAA	1306:1315	We next determined N-glycosylation sites of human NAAA by site-directed mutagenesis addressed to asparagine residues in six potential N-glycosylation sites.
17980170	3	40	theme	human	470:474	arg1	NAAA					476:479	human NAAA	470:479	human NAAA overexpressed in human embryonic kidney 293 cells	470:529	Here, we investigated the mechanism and significance of the cleavage of human NAAA overexpressed in human embryonic kidney 293 cells.
17980170	4	41	theme	cell	607:610	arg1	homogenate					612:621	the cell homogenate	603:621	the cell homogenate	603:621	Western blotting with anti-NAAA antibody revealed that most of NAAA in the cell homogenate was the cleaved 30-kDa form.
17980170	0	42	gly	glycosylation	27:39	arg1	amidase					80:86	N-acylethanolamine-hydrolyzing acid amidase	44:86	N-acylethanolamine-hydrolyzing acid amidase	44:86	Proteolytic activation and glycosylation of N-acylethanolamine-hydrolyzing acid amidase, a lysosomal enzyme involved in the endocannabinoid metabolism.
17980170	6	43	theme	N-palmitoylethanolamine-hydrolyzing	898:932	arg1	activity					934:941	the N-palmitoylethanolamine-hydrolyzing activity	894:941	the N-palmitoylethanolamine-hydrolyzing activity	894:941	When incubated at pH 4.5, the 48-kDa form was time-dependently converted to the 30-kDa form with concomitant increase in the N-palmitoylethanolamine-hydrolyzing activity.
17980170	11	44	theme	human	1306:1310	arg1	NAAA					1312:1315	human NAAA	1306:1315	human NAAA	1306:1315	We next determined N-glycosylation sites of human NAAA by site-directed mutagenesis addressed to asparagine residues in six potential N-glycosylation sites.
17980170	11	45	from	residues	1370:1377	arg1	sites					1412:1416	six potential N-glycosylation sites	1382:1416	six potential N-glycosylation sites	1382:1416	We next determined N-glycosylation sites of human NAAA by site-directed mutagenesis addressed to asparagine residues in six potential N-glycosylation sites.
17980170	3	46	dep	mechanism	424:432	arg1	the					420:422	the	420:422	the	420:422	Here, we investigated the mechanism and significance of the cleavage of human NAAA overexpressed in human embryonic kidney 293 cells.
17980170	1	47	theme	N-acylethanolamine-hydrolyzing	152:181	arg1	enzyme					218:223	a lysosomal enzyme	206:223	a lysosomal enzyme hydrolyzing bioactive N-acylethanolamines, including anandamide and N-palmitoylethanolamine	206:315	N-acylethanolamine-hydrolyzing acid amidase (NAAA) is a lysosomal enzyme hydrolyzing bioactive N-acylethanolamines, including anandamide and N-palmitoylethanolamine.
17980170	1	47	theme	N-acylethanolamine-hydrolyzing	152:181	arg1	NAAA					197:200	NAAA	197:200	NAAA	197:200	N-acylethanolamine-hydrolyzing acid amidase (NAAA) is a lysosomal enzyme hydrolyzing bioactive N-acylethanolamines, including anandamide and N-palmitoylethanolamine.
17980170	1	47	theme	N-acylethanolamine-hydrolyzing	152:181	arg1	amidase					188:194	N-acylethanolamine-hydrolyzing acid amidase	152:194	N-acylethanolamine-hydrolyzing acid amidase (NAAA)	152:201	N-acylethanolamine-hydrolyzing acid amidase (NAAA) is a lysosomal enzyme hydrolyzing bioactive N-acylethanolamines, including anandamide and N-palmitoylethanolamine.
17980170	6	48	theme	concomitant	870:880	arg1	increase					882:889	concomitant increase	870:889	concomitant increase in the N-palmitoylethanolamine-hydrolyzing activity	870:941	When incubated at pH 4.5, the 48-kDa form was time-dependently converted to the 30-kDa form with concomitant increase in the N-palmitoylethanolamine-hydrolyzing activity.
17980170	1	49	theme	acid	183:186	arg1	enzyme					218:223	a lysosomal enzyme	206:223	a lysosomal enzyme hydrolyzing bioactive N-acylethanolamines, including anandamide and N-palmitoylethanolamine	206:315	N-acylethanolamine-hydrolyzing acid amidase (NAAA) is a lysosomal enzyme hydrolyzing bioactive N-acylethanolamines, including anandamide and N-palmitoylethanolamine.
17980170	1	49	theme	acid	183:186	arg1	NAAA					197:200	NAAA	197:200	NAAA	197:200	N-acylethanolamine-hydrolyzing acid amidase (NAAA) is a lysosomal enzyme hydrolyzing bioactive N-acylethanolamines, including anandamide and N-palmitoylethanolamine.
17980170	1	49	theme	acid	183:186	arg1	amidase					188:194	N-acylethanolamine-hydrolyzing acid amidase	152:194	N-acylethanolamine-hydrolyzing acid amidase (NAAA)	152:201	N-acylethanolamine-hydrolyzing acid amidase (NAAA) is a lysosomal enzyme hydrolyzing bioactive N-acylethanolamines, including anandamide and N-palmitoylethanolamine.
17980170	10	50	theme	activation	1245:1254	arg1	step					1256:1259	a self-catalyzed activation step	1228:1259	a self-catalyzed activation step	1228:1259	These results suggested that this specific proteolysis is a self-catalyzed activation step.
17980170	10	50	theme	activation	1245:1254	arg1	proteolysis					1213:1223	this specific proteolysis	1199:1223	this specific proteolysis	1199:1223	These results suggested that this specific proteolysis is a self-catalyzed activation step.
17980170	11	51	gly	N-glycosylation	1281:1295	arg1	NAAA					1312:1315	human NAAA	1306:1315	human NAAA	1306:1315	We next determined N-glycosylation sites of human NAAA by site-directed mutagenesis addressed to asparagine residues in six potential N-glycosylation sites.
17980170	11	51	gly	N-glycosylation	1281:1295	arg2	sites					1297:1301	N-glycosylation sites	1281:1301	N-glycosylation sites of human NAAA	1281:1315	We next determined N-glycosylation sites of human NAAA by site-directed mutagenesis addressed to asparagine residues in six potential N-glycosylation sites.
17980170	11	51	gly	N-glycosylation	1281:1295	arg2	NAAA					1312:1315	human NAAA	1306:1315	human NAAA	1306:1315	We next determined N-glycosylation sites of human NAAA by site-directed mutagenesis addressed to asparagine residues in six potential N-glycosylation sites.
17980170	12	52	gly	N-glycosylation	1495:1509	arg2	Asn-107					1454:1460	Asn-107	1454:1460	Asn-107	1454:1460	The results exhibited that Asn-37, Asn-107, Asn-309, and Asn-333 are actual N-glycosylation sites.
17980170	12	52	gly	N-glycosylation	1495:1509	arg2	Asn-333					1476:1482	Asn-333	1476:1482	Asn-333	1476:1482	The results exhibited that Asn-37, Asn-107, Asn-309, and Asn-333 are actual N-glycosylation sites.
17980170	12	52	gly	N-glycosylation	1495:1509	arg2	Asn-37					1446:1451	Asn-37	1446:1451	Asn-37	1446:1451	The results exhibited that Asn-37, Asn-107, Asn-309, and Asn-333 are actual N-glycosylation sites.
17980170	12	52	gly	N-glycosylation	1495:1509	arg2	sites					1511:1515	actual N-glycosylation sites	1488:1515	actual N-glycosylation sites	1488:1515	The results exhibited that Asn-37, Asn-107, Asn-309, and Asn-333 are actual N-glycosylation sites.
17980170	12	52	gly	N-glycosylation	1495:1509	arg2	Asn-309					1463:1469	Asn-309	1463:1469	Asn-309	1463:1469	The results exhibited that Asn-37, Asn-107, Asn-309, and Asn-333 are actual N-glycosylation sites.
17980170	11	53	theme	asparagine	1359:1368	arg1	residues					1370:1377	asparagine residues	1359:1377	asparagine residues in six potential N-glycosylation sites	1359:1416	We next determined N-glycosylation sites of human NAAA by site-directed mutagenesis addressed to asparagine residues in six potential N-glycosylation sites.
17980170	10	54	theme	self-catalyzed	1230:1243	arg1	step					1256:1259	a self-catalyzed activation step	1228:1259	a self-catalyzed activation step	1228:1259	These results suggested that this specific proteolysis is a self-catalyzed activation step.
17980170	10	54	theme	self-catalyzed	1230:1243	arg1	proteolysis					1213:1223	this specific proteolysis	1199:1223	this specific proteolysis	1199:1223	These results suggested that this specific proteolysis is a self-catalyzed activation step.
17980170	11	55	theme	N-glycosylation	1396:1410	arg1	sites					1412:1416	six potential N-glycosylation sites	1382:1416	six potential N-glycosylation sites	1382:1416	We next determined N-glycosylation sites of human NAAA by site-directed mutagenesis addressed to asparagine residues in six potential N-glycosylation sites.
17980170	7	56	theme	48-kDa	957:962	arg1	form					964:967	The purified 48-kDa form	944:967	The purified 48-kDa form	944:967	The purified 48-kDa form was also cleaved and activated.
15152093	0	0	theme	proteolytic	91:101	arg1	activity					103:110	proteolytic activity	91:110	proteolytic activity	91:110	Identification of the N-glycosylation sites on glutamate carboxypeptidase II necessary for proteolytic activity.
15152093	3	1	theme	effective	710:718	arg1	marker					736:741	an effective prostate cancer marker	707:741	an effective prostate cancer marker	707:741	The prostate form of GCPII, termed prostate-specific membrane antigen (PSMA), is up-regulated in cancer and used as an effective prostate cancer marker.
15152093	3	1	theme	effective	710:718	arg1	form					604:607	The prostate form	591:607	The prostate form	591:607	The prostate form of GCPII, termed prostate-specific membrane antigen (PSMA), is up-regulated in cancer and used as an effective prostate cancer marker.
15152093	1	2	theme	membrane	156:163	arg1	II					140:141	Glutamate carboxypeptidase II	113:141	Glutamate carboxypeptidase II (GCPII)	113:149	Glutamate carboxypeptidase II (GCPII) is a membrane peptidase expressed in the prostate, central and peripheral nervous system, kidney, small intestine, and tumor-associated neovasculature.
15152093	1	2	theme	membrane	156:163	arg1	peptidase					165:173	a membrane peptidase	154:173	a membrane peptidase expressed in the prostate, central and peripheral nervous system, kidney, small intestine, and tumor-associated neovasculature	154:300	Glutamate carboxypeptidase II (GCPII) is a membrane peptidase expressed in the prostate, central and peripheral nervous system, kidney, small intestine, and tumor-associated neovasculature.
15152093	2	3	from	glutamate	465:473	arg1	cleft					491:495	the synaptic cleft	478:495	the synaptic cleft	478:495	The GCPII form expressed in the central nervous system, termed NAALADase, is responsible for the cleavage of N-acetyl-L-aspartyl-L-glutamate (NAAG) yielding free glutamate in the synaptic cleft, and is implicated in various pathologic conditions associated with glutamate excitotoxicity.
15152093	6	4	theme	GCPII	988:992	arg1	folding					946:952	proper folding	939:952	proper folding	939:952	In this paper we show that N-glycosylation is vital for proper folding and subsequent secretion of human GCPII.
15152093	6	4	theme	GCPII	988:992	arg1	secretion					969:977	subsequent secretion	958:977	subsequent secretion	958:977	In this paper we show that N-glycosylation is vital for proper folding and subsequent secretion of human GCPII.
15152093	2	5	theme	synaptic	482:489	arg1	cleft					491:495	the synaptic cleft	478:495	the synaptic cleft	478:495	The GCPII form expressed in the central nervous system, termed NAALADase, is responsible for the cleavage of N-acetyl-L-aspartyl-L-glutamate (NAAG) yielding free glutamate in the synaptic cleft, and is implicated in various pathologic conditions associated with glutamate excitotoxicity.
15152093	1	6	theme	small	249:253	arg1	intestine					255:263	small intestine	249:263	small intestine	249:263	Glutamate carboxypeptidase II (GCPII) is a membrane peptidase expressed in the prostate, central and peripheral nervous system, kidney, small intestine, and tumor-associated neovasculature.
15152093	2	7	theme	various	519:525	arg1	conditions					538:547	various pathologic conditions	519:547	various pathologic conditions associated with glutamate excitotoxicity	519:588	The GCPII form expressed in the central nervous system, termed NAALADase, is responsible for the cleavage of N-acetyl-L-aspartyl-L-glutamate (NAAG) yielding free glutamate in the synaptic cleft, and is implicated in various pathologic conditions associated with glutamate excitotoxicity.
15152093	0	8	from	Identification	0:13	arg1	carboxypeptidase					57:72	glutamate carboxypeptidase II	47:75	glutamate carboxypeptidase II	47:75	Identification of the N-glycosylation sites on glutamate carboxypeptidase II necessary for proteolytic activity.
15152093	7	9	theme	GCPII	1100:1104	arg1	activity					1123:1130	GCPII carboxypeptidase activity	1100:1130	GCPII carboxypeptidase activity	1100:1130	Analysis of the predicted N-glycosylation sites also provides evidence that these sites are critical for GCPII carboxypeptidase activity.
15152093	8	10	theme	described	1397:1405	arg1	models					1418:1423	previously described structural models	1386:1423	previously described structural models of GCPII	1386:1432	We confirm that all predicted N-glycosylation sites are occupied by an oligosaccharide moiety and show that glycosylation at sites distant from the putative catalytic domain is critical for the NAAG-hydrolyzing activity of GCPII calling the validity of previously described structural models of GCPII into question.
15152093	8	11	theme	predicted	1153:1161	arg1	sites					1179:1183	all predicted N-glycosylation sites	1149:1183	all predicted N-glycosylation sites	1149:1183	We confirm that all predicted N-glycosylation sites are occupied by an oligosaccharide moiety and show that glycosylation at sites distant from the putative catalytic domain is critical for the NAAG-hydrolyzing activity of GCPII calling the validity of previously described structural models of GCPII into question.
15152093	0	12	from	carboxypeptidase	57:72	arg1	Identification					0:13	Identification	0:13	Identification of the N-glycosylation sites on glutamate carboxypeptidase II	0:75	Identification of the N-glycosylation sites on glutamate carboxypeptidase II necessary for proteolytic activity.
15152093	7	13	theme	carboxypeptidase	1106:1121	arg1	activity					1123:1130	GCPII carboxypeptidase activity	1100:1130	GCPII carboxypeptidase activity	1100:1130	Analysis of the predicted N-glycosylation sites also provides evidence that these sites are critical for GCPII carboxypeptidase activity.
15152093	8	14	theme	GCPII	1356:1360	arg1	activity					1344:1351	the NAAG-hydrolyzing activity	1323:1351	the NAAG-hydrolyzing activity of GCPII	1323:1360	We confirm that all predicted N-glycosylation sites are occupied by an oligosaccharide moiety and show that glycosylation at sites distant from the putative catalytic domain is critical for the NAAG-hydrolyzing activity of GCPII calling the validity of previously described structural models of GCPII into question.
15152093	3	15	theme	cancer	729:734	arg1	marker					736:741	an effective prostate cancer marker	707:741	an effective prostate cancer marker	707:741	The prostate form of GCPII, termed prostate-specific membrane antigen (PSMA), is up-regulated in cancer and used as an effective prostate cancer marker.
15152093	3	15	theme	cancer	729:734	arg1	form					604:607	The prostate form	591:607	The prostate form	591:607	The prostate form of GCPII, termed prostate-specific membrane antigen (PSMA), is up-regulated in cancer and used as an effective prostate cancer marker.
15152093	8	16	from	domain	1300:1305	arg1	distant					1264:1270	distant	1264:1270	distant	1264:1270	We confirm that all predicted N-glycosylation sites are occupied by an oligosaccharide moiety and show that glycosylation at sites distant from the putative catalytic domain is critical for the NAAG-hydrolyzing activity of GCPII calling the validity of previously described structural models of GCPII into question.
15152093	4	17	theme	target	813:818	arg1	structure					770:778	the structure	766:778	the structure of this important pharmaceutical target	766:818	Little is known about the structure of this important pharmaceutical target.
15152093	2	18	theme	free	460:463	arg1	glutamate					465:473	free glutamate	460:473	free glutamate in the synaptic cleft	460:495	The GCPII form expressed in the central nervous system, termed NAALADase, is responsible for the cleavage of N-acetyl-L-aspartyl-L-glutamate (NAAG) yielding free glutamate in the synaptic cleft, and is implicated in various pathologic conditions associated with glutamate excitotoxicity.
15152093	8	19	theme	NAAG-hydrolyzing	1327:1342	arg1	activity					1344:1351	the NAAG-hydrolyzing activity	1323:1351	the NAAG-hydrolyzing activity of GCPII	1323:1360	We confirm that all predicted N-glycosylation sites are occupied by an oligosaccharide moiety and show that glycosylation at sites distant from the putative catalytic domain is critical for the NAAG-hydrolyzing activity of GCPII calling the validity of previously described structural models of GCPII into question.
15152093	8	20	theme	putative	1281:1288	arg1	domain					1300:1305	the putative catalytic domain	1277:1305	the putative catalytic domain	1277:1305	We confirm that all predicted N-glycosylation sites are occupied by an oligosaccharide moiety and show that glycosylation at sites distant from the putative catalytic domain is critical for the NAAG-hydrolyzing activity of GCPII calling the validity of previously described structural models of GCPII into question.
15152093	7	21	theme	N-glycosylation	1021:1035	arg1	sites					1037:1041	the predicted N-glycosylation sites	1007:1041	the predicted N-glycosylation sites	1007:1041	Analysis of the predicted N-glycosylation sites also provides evidence that these sites are critical for GCPII carboxypeptidase activity.
15152093	0	22	from	sites	38:42	arg1	carboxypeptidase					57:72	glutamate carboxypeptidase II	47:75	glutamate carboxypeptidase II	47:75	Identification of the N-glycosylation sites on glutamate carboxypeptidase II necessary for proteolytic activity.
15152093	8	23	theme	models	1418:1423	arg1	validity					1374:1381	the validity	1370:1381	the validity of previously described structural models of GCPII	1370:1432	We confirm that all predicted N-glycosylation sites are occupied by an oligosaccharide moiety and show that glycosylation at sites distant from the putative catalytic domain is critical for the NAAG-hydrolyzing activity of GCPII calling the validity of previously described structural models of GCPII into question.
15152093	8	24	theme	distant	1264:1270	arg1	sites					1258:1262	sites	1258:1262	sites distant from the putative catalytic domain	1258:1305	We confirm that all predicted N-glycosylation sites are occupied by an oligosaccharide moiety and show that glycosylation at sites distant from the putative catalytic domain is critical for the NAAG-hydrolyzing activity of GCPII calling the validity of previously described structural models of GCPII into question.
15152093	6	25	theme	subsequent	958:967	arg1	secretion					969:977	subsequent secretion	958:977	subsequent secretion	958:977	In this paper we show that N-glycosylation is vital for proper folding and subsequent secretion of human GCPII.
15152093	0	26	theme	N-glycosylation	22:36	arg1	sites					38:42	the N-glycosylation sites	18:42	the N-glycosylation sites on glutamate carboxypeptidase II	18:75	Identification of the N-glycosylation sites on glutamate carboxypeptidase II necessary for proteolytic activity.
15152093	1	27	theme	tumor-associated	270:285	arg1	neovasculature					287:300	tumor-associated neovasculature	270:300	tumor-associated neovasculature	270:300	Glutamate carboxypeptidase II (GCPII) is a membrane peptidase expressed in the prostate, central and peripheral nervous system, kidney, small intestine, and tumor-associated neovasculature.
15152093	8	28	theme	oligosaccharide	1204:1218	arg1	moiety					1220:1225	an oligosaccharide moiety	1201:1225	an oligosaccharide moiety	1201:1225	We confirm that all predicted N-glycosylation sites are occupied by an oligosaccharide moiety and show that glycosylation at sites distant from the putative catalytic domain is critical for the NAAG-hydrolyzing activity of GCPII calling the validity of previously described structural models of GCPII into question.
15152093	2	29	theme	GCPII	307:311	arg1	responsible					380:390	responsible	380:390	responsible	380:390	The GCPII form expressed in the central nervous system, termed NAALADase, is responsible for the cleavage of N-acetyl-L-aspartyl-L-glutamate (NAAG) yielding free glutamate in the synaptic cleft, and is implicated in various pathologic conditions associated with glutamate excitotoxicity.
15152093	2	29	theme	GCPII	307:311	arg1	form					313:316	The GCPII form	303:316	The GCPII form expressed in the central nervous system, termed NAALADase,	303:375	The GCPII form expressed in the central nervous system, termed NAALADase, is responsible for the cleavage of N-acetyl-L-aspartyl-L-glutamate (NAAG) yielding free glutamate in the synaptic cleft, and is implicated in various pathologic conditions associated with glutamate excitotoxicity.
15152093	2	30	theme	N-acetyl-L-aspartyl-L-glutamate	412:442	arg1	cleavage					400:407	the cleavage	396:407	the cleavage of N-acetyl-L-aspartyl-L-glutamate (NAAG) yielding free glutamate in the synaptic cleft	396:495	The GCPII form expressed in the central nervous system, termed NAALADase, is responsible for the cleavage of N-acetyl-L-aspartyl-L-glutamate (NAAG) yielding free glutamate in the synaptic cleft, and is implicated in various pathologic conditions associated with glutamate excitotoxicity.
15152093	8	31	gly	N-glycosylation	1163:1177	arg2	sites					1179:1183	all predicted N-glycosylation sites	1149:1183	all predicted N-glycosylation sites	1149:1183	We confirm that all predicted N-glycosylation sites are occupied by an oligosaccharide moiety and show that glycosylation at sites distant from the putative catalytic domain is critical for the NAAG-hydrolyzing activity of GCPII calling the validity of previously described structural models of GCPII into question.
15152093	8	32	gly	glycosylation	1241:1253	arg1	sites					1258:1262	sites	1258:1262	sites distant from the putative catalytic domain	1258:1305	We confirm that all predicted N-glycosylation sites are occupied by an oligosaccharide moiety and show that glycosylation at sites distant from the putative catalytic domain is critical for the NAAG-hydrolyzing activity of GCPII calling the validity of previously described structural models of GCPII into question.
15152093	8	32	gly	glycosylation	1241:1253	arg2	sites					1258:1262	sites	1258:1262	sites distant from the putative catalytic domain	1258:1305	We confirm that all predicted N-glycosylation sites are occupied by an oligosaccharide moiety and show that glycosylation at sites distant from the putative catalytic domain is critical for the NAAG-hydrolyzing activity of GCPII calling the validity of previously described structural models of GCPII into question.
15152093	1	33	theme	carboxypeptidase	123:138	arg1	GCPII					144:148	GCPII	144:148	GCPII	144:148	Glutamate carboxypeptidase II (GCPII) is a membrane peptidase expressed in the prostate, central and peripheral nervous system, kidney, small intestine, and tumor-associated neovasculature.
15152093	1	33	theme	carboxypeptidase	123:138	arg1	II					140:141	Glutamate carboxypeptidase II	113:141	Glutamate carboxypeptidase II (GCPII)	113:149	Glutamate carboxypeptidase II (GCPII) is a membrane peptidase expressed in the prostate, central and peripheral nervous system, kidney, small intestine, and tumor-associated neovasculature.
15152093	1	33	theme	carboxypeptidase	123:138	arg1	peptidase					165:173	a membrane peptidase	154:173	a membrane peptidase expressed in the prostate, central and peripheral nervous system, kidney, small intestine, and tumor-associated neovasculature	154:300	Glutamate carboxypeptidase II (GCPII) is a membrane peptidase expressed in the prostate, central and peripheral nervous system, kidney, small intestine, and tumor-associated neovasculature.
15152093	1	34	theme	central	202:208	arg1	system					233:238	central and peripheral nervous system	202:238	system	233:238	Glutamate carboxypeptidase II (GCPII) is a membrane peptidase expressed in the prostate, central and peripheral nervous system, kidney, small intestine, and tumor-associated neovasculature.
15152093	6	35	theme	proper	939:944	arg1	folding					946:952	proper folding	939:952	proper folding	939:952	In this paper we show that N-glycosylation is vital for proper folding and subsequent secretion of human GCPII.
15152093	8	36	used	occupied	1189:1196	arg2	sites					1179:1183	all predicted N-glycosylation sites	1149:1183	all predicted N-glycosylation sites	1149:1183	We confirm that all predicted N-glycosylation sites are occupied by an oligosaccharide moiety and show that glycosylation at sites distant from the putative catalytic domain is critical for the NAAG-hydrolyzing activity of GCPII calling the validity of previously described structural models of GCPII into question.
15152093	8	37	theme	catalytic	1290:1298	arg1	domain					1300:1305	the putative catalytic domain	1277:1305	the putative catalytic domain	1277:1305	We confirm that all predicted N-glycosylation sites are occupied by an oligosaccharide moiety and show that glycosylation at sites distant from the putative catalytic domain is critical for the NAAG-hydrolyzing activity of GCPII calling the validity of previously described structural models of GCPII into question.
15152093	3	38	theme	prostate	720:727	arg1	marker					736:741	an effective prostate cancer marker	707:741	an effective prostate cancer marker	707:741	The prostate form of GCPII, termed prostate-specific membrane antigen (PSMA), is up-regulated in cancer and used as an effective prostate cancer marker.
15152093	3	38	theme	prostate	720:727	arg1	form					604:607	The prostate form	591:607	The prostate form	591:607	The prostate form of GCPII, termed prostate-specific membrane antigen (PSMA), is up-regulated in cancer and used as an effective prostate cancer marker.
15152093	5	39	theme	membrane	834:841	arg1	GCPII					852:856	GCPII	852:856	GCPII	852:856	As a type II membrane protein, GCPII is heavily glycosylated.
15152093	5	39	theme	membrane	834:841	arg1	protein					843:849	a type II membrane protein	824:849	a type II membrane protein	824:849	As a type II membrane protein, GCPII is heavily glycosylated.
15152093	0	40	theme	sites	38:42	arg1	Identification					0:13	Identification	0:13	Identification of the N-glycosylation sites on glutamate carboxypeptidase II	0:75	Identification of the N-glycosylation sites on glutamate carboxypeptidase II necessary for proteolytic activity.
15152093	2	41	theme	pathologic	527:536	arg1	conditions					538:547	various pathologic conditions	519:547	various pathologic conditions associated with glutamate excitotoxicity	519:588	The GCPII form expressed in the central nervous system, termed NAALADase, is responsible for the cleavage of N-acetyl-L-aspartyl-L-glutamate (NAAG) yielding free glutamate in the synaptic cleft, and is implicated in various pathologic conditions associated with glutamate excitotoxicity.
15152093	6	42	theme	human	982:986	arg1	GCPII					988:992	human GCPII	982:992	human GCPII	982:992	In this paper we show that N-glycosylation is vital for proper folding and subsequent secretion of human GCPII.
15152093	1	43	dep	prostate	192:199	arg1	the					188:190	the	188:190	the	188:190	Glutamate carboxypeptidase II (GCPII) is a membrane peptidase expressed in the prostate, central and peripheral nervous system, kidney, small intestine, and tumor-associated neovasculature.
15152093	1	44	theme	peripheral	214:223	arg1	system					233:238	central and peripheral nervous system	202:238	system	233:238	Glutamate carboxypeptidase II (GCPII) is a membrane peptidase expressed in the prostate, central and peripheral nervous system, kidney, small intestine, and tumor-associated neovasculature.
15152093	8	45	theme	N-glycosylation	1163:1177	arg1	sites					1179:1183	all predicted N-glycosylation sites	1149:1183	all predicted N-glycosylation sites	1149:1183	We confirm that all predicted N-glycosylation sites are occupied by an oligosaccharide moiety and show that glycosylation at sites distant from the putative catalytic domain is critical for the NAAG-hydrolyzing activity of GCPII calling the validity of previously described structural models of GCPII into question.
15152093	7	46	theme	sites	1037:1041	arg1	Analysis					995:1002	Analysis	995:1002	Analysis of the predicted N-glycosylation sites	995:1041	Analysis of the predicted N-glycosylation sites also provides evidence that these sites are critical for GCPII carboxypeptidase activity.
15152093	3	47	theme	prostate	595:602	arg1	marker					736:741	an effective prostate cancer marker	707:741	an effective prostate cancer marker	707:741	The prostate form of GCPII, termed prostate-specific membrane antigen (PSMA), is up-regulated in cancer and used as an effective prostate cancer marker.
15152093	3	47	theme	prostate	595:602	arg1	form					604:607	The prostate form	591:607	The prostate form	591:607	The prostate form of GCPII, termed prostate-specific membrane antigen (PSMA), is up-regulated in cancer and used as an effective prostate cancer marker.
15152093	8	48	from	sites	1258:1262	arg1	glycosylation					1241:1253	glycosylation	1241:1253	glycosylation at sites distant from the putative catalytic domain	1241:1305	We confirm that all predicted N-glycosylation sites are occupied by an oligosaccharide moiety and show that glycosylation at sites distant from the putative catalytic domain is critical for the NAAG-hydrolyzing activity of GCPII calling the validity of previously described structural models of GCPII into question.
15152093	2	49	theme	nervous	343:349	arg1	system					351:356	the central nervous system	331:356	the central nervous system	331:356	The GCPII form expressed in the central nervous system, termed NAALADase, is responsible for the cleavage of N-acetyl-L-aspartyl-L-glutamate (NAAG) yielding free glutamate in the synaptic cleft, and is implicated in various pathologic conditions associated with glutamate excitotoxicity.
15152093	0	50	theme	glutamate	47:55	arg1	carboxypeptidase					57:72	glutamate carboxypeptidase II	47:75	glutamate carboxypeptidase II	47:75	Identification of the N-glycosylation sites on glutamate carboxypeptidase II necessary for proteolytic activity.
15152093	5	51	gly	glycosylated	869:880	arg1	GCPII					852:856	GCPII	852:856	GCPII	852:856	As a type II membrane protein, GCPII is heavily glycosylated.
15152093	5	51	gly	glycosylated	869:880	arg1	protein					843:849	a type II membrane protein	824:849	a type II membrane protein	824:849	As a type II membrane protein, GCPII is heavily glycosylated.
15152093	0	52	gly	N-glycosylation	22:36	arg2	sites					38:42	the N-glycosylation sites	18:42	the N-glycosylation sites on glutamate carboxypeptidase II	18:75	Identification of the N-glycosylation sites on glutamate carboxypeptidase II necessary for proteolytic activity.
15152093	2	53	theme	central	335:341	arg1	system					351:356	the central nervous system	331:356	the central nervous system	331:356	The GCPII form expressed in the central nervous system, termed NAALADase, is responsible for the cleavage of N-acetyl-L-aspartyl-L-glutamate (NAAG) yielding free glutamate in the synaptic cleft, and is implicated in various pathologic conditions associated with glutamate excitotoxicity.
15152093	7	54	theme	predicted	1011:1019	arg1	sites					1037:1041	the predicted N-glycosylation sites	1007:1041	the predicted N-glycosylation sites	1007:1041	Analysis of the predicted N-glycosylation sites also provides evidence that these sites are critical for GCPII carboxypeptidase activity.
15152093	3	55	theme	prostate-specific	626:642	arg1	PSMA					662:665	PSMA	662:665	PSMA	662:665	The prostate form of GCPII, termed prostate-specific membrane antigen (PSMA), is up-regulated in cancer and used as an effective prostate cancer marker.
15152093	3	55	theme	prostate-specific	626:642	arg1	antigen					653:659	prostate-specific membrane antigen	626:659	prostate-specific membrane antigen (PSMA)	626:666	The prostate form of GCPII, termed prostate-specific membrane antigen (PSMA), is up-regulated in cancer and used as an effective prostate cancer marker.
15152093	3	56	theme	GCPII	612:616	arg1	marker					736:741	an effective prostate cancer marker	707:741	an effective prostate cancer marker	707:741	The prostate form of GCPII, termed prostate-specific membrane antigen (PSMA), is up-regulated in cancer and used as an effective prostate cancer marker.
15152093	3	56	theme	GCPII	612:616	arg1	form					604:607	The prostate form	591:607	The prostate form	591:607	The prostate form of GCPII, termed prostate-specific membrane antigen (PSMA), is up-regulated in cancer and used as an effective prostate cancer marker.
15152093	7	57	gly	N-glycosylation	1021:1035	arg2	sites					1037:1041	the predicted N-glycosylation sites	1007:1041	the predicted N-glycosylation sites	1007:1041	Analysis of the predicted N-glycosylation sites also provides evidence that these sites are critical for GCPII carboxypeptidase activity.
15152093	1	58	theme	Glutamate	113:121	arg1	GCPII					144:148	GCPII	144:148	GCPII	144:148	Glutamate carboxypeptidase II (GCPII) is a membrane peptidase expressed in the prostate, central and peripheral nervous system, kidney, small intestine, and tumor-associated neovasculature.
15152093	1	58	theme	Glutamate	113:121	arg1	II					140:141	Glutamate carboxypeptidase II	113:141	Glutamate carboxypeptidase II (GCPII)	113:149	Glutamate carboxypeptidase II (GCPII) is a membrane peptidase expressed in the prostate, central and peripheral nervous system, kidney, small intestine, and tumor-associated neovasculature.
15152093	1	58	theme	Glutamate	113:121	arg1	peptidase					165:173	a membrane peptidase	154:173	a membrane peptidase expressed in the prostate, central and peripheral nervous system, kidney, small intestine, and tumor-associated neovasculature	154:300	Glutamate carboxypeptidase II (GCPII) is a membrane peptidase expressed in the prostate, central and peripheral nervous system, kidney, small intestine, and tumor-associated neovasculature.
15152093	1	59	theme	nervous	225:231	arg1	system					233:238	central and peripheral nervous system	202:238	system	233:238	Glutamate carboxypeptidase II (GCPII) is a membrane peptidase expressed in the prostate, central and peripheral nervous system, kidney, small intestine, and tumor-associated neovasculature.
15152093	2	60	theme	glutamate	565:573	arg1	excitotoxicity					575:588	glutamate excitotoxicity	565:588	glutamate excitotoxicity	565:588	The GCPII form expressed in the central nervous system, termed NAALADase, is responsible for the cleavage of N-acetyl-L-aspartyl-L-glutamate (NAAG) yielding free glutamate in the synaptic cleft, and is implicated in various pathologic conditions associated with glutamate excitotoxicity.
15152093	3	61	theme	membrane	644:651	arg1	PSMA					662:665	PSMA	662:665	PSMA	662:665	The prostate form of GCPII, termed prostate-specific membrane antigen (PSMA), is up-regulated in cancer and used as an effective prostate cancer marker.
15152093	3	61	theme	membrane	644:651	arg1	antigen					653:659	prostate-specific membrane antigen	626:659	prostate-specific membrane antigen (PSMA)	626:666	The prostate form of GCPII, termed prostate-specific membrane antigen (PSMA), is up-regulated in cancer and used as an effective prostate cancer marker.
15152093	8	62	theme	structural	1407:1416	arg1	models					1418:1423	previously described structural models	1386:1423	previously described structural models of GCPII	1386:1432	We confirm that all predicted N-glycosylation sites are occupied by an oligosaccharide moiety and show that glycosylation at sites distant from the putative catalytic domain is critical for the NAAG-hydrolyzing activity of GCPII calling the validity of previously described structural models of GCPII into question.
15152093	4	63	theme	pharmaceutical	798:811	arg1	target					813:818	this important pharmaceutical target	783:818	this important pharmaceutical target	783:818	Little is known about the structure of this important pharmaceutical target.
15152093	5	64	theme	type	826:829	arg1	GCPII					852:856	GCPII	852:856	GCPII	852:856	As a type II membrane protein, GCPII is heavily glycosylated.
15152093	5	64	theme	type	826:829	arg1	protein					843:849	a type II membrane protein	824:849	a type II membrane protein	824:849	As a type II membrane protein, GCPII is heavily glycosylated.
15152093	8	65	theme	GCPII	1428:1432	arg1	models					1418:1423	previously described structural models	1386:1423	previously described structural models of GCPII	1386:1432	We confirm that all predicted N-glycosylation sites are occupied by an oligosaccharide moiety and show that glycosylation at sites distant from the putative catalytic domain is critical for the NAAG-hydrolyzing activity of GCPII calling the validity of previously described structural models of GCPII into question.
15152093	4	66	theme	important	788:796	arg1	target					813:818	this important pharmaceutical target	783:818	this important pharmaceutical target	783:818	Little is known about the structure of this important pharmaceutical target.
15152093	3	67	used	used	699:702	arg2	marker					736:741	an effective prostate cancer marker	707:741	an effective prostate cancer marker	707:741	The prostate form of GCPII, termed prostate-specific membrane antigen (PSMA), is up-regulated in cancer and used as an effective prostate cancer marker.
15152093	3	67	used	used	699:702	arg2	form					604:607	The prostate form	591:607	The prostate form	591:607	The prostate form of GCPII, termed prostate-specific membrane antigen (PSMA), is up-regulated in cancer and used as an effective prostate cancer marker.
19409386	5	0	theme	mutants	766:772	arg1	expression					728:737	a diminished plasma membrane expression	699:737	a diminished plasma membrane expression of glycosylation-defective mutants	699:772	Immunofluorescence localisation revealed a diminished plasma membrane expression of glycosylation-defective mutants.
19409386	4	1	theme	multiple	571:578	arg1	substitutions					580:592	multiple substitutions	571:592	multiple substitutions	571:592	However, multiple substitutions resulted in a decreased transport rate, leaving K(t) unchanged.
19409386	2	2	theme	laevis	466:471	arg1	oocytes					473:479	X. laevis oocytes	463:479	X. laevis oocytes	463:479	To determine the functional role of N-glycosylation, glycosylation-deficient mutants were analyzed by two-electrode voltage-clamp measurements after expression in X. laevis oocytes.
19409386	0	3	from	role	4:7	arg1	function					41:48	transport function	31:48	transport function	31:48	The role of N-glycosylation in transport function and surface targeting of the human solute carrier PAT1.
19409386	0	3	from	role	4:7	arg1	targeting					62:70	surface targeting	54:70	surface targeting	54:70	The role of N-glycosylation in transport function and surface targeting of the human solute carrier PAT1.
19409386	0	4	theme	solute	85:90	arg1	PAT1					100:103	the human solute carrier PAT1	75:103	the human solute carrier PAT1	75:103	The role of N-glycosylation in transport function and surface targeting of the human solute carrier PAT1.
19409386	5	5	theme	glycosylation-defective	742:764	arg1	mutants					766:772	glycosylation-defective mutants	742:772	glycosylation-defective mutants	742:772	Immunofluorescence localisation revealed a diminished plasma membrane expression of glycosylation-defective mutants.
19409386	0	6	theme	human	79:83	arg1	PAT1					100:103	the human solute carrier PAT1	75:103	the human solute carrier PAT1	75:103	The role of N-glycosylation in transport function and surface targeting of the human solute carrier PAT1.
19409386	2	7	from	expression	449:458	arg1	oocytes					473:479	X. laevis oocytes	463:479	X. laevis oocytes	463:479	To determine the functional role of N-glycosylation, glycosylation-deficient mutants were analyzed by two-electrode voltage-clamp measurements after expression in X. laevis oocytes.
19409386	6	8	theme	transport	826:834	arg1	function					836:843	transport function	826:843	transport function	826:843	This indicates that N-glycans are not required for transport function, but are important for membrane targeting.
19409386	0	9	theme	PAT1	100:103	arg1	function					41:48	transport function	31:48	transport function	31:48	The role of N-glycosylation in transport function and surface targeting of the human solute carrier PAT1.
19409386	0	9	theme	PAT1	100:103	arg1	targeting					62:70	surface targeting	54:70	surface targeting	54:70	The role of N-glycosylation in transport function and surface targeting of the human solute carrier PAT1.
19409386	0	10	theme	carrier	92:98	arg1	PAT1					100:103	the human solute carrier PAT1	75:103	the human solute carrier PAT1	75:103	The role of N-glycosylation in transport function and surface targeting of the human solute carrier PAT1.
19409386	0	11	theme	transport	31:39	arg1	function					41:48	transport function	31:48	transport function	31:48	The role of N-glycosylation in transport function and surface targeting of the human solute carrier PAT1.
19409386	1	12	theme	Xenopus	142:148	arg1	laevis					150:155	Xenopus laevis	142:155	the Xenopus laevis expression system	138:173	In the present study we show in the Xenopus laevis expression system that the proton-coupled amino acid transporter 1 (PAT1, SLC36A1) is glycosylated at asparagine residues N174, N183 and N470.
19409386	1	13	dep	residues	270:277	arg1	N470					294:297	N470	294:297	N470	294:297	In the present study we show in the Xenopus laevis expression system that the proton-coupled amino acid transporter 1 (PAT1, SLC36A1) is glycosylated at asparagine residues N174, N183 and N470.
19409386	1	13	dep	residues	270:277	arg1	residues					270:277	asparagine residues	259:277	asparagine residues N174, N183 and N470	259:297	In the present study we show in the Xenopus laevis expression system that the proton-coupled amino acid transporter 1 (PAT1, SLC36A1) is glycosylated at asparagine residues N174, N183 and N470.
19409386	1	13	dep	residues	270:277	arg1	N183					285:288	N183	285:288	N183	285:288	In the present study we show in the Xenopus laevis expression system that the proton-coupled amino acid transporter 1 (PAT1, SLC36A1) is glycosylated at asparagine residues N174, N183 and N470.
19409386	1	13	dep	residues	270:277	arg1	N174					279:282	N174	279:282	N174	279:282	In the present study we show in the Xenopus laevis expression system that the proton-coupled amino acid transporter 1 (PAT1, SLC36A1) is glycosylated at asparagine residues N174, N183 and N470.
19409386	1	14	theme	laevis	150:155	arg1	system					168:173	the Xenopus laevis expression system	138:173	the Xenopus laevis expression system	138:173	In the present study we show in the Xenopus laevis expression system that the proton-coupled amino acid transporter 1 (PAT1, SLC36A1) is glycosylated at asparagine residues N174, N183 and N470.
19409386	2	15	theme	voltage-clamp	416:428	arg1	measurements					430:441	two-electrode voltage-clamp measurements	402:441	two-electrode voltage-clamp measurements	402:441	To determine the functional role of N-glycosylation, glycosylation-deficient mutants were analyzed by two-electrode voltage-clamp measurements after expression in X. laevis oocytes.
19409386	1	16	theme	expression	157:166	arg1	system					168:173	the Xenopus laevis expression system	138:173	the Xenopus laevis expression system	138:173	In the present study we show in the Xenopus laevis expression system that the proton-coupled amino acid transporter 1 (PAT1, SLC36A1) is glycosylated at asparagine residues N174, N183 and N470.
19409386	0	17	theme	N-glycosylation	12:26	arg1	role					4:7	The role	0:7	The role of N-glycosylation in transport function and surface targeting of the human solute carrier PAT1.	0:104	The role of N-glycosylation in transport function and surface targeting of the human solute carrier PAT1.
19409386	3	18	theme	transport	542:550	arg1	activity					552:559	transport activity	542:559	transport activity	542:559	Single replacements of asparagine residues had no effect on transport activity.
19409386	5	19	theme	diminished	701:710	arg1	expression					728:737	a diminished plasma membrane expression	699:737	a diminished plasma membrane expression of glycosylation-defective mutants	699:772	Immunofluorescence localisation revealed a diminished plasma membrane expression of glycosylation-defective mutants.
19409386	1	20	dep	transporter	210:220	arg1	PAT1					225:228	PAT1	225:228	PAT1	225:228	In the present study we show in the Xenopus laevis expression system that the proton-coupled amino acid transporter 1 (PAT1, SLC36A1) is glycosylated at asparagine residues N174, N183 and N470.
19409386	1	20	dep	transporter	210:220	arg1	SLC36A1					231:237	SLC36A1	231:237	SLC36A1	231:237	In the present study we show in the Xenopus laevis expression system that the proton-coupled amino acid transporter 1 (PAT1, SLC36A1) is glycosylated at asparagine residues N174, N183 and N470.
19409386	3	21	theme	asparagine	505:514	arg1	residues					516:523	asparagine residues	505:523	asparagine residues	505:523	Single replacements of asparagine residues had no effect on transport activity.
19409386	2	22	theme	X.	463:464	arg1	laevis					466:471	X. laevis	463:471	X. laevis oocytes	463:479	To determine the functional role of N-glycosylation, glycosylation-deficient mutants were analyzed by two-electrode voltage-clamp measurements after expression in X. laevis oocytes.
19409386	5	23	theme	plasma	712:717	arg1	expression					728:737	a diminished plasma membrane expression	699:737	a diminished plasma membrane expression of glycosylation-defective mutants	699:772	Immunofluorescence localisation revealed a diminished plasma membrane expression of glycosylation-defective mutants.
19409386	1	24	theme	asparagine	259:268	arg1	N470					294:297	N470	294:297	N470	294:297	In the present study we show in the Xenopus laevis expression system that the proton-coupled amino acid transporter 1 (PAT1, SLC36A1) is glycosylated at asparagine residues N174, N183 and N470.
19409386	1	24	theme	asparagine	259:268	arg1	residues					270:277	asparagine residues	259:277	asparagine residues N174, N183 and N470	259:297	In the present study we show in the Xenopus laevis expression system that the proton-coupled amino acid transporter 1 (PAT1, SLC36A1) is glycosylated at asparagine residues N174, N183 and N470.
19409386	1	24	theme	asparagine	259:268	arg1	N183					285:288	N183	285:288	N183	285:288	In the present study we show in the Xenopus laevis expression system that the proton-coupled amino acid transporter 1 (PAT1, SLC36A1) is glycosylated at asparagine residues N174, N183 and N470.
19409386	1	24	theme	asparagine	259:268	arg1	N174					279:282	N174	279:282	N174	279:282	In the present study we show in the Xenopus laevis expression system that the proton-coupled amino acid transporter 1 (PAT1, SLC36A1) is glycosylated at asparagine residues N174, N183 and N470.
19409386	5	25	theme	membrane	719:726	arg1	expression					728:737	a diminished plasma membrane expression	699:737	a diminished plasma membrane expression of glycosylation-defective mutants	699:772	Immunofluorescence localisation revealed a diminished plasma membrane expression of glycosylation-defective mutants.
19409386	2	26	theme	two-electrode	402:414	arg1	measurements					430:441	two-electrode voltage-clamp measurements	402:441	two-electrode voltage-clamp measurements	402:441	To determine the functional role of N-glycosylation, glycosylation-deficient mutants were analyzed by two-electrode voltage-clamp measurements after expression in X. laevis oocytes.
19409386	1	27	theme	proton-coupled	184:197	arg1	transporter					210:220	the proton-coupled amino acid transporter 1	180:222	the proton-coupled amino acid transporter 1 (PAT1, SLC36A1)	180:238	In the present study we show in the Xenopus laevis expression system that the proton-coupled amino acid transporter 1 (PAT1, SLC36A1) is glycosylated at asparagine residues N174, N183 and N470.
19409386	3	28	contain	had	525:527	arg1	replacements					489:500	Single replacements	482:500	Single replacements of asparagine residues	482:523	Single replacements of asparagine residues had no effect on transport activity.
19409386	3	28	contain	had	525:527	arg2	effect					532:537	no effect	529:537	no effect	529:537	Single replacements of asparagine residues had no effect on transport activity.
19409386	6	29	theme	membrane	868:875	arg1	targeting					877:885	membrane targeting	868:885	membrane targeting	868:885	This indicates that N-glycans are not required for transport function, but are important for membrane targeting.
19409386	5	30	theme	Immunofluorescence	658:675	arg1	localisation					677:688	Immunofluorescence localisation	658:688	Immunofluorescence localisation	658:688	Immunofluorescence localisation revealed a diminished plasma membrane expression of glycosylation-defective mutants.
19409386	0	31	gly	N-glycosylation	12:26	arg1	transport					31:39	transport function	31:48	transport function	31:48	The role of N-glycosylation in transport function and surface targeting of the human solute carrier PAT1.
19409386	0	31	gly	N-glycosylation	12:26	arg1	surface					54:60	surface targeting	54:70	surface targeting	54:70	The role of N-glycosylation in transport function and surface targeting of the human solute carrier PAT1.
19409386	0	31	gly	N-glycosylation	12:26	arg1	PAT1					100:103	the human solute carrier PAT1	75:103	the human solute carrier PAT1	75:103	The role of N-glycosylation in transport function and surface targeting of the human solute carrier PAT1.
19409386	3	32	theme	Single	482:487	arg1	replacements					489:500	Single replacements	482:500	Single replacements of asparagine residues	482:523	Single replacements of asparagine residues had no effect on transport activity.
19409386	1	33	gly	glycosylated	243:254	arg1	transporter					210:220	the proton-coupled amino acid transporter 1	180:222	the proton-coupled amino acid transporter 1 (PAT1, SLC36A1)	180:238	In the present study we show in the Xenopus laevis expression system that the proton-coupled amino acid transporter 1 (PAT1, SLC36A1) is glycosylated at asparagine residues N174, N183 and N470.
19409386	1	33	gly	glycosylated	243:254	arg2	N183					285:288	N183	285:288	N183	285:288	In the present study we show in the Xenopus laevis expression system that the proton-coupled amino acid transporter 1 (PAT1, SLC36A1) is glycosylated at asparagine residues N174, N183 and N470.
19409386	1	33	gly	glycosylated	243:254	arg2	residues					270:277	asparagine residues	259:277	asparagine residues N174, N183 and N470	259:297	In the present study we show in the Xenopus laevis expression system that the proton-coupled amino acid transporter 1 (PAT1, SLC36A1) is glycosylated at asparagine residues N174, N183 and N470.
19409386	1	33	gly	glycosylated	243:254	arg2	N174					279:282	N174	279:282	N174	279:282	In the present study we show in the Xenopus laevis expression system that the proton-coupled amino acid transporter 1 (PAT1, SLC36A1) is glycosylated at asparagine residues N174, N183 and N470.
19409386	1	33	gly	glycosylated	243:254	arg2	N470					294:297	N470	294:297	N470	294:297	In the present study we show in the Xenopus laevis expression system that the proton-coupled amino acid transporter 1 (PAT1, SLC36A1) is glycosylated at asparagine residues N174, N183 and N470.
19409386	1	34	theme	amino	199:203	arg1	transporter					210:220	the proton-coupled amino acid transporter 1	180:222	the proton-coupled amino acid transporter 1 (PAT1, SLC36A1)	180:238	In the present study we show in the Xenopus laevis expression system that the proton-coupled amino acid transporter 1 (PAT1, SLC36A1) is glycosylated at asparagine residues N174, N183 and N470.
19409386	1	35	theme	present	113:119	arg1	study					121:125	the present study	109:125	the present study	109:125	In the present study we show in the Xenopus laevis expression system that the proton-coupled amino acid transporter 1 (PAT1, SLC36A1) is glycosylated at asparagine residues N174, N183 and N470.
19409386	1	36	theme	acid	205:208	arg1	transporter					210:220	the proton-coupled amino acid transporter 1	180:222	the proton-coupled amino acid transporter 1 (PAT1, SLC36A1)	180:238	In the present study we show in the Xenopus laevis expression system that the proton-coupled amino acid transporter 1 (PAT1, SLC36A1) is glycosylated at asparagine residues N174, N183 and N470.
19409386	2	37	theme	glycosylation-deficient	353:375	arg1	mutants					377:383	glycosylation-deficient mutants	353:383	glycosylation-deficient mutants	353:383	To determine the functional role of N-glycosylation, glycosylation-deficient mutants were analyzed by two-electrode voltage-clamp measurements after expression in X. laevis oocytes.
19409386	2	38	theme	functional	317:326	arg1	role					328:331	the functional role	313:331	the functional role of N-glycosylation	313:350	To determine the functional role of N-glycosylation, glycosylation-deficient mutants were analyzed by two-electrode voltage-clamp measurements after expression in X. laevis oocytes.
19409386	2	39	theme	N-glycosylation	336:350	arg1	role					328:331	the functional role	313:331	the functional role of N-glycosylation	313:350	To determine the functional role of N-glycosylation, glycosylation-deficient mutants were analyzed by two-electrode voltage-clamp measurements after expression in X. laevis oocytes.
19409386	4	40	theme	transport	618:626	arg1	rate					628:631	a decreased transport rate	606:631	a decreased transport rate	606:631	However, multiple substitutions resulted in a decreased transport rate, leaving K(t) unchanged.
19409386	0	41	theme	surface	54:60	arg1	targeting					62:70	surface targeting	54:70	surface targeting	54:70	The role of N-glycosylation in transport function and surface targeting of the human solute carrier PAT1.
19409386	3	42	theme	residues	516:523	arg1	replacements					489:500	Single replacements	482:500	Single replacements of asparagine residues	482:523	Single replacements of asparagine residues had no effect on transport activity.
19409386	4	43	theme	decreased	608:616	arg1	rate					628:631	a decreased transport rate	606:631	a decreased transport rate	606:631	However, multiple substitutions resulted in a decreased transport rate, leaving K(t) unchanged.
15542393	9	0	theme	cholesterol	1641:1651	arg1	traficking					1653:1662	normal cholesterol traficking	1634:1662	normal cholesterol traficking	1634:1662	Further studies on the cellular location of Asn 58 and Asn 135 mutant proteins and their respective effect on restoration of normal cholesterol traficking in NPC2-/- cells led to the conclusion that only the oligosaccharide chain carried by Asn 58 is responsible for proper targeting of NPC2 to lysosomes, and is crucial for NPC2 function.
15542393	3	1	theme	protein	696:702	arg1	protein					696:702	the NPC2 protein	687:702	the NPC2 protein	687:702	Mutation identification in NPC2 patients did not provide insights into structure-function relationships, but recent studies brought important information on the cholesterol-binding site of the NPC2 protein.
15542393	3	1	theme	protein	696:702	arg1	site					679:682	the cholesterol-binding site	655:682	the cholesterol-binding site of the NPC2 protein	655:702	Mutation identification in NPC2 patients did not provide insights into structure-function relationships, but recent studies brought important information on the cholesterol-binding site of the NPC2 protein.
15542393	1	2	theme	lysosomal/late	249:262	arg1	system					274:279	the lysosomal/late endosomal system	245:279	the lysosomal/late endosomal system	245:279	Niemann-Pick disease type C (NPC), a neurovisceral disorder characterized by accumulation of cholesterol and glycolipids in the lysosomal/late endosomal system, is due to mutations on either the NPC1 or the NPC2 genes.
15542393	4	3	theme	biological	858:867	arg1	function					869:876	biological function	858:876	biological function	858:876	The present work was focused on localization and N-glycosylation of NPC2, considering that glycosylation is often essential for targeting, stability and biological function of proteins.
15542393	5	4	dep	location	1051:1058	arg1	variance					1018:1025	variance	1018:1025	variance	1018:1025	Using immunocytofluorescence in cultured human fibroblasts, we found that the native NPC2 protein is essentially lysosomal, at variance with the late endosomal location of NPC1.
15542393	3	5	theme	NPC2	525:528	arg1	patients					530:537	NPC2 patients	525:537	NPC2 patients	525:537	Mutation identification in NPC2 patients did not provide insights into structure-function relationships, but recent studies brought important information on the cholesterol-binding site of the NPC2 protein.
15542393	9	6	from	studies	1517:1523	arg1	restoration					1619:1629	restoration	1619:1629	restoration of normal cholesterol traficking in NPC2-/- cells	1619:1679	Further studies on the cellular location of Asn 58 and Asn 135 mutant proteins and their respective effect on restoration of normal cholesterol traficking in NPC2-/- cells led to the conclusion that only the oligosaccharide chain carried by Asn 58 is responsible for proper targeting of NPC2 to lysosomes, and is crucial for NPC2 function.
15542393	9	6	from	studies	1517:1523	arg1	location					1541:1548	the cellular location	1528:1548	the cellular location of Asn 58 and Asn 135 mutant proteins	1528:1586	Further studies on the cellular location of Asn 58 and Asn 135 mutant proteins and their respective effect on restoration of normal cholesterol traficking in NPC2-/- cells led to the conclusion that only the oligosaccharide chain carried by Asn 58 is responsible for proper targeting of NPC2 to lysosomes, and is crucial for NPC2 function.
15542393	9	7	theme	traficking	1653:1662	arg1	restoration					1619:1629	restoration	1619:1629	restoration of normal cholesterol traficking in NPC2-/- cells	1619:1679	Further studies on the cellular location of Asn 58 and Asn 135 mutant proteins and their respective effect on restoration of normal cholesterol traficking in NPC2-/- cells led to the conclusion that only the oligosaccharide chain carried by Asn 58 is responsible for proper targeting of NPC2 to lysosomes, and is crucial for NPC2 function.
15542393	0	8	theme	NPC2	107:110	arg1	protein					112:118	the NPC2 protein	103:118	the NPC2 protein	103:118	Niemann-Pick type C disease: importance of N-glycosylation sites for function and cellular location of the NPC2 protein.
15542393	8	9	with	hybrid	1452:1457	arg1	chains					1501:1506	no complex chains	1490:1506	no complex chains	1490:1506	The oligosaccharidic chains were of the hybrid and/or high mannose type, with no complex chains.
15542393	9	10	theme	oligosaccharide	1717:1731	arg1	chain					1733:1737	only the oligosaccharide chain	1708:1737	only the oligosaccharide chain carried by Asn 58	1708:1755	Further studies on the cellular location of Asn 58 and Asn 135 mutant proteins and their respective effect on restoration of normal cholesterol traficking in NPC2-/- cells led to the conclusion that only the oligosaccharide chain carried by Asn 58 is responsible for proper targeting of NPC2 to lysosomes, and is crucial for NPC2 function.
15542393	9	10	theme	oligosaccharide	1717:1731	arg1	responsible					1760:1770	responsible	1760:1770	responsible	1760:1770	Further studies on the cellular location of Asn 58 and Asn 135 mutant proteins and their respective effect on restoration of normal cholesterol traficking in NPC2-/- cells led to the conclusion that only the oligosaccharide chain carried by Asn 58 is responsible for proper targeting of NPC2 to lysosomes, and is crucial for NPC2 function.
15542393	9	10	theme	oligosaccharide	1717:1731	arg1	crucial					1822:1828	crucial	1822:1828	crucial	1822:1828	Further studies on the cellular location of Asn 58 and Asn 135 mutant proteins and their respective effect on restoration of normal cholesterol traficking in NPC2-/- cells led to the conclusion that only the oligosaccharide chain carried by Asn 58 is responsible for proper targeting of NPC2 to lysosomes, and is crucial for NPC2 function.
15542393	8	11	theme	mannose	1471:1477	arg1	type					1479:1482	high mannose type	1466:1482	high mannose type	1466:1482	The oligosaccharidic chains were of the hybrid and/or high mannose type, with no complex chains.
15542393	5	12	theme	NPC1	1063:1066	arg1	location					1051:1058	the late endosomal location	1032:1058	the late endosomal location of NPC1	1032:1066	Using immunocytofluorescence in cultured human fibroblasts, we found that the native NPC2 protein is essentially lysosomal, at variance with the late endosomal location of NPC1.
15542393	9	13	theme	mutant	1572:1577	arg1	proteins					1579:1586	mutant proteins	1572:1586	mutant proteins	1572:1586	Further studies on the cellular location of Asn 58 and Asn 135 mutant proteins and their respective effect on restoration of normal cholesterol traficking in NPC2-/- cells led to the conclusion that only the oligosaccharide chain carried by Asn 58 is responsible for proper targeting of NPC2 to lysosomes, and is crucial for NPC2 function.
15542393	3	14	theme	important	630:638	arg1	information					640:650	important information	630:650	important information on the cholesterol-binding site of the NPC2 protein	630:702	Mutation identification in NPC2 patients did not provide insights into structure-function relationships, but recent studies brought important information on the cholesterol-binding site of the NPC2 protein.
15542393	1	15	theme	Niemann-Pick	121:132	arg1	disorder					172:179	a neurovisceral disorder	156:179	a neurovisceral disorder characterized by accumulation of cholesterol and glycolipids in the lysosomal/late endosomal system	156:279	Niemann-Pick disease type C (NPC), a neurovisceral disorder characterized by accumulation of cholesterol and glycolipids in the lysosomal/late endosomal system, is due to mutations on either the NPC1 or the NPC2 genes.
15542393	1	15	theme	Niemann-Pick	121:132	arg1	disease					134:140	Niemann-Pick disease	121:140	Niemann-Pick disease type C (NPC)	121:153	Niemann-Pick disease type C (NPC), a neurovisceral disorder characterized by accumulation of cholesterol and glycolipids in the lysosomal/late endosomal system, is due to mutations on either the NPC1 or the NPC2 genes.
15542393	1	16	theme	type	142:145	arg1	NPC					150:152	NPC	150:152	NPC	150:152	Niemann-Pick disease type C (NPC), a neurovisceral disorder characterized by accumulation of cholesterol and glycolipids in the lysosomal/late endosomal system, is due to mutations on either the NPC1 or the NPC2 genes.
15542393	1	16	theme	type	142:145	arg1	C					147:147	type C	142:147	Niemann-Pick disease type C (NPC)	121:153	Niemann-Pick disease type C (NPC), a neurovisceral disorder characterized by accumulation of cholesterol and glycolipids in the lysosomal/late endosomal system, is due to mutations on either the NPC1 or the NPC2 genes.
15542393	0	17	theme	sites	59:63	arg1	importance					29:38	importance	29:38	Niemann-Pick type C disease: importance of N-glycosylation sites for function and cellular location of the NPC2 protein.	0:119	Niemann-Pick type C disease: importance of N-glycosylation sites for function and cellular location of the NPC2 protein.
15542393	5	18	theme	cultured	923:930	arg1	fibroblasts					938:948	cultured human fibroblasts	923:948	cultured human fibroblasts	923:948	Using immunocytofluorescence in cultured human fibroblasts, we found that the native NPC2 protein is essentially lysosomal, at variance with the late endosomal location of NPC1.
15542393	4	19	theme	present	709:715	arg1	work					717:720	The present work	705:720	The present work	705:720	The present work was focused on localization and N-glycosylation of NPC2, considering that glycosylation is often essential for targeting, stability and biological function of proteins.
15542393	7	20	theme	NPC2	1245:1248	arg1	protein					1250:1256	The intracellular human NPC2 protein	1221:1256	The intracellular human NPC2 protein	1221:1256	The intracellular human NPC2 protein occurred as two N-glycosylated forms, with either one single oligosaccharide chain attached to Asn 58 or two oligosaccharides attached to Asn 58 and 135.
15542393	0	21	theme	cellular	82:89	arg1	location					91:98	cellular location	82:98	cellular location	82:98	Niemann-Pick type C disease: importance of N-glycosylation sites for function and cellular location of the NPC2 protein.
15542393	9	22	theme	Asn	1553:1555	arg1	location					1541:1548	the cellular location	1528:1548	the cellular location of Asn 58 and Asn 135 mutant proteins	1528:1586	Further studies on the cellular location of Asn 58 and Asn 135 mutant proteins and their respective effect on restoration of normal cholesterol traficking in NPC2-/- cells led to the conclusion that only the oligosaccharide chain carried by Asn 58 is responsible for proper targeting of NPC2 to lysosomes, and is crucial for NPC2 function.
15542393	2	23	theme	NPC2	358:361	arg1	proteins					363:370	NPC1 and NPC2 proteins	349:370	NPC1 and NPC2 proteins	349:370	Although NPC1 and NPC2 proteins appear essential for proper cellular cholesterol trafficking, their precise functions and relationship have remained elusive.
15542393	9	24	theme	NPC2	1796:1799	arg1	targeting					1783:1791	proper targeting	1776:1791	proper targeting of NPC2 to lysosomes	1776:1812	Further studies on the cellular location of Asn 58 and Asn 135 mutant proteins and their respective effect on restoration of normal cholesterol traficking in NPC2-/- cells led to the conclusion that only the oligosaccharide chain carried by Asn 58 is responsible for proper targeting of NPC2 to lysosomes, and is crucial for NPC2 function.
15542393	2	25	theme	NPC1	349:352	arg1	proteins					363:370	NPC1 and NPC2 proteins	349:370	NPC1 and NPC2 proteins	349:370	Although NPC1 and NPC2 proteins appear essential for proper cellular cholesterol trafficking, their precise functions and relationship have remained elusive.
15542393	0	26	theme	Niemann-Pick	0:11	arg1	disease					20:26	Niemann-Pick type C disease	0:26	Niemann-Pick type C disease: importance of N-glycosylation sites for function and cellular location of the NPC2 protein.	0:119	Niemann-Pick type C disease: importance of N-glycosylation sites for function and cellular location of the NPC2 protein.
15542393	1	27	theme	endosomal	264:272	arg1	system					274:279	the lysosomal/late endosomal system	245:279	the lysosomal/late endosomal system	245:279	Niemann-Pick disease type C (NPC), a neurovisceral disorder characterized by accumulation of cholesterol and glycolipids in the lysosomal/late endosomal system, is due to mutations on either the NPC1 or the NPC2 genes.
15542393	5	28	theme	native	969:974	arg1	protein					981:987	the native NPC2 protein	965:987	the native NPC2 protein	965:987	Using immunocytofluorescence in cultured human fibroblasts, we found that the native NPC2 protein is essentially lysosomal, at variance with the late endosomal location of NPC1.
15542393	5	28	theme	native	969:974	arg1	lysosomal					1004:1012	lysosomal	1004:1012	lysosomal	1004:1012	Using immunocytofluorescence in cultured human fibroblasts, we found that the native NPC2 protein is essentially lysosomal, at variance with the late endosomal location of NPC1.
15542393	6	29	theme	cDNA	1083:1086	arg1	mutants					1088:1094	cDNA mutants	1083:1094	cDNA mutants affecting each of the three potential NPC2 N-glycosylation sites in NPC2-/- fibroblasts	1083:1182	Expression of cDNA mutants affecting each of the three potential NPC2 N-glycosylation sites in NPC2-/- fibroblasts showed that only two sites are used.
15542393	2	30	theme	cellular	400:407	arg1	trafficking					421:431	proper cellular cholesterol trafficking	393:431	proper cellular cholesterol trafficking	393:431	Although NPC1 and NPC2 proteins appear essential for proper cellular cholesterol trafficking, their precise functions and relationship have remained elusive.
15542393	1	31	dep	disease	134:140	arg1	NPC					150:152	NPC	150:152	NPC	150:152	Niemann-Pick disease type C (NPC), a neurovisceral disorder characterized by accumulation of cholesterol and glycolipids in the lysosomal/late endosomal system, is due to mutations on either the NPC1 or the NPC2 genes.
15542393	1	31	dep	disease	134:140	arg1	C					147:147	type C	142:147	Niemann-Pick disease type C (NPC)	121:153	Niemann-Pick disease type C (NPC), a neurovisceral disorder characterized by accumulation of cholesterol and glycolipids in the lysosomal/late endosomal system, is due to mutations on either the NPC1 or the NPC2 genes.
15542393	0	32	theme	C	18:18	arg1	disease					20:26	Niemann-Pick type C disease	0:26	Niemann-Pick type C disease: importance of N-glycosylation sites for function and cellular location of the NPC2 protein.	0:119	Niemann-Pick type C disease: importance of N-glycosylation sites for function and cellular location of the NPC2 protein.
15542393	7	33	gly	N-glycosylated	1274:1287	arg1	forms					1289:1293	two N-glycosylated forms	1270:1293	two N-glycosylated forms	1270:1293	The intracellular human NPC2 protein occurred as two N-glycosylated forms, with either one single oligosaccharide chain attached to Asn 58 or two oligosaccharides attached to Asn 58 and 135.
15542393	3	34	theme	cholesterol-binding	659:677	arg1	protein					696:702	the NPC2 protein	687:702	the NPC2 protein	687:702	Mutation identification in NPC2 patients did not provide insights into structure-function relationships, but recent studies brought important information on the cholesterol-binding site of the NPC2 protein.
15542393	3	34	theme	cholesterol-binding	659:677	arg1	site					679:682	the cholesterol-binding site	655:682	the cholesterol-binding site of the NPC2 protein	655:702	Mutation identification in NPC2 patients did not provide insights into structure-function relationships, but recent studies brought important information on the cholesterol-binding site of the NPC2 protein.
15542393	5	35	theme	endosomal	1041:1049	arg1	location					1051:1058	the late endosomal location	1032:1058	the late endosomal location of NPC1	1032:1066	Using immunocytofluorescence in cultured human fibroblasts, we found that the native NPC2 protein is essentially lysosomal, at variance with the late endosomal location of NPC1.
15542393	7	36	theme	oligosaccharide	1319:1333	arg1	chain					1335:1339	one single oligosaccharide chain	1308:1339	one single oligosaccharide chain attached to Asn 58	1308:1358	The intracellular human NPC2 protein occurred as two N-glycosylated forms, with either one single oligosaccharide chain attached to Asn 58 or two oligosaccharides attached to Asn 58 and 135.
15542393	9	37	theme	NPC2	1834:1837	arg1	function					1839:1846	NPC2 function	1834:1846	NPC2 function	1834:1846	Further studies on the cellular location of Asn 58 and Asn 135 mutant proteins and their respective effect on restoration of normal cholesterol traficking in NPC2-/- cells led to the conclusion that only the oligosaccharide chain carried by Asn 58 is responsible for proper targeting of NPC2 to lysosomes, and is crucial for NPC2 function.
15542393	3	38	theme	NPC2	691:694	arg1	protein					696:702	the NPC2 protein	687:702	the NPC2 protein	687:702	Mutation identification in NPC2 patients did not provide insights into structure-function relationships, but recent studies brought important information on the cholesterol-binding site of the NPC2 protein.
15542393	6	39	from	sites	1155:1159	arg1	fibroblasts					1172:1182	NPC2-/- fibroblasts	1164:1182	NPC2-/- fibroblasts	1164:1182	Expression of cDNA mutants affecting each of the three potential NPC2 N-glycosylation sites in NPC2-/- fibroblasts showed that only two sites are used.
15542393	6	40	theme	NPC2	1134:1137	arg1	sites					1155:1159	the three potential NPC2 N-glycosylation sites	1114:1159	the three potential NPC2 N-glycosylation sites in NPC2-/- fibroblasts	1114:1182	Expression of cDNA mutants affecting each of the three potential NPC2 N-glycosylation sites in NPC2-/- fibroblasts showed that only two sites are used.
15542393	3	41	theme	Mutation	498:505	arg1	identification					507:520	Mutation identification	498:520	Mutation identification in NPC2 patients	498:537	Mutation identification in NPC2 patients did not provide insights into structure-function relationships, but recent studies brought important information on the cholesterol-binding site of the NPC2 protein.
15542393	1	42	theme	cholesterol	214:224	arg1	accumulation					198:209	accumulation	198:209	accumulation of cholesterol and glycolipids in the lysosomal/late endosomal system	198:279	Niemann-Pick disease type C (NPC), a neurovisceral disorder characterized by accumulation of cholesterol and glycolipids in the lysosomal/late endosomal system, is due to mutations on either the NPC1 or the NPC2 genes.
15542393	0	43	gly	N-glycosylation	43:57	arg2	sites					59:63	N-glycosylation sites	43:63	N-glycosylation sites	43:63	Niemann-Pick type C disease: importance of N-glycosylation sites for function and cellular location of the NPC2 protein.
15542393	1	44	from	mutations	292:300	arg1	NPC1					316:319	the NPC1	312:319	the NPC1	312:319	Niemann-Pick disease type C (NPC), a neurovisceral disorder characterized by accumulation of cholesterol and glycolipids in the lysosomal/late endosomal system, is due to mutations on either the NPC1 or the NPC2 genes.
15542393	1	44	from	mutations	292:300	arg1	genes					333:337	the NPC2 genes	324:337	the NPC2 genes	324:337	Niemann-Pick disease type C (NPC), a neurovisceral disorder characterized by accumulation of cholesterol and glycolipids in the lysosomal/late endosomal system, is due to mutations on either the NPC1 or the NPC2 genes.
15542393	1	45	theme	glycolipids	230:240	arg1	accumulation					198:209	accumulation	198:209	accumulation of cholesterol and glycolipids in the lysosomal/late endosomal system	198:279	Niemann-Pick disease type C (NPC), a neurovisceral disorder characterized by accumulation of cholesterol and glycolipids in the lysosomal/late endosomal system, is due to mutations on either the NPC1 or the NPC2 genes.
15542393	4	46	theme	proteins	881:888	arg1	function					869:876	biological function	858:876	biological function	858:876	The present work was focused on localization and N-glycosylation of NPC2, considering that glycosylation is often essential for targeting, stability and biological function of proteins.
15542393	4	46	theme	proteins	881:888	arg1	targeting					833:841	targeting	833:841	targeting	833:841	The present work was focused on localization and N-glycosylation of NPC2, considering that glycosylation is often essential for targeting, stability and biological function of proteins.
15542393	4	46	theme	proteins	881:888	arg1	stability					844:852	stability	844:852	stability	844:852	The present work was focused on localization and N-glycosylation of NPC2, considering that glycosylation is often essential for targeting, stability and biological function of proteins.
15542393	3	47	from	information	640:650	arg1	protein					696:702	the NPC2 protein	687:702	the NPC2 protein	687:702	Mutation identification in NPC2 patients did not provide insights into structure-function relationships, but recent studies brought important information on the cholesterol-binding site of the NPC2 protein.
15542393	3	47	from	information	640:650	arg1	site					679:682	the cholesterol-binding site	655:682	the cholesterol-binding site of the NPC2 protein	655:702	Mutation identification in NPC2 patients did not provide insights into structure-function relationships, but recent studies brought important information on the cholesterol-binding site of the NPC2 protein.
15542393	9	48	theme	NPC2-/-	1667:1673	arg1	cells					1675:1679	NPC2-/- cells	1667:1679	NPC2-/- cells	1667:1679	Further studies on the cellular location of Asn 58 and Asn 135 mutant proteins and their respective effect on restoration of normal cholesterol traficking in NPC2-/- cells led to the conclusion that only the oligosaccharide chain carried by Asn 58 is responsible for proper targeting of NPC2 to lysosomes, and is crucial for NPC2 function.
15542393	9	49	theme	cellular	1532:1539	arg1	location					1541:1548	the cellular location	1528:1548	the cellular location of Asn 58 and Asn 135 mutant proteins	1528:1586	Further studies on the cellular location of Asn 58 and Asn 135 mutant proteins and their respective effect on restoration of normal cholesterol traficking in NPC2-/- cells led to the conclusion that only the oligosaccharide chain carried by Asn 58 is responsible for proper targeting of NPC2 to lysosomes, and is crucial for NPC2 function.
15542393	3	50	from	identification	507:520	arg1	patients					530:537	NPC2 patients	525:537	NPC2 patients	525:537	Mutation identification in NPC2 patients did not provide insights into structure-function relationships, but recent studies brought important information on the cholesterol-binding site of the NPC2 protein.
15542393	0	51	theme	protein	112:118	arg1	function					69:76	function	69:76	function	69:76	Niemann-Pick type C disease: importance of N-glycosylation sites for function and cellular location of the NPC2 protein.
15542393	0	51	theme	protein	112:118	arg1	location					91:98	cellular location	82:98	cellular location	82:98	Niemann-Pick type C disease: importance of N-glycosylation sites for function and cellular location of the NPC2 protein.
15542393	1	52	theme	neurovisceral	158:170	arg1	disorder					172:179	a neurovisceral disorder	156:179	a neurovisceral disorder characterized by accumulation of cholesterol and glycolipids in the lysosomal/late endosomal system	156:279	Niemann-Pick disease type C (NPC), a neurovisceral disorder characterized by accumulation of cholesterol and glycolipids in the lysosomal/late endosomal system, is due to mutations on either the NPC1 or the NPC2 genes.
15542393	1	52	theme	neurovisceral	158:170	arg1	disease					134:140	Niemann-Pick disease	121:140	Niemann-Pick disease type C (NPC)	121:153	Niemann-Pick disease type C (NPC), a neurovisceral disorder characterized by accumulation of cholesterol and glycolipids in the lysosomal/late endosomal system, is due to mutations on either the NPC1 or the NPC2 genes.
15542393	8	53	theme	high	1466:1469	arg1	type					1479:1482	high mannose type	1466:1482	high mannose type	1466:1482	The oligosaccharidic chains were of the hybrid and/or high mannose type, with no complex chains.
15542393	6	54	theme	NPC2-/-	1164:1170	arg1	fibroblasts					1172:1182	NPC2-/- fibroblasts	1164:1182	NPC2-/- fibroblasts	1164:1182	Expression of cDNA mutants affecting each of the three potential NPC2 N-glycosylation sites in NPC2-/- fibroblasts showed that only two sites are used.
15542393	5	55	with	lysosomal	1004:1012	arg1	location					1051:1058	the late endosomal location	1032:1058	the late endosomal location of NPC1	1032:1066	Using immunocytofluorescence in cultured human fibroblasts, we found that the native NPC2 protein is essentially lysosomal, at variance with the late endosomal location of NPC1.
15542393	3	56	theme	structure-function	569:586	arg1	relationships					588:600	structure-function relationships	569:600	structure-function relationships	569:600	Mutation identification in NPC2 patients did not provide insights into structure-function relationships, but recent studies brought important information on the cholesterol-binding site of the NPC2 protein.
15542393	1	57	from	accumulation	198:209	arg1	system					274:279	the lysosomal/late endosomal system	245:279	the lysosomal/late endosomal system	245:279	Niemann-Pick disease type C (NPC), a neurovisceral disorder characterized by accumulation of cholesterol and glycolipids in the lysosomal/late endosomal system, is due to mutations on either the NPC1 or the NPC2 genes.
15542393	9	58	theme	Further	1509:1515	arg1	studies					1517:1523	Further studies	1509:1523	Further studies on the cellular location of Asn 58 and Asn 135 mutant proteins	1509:1586	Further studies on the cellular location of Asn 58 and Asn 135 mutant proteins and their respective effect on restoration of normal cholesterol traficking in NPC2-/- cells led to the conclusion that only the oligosaccharide chain carried by Asn 58 is responsible for proper targeting of NPC2 to lysosomes, and is crucial for NPC2 function.
15542393	8	59	theme	complex	1493:1499	arg1	chains					1501:1506	no complex chains	1490:1506	no complex chains	1490:1506	The oligosaccharidic chains were of the hybrid and/or high mannose type, with no complex chains.
15542393	9	60	dep	Asn	1553:1555	arg1	proteins					1579:1586	mutant proteins	1572:1586	mutant proteins	1572:1586	Further studies on the cellular location of Asn 58 and Asn 135 mutant proteins and their respective effect on restoration of normal cholesterol traficking in NPC2-/- cells led to the conclusion that only the oligosaccharide chain carried by Asn 58 is responsible for proper targeting of NPC2 to lysosomes, and is crucial for NPC2 function.
15542393	7	61	attach	attached	1384:1391	arg1	Asn					1396:1398	Asn 58	1396:1401	Asn 58	1396:1401	The intracellular human NPC2 protein occurred as two N-glycosylated forms, with either one single oligosaccharide chain attached to Asn 58 or two oligosaccharides attached to Asn 58 and 135.
15542393	7	61	attach	attached	1384:1391	arg2	oligosaccharides					1367:1382	two oligosaccharides	1363:1382	two oligosaccharides attached to Asn 58 and 135	1363:1409	The intracellular human NPC2 protein occurred as two N-glycosylated forms, with either one single oligosaccharide chain attached to Asn 58 or two oligosaccharides attached to Asn 58 and 135.
15542393	7	61	attach	attached	1384:1391	arg1	135					1407:1409	135	1407:1409	135	1407:1409	The intracellular human NPC2 protein occurred as two N-glycosylated forms, with either one single oligosaccharide chain attached to Asn 58 or two oligosaccharides attached to Asn 58 and 135.
15542393	3	62	theme	recent	607:612	arg1	studies					614:620	recent studies	607:620	recent studies	607:620	Mutation identification in NPC2 patients did not provide insights into structure-function relationships, but recent studies brought important information on the cholesterol-binding site of the NPC2 protein.
15542393	5	63	from	immunocytofluorescence	897:918	arg1	fibroblasts					938:948	cultured human fibroblasts	923:948	cultured human fibroblasts	923:948	Using immunocytofluorescence in cultured human fibroblasts, we found that the native NPC2 protein is essentially lysosomal, at variance with the late endosomal location of NPC1.
15542393	7	64	theme	intracellular	1225:1237	arg1	protein					1250:1256	The intracellular human NPC2 protein	1221:1256	The intracellular human NPC2 protein	1221:1256	The intracellular human NPC2 protein occurred as two N-glycosylated forms, with either one single oligosaccharide chain attached to Asn 58 or two oligosaccharides attached to Asn 58 and 135.
15542393	7	65	theme	human	1239:1243	arg1	protein					1250:1256	The intracellular human NPC2 protein	1221:1256	The intracellular human NPC2 protein	1221:1256	The intracellular human NPC2 protein occurred as two N-glycosylated forms, with either one single oligosaccharide chain attached to Asn 58 or two oligosaccharides attached to Asn 58 and 135.
15542393	5	66	theme	human	932:936	arg1	fibroblasts					938:948	cultured human fibroblasts	923:948	cultured human fibroblasts	923:948	Using immunocytofluorescence in cultured human fibroblasts, we found that the native NPC2 protein is essentially lysosomal, at variance with the late endosomal location of NPC1.
15542393	9	67	theme	proper	1776:1781	arg1	targeting					1783:1791	proper targeting	1776:1791	proper targeting of NPC2 to lysosomes	1776:1812	Further studies on the cellular location of Asn 58 and Asn 135 mutant proteins and their respective effect on restoration of normal cholesterol traficking in NPC2-/- cells led to the conclusion that only the oligosaccharide chain carried by Asn 58 is responsible for proper targeting of NPC2 to lysosomes, and is crucial for NPC2 function.
15542393	4	68	theme	NPC2	773:776	arg1	N-glycosylation					754:768	N-glycosylation	754:768	N-glycosylation	754:768	The present work was focused on localization and N-glycosylation of NPC2, considering that glycosylation is often essential for targeting, stability and biological function of proteins.
15542393	4	68	theme	NPC2	773:776	arg1	localization					737:748	localization	737:748	localization	737:748	The present work was focused on localization and N-glycosylation of NPC2, considering that glycosylation is often essential for targeting, stability and biological function of proteins.
15542393	4	69	gly	N-glycosylation	754:768	arg1	NPC2					773:776	NPC2	773:776	NPC2	773:776	The present work was focused on localization and N-glycosylation of NPC2, considering that glycosylation is often essential for targeting, stability and biological function of proteins.
15542393	1	70	theme	NPC2	328:331	arg1	genes					333:337	the NPC2 genes	324:337	the NPC2 genes	324:337	Niemann-Pick disease type C (NPC), a neurovisceral disorder characterized by accumulation of cholesterol and glycolipids in the lysosomal/late endosomal system, is due to mutations on either the NPC1 or the NPC2 genes.
15542393	0	71	theme	type	13:16	arg1	disease					20:26	Niemann-Pick type C disease	0:26	Niemann-Pick type C disease: importance of N-glycosylation sites for function and cellular location of the NPC2 protein.	0:119	Niemann-Pick type C disease: importance of N-glycosylation sites for function and cellular location of the NPC2 protein.
15542393	9	72	theme	Asn	1564:1566	arg1	location					1541:1548	the cellular location	1528:1548	the cellular location of Asn 58 and Asn 135 mutant proteins	1528:1586	Further studies on the cellular location of Asn 58 and Asn 135 mutant proteins and their respective effect on restoration of normal cholesterol traficking in NPC2-/- cells led to the conclusion that only the oligosaccharide chain carried by Asn 58 is responsible for proper targeting of NPC2 to lysosomes, and is crucial for NPC2 function.
15542393	9	73	from	restoration	1619:1629	arg1	cells					1675:1679	NPC2-/- cells	1667:1679	NPC2-/- cells	1667:1679	Further studies on the cellular location of Asn 58 and Asn 135 mutant proteins and their respective effect on restoration of normal cholesterol traficking in NPC2-/- cells led to the conclusion that only the oligosaccharide chain carried by Asn 58 is responsible for proper targeting of NPC2 to lysosomes, and is crucial for NPC2 function.
15542393	6	74	theme	mutants	1088:1094	arg1	Expression					1069:1078	Expression	1069:1078	Expression of cDNA mutants affecting each of the three potential NPC2 N-glycosylation sites in NPC2-/- fibroblasts	1069:1182	Expression of cDNA mutants affecting each of the three potential NPC2 N-glycosylation sites in NPC2-/- fibroblasts showed that only two sites are used.
15542393	2	75	theme	cholesterol	409:419	arg1	trafficking					421:431	proper cellular cholesterol trafficking	393:431	proper cellular cholesterol trafficking	393:431	Although NPC1 and NPC2 proteins appear essential for proper cellular cholesterol trafficking, their precise functions and relationship have remained elusive.
15542393	6	76	gly	N-glycosylation	1139:1153	arg2	sites					1155:1159	the three potential NPC2 N-glycosylation sites	1114:1159	the three potential NPC2 N-glycosylation sites in NPC2-/- fibroblasts	1114:1182	Expression of cDNA mutants affecting each of the three potential NPC2 N-glycosylation sites in NPC2-/- fibroblasts showed that only two sites are used.
15542393	6	76	gly	N-glycosylation	1139:1153	arg2	three					1118:1122	three	1118:1122	three	1118:1122	Expression of cDNA mutants affecting each of the three potential NPC2 N-glycosylation sites in NPC2-/- fibroblasts showed that only two sites are used.
15542393	5	77	theme	NPC2	976:979	arg1	protein					981:987	the native NPC2 protein	965:987	the native NPC2 protein	965:987	Using immunocytofluorescence in cultured human fibroblasts, we found that the native NPC2 protein is essentially lysosomal, at variance with the late endosomal location of NPC1.
15542393	5	77	theme	NPC2	976:979	arg1	lysosomal					1004:1012	lysosomal	1004:1012	lysosomal	1004:1012	Using immunocytofluorescence in cultured human fibroblasts, we found that the native NPC2 protein is essentially lysosomal, at variance with the late endosomal location of NPC1.
15542393	9	78	from	effect	1609:1614	arg1	restoration					1619:1629	restoration	1619:1629	restoration of normal cholesterol traficking in NPC2-/- cells	1619:1679	Further studies on the cellular location of Asn 58 and Asn 135 mutant proteins and their respective effect on restoration of normal cholesterol traficking in NPC2-/- cells led to the conclusion that only the oligosaccharide chain carried by Asn 58 is responsible for proper targeting of NPC2 to lysosomes, and is crucial for NPC2 function.
15542393	9	78	from	effect	1609:1614	arg1	location					1541:1548	the cellular location	1528:1548	the cellular location of Asn 58 and Asn 135 mutant proteins	1528:1586	Further studies on the cellular location of Asn 58 and Asn 135 mutant proteins and their respective effect on restoration of normal cholesterol traficking in NPC2-/- cells led to the conclusion that only the oligosaccharide chain carried by Asn 58 is responsible for proper targeting of NPC2 to lysosomes, and is crucial for NPC2 function.
15542393	2	79	theme	proper	393:398	arg1	trafficking					421:431	proper cellular cholesterol trafficking	393:431	proper cellular cholesterol trafficking	393:431	Although NPC1 and NPC2 proteins appear essential for proper cellular cholesterol trafficking, their precise functions and relationship have remained elusive.
15542393	7	80	attach	attached	1341:1348	arg1	Asn					1353:1355	Asn 58	1353:1358	Asn 58	1353:1358	The intracellular human NPC2 protein occurred as two N-glycosylated forms, with either one single oligosaccharide chain attached to Asn 58 or two oligosaccharides attached to Asn 58 and 135.
15542393	7	80	attach	attached	1341:1348	arg2	chain					1335:1339	one single oligosaccharide chain	1308:1339	one single oligosaccharide chain attached to Asn 58	1308:1358	The intracellular human NPC2 protein occurred as two N-glycosylated forms, with either one single oligosaccharide chain attached to Asn 58 or two oligosaccharides attached to Asn 58 and 135.
15542393	6	81	theme	potential	1124:1132	arg1	sites					1155:1159	the three potential NPC2 N-glycosylation sites	1114:1159	the three potential NPC2 N-glycosylation sites in NPC2-/- fibroblasts	1114:1182	Expression of cDNA mutants affecting each of the three potential NPC2 N-glycosylation sites in NPC2-/- fibroblasts showed that only two sites are used.
15542393	4	82	gly	glycosylation	796:808	arg1	proteins					881:888	proteins	881:888	proteins	881:888	The present work was focused on localization and N-glycosylation of NPC2, considering that glycosylation is often essential for targeting, stability and biological function of proteins.
15542393	5	83	theme	late	1036:1039	arg1	location					1051:1058	the late endosomal location	1032:1058	the late endosomal location of NPC1	1032:1066	Using immunocytofluorescence in cultured human fibroblasts, we found that the native NPC2 protein is essentially lysosomal, at variance with the late endosomal location of NPC1.
15542393	7	84	theme	single	1312:1317	arg1	chain					1335:1339	one single oligosaccharide chain	1308:1339	one single oligosaccharide chain attached to Asn 58	1308:1358	The intracellular human NPC2 protein occurred as two N-glycosylated forms, with either one single oligosaccharide chain attached to Asn 58 or two oligosaccharides attached to Asn 58 and 135.
15542393	2	85	theme	precise	440:446	arg1	functions					448:456	their precise functions	434:456	their precise functions	434:456	Although NPC1 and NPC2 proteins appear essential for proper cellular cholesterol trafficking, their precise functions and relationship have remained elusive.
15542393	0	86	theme	N-glycosylation	43:57	arg1	sites					59:63	N-glycosylation sites	43:63	N-glycosylation sites	43:63	Niemann-Pick type C disease: importance of N-glycosylation sites for function and cellular location of the NPC2 protein.
15542393	9	87	theme	respective	1598:1607	arg1	effect					1609:1614	their respective effect	1592:1614	their respective effect on restoration of normal cholesterol traficking in NPC2-/- cells	1592:1679	Further studies on the cellular location of Asn 58 and Asn 135 mutant proteins and their respective effect on restoration of normal cholesterol traficking in NPC2-/- cells led to the conclusion that only the oligosaccharide chain carried by Asn 58 is responsible for proper targeting of NPC2 to lysosomes, and is crucial for NPC2 function.
15542393	8	88	theme	oligosaccharidic	1416:1431	arg1	chains					1433:1438	The oligosaccharidic chains	1412:1438	The oligosaccharidic chains	1412:1438	The oligosaccharidic chains were of the hybrid and/or high mannose type, with no complex chains.
15542393	6	89	used	used	1215:1218	arg2	sites					1205:1209	only two sites	1196:1209	only two sites	1196:1209	Expression of cDNA mutants affecting each of the three potential NPC2 N-glycosylation sites in NPC2-/- fibroblasts showed that only two sites are used.
15542393	9	90	theme	normal	1634:1639	arg1	traficking					1653:1662	normal cholesterol traficking	1634:1662	normal cholesterol traficking	1634:1662	Further studies on the cellular location of Asn 58 and Asn 135 mutant proteins and their respective effect on restoration of normal cholesterol traficking in NPC2-/- cells led to the conclusion that only the oligosaccharide chain carried by Asn 58 is responsible for proper targeting of NPC2 to lysosomes, and is crucial for NPC2 function.
15542393	0	91	dep	disease	20:26	arg1	importance					29:38	importance	29:38	Niemann-Pick type C disease: importance of N-glycosylation sites for function and cellular location of the NPC2 protein.	0:119	Niemann-Pick type C disease: importance of N-glycosylation sites for function and cellular location of the NPC2 protein.
15542393	6	92	theme	N-glycosylation	1139:1153	arg1	sites					1155:1159	the three potential NPC2 N-glycosylation sites	1114:1159	the three potential NPC2 N-glycosylation sites in NPC2-/- fibroblasts	1114:1182	Expression of cDNA mutants affecting each of the three potential NPC2 N-glycosylation sites in NPC2-/- fibroblasts showed that only two sites are used.
15542393	7	93	theme	N-glycosylated	1274:1287	arg1	forms					1289:1293	two N-glycosylated forms	1270:1293	two N-glycosylated forms	1270:1293	The intracellular human NPC2 protein occurred as two N-glycosylated forms, with either one single oligosaccharide chain attached to Asn 58 or two oligosaccharides attached to Asn 58 and 135.
17591618	11	0	with	structures	1700:1709	arg1	distribution					1727:1738	a relative distribution	1716:1738	a relative distribution varying between 45% for Asn804 and 75% for Asn864	1716:1788	Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077 are glycosylated essentially by diantennary disialylated structures with a relative distribution varying between 45% for Asn804 and 75% for Asn864.
17591618	7	1	theme	complex	1185:1191	arg1	glycans					1236:1242	complex, diantennary disialylated, non-fucosylated glycans	1185:1242	glycans	1236:1242	Quantitative analysis showed that CFH is mainly glycosylated by complex, diantennary disialylated, non-fucosylated glycans.
17591618	0	2	theme	pathway	173:179	arg1	regulation					143:152	the regulation	139:152	the regulation of the alternative pathway of the complement system	139:204	Site-specific N-glycan characterization of human complement factor H. Human complement factor H (CFH) is a plasma glycoprotein involved in the regulation of the alternative pathway of the complement system.
17591618	8	3	gly	non-fucosylated	1289:1303	arg1	oligosaccharides					1305:1320	Disialylated fucosylated and monosialylated non-fucosylated oligosaccharides	1245:1320	Disialylated fucosylated and monosialylated non-fucosylated oligosaccharides	1245:1320	Disialylated fucosylated and monosialylated non-fucosylated oligosaccharides were also identified.
17591618	8	4	theme	fucosylated	1258:1268	arg1	oligosaccharides					1305:1320	Disialylated fucosylated and monosialylated non-fucosylated oligosaccharides	1245:1320	Disialylated fucosylated and monosialylated non-fucosylated oligosaccharides	1245:1320	Disialylated fucosylated and monosialylated non-fucosylated oligosaccharides were also identified.
17591618	3	5	attach	present	414:420	arg2	we					411:412	we	411:412	we	411:412	In the current study, we present a quantitative glycosylation analysis of CFH using capillary electrophoresis and a complete site-specific N-glycan characterization using matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) and liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESIMS/MS).
17591618	3	5	attach	present	414:420	arg1	study					404:408	the current study	392:408	the current study	392:408	In the current study, we present a quantitative glycosylation analysis of CFH using capillary electrophoresis and a complete site-specific N-glycan characterization using matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) and liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESIMS/MS).
17591618	13	6	theme	sialylation	1946:1956	arg1	level					1958:1962	the sialylation level	1942:1962	the sialylation level along with the amount of triantennary structures	1942:2011	Interestingly, the sialylation level along with the amount of triantennary structures decreases from the N- to the C-terminal side of the protein.
17591618	10	7	theme	CFH	1561:1563	arg1	sequence					1549:1556	the NGSP sequence	1540:1556	the NGSP sequence of CFH	1540:1563	The absence of glycosylation at Asn199 of the NGSP sequence of CFH is shown.
17591618	3	8	theme	site-specific	514:526	arg1	characterization					537:552	a complete site-specific N-glycan characterization	503:552	a complete site-specific N-glycan characterization using matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) and liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESIMS/MS)	503:718	In the current study, we present a quantitative glycosylation analysis of CFH using capillary electrophoresis and a complete site-specific N-glycan characterization using matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) and liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESIMS/MS).
17591618	5	9	theme	diantennary	930:940	arg1	glycans					955:961	diantennary disialylated glycans	930:961	diantennary disialylated glycans of 2204 Da	930:972	This mass difference is consistent with CFH glycosylation by diantennary disialylated glycans of 2204 Da on eight sites.
17591618	8	10	theme	monosialylated	1274:1287	arg1	oligosaccharides					1305:1320	Disialylated fucosylated and monosialylated non-fucosylated oligosaccharides	1245:1320	Disialylated fucosylated and monosialylated non-fucosylated oligosaccharides	1245:1320	Disialylated fucosylated and monosialylated non-fucosylated oligosaccharides were also identified.
17591618	5	11	gly	glycosylation	913:925	arg1	sites					983:987	eight sites	977:987	eight sites	977:987	This mass difference is consistent with CFH glycosylation by diantennary disialylated glycans of 2204 Da on eight sites.
17591618	9	12	theme	site-specific	1459:1471	arg1	identification					1482:1495	site-specific N-glycan identification	1459:1495	site-specific N-glycan identification	1459:1495	MS analysis allowed complete characterization of the protein backbone, verification of the glycosylation sites and site-specific N-glycan identification.
17591618	0	13	theme	system	199:204	arg1	pathway					173:179	the alternative pathway	157:179	the alternative pathway of the complement system	157:204	Site-specific N-glycan characterization of human complement factor H. Human complement factor H (CFH) is a plasma glycoprotein involved in the regulation of the alternative pathway of the complement system.
17591618	10	14	theme	sequence	1549:1556	arg1	Asn199					1530:1535	Asn199	1530:1535	Asn199 of the NGSP sequence of CFH	1530:1563	The absence of glycosylation at Asn199 of the NGSP sequence of CFH is shown.
17591618	3	15	theme	desorption/ionization	582:602	arg1	MALDI-TOF					620:628	matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) and liquid chromatography-electrospray ionization tandem mass spectrometry	560:704	MALDI-TOF	620:628	In the current study, we present a quantitative glycosylation analysis of CFH using capillary electrophoresis and a complete site-specific N-glycan characterization using matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) and liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESIMS/MS).
17591618	3	15	theme	desorption/ionization	582:602	arg1	LC-ESIMS/MS					707:717	LC-ESIMS/MS	707:717	LC-ESIMS/MS	707:717	In the current study, we present a quantitative glycosylation analysis of CFH using capillary electrophoresis and a complete site-specific N-glycan characterization using matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) and liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESIMS/MS).
17591618	2	16	contain	containing	340:349	arg1	CFH					310:312	CFH	310:312	CFH	310:312	CFH is a 155-kDa glycoprotein containing nine potential N-glycosylation sites.
17591618	2	16	contain	containing	340:349	arg2	sites					382:386	nine potential N-glycosylation sites	351:386	nine potential N-glycosylation sites	351:386	CFH is a 155-kDa glycoprotein containing nine potential N-glycosylation sites.
17591618	2	16	contain	containing	340:349	arg1	glycoprotein					327:338	a 155-kDa glycoprotein	317:338	a 155-kDa glycoprotein containing nine potential N-glycosylation sites	317:386	CFH is a 155-kDa glycoprotein containing nine potential N-glycosylation sites.
17591618	3	17	theme	matrix-assisted	560:574	arg1	MALDI-TOF					620:628	matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) and liquid chromatography-electrospray ionization tandem mass spectrometry	560:704	MALDI-TOF	620:628	In the current study, we present a quantitative glycosylation analysis of CFH using capillary electrophoresis and a complete site-specific N-glycan characterization using matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) and liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESIMS/MS).
17591618	3	17	theme	matrix-assisted	560:574	arg1	LC-ESIMS/MS					707:717	LC-ESIMS/MS	707:717	LC-ESIMS/MS	707:717	In the current study, we present a quantitative glycosylation analysis of CFH using capillary electrophoresis and a complete site-specific N-glycan characterization using matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) and liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESIMS/MS).
17591618	6	18	theme	endoglycosidase	1015:1029	arg1	H					1031:1031	endoglycosidase H	1015:1031	endoglycosidase H (Endo H) deglycosylation	1015:1056	CFH was not sensitive to endoglycosidase H (Endo H) deglycosylation, indicating the absence of hybrid and oligomannose structures.
17591618	6	18	theme	endoglycosidase	1015:1029	arg1	H					1039:1039	Endo H	1034:1039	Endo H	1034:1039	CFH was not sensitive to endoglycosidase H (Endo H) deglycosylation, indicating the absence of hybrid and oligomannose structures.
17591618	12	19	gly	non-fucosylated	1873:1887	arg1	structures					1889:1898	triantennary trisialylated fucosylated and non-fucosylated structures	1830:1898	triantennary trisialylated fucosylated and non-fucosylated structures	1830:1898	Diantennary monosialylated glycans and triantennary trisialylated fucosylated and non-fucosylated structures have also been identified.
17591618	7	20	theme	Quantitative	1121:1132	arg1	analysis					1134:1141	Quantitative analysis	1121:1141	Quantitative analysis	1121:1141	Quantitative analysis showed that CFH is mainly glycosylated by complex, diantennary disialylated, non-fucosylated glycans.
17591618	9	21	theme	N-glycan	1473:1480	arg1	identification					1482:1495	site-specific N-glycan identification	1459:1495	site-specific N-glycan identification	1459:1495	MS analysis allowed complete characterization of the protein backbone, verification of the glycosylation sites and site-specific N-glycan identification.
17591618	12	22	theme	triantennary	1830:1841	arg1	structures					1889:1898	triantennary trisialylated fucosylated and non-fucosylated structures	1830:1898	triantennary trisialylated fucosylated and non-fucosylated structures	1830:1898	Diantennary monosialylated glycans and triantennary trisialylated fucosylated and non-fucosylated structures have also been identified.
17591618	1	23	from	deficiency	209:218	arg1	CFH					223:225	CFH	223:225	CFH	223:225	A deficiency in CFH is a cause of severe pathologies like atypical haemolytic uraemic syndrome (aHUS).
17591618	3	24	theme	ionization	670:679	arg1	spectrometry					693:704	matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) and liquid chromatography-electrospray ionization tandem mass spectrometry	560:704	spectrometry	693:704	In the current study, we present a quantitative glycosylation analysis of CFH using capillary electrophoresis and a complete site-specific N-glycan characterization using matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) and liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESIMS/MS).
17591618	12	25	theme	fucosylated	1857:1867	arg1	structures					1889:1898	triantennary trisialylated fucosylated and non-fucosylated structures	1830:1898	triantennary trisialylated fucosylated and non-fucosylated structures	1830:1898	Diantennary monosialylated glycans and triantennary trisialylated fucosylated and non-fucosylated structures have also been identified.
17591618	9	26	gly	glycosylation	1435:1447	arg2	sites					1449:1453	the glycosylation sites	1431:1453	the glycosylation sites	1431:1453	MS analysis allowed complete characterization of the protein backbone, verification of the glycosylation sites and site-specific N-glycan identification.
17591618	0	27	theme	Human	70:74	arg1	CFH					97:99	CFH	97:99	CFH	97:99	Site-specific N-glycan characterization of human complement factor H. Human complement factor H (CFH) is a plasma glycoprotein involved in the regulation of the alternative pathway of the complement system.
17591618	0	27	theme	Human	70:74	arg1	H					94:94	Human complement factor H	70:94	human complement factor H. Human complement factor H (CFH)	43:100	Site-specific N-glycan characterization of human complement factor H. Human complement factor H (CFH) is a plasma glycoprotein involved in the regulation of the alternative pathway of the complement system.
17591618	9	28	theme	backbone	1405:1412	arg1	verification					1415:1426	verification	1415:1426	verification of the glycosylation sites	1415:1453	MS analysis allowed complete characterization of the protein backbone, verification of the glycosylation sites and site-specific N-glycan identification.
17591618	9	28	theme	backbone	1405:1412	arg1	identification					1482:1495	site-specific N-glycan identification	1459:1495	site-specific N-glycan identification	1459:1495	MS analysis allowed complete characterization of the protein backbone, verification of the glycosylation sites and site-specific N-glycan identification.
17591618	9	28	theme	backbone	1405:1412	arg1	characterization					1373:1388	complete characterization	1364:1388	complete characterization of the protein backbone	1364:1412	MS analysis allowed complete characterization of the protein backbone, verification of the glycosylation sites and site-specific N-glycan identification.
17591618	3	29	theme	liquid	635:640	arg1	spectrometry					693:704	matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) and liquid chromatography-electrospray ionization tandem mass spectrometry	560:704	spectrometry	693:704	In the current study, we present a quantitative glycosylation analysis of CFH using capillary electrophoresis and a complete site-specific N-glycan characterization using matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) and liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESIMS/MS).
17591618	12	30	theme	Diantennary	1791:1801	arg1	glycans					1818:1824	Diantennary monosialylated glycans	1791:1824	Diantennary monosialylated glycans	1791:1824	Diantennary monosialylated glycans and triantennary trisialylated fucosylated and non-fucosylated structures have also been identified.
17591618	0	31	theme	factor	87:92	arg1	CFH					97:99	CFH	97:99	CFH	97:99	Site-specific N-glycan characterization of human complement factor H. Human complement factor H (CFH) is a plasma glycoprotein involved in the regulation of the alternative pathway of the complement system.
17591618	0	31	theme	factor	87:92	arg1	H					94:94	Human complement factor H	70:94	human complement factor H. Human complement factor H (CFH)	43:100	Site-specific N-glycan characterization of human complement factor H. Human complement factor H (CFH) is a plasma glycoprotein involved in the regulation of the alternative pathway of the complement system.
17591618	12	32	gly	trisialylated	1843:1855	arg1	structures					1889:1898	triantennary trisialylated fucosylated and non-fucosylated structures	1830:1898	triantennary trisialylated fucosylated and non-fucosylated structures	1830:1898	Diantennary monosialylated glycans and triantennary trisialylated fucosylated and non-fucosylated structures have also been identified.
17591618	4	33	theme	post-translational	829:846	arg1	modification					848:859	the major post-translational modification	819:859	the major post-translational modification of CFH	819:866	A 17.9-kDa mass decrease, observed after glycosidase treatment, indicated that N-glycosylation is the major post-translational modification of CFH.
17591618	4	33	theme	post-translational	829:846	arg1	N-glycosylation					800:814	N-glycosylation	800:814	N-glycosylation	800:814	A 17.9-kDa mass decrease, observed after glycosidase treatment, indicated that N-glycosylation is the major post-translational modification of CFH.
17591618	2	34	theme	N-glycosylation	366:380	arg1	sites					382:386	nine potential N-glycosylation sites	351:386	nine potential N-glycosylation sites	351:386	CFH is a 155-kDa glycoprotein containing nine potential N-glycosylation sites.
17591618	9	35	theme	sites	1449:1453	arg1	verification					1415:1426	verification	1415:1426	verification of the glycosylation sites	1415:1453	MS analysis allowed complete characterization of the protein backbone, verification of the glycosylation sites and site-specific N-glycan identification.
17591618	9	35	theme	sites	1449:1453	arg1	identification					1482:1495	site-specific N-glycan identification	1459:1495	site-specific N-glycan identification	1459:1495	MS analysis allowed complete characterization of the protein backbone, verification of the glycosylation sites and site-specific N-glycan identification.
17591618	9	35	theme	sites	1449:1453	arg1	characterization					1373:1388	complete characterization	1364:1388	complete characterization of the protein backbone	1364:1412	MS analysis allowed complete characterization of the protein backbone, verification of the glycosylation sites and site-specific N-glycan identification.
17591618	12	36	gly	monosialylated	1803:1816	arg1	glycans					1818:1824	Diantennary monosialylated glycans	1791:1824	Diantennary monosialylated glycans	1791:1824	Diantennary monosialylated glycans and triantennary trisialylated fucosylated and non-fucosylated structures have also been identified.
17591618	11	37	gly	disialylated	1687:1698	arg1	structures					1700:1709	diantennary disialylated structures	1675:1709	diantennary disialylated structures with a relative distribution varying between 45% for Asn804 and 75% for Asn864	1675:1788	Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077 are glycosylated essentially by diantennary disialylated structures with a relative distribution varying between 45% for Asn804 and 75% for Asn864.
17591618	3	38	theme	current	396:402	arg1	study					404:408	the current study	392:408	the current study	392:408	In the current study, we present a quantitative glycosylation analysis of CFH using capillary electrophoresis and a complete site-specific N-glycan characterization using matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) and liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESIMS/MS).
17591618	5	39	theme	mass	874:877	arg1	difference					879:888	This mass difference	869:888	This mass difference	869:888	This mass difference is consistent with CFH glycosylation by diantennary disialylated glycans of 2204 Da on eight sites.
17591618	1	40	theme	severe	241:246	arg1	pathologies					248:258	severe pathologies	241:258	severe pathologies like atypical haemolytic uraemic syndrome (aHUS)	241:307	A deficiency in CFH is a cause of severe pathologies like atypical haemolytic uraemic syndrome (aHUS).
17591618	3	41	theme	quantitative	424:435	arg1	analysis					451:458	a quantitative glycosylation analysis	422:458	a quantitative glycosylation analysis of CFH using capillary electrophoresis	422:497	In the current study, we present a quantitative glycosylation analysis of CFH using capillary electrophoresis and a complete site-specific N-glycan characterization using matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) and liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESIMS/MS).
17591618	6	42	theme	oligomannose	1096:1107	arg1	structures					1109:1118	oligomannose structures	1096:1118	oligomannose structures	1096:1118	CFH was not sensitive to endoglycosidase H (Endo H) deglycosylation, indicating the absence of hybrid and oligomannose structures.
17591618	5	43	with	consistent	893:902	arg1	glycosylation					913:925	CFH glycosylation	909:925	CFH glycosylation by diantennary disialylated glycans of 2204 Da on eight sites	909:987	This mass difference is consistent with CFH glycosylation by diantennary disialylated glycans of 2204 Da on eight sites.
17591618	3	44	gly	glycosylation	437:449	arg1	CFH					463:465	CFH	463:465	CFH using capillary electrophoresis	463:497	In the current study, we present a quantitative glycosylation analysis of CFH using capillary electrophoresis and a complete site-specific N-glycan characterization using matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) and liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESIMS/MS).
17591618	13	45	theme	structures	2002:2011	arg1	amount					1979:1984	the amount	1975:1984	the amount of triantennary structures	1975:2011	Interestingly, the sialylation level along with the amount of triantennary structures decreases from the N- to the C-terminal side of the protein.
17591618	13	45	theme	structures	2002:2011	arg1	structures					2002:2011	triantennary structures	1989:2011	triantennary structures	1989:2011	Interestingly, the sialylation level along with the amount of triantennary structures decreases from the N- to the C-terminal side of the protein.
17591618	0	46	theme	human	43:47	arg1	factor					60:65	human complement factor	43:65	human complement factor H. Human complement factor H (CFH)	43:100	Site-specific N-glycan characterization of human complement factor H. Human complement factor H (CFH) is a plasma glycoprotein involved in the regulation of the alternative pathway of the complement system.
17591618	1	47	theme	haemolytic	274:283	arg1	aHUS					303:306	aHUS	303:306	aHUS	303:306	A deficiency in CFH is a cause of severe pathologies like atypical haemolytic uraemic syndrome (aHUS).
17591618	1	47	theme	haemolytic	274:283	arg1	syndrome					293:300	atypical haemolytic uraemic syndrome	265:300	atypical haemolytic uraemic syndrome (aHUS)	265:307	A deficiency in CFH is a cause of severe pathologies like atypical haemolytic uraemic syndrome (aHUS).
17591618	0	48	dep	factor	60:65	arg1	H.					67:68	H.	67:68	H.	67:68	Site-specific N-glycan characterization of human complement factor H. Human complement factor H (CFH) is a plasma glycoprotein involved in the regulation of the alternative pathway of the complement system.
17591618	6	49	theme	hybrid	1085:1090	arg1	absence					1074:1080	the absence	1070:1080	the absence of hybrid and oligomannose structures	1070:1118	CFH was not sensitive to endoglycosidase H (Endo H) deglycosylation, indicating the absence of hybrid and oligomannose structures.
17591618	3	50	theme	mass	688:691	arg1	spectrometry					693:704	matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) and liquid chromatography-electrospray ionization tandem mass spectrometry	560:704	spectrometry	693:704	In the current study, we present a quantitative glycosylation analysis of CFH using capillary electrophoresis and a complete site-specific N-glycan characterization using matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) and liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESIMS/MS).
17591618	7	51	gly	disialylated	1206:1217	arg1	glycans					1236:1242	complex, diantennary disialylated, non-fucosylated glycans	1185:1242	glycans	1236:1242	Quantitative analysis showed that CFH is mainly glycosylated by complex, diantennary disialylated, non-fucosylated glycans.
17591618	11	52	theme	relative	1718:1725	arg1	distribution					1727:1738	a relative distribution	1716:1738	a relative distribution varying between 45% for Asn804 and 75% for Asn864	1716:1788	Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077 are glycosylated essentially by diantennary disialylated structures with a relative distribution varying between 45% for Asn804 and 75% for Asn864.
17591618	3	53	theme	CFH	463:465	arg1	analysis					451:458	a quantitative glycosylation analysis	422:458	a quantitative glycosylation analysis of CFH using capillary electrophoresis	422:497	In the current study, we present a quantitative glycosylation analysis of CFH using capillary electrophoresis and a complete site-specific N-glycan characterization using matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) and liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESIMS/MS).
17591618	3	53	theme	CFH	463:465	arg1	characterization					537:552	a complete site-specific N-glycan characterization	503:552	a complete site-specific N-glycan characterization using matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) and liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESIMS/MS)	503:718	In the current study, we present a quantitative glycosylation analysis of CFH using capillary electrophoresis and a complete site-specific N-glycan characterization using matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) and liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESIMS/MS).
17591618	7	54	theme	disialylated	1206:1217	arg1	glycans					1236:1242	complex, diantennary disialylated, non-fucosylated glycans	1185:1242	glycans	1236:1242	Quantitative analysis showed that CFH is mainly glycosylated by complex, diantennary disialylated, non-fucosylated glycans.
17591618	11	55	theme	diantennary	1675:1685	arg1	structures					1700:1709	diantennary disialylated structures	1675:1709	diantennary disialylated structures with a relative distribution varying between 45% for Asn804 and 75% for Asn864	1675:1788	Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077 are glycosylated essentially by diantennary disialylated structures with a relative distribution varying between 45% for Asn804 and 75% for Asn864.
17591618	0	56	theme	alternative	161:171	arg1	pathway					173:179	the alternative pathway	157:179	the alternative pathway of the complement system	157:204	Site-specific N-glycan characterization of human complement factor H. Human complement factor H (CFH) is a plasma glycoprotein involved in the regulation of the alternative pathway of the complement system.
17591618	8	57	gly	fucosylated	1258:1268	arg1	oligosaccharides					1305:1320	Disialylated fucosylated and monosialylated non-fucosylated oligosaccharides	1245:1320	Disialylated fucosylated and monosialylated non-fucosylated oligosaccharides	1245:1320	Disialylated fucosylated and monosialylated non-fucosylated oligosaccharides were also identified.
17591618	3	58	theme	capillary	473:481	arg1	electrophoresis					483:497	capillary electrophoresis	473:497	capillary electrophoresis	473:497	In the current study, we present a quantitative glycosylation analysis of CFH using capillary electrophoresis and a complete site-specific N-glycan characterization using matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) and liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESIMS/MS).
17591618	8	59	gly	monosialylated	1274:1287	arg1	oligosaccharides					1305:1320	Disialylated fucosylated and monosialylated non-fucosylated oligosaccharides	1245:1320	Disialylated fucosylated and monosialylated non-fucosylated oligosaccharides	1245:1320	Disialylated fucosylated and monosialylated non-fucosylated oligosaccharides were also identified.
17591618	3	60	theme	N-glycan	528:535	arg1	characterization					537:552	a complete site-specific N-glycan characterization	503:552	a complete site-specific N-glycan characterization using matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) and liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESIMS/MS)	503:718	In the current study, we present a quantitative glycosylation analysis of CFH using capillary electrophoresis and a complete site-specific N-glycan characterization using matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) and liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESIMS/MS).
17591618	5	61	gly	disialylated	942:953	arg1	glycans					955:961	diantennary disialylated glycans	930:961	diantennary disialylated glycans of 2204 Da	930:972	This mass difference is consistent with CFH glycosylation by diantennary disialylated glycans of 2204 Da on eight sites.
17591618	0	62	theme	complement	188:197	arg1	system					199:204	the complement system	184:204	the complement system	184:204	Site-specific N-glycan characterization of human complement factor H. Human complement factor H (CFH) is a plasma glycoprotein involved in the regulation of the alternative pathway of the complement system.
17591618	3	63	theme	complete	505:512	arg1	characterization					537:552	a complete site-specific N-glycan characterization	503:552	a complete site-specific N-glycan characterization using matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) and liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESIMS/MS)	503:718	In the current study, we present a quantitative glycosylation analysis of CFH using capillary electrophoresis and a complete site-specific N-glycan characterization using matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) and liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESIMS/MS).
17591618	8	64	theme	Disialylated	1245:1256	arg1	oligosaccharides					1305:1320	Disialylated fucosylated and monosialylated non-fucosylated oligosaccharides	1245:1320	Disialylated fucosylated and monosialylated non-fucosylated oligosaccharides	1245:1320	Disialylated fucosylated and monosialylated non-fucosylated oligosaccharides were also identified.
17591618	12	65	theme	non-fucosylated	1873:1887	arg1	structures					1889:1898	triantennary trisialylated fucosylated and non-fucosylated structures	1830:1898	triantennary trisialylated fucosylated and non-fucosylated structures	1830:1898	Diantennary monosialylated glycans and triantennary trisialylated fucosylated and non-fucosylated structures have also been identified.
17591618	11	66	theme	disialylated	1687:1698	arg1	structures					1700:1709	diantennary disialylated structures	1675:1709	diantennary disialylated structures with a relative distribution varying between 45% for Asn804 and 75% for Asn864	1675:1788	Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077 are glycosylated essentially by diantennary disialylated structures with a relative distribution varying between 45% for Asn804 and 75% for Asn864.
17591618	3	67	theme	laser	576:580	arg1	MALDI-TOF					620:628	matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) and liquid chromatography-electrospray ionization tandem mass spectrometry	560:704	MALDI-TOF	620:628	In the current study, we present a quantitative glycosylation analysis of CFH using capillary electrophoresis and a complete site-specific N-glycan characterization using matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) and liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESIMS/MS).
17591618	3	67	theme	laser	576:580	arg1	LC-ESIMS/MS					707:717	LC-ESIMS/MS	707:717	LC-ESIMS/MS	707:717	In the current study, we present a quantitative glycosylation analysis of CFH using capillary electrophoresis and a complete site-specific N-glycan characterization using matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) and liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESIMS/MS).
17591618	5	68	theme	disialylated	942:953	arg1	glycans					955:961	diantennary disialylated glycans	930:961	diantennary disialylated glycans of 2204 Da	930:972	This mass difference is consistent with CFH glycosylation by diantennary disialylated glycans of 2204 Da on eight sites.
17591618	6	69	theme	Endo	1034:1037	arg1	H					1031:1031	endoglycosidase H	1015:1031	endoglycosidase H (Endo H) deglycosylation	1015:1056	CFH was not sensitive to endoglycosidase H (Endo H) deglycosylation, indicating the absence of hybrid and oligomannose structures.
17591618	6	69	theme	Endo	1034:1037	arg1	H					1039:1039	Endo H	1034:1039	Endo H	1034:1039	CFH was not sensitive to endoglycosidase H (Endo H) deglycosylation, indicating the absence of hybrid and oligomannose structures.
17591618	0	70	theme	factor	60:65	arg1	characterization					23:38	Site-specific N-glycan characterization	0:38	Site-specific N-glycan characterization of human complement factor H. Human complement factor H (CFH)	0:100	Site-specific N-glycan characterization of human complement factor H. Human complement factor H (CFH) is a plasma glycoprotein involved in the regulation of the alternative pathway of the complement system.
17591618	0	70	theme	factor	60:65	arg1	glycoprotein					114:125	a plasma glycoprotein	105:125	a plasma glycoprotein involved in the regulation of the alternative pathway of the complement system	105:204	Site-specific N-glycan characterization of human complement factor H. Human complement factor H (CFH) is a plasma glycoprotein involved in the regulation of the alternative pathway of the complement system.
17591618	0	71	theme	plasma	107:112	arg1	glycoprotein					114:125	a plasma glycoprotein	105:125	a plasma glycoprotein involved in the regulation of the alternative pathway of the complement system	105:204	Site-specific N-glycan characterization of human complement factor H. Human complement factor H (CFH) is a plasma glycoprotein involved in the regulation of the alternative pathway of the complement system.
17591618	0	71	theme	plasma	107:112	arg1	characterization					23:38	Site-specific N-glycan characterization	0:38	Site-specific N-glycan characterization of human complement factor H. Human complement factor H (CFH)	0:100	Site-specific N-glycan characterization of human complement factor H. Human complement factor H (CFH) is a plasma glycoprotein involved in the regulation of the alternative pathway of the complement system.
17591618	10	72	theme	NGSP	1544:1547	arg1	sequence					1549:1556	the NGSP sequence	1540:1556	the NGSP sequence of CFH	1540:1563	The absence of glycosylation at Asn199 of the NGSP sequence of CFH is shown.
17591618	8	73	theme	non-fucosylated	1289:1303	arg1	oligosaccharides					1305:1320	Disialylated fucosylated and monosialylated non-fucosylated oligosaccharides	1245:1320	Disialylated fucosylated and monosialylated non-fucosylated oligosaccharides	1245:1320	Disialylated fucosylated and monosialylated non-fucosylated oligosaccharides were also identified.
17591618	6	74	theme	H	1031:1031	arg1	deglycosylation					1042:1056	endoglycosidase H (Endo H) deglycosylation	1015:1056	endoglycosidase H (Endo H) deglycosylation	1015:1056	CFH was not sensitive to endoglycosidase H (Endo H) deglycosylation, indicating the absence of hybrid and oligomannose structures.
17591618	5	75	theme	CFH	909:911	arg1	glycosylation					913:925	CFH glycosylation	909:925	CFH glycosylation by diantennary disialylated glycans of 2204 Da on eight sites	909:987	This mass difference is consistent with CFH glycosylation by diantennary disialylated glycans of 2204 Da on eight sites.
17591618	7	76	gly	glycosylated	1169:1180	arg1	CFH					1155:1157	CFH	1155:1157	CFH	1155:1157	Quantitative analysis showed that CFH is mainly glycosylated by complex, diantennary disialylated, non-fucosylated glycans.
17591618	9	77	theme	complete	1364:1371	arg1	characterization					1373:1388	complete characterization	1364:1388	complete characterization of the protein backbone	1364:1412	MS analysis allowed complete characterization of the protein backbone, verification of the glycosylation sites and site-specific N-glycan identification.
17591618	3	78	theme	time-of-flight	604:617	arg1	MALDI-TOF					620:628	matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) and liquid chromatography-electrospray ionization tandem mass spectrometry	560:704	MALDI-TOF	620:628	In the current study, we present a quantitative glycosylation analysis of CFH using capillary electrophoresis and a complete site-specific N-glycan characterization using matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) and liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESIMS/MS).
17591618	3	78	theme	time-of-flight	604:617	arg1	LC-ESIMS/MS					707:717	LC-ESIMS/MS	707:717	LC-ESIMS/MS	707:717	In the current study, we present a quantitative glycosylation analysis of CFH using capillary electrophoresis and a complete site-specific N-glycan characterization using matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) and liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESIMS/MS).
17591618	5	79	from	glycosylation	913:925	arg1	sites					983:987	eight sites	977:987	eight sites	977:987	This mass difference is consistent with CFH glycosylation by diantennary disialylated glycans of 2204 Da on eight sites.
17591618	3	80	theme	chromatography-electrospray	642:668	arg1	spectrometry					693:704	matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) and liquid chromatography-electrospray ionization tandem mass spectrometry	560:704	spectrometry	693:704	In the current study, we present a quantitative glycosylation analysis of CFH using capillary electrophoresis and a complete site-specific N-glycan characterization using matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) and liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESIMS/MS).
17591618	0	81	gly	glycoprotein	114:125	arg1	glycoprotein					114:125	a plasma glycoprotein	105:125	a plasma glycoprotein involved in the regulation of the alternative pathway of the complement system	105:204	Site-specific N-glycan characterization of human complement factor H. Human complement factor H (CFH) is a plasma glycoprotein involved in the regulation of the alternative pathway of the complement system.
17591618	0	81	gly	glycoprotein	114:125	arg1	characterization					23:38	Site-specific N-glycan characterization	0:38	Site-specific N-glycan characterization of human complement factor H. Human complement factor H (CFH)	0:100	Site-specific N-glycan characterization of human complement factor H. Human complement factor H (CFH) is a plasma glycoprotein involved in the regulation of the alternative pathway of the complement system.
17591618	4	82	theme	glycosidase	762:772	arg1	treatment					774:782	glycosidase treatment	762:782	glycosidase treatment	762:782	A 17.9-kDa mass decrease, observed after glycosidase treatment, indicated that N-glycosylation is the major post-translational modification of CFH.
17591618	13	83	theme	protein	2065:2071	arg1	side					2053:2056	the C-terminal side	2038:2056	the C-terminal side of the protein	2038:2071	Interestingly, the sialylation level along with the amount of triantennary structures decreases from the N- to the C-terminal side of the protein.
17591618	0	84	theme	complement	76:85	arg1	CFH					97:99	CFH	97:99	CFH	97:99	Site-specific N-glycan characterization of human complement factor H. Human complement factor H (CFH) is a plasma glycoprotein involved in the regulation of the alternative pathway of the complement system.
17591618	0	84	theme	complement	76:85	arg1	H					94:94	Human complement factor H	70:94	human complement factor H. Human complement factor H (CFH)	43:100	Site-specific N-glycan characterization of human complement factor H. Human complement factor H (CFH) is a plasma glycoprotein involved in the regulation of the alternative pathway of the complement system.
17591618	9	85	theme	protein	1397:1403	arg1	backbone					1405:1412	the protein backbone	1393:1412	the protein backbone	1393:1412	MS analysis allowed complete characterization of the protein backbone, verification of the glycosylation sites and site-specific N-glycan identification.
17591618	12	86	theme	trisialylated	1843:1855	arg1	structures					1889:1898	triantennary trisialylated fucosylated and non-fucosylated structures	1830:1898	triantennary trisialylated fucosylated and non-fucosylated structures	1830:1898	Diantennary monosialylated glycans and triantennary trisialylated fucosylated and non-fucosylated structures have also been identified.
17591618	4	87	theme	17.9-kDa	723:730	arg1	decrease					737:744	A 17.9-kDa mass decrease	721:744	A 17.9-kDa mass decrease	721:744	A 17.9-kDa mass decrease, observed after glycosidase treatment, indicated that N-glycosylation is the major post-translational modification of CFH.
17591618	5	88	theme	Da	971:972	arg1	glycans					955:961	diantennary disialylated glycans	930:961	diantennary disialylated glycans of 2204 Da	930:972	This mass difference is consistent with CFH glycosylation by diantennary disialylated glycans of 2204 Da on eight sites.
17591618	13	89	theme	C-terminal	2042:2051	arg1	side					2053:2056	the C-terminal side	2038:2056	the C-terminal side of the protein	2038:2071	Interestingly, the sialylation level along with the amount of triantennary structures decreases from the N- to the C-terminal side of the protein.
17591618	9	90	theme	MS	1344:1345	arg1	analysis					1347:1354	MS analysis	1344:1354	MS analysis	1344:1354	MS analysis allowed complete characterization of the protein backbone, verification of the glycosylation sites and site-specific N-glycan identification.
17591618	11	91	gly	glycosylated	1647:1658	arg1	Asn893					1615:1620	Asn893	1615:1620	Asn893	1615:1620	Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077 are glycosylated essentially by diantennary disialylated structures with a relative distribution varying between 45% for Asn804 and 75% for Asn864.
17591618	11	91	gly	glycosylated	1647:1658	arg1	Asn1011					1623:1629	Asn1011	1623:1629	Asn1011	1623:1629	Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077 are glycosylated essentially by diantennary disialylated structures with a relative distribution varying between 45% for Asn804 and 75% for Asn864.
17591618	11	91	gly	glycosylated	1647:1658	arg1	Asn511					1575:1580	Asn511	1575:1580	Asn511	1575:1580	Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077 are glycosylated essentially by diantennary disialylated structures with a relative distribution varying between 45% for Asn804 and 75% for Asn864.
17591618	11	91	gly	glycosylated	1647:1658	arg1	Asn804					1599:1604	Asn804	1599:1604	Asn804	1599:1604	Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077 are glycosylated essentially by diantennary disialylated structures with a relative distribution varying between 45% for Asn804 and 75% for Asn864.
17591618	11	91	gly	glycosylated	1647:1658	arg1	Asn1077					1635:1641	Asn1077	1635:1641	Asn1077	1635:1641	Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077 are glycosylated essentially by diantennary disialylated structures with a relative distribution varying between 45% for Asn804 and 75% for Asn864.
17591618	11	91	gly	glycosylated	1647:1658	arg1	Asn700					1583:1588	Asn700	1583:1588	Asn700	1583:1588	Asn511, Asn700, Asn784, Asn804, Asn864, Asn893, Asn1011 and Asn1077 are glycosylated essentially by diantennary disialylated structures with a relative distribution varying between 45% for Asn804 and 75% for Asn864.
17591618	12	92	theme	monosialylated	1803:1816	arg1	glycans					1818:1824	Diantennary monosialylated glycans	1791:1824	Diantennary monosialylated glycans	1791:1824	Diantennary monosialylated glycans and triantennary trisialylated fucosylated and non-fucosylated structures have also been identified.
17591618	12	93	gly	fucosylated	1857:1867	arg1	structures					1889:1898	triantennary trisialylated fucosylated and non-fucosylated structures	1830:1898	triantennary trisialylated fucosylated and non-fucosylated structures	1830:1898	Diantennary monosialylated glycans and triantennary trisialylated fucosylated and non-fucosylated structures have also been identified.
17591618	0	94	theme	Site-specific	0:12	arg1	characterization					23:38	Site-specific N-glycan characterization	0:38	Site-specific N-glycan characterization of human complement factor H. Human complement factor H (CFH)	0:100	Site-specific N-glycan characterization of human complement factor H. Human complement factor H (CFH) is a plasma glycoprotein involved in the regulation of the alternative pathway of the complement system.
17591618	0	94	theme	Site-specific	0:12	arg1	glycoprotein					114:125	a plasma glycoprotein	105:125	a plasma glycoprotein involved in the regulation of the alternative pathway of the complement system	105:204	Site-specific N-glycan characterization of human complement factor H. Human complement factor H (CFH) is a plasma glycoprotein involved in the regulation of the alternative pathway of the complement system.
17591618	9	95	theme	glycosylation	1435:1447	arg1	sites					1449:1453	the glycosylation sites	1431:1453	the glycosylation sites	1431:1453	MS analysis allowed complete characterization of the protein backbone, verification of the glycosylation sites and site-specific N-glycan identification.
17591618	2	96	gly	N-glycosylation	366:380	arg2	sites					382:386	nine potential N-glycosylation sites	351:386	nine potential N-glycosylation sites	351:386	CFH is a 155-kDa glycoprotein containing nine potential N-glycosylation sites.
17591618	2	96	gly	N-glycosylation	366:380	arg2	nine					351:354	nine	351:354	nine	351:354	CFH is a 155-kDa glycoprotein containing nine potential N-glycosylation sites.
17591618	4	97	theme	major	823:827	arg1	modification					848:859	the major post-translational modification	819:859	the major post-translational modification of CFH	819:866	A 17.9-kDa mass decrease, observed after glycosidase treatment, indicated that N-glycosylation is the major post-translational modification of CFH.
17591618	4	97	theme	major	823:827	arg1	N-glycosylation					800:814	N-glycosylation	800:814	N-glycosylation	800:814	A 17.9-kDa mass decrease, observed after glycosidase treatment, indicated that N-glycosylation is the major post-translational modification of CFH.
17591618	2	98	theme	potential	356:364	arg1	sites					382:386	nine potential N-glycosylation sites	351:386	nine potential N-glycosylation sites	351:386	CFH is a 155-kDa glycoprotein containing nine potential N-glycosylation sites.
17591618	0	99	theme	N-glycan	14:21	arg1	characterization					23:38	Site-specific N-glycan characterization	0:38	Site-specific N-glycan characterization of human complement factor H. Human complement factor H (CFH)	0:100	Site-specific N-glycan characterization of human complement factor H. Human complement factor H (CFH) is a plasma glycoprotein involved in the regulation of the alternative pathway of the complement system.
17591618	0	99	theme	N-glycan	14:21	arg1	glycoprotein					114:125	a plasma glycoprotein	105:125	a plasma glycoprotein involved in the regulation of the alternative pathway of the complement system	105:204	Site-specific N-glycan characterization of human complement factor H. Human complement factor H (CFH) is a plasma glycoprotein involved in the regulation of the alternative pathway of the complement system.
17591618	1	100	theme	pathologies	248:258	arg1	cause					232:236	a cause	230:236	a cause of severe pathologies like atypical haemolytic uraemic syndrome (aHUS)	230:307	A deficiency in CFH is a cause of severe pathologies like atypical haemolytic uraemic syndrome (aHUS).
17591618	1	100	theme	pathologies	248:258	arg1	deficiency					209:218	A deficiency	207:218	A deficiency in CFH	207:225	A deficiency in CFH is a cause of severe pathologies like atypical haemolytic uraemic syndrome (aHUS).
17591618	6	101	theme	structures	1109:1118	arg1	absence					1074:1080	the absence	1070:1080	the absence of hybrid and oligomannose structures	1070:1118	CFH was not sensitive to endoglycosidase H (Endo H) deglycosylation, indicating the absence of hybrid and oligomannose structures.
17591618	2	102	gly	glycoprotein	327:338	arg1	CFH					310:312	CFH	310:312	CFH	310:312	CFH is a 155-kDa glycoprotein containing nine potential N-glycosylation sites.
17591618	2	102	gly	glycoprotein	327:338	arg1	glycoprotein					327:338	a 155-kDa glycoprotein	317:338	a 155-kDa glycoprotein containing nine potential N-glycosylation sites	317:386	CFH is a 155-kDa glycoprotein containing nine potential N-glycosylation sites.
17591618	13	103	theme	triantennary	1989:2000	arg1	structures					2002:2011	triantennary structures	1989:2011	triantennary structures	1989:2011	Interestingly, the sialylation level along with the amount of triantennary structures decreases from the N- to the C-terminal side of the protein.
17591618	3	104	theme	glycosylation	437:449	arg1	analysis					451:458	a quantitative glycosylation analysis	422:458	a quantitative glycosylation analysis of CFH using capillary electrophoresis	422:497	In the current study, we present a quantitative glycosylation analysis of CFH using capillary electrophoresis and a complete site-specific N-glycan characterization using matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) and liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESIMS/MS).
17591618	0	105	theme	complement	49:58	arg1	factor					60:65	human complement factor	43:65	human complement factor H. Human complement factor H (CFH)	43:100	Site-specific N-glycan characterization of human complement factor H. Human complement factor H (CFH) is a plasma glycoprotein involved in the regulation of the alternative pathway of the complement system.
17591618	1	106	theme	atypical	265:272	arg1	aHUS					303:306	aHUS	303:306	aHUS	303:306	A deficiency in CFH is a cause of severe pathologies like atypical haemolytic uraemic syndrome (aHUS).
17591618	1	106	theme	atypical	265:272	arg1	syndrome					293:300	atypical haemolytic uraemic syndrome	265:300	atypical haemolytic uraemic syndrome (aHUS)	265:307	A deficiency in CFH is a cause of severe pathologies like atypical haemolytic uraemic syndrome (aHUS).
17591618	0	107	dep	H.	67:68	arg1	CFH					97:99	CFH	97:99	CFH	97:99	Site-specific N-glycan characterization of human complement factor H. Human complement factor H (CFH) is a plasma glycoprotein involved in the regulation of the alternative pathway of the complement system.
17591618	0	107	dep	H.	67:68	arg1	H					94:94	Human complement factor H	70:94	human complement factor H. Human complement factor H (CFH)	43:100	Site-specific N-glycan characterization of human complement factor H. Human complement factor H (CFH) is a plasma glycoprotein involved in the regulation of the alternative pathway of the complement system.
17591618	4	108	theme	mass	732:735	arg1	decrease					737:744	A 17.9-kDa mass decrease	721:744	A 17.9-kDa mass decrease	721:744	A 17.9-kDa mass decrease, observed after glycosidase treatment, indicated that N-glycosylation is the major post-translational modification of CFH.
17591618	3	109	theme	tandem	681:686	arg1	spectrometry					693:704	matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) and liquid chromatography-electrospray ionization tandem mass spectrometry	560:704	spectrometry	693:704	In the current study, we present a quantitative glycosylation analysis of CFH using capillary electrophoresis and a complete site-specific N-glycan characterization using matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) and liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESIMS/MS).
17591618	7	110	theme	diantennary	1194:1204	arg1	glycans					1236:1242	complex, diantennary disialylated, non-fucosylated glycans	1185:1242	glycans	1236:1242	Quantitative analysis showed that CFH is mainly glycosylated by complex, diantennary disialylated, non-fucosylated glycans.
17591618	1	111	theme	uraemic	285:291	arg1	aHUS					303:306	aHUS	303:306	aHUS	303:306	A deficiency in CFH is a cause of severe pathologies like atypical haemolytic uraemic syndrome (aHUS).
17591618	1	111	theme	uraemic	285:291	arg1	syndrome					293:300	atypical haemolytic uraemic syndrome	265:300	atypical haemolytic uraemic syndrome (aHUS)	265:307	A deficiency in CFH is a cause of severe pathologies like atypical haemolytic uraemic syndrome (aHUS).
17591618	10	112	from	Asn199	1530:1535	arg1	absence					1502:1508	The absence	1498:1508	The absence of glycosylation at Asn199 of the NGSP sequence of CFH	1498:1563	The absence of glycosylation at Asn199 of the NGSP sequence of CFH is shown.
17591618	7	113	dep	disialylated	1206:1217	arg1	non-fucosylated					1220:1234	non-fucosylated	1220:1234	non-fucosylated	1220:1234	Quantitative analysis showed that CFH is mainly glycosylated by complex, diantennary disialylated, non-fucosylated glycans.
17591618	10	114	theme	glycosylation	1513:1525	arg1	absence					1502:1508	The absence	1498:1508	The absence of glycosylation at Asn199 of the NGSP sequence of CFH	1498:1563	The absence of glycosylation at Asn199 of the NGSP sequence of CFH is shown.
17591618	4	115	theme	CFH	864:866	arg1	modification					848:859	the major post-translational modification	819:859	the major post-translational modification of CFH	819:866	A 17.9-kDa mass decrease, observed after glycosidase treatment, indicated that N-glycosylation is the major post-translational modification of CFH.
17591618	4	115	theme	CFH	864:866	arg1	N-glycosylation					800:814	N-glycosylation	800:814	N-glycosylation	800:814	A 17.9-kDa mass decrease, observed after glycosidase treatment, indicated that N-glycosylation is the major post-translational modification of CFH.
17591618	8	116	gly	Disialylated	1245:1256	arg1	oligosaccharides					1305:1320	Disialylated fucosylated and monosialylated non-fucosylated oligosaccharides	1245:1320	Disialylated fucosylated and monosialylated non-fucosylated oligosaccharides	1245:1320	Disialylated fucosylated and monosialylated non-fucosylated oligosaccharides were also identified.
17591618	2	117	theme	155-kDa	319:325	arg1	CFH					310:312	CFH	310:312	CFH	310:312	CFH is a 155-kDa glycoprotein containing nine potential N-glycosylation sites.
17591618	2	117	theme	155-kDa	319:325	arg1	glycoprotein					327:338	a 155-kDa glycoprotein	317:338	a 155-kDa glycoprotein containing nine potential N-glycosylation sites	317:386	CFH is a 155-kDa glycoprotein containing nine potential N-glycosylation sites.
15084511	8	0	theme	branched	1647:1654	arg1	structures					1656:1665	more highly branched structures	1635:1665	more highly branched structures	1635:1665	The appearance of only biantennary glycans at site Asn 433, coupled with the appearance of more highly branched structures at Asn 334 and 447, demonstrates that biantennary acceptors present at different sites on the same protein during biosynthesis can differ in their accessibility for branching by GnT-V.
15084511	8	1	theme	biantennary	1705:1715	arg1	acceptors					1717:1725	biantennary acceptors	1705:1725	biantennary acceptors present at different sites on the same protein during biosynthesis	1705:1792	The appearance of only biantennary glycans at site Asn 433, coupled with the appearance of more highly branched structures at Asn 334 and 447, demonstrates that biantennary acceptors present at different sites on the same protein during biosynthesis can differ in their accessibility for branching by GnT-V.
15084511	8	2	theme	present	1727:1733	arg1	acceptors					1717:1725	biantennary acceptors	1705:1725	biantennary acceptors present at different sites on the same protein during biosynthesis	1705:1792	The appearance of only biantennary glycans at site Asn 433, coupled with the appearance of more highly branched structures at Asn 334 and 447, demonstrates that biantennary acceptors present at different sites on the same protein during biosynthesis can differ in their accessibility for branching by GnT-V.
15084511	6	3	contain	contain	1318:1324	arg2	structures					1326:1335	structures	1326:1335	structures	1326:1335	Sites Asn 433 and 447 both contain structures that range from biantennary with two sialic acids to tetraantennary terminating with four sialic acids.
15084511	6	3	contain	contain	1318:1324	arg1	Sites					1291:1295	Sites	1291:1295	Sites Asn 433 and 447	1291:1311	Sites Asn 433 and 447 both contain structures that range from biantennary with two sialic acids to tetraantennary terminating with four sialic acids.
15084511	6	3	contain	contain	1318:1324	arg2	range					1342:1346	range	1342:1346	range from biantennary with two sialic acids to tetraantennary terminating with four sialic acids	1342:1438	Sites Asn 433 and 447 both contain structures that range from biantennary with two sialic acids to tetraantennary terminating with four sialic acids.
15084511	6	4	dep	contain	1318:1324	arg1	both					1313:1316	both	1313:1316	both	1313:1316	Sites Asn 433 and 447 both contain structures that range from biantennary with two sialic acids to tetraantennary terminating with four sialic acids.
15084511	6	4	dep	contain	1318:1324	arg1	that					1337:1340	that	1337:1340	that	1337:1340	Sites Asn 433 and 447 both contain structures that range from biantennary with two sialic acids to tetraantennary terminating with four sialic acids.
15084511	2	5	theme	glycans	654:660	arg1	range					637:641	a range	635:641	a range of complex glycans from bi- to tetraantennary species	635:695	Release of N-glycans by PNGase F treatment, followed by analysis of the permethylated glycans using MALDI-TOF MS, indicated a range of complex glycans from bi- to tetraantennary species.
15084511	0	6	theme	core	227:230	arg1	mannose					200:206	the alpha1,6 mannose	187:206	the alpha1,6 mannose of the trimannosyl core	187:230	Analysis of the site-specific N-glycosylation of beta1,6 N-acetylglucosaminyltransferase V. N-acetylglucosaminyltransferase V (GnT-V) catalyzes the addition of a beta1,6-linked GlcNAc to the alpha1,6 mannose of the trimannosyl core to form tri- and tetraantennary N-glycans and contains six putative N-linked sites.
15084511	8	7	theme	different	1738:1746	arg1	sites					1748:1752	different sites	1738:1752	different sites on the same protein during biosynthesis	1738:1792	The appearance of only biantennary glycans at site Asn 433, coupled with the appearance of more highly branched structures at Asn 334 and 447, demonstrates that biantennary acceptors present at different sites on the same protein during biosynthesis can differ in their accessibility for branching by GnT-V.
15084511	7	8	theme	predominant	1445:1455	arg1	triantennary					1506:1517	a triantennary	1504:1517	a triantennary with three sialic acids	1504:1541	The predominant glycan species found on both of these sites is a triantennary with three sialic acids.
15084511	7	8	theme	predominant	1445:1455	arg1	species					1464:1470	The predominant glycan species	1441:1470	The predominant glycan species found on both of these sites	1441:1499	The predominant glycan species found on both of these sites is a triantennary with three sialic acids.
15084511	3	9	theme	glycan	959:964	arg1	masses					966:971	various glycan masses	951:971	various glycan masses to the masses of the glycopeptides determined experimentally	951:1032	Mapping of the glycosylation sites was performed by enriching for trypsin-digested glycopeptides, followed by analysis of each fraction with Q-TOF MS. Predicted tryptic glycopeptides were identified by comparisons of theoretical masses of peptides with various glycan masses to the masses of the glycopeptides determined experimentally.
15084511	3	10	theme	trypsin-digested	764:779	arg1	glycopeptides					781:793	trypsin-digested glycopeptides	764:793	trypsin-digested glycopeptides	764:793	Mapping of the glycosylation sites was performed by enriching for trypsin-digested glycopeptides, followed by analysis of each fraction with Q-TOF MS. Predicted tryptic glycopeptides were identified by comparisons of theoretical masses of peptides with various glycan masses to the masses of the glycopeptides determined experimentally.
15084511	8	11	theme	same	1761:1764	arg1	protein					1766:1772	the same protein	1757:1772	the same protein during biosynthesis	1757:1792	The appearance of only biantennary glycans at site Asn 433, coupled with the appearance of more highly branched structures at Asn 334 and 447, demonstrates that biantennary acceptors present at different sites on the same protein during biosynthesis can differ in their accessibility for branching by GnT-V.
15084511	0	12	link	N-linked	300:307	arg1	sites					309:313	six putative N-linked sites	287:313	six putative N-linked sites	287:313	Analysis of the site-specific N-glycosylation of beta1,6 N-acetylglucosaminyltransferase V. N-acetylglucosaminyltransferase V (GnT-V) catalyzes the addition of a beta1,6-linked GlcNAc to the alpha1,6 mannose of the trimannosyl core to form tri- and tetraantennary N-glycans and contains six putative N-linked sites.
15084511	3	13	gly	glycopeptides	867:879	arg2	glycopeptides					867:879	Predicted tryptic glycopeptides	849:879	Predicted tryptic glycopeptides	849:879	Mapping of the glycosylation sites was performed by enriching for trypsin-digested glycopeptides, followed by analysis of each fraction with Q-TOF MS. Predicted tryptic glycopeptides were identified by comparisons of theoretical masses of peptides with various glycan masses to the masses of the glycopeptides determined experimentally.
15084511	2	14	theme	MALDI-TOF	611:619	arg1	MS					621:622	MALDI-TOF MS	611:622	MALDI-TOF MS	611:622	Release of N-glycans by PNGase F treatment, followed by analysis of the permethylated glycans using MALDI-TOF MS, indicated a range of complex glycans from bi- to tetraantennary species.
15084511	2	15	from	bi-	667:669	arg1	range					637:641	a range	635:641	a range of complex glycans from bi- to tetraantennary species	635:695	Release of N-glycans by PNGase F treatment, followed by analysis of the permethylated glycans using MALDI-TOF MS, indicated a range of complex glycans from bi- to tetraantennary species.
15084511	2	15	from	bi-	667:669	arg1	glycans					654:660	complex glycans	646:660	complex glycans from bi- to tetraantennary species	646:695	Release of N-glycans by PNGase F treatment, followed by analysis of the permethylated glycans using MALDI-TOF MS, indicated a range of complex glycans from bi- to tetraantennary species.
15084511	0	16	theme	GlcNAc	177:182	arg1	addition					148:155	the addition	144:155	the addition of a beta1,6-linked GlcNAc to the alpha1,6 mannose of the trimannosyl core	144:230	Analysis of the site-specific N-glycosylation of beta1,6 N-acetylglucosaminyltransferase V. N-acetylglucosaminyltransferase V (GnT-V) catalyzes the addition of a beta1,6-linked GlcNAc to the alpha1,6 mannose of the trimannosyl core to form tri- and tetraantennary N-glycans and contains six putative N-linked sites.
15084511	2	17	theme	glycans	597:603	arg1	analysis					567:574	analysis	567:574	analysis of the permethylated glycans using MALDI-TOF MS	567:622	Release of N-glycans by PNGase F treatment, followed by analysis of the permethylated glycans using MALDI-TOF MS, indicated a range of complex glycans from bi- to tetraantennary species.
15084511	2	18	theme	PNGase	535:540	arg1	treatment					544:552	PNGase F treatment	535:552	PNGase F treatment	535:552	Release of N-glycans by PNGase F treatment, followed by analysis of the permethylated glycans using MALDI-TOF MS, indicated a range of complex glycans from bi- to tetraantennary species.
15084511	3	19	theme	fraction	825:832	arg1	analysis					808:815	analysis	808:815	analysis of each fraction with Q-TOF MS. Predicted tryptic glycopeptides were identified by comparisons of theoretical masses of peptides with various glycan masses to the masses of the glycopeptides determined experimentally	808:1032	Mapping of the glycosylation sites was performed by enriching for trypsin-digested glycopeptides, followed by analysis of each fraction with Q-TOF MS. Predicted tryptic glycopeptides were identified by comparisons of theoretical masses of peptides with various glycan masses to the masses of the glycopeptides determined experimentally.
15084511	6	20	theme	sialic	1427:1432	arg1	acids					1434:1438	four sialic acids	1422:1438	four sialic acids	1422:1438	Sites Asn 433 and 447 both contain structures that range from biantennary with two sialic acids to tetraantennary terminating with four sialic acids.
15084511	2	21	theme	N-glycans	522:530	arg1	Release					511:517	Release	511:517	Release	511:517	Release of N-glycans by PNGase F treatment, followed by analysis of the permethylated glycans using MALDI-TOF MS, indicated a range of complex glycans from bi- to tetraantennary species.
15084511	8	22	attach	present	1727:1733	arg2	acceptors					1717:1725	biantennary acceptors	1705:1725	biantennary acceptors present at different sites on the same protein during biosynthesis	1705:1792	The appearance of only biantennary glycans at site Asn 433, coupled with the appearance of more highly branched structures at Asn 334 and 447, demonstrates that biantennary acceptors present at different sites on the same protein during biosynthesis can differ in their accessibility for branching by GnT-V.
15084511	8	22	attach	present	1727:1733	arg1	sites					1748:1752	different sites	1738:1752	different sites on the same protein during biosynthesis	1738:1792	The appearance of only biantennary glycans at site Asn 433, coupled with the appearance of more highly branched structures at Asn 334 and 447, demonstrates that biantennary acceptors present at different sites on the same protein during biosynthesis can differ in their accessibility for branching by GnT-V.
15084511	0	23	theme	V	124:124	arg1	N-glycosylation					30:44	the site-specific N-glycosylation	12:44	the site-specific N-glycosylation of beta1,6 N-acetylglucosaminyltransferase V. N-acetylglucosaminyltransferase V (GnT-V)	12:132	Analysis of the site-specific N-glycosylation of beta1,6 N-acetylglucosaminyltransferase V. N-acetylglucosaminyltransferase V (GnT-V) catalyzes the addition of a beta1,6-linked GlcNAc to the alpha1,6 mannose of the trimannosyl core to form tri- and tetraantennary N-glycans and contains six putative N-linked sites.
15084511	0	24	theme	tetraantennary	249:262	arg1	N-glycans					264:272	tri- and tetraantennary N-glycans	240:272	tri- and tetraantennary N-glycans	240:272	Analysis of the site-specific N-glycosylation of beta1,6 N-acetylglucosaminyltransferase V. N-acetylglucosaminyltransferase V (GnT-V) catalyzes the addition of a beta1,6-linked GlcNAc to the alpha1,6 mannose of the trimannosyl core to form tri- and tetraantennary N-glycans and contains six putative N-linked sites.
15084511	3	25	theme	theoretical	915:925	arg1	masses					927:932	theoretical masses	915:932	theoretical masses of peptides with various glycan masses to the masses of the glycopeptides determined experimentally	915:1032	Mapping of the glycosylation sites was performed by enriching for trypsin-digested glycopeptides, followed by analysis of each fraction with Q-TOF MS. Predicted tryptic glycopeptides were identified by comparisons of theoretical masses of peptides with various glycan masses to the masses of the glycopeptides determined experimentally.
15084511	8	26	from	447	1682:1684	arg1	appearance					1621:1630	the appearance	1617:1630	the appearance of more highly branched structures at Asn 334 and 447	1617:1684	The appearance of only biantennary glycans at site Asn 433, coupled with the appearance of more highly branched structures at Asn 334 and 447, demonstrates that biantennary acceptors present at different sites on the same protein during biosynthesis can differ in their accessibility for branching by GnT-V.
15084511	3	27	theme	Predicted	849:857	arg1	glycopeptides					867:879	Predicted tryptic glycopeptides	849:879	Predicted tryptic glycopeptides	849:879	Mapping of the glycosylation sites was performed by enriching for trypsin-digested glycopeptides, followed by analysis of each fraction with Q-TOF MS. Predicted tryptic glycopeptides were identified by comparisons of theoretical masses of peptides with various glycan masses to the masses of the glycopeptides determined experimentally.
15084511	1	28	theme	recombinant	396:406	arg1	GnT-V					414:418	recombinant human GnT-V	396:418	recombinant human GnT-V expressed in CHO cells	396:441	We used mass spectrometry techniques combined with exoglycosidase digestions of recombinant human GnT-V expressed in CHO cells, to identify its N-glycan structures and their sites of expression.
15084511	4	29	contain	containing	1111:1120	arg1	peptides					1102:1109	peptides	1102:1109	peptides containing sites Asn 334, 433, and 447	1102:1148	Of the three putative glycosylation sites in the catalytic region, peptides containing sites Asn 334, 433, and 447 were identified as being N-glycosylated.
15084511	4	29	contain	containing	1111:1120	arg2	sites					1122:1126	sites Asn 334, 433, and 447	1122:1148	sites Asn 334, 433, and 447	1122:1148	Of the three putative glycosylation sites in the catalytic region, peptides containing sites Asn 334, 433, and 447 were identified as being N-glycosylated.
15084511	0	30	link	beta1,6-linked	162:175	arg1	GlcNAc					177:182	a beta1,6-linked GlcNAc	160:182	a beta1,6-linked GlcNAc	160:182	Analysis of the site-specific N-glycosylation of beta1,6 N-acetylglucosaminyltransferase V. N-acetylglucosaminyltransferase V (GnT-V) catalyzes the addition of a beta1,6-linked GlcNAc to the alpha1,6 mannose of the trimannosyl core to form tri- and tetraantennary N-glycans and contains six putative N-linked sites.
15084511	8	31	from	334	1674:1676	arg1	appearance					1621:1630	the appearance	1617:1630	the appearance of more highly branched structures at Asn 334 and 447	1617:1684	The appearance of only biantennary glycans at site Asn 433, coupled with the appearance of more highly branched structures at Asn 334 and 447, demonstrates that biantennary acceptors present at different sites on the same protein during biosynthesis can differ in their accessibility for branching by GnT-V.
15084511	1	32	theme	GnT-V	414:418	arg1	digestions					382:391	exoglycosidase digestions	367:391	exoglycosidase digestions of recombinant human GnT-V expressed in CHO cells	367:441	We used mass spectrometry techniques combined with exoglycosidase digestions of recombinant human GnT-V expressed in CHO cells, to identify its N-glycan structures and their sites of expression.
15084511	4	33	theme	catalytic	1084:1092	arg1	region					1094:1099	the catalytic region	1080:1099	the catalytic region	1080:1099	Of the three putative glycosylation sites in the catalytic region, peptides containing sites Asn 334, 433, and 447 were identified as being N-glycosylated.
15084511	0	34	theme	N-linked	300:307	arg1	sites					309:313	six putative N-linked sites	287:313	six putative N-linked sites	287:313	Analysis of the site-specific N-glycosylation of beta1,6 N-acetylglucosaminyltransferase V. N-acetylglucosaminyltransferase V (GnT-V) catalyzes the addition of a beta1,6-linked GlcNAc to the alpha1,6 mannose of the trimannosyl core to form tri- and tetraantennary N-glycans and contains six putative N-linked sites.
15084511	8	35	theme	glycans	1579:1585	arg1	appearance					1548:1557	The appearance	1544:1557	The appearance	1544:1557	The appearance of only biantennary glycans at site Asn 433, coupled with the appearance of more highly branched structures at Asn 334 and 447, demonstrates that biantennary acceptors present at different sites on the same protein during biosynthesis can differ in their accessibility for branching by GnT-V.
15084511	4	36	theme	glycosylation	1057:1069	arg1	sites					1071:1075	the three putative glycosylation sites	1038:1075	the three putative glycosylation sites in the catalytic region	1038:1099	Of the three putative glycosylation sites in the catalytic region, peptides containing sites Asn 334, 433, and 447 were identified as being N-glycosylated.
15084511	8	37	theme	site	1590:1593	arg1	Asn					1595:1597	site Asn 433	1590:1601	site Asn 433	1590:1601	The appearance of only biantennary glycans at site Asn 433, coupled with the appearance of more highly branched structures at Asn 334 and 447, demonstrates that biantennary acceptors present at different sites on the same protein during biosynthesis can differ in their accessibility for branching by GnT-V.
15084511	0	38	theme	N-glycosylation	30:44	arg1	Analysis					0:7	Analysis	0:7	Analysis of the site-specific N-glycosylation of beta1,6 N-acetylglucosaminyltransferase V. N-acetylglucosaminyltransferase V (GnT-V)	0:132	Analysis of the site-specific N-glycosylation of beta1,6 N-acetylglucosaminyltransferase V. N-acetylglucosaminyltransferase V (GnT-V) catalyzes the addition of a beta1,6-linked GlcNAc to the alpha1,6 mannose of the trimannosyl core to form tri- and tetraantennary N-glycans and contains six putative N-linked sites.
15084511	1	39	theme	mass	324:327	arg1	techniques					342:351	mass spectrometry techniques	324:351	mass spectrometry techniques combined with exoglycosidase digestions of recombinant human GnT-V expressed in CHO cells	324:441	We used mass spectrometry techniques combined with exoglycosidase digestions of recombinant human GnT-V expressed in CHO cells, to identify its N-glycan structures and their sites of expression.
15084511	2	40	from	range	637:641	arg1	bi-					667:669	bi-	667:669	bi- to tetraantennary species	667:695	Release of N-glycans by PNGase F treatment, followed by analysis of the permethylated glycans using MALDI-TOF MS, indicated a range of complex glycans from bi- to tetraantennary species.
15084511	0	41	theme	V.	89:90	arg1	V					124:124	beta1,6 N-acetylglucosaminyltransferase V. N-acetylglucosaminyltransferase V	49:124	beta1,6 N-acetylglucosaminyltransferase V. N-acetylglucosaminyltransferase V (GnT-V)	49:132	Analysis of the site-specific N-glycosylation of beta1,6 N-acetylglucosaminyltransferase V. N-acetylglucosaminyltransferase V (GnT-V) catalyzes the addition of a beta1,6-linked GlcNAc to the alpha1,6 mannose of the trimannosyl core to form tri- and tetraantennary N-glycans and contains six putative N-linked sites.
15084511	0	41	theme	V.	89:90	arg1	GnT-V					127:131	GnT-V	127:131	GnT-V	127:131	Analysis of the site-specific N-glycosylation of beta1,6 N-acetylglucosaminyltransferase V. N-acetylglucosaminyltransferase V (GnT-V) catalyzes the addition of a beta1,6-linked GlcNAc to the alpha1,6 mannose of the trimannosyl core to form tri- and tetraantennary N-glycans and contains six putative N-linked sites.
15084511	0	42	theme	beta1,6	49:55	arg1	V					124:124	beta1,6 N-acetylglucosaminyltransferase V. N-acetylglucosaminyltransferase V	49:124	beta1,6 N-acetylglucosaminyltransferase V. N-acetylglucosaminyltransferase V (GnT-V)	49:132	Analysis of the site-specific N-glycosylation of beta1,6 N-acetylglucosaminyltransferase V. N-acetylglucosaminyltransferase V (GnT-V) catalyzes the addition of a beta1,6-linked GlcNAc to the alpha1,6 mannose of the trimannosyl core to form tri- and tetraantennary N-glycans and contains six putative N-linked sites.
15084511	0	42	theme	beta1,6	49:55	arg1	GnT-V					127:131	GnT-V	127:131	GnT-V	127:131	Analysis of the site-specific N-glycosylation of beta1,6 N-acetylglucosaminyltransferase V. N-acetylglucosaminyltransferase V (GnT-V) catalyzes the addition of a beta1,6-linked GlcNAc to the alpha1,6 mannose of the trimannosyl core to form tri- and tetraantennary N-glycans and contains six putative N-linked sites.
15084511	7	43	located	found	1472:1476	arg1	sites					1495:1499	these sites	1489:1499	these sites	1489:1499	The predominant glycan species found on both of these sites is a triantennary with three sialic acids.
15084511	7	43	located	found	1472:1476	arg2	triantennary					1506:1517	a triantennary	1504:1517	a triantennary with three sialic acids	1504:1541	The predominant glycan species found on both of these sites is a triantennary with three sialic acids.
15084511	7	43	located	found	1472:1476	arg2	species					1464:1470	The predominant glycan species	1441:1470	The predominant glycan species found on both of these sites	1441:1499	The predominant glycan species found on both of these sites is a triantennary with three sialic acids.
15084511	7	43	located	found	1472:1476	arg1	both					1481:1484	both	1481:1484	both	1481:1484	The predominant glycan species found on both of these sites is a triantennary with three sialic acids.
15084511	8	44	theme	Asn	1670:1672	arg1	334					1674:1676	Asn 334	1670:1676	Asn 334	1670:1676	The appearance of only biantennary glycans at site Asn 433, coupled with the appearance of more highly branched structures at Asn 334 and 447, demonstrates that biantennary acceptors present at different sites on the same protein during biosynthesis can differ in their accessibility for branching by GnT-V.
15084511	7	45	theme	sialic	1530:1535	arg1	acids					1537:1541	three sialic acids	1524:1541	three sialic acids	1524:1541	The predominant glycan species found on both of these sites is a triantennary with three sialic acids.
15084511	4	46	gly	glycosylation	1057:1069	arg2	three					1042:1046	three	1042:1046	three	1042:1046	Of the three putative glycosylation sites in the catalytic region, peptides containing sites Asn 334, 433, and 447 were identified as being N-glycosylated.
15084511	4	46	gly	glycosylation	1057:1069	arg2	sites					1071:1075	the three putative glycosylation sites	1038:1075	the three putative glycosylation sites in the catalytic region	1038:1099	Of the three putative glycosylation sites in the catalytic region, peptides containing sites Asn 334, 433, and 447 were identified as being N-glycosylated.
15084511	5	47	theme	sialic	1277:1282	arg1	acids					1284:1288	sialic acids	1277:1288	sialic acids	1277:1288	Asn 334 is glycosylated with only a biantennary structure with one or two terminating sialic acids.
15084511	4	48	from	sites	1071:1075	arg1	region					1094:1099	the catalytic region	1080:1099	the catalytic region	1080:1099	Of the three putative glycosylation sites in the catalytic region, peptides containing sites Asn 334, 433, and 447 were identified as being N-glycosylated.
15084511	8	49	from	Asn	1595:1597	arg1	glycans					1579:1585	only biantennary glycans	1562:1585	only biantennary glycans at site Asn 433	1562:1601	The appearance of only biantennary glycans at site Asn 433, coupled with the appearance of more highly branched structures at Asn 334 and 447, demonstrates that biantennary acceptors present at different sites on the same protein during biosynthesis can differ in their accessibility for branching by GnT-V.
15084511	8	49	from	Asn	1595:1597	arg1	appearance					1548:1557	The appearance	1544:1557	The appearance	1544:1557	The appearance of only biantennary glycans at site Asn 433, coupled with the appearance of more highly branched structures at Asn 334 and 447, demonstrates that biantennary acceptors present at different sites on the same protein during biosynthesis can differ in their accessibility for branching by GnT-V.
15084511	7	50	with	triantennary	1506:1517	arg1	acids					1537:1541	three sialic acids	1524:1541	three sialic acids	1524:1541	The predominant glycan species found on both of these sites is a triantennary with three sialic acids.
15084511	4	51	theme	Asn	1128:1130	arg1	334					1132:1134	Asn 334	1128:1134	Asn 334	1128:1134	Of the three putative glycosylation sites in the catalytic region, peptides containing sites Asn 334, 433, and 447 were identified as being N-glycosylated.
15084511	3	52	theme	glycosylation	713:725	arg1	sites					727:731	the glycosylation sites	709:731	the glycosylation sites	709:731	Mapping of the glycosylation sites was performed by enriching for trypsin-digested glycopeptides, followed by analysis of each fraction with Q-TOF MS. Predicted tryptic glycopeptides were identified by comparisons of theoretical masses of peptides with various glycan masses to the masses of the glycopeptides determined experimentally.
15084511	0	53	theme	trimannosyl	215:225	arg1	core					227:230	the trimannosyl core	211:230	the trimannosyl core	211:230	Analysis of the site-specific N-glycosylation of beta1,6 N-acetylglucosaminyltransferase V. N-acetylglucosaminyltransferase V (GnT-V) catalyzes the addition of a beta1,6-linked GlcNAc to the alpha1,6 mannose of the trimannosyl core to form tri- and tetraantennary N-glycans and contains six putative N-linked sites.
15084511	1	54	used	used	319:322	arg2	We					316:317	We	316:317	We	316:317	We used mass spectrometry techniques combined with exoglycosidase digestions of recombinant human GnT-V expressed in CHO cells, to identify its N-glycan structures and their sites of expression.
15084511	8	55	theme	structures	1656:1665	arg1	appearance					1621:1630	the appearance	1617:1630	the appearance of more highly branched structures at Asn 334 and 447	1617:1684	The appearance of only biantennary glycans at site Asn 433, coupled with the appearance of more highly branched structures at Asn 334 and 447, demonstrates that biantennary acceptors present at different sites on the same protein during biosynthesis can differ in their accessibility for branching by GnT-V.
15084511	6	56	with	biantennary	1353:1363	arg1	acids					1381:1385	two sialic acids	1370:1385	two sialic acids to tetraantennary terminating with four sialic acids	1370:1438	Sites Asn 433 and 447 both contain structures that range from biantennary with two sialic acids to tetraantennary terminating with four sialic acids.
15084511	8	57	from	appearance	1548:1557	arg1	Asn					1595:1597	site Asn 433	1590:1601	site Asn 433	1590:1601	The appearance of only biantennary glycans at site Asn 433, coupled with the appearance of more highly branched structures at Asn 334 and 447, demonstrates that biantennary acceptors present at different sites on the same protein during biosynthesis can differ in their accessibility for branching by GnT-V.
15084511	2	58	theme	complex	646:652	arg1	glycans					654:660	complex glycans	646:660	complex glycans from bi- to tetraantennary species	646:695	Release of N-glycans by PNGase F treatment, followed by analysis of the permethylated glycans using MALDI-TOF MS, indicated a range of complex glycans from bi- to tetraantennary species.
15084511	0	59	theme	tri-	240:243	arg1	N-glycans					264:272	tri- and tetraantennary N-glycans	240:272	tri- and tetraantennary N-glycans	240:272	Analysis of the site-specific N-glycosylation of beta1,6 N-acetylglucosaminyltransferase V. N-acetylglucosaminyltransferase V (GnT-V) catalyzes the addition of a beta1,6-linked GlcNAc to the alpha1,6 mannose of the trimannosyl core to form tri- and tetraantennary N-glycans and contains six putative N-linked sites.
15084511	1	60	theme	expression	499:508	arg1	expression					499:508	expression	499:508	expression	499:508	We used mass spectrometry techniques combined with exoglycosidase digestions of recombinant human GnT-V expressed in CHO cells, to identify its N-glycan structures and their sites of expression.
15084511	1	60	theme	expression	499:508	arg1	structures					469:478	its N-glycan structures	456:478	its N-glycan structures	456:478	We used mass spectrometry techniques combined with exoglycosidase digestions of recombinant human GnT-V expressed in CHO cells, to identify its N-glycan structures and their sites of expression.
15084511	1	60	theme	expression	499:508	arg1	sites					490:494	their sites	484:494	their sites of expression	484:508	We used mass spectrometry techniques combined with exoglycosidase digestions of recombinant human GnT-V expressed in CHO cells, to identify its N-glycan structures and their sites of expression.
15084511	7	61	theme	glycan	1457:1462	arg1	triantennary					1506:1517	a triantennary	1504:1517	a triantennary with three sialic acids	1504:1541	The predominant glycan species found on both of these sites is a triantennary with three sialic acids.
15084511	7	61	theme	glycan	1457:1462	arg1	species					1464:1470	The predominant glycan species	1441:1470	The predominant glycan species found on both of these sites	1441:1499	The predominant glycan species found on both of these sites is a triantennary with three sialic acids.
15084511	0	62	contain	contains	278:285	arg2	sites					309:313	six putative N-linked sites	287:313	six putative N-linked sites	287:313	Analysis of the site-specific N-glycosylation of beta1,6 N-acetylglucosaminyltransferase V. N-acetylglucosaminyltransferase V (GnT-V) catalyzes the addition of a beta1,6-linked GlcNAc to the alpha1,6 mannose of the trimannosyl core to form tri- and tetraantennary N-glycans and contains six putative N-linked sites.
15084511	0	62	contain	contains	278:285	arg1	Analysis					0:7	Analysis	0:7	Analysis of the site-specific N-glycosylation of beta1,6 N-acetylglucosaminyltransferase V. N-acetylglucosaminyltransferase V (GnT-V)	0:132	Analysis of the site-specific N-glycosylation of beta1,6 N-acetylglucosaminyltransferase V. N-acetylglucosaminyltransferase V (GnT-V) catalyzes the addition of a beta1,6-linked GlcNAc to the alpha1,6 mannose of the trimannosyl core to form tri- and tetraantennary N-glycans and contains six putative N-linked sites.
15084511	6	63	theme	sialic	1374:1379	arg1	acids					1381:1385	two sialic acids	1370:1385	two sialic acids to tetraantennary terminating with four sialic acids	1370:1438	Sites Asn 433 and 447 both contain structures that range from biantennary with two sialic acids to tetraantennary terminating with four sialic acids.
15084511	3	64	gly	glycopeptides	994:1006	arg2	glycopeptides					994:1006	the glycopeptides	990:1006	the glycopeptides determined experimentally	990:1032	Mapping of the glycosylation sites was performed by enriching for trypsin-digested glycopeptides, followed by analysis of each fraction with Q-TOF MS. Predicted tryptic glycopeptides were identified by comparisons of theoretical masses of peptides with various glycan masses to the masses of the glycopeptides determined experimentally.
15084511	0	65	theme	beta1,6-linked	162:175	arg1	GlcNAc					177:182	a beta1,6-linked GlcNAc	160:182	a beta1,6-linked GlcNAc	160:182	Analysis of the site-specific N-glycosylation of beta1,6 N-acetylglucosaminyltransferase V. N-acetylglucosaminyltransferase V (GnT-V) catalyzes the addition of a beta1,6-linked GlcNAc to the alpha1,6 mannose of the trimannosyl core to form tri- and tetraantennary N-glycans and contains six putative N-linked sites.
15084511	1	66	theme	CHO	433:435	arg1	cells					437:441	CHO cells	433:441	CHO cells	433:441	We used mass spectrometry techniques combined with exoglycosidase digestions of recombinant human GnT-V expressed in CHO cells, to identify its N-glycan structures and their sites of expression.
15084511	0	67	theme	alpha1,6	191:198	arg1	mannose					200:206	the alpha1,6 mannose	187:206	the alpha1,6 mannose of the trimannosyl core	187:230	Analysis of the site-specific N-glycosylation of beta1,6 N-acetylglucosaminyltransferase V. N-acetylglucosaminyltransferase V (GnT-V) catalyzes the addition of a beta1,6-linked GlcNAc to the alpha1,6 mannose of the trimannosyl core to form tri- and tetraantennary N-glycans and contains six putative N-linked sites.
15084511	4	68	dep	sites	1122:1126	arg1	433					1137:1139	433	1137:1139	433	1137:1139	Of the three putative glycosylation sites in the catalytic region, peptides containing sites Asn 334, 433, and 447 were identified as being N-glycosylated.
15084511	4	68	dep	sites	1122:1126	arg1	447					1146:1148	447	1146:1148	447	1146:1148	Of the three putative glycosylation sites in the catalytic region, peptides containing sites Asn 334, 433, and 447 were identified as being N-glycosylated.
15084511	4	68	dep	sites	1122:1126	arg1	334					1132:1134	Asn 334	1128:1134	Asn 334	1128:1134	Of the three putative glycosylation sites in the catalytic region, peptides containing sites Asn 334, 433, and 447 were identified as being N-glycosylated.
15084511	2	69	theme	permethylated	583:595	arg1	glycans					597:603	the permethylated glycans	579:603	the permethylated glycans using MALDI-TOF MS	579:622	Release of N-glycans by PNGase F treatment, followed by analysis of the permethylated glycans using MALDI-TOF MS, indicated a range of complex glycans from bi- to tetraantennary species.
15084511	0	70	theme	N-acetylglucosaminyltransferase	92:122	arg1	V					124:124	beta1,6 N-acetylglucosaminyltransferase V. N-acetylglucosaminyltransferase V	49:124	beta1,6 N-acetylglucosaminyltransferase V. N-acetylglucosaminyltransferase V (GnT-V)	49:132	Analysis of the site-specific N-glycosylation of beta1,6 N-acetylglucosaminyltransferase V. N-acetylglucosaminyltransferase V (GnT-V) catalyzes the addition of a beta1,6-linked GlcNAc to the alpha1,6 mannose of the trimannosyl core to form tri- and tetraantennary N-glycans and contains six putative N-linked sites.
15084511	0	70	theme	N-acetylglucosaminyltransferase	92:122	arg1	GnT-V					127:131	GnT-V	127:131	GnT-V	127:131	Analysis of the site-specific N-glycosylation of beta1,6 N-acetylglucosaminyltransferase V. N-acetylglucosaminyltransferase V (GnT-V) catalyzes the addition of a beta1,6-linked GlcNAc to the alpha1,6 mannose of the trimannosyl core to form tri- and tetraantennary N-glycans and contains six putative N-linked sites.
15084511	1	71	theme	N-glycan	460:467	arg1	structures					469:478	its N-glycan structures	456:478	its N-glycan structures	456:478	We used mass spectrometry techniques combined with exoglycosidase digestions of recombinant human GnT-V expressed in CHO cells, to identify its N-glycan structures and their sites of expression.
15084511	5	72	gly	glycosylated	1202:1213	arg1	Asn					1191:1193	Asn 334	1191:1197	Asn 334	1191:1197	Asn 334 is glycosylated with only a biantennary structure with one or two terminating sialic acids.
15084511	1	73	theme	exoglycosidase	367:380	arg1	digestions					382:391	exoglycosidase digestions	367:391	exoglycosidase digestions of recombinant human GnT-V expressed in CHO cells	367:441	We used mass spectrometry techniques combined with exoglycosidase digestions of recombinant human GnT-V expressed in CHO cells, to identify its N-glycan structures and their sites of expression.
15084511	3	74	theme	peptides	937:944	arg1	masses					927:932	theoretical masses	915:932	theoretical masses of peptides with various glycan masses to the masses of the glycopeptides determined experimentally	915:1032	Mapping of the glycosylation sites was performed by enriching for trypsin-digested glycopeptides, followed by analysis of each fraction with Q-TOF MS. Predicted tryptic glycopeptides were identified by comparisons of theoretical masses of peptides with various glycan masses to the masses of the glycopeptides determined experimentally.
15084511	2	75	theme	tetraantennary	674:687	arg1	species					689:695	tetraantennary species	674:695	tetraantennary species	674:695	Release of N-glycans by PNGase F treatment, followed by analysis of the permethylated glycans using MALDI-TOF MS, indicated a range of complex glycans from bi- to tetraantennary species.
15084511	3	76	with	peptides	937:944	arg1	masses					966:971	various glycan masses	951:971	various glycan masses to the masses of the glycopeptides determined experimentally	951:1032	Mapping of the glycosylation sites was performed by enriching for trypsin-digested glycopeptides, followed by analysis of each fraction with Q-TOF MS. Predicted tryptic glycopeptides were identified by comparisons of theoretical masses of peptides with various glycan masses to the masses of the glycopeptides determined experimentally.
15084511	3	77	with	analysis	808:815	arg1	Q-TOF					839:843	Q-TOF	839:843	Q-TOF MS. Predicted tryptic glycopeptides were identified by comparisons of theoretical masses of peptides with various glycan masses to the masses of the glycopeptides determined experimentally	839:1032	Mapping of the glycosylation sites was performed by enriching for trypsin-digested glycopeptides, followed by analysis of each fraction with Q-TOF MS. Predicted tryptic glycopeptides were identified by comparisons of theoretical masses of peptides with various glycan masses to the masses of the glycopeptides determined experimentally.
15084511	3	78	theme	masses	927:932	arg1	comparisons					900:910	comparisons	900:910	comparisons of theoretical masses of peptides with various glycan masses to the masses of the glycopeptides determined experimentally	900:1032	Mapping of the glycosylation sites was performed by enriching for trypsin-digested glycopeptides, followed by analysis of each fraction with Q-TOF MS. Predicted tryptic glycopeptides were identified by comparisons of theoretical masses of peptides with various glycan masses to the masses of the glycopeptides determined experimentally.
15084511	3	79	theme	tryptic	859:865	arg1	glycopeptides					867:879	Predicted tryptic glycopeptides	849:879	Predicted tryptic glycopeptides	849:879	Mapping of the glycosylation sites was performed by enriching for trypsin-digested glycopeptides, followed by analysis of each fraction with Q-TOF MS. Predicted tryptic glycopeptides were identified by comparisons of theoretical masses of peptides with various glycan masses to the masses of the glycopeptides determined experimentally.
15084511	1	80	theme	human	408:412	arg1	GnT-V					414:418	recombinant human GnT-V	396:418	recombinant human GnT-V expressed in CHO cells	396:441	We used mass spectrometry techniques combined with exoglycosidase digestions of recombinant human GnT-V expressed in CHO cells, to identify its N-glycan structures and their sites of expression.
15084511	2	81	theme	F	542:542	arg1	treatment					544:552	PNGase F treatment	535:552	PNGase F treatment	535:552	Release of N-glycans by PNGase F treatment, followed by analysis of the permethylated glycans using MALDI-TOF MS, indicated a range of complex glycans from bi- to tetraantennary species.
15084511	3	82	gly	glycopeptides	781:793	arg2	glycopeptides					781:793	trypsin-digested glycopeptides	764:793	trypsin-digested glycopeptides	764:793	Mapping of the glycosylation sites was performed by enriching for trypsin-digested glycopeptides, followed by analysis of each fraction with Q-TOF MS. Predicted tryptic glycopeptides were identified by comparisons of theoretical masses of peptides with various glycan masses to the masses of the glycopeptides determined experimentally.
15084511	3	83	theme	various	951:957	arg1	masses					966:971	various glycan masses	951:971	various glycan masses to the masses of the glycopeptides determined experimentally	951:1032	Mapping of the glycosylation sites was performed by enriching for trypsin-digested glycopeptides, followed by analysis of each fraction with Q-TOF MS. Predicted tryptic glycopeptides were identified by comparisons of theoretical masses of peptides with various glycan masses to the masses of the glycopeptides determined experimentally.
15084511	0	84	theme	site-specific	16:28	arg1	N-glycosylation					30:44	the site-specific N-glycosylation	12:44	the site-specific N-glycosylation of beta1,6 N-acetylglucosaminyltransferase V. N-acetylglucosaminyltransferase V (GnT-V)	12:132	Analysis of the site-specific N-glycosylation of beta1,6 N-acetylglucosaminyltransferase V. N-acetylglucosaminyltransferase V (GnT-V) catalyzes the addition of a beta1,6-linked GlcNAc to the alpha1,6 mannose of the trimannosyl core to form tri- and tetraantennary N-glycans and contains six putative N-linked sites.
15084511	6	85	from	biantennary	1353:1363	arg1	range					1342:1346	range	1342:1346	range from biantennary with two sialic acids to tetraantennary terminating with four sialic acids	1342:1438	Sites Asn 433 and 447 both contain structures that range from biantennary with two sialic acids to tetraantennary terminating with four sialic acids.
15084511	0	86	theme	putative	291:298	arg1	sites					309:313	six putative N-linked sites	287:313	six putative N-linked sites	287:313	Analysis of the site-specific N-glycosylation of beta1,6 N-acetylglucosaminyltransferase V. N-acetylglucosaminyltransferase V (GnT-V) catalyzes the addition of a beta1,6-linked GlcNAc to the alpha1,6 mannose of the trimannosyl core to form tri- and tetraantennary N-glycans and contains six putative N-linked sites.
15084511	5	87	theme	biantennary	1227:1237	arg1	structure					1239:1247	only a biantennary structure	1220:1247	only a biantennary structure with one or two terminating sialic acids	1220:1288	Asn 334 is glycosylated with only a biantennary structure with one or two terminating sialic acids.
15084511	4	88	theme	putative	1048:1055	arg1	sites					1071:1075	the three putative glycosylation sites	1038:1075	the three putative glycosylation sites in the catalytic region	1038:1099	Of the three putative glycosylation sites in the catalytic region, peptides containing sites Asn 334, 433, and 447 were identified as being N-glycosylated.
15084511	0	89	theme	N-acetylglucosaminyltransferase	57:87	arg1	V					124:124	beta1,6 N-acetylglucosaminyltransferase V. N-acetylglucosaminyltransferase V	49:124	beta1,6 N-acetylglucosaminyltransferase V. N-acetylglucosaminyltransferase V (GnT-V)	49:132	Analysis of the site-specific N-glycosylation of beta1,6 N-acetylglucosaminyltransferase V. N-acetylglucosaminyltransferase V (GnT-V) catalyzes the addition of a beta1,6-linked GlcNAc to the alpha1,6 mannose of the trimannosyl core to form tri- and tetraantennary N-glycans and contains six putative N-linked sites.
15084511	0	89	theme	N-acetylglucosaminyltransferase	57:87	arg1	GnT-V					127:131	GnT-V	127:131	GnT-V	127:131	Analysis of the site-specific N-glycosylation of beta1,6 N-acetylglucosaminyltransferase V. N-acetylglucosaminyltransferase V (GnT-V) catalyzes the addition of a beta1,6-linked GlcNAc to the alpha1,6 mannose of the trimannosyl core to form tri- and tetraantennary N-glycans and contains six putative N-linked sites.
15084511	1	90	theme	spectrometry	329:340	arg1	techniques					342:351	mass spectrometry techniques	324:351	mass spectrometry techniques combined with exoglycosidase digestions of recombinant human GnT-V expressed in CHO cells	324:441	We used mass spectrometry techniques combined with exoglycosidase digestions of recombinant human GnT-V expressed in CHO cells, to identify its N-glycan structures and their sites of expression.
15084511	8	91	theme	biantennary	1567:1577	arg1	glycans					1579:1585	only biantennary glycans	1562:1585	only biantennary glycans at site Asn 433	1562:1601	The appearance of only biantennary glycans at site Asn 433, coupled with the appearance of more highly branched structures at Asn 334 and 447, demonstrates that biantennary acceptors present at different sites on the same protein during biosynthesis can differ in their accessibility for branching by GnT-V.
15084511	3	92	gly	glycosylation	713:725	arg2	sites					727:731	the glycosylation sites	709:731	the glycosylation sites	709:731	Mapping of the glycosylation sites was performed by enriching for trypsin-digested glycopeptides, followed by analysis of each fraction with Q-TOF MS. Predicted tryptic glycopeptides were identified by comparisons of theoretical masses of peptides with various glycan masses to the masses of the glycopeptides determined experimentally.
15084511	5	93	with	structure	1239:1247	arg1	one					1254:1256	one	1254:1256	one	1254:1256	Asn 334 is glycosylated with only a biantennary structure with one or two terminating sialic acids.
15084511	5	93	with	structure	1239:1247	arg1	two					1261:1263	two	1261:1263	two	1261:1263	Asn 334 is glycosylated with only a biantennary structure with one or two terminating sialic acids.
15084511	0	94	gly	N-glycosylation	30:44	arg1	V					124:124	beta1,6 N-acetylglucosaminyltransferase V. N-acetylglucosaminyltransferase V	49:124	beta1,6 N-acetylglucosaminyltransferase V. N-acetylglucosaminyltransferase V (GnT-V)	49:132	Analysis of the site-specific N-glycosylation of beta1,6 N-acetylglucosaminyltransferase V. N-acetylglucosaminyltransferase V (GnT-V) catalyzes the addition of a beta1,6-linked GlcNAc to the alpha1,6 mannose of the trimannosyl core to form tri- and tetraantennary N-glycans and contains six putative N-linked sites.
15084511	0	94	gly	N-glycosylation	30:44	arg1	GnT-V					127:131	GnT-V	127:131	GnT-V	127:131	Analysis of the site-specific N-glycosylation of beta1,6 N-acetylglucosaminyltransferase V. N-acetylglucosaminyltransferase V (GnT-V) catalyzes the addition of a beta1,6-linked GlcNAc to the alpha1,6 mannose of the trimannosyl core to form tri- and tetraantennary N-glycans and contains six putative N-linked sites.
15084511	3	95	theme	glycopeptides	994:1006	arg1	masses					980:985	the masses	976:985	the masses of the glycopeptides determined experimentally	976:1032	Mapping of the glycosylation sites was performed by enriching for trypsin-digested glycopeptides, followed by analysis of each fraction with Q-TOF MS. Predicted tryptic glycopeptides were identified by comparisons of theoretical masses of peptides with various glycan masses to the masses of the glycopeptides determined experimentally.
15084511	6	96	dep	Sites	1291:1295	arg1	Asn					1297:1299	Asn 433	1297:1303	Asn 433	1297:1303	Sites Asn 433 and 447 both contain structures that range from biantennary with two sialic acids to tetraantennary terminating with four sialic acids.
15084511	6	96	dep	Sites	1291:1295	arg1	447					1309:1311	447	1309:1311	447	1309:1311	Sites Asn 433 and 447 both contain structures that range from biantennary with two sialic acids to tetraantennary terminating with four sialic acids.
15084511	3	97	theme	sites	727:731	arg1	Mapping					698:704	Mapping	698:704	Mapping of the glycosylation sites	698:731	Mapping of the glycosylation sites was performed by enriching for trypsin-digested glycopeptides, followed by analysis of each fraction with Q-TOF MS. Predicted tryptic glycopeptides were identified by comparisons of theoretical masses of peptides with various glycan masses to the masses of the glycopeptides determined experimentally.
15084511	8	98	from	sites	1748:1752	arg1	protein					1766:1772	the same protein	1757:1772	the same protein during biosynthesis	1757:1792	The appearance of only biantennary glycans at site Asn 433, coupled with the appearance of more highly branched structures at Asn 334 and 447, demonstrates that biantennary acceptors present at different sites on the same protein during biosynthesis can differ in their accessibility for branching by GnT-V.
15084511	8	98	from	sites	1748:1752	arg1	present					1727:1733	present	1727:1733	present	1727:1733	The appearance of only biantennary glycans at site Asn 433, coupled with the appearance of more highly branched structures at Asn 334 and 447, demonstrates that biantennary acceptors present at different sites on the same protein during biosynthesis can differ in their accessibility for branching by GnT-V.
14749323	7	0	theme	important	1316:1324	arg1	acid					1332:1335	this important amino acid	1311:1335	this important amino acid critically involved in the substrate binding	1311:1380	Disrupting Asp-39 resulted in a complete loss of transport activity in both mOAT1 and hOAT1 without affecting their cell surface expression, suggesting that the loss of function is not because of deglycosylation of Asp-39 per se but rather is likely because of the change of this important amino acid critically involved in the substrate binding.
14749323	5	1	gly	glycosylation	734:746	arg2	sites					748:752	putative glycosylation sites	725:752	putative glycosylation sites	725:752	In the present study, we investigated the effect of disrupting putative glycosylation sites in mOAT1 as well as its human counterpart, hOAT1, by mutating asparagine to glutamine and assessing mutant transporters in HeLa cells.
14749323	7	2	theme	transport	1085:1093	arg1	activity					1095:1102	transport activity	1085:1102	transport activity	1085:1102	Disrupting Asp-39 resulted in a complete loss of transport activity in both mOAT1 and hOAT1 without affecting their cell surface expression, suggesting that the loss of function is not because of deglycosylation of Asp-39 per se but rather is likely because of the change of this important amino acid critically involved in the substrate binding.
14749323	11	3	theme	organic	2160:2166	arg1	family					2186:2191	the organic anion transporter family	2156:2191	the organic anion transporter family	2156:2191	This study is the first molecular identification and characterization of glycosylation of OAT1 and may provide important insights into the structure-function relationships of the organic anion transporter family.
14749323	6	4	from	site	931:934	arg1	mOAT1					946:950	mOAT1	946:950	mOAT1	946:950	We showed that the putative glycosylation site Asp-39 in mOAT1 was not glycosylated but the corresponding site (Asp-39) in hOAT1 was glycosylated.
14749323	8	5	gly	glycosylation	1484:1496	arg1	OAT					1539:1541	OAT function	1539:1550	OAT function	1539:1550	Single replacement of asparagines at other sites had no effect on transport activity indicating that glycosylation at individual sites is not essential for OAT function.
14749323	8	5	gly	glycosylation	1484:1496	arg1	sites					1512:1516	individual sites	1501:1516	individual sites	1501:1516	Single replacement of asparagines at other sites had no effect on transport activity indicating that glycosylation at individual sites is not essential for OAT function.
14749323	8	5	gly	glycosylation	1484:1496	arg2	sites					1512:1516	individual sites	1501:1516	individual sites	1501:1516	Single replacement of asparagines at other sites had no effect on transport activity indicating that glycosylation at individual sites is not essential for OAT function.
14749323	4	6	theme	glycosylation	465:477	arg1	tunicamycin					418:428	tunicamycin	418:428	tunicamycin	418:428	274, 1519-1524) that tunicamycin, an inhibitor of asparagine-linked glycosylation, significantly inhibited organic anion transport in COS-7 cells expressing a mouse organic anion transporter (mOAT1), suggesting an important role of glycosylation in mOAT1 function.
14749323	4	6	theme	glycosylation	465:477	arg1	inhibitor					434:442	an inhibitor	431:442	an inhibitor of asparagine-linked glycosylation	431:477	274, 1519-1524) that tunicamycin, an inhibitor of asparagine-linked glycosylation, significantly inhibited organic anion transport in COS-7 cells expressing a mouse organic anion transporter (mOAT1), suggesting an important role of glycosylation in mOAT1 function.
14749323	2	7	dep	K.	309:310	arg1	1999					376:379	1999	376:379	1999	376:379	We reported previously (Kuze, K., Graves, P., Leahy, A., Wilson, P., Stuhlmann, H., and You, G. (1999) J. Biol.
14749323	2	7	dep	K.	309:310	arg1	Biol					385:388	Biol	385:388	Biol	385:388	We reported previously (Kuze, K., Graves, P., Leahy, A., Wilson, P., Stuhlmann, H., and You, G. (1999) J. Biol.
14749323	5	8	from	transporters	861:872	arg1	cells					882:886	HeLa cells	877:886	HeLa cells	877:886	In the present study, we investigated the effect of disrupting putative glycosylation sites in mOAT1 as well as its human counterpart, hOAT1, by mutating asparagine to glutamine and assessing mutant transporters in HeLa cells.
14749323	11	9	theme	OAT1	2071:2074	arg1	glycosylation					2054:2066	glycosylation	2054:2066	glycosylation of OAT1	2054:2074	This study is the first molecular identification and characterization of glycosylation of OAT1 and may provide important insights into the structure-function relationships of the organic anion transporter family.
14749323	1	10	theme	important	153:161	arg1	drugs					171:175	clinically important anionic drugs	142:175	clinically important anionic drugs	142:175	Organic anion transporters (OAT) play essential roles in the body disposition of clinically important anionic drugs, including antiviral drugs, antitumor drugs, antibiotics, antihypertensives, and anti-inflammatories.
14749323	1	10	theme	important	153:161	arg1	drugs					215:219	antitumor drugs	205:219	antitumor drugs	205:219	Organic anion transporters (OAT) play essential roles in the body disposition of clinically important anionic drugs, including antiviral drugs, antitumor drugs, antibiotics, antihypertensives, and anti-inflammatories.
14749323	1	10	theme	important	153:161	arg1	anti-inflammatories					258:276	anti-inflammatories	258:276	anti-inflammatories	258:276	Organic anion transporters (OAT) play essential roles in the body disposition of clinically important anionic drugs, including antiviral drugs, antitumor drugs, antibiotics, antihypertensives, and anti-inflammatories.
14749323	1	10	theme	important	153:161	arg1	antibiotics					222:232	antibiotics	222:232	antibiotics	222:232	Organic anion transporters (OAT) play essential roles in the body disposition of clinically important anionic drugs, including antiviral drugs, antitumor drugs, antibiotics, antihypertensives, and anti-inflammatories.
14749323	1	10	theme	important	153:161	arg1	drugs					198:202	antiviral drugs	188:202	antiviral drugs	188:202	Organic anion transporters (OAT) play essential roles in the body disposition of clinically important anionic drugs, including antiviral drugs, antitumor drugs, antibiotics, antihypertensives, and anti-inflammatories.
14749323	1	10	theme	important	153:161	arg1	antihypertensives					235:251	antihypertensives	235:251	antihypertensives	235:251	Organic anion transporters (OAT) play essential roles in the body disposition of clinically important anionic drugs, including antiviral drugs, antitumor drugs, antibiotics, antihypertensives, and anti-inflammatories.
14749323	10	11	dep	required	1857:1864	arg1	2					1813:1813	2	1813:1813	2	1813:1813	In summary, we provided the evidence that 1) Asp-39 is crucially involved in substrate recognition of OAT1, 2) glycosylation at individual sites is not required for OAT1 function, and 3) glycosylation plays an important role in the targeting of OAT1 onto the plasma membrane.
14749323	7	12	theme	Asp-39	1251:1256	arg1	deglycosylation					1232:1246	deglycosylation	1232:1246	deglycosylation of Asp-39 per se	1232:1263	Disrupting Asp-39 resulted in a complete loss of transport activity in both mOAT1 and hOAT1 without affecting their cell surface expression, suggesting that the loss of function is not because of deglycosylation of Asp-39 per se but rather is likely because of the change of this important amino acid critically involved in the substrate binding.
14749323	11	13	theme	glycosylation	2054:2066	arg1	identification					2015:2028	first molecular identification	1999:2028	first molecular identification	1999:2028	This study is the first molecular identification and characterization of glycosylation of OAT1 and may provide important insights into the structure-function relationships of the organic anion transporter family.
14749323	11	13	theme	glycosylation	2054:2066	arg1	characterization					2034:2049	characterization	2034:2049	characterization	2034:2049	This study is the first molecular identification and characterization of glycosylation of OAT1 and may provide important insights into the structure-function relationships of the organic anion transporter family.
14749323	4	14	theme	mouse	556:560	arg1	transporter					576:586	a mouse organic anion transporter	554:586	a mouse organic anion transporter (mOAT1)	554:594	274, 1519-1524) that tunicamycin, an inhibitor of asparagine-linked glycosylation, significantly inhibited organic anion transport in COS-7 cells expressing a mouse organic anion transporter (mOAT1), suggesting an important role of glycosylation in mOAT1 function.
14749323	4	14	theme	mouse	556:560	arg1	mOAT1					589:593	mOAT1	589:593	mOAT1	589:593	274, 1519-1524) that tunicamycin, an inhibitor of asparagine-linked glycosylation, significantly inhibited organic anion transport in COS-7 cells expressing a mouse organic anion transporter (mOAT1), suggesting an important role of glycosylation in mOAT1 function.
14749323	10	15	theme	substrate	1782:1790	arg1	recognition					1792:1802	substrate recognition	1782:1802	substrate recognition of OAT1	1782:1810	In summary, we provided the evidence that 1) Asp-39 is crucially involved in substrate recognition of OAT1, 2) glycosylation at individual sites is not required for OAT1 function, and 3) glycosylation plays an important role in the targeting of OAT1 onto the plasma membrane.
14749323	5	16	theme	glycosylation	734:746	arg1	sites					748:752	putative glycosylation sites	725:752	putative glycosylation sites	725:752	In the present study, we investigated the effect of disrupting putative glycosylation sites in mOAT1 as well as its human counterpart, hOAT1, by mutating asparagine to glutamine and assessing mutant transporters in HeLa cells.
14749323	1	17	theme	drugs	171:175	arg1	disposition					127:137	the body disposition	118:137	the body disposition of clinically important anionic drugs, including antiviral drugs, antitumor drugs, antibiotics, antihypertensives, and anti-inflammatories	118:276	Organic anion transporters (OAT) play essential roles in the body disposition of clinically important anionic drugs, including antiviral drugs, antitumor drugs, antibiotics, antihypertensives, and anti-inflammatories.
14749323	11	18	theme	important	2092:2100	arg1	insights					2102:2109	important insights	2092:2109	important insights into the structure-function relationships of the organic anion transporter family	2092:2191	This study is the first molecular identification and characterization of glycosylation of OAT1 and may provide important insights into the structure-function relationships of the organic anion transporter family.
14749323	4	19	from	transport	518:526	arg1	cells					537:541	COS-7 cells	531:541	COS-7 cells expressing a mouse organic anion transporter (mOAT1)	531:594	274, 1519-1524) that tunicamycin, an inhibitor of asparagine-linked glycosylation, significantly inhibited organic anion transport in COS-7 cells expressing a mouse organic anion transporter (mOAT1), suggesting an important role of glycosylation in mOAT1 function.
14749323	1	20	theme	essential	99:107	arg1	roles					109:113	essential roles	99:113	essential roles	99:113	Organic anion transporters (OAT) play essential roles in the body disposition of clinically important anionic drugs, including antiviral drugs, antitumor drugs, antibiotics, antihypertensives, and anti-inflammatories.
14749323	4	21	theme	COS-7	531:535	arg1	cells					537:541	COS-7 cells	531:541	COS-7 cells expressing a mouse organic anion transporter (mOAT1)	531:594	274, 1519-1524) that tunicamycin, an inhibitor of asparagine-linked glycosylation, significantly inhibited organic anion transport in COS-7 cells expressing a mouse organic anion transporter (mOAT1), suggesting an important role of glycosylation in mOAT1 function.
14749323	5	22	theme	human	778:782	arg1	hOAT1					797:801	hOAT1	797:801	hOAT1	797:801	In the present study, we investigated the effect of disrupting putative glycosylation sites in mOAT1 as well as its human counterpart, hOAT1, by mutating asparagine to glutamine and assessing mutant transporters in HeLa cells.
14749323	5	22	theme	human	778:782	arg1	counterpart					784:794	its human counterpart	774:794	its human counterpart	774:794	In the present study, we investigated the effect of disrupting putative glycosylation sites in mOAT1 as well as its human counterpart, hOAT1, by mutating asparagine to glutamine and assessing mutant transporters in HeLa cells.
14749323	7	23	theme	cell	1152:1155	arg1	expression					1165:1174	their cell surface expression	1146:1174	their cell surface expression	1146:1174	Disrupting Asp-39 resulted in a complete loss of transport activity in both mOAT1 and hOAT1 without affecting their cell surface expression, suggesting that the loss of function is not because of deglycosylation of Asp-39 per se but rather is likely because of the change of this important amino acid critically involved in the substrate binding.
14749323	4	24	theme	anion	570:574	arg1	transporter					576:586	a mouse organic anion transporter	554:586	a mouse organic anion transporter (mOAT1)	554:594	274, 1519-1524) that tunicamycin, an inhibitor of asparagine-linked glycosylation, significantly inhibited organic anion transport in COS-7 cells expressing a mouse organic anion transporter (mOAT1), suggesting an important role of glycosylation in mOAT1 function.
14749323	4	24	theme	anion	570:574	arg1	mOAT1					589:593	mOAT1	589:593	mOAT1	589:593	274, 1519-1524) that tunicamycin, an inhibitor of asparagine-linked glycosylation, significantly inhibited organic anion transport in COS-7 cells expressing a mouse organic anion transporter (mOAT1), suggesting an important role of glycosylation in mOAT1 function.
14749323	1	25	theme	body	122:125	arg1	disposition					127:137	the body disposition	118:137	the body disposition of clinically important anionic drugs, including antiviral drugs, antitumor drugs, antibiotics, antihypertensives, and anti-inflammatories	118:276	Organic anion transporters (OAT) play essential roles in the body disposition of clinically important anionic drugs, including antiviral drugs, antitumor drugs, antibiotics, antihypertensives, and anti-inflammatories.
14749323	10	26	theme	plasma	1964:1969	arg1	membrane					1971:1978	the plasma membrane	1960:1978	the plasma membrane	1960:1978	In summary, we provided the evidence that 1) Asp-39 is crucially involved in substrate recognition of OAT1, 2) glycosylation at individual sites is not required for OAT1 function, and 3) glycosylation plays an important role in the targeting of OAT1 onto the plasma membrane.
14749323	7	27	theme	complete	1068:1075	arg1	loss					1077:1080	a complete loss	1066:1080	a complete loss of transport activity	1066:1102	Disrupting Asp-39 resulted in a complete loss of transport activity in both mOAT1 and hOAT1 without affecting their cell surface expression, suggesting that the loss of function is not because of deglycosylation of Asp-39 per se but rather is likely because of the change of this important amino acid critically involved in the substrate binding.
14749323	0	28	from	Role	0:3	arg1	OAT1					55:58	the organic anion transporter OAT1	25:58	the organic anion transporter OAT1	25:58	Role of glycosylation in the organic anion transporter OAT1.
14749323	8	29	from	sites	1512:1516	arg1	glycosylation					1484:1496	glycosylation	1484:1496	glycosylation at individual sites	1484:1516	Single replacement of asparagines at other sites had no effect on transport activity indicating that glycosylation at individual sites is not essential for OAT function.
14749323	11	30	theme	molecular	2005:2013	arg1	identification					2015:2028	first molecular identification	1999:2028	first molecular identification	1999:2028	This study is the first molecular identification and characterization of glycosylation of OAT1 and may provide important insights into the structure-function relationships of the organic anion transporter family.
14749323	11	31	theme	transporter	2174:2184	arg1	family					2186:2191	the organic anion transporter family	2156:2191	the organic anion transporter family	2156:2191	This study is the first molecular identification and characterization of glycosylation of OAT1 and may provide important insights into the structure-function relationships of the organic anion transporter family.
14749323	1	32	theme	anion	69:73	arg1	OAT					89:91	OAT	89:91	OAT	89:91	Organic anion transporters (OAT) play essential roles in the body disposition of clinically important anionic drugs, including antiviral drugs, antitumor drugs, antibiotics, antihypertensives, and anti-inflammatories.
14749323	1	32	theme	anion	69:73	arg1	transporters					75:86	Organic anion transporters	61:86	Organic anion transporters (OAT)	61:92	Organic anion transporters (OAT) play essential roles in the body disposition of clinically important anionic drugs, including antiviral drugs, antitumor drugs, antibiotics, antihypertensives, and anti-inflammatories.
14749323	4	33	theme	important	611:619	arg1	role					621:624	an important role	608:624	an important role of glycosylation in mOAT1 function	608:659	274, 1519-1524) that tunicamycin, an inhibitor of asparagine-linked glycosylation, significantly inhibited organic anion transport in COS-7 cells expressing a mouse organic anion transporter (mOAT1), suggesting an important role of glycosylation in mOAT1 function.
14749323	6	34	theme	glycosylation	917:929	arg1	site					931:934	the putative glycosylation site Asp-39	904:941	the putative glycosylation site Asp-39 in mOAT1	904:950	We showed that the putative glycosylation site Asp-39 in mOAT1 was not glycosylated but the corresponding site (Asp-39) in hOAT1 was glycosylated.
14749323	0	35	theme	glycosylation	8:20	arg1	Role					0:3	Role	0:3	Role of glycosylation in the organic anion transporter OAT1.	0:59	Role of glycosylation in the organic anion transporter OAT1.
14749323	7	36	theme	substrate	1364:1372	arg1	binding					1374:1380	the substrate binding	1360:1380	the substrate binding	1360:1380	Disrupting Asp-39 resulted in a complete loss of transport activity in both mOAT1 and hOAT1 without affecting their cell surface expression, suggesting that the loss of function is not because of deglycosylation of Asp-39 per se but rather is likely because of the change of this important amino acid critically involved in the substrate binding.
14749323	7	37	theme	surface	1157:1163	arg1	expression					1165:1174	their cell surface expression	1146:1174	their cell surface expression	1146:1174	Disrupting Asp-39 resulted in a complete loss of transport activity in both mOAT1 and hOAT1 without affecting their cell surface expression, suggesting that the loss of function is not because of deglycosylation of Asp-39 per se but rather is likely because of the change of this important amino acid critically involved in the substrate binding.
14749323	9	38	theme	transporters	1668:1679	arg1	trafficking					1649:1659	the trafficking	1645:1659	the trafficking of the transporters to the plasma membrane	1645:1702	In contrast, a simultaneous replacement of all asparagines in both mOAT1 and hOAT1 impaired the trafficking of the transporters to the plasma membrane.
14749323	8	39	theme	asparagines	1405:1415	arg1	replacement					1390:1400	Single replacement	1383:1400	Single replacement of asparagines at other sites	1383:1430	Single replacement of asparagines at other sites had no effect on transport activity indicating that glycosylation at individual sites is not essential for OAT function.
14749323	5	40	theme	present	669:675	arg1	study					677:681	the present study	665:681	the present study	665:681	In the present study, we investigated the effect of disrupting putative glycosylation sites in mOAT1 as well as its human counterpart, hOAT1, by mutating asparagine to glutamine and assessing mutant transporters in HeLa cells.
14749323	6	41	theme	corresponding	981:993	arg1	Asp-39					1001:1006	Asp-39	1001:1006	Asp-39	1001:1006	We showed that the putative glycosylation site Asp-39 in mOAT1 was not glycosylated but the corresponding site (Asp-39) in hOAT1 was glycosylated.
14749323	6	41	theme	corresponding	981:993	arg1	site					995:998	the corresponding site	977:998	the corresponding site (Asp-39) in hOAT1	977:1016	We showed that the putative glycosylation site Asp-39 in mOAT1 was not glycosylated but the corresponding site (Asp-39) in hOAT1 was glycosylated.
14749323	8	42	theme	other	1420:1424	arg1	sites					1426:1430	other sites	1420:1430	other sites	1420:1430	Single replacement of asparagines at other sites had no effect on transport activity indicating that glycosylation at individual sites is not essential for OAT function.
14749323	6	43	gly	glycosylation	917:929	arg2	site					931:934	the putative glycosylation site Asp-39	904:941	the putative glycosylation site Asp-39 in mOAT1	904:950	We showed that the putative glycosylation site Asp-39 in mOAT1 was not glycosylated but the corresponding site (Asp-39) in hOAT1 was glycosylated.
14749323	6	43	gly	glycosylation	917:929	arg2	Asp-39					936:941	Asp-39	936:941	Asp-39	936:941	We showed that the putative glycosylation site Asp-39 in mOAT1 was not glycosylated but the corresponding site (Asp-39) in hOAT1 was glycosylated.
14749323	9	44	from	replacement	1581:1591	arg1	hOAT1					1630:1634	hOAT1	1630:1634	hOAT1	1630:1634	In contrast, a simultaneous replacement of all asparagines in both mOAT1 and hOAT1 impaired the trafficking of the transporters to the plasma membrane.
14749323	9	44	from	replacement	1581:1591	arg1	mOAT1					1620:1624	mOAT1	1620:1624	mOAT1	1620:1624	In contrast, a simultaneous replacement of all asparagines in both mOAT1 and hOAT1 impaired the trafficking of the transporters to the plasma membrane.
14749323	5	45	theme	mutant	854:859	arg1	transporters					861:872	mutant transporters	854:872	mutant transporters in HeLa cells	854:886	In the present study, we investigated the effect of disrupting putative glycosylation sites in mOAT1 as well as its human counterpart, hOAT1, by mutating asparagine to glutamine and assessing mutant transporters in HeLa cells.
14749323	10	46	dep	plays	1906:1910	arg1	3					1889:1889	3	1889:1889	3	1889:1889	In summary, we provided the evidence that 1) Asp-39 is crucially involved in substrate recognition of OAT1, 2) glycosylation at individual sites is not required for OAT1 function, and 3) glycosylation plays an important role in the targeting of OAT1 onto the plasma membrane.
14749323	8	47	theme	individual	1501:1510	arg1	sites					1512:1516	individual sites	1501:1516	individual sites	1501:1516	Single replacement of asparagines at other sites had no effect on transport activity indicating that glycosylation at individual sites is not essential for OAT function.
14749323	7	48	gly	deglycosylation	1232:1246	arg1	Asp-39					1251:1256	Asp-39	1251:1256	Asp-39	1251:1256	Disrupting Asp-39 resulted in a complete loss of transport activity in both mOAT1 and hOAT1 without affecting their cell surface expression, suggesting that the loss of function is not because of deglycosylation of Asp-39 per se but rather is likely because of the change of this important amino acid critically involved in the substrate binding.
14749323	7	49	theme	activity	1095:1102	arg1	loss					1077:1080	a complete loss	1066:1080	a complete loss of transport activity	1066:1102	Disrupting Asp-39 resulted in a complete loss of transport activity in both mOAT1 and hOAT1 without affecting their cell surface expression, suggesting that the loss of function is not because of deglycosylation of Asp-39 per se but rather is likely because of the change of this important amino acid critically involved in the substrate binding.
14749323	8	50	theme	transport	1449:1457	arg1	activity					1459:1466	transport activity	1449:1466	transport activity indicating that glycosylation at individual sites is not essential for OAT function	1449:1550	Single replacement of asparagines at other sites had no effect on transport activity indicating that glycosylation at individual sites is not essential for OAT function.
14749323	10	51	theme	important	1915:1923	arg1	role					1925:1928	an important role	1912:1928	an important role	1912:1928	In summary, we provided the evidence that 1) Asp-39 is crucially involved in substrate recognition of OAT1, 2) glycosylation at individual sites is not required for OAT1 function, and 3) glycosylation plays an important role in the targeting of OAT1 onto the plasma membrane.
14749323	4	52	theme	asparagine-linked	447:463	arg1	glycosylation					465:477	asparagine-linked glycosylation	447:477	asparagine-linked glycosylation	447:477	274, 1519-1524) that tunicamycin, an inhibitor of asparagine-linked glycosylation, significantly inhibited organic anion transport in COS-7 cells expressing a mouse organic anion transporter (mOAT1), suggesting an important role of glycosylation in mOAT1 function.
14749323	8	53	from	sites	1426:1430	arg1	replacement					1390:1400	Single replacement	1383:1400	Single replacement of asparagines at other sites	1383:1430	Single replacement of asparagines at other sites had no effect on transport activity indicating that glycosylation at individual sites is not essential for OAT function.
14749323	8	54	theme	OAT	1539:1541	arg1	function					1543:1550	OAT function	1539:1550	OAT function	1539:1550	Single replacement of asparagines at other sites had no effect on transport activity indicating that glycosylation at individual sites is not essential for OAT function.
14749323	5	55	theme	putative	725:732	arg1	sites					748:752	putative glycosylation sites	725:752	putative glycosylation sites	725:752	In the present study, we investigated the effect of disrupting putative glycosylation sites in mOAT1 as well as its human counterpart, hOAT1, by mutating asparagine to glutamine and assessing mutant transporters in HeLa cells.
14749323	0	56	theme	anion	37:41	arg1	OAT1					55:58	the organic anion transporter OAT1	25:58	the organic anion transporter OAT1	25:58	Role of glycosylation in the organic anion transporter OAT1.
14749323	1	57	theme	anionic	163:169	arg1	drugs					171:175	clinically important anionic drugs	142:175	clinically important anionic drugs	142:175	Organic anion transporters (OAT) play essential roles in the body disposition of clinically important anionic drugs, including antiviral drugs, antitumor drugs, antibiotics, antihypertensives, and anti-inflammatories.
14749323	1	57	theme	anionic	163:169	arg1	drugs					215:219	antitumor drugs	205:219	antitumor drugs	205:219	Organic anion transporters (OAT) play essential roles in the body disposition of clinically important anionic drugs, including antiviral drugs, antitumor drugs, antibiotics, antihypertensives, and anti-inflammatories.
14749323	1	57	theme	anionic	163:169	arg1	anti-inflammatories					258:276	anti-inflammatories	258:276	anti-inflammatories	258:276	Organic anion transporters (OAT) play essential roles in the body disposition of clinically important anionic drugs, including antiviral drugs, antitumor drugs, antibiotics, antihypertensives, and anti-inflammatories.
14749323	1	57	theme	anionic	163:169	arg1	antibiotics					222:232	antibiotics	222:232	antibiotics	222:232	Organic anion transporters (OAT) play essential roles in the body disposition of clinically important anionic drugs, including antiviral drugs, antitumor drugs, antibiotics, antihypertensives, and anti-inflammatories.
14749323	1	57	theme	anionic	163:169	arg1	drugs					198:202	antiviral drugs	188:202	antiviral drugs	188:202	Organic anion transporters (OAT) play essential roles in the body disposition of clinically important anionic drugs, including antiviral drugs, antitumor drugs, antibiotics, antihypertensives, and anti-inflammatories.
14749323	1	57	theme	anionic	163:169	arg1	antihypertensives					235:251	antihypertensives	235:251	antihypertensives	235:251	Organic anion transporters (OAT) play essential roles in the body disposition of clinically important anionic drugs, including antiviral drugs, antitumor drugs, antibiotics, antihypertensives, and anti-inflammatories.
14749323	11	58	theme	structure-function	2120:2137	arg1	relationships					2139:2151	the structure-function relationships	2116:2151	the structure-function relationships of the organic anion transporter family	2116:2191	This study is the first molecular identification and characterization of glycosylation of OAT1 and may provide important insights into the structure-function relationships of the organic anion transporter family.
14749323	4	59	theme	anion	512:516	arg1	transport					518:526	organic anion transport	504:526	organic anion transport in COS-7 cells expressing a mouse organic anion transporter (mOAT1)	504:594	274, 1519-1524) that tunicamycin, an inhibitor of asparagine-linked glycosylation, significantly inhibited organic anion transport in COS-7 cells expressing a mouse organic anion transporter (mOAT1), suggesting an important role of glycosylation in mOAT1 function.
14749323	6	60	gly	glycosylated	1022:1033	arg1	Asp-39					1001:1006	Asp-39	1001:1006	Asp-39	1001:1006	We showed that the putative glycosylation site Asp-39 in mOAT1 was not glycosylated but the corresponding site (Asp-39) in hOAT1 was glycosylated.
14749323	6	60	gly	glycosylated	1022:1033	arg1	site					995:998	the corresponding site	977:998	the corresponding site (Asp-39) in hOAT1	977:1016	We showed that the putative glycosylation site Asp-39 in mOAT1 was not glycosylated but the corresponding site (Asp-39) in hOAT1 was glycosylated.
14749323	1	61	theme	antiviral	188:196	arg1	drugs					198:202	antiviral drugs	188:202	antiviral drugs	188:202	Organic anion transporters (OAT) play essential roles in the body disposition of clinically important anionic drugs, including antiviral drugs, antitumor drugs, antibiotics, antihypertensives, and anti-inflammatories.
14749323	10	62	theme	OAT1	1807:1810	arg1	recognition					1792:1802	substrate recognition	1782:1802	substrate recognition of OAT1	1782:1810	In summary, we provided the evidence that 1) Asp-39 is crucially involved in substrate recognition of OAT1, 2) glycosylation at individual sites is not required for OAT1 function, and 3) glycosylation plays an important role in the targeting of OAT1 onto the plasma membrane.
14749323	10	63	theme	OAT1	1950:1953	arg1	targeting					1937:1945	the targeting	1933:1945	the targeting of OAT1 onto the plasma membrane	1933:1978	In summary, we provided the evidence that 1) Asp-39 is crucially involved in substrate recognition of OAT1, 2) glycosylation at individual sites is not required for OAT1 function, and 3) glycosylation plays an important role in the targeting of OAT1 onto the plasma membrane.
14749323	2	64	dep	reported	282:289	arg1	H.					359:360	H.	359:360	H.	359:360	We reported previously (Kuze, K., Graves, P., Leahy, A., Wilson, P., Stuhlmann, H., and You, G. (1999) J. Biol.
14749323	2	64	dep	reported	282:289	arg1	P.					321:322	P.	321:322	P.	321:322	We reported previously (Kuze, K., Graves, P., Leahy, A., Wilson, P., Stuhlmann, H., and You, G. (1999) J. Biol.
14749323	2	64	dep	reported	282:289	arg1	P.					344:345	P.	344:345	P.	344:345	We reported previously (Kuze, K., Graves, P., Leahy, A., Wilson, P., Stuhlmann, H., and You, G. (1999) J. Biol.
14749323	2	64	dep	reported	282:289	arg1	K.					309:310	K.	309:310	K.	309:310	We reported previously (Kuze, K., Graves, P., Leahy, A., Wilson, P., Stuhlmann, H., and You, G. (1999) J. Biol.
14749323	2	64	dep	reported	282:289	arg1	You					367:369	You	367:369	You	367:369	We reported previously (Kuze, K., Graves, P., Leahy, A., Wilson, P., Stuhlmann, H., and You, G. (1999) J. Biol.
14749323	2	64	dep	reported	282:289	arg1	Graves					313:318	Graves	313:318	Graves	313:318	We reported previously (Kuze, K., Graves, P., Leahy, A., Wilson, P., Stuhlmann, H., and You, G. (1999) J. Biol.
14749323	2	64	dep	reported	282:289	arg1	G					372:372	G	372:372	G	372:372	We reported previously (Kuze, K., Graves, P., Leahy, A., Wilson, P., Stuhlmann, H., and You, G. (1999) J. Biol.
14749323	2	64	dep	reported	282:289	arg1	A.					332:333	A.	332:333	A.	332:333	We reported previously (Kuze, K., Graves, P., Leahy, A., Wilson, P., Stuhlmann, H., and You, G. (1999) J. Biol.
14749323	9	65	theme	simultaneous	1568:1579	arg1	replacement					1581:1591	a simultaneous replacement	1566:1591	a simultaneous replacement of all asparagines in both mOAT1 and hOAT1	1566:1634	In contrast, a simultaneous replacement of all asparagines in both mOAT1 and hOAT1 impaired the trafficking of the transporters to the plasma membrane.
14749323	7	66	theme	function	1205:1212	arg1	loss					1197:1200	the loss	1193:1200	the loss of function	1193:1212	Disrupting Asp-39 resulted in a complete loss of transport activity in both mOAT1 and hOAT1 without affecting their cell surface expression, suggesting that the loss of function is not because of deglycosylation of Asp-39 per se but rather is likely because of the change of this important amino acid critically involved in the substrate binding.
14749323	4	67	gly	glycosylation	629:641	arg1	mOAT1					646:650	mOAT1 function	646:659	mOAT1 function	646:659	274, 1519-1524) that tunicamycin, an inhibitor of asparagine-linked glycosylation, significantly inhibited organic anion transport in COS-7 cells expressing a mouse organic anion transporter (mOAT1), suggesting an important role of glycosylation in mOAT1 function.
14749323	9	68	theme	plasma	1688:1693	arg1	membrane					1695:1702	the plasma membrane	1684:1702	the plasma membrane	1684:1702	In contrast, a simultaneous replacement of all asparagines in both mOAT1 and hOAT1 impaired the trafficking of the transporters to the plasma membrane.
14749323	11	69	theme	first	1999:2003	arg1	identification					2015:2028	first molecular identification	1999:2028	first molecular identification	1999:2028	This study is the first molecular identification and characterization of glycosylation of OAT1 and may provide important insights into the structure-function relationships of the organic anion transporter family.
14749323	4	70	theme	organic	562:568	arg1	transporter					576:586	a mouse organic anion transporter	554:586	a mouse organic anion transporter (mOAT1)	554:594	274, 1519-1524) that tunicamycin, an inhibitor of asparagine-linked glycosylation, significantly inhibited organic anion transport in COS-7 cells expressing a mouse organic anion transporter (mOAT1), suggesting an important role of glycosylation in mOAT1 function.
14749323	4	70	theme	organic	562:568	arg1	mOAT1					589:593	mOAT1	589:593	mOAT1	589:593	274, 1519-1524) that tunicamycin, an inhibitor of asparagine-linked glycosylation, significantly inhibited organic anion transport in COS-7 cells expressing a mouse organic anion transporter (mOAT1), suggesting an important role of glycosylation in mOAT1 function.
14749323	9	71	theme	asparagines	1600:1610	arg1	replacement					1581:1591	a simultaneous replacement	1566:1591	a simultaneous replacement of all asparagines in both mOAT1 and hOAT1	1566:1634	In contrast, a simultaneous replacement of all asparagines in both mOAT1 and hOAT1 impaired the trafficking of the transporters to the plasma membrane.
14749323	6	72	gly	glycosylated	960:971	arg1	site					931:934	the putative glycosylation site Asp-39	904:941	the putative glycosylation site Asp-39 in mOAT1	904:950	We showed that the putative glycosylation site Asp-39 in mOAT1 was not glycosylated but the corresponding site (Asp-39) in hOAT1 was glycosylated.
14749323	11	73	theme	family	2186:2191	arg1	relationships					2139:2151	the structure-function relationships	2116:2151	the structure-function relationships of the organic anion transporter family	2116:2191	This study is the first molecular identification and characterization of glycosylation of OAT1 and may provide important insights into the structure-function relationships of the organic anion transporter family.
14749323	7	74	theme	amino	1326:1330	arg1	acid					1332:1335	this important amino acid	1311:1335	this important amino acid critically involved in the substrate binding	1311:1380	Disrupting Asp-39 resulted in a complete loss of transport activity in both mOAT1 and hOAT1 without affecting their cell surface expression, suggesting that the loss of function is not because of deglycosylation of Asp-39 per se but rather is likely because of the change of this important amino acid critically involved in the substrate binding.
14749323	4	75	dep	274	397:399	arg1	1519-1524					402:410	1519-1524	402:410	1519-1524	402:410	274, 1519-1524) that tunicamycin, an inhibitor of asparagine-linked glycosylation, significantly inhibited organic anion transport in COS-7 cells expressing a mouse organic anion transporter (mOAT1), suggesting an important role of glycosylation in mOAT1 function.
14749323	10	76	dep	involved	1770:1777	arg1	1					1747:1747	1	1747:1747	1	1747:1747	In summary, we provided the evidence that 1) Asp-39 is crucially involved in substrate recognition of OAT1, 2) glycosylation at individual sites is not required for OAT1 function, and 3) glycosylation plays an important role in the targeting of OAT1 onto the plasma membrane.
14749323	11	77	theme	anion	2168:2172	arg1	family					2186:2191	the organic anion transporter family	2156:2191	the organic anion transporter family	2156:2191	This study is the first molecular identification and characterization of glycosylation of OAT1 and may provide important insights into the structure-function relationships of the organic anion transporter family.
14749323	4	78	theme	glycosylation	629:641	arg1	role					621:624	an important role	608:624	an important role of glycosylation in mOAT1 function	608:659	274, 1519-1524) that tunicamycin, an inhibitor of asparagine-linked glycosylation, significantly inhibited organic anion transport in COS-7 cells expressing a mouse organic anion transporter (mOAT1), suggesting an important role of glycosylation in mOAT1 function.
14749323	10	79	theme	individual	1833:1842	arg1	sites					1844:1848	individual sites	1833:1848	individual sites	1833:1848	In summary, we provided the evidence that 1) Asp-39 is crucially involved in substrate recognition of OAT1, 2) glycosylation at individual sites is not required for OAT1 function, and 3) glycosylation plays an important role in the targeting of OAT1 onto the plasma membrane.
14749323	1	80	theme	Organic	61:67	arg1	OAT					89:91	OAT	89:91	OAT	89:91	Organic anion transporters (OAT) play essential roles in the body disposition of clinically important anionic drugs, including antiviral drugs, antitumor drugs, antibiotics, antihypertensives, and anti-inflammatories.
14749323	1	80	theme	Organic	61:67	arg1	transporters					75:86	Organic anion transporters	61:86	Organic anion transporters (OAT)	61:92	Organic anion transporters (OAT) play essential roles in the body disposition of clinically important anionic drugs, including antiviral drugs, antitumor drugs, antibiotics, antihypertensives, and anti-inflammatories.
14749323	4	81	theme	mOAT1	646:650	arg1	function					652:659	mOAT1 function	646:659	mOAT1 function	646:659	274, 1519-1524) that tunicamycin, an inhibitor of asparagine-linked glycosylation, significantly inhibited organic anion transport in COS-7 cells expressing a mouse organic anion transporter (mOAT1), suggesting an important role of glycosylation in mOAT1 function.
14749323	11	82	gly	glycosylation	2054:2066	arg1	OAT1					2071:2074	OAT1	2071:2074	OAT1	2071:2074	This study is the first molecular identification and characterization of glycosylation of OAT1 and may provide important insights into the structure-function relationships of the organic anion transporter family.
14749323	4	83	from	role	621:624	arg1	function					652:659	mOAT1 function	646:659	mOAT1 function	646:659	274, 1519-1524) that tunicamycin, an inhibitor of asparagine-linked glycosylation, significantly inhibited organic anion transport in COS-7 cells expressing a mouse organic anion transporter (mOAT1), suggesting an important role of glycosylation in mOAT1 function.
14749323	4	84	dep	suggesting	597:606	arg1	inhibited					494:502	inhibited	494:502	inhibited organic anion transport in COS-7 cells expressing a mouse organic anion transporter (mOAT1)	494:594	274, 1519-1524) that tunicamycin, an inhibitor of asparagine-linked glycosylation, significantly inhibited organic anion transport in COS-7 cells expressing a mouse organic anion transporter (mOAT1), suggesting an important role of glycosylation in mOAT1 function.
14749323	8	85	theme	Single	1383:1388	arg1	replacement					1390:1400	Single replacement	1383:1400	Single replacement of asparagines at other sites	1383:1430	Single replacement of asparagines at other sites had no effect on transport activity indicating that glycosylation at individual sites is not essential for OAT function.
14749323	8	86	contain	had	1432:1434	arg1	replacement					1390:1400	Single replacement	1383:1400	Single replacement of asparagines at other sites	1383:1430	Single replacement of asparagines at other sites had no effect on transport activity indicating that glycosylation at individual sites is not essential for OAT function.
14749323	8	86	contain	had	1432:1434	arg2	effect					1439:1444	no effect	1436:1444	no effect	1436:1444	Single replacement of asparagines at other sites had no effect on transport activity indicating that glycosylation at individual sites is not essential for OAT function.
14749323	6	87	theme	putative	908:915	arg1	site					931:934	the putative glycosylation site Asp-39	904:941	the putative glycosylation site Asp-39 in mOAT1	904:950	We showed that the putative glycosylation site Asp-39 in mOAT1 was not glycosylated but the corresponding site (Asp-39) in hOAT1 was glycosylated.
14749323	0	88	theme	organic	29:35	arg1	OAT1					55:58	the organic anion transporter OAT1	25:58	the organic anion transporter OAT1	25:58	Role of glycosylation in the organic anion transporter OAT1.
14749323	5	89	theme	HeLa	877:880	arg1	cells					882:886	HeLa cells	877:886	HeLa cells	877:886	In the present study, we investigated the effect of disrupting putative glycosylation sites in mOAT1 as well as its human counterpart, hOAT1, by mutating asparagine to glutamine and assessing mutant transporters in HeLa cells.
14749323	0	90	theme	transporter	43:53	arg1	OAT1					55:58	the organic anion transporter OAT1	25:58	the organic anion transporter OAT1	25:58	Role of glycosylation in the organic anion transporter OAT1.
14749323	10	91	from	sites	1844:1848	arg1	glycosylation					1816:1828	glycosylation	1816:1828	glycosylation at individual sites	1816:1848	In summary, we provided the evidence that 1) Asp-39 is crucially involved in substrate recognition of OAT1, 2) glycosylation at individual sites is not required for OAT1 function, and 3) glycosylation plays an important role in the targeting of OAT1 onto the plasma membrane.
14749323	0	92	gly	glycosylation	8:20	arg1	anion					37:41	the organic anion transporter OAT1	25:58	the organic anion transporter OAT1	25:58	Role of glycosylation in the organic anion transporter OAT1.
14749323	0	92	gly	glycosylation	8:20	arg1	transporter					43:53	the organic anion transporter OAT1	25:58	the organic anion transporter OAT1	25:58	Role of glycosylation in the organic anion transporter OAT1.
14749323	11	93	dep	identification	2015:2028	arg1	the					1995:1997	the	1995:1997	the	1995:1997	This study is the first molecular identification and characterization of glycosylation of OAT1 and may provide important insights into the structure-function relationships of the organic anion transporter family.
14749323	6	94	from	site	995:998	arg1	hOAT1					1012:1016	hOAT1	1012:1016	hOAT1	1012:1016	We showed that the putative glycosylation site Asp-39 in mOAT1 was not glycosylated but the corresponding site (Asp-39) in hOAT1 was glycosylated.
14749323	4	95	link	asparagine-linked	447:463	arg1	glycosylation					465:477	asparagine-linked glycosylation	447:477	asparagine-linked glycosylation	447:477	274, 1519-1524) that tunicamycin, an inhibitor of asparagine-linked glycosylation, significantly inhibited organic anion transport in COS-7 cells expressing a mouse organic anion transporter (mOAT1), suggesting an important role of glycosylation in mOAT1 function.
14749323	10	96	gly	glycosylation	1816:1828	arg1	OAT1					1870:1873	OAT1 function	1870:1882	OAT1 function	1870:1882	In summary, we provided the evidence that 1) Asp-39 is crucially involved in substrate recognition of OAT1, 2) glycosylation at individual sites is not required for OAT1 function, and 3) glycosylation plays an important role in the targeting of OAT1 onto the plasma membrane.
14749323	10	96	gly	glycosylation	1816:1828	arg1	sites					1844:1848	individual sites	1833:1848	individual sites	1833:1848	In summary, we provided the evidence that 1) Asp-39 is crucially involved in substrate recognition of OAT1, 2) glycosylation at individual sites is not required for OAT1 function, and 3) glycosylation plays an important role in the targeting of OAT1 onto the plasma membrane.
14749323	10	96	gly	glycosylation	1816:1828	arg2	sites					1844:1848	individual sites	1833:1848	individual sites	1833:1848	In summary, we provided the evidence that 1) Asp-39 is crucially involved in substrate recognition of OAT1, 2) glycosylation at individual sites is not required for OAT1 function, and 3) glycosylation plays an important role in the targeting of OAT1 onto the plasma membrane.
14749323	10	97	theme	OAT1	1870:1873	arg1	function					1875:1882	OAT1 function	1870:1882	OAT1 function	1870:1882	In summary, we provided the evidence that 1) Asp-39 is crucially involved in substrate recognition of OAT1, 2) glycosylation at individual sites is not required for OAT1 function, and 3) glycosylation plays an important role in the targeting of OAT1 onto the plasma membrane.
14749323	1	98	theme	antitumor	205:213	arg1	drugs					215:219	antitumor drugs	205:219	antitumor drugs	205:219	Organic anion transporters (OAT) play essential roles in the body disposition of clinically important anionic drugs, including antiviral drugs, antitumor drugs, antibiotics, antihypertensives, and anti-inflammatories.
14749323	7	99	theme	acid	1332:1335	arg1	change					1301:1306	the change	1297:1306	the change of this important amino acid critically involved in the substrate binding	1297:1380	Disrupting Asp-39 resulted in a complete loss of transport activity in both mOAT1 and hOAT1 without affecting their cell surface expression, suggesting that the loss of function is not because of deglycosylation of Asp-39 per se but rather is likely because of the change of this important amino acid critically involved in the substrate binding.
14749323	4	100	theme	organic	504:510	arg1	transport					518:526	organic anion transport	504:526	organic anion transport in COS-7 cells expressing a mouse organic anion transporter (mOAT1)	504:594	274, 1519-1524) that tunicamycin, an inhibitor of asparagine-linked glycosylation, significantly inhibited organic anion transport in COS-7 cells expressing a mouse organic anion transporter (mOAT1), suggesting an important role of glycosylation in mOAT1 function.
19909340	6	0	theme	variant	1101:1107	arg1	protein					1109:1115	the resulting variant protein	1087:1115	the resulting variant protein	1087:1115	When Asn596 was converted to Gln596, the resulting variant protein was not glycosylated, and its protein level was about one-third of the wild type level in Flp-In-293 cells.
19909340	0	1	link	N-linked	14:21	arg1	glycosylation					23:35	N-linked glycosylation	14:35	N-linked glycosylation	14:35	Disruption of N-linked glycosylation enhances ubiquitin-mediated proteasomal degradation of the human ATP-binding cassette transporter ABCG2.
19909340	9	2	theme	ABCG2	1601:1605	arg1	protein					1613:1619	ABCG2 N596Q protein	1601:1619	ABCG2 N596Q protein	1601:1619	Immunofluorescence microscopy demonstrated that treatment with MG132 increased the level of ABCG2 N596Q protein both in intracellular compartments and in the plasma membrane.
19909340	3	3	theme	N-linked	552:559	arg1	glycan					561:566	the N-linked glycan	548:566	the N-linked glycan	548:566	In the present study, we aimed to analyze quantitatively the impact of the N-linked glycan on the protein stability of ABCG2.
19909340	1	4	theme	disulfide	289:297	arg1	bonds					299:303	intramolecular and intermolecular disulfide bonds	255:303	intramolecular and intermolecular disulfide bonds	255:303	The human ATP-binding cassette (ABC) transporter, ABCG2 (BCRP/MXR/ABCP), is a plasma membrane protein containing intramolecular and intermolecular disulfide bonds and an N-linked glycan at Asn596.
19909340	10	5	theme	de	1774:1775	arg1	ABCG2					1794:1798	de novo-synthesized ABCG2	1774:1798	de novo-synthesized ABCG2	1774:1798	In conclusion, we propose that the N-linked glycan at Asn596 is important for stabilizing de novo-synthesized ABCG2 and that disruption of this linkage results in protein destabilization and enhanced ubiquitin-mediated proteasomal degradation.
19909340	5	6	theme	glycosylation	849:861	arg1	inhibitors					863:872	various N-linked glycosylation inhibitors	832:872	various N-linked glycosylation inhibitors	832:872	When ABCG2 wild type-expressing cells were incubated with various N-linked glycosylation inhibitors, tunicamycin profoundly suppressed the protein expression level of ABCG2 and, accordingly, reduced the ABCG2-mediated cellular resistance to the cancer chemotherapeutic SN-38.
19909340	4	7	theme	cDNA	662:665	arg1	copy					648:651	one single copy	637:651	one single copy of ABCG2 cDNA	637:665	For this purpose, we incorporated one single copy of ABCG2 cDNA into a designated site of genomic DNA in Flp-In-293 cells to stably express ABCG2 or its variant proteins.
19909340	3	8	theme	protein	575:581	arg1	stability					583:591	the protein stability	571:591	the protein stability of ABCG2	571:600	In the present study, we aimed to analyze quantitatively the impact of the N-linked glycan on the protein stability of ABCG2.
19909340	6	9	theme	protein	1147:1153	arg1	level					1155:1159	its protein level	1143:1159	its protein level	1143:1159	When Asn596 was converted to Gln596, the resulting variant protein was not glycosylated, and its protein level was about one-third of the wild type level in Flp-In-293 cells.
19909340	5	10	theme	expression	921:930	arg1	level					932:936	the protein expression level	909:936	the protein expression level of ABCG2	909:945	When ABCG2 wild type-expressing cells were incubated with various N-linked glycosylation inhibitors, tunicamycin profoundly suppressed the protein expression level of ABCG2 and, accordingly, reduced the ABCG2-mediated cellular resistance to the cancer chemotherapeutic SN-38.
19909340	4	11	theme	single	641:646	arg1	copy					648:651	one single copy	637:651	one single copy of ABCG2 cDNA	637:665	For this purpose, we incorporated one single copy of ABCG2 cDNA into a designated site of genomic DNA in Flp-In-293 cells to stably express ABCG2 or its variant proteins.
19909340	5	12	theme	type-expressing	790:804	arg1	cells					806:810	ABCG2 wild type-expressing cells	779:810	ABCG2 wild type-expressing cells	779:810	When ABCG2 wild type-expressing cells were incubated with various N-linked glycosylation inhibitors, tunicamycin profoundly suppressed the protein expression level of ABCG2 and, accordingly, reduced the ABCG2-mediated cellular resistance to the cancer chemotherapeutic SN-38.
19909340	5	13	theme	various	832:838	arg1	inhibitors					863:872	various N-linked glycosylation inhibitors	832:872	various N-linked glycosylation inhibitors	832:872	When ABCG2 wild type-expressing cells were incubated with various N-linked glycosylation inhibitors, tunicamycin profoundly suppressed the protein expression level of ABCG2 and, accordingly, reduced the ABCG2-mediated cellular resistance to the cancer chemotherapeutic SN-38.
19909340	4	14	theme	genomic	693:699	arg1	DNA					701:703	genomic DNA	693:703	genomic DNA	693:703	For this purpose, we incorporated one single copy of ABCG2 cDNA into a designated site of genomic DNA in Flp-In-293 cells to stably express ABCG2 or its variant proteins.
19909340	10	15	theme	linkage	1828:1834	arg1	disruption					1809:1818	disruption	1809:1818	disruption of this linkage	1809:1834	In conclusion, we propose that the N-linked glycan at Asn596 is important for stabilizing de novo-synthesized ABCG2 and that disruption of this linkage results in protein destabilization and enhanced ubiquitin-mediated proteasomal degradation.
19909340	9	16	theme	Immunofluorescence	1509:1526	arg1	microscopy					1528:1537	Immunofluorescence microscopy	1509:1537	Immunofluorescence microscopy	1509:1537	Immunofluorescence microscopy demonstrated that treatment with MG132 increased the level of ABCG2 N596Q protein both in intracellular compartments and in the plasma membrane.
19909340	10	17	theme	enhanced	1875:1882	arg1	degradation					1915:1925	enhanced ubiquitin-mediated proteasomal degradation	1875:1925	enhanced ubiquitin-mediated proteasomal degradation	1875:1925	In conclusion, we propose that the N-linked glycan at Asn596 is important for stabilizing de novo-synthesized ABCG2 and that disruption of this linkage results in protein destabilization and enhanced ubiquitin-mediated proteasomal degradation.
19909340	1	18	theme	cassette	164:171	arg1	protein					236:242	a plasma membrane protein	218:242	a plasma membrane protein containing intramolecular and intermolecular disulfide bonds and an N-linked glycan at Asn596	218:336	The human ATP-binding cassette (ABC) transporter, ABCG2 (BCRP/MXR/ABCP), is a plasma membrane protein containing intramolecular and intermolecular disulfide bonds and an N-linked glycan at Asn596.
19909340	1	18	theme	cassette	164:171	arg1	ABCG2					192:196	ABCG2	192:196	ABCG2 (BCRP/MXR/ABCP)	192:212	The human ATP-binding cassette (ABC) transporter, ABCG2 (BCRP/MXR/ABCP), is a plasma membrane protein containing intramolecular and intermolecular disulfide bonds and an N-linked glycan at Asn596.
19909340	1	18	theme	cassette	164:171	arg1	transporter					179:189	The human ATP-binding cassette (ABC) transporter	142:189	The human ATP-binding cassette (ABC) transporter	142:189	The human ATP-binding cassette (ABC) transporter, ABCG2 (BCRP/MXR/ABCP), is a plasma membrane protein containing intramolecular and intermolecular disulfide bonds and an N-linked glycan at Asn596.
19909340	6	19	theme	type	1193:1196	arg1	level					1198:1202	the wild type level	1184:1202	the wild type level in Flp-In-293 cells	1184:1222	When Asn596 was converted to Gln596, the resulting variant protein was not glycosylated, and its protein level was about one-third of the wild type level in Flp-In-293 cells.
19909340	1	20	theme	ABC	174:176	arg1	protein					236:242	a plasma membrane protein	218:242	a plasma membrane protein containing intramolecular and intermolecular disulfide bonds and an N-linked glycan at Asn596	218:336	The human ATP-binding cassette (ABC) transporter, ABCG2 (BCRP/MXR/ABCP), is a plasma membrane protein containing intramolecular and intermolecular disulfide bonds and an N-linked glycan at Asn596.
19909340	1	20	theme	ABC	174:176	arg1	ABCG2					192:196	ABCG2	192:196	ABCG2 (BCRP/MXR/ABCP)	192:212	The human ATP-binding cassette (ABC) transporter, ABCG2 (BCRP/MXR/ABCP), is a plasma membrane protein containing intramolecular and intermolecular disulfide bonds and an N-linked glycan at Asn596.
19909340	1	20	theme	ABC	174:176	arg1	transporter					179:189	The human ATP-binding cassette (ABC) transporter	142:189	The human ATP-binding cassette (ABC) transporter	142:189	The human ATP-binding cassette (ABC) transporter, ABCG2 (BCRP/MXR/ABCP), is a plasma membrane protein containing intramolecular and intermolecular disulfide bonds and an N-linked glycan at Asn596.
19909340	0	21	theme	human	96:100	arg1	ABCG2					135:139	the human ATP-binding cassette transporter ABCG2	92:139	the human ATP-binding cassette transporter ABCG2	92:139	Disruption of N-linked glycosylation enhances ubiquitin-mediated proteasomal degradation of the human ATP-binding cassette transporter ABCG2.
19909340	8	22	theme	anti-ubiquitin	1335:1348	arg1	IgG1k					1350:1354	anti-ubiquitin IgG1k	1335:1354	anti-ubiquitin IgG1k after immunoprecipitation of ABCG2	1335:1389	Immunoblotting with anti-ubiquitin IgG1k after immunoprecipitation of ABCG2 revealed that the N596Q protein was ubiquitinated at levels that were significantly enhanced by treatment with MG132.
19909340	6	23	from	level	1198:1202	arg1	cells					1218:1222	Flp-In-293 cells	1207:1222	Flp-In-293 cells	1207:1222	When Asn596 was converted to Gln596, the resulting variant protein was not glycosylated, and its protein level was about one-third of the wild type level in Flp-In-293 cells.
19909340	0	24	theme	cassette	114:121	arg1	ABCG2					135:139	the human ATP-binding cassette transporter ABCG2	92:139	the human ATP-binding cassette transporter ABCG2	92:139	Disruption of N-linked glycosylation enhances ubiquitin-mediated proteasomal degradation of the human ATP-binding cassette transporter ABCG2.
19909340	2	25	theme	critical	409:416	arg1	bond					399:402	the intramolecular disulfide bond	370:402	the intramolecular disulfide bond	370:402	We have recently reported that the intramolecular disulfide bond is a critical checkpoint for determining the degradation fates of ABCG2.
19909340	2	25	theme	critical	409:416	arg1	checkpoint					418:427	a critical checkpoint	407:427	a critical checkpoint for determining the degradation fates of ABCG2	407:474	We have recently reported that the intramolecular disulfide bond is a critical checkpoint for determining the degradation fates of ABCG2.
19909340	0	26	theme	ABCG2	135:139	arg1	degradation					77:87	ubiquitin-mediated proteasomal degradation	46:87	ubiquitin-mediated proteasomal degradation of the human ATP-binding cassette transporter ABCG2	46:139	Disruption of N-linked glycosylation enhances ubiquitin-mediated proteasomal degradation of the human ATP-binding cassette transporter ABCG2.
19909340	5	27	theme	ABCG2-mediated	977:990	arg1	resistance					1001:1010	the ABCG2-mediated cellular resistance	973:1010	the ABCG2-mediated cellular resistance to the cancer chemotherapeutic SN-38	973:1047	When ABCG2 wild type-expressing cells were incubated with various N-linked glycosylation inhibitors, tunicamycin profoundly suppressed the protein expression level of ABCG2 and, accordingly, reduced the ABCG2-mediated cellular resistance to the cancer chemotherapeutic SN-38.
19909340	2	28	theme	ABCG2	470:474	arg1	fates					461:465	the degradation fates	445:465	the degradation fates of ABCG2	445:474	We have recently reported that the intramolecular disulfide bond is a critical checkpoint for determining the degradation fates of ABCG2.
19909340	5	29	dep	suppressed	898:907	arg1	reduced					965:971	reduced	965:971	reduced the ABCG2-mediated cellular resistance to the cancer chemotherapeutic SN-38	965:1047	When ABCG2 wild type-expressing cells were incubated with various N-linked glycosylation inhibitors, tunicamycin profoundly suppressed the protein expression level of ABCG2 and, accordingly, reduced the ABCG2-mediated cellular resistance to the cancer chemotherapeutic SN-38.
19909340	5	30	theme	wild	785:788	arg1	cells					806:810	ABCG2 wild type-expressing cells	779:810	ABCG2 wild type-expressing cells	779:810	When ABCG2 wild type-expressing cells were incubated with various N-linked glycosylation inhibitors, tunicamycin profoundly suppressed the protein expression level of ABCG2 and, accordingly, reduced the ABCG2-mediated cellular resistance to the cancer chemotherapeutic SN-38.
19909340	9	31	theme	N596Q	1607:1611	arg1	protein					1613:1619	ABCG2 N596Q protein	1601:1619	ABCG2 N596Q protein	1601:1619	Immunofluorescence microscopy demonstrated that treatment with MG132 increased the level of ABCG2 N596Q protein both in intracellular compartments and in the plasma membrane.
19909340	7	32	theme	protein	1306:1312	arg1	level					1285:1289	the level	1281:1289	the level of the variant protein	1281:1312	Treatment with MG132, a proteasome inhibitor, increased the level of the variant protein.
19909340	0	33	theme	N-linked	14:21	arg1	glycosylation					23:35	N-linked glycosylation	14:35	N-linked glycosylation	14:35	Disruption of N-linked glycosylation enhances ubiquitin-mediated proteasomal degradation of the human ATP-binding cassette transporter ABCG2.
19909340	9	34	theme	intracellular	1629:1641	arg1	compartments					1643:1654	intracellular compartments	1629:1654	intracellular compartments	1629:1654	Immunofluorescence microscopy demonstrated that treatment with MG132 increased the level of ABCG2 N596Q protein both in intracellular compartments and in the plasma membrane.
19909340	10	35	theme	proteasomal	1903:1913	arg1	degradation					1915:1925	enhanced ubiquitin-mediated proteasomal degradation	1875:1925	enhanced ubiquitin-mediated proteasomal degradation	1875:1925	In conclusion, we propose that the N-linked glycan at Asn596 is important for stabilizing de novo-synthesized ABCG2 and that disruption of this linkage results in protein destabilization and enhanced ubiquitin-mediated proteasomal degradation.
19909340	0	36	theme	proteasomal	65:75	arg1	degradation					77:87	ubiquitin-mediated proteasomal degradation	46:87	ubiquitin-mediated proteasomal degradation of the human ATP-binding cassette transporter ABCG2	46:139	Disruption of N-linked glycosylation enhances ubiquitin-mediated proteasomal degradation of the human ATP-binding cassette transporter ABCG2.
19909340	6	37	theme	wild	1188:1191	arg1	level					1198:1202	the wild type level	1184:1202	the wild type level in Flp-In-293 cells	1184:1222	When Asn596 was converted to Gln596, the resulting variant protein was not glycosylated, and its protein level was about one-third of the wild type level in Flp-In-293 cells.
19909340	5	38	theme	chemotherapeutic	1026:1041	arg1	SN-38					1043:1047	the cancer chemotherapeutic SN-38	1015:1047	the cancer chemotherapeutic SN-38	1015:1047	When ABCG2 wild type-expressing cells were incubated with various N-linked glycosylation inhibitors, tunicamycin profoundly suppressed the protein expression level of ABCG2 and, accordingly, reduced the ABCG2-mediated cellular resistance to the cancer chemotherapeutic SN-38.
19909340	1	39	theme	plasma	220:225	arg1	protein					236:242	a plasma membrane protein	218:242	a plasma membrane protein containing intramolecular and intermolecular disulfide bonds and an N-linked glycan at Asn596	218:336	The human ATP-binding cassette (ABC) transporter, ABCG2 (BCRP/MXR/ABCP), is a plasma membrane protein containing intramolecular and intermolecular disulfide bonds and an N-linked glycan at Asn596.
19909340	1	39	theme	plasma	220:225	arg1	transporter					179:189	The human ATP-binding cassette (ABC) transporter	142:189	The human ATP-binding cassette (ABC) transporter	142:189	The human ATP-binding cassette (ABC) transporter, ABCG2 (BCRP/MXR/ABCP), is a plasma membrane protein containing intramolecular and intermolecular disulfide bonds and an N-linked glycan at Asn596.
19909340	1	40	link	N-linked	312:319	arg1	glycan					321:326	an N-linked glycan	309:326	an N-linked glycan at Asn596	309:336	The human ATP-binding cassette (ABC) transporter, ABCG2 (BCRP/MXR/ABCP), is a plasma membrane protein containing intramolecular and intermolecular disulfide bonds and an N-linked glycan at Asn596.
19909340	2	41	theme	disulfide	389:397	arg1	bond					399:402	the intramolecular disulfide bond	370:402	the intramolecular disulfide bond	370:402	We have recently reported that the intramolecular disulfide bond is a critical checkpoint for determining the degradation fates of ABCG2.
19909340	2	41	theme	disulfide	389:397	arg1	checkpoint					418:427	a critical checkpoint	407:427	a critical checkpoint for determining the degradation fates of ABCG2	407:474	We have recently reported that the intramolecular disulfide bond is a critical checkpoint for determining the degradation fates of ABCG2.
19909340	10	42	link	N-linked	1719:1726	arg1	important					1748:1756	important	1748:1756	important	1748:1756	In conclusion, we propose that the N-linked glycan at Asn596 is important for stabilizing de novo-synthesized ABCG2 and that disruption of this linkage results in protein destabilization and enhanced ubiquitin-mediated proteasomal degradation.
19909340	10	42	link	N-linked	1719:1726	arg1	glycan					1728:1733	the N-linked glycan	1715:1733	the N-linked glycan at Asn596	1715:1743	In conclusion, we propose that the N-linked glycan at Asn596 is important for stabilizing de novo-synthesized ABCG2 and that disruption of this linkage results in protein destabilization and enhanced ubiquitin-mediated proteasomal degradation.
19909340	1	43	from	Asn596	331:336	arg1	bonds					299:303	intramolecular and intermolecular disulfide bonds	255:303	intramolecular and intermolecular disulfide bonds	255:303	The human ATP-binding cassette (ABC) transporter, ABCG2 (BCRP/MXR/ABCP), is a plasma membrane protein containing intramolecular and intermolecular disulfide bonds and an N-linked glycan at Asn596.
19909340	1	43	from	Asn596	331:336	arg1	glycan					321:326	an N-linked glycan	309:326	an N-linked glycan at Asn596	309:336	The human ATP-binding cassette (ABC) transporter, ABCG2 (BCRP/MXR/ABCP), is a plasma membrane protein containing intramolecular and intermolecular disulfide bonds and an N-linked glycan at Asn596.
19909340	8	44	with	treatment	1487:1495	arg1	MG132					1502:1506	MG132	1502:1506	MG132	1502:1506	Immunoblotting with anti-ubiquitin IgG1k after immunoprecipitation of ABCG2 revealed that the N596Q protein was ubiquitinated at levels that were significantly enhanced by treatment with MG132.
19909340	1	45	theme	intramolecular	255:268	arg1	bonds					299:303	intramolecular and intermolecular disulfide bonds	255:303	intramolecular and intermolecular disulfide bonds	255:303	The human ATP-binding cassette (ABC) transporter, ABCG2 (BCRP/MXR/ABCP), is a plasma membrane protein containing intramolecular and intermolecular disulfide bonds and an N-linked glycan at Asn596.
19909340	6	46	theme	resulting	1091:1099	arg1	protein					1109:1115	the resulting variant protein	1087:1115	the resulting variant protein	1087:1115	When Asn596 was converted to Gln596, the resulting variant protein was not glycosylated, and its protein level was about one-third of the wild type level in Flp-In-293 cells.
19909340	1	47	theme	intermolecular	274:287	arg1	bonds					299:303	intramolecular and intermolecular disulfide bonds	255:303	intramolecular and intermolecular disulfide bonds	255:303	The human ATP-binding cassette (ABC) transporter, ABCG2 (BCRP/MXR/ABCP), is a plasma membrane protein containing intramolecular and intermolecular disulfide bonds and an N-linked glycan at Asn596.
19909340	10	48	from	Asn596	1738:1743	arg1	important					1748:1756	important	1748:1756	important	1748:1756	In conclusion, we propose that the N-linked glycan at Asn596 is important for stabilizing de novo-synthesized ABCG2 and that disruption of this linkage results in protein destabilization and enhanced ubiquitin-mediated proteasomal degradation.
19909340	10	48	from	Asn596	1738:1743	arg1	glycan					1728:1733	the N-linked glycan	1715:1733	the N-linked glycan at Asn596	1715:1743	In conclusion, we propose that the N-linked glycan at Asn596 is important for stabilizing de novo-synthesized ABCG2 and that disruption of this linkage results in protein destabilization and enhanced ubiquitin-mediated proteasomal degradation.
19909340	10	49	theme	novo-synthesized	1777:1792	arg1	ABCG2					1794:1798	de novo-synthesized ABCG2	1774:1798	de novo-synthesized ABCG2	1774:1798	In conclusion, we propose that the N-linked glycan at Asn596 is important for stabilizing de novo-synthesized ABCG2 and that disruption of this linkage results in protein destabilization and enhanced ubiquitin-mediated proteasomal degradation.
19909340	5	50	theme	N-linked	840:847	arg1	inhibitors					863:872	various N-linked glycosylation inhibitors	832:872	various N-linked glycosylation inhibitors	832:872	When ABCG2 wild type-expressing cells were incubated with various N-linked glycosylation inhibitors, tunicamycin profoundly suppressed the protein expression level of ABCG2 and, accordingly, reduced the ABCG2-mediated cellular resistance to the cancer chemotherapeutic SN-38.
19909340	4	51	theme	ABCG2	656:660	arg1	cDNA					662:665	ABCG2 cDNA	656:665	ABCG2 cDNA	656:665	For this purpose, we incorporated one single copy of ABCG2 cDNA into a designated site of genomic DNA in Flp-In-293 cells to stably express ABCG2 or its variant proteins.
19909340	3	52	theme	glycan	561:566	arg1	impact					538:543	the impact	534:543	the impact of the N-linked glycan on the protein stability of ABCG2	534:600	In the present study, we aimed to analyze quantitatively the impact of the N-linked glycan on the protein stability of ABCG2.
19909340	3	53	theme	ABCG2	596:600	arg1	stability					583:591	the protein stability	571:591	the protein stability of ABCG2	571:600	In the present study, we aimed to analyze quantitatively the impact of the N-linked glycan on the protein stability of ABCG2.
19909340	5	54	theme	protein	913:919	arg1	level					932:936	the protein expression level	909:936	the protein expression level of ABCG2	909:945	When ABCG2 wild type-expressing cells were incubated with various N-linked glycosylation inhibitors, tunicamycin profoundly suppressed the protein expression level of ABCG2 and, accordingly, reduced the ABCG2-mediated cellular resistance to the cancer chemotherapeutic SN-38.
19909340	6	55	theme	Flp-In-293	1207:1216	arg1	cells					1218:1222	Flp-In-293 cells	1207:1222	Flp-In-293 cells	1207:1222	When Asn596 was converted to Gln596, the resulting variant protein was not glycosylated, and its protein level was about one-third of the wild type level in Flp-In-293 cells.
19909340	10	56	theme	ubiquitin-mediated	1884:1901	arg1	degradation					1915:1925	enhanced ubiquitin-mediated proteasomal degradation	1875:1925	enhanced ubiquitin-mediated proteasomal degradation	1875:1925	In conclusion, we propose that the N-linked glycan at Asn596 is important for stabilizing de novo-synthesized ABCG2 and that disruption of this linkage results in protein destabilization and enhanced ubiquitin-mediated proteasomal degradation.
19909340	1	57	theme	ATP-binding	152:162	arg1	protein					236:242	a plasma membrane protein	218:242	a plasma membrane protein containing intramolecular and intermolecular disulfide bonds and an N-linked glycan at Asn596	218:336	The human ATP-binding cassette (ABC) transporter, ABCG2 (BCRP/MXR/ABCP), is a plasma membrane protein containing intramolecular and intermolecular disulfide bonds and an N-linked glycan at Asn596.
19909340	1	57	theme	ATP-binding	152:162	arg1	ABCG2					192:196	ABCG2	192:196	ABCG2 (BCRP/MXR/ABCP)	192:212	The human ATP-binding cassette (ABC) transporter, ABCG2 (BCRP/MXR/ABCP), is a plasma membrane protein containing intramolecular and intermolecular disulfide bonds and an N-linked glycan at Asn596.
19909340	1	57	theme	ATP-binding	152:162	arg1	transporter					179:189	The human ATP-binding cassette (ABC) transporter	142:189	The human ATP-binding cassette (ABC) transporter	142:189	The human ATP-binding cassette (ABC) transporter, ABCG2 (BCRP/MXR/ABCP), is a plasma membrane protein containing intramolecular and intermolecular disulfide bonds and an N-linked glycan at Asn596.
19909340	6	58	theme	level	1198:1202	arg1	level					1198:1202	the wild type level	1184:1202	the wild type level in Flp-In-293 cells	1184:1222	When Asn596 was converted to Gln596, the resulting variant protein was not glycosylated, and its protein level was about one-third of the wild type level in Flp-In-293 cells.
19909340	6	58	theme	level	1198:1202	arg1	one-third					1171:1179	one-third	1171:1179	one-third	1171:1179	When Asn596 was converted to Gln596, the resulting variant protein was not glycosylated, and its protein level was about one-third of the wild type level in Flp-In-293 cells.
19909340	4	59	theme	DNA	701:703	arg1	site					685:688	a designated site	672:688	a designated site of genomic DNA in Flp-In-293 cells	672:723	For this purpose, we incorporated one single copy of ABCG2 cDNA into a designated site of genomic DNA in Flp-In-293 cells to stably express ABCG2 or its variant proteins.
19909340	4	59	theme	DNA	701:703	arg1	DNA					701:703	genomic DNA	693:703	genomic DNA	693:703	For this purpose, we incorporated one single copy of ABCG2 cDNA into a designated site of genomic DNA in Flp-In-293 cells to stably express ABCG2 or its variant proteins.
19909340	1	60	theme	human	146:150	arg1	protein					236:242	a plasma membrane protein	218:242	a plasma membrane protein containing intramolecular and intermolecular disulfide bonds and an N-linked glycan at Asn596	218:336	The human ATP-binding cassette (ABC) transporter, ABCG2 (BCRP/MXR/ABCP), is a plasma membrane protein containing intramolecular and intermolecular disulfide bonds and an N-linked glycan at Asn596.
19909340	1	60	theme	human	146:150	arg1	ABCG2					192:196	ABCG2	192:196	ABCG2 (BCRP/MXR/ABCP)	192:212	The human ATP-binding cassette (ABC) transporter, ABCG2 (BCRP/MXR/ABCP), is a plasma membrane protein containing intramolecular and intermolecular disulfide bonds and an N-linked glycan at Asn596.
19909340	1	60	theme	human	146:150	arg1	transporter					179:189	The human ATP-binding cassette (ABC) transporter	142:189	The human ATP-binding cassette (ABC) transporter	142:189	The human ATP-binding cassette (ABC) transporter, ABCG2 (BCRP/MXR/ABCP), is a plasma membrane protein containing intramolecular and intermolecular disulfide bonds and an N-linked glycan at Asn596.
19909340	7	61	with	Treatment	1225:1233	arg1	inhibitor					1260:1268	a proteasome inhibitor	1247:1268	a proteasome inhibitor	1247:1268	Treatment with MG132, a proteasome inhibitor, increased the level of the variant protein.
19909340	7	61	with	Treatment	1225:1233	arg1	MG132					1240:1244	MG132	1240:1244	MG132	1240:1244	Treatment with MG132, a proteasome inhibitor, increased the level of the variant protein.
19909340	3	62	from	impact	538:543	arg1	stability					583:591	the protein stability	571:591	the protein stability of ABCG2	571:600	In the present study, we aimed to analyze quantitatively the impact of the N-linked glycan on the protein stability of ABCG2.
19909340	0	63	theme	ATP-binding	102:112	arg1	ABCG2					135:139	the human ATP-binding cassette transporter ABCG2	92:139	the human ATP-binding cassette transporter ABCG2	92:139	Disruption of N-linked glycosylation enhances ubiquitin-mediated proteasomal degradation of the human ATP-binding cassette transporter ABCG2.
19909340	4	64	theme	designated	674:683	arg1	site					685:688	a designated site	672:688	a designated site of genomic DNA in Flp-In-293 cells	672:723	For this purpose, we incorporated one single copy of ABCG2 cDNA into a designated site of genomic DNA in Flp-In-293 cells to stably express ABCG2 or its variant proteins.
19909340	4	64	theme	designated	674:683	arg1	DNA					701:703	genomic DNA	693:703	genomic DNA	693:703	For this purpose, we incorporated one single copy of ABCG2 cDNA into a designated site of genomic DNA in Flp-In-293 cells to stably express ABCG2 or its variant proteins.
19909340	0	65	theme	transporter	123:133	arg1	ABCG2					135:139	the human ATP-binding cassette transporter ABCG2	92:139	the human ATP-binding cassette transporter ABCG2	92:139	Disruption of N-linked glycosylation enhances ubiquitin-mediated proteasomal degradation of the human ATP-binding cassette transporter ABCG2.
19909340	9	66	with	treatment	1557:1565	arg1	MG132					1572:1576	MG132	1572:1576	MG132	1572:1576	Immunofluorescence microscopy demonstrated that treatment with MG132 increased the level of ABCG2 N596Q protein both in intracellular compartments and in the plasma membrane.
19909340	3	67	link	N-linked	552:559	arg1	glycan					561:566	the N-linked glycan	548:566	the N-linked glycan	548:566	In the present study, we aimed to analyze quantitatively the impact of the N-linked glycan on the protein stability of ABCG2.
19909340	5	68	theme	ABCG2	779:783	arg1	cells					806:810	ABCG2 wild type-expressing cells	779:810	ABCG2 wild type-expressing cells	779:810	When ABCG2 wild type-expressing cells were incubated with various N-linked glycosylation inhibitors, tunicamycin profoundly suppressed the protein expression level of ABCG2 and, accordingly, reduced the ABCG2-mediated cellular resistance to the cancer chemotherapeutic SN-38.
19909340	5	69	link	N-linked	840:847	arg1	inhibitors					863:872	various N-linked glycosylation inhibitors	832:872	various N-linked glycosylation inhibitors	832:872	When ABCG2 wild type-expressing cells were incubated with various N-linked glycosylation inhibitors, tunicamycin profoundly suppressed the protein expression level of ABCG2 and, accordingly, reduced the ABCG2-mediated cellular resistance to the cancer chemotherapeutic SN-38.
19909340	5	70	theme	ABCG2	941:945	arg1	level					932:936	the protein expression level	909:936	the protein expression level of ABCG2	909:945	When ABCG2 wild type-expressing cells were incubated with various N-linked glycosylation inhibitors, tunicamycin profoundly suppressed the protein expression level of ABCG2 and, accordingly, reduced the ABCG2-mediated cellular resistance to the cancer chemotherapeutic SN-38.
19909340	7	71	theme	variant	1298:1304	arg1	protein					1306:1312	the variant protein	1294:1312	the variant protein	1294:1312	Treatment with MG132, a proteasome inhibitor, increased the level of the variant protein.
19909340	6	72	gly	glycosylated	1125:1136	arg1	protein					1109:1115	the resulting variant protein	1087:1115	the resulting variant protein	1087:1115	When Asn596 was converted to Gln596, the resulting variant protein was not glycosylated, and its protein level was about one-third of the wild type level in Flp-In-293 cells.
19909340	4	73	theme	Flp-In-293	708:717	arg1	cells					719:723	Flp-In-293 cells	708:723	Flp-In-293 cells	708:723	For this purpose, we incorporated one single copy of ABCG2 cDNA into a designated site of genomic DNA in Flp-In-293 cells to stably express ABCG2 or its variant proteins.
19909340	0	74	theme	glycosylation	23:35	arg1	Disruption					0:9	Disruption	0:9	Disruption of N-linked glycosylation	0:35	Disruption of N-linked glycosylation enhances ubiquitin-mediated proteasomal degradation of the human ATP-binding cassette transporter ABCG2.
19909340	9	75	theme	protein	1613:1619	arg1	level					1592:1596	the level	1588:1596	the level of ABCG2 N596Q protein	1588:1619	Immunofluorescence microscopy demonstrated that treatment with MG132 increased the level of ABCG2 N596Q protein both in intracellular compartments and in the plasma membrane.
19909340	1	76	contain	containing	244:253	arg1	protein					236:242	a plasma membrane protein	218:242	a plasma membrane protein containing intramolecular and intermolecular disulfide bonds and an N-linked glycan at Asn596	218:336	The human ATP-binding cassette (ABC) transporter, ABCG2 (BCRP/MXR/ABCP), is a plasma membrane protein containing intramolecular and intermolecular disulfide bonds and an N-linked glycan at Asn596.
19909340	1	76	contain	containing	244:253	arg2	bonds					299:303	intramolecular and intermolecular disulfide bonds	255:303	intramolecular and intermolecular disulfide bonds	255:303	The human ATP-binding cassette (ABC) transporter, ABCG2 (BCRP/MXR/ABCP), is a plasma membrane protein containing intramolecular and intermolecular disulfide bonds and an N-linked glycan at Asn596.
19909340	1	76	contain	containing	244:253	arg2	glycan					321:326	an N-linked glycan	309:326	an N-linked glycan at Asn596	309:336	The human ATP-binding cassette (ABC) transporter, ABCG2 (BCRP/MXR/ABCP), is a plasma membrane protein containing intramolecular and intermolecular disulfide bonds and an N-linked glycan at Asn596.
19909340	1	76	contain	containing	244:253	arg1	transporter					179:189	The human ATP-binding cassette (ABC) transporter	142:189	The human ATP-binding cassette (ABC) transporter	142:189	The human ATP-binding cassette (ABC) transporter, ABCG2 (BCRP/MXR/ABCP), is a plasma membrane protein containing intramolecular and intermolecular disulfide bonds and an N-linked glycan at Asn596.
19909340	2	77	theme	degradation	449:459	arg1	fates					461:465	the degradation fates	445:465	the degradation fates of ABCG2	445:474	We have recently reported that the intramolecular disulfide bond is a critical checkpoint for determining the degradation fates of ABCG2.
19909340	8	78	theme	ABCG2	1385:1389	arg1	immunoprecipitation					1362:1380	immunoprecipitation	1362:1380	immunoprecipitation of ABCG2	1362:1389	Immunoblotting with anti-ubiquitin IgG1k after immunoprecipitation of ABCG2 revealed that the N596Q protein was ubiquitinated at levels that were significantly enhanced by treatment with MG132.
19909340	3	79	theme	present	484:490	arg1	study					492:496	the present study	480:496	the present study	480:496	In the present study, we aimed to analyze quantitatively the impact of the N-linked glycan on the protein stability of ABCG2.
19909340	0	80	theme	ubiquitin-mediated	46:63	arg1	degradation					77:87	ubiquitin-mediated proteasomal degradation	46:87	ubiquitin-mediated proteasomal degradation of the human ATP-binding cassette transporter ABCG2	46:139	Disruption of N-linked glycosylation enhances ubiquitin-mediated proteasomal degradation of the human ATP-binding cassette transporter ABCG2.
19909340	1	81	theme	N-linked	312:319	arg1	glycan					321:326	an N-linked glycan	309:326	an N-linked glycan at Asn596	309:336	The human ATP-binding cassette (ABC) transporter, ABCG2 (BCRP/MXR/ABCP), is a plasma membrane protein containing intramolecular and intermolecular disulfide bonds and an N-linked glycan at Asn596.
19909340	5	82	theme	cancer	1019:1024	arg1	SN-38					1043:1047	the cancer chemotherapeutic SN-38	1015:1047	the cancer chemotherapeutic SN-38	1015:1047	When ABCG2 wild type-expressing cells were incubated with various N-linked glycosylation inhibitors, tunicamycin profoundly suppressed the protein expression level of ABCG2 and, accordingly, reduced the ABCG2-mediated cellular resistance to the cancer chemotherapeutic SN-38.
19909340	8	83	with	Immunoblotting	1315:1328	arg1	IgG1k					1350:1354	anti-ubiquitin IgG1k	1335:1354	anti-ubiquitin IgG1k after immunoprecipitation of ABCG2	1335:1389	Immunoblotting with anti-ubiquitin IgG1k after immunoprecipitation of ABCG2 revealed that the N596Q protein was ubiquitinated at levels that were significantly enhanced by treatment with MG132.
19909340	8	84	theme	N596Q	1409:1413	arg1	protein					1415:1421	the N596Q protein	1405:1421	the N596Q protein	1405:1421	Immunoblotting with anti-ubiquitin IgG1k after immunoprecipitation of ABCG2 revealed that the N596Q protein was ubiquitinated at levels that were significantly enhanced by treatment with MG132.
19909340	5	85	theme	cellular	992:999	arg1	resistance					1001:1010	the ABCG2-mediated cellular resistance	973:1010	the ABCG2-mediated cellular resistance to the cancer chemotherapeutic SN-38	973:1047	When ABCG2 wild type-expressing cells were incubated with various N-linked glycosylation inhibitors, tunicamycin profoundly suppressed the protein expression level of ABCG2 and, accordingly, reduced the ABCG2-mediated cellular resistance to the cancer chemotherapeutic SN-38.
19909340	7	86	theme	proteasome	1249:1258	arg1	inhibitor					1260:1268	a proteasome inhibitor	1247:1268	a proteasome inhibitor	1247:1268	Treatment with MG132, a proteasome inhibitor, increased the level of the variant protein.
19909340	7	86	theme	proteasome	1249:1258	arg1	MG132					1240:1244	MG132	1240:1244	MG132	1240:1244	Treatment with MG132, a proteasome inhibitor, increased the level of the variant protein.
19909340	4	87	theme	variant	756:762	arg1	proteins					764:771	its variant proteins	752:771	its variant proteins	752:771	For this purpose, we incorporated one single copy of ABCG2 cDNA into a designated site of genomic DNA in Flp-In-293 cells to stably express ABCG2 or its variant proteins.
19909340	10	88	theme	N-linked	1719:1726	arg1	important					1748:1756	important	1748:1756	important	1748:1756	In conclusion, we propose that the N-linked glycan at Asn596 is important for stabilizing de novo-synthesized ABCG2 and that disruption of this linkage results in protein destabilization and enhanced ubiquitin-mediated proteasomal degradation.
19909340	10	88	theme	N-linked	1719:1726	arg1	glycan					1728:1733	the N-linked glycan	1715:1733	the N-linked glycan at Asn596	1715:1743	In conclusion, we propose that the N-linked glycan at Asn596 is important for stabilizing de novo-synthesized ABCG2 and that disruption of this linkage results in protein destabilization and enhanced ubiquitin-mediated proteasomal degradation.
19909340	1	89	theme	membrane	227:234	arg1	protein					236:242	a plasma membrane protein	218:242	a plasma membrane protein containing intramolecular and intermolecular disulfide bonds and an N-linked glycan at Asn596	218:336	The human ATP-binding cassette (ABC) transporter, ABCG2 (BCRP/MXR/ABCP), is a plasma membrane protein containing intramolecular and intermolecular disulfide bonds and an N-linked glycan at Asn596.
19909340	1	89	theme	membrane	227:234	arg1	transporter					179:189	The human ATP-binding cassette (ABC) transporter	142:189	The human ATP-binding cassette (ABC) transporter	142:189	The human ATP-binding cassette (ABC) transporter, ABCG2 (BCRP/MXR/ABCP), is a plasma membrane protein containing intramolecular and intermolecular disulfide bonds and an N-linked glycan at Asn596.
19909340	9	90	theme	plasma	1667:1672	arg1	membrane					1674:1681	the plasma membrane	1663:1681	the plasma membrane	1663:1681	Immunofluorescence microscopy demonstrated that treatment with MG132 increased the level of ABCG2 N596Q protein both in intracellular compartments and in the plasma membrane.
19909340	10	91	theme	protein	1847:1853	arg1	destabilization					1855:1869	protein destabilization	1847:1869	protein destabilization	1847:1869	In conclusion, we propose that the N-linked glycan at Asn596 is important for stabilizing de novo-synthesized ABCG2 and that disruption of this linkage results in protein destabilization and enhanced ubiquitin-mediated proteasomal degradation.
19909340	2	92	theme	intramolecular	374:387	arg1	bond					399:402	the intramolecular disulfide bond	370:402	the intramolecular disulfide bond	370:402	We have recently reported that the intramolecular disulfide bond is a critical checkpoint for determining the degradation fates of ABCG2.
19909340	2	92	theme	intramolecular	374:387	arg1	checkpoint					418:427	a critical checkpoint	407:427	a critical checkpoint for determining the degradation fates of ABCG2	407:474	We have recently reported that the intramolecular disulfide bond is a critical checkpoint for determining the degradation fates of ABCG2.
19909340	4	93	from	site	685:688	arg1	cells					719:723	Flp-In-293 cells	708:723	Flp-In-293 cells	708:723	For this purpose, we incorporated one single copy of ABCG2 cDNA into a designated site of genomic DNA in Flp-In-293 cells to stably express ABCG2 or its variant proteins.
17117926	4	0	dep	ability	515:521	arg1	stimulate					598:606	stimulate	598:606	to stimulate cell migration	595:621	The palmitoylation was not essential for the secretion of Wnt-5a, but was necessary for its ability to suppress Wnt-3a-dependent T-cell factor transcriptional activity and to stimulate cell migration.
17117926	4	0	dep	ability	515:521	arg1	suppress					526:533	suppress	526:533	to suppress Wnt-3a-dependent T-cell factor transcriptional activity	523:589	The palmitoylation was not essential for the secretion of Wnt-5a, but was necessary for its ability to suppress Wnt-3a-dependent T-cell factor transcriptional activity and to stimulate cell migration.
17117926	10	1	theme	Wnt-5a	1355:1360	arg1	glycosylation					1338:1350	glycosylation	1338:1350	glycosylation of Wnt-5a	1338:1360	Thus the post-translational palmitoylation and glycosylation of Wnt-5a are important for the actions and secretion of Wnt-5a.
17117926	10	1	theme	Wnt-5a	1355:1360	arg1	palmitoylation					1319:1332	the post-translational palmitoylation	1296:1332	the post-translational palmitoylation	1296:1332	Thus the post-translational palmitoylation and glycosylation of Wnt-5a are important for the actions and secretion of Wnt-5a.
17117926	10	1	theme	Wnt-5a	1355:1360	arg1	important					1366:1374	important	1366:1374	important	1366:1374	Thus the post-translational palmitoylation and glycosylation of Wnt-5a are important for the actions and secretion of Wnt-5a.
17117926	3	2	from	Asn311	404:409	arg1	glycans					377:383	glycans	377:383	glycans at Asn114, Asn120, Asn311 and Asn325	377:420	We found that Wnt-5a is modified with palmitate at Cys104 and glycans at Asn114, Asn120, Asn311 and Asn325.
17117926	3	2	from	Asn311	404:409	arg1	Cys104					366:371	Cys104	366:371	Cys104	366:371	We found that Wnt-5a is modified with palmitate at Cys104 and glycans at Asn114, Asn120, Asn311 and Asn325.
17117926	6	3	theme	palmitoylation	813:826	arg1	site					828:831	the palmitoylation site	809:831	the palmitoylation site	809:831	Wild-type Wnt-5a induced the internalization of Fz (Frizzled) 5, but a Wnt-5a mutant that lacks the palmitoylation site did not.
17117926	1	4	theme	Wnt	183:185	arg1	signalling					187:196	Wnt signalling	183:196	Wnt signalling	183:196	Wnt-5a is a representative ligand that activates a beta-catenin-independent pathway in Wnt signalling.
17117926	4	5	theme	transcriptional	566:580	arg1	activity					582:589	Wnt-3a-dependent T-cell factor transcriptional activity	535:589	Wnt-3a-dependent T-cell factor transcriptional activity	535:589	The palmitoylation was not essential for the secretion of Wnt-5a, but was necessary for its ability to suppress Wnt-3a-dependent T-cell factor transcriptional activity and to stimulate cell migration.
17117926	8	6	theme	signal	1159:1164	arg1	cascades					1166:1173	intracellular signal cascades	1145:1173	intracellular signal cascades	1145:1173	These results indicate that palmitoylation of Wnt-5a is important for the triggering of signalling at the cell surface level and, therefore, that the lipid-unmodified form of Wnt-5a cannot activate intracellular signal cascades.
17117926	7	7	theme	Wnt-5a	939:944	arg1	palmitoylation					921:934	palmitoylation	921:934	palmitoylation of Wnt-5a	921:944	Furthermore, the binding of Wnt-5a to the extracellular domain of Fz5 required palmitoylation of Wnt-5a.
17117926	7	8	theme	Wnt-5a	870:875	arg1	binding					859:865	the binding	855:865	the binding of Wnt-5a to the extracellular domain of Fz5	855:910	Furthermore, the binding of Wnt-5a to the extracellular domain of Fz5 required palmitoylation of Wnt-5a.
17117926	9	9	theme	Wnt-5a	1283:1288	arg1	actions					1272:1278	the actions	1268:1278	the actions of Wnt-5a	1268:1288	In contrast, glycosylation was necessary for the secretion of Wnt-5a, but not essential for the actions of Wnt-5a.
17117926	8	10	theme	surface	1058:1064	arg1	level					1066:1070	the cell surface level	1049:1070	the cell surface level	1049:1070	These results indicate that palmitoylation of Wnt-5a is important for the triggering of signalling at the cell surface level and, therefore, that the lipid-unmodified form of Wnt-5a cannot activate intracellular signal cascades.
17117926	8	11	theme	signalling	1035:1044	arg1	triggering					1021:1030	the triggering	1017:1030	the triggering of signalling at the cell surface level	1017:1070	These results indicate that palmitoylation of Wnt-5a is important for the triggering of signalling at the cell surface level and, therefore, that the lipid-unmodified form of Wnt-5a cannot activate intracellular signal cascades.
17117926	8	12	theme	Wnt-5a	993:998	arg1	palmitoylation					975:988	palmitoylation	975:988	palmitoylation of Wnt-5a	975:998	These results indicate that palmitoylation of Wnt-5a is important for the triggering of signalling at the cell surface level and, therefore, that the lipid-unmodified form of Wnt-5a cannot activate intracellular signal cascades.
17117926	9	13	from	contrast	1179:1186	arg1	necessary					1207:1215	necessary	1207:1215	necessary	1207:1215	In contrast, glycosylation was necessary for the secretion of Wnt-5a, but not essential for the actions of Wnt-5a.
17117926	8	14	theme	cell	1053:1056	arg1	level					1066:1070	the cell surface level	1049:1070	the cell surface level	1049:1070	These results indicate that palmitoylation of Wnt-5a is important for the triggering of signalling at the cell surface level and, therefore, that the lipid-unmodified form of Wnt-5a cannot activate intracellular signal cascades.
17117926	1	15	from	pathway	172:178	arg1	signalling					187:196	Wnt signalling	183:196	Wnt signalling	183:196	Wnt-5a is a representative ligand that activates a beta-catenin-independent pathway in Wnt signalling.
17117926	2	16	theme	Wnt-5a	289:294	arg1	actions					278:284	the actions	274:284	the actions of Wnt-5a	274:294	In the present paper, the roles of the post-translational modifications in the actions of Wnt-5a were investigated.
17117926	2	17	from	roles	225:229	arg1	actions					278:284	the actions	274:284	the actions of Wnt-5a	274:294	In the present paper, the roles of the post-translational modifications in the actions of Wnt-5a were investigated.
17117926	4	18	theme	Wnt-5a	481:486	arg1	secretion					468:476	the secretion	464:476	the secretion of Wnt-5a	464:486	The palmitoylation was not essential for the secretion of Wnt-5a, but was necessary for its ability to suppress Wnt-3a-dependent T-cell factor transcriptional activity and to stimulate cell migration.
17117926	8	19	dep	important	1003:1011	arg1	activate					1136:1143	activate	1136:1143	activate intracellular signal cascades	1136:1173	These results indicate that palmitoylation of Wnt-5a is important for the triggering of signalling at the cell surface level and, therefore, that the lipid-unmodified form of Wnt-5a cannot activate intracellular signal cascades.
17117926	8	19	dep	important	1003:1011	arg1	form					1114:1117	the lipid-unmodified form	1093:1117	the lipid-unmodified form of Wnt-5a	1093:1127	These results indicate that palmitoylation of Wnt-5a is important for the triggering of signalling at the cell surface level and, therefore, that the lipid-unmodified form of Wnt-5a cannot activate intracellular signal cascades.
17117926	8	20	from	triggering	1021:1030	arg1	level					1066:1070	the cell surface level	1049:1070	the cell surface level	1049:1070	These results indicate that palmitoylation of Wnt-5a is important for the triggering of signalling at the cell surface level and, therefore, that the lipid-unmodified form of Wnt-5a cannot activate intracellular signal cascades.
17117926	5	21	theme	focal	641:645	arg1	kinase					656:661	focal adhesion kinase	641:661	focal adhesion kinase	641:661	Wnt-5a activated focal adhesion kinase and this activation also required palmitoylation.
17117926	6	22	theme	Wnt-5a	784:789	arg1	mutant					791:796	a Wnt-5a mutant	782:796	a Wnt-5a mutant that lacks the palmitoylation site	782:831	Wild-type Wnt-5a induced the internalization of Fz (Frizzled) 5, but a Wnt-5a mutant that lacks the palmitoylation site did not.
17117926	6	23	theme	Wild-type	713:721	arg1	Wnt-5a					723:728	Wild-type Wnt-5a	713:728	Wild-type Wnt-5a	713:728	Wild-type Wnt-5a induced the internalization of Fz (Frizzled) 5, but a Wnt-5a mutant that lacks the palmitoylation site did not.
17117926	0	24	theme	Post-translational	0:17	arg1	palmitoylation					19:32	Post-translational palmitoylation	0:32	Post-translational palmitoylation	0:32	Post-translational palmitoylation and glycosylation of Wnt-5a are necessary for its signalling.
17117926	4	25	theme	Wnt-3a-dependent	535:550	arg1	activity					582:589	Wnt-3a-dependent T-cell factor transcriptional activity	535:589	Wnt-3a-dependent T-cell factor transcriptional activity	535:589	The palmitoylation was not essential for the secretion of Wnt-5a, but was necessary for its ability to suppress Wnt-3a-dependent T-cell factor transcriptional activity and to stimulate cell migration.
17117926	5	26	theme	adhesion	647:654	arg1	kinase					656:661	focal adhesion kinase	641:661	focal adhesion kinase	641:661	Wnt-5a activated focal adhesion kinase and this activation also required palmitoylation.
17117926	10	27	theme	Wnt-5a	1409:1414	arg1	secretion					1396:1404	secretion	1396:1404	secretion	1396:1404	Thus the post-translational palmitoylation and glycosylation of Wnt-5a are important for the actions and secretion of Wnt-5a.
17117926	10	27	theme	Wnt-5a	1409:1414	arg1	actions					1384:1390	actions	1384:1390	actions	1384:1390	Thus the post-translational palmitoylation and glycosylation of Wnt-5a are important for the actions and secretion of Wnt-5a.
17117926	10	28	theme	post-translational	1300:1317	arg1	palmitoylation					1319:1332	the post-translational palmitoylation	1296:1332	the post-translational palmitoylation	1296:1332	Thus the post-translational palmitoylation and glycosylation of Wnt-5a are important for the actions and secretion of Wnt-5a.
17117926	10	28	theme	post-translational	1300:1317	arg1	important					1366:1374	important	1366:1374	important	1366:1374	Thus the post-translational palmitoylation and glycosylation of Wnt-5a are important for the actions and secretion of Wnt-5a.
17117926	9	29	gly	glycosylation	1189:1201	arg1	Wnt-5a					1283:1288	Wnt-5a	1283:1288	Wnt-5a	1283:1288	In contrast, glycosylation was necessary for the secretion of Wnt-5a, but not essential for the actions of Wnt-5a.
17117926	4	30	theme	factor	559:564	arg1	activity					582:589	Wnt-3a-dependent T-cell factor transcriptional activity	535:589	Wnt-3a-dependent T-cell factor transcriptional activity	535:589	The palmitoylation was not essential for the secretion of Wnt-5a, but was necessary for its ability to suppress Wnt-3a-dependent T-cell factor transcriptional activity and to stimulate cell migration.
17117926	1	31	theme	representative	108:121	arg1	ligand					123:128	a representative ligand	106:128	a representative ligand that activates a beta-catenin-independent pathway in Wnt signalling	106:196	Wnt-5a is a representative ligand that activates a beta-catenin-independent pathway in Wnt signalling.
17117926	1	31	theme	representative	108:121	arg1	Wnt-5a					96:101	Wnt-5a	96:101	Wnt-5a	96:101	Wnt-5a is a representative ligand that activates a beta-catenin-independent pathway in Wnt signalling.
17117926	0	32	theme	Wnt-5a	55:60	arg1	glycosylation					38:50	glycosylation	38:50	glycosylation of Wnt-5a	38:60	Post-translational palmitoylation and glycosylation of Wnt-5a are necessary for its signalling.
17117926	0	32	theme	Wnt-5a	55:60	arg1	palmitoylation					19:32	Post-translational palmitoylation	0:32	Post-translational palmitoylation	0:32	Post-translational palmitoylation and glycosylation of Wnt-5a are necessary for its signalling.
17117926	4	33	theme	T-cell	552:557	arg1	activity					582:589	Wnt-3a-dependent T-cell factor transcriptional activity	535:589	Wnt-3a-dependent T-cell factor transcriptional activity	535:589	The palmitoylation was not essential for the secretion of Wnt-5a, but was necessary for its ability to suppress Wnt-3a-dependent T-cell factor transcriptional activity and to stimulate cell migration.
17117926	2	34	theme	post-translational	238:255	arg1	modifications					257:269	the post-translational modifications	234:269	the post-translational modifications	234:269	In the present paper, the roles of the post-translational modifications in the actions of Wnt-5a were investigated.
17117926	8	35	from	level	1066:1070	arg1	signalling					1035:1044	signalling	1035:1044	signalling at the cell surface level	1035:1070	These results indicate that palmitoylation of Wnt-5a is important for the triggering of signalling at the cell surface level and, therefore, that the lipid-unmodified form of Wnt-5a cannot activate intracellular signal cascades.
17117926	8	35	from	level	1066:1070	arg1	triggering					1021:1030	the triggering	1017:1030	the triggering of signalling at the cell surface level	1017:1070	These results indicate that palmitoylation of Wnt-5a is important for the triggering of signalling at the cell surface level and, therefore, that the lipid-unmodified form of Wnt-5a cannot activate intracellular signal cascades.
17117926	9	36	theme	Wnt-5a	1238:1243	arg1	secretion					1225:1233	the secretion	1221:1233	the secretion of Wnt-5a	1221:1243	In contrast, glycosylation was necessary for the secretion of Wnt-5a, but not essential for the actions of Wnt-5a.
17117926	10	37	gly	glycosylation	1338:1350	arg1	Wnt-5a					1409:1414	Wnt-5a	1409:1414	Wnt-5a	1409:1414	Thus the post-translational palmitoylation and glycosylation of Wnt-5a are important for the actions and secretion of Wnt-5a.
17117926	10	37	gly	glycosylation	1338:1350	arg1	Wnt-5a					1355:1360	Wnt-5a	1355:1360	Wnt-5a	1355:1360	Thus the post-translational palmitoylation and glycosylation of Wnt-5a are important for the actions and secretion of Wnt-5a.
17117926	3	38	mod	modified	339:346	arg1	Wnt-5a					329:334	Wnt-5a	329:334	Wnt-5a	329:334	We found that Wnt-5a is modified with palmitate at Cys104 and glycans at Asn114, Asn120, Asn311 and Asn325.
17117926	3	38	mod	modified	339:346	arg3	palmitate					353:361	palmitate	353:361	palmitate	353:361	We found that Wnt-5a is modified with palmitate at Cys104 and glycans at Asn114, Asn120, Asn311 and Asn325.
17117926	0	39	gly	glycosylation	38:50	arg1	Wnt-5a					55:60	Wnt-5a	55:60	Wnt-5a	55:60	Post-translational palmitoylation and glycosylation of Wnt-5a are necessary for its signalling.
17117926	6	40	theme	Frizzled	765:772	arg1	internalization					742:756	the internalization	738:756	the internalization of Fz (Frizzled) 5	738:775	Wild-type Wnt-5a induced the internalization of Fz (Frizzled) 5, but a Wnt-5a mutant that lacks the palmitoylation site did not.
17117926	7	41	theme	Fz5	908:910	arg1	domain					898:903	the extracellular domain	880:903	the extracellular domain of Fz5	880:910	Furthermore, the binding of Wnt-5a to the extracellular domain of Fz5 required palmitoylation of Wnt-5a.
17117926	7	41	theme	Fz5	908:910	arg1	Fz5					908:910	Fz5	908:910	Fz5	908:910	Furthermore, the binding of Wnt-5a to the extracellular domain of Fz5 required palmitoylation of Wnt-5a.
17117926	4	42	theme	cell	608:611	arg1	migration					613:621	cell migration	608:621	cell migration	608:621	The palmitoylation was not essential for the secretion of Wnt-5a, but was necessary for its ability to suppress Wnt-3a-dependent T-cell factor transcriptional activity and to stimulate cell migration.
17117926	8	43	theme	lipid-unmodified	1097:1112	arg1	activate					1136:1143	activate	1136:1143	activate intracellular signal cascades	1136:1173	These results indicate that palmitoylation of Wnt-5a is important for the triggering of signalling at the cell surface level and, therefore, that the lipid-unmodified form of Wnt-5a cannot activate intracellular signal cascades.
17117926	8	43	theme	lipid-unmodified	1097:1112	arg1	form					1114:1117	the lipid-unmodified form	1093:1117	the lipid-unmodified form of Wnt-5a	1093:1127	These results indicate that palmitoylation of Wnt-5a is important for the triggering of signalling at the cell surface level and, therefore, that the lipid-unmodified form of Wnt-5a cannot activate intracellular signal cascades.
17117926	3	44	from	Asn325	415:420	arg1	glycans					377:383	glycans	377:383	glycans at Asn114, Asn120, Asn311 and Asn325	377:420	We found that Wnt-5a is modified with palmitate at Cys104 and glycans at Asn114, Asn120, Asn311 and Asn325.
17117926	3	44	from	Asn325	415:420	arg1	Cys104					366:371	Cys104	366:371	Cys104	366:371	We found that Wnt-5a is modified with palmitate at Cys104 and glycans at Asn114, Asn120, Asn311 and Asn325.
17117926	9	45	from	necessary	1207:1215	arg1	contrast					1179:1186	contrast	1179:1186	contrast	1179:1186	In contrast, glycosylation was necessary for the secretion of Wnt-5a, but not essential for the actions of Wnt-5a.
17117926	7	46	theme	extracellular	884:896	arg1	domain					898:903	the extracellular domain	880:903	the extracellular domain of Fz5	880:910	Furthermore, the binding of Wnt-5a to the extracellular domain of Fz5 required palmitoylation of Wnt-5a.
17117926	7	46	theme	extracellular	884:896	arg1	Fz5					908:910	Fz5	908:910	Fz5	908:910	Furthermore, the binding of Wnt-5a to the extracellular domain of Fz5 required palmitoylation of Wnt-5a.
17117926	8	47	theme	Wnt-5a	1122:1127	arg1	activate					1136:1143	activate	1136:1143	activate intracellular signal cascades	1136:1173	These results indicate that palmitoylation of Wnt-5a is important for the triggering of signalling at the cell surface level and, therefore, that the lipid-unmodified form of Wnt-5a cannot activate intracellular signal cascades.
17117926	8	47	theme	Wnt-5a	1122:1127	arg1	form					1114:1117	the lipid-unmodified form	1093:1117	the lipid-unmodified form of Wnt-5a	1093:1127	These results indicate that palmitoylation of Wnt-5a is important for the triggering of signalling at the cell surface level and, therefore, that the lipid-unmodified form of Wnt-5a cannot activate intracellular signal cascades.
17117926	2	48	theme	present	206:212	arg1	paper					214:218	the present paper	202:218	the present paper	202:218	In the present paper, the roles of the post-translational modifications in the actions of Wnt-5a were investigated.
17117926	6	49	theme	Fz	761:762	arg1	Frizzled					765:772	Fz (Frizzled) 5	761:775	Fz (Frizzled) 5	761:775	Wild-type Wnt-5a induced the internalization of Fz (Frizzled) 5, but a Wnt-5a mutant that lacks the palmitoylation site did not.
17117926	1	50	theme	beta-catenin-independent	147:170	arg1	pathway					172:178	a beta-catenin-independent pathway	145:178	a beta-catenin-independent pathway in Wnt signalling	145:196	Wnt-5a is a representative ligand that activates a beta-catenin-independent pathway in Wnt signalling.
17117926	3	51	from	Asn120	396:401	arg1	glycans					377:383	glycans	377:383	glycans at Asn114, Asn120, Asn311 and Asn325	377:420	We found that Wnt-5a is modified with palmitate at Cys104 and glycans at Asn114, Asn120, Asn311 and Asn325.
17117926	3	51	from	Asn120	396:401	arg1	Cys104					366:371	Cys104	366:371	Cys104	366:371	We found that Wnt-5a is modified with palmitate at Cys104 and glycans at Asn114, Asn120, Asn311 and Asn325.
17117926	2	52	theme	modifications	257:269	arg1	roles					225:229	the roles	221:229	the roles of the post-translational modifications in the actions of Wnt-5a	221:294	In the present paper, the roles of the post-translational modifications in the actions of Wnt-5a were investigated.
17117926	10	53	dep	actions	1384:1390	arg1	the					1380:1382	the	1380:1382	the	1380:1382	Thus the post-translational palmitoylation and glycosylation of Wnt-5a are important for the actions and secretion of Wnt-5a.
17117926	8	54	theme	intracellular	1145:1157	arg1	cascades					1166:1173	intracellular signal cascades	1145:1173	intracellular signal cascades	1145:1173	These results indicate that palmitoylation of Wnt-5a is important for the triggering of signalling at the cell surface level and, therefore, that the lipid-unmodified form of Wnt-5a cannot activate intracellular signal cascades.
15253437	3	0	theme	asparagine	790:799	arg1	residue					801:807	the asparagine residue	786:807	the asparagine residue	786:807	After hydrolysis with these enzymes, a single N-acetylglucosamine (GlcNAc) residue remains linked to the asparagine residue.
15253437	4	1	theme	glycosylation	987:999	arg1	site					1001:1004	the glycosylation site	983:1004	the glycosylation site	983:1004	The removal of the major part of the glycan simplifies the MS/MS fragment ion spectra of glycopeptides, while the remaining GlcNAc residue enables unambiguous assignment of the glycosylation site together with the amino acid sequence.
15253437	4	2	gly	glycosylation	987:999	arg2	site					1001:1004	the glycosylation site	983:1004	the glycosylation site	983:1004	The removal of the major part of the glycan simplifies the MS/MS fragment ion spectra of glycopeptides, while the remaining GlcNAc residue enables unambiguous assignment of the glycosylation site together with the amino acid sequence.
15253437	4	3	theme	glycan	847:852	arg1	part					835:838	the major part	825:838	the major part of the glycan	825:852	The removal of the major part of the glycan simplifies the MS/MS fragment ion spectra of glycopeptides, while the remaining GlcNAc residue enables unambiguous assignment of the glycosylation site together with the amino acid sequence.
15253437	1	4	theme	full	293:296	arg1	characterization					298:313	the full characterization	289:313	the full characterization of all glycan structures attached to each glycosylation site	289:374	Characterization of glycoproteins using mass spectrometry ranges from determination of carbohydrate-protein linkages to the full characterization of all glycan structures attached to each glycosylation site.
15253437	1	5	gly	glycoproteins	189:201	arg1	glycoproteins					189:201	glycoproteins	189:201	glycoproteins using mass spectrometry	189:225	Characterization of glycoproteins using mass spectrometry ranges from determination of carbohydrate-protein linkages to the full characterization of all glycan structures attached to each glycosylation site.
15253437	0	6	theme	glycosylation	97:109	arg1	sites					111:115	their glycosylation sites	91:115	their glycosylation sites	91:115	A new strategy for identification of N-glycosylated proteins and unambiguous assignment of their glycosylation sites using HILIC enrichment and partial deglycosylation.
15253437	2	7	theme	partial	588:594	arg1	deglycosylation					596:610	partial deglycosylation	588:610	partial deglycosylation using a combination of endo-beta-N-acetylglucosaminidases (EC 3.2.1.96)	588:682	In a novel approach to identify N-glycosylation sites in complex biological samples, we performed an enrichment of glycosylated peptides through hydrophilic interaction liquid chromatography (HILIC) followed by partial deglycosylation using a combination of endo-beta-N-acetylglucosaminidases (EC 3.2.1.96).
15253437	5	8	theme	human	1165:1169	arg1	plasma					1171:1176	human plasma	1165:1176	human plasma	1165:1176	We first tested our approach on a mixture of known glycoproteins, and subsequently the method was applied to samples of human plasma obtained by lectin chromatography followed by 1D gel-electrophoresis for determination of 62 glycosylation sites in 37 glycoproteins.
15253437	4	9	theme	unambiguous	957:967	arg1	assignment					969:978	unambiguous assignment	957:978	unambiguous assignment of the glycosylation site together with the amino acid sequence	957:1042	The removal of the major part of the glycan simplifies the MS/MS fragment ion spectra of glycopeptides, while the remaining GlcNAc residue enables unambiguous assignment of the glycosylation site together with the amino acid sequence.
15253437	5	10	from	sites	1285:1289	arg1	glycoproteins					1297:1309	37 glycoproteins	1294:1309	37 glycoproteins	1294:1309	We first tested our approach on a mixture of known glycoproteins, and subsequently the method was applied to samples of human plasma obtained by lectin chromatography followed by 1D gel-electrophoresis for determination of 62 glycosylation sites in 37 glycoproteins.
15253437	5	11	theme	plasma	1171:1176	arg1	samples					1154:1160	samples	1154:1160	samples of human plasma obtained by lectin chromatography followed by 1D gel-electrophoresis for determination of 62 glycosylation sites in 37 glycoproteins	1154:1309	We first tested our approach on a mixture of known glycoproteins, and subsequently the method was applied to samples of human plasma obtained by lectin chromatography followed by 1D gel-electrophoresis for determination of 62 glycosylation sites in 37 glycoproteins.
15253437	5	12	from	approach	1065:1072	arg1	mixture					1079:1085	a mixture	1077:1085	a mixture of known glycoproteins	1077:1108	We first tested our approach on a mixture of known glycoproteins, and subsequently the method was applied to samples of human plasma obtained by lectin chromatography followed by 1D gel-electrophoresis for determination of 62 glycosylation sites in 37 glycoproteins.
15253437	2	13	theme	complex	434:440	arg1	samples					453:459	complex biological samples	434:459	complex biological samples	434:459	In a novel approach to identify N-glycosylation sites in complex biological samples, we performed an enrichment of glycosylated peptides through hydrophilic interaction liquid chromatography (HILIC) followed by partial deglycosylation using a combination of endo-beta-N-acetylglucosaminidases (EC 3.2.1.96).
15253437	1	14	theme	glycoproteins	189:201	arg1	Characterization					169:184	Characterization	169:184	Characterization of glycoproteins using mass spectrometry	169:225	Characterization of glycoproteins using mass spectrometry ranges from determination of carbohydrate-protein linkages to the full characterization of all glycan structures attached to each glycosylation site.
15253437	0	15	theme	sites	111:115	arg1	strategy					6:13	A new strategy	0:13	A new strategy for identification of N-glycosylated proteins	0:59	A new strategy for identification of N-glycosylated proteins and unambiguous assignment of their glycosylation sites using HILIC enrichment and partial deglycosylation.
15253437	0	15	theme	sites	111:115	arg1	assignment					77:86	unambiguous assignment	65:86	unambiguous assignment of their glycosylation sites	65:115	A new strategy for identification of N-glycosylated proteins and unambiguous assignment of their glycosylation sites using HILIC enrichment and partial deglycosylation.
15253437	4	16	theme	ion	884:886	arg1	spectra					888:894	the MS/MS fragment ion spectra	865:894	the MS/MS fragment ion spectra of glycopeptides	865:911	The removal of the major part of the glycan simplifies the MS/MS fragment ion spectra of glycopeptides, while the remaining GlcNAc residue enables unambiguous assignment of the glycosylation site together with the amino acid sequence.
15253437	1	17	attach	attached	340:347	arg1	site					371:374	each glycosylation site	352:374	each glycosylation site	352:374	Characterization of glycoproteins using mass spectrometry ranges from determination of carbohydrate-protein linkages to the full characterization of all glycan structures attached to each glycosylation site.
15253437	1	17	attach	attached	340:347	arg2	structures					329:338	all glycan structures	318:338	all glycan structures attached to each glycosylation site	318:374	Characterization of glycoproteins using mass spectrometry ranges from determination of carbohydrate-protein linkages to the full characterization of all glycan structures attached to each glycosylation site.
15253437	4	18	theme	amino	1024:1028	arg1	sequence					1035:1042	the amino acid sequence	1020:1042	the amino acid sequence	1020:1042	The removal of the major part of the glycan simplifies the MS/MS fragment ion spectra of glycopeptides, while the remaining GlcNAc residue enables unambiguous assignment of the glycosylation site together with the amino acid sequence.
15253437	2	19	theme	biological	442:451	arg1	samples					453:459	complex biological samples	434:459	complex biological samples	434:459	In a novel approach to identify N-glycosylation sites in complex biological samples, we performed an enrichment of glycosylated peptides through hydrophilic interaction liquid chromatography (HILIC) followed by partial deglycosylation using a combination of endo-beta-N-acetylglucosaminidases (EC 3.2.1.96).
15253437	0	20	theme	new	2:4	arg1	strategy					6:13	A new strategy	0:13	A new strategy for identification of N-glycosylated proteins	0:59	A new strategy for identification of N-glycosylated proteins and unambiguous assignment of their glycosylation sites using HILIC enrichment and partial deglycosylation.
15253437	4	21	theme	GlcNAc	934:939	arg1	residue					941:947	the remaining GlcNAc residue	920:947	the remaining GlcNAc residue	920:947	The removal of the major part of the glycan simplifies the MS/MS fragment ion spectra of glycopeptides, while the remaining GlcNAc residue enables unambiguous assignment of the glycosylation site together with the amino acid sequence.
15253437	1	22	theme	mass	209:212	arg1	spectrometry					214:225	mass spectrometry	209:225	mass spectrometry	209:225	Characterization of glycoproteins using mass spectrometry ranges from determination of carbohydrate-protein linkages to the full characterization of all glycan structures attached to each glycosylation site.
15253437	2	23	theme	glycosylated	492:503	arg1	peptides					505:512	glycosylated peptides	492:512	glycosylated peptides	492:512	In a novel approach to identify N-glycosylation sites in complex biological samples, we performed an enrichment of glycosylated peptides through hydrophilic interaction liquid chromatography (HILIC) followed by partial deglycosylation using a combination of endo-beta-N-acetylglucosaminidases (EC 3.2.1.96).
15253437	1	24	theme	glycan	322:327	arg1	structures					329:338	all glycan structures	318:338	all glycan structures attached to each glycosylation site	318:374	Characterization of glycoproteins using mass spectrometry ranges from determination of carbohydrate-protein linkages to the full characterization of all glycan structures attached to each glycosylation site.
15253437	4	25	theme	remaining	924:932	arg1	residue					941:947	the remaining GlcNAc residue	920:947	the remaining GlcNAc residue	920:947	The removal of the major part of the glycan simplifies the MS/MS fragment ion spectra of glycopeptides, while the remaining GlcNAc residue enables unambiguous assignment of the glycosylation site together with the amino acid sequence.
15253437	2	26	from	sites	425:429	arg1	samples					453:459	complex biological samples	434:459	complex biological samples	434:459	In a novel approach to identify N-glycosylation sites in complex biological samples, we performed an enrichment of glycosylated peptides through hydrophilic interaction liquid chromatography (HILIC) followed by partial deglycosylation using a combination of endo-beta-N-acetylglucosaminidases (EC 3.2.1.96).
15253437	0	27	gly	glycosylation	97:109	arg2	sites					111:115	their glycosylation sites	91:115	their glycosylation sites	91:115	A new strategy for identification of N-glycosylated proteins and unambiguous assignment of their glycosylation sites using HILIC enrichment and partial deglycosylation.
15253437	5	28	from	determination	1251:1263	arg1	glycoproteins					1297:1309	37 glycoproteins	1294:1309	37 glycoproteins	1294:1309	We first tested our approach on a mixture of known glycoproteins, and subsequently the method was applied to samples of human plasma obtained by lectin chromatography followed by 1D gel-electrophoresis for determination of 62 glycosylation sites in 37 glycoproteins.
15253437	4	29	gly	glycopeptides	899:911	arg2	glycopeptides					899:911	glycopeptides	899:911	glycopeptides	899:911	The removal of the major part of the glycan simplifies the MS/MS fragment ion spectra of glycopeptides, while the remaining GlcNAc residue enables unambiguous assignment of the glycosylation site together with the amino acid sequence.
15253437	1	30	theme	structures	329:338	arg1	characterization					298:313	the full characterization	289:313	the full characterization of all glycan structures attached to each glycosylation site	289:374	Characterization of glycoproteins using mass spectrometry ranges from determination of carbohydrate-protein linkages to the full characterization of all glycan structures attached to each glycosylation site.
15253437	2	31	gly	N-glycosylation	409:423	arg2	sites					425:429	N-glycosylation sites	409:429	N-glycosylation sites in complex biological samples	409:459	In a novel approach to identify N-glycosylation sites in complex biological samples, we performed an enrichment of glycosylated peptides through hydrophilic interaction liquid chromatography (HILIC) followed by partial deglycosylation using a combination of endo-beta-N-acetylglucosaminidases (EC 3.2.1.96).
15253437	5	32	gly	glycoproteins	1297:1309	arg1	glycoproteins					1297:1309	37 glycoproteins	1294:1309	37 glycoproteins	1294:1309	We first tested our approach on a mixture of known glycoproteins, and subsequently the method was applied to samples of human plasma obtained by lectin chromatography followed by 1D gel-electrophoresis for determination of 62 glycosylation sites in 37 glycoproteins.
15253437	4	33	theme	part	835:838	arg1	removal					814:820	The removal	810:820	The removal of the major part of the glycan	810:852	The removal of the major part of the glycan simplifies the MS/MS fragment ion spectra of glycopeptides, while the remaining GlcNAc residue enables unambiguous assignment of the glycosylation site together with the amino acid sequence.
15253437	5	34	theme	glycosylation	1271:1283	arg1	sites					1285:1289	62 glycosylation sites	1268:1289	62 glycosylation sites in 37 glycoproteins	1268:1309	We first tested our approach on a mixture of known glycoproteins, and subsequently the method was applied to samples of human plasma obtained by lectin chromatography followed by 1D gel-electrophoresis for determination of 62 glycosylation sites in 37 glycoproteins.
15253437	0	35	theme	HILIC	123:127	arg1	enrichment					129:138	HILIC enrichment	123:138	HILIC enrichment	123:138	A new strategy for identification of N-glycosylated proteins and unambiguous assignment of their glycosylation sites using HILIC enrichment and partial deglycosylation.
15253437	3	36	theme	N-acetylglucosamine	731:749	arg1	residue					760:766	a single N-acetylglucosamine (GlcNAc) residue	722:766	a single N-acetylglucosamine (GlcNAc) residue	722:766	After hydrolysis with these enzymes, a single N-acetylglucosamine (GlcNAc) residue remains linked to the asparagine residue.
15253437	4	37	theme	major	829:833	arg1	part					835:838	the major part	825:838	the major part of the glycan	825:852	The removal of the major part of the glycan simplifies the MS/MS fragment ion spectra of glycopeptides, while the remaining GlcNAc residue enables unambiguous assignment of the glycosylation site together with the amino acid sequence.
15253437	2	38	theme	hydrophilic	522:532	arg1	HILIC					569:573	HILIC	569:573	HILIC	569:573	In a novel approach to identify N-glycosylation sites in complex biological samples, we performed an enrichment of glycosylated peptides through hydrophilic interaction liquid chromatography (HILIC) followed by partial deglycosylation using a combination of endo-beta-N-acetylglucosaminidases (EC 3.2.1.96).
15253437	2	38	theme	hydrophilic	522:532	arg1	chromatography					553:566	hydrophilic interaction liquid chromatography	522:566	hydrophilic interaction liquid chromatography (HILIC) followed by partial deglycosylation using a combination of endo-beta-N-acetylglucosaminidases (EC 3.2.1.96)	522:682	In a novel approach to identify N-glycosylation sites in complex biological samples, we performed an enrichment of glycosylated peptides through hydrophilic interaction liquid chromatography (HILIC) followed by partial deglycosylation using a combination of endo-beta-N-acetylglucosaminidases (EC 3.2.1.96).
15253437	2	39	theme	liquid	546:551	arg1	HILIC					569:573	HILIC	569:573	HILIC	569:573	In a novel approach to identify N-glycosylation sites in complex biological samples, we performed an enrichment of glycosylated peptides through hydrophilic interaction liquid chromatography (HILIC) followed by partial deglycosylation using a combination of endo-beta-N-acetylglucosaminidases (EC 3.2.1.96).
15253437	2	39	theme	liquid	546:551	arg1	chromatography					553:566	hydrophilic interaction liquid chromatography	522:566	hydrophilic interaction liquid chromatography (HILIC) followed by partial deglycosylation using a combination of endo-beta-N-acetylglucosaminidases (EC 3.2.1.96)	522:682	In a novel approach to identify N-glycosylation sites in complex biological samples, we performed an enrichment of glycosylated peptides through hydrophilic interaction liquid chromatography (HILIC) followed by partial deglycosylation using a combination of endo-beta-N-acetylglucosaminidases (EC 3.2.1.96).
15253437	5	40	theme	sites	1285:1289	arg1	determination					1251:1263	determination	1251:1263	determination of 62 glycosylation sites in 37 glycoproteins	1251:1309	We first tested our approach on a mixture of known glycoproteins, and subsequently the method was applied to samples of human plasma obtained by lectin chromatography followed by 1D gel-electrophoresis for determination of 62 glycosylation sites in 37 glycoproteins.
15253437	0	41	theme	partial	144:150	arg1	deglycosylation					152:166	partial deglycosylation	144:166	partial deglycosylation	144:166	A new strategy for identification of N-glycosylated proteins and unambiguous assignment of their glycosylation sites using HILIC enrichment and partial deglycosylation.
15253437	5	42	gly	glycoproteins	1096:1108	arg1	glycoproteins					1096:1108	known glycoproteins	1090:1108	known glycoproteins	1090:1108	We first tested our approach on a mixture of known glycoproteins, and subsequently the method was applied to samples of human plasma obtained by lectin chromatography followed by 1D gel-electrophoresis for determination of 62 glycosylation sites in 37 glycoproteins.
15253437	5	43	theme	known	1090:1094	arg1	glycoproteins					1096:1108	known glycoproteins	1090:1108	known glycoproteins	1090:1108	We first tested our approach on a mixture of known glycoproteins, and subsequently the method was applied to samples of human plasma obtained by lectin chromatography followed by 1D gel-electrophoresis for determination of 62 glycosylation sites in 37 glycoproteins.
15253437	2	44	theme	interaction	534:544	arg1	HILIC					569:573	HILIC	569:573	HILIC	569:573	In a novel approach to identify N-glycosylation sites in complex biological samples, we performed an enrichment of glycosylated peptides through hydrophilic interaction liquid chromatography (HILIC) followed by partial deglycosylation using a combination of endo-beta-N-acetylglucosaminidases (EC 3.2.1.96).
15253437	2	44	theme	interaction	534:544	arg1	chromatography					553:566	hydrophilic interaction liquid chromatography	522:566	hydrophilic interaction liquid chromatography (HILIC) followed by partial deglycosylation using a combination of endo-beta-N-acetylglucosaminidases (EC 3.2.1.96)	522:682	In a novel approach to identify N-glycosylation sites in complex biological samples, we performed an enrichment of glycosylated peptides through hydrophilic interaction liquid chromatography (HILIC) followed by partial deglycosylation using a combination of endo-beta-N-acetylglucosaminidases (EC 3.2.1.96).
15253437	5	45	theme	1D	1224:1225	arg1	gel-electrophoresis					1227:1245	1D gel-electrophoresis	1224:1245	1D gel-electrophoresis	1224:1245	We first tested our approach on a mixture of known glycoproteins, and subsequently the method was applied to samples of human plasma obtained by lectin chromatography followed by 1D gel-electrophoresis for determination of 62 glycosylation sites in 37 glycoproteins.
15253437	5	46	theme	glycoproteins	1096:1108	arg1	mixture					1079:1085	a mixture	1077:1085	a mixture of known glycoproteins	1077:1108	We first tested our approach on a mixture of known glycoproteins, and subsequently the method was applied to samples of human plasma obtained by lectin chromatography followed by 1D gel-electrophoresis for determination of 62 glycosylation sites in 37 glycoproteins.
15253437	3	47	with	hydrolysis	691:700	arg1	enzymes					713:719	these enzymes	707:719	these enzymes	707:719	After hydrolysis with these enzymes, a single N-acetylglucosamine (GlcNAc) residue remains linked to the asparagine residue.
15253437	0	48	theme	proteins	52:59	arg1	identification					19:32	identification	19:32	identification of N-glycosylated proteins	19:59	A new strategy for identification of N-glycosylated proteins and unambiguous assignment of their glycosylation sites using HILIC enrichment and partial deglycosylation.
15253437	1	49	theme	glycosylation	357:369	arg1	site					371:374	each glycosylation site	352:374	each glycosylation site	352:374	Characterization of glycoproteins using mass spectrometry ranges from determination of carbohydrate-protein linkages to the full characterization of all glycan structures attached to each glycosylation site.
15253437	3	50	theme	single	724:729	arg1	residue					760:766	a single N-acetylglucosamine (GlcNAc) residue	722:766	a single N-acetylglucosamine (GlcNAc) residue	722:766	After hydrolysis with these enzymes, a single N-acetylglucosamine (GlcNAc) residue remains linked to the asparagine residue.
15253437	0	51	theme	N-glycosylated	37:50	arg1	proteins					52:59	N-glycosylated proteins	37:59	N-glycosylated proteins	37:59	A new strategy for identification of N-glycosylated proteins and unambiguous assignment of their glycosylation sites using HILIC enrichment and partial deglycosylation.
15253437	5	52	from	glycoproteins	1297:1309	arg1	determination					1251:1263	determination	1251:1263	determination of 62 glycosylation sites in 37 glycoproteins	1251:1309	We first tested our approach on a mixture of known glycoproteins, and subsequently the method was applied to samples of human plasma obtained by lectin chromatography followed by 1D gel-electrophoresis for determination of 62 glycosylation sites in 37 glycoproteins.
15253437	4	53	theme	glycopeptides	899:911	arg1	spectra					888:894	the MS/MS fragment ion spectra	865:894	the MS/MS fragment ion spectra of glycopeptides	865:911	The removal of the major part of the glycan simplifies the MS/MS fragment ion spectra of glycopeptides, while the remaining GlcNAc residue enables unambiguous assignment of the glycosylation site together with the amino acid sequence.
15253437	2	54	theme	novel	382:386	arg1	approach					388:395	a novel approach	380:395	a novel approach to identify N-glycosylation sites in complex biological samples	380:459	In a novel approach to identify N-glycosylation sites in complex biological samples, we performed an enrichment of glycosylated peptides through hydrophilic interaction liquid chromatography (HILIC) followed by partial deglycosylation using a combination of endo-beta-N-acetylglucosaminidases (EC 3.2.1.96).
15253437	4	55	theme	site	1001:1004	arg1	assignment					969:978	unambiguous assignment	957:978	unambiguous assignment of the glycosylation site together with the amino acid sequence	957:1042	The removal of the major part of the glycan simplifies the MS/MS fragment ion spectra of glycopeptides, while the remaining GlcNAc residue enables unambiguous assignment of the glycosylation site together with the amino acid sequence.
15253437	4	56	theme	MS/MS	869:873	arg1	spectra					888:894	the MS/MS fragment ion spectra	865:894	the MS/MS fragment ion spectra of glycopeptides	865:911	The removal of the major part of the glycan simplifies the MS/MS fragment ion spectra of glycopeptides, while the remaining GlcNAc residue enables unambiguous assignment of the glycosylation site together with the amino acid sequence.
15253437	2	57	gly	glycosylated	492:503	arg1	peptides					505:512	glycosylated peptides	492:512	glycosylated peptides	492:512	In a novel approach to identify N-glycosylation sites in complex biological samples, we performed an enrichment of glycosylated peptides through hydrophilic interaction liquid chromatography (HILIC) followed by partial deglycosylation using a combination of endo-beta-N-acetylglucosaminidases (EC 3.2.1.96).
15253437	5	58	gly	glycosylation	1271:1283	arg2	sites					1285:1289	62 glycosylation sites	1268:1289	62 glycosylation sites in 37 glycoproteins	1268:1309	We first tested our approach on a mixture of known glycoproteins, and subsequently the method was applied to samples of human plasma obtained by lectin chromatography followed by 1D gel-electrophoresis for determination of 62 glycosylation sites in 37 glycoproteins.
15253437	5	58	gly	glycosylation	1271:1283	arg2	62					1268:1269	62	1268:1269	62	1268:1269	We first tested our approach on a mixture of known glycoproteins, and subsequently the method was applied to samples of human plasma obtained by lectin chromatography followed by 1D gel-electrophoresis for determination of 62 glycosylation sites in 37 glycoproteins.
15253437	1	59	theme	carbohydrate-protein	256:275	arg1	linkages					277:284	carbohydrate-protein linkages	256:284	carbohydrate-protein linkages	256:284	Characterization of glycoproteins using mass spectrometry ranges from determination of carbohydrate-protein linkages to the full characterization of all glycan structures attached to each glycosylation site.
15253437	2	60	theme	endo-beta-N-acetylglucosaminidases	635:668	arg1	combination					620:630	a combination	618:630	a combination of endo-beta-N-acetylglucosaminidases (EC 3.2.1.96)	618:682	In a novel approach to identify N-glycosylation sites in complex biological samples, we performed an enrichment of glycosylated peptides through hydrophilic interaction liquid chromatography (HILIC) followed by partial deglycosylation using a combination of endo-beta-N-acetylglucosaminidases (EC 3.2.1.96).
15253437	3	61	theme	GlcNAc	752:757	arg1	residue					760:766	a single N-acetylglucosamine (GlcNAc) residue	722:766	a single N-acetylglucosamine (GlcNAc) residue	722:766	After hydrolysis with these enzymes, a single N-acetylglucosamine (GlcNAc) residue remains linked to the asparagine residue.
15253437	1	62	gly	glycosylation	357:369	arg2	site					371:374	each glycosylation site	352:374	each glycosylation site	352:374	Characterization of glycoproteins using mass spectrometry ranges from determination of carbohydrate-protein linkages to the full characterization of all glycan structures attached to each glycosylation site.
15253437	1	63	theme	linkages	277:284	arg1	determination					239:251	determination	239:251	determination of carbohydrate-protein linkages	239:284	Characterization of glycoproteins using mass spectrometry ranges from determination of carbohydrate-protein linkages to the full characterization of all glycan structures attached to each glycosylation site.
15253437	0	64	theme	unambiguous	65:75	arg1	assignment					77:86	unambiguous assignment	65:86	unambiguous assignment of their glycosylation sites	65:115	A new strategy for identification of N-glycosylated proteins and unambiguous assignment of their glycosylation sites using HILIC enrichment and partial deglycosylation.
15253437	0	65	gly	N-glycosylated	37:50	arg1	proteins					52:59	N-glycosylated proteins	37:59	N-glycosylated proteins	37:59	A new strategy for identification of N-glycosylated proteins and unambiguous assignment of their glycosylation sites using HILIC enrichment and partial deglycosylation.
15253437	2	66	theme	peptides	505:512	arg1	enrichment					478:487	an enrichment	475:487	an enrichment of glycosylated peptides	475:512	In a novel approach to identify N-glycosylation sites in complex biological samples, we performed an enrichment of glycosylated peptides through hydrophilic interaction liquid chromatography (HILIC) followed by partial deglycosylation using a combination of endo-beta-N-acetylglucosaminidases (EC 3.2.1.96).
15253437	5	67	theme	lectin	1190:1195	arg1	chromatography					1197:1210	lectin chromatography	1190:1210	lectin chromatography followed by 1D gel-electrophoresis for determination of 62 glycosylation sites in 37 glycoproteins	1190:1309	We first tested our approach on a mixture of known glycoproteins, and subsequently the method was applied to samples of human plasma obtained by lectin chromatography followed by 1D gel-electrophoresis for determination of 62 glycosylation sites in 37 glycoproteins.
15253437	4	68	theme	fragment	875:882	arg1	spectra					888:894	the MS/MS fragment ion spectra	865:894	the MS/MS fragment ion spectra of glycopeptides	865:911	The removal of the major part of the glycan simplifies the MS/MS fragment ion spectra of glycopeptides, while the remaining GlcNAc residue enables unambiguous assignment of the glycosylation site together with the amino acid sequence.
15253437	2	69	theme	N-glycosylation	409:423	arg1	sites					425:429	N-glycosylation sites	409:429	N-glycosylation sites in complex biological samples	409:459	In a novel approach to identify N-glycosylation sites in complex biological samples, we performed an enrichment of glycosylated peptides through hydrophilic interaction liquid chromatography (HILIC) followed by partial deglycosylation using a combination of endo-beta-N-acetylglucosaminidases (EC 3.2.1.96).
15253437	4	70	theme	acid	1030:1033	arg1	sequence					1035:1042	the amino acid sequence	1020:1042	the amino acid sequence	1020:1042	The removal of the major part of the glycan simplifies the MS/MS fragment ion spectra of glycopeptides, while the remaining GlcNAc residue enables unambiguous assignment of the glycosylation site together with the amino acid sequence.
12731890	5	0	theme	receptor	1062:1069	arg1	form					1050:1053	the secreted form	1037:1053	the secreted form of the receptor	1037:1069	We show that an additional canonical site in the secreted form of the receptor is fully glycosylated.
12731890	6	1	theme	receptor	1211:1218	arg1	forms					1198:1202	the secreted forms	1185:1202	the secreted forms of the receptor	1185:1218	While the pattern of glycosylation is the same for the sites shared by the full-length and the secreted forms of the receptor, the oligosaccharides of the full-length receptor are more extensively processed.
12731890	3	2	theme	human	775:779	arg1	receptor					785:792	the recombinant human EGF receptor	759:792	the recombinant human EGF receptor heterologously expressed in Chinese hamster ovary cells	759:848	Our data show that the naturally expressed human EGF receptor is fully glycosylated on eight of the 11 canonical sites; two of the sites are not glycosylated, and one is partially glycosylated, a pattern of site-usage similar but not identical to those reported for the recombinant human EGF receptor heterologously expressed in Chinese hamster ovary cells.
12731890	6	3	theme	receptor	1261:1268	arg1	oligosaccharides					1225:1240	the oligosaccharides	1221:1240	the oligosaccharides of the full-length receptor	1221:1268	While the pattern of glycosylation is the same for the sites shared by the full-length and the secreted forms of the receptor, the oligosaccharides of the full-length receptor are more extensively processed.
12731890	7	4	theme	conditioned	1523:1533	arg1	medium					1535:1540	the conditioned medium	1519:1540	the conditioned medium	1519:1540	Finally, we provide evidence that in addition to the known secreted form of the receptor, a proteolytic cleavage product of the receptor corresponding to the full extracytoplasmic, ligand-binding domain is present in the conditioned medium.
12731890	7	5	from	medium	1535:1540	arg1	present					1508:1514	present	1508:1514	present	1508:1514	Finally, we provide evidence that in addition to the known secreted form of the receptor, a proteolytic cleavage product of the receptor corresponding to the full extracytoplasmic, ligand-binding domain is present in the conditioned medium.
12731890	7	5	from	medium	1535:1540	arg1	product					1415:1421	a proteolytic cleavage product	1392:1421	a proteolytic cleavage product of the receptor corresponding to the full extracytoplasmic, ligand-binding domain	1392:1503	Finally, we provide evidence that in addition to the known secreted form of the receptor, a proteolytic cleavage product of the receptor corresponding to the full extracytoplasmic, ligand-binding domain is present in the conditioned medium.
12731890	1	6	theme	cellular	168:175	arg1	responses					177:185	the cellular responses	164:185	the cellular responses to epidermal growth factor (EGF) and transforming growth factor-alpha (TGF-alpha)	164:267	The epidermal growth factor receptor is a transmembrane glycoprotein that mediates the cellular responses to epidermal growth factor (EGF) and transforming growth factor-alpha (TGF-alpha).
12731890	3	7	theme	Chinese	822:828	arg1	cells					844:848	Chinese hamster ovary cells	822:848	Chinese hamster ovary cells	822:848	Our data show that the naturally expressed human EGF receptor is fully glycosylated on eight of the 11 canonical sites; two of the sites are not glycosylated, and one is partially glycosylated, a pattern of site-usage similar but not identical to those reported for the recombinant human EGF receptor heterologously expressed in Chinese hamster ovary cells.
12731890	3	8	theme	EGF	781:783	arg1	receptor					785:792	the recombinant human EGF receptor	759:792	the recombinant human EGF receptor heterologously expressed in Chinese hamster ovary cells	759:848	Our data show that the naturally expressed human EGF receptor is fully glycosylated on eight of the 11 canonical sites; two of the sites are not glycosylated, and one is partially glycosylated, a pattern of site-usage similar but not identical to those reported for the recombinant human EGF receptor heterologously expressed in Chinese hamster ovary cells.
12731890	4	9	theme	atypical	899:906	arg1	site					912:915	an atypical NNC site	896:915	an atypical NNC site first identified in the receptor expressed in Chinese hamster ovary cells	896:989	We also confirm the partial glycosylation of an atypical NNC site first identified in the receptor expressed in Chinese hamster ovary cells.
12731890	4	10	gly	glycosylation	879:891	arg1	site					912:915	an atypical NNC site	896:915	an atypical NNC site first identified in the receptor expressed in Chinese hamster ovary cells	896:989	We also confirm the partial glycosylation of an atypical NNC site first identified in the receptor expressed in Chinese hamster ovary cells.
12731890	7	11	attach	present	1508:1514	arg2	product					1415:1421	a proteolytic cleavage product	1392:1421	a proteolytic cleavage product of the receptor corresponding to the full extracytoplasmic, ligand-binding domain	1392:1503	Finally, we provide evidence that in addition to the known secreted form of the receptor, a proteolytic cleavage product of the receptor corresponding to the full extracytoplasmic, ligand-binding domain is present in the conditioned medium.
12731890	7	11	attach	present	1508:1514	arg2	present					1508:1514	present	1508:1514	present	1508:1514	Finally, we provide evidence that in addition to the known secreted form of the receptor, a proteolytic cleavage product of the receptor corresponding to the full extracytoplasmic, ligand-binding domain is present in the conditioned medium.
12731890	7	11	attach	present	1508:1514	arg1	medium					1535:1540	the conditioned medium	1519:1540	the conditioned medium	1519:1540	Finally, we provide evidence that in addition to the known secreted form of the receptor, a proteolytic cleavage product of the receptor corresponding to the full extracytoplasmic, ligand-binding domain is present in the conditioned medium.
12731890	3	12	theme	hamster	830:836	arg1	cells					844:848	Chinese hamster ovary cells	822:848	Chinese hamster ovary cells	822:848	Our data show that the naturally expressed human EGF receptor is fully glycosylated on eight of the 11 canonical sites; two of the sites are not glycosylated, and one is partially glycosylated, a pattern of site-usage similar but not identical to those reported for the recombinant human EGF receptor heterologously expressed in Chinese hamster ovary cells.
12731890	7	13	theme	extracytoplasmic	1465:1480	arg1	domain					1498:1503	the full extracytoplasmic, ligand-binding domain	1456:1503	domain	1498:1503	Finally, we provide evidence that in addition to the known secreted form of the receptor, a proteolytic cleavage product of the receptor corresponding to the full extracytoplasmic, ligand-binding domain is present in the conditioned medium.
12731890	2	14	theme	receptor	301:308	arg1	study					278:282	this study	273:282	this study of the human EGF receptor naturally expressed in A431 cells	273:342	In this study of the human EGF receptor naturally expressed in A431 cells, the glycosylation sites of the full-length, membrane-bound receptor and of a secreted form of the receptor were characterized by mass spectrometry.
12731890	3	15	theme	human	536:540	arg1	receptor					546:553	the naturally expressed human EGF receptor	512:553	the naturally expressed human EGF receptor	512:553	Our data show that the naturally expressed human EGF receptor is fully glycosylated on eight of the 11 canonical sites; two of the sites are not glycosylated, and one is partially glycosylated, a pattern of site-usage similar but not identical to those reported for the recombinant human EGF receptor heterologously expressed in Chinese hamster ovary cells.
12731890	3	16	theme	expressed	526:534	arg1	receptor					546:553	the naturally expressed human EGF receptor	512:553	the naturally expressed human EGF receptor	512:553	Our data show that the naturally expressed human EGF receptor is fully glycosylated on eight of the 11 canonical sites; two of the sites are not glycosylated, and one is partially glycosylated, a pattern of site-usage similar but not identical to those reported for the recombinant human EGF receptor heterologously expressed in Chinese hamster ovary cells.
12731890	6	17	theme	full-length	1249:1259	arg1	receptor					1261:1268	the full-length receptor	1245:1268	the full-length receptor	1245:1268	While the pattern of glycosylation is the same for the sites shared by the full-length and the secreted forms of the receptor, the oligosaccharides of the full-length receptor are more extensively processed.
12731890	3	18	theme	recombinant	763:773	arg1	receptor					785:792	the recombinant human EGF receptor	759:792	the recombinant human EGF receptor heterologously expressed in Chinese hamster ovary cells	759:848	Our data show that the naturally expressed human EGF receptor is fully glycosylated on eight of the 11 canonical sites; two of the sites are not glycosylated, and one is partially glycosylated, a pattern of site-usage similar but not identical to those reported for the recombinant human EGF receptor heterologously expressed in Chinese hamster ovary cells.
12731890	4	19	theme	site	912:915	arg1	glycosylation					879:891	the partial glycosylation	867:891	the partial glycosylation of an atypical NNC site first identified in the receptor expressed in Chinese hamster ovary cells	867:989	We also confirm the partial glycosylation of an atypical NNC site first identified in the receptor expressed in Chinese hamster ovary cells.
12731890	5	20	theme	secreted	1041:1048	arg1	form					1050:1053	the secreted form	1037:1053	the secreted form of the receptor	1037:1069	We show that an additional canonical site in the secreted form of the receptor is fully glycosylated.
12731890	6	21	theme	secreted	1189:1196	arg1	forms					1198:1202	the secreted forms	1185:1202	the secreted forms of the receptor	1185:1218	While the pattern of glycosylation is the same for the sites shared by the full-length and the secreted forms of the receptor, the oligosaccharides of the full-length receptor are more extensively processed.
12731890	2	22	theme	full-length	376:386	arg1	receptor					404:411	the full-length, membrane-bound receptor	372:411	the full-length, membrane-bound receptor	372:411	In this study of the human EGF receptor naturally expressed in A431 cells, the glycosylation sites of the full-length, membrane-bound receptor and of a secreted form of the receptor were characterized by mass spectrometry.
12731890	4	23	theme	NNC	908:910	arg1	site					912:915	an atypical NNC site	896:915	an atypical NNC site first identified in the receptor expressed in Chinese hamster ovary cells	896:989	We also confirm the partial glycosylation of an atypical NNC site first identified in the receptor expressed in Chinese hamster ovary cells.
12731890	7	24	theme	ligand-binding	1483:1496	arg1	domain					1498:1503	the full extracytoplasmic, ligand-binding domain	1456:1503	domain	1498:1503	Finally, we provide evidence that in addition to the known secreted form of the receptor, a proteolytic cleavage product of the receptor corresponding to the full extracytoplasmic, ligand-binding domain is present in the conditioned medium.
12731890	4	25	theme	hamster	971:977	arg1	cells					985:989	Chinese hamster ovary cells	963:989	Chinese hamster ovary cells	963:989	We also confirm the partial glycosylation of an atypical NNC site first identified in the receptor expressed in Chinese hamster ovary cells.
12731890	6	26	theme	glycosylation	1115:1127	arg1	same					1136:1139	same	1136:1139	same	1136:1139	While the pattern of glycosylation is the same for the sites shared by the full-length and the secreted forms of the receptor, the oligosaccharides of the full-length receptor are more extensively processed.
12731890	6	26	theme	glycosylation	1115:1127	arg1	pattern					1104:1110	the pattern	1100:1110	the pattern of glycosylation	1100:1127	While the pattern of glycosylation is the same for the sites shared by the full-length and the secreted forms of the receptor, the oligosaccharides of the full-length receptor are more extensively processed.
12731890	2	27	theme	form	431:434	arg1	sites					363:367	the glycosylation sites	345:367	the glycosylation sites of the full-length, membrane-bound receptor and of a secreted form of the receptor	345:450	In this study of the human EGF receptor naturally expressed in A431 cells, the glycosylation sites of the full-length, membrane-bound receptor and of a secreted form of the receptor were characterized by mass spectrometry.
12731890	2	27	theme	form	431:434	arg1	form					431:434	a secreted form	420:434	a secreted form of the receptor	420:450	In this study of the human EGF receptor naturally expressed in A431 cells, the glycosylation sites of the full-length, membrane-bound receptor and of a secreted form of the receptor were characterized by mass spectrometry.
12731890	2	27	theme	form	431:434	arg1	receptor					404:411	the full-length, membrane-bound receptor	372:411	the full-length, membrane-bound receptor	372:411	In this study of the human EGF receptor naturally expressed in A431 cells, the glycosylation sites of the full-length, membrane-bound receptor and of a secreted form of the receptor were characterized by mass spectrometry.
12731890	7	28	located	present	1508:1514	arg2	product					1415:1421	a proteolytic cleavage product	1392:1421	a proteolytic cleavage product of the receptor corresponding to the full extracytoplasmic, ligand-binding domain	1392:1503	Finally, we provide evidence that in addition to the known secreted form of the receptor, a proteolytic cleavage product of the receptor corresponding to the full extracytoplasmic, ligand-binding domain is present in the conditioned medium.
12731890	7	28	located	present	1508:1514	arg2	present					1508:1514	present	1508:1514	present	1508:1514	Finally, we provide evidence that in addition to the known secreted form of the receptor, a proteolytic cleavage product of the receptor corresponding to the full extracytoplasmic, ligand-binding domain is present in the conditioned medium.
12731890	7	28	located	present	1508:1514	arg1	medium					1535:1540	the conditioned medium	1519:1540	the conditioned medium	1519:1540	Finally, we provide evidence that in addition to the known secreted form of the receptor, a proteolytic cleavage product of the receptor corresponding to the full extracytoplasmic, ligand-binding domain is present in the conditioned medium.
12731890	1	29	theme	epidermal	85:93	arg1	glycoprotein					137:148	a transmembrane glycoprotein	121:148	a transmembrane glycoprotein that mediates the cellular responses to epidermal growth factor (EGF) and transforming growth factor-alpha (TGF-alpha)	121:267	The epidermal growth factor receptor is a transmembrane glycoprotein that mediates the cellular responses to epidermal growth factor (EGF) and transforming growth factor-alpha (TGF-alpha).
12731890	1	29	theme	epidermal	85:93	arg1	receptor					109:116	The epidermal growth factor receptor	81:116	The epidermal growth factor receptor	81:116	The epidermal growth factor receptor is a transmembrane glycoprotein that mediates the cellular responses to epidermal growth factor (EGF) and transforming growth factor-alpha (TGF-alpha).
12731890	7	30	theme	receptor	1382:1389	arg1	form					1370:1373	the known secreted form	1351:1373	the known secreted form of the receptor	1351:1389	Finally, we provide evidence that in addition to the known secreted form of the receptor, a proteolytic cleavage product of the receptor corresponding to the full extracytoplasmic, ligand-binding domain is present in the conditioned medium.
12731890	1	31	theme	epidermal	190:198	arg1	EGF					215:217	EGF	215:217	EGF	215:217	The epidermal growth factor receptor is a transmembrane glycoprotein that mediates the cellular responses to epidermal growth factor (EGF) and transforming growth factor-alpha (TGF-alpha).
12731890	1	31	theme	epidermal	190:198	arg1	factor					207:212	epidermal growth factor	190:212	epidermal growth factor (EGF)	190:218	The epidermal growth factor receptor is a transmembrane glycoprotein that mediates the cellular responses to epidermal growth factor (EGF) and transforming growth factor-alpha (TGF-alpha).
12731890	2	32	theme	secreted	422:429	arg1	form					431:434	a secreted form	420:434	a secreted form of the receptor	420:450	In this study of the human EGF receptor naturally expressed in A431 cells, the glycosylation sites of the full-length, membrane-bound receptor and of a secreted form of the receptor were characterized by mass spectrometry.
12731890	7	33	theme	known	1355:1359	arg1	form					1370:1373	the known secreted form	1351:1373	the known secreted form of the receptor	1351:1389	Finally, we provide evidence that in addition to the known secreted form of the receptor, a proteolytic cleavage product of the receptor corresponding to the full extracytoplasmic, ligand-binding domain is present in the conditioned medium.
12731890	4	34	theme	Chinese	963:969	arg1	cells					985:989	Chinese hamster ovary cells	963:989	Chinese hamster ovary cells	963:989	We also confirm the partial glycosylation of an atypical NNC site first identified in the receptor expressed in Chinese hamster ovary cells.
12731890	2	35	theme	EGF	297:299	arg1	receptor					301:308	the human EGF receptor	287:308	the human EGF receptor naturally expressed in A431 cells	287:342	In this study of the human EGF receptor naturally expressed in A431 cells, the glycosylation sites of the full-length, membrane-bound receptor and of a secreted form of the receptor were characterized by mass spectrometry.
12731890	7	36	theme	secreted	1361:1368	arg1	form					1370:1373	the known secreted form	1351:1373	the known secreted form of the receptor	1351:1389	Finally, we provide evidence that in addition to the known secreted form of the receptor, a proteolytic cleavage product of the receptor corresponding to the full extracytoplasmic, ligand-binding domain is present in the conditioned medium.
12731890	1	37	theme	growth	200:205	arg1	EGF					215:217	EGF	215:217	EGF	215:217	The epidermal growth factor receptor is a transmembrane glycoprotein that mediates the cellular responses to epidermal growth factor (EGF) and transforming growth factor-alpha (TGF-alpha).
12731890	1	37	theme	growth	200:205	arg1	factor					207:212	epidermal growth factor	190:212	epidermal growth factor (EGF)	190:218	The epidermal growth factor receptor is a transmembrane glycoprotein that mediates the cellular responses to epidermal growth factor (EGF) and transforming growth factor-alpha (TGF-alpha).
12731890	0	38	theme	sites	34:38	arg1	Characterization					0:15	Characterization	0:15	Characterization of glycosylation sites of the epidermal growth factor receptor.	0:79	Characterization of glycosylation sites of the epidermal growth factor receptor.
12731890	3	39	gly	glycosylated	673:684	arg1	one					656:658	one	656:658	one	656:658	Our data show that the naturally expressed human EGF receptor is fully glycosylated on eight of the 11 canonical sites; two of the sites are not glycosylated, and one is partially glycosylated, a pattern of site-usage similar but not identical to those reported for the recombinant human EGF receptor heterologously expressed in Chinese hamster ovary cells.
12731890	4	40	theme	partial	871:877	arg1	glycosylation					879:891	the partial glycosylation	867:891	the partial glycosylation of an atypical NNC site first identified in the receptor expressed in Chinese hamster ovary cells	867:989	We also confirm the partial glycosylation of an atypical NNC site first identified in the receptor expressed in Chinese hamster ovary cells.
12731890	1	41	theme	factor	102:107	arg1	glycoprotein					137:148	a transmembrane glycoprotein	121:148	a transmembrane glycoprotein that mediates the cellular responses to epidermal growth factor (EGF) and transforming growth factor-alpha (TGF-alpha)	121:267	The epidermal growth factor receptor is a transmembrane glycoprotein that mediates the cellular responses to epidermal growth factor (EGF) and transforming growth factor-alpha (TGF-alpha).
12731890	1	41	theme	factor	102:107	arg1	receptor					109:116	The epidermal growth factor receptor	81:116	The epidermal growth factor receptor	81:116	The epidermal growth factor receptor is a transmembrane glycoprotein that mediates the cellular responses to epidermal growth factor (EGF) and transforming growth factor-alpha (TGF-alpha).
12731890	1	42	theme	growth	95:100	arg1	glycoprotein					137:148	a transmembrane glycoprotein	121:148	a transmembrane glycoprotein that mediates the cellular responses to epidermal growth factor (EGF) and transforming growth factor-alpha (TGF-alpha)	121:267	The epidermal growth factor receptor is a transmembrane glycoprotein that mediates the cellular responses to epidermal growth factor (EGF) and transforming growth factor-alpha (TGF-alpha).
12731890	1	42	theme	growth	95:100	arg1	receptor					109:116	The epidermal growth factor receptor	81:116	The epidermal growth factor receptor	81:116	The epidermal growth factor receptor is a transmembrane glycoprotein that mediates the cellular responses to epidermal growth factor (EGF) and transforming growth factor-alpha (TGF-alpha).
12731890	2	43	gly	glycosylation	349:361	arg2	form					431:434	a secreted form	420:434	a secreted form of the receptor	420:450	In this study of the human EGF receptor naturally expressed in A431 cells, the glycosylation sites of the full-length, membrane-bound receptor and of a secreted form of the receptor were characterized by mass spectrometry.
12731890	2	43	gly	glycosylation	349:361	arg2	sites					363:367	the glycosylation sites	345:367	the glycosylation sites of the full-length, membrane-bound receptor and of a secreted form of the receptor	345:450	In this study of the human EGF receptor naturally expressed in A431 cells, the glycosylation sites of the full-length, membrane-bound receptor and of a secreted form of the receptor were characterized by mass spectrometry.
12731890	2	43	gly	glycosylation	349:361	arg1	form					431:434	a secreted form	420:434	a secreted form of the receptor	420:450	In this study of the human EGF receptor naturally expressed in A431 cells, the glycosylation sites of the full-length, membrane-bound receptor and of a secreted form of the receptor were characterized by mass spectrometry.
12731890	2	43	gly	glycosylation	349:361	arg1	receptor					404:411	the full-length, membrane-bound receptor	372:411	the full-length, membrane-bound receptor	372:411	In this study of the human EGF receptor naturally expressed in A431 cells, the glycosylation sites of the full-length, membrane-bound receptor and of a secreted form of the receptor were characterized by mass spectrometry.
12731890	2	43	gly	glycosylation	349:361	arg2	receptor					404:411	the full-length, membrane-bound receptor	372:411	the full-length, membrane-bound receptor	372:411	In this study of the human EGF receptor naturally expressed in A431 cells, the glycosylation sites of the full-length, membrane-bound receptor and of a secreted form of the receptor were characterized by mass spectrometry.
12731890	5	44	theme	additional	1008:1017	arg1	site					1029:1032	an additional canonical site	1005:1032	an additional canonical site in the secreted form of the receptor	1005:1069	We show that an additional canonical site in the secreted form of the receptor is fully glycosylated.
12731890	3	45	theme	EGF	542:544	arg1	receptor					546:553	the naturally expressed human EGF receptor	512:553	the naturally expressed human EGF receptor	512:553	Our data show that the naturally expressed human EGF receptor is fully glycosylated on eight of the 11 canonical sites; two of the sites are not glycosylated, and one is partially glycosylated, a pattern of site-usage similar but not identical to those reported for the recombinant human EGF receptor heterologously expressed in Chinese hamster ovary cells.
12731890	2	46	theme	receptor	404:411	arg1	sites					363:367	the glycosylation sites	345:367	the glycosylation sites of the full-length, membrane-bound receptor and of a secreted form of the receptor	345:450	In this study of the human EGF receptor naturally expressed in A431 cells, the glycosylation sites of the full-length, membrane-bound receptor and of a secreted form of the receptor were characterized by mass spectrometry.
12731890	2	46	theme	receptor	404:411	arg1	form					431:434	a secreted form	420:434	a secreted form of the receptor	420:450	In this study of the human EGF receptor naturally expressed in A431 cells, the glycosylation sites of the full-length, membrane-bound receptor and of a secreted form of the receptor were characterized by mass spectrometry.
12731890	2	46	theme	receptor	404:411	arg1	receptor					404:411	the full-length, membrane-bound receptor	372:411	the full-length, membrane-bound receptor	372:411	In this study of the human EGF receptor naturally expressed in A431 cells, the glycosylation sites of the full-length, membrane-bound receptor and of a secreted form of the receptor were characterized by mass spectrometry.
12731890	1	47	gly	glycoprotein	137:148	arg1	glycoprotein					137:148	a transmembrane glycoprotein	121:148	a transmembrane glycoprotein that mediates the cellular responses to epidermal growth factor (EGF) and transforming growth factor-alpha (TGF-alpha)	121:267	The epidermal growth factor receptor is a transmembrane glycoprotein that mediates the cellular responses to epidermal growth factor (EGF) and transforming growth factor-alpha (TGF-alpha).
12731890	1	47	gly	glycoprotein	137:148	arg1	receptor					109:116	The epidermal growth factor receptor	81:116	The epidermal growth factor receptor	81:116	The epidermal growth factor receptor is a transmembrane glycoprotein that mediates the cellular responses to epidermal growth factor (EGF) and transforming growth factor-alpha (TGF-alpha).
12731890	5	48	theme	canonical	1019:1027	arg1	site					1029:1032	an additional canonical site	1005:1032	an additional canonical site in the secreted form of the receptor	1005:1069	We show that an additional canonical site in the secreted form of the receptor is fully glycosylated.
12731890	7	49	theme	cleavage	1406:1413	arg1	present					1508:1514	present	1508:1514	present	1508:1514	Finally, we provide evidence that in addition to the known secreted form of the receptor, a proteolytic cleavage product of the receptor corresponding to the full extracytoplasmic, ligand-binding domain is present in the conditioned medium.
12731890	7	49	theme	cleavage	1406:1413	arg1	product					1415:1421	a proteolytic cleavage product	1392:1421	a proteolytic cleavage product of the receptor corresponding to the full extracytoplasmic, ligand-binding domain	1392:1503	Finally, we provide evidence that in addition to the known secreted form of the receptor, a proteolytic cleavage product of the receptor corresponding to the full extracytoplasmic, ligand-binding domain is present in the conditioned medium.
12731890	3	50	gly	glycosylated	564:575	arg1	sites					606:610	the 11 canonical sites	589:610	the 11 canonical sites	589:610	Our data show that the naturally expressed human EGF receptor is fully glycosylated on eight of the 11 canonical sites; two of the sites are not glycosylated, and one is partially glycosylated, a pattern of site-usage similar but not identical to those reported for the recombinant human EGF receptor heterologously expressed in Chinese hamster ovary cells.
12731890	3	50	gly	glycosylated	564:575	arg1	eight					580:584	eight	580:584	eight	580:584	Our data show that the naturally expressed human EGF receptor is fully glycosylated on eight of the 11 canonical sites; two of the sites are not glycosylated, and one is partially glycosylated, a pattern of site-usage similar but not identical to those reported for the recombinant human EGF receptor heterologously expressed in Chinese hamster ovary cells.
12731890	3	50	gly	glycosylated	564:575	arg1	receptor					546:553	the naturally expressed human EGF receptor	512:553	the naturally expressed human EGF receptor	512:553	Our data show that the naturally expressed human EGF receptor is fully glycosylated on eight of the 11 canonical sites; two of the sites are not glycosylated, and one is partially glycosylated, a pattern of site-usage similar but not identical to those reported for the recombinant human EGF receptor heterologously expressed in Chinese hamster ovary cells.
12731890	3	50	gly	glycosylated	564:575	arg2	eight					580:584	eight	580:584	eight	580:584	Our data show that the naturally expressed human EGF receptor is fully glycosylated on eight of the 11 canonical sites; two of the sites are not glycosylated, and one is partially glycosylated, a pattern of site-usage similar but not identical to those reported for the recombinant human EGF receptor heterologously expressed in Chinese hamster ovary cells.
12731890	3	50	gly	glycosylated	564:575	arg2	sites					606:610	the 11 canonical sites	589:610	the 11 canonical sites	589:610	Our data show that the naturally expressed human EGF receptor is fully glycosylated on eight of the 11 canonical sites; two of the sites are not glycosylated, and one is partially glycosylated, a pattern of site-usage similar but not identical to those reported for the recombinant human EGF receptor heterologously expressed in Chinese hamster ovary cells.
12731890	3	50	gly	glycosylated	564:575	arg2	receptor					546:553	the naturally expressed human EGF receptor	512:553	the naturally expressed human EGF receptor	512:553	Our data show that the naturally expressed human EGF receptor is fully glycosylated on eight of the 11 canonical sites; two of the sites are not glycosylated, and one is partially glycosylated, a pattern of site-usage similar but not identical to those reported for the recombinant human EGF receptor heterologously expressed in Chinese hamster ovary cells.
12731890	2	51	theme	receptor	443:450	arg1	form					431:434	a secreted form	420:434	a secreted form of the receptor	420:450	In this study of the human EGF receptor naturally expressed in A431 cells, the glycosylation sites of the full-length, membrane-bound receptor and of a secreted form of the receptor were characterized by mass spectrometry.
12731890	3	52	theme	sites	606:610	arg1	sites					606:610	the 11 canonical sites	589:610	the 11 canonical sites	589:610	Our data show that the naturally expressed human EGF receptor is fully glycosylated on eight of the 11 canonical sites; two of the sites are not glycosylated, and one is partially glycosylated, a pattern of site-usage similar but not identical to those reported for the recombinant human EGF receptor heterologously expressed in Chinese hamster ovary cells.
12731890	3	52	theme	sites	606:610	arg1	eight					580:584	eight	580:584	eight	580:584	Our data show that the naturally expressed human EGF receptor is fully glycosylated on eight of the 11 canonical sites; two of the sites are not glycosylated, and one is partially glycosylated, a pattern of site-usage similar but not identical to those reported for the recombinant human EGF receptor heterologously expressed in Chinese hamster ovary cells.
12731890	0	53	theme	growth	57:62	arg1	receptor					71:78	the epidermal growth factor receptor	43:78	the epidermal growth factor receptor	43:78	Characterization of glycosylation sites of the epidermal growth factor receptor.
12731890	3	54	theme	identical	727:735	arg1	pattern					689:695	a pattern	687:695	a pattern of site-usage similar but not identical to those reported for the recombinant human EGF receptor heterologously expressed in Chinese hamster ovary cells	687:848	Our data show that the naturally expressed human EGF receptor is fully glycosylated on eight of the 11 canonical sites; two of the sites are not glycosylated, and one is partially glycosylated, a pattern of site-usage similar but not identical to those reported for the recombinant human EGF receptor heterologously expressed in Chinese hamster ovary cells.
12731890	5	55	from	site	1029:1032	arg1	form					1050:1053	the secreted form	1037:1053	the secreted form of the receptor	1037:1069	We show that an additional canonical site in the secreted form of the receptor is fully glycosylated.
12731890	0	56	theme	factor	64:69	arg1	receptor					71:78	the epidermal growth factor receptor	43:78	the epidermal growth factor receptor	43:78	Characterization of glycosylation sites of the epidermal growth factor receptor.
12731890	0	57	gly	glycosylation	20:32	arg2	sites					34:38	glycosylation sites	20:38	glycosylation sites of the epidermal growth factor receptor	20:78	Characterization of glycosylation sites of the epidermal growth factor receptor.
12731890	0	57	gly	glycosylation	20:32	arg1	receptor					71:78	the epidermal growth factor receptor	43:78	the epidermal growth factor receptor	43:78	Characterization of glycosylation sites of the epidermal growth factor receptor.
12731890	0	57	gly	glycosylation	20:32	arg2	receptor					71:78	the epidermal growth factor receptor	43:78	the epidermal growth factor receptor	43:78	Characterization of glycosylation sites of the epidermal growth factor receptor.
12731890	2	58	theme	A431	333:336	arg1	cells					338:342	A431 cells	333:342	A431 cells	333:342	In this study of the human EGF receptor naturally expressed in A431 cells, the glycosylation sites of the full-length, membrane-bound receptor and of a secreted form of the receptor were characterized by mass spectrometry.
12731890	0	59	theme	epidermal	47:55	arg1	receptor					71:78	the epidermal growth factor receptor	43:78	the epidermal growth factor receptor	43:78	Characterization of glycosylation sites of the epidermal growth factor receptor.
12731890	3	60	theme	similar	711:717	arg1	pattern					689:695	a pattern	687:695	a pattern of site-usage similar but not identical to those reported for the recombinant human EGF receptor heterologously expressed in Chinese hamster ovary cells	687:848	Our data show that the naturally expressed human EGF receptor is fully glycosylated on eight of the 11 canonical sites; two of the sites are not glycosylated, and one is partially glycosylated, a pattern of site-usage similar but not identical to those reported for the recombinant human EGF receptor heterologously expressed in Chinese hamster ovary cells.
12731890	7	61	from	present	1508:1514	arg1	medium					1535:1540	the conditioned medium	1519:1540	the conditioned medium	1519:1540	Finally, we provide evidence that in addition to the known secreted form of the receptor, a proteolytic cleavage product of the receptor corresponding to the full extracytoplasmic, ligand-binding domain is present in the conditioned medium.
12731890	3	62	theme	site-usage	700:709	arg1	pattern					689:695	a pattern	687:695	a pattern of site-usage similar but not identical to those reported for the recombinant human EGF receptor heterologously expressed in Chinese hamster ovary cells	687:848	Our data show that the naturally expressed human EGF receptor is fully glycosylated on eight of the 11 canonical sites; two of the sites are not glycosylated, and one is partially glycosylated, a pattern of site-usage similar but not identical to those reported for the recombinant human EGF receptor heterologously expressed in Chinese hamster ovary cells.
12731890	7	63	theme	full	1460:1463	arg1	domain					1498:1503	the full extracytoplasmic, ligand-binding domain	1456:1503	domain	1498:1503	Finally, we provide evidence that in addition to the known secreted form of the receptor, a proteolytic cleavage product of the receptor corresponding to the full extracytoplasmic, ligand-binding domain is present in the conditioned medium.
12731890	3	64	gly	glycosylated	638:649	arg1	two					613:615	two	613:615	two	613:615	Our data show that the naturally expressed human EGF receptor is fully glycosylated on eight of the 11 canonical sites; two of the sites are not glycosylated, and one is partially glycosylated, a pattern of site-usage similar but not identical to those reported for the recombinant human EGF receptor heterologously expressed in Chinese hamster ovary cells.
12731890	3	64	gly	glycosylated	638:649	arg1	sites					624:628	the sites	620:628	the sites	620:628	Our data show that the naturally expressed human EGF receptor is fully glycosylated on eight of the 11 canonical sites; two of the sites are not glycosylated, and one is partially glycosylated, a pattern of site-usage similar but not identical to those reported for the recombinant human EGF receptor heterologously expressed in Chinese hamster ovary cells.
12731890	7	65	theme	receptor	1430:1437	arg1	present					1508:1514	present	1508:1514	present	1508:1514	Finally, we provide evidence that in addition to the known secreted form of the receptor, a proteolytic cleavage product of the receptor corresponding to the full extracytoplasmic, ligand-binding domain is present in the conditioned medium.
12731890	7	65	theme	receptor	1430:1437	arg1	product					1415:1421	a proteolytic cleavage product	1392:1421	a proteolytic cleavage product of the receptor corresponding to the full extracytoplasmic, ligand-binding domain	1392:1503	Finally, we provide evidence that in addition to the known secreted form of the receptor, a proteolytic cleavage product of the receptor corresponding to the full extracytoplasmic, ligand-binding domain is present in the conditioned medium.
12731890	1	66	theme	transmembrane	123:135	arg1	glycoprotein					137:148	a transmembrane glycoprotein	121:148	a transmembrane glycoprotein that mediates the cellular responses to epidermal growth factor (EGF) and transforming growth factor-alpha (TGF-alpha)	121:267	The epidermal growth factor receptor is a transmembrane glycoprotein that mediates the cellular responses to epidermal growth factor (EGF) and transforming growth factor-alpha (TGF-alpha).
12731890	1	66	theme	transmembrane	123:135	arg1	receptor					109:116	The epidermal growth factor receptor	81:116	The epidermal growth factor receptor	81:116	The epidermal growth factor receptor is a transmembrane glycoprotein that mediates the cellular responses to epidermal growth factor (EGF) and transforming growth factor-alpha (TGF-alpha).
12731890	2	67	theme	human	291:295	arg1	receptor					301:308	the human EGF receptor	287:308	the human EGF receptor naturally expressed in A431 cells	287:342	In this study of the human EGF receptor naturally expressed in A431 cells, the glycosylation sites of the full-length, membrane-bound receptor and of a secreted form of the receptor were characterized by mass spectrometry.
12731890	3	68	theme	canonical	596:604	arg1	sites					606:610	the 11 canonical sites	589:610	the 11 canonical sites	589:610	Our data show that the naturally expressed human EGF receptor is fully glycosylated on eight of the 11 canonical sites; two of the sites are not glycosylated, and one is partially glycosylated, a pattern of site-usage similar but not identical to those reported for the recombinant human EGF receptor heterologously expressed in Chinese hamster ovary cells.
12731890	1	69	theme	transforming	224:235	arg1	TGF-alpha					258:266	TGF-alpha	258:266	TGF-alpha	258:266	The epidermal growth factor receptor is a transmembrane glycoprotein that mediates the cellular responses to epidermal growth factor (EGF) and transforming growth factor-alpha (TGF-alpha).
12731890	1	69	theme	transforming	224:235	arg1	factor-alpha					244:255	transforming growth factor-alpha	224:255	transforming growth factor-alpha (TGF-alpha)	224:267	The epidermal growth factor receptor is a transmembrane glycoprotein that mediates the cellular responses to epidermal growth factor (EGF) and transforming growth factor-alpha (TGF-alpha).
12731890	0	70	theme	receptor	71:78	arg1	sites					34:38	glycosylation sites	20:38	glycosylation sites of the epidermal growth factor receptor	20:78	Characterization of glycosylation sites of the epidermal growth factor receptor.
12731890	0	70	theme	receptor	71:78	arg1	receptor					71:78	the epidermal growth factor receptor	43:78	the epidermal growth factor receptor	43:78	Characterization of glycosylation sites of the epidermal growth factor receptor.
12731890	3	71	theme	sites	624:628	arg1	two					613:615	two	613:615	two	613:615	Our data show that the naturally expressed human EGF receptor is fully glycosylated on eight of the 11 canonical sites; two of the sites are not glycosylated, and one is partially glycosylated, a pattern of site-usage similar but not identical to those reported for the recombinant human EGF receptor heterologously expressed in Chinese hamster ovary cells.
12731890	3	71	theme	sites	624:628	arg1	sites					624:628	the sites	620:628	the sites	620:628	Our data show that the naturally expressed human EGF receptor is fully glycosylated on eight of the 11 canonical sites; two of the sites are not glycosylated, and one is partially glycosylated, a pattern of site-usage similar but not identical to those reported for the recombinant human EGF receptor heterologously expressed in Chinese hamster ovary cells.
12731890	2	72	dep	full-length	376:386	arg1	membrane-bound					389:402	membrane-bound	389:402	membrane-bound	389:402	In this study of the human EGF receptor naturally expressed in A431 cells, the glycosylation sites of the full-length, membrane-bound receptor and of a secreted form of the receptor were characterized by mass spectrometry.
12731890	5	73	gly	glycosylated	1080:1091	arg1	site					1029:1032	an additional canonical site	1005:1032	an additional canonical site in the secreted form of the receptor	1005:1069	We show that an additional canonical site in the secreted form of the receptor is fully glycosylated.
12731890	2	74	theme	glycosylation	349:361	arg1	sites					363:367	the glycosylation sites	345:367	the glycosylation sites of the full-length, membrane-bound receptor and of a secreted form of the receptor	345:450	In this study of the human EGF receptor naturally expressed in A431 cells, the glycosylation sites of the full-length, membrane-bound receptor and of a secreted form of the receptor were characterized by mass spectrometry.
12731890	2	74	theme	glycosylation	349:361	arg1	form					431:434	a secreted form	420:434	a secreted form of the receptor	420:450	In this study of the human EGF receptor naturally expressed in A431 cells, the glycosylation sites of the full-length, membrane-bound receptor and of a secreted form of the receptor were characterized by mass spectrometry.
12731890	2	74	theme	glycosylation	349:361	arg1	receptor					404:411	the full-length, membrane-bound receptor	372:411	the full-length, membrane-bound receptor	372:411	In this study of the human EGF receptor naturally expressed in A431 cells, the glycosylation sites of the full-length, membrane-bound receptor and of a secreted form of the receptor were characterized by mass spectrometry.
12731890	1	75	theme	growth	237:242	arg1	TGF-alpha					258:266	TGF-alpha	258:266	TGF-alpha	258:266	The epidermal growth factor receptor is a transmembrane glycoprotein that mediates the cellular responses to epidermal growth factor (EGF) and transforming growth factor-alpha (TGF-alpha).
12731890	1	75	theme	growth	237:242	arg1	factor-alpha					244:255	transforming growth factor-alpha	224:255	transforming growth factor-alpha (TGF-alpha)	224:267	The epidermal growth factor receptor is a transmembrane glycoprotein that mediates the cellular responses to epidermal growth factor (EGF) and transforming growth factor-alpha (TGF-alpha).
12731890	2	76	theme	mass	474:477	arg1	spectrometry					479:490	mass spectrometry	474:490	mass spectrometry	474:490	In this study of the human EGF receptor naturally expressed in A431 cells, the glycosylation sites of the full-length, membrane-bound receptor and of a secreted form of the receptor were characterized by mass spectrometry.
12731890	7	77	theme	proteolytic	1394:1404	arg1	present					1508:1514	present	1508:1514	present	1508:1514	Finally, we provide evidence that in addition to the known secreted form of the receptor, a proteolytic cleavage product of the receptor corresponding to the full extracytoplasmic, ligand-binding domain is present in the conditioned medium.
12731890	7	77	theme	proteolytic	1394:1404	arg1	product					1415:1421	a proteolytic cleavage product	1392:1421	a proteolytic cleavage product of the receptor corresponding to the full extracytoplasmic, ligand-binding domain	1392:1503	Finally, we provide evidence that in addition to the known secreted form of the receptor, a proteolytic cleavage product of the receptor corresponding to the full extracytoplasmic, ligand-binding domain is present in the conditioned medium.
12731890	0	78	theme	glycosylation	20:32	arg1	sites					34:38	glycosylation sites	20:38	glycosylation sites of the epidermal growth factor receptor	20:78	Characterization of glycosylation sites of the epidermal growth factor receptor.
12731890	0	78	theme	glycosylation	20:32	arg1	receptor					71:78	the epidermal growth factor receptor	43:78	the epidermal growth factor receptor	43:78	Characterization of glycosylation sites of the epidermal growth factor receptor.
12731890	4	79	theme	ovary	979:983	arg1	cells					985:989	Chinese hamster ovary cells	963:989	Chinese hamster ovary cells	963:989	We also confirm the partial glycosylation of an atypical NNC site first identified in the receptor expressed in Chinese hamster ovary cells.
12731890	3	80	theme	ovary	838:842	arg1	cells					844:848	Chinese hamster ovary cells	822:848	Chinese hamster ovary cells	822:848	Our data show that the naturally expressed human EGF receptor is fully glycosylated on eight of the 11 canonical sites; two of the sites are not glycosylated, and one is partially glycosylated, a pattern of site-usage similar but not identical to those reported for the recombinant human EGF receptor heterologously expressed in Chinese hamster ovary cells.
20805301	5	0	theme	HEK	797:799	arg1	cells					805:809	HEK 293 cells	797:809	HEK 293 cells	797:809	Bioinformatic analysis identified Asn177 as the only possible glycosylation site of CYP2W1, which was supported by the inability of an N177A mutant to be glycosylated in HEK 293 cells.
20805301	6	1	theme	available	1040:1048	arg1	CYP2W1					1033:1038	a topology making CYP2W1	1015:1038	a topology making CYP2W1 available to the ER glycosylation machinery	1015:1082	Analysis of the membrane topology indicated that unlike other cytochromes P450, CYP2W1 in HEK 293-transfected cells and in nontransfected Caco2TC7 and HepG2 cells is oriented toward the lumen of the ER, a topology making CYP2W1 available to the ER glycosylation machinery.
20805301	6	1	theme	available	1040:1048	arg1	lumen					998:1002	the lumen	994:1002	the lumen of the ER	994:1012	Analysis of the membrane topology indicated that unlike other cytochromes P450, CYP2W1 in HEK 293-transfected cells and in nontransfected Caco2TC7 and HepG2 cells is oriented toward the lumen of the ER, a topology making CYP2W1 available to the ER glycosylation machinery.
20805301	4	2	theme	cells	556:560	arg1	analysis					448:455	The analysis	444:455	The analysis of colorectal normal and cancer tissues and CYP2W1 overexpressing human embryonic kidney (HEK) 293 cells	444:560	The analysis of colorectal normal and cancer tissues and CYP2W1 overexpressing human embryonic kidney (HEK) 293 cells showed that a fraction of CYP2W1 is modified by N-glycosylation.
20805301	5	3	theme	Bioinformatic	627:639	arg1	analysis					641:648	Bioinformatic analysis	627:648	Bioinformatic analysis	627:648	Bioinformatic analysis identified Asn177 as the only possible glycosylation site of CYP2W1, which was supported by the inability of an N177A mutant to be glycosylated in HEK 293 cells.
20805301	6	4	theme	other	868:872	arg1	P450					886:889	other cytochromes P450	868:889	other cytochromes P450	868:889	Analysis of the membrane topology indicated that unlike other cytochromes P450, CYP2W1 in HEK 293-transfected cells and in nontransfected Caco2TC7 and HepG2 cells is oriented toward the lumen of the ER, a topology making CYP2W1 available to the ER glycosylation machinery.
20805301	7	5	theme	cell	1205:1208	arg1	surface					1210:1216	the cell surface	1201:1216	the cell surface	1201:1216	Immunofluorescence microscopy and cell surface biotinylation experiments revealed approximately 8% of the CYP2W1 on the cell surface.
20805301	2	6	theme	tumor	249:253	arg1	expression					255:264	a higher tumor expression	240:264	a higher tumor expression	240:264	Moreover, we have shown previously that a higher tumor expression is associated with less survival.
20805301	6	7	theme	topology	837:844	arg1	Analysis					812:819	Analysis	812:819	Analysis of the membrane topology	812:844	Analysis of the membrane topology indicated that unlike other cytochromes P450, CYP2W1 in HEK 293-transfected cells and in nontransfected Caco2TC7 and HepG2 cells is oriented toward the lumen of the ER, a topology making CYP2W1 available to the ER glycosylation machinery.
20805301	1	8	theme	colorectal	175:184	arg1	cells					193:197	colorectal cancer cells	175:197	colorectal cancer cells	175:197	Cytochrome P450 2W1 (CYP2W1) is expressed at high levels in colorectal cancer cells.
20805301	8	9	theme	reverse	1231:1237	arg1	orientation					1239:1249	the reverse orientation	1227:1249	the reverse orientation of CYP2W1 in the ER membrane	1227:1278	Despite the reverse orientation of CYP2W1 in the ER membrane, apparently making functional interactions with NADPH-cytochrome P450 reductase impossible, CYP2W1 in HEK 293 cells was active in the metabolism of indoline substrates and was able to activate aflatoxin B1 into cytotoxic products.
20805301	5	10	theme	glycosylation	689:701	arg1	Asn177					661:666	Asn177	661:666	Asn177	661:666	Bioinformatic analysis identified Asn177 as the only possible glycosylation site of CYP2W1, which was supported by the inability of an N177A mutant to be glycosylated in HEK 293 cells.
20805301	5	10	theme	glycosylation	689:701	arg1	site					703:706	the only possible glycosylation site	671:706	the only possible glycosylation site	671:706	Bioinformatic analysis identified Asn177 as the only possible glycosylation site of CYP2W1, which was supported by the inability of an N177A mutant to be glycosylated in HEK 293 cells.
20805301	5	10	theme	glycosylation	689:701	arg1	CYP2W1					711:716	CYP2W1	711:716	CYP2W1	711:716	Bioinformatic analysis identified Asn177 as the only possible glycosylation site of CYP2W1, which was supported by the inability of an N177A mutant to be glycosylated in HEK 293 cells.
20805301	6	11	theme	HEK	902:904	arg1	cells					922:926	HEK 293-transfected cells	902:926	HEK 293-transfected cells	902:926	Analysis of the membrane topology indicated that unlike other cytochromes P450, CYP2W1 in HEK 293-transfected cells and in nontransfected Caco2TC7 and HepG2 cells is oriented toward the lumen of the ER, a topology making CYP2W1 available to the ER glycosylation machinery.
20805301	5	12	gly	glycosylation	689:701	arg2	Asn177					661:666	Asn177	661:666	Asn177	661:666	Bioinformatic analysis identified Asn177 as the only possible glycosylation site of CYP2W1, which was supported by the inability of an N177A mutant to be glycosylated in HEK 293 cells.
20805301	5	12	gly	glycosylation	689:701	arg1	CYP2W1					711:716	CYP2W1	711:716	CYP2W1	711:716	Bioinformatic analysis identified Asn177 as the only possible glycosylation site of CYP2W1, which was supported by the inability of an N177A mutant to be glycosylated in HEK 293 cells.
20805301	5	12	gly	glycosylation	689:701	arg2	site					703:706	the only possible glycosylation site	671:706	the only possible glycosylation site	671:706	Bioinformatic analysis identified Asn177 as the only possible glycosylation site of CYP2W1, which was supported by the inability of an N177A mutant to be glycosylated in HEK 293 cells.
20805301	5	12	gly	glycosylation	689:701	arg2	CYP2W1					711:716	CYP2W1	711:716	CYP2W1	711:716	Bioinformatic analysis identified Asn177 as the only possible glycosylation site of CYP2W1, which was supported by the inability of an N177A mutant to be glycosylated in HEK 293 cells.
20805301	10	13	theme	colon	1747:1751	arg1	cancer					1753:1758	colon cancer	1747:1758	colon cancer	1747:1758	Together, these results suggest the possibility of using CYP2W1 as a drug target in the treatment of colon cancer using antibodies and/or specific CYP2W1 activated prodrugs.
20805301	8	14	theme	substrates	1437:1446	arg1	metabolism					1414:1423	the metabolism	1410:1423	the metabolism of indoline substrates	1410:1446	Despite the reverse orientation of CYP2W1 in the ER membrane, apparently making functional interactions with NADPH-cytochrome P450 reductase impossible, CYP2W1 in HEK 293 cells was active in the metabolism of indoline substrates and was able to activate aflatoxin B1 into cytotoxic products.
20805301	8	15	theme	ER	1268:1269	arg1	membrane					1271:1278	the ER membrane	1264:1278	the ER membrane	1264:1278	Despite the reverse orientation of CYP2W1 in the ER membrane, apparently making functional interactions with NADPH-cytochrome P450 reductase impossible, CYP2W1 in HEK 293 cells was active in the metabolism of indoline substrates and was able to activate aflatoxin B1 into cytotoxic products.
20805301	5	16	theme	only	675:678	arg1	Asn177					661:666	Asn177	661:666	Asn177	661:666	Bioinformatic analysis identified Asn177 as the only possible glycosylation site of CYP2W1, which was supported by the inability of an N177A mutant to be glycosylated in HEK 293 cells.
20805301	5	16	theme	only	675:678	arg1	site					703:706	the only possible glycosylation site	671:706	the only possible glycosylation site	671:706	Bioinformatic analysis identified Asn177 as the only possible glycosylation site of CYP2W1, which was supported by the inability of an N177A mutant to be glycosylated in HEK 293 cells.
20805301	5	16	theme	only	675:678	arg1	CYP2W1					711:716	CYP2W1	711:716	CYP2W1	711:716	Bioinformatic analysis identified Asn177 as the only possible glycosylation site of CYP2W1, which was supported by the inability of an N177A mutant to be glycosylated in HEK 293 cells.
20805301	10	17	theme	CYP2W1	1793:1798	arg1	prodrugs					1810:1817	specific CYP2W1 activated prodrugs	1784:1817	specific CYP2W1 activated prodrugs	1784:1817	Together, these results suggest the possibility of using CYP2W1 as a drug target in the treatment of colon cancer using antibodies and/or specific CYP2W1 activated prodrugs.
20805301	8	18	with	interactions	1310:1321	arg1	reductase					1350:1358	NADPH-cytochrome P450 reductase impossible	1328:1369	NADPH-cytochrome P450 reductase impossible	1328:1369	Despite the reverse orientation of CYP2W1 in the ER membrane, apparently making functional interactions with NADPH-cytochrome P450 reductase impossible, CYP2W1 in HEK 293 cells was active in the metabolism of indoline substrates and was able to activate aflatoxin B1 into cytotoxic products.
20805301	7	19	theme	CYP2W1	1191:1196	arg1	%					1182:1182	approximately 8%	1167:1182	approximately 8% of the CYP2W1	1167:1196	Immunofluorescence microscopy and cell surface biotinylation experiments revealed approximately 8% of the CYP2W1 on the cell surface.
20805301	7	19	theme	CYP2W1	1191:1196	arg1	CYP2W1					1191:1196	the CYP2W1	1187:1196	the CYP2W1	1187:1196	Immunofluorescence microscopy and cell surface biotinylation experiments revealed approximately 8% of the CYP2W1 on the cell surface.
20805301	4	20	dep	overexpressing	508:521	arg1	CYP2W1					501:506	CYP2W1	501:506	CYP2W1	501:506	The analysis of colorectal normal and cancer tissues and CYP2W1 overexpressing human embryonic kidney (HEK) 293 cells showed that a fraction of CYP2W1 is modified by N-glycosylation.
20805301	6	21	theme	HepG2	963:967	arg1	cells					969:973	nontransfected Caco2TC7 and HepG2 cells	935:973	cells	969:973	Analysis of the membrane topology indicated that unlike other cytochromes P450, CYP2W1 in HEK 293-transfected cells and in nontransfected Caco2TC7 and HepG2 cells is oriented toward the lumen of the ER, a topology making CYP2W1 available to the ER glycosylation machinery.
20805301	3	22	theme	post-translational	331:348	arg1	modification					350:361	post-translational modification	331:361	post-translational modification	331:361	In this study, we characterize post-translational modification, inverted endoplasmic reticulum (ER) topology, and catalytic activity of CYP2W1.
20805301	8	23	theme	aflatoxin	1473:1481	arg1	B1					1483:1484	aflatoxin B1	1473:1484	aflatoxin B1 into cytotoxic products	1473:1508	Despite the reverse orientation of CYP2W1 in the ER membrane, apparently making functional interactions with NADPH-cytochrome P450 reductase impossible, CYP2W1 in HEK 293 cells was active in the metabolism of indoline substrates and was able to activate aflatoxin B1 into cytotoxic products.
20805301	0	24	theme	catalytic	95:103	arg1	activity					105:112	catalytic activity	95:112	catalytic activity	95:112	Colorectal cancer-specific cytochrome P450 2W1: intracellular localization, glycosylation, and catalytic activity.
20805301	10	25	theme	drug	1715:1718	arg1	target					1720:1725	a drug target	1713:1725	a drug target	1713:1725	Together, these results suggest the possibility of using CYP2W1 as a drug target in the treatment of colon cancer using antibodies and/or specific CYP2W1 activated prodrugs.
20805301	10	25	theme	drug	1715:1718	arg1	CYP2W1					1703:1708	CYP2W1	1703:1708	CYP2W1	1703:1708	Together, these results suggest the possibility of using CYP2W1 as a drug target in the treatment of colon cancer using antibodies and/or specific CYP2W1 activated prodrugs.
20805301	8	26	theme	NADPH-cytochrome	1328:1343	arg1	reductase					1350:1358	NADPH-cytochrome P450 reductase impossible	1328:1369	NADPH-cytochrome P450 reductase impossible	1328:1369	Despite the reverse orientation of CYP2W1 in the ER membrane, apparently making functional interactions with NADPH-cytochrome P450 reductase impossible, CYP2W1 in HEK 293 cells was active in the metabolism of indoline substrates and was able to activate aflatoxin B1 into cytotoxic products.
20805301	3	27	theme	catalytic	414:422	arg1	activity					424:431	catalytic activity	414:431	catalytic activity of CYP2W1	414:441	In this study, we characterize post-translational modification, inverted endoplasmic reticulum (ER) topology, and catalytic activity of CYP2W1.
20805301	6	28	theme	topology	1017:1024	arg1	CYP2W1					1033:1038	a topology making CYP2W1	1015:1038	a topology making CYP2W1 available to the ER glycosylation machinery	1015:1082	Analysis of the membrane topology indicated that unlike other cytochromes P450, CYP2W1 in HEK 293-transfected cells and in nontransfected Caco2TC7 and HepG2 cells is oriented toward the lumen of the ER, a topology making CYP2W1 available to the ER glycosylation machinery.
20805301	6	28	theme	topology	1017:1024	arg1	lumen					998:1002	the lumen	994:1002	the lumen of the ER	994:1012	Analysis of the membrane topology indicated that unlike other cytochromes P450, CYP2W1 in HEK 293-transfected cells and in nontransfected Caco2TC7 and HepG2 cells is oriented toward the lumen of the ER, a topology making CYP2W1 available to the ER glycosylation machinery.
20805301	3	29	theme	endoplasmic	373:383	arg1	ER					396:397	ER	396:397	ER	396:397	In this study, we characterize post-translational modification, inverted endoplasmic reticulum (ER) topology, and catalytic activity of CYP2W1.
20805301	3	29	theme	endoplasmic	373:383	arg1	reticulum					385:393	endoplasmic reticulum	373:393	inverted endoplasmic reticulum (ER) topology	364:407	In this study, we characterize post-translational modification, inverted endoplasmic reticulum (ER) topology, and catalytic activity of CYP2W1.
20805301	4	30	theme	colorectal	460:469	arg1	tissues					489:495	cancer tissues	482:495	cancer tissues	482:495	The analysis of colorectal normal and cancer tissues and CYP2W1 overexpressing human embryonic kidney (HEK) 293 cells showed that a fraction of CYP2W1 is modified by N-glycosylation.
20805301	0	31	theme	Colorectal	0:9	arg1	P450					38:41	Colorectal cancer-specific cytochrome P450 2W1	0:45	Colorectal cancer-specific cytochrome P450 2W1	0:45	Colorectal cancer-specific cytochrome P450 2W1: intracellular localization, glycosylation, and catalytic activity.
20805301	9	32	theme	first	1540:1544	arg1	time					1546:1549	the first time	1536:1549	the first time	1536:1549	The study identifies for the first time a cytochrome P450 enzyme with a luminal ER orientation and still retaining catalytic activity.
20805301	4	33	theme	kidney	539:544	arg1	cells					556:560	CYP2W1 overexpressing human embryonic kidney (HEK) 293 cells	501:560	CYP2W1 overexpressing human embryonic kidney (HEK) 293 cells	501:560	The analysis of colorectal normal and cancer tissues and CYP2W1 overexpressing human embryonic kidney (HEK) 293 cells showed that a fraction of CYP2W1 is modified by N-glycosylation.
20805301	0	34	dep	localization	62:73	arg1	P450					38:41	Colorectal cancer-specific cytochrome P450 2W1	0:45	Colorectal cancer-specific cytochrome P450 2W1	0:45	Colorectal cancer-specific cytochrome P450 2W1: intracellular localization, glycosylation, and catalytic activity.
20805301	0	35	theme	cytochrome	27:36	arg1	P450					38:41	Colorectal cancer-specific cytochrome P450 2W1	0:45	Colorectal cancer-specific cytochrome P450 2W1	0:45	Colorectal cancer-specific cytochrome P450 2W1: intracellular localization, glycosylation, and catalytic activity.
20805301	6	36	theme	membrane	828:835	arg1	topology					837:844	the membrane topology	824:844	the membrane topology	824:844	Analysis of the membrane topology indicated that unlike other cytochromes P450, CYP2W1 in HEK 293-transfected cells and in nontransfected Caco2TC7 and HepG2 cells is oriented toward the lumen of the ER, a topology making CYP2W1 available to the ER glycosylation machinery.
20805301	1	37	theme	Cytochrome	115:124	arg1	P450					126:129	Cytochrome P450 2W1	115:133	Cytochrome P450 2W1 (CYP2W1)	115:142	Cytochrome P450 2W1 (CYP2W1) is expressed at high levels in colorectal cancer cells.
20805301	1	37	theme	Cytochrome	115:124	arg1	CYP2W1					136:141	CYP2W1	136:141	CYP2W1	136:141	Cytochrome P450 2W1 (CYP2W1) is expressed at high levels in colorectal cancer cells.
20805301	7	38	theme	cell	1119:1122	arg1	biotinylation					1132:1144	cell surface biotinylation	1119:1144	cell surface biotinylation	1119:1144	Immunofluorescence microscopy and cell surface biotinylation experiments revealed approximately 8% of the CYP2W1 on the cell surface.
20805301	9	39	theme	P450	1564:1567	arg1	enzyme					1569:1574	a cytochrome P450 enzyme	1551:1574	a cytochrome P450 enzyme with a luminal ER orientation	1551:1604	The study identifies for the first time a cytochrome P450 enzyme with a luminal ER orientation and still retaining catalytic activity.
20805301	5	40	theme	mutant	768:773	arg1	inability					746:754	the inability	742:754	the inability of an N177A mutant to be glycosylated in HEK 293 cells	742:809	Bioinformatic analysis identified Asn177 as the only possible glycosylation site of CYP2W1, which was supported by the inability of an N177A mutant to be glycosylated in HEK 293 cells.
20805301	10	41	theme	activated	1800:1808	arg1	prodrugs					1810:1817	specific CYP2W1 activated prodrugs	1784:1817	specific CYP2W1 activated prodrugs	1784:1817	Together, these results suggest the possibility of using CYP2W1 as a drug target in the treatment of colon cancer using antibodies and/or specific CYP2W1 activated prodrugs.
20805301	4	42	theme	human	523:527	arg1	HEK					547:549	HEK	547:549	HEK	547:549	The analysis of colorectal normal and cancer tissues and CYP2W1 overexpressing human embryonic kidney (HEK) 293 cells showed that a fraction of CYP2W1 is modified by N-glycosylation.
20805301	4	42	theme	human	523:527	arg1	kidney					539:544	human embryonic kidney	523:544	CYP2W1 overexpressing human embryonic kidney (HEK) 293 cells	501:560	The analysis of colorectal normal and cancer tissues and CYP2W1 overexpressing human embryonic kidney (HEK) 293 cells showed that a fraction of CYP2W1 is modified by N-glycosylation.
20805301	9	43	theme	luminal	1583:1589	arg1	orientation					1594:1604	a luminal ER orientation	1581:1604	a luminal ER orientation	1581:1604	The study identifies for the first time a cytochrome P450 enzyme with a luminal ER orientation and still retaining catalytic activity.
20805301	6	44	theme	ER	1057:1058	arg1	machinery					1074:1082	the ER glycosylation machinery	1053:1082	the ER glycosylation machinery	1053:1082	Analysis of the membrane topology indicated that unlike other cytochromes P450, CYP2W1 in HEK 293-transfected cells and in nontransfected Caco2TC7 and HepG2 cells is oriented toward the lumen of the ER, a topology making CYP2W1 available to the ER glycosylation machinery.
20805301	7	45	theme	Immunofluorescence	1085:1102	arg1	microscopy					1104:1113	Immunofluorescence microscopy	1085:1113	Immunofluorescence microscopy	1085:1113	Immunofluorescence microscopy and cell surface biotinylation experiments revealed approximately 8% of the CYP2W1 on the cell surface.
20805301	6	46	theme	cytochromes	874:884	arg1	P450					886:889	other cytochromes P450	868:889	other cytochromes P450	868:889	Analysis of the membrane topology indicated that unlike other cytochromes P450, CYP2W1 in HEK 293-transfected cells and in nontransfected Caco2TC7 and HepG2 cells is oriented toward the lumen of the ER, a topology making CYP2W1 available to the ER glycosylation machinery.
20805301	9	47	with	enzyme	1569:1574	arg1	orientation					1594:1604	a luminal ER orientation	1581:1604	a luminal ER orientation	1581:1604	The study identifies for the first time a cytochrome P450 enzyme with a luminal ER orientation and still retaining catalytic activity.
20805301	9	48	theme	catalytic	1626:1634	arg1	activity					1636:1643	catalytic activity	1626:1643	catalytic activity	1626:1643	The study identifies for the first time a cytochrome P450 enzyme with a luminal ER orientation and still retaining catalytic activity.
20805301	8	49	from	CYP2W1	1372:1377	arg1	cells					1390:1394	HEK 293 cells	1382:1394	HEK 293 cells	1382:1394	Despite the reverse orientation of CYP2W1 in the ER membrane, apparently making functional interactions with NADPH-cytochrome P450 reductase impossible, CYP2W1 in HEK 293 cells was active in the metabolism of indoline substrates and was able to activate aflatoxin B1 into cytotoxic products.
20805301	1	50	theme	high	160:163	arg1	levels					165:170	high levels	160:170	high levels	160:170	Cytochrome P450 2W1 (CYP2W1) is expressed at high levels in colorectal cancer cells.
20805301	0	51	theme	intracellular	48:60	arg1	localization					62:73	intracellular localization	48:73	intracellular localization	48:73	Colorectal cancer-specific cytochrome P450 2W1: intracellular localization, glycosylation, and catalytic activity.
20805301	4	52	mod	modified	598:605	arg1	fraction					576:583	a fraction	574:583	a fraction of CYP2W1	574:593	The analysis of colorectal normal and cancer tissues and CYP2W1 overexpressing human embryonic kidney (HEK) 293 cells showed that a fraction of CYP2W1 is modified by N-glycosylation.
20805301	4	52	mod	modified	598:605	arg3	N-glycosylation					610:624	N-glycosylation	610:624	N-glycosylation	610:624	The analysis of colorectal normal and cancer tissues and CYP2W1 overexpressing human embryonic kidney (HEK) 293 cells showed that a fraction of CYP2W1 is modified by N-glycosylation.
20805301	6	53	theme	nontransfected	935:948	arg1	Caco2TC7					950:957	nontransfected Caco2TC7 and HepG2 cells	935:973	Caco2TC7	950:957	Analysis of the membrane topology indicated that unlike other cytochromes P450, CYP2W1 in HEK 293-transfected cells and in nontransfected Caco2TC7 and HepG2 cells is oriented toward the lumen of the ER, a topology making CYP2W1 available to the ER glycosylation machinery.
20805301	5	54	theme	possible	680:687	arg1	Asn177					661:666	Asn177	661:666	Asn177	661:666	Bioinformatic analysis identified Asn177 as the only possible glycosylation site of CYP2W1, which was supported by the inability of an N177A mutant to be glycosylated in HEK 293 cells.
20805301	5	54	theme	possible	680:687	arg1	site					703:706	the only possible glycosylation site	671:706	the only possible glycosylation site	671:706	Bioinformatic analysis identified Asn177 as the only possible glycosylation site of CYP2W1, which was supported by the inability of an N177A mutant to be glycosylated in HEK 293 cells.
20805301	5	54	theme	possible	680:687	arg1	CYP2W1					711:716	CYP2W1	711:716	CYP2W1	711:716	Bioinformatic analysis identified Asn177 as the only possible glycosylation site of CYP2W1, which was supported by the inability of an N177A mutant to be glycosylated in HEK 293 cells.
20805301	5	55	gly	glycosylated	781:792	arg1	inability					746:754	the inability	742:754	the inability of an N177A mutant to be glycosylated in HEK 293 cells	742:809	Bioinformatic analysis identified Asn177 as the only possible glycosylation site of CYP2W1, which was supported by the inability of an N177A mutant to be glycosylated in HEK 293 cells.
20805301	2	56	theme	less	285:288	arg1	survival					290:297	less survival	285:297	less survival	285:297	Moreover, we have shown previously that a higher tumor expression is associated with less survival.
20805301	8	57	from	active	1400:1405	arg1	metabolism					1414:1423	the metabolism	1410:1423	the metabolism of indoline substrates	1410:1446	Despite the reverse orientation of CYP2W1 in the ER membrane, apparently making functional interactions with NADPH-cytochrome P450 reductase impossible, CYP2W1 in HEK 293 cells was active in the metabolism of indoline substrates and was able to activate aflatoxin B1 into cytotoxic products.
20805301	1	58	theme	cancer	186:191	arg1	cells					193:197	colorectal cancer cells	175:197	colorectal cancer cells	175:197	Cytochrome P450 2W1 (CYP2W1) is expressed at high levels in colorectal cancer cells.
20805301	6	59	theme	293-transfected	906:920	arg1	cells					922:926	HEK 293-transfected cells	902:926	HEK 293-transfected cells	902:926	Analysis of the membrane topology indicated that unlike other cytochromes P450, CYP2W1 in HEK 293-transfected cells and in nontransfected Caco2TC7 and HepG2 cells is oriented toward the lumen of the ER, a topology making CYP2W1 available to the ER glycosylation machinery.
20805301	8	60	theme	indoline	1428:1435	arg1	substrates					1437:1446	indoline substrates	1428:1446	indoline substrates	1428:1446	Despite the reverse orientation of CYP2W1 in the ER membrane, apparently making functional interactions with NADPH-cytochrome P450 reductase impossible, CYP2W1 in HEK 293 cells was active in the metabolism of indoline substrates and was able to activate aflatoxin B1 into cytotoxic products.
20805301	10	61	theme	cancer	1753:1758	arg1	treatment					1734:1742	the treatment	1730:1742	the treatment of colon cancer	1730:1758	Together, these results suggest the possibility of using CYP2W1 as a drug target in the treatment of colon cancer using antibodies and/or specific CYP2W1 activated prodrugs.
20805301	4	62	theme	tissues	489:495	arg1	analysis					448:455	The analysis	444:455	The analysis of colorectal normal and cancer tissues and CYP2W1 overexpressing human embryonic kidney (HEK) 293 cells	444:560	The analysis of colorectal normal and cancer tissues and CYP2W1 overexpressing human embryonic kidney (HEK) 293 cells showed that a fraction of CYP2W1 is modified by N-glycosylation.
20805301	8	63	theme	CYP2W1	1254:1259	arg1	orientation					1239:1249	the reverse orientation	1227:1249	the reverse orientation of CYP2W1 in the ER membrane	1227:1278	Despite the reverse orientation of CYP2W1 in the ER membrane, apparently making functional interactions with NADPH-cytochrome P450 reductase impossible, CYP2W1 in HEK 293 cells was active in the metabolism of indoline substrates and was able to activate aflatoxin B1 into cytotoxic products.
20805301	2	64	theme	higher	242:247	arg1	expression					255:264	a higher tumor expression	240:264	a higher tumor expression	240:264	Moreover, we have shown previously that a higher tumor expression is associated with less survival.
20805301	10	65	theme	specific	1784:1791	arg1	prodrugs					1810:1817	specific CYP2W1 activated prodrugs	1784:1817	specific CYP2W1 activated prodrugs	1784:1817	Together, these results suggest the possibility of using CYP2W1 as a drug target in the treatment of colon cancer using antibodies and/or specific CYP2W1 activated prodrugs.
20805301	8	66	from	orientation	1239:1249	arg1	membrane					1271:1278	the ER membrane	1264:1278	the ER membrane	1264:1278	Despite the reverse orientation of CYP2W1 in the ER membrane, apparently making functional interactions with NADPH-cytochrome P450 reductase impossible, CYP2W1 in HEK 293 cells was active in the metabolism of indoline substrates and was able to activate aflatoxin B1 into cytotoxic products.
20805301	4	67	theme	cancer	482:487	arg1	tissues					489:495	cancer tissues	482:495	cancer tissues	482:495	The analysis of colorectal normal and cancer tissues and CYP2W1 overexpressing human embryonic kidney (HEK) 293 cells showed that a fraction of CYP2W1 is modified by N-glycosylation.
20805301	8	68	from	metabolism	1414:1423	arg1	active					1400:1405	active	1400:1405	active	1400:1405	Despite the reverse orientation of CYP2W1 in the ER membrane, apparently making functional interactions with NADPH-cytochrome P450 reductase impossible, CYP2W1 in HEK 293 cells was active in the metabolism of indoline substrates and was able to activate aflatoxin B1 into cytotoxic products.
20805301	5	69	theme	CYP2W1	711:716	arg1	Asn177					661:666	Asn177	661:666	Asn177	661:666	Bioinformatic analysis identified Asn177 as the only possible glycosylation site of CYP2W1, which was supported by the inability of an N177A mutant to be glycosylated in HEK 293 cells.
20805301	5	69	theme	CYP2W1	711:716	arg1	site					703:706	the only possible glycosylation site	671:706	the only possible glycosylation site	671:706	Bioinformatic analysis identified Asn177 as the only possible glycosylation site of CYP2W1, which was supported by the inability of an N177A mutant to be glycosylated in HEK 293 cells.
20805301	5	69	theme	CYP2W1	711:716	arg1	CYP2W1					711:716	CYP2W1	711:716	CYP2W1	711:716	Bioinformatic analysis identified Asn177 as the only possible glycosylation site of CYP2W1, which was supported by the inability of an N177A mutant to be glycosylated in HEK 293 cells.
20805301	8	70	theme	cytotoxic	1491:1499	arg1	products					1501:1508	cytotoxic products	1491:1508	cytotoxic products	1491:1508	Despite the reverse orientation of CYP2W1 in the ER membrane, apparently making functional interactions with NADPH-cytochrome P450 reductase impossible, CYP2W1 in HEK 293 cells was active in the metabolism of indoline substrates and was able to activate aflatoxin B1 into cytotoxic products.
20805301	8	71	theme	functional	1299:1308	arg1	interactions					1310:1321	functional interactions	1299:1321	functional interactions with NADPH-cytochrome P450 reductase impossible	1299:1369	Despite the reverse orientation of CYP2W1 in the ER membrane, apparently making functional interactions with NADPH-cytochrome P450 reductase impossible, CYP2W1 in HEK 293 cells was active in the metabolism of indoline substrates and was able to activate aflatoxin B1 into cytotoxic products.
20805301	6	72	theme	making	1026:1031	arg1	CYP2W1					1033:1038	a topology making CYP2W1	1015:1038	a topology making CYP2W1 available to the ER glycosylation machinery	1015:1082	Analysis of the membrane topology indicated that unlike other cytochromes P450, CYP2W1 in HEK 293-transfected cells and in nontransfected Caco2TC7 and HepG2 cells is oriented toward the lumen of the ER, a topology making CYP2W1 available to the ER glycosylation machinery.
20805301	6	72	theme	making	1026:1031	arg1	lumen					998:1002	the lumen	994:1002	the lumen of the ER	994:1012	Analysis of the membrane topology indicated that unlike other cytochromes P450, CYP2W1 in HEK 293-transfected cells and in nontransfected Caco2TC7 and HepG2 cells is oriented toward the lumen of the ER, a topology making CYP2W1 available to the ER glycosylation machinery.
20805301	4	73	theme	normal	471:476	arg1	tissues					489:495	cancer tissues	482:495	cancer tissues	482:495	The analysis of colorectal normal and cancer tissues and CYP2W1 overexpressing human embryonic kidney (HEK) 293 cells showed that a fraction of CYP2W1 is modified by N-glycosylation.
20805301	7	74	dep	microscopy	1104:1113	arg1	experiments					1146:1156	experiments	1146:1156	experiments	1146:1156	Immunofluorescence microscopy and cell surface biotinylation experiments revealed approximately 8% of the CYP2W1 on the cell surface.
20805301	0	75	theme	cancer-specific	11:25	arg1	P450					38:41	Colorectal cancer-specific cytochrome P450 2W1	0:45	Colorectal cancer-specific cytochrome P450 2W1	0:45	Colorectal cancer-specific cytochrome P450 2W1: intracellular localization, glycosylation, and catalytic activity.
20805301	3	76	theme	reticulum	385:393	arg1	topology					400:407	inverted endoplasmic reticulum (ER) topology	364:407	inverted endoplasmic reticulum (ER) topology	364:407	In this study, we characterize post-translational modification, inverted endoplasmic reticulum (ER) topology, and catalytic activity of CYP2W1.
20805301	8	77	theme	P450	1345:1348	arg1	reductase					1350:1358	NADPH-cytochrome P450 reductase impossible	1328:1369	NADPH-cytochrome P450 reductase impossible	1328:1369	Despite the reverse orientation of CYP2W1 in the ER membrane, apparently making functional interactions with NADPH-cytochrome P450 reductase impossible, CYP2W1 in HEK 293 cells was active in the metabolism of indoline substrates and was able to activate aflatoxin B1 into cytotoxic products.
20805301	7	78	theme	surface	1124:1130	arg1	biotinylation					1132:1144	cell surface biotinylation	1119:1144	cell surface biotinylation	1119:1144	Immunofluorescence microscopy and cell surface biotinylation experiments revealed approximately 8% of the CYP2W1 on the cell surface.
20805301	6	79	theme	ER	1011:1012	arg1	lumen					998:1002	the lumen	994:1002	the lumen of the ER	994:1012	Analysis of the membrane topology indicated that unlike other cytochromes P450, CYP2W1 in HEK 293-transfected cells and in nontransfected Caco2TC7 and HepG2 cells is oriented toward the lumen of the ER, a topology making CYP2W1 available to the ER glycosylation machinery.
20805301	6	79	theme	ER	1011:1012	arg1	CYP2W1					1033:1038	a topology making CYP2W1	1015:1038	a topology making CYP2W1 available to the ER glycosylation machinery	1015:1082	Analysis of the membrane topology indicated that unlike other cytochromes P450, CYP2W1 in HEK 293-transfected cells and in nontransfected Caco2TC7 and HepG2 cells is oriented toward the lumen of the ER, a topology making CYP2W1 available to the ER glycosylation machinery.
20805301	3	80	theme	inverted	364:371	arg1	topology					400:407	inverted endoplasmic reticulum (ER) topology	364:407	inverted endoplasmic reticulum (ER) topology	364:407	In this study, we characterize post-translational modification, inverted endoplasmic reticulum (ER) topology, and catalytic activity of CYP2W1.
20805301	8	81	theme	impossible	1360:1369	arg1	reductase					1350:1358	NADPH-cytochrome P450 reductase impossible	1328:1369	NADPH-cytochrome P450 reductase impossible	1328:1369	Despite the reverse orientation of CYP2W1 in the ER membrane, apparently making functional interactions with NADPH-cytochrome P450 reductase impossible, CYP2W1 in HEK 293 cells was active in the metabolism of indoline substrates and was able to activate aflatoxin B1 into cytotoxic products.
20805301	9	82	theme	cytochrome	1553:1562	arg1	enzyme					1569:1574	a cytochrome P450 enzyme	1551:1574	a cytochrome P450 enzyme with a luminal ER orientation	1551:1604	The study identifies for the first time a cytochrome P450 enzyme with a luminal ER orientation and still retaining catalytic activity.
20805301	4	83	theme	overexpressing	508:521	arg1	cells					556:560	CYP2W1 overexpressing human embryonic kidney (HEK) 293 cells	501:560	CYP2W1 overexpressing human embryonic kidney (HEK) 293 cells	501:560	The analysis of colorectal normal and cancer tissues and CYP2W1 overexpressing human embryonic kidney (HEK) 293 cells showed that a fraction of CYP2W1 is modified by N-glycosylation.
20805301	3	84	theme	CYP2W1	436:441	arg1	activity					424:431	catalytic activity	414:431	catalytic activity of CYP2W1	414:441	In this study, we characterize post-translational modification, inverted endoplasmic reticulum (ER) topology, and catalytic activity of CYP2W1.
20805301	3	84	theme	CYP2W1	436:441	arg1	topology					400:407	inverted endoplasmic reticulum (ER) topology	364:407	inverted endoplasmic reticulum (ER) topology	364:407	In this study, we characterize post-translational modification, inverted endoplasmic reticulum (ER) topology, and catalytic activity of CYP2W1.
20805301	3	84	theme	CYP2W1	436:441	arg1	modification					350:361	post-translational modification	331:361	post-translational modification	331:361	In this study, we characterize post-translational modification, inverted endoplasmic reticulum (ER) topology, and catalytic activity of CYP2W1.
20805301	5	85	theme	N177A	762:766	arg1	mutant					768:773	an N177A mutant	759:773	an N177A mutant	759:773	Bioinformatic analysis identified Asn177 as the only possible glycosylation site of CYP2W1, which was supported by the inability of an N177A mutant to be glycosylated in HEK 293 cells.
20805301	4	86	theme	embryonic	529:537	arg1	HEK					547:549	HEK	547:549	HEK	547:549	The analysis of colorectal normal and cancer tissues and CYP2W1 overexpressing human embryonic kidney (HEK) 293 cells showed that a fraction of CYP2W1 is modified by N-glycosylation.
20805301	4	86	theme	embryonic	529:537	arg1	kidney					539:544	human embryonic kidney	523:544	CYP2W1 overexpressing human embryonic kidney (HEK) 293 cells	501:560	The analysis of colorectal normal and cancer tissues and CYP2W1 overexpressing human embryonic kidney (HEK) 293 cells showed that a fraction of CYP2W1 is modified by N-glycosylation.
20805301	6	87	from	CYP2W1	892:897	arg1	Caco2TC7					950:957	nontransfected Caco2TC7 and HepG2 cells	935:973	Caco2TC7	950:957	Analysis of the membrane topology indicated that unlike other cytochromes P450, CYP2W1 in HEK 293-transfected cells and in nontransfected Caco2TC7 and HepG2 cells is oriented toward the lumen of the ER, a topology making CYP2W1 available to the ER glycosylation machinery.
20805301	6	87	from	CYP2W1	892:897	arg1	cells					969:973	nontransfected Caco2TC7 and HepG2 cells	935:973	cells	969:973	Analysis of the membrane topology indicated that unlike other cytochromes P450, CYP2W1 in HEK 293-transfected cells and in nontransfected Caco2TC7 and HepG2 cells is oriented toward the lumen of the ER, a topology making CYP2W1 available to the ER glycosylation machinery.
20805301	6	87	from	CYP2W1	892:897	arg1	cells					922:926	HEK 293-transfected cells	902:926	HEK 293-transfected cells	902:926	Analysis of the membrane topology indicated that unlike other cytochromes P450, CYP2W1 in HEK 293-transfected cells and in nontransfected Caco2TC7 and HepG2 cells is oriented toward the lumen of the ER, a topology making CYP2W1 available to the ER glycosylation machinery.
20805301	8	88	theme	HEK	1382:1384	arg1	cells					1390:1394	HEK 293 cells	1382:1394	HEK 293 cells	1382:1394	Despite the reverse orientation of CYP2W1 in the ER membrane, apparently making functional interactions with NADPH-cytochrome P450 reductase impossible, CYP2W1 in HEK 293 cells was active in the metabolism of indoline substrates and was able to activate aflatoxin B1 into cytotoxic products.
20805301	6	89	theme	glycosylation	1060:1072	arg1	machinery					1074:1082	the ER glycosylation machinery	1053:1082	the ER glycosylation machinery	1053:1082	Analysis of the membrane topology indicated that unlike other cytochromes P450, CYP2W1 in HEK 293-transfected cells and in nontransfected Caco2TC7 and HepG2 cells is oriented toward the lumen of the ER, a topology making CYP2W1 available to the ER glycosylation machinery.
20805301	9	90	theme	ER	1591:1592	arg1	orientation					1594:1604	a luminal ER orientation	1581:1604	a luminal ER orientation	1581:1604	The study identifies for the first time a cytochrome P450 enzyme with a luminal ER orientation and still retaining catalytic activity.
20805301	4	91	theme	CYP2W1	588:593	arg1	fraction					576:583	a fraction	574:583	a fraction of CYP2W1	574:593	The analysis of colorectal normal and cancer tissues and CYP2W1 overexpressing human embryonic kidney (HEK) 293 cells showed that a fraction of CYP2W1 is modified by N-glycosylation.
23613470	0	0	theme	epithelial	69:78	arg1	cells					80:84	polarized epithelial cells	59:84	polarized epithelial cells	59:84	The apical and basolateral secretion of Wnt11 and Wnt3a in polarized epithelial cells is regulated by different mechanisms.
23613470	3	1	theme	polarized	639:647	arg1	secretion					649:657	the polarized secretion	635:657	the polarized secretion of Wnts	635:665	Glycosylation was shown to be important for the sorting of some transmembrane and secreted proteins, but glycan profiles and their roles in the polarized secretion of Wnts has not yet been demonstrated.
23613470	10	2	theme	basolateral	1508:1518	arg1	secretion					1520:1528	the basolateral secretion	1504:1528	the basolateral secretion of Wnt3a	1504:1537	The recycling of Wls by AP-2 was necessary for the basolateral secretion of Wnt3a but not for the apical secretion of Wnt11.
23613470	2	3	from	role	380:383	arg1	sorting					399:405	the sorting	395:405	the sorting of Wnts to the final destination in polarized epithelial cells	395:468	Although Wntless (Wls) has been shown to interact with Wnts and support their secretion, the role of Wls in the sorting of Wnts to the final destination in polarized epithelial cells have not been clarified.
23613470	0	4	theme	polarized	59:67	arg1	cells					80:84	polarized epithelial cells	59:84	polarized epithelial cells	59:84	The apical and basolateral secretion of Wnt11 and Wnt3a in polarized epithelial cells is regulated by different mechanisms.
23613470	8	5	from	galectin-3	1219:1228	arg1	processing					1195:1204	Glycosylation processing	1181:1204	Glycosylation processing at Asn40 and galectin-3	1181:1228	Glycosylation processing at Asn40 and galectin-3 were required for the apical secretion of Wnt11, whereas clathrin and adaptor protein-1 were required for the basolateral secretion of Wnt3a.
23613470	1	6	theme	lipid-modified	145:158	arg1	morphogens					160:169	glycan- and lipid-modified morphogens	133:169	glycan- and lipid-modified morphogens that are important for cellular responses	133:211	Wnts are glycan- and lipid-modified morphogens that are important for cellular responses, but how Wnts are secreted in polarized epithelial cells remains unclear.
23613470	1	6	theme	lipid-modified	145:158	arg1	Wnts					124:127	Wnts	124:127	Wnts	124:127	Wnts are glycan- and lipid-modified morphogens that are important for cellular responses, but how Wnts are secreted in polarized epithelial cells remains unclear.
23613470	6	7	theme	basolateral	922:932	arg1	membrane					934:941	the basolateral membrane	918:941	the basolateral membrane	918:941	Wls was localized to the basolateral membrane.
23613470	11	8	theme	polarized	1640:1648	arg1	secretion					1650:1658	the polarized secretion	1636:1658	the polarized secretion of Wnt11 and Wnt3a	1636:1677	These results suggest that Wls has different roles in the polarized secretion of Wnt11 and Wnt3a and that glycosylation processing of Wnts decides their secretory routes.
23613470	7	9	mod	modified	995:1002	arg3	high-mannose					1033:1044	high-mannose(Asn90)-	1033:1052	high-mannose(Asn90)-	1033:1052	Mass-spectrometric analyses revealed that Wnt11 is modified with complex/hybrid(Asn40)-, high-mannose(Asn90)- and high-mannose/hybrid(Asn300)-type glycans and that Wnt3a is modified with two high-mannose-type glycans (Asn87 and Asn298).
23613470	7	9	mod	modified	995:1002	arg1	Wnt11					986:990	Wnt11	986:990	Wnt11	986:990	Mass-spectrometric analyses revealed that Wnt11 is modified with complex/hybrid(Asn40)-, high-mannose(Asn90)- and high-mannose/hybrid(Asn300)-type glycans and that Wnt3a is modified with two high-mannose-type glycans (Asn87 and Asn298).
23613470	7	9	mod	modified	995:1002	arg3	glycans					1091:1097	high-mannose/hybrid(Asn300)-type glycans	1058:1097	high-mannose/hybrid(Asn300)-type glycans	1058:1097	Mass-spectrometric analyses revealed that Wnt11 is modified with complex/hybrid(Asn40)-, high-mannose(Asn90)- and high-mannose/hybrid(Asn300)-type glycans and that Wnt3a is modified with two high-mannose-type glycans (Asn87 and Asn298).
23613470	7	9	mod	modified	995:1002	arg3	complex/hybrid					1009:1022	complex/hybrid(Asn40)-	1009:1030	complex/hybrid(Asn40)-	1009:1030	Mass-spectrometric analyses revealed that Wnt11 is modified with complex/hybrid(Asn40)-, high-mannose(Asn90)- and high-mannose/hybrid(Asn300)-type glycans and that Wnt3a is modified with two high-mannose-type glycans (Asn87 and Asn298).
23613470	3	10	from	profiles	607:614	arg1	secretion					649:657	the polarized secretion	635:657	the polarized secretion of Wnts	635:665	Glycosylation was shown to be important for the sorting of some transmembrane and secreted proteins, but glycan profiles and their roles in the polarized secretion of Wnts has not yet been demonstrated.
23613470	1	11	theme	polarized	243:251	arg1	cells					264:268	polarized epithelial cells	243:268	polarized epithelial cells	243:268	Wnts are glycan- and lipid-modified morphogens that are important for cellular responses, but how Wnts are secreted in polarized epithelial cells remains unclear.
23613470	10	12	theme	Wls	1474:1476	arg1	necessary					1490:1498	necessary	1490:1498	necessary	1490:1498	The recycling of Wls by AP-2 was necessary for the basolateral secretion of Wnt3a but not for the apical secretion of Wnt11.
23613470	10	12	theme	Wls	1474:1476	arg1	recycling					1461:1469	The recycling	1457:1469	The recycling of Wls by AP-2	1457:1484	The recycling of Wls by AP-2 was necessary for the basolateral secretion of Wnt3a but not for the apical secretion of Wnt11.
23613470	3	13	theme	Wnts	662:665	arg1	secretion					649:657	the polarized secretion	635:657	the polarized secretion of Wnts	635:665	Glycosylation was shown to be important for the sorting of some transmembrane and secreted proteins, but glycan profiles and their roles in the polarized secretion of Wnts has not yet been demonstrated.
23613470	8	14	from	Asn40	1209:1213	arg1	processing					1195:1204	Glycosylation processing	1181:1204	Glycosylation processing at Asn40 and galectin-3	1181:1228	Glycosylation processing at Asn40 and galectin-3 were required for the apical secretion of Wnt11, whereas clathrin and adaptor protein-1 were required for the basolateral secretion of Wnt3a.
23613470	8	15	theme	apical	1252:1257	arg1	secretion					1259:1267	the apical secretion	1248:1267	the apical secretion of Wnt11	1248:1276	Glycosylation processing at Asn40 and galectin-3 were required for the apical secretion of Wnt11, whereas clathrin and adaptor protein-1 were required for the basolateral secretion of Wnt3a.
23613470	1	16	theme	epithelial	253:262	arg1	cells					264:268	polarized epithelial cells	243:268	polarized epithelial cells	243:268	Wnts are glycan- and lipid-modified morphogens that are important for cellular responses, but how Wnts are secreted in polarized epithelial cells remains unclear.
23613470	11	17	theme	secretory	1735:1743	arg1	routes					1745:1750	their secretory routes	1729:1750	their secretory routes	1729:1750	These results suggest that Wls has different roles in the polarized secretion of Wnt11 and Wnt3a and that glycosylation processing of Wnts decides their secretory routes.
23613470	8	18	theme	Wnt11	1272:1276	arg1	secretion					1259:1267	the apical secretion	1248:1267	the apical secretion of Wnt11	1248:1276	Glycosylation processing at Asn40 and galectin-3 were required for the apical secretion of Wnt11, whereas clathrin and adaptor protein-1 were required for the basolateral secretion of Wnt3a.
23613470	2	19	theme	epithelial	453:462	arg1	cells					464:468	polarized epithelial cells	443:468	polarized epithelial cells	443:468	Although Wntless (Wls) has been shown to interact with Wnts and support their secretion, the role of Wls in the sorting of Wnts to the final destination in polarized epithelial cells have not been clarified.
23613470	2	20	theme	final	422:426	arg1	destination					428:438	the final destination	418:438	the final destination in polarized epithelial cells	418:468	Although Wntless (Wls) has been shown to interact with Wnts and support their secretion, the role of Wls in the sorting of Wnts to the final destination in polarized epithelial cells have not been clarified.
23613470	11	21	theme	Wnt11	1663:1667	arg1	secretion					1650:1658	the polarized secretion	1636:1658	the polarized secretion of Wnt11 and Wnt3a	1636:1677	These results suggest that Wls has different roles in the polarized secretion of Wnt11 and Wnt3a and that glycosylation processing of Wnts decides their secretory routes.
23613470	0	22	theme	apical	4:9	arg1	secretion					27:35	The apical and basolateral secretion	0:35	The apical and basolateral secretion of Wnt11 and Wnt3a in polarized epithelial cells	0:84	The apical and basolateral secretion of Wnt11 and Wnt3a in polarized epithelial cells is regulated by different mechanisms.
23613470	0	23	from	secretion	27:35	arg1	cells					80:84	polarized epithelial cells	59:84	polarized epithelial cells	59:84	The apical and basolateral secretion of Wnt11 and Wnt3a in polarized epithelial cells is regulated by different mechanisms.
23613470	8	24	theme	adaptor	1300:1306	arg1	protein-1					1308:1316	adaptor protein-1	1300:1316	adaptor protein-1	1300:1316	Glycosylation processing at Asn40 and galectin-3 were required for the apical secretion of Wnt11, whereas clathrin and adaptor protein-1 were required for the basolateral secretion of Wnt3a.
23613470	7	25	theme	high-mannose-type	1135:1151	arg1	Asn298					1172:1177	Asn298	1172:1177	Asn298	1172:1177	Mass-spectrometric analyses revealed that Wnt11 is modified with complex/hybrid(Asn40)-, high-mannose(Asn90)- and high-mannose/hybrid(Asn300)-type glycans and that Wnt3a is modified with two high-mannose-type glycans (Asn87 and Asn298).
23613470	7	25	theme	high-mannose-type	1135:1151	arg1	Asn87					1162:1166	Asn87	1162:1166	Asn87	1162:1166	Mass-spectrometric analyses revealed that Wnt11 is modified with complex/hybrid(Asn40)-, high-mannose(Asn90)- and high-mannose/hybrid(Asn300)-type glycans and that Wnt3a is modified with two high-mannose-type glycans (Asn87 and Asn298).
23613470	7	25	theme	high-mannose-type	1135:1151	arg1	glycans					1153:1159	two high-mannose-type glycans	1131:1159	two high-mannose-type glycans (Asn87 and Asn298)	1131:1178	Mass-spectrometric analyses revealed that Wnt11 is modified with complex/hybrid(Asn40)-, high-mannose(Asn90)- and high-mannose/hybrid(Asn300)-type glycans and that Wnt3a is modified with two high-mannose-type glycans (Asn87 and Asn298).
23613470	4	26	theme	different	772:780	arg1	mechanisms					782:791	different mechanisms	772:791	different mechanisms	772:791	Here we show the apical and basolateral secretion of Wnts is regulated by different mechanisms.
23613470	5	27	theme	polarized	869:877	arg1	cells					890:894	polarized epithelial cells	869:894	polarized epithelial cells	869:894	Wnt11 and Wnt3a were secreted apically and basolaterally, respectively, in polarized epithelial cells.
23613470	10	28	theme	Wnt3a	1533:1537	arg1	secretion					1520:1528	the basolateral secretion	1504:1528	the basolateral secretion of Wnt3a	1504:1537	The recycling of Wls by AP-2 was necessary for the basolateral secretion of Wnt3a but not for the apical secretion of Wnt11.
23613470	0	29	theme	basolateral	15:25	arg1	secretion					27:35	The apical and basolateral secretion	0:35	The apical and basolateral secretion of Wnt11 and Wnt3a in polarized epithelial cells	0:84	The apical and basolateral secretion of Wnt11 and Wnt3a in polarized epithelial cells is regulated by different mechanisms.
23613470	5	30	theme	epithelial	879:888	arg1	cells					890:894	polarized epithelial cells	869:894	polarized epithelial cells	869:894	Wnt11 and Wnt3a were secreted apically and basolaterally, respectively, in polarized epithelial cells.
23613470	2	31	theme	Wls	388:390	arg1	role					380:383	the role	376:383	the role of Wls in the sorting of Wnts to the final destination in polarized epithelial cells	376:468	Although Wntless (Wls) has been shown to interact with Wnts and support their secretion, the role of Wls in the sorting of Wnts to the final destination in polarized epithelial cells have not been clarified.
23613470	0	32	theme	different	102:110	arg1	mechanisms					112:121	different mechanisms	102:121	different mechanisms	102:121	The apical and basolateral secretion of Wnt11 and Wnt3a in polarized epithelial cells is regulated by different mechanisms.
23613470	2	33	from	destination	428:438	arg1	cells					464:468	polarized epithelial cells	443:468	polarized epithelial cells	443:468	Although Wntless (Wls) has been shown to interact with Wnts and support their secretion, the role of Wls in the sorting of Wnts to the final destination in polarized epithelial cells have not been clarified.
23613470	1	34	theme	cellular	194:201	arg1	responses					203:211	cellular responses	194:211	cellular responses	194:211	Wnts are glycan- and lipid-modified morphogens that are important for cellular responses, but how Wnts are secreted in polarized epithelial cells remains unclear.
23613470	3	35	from	roles	626:630	arg1	secretion					649:657	the polarized secretion	635:657	the polarized secretion of Wnts	635:665	Glycosylation was shown to be important for the sorting of some transmembrane and secreted proteins, but glycan profiles and their roles in the polarized secretion of Wnts has not yet been demonstrated.
23613470	11	36	theme	Wnt3a	1673:1677	arg1	secretion					1650:1658	the polarized secretion	1636:1658	the polarized secretion of Wnt11 and Wnt3a	1636:1677	These results suggest that Wls has different roles in the polarized secretion of Wnt11 and Wnt3a and that glycosylation processing of Wnts decides their secretory routes.
23613470	10	37	theme	apical	1555:1560	arg1	secretion					1562:1570	the apical secretion	1551:1570	the apical secretion of Wnt11	1551:1579	The recycling of Wls by AP-2 was necessary for the basolateral secretion of Wnt3a but not for the apical secretion of Wnt11.
23613470	7	38	dep	glycans	1153:1159	arg1	Asn298					1172:1177	Asn298	1172:1177	Asn298	1172:1177	Mass-spectrometric analyses revealed that Wnt11 is modified with complex/hybrid(Asn40)-, high-mannose(Asn90)- and high-mannose/hybrid(Asn300)-type glycans and that Wnt3a is modified with two high-mannose-type glycans (Asn87 and Asn298).
23613470	7	38	dep	glycans	1153:1159	arg1	Asn87					1162:1166	Asn87	1162:1166	Asn87	1162:1166	Mass-spectrometric analyses revealed that Wnt11 is modified with complex/hybrid(Asn40)-, high-mannose(Asn90)- and high-mannose/hybrid(Asn300)-type glycans and that Wnt3a is modified with two high-mannose-type glycans (Asn87 and Asn298).
23613470	7	38	dep	glycans	1153:1159	arg1	glycans					1153:1159	two high-mannose-type glycans	1131:1159	two high-mannose-type glycans (Asn87 and Asn298)	1131:1178	Mass-spectrometric analyses revealed that Wnt11 is modified with complex/hybrid(Asn40)-, high-mannose(Asn90)- and high-mannose/hybrid(Asn300)-type glycans and that Wnt3a is modified with two high-mannose-type glycans (Asn87 and Asn298).
23613470	3	39	theme	secreted	577:584	arg1	proteins					586:593	some transmembrane and secreted proteins	554:593	some transmembrane and secreted proteins	554:593	Glycosylation was shown to be important for the sorting of some transmembrane and secreted proteins, but glycan profiles and their roles in the polarized secretion of Wnts has not yet been demonstrated.
23613470	7	40	mod	modified	1117:1124	arg3	glycans					1153:1159	two high-mannose-type glycans	1131:1159	two high-mannose-type glycans (Asn87 and Asn298)	1131:1178	Mass-spectrometric analyses revealed that Wnt11 is modified with complex/hybrid(Asn40)-, high-mannose(Asn90)- and high-mannose/hybrid(Asn300)-type glycans and that Wnt3a is modified with two high-mannose-type glycans (Asn87 and Asn298).
23613470	7	40	mod	modified	1117:1124	arg3	Asn87					1162:1166	Asn87	1162:1166	Asn87	1162:1166	Mass-spectrometric analyses revealed that Wnt11 is modified with complex/hybrid(Asn40)-, high-mannose(Asn90)- and high-mannose/hybrid(Asn300)-type glycans and that Wnt3a is modified with two high-mannose-type glycans (Asn87 and Asn298).
23613470	7	40	mod	modified	1117:1124	arg1	Wnt3a					1108:1112	Wnt3a	1108:1112	Wnt3a	1108:1112	Mass-spectrometric analyses revealed that Wnt11 is modified with complex/hybrid(Asn40)-, high-mannose(Asn90)- and high-mannose/hybrid(Asn300)-type glycans and that Wnt3a is modified with two high-mannose-type glycans (Asn87 and Asn298).
23613470	7	40	mod	modified	1117:1124	arg3	Asn298					1172:1177	Asn298	1172:1177	Asn298	1172:1177	Mass-spectrometric analyses revealed that Wnt11 is modified with complex/hybrid(Asn40)-, high-mannose(Asn90)- and high-mannose/hybrid(Asn300)-type glycans and that Wnt3a is modified with two high-mannose-type glycans (Asn87 and Asn298).
23613470	8	41	theme	Wnt3a	1365:1369	arg1	secretion					1352:1360	the basolateral secretion	1336:1360	the basolateral secretion of Wnt3a	1336:1369	Glycosylation processing at Asn40 and galectin-3 were required for the apical secretion of Wnt11, whereas clathrin and adaptor protein-1 were required for the basolateral secretion of Wnt3a.
23613470	8	42	theme	Glycosylation	1181:1193	arg1	processing					1195:1204	Glycosylation processing	1181:1204	Glycosylation processing at Asn40 and galectin-3	1181:1228	Glycosylation processing at Asn40 and galectin-3 were required for the apical secretion of Wnt11, whereas clathrin and adaptor protein-1 were required for the basolateral secretion of Wnt3a.
23613470	2	43	theme	Wnts	410:413	arg1	sorting					399:405	the sorting	395:405	the sorting of Wnts to the final destination in polarized epithelial cells	395:468	Although Wntless (Wls) has been shown to interact with Wnts and support their secretion, the role of Wls in the sorting of Wnts to the final destination in polarized epithelial cells have not been clarified.
23613470	11	44	theme	Wnts	1716:1719	arg1	processing					1702:1711	glycosylation processing	1688:1711	glycosylation processing of Wnts	1688:1719	These results suggest that Wls has different roles in the polarized secretion of Wnt11 and Wnt3a and that glycosylation processing of Wnts decides their secretory routes.
23613470	3	45	theme	proteins	586:593	arg1	sorting					543:549	the sorting	539:549	the sorting of some transmembrane and secreted proteins	539:593	Glycosylation was shown to be important for the sorting of some transmembrane and secreted proteins, but glycan profiles and their roles in the polarized secretion of Wnts has not yet been demonstrated.
23613470	8	46	dep	required	1235:1242	arg1	whereas					1279:1285	whereas	1279:1285	whereas	1279:1285	Glycosylation processing at Asn40 and galectin-3 were required for the apical secretion of Wnt11, whereas clathrin and adaptor protein-1 were required for the basolateral secretion of Wnt3a.
23613470	9	47	theme	Asn40	1393:1397	arg1	site					1413:1416	the Asn40 glycosylation site	1389:1416	the Asn40 glycosylation site of Wnt11	1389:1425	By the fusion of the Asn40 glycosylation site of Wnt11, Wnt3a was secreted apically.
23613470	9	47	theme	Asn40	1393:1397	arg1	Wnt11					1421:1425	Wnt11	1421:1425	Wnt11	1421:1425	By the fusion of the Asn40 glycosylation site of Wnt11, Wnt3a was secreted apically.
23613470	0	48	theme	Wnt11	40:44	arg1	secretion					27:35	The apical and basolateral secretion	0:35	The apical and basolateral secretion of Wnt11 and Wnt3a in polarized epithelial cells	0:84	The apical and basolateral secretion of Wnt11 and Wnt3a in polarized epithelial cells is regulated by different mechanisms.
23613470	11	49	theme	glycosylation	1688:1700	arg1	processing					1702:1711	glycosylation processing	1688:1711	glycosylation processing of Wnts	1688:1719	These results suggest that Wls has different roles in the polarized secretion of Wnt11 and Wnt3a and that glycosylation processing of Wnts decides their secretory routes.
23613470	4	50	theme	Wnts	751:754	arg1	secretion					738:746	the apical and basolateral secretion	711:746	the apical and basolateral secretion of Wnts	711:754	Here we show the apical and basolateral secretion of Wnts is regulated by different mechanisms.
23613470	9	51	theme	glycosylation	1399:1411	arg1	site					1413:1416	the Asn40 glycosylation site	1389:1416	the Asn40 glycosylation site of Wnt11	1389:1425	By the fusion of the Asn40 glycosylation site of Wnt11, Wnt3a was secreted apically.
23613470	9	51	theme	glycosylation	1399:1411	arg1	Wnt11					1421:1425	Wnt11	1421:1425	Wnt11	1421:1425	By the fusion of the Asn40 glycosylation site of Wnt11, Wnt3a was secreted apically.
23613470	8	52	theme	basolateral	1340:1350	arg1	secretion					1352:1360	the basolateral secretion	1336:1360	the basolateral secretion of Wnt3a	1336:1369	Glycosylation processing at Asn40 and galectin-3 were required for the apical secretion of Wnt11, whereas clathrin and adaptor protein-1 were required for the basolateral secretion of Wnt3a.
23613470	4	53	theme	apical	715:720	arg1	secretion					738:746	the apical and basolateral secretion	711:746	the apical and basolateral secretion of Wnts	711:754	Here we show the apical and basolateral secretion of Wnts is regulated by different mechanisms.
23613470	3	54	theme	transmembrane	559:571	arg1	proteins					586:593	some transmembrane and secreted proteins	554:593	some transmembrane and secreted proteins	554:593	Glycosylation was shown to be important for the sorting of some transmembrane and secreted proteins, but glycan profiles and their roles in the polarized secretion of Wnts has not yet been demonstrated.
23613470	7	55	theme	Mass-spectrometric	944:961	arg1	analyses					963:970	Mass-spectrometric analyses	944:970	Mass-spectrometric analyses	944:970	Mass-spectrometric analyses revealed that Wnt11 is modified with complex/hybrid(Asn40)-, high-mannose(Asn90)- and high-mannose/hybrid(Asn300)-type glycans and that Wnt3a is modified with two high-mannose-type glycans (Asn87 and Asn298).
23613470	9	56	theme	site	1413:1416	arg1	fusion					1379:1384	the fusion	1375:1384	the fusion of the Asn40 glycosylation site of Wnt11	1375:1425	By the fusion of the Asn40 glycosylation site of Wnt11, Wnt3a was secreted apically.
23613470	3	57	theme	glycan	600:605	arg1	profiles					607:614	glycan profiles	600:614	glycan profiles	600:614	Glycosylation was shown to be important for the sorting of some transmembrane and secreted proteins, but glycan profiles and their roles in the polarized secretion of Wnts has not yet been demonstrated.
23613470	10	58	theme	Wnt11	1575:1579	arg1	secretion					1562:1570	the apical secretion	1551:1570	the apical secretion of Wnt11	1551:1579	The recycling of Wls by AP-2 was necessary for the basolateral secretion of Wnt3a but not for the apical secretion of Wnt11.
23613470	11	59	contain	has	1613:1615	arg1	Wls					1609:1611	Wls	1609:1611	Wls	1609:1611	These results suggest that Wls has different roles in the polarized secretion of Wnt11 and Wnt3a and that glycosylation processing of Wnts decides their secretory routes.
23613470	11	59	contain	has	1613:1615	arg2	roles					1627:1631	different roles	1617:1631	different roles	1617:1631	These results suggest that Wls has different roles in the polarized secretion of Wnt11 and Wnt3a and that glycosylation processing of Wnts decides their secretory routes.
23613470	2	60	theme	polarized	443:451	arg1	cells					464:468	polarized epithelial cells	443:468	polarized epithelial cells	443:468	Although Wntless (Wls) has been shown to interact with Wnts and support their secretion, the role of Wls in the sorting of Wnts to the final destination in polarized epithelial cells have not been clarified.
23613470	4	61	theme	basolateral	726:736	arg1	secretion					738:746	the apical and basolateral secretion	711:746	the apical and basolateral secretion of Wnts	711:754	Here we show the apical and basolateral secretion of Wnts is regulated by different mechanisms.
23613470	9	62	theme	Wnt11	1421:1425	arg1	site					1413:1416	the Asn40 glycosylation site	1389:1416	the Asn40 glycosylation site of Wnt11	1389:1425	By the fusion of the Asn40 glycosylation site of Wnt11, Wnt3a was secreted apically.
23613470	9	62	theme	Wnt11	1421:1425	arg1	Wnt11					1421:1425	Wnt11	1421:1425	Wnt11	1421:1425	By the fusion of the Asn40 glycosylation site of Wnt11, Wnt3a was secreted apically.
23613470	4	63	dep	show	706:709	arg1	regulated					759:767	regulated	759:767	show the apical and basolateral secretion of Wnts is regulated by different mechanisms	706:791	Here we show the apical and basolateral secretion of Wnts is regulated by different mechanisms.
23613470	11	64	theme	different	1617:1625	arg1	roles					1627:1631	different roles	1617:1631	different roles	1617:1631	These results suggest that Wls has different roles in the polarized secretion of Wnt11 and Wnt3a and that glycosylation processing of Wnts decides their secretory routes.
23613470	0	65	theme	Wnt3a	50:54	arg1	secretion					27:35	The apical and basolateral secretion	0:35	The apical and basolateral secretion of Wnt11 and Wnt3a in polarized epithelial cells	0:84	The apical and basolateral secretion of Wnt11 and Wnt3a in polarized epithelial cells is regulated by different mechanisms.
23613470	9	66	gly	glycosylation	1399:1411	arg2	Wnt11					1421:1425	Wnt11	1421:1425	Wnt11	1421:1425	By the fusion of the Asn40 glycosylation site of Wnt11, Wnt3a was secreted apically.
23613470	9	66	gly	glycosylation	1399:1411	arg1	Wnt11					1421:1425	Wnt11	1421:1425	Wnt11	1421:1425	By the fusion of the Asn40 glycosylation site of Wnt11, Wnt3a was secreted apically.
23613470	9	66	gly	glycosylation	1399:1411	arg2	site					1413:1416	the Asn40 glycosylation site	1389:1416	the Asn40 glycosylation site of Wnt11	1389:1425	By the fusion of the Asn40 glycosylation site of Wnt11, Wnt3a was secreted apically.
23613470	7	67	theme	-type	1085:1089	arg1	glycans					1091:1097	high-mannose/hybrid(Asn300)-type glycans	1058:1097	high-mannose/hybrid(Asn300)-type glycans	1058:1097	Mass-spectrometric analyses revealed that Wnt11 is modified with complex/hybrid(Asn40)-, high-mannose(Asn90)- and high-mannose/hybrid(Asn300)-type glycans and that Wnt3a is modified with two high-mannose-type glycans (Asn87 and Asn298).
23613470	1	68	theme	glycan-	133:139	arg1	morphogens					160:169	glycan- and lipid-modified morphogens	133:169	glycan- and lipid-modified morphogens that are important for cellular responses	133:211	Wnts are glycan- and lipid-modified morphogens that are important for cellular responses, but how Wnts are secreted in polarized epithelial cells remains unclear.
23613470	1	68	theme	glycan-	133:139	arg1	Wnts					124:127	Wnts	124:127	Wnts	124:127	Wnts are glycan- and lipid-modified morphogens that are important for cellular responses, but how Wnts are secreted in polarized epithelial cells remains unclear.
11769972	4	0	theme	subcellular	976:986	arg1	localization					988:999	subcellular localization	976:999	subcellular localization	976:999	Purification and characterization of the mutant proteins demonstrated that: (i) both O-glycosylation sites of HB-EGF are utilized, (ii) HB-EGF secretion does not require O-glycosylation, (iii) removal of O-glycans does not affect proteolytic cleavage of the HB-EGF precursor, nor does it influence HB-EGF intracellular trafficking or subcellular localization, and (iv) HB-EGF produced by HeLa cells is heavily sialylated.
11769972	5	1	from	differences	1160:1170	arg1	activity					1192:1199	receptor binding activity	1175:1199	receptor binding activity	1175:1199	Comparisons between glycosylation mutants and wild-type HB-EGF revealed no significant apparent differences in receptor binding activity.
11769972	1	2	theme	growth	173:178	arg1	HB-EGF					188:193	HB-EGF	188:193	HB-EGF	188:193	Heparin-binding epidermal growth factor-like growth factor (HB-EGF) is a 22 kDa, O-glycosylated protein.
11769972	1	2	theme	growth	173:178	arg1	protein					224:230	a 22 kDa, O-glycosylated protein	199:230	a 22 kDa, O-glycosylated protein	199:230	Heparin-binding epidermal growth factor-like growth factor (HB-EGF) is a 22 kDa, O-glycosylated protein.
11769972	1	2	theme	growth	173:178	arg1	factor					180:185	Heparin-binding epidermal growth factor-like growth factor	128:185	Heparin-binding epidermal growth factor-like growth factor (HB-EGF)	128:194	Heparin-binding epidermal growth factor-like growth factor (HB-EGF) is a 22 kDa, O-glycosylated protein.
11769972	4	3	used	utilized	763:770	arg2	sites					743:747	O-glycosylation sites	727:747	O-glycosylation sites of HB-EGF	727:757	Purification and characterization of the mutant proteins demonstrated that: (i) both O-glycosylation sites of HB-EGF are utilized, (ii) HB-EGF secretion does not require O-glycosylation, (iii) removal of O-glycans does not affect proteolytic cleavage of the HB-EGF precursor, nor does it influence HB-EGF intracellular trafficking or subcellular localization, and (iv) HB-EGF produced by HeLa cells is heavily sialylated.
11769972	4	3	used	utilized	763:770	arg2	HB-EGF					752:757	HB-EGF	752:757	HB-EGF	752:757	Purification and characterization of the mutant proteins demonstrated that: (i) both O-glycosylation sites of HB-EGF are utilized, (ii) HB-EGF secretion does not require O-glycosylation, (iii) removal of O-glycans does not affect proteolytic cleavage of the HB-EGF precursor, nor does it influence HB-EGF intracellular trafficking or subcellular localization, and (iv) HB-EGF produced by HeLa cells is heavily sialylated.
11769972	4	4	theme	HB-EGF	900:905	arg1	precursor					907:915	the HB-EGF precursor	896:915	the HB-EGF precursor	896:915	Purification and characterization of the mutant proteins demonstrated that: (i) both O-glycosylation sites of HB-EGF are utilized, (ii) HB-EGF secretion does not require O-glycosylation, (iii) removal of O-glycans does not affect proteolytic cleavage of the HB-EGF precursor, nor does it influence HB-EGF intracellular trafficking or subcellular localization, and (iv) HB-EGF produced by HeLa cells is heavily sialylated.
11769972	4	5	theme	O-glycans	846:854	arg1	removal					835:841	(iii) removal	829:841	(iii) removal of O-glycans	829:854	Purification and characterization of the mutant proteins demonstrated that: (i) both O-glycosylation sites of HB-EGF are utilized, (ii) HB-EGF secretion does not require O-glycosylation, (iii) removal of O-glycans does not affect proteolytic cleavage of the HB-EGF precursor, nor does it influence HB-EGF intracellular trafficking or subcellular localization, and (iv) HB-EGF produced by HeLa cells is heavily sialylated.
11769972	0	6	theme	O-glycosylation	90:104	arg1	sites					106:110	O-glycosylation sites	90:110	O-glycosylation sites	90:110	Site-directed mutagenesis of heparin-binding EGF-like growth factor (HB-EGF): analysis of O-glycosylation sites and properties.
11769972	1	7	gly	O-glycosylated	209:222	arg1	kDa					204:206	kDa	204:206	kDa	204:206	Heparin-binding epidermal growth factor-like growth factor (HB-EGF) is a 22 kDa, O-glycosylated protein.
11769972	3	8	theme	glycosylation	556:568	arg1	Thr75					577:581	Thr75	577:581	Thr75	577:581	Site-directed mutagenesis of HB-EGF cDNA using oligonucleotide- and PCR-directed techniques was performed to change the potential glycosylation sites, Thr75 and Thr85, to alanine residues to prevent O-glycosylation.
11769972	3	8	theme	glycosylation	556:568	arg1	sites					570:574	the potential glycosylation sites	542:574	the potential glycosylation sites	542:574	Site-directed mutagenesis of HB-EGF cDNA using oligonucleotide- and PCR-directed techniques was performed to change the potential glycosylation sites, Thr75 and Thr85, to alanine residues to prevent O-glycosylation.
11769972	3	8	theme	glycosylation	556:568	arg1	Thr85					587:591	Thr85	587:591	Thr85	587:591	Site-directed mutagenesis of HB-EGF cDNA using oligonucleotide- and PCR-directed techniques was performed to change the potential glycosylation sites, Thr75 and Thr85, to alanine residues to prevent O-glycosylation.
11769972	4	9	theme	mutant	683:688	arg1	proteins					690:697	the mutant proteins	679:697	the mutant proteins	679:697	Purification and characterization of the mutant proteins demonstrated that: (i) both O-glycosylation sites of HB-EGF are utilized, (ii) HB-EGF secretion does not require O-glycosylation, (iii) removal of O-glycans does not affect proteolytic cleavage of the HB-EGF precursor, nor does it influence HB-EGF intracellular trafficking or subcellular localization, and (iv) HB-EGF produced by HeLa cells is heavily sialylated.
11769972	2	10	theme	secreted	322:329	arg1	protein					342:348	a secreted, bioactive protein	320:348	a secreted, bioactive protein	320:348	HeLa cells infected with a recombinant vaccinia virus expressing human HB-EGF produced a secreted, bioactive protein, with Mr 22,000 that was decreased to 14,000 by treatment with O-glycanase.
11769972	4	11	theme	HB-EGF	940:945	arg1	trafficking					961:971	HB-EGF intracellular trafficking	940:971	HB-EGF intracellular trafficking	940:971	Purification and characterization of the mutant proteins demonstrated that: (i) both O-glycosylation sites of HB-EGF are utilized, (ii) HB-EGF secretion does not require O-glycosylation, (iii) removal of O-glycans does not affect proteolytic cleavage of the HB-EGF precursor, nor does it influence HB-EGF intracellular trafficking or subcellular localization, and (iv) HB-EGF produced by HeLa cells is heavily sialylated.
11769972	4	12	dep	removal	835:841	arg1	iii					830:832	iii	830:832	iii	830:832	Purification and characterization of the mutant proteins demonstrated that: (i) both O-glycosylation sites of HB-EGF are utilized, (ii) HB-EGF secretion does not require O-glycosylation, (iii) removal of O-glycans does not affect proteolytic cleavage of the HB-EGF precursor, nor does it influence HB-EGF intracellular trafficking or subcellular localization, and (iv) HB-EGF produced by HeLa cells is heavily sialylated.
11769972	2	13	theme	vaccinia	272:279	arg1	virus					281:285	a recombinant vaccinia virus	258:285	a recombinant vaccinia virus expressing human HB-EGF	258:309	HeLa cells infected with a recombinant vaccinia virus expressing human HB-EGF produced a secreted, bioactive protein, with Mr 22,000 that was decreased to 14,000 by treatment with O-glycanase.
11769972	3	14	theme	Site-directed	426:438	arg1	mutagenesis					440:450	Site-directed mutagenesis	426:450	Site-directed mutagenesis of HB-EGF cDNA using oligonucleotide- and PCR-directed techniques	426:516	Site-directed mutagenesis of HB-EGF cDNA using oligonucleotide- and PCR-directed techniques was performed to change the potential glycosylation sites, Thr75 and Thr85, to alanine residues to prevent O-glycosylation.
11769972	0	15	theme	sites	106:110	arg1	analysis					78:85	analysis	78:85	Site-directed mutagenesis of heparin-binding EGF-like growth factor (HB-EGF): analysis of O-glycosylation sites and properties.	0:126	Site-directed mutagenesis of heparin-binding EGF-like growth factor (HB-EGF): analysis of O-glycosylation sites and properties.
11769972	4	16	dep	HB-EGF	1011:1016	arg1	iv					1007:1008	iv	1007:1008	iv	1007:1008	Purification and characterization of the mutant proteins demonstrated that: (i) both O-glycosylation sites of HB-EGF are utilized, (ii) HB-EGF secretion does not require O-glycosylation, (iii) removal of O-glycans does not affect proteolytic cleavage of the HB-EGF precursor, nor does it influence HB-EGF intracellular trafficking or subcellular localization, and (iv) HB-EGF produced by HeLa cells is heavily sialylated.
11769972	2	17	theme	recombinant	260:270	arg1	virus					281:285	a recombinant vaccinia virus	258:285	a recombinant vaccinia virus expressing human HB-EGF	258:309	HeLa cells infected with a recombinant vaccinia virus expressing human HB-EGF produced a secreted, bioactive protein, with Mr 22,000 that was decreased to 14,000 by treatment with O-glycanase.
11769972	2	18	with	treatment	398:406	arg1	O-glycanase					413:423	O-glycanase	413:423	O-glycanase	413:423	HeLa cells infected with a recombinant vaccinia virus expressing human HB-EGF produced a secreted, bioactive protein, with Mr 22,000 that was decreased to 14,000 by treatment with O-glycanase.
11769972	4	19	theme	HB-EGF	752:757	arg1	HB-EGF					752:757	HB-EGF	752:757	HB-EGF	752:757	Purification and characterization of the mutant proteins demonstrated that: (i) both O-glycosylation sites of HB-EGF are utilized, (ii) HB-EGF secretion does not require O-glycosylation, (iii) removal of O-glycans does not affect proteolytic cleavage of the HB-EGF precursor, nor does it influence HB-EGF intracellular trafficking or subcellular localization, and (iv) HB-EGF produced by HeLa cells is heavily sialylated.
11769972	4	19	theme	HB-EGF	752:757	arg1	sites					743:747	O-glycosylation sites	727:747	O-glycosylation sites of HB-EGF	727:757	Purification and characterization of the mutant proteins demonstrated that: (i) both O-glycosylation sites of HB-EGF are utilized, (ii) HB-EGF secretion does not require O-glycosylation, (iii) removal of O-glycans does not affect proteolytic cleavage of the HB-EGF precursor, nor does it influence HB-EGF intracellular trafficking or subcellular localization, and (iv) HB-EGF produced by HeLa cells is heavily sialylated.
11769972	5	20	theme	glycosylation	1084:1096	arg1	mutants					1098:1104	glycosylation mutants	1084:1104	glycosylation mutants	1084:1104	Comparisons between glycosylation mutants and wild-type HB-EGF revealed no significant apparent differences in receptor binding activity.
11769972	4	21	dep	secretion	785:793	arg1	ii					774:775	ii	774:775	ii	774:775	Purification and characterization of the mutant proteins demonstrated that: (i) both O-glycosylation sites of HB-EGF are utilized, (ii) HB-EGF secretion does not require O-glycosylation, (iii) removal of O-glycans does not affect proteolytic cleavage of the HB-EGF precursor, nor does it influence HB-EGF intracellular trafficking or subcellular localization, and (iv) HB-EGF produced by HeLa cells is heavily sialylated.
11769972	0	22	theme	Site-directed	0:12	arg1	mutagenesis					14:24	Site-directed mutagenesis	0:24	Site-directed mutagenesis of heparin-binding EGF-like growth factor (HB-EGF): analysis of O-glycosylation sites and properties.	0:126	Site-directed mutagenesis of heparin-binding EGF-like growth factor (HB-EGF): analysis of O-glycosylation sites and properties.
11769972	5	23	theme	receptor	1175:1182	arg1	activity					1192:1199	receptor binding activity	1175:1199	receptor binding activity	1175:1199	Comparisons between glycosylation mutants and wild-type HB-EGF revealed no significant apparent differences in receptor binding activity.
11769972	4	24	theme	O-glycosylation	727:741	arg1	HB-EGF					752:757	HB-EGF	752:757	HB-EGF	752:757	Purification and characterization of the mutant proteins demonstrated that: (i) both O-glycosylation sites of HB-EGF are utilized, (ii) HB-EGF secretion does not require O-glycosylation, (iii) removal of O-glycans does not affect proteolytic cleavage of the HB-EGF precursor, nor does it influence HB-EGF intracellular trafficking or subcellular localization, and (iv) HB-EGF produced by HeLa cells is heavily sialylated.
11769972	4	24	theme	O-glycosylation	727:741	arg1	sites					743:747	O-glycosylation sites	727:747	O-glycosylation sites of HB-EGF	727:757	Purification and characterization of the mutant proteins demonstrated that: (i) both O-glycosylation sites of HB-EGF are utilized, (ii) HB-EGF secretion does not require O-glycosylation, (iii) removal of O-glycans does not affect proteolytic cleavage of the HB-EGF precursor, nor does it influence HB-EGF intracellular trafficking or subcellular localization, and (iv) HB-EGF produced by HeLa cells is heavily sialylated.
11769972	0	25	gly	O-glycosylation	90:104	arg2	sites					106:110	O-glycosylation sites	90:110	O-glycosylation sites	90:110	Site-directed mutagenesis of heparin-binding EGF-like growth factor (HB-EGF): analysis of O-glycosylation sites and properties.
11769972	3	26	gly	glycosylation	556:568	arg2	Thr85					587:591	Thr85	587:591	Thr85	587:591	Site-directed mutagenesis of HB-EGF cDNA using oligonucleotide- and PCR-directed techniques was performed to change the potential glycosylation sites, Thr75 and Thr85, to alanine residues to prevent O-glycosylation.
11769972	3	26	gly	glycosylation	556:568	arg2	Thr75					577:581	Thr75	577:581	Thr75	577:581	Site-directed mutagenesis of HB-EGF cDNA using oligonucleotide- and PCR-directed techniques was performed to change the potential glycosylation sites, Thr75 and Thr85, to alanine residues to prevent O-glycosylation.
11769972	3	26	gly	glycosylation	556:568	arg2	sites					570:574	the potential glycosylation sites	542:574	the potential glycosylation sites	542:574	Site-directed mutagenesis of HB-EGF cDNA using oligonucleotide- and PCR-directed techniques was performed to change the potential glycosylation sites, Thr75 and Thr85, to alanine residues to prevent O-glycosylation.
11769972	0	27	theme	heparin-binding	29:43	arg1	HB-EGF					69:74	HB-EGF	69:74	HB-EGF	69:74	Site-directed mutagenesis of heparin-binding EGF-like growth factor (HB-EGF): analysis of O-glycosylation sites and properties.
11769972	0	27	theme	heparin-binding	29:43	arg1	factor					61:66	heparin-binding EGF-like growth factor	29:66	heparin-binding EGF-like growth factor (HB-EGF)	29:75	Site-directed mutagenesis of heparin-binding EGF-like growth factor (HB-EGF): analysis of O-glycosylation sites and properties.
11769972	5	28	theme	binding	1184:1190	arg1	activity					1192:1199	receptor binding activity	1175:1199	receptor binding activity	1175:1199	Comparisons between glycosylation mutants and wild-type HB-EGF revealed no significant apparent differences in receptor binding activity.
11769972	4	29	theme	precursor	907:915	arg1	cleavage					884:891	proteolytic cleavage	872:891	proteolytic cleavage of the HB-EGF precursor	872:915	Purification and characterization of the mutant proteins demonstrated that: (i) both O-glycosylation sites of HB-EGF are utilized, (ii) HB-EGF secretion does not require O-glycosylation, (iii) removal of O-glycans does not affect proteolytic cleavage of the HB-EGF precursor, nor does it influence HB-EGF intracellular trafficking or subcellular localization, and (iv) HB-EGF produced by HeLa cells is heavily sialylated.
11769972	3	30	theme	alanine	597:603	arg1	residues					605:612	alanine residues	597:612	alanine residues	597:612	Site-directed mutagenesis of HB-EGF cDNA using oligonucleotide- and PCR-directed techniques was performed to change the potential glycosylation sites, Thr75 and Thr85, to alanine residues to prevent O-glycosylation.
11769972	3	31	theme	cDNA	462:465	arg1	mutagenesis					440:450	Site-directed mutagenesis	426:450	Site-directed mutagenesis of HB-EGF cDNA using oligonucleotide- and PCR-directed techniques	426:516	Site-directed mutagenesis of HB-EGF cDNA using oligonucleotide- and PCR-directed techniques was performed to change the potential glycosylation sites, Thr75 and Thr85, to alanine residues to prevent O-glycosylation.
11769972	2	32	dep	secreted	322:329	arg1	bioactive					332:340	bioactive	332:340	bioactive	332:340	HeLa cells infected with a recombinant vaccinia virus expressing human HB-EGF produced a secreted, bioactive protein, with Mr 22,000 that was decreased to 14,000 by treatment with O-glycanase.
11769972	0	33	theme	properties	116:125	arg1	analysis					78:85	analysis	78:85	Site-directed mutagenesis of heparin-binding EGF-like growth factor (HB-EGF): analysis of O-glycosylation sites and properties.	0:126	Site-directed mutagenesis of heparin-binding EGF-like growth factor (HB-EGF): analysis of O-glycosylation sites and properties.
11769972	2	34	theme	human	298:302	arg1	HB-EGF					304:309	human HB-EGF	298:309	human HB-EGF	298:309	HeLa cells infected with a recombinant vaccinia virus expressing human HB-EGF produced a secreted, bioactive protein, with Mr 22,000 that was decreased to 14,000 by treatment with O-glycanase.
11769972	1	35	theme	22	201:202	arg1	kDa					204:206	kDa	204:206	kDa	204:206	Heparin-binding epidermal growth factor-like growth factor (HB-EGF) is a 22 kDa, O-glycosylated protein.
11769972	0	36	theme	growth	54:59	arg1	HB-EGF					69:74	HB-EGF	69:74	HB-EGF	69:74	Site-directed mutagenesis of heparin-binding EGF-like growth factor (HB-EGF): analysis of O-glycosylation sites and properties.
11769972	0	36	theme	growth	54:59	arg1	factor					61:66	heparin-binding EGF-like growth factor	29:66	heparin-binding EGF-like growth factor (HB-EGF)	29:75	Site-directed mutagenesis of heparin-binding EGF-like growth factor (HB-EGF): analysis of O-glycosylation sites and properties.
11769972	4	37	gly	O-glycosylation	727:741	arg2	sites					743:747	O-glycosylation sites	727:747	O-glycosylation sites of HB-EGF	727:757	Purification and characterization of the mutant proteins demonstrated that: (i) both O-glycosylation sites of HB-EGF are utilized, (ii) HB-EGF secretion does not require O-glycosylation, (iii) removal of O-glycans does not affect proteolytic cleavage of the HB-EGF precursor, nor does it influence HB-EGF intracellular trafficking or subcellular localization, and (iv) HB-EGF produced by HeLa cells is heavily sialylated.
11769972	4	37	gly	O-glycosylation	727:741	arg1	HB-EGF					752:757	HB-EGF	752:757	HB-EGF	752:757	Purification and characterization of the mutant proteins demonstrated that: (i) both O-glycosylation sites of HB-EGF are utilized, (ii) HB-EGF secretion does not require O-glycosylation, (iii) removal of O-glycans does not affect proteolytic cleavage of the HB-EGF precursor, nor does it influence HB-EGF intracellular trafficking or subcellular localization, and (iv) HB-EGF produced by HeLa cells is heavily sialylated.
11769972	4	37	gly	O-glycosylation	727:741	arg2	HB-EGF					752:757	HB-EGF	752:757	HB-EGF	752:757	Purification and characterization of the mutant proteins demonstrated that: (i) both O-glycosylation sites of HB-EGF are utilized, (ii) HB-EGF secretion does not require O-glycosylation, (iii) removal of O-glycans does not affect proteolytic cleavage of the HB-EGF precursor, nor does it influence HB-EGF intracellular trafficking or subcellular localization, and (iv) HB-EGF produced by HeLa cells is heavily sialylated.
11769972	4	38	gly	sialylated	1052:1061	arg1	HB-EGF					1011:1016	(iv) HB-EGF	1006:1016	(iv) HB-EGF produced by HeLa cells	1006:1039	Purification and characterization of the mutant proteins demonstrated that: (i) both O-glycosylation sites of HB-EGF are utilized, (ii) HB-EGF secretion does not require O-glycosylation, (iii) removal of O-glycans does not affect proteolytic cleavage of the HB-EGF precursor, nor does it influence HB-EGF intracellular trafficking or subcellular localization, and (iv) HB-EGF produced by HeLa cells is heavily sialylated.
11769972	2	39	theme	HeLa	233:236	arg1	cells					238:242	HeLa cells	233:242	HeLa cells infected with a recombinant vaccinia virus expressing human HB-EGF	233:309	HeLa cells infected with a recombinant vaccinia virus expressing human HB-EGF produced a secreted, bioactive protein, with Mr 22,000 that was decreased to 14,000 by treatment with O-glycanase.
11769972	4	40	theme	proteins	690:697	arg1	characterization					659:674	characterization	659:674	characterization	659:674	Purification and characterization of the mutant proteins demonstrated that: (i) both O-glycosylation sites of HB-EGF are utilized, (ii) HB-EGF secretion does not require O-glycosylation, (iii) removal of O-glycans does not affect proteolytic cleavage of the HB-EGF precursor, nor does it influence HB-EGF intracellular trafficking or subcellular localization, and (iv) HB-EGF produced by HeLa cells is heavily sialylated.
11769972	4	40	theme	proteins	690:697	arg1	Purification					642:653	Purification	642:653	Purification	642:653	Purification and characterization of the mutant proteins demonstrated that: (i) both O-glycosylation sites of HB-EGF are utilized, (ii) HB-EGF secretion does not require O-glycosylation, (iii) removal of O-glycans does not affect proteolytic cleavage of the HB-EGF precursor, nor does it influence HB-EGF intracellular trafficking or subcellular localization, and (iv) HB-EGF produced by HeLa cells is heavily sialylated.
11769972	1	41	theme	kDa	204:206	arg1	protein					224:230	a 22 kDa, O-glycosylated protein	199:230	a 22 kDa, O-glycosylated protein	199:230	Heparin-binding epidermal growth factor-like growth factor (HB-EGF) is a 22 kDa, O-glycosylated protein.
11769972	1	41	theme	kDa	204:206	arg1	factor					180:185	Heparin-binding epidermal growth factor-like growth factor	128:185	Heparin-binding epidermal growth factor-like growth factor (HB-EGF)	128:194	Heparin-binding epidermal growth factor-like growth factor (HB-EGF) is a 22 kDa, O-glycosylated protein.
11769972	0	42	theme	EGF-like	45:52	arg1	HB-EGF					69:74	HB-EGF	69:74	HB-EGF	69:74	Site-directed mutagenesis of heparin-binding EGF-like growth factor (HB-EGF): analysis of O-glycosylation sites and properties.
11769972	0	42	theme	EGF-like	45:52	arg1	factor					61:66	heparin-binding EGF-like growth factor	29:66	heparin-binding EGF-like growth factor (HB-EGF)	29:75	Site-directed mutagenesis of heparin-binding EGF-like growth factor (HB-EGF): analysis of O-glycosylation sites and properties.
11769972	5	43	theme	significant	1139:1149	arg1	differences					1160:1170	no significant apparent differences	1136:1170	no significant apparent differences in receptor binding activity	1136:1199	Comparisons between glycosylation mutants and wild-type HB-EGF revealed no significant apparent differences in receptor binding activity.
11769972	3	44	theme	HB-EGF	455:460	arg1	cDNA					462:465	HB-EGF cDNA	455:465	HB-EGF cDNA using oligonucleotide- and PCR-directed techniques	455:516	Site-directed mutagenesis of HB-EGF cDNA using oligonucleotide- and PCR-directed techniques was performed to change the potential glycosylation sites, Thr75 and Thr85, to alanine residues to prevent O-glycosylation.
11769972	5	45	theme	apparent	1151:1158	arg1	differences					1160:1170	no significant apparent differences	1136:1170	no significant apparent differences in receptor binding activity	1136:1199	Comparisons between glycosylation mutants and wild-type HB-EGF revealed no significant apparent differences in receptor binding activity.
11769972	3	46	theme	PCR-directed	494:505	arg1	techniques					507:516	oligonucleotide- and PCR-directed techniques	473:516	oligonucleotide- and PCR-directed techniques	473:516	Site-directed mutagenesis of HB-EGF cDNA using oligonucleotide- and PCR-directed techniques was performed to change the potential glycosylation sites, Thr75 and Thr85, to alanine residues to prevent O-glycosylation.
11769972	0	47	theme	factor	61:66	arg1	mutagenesis					14:24	Site-directed mutagenesis	0:24	Site-directed mutagenesis of heparin-binding EGF-like growth factor (HB-EGF): analysis of O-glycosylation sites and properties.	0:126	Site-directed mutagenesis of heparin-binding EGF-like growth factor (HB-EGF): analysis of O-glycosylation sites and properties.
11769972	4	48	theme	proteolytic	872:882	arg1	cleavage					884:891	proteolytic cleavage	872:891	proteolytic cleavage of the HB-EGF precursor	872:915	Purification and characterization of the mutant proteins demonstrated that: (i) both O-glycosylation sites of HB-EGF are utilized, (ii) HB-EGF secretion does not require O-glycosylation, (iii) removal of O-glycans does not affect proteolytic cleavage of the HB-EGF precursor, nor does it influence HB-EGF intracellular trafficking or subcellular localization, and (iv) HB-EGF produced by HeLa cells is heavily sialylated.
11769972	1	49	theme	factor-like	161:171	arg1	HB-EGF					188:193	HB-EGF	188:193	HB-EGF	188:193	Heparin-binding epidermal growth factor-like growth factor (HB-EGF) is a 22 kDa, O-glycosylated protein.
11769972	1	49	theme	factor-like	161:171	arg1	protein					224:230	a 22 kDa, O-glycosylated protein	199:230	a 22 kDa, O-glycosylated protein	199:230	Heparin-binding epidermal growth factor-like growth factor (HB-EGF) is a 22 kDa, O-glycosylated protein.
11769972	1	49	theme	factor-like	161:171	arg1	factor					180:185	Heparin-binding epidermal growth factor-like growth factor	128:185	Heparin-binding epidermal growth factor-like growth factor (HB-EGF)	128:194	Heparin-binding epidermal growth factor-like growth factor (HB-EGF) is a 22 kDa, O-glycosylated protein.
11769972	1	50	dep	kDa	204:206	arg1	O-glycosylated					209:222	O-glycosylated	209:222	O-glycosylated	209:222	Heparin-binding epidermal growth factor-like growth factor (HB-EGF) is a 22 kDa, O-glycosylated protein.
11769972	1	51	theme	Heparin-binding	128:142	arg1	HB-EGF					188:193	HB-EGF	188:193	HB-EGF	188:193	Heparin-binding epidermal growth factor-like growth factor (HB-EGF) is a 22 kDa, O-glycosylated protein.
11769972	1	51	theme	Heparin-binding	128:142	arg1	protein					224:230	a 22 kDa, O-glycosylated protein	199:230	a 22 kDa, O-glycosylated protein	199:230	Heparin-binding epidermal growth factor-like growth factor (HB-EGF) is a 22 kDa, O-glycosylated protein.
11769972	1	51	theme	Heparin-binding	128:142	arg1	factor					180:185	Heparin-binding epidermal growth factor-like growth factor	128:185	Heparin-binding epidermal growth factor-like growth factor (HB-EGF)	128:194	Heparin-binding epidermal growth factor-like growth factor (HB-EGF) is a 22 kDa, O-glycosylated protein.
11769972	3	52	theme	potential	546:554	arg1	Thr75					577:581	Thr75	577:581	Thr75	577:581	Site-directed mutagenesis of HB-EGF cDNA using oligonucleotide- and PCR-directed techniques was performed to change the potential glycosylation sites, Thr75 and Thr85, to alanine residues to prevent O-glycosylation.
11769972	3	52	theme	potential	546:554	arg1	sites					570:574	the potential glycosylation sites	542:574	the potential glycosylation sites	542:574	Site-directed mutagenesis of HB-EGF cDNA using oligonucleotide- and PCR-directed techniques was performed to change the potential glycosylation sites, Thr75 and Thr85, to alanine residues to prevent O-glycosylation.
11769972	3	52	theme	potential	546:554	arg1	Thr85					587:591	Thr85	587:591	Thr85	587:591	Site-directed mutagenesis of HB-EGF cDNA using oligonucleotide- and PCR-directed techniques was performed to change the potential glycosylation sites, Thr75 and Thr85, to alanine residues to prevent O-glycosylation.
11769972	4	53	theme	HB-EGF	778:783	arg1	secretion					785:793	(ii) HB-EGF secretion	773:793	(ii) HB-EGF secretion	773:793	Purification and characterization of the mutant proteins demonstrated that: (i) both O-glycosylation sites of HB-EGF are utilized, (ii) HB-EGF secretion does not require O-glycosylation, (iii) removal of O-glycans does not affect proteolytic cleavage of the HB-EGF precursor, nor does it influence HB-EGF intracellular trafficking or subcellular localization, and (iv) HB-EGF produced by HeLa cells is heavily sialylated.
11769972	1	54	theme	epidermal	144:152	arg1	HB-EGF					188:193	HB-EGF	188:193	HB-EGF	188:193	Heparin-binding epidermal growth factor-like growth factor (HB-EGF) is a 22 kDa, O-glycosylated protein.
11769972	1	54	theme	epidermal	144:152	arg1	protein					224:230	a 22 kDa, O-glycosylated protein	199:230	a 22 kDa, O-glycosylated protein	199:230	Heparin-binding epidermal growth factor-like growth factor (HB-EGF) is a 22 kDa, O-glycosylated protein.
11769972	1	54	theme	epidermal	144:152	arg1	factor					180:185	Heparin-binding epidermal growth factor-like growth factor	128:185	Heparin-binding epidermal growth factor-like growth factor (HB-EGF)	128:194	Heparin-binding epidermal growth factor-like growth factor (HB-EGF) is a 22 kDa, O-glycosylated protein.
11769972	3	55	theme	oligonucleotide-	473:488	arg1	techniques					507:516	oligonucleotide- and PCR-directed techniques	473:516	oligonucleotide- and PCR-directed techniques	473:516	Site-directed mutagenesis of HB-EGF cDNA using oligonucleotide- and PCR-directed techniques was performed to change the potential glycosylation sites, Thr75 and Thr85, to alanine residues to prevent O-glycosylation.
11769972	0	56	dep	mutagenesis	14:24	arg1	analysis					78:85	analysis	78:85	Site-directed mutagenesis of heparin-binding EGF-like growth factor (HB-EGF): analysis of O-glycosylation sites and properties.	0:126	Site-directed mutagenesis of heparin-binding EGF-like growth factor (HB-EGF): analysis of O-glycosylation sites and properties.
11769972	1	57	theme	growth	154:159	arg1	HB-EGF					188:193	HB-EGF	188:193	HB-EGF	188:193	Heparin-binding epidermal growth factor-like growth factor (HB-EGF) is a 22 kDa, O-glycosylated protein.
11769972	1	57	theme	growth	154:159	arg1	protein					224:230	a 22 kDa, O-glycosylated protein	199:230	a 22 kDa, O-glycosylated protein	199:230	Heparin-binding epidermal growth factor-like growth factor (HB-EGF) is a 22 kDa, O-glycosylated protein.
11769972	1	57	theme	growth	154:159	arg1	factor					180:185	Heparin-binding epidermal growth factor-like growth factor	128:185	Heparin-binding epidermal growth factor-like growth factor (HB-EGF)	128:194	Heparin-binding epidermal growth factor-like growth factor (HB-EGF) is a 22 kDa, O-glycosylated protein.
11769972	4	58	theme	intracellular	947:959	arg1	trafficking					961:971	HB-EGF intracellular trafficking	940:971	HB-EGF intracellular trafficking	940:971	Purification and characterization of the mutant proteins demonstrated that: (i) both O-glycosylation sites of HB-EGF are utilized, (ii) HB-EGF secretion does not require O-glycosylation, (iii) removal of O-glycans does not affect proteolytic cleavage of the HB-EGF precursor, nor does it influence HB-EGF intracellular trafficking or subcellular localization, and (iv) HB-EGF produced by HeLa cells is heavily sialylated.
11769972	5	59	theme	wild-type	1110:1118	arg1	HB-EGF					1120:1125	wild-type HB-EGF	1110:1125	wild-type HB-EGF	1110:1125	Comparisons between glycosylation mutants and wild-type HB-EGF revealed no significant apparent differences in receptor binding activity.
11769972	2	60	theme	Mr	356:357	arg1	22,000					359:364	Mr 22,000	356:364	Mr 22,000 that was decreased to 14,000 by treatment with O-glycanase	356:423	HeLa cells infected with a recombinant vaccinia virus expressing human HB-EGF produced a secreted, bioactive protein, with Mr 22,000 that was decreased to 14,000 by treatment with O-glycanase.
11769972	4	61	theme	HeLa	1030:1033	arg1	cells					1035:1039	HeLa cells	1030:1039	HeLa cells	1030:1039	Purification and characterization of the mutant proteins demonstrated that: (i) both O-glycosylation sites of HB-EGF are utilized, (ii) HB-EGF secretion does not require O-glycosylation, (iii) removal of O-glycans does not affect proteolytic cleavage of the HB-EGF precursor, nor does it influence HB-EGF intracellular trafficking or subcellular localization, and (iv) HB-EGF produced by HeLa cells is heavily sialylated.
11511810	6	0	theme	N-terminal	972:981	arg1	sites					1009:1013	the N-terminal potential N-glycosylation sites	968:1013	the N-terminal potential N-glycosylation sites	968:1013	We then made a series of mutants, in which the asparagine residues in the N-terminal potential N-glycosylation sites were replaced by glutamine.
11511810	3	1	gly	N-glycosylation	565:579	arg2	sites					581:585	these potential N-glycosylation sites	549:585	these potential N-glycosylation sites	549:585	In the present study, we have analysed the glycosylation of these potential N-glycosylation sites.
11511810	12	2	theme	activity	1894:1901	arg1	expression					1873:1882	expression	1873:1882	expression of enzyme activity	1873:1901	Individually, their glycosylation does not contribute considerably to expression of enzyme activity.
11511810	3	3	gly	glycosylation	532:544	arg1	study					504:508	the present study	492:508	the present study	492:508	In the present study, we have analysed the glycosylation of these potential N-glycosylation sites.
11511810	3	3	gly	glycosylation	532:544	arg1	sites					581:585	these potential N-glycosylation sites	549:585	these potential N-glycosylation sites	549:585	In the present study, we have analysed the glycosylation of these potential N-glycosylation sites.
11511810	10	4	theme	activity	1619:1626	arg1	expression					1593:1602	expression	1593:1602	expression of full enzyme activity of both hFucTV and -VI	1593:1649	In addition, castanospermine treatment diminished the enzyme activity and hence trimming of the N-linked glycans are required for expression of full enzyme activity of both hFucTV and -VI.
11511810	5	5	theme	molecular	766:774	arg1	mass					776:779	molecular mass	766:779	molecular mass	766:779	The difference in molecular mass between the proteins in treated and untreated cells corresponded to the presence of at least three N-linked glycans.
11511810	12	6	gly	glycosylation	1823:1835	arg1	activity					1894:1901	enzyme activity	1887:1901	enzyme activity	1887:1901	Individually, their glycosylation does not contribute considerably to expression of enzyme activity.
11511810	8	7	theme	double	1243:1248	arg1	mutant					1250:1255	the hFucTVI N46Q/N91Q double mutant	1221:1255	the hFucTVI N46Q/N91Q double mutant	1221:1255	All the single mutants and the hFucTVI N46Q/N91Q double mutant exhibited enzyme activities that did not differ considerably from the wt activities.
11511810	11	8	theme	present	1656:1662	arg1	study					1664:1668	The present study	1652:1668	The present study	1652:1668	The present study demonstrates that both of the N-terminal potential N-glycosylation sites in hFucTV and one of the sites in hFucTVI are glycosylated.
11511810	13	9	from	elimination	1913:1923	arg1	hFucTV					1942:1947	hFucTV	1942:1947	hFucTV	1942:1947	However, elimination of both sites in hFucTV reduces the enzyme activity.
11511810	8	10	theme	wt	1327:1328	arg1	activities					1330:1339	the wt activities	1323:1339	the wt activities	1323:1339	All the single mutants and the hFucTVI N46Q/N91Q double mutant exhibited enzyme activities that did not differ considerably from the wt activities.
11511810	11	11	theme	sites	1768:1772	arg1	sites					1768:1772	the sites	1764:1772	the sites in hFucTVI	1764:1783	The present study demonstrates that both of the N-terminal potential N-glycosylation sites in hFucTV and one of the sites in hFucTVI are glycosylated.
11511810	11	11	theme	sites	1768:1772	arg1	hFucTV					1746:1751	hFucTV	1746:1751	hFucTV	1746:1751	The present study demonstrates that both of the N-terminal potential N-glycosylation sites in hFucTV and one of the sites in hFucTVI are glycosylated.
11511810	10	12	theme	castanospermine	1476:1490	arg1	treatment					1492:1500	castanospermine treatment	1476:1500	castanospermine treatment	1476:1500	In addition, castanospermine treatment diminished the enzyme activity and hence trimming of the N-linked glycans are required for expression of full enzyme activity of both hFucTV and -VI.
11511810	4	13	from	proteins	719:726	arg1	cells					741:745	untreated cells	731:745	untreated cells	731:745	Initially, we compared the molecular mass of hFucTV and -VI expressed in COS-7 cells treated with tunicamycin with the mass of the proteins in untreated cells.
11511810	5	14	theme	untreated	817:825	arg1	cells					827:831	treated and untreated cells	805:831	treated and untreated cells	805:831	The difference in molecular mass between the proteins in treated and untreated cells corresponded to the presence of at least three N-linked glycans.
11511810	8	15	theme	enzyme	1267:1272	arg1	activities					1274:1283	enzyme activities	1267:1283	enzyme activities that did not differ considerably from the wt activities	1267:1339	All the single mutants and the hFucTVI N46Q/N91Q double mutant exhibited enzyme activities that did not differ considerably from the wt activities.
11511810	9	16	theme	N60Q/N105Q	1385:1394	arg1	mutant					1403:1408	the hFucTV N60Q/N105Q double mutant	1374:1408	the hFucTV N60Q/N105Q double mutant	1374:1408	However, the enzyme activity of the hFucTV N60Q/N105Q double mutant was reduced to approximately 40% of the wt activity.
11511810	1	17	dep	hFucTV	245:250	arg1	Asn198					279:284	Asn198	279:284	Asn198	279:284	Human alpha1,3-fucosyltransferase V and -VI (hFucTV and -VI) each contain four potential N-glycosylation sites (hFucTV: Asn60, Asn105, Asn167 and Asn198 and hFucTVI: Asn46, Asn91, Asn153 and Asn184).
11511810	1	17	dep	hFucTV	245:250	arg1	Asn153					313:318	Asn153	313:318	Asn153	313:318	Human alpha1,3-fucosyltransferase V and -VI (hFucTV and -VI) each contain four potential N-glycosylation sites (hFucTV: Asn60, Asn105, Asn167 and Asn198 and hFucTVI: Asn46, Asn91, Asn153 and Asn184).
11511810	1	17	dep	hFucTV	245:250	arg1	Asn184					324:329	Asn184	324:329	Asn184	324:329	Human alpha1,3-fucosyltransferase V and -VI (hFucTV and -VI) each contain four potential N-glycosylation sites (hFucTV: Asn60, Asn105, Asn167 and Asn198 and hFucTVI: Asn46, Asn91, Asn153 and Asn184).
11511810	1	17	dep	hFucTV	245:250	arg1	Asn167					268:273	Asn167	268:273	Asn167	268:273	Human alpha1,3-fucosyltransferase V and -VI (hFucTV and -VI) each contain four potential N-glycosylation sites (hFucTV: Asn60, Asn105, Asn167 and Asn198 and hFucTVI: Asn46, Asn91, Asn153 and Asn184).
11511810	1	17	dep	hFucTV	245:250	arg1	Asn46					299:303	Asn46	299:303	Asn46	299:303	Human alpha1,3-fucosyltransferase V and -VI (hFucTV and -VI) each contain four potential N-glycosylation sites (hFucTV: Asn60, Asn105, Asn167 and Asn198 and hFucTVI: Asn46, Asn91, Asn153 and Asn184).
11511810	1	17	dep	hFucTV	245:250	arg1	Asn91					306:310	Asn91	306:310	Asn91	306:310	Human alpha1,3-fucosyltransferase V and -VI (hFucTV and -VI) each contain four potential N-glycosylation sites (hFucTV: Asn60, Asn105, Asn167 and Asn198 and hFucTVI: Asn46, Asn91, Asn153 and Asn184).
11511810	1	17	dep	hFucTV	245:250	arg1	Asn60					253:257	Asn60	253:257	Asn60	253:257	Human alpha1,3-fucosyltransferase V and -VI (hFucTV and -VI) each contain four potential N-glycosylation sites (hFucTV: Asn60, Asn105, Asn167 and Asn198 and hFucTVI: Asn46, Asn91, Asn153 and Asn184).
11511810	10	18	theme	N-linked	1559:1566	arg1	glycans					1568:1574	the N-linked glycans	1555:1574	the N-linked glycans are required for expression of full enzyme activity of both hFucTV and -VI	1555:1649	In addition, castanospermine treatment diminished the enzyme activity and hence trimming of the N-linked glycans are required for expression of full enzyme activity of both hFucTV and -VI.
11511810	9	19	theme	mutant	1403:1408	arg1	activity					1362:1369	the enzyme activity	1351:1369	the enzyme activity of the hFucTV N60Q/N105Q double mutant	1351:1408	However, the enzyme activity of the hFucTV N60Q/N105Q double mutant was reduced to approximately 40% of the wt activity.
11511810	4	20	theme	molecular	615:623	arg1	mass					625:628	the molecular mass	611:628	the molecular mass of hFucTV and -VI expressed in COS-7 cells treated with tunicamycin with the mass of the proteins in untreated cells	611:745	Initially, we compared the molecular mass of hFucTV and -VI expressed in COS-7 cells treated with tunicamycin with the mass of the proteins in untreated cells.
11511810	0	21	theme	alpha1,3-fucosyltransferase	77:103	arg1	V					105:105	the human alpha1,3-fucosyltransferase V	67:105	the human alpha1,3-fucosyltransferase V	67:105	Glycosylation of the N-terminal potential N-glycosylation sites in the human alpha1,3-fucosyltransferase V and -VI (hFucTV and -VI).
11511810	7	22	gly	glycosylated	1180:1191	arg1	hFucTVI					1138:1144	hFucTVI	1138:1144	hFucTVI	1138:1144	Western blotting analyses demonstrated that both sites in hFucTV were glycosylated, whereas in hFucTVI only one of the sites (Asn91) was glycosylated.
11511810	7	22	gly	glycosylated	1180:1191	arg1	one					1151:1153	one	1151:1153	one	1151:1153	Western blotting analyses demonstrated that both sites in hFucTV were glycosylated, whereas in hFucTVI only one of the sites (Asn91) was glycosylated.
11511810	7	22	gly	glycosylated	1180:1191	arg2	sites					1162:1166	the sites	1158:1166	the sites (Asn91)	1158:1174	Western blotting analyses demonstrated that both sites in hFucTV were glycosylated, whereas in hFucTVI only one of the sites (Asn91) was glycosylated.
11511810	7	22	gly	glycosylated	1180:1191	arg2	Asn91					1169:1173	Asn91	1169:1173	Asn91	1169:1173	Western blotting analyses demonstrated that both sites in hFucTV were glycosylated, whereas in hFucTVI only one of the sites (Asn91) was glycosylated.
11511810	7	22	gly	glycosylated	1180:1191	arg1	sites					1162:1166	the sites	1158:1166	the sites (Asn91)	1158:1174	Western blotting analyses demonstrated that both sites in hFucTV were glycosylated, whereas in hFucTVI only one of the sites (Asn91) was glycosylated.
11511810	7	22	gly	glycosylated	1180:1191	arg2	one					1151:1153	one	1151:1153	one	1151:1153	Western blotting analyses demonstrated that both sites in hFucTV were glycosylated, whereas in hFucTVI only one of the sites (Asn91) was glycosylated.
11511810	7	22	gly	glycosylated	1180:1191	arg1	Asn91					1169:1173	Asn91	1169:1173	Asn91	1169:1173	Western blotting analyses demonstrated that both sites in hFucTV were glycosylated, whereas in hFucTVI only one of the sites (Asn91) was glycosylated.
11511810	5	23	theme	treated	805:811	arg1	cells					827:831	treated and untreated cells	805:831	treated and untreated cells	805:831	The difference in molecular mass between the proteins in treated and untreated cells corresponded to the presence of at least three N-linked glycans.
11511810	0	24	from	Glycosylation	0:12	arg1	V					105:105	the human alpha1,3-fucosyltransferase V	67:105	the human alpha1,3-fucosyltransferase V	67:105	Glycosylation of the N-terminal potential N-glycosylation sites in the human alpha1,3-fucosyltransferase V and -VI (hFucTV and -VI).
11511810	11	25	gly	N-glycosylation	1721:1735	arg2	sites					1737:1741	the N-terminal potential N-glycosylation sites	1696:1741	the N-terminal potential N-glycosylation sites in hFucTV and one of the sites in hFucTVI	1696:1783	The present study demonstrates that both of the N-terminal potential N-glycosylation sites in hFucTV and one of the sites in hFucTVI are glycosylated.
11511810	0	26	from	sites	58:62	arg1	V					105:105	the human alpha1,3-fucosyltransferase V	67:105	the human alpha1,3-fucosyltransferase V	67:105	Glycosylation of the N-terminal potential N-glycosylation sites in the human alpha1,3-fucosyltransferase V and -VI (hFucTV and -VI).
11511810	2	27	gly	Glycosylation	333:345	arg1	sites					395:399	the two N-terminal potential N-glycosylation sites	350:399	the two N-terminal potential N-glycosylation sites (hFucTV: Asn60, Asn105 and hFucTVI: Asn46 and Asn91)	350:452	Glycosylation of the two N-terminal potential N-glycosylation sites (hFucTV: Asn60, Asn105 and hFucTVI: Asn46 and Asn91) have never been studied in detail.
11511810	2	27	gly	Glycosylation	333:345	arg1	detail					481:486	detail	481:486	detail	481:486	Glycosylation of the two N-terminal potential N-glycosylation sites (hFucTV: Asn60, Asn105 and hFucTVI: Asn46 and Asn91) have never been studied in detail.
11511810	8	28	theme	N46Q/N91Q	1233:1241	arg1	mutant					1250:1255	the hFucTVI N46Q/N91Q double mutant	1221:1255	the hFucTVI N46Q/N91Q double mutant	1221:1255	All the single mutants and the hFucTVI N46Q/N91Q double mutant exhibited enzyme activities that did not differ considerably from the wt activities.
11511810	13	29	theme	sites	1933:1937	arg1	elimination					1913:1923	elimination	1913:1923	elimination of both sites in hFucTV	1913:1947	However, elimination of both sites in hFucTV reduces the enzyme activity.
11511810	0	30	theme	N-glycosylation	42:56	arg1	sites					58:62	the N-terminal potential N-glycosylation sites	17:62	the N-terminal potential N-glycosylation sites in the human alpha1,3-fucosyltransferase V	17:105	Glycosylation of the N-terminal potential N-glycosylation sites in the human alpha1,3-fucosyltransferase V and -VI (hFucTV and -VI).
11511810	5	31	theme	N-linked	880:887	arg1	glycans					889:895	at least three N-linked glycans	865:895	at least three N-linked glycans	865:895	The difference in molecular mass between the proteins in treated and untreated cells corresponded to the presence of at least three N-linked glycans.
11511810	2	32	theme	sites	395:399	arg1	Glycosylation					333:345	Glycosylation	333:345	Glycosylation of the two N-terminal potential N-glycosylation sites (hFucTV: Asn60, Asn105 and hFucTVI: Asn46 and Asn91)	333:452	Glycosylation of the two N-terminal potential N-glycosylation sites (hFucTV: Asn60, Asn105 and hFucTVI: Asn46 and Asn91) have never been studied in detail.
11511810	7	33	dep	glycosylated	1113:1124	arg1	whereas					1127:1133	whereas	1127:1133	whereas	1127:1133	Western blotting analyses demonstrated that both sites in hFucTV were glycosylated, whereas in hFucTVI only one of the sites (Asn91) was glycosylated.
11511810	4	34	theme	COS-7	661:665	arg1	cells					667:671	COS-7 cells	661:671	COS-7 cells treated with tunicamycin with the mass of the proteins in untreated cells	661:745	Initially, we compared the molecular mass of hFucTV and -VI expressed in COS-7 cells treated with tunicamycin with the mass of the proteins in untreated cells.
11511810	2	35	theme	potential	369:377	arg1	sites					395:399	the two N-terminal potential N-glycosylation sites	350:399	the two N-terminal potential N-glycosylation sites (hFucTV: Asn60, Asn105 and hFucTVI: Asn46 and Asn91)	350:452	Glycosylation of the two N-terminal potential N-glycosylation sites (hFucTV: Asn60, Asn105 and hFucTVI: Asn46 and Asn91) have never been studied in detail.
11511810	11	36	from	sites	1768:1772	arg1	hFucTVI					1777:1783	hFucTVI	1777:1783	hFucTVI	1777:1783	The present study demonstrates that both of the N-terminal potential N-glycosylation sites in hFucTV and one of the sites in hFucTVI are glycosylated.
11511810	9	37	theme	activity	1453:1460	arg1	%					1441:1441	approximately 40%	1425:1441	approximately 40% of the wt activity	1425:1460	However, the enzyme activity of the hFucTV N60Q/N105Q double mutant was reduced to approximately 40% of the wt activity.
11511810	9	37	theme	activity	1453:1460	arg1	activity					1453:1460	the wt activity	1446:1460	the wt activity	1446:1460	However, the enzyme activity of the hFucTV N60Q/N105Q double mutant was reduced to approximately 40% of the wt activity.
11511810	1	38	theme	Human	133:137	arg1	V					167:167	Human alpha1,3-fucosyltransferase V	133:167	Human alpha1,3-fucosyltransferase V	133:167	Human alpha1,3-fucosyltransferase V and -VI (hFucTV and -VI) each contain four potential N-glycosylation sites (hFucTV: Asn60, Asn105, Asn167 and Asn198 and hFucTVI: Asn46, Asn91, Asn153 and Asn184).
11511810	3	39	theme	N-glycosylation	565:579	arg1	sites					581:585	these potential N-glycosylation sites	549:585	these potential N-glycosylation sites	549:585	In the present study, we have analysed the glycosylation of these potential N-glycosylation sites.
11511810	4	40	theme	proteins	719:726	arg1	mass					707:710	the mass	703:710	the mass of the proteins in untreated cells	703:745	Initially, we compared the molecular mass of hFucTV and -VI expressed in COS-7 cells treated with tunicamycin with the mass of the proteins in untreated cells.
11511810	0	41	theme	potential	32:40	arg1	sites					58:62	the N-terminal potential N-glycosylation sites	17:62	the N-terminal potential N-glycosylation sites in the human alpha1,3-fucosyltransferase V	17:105	Glycosylation of the N-terminal potential N-glycosylation sites in the human alpha1,3-fucosyltransferase V and -VI (hFucTV and -VI).
11511810	7	42	theme	blotting	1051:1058	arg1	analyses					1060:1067	Western blotting analyses	1043:1067	Western blotting analyses	1043:1067	Western blotting analyses demonstrated that both sites in hFucTV were glycosylated, whereas in hFucTVI only one of the sites (Asn91) was glycosylated.
11511810	6	43	theme	mutants	923:929	arg1	series					913:918	a series	911:918	a series	911:918	We then made a series of mutants, in which the asparagine residues in the N-terminal potential N-glycosylation sites were replaced by glutamine.
11511810	4	44	theme	untreated	731:739	arg1	cells					741:745	untreated cells	731:745	untreated cells	731:745	Initially, we compared the molecular mass of hFucTV and -VI expressed in COS-7 cells treated with tunicamycin with the mass of the proteins in untreated cells.
11511810	0	45	theme	sites	58:62	arg1	-VI					111:113	-VI	111:113	-VI (hFucTV and -VI)	111:130	Glycosylation of the N-terminal potential N-glycosylation sites in the human alpha1,3-fucosyltransferase V and -VI (hFucTV and -VI).
11511810	0	45	theme	sites	58:62	arg1	Glycosylation					0:12	Glycosylation	0:12	Glycosylation of the N-terminal potential N-glycosylation sites in the human alpha1,3-fucosyltransferase V	0:105	Glycosylation of the N-terminal potential N-glycosylation sites in the human alpha1,3-fucosyltransferase V and -VI (hFucTV and -VI).
11511810	11	46	theme	potential	1711:1719	arg1	sites					1737:1741	the N-terminal potential N-glycosylation sites	1696:1741	the N-terminal potential N-glycosylation sites in hFucTV and one of the sites in hFucTVI	1696:1783	The present study demonstrates that both of the N-terminal potential N-glycosylation sites in hFucTV and one of the sites in hFucTVI are glycosylated.
11511810	0	47	gly	N-glycosylation	42:56	arg2	sites					58:62	the N-terminal potential N-glycosylation sites	17:62	the N-terminal potential N-glycosylation sites in the human alpha1,3-fucosyltransferase V	17:105	Glycosylation of the N-terminal potential N-glycosylation sites in the human alpha1,3-fucosyltransferase V and -VI (hFucTV and -VI).
11511810	7	48	theme	sites	1162:1166	arg1	one					1151:1153	one	1151:1153	one	1151:1153	Western blotting analyses demonstrated that both sites in hFucTV were glycosylated, whereas in hFucTVI only one of the sites (Asn91) was glycosylated.
11511810	7	48	theme	sites	1162:1166	arg1	sites					1162:1166	the sites	1158:1166	the sites (Asn91)	1158:1174	Western blotting analyses demonstrated that both sites in hFucTV were glycosylated, whereas in hFucTVI only one of the sites (Asn91) was glycosylated.
11511810	7	48	theme	sites	1162:1166	arg1	Asn91					1169:1173	Asn91	1169:1173	Asn91	1169:1173	Western blotting analyses demonstrated that both sites in hFucTV were glycosylated, whereas in hFucTVI only one of the sites (Asn91) was glycosylated.
11511810	10	49	theme	enzyme	1612:1617	arg1	activity					1619:1626	full enzyme activity	1607:1626	full enzyme activity of both hFucTV and -VI	1607:1649	In addition, castanospermine treatment diminished the enzyme activity and hence trimming of the N-linked glycans are required for expression of full enzyme activity of both hFucTV and -VI.
11511810	1	50	theme	N-glycosylation	222:236	arg1	sites					238:242	four potential N-glycosylation sites	207:242	four potential N-glycosylation sites	207:242	Human alpha1,3-fucosyltransferase V and -VI (hFucTV and -VI) each contain four potential N-glycosylation sites (hFucTV: Asn60, Asn105, Asn167 and Asn198 and hFucTVI: Asn46, Asn91, Asn153 and Asn184).
11511810	10	51	dep	glycans	1568:1574	arg1	required					1580:1587	required	1580:1587	are required for expression of full enzyme activity of both hFucTV and -VI	1576:1649	In addition, castanospermine treatment diminished the enzyme activity and hence trimming of the N-linked glycans are required for expression of full enzyme activity of both hFucTV and -VI.
11511810	6	52	theme	potential	983:991	arg1	sites					1009:1013	the N-terminal potential N-glycosylation sites	968:1013	the N-terminal potential N-glycosylation sites	968:1013	We then made a series of mutants, in which the asparagine residues in the N-terminal potential N-glycosylation sites were replaced by glutamine.
11511810	1	53	dep	-VI	173:175	arg1	hFucTV					178:183	hFucTV	178:183	hFucTV	178:183	Human alpha1,3-fucosyltransferase V and -VI (hFucTV and -VI) each contain four potential N-glycosylation sites (hFucTV: Asn60, Asn105, Asn167 and Asn198 and hFucTVI: Asn46, Asn91, Asn153 and Asn184).
11511810	1	53	dep	-VI	173:175	arg1	-VI					189:191	-VI	189:191	-VI	189:191	Human alpha1,3-fucosyltransferase V and -VI (hFucTV and -VI) each contain four potential N-glycosylation sites (hFucTV: Asn60, Asn105, Asn167 and Asn198 and hFucTVI: Asn46, Asn91, Asn153 and Asn184).
11511810	10	54	theme	hFucTV	1636:1641	arg1	activity					1619:1626	full enzyme activity	1607:1626	full enzyme activity of both hFucTV and -VI	1607:1649	In addition, castanospermine treatment diminished the enzyme activity and hence trimming of the N-linked glycans are required for expression of full enzyme activity of both hFucTV and -VI.
11511810	5	55	link	N-linked	880:887	arg1	glycans					889:895	at least three N-linked glycans	865:895	at least three N-linked glycans	865:895	The difference in molecular mass between the proteins in treated and untreated cells corresponded to the presence of at least three N-linked glycans.
11511810	6	56	from	residues	956:963	arg1	sites					1009:1013	the N-terminal potential N-glycosylation sites	968:1013	the N-terminal potential N-glycosylation sites	968:1013	We then made a series of mutants, in which the asparagine residues in the N-terminal potential N-glycosylation sites were replaced by glutamine.
11511810	12	57	theme	enzyme	1887:1892	arg1	activity					1894:1901	enzyme activity	1887:1901	enzyme activity	1887:1901	Individually, their glycosylation does not contribute considerably to expression of enzyme activity.
11511810	6	58	gly	N-glycosylation	993:1007	arg2	sites					1009:1013	the N-terminal potential N-glycosylation sites	968:1013	the N-terminal potential N-glycosylation sites	968:1013	We then made a series of mutants, in which the asparagine residues in the N-terminal potential N-glycosylation sites were replaced by glutamine.
11511810	10	59	theme	-VI	1647:1649	arg1	activity					1619:1626	full enzyme activity	1607:1626	full enzyme activity of both hFucTV and -VI	1607:1649	In addition, castanospermine treatment diminished the enzyme activity and hence trimming of the N-linked glycans are required for expression of full enzyme activity of both hFucTV and -VI.
11511810	7	60	from	sites	1092:1096	arg1	hFucTV					1101:1106	hFucTV	1101:1106	hFucTV	1101:1106	Western blotting analyses demonstrated that both sites in hFucTV were glycosylated, whereas in hFucTVI only one of the sites (Asn91) was glycosylated.
11511810	9	61	theme	enzyme	1355:1360	arg1	activity					1362:1369	the enzyme activity	1351:1369	the enzyme activity of the hFucTV N60Q/N105Q double mutant	1351:1408	However, the enzyme activity of the hFucTV N60Q/N105Q double mutant was reduced to approximately 40% of the wt activity.
11511810	11	62	theme	N-terminal	1700:1709	arg1	sites					1737:1741	the N-terminal potential N-glycosylation sites	1696:1741	the N-terminal potential N-glycosylation sites in hFucTV and one of the sites in hFucTVI	1696:1783	The present study demonstrates that both of the N-terminal potential N-glycosylation sites in hFucTV and one of the sites in hFucTVI are glycosylated.
11511810	3	63	theme	present	496:502	arg1	study					504:508	the present study	492:508	the present study	492:508	In the present study, we have analysed the glycosylation of these potential N-glycosylation sites.
11511810	5	64	from	difference	752:761	arg1	mass					776:779	molecular mass	766:779	molecular mass	766:779	The difference in molecular mass between the proteins in treated and untreated cells corresponded to the presence of at least three N-linked glycans.
11511810	0	65	from	-VI	111:113	arg1	V					105:105	the human alpha1,3-fucosyltransferase V	67:105	the human alpha1,3-fucosyltransferase V	67:105	Glycosylation of the N-terminal potential N-glycosylation sites in the human alpha1,3-fucosyltransferase V and -VI (hFucTV and -VI).
11511810	4	66	theme	hFucTV	633:638	arg1	mass					625:628	the molecular mass	611:628	the molecular mass of hFucTV and -VI expressed in COS-7 cells treated with tunicamycin with the mass of the proteins in untreated cells	611:745	Initially, we compared the molecular mass of hFucTV and -VI expressed in COS-7 cells treated with tunicamycin with the mass of the proteins in untreated cells.
11511810	0	67	theme	human	71:75	arg1	V					105:105	the human alpha1,3-fucosyltransferase V	67:105	the human alpha1,3-fucosyltransferase V	67:105	Glycosylation of the N-terminal potential N-glycosylation sites in the human alpha1,3-fucosyltransferase V and -VI (hFucTV and -VI).
11511810	4	68	from	mass	707:710	arg1	cells					741:745	untreated cells	731:745	untreated cells	731:745	Initially, we compared the molecular mass of hFucTV and -VI expressed in COS-7 cells treated with tunicamycin with the mass of the proteins in untreated cells.
11511810	9	69	theme	double	1396:1401	arg1	mutant					1403:1408	the hFucTV N60Q/N105Q double mutant	1374:1408	the hFucTV N60Q/N105Q double mutant	1374:1408	However, the enzyme activity of the hFucTV N60Q/N105Q double mutant was reduced to approximately 40% of the wt activity.
11511810	2	70	dep	Asn60	410:414	arg1	Asn91					447:451	Asn91	447:451	Asn91	447:451	Glycosylation of the two N-terminal potential N-glycosylation sites (hFucTV: Asn60, Asn105 and hFucTVI: Asn46 and Asn91) have never been studied in detail.
11511810	2	70	dep	Asn60	410:414	arg1	Asn46					437:441	Asn46	437:441	Asn46	437:441	Glycosylation of the two N-terminal potential N-glycosylation sites (hFucTV: Asn60, Asn105 and hFucTVI: Asn46 and Asn91) have never been studied in detail.
11511810	11	71	gly	glycosylated	1789:1800	arg1	sites					1737:1741	the N-terminal potential N-glycosylation sites	1696:1741	the N-terminal potential N-glycosylation sites in hFucTV and one of the sites in hFucTVI	1696:1783	The present study demonstrates that both of the N-terminal potential N-glycosylation sites in hFucTV and one of the sites in hFucTVI are glycosylated.
11511810	11	71	gly	glycosylated	1789:1800	arg1	both					1688:1691	both	1688:1691	both	1688:1691	The present study demonstrates that both of the N-terminal potential N-glycosylation sites in hFucTV and one of the sites in hFucTVI are glycosylated.
11511810	10	72	link	N-linked	1559:1566	arg1	glycans					1568:1574	the N-linked glycans	1555:1574	the N-linked glycans are required for expression of full enzyme activity of both hFucTV and -VI	1555:1649	In addition, castanospermine treatment diminished the enzyme activity and hence trimming of the N-linked glycans are required for expression of full enzyme activity of both hFucTV and -VI.
11511810	8	73	theme	single	1202:1207	arg1	mutants					1209:1215	All the single mutants	1194:1215	All the single mutants	1194:1215	All the single mutants and the hFucTVI N46Q/N91Q double mutant exhibited enzyme activities that did not differ considerably from the wt activities.
11511810	0	74	from	V	105:105	arg1	-VI					111:113	-VI	111:113	-VI (hFucTV and -VI)	111:130	Glycosylation of the N-terminal potential N-glycosylation sites in the human alpha1,3-fucosyltransferase V and -VI (hFucTV and -VI).
11511810	0	74	from	V	105:105	arg1	Glycosylation					0:12	Glycosylation	0:12	Glycosylation of the N-terminal potential N-glycosylation sites in the human alpha1,3-fucosyltransferase V	0:105	Glycosylation of the N-terminal potential N-glycosylation sites in the human alpha1,3-fucosyltransferase V and -VI (hFucTV and -VI).
11511810	13	75	theme	enzyme	1961:1966	arg1	activity					1968:1975	the enzyme activity	1957:1975	the enzyme activity	1957:1975	However, elimination of both sites in hFucTV reduces the enzyme activity.
11511810	11	76	theme	N-glycosylation	1721:1735	arg1	sites					1737:1741	the N-terminal potential N-glycosylation sites	1696:1741	the N-terminal potential N-glycosylation sites in hFucTV and one of the sites in hFucTVI	1696:1783	The present study demonstrates that both of the N-terminal potential N-glycosylation sites in hFucTV and one of the sites in hFucTVI are glycosylated.
11511810	2	77	dep	sites	395:399	arg1	hFucTV					402:407	hFucTV	402:407	hFucTV	402:407	Glycosylation of the two N-terminal potential N-glycosylation sites (hFucTV: Asn60, Asn105 and hFucTVI: Asn46 and Asn91) have never been studied in detail.
11511810	1	78	gly	N-glycosylation	222:236	arg2	four					207:210	four	207:210	four	207:210	Human alpha1,3-fucosyltransferase V and -VI (hFucTV and -VI) each contain four potential N-glycosylation sites (hFucTV: Asn60, Asn105, Asn167 and Asn198 and hFucTVI: Asn46, Asn91, Asn153 and Asn184).
11511810	1	78	gly	N-glycosylation	222:236	arg2	sites					238:242	four potential N-glycosylation sites	207:242	four potential N-glycosylation sites	207:242	Human alpha1,3-fucosyltransferase V and -VI (hFucTV and -VI) each contain four potential N-glycosylation sites (hFucTV: Asn60, Asn105, Asn167 and Asn198 and hFucTVI: Asn46, Asn91, Asn153 and Asn184).
11511810	0	79	dep	-VI	111:113	arg1	-VI					127:129	-VI	127:129	-VI	127:129	Glycosylation of the N-terminal potential N-glycosylation sites in the human alpha1,3-fucosyltransferase V and -VI (hFucTV and -VI).
11511810	0	79	dep	-VI	111:113	arg1	hFucTV					116:121	hFucTV	116:121	hFucTV	116:121	Glycosylation of the N-terminal potential N-glycosylation sites in the human alpha1,3-fucosyltransferase V and -VI (hFucTV and -VI).
11511810	4	80	from	cells	741:745	arg1	mass					707:710	the mass	703:710	the mass of the proteins in untreated cells	703:745	Initially, we compared the molecular mass of hFucTV and -VI expressed in COS-7 cells treated with tunicamycin with the mass of the proteins in untreated cells.
11511810	2	81	dep	hFucTV	402:407	arg1	Asn60					410:414	Asn60	410:414	Asn60	410:414	Glycosylation of the two N-terminal potential N-glycosylation sites (hFucTV: Asn60, Asn105 and hFucTVI: Asn46 and Asn91) have never been studied in detail.
11511810	2	81	dep	hFucTV	402:407	arg1	hFucTVI					428:434	hFucTVI	428:434	hFucTVI	428:434	Glycosylation of the two N-terminal potential N-glycosylation sites (hFucTV: Asn60, Asn105 and hFucTVI: Asn46 and Asn91) have never been studied in detail.
11511810	2	81	dep	hFucTV	402:407	arg1	Asn105					417:422	Asn105	417:422	Asn105	417:422	Glycosylation of the two N-terminal potential N-glycosylation sites (hFucTV: Asn60, Asn105 and hFucTVI: Asn46 and Asn91) have never been studied in detail.
11511810	6	82	theme	asparagine	945:954	arg1	residues					956:963	the asparagine residues	941:963	the asparagine residues in the N-terminal potential N-glycosylation sites	941:1013	We then made a series of mutants, in which the asparagine residues in the N-terminal potential N-glycosylation sites were replaced by glutamine.
11511810	11	83	from	sites	1737:1741	arg1	one					1757:1759	one	1757:1759	one	1757:1759	The present study demonstrates that both of the N-terminal potential N-glycosylation sites in hFucTV and one of the sites in hFucTVI are glycosylated.
11511810	11	83	from	sites	1737:1741	arg1	sites					1768:1772	the sites	1764:1772	the sites in hFucTVI	1764:1783	The present study demonstrates that both of the N-terminal potential N-glycosylation sites in hFucTV and one of the sites in hFucTVI are glycosylated.
11511810	11	83	from	sites	1737:1741	arg1	hFucTV					1746:1751	hFucTV	1746:1751	hFucTV	1746:1751	The present study demonstrates that both of the N-terminal potential N-glycosylation sites in hFucTV and one of the sites in hFucTVI are glycosylated.
11511810	4	84	theme	-VI	644:646	arg1	mass					625:628	the molecular mass	611:628	the molecular mass of hFucTV and -VI expressed in COS-7 cells treated with tunicamycin with the mass of the proteins in untreated cells	611:745	Initially, we compared the molecular mass of hFucTV and -VI expressed in COS-7 cells treated with tunicamycin with the mass of the proteins in untreated cells.
11511810	10	85	theme	enzyme	1517:1522	arg1	activity					1524:1531	the enzyme activity	1513:1531	the enzyme activity	1513:1531	In addition, castanospermine treatment diminished the enzyme activity and hence trimming of the N-linked glycans are required for expression of full enzyme activity of both hFucTV and -VI.
11511810	0	86	theme	N-terminal	21:30	arg1	sites					58:62	the N-terminal potential N-glycosylation sites	17:62	the N-terminal potential N-glycosylation sites in the human alpha1,3-fucosyltransferase V	17:105	Glycosylation of the N-terminal potential N-glycosylation sites in the human alpha1,3-fucosyltransferase V and -VI (hFucTV and -VI).
11511810	5	87	from	proteins	793:800	arg1	cells					827:831	treated and untreated cells	805:831	treated and untreated cells	805:831	The difference in molecular mass between the proteins in treated and untreated cells corresponded to the presence of at least three N-linked glycans.
11511810	9	88	theme	wt	1450:1451	arg1	activity					1453:1460	the wt activity	1446:1460	the wt activity	1446:1460	However, the enzyme activity of the hFucTV N60Q/N105Q double mutant was reduced to approximately 40% of the wt activity.
11511810	2	89	theme	N-glycosylation	379:393	arg1	sites					395:399	the two N-terminal potential N-glycosylation sites	350:399	the two N-terminal potential N-glycosylation sites (hFucTV: Asn60, Asn105 and hFucTVI: Asn46 and Asn91)	350:452	Glycosylation of the two N-terminal potential N-glycosylation sites (hFucTV: Asn60, Asn105 and hFucTVI: Asn46 and Asn91) have never been studied in detail.
11511810	3	90	theme	potential	555:563	arg1	sites					581:585	these potential N-glycosylation sites	549:585	these potential N-glycosylation sites	549:585	In the present study, we have analysed the glycosylation of these potential N-glycosylation sites.
11511810	7	91	gly	glycosylated	1113:1124	arg1	sites					1092:1096	both sites	1087:1096	both sites in hFucTV	1087:1106	Western blotting analyses demonstrated that both sites in hFucTV were glycosylated, whereas in hFucTVI only one of the sites (Asn91) was glycosylated.
11511810	2	92	theme	N-terminal	358:367	arg1	sites					395:399	the two N-terminal potential N-glycosylation sites	350:399	the two N-terminal potential N-glycosylation sites (hFucTV: Asn60, Asn105 and hFucTVI: Asn46 and Asn91)	350:452	Glycosylation of the two N-terminal potential N-glycosylation sites (hFucTV: Asn60, Asn105 and hFucTVI: Asn46 and Asn91) have never been studied in detail.
11511810	7	93	theme	Western	1043:1049	arg1	analyses					1060:1067	Western blotting analyses	1043:1067	Western blotting analyses	1043:1067	Western blotting analyses demonstrated that both sites in hFucTV were glycosylated, whereas in hFucTVI only one of the sites (Asn91) was glycosylated.
11511810	0	94	gly	Glycosylation	0:12	arg1	sites					58:62	the N-terminal potential N-glycosylation sites	17:62	the N-terminal potential N-glycosylation sites in the human alpha1,3-fucosyltransferase V	17:105	Glycosylation of the N-terminal potential N-glycosylation sites in the human alpha1,3-fucosyltransferase V and -VI (hFucTV and -VI).
11511810	1	95	contain	contain	199:205	arg2	sites					238:242	four potential N-glycosylation sites	207:242	four potential N-glycosylation sites	207:242	Human alpha1,3-fucosyltransferase V and -VI (hFucTV and -VI) each contain four potential N-glycosylation sites (hFucTV: Asn60, Asn105, Asn167 and Asn198 and hFucTVI: Asn46, Asn91, Asn153 and Asn184).
11511810	1	95	contain	contain	199:205	arg1	-VI					173:175	-VI	173:175	-VI (hFucTV and -VI)	173:192	Human alpha1,3-fucosyltransferase V and -VI (hFucTV and -VI) each contain four potential N-glycosylation sites (hFucTV: Asn60, Asn105, Asn167 and Asn198 and hFucTVI: Asn46, Asn91, Asn153 and Asn184).
11511810	1	95	contain	contain	199:205	arg1	V					167:167	Human alpha1,3-fucosyltransferase V	133:167	Human alpha1,3-fucosyltransferase V	133:167	Human alpha1,3-fucosyltransferase V and -VI (hFucTV and -VI) each contain four potential N-glycosylation sites (hFucTV: Asn60, Asn105, Asn167 and Asn198 and hFucTVI: Asn46, Asn91, Asn153 and Asn184).
11511810	1	96	theme	alpha1,3-fucosyltransferase	139:165	arg1	V					167:167	Human alpha1,3-fucosyltransferase V	133:167	Human alpha1,3-fucosyltransferase V	133:167	Human alpha1,3-fucosyltransferase V and -VI (hFucTV and -VI) each contain four potential N-glycosylation sites (hFucTV: Asn60, Asn105, Asn167 and Asn198 and hFucTVI: Asn46, Asn91, Asn153 and Asn184).
11511810	5	97	theme	glycans	889:895	arg1	presence					853:860	the presence	849:860	the presence of at least three N-linked glycans	849:895	The difference in molecular mass between the proteins in treated and untreated cells corresponded to the presence of at least three N-linked glycans.
11511810	3	98	theme	sites	581:585	arg1	glycosylation					532:544	the glycosylation	528:544	the glycosylation of these potential N-glycosylation sites	528:585	In the present study, we have analysed the glycosylation of these potential N-glycosylation sites.
11511810	1	99	dep	contain	199:205	arg1	hFucTV					245:250	hFucTV	245:250	hFucTV	245:250	Human alpha1,3-fucosyltransferase V and -VI (hFucTV and -VI) each contain four potential N-glycosylation sites (hFucTV: Asn60, Asn105, Asn167 and Asn198 and hFucTVI: Asn46, Asn91, Asn153 and Asn184).
11511810	10	100	theme	glycans	1568:1574	arg1	activity					1524:1531	the enzyme activity	1513:1531	the enzyme activity	1513:1531	In addition, castanospermine treatment diminished the enzyme activity and hence trimming of the N-linked glycans are required for expression of full enzyme activity of both hFucTV and -VI.
11511810	10	100	theme	glycans	1568:1574	arg1	trimming					1543:1550	trimming	1543:1550	trimming of the N-linked glycans are required for expression of full enzyme activity of both hFucTV and -VI	1543:1649	In addition, castanospermine treatment diminished the enzyme activity and hence trimming of the N-linked glycans are required for expression of full enzyme activity of both hFucTV and -VI.
11511810	1	101	theme	potential	212:220	arg1	sites					238:242	four potential N-glycosylation sites	207:242	four potential N-glycosylation sites	207:242	Human alpha1,3-fucosyltransferase V and -VI (hFucTV and -VI) each contain four potential N-glycosylation sites (hFucTV: Asn60, Asn105, Asn167 and Asn198 and hFucTVI: Asn46, Asn91, Asn153 and Asn184).
11511810	2	102	gly	N-glycosylation	379:393	arg2	two					354:356	two	354:356	two	354:356	Glycosylation of the two N-terminal potential N-glycosylation sites (hFucTV: Asn60, Asn105 and hFucTVI: Asn46 and Asn91) have never been studied in detail.
11511810	2	102	gly	N-glycosylation	379:393	arg2	sites					395:399	the two N-terminal potential N-glycosylation sites	350:399	the two N-terminal potential N-glycosylation sites (hFucTV: Asn60, Asn105 and hFucTVI: Asn46 and Asn91)	350:452	Glycosylation of the two N-terminal potential N-glycosylation sites (hFucTV: Asn60, Asn105 and hFucTVI: Asn46 and Asn91) have never been studied in detail.
11511810	6	103	theme	N-glycosylation	993:1007	arg1	sites					1009:1013	the N-terminal potential N-glycosylation sites	968:1013	the N-terminal potential N-glycosylation sites	968:1013	We then made a series of mutants, in which the asparagine residues in the N-terminal potential N-glycosylation sites were replaced by glutamine.
11511810	10	104	theme	full	1607:1610	arg1	activity					1619:1626	full enzyme activity	1607:1626	full enzyme activity of both hFucTV and -VI	1607:1649	In addition, castanospermine treatment diminished the enzyme activity and hence trimming of the N-linked glycans are required for expression of full enzyme activity of both hFucTV and -VI.
21932778	4	0	theme	N-glycosylation	622:636	arg1	sites					638:642	the potential N-glycosylation sites	608:642	the potential N-glycosylation sites	608:642	Mutagenesis and enzymatic cleavage indicated that the potential N-glycosylation sites are invariably occupied.
21932778	6	1	theme	sulfate	885:891	arg1	substitution					893:904	Heparan sulfate substitution	877:904	Heparan sulfate substitution of N-glycosylation mutant N116Q	877:936	Heparan sulfate substitution of N-glycosylation mutant N116Q was similar to wild-type glypican-1 while the N79Q mutant and also the double mutant N79Q,N116Q were mostly secreted as high-molecular-weight heparan sulfate proteoglycan.
21932778	6	2	theme	N79Q	984:987	arg1	mutant					1016:1021	the double mutant	1005:1021	the N79Q mutant and also the double mutant N79Q,N116Q	980:1032	Heparan sulfate substitution of N-glycosylation mutant N116Q was similar to wild-type glypican-1 while the N79Q mutant and also the double mutant N79Q,N116Q were mostly secreted as high-molecular-weight heparan sulfate proteoglycan.
21932778	6	2	theme	N79Q	984:987	arg1	mutant					989:994	the N79Q mutant	980:994	the N79Q mutant and also the double mutant N79Q,N116Q	980:1032	Heparan sulfate substitution of N-glycosylation mutant N116Q was similar to wild-type glypican-1 while the N79Q mutant and also the double mutant N79Q,N116Q were mostly secreted as high-molecular-weight heparan sulfate proteoglycan.
21932778	6	2	theme	N79Q	984:987	arg1	proteoglycan					1096:1107	high-molecular-weight heparan sulfate proteoglycan	1058:1107	high-molecular-weight heparan sulfate proteoglycan	1058:1107	Heparan sulfate substitution of N-glycosylation mutant N116Q was similar to wild-type glypican-1 while the N79Q mutant and also the double mutant N79Q,N116Q were mostly secreted as high-molecular-weight heparan sulfate proteoglycan.
21932778	5	3	theme	N-linked	723:730	arg1	glycosylation					732:744	the N-linked glycosylation	719:744	the N-linked glycosylation of glypican-1	719:758	Experiments using the drug tunicamycin to inhibit the N-linked glycosylation of glypican-1 showed that secretion of anchorless glypican-1 was reduced and that the protein did not accumulate inside the cells.
21932778	8	4	theme	single	1296:1301	arg1	transition					1313:1322	A single unfolding transition	1294:1322	A single unfolding transition at high concentrations of urea	1294:1353	A single unfolding transition at high concentrations of urea was found for both N-deglycosylated glypican-1 and glypican-1 in which the N-glycosylation sites had been removed by mutagenesis when chemical denaturation was monitored by circular dichroism and fluorescence emission spectroscopy.
21932778	2	5	theme	N-glycosylation	291:305	arg1	sites					307:311	potential N-glycosylation sites	281:311	potential N-glycosylation sites	281:311	The primary structures of glypican core proteins contain potential N-glycosylation sites, but the importance of N-glycosylation in glypicans has never been investigated in detail.
21932778	8	6	from	concentrations	1332:1345	arg1	transition					1313:1322	A single unfolding transition	1294:1322	A single unfolding transition at high concentrations of urea	1294:1353	A single unfolding transition at high concentrations of urea was found for both N-deglycosylated glypican-1 and glypican-1 in which the N-glycosylation sites had been removed by mutagenesis when chemical denaturation was monitored by circular dichroism and fluorescence emission spectroscopy.
21932778	8	7	theme	N-deglycosylated	1374:1389	arg1	glypican-1					1391:1400	N-deglycosylated glypican-1	1374:1400	N-deglycosylated glypican-1	1374:1400	A single unfolding transition at high concentrations of urea was found for both N-deglycosylated glypican-1 and glypican-1 in which the N-glycosylation sites had been removed by mutagenesis when chemical denaturation was monitored by circular dichroism and fluorescence emission spectroscopy.
21932778	7	8	theme	fluorescence	1200:1211	arg1	spectra					1222:1228	far-UV circular dichroism and fluorescence emission spectra	1170:1228	spectra	1222:1228	N-Glycosylation mutants and N-deglycosylated glypican-1 had far-UV circular dichroism and fluorescence emission spectra that were highly similar to those of N-glycosylated glypican-1.
21932778	1	9	theme	heparan	200:206	arg1	chains					216:221	their heparan sulfate chains	194:221	their heparan sulfate chains	194:221	Glypicans are cell-surface heparan sulfate proteoglycans that regulate developmental signaling pathways by binding growth factors to their heparan sulfate chains.
21932778	8	10	theme	high	1327:1330	arg1	concentrations					1332:1345	high concentrations	1327:1345	high concentrations of urea	1327:1353	A single unfolding transition at high concentrations of urea was found for both N-deglycosylated glypican-1 and glypican-1 in which the N-glycosylation sites had been removed by mutagenesis when chemical denaturation was monitored by circular dichroism and fluorescence emission spectroscopy.
21932778	9	11	theme	glycans	1863:1869	arg1	absence					1843:1849	the absence	1839:1849	the absence of N-linked glycans	1839:1869	In summary, we have found that the potential N-glycosylation sites in glypican-1 are invariably occupied and that the N-linked glycans on glypican-1 affect protein expression and heparan sulfate substitution but that correct folding can be obtained in the absence of N-linked glycans.
21932778	0	12	link	N-linked	23:30	arg1	glycans					32:38	N-linked glycans	23:38	N-linked glycans	23:38	The structural role of N-linked glycans on human glypican-1.
21932778	5	13	theme	anchorless	785:794	arg1	glypican-1					796:805	anchorless glypican-1	785:805	anchorless glypican-1	785:805	Experiments using the drug tunicamycin to inhibit the N-linked glycosylation of glypican-1 showed that secretion of anchorless glypican-1 was reduced and that the protein did not accumulate inside the cells.
21932778	7	14	theme	far-UV	1170:1175	arg1	dichroism					1186:1194	far-UV circular dichroism and fluorescence emission spectra	1170:1228	dichroism	1186:1194	N-Glycosylation mutants and N-deglycosylated glypican-1 had far-UV circular dichroism and fluorescence emission spectra that were highly similar to those of N-glycosylated glypican-1.
21932778	9	15	theme	N-glycosylation	1632:1646	arg1	sites					1648:1652	the potential N-glycosylation sites	1618:1652	the potential N-glycosylation sites in glypican-1	1618:1666	In summary, we have found that the potential N-glycosylation sites in glypican-1 are invariably occupied and that the N-linked glycans on glypican-1 affect protein expression and heparan sulfate substitution but that correct folding can be obtained in the absence of N-linked glycans.
21932778	6	16	dep	mutant	1016:1021	arg1	N116Q					1028:1032	N116Q	1028:1032	N116Q	1028:1032	Heparan sulfate substitution of N-glycosylation mutant N116Q was similar to wild-type glypican-1 while the N79Q mutant and also the double mutant N79Q,N116Q were mostly secreted as high-molecular-weight heparan sulfate proteoglycan.
21932778	2	17	theme	primary	228:234	arg1	structures					236:245	The primary structures	224:245	The primary structures of glypican core proteins	224:271	The primary structures of glypican core proteins contain potential N-glycosylation sites, but the importance of N-glycosylation in glypicans has never been investigated in detail.
21932778	9	18	theme	protein	1743:1749	arg1	expression					1751:1760	protein expression	1743:1760	protein expression	1743:1760	In summary, we have found that the potential N-glycosylation sites in glypican-1 are invariably occupied and that the N-linked glycans on glypican-1 affect protein expression and heparan sulfate substitution but that correct folding can be obtained in the absence of N-linked glycans.
21932778	1	19	theme	signaling	146:154	arg1	pathways					156:163	developmental signaling pathways	132:163	developmental signaling pathways	132:163	Glypicans are cell-surface heparan sulfate proteoglycans that regulate developmental signaling pathways by binding growth factors to their heparan sulfate chains.
21932778	9	20	used	occupied	1683:1690	arg2	sites					1648:1652	the potential N-glycosylation sites	1618:1652	the potential N-glycosylation sites in glypican-1	1618:1666	In summary, we have found that the potential N-glycosylation sites in glypican-1 are invariably occupied and that the N-linked glycans on glypican-1 affect protein expression and heparan sulfate substitution but that correct folding can be obtained in the absence of N-linked glycans.
21932778	2	21	theme	core	259:262	arg1	proteins					264:271	glypican core proteins	250:271	glypican core proteins	250:271	The primary structures of glypican core proteins contain potential N-glycosylation sites, but the importance of N-glycosylation in glypicans has never been investigated in detail.
21932778	2	22	from	importance	322:331	arg1	glypicans					355:363	glypicans	355:363	glypicans	355:363	The primary structures of glypican core proteins contain potential N-glycosylation sites, but the importance of N-glycosylation in glypicans has never been investigated in detail.
21932778	6	23	theme	sulfate	1088:1094	arg1	mutant					1016:1021	the double mutant	1005:1021	the N79Q mutant and also the double mutant N79Q,N116Q	980:1032	Heparan sulfate substitution of N-glycosylation mutant N116Q was similar to wild-type glypican-1 while the N79Q mutant and also the double mutant N79Q,N116Q were mostly secreted as high-molecular-weight heparan sulfate proteoglycan.
21932778	6	23	theme	sulfate	1088:1094	arg1	proteoglycan					1096:1107	high-molecular-weight heparan sulfate proteoglycan	1058:1107	high-molecular-weight heparan sulfate proteoglycan	1058:1107	Heparan sulfate substitution of N-glycosylation mutant N116Q was similar to wild-type glypican-1 while the N79Q mutant and also the double mutant N79Q,N116Q were mostly secreted as high-molecular-weight heparan sulfate proteoglycan.
21932778	6	23	theme	sulfate	1088:1094	arg1	mutant					989:994	the N79Q mutant	980:994	the N79Q mutant and also the double mutant N79Q,N116Q	980:1032	Heparan sulfate substitution of N-glycosylation mutant N116Q was similar to wild-type glypican-1 while the N79Q mutant and also the double mutant N79Q,N116Q were mostly secreted as high-molecular-weight heparan sulfate proteoglycan.
21932778	0	24	from	role	15:18	arg1	glypican-1					49:58	human glypican-1	43:58	human glypican-1	43:58	The structural role of N-linked glycans on human glypican-1.
21932778	3	25	from	role	425:428	arg1	Asn-79					471:476	Asn-79	471:476	Asn-79	471:476	Here, we studied the role of the possible N-glycosylation sites at Asn-79 and Asn-116 in recombinant anchorless glypican-1 expressed in eukaryotic cells.
21932778	3	25	from	role	425:428	arg1	glypican-1					516:525	recombinant anchorless glypican-1	493:525	recombinant anchorless glypican-1 expressed in eukaryotic cells	493:555	Here, we studied the role of the possible N-glycosylation sites at Asn-79 and Asn-116 in recombinant anchorless glypican-1 expressed in eukaryotic cells.
21932778	3	25	from	role	425:428	arg1	Asn-116					482:488	Asn-116	482:488	Asn-116	482:488	Here, we studied the role of the possible N-glycosylation sites at Asn-79 and Asn-116 in recombinant anchorless glypican-1 expressed in eukaryotic cells.
21932778	1	26	theme	growth	176:181	arg1	factors					183:189	growth factors	176:189	growth factors	176:189	Glypicans are cell-surface heparan sulfate proteoglycans that regulate developmental signaling pathways by binding growth factors to their heparan sulfate chains.
21932778	6	27	theme	high-molecular-weight	1058:1078	arg1	mutant					1016:1021	the double mutant	1005:1021	the N79Q mutant and also the double mutant N79Q,N116Q	980:1032	Heparan sulfate substitution of N-glycosylation mutant N116Q was similar to wild-type glypican-1 while the N79Q mutant and also the double mutant N79Q,N116Q were mostly secreted as high-molecular-weight heparan sulfate proteoglycan.
21932778	6	27	theme	high-molecular-weight	1058:1078	arg1	proteoglycan					1096:1107	high-molecular-weight heparan sulfate proteoglycan	1058:1107	high-molecular-weight heparan sulfate proteoglycan	1058:1107	Heparan sulfate substitution of N-glycosylation mutant N116Q was similar to wild-type glypican-1 while the N79Q mutant and also the double mutant N79Q,N116Q were mostly secreted as high-molecular-weight heparan sulfate proteoglycan.
21932778	6	27	theme	high-molecular-weight	1058:1078	arg1	mutant					989:994	the N79Q mutant	980:994	the N79Q mutant and also the double mutant N79Q,N116Q	980:1032	Heparan sulfate substitution of N-glycosylation mutant N116Q was similar to wild-type glypican-1 while the N79Q mutant and also the double mutant N79Q,N116Q were mostly secreted as high-molecular-weight heparan sulfate proteoglycan.
21932778	9	28	theme	N-linked	1705:1712	arg1	glycans					1714:1720	the N-linked glycans	1701:1720	the N-linked glycans on glypican-1	1701:1734	In summary, we have found that the potential N-glycosylation sites in glypican-1 are invariably occupied and that the N-linked glycans on glypican-1 affect protein expression and heparan sulfate substitution but that correct folding can be obtained in the absence of N-linked glycans.
21932778	3	29	theme	N-glycosylation	446:460	arg1	sites					462:466	the possible N-glycosylation sites	433:466	the possible N-glycosylation sites at Asn-79 and Asn-116	433:488	Here, we studied the role of the possible N-glycosylation sites at Asn-79 and Asn-116 in recombinant anchorless glypican-1 expressed in eukaryotic cells.
21932778	9	30	link	N-linked	1854:1861	arg1	glycans					1863:1869	N-linked glycans	1854:1869	N-linked glycans	1854:1869	In summary, we have found that the potential N-glycosylation sites in glypican-1 are invariably occupied and that the N-linked glycans on glypican-1 affect protein expression and heparan sulfate substitution but that correct folding can be obtained in the absence of N-linked glycans.
21932778	8	31	gly	N-glycosylation	1430:1444	arg2	sites					1446:1450	the N-glycosylation sites	1426:1450	the N-glycosylation sites	1426:1450	A single unfolding transition at high concentrations of urea was found for both N-deglycosylated glypican-1 and glypican-1 in which the N-glycosylation sites had been removed by mutagenesis when chemical denaturation was monitored by circular dichroism and fluorescence emission spectroscopy.
21932778	1	32	theme	heparan	88:94	arg1	Glypicans					61:69	Glypicans	61:69	Glypicans	61:69	Glypicans are cell-surface heparan sulfate proteoglycans that regulate developmental signaling pathways by binding growth factors to their heparan sulfate chains.
21932778	1	32	theme	heparan	88:94	arg1	proteoglycans					104:116	cell-surface heparan sulfate proteoglycans	75:116	cell-surface heparan sulfate proteoglycans that regulate developmental signaling pathways by binding growth factors to their heparan sulfate chains	75:221	Glypicans are cell-surface heparan sulfate proteoglycans that regulate developmental signaling pathways by binding growth factors to their heparan sulfate chains.
21932778	8	33	theme	circular	1528:1535	arg1	dichroism					1537:1545	circular dichroism	1528:1545	circular dichroism	1528:1545	A single unfolding transition at high concentrations of urea was found for both N-deglycosylated glypican-1 and glypican-1 in which the N-glycosylation sites had been removed by mutagenesis when chemical denaturation was monitored by circular dichroism and fluorescence emission spectroscopy.
21932778	7	34	contain	had	1166:1168	arg2	dichroism					1186:1194	far-UV circular dichroism and fluorescence emission spectra	1170:1228	dichroism	1186:1194	N-Glycosylation mutants and N-deglycosylated glypican-1 had far-UV circular dichroism and fluorescence emission spectra that were highly similar to those of N-glycosylated glypican-1.
21932778	7	34	contain	had	1166:1168	arg1	mutants					1126:1132	N-Glycosylation mutants	1110:1132	N-Glycosylation mutants	1110:1132	N-Glycosylation mutants and N-deglycosylated glypican-1 had far-UV circular dichroism and fluorescence emission spectra that were highly similar to those of N-glycosylated glypican-1.
21932778	7	34	contain	had	1166:1168	arg1	glypican-1					1155:1164	N-deglycosylated glypican-1	1138:1164	N-deglycosylated glypican-1	1138:1164	N-Glycosylation mutants and N-deglycosylated glypican-1 had far-UV circular dichroism and fluorescence emission spectra that were highly similar to those of N-glycosylated glypican-1.
21932778	7	34	contain	had	1166:1168	arg2	spectra					1222:1228	far-UV circular dichroism and fluorescence emission spectra	1170:1228	spectra	1222:1228	N-Glycosylation mutants and N-deglycosylated glypican-1 had far-UV circular dichroism and fluorescence emission spectra that were highly similar to those of N-glycosylated glypican-1.
21932778	7	35	gly	N-glycosylated	1267:1280	arg1	glypican-1					1282:1291	N-glycosylated glypican-1	1267:1291	N-glycosylated glypican-1	1267:1291	N-Glycosylation mutants and N-deglycosylated glypican-1 had far-UV circular dichroism and fluorescence emission spectra that were highly similar to those of N-glycosylated glypican-1.
21932778	7	36	theme	N-glycosylated	1267:1280	arg1	glypican-1					1282:1291	N-glycosylated glypican-1	1267:1291	N-glycosylated glypican-1	1267:1291	N-Glycosylation mutants and N-deglycosylated glypican-1 had far-UV circular dichroism and fluorescence emission spectra that were highly similar to those of N-glycosylated glypican-1.
21932778	0	37	theme	N-linked	23:30	arg1	glycans					32:38	N-linked glycans	23:38	N-linked glycans	23:38	The structural role of N-linked glycans on human glypican-1.
21932778	9	38	theme	heparan	1766:1772	arg1	sulfate					1774:1780	heparan sulfate	1766:1780	heparan sulfate	1766:1780	In summary, we have found that the potential N-glycosylation sites in glypican-1 are invariably occupied and that the N-linked glycans on glypican-1 affect protein expression and heparan sulfate substitution but that correct folding can be obtained in the absence of N-linked glycans.
21932778	8	39	theme	emission	1564:1571	arg1	spectroscopy					1573:1584	fluorescence emission spectroscopy	1551:1584	fluorescence emission spectroscopy	1551:1584	A single unfolding transition at high concentrations of urea was found for both N-deglycosylated glypican-1 and glypican-1 in which the N-glycosylation sites had been removed by mutagenesis when chemical denaturation was monitored by circular dichroism and fluorescence emission spectroscopy.
21932778	3	40	from	Asn-79	471:476	arg1	sites					462:466	the possible N-glycosylation sites	433:466	the possible N-glycosylation sites at Asn-79 and Asn-116	433:488	Here, we studied the role of the possible N-glycosylation sites at Asn-79 and Asn-116 in recombinant anchorless glypican-1 expressed in eukaryotic cells.
21932778	3	40	from	Asn-79	471:476	arg1	role					425:428	the role	421:428	the role of the possible N-glycosylation sites at Asn-79 and Asn-116 in recombinant anchorless glypican-1 expressed in eukaryotic cells	421:555	Here, we studied the role of the possible N-glycosylation sites at Asn-79 and Asn-116 in recombinant anchorless glypican-1 expressed in eukaryotic cells.
21932778	3	41	theme	anchorless	505:514	arg1	glypican-1					516:525	recombinant anchorless glypican-1	493:525	recombinant anchorless glypican-1 expressed in eukaryotic cells	493:555	Here, we studied the role of the possible N-glycosylation sites at Asn-79 and Asn-116 in recombinant anchorless glypican-1 expressed in eukaryotic cells.
21932778	6	42	theme	mutant	925:930	arg1	N116Q					932:936	N-glycosylation mutant N116Q	909:936	N-glycosylation mutant N116Q	909:936	Heparan sulfate substitution of N-glycosylation mutant N116Q was similar to wild-type glypican-1 while the N79Q mutant and also the double mutant N79Q,N116Q were mostly secreted as high-molecular-weight heparan sulfate proteoglycan.
21932778	3	43	from	Asn-116	482:488	arg1	sites					462:466	the possible N-glycosylation sites	433:466	the possible N-glycosylation sites at Asn-79 and Asn-116	433:488	Here, we studied the role of the possible N-glycosylation sites at Asn-79 and Asn-116 in recombinant anchorless glypican-1 expressed in eukaryotic cells.
21932778	3	43	from	Asn-116	482:488	arg1	role					425:428	the role	421:428	the role of the possible N-glycosylation sites at Asn-79 and Asn-116 in recombinant anchorless glypican-1 expressed in eukaryotic cells	421:555	Here, we studied the role of the possible N-glycosylation sites at Asn-79 and Asn-116 in recombinant anchorless glypican-1 expressed in eukaryotic cells.
21932778	9	44	dep	expression	1751:1760	arg1	substitution					1782:1793	substitution	1782:1793	substitution	1782:1793	In summary, we have found that the potential N-glycosylation sites in glypican-1 are invariably occupied and that the N-linked glycans on glypican-1 affect protein expression and heparan sulfate substitution but that correct folding can be obtained in the absence of N-linked glycans.
21932778	9	45	from	glycans	1714:1720	arg1	glypican-1					1725:1734	glypican-1	1725:1734	glypican-1	1725:1734	In summary, we have found that the potential N-glycosylation sites in glypican-1 are invariably occupied and that the N-linked glycans on glypican-1 affect protein expression and heparan sulfate substitution but that correct folding can be obtained in the absence of N-linked glycans.
21932778	3	46	theme	eukaryotic	540:549	arg1	cells					551:555	eukaryotic cells	540:555	eukaryotic cells	540:555	Here, we studied the role of the possible N-glycosylation sites at Asn-79 and Asn-116 in recombinant anchorless glypican-1 expressed in eukaryotic cells.
21932778	6	47	theme	wild-type	953:961	arg1	glypican-1					963:972	wild-type glypican-1	953:972	wild-type glypican-1	953:972	Heparan sulfate substitution of N-glycosylation mutant N116Q was similar to wild-type glypican-1 while the N79Q mutant and also the double mutant N79Q,N116Q were mostly secreted as high-molecular-weight heparan sulfate proteoglycan.
21932778	4	48	theme	potential	612:620	arg1	sites					638:642	the potential N-glycosylation sites	608:642	the potential N-glycosylation sites	608:642	Mutagenesis and enzymatic cleavage indicated that the potential N-glycosylation sites are invariably occupied.
21932778	6	49	theme	Heparan	877:883	arg1	sulfate					885:891	Heparan sulfate	877:891	Heparan sulfate substitution of N-glycosylation mutant N116Q	877:936	Heparan sulfate substitution of N-glycosylation mutant N116Q was similar to wild-type glypican-1 while the N79Q mutant and also the double mutant N79Q,N116Q were mostly secreted as high-molecular-weight heparan sulfate proteoglycan.
21932778	2	50	contain	contain	273:279	arg1	structures					236:245	The primary structures	224:245	The primary structures of glypican core proteins	224:271	The primary structures of glypican core proteins contain potential N-glycosylation sites, but the importance of N-glycosylation in glypicans has never been investigated in detail.
21932778	2	50	contain	contain	273:279	arg2	sites					307:311	potential N-glycosylation sites	281:311	potential N-glycosylation sites	281:311	The primary structures of glypican core proteins contain potential N-glycosylation sites, but the importance of N-glycosylation in glypicans has never been investigated in detail.
21932778	2	51	gly	N-glycosylation	291:305	arg2	sites					307:311	potential N-glycosylation sites	281:311	potential N-glycosylation sites	281:311	The primary structures of glypican core proteins contain potential N-glycosylation sites, but the importance of N-glycosylation in glypicans has never been investigated in detail.
21932778	7	52	theme	emission	1213:1220	arg1	spectra					1222:1228	far-UV circular dichroism and fluorescence emission spectra	1170:1228	spectra	1222:1228	N-Glycosylation mutants and N-deglycosylated glypican-1 had far-UV circular dichroism and fluorescence emission spectra that were highly similar to those of N-glycosylated glypican-1.
21932778	9	53	link	N-linked	1705:1712	arg1	glycans					1714:1720	the N-linked glycans	1701:1720	the N-linked glycans on glypican-1	1701:1734	In summary, we have found that the potential N-glycosylation sites in glypican-1 are invariably occupied and that the N-linked glycans on glypican-1 affect protein expression and heparan sulfate substitution but that correct folding can be obtained in the absence of N-linked glycans.
21932778	5	54	theme	drug	691:694	arg1	tunicamycin					696:706	the drug tunicamycin	687:706	the drug tunicamycin	687:706	Experiments using the drug tunicamycin to inhibit the N-linked glycosylation of glypican-1 showed that secretion of anchorless glypican-1 was reduced and that the protein did not accumulate inside the cells.
21932778	2	55	theme	N-glycosylation	336:350	arg1	importance					322:331	the importance	318:331	the importance of N-glycosylation in glypicans	318:363	The primary structures of glypican core proteins contain potential N-glycosylation sites, but the importance of N-glycosylation in glypicans has never been investigated in detail.
21932778	8	56	theme	unfolding	1303:1311	arg1	transition					1313:1322	A single unfolding transition	1294:1322	A single unfolding transition at high concentrations of urea	1294:1353	A single unfolding transition at high concentrations of urea was found for both N-deglycosylated glypican-1 and glypican-1 in which the N-glycosylation sites had been removed by mutagenesis when chemical denaturation was monitored by circular dichroism and fluorescence emission spectroscopy.
21932778	9	57	theme	N-linked	1854:1861	arg1	glycans					1863:1869	N-linked glycans	1854:1869	N-linked glycans	1854:1869	In summary, we have found that the potential N-glycosylation sites in glypican-1 are invariably occupied and that the N-linked glycans on glypican-1 affect protein expression and heparan sulfate substitution but that correct folding can be obtained in the absence of N-linked glycans.
21932778	9	58	from	sites	1648:1652	arg1	glypican-1					1657:1666	glypican-1	1657:1666	glypican-1	1657:1666	In summary, we have found that the potential N-glycosylation sites in glypican-1 are invariably occupied and that the N-linked glycans on glypican-1 affect protein expression and heparan sulfate substitution but that correct folding can be obtained in the absence of N-linked glycans.
21932778	7	59	theme	circular	1177:1184	arg1	dichroism					1186:1194	far-UV circular dichroism and fluorescence emission spectra	1170:1228	dichroism	1186:1194	N-Glycosylation mutants and N-deglycosylated glypican-1 had far-UV circular dichroism and fluorescence emission spectra that were highly similar to those of N-glycosylated glypican-1.
21932778	1	60	theme	sulfate	208:214	arg1	chains					216:221	their heparan sulfate chains	194:221	their heparan sulfate chains	194:221	Glypicans are cell-surface heparan sulfate proteoglycans that regulate developmental signaling pathways by binding growth factors to their heparan sulfate chains.
21932778	2	61	theme	glypican	250:257	arg1	proteins					264:271	glypican core proteins	250:271	glypican core proteins	250:271	The primary structures of glypican core proteins contain potential N-glycosylation sites, but the importance of N-glycosylation in glypicans has never been investigated in detail.
21932778	9	62	theme	potential	1622:1630	arg1	sites					1648:1652	the potential N-glycosylation sites	1618:1652	the potential N-glycosylation sites in glypican-1	1618:1666	In summary, we have found that the potential N-glycosylation sites in glypican-1 are invariably occupied and that the N-linked glycans on glypican-1 affect protein expression and heparan sulfate substitution but that correct folding can be obtained in the absence of N-linked glycans.
21932778	7	63	theme	N-deglycosylated	1138:1153	arg1	glypican-1					1155:1164	N-deglycosylated glypican-1	1138:1164	N-deglycosylated glypican-1	1138:1164	N-Glycosylation mutants and N-deglycosylated glypican-1 had far-UV circular dichroism and fluorescence emission spectra that were highly similar to those of N-glycosylated glypican-1.
21932778	8	64	gly	N-deglycosylated	1374:1389	arg1	glypican-1					1391:1400	N-deglycosylated glypican-1	1374:1400	N-deglycosylated glypican-1	1374:1400	A single unfolding transition at high concentrations of urea was found for both N-deglycosylated glypican-1 and glypican-1 in which the N-glycosylation sites had been removed by mutagenesis when chemical denaturation was monitored by circular dichroism and fluorescence emission spectroscopy.
21932778	7	65	theme	N-Glycosylation	1110:1124	arg1	mutants					1126:1132	N-Glycosylation mutants	1110:1132	N-Glycosylation mutants	1110:1132	N-Glycosylation mutants and N-deglycosylated glypican-1 had far-UV circular dichroism and fluorescence emission spectra that were highly similar to those of N-glycosylated glypican-1.
21932778	8	66	theme	urea	1350:1353	arg1	concentrations					1332:1345	high concentrations	1327:1345	high concentrations of urea	1327:1353	A single unfolding transition at high concentrations of urea was found for both N-deglycosylated glypican-1 and glypican-1 in which the N-glycosylation sites had been removed by mutagenesis when chemical denaturation was monitored by circular dichroism and fluorescence emission spectroscopy.
21932778	6	67	theme	double	1009:1014	arg1	mutant					1016:1021	the double mutant	1005:1021	the N79Q mutant and also the double mutant N79Q,N116Q	980:1032	Heparan sulfate substitution of N-glycosylation mutant N116Q was similar to wild-type glypican-1 while the N79Q mutant and also the double mutant N79Q,N116Q were mostly secreted as high-molecular-weight heparan sulfate proteoglycan.
21932778	6	67	theme	double	1009:1014	arg1	proteoglycan					1096:1107	high-molecular-weight heparan sulfate proteoglycan	1058:1107	high-molecular-weight heparan sulfate proteoglycan	1058:1107	Heparan sulfate substitution of N-glycosylation mutant N116Q was similar to wild-type glypican-1 while the N79Q mutant and also the double mutant N79Q,N116Q were mostly secreted as high-molecular-weight heparan sulfate proteoglycan.
21932778	6	67	theme	double	1009:1014	arg1	mutant					989:994	the N79Q mutant	980:994	the N79Q mutant and also the double mutant N79Q,N116Q	980:1032	Heparan sulfate substitution of N-glycosylation mutant N116Q was similar to wild-type glypican-1 while the N79Q mutant and also the double mutant N79Q,N116Q were mostly secreted as high-molecular-weight heparan sulfate proteoglycan.
21932778	7	68	gly	N-deglycosylated	1138:1153	arg1	glypican-1					1155:1164	N-deglycosylated glypican-1	1138:1164	N-deglycosylated glypican-1	1138:1164	N-Glycosylation mutants and N-deglycosylated glypican-1 had far-UV circular dichroism and fluorescence emission spectra that were highly similar to those of N-glycosylated glypican-1.
21932778	5	69	theme	glypican-1	749:758	arg1	glycosylation					732:744	the N-linked glycosylation	719:744	the N-linked glycosylation of glypican-1	719:758	Experiments using the drug tunicamycin to inhibit the N-linked glycosylation of glypican-1 showed that secretion of anchorless glypican-1 was reduced and that the protein did not accumulate inside the cells.
21932778	2	70	theme	potential	281:289	arg1	sites					307:311	potential N-glycosylation sites	281:311	potential N-glycosylation sites	281:311	The primary structures of glypican core proteins contain potential N-glycosylation sites, but the importance of N-glycosylation in glypicans has never been investigated in detail.
21932778	1	71	theme	developmental	132:144	arg1	pathways					156:163	developmental signaling pathways	132:163	developmental signaling pathways	132:163	Glypicans are cell-surface heparan sulfate proteoglycans that regulate developmental signaling pathways by binding growth factors to their heparan sulfate chains.
21932778	9	72	gly	N-glycosylation	1632:1646	arg2	sites					1648:1652	the potential N-glycosylation sites	1618:1652	the potential N-glycosylation sites in glypican-1	1618:1666	In summary, we have found that the potential N-glycosylation sites in glypican-1 are invariably occupied and that the N-linked glycans on glypican-1 affect protein expression and heparan sulfate substitution but that correct folding can be obtained in the absence of N-linked glycans.
21932778	8	73	theme	N-glycosylation	1430:1444	arg1	sites					1446:1450	the N-glycosylation sites	1426:1450	the N-glycosylation sites	1426:1450	A single unfolding transition at high concentrations of urea was found for both N-deglycosylated glypican-1 and glypican-1 in which the N-glycosylation sites had been removed by mutagenesis when chemical denaturation was monitored by circular dichroism and fluorescence emission spectroscopy.
21932778	2	74	theme	proteins	264:271	arg1	structures					236:245	The primary structures	224:245	The primary structures of glypican core proteins	224:271	The primary structures of glypican core proteins contain potential N-glycosylation sites, but the importance of N-glycosylation in glypicans has never been investigated in detail.
21932778	5	75	gly	glycosylation	732:744	arg1	glypican-1					749:758	glypican-1	749:758	glypican-1	749:758	Experiments using the drug tunicamycin to inhibit the N-linked glycosylation of glypican-1 showed that secretion of anchorless glypican-1 was reduced and that the protein did not accumulate inside the cells.
21932778	6	76	theme	heparan	1080:1086	arg1	mutant					1016:1021	the double mutant	1005:1021	the N79Q mutant and also the double mutant N79Q,N116Q	980:1032	Heparan sulfate substitution of N-glycosylation mutant N116Q was similar to wild-type glypican-1 while the N79Q mutant and also the double mutant N79Q,N116Q were mostly secreted as high-molecular-weight heparan sulfate proteoglycan.
21932778	6	76	theme	heparan	1080:1086	arg1	proteoglycan					1096:1107	high-molecular-weight heparan sulfate proteoglycan	1058:1107	high-molecular-weight heparan sulfate proteoglycan	1058:1107	Heparan sulfate substitution of N-glycosylation mutant N116Q was similar to wild-type glypican-1 while the N79Q mutant and also the double mutant N79Q,N116Q were mostly secreted as high-molecular-weight heparan sulfate proteoglycan.
21932778	6	76	theme	heparan	1080:1086	arg1	mutant					989:994	the N79Q mutant	980:994	the N79Q mutant and also the double mutant N79Q,N116Q	980:1032	Heparan sulfate substitution of N-glycosylation mutant N116Q was similar to wild-type glypican-1 while the N79Q mutant and also the double mutant N79Q,N116Q were mostly secreted as high-molecular-weight heparan sulfate proteoglycan.
21932778	5	77	theme	glypican-1	796:805	arg1	secretion					772:780	secretion	772:780	secretion of anchorless glypican-1	772:805	Experiments using the drug tunicamycin to inhibit the N-linked glycosylation of glypican-1 showed that secretion of anchorless glypican-1 was reduced and that the protein did not accumulate inside the cells.
21932778	8	78	theme	chemical	1489:1496	arg1	denaturation					1498:1509	chemical denaturation	1489:1509	chemical denaturation	1489:1509	A single unfolding transition at high concentrations of urea was found for both N-deglycosylated glypican-1 and glypican-1 in which the N-glycosylation sites had been removed by mutagenesis when chemical denaturation was monitored by circular dichroism and fluorescence emission spectroscopy.
21932778	3	79	theme	sites	462:466	arg1	role					425:428	the role	421:428	the role of the possible N-glycosylation sites at Asn-79 and Asn-116 in recombinant anchorless glypican-1 expressed in eukaryotic cells	421:555	Here, we studied the role of the possible N-glycosylation sites at Asn-79 and Asn-116 in recombinant anchorless glypican-1 expressed in eukaryotic cells.
21932778	0	80	theme	structural	4:13	arg1	role					15:18	The structural role	0:18	The structural role of N-linked glycans on human glypican-1	0:58	The structural role of N-linked glycans on human glypican-1.
21932778	4	81	gly	N-glycosylation	622:636	arg2	sites					638:642	the potential N-glycosylation sites	608:642	the potential N-glycosylation sites	608:642	Mutagenesis and enzymatic cleavage indicated that the potential N-glycosylation sites are invariably occupied.
21932778	1	82	theme	cell-surface	75:86	arg1	Glypicans					61:69	Glypicans	61:69	Glypicans	61:69	Glypicans are cell-surface heparan sulfate proteoglycans that regulate developmental signaling pathways by binding growth factors to their heparan sulfate chains.
21932778	1	82	theme	cell-surface	75:86	arg1	proteoglycans					104:116	cell-surface heparan sulfate proteoglycans	75:116	cell-surface heparan sulfate proteoglycans that regulate developmental signaling pathways by binding growth factors to their heparan sulfate chains	75:221	Glypicans are cell-surface heparan sulfate proteoglycans that regulate developmental signaling pathways by binding growth factors to their heparan sulfate chains.
21932778	3	83	theme	possible	437:444	arg1	sites					462:466	the possible N-glycosylation sites	433:466	the possible N-glycosylation sites at Asn-79 and Asn-116	433:488	Here, we studied the role of the possible N-glycosylation sites at Asn-79 and Asn-116 in recombinant anchorless glypican-1 expressed in eukaryotic cells.
21932778	1	84	theme	sulfate	96:102	arg1	Glypicans					61:69	Glypicans	61:69	Glypicans	61:69	Glypicans are cell-surface heparan sulfate proteoglycans that regulate developmental signaling pathways by binding growth factors to their heparan sulfate chains.
21932778	1	84	theme	sulfate	96:102	arg1	proteoglycans					104:116	cell-surface heparan sulfate proteoglycans	75:116	cell-surface heparan sulfate proteoglycans that regulate developmental signaling pathways by binding growth factors to their heparan sulfate chains	75:221	Glypicans are cell-surface heparan sulfate proteoglycans that regulate developmental signaling pathways by binding growth factors to their heparan sulfate chains.
21932778	5	85	link	N-linked	723:730	arg1	glycosylation					732:744	the N-linked glycosylation	719:744	the N-linked glycosylation of glypican-1	719:758	Experiments using the drug tunicamycin to inhibit the N-linked glycosylation of glypican-1 showed that secretion of anchorless glypican-1 was reduced and that the protein did not accumulate inside the cells.
21932778	0	86	theme	glycans	32:38	arg1	role					15:18	The structural role	0:18	The structural role of N-linked glycans on human glypican-1	0:58	The structural role of N-linked glycans on human glypican-1.
21932778	0	87	theme	human	43:47	arg1	glypican-1					49:58	human glypican-1	43:58	human glypican-1	43:58	The structural role of N-linked glycans on human glypican-1.
21932778	6	88	theme	N116Q	932:936	arg1	substitution					893:904	Heparan sulfate substitution	877:904	Heparan sulfate substitution of N-glycosylation mutant N116Q	877:936	Heparan sulfate substitution of N-glycosylation mutant N116Q was similar to wild-type glypican-1 while the N79Q mutant and also the double mutant N79Q,N116Q were mostly secreted as high-molecular-weight heparan sulfate proteoglycan.
21932778	4	89	used	occupied	659:666	arg2	sites					638:642	the potential N-glycosylation sites	608:642	the potential N-glycosylation sites	608:642	Mutagenesis and enzymatic cleavage indicated that the potential N-glycosylation sites are invariably occupied.
21932778	4	90	theme	enzymatic	574:582	arg1	cleavage					584:591	enzymatic cleavage	574:591	enzymatic cleavage	574:591	Mutagenesis and enzymatic cleavage indicated that the potential N-glycosylation sites are invariably occupied.
21932778	8	91	theme	fluorescence	1551:1562	arg1	spectroscopy					1573:1584	fluorescence emission spectroscopy	1551:1584	fluorescence emission spectroscopy	1551:1584	A single unfolding transition at high concentrations of urea was found for both N-deglycosylated glypican-1 and glypican-1 in which the N-glycosylation sites had been removed by mutagenesis when chemical denaturation was monitored by circular dichroism and fluorescence emission spectroscopy.
21932778	6	92	theme	N-glycosylation	909:923	arg1	N116Q					932:936	N-glycosylation mutant N116Q	909:936	N-glycosylation mutant N116Q	909:936	Heparan sulfate substitution of N-glycosylation mutant N116Q was similar to wild-type glypican-1 while the N79Q mutant and also the double mutant N79Q,N116Q were mostly secreted as high-molecular-weight heparan sulfate proteoglycan.
21932778	3	93	gly	N-glycosylation	446:460	arg2	Asn-116					482:488	Asn-116	482:488	Asn-116	482:488	Here, we studied the role of the possible N-glycosylation sites at Asn-79 and Asn-116 in recombinant anchorless glypican-1 expressed in eukaryotic cells.
21932778	3	93	gly	N-glycosylation	446:460	arg2	Asn-79					471:476	Asn-79	471:476	Asn-79	471:476	Here, we studied the role of the possible N-glycosylation sites at Asn-79 and Asn-116 in recombinant anchorless glypican-1 expressed in eukaryotic cells.
21932778	3	93	gly	N-glycosylation	446:460	arg2	sites					462:466	the possible N-glycosylation sites	433:466	the possible N-glycosylation sites at Asn-79 and Asn-116	433:488	Here, we studied the role of the possible N-glycosylation sites at Asn-79 and Asn-116 in recombinant anchorless glypican-1 expressed in eukaryotic cells.
21932778	3	94	theme	recombinant	493:503	arg1	glypican-1					516:525	recombinant anchorless glypican-1	493:525	recombinant anchorless glypican-1 expressed in eukaryotic cells	493:555	Here, we studied the role of the possible N-glycosylation sites at Asn-79 and Asn-116 in recombinant anchorless glypican-1 expressed in eukaryotic cells.
21932778	9	95	theme	correct	1804:1810	arg1	folding					1812:1818	correct folding	1804:1818	correct folding	1804:1818	In summary, we have found that the potential N-glycosylation sites in glypican-1 are invariably occupied and that the N-linked glycans on glypican-1 affect protein expression and heparan sulfate substitution but that correct folding can be obtained in the absence of N-linked glycans.
9884403	1	0	gly	N-glycosylation	93:107	arg1	glycoprotein					138:149	human Tamm-Horsfall glycoprotein	118:149	human Tamm-Horsfall glycoprotein from one healthy male donor	118:177	The N-glycosylation sites of human Tamm-Horsfall glycoprotein from one healthy male donor have been characterized, based on an approach using endoproteinase Glu-C (V-8 protease, Staphylococcus aureus ) digestion and a combination of chromatographic techniques, automated Edman sequencing, and fast atom bombardment mass spectrometry.
9884403	1	0	gly	N-glycosylation	93:107	arg2	glycoprotein					138:149	human Tamm-Horsfall glycoprotein	118:149	human Tamm-Horsfall glycoprotein from one healthy male donor	118:177	The N-glycosylation sites of human Tamm-Horsfall glycoprotein from one healthy male donor have been characterized, based on an approach using endoproteinase Glu-C (V-8 protease, Staphylococcus aureus ) digestion and a combination of chromatographic techniques, automated Edman sequencing, and fast atom bombardment mass spectrometry.
9884403	1	0	gly	N-glycosylation	93:107	arg2	donor					173:177	one healthy male donor	156:177	one healthy male donor	156:177	The N-glycosylation sites of human Tamm-Horsfall glycoprotein from one healthy male donor have been characterized, based on an approach using endoproteinase Glu-C (V-8 protease, Staphylococcus aureus ) digestion and a combination of chromatographic techniques, automated Edman sequencing, and fast atom bombardment mass spectrometry.
9884403	1	0	gly	N-glycosylation	93:107	arg2	sites					109:113	The N-glycosylation sites	89:113	The N-glycosylation sites of human Tamm-Horsfall glycoprotein from one healthy male donor	89:177	The N-glycosylation sites of human Tamm-Horsfall glycoprotein from one healthy male donor have been characterized, based on an approach using endoproteinase Glu-C (V-8 protease, Staphylococcus aureus ) digestion and a combination of chromatographic techniques, automated Edman sequencing, and fast atom bombardment mass spectrometry.
9884403	1	1	theme	Edman	360:364	arg1	sequencing					366:375	automated Edman sequencing	350:375	automated Edman sequencing	350:375	The N-glycosylation sites of human Tamm-Horsfall glycoprotein from one healthy male donor have been characterized, based on an approach using endoproteinase Glu-C (V-8 protease, Staphylococcus aureus ) digestion and a combination of chromatographic techniques, automated Edman sequencing, and fast atom bombardment mass spectrometry.
9884403	4	2	theme	Glycosylation	850:862	arg1	Asn489					869:874	Glycosylation site Asn489	850:874	Glycosylation site Asn489	850:874	Glycosylation site Asn489 contains mainly di- and tri-charged oligosaccharides which comprise, among others, the GalNAc4 S (beta1-4)GlcNAc terminal sequence.
9884403	0	3	from	glycosylation	38:50	arg1	glycoprotein					75:86	human Tamm-Horsfall glycoprotein	55:86	human Tamm-Horsfall glycoprotein	55:86	Glycosylation sites and site-specific glycosylation in human Tamm-Horsfall glycoprotein.
9884403	2	4	from	Asn14	616:620	arg1	site					608:611	the potential glycosylation site	580:611	the potential glycosylation site	580:611	Seven out of the eight potential N-glycosylation sites, namely, Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489, turned out to be glycosylated, and the potential glycosylation site at Asn14, being close to the N-terminus, is not used.
9884403	5	5	theme	Man5GlcNAc2to	1096:1108	arg1	Man8GlcNAc2					1110:1120	Man5GlcNAc2to Man8GlcNAc2	1096:1120	Man5GlcNAc2to Man8GlcNAc2	1096:1120	Only glycosylation site Asn251 bears oligomannose-type carbohydrate chains ranging from Man5GlcNAc2to Man8GlcNAc2, in addition to a small amount of complex-type structures.
9884403	3	6	theme	chromatographic	792:806	arg1	profiling					808:816	high-pH anion-exchange chromatographic profiling	769:816	high-pH anion-exchange chromatographic profiling	769:816	The carbohydrate microheterogeneity on three of the glycosylation sites was studied in more detail by high-pH anion-exchange chromatographic profiling and 500 MHz1H-NMR spectroscopy.
9884403	4	7	theme	tri-charged	900:910	arg1	oligosaccharides					912:927	tri-charged oligosaccharides	900:927	tri-charged oligosaccharides	900:927	Glycosylation site Asn489 contains mainly di- and tri-charged oligosaccharides which comprise, among others, the GalNAc4 S (beta1-4)GlcNAc terminal sequence.
9884403	0	8	from	sites	14:18	arg1	glycoprotein					75:86	human Tamm-Horsfall glycoprotein	55:86	human Tamm-Horsfall glycoprotein	55:86	Glycosylation sites and site-specific glycosylation in human Tamm-Horsfall glycoprotein.
9884403	6	9	theme	similar	1263:1269	arg1	heterogeneity					1248:1260	a large heterogeneity	1240:1260	a large heterogeneity	1240:1260	Profiling of the carbohydrate moieties of Asn208 indicates a large heterogeneity, similar to that established for native human Tamm-Horsfall glycoprotein, namely, multiply charged complex-type carbohydrate structures, terminated by sulfate groups, sialic acid residues, and/or the Sda-determinant.
9884403	5	10	theme	complex-type	1156:1167	arg1	structures					1169:1178	complex-type structures	1156:1178	complex-type structures	1156:1178	Only glycosylation site Asn251 bears oligomannose-type carbohydrate chains ranging from Man5GlcNAc2to Man8GlcNAc2, in addition to a small amount of complex-type structures.
9884403	6	11	theme	sulfate	1413:1419	arg1	groups					1421:1426	sulfate groups	1413:1426	sulfate groups	1413:1426	Profiling of the carbohydrate moieties of Asn208 indicates a large heterogeneity, similar to that established for native human Tamm-Horsfall glycoprotein, namely, multiply charged complex-type carbohydrate structures, terminated by sulfate groups, sialic acid residues, and/or the Sda-determinant.
9884403	5	12	theme	carbohydrate	1063:1074	arg1	chains					1076:1081	oligomannose-type carbohydrate chains	1045:1081	oligomannose-type carbohydrate chains ranging from Man5GlcNAc2to Man8GlcNAc2	1045:1120	Only glycosylation site Asn251 bears oligomannose-type carbohydrate chains ranging from Man5GlcNAc2to Man8GlcNAc2, in addition to a small amount of complex-type structures.
9884403	3	13	gly	glycosylation	719:731	arg2	sites					733:737	the glycosylation sites	715:737	the glycosylation sites	715:737	The carbohydrate microheterogeneity on three of the glycosylation sites was studied in more detail by high-pH anion-exchange chromatographic profiling and 500 MHz1H-NMR spectroscopy.
9884403	5	14	theme	Only	1008:1011	arg1	Asn251					1032:1037	Only glycosylation site Asn251	1008:1037	Only glycosylation site Asn251	1008:1037	Only glycosylation site Asn251 bears oligomannose-type carbohydrate chains ranging from Man5GlcNAc2to Man8GlcNAc2, in addition to a small amount of complex-type structures.
9884403	0	15	gly	glycoprotein	75:86	arg1	glycoprotein					75:86	human Tamm-Horsfall glycoprotein	55:86	human Tamm-Horsfall glycoprotein	55:86	Glycosylation sites and site-specific glycosylation in human Tamm-Horsfall glycoprotein.
9884403	6	16	dep	that	1274:1277	arg1	established					1279:1289	established	1279:1289	established for native human Tamm-Horsfall glycoprotein, namely, multiply charged complex-type carbohydrate structures, terminated by sulfate groups, sialic acid residues, and/or the Sda-determinant	1279:1476	Profiling of the carbohydrate moieties of Asn208 indicates a large heterogeneity, similar to that established for native human Tamm-Horsfall glycoprotein, namely, multiply charged complex-type carbohydrate structures, terminated by sulfate groups, sialic acid residues, and/or the Sda-determinant.
9884403	3	17	theme	high-pH	769:775	arg1	profiling					808:816	high-pH anion-exchange chromatographic profiling	769:816	high-pH anion-exchange chromatographic profiling	769:816	The carbohydrate microheterogeneity on three of the glycosylation sites was studied in more detail by high-pH anion-exchange chromatographic profiling and 500 MHz1H-NMR spectroscopy.
9884403	3	18	theme	carbohydrate	671:682	arg1	microheterogeneity					684:701	The carbohydrate microheterogeneity	667:701	The carbohydrate microheterogeneity on three of the glycosylation sites	667:737	The carbohydrate microheterogeneity on three of the glycosylation sites was studied in more detail by high-pH anion-exchange chromatographic profiling and 500 MHz1H-NMR spectroscopy.
9884403	4	19	theme	site	864:867	arg1	Asn489					869:874	Glycosylation site Asn489	850:874	Glycosylation site Asn489	850:874	Glycosylation site Asn489 contains mainly di- and tri-charged oligosaccharides which comprise, among others, the GalNAc4 S (beta1-4)GlcNAc terminal sequence.
9884403	3	20	from	microheterogeneity	684:701	arg1	sites					733:737	the glycosylation sites	715:737	the glycosylation sites	715:737	The carbohydrate microheterogeneity on three of the glycosylation sites was studied in more detail by high-pH anion-exchange chromatographic profiling and 500 MHz1H-NMR spectroscopy.
9884403	3	20	from	microheterogeneity	684:701	arg1	three					706:710	three	706:710	three	706:710	The carbohydrate microheterogeneity on three of the glycosylation sites was studied in more detail by high-pH anion-exchange chromatographic profiling and 500 MHz1H-NMR spectroscopy.
9884403	3	21	theme	anion-exchange	777:790	arg1	profiling					808:816	high-pH anion-exchange chromatographic profiling	769:816	high-pH anion-exchange chromatographic profiling	769:816	The carbohydrate microheterogeneity on three of the glycosylation sites was studied in more detail by high-pH anion-exchange chromatographic profiling and 500 MHz1H-NMR spectroscopy.
9884403	1	22	theme	fast	382:385	arg1	spectrometry					409:420	fast atom bombardment mass spectrometry	382:420	fast atom bombardment mass spectrometry	382:420	The N-glycosylation sites of human Tamm-Horsfall glycoprotein from one healthy male donor have been characterized, based on an approach using endoproteinase Glu-C (V-8 protease, Staphylococcus aureus ) digestion and a combination of chromatographic techniques, automated Edman sequencing, and fast atom bombardment mass spectrometry.
9884403	1	23	from	donor	173:177	arg1	glycoprotein					138:149	human Tamm-Horsfall glycoprotein	118:149	human Tamm-Horsfall glycoprotein from one healthy male donor	118:177	The N-glycosylation sites of human Tamm-Horsfall glycoprotein from one healthy male donor have been characterized, based on an approach using endoproteinase Glu-C (V-8 protease, Staphylococcus aureus ) digestion and a combination of chromatographic techniques, automated Edman sequencing, and fast atom bombardment mass spectrometry.
9884403	1	23	from	donor	173:177	arg1	sites					109:113	The N-glycosylation sites	89:113	The N-glycosylation sites of human Tamm-Horsfall glycoprotein from one healthy male donor	89:177	The N-glycosylation sites of human Tamm-Horsfall glycoprotein from one healthy male donor have been characterized, based on an approach using endoproteinase Glu-C (V-8 protease, Staphylococcus aureus ) digestion and a combination of chromatographic techniques, automated Edman sequencing, and fast atom bombardment mass spectrometry.
9884403	2	24	gly	glycosylation	594:606	arg2	site					608:611	the potential glycosylation site	580:611	the potential glycosylation site	580:611	Seven out of the eight potential N-glycosylation sites, namely, Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489, turned out to be glycosylated, and the potential glycosylation site at Asn14, being close to the N-terminus, is not used.
9884403	2	24	gly	glycosylation	594:606	arg2	Asn14					616:620	Asn14	616:620	Asn14	616:620	Seven out of the eight potential N-glycosylation sites, namely, Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489, turned out to be glycosylated, and the potential glycosylation site at Asn14, being close to the N-terminus, is not used.
9884403	4	25	theme	GlcNAc	982:987	arg1	sequence					998:1005	the GalNAc4 S (beta1-4)GlcNAc terminal sequence	959:1005	the GalNAc4 S (beta1-4)GlcNAc terminal sequence	959:1005	Glycosylation site Asn489 contains mainly di- and tri-charged oligosaccharides which comprise, among others, the GalNAc4 S (beta1-4)GlcNAc terminal sequence.
9884403	1	26	theme	atom	387:390	arg1	spectrometry					409:420	fast atom bombardment mass spectrometry	382:420	fast atom bombardment mass spectrometry	382:420	The N-glycosylation sites of human Tamm-Horsfall glycoprotein from one healthy male donor have been characterized, based on an approach using endoproteinase Glu-C (V-8 protease, Staphylococcus aureus ) digestion and a combination of chromatographic techniques, automated Edman sequencing, and fast atom bombardment mass spectrometry.
9884403	2	27	theme	glycosylation	594:606	arg1	site					608:611	the potential glycosylation site	580:611	the potential glycosylation site	580:611	Seven out of the eight potential N-glycosylation sites, namely, Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489, turned out to be glycosylated, and the potential glycosylation site at Asn14, being close to the N-terminus, is not used.
9884403	1	28	theme	N-glycosylation	93:107	arg1	glycoprotein					138:149	human Tamm-Horsfall glycoprotein	118:149	human Tamm-Horsfall glycoprotein from one healthy male donor	118:177	The N-glycosylation sites of human Tamm-Horsfall glycoprotein from one healthy male donor have been characterized, based on an approach using endoproteinase Glu-C (V-8 protease, Staphylococcus aureus ) digestion and a combination of chromatographic techniques, automated Edman sequencing, and fast atom bombardment mass spectrometry.
9884403	1	28	theme	N-glycosylation	93:107	arg1	sites					109:113	The N-glycosylation sites	89:113	The N-glycosylation sites of human Tamm-Horsfall glycoprotein from one healthy male donor	89:177	The N-glycosylation sites of human Tamm-Horsfall glycoprotein from one healthy male donor have been characterized, based on an approach using endoproteinase Glu-C (V-8 protease, Staphylococcus aureus ) digestion and a combination of chromatographic techniques, automated Edman sequencing, and fast atom bombardment mass spectrometry.
9884403	4	29	contain	contains	876:883	arg2	oligosaccharides					912:927	tri-charged oligosaccharides	900:927	tri-charged oligosaccharides	900:927	Glycosylation site Asn489 contains mainly di- and tri-charged oligosaccharides which comprise, among others, the GalNAc4 S (beta1-4)GlcNAc terminal sequence.
9884403	4	29	contain	contains	876:883	arg2	di-					892:894	di-	892:894	di-	892:894	Glycosylation site Asn489 contains mainly di- and tri-charged oligosaccharides which comprise, among others, the GalNAc4 S (beta1-4)GlcNAc terminal sequence.
9884403	4	29	contain	contains	876:883	arg1	Asn489					869:874	Glycosylation site Asn489	850:874	Glycosylation site Asn489	850:874	Glycosylation site Asn489 contains mainly di- and tri-charged oligosaccharides which comprise, among others, the GalNAc4 S (beta1-4)GlcNAc terminal sequence.
9884403	3	30	theme	glycosylation	719:731	arg1	sites					733:737	the glycosylation sites	715:737	the glycosylation sites	715:737	The carbohydrate microheterogeneity on three of the glycosylation sites was studied in more detail by high-pH anion-exchange chromatographic profiling and 500 MHz1H-NMR spectroscopy.
9884403	1	31	theme	bombardment	392:402	arg1	spectrometry					409:420	fast atom bombardment mass spectrometry	382:420	fast atom bombardment mass spectrometry	382:420	The N-glycosylation sites of human Tamm-Horsfall glycoprotein from one healthy male donor have been characterized, based on an approach using endoproteinase Glu-C (V-8 protease, Staphylococcus aureus ) digestion and a combination of chromatographic techniques, automated Edman sequencing, and fast atom bombardment mass spectrometry.
9884403	2	32	theme	potential	584:592	arg1	site					608:611	the potential glycosylation site	580:611	the potential glycosylation site	580:611	Seven out of the eight potential N-glycosylation sites, namely, Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489, turned out to be glycosylated, and the potential glycosylation site at Asn14, being close to the N-terminus, is not used.
9884403	6	33	theme	Tamm-Horsfall	1308:1320	arg1	glycoprotein					1322:1333	native human Tamm-Horsfall glycoprotein	1295:1333	native human Tamm-Horsfall glycoprotein	1295:1333	Profiling of the carbohydrate moieties of Asn208 indicates a large heterogeneity, similar to that established for native human Tamm-Horsfall glycoprotein, namely, multiply charged complex-type carbohydrate structures, terminated by sulfate groups, sialic acid residues, and/or the Sda-determinant.
9884403	5	34	theme	structures	1169:1178	arg1	amount					1146:1151	a small amount	1138:1151	a small amount of complex-type structures	1138:1178	Only glycosylation site Asn251 bears oligomannose-type carbohydrate chains ranging from Man5GlcNAc2to Man8GlcNAc2, in addition to a small amount of complex-type structures.
9884403	5	34	theme	structures	1169:1178	arg1	structures					1169:1178	complex-type structures	1156:1178	complex-type structures	1156:1178	Only glycosylation site Asn251 bears oligomannose-type carbohydrate chains ranging from Man5GlcNAc2to Man8GlcNAc2, in addition to a small amount of complex-type structures.
9884403	6	35	theme	acid	1436:1439	arg1	residues					1441:1448	sialic acid residues	1429:1448	sialic acid residues	1429:1448	Profiling of the carbohydrate moieties of Asn208 indicates a large heterogeneity, similar to that established for native human Tamm-Horsfall glycoprotein, namely, multiply charged complex-type carbohydrate structures, terminated by sulfate groups, sialic acid residues, and/or the Sda-determinant.
9884403	0	36	theme	Glycosylation	0:12	arg1	sites					14:18	Glycosylation sites	0:18	Glycosylation sites	0:18	Glycosylation sites and site-specific glycosylation in human Tamm-Horsfall glycoprotein.
9884403	5	37	theme	oligomannose-type	1045:1061	arg1	chains					1076:1081	oligomannose-type carbohydrate chains	1045:1081	oligomannose-type carbohydrate chains ranging from Man5GlcNAc2to Man8GlcNAc2	1045:1120	Only glycosylation site Asn251 bears oligomannose-type carbohydrate chains ranging from Man5GlcNAc2to Man8GlcNAc2, in addition to a small amount of complex-type structures.
9884403	6	38	theme	charged	1353:1359	arg1	structures					1387:1396	multiply charged complex-type carbohydrate structures	1344:1396	multiply charged complex-type carbohydrate structures	1344:1396	Profiling of the carbohydrate moieties of Asn208 indicates a large heterogeneity, similar to that established for native human Tamm-Horsfall glycoprotein, namely, multiply charged complex-type carbohydrate structures, terminated by sulfate groups, sialic acid residues, and/or the Sda-determinant.
9884403	6	39	gly	glycoprotein	1322:1333	arg1	glycoprotein					1322:1333	native human Tamm-Horsfall glycoprotein	1295:1333	native human Tamm-Horsfall glycoprotein	1295:1333	Profiling of the carbohydrate moieties of Asn208 indicates a large heterogeneity, similar to that established for native human Tamm-Horsfall glycoprotein, namely, multiply charged complex-type carbohydrate structures, terminated by sulfate groups, sialic acid residues, and/or the Sda-determinant.
9884403	0	40	theme	site-specific	24:36	arg1	glycosylation					38:50	site-specific glycosylation	24:50	site-specific glycosylation	24:50	Glycosylation sites and site-specific glycosylation in human Tamm-Horsfall glycoprotein.
9884403	6	41	theme	moieties	1211:1218	arg1	Profiling					1181:1189	Profiling	1181:1189	Profiling of the carbohydrate moieties of Asn208	1181:1228	Profiling of the carbohydrate moieties of Asn208 indicates a large heterogeneity, similar to that established for native human Tamm-Horsfall glycoprotein, namely, multiply charged complex-type carbohydrate structures, terminated by sulfate groups, sialic acid residues, and/or the Sda-determinant.
9884403	6	42	theme	carbohydrate	1374:1385	arg1	structures					1387:1396	multiply charged complex-type carbohydrate structures	1344:1396	multiply charged complex-type carbohydrate structures	1344:1396	Profiling of the carbohydrate moieties of Asn208 indicates a large heterogeneity, similar to that established for native human Tamm-Horsfall glycoprotein, namely, multiply charged complex-type carbohydrate structures, terminated by sulfate groups, sialic acid residues, and/or the Sda-determinant.
9884403	1	43	theme	human	118:122	arg1	glycoprotein					138:149	human Tamm-Horsfall glycoprotein	118:149	human Tamm-Horsfall glycoprotein from one healthy male donor	118:177	The N-glycosylation sites of human Tamm-Horsfall glycoprotein from one healthy male donor have been characterized, based on an approach using endoproteinase Glu-C (V-8 protease, Staphylococcus aureus ) digestion and a combination of chromatographic techniques, automated Edman sequencing, and fast atom bombardment mass spectrometry.
9884403	2	44	theme	potential	446:454	arg1	sites					472:476	the eight potential N-glycosylation sites	436:476	the eight potential N-glycosylation sites	436:476	Seven out of the eight potential N-glycosylation sites, namely, Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489, turned out to be glycosylated, and the potential glycosylation site at Asn14, being close to the N-terminus, is not used.
9884403	1	45	gly	glycoprotein	138:149	arg1	glycoprotein					138:149	human Tamm-Horsfall glycoprotein	118:149	human Tamm-Horsfall glycoprotein from one healthy male donor	118:177	The N-glycosylation sites of human Tamm-Horsfall glycoprotein from one healthy male donor have been characterized, based on an approach using endoproteinase Glu-C (V-8 protease, Staphylococcus aureus ) digestion and a combination of chromatographic techniques, automated Edman sequencing, and fast atom bombardment mass spectrometry.
9884403	1	46	theme	mass	404:407	arg1	spectrometry					409:420	fast atom bombardment mass spectrometry	382:420	fast atom bombardment mass spectrometry	382:420	The N-glycosylation sites of human Tamm-Horsfall glycoprotein from one healthy male donor have been characterized, based on an approach using endoproteinase Glu-C (V-8 protease, Staphylococcus aureus ) digestion and a combination of chromatographic techniques, automated Edman sequencing, and fast atom bombardment mass spectrometry.
9884403	1	47	theme	Tamm-Horsfall	124:136	arg1	glycoprotein					138:149	human Tamm-Horsfall glycoprotein	118:149	human Tamm-Horsfall glycoprotein from one healthy male donor	118:177	The N-glycosylation sites of human Tamm-Horsfall glycoprotein from one healthy male donor have been characterized, based on an approach using endoproteinase Glu-C (V-8 protease, Staphylococcus aureus ) digestion and a combination of chromatographic techniques, automated Edman sequencing, and fast atom bombardment mass spectrometry.
9884403	6	48	theme	human	1302:1306	arg1	glycoprotein					1322:1333	native human Tamm-Horsfall glycoprotein	1295:1333	native human Tamm-Horsfall glycoprotein	1295:1333	Profiling of the carbohydrate moieties of Asn208 indicates a large heterogeneity, similar to that established for native human Tamm-Horsfall glycoprotein, namely, multiply charged complex-type carbohydrate structures, terminated by sulfate groups, sialic acid residues, and/or the Sda-determinant.
9884403	6	49	theme	carbohydrate	1198:1209	arg1	moieties					1211:1218	the carbohydrate moieties	1194:1218	the carbohydrate moieties of Asn208	1194:1228	Profiling of the carbohydrate moieties of Asn208 indicates a large heterogeneity, similar to that established for native human Tamm-Horsfall glycoprotein, namely, multiply charged complex-type carbohydrate structures, terminated by sulfate groups, sialic acid residues, and/or the Sda-determinant.
9884403	5	50	contain	bears	1039:1043	arg3	amount					1146:1151	a small amount	1138:1151	a small amount of complex-type structures	1138:1178	Only glycosylation site Asn251 bears oligomannose-type carbohydrate chains ranging from Man5GlcNAc2to Man8GlcNAc2, in addition to a small amount of complex-type structures.
9884403	5	50	contain	bears	1039:1043	arg2	chains					1076:1081	oligomannose-type carbohydrate chains	1045:1081	oligomannose-type carbohydrate chains ranging from Man5GlcNAc2to Man8GlcNAc2	1045:1120	Only glycosylation site Asn251 bears oligomannose-type carbohydrate chains ranging from Man5GlcNAc2to Man8GlcNAc2, in addition to a small amount of complex-type structures.
9884403	5	50	contain	bears	1039:1043	arg1	Asn251					1032:1037	Only glycosylation site Asn251	1008:1037	Only glycosylation site Asn251	1008:1037	Only glycosylation site Asn251 bears oligomannose-type carbohydrate chains ranging from Man5GlcNAc2to Man8GlcNAc2, in addition to a small amount of complex-type structures.
9884403	5	50	contain	bears	1039:1043	arg3	structures					1169:1178	complex-type structures	1156:1178	complex-type structures	1156:1178	Only glycosylation site Asn251 bears oligomannose-type carbohydrate chains ranging from Man5GlcNAc2to Man8GlcNAc2, in addition to a small amount of complex-type structures.
9884403	2	51	theme	N-glycosylation	456:470	arg1	sites					472:476	the eight potential N-glycosylation sites	436:476	the eight potential N-glycosylation sites	436:476	Seven out of the eight potential N-glycosylation sites, namely, Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489, turned out to be glycosylated, and the potential glycosylation site at Asn14, being close to the N-terminus, is not used.
9884403	1	52	theme	endoproteinase	231:244	arg1	digestion					291:299	endoproteinase Glu-C (V-8 protease, Staphylococcus aureus ) digestion	231:299	endoproteinase Glu-C (V-8 protease, Staphylococcus aureus ) digestion	231:299	The N-glycosylation sites of human Tamm-Horsfall glycoprotein from one healthy male donor have been characterized, based on an approach using endoproteinase Glu-C (V-8 protease, Staphylococcus aureus ) digestion and a combination of chromatographic techniques, automated Edman sequencing, and fast atom bombardment mass spectrometry.
9884403	0	53	theme	Tamm-Horsfall	61:73	arg1	glycoprotein					75:86	human Tamm-Horsfall glycoprotein	55:86	human Tamm-Horsfall glycoprotein	55:86	Glycosylation sites and site-specific glycosylation in human Tamm-Horsfall glycoprotein.
9884403	1	54	theme	chromatographic	322:336	arg1	techniques					338:347	chromatographic techniques	322:347	chromatographic techniques	322:347	The N-glycosylation sites of human Tamm-Horsfall glycoprotein from one healthy male donor have been characterized, based on an approach using endoproteinase Glu-C (V-8 protease, Staphylococcus aureus ) digestion and a combination of chromatographic techniques, automated Edman sequencing, and fast atom bombardment mass spectrometry.
9884403	1	55	dep	characterized	189:201	arg1	based					204:208	based	204:208	based on an approach using endoproteinase Glu-C (V-8 protease, Staphylococcus aureus ) digestion and a combination of chromatographic techniques, automated Edman sequencing, and fast atom bombardment mass spectrometry	204:420	The N-glycosylation sites of human Tamm-Horsfall glycoprotein from one healthy male donor have been characterized, based on an approach using endoproteinase Glu-C (V-8 protease, Staphylococcus aureus ) digestion and a combination of chromatographic techniques, automated Edman sequencing, and fast atom bombardment mass spectrometry.
9884403	5	56	dep	amount	1146:1151	arg1	addition					1126:1133	addition	1126:1133	addition	1126:1133	Only glycosylation site Asn251 bears oligomannose-type carbohydrate chains ranging from Man5GlcNAc2to Man8GlcNAc2, in addition to a small amount of complex-type structures.
9884403	1	57	theme	glycoprotein	138:149	arg1	glycoprotein					138:149	human Tamm-Horsfall glycoprotein	118:149	human Tamm-Horsfall glycoprotein from one healthy male donor	118:177	The N-glycosylation sites of human Tamm-Horsfall glycoprotein from one healthy male donor have been characterized, based on an approach using endoproteinase Glu-C (V-8 protease, Staphylococcus aureus ) digestion and a combination of chromatographic techniques, automated Edman sequencing, and fast atom bombardment mass spectrometry.
9884403	1	57	theme	glycoprotein	138:149	arg1	sites					109:113	The N-glycosylation sites	89:113	The N-glycosylation sites of human Tamm-Horsfall glycoprotein from one healthy male donor	89:177	The N-glycosylation sites of human Tamm-Horsfall glycoprotein from one healthy male donor have been characterized, based on an approach using endoproteinase Glu-C (V-8 protease, Staphylococcus aureus ) digestion and a combination of chromatographic techniques, automated Edman sequencing, and fast atom bombardment mass spectrometry.
9884403	0	58	theme	human	55:59	arg1	glycoprotein					75:86	human Tamm-Horsfall glycoprotein	55:86	human Tamm-Horsfall glycoprotein	55:86	Glycosylation sites and site-specific glycosylation in human Tamm-Horsfall glycoprotein.
9884403	1	59	theme	techniques	338:347	arg1	sequencing					366:375	automated Edman sequencing	350:375	automated Edman sequencing	350:375	The N-glycosylation sites of human Tamm-Horsfall glycoprotein from one healthy male donor have been characterized, based on an approach using endoproteinase Glu-C (V-8 protease, Staphylococcus aureus ) digestion and a combination of chromatographic techniques, automated Edman sequencing, and fast atom bombardment mass spectrometry.
9884403	1	59	theme	techniques	338:347	arg1	digestion					291:299	endoproteinase Glu-C (V-8 protease, Staphylococcus aureus ) digestion	231:299	endoproteinase Glu-C (V-8 protease, Staphylococcus aureus ) digestion	231:299	The N-glycosylation sites of human Tamm-Horsfall glycoprotein from one healthy male donor have been characterized, based on an approach using endoproteinase Glu-C (V-8 protease, Staphylococcus aureus ) digestion and a combination of chromatographic techniques, automated Edman sequencing, and fast atom bombardment mass spectrometry.
9884403	1	59	theme	techniques	338:347	arg1	combination					307:317	a combination	305:317	a combination of chromatographic techniques	305:347	The N-glycosylation sites of human Tamm-Horsfall glycoprotein from one healthy male donor have been characterized, based on an approach using endoproteinase Glu-C (V-8 protease, Staphylococcus aureus ) digestion and a combination of chromatographic techniques, automated Edman sequencing, and fast atom bombardment mass spectrometry.
9884403	1	59	theme	techniques	338:347	arg1	spectrometry					409:420	fast atom bombardment mass spectrometry	382:420	fast atom bombardment mass spectrometry	382:420	The N-glycosylation sites of human Tamm-Horsfall glycoprotein from one healthy male donor have been characterized, based on an approach using endoproteinase Glu-C (V-8 protease, Staphylococcus aureus ) digestion and a combination of chromatographic techniques, automated Edman sequencing, and fast atom bombardment mass spectrometry.
9884403	6	60	theme	complex-type	1361:1372	arg1	structures					1387:1396	multiply charged complex-type carbohydrate structures	1344:1396	multiply charged complex-type carbohydrate structures	1344:1396	Profiling of the carbohydrate moieties of Asn208 indicates a large heterogeneity, similar to that established for native human Tamm-Horsfall glycoprotein, namely, multiply charged complex-type carbohydrate structures, terminated by sulfate groups, sialic acid residues, and/or the Sda-determinant.
9884403	5	61	theme	site	1027:1030	arg1	Asn251					1032:1037	Only glycosylation site Asn251	1008:1037	Only glycosylation site Asn251	1008:1037	Only glycosylation site Asn251 bears oligomannose-type carbohydrate chains ranging from Man5GlcNAc2to Man8GlcNAc2, in addition to a small amount of complex-type structures.
9884403	5	62	theme	glycosylation	1013:1025	arg1	Asn251					1032:1037	Only glycosylation site Asn251	1008:1037	Only glycosylation site Asn251	1008:1037	Only glycosylation site Asn251 bears oligomannose-type carbohydrate chains ranging from Man5GlcNAc2to Man8GlcNAc2, in addition to a small amount of complex-type structures.
9884403	3	63	theme	MHz1H-NMR	826:834	arg1	spectroscopy					836:847	500 MHz1H-NMR spectroscopy	822:847	500 MHz1H-NMR spectroscopy	822:847	The carbohydrate microheterogeneity on three of the glycosylation sites was studied in more detail by high-pH anion-exchange chromatographic profiling and 500 MHz1H-NMR spectroscopy.
9884403	3	64	theme	sites	733:737	arg1	sites					733:737	the glycosylation sites	715:737	the glycosylation sites	715:737	The carbohydrate microheterogeneity on three of the glycosylation sites was studied in more detail by high-pH anion-exchange chromatographic profiling and 500 MHz1H-NMR spectroscopy.
9884403	3	64	theme	sites	733:737	arg1	three					706:710	three	706:710	three	706:710	The carbohydrate microheterogeneity on three of the glycosylation sites was studied in more detail by high-pH anion-exchange chromatographic profiling and 500 MHz1H-NMR spectroscopy.
9884403	6	65	theme	native	1295:1300	arg1	glycoprotein					1322:1333	native human Tamm-Horsfall glycoprotein	1295:1333	native human Tamm-Horsfall glycoprotein	1295:1333	Profiling of the carbohydrate moieties of Asn208 indicates a large heterogeneity, similar to that established for native human Tamm-Horsfall glycoprotein, namely, multiply charged complex-type carbohydrate structures, terminated by sulfate groups, sialic acid residues, and/or the Sda-determinant.
9884403	6	66	theme	Asn208	1223:1228	arg1	moieties					1211:1218	the carbohydrate moieties	1194:1218	the carbohydrate moieties of Asn208	1194:1228	Profiling of the carbohydrate moieties of Asn208 indicates a large heterogeneity, similar to that established for native human Tamm-Horsfall glycoprotein, namely, multiply charged complex-type carbohydrate structures, terminated by sulfate groups, sialic acid residues, and/or the Sda-determinant.
9884403	0	67	gly	glycosylation	38:50	arg1	glycoprotein					75:86	human Tamm-Horsfall glycoprotein	55:86	human Tamm-Horsfall glycoprotein	55:86	Glycosylation sites and site-specific glycosylation in human Tamm-Horsfall glycoprotein.
9884403	6	68	theme	large	1242:1246	arg1	heterogeneity					1248:1260	a large heterogeneity	1240:1260	a large heterogeneity	1240:1260	Profiling of the carbohydrate moieties of Asn208 indicates a large heterogeneity, similar to that established for native human Tamm-Horsfall glycoprotein, namely, multiply charged complex-type carbohydrate structures, terminated by sulfate groups, sialic acid residues, and/or the Sda-determinant.
9884403	1	69	theme	Glu-C	246:250	arg1	digestion					291:299	endoproteinase Glu-C (V-8 protease, Staphylococcus aureus ) digestion	231:299	endoproteinase Glu-C (V-8 protease, Staphylococcus aureus ) digestion	231:299	The N-glycosylation sites of human Tamm-Horsfall glycoprotein from one healthy male donor have been characterized, based on an approach using endoproteinase Glu-C (V-8 protease, Staphylococcus aureus ) digestion and a combination of chromatographic techniques, automated Edman sequencing, and fast atom bombardment mass spectrometry.
9884403	1	70	dep	digestion	291:299	arg1	protease					257:264	V-8 protease	253:264	V-8 protease	253:264	The N-glycosylation sites of human Tamm-Horsfall glycoprotein from one healthy male donor have been characterized, based on an approach using endoproteinase Glu-C (V-8 protease, Staphylococcus aureus ) digestion and a combination of chromatographic techniques, automated Edman sequencing, and fast atom bombardment mass spectrometry.
9884403	1	70	dep	digestion	291:299	arg1	aureus					282:287	Staphylococcus aureus	267:287	Staphylococcus aureus	267:287	The N-glycosylation sites of human Tamm-Horsfall glycoprotein from one healthy male donor have been characterized, based on an approach using endoproteinase Glu-C (V-8 protease, Staphylococcus aureus ) digestion and a combination of chromatographic techniques, automated Edman sequencing, and fast atom bombardment mass spectrometry.
9884403	1	71	theme	healthy	160:166	arg1	donor					173:177	one healthy male donor	156:177	one healthy male donor	156:177	The N-glycosylation sites of human Tamm-Horsfall glycoprotein from one healthy male donor have been characterized, based on an approach using endoproteinase Glu-C (V-8 protease, Staphylococcus aureus ) digestion and a combination of chromatographic techniques, automated Edman sequencing, and fast atom bombardment mass spectrometry.
9884403	1	72	from	sites	109:113	arg1	donor					173:177	one healthy male donor	156:177	one healthy male donor	156:177	The N-glycosylation sites of human Tamm-Horsfall glycoprotein from one healthy male donor have been characterized, based on an approach using endoproteinase Glu-C (V-8 protease, Staphylococcus aureus ) digestion and a combination of chromatographic techniques, automated Edman sequencing, and fast atom bombardment mass spectrometry.
9884403	2	73	gly	glycosylated	562:573	arg1	Seven					423:427	Seven	423:427	Seven	423:427	Seven out of the eight potential N-glycosylation sites, namely, Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489, turned out to be glycosylated, and the potential glycosylation site at Asn14, being close to the N-terminus, is not used.
9884403	2	73	gly	glycosylated	562:573	arg1	Asn298					517:522	Asn298	517:522	Asn298	517:522	Seven out of the eight potential N-glycosylation sites, namely, Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489, turned out to be glycosylated, and the potential glycosylation site at Asn14, being close to the N-terminus, is not used.
9884403	2	73	gly	glycosylated	562:573	arg1	Asn56					494:498	Asn56	494:498	Asn56	494:498	Seven out of the eight potential N-glycosylation sites, namely, Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489, turned out to be glycosylated, and the potential glycosylation site at Asn14, being close to the N-terminus, is not used.
9884403	2	73	gly	glycosylated	562:573	arg1	Asn208					501:506	Asn208	501:506	Asn208	501:506	Seven out of the eight potential N-glycosylation sites, namely, Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489, turned out to be glycosylated, and the potential glycosylation site at Asn14, being close to the N-terminus, is not used.
9884403	2	73	gly	glycosylated	562:573	arg1	Asn372					525:530	Asn372	525:530	Asn372	525:530	Seven out of the eight potential N-glycosylation sites, namely, Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489, turned out to be glycosylated, and the potential glycosylation site at Asn14, being close to the N-terminus, is not used.
9884403	2	73	gly	glycosylated	562:573	arg1	Asn489					537:542	Asn489	537:542	Asn489	537:542	Seven out of the eight potential N-glycosylation sites, namely, Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489, turned out to be glycosylated, and the potential glycosylation site at Asn14, being close to the N-terminus, is not used.
9884403	2	73	gly	glycosylated	562:573	arg1	Asn52					487:491	Asn52	487:491	Asn52	487:491	Seven out of the eight potential N-glycosylation sites, namely, Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489, turned out to be glycosylated, and the potential glycosylation site at Asn14, being close to the N-terminus, is not used.
9884403	2	73	gly	glycosylated	562:573	arg1	Asn251					509:514	Asn251	509:514	Asn251	509:514	Seven out of the eight potential N-glycosylation sites, namely, Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489, turned out to be glycosylated, and the potential glycosylation site at Asn14, being close to the N-terminus, is not used.
9884403	5	74	theme	small	1140:1144	arg1	amount					1146:1151	a small amount	1138:1151	a small amount of complex-type structures	1138:1178	Only glycosylation site Asn251 bears oligomannose-type carbohydrate chains ranging from Man5GlcNAc2to Man8GlcNAc2, in addition to a small amount of complex-type structures.
9884403	5	74	theme	small	1140:1144	arg1	structures					1169:1178	complex-type structures	1156:1178	complex-type structures	1156:1178	Only glycosylation site Asn251 bears oligomannose-type carbohydrate chains ranging from Man5GlcNAc2to Man8GlcNAc2, in addition to a small amount of complex-type structures.
9884403	1	75	theme	male	168:171	arg1	donor					173:177	one healthy male donor	156:177	one healthy male donor	156:177	The N-glycosylation sites of human Tamm-Horsfall glycoprotein from one healthy male donor have been characterized, based on an approach using endoproteinase Glu-C (V-8 protease, Staphylococcus aureus ) digestion and a combination of chromatographic techniques, automated Edman sequencing, and fast atom bombardment mass spectrometry.
9884403	5	76	gly	glycosylation	1013:1025	arg2	site					1027:1030	Only glycosylation site Asn251	1008:1037	Only glycosylation site Asn251	1008:1037	Only glycosylation site Asn251 bears oligomannose-type carbohydrate chains ranging from Man5GlcNAc2to Man8GlcNAc2, in addition to a small amount of complex-type structures.
9884403	5	76	gly	glycosylation	1013:1025	arg2	Asn251					1032:1037	Only glycosylation site Asn251	1008:1037	Only glycosylation site Asn251	1008:1037	Only glycosylation site Asn251 bears oligomannose-type carbohydrate chains ranging from Man5GlcNAc2to Man8GlcNAc2, in addition to a small amount of complex-type structures.
9884403	1	77	theme	V-8	253:255	arg1	protease					257:264	V-8 protease	253:264	V-8 protease	253:264	The N-glycosylation sites of human Tamm-Horsfall glycoprotein from one healthy male donor have been characterized, based on an approach using endoproteinase Glu-C (V-8 protease, Staphylococcus aureus ) digestion and a combination of chromatographic techniques, automated Edman sequencing, and fast atom bombardment mass spectrometry.
9884403	1	77	theme	V-8	253:255	arg1	aureus					282:287	Staphylococcus aureus	267:287	Staphylococcus aureus	267:287	The N-glycosylation sites of human Tamm-Horsfall glycoprotein from one healthy male donor have been characterized, based on an approach using endoproteinase Glu-C (V-8 protease, Staphylococcus aureus ) digestion and a combination of chromatographic techniques, automated Edman sequencing, and fast atom bombardment mass spectrometry.
9884403	4	78	theme	terminal	989:996	arg1	sequence					998:1005	the GalNAc4 S (beta1-4)GlcNAc terminal sequence	959:1005	the GalNAc4 S (beta1-4)GlcNAc terminal sequence	959:1005	Glycosylation site Asn489 contains mainly di- and tri-charged oligosaccharides which comprise, among others, the GalNAc4 S (beta1-4)GlcNAc terminal sequence.
9884403	1	79	theme	automated	350:358	arg1	sequencing					366:375	automated Edman sequencing	350:375	automated Edman sequencing	350:375	The N-glycosylation sites of human Tamm-Horsfall glycoprotein from one healthy male donor have been characterized, based on an approach using endoproteinase Glu-C (V-8 protease, Staphylococcus aureus ) digestion and a combination of chromatographic techniques, automated Edman sequencing, and fast atom bombardment mass spectrometry.
9884403	2	80	gly	N-glycosylation	456:470	arg2	eight					440:444	eight	440:444	eight	440:444	Seven out of the eight potential N-glycosylation sites, namely, Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489, turned out to be glycosylated, and the potential glycosylation site at Asn14, being close to the N-terminus, is not used.
9884403	2	80	gly	N-glycosylation	456:470	arg2	sites					472:476	the eight potential N-glycosylation sites	436:476	the eight potential N-glycosylation sites	436:476	Seven out of the eight potential N-glycosylation sites, namely, Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489, turned out to be glycosylated, and the potential glycosylation site at Asn14, being close to the N-terminus, is not used.
9884403	6	81	theme	sialic	1429:1434	arg1	residues					1441:1448	sialic acid residues	1429:1448	sialic acid residues	1429:1448	Profiling of the carbohydrate moieties of Asn208 indicates a large heterogeneity, similar to that established for native human Tamm-Horsfall glycoprotein, namely, multiply charged complex-type carbohydrate structures, terminated by sulfate groups, sialic acid residues, and/or the Sda-determinant.
9884403	2	82	used	used	661:664	arg2	site					608:611	the potential glycosylation site	580:611	the potential glycosylation site	580:611	Seven out of the eight potential N-glycosylation sites, namely, Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489, turned out to be glycosylated, and the potential glycosylation site at Asn14, being close to the N-terminus, is not used.
9884403	2	82	used	used	661:664	arg2	Asn14					616:620	Asn14	616:620	Asn14	616:620	Seven out of the eight potential N-glycosylation sites, namely, Asn52, Asn56, Asn208, Asn251, Asn298, Asn372, and Asn489, turned out to be glycosylated, and the potential glycosylation site at Asn14, being close to the N-terminus, is not used.
9884403	3	83	theme	more	754:757	arg1	detail					759:764	more detail	754:764	more detail	754:764	The carbohydrate microheterogeneity on three of the glycosylation sites was studied in more detail by high-pH anion-exchange chromatographic profiling and 500 MHz1H-NMR spectroscopy.
16103099	0	0	theme	human	82:86	arg1	lines					99:103	human tumor cell lines	82:103	human tumor cell lines	82:103	RECK-mediated suppression of tumor cell invasion is regulated by glycosylation in human tumor cell lines.
16103099	1	1	gly	glycoprotein	158:169	arg1	glycoprotein					158:169	a glycosylphosphatidylinositol (GPI)-anchored glycoprotein	112:169	a glycosylphosphatidylinositol (GPI)-anchored glycoprotein	112:169	RECK, a glycosylphosphatidylinositol (GPI)-anchored glycoprotein, negatively regulates matrix metalloproteinases (MMP), such as MMP-9, and inhibits tumor invasion and metastasis.
16103099	1	1	gly	glycoprotein	158:169	arg1	RECK					106:109	RECK	106:109	RECK	106:109	RECK, a glycosylphosphatidylinositol (GPI)-anchored glycoprotein, negatively regulates matrix metalloproteinases (MMP), such as MMP-9, and inhibits tumor invasion and metastasis.
16103099	2	2	theme	RECK	328:331	arg1	sequence					310:317	The predicted amino acid sequence	285:317	The predicted amino acid sequence of human RECK	285:331	The predicted amino acid sequence of human RECK includes five putative N-glycosylation sites; however, the precise biochemical role of glycosylated RECK remains unknown.
16103099	4	3	theme	HT1080	673:678	arg1	cells					680:684	HT1080 cells	673:684	HT1080 cells	673:684	RECK protein was glycosylated at Asn86, Asn200, Asn297, and Asn352 residues but not at the Asn39 residue in HT1080 cells.
16103099	0	4	theme	cell	94:97	arg1	lines					99:103	human tumor cell lines	82:103	human tumor cell lines	82:103	RECK-mediated suppression of tumor cell invasion is regulated by glycosylation in human tumor cell lines.
16103099	7	5	theme	MMP-9	1257:1261	arg1	secretion					1263:1271	MMP-9 secretion	1257:1271	MMP-9 secretion	1257:1271	Thus, these findings indicate that glycosylation mediates RECK suppression of tumor cell invasion by multiple mechanisms such as suppressing MMP-9 secretion and inhibiting MMP-2 activation.
16103099	5	6	theme	GPI-anchored	806:817	arg1	protein					819:825	a GPI-anchored protein	804:825	a GPI-anchored protein	804:825	Although the glycosylation of these asparagine sites did not play a role in the cell surface localization of RECK as a GPI-anchored protein, the glycosylation of RECK Asn297 residue was involved in the suppression of MMP-9 secretion and Asn352 residue was necessary to inhibit MMP-2 activation.
16103099	5	6	theme	GPI-anchored	806:817	arg1	role					755:758	a role	753:758	a role	753:758	Although the glycosylation of these asparagine sites did not play a role in the cell surface localization of RECK as a GPI-anchored protein, the glycosylation of RECK Asn297 residue was involved in the suppression of MMP-9 secretion and Asn352 residue was necessary to inhibit MMP-2 activation.
16103099	3	7	theme	RECK	533:536	arg1	glycosylation					499:511	glycosylation	499:511	glycosylation	499:511	In this study, we examined the link between glycosylation and the function of RECK in human tumor cell lines.
16103099	3	7	theme	RECK	533:536	arg1	function					521:528	the function	517:528	the function of RECK in human tumor cell lines	517:562	In this study, we examined the link between glycosylation and the function of RECK in human tumor cell lines.
16103099	0	8	theme	tumor	88:92	arg1	lines					99:103	human tumor cell lines	82:103	human tumor cell lines	82:103	RECK-mediated suppression of tumor cell invasion is regulated by glycosylation in human tumor cell lines.
16103099	4	9	theme	Asn39	656:660	arg1	residue					662:668	the Asn39 residue	652:668	the Asn39 residue in HT1080 cells	652:684	RECK protein was glycosylated at Asn86, Asn200, Asn297, and Asn352 residues but not at the Asn39 residue in HT1080 cells.
16103099	7	10	theme	RECK	1174:1177	arg1	suppression					1179:1189	RECK suppression	1174:1189	RECK suppression of tumor cell invasion by multiple mechanisms such as suppressing MMP-9 secretion and inhibiting MMP-2 activation	1174:1303	Thus, these findings indicate that glycosylation mediates RECK suppression of tumor cell invasion by multiple mechanisms such as suppressing MMP-9 secretion and inhibiting MMP-2 activation.
16103099	6	11	gly	glycosylation	1055:1067	arg1	Asn297					1079:1084	Asn297	1079:1084	Asn297	1079:1084	Moreover, RECK-suppressed tumor cell invasion was reversed by inhibiting glycosylation at Asn86, Asn297, and Asn352 residues of RECK.
16103099	6	11	gly	glycosylation	1055:1067	arg1	RECK					1110:1113	RECK	1110:1113	RECK	1110:1113	Moreover, RECK-suppressed tumor cell invasion was reversed by inhibiting glycosylation at Asn86, Asn297, and Asn352 residues of RECK.
16103099	6	11	gly	glycosylation	1055:1067	arg1	residues					1098:1105	Asn86, Asn297, and Asn352 residues	1072:1105	residues	1098:1105	Moreover, RECK-suppressed tumor cell invasion was reversed by inhibiting glycosylation at Asn86, Asn297, and Asn352 residues of RECK.
16103099	4	12	gly	glycosylated	582:593	arg2	residue					662:668	the Asn39 residue	652:668	the Asn39 residue in HT1080 cells	652:684	RECK protein was glycosylated at Asn86, Asn200, Asn297, and Asn352 residues but not at the Asn39 residue in HT1080 cells.
16103099	4	12	gly	glycosylated	582:593	arg1	protein					570:576	RECK protein	565:576	RECK protein	565:576	RECK protein was glycosylated at Asn86, Asn200, Asn297, and Asn352 residues but not at the Asn39 residue in HT1080 cells.
16103099	4	12	gly	glycosylated	582:593	arg2	residues					632:639	Asn86, Asn200, Asn297, and Asn352 residues	598:639	Asn86, Asn200, Asn297, and Asn352 residues	598:639	RECK protein was glycosylated at Asn86, Asn200, Asn297, and Asn352 residues but not at the Asn39 residue in HT1080 cells.
16103099	6	13	theme	Asn352	1091:1096	arg1	RECK					1110:1113	RECK	1110:1113	RECK	1110:1113	Moreover, RECK-suppressed tumor cell invasion was reversed by inhibiting glycosylation at Asn86, Asn297, and Asn352 residues of RECK.
16103099	6	13	theme	Asn352	1091:1096	arg1	residues					1098:1105	Asn86, Asn297, and Asn352 residues	1072:1105	residues	1098:1105	Moreover, RECK-suppressed tumor cell invasion was reversed by inhibiting glycosylation at Asn86, Asn297, and Asn352 residues of RECK.
16103099	4	14	theme	Asn297	613:618	arg1	residues					632:639	Asn86, Asn200, Asn297, and Asn352 residues	598:639	Asn86, Asn200, Asn297, and Asn352 residues	598:639	RECK protein was glycosylated at Asn86, Asn200, Asn297, and Asn352 residues but not at the Asn39 residue in HT1080 cells.
16103099	0	15	theme	RECK-mediated	0:12	arg1	suppression					14:24	RECK-mediated suppression	0:24	RECK-mediated suppression of tumor cell invasion	0:47	RECK-mediated suppression of tumor cell invasion is regulated by glycosylation in human tumor cell lines.
16103099	6	16	theme	cell	1014:1017	arg1	invasion					1019:1026	RECK-suppressed tumor cell invasion	992:1026	RECK-suppressed tumor cell invasion	992:1026	Moreover, RECK-suppressed tumor cell invasion was reversed by inhibiting glycosylation at Asn86, Asn297, and Asn352 residues of RECK.
16103099	6	17	theme	RECK-suppressed	992:1006	arg1	invasion					1019:1026	RECK-suppressed tumor cell invasion	992:1026	RECK-suppressed tumor cell invasion	992:1026	Moreover, RECK-suppressed tumor cell invasion was reversed by inhibiting glycosylation at Asn86, Asn297, and Asn352 residues of RECK.
16103099	2	18	theme	RECK	433:436	arg1	role					412:415	the precise biochemical role	388:415	the precise biochemical role of glycosylated RECK	388:436	The predicted amino acid sequence of human RECK includes five putative N-glycosylation sites; however, the precise biochemical role of glycosylated RECK remains unknown.
16103099	2	19	gly	N-glycosylation	356:370	arg2	five					342:345	five	342:345	five	342:345	The predicted amino acid sequence of human RECK includes five putative N-glycosylation sites; however, the precise biochemical role of glycosylated RECK remains unknown.
16103099	2	19	gly	N-glycosylation	356:370	arg2	sites					372:376	five putative N-glycosylation sites	342:376	five putative N-glycosylation sites	342:376	The predicted amino acid sequence of human RECK includes five putative N-glycosylation sites; however, the precise biochemical role of glycosylated RECK remains unknown.
16103099	2	20	theme	amino	299:303	arg1	sequence					310:317	The predicted amino acid sequence	285:317	The predicted amino acid sequence of human RECK	285:331	The predicted amino acid sequence of human RECK includes five putative N-glycosylation sites; however, the precise biochemical role of glycosylated RECK remains unknown.
16103099	7	21	theme	tumor	1194:1198	arg1	invasion					1205:1212	tumor cell invasion	1194:1212	tumor cell invasion	1194:1212	Thus, these findings indicate that glycosylation mediates RECK suppression of tumor cell invasion by multiple mechanisms such as suppressing MMP-9 secretion and inhibiting MMP-2 activation.
16103099	5	22	theme	RECK	796:799	arg1	localization					780:791	the cell surface localization	763:791	the cell surface localization of RECK	763:799	Although the glycosylation of these asparagine sites did not play a role in the cell surface localization of RECK as a GPI-anchored protein, the glycosylation of RECK Asn297 residue was involved in the suppression of MMP-9 secretion and Asn352 residue was necessary to inhibit MMP-2 activation.
16103099	2	23	theme	glycosylated	420:431	arg1	RECK					433:436	glycosylated RECK	420:436	glycosylated RECK	420:436	The predicted amino acid sequence of human RECK includes five putative N-glycosylation sites; however, the precise biochemical role of glycosylated RECK remains unknown.
16103099	1	24	theme	tumor	254:258	arg1	invasion					260:267	tumor invasion	254:267	tumor invasion	254:267	RECK, a glycosylphosphatidylinositol (GPI)-anchored glycoprotein, negatively regulates matrix metalloproteinases (MMP), such as MMP-9, and inhibits tumor invasion and metastasis.
16103099	2	25	theme	predicted	289:297	arg1	sequence					310:317	The predicted amino acid sequence	285:317	The predicted amino acid sequence of human RECK	285:331	The predicted amino acid sequence of human RECK includes five putative N-glycosylation sites; however, the precise biochemical role of glycosylated RECK remains unknown.
16103099	2	26	theme	N-glycosylation	356:370	arg1	sites					372:376	five putative N-glycosylation sites	342:376	five putative N-glycosylation sites	342:376	The predicted amino acid sequence of human RECK includes five putative N-glycosylation sites; however, the precise biochemical role of glycosylated RECK remains unknown.
16103099	0	27	theme	tumor	29:33	arg1	invasion					40:47	tumor cell invasion	29:47	tumor cell invasion	29:47	RECK-mediated suppression of tumor cell invasion is regulated by glycosylation in human tumor cell lines.
16103099	5	28	gly	glycosylation	832:844	arg1	suppression					889:899	the suppression	885:899	the suppression of MMP-9 secretion	885:918	Although the glycosylation of these asparagine sites did not play a role in the cell surface localization of RECK as a GPI-anchored protein, the glycosylation of RECK Asn297 residue was involved in the suppression of MMP-9 secretion and Asn352 residue was necessary to inhibit MMP-2 activation.
16103099	5	28	gly	glycosylation	832:844	arg1	residue					861:867	RECK Asn297 residue	849:867	RECK Asn297 residue	849:867	Although the glycosylation of these asparagine sites did not play a role in the cell surface localization of RECK as a GPI-anchored protein, the glycosylation of RECK Asn297 residue was involved in the suppression of MMP-9 secretion and Asn352 residue was necessary to inhibit MMP-2 activation.
16103099	5	29	theme	RECK	849:852	arg1	residue					861:867	RECK Asn297 residue	849:867	RECK Asn297 residue	849:867	Although the glycosylation of these asparagine sites did not play a role in the cell surface localization of RECK as a GPI-anchored protein, the glycosylation of RECK Asn297 residue was involved in the suppression of MMP-9 secretion and Asn352 residue was necessary to inhibit MMP-2 activation.
16103099	2	30	theme	biochemical	400:410	arg1	role					412:415	the precise biochemical role	388:415	the precise biochemical role of glycosylated RECK	388:436	The predicted amino acid sequence of human RECK includes five putative N-glycosylation sites; however, the precise biochemical role of glycosylated RECK remains unknown.
16103099	3	31	theme	human	541:545	arg1	lines					558:562	human tumor cell lines	541:562	human tumor cell lines	541:562	In this study, we examined the link between glycosylation and the function of RECK in human tumor cell lines.
16103099	5	32	theme	residue	861:867	arg1	glycosylation					832:844	the glycosylation	828:844	the glycosylation of RECK Asn297 residue	828:867	Although the glycosylation of these asparagine sites did not play a role in the cell surface localization of RECK as a GPI-anchored protein, the glycosylation of RECK Asn297 residue was involved in the suppression of MMP-9 secretion and Asn352 residue was necessary to inhibit MMP-2 activation.
16103099	1	33	theme	-anchored	148:156	arg1	glycoprotein					158:169	a glycosylphosphatidylinositol (GPI)-anchored glycoprotein	112:169	a glycosylphosphatidylinositol (GPI)-anchored glycoprotein	112:169	RECK, a glycosylphosphatidylinositol (GPI)-anchored glycoprotein, negatively regulates matrix metalloproteinases (MMP), such as MMP-9, and inhibits tumor invasion and metastasis.
16103099	1	33	theme	-anchored	148:156	arg1	RECK					106:109	RECK	106:109	RECK	106:109	RECK, a glycosylphosphatidylinositol (GPI)-anchored glycoprotein, negatively regulates matrix metalloproteinases (MMP), such as MMP-9, and inhibits tumor invasion and metastasis.
16103099	2	34	theme	precise	392:398	arg1	role					412:415	the precise biochemical role	388:415	the precise biochemical role of glycosylated RECK	388:436	The predicted amino acid sequence of human RECK includes five putative N-glycosylation sites; however, the precise biochemical role of glycosylated RECK remains unknown.
16103099	0	35	theme	invasion	40:47	arg1	suppression					14:24	RECK-mediated suppression	0:24	RECK-mediated suppression of tumor cell invasion	0:47	RECK-mediated suppression of tumor cell invasion is regulated by glycosylation in human tumor cell lines.
16103099	7	36	theme	multiple	1217:1224	arg1	mechanisms					1226:1235	multiple mechanisms	1217:1235	multiple mechanisms such as suppressing MMP-9 secretion and inhibiting MMP-2 activation	1217:1303	Thus, these findings indicate that glycosylation mediates RECK suppression of tumor cell invasion by multiple mechanisms such as suppressing MMP-9 secretion and inhibiting MMP-2 activation.
16103099	5	37	theme	cell	767:770	arg1	localization					780:791	the cell surface localization	763:791	the cell surface localization of RECK	763:799	Although the glycosylation of these asparagine sites did not play a role in the cell surface localization of RECK as a GPI-anchored protein, the glycosylation of RECK Asn297 residue was involved in the suppression of MMP-9 secretion and Asn352 residue was necessary to inhibit MMP-2 activation.
16103099	6	38	theme	RECK	1110:1113	arg1	RECK					1110:1113	RECK	1110:1113	RECK	1110:1113	Moreover, RECK-suppressed tumor cell invasion was reversed by inhibiting glycosylation at Asn86, Asn297, and Asn352 residues of RECK.
16103099	6	38	theme	RECK	1110:1113	arg1	residues					1098:1105	Asn86, Asn297, and Asn352 residues	1072:1105	residues	1098:1105	Moreover, RECK-suppressed tumor cell invasion was reversed by inhibiting glycosylation at Asn86, Asn297, and Asn352 residues of RECK.
16103099	4	39	theme	Asn200	605:610	arg1	residues					632:639	Asn86, Asn200, Asn297, and Asn352 residues	598:639	Asn86, Asn200, Asn297, and Asn352 residues	598:639	RECK protein was glycosylated at Asn86, Asn200, Asn297, and Asn352 residues but not at the Asn39 residue in HT1080 cells.
16103099	0	40	theme	cell	35:38	arg1	invasion					40:47	tumor cell invasion	29:47	tumor cell invasion	29:47	RECK-mediated suppression of tumor cell invasion is regulated by glycosylation in human tumor cell lines.
16103099	5	41	theme	asparagine	723:732	arg1	sites					734:738	these asparagine sites	717:738	these asparagine sites	717:738	Although the glycosylation of these asparagine sites did not play a role in the cell surface localization of RECK as a GPI-anchored protein, the glycosylation of RECK Asn297 residue was involved in the suppression of MMP-9 secretion and Asn352 residue was necessary to inhibit MMP-2 activation.
16103099	6	42	theme	tumor	1008:1012	arg1	invasion					1019:1026	RECK-suppressed tumor cell invasion	992:1026	RECK-suppressed tumor cell invasion	992:1026	Moreover, RECK-suppressed tumor cell invasion was reversed by inhibiting glycosylation at Asn86, Asn297, and Asn352 residues of RECK.
16103099	5	43	theme	surface	772:778	arg1	localization					780:791	the cell surface localization	763:791	the cell surface localization of RECK	763:799	Although the glycosylation of these asparagine sites did not play a role in the cell surface localization of RECK as a GPI-anchored protein, the glycosylation of RECK Asn297 residue was involved in the suppression of MMP-9 secretion and Asn352 residue was necessary to inhibit MMP-2 activation.
16103099	5	44	theme	sites	734:738	arg1	glycosylation					700:712	the glycosylation	696:712	the glycosylation of these asparagine sites	696:738	Although the glycosylation of these asparagine sites did not play a role in the cell surface localization of RECK as a GPI-anchored protein, the glycosylation of RECK Asn297 residue was involved in the suppression of MMP-9 secretion and Asn352 residue was necessary to inhibit MMP-2 activation.
16103099	3	45	theme	tumor	547:551	arg1	lines					558:562	human tumor cell lines	541:562	human tumor cell lines	541:562	In this study, we examined the link between glycosylation and the function of RECK in human tumor cell lines.
16103099	2	46	theme	human	322:326	arg1	RECK					328:331	human RECK	322:331	human RECK	322:331	The predicted amino acid sequence of human RECK includes five putative N-glycosylation sites; however, the precise biochemical role of glycosylated RECK remains unknown.
16103099	3	47	theme	cell	553:556	arg1	lines					558:562	human tumor cell lines	541:562	human tumor cell lines	541:562	In this study, we examined the link between glycosylation and the function of RECK in human tumor cell lines.
16103099	7	48	theme	cell	1200:1203	arg1	invasion					1205:1212	tumor cell invasion	1194:1212	tumor cell invasion	1194:1212	Thus, these findings indicate that glycosylation mediates RECK suppression of tumor cell invasion by multiple mechanisms such as suppressing MMP-9 secretion and inhibiting MMP-2 activation.
16103099	7	49	theme	invasion	1205:1212	arg1	suppression					1179:1189	RECK suppression	1174:1189	RECK suppression of tumor cell invasion by multiple mechanisms such as suppressing MMP-9 secretion and inhibiting MMP-2 activation	1174:1303	Thus, these findings indicate that glycosylation mediates RECK suppression of tumor cell invasion by multiple mechanisms such as suppressing MMP-9 secretion and inhibiting MMP-2 activation.
16103099	4	50	from	residue	662:668	arg1	cells					680:684	HT1080 cells	673:684	HT1080 cells	673:684	RECK protein was glycosylated at Asn86, Asn200, Asn297, and Asn352 residues but not at the Asn39 residue in HT1080 cells.
16103099	5	51	theme	Asn352	924:929	arg1	residue					931:937	Asn352 residue	924:937	Asn352 residue	924:937	Although the glycosylation of these asparagine sites did not play a role in the cell surface localization of RECK as a GPI-anchored protein, the glycosylation of RECK Asn297 residue was involved in the suppression of MMP-9 secretion and Asn352 residue was necessary to inhibit MMP-2 activation.
16103099	5	52	theme	Asn297	854:859	arg1	residue					861:867	RECK Asn297 residue	849:867	RECK Asn297 residue	849:867	Although the glycosylation of these asparagine sites did not play a role in the cell surface localization of RECK as a GPI-anchored protein, the glycosylation of RECK Asn297 residue was involved in the suppression of MMP-9 secretion and Asn352 residue was necessary to inhibit MMP-2 activation.
16103099	5	53	theme	MMP-2	964:968	arg1	activation					970:979	MMP-2 activation	964:979	MMP-2 activation	964:979	Although the glycosylation of these asparagine sites did not play a role in the cell surface localization of RECK as a GPI-anchored protein, the glycosylation of RECK Asn297 residue was involved in the suppression of MMP-9 secretion and Asn352 residue was necessary to inhibit MMP-2 activation.
16103099	2	54	gly	glycosylated	420:431	arg1	RECK					433:436	glycosylated RECK	420:436	glycosylated RECK	420:436	The predicted amino acid sequence of human RECK includes five putative N-glycosylation sites; however, the precise biochemical role of glycosylated RECK remains unknown.
16103099	5	55	gly	glycosylation	700:712	arg1	sites					734:738	these asparagine sites	717:738	these asparagine sites	717:738	Although the glycosylation of these asparagine sites did not play a role in the cell surface localization of RECK as a GPI-anchored protein, the glycosylation of RECK Asn297 residue was involved in the suppression of MMP-9 secretion and Asn352 residue was necessary to inhibit MMP-2 activation.
16103099	3	56	gly	glycosylation	499:511	arg1	lines					558:562	human tumor cell lines	541:562	human tumor cell lines	541:562	In this study, we examined the link between glycosylation and the function of RECK in human tumor cell lines.
16103099	3	56	gly	glycosylation	499:511	arg1	RECK					533:536	RECK	533:536	RECK	533:536	In this study, we examined the link between glycosylation and the function of RECK in human tumor cell lines.
16103099	5	57	theme	secretion	910:918	arg1	suppression					889:899	the suppression	885:899	the suppression of MMP-9 secretion	885:918	Although the glycosylation of these asparagine sites did not play a role in the cell surface localization of RECK as a GPI-anchored protein, the glycosylation of RECK Asn297 residue was involved in the suppression of MMP-9 secretion and Asn352 residue was necessary to inhibit MMP-2 activation.
16103099	2	58	theme	acid	305:308	arg1	sequence					310:317	The predicted amino acid sequence	285:317	The predicted amino acid sequence of human RECK	285:331	The predicted amino acid sequence of human RECK includes five putative N-glycosylation sites; however, the precise biochemical role of glycosylated RECK remains unknown.
16103099	4	59	theme	RECK	565:568	arg1	protein					570:576	RECK protein	565:576	RECK protein	565:576	RECK protein was glycosylated at Asn86, Asn200, Asn297, and Asn352 residues but not at the Asn39 residue in HT1080 cells.
16103099	3	60	from	function	521:528	arg1	lines					558:562	human tumor cell lines	541:562	human tumor cell lines	541:562	In this study, we examined the link between glycosylation and the function of RECK in human tumor cell lines.
16103099	1	61	theme	matrix	193:198	arg1	metalloproteinases					200:217	matrix metalloproteinases	193:217	matrix metalloproteinases (MMP)	193:223	RECK, a glycosylphosphatidylinositol (GPI)-anchored glycoprotein, negatively regulates matrix metalloproteinases (MMP), such as MMP-9, and inhibits tumor invasion and metastasis.
16103099	1	61	theme	matrix	193:198	arg1	MMP-9					234:238	MMP-9	234:238	MMP-9	234:238	RECK, a glycosylphosphatidylinositol (GPI)-anchored glycoprotein, negatively regulates matrix metalloproteinases (MMP), such as MMP-9, and inhibits tumor invasion and metastasis.
16103099	1	61	theme	matrix	193:198	arg1	MMP					220:222	MMP	220:222	MMP	220:222	RECK, a glycosylphosphatidylinositol (GPI)-anchored glycoprotein, negatively regulates matrix metalloproteinases (MMP), such as MMP-9, and inhibits tumor invasion and metastasis.
16103099	2	62	theme	putative	347:354	arg1	sites					372:376	five putative N-glycosylation sites	342:376	five putative N-glycosylation sites	342:376	The predicted amino acid sequence of human RECK includes five putative N-glycosylation sites; however, the precise biochemical role of glycosylated RECK remains unknown.
16103099	5	63	theme	MMP-9	904:908	arg1	secretion					910:918	MMP-9 secretion	904:918	MMP-9 secretion	904:918	Although the glycosylation of these asparagine sites did not play a role in the cell surface localization of RECK as a GPI-anchored protein, the glycosylation of RECK Asn297 residue was involved in the suppression of MMP-9 secretion and Asn352 residue was necessary to inhibit MMP-2 activation.
16103099	7	64	theme	MMP-2	1288:1292	arg1	activation					1294:1303	MMP-2 activation	1288:1303	MMP-2 activation	1288:1303	Thus, these findings indicate that glycosylation mediates RECK suppression of tumor cell invasion by multiple mechanisms such as suppressing MMP-9 secretion and inhibiting MMP-2 activation.
16103099	4	65	theme	Asn86	598:602	arg1	residues					632:639	Asn86, Asn200, Asn297, and Asn352 residues	598:639	Asn86, Asn200, Asn297, and Asn352 residues	598:639	RECK protein was glycosylated at Asn86, Asn200, Asn297, and Asn352 residues but not at the Asn39 residue in HT1080 cells.
16103099	4	66	theme	Asn352	625:630	arg1	residues					632:639	Asn86, Asn200, Asn297, and Asn352 residues	598:639	Asn86, Asn200, Asn297, and Asn352 residues	598:639	RECK protein was glycosylated at Asn86, Asn200, Asn297, and Asn352 residues but not at the Asn39 residue in HT1080 cells.
16103099	3	67	from	glycosylation	499:511	arg1	lines					558:562	human tumor cell lines	541:562	human tumor cell lines	541:562	In this study, we examined the link between glycosylation and the function of RECK in human tumor cell lines.
12590919	0	0	theme	transporter-2	97:109	arg1	mutants					51:57	site-directed glycosylation mutants	23:57	site-directed glycosylation mutants of the human equilibrative nucleoside transporter-2	23:109	Functional analysis of site-directed glycosylation mutants of the human equilibrative nucleoside transporter-2.
12590919	5	1	from	increase	802:809	arg1	IC					814:815	IC(50)	814:819	IC(50) for dipyridamole	814:836	All mutants had a two- to threefold increase in IC(50) for dipyridamole.
12590919	0	2	theme	nucleoside	86:95	arg1	transporter-2					97:109	the human equilibrative nucleoside transporter-2	62:109	the human equilibrative nucleoside transporter-2	62:109	Functional analysis of site-directed glycosylation mutants of the human equilibrative nucleoside transporter-2.
12590919	4	3	theme	efficient	713:721	arg1	targeting					723:731	efficient targeting	713:731	efficient targeting of hENT2 to the plasma membrane	713:763	Our results show that although the apparent affinities for [3H]uridine and [3H]cytidine of the mutants were indistinguishable from those of the wild-type protein, N-glycosylation was required for efficient targeting of hENT2 to the plasma membrane.
12590919	4	4	theme	apparent	552:559	arg1	indistinguishable					625:641	indistinguishable	625:641	indistinguishable	625:641	Our results show that although the apparent affinities for [3H]uridine and [3H]cytidine of the mutants were indistinguishable from those of the wild-type protein, N-glycosylation was required for efficient targeting of hENT2 to the plasma membrane.
12590919	4	4	theme	apparent	552:559	arg1	affinities					561:570	the apparent affinities	548:570	the apparent affinities for [3H]uridine and [3H]cytidine of the mutants	548:618	Our results show that although the apparent affinities for [3H]uridine and [3H]cytidine of the mutants were indistinguishable from those of the wild-type protein, N-glycosylation was required for efficient targeting of hENT2 to the plasma membrane.
12590919	4	5	gly	N-glycosylation	680:694	arg1	hENT2					736:740	hENT2	736:740	hENT2	736:740	Our results show that although the apparent affinities for [3H]uridine and [3H]cytidine of the mutants were indistinguishable from those of the wild-type protein, N-glycosylation was required for efficient targeting of hENT2 to the plasma membrane.
12590919	3	6	dep	mutants	416:422	arg1	N48/57D					441:447	N48/57D	441:447	N48/57D	441:447	We address these questions using N-glycosylation mutants (N48D, N57D, and N48/57D) and demonstrate that hENT2 is glycosylated at Asn(48) and Asn(57).
12590919	3	6	dep	mutants	416:422	arg1	N48D					425:428	N48D	425:428	N48D	425:428	We address these questions using N-glycosylation mutants (N48D, N57D, and N48/57D) and demonstrate that hENT2 is glycosylated at Asn(48) and Asn(57).
12590919	3	6	dep	mutants	416:422	arg1	mutants					416:422	N-glycosylation mutants	400:422	N-glycosylation mutants (N48D, N57D, and N48/57D)	400:448	We address these questions using N-glycosylation mutants (N48D, N57D, and N48/57D) and demonstrate that hENT2 is glycosylated at Asn(48) and Asn(57).
12590919	3	6	dep	mutants	416:422	arg1	N57D					431:434	N57D	431:434	N57D	431:434	We address these questions using N-glycosylation mutants (N48D, N57D, and N48/57D) and demonstrate that hENT2 is glycosylated at Asn(48) and Asn(57).
12590919	7	7	theme	hENT2	967:971	arg1	insensitivity					950:962	the relative insensitivity	937:962	the relative insensitivity of hENT2 to inhibitors	937:985	We conclude that the relative insensitivity of hENT2 to inhibitors is primarily due to its primary structure and not to glycosylation.
12590919	7	7	theme	hENT2	967:971	arg1	structure					1019:1027	its primary structure	1007:1027	its primary structure	1007:1027	We conclude that the relative insensitivity of hENT2 to inhibitors is primarily due to its primary structure and not to glycosylation.
12590919	5	8	theme	threefold	792:800	arg1	increase					802:809	a two- to threefold increase	782:809	a two- to threefold increase in IC(50) for dipyridamole	782:836	All mutants had a two- to threefold increase in IC(50) for dipyridamole.
12590919	1	9	gly	glycosylation	120:132	arg1	nucleoside					151:160	nucleoside transport	151:170	nucleoside transport	151:170	Protein glycosylation is important for nucleoside transport, and this has been demonstrated for the human equilibrative nucleoside transporter-1 (hENT1).
12590919	7	10	theme	primary	1011:1017	arg1	insensitivity					950:962	the relative insensitivity	937:962	the relative insensitivity of hENT2 to inhibitors	937:985	We conclude that the relative insensitivity of hENT2 to inhibitors is primarily due to its primary structure and not to glycosylation.
12590919	7	10	theme	primary	1011:1017	arg1	structure					1019:1027	its primary structure	1007:1027	its primary structure	1007:1027	We conclude that the relative insensitivity of hENT2 to inhibitors is primarily due to its primary structure and not to glycosylation.
12590919	3	11	theme	N-glycosylation	400:414	arg1	N48/57D					441:447	N48/57D	441:447	N48/57D	441:447	We address these questions using N-glycosylation mutants (N48D, N57D, and N48/57D) and demonstrate that hENT2 is glycosylated at Asn(48) and Asn(57).
12590919	3	11	theme	N-glycosylation	400:414	arg1	N48D					425:428	N48D	425:428	N48D	425:428	We address these questions using N-glycosylation mutants (N48D, N57D, and N48/57D) and demonstrate that hENT2 is glycosylated at Asn(48) and Asn(57).
12590919	3	11	theme	N-glycosylation	400:414	arg1	mutants					416:422	N-glycosylation mutants	400:422	N-glycosylation mutants (N48D, N57D, and N48/57D)	400:448	We address these questions using N-glycosylation mutants (N48D, N57D, and N48/57D) and demonstrate that hENT2 is glycosylated at Asn(48) and Asn(57).
12590919	3	11	theme	N-glycosylation	400:414	arg1	N57D					431:434	N57D	431:434	N57D	431:434	We address these questions using N-glycosylation mutants (N48D, N57D, and N48/57D) and demonstrate that hENT2 is glycosylated at Asn(48) and Asn(57).
12590919	4	12	theme	mutants	612:618	arg1	indistinguishable					625:641	indistinguishable	625:641	indistinguishable	625:641	Our results show that although the apparent affinities for [3H]uridine and [3H]cytidine of the mutants were indistinguishable from those of the wild-type protein, N-glycosylation was required for efficient targeting of hENT2 to the plasma membrane.
12590919	4	12	theme	mutants	612:618	arg1	affinities					561:570	the apparent affinities	548:570	the apparent affinities for [3H]uridine and [3H]cytidine of the mutants	548:618	Our results show that although the apparent affinities for [3H]uridine and [3H]cytidine of the mutants were indistinguishable from those of the wild-type protein, N-glycosylation was required for efficient targeting of hENT2 to the plasma membrane.
12590919	0	13	theme	Functional	0:9	arg1	analysis					11:18	Functional analysis	0:18	Functional analysis of site-directed glycosylation mutants of the human equilibrative nucleoside transporter-2	0:109	Functional analysis of site-directed glycosylation mutants of the human equilibrative nucleoside transporter-2.
12590919	6	14	from	increase	890:897	arg1	IC					902:903	IC(50)	902:907	IC(50) for NBMPR	902:917	N57D and N48/57D, but not N48D, also had a twofold increase in IC(50) for NBMPR.
12590919	1	15	theme	Protein	112:118	arg1	glycosylation					120:132	Protein glycosylation	112:132	Protein glycosylation	112:132	Protein glycosylation is important for nucleoside transport, and this has been demonstrated for the human equilibrative nucleoside transporter-1 (hENT1).
12590919	0	16	theme	site-directed	23:35	arg1	mutants					51:57	site-directed glycosylation mutants	23:57	site-directed glycosylation mutants of the human equilibrative nucleoside transporter-2	23:109	Functional analysis of site-directed glycosylation mutants of the human equilibrative nucleoside transporter-2.
12590919	5	17	contain	had	778:780	arg2	increase					802:809	a two- to threefold increase	782:809	a two- to threefold increase in IC(50) for dipyridamole	782:836	All mutants had a two- to threefold increase in IC(50) for dipyridamole.
12590919	5	17	contain	had	778:780	arg1	mutants					770:776	All mutants	766:776	All mutants	766:776	All mutants had a two- to threefold increase in IC(50) for dipyridamole.
12590919	3	18	gly	glycosylated	480:491	arg2	Asn					508:510	Asn(57)	508:514	Asn(57)	508:514	We address these questions using N-glycosylation mutants (N48D, N57D, and N48/57D) and demonstrate that hENT2 is glycosylated at Asn(48) and Asn(57).
12590919	3	18	gly	glycosylated	480:491	arg2	Asn					496:498	Asn(48)	496:502	Asn(48)	496:502	We address these questions using N-glycosylation mutants (N48D, N57D, and N48/57D) and demonstrate that hENT2 is glycosylated at Asn(48) and Asn(57).
12590919	3	18	gly	glycosylated	480:491	arg1	hENT2					471:475	hENT2	471:475	hENT2	471:475	We address these questions using N-glycosylation mutants (N48D, N57D, and N48/57D) and demonstrate that hENT2 is glycosylated at Asn(48) and Asn(57).
12590919	1	19	theme	human	212:216	arg1	hENT1					258:262	hENT1	258:262	hENT1	258:262	Protein glycosylation is important for nucleoside transport, and this has been demonstrated for the human equilibrative nucleoside transporter-1 (hENT1).
12590919	1	19	theme	human	212:216	arg1	transporter-1					243:255	the human equilibrative nucleoside transporter-1	208:255	the human equilibrative nucleoside transporter-1 (hENT1)	208:263	Protein glycosylation is important for nucleoside transport, and this has been demonstrated for the human equilibrative nucleoside transporter-1 (hENT1).
12590919	2	20	theme	hENT2	329:333	arg1	functions					316:324	the functions	312:324	the functions of hENT2	312:333	It is not known whether glycosylation affects the functions of hENT2 or where hENT2 is glycosylated.
12590919	7	21	theme	relative	941:948	arg1	insensitivity					950:962	the relative insensitivity	937:962	the relative insensitivity of hENT2 to inhibitors	937:985	We conclude that the relative insensitivity of hENT2 to inhibitors is primarily due to its primary structure and not to glycosylation.
12590919	7	21	theme	relative	941:948	arg1	structure					1019:1027	its primary structure	1007:1027	its primary structure	1007:1027	We conclude that the relative insensitivity of hENT2 to inhibitors is primarily due to its primary structure and not to glycosylation.
12590919	1	22	theme	equilibrative	218:230	arg1	hENT1					258:262	hENT1	258:262	hENT1	258:262	Protein glycosylation is important for nucleoside transport, and this has been demonstrated for the human equilibrative nucleoside transporter-1 (hENT1).
12590919	1	22	theme	equilibrative	218:230	arg1	transporter-1					243:255	the human equilibrative nucleoside transporter-1	208:255	the human equilibrative nucleoside transporter-1 (hENT1)	208:263	Protein glycosylation is important for nucleoside transport, and this has been demonstrated for the human equilibrative nucleoside transporter-1 (hENT1).
12590919	0	23	theme	mutants	51:57	arg1	analysis					11:18	Functional analysis	0:18	Functional analysis of site-directed glycosylation mutants of the human equilibrative nucleoside transporter-2	0:109	Functional analysis of site-directed glycosylation mutants of the human equilibrative nucleoside transporter-2.
12590919	1	24	theme	nucleoside	232:241	arg1	hENT1					258:262	hENT1	258:262	hENT1	258:262	Protein glycosylation is important for nucleoside transport, and this has been demonstrated for the human equilibrative nucleoside transporter-1 (hENT1).
12590919	1	24	theme	nucleoside	232:241	arg1	transporter-1					243:255	the human equilibrative nucleoside transporter-1	208:255	the human equilibrative nucleoside transporter-1 (hENT1)	208:263	Protein glycosylation is important for nucleoside transport, and this has been demonstrated for the human equilibrative nucleoside transporter-1 (hENT1).
12590919	0	25	theme	glycosylation	37:49	arg1	mutants					51:57	site-directed glycosylation mutants	23:57	site-directed glycosylation mutants of the human equilibrative nucleoside transporter-2	23:109	Functional analysis of site-directed glycosylation mutants of the human equilibrative nucleoside transporter-2.
12590919	8	26	theme	hENT1	1079:1083	arg1	function					1085:1092	hENT1 function	1079:1092	hENT1 function	1079:1092	Glycosylation modulates hENT1 function, but is not required for hENT2.
12590919	2	27	gly	glycosylation	290:302	arg1	hENT2					329:333	hENT2	329:333	hENT2	329:333	It is not known whether glycosylation affects the functions of hENT2 or where hENT2 is glycosylated.
12590919	5	28	dep	threefold	792:800	arg1	to					789:790	to	789:790	to	789:790	All mutants had a two- to threefold increase in IC(50) for dipyridamole.
12590919	2	29	gly	glycosylated	353:364	arg1	hENT2					344:348	hENT2	344:348	hENT2	344:348	It is not known whether glycosylation affects the functions of hENT2 or where hENT2 is glycosylated.
12590919	6	30	contain	had	876:878	arg1	N48/57D					848:854	N48/57D	848:854	N48/57D	848:854	N57D and N48/57D, but not N48D, also had a twofold increase in IC(50) for NBMPR.
12590919	6	30	contain	had	876:878	arg1	N57D					839:842	N57D	839:842	N57D	839:842	N57D and N48/57D, but not N48D, also had a twofold increase in IC(50) for NBMPR.
12590919	6	30	contain	had	876:878	arg1	N48D					865:868	N48D	865:868	N48D	865:868	N57D and N48/57D, but not N48D, also had a twofold increase in IC(50) for NBMPR.
12590919	6	30	contain	had	876:878	arg2	increase					890:897	a twofold increase	880:897	a twofold increase in IC(50) for NBMPR	880:917	N57D and N48/57D, but not N48D, also had a twofold increase in IC(50) for NBMPR.
12590919	1	31	theme	nucleoside	151:160	arg1	transport					162:170	nucleoside transport	151:170	nucleoside transport	151:170	Protein glycosylation is important for nucleoside transport, and this has been demonstrated for the human equilibrative nucleoside transporter-1 (hENT1).
12590919	6	32	theme	twofold	882:888	arg1	increase					890:897	a twofold increase	880:897	a twofold increase in IC(50) for NBMPR	880:917	N57D and N48/57D, but not N48D, also had a twofold increase in IC(50) for NBMPR.
12590919	4	33	theme	hENT2	736:740	arg1	targeting					723:731	efficient targeting	713:731	efficient targeting of hENT2 to the plasma membrane	713:763	Our results show that although the apparent affinities for [3H]uridine and [3H]cytidine of the mutants were indistinguishable from those of the wild-type protein, N-glycosylation was required for efficient targeting of hENT2 to the plasma membrane.
12590919	4	34	theme	wild-type	661:669	arg1	protein					671:677	the wild-type protein	657:677	the wild-type protein	657:677	Our results show that although the apparent affinities for [3H]uridine and [3H]cytidine of the mutants were indistinguishable from those of the wild-type protein, N-glycosylation was required for efficient targeting of hENT2 to the plasma membrane.
12590919	0	35	theme	equilibrative	72:84	arg1	transporter-2					97:109	the human equilibrative nucleoside transporter-2	62:109	the human equilibrative nucleoside transporter-2	62:109	Functional analysis of site-directed glycosylation mutants of the human equilibrative nucleoside transporter-2.
12590919	4	36	theme	plasma	749:754	arg1	membrane					756:763	the plasma membrane	745:763	the plasma membrane	745:763	Our results show that although the apparent affinities for [3H]uridine and [3H]cytidine of the mutants were indistinguishable from those of the wild-type protein, N-glycosylation was required for efficient targeting of hENT2 to the plasma membrane.
12590919	0	37	theme	human	66:70	arg1	transporter-2					97:109	the human equilibrative nucleoside transporter-2	62:109	the human equilibrative nucleoside transporter-2	62:109	Functional analysis of site-directed glycosylation mutants of the human equilibrative nucleoside transporter-2.
12590919	4	38	dep	cytidine	596:603	arg1	[3H					576:578	[3H	576:578	[3H	576:578	Our results show that although the apparent affinities for [3H]uridine and [3H]cytidine of the mutants were indistinguishable from those of the wild-type protein, N-glycosylation was required for efficient targeting of hENT2 to the plasma membrane.
12590919	4	39	from	those	648:652	arg1	indistinguishable					625:641	indistinguishable	625:641	indistinguishable	625:641	Our results show that although the apparent affinities for [3H]uridine and [3H]cytidine of the mutants were indistinguishable from those of the wild-type protein, N-glycosylation was required for efficient targeting of hENT2 to the plasma membrane.
12590919	4	39	from	those	648:652	arg1	affinities					561:570	the apparent affinities	548:570	the apparent affinities for [3H]uridine and [3H]cytidine of the mutants	548:618	Our results show that although the apparent affinities for [3H]uridine and [3H]cytidine of the mutants were indistinguishable from those of the wild-type protein, N-glycosylation was required for efficient targeting of hENT2 to the plasma membrane.
20332087	0	0	theme	glycosylation	93:105	arg1	pattern					14:20	Glycosylation pattern	0:20	Glycosylation pattern of mature dimeric leukocyte and recombinant monomeric myeloperoxidase: glycosylation	0:105	Glycosylation pattern of mature dimeric leukocyte and recombinant monomeric myeloperoxidase: glycosylation is required for optimal enzymatic activity.
20332087	1	1	theme	myeloperoxidase	170:184	arg1	scope					240:244	the scope	236:244	the scope of many recent studies	236:267	The involvement of myeloperoxidase (MPO) in various inflammatory conditions has been the scope of many recent studies.
20332087	1	1	theme	myeloperoxidase	170:184	arg1	involvement					155:165	The involvement	151:165	The involvement of myeloperoxidase (MPO) in various inflammatory conditions	151:225	The involvement of myeloperoxidase (MPO) in various inflammatory conditions has been the scope of many recent studies.
20332087	1	2	theme	recent	254:259	arg1	studies					261:267	many recent studies	249:267	many recent studies	249:267	The involvement of myeloperoxidase (MPO) in various inflammatory conditions has been the scope of many recent studies.
20332087	5	3	theme	conserved	743:751	arg1	N-glycans					806:814	a well conserved micro- and macro-heterogeneity and more complex-type N-glycans	736:814	a well conserved micro- and macro-heterogeneity and more complex-type N-glycans for the recombinant form	736:839	Site by site analysis demonstrated a well conserved micro- and macro-heterogeneity and more complex-type N-glycans for the recombinant form.
20332087	3	4	theme	monomeric	507:515	arg1	MPO					517:519	monomeric MPO	507:519	monomeric MPO recombinantly expressed in Chinese hamster ovary cells	507:574	Here, the N-glycan composition of native dimeric human MPO purified from neutrophils and of monomeric MPO recombinantly expressed in Chinese hamster ovary cells has been investigated.
20332087	2	5	from	role	319:322	arg1	function					389:396	biological function	378:396	biological function	378:396	Besides its well studied catalytic activity, the role of its overall structure and glycosylation pattern in biological function is barely known.
20332087	1	6	theme	studies	261:267	arg1	scope					240:244	the scope	236:244	the scope of many recent studies	236:267	The involvement of myeloperoxidase (MPO) in various inflammatory conditions has been the scope of many recent studies.
20332087	1	6	theme	studies	261:267	arg1	involvement					155:165	The involvement	151:165	The involvement of myeloperoxidase (MPO) in various inflammatory conditions	151:225	The involvement of myeloperoxidase (MPO) in various inflammatory conditions has been the scope of many recent studies.
20332087	6	7	theme	recombinant	916:926	arg1	MPO					928:930	recombinant MPO	916:930	recombinant MPO	916:930	Comparison of biological functionality of glycosylated and deglycosylated recombinant MPO suggests that glycosylation is required for optimal enzymatic activity.
20332087	2	8	theme	catalytic	295:303	arg1	activity					305:312	its well studied catalytic activity	278:312	its well studied catalytic activity	278:312	Besides its well studied catalytic activity, the role of its overall structure and glycosylation pattern in biological function is barely known.
20332087	3	9	theme	hamster	556:562	arg1	cells					570:574	Chinese hamster ovary cells	548:574	Chinese hamster ovary cells	548:574	Here, the N-glycan composition of native dimeric human MPO purified from neutrophils and of monomeric MPO recombinantly expressed in Chinese hamster ovary cells has been investigated.
20332087	6	10	theme	deglycosylated	901:914	arg1	functionality					867:879	biological functionality	856:879	biological functionality of glycosylated and deglycosylated recombinant MPO	856:930	Comparison of biological functionality of glycosylated and deglycosylated recombinant MPO suggests that glycosylation is required for optimal enzymatic activity.
20332087	2	11	theme	studied	287:293	arg1	activity					305:312	its well studied catalytic activity	278:312	its well studied catalytic activity	278:312	Besides its well studied catalytic activity, the role of its overall structure and glycosylation pattern in biological function is barely known.
20332087	1	12	from	involvement	155:165	arg1	conditions					216:225	various inflammatory conditions	195:225	various inflammatory conditions	195:225	The involvement of myeloperoxidase (MPO) in various inflammatory conditions has been the scope of many recent studies.
20332087	2	13	theme	glycosylation	353:365	arg1	pattern					367:373	glycosylation pattern	353:373	glycosylation pattern	353:373	Besides its well studied catalytic activity, the role of its overall structure and glycosylation pattern in biological function is barely known.
20332087	0	14	theme	optimal	123:129	arg1	activity					141:148	optimal enzymatic activity	123:148	optimal enzymatic activity	123:148	Glycosylation pattern of mature dimeric leukocyte and recombinant monomeric myeloperoxidase: glycosylation is required for optimal enzymatic activity.
20332087	5	15	theme	recombinant	824:834	arg1	form					836:839	the recombinant form	820:839	the recombinant form	820:839	Site by site analysis demonstrated a well conserved micro- and macro-heterogeneity and more complex-type N-glycans for the recombinant form.
20332087	4	16	theme	N-glycans	636:644	arg1	presence					619:626	the presence	615:626	the presence of five N-glycans at positions 323, 355, 391, 483, 729	615:681	Analyses showed the presence of five N-glycans at positions 323, 355, 391, 483, 729 in both proteins.
20332087	6	17	theme	glycosylated	884:895	arg1	functionality					867:879	biological functionality	856:879	biological functionality of glycosylated and deglycosylated recombinant MPO	856:930	Comparison of biological functionality of glycosylated and deglycosylated recombinant MPO suggests that glycosylation is required for optimal enzymatic activity.
20332087	3	18	theme	N-glycan	425:432	arg1	composition					434:444	the N-glycan composition	421:444	the N-glycan composition of native dimeric human MPO purified from neutrophils and of monomeric MPO recombinantly expressed in Chinese hamster ovary cells	421:574	Here, the N-glycan composition of native dimeric human MPO purified from neutrophils and of monomeric MPO recombinantly expressed in Chinese hamster ovary cells has been investigated.
20332087	5	19	theme	site	709:712	arg1	analysis					714:721	site analysis	709:721	site analysis	709:721	Site by site analysis demonstrated a well conserved micro- and macro-heterogeneity and more complex-type N-glycans for the recombinant form.
20332087	5	20	dep	conserved	743:751	arg1	macro-heterogeneity					764:782	macro-heterogeneity	764:782	macro-heterogeneity	764:782	Site by site analysis demonstrated a well conserved micro- and macro-heterogeneity and more complex-type N-glycans for the recombinant form.
20332087	5	20	dep	conserved	743:751	arg1	complex-type					793:804	complex-type	793:804	complex-type	793:804	Site by site analysis demonstrated a well conserved micro- and macro-heterogeneity and more complex-type N-glycans for the recombinant form.
20332087	5	20	dep	conserved	743:751	arg1	micro-					753:758	micro-	753:758	micro-	753:758	Site by site analysis demonstrated a well conserved micro- and macro-heterogeneity and more complex-type N-glycans for the recombinant form.
20332087	0	21	theme	Glycosylation	0:12	arg1	pattern					14:20	Glycosylation pattern	0:20	Glycosylation pattern of mature dimeric leukocyte and recombinant monomeric myeloperoxidase: glycosylation	0:105	Glycosylation pattern of mature dimeric leukocyte and recombinant monomeric myeloperoxidase: glycosylation is required for optimal enzymatic activity.
20332087	2	22	theme	biological	378:387	arg1	function					389:396	biological function	378:396	biological function	378:396	Besides its well studied catalytic activity, the role of its overall structure and glycosylation pattern in biological function is barely known.
20332087	0	23	theme	mature	25:30	arg1	leukocyte					40:48	mature dimeric leukocyte	25:48	mature dimeric leukocyte	25:48	Glycosylation pattern of mature dimeric leukocyte and recombinant monomeric myeloperoxidase: glycosylation is required for optimal enzymatic activity.
20332087	3	24	theme	ovary	564:568	arg1	cells					570:574	Chinese hamster ovary cells	548:574	Chinese hamster ovary cells	548:574	Here, the N-glycan composition of native dimeric human MPO purified from neutrophils and of monomeric MPO recombinantly expressed in Chinese hamster ovary cells has been investigated.
20332087	4	25	from	positions	649:657	arg1	presence					619:626	the presence	615:626	the presence of five N-glycans at positions 323, 355, 391, 483, 729	615:681	Analyses showed the presence of five N-glycans at positions 323, 355, 391, 483, 729 in both proteins.
20332087	1	26	theme	inflammatory	203:214	arg1	conditions					216:225	various inflammatory conditions	195:225	various inflammatory conditions	195:225	The involvement of myeloperoxidase (MPO) in various inflammatory conditions has been the scope of many recent studies.
20332087	6	27	theme	enzymatic	984:992	arg1	activity					994:1001	optimal enzymatic activity	976:1001	optimal enzymatic activity	976:1001	Comparison of biological functionality of glycosylated and deglycosylated recombinant MPO suggests that glycosylation is required for optimal enzymatic activity.
20332087	0	28	theme	enzymatic	131:139	arg1	activity					141:148	optimal enzymatic activity	123:148	optimal enzymatic activity	123:148	Glycosylation pattern of mature dimeric leukocyte and recombinant monomeric myeloperoxidase: glycosylation is required for optimal enzymatic activity.
20332087	6	29	theme	functionality	867:879	arg1	Comparison					842:851	Comparison	842:851	Comparison of biological functionality of glycosylated and deglycosylated recombinant MPO	842:930	Comparison of biological functionality of glycosylated and deglycosylated recombinant MPO suggests that glycosylation is required for optimal enzymatic activity.
20332087	3	30	theme	MPO	470:472	arg1	composition					434:444	the N-glycan composition	421:444	the N-glycan composition of native dimeric human MPO purified from neutrophils and of monomeric MPO recombinantly expressed in Chinese hamster ovary cells	421:574	Here, the N-glycan composition of native dimeric human MPO purified from neutrophils and of monomeric MPO recombinantly expressed in Chinese hamster ovary cells has been investigated.
20332087	0	31	theme	leukocyte	40:48	arg1	pattern					14:20	Glycosylation pattern	0:20	Glycosylation pattern of mature dimeric leukocyte and recombinant monomeric myeloperoxidase: glycosylation	0:105	Glycosylation pattern of mature dimeric leukocyte and recombinant monomeric myeloperoxidase: glycosylation is required for optimal enzymatic activity.
20332087	6	32	theme	optimal	976:982	arg1	activity					994:1001	optimal enzymatic activity	976:1001	optimal enzymatic activity	976:1001	Comparison of biological functionality of glycosylated and deglycosylated recombinant MPO suggests that glycosylation is required for optimal enzymatic activity.
20332087	7	33	theme	MPO	1090:1092	arg1	structure					1077:1085	the three-dimensional structure	1055:1085	the three-dimensional structure of MPO	1055:1092	Data are discussed with regard to biosynthesis and the three-dimensional structure of MPO.
20332087	7	33	theme	MPO	1090:1092	arg1	biosynthesis					1038:1049	biosynthesis	1038:1049	biosynthesis	1038:1049	Data are discussed with regard to biosynthesis and the three-dimensional structure of MPO.
20332087	6	34	theme	biological	856:865	arg1	functionality					867:879	biological functionality	856:879	biological functionality of glycosylated and deglycosylated recombinant MPO	856:930	Comparison of biological functionality of glycosylated and deglycosylated recombinant MPO suggests that glycosylation is required for optimal enzymatic activity.
20332087	1	35	theme	various	195:201	arg1	conditions					216:225	various inflammatory conditions	195:225	various inflammatory conditions	195:225	The involvement of myeloperoxidase (MPO) in various inflammatory conditions has been the scope of many recent studies.
20332087	3	36	theme	native	449:454	arg1	MPO					470:472	native dimeric human MPO	449:472	native dimeric human MPO purified from neutrophils	449:498	Here, the N-glycan composition of native dimeric human MPO purified from neutrophils and of monomeric MPO recombinantly expressed in Chinese hamster ovary cells has been investigated.
20332087	0	37	theme	dimeric	32:38	arg1	leukocyte					40:48	mature dimeric leukocyte	25:48	mature dimeric leukocyte	25:48	Glycosylation pattern of mature dimeric leukocyte and recombinant monomeric myeloperoxidase: glycosylation is required for optimal enzymatic activity.
20332087	4	38	attach	presence	619:626	arg1	positions					649:657	positions 323, 355, 391, 483, 729	649:681	positions 323, 355, 391, 483, 729	649:681	Analyses showed the presence of five N-glycans at positions 323, 355, 391, 483, 729 in both proteins.
20332087	4	38	attach	presence	619:626	arg2	N-glycans					636:644	five N-glycans	631:644	five N-glycans	631:644	Analyses showed the presence of five N-glycans at positions 323, 355, 391, 483, 729 in both proteins.
20332087	3	39	theme	dimeric	456:462	arg1	MPO					470:472	native dimeric human MPO	449:472	native dimeric human MPO purified from neutrophils	449:498	Here, the N-glycan composition of native dimeric human MPO purified from neutrophils and of monomeric MPO recombinantly expressed in Chinese hamster ovary cells has been investigated.
20332087	0	40	theme	recombinant	54:64	arg1	glycosylation					93:105	recombinant monomeric myeloperoxidase: glycosylation	54:105	recombinant monomeric myeloperoxidase: glycosylation	54:105	Glycosylation pattern of mature dimeric leukocyte and recombinant monomeric myeloperoxidase: glycosylation is required for optimal enzymatic activity.
20332087	2	41	theme	structure	339:347	arg1	role					319:322	the role	315:322	the role of its overall structure and glycosylation pattern in biological function	315:396	Besides its well studied catalytic activity, the role of its overall structure and glycosylation pattern in biological function is barely known.
20332087	2	42	theme	overall	331:337	arg1	structure					339:347	its overall structure	327:347	its overall structure	327:347	Besides its well studied catalytic activity, the role of its overall structure and glycosylation pattern in biological function is barely known.
20332087	6	43	dep	glycosylated	884:895	arg1	MPO					928:930	recombinant MPO	916:930	recombinant MPO	916:930	Comparison of biological functionality of glycosylated and deglycosylated recombinant MPO suggests that glycosylation is required for optimal enzymatic activity.
20332087	7	44	theme	three-dimensional	1059:1075	arg1	structure					1077:1085	the three-dimensional structure	1055:1085	the three-dimensional structure of MPO	1055:1092	Data are discussed with regard to biosynthesis and the three-dimensional structure of MPO.
20332087	3	45	theme	Chinese	548:554	arg1	cells					570:574	Chinese hamster ovary cells	548:574	Chinese hamster ovary cells	548:574	Here, the N-glycan composition of native dimeric human MPO purified from neutrophils and of monomeric MPO recombinantly expressed in Chinese hamster ovary cells has been investigated.
20332087	0	46	theme	myeloperoxidase	76:90	arg1	glycosylation					93:105	recombinant monomeric myeloperoxidase: glycosylation	54:105	recombinant monomeric myeloperoxidase: glycosylation	54:105	Glycosylation pattern of mature dimeric leukocyte and recombinant monomeric myeloperoxidase: glycosylation is required for optimal enzymatic activity.
20332087	3	47	theme	human	464:468	arg1	MPO					470:472	native dimeric human MPO	449:472	native dimeric human MPO purified from neutrophils	449:498	Here, the N-glycan composition of native dimeric human MPO purified from neutrophils and of monomeric MPO recombinantly expressed in Chinese hamster ovary cells has been investigated.
20332087	3	48	theme	MPO	517:519	arg1	composition					434:444	the N-glycan composition	421:444	the N-glycan composition of native dimeric human MPO purified from neutrophils and of monomeric MPO recombinantly expressed in Chinese hamster ovary cells	421:574	Here, the N-glycan composition of native dimeric human MPO purified from neutrophils and of monomeric MPO recombinantly expressed in Chinese hamster ovary cells has been investigated.
20332087	0	49	theme	monomeric	66:74	arg1	glycosylation					93:105	recombinant monomeric myeloperoxidase: glycosylation	54:105	recombinant monomeric myeloperoxidase: glycosylation	54:105	Glycosylation pattern of mature dimeric leukocyte and recombinant monomeric myeloperoxidase: glycosylation is required for optimal enzymatic activity.
20332087	2	50	theme	pattern	367:373	arg1	role					319:322	the role	315:322	the role of its overall structure and glycosylation pattern in biological function	315:396	Besides its well studied catalytic activity, the role of its overall structure and glycosylation pattern in biological function is barely known.
20332087	1	51	theme	many	249:252	arg1	studies					261:267	many recent studies	249:267	many recent studies	249:267	The involvement of myeloperoxidase (MPO) in various inflammatory conditions has been the scope of many recent studies.
19088065	8	0	theme	molecular	969:977	arg1	difference					986:995	the molecular weight difference	965:995	the molecular weight difference between the two isoforms	965:1020	Mobility gel shift Western blot analysis coupled with glycosidase digestion showed that the molecular weight difference between the two isoforms was because of differential glycosylation patterns.
19088065	5	1	theme	high	551:554	arg1	levels					556:561	high levels	551:561	high levels	551:561	Under physiological conditions, KLK6 is expressed highly in the central nervous system and found at high levels in cerebrospinal fluid from where it enters the circulation.
19088065	4	2	theme	carcinomas	374:383	arg1	majority					354:361	The majority	350:361	The majority of ovarian carcinomas	350:383	The majority of ovarian carcinomas express high levels of KLK6, which diffuses into the circulation.
19088065	11	3	theme	tandem	1515:1520	arg1	spectrometry					1527:1538	electrospray ionization-Orbitrap tandem mass spectrometry	1482:1538	electrospray ionization-Orbitrap tandem mass spectrometry	1482:1538	The structure and composition of glycans of both KLK6 isoforms was elucidated by glycopeptide monitoring with electrospray ionization-Orbitrap tandem mass spectrometry.
19088065	3	4	from	elevation	271:279	arg1	serum					284:288	serum	284:288	serum	284:288	Kallikrein 6 (KLK6) elevation in serum is a diagnostic and prognostic indicator in ovarian cancer.
19088065	3	5	theme	Kallikrein	251:260	arg1	elevation					271:279	Kallikrein 6 (KLK6) elevation	251:279	Kallikrein 6 (KLK6) elevation in serum	251:288	Kallikrein 6 (KLK6) elevation in serum is a diagnostic and prognostic indicator in ovarian cancer.
19088065	3	5	theme	Kallikrein	251:260	arg1	indicator					321:329	a diagnostic and prognostic indicator	293:329	a diagnostic and prognostic indicator in ovarian cancer	293:347	Kallikrein 6 (KLK6) elevation in serum is a diagnostic and prognostic indicator in ovarian cancer.
19088065	4	6	theme	high	393:396	arg1	levels					398:403	high levels	393:403	high levels	393:403	The majority of ovarian carcinomas express high levels of KLK6, which diffuses into the circulation.
19088065	11	7	theme	electrospray	1482:1493	arg1	spectrometry					1527:1538	electrospray ionization-Orbitrap tandem mass spectrometry	1482:1538	electrospray ionization-Orbitrap tandem mass spectrometry	1482:1538	The structure and composition of glycans of both KLK6 isoforms was elucidated by glycopeptide monitoring with electrospray ionization-Orbitrap tandem mass spectrometry.
19088065	7	8	theme	post-translational	823:840	arg1	modifications					842:854	different post-translational modifications	813:854	different post-translational modifications on the two isoforms	813:874	Anion-exchange chromatography was used to reveal different post-translational modifications on the two isoforms.
19088065	12	9	theme	early	1696:1700	arg1	diagnosis					1702:1710	the early diagnosis	1692:1710	the early diagnosis of ovarian carcinoma	1692:1731	Therefore, the extensive and almost exclusive sialylation of KLK6 from ovarian cancer cells could lead to the development of an improved biomarker for the early diagnosis of ovarian carcinoma.
19088065	5	10	theme	physiological	457:469	arg1	conditions					471:480	physiological conditions	457:480	physiological conditions	457:480	Under physiological conditions, KLK6 is expressed highly in the central nervous system and found at high levels in cerebrospinal fluid from where it enters the circulation.
19088065	5	11	theme	nervous	523:529	arg1	system					531:536	the central nervous system	511:536	the central nervous system	511:536	Under physiological conditions, KLK6 is expressed highly in the central nervous system and found at high levels in cerebrospinal fluid from where it enters the circulation.
19088065	10	12	theme	alpha2-6-linked	1343:1357	arg1	acid					1366:1369	alpha2-6-linked sialic acid	1343:1369	alpha2-6-linked sialic acid	1343:1369	Using a Sambucus nigra agglutinin-monoclonal antibody sandwich enzyme-linked immunosorbent assay approach, it was shown that ovarian cancer-derived KLK6 was modified with alpha2-6-linked sialic acid.
19088065	12	13	theme	improved	1669:1676	arg1	biomarker					1678:1686	an improved biomarker	1666:1686	an improved biomarker for the early diagnosis of ovarian carcinoma	1666:1731	Therefore, the extensive and almost exclusive sialylation of KLK6 from ovarian cancer cells could lead to the development of an improved biomarker for the early diagnosis of ovarian carcinoma.
19088065	11	14	theme	KLK6	1421:1424	arg1	isoforms					1426:1433	both KLK6 isoforms	1416:1433	both KLK6 isoforms	1416:1433	The structure and composition of glycans of both KLK6 isoforms was elucidated by glycopeptide monitoring with electrospray ionization-Orbitrap tandem mass spectrometry.
19088065	9	15	attach	presence	1078:1085	arg1	KLK6					1123:1126	KLK6	1123:1126	KLK6	1123:1126	The presence of a single N-glycosylation site on KLK6 was confirmed by site-directed mutagenesis.
19088065	9	15	attach	presence	1078:1085	arg2	site					1115:1118	a single N-glycosylation site	1090:1118	a single N-glycosylation site	1090:1118	The presence of a single N-glycosylation site on KLK6 was confirmed by site-directed mutagenesis.
19088065	12	16	theme	extensive	1556:1564	arg1	sialylation					1587:1597	the extensive and almost exclusive sialylation	1552:1597	the extensive and almost exclusive sialylation of KLK6 from ovarian cancer cells	1552:1631	Therefore, the extensive and almost exclusive sialylation of KLK6 from ovarian cancer cells could lead to the development of an improved biomarker for the early diagnosis of ovarian carcinoma.
19088065	1	17	theme	more	132:135	arg1	deaths					137:142	more deaths	132:142	more deaths	132:142	Ovarian cancer causes more deaths than any other gynecological disorder.
19088065	3	18	theme	prognostic	310:319	arg1	elevation					271:279	Kallikrein 6 (KLK6) elevation	251:279	Kallikrein 6 (KLK6) elevation in serum	251:288	Kallikrein 6 (KLK6) elevation in serum is a diagnostic and prognostic indicator in ovarian cancer.
19088065	3	18	theme	prognostic	310:319	arg1	indicator					321:329	a diagnostic and prognostic indicator	293:329	a diagnostic and prognostic indicator in ovarian cancer	293:347	Kallikrein 6 (KLK6) elevation in serum is a diagnostic and prognostic indicator in ovarian cancer.
19088065	0	19	theme	cancer	66:71	arg1	cells					73:77	ovarian cancer cells	58:77	ovarian cancer cells	58:77	Differential N-glycosylation of kallikrein 6 derived from ovarian cancer cells or the central nervous system.
19088065	2	20	theme	malignancy	239:248	arg1	hallmarks					221:229	the hallmarks	217:229	the hallmarks of this malignancy	217:248	Perturbed glycosylation is one of the hallmarks of this malignancy.
19088065	3	21	theme	diagnostic	295:304	arg1	elevation					271:279	Kallikrein 6 (KLK6) elevation	251:279	Kallikrein 6 (KLK6) elevation in serum	251:288	Kallikrein 6 (KLK6) elevation in serum is a diagnostic and prognostic indicator in ovarian cancer.
19088065	3	21	theme	diagnostic	295:304	arg1	indicator					321:329	a diagnostic and prognostic indicator	293:329	a diagnostic and prognostic indicator in ovarian cancer	293:347	Kallikrein 6 (KLK6) elevation in serum is a diagnostic and prognostic indicator in ovarian cancer.
19088065	8	22	theme	differential	1037:1048	arg1	patterns					1064:1071	differential glycosylation patterns	1037:1071	differential glycosylation patterns	1037:1071	Mobility gel shift Western blot analysis coupled with glycosidase digestion showed that the molecular weight difference between the two isoforms was because of differential glycosylation patterns.
19088065	5	23	theme	cerebrospinal	566:578	arg1	fluid					580:584	cerebrospinal fluid	566:584	cerebrospinal fluid from where it enters the circulation	566:621	Under physiological conditions, KLK6 is expressed highly in the central nervous system and found at high levels in cerebrospinal fluid from where it enters the circulation.
19088065	1	24	theme	other	153:157	arg1	disorder					173:180	any other gynecological disorder	149:180	any other gynecological disorder	149:180	Ovarian cancer causes more deaths than any other gynecological disorder.
19088065	10	25	theme	cancer-derived	1305:1318	arg1	KLK6					1320:1323	ovarian cancer-derived KLK6	1297:1323	ovarian cancer-derived KLK6	1297:1323	Using a Sambucus nigra agglutinin-monoclonal antibody sandwich enzyme-linked immunosorbent assay approach, it was shown that ovarian cancer-derived KLK6 was modified with alpha2-6-linked sialic acid.
19088065	0	26	theme	central	86:92	arg1	system					102:107	the central nervous system	82:107	the central nervous system	82:107	Differential N-glycosylation of kallikrein 6 derived from ovarian cancer cells or the central nervous system.
19088065	8	27	theme	Mobility	877:884	arg1	analysis					909:916	Mobility gel shift Western blot analysis	877:916	Mobility gel shift Western blot analysis coupled with glycosidase digestion	877:951	Mobility gel shift Western blot analysis coupled with glycosidase digestion showed that the molecular weight difference between the two isoforms was because of differential glycosylation patterns.
19088065	9	28	theme	N-glycosylation	1099:1113	arg1	site					1115:1118	a single N-glycosylation site	1090:1118	a single N-glycosylation site	1090:1118	The presence of a single N-glycosylation site on KLK6 was confirmed by site-directed mutagenesis.
19088065	10	29	theme	assay	1263:1267	arg1	approach					1269:1276	a Sambucus nigra agglutinin-monoclonal antibody sandwich enzyme-linked immunosorbent assay approach	1178:1276	a Sambucus nigra agglutinin-monoclonal antibody sandwich enzyme-linked immunosorbent assay approach	1178:1276	Using a Sambucus nigra agglutinin-monoclonal antibody sandwich enzyme-linked immunosorbent assay approach, it was shown that ovarian cancer-derived KLK6 was modified with alpha2-6-linked sialic acid.
19088065	8	30	theme	shift	890:894	arg1	analysis					909:916	Mobility gel shift Western blot analysis	877:916	Mobility gel shift Western blot analysis coupled with glycosidase digestion	877:951	Mobility gel shift Western blot analysis coupled with glycosidase digestion showed that the molecular weight difference between the two isoforms was because of differential glycosylation patterns.
19088065	0	31	theme	Differential	0:11	arg1	N-glycosylation					13:27	Differential N-glycosylation	0:27	Differential N-glycosylation of kallikrein 6	0:43	Differential N-glycosylation of kallikrein 6 derived from ovarian cancer cells or the central nervous system.
19088065	12	32	from	cells	1627:1631	arg1	sialylation					1587:1597	the extensive and almost exclusive sialylation	1552:1597	the extensive and almost exclusive sialylation of KLK6 from ovarian cancer cells	1552:1631	Therefore, the extensive and almost exclusive sialylation of KLK6 from ovarian cancer cells could lead to the development of an improved biomarker for the early diagnosis of ovarian carcinoma.
19088065	8	33	theme	blot	904:907	arg1	analysis					909:916	Mobility gel shift Western blot analysis	877:916	Mobility gel shift Western blot analysis coupled with glycosidase digestion	877:951	Mobility gel shift Western blot analysis coupled with glycosidase digestion showed that the molecular weight difference between the two isoforms was because of differential glycosylation patterns.
19088065	10	34	link	alpha2-6-linked	1343:1357	arg1	acid					1366:1369	alpha2-6-linked sialic acid	1343:1369	alpha2-6-linked sialic acid	1343:1369	Using a Sambucus nigra agglutinin-monoclonal antibody sandwich enzyme-linked immunosorbent assay approach, it was shown that ovarian cancer-derived KLK6 was modified with alpha2-6-linked sialic acid.
19088065	12	35	gly	sialylation	1587:1597	arg1	KLK6					1602:1605	KLK6	1602:1605	KLK6	1602:1605	Therefore, the extensive and almost exclusive sialylation of KLK6 from ovarian cancer cells could lead to the development of an improved biomarker for the early diagnosis of ovarian carcinoma.
19088065	10	36	theme	agglutinin-monoclonal	1195:1215	arg1	assay					1263:1267	a Sambucus nigra agglutinin-monoclonal antibody sandwich enzyme-linked immunosorbent assay	1178:1267	a Sambucus nigra agglutinin-monoclonal antibody sandwich enzyme-linked immunosorbent assay approach	1178:1276	Using a Sambucus nigra agglutinin-monoclonal antibody sandwich enzyme-linked immunosorbent assay approach, it was shown that ovarian cancer-derived KLK6 was modified with alpha2-6-linked sialic acid.
19088065	12	37	theme	cancer	1620:1625	arg1	cells					1627:1631	ovarian cancer cells	1612:1631	ovarian cancer cells	1612:1631	Therefore, the extensive and almost exclusive sialylation of KLK6 from ovarian cancer cells could lead to the development of an improved biomarker for the early diagnosis of ovarian carcinoma.
19088065	0	38	gly	N-glycosylation	13:27	arg1	kallikrein					32:41	kallikrein 6	32:43	kallikrein 6	32:43	Differential N-glycosylation of kallikrein 6 derived from ovarian cancer cells or the central nervous system.
19088065	8	39	theme	glycosidase	931:941	arg1	digestion					943:951	glycosidase digestion	931:951	glycosidase digestion	931:951	Mobility gel shift Western blot analysis coupled with glycosidase digestion showed that the molecular weight difference between the two isoforms was because of differential glycosylation patterns.
19088065	11	40	dep	structure	1376:1384	arg1	The					1372:1374	The	1372:1374	The	1372:1374	The structure and composition of glycans of both KLK6 isoforms was elucidated by glycopeptide monitoring with electrospray ionization-Orbitrap tandem mass spectrometry.
19088065	7	41	used	used	798:801	arg2	chromatography					779:792	Anion-exchange chromatography	764:792	Anion-exchange chromatography	764:792	Anion-exchange chromatography was used to reveal different post-translational modifications on the two isoforms.
19088065	10	42	theme	Sambucus	1180:1187	arg1	assay					1263:1267	a Sambucus nigra agglutinin-monoclonal antibody sandwich enzyme-linked immunosorbent assay	1178:1267	a Sambucus nigra agglutinin-monoclonal antibody sandwich enzyme-linked immunosorbent assay approach	1178:1276	Using a Sambucus nigra agglutinin-monoclonal antibody sandwich enzyme-linked immunosorbent assay approach, it was shown that ovarian cancer-derived KLK6 was modified with alpha2-6-linked sialic acid.
19088065	12	43	theme	exclusive	1577:1585	arg1	sialylation					1587:1597	the extensive and almost exclusive sialylation	1552:1597	the extensive and almost exclusive sialylation of KLK6 from ovarian cancer cells	1552:1631	Therefore, the extensive and almost exclusive sialylation of KLK6 from ovarian cancer cells could lead to the development of an improved biomarker for the early diagnosis of ovarian carcinoma.
19088065	10	44	link	enzyme-linked	1235:1247	arg1	assay					1263:1267	a Sambucus nigra agglutinin-monoclonal antibody sandwich enzyme-linked immunosorbent assay	1178:1267	a Sambucus nigra agglutinin-monoclonal antibody sandwich enzyme-linked immunosorbent assay approach	1178:1276	Using a Sambucus nigra agglutinin-monoclonal antibody sandwich enzyme-linked immunosorbent assay approach, it was shown that ovarian cancer-derived KLK6 was modified with alpha2-6-linked sialic acid.
19088065	6	45	theme	cancer	718:723	arg1	ascites					725:731	ovarian cancer ascites fluid and cerebrospinal fluid	710:761	ovarian cancer ascites fluid and cerebrospinal fluid	710:761	Our aim was to characterize and compare the N-glycosylation status of this protein in ovarian cancer ascites fluid and cerebrospinal fluid.
19088065	6	45	theme	cancer	718:723	arg1	fluid					733:737	fluid	733:737	fluid	733:737	Our aim was to characterize and compare the N-glycosylation status of this protein in ovarian cancer ascites fluid and cerebrospinal fluid.
19088065	6	45	theme	cancer	718:723	arg1	fluid					757:761	cerebrospinal fluid	743:761	cerebrospinal fluid	743:761	Our aim was to characterize and compare the N-glycosylation status of this protein in ovarian cancer ascites fluid and cerebrospinal fluid.
19088065	10	46	theme	immunosorbent	1249:1261	arg1	assay					1263:1267	a Sambucus nigra agglutinin-monoclonal antibody sandwich enzyme-linked immunosorbent assay	1178:1267	a Sambucus nigra agglutinin-monoclonal antibody sandwich enzyme-linked immunosorbent assay approach	1178:1276	Using a Sambucus nigra agglutinin-monoclonal antibody sandwich enzyme-linked immunosorbent assay approach, it was shown that ovarian cancer-derived KLK6 was modified with alpha2-6-linked sialic acid.
19088065	11	47	theme	glycopeptide	1453:1464	arg1	monitoring					1466:1475	glycopeptide monitoring	1453:1475	glycopeptide monitoring with electrospray ionization-Orbitrap tandem mass spectrometry	1453:1538	The structure and composition of glycans of both KLK6 isoforms was elucidated by glycopeptide monitoring with electrospray ionization-Orbitrap tandem mass spectrometry.
19088065	10	48	theme	sandwich	1226:1233	arg1	assay					1263:1267	a Sambucus nigra agglutinin-monoclonal antibody sandwich enzyme-linked immunosorbent assay	1178:1267	a Sambucus nigra agglutinin-monoclonal antibody sandwich enzyme-linked immunosorbent assay approach	1178:1276	Using a Sambucus nigra agglutinin-monoclonal antibody sandwich enzyme-linked immunosorbent assay approach, it was shown that ovarian cancer-derived KLK6 was modified with alpha2-6-linked sialic acid.
19088065	10	49	dep	Sambucus	1180:1187	arg1	nigra					1189:1193	nigra	1189:1193	nigra	1189:1193	Using a Sambucus nigra agglutinin-monoclonal antibody sandwich enzyme-linked immunosorbent assay approach, it was shown that ovarian cancer-derived KLK6 was modified with alpha2-6-linked sialic acid.
19088065	8	50	theme	weight	979:984	arg1	difference					986:995	the molecular weight difference	965:995	the molecular weight difference between the two isoforms	965:1020	Mobility gel shift Western blot analysis coupled with glycosidase digestion showed that the molecular weight difference between the two isoforms was because of differential glycosylation patterns.
19088065	6	51	dep	ascites	725:731	arg1	ascites					725:731	ovarian cancer ascites fluid and cerebrospinal fluid	710:761	ovarian cancer ascites fluid and cerebrospinal fluid	710:761	Our aim was to characterize and compare the N-glycosylation status of this protein in ovarian cancer ascites fluid and cerebrospinal fluid.
19088065	6	51	dep	ascites	725:731	arg1	fluid					733:737	fluid	733:737	fluid	733:737	Our aim was to characterize and compare the N-glycosylation status of this protein in ovarian cancer ascites fluid and cerebrospinal fluid.
19088065	6	51	dep	ascites	725:731	arg1	fluid					757:761	cerebrospinal fluid	743:761	cerebrospinal fluid	743:761	Our aim was to characterize and compare the N-glycosylation status of this protein in ovarian cancer ascites fluid and cerebrospinal fluid.
19088065	11	52	theme	ionization-Orbitrap	1495:1513	arg1	spectrometry					1527:1538	electrospray ionization-Orbitrap tandem mass spectrometry	1482:1538	electrospray ionization-Orbitrap tandem mass spectrometry	1482:1538	The structure and composition of glycans of both KLK6 isoforms was elucidated by glycopeptide monitoring with electrospray ionization-Orbitrap tandem mass spectrometry.
19088065	1	53	theme	gynecological	159:171	arg1	disorder					173:180	any other gynecological disorder	149:180	any other gynecological disorder	149:180	Ovarian cancer causes more deaths than any other gynecological disorder.
19088065	6	54	from	status	684:689	arg1	ascites					725:731	ovarian cancer ascites fluid and cerebrospinal fluid	710:761	ovarian cancer ascites fluid and cerebrospinal fluid	710:761	Our aim was to characterize and compare the N-glycosylation status of this protein in ovarian cancer ascites fluid and cerebrospinal fluid.
19088065	6	54	from	status	684:689	arg1	fluid					733:737	fluid	733:737	fluid	733:737	Our aim was to characterize and compare the N-glycosylation status of this protein in ovarian cancer ascites fluid and cerebrospinal fluid.
19088065	6	54	from	status	684:689	arg1	fluid					757:761	cerebrospinal fluid	743:761	cerebrospinal fluid	743:761	Our aim was to characterize and compare the N-glycosylation status of this protein in ovarian cancer ascites fluid and cerebrospinal fluid.
19088065	11	55	theme	glycans	1405:1411	arg1	composition					1390:1400	composition	1390:1400	composition	1390:1400	The structure and composition of glycans of both KLK6 isoforms was elucidated by glycopeptide monitoring with electrospray ionization-Orbitrap tandem mass spectrometry.
19088065	11	55	theme	glycans	1405:1411	arg1	structure					1376:1384	structure	1376:1384	structure	1376:1384	The structure and composition of glycans of both KLK6 isoforms was elucidated by glycopeptide monitoring with electrospray ionization-Orbitrap tandem mass spectrometry.
19088065	4	56	theme	ovarian	366:372	arg1	carcinomas					374:383	ovarian carcinomas	366:383	ovarian carcinomas	366:383	The majority of ovarian carcinomas express high levels of KLK6, which diffuses into the circulation.
19088065	12	57	theme	carcinoma	1723:1731	arg1	diagnosis					1702:1710	the early diagnosis	1692:1710	the early diagnosis of ovarian carcinoma	1692:1731	Therefore, the extensive and almost exclusive sialylation of KLK6 from ovarian cancer cells could lead to the development of an improved biomarker for the early diagnosis of ovarian carcinoma.
19088065	6	58	theme	cerebrospinal	743:755	arg1	ascites					725:731	ovarian cancer ascites fluid and cerebrospinal fluid	710:761	ovarian cancer ascites fluid and cerebrospinal fluid	710:761	Our aim was to characterize and compare the N-glycosylation status of this protein in ovarian cancer ascites fluid and cerebrospinal fluid.
19088065	6	58	theme	cerebrospinal	743:755	arg1	fluid					757:761	cerebrospinal fluid	743:761	cerebrospinal fluid	743:761	Our aim was to characterize and compare the N-glycosylation status of this protein in ovarian cancer ascites fluid and cerebrospinal fluid.
19088065	12	59	theme	ovarian	1715:1721	arg1	carcinoma					1723:1731	ovarian carcinoma	1715:1731	ovarian carcinoma	1715:1731	Therefore, the extensive and almost exclusive sialylation of KLK6 from ovarian cancer cells could lead to the development of an improved biomarker for the early diagnosis of ovarian carcinoma.
19088065	11	60	theme	mass	1522:1525	arg1	spectrometry					1527:1538	electrospray ionization-Orbitrap tandem mass spectrometry	1482:1538	electrospray ionization-Orbitrap tandem mass spectrometry	1482:1538	The structure and composition of glycans of both KLK6 isoforms was elucidated by glycopeptide monitoring with electrospray ionization-Orbitrap tandem mass spectrometry.
19088065	11	61	theme	isoforms	1426:1433	arg1	glycans					1405:1411	glycans	1405:1411	glycans of both KLK6 isoforms	1405:1433	The structure and composition of glycans of both KLK6 isoforms was elucidated by glycopeptide monitoring with electrospray ionization-Orbitrap tandem mass spectrometry.
19088065	10	62	mod	modified	1329:1336	arg1	KLK6					1320:1323	ovarian cancer-derived KLK6	1297:1323	ovarian cancer-derived KLK6	1297:1323	Using a Sambucus nigra agglutinin-monoclonal antibody sandwich enzyme-linked immunosorbent assay approach, it was shown that ovarian cancer-derived KLK6 was modified with alpha2-6-linked sialic acid.
19088065	10	62	mod	modified	1329:1336	arg3	acid					1366:1369	alpha2-6-linked sialic acid	1343:1369	alpha2-6-linked sialic acid	1343:1369	Using a Sambucus nigra agglutinin-monoclonal antibody sandwich enzyme-linked immunosorbent assay approach, it was shown that ovarian cancer-derived KLK6 was modified with alpha2-6-linked sialic acid.
19088065	12	63	theme	biomarker	1678:1686	arg1	development					1651:1661	the development	1647:1661	the development of an improved biomarker for the early diagnosis of ovarian carcinoma	1647:1731	Therefore, the extensive and almost exclusive sialylation of KLK6 from ovarian cancer cells could lead to the development of an improved biomarker for the early diagnosis of ovarian carcinoma.
19088065	2	64	theme	hallmarks	221:229	arg1	one					210:212	one	210:212	one	210:212	Perturbed glycosylation is one of the hallmarks of this malignancy.
19088065	2	64	theme	hallmarks	221:229	arg1	hallmarks					221:229	the hallmarks	217:229	the hallmarks of this malignancy	217:248	Perturbed glycosylation is one of the hallmarks of this malignancy.
19088065	1	65	theme	Ovarian	110:116	arg1	cancer					118:123	Ovarian cancer	110:123	Ovarian cancer	110:123	Ovarian cancer causes more deaths than any other gynecological disorder.
19088065	4	66	theme	KLK6	408:411	arg1	levels					398:403	high levels	393:403	high levels	393:403	The majority of ovarian carcinomas express high levels of KLK6, which diffuses into the circulation.
19088065	10	67	theme	ovarian	1297:1303	arg1	KLK6					1320:1323	ovarian cancer-derived KLK6	1297:1323	ovarian cancer-derived KLK6	1297:1323	Using a Sambucus nigra agglutinin-monoclonal antibody sandwich enzyme-linked immunosorbent assay approach, it was shown that ovarian cancer-derived KLK6 was modified with alpha2-6-linked sialic acid.
19088065	3	68	from	indicator	321:329	arg1	cancer					342:347	ovarian cancer	334:347	ovarian cancer	334:347	Kallikrein 6 (KLK6) elevation in serum is a diagnostic and prognostic indicator in ovarian cancer.
19088065	8	69	theme	glycosylation	1050:1062	arg1	patterns					1064:1071	differential glycosylation patterns	1037:1071	differential glycosylation patterns	1037:1071	Mobility gel shift Western blot analysis coupled with glycosidase digestion showed that the molecular weight difference between the two isoforms was because of differential glycosylation patterns.
19088065	5	70	theme	central	515:521	arg1	system					531:536	the central nervous system	511:536	the central nervous system	511:536	Under physiological conditions, KLK6 is expressed highly in the central nervous system and found at high levels in cerebrospinal fluid from where it enters the circulation.
19088065	0	71	theme	nervous	94:100	arg1	system					102:107	the central nervous system	82:107	the central nervous system	82:107	Differential N-glycosylation of kallikrein 6 derived from ovarian cancer cells or the central nervous system.
19088065	9	72	theme	single	1092:1097	arg1	site					1115:1118	a single N-glycosylation site	1090:1118	a single N-glycosylation site	1090:1118	The presence of a single N-glycosylation site on KLK6 was confirmed by site-directed mutagenesis.
19088065	3	73	theme	ovarian	334:340	arg1	cancer					342:347	ovarian cancer	334:347	ovarian cancer	334:347	Kallikrein 6 (KLK6) elevation in serum is a diagnostic and prognostic indicator in ovarian cancer.
19088065	10	74	link	cancer-derived	1305:1318	arg1	KLK6					1320:1323	ovarian cancer-derived KLK6	1297:1323	ovarian cancer-derived KLK6	1297:1323	Using a Sambucus nigra agglutinin-monoclonal antibody sandwich enzyme-linked immunosorbent assay approach, it was shown that ovarian cancer-derived KLK6 was modified with alpha2-6-linked sialic acid.
19088065	10	75	theme	enzyme-linked	1235:1247	arg1	assay					1263:1267	a Sambucus nigra agglutinin-monoclonal antibody sandwich enzyme-linked immunosorbent assay	1178:1267	a Sambucus nigra agglutinin-monoclonal antibody sandwich enzyme-linked immunosorbent assay approach	1178:1276	Using a Sambucus nigra agglutinin-monoclonal antibody sandwich enzyme-linked immunosorbent assay approach, it was shown that ovarian cancer-derived KLK6 was modified with alpha2-6-linked sialic acid.
19088065	9	76	theme	site	1115:1118	arg1	presence					1078:1085	The presence	1074:1085	The presence of a single N-glycosylation site on KLK6	1074:1126	The presence of a single N-glycosylation site on KLK6 was confirmed by site-directed mutagenesis.
19088065	11	77	gly	glycopeptide	1453:1464	arg2	glycopeptide					1453:1464	glycopeptide	1453:1464	glycopeptide	1453:1464	The structure and composition of glycans of both KLK6 isoforms was elucidated by glycopeptide monitoring with electrospray ionization-Orbitrap tandem mass spectrometry.
19088065	8	78	theme	gel	886:888	arg1	analysis					909:916	Mobility gel shift Western blot analysis	877:916	Mobility gel shift Western blot analysis coupled with glycosidase digestion	877:951	Mobility gel shift Western blot analysis coupled with glycosidase digestion showed that the molecular weight difference between the two isoforms was because of differential glycosylation patterns.
19088065	0	79	theme	kallikrein	32:41	arg1	N-glycosylation					13:27	Differential N-glycosylation	0:27	Differential N-glycosylation of kallikrein 6	0:43	Differential N-glycosylation of kallikrein 6 derived from ovarian cancer cells or the central nervous system.
19088065	9	80	gly	N-glycosylation	1099:1113	arg2	site					1115:1118	a single N-glycosylation site	1090:1118	a single N-glycosylation site	1090:1118	The presence of a single N-glycosylation site on KLK6 was confirmed by site-directed mutagenesis.
19088065	8	81	theme	Western	896:902	arg1	analysis					909:916	Mobility gel shift Western blot analysis	877:916	Mobility gel shift Western blot analysis coupled with glycosidase digestion	877:951	Mobility gel shift Western blot analysis coupled with glycosidase digestion showed that the molecular weight difference between the two isoforms was because of differential glycosylation patterns.
19088065	2	82	theme	Perturbed	183:191	arg1	glycosylation					193:205	Perturbed glycosylation	183:205	Perturbed glycosylation	183:205	Perturbed glycosylation is one of the hallmarks of this malignancy.
19088065	7	83	theme	different	813:821	arg1	modifications					842:854	different post-translational modifications	813:854	different post-translational modifications on the two isoforms	813:874	Anion-exchange chromatography was used to reveal different post-translational modifications on the two isoforms.
19088065	10	84	theme	sialic	1359:1364	arg1	acid					1366:1369	alpha2-6-linked sialic acid	1343:1369	alpha2-6-linked sialic acid	1343:1369	Using a Sambucus nigra agglutinin-monoclonal antibody sandwich enzyme-linked immunosorbent assay approach, it was shown that ovarian cancer-derived KLK6 was modified with alpha2-6-linked sialic acid.
19088065	12	85	theme	KLK6	1602:1605	arg1	sialylation					1587:1597	the extensive and almost exclusive sialylation	1552:1597	the extensive and almost exclusive sialylation of KLK6 from ovarian cancer cells	1552:1631	Therefore, the extensive and almost exclusive sialylation of KLK6 from ovarian cancer cells could lead to the development of an improved biomarker for the early diagnosis of ovarian carcinoma.
19088065	9	86	theme	site-directed	1145:1157	arg1	mutagenesis					1159:1169	site-directed mutagenesis	1145:1169	site-directed mutagenesis	1145:1169	The presence of a single N-glycosylation site on KLK6 was confirmed by site-directed mutagenesis.
19088065	0	87	theme	ovarian	58:64	arg1	cells					73:77	ovarian cancer cells	58:77	ovarian cancer cells	58:77	Differential N-glycosylation of kallikrein 6 derived from ovarian cancer cells or the central nervous system.
19088065	7	88	theme	Anion-exchange	764:777	arg1	chromatography					779:792	Anion-exchange chromatography	764:792	Anion-exchange chromatography	764:792	Anion-exchange chromatography was used to reveal different post-translational modifications on the two isoforms.
19088065	12	89	theme	ovarian	1612:1618	arg1	cells					1627:1631	ovarian cancer cells	1612:1631	ovarian cancer cells	1612:1631	Therefore, the extensive and almost exclusive sialylation of KLK6 from ovarian cancer cells could lead to the development of an improved biomarker for the early diagnosis of ovarian carcinoma.
19088065	7	90	from	modifications	842:854	arg1	isoforms					867:874	the two isoforms	859:874	the two isoforms	859:874	Anion-exchange chromatography was used to reveal different post-translational modifications on the two isoforms.
19088065	9	91	from	presence	1078:1085	arg1	KLK6					1123:1126	KLK6	1123:1126	KLK6	1123:1126	The presence of a single N-glycosylation site on KLK6 was confirmed by site-directed mutagenesis.
19088065	6	92	theme	ovarian	710:716	arg1	ascites					725:731	ovarian cancer ascites fluid and cerebrospinal fluid	710:761	ovarian cancer ascites fluid and cerebrospinal fluid	710:761	Our aim was to characterize and compare the N-glycosylation status of this protein in ovarian cancer ascites fluid and cerebrospinal fluid.
19088065	6	92	theme	ovarian	710:716	arg1	fluid					733:737	fluid	733:737	fluid	733:737	Our aim was to characterize and compare the N-glycosylation status of this protein in ovarian cancer ascites fluid and cerebrospinal fluid.
19088065	6	92	theme	ovarian	710:716	arg1	fluid					757:761	cerebrospinal fluid	743:761	cerebrospinal fluid	743:761	Our aim was to characterize and compare the N-glycosylation status of this protein in ovarian cancer ascites fluid and cerebrospinal fluid.
19088065	6	93	theme	N-glycosylation	668:682	arg1	status					684:689	the N-glycosylation status	664:689	the N-glycosylation status of this protein in ovarian cancer ascites fluid and cerebrospinal fluid	664:761	Our aim was to characterize and compare the N-glycosylation status of this protein in ovarian cancer ascites fluid and cerebrospinal fluid.
19088065	6	94	gly	N-glycosylation	668:682	arg1	protein					699:705	this protein	694:705	this protein	694:705	Our aim was to characterize and compare the N-glycosylation status of this protein in ovarian cancer ascites fluid and cerebrospinal fluid.
19088065	11	95	with	monitoring	1466:1475	arg1	spectrometry					1527:1538	electrospray ionization-Orbitrap tandem mass spectrometry	1482:1538	electrospray ionization-Orbitrap tandem mass spectrometry	1482:1538	The structure and composition of glycans of both KLK6 isoforms was elucidated by glycopeptide monitoring with electrospray ionization-Orbitrap tandem mass spectrometry.
19088065	6	96	theme	protein	699:705	arg1	status					684:689	the N-glycosylation status	664:689	the N-glycosylation status of this protein in ovarian cancer ascites fluid and cerebrospinal fluid	664:761	Our aim was to characterize and compare the N-glycosylation status of this protein in ovarian cancer ascites fluid and cerebrospinal fluid.
19088065	10	97	theme	antibody	1217:1224	arg1	assay					1263:1267	a Sambucus nigra agglutinin-monoclonal antibody sandwich enzyme-linked immunosorbent assay	1178:1267	a Sambucus nigra agglutinin-monoclonal antibody sandwich enzyme-linked immunosorbent assay approach	1178:1276	Using a Sambucus nigra agglutinin-monoclonal antibody sandwich enzyme-linked immunosorbent assay approach, it was shown that ovarian cancer-derived KLK6 was modified with alpha2-6-linked sialic acid.
10988254	4	0	theme	activity	827:834	arg1	%					818:818	approximately 40%	802:818	approximately 40% of the activity of the native enzyme	802:855	Tunicamycin treatment completely abolished hFucTIII enzyme activity while castanospermine treatment diminished hFucTIII enzyme activity to approximately 40% of the activity of the native enzyme.
10988254	4	0	theme	activity	827:834	arg1	activity					827:834	the activity	823:834	the activity of the native enzyme	823:855	Tunicamycin treatment completely abolished hFucTIII enzyme activity while castanospermine treatment diminished hFucTIII enzyme activity to approximately 40% of the activity of the native enzyme.
10988254	7	1	theme	different	1306:1314	arg1	effects					1316:1322	different effects	1306:1322	different effects	1306:1322	All the mutants exhibited lower enzyme activity than the wild type and elimination of individual sites had different effects on the activity.
10988254	10	2	theme	activity	1797:1804	arg1	expression					1771:1780	expression	1771:1780	expression of full enzyme activity	1771:1804	The present study demonstrates that hFucTIII, -V, and -VI require N-glycosylation at the two conserved C-terminal N-glycosylation sites for expression of full enzyme activity.
10988254	0	3	theme	full	157:160	arg1	activity					169:176	full enzyme activity	157:176	full enzyme activity	157:176	The C-terminal N-glycosylation sites of the human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, adn -VI) are necessary for the expression of full enzyme activity.
10988254	7	4	theme	sites	1296:1300	arg1	elimination					1270:1280	elimination	1270:1280	elimination of individual sites	1270:1300	All the mutants exhibited lower enzyme activity than the wild type and elimination of individual sites had different effects on the activity.
10988254	6	5	theme	wild	1142:1145	arg1	type					1147:1150	wild type	1142:1150	wild type	1142:1150	Subsequently, the hFucTIII, -V, and -VI wild type and the mutants were expressed in COS-7 cells.
10988254	9	6	theme	Km	1556:1557	arg1	values					1559:1564	the Km values	1552:1564	the Km values for the oligosaccharide acceptor and the nucleotide sugar donor	1552:1628	Kinetic analysis of hFucTIII revealed that lack of glycosylation at Asn185 did not change the Km values for the oligosaccharide acceptor and the nucleotide sugar donor.
10988254	3	7	from	sites	644:648	arg1	hFucTIII					653:660	hFucTIII	653:660	hFucTIII	653:660	In the present study, we have analyzed the functional role of these potential N-glycosylation sites, laying the main emphasis on the sites in hFucTIII.
10988254	5	8	theme	mutant	971:976	arg1	DNAs					986:989	mutant genomic DNAs	971:989	mutant genomic DNAs in which the asparagine residues in the potential C-terminal N-glycosylation sites were replaced by glutamine	971:1099	To further analyze the role of the conserved N-glycosylation sites in hFucTIII, -V, and -VI, we made a series of mutant genomic DNAs in which the asparagine residues in the potential C-terminal N-glycosylation sites were replaced by glutamine.
10988254	5	9	theme	DNAs	986:989	arg1	series					961:966	a series	959:966	a series of mutant genomic DNAs in which the asparagine residues in the potential C-terminal N-glycosylation sites were replaced by glutamine	959:1099	To further analyze the role of the conserved N-glycosylation sites in hFucTIII, -V, and -VI, we made a series of mutant genomic DNAs in which the asparagine residues in the potential C-terminal N-glycosylation sites were replaced by glutamine.
10988254	9	10	from	Asn185	1530:1535	arg1	lack					1505:1508	lack	1505:1508	lack of glycosylation at Asn185	1505:1535	Kinetic analysis of hFucTIII revealed that lack of glycosylation at Asn185 did not change the Km values for the oligosaccharide acceptor and the nucleotide sugar donor.
10988254	9	11	theme	oligosaccharide	1574:1588	arg1	acceptor					1590:1597	the oligosaccharide acceptor	1570:1597	the oligosaccharide acceptor	1570:1597	Kinetic analysis of hFucTIII revealed that lack of glycosylation at Asn185 did not change the Km values for the oligosaccharide acceptor and the nucleotide sugar donor.
10988254	7	12	theme	wild	1256:1259	arg1	type					1261:1264	the wild type	1252:1264	the wild type	1252:1264	All the mutants exhibited lower enzyme activity than the wild type and elimination of individual sites had different effects on the activity.
10988254	4	13	theme	enzyme	850:855	arg1	activity					827:834	the activity	823:834	the activity of the native enzyme	823:855	Tunicamycin treatment completely abolished hFucTIII enzyme activity while castanospermine treatment diminished hFucTIII enzyme activity to approximately 40% of the activity of the native enzyme.
10988254	6	14	theme	COS-7	1186:1190	arg1	cells					1192:1196	COS-7 cells	1186:1196	COS-7 cells	1186:1196	Subsequently, the hFucTIII, -V, and -VI wild type and the mutants were expressed in COS-7 cells.
10988254	9	15	theme	nucleotide	1607:1616	arg1	donor					1624:1628	the nucleotide sugar donor	1603:1628	the nucleotide sugar donor	1603:1628	Kinetic analysis of hFucTIII revealed that lack of glycosylation at Asn185 did not change the Km values for the oligosaccharide acceptor and the nucleotide sugar donor.
10988254	7	16	theme	enzyme	1231:1236	arg1	activity					1238:1245	lower enzyme activity	1225:1245	lower enzyme activity	1225:1245	All the mutants exhibited lower enzyme activity than the wild type and elimination of individual sites had different effects on the activity.
10988254	5	17	gly	N-glycosylation	1052:1066	arg2	sites					1068:1072	the potential C-terminal N-glycosylation sites	1027:1072	the potential C-terminal N-glycosylation sites	1027:1072	To further analyze the role of the conserved N-glycosylation sites in hFucTIII, -V, and -VI, we made a series of mutant genomic DNAs in which the asparagine residues in the potential C-terminal N-glycosylation sites were replaced by glutamine.
10988254	8	18	theme	protein	1374:1380	arg1	level					1382:1386	the protein level	1370:1386	the protein level of the mutants in the cells	1370:1414	The mutations did not affect the protein level of the mutants in the cells, but reduced the molecular mass as predicted.
10988254	0	19	theme	-V	85:86	arg1	-V					85:86	-V	85:86	-V	85:86	The C-terminal N-glycosylation sites of the human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, adn -VI) are necessary for the expression of full enzyme activity.
10988254	0	19	theme	-V	85:86	arg1	alpha1,3/4-fucosyltransferase					50:78	the human alpha1,3/4-fucosyltransferase III	40:82	the human alpha1,3/4-fucosyltransferase III	40:82	The C-terminal N-glycosylation sites of the human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, adn -VI) are necessary for the expression of full enzyme activity.
10988254	0	19	theme	-V	85:86	arg1	sites					31:35	The C-terminal N-glycosylation sites	0:35	The C-terminal N-glycosylation sites of the human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, adn -VI)	0:119	The C-terminal N-glycosylation sites of the human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, adn -VI) are necessary for the expression of full enzyme activity.
10988254	0	19	theme	-V	85:86	arg1	-VI					93:95	-VI	93:95	-VI (hFucTIII, -V, adn -VI)	93:119	The C-terminal N-glycosylation sites of the human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, adn -VI) are necessary for the expression of full enzyme activity.
10988254	0	19	theme	-V	85:86	arg1	necessary					125:133	necessary	125:133	necessary	125:133	The C-terminal N-glycosylation sites of the human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, adn -VI) are necessary for the expression of full enzyme activity.
10988254	5	20	theme	potential	1031:1039	arg1	sites					1068:1072	the potential C-terminal N-glycosylation sites	1027:1072	the potential C-terminal N-glycosylation sites	1027:1072	To further analyze the role of the conserved N-glycosylation sites in hFucTIII, -V, and -VI, we made a series of mutant genomic DNAs in which the asparagine residues in the potential C-terminal N-glycosylation sites were replaced by glutamine.
10988254	5	21	theme	N-glycosylation	903:917	arg1	sites					919:923	the conserved N-glycosylation sites	889:923	the conserved N-glycosylation sites	889:923	To further analyze the role of the conserved N-glycosylation sites in hFucTIII, -V, and -VI, we made a series of mutant genomic DNAs in which the asparagine residues in the potential C-terminal N-glycosylation sites were replaced by glutamine.
10988254	8	22	theme	mutants	1395:1401	arg1	level					1382:1386	the protein level	1370:1386	the protein level of the mutants in the cells	1370:1414	The mutations did not affect the protein level of the mutants in the cells, but reduced the molecular mass as predicted.
10988254	4	23	theme	hFucTIII	706:713	arg1	activity					722:729	hFucTIII enzyme activity	706:729	hFucTIII enzyme activity	706:729	Tunicamycin treatment completely abolished hFucTIII enzyme activity while castanospermine treatment diminished hFucTIII enzyme activity to approximately 40% of the activity of the native enzyme.
10988254	5	24	theme	asparagine	1004:1013	arg1	residues					1015:1022	the asparagine residues	1000:1022	the asparagine residues in the potential C-terminal N-glycosylation sites	1000:1072	To further analyze the role of the conserved N-glycosylation sites in hFucTIII, -V, and -VI, we made a series of mutant genomic DNAs in which the asparagine residues in the potential C-terminal N-glycosylation sites were replaced by glutamine.
10988254	7	25	theme	lower	1225:1229	arg1	activity					1238:1245	lower enzyme activity	1225:1245	lower enzyme activity	1225:1245	All the mutants exhibited lower enzyme activity than the wild type and elimination of individual sites had different effects on the activity.
10988254	5	26	gly	N-glycosylation	903:917	arg2	sites					919:923	the conserved N-glycosylation sites	889:923	the conserved N-glycosylation sites	889:923	To further analyze the role of the conserved N-glycosylation sites in hFucTIII, -V, and -VI, we made a series of mutant genomic DNAs in which the asparagine residues in the potential C-terminal N-glycosylation sites were replaced by glutamine.
10988254	5	27	from	residues	1015:1022	arg1	sites					1068:1072	the potential C-terminal N-glycosylation sites	1027:1072	the potential C-terminal N-glycosylation sites	1027:1072	To further analyze the role of the conserved N-glycosylation sites in hFucTIII, -V, and -VI, we made a series of mutant genomic DNAs in which the asparagine residues in the potential C-terminal N-glycosylation sites were replaced by glutamine.
10988254	1	28	theme	fucosylated	247:257	arg1	glycoconjugates					272:286	fucosylated cell surface glycoconjugates	247:286	fucosylated cell surface glycoconjugates	247:286	The alpha1,3/4-fucosyltransferases are involved in the synthesis of fucosylated cell surface glycoconjugates.
10988254	2	29	dep	sites	415:419	arg1	sites					415:419	two conserved C-terminal N-glycosylation sites	374:419	two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184)	374:508	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	2	29	dep	sites	415:419	arg1	Asn184					502:507	Asn184	502:507	Asn184	502:507	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	2	29	dep	sites	415:419	arg1	hFucTV					451:456	hFucTV	451:456	hFucTV	451:456	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	2	29	dep	sites	415:419	arg1	hFucTIII					422:429	hFucTIII	422:429	hFucTIII	422:429	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	2	29	dep	sites	415:419	arg1	Asn153					491:496	Asn153	491:496	Asn153	491:496	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	2	29	dep	sites	415:419	arg1	Asn154					432:437	Asn154	432:437	Asn154	432:437	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	2	29	dep	sites	415:419	arg1	Asn167					459:464	Asn167	459:464	Asn167	459:464	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	2	30	theme	N-glycosylation	399:413	arg1	Asn198					470:475	Asn198	470:475	Asn198	470:475	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	2	30	theme	N-glycosylation	399:413	arg1	sites					415:419	two conserved C-terminal N-glycosylation sites	374:419	two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184)	374:508	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	2	30	theme	N-glycosylation	399:413	arg1	Asn184					502:507	Asn184	502:507	Asn184	502:507	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	2	30	theme	N-glycosylation	399:413	arg1	Asn185					443:448	Asn185	443:448	Asn185	443:448	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	2	30	theme	N-glycosylation	399:413	arg1	hFucTV					451:456	hFucTV	451:456	hFucTV	451:456	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	2	30	theme	N-glycosylation	399:413	arg1	hFucTIII					422:429	hFucTIII	422:429	hFucTIII	422:429	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	2	30	theme	N-glycosylation	399:413	arg1	Asn153					491:496	Asn153	491:496	Asn153	491:496	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	2	30	theme	N-glycosylation	399:413	arg1	Asn154					432:437	Asn154	432:437	Asn154	432:437	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	2	30	theme	N-glycosylation	399:413	arg1	Asn167					459:464	Asn167	459:464	Asn167	459:464	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	4	31	theme	Tunicamycin	663:673	arg1	treatment					675:683	Tunicamycin treatment	663:683	Tunicamycin treatment	663:683	Tunicamycin treatment completely abolished hFucTIII enzyme activity while castanospermine treatment diminished hFucTIII enzyme activity to approximately 40% of the activity of the native enzyme.
10988254	2	32	theme	conserved	378:386	arg1	Asn198					470:475	Asn198	470:475	Asn198	470:475	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	2	32	theme	conserved	378:386	arg1	sites					415:419	two conserved C-terminal N-glycosylation sites	374:419	two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184)	374:508	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	2	32	theme	conserved	378:386	arg1	Asn184					502:507	Asn184	502:507	Asn184	502:507	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	2	32	theme	conserved	378:386	arg1	Asn185					443:448	Asn185	443:448	Asn185	443:448	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	2	32	theme	conserved	378:386	arg1	hFucTV					451:456	hFucTV	451:456	hFucTV	451:456	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	2	32	theme	conserved	378:386	arg1	hFucTIII					422:429	hFucTIII	422:429	hFucTIII	422:429	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	2	32	theme	conserved	378:386	arg1	Asn153					491:496	Asn153	491:496	Asn153	491:496	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	2	32	theme	conserved	378:386	arg1	Asn154					432:437	Asn154	432:437	Asn154	432:437	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	2	32	theme	conserved	378:386	arg1	Asn167					459:464	Asn167	459:464	Asn167	459:464	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	0	33	theme	N-glycosylation	15:29	arg1	-V					85:86	-V	85:86	-V	85:86	The C-terminal N-glycosylation sites of the human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, adn -VI) are necessary for the expression of full enzyme activity.
10988254	0	33	theme	N-glycosylation	15:29	arg1	alpha1,3/4-fucosyltransferase					50:78	the human alpha1,3/4-fucosyltransferase III	40:82	the human alpha1,3/4-fucosyltransferase III	40:82	The C-terminal N-glycosylation sites of the human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, adn -VI) are necessary for the expression of full enzyme activity.
10988254	0	33	theme	N-glycosylation	15:29	arg1	sites					31:35	The C-terminal N-glycosylation sites	0:35	The C-terminal N-glycosylation sites of the human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, adn -VI)	0:119	The C-terminal N-glycosylation sites of the human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, adn -VI) are necessary for the expression of full enzyme activity.
10988254	0	33	theme	N-glycosylation	15:29	arg1	-VI					93:95	-VI	93:95	-VI (hFucTIII, -V, adn -VI)	93:119	The C-terminal N-glycosylation sites of the human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, adn -VI) are necessary for the expression of full enzyme activity.
10988254	0	33	theme	N-glycosylation	15:29	arg1	necessary					125:133	necessary	125:133	necessary	125:133	The C-terminal N-glycosylation sites of the human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, adn -VI) are necessary for the expression of full enzyme activity.
10988254	1	34	theme	surface	264:270	arg1	glycoconjugates					272:286	fucosylated cell surface glycoconjugates	247:286	fucosylated cell surface glycoconjugates	247:286	The alpha1,3/4-fucosyltransferases are involved in the synthesis of fucosylated cell surface glycoconjugates.
10988254	5	35	theme	N-glycosylation	1052:1066	arg1	sites					1068:1072	the potential C-terminal N-glycosylation sites	1027:1072	the potential C-terminal N-glycosylation sites	1027:1072	To further analyze the role of the conserved N-glycosylation sites in hFucTIII, -V, and -VI, we made a series of mutant genomic DNAs in which the asparagine residues in the potential C-terminal N-glycosylation sites were replaced by glutamine.
10988254	9	36	theme	Kinetic	1462:1468	arg1	analysis					1470:1477	Kinetic analysis	1462:1477	Kinetic analysis of hFucTIII	1462:1489	Kinetic analysis of hFucTIII revealed that lack of glycosylation at Asn185 did not change the Km values for the oligosaccharide acceptor and the nucleotide sugar donor.
10988254	8	37	theme	molecular	1433:1441	arg1	mass					1443:1446	the molecular mass	1429:1446	the molecular mass	1429:1446	The mutations did not affect the protein level of the mutants in the cells, but reduced the molecular mass as predicted.
10988254	3	38	theme	functional	554:563	arg1	role					565:568	the functional role	550:568	the functional role of these potential N-glycosylation sites	550:609	In the present study, we have analyzed the functional role of these potential N-glycosylation sites, laying the main emphasis on the sites in hFucTIII.
10988254	4	39	theme	enzyme	783:788	arg1	activity					790:797	hFucTIII enzyme activity	774:797	hFucTIII enzyme activity	774:797	Tunicamycin treatment completely abolished hFucTIII enzyme activity while castanospermine treatment diminished hFucTIII enzyme activity to approximately 40% of the activity of the native enzyme.
10988254	0	40	theme	human	44:48	arg1	alpha1,3/4-fucosyltransferase					50:78	the human alpha1,3/4-fucosyltransferase III	40:82	the human alpha1,3/4-fucosyltransferase III	40:82	The C-terminal N-glycosylation sites of the human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, adn -VI) are necessary for the expression of full enzyme activity.
10988254	10	41	theme	N-glycosylation	1745:1759	arg1	sites					1761:1765	the two conserved C-terminal N-glycosylation sites	1716:1765	the two conserved C-terminal N-glycosylation sites for expression of full enzyme activity	1716:1804	The present study demonstrates that hFucTIII, -V, and -VI require N-glycosylation at the two conserved C-terminal N-glycosylation sites for expression of full enzyme activity.
10988254	3	42	gly	N-glycosylation	589:603	arg2	sites					605:609	these potential N-glycosylation sites	573:609	these potential N-glycosylation sites	573:609	In the present study, we have analyzed the functional role of these potential N-glycosylation sites, laying the main emphasis on the sites in hFucTIII.
10988254	10	43	theme	conserved	1724:1732	arg1	sites					1761:1765	the two conserved C-terminal N-glycosylation sites	1716:1765	the two conserved C-terminal N-glycosylation sites for expression of full enzyme activity	1716:1804	The present study demonstrates that hFucTIII, -V, and -VI require N-glycosylation at the two conserved C-terminal N-glycosylation sites for expression of full enzyme activity.
10988254	4	44	theme	castanospermine	737:751	arg1	treatment					753:761	castanospermine treatment	737:761	castanospermine treatment	737:761	Tunicamycin treatment completely abolished hFucTIII enzyme activity while castanospermine treatment diminished hFucTIII enzyme activity to approximately 40% of the activity of the native enzyme.
10988254	5	45	from	role	881:884	arg1	-V					938:939	-V	938:939	-V	938:939	To further analyze the role of the conserved N-glycosylation sites in hFucTIII, -V, and -VI, we made a series of mutant genomic DNAs in which the asparagine residues in the potential C-terminal N-glycosylation sites were replaced by glutamine.
10988254	5	45	from	role	881:884	arg1	-VI					946:948	-VI	946:948	-VI	946:948	To further analyze the role of the conserved N-glycosylation sites in hFucTIII, -V, and -VI, we made a series of mutant genomic DNAs in which the asparagine residues in the potential C-terminal N-glycosylation sites were replaced by glutamine.
10988254	5	45	from	role	881:884	arg1	hFucTIII					928:935	hFucTIII	928:935	hFucTIII	928:935	To further analyze the role of the conserved N-glycosylation sites in hFucTIII, -V, and -VI, we made a series of mutant genomic DNAs in which the asparagine residues in the potential C-terminal N-glycosylation sites were replaced by glutamine.
10988254	2	46	gly	N-glycosylation	399:413	arg2	Asn185					443:448	Asn185	443:448	Asn185	443:448	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	2	46	gly	N-glycosylation	399:413	arg2	two					374:376	two	374:376	two	374:376	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	2	46	gly	N-glycosylation	399:413	arg2	hFucTIII					422:429	hFucTIII	422:429	hFucTIII	422:429	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	2	46	gly	N-glycosylation	399:413	arg2	hFucTV					451:456	hFucTV	451:456	hFucTV	451:456	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	2	46	gly	N-glycosylation	399:413	arg2	Asn154					432:437	Asn154	432:437	Asn154	432:437	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	2	46	gly	N-glycosylation	399:413	arg2	Asn153					491:496	Asn153	491:496	Asn153	491:496	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	2	46	gly	N-glycosylation	399:413	arg2	Asn167					459:464	Asn167	459:464	Asn167	459:464	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	2	46	gly	N-glycosylation	399:413	arg2	Asn184					502:507	Asn184	502:507	Asn184	502:507	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	2	46	gly	N-glycosylation	399:413	arg2	Asn198					470:475	Asn198	470:475	Asn198	470:475	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	2	46	gly	N-glycosylation	399:413	arg2	sites					415:419	two conserved C-terminal N-glycosylation sites	374:419	two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184)	374:508	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	7	47	contain	had	1302:1304	arg2	effects					1316:1322	different effects	1306:1322	different effects	1306:1322	All the mutants exhibited lower enzyme activity than the wild type and elimination of individual sites had different effects on the activity.
10988254	7	47	contain	had	1302:1304	arg1	elimination					1270:1280	elimination	1270:1280	elimination of individual sites	1270:1300	All the mutants exhibited lower enzyme activity than the wild type and elimination of individual sites had different effects on the activity.
10988254	3	48	theme	main	623:626	arg1	emphasis					628:635	the main emphasis	619:635	the main emphasis on the sites in hFucTIII	619:660	In the present study, we have analyzed the functional role of these potential N-glycosylation sites, laying the main emphasis on the sites in hFucTIII.
10988254	9	49	theme	glycosylation	1513:1525	arg1	lack					1505:1508	lack	1505:1508	lack of glycosylation at Asn185	1505:1535	Kinetic analysis of hFucTIII revealed that lack of glycosylation at Asn185 did not change the Km values for the oligosaccharide acceptor and the nucleotide sugar donor.
10988254	0	50	theme	enzyme	162:167	arg1	activity					169:176	full enzyme activity	157:176	full enzyme activity	157:176	The C-terminal N-glycosylation sites of the human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, adn -VI) are necessary for the expression of full enzyme activity.
10988254	10	51	gly	N-glycosylation	1745:1759	arg2	sites					1761:1765	the two conserved C-terminal N-glycosylation sites	1716:1765	the two conserved C-terminal N-glycosylation sites for expression of full enzyme activity	1716:1804	The present study demonstrates that hFucTIII, -V, and -VI require N-glycosylation at the two conserved C-terminal N-glycosylation sites for expression of full enzyme activity.
10988254	10	51	gly	N-glycosylation	1745:1759	arg2	two					1720:1722	two	1720:1722	two	1720:1722	The present study demonstrates that hFucTIII, -V, and -VI require N-glycosylation at the two conserved C-terminal N-glycosylation sites for expression of full enzyme activity.
10988254	3	52	from	emphasis	628:635	arg1	sites					644:648	the sites	640:648	the sites in hFucTIII	640:660	In the present study, we have analyzed the functional role of these potential N-glycosylation sites, laying the main emphasis on the sites in hFucTIII.
10988254	10	53	theme	enzyme	1790:1795	arg1	activity					1797:1804	full enzyme activity	1785:1804	full enzyme activity	1785:1804	The present study demonstrates that hFucTIII, -V, and -VI require N-glycosylation at the two conserved C-terminal N-glycosylation sites for expression of full enzyme activity.
10988254	0	54	theme	activity	169:176	arg1	expression					143:152	the expression	139:152	the expression of full enzyme activity	139:176	The C-terminal N-glycosylation sites of the human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, adn -VI) are necessary for the expression of full enzyme activity.
10988254	2	55	theme	Human	289:293	arg1	alpha1,3/4-fucosyltransferase					295:323	Human alpha1,3/4-fucosyltransferase III	289:327	Human alpha1,3/4-fucosyltransferase III	289:327	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	7	56	theme	individual	1285:1294	arg1	sites					1296:1300	individual sites	1285:1300	individual sites	1285:1300	All the mutants exhibited lower enzyme activity than the wild type and elimination of individual sites had different effects on the activity.
10988254	0	57	theme	adn	112:114	arg1	-VI					116:118	adn -VI	112:118	adn -VI	112:118	The C-terminal N-glycosylation sites of the human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, adn -VI) are necessary for the expression of full enzyme activity.
10988254	0	57	theme	adn	112:114	arg1	hFucTIII					98:105	hFucTIII	98:105	hFucTIII	98:105	The C-terminal N-glycosylation sites of the human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, adn -VI) are necessary for the expression of full enzyme activity.
10988254	5	58	theme	genomic	978:984	arg1	DNAs					986:989	mutant genomic DNAs	971:989	mutant genomic DNAs in which the asparagine residues in the potential C-terminal N-glycosylation sites were replaced by glutamine	971:1099	To further analyze the role of the conserved N-glycosylation sites in hFucTIII, -V, and -VI, we made a series of mutant genomic DNAs in which the asparagine residues in the potential C-terminal N-glycosylation sites were replaced by glutamine.
10988254	3	59	theme	present	518:524	arg1	study					526:530	the present study	514:530	the present study	514:530	In the present study, we have analyzed the functional role of these potential N-glycosylation sites, laying the main emphasis on the sites in hFucTIII.
10988254	10	60	gly	N-glycosylation	1697:1711	arg1	sites					1761:1765	the two conserved C-terminal N-glycosylation sites	1716:1765	the two conserved C-terminal N-glycosylation sites for expression of full enzyme activity	1716:1804	The present study demonstrates that hFucTIII, -V, and -VI require N-glycosylation at the two conserved C-terminal N-glycosylation sites for expression of full enzyme activity.
10988254	1	61	gly	fucosylated	247:257	arg1	glycoconjugates					272:286	fucosylated cell surface glycoconjugates	247:286	fucosylated cell surface glycoconjugates	247:286	The alpha1,3/4-fucosyltransferases are involved in the synthesis of fucosylated cell surface glycoconjugates.
10988254	3	62	theme	sites	605:609	arg1	role					565:568	the functional role	550:568	the functional role of these potential N-glycosylation sites	550:609	In the present study, we have analyzed the functional role of these potential N-glycosylation sites, laying the main emphasis on the sites in hFucTIII.
10988254	2	63	contain	contain	366:372	arg2	Asn185					443:448	Asn185	443:448	Asn185	443:448	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	2	63	contain	contain	366:372	arg1	alpha1,3/4-fucosyltransferase					295:323	Human alpha1,3/4-fucosyltransferase III	289:327	Human alpha1,3/4-fucosyltransferase III	289:327	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	2	63	contain	contain	366:372	arg2	hFucTIII					422:429	hFucTIII	422:429	hFucTIII	422:429	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	2	63	contain	contain	366:372	arg1	-VI					338:340	-VI	338:340	-VI (hFucTIII, -V, and -VI)	338:364	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	2	63	contain	contain	366:372	arg2	hFucTV					451:456	hFucTV	451:456	hFucTV	451:456	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	2	63	contain	contain	366:372	arg2	Asn154					432:437	Asn154	432:437	Asn154	432:437	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	2	63	contain	contain	366:372	arg2	Asn153					491:496	Asn153	491:496	Asn153	491:496	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	2	63	contain	contain	366:372	arg2	Asn167					459:464	Asn167	459:464	Asn167	459:464	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	2	63	contain	contain	366:372	arg2	Asn184					502:507	Asn184	502:507	Asn184	502:507	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	2	63	contain	contain	366:372	arg2	Asn198					470:475	Asn198	470:475	Asn198	470:475	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	2	63	contain	contain	366:372	arg1	-V					330:331	-V	330:331	-V	330:331	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	2	63	contain	contain	366:372	arg2	sites					415:419	two conserved C-terminal N-glycosylation sites	374:419	two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184)	374:508	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	10	64	theme	present	1635:1641	arg1	study					1643:1647	The present study	1631:1647	The present study	1631:1647	The present study demonstrates that hFucTIII, -V, and -VI require N-glycosylation at the two conserved C-terminal N-glycosylation sites for expression of full enzyme activity.
10988254	4	65	theme	native	843:848	arg1	enzyme					850:855	the native enzyme	839:855	the native enzyme	839:855	Tunicamycin treatment completely abolished hFucTIII enzyme activity while castanospermine treatment diminished hFucTIII enzyme activity to approximately 40% of the activity of the native enzyme.
10988254	6	66	dep	hFucTIII	1120:1127	arg1	type					1147:1150	wild type	1142:1150	wild type	1142:1150	Subsequently, the hFucTIII, -V, and -VI wild type and the mutants were expressed in COS-7 cells.
10988254	9	67	theme	sugar	1618:1622	arg1	donor					1624:1628	the nucleotide sugar donor	1603:1628	the nucleotide sugar donor	1603:1628	Kinetic analysis of hFucTIII revealed that lack of glycosylation at Asn185 did not change the Km values for the oligosaccharide acceptor and the nucleotide sugar donor.
10988254	0	68	theme	-VI	93:95	arg1	-V					85:86	-V	85:86	-V	85:86	The C-terminal N-glycosylation sites of the human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, adn -VI) are necessary for the expression of full enzyme activity.
10988254	0	68	theme	-VI	93:95	arg1	alpha1,3/4-fucosyltransferase					50:78	the human alpha1,3/4-fucosyltransferase III	40:82	the human alpha1,3/4-fucosyltransferase III	40:82	The C-terminal N-glycosylation sites of the human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, adn -VI) are necessary for the expression of full enzyme activity.
10988254	0	68	theme	-VI	93:95	arg1	sites					31:35	The C-terminal N-glycosylation sites	0:35	The C-terminal N-glycosylation sites of the human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, adn -VI)	0:119	The C-terminal N-glycosylation sites of the human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, adn -VI) are necessary for the expression of full enzyme activity.
10988254	0	68	theme	-VI	93:95	arg1	-VI					93:95	-VI	93:95	-VI (hFucTIII, -V, adn -VI)	93:119	The C-terminal N-glycosylation sites of the human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, adn -VI) are necessary for the expression of full enzyme activity.
10988254	0	68	theme	-VI	93:95	arg1	necessary					125:133	necessary	125:133	necessary	125:133	The C-terminal N-glycosylation sites of the human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, adn -VI) are necessary for the expression of full enzyme activity.
10988254	5	69	theme	C-terminal	1041:1050	arg1	sites					1068:1072	the potential C-terminal N-glycosylation sites	1027:1072	the potential C-terminal N-glycosylation sites	1027:1072	To further analyze the role of the conserved N-glycosylation sites in hFucTIII, -V, and -VI, we made a series of mutant genomic DNAs in which the asparagine residues in the potential C-terminal N-glycosylation sites were replaced by glutamine.
10988254	5	70	theme	conserved	893:901	arg1	sites					919:923	the conserved N-glycosylation sites	889:923	the conserved N-glycosylation sites	889:923	To further analyze the role of the conserved N-glycosylation sites in hFucTIII, -V, and -VI, we made a series of mutant genomic DNAs in which the asparagine residues in the potential C-terminal N-glycosylation sites were replaced by glutamine.
10988254	2	71	dep	-VI	338:340	arg1	-V					353:354	-V	353:354	-V	353:354	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	2	71	dep	-VI	338:340	arg1	-VI					361:363	-VI	361:363	-VI	361:363	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	2	71	dep	-VI	338:340	arg1	hFucTIII					343:350	hFucTIII	343:350	hFucTIII	343:350	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	5	72	theme	sites	919:923	arg1	role					881:884	the role	877:884	the role of the conserved N-glycosylation sites in hFucTIII, -V, and -VI	877:948	To further analyze the role of the conserved N-glycosylation sites in hFucTIII, -V, and -VI, we made a series of mutant genomic DNAs in which the asparagine residues in the potential C-terminal N-glycosylation sites were replaced by glutamine.
10988254	0	73	theme	C-terminal	4:13	arg1	-V					85:86	-V	85:86	-V	85:86	The C-terminal N-glycosylation sites of the human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, adn -VI) are necessary for the expression of full enzyme activity.
10988254	0	73	theme	C-terminal	4:13	arg1	alpha1,3/4-fucosyltransferase					50:78	the human alpha1,3/4-fucosyltransferase III	40:82	the human alpha1,3/4-fucosyltransferase III	40:82	The C-terminal N-glycosylation sites of the human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, adn -VI) are necessary for the expression of full enzyme activity.
10988254	0	73	theme	C-terminal	4:13	arg1	sites					31:35	The C-terminal N-glycosylation sites	0:35	The C-terminal N-glycosylation sites of the human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, adn -VI)	0:119	The C-terminal N-glycosylation sites of the human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, adn -VI) are necessary for the expression of full enzyme activity.
10988254	0	73	theme	C-terminal	4:13	arg1	-VI					93:95	-VI	93:95	-VI (hFucTIII, -V, adn -VI)	93:119	The C-terminal N-glycosylation sites of the human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, adn -VI) are necessary for the expression of full enzyme activity.
10988254	0	73	theme	C-terminal	4:13	arg1	necessary					125:133	necessary	125:133	necessary	125:133	The C-terminal N-glycosylation sites of the human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, adn -VI) are necessary for the expression of full enzyme activity.
10988254	3	74	theme	potential	579:587	arg1	sites					605:609	these potential N-glycosylation sites	573:609	these potential N-glycosylation sites	573:609	In the present study, we have analyzed the functional role of these potential N-glycosylation sites, laying the main emphasis on the sites in hFucTIII.
10988254	8	75	from	level	1382:1386	arg1	cells					1410:1414	the cells	1406:1414	the cells	1406:1414	The mutations did not affect the protein level of the mutants in the cells, but reduced the molecular mass as predicted.
10988254	1	76	theme	cell	259:262	arg1	glycoconjugates					272:286	fucosylated cell surface glycoconjugates	247:286	fucosylated cell surface glycoconjugates	247:286	The alpha1,3/4-fucosyltransferases are involved in the synthesis of fucosylated cell surface glycoconjugates.
10988254	2	77	theme	C-terminal	388:397	arg1	Asn198					470:475	Asn198	470:475	Asn198	470:475	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	2	77	theme	C-terminal	388:397	arg1	sites					415:419	two conserved C-terminal N-glycosylation sites	374:419	two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184)	374:508	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	2	77	theme	C-terminal	388:397	arg1	Asn184					502:507	Asn184	502:507	Asn184	502:507	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	2	77	theme	C-terminal	388:397	arg1	Asn185					443:448	Asn185	443:448	Asn185	443:448	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	2	77	theme	C-terminal	388:397	arg1	hFucTV					451:456	hFucTV	451:456	hFucTV	451:456	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	2	77	theme	C-terminal	388:397	arg1	hFucTIII					422:429	hFucTIII	422:429	hFucTIII	422:429	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	2	77	theme	C-terminal	388:397	arg1	Asn153					491:496	Asn153	491:496	Asn153	491:496	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	2	77	theme	C-terminal	388:397	arg1	Asn154					432:437	Asn154	432:437	Asn154	432:437	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	2	77	theme	C-terminal	388:397	arg1	Asn167					459:464	Asn167	459:464	Asn167	459:464	Human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, and -VI) contain two conserved C-terminal N-glycosylation sites (hFucTIII: Asn154 and Asn185; hFucTV: Asn167 and Asn198; and hFucTVI: Asn153 and Asn184).
10988254	0	78	dep	-VI	93:95	arg1	-V					108:109	-V	108:109	-V	108:109	The C-terminal N-glycosylation sites of the human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, adn -VI) are necessary for the expression of full enzyme activity.
10988254	0	78	dep	-VI	93:95	arg1	-VI					116:118	adn -VI	112:118	adn -VI	112:118	The C-terminal N-glycosylation sites of the human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, adn -VI) are necessary for the expression of full enzyme activity.
10988254	0	78	dep	-VI	93:95	arg1	hFucTIII					98:105	hFucTIII	98:105	hFucTIII	98:105	The C-terminal N-glycosylation sites of the human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, adn -VI) are necessary for the expression of full enzyme activity.
10988254	1	79	theme	glycoconjugates	272:286	arg1	synthesis					234:242	the synthesis	230:242	the synthesis of fucosylated cell surface glycoconjugates	230:286	The alpha1,3/4-fucosyltransferases are involved in the synthesis of fucosylated cell surface glycoconjugates.
10988254	0	80	theme	alpha1,3/4-fucosyltransferase	50:78	arg1	-V					85:86	-V	85:86	-V	85:86	The C-terminal N-glycosylation sites of the human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, adn -VI) are necessary for the expression of full enzyme activity.
10988254	0	80	theme	alpha1,3/4-fucosyltransferase	50:78	arg1	alpha1,3/4-fucosyltransferase					50:78	the human alpha1,3/4-fucosyltransferase III	40:82	the human alpha1,3/4-fucosyltransferase III	40:82	The C-terminal N-glycosylation sites of the human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, adn -VI) are necessary for the expression of full enzyme activity.
10988254	0	80	theme	alpha1,3/4-fucosyltransferase	50:78	arg1	sites					31:35	The C-terminal N-glycosylation sites	0:35	The C-terminal N-glycosylation sites of the human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, adn -VI)	0:119	The C-terminal N-glycosylation sites of the human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, adn -VI) are necessary for the expression of full enzyme activity.
10988254	0	80	theme	alpha1,3/4-fucosyltransferase	50:78	arg1	-VI					93:95	-VI	93:95	-VI (hFucTIII, -V, adn -VI)	93:119	The C-terminal N-glycosylation sites of the human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, adn -VI) are necessary for the expression of full enzyme activity.
10988254	0	80	theme	alpha1,3/4-fucosyltransferase	50:78	arg1	necessary					125:133	necessary	125:133	necessary	125:133	The C-terminal N-glycosylation sites of the human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, adn -VI) are necessary for the expression of full enzyme activity.
10988254	0	81	gly	N-glycosylation	15:29	arg1	-VI					93:95	-VI	93:95	-VI (hFucTIII, -V, adn -VI)	93:119	The C-terminal N-glycosylation sites of the human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, adn -VI) are necessary for the expression of full enzyme activity.
10988254	0	81	gly	N-glycosylation	15:29	arg2	-V					85:86	-V	85:86	-V	85:86	The C-terminal N-glycosylation sites of the human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, adn -VI) are necessary for the expression of full enzyme activity.
10988254	0	81	gly	N-glycosylation	15:29	arg2	alpha1,3/4-fucosyltransferase					50:78	the human alpha1,3/4-fucosyltransferase III	40:82	the human alpha1,3/4-fucosyltransferase III	40:82	The C-terminal N-glycosylation sites of the human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, adn -VI) are necessary for the expression of full enzyme activity.
10988254	0	81	gly	N-glycosylation	15:29	arg2	-VI					93:95	-VI	93:95	-VI (hFucTIII, -V, adn -VI)	93:119	The C-terminal N-glycosylation sites of the human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, adn -VI) are necessary for the expression of full enzyme activity.
10988254	0	81	gly	N-glycosylation	15:29	arg1	-V					85:86	-V	85:86	-V	85:86	The C-terminal N-glycosylation sites of the human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, adn -VI) are necessary for the expression of full enzyme activity.
10988254	0	81	gly	N-glycosylation	15:29	arg2	necessary					125:133	necessary	125:133	necessary	125:133	The C-terminal N-glycosylation sites of the human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, adn -VI) are necessary for the expression of full enzyme activity.
10988254	0	81	gly	N-glycosylation	15:29	arg2	sites					31:35	The C-terminal N-glycosylation sites	0:35	The C-terminal N-glycosylation sites of the human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, adn -VI)	0:119	The C-terminal N-glycosylation sites of the human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, adn -VI) are necessary for the expression of full enzyme activity.
10988254	0	81	gly	N-glycosylation	15:29	arg1	alpha1,3/4-fucosyltransferase					50:78	the human alpha1,3/4-fucosyltransferase III	40:82	the human alpha1,3/4-fucosyltransferase III	40:82	The C-terminal N-glycosylation sites of the human alpha1,3/4-fucosyltransferase III, -V, and -VI (hFucTIII, -V, adn -VI) are necessary for the expression of full enzyme activity.
10988254	3	82	theme	N-glycosylation	589:603	arg1	sites					605:609	these potential N-glycosylation sites	573:609	these potential N-glycosylation sites	573:609	In the present study, we have analyzed the functional role of these potential N-glycosylation sites, laying the main emphasis on the sites in hFucTIII.
10988254	4	83	theme	hFucTIII	774:781	arg1	activity					790:797	hFucTIII enzyme activity	774:797	hFucTIII enzyme activity	774:797	Tunicamycin treatment completely abolished hFucTIII enzyme activity while castanospermine treatment diminished hFucTIII enzyme activity to approximately 40% of the activity of the native enzyme.
10988254	9	84	theme	hFucTIII	1482:1489	arg1	analysis					1470:1477	Kinetic analysis	1462:1477	Kinetic analysis of hFucTIII	1462:1489	Kinetic analysis of hFucTIII revealed that lack of glycosylation at Asn185 did not change the Km values for the oligosaccharide acceptor and the nucleotide sugar donor.
10988254	10	85	theme	C-terminal	1734:1743	arg1	sites					1761:1765	the two conserved C-terminal N-glycosylation sites	1716:1765	the two conserved C-terminal N-glycosylation sites for expression of full enzyme activity	1716:1804	The present study demonstrates that hFucTIII, -V, and -VI require N-glycosylation at the two conserved C-terminal N-glycosylation sites for expression of full enzyme activity.
10988254	4	86	theme	enzyme	715:720	arg1	activity					722:729	hFucTIII enzyme activity	706:729	hFucTIII enzyme activity	706:729	Tunicamycin treatment completely abolished hFucTIII enzyme activity while castanospermine treatment diminished hFucTIII enzyme activity to approximately 40% of the activity of the native enzyme.
10988254	10	87	theme	full	1785:1788	arg1	activity					1797:1804	full enzyme activity	1785:1804	full enzyme activity	1785:1804	The present study demonstrates that hFucTIII, -V, and -VI require N-glycosylation at the two conserved C-terminal N-glycosylation sites for expression of full enzyme activity.
18381078	1	0	theme	membrane	287:294	arg1	proteins					296:303	several plasma membrane proteins	272:303	several plasma membrane proteins	272:303	A disintegrin and metalloprotease 10 (ADAM10) is a type I transmembrane glycoprotein with four potential N-glycosylation sites (N267, N278, N439 and N551), that cleaves several plasma membrane proteins.
18381078	9	1	from	exosomes	1076:1083	arg1	fraction					1052:1059	a fraction	1050:1059	a fraction of ADAM10 from exosomes	1050:1083	Here, a fraction of ADAM10 from exosomes was found to contain more processed N-linked glycans than the cellular enzyme.
18381078	0	2	from	role	11:14	arg1	activity					79:86	activity	79:86	activity	79:86	Functional role of N-glycosylation from ADAM10 in processing, localization and activity of the enzyme.
18381078	0	2	from	role	11:14	arg1	localization					62:73	localization	62:73	localization	62:73	Functional role of N-glycosylation from ADAM10 in processing, localization and activity of the enzyme.
18381078	0	2	from	role	11:14	arg1	processing					50:59	processing	50:59	processing	50:59	Functional role of N-glycosylation from ADAM10 in processing, localization and activity of the enzyme.
18381078	1	3	gly	N-glycosylation	208:222	arg2	four					193:196	four	193:196	four	193:196	A disintegrin and metalloprotease 10 (ADAM10) is a type I transmembrane glycoprotein with four potential N-glycosylation sites (N267, N278, N439 and N551), that cleaves several plasma membrane proteins.
18381078	1	3	gly	N-glycosylation	208:222	arg2	N439					243:246	N439	243:246	N439	243:246	A disintegrin and metalloprotease 10 (ADAM10) is a type I transmembrane glycoprotein with four potential N-glycosylation sites (N267, N278, N439 and N551), that cleaves several plasma membrane proteins.
18381078	1	3	gly	N-glycosylation	208:222	arg2	N278					237:240	N278	237:240	N278	237:240	A disintegrin and metalloprotease 10 (ADAM10) is a type I transmembrane glycoprotein with four potential N-glycosylation sites (N267, N278, N439 and N551), that cleaves several plasma membrane proteins.
18381078	1	3	gly	N-glycosylation	208:222	arg2	N551					252:255	N551	252:255	N551	252:255	A disintegrin and metalloprotease 10 (ADAM10) is a type I transmembrane glycoprotein with four potential N-glycosylation sites (N267, N278, N439 and N551), that cleaves several plasma membrane proteins.
18381078	1	3	gly	N-glycosylation	208:222	arg2	sites					224:228	four potential N-glycosylation sites	193:228	four potential N-glycosylation sites (N267, N278, N439 and N551)	193:256	A disintegrin and metalloprotease 10 (ADAM10) is a type I transmembrane glycoprotein with four potential N-glycosylation sites (N267, N278, N439 and N551), that cleaves several plasma membrane proteins.
18381078	6	4	theme	increased	828:836	arg1	susceptibility					845:858	increased ADAM10 susceptibility	828:858	increased ADAM10 susceptibility to proteolysis	828:873	S441A showed increased ADAM10 susceptibility to proteolysis.
18381078	7	5	theme	N267	888:891	arg1	Mutation					876:883	Mutation	876:883	Mutation of N267, N439 and N551	876:906	Mutation of N267, N439 and N551 did not completely abolish enzyme activity, however, reduced levels were found.
18381078	9	6	contain	contain	1098:1104	arg2	glycans					1130:1136	more processed N-linked glycans	1106:1136	more processed N-linked glycans than the cellular enzyme	1106:1161	Here, a fraction of ADAM10 from exosomes was found to contain more processed N-linked glycans than the cellular enzyme.
18381078	9	6	contain	contain	1098:1104	arg1	fraction					1052:1059	a fraction	1050:1059	a fraction of ADAM10 from exosomes	1050:1083	Here, a fraction of ADAM10 from exosomes was found to contain more processed N-linked glycans than the cellular enzyme.
18381078	5	7	theme	metalloprotease	679:693	arg1	activity					695:702	metalloprotease activity	679:702	metalloprotease activity	679:702	Furthermore, it exhibited only residual levels of metalloprotease activity in vivo towards the L1 cell adhesion molecule, as well as in vitro, using a ProTNF-alpha peptide as substrate.
18381078	1	8	gly	glycoprotein	175:186	arg1	glycoprotein					175:186	a type I transmembrane glycoprotein	152:186	a type I transmembrane glycoprotein	152:186	A disintegrin and metalloprotease 10 (ADAM10) is a type I transmembrane glycoprotein with four potential N-glycosylation sites (N267, N278, N439 and N551), that cleaves several plasma membrane proteins.
18381078	1	8	gly	glycoprotein	175:186	arg1	metalloprotease					121:135	metalloprotease 10	121:138	metalloprotease 10	121:138	A disintegrin and metalloprotease 10 (ADAM10) is a type I transmembrane glycoprotein with four potential N-glycosylation sites (N267, N278, N439 and N551), that cleaves several plasma membrane proteins.
18381078	1	8	gly	glycoprotein	175:186	arg1	disintegrin					105:115	A disintegrin	103:115	A disintegrin	103:115	A disintegrin and metalloprotease 10 (ADAM10) is a type I transmembrane glycoprotein with four potential N-glycosylation sites (N267, N278, N439 and N551), that cleaves several plasma membrane proteins.
18381078	5	9	theme	ProTNF-alpha	780:791	arg1	peptide					793:799	a ProTNF-alpha peptide	778:799	a ProTNF-alpha peptide	778:799	Furthermore, it exhibited only residual levels of metalloprotease activity in vivo towards the L1 cell adhesion molecule, as well as in vitro, using a ProTNF-alpha peptide as substrate.
18381078	3	10	theme	Individual	387:396	arg1	mutants					419:425	Individual N-glycosylation site mutants	387:425	Individual N-glycosylation site mutants S269A, T280A, S441A, T553A	387:452	Individual N-glycosylation site mutants S269A, T280A, S441A, T553A were constructed, and results indicated that all sites were occupied.
18381078	0	11	theme	enzyme	95:100	arg1	activity					79:86	activity	79:86	activity	79:86	Functional role of N-glycosylation from ADAM10 in processing, localization and activity of the enzyme.
18381078	0	11	theme	enzyme	95:100	arg1	localization					62:73	localization	62:73	localization	62:73	Functional role of N-glycosylation from ADAM10 in processing, localization and activity of the enzyme.
18381078	0	11	theme	enzyme	95:100	arg1	processing					50:59	processing	50:59	processing	50:59	Functional role of N-glycosylation from ADAM10 in processing, localization and activity of the enzyme.
18381078	0	12	from	ADAM10	40:45	arg1	role					11:14	Functional role	0:14	Functional role of N-glycosylation from ADAM10 in processing, localization and activity of the enzyme.	0:101	Functional role of N-glycosylation from ADAM10 in processing, localization and activity of the enzyme.
18381078	9	13	link	N-linked	1121:1128	arg1	glycans					1130:1136	more processed N-linked glycans	1106:1136	more processed N-linked glycans than the cellular enzyme	1106:1161	Here, a fraction of ADAM10 from exosomes was found to contain more processed N-linked glycans than the cellular enzyme.
18381078	3	14	theme	N-glycosylation	398:412	arg1	mutants					419:425	Individual N-glycosylation site mutants	387:425	Individual N-glycosylation site mutants S269A, T280A, S441A, T553A	387:452	Individual N-glycosylation site mutants S269A, T280A, S441A, T553A were constructed, and results indicated that all sites were occupied.
18381078	6	15	theme	ADAM10	838:843	arg1	susceptibility					845:858	increased ADAM10 susceptibility	828:858	increased ADAM10 susceptibility to proteolysis	828:873	S441A showed increased ADAM10 susceptibility to proteolysis.
18381078	1	16	theme	type	154:157	arg1	glycoprotein					175:186	a type I transmembrane glycoprotein	152:186	a type I transmembrane glycoprotein	152:186	A disintegrin and metalloprotease 10 (ADAM10) is a type I transmembrane glycoprotein with four potential N-glycosylation sites (N267, N278, N439 and N551), that cleaves several plasma membrane proteins.
18381078	1	16	theme	type	154:157	arg1	metalloprotease					121:135	metalloprotease 10	121:138	metalloprotease 10	121:138	A disintegrin and metalloprotease 10 (ADAM10) is a type I transmembrane glycoprotein with four potential N-glycosylation sites (N267, N278, N439 and N551), that cleaves several plasma membrane proteins.
18381078	1	16	theme	type	154:157	arg1	disintegrin					105:115	A disintegrin	103:115	A disintegrin	103:115	A disintegrin and metalloprotease 10 (ADAM10) is a type I transmembrane glycoprotein with four potential N-glycosylation sites (N267, N278, N439 and N551), that cleaves several plasma membrane proteins.
18381078	0	17	theme	Functional	0:9	arg1	role					11:14	Functional role	0:14	Functional role of N-glycosylation from ADAM10 in processing, localization and activity of the enzyme.	0:101	Functional role of N-glycosylation from ADAM10 in processing, localization and activity of the enzyme.
18381078	9	18	theme	processed	1111:1119	arg1	glycans					1130:1136	more processed N-linked glycans	1106:1136	more processed N-linked glycans than the cellular enzyme	1106:1161	Here, a fraction of ADAM10 from exosomes was found to contain more processed N-linked glycans than the cellular enzyme.
18381078	2	19	contain	contain	340:346	arg2	glycans					378:384	high-mannose and complex-type glycans	348:384	glycans	378:384	In this work, ADAM10 was found to contain high-mannose and complex-type glycans.
18381078	2	19	contain	contain	340:346	arg1	ADAM10					320:325	ADAM10	320:325	ADAM10	320:325	In this work, ADAM10 was found to contain high-mannose and complex-type glycans.
18381078	0	20	theme	N-glycosylation	19:33	arg1	role					11:14	Functional role	0:14	Functional role of N-glycosylation from ADAM10 in processing, localization and activity of the enzyme.	0:101	Functional role of N-glycosylation from ADAM10 in processing, localization and activity of the enzyme.
18381078	9	21	theme	N-linked	1121:1128	arg1	glycans					1130:1136	more processed N-linked glycans	1106:1136	more processed N-linked glycans than the cellular enzyme	1106:1161	Here, a fraction of ADAM10 from exosomes was found to contain more processed N-linked glycans than the cellular enzyme.
18381078	10	22	from	conclusion	1167:1176	arg1	crucial					1198:1204	crucial	1198:1204	crucial	1198:1204	In conclusion, N-glycosylation is crucial for ADAM10 processing and resistance to proteolysis, and results suggest that it is required for full-enzyme activity.
18381078	7	23	theme	N439	894:897	arg1	Mutation					876:883	Mutation	876:883	Mutation of N267, N439 and N551	876:906	Mutation of N267, N439 and N551 did not completely abolish enzyme activity, however, reduced levels were found.
18381078	2	24	theme	complex-type	365:376	arg1	glycans					378:384	high-mannose and complex-type glycans	348:384	glycans	378:384	In this work, ADAM10 was found to contain high-mannose and complex-type glycans.
18381078	1	25	dep	sites	224:228	arg1	N551					252:255	N551	252:255	N551	252:255	A disintegrin and metalloprotease 10 (ADAM10) is a type I transmembrane glycoprotein with four potential N-glycosylation sites (N267, N278, N439 and N551), that cleaves several plasma membrane proteins.
18381078	1	25	dep	sites	224:228	arg1	sites					224:228	four potential N-glycosylation sites	193:228	four potential N-glycosylation sites (N267, N278, N439 and N551)	193:256	A disintegrin and metalloprotease 10 (ADAM10) is a type I transmembrane glycoprotein with four potential N-glycosylation sites (N267, N278, N439 and N551), that cleaves several plasma membrane proteins.
18381078	1	25	dep	sites	224:228	arg1	N439					243:246	N439	243:246	N439	243:246	A disintegrin and metalloprotease 10 (ADAM10) is a type I transmembrane glycoprotein with four potential N-glycosylation sites (N267, N278, N439 and N551), that cleaves several plasma membrane proteins.
18381078	1	25	dep	sites	224:228	arg1	N278					237:240	N278	237:240	N278	237:240	A disintegrin and metalloprotease 10 (ADAM10) is a type I transmembrane glycoprotein with four potential N-glycosylation sites (N267, N278, N439 and N551), that cleaves several plasma membrane proteins.
18381078	10	26	theme	ADAM10	1210:1215	arg1	processing					1217:1226	ADAM10 processing	1210:1226	ADAM10 processing	1210:1226	In conclusion, N-glycosylation is crucial for ADAM10 processing and resistance to proteolysis, and results suggest that it is required for full-enzyme activity.
18381078	4	27	theme	endoplasmic	561:571	arg1	reticulum					573:581	the endoplasmic reticulum	557:581	the endoplasmic reticulum	557:581	T280A was found to accumulate in the endoplasmic reticulum as the non-processed precursor of the enzyme.
18381078	5	28	theme	L1	724:725	arg1	molecule					741:748	the L1 cell adhesion molecule	720:748	the L1 cell adhesion molecule	720:748	Furthermore, it exhibited only residual levels of metalloprotease activity in vivo towards the L1 cell adhesion molecule, as well as in vitro, using a ProTNF-alpha peptide as substrate.
18381078	8	29	theme	secretory	1010:1018	arg1	vesicles					1020:1027	secretory vesicles	1010:1027	secretory vesicles	1010:1027	ADAM10 is sorted into secretory vesicles, the exosomes.
18381078	8	29	theme	secretory	1010:1018	arg1	exosomes					1034:1041	the exosomes	1030:1041	the exosomes	1030:1041	ADAM10 is sorted into secretory vesicles, the exosomes.
18381078	3	30	used	occupied	514:521	arg2	sites					503:507	all sites	499:507	all sites	499:507	Individual N-glycosylation site mutants S269A, T280A, S441A, T553A were constructed, and results indicated that all sites were occupied.
18381078	2	31	theme	high-mannose	348:359	arg1	glycans					378:384	high-mannose and complex-type glycans	348:384	glycans	378:384	In this work, ADAM10 was found to contain high-mannose and complex-type glycans.
18381078	5	32	theme	cell	727:730	arg1	molecule					741:748	the L1 cell adhesion molecule	720:748	the L1 cell adhesion molecule	720:748	Furthermore, it exhibited only residual levels of metalloprotease activity in vivo towards the L1 cell adhesion molecule, as well as in vitro, using a ProTNF-alpha peptide as substrate.
18381078	1	33	with	glycoprotein	175:186	arg1	sites					224:228	four potential N-glycosylation sites	193:228	four potential N-glycosylation sites (N267, N278, N439 and N551)	193:256	A disintegrin and metalloprotease 10 (ADAM10) is a type I transmembrane glycoprotein with four potential N-glycosylation sites (N267, N278, N439 and N551), that cleaves several plasma membrane proteins.
18381078	1	33	with	glycoprotein	175:186	arg1	N551					252:255	N551	252:255	N551	252:255	A disintegrin and metalloprotease 10 (ADAM10) is a type I transmembrane glycoprotein with four potential N-glycosylation sites (N267, N278, N439 and N551), that cleaves several plasma membrane proteins.
18381078	1	33	with	glycoprotein	175:186	arg1	N439					243:246	N439	243:246	N439	243:246	A disintegrin and metalloprotease 10 (ADAM10) is a type I transmembrane glycoprotein with four potential N-glycosylation sites (N267, N278, N439 and N551), that cleaves several plasma membrane proteins.
18381078	1	33	with	glycoprotein	175:186	arg1	N278					237:240	N278	237:240	N278	237:240	A disintegrin and metalloprotease 10 (ADAM10) is a type I transmembrane glycoprotein with four potential N-glycosylation sites (N267, N278, N439 and N551), that cleaves several plasma membrane proteins.
18381078	5	34	theme	activity	695:702	arg1	levels					669:674	only residual levels	655:674	only residual levels of metalloprotease activity	655:702	Furthermore, it exhibited only residual levels of metalloprotease activity in vivo towards the L1 cell adhesion molecule, as well as in vitro, using a ProTNF-alpha peptide as substrate.
18381078	5	35	theme	adhesion	732:739	arg1	molecule					741:748	the L1 cell adhesion molecule	720:748	the L1 cell adhesion molecule	720:748	Furthermore, it exhibited only residual levels of metalloprotease activity in vivo towards the L1 cell adhesion molecule, as well as in vitro, using a ProTNF-alpha peptide as substrate.
18381078	7	36	theme	reduced	961:967	arg1	levels					969:974	reduced levels	961:974	reduced levels	961:974	Mutation of N267, N439 and N551 did not completely abolish enzyme activity, however, reduced levels were found.
18381078	9	37	theme	cellular	1147:1154	arg1	enzyme					1156:1161	the cellular enzyme	1143:1161	the cellular enzyme	1143:1161	Here, a fraction of ADAM10 from exosomes was found to contain more processed N-linked glycans than the cellular enzyme.
18381078	10	38	from	crucial	1198:1204	arg1	conclusion					1167:1176	conclusion	1167:1176	conclusion	1167:1176	In conclusion, N-glycosylation is crucial for ADAM10 processing and resistance to proteolysis, and results suggest that it is required for full-enzyme activity.
18381078	5	39	theme	residual	660:667	arg1	levels					669:674	only residual levels	655:674	only residual levels of metalloprotease activity	655:702	Furthermore, it exhibited only residual levels of metalloprotease activity in vivo towards the L1 cell adhesion molecule, as well as in vitro, using a ProTNF-alpha peptide as substrate.
18381078	2	40	located	found	331:335	arg2	ADAM10					320:325	ADAM10	320:325	ADAM10	320:325	In this work, ADAM10 was found to contain high-mannose and complex-type glycans.
18381078	2	40	located	found	331:335	arg1	work					314:317	this work	309:317	this work	309:317	In this work, ADAM10 was found to contain high-mannose and complex-type glycans.
18381078	0	41	gly	N-glycosylation	19:33	arg1	enzyme					95:100	the enzyme	91:100	the enzyme	91:100	Functional role of N-glycosylation from ADAM10 in processing, localization and activity of the enzyme.
18381078	1	42	theme	several	272:278	arg1	proteins					296:303	several plasma membrane proteins	272:303	several plasma membrane proteins	272:303	A disintegrin and metalloprotease 10 (ADAM10) is a type I transmembrane glycoprotein with four potential N-glycosylation sites (N267, N278, N439 and N551), that cleaves several plasma membrane proteins.
18381078	3	43	gly	N-glycosylation	398:412	arg2	mutants					419:425	Individual N-glycosylation site mutants	387:425	Individual N-glycosylation site mutants S269A, T280A, S441A, T553A	387:452	Individual N-glycosylation site mutants S269A, T280A, S441A, T553A were constructed, and results indicated that all sites were occupied.
18381078	3	43	gly	N-glycosylation	398:412	arg2	site					414:417	Individual N-glycosylation site mutants	387:425	Individual N-glycosylation site mutants S269A, T280A, S441A, T553A	387:452	Individual N-glycosylation site mutants S269A, T280A, S441A, T553A were constructed, and results indicated that all sites were occupied.
18381078	7	44	theme	enzyme	935:940	arg1	activity					942:949	enzyme activity	935:949	enzyme activity	935:949	Mutation of N267, N439 and N551 did not completely abolish enzyme activity, however, reduced levels were found.
18381078	9	45	theme	ADAM10	1064:1069	arg1	fraction					1052:1059	a fraction	1050:1059	a fraction of ADAM10 from exosomes	1050:1083	Here, a fraction of ADAM10 from exosomes was found to contain more processed N-linked glycans than the cellular enzyme.
18381078	1	46	theme	potential	198:206	arg1	sites					224:228	four potential N-glycosylation sites	193:228	four potential N-glycosylation sites (N267, N278, N439 and N551)	193:256	A disintegrin and metalloprotease 10 (ADAM10) is a type I transmembrane glycoprotein with four potential N-glycosylation sites (N267, N278, N439 and N551), that cleaves several plasma membrane proteins.
18381078	1	46	theme	potential	198:206	arg1	N551					252:255	N551	252:255	N551	252:255	A disintegrin and metalloprotease 10 (ADAM10) is a type I transmembrane glycoprotein with four potential N-glycosylation sites (N267, N278, N439 and N551), that cleaves several plasma membrane proteins.
18381078	1	46	theme	potential	198:206	arg1	N439					243:246	N439	243:246	N439	243:246	A disintegrin and metalloprotease 10 (ADAM10) is a type I transmembrane glycoprotein with four potential N-glycosylation sites (N267, N278, N439 and N551), that cleaves several plasma membrane proteins.
18381078	1	46	theme	potential	198:206	arg1	N278					237:240	N278	237:240	N278	237:240	A disintegrin and metalloprotease 10 (ADAM10) is a type I transmembrane glycoprotein with four potential N-glycosylation sites (N267, N278, N439 and N551), that cleaves several plasma membrane proteins.
18381078	3	47	dep	mutants	419:425	arg1	S441A					441:445	S441A	441:445	S441A	441:445	Individual N-glycosylation site mutants S269A, T280A, S441A, T553A were constructed, and results indicated that all sites were occupied.
18381078	3	47	dep	mutants	419:425	arg1	T280A					434:438	T280A	434:438	T280A	434:438	Individual N-glycosylation site mutants S269A, T280A, S441A, T553A were constructed, and results indicated that all sites were occupied.
18381078	3	47	dep	mutants	419:425	arg1	T553A					448:452	T553A	448:452	T553A	448:452	Individual N-glycosylation site mutants S269A, T280A, S441A, T553A were constructed, and results indicated that all sites were occupied.
18381078	1	48	theme	N-glycosylation	208:222	arg1	sites					224:228	four potential N-glycosylation sites	193:228	four potential N-glycosylation sites (N267, N278, N439 and N551)	193:256	A disintegrin and metalloprotease 10 (ADAM10) is a type I transmembrane glycoprotein with four potential N-glycosylation sites (N267, N278, N439 and N551), that cleaves several plasma membrane proteins.
18381078	1	48	theme	N-glycosylation	208:222	arg1	N551					252:255	N551	252:255	N551	252:255	A disintegrin and metalloprotease 10 (ADAM10) is a type I transmembrane glycoprotein with four potential N-glycosylation sites (N267, N278, N439 and N551), that cleaves several plasma membrane proteins.
18381078	1	48	theme	N-glycosylation	208:222	arg1	N439					243:246	N439	243:246	N439	243:246	A disintegrin and metalloprotease 10 (ADAM10) is a type I transmembrane glycoprotein with four potential N-glycosylation sites (N267, N278, N439 and N551), that cleaves several plasma membrane proteins.
18381078	1	48	theme	N-glycosylation	208:222	arg1	N278					237:240	N278	237:240	N278	237:240	A disintegrin and metalloprotease 10 (ADAM10) is a type I transmembrane glycoprotein with four potential N-glycosylation sites (N267, N278, N439 and N551), that cleaves several plasma membrane proteins.
18381078	3	49	theme	site	414:417	arg1	mutants					419:425	Individual N-glycosylation site mutants	387:425	Individual N-glycosylation site mutants S269A, T280A, S441A, T553A	387:452	Individual N-glycosylation site mutants S269A, T280A, S441A, T553A were constructed, and results indicated that all sites were occupied.
18381078	1	50	theme	transmembrane	161:173	arg1	glycoprotein					175:186	a type I transmembrane glycoprotein	152:186	a type I transmembrane glycoprotein	152:186	A disintegrin and metalloprotease 10 (ADAM10) is a type I transmembrane glycoprotein with four potential N-glycosylation sites (N267, N278, N439 and N551), that cleaves several plasma membrane proteins.
18381078	1	50	theme	transmembrane	161:173	arg1	metalloprotease					121:135	metalloprotease 10	121:138	metalloprotease 10	121:138	A disintegrin and metalloprotease 10 (ADAM10) is a type I transmembrane glycoprotein with four potential N-glycosylation sites (N267, N278, N439 and N551), that cleaves several plasma membrane proteins.
18381078	1	50	theme	transmembrane	161:173	arg1	disintegrin					105:115	A disintegrin	103:115	A disintegrin	103:115	A disintegrin and metalloprotease 10 (ADAM10) is a type I transmembrane glycoprotein with four potential N-glycosylation sites (N267, N278, N439 and N551), that cleaves several plasma membrane proteins.
18381078	4	51	theme	non-processed	590:602	arg1	precursor					604:612	the non-processed precursor	586:612	the non-processed precursor of the enzyme	586:626	T280A was found to accumulate in the endoplasmic reticulum as the non-processed precursor of the enzyme.
18381078	10	52	theme	full-enzyme	1303:1313	arg1	activity					1315:1322	full-enzyme activity	1303:1322	full-enzyme activity	1303:1322	In conclusion, N-glycosylation is crucial for ADAM10 processing and resistance to proteolysis, and results suggest that it is required for full-enzyme activity.
18381078	1	53	theme	plasma	280:285	arg1	proteins					296:303	several plasma membrane proteins	272:303	several plasma membrane proteins	272:303	A disintegrin and metalloprotease 10 (ADAM10) is a type I transmembrane glycoprotein with four potential N-glycosylation sites (N267, N278, N439 and N551), that cleaves several plasma membrane proteins.
18381078	7	54	theme	N551	903:906	arg1	Mutation					876:883	Mutation	876:883	Mutation of N267, N439 and N551	876:906	Mutation of N267, N439 and N551 did not completely abolish enzyme activity, however, reduced levels were found.
18381078	4	55	theme	enzyme	621:626	arg1	precursor					604:612	the non-processed precursor	586:612	the non-processed precursor of the enzyme	586:626	T280A was found to accumulate in the endoplasmic reticulum as the non-processed precursor of the enzyme.
24311690	1	0	theme	human	123:127	arg1	progression					140:150	human cell-cycle progression	123:150	human cell-cycle progression	123:150	Host cell factor-1 (HCF-1), a transcriptional co-regulator of human cell-cycle progression, undergoes proteolytic maturation in which any of six repeated sequences is cleaved by the nutrient-responsive glycosyltransferase, O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT).
24311690	6	1	theme	active	961:966	arg1	site					968:971	the same active site	952:971	the same active site	952:971	Thus, protein glycosylation and HCF-1 cleavage occur in the same active site.
24311690	1	2	theme	cell-cycle	129:138	arg1	progression					140:150	human cell-cycle progression	123:150	human cell-cycle progression	123:150	Host cell factor-1 (HCF-1), a transcriptional co-regulator of human cell-cycle progression, undergoes proteolytic maturation in which any of six repeated sequences is cleaved by the nutrient-responsive glycosyltransferase, O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT).
24311690	2	3	theme	glycosyltransferase	527:545	arg1	site					554:557	the glycosyltransferase active site	523:557	the glycosyltransferase active site	523:557	We report that the tetratricopeptide-repeat domain of O-GlcNAc transferase binds the carboxyl-terminal portion of an HCF-1 proteolytic repeat such that the cleavage region lies in the glycosyltransferase active site above uridine diphosphate-GlcNAc.
24311690	6	4	theme	same	956:959	arg1	site					968:971	the same active site	952:971	the same active site	952:971	Thus, protein glycosylation and HCF-1 cleavage occur in the same active site.
24311690	4	5	theme	cysteine	701:708	arg1	residues					724:731	cysteine and glutamate residues	701:731	cysteine and glutamate residues	701:731	Cleavage occurs between cysteine and glutamate residues and results in a pyroglutamate product.
24311690	2	6	dep	repeat	478:483	arg1	lies					515:518	lies	515:518	lies in the glycosyltransferase active site above uridine diphosphate-GlcNAc	515:590	We report that the tetratricopeptide-repeat domain of O-GlcNAc transferase binds the carboxyl-terminal portion of an HCF-1 proteolytic repeat such that the cleavage region lies in the glycosyltransferase active site above uridine diphosphate-GlcNAc.
24311690	4	7	theme	glutamate	714:722	arg1	residues					724:731	cysteine and glutamate residues	701:731	cysteine and glutamate residues	701:731	Cleavage occurs between cysteine and glutamate residues and results in a pyroglutamate product.
24311690	1	8	theme	progression	140:150	arg1	factor-1					71:78	Host cell factor-1	61:78	Host cell factor-1 (HCF-1)	61:86	Host cell factor-1 (HCF-1), a transcriptional co-regulator of human cell-cycle progression, undergoes proteolytic maturation in which any of six repeated sequences is cleaved by the nutrient-responsive glycosyltransferase, O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT).
24311690	1	8	theme	progression	140:150	arg1	co-regulator					107:118	a transcriptional co-regulator	89:118	a transcriptional co-regulator of human cell-cycle progression	89:150	Host cell factor-1 (HCF-1), a transcriptional co-regulator of human cell-cycle progression, undergoes proteolytic maturation in which any of six repeated sequences is cleaved by the nutrient-responsive glycosyltransferase, O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT).
24311690	5	9	theme	cleavage	791:798	arg1	glutamate					805:813	the cleavage site glutamate	787:813	the cleavage site glutamate	787:813	Conversion of the cleavage site glutamate into serine converts an HCF-1 proteolytic repeat into a glycosylation substrate.
24311690	6	10	theme	protein	902:908	arg1	glycosylation					910:922	protein glycosylation	902:922	protein glycosylation	902:922	Thus, protein glycosylation and HCF-1 cleavage occur in the same active site.
24311690	1	11	theme	Host	61:64	arg1	factor-1					71:78	Host cell factor-1	61:78	Host cell factor-1 (HCF-1)	61:86	Host cell factor-1 (HCF-1), a transcriptional co-regulator of human cell-cycle progression, undergoes proteolytic maturation in which any of six repeated sequences is cleaved by the nutrient-responsive glycosyltransferase, O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT).
24311690	1	11	theme	Host	61:64	arg1	co-regulator					107:118	a transcriptional co-regulator	89:118	a transcriptional co-regulator of human cell-cycle progression	89:150	Host cell factor-1 (HCF-1), a transcriptional co-regulator of human cell-cycle progression, undergoes proteolytic maturation in which any of six repeated sequences is cleaved by the nutrient-responsive glycosyltransferase, O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT).
24311690	1	11	theme	Host	61:64	arg1	HCF-1					81:85	HCF-1	81:85	HCF-1	81:85	Host cell factor-1 (HCF-1), a transcriptional co-regulator of human cell-cycle progression, undergoes proteolytic maturation in which any of six repeated sequences is cleaved by the nutrient-responsive glycosyltransferase, O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT).
24311690	5	12	theme	site	800:803	arg1	glutamate					805:813	the cleavage site glutamate	787:813	the cleavage site glutamate	787:813	Conversion of the cleavage site glutamate into serine converts an HCF-1 proteolytic repeat into a glycosylation substrate.
24311690	1	13	theme	cell	66:69	arg1	factor-1					71:78	Host cell factor-1	61:78	Host cell factor-1 (HCF-1)	61:86	Host cell factor-1 (HCF-1), a transcriptional co-regulator of human cell-cycle progression, undergoes proteolytic maturation in which any of six repeated sequences is cleaved by the nutrient-responsive glycosyltransferase, O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT).
24311690	1	13	theme	cell	66:69	arg1	co-regulator					107:118	a transcriptional co-regulator	89:118	a transcriptional co-regulator of human cell-cycle progression	89:150	Host cell factor-1 (HCF-1), a transcriptional co-regulator of human cell-cycle progression, undergoes proteolytic maturation in which any of six repeated sequences is cleaved by the nutrient-responsive glycosyltransferase, O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT).
24311690	1	13	theme	cell	66:69	arg1	HCF-1					81:85	HCF-1	81:85	HCF-1	81:85	Host cell factor-1 (HCF-1), a transcriptional co-regulator of human cell-cycle progression, undergoes proteolytic maturation in which any of six repeated sequences is cleaved by the nutrient-responsive glycosyltransferase, O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT).
24311690	2	14	theme	tetratricopeptide-repeat	362:385	arg1	domain					387:392	the tetratricopeptide-repeat domain	358:392	the tetratricopeptide-repeat domain of O-GlcNAc transferase	358:416	We report that the tetratricopeptide-repeat domain of O-GlcNAc transferase binds the carboxyl-terminal portion of an HCF-1 proteolytic repeat such that the cleavage region lies in the glycosyltransferase active site above uridine diphosphate-GlcNAc.
24311690	2	14	theme	tetratricopeptide-repeat	362:385	arg1	transferase					406:416	O-GlcNAc transferase	397:416	O-GlcNAc transferase	397:416	We report that the tetratricopeptide-repeat domain of O-GlcNAc transferase binds the carboxyl-terminal portion of an HCF-1 proteolytic repeat such that the cleavage region lies in the glycosyltransferase active site above uridine diphosphate-GlcNAc.
24311690	1	15	theme	nutrient-responsive	243:261	arg1	transferase					324:334	O-linked N-acetylglucosamine (O-GlcNAc) transferase	284:334	O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT)	284:340	Host cell factor-1 (HCF-1), a transcriptional co-regulator of human cell-cycle progression, undergoes proteolytic maturation in which any of six repeated sequences is cleaved by the nutrient-responsive glycosyltransferase, O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT).
24311690	1	15	theme	nutrient-responsive	243:261	arg1	glycosyltransferase					263:281	the nutrient-responsive glycosyltransferase	239:281	the nutrient-responsive glycosyltransferase	239:281	Host cell factor-1 (HCF-1), a transcriptional co-regulator of human cell-cycle progression, undergoes proteolytic maturation in which any of six repeated sequences is cleaved by the nutrient-responsive glycosyltransferase, O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT).
24311690	1	16	theme	proteolytic	163:173	arg1	maturation					175:184	proteolytic maturation	163:184	proteolytic maturation in which any of six repeated sequences is cleaved by the nutrient-responsive glycosyltransferase, O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT)	163:340	Host cell factor-1 (HCF-1), a transcriptional co-regulator of human cell-cycle progression, undergoes proteolytic maturation in which any of six repeated sequences is cleaved by the nutrient-responsive glycosyltransferase, O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT).
24311690	2	17	theme	uridine	565:571	arg1	diphosphate-GlcNAc					573:590	uridine diphosphate-GlcNAc	565:590	uridine diphosphate-GlcNAc	565:590	We report that the tetratricopeptide-repeat domain of O-GlcNAc transferase binds the carboxyl-terminal portion of an HCF-1 proteolytic repeat such that the cleavage region lies in the glycosyltransferase active site above uridine diphosphate-GlcNAc.
24311690	5	18	theme	HCF-1	839:843	arg1	repeat					857:862	an HCF-1 proteolytic repeat	836:862	an HCF-1 proteolytic repeat	836:862	Conversion of the cleavage site glutamate into serine converts an HCF-1 proteolytic repeat into a glycosylation substrate.
24311690	2	19	theme	carboxyl-terminal	428:444	arg1	portion					446:452	the carboxyl-terminal portion	424:452	the carboxyl-terminal portion of an HCF-1 proteolytic repeat such that the cleavage region lies in the glycosyltransferase active site above uridine diphosphate-GlcNAc	424:590	We report that the tetratricopeptide-repeat domain of O-GlcNAc transferase binds the carboxyl-terminal portion of an HCF-1 proteolytic repeat such that the cleavage region lies in the glycosyltransferase active site above uridine diphosphate-GlcNAc.
24311690	2	20	dep	lies	515:518	arg1	such					485:488	such	485:488	such	485:488	We report that the tetratricopeptide-repeat domain of O-GlcNAc transferase binds the carboxyl-terminal portion of an HCF-1 proteolytic repeat such that the cleavage region lies in the glycosyltransferase active site above uridine diphosphate-GlcNAc.
24311690	6	21	theme	HCF-1	928:932	arg1	cleavage					934:941	HCF-1 cleavage	928:941	HCF-1 cleavage	928:941	Thus, protein glycosylation and HCF-1 cleavage occur in the same active site.
24311690	0	22	theme	active	24:29	arg1	site					31:34	the active site	20:34	the active site of O-GlcNAc transferase	20:58	HCF-1 is cleaved in the active site of O-GlcNAc transferase.
24311690	0	22	theme	active	24:29	arg1	transferase					48:58	O-GlcNAc transferase	39:58	O-GlcNAc transferase	39:58	HCF-1 is cleaved in the active site of O-GlcNAc transferase.
24311690	1	23	theme	O-linked	284:291	arg1	O-GlcNAc					314:321	O-GlcNAc	314:321	O-GlcNAc	314:321	Host cell factor-1 (HCF-1), a transcriptional co-regulator of human cell-cycle progression, undergoes proteolytic maturation in which any of six repeated sequences is cleaved by the nutrient-responsive glycosyltransferase, O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT).
24311690	1	23	theme	O-linked	284:291	arg1	N-acetylglucosamine					293:311	O-linked N-acetylglucosamine	284:311	O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT)	284:340	Host cell factor-1 (HCF-1), a transcriptional co-regulator of human cell-cycle progression, undergoes proteolytic maturation in which any of six repeated sequences is cleaved by the nutrient-responsive glycosyltransferase, O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT).
24311690	6	24	gly	glycosylation	910:922	arg2	site					968:971	the same active site	952:971	the same active site	952:971	Thus, protein glycosylation and HCF-1 cleavage occur in the same active site.
24311690	2	25	theme	transferase	406:416	arg1	domain					387:392	the tetratricopeptide-repeat domain	358:392	the tetratricopeptide-repeat domain of O-GlcNAc transferase	358:416	We report that the tetratricopeptide-repeat domain of O-GlcNAc transferase binds the carboxyl-terminal portion of an HCF-1 proteolytic repeat such that the cleavage region lies in the glycosyltransferase active site above uridine diphosphate-GlcNAc.
24311690	2	25	theme	transferase	406:416	arg1	transferase					406:416	O-GlcNAc transferase	397:416	O-GlcNAc transferase	397:416	We report that the tetratricopeptide-repeat domain of O-GlcNAc transferase binds the carboxyl-terminal portion of an HCF-1 proteolytic repeat such that the cleavage region lies in the glycosyltransferase active site above uridine diphosphate-GlcNAc.
24311690	2	26	theme	repeat	478:483	arg1	portion					446:452	the carboxyl-terminal portion	424:452	the carboxyl-terminal portion of an HCF-1 proteolytic repeat such that the cleavage region lies in the glycosyltransferase active site above uridine diphosphate-GlcNAc	424:590	We report that the tetratricopeptide-repeat domain of O-GlcNAc transferase binds the carboxyl-terminal portion of an HCF-1 proteolytic repeat such that the cleavage region lies in the glycosyltransferase active site above uridine diphosphate-GlcNAc.
24311690	1	27	theme	N-acetylglucosamine	293:311	arg1	OGT					337:339	OGT	337:339	OGT	337:339	Host cell factor-1 (HCF-1), a transcriptional co-regulator of human cell-cycle progression, undergoes proteolytic maturation in which any of six repeated sequences is cleaved by the nutrient-responsive glycosyltransferase, O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT).
24311690	1	27	theme	N-acetylglucosamine	293:311	arg1	transferase					324:334	O-linked N-acetylglucosamine (O-GlcNAc) transferase	284:334	O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT)	284:340	Host cell factor-1 (HCF-1), a transcriptional co-regulator of human cell-cycle progression, undergoes proteolytic maturation in which any of six repeated sequences is cleaved by the nutrient-responsive glycosyltransferase, O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT).
24311690	1	27	theme	N-acetylglucosamine	293:311	arg1	glycosyltransferase					263:281	the nutrient-responsive glycosyltransferase	239:281	the nutrient-responsive glycosyltransferase	239:281	Host cell factor-1 (HCF-1), a transcriptional co-regulator of human cell-cycle progression, undergoes proteolytic maturation in which any of six repeated sequences is cleaved by the nutrient-responsive glycosyltransferase, O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT).
24311690	2	28	theme	active	547:552	arg1	site					554:557	the glycosyltransferase active site	523:557	the glycosyltransferase active site	523:557	We report that the tetratricopeptide-repeat domain of O-GlcNAc transferase binds the carboxyl-terminal portion of an HCF-1 proteolytic repeat such that the cleavage region lies in the glycosyltransferase active site above uridine diphosphate-GlcNAc.
24311690	2	29	theme	O-GlcNAc	397:404	arg1	transferase					406:416	O-GlcNAc transferase	397:416	O-GlcNAc transferase	397:416	We report that the tetratricopeptide-repeat domain of O-GlcNAc transferase binds the carboxyl-terminal portion of an HCF-1 proteolytic repeat such that the cleavage region lies in the glycosyltransferase active site above uridine diphosphate-GlcNAc.
24311690	2	30	theme	proteolytic	466:476	arg1	repeat					478:483	an HCF-1 proteolytic repeat	457:483	an HCF-1 proteolytic repeat such that the cleavage region lies in the glycosyltransferase active site above uridine diphosphate-GlcNAc	457:590	We report that the tetratricopeptide-repeat domain of O-GlcNAc transferase binds the carboxyl-terminal portion of an HCF-1 proteolytic repeat such that the cleavage region lies in the glycosyltransferase active site above uridine diphosphate-GlcNAc.
24311690	5	31	theme	proteolytic	845:855	arg1	repeat					857:862	an HCF-1 proteolytic repeat	836:862	an HCF-1 proteolytic repeat	836:862	Conversion of the cleavage site glutamate into serine converts an HCF-1 proteolytic repeat into a glycosylation substrate.
24311690	2	32	theme	cleavage	499:506	arg1	region					508:513	the cleavage region	495:513	the cleavage region	495:513	We report that the tetratricopeptide-repeat domain of O-GlcNAc transferase binds the carboxyl-terminal portion of an HCF-1 proteolytic repeat such that the cleavage region lies in the glycosyltransferase active site above uridine diphosphate-GlcNAc.
24311690	4	33	theme	pyroglutamate	750:762	arg1	product					764:770	a pyroglutamate product	748:770	a pyroglutamate product	748:770	Cleavage occurs between cysteine and glutamate residues and results in a pyroglutamate product.
24311690	2	34	theme	HCF-1	460:464	arg1	repeat					478:483	an HCF-1 proteolytic repeat	457:483	an HCF-1 proteolytic repeat such that the cleavage region lies in the glycosyltransferase active site above uridine diphosphate-GlcNAc	457:590	We report that the tetratricopeptide-repeat domain of O-GlcNAc transferase binds the carboxyl-terminal portion of an HCF-1 proteolytic repeat such that the cleavage region lies in the glycosyltransferase active site above uridine diphosphate-GlcNAc.
24311690	3	35	theme	glycosylation-competent	634:656	arg1	substrate					666:674	a glycosylation-competent peptide substrate	632:674	a glycosylation-competent peptide substrate	632:674	The conformation is similar to that of a glycosylation-competent peptide substrate.
24311690	5	36	theme	glutamate	805:813	arg1	Conversion					773:782	Conversion	773:782	Conversion of the cleavage site glutamate into serine	773:825	Conversion of the cleavage site glutamate into serine converts an HCF-1 proteolytic repeat into a glycosylation substrate.
24311690	3	37	theme	peptide	658:664	arg1	substrate					666:674	a glycosylation-competent peptide substrate	632:674	a glycosylation-competent peptide substrate	632:674	The conformation is similar to that of a glycosylation-competent peptide substrate.
24311690	1	38	theme	transcriptional	91:105	arg1	factor-1					71:78	Host cell factor-1	61:78	Host cell factor-1 (HCF-1)	61:86	Host cell factor-1 (HCF-1), a transcriptional co-regulator of human cell-cycle progression, undergoes proteolytic maturation in which any of six repeated sequences is cleaved by the nutrient-responsive glycosyltransferase, O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT).
24311690	1	38	theme	transcriptional	91:105	arg1	co-regulator					107:118	a transcriptional co-regulator	89:118	a transcriptional co-regulator of human cell-cycle progression	89:150	Host cell factor-1 (HCF-1), a transcriptional co-regulator of human cell-cycle progression, undergoes proteolytic maturation in which any of six repeated sequences is cleaved by the nutrient-responsive glycosyltransferase, O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT).
24311690	0	39	theme	transferase	48:58	arg1	site					31:34	the active site	20:34	the active site of O-GlcNAc transferase	20:58	HCF-1 is cleaved in the active site of O-GlcNAc transferase.
24311690	0	39	theme	transferase	48:58	arg1	transferase					48:58	O-GlcNAc transferase	39:58	O-GlcNAc transferase	39:58	HCF-1 is cleaved in the active site of O-GlcNAc transferase.
24311690	1	40	link	O-linked	284:291	arg1	O-GlcNAc					314:321	O-GlcNAc	314:321	O-GlcNAc	314:321	Host cell factor-1 (HCF-1), a transcriptional co-regulator of human cell-cycle progression, undergoes proteolytic maturation in which any of six repeated sequences is cleaved by the nutrient-responsive glycosyltransferase, O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT).
24311690	1	40	link	O-linked	284:291	arg1	N-acetylglucosamine					293:311	O-linked N-acetylglucosamine	284:311	O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT)	284:340	Host cell factor-1 (HCF-1), a transcriptional co-regulator of human cell-cycle progression, undergoes proteolytic maturation in which any of six repeated sequences is cleaved by the nutrient-responsive glycosyltransferase, O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT).
24311690	1	41	theme	repeated	206:213	arg1	sequences					215:223	six repeated sequences	202:223	six repeated sequences	202:223	Host cell factor-1 (HCF-1), a transcriptional co-regulator of human cell-cycle progression, undergoes proteolytic maturation in which any of six repeated sequences is cleaved by the nutrient-responsive glycosyltransferase, O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT).
24311690	0	42	theme	O-GlcNAc	39:46	arg1	transferase					48:58	O-GlcNAc transferase	39:58	O-GlcNAc transferase	39:58	HCF-1 is cleaved in the active site of O-GlcNAc transferase.
24311690	5	43	theme	glycosylation	871:883	arg1	substrate					885:893	a glycosylation substrate	869:893	a glycosylation substrate	869:893	Conversion of the cleavage site glutamate into serine converts an HCF-1 proteolytic repeat into a glycosylation substrate.
14702339	11	0	theme	oligosaccharide	1821:1835	arg1	Asn-286					1840:1846	oligosaccharide at Asn-286	1821:1846	oligosaccharide at Asn-286	1821:1846	Thus, a dual role of oligosaccharide at Asn-286 in folding and lysosomal targeting could contribute to the unusual, but cell type-dependent, fate of misfolded TPP I conformer and represent the molecular basis of the disease process in subjects with naturally occurring missense mutation at Asn-286.
14702339	11	1	from	process	2024:2030	arg1	subjects					2035:2042	subjects	2035:2042	subjects with naturally occurring missense mutation at Asn-286	2035:2096	Thus, a dual role of oligosaccharide at Asn-286 in folding and lysosomal targeting could contribute to the unusual, but cell type-dependent, fate of misfolded TPP I conformer and represent the molecular basis of the disease process in subjects with naturally occurring missense mutation at Asn-286.
14702339	3	2	theme	Chinese	673:679	arg1	ovary					689:693	Chinese hamster ovary	673:693	Chinese hamster ovary	673:693	To analyze the role of N-glycosylation in the function of the enzyme, we obliterated each N- glycosylation consensus sequence by substituting Gln for Asn, either individually or in combinations, and expressed mutated cDNAs in Chinese hamster ovary and human embryonic kidney 293 cells.
14702339	4	3	theme	N-glycosylation	797:811	arg1	sites					813:817	all five N-glycosylation sites	788:817	all five N-glycosylation sites	788:817	Here, we demonstrate that human TPP I in vivo utilizes all five N-glycosylation sites.
14702339	6	4	theme	hamster	1076:1082	arg1	cells					1090:1094	Chinese hamster ovary cells	1068:1094	Chinese hamster ovary cells	1068:1094	However, in contrast to other misfolded proteins that are retained in the endoplasmic reticulum, only a fraction of misfolded TPP I mutant expressed in Chinese hamster ovary cells, but not in human embryonic kidney 293 cells, was arrested in the ER, whereas its major portion was secreted.
14702339	3	5	theme	kidney	715:720	arg1	cells					726:730	human embryonic kidney 293 cells	699:730	human embryonic kidney 293 cells	699:730	To analyze the role of N-glycosylation in the function of the enzyme, we obliterated each N- glycosylation consensus sequence by substituting Gln for Asn, either individually or in combinations, and expressed mutated cDNAs in Chinese hamster ovary and human embryonic kidney 293 cells.
14702339	3	6	from	role	462:465	arg1	function					493:500	the function	489:500	the function of the enzyme	489:514	To analyze the role of N-glycosylation in the function of the enzyme, we obliterated each N- glycosylation consensus sequence by substituting Gln for Asn, either individually or in combinations, and expressed mutated cDNAs in Chinese hamster ovary and human embryonic kidney 293 cells.
14702339	3	7	theme	N-	537:538	arg1	sequence					564:571	each N- glycosylation consensus sequence	532:571	each N- glycosylation consensus sequence	532:571	To analyze the role of N-glycosylation in the function of the enzyme, we obliterated each N- glycosylation consensus sequence by substituting Gln for Asn, either individually or in combinations, and expressed mutated cDNAs in Chinese hamster ovary and human embryonic kidney 293 cells.
14702339	3	8	theme	consensus	554:562	arg1	sequence					564:571	each N- glycosylation consensus sequence	532:571	each N- glycosylation consensus sequence	532:571	To analyze the role of N-glycosylation in the function of the enzyme, we obliterated each N- glycosylation consensus sequence by substituting Gln for Asn, either individually or in combinations, and expressed mutated cDNAs in Chinese hamster ovary and human embryonic kidney 293 cells.
14702339	7	9	theme	residual	1292:1299	arg1	activity					1307:1314	only residual TPP I activity	1287:1314	only residual TPP I activity	1287:1314	Secreted proenzyme formed non-native, interchain disulfide bridges and displayed only residual TPP I activity upon acidification.
14702339	3	10	theme	human	699:703	arg1	kidney					715:720	human embryonic kidney 293	699:724	human embryonic kidney 293 cells	699:730	To analyze the role of N-glycosylation in the function of the enzyme, we obliterated each N- glycosylation consensus sequence by substituting Gln for Asn, either individually or in combinations, and expressed mutated cDNAs in Chinese hamster ovary and human embryonic kidney 293 cells.
14702339	11	11	theme	type-dependent	1925:1938	arg1	fate					1941:1944	the unusual, but cell type-dependent, fate	1903:1944	the unusual, but cell type-dependent, fate of misfolded TPP I conformer	1903:1973	Thus, a dual role of oligosaccharide at Asn-286 in folding and lysosomal targeting could contribute to the unusual, but cell type-dependent, fate of misfolded TPP I conformer and represent the molecular basis of the disease process in subjects with naturally occurring missense mutation at Asn-286.
14702339	8	12	theme	small	1338:1342	arg1	portion					1344:1350	A small portion	1336:1350	A small portion of TPP I missing Asn-286-linked glycan	1336:1389	A small portion of TPP I missing Asn-286-linked glycan reached the lysosome and was processed to an active species; however, it showed low thermal and pH stability.
14702339	3	13	dep	Asn	597:599	arg1	combinations					628:639	combinations	628:639	combinations	628:639	To analyze the role of N-glycosylation in the function of the enzyme, we obliterated each N- glycosylation consensus sequence by substituting Gln for Asn, either individually or in combinations, and expressed mutated cDNAs in Chinese hamster ovary and human embryonic kidney 293 cells.
14702339	3	13	dep	Asn	597:599	arg1	either					602:607	either	602:607	either	602:607	To analyze the role of N-glycosylation in the function of the enzyme, we obliterated each N- glycosylation consensus sequence by substituting Gln for Asn, either individually or in combinations, and expressed mutated cDNAs in Chinese hamster ovary and human embryonic kidney 293 cells.
14702339	9	14	from	Asn-313	1532:1538	arg1	N-Glycans					1501:1509	N-Glycans	1501:1509	N-Glycans at Asn-210, Asn-222, Asn-313, and Asn-443	1501:1551	N-Glycans at Asn-210, Asn-222, Asn-313, and Asn-443 contributed slightly to the specific activity of the enzyme and its resistance to alkaline pH-induced inactivation.
14702339	11	15	theme	I	1963:1963	arg1	conformer					1965:1973	misfolded TPP I conformer	1949:1973	misfolded TPP I conformer	1949:1973	Thus, a dual role of oligosaccharide at Asn-286 in folding and lysosomal targeting could contribute to the unusual, but cell type-dependent, fate of misfolded TPP I conformer and represent the molecular basis of the disease process in subjects with naturally occurring missense mutation at Asn-286.
14702339	10	16	theme	Phospholabeling	1669:1683	arg1	experiments					1685:1695	Phospholabeling experiments	1669:1695	Phospholabeling experiments	1669:1695	Phospholabeling experiments revealed that N-glycans at Asn-210 and Asn-286 of TPP I preferentially accept a phosphomannose marker.
14702339	9	17	from	Asn-222	1523:1529	arg1	N-Glycans					1501:1509	N-Glycans	1501:1509	N-Glycans at Asn-210, Asn-222, Asn-313, and Asn-443	1501:1551	N-Glycans at Asn-210, Asn-222, Asn-313, and Asn-443 contributed slightly to the specific activity of the enzyme and its resistance to alkaline pH-induced inactivation.
14702339	11	18	theme	misfolded	1949:1957	arg1	conformer					1965:1973	misfolded TPP I conformer	1949:1973	misfolded TPP I conformer	1949:1973	Thus, a dual role of oligosaccharide at Asn-286 in folding and lysosomal targeting could contribute to the unusual, but cell type-dependent, fate of misfolded TPP I conformer and represent the molecular basis of the disease process in subjects with naturally occurring missense mutation at Asn-286.
14702339	6	19	theme	embryonic	1114:1122	arg1	kidney					1124:1129	human embryonic kidney 293	1108:1133	human embryonic kidney 293 cells	1108:1139	However, in contrast to other misfolded proteins that are retained in the endoplasmic reticulum, only a fraction of misfolded TPP I mutant expressed in Chinese hamster ovary cells, but not in human embryonic kidney 293 cells, was arrested in the ER, whereas its major portion was secreted.
14702339	6	20	theme	major	1178:1182	arg1	portion					1184:1190	its major portion	1174:1190	its major portion	1174:1190	However, in contrast to other misfolded proteins that are retained in the endoplasmic reticulum, only a fraction of misfolded TPP I mutant expressed in Chinese hamster ovary cells, but not in human embryonic kidney 293 cells, was arrested in the ER, whereas its major portion was secreted.
14702339	6	21	theme	misfolded	946:954	arg1	proteins					956:963	other misfolded proteins	940:963	other misfolded proteins that are retained in the endoplasmic reticulum	940:1010	However, in contrast to other misfolded proteins that are retained in the endoplasmic reticulum, only a fraction of misfolded TPP I mutant expressed in Chinese hamster ovary cells, but not in human embryonic kidney 293 cells, was arrested in the ER, whereas its major portion was secreted.
14702339	8	22	theme	Asn-286-linked	1369:1382	arg1	glycan					1384:1389	Asn-286-linked glycan	1369:1389	Asn-286-linked glycan	1369:1389	A small portion of TPP I missing Asn-286-linked glycan reached the lysosome and was processed to an active species; however, it showed low thermal and pH stability.
14702339	7	23	theme	non-native	1232:1241	arg1	bridges					1265:1271	non-native, interchain disulfide bridges	1232:1271	non-native, interchain disulfide bridges	1232:1271	Secreted proenzyme formed non-native, interchain disulfide bridges and displayed only residual TPP I activity upon acidification.
14702339	9	24	theme	enzyme	1606:1611	arg1	resistance					1621:1630	its resistance	1617:1630	its resistance to alkaline pH-induced inactivation	1617:1666	N-Glycans at Asn-210, Asn-222, Asn-313, and Asn-443 contributed slightly to the specific activity of the enzyme and its resistance to alkaline pH-induced inactivation.
14702339	9	24	theme	enzyme	1606:1611	arg1	activity					1590:1597	the specific activity	1577:1597	the specific activity of the enzyme	1577:1611	N-Glycans at Asn-210, Asn-222, Asn-313, and Asn-443 contributed slightly to the specific activity of the enzyme and its resistance to alkaline pH-induced inactivation.
14702339	5	25	theme	sites	848:852	arg1	one					835:837	one	835:837	one	835:837	Elimination of one of these sites, at Asn-286, dramatically affected the folding of the enzyme.
14702339	5	25	theme	sites	848:852	arg1	sites					848:852	these sites	842:852	these sites	842:852	Elimination of one of these sites, at Asn-286, dramatically affected the folding of the enzyme.
14702339	9	26	theme	alkaline	1635:1642	arg1	inactivation					1655:1666	alkaline pH-induced inactivation	1635:1666	alkaline pH-induced inactivation	1635:1666	N-Glycans at Asn-210, Asn-222, Asn-313, and Asn-443 contributed slightly to the specific activity of the enzyme and its resistance to alkaline pH-induced inactivation.
14702339	6	27	theme	human	1108:1112	arg1	kidney					1124:1129	human embryonic kidney 293	1108:1133	human embryonic kidney 293 cells	1108:1139	However, in contrast to other misfolded proteins that are retained in the endoplasmic reticulum, only a fraction of misfolded TPP I mutant expressed in Chinese hamster ovary cells, but not in human embryonic kidney 293 cells, was arrested in the ER, whereas its major portion was secreted.
14702339	0	28	theme	tripeptidyl-peptidase	76:96	arg1	TPP					126:128	TPP	126:128	TPP	126:128	N-glycosylation is crucial for folding, trafficking, and stability of human tripeptidyl-peptidase I. Tripeptidyl-peptidase I (TPP I) is a lysosomal serine-carboxyl peptidase that sequentially removes tripeptides from polypeptides.
14702339	0	28	theme	tripeptidyl-peptidase	76:96	arg1	I					123:123	human tripeptidyl-peptidase I. Tripeptidyl-peptidase I	70:123	human tripeptidyl-peptidase I. Tripeptidyl-peptidase I (TPP I)	70:131	N-glycosylation is crucial for folding, trafficking, and stability of human tripeptidyl-peptidase I. Tripeptidyl-peptidase I (TPP I) is a lysosomal serine-carboxyl peptidase that sequentially removes tripeptides from polypeptides.
14702339	2	29	contain	has	361:363	arg2	sites					396:400	five potential N-glycosylation sites	365:400	five potential N-glycosylation sites	365:400	Human TPP I has five potential N-glycosylation sites at Asn residues 210, 222, 286, 313, and 443.
14702339	2	29	contain	has	361:363	arg1	I					359:359	Human TPP I	349:359	Human TPP I	349:359	Human TPP I has five potential N-glycosylation sites at Asn residues 210, 222, 286, 313, and 443.
14702339	0	30	theme	Tripeptidyl-peptidase	101:121	arg1	TPP					126:128	TPP	126:128	TPP	126:128	N-glycosylation is crucial for folding, trafficking, and stability of human tripeptidyl-peptidase I. Tripeptidyl-peptidase I (TPP I) is a lysosomal serine-carboxyl peptidase that sequentially removes tripeptides from polypeptides.
14702339	0	30	theme	Tripeptidyl-peptidase	101:121	arg1	I					123:123	human tripeptidyl-peptidase I. Tripeptidyl-peptidase I	70:123	human tripeptidyl-peptidase I. Tripeptidyl-peptidase I (TPP I)	70:131	N-glycosylation is crucial for folding, trafficking, and stability of human tripeptidyl-peptidase I. Tripeptidyl-peptidase I (TPP I) is a lysosomal serine-carboxyl peptidase that sequentially removes tripeptides from polypeptides.
14702339	5	31	from	Asn-286	858:864	arg1	Elimination					820:830	Elimination	820:830	Elimination	820:830	Elimination of one of these sites, at Asn-286, dramatically affected the folding of the enzyme.
14702339	7	32	theme	Secreted	1206:1213	arg1	proenzyme					1215:1223	Secreted proenzyme	1206:1223	Secreted proenzyme	1206:1223	Secreted proenzyme formed non-native, interchain disulfide bridges and displayed only residual TPP I activity upon acidification.
14702339	11	33	theme	process	2024:2030	arg1	basis					2003:2007	the molecular basis	1989:2007	the molecular basis of the disease process in subjects with naturally occurring missense mutation at Asn-286	1989:2096	Thus, a dual role of oligosaccharide at Asn-286 in folding and lysosomal targeting could contribute to the unusual, but cell type-dependent, fate of misfolded TPP I conformer and represent the molecular basis of the disease process in subjects with naturally occurring missense mutation at Asn-286.
14702339	8	34	theme	active	1436:1441	arg1	species					1443:1449	an active species	1433:1449	an active species	1433:1449	A small portion of TPP I missing Asn-286-linked glycan reached the lysosome and was processed to an active species; however, it showed low thermal and pH stability.
14702339	11	35	theme	at	1837:1838	arg1	Asn-286					1840:1846	oligosaccharide at Asn-286	1821:1846	oligosaccharide at Asn-286	1821:1846	Thus, a dual role of oligosaccharide at Asn-286 in folding and lysosomal targeting could contribute to the unusual, but cell type-dependent, fate of misfolded TPP I conformer and represent the molecular basis of the disease process in subjects with naturally occurring missense mutation at Asn-286.
14702339	1	36	theme	classic	294:300	arg1	lipofuscinosis					333:346	the classic late infantile neuronal ceroid lipofuscinosis	290:346	the classic late infantile neuronal ceroid lipofuscinosis	290:346	Naturally occurring mutations in TPP I are associated with the classic late infantile neuronal ceroid lipofuscinosis.
14702339	8	37	link	Asn-286-linked	1369:1382	arg1	glycan					1384:1389	Asn-286-linked glycan	1369:1389	Asn-286-linked glycan	1369:1389	A small portion of TPP I missing Asn-286-linked glycan reached the lysosome and was processed to an active species; however, it showed low thermal and pH stability.
14702339	11	38	theme	missense	2069:2076	arg1	mutation					2078:2085	naturally occurring missense mutation	2049:2085	naturally occurring missense mutation at Asn-286	2049:2096	Thus, a dual role of oligosaccharide at Asn-286 in folding and lysosomal targeting could contribute to the unusual, but cell type-dependent, fate of misfolded TPP I conformer and represent the molecular basis of the disease process in subjects with naturally occurring missense mutation at Asn-286.
14702339	10	39	theme	TPP	1747:1749	arg1	Asn-286					1736:1742	Asn-286	1736:1742	Asn-286	1736:1742	Phospholabeling experiments revealed that N-glycans at Asn-210 and Asn-286 of TPP I preferentially accept a phosphomannose marker.
14702339	10	39	theme	TPP	1747:1749	arg1	Asn-210					1724:1730	Asn-210	1724:1730	Asn-210	1724:1730	Phospholabeling experiments revealed that N-glycans at Asn-210 and Asn-286 of TPP I preferentially accept a phosphomannose marker.
14702339	1	40	theme	infantile	307:315	arg1	lipofuscinosis					333:346	the classic late infantile neuronal ceroid lipofuscinosis	290:346	the classic late infantile neuronal ceroid lipofuscinosis	290:346	Naturally occurring mutations in TPP I are associated with the classic late infantile neuronal ceroid lipofuscinosis.
14702339	0	41	from	polypeptides	217:228	arg1	tripeptides					200:210	tripeptides	200:210	tripeptides from polypeptides	200:228	N-glycosylation is crucial for folding, trafficking, and stability of human tripeptidyl-peptidase I. Tripeptidyl-peptidase I (TPP I) is a lysosomal serine-carboxyl peptidase that sequentially removes tripeptides from polypeptides.
14702339	11	42	from	subjects	2035:2042	arg1	basis					2003:2007	the molecular basis	1989:2007	the molecular basis of the disease process in subjects with naturally occurring missense mutation at Asn-286	1989:2096	Thus, a dual role of oligosaccharide at Asn-286 in folding and lysosomal targeting could contribute to the unusual, but cell type-dependent, fate of misfolded TPP I conformer and represent the molecular basis of the disease process in subjects with naturally occurring missense mutation at Asn-286.
14702339	1	43	theme	ceroid	326:331	arg1	lipofuscinosis					333:346	the classic late infantile neuronal ceroid lipofuscinosis	290:346	the classic late infantile neuronal ceroid lipofuscinosis	290:346	Naturally occurring mutations in TPP I are associated with the classic late infantile neuronal ceroid lipofuscinosis.
14702339	6	44	theme	I	1046:1046	arg1	mutant					1048:1053	misfolded TPP I mutant	1032:1053	misfolded TPP I mutant expressed in Chinese hamster ovary cells	1032:1094	However, in contrast to other misfolded proteins that are retained in the endoplasmic reticulum, only a fraction of misfolded TPP I mutant expressed in Chinese hamster ovary cells, but not in human embryonic kidney 293 cells, was arrested in the ER, whereas its major portion was secreted.
14702339	11	45	from	Asn-286	2090:2096	arg1	mutation					2078:2085	naturally occurring missense mutation	2049:2085	naturally occurring missense mutation at Asn-286	2049:2096	Thus, a dual role of oligosaccharide at Asn-286 in folding and lysosomal targeting could contribute to the unusual, but cell type-dependent, fate of misfolded TPP I conformer and represent the molecular basis of the disease process in subjects with naturally occurring missense mutation at Asn-286.
14702339	2	46	theme	Human	349:353	arg1	I					359:359	Human TPP I	349:359	Human TPP I	349:359	Human TPP I has five potential N-glycosylation sites at Asn residues 210, 222, 286, 313, and 443.
14702339	6	47	theme	misfolded	1032:1040	arg1	mutant					1048:1053	misfolded TPP I mutant	1032:1053	misfolded TPP I mutant expressed in Chinese hamster ovary cells	1032:1094	However, in contrast to other misfolded proteins that are retained in the endoplasmic reticulum, only a fraction of misfolded TPP I mutant expressed in Chinese hamster ovary cells, but not in human embryonic kidney 293 cells, was arrested in the ER, whereas its major portion was secreted.
14702339	11	48	theme	dual	1808:1811	arg1	role					1813:1816	a dual role	1806:1816	a dual role of oligosaccharide at Asn-286 in folding and lysosomal targeting	1806:1881	Thus, a dual role of oligosaccharide at Asn-286 in folding and lysosomal targeting could contribute to the unusual, but cell type-dependent, fate of misfolded TPP I conformer and represent the molecular basis of the disease process in subjects with naturally occurring missense mutation at Asn-286.
14702339	4	49	theme	human	759:763	arg1	I					769:769	human TPP I	759:769	human TPP I	759:769	Here, we demonstrate that human TPP I in vivo utilizes all five N-glycosylation sites.
14702339	2	50	theme	N-glycosylation	380:394	arg1	sites					396:400	five potential N-glycosylation sites	365:400	five potential N-glycosylation sites	365:400	Human TPP I has five potential N-glycosylation sites at Asn residues 210, 222, 286, 313, and 443.
14702339	10	51	from	Asn-286	1736:1742	arg1	N-glycans					1711:1719	N-glycans	1711:1719	N-glycans at Asn-210 and Asn-286 of TPP I	1711:1751	Phospholabeling experiments revealed that N-glycans at Asn-210 and Asn-286 of TPP I preferentially accept a phosphomannose marker.
14702339	8	52	theme	pH	1487:1488	arg1	stability					1490:1498	low thermal and pH stability	1471:1498	stability	1490:1498	A small portion of TPP I missing Asn-286-linked glycan reached the lysosome and was processed to an active species; however, it showed low thermal and pH stability.
14702339	6	53	from	fraction	1020:1027	arg1	cells					1135:1139	human embryonic kidney 293 cells	1108:1139	human embryonic kidney 293 cells	1108:1139	However, in contrast to other misfolded proteins that are retained in the endoplasmic reticulum, only a fraction of misfolded TPP I mutant expressed in Chinese hamster ovary cells, but not in human embryonic kidney 293 cells, was arrested in the ER, whereas its major portion was secreted.
14702339	3	54	theme	N-glycosylation	470:484	arg1	role					462:465	the role	458:465	the role of N-glycosylation in the function of the enzyme	458:514	To analyze the role of N-glycosylation in the function of the enzyme, we obliterated each N- glycosylation consensus sequence by substituting Gln for Asn, either individually or in combinations, and expressed mutated cDNAs in Chinese hamster ovary and human embryonic kidney 293 cells.
14702339	11	55	theme	molecular	1993:2001	arg1	basis					2003:2007	the molecular basis	1989:2007	the molecular basis of the disease process in subjects with naturally occurring missense mutation at Asn-286	1989:2096	Thus, a dual role of oligosaccharide at Asn-286 in folding and lysosomal targeting could contribute to the unusual, but cell type-dependent, fate of misfolded TPP I conformer and represent the molecular basis of the disease process in subjects with naturally occurring missense mutation at Asn-286.
14702339	3	56	theme	mutated	656:662	arg1	cDNAs					664:668	mutated cDNAs	656:668	mutated cDNAs	656:668	To analyze the role of N-glycosylation in the function of the enzyme, we obliterated each N- glycosylation consensus sequence by substituting Gln for Asn, either individually or in combinations, and expressed mutated cDNAs in Chinese hamster ovary and human embryonic kidney 293 cells.
14702339	3	57	theme	enzyme	509:514	arg1	function					493:500	the function	489:500	the function of the enzyme	489:514	To analyze the role of N-glycosylation in the function of the enzyme, we obliterated each N- glycosylation consensus sequence by substituting Gln for Asn, either individually or in combinations, and expressed mutated cDNAs in Chinese hamster ovary and human embryonic kidney 293 cells.
14702339	11	58	theme	disease	2016:2022	arg1	process					2024:2030	the disease process	2012:2030	the disease process in subjects with naturally occurring missense mutation at Asn-286	2012:2096	Thus, a dual role of oligosaccharide at Asn-286 in folding and lysosomal targeting could contribute to the unusual, but cell type-dependent, fate of misfolded TPP I conformer and represent the molecular basis of the disease process in subjects with naturally occurring missense mutation at Asn-286.
14702339	6	59	theme	ovary	1084:1088	arg1	cells					1090:1094	Chinese hamster ovary cells	1068:1094	Chinese hamster ovary cells	1068:1094	However, in contrast to other misfolded proteins that are retained in the endoplasmic reticulum, only a fraction of misfolded TPP I mutant expressed in Chinese hamster ovary cells, but not in human embryonic kidney 293 cells, was arrested in the ER, whereas its major portion was secreted.
14702339	3	60	theme	hamster	681:687	arg1	ovary					689:693	Chinese hamster ovary	673:693	Chinese hamster ovary	673:693	To analyze the role of N-glycosylation in the function of the enzyme, we obliterated each N- glycosylation consensus sequence by substituting Gln for Asn, either individually or in combinations, and expressed mutated cDNAs in Chinese hamster ovary and human embryonic kidney 293 cells.
14702339	11	61	from	basis	2003:2007	arg1	subjects					2035:2042	subjects	2035:2042	subjects with naturally occurring missense mutation at Asn-286	2035:2096	Thus, a dual role of oligosaccharide at Asn-286 in folding and lysosomal targeting could contribute to the unusual, but cell type-dependent, fate of misfolded TPP I conformer and represent the molecular basis of the disease process in subjects with naturally occurring missense mutation at Asn-286.
14702339	9	62	from	Asn-443	1545:1551	arg1	N-Glycans					1501:1509	N-Glycans	1501:1509	N-Glycans at Asn-210, Asn-222, Asn-313, and Asn-443	1501:1551	N-Glycans at Asn-210, Asn-222, Asn-313, and Asn-443 contributed slightly to the specific activity of the enzyme and its resistance to alkaline pH-induced inactivation.
14702339	6	63	theme	Chinese	1068:1074	arg1	cells					1090:1094	Chinese hamster ovary cells	1068:1094	Chinese hamster ovary cells	1068:1094	However, in contrast to other misfolded proteins that are retained in the endoplasmic reticulum, only a fraction of misfolded TPP I mutant expressed in Chinese hamster ovary cells, but not in human embryonic kidney 293 cells, was arrested in the ER, whereas its major portion was secreted.
14702339	11	64	theme	unusual	1907:1913	arg1	fate					1941:1944	the unusual, but cell type-dependent, fate	1903:1944	the unusual, but cell type-dependent, fate of misfolded TPP I conformer	1903:1973	Thus, a dual role of oligosaccharide at Asn-286 in folding and lysosomal targeting could contribute to the unusual, but cell type-dependent, fate of misfolded TPP I conformer and represent the molecular basis of the disease process in subjects with naturally occurring missense mutation at Asn-286.
14702339	7	65	dep	non-native	1232:1241	arg1	interchain					1244:1253	interchain	1244:1253	interchain	1244:1253	Secreted proenzyme formed non-native, interchain disulfide bridges and displayed only residual TPP I activity upon acidification.
14702339	7	66	theme	TPP	1301:1303	arg1	activity					1307:1314	only residual TPP I activity	1287:1314	only residual TPP I activity	1287:1314	Secreted proenzyme formed non-native, interchain disulfide bridges and displayed only residual TPP I activity upon acidification.
14702339	11	67	from	Asn-286	1840:1846	arg1	oligosaccharide					1821:1835	oligosaccharide at Asn-286	1821:1846	oligosaccharide at Asn-286	1821:1846	Thus, a dual role of oligosaccharide at Asn-286 in folding and lysosomal targeting could contribute to the unusual, but cell type-dependent, fate of misfolded TPP I conformer and represent the molecular basis of the disease process in subjects with naturally occurring missense mutation at Asn-286.
14702339	11	67	from	Asn-286	1840:1846	arg1	at					1837:1838	oligosaccharide at Asn-286	1821:1846	oligosaccharide at Asn-286	1821:1846	Thus, a dual role of oligosaccharide at Asn-286 in folding and lysosomal targeting could contribute to the unusual, but cell type-dependent, fate of misfolded TPP I conformer and represent the molecular basis of the disease process in subjects with naturally occurring missense mutation at Asn-286.
14702339	3	68	theme	embryonic	705:713	arg1	kidney					715:720	human embryonic kidney 293	699:724	human embryonic kidney 293 cells	699:730	To analyze the role of N-glycosylation in the function of the enzyme, we obliterated each N- glycosylation consensus sequence by substituting Gln for Asn, either individually or in combinations, and expressed mutated cDNAs in Chinese hamster ovary and human embryonic kidney 293 cells.
14702339	11	69	theme	Asn-286	1840:1846	arg1	role					1813:1816	a dual role	1806:1816	a dual role of oligosaccharide at Asn-286 in folding and lysosomal targeting	1806:1881	Thus, a dual role of oligosaccharide at Asn-286 in folding and lysosomal targeting could contribute to the unusual, but cell type-dependent, fate of misfolded TPP I conformer and represent the molecular basis of the disease process in subjects with naturally occurring missense mutation at Asn-286.
14702339	9	70	theme	specific	1581:1588	arg1	activity					1590:1597	the specific activity	1577:1597	the specific activity of the enzyme	1577:1611	N-Glycans at Asn-210, Asn-222, Asn-313, and Asn-443 contributed slightly to the specific activity of the enzyme and its resistance to alkaline pH-induced inactivation.
14702339	8	71	theme	TPP	1355:1357	arg1	portion					1344:1350	A small portion	1336:1350	A small portion of TPP I missing Asn-286-linked glycan	1336:1389	A small portion of TPP I missing Asn-286-linked glycan reached the lysosome and was processed to an active species; however, it showed low thermal and pH stability.
14702339	1	72	from	mutations	251:259	arg1	TPP					264:266	TPP I	264:268	TPP I	264:268	Naturally occurring mutations in TPP I are associated with the classic late infantile neuronal ceroid lipofuscinosis.
14702339	3	73	theme	glycosylation	540:552	arg1	sequence					564:571	each N- glycosylation consensus sequence	532:571	each N- glycosylation consensus sequence	532:571	To analyze the role of N-glycosylation in the function of the enzyme, we obliterated each N- glycosylation consensus sequence by substituting Gln for Asn, either individually or in combinations, and expressed mutated cDNAs in Chinese hamster ovary and human embryonic kidney 293 cells.
14702339	11	74	theme	conformer	1965:1973	arg1	fate					1941:1944	the unusual, but cell type-dependent, fate	1903:1944	the unusual, but cell type-dependent, fate of misfolded TPP I conformer	1903:1973	Thus, a dual role of oligosaccharide at Asn-286 in folding and lysosomal targeting could contribute to the unusual, but cell type-dependent, fate of misfolded TPP I conformer and represent the molecular basis of the disease process in subjects with naturally occurring missense mutation at Asn-286.
14702339	6	75	theme	kidney	1124:1129	arg1	cells					1135:1139	human embryonic kidney 293 cells	1108:1139	human embryonic kidney 293 cells	1108:1139	However, in contrast to other misfolded proteins that are retained in the endoplasmic reticulum, only a fraction of misfolded TPP I mutant expressed in Chinese hamster ovary cells, but not in human embryonic kidney 293 cells, was arrested in the ER, whereas its major portion was secreted.
14702339	11	76	from	role	1813:1816	arg1	folding					1851:1857	folding	1851:1857	folding	1851:1857	Thus, a dual role of oligosaccharide at Asn-286 in folding and lysosomal targeting could contribute to the unusual, but cell type-dependent, fate of misfolded TPP I conformer and represent the molecular basis of the disease process in subjects with naturally occurring missense mutation at Asn-286.
14702339	11	76	from	role	1813:1816	arg1	targeting					1873:1881	lysosomal targeting	1863:1881	lysosomal targeting	1863:1881	Thus, a dual role of oligosaccharide at Asn-286 in folding and lysosomal targeting could contribute to the unusual, but cell type-dependent, fate of misfolded TPP I conformer and represent the molecular basis of the disease process in subjects with naturally occurring missense mutation at Asn-286.
14702339	0	77	theme	serine-carboxyl	148:162	arg1	peptidase					164:172	a lysosomal serine-carboxyl peptidase	136:172	a lysosomal serine-carboxyl peptidase that sequentially removes tripeptides from polypeptides	136:228	N-glycosylation is crucial for folding, trafficking, and stability of human tripeptidyl-peptidase I. Tripeptidyl-peptidase I (TPP I) is a lysosomal serine-carboxyl peptidase that sequentially removes tripeptides from polypeptides.
14702339	11	78	theme	lysosomal	1863:1871	arg1	targeting					1873:1881	lysosomal targeting	1863:1881	lysosomal targeting	1863:1881	Thus, a dual role of oligosaccharide at Asn-286 in folding and lysosomal targeting could contribute to the unusual, but cell type-dependent, fate of misfolded TPP I conformer and represent the molecular basis of the disease process in subjects with naturally occurring missense mutation at Asn-286.
14702339	11	79	with	subjects	2035:2042	arg1	mutation					2078:2085	naturally occurring missense mutation	2049:2085	naturally occurring missense mutation at Asn-286	2049:2096	Thus, a dual role of oligosaccharide at Asn-286 in folding and lysosomal targeting could contribute to the unusual, but cell type-dependent, fate of misfolded TPP I conformer and represent the molecular basis of the disease process in subjects with naturally occurring missense mutation at Asn-286.
14702339	11	80	theme	TPP	1959:1961	arg1	conformer					1965:1973	misfolded TPP I conformer	1949:1973	misfolded TPP I conformer	1949:1973	Thus, a dual role of oligosaccharide at Asn-286 in folding and lysosomal targeting could contribute to the unusual, but cell type-dependent, fate of misfolded TPP I conformer and represent the molecular basis of the disease process in subjects with naturally occurring missense mutation at Asn-286.
14702339	7	81	theme	disulfide	1255:1263	arg1	bridges					1265:1271	non-native, interchain disulfide bridges	1232:1271	non-native, interchain disulfide bridges	1232:1271	Secreted proenzyme formed non-native, interchain disulfide bridges and displayed only residual TPP I activity upon acidification.
14702339	5	82	theme	one	835:837	arg1	Elimination					820:830	Elimination	820:830	Elimination	820:830	Elimination of one of these sites, at Asn-286, dramatically affected the folding of the enzyme.
14702339	6	83	theme	other	940:944	arg1	proteins					956:963	other misfolded proteins	940:963	other misfolded proteins that are retained in the endoplasmic reticulum	940:1010	However, in contrast to other misfolded proteins that are retained in the endoplasmic reticulum, only a fraction of misfolded TPP I mutant expressed in Chinese hamster ovary cells, but not in human embryonic kidney 293 cells, was arrested in the ER, whereas its major portion was secreted.
14702339	0	84	theme	human	70:74	arg1	TPP					126:128	TPP	126:128	TPP	126:128	N-glycosylation is crucial for folding, trafficking, and stability of human tripeptidyl-peptidase I. Tripeptidyl-peptidase I (TPP I) is a lysosomal serine-carboxyl peptidase that sequentially removes tripeptides from polypeptides.
14702339	0	84	theme	human	70:74	arg1	I					123:123	human tripeptidyl-peptidase I. Tripeptidyl-peptidase I	70:123	human tripeptidyl-peptidase I. Tripeptidyl-peptidase I (TPP I)	70:131	N-glycosylation is crucial for folding, trafficking, and stability of human tripeptidyl-peptidase I. Tripeptidyl-peptidase I (TPP I) is a lysosomal serine-carboxyl peptidase that sequentially removes tripeptides from polypeptides.
14702339	0	85	theme	I.	98:99	arg1	TPP					126:128	TPP	126:128	TPP	126:128	N-glycosylation is crucial for folding, trafficking, and stability of human tripeptidyl-peptidase I. Tripeptidyl-peptidase I (TPP I) is a lysosomal serine-carboxyl peptidase that sequentially removes tripeptides from polypeptides.
14702339	0	85	theme	I.	98:99	arg1	I					123:123	human tripeptidyl-peptidase I. Tripeptidyl-peptidase I	70:123	human tripeptidyl-peptidase I. Tripeptidyl-peptidase I (TPP I)	70:131	N-glycosylation is crucial for folding, trafficking, and stability of human tripeptidyl-peptidase I. Tripeptidyl-peptidase I (TPP I) is a lysosomal serine-carboxyl peptidase that sequentially removes tripeptides from polypeptides.
14702339	0	86	theme	lysosomal	138:146	arg1	peptidase					164:172	a lysosomal serine-carboxyl peptidase	136:172	a lysosomal serine-carboxyl peptidase that sequentially removes tripeptides from polypeptides	136:228	N-glycosylation is crucial for folding, trafficking, and stability of human tripeptidyl-peptidase I. Tripeptidyl-peptidase I (TPP I) is a lysosomal serine-carboxyl peptidase that sequentially removes tripeptides from polypeptides.
14702339	9	87	theme	pH-induced	1644:1653	arg1	inactivation					1655:1666	alkaline pH-induced inactivation	1635:1666	alkaline pH-induced inactivation	1635:1666	N-Glycans at Asn-210, Asn-222, Asn-313, and Asn-443 contributed slightly to the specific activity of the enzyme and its resistance to alkaline pH-induced inactivation.
14702339	0	88	theme	I	123:123	arg1	trafficking					40:50	trafficking	40:50	trafficking	40:50	N-glycosylation is crucial for folding, trafficking, and stability of human tripeptidyl-peptidase I. Tripeptidyl-peptidase I (TPP I) is a lysosomal serine-carboxyl peptidase that sequentially removes tripeptides from polypeptides.
14702339	0	88	theme	I	123:123	arg1	stability					57:65	stability	57:65	stability	57:65	N-glycosylation is crucial for folding, trafficking, and stability of human tripeptidyl-peptidase I. Tripeptidyl-peptidase I (TPP I) is a lysosomal serine-carboxyl peptidase that sequentially removes tripeptides from polypeptides.
14702339	0	88	theme	I	123:123	arg1	folding					31:37	folding	31:37	folding	31:37	N-glycosylation is crucial for folding, trafficking, and stability of human tripeptidyl-peptidase I. Tripeptidyl-peptidase I (TPP I) is a lysosomal serine-carboxyl peptidase that sequentially removes tripeptides from polypeptides.
14702339	5	89	theme	enzyme	908:913	arg1	folding					893:899	the folding	889:899	the folding of the enzyme	889:913	Elimination of one of these sites, at Asn-286, dramatically affected the folding of the enzyme.
14702339	9	90	from	Asn-210	1514:1520	arg1	N-Glycans					1501:1509	N-Glycans	1501:1509	N-Glycans at Asn-210, Asn-222, Asn-313, and Asn-443	1501:1551	N-Glycans at Asn-210, Asn-222, Asn-313, and Asn-443 contributed slightly to the specific activity of the enzyme and its resistance to alkaline pH-induced inactivation.
14702339	3	91	gly	N-glycosylation	470:484	arg1	enzyme					509:514	the enzyme	505:514	the enzyme	505:514	To analyze the role of N-glycosylation in the function of the enzyme, we obliterated each N- glycosylation consensus sequence by substituting Gln for Asn, either individually or in combinations, and expressed mutated cDNAs in Chinese hamster ovary and human embryonic kidney 293 cells.
14702339	2	92	theme	Asn	405:407	arg1	residues					409:416	Asn residues 210, 222, 286, 313, and 443	405:444	Asn residues 210, 222, 286, 313, and 443	405:444	Human TPP I has five potential N-glycosylation sites at Asn residues 210, 222, 286, 313, and 443.
14702339	6	93	theme	endoplasmic	990:1000	arg1	reticulum					1002:1010	the endoplasmic reticulum	986:1010	the endoplasmic reticulum	986:1010	However, in contrast to other misfolded proteins that are retained in the endoplasmic reticulum, only a fraction of misfolded TPP I mutant expressed in Chinese hamster ovary cells, but not in human embryonic kidney 293 cells, was arrested in the ER, whereas its major portion was secreted.
14702339	2	94	gly	N-glycosylation	380:394	arg2	sites					396:400	five potential N-glycosylation sites	365:400	five potential N-glycosylation sites	365:400	Human TPP I has five potential N-glycosylation sites at Asn residues 210, 222, 286, 313, and 443.
14702339	2	94	gly	N-glycosylation	380:394	arg2	five					365:368	five	365:368	five	365:368	Human TPP I has five potential N-glycosylation sites at Asn residues 210, 222, 286, 313, and 443.
14702339	1	95	theme	late	302:305	arg1	lipofuscinosis					333:346	the classic late infantile neuronal ceroid lipofuscinosis	290:346	the classic late infantile neuronal ceroid lipofuscinosis	290:346	Naturally occurring mutations in TPP I are associated with the classic late infantile neuronal ceroid lipofuscinosis.
14702339	10	96	from	Asn-210	1724:1730	arg1	N-glycans					1711:1719	N-glycans	1711:1719	N-glycans at Asn-210 and Asn-286 of TPP I	1711:1751	Phospholabeling experiments revealed that N-glycans at Asn-210 and Asn-286 of TPP I preferentially accept a phosphomannose marker.
14702339	4	97	theme	TPP	765:767	arg1	I					769:769	human TPP I	759:769	human TPP I	759:769	Here, we demonstrate that human TPP I in vivo utilizes all five N-glycosylation sites.
14702339	1	98	theme	occurring	241:249	arg1	mutations					251:259	Naturally occurring mutations	231:259	Naturally occurring mutations in TPP I	231:268	Naturally occurring mutations in TPP I are associated with the classic late infantile neuronal ceroid lipofuscinosis.
14702339	1	99	theme	neuronal	317:324	arg1	lipofuscinosis					333:346	the classic late infantile neuronal ceroid lipofuscinosis	290:346	the classic late infantile neuronal ceroid lipofuscinosis	290:346	Naturally occurring mutations in TPP I are associated with the classic late infantile neuronal ceroid lipofuscinosis.
14702339	6	100	theme	mutant	1048:1053	arg1	fraction					1020:1027	only a fraction	1013:1027	only a fraction of misfolded TPP I mutant expressed in Chinese hamster ovary cells, but not in human embryonic kidney 293 cells,	1013:1140	However, in contrast to other misfolded proteins that are retained in the endoplasmic reticulum, only a fraction of misfolded TPP I mutant expressed in Chinese hamster ovary cells, but not in human embryonic kidney 293 cells, was arrested in the ER, whereas its major portion was secreted.
14702339	11	101	theme	occurring	2059:2067	arg1	mutation					2078:2085	naturally occurring missense mutation	2049:2085	naturally occurring missense mutation at Asn-286	2049:2096	Thus, a dual role of oligosaccharide at Asn-286 in folding and lysosomal targeting could contribute to the unusual, but cell type-dependent, fate of misfolded TPP I conformer and represent the molecular basis of the disease process in subjects with naturally occurring missense mutation at Asn-286.
14702339	10	102	theme	phosphomannose	1777:1790	arg1	marker					1792:1797	a phosphomannose marker	1775:1797	a phosphomannose marker	1775:1797	Phospholabeling experiments revealed that N-glycans at Asn-210 and Asn-286 of TPP I preferentially accept a phosphomannose marker.
14702339	2	103	theme	TPP	355:357	arg1	I					359:359	Human TPP I	349:359	Human TPP I	349:359	Human TPP I has five potential N-glycosylation sites at Asn residues 210, 222, 286, 313, and 443.
14702339	6	104	theme	TPP	1042:1044	arg1	mutant					1048:1053	misfolded TPP I mutant	1032:1053	misfolded TPP I mutant expressed in Chinese hamster ovary cells	1032:1094	However, in contrast to other misfolded proteins that are retained in the endoplasmic reticulum, only a fraction of misfolded TPP I mutant expressed in Chinese hamster ovary cells, but not in human embryonic kidney 293 cells, was arrested in the ER, whereas its major portion was secreted.
14702339	3	105	dep	either	602:607	arg1	individually					609:620	individually	609:620	individually	609:620	To analyze the role of N-glycosylation in the function of the enzyme, we obliterated each N- glycosylation consensus sequence by substituting Gln for Asn, either individually or in combinations, and expressed mutated cDNAs in Chinese hamster ovary and human embryonic kidney 293 cells.
14702339	4	106	gly	N-glycosylation	797:811	arg2	sites					813:817	all five N-glycosylation sites	788:817	all five N-glycosylation sites	788:817	Here, we demonstrate that human TPP I in vivo utilizes all five N-glycosylation sites.
14702339	4	106	gly	N-glycosylation	797:811	arg2	five					792:795	five	792:795	five	792:795	Here, we demonstrate that human TPP I in vivo utilizes all five N-glycosylation sites.
14702339	2	107	theme	potential	370:378	arg1	sites					396:400	five potential N-glycosylation sites	365:400	five potential N-glycosylation sites	365:400	Human TPP I has five potential N-glycosylation sites at Asn residues 210, 222, 286, 313, and 443.
24706782	4	0	theme	most	579:582	arg1	proteins					598:605	the most complex human proteins	575:605	the most complex human proteins	575:605	However, whether they are able to express proteins like IgM antibodies, which range among the most complex human proteins, remains unknown so far.
24706782	11	1	theme	in	1501:1502	arg1	generation					1511:1520	The in planta generation	1497:1520	The in planta generation of one of the most complex human proteins	1497:1562	The in planta generation of one of the most complex human proteins opens new pathways toward the production of difficult-to-express proteins for pharmaceutical applications.
24706782	9	2	theme	IgM	1228:1230	arg1	model					1208:1212	A glycosylated model	1193:1212	A glycosylated model of pentameric IgM	1193:1230	A glycosylated model of pentameric IgM exhibits different accessibility of the glycosylation sites, explaining site-specific glycosylation.
24706782	7	3	theme	glycosylation	863:875	arg1	analysis					877:884	Detailed glycosylation analysis	854:884	Detailed glycosylation analysis	854:884	Detailed glycosylation analysis exhibited complex and oligomannosidic N-glycans in a site-specific manner on human-serum IgM and on plant- and human-cell-line-produced SM6.
24706782	4	4	theme	human	592:596	arg1	proteins					598:605	the most complex human proteins	575:605	the most complex human proteins	575:605	However, whether they are able to express proteins like IgM antibodies, which range among the most complex human proteins, remains unknown so far.
24706782	5	5	theme	in	651:652	arg1	generation					661:670	the in planta generation	647:670	the in planta generation of the functionally active monoclonal antitumor IgM PAT-SM6 (SM6)	647:736	Here we report the in planta generation of the functionally active monoclonal antitumor IgM PAT-SM6 (SM6).
24706782	9	6	theme	different	1241:1249	arg1	accessibility					1251:1263	different accessibility	1241:1263	different accessibility of the glycosylation sites	1241:1290	A glycosylated model of pentameric IgM exhibits different accessibility of the glycosylation sites, explaining site-specific glycosylation.
24706782	12	7	theme	sugar	1799:1803	arg1	moieties					1805:1812	sugar moieties	1799:1812	sugar moieties	1799:1812	Moreover, the generation of IgMs with a controlled glycosylation pattern allows the study of the so far unknown contribution of sugar moieties to the function of IgMs.
24706782	6	8	dep	accumulates	755:765	arg1	leaves					776:781	leaves	776:781	leaves	776:781	SM6 efficiently accumulates in plant leaves and assembles correctly into heterooligomers (pentamers and hexamers).
24706782	11	9	theme	one	1525:1527	arg1	generation					1511:1520	The in planta generation	1497:1520	The in planta generation of one of the most complex human proteins	1497:1562	The in planta generation of one of the most complex human proteins opens new pathways toward the production of difficult-to-express proteins for pharmaceutical applications.
24706782	2	10	theme	cell	277:280	arg1	culture					282:288	mammalian cell culture	267:288	mammalian cell culture	267:288	Although the expression of IgM antibodies in mammalian cell culture is established, this approach remains costly and alternative methods have not been developed yet.
24706782	9	11	theme	glycosylation	1272:1284	arg1	sites					1286:1290	the glycosylation sites	1268:1290	the glycosylation sites	1268:1290	A glycosylated model of pentameric IgM exhibits different accessibility of the glycosylation sites, explaining site-specific glycosylation.
24706782	5	12	theme	active	692:697	arg1	SM6					733:735	SM6	733:735	SM6	733:735	Here we report the in planta generation of the functionally active monoclonal antitumor IgM PAT-SM6 (SM6).
24706782	5	12	theme	active	692:697	arg1	PAT-SM6					724:730	monoclonal antitumor IgM PAT-SM6	699:730	the functionally active monoclonal antitumor IgM PAT-SM6 (SM6)	675:736	Here we report the in planta generation of the functionally active monoclonal antitumor IgM PAT-SM6 (SM6).
24706782	5	13	theme	antitumor	710:718	arg1	SM6					733:735	SM6	733:735	SM6	733:735	Here we report the in planta generation of the functionally active monoclonal antitumor IgM PAT-SM6 (SM6).
24706782	5	13	theme	antitumor	710:718	arg1	PAT-SM6					724:730	monoclonal antitumor IgM PAT-SM6	699:730	the functionally active monoclonal antitumor IgM PAT-SM6 (SM6)	675:736	Here we report the in planta generation of the functionally active monoclonal antitumor IgM PAT-SM6 (SM6).
24706782	9	14	theme	site-specific	1304:1316	arg1	glycosylation					1318:1330	site-specific glycosylation	1304:1330	site-specific glycosylation	1304:1330	A glycosylated model of pentameric IgM exhibits different accessibility of the glycosylation sites, explaining site-specific glycosylation.
24706782	12	15	theme	glycosylation	1722:1734	arg1	pattern					1736:1742	a controlled glycosylation pattern	1709:1742	a controlled glycosylation pattern	1709:1742	Moreover, the generation of IgMs with a controlled glycosylation pattern allows the study of the so far unknown contribution of sugar moieties to the function of IgMs.
24706782	11	16	theme	difficult-to-express	1608:1627	arg1	proteins					1629:1636	difficult-to-express proteins	1608:1636	difficult-to-express proteins for pharmaceutical applications	1608:1668	The in planta generation of one of the most complex human proteins opens new pathways toward the production of difficult-to-express proteins for pharmaceutical applications.
24706782	7	17	theme	human-cell-line-produced	997:1020	arg1	SM6					1022:1024	plant- and human-cell-line-produced SM6	986:1024	plant- and human-cell-line-produced SM6	986:1024	Detailed glycosylation analysis exhibited complex and oligomannosidic N-glycans in a site-specific manner on human-serum IgM and on plant- and human-cell-line-produced SM6.
24706782	2	18	theme	IgM	249:251	arg1	antibodies					253:262	IgM antibodies	249:262	IgM antibodies	249:262	Although the expression of IgM antibodies in mammalian cell culture is established, this approach remains costly and alternative methods have not been developed yet.
24706782	7	19	theme	plant-	986:991	arg1	SM6					1022:1024	plant- and human-cell-line-produced SM6	986:1024	plant- and human-cell-line-produced SM6	986:1024	Detailed glycosylation analysis exhibited complex and oligomannosidic N-glycans in a site-specific manner on human-serum IgM and on plant- and human-cell-line-produced SM6.
24706782	1	20	theme	innate	141:146	arg1	mechanisms					156:165	the human's innate defense mechanisms	129:165	the human's innate defense mechanisms	129:165	IgM antibodies are an important player of the human's innate defense mechanisms and increasingly have gained interest as therapeutics.
24706782	12	21	theme	IgMs	1699:1702	arg1	generation					1685:1694	the generation	1681:1694	the generation of IgMs with a controlled glycosylation pattern	1681:1742	Moreover, the generation of IgMs with a controlled glycosylation pattern allows the study of the so far unknown contribution of sugar moieties to the function of IgMs.
24706782	0	22	from	glycoengineering	15:30	arg1	plants					79:84	plants	79:84	plants	79:84	Expression and glycoengineering of functionally active heteromultimeric IgM in plants.
24706782	1	23	theme	mechanisms	156:165	arg1	player					119:124	an important player	106:124	an important player of the human's innate defense mechanisms	106:165	IgM antibodies are an important player of the human's innate defense mechanisms and increasingly have gained interest as therapeutics.
24706782	1	23	theme	mechanisms	156:165	arg1	antibodies					91:100	IgM antibodies	87:100	IgM antibodies	87:100	IgM antibodies are an important player of the human's innate defense mechanisms and increasingly have gained interest as therapeutics.
24706782	0	24	from	Expression	0:9	arg1	plants					79:84	plants	79:84	plants	79:84	Expression and glycoengineering of functionally active heteromultimeric IgM in plants.
24706782	5	25	theme	PAT-SM6	724:730	arg1	generation					661:670	the in planta generation	647:670	the in planta generation of the functionally active monoclonal antitumor IgM PAT-SM6 (SM6)	647:736	Here we report the in planta generation of the functionally active monoclonal antitumor IgM PAT-SM6 (SM6).
24706782	7	26	theme	human-serum	963:973	arg1	IgM					975:977	human-serum IgM	963:977	human-serum IgM	963:977	Detailed glycosylation analysis exhibited complex and oligomannosidic N-glycans in a site-specific manner on human-serum IgM and on plant- and human-cell-line-produced SM6.
24706782	10	27	gly	glycoforms	1431:1440	arg1	SM6					1427:1429	plant-derived SM6 glycoforms	1413:1440	plant-derived SM6 glycoforms	1413:1440	Biochemical and biophysical properties and importantly biological activities of plant-derived SM6 glycoforms are comparable to the human-cell-derived counterparts.
24706782	11	28	theme	proteins	1555:1562	arg1	one					1525:1527	one	1525:1527	one	1525:1527	The in planta generation of one of the most complex human proteins opens new pathways toward the production of difficult-to-express proteins for pharmaceutical applications.
24706782	11	28	theme	proteins	1555:1562	arg1	proteins					1555:1562	the most complex human proteins	1532:1562	the most complex human proteins	1532:1562	The in planta generation of one of the most complex human proteins opens new pathways toward the production of difficult-to-express proteins for pharmaceutical applications.
24706782	1	29	theme	IgM	87:89	arg1	player					119:124	an important player	106:124	an important player of the human's innate defense mechanisms	106:165	IgM antibodies are an important player of the human's innate defense mechanisms and increasingly have gained interest as therapeutics.
24706782	1	29	theme	IgM	87:89	arg1	antibodies					91:100	IgM antibodies	87:100	IgM antibodies	87:100	IgM antibodies are an important player of the human's innate defense mechanisms and increasingly have gained interest as therapeutics.
24706782	12	30	theme	moieties	1805:1812	arg1	contribution					1783:1794	the so far unknown contribution	1764:1794	the so far unknown contribution of sugar moieties to the function of IgMs	1764:1836	Moreover, the generation of IgMs with a controlled glycosylation pattern allows the study of the so far unknown contribution of sugar moieties to the function of IgMs.
24706782	11	31	theme	complex	1541:1547	arg1	proteins					1555:1562	the most complex human proteins	1532:1562	the most complex human proteins	1532:1562	The in planta generation of one of the most complex human proteins opens new pathways toward the production of difficult-to-express proteins for pharmaceutical applications.
24706782	6	32	dep	heterooligomers	812:826	arg1	pentamers					829:837	pentamers	829:837	pentamers	829:837	SM6 efficiently accumulates in plant leaves and assembles correctly into heterooligomers (pentamers and hexamers).
24706782	6	32	dep	heterooligomers	812:826	arg1	hexamers					843:850	hexamers	843:850	hexamers	843:850	SM6 efficiently accumulates in plant leaves and assembles correctly into heterooligomers (pentamers and hexamers).
24706782	10	33	theme	plant-derived	1413:1425	arg1	glycoforms					1431:1440	plant-derived SM6 glycoforms	1413:1440	plant-derived SM6 glycoforms	1413:1440	Biochemical and biophysical properties and importantly biological activities of plant-derived SM6 glycoforms are comparable to the human-cell-derived counterparts.
24706782	3	34	theme	proteins	475:482	arg1	production					424:433	the production	420:433	the production of therapeutically relevant recombinant proteins	420:482	Plants have a proven record for the production of therapeutically relevant recombinant proteins.
24706782	1	35	theme	important	109:117	arg1	player					119:124	an important player	106:124	an important player of the human's innate defense mechanisms	106:165	IgM antibodies are an important player of the human's innate defense mechanisms and increasingly have gained interest as therapeutics.
24706782	1	35	theme	important	109:117	arg1	antibodies					91:100	IgM antibodies	87:100	IgM antibodies	87:100	IgM antibodies are an important player of the human's innate defense mechanisms and increasingly have gained interest as therapeutics.
24706782	12	36	theme	unknown	1775:1781	arg1	contribution					1783:1794	the so far unknown contribution	1764:1794	the so far unknown contribution of sugar moieties to the function of IgMs	1764:1836	Moreover, the generation of IgMs with a controlled glycosylation pattern allows the study of the so far unknown contribution of sugar moieties to the function of IgMs.
24706782	11	37	theme	new	1570:1572	arg1	pathways					1574:1581	new pathways	1570:1581	new pathways	1570:1581	The in planta generation of one of the most complex human proteins opens new pathways toward the production of difficult-to-express proteins for pharmaceutical applications.
24706782	3	38	theme	relevant	454:461	arg1	proteins					475:482	therapeutically relevant recombinant proteins	438:482	therapeutically relevant recombinant proteins	438:482	Plants have a proven record for the production of therapeutically relevant recombinant proteins.
24706782	8	39	theme	sialylated	1119:1128	arg1	oligosaccharides					1141:1156	sialylated human-type oligosaccharides	1119:1156	sialylated human-type oligosaccharides	1119:1156	Moreover, extensive in planta glycoengineering allowed the generation of SM6 decorated with sialylated human-type oligosaccharides, comparable to plasma-derived IgM.
24706782	0	40	theme	heteromultimeric	55:70	arg1	IgM					72:74	functionally active heteromultimeric IgM	35:74	functionally active heteromultimeric IgM	35:74	Expression and glycoengineering of functionally active heteromultimeric IgM in plants.
24706782	4	41	theme	IgM	541:543	arg1	antibodies					545:554	IgM antibodies	541:554	IgM antibodies	541:554	However, whether they are able to express proteins like IgM antibodies, which range among the most complex human proteins, remains unknown so far.
24706782	10	42	theme	glycoforms	1431:1440	arg1	properties					1361:1370	Biochemical and biophysical properties	1333:1370	Biochemical and biophysical properties	1333:1370	Biochemical and biophysical properties and importantly biological activities of plant-derived SM6 glycoforms are comparable to the human-cell-derived counterparts.
24706782	10	42	theme	glycoforms	1431:1440	arg1	activities					1399:1408	importantly biological activities	1376:1408	importantly biological activities	1376:1408	Biochemical and biophysical properties and importantly biological activities of plant-derived SM6 glycoforms are comparable to the human-cell-derived counterparts.
24706782	8	43	theme	comparable	1159:1168	arg1	oligosaccharides					1141:1156	sialylated human-type oligosaccharides	1119:1156	sialylated human-type oligosaccharides	1119:1156	Moreover, extensive in planta glycoengineering allowed the generation of SM6 decorated with sialylated human-type oligosaccharides, comparable to plasma-derived IgM.
24706782	11	44	theme	planta	1504:1509	arg1	generation					1511:1520	The in planta generation	1497:1520	The in planta generation of one of the most complex human proteins	1497:1562	The in planta generation of one of the most complex human proteins opens new pathways toward the production of difficult-to-express proteins for pharmaceutical applications.
24706782	10	45	theme	biophysical	1349:1359	arg1	properties					1361:1370	Biochemical and biophysical properties	1333:1370	Biochemical and biophysical properties	1333:1370	Biochemical and biophysical properties and importantly biological activities of plant-derived SM6 glycoforms are comparable to the human-cell-derived counterparts.
24706782	7	46	theme	oligomannosidic	908:922	arg1	N-glycans					924:932	complex and oligomannosidic N-glycans	896:932	N-glycans	924:932	Detailed glycosylation analysis exhibited complex and oligomannosidic N-glycans in a site-specific manner on human-serum IgM and on plant- and human-cell-line-produced SM6.
24706782	8	47	theme	plasma-derived	1173:1186	arg1	IgM					1188:1190	plasma-derived IgM	1173:1190	plasma-derived IgM	1173:1190	Moreover, extensive in planta glycoengineering allowed the generation of SM6 decorated with sialylated human-type oligosaccharides, comparable to plasma-derived IgM.
24706782	9	48	theme	pentameric	1217:1226	arg1	IgM					1228:1230	pentameric IgM	1217:1230	pentameric IgM	1217:1230	A glycosylated model of pentameric IgM exhibits different accessibility of the glycosylation sites, explaining site-specific glycosylation.
24706782	7	49	theme	complex	896:902	arg1	N-glycans					924:932	complex and oligomannosidic N-glycans	896:932	N-glycans	924:932	Detailed glycosylation analysis exhibited complex and oligomannosidic N-glycans in a site-specific manner on human-serum IgM and on plant- and human-cell-line-produced SM6.
24706782	10	50	link	human-cell-derived	1464:1481	arg1	counterparts					1483:1494	the human-cell-derived counterparts	1460:1494	the human-cell-derived counterparts	1460:1494	Biochemical and biophysical properties and importantly biological activities of plant-derived SM6 glycoforms are comparable to the human-cell-derived counterparts.
24706782	9	51	gly	glycosylated	1195:1206	arg1	model					1208:1212	A glycosylated model	1193:1212	A glycosylated model of pentameric IgM	1193:1230	A glycosylated model of pentameric IgM exhibits different accessibility of the glycosylation sites, explaining site-specific glycosylation.
24706782	4	52	theme	complex	584:590	arg1	proteins					598:605	the most complex human proteins	575:605	the most complex human proteins	575:605	However, whether they are able to express proteins like IgM antibodies, which range among the most complex human proteins, remains unknown so far.
24706782	7	53	theme	Detailed	854:861	arg1	analysis					877:884	Detailed glycosylation analysis	854:884	Detailed glycosylation analysis	854:884	Detailed glycosylation analysis exhibited complex and oligomannosidic N-glycans in a site-specific manner on human-serum IgM and on plant- and human-cell-line-produced SM6.
24706782	3	54	contain	have	395:398	arg1	Plants					388:393	Plants	388:393	Plants	388:393	Plants have a proven record for the production of therapeutically relevant recombinant proteins.
24706782	3	54	contain	have	395:398	arg2	record					409:414	a proven record	400:414	a proven record for the production of therapeutically relevant recombinant proteins	400:482	Plants have a proven record for the production of therapeutically relevant recombinant proteins.
24706782	8	55	theme	extensive	1037:1045	arg1	glycoengineering					1057:1072	extensive in planta glycoengineering	1037:1072	extensive in planta glycoengineering	1037:1072	Moreover, extensive in planta glycoengineering allowed the generation of SM6 decorated with sialylated human-type oligosaccharides, comparable to plasma-derived IgM.
24706782	9	56	theme	sites	1286:1290	arg1	accessibility					1251:1263	different accessibility	1241:1263	different accessibility of the glycosylation sites	1241:1290	A glycosylated model of pentameric IgM exhibits different accessibility of the glycosylation sites, explaining site-specific glycosylation.
24706782	8	57	from	planta	1050:1055	arg1	extensive					1037:1045	extensive	1037:1045	extensive	1037:1045	Moreover, extensive in planta glycoengineering allowed the generation of SM6 decorated with sialylated human-type oligosaccharides, comparable to plasma-derived IgM.
24706782	5	58	theme	monoclonal	699:708	arg1	SM6					733:735	SM6	733:735	SM6	733:735	Here we report the in planta generation of the functionally active monoclonal antitumor IgM PAT-SM6 (SM6).
24706782	5	58	theme	monoclonal	699:708	arg1	PAT-SM6					724:730	monoclonal antitumor IgM PAT-SM6	699:730	the functionally active monoclonal antitumor IgM PAT-SM6 (SM6)	675:736	Here we report the in planta generation of the functionally active monoclonal antitumor IgM PAT-SM6 (SM6).
24706782	10	59	theme	Biochemical	1333:1343	arg1	properties					1361:1370	Biochemical and biophysical properties	1333:1370	Biochemical and biophysical properties	1333:1370	Biochemical and biophysical properties and importantly biological activities of plant-derived SM6 glycoforms are comparable to the human-cell-derived counterparts.
24706782	12	60	theme	controlled	1711:1720	arg1	pattern					1736:1742	a controlled glycosylation pattern	1709:1742	a controlled glycosylation pattern	1709:1742	Moreover, the generation of IgMs with a controlled glycosylation pattern allows the study of the so far unknown contribution of sugar moieties to the function of IgMs.
24706782	12	61	with	generation	1685:1694	arg1	pattern					1736:1742	a controlled glycosylation pattern	1709:1742	a controlled glycosylation pattern	1709:1742	Moreover, the generation of IgMs with a controlled glycosylation pattern allows the study of the so far unknown contribution of sugar moieties to the function of IgMs.
24706782	5	62	theme	planta	654:659	arg1	generation					661:670	the in planta generation	647:670	the in planta generation of the functionally active monoclonal antitumor IgM PAT-SM6 (SM6)	647:736	Here we report the in planta generation of the functionally active monoclonal antitumor IgM PAT-SM6 (SM6).
24706782	9	63	gly	glycosylation	1272:1284	arg2	sites					1286:1290	the glycosylation sites	1268:1290	the glycosylation sites	1268:1290	A glycosylated model of pentameric IgM exhibits different accessibility of the glycosylation sites, explaining site-specific glycosylation.
24706782	4	64	dep	remains	608:614	arg1	able					511:514	able	511:514	able	511:514	However, whether they are able to express proteins like IgM antibodies, which range among the most complex human proteins, remains unknown so far.
24706782	2	65	theme	mammalian	267:275	arg1	culture					282:288	mammalian cell culture	267:288	mammalian cell culture	267:288	Although the expression of IgM antibodies in mammalian cell culture is established, this approach remains costly and alternative methods have not been developed yet.
24706782	8	66	link	plasma-derived	1173:1186	arg1	IgM					1188:1190	plasma-derived IgM	1173:1190	plasma-derived IgM	1173:1190	Moreover, extensive in planta glycoengineering allowed the generation of SM6 decorated with sialylated human-type oligosaccharides, comparable to plasma-derived IgM.
24706782	12	67	theme	IgMs	1833:1836	arg1	function					1821:1828	the function	1817:1828	the function of IgMs	1817:1836	Moreover, the generation of IgMs with a controlled glycosylation pattern allows the study of the so far unknown contribution of sugar moieties to the function of IgMs.
24706782	2	68	theme	antibodies	253:262	arg1	expression					235:244	the expression	231:244	the expression of IgM antibodies in mammalian cell culture	231:288	Although the expression of IgM antibodies in mammalian cell culture is established, this approach remains costly and alternative methods have not been developed yet.
24706782	11	69	theme	pharmaceutical	1642:1655	arg1	applications					1657:1668	pharmaceutical applications	1642:1668	pharmaceutical applications	1642:1668	The in planta generation of one of the most complex human proteins opens new pathways toward the production of difficult-to-express proteins for pharmaceutical applications.
24706782	1	70	theme	defense	148:154	arg1	mechanisms					156:165	the human's innate defense mechanisms	129:165	the human's innate defense mechanisms	129:165	IgM antibodies are an important player of the human's innate defense mechanisms and increasingly have gained interest as therapeutics.
24706782	11	71	theme	proteins	1629:1636	arg1	production					1594:1603	the production	1590:1603	the production of difficult-to-express proteins for pharmaceutical applications	1590:1668	The in planta generation of one of the most complex human proteins opens new pathways toward the production of difficult-to-express proteins for pharmaceutical applications.
24706782	5	72	theme	IgM	720:722	arg1	SM6					733:735	SM6	733:735	SM6	733:735	Here we report the in planta generation of the functionally active monoclonal antitumor IgM PAT-SM6 (SM6).
24706782	5	72	theme	IgM	720:722	arg1	PAT-SM6					724:730	monoclonal antitumor IgM PAT-SM6	699:730	the functionally active monoclonal antitumor IgM PAT-SM6 (SM6)	675:736	Here we report the in planta generation of the functionally active monoclonal antitumor IgM PAT-SM6 (SM6).
24706782	10	73	theme	biological	1388:1397	arg1	activities					1399:1408	importantly biological activities	1376:1408	importantly biological activities	1376:1408	Biochemical and biophysical properties and importantly biological activities of plant-derived SM6 glycoforms are comparable to the human-cell-derived counterparts.
24706782	11	74	theme	human	1549:1553	arg1	proteins					1555:1562	the most complex human proteins	1532:1562	the most complex human proteins	1532:1562	The in planta generation of one of the most complex human proteins opens new pathways toward the production of difficult-to-express proteins for pharmaceutical applications.
24706782	12	75	theme	contribution	1783:1794	arg1	study					1755:1759	the study	1751:1759	the study of the so far unknown contribution of sugar moieties to the function of IgMs	1751:1836	Moreover, the generation of IgMs with a controlled glycosylation pattern allows the study of the so far unknown contribution of sugar moieties to the function of IgMs.
24706782	8	76	gly	sialylated	1119:1128	arg1	oligosaccharides					1141:1156	sialylated human-type oligosaccharides	1119:1156	sialylated human-type oligosaccharides	1119:1156	Moreover, extensive in planta glycoengineering allowed the generation of SM6 decorated with sialylated human-type oligosaccharides, comparable to plasma-derived IgM.
24706782	8	77	theme	SM6	1100:1102	arg1	generation					1086:1095	the generation	1082:1095	the generation of SM6 decorated with sialylated human-type oligosaccharides, comparable to plasma-derived IgM	1082:1190	Moreover, extensive in planta glycoengineering allowed the generation of SM6 decorated with sialylated human-type oligosaccharides, comparable to plasma-derived IgM.
24706782	2	78	from	expression	235:244	arg1	culture					282:288	mammalian cell culture	267:288	mammalian cell culture	267:288	Although the expression of IgM antibodies in mammalian cell culture is established, this approach remains costly and alternative methods have not been developed yet.
24706782	10	79	theme	SM6	1427:1429	arg1	glycoforms					1431:1440	plant-derived SM6 glycoforms	1413:1440	plant-derived SM6 glycoforms	1413:1440	Biochemical and biophysical properties and importantly biological activities of plant-derived SM6 glycoforms are comparable to the human-cell-derived counterparts.
24706782	7	80	theme	site-specific	939:951	arg1	manner					953:958	a site-specific manner	937:958	a site-specific manner	937:958	Detailed glycosylation analysis exhibited complex and oligomannosidic N-glycans in a site-specific manner on human-serum IgM and on plant- and human-cell-line-produced SM6.
24706782	0	81	theme	active	48:53	arg1	IgM					72:74	functionally active heteromultimeric IgM	35:74	functionally active heteromultimeric IgM	35:74	Expression and glycoengineering of functionally active heteromultimeric IgM in plants.
24706782	8	82	theme	human-type	1130:1139	arg1	oligosaccharides					1141:1156	sialylated human-type oligosaccharides	1119:1156	sialylated human-type oligosaccharides	1119:1156	Moreover, extensive in planta glycoengineering allowed the generation of SM6 decorated with sialylated human-type oligosaccharides, comparable to plasma-derived IgM.
24706782	3	83	theme	recombinant	463:473	arg1	proteins					475:482	therapeutically relevant recombinant proteins	438:482	therapeutically relevant recombinant proteins	438:482	Plants have a proven record for the production of therapeutically relevant recombinant proteins.
24706782	0	84	theme	IgM	72:74	arg1	glycoengineering					15:30	glycoengineering	15:30	glycoengineering	15:30	Expression and glycoengineering of functionally active heteromultimeric IgM in plants.
24706782	0	84	theme	IgM	72:74	arg1	Expression					0:9	Expression	0:9	Expression	0:9	Expression and glycoengineering of functionally active heteromultimeric IgM in plants.
24706782	3	85	theme	proven	402:407	arg1	record					409:414	a proven record	400:414	a proven record for the production of therapeutically relevant recombinant proteins	400:482	Plants have a proven record for the production of therapeutically relevant recombinant proteins.
24706782	2	86	theme	alternative	339:349	arg1	methods					351:357	alternative methods	339:357	alternative methods	339:357	Although the expression of IgM antibodies in mammalian cell culture is established, this approach remains costly and alternative methods have not been developed yet.
24706782	10	87	link	plant-derived	1413:1425	arg1	glycoforms					1431:1440	plant-derived SM6 glycoforms	1413:1440	plant-derived SM6 glycoforms	1413:1440	Biochemical and biophysical properties and importantly biological activities of plant-derived SM6 glycoforms are comparable to the human-cell-derived counterparts.
24706782	9	88	theme	glycosylated	1195:1206	arg1	model					1208:1212	A glycosylated model	1193:1212	A glycosylated model of pentameric IgM	1193:1230	A glycosylated model of pentameric IgM exhibits different accessibility of the glycosylation sites, explaining site-specific glycosylation.
24706782	11	89	theme	most	1536:1539	arg1	proteins					1555:1562	the most complex human proteins	1532:1562	the most complex human proteins	1532:1562	The in planta generation of one of the most complex human proteins opens new pathways toward the production of difficult-to-express proteins for pharmaceutical applications.
24706782	8	90	from	extensive	1037:1045	arg1	planta					1050:1055	planta	1050:1055	planta	1050:1055	Moreover, extensive in planta glycoengineering allowed the generation of SM6 decorated with sialylated human-type oligosaccharides, comparable to plasma-derived IgM.
24706782	10	91	theme	human-cell-derived	1464:1481	arg1	counterparts					1483:1494	the human-cell-derived counterparts	1460:1494	the human-cell-derived counterparts	1460:1494	Biochemical and biophysical properties and importantly biological activities of plant-derived SM6 glycoforms are comparable to the human-cell-derived counterparts.
21569618	11	0	theme	chemotherapeutic	1615:1630	arg1	agents					1632:1637	novel chemotherapeutic agents	1609:1637	novel chemotherapeutic agents	1609:1637	In addition these phosphorylation sites may be targeted by novel chemotherapeutic agents to prevent phosphorylation lead by HCV viral entry complex.
21569618	5	1	with	assembly	613:620	arg1	junctions					633:641	tight junctions	627:641	tight junctions	627:641	The claudin-1 assembly with tight junctions is regulated by post translational modifications.
21569618	9	2	contain	have	1249:1252	arg2	potential					1254:1262	potential	1254:1262	potential for O-β-GlcNAc and phosphorylation interplay	1254:1307	We also identified Yin Yang sites that may have potential for O-β-GlcNAc and phosphorylation interplay at same Ser/Thr residues.
21569618	9	2	contain	have	1249:1252	arg1	sites					1234:1238	Yin Yang sites	1225:1238	Yin Yang sites that may have potential for O-β-GlcNAc and phosphorylation interplay at same Ser/Thr residues	1225:1332	We also identified Yin Yang sites that may have potential for O-β-GlcNAc and phosphorylation interplay at same Ser/Thr residues.
21569618	8	3	theme	O-glycosylation	1183:1197	arg1	sites					1199:1203	possible O-glycosylation sites	1174:1203	possible O-glycosylation sites	1174:1203	Netphos 2.0 and Disphos 1.3 programs were used for potential phosphorylation; NetPhosK 1.0 and KinasePhos for kinase prediction; and YinOYang 1.2 and OGPET to predict possible O-glycosylation sites.
21569618	0	4	contain	has	39:41	arg2	potential					48:56	high potential	43:56	high potential for phosphorylation and O-glycosylation	43:96	Claudin-1 required for HCV virus entry has high potential for phosphorylation and O-glycosylation.
21569618	0	4	contain	has	39:41	arg1	Claudin-1					0:8	Claudin-1	0:8	Claudin-1 required for HCV virus entry	0:37	Claudin-1 required for HCV virus entry has high potential for phosphorylation and O-glycosylation.
21569618	1	5	theme	cirrhosis	154:162	arg1	carcinoma					140:148	hepatocellular carcinoma	125:148	hepatocellular carcinoma	125:148	HCV is a leading cause of hepatocellular carcinoma and cirrhosis all over the world.
21569618	1	5	theme	cirrhosis	154:162	arg1	all					164:166	cirrhosis all	154:166	cirrhosis all over the world	154:181	HCV is a leading cause of hepatocellular carcinoma and cirrhosis all over the world.
21569618	10	6	theme	first	1346:1350	arg1	time					1352:1355	the first time	1342:1355	the first time	1342:1355	We for the first time proposed that alternate phosphorylation and O-β-GlcNAc modification on Ser 192, Ser 205, Ser 206; and Thr 191 may provide an on/off switch to regulate assembly of claudin-1 at tight junctions.
21569618	3	7	theme	therapeutic	342:352	arg1	strategies					354:363	therapeutic strategies	342:363	therapeutic strategies	342:363	For therapeutic strategies, regulation of viral entry into the host cells holds a lot of promise.
21569618	9	8	theme	phosphorylation	1283:1297	arg1	interplay					1299:1307	phosphorylation interplay	1283:1307	phosphorylation interplay	1283:1307	We also identified Yin Yang sites that may have potential for O-β-GlcNAc and phosphorylation interplay at same Ser/Thr residues.
21569618	5	9	theme	tight	627:631	arg1	junctions					633:641	tight junctions	627:641	tight junctions	627:641	The claudin-1 assembly with tight junctions is regulated by post translational modifications.
21569618	6	10	with	claudins	700:707	arg1	junctions					745:753	tight junctions	739:753	tight junctions	739:753	During claudins assembly and disassembly with tight junctions, phosphorylation is required at C-terminal tail.
21569618	8	11	theme	Disphos	1023:1029	arg1	programs					1035:1042	Netphos 2.0 and Disphos 1.3 programs	1007:1042	Netphos 2.0 and Disphos 1.3 programs	1007:1042	Netphos 2.0 and Disphos 1.3 programs were used for potential phosphorylation; NetPhosK 1.0 and KinasePhos for kinase prediction; and YinOYang 1.2 and OGPET to predict possible O-glycosylation sites.
21569618	10	12	theme	alternate	1371:1379	arg1	phosphorylation					1381:1395	alternate phosphorylation	1371:1395	alternate phosphorylation	1371:1395	We for the first time proposed that alternate phosphorylation and O-β-GlcNAc modification on Ser 192, Ser 205, Ser 206; and Thr 191 may provide an on/off switch to regulate assembly of claudin-1 at tight junctions.
21569618	4	13	theme	HCV	553:555	arg1	binding					557:563	HCV binding	553:563	HCV binding	553:563	During HCV infection claudin-1 is highly expressed in liver and believed to be associated with HCV virus entry after HCV binding with or without co-receptor CD81.
21569618	4	14	theme	HCV	443:445	arg1	infection					447:455	HCV infection	443:455	HCV infection	443:455	During HCV infection claudin-1 is highly expressed in liver and believed to be associated with HCV virus entry after HCV binding with or without co-receptor CD81.
21569618	6	15	theme	C-terminal	787:796	arg1	tail					798:801	C-terminal tail	787:801	C-terminal tail	787:801	During claudins assembly and disassembly with tight junctions, phosphorylation is required at C-terminal tail.
21569618	7	16	theme	O-β-GlcNAc	864:873	arg1	modification					875:886	O-β-GlcNAc modification	864:886	O-β-GlcNAc modification	864:886	In cellular proteins, interplay between phosphorylation and O-β-GlcNAc modification is believed to be functional switch, but it is very difficult to monitor these functional and vibrant changes in vivo.
21569618	10	17	theme	claudin-1	1520:1528	arg1	assembly					1508:1515	assembly	1508:1515	assembly of claudin-1	1508:1528	We for the first time proposed that alternate phosphorylation and O-β-GlcNAc modification on Ser 192, Ser 205, Ser 206; and Thr 191 may provide an on/off switch to regulate assembly of claudin-1 at tight junctions.
21569618	9	18	theme	same	1312:1315	arg1	residues					1325:1332	same Ser/Thr residues	1312:1332	same Ser/Thr residues	1312:1332	We also identified Yin Yang sites that may have potential for O-β-GlcNAc and phosphorylation interplay at same Ser/Thr residues.
21569618	11	19	theme	phosphorylation	1568:1582	arg1	sites					1584:1588	these phosphorylation sites	1562:1588	these phosphorylation sites	1562:1588	In addition these phosphorylation sites may be targeted by novel chemotherapeutic agents to prevent phosphorylation lead by HCV viral entry complex.
21569618	9	20	theme	Ser/Thr	1317:1323	arg1	residues					1325:1332	same Ser/Thr residues	1312:1332	same Ser/Thr residues	1312:1332	We also identified Yin Yang sites that may have potential for O-β-GlcNAc and phosphorylation interplay at same Ser/Thr residues.
21569618	3	21	theme	viral	380:384	arg1	entry					386:390	viral entry	380:390	viral entry into the host cells	380:410	For therapeutic strategies, regulation of viral entry into the host cells holds a lot of promise.
21569618	5	22	theme	claudin-1	603:611	arg1	assembly					613:620	The claudin-1 assembly	599:620	The claudin-1 assembly with tight junctions	599:641	The claudin-1 assembly with tight junctions is regulated by post translational modifications.
21569618	8	23	theme	Netphos	1007:1013	arg1	programs					1035:1042	Netphos 2.0 and Disphos 1.3 programs	1007:1042	Netphos 2.0 and Disphos 1.3 programs	1007:1042	Netphos 2.0 and Disphos 1.3 programs were used for potential phosphorylation; NetPhosK 1.0 and KinasePhos for kinase prediction; and YinOYang 1.2 and OGPET to predict possible O-glycosylation sites.
21569618	11	24	theme	viral	1678:1682	arg1	entry					1684:1688	HCV viral entry complex	1674:1696	HCV viral entry complex	1674:1696	In addition these phosphorylation sites may be targeted by novel chemotherapeutic agents to prevent phosphorylation lead by HCV viral entry complex.
21569618	0	25	theme	HCV	23:25	arg1	entry					33:37	HCV virus entry	23:37	HCV virus entry	23:37	Claudin-1 required for HCV virus entry has high potential for phosphorylation and O-glycosylation.
21569618	5	26	theme	translational	664:676	arg1	modifications					678:690	post translational modifications	659:690	post translational modifications	659:690	The claudin-1 assembly with tight junctions is regulated by post translational modifications.
21569618	8	27	gly	O-glycosylation	1183:1197	arg2	sites					1199:1203	possible O-glycosylation sites	1174:1203	possible O-glycosylation sites	1174:1203	Netphos 2.0 and Disphos 1.3 programs were used for potential phosphorylation; NetPhosK 1.0 and KinasePhos for kinase prediction; and YinOYang 1.2 and OGPET to predict possible O-glycosylation sites.
21569618	8	28	theme	possible	1174:1181	arg1	sites					1199:1203	possible O-glycosylation sites	1174:1203	possible O-glycosylation sites	1174:1203	Netphos 2.0 and Disphos 1.3 programs were used for potential phosphorylation; NetPhosK 1.0 and KinasePhos for kinase prediction; and YinOYang 1.2 and OGPET to predict possible O-glycosylation sites.
21569618	4	29	theme	virus	535:539	arg1	entry					541:545	HCV virus entry	531:545	HCV virus entry after HCV binding with or without co-receptor CD81	531:596	During HCV infection claudin-1 is highly expressed in liver and believed to be associated with HCV virus entry after HCV binding with or without co-receptor CD81.
21569618	8	30	theme	potential	1058:1066	arg1	phosphorylation					1068:1082	potential phosphorylation	1058:1082	potential phosphorylation	1058:1082	Netphos 2.0 and Disphos 1.3 programs were used for potential phosphorylation; NetPhosK 1.0 and KinasePhos for kinase prediction; and YinOYang 1.2 and OGPET to predict possible O-glycosylation sites.
21569618	11	31	theme	HCV	1674:1676	arg1	entry					1684:1688	HCV viral entry complex	1674:1696	HCV viral entry complex	1674:1696	In addition these phosphorylation sites may be targeted by novel chemotherapeutic agents to prevent phosphorylation lead by HCV viral entry complex.
21569618	7	32	theme	cellular	807:814	arg1	proteins					816:823	cellular proteins	807:823	cellular proteins	807:823	In cellular proteins, interplay between phosphorylation and O-β-GlcNAc modification is believed to be functional switch, but it is very difficult to monitor these functional and vibrant changes in vivo.
21569618	10	33	from	modification	1412:1423	arg1	Ser					1437:1439	Ser 205	1437:1443	Ser 205	1437:1443	We for the first time proposed that alternate phosphorylation and O-β-GlcNAc modification on Ser 192, Ser 205, Ser 206; and Thr 191 may provide an on/off switch to regulate assembly of claudin-1 at tight junctions.
21569618	10	33	from	modification	1412:1423	arg1	Ser					1446:1448	Ser 206	1446:1452	Ser 206	1446:1452	We for the first time proposed that alternate phosphorylation and O-β-GlcNAc modification on Ser 192, Ser 205, Ser 206; and Thr 191 may provide an on/off switch to regulate assembly of claudin-1 at tight junctions.
21569618	10	33	from	modification	1412:1423	arg1	Thr					1459:1461	Thr 191	1459:1465	Thr 191	1459:1465	We for the first time proposed that alternate phosphorylation and O-β-GlcNAc modification on Ser 192, Ser 205, Ser 206; and Thr 191 may provide an on/off switch to regulate assembly of claudin-1 at tight junctions.
21569618	10	33	from	modification	1412:1423	arg1	Ser					1428:1430	Ser 192	1428:1434	Ser 192	1428:1434	We for the first time proposed that alternate phosphorylation and O-β-GlcNAc modification on Ser 192, Ser 205, Ser 206; and Thr 191 may provide an on/off switch to regulate assembly of claudin-1 at tight junctions.
21569618	4	34	theme	HCV	531:533	arg1	entry					541:545	HCV virus entry	531:545	HCV virus entry after HCV binding with or without co-receptor CD81	531:596	During HCV infection claudin-1 is highly expressed in liver and believed to be associated with HCV virus entry after HCV binding with or without co-receptor CD81.
21569618	9	35	theme	Yin	1225:1227	arg1	Yang					1229:1232	Yin Yang	1225:1232	Yin Yang sites that may have potential for O-β-GlcNAc and phosphorylation interplay at same Ser/Thr residues	1225:1332	We also identified Yin Yang sites that may have potential for O-β-GlcNAc and phosphorylation interplay at same Ser/Thr residues.
21569618	0	36	theme	virus	27:31	arg1	entry					33:37	HCV virus entry	23:37	HCV virus entry	23:37	Claudin-1 required for HCV virus entry has high potential for phosphorylation and O-glycosylation.
21569618	3	37	theme	host	401:404	arg1	cells					406:410	the host cells	397:410	the host cells	397:410	For therapeutic strategies, regulation of viral entry into the host cells holds a lot of promise.
21569618	9	38	theme	Yang	1229:1232	arg1	sites					1234:1238	Yin Yang sites	1225:1238	Yin Yang sites that may have potential for O-β-GlcNAc and phosphorylation interplay at same Ser/Thr residues	1225:1332	We also identified Yin Yang sites that may have potential for O-β-GlcNAc and phosphorylation interplay at same Ser/Thr residues.
21569618	2	39	theme	tight	213:217	arg1	proteins					230:237	tight junction's proteins	213:237	tight junction's proteins that are responsible for establishing barriers for controlling the flow of molecules around cells	213:335	Claudins belong to family of tight junction's proteins that are responsible for establishing barriers for controlling the flow of molecules around cells.
21569618	3	40	theme	promise	427:433	arg1	promise					427:433	promise	427:433	promise	427:433	For therapeutic strategies, regulation of viral entry into the host cells holds a lot of promise.
21569618	3	40	theme	promise	427:433	arg1	lot					420:422	a lot	418:422	a lot of promise	418:433	For therapeutic strategies, regulation of viral entry into the host cells holds a lot of promise.
21569618	0	41	theme	high	43:46	arg1	potential					48:56	high potential	43:56	high potential for phosphorylation and O-glycosylation	43:96	Claudin-1 required for HCV virus entry has high potential for phosphorylation and O-glycosylation.
21569618	8	42	used	used	1049:1052	arg2	programs					1035:1042	Netphos 2.0 and Disphos 1.3 programs	1007:1042	Netphos 2.0 and Disphos 1.3 programs	1007:1042	Netphos 2.0 and Disphos 1.3 programs were used for potential phosphorylation; NetPhosK 1.0 and KinasePhos for kinase prediction; and YinOYang 1.2 and OGPET to predict possible O-glycosylation sites.
21569618	8	43	theme	kinase	1117:1122	arg1	prediction					1124:1133	kinase prediction	1117:1133	kinase prediction	1117:1133	Netphos 2.0 and Disphos 1.3 programs were used for potential phosphorylation; NetPhosK 1.0 and KinasePhos for kinase prediction; and YinOYang 1.2 and OGPET to predict possible O-glycosylation sites.
21569618	10	44	theme	on/off	1482:1487	arg1	switch					1489:1494	an on/off switch	1479:1494	an on/off switch to regulate assembly of claudin-1 at tight junctions	1479:1547	We for the first time proposed that alternate phosphorylation and O-β-GlcNAc modification on Ser 192, Ser 205, Ser 206; and Thr 191 may provide an on/off switch to regulate assembly of claudin-1 at tight junctions.
21569618	6	45	theme	tight	739:743	arg1	junctions					745:753	tight junctions	739:753	tight junctions	739:753	During claudins assembly and disassembly with tight junctions, phosphorylation is required at C-terminal tail.
21569618	1	46	theme	leading	108:114	arg1	cause					116:120	a leading cause	106:120	a leading cause of hepatocellular carcinoma	106:148	HCV is a leading cause of hepatocellular carcinoma and cirrhosis all over the world.
21569618	1	46	theme	leading	108:114	arg1	HCV					99:101	HCV	99:101	HCV	99:101	HCV is a leading cause of hepatocellular carcinoma and cirrhosis all over the world.
21569618	10	47	theme	O-β-GlcNAc	1401:1410	arg1	modification					1412:1423	O-β-GlcNAc modification	1401:1423	O-β-GlcNAc modification	1401:1423	We for the first time proposed that alternate phosphorylation and O-β-GlcNAc modification on Ser 192, Ser 205, Ser 206; and Thr 191 may provide an on/off switch to regulate assembly of claudin-1 at tight junctions.
21569618	2	48	theme	molecules	314:322	arg1	flow					306:309	the flow	302:309	the flow of molecules around cells	302:335	Claudins belong to family of tight junction's proteins that are responsible for establishing barriers for controlling the flow of molecules around cells.
21569618	6	49	dep	claudins	700:707	arg1	claudins					700:707	claudins assembly and disassembly	700:732	claudins assembly and disassembly with tight junctions	700:753	During claudins assembly and disassembly with tight junctions, phosphorylation is required at C-terminal tail.
21569618	6	49	dep	claudins	700:707	arg1	disassembly					722:732	disassembly	722:732	disassembly	722:732	During claudins assembly and disassembly with tight junctions, phosphorylation is required at C-terminal tail.
21569618	6	49	dep	claudins	700:707	arg1	assembly					709:716	assembly	709:716	assembly	709:716	During claudins assembly and disassembly with tight junctions, phosphorylation is required at C-terminal tail.
21569618	5	50	theme	post	659:662	arg1	modifications					678:690	post translational modifications	659:690	post translational modifications	659:690	The claudin-1 assembly with tight junctions is regulated by post translational modifications.
21569618	7	51	theme	vibrant	982:988	arg1	changes					990:996	these functional and vibrant changes	961:996	these functional and vibrant changes	961:996	In cellular proteins, interplay between phosphorylation and O-β-GlcNAc modification is believed to be functional switch, but it is very difficult to monitor these functional and vibrant changes in vivo.
21569618	10	52	from	phosphorylation	1381:1395	arg1	Ser					1437:1439	Ser 205	1437:1443	Ser 205	1437:1443	We for the first time proposed that alternate phosphorylation and O-β-GlcNAc modification on Ser 192, Ser 205, Ser 206; and Thr 191 may provide an on/off switch to regulate assembly of claudin-1 at tight junctions.
21569618	10	52	from	phosphorylation	1381:1395	arg1	Ser					1446:1448	Ser 206	1446:1452	Ser 206	1446:1452	We for the first time proposed that alternate phosphorylation and O-β-GlcNAc modification on Ser 192, Ser 205, Ser 206; and Thr 191 may provide an on/off switch to regulate assembly of claudin-1 at tight junctions.
21569618	10	52	from	phosphorylation	1381:1395	arg1	Thr					1459:1461	Thr 191	1459:1465	Thr 191	1459:1465	We for the first time proposed that alternate phosphorylation and O-β-GlcNAc modification on Ser 192, Ser 205, Ser 206; and Thr 191 may provide an on/off switch to regulate assembly of claudin-1 at tight junctions.
21569618	10	52	from	phosphorylation	1381:1395	arg1	Ser					1428:1430	Ser 192	1428:1434	Ser 192	1428:1434	We for the first time proposed that alternate phosphorylation and O-β-GlcNAc modification on Ser 192, Ser 205, Ser 206; and Thr 191 may provide an on/off switch to regulate assembly of claudin-1 at tight junctions.
21569618	11	53	theme	complex	1690:1696	arg1	entry					1684:1688	HCV viral entry complex	1674:1696	HCV viral entry complex	1674:1696	In addition these phosphorylation sites may be targeted by novel chemotherapeutic agents to prevent phosphorylation lead by HCV viral entry complex.
21569618	1	54	theme	hepatocellular	125:138	arg1	carcinoma					140:148	hepatocellular carcinoma	125:148	hepatocellular carcinoma	125:148	HCV is a leading cause of hepatocellular carcinoma and cirrhosis all over the world.
21569618	7	55	theme	functional	906:915	arg1	switch					917:922	functional switch	906:922	functional switch	906:922	In cellular proteins, interplay between phosphorylation and O-β-GlcNAc modification is believed to be functional switch, but it is very difficult to monitor these functional and vibrant changes in vivo.
21569618	4	56	theme	co-receptor	581:591	arg1	CD81					593:596	co-receptor CD81	581:596	co-receptor CD81	581:596	During HCV infection claudin-1 is highly expressed in liver and believed to be associated with HCV virus entry after HCV binding with or without co-receptor CD81.
21569618	3	57	theme	entry	386:390	arg1	regulation					366:375	regulation	366:375	regulation of viral entry into the host cells	366:410	For therapeutic strategies, regulation of viral entry into the host cells holds a lot of promise.
21569618	11	58	theme	novel	1609:1613	arg1	agents					1632:1637	novel chemotherapeutic agents	1609:1637	novel chemotherapeutic agents	1609:1637	In addition these phosphorylation sites may be targeted by novel chemotherapeutic agents to prevent phosphorylation lead by HCV viral entry complex.
21569618	7	59	theme	functional	967:976	arg1	changes					990:996	these functional and vibrant changes	961:996	these functional and vibrant changes	961:996	In cellular proteins, interplay between phosphorylation and O-β-GlcNAc modification is believed to be functional switch, but it is very difficult to monitor these functional and vibrant changes in vivo.
21569618	1	60	theme	carcinoma	140:148	arg1	cause					116:120	a leading cause	106:120	a leading cause of hepatocellular carcinoma	106:148	HCV is a leading cause of hepatocellular carcinoma and cirrhosis all over the world.
21569618	1	60	theme	carcinoma	140:148	arg1	carcinoma					140:148	hepatocellular carcinoma	125:148	hepatocellular carcinoma	125:148	HCV is a leading cause of hepatocellular carcinoma and cirrhosis all over the world.
21569618	1	60	theme	carcinoma	140:148	arg1	all					164:166	cirrhosis all	154:166	cirrhosis all over the world	154:181	HCV is a leading cause of hepatocellular carcinoma and cirrhosis all over the world.
21569618	1	60	theme	carcinoma	140:148	arg1	HCV					99:101	HCV	99:101	HCV	99:101	HCV is a leading cause of hepatocellular carcinoma and cirrhosis all over the world.
21569618	10	61	theme	tight	1533:1537	arg1	junctions					1539:1547	tight junctions	1533:1547	tight junctions	1533:1547	We for the first time proposed that alternate phosphorylation and O-β-GlcNAc modification on Ser 192, Ser 205, Ser 206; and Thr 191 may provide an on/off switch to regulate assembly of claudin-1 at tight junctions.
19898896	4	0	gly	glycosylated	726:737	arg1	NN163/166AA					706:716	NN163/166AA	706:716	NN163/166AA	706:716	Here, we show that the double mutant prestin(NN163/166AA) is not glycosylated and shows the expected NLC properties in the untreated and cholesterol-depleted HEK 293 cell model.
19898896	4	0	gly	glycosylated	726:737	arg1	prestin					698:704	the double mutant prestin	680:704	the double mutant prestin(NN163/166AA)	680:717	Here, we show that the double mutant prestin(NN163/166AA) is not glycosylated and shows the expected NLC properties in the untreated and cholesterol-depleted HEK 293 cell model.
19898896	6	1	theme	membrane	1161:1168	arg1	cholesterol					1170:1180	increased membrane cholesterol	1151:1180	increased membrane cholesterol	1151:1180	However, in the presence of increased membrane cholesterol, unlike the hyperpolarizing shift in NLC seen with WT prestin, cells expressing prestin(NN163/166AA) exhibit a linear capacitance function.
19898896	11	2	theme	caveolin-dependent	2059:2076	arg1	mechanisms					2078:2087	caveolin-dependent mechanisms	2059:2087	caveolin-dependent mechanisms	2059:2087	We speculate that the cholesterol regulation of prestin occurs through localization to and internalization from membrane microdomains by clathrin- and caveolin-dependent mechanisms.
19898896	1	3	theme	functions	164:172	arg1	degradation					201:211	degradation	201:211	degradation	201:211	Glycosylation is a common post-translational modification of proteins and is implicated in a variety of cellular functions including protein folding, degradation, sorting and trafficking, and membrane protein recycling.
19898896	1	3	theme	functions	164:172	arg1	functions					164:172	cellular functions	155:172	cellular functions including protein folding, degradation, sorting and trafficking, and membrane protein recycling	155:268	Glycosylation is a common post-translational modification of proteins and is implicated in a variety of cellular functions including protein folding, degradation, sorting and trafficking, and membrane protein recycling.
19898896	1	3	theme	functions	164:172	arg1	sorting					214:220	sorting	214:220	sorting	214:220	Glycosylation is a common post-translational modification of proteins and is implicated in a variety of cellular functions including protein folding, degradation, sorting and trafficking, and membrane protein recycling.
19898896	1	3	theme	functions	164:172	arg1	recycling					260:268	membrane protein recycling	243:268	membrane protein recycling	243:268	Glycosylation is a common post-translational modification of proteins and is implicated in a variety of cellular functions including protein folding, degradation, sorting and trafficking, and membrane protein recycling.
19898896	1	3	theme	functions	164:172	arg1	variety					144:150	a variety	142:150	a variety of cellular functions including protein folding, degradation, sorting and trafficking, and membrane protein recycling	142:268	Glycosylation is a common post-translational modification of proteins and is implicated in a variety of cellular functions including protein folding, degradation, sorting and trafficking, and membrane protein recycling.
19898896	1	3	theme	functions	164:172	arg1	folding					192:198	protein folding	184:198	protein folding	184:198	Glycosylation is a common post-translational modification of proteins and is implicated in a variety of cellular functions including protein folding, degradation, sorting and trafficking, and membrane protein recycling.
19898896	2	4	from	process	444:450	arg1	transduction					464:475	auditory transduction	455:475	auditory transduction	455:475	The membrane protein prestin is an essential component of the membrane-based motor driving electromotility changes (electromotility) in the outer hair cell (OHC), a central process in auditory transduction.
19898896	4	5	theme	cell	827:830	arg1	model					832:836	the untreated and cholesterol-depleted HEK 293 cell model	780:836	the untreated and cholesterol-depleted HEK 293 cell model	780:836	Here, we show that the double mutant prestin(NN163/166AA) is not glycosylated and shows the expected NLC properties in the untreated and cholesterol-depleted HEK 293 cell model.
19898896	5	6	theme	WT	859:860	arg1	prestin					862:868	WT prestin	859:868	WT prestin that readily forms oligomers	859:897	In addition, unlike WT prestin that readily forms oligomers, prestin(NN163/166AA) is enriched as monomers and more mobile in the plasma membrane, suggesting that oligomerization of prestin is dependent on glycosylation but is not essential for the generation of NLC in HEK 293 cells.
19898896	11	7	dep	localization	1979:1990	arg1	to					1992:1993	to	1992:1993	to	1992:1993	We speculate that the cholesterol regulation of prestin occurs through localization to and internalization from membrane microdomains by clathrin- and caveolin-dependent mechanisms.
19898896	6	8	theme	hyperpolarizing	1194:1208	arg1	shift					1210:1214	the hyperpolarizing shift	1190:1214	the hyperpolarizing shift in NLC seen with WT prestin	1190:1242	However, in the presence of increased membrane cholesterol, unlike the hyperpolarizing shift in NLC seen with WT prestin, cells expressing prestin(NN163/166AA) exhibit a linear capacitance function.
19898896	10	9	theme	regulatory	1834:1843	arg1	role					1845:1848	a regulatory role	1832:1848	a regulatory role for cellular trafficking and sorting in prestin function	1832:1905	These observations are the first to implicate a regulatory role for cellular trafficking and sorting in prestin function.
19898896	3	10	gly	N-glycosylation	524:538	arg2	sites					540:544	two N-glycosylation sites	520:544	two N-glycosylation sites (N163, N166) that, when mutated, marginally affect prestin nonlinear capacitance (NLC) function in cultured cells	520:658	Prestin was earlier identified to possess two N-glycosylation sites (N163, N166) that, when mutated, marginally affect prestin nonlinear capacitance (NLC) function in cultured cells.
19898896	3	10	gly	N-glycosylation	524:538	arg2	two					520:522	two	520:522	two	520:522	Prestin was earlier identified to possess two N-glycosylation sites (N163, N166) that, when mutated, marginally affect prestin nonlinear capacitance (NLC) function in cultured cells.
19898896	3	10	gly	N-glycosylation	524:538	arg2	N166					553:556	N166	553:556	N166	553:556	Prestin was earlier identified to possess two N-glycosylation sites (N163, N166) that, when mutated, marginally affect prestin nonlinear capacitance (NLC) function in cultured cells.
19898896	11	11	theme	prestin	1956:1962	arg1	regulation					1942:1951	the cholesterol regulation	1926:1951	the cholesterol regulation of prestin	1926:1962	We speculate that the cholesterol regulation of prestin occurs through localization to and internalization from membrane microdomains by clathrin- and caveolin-dependent mechanisms.
19898896	7	12	theme	cellular	1458:1465	arg1	trafficking					1467:1477	cholesterol-dependent cellular trafficking	1436:1477	cholesterol-dependent cellular trafficking	1436:1477	In an attempt to explain this finding, we discovered that both WT prestin and prestin(NN163/166AA) participate in cholesterol-dependent cellular trafficking.
19898896	5	13	from	generation	1087:1096	arg1	cells					1116:1120	HEK 293 cells	1108:1120	HEK 293 cells	1108:1120	In addition, unlike WT prestin that readily forms oligomers, prestin(NN163/166AA) is enriched as monomers and more mobile in the plasma membrane, suggesting that oligomerization of prestin is dependent on glycosylation but is not essential for the generation of NLC in HEK 293 cells.
19898896	1	14	theme	common	70:75	arg1	modification					96:107	a common post-translational modification	68:107	a common post-translational modification of proteins	68:119	Glycosylation is a common post-translational modification of proteins and is implicated in a variety of cellular functions including protein folding, degradation, sorting and trafficking, and membrane protein recycling.
19898896	1	14	theme	common	70:75	arg1	Glycosylation					51:63	Glycosylation	51:63	Glycosylation	51:63	Glycosylation is a common post-translational modification of proteins and is implicated in a variety of cellular functions including protein folding, degradation, sorting and trafficking, and membrane protein recycling.
19898896	11	15	theme	cholesterol	1930:1940	arg1	regulation					1942:1951	the cholesterol regulation	1926:1951	the cholesterol regulation of prestin	1926:1962	We speculate that the cholesterol regulation of prestin occurs through localization to and internalization from membrane microdomains by clathrin- and caveolin-dependent mechanisms.
19898896	4	16	theme	double	684:689	arg1	NN163/166AA					706:716	NN163/166AA	706:716	NN163/166AA	706:716	Here, we show that the double mutant prestin(NN163/166AA) is not glycosylated and shows the expected NLC properties in the untreated and cholesterol-depleted HEK 293 cell model.
19898896	4	16	theme	double	684:689	arg1	prestin					698:704	the double mutant prestin	680:704	the double mutant prestin(NN163/166AA)	680:717	Here, we show that the double mutant prestin(NN163/166AA) is not glycosylated and shows the expected NLC properties in the untreated and cholesterol-depleted HEK 293 cell model.
19898896	10	17	theme	cellular	1854:1861	arg1	trafficking					1863:1873	cellular trafficking	1854:1873	cellular trafficking	1854:1873	These observations are the first to implicate a regulatory role for cellular trafficking and sorting in prestin function.
19898896	4	18	theme	cholesterol-depleted	798:817	arg1	model					832:836	the untreated and cholesterol-depleted HEK 293 cell model	780:836	the untreated and cholesterol-depleted HEK 293 cell model	780:836	Here, we show that the double mutant prestin(NN163/166AA) is not glycosylated and shows the expected NLC properties in the untreated and cholesterol-depleted HEK 293 cell model.
19898896	1	19	theme	post-translational	77:94	arg1	modification					96:107	a common post-translational modification	68:107	a common post-translational modification of proteins	68:119	Glycosylation is a common post-translational modification of proteins and is implicated in a variety of cellular functions including protein folding, degradation, sorting and trafficking, and membrane protein recycling.
19898896	1	19	theme	post-translational	77:94	arg1	Glycosylation					51:63	Glycosylation	51:63	Glycosylation	51:63	Glycosylation is a common post-translational modification of proteins and is implicated in a variety of cellular functions including protein folding, degradation, sorting and trafficking, and membrane protein recycling.
19898896	1	20	theme	protein	184:190	arg1	folding					192:198	protein folding	184:198	protein folding	184:198	Glycosylation is a common post-translational modification of proteins and is implicated in a variety of cellular functions including protein folding, degradation, sorting and trafficking, and membrane protein recycling.
19898896	3	21	from	function	633:640	arg1	cells					654:658	cultured cells	645:658	cultured cells	645:658	Prestin was earlier identified to possess two N-glycosylation sites (N163, N166) that, when mutated, marginally affect prestin nonlinear capacitance (NLC) function in cultured cells.
19898896	9	22	theme	prestin	1764:1770	arg1	self-association					1719:1734	self-association	1719:1734	self-association	1719:1734	Based on our observations, we conclude that glycosylation regulates self-association and cellular trafficking of prestin(NN163/166AA).
19898896	9	22	theme	prestin	1764:1770	arg1	trafficking					1749:1759	cellular trafficking	1740:1759	cellular trafficking	1740:1759	Based on our observations, we conclude that glycosylation regulates self-association and cellular trafficking of prestin(NN163/166AA).
19898896	2	23	theme	protein	284:290	arg1	component					316:324	an essential component	303:324	an essential component of the membrane-based motor driving electromotility changes (electromotility) in the outer hair cell (OHC), a central process in auditory transduction	303:475	The membrane protein prestin is an essential component of the membrane-based motor driving electromotility changes (electromotility) in the outer hair cell (OHC), a central process in auditory transduction.
19898896	2	23	theme	protein	284:290	arg1	prestin					292:298	The membrane protein prestin	271:298	The membrane protein prestin	271:298	The membrane protein prestin is an essential component of the membrane-based motor driving electromotility changes (electromotility) in the outer hair cell (OHC), a central process in auditory transduction.
19898896	2	24	theme	outer	411:415	arg1	process					444:450	a central process	434:450	a central process in auditory transduction	434:475	The membrane protein prestin is an essential component of the membrane-based motor driving electromotility changes (electromotility) in the outer hair cell (OHC), a central process in auditory transduction.
19898896	2	24	theme	outer	411:415	arg1	OHC					428:430	OHC	428:430	OHC	428:430	The membrane protein prestin is an essential component of the membrane-based motor driving electromotility changes (electromotility) in the outer hair cell (OHC), a central process in auditory transduction.
19898896	2	24	theme	outer	411:415	arg1	cell					422:425	the outer hair cell	407:425	the outer hair cell (OHC)	407:431	The membrane protein prestin is an essential component of the membrane-based motor driving electromotility changes (electromotility) in the outer hair cell (OHC), a central process in auditory transduction.
19898896	3	25	theme	N-glycosylation	524:538	arg1	sites					540:544	two N-glycosylation sites	520:544	two N-glycosylation sites (N163, N166) that, when mutated, marginally affect prestin nonlinear capacitance (NLC) function in cultured cells	520:658	Prestin was earlier identified to possess two N-glycosylation sites (N163, N166) that, when mutated, marginally affect prestin nonlinear capacitance (NLC) function in cultured cells.
19898896	3	25	theme	N-glycosylation	524:538	arg1	N166					553:556	N166	553:556	N166	553:556	Prestin was earlier identified to possess two N-glycosylation sites (N163, N166) that, when mutated, marginally affect prestin nonlinear capacitance (NLC) function in cultured cells.
19898896	6	26	theme	cholesterol	1170:1180	arg1	presence					1139:1146	the presence	1135:1146	the presence of increased membrane cholesterol	1135:1180	However, in the presence of increased membrane cholesterol, unlike the hyperpolarizing shift in NLC seen with WT prestin, cells expressing prestin(NN163/166AA) exhibit a linear capacitance function.
19898896	2	27	from	changes	378:384	arg1	process					444:450	a central process	434:450	a central process in auditory transduction	434:475	The membrane protein prestin is an essential component of the membrane-based motor driving electromotility changes (electromotility) in the outer hair cell (OHC), a central process in auditory transduction.
19898896	2	27	from	changes	378:384	arg1	OHC					428:430	OHC	428:430	OHC	428:430	The membrane protein prestin is an essential component of the membrane-based motor driving electromotility changes (electromotility) in the outer hair cell (OHC), a central process in auditory transduction.
19898896	2	27	from	changes	378:384	arg1	cell					422:425	the outer hair cell	407:425	the outer hair cell (OHC)	407:431	The membrane protein prestin is an essential component of the membrane-based motor driving electromotility changes (electromotility) in the outer hair cell (OHC), a central process in auditory transduction.
19898896	5	28	from	monomers	936:943	arg1	membrane					975:982	the plasma membrane	964:982	the plasma membrane	964:982	In addition, unlike WT prestin that readily forms oligomers, prestin(NN163/166AA) is enriched as monomers and more mobile in the plasma membrane, suggesting that oligomerization of prestin is dependent on glycosylation but is not essential for the generation of NLC in HEK 293 cells.
19898896	2	29	theme	central	436:442	arg1	process					444:450	a central process	434:450	a central process in auditory transduction	434:475	The membrane protein prestin is an essential component of the membrane-based motor driving electromotility changes (electromotility) in the outer hair cell (OHC), a central process in auditory transduction.
19898896	2	29	theme	central	436:442	arg1	cell					422:425	the outer hair cell	407:425	the outer hair cell (OHC)	407:431	The membrane protein prestin is an essential component of the membrane-based motor driving electromotility changes (electromotility) in the outer hair cell (OHC), a central process in auditory transduction.
19898896	10	30	theme	prestin	1890:1896	arg1	function					1898:1905	prestin function	1890:1905	prestin function	1890:1905	These observations are the first to implicate a regulatory role for cellular trafficking and sorting in prestin function.
19898896	4	31	theme	HEK	819:821	arg1	model					832:836	the untreated and cholesterol-depleted HEK 293 cell model	780:836	the untreated and cholesterol-depleted HEK 293 cell model	780:836	Here, we show that the double mutant prestin(NN163/166AA) is not glycosylated and shows the expected NLC properties in the untreated and cholesterol-depleted HEK 293 cell model.
19898896	1	32	theme	proteins	112:119	arg1	modification					96:107	a common post-translational modification	68:107	a common post-translational modification of proteins	68:119	Glycosylation is a common post-translational modification of proteins and is implicated in a variety of cellular functions including protein folding, degradation, sorting and trafficking, and membrane protein recycling.
19898896	1	32	theme	proteins	112:119	arg1	Glycosylation					51:63	Glycosylation	51:63	Glycosylation	51:63	Glycosylation is a common post-translational modification of proteins and is implicated in a variety of cellular functions including protein folding, degradation, sorting and trafficking, and membrane protein recycling.
19898896	8	33	theme	function	1641:1648	arg1	loss					1629:1632	the loss	1625:1632	the loss of NLC function	1625:1648	In contrast to WT prestin, prestin(NN163/166AA) shows a significant cholesterol-dependent decrease in cell-surface expression, which may explain the loss of NLC function.
19898896	0	34	theme	cellular	32:39	arg1	activity					41:48	prestin cellular activity	24:48	prestin cellular activity	24:48	Glycosylation regulates prestin cellular activity.
19898896	5	35	theme	HEK	1108:1110	arg1	cells					1116:1120	HEK 293 cells	1108:1120	HEK 293 cells	1108:1120	In addition, unlike WT prestin that readily forms oligomers, prestin(NN163/166AA) is enriched as monomers and more mobile in the plasma membrane, suggesting that oligomerization of prestin is dependent on glycosylation but is not essential for the generation of NLC in HEK 293 cells.
19898896	8	36	theme	NLC	1637:1639	arg1	function					1641:1648	NLC function	1637:1648	NLC function	1637:1648	In contrast to WT prestin, prestin(NN163/166AA) shows a significant cholesterol-dependent decrease in cell-surface expression, which may explain the loss of NLC function.
19898896	3	37	dep	affect	590:595	arg1	sites					540:544	two N-glycosylation sites	520:544	two N-glycosylation sites (N163, N166) that, when mutated, marginally affect prestin nonlinear capacitance (NLC) function in cultured cells	520:658	Prestin was earlier identified to possess two N-glycosylation sites (N163, N166) that, when mutated, marginally affect prestin nonlinear capacitance (NLC) function in cultured cells.
19898896	3	37	dep	affect	590:595	arg1	N166					553:556	N166	553:556	N166	553:556	Prestin was earlier identified to possess two N-glycosylation sites (N163, N166) that, when mutated, marginally affect prestin nonlinear capacitance (NLC) function in cultured cells.
19898896	0	38	theme	prestin	24:30	arg1	activity					41:48	prestin cellular activity	24:48	prestin cellular activity	24:48	Glycosylation regulates prestin cellular activity.
19898896	8	39	from	decrease	1570:1577	arg1	expression					1595:1604	cell-surface expression	1582:1604	cell-surface expression	1582:1604	In contrast to WT prestin, prestin(NN163/166AA) shows a significant cholesterol-dependent decrease in cell-surface expression, which may explain the loss of NLC function.
19898896	2	40	theme	essential	306:314	arg1	component					316:324	an essential component	303:324	an essential component of the membrane-based motor driving electromotility changes (electromotility) in the outer hair cell (OHC), a central process in auditory transduction	303:475	The membrane protein prestin is an essential component of the membrane-based motor driving electromotility changes (electromotility) in the outer hair cell (OHC), a central process in auditory transduction.
19898896	2	40	theme	essential	306:314	arg1	prestin					292:298	The membrane protein prestin	271:298	The membrane protein prestin	271:298	The membrane protein prestin is an essential component of the membrane-based motor driving electromotility changes (electromotility) in the outer hair cell (OHC), a central process in auditory transduction.
19898896	8	41	theme	WT	1495:1496	arg1	prestin					1498:1504	WT prestin	1495:1504	WT prestin	1495:1504	In contrast to WT prestin, prestin(NN163/166AA) shows a significant cholesterol-dependent decrease in cell-surface expression, which may explain the loss of NLC function.
19898896	7	42	theme	cholesterol-dependent	1436:1456	arg1	trafficking					1467:1477	cholesterol-dependent cellular trafficking	1436:1477	cholesterol-dependent cellular trafficking	1436:1477	In an attempt to explain this finding, we discovered that both WT prestin and prestin(NN163/166AA) participate in cholesterol-dependent cellular trafficking.
19898896	6	43	theme	increased	1151:1159	arg1	cholesterol					1170:1180	increased membrane cholesterol	1151:1180	increased membrane cholesterol	1151:1180	However, in the presence of increased membrane cholesterol, unlike the hyperpolarizing shift in NLC seen with WT prestin, cells expressing prestin(NN163/166AA) exhibit a linear capacitance function.
19898896	2	44	theme	hair	417:420	arg1	process					444:450	a central process	434:450	a central process in auditory transduction	434:475	The membrane protein prestin is an essential component of the membrane-based motor driving electromotility changes (electromotility) in the outer hair cell (OHC), a central process in auditory transduction.
19898896	2	44	theme	hair	417:420	arg1	OHC					428:430	OHC	428:430	OHC	428:430	The membrane protein prestin is an essential component of the membrane-based motor driving electromotility changes (electromotility) in the outer hair cell (OHC), a central process in auditory transduction.
19898896	2	44	theme	hair	417:420	arg1	cell					422:425	the outer hair cell	407:425	the outer hair cell (OHC)	407:431	The membrane protein prestin is an essential component of the membrane-based motor driving electromotility changes (electromotility) in the outer hair cell (OHC), a central process in auditory transduction.
19898896	10	45	from	role	1845:1848	arg1	function					1898:1905	prestin function	1890:1905	prestin function	1890:1905	These observations are the first to implicate a regulatory role for cellular trafficking and sorting in prestin function.
19898896	5	46	theme	prestin	1020:1026	arg1	oligomerization					1001:1015	oligomerization	1001:1015	oligomerization of prestin	1001:1026	In addition, unlike WT prestin that readily forms oligomers, prestin(NN163/166AA) is enriched as monomers and more mobile in the plasma membrane, suggesting that oligomerization of prestin is dependent on glycosylation but is not essential for the generation of NLC in HEK 293 cells.
19898896	11	47	from	microdomains	2029:2040	arg1	localization					1979:1990	localization	1979:1990	localization	1979:1990	We speculate that the cholesterol regulation of prestin occurs through localization to and internalization from membrane microdomains by clathrin- and caveolin-dependent mechanisms.
19898896	11	47	from	microdomains	2029:2040	arg1	internalization					1999:2013	internalization	1999:2013	internalization	1999:2013	We speculate that the cholesterol regulation of prestin occurs through localization to and internalization from membrane microdomains by clathrin- and caveolin-dependent mechanisms.
19898896	5	48	theme	NLC	1101:1103	arg1	generation					1087:1096	the generation	1083:1096	the generation of NLC in HEK 293 cells	1083:1120	In addition, unlike WT prestin that readily forms oligomers, prestin(NN163/166AA) is enriched as monomers and more mobile in the plasma membrane, suggesting that oligomerization of prestin is dependent on glycosylation but is not essential for the generation of NLC in HEK 293 cells.
19898896	2	49	theme	auditory	455:462	arg1	transduction					464:475	auditory transduction	455:475	auditory transduction	455:475	The membrane protein prestin is an essential component of the membrane-based motor driving electromotility changes (electromotility) in the outer hair cell (OHC), a central process in auditory transduction.
19898896	9	50	theme	cellular	1740:1747	arg1	trafficking					1749:1759	cellular trafficking	1740:1759	cellular trafficking	1740:1759	Based on our observations, we conclude that glycosylation regulates self-association and cellular trafficking of prestin(NN163/166AA).
19898896	6	51	theme	WT	1233:1234	arg1	prestin					1236:1242	WT prestin	1233:1242	WT prestin	1233:1242	However, in the presence of increased membrane cholesterol, unlike the hyperpolarizing shift in NLC seen with WT prestin, cells expressing prestin(NN163/166AA) exhibit a linear capacitance function.
19898896	4	52	theme	untreated	784:792	arg1	model					832:836	the untreated and cholesterol-depleted HEK 293 cell model	780:836	the untreated and cholesterol-depleted HEK 293 cell model	780:836	Here, we show that the double mutant prestin(NN163/166AA) is not glycosylated and shows the expected NLC properties in the untreated and cholesterol-depleted HEK 293 cell model.
19898896	2	53	theme	electromotility	362:376	arg1	electromotility					387:401	electromotility	387:401	electromotility	387:401	The membrane protein prestin is an essential component of the membrane-based motor driving electromotility changes (electromotility) in the outer hair cell (OHC), a central process in auditory transduction.
19898896	2	53	theme	electromotility	362:376	arg1	changes					378:384	electromotility changes	362:384	electromotility changes (electromotility) in the outer hair cell (OHC), a central process in auditory transduction	362:475	The membrane protein prestin is an essential component of the membrane-based motor driving electromotility changes (electromotility) in the outer hair cell (OHC), a central process in auditory transduction.
19898896	1	54	gly	Glycosylation	51:63	arg1	degradation					201:211	degradation	201:211	degradation	201:211	Glycosylation is a common post-translational modification of proteins and is implicated in a variety of cellular functions including protein folding, degradation, sorting and trafficking, and membrane protein recycling.
19898896	1	54	gly	Glycosylation	51:63	arg1	functions					164:172	cellular functions	155:172	cellular functions including protein folding, degradation, sorting and trafficking, and membrane protein recycling	155:268	Glycosylation is a common post-translational modification of proteins and is implicated in a variety of cellular functions including protein folding, degradation, sorting and trafficking, and membrane protein recycling.
19898896	1	54	gly	Glycosylation	51:63	arg1	sorting					214:220	sorting	214:220	sorting	214:220	Glycosylation is a common post-translational modification of proteins and is implicated in a variety of cellular functions including protein folding, degradation, sorting and trafficking, and membrane protein recycling.
19898896	1	54	gly	Glycosylation	51:63	arg1	recycling					260:268	membrane protein recycling	243:268	membrane protein recycling	243:268	Glycosylation is a common post-translational modification of proteins and is implicated in a variety of cellular functions including protein folding, degradation, sorting and trafficking, and membrane protein recycling.
19898896	1	54	gly	Glycosylation	51:63	arg1	variety					144:150	a variety	142:150	a variety of cellular functions including protein folding, degradation, sorting and trafficking, and membrane protein recycling	142:268	Glycosylation is a common post-translational modification of proteins and is implicated in a variety of cellular functions including protein folding, degradation, sorting and trafficking, and membrane protein recycling.
19898896	1	54	gly	Glycosylation	51:63	arg1	folding					192:198	protein folding	184:198	protein folding	184:198	Glycosylation is a common post-translational modification of proteins and is implicated in a variety of cellular functions including protein folding, degradation, sorting and trafficking, and membrane protein recycling.
19898896	7	55	theme	WT	1385:1386	arg1	prestin					1388:1394	WT prestin	1385:1394	WT prestin	1385:1394	In an attempt to explain this finding, we discovered that both WT prestin and prestin(NN163/166AA) participate in cholesterol-dependent cellular trafficking.
19898896	5	56	theme	plasma	968:973	arg1	membrane					975:982	the plasma membrane	964:982	the plasma membrane	964:982	In addition, unlike WT prestin that readily forms oligomers, prestin(NN163/166AA) is enriched as monomers and more mobile in the plasma membrane, suggesting that oligomerization of prestin is dependent on glycosylation but is not essential for the generation of NLC in HEK 293 cells.
19898896	4	57	theme	expected	753:760	arg1	properties					766:775	the expected NLC properties	749:775	the expected NLC properties in the untreated and cholesterol-depleted HEK 293 cell model	749:836	Here, we show that the double mutant prestin(NN163/166AA) is not glycosylated and shows the expected NLC properties in the untreated and cholesterol-depleted HEK 293 cell model.
19898896	3	58	theme	nonlinear	605:613	arg1	NLC					628:630	NLC	628:630	NLC	628:630	Prestin was earlier identified to possess two N-glycosylation sites (N163, N166) that, when mutated, marginally affect prestin nonlinear capacitance (NLC) function in cultured cells.
19898896	3	58	theme	nonlinear	605:613	arg1	capacitance					615:625	prestin nonlinear capacitance	597:625	prestin nonlinear capacitance (NLC) function in cultured cells	597:658	Prestin was earlier identified to possess two N-glycosylation sites (N163, N166) that, when mutated, marginally affect prestin nonlinear capacitance (NLC) function in cultured cells.
19898896	2	59	theme	membrane	275:282	arg1	component					316:324	an essential component	303:324	an essential component of the membrane-based motor driving electromotility changes (electromotility) in the outer hair cell (OHC), a central process in auditory transduction	303:475	The membrane protein prestin is an essential component of the membrane-based motor driving electromotility changes (electromotility) in the outer hair cell (OHC), a central process in auditory transduction.
19898896	2	59	theme	membrane	275:282	arg1	prestin					292:298	The membrane protein prestin	271:298	The membrane protein prestin	271:298	The membrane protein prestin is an essential component of the membrane-based motor driving electromotility changes (electromotility) in the outer hair cell (OHC), a central process in auditory transduction.
19898896	4	60	from	properties	766:775	arg1	model					832:836	the untreated and cholesterol-depleted HEK 293 cell model	780:836	the untreated and cholesterol-depleted HEK 293 cell model	780:836	Here, we show that the double mutant prestin(NN163/166AA) is not glycosylated and shows the expected NLC properties in the untreated and cholesterol-depleted HEK 293 cell model.
19898896	2	61	theme	motor	348:352	arg1	component					316:324	an essential component	303:324	an essential component of the membrane-based motor driving electromotility changes (electromotility) in the outer hair cell (OHC), a central process in auditory transduction	303:475	The membrane protein prestin is an essential component of the membrane-based motor driving electromotility changes (electromotility) in the outer hair cell (OHC), a central process in auditory transduction.
19898896	2	61	theme	motor	348:352	arg1	prestin					292:298	The membrane protein prestin	271:298	The membrane protein prestin	271:298	The membrane protein prestin is an essential component of the membrane-based motor driving electromotility changes (electromotility) in the outer hair cell (OHC), a central process in auditory transduction.
19898896	8	62	theme	cholesterol-dependent	1548:1568	arg1	decrease					1570:1577	a significant cholesterol-dependent decrease	1534:1577	a significant cholesterol-dependent decrease in cell-surface expression, which may explain the loss of NLC function	1534:1648	In contrast to WT prestin, prestin(NN163/166AA) shows a significant cholesterol-dependent decrease in cell-surface expression, which may explain the loss of NLC function.
19898896	11	63	theme	membrane	2020:2027	arg1	microdomains					2029:2040	membrane microdomains	2020:2040	membrane microdomains	2020:2040	We speculate that the cholesterol regulation of prestin occurs through localization to and internalization from membrane microdomains by clathrin- and caveolin-dependent mechanisms.
19898896	3	64	theme	capacitance	615:625	arg1	function					633:640	prestin nonlinear capacitance (NLC) function	597:640	prestin nonlinear capacitance (NLC) function in cultured cells	597:658	Prestin was earlier identified to possess two N-glycosylation sites (N163, N166) that, when mutated, marginally affect prestin nonlinear capacitance (NLC) function in cultured cells.
19898896	2	65	theme	membrane-based	333:346	arg1	motor					348:352	the membrane-based motor	329:352	the membrane-based motor driving electromotility changes (electromotility) in the outer hair cell (OHC), a central process in auditory transduction	329:475	The membrane protein prestin is an essential component of the membrane-based motor driving electromotility changes (electromotility) in the outer hair cell (OHC), a central process in auditory transduction.
19898896	8	66	theme	cell-surface	1582:1593	arg1	expression					1595:1604	cell-surface expression	1582:1604	cell-surface expression	1582:1604	In contrast to WT prestin, prestin(NN163/166AA) shows a significant cholesterol-dependent decrease in cell-surface expression, which may explain the loss of NLC function.
19898896	4	67	theme	mutant	691:696	arg1	NN163/166AA					706:716	NN163/166AA	706:716	NN163/166AA	706:716	Here, we show that the double mutant prestin(NN163/166AA) is not glycosylated and shows the expected NLC properties in the untreated and cholesterol-depleted HEK 293 cell model.
19898896	4	67	theme	mutant	691:696	arg1	prestin					698:704	the double mutant prestin	680:704	the double mutant prestin(NN163/166AA)	680:717	Here, we show that the double mutant prestin(NN163/166AA) is not glycosylated and shows the expected NLC properties in the untreated and cholesterol-depleted HEK 293 cell model.
19898896	6	68	theme	capacitance	1300:1310	arg1	function					1312:1319	a linear capacitance function	1291:1319	a linear capacitance function	1291:1319	However, in the presence of increased membrane cholesterol, unlike the hyperpolarizing shift in NLC seen with WT prestin, cells expressing prestin(NN163/166AA) exhibit a linear capacitance function.
19898896	3	69	theme	cultured	645:652	arg1	cells					654:658	cultured cells	645:658	cultured cells	645:658	Prestin was earlier identified to possess two N-glycosylation sites (N163, N166) that, when mutated, marginally affect prestin nonlinear capacitance (NLC) function in cultured cells.
19898896	4	70	theme	NLC	762:764	arg1	properties					766:775	the expected NLC properties	749:775	the expected NLC properties in the untreated and cholesterol-depleted HEK 293 cell model	749:836	Here, we show that the double mutant prestin(NN163/166AA) is not glycosylated and shows the expected NLC properties in the untreated and cholesterol-depleted HEK 293 cell model.
19898896	6	71	from	shift	1210:1214	arg1	NLC					1219:1221	NLC	1219:1221	NLC seen with WT prestin	1219:1242	However, in the presence of increased membrane cholesterol, unlike the hyperpolarizing shift in NLC seen with WT prestin, cells expressing prestin(NN163/166AA) exhibit a linear capacitance function.
19898896	1	72	theme	membrane	243:250	arg1	recycling					260:268	membrane protein recycling	243:268	membrane protein recycling	243:268	Glycosylation is a common post-translational modification of proteins and is implicated in a variety of cellular functions including protein folding, degradation, sorting and trafficking, and membrane protein recycling.
19898896	6	73	theme	linear	1293:1298	arg1	function					1312:1319	a linear capacitance function	1291:1319	a linear capacitance function	1291:1319	However, in the presence of increased membrane cholesterol, unlike the hyperpolarizing shift in NLC seen with WT prestin, cells expressing prestin(NN163/166AA) exhibit a linear capacitance function.
19898896	3	74	contain	possess	512:518	arg2	sites					540:544	two N-glycosylation sites	520:544	two N-glycosylation sites (N163, N166) that, when mutated, marginally affect prestin nonlinear capacitance (NLC) function in cultured cells	520:658	Prestin was earlier identified to possess two N-glycosylation sites (N163, N166) that, when mutated, marginally affect prestin nonlinear capacitance (NLC) function in cultured cells.
19898896	3	74	contain	possess	512:518	arg1	Prestin					478:484	Prestin	478:484	Prestin	478:484	Prestin was earlier identified to possess two N-glycosylation sites (N163, N166) that, when mutated, marginally affect prestin nonlinear capacitance (NLC) function in cultured cells.
19898896	3	74	contain	possess	512:518	arg2	N166					553:556	N166	553:556	N166	553:556	Prestin was earlier identified to possess two N-glycosylation sites (N163, N166) that, when mutated, marginally affect prestin nonlinear capacitance (NLC) function in cultured cells.
19898896	3	75	theme	prestin	597:603	arg1	NLC					628:630	NLC	628:630	NLC	628:630	Prestin was earlier identified to possess two N-glycosylation sites (N163, N166) that, when mutated, marginally affect prestin nonlinear capacitance (NLC) function in cultured cells.
19898896	3	75	theme	prestin	597:603	arg1	capacitance					615:625	prestin nonlinear capacitance	597:625	prestin nonlinear capacitance (NLC) function in cultured cells	597:658	Prestin was earlier identified to possess two N-glycosylation sites (N163, N166) that, when mutated, marginally affect prestin nonlinear capacitance (NLC) function in cultured cells.
19898896	1	76	theme	cellular	155:162	arg1	sorting					214:220	sorting	214:220	sorting	214:220	Glycosylation is a common post-translational modification of proteins and is implicated in a variety of cellular functions including protein folding, degradation, sorting and trafficking, and membrane protein recycling.
19898896	1	76	theme	cellular	155:162	arg1	degradation					201:211	degradation	201:211	degradation	201:211	Glycosylation is a common post-translational modification of proteins and is implicated in a variety of cellular functions including protein folding, degradation, sorting and trafficking, and membrane protein recycling.
19898896	1	76	theme	cellular	155:162	arg1	functions					164:172	cellular functions	155:172	cellular functions including protein folding, degradation, sorting and trafficking, and membrane protein recycling	155:268	Glycosylation is a common post-translational modification of proteins and is implicated in a variety of cellular functions including protein folding, degradation, sorting and trafficking, and membrane protein recycling.
19898896	1	76	theme	cellular	155:162	arg1	folding					192:198	protein folding	184:198	protein folding	184:198	Glycosylation is a common post-translational modification of proteins and is implicated in a variety of cellular functions including protein folding, degradation, sorting and trafficking, and membrane protein recycling.
19898896	1	76	theme	cellular	155:162	arg1	recycling					260:268	membrane protein recycling	243:268	membrane protein recycling	243:268	Glycosylation is a common post-translational modification of proteins and is implicated in a variety of cellular functions including protein folding, degradation, sorting and trafficking, and membrane protein recycling.
19898896	8	77	theme	significant	1536:1546	arg1	decrease					1570:1577	a significant cholesterol-dependent decrease	1534:1577	a significant cholesterol-dependent decrease in cell-surface expression, which may explain the loss of NLC function	1534:1648	In contrast to WT prestin, prestin(NN163/166AA) shows a significant cholesterol-dependent decrease in cell-surface expression, which may explain the loss of NLC function.
19898896	1	78	theme	protein	252:258	arg1	recycling					260:268	membrane protein recycling	243:268	membrane protein recycling	243:268	Glycosylation is a common post-translational modification of proteins and is implicated in a variety of cellular functions including protein folding, degradation, sorting and trafficking, and membrane protein recycling.
17714874	0	0	theme	glycation	85:93	arg1	endproducts					95:105	advanced glycation endproducts	76:105	advanced glycation endproducts	76:105	De-N-glycosylation or G82S mutation of RAGE sensitizes its interaction with advanced glycation endproducts.
17714874	2	1	gly	N-glycosylation	287:301	arg2	sites					303:307	two N-glycosylation sites	283:307	two N-glycosylation sites	283:307	RAGE has two N-glycosylation sites in and near the AGE-binding domain, and G82S mutation in the second N-glycosylation motif was recently reported in human.
17714874	2	1	gly	N-glycosylation	287:301	arg2	two					283:285	two	283:285	two	283:285	RAGE has two N-glycosylation sites in and near the AGE-binding domain, and G82S mutation in the second N-glycosylation motif was recently reported in human.
17714874	7	2	theme	RAGE-expressing	1157:1171	arg1	cells					1173:1177	wild-type RAGE-expressing cells	1147:1177	wild-type RAGE-expressing cells	1147:1177	Exposure to low glucose resulted in the appearance of RAGE proteins of deglycosylated size in wild-type RAGE-expressing cells and significantly enhanced glycolaldehyde-derived AGE-induced VEGF mRNA expression.
17714874	6	3	theme	wild-type	1032:1040	arg1	expressor					1042:1050	wild-type expressor	1032:1050	wild-type expressor	1032:1050	AGE-induced upregulation of VEGF mRNA was significantly augmented in endothelial cell-derived ECV304 cells expressing de-N-glycosylated and G82S RAGE when compared with wild-type expressor.
17714874	0	4	theme	advanced	76:83	arg1	endproducts					95:105	advanced glycation endproducts	76:105	advanced glycation endproducts	76:105	De-N-glycosylation or G82S mutation of RAGE sensitizes its interaction with advanced glycation endproducts.
17714874	1	5	theme	diabetic	241:248	arg1	complications					259:271	diabetic vascular complications	241:271	diabetic vascular complications	241:271	Interactions between advanced glycation endproducts (AGE) and the receptor for AGE (RAGE) have been implicated in the development of diabetic vascular complications.
17714874	6	6	link	cell-derived	944:955	arg1	cells					964:968	endothelial cell-derived ECV304 cells	932:968	endothelial cell-derived ECV304 cells expressing de-N-glycosylated and G82S RAGE	932:1011	AGE-induced upregulation of VEGF mRNA was significantly augmented in endothelial cell-derived ECV304 cells expressing de-N-glycosylated and G82S RAGE when compared with wild-type expressor.
17714874	1	7	theme	vascular	250:257	arg1	complications					259:271	diabetic vascular complications	241:271	diabetic vascular complications	241:271	Interactions between advanced glycation endproducts (AGE) and the receptor for AGE (RAGE) have been implicated in the development of diabetic vascular complications.
17714874	7	8	theme	wild-type	1147:1155	arg1	cells					1173:1177	wild-type RAGE-expressing cells	1147:1177	wild-type RAGE-expressing cells	1147:1177	Exposure to low glucose resulted in the appearance of RAGE proteins of deglycosylated size in wild-type RAGE-expressing cells and significantly enhanced glycolaldehyde-derived AGE-induced VEGF mRNA expression.
17714874	4	9	gly	de-N-glycosylation	585:602	arg1	cells					650:654	COS-7 cells	644:654	COS-7 cells	644:654	Recombinant wild-type, de-N-glycosylation and G82S RAGE proteins were produced in COS-7 cells, purified and assayed for ligand-binding abilities.
17714874	1	10	theme	complications	259:271	arg1	development					226:236	the development	222:236	the development of diabetic vascular complications	222:271	Interactions between advanced glycation endproducts (AGE) and the receptor for AGE (RAGE) have been implicated in the development of diabetic vascular complications.
17714874	4	11	theme	ligand-binding	682:695	arg1	abilities					697:705	ligand-binding abilities	682:705	ligand-binding abilities	682:705	Recombinant wild-type, de-N-glycosylation and G82S RAGE proteins were produced in COS-7 cells, purified and assayed for ligand-binding abilities.
17714874	7	12	theme	VEGF	1241:1244	arg1	expression					1251:1260	glycolaldehyde-derived AGE-induced VEGF mRNA expression	1206:1260	glycolaldehyde-derived AGE-induced VEGF mRNA expression	1206:1260	Exposure to low glucose resulted in the appearance of RAGE proteins of deglycosylated size in wild-type RAGE-expressing cells and significantly enhanced glycolaldehyde-derived AGE-induced VEGF mRNA expression.
17714874	0	13	with	interaction	59:69	arg1	endproducts					95:105	advanced glycation endproducts	76:105	advanced glycation endproducts	76:105	De-N-glycosylation or G82S mutation of RAGE sensitizes its interaction with advanced glycation endproducts.
17714874	2	14	theme	N-glycosylation	377:391	arg1	motif					393:397	the second N-glycosylation motif	366:397	the second N-glycosylation motif	366:397	RAGE has two N-glycosylation sites in and near the AGE-binding domain, and G82S mutation in the second N-glycosylation motif was recently reported in human.
17714874	6	15	theme	VEGF	891:894	arg1	mRNA					896:899	VEGF mRNA	891:899	VEGF mRNA	891:899	AGE-induced upregulation of VEGF mRNA was significantly augmented in endothelial cell-derived ECV304 cells expressing de-N-glycosylated and G82S RAGE when compared with wild-type expressor.
17714874	2	16	gly	N-glycosylation	377:391	arg2	motif					393:397	the second N-glycosylation motif	366:397	the second N-glycosylation motif	366:397	RAGE has two N-glycosylation sites in and near the AGE-binding domain, and G82S mutation in the second N-glycosylation motif was recently reported in human.
17714874	2	17	theme	second	370:375	arg1	motif					393:397	the second N-glycosylation motif	366:397	the second N-glycosylation motif	366:397	RAGE has two N-glycosylation sites in and near the AGE-binding domain, and G82S mutation in the second N-glycosylation motif was recently reported in human.
17714874	7	18	theme	mRNA	1246:1249	arg1	expression					1251:1260	glycolaldehyde-derived AGE-induced VEGF mRNA expression	1206:1260	glycolaldehyde-derived AGE-induced VEGF mRNA expression	1206:1260	Exposure to low glucose resulted in the appearance of RAGE proteins of deglycosylated size in wild-type RAGE-expressing cells and significantly enhanced glycolaldehyde-derived AGE-induced VEGF mRNA expression.
17714874	7	19	theme	proteins	1112:1119	arg1	appearance					1093:1102	the appearance	1089:1102	the appearance of RAGE proteins of deglycosylated size	1089:1142	Exposure to low glucose resulted in the appearance of RAGE proteins of deglycosylated size in wild-type RAGE-expressing cells and significantly enhanced glycolaldehyde-derived AGE-induced VEGF mRNA expression.
17714874	3	20	theme	cellular	536:543	arg1	response					545:552	cellular response	536:552	cellular response to AGE	536:559	In this study, we examined whether de-N-glycosylation or G82S of RAGE affect its ability to bind AGE and cellular response to AGE.
17714874	6	21	theme	mRNA	896:899	arg1	upregulation					875:886	AGE-induced upregulation	863:886	AGE-induced upregulation of VEGF mRNA	863:899	AGE-induced upregulation of VEGF mRNA was significantly augmented in endothelial cell-derived ECV304 cells expressing de-N-glycosylated and G82S RAGE when compared with wild-type expressor.
17714874	2	22	from	mutation	354:361	arg1	motif					393:397	the second N-glycosylation motif	366:397	the second N-glycosylation motif	366:397	RAGE has two N-glycosylation sites in and near the AGE-binding domain, and G82S mutation in the second N-glycosylation motif was recently reported in human.
17714874	3	23	gly	de-N-glycosylation	466:483	arg1	RAGE					496:499	RAGE	496:499	RAGE	496:499	In this study, we examined whether de-N-glycosylation or G82S of RAGE affect its ability to bind AGE and cellular response to AGE.
17714874	4	24	theme	COS-7	644:648	arg1	cells					650:654	COS-7 cells	644:654	COS-7 cells	644:654	Recombinant wild-type, de-N-glycosylation and G82S RAGE proteins were produced in COS-7 cells, purified and assayed for ligand-binding abilities.
17714874	7	25	theme	AGE-induced	1229:1239	arg1	expression					1251:1260	glycolaldehyde-derived AGE-induced VEGF mRNA expression	1206:1260	glycolaldehyde-derived AGE-induced VEGF mRNA expression	1206:1260	Exposure to low glucose resulted in the appearance of RAGE proteins of deglycosylated size in wild-type RAGE-expressing cells and significantly enhanced glycolaldehyde-derived AGE-induced VEGF mRNA expression.
17714874	7	26	link	glycolaldehyde-derived	1206:1227	arg1	expression					1251:1260	glycolaldehyde-derived AGE-induced VEGF mRNA expression	1206:1260	glycolaldehyde-derived AGE-induced VEGF mRNA expression	1206:1260	Exposure to low glucose resulted in the appearance of RAGE proteins of deglycosylated size in wild-type RAGE-expressing cells and significantly enhanced glycolaldehyde-derived AGE-induced VEGF mRNA expression.
17714874	7	27	theme	size	1139:1142	arg1	appearance					1093:1102	the appearance	1089:1102	the appearance of RAGE proteins of deglycosylated size	1089:1142	Exposure to low glucose resulted in the appearance of RAGE proteins of deglycosylated size in wild-type RAGE-expressing cells and significantly enhanced glycolaldehyde-derived AGE-induced VEGF mRNA expression.
17714874	4	28	theme	RAGE	613:616	arg1	proteins					618:625	G82S RAGE proteins	608:625	G82S RAGE proteins	608:625	Recombinant wild-type, de-N-glycosylation and G82S RAGE proteins were produced in COS-7 cells, purified and assayed for ligand-binding abilities.
17714874	5	29	gly	De-N-glycosylation	708:725	arg1	N81					730:732	N81	730:732	N81	730:732	De-N-glycosylation at N81 and G82S mutation decreased Kd for glycolaldehyde-derived AGE to three orders of magnitude lower levels compared with wild-type.
17714874	5	29	gly	De-N-glycosylation	708:725	arg1	mutation					743:750	G82S mutation	738:750	G82S mutation	738:750	De-N-glycosylation at N81 and G82S mutation decreased Kd for glycolaldehyde-derived AGE to three orders of magnitude lower levels compared with wild-type.
17714874	5	29	gly	De-N-glycosylation	708:725	arg2	mutation					743:750	G82S mutation	738:750	G82S mutation	738:750	De-N-glycosylation at N81 and G82S mutation decreased Kd for glycolaldehyde-derived AGE to three orders of magnitude lower levels compared with wild-type.
17714874	5	29	gly	De-N-glycosylation	708:725	arg2	N81					730:732	N81	730:732	N81	730:732	De-N-glycosylation at N81 and G82S mutation decreased Kd for glycolaldehyde-derived AGE to three orders of magnitude lower levels compared with wild-type.
17714874	2	30	contain	has	279:281	arg2	sites					303:307	two N-glycosylation sites	283:307	two N-glycosylation sites	283:307	RAGE has two N-glycosylation sites in and near the AGE-binding domain, and G82S mutation in the second N-glycosylation motif was recently reported in human.
17714874	2	30	contain	has	279:281	arg1	RAGE					274:277	RAGE	274:277	RAGE	274:277	RAGE has two N-glycosylation sites in and near the AGE-binding domain, and G82S mutation in the second N-glycosylation motif was recently reported in human.
17714874	7	31	theme	RAGE	1107:1110	arg1	proteins					1112:1119	RAGE proteins	1107:1119	RAGE proteins	1107:1119	Exposure to low glucose resulted in the appearance of RAGE proteins of deglycosylated size in wild-type RAGE-expressing cells and significantly enhanced glycolaldehyde-derived AGE-induced VEGF mRNA expression.
17714874	5	32	from	N81	730:732	arg1	De-N-glycosylation					708:725	De-N-glycosylation	708:725	De-N-glycosylation at N81 and G82S mutation	708:750	De-N-glycosylation at N81 and G82S mutation decreased Kd for glycolaldehyde-derived AGE to three orders of magnitude lower levels compared with wild-type.
17714874	2	33	theme	N-glycosylation	287:301	arg1	sites					303:307	two N-glycosylation sites	283:307	two N-glycosylation sites	283:307	RAGE has two N-glycosylation sites in and near the AGE-binding domain, and G82S mutation in the second N-glycosylation motif was recently reported in human.
17714874	4	34	theme	G82S	608:611	arg1	proteins					618:625	G82S RAGE proteins	608:625	G82S RAGE proteins	608:625	Recombinant wild-type, de-N-glycosylation and G82S RAGE proteins were produced in COS-7 cells, purified and assayed for ligand-binding abilities.
17714874	0	35	theme	RAGE	39:42	arg1	G82S					22:25	G82S	22:25	G82S	22:25	De-N-glycosylation or G82S mutation of RAGE sensitizes its interaction with advanced glycation endproducts.
17714874	0	35	theme	RAGE	39:42	arg1	De-N-glycosylation					0:17	De-N-glycosylation	0:17	De-N-glycosylation	0:17	De-N-glycosylation or G82S mutation of RAGE sensitizes its interaction with advanced glycation endproducts.
17714874	2	36	theme	AGE-binding	325:335	arg1	domain					337:342	the AGE-binding domain	321:342	the AGE-binding domain	321:342	RAGE has two N-glycosylation sites in and near the AGE-binding domain, and G82S mutation in the second N-glycosylation motif was recently reported in human.
17714874	6	37	theme	AGE-induced	863:873	arg1	upregulation					875:886	AGE-induced upregulation	863:886	AGE-induced upregulation of VEGF mRNA	863:899	AGE-induced upregulation of VEGF mRNA was significantly augmented in endothelial cell-derived ECV304 cells expressing de-N-glycosylated and G82S RAGE when compared with wild-type expressor.
17714874	0	38	gly	De-N-glycosylation	0:17	arg1	RAGE					39:42	RAGE	39:42	RAGE	39:42	De-N-glycosylation or G82S mutation of RAGE sensitizes its interaction with advanced glycation endproducts.
17714874	8	39	theme	AGE	1330:1332	arg1	ligands					1334:1340	AGE ligands	1330:1340	AGE ligands	1330:1340	De-N-glycosylation or G82S mutation of RAGE increases affinity for AGE ligands, and may sensitize cells or conditions with it to AGE.
17714874	5	40	theme	glycolaldehyde-derived	769:790	arg1	AGE					792:794	glycolaldehyde-derived AGE	769:794	glycolaldehyde-derived AGE	769:794	De-N-glycosylation at N81 and G82S mutation decreased Kd for glycolaldehyde-derived AGE to three orders of magnitude lower levels compared with wild-type.
17714874	7	41	theme	glycolaldehyde-derived	1206:1227	arg1	expression					1251:1260	glycolaldehyde-derived AGE-induced VEGF mRNA expression	1206:1260	glycolaldehyde-derived AGE-induced VEGF mRNA expression	1206:1260	Exposure to low glucose resulted in the appearance of RAGE proteins of deglycosylated size in wild-type RAGE-expressing cells and significantly enhanced glycolaldehyde-derived AGE-induced VEGF mRNA expression.
17714874	8	42	theme	G82S	1285:1288	arg1	mutation					1290:1297	De-N-glycosylation or G82S mutation	1263:1297	De-N-glycosylation or G82S mutation of RAGE	1263:1305	De-N-glycosylation or G82S mutation of RAGE increases affinity for AGE ligands, and may sensitize cells or conditions with it to AGE.
17714874	8	43	theme	De-N-glycosylation	1263:1280	arg1	mutation					1290:1297	De-N-glycosylation or G82S mutation	1263:1297	De-N-glycosylation or G82S mutation of RAGE	1263:1305	De-N-glycosylation or G82S mutation of RAGE increases affinity for AGE ligands, and may sensitize cells or conditions with it to AGE.
17714874	8	44	with	cells	1361:1365	arg1	it					1386:1387	it	1386:1387	it	1386:1387	De-N-glycosylation or G82S mutation of RAGE increases affinity for AGE ligands, and may sensitize cells or conditions with it to AGE.
17714874	1	45	theme	advanced	129:136	arg1	endproducts					148:158	advanced glycation endproducts	129:158	advanced glycation endproducts (AGE)	129:164	Interactions between advanced glycation endproducts (AGE) and the receptor for AGE (RAGE) have been implicated in the development of diabetic vascular complications.
17714874	1	45	theme	advanced	129:136	arg1	AGE					161:163	AGE	161:163	AGE	161:163	Interactions between advanced glycation endproducts (AGE) and the receptor for AGE (RAGE) have been implicated in the development of diabetic vascular complications.
17714874	8	46	theme	RAGE	1302:1305	arg1	mutation					1290:1297	De-N-glycosylation or G82S mutation	1263:1297	De-N-glycosylation or G82S mutation of RAGE	1263:1305	De-N-glycosylation or G82S mutation of RAGE increases affinity for AGE ligands, and may sensitize cells or conditions with it to AGE.
17714874	6	47	theme	ECV304	957:962	arg1	cells					964:968	endothelial cell-derived ECV304 cells	932:968	endothelial cell-derived ECV304 cells expressing de-N-glycosylated and G82S RAGE	932:1011	AGE-induced upregulation of VEGF mRNA was significantly augmented in endothelial cell-derived ECV304 cells expressing de-N-glycosylated and G82S RAGE when compared with wild-type expressor.
17714874	5	48	link	glycolaldehyde-derived	769:790	arg1	AGE					792:794	glycolaldehyde-derived AGE	769:794	glycolaldehyde-derived AGE	769:794	De-N-glycosylation at N81 and G82S mutation decreased Kd for glycolaldehyde-derived AGE to three orders of magnitude lower levels compared with wild-type.
17714874	1	49	theme	glycation	138:146	arg1	endproducts					148:158	advanced glycation endproducts	129:158	advanced glycation endproducts (AGE)	129:164	Interactions between advanced glycation endproducts (AGE) and the receptor for AGE (RAGE) have been implicated in the development of diabetic vascular complications.
17714874	1	49	theme	glycation	138:146	arg1	AGE					161:163	AGE	161:163	AGE	161:163	Interactions between advanced glycation endproducts (AGE) and the receptor for AGE (RAGE) have been implicated in the development of diabetic vascular complications.
17714874	6	50	theme	cell-derived	944:955	arg1	cells					964:968	endothelial cell-derived ECV304 cells	932:968	endothelial cell-derived ECV304 cells expressing de-N-glycosylated and G82S RAGE	932:1011	AGE-induced upregulation of VEGF mRNA was significantly augmented in endothelial cell-derived ECV304 cells expressing de-N-glycosylated and G82S RAGE when compared with wild-type expressor.
17714874	7	51	theme	low	1065:1067	arg1	glucose					1069:1075	low glucose	1065:1075	low glucose	1065:1075	Exposure to low glucose resulted in the appearance of RAGE proteins of deglycosylated size in wild-type RAGE-expressing cells and significantly enhanced glycolaldehyde-derived AGE-induced VEGF mRNA expression.
17714874	6	52	dep	de-N-glycosylated	981:997	arg1	RAGE					1008:1011	RAGE	1008:1011	RAGE	1008:1011	AGE-induced upregulation of VEGF mRNA was significantly augmented in endothelial cell-derived ECV304 cells expressing de-N-glycosylated and G82S RAGE when compared with wild-type expressor.
17714874	7	53	theme	deglycosylated	1124:1137	arg1	size					1139:1142	deglycosylated size	1124:1142	deglycosylated size	1124:1142	Exposure to low glucose resulted in the appearance of RAGE proteins of deglycosylated size in wild-type RAGE-expressing cells and significantly enhanced glycolaldehyde-derived AGE-induced VEGF mRNA expression.
17714874	5	54	theme	magnitude	815:823	arg1	orders					805:810	three orders	799:810	three orders of magnitude	799:823	De-N-glycosylation at N81 and G82S mutation decreased Kd for glycolaldehyde-derived AGE to three orders of magnitude lower levels compared with wild-type.
17714874	8	55	with	conditions	1370:1379	arg1	it					1386:1387	it	1386:1387	it	1386:1387	De-N-glycosylation or G82S mutation of RAGE increases affinity for AGE ligands, and may sensitize cells or conditions with it to AGE.
17714874	5	56	theme	G82S	738:741	arg1	mutation					743:750	G82S mutation	738:750	G82S mutation	738:750	De-N-glycosylation at N81 and G82S mutation decreased Kd for glycolaldehyde-derived AGE to three orders of magnitude lower levels compared with wild-type.
17714874	5	57	from	mutation	743:750	arg1	De-N-glycosylation					708:725	De-N-glycosylation	708:725	De-N-glycosylation at N81 and G82S mutation	708:750	De-N-glycosylation at N81 and G82S mutation decreased Kd for glycolaldehyde-derived AGE to three orders of magnitude lower levels compared with wild-type.
17714874	5	58	theme	lower	825:829	arg1	levels					831:836	three orders of magnitude lower levels	799:836	three orders of magnitude lower levels	799:836	De-N-glycosylation at N81 and G82S mutation decreased Kd for glycolaldehyde-derived AGE to three orders of magnitude lower levels compared with wild-type.
17714874	3	59	theme	RAGE	496:499	arg1	de-N-glycosylation					466:483	de-N-glycosylation	466:483	de-N-glycosylation	466:483	In this study, we examined whether de-N-glycosylation or G82S of RAGE affect its ability to bind AGE and cellular response to AGE.
17714874	3	59	theme	RAGE	496:499	arg1	G82S					488:491	G82S	488:491	G82S	488:491	In this study, we examined whether de-N-glycosylation or G82S of RAGE affect its ability to bind AGE and cellular response to AGE.
17714874	7	60	gly	deglycosylated	1124:1137	arg1	size					1139:1142	deglycosylated size	1124:1142	deglycosylated size	1124:1142	Exposure to low glucose resulted in the appearance of RAGE proteins of deglycosylated size in wild-type RAGE-expressing cells and significantly enhanced glycolaldehyde-derived AGE-induced VEGF mRNA expression.
17714874	6	61	theme	endothelial	932:942	arg1	cells					964:968	endothelial cell-derived ECV304 cells	932:968	endothelial cell-derived ECV304 cells expressing de-N-glycosylated and G82S RAGE	932:1011	AGE-induced upregulation of VEGF mRNA was significantly augmented in endothelial cell-derived ECV304 cells expressing de-N-glycosylated and G82S RAGE when compared with wild-type expressor.
17714874	0	62	dep	De-N-glycosylation	0:17	arg1	mutation					27:34	mutation	27:34	mutation	27:34	De-N-glycosylation or G82S mutation of RAGE sensitizes its interaction with advanced glycation endproducts.
17714874	2	63	theme	G82S	349:352	arg1	mutation					354:361	G82S mutation	349:361	G82S mutation in the second N-glycosylation motif	349:397	RAGE has two N-glycosylation sites in and near the AGE-binding domain, and G82S mutation in the second N-glycosylation motif was recently reported in human.
27798666	7	0	attach	presence	1121:1128	arg1	NRP1-FS					1140:1146	NRP1-FS	1140:1146	NRP1-FS	1140:1146	As expected, the high molecular weight products appearing as a smear in SDS-PAGE and reflecting the presence of GAG in NRP1-FS were undetectable in the NRP1-Δ7 protein.
27798666	7	0	attach	presence	1121:1128	arg2	GAG					1133:1135	GAG	1133:1135	GAG	1133:1135	As expected, the high molecular weight products appearing as a smear in SDS-PAGE and reflecting the presence of GAG in NRP1-FS were undetectable in the NRP1-Δ7 protein.
27798666	3	1	theme	antagonist	527:536	arg1	properties					538:547	antagonist properties	527:547	antagonist properties	527:547	Its primary mRNA is subjected to alternative splicing mechanisms generating different isoforms, some of which lack the transmembrane domain and display antagonist properties to NRP1 full size (FS).
27798666	9	2	theme	biological	1370:1379	arg1	properties					1381:1390	the biological properties	1366:1390	the biological properties of this isoform	1366:1406	To investigate the biological properties of this isoform, we generated prostatic (PC3) and breast (MDA-MB-231) cancer cells able to express recombinant NRP1-FS or NRP1-Δ7 in a doxycycline-inducible manner.
27798666	8	3	theme	appreciable	1229:1239	arg1	level					1241:1245	an appreciable level	1226:1245	an appreciable level	1226:1245	NRP1-Δ7 mRNA was found expressed at an appreciable level, between 10 and 30% of the total NRP1, by various cells lines and tissues from human and murine origin.
27798666	3	4	theme	full	557:560	arg1	size					562:565	NRP1 full size	552:565	NRP1 full size (FS)	552:570	Its primary mRNA is subjected to alternative splicing mechanisms generating different isoforms, some of which lack the transmembrane domain and display antagonist properties to NRP1 full size (FS).
27798666	3	4	theme	full	557:560	arg1	FS					568:569	FS	568:569	FS	568:569	Its primary mRNA is subjected to alternative splicing mechanisms generating different isoforms, some of which lack the transmembrane domain and display antagonist properties to NRP1 full size (FS).
27798666	9	5	theme	isoform	1400:1406	arg1	properties					1381:1390	the biological properties	1366:1390	the biological properties of this isoform	1366:1406	To investigate the biological properties of this isoform, we generated prostatic (PC3) and breast (MDA-MB-231) cancer cells able to express recombinant NRP1-FS or NRP1-Δ7 in a doxycycline-inducible manner.
27798666	10	6	theme	expected	1739:1746	arg1	effects					1771:1777	the expected opposite "pro-tumoral" effects	1735:1777	the expected opposite "pro-tumoral" effects	1735:1777	Cells with increased expression of NRP1-Δ7 were characterized in vitro by a significant reduction of proliferation, migration and anchorage-independent growth, while NRP1-FS had the expected opposite "pro-tumoral" effects.
27798666	5	7	theme	acids	863:867	arg1	deletion					843:850	a deletion	841:850	a deletion of 7 amino acids occurring two residues downstream of the O-glycosylation site	841:929	Here, we characterized a novel splice variant which has never been investigated, NRP1-Δ7, differing from the NRP1-FS by a deletion of 7 amino acids occurring two residues downstream of the O-glycosylation site.
27798666	12	8	theme	tumors	1940:1945	arg1	vascularization					1957:1971	their vascularization	1951:1971	their vascularization in vivo	1951:1979	Finally, we showed that NRP1-Δ7 inhibited growth of prostatic tumors and their vascularization in vivo.
27798666	12	8	theme	tumors	1940:1945	arg1	growth					1920:1925	growth	1920:1925	growth of prostatic tumors	1920:1945	Finally, we showed that NRP1-Δ7 inhibited growth of prostatic tumors and their vascularization in vivo.
27798666	6	9	theme	aspartic	965:972	arg1	residues					974:981	two aspartic residues	961:981	two aspartic residues critical for efficient glycosylation	961:1018	This short sequence contains two aspartic residues critical for efficient glycosylation.
27798666	2	10	theme	cancer	355:360	arg1	progression					362:372	cancer progression	355:372	cancer progression	355:372	It is involved in axonal development, angiogenesis and cancer progression.
27798666	9	11	theme	prostatic	1422:1430	arg1	PC3					1433:1435	prostatic (PC3) and breast (MDA-MB-231) cancer cells	1422:1473	PC3	1433:1435	To investigate the biological properties of this isoform, we generated prostatic (PC3) and breast (MDA-MB-231) cancer cells able to express recombinant NRP1-FS or NRP1-Δ7 in a doxycycline-inducible manner.
27798666	10	12	theme	increased	1568:1576	arg1	expression					1578:1587	increased expression	1568:1587	increased expression of NRP1-Δ7	1568:1598	Cells with increased expression of NRP1-Δ7 were characterized in vitro by a significant reduction of proliferation, migration and anchorage-independent growth, while NRP1-FS had the expected opposite "pro-tumoral" effects.
27798666	11	13	theme	VEGF-A165	1785:1793	arg1	treatment					1795:1803	VEGF-A165 treatment	1785:1803	VEGF-A165 treatment	1785:1803	Upon VEGF-A165 treatment, a lower internalization rate was observed for NRP1-Δ7 than for NRP1-FS.
27798666	10	14	theme	"	1769:1769	arg1	effects					1771:1777	the expected opposite "pro-tumoral" effects	1735:1777	the expected opposite "pro-tumoral" effects	1735:1777	Cells with increased expression of NRP1-Δ7 were characterized in vitro by a significant reduction of proliferation, migration and anchorage-independent growth, while NRP1-FS had the expected opposite "pro-tumoral" effects.
27798666	6	15	theme	short	937:941	arg1	sequence					943:950	This short sequence	932:950	This short sequence	932:950	This short sequence contains two aspartic residues critical for efficient glycosylation.
27798666	7	16	theme	weight	1053:1058	arg1	undetectable					1153:1164	undetectable	1153:1164	undetectable	1153:1164	As expected, the high molecular weight products appearing as a smear in SDS-PAGE and reflecting the presence of GAG in NRP1-FS were undetectable in the NRP1-Δ7 protein.
27798666	7	16	theme	weight	1053:1058	arg1	products					1060:1067	the high molecular weight products	1034:1067	the high molecular weight products appearing as a smear in SDS-PAGE and reflecting the presence of GAG in NRP1-FS	1034:1146	As expected, the high molecular weight products appearing as a smear in SDS-PAGE and reflecting the presence of GAG in NRP1-FS were undetectable in the NRP1-Δ7 protein.
27798666	8	17	theme	total	1274:1278	arg1	NRP1					1280:1283	the total NRP1	1270:1283	the total NRP1	1270:1283	NRP1-Δ7 mRNA was found expressed at an appreciable level, between 10 and 30% of the total NRP1, by various cells lines and tissues from human and murine origin.
27798666	7	18	theme	high	1038:1041	arg1	weight					1053:1058	high molecular weight	1038:1058	the high molecular weight products appearing as a smear in SDS-PAGE and reflecting the presence of GAG in NRP1-FS	1034:1146	As expected, the high molecular weight products appearing as a smear in SDS-PAGE and reflecting the presence of GAG in NRP1-FS were undetectable in the NRP1-Δ7 protein.
27798666	5	19	theme	site	926:929	arg1	downstream					892:901	downstream	892:901	downstream	892:901	Here, we characterized a novel splice variant which has never been investigated, NRP1-Δ7, differing from the NRP1-FS by a deletion of 7 amino acids occurring two residues downstream of the O-glycosylation site.
27798666	5	20	theme	O-glycosylation	910:924	arg1	site					926:929	the O-glycosylation site	906:929	the O-glycosylation site	906:929	Here, we characterized a novel splice variant which has never been investigated, NRP1-Δ7, differing from the NRP1-FS by a deletion of 7 amino acids occurring two residues downstream of the O-glycosylation site.
27798666	4	21	mod	modified	610:617	arg3	addition					626:633	the addition	622:633	the addition of glycosaminoglycans (GAG) side chains through an O-glycosylation site at serine612	622:718	NRP1 is further post-translationally modified by the addition of glycosaminoglycans (GAG) side chains through an O-glycosylation site at serine612.
27798666	4	21	mod	modified	610:617	arg1	NRP1					573:576	NRP1	573:576	NRP1	573:576	NRP1 is further post-translationally modified by the addition of glycosaminoglycans (GAG) side chains through an O-glycosylation site at serine612.
27798666	13	22	theme	splice	2018:2023	arg1	variant					2025:2031	a splice variant	2016:2031	a splice variant displaying anti-tumorigenic properties in vitro and in vivo	2016:2091	This report identifies NRP1-Δ7 as a splice variant displaying anti-tumorigenic properties in vitro and in vivo, emphasizing the need to consider this isoform in future studies.
27798666	13	22	theme	splice	2018:2023	arg1	NRP1-Δ7					2005:2011	NRP1-Δ7	2005:2011	NRP1-Δ7	2005:2011	This report identifies NRP1-Δ7 as a splice variant displaying anti-tumorigenic properties in vitro and in vivo, emphasizing the need to consider this isoform in future studies.
27798666	8	23	theme	various	1289:1295	arg1	lines					1303:1307	various cells lines	1289:1307	various cells lines	1289:1307	NRP1-Δ7 mRNA was found expressed at an appreciable level, between 10 and 30% of the total NRP1, by various cells lines and tissues from human and murine origin.
27798666	5	24	theme	downstream	892:901	arg1	residues					883:890	two residues	879:890	two residues downstream of the O-glycosylation site	879:929	Here, we characterized a novel splice variant which has never been investigated, NRP1-Δ7, differing from the NRP1-FS by a deletion of 7 amino acids occurring two residues downstream of the O-glycosylation site.
27798666	6	25	theme	efficient	996:1004	arg1	glycosylation					1006:1018	efficient glycosylation	996:1018	efficient glycosylation	996:1018	This short sequence contains two aspartic residues critical for efficient glycosylation.
27798666	10	26	contain	had	1731:1733	arg1	NRP1-FS					1723:1729	NRP1-FS	1723:1729	NRP1-FS	1723:1729	Cells with increased expression of NRP1-Δ7 were characterized in vitro by a significant reduction of proliferation, migration and anchorage-independent growth, while NRP1-FS had the expected opposite "pro-tumoral" effects.
27798666	10	26	contain	had	1731:1733	arg2	effects					1771:1777	the expected opposite "pro-tumoral" effects	1735:1777	the expected opposite "pro-tumoral" effects	1735:1777	Cells with increased expression of NRP1-Δ7 were characterized in vitro by a significant reduction of proliferation, migration and anchorage-independent growth, while NRP1-FS had the expected opposite "pro-tumoral" effects.
27798666	6	27	theme	critical	983:990	arg1	residues					974:981	two aspartic residues	961:981	two aspartic residues critical for efficient glycosylation	961:1018	This short sequence contains two aspartic residues critical for efficient glycosylation.
27798666	5	28	theme	splice	752:757	arg1	NRP1-Δ7					802:808	NRP1-Δ7	802:808	NRP1-Δ7	802:808	Here, we characterized a novel splice variant which has never been investigated, NRP1-Δ7, differing from the NRP1-FS by a deletion of 7 amino acids occurring two residues downstream of the O-glycosylation site.
27798666	5	28	theme	splice	752:757	arg1	variant					759:765	a novel splice variant	744:765	a novel splice variant which has never been investigated	744:799	Here, we characterized a novel splice variant which has never been investigated, NRP1-Δ7, differing from the NRP1-FS by a deletion of 7 amino acids occurring two residues downstream of the O-glycosylation site.
27798666	9	29	theme	recombinant	1491:1501	arg1	NRP1-FS					1503:1509	recombinant NRP1-FS	1491:1509	recombinant NRP1-FS	1491:1509	To investigate the biological properties of this isoform, we generated prostatic (PC3) and breast (MDA-MB-231) cancer cells able to express recombinant NRP1-FS or NRP1-Δ7 in a doxycycline-inducible manner.
27798666	8	30	theme	human	1326:1330	arg1	origin					1343:1348	human and murine origin	1326:1348	human and murine origin	1326:1348	NRP1-Δ7 mRNA was found expressed at an appreciable level, between 10 and 30% of the total NRP1, by various cells lines and tissues from human and murine origin.
27798666	10	31	theme	NRP1-Δ7	1592:1598	arg1	expression					1578:1587	increased expression	1568:1587	increased expression of NRP1-Δ7	1568:1598	Cells with increased expression of NRP1-Δ7 were characterized in vitro by a significant reduction of proliferation, migration and anchorage-independent growth, while NRP1-FS had the expected opposite "pro-tumoral" effects.
27798666	7	32	theme	NRP1-Δ7	1173:1179	arg1	protein					1181:1187	the NRP1-Δ7 protein	1169:1187	the NRP1-Δ7 protein	1169:1187	As expected, the high molecular weight products appearing as a smear in SDS-PAGE and reflecting the presence of GAG in NRP1-FS were undetectable in the NRP1-Δ7 protein.
27798666	3	33	theme	primary	379:385	arg1	mRNA					387:390	Its primary mRNA	375:390	Its primary mRNA	375:390	Its primary mRNA is subjected to alternative splicing mechanisms generating different isoforms, some of which lack the transmembrane domain and display antagonist properties to NRP1 full size (FS).
27798666	8	34	theme	murine	1336:1341	arg1	origin					1343:1348	human and murine origin	1326:1348	human and murine origin	1326:1348	NRP1-Δ7 mRNA was found expressed at an appreciable level, between 10 and 30% of the total NRP1, by various cells lines and tissues from human and murine origin.
27798666	0	35	theme	Physiological	8:20	arg1	Variant					57:63	A Novel Physiological Glycosaminoglycan-Deficient Splice Variant	0:63	A Novel Physiological Glycosaminoglycan-Deficient Splice Variant of Neuropilin-1	0:79	A Novel Physiological Glycosaminoglycan-Deficient Splice Variant of Neuropilin-1 Is Anti-Tumorigenic In Vitro and In Vivo.
27798666	0	35	theme	Physiological	8:20	arg1	Anti-Tumorigenic					84:99	Anti-Tumorigenic	84:99	Anti-Tumorigenic	84:99	A Novel Physiological Glycosaminoglycan-Deficient Splice Variant of Neuropilin-1 Is Anti-Tumorigenic In Vitro and In Vivo.
27798666	3	36	theme	splicing	420:427	arg1	mechanisms					429:438	alternative splicing mechanisms	408:438	alternative splicing mechanisms generating different isoforms, some of which lack the transmembrane domain and display antagonist properties to NRP1 full size (FS)	408:570	Its primary mRNA is subjected to alternative splicing mechanisms generating different isoforms, some of which lack the transmembrane domain and display antagonist properties to NRP1 full size (FS).
27798666	8	37	dep	found	1207:1211	arg1	expressed					1213:1221	expressed	1213:1221	expressed	1213:1221	NRP1-Δ7 mRNA was found expressed at an appreciable level, between 10 and 30% of the total NRP1, by various cells lines and tissues from human and murine origin.
27798666	6	38	contain	contains	952:959	arg2	residues					974:981	two aspartic residues	961:981	two aspartic residues critical for efficient glycosylation	961:1018	This short sequence contains two aspartic residues critical for efficient glycosylation.
27798666	6	38	contain	contains	952:959	arg1	sequence					943:950	This short sequence	932:950	This short sequence	932:950	This short sequence contains two aspartic residues critical for efficient glycosylation.
27798666	0	39	theme	Splice	50:55	arg1	Variant					57:63	A Novel Physiological Glycosaminoglycan-Deficient Splice Variant	0:63	A Novel Physiological Glycosaminoglycan-Deficient Splice Variant of Neuropilin-1	0:79	A Novel Physiological Glycosaminoglycan-Deficient Splice Variant of Neuropilin-1 Is Anti-Tumorigenic In Vitro and In Vivo.
27798666	0	39	theme	Splice	50:55	arg1	Anti-Tumorigenic					84:99	Anti-Tumorigenic	84:99	Anti-Tumorigenic	84:99	A Novel Physiological Glycosaminoglycan-Deficient Splice Variant of Neuropilin-1 Is Anti-Tumorigenic In Vitro and In Vivo.
27798666	9	40	theme	doxycycline-inducible	1527:1547	arg1	manner					1549:1554	a doxycycline-inducible manner	1525:1554	a doxycycline-inducible manner	1525:1554	To investigate the biological properties of this isoform, we generated prostatic (PC3) and breast (MDA-MB-231) cancer cells able to express recombinant NRP1-FS or NRP1-Δ7 in a doxycycline-inducible manner.
27798666	11	41	theme	lower	1808:1812	arg1	rate					1830:1833	a lower internalization rate	1806:1833	a lower internalization rate	1806:1833	Upon VEGF-A165 treatment, a lower internalization rate was observed for NRP1-Δ7 than for NRP1-FS.
27798666	4	42	dep	glycosaminoglycans	638:655	arg1	chains					668:673	side chains	663:673	glycosaminoglycans (GAG) side chains through an O-glycosylation site at serine612	638:718	NRP1 is further post-translationally modified by the addition of glycosaminoglycans (GAG) side chains through an O-glycosylation site at serine612.
27798666	10	43	theme	growth	1709:1714	arg1	reduction					1645:1653	a significant reduction	1631:1653	a significant reduction of proliferation, migration and anchorage-independent growth	1631:1714	Cells with increased expression of NRP1-Δ7 were characterized in vitro by a significant reduction of proliferation, migration and anchorage-independent growth, while NRP1-FS had the expected opposite "pro-tumoral" effects.
27798666	4	44	theme	O-glycosylation	686:700	arg1	site					702:705	an O-glycosylation site	683:705	an O-glycosylation site at serine612	683:718	NRP1 is further post-translationally modified by the addition of glycosaminoglycans (GAG) side chains through an O-glycosylation site at serine612.
27798666	7	45	dep	products	1060:1067	arg1	appearing					1069:1077	appearing	1069:1077	appearing as a smear in SDS-PAGE	1069:1100	As expected, the high molecular weight products appearing as a smear in SDS-PAGE and reflecting the presence of GAG in NRP1-FS were undetectable in the NRP1-Δ7 protein.
27798666	7	45	dep	products	1060:1067	arg1	reflecting					1106:1115	reflecting	1106:1115	reflecting the presence of GAG in NRP1-FS	1106:1146	As expected, the high molecular weight products appearing as a smear in SDS-PAGE and reflecting the presence of GAG in NRP1-FS were undetectable in the NRP1-Δ7 protein.
27798666	7	46	theme	molecular	1043:1051	arg1	weight					1053:1058	high molecular weight	1038:1058	the high molecular weight products appearing as a smear in SDS-PAGE and reflecting the presence of GAG in NRP1-FS	1034:1146	As expected, the high molecular weight products appearing as a smear in SDS-PAGE and reflecting the presence of GAG in NRP1-FS were undetectable in the NRP1-Δ7 protein.
27798666	10	47	theme	anchorage-independent	1687:1707	arg1	growth					1709:1714	anchorage-independent growth	1687:1714	anchorage-independent growth	1687:1714	Cells with increased expression of NRP1-Δ7 were characterized in vitro by a significant reduction of proliferation, migration and anchorage-independent growth, while NRP1-FS had the expected opposite "pro-tumoral" effects.
27798666	0	48	theme	Neuropilin-1	68:79	arg1	Variant					57:63	A Novel Physiological Glycosaminoglycan-Deficient Splice Variant	0:63	A Novel Physiological Glycosaminoglycan-Deficient Splice Variant of Neuropilin-1	0:79	A Novel Physiological Glycosaminoglycan-Deficient Splice Variant of Neuropilin-1 Is Anti-Tumorigenic In Vitro and In Vivo.
27798666	0	48	theme	Neuropilin-1	68:79	arg1	Anti-Tumorigenic					84:99	Anti-Tumorigenic	84:99	Anti-Tumorigenic	84:99	A Novel Physiological Glycosaminoglycan-Deficient Splice Variant of Neuropilin-1 Is Anti-Tumorigenic In Vitro and In Vivo.
27798666	10	49	theme	migration	1673:1681	arg1	reduction					1645:1653	a significant reduction	1631:1653	a significant reduction of proliferation, migration and anchorage-independent growth	1631:1714	Cells with increased expression of NRP1-Δ7 were characterized in vitro by a significant reduction of proliferation, migration and anchorage-independent growth, while NRP1-FS had the expected opposite "pro-tumoral" effects.
27798666	2	50	theme	axonal	318:323	arg1	development					325:335	axonal development	318:335	axonal development	318:335	It is involved in axonal development, angiogenesis and cancer progression.
27798666	9	51	theme	cancer	1462:1467	arg1	cells					1469:1473	prostatic (PC3) and breast (MDA-MB-231) cancer cells	1422:1473	cells	1469:1473	To investigate the biological properties of this isoform, we generated prostatic (PC3) and breast (MDA-MB-231) cancer cells able to express recombinant NRP1-FS or NRP1-Δ7 in a doxycycline-inducible manner.
27798666	10	52	theme	proliferation	1658:1670	arg1	reduction					1645:1653	a significant reduction	1631:1653	a significant reduction of proliferation, migration and anchorage-independent growth	1631:1714	Cells with increased expression of NRP1-Δ7 were characterized in vitro by a significant reduction of proliferation, migration and anchorage-independent growth, while NRP1-FS had the expected opposite "pro-tumoral" effects.
27798666	3	53	theme	NRP1	552:555	arg1	size					562:565	NRP1 full size	552:565	NRP1 full size (FS)	552:570	Its primary mRNA is subjected to alternative splicing mechanisms generating different isoforms, some of which lack the transmembrane domain and display antagonist properties to NRP1 full size (FS).
27798666	3	53	theme	NRP1	552:555	arg1	FS					568:569	FS	568:569	FS	568:569	Its primary mRNA is subjected to alternative splicing mechanisms generating different isoforms, some of which lack the transmembrane domain and display antagonist properties to NRP1 full size (FS).
27798666	4	54	theme	side	663:666	arg1	chains					668:673	side chains	663:673	glycosaminoglycans (GAG) side chains through an O-glycosylation site at serine612	638:718	NRP1 is further post-translationally modified by the addition of glycosaminoglycans (GAG) side chains through an O-glycosylation site at serine612.
27798666	10	55	theme	opposite	1748:1755	arg1	effects					1771:1777	the expected opposite "pro-tumoral" effects	1735:1777	the expected opposite "pro-tumoral" effects	1735:1777	Cells with increased expression of NRP1-Δ7 were characterized in vitro by a significant reduction of proliferation, migration and anchorage-independent growth, while NRP1-FS had the expected opposite "pro-tumoral" effects.
27798666	8	56	from	origin	1343:1348	arg1	tissues					1313:1319	tissues	1313:1319	tissues	1313:1319	NRP1-Δ7 mRNA was found expressed at an appreciable level, between 10 and 30% of the total NRP1, by various cells lines and tissues from human and murine origin.
27798666	8	56	from	origin	1343:1348	arg1	lines					1303:1307	various cells lines	1289:1307	various cells lines	1289:1307	NRP1-Δ7 mRNA was found expressed at an appreciable level, between 10 and 30% of the total NRP1, by various cells lines and tissues from human and murine origin.
27798666	5	57	theme	amino	857:861	arg1	acids					863:867	7 amino acids	855:867	7 amino acids occurring two residues downstream of the O-glycosylation site	855:929	Here, we characterized a novel splice variant which has never been investigated, NRP1-Δ7, differing from the NRP1-FS by a deletion of 7 amino acids occurring two residues downstream of the O-glycosylation site.
27798666	8	58	theme	NRP1-Δ7	1190:1196	arg1	mRNA					1198:1201	NRP1-Δ7 mRNA	1190:1201	NRP1-Δ7 mRNA	1190:1201	NRP1-Δ7 mRNA was found expressed at an appreciable level, between 10 and 30% of the total NRP1, by various cells lines and tissues from human and murine origin.
27798666	7	59	from	protein	1181:1187	arg1	products					1060:1067	the high molecular weight products	1034:1067	the high molecular weight products appearing as a smear in SDS-PAGE and reflecting the presence of GAG in NRP1-FS	1034:1146	As expected, the high molecular weight products appearing as a smear in SDS-PAGE and reflecting the presence of GAG in NRP1-FS were undetectable in the NRP1-Δ7 protein.
27798666	7	59	from	protein	1181:1187	arg1	undetectable					1153:1164	undetectable	1153:1164	undetectable	1153:1164	As expected, the high molecular weight products appearing as a smear in SDS-PAGE and reflecting the presence of GAG in NRP1-FS were undetectable in the NRP1-Δ7 protein.
27798666	4	60	theme	glycosaminoglycans	638:655	arg1	addition					626:633	the addition	622:633	the addition of glycosaminoglycans (GAG) side chains through an O-glycosylation site at serine612	622:718	NRP1 is further post-translationally modified by the addition of glycosaminoglycans (GAG) side chains through an O-glycosylation site at serine612.
27798666	1	61	theme	growth	206:211	arg1	factors					213:219	several growth factors	198:219	several growth factors	198:219	Neuropilin-1 (NRP1) is a transmembrane protein acting as a co-receptor for several growth factors and interacting with other proteins such as integrins and plexins/semaphorins.
27798666	5	62	gly	O-glycosylation	910:924	arg2	site					926:929	the O-glycosylation site	906:929	the O-glycosylation site	906:929	Here, we characterized a novel splice variant which has never been investigated, NRP1-Δ7, differing from the NRP1-FS by a deletion of 7 amino acids occurring two residues downstream of the O-glycosylation site.
27798666	4	63	gly	O-glycosylation	686:700	arg2	serine612					710:718	serine612	710:718	serine612	710:718	NRP1 is further post-translationally modified by the addition of glycosaminoglycans (GAG) side chains through an O-glycosylation site at serine612.
27798666	4	63	gly	O-glycosylation	686:700	arg2	site					702:705	an O-glycosylation site	683:705	an O-glycosylation site at serine612	683:718	NRP1 is further post-translationally modified by the addition of glycosaminoglycans (GAG) side chains through an O-glycosylation site at serine612.
27798666	10	64	theme	pro-tumoral	1758:1768	arg1	effects					1771:1777	the expected opposite "pro-tumoral" effects	1735:1777	the expected opposite "pro-tumoral" effects	1735:1777	Cells with increased expression of NRP1-Δ7 were characterized in vitro by a significant reduction of proliferation, migration and anchorage-independent growth, while NRP1-FS had the expected opposite "pro-tumoral" effects.
27798666	9	65	theme	breast	1442:1447	arg1	cells					1469:1473	prostatic (PC3) and breast (MDA-MB-231) cancer cells	1422:1473	cells	1469:1473	To investigate the biological properties of this isoform, we generated prostatic (PC3) and breast (MDA-MB-231) cancer cells able to express recombinant NRP1-FS or NRP1-Δ7 in a doxycycline-inducible manner.
27798666	9	66	theme	MDA-MB-231	1450:1459	arg1	cells					1469:1473	prostatic (PC3) and breast (MDA-MB-231) cancer cells	1422:1473	cells	1469:1473	To investigate the biological properties of this isoform, we generated prostatic (PC3) and breast (MDA-MB-231) cancer cells able to express recombinant NRP1-FS or NRP1-Δ7 in a doxycycline-inducible manner.
27798666	12	67	theme	prostatic	1930:1938	arg1	tumors					1940:1945	prostatic tumors	1930:1945	prostatic tumors	1930:1945	Finally, we showed that NRP1-Δ7 inhibited growth of prostatic tumors and their vascularization in vivo.
27798666	8	68	theme	NRP1	1280:1283	arg1	%					1265:1265	10 and 30%	1256:1265	10 and 30% of the total NRP1	1256:1283	NRP1-Δ7 mRNA was found expressed at an appreciable level, between 10 and 30% of the total NRP1, by various cells lines and tissues from human and murine origin.
27798666	8	68	theme	NRP1	1280:1283	arg1	NRP1					1280:1283	the total NRP1	1270:1283	the total NRP1	1270:1283	NRP1-Δ7 mRNA was found expressed at an appreciable level, between 10 and 30% of the total NRP1, by various cells lines and tissues from human and murine origin.
27798666	1	69	theme	transmembrane	148:160	arg1	Neuropilin-1					123:134	Neuropilin-1	123:134	Neuropilin-1 (NRP1)	123:141	Neuropilin-1 (NRP1) is a transmembrane protein acting as a co-receptor for several growth factors and interacting with other proteins such as integrins and plexins/semaphorins.
27798666	1	69	theme	transmembrane	148:160	arg1	protein					162:168	a transmembrane protein	146:168	a transmembrane protein acting as a co-receptor for several growth factors and interacting with other proteins such as integrins and plexins/semaphorins	146:297	Neuropilin-1 (NRP1) is a transmembrane protein acting as a co-receptor for several growth factors and interacting with other proteins such as integrins and plexins/semaphorins.
27798666	13	70	theme	anti-tumorigenic	2044:2059	arg1	properties					2061:2070	anti-tumorigenic properties	2044:2070	anti-tumorigenic properties in vitro and in vivo	2044:2091	This report identifies NRP1-Δ7 as a splice variant displaying anti-tumorigenic properties in vitro and in vivo, emphasizing the need to consider this isoform in future studies.
27798666	9	71	theme	able	1475:1478	arg1	PC3					1433:1435	prostatic (PC3) and breast (MDA-MB-231) cancer cells	1422:1473	PC3	1433:1435	To investigate the biological properties of this isoform, we generated prostatic (PC3) and breast (MDA-MB-231) cancer cells able to express recombinant NRP1-FS or NRP1-Δ7 in a doxycycline-inducible manner.
27798666	7	72	from	undetectable	1153:1164	arg1	protein					1181:1187	the NRP1-Δ7 protein	1169:1187	the NRP1-Δ7 protein	1169:1187	As expected, the high molecular weight products appearing as a smear in SDS-PAGE and reflecting the presence of GAG in NRP1-FS were undetectable in the NRP1-Δ7 protein.
27798666	8	73	theme	cells	1297:1301	arg1	lines					1303:1307	various cells lines	1289:1307	various cells lines	1289:1307	NRP1-Δ7 mRNA was found expressed at an appreciable level, between 10 and 30% of the total NRP1, by various cells lines and tissues from human and murine origin.
27798666	3	74	theme	transmembrane	494:506	arg1	domain					508:513	the transmembrane domain	490:513	the transmembrane domain	490:513	Its primary mRNA is subjected to alternative splicing mechanisms generating different isoforms, some of which lack the transmembrane domain and display antagonist properties to NRP1 full size (FS).
27798666	5	75	theme	novel	746:750	arg1	NRP1-Δ7					802:808	NRP1-Δ7	802:808	NRP1-Δ7	802:808	Here, we characterized a novel splice variant which has never been investigated, NRP1-Δ7, differing from the NRP1-FS by a deletion of 7 amino acids occurring two residues downstream of the O-glycosylation site.
27798666	5	75	theme	novel	746:750	arg1	variant					759:765	a novel splice variant	744:765	a novel splice variant which has never been investigated	744:799	Here, we characterized a novel splice variant which has never been investigated, NRP1-Δ7, differing from the NRP1-FS by a deletion of 7 amino acids occurring two residues downstream of the O-glycosylation site.
27798666	1	76	theme	several	198:204	arg1	factors					213:219	several growth factors	198:219	several growth factors	198:219	Neuropilin-1 (NRP1) is a transmembrane protein acting as a co-receptor for several growth factors and interacting with other proteins such as integrins and plexins/semaphorins.
27798666	0	77	theme	Novel	2:6	arg1	Variant					57:63	A Novel Physiological Glycosaminoglycan-Deficient Splice Variant	0:63	A Novel Physiological Glycosaminoglycan-Deficient Splice Variant of Neuropilin-1	0:79	A Novel Physiological Glycosaminoglycan-Deficient Splice Variant of Neuropilin-1 Is Anti-Tumorigenic In Vitro and In Vivo.
27798666	0	77	theme	Novel	2:6	arg1	Anti-Tumorigenic					84:99	Anti-Tumorigenic	84:99	Anti-Tumorigenic	84:99	A Novel Physiological Glycosaminoglycan-Deficient Splice Variant of Neuropilin-1 Is Anti-Tumorigenic In Vitro and In Vivo.
27798666	1	78	dep	protein	162:168	arg1	acting					170:175	acting	170:175	acting as a co-receptor for several growth factors	170:219	Neuropilin-1 (NRP1) is a transmembrane protein acting as a co-receptor for several growth factors and interacting with other proteins such as integrins and plexins/semaphorins.
27798666	1	78	dep	protein	162:168	arg1	interacting					225:235	interacting	225:235	interacting with other proteins such as integrins and plexins/semaphorins	225:297	Neuropilin-1 (NRP1) is a transmembrane protein acting as a co-receptor for several growth factors and interacting with other proteins such as integrins and plexins/semaphorins.
27798666	3	79	theme	different	451:459	arg1	isoforms					461:468	different isoforms	451:468	different isoforms	451:468	Its primary mRNA is subjected to alternative splicing mechanisms generating different isoforms, some of which lack the transmembrane domain and display antagonist properties to NRP1 full size (FS).
27798666	0	80	theme	Glycosaminoglycan-Deficient	22:48	arg1	Variant					57:63	A Novel Physiological Glycosaminoglycan-Deficient Splice Variant	0:63	A Novel Physiological Glycosaminoglycan-Deficient Splice Variant of Neuropilin-1	0:79	A Novel Physiological Glycosaminoglycan-Deficient Splice Variant of Neuropilin-1 Is Anti-Tumorigenic In Vitro and In Vivo.
27798666	0	80	theme	Glycosaminoglycan-Deficient	22:48	arg1	Anti-Tumorigenic					84:99	Anti-Tumorigenic	84:99	Anti-Tumorigenic	84:99	A Novel Physiological Glycosaminoglycan-Deficient Splice Variant of Neuropilin-1 Is Anti-Tumorigenic In Vitro and In Vivo.
27798666	7	81	theme	GAG	1133:1135	arg1	smear					1084:1088	a smear	1082:1088	a smear	1082:1088	As expected, the high molecular weight products appearing as a smear in SDS-PAGE and reflecting the presence of GAG in NRP1-FS were undetectable in the NRP1-Δ7 protein.
27798666	7	81	theme	GAG	1133:1135	arg1	presence					1121:1128	the presence	1117:1128	the presence of GAG in NRP1-FS	1117:1146	As expected, the high molecular weight products appearing as a smear in SDS-PAGE and reflecting the presence of GAG in NRP1-FS were undetectable in the NRP1-Δ7 protein.
27798666	3	82	theme	alternative	408:418	arg1	mechanisms					429:438	alternative splicing mechanisms	408:438	alternative splicing mechanisms generating different isoforms, some of which lack the transmembrane domain and display antagonist properties to NRP1 full size (FS)	408:570	Its primary mRNA is subjected to alternative splicing mechanisms generating different isoforms, some of which lack the transmembrane domain and display antagonist properties to NRP1 full size (FS).
27798666	7	83	from	presence	1121:1128	arg1	NRP1-FS					1140:1146	NRP1-FS	1140:1146	NRP1-FS	1140:1146	As expected, the high molecular weight products appearing as a smear in SDS-PAGE and reflecting the presence of GAG in NRP1-FS were undetectable in the NRP1-Δ7 protein.
27798666	11	84	theme	internalization	1814:1828	arg1	rate					1830:1833	a lower internalization rate	1806:1833	a lower internalization rate	1806:1833	Upon VEGF-A165 treatment, a lower internalization rate was observed for NRP1-Δ7 than for NRP1-FS.
27798666	10	85	theme	significant	1633:1643	arg1	reduction					1645:1653	a significant reduction	1631:1653	a significant reduction of proliferation, migration and anchorage-independent growth	1631:1714	Cells with increased expression of NRP1-Δ7 were characterized in vitro by a significant reduction of proliferation, migration and anchorage-independent growth, while NRP1-FS had the expected opposite "pro-tumoral" effects.
27798666	10	86	with	Cells	1557:1561	arg1	expression					1578:1587	increased expression	1568:1587	increased expression of NRP1-Δ7	1568:1598	Cells with increased expression of NRP1-Δ7 were characterized in vitro by a significant reduction of proliferation, migration and anchorage-independent growth, while NRP1-FS had the expected opposite "pro-tumoral" effects.
27798666	13	87	theme	future	2143:2148	arg1	studies					2150:2156	future studies	2143:2156	future studies	2143:2156	This report identifies NRP1-Δ7 as a splice variant displaying anti-tumorigenic properties in vitro and in vivo, emphasizing the need to consider this isoform in future studies.
27798666	4	88	from	serine612	710:718	arg1	site					702:705	an O-glycosylation site	683:705	an O-glycosylation site at serine612	683:718	NRP1 is further post-translationally modified by the addition of glycosaminoglycans (GAG) side chains through an O-glycosylation site at serine612.
27798666	1	89	theme	other	242:246	arg1	plexins/semaphorins					279:297	plexins/semaphorins	279:297	plexins/semaphorins	279:297	Neuropilin-1 (NRP1) is a transmembrane protein acting as a co-receptor for several growth factors and interacting with other proteins such as integrins and plexins/semaphorins.
27798666	1	89	theme	other	242:246	arg1	proteins					248:255	other proteins	242:255	other proteins such as integrins and plexins/semaphorins	242:297	Neuropilin-1 (NRP1) is a transmembrane protein acting as a co-receptor for several growth factors and interacting with other proteins such as integrins and plexins/semaphorins.
27798666	1	89	theme	other	242:246	arg1	integrins					265:273	integrins	265:273	integrins	265:273	Neuropilin-1 (NRP1) is a transmembrane protein acting as a co-receptor for several growth factors and interacting with other proteins such as integrins and plexins/semaphorins.
15807535	0	0	theme	plasma	151:156	arg1	membrane					158:165	the plasma membrane	147:165	the plasma membrane	147:165	N-Linked glycosylation of the human ABC transporter ABCG2 on asparagine 596 is not essential for expression, transport activity, or trafficking to the plasma membrane.
15807535	1	1	theme	plasma	234:239	arg1	ABCG2					216:220	The human ATP-binding cassette half-transporter ABCG2	168:220	The human ATP-binding cassette half-transporter ABCG2	168:220	The human ATP-binding cassette half-transporter ABCG2 is a 72 kDa plasma membrane protein that can confer multidrug resistance to cells in culture when overexpressed.
15807535	1	1	theme	plasma	234:239	arg1	protein					250:256	a 72 kDa plasma membrane protein	225:256	a 72 kDa plasma membrane protein that can confer multidrug resistance to cells in culture when overexpressed	225:332	The human ATP-binding cassette half-transporter ABCG2 is a 72 kDa plasma membrane protein that can confer multidrug resistance to cells in culture when overexpressed.
15807535	6	2	theme	similar	1190:1196	arg1	half-lives					1198:1207	similar half-lives	1190:1207	similar half-lives	1190:1207	Immunoblot and pulse-chase analyses revealed that the glycosylation-deficient ABCG2 (N596Q) variant and the glycosylated parent transporter are expressed equivalently at steady state and have similar half-lives.
15807535	7	3	attach	present	1299:1305	arg1	membrane					1321:1328	the plasma membrane	1310:1328	the plasma membrane	1310:1328	Cell surface analysis of ABCG2 expression showed comparable amounts of the N596Q variant present at the plasma membrane compared to the glycosylated ABCG2 protein.
15807535	7	3	attach	present	1299:1305	arg2	variant					1291:1297	the N596Q variant	1281:1297	the N596Q variant present at the plasma membrane	1281:1328	Cell surface analysis of ABCG2 expression showed comparable amounts of the N596Q variant present at the plasma membrane compared to the glycosylated ABCG2 protein.
15807535	9	4	gly	glycosylated	1709:1720	arg1	ABCG2					1722:1726	glycosylated ABCG2	1709:1726	glycosylated ABCG2	1709:1726	Furthermore, in crude membrane preparations, neither the basal nor the prazosin-stimulated ( approximately 2-fold) ATPase activities of ABCG2 (N596Q) were affected compared to glycosylated ABCG2.
15807535	4	5	theme	Site-directed	639:651	arg1	experiments					665:675	Site-directed mutagenesis experiments	639:675	Site-directed mutagenesis experiments	639:675	Site-directed mutagenesis experiments, in which each Asn was changed to Gln independently, revealed that only asparagine 596 is N-linked glycosylated.
15807535	10	6	theme	transporter	1756:1766	arg1	trafficking					1768:1778	transporter trafficking	1756:1778	transporter trafficking	1756:1778	Although subtle defects in transporter trafficking and function may exist, these data taken together suggest that N-glycosylation at arginine 596 is not essential for the expression, trafficking to the plasma membrane, or the overall function of ABCG2.
15807535	4	7	dep	glycosylated	776:787	arg1	N-linked					767:774	N-linked	767:774	N-linked	767:774	Site-directed mutagenesis experiments, in which each Asn was changed to Gln independently, revealed that only asparagine 596 is N-linked glycosylated.
15807535	2	8	with	treatment	401:409	arg1	F					438:438	peptide N-glycosidase F	416:438	peptide N-glycosidase F	416:438	Both transiently and stably expressed ABCG2 are glycosylated, and treatment with peptide N-glycosidase F reduces the apparent molecular mass on SDS-PAGE gels to approximately 60 kDa.
15807535	6	9	theme	steady	1168:1173	arg1	state					1175:1179	steady state	1168:1179	steady state	1168:1179	Immunoblot and pulse-chase analyses revealed that the glycosylation-deficient ABCG2 (N596Q) variant and the glycosylated parent transporter are expressed equivalently at steady state and have similar half-lives.
15807535	10	10	theme	ABCG2	1975:1979	arg1	trafficking					1912:1922	trafficking	1912:1922	trafficking to the plasma membrane	1912:1945	Although subtle defects in transporter trafficking and function may exist, these data taken together suggest that N-glycosylation at arginine 596 is not essential for the expression, trafficking to the plasma membrane, or the overall function of ABCG2.
15807535	10	10	theme	ABCG2	1975:1979	arg1	expression					1900:1909	the expression	1896:1909	the expression	1896:1909	Although subtle defects in transporter trafficking and function may exist, these data taken together suggest that N-glycosylation at arginine 596 is not essential for the expression, trafficking to the plasma membrane, or the overall function of ABCG2.
15807535	10	10	theme	ABCG2	1975:1979	arg1	function					1963:1970	the overall function	1951:1970	the overall function of ABCG2	1951:1979	Although subtle defects in transporter trafficking and function may exist, these data taken together suggest that N-glycosylation at arginine 596 is not essential for the expression, trafficking to the plasma membrane, or the overall function of ABCG2.
15807535	10	11	from	defects	1745:1751	arg1	function					1784:1791	function	1784:1791	function	1784:1791	Although subtle defects in transporter trafficking and function may exist, these data taken together suggest that N-glycosylation at arginine 596 is not essential for the expression, trafficking to the plasma membrane, or the overall function of ABCG2.
15807535	10	11	from	defects	1745:1751	arg1	trafficking					1768:1778	transporter trafficking	1756:1778	transporter trafficking	1756:1778	Although subtle defects in transporter trafficking and function may exist, these data taken together suggest that N-glycosylation at arginine 596 is not essential for the expression, trafficking to the plasma membrane, or the overall function of ABCG2.
15807535	3	12	theme	N-linked	561:568	arg1	sites					584:588	three potential N-linked glycosylation sites	545:588	three potential N-linked glycosylation sites	545:588	Sequence analysis revealed three potential N-linked glycosylation sites in human ABCG2 at amino acids 418, 557, and 596.
15807535	5	13	theme	direct	819:824	arg1	identification					826:839	the first direct identification	809:839	the first direct identification of the modified residue in ABCG2	809:872	These data provide the first direct identification of the modified residue in ABCG2 and evidence for the localization of loop 5 to the extracellular space, previously only predicted from hydropathy analysis.
15807535	5	14	from	identification	826:839	arg1	ABCG2					868:872	ABCG2	868:872	ABCG2	868:872	These data provide the first direct identification of the modified residue in ABCG2 and evidence for the localization of loop 5 to the extracellular space, previously only predicted from hydropathy analysis.
15807535	1	15	theme	half-transporter	199:214	arg1	ABCG2					216:220	The human ATP-binding cassette half-transporter ABCG2	168:220	The human ATP-binding cassette half-transporter ABCG2	168:220	The human ATP-binding cassette half-transporter ABCG2 is a 72 kDa plasma membrane protein that can confer multidrug resistance to cells in culture when overexpressed.
15807535	1	15	theme	half-transporter	199:214	arg1	protein					250:256	a 72 kDa plasma membrane protein	225:256	a 72 kDa plasma membrane protein that can confer multidrug resistance to cells in culture when overexpressed	225:332	The human ATP-binding cassette half-transporter ABCG2 is a 72 kDa plasma membrane protein that can confer multidrug resistance to cells in culture when overexpressed.
15807535	8	16	theme	intact	1461:1466	arg1	cells					1468:1472	intact cells	1461:1472	intact cells comparable to that in cells expressing glycosylated ABCG2	1461:1530	The ABCG2 (N596Q) variant is also functional, demonstrating rhodamine 123 transport in intact cells comparable to that in cells expressing glycosylated ABCG2.
15807535	3	17	theme	human	593:597	arg1	ABCG2					599:603	human ABCG2	593:603	human ABCG2	593:603	Sequence analysis revealed three potential N-linked glycosylation sites in human ABCG2 at amino acids 418, 557, and 596.
15807535	8	18	theme	comparable	1474:1483	arg1	cells					1468:1472	intact cells	1461:1472	intact cells comparable to that in cells expressing glycosylated ABCG2	1461:1530	The ABCG2 (N596Q) variant is also functional, demonstrating rhodamine 123 transport in intact cells comparable to that in cells expressing glycosylated ABCG2.
15807535	5	19	from	residue	857:863	arg1	ABCG2					868:872	ABCG2	868:872	ABCG2	868:872	These data provide the first direct identification of the modified residue in ABCG2 and evidence for the localization of loop 5 to the extracellular space, previously only predicted from hydropathy analysis.
15807535	5	20	theme	loop	911:914	arg1	localization					895:906	the localization	891:906	the localization of loop 5 to the extracellular space	891:943	These data provide the first direct identification of the modified residue in ABCG2 and evidence for the localization of loop 5 to the extracellular space, previously only predicted from hydropathy analysis.
15807535	7	21	theme	ABCG2	1359:1363	arg1	protein					1365:1371	the glycosylated ABCG2 protein	1342:1371	the glycosylated ABCG2 protein	1342:1371	Cell surface analysis of ABCG2 expression showed comparable amounts of the N596Q variant present at the plasma membrane compared to the glycosylated ABCG2 protein.
15807535	9	22	dep	basal	1590:1594	arg1	activities					1655:1664	ATPase activities	1648:1664	ATPase activities	1648:1664	Furthermore, in crude membrane preparations, neither the basal nor the prazosin-stimulated ( approximately 2-fold) ATPase activities of ABCG2 (N596Q) were affected compared to glycosylated ABCG2.
15807535	7	23	theme	expression	1241:1250	arg1	analysis					1223:1230	Cell surface analysis	1210:1230	Cell surface analysis of ABCG2 expression	1210:1250	Cell surface analysis of ABCG2 expression showed comparable amounts of the N596Q variant present at the plasma membrane compared to the glycosylated ABCG2 protein.
15807535	2	24	theme	SDS-PAGE	479:486	arg1	gels					488:491	SDS-PAGE gels	479:491	SDS-PAGE gels	479:491	Both transiently and stably expressed ABCG2 are glycosylated, and treatment with peptide N-glycosidase F reduces the apparent molecular mass on SDS-PAGE gels to approximately 60 kDa.
15807535	8	25	from	transport	1448:1456	arg1	cells					1468:1472	intact cells	1461:1472	intact cells comparable to that in cells expressing glycosylated ABCG2	1461:1530	The ABCG2 (N596Q) variant is also functional, demonstrating rhodamine 123 transport in intact cells comparable to that in cells expressing glycosylated ABCG2.
15807535	5	26	from	evidence	878:885	arg1	ABCG2					868:872	ABCG2	868:872	ABCG2	868:872	These data provide the first direct identification of the modified residue in ABCG2 and evidence for the localization of loop 5 to the extracellular space, previously only predicted from hydropathy analysis.
15807535	8	27	theme	glycosylated	1513:1524	arg1	ABCG2					1526:1530	glycosylated ABCG2	1513:1530	glycosylated ABCG2	1513:1530	The ABCG2 (N596Q) variant is also functional, demonstrating rhodamine 123 transport in intact cells comparable to that in cells expressing glycosylated ABCG2.
15807535	4	28	theme	only	744:747	arg1	596					760:762	only asparagine 596	744:762	only asparagine 596	744:762	Site-directed mutagenesis experiments, in which each Asn was changed to Gln independently, revealed that only asparagine 596 is N-linked glycosylated.
15807535	7	29	theme	surface	1215:1221	arg1	analysis					1223:1230	Cell surface analysis	1210:1230	Cell surface analysis of ABCG2 expression	1210:1250	Cell surface analysis of ABCG2 expression showed comparable amounts of the N596Q variant present at the plasma membrane compared to the glycosylated ABCG2 protein.
15807535	5	30	from	ABCG2	868:872	arg1	identification					826:839	the first direct identification	809:839	the first direct identification of the modified residue in ABCG2	809:872	These data provide the first direct identification of the modified residue in ABCG2 and evidence for the localization of loop 5 to the extracellular space, previously only predicted from hydropathy analysis.
15807535	5	30	from	ABCG2	868:872	arg1	evidence					878:885	evidence	878:885	evidence for the localization of loop 5 to the extracellular space	878:943	These data provide the first direct identification of the modified residue in ABCG2 and evidence for the localization of loop 5 to the extracellular space, previously only predicted from hydropathy analysis.
15807535	9	31	theme	membrane	1555:1562	arg1	preparations					1564:1575	crude membrane preparations	1549:1575	crude membrane preparations	1549:1575	Furthermore, in crude membrane preparations, neither the basal nor the prazosin-stimulated ( approximately 2-fold) ATPase activities of ABCG2 (N596Q) were affected compared to glycosylated ABCG2.
15807535	7	32	theme	glycosylated	1346:1357	arg1	protein					1365:1371	the glycosylated ABCG2 protein	1342:1371	the glycosylated ABCG2 protein	1342:1371	Cell surface analysis of ABCG2 expression showed comparable amounts of the N596Q variant present at the plasma membrane compared to the glycosylated ABCG2 protein.
15807535	6	33	gly	glycosylated	1106:1117	arg1	transporter					1126:1136	the glycosylated parent transporter	1102:1136	the glycosylated parent transporter	1102:1136	Immunoblot and pulse-chase analyses revealed that the glycosylation-deficient ABCG2 (N596Q) variant and the glycosylated parent transporter are expressed equivalently at steady state and have similar half-lives.
15807535	0	34	theme	asparagine	61:70	arg1	596					72:74	asparagine 596	61:74	asparagine 596	61:74	N-Linked glycosylation of the human ABC transporter ABCG2 on asparagine 596 is not essential for expression, transport activity, or trafficking to the plasma membrane.
15807535	0	35	theme	N-Linked	0:7	arg1	glycosylation					9:21	N-Linked glycosylation	0:21	N-Linked glycosylation of the human ABC transporter ABCG2 on asparagine 596	0:74	N-Linked glycosylation of the human ABC transporter ABCG2 on asparagine 596 is not essential for expression, transport activity, or trafficking to the plasma membrane.
15807535	6	36	theme	glycosylation-deficient	1052:1074	arg1	variant					1090:1096	the glycosylation-deficient ABCG2 (N596Q) variant	1048:1096	the glycosylation-deficient ABCG2 (N596Q) variant	1048:1096	Immunoblot and pulse-chase analyses revealed that the glycosylation-deficient ABCG2 (N596Q) variant and the glycosylated parent transporter are expressed equivalently at steady state and have similar half-lives.
15807535	2	37	theme	N-glycosidase	424:436	arg1	F					438:438	peptide N-glycosidase F	416:438	peptide N-glycosidase F	416:438	Both transiently and stably expressed ABCG2 are glycosylated, and treatment with peptide N-glycosidase F reduces the apparent molecular mass on SDS-PAGE gels to approximately 60 kDa.
15807535	5	38	theme	extracellular	925:937	arg1	space					939:943	the extracellular space	921:943	the extracellular space	921:943	These data provide the first direct identification of the modified residue in ABCG2 and evidence for the localization of loop 5 to the extracellular space, previously only predicted from hydropathy analysis.
15807535	10	39	from	arginine	1862:1869	arg1	N-glycosylation					1843:1857	N-glycosylation	1843:1857	N-glycosylation at arginine 596	1843:1873	Although subtle defects in transporter trafficking and function may exist, these data taken together suggest that N-glycosylation at arginine 596 is not essential for the expression, trafficking to the plasma membrane, or the overall function of ABCG2.
15807535	0	40	theme	human	30:34	arg1	ABCG2					52:56	the human ABC transporter ABCG2	26:56	the human ABC transporter ABCG2	26:56	N-Linked glycosylation of the human ABC transporter ABCG2 on asparagine 596 is not essential for expression, transport activity, or trafficking to the plasma membrane.
15807535	0	41	gly	glycosylation	9:21	arg1	596					72:74	asparagine 596	61:74	asparagine 596	61:74	N-Linked glycosylation of the human ABC transporter ABCG2 on asparagine 596 is not essential for expression, transport activity, or trafficking to the plasma membrane.
15807535	0	41	gly	glycosylation	9:21	arg1	transport					109:117	transport activity	109:126	transport activity	109:126	N-Linked glycosylation of the human ABC transporter ABCG2 on asparagine 596 is not essential for expression, transport activity, or trafficking to the plasma membrane.
15807535	0	41	gly	glycosylation	9:21	arg1	ABCG2					52:56	the human ABC transporter ABCG2	26:56	the human ABC transporter ABCG2	26:56	N-Linked glycosylation of the human ABC transporter ABCG2 on asparagine 596 is not essential for expression, transport activity, or trafficking to the plasma membrane.
15807535	2	42	theme	apparent	452:459	arg1	mass					471:474	the apparent molecular mass	448:474	the apparent molecular mass on SDS-PAGE gels	448:491	Both transiently and stably expressed ABCG2 are glycosylated, and treatment with peptide N-glycosidase F reduces the apparent molecular mass on SDS-PAGE gels to approximately 60 kDa.
15807535	0	43	theme	transporter	40:50	arg1	ABCG2					52:56	the human ABC transporter ABCG2	26:56	the human ABC transporter ABCG2	26:56	N-Linked glycosylation of the human ABC transporter ABCG2 on asparagine 596 is not essential for expression, transport activity, or trafficking to the plasma membrane.
15807535	7	44	theme	present	1299:1305	arg1	variant					1291:1297	the N596Q variant	1281:1297	the N596Q variant present at the plasma membrane	1281:1328	Cell surface analysis of ABCG2 expression showed comparable amounts of the N596Q variant present at the plasma membrane compared to the glycosylated ABCG2 protein.
15807535	6	45	theme	glycosylated	1106:1117	arg1	transporter					1126:1136	the glycosylated parent transporter	1102:1136	the glycosylated parent transporter	1102:1136	Immunoblot and pulse-chase analyses revealed that the glycosylation-deficient ABCG2 (N596Q) variant and the glycosylated parent transporter are expressed equivalently at steady state and have similar half-lives.
15807535	5	46	theme	modified	848:855	arg1	residue					857:863	the modified residue	844:863	the modified residue in ABCG2	844:872	These data provide the first direct identification of the modified residue in ABCG2 and evidence for the localization of loop 5 to the extracellular space, previously only predicted from hydropathy analysis.
15807535	0	47	theme	ABCG2	52:56	arg1	glycosylation					9:21	N-Linked glycosylation	0:21	N-Linked glycosylation of the human ABC transporter ABCG2 on asparagine 596	0:74	N-Linked glycosylation of the human ABC transporter ABCG2 on asparagine 596 is not essential for expression, transport activity, or trafficking to the plasma membrane.
15807535	1	48	from	cells	298:302	arg1	culture					307:313	culture	307:313	culture	307:313	The human ATP-binding cassette half-transporter ABCG2 is a 72 kDa plasma membrane protein that can confer multidrug resistance to cells in culture when overexpressed.
15807535	10	49	theme	subtle	1738:1743	arg1	defects					1745:1751	subtle defects	1738:1751	subtle defects in transporter trafficking and function	1738:1791	Although subtle defects in transporter trafficking and function may exist, these data taken together suggest that N-glycosylation at arginine 596 is not essential for the expression, trafficking to the plasma membrane, or the overall function of ABCG2.
15807535	1	50	theme	kDa	230:232	arg1	ABCG2					216:220	The human ATP-binding cassette half-transporter ABCG2	168:220	The human ATP-binding cassette half-transporter ABCG2	168:220	The human ATP-binding cassette half-transporter ABCG2 is a 72 kDa plasma membrane protein that can confer multidrug resistance to cells in culture when overexpressed.
15807535	1	50	theme	kDa	230:232	arg1	protein					250:256	a 72 kDa plasma membrane protein	225:256	a 72 kDa plasma membrane protein that can confer multidrug resistance to cells in culture when overexpressed	225:332	The human ATP-binding cassette half-transporter ABCG2 is a 72 kDa plasma membrane protein that can confer multidrug resistance to cells in culture when overexpressed.
15807535	9	51	theme	ABCG2	1669:1673	arg1	basal					1590:1594	basal	1590:1594	basal	1590:1594	Furthermore, in crude membrane preparations, neither the basal nor the prazosin-stimulated ( approximately 2-fold) ATPase activities of ABCG2 (N596Q) were affected compared to glycosylated ABCG2.
15807535	7	52	theme	comparable	1259:1268	arg1	amounts					1270:1276	comparable amounts	1259:1276	comparable amounts of the N596Q variant present at the plasma membrane	1259:1328	Cell surface analysis of ABCG2 expression showed comparable amounts of the N596Q variant present at the plasma membrane compared to the glycosylated ABCG2 protein.
15807535	7	52	theme	comparable	1259:1268	arg1	variant					1291:1297	the N596Q variant	1281:1297	the N596Q variant present at the plasma membrane	1281:1328	Cell surface analysis of ABCG2 expression showed comparable amounts of the N596Q variant present at the plasma membrane compared to the glycosylated ABCG2 protein.
15807535	1	53	theme	membrane	241:248	arg1	ABCG2					216:220	The human ATP-binding cassette half-transporter ABCG2	168:220	The human ATP-binding cassette half-transporter ABCG2	168:220	The human ATP-binding cassette half-transporter ABCG2 is a 72 kDa plasma membrane protein that can confer multidrug resistance to cells in culture when overexpressed.
15807535	1	53	theme	membrane	241:248	arg1	protein					250:256	a 72 kDa plasma membrane protein	225:256	a 72 kDa plasma membrane protein that can confer multidrug resistance to cells in culture when overexpressed	225:332	The human ATP-binding cassette half-transporter ABCG2 is a 72 kDa plasma membrane protein that can confer multidrug resistance to cells in culture when overexpressed.
15807535	3	54	theme	Sequence	518:525	arg1	analysis					527:534	Sequence analysis	518:534	Sequence analysis	518:534	Sequence analysis revealed three potential N-linked glycosylation sites in human ABCG2 at amino acids 418, 557, and 596.
15807535	3	55	theme	glycosylation	570:582	arg1	sites					584:588	three potential N-linked glycosylation sites	545:588	three potential N-linked glycosylation sites	545:588	Sequence analysis revealed three potential N-linked glycosylation sites in human ABCG2 at amino acids 418, 557, and 596.
15807535	5	56	theme	residue	857:863	arg1	identification					826:839	the first direct identification	809:839	the first direct identification of the modified residue in ABCG2	809:872	These data provide the first direct identification of the modified residue in ABCG2 and evidence for the localization of loop 5 to the extracellular space, previously only predicted from hydropathy analysis.
15807535	5	56	theme	residue	857:863	arg1	evidence					878:885	evidence	878:885	evidence for the localization of loop 5 to the extracellular space	878:943	These data provide the first direct identification of the modified residue in ABCG2 and evidence for the localization of loop 5 to the extracellular space, previously only predicted from hydropathy analysis.
15807535	4	57	theme	mutagenesis	653:663	arg1	experiments					665:675	Site-directed mutagenesis experiments	639:675	Site-directed mutagenesis experiments	639:675	Site-directed mutagenesis experiments, in which each Asn was changed to Gln independently, revealed that only asparagine 596 is N-linked glycosylated.
15807535	0	58	theme	transport	109:117	arg1	activity					119:126	transport activity	109:126	transport activity	109:126	N-Linked glycosylation of the human ABC transporter ABCG2 on asparagine 596 is not essential for expression, transport activity, or trafficking to the plasma membrane.
15807535	3	59	theme	potential	551:559	arg1	sites					584:588	three potential N-linked glycosylation sites	545:588	three potential N-linked glycosylation sites	545:588	Sequence analysis revealed three potential N-linked glycosylation sites in human ABCG2 at amino acids 418, 557, and 596.
15807535	1	60	theme	human	172:176	arg1	ABCG2					216:220	The human ATP-binding cassette half-transporter ABCG2	168:220	The human ATP-binding cassette half-transporter ABCG2	168:220	The human ATP-binding cassette half-transporter ABCG2 is a 72 kDa plasma membrane protein that can confer multidrug resistance to cells in culture when overexpressed.
15807535	1	60	theme	human	172:176	arg1	protein					250:256	a 72 kDa plasma membrane protein	225:256	a 72 kDa plasma membrane protein that can confer multidrug resistance to cells in culture when overexpressed	225:332	The human ATP-binding cassette half-transporter ABCG2 is a 72 kDa plasma membrane protein that can confer multidrug resistance to cells in culture when overexpressed.
15807535	9	61	theme	glycosylated	1709:1720	arg1	ABCG2					1722:1726	glycosylated ABCG2	1709:1726	glycosylated ABCG2	1709:1726	Furthermore, in crude membrane preparations, neither the basal nor the prazosin-stimulated ( approximately 2-fold) ATPase activities of ABCG2 (N596Q) were affected compared to glycosylated ABCG2.
15807535	10	62	theme	overall	1955:1961	arg1	function					1963:1970	the overall function	1951:1970	the overall function of ABCG2	1951:1979	Although subtle defects in transporter trafficking and function may exist, these data taken together suggest that N-glycosylation at arginine 596 is not essential for the expression, trafficking to the plasma membrane, or the overall function of ABCG2.
15807535	9	63	dep	prazosin-stimulated	1604:1622	arg1	2-fold					1640:1645	2-fold	1640:1645	2-fold	1640:1645	Furthermore, in crude membrane preparations, neither the basal nor the prazosin-stimulated ( approximately 2-fold) ATPase activities of ABCG2 (N596Q) were affected compared to glycosylated ABCG2.
15807535	1	64	theme	cassette	190:197	arg1	ABCG2					216:220	The human ATP-binding cassette half-transporter ABCG2	168:220	The human ATP-binding cassette half-transporter ABCG2	168:220	The human ATP-binding cassette half-transporter ABCG2 is a 72 kDa plasma membrane protein that can confer multidrug resistance to cells in culture when overexpressed.
15807535	1	64	theme	cassette	190:197	arg1	protein					250:256	a 72 kDa plasma membrane protein	225:256	a 72 kDa plasma membrane protein that can confer multidrug resistance to cells in culture when overexpressed	225:332	The human ATP-binding cassette half-transporter ABCG2 is a 72 kDa plasma membrane protein that can confer multidrug resistance to cells in culture when overexpressed.
15807535	3	65	gly	glycosylation	570:582	arg2	sites					584:588	three potential N-linked glycosylation sites	545:588	three potential N-linked glycosylation sites	545:588	Sequence analysis revealed three potential N-linked glycosylation sites in human ABCG2 at amino acids 418, 557, and 596.
15807535	3	65	gly	glycosylation	570:582	arg2	three					545:549	three	545:549	three	545:549	Sequence analysis revealed three potential N-linked glycosylation sites in human ABCG2 at amino acids 418, 557, and 596.
15807535	8	66	gly	glycosylated	1513:1524	arg1	ABCG2					1526:1530	glycosylated ABCG2	1513:1530	glycosylated ABCG2	1513:1530	The ABCG2 (N596Q) variant is also functional, demonstrating rhodamine 123 transport in intact cells comparable to that in cells expressing glycosylated ABCG2.
15807535	6	67	theme	pulse-chase	1013:1023	arg1	analyses					1025:1032	Immunoblot and pulse-chase analyses	998:1032	analyses	1025:1032	Immunoblot and pulse-chase analyses revealed that the glycosylation-deficient ABCG2 (N596Q) variant and the glycosylated parent transporter are expressed equivalently at steady state and have similar half-lives.
15807535	7	68	theme	ABCG2	1235:1239	arg1	expression					1241:1250	ABCG2 expression	1235:1250	ABCG2 expression	1235:1250	Cell surface analysis of ABCG2 expression showed comparable amounts of the N596Q variant present at the plasma membrane compared to the glycosylated ABCG2 protein.
15807535	3	69	theme	amino	608:612	arg1	acids					614:618	amino acids 418	608:622	amino acids 418	608:622	Sequence analysis revealed three potential N-linked glycosylation sites in human ABCG2 at amino acids 418, 557, and 596.
15807535	5	70	theme	first	813:817	arg1	identification					826:839	the first direct identification	809:839	the first direct identification of the modified residue in ABCG2	809:872	These data provide the first direct identification of the modified residue in ABCG2 and evidence for the localization of loop 5 to the extracellular space, previously only predicted from hydropathy analysis.
15807535	6	71	theme	Immunoblot	998:1007	arg1	analyses					1025:1032	Immunoblot and pulse-chase analyses	998:1032	analyses	1025:1032	Immunoblot and pulse-chase analyses revealed that the glycosylation-deficient ABCG2 (N596Q) variant and the glycosylated parent transporter are expressed equivalently at steady state and have similar half-lives.
15807535	3	72	link	N-linked	561:568	arg1	sites					584:588	three potential N-linked glycosylation sites	545:588	three potential N-linked glycosylation sites	545:588	Sequence analysis revealed three potential N-linked glycosylation sites in human ABCG2 at amino acids 418, 557, and 596.
15807535	0	73	from	glycosylation	9:21	arg1	596					72:74	asparagine 596	61:74	asparagine 596	61:74	N-Linked glycosylation of the human ABC transporter ABCG2 on asparagine 596 is not essential for expression, transport activity, or trafficking to the plasma membrane.
15807535	7	74	theme	Cell	1210:1213	arg1	analysis					1223:1230	Cell surface analysis	1210:1230	Cell surface analysis of ABCG2 expression	1210:1250	Cell surface analysis of ABCG2 expression showed comparable amounts of the N596Q variant present at the plasma membrane compared to the glycosylated ABCG2 protein.
15807535	9	75	theme	crude	1549:1553	arg1	preparations					1564:1575	crude membrane preparations	1549:1575	crude membrane preparations	1549:1575	Furthermore, in crude membrane preparations, neither the basal nor the prazosin-stimulated ( approximately 2-fold) ATPase activities of ABCG2 (N596Q) were affected compared to glycosylated ABCG2.
15807535	7	76	theme	N596Q	1285:1289	arg1	variant					1291:1297	the N596Q variant	1281:1297	the N596Q variant present at the plasma membrane	1281:1328	Cell surface analysis of ABCG2 expression showed comparable amounts of the N596Q variant present at the plasma membrane compared to the glycosylated ABCG2 protein.
15807535	7	77	gly	glycosylated	1346:1357	arg1	protein					1365:1371	the glycosylated ABCG2 protein	1342:1371	the glycosylated ABCG2 protein	1342:1371	Cell surface analysis of ABCG2 expression showed comparable amounts of the N596Q variant present at the plasma membrane compared to the glycosylated ABCG2 protein.
15807535	1	78	theme	ATP-binding	178:188	arg1	ABCG2					216:220	The human ATP-binding cassette half-transporter ABCG2	168:220	The human ATP-binding cassette half-transporter ABCG2	168:220	The human ATP-binding cassette half-transporter ABCG2 is a 72 kDa plasma membrane protein that can confer multidrug resistance to cells in culture when overexpressed.
15807535	1	78	theme	ATP-binding	178:188	arg1	protein					250:256	a 72 kDa plasma membrane protein	225:256	a 72 kDa plasma membrane protein that can confer multidrug resistance to cells in culture when overexpressed	225:332	The human ATP-binding cassette half-transporter ABCG2 is a 72 kDa plasma membrane protein that can confer multidrug resistance to cells in culture when overexpressed.
15807535	6	79	theme	N596Q	1083:1087	arg1	variant					1090:1096	the glycosylation-deficient ABCG2 (N596Q) variant	1048:1096	the glycosylation-deficient ABCG2 (N596Q) variant	1048:1096	Immunoblot and pulse-chase analyses revealed that the glycosylation-deficient ABCG2 (N596Q) variant and the glycosylated parent transporter are expressed equivalently at steady state and have similar half-lives.
15807535	2	80	from	mass	471:474	arg1	gels					488:491	SDS-PAGE gels	479:491	SDS-PAGE gels	479:491	Both transiently and stably expressed ABCG2 are glycosylated, and treatment with peptide N-glycosidase F reduces the apparent molecular mass on SDS-PAGE gels to approximately 60 kDa.
15807535	2	81	gly	glycosylated	383:394	arg1	ABCG2					373:377	Both transiently and stably expressed ABCG2	335:377	Both transiently and stably expressed ABCG2	335:377	Both transiently and stably expressed ABCG2 are glycosylated, and treatment with peptide N-glycosidase F reduces the apparent molecular mass on SDS-PAGE gels to approximately 60 kDa.
15807535	4	82	theme	asparagine	749:758	arg1	596					760:762	only asparagine 596	744:762	only asparagine 596	744:762	Site-directed mutagenesis experiments, in which each Asn was changed to Gln independently, revealed that only asparagine 596 is N-linked glycosylated.
15807535	7	83	dep	showed	1252:1257	arg1	compared					1330:1337	compared	1330:1337	showed comparable amounts of the N596Q variant present at the plasma membrane compared to the glycosylated ABCG2 protein	1252:1371	Cell surface analysis of ABCG2 expression showed comparable amounts of the N596Q variant present at the plasma membrane compared to the glycosylated ABCG2 protein.
15807535	6	84	theme	ABCG2	1076:1080	arg1	variant					1090:1096	the glycosylation-deficient ABCG2 (N596Q) variant	1048:1096	the glycosylation-deficient ABCG2 (N596Q) variant	1048:1096	Immunoblot and pulse-chase analyses revealed that the glycosylation-deficient ABCG2 (N596Q) variant and the glycosylated parent transporter are expressed equivalently at steady state and have similar half-lives.
15807535	8	85	theme	ABCG2	1378:1382	arg1	variant					1392:1398	The ABCG2 (N596Q) variant	1374:1398	The ABCG2 (N596Q) variant	1374:1398	The ABCG2 (N596Q) variant is also functional, demonstrating rhodamine 123 transport in intact cells comparable to that in cells expressing glycosylated ABCG2.
15807535	8	85	theme	ABCG2	1378:1382	arg1	functional					1408:1417	functional	1408:1417	functional	1408:1417	The ABCG2 (N596Q) variant is also functional, demonstrating rhodamine 123 transport in intact cells comparable to that in cells expressing glycosylated ABCG2.
15807535	2	86	theme	expressed	363:371	arg1	ABCG2					373:377	Both transiently and stably expressed ABCG2	335:377	Both transiently and stably expressed ABCG2	335:377	Both transiently and stably expressed ABCG2 are glycosylated, and treatment with peptide N-glycosidase F reduces the apparent molecular mass on SDS-PAGE gels to approximately 60 kDa.
15807535	9	87	theme	ATPase	1648:1653	arg1	activities					1655:1664	ATPase activities	1648:1664	ATPase activities	1648:1664	Furthermore, in crude membrane preparations, neither the basal nor the prazosin-stimulated ( approximately 2-fold) ATPase activities of ABCG2 (N596Q) were affected compared to glycosylated ABCG2.
15807535	7	88	theme	plasma	1314:1319	arg1	membrane					1321:1328	the plasma membrane	1310:1328	the plasma membrane	1310:1328	Cell surface analysis of ABCG2 expression showed comparable amounts of the N596Q variant present at the plasma membrane compared to the glycosylated ABCG2 protein.
15807535	2	89	theme	peptide	416:422	arg1	F					438:438	peptide N-glycosidase F	416:438	peptide N-glycosidase F	416:438	Both transiently and stably expressed ABCG2 are glycosylated, and treatment with peptide N-glycosidase F reduces the apparent molecular mass on SDS-PAGE gels to approximately 60 kDa.
15807535	8	90	theme	N596Q	1385:1389	arg1	variant					1392:1398	The ABCG2 (N596Q) variant	1374:1398	The ABCG2 (N596Q) variant	1374:1398	The ABCG2 (N596Q) variant is also functional, demonstrating rhodamine 123 transport in intact cells comparable to that in cells expressing glycosylated ABCG2.
15807535	8	90	theme	N596Q	1385:1389	arg1	functional					1408:1417	functional	1408:1417	functional	1408:1417	The ABCG2 (N596Q) variant is also functional, demonstrating rhodamine 123 transport in intact cells comparable to that in cells expressing glycosylated ABCG2.
15807535	0	91	theme	ABC	36:38	arg1	ABCG2					52:56	the human ABC transporter ABCG2	26:56	the human ABC transporter ABCG2	26:56	N-Linked glycosylation of the human ABC transporter ABCG2 on asparagine 596 is not essential for expression, transport activity, or trafficking to the plasma membrane.
15807535	1	92	theme	multidrug	274:282	arg1	resistance					284:293	multidrug resistance	274:293	multidrug resistance to cells in culture	274:313	The human ATP-binding cassette half-transporter ABCG2 is a 72 kDa plasma membrane protein that can confer multidrug resistance to cells in culture when overexpressed.
15807535	2	93	theme	molecular	461:469	arg1	mass					471:474	the apparent molecular mass	448:474	the apparent molecular mass on SDS-PAGE gels	448:491	Both transiently and stably expressed ABCG2 are glycosylated, and treatment with peptide N-glycosidase F reduces the apparent molecular mass on SDS-PAGE gels to approximately 60 kDa.
15807535	4	94	gly	glycosylated	776:787	arg1	596					760:762	only asparagine 596	744:762	only asparagine 596	744:762	Site-directed mutagenesis experiments, in which each Asn was changed to Gln independently, revealed that only asparagine 596 is N-linked glycosylated.
15807535	7	95	theme	variant	1291:1297	arg1	amounts					1270:1276	comparable amounts	1259:1276	comparable amounts of the N596Q variant present at the plasma membrane	1259:1328	Cell surface analysis of ABCG2 expression showed comparable amounts of the N596Q variant present at the plasma membrane compared to the glycosylated ABCG2 protein.
15807535	7	95	theme	variant	1291:1297	arg1	variant					1291:1297	the N596Q variant	1281:1297	the N596Q variant present at the plasma membrane	1281:1328	Cell surface analysis of ABCG2 expression showed comparable amounts of the N596Q variant present at the plasma membrane compared to the glycosylated ABCG2 protein.
15807535	7	96	from	membrane	1321:1328	arg1	present					1299:1305	present	1299:1305	present	1299:1305	Cell surface analysis of ABCG2 expression showed comparable amounts of the N596Q variant present at the plasma membrane compared to the glycosylated ABCG2 protein.
15807535	6	97	theme	parent	1119:1124	arg1	transporter					1126:1136	the glycosylated parent transporter	1102:1136	the glycosylated parent transporter	1102:1136	Immunoblot and pulse-chase analyses revealed that the glycosylation-deficient ABCG2 (N596Q) variant and the glycosylated parent transporter are expressed equivalently at steady state and have similar half-lives.
15807535	5	98	theme	hydropathy	977:986	arg1	analysis					988:995	hydropathy analysis	977:995	hydropathy analysis	977:995	These data provide the first direct identification of the modified residue in ABCG2 and evidence for the localization of loop 5 to the extracellular space, previously only predicted from hydropathy analysis.
15807535	6	99	contain	have	1185:1188	arg2	half-lives					1198:1207	similar half-lives	1190:1207	similar half-lives	1190:1207	Immunoblot and pulse-chase analyses revealed that the glycosylation-deficient ABCG2 (N596Q) variant and the glycosylated parent transporter are expressed equivalently at steady state and have similar half-lives.
15807535	6	99	contain	have	1185:1188	arg1	variant					1090:1096	the glycosylation-deficient ABCG2 (N596Q) variant	1048:1096	the glycosylation-deficient ABCG2 (N596Q) variant	1048:1096	Immunoblot and pulse-chase analyses revealed that the glycosylation-deficient ABCG2 (N596Q) variant and the glycosylated parent transporter are expressed equivalently at steady state and have similar half-lives.
15807535	10	100	theme	plasma	1931:1936	arg1	membrane					1938:1945	the plasma membrane	1927:1945	the plasma membrane	1927:1945	Although subtle defects in transporter trafficking and function may exist, these data taken together suggest that N-glycosylation at arginine 596 is not essential for the expression, trafficking to the plasma membrane, or the overall function of ABCG2.
15807535	8	101	theme	rhodamine	1434:1442	arg1	transport					1448:1456	rhodamine 123 transport	1434:1456	rhodamine 123 transport in intact cells comparable to that in cells expressing glycosylated ABCG2	1434:1530	The ABCG2 (N596Q) variant is also functional, demonstrating rhodamine 123 transport in intact cells comparable to that in cells expressing glycosylated ABCG2.
15807535	10	102	gly	N-glycosylation	1843:1857	arg2	arginine					1862:1869	arginine 596	1862:1873	arginine 596	1862:1873	Although subtle defects in transporter trafficking and function may exist, these data taken together suggest that N-glycosylation at arginine 596 is not essential for the expression, trafficking to the plasma membrane, or the overall function of ABCG2.
15807535	10	102	gly	N-glycosylation	1843:1857	arg1	ABCG2					1975:1979	ABCG2	1975:1979	ABCG2	1975:1979	Although subtle defects in transporter trafficking and function may exist, these data taken together suggest that N-glycosylation at arginine 596 is not essential for the expression, trafficking to the plasma membrane, or the overall function of ABCG2.
15807535	10	102	gly	N-glycosylation	1843:1857	arg1	arginine					1862:1869	arginine 596	1862:1873	arginine 596	1862:1873	Although subtle defects in transporter trafficking and function may exist, these data taken together suggest that N-glycosylation at arginine 596 is not essential for the expression, trafficking to the plasma membrane, or the overall function of ABCG2.
24103369	2	0	theme	liver	327:331	arg1	diseases					333:340	liver diseases	327:340	liver diseases	327:340	In our previous report, the overall N-glycans of sera haptoglobin (Hp) β chain were found to be different in liver diseases.
24103369	6	1	theme	HCC	1124:1126	arg1	patients					1128:1135	LC and HCC patients	1117:1135	patients	1128:1135	The quantitative results revealed that the sialylation of NLFLN(207)HSEN(211)ATAK and the fucosylated structure at all glycopeptides increased significantly in LC and HCC patients compared with those in HBV patients and healthy individuals.
24103369	2	2	from	different	314:322	arg1	diseases					333:340	liver diseases	327:340	liver diseases	327:340	In our previous report, the overall N-glycans of sera haptoglobin (Hp) β chain were found to be different in liver diseases.
24103369	6	3	theme	LC	1117:1118	arg1	patients					1128:1135	LC and HCC patients	1117:1135	patients	1128:1135	The quantitative results revealed that the sialylation of NLFLN(207)HSEN(211)ATAK and the fucosylated structure at all glycopeptides increased significantly in LC and HCC patients compared with those in HBV patients and healthy individuals.
24103369	5	4	theme	hepatitis	575:583	arg1	HBV					594:596	HBV	594:596	HBV	594:596	Sera Hp β chain in healthy individuals as well as patients with hepatitis B virus (HBV), liver cirrhosis (LC) and hepatocellular carcinoma (HCC) were purified, digested and subjected to liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry, which allowed identification and structure determination of the glycopeptide, as well as the relative quantification of glycans present on each glycopeptide.
24103369	5	4	theme	hepatitis	575:583	arg1	virus					587:591	hepatitis B virus	575:591	hepatitis B virus (HBV)	575:597	Sera Hp β chain in healthy individuals as well as patients with hepatitis B virus (HBV), liver cirrhosis (LC) and hepatocellular carcinoma (HCC) were purified, digested and subjected to liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry, which allowed identification and structure determination of the glycopeptide, as well as the relative quantification of glycans present on each glycopeptide.
24103369	2	5	theme	haptoglobin	272:282	arg1	chain					291:295	sera haptoglobin (Hp) β chain	267:295	sera haptoglobin (Hp) β chain	267:295	In our previous report, the overall N-glycans of sera haptoglobin (Hp) β chain were found to be different in liver diseases.
24103369	1	6	theme	clinical	183:190	arg1	application					192:202	clinical application	183:202	clinical application	183:202	The site-specific characterization of N-glycans in glycoproteins with the potential of clinical application is important.
24103369	6	7	theme	healthy	1177:1183	arg1	individuals					1185:1195	healthy individuals	1177:1195	healthy individuals	1177:1195	The quantitative results revealed that the sialylation of NLFLN(207)HSEN(211)ATAK and the fucosylated structure at all glycopeptides increased significantly in LC and HCC patients compared with those in HBV patients and healthy individuals.
24103369	5	8	theme	structure	832:840	arg1	determination					842:854	structure determination	832:854	structure determination	832:854	Sera Hp β chain in healthy individuals as well as patients with hepatitis B virus (HBV), liver cirrhosis (LC) and hepatocellular carcinoma (HCC) were purified, digested and subjected to liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry, which allowed identification and structure determination of the glycopeptide, as well as the relative quantification of glycans present on each glycopeptide.
24103369	1	9	from	characterization	114:129	arg1	glycoproteins					147:159	glycoproteins	147:159	glycoproteins with the potential of clinical application	147:202	The site-specific characterization of N-glycans in glycoproteins with the potential of clinical application is important.
24103369	3	10	contain	contains	354:361	arg2	N-glycosylation					387:401	N-glycosylation	387:401	N-glycosylation	387:401	Hp β chain contains four potential sites of N-glycosylation.
24103369	3	10	contain	contains	354:361	arg2	sites					378:382	four potential sites	363:382	four potential sites of N-glycosylation	363:401	Hp β chain contains four potential sites of N-glycosylation.
24103369	3	10	contain	contains	354:361	arg1	chain					348:352	Hp β chain	343:352	Hp β chain	343:352	Hp β chain contains four potential sites of N-glycosylation.
24103369	6	11	gly	glycopeptides	1076:1088	arg2	glycopeptides					1076:1088	all glycopeptides	1072:1088	all glycopeptides	1072:1088	The quantitative results revealed that the sialylation of NLFLN(207)HSEN(211)ATAK and the fucosylated structure at all glycopeptides increased significantly in LC and HCC patients compared with those in HBV patients and healthy individuals.
24103369	2	12	theme	β	289:289	arg1	chain					291:295	sera haptoglobin (Hp) β chain	267:295	sera haptoglobin (Hp) β chain	267:295	In our previous report, the overall N-glycans of sera haptoglobin (Hp) β chain were found to be different in liver diseases.
24103369	5	13	theme	collision	757:765	arg1	spectrometry					785:796	liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry	697:796	liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry	697:796	Sera Hp β chain in healthy individuals as well as patients with hepatitis B virus (HBV), liver cirrhosis (LC) and hepatocellular carcinoma (HCC) were purified, digested and subjected to liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry, which allowed identification and structure determination of the glycopeptide, as well as the relative quantification of glycans present on each glycopeptide.
24103369	5	14	with	patients	561:568	arg1	carcinoma					640:648	hepatocellular carcinoma	625:648	hepatocellular carcinoma (HCC)	625:654	Sera Hp β chain in healthy individuals as well as patients with hepatitis B virus (HBV), liver cirrhosis (LC) and hepatocellular carcinoma (HCC) were purified, digested and subjected to liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry, which allowed identification and structure determination of the glycopeptide, as well as the relative quantification of glycans present on each glycopeptide.
24103369	5	14	with	patients	561:568	arg1	virus					587:591	hepatitis B virus	575:591	hepatitis B virus (HBV)	575:597	Sera Hp β chain in healthy individuals as well as patients with hepatitis B virus (HBV), liver cirrhosis (LC) and hepatocellular carcinoma (HCC) were purified, digested and subjected to liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry, which allowed identification and structure determination of the glycopeptide, as well as the relative quantification of glycans present on each glycopeptide.
24103369	5	14	with	patients	561:568	arg1	cirrhosis					606:614	liver cirrhosis	600:614	liver cirrhosis (LC)	600:619	Sera Hp β chain in healthy individuals as well as patients with hepatitis B virus (HBV), liver cirrhosis (LC) and hepatocellular carcinoma (HCC) were purified, digested and subjected to liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry, which allowed identification and structure determination of the glycopeptide, as well as the relative quantification of glycans present on each glycopeptide.
24103369	5	14	with	patients	561:568	arg1	LC					617:618	LC	617:618	LC	617:618	Sera Hp β chain in healthy individuals as well as patients with hepatitis B virus (HBV), liver cirrhosis (LC) and hepatocellular carcinoma (HCC) were purified, digested and subjected to liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry, which allowed identification and structure determination of the glycopeptide, as well as the relative quantification of glycans present on each glycopeptide.
24103369	5	14	with	patients	561:568	arg1	HCC					651:653	HCC	651:653	HCC	651:653	Sera Hp β chain in healthy individuals as well as patients with hepatitis B virus (HBV), liver cirrhosis (LC) and hepatocellular carcinoma (HCC) were purified, digested and subjected to liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry, which allowed identification and structure determination of the glycopeptide, as well as the relative quantification of glycans present on each glycopeptide.
24103369	5	14	with	patients	561:568	arg1	HBV					594:596	HBV	594:596	HBV	594:596	Sera Hp β chain in healthy individuals as well as patients with hepatitis B virus (HBV), liver cirrhosis (LC) and hepatocellular carcinoma (HCC) were purified, digested and subjected to liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry, which allowed identification and structure determination of the glycopeptide, as well as the relative quantification of glycans present on each glycopeptide.
24103369	6	15	theme	HBV	1160:1162	arg1	patients					1164:1171	HBV patients	1160:1171	HBV patients	1160:1171	The quantitative results revealed that the sialylation of NLFLN(207)HSEN(211)ATAK and the fucosylated structure at all glycopeptides increased significantly in LC and HCC patients compared with those in HBV patients and healthy individuals.
24103369	1	16	gly	glycoproteins	147:159	arg1	glycoproteins					147:159	glycoproteins	147:159	glycoproteins with the potential of clinical application	147:202	The site-specific characterization of N-glycans in glycoproteins with the potential of clinical application is important.
24103369	2	17	theme	previous	225:232	arg1	report					234:239	our previous report	221:239	our previous report	221:239	In our previous report, the overall N-glycans of sera haptoglobin (Hp) β chain were found to be different in liver diseases.
24103369	5	18	theme	Hp	516:517	arg1	chain					521:525	Sera Hp β chain	511:525	Sera Hp β chain in healthy individuals as well as patients with hepatitis B virus (HBV), liver cirrhosis (LC) and hepatocellular carcinoma (HCC)	511:654	Sera Hp β chain in healthy individuals as well as patients with hepatitis B virus (HBV), liver cirrhosis (LC) and hepatocellular carcinoma (HCC) were purified, digested and subjected to liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry, which allowed identification and structure determination of the glycopeptide, as well as the relative quantification of glycans present on each glycopeptide.
24103369	5	19	gly	glycopeptide	863:874	arg2	glycopeptide					863:874	the glycopeptide	859:874	the glycopeptide	859:874	Sera Hp β chain in healthy individuals as well as patients with hepatitis B virus (HBV), liver cirrhosis (LC) and hepatocellular carcinoma (HCC) were purified, digested and subjected to liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry, which allowed identification and structure determination of the glycopeptide, as well as the relative quantification of glycans present on each glycopeptide.
24103369	8	20	theme	early	1378:1382	arg1	hepatocarcinogenesis					1384:1403	early hepatocarcinogenesis	1378:1403	early hepatocarcinogenesis	1378:1403	Thus, the sialylated and fucosylated glycoforms of Hp β chain might be related to early hepatocarcinogenesis and also might be useful as novel differential markers for LC and HCC patients.
24103369	5	21	from	chain	521:525	arg1	individuals					538:548	healthy individuals	530:548	healthy individuals as well as patients with hepatitis B virus (HBV), liver cirrhosis (LC) and hepatocellular carcinoma (HCC)	530:654	Sera Hp β chain in healthy individuals as well as patients with hepatitis B virus (HBV), liver cirrhosis (LC) and hepatocellular carcinoma (HCC) were purified, digested and subjected to liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry, which allowed identification and structure determination of the glycopeptide, as well as the relative quantification of glycans present on each glycopeptide.
24103369	5	21	from	chain	521:525	arg1	patients					561:568	patients	561:568	healthy individuals as well as patients with hepatitis B virus (HBV), liver cirrhosis (LC) and hepatocellular carcinoma (HCC)	530:654	Sera Hp β chain in healthy individuals as well as patients with hepatitis B virus (HBV), liver cirrhosis (LC) and hepatocellular carcinoma (HCC) were purified, digested and subjected to liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry, which allowed identification and structure determination of the glycopeptide, as well as the relative quantification of glycans present on each glycopeptide.
24103369	0	22	theme	β	69:69	arg1	chain					71:75	sera haptoglobin β chain	52:75	sera haptoglobin β chain in liver diseases	52:93	Quantitative analysis of site-specific N-glycans on sera haptoglobin β chain in liver diseases.
24103369	2	23	theme	overall	246:252	arg1	different					314:322	different	314:322	different	314:322	In our previous report, the overall N-glycans of sera haptoglobin (Hp) β chain were found to be different in liver diseases.
24103369	2	23	theme	overall	246:252	arg1	N-glycans					254:262	the overall N-glycans	242:262	the overall N-glycans of sera haptoglobin (Hp) β chain	242:295	In our previous report, the overall N-glycans of sera haptoglobin (Hp) β chain were found to be different in liver diseases.
24103369	5	24	theme	glycopeptide	863:874	arg1	quantification					901:914	the relative quantification	888:914	the relative quantification of glycans present on each glycopeptide	888:954	Sera Hp β chain in healthy individuals as well as patients with hepatitis B virus (HBV), liver cirrhosis (LC) and hepatocellular carcinoma (HCC) were purified, digested and subjected to liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry, which allowed identification and structure determination of the glycopeptide, as well as the relative quantification of glycans present on each glycopeptide.
24103369	5	24	theme	glycopeptide	863:874	arg1	identification					813:826	identification	813:826	identification	813:826	Sera Hp β chain in healthy individuals as well as patients with hepatitis B virus (HBV), liver cirrhosis (LC) and hepatocellular carcinoma (HCC) were purified, digested and subjected to liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry, which allowed identification and structure determination of the glycopeptide, as well as the relative quantification of glycans present on each glycopeptide.
24103369	5	24	theme	glycopeptide	863:874	arg1	determination					842:854	structure determination	832:854	structure determination	832:854	Sera Hp β chain in healthy individuals as well as patients with hepatitis B virus (HBV), liver cirrhosis (LC) and hepatocellular carcinoma (HCC) were purified, digested and subjected to liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry, which allowed identification and structure determination of the glycopeptide, as well as the relative quantification of glycans present on each glycopeptide.
24103369	4	25	theme	β	475:475	arg1	chain					477:481	Hp β chain	472:481	Hp β chain	472:481	In this study, we investigated the potential change of N-glycans on Hp β chain in a site-specific fashion.
24103369	5	26	theme	present	927:933	arg1	glycans					919:925	glycans	919:925	glycans present on each glycopeptide	919:954	Sera Hp β chain in healthy individuals as well as patients with hepatitis B virus (HBV), liver cirrhosis (LC) and hepatocellular carcinoma (HCC) were purified, digested and subjected to liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry, which allowed identification and structure determination of the glycopeptide, as well as the relative quantification of glycans present on each glycopeptide.
24103369	7	27	from	diseases	1266:1273	arg1	patterns					1226:1233	different N-glycan patterns	1207:1233	different N-glycan patterns of Hp β chain in various liver diseases	1207:1273	A set of different N-glycan patterns of Hp β chain in various liver diseases has been determined.
24103369	4	28	theme	potential	439:447	arg1	change					449:454	the potential change	435:454	the potential change of N-glycans on Hp β chain	435:481	In this study, we investigated the potential change of N-glycans on Hp β chain in a site-specific fashion.
24103369	7	29	theme	β	1241:1241	arg1	chain					1243:1247	Hp β chain	1238:1247	Hp β chain in various liver diseases	1238:1273	A set of different N-glycan patterns of Hp β chain in various liver diseases has been determined.
24103369	7	30	theme	liver	1260:1264	arg1	diseases					1266:1273	various liver diseases	1252:1273	various liver diseases	1252:1273	A set of different N-glycan patterns of Hp β chain in various liver diseases has been determined.
24103369	0	31	theme	Quantitative	0:11	arg1	analysis					13:20	Quantitative analysis	0:20	Quantitative analysis of site-specific N-glycans on sera haptoglobin β chain in liver diseases.	0:94	Quantitative analysis of site-specific N-glycans on sera haptoglobin β chain in liver diseases.
24103369	5	32	theme	healthy	530:536	arg1	individuals					538:548	healthy individuals	530:548	healthy individuals as well as patients with hepatitis B virus (HBV), liver cirrhosis (LC) and hepatocellular carcinoma (HCC)	530:654	Sera Hp β chain in healthy individuals as well as patients with hepatitis B virus (HBV), liver cirrhosis (LC) and hepatocellular carcinoma (HCC) were purified, digested and subjected to liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry, which allowed identification and structure determination of the glycopeptide, as well as the relative quantification of glycans present on each glycopeptide.
24103369	5	33	theme	relative	892:899	arg1	quantification					901:914	the relative quantification	888:914	the relative quantification of glycans present on each glycopeptide	888:954	Sera Hp β chain in healthy individuals as well as patients with hepatitis B virus (HBV), liver cirrhosis (LC) and hepatocellular carcinoma (HCC) were purified, digested and subjected to liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry, which allowed identification and structure determination of the glycopeptide, as well as the relative quantification of glycans present on each glycopeptide.
24103369	3	34	theme	β	346:346	arg1	chain					348:352	Hp β chain	343:352	Hp β chain	343:352	Hp β chain contains four potential sites of N-glycosylation.
24103369	2	35	located	found	302:306	arg2	N-glycans					254:262	the overall N-glycans	242:262	the overall N-glycans of sera haptoglobin (Hp) β chain	242:295	In our previous report, the overall N-glycans of sera haptoglobin (Hp) β chain were found to be different in liver diseases.
24103369	2	35	located	found	302:306	arg1	report					234:239	our previous report	221:239	our previous report	221:239	In our previous report, the overall N-glycans of sera haptoglobin (Hp) β chain were found to be different in liver diseases.
24103369	2	35	located	found	302:306	arg2	different					314:322	different	314:322	different	314:322	In our previous report, the overall N-glycans of sera haptoglobin (Hp) β chain were found to be different in liver diseases.
24103369	5	36	theme	dissociation	767:778	arg1	spectrometry					785:796	liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry	697:796	liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry	697:796	Sera Hp β chain in healthy individuals as well as patients with hepatitis B virus (HBV), liver cirrhosis (LC) and hepatocellular carcinoma (HCC) were purified, digested and subjected to liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry, which allowed identification and structure determination of the glycopeptide, as well as the relative quantification of glycans present on each glycopeptide.
24103369	1	37	theme	site-specific	100:112	arg1	characterization					114:129	The site-specific characterization	96:129	The site-specific characterization of N-glycans in glycoproteins with the potential of clinical application	96:202	The site-specific characterization of N-glycans in glycoproteins with the potential of clinical application is important.
24103369	1	37	theme	site-specific	100:112	arg1	important					207:215	important	207:215	important	207:215	The site-specific characterization of N-glycans in glycoproteins with the potential of clinical application is important.
24103369	6	38	theme	NLFLN	1015:1019	arg1	ATAK					1034:1037	NLFLN(207)HSEN(211)ATAK	1015:1037	NLFLN(207)HSEN(211)ATAK	1015:1037	The quantitative results revealed that the sialylation of NLFLN(207)HSEN(211)ATAK and the fucosylated structure at all glycopeptides increased significantly in LC and HCC patients compared with those in HBV patients and healthy individuals.
24103369	8	39	theme	HCC	1471:1473	arg1	patients					1475:1482	HCC patients	1471:1482	HCC patients	1471:1482	Thus, the sialylated and fucosylated glycoforms of Hp β chain might be related to early hepatocarcinogenesis and also might be useful as novel differential markers for LC and HCC patients.
24103369	6	40	gly	sialylation	1000:1010	arg1	ATAK					1034:1037	NLFLN(207)HSEN(211)ATAK	1015:1037	NLFLN(207)HSEN(211)ATAK	1015:1037	The quantitative results revealed that the sialylation of NLFLN(207)HSEN(211)ATAK and the fucosylated structure at all glycopeptides increased significantly in LC and HCC patients compared with those in HBV patients and healthy individuals.
24103369	6	40	gly	sialylation	1000:1010	arg1	glycopeptides					1076:1088	all glycopeptides	1072:1088	all glycopeptides	1072:1088	The quantitative results revealed that the sialylation of NLFLN(207)HSEN(211)ATAK and the fucosylated structure at all glycopeptides increased significantly in LC and HCC patients compared with those in HBV patients and healthy individuals.
24103369	0	41	theme	N-glycans	39:47	arg1	analysis					13:20	Quantitative analysis	0:20	Quantitative analysis of site-specific N-glycans on sera haptoglobin β chain in liver diseases.	0:94	Quantitative analysis of site-specific N-glycans on sera haptoglobin β chain in liver diseases.
24103369	3	42	theme	N-glycosylation	387:401	arg1	sites					378:382	four potential sites	363:382	four potential sites of N-glycosylation	363:401	Hp β chain contains four potential sites of N-glycosylation.
24103369	3	42	theme	N-glycosylation	387:401	arg1	N-glycosylation					387:401	N-glycosylation	387:401	N-glycosylation	387:401	Hp β chain contains four potential sites of N-glycosylation.
24103369	7	43	from	patterns	1226:1233	arg1	diseases					1266:1273	various liver diseases	1252:1273	various liver diseases	1252:1273	A set of different N-glycan patterns of Hp β chain in various liver diseases has been determined.
24103369	3	44	theme	potential	368:376	arg1	sites					378:382	four potential sites	363:382	four potential sites of N-glycosylation	363:401	Hp β chain contains four potential sites of N-glycosylation.
24103369	3	44	theme	potential	368:376	arg1	N-glycosylation					387:401	N-glycosylation	387:401	N-glycosylation	387:401	Hp β chain contains four potential sites of N-glycosylation.
24103369	5	45	theme	chromatography-electrospray	704:730	arg1	spectrometry					785:796	liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry	697:796	liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry	697:796	Sera Hp β chain in healthy individuals as well as patients with hepatitis B virus (HBV), liver cirrhosis (LC) and hepatocellular carcinoma (HCC) were purified, digested and subjected to liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry, which allowed identification and structure determination of the glycopeptide, as well as the relative quantification of glycans present on each glycopeptide.
24103369	7	46	theme	N-glycan	1217:1224	arg1	patterns					1226:1233	different N-glycan patterns	1207:1233	different N-glycan patterns of Hp β chain in various liver diseases	1207:1273	A set of different N-glycan patterns of Hp β chain in various liver diseases has been determined.
24103369	4	47	theme	site-specific	488:500	arg1	fashion					502:508	a site-specific fashion	486:508	a site-specific fashion	486:508	In this study, we investigated the potential change of N-glycans on Hp β chain in a site-specific fashion.
24103369	8	48	theme	Hp	1347:1348	arg1	chain					1352:1356	Hp β chain	1347:1356	Hp β chain	1347:1356	Thus, the sialylated and fucosylated glycoforms of Hp β chain might be related to early hepatocarcinogenesis and also might be useful as novel differential markers for LC and HCC patients.
24103369	8	49	gly	sialylated	1306:1315	arg1	useful					1423:1428	useful	1423:1428	useful	1423:1428	Thus, the sialylated and fucosylated glycoforms of Hp β chain might be related to early hepatocarcinogenesis and also might be useful as novel differential markers for LC and HCC patients.
24103369	8	49	gly	sialylated	1306:1315	arg1	related					1367:1373	related	1367:1373	related	1367:1373	Thus, the sialylated and fucosylated glycoforms of Hp β chain might be related to early hepatocarcinogenesis and also might be useful as novel differential markers for LC and HCC patients.
24103369	8	49	gly	sialylated	1306:1315	arg1	glycoforms					1333:1342	the sialylated and fucosylated glycoforms	1302:1342	the sialylated and fucosylated glycoforms of Hp β chain	1302:1356	Thus, the sialylated and fucosylated glycoforms of Hp β chain might be related to early hepatocarcinogenesis and also might be useful as novel differential markers for LC and HCC patients.
24103369	8	49	gly	sialylated	1306:1315	arg1	chain					1352:1356	Hp β chain	1347:1356	Hp β chain	1347:1356	Thus, the sialylated and fucosylated glycoforms of Hp β chain might be related to early hepatocarcinogenesis and also might be useful as novel differential markers for LC and HCC patients.
24103369	7	50	from	chain	1243:1247	arg1	diseases					1266:1273	various liver diseases	1252:1273	various liver diseases	1252:1273	A set of different N-glycan patterns of Hp β chain in various liver diseases has been determined.
24103369	8	51	theme	chain	1352:1356	arg1	useful					1423:1428	useful	1423:1428	useful	1423:1428	Thus, the sialylated and fucosylated glycoforms of Hp β chain might be related to early hepatocarcinogenesis and also might be useful as novel differential markers for LC and HCC patients.
24103369	8	51	theme	chain	1352:1356	arg1	related					1367:1373	related	1367:1373	related	1367:1373	Thus, the sialylated and fucosylated glycoforms of Hp β chain might be related to early hepatocarcinogenesis and also might be useful as novel differential markers for LC and HCC patients.
24103369	8	51	theme	chain	1352:1356	arg1	glycoforms					1333:1342	the sialylated and fucosylated glycoforms	1302:1342	the sialylated and fucosylated glycoforms of Hp β chain	1302:1356	Thus, the sialylated and fucosylated glycoforms of Hp β chain might be related to early hepatocarcinogenesis and also might be useful as novel differential markers for LC and HCC patients.
24103369	8	52	gly	fucosylated	1321:1331	arg1	useful					1423:1428	useful	1423:1428	useful	1423:1428	Thus, the sialylated and fucosylated glycoforms of Hp β chain might be related to early hepatocarcinogenesis and also might be useful as novel differential markers for LC and HCC patients.
24103369	8	52	gly	fucosylated	1321:1331	arg1	related					1367:1373	related	1367:1373	related	1367:1373	Thus, the sialylated and fucosylated glycoforms of Hp β chain might be related to early hepatocarcinogenesis and also might be useful as novel differential markers for LC and HCC patients.
24103369	8	52	gly	fucosylated	1321:1331	arg1	glycoforms					1333:1342	the sialylated and fucosylated glycoforms	1302:1342	the sialylated and fucosylated glycoforms of Hp β chain	1302:1356	Thus, the sialylated and fucosylated glycoforms of Hp β chain might be related to early hepatocarcinogenesis and also might be useful as novel differential markers for LC and HCC patients.
24103369	8	52	gly	fucosylated	1321:1331	arg1	chain					1352:1356	Hp β chain	1347:1356	Hp β chain	1347:1356	Thus, the sialylated and fucosylated glycoforms of Hp β chain might be related to early hepatocarcinogenesis and also might be useful as novel differential markers for LC and HCC patients.
24103369	5	53	theme	liquid	697:702	arg1	spectrometry					785:796	liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry	697:796	liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry	697:796	Sera Hp β chain in healthy individuals as well as patients with hepatitis B virus (HBV), liver cirrhosis (LC) and hepatocellular carcinoma (HCC) were purified, digested and subjected to liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry, which allowed identification and structure determination of the glycopeptide, as well as the relative quantification of glycans present on each glycopeptide.
24103369	6	54	theme	ATAK	1034:1037	arg1	sialylation					1000:1010	the sialylation	996:1010	the sialylation of NLFLN(207)HSEN(211)ATAK	996:1037	The quantitative results revealed that the sialylation of NLFLN(207)HSEN(211)ATAK and the fucosylated structure at all glycopeptides increased significantly in LC and HCC patients compared with those in HBV patients and healthy individuals.
24103369	6	54	theme	ATAK	1034:1037	arg1	structure					1059:1067	the fucosylated structure	1043:1067	the fucosylated structure at all glycopeptides	1043:1088	The quantitative results revealed that the sialylation of NLFLN(207)HSEN(211)ATAK and the fucosylated structure at all glycopeptides increased significantly in LC and HCC patients compared with those in HBV patients and healthy individuals.
24103369	4	55	from	change	449:454	arg1	chain					477:481	Hp β chain	472:481	Hp β chain	472:481	In this study, we investigated the potential change of N-glycans on Hp β chain in a site-specific fashion.
24103369	0	56	theme	sera	52:55	arg1	chain					71:75	sera haptoglobin β chain	52:75	sera haptoglobin β chain in liver diseases	52:93	Quantitative analysis of site-specific N-glycans on sera haptoglobin β chain in liver diseases.
24103369	2	57	from	diseases	333:340	arg1	different					314:322	different	314:322	different	314:322	In our previous report, the overall N-glycans of sera haptoglobin (Hp) β chain were found to be different in liver diseases.
24103369	2	57	from	diseases	333:340	arg1	N-glycans					254:262	the overall N-glycans	242:262	the overall N-glycans of sera haptoglobin (Hp) β chain	242:295	In our previous report, the overall N-glycans of sera haptoglobin (Hp) β chain were found to be different in liver diseases.
24103369	5	58	theme	B	585:585	arg1	HBV					594:596	HBV	594:596	HBV	594:596	Sera Hp β chain in healthy individuals as well as patients with hepatitis B virus (HBV), liver cirrhosis (LC) and hepatocellular carcinoma (HCC) were purified, digested and subjected to liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry, which allowed identification and structure determination of the glycopeptide, as well as the relative quantification of glycans present on each glycopeptide.
24103369	5	58	theme	B	585:585	arg1	virus					587:591	hepatitis B virus	575:591	hepatitis B virus (HBV)	575:597	Sera Hp β chain in healthy individuals as well as patients with hepatitis B virus (HBV), liver cirrhosis (LC) and hepatocellular carcinoma (HCC) were purified, digested and subjected to liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry, which allowed identification and structure determination of the glycopeptide, as well as the relative quantification of glycans present on each glycopeptide.
24103369	1	59	theme	application	192:202	arg1	potential					170:178	the potential	166:178	the potential of clinical application	166:202	The site-specific characterization of N-glycans in glycoproteins with the potential of clinical application is important.
24103369	5	60	attach	present	927:933	arg1	glycopeptide					943:954	each glycopeptide	938:954	each glycopeptide	938:954	Sera Hp β chain in healthy individuals as well as patients with hepatitis B virus (HBV), liver cirrhosis (LC) and hepatocellular carcinoma (HCC) were purified, digested and subjected to liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry, which allowed identification and structure determination of the glycopeptide, as well as the relative quantification of glycans present on each glycopeptide.
24103369	5	60	attach	present	927:933	arg2	glycans					919:925	glycans	919:925	glycans present on each glycopeptide	919:954	Sera Hp β chain in healthy individuals as well as patients with hepatitis B virus (HBV), liver cirrhosis (LC) and hepatocellular carcinoma (HCC) were purified, digested and subjected to liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry, which allowed identification and structure determination of the glycopeptide, as well as the relative quantification of glycans present on each glycopeptide.
24103369	2	61	theme	chain	291:295	arg1	different					314:322	different	314:322	different	314:322	In our previous report, the overall N-glycans of sera haptoglobin (Hp) β chain were found to be different in liver diseases.
24103369	2	61	theme	chain	291:295	arg1	N-glycans					254:262	the overall N-glycans	242:262	the overall N-glycans of sera haptoglobin (Hp) β chain	242:295	In our previous report, the overall N-glycans of sera haptoglobin (Hp) β chain were found to be different in liver diseases.
24103369	5	62	theme	mass	780:783	arg1	spectrometry					785:796	liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry	697:796	liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry	697:796	Sera Hp β chain in healthy individuals as well as patients with hepatitis B virus (HBV), liver cirrhosis (LC) and hepatocellular carcinoma (HCC) were purified, digested and subjected to liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry, which allowed identification and structure determination of the glycopeptide, as well as the relative quantification of glycans present on each glycopeptide.
24103369	5	63	theme	hepatocellular	625:638	arg1	HCC					651:653	HCC	651:653	HCC	651:653	Sera Hp β chain in healthy individuals as well as patients with hepatitis B virus (HBV), liver cirrhosis (LC) and hepatocellular carcinoma (HCC) were purified, digested and subjected to liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry, which allowed identification and structure determination of the glycopeptide, as well as the relative quantification of glycans present on each glycopeptide.
24103369	5	63	theme	hepatocellular	625:638	arg1	carcinoma					640:648	hepatocellular carcinoma	625:648	hepatocellular carcinoma (HCC)	625:654	Sera Hp β chain in healthy individuals as well as patients with hepatitis B virus (HBV), liver cirrhosis (LC) and hepatocellular carcinoma (HCC) were purified, digested and subjected to liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry, which allowed identification and structure determination of the glycopeptide, as well as the relative quantification of glycans present on each glycopeptide.
24103369	0	64	from	chain	71:75	arg1	diseases					86:93	liver diseases	80:93	liver diseases	80:93	Quantitative analysis of site-specific N-glycans on sera haptoglobin β chain in liver diseases.
24103369	5	65	theme	liver	600:604	arg1	LC					617:618	LC	617:618	LC	617:618	Sera Hp β chain in healthy individuals as well as patients with hepatitis B virus (HBV), liver cirrhosis (LC) and hepatocellular carcinoma (HCC) were purified, digested and subjected to liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry, which allowed identification and structure determination of the glycopeptide, as well as the relative quantification of glycans present on each glycopeptide.
24103369	5	65	theme	liver	600:604	arg1	cirrhosis					606:614	liver cirrhosis	600:614	liver cirrhosis (LC)	600:619	Sera Hp β chain in healthy individuals as well as patients with hepatitis B virus (HBV), liver cirrhosis (LC) and hepatocellular carcinoma (HCC) were purified, digested and subjected to liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry, which allowed identification and structure determination of the glycopeptide, as well as the relative quantification of glycans present on each glycopeptide.
24103369	5	66	with	individuals	538:548	arg1	carcinoma					640:648	hepatocellular carcinoma	625:648	hepatocellular carcinoma (HCC)	625:654	Sera Hp β chain in healthy individuals as well as patients with hepatitis B virus (HBV), liver cirrhosis (LC) and hepatocellular carcinoma (HCC) were purified, digested and subjected to liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry, which allowed identification and structure determination of the glycopeptide, as well as the relative quantification of glycans present on each glycopeptide.
24103369	5	66	with	individuals	538:548	arg1	virus					587:591	hepatitis B virus	575:591	hepatitis B virus (HBV)	575:597	Sera Hp β chain in healthy individuals as well as patients with hepatitis B virus (HBV), liver cirrhosis (LC) and hepatocellular carcinoma (HCC) were purified, digested and subjected to liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry, which allowed identification and structure determination of the glycopeptide, as well as the relative quantification of glycans present on each glycopeptide.
24103369	5	66	with	individuals	538:548	arg1	cirrhosis					606:614	liver cirrhosis	600:614	liver cirrhosis (LC)	600:619	Sera Hp β chain in healthy individuals as well as patients with hepatitis B virus (HBV), liver cirrhosis (LC) and hepatocellular carcinoma (HCC) were purified, digested and subjected to liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry, which allowed identification and structure determination of the glycopeptide, as well as the relative quantification of glycans present on each glycopeptide.
24103369	5	66	with	individuals	538:548	arg1	LC					617:618	LC	617:618	LC	617:618	Sera Hp β chain in healthy individuals as well as patients with hepatitis B virus (HBV), liver cirrhosis (LC) and hepatocellular carcinoma (HCC) were purified, digested and subjected to liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry, which allowed identification and structure determination of the glycopeptide, as well as the relative quantification of glycans present on each glycopeptide.
24103369	5	66	with	individuals	538:548	arg1	HCC					651:653	HCC	651:653	HCC	651:653	Sera Hp β chain in healthy individuals as well as patients with hepatitis B virus (HBV), liver cirrhosis (LC) and hepatocellular carcinoma (HCC) were purified, digested and subjected to liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry, which allowed identification and structure determination of the glycopeptide, as well as the relative quantification of glycans present on each glycopeptide.
24103369	5	66	with	individuals	538:548	arg1	HBV					594:596	HBV	594:596	HBV	594:596	Sera Hp β chain in healthy individuals as well as patients with hepatitis B virus (HBV), liver cirrhosis (LC) and hepatocellular carcinoma (HCC) were purified, digested and subjected to liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry, which allowed identification and structure determination of the glycopeptide, as well as the relative quantification of glycans present on each glycopeptide.
24103369	5	67	theme	Sera	511:514	arg1	chain					521:525	Sera Hp β chain	511:525	Sera Hp β chain in healthy individuals as well as patients with hepatitis B virus (HBV), liver cirrhosis (LC) and hepatocellular carcinoma (HCC)	511:654	Sera Hp β chain in healthy individuals as well as patients with hepatitis B virus (HBV), liver cirrhosis (LC) and hepatocellular carcinoma (HCC) were purified, digested and subjected to liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry, which allowed identification and structure determination of the glycopeptide, as well as the relative quantification of glycans present on each glycopeptide.
24103369	2	68	theme	sera	267:270	arg1	Hp					285:286	Hp	285:286	Hp	285:286	In our previous report, the overall N-glycans of sera haptoglobin (Hp) β chain were found to be different in liver diseases.
24103369	2	68	theme	sera	267:270	arg1	haptoglobin					272:282	sera haptoglobin	267:282	sera haptoglobin (Hp) β chain	267:295	In our previous report, the overall N-glycans of sera haptoglobin (Hp) β chain were found to be different in liver diseases.
24103369	5	69	theme	β	519:519	arg1	chain					521:525	Sera Hp β chain	511:525	Sera Hp β chain in healthy individuals as well as patients with hepatitis B virus (HBV), liver cirrhosis (LC) and hepatocellular carcinoma (HCC)	511:654	Sera Hp β chain in healthy individuals as well as patients with hepatitis B virus (HBV), liver cirrhosis (LC) and hepatocellular carcinoma (HCC) were purified, digested and subjected to liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry, which allowed identification and structure determination of the glycopeptide, as well as the relative quantification of glycans present on each glycopeptide.
24103369	1	70	theme	N-glycans	134:142	arg1	characterization					114:129	The site-specific characterization	96:129	The site-specific characterization of N-glycans in glycoproteins with the potential of clinical application	96:202	The site-specific characterization of N-glycans in glycoproteins with the potential of clinical application is important.
24103369	1	70	theme	N-glycans	134:142	arg1	important					207:215	important	207:215	important	207:215	The site-specific characterization of N-glycans in glycoproteins with the potential of clinical application is important.
24103369	4	71	theme	Hp	472:473	arg1	chain					477:481	Hp β chain	472:481	Hp β chain	472:481	In this study, we investigated the potential change of N-glycans on Hp β chain in a site-specific fashion.
24103369	0	72	theme	liver	80:84	arg1	diseases					86:93	liver diseases	80:93	liver diseases	80:93	Quantitative analysis of site-specific N-glycans on sera haptoglobin β chain in liver diseases.
24103369	3	73	gly	N-glycosylation	387:401	arg2	N-glycosylation					387:401	N-glycosylation	387:401	N-glycosylation	387:401	Hp β chain contains four potential sites of N-glycosylation.
24103369	3	73	gly	N-glycosylation	387:401	arg2	sites					378:382	four potential sites	363:382	four potential sites of N-glycosylation	363:401	Hp β chain contains four potential sites of N-glycosylation.
24103369	6	74	theme	quantitative	961:972	arg1	results					974:980	The quantitative results	957:980	The quantitative results	957:980	The quantitative results revealed that the sialylation of NLFLN(207)HSEN(211)ATAK and the fucosylated structure at all glycopeptides increased significantly in LC and HCC patients compared with those in HBV patients and healthy individuals.
24103369	0	75	from	analysis	13:20	arg1	chain					71:75	sera haptoglobin β chain	52:75	sera haptoglobin β chain in liver diseases	52:93	Quantitative analysis of site-specific N-glycans on sera haptoglobin β chain in liver diseases.
24103369	1	76	with	glycoproteins	147:159	arg1	potential					170:178	the potential	166:178	the potential of clinical application	166:202	The site-specific characterization of N-glycans in glycoproteins with the potential of clinical application is important.
24103369	5	77	theme	glycans	919:925	arg1	quantification					901:914	the relative quantification	888:914	the relative quantification of glycans present on each glycopeptide	888:954	Sera Hp β chain in healthy individuals as well as patients with hepatitis B virus (HBV), liver cirrhosis (LC) and hepatocellular carcinoma (HCC) were purified, digested and subjected to liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry, which allowed identification and structure determination of the glycopeptide, as well as the relative quantification of glycans present on each glycopeptide.
24103369	5	77	theme	glycans	919:925	arg1	identification					813:826	identification	813:826	identification	813:826	Sera Hp β chain in healthy individuals as well as patients with hepatitis B virus (HBV), liver cirrhosis (LC) and hepatocellular carcinoma (HCC) were purified, digested and subjected to liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry, which allowed identification and structure determination of the glycopeptide, as well as the relative quantification of glycans present on each glycopeptide.
24103369	5	77	theme	glycans	919:925	arg1	determination					842:854	structure determination	832:854	structure determination	832:854	Sera Hp β chain in healthy individuals as well as patients with hepatitis B virus (HBV), liver cirrhosis (LC) and hepatocellular carcinoma (HCC) were purified, digested and subjected to liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry, which allowed identification and structure determination of the glycopeptide, as well as the relative quantification of glycans present on each glycopeptide.
24103369	3	78	theme	Hp	343:344	arg1	chain					348:352	Hp β chain	343:352	Hp β chain	343:352	Hp β chain contains four potential sites of N-glycosylation.
24103369	8	79	theme	differential	1439:1450	arg1	markers					1452:1458	novel differential markers	1433:1458	novel differential markers for LC and HCC patients	1433:1482	Thus, the sialylated and fucosylated glycoforms of Hp β chain might be related to early hepatocarcinogenesis and also might be useful as novel differential markers for LC and HCC patients.
24103369	7	80	theme	various	1252:1258	arg1	diseases					1266:1273	various liver diseases	1252:1273	various liver diseases	1252:1273	A set of different N-glycan patterns of Hp β chain in various liver diseases has been determined.
24103369	4	81	theme	N-glycans	459:467	arg1	change					449:454	the potential change	435:454	the potential change of N-glycans on Hp β chain	435:481	In this study, we investigated the potential change of N-glycans on Hp β chain in a site-specific fashion.
24103369	5	82	theme	ionization-higher	732:748	arg1	spectrometry					785:796	liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry	697:796	liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry	697:796	Sera Hp β chain in healthy individuals as well as patients with hepatitis B virus (HBV), liver cirrhosis (LC) and hepatocellular carcinoma (HCC) were purified, digested and subjected to liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry, which allowed identification and structure determination of the glycopeptide, as well as the relative quantification of glycans present on each glycopeptide.
24103369	8	83	theme	novel	1433:1437	arg1	markers					1452:1458	novel differential markers	1433:1458	novel differential markers for LC and HCC patients	1433:1482	Thus, the sialylated and fucosylated glycoforms of Hp β chain might be related to early hepatocarcinogenesis and also might be useful as novel differential markers for LC and HCC patients.
24103369	7	84	theme	chain	1243:1247	arg1	patterns					1226:1233	different N-glycan patterns	1207:1233	different N-glycan patterns of Hp β chain in various liver diseases	1207:1273	A set of different N-glycan patterns of Hp β chain in various liver diseases has been determined.
24103369	6	85	gly	fucosylated	1047:1057	arg1	structure					1059:1067	the fucosylated structure	1043:1067	the fucosylated structure at all glycopeptides	1043:1088	The quantitative results revealed that the sialylation of NLFLN(207)HSEN(211)ATAK and the fucosylated structure at all glycopeptides increased significantly in LC and HCC patients compared with those in HBV patients and healthy individuals.
24103369	6	86	from	glycopeptides	1076:1088	arg1	sialylation					1000:1010	the sialylation	996:1010	the sialylation of NLFLN(207)HSEN(211)ATAK	996:1037	The quantitative results revealed that the sialylation of NLFLN(207)HSEN(211)ATAK and the fucosylated structure at all glycopeptides increased significantly in LC and HCC patients compared with those in HBV patients and healthy individuals.
24103369	6	86	from	glycopeptides	1076:1088	arg1	structure					1059:1067	the fucosylated structure	1043:1067	the fucosylated structure at all glycopeptides	1043:1088	The quantitative results revealed that the sialylation of NLFLN(207)HSEN(211)ATAK and the fucosylated structure at all glycopeptides increased significantly in LC and HCC patients compared with those in HBV patients and healthy individuals.
24103369	0	87	theme	site-specific	25:37	arg1	N-glycans					39:47	site-specific N-glycans	25:47	site-specific N-glycans	25:47	Quantitative analysis of site-specific N-glycans on sera haptoglobin β chain in liver diseases.
24103369	5	88	theme	energy	750:755	arg1	spectrometry					785:796	liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry	697:796	liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry	697:796	Sera Hp β chain in healthy individuals as well as patients with hepatitis B virus (HBV), liver cirrhosis (LC) and hepatocellular carcinoma (HCC) were purified, digested and subjected to liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry, which allowed identification and structure determination of the glycopeptide, as well as the relative quantification of glycans present on each glycopeptide.
24103369	7	89	theme	Hp	1238:1239	arg1	chain					1243:1247	Hp β chain	1238:1247	Hp β chain in various liver diseases	1238:1273	A set of different N-glycan patterns of Hp β chain in various liver diseases has been determined.
24103369	7	90	theme	patterns	1226:1233	arg1	patterns					1226:1233	different N-glycan patterns	1207:1233	different N-glycan patterns of Hp β chain in various liver diseases	1207:1273	A set of different N-glycan patterns of Hp β chain in various liver diseases has been determined.
24103369	7	90	theme	patterns	1226:1233	arg1	set					1200:1202	A set	1198:1202	A set of different N-glycan patterns of Hp β chain in various liver diseases	1198:1273	A set of different N-glycan patterns of Hp β chain in various liver diseases has been determined.
24103369	5	91	gly	glycopeptide	943:954	arg2	glycopeptide					943:954	each glycopeptide	938:954	each glycopeptide	938:954	Sera Hp β chain in healthy individuals as well as patients with hepatitis B virus (HBV), liver cirrhosis (LC) and hepatocellular carcinoma (HCC) were purified, digested and subjected to liquid chromatography-electrospray ionization-higher energy collision dissociation mass spectrometry, which allowed identification and structure determination of the glycopeptide, as well as the relative quantification of glycans present on each glycopeptide.
24103369	8	92	theme	sialylated	1306:1315	arg1	useful					1423:1428	useful	1423:1428	useful	1423:1428	Thus, the sialylated and fucosylated glycoforms of Hp β chain might be related to early hepatocarcinogenesis and also might be useful as novel differential markers for LC and HCC patients.
24103369	8	92	theme	sialylated	1306:1315	arg1	related					1367:1373	related	1367:1373	related	1367:1373	Thus, the sialylated and fucosylated glycoforms of Hp β chain might be related to early hepatocarcinogenesis and also might be useful as novel differential markers for LC and HCC patients.
24103369	8	92	theme	sialylated	1306:1315	arg1	glycoforms					1333:1342	the sialylated and fucosylated glycoforms	1302:1342	the sialylated and fucosylated glycoforms of Hp β chain	1302:1356	Thus, the sialylated and fucosylated glycoforms of Hp β chain might be related to early hepatocarcinogenesis and also might be useful as novel differential markers for LC and HCC patients.
24103369	0	93	theme	haptoglobin	57:67	arg1	chain					71:75	sera haptoglobin β chain	52:75	sera haptoglobin β chain in liver diseases	52:93	Quantitative analysis of site-specific N-glycans on sera haptoglobin β chain in liver diseases.
24103369	7	94	theme	different	1207:1215	arg1	patterns					1226:1233	different N-glycan patterns	1207:1233	different N-glycan patterns of Hp β chain in various liver diseases	1207:1273	A set of different N-glycan patterns of Hp β chain in various liver diseases has been determined.
24103369	8	95	theme	fucosylated	1321:1331	arg1	useful					1423:1428	useful	1423:1428	useful	1423:1428	Thus, the sialylated and fucosylated glycoforms of Hp β chain might be related to early hepatocarcinogenesis and also might be useful as novel differential markers for LC and HCC patients.
24103369	8	95	theme	fucosylated	1321:1331	arg1	related					1367:1373	related	1367:1373	related	1367:1373	Thus, the sialylated and fucosylated glycoforms of Hp β chain might be related to early hepatocarcinogenesis and also might be useful as novel differential markers for LC and HCC patients.
24103369	8	95	theme	fucosylated	1321:1331	arg1	glycoforms					1333:1342	the sialylated and fucosylated glycoforms	1302:1342	the sialylated and fucosylated glycoforms of Hp β chain	1302:1356	Thus, the sialylated and fucosylated glycoforms of Hp β chain might be related to early hepatocarcinogenesis and also might be useful as novel differential markers for LC and HCC patients.
24103369	6	96	theme	fucosylated	1047:1057	arg1	structure					1059:1067	the fucosylated structure	1043:1067	the fucosylated structure at all glycopeptides	1043:1088	The quantitative results revealed that the sialylation of NLFLN(207)HSEN(211)ATAK and the fucosylated structure at all glycopeptides increased significantly in LC and HCC patients compared with those in HBV patients and healthy individuals.
24103369	6	97	theme	HSEN	1025:1028	arg1	ATAK					1034:1037	NLFLN(207)HSEN(211)ATAK	1015:1037	NLFLN(207)HSEN(211)ATAK	1015:1037	The quantitative results revealed that the sialylation of NLFLN(207)HSEN(211)ATAK and the fucosylated structure at all glycopeptides increased significantly in LC and HCC patients compared with those in HBV patients and healthy individuals.
24103369	8	98	theme	β	1350:1350	arg1	chain					1352:1356	Hp β chain	1347:1356	Hp β chain	1347:1356	Thus, the sialylated and fucosylated glycoforms of Hp β chain might be related to early hepatocarcinogenesis and also might be useful as novel differential markers for LC and HCC patients.
24103369	8	99	gly	glycoforms	1333:1342	arg1	chain					1352:1356	Hp β chain	1347:1356	Hp β chain	1347:1356	Thus, the sialylated and fucosylated glycoforms of Hp β chain might be related to early hepatocarcinogenesis and also might be useful as novel differential markers for LC and HCC patients.
17222411	0	0	theme	factor	96:101	arg1	structure					53:61	glycan structure	46:61	Functional glycosylation of human podoplanin: glycan structure of platelet aggregation-inducing factor.	0:102	Functional glycosylation of human podoplanin: glycan structure of platelet aggregation-inducing factor.
17222411	0	1	theme	aggregation-inducing	75:94	arg1	factor					96:101	platelet aggregation-inducing factor	66:101	platelet aggregation-inducing factor	66:101	Functional glycosylation of human podoplanin: glycan structure of platelet aggregation-inducing factor.
17222411	4	2	theme	disialyl-corel	598:611	arg1	structure					678:686	the disialyl-corel (NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr) structure	594:686	the disialyl-corel (NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr) structure	594:686	Analyses of glycopeptides produced by Edman degradation and mass spectrometry revealed that the disialyl-corel (NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr) structure was primarily attached to a glycosylation site at residue Thr52.
17222411	4	2	theme	disialyl-corel	598:611	arg1	l-O-Thr					669:675	NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr	614:675	NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr	614:675	Analyses of glycopeptides produced by Edman degradation and mass spectrometry revealed that the disialyl-corel (NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr) structure was primarily attached to a glycosylation site at residue Thr52.
17222411	3	3	theme	lectin	483:488	arg1	microarray					490:499	lectin microarray	483:499	lectin microarray	483:499	Endogenous or recombinant human podoplanin were purified, and total glycosylation profiles were surveyed by lectin microarray.
17222411	4	4	theme	alpha2-3Gal	620:630	arg1	structure					678:686	the disialyl-corel (NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr) structure	594:686	the disialyl-corel (NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr) structure	594:686	Analyses of glycopeptides produced by Edman degradation and mass spectrometry revealed that the disialyl-corel (NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr) structure was primarily attached to a glycosylation site at residue Thr52.
17222411	4	4	theme	alpha2-3Gal	620:630	arg1	l-O-Thr					669:675	NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr	614:675	NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr	614:675	Analyses of glycopeptides produced by Edman degradation and mass spectrometry revealed that the disialyl-corel (NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr) structure was primarily attached to a glycosylation site at residue Thr52.
17222411	4	5	theme	NeuAc	614:618	arg1	structure					678:686	the disialyl-corel (NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr) structure	594:686	the disialyl-corel (NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr) structure	594:686	Analyses of glycopeptides produced by Edman degradation and mass spectrometry revealed that the disialyl-corel (NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr) structure was primarily attached to a glycosylation site at residue Thr52.
17222411	4	5	theme	NeuAc	614:618	arg1	l-O-Thr					669:675	NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr	614:675	NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr	614:675	Analyses of glycopeptides produced by Edman degradation and mass spectrometry revealed that the disialyl-corel (NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr) structure was primarily attached to a glycosylation site at residue Thr52.
17222411	5	6	theme	Sialic	753:758	arg1	podoplanin					775:784	Sialic acid-deficient podoplanin	753:784	Sialic acid-deficient podoplanin	753:784	Sialic acid-deficient podoplanin recovered its activity after additional sialylation.
17222411	4	7	attach	attached	702:709	arg1	site					730:733	a glycosylation site	714:733	a glycosylation site at residue Thr52	714:750	Analyses of glycopeptides produced by Edman degradation and mass spectrometry revealed that the disialyl-corel (NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr) structure was primarily attached to a glycosylation site at residue Thr52.
17222411	4	7	attach	attached	702:709	arg2	structure					678:686	the disialyl-corel (NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr) structure	594:686	the disialyl-corel (NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr) structure	594:686	Analyses of glycopeptides produced by Edman degradation and mass spectrometry revealed that the disialyl-corel (NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr) structure was primarily attached to a glycosylation site at residue Thr52.
17222411	4	7	attach	attached	702:709	arg2	l-O-Thr					669:675	NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr	614:675	NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr	614:675	Analyses of glycopeptides produced by Edman degradation and mass spectrometry revealed that the disialyl-corel (NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr) structure was primarily attached to a glycosylation site at residue Thr52.
17222411	4	8	theme	alpha2-6	647:654	arg1	structure					678:686	the disialyl-corel (NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr) structure	594:686	the disialyl-corel (NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr) structure	594:686	Analyses of glycopeptides produced by Edman degradation and mass spectrometry revealed that the disialyl-corel (NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr) structure was primarily attached to a glycosylation site at residue Thr52.
17222411	4	8	theme	alpha2-6	647:654	arg1	l-O-Thr					669:675	NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr	614:675	NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr	614:675	Analyses of glycopeptides produced by Edman degradation and mass spectrometry revealed that the disialyl-corel (NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr) structure was primarily attached to a glycosylation site at residue Thr52.
17222411	4	9	gly	glycopeptides	514:526	arg2	glycopeptides					514:526	glycopeptides	514:526	glycopeptides produced by Edman degradation and mass spectrometry	514:578	Analyses of glycopeptides produced by Edman degradation and mass spectrometry revealed that the disialyl-corel (NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr) structure was primarily attached to a glycosylation site at residue Thr52.
17222411	1	10	theme	key	171:173	arg1	role					175:178	a key role	169:178	a key role	169:178	Podoplanin (Aggrus) is a mucin-type sialoglycoprotein that plays a key role in tumor cell-induced platelet aggregation.
17222411	5	11	theme	acid-deficient	760:773	arg1	podoplanin					775:784	Sialic acid-deficient podoplanin	753:784	Sialic acid-deficient podoplanin	753:784	Sialic acid-deficient podoplanin recovered its activity after additional sialylation.
17222411	6	12	theme	platelet	933:940	arg1	aggregation					942:952	podoplanin-induced platelet aggregation	914:952	podoplanin-induced platelet aggregation	914:952	These results indicated that the sialylated Corel at Thr52 is critical for podoplanin-induced platelet aggregation.
17222411	3	13	theme	recombinant	389:399	arg1	podoplanin					407:416	Endogenous or recombinant human podoplanin	375:416	podoplanin	407:416	Endogenous or recombinant human podoplanin were purified, and total glycosylation profiles were surveyed by lectin microarray.
17222411	3	14	theme	glycosylation	443:455	arg1	profiles					457:464	total glycosylation profiles	437:464	total glycosylation profiles	437:464	Endogenous or recombinant human podoplanin were purified, and total glycosylation profiles were surveyed by lectin microarray.
17222411	6	15	theme	podoplanin-induced	914:931	arg1	aggregation					942:952	podoplanin-induced platelet aggregation	914:952	podoplanin-induced platelet aggregation	914:952	These results indicated that the sialylated Corel at Thr52 is critical for podoplanin-induced platelet aggregation.
17222411	6	16	gly	sialylated	872:881	arg1	critical					901:908	critical	901:908	critical	901:908	These results indicated that the sialylated Corel at Thr52 is critical for podoplanin-induced platelet aggregation.
17222411	6	16	gly	sialylated	872:881	arg1	Thr52					892:896	the sialylated Corel at Thr52	868:896	the sialylated Corel at Thr52	868:896	These results indicated that the sialylated Corel at Thr52 is critical for podoplanin-induced platelet aggregation.
17222411	0	17	theme	Functional	0:9	arg1	glycosylation					11:23	Functional glycosylation	0:23	Functional glycosylation of human podoplanin: glycan structure of platelet aggregation-inducing factor.	0:102	Functional glycosylation of human podoplanin: glycan structure of platelet aggregation-inducing factor.
17222411	2	18	theme	PLAG	312:315	arg1	podoplanin					333:342	human podoplanin	327:342	human podoplanin	327:342	Podoplanin possesses a platelet aggregation-stimulating (PLAG) domain, and Thr52 in the PLAG domain of human podoplanin is important for its activity.
17222411	2	18	theme	PLAG	312:315	arg1	domain					317:322	the PLAG domain	308:322	the PLAG domain of human podoplanin	308:342	Podoplanin possesses a platelet aggregation-stimulating (PLAG) domain, and Thr52 in the PLAG domain of human podoplanin is important for its activity.
17222411	0	19	theme	human	28:32	arg1	podoplanin					34:43	human podoplanin	28:43	human podoplanin	28:43	Functional glycosylation of human podoplanin: glycan structure of platelet aggregation-inducing factor.
17222411	4	20	gly	glycosylation	716:728	arg2	residue					738:744	residue Thr52	738:750	residue Thr52	738:750	Analyses of glycopeptides produced by Edman degradation and mass spectrometry revealed that the disialyl-corel (NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr) structure was primarily attached to a glycosylation site at residue Thr52.
17222411	4	20	gly	glycosylation	716:728	arg2	site					730:733	a glycosylation site	714:733	a glycosylation site at residue Thr52	714:750	Analyses of glycopeptides produced by Edman degradation and mass spectrometry revealed that the disialyl-corel (NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr) structure was primarily attached to a glycosylation site at residue Thr52.
17222411	1	21	theme	cell-induced	189:200	arg1	aggregation					211:221	tumor cell-induced platelet aggregation	183:221	tumor cell-induced platelet aggregation	183:221	Podoplanin (Aggrus) is a mucin-type sialoglycoprotein that plays a key role in tumor cell-induced platelet aggregation.
17222411	3	22	theme	Endogenous	375:384	arg1	podoplanin					407:416	Endogenous or recombinant human podoplanin	375:416	podoplanin	407:416	Endogenous or recombinant human podoplanin were purified, and total glycosylation profiles were surveyed by lectin microarray.
17222411	1	23	theme	platelet	202:209	arg1	aggregation					211:221	tumor cell-induced platelet aggregation	183:221	tumor cell-induced platelet aggregation	183:221	Podoplanin (Aggrus) is a mucin-type sialoglycoprotein that plays a key role in tumor cell-induced platelet aggregation.
17222411	4	24	theme	glycosylation	716:728	arg1	site					730:733	a glycosylation site	714:733	a glycosylation site at residue Thr52	714:750	Analyses of glycopeptides produced by Edman degradation and mass spectrometry revealed that the disialyl-corel (NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr) structure was primarily attached to a glycosylation site at residue Thr52.
17222411	2	25	theme	platelet	247:254	arg1	domain					287:292	a platelet aggregation-stimulating (PLAG) domain	245:292	a platelet aggregation-stimulating (PLAG) domain	245:292	Podoplanin possesses a platelet aggregation-stimulating (PLAG) domain, and Thr52 in the PLAG domain of human podoplanin is important for its activity.
17222411	4	26	theme	alpha	663:667	arg1	structure					678:686	the disialyl-corel (NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr) structure	594:686	the disialyl-corel (NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr) structure	594:686	Analyses of glycopeptides produced by Edman degradation and mass spectrometry revealed that the disialyl-corel (NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr) structure was primarily attached to a glycosylation site at residue Thr52.
17222411	4	26	theme	alpha	663:667	arg1	l-O-Thr					669:675	NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr	614:675	NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr	614:675	Analyses of glycopeptides produced by Edman degradation and mass spectrometry revealed that the disialyl-corel (NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr) structure was primarily attached to a glycosylation site at residue Thr52.
17222411	0	27	theme	podoplanin	34:43	arg1	glycosylation					11:23	Functional glycosylation	0:23	Functional glycosylation of human podoplanin: glycan structure of platelet aggregation-inducing factor.	0:102	Functional glycosylation of human podoplanin: glycan structure of platelet aggregation-inducing factor.
17222411	5	28	theme	additional	815:824	arg1	sialylation					826:836	additional sialylation	815:836	additional sialylation	815:836	Sialic acid-deficient podoplanin recovered its activity after additional sialylation.
17222411	0	29	gly	glycosylation	11:23	arg1	podoplanin					34:43	human podoplanin	28:43	human podoplanin	28:43	Functional glycosylation of human podoplanin: glycan structure of platelet aggregation-inducing factor.
17222411	4	30	theme	GalNAc	656:661	arg1	structure					678:686	the disialyl-corel (NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr) structure	594:686	the disialyl-corel (NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr) structure	594:686	Analyses of glycopeptides produced by Edman degradation and mass spectrometry revealed that the disialyl-corel (NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr) structure was primarily attached to a glycosylation site at residue Thr52.
17222411	4	30	theme	GalNAc	656:661	arg1	l-O-Thr					669:675	NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr	614:675	NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr	614:675	Analyses of glycopeptides produced by Edman degradation and mass spectrometry revealed that the disialyl-corel (NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr) structure was primarily attached to a glycosylation site at residue Thr52.
17222411	3	31	theme	human	401:405	arg1	podoplanin					407:416	Endogenous or recombinant human podoplanin	375:416	podoplanin	407:416	Endogenous or recombinant human podoplanin were purified, and total glycosylation profiles were surveyed by lectin microarray.
17222411	4	32	theme	Edman	540:544	arg1	degradation					546:556	Edman degradation	540:556	Edman degradation	540:556	Analyses of glycopeptides produced by Edman degradation and mass spectrometry revealed that the disialyl-corel (NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr) structure was primarily attached to a glycosylation site at residue Thr52.
17222411	3	33	theme	total	437:441	arg1	profiles					457:464	total glycosylation profiles	437:464	total glycosylation profiles	437:464	Endogenous or recombinant human podoplanin were purified, and total glycosylation profiles were surveyed by lectin microarray.
17222411	0	34	theme	glycan	46:51	arg1	structure					53:61	glycan structure	46:61	Functional glycosylation of human podoplanin: glycan structure of platelet aggregation-inducing factor.	0:102	Functional glycosylation of human podoplanin: glycan structure of platelet aggregation-inducing factor.
17222411	4	35	theme	mass	562:565	arg1	spectrometry					567:578	mass spectrometry	562:578	mass spectrometry	562:578	Analyses of glycopeptides produced by Edman degradation and mass spectrometry revealed that the disialyl-corel (NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr) structure was primarily attached to a glycosylation site at residue Thr52.
17222411	1	36	gly	sialoglycoprotein	140:156	arg1	Podoplanin					104:113	Podoplanin	104:113	Podoplanin (Aggrus)	104:122	Podoplanin (Aggrus) is a mucin-type sialoglycoprotein that plays a key role in tumor cell-induced platelet aggregation.
17222411	1	36	gly	sialoglycoprotein	140:156	arg1	sialoglycoprotein					140:156	a mucin-type sialoglycoprotein	127:156	a mucin-type sialoglycoprotein that plays a key role in tumor cell-induced platelet aggregation	127:221	Podoplanin (Aggrus) is a mucin-type sialoglycoprotein that plays a key role in tumor cell-induced platelet aggregation.
17222411	6	37	theme	at	889:890	arg1	critical					901:908	critical	901:908	critical	901:908	These results indicated that the sialylated Corel at Thr52 is critical for podoplanin-induced platelet aggregation.
17222411	6	37	theme	at	889:890	arg1	Thr52					892:896	the sialylated Corel at Thr52	868:896	the sialylated Corel at Thr52	868:896	These results indicated that the sialylated Corel at Thr52 is critical for podoplanin-induced platelet aggregation.
17222411	2	38	theme	podoplanin	333:342	arg1	podoplanin					333:342	human podoplanin	327:342	human podoplanin	327:342	Podoplanin possesses a platelet aggregation-stimulating (PLAG) domain, and Thr52 in the PLAG domain of human podoplanin is important for its activity.
17222411	2	38	theme	podoplanin	333:342	arg1	domain					317:322	the PLAG domain	308:322	the PLAG domain of human podoplanin	308:342	Podoplanin possesses a platelet aggregation-stimulating (PLAG) domain, and Thr52 in the PLAG domain of human podoplanin is important for its activity.
17222411	4	39	from	residue	738:744	arg1	site					730:733	a glycosylation site	714:733	a glycosylation site at residue Thr52	714:750	Analyses of glycopeptides produced by Edman degradation and mass spectrometry revealed that the disialyl-corel (NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr) structure was primarily attached to a glycosylation site at residue Thr52.
17222411	6	40	theme	Corel	883:887	arg1	critical					901:908	critical	901:908	critical	901:908	These results indicated that the sialylated Corel at Thr52 is critical for podoplanin-induced platelet aggregation.
17222411	6	40	theme	Corel	883:887	arg1	Thr52					892:896	the sialylated Corel at Thr52	868:896	the sialylated Corel at Thr52	868:896	These results indicated that the sialylated Corel at Thr52 is critical for podoplanin-induced platelet aggregation.
17222411	6	41	from	Thr52	892:896	arg1	Corel					883:887	the sialylated Corel at Thr52	868:896	the sialylated Corel at Thr52	868:896	These results indicated that the sialylated Corel at Thr52 is critical for podoplanin-induced platelet aggregation.
17222411	6	41	from	Thr52	892:896	arg1	at					889:890	the sialylated Corel at Thr52	868:896	the sialylated Corel at Thr52	868:896	These results indicated that the sialylated Corel at Thr52 is critical for podoplanin-induced platelet aggregation.
17222411	2	42	theme	human	327:331	arg1	podoplanin					333:342	human podoplanin	327:342	human podoplanin	327:342	Podoplanin possesses a platelet aggregation-stimulating (PLAG) domain, and Thr52 in the PLAG domain of human podoplanin is important for its activity.
17222411	4	43	theme	l-3	637:639	arg1	structure					678:686	the disialyl-corel (NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr) structure	594:686	the disialyl-corel (NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr) structure	594:686	Analyses of glycopeptides produced by Edman degradation and mass spectrometry revealed that the disialyl-corel (NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr) structure was primarily attached to a glycosylation site at residue Thr52.
17222411	4	43	theme	l-3	637:639	arg1	l-O-Thr					669:675	NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr	614:675	NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr	614:675	Analyses of glycopeptides produced by Edman degradation and mass spectrometry revealed that the disialyl-corel (NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr) structure was primarily attached to a glycosylation site at residue Thr52.
17222411	6	44	theme	sialylated	872:881	arg1	critical					901:908	critical	901:908	critical	901:908	These results indicated that the sialylated Corel at Thr52 is critical for podoplanin-induced platelet aggregation.
17222411	6	44	theme	sialylated	872:881	arg1	Thr52					892:896	the sialylated Corel at Thr52	868:896	the sialylated Corel at Thr52	868:896	These results indicated that the sialylated Corel at Thr52 is critical for podoplanin-induced platelet aggregation.
17222411	2	45	theme	PLAG	281:284	arg1	domain					287:292	a platelet aggregation-stimulating (PLAG) domain	245:292	a platelet aggregation-stimulating (PLAG) domain	245:292	Podoplanin possesses a platelet aggregation-stimulating (PLAG) domain, and Thr52 in the PLAG domain of human podoplanin is important for its activity.
17222411	1	46	theme	mucin-type	129:138	arg1	Podoplanin					104:113	Podoplanin	104:113	Podoplanin (Aggrus)	104:122	Podoplanin (Aggrus) is a mucin-type sialoglycoprotein that plays a key role in tumor cell-induced platelet aggregation.
17222411	1	46	theme	mucin-type	129:138	arg1	sialoglycoprotein					140:156	a mucin-type sialoglycoprotein	127:156	a mucin-type sialoglycoprotein that plays a key role in tumor cell-induced platelet aggregation	127:221	Podoplanin (Aggrus) is a mucin-type sialoglycoprotein that plays a key role in tumor cell-induced platelet aggregation.
17222411	2	47	from	Thr52	299:303	arg1	podoplanin					333:342	human podoplanin	327:342	human podoplanin	327:342	Podoplanin possesses a platelet aggregation-stimulating (PLAG) domain, and Thr52 in the PLAG domain of human podoplanin is important for its activity.
17222411	2	47	from	Thr52	299:303	arg1	domain					317:322	the PLAG domain	308:322	the PLAG domain of human podoplanin	308:342	Podoplanin possesses a platelet aggregation-stimulating (PLAG) domain, and Thr52 in the PLAG domain of human podoplanin is important for its activity.
17222411	2	48	contain	possesses	235:243	arg2	domain					287:292	a platelet aggregation-stimulating (PLAG) domain	245:292	a platelet aggregation-stimulating (PLAG) domain	245:292	Podoplanin possesses a platelet aggregation-stimulating (PLAG) domain, and Thr52 in the PLAG domain of human podoplanin is important for its activity.
17222411	2	48	contain	possesses	235:243	arg1	Podoplanin					224:233	Podoplanin	224:233	Podoplanin	224:233	Podoplanin possesses a platelet aggregation-stimulating (PLAG) domain, and Thr52 in the PLAG domain of human podoplanin is important for its activity.
17222411	0	49	theme	platelet	66:73	arg1	factor					96:101	platelet aggregation-inducing factor	66:101	platelet aggregation-inducing factor	66:101	Functional glycosylation of human podoplanin: glycan structure of platelet aggregation-inducing factor.
17222411	0	50	dep	glycosylation	11:23	arg1	structure					53:61	glycan structure	46:61	Functional glycosylation of human podoplanin: glycan structure of platelet aggregation-inducing factor.	0:102	Functional glycosylation of human podoplanin: glycan structure of platelet aggregation-inducing factor.
17222411	4	51	theme	NeuAc	641:645	arg1	structure					678:686	the disialyl-corel (NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr) structure	594:686	the disialyl-corel (NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr) structure	594:686	Analyses of glycopeptides produced by Edman degradation and mass spectrometry revealed that the disialyl-corel (NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr) structure was primarily attached to a glycosylation site at residue Thr52.
17222411	4	51	theme	NeuAc	641:645	arg1	l-O-Thr					669:675	NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr	614:675	NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr	614:675	Analyses of glycopeptides produced by Edman degradation and mass spectrometry revealed that the disialyl-corel (NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr) structure was primarily attached to a glycosylation site at residue Thr52.
17222411	4	52	theme	glycopeptides	514:526	arg1	Analyses					502:509	Analyses	502:509	Analyses of glycopeptides produced by Edman degradation and mass spectrometry	502:578	Analyses of glycopeptides produced by Edman degradation and mass spectrometry revealed that the disialyl-corel (NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr) structure was primarily attached to a glycosylation site at residue Thr52.
17222411	2	53	theme	aggregation-stimulating	256:278	arg1	domain					287:292	a platelet aggregation-stimulating (PLAG) domain	245:292	a platelet aggregation-stimulating (PLAG) domain	245:292	Podoplanin possesses a platelet aggregation-stimulating (PLAG) domain, and Thr52 in the PLAG domain of human podoplanin is important for its activity.
17222411	4	54	theme	beta	632:635	arg1	structure					678:686	the disialyl-corel (NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr) structure	594:686	the disialyl-corel (NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr) structure	594:686	Analyses of glycopeptides produced by Edman degradation and mass spectrometry revealed that the disialyl-corel (NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr) structure was primarily attached to a glycosylation site at residue Thr52.
17222411	4	54	theme	beta	632:635	arg1	l-O-Thr					669:675	NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr	614:675	NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr	614:675	Analyses of glycopeptides produced by Edman degradation and mass spectrometry revealed that the disialyl-corel (NeuAc alpha2-3Gal beta l-3(NeuAc alpha2-6)GalNAc alpha l-O-Thr) structure was primarily attached to a glycosylation site at residue Thr52.
11415438	9	0	theme	total	1423:1427	arg1	expression					1438:1447	total receptor expression	1423:1447	total receptor expression	1423:1447	The glycosylation status of the V(1a)R did, however, regulate the level of total receptor expression and also the abundance of receptor at the cell surface.
11415438	6	1	theme	1a	1031:1032	arg1	R					1034:1034	The V(1a)R	1025:1034	The V(1a)R	1025:1034	The V(1a)R is not O-glycosylated.
11415438	6	1	theme	1a	1031:1032	arg1	O-glycosylated					1043:1056	O-glycosylated	1043:1056	O-glycosylated	1043:1056	The V(1a)R is not O-glycosylated.
11415438	4	2	theme	putative	770:777	arg1	sites					795:799	the four putative N-glycosylation sites	761:799	the four putative N-glycosylation sites at Asn(14), Asn(27), Asn(198) and Asn(333)	761:842	Using a combination of translation systems that are either glycosylation-competent or do not support glycosylation, we established that of the four putative N-glycosylation sites at Asn(14), Asn(27), Asn(198) and Asn(333) only the first three sites are actually modified by carbohydrate.
11415438	6	3	theme	V	1029:1029	arg1	R					1034:1034	The V(1a)R	1025:1034	The V(1a)R	1025:1034	The V(1a)R is not O-glycosylated.
11415438	6	3	theme	V	1029:1029	arg1	O-glycosylated					1043:1056	O-glycosylated	1043:1056	O-glycosylated	1043:1056	The V(1a)R is not O-glycosylated.
11415438	1	4	theme	large	163:167	arg1	family					169:174	the large family	159:174	the large family of G-protein-coupled receptors (GPCRs)	159:213	Most of the large family of G-protein-coupled receptors (GPCRs) possess putative N-glycosylation sites within their N-termini.
11415438	10	5	theme	regulation	1537:1546	arg1	nature					1522:1527	the nature	1518:1527	the nature of this regulation (increased or decreased expression)	1518:1582	Furthermore, the nature of this regulation (increased or decreased expression) was dictated by the locus of the oligosaccharide modification.
11415438	4	6	from	Asn	822:824	arg1	sites					795:799	the four putative N-glycosylation sites	761:799	the four putative N-glycosylation sites at Asn(14), Asn(27), Asn(198) and Asn(333)	761:842	Using a combination of translation systems that are either glycosylation-competent or do not support glycosylation, we established that of the four putative N-glycosylation sites at Asn(14), Asn(27), Asn(198) and Asn(333) only the first three sites are actually modified by carbohydrate.
11415438	1	7	theme	receptors	197:205	arg1	family					169:174	the large family	159:174	the large family of G-protein-coupled receptors (GPCRs)	159:213	Most of the large family of G-protein-coupled receptors (GPCRs) possess putative N-glycosylation sites within their N-termini.
11415438	9	8	theme	receptor	1475:1482	arg1	abundance					1462:1470	the abundance	1458:1470	the abundance of receptor at the cell surface	1458:1502	The glycosylation status of the V(1a)R did, however, regulate the level of total receptor expression and also the abundance of receptor at the cell surface.
11415438	0	9	from	receptor	74:81	arg1	signalling					124:133	receptor signalling	115:133	receptor signalling	115:133	Identification of the glycosylation sites utilized on the V1a vasopressin receptor and assessment of their role in receptor signalling and expression.
11415438	0	9	from	receptor	74:81	arg1	expression					139:148	expression	139:148	expression	139:148	Identification of the glycosylation sites utilized on the V1a vasopressin receptor and assessment of their role in receptor signalling and expression.
11415438	3	10	theme	vasopressin	555:565	arg1	R					582:582	V(1a)R	577:582	V(1a)R	577:582	The occurrence and function of glycosylation of the V(1a) vasopressin receptor (V(1a)R) has been investigated in this study.
11415438	3	10	theme	vasopressin	555:565	arg1	receptor					567:574	the V(1a) vasopressin receptor	545:574	the V(1a) vasopressin receptor (V(1a)R)	545:583	The occurrence and function of glycosylation of the V(1a) vasopressin receptor (V(1a)R) has been investigated in this study.
11415438	3	11	theme	1a	551:552	arg1	R					582:582	V(1a)R	577:582	V(1a)R	577:582	The occurrence and function of glycosylation of the V(1a) vasopressin receptor (V(1a)R) has been investigated in this study.
11415438	3	11	theme	1a	551:552	arg1	receptor					567:574	the V(1a) vasopressin receptor	545:574	the V(1a) vasopressin receptor (V(1a)R)	545:583	The occurrence and function of glycosylation of the V(1a) vasopressin receptor (V(1a)R) has been investigated in this study.
11415438	13	12	theme	cell	1992:1995	arg1	surface					1997:2003	the cell surface	1988:2003	the cell surface	1988:2003	Glycosylation is not required, however, for efficient trafficking of the receptor to the cell surface.
11415438	11	13	theme	wild-type	1729:1737	arg1	expression					1739:1748	wild-type expression	1729:1748	wild-type expression	1729:1748	Modification of any one of the consensus sites alone, however, was sufficient for wild-type expression, indicating a redundancy within the glycosylation sites.
11415438	4	14	theme	translation	645:655	arg1	systems					657:663	translation systems	645:663	translation systems that are either glycosylation-competent or do not support glycosylation	645:735	Using a combination of translation systems that are either glycosylation-competent or do not support glycosylation, we established that of the four putative N-glycosylation sites at Asn(14), Asn(27), Asn(198) and Asn(333) only the first three sites are actually modified by carbohydrate.
11415438	0	15	from	assessment	87:96	arg1	signalling					124:133	receptor signalling	115:133	receptor signalling	115:133	Identification of the glycosylation sites utilized on the V1a vasopressin receptor and assessment of their role in receptor signalling and expression.
11415438	0	15	from	assessment	87:96	arg1	expression					139:148	expression	139:148	expression	139:148	Identification of the glycosylation sites utilized on the V1a vasopressin receptor and assessment of their role in receptor signalling and expression.
11415438	7	16	theme	HEK	1172:1174	arg1	cells					1181:1185	HEK 293T cells	1172:1185	HEK 293T cells	1172:1185	The functionality of a series of glycosylation-defective V(1a)R constructs was characterized after expression in HEK 293T cells.
11415438	11	17	theme	sites	1688:1692	arg1	one					1667:1669	one	1667:1669	one	1667:1669	Modification of any one of the consensus sites alone, however, was sufficient for wild-type expression, indicating a redundancy within the glycosylation sites.
11415438	11	17	theme	sites	1688:1692	arg1	sites					1688:1692	the consensus sites	1674:1692	the consensus sites alone	1674:1698	Modification of any one of the consensus sites alone, however, was sufficient for wild-type expression, indicating a redundancy within the glycosylation sites.
11415438	14	18	theme	functional	2033:2042	arg1	importance					2044:2053	the functional importance	2029:2053	the functional importance of N-glycosylation of the V(1a)R	2029:2086	This study establishes the functional importance of N-glycosylation of the V(1a)R.
11415438	0	19	theme	V1a	58:60	arg1	receptor					74:81	the V1a vasopressin receptor	54:81	the V1a vasopressin receptor	54:81	Identification of the glycosylation sites utilized on the V1a vasopressin receptor and assessment of their role in receptor signalling and expression.
11415438	5	20	theme	site-directed	965:977	arg1	mutagenesis					979:989	site-directed mutagenesis	965:989	site-directed mutagenesis	965:989	This was confirmed by disruption of consensus sites by site-directed mutagenesis, individually and in combination.
11415438	8	21	theme	ligand	1297:1302	arg1	classes					1286:1292	the four classes	1277:1292	the four classes of ligand available	1277:1312	It was found that carbohydrate moieties are not required for the receptor to bind any of the four classes of ligand available, or for intracellular signalling.
11415438	4	22	from	Asn	804:806	arg1	sites					795:799	the four putative N-glycosylation sites	761:799	the four putative N-glycosylation sites at Asn(14), Asn(27), Asn(198) and Asn(333)	761:842	Using a combination of translation systems that are either glycosylation-competent or do not support glycosylation, we established that of the four putative N-glycosylation sites at Asn(14), Asn(27), Asn(198) and Asn(333) only the first three sites are actually modified by carbohydrate.
11415438	14	23	gly	N-glycosylation	2058:2072	arg1	R					2086:2086	the V(1a)R	2077:2086	the V(1a)R	2077:2086	This study establishes the functional importance of N-glycosylation of the V(1a)R.
11415438	1	24	gly	N-glycosylation	232:246	arg2	sites					248:252	putative N-glycosylation sites	223:252	putative N-glycosylation sites within their N-termini	223:275	Most of the large family of G-protein-coupled receptors (GPCRs) possess putative N-glycosylation sites within their N-termini.
11415438	9	25	theme	glycosylation	1352:1364	arg1	status					1366:1371	The glycosylation status	1348:1371	The glycosylation status of the V(1a)R	1348:1385	The glycosylation status of the V(1a)R did, however, regulate the level of total receptor expression and also the abundance of receptor at the cell surface.
11415438	3	26	gly	glycosylation	528:540	arg1	R					582:582	V(1a)R	577:582	V(1a)R	577:582	The occurrence and function of glycosylation of the V(1a) vasopressin receptor (V(1a)R) has been investigated in this study.
11415438	3	26	gly	glycosylation	528:540	arg1	receptor					567:574	the V(1a) vasopressin receptor	545:574	the V(1a) vasopressin receptor (V(1a)R)	545:583	The occurrence and function of glycosylation of the V(1a) vasopressin receptor (V(1a)R) has been investigated in this study.
11415438	11	27	theme	one	1667:1669	arg1	Modification					1647:1658	Modification	1647:1658	Modification of any one of the consensus sites alone	1647:1698	Modification of any one of the consensus sites alone, however, was sufficient for wild-type expression, indicating a redundancy within the glycosylation sites.
11415438	5	28	theme	sites	956:960	arg1	disruption					932:941	disruption	932:941	disruption of consensus sites by site-directed mutagenesis	932:989	This was confirmed by disruption of consensus sites by site-directed mutagenesis, individually and in combination.
11415438	9	29	theme	V	1380:1380	arg1	R					1385:1385	the V(1a)R	1376:1385	the V(1a)R	1376:1385	The glycosylation status of the V(1a)R did, however, regulate the level of total receptor expression and also the abundance of receptor at the cell surface.
11415438	2	30	theme	glycosylation	378:390	arg1	sites					392:396	the consensus glycosylation sites	364:396	the consensus glycosylation sites	364:396	However, for the vast majority of GPCRs, it has not been determined which, if any, of the consensus glycosylation sites are actually utilized or what the functional ramifications are of modification by oligosaccharide.
11415438	13	31	theme	efficient	1947:1955	arg1	trafficking					1957:1967	efficient trafficking	1947:1967	efficient trafficking of the receptor to the cell surface	1947:2003	Glycosylation is not required, however, for efficient trafficking of the receptor to the cell surface.
11415438	9	32	theme	1a	1382:1383	arg1	R					1385:1385	the V(1a)R	1376:1385	the V(1a)R	1376:1385	The glycosylation status of the V(1a)R did, however, regulate the level of total receptor expression and also the abundance of receptor at the cell surface.
11415438	2	33	theme	functional	432:441	arg1	ramifications					443:455	the functional ramifications	428:455	the functional ramifications	428:455	However, for the vast majority of GPCRs, it has not been determined which, if any, of the consensus glycosylation sites are actually utilized or what the functional ramifications are of modification by oligosaccharide.
11415438	0	34	theme	sites	36:40	arg1	Identification					0:13	Identification	0:13	Identification of the glycosylation sites	0:40	Identification of the glycosylation sites utilized on the V1a vasopressin receptor and assessment of their role in receptor signalling and expression.
11415438	9	35	theme	R	1385:1385	arg1	status					1366:1371	The glycosylation status	1348:1371	The glycosylation status of the V(1a)R	1348:1385	The glycosylation status of the V(1a)R did, however, regulate the level of total receptor expression and also the abundance of receptor at the cell surface.
11415438	7	36	theme	R	1121:1121	arg1	constructs					1123:1132	glycosylation-defective V(1a)R constructs	1092:1132	glycosylation-defective V(1a)R constructs	1092:1132	The functionality of a series of glycosylation-defective V(1a)R constructs was characterized after expression in HEK 293T cells.
11415438	0	37	gly	glycosylation	22:34	arg2	sites					36:40	the glycosylation sites	18:40	the glycosylation sites	18:40	Identification of the glycosylation sites utilized on the V1a vasopressin receptor and assessment of their role in receptor signalling and expression.
11415438	7	38	theme	1a	1118:1119	arg1	constructs					1123:1132	glycosylation-defective V(1a)R constructs	1092:1132	glycosylation-defective V(1a)R constructs	1092:1132	The functionality of a series of glycosylation-defective V(1a)R constructs was characterized after expression in HEK 293T cells.
11415438	7	39	theme	V	1116:1116	arg1	constructs					1123:1132	glycosylation-defective V(1a)R constructs	1092:1132	glycosylation-defective V(1a)R constructs	1092:1132	The functionality of a series of glycosylation-defective V(1a)R constructs was characterized after expression in HEK 293T cells.
11415438	11	40	gly	glycosylation	1786:1798	arg2	sites					1800:1804	the glycosylation sites	1782:1804	the glycosylation sites	1782:1804	Modification of any one of the consensus sites alone, however, was sufficient for wild-type expression, indicating a redundancy within the glycosylation sites.
11415438	10	41	theme	oligosaccharide	1617:1631	arg1	modification					1633:1644	the oligosaccharide modification	1613:1644	the oligosaccharide modification	1613:1644	Furthermore, the nature of this regulation (increased or decreased expression) was dictated by the locus of the oligosaccharide modification.
11415438	1	42	theme	putative	223:230	arg1	sites					248:252	putative N-glycosylation sites	223:252	putative N-glycosylation sites within their N-termini	223:275	Most of the large family of G-protein-coupled receptors (GPCRs) possess putative N-glycosylation sites within their N-termini.
11415438	7	43	from	expression	1158:1167	arg1	cells					1181:1185	HEK 293T cells	1172:1185	HEK 293T cells	1172:1185	The functionality of a series of glycosylation-defective V(1a)R constructs was characterized after expression in HEK 293T cells.
11415438	14	44	theme	R	2086:2086	arg1	N-glycosylation					2058:2072	N-glycosylation	2058:2072	N-glycosylation of the V(1a)R	2058:2086	This study establishes the functional importance of N-glycosylation of the V(1a)R.
11415438	9	45	theme	expression	1438:1447	arg1	level					1414:1418	the level	1410:1418	the level of total receptor expression	1410:1447	The glycosylation status of the V(1a)R did, however, regulate the level of total receptor expression and also the abundance of receptor at the cell surface.
11415438	9	46	theme	receptor	1429:1436	arg1	expression					1438:1447	total receptor expression	1423:1447	total receptor expression	1423:1447	The glycosylation status of the V(1a)R did, however, regulate the level of total receptor expression and also the abundance of receptor at the cell surface.
11415438	0	47	from	expression	139:148	arg1	receptor					74:81	the V1a vasopressin receptor	54:81	the V1a vasopressin receptor	54:81	Identification of the glycosylation sites utilized on the V1a vasopressin receptor and assessment of their role in receptor signalling and expression.
11415438	0	47	from	expression	139:148	arg1	assessment					87:96	assessment	87:96	assessment of their role in receptor signalling and expression	87:148	Identification of the glycosylation sites utilized on the V1a vasopressin receptor and assessment of their role in receptor signalling and expression.
11415438	6	48	gly	O-glycosylated	1043:1056	arg1	R					1034:1034	The V(1a)R	1025:1034	The V(1a)R	1025:1034	The V(1a)R is not O-glycosylated.
11415438	6	48	gly	O-glycosylated	1043:1056	arg1	O-glycosylated					1043:1056	O-glycosylated	1043:1056	O-glycosylated	1043:1056	The V(1a)R is not O-glycosylated.
11415438	14	49	theme	1a	2083:2084	arg1	R					2086:2086	the V(1a)R	2077:2086	the V(1a)R	2077:2086	This study establishes the functional importance of N-glycosylation of the V(1a)R.
11415438	2	50	used	utilized	411:418	arg2	any					356:358	any	356:358	any	356:358	However, for the vast majority of GPCRs, it has not been determined which, if any, of the consensus glycosylation sites are actually utilized or what the functional ramifications are of modification by oligosaccharide.
11415438	14	51	theme	V	2081:2081	arg1	R					2086:2086	the V(1a)R	2077:2086	the V(1a)R	2077:2086	This study establishes the functional importance of N-glycosylation of the V(1a)R.
11415438	11	52	theme	glycosylation	1786:1798	arg1	sites					1800:1804	the glycosylation sites	1782:1804	the glycosylation sites	1782:1804	Modification of any one of the consensus sites alone, however, was sufficient for wild-type expression, indicating a redundancy within the glycosylation sites.
11415438	4	53	theme	N-glycosylation	779:793	arg1	sites					795:799	the four putative N-glycosylation sites	761:799	the four putative N-glycosylation sites at Asn(14), Asn(27), Asn(198) and Asn(333)	761:842	Using a combination of translation systems that are either glycosylation-competent or do not support glycosylation, we established that of the four putative N-glycosylation sites at Asn(14), Asn(27), Asn(198) and Asn(333) only the first three sites are actually modified by carbohydrate.
11415438	12	54	theme	V	1882:1882	arg1	R					1887:1887	the V(1a)R	1878:1887	the V(1a)R	1878:1887	A role for the carbohydrate in the correct folding or stabilization of the V(1a)R is indicated.
11415438	0	55	theme	receptor	115:122	arg1	signalling					124:133	receptor signalling	115:133	receptor signalling	115:133	Identification of the glycosylation sites utilized on the V1a vasopressin receptor and assessment of their role in receptor signalling and expression.
11415438	2	56	theme	vast	295:298	arg1	majority					300:307	the vast majority	291:307	the vast majority of GPCRs	291:316	However, for the vast majority of GPCRs, it has not been determined which, if any, of the consensus glycosylation sites are actually utilized or what the functional ramifications are of modification by oligosaccharide.
11415438	1	57	theme	G-protein-coupled	179:195	arg1	receptors					197:205	G-protein-coupled receptors	179:205	G-protein-coupled receptors (GPCRs)	179:213	Most of the large family of G-protein-coupled receptors (GPCRs) possess putative N-glycosylation sites within their N-termini.
11415438	1	57	theme	G-protein-coupled	179:195	arg1	GPCRs					208:212	GPCRs	208:212	GPCRs	208:212	Most of the large family of G-protein-coupled receptors (GPCRs) possess putative N-glycosylation sites within their N-termini.
11415438	3	58	theme	V	549:549	arg1	R					582:582	V(1a)R	577:582	V(1a)R	577:582	The occurrence and function of glycosylation of the V(1a) vasopressin receptor (V(1a)R) has been investigated in this study.
11415438	3	58	theme	V	549:549	arg1	receptor					567:574	the V(1a) vasopressin receptor	545:574	the V(1a) vasopressin receptor (V(1a)R)	545:583	The occurrence and function of glycosylation of the V(1a) vasopressin receptor (V(1a)R) has been investigated in this study.
11415438	12	59	theme	correct	1842:1848	arg1	folding					1850:1856	folding	1850:1856	folding	1850:1856	A role for the carbohydrate in the correct folding or stabilization of the V(1a)R is indicated.
11415438	4	60	gly	N-glycosylation	779:793	arg2	Asn					804:806	Asn	804:806	Asn(14)	804:810	Using a combination of translation systems that are either glycosylation-competent or do not support glycosylation, we established that of the four putative N-glycosylation sites at Asn(14), Asn(27), Asn(198) and Asn(333) only the first three sites are actually modified by carbohydrate.
11415438	4	60	gly	N-glycosylation	779:793	arg2	198					826:828	198	826:828	198	826:828	Using a combination of translation systems that are either glycosylation-competent or do not support glycosylation, we established that of the four putative N-glycosylation sites at Asn(14), Asn(27), Asn(198) and Asn(333) only the first three sites are actually modified by carbohydrate.
11415438	4	60	gly	N-glycosylation	779:793	arg2	Asn					813:815	Asn	813:815	Asn(27)	813:819	Using a combination of translation systems that are either glycosylation-competent or do not support glycosylation, we established that of the four putative N-glycosylation sites at Asn(14), Asn(27), Asn(198) and Asn(333) only the first three sites are actually modified by carbohydrate.
11415438	4	60	gly	N-glycosylation	779:793	arg2	14					808:809	14	808:809	14	808:809	Using a combination of translation systems that are either glycosylation-competent or do not support glycosylation, we established that of the four putative N-glycosylation sites at Asn(14), Asn(27), Asn(198) and Asn(333) only the first three sites are actually modified by carbohydrate.
11415438	4	60	gly	N-glycosylation	779:793	arg2	27					817:818	27	817:818	27	817:818	Using a combination of translation systems that are either glycosylation-competent or do not support glycosylation, we established that of the four putative N-glycosylation sites at Asn(14), Asn(27), Asn(198) and Asn(333) only the first three sites are actually modified by carbohydrate.
11415438	4	60	gly	N-glycosylation	779:793	arg2	Asn					822:824	Asn	822:824	Asn(198)	822:829	Using a combination of translation systems that are either glycosylation-competent or do not support glycosylation, we established that of the four putative N-glycosylation sites at Asn(14), Asn(27), Asn(198) and Asn(333) only the first three sites are actually modified by carbohydrate.
11415438	4	60	gly	N-glycosylation	779:793	arg2	Asn					835:837	Asn	835:837	Asn(333)	835:842	Using a combination of translation systems that are either glycosylation-competent or do not support glycosylation, we established that of the four putative N-glycosylation sites at Asn(14), Asn(27), Asn(198) and Asn(333) only the first three sites are actually modified by carbohydrate.
11415438	4	60	gly	N-glycosylation	779:793	arg2	four					765:768	four	765:768	four	765:768	Using a combination of translation systems that are either glycosylation-competent or do not support glycosylation, we established that of the four putative N-glycosylation sites at Asn(14), Asn(27), Asn(198) and Asn(333) only the first three sites are actually modified by carbohydrate.
11415438	4	60	gly	N-glycosylation	779:793	arg2	333					839:841	333	839:841	333	839:841	Using a combination of translation systems that are either glycosylation-competent or do not support glycosylation, we established that of the four putative N-glycosylation sites at Asn(14), Asn(27), Asn(198) and Asn(333) only the first three sites are actually modified by carbohydrate.
11415438	4	60	gly	N-glycosylation	779:793	arg2	sites					795:799	the four putative N-glycosylation sites	761:799	the four putative N-glycosylation sites at Asn(14), Asn(27), Asn(198) and Asn(333)	761:842	Using a combination of translation systems that are either glycosylation-competent or do not support glycosylation, we established that of the four putative N-glycosylation sites at Asn(14), Asn(27), Asn(198) and Asn(333) only the first three sites are actually modified by carbohydrate.
11415438	1	61	contain	possess	215:221	arg1	family					169:174	the large family	159:174	the large family of G-protein-coupled receptors (GPCRs)	159:213	Most of the large family of G-protein-coupled receptors (GPCRs) possess putative N-glycosylation sites within their N-termini.
11415438	1	61	contain	possess	215:221	arg1	Most					151:154	Most	151:154	Most	151:154	Most of the large family of G-protein-coupled receptors (GPCRs) possess putative N-glycosylation sites within their N-termini.
11415438	1	61	contain	possess	215:221	arg2	sites					248:252	putative N-glycosylation sites	223:252	putative N-glycosylation sites within their N-termini	223:275	Most of the large family of G-protein-coupled receptors (GPCRs) possess putative N-glycosylation sites within their N-termini.
11415438	3	62	dep	occurrence	501:510	arg1	The					497:499	The	497:499	The	497:499	The occurrence and function of glycosylation of the V(1a) vasopressin receptor (V(1a)R) has been investigated in this study.
11415438	9	63	theme	cell	1491:1494	arg1	surface					1496:1502	the cell surface	1487:1502	the cell surface	1487:1502	The glycosylation status of the V(1a)R did, however, regulate the level of total receptor expression and also the abundance of receptor at the cell surface.
11415438	0	64	from	role	107:110	arg1	signalling					124:133	receptor signalling	115:133	receptor signalling	115:133	Identification of the glycosylation sites utilized on the V1a vasopressin receptor and assessment of their role in receptor signalling and expression.
11415438	0	64	from	role	107:110	arg1	expression					139:148	expression	139:148	expression	139:148	Identification of the glycosylation sites utilized on the V1a vasopressin receptor and assessment of their role in receptor signalling and expression.
11415438	14	65	theme	N-glycosylation	2058:2072	arg1	importance					2044:2053	the functional importance	2029:2053	the functional importance of N-glycosylation of the V(1a)R	2029:2086	This study establishes the functional importance of N-glycosylation of the V(1a)R.
11415438	4	66	from	Asn	813:815	arg1	sites					795:799	the four putative N-glycosylation sites	761:799	the four putative N-glycosylation sites at Asn(14), Asn(27), Asn(198) and Asn(333)	761:842	Using a combination of translation systems that are either glycosylation-competent or do not support glycosylation, we established that of the four putative N-glycosylation sites at Asn(14), Asn(27), Asn(198) and Asn(333) only the first three sites are actually modified by carbohydrate.
11415438	3	67	theme	V	577:577	arg1	R					582:582	V(1a)R	577:582	V(1a)R	577:582	The occurrence and function of glycosylation of the V(1a) vasopressin receptor (V(1a)R) has been investigated in this study.
11415438	3	67	theme	V	577:577	arg1	receptor					567:574	the V(1a) vasopressin receptor	545:574	the V(1a) vasopressin receptor (V(1a)R)	545:583	The occurrence and function of glycosylation of the V(1a) vasopressin receptor (V(1a)R) has been investigated in this study.
11415438	3	68	theme	glycosylation	528:540	arg1	function					516:523	function	516:523	function	516:523	The occurrence and function of glycosylation of the V(1a) vasopressin receptor (V(1a)R) has been investigated in this study.
11415438	3	68	theme	glycosylation	528:540	arg1	occurrence					501:510	occurrence	501:510	occurrence	501:510	The occurrence and function of glycosylation of the V(1a) vasopressin receptor (V(1a)R) has been investigated in this study.
11415438	9	69	from	surface	1496:1502	arg1	abundance					1462:1470	the abundance	1458:1470	the abundance of receptor at the cell surface	1458:1502	The glycosylation status of the V(1a)R did, however, regulate the level of total receptor expression and also the abundance of receptor at the cell surface.
11415438	10	70	dep	regulation	1537:1546	arg1	decreased					1562:1570	decreased	1562:1570	decreased expression	1562:1581	Furthermore, the nature of this regulation (increased or decreased expression) was dictated by the locus of the oligosaccharide modification.
11415438	10	70	dep	regulation	1537:1546	arg1	increased					1549:1557	increased	1549:1557	increased	1549:1557	Furthermore, the nature of this regulation (increased or decreased expression) was dictated by the locus of the oligosaccharide modification.
11415438	0	71	theme	vasopressin	62:72	arg1	receptor					74:81	the V1a vasopressin receptor	54:81	the V1a vasopressin receptor	54:81	Identification of the glycosylation sites utilized on the V1a vasopressin receptor and assessment of their role in receptor signalling and expression.
11415438	3	72	theme	receptor	567:574	arg1	glycosylation					528:540	glycosylation	528:540	glycosylation of the V(1a) vasopressin receptor (V(1a)R)	528:583	The occurrence and function of glycosylation of the V(1a) vasopressin receptor (V(1a)R) has been investigated in this study.
11415438	12	73	from	role	1809:1812	arg1	stabilization					1861:1873	stabilization	1861:1873	stabilization	1861:1873	A role for the carbohydrate in the correct folding or stabilization of the V(1a)R is indicated.
11415438	12	73	from	role	1809:1812	arg1	folding					1850:1856	folding	1850:1856	folding	1850:1856	A role for the carbohydrate in the correct folding or stabilization of the V(1a)R is indicated.
11415438	8	74	theme	available	1304:1312	arg1	ligand					1297:1302	ligand available	1297:1312	ligand available	1297:1312	It was found that carbohydrate moieties are not required for the receptor to bind any of the four classes of ligand available, or for intracellular signalling.
11415438	7	75	theme	293T	1176:1179	arg1	cells					1181:1185	HEK 293T cells	1172:1185	HEK 293T cells	1172:1185	The functionality of a series of glycosylation-defective V(1a)R constructs was characterized after expression in HEK 293T cells.
11415438	13	76	theme	receptor	1976:1983	arg1	trafficking					1957:1967	efficient trafficking	1947:1967	efficient trafficking of the receptor to the cell surface	1947:2003	Glycosylation is not required, however, for efficient trafficking of the receptor to the cell surface.
11415438	2	77	gly	glycosylation	378:390	arg2	sites					392:396	the consensus glycosylation sites	364:396	the consensus glycosylation sites	364:396	However, for the vast majority of GPCRs, it has not been determined which, if any, of the consensus glycosylation sites are actually utilized or what the functional ramifications are of modification by oligosaccharide.
11415438	8	78	theme	intracellular	1322:1334	arg1	signalling					1336:1345	intracellular signalling	1322:1345	intracellular signalling	1322:1345	It was found that carbohydrate moieties are not required for the receptor to bind any of the four classes of ligand available, or for intracellular signalling.
11415438	0	79	theme	role	107:110	arg1	receptor					74:81	the V1a vasopressin receptor	54:81	the V1a vasopressin receptor	54:81	Identification of the glycosylation sites utilized on the V1a vasopressin receptor and assessment of their role in receptor signalling and expression.
11415438	0	79	theme	role	107:110	arg1	assessment					87:96	assessment	87:96	assessment of their role in receptor signalling and expression	87:148	Identification of the glycosylation sites utilized on the V1a vasopressin receptor and assessment of their role in receptor signalling and expression.
11415438	5	80	theme	consensus	946:954	arg1	sites					956:960	consensus sites	946:960	consensus sites	946:960	This was confirmed by disruption of consensus sites by site-directed mutagenesis, individually and in combination.
11415438	0	81	from	signalling	124:133	arg1	receptor					74:81	the V1a vasopressin receptor	54:81	the V1a vasopressin receptor	54:81	Identification of the glycosylation sites utilized on the V1a vasopressin receptor and assessment of their role in receptor signalling and expression.
11415438	0	81	from	signalling	124:133	arg1	assessment					87:96	assessment	87:96	assessment of their role in receptor signalling and expression	87:148	Identification of the glycosylation sites utilized on the V1a vasopressin receptor and assessment of their role in receptor signalling and expression.
11415438	0	82	used	utilized	42:49	arg2	Identification					0:13	Identification	0:13	Identification of the glycosylation sites	0:40	Identification of the glycosylation sites utilized on the V1a vasopressin receptor and assessment of their role in receptor signalling and expression.
11415438	2	83	dep	utilized	411:418	arg1	which					346:350	which	346:350	which	346:350	However, for the vast majority of GPCRs, it has not been determined which, if any, of the consensus glycosylation sites are actually utilized or what the functional ramifications are of modification by oligosaccharide.
11415438	9	84	gly	glycosylation	1352:1364	arg1	R					1385:1385	the V(1a)R	1376:1385	the V(1a)R	1376:1385	The glycosylation status of the V(1a)R did, however, regulate the level of total receptor expression and also the abundance of receptor at the cell surface.
11415438	4	85	theme	systems	657:663	arg1	combination					630:640	a combination	628:640	a combination of translation systems that are either glycosylation-competent or do not support glycosylation	628:735	Using a combination of translation systems that are either glycosylation-competent or do not support glycosylation, we established that of the four putative N-glycosylation sites at Asn(14), Asn(27), Asn(198) and Asn(333) only the first three sites are actually modified by carbohydrate.
11415438	0	86	theme	glycosylation	22:34	arg1	sites					36:40	the glycosylation sites	18:40	the glycosylation sites	18:40	Identification of the glycosylation sites utilized on the V1a vasopressin receptor and assessment of their role in receptor signalling and expression.
11415438	7	87	theme	constructs	1123:1132	arg1	series					1082:1087	a series	1080:1087	a series of glycosylation-defective V(1a)R constructs	1080:1132	The functionality of a series of glycosylation-defective V(1a)R constructs was characterized after expression in HEK 293T cells.
11415438	2	88	theme	consensus	368:376	arg1	sites					392:396	the consensus glycosylation sites	364:396	the consensus glycosylation sites	364:396	However, for the vast majority of GPCRs, it has not been determined which, if any, of the consensus glycosylation sites are actually utilized or what the functional ramifications are of modification by oligosaccharide.
11415438	3	89	theme	1a	579:580	arg1	R					582:582	V(1a)R	577:582	V(1a)R	577:582	The occurrence and function of glycosylation of the V(1a) vasopressin receptor (V(1a)R) has been investigated in this study.
11415438	3	89	theme	1a	579:580	arg1	receptor					567:574	the V(1a) vasopressin receptor	545:574	the V(1a) vasopressin receptor (V(1a)R)	545:583	The occurrence and function of glycosylation of the V(1a) vasopressin receptor (V(1a)R) has been investigated in this study.
11415438	8	90	theme	carbohydrate	1206:1217	arg1	moieties					1219:1226	carbohydrate moieties	1206:1226	carbohydrate moieties	1206:1226	It was found that carbohydrate moieties are not required for the receptor to bind any of the four classes of ligand available, or for intracellular signalling.
11415438	11	91	theme	consensus	1678:1686	arg1	sites					1688:1692	the consensus sites	1674:1692	the consensus sites alone	1674:1698	Modification of any one of the consensus sites alone, however, was sufficient for wild-type expression, indicating a redundancy within the glycosylation sites.
11415438	4	92	mod	modified	884:891	arg3	carbohydrate					896:907	carbohydrate	896:907	carbohydrate	896:907	Using a combination of translation systems that are either glycosylation-competent or do not support glycosylation, we established that of the four putative N-glycosylation sites at Asn(14), Asn(27), Asn(198) and Asn(333) only the first three sites are actually modified by carbohydrate.
11415438	4	92	mod	modified	884:891	arg1	sites					865:869	only the first three sites	844:869	only the first three sites	844:869	Using a combination of translation systems that are either glycosylation-competent or do not support glycosylation, we established that of the four putative N-glycosylation sites at Asn(14), Asn(27), Asn(198) and Asn(333) only the first three sites are actually modified by carbohydrate.
11415438	12	93	dep	folding	1850:1856	arg1	the					1838:1840	the	1838:1840	the	1838:1840	A role for the carbohydrate in the correct folding or stabilization of the V(1a)R is indicated.
11415438	4	94	theme	first	853:857	arg1	sites					865:869	only the first three sites	844:869	only the first three sites	844:869	Using a combination of translation systems that are either glycosylation-competent or do not support glycosylation, we established that of the four putative N-glycosylation sites at Asn(14), Asn(27), Asn(198) and Asn(333) only the first three sites are actually modified by carbohydrate.
11415438	12	95	theme	R	1887:1887	arg1	stabilization					1861:1873	stabilization	1861:1873	stabilization	1861:1873	A role for the carbohydrate in the correct folding or stabilization of the V(1a)R is indicated.
11415438	12	95	theme	R	1887:1887	arg1	folding					1850:1856	folding	1850:1856	folding	1850:1856	A role for the carbohydrate in the correct folding or stabilization of the V(1a)R is indicated.
11415438	7	96	theme	glycosylation-defective	1092:1114	arg1	constructs					1123:1132	glycosylation-defective V(1a)R constructs	1092:1132	glycosylation-defective V(1a)R constructs	1092:1132	The functionality of a series of glycosylation-defective V(1a)R constructs was characterized after expression in HEK 293T cells.
11415438	10	97	theme	modification	1633:1644	arg1	locus					1604:1608	the locus	1600:1608	the locus of the oligosaccharide modification	1600:1644	Furthermore, the nature of this regulation (increased or decreased expression) was dictated by the locus of the oligosaccharide modification.
11415438	12	98	theme	1a	1884:1885	arg1	R					1887:1887	the V(1a)R	1878:1887	the V(1a)R	1878:1887	A role for the carbohydrate in the correct folding or stabilization of the V(1a)R is indicated.
11415438	2	99	theme	GPCRs	312:316	arg1	majority					300:307	the vast majority	291:307	the vast majority of GPCRs	291:316	However, for the vast majority of GPCRs, it has not been determined which, if any, of the consensus glycosylation sites are actually utilized or what the functional ramifications are of modification by oligosaccharide.
11415438	7	100	theme	series	1082:1087	arg1	functionality					1063:1075	The functionality	1059:1075	The functionality of a series of glycosylation-defective V(1a)R constructs	1059:1132	The functionality of a series of glycosylation-defective V(1a)R constructs was characterized after expression in HEK 293T cells.
11415438	1	101	theme	N-glycosylation	232:246	arg1	sites					248:252	putative N-glycosylation sites	223:252	putative N-glycosylation sites within their N-termini	223:275	Most of the large family of G-protein-coupled receptors (GPCRs) possess putative N-glycosylation sites within their N-termini.
11415438	4	102	from	Asn	835:837	arg1	sites					795:799	the four putative N-glycosylation sites	761:799	the four putative N-glycosylation sites at Asn(14), Asn(27), Asn(198) and Asn(333)	761:842	Using a combination of translation systems that are either glycosylation-competent or do not support glycosylation, we established that of the four putative N-glycosylation sites at Asn(14), Asn(27), Asn(198) and Asn(333) only the first three sites are actually modified by carbohydrate.
15450944	6	0	theme	important	1364:1372	arg1	role					1374:1377	an important role	1361:1377	an important role for N-glycosylation at multiple identified asparagine residues	1361:1440	The present study demonstrates an important role for N-glycosylation at multiple identified asparagine residues in the N-terminus of the h5-HT3A receptor subunit.
15450944	5	1	theme	radioligand	1108:1118	arg1	studies					1128:1134	the radioligand binding studies	1104:1134	the radioligand binding studies	1104:1134	Corresponding with the radioligand binding studies, immunocytochemical studies demonstrated that substitution of each asparagine either prevented (N81, N147, N163) or reduced considerably (N5) mutant protein expression within the cell membrane.
15450944	3	2	theme	Site-directed	513:525	arg1	studies					539:545	Site-directed mutagenesis studies	513:545	Site-directed mutagenesis studies individually substituting four identified N-terminal asparagines (N5, N81, N147, N163)	513:632	Site-directed mutagenesis studies individually substituting four identified N-terminal asparagines (N5, N81, N147, N163) demonstrated that each expressed mutant displayed a reduced molecular weight (by approximately 3 kDa) suggesting that each asparagine residue was subject to N-glycosylation.
15450944	5	3	theme	asparagine	1203:1212	arg1	substitution					1182:1193	substitution	1182:1193	substitution of each asparagine	1182:1212	Corresponding with the radioligand binding studies, immunocytochemical studies demonstrated that substitution of each asparagine either prevented (N81, N147, N163) or reduced considerably (N5) mutant protein expression within the cell membrane.
15450944	0	4	theme	subunit	93:99	arg1	N-glycosylation					33:47	N-glycosylation	33:47	N-glycosylation of the human 5-hydroxytryptamine3A receptor subunit	33:99	Identification and importance of N-glycosylation of the human 5-hydroxytryptamine3A receptor subunit.
15450944	5	5	theme	binding	1120:1126	arg1	studies					1128:1134	the radioligand binding studies	1104:1134	the radioligand binding studies	1104:1134	Corresponding with the radioligand binding studies, immunocytochemical studies demonstrated that substitution of each asparagine either prevented (N81, N147, N163) or reduced considerably (N5) mutant protein expression within the cell membrane.
15450944	4	6	dep	reduced	1023:1029	arg1	N5					1032:1033	N5	1032:1033	N5	1032:1033	In addition, 5-HT3 receptor binding studies indicated that prevention of N-glycosylation, by individual amino acid substitution at each of the four asparagine residues, either prevented (N81, N147, N163) or greatly reduced (N5) the production of a 5-HT3 receptor binding site.
15450944	1	7	theme	human	176:180	arg1	subunit					225:231	the human (h) 5-hydroxytryptamine3 (5-HT3A) receptor subunit	172:231	the human (h) 5-hydroxytryptamine3 (5-HT3A) receptor subunit expressed in COS-7 cells	172:256	We investigated the presence and potential role of N-glycosylation of the human (h) 5-hydroxytryptamine3 (5-HT3A) receptor subunit expressed in COS-7 cells.
15450944	6	8	from	residues	1433:1440	arg1	role					1374:1377	an important role	1361:1377	an important role for N-glycosylation at multiple identified asparagine residues	1361:1440	The present study demonstrates an important role for N-glycosylation at multiple identified asparagine residues in the N-terminus of the h5-HT3A receptor subunit.
15450944	4	9	theme	amino	912:916	arg1	substitution					923:934	individual amino acid substitution	901:934	individual amino acid substitution at each of the four asparagine residues	901:974	In addition, 5-HT3 receptor binding studies indicated that prevention of N-glycosylation, by individual amino acid substitution at each of the four asparagine residues, either prevented (N81, N147, N163) or greatly reduced (N5) the production of a 5-HT3 receptor binding site.
15450944	2	10	theme	N-glycosylation	288:302	arg1	tunicamycin					315:325	tunicamycin	315:325	tunicamycin	315:325	Incubation of cells with the N-glycosylation inhibitor, tunicamycin, reduced the molecular weight of the predominant immunoreactive h5-HT3A subunit species (from approximately 59 to 45 kDa) indicating that the h5-HT3A subunit is normally N-glycosylated.
15450944	2	10	theme	N-glycosylation	288:302	arg1	inhibitor					304:312	the N-glycosylation inhibitor	284:312	the N-glycosylation inhibitor	284:312	Incubation of cells with the N-glycosylation inhibitor, tunicamycin, reduced the molecular weight of the predominant immunoreactive h5-HT3A subunit species (from approximately 59 to 45 kDa) indicating that the h5-HT3A subunit is normally N-glycosylated.
15450944	5	11	with	Corresponding	1085:1097	arg1	studies					1128:1134	the radioligand binding studies	1104:1134	the radioligand binding studies	1104:1134	Corresponding with the radioligand binding studies, immunocytochemical studies demonstrated that substitution of each asparagine either prevented (N81, N147, N163) or reduced considerably (N5) mutant protein expression within the cell membrane.
15450944	4	12	theme	individual	901:910	arg1	substitution					923:934	individual amino acid substitution	901:934	individual amino acid substitution at each of the four asparagine residues	901:974	In addition, 5-HT3 receptor binding studies indicated that prevention of N-glycosylation, by individual amino acid substitution at each of the four asparagine residues, either prevented (N81, N147, N163) or greatly reduced (N5) the production of a 5-HT3 receptor binding site.
15450944	2	13	from	weight	350:355	arg1	kDa					444:446	approximately 59 to 45 kDa	421:446	approximately 59 to 45 kDa	421:446	Incubation of cells with the N-glycosylation inhibitor, tunicamycin, reduced the molecular weight of the predominant immunoreactive h5-HT3A subunit species (from approximately 59 to 45 kDa) indicating that the h5-HT3A subunit is normally N-glycosylated.
15450944	3	14	theme	N-terminal	589:598	arg1	asparagines					600:610	four identified N-terminal asparagines	573:610	four identified N-terminal asparagines (N5, N81, N147, N163)	573:632	Site-directed mutagenesis studies individually substituting four identified N-terminal asparagines (N5, N81, N147, N163) demonstrated that each expressed mutant displayed a reduced molecular weight (by approximately 3 kDa) suggesting that each asparagine residue was subject to N-glycosylation.
15450944	6	15	theme	present	1334:1340	arg1	study					1342:1346	The present study	1330:1346	The present study	1330:1346	The present study demonstrates an important role for N-glycosylation at multiple identified asparagine residues in the N-terminus of the h5-HT3A receptor subunit.
15450944	5	16	dep	prevented	1221:1229	arg1	N81					1232:1234	N81	1232:1234	N81	1232:1234	Corresponding with the radioligand binding studies, immunocytochemical studies demonstrated that substitution of each asparagine either prevented (N81, N147, N163) or reduced considerably (N5) mutant protein expression within the cell membrane.
15450944	5	17	theme	cell	1315:1318	arg1	membrane					1320:1327	the cell membrane	1311:1327	the cell membrane	1311:1327	Corresponding with the radioligand binding studies, immunocytochemical studies demonstrated that substitution of each asparagine either prevented (N81, N147, N163) or reduced considerably (N5) mutant protein expression within the cell membrane.
15450944	2	18	dep	45	441:442	arg1	to					438:439	to	438:439	to	438:439	Incubation of cells with the N-glycosylation inhibitor, tunicamycin, reduced the molecular weight of the predominant immunoreactive h5-HT3A subunit species (from approximately 59 to 45 kDa) indicating that the h5-HT3A subunit is normally N-glycosylated.
15450944	2	19	theme	cells	273:277	arg1	Incubation					259:268	Incubation	259:268	Incubation of cells with the N-glycosylation inhibitor, tunicamycin,	259:326	Incubation of cells with the N-glycosylation inhibitor, tunicamycin, reduced the molecular weight of the predominant immunoreactive h5-HT3A subunit species (from approximately 59 to 45 kDa) indicating that the h5-HT3A subunit is normally N-glycosylated.
15450944	1	20	theme	h	183:183	arg1	subunit					225:231	the human (h) 5-hydroxytryptamine3 (5-HT3A) receptor subunit	172:231	the human (h) 5-hydroxytryptamine3 (5-HT3A) receptor subunit expressed in COS-7 cells	172:256	We investigated the presence and potential role of N-glycosylation of the human (h) 5-hydroxytryptamine3 (5-HT3A) receptor subunit expressed in COS-7 cells.
15450944	3	21	theme	asparagine	757:766	arg1	residue					768:774	each asparagine residue	752:774	each asparagine residue	752:774	Site-directed mutagenesis studies individually substituting four identified N-terminal asparagines (N5, N81, N147, N163) demonstrated that each expressed mutant displayed a reduced molecular weight (by approximately 3 kDa) suggesting that each asparagine residue was subject to N-glycosylation.
15450944	4	22	theme	N-glycosylation	881:895	arg1	prevention					867:876	prevention	867:876	prevention of N-glycosylation	867:895	In addition, 5-HT3 receptor binding studies indicated that prevention of N-glycosylation, by individual amino acid substitution at each of the four asparagine residues, either prevented (N81, N147, N163) or greatly reduced (N5) the production of a 5-HT3 receptor binding site.
15450944	5	23	dep	reduced	1252:1258	arg1	N5					1274:1275	N5	1274:1275	N5	1274:1275	Corresponding with the radioligand binding studies, immunocytochemical studies demonstrated that substitution of each asparagine either prevented (N81, N147, N163) or reduced considerably (N5) mutant protein expression within the cell membrane.
15450944	2	24	gly	N-glycosylated	497:510	arg1	N-glycosylated					497:510	N-glycosylated	497:510	N-glycosylated	497:510	Incubation of cells with the N-glycosylation inhibitor, tunicamycin, reduced the molecular weight of the predominant immunoreactive h5-HT3A subunit species (from approximately 59 to 45 kDa) indicating that the h5-HT3A subunit is normally N-glycosylated.
15450944	2	24	gly	N-glycosylated	497:510	arg1	subunit					477:483	the h5-HT3A subunit	465:483	the h5-HT3A subunit	465:483	Incubation of cells with the N-glycosylation inhibitor, tunicamycin, reduced the molecular weight of the predominant immunoreactive h5-HT3A subunit species (from approximately 59 to 45 kDa) indicating that the h5-HT3A subunit is normally N-glycosylated.
15450944	4	25	theme	acid	918:921	arg1	substitution					923:934	individual amino acid substitution	901:934	individual amino acid substitution at each of the four asparagine residues	901:974	In addition, 5-HT3 receptor binding studies indicated that prevention of N-glycosylation, by individual amino acid substitution at each of the four asparagine residues, either prevented (N81, N147, N163) or greatly reduced (N5) the production of a 5-HT3 receptor binding site.
15450944	2	26	theme	subunit	399:405	arg1	species					407:413	the predominant immunoreactive h5-HT3A subunit species	360:413	the predominant immunoreactive h5-HT3A subunit species (from approximately 59 to 45 kDa)	360:447	Incubation of cells with the N-glycosylation inhibitor, tunicamycin, reduced the molecular weight of the predominant immunoreactive h5-HT3A subunit species (from approximately 59 to 45 kDa) indicating that the h5-HT3A subunit is normally N-glycosylated.
15450944	4	27	from	each	939:942	arg1	substitution					923:934	individual amino acid substitution	901:934	individual amino acid substitution at each of the four asparagine residues	901:974	In addition, 5-HT3 receptor binding studies indicated that prevention of N-glycosylation, by individual amino acid substitution at each of the four asparagine residues, either prevented (N81, N147, N163) or greatly reduced (N5) the production of a 5-HT3 receptor binding site.
15450944	5	28	theme	mutant	1278:1283	arg1	expression					1293:1302	mutant protein expression	1278:1302	mutant protein expression	1278:1302	Corresponding with the radioligand binding studies, immunocytochemical studies demonstrated that substitution of each asparagine either prevented (N81, N147, N163) or reduced considerably (N5) mutant protein expression within the cell membrane.
15450944	2	29	theme	h5-HT3A	391:397	arg1	species					407:413	the predominant immunoreactive h5-HT3A subunit species	360:413	the predominant immunoreactive h5-HT3A subunit species (from approximately 59 to 45 kDa)	360:447	Incubation of cells with the N-glycosylation inhibitor, tunicamycin, reduced the molecular weight of the predominant immunoreactive h5-HT3A subunit species (from approximately 59 to 45 kDa) indicating that the h5-HT3A subunit is normally N-glycosylated.
15450944	4	30	dep	prevented	984:992	arg1	N81					995:997	N81	995:997	N81	995:997	In addition, 5-HT3 receptor binding studies indicated that prevention of N-glycosylation, by individual amino acid substitution at each of the four asparagine residues, either prevented (N81, N147, N163) or greatly reduced (N5) the production of a 5-HT3 receptor binding site.
15450944	5	31	theme	protein	1285:1291	arg1	expression					1293:1302	mutant protein expression	1278:1302	mutant protein expression	1278:1302	Corresponding with the radioligand binding studies, immunocytochemical studies demonstrated that substitution of each asparagine either prevented (N81, N147, N163) or reduced considerably (N5) mutant protein expression within the cell membrane.
15450944	4	32	theme	site	1079:1082	arg1	production					1040:1049	the production	1036:1049	the production of a 5-HT3 receptor binding site	1036:1082	In addition, 5-HT3 receptor binding studies indicated that prevention of N-glycosylation, by individual amino acid substitution at each of the four asparagine residues, either prevented (N81, N147, N163) or greatly reduced (N5) the production of a 5-HT3 receptor binding site.
15450944	6	33	theme	asparagine	1422:1431	arg1	residues					1433:1440	multiple identified asparagine residues	1402:1440	multiple identified asparagine residues	1402:1440	The present study demonstrates an important role for N-glycosylation at multiple identified asparagine residues in the N-terminus of the h5-HT3A receptor subunit.
15450944	2	34	theme	immunoreactive	376:389	arg1	species					407:413	the predominant immunoreactive h5-HT3A subunit species	360:413	the predominant immunoreactive h5-HT3A subunit species (from approximately 59 to 45 kDa)	360:447	Incubation of cells with the N-glycosylation inhibitor, tunicamycin, reduced the molecular weight of the predominant immunoreactive h5-HT3A subunit species (from approximately 59 to 45 kDa) indicating that the h5-HT3A subunit is normally N-glycosylated.
15450944	6	35	theme	multiple	1402:1409	arg1	residues					1433:1440	multiple identified asparagine residues	1402:1440	multiple identified asparagine residues	1402:1440	The present study demonstrates an important role for N-glycosylation at multiple identified asparagine residues in the N-terminus of the h5-HT3A receptor subunit.
15450944	3	36	theme	mutagenesis	527:537	arg1	studies					539:545	Site-directed mutagenesis studies	513:545	Site-directed mutagenesis studies individually substituting four identified N-terminal asparagines (N5, N81, N147, N163)	513:632	Site-directed mutagenesis studies individually substituting four identified N-terminal asparagines (N5, N81, N147, N163) demonstrated that each expressed mutant displayed a reduced molecular weight (by approximately 3 kDa) suggesting that each asparagine residue was subject to N-glycosylation.
15450944	1	37	theme	5-HT3A	208:213	arg1	subunit					225:231	the human (h) 5-hydroxytryptamine3 (5-HT3A) receptor subunit	172:231	the human (h) 5-hydroxytryptamine3 (5-HT3A) receptor subunit expressed in COS-7 cells	172:256	We investigated the presence and potential role of N-glycosylation of the human (h) 5-hydroxytryptamine3 (5-HT3A) receptor subunit expressed in COS-7 cells.
15450944	6	38	theme	identified	1411:1420	arg1	residues					1433:1440	multiple identified asparagine residues	1402:1440	multiple identified asparagine residues	1402:1440	The present study demonstrates an important role for N-glycosylation at multiple identified asparagine residues in the N-terminus of the h5-HT3A receptor subunit.
15450944	2	39	theme	molecular	340:348	arg1	weight					350:355	the molecular weight	336:355	the molecular weight of the predominant immunoreactive h5-HT3A subunit species (from approximately 59 to 45 kDa)	336:447	Incubation of cells with the N-glycosylation inhibitor, tunicamycin, reduced the molecular weight of the predominant immunoreactive h5-HT3A subunit species (from approximately 59 to 45 kDa) indicating that the h5-HT3A subunit is normally N-glycosylated.
15450944	4	40	theme	asparagine	956:965	arg1	residues					967:974	the four asparagine residues	947:974	the four asparagine residues	947:974	In addition, 5-HT3 receptor binding studies indicated that prevention of N-glycosylation, by individual amino acid substitution at each of the four asparagine residues, either prevented (N81, N147, N163) or greatly reduced (N5) the production of a 5-HT3 receptor binding site.
15450944	4	41	theme	binding	836:842	arg1	studies					844:850	5-HT3 receptor binding studies	821:850	5-HT3 receptor binding studies	821:850	In addition, 5-HT3 receptor binding studies indicated that prevention of N-glycosylation, by individual amino acid substitution at each of the four asparagine residues, either prevented (N81, N147, N163) or greatly reduced (N5) the production of a 5-HT3 receptor binding site.
15450944	1	42	theme	5-hydroxytryptamine3	186:205	arg1	subunit					225:231	the human (h) 5-hydroxytryptamine3 (5-HT3A) receptor subunit	172:231	the human (h) 5-hydroxytryptamine3 (5-HT3A) receptor subunit expressed in COS-7 cells	172:256	We investigated the presence and potential role of N-glycosylation of the human (h) 5-hydroxytryptamine3 (5-HT3A) receptor subunit expressed in COS-7 cells.
15450944	2	43	theme	h5-HT3A	469:475	arg1	N-glycosylated					497:510	N-glycosylated	497:510	N-glycosylated	497:510	Incubation of cells with the N-glycosylation inhibitor, tunicamycin, reduced the molecular weight of the predominant immunoreactive h5-HT3A subunit species (from approximately 59 to 45 kDa) indicating that the h5-HT3A subunit is normally N-glycosylated.
15450944	2	43	theme	h5-HT3A	469:475	arg1	subunit					477:483	the h5-HT3A subunit	465:483	the h5-HT3A subunit	465:483	Incubation of cells with the N-glycosylation inhibitor, tunicamycin, reduced the molecular weight of the predominant immunoreactive h5-HT3A subunit species (from approximately 59 to 45 kDa) indicating that the h5-HT3A subunit is normally N-glycosylated.
15450944	0	44	theme	N-glycosylation	33:47	arg1	importance					19:28	importance	19:28	importance	19:28	Identification and importance of N-glycosylation of the human 5-hydroxytryptamine3A receptor subunit.
15450944	0	44	theme	N-glycosylation	33:47	arg1	Identification					0:13	Identification	0:13	Identification	0:13	Identification and importance of N-glycosylation of the human 5-hydroxytryptamine3A receptor subunit.
15450944	5	45	dep	N81	1232:1234	arg1	N163					1243:1246	N163	1243:1246	N163	1243:1246	Corresponding with the radioligand binding studies, immunocytochemical studies demonstrated that substitution of each asparagine either prevented (N81, N147, N163) or reduced considerably (N5) mutant protein expression within the cell membrane.
15450944	4	46	theme	receptor	827:834	arg1	studies					844:850	5-HT3 receptor binding studies	821:850	5-HT3 receptor binding studies	821:850	In addition, 5-HT3 receptor binding studies indicated that prevention of N-glycosylation, by individual amino acid substitution at each of the four asparagine residues, either prevented (N81, N147, N163) or greatly reduced (N5) the production of a 5-HT3 receptor binding site.
15450944	1	47	theme	receptor	216:223	arg1	subunit					225:231	the human (h) 5-hydroxytryptamine3 (5-HT3A) receptor subunit	172:231	the human (h) 5-hydroxytryptamine3 (5-HT3A) receptor subunit expressed in COS-7 cells	172:256	We investigated the presence and potential role of N-glycosylation of the human (h) 5-hydroxytryptamine3 (5-HT3A) receptor subunit expressed in COS-7 cells.
15450944	0	48	theme	human	56:60	arg1	subunit					93:99	the human 5-hydroxytryptamine3A receptor subunit	52:99	the human 5-hydroxytryptamine3A receptor subunit	52:99	Identification and importance of N-glycosylation of the human 5-hydroxytryptamine3A receptor subunit.
15450944	5	49	theme	immunocytochemical	1137:1154	arg1	studies					1156:1162	immunocytochemical studies	1137:1162	immunocytochemical studies	1137:1162	Corresponding with the radioligand binding studies, immunocytochemical studies demonstrated that substitution of each asparagine either prevented (N81, N147, N163) or reduced considerably (N5) mutant protein expression within the cell membrane.
15450944	3	50	theme	expressed	657:665	arg1	mutant					667:672	each expressed mutant	652:672	each expressed mutant	652:672	Site-directed mutagenesis studies individually substituting four identified N-terminal asparagines (N5, N81, N147, N163) demonstrated that each expressed mutant displayed a reduced molecular weight (by approximately 3 kDa) suggesting that each asparagine residue was subject to N-glycosylation.
15450944	6	51	theme	subunit	1484:1490	arg1	N-terminus					1449:1458	the N-terminus	1445:1458	the N-terminus of the h5-HT3A receptor subunit	1445:1490	The present study demonstrates an important role for N-glycosylation at multiple identified asparagine residues in the N-terminus of the h5-HT3A receptor subunit.
15450944	1	52	gly	N-glycosylation	153:167	arg1	subunit					225:231	the human (h) 5-hydroxytryptamine3 (5-HT3A) receptor subunit	172:231	the human (h) 5-hydroxytryptamine3 (5-HT3A) receptor subunit expressed in COS-7 cells	172:256	We investigated the presence and potential role of N-glycosylation of the human (h) 5-hydroxytryptamine3 (5-HT3A) receptor subunit expressed in COS-7 cells.
15450944	3	53	theme	molecular	694:702	arg1	weight					704:709	a reduced molecular weight	684:709	a reduced molecular weight (by approximately 3 kDa)	684:734	Site-directed mutagenesis studies individually substituting four identified N-terminal asparagines (N5, N81, N147, N163) demonstrated that each expressed mutant displayed a reduced molecular weight (by approximately 3 kDa) suggesting that each asparagine residue was subject to N-glycosylation.
15450944	6	54	theme	receptor	1475:1482	arg1	subunit					1484:1490	the h5-HT3A receptor subunit	1463:1490	the h5-HT3A receptor subunit	1463:1490	The present study demonstrates an important role for N-glycosylation at multiple identified asparagine residues in the N-terminus of the h5-HT3A receptor subunit.
15450944	1	55	theme	potential	135:143	arg1	role					145:148	potential role	135:148	potential role	135:148	We investigated the presence and potential role of N-glycosylation of the human (h) 5-hydroxytryptamine3 (5-HT3A) receptor subunit expressed in COS-7 cells.
15450944	4	56	theme	5-HT3	1056:1060	arg1	site					1079:1082	a 5-HT3 receptor binding site	1054:1082	a 5-HT3 receptor binding site	1054:1082	In addition, 5-HT3 receptor binding studies indicated that prevention of N-glycosylation, by individual amino acid substitution at each of the four asparagine residues, either prevented (N81, N147, N163) or greatly reduced (N5) the production of a 5-HT3 receptor binding site.
15450944	2	57	with	Incubation	259:268	arg1	tunicamycin					315:325	tunicamycin	315:325	tunicamycin	315:325	Incubation of cells with the N-glycosylation inhibitor, tunicamycin, reduced the molecular weight of the predominant immunoreactive h5-HT3A subunit species (from approximately 59 to 45 kDa) indicating that the h5-HT3A subunit is normally N-glycosylated.
15450944	2	57	with	Incubation	259:268	arg1	inhibitor					304:312	the N-glycosylation inhibitor	284:312	the N-glycosylation inhibitor	284:312	Incubation of cells with the N-glycosylation inhibitor, tunicamycin, reduced the molecular weight of the predominant immunoreactive h5-HT3A subunit species (from approximately 59 to 45 kDa) indicating that the h5-HT3A subunit is normally N-glycosylated.
15450944	4	58	dep	N81	995:997	arg1	N163					1006:1009	N163	1006:1009	N163	1006:1009	In addition, 5-HT3 receptor binding studies indicated that prevention of N-glycosylation, by individual amino acid substitution at each of the four asparagine residues, either prevented (N81, N147, N163) or greatly reduced (N5) the production of a 5-HT3 receptor binding site.
15450944	0	59	gly	N-glycosylation	33:47	arg1	subunit					93:99	the human 5-hydroxytryptamine3A receptor subunit	52:99	the human 5-hydroxytryptamine3A receptor subunit	52:99	Identification and importance of N-glycosylation of the human 5-hydroxytryptamine3A receptor subunit.
15450944	1	60	theme	subunit	225:231	arg1	N-glycosylation					153:167	N-glycosylation	153:167	N-glycosylation of the human (h) 5-hydroxytryptamine3 (5-HT3A) receptor subunit expressed in COS-7 cells	153:256	We investigated the presence and potential role of N-glycosylation of the human (h) 5-hydroxytryptamine3 (5-HT3A) receptor subunit expressed in COS-7 cells.
15450944	3	61	theme	identified	578:587	arg1	asparagines					600:610	four identified N-terminal asparagines	573:610	four identified N-terminal asparagines (N5, N81, N147, N163)	573:632	Site-directed mutagenesis studies individually substituting four identified N-terminal asparagines (N5, N81, N147, N163) demonstrated that each expressed mutant displayed a reduced molecular weight (by approximately 3 kDa) suggesting that each asparagine residue was subject to N-glycosylation.
15450944	4	62	theme	receptor	1062:1069	arg1	site					1079:1082	a 5-HT3 receptor binding site	1054:1082	a 5-HT3 receptor binding site	1054:1082	In addition, 5-HT3 receptor binding studies indicated that prevention of N-glycosylation, by individual amino acid substitution at each of the four asparagine residues, either prevented (N81, N147, N163) or greatly reduced (N5) the production of a 5-HT3 receptor binding site.
15450944	2	63	theme	predominant	364:374	arg1	species					407:413	the predominant immunoreactive h5-HT3A subunit species	360:413	the predominant immunoreactive h5-HT3A subunit species (from approximately 59 to 45 kDa)	360:447	Incubation of cells with the N-glycosylation inhibitor, tunicamycin, reduced the molecular weight of the predominant immunoreactive h5-HT3A subunit species (from approximately 59 to 45 kDa) indicating that the h5-HT3A subunit is normally N-glycosylated.
15450944	4	64	theme	binding	1071:1077	arg1	site					1079:1082	a 5-HT3 receptor binding site	1054:1082	a 5-HT3 receptor binding site	1054:1082	In addition, 5-HT3 receptor binding studies indicated that prevention of N-glycosylation, by individual amino acid substitution at each of the four asparagine residues, either prevented (N81, N147, N163) or greatly reduced (N5) the production of a 5-HT3 receptor binding site.
15450944	0	65	theme	receptor	84:91	arg1	subunit					93:99	the human 5-hydroxytryptamine3A receptor subunit	52:99	the human 5-hydroxytryptamine3A receptor subunit	52:99	Identification and importance of N-glycosylation of the human 5-hydroxytryptamine3A receptor subunit.
15450944	3	66	theme	reduced	686:692	arg1	weight					704:709	a reduced molecular weight	684:709	a reduced molecular weight (by approximately 3 kDa)	684:734	Site-directed mutagenesis studies individually substituting four identified N-terminal asparagines (N5, N81, N147, N163) demonstrated that each expressed mutant displayed a reduced molecular weight (by approximately 3 kDa) suggesting that each asparagine residue was subject to N-glycosylation.
15450944	4	67	theme	5-HT3	821:825	arg1	studies					844:850	5-HT3 receptor binding studies	821:850	5-HT3 receptor binding studies	821:850	In addition, 5-HT3 receptor binding studies indicated that prevention of N-glycosylation, by individual amino acid substitution at each of the four asparagine residues, either prevented (N81, N147, N163) or greatly reduced (N5) the production of a 5-HT3 receptor binding site.
15450944	3	68	dep	asparagines	600:610	arg1	N81					617:619	N81	617:619	N81	617:619	Site-directed mutagenesis studies individually substituting four identified N-terminal asparagines (N5, N81, N147, N163) demonstrated that each expressed mutant displayed a reduced molecular weight (by approximately 3 kDa) suggesting that each asparagine residue was subject to N-glycosylation.
15450944	3	68	dep	asparagines	600:610	arg1	N5					613:614	N5	613:614	N5	613:614	Site-directed mutagenesis studies individually substituting four identified N-terminal asparagines (N5, N81, N147, N163) demonstrated that each expressed mutant displayed a reduced molecular weight (by approximately 3 kDa) suggesting that each asparagine residue was subject to N-glycosylation.
15450944	3	68	dep	asparagines	600:610	arg1	N163					628:631	N163	628:631	N163	628:631	Site-directed mutagenesis studies individually substituting four identified N-terminal asparagines (N5, N81, N147, N163) demonstrated that each expressed mutant displayed a reduced molecular weight (by approximately 3 kDa) suggesting that each asparagine residue was subject to N-glycosylation.
15450944	1	69	theme	N-glycosylation	153:167	arg1	role					145:148	potential role	135:148	potential role	135:148	We investigated the presence and potential role of N-glycosylation of the human (h) 5-hydroxytryptamine3 (5-HT3A) receptor subunit expressed in COS-7 cells.
15450944	1	69	theme	N-glycosylation	153:167	arg1	presence					122:129	presence	122:129	presence	122:129	We investigated the presence and potential role of N-glycosylation of the human (h) 5-hydroxytryptamine3 (5-HT3A) receptor subunit expressed in COS-7 cells.
15450944	2	70	theme	species	407:413	arg1	weight					350:355	the molecular weight	336:355	the molecular weight of the predominant immunoreactive h5-HT3A subunit species (from approximately 59 to 45 kDa)	336:447	Incubation of cells with the N-glycosylation inhibitor, tunicamycin, reduced the molecular weight of the predominant immunoreactive h5-HT3A subunit species (from approximately 59 to 45 kDa) indicating that the h5-HT3A subunit is normally N-glycosylated.
15450944	0	71	theme	5-hydroxytryptamine3A	62:82	arg1	subunit					93:99	the human 5-hydroxytryptamine3A receptor subunit	52:99	the human 5-hydroxytryptamine3A receptor subunit	52:99	Identification and importance of N-glycosylation of the human 5-hydroxytryptamine3A receptor subunit.
15450944	2	72	from	kDa	444:446	arg1	species					407:413	the predominant immunoreactive h5-HT3A subunit species	360:413	the predominant immunoreactive h5-HT3A subunit species (from approximately 59 to 45 kDa)	360:447	Incubation of cells with the N-glycosylation inhibitor, tunicamycin, reduced the molecular weight of the predominant immunoreactive h5-HT3A subunit species (from approximately 59 to 45 kDa) indicating that the h5-HT3A subunit is normally N-glycosylated.
15450944	2	72	from	kDa	444:446	arg1	weight					350:355	the molecular weight	336:355	the molecular weight of the predominant immunoreactive h5-HT3A subunit species (from approximately 59 to 45 kDa)	336:447	Incubation of cells with the N-glycosylation inhibitor, tunicamycin, reduced the molecular weight of the predominant immunoreactive h5-HT3A subunit species (from approximately 59 to 45 kDa) indicating that the h5-HT3A subunit is normally N-glycosylated.
15450944	1	73	dep	presence	122:129	arg1	the					118:120	the	118:120	the	118:120	We investigated the presence and potential role of N-glycosylation of the human (h) 5-hydroxytryptamine3 (5-HT3A) receptor subunit expressed in COS-7 cells.
15450944	6	74	theme	h5-HT3A	1467:1473	arg1	subunit					1484:1490	the h5-HT3A receptor subunit	1463:1490	the h5-HT3A receptor subunit	1463:1490	The present study demonstrates an important role for N-glycosylation at multiple identified asparagine residues in the N-terminus of the h5-HT3A receptor subunit.
15450944	1	75	theme	COS-7	246:250	arg1	cells					252:256	COS-7 cells	246:256	COS-7 cells	246:256	We investigated the presence and potential role of N-glycosylation of the human (h) 5-hydroxytryptamine3 (5-HT3A) receptor subunit expressed in COS-7 cells.
22766194	6	0	theme	NEP	1268:1270	arg1	activity					1272:1279	NEP activity	1268:1279	NEP activity	1268:1279	Although neither desialylation nor further degalactosylation caused defective NEP activity, removal of only a small part of N-glycans by treatment with glycopeptidase F under non-denaturing conditions decreased NEP activity completely.
22766194	3	1	gly	N-glycosylation	486:500	arg2	6					474:474	6	474:474	6	474:474	Although CD10 molecules of the human pre-B-cell line NALM-6 have 6 consensus N-glycosylation sites, three of them are known to be N-glycosylated by X-ray crystallography.
22766194	3	1	gly	N-glycosylation	486:500	arg2	sites					502:506	6 consensus N-glycosylation sites	474:506	6 consensus N-glycosylation sites	474:506	Although CD10 molecules of the human pre-B-cell line NALM-6 have 6 consensus N-glycosylation sites, three of them are known to be N-glycosylated by X-ray crystallography.
22766194	7	2	from	sites	1320:1324	arg1	cells					1344:1348	HEK293 cells	1337:1348	HEK293 cells introduced with wild type-CD10	1337:1379	All of the three consensus sites of CD10 in HEK293 cells introduced with wild type-CD10 were confirmed to be N-glycosylated.
22766194	10	3	theme	plasma	1778:1783	arg1	membrane					1785:1792	plasma membrane	1778:1792	plasma membrane	1778:1792	GENERAL SIGNIFICANCE: Quality control system does not allow dysfunctional ecto-type proteases to express on plasma membrane.
22766194	6	4	theme	glycopeptidase	1209:1222	arg1	F					1224:1224	glycopeptidase F	1209:1224	glycopeptidase F under non-denaturing conditions	1209:1256	Although neither desialylation nor further degalactosylation caused defective NEP activity, removal of only a small part of N-glycans by treatment with glycopeptidase F under non-denaturing conditions decreased NEP activity completely.
22766194	9	5	gly	N-glycosylation	1567:1581	arg1	surface					1650:1656	surface expression	1650:1667	surface expression	1650:1667	CONCLUSIONS: N-glycosylation at Asn(628) is essential not only for NEP activities, but also for surface expression.
22766194	9	5	gly	N-glycosylation	1567:1581	arg1	628					1590:1592	628	1590:1592	628	1590:1592	CONCLUSIONS: N-glycosylation at Asn(628) is essential not only for NEP activities, but also for surface expression.
22766194	9	5	gly	N-glycosylation	1567:1581	arg2	Asn					1586:1588	Asn	1586:1588	Asn(628)	1586:1593	CONCLUSIONS: N-glycosylation at Asn(628) is essential not only for NEP activities, but also for surface expression.
22766194	9	5	gly	N-glycosylation	1567:1581	arg1	Asn					1586:1588	Asn	1586:1588	Asn(628)	1586:1593	CONCLUSIONS: N-glycosylation at Asn(628) is essential not only for NEP activities, but also for surface expression.
22766194	9	5	gly	N-glycosylation	1567:1581	arg2	628					1590:1592	628	1590:1592	628	1590:1592	CONCLUSIONS: N-glycosylation at Asn(628) is essential not only for NEP activities, but also for surface expression.
22766194	9	5	gly	N-glycosylation	1567:1581	arg1	NEP					1621:1623	NEP activities	1621:1634	NEP activities	1621:1634	CONCLUSIONS: N-glycosylation at Asn(628) is essential not only for NEP activities, but also for surface expression.
22766194	4	6	theme	CD10	897:900	arg1	activities					865:874	the NEP activities	857:874	the NEP activities of the sugar-altered CD10	857:900	METHODS: In order to investigate the role of N-glycans in the full expression of NEP activity, we modified N-glycans by treatment of NALM6 cells with various glycosidases or alter each of the consensus N-glycosylation sites by generating site-directed mutagenesis and compared the NEP activities of the sugar-altered CD10 with those of intact CD10.
22766194	1	7	theme	cells	297:301	arg1	cells					297:301	cells	297:301	cells from normal tissues	297:321	BACKGROUND: CD10, also known as neprilysin or enkephalinase exhibiting neutral endopeptidase (NEP) activity, is expressed by B-lineage hematopoietic cells as well as a variety of cells from normal tissues.
22766194	1	7	theme	cells	297:301	arg1	variety					286:292	a variety	284:292	B-lineage hematopoietic cells as well as a variety of cells from normal tissues	243:321	BACKGROUND: CD10, also known as neprilysin or enkephalinase exhibiting neutral endopeptidase (NEP) activity, is expressed by B-lineage hematopoietic cells as well as a variety of cells from normal tissues.
22766194	1	7	theme	cells	297:301	arg1	cells					267:271	B-lineage hematopoietic cells	243:271	B-lineage hematopoietic cells as well as a variety of cells from normal tissues	243:321	BACKGROUND: CD10, also known as neprilysin or enkephalinase exhibiting neutral endopeptidase (NEP) activity, is expressed by B-lineage hematopoietic cells as well as a variety of cells from normal tissues.
22766194	1	8	from	cells	267:271	arg1	tissues					315:321	normal tissues	308:321	normal tissues	308:321	BACKGROUND: CD10, also known as neprilysin or enkephalinase exhibiting neutral endopeptidase (NEP) activity, is expressed by B-lineage hematopoietic cells as well as a variety of cells from normal tissues.
22766194	6	9	theme	N-glycans	1181:1189	arg1	part					1173:1176	only a small part	1160:1176	only a small part of N-glycans	1160:1189	Although neither desialylation nor further degalactosylation caused defective NEP activity, removal of only a small part of N-glycans by treatment with glycopeptidase F under non-denaturing conditions decreased NEP activity completely.
22766194	10	10	theme	Quality	1692:1698	arg1	system					1708:1713	GENERAL SIGNIFICANCE: Quality control system	1670:1713	GENERAL SIGNIFICANCE: Quality control system	1670:1713	GENERAL SIGNIFICANCE: Quality control system does not allow dysfunctional ecto-type proteases to express on plasma membrane.
22766194	4	11	theme	sugar-altered	883:895	arg1	CD10					897:900	the sugar-altered CD10	879:900	the sugar-altered CD10	879:900	METHODS: In order to investigate the role of N-glycans in the full expression of NEP activity, we modified N-glycans by treatment of NALM6 cells with various glycosidases or alter each of the consensus N-glycosylation sites by generating site-directed mutagenesis and compared the NEP activities of the sugar-altered CD10 with those of intact CD10.
22766194	6	12	theme	non-denaturing	1232:1245	arg1	conditions					1247:1256	non-denaturing conditions	1232:1256	non-denaturing conditions	1232:1256	Although neither desialylation nor further degalactosylation caused defective NEP activity, removal of only a small part of N-glycans by treatment with glycopeptidase F under non-denaturing conditions decreased NEP activity completely.
22766194	3	13	theme	line	457:460	arg1	molecules					423:431	CD10 molecules	418:431	CD10 molecules of the human pre-B-cell line NALM-6	418:467	Although CD10 molecules of the human pre-B-cell line NALM-6 have 6 consensus N-glycosylation sites, three of them are known to be N-glycosylated by X-ray crystallography.
22766194	4	14	from	role	617:620	arg1	expression					647:656	the full expression	638:656	the full expression of NEP activity	638:672	METHODS: In order to investigate the role of N-glycans in the full expression of NEP activity, we modified N-glycans by treatment of NALM6 cells with various glycosidases or alter each of the consensus N-glycosylation sites by generating site-directed mutagenesis and compared the NEP activities of the sugar-altered CD10 with those of intact CD10.
22766194	1	15	theme	normal	308:313	arg1	tissues					315:321	normal tissues	308:321	normal tissues	308:321	BACKGROUND: CD10, also known as neprilysin or enkephalinase exhibiting neutral endopeptidase (NEP) activity, is expressed by B-lineage hematopoietic cells as well as a variety of cells from normal tissues.
22766194	3	16	theme	consensus	476:484	arg1	sites					502:506	6 consensus N-glycosylation sites	474:506	6 consensus N-glycosylation sites	474:506	Although CD10 molecules of the human pre-B-cell line NALM-6 have 6 consensus N-glycosylation sites, three of them are known to be N-glycosylated by X-ray crystallography.
22766194	6	17	theme	small	1167:1171	arg1	part					1173:1176	only a small part	1160:1176	only a small part of N-glycans	1160:1189	Although neither desialylation nor further degalactosylation caused defective NEP activity, removal of only a small part of N-glycans by treatment with glycopeptidase F under non-denaturing conditions decreased NEP activity completely.
22766194	0	18	theme	surface	63:69	arg1	expression					71:80	surface expression	63:80	surface expression	63:80	The human CD10 lacking an N-glycan at Asn(628) is deficient in surface expression and neutral endopeptidase activity.
22766194	7	19	gly	N-glycosylated	1402:1415	arg1	CD10					1329:1332	CD10	1329:1332	CD10	1329:1332	All of the three consensus sites of CD10 in HEK293 cells introduced with wild type-CD10 were confirmed to be N-glycosylated.
22766194	7	19	gly	N-glycosylated	1402:1415	arg1	sites					1320:1324	the three consensus sites	1300:1324	the three consensus sites of CD10 in HEK293 cells introduced with wild type-CD10	1300:1379	All of the three consensus sites of CD10 in HEK293 cells introduced with wild type-CD10 were confirmed to be N-glycosylated.
22766194	7	19	gly	N-glycosylated	1402:1415	arg1	All					1293:1295	All	1293:1295	All	1293:1295	All of the three consensus sites of CD10 in HEK293 cells introduced with wild type-CD10 were confirmed to be N-glycosylated.
22766194	3	20	theme	N-glycosylation	486:500	arg1	sites					502:506	6 consensus N-glycosylation sites	474:506	6 consensus N-glycosylation sites	474:506	Although CD10 molecules of the human pre-B-cell line NALM-6 have 6 consensus N-glycosylation sites, three of them are known to be N-glycosylated by X-ray crystallography.
22766194	7	21	theme	consensus	1310:1318	arg1	CD10					1329:1332	CD10	1329:1332	CD10	1329:1332	All of the three consensus sites of CD10 in HEK293 cells introduced with wild type-CD10 were confirmed to be N-glycosylated.
22766194	7	21	theme	consensus	1310:1318	arg1	sites					1320:1324	the three consensus sites	1300:1324	the three consensus sites of CD10 in HEK293 cells introduced with wild type-CD10	1300:1379	All of the three consensus sites of CD10 in HEK293 cells introduced with wild type-CD10 were confirmed to be N-glycosylated.
22766194	0	22	theme	human	4:8	arg1	CD10					10:13	The human CD10	0:13	The human CD10 lacking an N-glycan at Asn(628)	0:45	The human CD10 lacking an N-glycan at Asn(628) is deficient in surface expression and neutral endopeptidase activity.
22766194	0	22	theme	human	4:8	arg1	deficient					50:58	deficient	50:58	deficient	50:58	The human CD10 lacking an N-glycan at Asn(628) is deficient in surface expression and neutral endopeptidase activity.
22766194	6	23	theme	NEP	1135:1137	arg1	activity					1139:1146	defective NEP activity	1125:1146	defective NEP activity	1125:1146	Although neither desialylation nor further degalactosylation caused defective NEP activity, removal of only a small part of N-glycans by treatment with glycopeptidase F under non-denaturing conditions decreased NEP activity completely.
22766194	4	24	theme	N-glycosylation	782:796	arg1	sites					798:802	the consensus N-glycosylation sites	768:802	the consensus N-glycosylation sites	768:802	METHODS: In order to investigate the role of N-glycans in the full expression of NEP activity, we modified N-glycans by treatment of NALM6 cells with various glycosidases or alter each of the consensus N-glycosylation sites by generating site-directed mutagenesis and compared the NEP activities of the sugar-altered CD10 with those of intact CD10.
22766194	3	25	theme	them	518:521	arg1	them					518:521	them	518:521	them	518:521	Although CD10 molecules of the human pre-B-cell line NALM-6 have 6 consensus N-glycosylation sites, three of them are known to be N-glycosylated by X-ray crystallography.
22766194	3	25	theme	them	518:521	arg1	three					509:513	three	509:513	three	509:513	Although CD10 molecules of the human pre-B-cell line NALM-6 have 6 consensus N-glycosylation sites, three of them are known to be N-glycosylated by X-ray crystallography.
22766194	8	26	theme	HEK293	1477:1482	arg1	cells					1484:1488	HEK293 cells	1477:1488	HEK293 cells	1477:1488	Surface expression of N-glycan at Asn(628)-deleted CD10 by HEK293 cells was greatly decreased as well as it lost entire NEP activities.
22766194	10	27	theme	SIGNIFICANCE	1678:1689	arg1	system					1708:1713	GENERAL SIGNIFICANCE: Quality control system	1670:1713	GENERAL SIGNIFICANCE: Quality control system	1670:1713	GENERAL SIGNIFICANCE: Quality control system does not allow dysfunctional ecto-type proteases to express on plasma membrane.
22766194	2	28	theme	inflammatory	385:396	arg1	responses					398:406	inflammatory responses	385:406	inflammatory responses	385:406	It cleaves peptides such as cytokines to act for terminating inflammatory responses.
22766194	10	29	theme	dysfunctional	1730:1742	arg1	proteases					1754:1762	dysfunctional ecto-type proteases	1730:1762	dysfunctional ecto-type proteases	1730:1762	GENERAL SIGNIFICANCE: Quality control system does not allow dysfunctional ecto-type proteases to express on plasma membrane.
22766194	4	30	theme	consensus	772:780	arg1	sites					798:802	the consensus N-glycosylation sites	768:802	the consensus N-glycosylation sites	768:802	METHODS: In order to investigate the role of N-glycans in the full expression of NEP activity, we modified N-glycans by treatment of NALM6 cells with various glycosidases or alter each of the consensus N-glycosylation sites by generating site-directed mutagenesis and compared the NEP activities of the sugar-altered CD10 with those of intact CD10.
22766194	4	31	theme	activity	665:672	arg1	expression					647:656	the full expression	638:656	the full expression of NEP activity	638:672	METHODS: In order to investigate the role of N-glycans in the full expression of NEP activity, we modified N-glycans by treatment of NALM6 cells with various glycosidases or alter each of the consensus N-glycosylation sites by generating site-directed mutagenesis and compared the NEP activities of the sugar-altered CD10 with those of intact CD10.
22766194	8	32	theme	Surface	1418:1424	arg1	expression					1426:1435	Surface expression	1418:1435	Surface expression of N-glycan at Asn(628)-deleted CD10 by HEK293 cells	1418:1488	Surface expression of N-glycan at Asn(628)-deleted CD10 by HEK293 cells was greatly decreased as well as it lost entire NEP activities.
22766194	7	33	theme	HEK293	1337:1342	arg1	cells					1344:1348	HEK293 cells	1337:1348	HEK293 cells introduced with wild type-CD10	1337:1379	All of the three consensus sites of CD10 in HEK293 cells introduced with wild type-CD10 were confirmed to be N-glycosylated.
22766194	4	34	with	treatment	700:708	arg1	glycosidases					738:749	various glycosidases	730:749	various glycosidases	730:749	METHODS: In order to investigate the role of N-glycans in the full expression of NEP activity, we modified N-glycans by treatment of NALM6 cells with various glycosidases or alter each of the consensus N-glycosylation sites by generating site-directed mutagenesis and compared the NEP activities of the sugar-altered CD10 with those of intact CD10.
22766194	0	35	theme	neutral	86:92	arg1	activity					108:115	neutral endopeptidase activity	86:115	neutral endopeptidase activity	86:115	The human CD10 lacking an N-glycan at Asn(628) is deficient in surface expression and neutral endopeptidase activity.
22766194	3	36	contain	have	469:472	arg2	sites					502:506	6 consensus N-glycosylation sites	474:506	6 consensus N-glycosylation sites	474:506	Although CD10 molecules of the human pre-B-cell line NALM-6 have 6 consensus N-glycosylation sites, three of them are known to be N-glycosylated by X-ray crystallography.
22766194	3	36	contain	have	469:472	arg1	molecules					423:431	CD10 molecules	418:431	CD10 molecules of the human pre-B-cell line NALM-6	418:467	Although CD10 molecules of the human pre-B-cell line NALM-6 have 6 consensus N-glycosylation sites, three of them are known to be N-glycosylated by X-ray crystallography.
22766194	3	37	gly	N-glycosylated	539:552	arg1	them					518:521	them	518:521	them	518:521	Although CD10 molecules of the human pre-B-cell line NALM-6 have 6 consensus N-glycosylation sites, three of them are known to be N-glycosylated by X-ray crystallography.
22766194	3	37	gly	N-glycosylated	539:552	arg1	three					509:513	three	509:513	three	509:513	Although CD10 molecules of the human pre-B-cell line NALM-6 have 6 consensus N-glycosylation sites, three of them are known to be N-glycosylated by X-ray crystallography.
22766194	6	38	theme	defective	1125:1133	arg1	activity					1139:1146	defective NEP activity	1125:1146	defective NEP activity	1125:1146	Although neither desialylation nor further degalactosylation caused defective NEP activity, removal of only a small part of N-glycans by treatment with glycopeptidase F under non-denaturing conditions decreased NEP activity completely.
22766194	1	39	theme	B-lineage	243:251	arg1	cells					267:271	B-lineage hematopoietic cells	243:271	B-lineage hematopoietic cells as well as a variety of cells from normal tissues	243:321	BACKGROUND: CD10, also known as neprilysin or enkephalinase exhibiting neutral endopeptidase (NEP) activity, is expressed by B-lineage hematopoietic cells as well as a variety of cells from normal tissues.
22766194	4	40	theme	NEP	861:863	arg1	activities					865:874	the NEP activities	857:874	the NEP activities of the sugar-altered CD10	857:900	METHODS: In order to investigate the role of N-glycans in the full expression of NEP activity, we modified N-glycans by treatment of NALM6 cells with various glycosidases or alter each of the consensus N-glycosylation sites by generating site-directed mutagenesis and compared the NEP activities of the sugar-altered CD10 with those of intact CD10.
22766194	10	41	theme	control	1700:1706	arg1	system					1708:1713	GENERAL SIGNIFICANCE: Quality control system	1670:1713	GENERAL SIGNIFICANCE: Quality control system	1670:1713	GENERAL SIGNIFICANCE: Quality control system does not allow dysfunctional ecto-type proteases to express on plasma membrane.
22766194	1	42	theme	hematopoietic	253:265	arg1	cells					267:271	B-lineage hematopoietic cells	243:271	B-lineage hematopoietic cells as well as a variety of cells from normal tissues	243:321	BACKGROUND: CD10, also known as neprilysin or enkephalinase exhibiting neutral endopeptidase (NEP) activity, is expressed by B-lineage hematopoietic cells as well as a variety of cells from normal tissues.
22766194	9	43	theme	NEP	1621:1623	arg1	activities					1625:1634	NEP activities	1621:1634	NEP activities	1621:1634	CONCLUSIONS: N-glycosylation at Asn(628) is essential not only for NEP activities, but also for surface expression.
22766194	5	44	theme	raft	1003:1006	arg1	microdomains					1008:1019	raft microdomains	1003:1019	raft microdomains	1003:1019	RESULTS: CD10 of the human B-cell line NALM-6 was dominantly localized in raft microdomains and heterogeneously N-glycosylated.
22766194	5	45	located	localized	990:998	arg1	microdomains					1008:1019	raft microdomains	1003:1019	raft microdomains	1003:1019	RESULTS: CD10 of the human B-cell line NALM-6 was dominantly localized in raft microdomains and heterogeneously N-glycosylated.
22766194	5	45	located	localized	990:998	arg2	CD10					938:941	CD10	938:941	CD10 of the human B-cell line NALM-6	938:973	RESULTS: CD10 of the human B-cell line NALM-6 was dominantly localized in raft microdomains and heterogeneously N-glycosylated.
22766194	0	46	theme	endopeptidase	94:106	arg1	activity					108:115	neutral endopeptidase activity	86:115	neutral endopeptidase activity	86:115	The human CD10 lacking an N-glycan at Asn(628) is deficient in surface expression and neutral endopeptidase activity.
22766194	4	47	theme	full	642:645	arg1	expression					647:656	the full expression	638:656	the full expression of NEP activity	638:672	METHODS: In order to investigate the role of N-glycans in the full expression of NEP activity, we modified N-glycans by treatment of NALM6 cells with various glycosidases or alter each of the consensus N-glycosylation sites by generating site-directed mutagenesis and compared the NEP activities of the sugar-altered CD10 with those of intact CD10.
22766194	5	48	theme	human	950:954	arg1	line					963:966	the human B-cell line NALM-6	946:973	the human B-cell line NALM-6	946:973	RESULTS: CD10 of the human B-cell line NALM-6 was dominantly localized in raft microdomains and heterogeneously N-glycosylated.
22766194	4	49	gly	N-glycosylation	782:796	arg2	sites					798:802	the consensus N-glycosylation sites	768:802	the consensus N-glycosylation sites	768:802	METHODS: In order to investigate the role of N-glycans in the full expression of NEP activity, we modified N-glycans by treatment of NALM6 cells with various glycosidases or alter each of the consensus N-glycosylation sites by generating site-directed mutagenesis and compared the NEP activities of the sugar-altered CD10 with those of intact CD10.
22766194	8	50	theme	Asn	1452:1454	arg1	CD10					1469:1472	Asn(628)-deleted CD10	1452:1472	Asn(628)-deleted CD10 by HEK293 cells	1452:1488	Surface expression of N-glycan at Asn(628)-deleted CD10 by HEK293 cells was greatly decreased as well as it lost entire NEP activities.
22766194	8	51	theme	N-glycan	1440:1447	arg1	expression					1426:1435	Surface expression	1418:1435	Surface expression of N-glycan at Asn(628)-deleted CD10 by HEK293 cells	1418:1488	Surface expression of N-glycan at Asn(628)-deleted CD10 by HEK293 cells was greatly decreased as well as it lost entire NEP activities.
22766194	4	52	theme	site-directed	818:830	arg1	mutagenesis					832:842	site-directed mutagenesis	818:842	site-directed mutagenesis	818:842	METHODS: In order to investigate the role of N-glycans in the full expression of NEP activity, we modified N-glycans by treatment of NALM6 cells with various glycosidases or alter each of the consensus N-glycosylation sites by generating site-directed mutagenesis and compared the NEP activities of the sugar-altered CD10 with those of intact CD10.
22766194	5	53	theme	B-cell	956:961	arg1	line					963:966	the human B-cell line NALM-6	946:973	the human B-cell line NALM-6	946:973	RESULTS: CD10 of the human B-cell line NALM-6 was dominantly localized in raft microdomains and heterogeneously N-glycosylated.
22766194	8	54	from	CD10	1469:1472	arg1	expression					1426:1435	Surface expression	1418:1435	Surface expression of N-glycan at Asn(628)-deleted CD10 by HEK293 cells	1418:1488	Surface expression of N-glycan at Asn(628)-deleted CD10 by HEK293 cells was greatly decreased as well as it lost entire NEP activities.
22766194	3	55	theme	human	440:444	arg1	line					457:460	the human pre-B-cell line NALM-6	436:467	the human pre-B-cell line NALM-6	436:467	Although CD10 molecules of the human pre-B-cell line NALM-6 have 6 consensus N-glycosylation sites, three of them are known to be N-glycosylated by X-ray crystallography.
22766194	1	56	from	variety	286:292	arg1	tissues					315:321	normal tissues	308:321	normal tissues	308:321	BACKGROUND: CD10, also known as neprilysin or enkephalinase exhibiting neutral endopeptidase (NEP) activity, is expressed by B-lineage hematopoietic cells as well as a variety of cells from normal tissues.
22766194	8	57	theme	NEP	1538:1540	arg1	activities					1542:1551	entire NEP activities	1531:1551	entire NEP activities	1531:1551	Surface expression of N-glycan at Asn(628)-deleted CD10 by HEK293 cells was greatly decreased as well as it lost entire NEP activities.
22766194	8	58	theme	-deleted	1460:1467	arg1	CD10					1469:1472	Asn(628)-deleted CD10	1452:1472	Asn(628)-deleted CD10 by HEK293 cells	1452:1488	Surface expression of N-glycan at Asn(628)-deleted CD10 by HEK293 cells was greatly decreased as well as it lost entire NEP activities.
22766194	0	59	from	expression	71:80	arg1	CD10					10:13	The human CD10	0:13	The human CD10 lacking an N-glycan at Asn(628)	0:45	The human CD10 lacking an N-glycan at Asn(628) is deficient in surface expression and neutral endopeptidase activity.
22766194	0	59	from	expression	71:80	arg1	deficient					50:58	deficient	50:58	deficient	50:58	The human CD10 lacking an N-glycan at Asn(628) is deficient in surface expression and neutral endopeptidase activity.
22766194	5	60	theme	line	963:966	arg1	CD10					938:941	CD10	938:941	CD10 of the human B-cell line NALM-6	938:973	RESULTS: CD10 of the human B-cell line NALM-6 was dominantly localized in raft microdomains and heterogeneously N-glycosylated.
22766194	3	61	theme	pre-B-cell	446:455	arg1	line					457:460	the human pre-B-cell line NALM-6	436:467	the human pre-B-cell line NALM-6	436:467	Although CD10 molecules of the human pre-B-cell line NALM-6 have 6 consensus N-glycosylation sites, three of them are known to be N-glycosylated by X-ray crystallography.
22766194	8	62	theme	entire	1531:1536	arg1	activities					1542:1551	entire NEP activities	1531:1551	entire NEP activities	1531:1551	Surface expression of N-glycan at Asn(628)-deleted CD10 by HEK293 cells was greatly decreased as well as it lost entire NEP activities.
22766194	9	63	theme	surface	1650:1656	arg1	expression					1658:1667	surface expression	1650:1667	surface expression	1650:1667	CONCLUSIONS: N-glycosylation at Asn(628) is essential not only for NEP activities, but also for surface expression.
22766194	6	64	theme	part	1173:1176	arg1	removal					1149:1155	removal	1149:1155	removal of only a small part of N-glycans by treatment with glycopeptidase F under non-denaturing conditions	1149:1256	Although neither desialylation nor further degalactosylation caused defective NEP activity, removal of only a small part of N-glycans by treatment with glycopeptidase F under non-denaturing conditions decreased NEP activity completely.
22766194	4	65	theme	cells	719:723	arg1	treatment					700:708	treatment	700:708	treatment of NALM6 cells with various glycosidases	700:749	METHODS: In order to investigate the role of N-glycans in the full expression of NEP activity, we modified N-glycans by treatment of NALM6 cells with various glycosidases or alter each of the consensus N-glycosylation sites by generating site-directed mutagenesis and compared the NEP activities of the sugar-altered CD10 with those of intact CD10.
22766194	10	66	theme	ecto-type	1744:1752	arg1	proteases					1754:1762	dysfunctional ecto-type proteases	1730:1762	dysfunctional ecto-type proteases	1730:1762	GENERAL SIGNIFICANCE: Quality control system does not allow dysfunctional ecto-type proteases to express on plasma membrane.
22766194	4	67	theme	NEP	661:663	arg1	activity					665:672	NEP activity	661:672	NEP activity	661:672	METHODS: In order to investigate the role of N-glycans in the full expression of NEP activity, we modified N-glycans by treatment of NALM6 cells with various glycosidases or alter each of the consensus N-glycosylation sites by generating site-directed mutagenesis and compared the NEP activities of the sugar-altered CD10 with those of intact CD10.
22766194	7	68	theme	wild	1366:1369	arg1	type-CD10					1371:1379	wild type-CD10	1366:1379	wild type-CD10	1366:1379	All of the three consensus sites of CD10 in HEK293 cells introduced with wild type-CD10 were confirmed to be N-glycosylated.
22766194	0	69	from	activity	108:115	arg1	CD10					10:13	The human CD10	0:13	The human CD10 lacking an N-glycan at Asn(628)	0:45	The human CD10 lacking an N-glycan at Asn(628) is deficient in surface expression and neutral endopeptidase activity.
22766194	0	69	from	activity	108:115	arg1	deficient					50:58	deficient	50:58	deficient	50:58	The human CD10 lacking an N-glycan at Asn(628) is deficient in surface expression and neutral endopeptidase activity.
22766194	10	70	theme	GENERAL	1670:1676	arg1	system					1708:1713	GENERAL SIGNIFICANCE: Quality control system	1670:1713	GENERAL SIGNIFICANCE: Quality control system	1670:1713	GENERAL SIGNIFICANCE: Quality control system does not allow dysfunctional ecto-type proteases to express on plasma membrane.
22766194	4	71	theme	NALM6	713:717	arg1	cells					719:723	NALM6 cells	713:723	NALM6 cells	713:723	METHODS: In order to investigate the role of N-glycans in the full expression of NEP activity, we modified N-glycans by treatment of NALM6 cells with various glycosidases or alter each of the consensus N-glycosylation sites by generating site-directed mutagenesis and compared the NEP activities of the sugar-altered CD10 with those of intact CD10.
22766194	9	72	from	Asn	1586:1588	arg1	N-glycosylation					1567:1581	N-glycosylation	1567:1581	N-glycosylation at Asn(628)	1567:1593	CONCLUSIONS: N-glycosylation at Asn(628) is essential not only for NEP activities, but also for surface expression.
22766194	6	73	theme	further	1092:1098	arg1	degalactosylation					1100:1116	further degalactosylation	1092:1116	further degalactosylation	1092:1116	Although neither desialylation nor further degalactosylation caused defective NEP activity, removal of only a small part of N-glycans by treatment with glycopeptidase F under non-denaturing conditions decreased NEP activity completely.
22766194	1	74	theme	endopeptidase	197:209	arg1	activity					217:224	neutral endopeptidase (NEP) activity	189:224	neutral endopeptidase (NEP) activity	189:224	BACKGROUND: CD10, also known as neprilysin or enkephalinase exhibiting neutral endopeptidase (NEP) activity, is expressed by B-lineage hematopoietic cells as well as a variety of cells from normal tissues.
22766194	4	75	theme	intact	916:921	arg1	CD10					923:926	intact CD10	916:926	intact CD10	916:926	METHODS: In order to investigate the role of N-glycans in the full expression of NEP activity, we modified N-glycans by treatment of NALM6 cells with various glycosidases or alter each of the consensus N-glycosylation sites by generating site-directed mutagenesis and compared the NEP activities of the sugar-altered CD10 with those of intact CD10.
22766194	0	76	from	deficient	50:58	arg1	activity					108:115	neutral endopeptidase activity	86:115	neutral endopeptidase activity	86:115	The human CD10 lacking an N-glycan at Asn(628) is deficient in surface expression and neutral endopeptidase activity.
22766194	0	76	from	deficient	50:58	arg1	expression					71:80	surface expression	63:80	surface expression	63:80	The human CD10 lacking an N-glycan at Asn(628) is deficient in surface expression and neutral endopeptidase activity.
22766194	4	77	theme	various	730:736	arg1	glycosidases					738:749	various glycosidases	730:749	various glycosidases	730:749	METHODS: In order to investigate the role of N-glycans in the full expression of NEP activity, we modified N-glycans by treatment of NALM6 cells with various glycosidases or alter each of the consensus N-glycosylation sites by generating site-directed mutagenesis and compared the NEP activities of the sugar-altered CD10 with those of intact CD10.
22766194	3	78	theme	CD10	418:421	arg1	molecules					423:431	CD10 molecules	418:431	CD10 molecules of the human pre-B-cell line NALM-6	418:467	Although CD10 molecules of the human pre-B-cell line NALM-6 have 6 consensus N-glycosylation sites, three of them are known to be N-glycosylated by X-ray crystallography.
22766194	4	79	theme	N-glycans	625:633	arg1	role					617:620	the role	613:620	the role of N-glycans in the full expression of NEP activity	613:672	METHODS: In order to investigate the role of N-glycans in the full expression of NEP activity, we modified N-glycans by treatment of NALM6 cells with various glycosidases or alter each of the consensus N-glycosylation sites by generating site-directed mutagenesis and compared the NEP activities of the sugar-altered CD10 with those of intact CD10.
22766194	6	80	with	treatment	1194:1202	arg1	F					1224:1224	glycopeptidase F	1209:1224	glycopeptidase F under non-denaturing conditions	1209:1256	Although neither desialylation nor further degalactosylation caused defective NEP activity, removal of only a small part of N-glycans by treatment with glycopeptidase F under non-denaturing conditions decreased NEP activity completely.
22766194	7	81	theme	CD10	1329:1332	arg1	CD10					1329:1332	CD10	1329:1332	CD10	1329:1332	All of the three consensus sites of CD10 in HEK293 cells introduced with wild type-CD10 were confirmed to be N-glycosylated.
22766194	7	81	theme	CD10	1329:1332	arg1	sites					1320:1324	the three consensus sites	1300:1324	the three consensus sites of CD10 in HEK293 cells introduced with wild type-CD10	1300:1379	All of the three consensus sites of CD10 in HEK293 cells introduced with wild type-CD10 were confirmed to be N-glycosylated.
22766194	3	82	theme	X-ray	557:561	arg1	crystallography					563:577	X-ray crystallography	557:577	X-ray crystallography	557:577	Although CD10 molecules of the human pre-B-cell line NALM-6 have 6 consensus N-glycosylation sites, three of them are known to be N-glycosylated by X-ray crystallography.
22766194	1	83	theme	neutral	189:195	arg1	NEP					212:214	NEP	212:214	NEP	212:214	BACKGROUND: CD10, also known as neprilysin or enkephalinase exhibiting neutral endopeptidase (NEP) activity, is expressed by B-lineage hematopoietic cells as well as a variety of cells from normal tissues.
22766194	1	83	theme	neutral	189:195	arg1	endopeptidase					197:209	neutral endopeptidase	189:209	neutral endopeptidase (NEP) activity	189:224	BACKGROUND: CD10, also known as neprilysin or enkephalinase exhibiting neutral endopeptidase (NEP) activity, is expressed by B-lineage hematopoietic cells as well as a variety of cells from normal tissues.
22766194	1	84	from	tissues	315:321	arg1	cells					297:301	cells	297:301	cells from normal tissues	297:321	BACKGROUND: CD10, also known as neprilysin or enkephalinase exhibiting neutral endopeptidase (NEP) activity, is expressed by B-lineage hematopoietic cells as well as a variety of cells from normal tissues.
22766194	1	84	from	tissues	315:321	arg1	variety					286:292	a variety	284:292	B-lineage hematopoietic cells as well as a variety of cells from normal tissues	243:321	BACKGROUND: CD10, also known as neprilysin or enkephalinase exhibiting neutral endopeptidase (NEP) activity, is expressed by B-lineage hematopoietic cells as well as a variety of cells from normal tissues.
22766194	1	84	from	tissues	315:321	arg1	cells					267:271	B-lineage hematopoietic cells	243:271	B-lineage hematopoietic cells as well as a variety of cells from normal tissues	243:321	BACKGROUND: CD10, also known as neprilysin or enkephalinase exhibiting neutral endopeptidase (NEP) activity, is expressed by B-lineage hematopoietic cells as well as a variety of cells from normal tissues.
29941599	0	0	theme	EZH2	96:99	arg1	stability					30:38	stability	30:38	stability	30:38	O-GlcNAcylation regulates the stability and enzymatic activity of the histone methyltransferase EZH2.
29941599	0	0	theme	EZH2	96:99	arg1	activity					54:61	enzymatic activity	44:61	enzymatic activity	44:61	O-GlcNAcylation regulates the stability and enzymatic activity of the histone methyltransferase EZH2.
29941599	1	1	attach	attachment	129:138	arg1	Thr					188:190	Thr	188:190	Thr	188:190	Protein O-glycosylation by attachment of β-N-acetylglucosamine (GlcNAc) to the Ser or Thr residue is a major posttranslational glycosylation event and is often associated with protein folding, stability, and activity.
29941599	1	1	attach	attachment	129:138	arg1	Ser					181:183	Ser	181:183	Ser	181:183	Protein O-glycosylation by attachment of β-N-acetylglucosamine (GlcNAc) to the Ser or Thr residue is a major posttranslational glycosylation event and is often associated with protein folding, stability, and activity.
29941599	1	1	attach	attachment	129:138	arg2	GlcNAc					166:171	GlcNAc	166:171	GlcNAc	166:171	Protein O-glycosylation by attachment of β-N-acetylglucosamine (GlcNAc) to the Ser or Thr residue is a major posttranslational glycosylation event and is often associated with protein folding, stability, and activity.
29941599	1	1	attach	attachment	129:138	arg2	β-N-acetylglucosamine					143:163	β-N-acetylglucosamine	143:163	β-N-acetylglucosamine (GlcNAc)	143:172	Protein O-glycosylation by attachment of β-N-acetylglucosamine (GlcNAc) to the Ser or Thr residue is a major posttranslational glycosylation event and is often associated with protein folding, stability, and activity.
29941599	0	2	theme	methyltransferase	78:94	arg1	EZH2					96:99	the histone methyltransferase EZH2	66:99	the histone methyltransferase EZH2	66:99	O-GlcNAcylation regulates the stability and enzymatic activity of the histone methyltransferase EZH2.
29941599	3	3	theme	labeling	681:688	arg1	method					665:670	a fluorescence-based method	644:670	a fluorescence-based method of sugar labeling combined with mass spectrometry	644:720	In this study, we employed a fluorescence-based method of sugar labeling combined with mass spectrometry to investigate EZH2 glycosylation and identified five O-GlcNAcylation sites.
29941599	2	4	theme	tumor	598:602	arg1	suppression					604:614	tumor suppression	598:614	tumor suppression	598:614	The methylation of histone H3 at Lys-27 catalyzed by the methyltransferase EZH2 was known to suppress gene expression and cancer development, and we previously reported that the O-GlcNAcylation of EZH2 at S76 stabilized EZH2 and facilitated the formation of H3K27me3 to inhibit tumor suppression.
29941599	5	5	from	Mutation	1032:1039	arg1	EZH2					1115:1118	EZH2	1115:1118	EZH2	1115:1118	Mutation of the C-terminal O-GlcNAcylation site (S729A) in the catalytic domain of EZH2 abolishes the di- and trimethylation activities, but not the monomethylation of H3K27, nor the integrity of the PRC2/EZH2 core complex.
29941599	5	5	from	Mutation	1032:1039	arg1	domain					1105:1110	the catalytic domain	1091:1110	the catalytic domain of EZH2	1091:1118	Mutation of the C-terminal O-GlcNAcylation site (S729A) in the catalytic domain of EZH2 abolishes the di- and trimethylation activities, but not the monomethylation of H3K27, nor the integrity of the PRC2/EZH2 core complex.
29941599	6	6	theme	selective	1409:1417	arg1	inhibition					1419:1428	selective inhibition	1409:1428	selective inhibition of EZH2 O-GlcNAcylation	1409:1452	Our results show the effect of individual O-GlcNAcylation sites on the function of EZH2 and suggest an alternative approach to tumor suppression through selective inhibition of EZH2 O-GlcNAcylation.
29941599	5	7	theme	catalytic	1095:1103	arg1	EZH2					1115:1118	EZH2	1115:1118	EZH2	1115:1118	Mutation of the C-terminal O-GlcNAcylation site (S729A) in the catalytic domain of EZH2 abolishes the di- and trimethylation activities, but not the monomethylation of H3K27, nor the integrity of the PRC2/EZH2 core complex.
29941599	5	7	theme	catalytic	1095:1103	arg1	domain					1105:1110	the catalytic domain	1091:1110	the catalytic domain of EZH2	1091:1118	Mutation of the C-terminal O-GlcNAcylation site (S729A) in the catalytic domain of EZH2 abolishes the di- and trimethylation activities, but not the monomethylation of H3K27, nor the integrity of the PRC2/EZH2 core complex.
29941599	4	8	theme	more	836:839	arg1	mutation					817:824	mutation	817:824	mutation of one or more of the O-GlcNAcylation sites S73A, S76A, S84A, and T313A in the N-terminal region	817:921	We also find that mutation of one or more of the O-GlcNAcylation sites S73A, S76A, S84A, and T313A in the N-terminal region decreases the stability of EZH2, but does not affect its association with the PRC2 components SUZ12 and EED.
29941599	6	9	theme	sites	1314:1318	arg1	effect					1277:1282	the effect	1273:1282	the effect of individual O-GlcNAcylation sites on the function of EZH2	1273:1342	Our results show the effect of individual O-GlcNAcylation sites on the function of EZH2 and suggest an alternative approach to tumor suppression through selective inhibition of EZH2 O-GlcNAcylation.
29941599	5	10	theme	O-GlcNAcylation	1059:1073	arg1	S729A					1081:1085	S729A	1081:1085	S729A	1081:1085	Mutation of the C-terminal O-GlcNAcylation site (S729A) in the catalytic domain of EZH2 abolishes the di- and trimethylation activities, but not the monomethylation of H3K27, nor the integrity of the PRC2/EZH2 core complex.
29941599	5	10	theme	O-GlcNAcylation	1059:1073	arg1	site					1075:1078	the C-terminal O-GlcNAcylation site	1044:1078	the C-terminal O-GlcNAcylation site (S729A)	1044:1086	Mutation of the C-terminal O-GlcNAcylation site (S729A) in the catalytic domain of EZH2 abolishes the di- and trimethylation activities, but not the monomethylation of H3K27, nor the integrity of the PRC2/EZH2 core complex.
29941599	1	11	theme	protein	278:284	arg1	folding					286:292	protein folding	278:292	protein folding	278:292	Protein O-glycosylation by attachment of β-N-acetylglucosamine (GlcNAc) to the Ser or Thr residue is a major posttranslational glycosylation event and is often associated with protein folding, stability, and activity.
29941599	2	12	theme	EZH2	517:520	arg1	O-GlcNAcylation					498:512	the O-GlcNAcylation	494:512	the O-GlcNAcylation of EZH2 at S76	494:527	The methylation of histone H3 at Lys-27 catalyzed by the methyltransferase EZH2 was known to suppress gene expression and cancer development, and we previously reported that the O-GlcNAcylation of EZH2 at S76 stabilized EZH2 and facilitated the formation of H3K27me3 to inhibit tumor suppression.
29941599	3	13	theme	EZH2	737:740	arg1	glycosylation					742:754	EZH2 glycosylation	737:754	EZH2 glycosylation	737:754	In this study, we employed a fluorescence-based method of sugar labeling combined with mass spectrometry to investigate EZH2 glycosylation and identified five O-GlcNAcylation sites.
29941599	4	14	dep	components	1006:1015	arg1	EED					1027:1029	EED	1027:1029	EED	1027:1029	We also find that mutation of one or more of the O-GlcNAcylation sites S73A, S76A, S84A, and T313A in the N-terminal region decreases the stability of EZH2, but does not affect its association with the PRC2 components SUZ12 and EED.
29941599	4	14	dep	components	1006:1015	arg1	SUZ12					1017:1021	SUZ12	1017:1021	SUZ12	1017:1021	We also find that mutation of one or more of the O-GlcNAcylation sites S73A, S76A, S84A, and T313A in the N-terminal region decreases the stability of EZH2, but does not affect its association with the PRC2 components SUZ12 and EED.
29941599	4	14	dep	components	1006:1015	arg1	components					1006:1015	the PRC2 components SUZ12 and EED	997:1029	the PRC2 components SUZ12 and EED	997:1029	We also find that mutation of one or more of the O-GlcNAcylation sites S73A, S76A, S84A, and T313A in the N-terminal region decreases the stability of EZH2, but does not affect its association with the PRC2 components SUZ12 and EED.
29941599	6	15	theme	O-GlcNAcylation	1438:1452	arg1	inhibition					1419:1428	selective inhibition	1409:1428	selective inhibition of EZH2 O-GlcNAcylation	1409:1452	Our results show the effect of individual O-GlcNAcylation sites on the function of EZH2 and suggest an alternative approach to tumor suppression through selective inhibition of EZH2 O-GlcNAcylation.
29941599	6	16	theme	individual	1287:1296	arg1	sites					1314:1318	individual O-GlcNAcylation sites	1287:1318	individual O-GlcNAcylation sites	1287:1318	Our results show the effect of individual O-GlcNAcylation sites on the function of EZH2 and suggest an alternative approach to tumor suppression through selective inhibition of EZH2 O-GlcNAcylation.
29941599	6	17	theme	O-GlcNAcylation	1298:1312	arg1	sites					1314:1318	individual O-GlcNAcylation sites	1287:1318	individual O-GlcNAcylation sites	1287:1318	Our results show the effect of individual O-GlcNAcylation sites on the function of EZH2 and suggest an alternative approach to tumor suppression through selective inhibition of EZH2 O-GlcNAcylation.
29941599	6	18	theme	alternative	1359:1369	arg1	approach					1371:1378	an alternative approach	1356:1378	an alternative approach to tumor suppression through selective inhibition of EZH2 O-GlcNAcylation	1356:1452	Our results show the effect of individual O-GlcNAcylation sites on the function of EZH2 and suggest an alternative approach to tumor suppression through selective inhibition of EZH2 O-GlcNAcylation.
29941599	2	19	from	Lys-27	353:358	arg1	methylation					324:334	The methylation	320:334	The methylation of histone H3 at Lys-27 catalyzed by the methyltransferase EZH2	320:398	The methylation of histone H3 at Lys-27 catalyzed by the methyltransferase EZH2 was known to suppress gene expression and cancer development, and we previously reported that the O-GlcNAcylation of EZH2 at S76 stabilized EZH2 and facilitated the formation of H3K27me3 to inhibit tumor suppression.
29941599	6	20	theme	tumor	1383:1387	arg1	suppression					1389:1399	tumor suppression	1383:1399	tumor suppression	1383:1399	Our results show the effect of individual O-GlcNAcylation sites on the function of EZH2 and suggest an alternative approach to tumor suppression through selective inhibition of EZH2 O-GlcNAcylation.
29941599	5	21	theme	EZH2	1115:1118	arg1	EZH2					1115:1118	EZH2	1115:1118	EZH2	1115:1118	Mutation of the C-terminal O-GlcNAcylation site (S729A) in the catalytic domain of EZH2 abolishes the di- and trimethylation activities, but not the monomethylation of H3K27, nor the integrity of the PRC2/EZH2 core complex.
29941599	5	21	theme	EZH2	1115:1118	arg1	domain					1105:1110	the catalytic domain	1091:1110	the catalytic domain of EZH2	1091:1118	Mutation of the C-terminal O-GlcNAcylation site (S729A) in the catalytic domain of EZH2 abolishes the di- and trimethylation activities, but not the monomethylation of H3K27, nor the integrity of the PRC2/EZH2 core complex.
29941599	4	22	dep	sites	864:868	arg1	S73A					870:873	S73A	870:873	the O-GlcNAcylation sites S73A	844:873	We also find that mutation of one or more of the O-GlcNAcylation sites S73A, S76A, S84A, and T313A in the N-terminal region decreases the stability of EZH2, but does not affect its association with the PRC2 components SUZ12 and EED.
29941599	6	23	from	effect	1277:1282	arg1	function					1327:1334	the function	1323:1334	the function of EZH2	1323:1342	Our results show the effect of individual O-GlcNAcylation sites on the function of EZH2 and suggest an alternative approach to tumor suppression through selective inhibition of EZH2 O-GlcNAcylation.
29941599	4	24	theme	sites	864:868	arg1	one					829:831	one	829:831	one	829:831	We also find that mutation of one or more of the O-GlcNAcylation sites S73A, S76A, S84A, and T313A in the N-terminal region decreases the stability of EZH2, but does not affect its association with the PRC2 components SUZ12 and EED.
29941599	4	24	theme	sites	864:868	arg1	S84A					882:885	S84A	882:885	S84A	882:885	We also find that mutation of one or more of the O-GlcNAcylation sites S73A, S76A, S84A, and T313A in the N-terminal region decreases the stability of EZH2, but does not affect its association with the PRC2 components SUZ12 and EED.
29941599	4	24	theme	sites	864:868	arg1	sites					864:868	the O-GlcNAcylation sites S73A	844:873	the O-GlcNAcylation sites S73A	844:873	We also find that mutation of one or more of the O-GlcNAcylation sites S73A, S76A, S84A, and T313A in the N-terminal region decreases the stability of EZH2, but does not affect its association with the PRC2 components SUZ12 and EED.
29941599	4	24	theme	sites	864:868	arg1	S76A					876:879	S76A	876:879	S76A	876:879	We also find that mutation of one or more of the O-GlcNAcylation sites S73A, S76A, S84A, and T313A in the N-terminal region decreases the stability of EZH2, but does not affect its association with the PRC2 components SUZ12 and EED.
29941599	4	24	theme	sites	864:868	arg1	T313A					892:896	T313A	892:896	T313A	892:896	We also find that mutation of one or more of the O-GlcNAcylation sites S73A, S76A, S84A, and T313A in the N-terminal region decreases the stability of EZH2, but does not affect its association with the PRC2 components SUZ12 and EED.
29941599	3	25	theme	fluorescence-based	646:663	arg1	method					665:670	a fluorescence-based method	644:670	a fluorescence-based method of sugar labeling combined with mass spectrometry	644:720	In this study, we employed a fluorescence-based method of sugar labeling combined with mass spectrometry to investigate EZH2 glycosylation and identified five O-GlcNAcylation sites.
29941599	5	26	theme	site	1075:1078	arg1	Mutation					1032:1039	Mutation	1032:1039	Mutation of the C-terminal O-GlcNAcylation site (S729A) in the catalytic domain of EZH2	1032:1118	Mutation of the C-terminal O-GlcNAcylation site (S729A) in the catalytic domain of EZH2 abolishes the di- and trimethylation activities, but not the monomethylation of H3K27, nor the integrity of the PRC2/EZH2 core complex.
29941599	2	27	theme	methyltransferase	377:393	arg1	EZH2					395:398	the methyltransferase EZH2	373:398	the methyltransferase EZH2	373:398	The methylation of histone H3 at Lys-27 catalyzed by the methyltransferase EZH2 was known to suppress gene expression and cancer development, and we previously reported that the O-GlcNAcylation of EZH2 at S76 stabilized EZH2 and facilitated the formation of H3K27me3 to inhibit tumor suppression.
29941599	2	28	theme	cancer	442:447	arg1	development					449:459	cancer development	442:459	cancer development	442:459	The methylation of histone H3 at Lys-27 catalyzed by the methyltransferase EZH2 was known to suppress gene expression and cancer development, and we previously reported that the O-GlcNAcylation of EZH2 at S76 stabilized EZH2 and facilitated the formation of H3K27me3 to inhibit tumor suppression.
29941599	4	29	theme	O-GlcNAcylation	848:862	arg1	sites					864:868	the O-GlcNAcylation sites S73A	844:873	the O-GlcNAcylation sites S73A	844:873	We also find that mutation of one or more of the O-GlcNAcylation sites S73A, S76A, S84A, and T313A in the N-terminal region decreases the stability of EZH2, but does not affect its association with the PRC2 components SUZ12 and EED.
29941599	1	30	theme	Protein	102:108	arg1	O-glycosylation					110:124	Protein O-glycosylation	102:124	Protein O-glycosylation by attachment of β-N-acetylglucosamine (GlcNAc) to the Ser or Thr residue	102:198	Protein O-glycosylation by attachment of β-N-acetylglucosamine (GlcNAc) to the Ser or Thr residue is a major posttranslational glycosylation event and is often associated with protein folding, stability, and activity.
29941599	1	30	theme	Protein	102:108	arg1	event					243:247	a major posttranslational glycosylation event	203:247	a major posttranslational glycosylation event	203:247	Protein O-glycosylation by attachment of β-N-acetylglucosamine (GlcNAc) to the Ser or Thr residue is a major posttranslational glycosylation event and is often associated with protein folding, stability, and activity.
29941599	5	31	theme	complex	1247:1253	arg1	integrity					1215:1223	the integrity	1211:1223	the integrity of the PRC2/EZH2 core complex	1211:1253	Mutation of the C-terminal O-GlcNAcylation site (S729A) in the catalytic domain of EZH2 abolishes the di- and trimethylation activities, but not the monomethylation of H3K27, nor the integrity of the PRC2/EZH2 core complex.
29941599	5	32	theme	di-	1134:1136	arg1	activities					1157:1166	the di- and trimethylation activities	1130:1166	the di- and trimethylation activities	1130:1166	Mutation of the C-terminal O-GlcNAcylation site (S729A) in the catalytic domain of EZH2 abolishes the di- and trimethylation activities, but not the monomethylation of H3K27, nor the integrity of the PRC2/EZH2 core complex.
29941599	2	33	theme	gene	422:425	arg1	expression					427:436	gene expression	422:436	gene expression	422:436	The methylation of histone H3 at Lys-27 catalyzed by the methyltransferase EZH2 was known to suppress gene expression and cancer development, and we previously reported that the O-GlcNAcylation of EZH2 at S76 stabilized EZH2 and facilitated the formation of H3K27me3 to inhibit tumor suppression.
29941599	4	34	theme	PRC2	1001:1004	arg1	EED					1027:1029	EED	1027:1029	EED	1027:1029	We also find that mutation of one or more of the O-GlcNAcylation sites S73A, S76A, S84A, and T313A in the N-terminal region decreases the stability of EZH2, but does not affect its association with the PRC2 components SUZ12 and EED.
29941599	4	34	theme	PRC2	1001:1004	arg1	SUZ12					1017:1021	SUZ12	1017:1021	SUZ12	1017:1021	We also find that mutation of one or more of the O-GlcNAcylation sites S73A, S76A, S84A, and T313A in the N-terminal region decreases the stability of EZH2, but does not affect its association with the PRC2 components SUZ12 and EED.
29941599	4	34	theme	PRC2	1001:1004	arg1	components					1006:1015	the PRC2 components SUZ12 and EED	997:1029	the PRC2 components SUZ12 and EED	997:1029	We also find that mutation of one or more of the O-GlcNAcylation sites S73A, S76A, S84A, and T313A in the N-terminal region decreases the stability of EZH2, but does not affect its association with the PRC2 components SUZ12 and EED.
29941599	0	35	theme	enzymatic	44:52	arg1	activity					54:61	enzymatic activity	44:61	enzymatic activity	44:61	O-GlcNAcylation regulates the stability and enzymatic activity of the histone methyltransferase EZH2.
29941599	5	36	theme	trimethylation	1142:1155	arg1	activities					1157:1166	the di- and trimethylation activities	1130:1166	the di- and trimethylation activities	1130:1166	Mutation of the C-terminal O-GlcNAcylation site (S729A) in the catalytic domain of EZH2 abolishes the di- and trimethylation activities, but not the monomethylation of H3K27, nor the integrity of the PRC2/EZH2 core complex.
29941599	4	37	theme	one	829:831	arg1	mutation					817:824	mutation	817:824	mutation of one or more of the O-GlcNAcylation sites S73A, S76A, S84A, and T313A in the N-terminal region	817:921	We also find that mutation of one or more of the O-GlcNAcylation sites S73A, S76A, S84A, and T313A in the N-terminal region decreases the stability of EZH2, but does not affect its association with the PRC2 components SUZ12 and EED.
29941599	6	38	theme	EZH2	1433:1436	arg1	O-GlcNAcylation					1438:1452	EZH2 O-GlcNAcylation	1433:1452	EZH2 O-GlcNAcylation	1433:1452	Our results show the effect of individual O-GlcNAcylation sites on the function of EZH2 and suggest an alternative approach to tumor suppression through selective inhibition of EZH2 O-GlcNAcylation.
29941599	1	39	theme	major	205:209	arg1	O-glycosylation					110:124	Protein O-glycosylation	102:124	Protein O-glycosylation by attachment of β-N-acetylglucosamine (GlcNAc) to the Ser or Thr residue	102:198	Protein O-glycosylation by attachment of β-N-acetylglucosamine (GlcNAc) to the Ser or Thr residue is a major posttranslational glycosylation event and is often associated with protein folding, stability, and activity.
29941599	1	39	theme	major	205:209	arg1	event					243:247	a major posttranslational glycosylation event	203:247	a major posttranslational glycosylation event	203:247	Protein O-glycosylation by attachment of β-N-acetylglucosamine (GlcNAc) to the Ser or Thr residue is a major posttranslational glycosylation event and is often associated with protein folding, stability, and activity.
29941599	4	40	with	association	980:990	arg1	EED					1027:1029	EED	1027:1029	EED	1027:1029	We also find that mutation of one or more of the O-GlcNAcylation sites S73A, S76A, S84A, and T313A in the N-terminal region decreases the stability of EZH2, but does not affect its association with the PRC2 components SUZ12 and EED.
29941599	4	40	with	association	980:990	arg1	SUZ12					1017:1021	SUZ12	1017:1021	SUZ12	1017:1021	We also find that mutation of one or more of the O-GlcNAcylation sites S73A, S76A, S84A, and T313A in the N-terminal region decreases the stability of EZH2, but does not affect its association with the PRC2 components SUZ12 and EED.
29941599	4	40	with	association	980:990	arg1	components					1006:1015	the PRC2 components SUZ12 and EED	997:1029	the PRC2 components SUZ12 and EED	997:1029	We also find that mutation of one or more of the O-GlcNAcylation sites S73A, S76A, S84A, and T313A in the N-terminal region decreases the stability of EZH2, but does not affect its association with the PRC2 components SUZ12 and EED.
29941599	4	41	theme	N-terminal	905:914	arg1	region					916:921	the N-terminal region	901:921	the N-terminal region	901:921	We also find that mutation of one or more of the O-GlcNAcylation sites S73A, S76A, S84A, and T313A in the N-terminal region decreases the stability of EZH2, but does not affect its association with the PRC2 components SUZ12 and EED.
29941599	1	42	theme	posttranslational	211:227	arg1	O-glycosylation					110:124	Protein O-glycosylation	102:124	Protein O-glycosylation by attachment of β-N-acetylglucosamine (GlcNAc) to the Ser or Thr residue	102:198	Protein O-glycosylation by attachment of β-N-acetylglucosamine (GlcNAc) to the Ser or Thr residue is a major posttranslational glycosylation event and is often associated with protein folding, stability, and activity.
29941599	1	42	theme	posttranslational	211:227	arg1	event					243:247	a major posttranslational glycosylation event	203:247	a major posttranslational glycosylation event	203:247	Protein O-glycosylation by attachment of β-N-acetylglucosamine (GlcNAc) to the Ser or Thr residue is a major posttranslational glycosylation event and is often associated with protein folding, stability, and activity.
29941599	2	43	theme	H3K27me3	578:585	arg1	formation					565:573	the formation	561:573	the formation of H3K27me3 to inhibit tumor suppression	561:614	The methylation of histone H3 at Lys-27 catalyzed by the methyltransferase EZH2 was known to suppress gene expression and cancer development, and we previously reported that the O-GlcNAcylation of EZH2 at S76 stabilized EZH2 and facilitated the formation of H3K27me3 to inhibit tumor suppression.
29941599	5	44	theme	C-terminal	1048:1057	arg1	S729A					1081:1085	S729A	1081:1085	S729A	1081:1085	Mutation of the C-terminal O-GlcNAcylation site (S729A) in the catalytic domain of EZH2 abolishes the di- and trimethylation activities, but not the monomethylation of H3K27, nor the integrity of the PRC2/EZH2 core complex.
29941599	5	44	theme	C-terminal	1048:1057	arg1	site					1075:1078	the C-terminal O-GlcNAcylation site	1044:1078	the C-terminal O-GlcNAcylation site (S729A)	1044:1086	Mutation of the C-terminal O-GlcNAcylation site (S729A) in the catalytic domain of EZH2 abolishes the di- and trimethylation activities, but not the monomethylation of H3K27, nor the integrity of the PRC2/EZH2 core complex.
29941599	1	45	dep	Ser	181:183	arg1	residue					192:198	residue	192:198	residue	192:198	Protein O-glycosylation by attachment of β-N-acetylglucosamine (GlcNAc) to the Ser or Thr residue is a major posttranslational glycosylation event and is often associated with protein folding, stability, and activity.
29941599	1	45	dep	Ser	181:183	arg1	the					177:179	the	177:179	the	177:179	Protein O-glycosylation by attachment of β-N-acetylglucosamine (GlcNAc) to the Ser or Thr residue is a major posttranslational glycosylation event and is often associated with protein folding, stability, and activity.
29941599	2	46	theme	H3	347:348	arg1	methylation					324:334	The methylation	320:334	The methylation of histone H3 at Lys-27 catalyzed by the methyltransferase EZH2	320:398	The methylation of histone H3 at Lys-27 catalyzed by the methyltransferase EZH2 was known to suppress gene expression and cancer development, and we previously reported that the O-GlcNAcylation of EZH2 at S76 stabilized EZH2 and facilitated the formation of H3K27me3 to inhibit tumor suppression.
29941599	5	47	dep	di-	1134:1136	arg1	the					1130:1132	the	1130:1132	the	1130:1132	Mutation of the C-terminal O-GlcNAcylation site (S729A) in the catalytic domain of EZH2 abolishes the di- and trimethylation activities, but not the monomethylation of H3K27, nor the integrity of the PRC2/EZH2 core complex.
29941599	3	48	theme	O-GlcNAcylation	776:790	arg1	sites					792:796	five O-GlcNAcylation sites	771:796	five O-GlcNAcylation sites	771:796	In this study, we employed a fluorescence-based method of sugar labeling combined with mass spectrometry to investigate EZH2 glycosylation and identified five O-GlcNAcylation sites.
29941599	2	49	theme	histone	339:345	arg1	H3					347:348	histone H3	339:348	histone H3	339:348	The methylation of histone H3 at Lys-27 catalyzed by the methyltransferase EZH2 was known to suppress gene expression and cancer development, and we previously reported that the O-GlcNAcylation of EZH2 at S76 stabilized EZH2 and facilitated the formation of H3K27me3 to inhibit tumor suppression.
29941599	3	50	theme	sugar	675:679	arg1	labeling					681:688	sugar labeling	675:688	sugar labeling combined with mass spectrometry	675:720	In this study, we employed a fluorescence-based method of sugar labeling combined with mass spectrometry to investigate EZH2 glycosylation and identified five O-GlcNAcylation sites.
29941599	0	51	dep	stability	30:38	arg1	the					26:28	the	26:28	the	26:28	O-GlcNAcylation regulates the stability and enzymatic activity of the histone methyltransferase EZH2.
29941599	1	52	theme	β-N-acetylglucosamine	143:163	arg1	attachment					129:138	attachment	129:138	attachment of β-N-acetylglucosamine (GlcNAc) to the Ser or Thr residue	129:198	Protein O-glycosylation by attachment of β-N-acetylglucosamine (GlcNAc) to the Ser or Thr residue is a major posttranslational glycosylation event and is often associated with protein folding, stability, and activity.
29941599	1	53	theme	glycosylation	229:241	arg1	O-glycosylation					110:124	Protein O-glycosylation	102:124	Protein O-glycosylation by attachment of β-N-acetylglucosamine (GlcNAc) to the Ser or Thr residue	102:198	Protein O-glycosylation by attachment of β-N-acetylglucosamine (GlcNAc) to the Ser or Thr residue is a major posttranslational glycosylation event and is often associated with protein folding, stability, and activity.
29941599	1	53	theme	glycosylation	229:241	arg1	event					243:247	a major posttranslational glycosylation event	203:247	a major posttranslational glycosylation event	203:247	Protein O-glycosylation by attachment of β-N-acetylglucosamine (GlcNAc) to the Ser or Thr residue is a major posttranslational glycosylation event and is often associated with protein folding, stability, and activity.
29941599	2	54	from	S76	525:527	arg1	O-GlcNAcylation					498:512	the O-GlcNAcylation	494:512	the O-GlcNAcylation of EZH2 at S76	494:527	The methylation of histone H3 at Lys-27 catalyzed by the methyltransferase EZH2 was known to suppress gene expression and cancer development, and we previously reported that the O-GlcNAcylation of EZH2 at S76 stabilized EZH2 and facilitated the formation of H3K27me3 to inhibit tumor suppression.
29941599	6	55	theme	EZH2	1339:1342	arg1	function					1327:1334	the function	1323:1334	the function of EZH2	1323:1342	Our results show the effect of individual O-GlcNAcylation sites on the function of EZH2 and suggest an alternative approach to tumor suppression through selective inhibition of EZH2 O-GlcNAcylation.
29941599	4	56	from	mutation	817:824	arg1	region					916:921	the N-terminal region	901:921	the N-terminal region	901:921	We also find that mutation of one or more of the O-GlcNAcylation sites S73A, S76A, S84A, and T313A in the N-terminal region decreases the stability of EZH2, but does not affect its association with the PRC2 components SUZ12 and EED.
29941599	5	57	theme	PRC2/EZH2	1232:1240	arg1	complex					1247:1253	the PRC2/EZH2 core complex	1228:1253	the PRC2/EZH2 core complex	1228:1253	Mutation of the C-terminal O-GlcNAcylation site (S729A) in the catalytic domain of EZH2 abolishes the di- and trimethylation activities, but not the monomethylation of H3K27, nor the integrity of the PRC2/EZH2 core complex.
29941599	0	58	theme	histone	70:76	arg1	EZH2					96:99	the histone methyltransferase EZH2	66:99	the histone methyltransferase EZH2	66:99	O-GlcNAcylation regulates the stability and enzymatic activity of the histone methyltransferase EZH2.
29941599	5	59	theme	core	1242:1245	arg1	complex					1247:1253	the PRC2/EZH2 core complex	1228:1253	the PRC2/EZH2 core complex	1228:1253	Mutation of the C-terminal O-GlcNAcylation site (S729A) in the catalytic domain of EZH2 abolishes the di- and trimethylation activities, but not the monomethylation of H3K27, nor the integrity of the PRC2/EZH2 core complex.
29941599	4	60	theme	EZH2	950:953	arg1	stability					937:945	the stability	933:945	the stability of EZH2	933:953	We also find that mutation of one or more of the O-GlcNAcylation sites S73A, S76A, S84A, and T313A in the N-terminal region decreases the stability of EZH2, but does not affect its association with the PRC2 components SUZ12 and EED.
29941599	3	61	theme	mass	704:707	arg1	spectrometry					709:720	mass spectrometry	704:720	mass spectrometry	704:720	In this study, we employed a fluorescence-based method of sugar labeling combined with mass spectrometry to investigate EZH2 glycosylation and identified five O-GlcNAcylation sites.
29941599	5	62	theme	H3K27	1200:1204	arg1	monomethylation					1181:1195	the monomethylation	1177:1195	the monomethylation of H3K27	1177:1204	Mutation of the C-terminal O-GlcNAcylation site (S729A) in the catalytic domain of EZH2 abolishes the di- and trimethylation activities, but not the monomethylation of H3K27, nor the integrity of the PRC2/EZH2 core complex.
10713140	5	0	theme	tyrosinase	787:796	arg1	mutants					798:804	15 tyrosinase mutants	784:804	15 tyrosinase mutants lacking one or more of the occupied N-glycosylation sites	784:862	Analysis of the folding pathway and activity of 15 tyrosinase mutants lacking one or more of the occupied N-glycosylation sites shows that glycans at any two N-glycosylation sites are sufficient to interact with calnexin and give partial activity, but a specific pair of sites (Asn(86) and Asn(371)) is required for full activity.
10713140	6	1	with	mutants	1071:1077	arg1	sites					1114:1118	less than two N-glycosylation sites	1084:1118	less than two N-glycosylation sites	1084:1118	The mutants with less than two N-glycosylation sites do not interact with calnexin and show a complete absence of enzyme activity.
10713140	1	2	theme	melanin	168:174	arg1	biosynthesis					176:187	melanin biosynthesis	168:187	melanin biosynthesis in mammals	168:198	Tyrosinase is a copper-containing enzyme that regulates melanin biosynthesis in mammals.
10713140	2	3	from	type	325:328	arg1	humans					336:341	humans	336:341	humans	336:341	Mutations at a single N-glycosylation sequon of tyrosinase have been reported to be responsible for oculocutaneous albinism type IA in humans, characterized by inactive tyrosinase and the total absence of pigmentation.
10713140	5	4	theme	mutants	798:804	arg1	Analysis					736:743	Analysis	736:743	Analysis of the folding pathway	736:766	Analysis of the folding pathway and activity of 15 tyrosinase mutants lacking one or more of the occupied N-glycosylation sites shows that glycans at any two N-glycosylation sites are sufficient to interact with calnexin and give partial activity, but a specific pair of sites (Asn(86) and Asn(371)) is required for full activity.
10713140	5	4	theme	mutants	798:804	arg1	activity					772:779	activity	772:779	activity	772:779	Analysis of the folding pathway and activity of 15 tyrosinase mutants lacking one or more of the occupied N-glycosylation sites shows that glycans at any two N-glycosylation sites are sufficient to interact with calnexin and give partial activity, but a specific pair of sites (Asn(86) and Asn(371)) is required for full activity.
10713140	7	5	theme	Copper	1198:1203	arg1	analysis					1205:1212	Copper analysis	1198:1212	Copper analysis of selected mutants	1198:1232	Copper analysis of selected mutants suggests that the observed partial activity is due to two populations with differential copper content.
10713140	5	6	theme	folding	752:758	arg1	pathway					760:766	the folding pathway	748:766	the folding pathway	748:766	Analysis of the folding pathway and activity of 15 tyrosinase mutants lacking one or more of the occupied N-glycosylation sites shows that glycans at any two N-glycosylation sites are sufficient to interact with calnexin and give partial activity, but a specific pair of sites (Asn(86) and Asn(371)) is required for full activity.
10713140	5	7	theme	sites	1007:1011	arg1	pair					999:1002	a specific pair	988:1002	a specific pair of sites (Asn(86) and Asn(371))	988:1034	Analysis of the folding pathway and activity of 15 tyrosinase mutants lacking one or more of the occupied N-glycosylation sites shows that glycans at any two N-glycosylation sites are sufficient to interact with calnexin and give partial activity, but a specific pair of sites (Asn(86) and Asn(371)) is required for full activity.
10713140	5	8	gly	N-glycosylation	894:908	arg2	sites					910:914	any two N-glycosylation sites	886:914	any two N-glycosylation sites	886:914	Analysis of the folding pathway and activity of 15 tyrosinase mutants lacking one or more of the occupied N-glycosylation sites shows that glycans at any two N-glycosylation sites are sufficient to interact with calnexin and give partial activity, but a specific pair of sites (Asn(86) and Asn(371)) is required for full activity.
10713140	5	8	gly	N-glycosylation	894:908	arg2	two					890:892	two	890:892	two	890:892	Analysis of the folding pathway and activity of 15 tyrosinase mutants lacking one or more of the occupied N-glycosylation sites shows that glycans at any two N-glycosylation sites are sufficient to interact with calnexin and give partial activity, but a specific pair of sites (Asn(86) and Asn(371)) is required for full activity.
10713140	1	9	from	biosynthesis	176:187	arg1	mammals					192:198	mammals	192:198	mammals	192:198	Tyrosinase is a copper-containing enzyme that regulates melanin biosynthesis in mammals.
10713140	2	10	theme	albinism	316:323	arg1	type					325:328	oculocutaneous albinism type IA	301:331	oculocutaneous albinism type IA	301:331	Mutations at a single N-glycosylation sequon of tyrosinase have been reported to be responsible for oculocutaneous albinism type IA in humans, characterized by inactive tyrosinase and the total absence of pigmentation.
10713140	0	11	theme	quality	95:101	arg1	control					103:109	quality control	95:109	quality control	95:109	Mutations at critical N-glycosylation sites reduce tyrosinase activity by altering folding and quality control.
10713140	5	12	theme	full	1052:1055	arg1	activity					1057:1064	full activity	1052:1064	full activity	1052:1064	Analysis of the folding pathway and activity of 15 tyrosinase mutants lacking one or more of the occupied N-glycosylation sites shows that glycans at any two N-glycosylation sites are sufficient to interact with calnexin and give partial activity, but a specific pair of sites (Asn(86) and Asn(371)) is required for full activity.
10713140	5	13	from	sites	910:914	arg1	glycans					875:881	glycans	875:881	glycans at any two N-glycosylation sites	875:914	Analysis of the folding pathway and activity of 15 tyrosinase mutants lacking one or more of the occupied N-glycosylation sites shows that glycans at any two N-glycosylation sites are sufficient to interact with calnexin and give partial activity, but a specific pair of sites (Asn(86) and Asn(371)) is required for full activity.
10713140	2	14	theme	oculocutaneous	301:314	arg1	type					325:328	oculocutaneous albinism type IA	301:331	oculocutaneous albinism type IA	301:331	Mutations at a single N-glycosylation sequon of tyrosinase have been reported to be responsible for oculocutaneous albinism type IA in humans, characterized by inactive tyrosinase and the total absence of pigmentation.
10713140	3	15	theme	active	508:513	arg1	tyrosinase					515:524	biologically active tyrosinase	495:524	biologically active tyrosinase	495:524	To probe the role that each N-glycosylation site plays in the synthesis of biologically active tyrosinase, we analyzed the calnexin mediated folding of tyrosinase N-glycosylation mutants.
10713140	5	16	theme	specific	990:997	arg1	pair					999:1002	a specific pair	988:1002	a specific pair of sites (Asn(86) and Asn(371))	988:1034	Analysis of the folding pathway and activity of 15 tyrosinase mutants lacking one or more of the occupied N-glycosylation sites shows that glycans at any two N-glycosylation sites are sufficient to interact with calnexin and give partial activity, but a specific pair of sites (Asn(86) and Asn(371)) is required for full activity.
10713140	2	17	from	sequon	239:244	arg1	Mutations					201:209	Mutations	201:209	Mutations at a single N-glycosylation sequon of tyrosinase	201:258	Mutations at a single N-glycosylation sequon of tyrosinase have been reported to be responsible for oculocutaneous albinism type IA in humans, characterized by inactive tyrosinase and the total absence of pigmentation.
10713140	3	18	theme	N-glycosylation	448:462	arg1	site					464:467	each N-glycosylation site	443:467	each N-glycosylation site	443:467	To probe the role that each N-glycosylation site plays in the synthesis of biologically active tyrosinase, we analyzed the calnexin mediated folding of tyrosinase N-glycosylation mutants.
10713140	4	19	gly	N-glycosylation	658:672	arg2	six					644:646	six	644:646	six	644:646	We have determined that four of the six potential N-glycosylation sites, including that associated with albinism, are occupied.
10713140	4	19	gly	N-glycosylation	658:672	arg2	sites					674:678	the six potential N-glycosylation sites	640:678	the six potential N-glycosylation sites	640:678	We have determined that four of the six potential N-glycosylation sites, including that associated with albinism, are occupied.
10713140	6	20	theme	N-glycosylation	1098:1112	arg1	sites					1114:1118	less than two N-glycosylation sites	1084:1118	less than two N-glycosylation sites	1084:1118	The mutants with less than two N-glycosylation sites do not interact with calnexin and show a complete absence of enzyme activity.
10713140	3	21	theme	mediated	552:559	arg1	folding					561:567	the calnexin mediated folding	539:567	the calnexin mediated folding of tyrosinase N-glycosylation mutants	539:605	To probe the role that each N-glycosylation site plays in the synthesis of biologically active tyrosinase, we analyzed the calnexin mediated folding of tyrosinase N-glycosylation mutants.
10713140	2	22	theme	pigmentation	406:417	arg1	absence					395:401	the total absence	385:401	the total absence of pigmentation	385:417	Mutations at a single N-glycosylation sequon of tyrosinase have been reported to be responsible for oculocutaneous albinism type IA in humans, characterized by inactive tyrosinase and the total absence of pigmentation.
10713140	2	22	theme	pigmentation	406:417	arg1	tyrosinase					370:379	inactive tyrosinase	361:379	inactive tyrosinase	361:379	Mutations at a single N-glycosylation sequon of tyrosinase have been reported to be responsible for oculocutaneous albinism type IA in humans, characterized by inactive tyrosinase and the total absence of pigmentation.
10713140	0	23	from	sites	38:42	arg1	Mutations					0:8	Mutations	0:8	Mutations at critical N-glycosylation sites	0:42	Mutations at critical N-glycosylation sites reduce tyrosinase activity by altering folding and quality control.
10713140	8	24	theme	certain	1554:1560	arg1	disorders					1575:1583	certain pigmentation disorders	1554:1583	certain pigmentation disorders	1554:1583	By correlating the degree of folding with the activity of tyrosinase, we propose a local folding mechanism for tyrosinase that can explain the mechanism of inactivation of tyrosinase N-glycosylation mutants found in certain pigmentation disorders.
10713140	4	25	used	occupied	726:733	arg2	four					632:635	four	632:635	four	632:635	We have determined that four of the six potential N-glycosylation sites, including that associated with albinism, are occupied.
10713140	4	25	used	occupied	726:733	arg2	sites					674:678	the six potential N-glycosylation sites	640:678	the six potential N-glycosylation sites	640:678	We have determined that four of the six potential N-glycosylation sites, including that associated with albinism, are occupied.
10713140	3	26	theme	mutants	599:605	arg1	folding					561:567	the calnexin mediated folding	539:567	the calnexin mediated folding of tyrosinase N-glycosylation mutants	539:605	To probe the role that each N-glycosylation site plays in the synthesis of biologically active tyrosinase, we analyzed the calnexin mediated folding of tyrosinase N-glycosylation mutants.
10713140	8	27	theme	folding	1427:1433	arg1	mechanism					1435:1443	a local folding mechanism	1419:1443	a local folding mechanism for tyrosinase that can explain the mechanism of inactivation of tyrosinase N-glycosylation mutants found in certain pigmentation disorders	1419:1583	By correlating the degree of folding with the activity of tyrosinase, we propose a local folding mechanism for tyrosinase that can explain the mechanism of inactivation of tyrosinase N-glycosylation mutants found in certain pigmentation disorders.
10713140	5	28	theme	partial	966:972	arg1	activity					974:981	partial activity	966:981	partial activity	966:981	Analysis of the folding pathway and activity of 15 tyrosinase mutants lacking one or more of the occupied N-glycosylation sites shows that glycans at any two N-glycosylation sites are sufficient to interact with calnexin and give partial activity, but a specific pair of sites (Asn(86) and Asn(371)) is required for full activity.
10713140	7	29	theme	copper	1322:1327	arg1	content					1329:1335	differential copper content	1309:1335	differential copper content	1309:1335	Copper analysis of selected mutants suggests that the observed partial activity is due to two populations with differential copper content.
10713140	5	30	theme	N-glycosylation	894:908	arg1	sites					910:914	any two N-glycosylation sites	886:914	any two N-glycosylation sites	886:914	Analysis of the folding pathway and activity of 15 tyrosinase mutants lacking one or more of the occupied N-glycosylation sites shows that glycans at any two N-glycosylation sites are sufficient to interact with calnexin and give partial activity, but a specific pair of sites (Asn(86) and Asn(371)) is required for full activity.
10713140	0	31	theme	N-glycosylation	22:36	arg1	sites					38:42	critical N-glycosylation sites	13:42	critical N-glycosylation sites	13:42	Mutations at critical N-glycosylation sites reduce tyrosinase activity by altering folding and quality control.
10713140	6	32	gly	N-glycosylation	1098:1112	arg2	two					1094:1096	two	1094:1096	two	1094:1096	The mutants with less than two N-glycosylation sites do not interact with calnexin and show a complete absence of enzyme activity.
10713140	6	32	gly	N-glycosylation	1098:1112	arg2	sites					1114:1118	less than two N-glycosylation sites	1084:1118	less than two N-glycosylation sites	1084:1118	The mutants with less than two N-glycosylation sites do not interact with calnexin and show a complete absence of enzyme activity.
10713140	8	33	theme	mutants	1537:1543	arg1	inactivation					1494:1505	inactivation	1494:1505	inactivation of tyrosinase N-glycosylation mutants found in certain pigmentation disorders	1494:1583	By correlating the degree of folding with the activity of tyrosinase, we propose a local folding mechanism for tyrosinase that can explain the mechanism of inactivation of tyrosinase N-glycosylation mutants found in certain pigmentation disorders.
10713140	3	34	theme	tyrosinase	572:581	arg1	mutants					599:605	tyrosinase N-glycosylation mutants	572:605	tyrosinase N-glycosylation mutants	572:605	To probe the role that each N-glycosylation site plays in the synthesis of biologically active tyrosinase, we analyzed the calnexin mediated folding of tyrosinase N-glycosylation mutants.
10713140	4	35	theme	N-glycosylation	658:672	arg1	sites					674:678	the six potential N-glycosylation sites	640:678	the six potential N-glycosylation sites	640:678	We have determined that four of the six potential N-glycosylation sites, including that associated with albinism, are occupied.
10713140	0	36	theme	critical	13:20	arg1	sites					38:42	critical N-glycosylation sites	13:42	critical N-glycosylation sites	13:42	Mutations at critical N-glycosylation sites reduce tyrosinase activity by altering folding and quality control.
10713140	8	37	theme	N-glycosylation	1521:1535	arg1	mutants					1537:1543	tyrosinase N-glycosylation mutants	1510:1543	tyrosinase N-glycosylation mutants found in certain pigmentation disorders	1510:1583	By correlating the degree of folding with the activity of tyrosinase, we propose a local folding mechanism for tyrosinase that can explain the mechanism of inactivation of tyrosinase N-glycosylation mutants found in certain pigmentation disorders.
10713140	3	38	theme	N-glycosylation	583:597	arg1	mutants					599:605	tyrosinase N-glycosylation mutants	572:605	tyrosinase N-glycosylation mutants	572:605	To probe the role that each N-glycosylation site plays in the synthesis of biologically active tyrosinase, we analyzed the calnexin mediated folding of tyrosinase N-glycosylation mutants.
10713140	5	39	theme	occupied	833:840	arg1	sites					858:862	the occupied N-glycosylation sites	829:862	the occupied N-glycosylation sites	829:862	Analysis of the folding pathway and activity of 15 tyrosinase mutants lacking one or more of the occupied N-glycosylation sites shows that glycans at any two N-glycosylation sites are sufficient to interact with calnexin and give partial activity, but a specific pair of sites (Asn(86) and Asn(371)) is required for full activity.
10713140	4	40	theme	potential	648:656	arg1	sites					674:678	the six potential N-glycosylation sites	640:678	the six potential N-glycosylation sites	640:678	We have determined that four of the six potential N-glycosylation sites, including that associated with albinism, are occupied.
10713140	7	41	theme	observed	1252:1259	arg1	due					1281:1283	due	1281:1283	due	1281:1283	Copper analysis of selected mutants suggests that the observed partial activity is due to two populations with differential copper content.
10713140	7	41	theme	observed	1252:1259	arg1	activity					1269:1276	the observed partial activity	1248:1276	the observed partial activity	1248:1276	Copper analysis of selected mutants suggests that the observed partial activity is due to two populations with differential copper content.
10713140	8	42	theme	tyrosinase	1510:1519	arg1	mutants					1537:1543	tyrosinase N-glycosylation mutants	1510:1543	tyrosinase N-glycosylation mutants found in certain pigmentation disorders	1510:1583	By correlating the degree of folding with the activity of tyrosinase, we propose a local folding mechanism for tyrosinase that can explain the mechanism of inactivation of tyrosinase N-glycosylation mutants found in certain pigmentation disorders.
10713140	8	43	theme	tyrosinase	1396:1405	arg1	activity					1384:1391	the activity	1380:1391	the activity of tyrosinase	1380:1405	By correlating the degree of folding with the activity of tyrosinase, we propose a local folding mechanism for tyrosinase that can explain the mechanism of inactivation of tyrosinase N-glycosylation mutants found in certain pigmentation disorders.
10713140	6	44	theme	activity	1188:1195	arg1	absence					1170:1176	a complete absence	1159:1176	a complete absence of enzyme activity	1159:1195	The mutants with less than two N-glycosylation sites do not interact with calnexin and show a complete absence of enzyme activity.
10713140	8	45	located	found	1545:1549	arg1	disorders					1575:1583	certain pigmentation disorders	1554:1583	certain pigmentation disorders	1554:1583	By correlating the degree of folding with the activity of tyrosinase, we propose a local folding mechanism for tyrosinase that can explain the mechanism of inactivation of tyrosinase N-glycosylation mutants found in certain pigmentation disorders.
10713140	8	45	located	found	1545:1549	arg2	mutants					1537:1543	tyrosinase N-glycosylation mutants	1510:1543	tyrosinase N-glycosylation mutants found in certain pigmentation disorders	1510:1583	By correlating the degree of folding with the activity of tyrosinase, we propose a local folding mechanism for tyrosinase that can explain the mechanism of inactivation of tyrosinase N-glycosylation mutants found in certain pigmentation disorders.
10713140	2	46	theme	tyrosinase	249:258	arg1	sequon					239:244	a single N-glycosylation sequon	214:244	a single N-glycosylation sequon of tyrosinase	214:258	Mutations at a single N-glycosylation sequon of tyrosinase have been reported to be responsible for oculocutaneous albinism type IA in humans, characterized by inactive tyrosinase and the total absence of pigmentation.
10713140	4	47	theme	sites	674:678	arg1	sites					674:678	the six potential N-glycosylation sites	640:678	the six potential N-glycosylation sites	640:678	We have determined that four of the six potential N-glycosylation sites, including that associated with albinism, are occupied.
10713140	4	47	theme	sites	674:678	arg1	four					632:635	four	632:635	four	632:635	We have determined that four of the six potential N-glycosylation sites, including that associated with albinism, are occupied.
10713140	8	48	theme	local	1421:1425	arg1	mechanism					1435:1443	a local folding mechanism	1419:1443	a local folding mechanism for tyrosinase that can explain the mechanism of inactivation of tyrosinase N-glycosylation mutants found in certain pigmentation disorders	1419:1583	By correlating the degree of folding with the activity of tyrosinase, we propose a local folding mechanism for tyrosinase that can explain the mechanism of inactivation of tyrosinase N-glycosylation mutants found in certain pigmentation disorders.
10713140	8	49	theme	pigmentation	1562:1573	arg1	disorders					1575:1583	certain pigmentation disorders	1554:1583	certain pigmentation disorders	1554:1583	By correlating the degree of folding with the activity of tyrosinase, we propose a local folding mechanism for tyrosinase that can explain the mechanism of inactivation of tyrosinase N-glycosylation mutants found in certain pigmentation disorders.
10713140	8	50	theme	inactivation	1494:1505	arg1	mechanism					1481:1489	the mechanism	1477:1489	the mechanism of inactivation of tyrosinase N-glycosylation mutants found in certain pigmentation disorders	1477:1583	By correlating the degree of folding with the activity of tyrosinase, we propose a local folding mechanism for tyrosinase that can explain the mechanism of inactivation of tyrosinase N-glycosylation mutants found in certain pigmentation disorders.
10713140	5	51	gly	N-glycosylation	842:856	arg2	sites					858:862	the occupied N-glycosylation sites	829:862	the occupied N-glycosylation sites	829:862	Analysis of the folding pathway and activity of 15 tyrosinase mutants lacking one or more of the occupied N-glycosylation sites shows that glycans at any two N-glycosylation sites are sufficient to interact with calnexin and give partial activity, but a specific pair of sites (Asn(86) and Asn(371)) is required for full activity.
10713140	2	52	theme	inactive	361:368	arg1	tyrosinase					370:379	inactive tyrosinase	361:379	inactive tyrosinase	361:379	Mutations at a single N-glycosylation sequon of tyrosinase have been reported to be responsible for oculocutaneous albinism type IA in humans, characterized by inactive tyrosinase and the total absence of pigmentation.
10713140	0	53	theme	tyrosinase	51:60	arg1	activity					62:69	tyrosinase activity	51:69	tyrosinase activity	51:69	Mutations at critical N-glycosylation sites reduce tyrosinase activity by altering folding and quality control.
10713140	8	54	theme	folding	1367:1373	arg1	degree					1357:1362	the degree	1353:1362	the degree of folding	1353:1373	By correlating the degree of folding with the activity of tyrosinase, we propose a local folding mechanism for tyrosinase that can explain the mechanism of inactivation of tyrosinase N-glycosylation mutants found in certain pigmentation disorders.
10713140	2	55	theme	N-glycosylation	223:237	arg1	sequon					239:244	a single N-glycosylation sequon	214:244	a single N-glycosylation sequon of tyrosinase	214:258	Mutations at a single N-glycosylation sequon of tyrosinase have been reported to be responsible for oculocutaneous albinism type IA in humans, characterized by inactive tyrosinase and the total absence of pigmentation.
10713140	0	56	gly	N-glycosylation	22:36	arg2	sites					38:42	critical N-glycosylation sites	13:42	critical N-glycosylation sites	13:42	Mutations at critical N-glycosylation sites reduce tyrosinase activity by altering folding and quality control.
10713140	3	57	theme	tyrosinase	515:524	arg1	synthesis					482:490	the synthesis	478:490	the synthesis of biologically active tyrosinase	478:524	To probe the role that each N-glycosylation site plays in the synthesis of biologically active tyrosinase, we analyzed the calnexin mediated folding of tyrosinase N-glycosylation mutants.
10713140	2	58	theme	single	216:221	arg1	sequon					239:244	a single N-glycosylation sequon	214:244	a single N-glycosylation sequon of tyrosinase	214:258	Mutations at a single N-glycosylation sequon of tyrosinase have been reported to be responsible for oculocutaneous albinism type IA in humans, characterized by inactive tyrosinase and the total absence of pigmentation.
10713140	6	59	theme	complete	1161:1168	arg1	absence					1170:1176	a complete absence	1159:1176	a complete absence of enzyme activity	1159:1195	The mutants with less than two N-glycosylation sites do not interact with calnexin and show a complete absence of enzyme activity.
10713140	6	60	theme	enzyme	1181:1186	arg1	activity					1188:1195	enzyme activity	1181:1195	enzyme activity	1181:1195	The mutants with less than two N-glycosylation sites do not interact with calnexin and show a complete absence of enzyme activity.
10713140	1	61	theme	copper-containing	128:144	arg1	enzyme					146:151	a copper-containing enzyme	126:151	a copper-containing enzyme that regulates melanin biosynthesis in mammals	126:198	Tyrosinase is a copper-containing enzyme that regulates melanin biosynthesis in mammals.
10713140	1	61	theme	copper-containing	128:144	arg1	Tyrosinase					112:121	Tyrosinase	112:121	Tyrosinase	112:121	Tyrosinase is a copper-containing enzyme that regulates melanin biosynthesis in mammals.
10713140	2	62	gly	N-glycosylation	223:237	arg2	sequon					239:244	a single N-glycosylation sequon	214:244	a single N-glycosylation sequon of tyrosinase	214:258	Mutations at a single N-glycosylation sequon of tyrosinase have been reported to be responsible for oculocutaneous albinism type IA in humans, characterized by inactive tyrosinase and the total absence of pigmentation.
10713140	3	63	gly	N-glycosylation	448:462	arg2	site					464:467	each N-glycosylation site	443:467	each N-glycosylation site	443:467	To probe the role that each N-glycosylation site plays in the synthesis of biologically active tyrosinase, we analyzed the calnexin mediated folding of tyrosinase N-glycosylation mutants.
10713140	7	64	theme	mutants	1226:1232	arg1	analysis					1205:1212	Copper analysis	1198:1212	Copper analysis of selected mutants	1198:1232	Copper analysis of selected mutants suggests that the observed partial activity is due to two populations with differential copper content.
10713140	7	65	theme	selected	1217:1224	arg1	mutants					1226:1232	selected mutants	1217:1232	selected mutants	1217:1232	Copper analysis of selected mutants suggests that the observed partial activity is due to two populations with differential copper content.
10713140	7	66	with	populations	1292:1302	arg1	content					1329:1335	differential copper content	1309:1335	differential copper content	1309:1335	Copper analysis of selected mutants suggests that the observed partial activity is due to two populations with differential copper content.
10713140	5	67	dep	sites	1007:1011	arg1	Asn					1026:1028	Asn(371)	1026:1033	Asn(371)	1026:1033	Analysis of the folding pathway and activity of 15 tyrosinase mutants lacking one or more of the occupied N-glycosylation sites shows that glycans at any two N-glycosylation sites are sufficient to interact with calnexin and give partial activity, but a specific pair of sites (Asn(86) and Asn(371)) is required for full activity.
10713140	5	67	dep	sites	1007:1011	arg1	Asn					1014:1016	Asn(86)	1014:1020	Asn(86)	1014:1020	Analysis of the folding pathway and activity of 15 tyrosinase mutants lacking one or more of the occupied N-glycosylation sites shows that glycans at any two N-glycosylation sites are sufficient to interact with calnexin and give partial activity, but a specific pair of sites (Asn(86) and Asn(371)) is required for full activity.
10713140	5	67	dep	sites	1007:1011	arg1	sites					1007:1011	sites	1007:1011	sites (Asn(86) and Asn(371))	1007:1034	Analysis of the folding pathway and activity of 15 tyrosinase mutants lacking one or more of the occupied N-glycosylation sites shows that glycans at any two N-glycosylation sites are sufficient to interact with calnexin and give partial activity, but a specific pair of sites (Asn(86) and Asn(371)) is required for full activity.
10713140	5	68	theme	sites	858:862	arg1	sites					858:862	the occupied N-glycosylation sites	829:862	the occupied N-glycosylation sites	829:862	Analysis of the folding pathway and activity of 15 tyrosinase mutants lacking one or more of the occupied N-glycosylation sites shows that glycans at any two N-glycosylation sites are sufficient to interact with calnexin and give partial activity, but a specific pair of sites (Asn(86) and Asn(371)) is required for full activity.
10713140	5	68	theme	sites	858:862	arg1	one					814:816	one	814:816	one	814:816	Analysis of the folding pathway and activity of 15 tyrosinase mutants lacking one or more of the occupied N-glycosylation sites shows that glycans at any two N-glycosylation sites are sufficient to interact with calnexin and give partial activity, but a specific pair of sites (Asn(86) and Asn(371)) is required for full activity.
10713140	2	69	theme	total	389:393	arg1	absence					395:401	the total absence	385:401	the total absence of pigmentation	385:417	Mutations at a single N-glycosylation sequon of tyrosinase have been reported to be responsible for oculocutaneous albinism type IA in humans, characterized by inactive tyrosinase and the total absence of pigmentation.
10713140	7	70	theme	partial	1261:1267	arg1	due					1281:1283	due	1281:1283	due	1281:1283	Copper analysis of selected mutants suggests that the observed partial activity is due to two populations with differential copper content.
10713140	7	70	theme	partial	1261:1267	arg1	activity					1269:1276	the observed partial activity	1248:1276	the observed partial activity	1248:1276	Copper analysis of selected mutants suggests that the observed partial activity is due to two populations with differential copper content.
10713140	7	71	theme	differential	1309:1320	arg1	content					1329:1335	differential copper content	1309:1335	differential copper content	1309:1335	Copper analysis of selected mutants suggests that the observed partial activity is due to two populations with differential copper content.
10713140	5	72	theme	N-glycosylation	842:856	arg1	sites					858:862	the occupied N-glycosylation sites	829:862	the occupied N-glycosylation sites	829:862	Analysis of the folding pathway and activity of 15 tyrosinase mutants lacking one or more of the occupied N-glycosylation sites shows that glycans at any two N-glycosylation sites are sufficient to interact with calnexin and give partial activity, but a specific pair of sites (Asn(86) and Asn(371)) is required for full activity.
10713140	5	73	theme	pathway	760:766	arg1	Analysis					736:743	Analysis	736:743	Analysis of the folding pathway	736:766	Analysis of the folding pathway and activity of 15 tyrosinase mutants lacking one or more of the occupied N-glycosylation sites shows that glycans at any two N-glycosylation sites are sufficient to interact with calnexin and give partial activity, but a specific pair of sites (Asn(86) and Asn(371)) is required for full activity.
10713140	5	73	theme	pathway	760:766	arg1	activity					772:779	activity	772:779	activity	772:779	Analysis of the folding pathway and activity of 15 tyrosinase mutants lacking one or more of the occupied N-glycosylation sites shows that glycans at any two N-glycosylation sites are sufficient to interact with calnexin and give partial activity, but a specific pair of sites (Asn(86) and Asn(371)) is required for full activity.
15474009	0	0	theme	human	56:60	arg1	transferrin					62:72	human transferrin	56:72	human transferrin	56:72	N-glycosylation at Asn(491) in the Asn-Xaa-Cys motif of human transferrin.
15474009	0	1	from	Asn	19:21	arg1	N-glycosylation					0:14	N-glycosylation	0:14	N-glycosylation at Asn(491) in the Asn-Xaa-Cys motif of human transferrin.	0:73	N-glycosylation at Asn(491) in the Asn-Xaa-Cys motif of human transferrin.
15474009	2	2	from	motif	440:444	arg1	located					416:422	located	416:422	located	416:422	Both MS techniques clearly revealed the sequences of and the attachment sites of bi-antennary complex-type oligosaccharides, at both Asn432 and Asn630, both of which are located in a well-known motif for N-glycosylation, Asn-Xaa-Ser/Thr, but also at Asn491 in the Asn-Xaa-Cys motif.
15474009	1	3	theme	matrix-assisted	150:164	arg1	ionization					183:192	matrix-assisted laser desorption ionization	150:192	matrix-assisted laser desorption ionization	150:192	Glycopeptides derived from human transferrin were exhaustively analyzed by matrix-assisted laser desorption ionization and electrospray ionization mass spectrometry (MS).
15474009	2	4	theme	Asn-Xaa-Cys	510:520	arg1	motif					522:526	the Asn-Xaa-Cys motif	506:526	the Asn-Xaa-Cys motif	506:526	Both MS techniques clearly revealed the sequences of and the attachment sites of bi-antennary complex-type oligosaccharides, at both Asn432 and Asn630, both of which are located in a well-known motif for N-glycosylation, Asn-Xaa-Ser/Thr, but also at Asn491 in the Asn-Xaa-Cys motif.
15474009	0	5	from	N-glycosylation	0:14	arg1	motif					47:51	the Asn-Xaa-Cys motif	31:51	the Asn-Xaa-Cys motif of human transferrin	31:72	N-glycosylation at Asn(491) in the Asn-Xaa-Cys motif of human transferrin.
15474009	0	6	theme	transferrin	62:72	arg1	motif					47:51	the Asn-Xaa-Cys motif	31:51	the Asn-Xaa-Cys motif of human transferrin	31:72	N-glycosylation at Asn(491) in the Asn-Xaa-Cys motif of human transferrin.
15474009	3	7	from	site	588:591	arg1	glycoproteins					604:616	several glycoproteins	596:616	several glycoproteins	596:616	The latter has been reported to be a minor N-glycosylation site in several glycoproteins.
15474009	1	8	theme	laser	166:170	arg1	ionization					183:192	matrix-assisted laser desorption ionization	150:192	matrix-assisted laser desorption ionization	150:192	Glycopeptides derived from human transferrin were exhaustively analyzed by matrix-assisted laser desorption ionization and electrospray ionization mass spectrometry (MS).
15474009	1	9	theme	desorption	172:181	arg1	ionization					183:192	matrix-assisted laser desorption ionization	150:192	matrix-assisted laser desorption ionization	150:192	Glycopeptides derived from human transferrin were exhaustively analyzed by matrix-assisted laser desorption ionization and electrospray ionization mass spectrometry (MS).
15474009	4	10	dep	%	712:712	arg1	mol					709:711	mol	709:711	mol	709:711	The relative abundance of this abnormal glycosylation was estimated to be approximately 2 mol% of the transferrin preparation used in this study.
15474009	4	11	theme	glycosylation	659:671	arg1	abundance					632:640	The relative abundance	619:640	The relative abundance of this abnormal glycosylation	619:671	The relative abundance of this abnormal glycosylation was estimated to be approximately 2 mol% of the transferrin preparation used in this study.
15474009	4	11	theme	glycosylation	659:671	arg1	preparation					733:743	the transferrin preparation	717:743	the transferrin preparation used in this study	717:762	The relative abundance of this abnormal glycosylation was estimated to be approximately 2 mol% of the transferrin preparation used in this study.
15474009	4	11	theme	glycosylation	659:671	arg1	%					712:712	approximately 2 mol%	693:712	approximately 2 mol% of the transferrin preparation used in this study	693:762	The relative abundance of this abnormal glycosylation was estimated to be approximately 2 mol% of the transferrin preparation used in this study.
15474009	2	12	theme	well-known	429:438	arg1	motif					440:444	a well-known motif	427:444	a well-known motif for N-glycosylation	427:464	Both MS techniques clearly revealed the sequences of and the attachment sites of bi-antennary complex-type oligosaccharides, at both Asn432 and Asn630, both of which are located in a well-known motif for N-glycosylation, Asn-Xaa-Ser/Thr, but also at Asn491 in the Asn-Xaa-Cys motif.
15474009	2	12	theme	well-known	429:438	arg1	Asn-Xaa-Ser/Thr					467:481	Asn-Xaa-Ser/Thr	467:481	Asn-Xaa-Ser/Thr	467:481	Both MS techniques clearly revealed the sequences of and the attachment sites of bi-antennary complex-type oligosaccharides, at both Asn432 and Asn630, both of which are located in a well-known motif for N-glycosylation, Asn-Xaa-Ser/Thr, but also at Asn491 in the Asn-Xaa-Cys motif.
15474009	2	13	theme	attachment	307:316	arg1	oligosaccharides					353:368	bi-antennary complex-type oligosaccharides	327:368	bi-antennary complex-type oligosaccharides	327:368	Both MS techniques clearly revealed the sequences of and the attachment sites of bi-antennary complex-type oligosaccharides, at both Asn432 and Asn630, both of which are located in a well-known motif for N-glycosylation, Asn-Xaa-Ser/Thr, but also at Asn491 in the Asn-Xaa-Cys motif.
15474009	2	13	theme	attachment	307:316	arg1	sites					318:322	the attachment sites	303:322	the attachment sites of bi-antennary complex-type oligosaccharides	303:368	Both MS techniques clearly revealed the sequences of and the attachment sites of bi-antennary complex-type oligosaccharides, at both Asn432 and Asn630, both of which are located in a well-known motif for N-glycosylation, Asn-Xaa-Ser/Thr, but also at Asn491 in the Asn-Xaa-Cys motif.
15474009	4	14	theme	abnormal	650:657	arg1	glycosylation					659:671	this abnormal glycosylation	645:671	this abnormal glycosylation	645:671	The relative abundance of this abnormal glycosylation was estimated to be approximately 2 mol% of the transferrin preparation used in this study.
15474009	4	15	theme	preparation	733:743	arg1	preparation					733:743	the transferrin preparation	717:743	the transferrin preparation used in this study	717:762	The relative abundance of this abnormal glycosylation was estimated to be approximately 2 mol% of the transferrin preparation used in this study.
15474009	4	15	theme	preparation	733:743	arg1	abundance					632:640	The relative abundance	619:640	The relative abundance of this abnormal glycosylation	619:671	The relative abundance of this abnormal glycosylation was estimated to be approximately 2 mol% of the transferrin preparation used in this study.
15474009	4	15	theme	preparation	733:743	arg1	%					712:712	approximately 2 mol%	693:712	approximately 2 mol% of the transferrin preparation used in this study	693:762	The relative abundance of this abnormal glycosylation was estimated to be approximately 2 mol% of the transferrin preparation used in this study.
15474009	3	16	theme	minor	566:570	arg1	latter					533:538	latter	533:538	latter	533:538	The latter has been reported to be a minor N-glycosylation site in several glycoproteins.
15474009	3	16	theme	minor	566:570	arg1	site					588:591	a minor N-glycosylation site	564:591	a minor N-glycosylation site in several glycoproteins	564:616	The latter has been reported to be a minor N-glycosylation site in several glycoproteins.
15474009	1	17	theme	electrospray	198:209	arg1	MS					241:242	MS	241:242	MS	241:242	Glycopeptides derived from human transferrin were exhaustively analyzed by matrix-assisted laser desorption ionization and electrospray ionization mass spectrometry (MS).
15474009	1	17	theme	electrospray	198:209	arg1	spectrometry					227:238	electrospray ionization mass spectrometry	198:238	electrospray ionization mass spectrometry (MS)	198:243	Glycopeptides derived from human transferrin were exhaustively analyzed by matrix-assisted laser desorption ionization and electrospray ionization mass spectrometry (MS).
15474009	4	18	dep	mol	709:711	arg1	2					707:707	2	707:707	2	707:707	The relative abundance of this abnormal glycosylation was estimated to be approximately 2 mol% of the transferrin preparation used in this study.
15474009	4	19	theme	transferrin	721:731	arg1	preparation					733:743	the transferrin preparation	717:743	the transferrin preparation used in this study	717:762	The relative abundance of this abnormal glycosylation was estimated to be approximately 2 mol% of the transferrin preparation used in this study.
15474009	1	20	theme	ionization	211:220	arg1	MS					241:242	MS	241:242	MS	241:242	Glycopeptides derived from human transferrin were exhaustively analyzed by matrix-assisted laser desorption ionization and electrospray ionization mass spectrometry (MS).
15474009	1	20	theme	ionization	211:220	arg1	spectrometry					227:238	electrospray ionization mass spectrometry	198:238	electrospray ionization mass spectrometry (MS)	198:243	Glycopeptides derived from human transferrin were exhaustively analyzed by matrix-assisted laser desorption ionization and electrospray ionization mass spectrometry (MS).
15474009	2	21	theme	complex-type	340:351	arg1	oligosaccharides					353:368	bi-antennary complex-type oligosaccharides	327:368	bi-antennary complex-type oligosaccharides	327:368	Both MS techniques clearly revealed the sequences of and the attachment sites of bi-antennary complex-type oligosaccharides, at both Asn432 and Asn630, both of which are located in a well-known motif for N-glycosylation, Asn-Xaa-Ser/Thr, but also at Asn491 in the Asn-Xaa-Cys motif.
15474009	2	22	located	located	416:422	arg2	Asn432					379:384	Asn432	379:384	Asn432	379:384	Both MS techniques clearly revealed the sequences of and the attachment sites of bi-antennary complex-type oligosaccharides, at both Asn432 and Asn630, both of which are located in a well-known motif for N-glycosylation, Asn-Xaa-Ser/Thr, but also at Asn491 in the Asn-Xaa-Cys motif.
15474009	2	22	located	located	416:422	arg1	motif					440:444	a well-known motif	427:444	a well-known motif for N-glycosylation	427:464	Both MS techniques clearly revealed the sequences of and the attachment sites of bi-antennary complex-type oligosaccharides, at both Asn432 and Asn630, both of which are located in a well-known motif for N-glycosylation, Asn-Xaa-Ser/Thr, but also at Asn491 in the Asn-Xaa-Cys motif.
15474009	2	22	located	located	416:422	arg2	both					398:401	both	398:401	both	398:401	Both MS techniques clearly revealed the sequences of and the attachment sites of bi-antennary complex-type oligosaccharides, at both Asn432 and Asn630, both of which are located in a well-known motif for N-glycosylation, Asn-Xaa-Ser/Thr, but also at Asn491 in the Asn-Xaa-Cys motif.
15474009	2	22	located	located	416:422	arg1	Asn-Xaa-Ser/Thr					467:481	Asn-Xaa-Ser/Thr	467:481	Asn-Xaa-Ser/Thr	467:481	Both MS techniques clearly revealed the sequences of and the attachment sites of bi-antennary complex-type oligosaccharides, at both Asn432 and Asn630, both of which are located in a well-known motif for N-glycosylation, Asn-Xaa-Ser/Thr, but also at Asn491 in the Asn-Xaa-Cys motif.
15474009	0	23	gly	N-glycosylation	0:14	arg1	Asn					19:21	Asn	19:21	Asn(491)	19:26	N-glycosylation at Asn(491) in the Asn-Xaa-Cys motif of human transferrin.
15474009	0	23	gly	N-glycosylation	0:14	arg2	491					23:25	491	23:25	491	23:25	N-glycosylation at Asn(491) in the Asn-Xaa-Cys motif of human transferrin.
15474009	0	23	gly	N-glycosylation	0:14	arg1	motif					47:51	the Asn-Xaa-Cys motif	31:51	the Asn-Xaa-Cys motif of human transferrin	31:72	N-glycosylation at Asn(491) in the Asn-Xaa-Cys motif of human transferrin.
15474009	0	23	gly	N-glycosylation	0:14	arg1	491					23:25	491	23:25	491	23:25	N-glycosylation at Asn(491) in the Asn-Xaa-Cys motif of human transferrin.
15474009	0	23	gly	N-glycosylation	0:14	arg2	Asn					19:21	Asn	19:21	Asn(491)	19:26	N-glycosylation at Asn(491) in the Asn-Xaa-Cys motif of human transferrin.
15474009	1	24	theme	mass	222:225	arg1	MS					241:242	MS	241:242	MS	241:242	Glycopeptides derived from human transferrin were exhaustively analyzed by matrix-assisted laser desorption ionization and electrospray ionization mass spectrometry (MS).
15474009	1	24	theme	mass	222:225	arg1	spectrometry					227:238	electrospray ionization mass spectrometry	198:238	electrospray ionization mass spectrometry (MS)	198:243	Glycopeptides derived from human transferrin were exhaustively analyzed by matrix-assisted laser desorption ionization and electrospray ionization mass spectrometry (MS).
15474009	3	25	gly	glycoproteins	604:616	arg1	glycoproteins					604:616	several glycoproteins	596:616	several glycoproteins	596:616	The latter has been reported to be a minor N-glycosylation site in several glycoproteins.
15474009	3	26	theme	N-glycosylation	572:586	arg1	latter					533:538	latter	533:538	latter	533:538	The latter has been reported to be a minor N-glycosylation site in several glycoproteins.
15474009	3	26	theme	N-glycosylation	572:586	arg1	site					588:591	a minor N-glycosylation site	564:591	a minor N-glycosylation site in several glycoproteins	564:616	The latter has been reported to be a minor N-glycosylation site in several glycoproteins.
15474009	4	27	theme	relative	623:630	arg1	abundance					632:640	The relative abundance	619:640	The relative abundance of this abnormal glycosylation	619:671	The relative abundance of this abnormal glycosylation was estimated to be approximately 2 mol% of the transferrin preparation used in this study.
15474009	4	27	theme	relative	623:630	arg1	preparation					733:743	the transferrin preparation	717:743	the transferrin preparation used in this study	717:762	The relative abundance of this abnormal glycosylation was estimated to be approximately 2 mol% of the transferrin preparation used in this study.
15474009	4	27	theme	relative	623:630	arg1	%					712:712	approximately 2 mol%	693:712	approximately 2 mol% of the transferrin preparation used in this study	693:762	The relative abundance of this abnormal glycosylation was estimated to be approximately 2 mol% of the transferrin preparation used in this study.
15474009	2	28	theme	oligosaccharides	353:368	arg1	sequences					286:294	the sequences	282:294	the sequences of	282:297	Both MS techniques clearly revealed the sequences of and the attachment sites of bi-antennary complex-type oligosaccharides, at both Asn432 and Asn630, both of which are located in a well-known motif for N-glycosylation, Asn-Xaa-Ser/Thr, but also at Asn491 in the Asn-Xaa-Cys motif.
15474009	2	28	theme	oligosaccharides	353:368	arg1	oligosaccharides					353:368	bi-antennary complex-type oligosaccharides	327:368	bi-antennary complex-type oligosaccharides	327:368	Both MS techniques clearly revealed the sequences of and the attachment sites of bi-antennary complex-type oligosaccharides, at both Asn432 and Asn630, both of which are located in a well-known motif for N-glycosylation, Asn-Xaa-Ser/Thr, but also at Asn491 in the Asn-Xaa-Cys motif.
15474009	2	28	theme	oligosaccharides	353:368	arg1	sites					318:322	the attachment sites	303:322	the attachment sites of bi-antennary complex-type oligosaccharides	303:368	Both MS techniques clearly revealed the sequences of and the attachment sites of bi-antennary complex-type oligosaccharides, at both Asn432 and Asn630, both of which are located in a well-known motif for N-glycosylation, Asn-Xaa-Ser/Thr, but also at Asn491 in the Asn-Xaa-Cys motif.
15474009	1	29	attach	derived	89:95	arg1	transferrin					108:118	human transferrin	102:118	human transferrin	102:118	Glycopeptides derived from human transferrin were exhaustively analyzed by matrix-assisted laser desorption ionization and electrospray ionization mass spectrometry (MS).
15474009	1	29	attach	derived	89:95	arg2	Glycopeptides					75:87	Glycopeptides	75:87	Glycopeptides derived from human transferrin	75:118	Glycopeptides derived from human transferrin were exhaustively analyzed by matrix-assisted laser desorption ionization and electrospray ionization mass spectrometry (MS).
15474009	1	30	theme	human	102:106	arg1	transferrin					108:118	human transferrin	102:118	human transferrin	102:118	Glycopeptides derived from human transferrin were exhaustively analyzed by matrix-assisted laser desorption ionization and electrospray ionization mass spectrometry (MS).
15474009	2	31	from	Asn491	496:501	arg1	motif					522:526	the Asn-Xaa-Cys motif	506:526	the Asn-Xaa-Cys motif	506:526	Both MS techniques clearly revealed the sequences of and the attachment sites of bi-antennary complex-type oligosaccharides, at both Asn432 and Asn630, both of which are located in a well-known motif for N-glycosylation, Asn-Xaa-Ser/Thr, but also at Asn491 in the Asn-Xaa-Cys motif.
15474009	3	32	theme	several	596:602	arg1	glycoproteins					604:616	several glycoproteins	596:616	several glycoproteins	596:616	The latter has been reported to be a minor N-glycosylation site in several glycoproteins.
15474009	2	33	theme	bi-antennary	327:338	arg1	oligosaccharides					353:368	bi-antennary complex-type oligosaccharides	327:368	bi-antennary complex-type oligosaccharides	327:368	Both MS techniques clearly revealed the sequences of and the attachment sites of bi-antennary complex-type oligosaccharides, at both Asn432 and Asn630, both of which are located in a well-known motif for N-glycosylation, Asn-Xaa-Ser/Thr, but also at Asn491 in the Asn-Xaa-Cys motif.
15474009	2	34	theme	MS	251:252	arg1	techniques					254:263	Both MS techniques	246:263	Both MS techniques	246:263	Both MS techniques clearly revealed the sequences of and the attachment sites of bi-antennary complex-type oligosaccharides, at both Asn432 and Asn630, both of which are located in a well-known motif for N-glycosylation, Asn-Xaa-Ser/Thr, but also at Asn491 in the Asn-Xaa-Cys motif.
15474009	3	35	gly	N-glycosylation	572:586	arg2	latter					533:538	latter	533:538	latter	533:538	The latter has been reported to be a minor N-glycosylation site in several glycoproteins.
15474009	3	35	gly	N-glycosylation	572:586	arg2	site					588:591	a minor N-glycosylation site	564:591	a minor N-glycosylation site in several glycoproteins	564:616	The latter has been reported to be a minor N-glycosylation site in several glycoproteins.
15474009	0	36	theme	Asn-Xaa-Cys	35:45	arg1	motif					47:51	the Asn-Xaa-Cys motif	31:51	the Asn-Xaa-Cys motif of human transferrin	31:72	N-glycosylation at Asn(491) in the Asn-Xaa-Cys motif of human transferrin.
15474009	2	37	from	located	416:422	arg1	motif					440:444	a well-known motif	427:444	a well-known motif for N-glycosylation	427:464	Both MS techniques clearly revealed the sequences of and the attachment sites of bi-antennary complex-type oligosaccharides, at both Asn432 and Asn630, both of which are located in a well-known motif for N-glycosylation, Asn-Xaa-Ser/Thr, but also at Asn491 in the Asn-Xaa-Cys motif.
15474009	2	37	from	located	416:422	arg1	Asn-Xaa-Ser/Thr					467:481	Asn-Xaa-Ser/Thr	467:481	Asn-Xaa-Ser/Thr	467:481	Both MS techniques clearly revealed the sequences of and the attachment sites of bi-antennary complex-type oligosaccharides, at both Asn432 and Asn630, both of which are located in a well-known motif for N-glycosylation, Asn-Xaa-Ser/Thr, but also at Asn491 in the Asn-Xaa-Cys motif.
15498570	0	0	theme	glycoprotein	78:89	arg1	secretion					42:50	efficient secretion	32:50	efficient secretion of a novel human secreted glycoprotein, hPAP21	32:97	N-glycosylation is required for efficient secretion of a novel human secreted glycoprotein, hPAP21.
15498570	1	1	from	peptide	373:379	arg1	N-terminus					388:397	its N-terminus	384:397	its N-terminus	384:397	The present study reported the isolation and characterization of a novel human secreted protein, named as hPAP21 (human protease-associated domain-containing protein, 21 kDa), encoded by the hypothetical gene chromosome 2 open reading frame 7 (C2orf7) that contains signal peptide in its N-terminus, without transmembrane domain, except for PA domain in its middle.
15498570	6	2	theme	Asn171	1163:1168	arg1	process					1205:1211	potential crucial process	1187:1211	potential crucial process for the secretory protein	1187:1237	Furthermore, N-glycosylation of Asn171 was confirmed as potential crucial process for the secretory protein via site-directed mutagenesis assay.
15498570	6	2	theme	Asn171	1163:1168	arg1	N-glycosylation					1144:1158	N-glycosylation	1144:1158	N-glycosylation of Asn171	1144:1168	Furthermore, N-glycosylation of Asn171 was confirmed as potential crucial process for the secretory protein via site-directed mutagenesis assay.
15498570	4	3	theme	glycosylation	916:928	arg1	types					930:934	glycosylation types	916:934	glycosylation types	916:934	To define whether the glycosylation was important process for its secretion, endoglycosidase H (Endo H) and PNGase F (PNG F) were employed to evaluate the effect of glycosylation types on secretion of hPAP21.
15498570	1	4	theme	domain-containing	240:256	arg1	protein					258:264	human protease-associated domain-containing protein	214:264	human protease-associated domain-containing protein	214:264	The present study reported the isolation and characterization of a novel human secreted protein, named as hPAP21 (human protease-associated domain-containing protein, 21 kDa), encoded by the hypothetical gene chromosome 2 open reading frame 7 (C2orf7) that contains signal peptide in its N-terminus, without transmembrane domain, except for PA domain in its middle.
15498570	1	4	theme	domain-containing	240:256	arg1	kDa					270:272	21 kDa	267:272	21 kDa	267:272	The present study reported the isolation and characterization of a novel human secreted protein, named as hPAP21 (human protease-associated domain-containing protein, 21 kDa), encoded by the hypothetical gene chromosome 2 open reading frame 7 (C2orf7) that contains signal peptide in its N-terminus, without transmembrane domain, except for PA domain in its middle.
15498570	0	5	theme	secreted	69:76	arg1	hPAP21					92:97	hPAP21	92:97	hPAP21	92:97	N-glycosylation is required for efficient secretion of a novel human secreted glycoprotein, hPAP21.
15498570	0	5	theme	secreted	69:76	arg1	glycoprotein					78:89	a novel human secreted glycoprotein	55:89	a novel human secreted glycoprotein	55:89	N-glycosylation is required for efficient secretion of a novel human secreted glycoprotein, hPAP21.
15498570	1	6	theme	open	322:325	arg1	frame					335:339	the hypothetical gene chromosome 2 open reading frame 7	287:341	the hypothetical gene chromosome 2 open reading frame 7 (C2orf7) that contains signal peptide in its N-terminus	287:397	The present study reported the isolation and characterization of a novel human secreted protein, named as hPAP21 (human protease-associated domain-containing protein, 21 kDa), encoded by the hypothetical gene chromosome 2 open reading frame 7 (C2orf7) that contains signal peptide in its N-terminus, without transmembrane domain, except for PA domain in its middle.
15498570	1	6	theme	open	322:325	arg1	C2orf7					344:349	C2orf7	344:349	C2orf7	344:349	The present study reported the isolation and characterization of a novel human secreted protein, named as hPAP21 (human protease-associated domain-containing protein, 21 kDa), encoded by the hypothetical gene chromosome 2 open reading frame 7 (C2orf7) that contains signal peptide in its N-terminus, without transmembrane domain, except for PA domain in its middle.
15498570	2	7	theme	culture	551:557	arg1	medium					559:564	culture medium	551:564	culture medium	551:564	Western blotting assay indicated that the c-Myc tagged hPAP21 could be secreted into culture medium in the transfected Chinese hamster ovary cells.
15498570	6	8	theme	secretory	1221:1229	arg1	protein					1231:1237	the secretory protein	1217:1237	the secretory protein	1217:1237	Furthermore, N-glycosylation of Asn171 was confirmed as potential crucial process for the secretory protein via site-directed mutagenesis assay.
15498570	5	9	theme	hPAP21	1123:1128	arg1	secretion					1110:1118	the secretion	1106:1118	the secretion of hPAP21	1106:1128	Interestingly, the extracellular forms were primarily sensitive to PNG F, not Endo H, implying that complex N-glycosylation could be required for the secretion of hPAP21.
15498570	5	10	theme	complex	1060:1066	arg1	N-glycosylation					1068:1082	complex N-glycosylation	1060:1082	complex N-glycosylation	1060:1082	Interestingly, the extracellular forms were primarily sensitive to PNG F, not Endo H, implying that complex N-glycosylation could be required for the secretion of hPAP21.
15498570	1	11	theme	reading	327:333	arg1	frame					335:339	the hypothetical gene chromosome 2 open reading frame 7	287:341	the hypothetical gene chromosome 2 open reading frame 7 (C2orf7) that contains signal peptide in its N-terminus	287:397	The present study reported the isolation and characterization of a novel human secreted protein, named as hPAP21 (human protease-associated domain-containing protein, 21 kDa), encoded by the hypothetical gene chromosome 2 open reading frame 7 (C2orf7) that contains signal peptide in its N-terminus, without transmembrane domain, except for PA domain in its middle.
15498570	1	11	theme	reading	327:333	arg1	C2orf7					344:349	C2orf7	344:349	C2orf7	344:349	The present study reported the isolation and characterization of a novel human secreted protein, named as hPAP21 (human protease-associated domain-containing protein, 21 kDa), encoded by the hypothetical gene chromosome 2 open reading frame 7 (C2orf7) that contains signal peptide in its N-terminus, without transmembrane domain, except for PA domain in its middle.
15498570	2	12	theme	ovary	601:605	arg1	cells					607:611	the transfected Chinese hamster ovary cells	569:611	the transfected Chinese hamster ovary cells	569:611	Western blotting assay indicated that the c-Myc tagged hPAP21 could be secreted into culture medium in the transfected Chinese hamster ovary cells.
15498570	4	13	theme	PNG	869:871	arg1	F					866:866	PNGase F	859:866	PNGase F (PNG F)	859:874	To define whether the glycosylation was important process for its secretion, endoglycosidase H (Endo H) and PNGase F (PNG F) were employed to evaluate the effect of glycosylation types on secretion of hPAP21.
15498570	4	13	theme	PNG	869:871	arg1	F					873:873	PNG F	869:873	PNG F	869:873	To define whether the glycosylation was important process for its secretion, endoglycosidase H (Endo H) and PNGase F (PNG F) were employed to evaluate the effect of glycosylation types on secretion of hPAP21.
15498570	2	14	theme	blotting	474:481	arg1	assay					483:487	Western blotting assay	466:487	Western blotting assay	466:487	Western blotting assay indicated that the c-Myc tagged hPAP21 could be secreted into culture medium in the transfected Chinese hamster ovary cells.
15498570	7	15	theme	functions	1339:1347	arg1	understanding					1312:1324	the understanding	1308:1324	the understanding of molecular functions of hPAP21	1308:1357	All data will be contributed to the understanding of molecular functions of hPAP21.
15498570	4	16	theme	important	791:799	arg1	glycosylation					773:785	the glycosylation	769:785	the glycosylation	769:785	To define whether the glycosylation was important process for its secretion, endoglycosidase H (Endo H) and PNGase F (PNG F) were employed to evaluate the effect of glycosylation types on secretion of hPAP21.
15498570	4	16	theme	important	791:799	arg1	process					801:807	important process	791:807	important process	791:807	To define whether the glycosylation was important process for its secretion, endoglycosidase H (Endo H) and PNGase F (PNG F) were employed to evaluate the effect of glycosylation types on secretion of hPAP21.
15498570	1	17	theme	transmembrane	408:420	arg1	domain					422:427	transmembrane domain	408:427	transmembrane domain	408:427	The present study reported the isolation and characterization of a novel human secreted protein, named as hPAP21 (human protease-associated domain-containing protein, 21 kDa), encoded by the hypothetical gene chromosome 2 open reading frame 7 (C2orf7) that contains signal peptide in its N-terminus, without transmembrane domain, except for PA domain in its middle.
15498570	2	18	theme	Western	466:472	arg1	assay					483:487	Western blotting assay	466:487	Western blotting assay	466:487	Western blotting assay indicated that the c-Myc tagged hPAP21 could be secreted into culture medium in the transfected Chinese hamster ovary cells.
15498570	2	19	theme	Chinese	585:591	arg1	cells					607:611	the transfected Chinese hamster ovary cells	569:611	the transfected Chinese hamster ovary cells	569:611	Western blotting assay indicated that the c-Myc tagged hPAP21 could be secreted into culture medium in the transfected Chinese hamster ovary cells.
15498570	2	20	theme	hamster	593:599	arg1	cells					607:611	the transfected Chinese hamster ovary cells	569:611	the transfected Chinese hamster ovary cells	569:611	Western blotting assay indicated that the c-Myc tagged hPAP21 could be secreted into culture medium in the transfected Chinese hamster ovary cells.
15498570	6	21	theme	mutagenesis	1257:1267	arg1	assay					1269:1273	site-directed mutagenesis assay	1243:1273	site-directed mutagenesis assay	1243:1273	Furthermore, N-glycosylation of Asn171 was confirmed as potential crucial process for the secretory protein via site-directed mutagenesis assay.
15498570	3	22	dep	forms	704:708	arg1	whatever					646:653	whatever	646:653	whatever	646:653	However, the molecular weights, whatever intracellular (28 kDa) or extracellular (30 kDa) forms, are larger than that of the prediction.
15498570	2	23	theme	transfected	573:583	arg1	cells					607:611	the transfected Chinese hamster ovary cells	569:611	the transfected Chinese hamster ovary cells	569:611	Western blotting assay indicated that the c-Myc tagged hPAP21 could be secreted into culture medium in the transfected Chinese hamster ovary cells.
15498570	0	24	gly	glycoprotein	78:89	arg1	hPAP21					92:97	hPAP21	92:97	hPAP21	92:97	N-glycosylation is required for efficient secretion of a novel human secreted glycoprotein, hPAP21.
15498570	0	24	gly	glycoprotein	78:89	arg1	glycoprotein					78:89	a novel human secreted glycoprotein	55:89	a novel human secreted glycoprotein	55:89	N-glycosylation is required for efficient secretion of a novel human secreted glycoprotein, hPAP21.
15498570	7	25	theme	molecular	1329:1337	arg1	functions					1339:1347	molecular functions	1329:1347	molecular functions of hPAP21	1329:1357	All data will be contributed to the understanding of molecular functions of hPAP21.
15498570	1	26	theme	novel	167:171	arg1	protein					188:194	a novel human secreted protein	165:194	a novel human secreted protein	165:194	The present study reported the isolation and characterization of a novel human secreted protein, named as hPAP21 (human protease-associated domain-containing protein, 21 kDa), encoded by the hypothetical gene chromosome 2 open reading frame 7 (C2orf7) that contains signal peptide in its N-terminus, without transmembrane domain, except for PA domain in its middle.
15498570	3	27	dep	intracellular	655:667	arg1	kDa					673:675	28 kDa	670:675	28 kDa	670:675	However, the molecular weights, whatever intracellular (28 kDa) or extracellular (30 kDa) forms, are larger than that of the prediction.
15498570	1	28	theme	human	173:177	arg1	protein					188:194	a novel human secreted protein	165:194	a novel human secreted protein	165:194	The present study reported the isolation and characterization of a novel human secreted protein, named as hPAP21 (human protease-associated domain-containing protein, 21 kDa), encoded by the hypothetical gene chromosome 2 open reading frame 7 (C2orf7) that contains signal peptide in its N-terminus, without transmembrane domain, except for PA domain in its middle.
15498570	6	29	theme	crucial	1197:1203	arg1	N-glycosylation					1144:1158	N-glycosylation	1144:1158	N-glycosylation of Asn171	1144:1168	Furthermore, N-glycosylation of Asn171 was confirmed as potential crucial process for the secretory protein via site-directed mutagenesis assay.
15498570	6	29	theme	crucial	1197:1203	arg1	process					1205:1211	potential crucial process	1187:1211	potential crucial process for the secretory protein	1187:1237	Furthermore, N-glycosylation of Asn171 was confirmed as potential crucial process for the secretory protein via site-directed mutagenesis assay.
15498570	5	30	theme	Endo	1038:1041	arg1	H					1043:1043	Endo H	1038:1043	Endo H	1038:1043	Interestingly, the extracellular forms were primarily sensitive to PNG F, not Endo H, implying that complex N-glycosylation could be required for the secretion of hPAP21.
15498570	5	30	theme	Endo	1038:1041	arg1	F					1031:1031	PNG F	1027:1031	PNG F	1027:1031	Interestingly, the extracellular forms were primarily sensitive to PNG F, not Endo H, implying that complex N-glycosylation could be required for the secretion of hPAP21.
15498570	5	31	gly	N-glycosylation	1068:1082	arg1	hPAP21					1123:1128	hPAP21	1123:1128	hPAP21	1123:1128	Interestingly, the extracellular forms were primarily sensitive to PNG F, not Endo H, implying that complex N-glycosylation could be required for the secretion of hPAP21.
15498570	1	32	theme	secreted	179:186	arg1	protein					188:194	a novel human secreted protein	165:194	a novel human secreted protein	165:194	The present study reported the isolation and characterization of a novel human secreted protein, named as hPAP21 (human protease-associated domain-containing protein, 21 kDa), encoded by the hypothetical gene chromosome 2 open reading frame 7 (C2orf7) that contains signal peptide in its N-terminus, without transmembrane domain, except for PA domain in its middle.
15498570	4	33	from	effect	906:911	arg1	secretion					939:947	secretion	939:947	secretion of hPAP21	939:957	To define whether the glycosylation was important process for its secretion, endoglycosidase H (Endo H) and PNGase F (PNG F) were employed to evaluate the effect of glycosylation types on secretion of hPAP21.
15498570	2	34	theme	c-Myc	508:512	arg1	hPAP21					521:526	the c-Myc tagged hPAP21	504:526	the c-Myc tagged hPAP21	504:526	Western blotting assay indicated that the c-Myc tagged hPAP21 could be secreted into culture medium in the transfected Chinese hamster ovary cells.
15498570	1	35	theme	PA	441:442	arg1	domain					444:449	PA domain	441:449	PA domain in its middle	441:463	The present study reported the isolation and characterization of a novel human secreted protein, named as hPAP21 (human protease-associated domain-containing protein, 21 kDa), encoded by the hypothetical gene chromosome 2 open reading frame 7 (C2orf7) that contains signal peptide in its N-terminus, without transmembrane domain, except for PA domain in its middle.
15498570	1	36	dep	isolation	131:139	arg1	the					127:129	the	127:129	the	127:129	The present study reported the isolation and characterization of a novel human secreted protein, named as hPAP21 (human protease-associated domain-containing protein, 21 kDa), encoded by the hypothetical gene chromosome 2 open reading frame 7 (C2orf7) that contains signal peptide in its N-terminus, without transmembrane domain, except for PA domain in its middle.
15498570	1	37	theme	protein	188:194	arg1	characterization					145:160	characterization	145:160	characterization	145:160	The present study reported the isolation and characterization of a novel human secreted protein, named as hPAP21 (human protease-associated domain-containing protein, 21 kDa), encoded by the hypothetical gene chromosome 2 open reading frame 7 (C2orf7) that contains signal peptide in its N-terminus, without transmembrane domain, except for PA domain in its middle.
15498570	1	37	theme	protein	188:194	arg1	isolation					131:139	isolation	131:139	isolation	131:139	The present study reported the isolation and characterization of a novel human secreted protein, named as hPAP21 (human protease-associated domain-containing protein, 21 kDa), encoded by the hypothetical gene chromosome 2 open reading frame 7 (C2orf7) that contains signal peptide in its N-terminus, without transmembrane domain, except for PA domain in its middle.
15498570	4	38	theme	endoglycosidase	828:842	arg1	H					844:844	endoglycosidase H	828:844	endoglycosidase H (Endo H)	828:853	To define whether the glycosylation was important process for its secretion, endoglycosidase H (Endo H) and PNGase F (PNG F) were employed to evaluate the effect of glycosylation types on secretion of hPAP21.
15498570	4	38	theme	endoglycosidase	828:842	arg1	H					852:852	Endo H	847:852	Endo H	847:852	To define whether the glycosylation was important process for its secretion, endoglycosidase H (Endo H) and PNGase F (PNG F) were employed to evaluate the effect of glycosylation types on secretion of hPAP21.
15498570	3	39	theme	extracellular	681:693	arg1	forms					704:708	intracellular (28 kDa) or extracellular (30 kDa) forms	655:708	intracellular (28 kDa) or extracellular (30 kDa) forms	655:708	However, the molecular weights, whatever intracellular (28 kDa) or extracellular (30 kDa) forms, are larger than that of the prediction.
15498570	4	40	theme	Endo	847:850	arg1	H					844:844	endoglycosidase H	828:844	endoglycosidase H (Endo H)	828:853	To define whether the glycosylation was important process for its secretion, endoglycosidase H (Endo H) and PNGase F (PNG F) were employed to evaluate the effect of glycosylation types on secretion of hPAP21.
15498570	4	40	theme	Endo	847:850	arg1	H					852:852	Endo H	847:852	Endo H	847:852	To define whether the glycosylation was important process for its secretion, endoglycosidase H (Endo H) and PNGase F (PNG F) were employed to evaluate the effect of glycosylation types on secretion of hPAP21.
15498570	0	41	gly	N-glycosylation	0:14	arg1	hPAP21					92:97	hPAP21	92:97	hPAP21	92:97	N-glycosylation is required for efficient secretion of a novel human secreted glycoprotein, hPAP21.
15498570	0	41	gly	N-glycosylation	0:14	arg1	glycoprotein					78:89	a novel human secreted glycoprotein	55:89	a novel human secreted glycoprotein	55:89	N-glycosylation is required for efficient secretion of a novel human secreted glycoprotein, hPAP21.
15498570	1	42	from	domain	444:449	arg1	middle					458:463	its middle	454:463	its middle	454:463	The present study reported the isolation and characterization of a novel human secreted protein, named as hPAP21 (human protease-associated domain-containing protein, 21 kDa), encoded by the hypothetical gene chromosome 2 open reading frame 7 (C2orf7) that contains signal peptide in its N-terminus, without transmembrane domain, except for PA domain in its middle.
15498570	0	43	theme	efficient	32:40	arg1	secretion					42:50	efficient secretion	32:50	efficient secretion of a novel human secreted glycoprotein, hPAP21	32:97	N-glycosylation is required for efficient secretion of a novel human secreted glycoprotein, hPAP21.
15498570	5	44	theme	PNG	1027:1029	arg1	H					1043:1043	Endo H	1038:1043	Endo H	1038:1043	Interestingly, the extracellular forms were primarily sensitive to PNG F, not Endo H, implying that complex N-glycosylation could be required for the secretion of hPAP21.
15498570	5	44	theme	PNG	1027:1029	arg1	F					1031:1031	PNG F	1027:1031	PNG F	1027:1031	Interestingly, the extracellular forms were primarily sensitive to PNG F, not Endo H, implying that complex N-glycosylation could be required for the secretion of hPAP21.
15498570	6	45	theme	potential	1187:1195	arg1	N-glycosylation					1144:1158	N-glycosylation	1144:1158	N-glycosylation of Asn171	1144:1168	Furthermore, N-glycosylation of Asn171 was confirmed as potential crucial process for the secretory protein via site-directed mutagenesis assay.
15498570	6	45	theme	potential	1187:1195	arg1	process					1205:1211	potential crucial process	1187:1211	potential crucial process for the secretory protein	1187:1237	Furthermore, N-glycosylation of Asn171 was confirmed as potential crucial process for the secretory protein via site-directed mutagenesis assay.
15498570	1	46	dep	hPAP21	206:211	arg1	protein					258:264	human protease-associated domain-containing protein	214:264	human protease-associated domain-containing protein	214:264	The present study reported the isolation and characterization of a novel human secreted protein, named as hPAP21 (human protease-associated domain-containing protein, 21 kDa), encoded by the hypothetical gene chromosome 2 open reading frame 7 (C2orf7) that contains signal peptide in its N-terminus, without transmembrane domain, except for PA domain in its middle.
15498570	1	46	dep	hPAP21	206:211	arg1	kDa					270:272	21 kDa	267:272	21 kDa	267:272	The present study reported the isolation and characterization of a novel human secreted protein, named as hPAP21 (human protease-associated domain-containing protein, 21 kDa), encoded by the hypothetical gene chromosome 2 open reading frame 7 (C2orf7) that contains signal peptide in its N-terminus, without transmembrane domain, except for PA domain in its middle.
15498570	7	47	theme	hPAP21	1352:1357	arg1	functions					1339:1347	molecular functions	1329:1347	molecular functions of hPAP21	1329:1357	All data will be contributed to the understanding of molecular functions of hPAP21.
15498570	1	48	theme	signal	366:371	arg1	peptide					373:379	signal peptide	366:379	signal peptide in its N-terminus	366:397	The present study reported the isolation and characterization of a novel human secreted protein, named as hPAP21 (human protease-associated domain-containing protein, 21 kDa), encoded by the hypothetical gene chromosome 2 open reading frame 7 (C2orf7) that contains signal peptide in its N-terminus, without transmembrane domain, except for PA domain in its middle.
15498570	5	49	theme	extracellular	979:991	arg1	forms					993:997	the extracellular forms	975:997	the extracellular forms	975:997	Interestingly, the extracellular forms were primarily sensitive to PNG F, not Endo H, implying that complex N-glycosylation could be required for the secretion of hPAP21.
15498570	5	49	theme	extracellular	979:991	arg1	sensitive					1014:1022	sensitive	1014:1022	sensitive	1014:1022	Interestingly, the extracellular forms were primarily sensitive to PNG F, not Endo H, implying that complex N-glycosylation could be required for the secretion of hPAP21.
15498570	1	50	theme	present	104:110	arg1	study					112:116	The present study	100:116	The present study	100:116	The present study reported the isolation and characterization of a novel human secreted protein, named as hPAP21 (human protease-associated domain-containing protein, 21 kDa), encoded by the hypothetical gene chromosome 2 open reading frame 7 (C2orf7) that contains signal peptide in its N-terminus, without transmembrane domain, except for PA domain in its middle.
15498570	1	51	theme	hypothetical	291:302	arg1	frame					335:339	the hypothetical gene chromosome 2 open reading frame 7	287:341	the hypothetical gene chromosome 2 open reading frame 7 (C2orf7) that contains signal peptide in its N-terminus	287:397	The present study reported the isolation and characterization of a novel human secreted protein, named as hPAP21 (human protease-associated domain-containing protein, 21 kDa), encoded by the hypothetical gene chromosome 2 open reading frame 7 (C2orf7) that contains signal peptide in its N-terminus, without transmembrane domain, except for PA domain in its middle.
15498570	1	51	theme	hypothetical	291:302	arg1	C2orf7					344:349	C2orf7	344:349	C2orf7	344:349	The present study reported the isolation and characterization of a novel human secreted protein, named as hPAP21 (human protease-associated domain-containing protein, 21 kDa), encoded by the hypothetical gene chromosome 2 open reading frame 7 (C2orf7) that contains signal peptide in its N-terminus, without transmembrane domain, except for PA domain in its middle.
15498570	3	52	dep	extracellular	681:693	arg1	kDa					699:701	30 kDa	696:701	30 kDa	696:701	However, the molecular weights, whatever intracellular (28 kDa) or extracellular (30 kDa) forms, are larger than that of the prediction.
15498570	4	53	theme	PNGase	859:864	arg1	F					866:866	PNGase F	859:866	PNGase F (PNG F)	859:874	To define whether the glycosylation was important process for its secretion, endoglycosidase H (Endo H) and PNGase F (PNG F) were employed to evaluate the effect of glycosylation types on secretion of hPAP21.
15498570	4	53	theme	PNGase	859:864	arg1	F					873:873	PNG F	869:873	PNG F	869:873	To define whether the glycosylation was important process for its secretion, endoglycosidase H (Endo H) and PNGase F (PNG F) were employed to evaluate the effect of glycosylation types on secretion of hPAP21.
15498570	1	54	theme	gene	304:307	arg1	frame					335:339	the hypothetical gene chromosome 2 open reading frame 7	287:341	the hypothetical gene chromosome 2 open reading frame 7 (C2orf7) that contains signal peptide in its N-terminus	287:397	The present study reported the isolation and characterization of a novel human secreted protein, named as hPAP21 (human protease-associated domain-containing protein, 21 kDa), encoded by the hypothetical gene chromosome 2 open reading frame 7 (C2orf7) that contains signal peptide in its N-terminus, without transmembrane domain, except for PA domain in its middle.
15498570	1	54	theme	gene	304:307	arg1	C2orf7					344:349	C2orf7	344:349	C2orf7	344:349	The present study reported the isolation and characterization of a novel human secreted protein, named as hPAP21 (human protease-associated domain-containing protein, 21 kDa), encoded by the hypothetical gene chromosome 2 open reading frame 7 (C2orf7) that contains signal peptide in its N-terminus, without transmembrane domain, except for PA domain in its middle.
15498570	3	55	theme	molecular	627:635	arg1	weights					637:643	the molecular weights	623:643	the molecular weights	623:643	However, the molecular weights, whatever intracellular (28 kDa) or extracellular (30 kDa) forms, are larger than that of the prediction.
15498570	3	55	theme	molecular	627:635	arg1	larger					715:720	larger	715:720	larger	715:720	However, the molecular weights, whatever intracellular (28 kDa) or extracellular (30 kDa) forms, are larger than that of the prediction.
15498570	4	56	theme	hPAP21	952:957	arg1	secretion					939:947	secretion	939:947	secretion of hPAP21	939:957	To define whether the glycosylation was important process for its secretion, endoglycosidase H (Endo H) and PNGase F (PNG F) were employed to evaluate the effect of glycosylation types on secretion of hPAP21.
15498570	2	57	theme	tagged	514:519	arg1	hPAP21					521:526	the c-Myc tagged hPAP21	504:526	the c-Myc tagged hPAP21	504:526	Western blotting assay indicated that the c-Myc tagged hPAP21 could be secreted into culture medium in the transfected Chinese hamster ovary cells.
15498570	0	58	theme	human	63:67	arg1	hPAP21					92:97	hPAP21	92:97	hPAP21	92:97	N-glycosylation is required for efficient secretion of a novel human secreted glycoprotein, hPAP21.
15498570	0	58	theme	human	63:67	arg1	glycoprotein					78:89	a novel human secreted glycoprotein	55:89	a novel human secreted glycoprotein	55:89	N-glycosylation is required for efficient secretion of a novel human secreted glycoprotein, hPAP21.
15498570	6	59	theme	site-directed	1243:1255	arg1	mutagenesis					1257:1267	site-directed mutagenesis	1243:1267	site-directed mutagenesis assay	1243:1273	Furthermore, N-glycosylation of Asn171 was confirmed as potential crucial process for the secretory protein via site-directed mutagenesis assay.
15498570	6	60	gly	N-glycosylation	1144:1158	arg1	Asn171					1163:1168	Asn171	1163:1168	Asn171	1163:1168	Furthermore, N-glycosylation of Asn171 was confirmed as potential crucial process for the secretory protein via site-directed mutagenesis assay.
15498570	1	61	contain	contains	357:364	arg2	peptide					373:379	signal peptide	366:379	signal peptide in its N-terminus	366:397	The present study reported the isolation and characterization of a novel human secreted protein, named as hPAP21 (human protease-associated domain-containing protein, 21 kDa), encoded by the hypothetical gene chromosome 2 open reading frame 7 (C2orf7) that contains signal peptide in its N-terminus, without transmembrane domain, except for PA domain in its middle.
15498570	1	61	contain	contains	357:364	arg1	frame					335:339	the hypothetical gene chromosome 2 open reading frame 7	287:341	the hypothetical gene chromosome 2 open reading frame 7 (C2orf7) that contains signal peptide in its N-terminus	287:397	The present study reported the isolation and characterization of a novel human secreted protein, named as hPAP21 (human protease-associated domain-containing protein, 21 kDa), encoded by the hypothetical gene chromosome 2 open reading frame 7 (C2orf7) that contains signal peptide in its N-terminus, without transmembrane domain, except for PA domain in its middle.
15498570	1	61	contain	contains	357:364	arg1	C2orf7					344:349	C2orf7	344:349	C2orf7	344:349	The present study reported the isolation and characterization of a novel human secreted protein, named as hPAP21 (human protease-associated domain-containing protein, 21 kDa), encoded by the hypothetical gene chromosome 2 open reading frame 7 (C2orf7) that contains signal peptide in its N-terminus, without transmembrane domain, except for PA domain in its middle.
15498570	1	62	theme	human	214:218	arg1	protein					258:264	human protease-associated domain-containing protein	214:264	human protease-associated domain-containing protein	214:264	The present study reported the isolation and characterization of a novel human secreted protein, named as hPAP21 (human protease-associated domain-containing protein, 21 kDa), encoded by the hypothetical gene chromosome 2 open reading frame 7 (C2orf7) that contains signal peptide in its N-terminus, without transmembrane domain, except for PA domain in its middle.
15498570	1	62	theme	human	214:218	arg1	kDa					270:272	21 kDa	267:272	21 kDa	267:272	The present study reported the isolation and characterization of a novel human secreted protein, named as hPAP21 (human protease-associated domain-containing protein, 21 kDa), encoded by the hypothetical gene chromosome 2 open reading frame 7 (C2orf7) that contains signal peptide in its N-terminus, without transmembrane domain, except for PA domain in its middle.
15498570	0	63	theme	novel	57:61	arg1	hPAP21					92:97	hPAP21	92:97	hPAP21	92:97	N-glycosylation is required for efficient secretion of a novel human secreted glycoprotein, hPAP21.
15498570	0	63	theme	novel	57:61	arg1	glycoprotein					78:89	a novel human secreted glycoprotein	55:89	a novel human secreted glycoprotein	55:89	N-glycosylation is required for efficient secretion of a novel human secreted glycoprotein, hPAP21.
15498570	1	64	theme	chromosome	309:318	arg1	frame					335:339	the hypothetical gene chromosome 2 open reading frame 7	287:341	the hypothetical gene chromosome 2 open reading frame 7 (C2orf7) that contains signal peptide in its N-terminus	287:397	The present study reported the isolation and characterization of a novel human secreted protein, named as hPAP21 (human protease-associated domain-containing protein, 21 kDa), encoded by the hypothetical gene chromosome 2 open reading frame 7 (C2orf7) that contains signal peptide in its N-terminus, without transmembrane domain, except for PA domain in its middle.
15498570	1	64	theme	chromosome	309:318	arg1	C2orf7					344:349	C2orf7	344:349	C2orf7	344:349	The present study reported the isolation and characterization of a novel human secreted protein, named as hPAP21 (human protease-associated domain-containing protein, 21 kDa), encoded by the hypothetical gene chromosome 2 open reading frame 7 (C2orf7) that contains signal peptide in its N-terminus, without transmembrane domain, except for PA domain in its middle.
15498570	3	65	theme	intracellular	655:667	arg1	forms					704:708	intracellular (28 kDa) or extracellular (30 kDa) forms	655:708	intracellular (28 kDa) or extracellular (30 kDa) forms	655:708	However, the molecular weights, whatever intracellular (28 kDa) or extracellular (30 kDa) forms, are larger than that of the prediction.
15498570	4	66	theme	types	930:934	arg1	effect					906:911	the effect	902:911	the effect of glycosylation types on secretion of hPAP21	902:957	To define whether the glycosylation was important process for its secretion, endoglycosidase H (Endo H) and PNGase F (PNG F) were employed to evaluate the effect of glycosylation types on secretion of hPAP21.
15498570	1	67	theme	protease-associated	220:238	arg1	protein					258:264	human protease-associated domain-containing protein	214:264	human protease-associated domain-containing protein	214:264	The present study reported the isolation and characterization of a novel human secreted protein, named as hPAP21 (human protease-associated domain-containing protein, 21 kDa), encoded by the hypothetical gene chromosome 2 open reading frame 7 (C2orf7) that contains signal peptide in its N-terminus, without transmembrane domain, except for PA domain in its middle.
15498570	1	67	theme	protease-associated	220:238	arg1	kDa					270:272	21 kDa	267:272	21 kDa	267:272	The present study reported the isolation and characterization of a novel human secreted protein, named as hPAP21 (human protease-associated domain-containing protein, 21 kDa), encoded by the hypothetical gene chromosome 2 open reading frame 7 (C2orf7) that contains signal peptide in its N-terminus, without transmembrane domain, except for PA domain in its middle.
17525160	4	0	theme	wild-type	506:514	arg1	hCTR1					516:520	wild-type hCTR1	506:520	wild-type hCTR1	506:520	We show that in mammalian cells the N15Q mutant protein trafficked to the plasma membrane and mediated copper uptake at 75% of the rate of wild-type hCTR1.
17525160	10	1	theme	hCTR1	1167:1171	arg1	Expression					1143:1152	Expression	1143:1152	Expression of wild-type hCTR1 in mutant Chinese hamster ovary cells that were unable to initiate O-glycosylation	1143:1254	Expression of wild-type hCTR1 in mutant Chinese hamster ovary cells that were unable to initiate O-glycosylation also resulted in hCTR1 cleavage to produce the 17-kDa polypeptide.
17525160	8	2	theme	alanine	924:930	arg1	substitutions					932:944	alanine substitutions	924:944	alanine substitutions at Thr-27	924:954	Expression of alanine substitutions at Thr-27 resulted in proteolytic cleavage of hCTR1 on the carboxyl side of the T27A mutations.
17525160	5	3	theme	O-linked	599:606	arg1	polysaccharides					608:622	O-linked polysaccharides	599:622	O-linked polysaccharides	599:622	We demonstrate that the extracellular amino terminus of hCTR1 also contains O-linked polysaccharides.
17525160	0	4	link	O-linked	0:7	arg1	glycosylation					9:21	O-linked glycosylation	0:21	O-linked glycosylation at threonine 27	0:37	O-linked glycosylation at threonine 27 protects the copper transporter hCTR1 from proteolytic cleavage in mammalian cells.
17525160	5	5	theme	amino	561:565	arg1	terminus					567:574	the extracellular amino terminus	543:574	the extracellular amino terminus of hCTR1	543:583	We demonstrate that the extracellular amino terminus of hCTR1 also contains O-linked polysaccharides.
17525160	7	6	theme	substitution	799:810	arg1	mutants					812:818	alanine substitution mutants	791:818	alanine substitution mutants	791:818	Expression of amino-terminal truncations and alanine substitution mutants of hCTR1 in HEK293 and MDCK cells localized the site of O-linked glycosylation to Thr-27.
17525160	7	7	from	Expression	746:755	arg1	cells					848:852	HEK293 and MDCK cells	832:852	cells	848:852	Expression of amino-terminal truncations and alanine substitution mutants of hCTR1 in HEK293 and MDCK cells localized the site of O-linked glycosylation to Thr-27.
17525160	6	8	theme	protein	726:732	arg1	mass					697:700	the apparent mass	684:700	the apparent mass of hCTR1 or N15Q mutant protein	684:732	Glycosidase treatment that removed O-linked sugars reduced the apparent mass of hCTR1 or N15Q mutant protein by 1-2 kDa.
17525160	8	9	theme	proteolytic	968:978	arg1	cleavage					980:987	proteolytic cleavage	968:987	proteolytic cleavage of hCTR1 on the carboxyl side of the T27A mutations	968:1039	Expression of alanine substitutions at Thr-27 resulted in proteolytic cleavage of hCTR1 on the carboxyl side of the T27A mutations.
17525160	7	10	theme	amino-terminal	760:773	arg1	truncations					775:785	amino-terminal truncations	760:785	amino-terminal truncations	760:785	Expression of amino-terminal truncations and alanine substitution mutants of hCTR1 in HEK293 and MDCK cells localized the site of O-linked glycosylation to Thr-27.
17525160	11	11	theme	17-kDa	1327:1332	arg1	located					1356:1362	located	1356:1362	located	1356:1362	The 17-kDa hCTR1 polypeptide was located in the plasma membrane and mediated copper uptake at about 50% that of the rate of wild-type hCTR1.
17525160	11	11	theme	17-kDa	1327:1332	arg1	polypeptide					1340:1350	The 17-kDa hCTR1 polypeptide	1323:1350	The 17-kDa hCTR1 polypeptide	1323:1350	The 17-kDa hCTR1 polypeptide was located in the plasma membrane and mediated copper uptake at about 50% that of the rate of wild-type hCTR1.
17525160	4	12	theme	N15Q	403:406	arg1	protein					415:421	the N15Q mutant protein	399:421	the N15Q mutant protein	399:421	We show that in mammalian cells the N15Q mutant protein trafficked to the plasma membrane and mediated copper uptake at 75% of the rate of wild-type hCTR1.
17525160	12	13	theme	remaining	1663:1671	arg1	polypeptide					1673:1683	the remaining polypeptide	1659:1683	the remaining polypeptide	1659:1683	Thus, O-linked glycosylation at Thr-27 is necessary to prevent proteolytic cleavage that removes half of the extracellular amino terminus of hCTR1 and significantly impairs transport activity of the remaining polypeptide.
17525160	12	14	theme	proteolytic	1527:1537	arg1	cleavage					1539:1546	proteolytic cleavage	1527:1546	proteolytic cleavage that removes half of the extracellular amino terminus of hCTR1 and significantly impairs transport activity of the remaining polypeptide	1527:1683	Thus, O-linked glycosylation at Thr-27 is necessary to prevent proteolytic cleavage that removes half of the extracellular amino terminus of hCTR1 and significantly impairs transport activity of the remaining polypeptide.
17525160	10	15	theme	hamster	1191:1197	arg1	cells					1205:1209	mutant Chinese hamster ovary cells	1176:1209	mutant Chinese hamster ovary cells that were unable to initiate O-glycosylation	1176:1254	Expression of wild-type hCTR1 in mutant Chinese hamster ovary cells that were unable to initiate O-glycosylation also resulted in hCTR1 cleavage to produce the 17-kDa polypeptide.
17525160	2	16	theme	hCTR1	221:225	arg1	antibodies					227:236	hCTR1 antibodies	221:236	hCTR1 antibodies	221:236	hCTR1 antibodies recognize multiple bands in SDS-PAGE centered at 35 kDa.
17525160	6	17	theme	Glycosidase	625:635	arg1	treatment					637:645	Glycosidase treatment	625:645	Glycosidase treatment that removed O-linked sugars	625:674	Glycosidase treatment that removed O-linked sugars reduced the apparent mass of hCTR1 or N15Q mutant protein by 1-2 kDa.
17525160	0	18	from	cleavage	94:101	arg1	cells					116:120	mammalian cells	106:120	mammalian cells	106:120	O-linked glycosylation at threonine 27 protects the copper transporter hCTR1 from proteolytic cleavage in mammalian cells.
17525160	12	19	theme	O-linked	1470:1477	arg1	glycosylation					1479:1491	O-linked glycosylation	1470:1491	O-linked glycosylation at Thr-27	1470:1501	Thus, O-linked glycosylation at Thr-27 is necessary to prevent proteolytic cleavage that removes half of the extracellular amino terminus of hCTR1 and significantly impairs transport activity of the remaining polypeptide.
17525160	10	20	theme	mutant	1176:1181	arg1	cells					1205:1209	mutant Chinese hamster ovary cells	1176:1209	mutant Chinese hamster ovary cells that were unable to initiate O-glycosylation	1176:1254	Expression of wild-type hCTR1 in mutant Chinese hamster ovary cells that were unable to initiate O-glycosylation also resulted in hCTR1 cleavage to produce the 17-kDa polypeptide.
17525160	0	21	theme	transporter	59:69	arg1	hCTR1					71:75	the copper transporter hCTR1	48:75	the copper transporter hCTR1	48:75	O-linked glycosylation at threonine 27 protects the copper transporter hCTR1 from proteolytic cleavage in mammalian cells.
17525160	12	22	gly	glycosylation	1479:1491	arg1	Thr-27					1496:1501	Thr-27	1496:1501	Thr-27	1496:1501	Thus, O-linked glycosylation at Thr-27 is necessary to prevent proteolytic cleavage that removes half of the extracellular amino terminus of hCTR1 and significantly impairs transport activity of the remaining polypeptide.
17525160	12	22	gly	glycosylation	1479:1491	arg2	Thr-27					1496:1501	Thr-27	1496:1501	Thr-27	1496:1501	Thus, O-linked glycosylation at Thr-27 is necessary to prevent proteolytic cleavage that removes half of the extracellular amino terminus of hCTR1 and significantly impairs transport activity of the remaining polypeptide.
17525160	1	23	theme	uptake	146:151	arg1	hCTR1					162:166	hCTR1	162:166	hCTR1	162:166	The major human copper uptake protein, hCTR1, has 190 amino acids and a predicted mass of 21 kDa.
17525160	1	23	theme	uptake	146:151	arg1	protein					153:159	The major human copper uptake protein	123:159	The major human copper uptake protein	123:159	The major human copper uptake protein, hCTR1, has 190 amino acids and a predicted mass of 21 kDa.
17525160	12	24	theme	transport	1637:1645	arg1	activity					1647:1654	transport activity	1637:1654	transport activity of the remaining polypeptide	1637:1683	Thus, O-linked glycosylation at Thr-27 is necessary to prevent proteolytic cleavage that removes half of the extracellular amino terminus of hCTR1 and significantly impairs transport activity of the remaining polypeptide.
17525160	4	25	theme	plasma	441:446	arg1	membrane					448:455	the plasma membrane	437:455	the plasma membrane	437:455	We show that in mammalian cells the N15Q mutant protein trafficked to the plasma membrane and mediated copper uptake at 75% of the rate of wild-type hCTR1.
17525160	11	26	dep	%	1425:1425	arg1	that					1427:1430	that	1427:1430	that	1427:1430	The 17-kDa hCTR1 polypeptide was located in the plasma membrane and mediated copper uptake at about 50% that of the rate of wild-type hCTR1.
17525160	3	27	theme	mass	318:321	arg1	Part					295:298	Part	295:298	Part of this increased mass	295:321	Part of this increased mass is due to N-linked glycosylation at Asn-15.
17525160	11	28	theme	wild-type	1447:1455	arg1	hCTR1					1457:1461	wild-type hCTR1	1447:1461	wild-type hCTR1	1447:1461	The 17-kDa hCTR1 polypeptide was located in the plasma membrane and mediated copper uptake at about 50% that of the rate of wild-type hCTR1.
17525160	6	29	link	O-linked	660:667	arg1	sugars					669:674	O-linked sugars	660:674	O-linked sugars	660:674	Glycosidase treatment that removed O-linked sugars reduced the apparent mass of hCTR1 or N15Q mutant protein by 1-2 kDa.
17525160	12	30	theme	hCTR1	1605:1609	arg1	terminus					1593:1600	the extracellular amino terminus	1569:1600	the extracellular amino terminus of hCTR1	1569:1609	Thus, O-linked glycosylation at Thr-27 is necessary to prevent proteolytic cleavage that removes half of the extracellular amino terminus of hCTR1 and significantly impairs transport activity of the remaining polypeptide.
17525160	1	31	theme	human	133:137	arg1	hCTR1					162:166	hCTR1	162:166	hCTR1	162:166	The major human copper uptake protein, hCTR1, has 190 amino acids and a predicted mass of 21 kDa.
17525160	1	31	theme	human	133:137	arg1	protein					153:159	The major human copper uptake protein	123:159	The major human copper uptake protein	123:159	The major human copper uptake protein, hCTR1, has 190 amino acids and a predicted mass of 21 kDa.
17525160	6	32	theme	O-linked	660:667	arg1	sugars					669:674	O-linked sugars	660:674	O-linked sugars	660:674	Glycosidase treatment that removed O-linked sugars reduced the apparent mass of hCTR1 or N15Q mutant protein by 1-2 kDa.
17525160	0	33	theme	mammalian	106:114	arg1	cells					116:120	mammalian cells	106:120	mammalian cells	106:120	O-linked glycosylation at threonine 27 protects the copper transporter hCTR1 from proteolytic cleavage in mammalian cells.
17525160	8	34	theme	carboxyl	1005:1012	arg1	side					1014:1017	the carboxyl side	1001:1017	the carboxyl side of the T27A mutations	1001:1039	Expression of alanine substitutions at Thr-27 resulted in proteolytic cleavage of hCTR1 on the carboxyl side of the T27A mutations.
17525160	7	35	theme	glycosylation	885:897	arg1	glycosylation					885:897	O-linked glycosylation	876:897	O-linked glycosylation	876:897	Expression of amino-terminal truncations and alanine substitution mutants of hCTR1 in HEK293 and MDCK cells localized the site of O-linked glycosylation to Thr-27.
17525160	7	35	theme	glycosylation	885:897	arg1	site					868:871	the site	864:871	the site of O-linked glycosylation	864:897	Expression of amino-terminal truncations and alanine substitution mutants of hCTR1 in HEK293 and MDCK cells localized the site of O-linked glycosylation to Thr-27.
17525160	3	36	theme	N-linked	333:340	arg1	glycosylation					342:354	N-linked glycosylation	333:354	N-linked glycosylation	333:354	Part of this increased mass is due to N-linked glycosylation at Asn-15.
17525160	0	37	theme	O-linked	0:7	arg1	glycosylation					9:21	O-linked glycosylation	0:21	O-linked glycosylation at threonine 27	0:37	O-linked glycosylation at threonine 27 protects the copper transporter hCTR1 from proteolytic cleavage in mammalian cells.
17525160	12	38	theme	extracellular	1573:1585	arg1	terminus					1593:1600	the extracellular amino terminus	1569:1600	the extracellular amino terminus of hCTR1	1569:1609	Thus, O-linked glycosylation at Thr-27 is necessary to prevent proteolytic cleavage that removes half of the extracellular amino terminus of hCTR1 and significantly impairs transport activity of the remaining polypeptide.
17525160	10	39	theme	hCTR1	1273:1277	arg1	cleavage					1279:1286	hCTR1 cleavage	1273:1286	hCTR1 cleavage	1273:1286	Expression of wild-type hCTR1 in mutant Chinese hamster ovary cells that were unable to initiate O-glycosylation also resulted in hCTR1 cleavage to produce the 17-kDa polypeptide.
17525160	8	40	theme	T27A	1026:1029	arg1	mutations					1031:1039	the T27A mutations	1022:1039	the T27A mutations	1022:1039	Expression of alanine substitutions at Thr-27 resulted in proteolytic cleavage of hCTR1 on the carboxyl side of the T27A mutations.
17525160	12	41	theme	terminus	1593:1600	arg1	half					1561:1564	half	1561:1564	half of the extracellular amino terminus of hCTR1	1561:1609	Thus, O-linked glycosylation at Thr-27 is necessary to prevent proteolytic cleavage that removes half of the extracellular amino terminus of hCTR1 and significantly impairs transport activity of the remaining polypeptide.
17525160	8	42	from	Expression	910:919	arg1	Thr-27					949:954	Thr-27	949:954	Thr-27	949:954	Expression of alanine substitutions at Thr-27 resulted in proteolytic cleavage of hCTR1 on the carboxyl side of the T27A mutations.
17525160	1	43	contain	has	169:171	arg2	acids					183:187	190 amino acids	173:187	190 amino acids	173:187	The major human copper uptake protein, hCTR1, has 190 amino acids and a predicted mass of 21 kDa.
17525160	1	43	contain	has	169:171	arg1	protein					153:159	The major human copper uptake protein	123:159	The major human copper uptake protein	123:159	The major human copper uptake protein, hCTR1, has 190 amino acids and a predicted mass of 21 kDa.
17525160	1	43	contain	has	169:171	arg1	hCTR1					162:166	hCTR1	162:166	hCTR1	162:166	The major human copper uptake protein, hCTR1, has 190 amino acids and a predicted mass of 21 kDa.
17525160	1	43	contain	has	169:171	arg2	mass					205:208	a predicted mass	193:208	a predicted mass of 21 kDa	193:218	The major human copper uptake protein, hCTR1, has 190 amino acids and a predicted mass of 21 kDa.
17525160	9	44	theme	17-kDa	1067:1072	arg1	polypeptide					1074:1084	a 17-kDa polypeptide	1065:1084	a 17-kDa polypeptide missing approximately the first 30 amino acids of hCTR1	1065:1140	This cleavage produced a 17-kDa polypeptide missing approximately the first 30 amino acids of hCTR1.
17525160	0	45	gly	glycosylation	9:21	arg1	threonine					26:34	threonine 27	26:37	threonine 27	26:37	O-linked glycosylation at threonine 27 protects the copper transporter hCTR1 from proteolytic cleavage in mammalian cells.
17525160	0	45	gly	glycosylation	9:21	arg2	threonine					26:34	threonine 27	26:37	threonine 27	26:37	O-linked glycosylation at threonine 27 protects the copper transporter hCTR1 from proteolytic cleavage in mammalian cells.
17525160	4	46	theme	copper	470:475	arg1	uptake					477:482	copper uptake	470:482	copper uptake	470:482	We show that in mammalian cells the N15Q mutant protein trafficked to the plasma membrane and mediated copper uptake at 75% of the rate of wild-type hCTR1.
17525160	1	47	theme	predicted	195:203	arg1	mass					205:208	a predicted mass	193:208	a predicted mass of 21 kDa	193:218	The major human copper uptake protein, hCTR1, has 190 amino acids and a predicted mass of 21 kDa.
17525160	6	48	theme	N15Q	714:717	arg1	protein					726:732	N15Q mutant protein	714:732	N15Q mutant protein	714:732	Glycosidase treatment that removed O-linked sugars reduced the apparent mass of hCTR1 or N15Q mutant protein by 1-2 kDa.
17525160	7	49	gly	glycosylation	885:897	arg2	site					868:871	the site	864:871	the site of O-linked glycosylation	864:897	Expression of amino-terminal truncations and alanine substitution mutants of hCTR1 in HEK293 and MDCK cells localized the site of O-linked glycosylation to Thr-27.
17525160	7	49	gly	glycosylation	885:897	arg2	glycosylation					885:897	O-linked glycosylation	876:897	O-linked glycosylation	876:897	Expression of amino-terminal truncations and alanine substitution mutants of hCTR1 in HEK293 and MDCK cells localized the site of O-linked glycosylation to Thr-27.
17525160	6	50	theme	apparent	688:695	arg1	mass					697:700	the apparent mass	684:700	the apparent mass of hCTR1 or N15Q mutant protein	684:732	Glycosidase treatment that removed O-linked sugars reduced the apparent mass of hCTR1 or N15Q mutant protein by 1-2 kDa.
17525160	11	51	theme	hCTR1	1334:1338	arg1	located					1356:1362	located	1356:1362	located	1356:1362	The 17-kDa hCTR1 polypeptide was located in the plasma membrane and mediated copper uptake at about 50% that of the rate of wild-type hCTR1.
17525160	11	51	theme	hCTR1	1334:1338	arg1	polypeptide					1340:1350	The 17-kDa hCTR1 polypeptide	1323:1350	The 17-kDa hCTR1 polypeptide	1323:1350	The 17-kDa hCTR1 polypeptide was located in the plasma membrane and mediated copper uptake at about 50% that of the rate of wild-type hCTR1.
17525160	5	52	theme	hCTR1	579:583	arg1	terminus					567:574	the extracellular amino terminus	543:574	the extracellular amino terminus of hCTR1	543:583	We demonstrate that the extracellular amino terminus of hCTR1 also contains O-linked polysaccharides.
17525160	7	53	theme	MDCK	843:846	arg1	cells					848:852	HEK293 and MDCK cells	832:852	cells	848:852	Expression of amino-terminal truncations and alanine substitution mutants of hCTR1 in HEK293 and MDCK cells localized the site of O-linked glycosylation to Thr-27.
17525160	1	54	theme	kDa	216:218	arg1	acids					183:187	190 amino acids	173:187	190 amino acids	173:187	The major human copper uptake protein, hCTR1, has 190 amino acids and a predicted mass of 21 kDa.
17525160	1	54	theme	kDa	216:218	arg1	mass					205:208	a predicted mass	193:208	a predicted mass of 21 kDa	193:218	The major human copper uptake protein, hCTR1, has 190 amino acids and a predicted mass of 21 kDa.
17525160	8	55	theme	substitutions	932:944	arg1	Expression					910:919	Expression	910:919	Expression of alanine substitutions at Thr-27	910:954	Expression of alanine substitutions at Thr-27 resulted in proteolytic cleavage of hCTR1 on the carboxyl side of the T27A mutations.
17525160	11	56	theme	plasma	1371:1376	arg1	membrane					1378:1385	the plasma membrane	1367:1385	the plasma membrane	1367:1385	The 17-kDa hCTR1 polypeptide was located in the plasma membrane and mediated copper uptake at about 50% that of the rate of wild-type hCTR1.
17525160	9	57	theme	hCTR1	1136:1140	arg1	acids					1127:1131	approximately the first 30 amino acids	1094:1131	approximately the first 30 amino acids of hCTR1	1094:1140	This cleavage produced a 17-kDa polypeptide missing approximately the first 30 amino acids of hCTR1.
17525160	7	58	theme	HEK293	832:837	arg1	cells					848:852	HEK293 and MDCK cells	832:852	cells	848:852	Expression of amino-terminal truncations and alanine substitution mutants of hCTR1 in HEK293 and MDCK cells localized the site of O-linked glycosylation to Thr-27.
17525160	10	59	theme	wild-type	1157:1165	arg1	hCTR1					1167:1171	wild-type hCTR1	1157:1171	wild-type hCTR1	1157:1171	Expression of wild-type hCTR1 in mutant Chinese hamster ovary cells that were unable to initiate O-glycosylation also resulted in hCTR1 cleavage to produce the 17-kDa polypeptide.
17525160	4	60	theme	hCTR1	516:520	arg1	rate					498:501	the rate	494:501	the rate of wild-type hCTR1	494:520	We show that in mammalian cells the N15Q mutant protein trafficked to the plasma membrane and mediated copper uptake at 75% of the rate of wild-type hCTR1.
17525160	5	61	theme	extracellular	547:559	arg1	terminus					567:574	the extracellular amino terminus	543:574	the extracellular amino terminus of hCTR1	543:583	We demonstrate that the extracellular amino terminus of hCTR1 also contains O-linked polysaccharides.
17525160	2	62	theme	multiple	248:255	arg1	bands					257:261	multiple bands	248:261	multiple bands	248:261	hCTR1 antibodies recognize multiple bands in SDS-PAGE centered at 35 kDa.
17525160	7	63	theme	hCTR1	823:827	arg1	mutants					812:818	alanine substitution mutants	791:818	alanine substitution mutants	791:818	Expression of amino-terminal truncations and alanine substitution mutants of hCTR1 in HEK293 and MDCK cells localized the site of O-linked glycosylation to Thr-27.
17525160	7	63	theme	hCTR1	823:827	arg1	truncations					775:785	amino-terminal truncations	760:785	amino-terminal truncations	760:785	Expression of amino-terminal truncations and alanine substitution mutants of hCTR1 in HEK293 and MDCK cells localized the site of O-linked glycosylation to Thr-27.
17525160	7	64	theme	mutants	812:818	arg1	Expression					746:755	Expression	746:755	Expression of amino-terminal truncations and alanine substitution mutants of hCTR1 in HEK293 and MDCK cells	746:852	Expression of amino-terminal truncations and alanine substitution mutants of hCTR1 in HEK293 and MDCK cells localized the site of O-linked glycosylation to Thr-27.
17525160	6	65	theme	mutant	719:724	arg1	protein					726:732	N15Q mutant protein	714:732	N15Q mutant protein	714:732	Glycosidase treatment that removed O-linked sugars reduced the apparent mass of hCTR1 or N15Q mutant protein by 1-2 kDa.
17525160	7	66	theme	alanine	791:797	arg1	mutants					812:818	alanine substitution mutants	791:818	alanine substitution mutants	791:818	Expression of amino-terminal truncations and alanine substitution mutants of hCTR1 in HEK293 and MDCK cells localized the site of O-linked glycosylation to Thr-27.
17525160	1	67	theme	amino	177:181	arg1	acids					183:187	190 amino acids	173:187	190 amino acids	173:187	The major human copper uptake protein, hCTR1, has 190 amino acids and a predicted mass of 21 kDa.
17525160	10	68	from	Expression	1143:1152	arg1	cells					1205:1209	mutant Chinese hamster ovary cells	1176:1209	mutant Chinese hamster ovary cells that were unable to initiate O-glycosylation	1176:1254	Expression of wild-type hCTR1 in mutant Chinese hamster ovary cells that were unable to initiate O-glycosylation also resulted in hCTR1 cleavage to produce the 17-kDa polypeptide.
17525160	7	69	theme	truncations	775:785	arg1	Expression					746:755	Expression	746:755	Expression of amino-terminal truncations and alanine substitution mutants of hCTR1 in HEK293 and MDCK cells	746:852	Expression of amino-terminal truncations and alanine substitution mutants of hCTR1 in HEK293 and MDCK cells localized the site of O-linked glycosylation to Thr-27.
17525160	4	70	theme	mutant	408:413	arg1	protein					415:421	the N15Q mutant protein	399:421	the N15Q mutant protein	399:421	We show that in mammalian cells the N15Q mutant protein trafficked to the plasma membrane and mediated copper uptake at 75% of the rate of wild-type hCTR1.
17525160	11	71	from	membrane	1378:1385	arg1	located					1356:1362	located	1356:1362	located	1356:1362	The 17-kDa hCTR1 polypeptide was located in the plasma membrane and mediated copper uptake at about 50% that of the rate of wild-type hCTR1.
17525160	11	71	from	membrane	1378:1385	arg1	polypeptide					1340:1350	The 17-kDa hCTR1 polypeptide	1323:1350	The 17-kDa hCTR1 polypeptide	1323:1350	The 17-kDa hCTR1 polypeptide was located in the plasma membrane and mediated copper uptake at about 50% that of the rate of wild-type hCTR1.
17525160	10	72	theme	ovary	1199:1203	arg1	cells					1205:1209	mutant Chinese hamster ovary cells	1176:1209	mutant Chinese hamster ovary cells that were unable to initiate O-glycosylation	1176:1254	Expression of wild-type hCTR1 in mutant Chinese hamster ovary cells that were unable to initiate O-glycosylation also resulted in hCTR1 cleavage to produce the 17-kDa polypeptide.
17525160	11	73	located	located	1356:1362	arg2	located					1356:1362	located	1356:1362	located	1356:1362	The 17-kDa hCTR1 polypeptide was located in the plasma membrane and mediated copper uptake at about 50% that of the rate of wild-type hCTR1.
17525160	11	73	located	located	1356:1362	arg2	polypeptide					1340:1350	The 17-kDa hCTR1 polypeptide	1323:1350	The 17-kDa hCTR1 polypeptide	1323:1350	The 17-kDa hCTR1 polypeptide was located in the plasma membrane and mediated copper uptake at about 50% that of the rate of wild-type hCTR1.
17525160	11	73	located	located	1356:1362	arg1	membrane					1378:1385	the plasma membrane	1367:1385	the plasma membrane	1367:1385	The 17-kDa hCTR1 polypeptide was located in the plasma membrane and mediated copper uptake at about 50% that of the rate of wild-type hCTR1.
17525160	1	74	theme	major	127:131	arg1	hCTR1					162:166	hCTR1	162:166	hCTR1	162:166	The major human copper uptake protein, hCTR1, has 190 amino acids and a predicted mass of 21 kDa.
17525160	1	74	theme	major	127:131	arg1	protein					153:159	The major human copper uptake protein	123:159	The major human copper uptake protein	123:159	The major human copper uptake protein, hCTR1, has 190 amino acids and a predicted mass of 21 kDa.
17525160	4	75	theme	mammalian	383:391	arg1	cells					393:397	mammalian cells	383:397	mammalian cells	383:397	We show that in mammalian cells the N15Q mutant protein trafficked to the plasma membrane and mediated copper uptake at 75% of the rate of wild-type hCTR1.
17525160	10	76	theme	Chinese	1183:1189	arg1	cells					1205:1209	mutant Chinese hamster ovary cells	1176:1209	mutant Chinese hamster ovary cells that were unable to initiate O-glycosylation	1176:1254	Expression of wild-type hCTR1 in mutant Chinese hamster ovary cells that were unable to initiate O-glycosylation also resulted in hCTR1 cleavage to produce the 17-kDa polypeptide.
17525160	7	77	link	O-linked	876:883	arg1	glycosylation					885:897	O-linked glycosylation	876:897	O-linked glycosylation	876:897	Expression of amino-terminal truncations and alanine substitution mutants of hCTR1 in HEK293 and MDCK cells localized the site of O-linked glycosylation to Thr-27.
17525160	11	78	from	located	1356:1362	arg1	membrane					1378:1385	the plasma membrane	1367:1385	the plasma membrane	1367:1385	The 17-kDa hCTR1 polypeptide was located in the plasma membrane and mediated copper uptake at about 50% that of the rate of wild-type hCTR1.
17525160	3	79	link	N-linked	333:340	arg1	glycosylation					342:354	N-linked glycosylation	333:354	N-linked glycosylation	333:354	Part of this increased mass is due to N-linked glycosylation at Asn-15.
17525160	1	80	theme	copper	139:144	arg1	hCTR1					162:166	hCTR1	162:166	hCTR1	162:166	The major human copper uptake protein, hCTR1, has 190 amino acids and a predicted mass of 21 kDa.
17525160	1	80	theme	copper	139:144	arg1	protein					153:159	The major human copper uptake protein	123:159	The major human copper uptake protein	123:159	The major human copper uptake protein, hCTR1, has 190 amino acids and a predicted mass of 21 kDa.
17525160	12	81	theme	polypeptide	1673:1683	arg1	activity					1647:1654	transport activity	1637:1654	transport activity of the remaining polypeptide	1637:1683	Thus, O-linked glycosylation at Thr-27 is necessary to prevent proteolytic cleavage that removes half of the extracellular amino terminus of hCTR1 and significantly impairs transport activity of the remaining polypeptide.
17525160	0	82	from	threonine	26:34	arg1	glycosylation					9:21	O-linked glycosylation	0:21	O-linked glycosylation at threonine 27	0:37	O-linked glycosylation at threonine 27 protects the copper transporter hCTR1 from proteolytic cleavage in mammalian cells.
17525160	11	83	theme	hCTR1	1457:1461	arg1	rate					1439:1442	the rate	1435:1442	the rate of wild-type hCTR1	1435:1461	The 17-kDa hCTR1 polypeptide was located in the plasma membrane and mediated copper uptake at about 50% that of the rate of wild-type hCTR1.
17525160	0	84	theme	proteolytic	82:92	arg1	cleavage					94:101	proteolytic cleavage	82:101	proteolytic cleavage in mammalian cells	82:120	O-linked glycosylation at threonine 27 protects the copper transporter hCTR1 from proteolytic cleavage in mammalian cells.
17525160	3	85	from	Asn-15	359:364	arg1	glycosylation					342:354	N-linked glycosylation	333:354	N-linked glycosylation	333:354	Part of this increased mass is due to N-linked glycosylation at Asn-15.
17525160	8	86	theme	hCTR1	992:996	arg1	cleavage					980:987	proteolytic cleavage	968:987	proteolytic cleavage of hCTR1 on the carboxyl side of the T27A mutations	968:1039	Expression of alanine substitutions at Thr-27 resulted in proteolytic cleavage of hCTR1 on the carboxyl side of the T27A mutations.
17525160	12	87	from	Thr-27	1496:1501	arg1	glycosylation					1479:1491	O-linked glycosylation	1470:1491	O-linked glycosylation at Thr-27	1470:1501	Thus, O-linked glycosylation at Thr-27 is necessary to prevent proteolytic cleavage that removes half of the extracellular amino terminus of hCTR1 and significantly impairs transport activity of the remaining polypeptide.
17525160	11	88	theme	copper	1400:1405	arg1	uptake					1407:1412	copper uptake	1400:1412	copper uptake	1400:1412	The 17-kDa hCTR1 polypeptide was located in the plasma membrane and mediated copper uptake at about 50% that of the rate of wild-type hCTR1.
17525160	3	89	gly	glycosylation	342:354	arg1	Asn-15					359:364	Asn-15	359:364	Asn-15	359:364	Part of this increased mass is due to N-linked glycosylation at Asn-15.
17525160	3	89	gly	glycosylation	342:354	arg2	Asn-15					359:364	Asn-15	359:364	Asn-15	359:364	Part of this increased mass is due to N-linked glycosylation at Asn-15.
17525160	3	90	theme	increased	308:316	arg1	mass					318:321	this increased mass	303:321	this increased mass	303:321	Part of this increased mass is due to N-linked glycosylation at Asn-15.
17525160	5	91	contain	contains	590:597	arg1	terminus					567:574	the extracellular amino terminus	543:574	the extracellular amino terminus of hCTR1	543:583	We demonstrate that the extracellular amino terminus of hCTR1 also contains O-linked polysaccharides.
17525160	5	91	contain	contains	590:597	arg2	polysaccharides					608:622	O-linked polysaccharides	599:622	O-linked polysaccharides	599:622	We demonstrate that the extracellular amino terminus of hCTR1 also contains O-linked polysaccharides.
17525160	12	92	link	O-linked	1470:1477	arg1	glycosylation					1479:1491	O-linked glycosylation	1470:1491	O-linked glycosylation at Thr-27	1470:1501	Thus, O-linked glycosylation at Thr-27 is necessary to prevent proteolytic cleavage that removes half of the extracellular amino terminus of hCTR1 and significantly impairs transport activity of the remaining polypeptide.
17525160	8	93	theme	mutations	1031:1039	arg1	side					1014:1017	the carboxyl side	1001:1017	the carboxyl side of the T27A mutations	1001:1039	Expression of alanine substitutions at Thr-27 resulted in proteolytic cleavage of hCTR1 on the carboxyl side of the T27A mutations.
17525160	7	94	theme	O-linked	876:883	arg1	glycosylation					885:897	O-linked glycosylation	876:897	O-linked glycosylation	876:897	Expression of amino-terminal truncations and alanine substitution mutants of hCTR1 in HEK293 and MDCK cells localized the site of O-linked glycosylation to Thr-27.
17525160	4	95	theme	rate	498:501	arg1	%					489:489	75%	487:489	75% of the rate of wild-type hCTR1	487:520	We show that in mammalian cells the N15Q mutant protein trafficked to the plasma membrane and mediated copper uptake at 75% of the rate of wild-type hCTR1.
17525160	4	95	theme	rate	498:501	arg1	rate					498:501	the rate	494:501	the rate of wild-type hCTR1	494:520	We show that in mammalian cells the N15Q mutant protein trafficked to the plasma membrane and mediated copper uptake at 75% of the rate of wild-type hCTR1.
17525160	5	96	link	O-linked	599:606	arg1	polysaccharides					608:622	O-linked polysaccharides	599:622	O-linked polysaccharides	599:622	We demonstrate that the extracellular amino terminus of hCTR1 also contains O-linked polysaccharides.
17525160	12	97	theme	amino	1587:1591	arg1	terminus					1593:1600	the extracellular amino terminus	1569:1600	the extracellular amino terminus of hCTR1	1569:1609	Thus, O-linked glycosylation at Thr-27 is necessary to prevent proteolytic cleavage that removes half of the extracellular amino terminus of hCTR1 and significantly impairs transport activity of the remaining polypeptide.
17525160	10	98	theme	17-kDa	1303:1308	arg1	polypeptide					1310:1320	the 17-kDa polypeptide	1299:1320	the 17-kDa polypeptide	1299:1320	Expression of wild-type hCTR1 in mutant Chinese hamster ovary cells that were unable to initiate O-glycosylation also resulted in hCTR1 cleavage to produce the 17-kDa polypeptide.
17525160	0	99	theme	copper	52:57	arg1	hCTR1					71:75	the copper transporter hCTR1	48:75	the copper transporter hCTR1	48:75	O-linked glycosylation at threonine 27 protects the copper transporter hCTR1 from proteolytic cleavage in mammalian cells.
17525160	11	100	theme	rate	1439:1442	arg1	rate					1439:1442	the rate	1435:1442	the rate of wild-type hCTR1	1435:1461	The 17-kDa hCTR1 polypeptide was located in the plasma membrane and mediated copper uptake at about 50% that of the rate of wild-type hCTR1.
17525160	11	100	theme	rate	1439:1442	arg1	%					1425:1425	about 50%	1417:1425	about 50% that of the rate of wild-type hCTR1	1417:1461	The 17-kDa hCTR1 polypeptide was located in the plasma membrane and mediated copper uptake at about 50% that of the rate of wild-type hCTR1.
17525160	8	101	from	Thr-27	949:954	arg1	Expression					910:919	Expression	910:919	Expression of alanine substitutions at Thr-27	910:954	Expression of alanine substitutions at Thr-27 resulted in proteolytic cleavage of hCTR1 on the carboxyl side of the T27A mutations.
17525160	8	101	from	Thr-27	949:954	arg1	substitutions					932:944	alanine substitutions	924:944	alanine substitutions at Thr-27	924:954	Expression of alanine substitutions at Thr-27 resulted in proteolytic cleavage of hCTR1 on the carboxyl side of the T27A mutations.
17525160	6	102	theme	hCTR1	705:709	arg1	mass					697:700	the apparent mass	684:700	the apparent mass of hCTR1 or N15Q mutant protein	684:732	Glycosidase treatment that removed O-linked sugars reduced the apparent mass of hCTR1 or N15Q mutant protein by 1-2 kDa.
17525160	9	103	theme	first	1112:1116	arg1	acids					1127:1131	approximately the first 30 amino acids	1094:1131	approximately the first 30 amino acids of hCTR1	1094:1140	This cleavage produced a 17-kDa polypeptide missing approximately the first 30 amino acids of hCTR1.
17525160	8	104	from	cleavage	980:987	arg1	side					1014:1017	the carboxyl side	1001:1017	the carboxyl side of the T27A mutations	1001:1039	Expression of alanine substitutions at Thr-27 resulted in proteolytic cleavage of hCTR1 on the carboxyl side of the T27A mutations.
17525160	9	105	theme	amino	1121:1125	arg1	acids					1127:1131	approximately the first 30 amino acids	1094:1131	approximately the first 30 amino acids of hCTR1	1094:1140	This cleavage produced a 17-kDa polypeptide missing approximately the first 30 amino acids of hCTR1.
12901863	1	0	theme	transporter	133:143	arg1	ABCC6					154:158	ABCC6	154:158	ABCC6 (MRP6)	154:165	Mutations in the gene coding for a human ABC transporter protein, ABCC6 (MRP6), are responsible for the development of pseudoxanthoma elasticum.
12901863	1	0	theme	transporter	133:143	arg1	protein					145:151	a human ABC transporter protein	121:151	a human ABC transporter protein	121:151	Mutations in the gene coding for a human ABC transporter protein, ABCC6 (MRP6), are responsible for the development of pseudoxanthoma elasticum.
12901863	1	1	theme	pseudoxanthoma	207:220	arg1	elasticum					222:230	pseudoxanthoma elasticum	207:230	pseudoxanthoma elasticum	207:230	Mutations in the gene coding for a human ABC transporter protein, ABCC6 (MRP6), are responsible for the development of pseudoxanthoma elasticum.
12901863	0	2	theme	MDCKII	74:79	arg1	cells					81:85	MDCKII cells	74:85	MDCKII cells	74:85	Subcellular localization and N-glycosylation of human ABCC6, expressed in MDCKII cells.
12901863	1	3	theme	elasticum	222:230	arg1	development					192:202	the development	188:202	the development of pseudoxanthoma elasticum	188:230	Mutations in the gene coding for a human ABC transporter protein, ABCC6 (MRP6), are responsible for the development of pseudoxanthoma elasticum.
12901863	3	4	dep	form	506:509	arg1	contrast					472:479	contrast	472:479	contrast	472:479	The human ABCC6 in MDCKII cells was found to be glycosylated, in contrast to the underglycosylated form of the protein, as expressed in Sf9 cells.
12901863	4	5	gly	glycosylation	585:597	arg2	site					599:602	the major glycosylation site	575:602	the major glycosylation site(s) in ABCC6	575:614	In order to localize the major glycosylation site(s) in ABCC6, we applied limited proteolysis on the fully glycosylated and underglycosylated forms, followed by immunodetection with region-specific antibodies for ABCC6.
12901863	4	5	gly	glycosylation	585:597	arg2	s					604:604	s	604:604	s	604:604	In order to localize the major glycosylation site(s) in ABCC6, we applied limited proteolysis on the fully glycosylated and underglycosylated forms, followed by immunodetection with region-specific antibodies for ABCC6.
12901863	5	6	from	located	816:822	arg1	region					856:861	the extracellular N-terminal region	827:861	the extracellular N-terminal region of human ABCC6	827:876	Our results indicate that Asn15, which is located in the extracellular N-terminal region of human ABCC6, is the only N-glycosylation site in this protein.
12901863	6	7	theme	pathological	1095:1106	arg1	variants					1108:1115	the normal and pathological variants	1080:1115	the normal and pathological variants of human ABCC6	1080:1130	The polarized mammalian expression system characterized here provides a useful tool for further examination of routing, glycosylation, and function of the normal and pathological variants of human ABCC6.
12901863	5	8	theme	ABCC6	872:876	arg1	region					856:861	the extracellular N-terminal region	827:861	the extracellular N-terminal region of human ABCC6	827:876	Our results indicate that Asn15, which is located in the extracellular N-terminal region of human ABCC6, is the only N-glycosylation site in this protein.
12901863	2	9	from	transduction	301:312	arg1	cells					346:350	polarized mammalian (MDCKII) cells	317:350	polarized mammalian (MDCKII) cells	317:350	Here, we demonstrate that human ABCC6, when expressed by retroviral transduction in polarized mammalian (MDCKII) cells, is exclusively localized to the basolateral membrane.
12901863	3	10	gly	glycosylated	455:466	arg1	ABCC6					417:421	The human ABCC6	407:421	The human ABCC6 in MDCKII cells	407:437	The human ABCC6 in MDCKII cells was found to be glycosylated, in contrast to the underglycosylated form of the protein, as expressed in Sf9 cells.
12901863	4	11	from	site	599:602	arg1	ABCC6					610:614	ABCC6	610:614	ABCC6	610:614	In order to localize the major glycosylation site(s) in ABCC6, we applied limited proteolysis on the fully glycosylated and underglycosylated forms, followed by immunodetection with region-specific antibodies for ABCC6.
12901863	5	12	theme	N-terminal	845:854	arg1	region					856:861	the extracellular N-terminal region	827:861	the extracellular N-terminal region of human ABCC6	827:876	Our results indicate that Asn15, which is located in the extracellular N-terminal region of human ABCC6, is the only N-glycosylation site in this protein.
12901863	6	13	theme	useful	1001:1006	arg1	tool					1008:1011	a useful tool	999:1011	a useful tool for further examination of routing, glycosylation, and function of the normal and pathological variants of human ABCC6	999:1130	The polarized mammalian expression system characterized here provides a useful tool for further examination of routing, glycosylation, and function of the normal and pathological variants of human ABCC6.
12901863	4	14	theme	underglycosylated	678:694	arg1	forms					696:700	underglycosylated forms	678:700	underglycosylated forms	678:700	In order to localize the major glycosylation site(s) in ABCC6, we applied limited proteolysis on the fully glycosylated and underglycosylated forms, followed by immunodetection with region-specific antibodies for ABCC6.
12901863	4	15	theme	major	579:583	arg1	s					604:604	s	604:604	s	604:604	In order to localize the major glycosylation site(s) in ABCC6, we applied limited proteolysis on the fully glycosylated and underglycosylated forms, followed by immunodetection with region-specific antibodies for ABCC6.
12901863	4	15	theme	major	579:583	arg1	site					599:602	the major glycosylation site	575:602	the major glycosylation site(s) in ABCC6	575:614	In order to localize the major glycosylation site(s) in ABCC6, we applied limited proteolysis on the fully glycosylated and underglycosylated forms, followed by immunodetection with region-specific antibodies for ABCC6.
12901863	6	16	theme	mammalian	943:951	arg1	system					964:969	The polarized mammalian expression system	929:969	The polarized mammalian expression system characterized here	929:988	The polarized mammalian expression system characterized here provides a useful tool for further examination of routing, glycosylation, and function of the normal and pathological variants of human ABCC6.
12901863	5	17	located	located	816:822	arg2	Asn15					800:804	Asn15	800:804	Asn15	800:804	Our results indicate that Asn15, which is located in the extracellular N-terminal region of human ABCC6, is the only N-glycosylation site in this protein.
12901863	5	17	located	located	816:822	arg1	region					856:861	the extracellular N-terminal region	827:861	the extracellular N-terminal region of human ABCC6	827:876	Our results indicate that Asn15, which is located in the extracellular N-terminal region of human ABCC6, is the only N-glycosylation site in this protein.
12901863	5	17	located	located	816:822	arg2	site					907:910	the only N-glycosylation site	882:910	the only N-glycosylation site in this protein	882:926	Our results indicate that Asn15, which is located in the extracellular N-terminal region of human ABCC6, is the only N-glycosylation site in this protein.
12901863	6	18	gly	glycosylation	1049:1061	arg1	variants					1108:1115	the normal and pathological variants	1080:1115	the normal and pathological variants of human ABCC6	1080:1130	The polarized mammalian expression system characterized here provides a useful tool for further examination of routing, glycosylation, and function of the normal and pathological variants of human ABCC6.
12901863	5	19	theme	only	886:889	arg1	site					907:910	the only N-glycosylation site	882:910	the only N-glycosylation site in this protein	882:926	Our results indicate that Asn15, which is located in the extracellular N-terminal region of human ABCC6, is the only N-glycosylation site in this protein.
12901863	5	19	theme	only	886:889	arg1	Asn15					800:804	Asn15	800:804	Asn15	800:804	Our results indicate that Asn15, which is located in the extracellular N-terminal region of human ABCC6, is the only N-glycosylation site in this protein.
12901863	4	20	gly	underglycosylated	678:694	arg1	forms					696:700	underglycosylated forms	678:700	underglycosylated forms	678:700	In order to localize the major glycosylation site(s) in ABCC6, we applied limited proteolysis on the fully glycosylated and underglycosylated forms, followed by immunodetection with region-specific antibodies for ABCC6.
12901863	5	21	from	site	907:910	arg1	protein					920:926	this protein	915:926	this protein	915:926	Our results indicate that Asn15, which is located in the extracellular N-terminal region of human ABCC6, is the only N-glycosylation site in this protein.
12901863	0	22	theme	Subcellular	0:10	arg1	localization					12:23	Subcellular localization	0:23	Subcellular localization	0:23	Subcellular localization and N-glycosylation of human ABCC6, expressed in MDCKII cells.
12901863	4	23	theme	limited	628:634	arg1	proteolysis					636:646	limited proteolysis	628:646	limited proteolysis	628:646	In order to localize the major glycosylation site(s) in ABCC6, we applied limited proteolysis on the fully glycosylated and underglycosylated forms, followed by immunodetection with region-specific antibodies for ABCC6.
12901863	2	24	theme	MDCKII	338:343	arg1	cells					346:350	polarized mammalian (MDCKII) cells	317:350	polarized mammalian (MDCKII) cells	317:350	Here, we demonstrate that human ABCC6, when expressed by retroviral transduction in polarized mammalian (MDCKII) cells, is exclusively localized to the basolateral membrane.
12901863	2	25	theme	basolateral	385:395	arg1	membrane					397:404	the basolateral membrane	381:404	the basolateral membrane	381:404	Here, we demonstrate that human ABCC6, when expressed by retroviral transduction in polarized mammalian (MDCKII) cells, is exclusively localized to the basolateral membrane.
12901863	0	26	gly	N-glycosylation	29:43	arg1	ABCC6					54:58	human ABCC6	48:58	human ABCC6	48:58	Subcellular localization and N-glycosylation of human ABCC6, expressed in MDCKII cells.
12901863	3	27	theme	underglycosylated	488:504	arg1	form					506:509	the underglycosylated form	484:509	the underglycosylated form of the protein	484:524	The human ABCC6 in MDCKII cells was found to be glycosylated, in contrast to the underglycosylated form of the protein, as expressed in Sf9 cells.
12901863	6	28	theme	function	1068:1075	arg1	examination					1025:1035	further examination	1017:1035	further examination of routing, glycosylation, and function of the normal and pathological variants of human ABCC6	1017:1130	The polarized mammalian expression system characterized here provides a useful tool for further examination of routing, glycosylation, and function of the normal and pathological variants of human ABCC6.
12901863	6	29	theme	normal	1084:1089	arg1	variants					1108:1115	the normal and pathological variants	1080:1115	the normal and pathological variants of human ABCC6	1080:1130	The polarized mammalian expression system characterized here provides a useful tool for further examination of routing, glycosylation, and function of the normal and pathological variants of human ABCC6.
12901863	2	30	theme	human	259:263	arg1	ABCC6					265:269	human ABCC6	259:269	human ABCC6	259:269	Here, we demonstrate that human ABCC6, when expressed by retroviral transduction in polarized mammalian (MDCKII) cells, is exclusively localized to the basolateral membrane.
12901863	0	31	theme	human	48:52	arg1	ABCC6					54:58	human ABCC6	48:58	human ABCC6	48:58	Subcellular localization and N-glycosylation of human ABCC6, expressed in MDCKII cells.
12901863	4	32	theme	glycosylation	585:597	arg1	s					604:604	s	604:604	s	604:604	In order to localize the major glycosylation site(s) in ABCC6, we applied limited proteolysis on the fully glycosylated and underglycosylated forms, followed by immunodetection with region-specific antibodies for ABCC6.
12901863	4	32	theme	glycosylation	585:597	arg1	site					599:602	the major glycosylation site	575:602	the major glycosylation site(s) in ABCC6	575:614	In order to localize the major glycosylation site(s) in ABCC6, we applied limited proteolysis on the fully glycosylated and underglycosylated forms, followed by immunodetection with region-specific antibodies for ABCC6.
12901863	6	33	theme	expression	953:962	arg1	system					964:969	The polarized mammalian expression system	929:969	The polarized mammalian expression system characterized here	929:988	The polarized mammalian expression system characterized here provides a useful tool for further examination of routing, glycosylation, and function of the normal and pathological variants of human ABCC6.
12901863	5	34	gly	N-glycosylation	891:905	arg2	Asn15					800:804	Asn15	800:804	Asn15	800:804	Our results indicate that Asn15, which is located in the extracellular N-terminal region of human ABCC6, is the only N-glycosylation site in this protein.
12901863	5	34	gly	N-glycosylation	891:905	arg2	site					907:910	the only N-glycosylation site	882:910	the only N-glycosylation site in this protein	882:926	Our results indicate that Asn15, which is located in the extracellular N-terminal region of human ABCC6, is the only N-glycosylation site in this protein.
12901863	2	35	theme	polarized	317:325	arg1	cells					346:350	polarized mammalian (MDCKII) cells	317:350	polarized mammalian (MDCKII) cells	317:350	Here, we demonstrate that human ABCC6, when expressed by retroviral transduction in polarized mammalian (MDCKII) cells, is exclusively localized to the basolateral membrane.
12901863	3	36	theme	human	411:415	arg1	ABCC6					417:421	The human ABCC6	407:421	The human ABCC6 in MDCKII cells	407:437	The human ABCC6 in MDCKII cells was found to be glycosylated, in contrast to the underglycosylated form of the protein, as expressed in Sf9 cells.
12901863	4	37	theme	region-specific	736:750	arg1	antibodies					752:761	region-specific antibodies	736:761	region-specific antibodies for ABCC6	736:771	In order to localize the major glycosylation site(s) in ABCC6, we applied limited proteolysis on the fully glycosylated and underglycosylated forms, followed by immunodetection with region-specific antibodies for ABCC6.
12901863	3	38	theme	protein	518:524	arg1	form					506:509	the underglycosylated form	484:509	the underglycosylated form of the protein	484:524	The human ABCC6 in MDCKII cells was found to be glycosylated, in contrast to the underglycosylated form of the protein, as expressed in Sf9 cells.
12901863	6	39	theme	routing	1040:1046	arg1	examination					1025:1035	further examination	1017:1035	further examination of routing, glycosylation, and function of the normal and pathological variants of human ABCC6	1017:1130	The polarized mammalian expression system characterized here provides a useful tool for further examination of routing, glycosylation, and function of the normal and pathological variants of human ABCC6.
12901863	6	40	theme	glycosylation	1049:1061	arg1	examination					1025:1035	further examination	1017:1035	further examination of routing, glycosylation, and function of the normal and pathological variants of human ABCC6	1017:1130	The polarized mammalian expression system characterized here provides a useful tool for further examination of routing, glycosylation, and function of the normal and pathological variants of human ABCC6.
12901863	0	41	theme	ABCC6	54:58	arg1	N-glycosylation					29:43	N-glycosylation	29:43	N-glycosylation	29:43	Subcellular localization and N-glycosylation of human ABCC6, expressed in MDCKII cells.
12901863	0	41	theme	ABCC6	54:58	arg1	localization					12:23	Subcellular localization	0:23	Subcellular localization	0:23	Subcellular localization and N-glycosylation of human ABCC6, expressed in MDCKII cells.
12901863	1	42	theme	ABC	129:131	arg1	ABCC6					154:158	ABCC6	154:158	ABCC6 (MRP6)	154:165	Mutations in the gene coding for a human ABC transporter protein, ABCC6 (MRP6), are responsible for the development of pseudoxanthoma elasticum.
12901863	1	42	theme	ABC	129:131	arg1	protein					145:151	a human ABC transporter protein	121:151	a human ABC transporter protein	121:151	Mutations in the gene coding for a human ABC transporter protein, ABCC6 (MRP6), are responsible for the development of pseudoxanthoma elasticum.
12901863	3	43	from	ABCC6	417:421	arg1	cells					433:437	MDCKII cells	426:437	MDCKII cells	426:437	The human ABCC6 in MDCKII cells was found to be glycosylated, in contrast to the underglycosylated form of the protein, as expressed in Sf9 cells.
12901863	2	44	theme	retroviral	290:299	arg1	transduction					301:312	retroviral transduction	290:312	retroviral transduction in polarized mammalian (MDCKII) cells	290:350	Here, we demonstrate that human ABCC6, when expressed by retroviral transduction in polarized mammalian (MDCKII) cells, is exclusively localized to the basolateral membrane.
12901863	6	45	theme	variants	1108:1115	arg1	function					1068:1075	function	1068:1075	function	1068:1075	The polarized mammalian expression system characterized here provides a useful tool for further examination of routing, glycosylation, and function of the normal and pathological variants of human ABCC6.
12901863	6	45	theme	variants	1108:1115	arg1	routing					1040:1046	routing	1040:1046	routing	1040:1046	The polarized mammalian expression system characterized here provides a useful tool for further examination of routing, glycosylation, and function of the normal and pathological variants of human ABCC6.
12901863	6	45	theme	variants	1108:1115	arg1	glycosylation					1049:1061	glycosylation	1049:1061	glycosylation	1049:1061	The polarized mammalian expression system characterized here provides a useful tool for further examination of routing, glycosylation, and function of the normal and pathological variants of human ABCC6.
12901863	6	46	theme	ABCC6	1126:1130	arg1	variants					1108:1115	the normal and pathological variants	1080:1115	the normal and pathological variants of human ABCC6	1080:1130	The polarized mammalian expression system characterized here provides a useful tool for further examination of routing, glycosylation, and function of the normal and pathological variants of human ABCC6.
12901863	5	47	theme	N-glycosylation	891:905	arg1	site					907:910	the only N-glycosylation site	882:910	the only N-glycosylation site in this protein	882:926	Our results indicate that Asn15, which is located in the extracellular N-terminal region of human ABCC6, is the only N-glycosylation site in this protein.
12901863	5	47	theme	N-glycosylation	891:905	arg1	Asn15					800:804	Asn15	800:804	Asn15	800:804	Our results indicate that Asn15, which is located in the extracellular N-terminal region of human ABCC6, is the only N-glycosylation site in this protein.
12901863	3	48	theme	MDCKII	426:431	arg1	cells					433:437	MDCKII cells	426:437	MDCKII cells	426:437	The human ABCC6 in MDCKII cells was found to be glycosylated, in contrast to the underglycosylated form of the protein, as expressed in Sf9 cells.
12901863	5	49	theme	human	866:870	arg1	ABCC6					872:876	human ABCC6	866:876	human ABCC6	866:876	Our results indicate that Asn15, which is located in the extracellular N-terminal region of human ABCC6, is the only N-glycosylation site in this protein.
12901863	6	50	theme	polarized	933:941	arg1	system					964:969	The polarized mammalian expression system	929:969	The polarized mammalian expression system characterized here	929:988	The polarized mammalian expression system characterized here provides a useful tool for further examination of routing, glycosylation, and function of the normal and pathological variants of human ABCC6.
12901863	6	51	theme	human	1120:1124	arg1	ABCC6					1126:1130	human ABCC6	1120:1130	human ABCC6	1120:1130	The polarized mammalian expression system characterized here provides a useful tool for further examination of routing, glycosylation, and function of the normal and pathological variants of human ABCC6.
12901863	3	52	gly	underglycosylated	488:504	arg1	form					506:509	the underglycosylated form	484:509	the underglycosylated form of the protein	484:524	The human ABCC6 in MDCKII cells was found to be glycosylated, in contrast to the underglycosylated form of the protein, as expressed in Sf9 cells.
12901863	3	52	gly	underglycosylated	488:504	arg1	protein					518:524	the protein	514:524	the protein	514:524	The human ABCC6 in MDCKII cells was found to be glycosylated, in contrast to the underglycosylated form of the protein, as expressed in Sf9 cells.
12901863	5	53	from	region	856:861	arg1	located					816:822	located	816:822	located	816:822	Our results indicate that Asn15, which is located in the extracellular N-terminal region of human ABCC6, is the only N-glycosylation site in this protein.
12901863	5	54	theme	extracellular	831:843	arg1	region					856:861	the extracellular N-terminal region	827:861	the extracellular N-terminal region of human ABCC6	827:876	Our results indicate that Asn15, which is located in the extracellular N-terminal region of human ABCC6, is the only N-glycosylation site in this protein.
12901863	6	55	theme	further	1017:1023	arg1	examination					1025:1035	further examination	1017:1035	further examination of routing, glycosylation, and function of the normal and pathological variants of human ABCC6	1017:1130	The polarized mammalian expression system characterized here provides a useful tool for further examination of routing, glycosylation, and function of the normal and pathological variants of human ABCC6.
12901863	1	56	theme	human	123:127	arg1	ABCC6					154:158	ABCC6	154:158	ABCC6 (MRP6)	154:165	Mutations in the gene coding for a human ABC transporter protein, ABCC6 (MRP6), are responsible for the development of pseudoxanthoma elasticum.
12901863	1	56	theme	human	123:127	arg1	protein					145:151	a human ABC transporter protein	121:151	a human ABC transporter protein	121:151	Mutations in the gene coding for a human ABC transporter protein, ABCC6 (MRP6), are responsible for the development of pseudoxanthoma elasticum.
12901863	1	57	from	Mutations	88:96	arg1	gene					105:108	the gene	101:108	the gene coding for a human ABC transporter protein, ABCC6 (MRP6),	101:166	Mutations in the gene coding for a human ABC transporter protein, ABCC6 (MRP6), are responsible for the development of pseudoxanthoma elasticum.
12901863	3	58	theme	Sf9	543:545	arg1	cells					547:551	Sf9 cells	543:551	Sf9 cells	543:551	The human ABCC6 in MDCKII cells was found to be glycosylated, in contrast to the underglycosylated form of the protein, as expressed in Sf9 cells.
12901863	2	59	theme	mammalian	327:335	arg1	cells					346:350	polarized mammalian (MDCKII) cells	317:350	polarized mammalian (MDCKII) cells	317:350	Here, we demonstrate that human ABCC6, when expressed by retroviral transduction in polarized mammalian (MDCKII) cells, is exclusively localized to the basolateral membrane.
12901863	4	60	with	immunodetection	715:729	arg1	antibodies					752:761	region-specific antibodies	736:761	region-specific antibodies for ABCC6	736:771	In order to localize the major glycosylation site(s) in ABCC6, we applied limited proteolysis on the fully glycosylated and underglycosylated forms, followed by immunodetection with region-specific antibodies for ABCC6.
22849435	4	0	theme	Glycomics	676:684	arg1	analyses					686:693	advanced MS. Glycomics analyses	663:693	advanced MS. Glycomics analyses revealed approximately 100 distinct N-glycan compositions and identified a variety of structural features, including lactosaminic extensions, ABH antigens and sulfated antennae, as well as bisecting and terminal GlcNAc residues	663:921	The present paper reports analyses of the human plasma vWF N-glycan population using advanced MS. Glycomics analyses revealed approximately 100 distinct N-glycan compositions and identified a variety of structural features, including lactosaminic extensions, ABH antigens and sulfated antennae, as well as bisecting and terminal GlcNAc residues.
22849435	6	1	theme	sites	1049:1053	arg1	sites					1049:1053	the consensus sites	1035:1053	the consensus sites known to carry N-glycans	1035:1078	Glycoproteomics analyses mapped ten of the consensus sites known to carry N-glycans.
22849435	6	1	theme	sites	1049:1053	arg1	ten					1028:1030	ten	1028:1030	ten	1028:1030	Glycoproteomics analyses mapped ten of the consensus sites known to carry N-glycans.
22849435	1	2	theme	normal	120:125	arg1	haemostasis					127:137	normal haemostasis	120:137	normal haemostasis	120:137	vWF (von Willebrand factor) is a key component for maintenance of normal haemostasis, acting as the carrier protein of the coagulant Factor VIII and mediating platelet adhesion at sites of vascular injury.
22849435	6	3	theme	Glycoproteomics	996:1010	arg1	analyses					1012:1019	Glycoproteomics analyses	996:1019	Glycoproteomics analyses	996:1019	Glycoproteomics analyses mapped ten of the consensus sites known to carry N-glycans.
22849435	5	4	theme	N-glycan	950:957	arg1	structures					959:968	some 300 N-glycan structures	941:968	some 300 N-glycan structures	941:968	We estimate that some 300 N-glycan structures are carried by human vWF.
22849435	9	5	theme	Asn	1279:1281	arg1	site					1289:1292	the Asn(2635) site	1275:1292	the Asn(2635) site	1275:1292	Also, the Asn(2635) site, previously designated as unoccupied, was found to be highly glycosylated.
22849435	10	6	theme	populations	1407:1417	arg1	delineation					1373:1383	The delineation	1369:1383	The delineation of such varied glycan populations in conjunction with current models explaining vWF activity	1369:1476	The delineation of such varied glycan populations in conjunction with current models explaining vWF activity will facilitate research aimed at providing a better understanding of the influence of glycosylation on vWF function.
22849435	1	7	theme	haemostasis	127:137	arg1	maintenance					105:115	maintenance	105:115	maintenance of normal haemostasis	105:137	vWF (von Willebrand factor) is a key component for maintenance of normal haemostasis, acting as the carrier protein of the coagulant Factor VIII and mediating platelet adhesion at sites of vascular injury.
22849435	1	8	theme	platelet	213:220	arg1	protein					162:168	the carrier protein	150:168	the carrier protein of the coagulant Factor VIII	150:197	vWF (von Willebrand factor) is a key component for maintenance of normal haemostasis, acting as the carrier protein of the coagulant Factor VIII and mediating platelet adhesion at sites of vascular injury.
22849435	1	8	theme	platelet	213:220	arg1	adhesion					222:229	platelet adhesion	213:229	platelet adhesion	213:229	vWF (von Willebrand factor) is a key component for maintenance of normal haemostasis, acting as the carrier protein of the coagulant Factor VIII and mediating platelet adhesion at sites of vascular injury.
22849435	4	9	theme	structural	781:790	arg1	extensions					825:834	lactosaminic extensions	812:834	lactosaminic extensions	812:834	The present paper reports analyses of the human plasma vWF N-glycan population using advanced MS. Glycomics analyses revealed approximately 100 distinct N-glycan compositions and identified a variety of structural features, including lactosaminic extensions, ABH antigens and sulfated antennae, as well as bisecting and terminal GlcNAc residues.
22849435	4	9	theme	structural	781:790	arg1	antigens					841:848	ABH antigens	837:848	ABH antigens	837:848	The present paper reports analyses of the human plasma vWF N-glycan population using advanced MS. Glycomics analyses revealed approximately 100 distinct N-glycan compositions and identified a variety of structural features, including lactosaminic extensions, ABH antigens and sulfated antennae, as well as bisecting and terminal GlcNAc residues.
22849435	4	9	theme	structural	781:790	arg1	antennae					863:870	sulfated antennae	854:870	sulfated antennae	854:870	The present paper reports analyses of the human plasma vWF N-glycan population using advanced MS. Glycomics analyses revealed approximately 100 distinct N-glycan compositions and identified a variety of structural features, including lactosaminic extensions, ABH antigens and sulfated antennae, as well as bisecting and terminal GlcNAc residues.
22849435	4	9	theme	structural	781:790	arg1	features					792:799	structural features	781:799	structural features	781:799	The present paper reports analyses of the human plasma vWF N-glycan population using advanced MS. Glycomics analyses revealed approximately 100 distinct N-glycan compositions and identified a variety of structural features, including lactosaminic extensions, ABH antigens and sulfated antennae, as well as bisecting and terminal GlcNAc residues.
22849435	10	10	theme	glycan	1400:1405	arg1	populations					1407:1417	such varied glycan populations	1388:1417	such varied glycan populations in conjunction with current models explaining vWF activity	1388:1476	The delineation of such varied glycan populations in conjunction with current models explaining vWF activity will facilitate research aimed at providing a better understanding of the influence of glycosylation on vWF function.
22849435	1	11	dep	component	91:99	arg1	acting					140:145	acting	140:145	acting as the carrier protein of the coagulant Factor VIII	140:197	vWF (von Willebrand factor) is a key component for maintenance of normal haemostasis, acting as the carrier protein of the coagulant Factor VIII and mediating platelet adhesion at sites of vascular injury.
22849435	1	11	dep	component	91:99	arg1	mediating					203:211	mediating	203:211	mediating platelet adhesion at sites of vascular injury	203:257	vWF (von Willebrand factor) is a key component for maintenance of normal haemostasis, acting as the carrier protein of the coagulant Factor VIII and mediating platelet adhesion at sites of vascular injury.
22849435	4	12	dep	analyses	686:693	arg1	revealed					695:702	revealed	695:702	revealed approximately 100 distinct N-glycan compositions	695:751	The present paper reports analyses of the human plasma vWF N-glycan population using advanced MS. Glycomics analyses revealed approximately 100 distinct N-glycan compositions and identified a variety of structural features, including lactosaminic extensions, ABH antigens and sulfated antennae, as well as bisecting and terminal GlcNAc residues.
22849435	4	12	dep	analyses	686:693	arg1	identified					757:766	identified	757:766	identified a variety of structural features, including lactosaminic extensions, ABH antigens and sulfated antennae, as well as bisecting and terminal GlcNAc residues	757:921	The present paper reports analyses of the human plasma vWF N-glycan population using advanced MS. Glycomics analyses revealed approximately 100 distinct N-glycan compositions and identified a variety of structural features, including lactosaminic extensions, ABH antigens and sulfated antennae, as well as bisecting and terminal GlcNAc residues.
22849435	2	13	theme	ample	269:273	arg1	evidence					275:282	ample evidence that vWF glycan moieties are crucial determinants of its expression and function	269:363	ample evidence that vWF glycan moieties are crucial determinants of its expression and function	269:363	There is ample evidence that vWF glycan moieties are crucial determinants of its expression and function.
22849435	3	14	theme	molecular	498:506	arg1	mechanism					508:516	the molecular mechanism	494:516	the molecular mechanism underlying this phenomenon	494:543	Of particular clinical interest, ABH antigens influence vWF plasma levels according to the blood group of individuals, although the molecular mechanism underlying this phenomenon remains incompletely understood.
22849435	3	15	theme	blood	457:461	arg1	group					463:467	the blood group	453:467	the blood group of individuals	453:482	Of particular clinical interest, ABH antigens influence vWF plasma levels according to the blood group of individuals, although the molecular mechanism underlying this phenomenon remains incompletely understood.
22849435	3	15	theme	blood	457:461	arg1	individuals					472:482	individuals	472:482	individuals	472:482	Of particular clinical interest, ABH antigens influence vWF plasma levels according to the blood group of individuals, although the molecular mechanism underlying this phenomenon remains incompletely understood.
22849435	4	16	theme	N-glycan	731:738	arg1	compositions					740:751	approximately 100 distinct N-glycan compositions	704:751	approximately 100 distinct N-glycan compositions	704:751	The present paper reports analyses of the human plasma vWF N-glycan population using advanced MS. Glycomics analyses revealed approximately 100 distinct N-glycan compositions and identified a variety of structural features, including lactosaminic extensions, ABH antigens and sulfated antennae, as well as bisecting and terminal GlcNAc residues.
22849435	4	17	theme	population	646:655	arg1	analyses					604:611	analyses	604:611	analyses of the human plasma vWF N-glycan population using advanced MS. Glycomics analyses revealed approximately 100 distinct N-glycan compositions and identified a variety of structural features, including lactosaminic extensions, ABH antigens and sulfated antennae, as well as bisecting and terminal GlcNAc residues	604:921	The present paper reports analyses of the human plasma vWF N-glycan population using advanced MS. Glycomics analyses revealed approximately 100 distinct N-glycan compositions and identified a variety of structural features, including lactosaminic extensions, ABH antigens and sulfated antennae, as well as bisecting and terminal GlcNAc residues.
22849435	4	18	theme	vWF	633:635	arg1	population					646:655	the human plasma vWF N-glycan population	616:655	the human plasma vWF N-glycan population using advanced MS. Glycomics analyses revealed approximately 100 distinct N-glycan compositions and identified a variety of structural features, including lactosaminic extensions, ABH antigens and sulfated antennae, as well as bisecting and terminal GlcNAc residues	616:921	The present paper reports analyses of the human plasma vWF N-glycan population using advanced MS. Glycomics analyses revealed approximately 100 distinct N-glycan compositions and identified a variety of structural features, including lactosaminic extensions, ABH antigens and sulfated antennae, as well as bisecting and terminal GlcNAc residues.
22849435	7	19	theme	many	1136:1139	arg1	features					1152:1159	many structural features	1136:1159	many structural features	1136:1159	Glycan populations were found to be distinct, although many structural features were shared across all sites.
22849435	7	20	theme	structural	1141:1150	arg1	features					1152:1159	many structural features	1136:1159	many structural features	1136:1159	Glycan populations were found to be distinct, although many structural features were shared across all sites.
22849435	10	21	theme	such	1388:1391	arg1	populations					1407:1417	such varied glycan populations	1388:1417	such varied glycan populations in conjunction with current models explaining vWF activity	1388:1476	The delineation of such varied glycan populations in conjunction with current models explaining vWF activity will facilitate research aimed at providing a better understanding of the influence of glycosylation on vWF function.
22849435	1	22	theme	von	59:61	arg1	factor					74:79	von Willebrand factor	59:79	von Willebrand factor	59:79	vWF (von Willebrand factor) is a key component for maintenance of normal haemostasis, acting as the carrier protein of the coagulant Factor VIII and mediating platelet adhesion at sites of vascular injury.
22849435	1	22	theme	von	59:61	arg1	vWF					54:56	vWF	54:56	vWF (von Willebrand factor)	54:80	vWF (von Willebrand factor) is a key component for maintenance of normal haemostasis, acting as the carrier protein of the coagulant Factor VIII and mediating platelet adhesion at sites of vascular injury.
22849435	2	23	theme	expression	341:350	arg1	moieties					300:307	vWF glycan moieties	289:307	vWF glycan moieties	289:307	There is ample evidence that vWF glycan moieties are crucial determinants of its expression and function.
22849435	2	23	theme	expression	341:350	arg1	determinants					321:332	crucial determinants	313:332	crucial determinants of its expression and function	313:363	There is ample evidence that vWF glycan moieties are crucial determinants of its expression and function.
22849435	10	24	from	populations	1407:1417	arg1	conjunction					1422:1432	conjunction	1422:1432	conjunction with current models explaining vWF activity	1422:1476	The delineation of such varied glycan populations in conjunction with current models explaining vWF activity will facilitate research aimed at providing a better understanding of the influence of glycosylation on vWF function.
22849435	1	25	theme	injury	252:257	arg1	sites					234:238	sites	234:238	sites of vascular injury	234:257	vWF (von Willebrand factor) is a key component for maintenance of normal haemostasis, acting as the carrier protein of the coagulant Factor VIII and mediating platelet adhesion at sites of vascular injury.
22849435	1	25	theme	injury	252:257	arg1	injury					252:257	vascular injury	243:257	vascular injury	243:257	vWF (von Willebrand factor) is a key component for maintenance of normal haemostasis, acting as the carrier protein of the coagulant Factor VIII and mediating platelet adhesion at sites of vascular injury.
22849435	7	26	theme	Glycan	1081:1086	arg1	populations					1088:1098	Glycan populations	1081:1098	Glycan populations	1081:1098	Glycan populations were found to be distinct, although many structural features were shared across all sites.
22849435	4	27	theme	plasma	626:631	arg1	population					646:655	the human plasma vWF N-glycan population	616:655	the human plasma vWF N-glycan population using advanced MS. Glycomics analyses revealed approximately 100 distinct N-glycan compositions and identified a variety of structural features, including lactosaminic extensions, ABH antigens and sulfated antennae, as well as bisecting and terminal GlcNAc residues	616:921	The present paper reports analyses of the human plasma vWF N-glycan population using advanced MS. Glycomics analyses revealed approximately 100 distinct N-glycan compositions and identified a variety of structural features, including lactosaminic extensions, ABH antigens and sulfated antennae, as well as bisecting and terminal GlcNAc residues.
22849435	1	28	theme	Willebrand	63:72	arg1	factor					74:79	von Willebrand factor	59:79	von Willebrand factor	59:79	vWF (von Willebrand factor) is a key component for maintenance of normal haemostasis, acting as the carrier protein of the coagulant Factor VIII and mediating platelet adhesion at sites of vascular injury.
22849435	1	28	theme	Willebrand	63:72	arg1	vWF					54:56	vWF	54:56	vWF (von Willebrand factor)	54:80	vWF (von Willebrand factor) is a key component for maintenance of normal haemostasis, acting as the carrier protein of the coagulant Factor VIII and mediating platelet adhesion at sites of vascular injury.
22849435	3	29	theme	clinical	380:387	arg1	interest					389:396	particular clinical interest	369:396	particular clinical interest	369:396	Of particular clinical interest, ABH antigens influence vWF plasma levels according to the blood group of individuals, although the molecular mechanism underlying this phenomenon remains incompletely understood.
22849435	10	30	theme	vWF	1582:1584	arg1	function					1586:1593	vWF function	1582:1593	vWF function	1582:1593	The delineation of such varied glycan populations in conjunction with current models explaining vWF activity will facilitate research aimed at providing a better understanding of the influence of glycosylation on vWF function.
22849435	10	31	theme	varied	1393:1398	arg1	populations					1407:1417	such varied glycan populations	1388:1417	such varied glycan populations in conjunction with current models explaining vWF activity	1388:1476	The delineation of such varied glycan populations in conjunction with current models explaining vWF activity will facilitate research aimed at providing a better understanding of the influence of glycosylation on vWF function.
22849435	4	32	theme	sulfated	854:861	arg1	antennae					863:870	sulfated antennae	854:870	sulfated antennae	854:870	The present paper reports analyses of the human plasma vWF N-glycan population using advanced MS. Glycomics analyses revealed approximately 100 distinct N-glycan compositions and identified a variety of structural features, including lactosaminic extensions, ABH antigens and sulfated antennae, as well as bisecting and terminal GlcNAc residues.
22849435	10	33	gly	glycosylation	1565:1577	arg1	vWF					1582:1584	vWF function	1582:1593	vWF function	1582:1593	The delineation of such varied glycan populations in conjunction with current models explaining vWF activity will facilitate research aimed at providing a better understanding of the influence of glycosylation on vWF function.
22849435	4	34	theme	distinct	722:729	arg1	compositions					740:751	approximately 100 distinct N-glycan compositions	704:751	approximately 100 distinct N-glycan compositions	704:751	The present paper reports analyses of the human plasma vWF N-glycan population using advanced MS. Glycomics analyses revealed approximately 100 distinct N-glycan compositions and identified a variety of structural features, including lactosaminic extensions, ABH antigens and sulfated antennae, as well as bisecting and terminal GlcNAc residues.
22849435	8	35	theme	N-glycosylation	1246:1260	arg1	sites					1262:1266	particular N-glycosylation sites	1235:1266	particular N-glycosylation sites	1235:1266	Notably, the H antigen is not restricted to particular N-glycosylation sites.
22849435	4	36	theme	N-glycan	637:644	arg1	population					646:655	the human plasma vWF N-glycan population	616:655	the human plasma vWF N-glycan population using advanced MS. Glycomics analyses revealed approximately 100 distinct N-glycan compositions and identified a variety of structural features, including lactosaminic extensions, ABH antigens and sulfated antennae, as well as bisecting and terminal GlcNAc residues	616:921	The present paper reports analyses of the human plasma vWF N-glycan population using advanced MS. Glycomics analyses revealed approximately 100 distinct N-glycan compositions and identified a variety of structural features, including lactosaminic extensions, ABH antigens and sulfated antennae, as well as bisecting and terminal GlcNAc residues.
22849435	8	37	theme	H	1204:1204	arg1	antigen					1206:1212	the H antigen	1200:1212	the H antigen	1200:1212	Notably, the H antigen is not restricted to particular N-glycosylation sites.
22849435	8	37	theme	H	1204:1204	arg1	restricted					1221:1230	restricted	1221:1230	restricted	1221:1230	Notably, the H antigen is not restricted to particular N-glycosylation sites.
22849435	10	38	with	conjunction	1422:1432	arg1	models					1447:1452	current models	1439:1452	current models explaining vWF activity	1439:1476	The delineation of such varied glycan populations in conjunction with current models explaining vWF activity will facilitate research aimed at providing a better understanding of the influence of glycosylation on vWF function.
22849435	1	39	theme	carrier	154:160	arg1	protein					162:168	the carrier protein	150:168	the carrier protein of the coagulant Factor VIII	150:197	vWF (von Willebrand factor) is a key component for maintenance of normal haemostasis, acting as the carrier protein of the coagulant Factor VIII and mediating platelet adhesion at sites of vascular injury.
22849435	1	39	theme	carrier	154:160	arg1	adhesion					222:229	platelet adhesion	213:229	platelet adhesion	213:229	vWF (von Willebrand factor) is a key component for maintenance of normal haemostasis, acting as the carrier protein of the coagulant Factor VIII and mediating platelet adhesion at sites of vascular injury.
22849435	10	40	theme	glycosylation	1565:1577	arg1	influence					1552:1560	the influence	1548:1560	the influence of glycosylation on vWF function	1548:1593	The delineation of such varied glycan populations in conjunction with current models explaining vWF activity will facilitate research aimed at providing a better understanding of the influence of glycosylation on vWF function.
22849435	1	41	theme	vascular	243:250	arg1	injury					252:257	vascular injury	243:257	vascular injury	243:257	vWF (von Willebrand factor) is a key component for maintenance of normal haemostasis, acting as the carrier protein of the coagulant Factor VIII and mediating platelet adhesion at sites of vascular injury.
22849435	4	42	theme	present	582:588	arg1	paper					590:594	The present paper	578:594	The present paper	578:594	The present paper reports analyses of the human plasma vWF N-glycan population using advanced MS. Glycomics analyses revealed approximately 100 distinct N-glycan compositions and identified a variety of structural features, including lactosaminic extensions, ABH antigens and sulfated antennae, as well as bisecting and terminal GlcNAc residues.
22849435	4	43	theme	MS.	672:674	arg1	analyses					686:693	advanced MS. Glycomics analyses	663:693	advanced MS. Glycomics analyses revealed approximately 100 distinct N-glycan compositions and identified a variety of structural features, including lactosaminic extensions, ABH antigens and sulfated antennae, as well as bisecting and terminal GlcNAc residues	663:921	The present paper reports analyses of the human plasma vWF N-glycan population using advanced MS. Glycomics analyses revealed approximately 100 distinct N-glycan compositions and identified a variety of structural features, including lactosaminic extensions, ABH antigens and sulfated antennae, as well as bisecting and terminal GlcNAc residues.
22849435	3	44	theme	plasma	426:431	arg1	levels					433:438	vWF plasma levels	422:438	vWF plasma levels	422:438	Of particular clinical interest, ABH antigens influence vWF plasma levels according to the blood group of individuals, although the molecular mechanism underlying this phenomenon remains incompletely understood.
22849435	0	45	theme	von	31:33	arg1	factor					46:51	human von Willebrand factor	25:51	human von Willebrand factor	25:51	Mapping the N-glycome of human von Willebrand factor.
22849435	2	46	theme	vWF	289:291	arg1	moieties					300:307	vWF glycan moieties	289:307	vWF glycan moieties	289:307	There is ample evidence that vWF glycan moieties are crucial determinants of its expression and function.
22849435	2	46	theme	vWF	289:291	arg1	determinants					321:332	crucial determinants	313:332	crucial determinants of its expression and function	313:363	There is ample evidence that vWF glycan moieties are crucial determinants of its expression and function.
22849435	10	47	theme	vWF	1465:1467	arg1	activity					1469:1476	vWF activity	1465:1476	vWF activity	1465:1476	The delineation of such varied glycan populations in conjunction with current models explaining vWF activity will facilitate research aimed at providing a better understanding of the influence of glycosylation on vWF function.
22849435	6	48	theme	consensus	1039:1047	arg1	sites					1049:1053	the consensus sites	1035:1053	the consensus sites known to carry N-glycans	1035:1078	Glycoproteomics analyses mapped ten of the consensus sites known to carry N-glycans.
22849435	4	49	theme	human	620:624	arg1	population					646:655	the human plasma vWF N-glycan population	616:655	the human plasma vWF N-glycan population using advanced MS. Glycomics analyses revealed approximately 100 distinct N-glycan compositions and identified a variety of structural features, including lactosaminic extensions, ABH antigens and sulfated antennae, as well as bisecting and terminal GlcNAc residues	616:921	The present paper reports analyses of the human plasma vWF N-glycan population using advanced MS. Glycomics analyses revealed approximately 100 distinct N-glycan compositions and identified a variety of structural features, including lactosaminic extensions, ABH antigens and sulfated antennae, as well as bisecting and terminal GlcNAc residues.
22849435	0	50	theme	human	25:29	arg1	factor					46:51	human von Willebrand factor	25:51	human von Willebrand factor	25:51	Mapping the N-glycome of human von Willebrand factor.
22849435	3	51	theme	particular	369:378	arg1	interest					389:396	particular clinical interest	369:396	particular clinical interest	369:396	Of particular clinical interest, ABH antigens influence vWF plasma levels according to the blood group of individuals, although the molecular mechanism underlying this phenomenon remains incompletely understood.
22849435	10	52	from	understanding	1531:1543	arg1	function					1586:1593	vWF function	1582:1593	vWF function	1582:1593	The delineation of such varied glycan populations in conjunction with current models explaining vWF activity will facilitate research aimed at providing a better understanding of the influence of glycosylation on vWF function.
22849435	4	53	theme	lactosaminic	812:823	arg1	extensions					825:834	lactosaminic extensions	812:834	lactosaminic extensions	812:834	The present paper reports analyses of the human plasma vWF N-glycan population using advanced MS. Glycomics analyses revealed approximately 100 distinct N-glycan compositions and identified a variety of structural features, including lactosaminic extensions, ABH antigens and sulfated antennae, as well as bisecting and terminal GlcNAc residues.
22849435	2	54	theme	function	356:363	arg1	moieties					300:307	vWF glycan moieties	289:307	vWF glycan moieties	289:307	There is ample evidence that vWF glycan moieties are crucial determinants of its expression and function.
22849435	2	54	theme	function	356:363	arg1	determinants					321:332	crucial determinants	313:332	crucial determinants of its expression and function	313:363	There is ample evidence that vWF glycan moieties are crucial determinants of its expression and function.
22849435	0	55	theme	factor	46:51	arg1	N-glycome					12:20	the N-glycome	8:20	the N-glycome of human von Willebrand factor	8:51	Mapping the N-glycome of human von Willebrand factor.
22849435	10	56	from	conjunction	1422:1432	arg1	delineation					1373:1383	The delineation	1369:1383	The delineation of such varied glycan populations in conjunction with current models explaining vWF activity	1369:1476	The delineation of such varied glycan populations in conjunction with current models explaining vWF activity will facilitate research aimed at providing a better understanding of the influence of glycosylation on vWF function.
22849435	4	57	theme	ABH	837:839	arg1	antigens					841:848	ABH antigens	837:848	ABH antigens	837:848	The present paper reports analyses of the human plasma vWF N-glycan population using advanced MS. Glycomics analyses revealed approximately 100 distinct N-glycan compositions and identified a variety of structural features, including lactosaminic extensions, ABH antigens and sulfated antennae, as well as bisecting and terminal GlcNAc residues.
22849435	2	58	theme	glycan	293:298	arg1	moieties					300:307	vWF glycan moieties	289:307	vWF glycan moieties	289:307	There is ample evidence that vWF glycan moieties are crucial determinants of its expression and function.
22849435	2	58	theme	glycan	293:298	arg1	determinants					321:332	crucial determinants	313:332	crucial determinants of its expression and function	313:363	There is ample evidence that vWF glycan moieties are crucial determinants of its expression and function.
22849435	0	59	theme	Willebrand	35:44	arg1	factor					46:51	human von Willebrand factor	25:51	human von Willebrand factor	25:51	Mapping the N-glycome of human von Willebrand factor.
22849435	8	60	gly	N-glycosylation	1246:1260	arg2	sites					1262:1266	particular N-glycosylation sites	1235:1266	particular N-glycosylation sites	1235:1266	Notably, the H antigen is not restricted to particular N-glycosylation sites.
22849435	9	61	gly	glycosylated	1355:1366	arg1	site					1289:1292	the Asn(2635) site	1275:1292	the Asn(2635) site	1275:1292	Also, the Asn(2635) site, previously designated as unoccupied, was found to be highly glycosylated.
22849435	1	62	theme	key	87:89	arg1	component					91:99	a key component	85:99	a key component for maintenance of normal haemostasis	85:137	vWF (von Willebrand factor) is a key component for maintenance of normal haemostasis, acting as the carrier protein of the coagulant Factor VIII and mediating platelet adhesion at sites of vascular injury.
22849435	1	62	theme	key	87:89	arg1	vWF					54:56	vWF	54:56	vWF (von Willebrand factor)	54:80	vWF (von Willebrand factor) is a key component for maintenance of normal haemostasis, acting as the carrier protein of the coagulant Factor VIII and mediating platelet adhesion at sites of vascular injury.
22849435	10	63	theme	current	1439:1445	arg1	models					1447:1452	current models	1439:1452	current models explaining vWF activity	1439:1476	The delineation of such varied glycan populations in conjunction with current models explaining vWF activity will facilitate research aimed at providing a better understanding of the influence of glycosylation on vWF function.
22849435	4	64	theme	GlcNAc	907:912	arg1	features					792:799	structural features	781:799	structural features	781:799	The present paper reports analyses of the human plasma vWF N-glycan population using advanced MS. Glycomics analyses revealed approximately 100 distinct N-glycan compositions and identified a variety of structural features, including lactosaminic extensions, ABH antigens and sulfated antennae, as well as bisecting and terminal GlcNAc residues.
22849435	4	64	theme	GlcNAc	907:912	arg1	residues					914:921	terminal GlcNAc residues	898:921	terminal GlcNAc residues	898:921	The present paper reports analyses of the human plasma vWF N-glycan population using advanced MS. Glycomics analyses revealed approximately 100 distinct N-glycan compositions and identified a variety of structural features, including lactosaminic extensions, ABH antigens and sulfated antennae, as well as bisecting and terminal GlcNAc residues.
22849435	5	65	theme	human	985:989	arg1	vWF					991:993	human vWF	985:993	human vWF	985:993	We estimate that some 300 N-glycan structures are carried by human vWF.
22849435	4	66	theme	features	792:799	arg1	antigens					841:848	ABH antigens	837:848	ABH antigens	837:848	The present paper reports analyses of the human plasma vWF N-glycan population using advanced MS. Glycomics analyses revealed approximately 100 distinct N-glycan compositions and identified a variety of structural features, including lactosaminic extensions, ABH antigens and sulfated antennae, as well as bisecting and terminal GlcNAc residues.
22849435	4	66	theme	features	792:799	arg1	bisecting					884:892	bisecting	884:892	bisecting	884:892	The present paper reports analyses of the human plasma vWF N-glycan population using advanced MS. Glycomics analyses revealed approximately 100 distinct N-glycan compositions and identified a variety of structural features, including lactosaminic extensions, ABH antigens and sulfated antennae, as well as bisecting and terminal GlcNAc residues.
22849435	4	66	theme	features	792:799	arg1	antennae					863:870	sulfated antennae	854:870	sulfated antennae	854:870	The present paper reports analyses of the human plasma vWF N-glycan population using advanced MS. Glycomics analyses revealed approximately 100 distinct N-glycan compositions and identified a variety of structural features, including lactosaminic extensions, ABH antigens and sulfated antennae, as well as bisecting and terminal GlcNAc residues.
22849435	4	66	theme	features	792:799	arg1	variety					770:776	a variety	768:776	a variety of structural features, including lactosaminic extensions, ABH antigens and sulfated antennae, as well as bisecting and terminal GlcNAc residues	768:921	The present paper reports analyses of the human plasma vWF N-glycan population using advanced MS. Glycomics analyses revealed approximately 100 distinct N-glycan compositions and identified a variety of structural features, including lactosaminic extensions, ABH antigens and sulfated antennae, as well as bisecting and terminal GlcNAc residues.
22849435	4	66	theme	features	792:799	arg1	extensions					825:834	lactosaminic extensions	812:834	lactosaminic extensions	812:834	The present paper reports analyses of the human plasma vWF N-glycan population using advanced MS. Glycomics analyses revealed approximately 100 distinct N-glycan compositions and identified a variety of structural features, including lactosaminic extensions, ABH antigens and sulfated antennae, as well as bisecting and terminal GlcNAc residues.
22849435	4	66	theme	features	792:799	arg1	features					792:799	structural features	781:799	structural features	781:799	The present paper reports analyses of the human plasma vWF N-glycan population using advanced MS. Glycomics analyses revealed approximately 100 distinct N-glycan compositions and identified a variety of structural features, including lactosaminic extensions, ABH antigens and sulfated antennae, as well as bisecting and terminal GlcNAc residues.
22849435	4	66	theme	features	792:799	arg1	residues					914:921	terminal GlcNAc residues	898:921	terminal GlcNAc residues	898:921	The present paper reports analyses of the human plasma vWF N-glycan population using advanced MS. Glycomics analyses revealed approximately 100 distinct N-glycan compositions and identified a variety of structural features, including lactosaminic extensions, ABH antigens and sulfated antennae, as well as bisecting and terminal GlcNAc residues.
22849435	8	67	theme	particular	1235:1244	arg1	sites					1262:1266	particular N-glycosylation sites	1235:1266	particular N-glycosylation sites	1235:1266	Notably, the H antigen is not restricted to particular N-glycosylation sites.
22849435	10	68	from	delineation	1373:1383	arg1	conjunction					1422:1432	conjunction	1422:1432	conjunction with current models explaining vWF activity	1422:1476	The delineation of such varied glycan populations in conjunction with current models explaining vWF activity will facilitate research aimed at providing a better understanding of the influence of glycosylation on vWF function.
22849435	1	69	theme	coagulant	177:185	arg1	VIII					194:197	the coagulant Factor VIII	173:197	the coagulant Factor VIII	173:197	vWF (von Willebrand factor) is a key component for maintenance of normal haemostasis, acting as the carrier protein of the coagulant Factor VIII and mediating platelet adhesion at sites of vascular injury.
22849435	4	70	theme	terminal	898:905	arg1	features					792:799	structural features	781:799	structural features	781:799	The present paper reports analyses of the human plasma vWF N-glycan population using advanced MS. Glycomics analyses revealed approximately 100 distinct N-glycan compositions and identified a variety of structural features, including lactosaminic extensions, ABH antigens and sulfated antennae, as well as bisecting and terminal GlcNAc residues.
22849435	4	70	theme	terminal	898:905	arg1	residues					914:921	terminal GlcNAc residues	898:921	terminal GlcNAc residues	898:921	The present paper reports analyses of the human plasma vWF N-glycan population using advanced MS. Glycomics analyses revealed approximately 100 distinct N-glycan compositions and identified a variety of structural features, including lactosaminic extensions, ABH antigens and sulfated antennae, as well as bisecting and terminal GlcNAc residues.
22849435	3	71	dep	influence	412:420	arg1	although					485:492	although	485:492	although	485:492	Of particular clinical interest, ABH antigens influence vWF plasma levels according to the blood group of individuals, although the molecular mechanism underlying this phenomenon remains incompletely understood.
22849435	10	72	from	function	1586:1593	arg1	understanding					1531:1543	a better understanding	1522:1543	a better understanding of the influence of glycosylation on vWF function	1522:1593	The delineation of such varied glycan populations in conjunction with current models explaining vWF activity will facilitate research aimed at providing a better understanding of the influence of glycosylation on vWF function.
22849435	3	73	theme	individuals	472:482	arg1	group					463:467	the blood group	453:467	the blood group of individuals	453:482	Of particular clinical interest, ABH antigens influence vWF plasma levels according to the blood group of individuals, although the molecular mechanism underlying this phenomenon remains incompletely understood.
22849435	3	73	theme	individuals	472:482	arg1	individuals					472:482	individuals	472:482	individuals	472:482	Of particular clinical interest, ABH antigens influence vWF plasma levels according to the blood group of individuals, although the molecular mechanism underlying this phenomenon remains incompletely understood.
22849435	1	74	theme	Factor	187:192	arg1	VIII					194:197	the coagulant Factor VIII	173:197	the coagulant Factor VIII	173:197	vWF (von Willebrand factor) is a key component for maintenance of normal haemostasis, acting as the carrier protein of the coagulant Factor VIII and mediating platelet adhesion at sites of vascular injury.
22849435	10	75	from	influence	1552:1560	arg1	function					1586:1593	vWF function	1582:1593	vWF function	1582:1593	The delineation of such varied glycan populations in conjunction with current models explaining vWF activity will facilitate research aimed at providing a better understanding of the influence of glycosylation on vWF function.
22849435	3	76	theme	vWF	422:424	arg1	levels					433:438	vWF plasma levels	422:438	vWF plasma levels	422:438	Of particular clinical interest, ABH antigens influence vWF plasma levels according to the blood group of individuals, although the molecular mechanism underlying this phenomenon remains incompletely understood.
22849435	4	77	theme	advanced	663:670	arg1	analyses					686:693	advanced MS. Glycomics analyses	663:693	advanced MS. Glycomics analyses revealed approximately 100 distinct N-glycan compositions and identified a variety of structural features, including lactosaminic extensions, ABH antigens and sulfated antennae, as well as bisecting and terminal GlcNAc residues	663:921	The present paper reports analyses of the human plasma vWF N-glycan population using advanced MS. Glycomics analyses revealed approximately 100 distinct N-glycan compositions and identified a variety of structural features, including lactosaminic extensions, ABH antigens and sulfated antennae, as well as bisecting and terminal GlcNAc residues.
22849435	3	78	theme	ABH	399:401	arg1	antigens					403:410	ABH antigens	399:410	ABH antigens	399:410	Of particular clinical interest, ABH antigens influence vWF plasma levels according to the blood group of individuals, although the molecular mechanism underlying this phenomenon remains incompletely understood.
22849435	1	79	theme	VIII	194:197	arg1	protein					162:168	the carrier protein	150:168	the carrier protein of the coagulant Factor VIII	150:197	vWF (von Willebrand factor) is a key component for maintenance of normal haemostasis, acting as the carrier protein of the coagulant Factor VIII and mediating platelet adhesion at sites of vascular injury.
22849435	1	79	theme	VIII	194:197	arg1	adhesion					222:229	platelet adhesion	213:229	platelet adhesion	213:229	vWF (von Willebrand factor) is a key component for maintenance of normal haemostasis, acting as the carrier protein of the coagulant Factor VIII and mediating platelet adhesion at sites of vascular injury.
22849435	10	80	theme	better	1524:1529	arg1	understanding					1531:1543	a better understanding	1522:1543	a better understanding of the influence of glycosylation on vWF function	1522:1593	The delineation of such varied glycan populations in conjunction with current models explaining vWF activity will facilitate research aimed at providing a better understanding of the influence of glycosylation on vWF function.
22849435	2	81	theme	crucial	313:319	arg1	moieties					300:307	vWF glycan moieties	289:307	vWF glycan moieties	289:307	There is ample evidence that vWF glycan moieties are crucial determinants of its expression and function.
22849435	2	81	theme	crucial	313:319	arg1	determinants					321:332	crucial determinants	313:332	crucial determinants of its expression and function	313:363	There is ample evidence that vWF glycan moieties are crucial determinants of its expression and function.
22849435	10	82	theme	influence	1552:1560	arg1	understanding					1531:1543	a better understanding	1522:1543	a better understanding of the influence of glycosylation on vWF function	1522:1593	The delineation of such varied glycan populations in conjunction with current models explaining vWF activity will facilitate research aimed at providing a better understanding of the influence of glycosylation on vWF function.
23944609	6	0	gly	glycopeptides	1114:1126	arg2	glycopeptides					1114:1126	low abundance IgG glycopeptides	1096:1126	low abundance IgG glycopeptides	1096:1126	The remarkable sensitivity and selectivity of MRM enable the detection of low abundance IgG glycopeptides, even when IgG was digested directly in serum with no cleanup prior to the liquid chromatography.
23944609	1	1	theme	glycan	161:166	arg1	characterization					168:183	glycan characterization	161:183	glycan characterization by the global profiling of released glycans	161:227	Studies aimed toward glycan biomarker discovery have focused on glycan characterization by the global profiling of released glycans.
23944609	4	2	theme	quantitative	659:670	arg1	changes					672:678	quantitative changes	659:678	quantitative changes in glycosylation	659:695	We have developed a method using MRM to monitor protein glycosylation normalized to absolute protein concentrations to examine quantitative changes in glycosylation at a site-specific level.
23944609	0	3	theme	reaction	76:83	arg1	monitoring					85:94	multiple reaction monitoring	67:94	multiple reaction monitoring	67:94	Absolute quantitation of immunoglobulin G and its glycoforms using multiple reaction monitoring.
23944609	5	4	from	change	989:994	arg1	concentration					1007:1019	protein concentration	999:1019	protein concentration	999:1019	This new approach provides information regarding both the absolute amount of protein and the site-specific glycosylation profile and will thus be useful to determine if altered glycosylation profiles in serum/plasma are due to a change in protein glycosylation or a change in protein concentration.
23944609	5	4	from	change	989:994	arg1	glycosylation					970:982	protein glycosylation	962:982	protein glycosylation	962:982	This new approach provides information regarding both the absolute amount of protein and the site-specific glycosylation profile and will thus be useful to determine if altered glycosylation profiles in serum/plasma are due to a change in protein glycosylation or a change in protein concentration.
23944609	6	5	theme	low	1096:1098	arg1	glycopeptides					1114:1126	low abundance IgG glycopeptides	1096:1126	low abundance IgG glycopeptides	1096:1126	The remarkable sensitivity and selectivity of MRM enable the detection of low abundance IgG glycopeptides, even when IgG was digested directly in serum with no cleanup prior to the liquid chromatography.
23944609	3	6	theme	glycans	401:407	arg1	Quantitation					366:377	Quantitation	366:377	Quantitation of peptide-conjugated glycans	366:407	Quantitation of peptide-conjugated glycans directly facilitates the differential analysis of distinct glycoforms associated with specific proteins at distinct sites.
23944609	8	7	theme	accurate	1468:1475	arg1	abundances					1477:1486	more accurate abundances	1463:1486	more accurate abundances	1463:1486	The results show that IgG glycopeptides can be analyzed directly from serum (without enrichment) and yield more accurate abundances when normalized to the protein content.
23944609	9	8	theme	use	1594:1596	arg1	study					1574:1578	the most comprehensive study	1551:1578	the most comprehensive study so far of the use of multiple reaction monitoring for the quantitation of glycoproteins and their glycosylation patterns in biofluids	1551:1712	This report represents the most comprehensive study so far of the use of multiple reaction monitoring for the quantitation of glycoproteins and their glycosylation patterns in biofluids.
23944609	9	9	theme	multiple	1601:1608	arg1	monitoring					1619:1628	multiple reaction monitoring	1601:1628	multiple reaction monitoring	1601:1628	This report represents the most comprehensive study so far of the use of multiple reaction monitoring for the quantitation of glycoproteins and their glycosylation patterns in biofluids.
23944609	4	10	from	changes	672:678	arg1	glycosylation					683:695	glycosylation	683:695	glycosylation	683:695	We have developed a method using MRM to monitor protein glycosylation normalized to absolute protein concentrations to examine quantitative changes in glycosylation at a site-specific level.
23944609	7	11	theme	IgG	1330:1332	arg1	quantitation					1342:1353	IgG protein quantitation	1330:1353	IgG protein quantitation	1330:1353	Our results show a low limit of detection of 60 amol and a wide dynamic range of 3 orders magnitude for IgG protein quantitation.
23944609	5	12	theme	protein	999:1005	arg1	concentration					1007:1019	protein concentration	999:1019	protein concentration	999:1019	This new approach provides information regarding both the absolute amount of protein and the site-specific glycosylation profile and will thus be useful to determine if altered glycosylation profiles in serum/plasma are due to a change in protein glycosylation or a change in protein concentration.
23944609	2	13	theme	new	301:303	arg1	types					305:309	new types	301:309	new types of biomarkers	301:323	Site-specific glycosylation analysis is less developed but may provide new types of biomarkers with higher sensitivity and specificity.
23944609	5	14	theme	protein	962:968	arg1	glycosylation					970:982	protein glycosylation	962:982	protein glycosylation	962:982	This new approach provides information regarding both the absolute amount of protein and the site-specific glycosylation profile and will thus be useful to determine if altered glycosylation profiles in serum/plasma are due to a change in protein glycosylation or a change in protein concentration.
23944609	3	15	theme	peptide-conjugated	382:399	arg1	glycans					401:407	peptide-conjugated glycans	382:407	peptide-conjugated glycans	382:407	Quantitation of peptide-conjugated glycans directly facilitates the differential analysis of distinct glycoforms associated with specific proteins at distinct sites.
23944609	8	16	gly	glycopeptides	1382:1394	arg2	glycopeptides					1382:1394	IgG glycopeptides	1378:1394	IgG glycopeptides	1378:1394	The results show that IgG glycopeptides can be analyzed directly from serum (without enrichment) and yield more accurate abundances when normalized to the protein content.
23944609	6	17	theme	abundance	1100:1108	arg1	glycopeptides					1114:1126	low abundance IgG glycopeptides	1096:1126	low abundance IgG glycopeptides	1096:1126	The remarkable sensitivity and selectivity of MRM enable the detection of low abundance IgG glycopeptides, even when IgG was digested directly in serum with no cleanup prior to the liquid chromatography.
23944609	7	18	theme	amol	1274:1277	arg1	detection					1258:1266	detection	1258:1266	detection of 60 amol	1258:1277	Our results show a low limit of detection of 60 amol and a wide dynamic range of 3 orders magnitude for IgG protein quantitation.
23944609	7	19	theme	detection	1258:1266	arg1	limit					1249:1253	a low limit	1243:1253	a low limit of detection of 60 amol	1243:1277	Our results show a low limit of detection of 60 amol and a wide dynamic range of 3 orders magnitude for IgG protein quantitation.
23944609	7	19	theme	detection	1258:1266	arg1	range					1298:1302	a wide dynamic range	1283:1302	a wide dynamic range of 3 orders magnitude	1283:1324	Our results show a low limit of detection of 60 amol and a wide dynamic range of 3 orders magnitude for IgG protein quantitation.
23944609	3	20	theme	differential	434:445	arg1	analysis					447:454	the differential analysis	430:454	the differential analysis of distinct glycoforms associated with specific proteins at distinct sites	430:529	Quantitation of peptide-conjugated glycans directly facilitates the differential analysis of distinct glycoforms associated with specific proteins at distinct sites.
23944609	5	21	from	profiles	914:921	arg1	serum/plasma					926:937	serum/plasma	926:937	serum/plasma	926:937	This new approach provides information regarding both the absolute amount of protein and the site-specific glycosylation profile and will thus be useful to determine if altered glycosylation profiles in serum/plasma are due to a change in protein glycosylation or a change in protein concentration.
23944609	7	22	theme	wide	1285:1288	arg1	range					1298:1302	a wide dynamic range	1283:1302	a wide dynamic range of 3 orders magnitude	1283:1324	Our results show a low limit of detection of 60 amol and a wide dynamic range of 3 orders magnitude for IgG protein quantitation.
23944609	7	23	theme	magnitude	1316:1324	arg1	limit					1249:1253	a low limit	1243:1253	a low limit of detection of 60 amol	1243:1277	Our results show a low limit of detection of 60 amol and a wide dynamic range of 3 orders magnitude for IgG protein quantitation.
23944609	7	23	theme	magnitude	1316:1324	arg1	range					1298:1302	a wide dynamic range	1283:1302	a wide dynamic range of 3 orders magnitude	1283:1324	Our results show a low limit of detection of 60 amol and a wide dynamic range of 3 orders magnitude for IgG protein quantitation.
23944609	5	24	gly	glycosylation	830:842	arg1	protein					800:806	protein	800:806	protein	800:806	This new approach provides information regarding both the absolute amount of protein and the site-specific glycosylation profile and will thus be useful to determine if altered glycosylation profiles in serum/plasma are due to a change in protein glycosylation or a change in protein concentration.
23944609	9	25	from	patterns	1692:1699	arg1	biofluids					1704:1712	biofluids	1704:1712	biofluids	1704:1712	This report represents the most comprehensive study so far of the use of multiple reaction monitoring for the quantitation of glycoproteins and their glycosylation patterns in biofluids.
23944609	1	26	theme	global	192:197	arg1	profiling					199:207	the global profiling	188:207	the global profiling of released glycans	188:227	Studies aimed toward glycan biomarker discovery have focused on glycan characterization by the global profiling of released glycans.
23944609	0	27	theme	Absolute	0:7	arg1	quantitation					9:20	Absolute quantitation	0:20	Absolute quantitation of immunoglobulin G and its glycoforms	0:59	Absolute quantitation of immunoglobulin G and its glycoforms using multiple reaction monitoring.
23944609	4	28	theme	protein	625:631	arg1	concentrations					633:646	absolute protein concentrations	616:646	absolute protein concentrations	616:646	We have developed a method using MRM to monitor protein glycosylation normalized to absolute protein concentrations to examine quantitative changes in glycosylation at a site-specific level.
23944609	5	29	theme	new	728:730	arg1	approach					732:739	This new approach	723:739	This new approach	723:739	This new approach provides information regarding both the absolute amount of protein and the site-specific glycosylation profile and will thus be useful to determine if altered glycosylation profiles in serum/plasma are due to a change in protein glycosylation or a change in protein concentration.
23944609	2	30	theme	higher	330:335	arg1	sensitivity					337:347	higher sensitivity	330:347	higher sensitivity	330:347	Site-specific glycosylation analysis is less developed but may provide new types of biomarkers with higher sensitivity and specificity.
23944609	5	31	theme	site-specific	816:828	arg1	profile					844:850	the site-specific glycosylation profile	812:850	the site-specific glycosylation profile	812:850	This new approach provides information regarding both the absolute amount of protein and the site-specific glycosylation profile and will thus be useful to determine if altered glycosylation profiles in serum/plasma are due to a change in protein glycosylation or a change in protein concentration.
23944609	3	32	theme	specific	495:502	arg1	proteins					504:511	specific proteins	495:511	specific proteins at distinct sites	495:529	Quantitation of peptide-conjugated glycans directly facilitates the differential analysis of distinct glycoforms associated with specific proteins at distinct sites.
23944609	0	33	theme	immunoglobulin	25:38	arg1	G					40:40	immunoglobulin G	25:40	immunoglobulin G	25:40	Absolute quantitation of immunoglobulin G and its glycoforms using multiple reaction monitoring.
23944609	4	34	theme	absolute	616:623	arg1	concentrations					633:646	absolute protein concentrations	616:646	absolute protein concentrations	616:646	We have developed a method using MRM to monitor protein glycosylation normalized to absolute protein concentrations to examine quantitative changes in glycosylation at a site-specific level.
23944609	6	35	theme	MRM	1068:1070	arg1	selectivity					1053:1063	selectivity	1053:1063	selectivity	1053:1063	The remarkable sensitivity and selectivity of MRM enable the detection of low abundance IgG glycopeptides, even when IgG was digested directly in serum with no cleanup prior to the liquid chromatography.
23944609	6	35	theme	MRM	1068:1070	arg1	sensitivity					1037:1047	remarkable sensitivity	1026:1047	remarkable sensitivity	1026:1047	The remarkable sensitivity and selectivity of MRM enable the detection of low abundance IgG glycopeptides, even when IgG was digested directly in serum with no cleanup prior to the liquid chromatography.
23944609	5	36	theme	protein	800:806	arg1	profile					844:850	the site-specific glycosylation profile	812:850	the site-specific glycosylation profile	812:850	This new approach provides information regarding both the absolute amount of protein and the site-specific glycosylation profile and will thus be useful to determine if altered glycosylation profiles in serum/plasma are due to a change in protein glycosylation or a change in protein concentration.
23944609	5	36	theme	protein	800:806	arg1	protein					800:806	protein	800:806	protein	800:806	This new approach provides information regarding both the absolute amount of protein and the site-specific glycosylation profile and will thus be useful to determine if altered glycosylation profiles in serum/plasma are due to a change in protein glycosylation or a change in protein concentration.
23944609	5	36	theme	protein	800:806	arg1	amount					790:795	the absolute amount	777:795	the absolute amount of protein	777:806	This new approach provides information regarding both the absolute amount of protein and the site-specific glycosylation profile and will thus be useful to determine if altered glycosylation profiles in serum/plasma are due to a change in protein glycosylation or a change in protein concentration.
23944609	6	37	dep	sensitivity	1037:1047	arg1	The					1022:1024	The	1022:1024	The	1022:1024	The remarkable sensitivity and selectivity of MRM enable the detection of low abundance IgG glycopeptides, even when IgG was digested directly in serum with no cleanup prior to the liquid chromatography.
23944609	2	38	theme	biomarkers	314:323	arg1	types					305:309	new types	301:309	new types of biomarkers	301:323	Site-specific glycosylation analysis is less developed but may provide new types of biomarkers with higher sensitivity and specificity.
23944609	1	39	theme	released	212:219	arg1	glycans					221:227	released glycans	212:227	released glycans	212:227	Studies aimed toward glycan biomarker discovery have focused on glycan characterization by the global profiling of released glycans.
23944609	3	40	theme	glycoforms	468:477	arg1	analysis					447:454	the differential analysis	430:454	the differential analysis of distinct glycoforms associated with specific proteins at distinct sites	430:529	Quantitation of peptide-conjugated glycans directly facilitates the differential analysis of distinct glycoforms associated with specific proteins at distinct sites.
23944609	9	41	theme	monitoring	1619:1628	arg1	use					1594:1596	the use	1590:1596	the use of multiple reaction monitoring for the quantitation of glycoproteins and their glycosylation patterns in biofluids	1590:1712	This report represents the most comprehensive study so far of the use of multiple reaction monitoring for the quantitation of glycoproteins and their glycosylation patterns in biofluids.
23944609	3	42	theme	distinct	516:523	arg1	sites					525:529	distinct sites	516:529	distinct sites	516:529	Quantitation of peptide-conjugated glycans directly facilitates the differential analysis of distinct glycoforms associated with specific proteins at distinct sites.
23944609	9	43	from	glycoproteins	1654:1666	arg1	biofluids					1704:1712	biofluids	1704:1712	biofluids	1704:1712	This report represents the most comprehensive study so far of the use of multiple reaction monitoring for the quantitation of glycoproteins and their glycosylation patterns in biofluids.
23944609	1	44	theme	glycans	221:227	arg1	profiling					199:207	the global profiling	188:207	the global profiling of released glycans	188:227	Studies aimed toward glycan biomarker discovery have focused on glycan characterization by the global profiling of released glycans.
23944609	0	45	theme	G	40:40	arg1	quantitation					9:20	Absolute quantitation	0:20	Absolute quantitation of immunoglobulin G and its glycoforms	0:59	Absolute quantitation of immunoglobulin G and its glycoforms using multiple reaction monitoring.
23944609	9	46	theme	patterns	1692:1699	arg1	quantitation					1638:1649	the quantitation	1634:1649	the quantitation of glycoproteins and their glycosylation patterns in biofluids	1634:1712	This report represents the most comprehensive study so far of the use of multiple reaction monitoring for the quantitation of glycoproteins and their glycosylation patterns in biofluids.
23944609	6	47	theme	glycopeptides	1114:1126	arg1	detection					1083:1091	the detection	1079:1091	the detection of low abundance IgG glycopeptides, even when IgG was digested directly in serum with no cleanup prior to the liquid chromatography	1079:1223	The remarkable sensitivity and selectivity of MRM enable the detection of low abundance IgG glycopeptides, even when IgG was digested directly in serum with no cleanup prior to the liquid chromatography.
23944609	7	48	theme	low	1245:1247	arg1	limit					1249:1253	a low limit	1243:1253	a low limit of detection of 60 amol	1243:1277	Our results show a low limit of detection of 60 amol and a wide dynamic range of 3 orders magnitude for IgG protein quantitation.
23944609	0	49	theme	glycoforms	50:59	arg1	quantitation					9:20	Absolute quantitation	0:20	Absolute quantitation of immunoglobulin G and its glycoforms	0:59	Absolute quantitation of immunoglobulin G and its glycoforms using multiple reaction monitoring.
23944609	4	50	theme	protein	580:586	arg1	glycosylation					588:600	protein glycosylation	580:600	protein glycosylation normalized to absolute protein concentrations	580:646	We have developed a method using MRM to monitor protein glycosylation normalized to absolute protein concentrations to examine quantitative changes in glycosylation at a site-specific level.
23944609	5	51	theme	altered	892:898	arg1	profiles					914:921	altered glycosylation profiles	892:921	altered glycosylation profiles in serum/plasma	892:937	This new approach provides information regarding both the absolute amount of protein and the site-specific glycosylation profile and will thus be useful to determine if altered glycosylation profiles in serum/plasma are due to a change in protein glycosylation or a change in protein concentration.
23944609	8	52	theme	protein	1511:1517	arg1	content					1519:1525	the protein content	1507:1525	the protein content	1507:1525	The results show that IgG glycopeptides can be analyzed directly from serum (without enrichment) and yield more accurate abundances when normalized to the protein content.
23944609	2	53	theme	glycosylation	244:256	arg1	analysis					258:265	Site-specific glycosylation analysis	230:265	Site-specific glycosylation analysis	230:265	Site-specific glycosylation analysis is less developed but may provide new types of biomarkers with higher sensitivity and specificity.
23944609	3	54	from	sites	525:529	arg1	proteins					504:511	specific proteins	495:511	specific proteins at distinct sites	495:529	Quantitation of peptide-conjugated glycans directly facilitates the differential analysis of distinct glycoforms associated with specific proteins at distinct sites.
23944609	1	55	theme	glycan	118:123	arg1	discovery					135:143	glycan biomarker discovery	118:143	glycan biomarker discovery	118:143	Studies aimed toward glycan biomarker discovery have focused on glycan characterization by the global profiling of released glycans.
23944609	3	56	theme	distinct	459:466	arg1	glycoforms					468:477	distinct glycoforms	459:477	distinct glycoforms associated with specific proteins at distinct sites	459:529	Quantitation of peptide-conjugated glycans directly facilitates the differential analysis of distinct glycoforms associated with specific proteins at distinct sites.
23944609	9	57	from	biofluids	1704:1712	arg1	quantitation					1638:1649	the quantitation	1634:1649	the quantitation of glycoproteins and their glycosylation patterns in biofluids	1634:1712	This report represents the most comprehensive study so far of the use of multiple reaction monitoring for the quantitation of glycoproteins and their glycosylation patterns in biofluids.
23944609	7	58	theme	dynamic	1290:1296	arg1	range					1298:1302	a wide dynamic range	1283:1302	a wide dynamic range of 3 orders magnitude	1283:1324	Our results show a low limit of detection of 60 amol and a wide dynamic range of 3 orders magnitude for IgG protein quantitation.
23944609	2	59	theme	Site-specific	230:242	arg1	analysis					258:265	Site-specific glycosylation analysis	230:265	Site-specific glycosylation analysis	230:265	Site-specific glycosylation analysis is less developed but may provide new types of biomarkers with higher sensitivity and specificity.
23944609	7	60	theme	protein	1334:1340	arg1	quantitation					1342:1353	IgG protein quantitation	1330:1353	IgG protein quantitation	1330:1353	Our results show a low limit of detection of 60 amol and a wide dynamic range of 3 orders magnitude for IgG protein quantitation.
23944609	1	61	theme	biomarker	125:133	arg1	discovery					135:143	glycan biomarker discovery	118:143	glycan biomarker discovery	118:143	Studies aimed toward glycan biomarker discovery have focused on glycan characterization by the global profiling of released glycans.
23944609	6	62	theme	remarkable	1026:1035	arg1	sensitivity					1037:1047	remarkable sensitivity	1026:1047	remarkable sensitivity	1026:1047	The remarkable sensitivity and selectivity of MRM enable the detection of low abundance IgG glycopeptides, even when IgG was digested directly in serum with no cleanup prior to the liquid chromatography.
23944609	5	63	theme	absolute	781:788	arg1	protein					800:806	protein	800:806	protein	800:806	This new approach provides information regarding both the absolute amount of protein and the site-specific glycosylation profile and will thus be useful to determine if altered glycosylation profiles in serum/plasma are due to a change in protein glycosylation or a change in protein concentration.
23944609	5	63	theme	absolute	781:788	arg1	amount					790:795	the absolute amount	777:795	the absolute amount of protein	777:806	This new approach provides information regarding both the absolute amount of protein and the site-specific glycosylation profile and will thus be useful to determine if altered glycosylation profiles in serum/plasma are due to a change in protein glycosylation or a change in protein concentration.
23944609	9	64	theme	glycosylation	1678:1690	arg1	patterns					1692:1699	their glycosylation patterns	1672:1699	their glycosylation patterns in biofluids	1672:1712	This report represents the most comprehensive study so far of the use of multiple reaction monitoring for the quantitation of glycoproteins and their glycosylation patterns in biofluids.
23944609	9	65	theme	glycoproteins	1654:1666	arg1	quantitation					1638:1649	the quantitation	1634:1649	the quantitation of glycoproteins and their glycosylation patterns in biofluids	1634:1712	This report represents the most comprehensive study so far of the use of multiple reaction monitoring for the quantitation of glycoproteins and their glycosylation patterns in biofluids.
23944609	6	66	theme	liquid	1203:1208	arg1	chromatography					1210:1223	the liquid chromatography	1199:1223	the liquid chromatography	1199:1223	The remarkable sensitivity and selectivity of MRM enable the detection of low abundance IgG glycopeptides, even when IgG was digested directly in serum with no cleanup prior to the liquid chromatography.
23944609	9	67	from	quantitation	1638:1649	arg1	biofluids					1704:1712	biofluids	1704:1712	biofluids	1704:1712	This report represents the most comprehensive study so far of the use of multiple reaction monitoring for the quantitation of glycoproteins and their glycosylation patterns in biofluids.
23944609	9	68	gly	glycoproteins	1654:1666	arg1	glycoproteins					1654:1666	glycoproteins	1654:1666	glycoproteins	1654:1666	This report represents the most comprehensive study so far of the use of multiple reaction monitoring for the quantitation of glycoproteins and their glycosylation patterns in biofluids.
23944609	9	69	theme	reaction	1610:1617	arg1	monitoring					1619:1628	multiple reaction monitoring	1601:1628	multiple reaction monitoring	1601:1628	This report represents the most comprehensive study so far of the use of multiple reaction monitoring for the quantitation of glycoproteins and their glycosylation patterns in biofluids.
23944609	8	70	theme	IgG	1378:1380	arg1	glycopeptides					1382:1394	IgG glycopeptides	1378:1394	IgG glycopeptides	1378:1394	The results show that IgG glycopeptides can be analyzed directly from serum (without enrichment) and yield more accurate abundances when normalized to the protein content.
23944609	6	71	theme	prior	1190:1194	arg1	cleanup					1182:1188	no cleanup	1179:1188	no cleanup prior to the liquid chromatography	1179:1223	The remarkable sensitivity and selectivity of MRM enable the detection of low abundance IgG glycopeptides, even when IgG was digested directly in serum with no cleanup prior to the liquid chromatography.
23944609	9	72	theme	comprehensive	1560:1572	arg1	study					1574:1578	the most comprehensive study	1551:1578	the most comprehensive study so far of the use of multiple reaction monitoring for the quantitation of glycoproteins and their glycosylation patterns in biofluids	1551:1712	This report represents the most comprehensive study so far of the use of multiple reaction monitoring for the quantitation of glycoproteins and their glycosylation patterns in biofluids.
23944609	0	73	theme	multiple	67:74	arg1	monitoring					85:94	multiple reaction monitoring	67:94	multiple reaction monitoring	67:94	Absolute quantitation of immunoglobulin G and its glycoforms using multiple reaction monitoring.
23944609	7	74	theme	orders	1309:1314	arg1	magnitude					1316:1324	3 orders magnitude	1307:1324	3 orders magnitude	1307:1324	Our results show a low limit of detection of 60 amol and a wide dynamic range of 3 orders magnitude for IgG protein quantitation.
23944609	4	75	theme	site-specific	702:714	arg1	level					716:720	a site-specific level	700:720	a site-specific level	700:720	We have developed a method using MRM to monitor protein glycosylation normalized to absolute protein concentrations to examine quantitative changes in glycosylation at a site-specific level.
23944609	6	76	theme	IgG	1110:1112	arg1	glycopeptides					1114:1126	low abundance IgG glycopeptides	1096:1126	low abundance IgG glycopeptides	1096:1126	The remarkable sensitivity and selectivity of MRM enable the detection of low abundance IgG glycopeptides, even when IgG was digested directly in serum with no cleanup prior to the liquid chromatography.
23944609	5	77	from	change	952:957	arg1	concentration					1007:1019	protein concentration	999:1019	protein concentration	999:1019	This new approach provides information regarding both the absolute amount of protein and the site-specific glycosylation profile and will thus be useful to determine if altered glycosylation profiles in serum/plasma are due to a change in protein glycosylation or a change in protein concentration.
23944609	5	77	from	change	952:957	arg1	glycosylation					970:982	protein glycosylation	962:982	protein glycosylation	962:982	This new approach provides information regarding both the absolute amount of protein and the site-specific glycosylation profile and will thus be useful to determine if altered glycosylation profiles in serum/plasma are due to a change in protein glycosylation or a change in protein concentration.
23944609	5	78	theme	glycosylation	900:912	arg1	profiles					914:921	altered glycosylation profiles	892:921	altered glycosylation profiles in serum/plasma	892:937	This new approach provides information regarding both the absolute amount of protein and the site-specific glycosylation profile and will thus be useful to determine if altered glycosylation profiles in serum/plasma are due to a change in protein glycosylation or a change in protein concentration.
23944609	5	79	theme	glycosylation	830:842	arg1	profile					844:850	the site-specific glycosylation profile	812:850	the site-specific glycosylation profile	812:850	This new approach provides information regarding both the absolute amount of protein and the site-specific glycosylation profile and will thus be useful to determine if altered glycosylation profiles in serum/plasma are due to a change in protein glycosylation or a change in protein concentration.
25713063	0	0	theme	high	81:84	arg1	peroxidasin					18:28	Multidomain human peroxidasin 1	0:30	Multidomain human peroxidasin 1	0:30	Multidomain human peroxidasin 1 is a highly glycosylated and stable homotrimeric high spin ferric peroxidase.
25713063	0	0	theme	high	81:84	arg1	peroxidase					98:107	a highly glycosylated and stable homotrimeric high spin ferric peroxidase	35:107	a highly glycosylated and stable homotrimeric high spin ferric peroxidase	35:107	Multidomain human peroxidasin 1 is a highly glycosylated and stable homotrimeric high spin ferric peroxidase.
25713063	5	1	theme	-233	732:735	arg1	±					737:737	±	737:737	±	737:737	The homotrimeric iron protein contains a covalently bound ferric high spin heme per subunit with a standard reduction potential of the Fe(III)/Fe(II) couple of -233 ± 5 mV at pH 7.0.
25713063	7	2	theme	biosynthetic	1047:1058	arg1	function					1060:1067	proposed biosynthetic function	1038:1067	proposed biosynthetic function	1038:1067	This is discussed with respect to its structure and proposed biosynthetic function in collagen IV cross-linking.
25713063	6	3	theme	similar	827:833	arg1	properties					816:825	biophysical properties	804:825	biophysical properties similar to human peroxidases	804:854	Despite sequence homology at the active site and biophysical properties similar to human peroxidases, the catalytic efficiency of bromide oxidation (kcat/KM(app)) of full-length hsPxd01 is rather low but increased upon truncation.
25713063	6	4	theme	hsPxd01	933:939	arg1	efficiency					871:880	the catalytic efficiency	857:880	the catalytic efficiency of bromide oxidation (kcat/KM(app)) of full-length hsPxd01	857:939	Despite sequence homology at the active site and biophysical properties similar to human peroxidases, the catalytic efficiency of bromide oxidation (kcat/KM(app)) of full-length hsPxd01 is rather low but increased upon truncation.
25713063	0	5	theme	homotrimeric	68:79	arg1	peroxidasin					18:28	Multidomain human peroxidasin 1	0:30	Multidomain human peroxidasin 1	0:30	Multidomain human peroxidasin 1 is a highly glycosylated and stable homotrimeric high spin ferric peroxidase.
25713063	0	5	theme	homotrimeric	68:79	arg1	peroxidase					98:107	a highly glycosylated and stable homotrimeric high spin ferric peroxidase	35:107	a highly glycosylated and stable homotrimeric high spin ferric peroxidase	35:107	Multidomain human peroxidasin 1 is a highly glycosylated and stable homotrimeric high spin ferric peroxidase.
25713063	6	6	theme	sequence	763:770	arg1	homology					772:779	sequence homology	763:779	sequence homology at the active site and biophysical properties similar to human peroxidases	763:854	Despite sequence homology at the active site and biophysical properties similar to human peroxidases, the catalytic efficiency of bromide oxidation (kcat/KM(app)) of full-length hsPxd01 is rather low but increased upon truncation.
25713063	7	7	theme	proposed	1038:1045	arg1	function					1060:1067	proposed biosynthetic function	1038:1067	proposed biosynthetic function	1038:1067	This is discussed with respect to its structure and proposed biosynthetic function in collagen IV cross-linking.
25713063	1	8	theme	sulfilimine	226:236	arg1	cross-links					238:248	sulfilimine cross-links	226:248	sulfilimine cross-links	226:248	Human peroxidasin 1 (hsPxd01) is a multidomain heme peroxidase that uses bromide as a cofactor for the formation of sulfilimine cross-links.
25713063	0	9	theme	ferric	91:96	arg1	peroxidasin					18:28	Multidomain human peroxidasin 1	0:30	Multidomain human peroxidasin 1	0:30	Multidomain human peroxidasin 1 is a highly glycosylated and stable homotrimeric high spin ferric peroxidase.
25713063	0	9	theme	ferric	91:96	arg1	peroxidase					98:107	a highly glycosylated and stable homotrimeric high spin ferric peroxidase	35:107	a highly glycosylated and stable homotrimeric high spin ferric peroxidase	35:107	Multidomain human peroxidasin 1 is a highly glycosylated and stable homotrimeric high spin ferric peroxidase.
25713063	4	10	theme	oligomeric	514:523	arg1	structure					525:533	the oligomeric structure	510:533	the oligomeric structure	510:533	The N-glycosylation site occupancy and disulfide pattern, the oligomeric structure, and unfolding pathway are reported.
25713063	2	11	theme	critical	270:277	arg1	reinforcement					290:302	critical structural reinforcement	270:302	critical structural reinforcement to collagen IV scaffolds	270:327	The latter confers critical structural reinforcement to collagen IV scaffolds.
25713063	1	12	theme	cross-links	238:248	arg1	formation					213:221	the formation	209:221	the formation of sulfilimine cross-links	209:248	Human peroxidasin 1 (hsPxd01) is a multidomain heme peroxidase that uses bromide as a cofactor for the formation of sulfilimine cross-links.
25713063	0	13	theme	spin	86:89	arg1	peroxidasin					18:28	Multidomain human peroxidasin 1	0:30	Multidomain human peroxidasin 1	0:30	Multidomain human peroxidasin 1 is a highly glycosylated and stable homotrimeric high spin ferric peroxidase.
25713063	0	13	theme	spin	86:89	arg1	peroxidase					98:107	a highly glycosylated and stable homotrimeric high spin ferric peroxidase	35:107	a highly glycosylated and stable homotrimeric high spin ferric peroxidase	35:107	Multidomain human peroxidasin 1 is a highly glycosylated and stable homotrimeric high spin ferric peroxidase.
25713063	5	14	theme	standard	671:678	arg1	potential					690:698	a standard reduction potential	669:698	a standard reduction potential of the Fe(III)/Fe(II) couple of -233 ± 5 mV at pH 7.0	669:752	The homotrimeric iron protein contains a covalently bound ferric high spin heme per subunit with a standard reduction potential of the Fe(III)/Fe(II) couple of -233 ± 5 mV at pH 7.0.
25713063	5	15	theme	bound	624:628	arg1	heme					647:650	a covalently bound ferric high spin heme	611:650	a covalently bound ferric high spin heme per subunit with a standard reduction potential of the Fe(III)/Fe(II) couple of -233 ± 5 mV at pH 7.0	611:752	The homotrimeric iron protein contains a covalently bound ferric high spin heme per subunit with a standard reduction potential of the Fe(III)/Fe(II) couple of -233 ± 5 mV at pH 7.0.
25713063	5	16	with	heme	647:650	arg1	potential					690:698	a standard reduction potential	669:698	a standard reduction potential of the Fe(III)/Fe(II) couple of -233 ± 5 mV at pH 7.0	669:752	The homotrimeric iron protein contains a covalently bound ferric high spin heme per subunit with a standard reduction potential of the Fe(III)/Fe(II) couple of -233 ± 5 mV at pH 7.0.
25713063	5	17	theme	high	637:640	arg1	heme					647:650	a covalently bound ferric high spin heme	611:650	a covalently bound ferric high spin heme per subunit with a standard reduction potential of the Fe(III)/Fe(II) couple of -233 ± 5 mV at pH 7.0	611:752	The homotrimeric iron protein contains a covalently bound ferric high spin heme per subunit with a standard reduction potential of the Fe(III)/Fe(II) couple of -233 ± 5 mV at pH 7.0.
25713063	5	18	theme	ferric	630:635	arg1	heme					647:650	a covalently bound ferric high spin heme	611:650	a covalently bound ferric high spin heme per subunit with a standard reduction potential of the Fe(III)/Fe(II) couple of -233 ± 5 mV at pH 7.0	611:752	The homotrimeric iron protein contains a covalently bound ferric high spin heme per subunit with a standard reduction potential of the Fe(III)/Fe(II) couple of -233 ± 5 mV at pH 7.0.
25713063	1	19	theme	multidomain	145:155	arg1	peroxidase					162:171	a multidomain heme peroxidase	143:171	a multidomain heme peroxidase that uses bromide as a cofactor for the formation of sulfilimine cross-links	143:248	Human peroxidasin 1 (hsPxd01) is a multidomain heme peroxidase that uses bromide as a cofactor for the formation of sulfilimine cross-links.
25713063	1	19	theme	multidomain	145:155	arg1	peroxidasin					116:126	Human peroxidasin 1	110:128	Human peroxidasin 1 (hsPxd01)	110:138	Human peroxidasin 1 (hsPxd01) is a multidomain heme peroxidase that uses bromide as a cofactor for the formation of sulfilimine cross-links.
25713063	5	20	theme	spin	642:645	arg1	heme					647:650	a covalently bound ferric high spin heme	611:650	a covalently bound ferric high spin heme per subunit with a standard reduction potential of the Fe(III)/Fe(II) couple of -233 ± 5 mV at pH 7.0	611:752	The homotrimeric iron protein contains a covalently bound ferric high spin heme per subunit with a standard reduction potential of the Fe(III)/Fe(II) couple of -233 ± 5 mV at pH 7.0.
25713063	5	21	theme	homotrimeric	576:587	arg1	protein					594:600	The homotrimeric iron protein	572:600	The homotrimeric iron protein	572:600	The homotrimeric iron protein contains a covalently bound ferric high spin heme per subunit with a standard reduction potential of the Fe(III)/Fe(II) couple of -233 ± 5 mV at pH 7.0.
25713063	3	22	theme	nonenzymatic	383:394	arg1	domains					396:402	nonenzymatic domains	383:402	nonenzymatic domains	383:402	Here, hsPxd01 and various truncated variants lacking nonenzymatic domains were recombinantly expressed in HEK cell lines.
25713063	1	23	theme	heme	157:160	arg1	peroxidase					162:171	a multidomain heme peroxidase	143:171	a multidomain heme peroxidase that uses bromide as a cofactor for the formation of sulfilimine cross-links	143:248	Human peroxidasin 1 (hsPxd01) is a multidomain heme peroxidase that uses bromide as a cofactor for the formation of sulfilimine cross-links.
25713063	1	23	theme	heme	157:160	arg1	peroxidasin					116:126	Human peroxidasin 1	110:128	Human peroxidasin 1 (hsPxd01)	110:138	Human peroxidasin 1 (hsPxd01) is a multidomain heme peroxidase that uses bromide as a cofactor for the formation of sulfilimine cross-links.
25713063	0	24	theme	human	12:16	arg1	peroxidasin					18:28	Multidomain human peroxidasin 1	0:30	Multidomain human peroxidasin 1	0:30	Multidomain human peroxidasin 1 is a highly glycosylated and stable homotrimeric high spin ferric peroxidase.
25713063	0	24	theme	human	12:16	arg1	peroxidase					98:107	a highly glycosylated and stable homotrimeric high spin ferric peroxidase	35:107	a highly glycosylated and stable homotrimeric high spin ferric peroxidase	35:107	Multidomain human peroxidasin 1 is a highly glycosylated and stable homotrimeric high spin ferric peroxidase.
25713063	4	25	theme	disulfide	491:499	arg1	pattern					501:507	disulfide pattern	491:507	disulfide pattern	491:507	The N-glycosylation site occupancy and disulfide pattern, the oligomeric structure, and unfolding pathway are reported.
25713063	5	26	theme	iron	589:592	arg1	protein					594:600	The homotrimeric iron protein	572:600	The homotrimeric iron protein	572:600	The homotrimeric iron protein contains a covalently bound ferric high spin heme per subunit with a standard reduction potential of the Fe(III)/Fe(II) couple of -233 ± 5 mV at pH 7.0.
25713063	2	27	theme	collagen	307:314	arg1	scaffolds					319:327	collagen IV scaffolds	307:327	collagen IV scaffolds	307:327	The latter confers critical structural reinforcement to collagen IV scaffolds.
25713063	6	28	theme	human	838:842	arg1	peroxidases					844:854	human peroxidases	838:854	human peroxidases	838:854	Despite sequence homology at the active site and biophysical properties similar to human peroxidases, the catalytic efficiency of bromide oxidation (kcat/KM(app)) of full-length hsPxd01 is rather low but increased upon truncation.
25713063	0	29	theme	Multidomain	0:10	arg1	peroxidasin					18:28	Multidomain human peroxidasin 1	0:30	Multidomain human peroxidasin 1	0:30	Multidomain human peroxidasin 1 is a highly glycosylated and stable homotrimeric high spin ferric peroxidase.
25713063	0	29	theme	Multidomain	0:10	arg1	peroxidase					98:107	a highly glycosylated and stable homotrimeric high spin ferric peroxidase	35:107	a highly glycosylated and stable homotrimeric high spin ferric peroxidase	35:107	Multidomain human peroxidasin 1 is a highly glycosylated and stable homotrimeric high spin ferric peroxidase.
25713063	6	30	from	site	795:798	arg1	homology					772:779	sequence homology	763:779	sequence homology at the active site and biophysical properties similar to human peroxidases	763:854	Despite sequence homology at the active site and biophysical properties similar to human peroxidases, the catalytic efficiency of bromide oxidation (kcat/KM(app)) of full-length hsPxd01 is rather low but increased upon truncation.
25713063	3	31	theme	HEK	436:438	arg1	lines					445:449	HEK cell lines	436:449	HEK cell lines	436:449	Here, hsPxd01 and various truncated variants lacking nonenzymatic domains were recombinantly expressed in HEK cell lines.
25713063	3	32	theme	truncated	356:364	arg1	variants					366:373	various truncated variants	348:373	various truncated variants lacking nonenzymatic domains	348:402	Here, hsPxd01 and various truncated variants lacking nonenzymatic domains were recombinantly expressed in HEK cell lines.
25713063	5	33	theme	Fe	707:708	arg1	/Fe					714:716	the Fe(III)/Fe(II)	703:720	the Fe(III)/Fe(II) couple of -233 ± 5 mV at pH 7.0	703:752	The homotrimeric iron protein contains a covalently bound ferric high spin heme per subunit with a standard reduction potential of the Fe(III)/Fe(II) couple of -233 ± 5 mV at pH 7.0.
25713063	5	34	contain	contains	602:609	arg1	protein					594:600	The homotrimeric iron protein	572:600	The homotrimeric iron protein	572:600	The homotrimeric iron protein contains a covalently bound ferric high spin heme per subunit with a standard reduction potential of the Fe(III)/Fe(II) couple of -233 ± 5 mV at pH 7.0.
25713063	5	34	contain	contains	602:609	arg2	heme					647:650	a covalently bound ferric high spin heme	611:650	a covalently bound ferric high spin heme per subunit with a standard reduction potential of the Fe(III)/Fe(II) couple of -233 ± 5 mV at pH 7.0	611:752	The homotrimeric iron protein contains a covalently bound ferric high spin heme per subunit with a standard reduction potential of the Fe(III)/Fe(II) couple of -233 ± 5 mV at pH 7.0.
25713063	2	35	theme	structural	279:288	arg1	reinforcement					290:302	critical structural reinforcement	270:302	critical structural reinforcement to collagen IV scaffolds	270:327	The latter confers critical structural reinforcement to collagen IV scaffolds.
25713063	6	36	theme	catalytic	861:869	arg1	efficiency					871:880	the catalytic efficiency	857:880	the catalytic efficiency of bromide oxidation (kcat/KM(app)) of full-length hsPxd01	857:939	Despite sequence homology at the active site and biophysical properties similar to human peroxidases, the catalytic efficiency of bromide oxidation (kcat/KM(app)) of full-length hsPxd01 is rather low but increased upon truncation.
25713063	5	37	theme	5	739:739	arg1	±					737:737	±	737:737	±	737:737	The homotrimeric iron protein contains a covalently bound ferric high spin heme per subunit with a standard reduction potential of the Fe(III)/Fe(II) couple of -233 ± 5 mV at pH 7.0.
25713063	7	38	from	structure	1024:1032	arg1	cross-linking					1084:1096	collagen IV cross-linking	1072:1096	collagen IV cross-linking	1072:1096	This is discussed with respect to its structure and proposed biosynthetic function in collagen IV cross-linking.
25713063	6	39	theme	biophysical	804:814	arg1	properties					816:825	biophysical properties	804:825	biophysical properties similar to human peroxidases	804:854	Despite sequence homology at the active site and biophysical properties similar to human peroxidases, the catalytic efficiency of bromide oxidation (kcat/KM(app)) of full-length hsPxd01 is rather low but increased upon truncation.
25713063	3	40	theme	cell	440:443	arg1	lines					445:449	HEK cell lines	436:449	HEK cell lines	436:449	Here, hsPxd01 and various truncated variants lacking nonenzymatic domains were recombinantly expressed in HEK cell lines.
25713063	6	41	theme	full-length	921:931	arg1	hsPxd01					933:939	full-length hsPxd01	921:939	full-length hsPxd01	921:939	Despite sequence homology at the active site and biophysical properties similar to human peroxidases, the catalytic efficiency of bromide oxidation (kcat/KM(app)) of full-length hsPxd01 is rather low but increased upon truncation.
25713063	4	42	theme	site	472:475	arg1	occupancy					477:485	The N-glycosylation site occupancy	452:485	The N-glycosylation site occupancy	452:485	The N-glycosylation site occupancy and disulfide pattern, the oligomeric structure, and unfolding pathway are reported.
25713063	6	43	from	properties	816:825	arg1	homology					772:779	sequence homology	763:779	sequence homology at the active site and biophysical properties similar to human peroxidases	763:854	Despite sequence homology at the active site and biophysical properties similar to human peroxidases, the catalytic efficiency of bromide oxidation (kcat/KM(app)) of full-length hsPxd01 is rather low but increased upon truncation.
25713063	7	44	from	function	1060:1067	arg1	cross-linking					1084:1096	collagen IV cross-linking	1072:1096	collagen IV cross-linking	1072:1096	This is discussed with respect to its structure and proposed biosynthetic function in collagen IV cross-linking.
25713063	0	45	theme	glycosylated	44:55	arg1	peroxidasin					18:28	Multidomain human peroxidasin 1	0:30	Multidomain human peroxidasin 1	0:30	Multidomain human peroxidasin 1 is a highly glycosylated and stable homotrimeric high spin ferric peroxidase.
25713063	0	45	theme	glycosylated	44:55	arg1	peroxidase					98:107	a highly glycosylated and stable homotrimeric high spin ferric peroxidase	35:107	a highly glycosylated and stable homotrimeric high spin ferric peroxidase	35:107	Multidomain human peroxidasin 1 is a highly glycosylated and stable homotrimeric high spin ferric peroxidase.
25713063	5	46	theme	/Fe	714:716	arg1	potential					690:698	a standard reduction potential	669:698	a standard reduction potential of the Fe(III)/Fe(II) couple of -233 ± 5 mV at pH 7.0	669:752	The homotrimeric iron protein contains a covalently bound ferric high spin heme per subunit with a standard reduction potential of the Fe(III)/Fe(II) couple of -233 ± 5 mV at pH 7.0.
25713063	5	47	theme	reduction	680:688	arg1	potential					690:698	a standard reduction potential	669:698	a standard reduction potential of the Fe(III)/Fe(II) couple of -233 ± 5 mV at pH 7.0	669:752	The homotrimeric iron protein contains a covalently bound ferric high spin heme per subunit with a standard reduction potential of the Fe(III)/Fe(II) couple of -233 ± 5 mV at pH 7.0.
25713063	4	48	theme	N-glycosylation	456:470	arg1	occupancy					477:485	The N-glycosylation site occupancy	452:485	The N-glycosylation site occupancy	452:485	The N-glycosylation site occupancy and disulfide pattern, the oligomeric structure, and unfolding pathway are reported.
25713063	1	49	theme	Human	110:114	arg1	peroxidase					162:171	a multidomain heme peroxidase	143:171	a multidomain heme peroxidase that uses bromide as a cofactor for the formation of sulfilimine cross-links	143:248	Human peroxidasin 1 (hsPxd01) is a multidomain heme peroxidase that uses bromide as a cofactor for the formation of sulfilimine cross-links.
25713063	1	49	theme	Human	110:114	arg1	peroxidasin					116:126	Human peroxidasin 1	110:128	Human peroxidasin 1 (hsPxd01)	110:138	Human peroxidasin 1 (hsPxd01) is a multidomain heme peroxidase that uses bromide as a cofactor for the formation of sulfilimine cross-links.
25713063	1	49	theme	Human	110:114	arg1	hsPxd01					131:137	hsPxd01	131:137	hsPxd01	131:137	Human peroxidasin 1 (hsPxd01) is a multidomain heme peroxidase that uses bromide as a cofactor for the formation of sulfilimine cross-links.
25713063	7	50	theme	collagen	1072:1079	arg1	cross-linking					1084:1096	collagen IV cross-linking	1072:1096	collagen IV cross-linking	1072:1096	This is discussed with respect to its structure and proposed biosynthetic function in collagen IV cross-linking.
25713063	6	51	theme	bromide	885:891	arg1	oxidation					893:901	bromide oxidation	885:901	bromide oxidation	885:901	Despite sequence homology at the active site and biophysical properties similar to human peroxidases, the catalytic efficiency of bromide oxidation (kcat/KM(app)) of full-length hsPxd01 is rather low but increased upon truncation.
25713063	6	52	theme	active	788:793	arg1	site					795:798	the active site	784:798	the active site	784:798	Despite sequence homology at the active site and biophysical properties similar to human peroxidases, the catalytic efficiency of bromide oxidation (kcat/KM(app)) of full-length hsPxd01 is rather low but increased upon truncation.
25713063	4	53	theme	unfolding	540:548	arg1	pathway					550:556	unfolding pathway	540:556	unfolding pathway	540:556	The N-glycosylation site occupancy and disulfide pattern, the oligomeric structure, and unfolding pathway are reported.
25713063	5	54	dep	/Fe	714:716	arg1	couple					722:727	couple	722:727	couple of -233 ± 5 mV at pH 7.0	722:752	The homotrimeric iron protein contains a covalently bound ferric high spin heme per subunit with a standard reduction potential of the Fe(III)/Fe(II) couple of -233 ± 5 mV at pH 7.0.
25713063	2	55	theme	IV	316:317	arg1	scaffolds					319:327	collagen IV scaffolds	307:327	collagen IV scaffolds	307:327	The latter confers critical structural reinforcement to collagen IV scaffolds.
25713063	4	56	gly	N-glycosylation	456:470	arg2	site					472:475	The N-glycosylation site occupancy	452:485	The N-glycosylation site occupancy	452:485	The N-glycosylation site occupancy and disulfide pattern, the oligomeric structure, and unfolding pathway are reported.
25713063	4	56	gly	N-glycosylation	456:470	arg2	occupancy					477:485	The N-glycosylation site occupancy	452:485	The N-glycosylation site occupancy	452:485	The N-glycosylation site occupancy and disulfide pattern, the oligomeric structure, and unfolding pathway are reported.
25713063	0	57	theme	stable	61:66	arg1	peroxidasin					18:28	Multidomain human peroxidasin 1	0:30	Multidomain human peroxidasin 1	0:30	Multidomain human peroxidasin 1 is a highly glycosylated and stable homotrimeric high spin ferric peroxidase.
25713063	0	57	theme	stable	61:66	arg1	peroxidase					98:107	a highly glycosylated and stable homotrimeric high spin ferric peroxidase	35:107	a highly glycosylated and stable homotrimeric high spin ferric peroxidase	35:107	Multidomain human peroxidasin 1 is a highly glycosylated and stable homotrimeric high spin ferric peroxidase.
25713063	6	58	dep	efficiency	871:880	arg1	app					912:914	app	912:914	app	912:914	Despite sequence homology at the active site and biophysical properties similar to human peroxidases, the catalytic efficiency of bromide oxidation (kcat/KM(app)) of full-length hsPxd01 is rather low but increased upon truncation.
25713063	6	58	dep	efficiency	871:880	arg1	kcat/KM					904:910	kcat/KM	904:910	kcat/KM(app)	904:915	Despite sequence homology at the active site and biophysical properties similar to human peroxidases, the catalytic efficiency of bromide oxidation (kcat/KM(app)) of full-length hsPxd01 is rather low but increased upon truncation.
25713063	0	59	gly	glycosylated	44:55	arg1	peroxidasin					18:28	Multidomain human peroxidasin 1	0:30	Multidomain human peroxidasin 1	0:30	Multidomain human peroxidasin 1 is a highly glycosylated and stable homotrimeric high spin ferric peroxidase.
25713063	0	59	gly	glycosylated	44:55	arg1	peroxidase					98:107	a highly glycosylated and stable homotrimeric high spin ferric peroxidase	35:107	a highly glycosylated and stable homotrimeric high spin ferric peroxidase	35:107	Multidomain human peroxidasin 1 is a highly glycosylated and stable homotrimeric high spin ferric peroxidase.
25713063	6	60	theme	oxidation	893:901	arg1	efficiency					871:880	the catalytic efficiency	857:880	the catalytic efficiency of bromide oxidation (kcat/KM(app)) of full-length hsPxd01	857:939	Despite sequence homology at the active site and biophysical properties similar to human peroxidases, the catalytic efficiency of bromide oxidation (kcat/KM(app)) of full-length hsPxd01 is rather low but increased upon truncation.
25713063	3	61	theme	various	348:354	arg1	variants					366:373	various truncated variants	348:373	various truncated variants lacking nonenzymatic domains	348:402	Here, hsPxd01 and various truncated variants lacking nonenzymatic domains were recombinantly expressed in HEK cell lines.
16716077	7	0	theme	Mut-Fe	1454:1459	arg1	hTF					1464:1466	Mut-Fe(C) hTF	1454:1466	Mut-Fe(C) hTF	1454:1466	The rate of iron release from Fe(C) hTF and Mut-Fe(C) hTF in complex with the sTFR and the sTFR mutants at pH 5.6 reveals that only the N317D mutant has a significant effect.
16716077	2	1	contain	has	346:348	arg2	Asn317					394:399	Asn317	394:399	Asn317	394:399	The sTFR (residues 121-760) has three N-linked glycosylation sites (Asn251, Asn317, and Asn727).
16716077	2	1	contain	has	346:348	arg1	sTFR					322:325	The sTFR	318:325	The sTFR (residues 121-760)	318:344	The sTFR (residues 121-760) has three N-linked glycosylation sites (Asn251, Asn317, and Asn727).
16716077	2	1	contain	has	346:348	arg2	Asn727					406:411	Asn727	406:411	Asn727	406:411	The sTFR (residues 121-760) has three N-linked glycosylation sites (Asn251, Asn317, and Asn727).
16716077	2	1	contain	has	346:348	arg2	sites					379:383	three N-linked glycosylation sites	350:383	three N-linked glycosylation sites (Asn251, Asn317, and Asn727)	350:412	The sTFR (residues 121-760) has three N-linked glycosylation sites (Asn251, Asn317, and Asn727).
16716077	2	1	contain	has	346:348	arg2	Asn251					386:391	Asn251	386:391	Asn251	386:391	The sTFR (residues 121-760) has three N-linked glycosylation sites (Asn251, Asn317, and Asn727).
16716077	2	1	contain	has	346:348	arg1	residues					328:335	residues 121-760	328:343	residues 121-760	328:343	The sTFR (residues 121-760) has three N-linked glycosylation sites (Asn251, Asn317, and Asn727).
16716077	6	2	theme	release	1210:1216	arg1	rate					1218:1221	a 30-fold slower iron release rate	1188:1221	designated Mut-Fe(C) hTF that features a 30-fold slower iron release rate	1149:1221	The effect of glycosylation on binding to diferric human transferrin (Fe(2) hTF), an authentic monoferric hTF with iron in the C-lobe (designated Fe(C) hTF), and a mutant (designated Mut-Fe(C) hTF that features a 30-fold slower iron release rate) was determined by surface plasmon resonance; a small ( approximately 20%) but consistent difference is noted for the binding of Fe(C) hTF and the Mut-Fe(C) hTF to the sTFR N317D mutant.
16716077	6	3	from	hTF	1083:1085	arg1	mutant					1141:1146	a mutant	1139:1146	a mutant (designated Mut-Fe(C) hTF that features a 30-fold slower iron release rate)	1139:1222	The effect of glycosylation on binding to diferric human transferrin (Fe(2) hTF), an authentic monoferric hTF with iron in the C-lobe (designated Fe(C) hTF), and a mutant (designated Mut-Fe(C) hTF that features a 30-fold slower iron release rate) was determined by surface plasmon resonance; a small ( approximately 20%) but consistent difference is noted for the binding of Fe(C) hTF and the Mut-Fe(C) hTF to the sTFR N317D mutant.
16716077	6	3	from	hTF	1083:1085	arg1	hTF					1129:1131	designated Fe(C) hTF	1112:1131	designated Fe(C) hTF	1112:1131	The effect of glycosylation on binding to diferric human transferrin (Fe(2) hTF), an authentic monoferric hTF with iron in the C-lobe (designated Fe(C) hTF), and a mutant (designated Mut-Fe(C) hTF that features a 30-fold slower iron release rate) was determined by surface plasmon resonance; a small ( approximately 20%) but consistent difference is noted for the binding of Fe(C) hTF and the Mut-Fe(C) hTF to the sTFR N317D mutant.
16716077	6	3	from	hTF	1083:1085	arg1	C-lobe					1104:1109	the C-lobe	1100:1109	the C-lobe (designated Fe(C) hTF)	1100:1132	The effect of glycosylation on binding to diferric human transferrin (Fe(2) hTF), an authentic monoferric hTF with iron in the C-lobe (designated Fe(C) hTF), and a mutant (designated Mut-Fe(C) hTF that features a 30-fold slower iron release rate) was determined by surface plasmon resonance; a small ( approximately 20%) but consistent difference is noted for the binding of Fe(C) hTF and the Mut-Fe(C) hTF to the sTFR N317D mutant.
16716077	7	4	theme	C	1443:1443	arg1	hTF					1446:1448	Fe(C) hTF	1440:1448	Fe(C) hTF	1440:1448	The rate of iron release from Fe(C) hTF and Mut-Fe(C) hTF in complex with the sTFR and the sTFR mutants at pH 5.6 reveals that only the N317D mutant has a significant effect.
16716077	6	5	theme	human	1028:1032	arg1	transferrin					1034:1044	diferric human transferrin	1019:1044	diferric human transferrin (Fe(2) hTF)	1019:1056	The effect of glycosylation on binding to diferric human transferrin (Fe(2) hTF), an authentic monoferric hTF with iron in the C-lobe (designated Fe(C) hTF), and a mutant (designated Mut-Fe(C) hTF that features a 30-fold slower iron release rate) was determined by surface plasmon resonance; a small ( approximately 20%) but consistent difference is noted for the binding of Fe(C) hTF and the Mut-Fe(C) hTF to the sTFR N317D mutant.
16716077	6	5	theme	human	1028:1032	arg1	hTF					1053:1055	Fe(2) hTF	1047:1055	Fe(2) hTF	1047:1055	The effect of glycosylation on binding to diferric human transferrin (Fe(2) hTF), an authentic monoferric hTF with iron in the C-lobe (designated Fe(C) hTF), and a mutant (designated Mut-Fe(C) hTF that features a 30-fold slower iron release rate) was determined by surface plasmon resonance; a small ( approximately 20%) but consistent difference is noted for the binding of Fe(C) hTF and the Mut-Fe(C) hTF to the sTFR N317D mutant.
16716077	6	6	theme	designated	1149:1158	arg1	hTF					1170:1172	designated Mut-Fe(C) hTF	1149:1172	designated Mut-Fe(C) hTF that features a 30-fold slower iron release rate	1149:1221	The effect of glycosylation on binding to diferric human transferrin (Fe(2) hTF), an authentic monoferric hTF with iron in the C-lobe (designated Fe(C) hTF), and a mutant (designated Mut-Fe(C) hTF that features a 30-fold slower iron release rate) was determined by surface plasmon resonance; a small ( approximately 20%) but consistent difference is noted for the binding of Fe(C) hTF and the Mut-Fe(C) hTF to the sTFR N317D mutant.
16716077	1	7	theme	receptor	153:160	arg1	portion					126:132	the soluble portion	114:132	the soluble portion of the transferrin receptor (sTFR)	114:167	Production of the soluble portion of the transferrin receptor (sTFR) by baby hamster kidney (BHK) cells is described, and the effect of glycosylation on the biological function of sTFR is evaluated for the first time.
16716077	7	8	theme	Fe	1440:1441	arg1	hTF					1446:1448	Fe(C) hTF	1440:1448	Fe(C) hTF	1440:1448	The rate of iron release from Fe(C) hTF and Mut-Fe(C) hTF in complex with the sTFR and the sTFR mutants at pH 5.6 reveals that only the N317D mutant has a significant effect.
16716077	6	9	theme	authentic	1062:1070	arg1	hTF					1083:1085	an authentic monoferric hTF	1059:1085	an authentic monoferric hTF with iron in the C-lobe (designated Fe(C) hTF), and a mutant (designated Mut-Fe(C) hTF that features a 30-fold slower iron release rate)	1059:1222	The effect of glycosylation on binding to diferric human transferrin (Fe(2) hTF), an authentic monoferric hTF with iron in the C-lobe (designated Fe(C) hTF), and a mutant (designated Mut-Fe(C) hTF that features a 30-fold slower iron release rate) was determined by surface plasmon resonance; a small ( approximately 20%) but consistent difference is noted for the binding of Fe(C) hTF and the Mut-Fe(C) hTF to the sTFR N317D mutant.
16716077	3	10	theme	culture	476:482	arg1	medium					484:489	the tissue culture medium	465:489	the tissue culture medium ( approximately 40 mg/L)	465:514	Although fully glycosylated sTFR is secreted into the tissue culture medium ( approximately 40 mg/L), no nonglycosylated sTFR could be produced, suggesting that carbohydrate is critical to the folding, stability, and/or secretion of the receptor.
16716077	3	10	theme	culture	476:482	arg1	mg/L					510:513	approximately 40 mg/L	493:513	approximately 40 mg/L	493:513	Although fully glycosylated sTFR is secreted into the tissue culture medium ( approximately 40 mg/L), no nonglycosylated sTFR could be produced, suggesting that carbohydrate is critical to the folding, stability, and/or secretion of the receptor.
16716077	7	11	theme	release	1427:1433	arg1	rate					1414:1417	The rate	1410:1417	The rate of iron release from Fe(C) hTF and Mut-Fe(C) hTF in complex with the sTFR and the sTFR mutants at pH 5.6	1410:1522	The rate of iron release from Fe(C) hTF and Mut-Fe(C) hTF in complex with the sTFR and the sTFR mutants at pH 5.6 reveals that only the N317D mutant has a significant effect.
16716077	7	12	from	rate	1414:1417	arg1	hTF					1464:1466	Mut-Fe(C) hTF	1454:1466	Mut-Fe(C) hTF	1454:1466	The rate of iron release from Fe(C) hTF and Mut-Fe(C) hTF in complex with the sTFR and the sTFR mutants at pH 5.6 reveals that only the N317D mutant has a significant effect.
16716077	7	12	from	rate	1414:1417	arg1	mutants					1506:1512	the sTFR mutants	1497:1512	the sTFR mutants at pH 5.6	1497:1522	The rate of iron release from Fe(C) hTF and Mut-Fe(C) hTF in complex with the sTFR and the sTFR mutants at pH 5.6 reveals that only the N317D mutant has a significant effect.
16716077	7	12	from	rate	1414:1417	arg1	hTF					1446:1448	Fe(C) hTF	1440:1448	Fe(C) hTF	1440:1448	The rate of iron release from Fe(C) hTF and Mut-Fe(C) hTF in complex with the sTFR and the sTFR mutants at pH 5.6 reveals that only the N317D mutant has a significant effect.
16716077	5	13	theme	carbohydrate	929:940	arg1	dimerization					881:892	dimerization	881:892	dimerization of the sTFR	881:904	Analysis by electrospray ionization mass spectrometry confirms dimerization of the sTFR and the absence of the carbohydrate at the single site in each mutant.
16716077	5	13	theme	carbohydrate	929:940	arg1	absence					914:920	the absence	910:920	the absence of the carbohydrate	910:940	Analysis by electrospray ionization mass spectrometry confirms dimerization of the sTFR and the absence of the carbohydrate at the single site in each mutant.
16716077	7	14	theme	significant	1565:1575	arg1	effect					1577:1582	a significant effect	1563:1582	a significant effect	1563:1582	The rate of iron release from Fe(C) hTF and Mut-Fe(C) hTF in complex with the sTFR and the sTFR mutants at pH 5.6 reveals that only the N317D mutant has a significant effect.
16716077	4	15	theme	N317D	796:800	arg1	mutant					802:807	the N317D mutant	792:807	the N317D mutant	792:807	Mutants in which glycosylation at positions 251 and 727 (N251D and N727D) is eliminated are well expressed, whereas production of the N317D mutant is poor.
16716077	6	16	theme	hTF	1380:1382	arg1	binding					1341:1347	the binding	1337:1347	the binding of Fe(C) hTF and the Mut-Fe(C) hTF to the sTFR N317D mutant	1337:1407	The effect of glycosylation on binding to diferric human transferrin (Fe(2) hTF), an authentic monoferric hTF with iron in the C-lobe (designated Fe(C) hTF), and a mutant (designated Mut-Fe(C) hTF that features a 30-fold slower iron release rate) was determined by surface plasmon resonance; a small ( approximately 20%) but consistent difference is noted for the binding of Fe(C) hTF and the Mut-Fe(C) hTF to the sTFR N317D mutant.
16716077	4	17	from	727	714:716	arg1	glycosylation					679:691	glycosylation	679:691	glycosylation at positions 251 and 727 (N251D and N727D)	679:734	Mutants in which glycosylation at positions 251 and 727 (N251D and N727D) is eliminated are well expressed, whereas production of the N317D mutant is poor.
16716077	1	18	theme	hamster	177:183	arg1	BHK					193:195	BHK	193:195	BHK	193:195	Production of the soluble portion of the transferrin receptor (sTFR) by baby hamster kidney (BHK) cells is described, and the effect of glycosylation on the biological function of sTFR is evaluated for the first time.
16716077	1	18	theme	hamster	177:183	arg1	kidney					185:190	baby hamster kidney	172:190	baby hamster kidney (BHK) cells	172:202	Production of the soluble portion of the transferrin receptor (sTFR) by baby hamster kidney (BHK) cells is described, and the effect of glycosylation on the biological function of sTFR is evaluated for the first time.
16716077	6	19	theme	Fe	1123:1124	arg1	hTF					1129:1131	designated Fe(C) hTF	1112:1131	designated Fe(C) hTF	1112:1131	The effect of glycosylation on binding to diferric human transferrin (Fe(2) hTF), an authentic monoferric hTF with iron in the C-lobe (designated Fe(C) hTF), and a mutant (designated Mut-Fe(C) hTF that features a 30-fold slower iron release rate) was determined by surface plasmon resonance; a small ( approximately 20%) but consistent difference is noted for the binding of Fe(C) hTF and the Mut-Fe(C) hTF to the sTFR N317D mutant.
16716077	6	19	theme	Fe	1123:1124	arg1	C-lobe					1104:1109	the C-lobe	1100:1109	the C-lobe (designated Fe(C) hTF)	1100:1132	The effect of glycosylation on binding to diferric human transferrin (Fe(2) hTF), an authentic monoferric hTF with iron in the C-lobe (designated Fe(C) hTF), and a mutant (designated Mut-Fe(C) hTF that features a 30-fold slower iron release rate) was determined by surface plasmon resonance; a small ( approximately 20%) but consistent difference is noted for the binding of Fe(C) hTF and the Mut-Fe(C) hTF to the sTFR N317D mutant.
16716077	6	20	dep	hTF	1380:1382	arg1	C					1377:1377	C	1377:1377	C	1377:1377	The effect of glycosylation on binding to diferric human transferrin (Fe(2) hTF), an authentic monoferric hTF with iron in the C-lobe (designated Fe(C) hTF), and a mutant (designated Mut-Fe(C) hTF that features a 30-fold slower iron release rate) was determined by surface plasmon resonance; a small ( approximately 20%) but consistent difference is noted for the binding of Fe(C) hTF and the Mut-Fe(C) hTF to the sTFR N317D mutant.
16716077	6	21	theme	Mut-Fe	1370:1375	arg1	hTF					1380:1382	the Mut-Fe(C) hTF	1366:1382	the Mut-Fe(C) hTF	1366:1382	The effect of glycosylation on binding to diferric human transferrin (Fe(2) hTF), an authentic monoferric hTF with iron in the C-lobe (designated Fe(C) hTF), and a mutant (designated Mut-Fe(C) hTF that features a 30-fold slower iron release rate) was determined by surface plasmon resonance; a small ( approximately 20%) but consistent difference is noted for the binding of Fe(C) hTF and the Mut-Fe(C) hTF to the sTFR N317D mutant.
16716077	6	22	theme	consistent	1302:1311	arg1	difference					1313:1322	consistent difference	1302:1322	consistent difference	1302:1322	The effect of glycosylation on binding to diferric human transferrin (Fe(2) hTF), an authentic monoferric hTF with iron in the C-lobe (designated Fe(C) hTF), and a mutant (designated Mut-Fe(C) hTF that features a 30-fold slower iron release rate) was determined by surface plasmon resonance; a small ( approximately 20%) but consistent difference is noted for the binding of Fe(C) hTF and the Mut-Fe(C) hTF to the sTFR N317D mutant.
16716077	6	23	with	hTF	1083:1085	arg1	iron					1092:1095	iron	1092:1095	iron	1092:1095	The effect of glycosylation on binding to diferric human transferrin (Fe(2) hTF), an authentic monoferric hTF with iron in the C-lobe (designated Fe(C) hTF), and a mutant (designated Mut-Fe(C) hTF that features a 30-fold slower iron release rate) was determined by surface plasmon resonance; a small ( approximately 20%) but consistent difference is noted for the binding of Fe(C) hTF and the Mut-Fe(C) hTF to the sTFR N317D mutant.
16716077	6	24	theme	Mut-Fe	1160:1165	arg1	hTF					1170:1172	designated Mut-Fe(C) hTF	1149:1172	designated Mut-Fe(C) hTF that features a 30-fold slower iron release rate	1149:1221	The effect of glycosylation on binding to diferric human transferrin (Fe(2) hTF), an authentic monoferric hTF with iron in the C-lobe (designated Fe(C) hTF), and a mutant (designated Mut-Fe(C) hTF that features a 30-fold slower iron release rate) was determined by surface plasmon resonance; a small ( approximately 20%) but consistent difference is noted for the binding of Fe(C) hTF and the Mut-Fe(C) hTF to the sTFR N317D mutant.
16716077	1	25	theme	portion	126:132	arg1	Production					100:109	Production	100:109	Production of the soluble portion of the transferrin receptor (sTFR) by baby hamster kidney (BHK) cells	100:202	Production of the soluble portion of the transferrin receptor (sTFR) by baby hamster kidney (BHK) cells is described, and the effect of glycosylation on the biological function of sTFR is evaluated for the first time.
16716077	1	26	theme	sTFR	280:283	arg1	function					268:275	the biological function	253:275	the biological function of sTFR	253:283	Production of the soluble portion of the transferrin receptor (sTFR) by baby hamster kidney (BHK) cells is described, and the effect of glycosylation on the biological function of sTFR is evaluated for the first time.
16716077	2	27	dep	sites	379:383	arg1	Asn317					394:399	Asn317	394:399	Asn317	394:399	The sTFR (residues 121-760) has three N-linked glycosylation sites (Asn251, Asn317, and Asn727).
16716077	2	27	dep	sites	379:383	arg1	Asn727					406:411	Asn727	406:411	Asn727	406:411	The sTFR (residues 121-760) has three N-linked glycosylation sites (Asn251, Asn317, and Asn727).
16716077	2	27	dep	sites	379:383	arg1	Asn251					386:391	Asn251	386:391	Asn251	386:391	The sTFR (residues 121-760) has three N-linked glycosylation sites (Asn251, Asn317, and Asn727).
16716077	2	27	dep	sites	379:383	arg1	sites					379:383	three N-linked glycosylation sites	350:383	three N-linked glycosylation sites (Asn251, Asn317, and Asn727)	350:412	The sTFR (residues 121-760) has three N-linked glycosylation sites (Asn251, Asn317, and Asn727).
16716077	6	28	theme	hTF	1358:1360	arg1	binding					1341:1347	the binding	1337:1347	the binding of Fe(C) hTF and the Mut-Fe(C) hTF to the sTFR N317D mutant	1337:1407	The effect of glycosylation on binding to diferric human transferrin (Fe(2) hTF), an authentic monoferric hTF with iron in the C-lobe (designated Fe(C) hTF), and a mutant (designated Mut-Fe(C) hTF that features a 30-fold slower iron release rate) was determined by surface plasmon resonance; a small ( approximately 20%) but consistent difference is noted for the binding of Fe(C) hTF and the Mut-Fe(C) hTF to the sTFR N317D mutant.
16716077	0	29	from	Effect	0:5	arg1	function					31:38	the function	27:38	the function of a soluble, recombinant form of the transferrin receptor	27:97	Effect of glycosylation on the function of a soluble, recombinant form of the transferrin receptor.
16716077	7	30	contain	has	1559:1561	arg2	effect					1577:1582	a significant effect	1563:1582	a significant effect	1563:1582	The rate of iron release from Fe(C) hTF and Mut-Fe(C) hTF in complex with the sTFR and the sTFR mutants at pH 5.6 reveals that only the N317D mutant has a significant effect.
16716077	7	30	contain	has	1559:1561	arg1	mutant					1552:1557	only the N317D mutant	1537:1557	only the N317D mutant	1537:1557	The rate of iron release from Fe(C) hTF and Mut-Fe(C) hTF in complex with the sTFR and the sTFR mutants at pH 5.6 reveals that only the N317D mutant has a significant effect.
16716077	6	31	theme	N317D	1396:1400	arg1	mutant					1402:1407	the sTFR N317D mutant	1387:1407	the sTFR N317D mutant	1387:1407	The effect of glycosylation on binding to diferric human transferrin (Fe(2) hTF), an authentic monoferric hTF with iron in the C-lobe (designated Fe(C) hTF), and a mutant (designated Mut-Fe(C) hTF that features a 30-fold slower iron release rate) was determined by surface plasmon resonance; a small ( approximately 20%) but consistent difference is noted for the binding of Fe(C) hTF and the Mut-Fe(C) hTF to the sTFR N317D mutant.
16716077	2	32	link	N-linked	356:363	arg1	Asn317					394:399	Asn317	394:399	Asn317	394:399	The sTFR (residues 121-760) has three N-linked glycosylation sites (Asn251, Asn317, and Asn727).
16716077	2	32	link	N-linked	356:363	arg1	Asn727					406:411	Asn727	406:411	Asn727	406:411	The sTFR (residues 121-760) has three N-linked glycosylation sites (Asn251, Asn317, and Asn727).
16716077	2	32	link	N-linked	356:363	arg1	Asn251					386:391	Asn251	386:391	Asn251	386:391	The sTFR (residues 121-760) has three N-linked glycosylation sites (Asn251, Asn317, and Asn727).
16716077	2	32	link	N-linked	356:363	arg1	sites					379:383	three N-linked glycosylation sites	350:383	three N-linked glycosylation sites (Asn251, Asn317, and Asn727)	350:412	The sTFR (residues 121-760) has three N-linked glycosylation sites (Asn251, Asn317, and Asn727).
16716077	0	33	theme	transferrin	78:88	arg1	receptor					90:97	the transferrin receptor	74:97	the transferrin receptor	74:97	Effect of glycosylation on the function of a soluble, recombinant form of the transferrin receptor.
16716077	6	34	theme	Fe	1352:1353	arg1	hTF					1358:1360	Fe(C) hTF	1352:1360	Fe(C) hTF	1352:1360	The effect of glycosylation on binding to diferric human transferrin (Fe(2) hTF), an authentic monoferric hTF with iron in the C-lobe (designated Fe(C) hTF), and a mutant (designated Mut-Fe(C) hTF that features a 30-fold slower iron release rate) was determined by surface plasmon resonance; a small ( approximately 20%) but consistent difference is noted for the binding of Fe(C) hTF and the Mut-Fe(C) hTF to the sTFR N317D mutant.
16716077	5	35	theme	ionization	843:852	arg1	spectrometry					859:870	electrospray ionization mass spectrometry	830:870	electrospray ionization mass spectrometry	830:870	Analysis by electrospray ionization mass spectrometry confirms dimerization of the sTFR and the absence of the carbohydrate at the single site in each mutant.
16716077	2	36	theme	glycosylation	365:377	arg1	Asn317					394:399	Asn317	394:399	Asn317	394:399	The sTFR (residues 121-760) has three N-linked glycosylation sites (Asn251, Asn317, and Asn727).
16716077	2	36	theme	glycosylation	365:377	arg1	Asn727					406:411	Asn727	406:411	Asn727	406:411	The sTFR (residues 121-760) has three N-linked glycosylation sites (Asn251, Asn317, and Asn727).
16716077	2	36	theme	glycosylation	365:377	arg1	Asn251					386:391	Asn251	386:391	Asn251	386:391	The sTFR (residues 121-760) has three N-linked glycosylation sites (Asn251, Asn317, and Asn727).
16716077	2	36	theme	glycosylation	365:377	arg1	sites					379:383	three N-linked glycosylation sites	350:383	three N-linked glycosylation sites (Asn251, Asn317, and Asn727)	350:412	The sTFR (residues 121-760) has three N-linked glycosylation sites (Asn251, Asn317, and Asn727).
16716077	0	37	theme	glycosylation	10:22	arg1	Effect					0:5	Effect	0:5	Effect of glycosylation on the function of a soluble, recombinant form of the transferrin receptor	0:97	Effect of glycosylation on the function of a soluble, recombinant form of the transferrin receptor.
16716077	0	38	dep	soluble	45:51	arg1	recombinant					54:64	recombinant	54:64	recombinant	54:64	Effect of glycosylation on the function of a soluble, recombinant form of the transferrin receptor.
16716077	6	39	dep	hTF	1358:1360	arg1	C					1355:1355	C	1355:1355	C	1355:1355	The effect of glycosylation on binding to diferric human transferrin (Fe(2) hTF), an authentic monoferric hTF with iron in the C-lobe (designated Fe(C) hTF), and a mutant (designated Mut-Fe(C) hTF that features a 30-fold slower iron release rate) was determined by surface plasmon resonance; a small ( approximately 20%) but consistent difference is noted for the binding of Fe(C) hTF and the Mut-Fe(C) hTF to the sTFR N317D mutant.
16716077	7	40	from	hTF	1464:1466	arg1	rate					1414:1417	The rate	1410:1417	The rate of iron release from Fe(C) hTF and Mut-Fe(C) hTF in complex with the sTFR and the sTFR mutants at pH 5.6	1410:1522	The rate of iron release from Fe(C) hTF and Mut-Fe(C) hTF in complex with the sTFR and the sTFR mutants at pH 5.6 reveals that only the N317D mutant has a significant effect.
16716077	7	40	from	hTF	1464:1466	arg1	release					1427:1433	iron release	1422:1433	iron release from Fe(C) hTF and Mut-Fe(C) hTF in complex with the sTFR and the sTFR mutants at pH 5.6	1422:1522	The rate of iron release from Fe(C) hTF and Mut-Fe(C) hTF in complex with the sTFR and the sTFR mutants at pH 5.6 reveals that only the N317D mutant has a significant effect.
16716077	7	40	from	hTF	1464:1466	arg1	complex					1471:1477	complex	1471:1477	complex with the sTFR	1471:1491	The rate of iron release from Fe(C) hTF and Mut-Fe(C) hTF in complex with the sTFR and the sTFR mutants at pH 5.6 reveals that only the N317D mutant has a significant effect.
16716077	2	41	dep	residues	328:335	arg1	121-760					337:343	121-760	337:343	121-760	337:343	The sTFR (residues 121-760) has three N-linked glycosylation sites (Asn251, Asn317, and Asn727).
16716077	1	42	theme	glycosylation	236:248	arg1	effect					226:231	the effect	222:231	the effect of glycosylation on the biological function of sTFR	222:283	Production of the soluble portion of the transferrin receptor (sTFR) by baby hamster kidney (BHK) cells is described, and the effect of glycosylation on the biological function of sTFR is evaluated for the first time.
16716077	6	43	dep	hTF	1170:1172	arg1	rate					1218:1221	a 30-fold slower iron release rate	1188:1221	designated Mut-Fe(C) hTF that features a 30-fold slower iron release rate	1149:1221	The effect of glycosylation on binding to diferric human transferrin (Fe(2) hTF), an authentic monoferric hTF with iron in the C-lobe (designated Fe(C) hTF), and a mutant (designated Mut-Fe(C) hTF that features a 30-fold slower iron release rate) was determined by surface plasmon resonance; a small ( approximately 20%) but consistent difference is noted for the binding of Fe(C) hTF and the Mut-Fe(C) hTF to the sTFR N317D mutant.
16716077	0	44	theme	soluble	45:51	arg1	form					66:69	a soluble, recombinant form	43:69	a soluble, recombinant form of the transferrin receptor	43:97	Effect of glycosylation on the function of a soluble, recombinant form of the transferrin receptor.
16716077	6	45	theme	C	1167:1167	arg1	hTF					1170:1172	designated Mut-Fe(C) hTF	1149:1172	designated Mut-Fe(C) hTF that features a 30-fold slower iron release rate	1149:1221	The effect of glycosylation on binding to diferric human transferrin (Fe(2) hTF), an authentic monoferric hTF with iron in the C-lobe (designated Fe(C) hTF), and a mutant (designated Mut-Fe(C) hTF that features a 30-fold slower iron release rate) was determined by surface plasmon resonance; a small ( approximately 20%) but consistent difference is noted for the binding of Fe(C) hTF and the Mut-Fe(C) hTF to the sTFR N317D mutant.
16716077	6	46	from	effect	981:986	arg1	binding					1008:1014	binding	1008:1014	binding to diferric human transferrin (Fe(2) hTF), an authentic monoferric hTF with iron in the C-lobe (designated Fe(C) hTF), and a mutant (designated Mut-Fe(C) hTF that features a 30-fold slower iron release rate) was determined by surface plasmon resonance	1008:1266	The effect of glycosylation on binding to diferric human transferrin (Fe(2) hTF), an authentic monoferric hTF with iron in the C-lobe (designated Fe(C) hTF), and a mutant (designated Mut-Fe(C) hTF that features a 30-fold slower iron release rate) was determined by surface plasmon resonance; a small ( approximately 20%) but consistent difference is noted for the binding of Fe(C) hTF and the Mut-Fe(C) hTF to the sTFR N317D mutant.
16716077	1	47	theme	kidney	185:190	arg1	cells					198:202	baby hamster kidney (BHK) cells	172:202	baby hamster kidney (BHK) cells	172:202	Production of the soluble portion of the transferrin receptor (sTFR) by baby hamster kidney (BHK) cells is described, and the effect of glycosylation on the biological function of sTFR is evaluated for the first time.
16716077	2	48	gly	glycosylation	365:377	arg2	Asn317					394:399	Asn317	394:399	Asn317	394:399	The sTFR (residues 121-760) has three N-linked glycosylation sites (Asn251, Asn317, and Asn727).
16716077	2	48	gly	glycosylation	365:377	arg2	Asn251					386:391	Asn251	386:391	Asn251	386:391	The sTFR (residues 121-760) has three N-linked glycosylation sites (Asn251, Asn317, and Asn727).
16716077	2	48	gly	glycosylation	365:377	arg2	Asn727					406:411	Asn727	406:411	Asn727	406:411	The sTFR (residues 121-760) has three N-linked glycosylation sites (Asn251, Asn317, and Asn727).
16716077	2	48	gly	glycosylation	365:377	arg2	sites					379:383	three N-linked glycosylation sites	350:383	three N-linked glycosylation sites (Asn251, Asn317, and Asn727)	350:412	The sTFR (residues 121-760) has three N-linked glycosylation sites (Asn251, Asn317, and Asn727).
16716077	2	48	gly	glycosylation	365:377	arg2	three					350:354	three	350:354	three	350:354	The sTFR (residues 121-760) has three N-linked glycosylation sites (Asn251, Asn317, and Asn727).
16716077	4	49	dep	expressed	759:767	arg1	whereas					770:776	whereas	770:776	whereas	770:776	Mutants in which glycosylation at positions 251 and 727 (N251D and N727D) is eliminated are well expressed, whereas production of the N317D mutant is poor.
16716077	7	50	from	hTF	1446:1448	arg1	rate					1414:1417	The rate	1410:1417	The rate of iron release from Fe(C) hTF and Mut-Fe(C) hTF in complex with the sTFR and the sTFR mutants at pH 5.6	1410:1522	The rate of iron release from Fe(C) hTF and Mut-Fe(C) hTF in complex with the sTFR and the sTFR mutants at pH 5.6 reveals that only the N317D mutant has a significant effect.
16716077	7	50	from	hTF	1446:1448	arg1	release					1427:1433	iron release	1422:1433	iron release from Fe(C) hTF and Mut-Fe(C) hTF in complex with the sTFR and the sTFR mutants at pH 5.6	1422:1522	The rate of iron release from Fe(C) hTF and Mut-Fe(C) hTF in complex with the sTFR and the sTFR mutants at pH 5.6 reveals that only the N317D mutant has a significant effect.
16716077	7	50	from	hTF	1446:1448	arg1	complex					1471:1477	complex	1471:1477	complex with the sTFR	1471:1491	The rate of iron release from Fe(C) hTF and Mut-Fe(C) hTF in complex with the sTFR and the sTFR mutants at pH 5.6 reveals that only the N317D mutant has a significant effect.
16716077	0	51	gly	glycosylation	10:22	arg1	form					66:69	a soluble, recombinant form	43:69	a soluble, recombinant form of the transferrin receptor	43:97	Effect of glycosylation on the function of a soluble, recombinant form of the transferrin receptor.
16716077	6	52	theme	iron	1205:1208	arg1	rate					1218:1221	a 30-fold slower iron release rate	1188:1221	designated Mut-Fe(C) hTF that features a 30-fold slower iron release rate	1149:1221	The effect of glycosylation on binding to diferric human transferrin (Fe(2) hTF), an authentic monoferric hTF with iron in the C-lobe (designated Fe(C) hTF), and a mutant (designated Mut-Fe(C) hTF that features a 30-fold slower iron release rate) was determined by surface plasmon resonance; a small ( approximately 20%) but consistent difference is noted for the binding of Fe(C) hTF and the Mut-Fe(C) hTF to the sTFR N317D mutant.
16716077	3	53	gly	nonglycosylated	520:534	arg1	sTFR					536:539	no nonglycosylated sTFR	517:539	no nonglycosylated sTFR	517:539	Although fully glycosylated sTFR is secreted into the tissue culture medium ( approximately 40 mg/L), no nonglycosylated sTFR could be produced, suggesting that carbohydrate is critical to the folding, stability, and/or secretion of the receptor.
16716077	1	54	from	effect	226:231	arg1	function					268:275	the biological function	253:275	the biological function of sTFR	253:283	Production of the soluble portion of the transferrin receptor (sTFR) by baby hamster kidney (BHK) cells is described, and the effect of glycosylation on the biological function of sTFR is evaluated for the first time.
16716077	3	55	theme	glycosylated	430:441	arg1	sTFR					443:446	fully glycosylated sTFR	424:446	fully glycosylated sTFR	424:446	Although fully glycosylated sTFR is secreted into the tissue culture medium ( approximately 40 mg/L), no nonglycosylated sTFR could be produced, suggesting that carbohydrate is critical to the folding, stability, and/or secretion of the receptor.
16716077	1	56	theme	transferrin	141:151	arg1	sTFR					163:166	sTFR	163:166	sTFR	163:166	Production of the soluble portion of the transferrin receptor (sTFR) by baby hamster kidney (BHK) cells is described, and the effect of glycosylation on the biological function of sTFR is evaluated for the first time.
16716077	1	56	theme	transferrin	141:151	arg1	receptor					153:160	transferrin receptor	141:160	the transferrin receptor (sTFR)	137:167	Production of the soluble portion of the transferrin receptor (sTFR) by baby hamster kidney (BHK) cells is described, and the effect of glycosylation on the biological function of sTFR is evaluated for the first time.
16716077	6	57	theme	diferric	1019:1026	arg1	transferrin					1034:1044	diferric human transferrin	1019:1044	diferric human transferrin (Fe(2) hTF)	1019:1056	The effect of glycosylation on binding to diferric human transferrin (Fe(2) hTF), an authentic monoferric hTF with iron in the C-lobe (designated Fe(C) hTF), and a mutant (designated Mut-Fe(C) hTF that features a 30-fold slower iron release rate) was determined by surface plasmon resonance; a small ( approximately 20%) but consistent difference is noted for the binding of Fe(C) hTF and the Mut-Fe(C) hTF to the sTFR N317D mutant.
16716077	6	57	theme	diferric	1019:1026	arg1	hTF					1053:1055	Fe(2) hTF	1047:1055	Fe(2) hTF	1047:1055	The effect of glycosylation on binding to diferric human transferrin (Fe(2) hTF), an authentic monoferric hTF with iron in the C-lobe (designated Fe(C) hTF), and a mutant (designated Mut-Fe(C) hTF that features a 30-fold slower iron release rate) was determined by surface plasmon resonance; a small ( approximately 20%) but consistent difference is noted for the binding of Fe(C) hTF and the Mut-Fe(C) hTF to the sTFR N317D mutant.
16716077	6	58	theme	monoferric	1072:1081	arg1	hTF					1083:1085	an authentic monoferric hTF	1059:1085	an authentic monoferric hTF with iron in the C-lobe (designated Fe(C) hTF), and a mutant (designated Mut-Fe(C) hTF that features a 30-fold slower iron release rate)	1059:1222	The effect of glycosylation on binding to diferric human transferrin (Fe(2) hTF), an authentic monoferric hTF with iron in the C-lobe (designated Fe(C) hTF), and a mutant (designated Mut-Fe(C) hTF that features a 30-fold slower iron release rate) was determined by surface plasmon resonance; a small ( approximately 20%) but consistent difference is noted for the binding of Fe(C) hTF and the Mut-Fe(C) hTF to the sTFR N317D mutant.
16716077	3	59	theme	tissue	469:474	arg1	medium					484:489	the tissue culture medium	465:489	the tissue culture medium ( approximately 40 mg/L)	465:514	Although fully glycosylated sTFR is secreted into the tissue culture medium ( approximately 40 mg/L), no nonglycosylated sTFR could be produced, suggesting that carbohydrate is critical to the folding, stability, and/or secretion of the receptor.
16716077	3	59	theme	tissue	469:474	arg1	mg/L					510:513	approximately 40 mg/L	493:513	approximately 40 mg/L	493:513	Although fully glycosylated sTFR is secreted into the tissue culture medium ( approximately 40 mg/L), no nonglycosylated sTFR could be produced, suggesting that carbohydrate is critical to the folding, stability, and/or secretion of the receptor.
16716077	7	60	from	pH	1517:1518	arg1	hTF					1464:1466	Mut-Fe(C) hTF	1454:1466	Mut-Fe(C) hTF	1454:1466	The rate of iron release from Fe(C) hTF and Mut-Fe(C) hTF in complex with the sTFR and the sTFR mutants at pH 5.6 reveals that only the N317D mutant has a significant effect.
16716077	7	60	from	pH	1517:1518	arg1	mutants					1506:1512	the sTFR mutants	1497:1512	the sTFR mutants at pH 5.6	1497:1522	The rate of iron release from Fe(C) hTF and Mut-Fe(C) hTF in complex with the sTFR and the sTFR mutants at pH 5.6 reveals that only the N317D mutant has a significant effect.
16716077	7	60	from	pH	1517:1518	arg1	hTF					1446:1448	Fe(C) hTF	1440:1448	Fe(C) hTF	1440:1448	The rate of iron release from Fe(C) hTF and Mut-Fe(C) hTF in complex with the sTFR and the sTFR mutants at pH 5.6 reveals that only the N317D mutant has a significant effect.
16716077	7	61	theme	iron	1422:1425	arg1	release					1427:1433	iron release	1422:1433	iron release from Fe(C) hTF and Mut-Fe(C) hTF in complex with the sTFR and the sTFR mutants at pH 5.6	1422:1522	The rate of iron release from Fe(C) hTF and Mut-Fe(C) hTF in complex with the sTFR and the sTFR mutants at pH 5.6 reveals that only the N317D mutant has a significant effect.
16716077	6	62	dep	binding	1008:1014	arg1	determined					1228:1237	determined	1228:1237	was determined by surface plasmon resonance	1224:1266	The effect of glycosylation on binding to diferric human transferrin (Fe(2) hTF), an authentic monoferric hTF with iron in the C-lobe (designated Fe(C) hTF), and a mutant (designated Mut-Fe(C) hTF that features a 30-fold slower iron release rate) was determined by surface plasmon resonance; a small ( approximately 20%) but consistent difference is noted for the binding of Fe(C) hTF and the Mut-Fe(C) hTF to the sTFR N317D mutant.
16716077	7	63	theme	sTFR	1501:1504	arg1	mutants					1506:1512	the sTFR mutants	1497:1512	the sTFR mutants at pH 5.6	1497:1522	The rate of iron release from Fe(C) hTF and Mut-Fe(C) hTF in complex with the sTFR and the sTFR mutants at pH 5.6 reveals that only the N317D mutant has a significant effect.
16716077	6	64	theme	glycosylation	991:1003	arg1	effect					981:986	The effect	977:986	The effect of glycosylation on binding to diferric human transferrin (Fe(2) hTF), an authentic monoferric hTF with iron in the C-lobe (designated Fe(C) hTF), and a mutant (designated Mut-Fe(C) hTF that features a 30-fold slower iron release rate) was determined by surface plasmon resonance	977:1266	The effect of glycosylation on binding to diferric human transferrin (Fe(2) hTF), an authentic monoferric hTF with iron in the C-lobe (designated Fe(C) hTF), and a mutant (designated Mut-Fe(C) hTF that features a 30-fold slower iron release rate) was determined by surface plasmon resonance; a small ( approximately 20%) but consistent difference is noted for the binding of Fe(C) hTF and the Mut-Fe(C) hTF to the sTFR N317D mutant.
16716077	6	65	theme	plasmon	1250:1256	arg1	resonance					1258:1266	surface plasmon resonance	1242:1266	surface plasmon resonance	1242:1266	The effect of glycosylation on binding to diferric human transferrin (Fe(2) hTF), an authentic monoferric hTF with iron in the C-lobe (designated Fe(C) hTF), and a mutant (designated Mut-Fe(C) hTF that features a 30-fold slower iron release rate) was determined by surface plasmon resonance; a small ( approximately 20%) but consistent difference is noted for the binding of Fe(C) hTF and the Mut-Fe(C) hTF to the sTFR N317D mutant.
16716077	1	66	theme	baby	172:175	arg1	BHK					193:195	BHK	193:195	BHK	193:195	Production of the soluble portion of the transferrin receptor (sTFR) by baby hamster kidney (BHK) cells is described, and the effect of glycosylation on the biological function of sTFR is evaluated for the first time.
16716077	1	66	theme	baby	172:175	arg1	kidney					185:190	baby hamster kidney	172:190	baby hamster kidney (BHK) cells	172:202	Production of the soluble portion of the transferrin receptor (sTFR) by baby hamster kidney (BHK) cells is described, and the effect of glycosylation on the biological function of sTFR is evaluated for the first time.
16716077	5	67	theme	single	949:954	arg1	site					956:959	the single site	945:959	the single site in each mutant	945:974	Analysis by electrospray ionization mass spectrometry confirms dimerization of the sTFR and the absence of the carbohydrate at the single site in each mutant.
16716077	6	68	dep	hTF	1129:1131	arg1	C					1126:1126	C	1126:1126	C	1126:1126	The effect of glycosylation on binding to diferric human transferrin (Fe(2) hTF), an authentic monoferric hTF with iron in the C-lobe (designated Fe(C) hTF), and a mutant (designated Mut-Fe(C) hTF that features a 30-fold slower iron release rate) was determined by surface plasmon resonance; a small ( approximately 20%) but consistent difference is noted for the binding of Fe(C) hTF and the Mut-Fe(C) hTF to the sTFR N317D mutant.
16716077	3	69	theme	receptor	652:659	arg1	folding					608:614	folding	608:614	folding	608:614	Although fully glycosylated sTFR is secreted into the tissue culture medium ( approximately 40 mg/L), no nonglycosylated sTFR could be produced, suggesting that carbohydrate is critical to the folding, stability, and/or secretion of the receptor.
16716077	6	70	theme	designated	1112:1121	arg1	hTF					1129:1131	designated Fe(C) hTF	1112:1131	designated Fe(C) hTF	1112:1131	The effect of glycosylation on binding to diferric human transferrin (Fe(2) hTF), an authentic monoferric hTF with iron in the C-lobe (designated Fe(C) hTF), and a mutant (designated Mut-Fe(C) hTF that features a 30-fold slower iron release rate) was determined by surface plasmon resonance; a small ( approximately 20%) but consistent difference is noted for the binding of Fe(C) hTF and the Mut-Fe(C) hTF to the sTFR N317D mutant.
16716077	6	70	theme	designated	1112:1121	arg1	C-lobe					1104:1109	the C-lobe	1100:1109	the C-lobe (designated Fe(C) hTF)	1100:1132	The effect of glycosylation on binding to diferric human transferrin (Fe(2) hTF), an authentic monoferric hTF with iron in the C-lobe (designated Fe(C) hTF), and a mutant (designated Mut-Fe(C) hTF that features a 30-fold slower iron release rate) was determined by surface plasmon resonance; a small ( approximately 20%) but consistent difference is noted for the binding of Fe(C) hTF and the Mut-Fe(C) hTF to the sTFR N317D mutant.
16716077	4	71	from	positions	696:704	arg1	glycosylation					679:691	glycosylation	679:691	glycosylation at positions 251 and 727 (N251D and N727D)	679:734	Mutants in which glycosylation at positions 251 and 727 (N251D and N727D) is eliminated are well expressed, whereas production of the N317D mutant is poor.
16716077	1	72	gly	glycosylation	236:248	arg1	sTFR					280:283	sTFR	280:283	sTFR	280:283	Production of the soluble portion of the transferrin receptor (sTFR) by baby hamster kidney (BHK) cells is described, and the effect of glycosylation on the biological function of sTFR is evaluated for the first time.
16716077	1	73	theme	soluble	118:124	arg1	portion					126:132	the soluble portion	114:132	the soluble portion of the transferrin receptor (sTFR)	114:167	Production of the soluble portion of the transferrin receptor (sTFR) by baby hamster kidney (BHK) cells is described, and the effect of glycosylation on the biological function of sTFR is evaluated for the first time.
16716077	6	74	theme	Fe	1047:1048	arg1	transferrin					1034:1044	diferric human transferrin	1019:1044	diferric human transferrin (Fe(2) hTF)	1019:1056	The effect of glycosylation on binding to diferric human transferrin (Fe(2) hTF), an authentic monoferric hTF with iron in the C-lobe (designated Fe(C) hTF), and a mutant (designated Mut-Fe(C) hTF that features a 30-fold slower iron release rate) was determined by surface plasmon resonance; a small ( approximately 20%) but consistent difference is noted for the binding of Fe(C) hTF and the Mut-Fe(C) hTF to the sTFR N317D mutant.
16716077	6	74	theme	Fe	1047:1048	arg1	hTF					1053:1055	Fe(2) hTF	1047:1055	Fe(2) hTF	1047:1055	The effect of glycosylation on binding to diferric human transferrin (Fe(2) hTF), an authentic monoferric hTF with iron in the C-lobe (designated Fe(C) hTF), and a mutant (designated Mut-Fe(C) hTF that features a 30-fold slower iron release rate) was determined by surface plasmon resonance; a small ( approximately 20%) but consistent difference is noted for the binding of Fe(C) hTF and the Mut-Fe(C) hTF to the sTFR N317D mutant.
16716077	6	75	dep	hTF	1053:1055	arg1	2					1050:1050	2	1050:1050	2	1050:1050	The effect of glycosylation on binding to diferric human transferrin (Fe(2) hTF), an authentic monoferric hTF with iron in the C-lobe (designated Fe(C) hTF), and a mutant (designated Mut-Fe(C) hTF that features a 30-fold slower iron release rate) was determined by surface plasmon resonance; a small ( approximately 20%) but consistent difference is noted for the binding of Fe(C) hTF and the Mut-Fe(C) hTF to the sTFR N317D mutant.
16716077	0	76	theme	form	66:69	arg1	function					31:38	the function	27:38	the function of a soluble, recombinant form of the transferrin receptor	27:97	Effect of glycosylation on the function of a soluble, recombinant form of the transferrin receptor.
16716077	7	77	theme	N317D	1546:1550	arg1	mutant					1552:1557	only the N317D mutant	1537:1557	only the N317D mutant	1537:1557	The rate of iron release from Fe(C) hTF and Mut-Fe(C) hTF in complex with the sTFR and the sTFR mutants at pH 5.6 reveals that only the N317D mutant has a significant effect.
16716077	3	78	gly	glycosylated	430:441	arg1	sTFR					443:446	fully glycosylated sTFR	424:446	fully glycosylated sTFR	424:446	Although fully glycosylated sTFR is secreted into the tissue culture medium ( approximately 40 mg/L), no nonglycosylated sTFR could be produced, suggesting that carbohydrate is critical to the folding, stability, and/or secretion of the receptor.
16716077	6	79	dep	mutant	1141:1146	arg1	hTF					1170:1172	designated Mut-Fe(C) hTF	1149:1172	designated Mut-Fe(C) hTF that features a 30-fold slower iron release rate	1149:1221	The effect of glycosylation on binding to diferric human transferrin (Fe(2) hTF), an authentic monoferric hTF with iron in the C-lobe (designated Fe(C) hTF), and a mutant (designated Mut-Fe(C) hTF that features a 30-fold slower iron release rate) was determined by surface plasmon resonance; a small ( approximately 20%) but consistent difference is noted for the binding of Fe(C) hTF and the Mut-Fe(C) hTF to the sTFR N317D mutant.
16716077	7	80	from	mutants	1506:1512	arg1	rate					1414:1417	The rate	1410:1417	The rate of iron release from Fe(C) hTF and Mut-Fe(C) hTF in complex with the sTFR and the sTFR mutants at pH 5.6	1410:1522	The rate of iron release from Fe(C) hTF and Mut-Fe(C) hTF in complex with the sTFR and the sTFR mutants at pH 5.6 reveals that only the N317D mutant has a significant effect.
16716077	7	80	from	mutants	1506:1512	arg1	release					1427:1433	iron release	1422:1433	iron release from Fe(C) hTF and Mut-Fe(C) hTF in complex with the sTFR and the sTFR mutants at pH 5.6	1422:1522	The rate of iron release from Fe(C) hTF and Mut-Fe(C) hTF in complex with the sTFR and the sTFR mutants at pH 5.6 reveals that only the N317D mutant has a significant effect.
16716077	7	80	from	mutants	1506:1512	arg1	complex					1471:1477	complex	1471:1477	complex with the sTFR	1471:1491	The rate of iron release from Fe(C) hTF and Mut-Fe(C) hTF in complex with the sTFR and the sTFR mutants at pH 5.6 reveals that only the N317D mutant has a significant effect.
16716077	4	81	theme	mutant	802:807	arg1	production					778:787	production	778:787	production of the N317D mutant	778:807	Mutants in which glycosylation at positions 251 and 727 (N251D and N727D) is eliminated are well expressed, whereas production of the N317D mutant is poor.
16716077	0	82	theme	receptor	90:97	arg1	form					66:69	a soluble, recombinant form	43:69	a soluble, recombinant form of the transferrin receptor	43:97	Effect of glycosylation on the function of a soluble, recombinant form of the transferrin receptor.
16716077	5	83	theme	electrospray	830:841	arg1	spectrometry					859:870	electrospray ionization mass spectrometry	830:870	electrospray ionization mass spectrometry	830:870	Analysis by electrospray ionization mass spectrometry confirms dimerization of the sTFR and the absence of the carbohydrate at the single site in each mutant.
16716077	8	84	theme	TFR	1648:1650	arg1	region					1634:1639	a region	1632:1639	a region of the TFR previously shown to interact with hTF	1632:1688	The carbohydrate at position 317 lies close to a region of the TFR previously shown to interact with hTF.
16716077	6	85	theme	sTFR	1391:1394	arg1	mutant					1402:1407	the sTFR N317D mutant	1387:1407	the sTFR N317D mutant	1387:1407	The effect of glycosylation on binding to diferric human transferrin (Fe(2) hTF), an authentic monoferric hTF with iron in the C-lobe (designated Fe(C) hTF), and a mutant (designated Mut-Fe(C) hTF that features a 30-fold slower iron release rate) was determined by surface plasmon resonance; a small ( approximately 20%) but consistent difference is noted for the binding of Fe(C) hTF and the Mut-Fe(C) hTF to the sTFR N317D mutant.
16716077	6	86	theme	slower	1198:1203	arg1	rate					1218:1221	a 30-fold slower iron release rate	1188:1221	designated Mut-Fe(C) hTF that features a 30-fold slower iron release rate	1149:1221	The effect of glycosylation on binding to diferric human transferrin (Fe(2) hTF), an authentic monoferric hTF with iron in the C-lobe (designated Fe(C) hTF), and a mutant (designated Mut-Fe(C) hTF that features a 30-fold slower iron release rate) was determined by surface plasmon resonance; a small ( approximately 20%) but consistent difference is noted for the binding of Fe(C) hTF and the Mut-Fe(C) hTF to the sTFR N317D mutant.
16716077	1	87	theme	first	306:310	arg1	time					312:315	the first time	302:315	the first time	302:315	Production of the soluble portion of the transferrin receptor (sTFR) by baby hamster kidney (BHK) cells is described, and the effect of glycosylation on the biological function of sTFR is evaluated for the first time.
16716077	2	88	theme	N-linked	356:363	arg1	Asn317					394:399	Asn317	394:399	Asn317	394:399	The sTFR (residues 121-760) has three N-linked glycosylation sites (Asn251, Asn317, and Asn727).
16716077	2	88	theme	N-linked	356:363	arg1	Asn727					406:411	Asn727	406:411	Asn727	406:411	The sTFR (residues 121-760) has three N-linked glycosylation sites (Asn251, Asn317, and Asn727).
16716077	2	88	theme	N-linked	356:363	arg1	Asn251					386:391	Asn251	386:391	Asn251	386:391	The sTFR (residues 121-760) has three N-linked glycosylation sites (Asn251, Asn317, and Asn727).
16716077	2	88	theme	N-linked	356:363	arg1	sites					379:383	three N-linked glycosylation sites	350:383	three N-linked glycosylation sites (Asn251, Asn317, and Asn727)	350:412	The sTFR (residues 121-760) has three N-linked glycosylation sites (Asn251, Asn317, and Asn727).
16716077	5	89	from	site	956:959	arg1	mutant					969:974	each mutant	964:974	each mutant	964:974	Analysis by electrospray ionization mass spectrometry confirms dimerization of the sTFR and the absence of the carbohydrate at the single site in each mutant.
16716077	3	90	theme	nonglycosylated	520:534	arg1	sTFR					536:539	no nonglycosylated sTFR	517:539	no nonglycosylated sTFR	517:539	Although fully glycosylated sTFR is secreted into the tissue culture medium ( approximately 40 mg/L), no nonglycosylated sTFR could be produced, suggesting that carbohydrate is critical to the folding, stability, and/or secretion of the receptor.
16716077	4	91	gly	glycosylation	679:691	arg2	727					714:716	727	714:716	727	714:716	Mutants in which glycosylation at positions 251 and 727 (N251D and N727D) is eliminated are well expressed, whereas production of the N317D mutant is poor.
16716077	4	91	gly	glycosylation	679:691	arg1	N251D					719:723	N251D	719:723	N251D	719:723	Mutants in which glycosylation at positions 251 and 727 (N251D and N727D) is eliminated are well expressed, whereas production of the N317D mutant is poor.
16716077	4	91	gly	glycosylation	679:691	arg1	N727D					729:733	N727D	729:733	N727D	729:733	Mutants in which glycosylation at positions 251 and 727 (N251D and N727D) is eliminated are well expressed, whereas production of the N317D mutant is poor.
16716077	4	91	gly	glycosylation	679:691	arg1	positions					696:704	positions 251 and 727	696:716	positions	696:704	Mutants in which glycosylation at positions 251 and 727 (N251D and N727D) is eliminated are well expressed, whereas production of the N317D mutant is poor.
16716077	4	91	gly	glycosylation	679:691	arg1	Mutants					662:668	Mutants	662:668	Mutants in which glycosylation at positions 251 and 727 (N251D and N727D) is eliminated	662:748	Mutants in which glycosylation at positions 251 and 727 (N251D and N727D) is eliminated are well expressed, whereas production of the N317D mutant is poor.
16716077	4	91	gly	glycosylation	679:691	arg2	N251D					719:723	N251D	719:723	N251D	719:723	Mutants in which glycosylation at positions 251 and 727 (N251D and N727D) is eliminated are well expressed, whereas production of the N317D mutant is poor.
16716077	4	91	gly	glycosylation	679:691	arg1	727					714:716	727	714:716	727	714:716	Mutants in which glycosylation at positions 251 and 727 (N251D and N727D) is eliminated are well expressed, whereas production of the N317D mutant is poor.
16716077	4	91	gly	glycosylation	679:691	arg2	N727D					729:733	N727D	729:733	N727D	729:733	Mutants in which glycosylation at positions 251 and 727 (N251D and N727D) is eliminated are well expressed, whereas production of the N317D mutant is poor.
16716077	4	91	gly	glycosylation	679:691	arg2	positions					696:704	positions 251 and 727	696:716	positions	696:704	Mutants in which glycosylation at positions 251 and 727 (N251D and N727D) is eliminated are well expressed, whereas production of the N317D mutant is poor.
16716077	5	92	theme	sTFR	901:904	arg1	dimerization					881:892	dimerization	881:892	dimerization of the sTFR	881:904	Analysis by electrospray ionization mass spectrometry confirms dimerization of the sTFR and the absence of the carbohydrate at the single site in each mutant.
16716077	5	92	theme	sTFR	901:904	arg1	absence					914:920	the absence	910:920	the absence of the carbohydrate	910:940	Analysis by electrospray ionization mass spectrometry confirms dimerization of the sTFR and the absence of the carbohydrate at the single site in each mutant.
16716077	8	93	from	position	1605:1612	arg1	carbohydrate					1589:1600	The carbohydrate	1585:1600	The carbohydrate at position 317	1585:1616	The carbohydrate at position 317 lies close to a region of the TFR previously shown to interact with hTF.
16716077	6	94	theme	surface	1242:1248	arg1	resonance					1258:1266	surface plasmon resonance	1242:1266	surface plasmon resonance	1242:1266	The effect of glycosylation on binding to diferric human transferrin (Fe(2) hTF), an authentic monoferric hTF with iron in the C-lobe (designated Fe(C) hTF), and a mutant (designated Mut-Fe(C) hTF that features a 30-fold slower iron release rate) was determined by surface plasmon resonance; a small ( approximately 20%) but consistent difference is noted for the binding of Fe(C) hTF and the Mut-Fe(C) hTF to the sTFR N317D mutant.
16716077	1	95	theme	biological	257:266	arg1	function					268:275	the biological function	253:275	the biological function of sTFR	253:283	Production of the soluble portion of the transferrin receptor (sTFR) by baby hamster kidney (BHK) cells is described, and the effect of glycosylation on the biological function of sTFR is evaluated for the first time.
16716077	5	96	theme	mass	854:857	arg1	spectrometry					859:870	electrospray ionization mass spectrometry	830:870	electrospray ionization mass spectrometry	830:870	Analysis by electrospray ionization mass spectrometry confirms dimerization of the sTFR and the absence of the carbohydrate at the single site in each mutant.
16716077	7	97	with	complex	1471:1477	arg1	sTFR					1488:1491	the sTFR	1484:1491	the sTFR	1484:1491	The rate of iron release from Fe(C) hTF and Mut-Fe(C) hTF in complex with the sTFR and the sTFR mutants at pH 5.6 reveals that only the N317D mutant has a significant effect.
16716077	4	98	dep	positions	696:704	arg1	N727D					729:733	N727D	729:733	N727D	729:733	Mutants in which glycosylation at positions 251 and 727 (N251D and N727D) is eliminated are well expressed, whereas production of the N317D mutant is poor.
16716077	4	98	dep	positions	696:704	arg1	N251D					719:723	N251D	719:723	N251D	719:723	Mutants in which glycosylation at positions 251 and 727 (N251D and N727D) is eliminated are well expressed, whereas production of the N317D mutant is poor.
16716077	4	98	dep	positions	696:704	arg1	positions					696:704	positions 251 and 727	696:716	positions	696:704	Mutants in which glycosylation at positions 251 and 727 (N251D and N727D) is eliminated are well expressed, whereas production of the N317D mutant is poor.
16716077	7	99	theme	C	1461:1461	arg1	hTF					1464:1466	Mut-Fe(C) hTF	1454:1466	Mut-Fe(C) hTF	1454:1466	The rate of iron release from Fe(C) hTF and Mut-Fe(C) hTF in complex with the sTFR and the sTFR mutants at pH 5.6 reveals that only the N317D mutant has a significant effect.
16880503	12	0	theme	oligosaccharides	1799:1814	arg1	content					1774:1780	a higher fucose content	1758:1780	a higher fucose content of Asn-13-linked oligosaccharides	1758:1814	The glycans of free hCGbeta were larger and had a higher fucose content of Asn-13-linked oligosaccharides than intact hCG.
16880503	4	1	dep	"	525:525	arg1	hCGh					532:535	hCGh	532:535	hCGh	532:535	These glycoforms, which are called "hyperglycosylated" hCG (hCGh), have been reported to contain more complex glycan moieties.
16880503	4	1	dep	"	525:525	arg1	hCG					527:529	hCG	527:529	"hyperglycosylated" hCG (hCGh)	507:536	These glycoforms, which are called "hyperglycosylated" hCG (hCGh), have been reported to contain more complex glycan moieties.
16880503	8	2	from	Ser-132	1198:1204	arg1	N-glycans					1125:1133	N-glycans	1125:1133	N-glycans at Asn-13 and Asn-30 as well as O-glycans at Ser-121, Ser-127, Ser-132, and Ser-138	1125:1217	N-glycans at Asn-13 and Asn-30 as well as O-glycans at Ser-121, Ser-127, Ser-132, and Ser-138 were characterized.
16880503	8	2	from	Ser-132	1198:1204	arg1	O-glycans					1167:1175	O-glycans	1167:1175	N-glycans at Asn-13 and Asn-30 as well as O-glycans at Ser-121, Ser-127, Ser-132, and Ser-138	1125:1217	N-glycans at Asn-13 and Asn-30 as well as O-glycans at Ser-121, Ser-127, Ser-132, and Ser-138 were characterized.
16880503	9	3	link	cancer-derived	1437:1450	arg1	hCGbeta					1452:1458	cancer-derived hCGbeta	1437:1458	cancer-derived hCGbeta	1437:1458	In all samples, the major type of N-glycan was a biantennary complex-type structure, but triantennary structures linked to Asn-30 as well as fucosylation of the Asn-13-bound glycan are increased in cancer-derived hCGbeta.
16880503	2	4	theme	glycoprotein	330:341	arg1	hormone					343:349	a glycoprotein hormone	328:349	a glycoprotein hormone produced in high concentrations during pregnancy	328:398	Human chorionic gonadotropin (hCG) is a glycoprotein hormone produced in high concentrations during pregnancy.
16880503	2	4	theme	glycoprotein	330:341	arg1	gonadotropin					306:317	Human chorionic gonadotropin	290:317	Human chorionic gonadotropin (hCG)	290:323	Human chorionic gonadotropin (hCG) is a glycoprotein hormone produced in high concentrations during pregnancy.
16880503	9	5	theme	cancer-derived	1437:1450	arg1	hCGbeta					1452:1458	cancer-derived hCGbeta	1437:1458	cancer-derived hCGbeta	1437:1458	In all samples, the major type of N-glycan was a biantennary complex-type structure, but triantennary structures linked to Asn-30 as well as fucosylation of the Asn-13-bound glycan are increased in cancer-derived hCGbeta.
16880503	12	6	theme	fucose	1767:1772	arg1	content					1774:1780	a higher fucose content	1758:1780	a higher fucose content of Asn-13-linked oligosaccharides	1758:1814	The glycans of free hCGbeta were larger and had a higher fucose content of Asn-13-linked oligosaccharides than intact hCG.
16880503	5	7	theme	various	668:674	arg1	origins					676:682	various origins	668:682	various origins	668:682	We have analyzed tryptic glycopeptides of the beta-subunit of hCG of various origins by liquid chromatography (LC) connected to an electrospray mass spectrometer.
16880503	6	8	theme	analysis	848:855	arg1	software					857:864	differential expression analysis software	824:864	differential expression analysis software	824:864	Site-specific glycan structures were visualized by the use of differential expression analysis software.
16880503	11	9	from	Ser-132	1677:1683	arg1	glycans					1648:1654	Core-2 glycans	1641:1654	Core-2 glycans at either Ser-127 or Ser-132	1641:1683	Core-2 glycans at either Ser-127 or Ser-132 were enriched in cancer.
16880503	10	10	theme	unoccupied	1615:1624	arg1	sites					1609:1613	putative sites	1600:1613	putative sites unoccupied by any glycan	1600:1638	There were significant site-specific differences in the O-glycans, with constant core-2 glycans at Ser-121, core-1 glycans at Ser-138, and putative sites unoccupied by any glycan.
16880503	6	11	theme	differential	824:835	arg1	software					857:864	differential expression analysis software	824:864	differential expression analysis software	824:864	Site-specific glycan structures were visualized by the use of differential expression analysis software.
16880503	2	12	theme	high	363:366	arg1	concentrations					368:381	high concentrations	363:381	high concentrations	363:381	Human chorionic gonadotropin (hCG) is a glycoprotein hormone produced in high concentrations during pregnancy.
16880503	9	13	from	structure	1313:1321	arg1	samples					1246:1252	all samples	1242:1252	all samples	1242:1252	In all samples, the major type of N-glycan was a biantennary complex-type structure, but triantennary structures linked to Asn-30 as well as fucosylation of the Asn-13-bound glycan are increased in cancer-derived hCGbeta.
16880503	10	14	theme	putative	1600:1607	arg1	sites					1609:1613	putative sites	1600:1613	putative sites unoccupied by any glycan	1600:1638	There were significant site-specific differences in the O-glycans, with constant core-2 glycans at Ser-121, core-1 glycans at Ser-138, and putative sites unoccupied by any glycan.
16880503	7	15	theme	cell	1114:1117	arg1	line					1119:1122	a choriocarcinoma cell line	1096:1122	a choriocarcinoma cell line	1096:1122	hCGbeta was purified from urine of two patients with testicular cancer, one with choriocarcinoma, one with an invasive mole, two pregnant women at early and late gestation, from a pharmaceutical preparation and culture medium of a choriocarcinoma cell line.
16880503	2	16	theme	Human	290:294	arg1	hormone					343:349	a glycoprotein hormone	328:349	a glycoprotein hormone produced in high concentrations during pregnancy	328:398	Human chorionic gonadotropin (hCG) is a glycoprotein hormone produced in high concentrations during pregnancy.
16880503	2	16	theme	Human	290:294	arg1	hCG					320:322	hCG	320:322	hCG	320:322	Human chorionic gonadotropin (hCG) is a glycoprotein hormone produced in high concentrations during pregnancy.
16880503	2	16	theme	Human	290:294	arg1	gonadotropin					306:317	Human chorionic gonadotropin	290:317	Human chorionic gonadotropin (hCG)	290:323	Human chorionic gonadotropin (hCG) is a glycoprotein hormone produced in high concentrations during pregnancy.
16880503	9	17	theme	major	1259:1263	arg1	type					1265:1268	the major type	1255:1268	the major type of N-glycan	1255:1280	In all samples, the major type of N-glycan was a biantennary complex-type structure, but triantennary structures linked to Asn-30 as well as fucosylation of the Asn-13-bound glycan are increased in cancer-derived hCGbeta.
16880503	9	17	theme	major	1259:1263	arg1	structure					1313:1321	a biantennary complex-type structure	1286:1321	a biantennary complex-type structure	1286:1321	In all samples, the major type of N-glycan was a biantennary complex-type structure, but triantennary structures linked to Asn-30 as well as fucosylation of the Asn-13-bound glycan are increased in cancer-derived hCGbeta.
16880503	10	18	from	differences	1498:1508	arg1	O-glycans					1517:1525	the O-glycans	1513:1525	the O-glycans	1513:1525	There were significant site-specific differences in the O-glycans, with constant core-2 glycans at Ser-121, core-1 glycans at Ser-138, and putative sites unoccupied by any glycan.
16880503	7	19	theme	late	1024:1027	arg1	gestation					1029:1037	early and late gestation	1014:1037	early and late gestation	1014:1037	hCGbeta was purified from urine of two patients with testicular cancer, one with choriocarcinoma, one with an invasive mole, two pregnant women at early and late gestation, from a pharmaceutical preparation and culture medium of a choriocarcinoma cell line.
16880503	12	20	theme	hCGbeta	1730:1736	arg1	larger					1743:1748	larger	1743:1748	larger	1743:1748	The glycans of free hCGbeta were larger and had a higher fucose content of Asn-13-linked oligosaccharides than intact hCG.
16880503	12	20	theme	hCGbeta	1730:1736	arg1	glycans					1714:1720	The glycans	1710:1720	The glycans of free hCGbeta	1710:1736	The glycans of free hCGbeta were larger and had a higher fucose content of Asn-13-linked oligosaccharides than intact hCG.
16880503	7	21	theme	early	1014:1018	arg1	gestation					1029:1037	early and late gestation	1014:1037	early and late gestation	1014:1037	hCGbeta was purified from urine of two patients with testicular cancer, one with choriocarcinoma, one with an invasive mole, two pregnant women at early and late gestation, from a pharmaceutical preparation and culture medium of a choriocarcinoma cell line.
16880503	1	22	theme	important	185:193	arg1	Glycosylation					165:177	Glycosylation	165:177	Glycosylation	165:177	Glycosylation is an important posttranslational modification in proteins, and aberrant glycosylation occurs in malignancies.
16880503	1	22	theme	important	185:193	arg1	modification					213:224	an important posttranslational modification	182:224	an important posttranslational modification in proteins	182:236	Glycosylation is an important posttranslational modification in proteins, and aberrant glycosylation occurs in malignancies.
16880503	0	23	from	analysis	21:28	arg1	pregnancy					97:105	pregnancy	97:105	pregnancy	97:105	Site-specific glycan analysis of human chorionic gonadotropin beta-subunit from malignancies and pregnancy by liquid chromatography--electrospray mass spectrometry.
16880503	0	23	from	analysis	21:28	arg1	malignancies					80:91	malignancies	80:91	malignancies	80:91	Site-specific glycan analysis of human chorionic gonadotropin beta-subunit from malignancies and pregnancy by liquid chromatography--electrospray mass spectrometry.
16880503	9	24	theme	biantennary	1288:1298	arg1	type					1265:1268	the major type	1255:1268	the major type of N-glycan	1255:1280	In all samples, the major type of N-glycan was a biantennary complex-type structure, but triantennary structures linked to Asn-30 as well as fucosylation of the Asn-13-bound glycan are increased in cancer-derived hCGbeta.
16880503	9	24	theme	biantennary	1288:1298	arg1	structure					1313:1321	a biantennary complex-type structure	1286:1321	a biantennary complex-type structure	1286:1321	In all samples, the major type of N-glycan was a biantennary complex-type structure, but triantennary structures linked to Asn-30 as well as fucosylation of the Asn-13-bound glycan are increased in cancer-derived hCGbeta.
16880503	8	25	from	Asn-30	1149:1154	arg1	N-glycans					1125:1133	N-glycans	1125:1133	N-glycans at Asn-13 and Asn-30 as well as O-glycans at Ser-121, Ser-127, Ser-132, and Ser-138	1125:1217	N-glycans at Asn-13 and Asn-30 as well as O-glycans at Ser-121, Ser-127, Ser-132, and Ser-138 were characterized.
16880503	8	25	from	Asn-30	1149:1154	arg1	O-glycans					1167:1175	O-glycans	1167:1175	N-glycans at Asn-13 and Asn-30 as well as O-glycans at Ser-121, Ser-127, Ser-132, and Ser-138	1125:1217	N-glycans at Asn-13 and Asn-30 as well as O-glycans at Ser-121, Ser-127, Ser-132, and Ser-138 were characterized.
16880503	8	26	from	Asn-13	1138:1143	arg1	N-glycans					1125:1133	N-glycans	1125:1133	N-glycans at Asn-13 and Asn-30 as well as O-glycans at Ser-121, Ser-127, Ser-132, and Ser-138	1125:1217	N-glycans at Asn-13 and Asn-30 as well as O-glycans at Ser-121, Ser-127, Ser-132, and Ser-138 were characterized.
16880503	8	26	from	Asn-13	1138:1143	arg1	O-glycans					1167:1175	O-glycans	1167:1175	N-glycans at Asn-13 and Asn-30 as well as O-glycans at Ser-121, Ser-127, Ser-132, and Ser-138	1125:1217	N-glycans at Asn-13 and Asn-30 as well as O-glycans at Ser-121, Ser-127, Ser-132, and Ser-138 were characterized.
16880503	0	27	theme	chromatography--electrospray	117:144	arg1	spectrometry					151:162	liquid chromatography--electrospray mass spectrometry	110:162	liquid chromatography--electrospray mass spectrometry	110:162	Site-specific glycan analysis of human chorionic gonadotropin beta-subunit from malignancies and pregnancy by liquid chromatography--electrospray mass spectrometry.
16880503	10	28	theme	site-specific	1484:1496	arg1	differences					1498:1508	significant site-specific differences	1472:1508	significant site-specific differences in the O-glycans	1472:1525	There were significant site-specific differences in the O-glycans, with constant core-2 glycans at Ser-121, core-1 glycans at Ser-138, and putative sites unoccupied by any glycan.
16880503	13	29	theme	variant	1897:1903	arg1	detection					1857:1865	the detection	1853:1865	the detection of this malignancy-associated variant	1853:1903	This may facilitate the detection of this malignancy-associated variant by a lectin assay.
16880503	0	30	theme	Site-specific	0:12	arg1	analysis					21:28	Site-specific glycan analysis	0:28	Site-specific glycan analysis of human chorionic gonadotropin beta-subunit from malignancies and pregnancy by liquid chromatography--electrospray mass spectrometry.	0:163	Site-specific glycan analysis of human chorionic gonadotropin beta-subunit from malignancies and pregnancy by liquid chromatography--electrospray mass spectrometry.
16880503	3	31	theme	particular	425:434	arg1	It					401:402	It	401:402	It	401:402	It is also expressed as particular glycoforms by certain malignancies.
16880503	3	31	theme	particular	425:434	arg1	glycoforms					436:445	particular glycoforms	425:445	particular glycoforms	425:445	It is also expressed as particular glycoforms by certain malignancies.
16880503	9	32	gly	fucosylation	1380:1391	arg1	glycan					1413:1418	the Asn-13-bound glycan	1396:1418	the Asn-13-bound glycan	1396:1418	In all samples, the major type of N-glycan was a biantennary complex-type structure, but triantennary structures linked to Asn-30 as well as fucosylation of the Asn-13-bound glycan are increased in cancer-derived hCGbeta.
16880503	0	33	theme	human	33:37	arg1	beta-subunit					62:73	human chorionic gonadotropin beta-subunit	33:73	human chorionic gonadotropin beta-subunit from malignancies and pregnancy	33:105	Site-specific glycan analysis of human chorionic gonadotropin beta-subunit from malignancies and pregnancy by liquid chromatography--electrospray mass spectrometry.
16880503	0	34	theme	gonadotropin	49:60	arg1	beta-subunit					62:73	human chorionic gonadotropin beta-subunit	33:73	human chorionic gonadotropin beta-subunit from malignancies and pregnancy	33:105	Site-specific glycan analysis of human chorionic gonadotropin beta-subunit from malignancies and pregnancy by liquid chromatography--electrospray mass spectrometry.
16880503	10	35	from	Ser-138	1587:1593	arg1	glycans					1576:1582	core-1 glycans	1569:1582	core-1 glycans at Ser-138	1569:1593	There were significant site-specific differences in the O-glycans, with constant core-2 glycans at Ser-121, core-1 glycans at Ser-138, and putative sites unoccupied by any glycan.
16880503	10	35	from	Ser-138	1587:1593	arg1	glycans					1549:1555	constant core-2 glycans	1533:1555	constant core-2 glycans at Ser-121	1533:1566	There were significant site-specific differences in the O-glycans, with constant core-2 glycans at Ser-121, core-1 glycans at Ser-138, and putative sites unoccupied by any glycan.
16880503	10	35	from	Ser-138	1587:1593	arg1	sites					1609:1613	putative sites	1600:1613	putative sites unoccupied by any glycan	1600:1638	There were significant site-specific differences in the O-glycans, with constant core-2 glycans at Ser-121, core-1 glycans at Ser-138, and putative sites unoccupied by any glycan.
16880503	4	36	theme	complex	574:580	arg1	moieties					589:596	more complex glycan moieties	569:596	more complex glycan moieties	569:596	These glycoforms, which are called "hyperglycosylated" hCG (hCGh), have been reported to contain more complex glycan moieties.
16880503	10	37	theme	core-2	1542:1547	arg1	glycans					1549:1555	constant core-2 glycans	1533:1555	constant core-2 glycans at Ser-121	1533:1566	There were significant site-specific differences in the O-glycans, with constant core-2 glycans at Ser-121, core-1 glycans at Ser-138, and putative sites unoccupied by any glycan.
16880503	4	38	gly	hyperglycosylated	508:524	arg1	"					525:525	"hyperglycosylated" hCG (hCGh)	507:536	"hyperglycosylated" hCG (hCGh)	507:536	These glycoforms, which are called "hyperglycosylated" hCG (hCGh), have been reported to contain more complex glycan moieties.
16880503	12	39	theme	Asn-13-linked	1785:1797	arg1	oligosaccharides					1799:1814	Asn-13-linked oligosaccharides	1785:1814	Asn-13-linked oligosaccharides	1785:1814	The glycans of free hCGbeta were larger and had a higher fucose content of Asn-13-linked oligosaccharides than intact hCG.
16880503	14	40	from	glycan	2027:2032	arg1	Ser-132					2037:2043	Ser-132	2037:2043	Ser-132	2037:2043	Analysis of hCGh affinity purified with antibody B152 confirmed that this antibody recognizes a core-2 glycan on Ser-132.
16880503	11	41	theme	Core-2	1641:1646	arg1	glycans					1648:1654	Core-2 glycans	1641:1654	Core-2 glycans at either Ser-127 or Ser-132	1641:1683	Core-2 glycans at either Ser-127 or Ser-132 were enriched in cancer.
16880503	9	42	theme	Asn-13-bound	1400:1411	arg1	glycan					1413:1418	the Asn-13-bound glycan	1396:1418	the Asn-13-bound glycan	1396:1418	In all samples, the major type of N-glycan was a biantennary complex-type structure, but triantennary structures linked to Asn-30 as well as fucosylation of the Asn-13-bound glycan are increased in cancer-derived hCGbeta.
16880503	12	43	link	Asn-13-linked	1785:1797	arg1	oligosaccharides					1799:1814	Asn-13-linked oligosaccharides	1785:1814	Asn-13-linked oligosaccharides	1785:1814	The glycans of free hCGbeta were larger and had a higher fucose content of Asn-13-linked oligosaccharides than intact hCG.
16880503	8	44	from	Ser-138	1211:1217	arg1	N-glycans					1125:1133	N-glycans	1125:1133	N-glycans at Asn-13 and Asn-30 as well as O-glycans at Ser-121, Ser-127, Ser-132, and Ser-138	1125:1217	N-glycans at Asn-13 and Asn-30 as well as O-glycans at Ser-121, Ser-127, Ser-132, and Ser-138 were characterized.
16880503	8	44	from	Ser-138	1211:1217	arg1	O-glycans					1167:1175	O-glycans	1167:1175	N-glycans at Asn-13 and Asn-30 as well as O-glycans at Ser-121, Ser-127, Ser-132, and Ser-138	1125:1217	N-glycans at Asn-13 and Asn-30 as well as O-glycans at Ser-121, Ser-127, Ser-132, and Ser-138 were characterized.
16880503	14	45	theme	affinity	1941:1948	arg1	Analysis					1924:1931	Analysis	1924:1931	Analysis of hCGh affinity purified with antibody B152	1924:1976	Analysis of hCGh affinity purified with antibody B152 confirmed that this antibody recognizes a core-2 glycan on Ser-132.
16880503	5	46	theme	liquid	687:692	arg1	chromatography					694:707	liquid chromatography	687:707	liquid chromatography (LC) connected to an electrospray mass spectrometer	687:759	We have analyzed tryptic glycopeptides of the beta-subunit of hCG of various origins by liquid chromatography (LC) connected to an electrospray mass spectrometer.
16880503	5	46	theme	liquid	687:692	arg1	LC					710:711	LC	710:711	LC	710:711	We have analyzed tryptic glycopeptides of the beta-subunit of hCG of various origins by liquid chromatography (LC) connected to an electrospray mass spectrometer.
16880503	6	47	theme	Site-specific	762:774	arg1	structures					783:792	Site-specific glycan structures	762:792	Site-specific glycan structures	762:792	Site-specific glycan structures were visualized by the use of differential expression analysis software.
16880503	5	48	theme	origins	676:682	arg1	hCG					661:663	hCG	661:663	hCG of various origins	661:682	We have analyzed tryptic glycopeptides of the beta-subunit of hCG of various origins by liquid chromatography (LC) connected to an electrospray mass spectrometer.
16880503	12	49	theme	higher	1760:1765	arg1	content					1774:1780	a higher fucose content	1758:1780	a higher fucose content of Asn-13-linked oligosaccharides	1758:1814	The glycans of free hCGbeta were larger and had a higher fucose content of Asn-13-linked oligosaccharides than intact hCG.
16880503	2	50	gly	glycoprotein	330:341	arg1	glycoprotein					330:341	a glycoprotein hormone	328:349	a glycoprotein hormone produced in high concentrations during pregnancy	328:398	Human chorionic gonadotropin (hCG) is a glycoprotein hormone produced in high concentrations during pregnancy.
16880503	5	51	gly	glycopeptides	624:636	arg1	beta-subunit					645:656	the beta-subunit	641:656	the beta-subunit of hCG of various origins	641:682	We have analyzed tryptic glycopeptides of the beta-subunit of hCG of various origins by liquid chromatography (LC) connected to an electrospray mass spectrometer.
16880503	5	51	gly	glycopeptides	624:636	arg2	glycopeptides					624:636	tryptic glycopeptides	616:636	tryptic glycopeptides of the beta-subunit of hCG of various origins	616:682	We have analyzed tryptic glycopeptides of the beta-subunit of hCG of various origins by liquid chromatography (LC) connected to an electrospray mass spectrometer.
16880503	1	52	gly	glycosylation	252:264	arg2	malignancies					276:287	malignancies	276:287	malignancies	276:287	Glycosylation is an important posttranslational modification in proteins, and aberrant glycosylation occurs in malignancies.
16880503	6	53	theme	software	857:864	arg1	use					817:819	the use	813:819	the use of differential expression analysis software	813:864	Site-specific glycan structures were visualized by the use of differential expression analysis software.
16880503	4	54	contain	contain	561:567	arg2	moieties					589:596	more complex glycan moieties	569:596	more complex glycan moieties	569:596	These glycoforms, which are called "hyperglycosylated" hCG (hCGh), have been reported to contain more complex glycan moieties.
16880503	4	54	contain	contain	561:567	arg1	glycoforms					478:487	These glycoforms	472:487	These glycoforms	472:487	These glycoforms, which are called "hyperglycosylated" hCG (hCGh), have been reported to contain more complex glycan moieties.
16880503	7	55	theme	testicular	920:929	arg1	cancer					931:936	testicular cancer	920:936	testicular cancer	920:936	hCGbeta was purified from urine of two patients with testicular cancer, one with choriocarcinoma, one with an invasive mole, two pregnant women at early and late gestation, from a pharmaceutical preparation and culture medium of a choriocarcinoma cell line.
16880503	14	56	theme	hCGh	1936:1939	arg1	affinity					1941:1948	hCGh affinity	1936:1948	hCGh affinity purified with antibody B152	1936:1976	Analysis of hCGh affinity purified with antibody B152 confirmed that this antibody recognizes a core-2 glycan on Ser-132.
16880503	7	57	theme	line	1119:1122	arg1	preparation					1062:1072	a pharmaceutical preparation	1045:1072	a pharmaceutical preparation	1045:1072	hCGbeta was purified from urine of two patients with testicular cancer, one with choriocarcinoma, one with an invasive mole, two pregnant women at early and late gestation, from a pharmaceutical preparation and culture medium of a choriocarcinoma cell line.
16880503	7	57	theme	line	1119:1122	arg1	medium					1086:1091	culture medium	1078:1091	culture medium	1078:1091	hCGbeta was purified from urine of two patients with testicular cancer, one with choriocarcinoma, one with an invasive mole, two pregnant women at early and late gestation, from a pharmaceutical preparation and culture medium of a choriocarcinoma cell line.
16880503	6	58	theme	expression	837:846	arg1	software					857:864	differential expression analysis software	824:864	differential expression analysis software	824:864	Site-specific glycan structures were visualized by the use of differential expression analysis software.
16880503	7	59	theme	patients	906:913	arg1	urine					893:897	urine	893:897	urine of two patients with testicular cancer, one with choriocarcinoma, one with an invasive mole, two pregnant women at early and late gestation,	893:1038	hCGbeta was purified from urine of two patients with testicular cancer, one with choriocarcinoma, one with an invasive mole, two pregnant women at early and late gestation, from a pharmaceutical preparation and culture medium of a choriocarcinoma cell line.
16880503	7	60	from	gestation	1029:1037	arg1	patients					906:913	two patients	902:913	two patients with testicular cancer	902:936	hCGbeta was purified from urine of two patients with testicular cancer, one with choriocarcinoma, one with an invasive mole, two pregnant women at early and late gestation, from a pharmaceutical preparation and culture medium of a choriocarcinoma cell line.
16880503	7	60	from	gestation	1029:1037	arg1	women					1005:1009	two pregnant women	992:1009	two pregnant women at early and late gestation	992:1037	hCGbeta was purified from urine of two patients with testicular cancer, one with choriocarcinoma, one with an invasive mole, two pregnant women at early and late gestation, from a pharmaceutical preparation and culture medium of a choriocarcinoma cell line.
16880503	5	61	theme	electrospray	730:741	arg1	spectrometer					748:759	an electrospray mass spectrometer	727:759	an electrospray mass spectrometer	727:759	We have analyzed tryptic glycopeptides of the beta-subunit of hCG of various origins by liquid chromatography (LC) connected to an electrospray mass spectrometer.
16880503	1	62	theme	aberrant	243:250	arg1	glycosylation					252:264	aberrant glycosylation	243:264	aberrant glycosylation	243:264	Glycosylation is an important posttranslational modification in proteins, and aberrant glycosylation occurs in malignancies.
16880503	4	63	theme	hyperglycosylated	508:524	arg1	"					525:525	"hyperglycosylated" hCG (hCGh)	507:536	"hyperglycosylated" hCG (hCGh)	507:536	These glycoforms, which are called "hyperglycosylated" hCG (hCGh), have been reported to contain more complex glycan moieties.
16880503	7	64	theme	pregnant	996:1003	arg1	patients					906:913	two patients	902:913	two patients with testicular cancer	902:936	hCGbeta was purified from urine of two patients with testicular cancer, one with choriocarcinoma, one with an invasive mole, two pregnant women at early and late gestation, from a pharmaceutical preparation and culture medium of a choriocarcinoma cell line.
16880503	7	64	theme	pregnant	996:1003	arg1	women					1005:1009	two pregnant women	992:1009	two pregnant women at early and late gestation	992:1037	hCGbeta was purified from urine of two patients with testicular cancer, one with choriocarcinoma, one with an invasive mole, two pregnant women at early and late gestation, from a pharmaceutical preparation and culture medium of a choriocarcinoma cell line.
16880503	2	65	theme	chorionic	296:304	arg1	hormone					343:349	a glycoprotein hormone	328:349	a glycoprotein hormone produced in high concentrations during pregnancy	328:398	Human chorionic gonadotropin (hCG) is a glycoprotein hormone produced in high concentrations during pregnancy.
16880503	2	65	theme	chorionic	296:304	arg1	hCG					320:322	hCG	320:322	hCG	320:322	Human chorionic gonadotropin (hCG) is a glycoprotein hormone produced in high concentrations during pregnancy.
16880503	2	65	theme	chorionic	296:304	arg1	gonadotropin					306:317	Human chorionic gonadotropin	290:317	Human chorionic gonadotropin (hCG)	290:323	Human chorionic gonadotropin (hCG) is a glycoprotein hormone produced in high concentrations during pregnancy.
16880503	0	66	from	malignancies	80:91	arg1	analysis					21:28	Site-specific glycan analysis	0:28	Site-specific glycan analysis of human chorionic gonadotropin beta-subunit from malignancies and pregnancy by liquid chromatography--electrospray mass spectrometry.	0:163	Site-specific glycan analysis of human chorionic gonadotropin beta-subunit from malignancies and pregnancy by liquid chromatography--electrospray mass spectrometry.
16880503	0	66	from	malignancies	80:91	arg1	beta-subunit					62:73	human chorionic gonadotropin beta-subunit	33:73	human chorionic gonadotropin beta-subunit from malignancies and pregnancy	33:105	Site-specific glycan analysis of human chorionic gonadotropin beta-subunit from malignancies and pregnancy by liquid chromatography--electrospray mass spectrometry.
16880503	7	67	theme	culture	1078:1084	arg1	medium					1086:1091	culture medium	1078:1091	culture medium	1078:1091	hCGbeta was purified from urine of two patients with testicular cancer, one with choriocarcinoma, one with an invasive mole, two pregnant women at early and late gestation, from a pharmaceutical preparation and culture medium of a choriocarcinoma cell line.
16880503	7	68	theme	pharmaceutical	1047:1060	arg1	preparation					1062:1072	a pharmaceutical preparation	1045:1072	a pharmaceutical preparation	1045:1072	hCGbeta was purified from urine of two patients with testicular cancer, one with choriocarcinoma, one with an invasive mole, two pregnant women at early and late gestation, from a pharmaceutical preparation and culture medium of a choriocarcinoma cell line.
16880503	7	69	theme	choriocarcinoma	1098:1112	arg1	line					1119:1122	a choriocarcinoma cell line	1096:1122	a choriocarcinoma cell line	1096:1122	hCGbeta was purified from urine of two patients with testicular cancer, one with choriocarcinoma, one with an invasive mole, two pregnant women at early and late gestation, from a pharmaceutical preparation and culture medium of a choriocarcinoma cell line.
16880503	7	70	with	patients	906:913	arg1	cancer					931:936	testicular cancer	920:936	testicular cancer	920:936	hCGbeta was purified from urine of two patients with testicular cancer, one with choriocarcinoma, one with an invasive mole, two pregnant women at early and late gestation, from a pharmaceutical preparation and culture medium of a choriocarcinoma cell line.
16880503	5	71	theme	beta-subunit	645:656	arg1	glycopeptides					624:636	tryptic glycopeptides	616:636	tryptic glycopeptides of the beta-subunit of hCG of various origins	616:682	We have analyzed tryptic glycopeptides of the beta-subunit of hCG of various origins by liquid chromatography (LC) connected to an electrospray mass spectrometer.
16880503	12	72	contain	had	1754:1756	arg2	content					1774:1780	a higher fucose content	1758:1780	a higher fucose content of Asn-13-linked oligosaccharides	1758:1814	The glycans of free hCGbeta were larger and had a higher fucose content of Asn-13-linked oligosaccharides than intact hCG.
16880503	12	72	contain	had	1754:1756	arg1	larger					1743:1748	larger	1743:1748	larger	1743:1748	The glycans of free hCGbeta were larger and had a higher fucose content of Asn-13-linked oligosaccharides than intact hCG.
16880503	12	72	contain	had	1754:1756	arg1	glycans					1714:1720	The glycans	1710:1720	The glycans of free hCGbeta	1710:1736	The glycans of free hCGbeta were larger and had a higher fucose content of Asn-13-linked oligosaccharides than intact hCG.
16880503	9	73	theme	N-glycan	1273:1280	arg1	type					1265:1268	the major type	1255:1268	the major type of N-glycan	1255:1280	In all samples, the major type of N-glycan was a biantennary complex-type structure, but triantennary structures linked to Asn-30 as well as fucosylation of the Asn-13-bound glycan are increased in cancer-derived hCGbeta.
16880503	9	73	theme	N-glycan	1273:1280	arg1	structure					1313:1321	a biantennary complex-type structure	1286:1321	a biantennary complex-type structure	1286:1321	In all samples, the major type of N-glycan was a biantennary complex-type structure, but triantennary structures linked to Asn-30 as well as fucosylation of the Asn-13-bound glycan are increased in cancer-derived hCGbeta.
16880503	12	74	theme	free	1725:1728	arg1	hCGbeta					1730:1736	free hCGbeta	1725:1736	free hCGbeta	1725:1736	The glycans of free hCGbeta were larger and had a higher fucose content of Asn-13-linked oligosaccharides than intact hCG.
16880503	1	75	theme	posttranslational	195:211	arg1	Glycosylation					165:177	Glycosylation	165:177	Glycosylation	165:177	Glycosylation is an important posttranslational modification in proteins, and aberrant glycosylation occurs in malignancies.
16880503	1	75	theme	posttranslational	195:211	arg1	modification					213:224	an important posttranslational modification	182:224	an important posttranslational modification in proteins	182:236	Glycosylation is an important posttranslational modification in proteins, and aberrant glycosylation occurs in malignancies.
16880503	5	76	theme	mass	743:746	arg1	spectrometer					748:759	an electrospray mass spectrometer	727:759	an electrospray mass spectrometer	727:759	We have analyzed tryptic glycopeptides of the beta-subunit of hCG of various origins by liquid chromatography (LC) connected to an electrospray mass spectrometer.
16880503	13	77	theme	lectin	1910:1915	arg1	assay					1917:1921	a lectin assay	1908:1921	a lectin assay	1908:1921	This may facilitate the detection of this malignancy-associated variant by a lectin assay.
16880503	0	78	from	pregnancy	97:105	arg1	analysis					21:28	Site-specific glycan analysis	0:28	Site-specific glycan analysis of human chorionic gonadotropin beta-subunit from malignancies and pregnancy by liquid chromatography--electrospray mass spectrometry.	0:163	Site-specific glycan analysis of human chorionic gonadotropin beta-subunit from malignancies and pregnancy by liquid chromatography--electrospray mass spectrometry.
16880503	0	78	from	pregnancy	97:105	arg1	beta-subunit					62:73	human chorionic gonadotropin beta-subunit	33:73	human chorionic gonadotropin beta-subunit from malignancies and pregnancy	33:105	Site-specific glycan analysis of human chorionic gonadotropin beta-subunit from malignancies and pregnancy by liquid chromatography--electrospray mass spectrometry.
16880503	0	79	theme	liquid	110:115	arg1	spectrometry					151:162	liquid chromatography--electrospray mass spectrometry	110:162	liquid chromatography--electrospray mass spectrometry	110:162	Site-specific glycan analysis of human chorionic gonadotropin beta-subunit from malignancies and pregnancy by liquid chromatography--electrospray mass spectrometry.
16880503	9	80	theme	complex-type	1300:1311	arg1	type					1265:1268	the major type	1255:1268	the major type of N-glycan	1255:1280	In all samples, the major type of N-glycan was a biantennary complex-type structure, but triantennary structures linked to Asn-30 as well as fucosylation of the Asn-13-bound glycan are increased in cancer-derived hCGbeta.
16880503	9	80	theme	complex-type	1300:1311	arg1	structure					1313:1321	a biantennary complex-type structure	1286:1321	a biantennary complex-type structure	1286:1321	In all samples, the major type of N-glycan was a biantennary complex-type structure, but triantennary structures linked to Asn-30 as well as fucosylation of the Asn-13-bound glycan are increased in cancer-derived hCGbeta.
16880503	1	81	from	modification	213:224	arg1	proteins					229:236	proteins	229:236	proteins	229:236	Glycosylation is an important posttranslational modification in proteins, and aberrant glycosylation occurs in malignancies.
16880503	0	82	theme	mass	146:149	arg1	spectrometry					151:162	liquid chromatography--electrospray mass spectrometry	110:162	liquid chromatography--electrospray mass spectrometry	110:162	Site-specific glycan analysis of human chorionic gonadotropin beta-subunit from malignancies and pregnancy by liquid chromatography--electrospray mass spectrometry.
16880503	5	83	theme	hCG	661:663	arg1	beta-subunit					645:656	the beta-subunit	641:656	the beta-subunit of hCG of various origins	641:682	We have analyzed tryptic glycopeptides of the beta-subunit of hCG of various origins by liquid chromatography (LC) connected to an electrospray mass spectrometer.
16880503	13	84	theme	malignancy-associated	1875:1895	arg1	variant					1897:1903	this malignancy-associated variant	1870:1903	this malignancy-associated variant	1870:1903	This may facilitate the detection of this malignancy-associated variant by a lectin assay.
16880503	0	85	theme	glycan	14:19	arg1	analysis					21:28	Site-specific glycan analysis	0:28	Site-specific glycan analysis of human chorionic gonadotropin beta-subunit from malignancies and pregnancy by liquid chromatography--electrospray mass spectrometry.	0:163	Site-specific glycan analysis of human chorionic gonadotropin beta-subunit from malignancies and pregnancy by liquid chromatography--electrospray mass spectrometry.
16880503	9	86	theme	triantennary	1328:1339	arg1	structures					1341:1350	triantennary structures	1328:1350	triantennary structures linked to Asn-30 as well as fucosylation of the Asn-13-bound glycan	1328:1418	In all samples, the major type of N-glycan was a biantennary complex-type structure, but triantennary structures linked to Asn-30 as well as fucosylation of the Asn-13-bound glycan are increased in cancer-derived hCGbeta.
16880503	5	87	theme	tryptic	616:622	arg1	glycopeptides					624:636	tryptic glycopeptides	616:636	tryptic glycopeptides of the beta-subunit of hCG of various origins	616:682	We have analyzed tryptic glycopeptides of the beta-subunit of hCG of various origins by liquid chromatography (LC) connected to an electrospray mass spectrometer.
16880503	14	88	theme	core-2	2020:2025	arg1	glycan					2027:2032	a core-2 glycan	2018:2032	a core-2 glycan on Ser-132	2018:2043	Analysis of hCGh affinity purified with antibody B152 confirmed that this antibody recognizes a core-2 glycan on Ser-132.
16880503	3	89	theme	certain	450:456	arg1	malignancies					458:469	certain malignancies	450:469	certain malignancies	450:469	It is also expressed as particular glycoforms by certain malignancies.
16880503	10	90	theme	significant	1472:1482	arg1	differences					1498:1508	significant site-specific differences	1472:1508	significant site-specific differences in the O-glycans	1472:1525	There were significant site-specific differences in the O-glycans, with constant core-2 glycans at Ser-121, core-1 glycans at Ser-138, and putative sites unoccupied by any glycan.
16880503	7	91	theme	invasive	977:984	arg1	mole					986:989	an invasive mole	974:989	an invasive mole	974:989	hCGbeta was purified from urine of two patients with testicular cancer, one with choriocarcinoma, one with an invasive mole, two pregnant women at early and late gestation, from a pharmaceutical preparation and culture medium of a choriocarcinoma cell line.
16880503	0	92	theme	chorionic	39:47	arg1	beta-subunit					62:73	human chorionic gonadotropin beta-subunit	33:73	human chorionic gonadotropin beta-subunit from malignancies and pregnancy	33:105	Site-specific glycan analysis of human chorionic gonadotropin beta-subunit from malignancies and pregnancy by liquid chromatography--electrospray mass spectrometry.
16880503	10	93	from	Ser-121	1560:1566	arg1	glycans					1576:1582	core-1 glycans	1569:1582	core-1 glycans at Ser-138	1569:1593	There were significant site-specific differences in the O-glycans, with constant core-2 glycans at Ser-121, core-1 glycans at Ser-138, and putative sites unoccupied by any glycan.
16880503	10	93	from	Ser-121	1560:1566	arg1	glycans					1549:1555	constant core-2 glycans	1533:1555	constant core-2 glycans at Ser-121	1533:1566	There were significant site-specific differences in the O-glycans, with constant core-2 glycans at Ser-121, core-1 glycans at Ser-138, and putative sites unoccupied by any glycan.
16880503	10	93	from	Ser-121	1560:1566	arg1	sites					1609:1613	putative sites	1600:1613	putative sites unoccupied by any glycan	1600:1638	There were significant site-specific differences in the O-glycans, with constant core-2 glycans at Ser-121, core-1 glycans at Ser-138, and putative sites unoccupied by any glycan.
16880503	9	94	attach	linked	1352:1357	arg2	structures					1341:1350	triantennary structures	1328:1350	triantennary structures linked to Asn-30 as well as fucosylation of the Asn-13-bound glycan	1328:1418	In all samples, the major type of N-glycan was a biantennary complex-type structure, but triantennary structures linked to Asn-30 as well as fucosylation of the Asn-13-bound glycan are increased in cancer-derived hCGbeta.
16880503	9	94	attach	linked	1352:1357	arg1	Asn-30					1362:1367	Asn-30	1362:1367	Asn-30 as well as fucosylation of the Asn-13-bound glycan	1362:1418	In all samples, the major type of N-glycan was a biantennary complex-type structure, but triantennary structures linked to Asn-30 as well as fucosylation of the Asn-13-bound glycan are increased in cancer-derived hCGbeta.
16880503	9	94	attach	linked	1352:1357	arg1	fucosylation					1380:1391	fucosylation	1380:1391	Asn-30 as well as fucosylation of the Asn-13-bound glycan	1362:1418	In all samples, the major type of N-glycan was a biantennary complex-type structure, but triantennary structures linked to Asn-30 as well as fucosylation of the Asn-13-bound glycan are increased in cancer-derived hCGbeta.
16880503	0	95	theme	beta-subunit	62:73	arg1	analysis					21:28	Site-specific glycan analysis	0:28	Site-specific glycan analysis of human chorionic gonadotropin beta-subunit from malignancies and pregnancy by liquid chromatography--electrospray mass spectrometry.	0:163	Site-specific glycan analysis of human chorionic gonadotropin beta-subunit from malignancies and pregnancy by liquid chromatography--electrospray mass spectrometry.
16880503	12	96	theme	intact	1821:1826	arg1	hCG					1828:1830	intact hCG	1821:1830	intact hCG	1821:1830	The glycans of free hCGbeta were larger and had a higher fucose content of Asn-13-linked oligosaccharides than intact hCG.
16880503	11	97	from	Ser-127	1666:1672	arg1	glycans					1648:1654	Core-2 glycans	1641:1654	Core-2 glycans at either Ser-127 or Ser-132	1641:1683	Core-2 glycans at either Ser-127 or Ser-132 were enriched in cancer.
16880503	4	98	theme	glycan	582:587	arg1	moieties					589:596	more complex glycan moieties	569:596	more complex glycan moieties	569:596	These glycoforms, which are called "hyperglycosylated" hCG (hCGh), have been reported to contain more complex glycan moieties.
16880503	8	99	from	Ser-127	1189:1195	arg1	N-glycans					1125:1133	N-glycans	1125:1133	N-glycans at Asn-13 and Asn-30 as well as O-glycans at Ser-121, Ser-127, Ser-132, and Ser-138	1125:1217	N-glycans at Asn-13 and Asn-30 as well as O-glycans at Ser-121, Ser-127, Ser-132, and Ser-138 were characterized.
16880503	8	99	from	Ser-127	1189:1195	arg1	O-glycans					1167:1175	O-glycans	1167:1175	N-glycans at Asn-13 and Asn-30 as well as O-glycans at Ser-121, Ser-127, Ser-132, and Ser-138	1125:1217	N-glycans at Asn-13 and Asn-30 as well as O-glycans at Ser-121, Ser-127, Ser-132, and Ser-138 were characterized.
16880503	14	100	theme	antibody	1964:1971	arg1	B152					1973:1976	antibody B152	1964:1976	antibody B152	1964:1976	Analysis of hCGh affinity purified with antibody B152 confirmed that this antibody recognizes a core-2 glycan on Ser-132.
16880503	10	101	theme	constant	1533:1540	arg1	glycans					1549:1555	constant core-2 glycans	1533:1555	constant core-2 glycans at Ser-121	1533:1566	There were significant site-specific differences in the O-glycans, with constant core-2 glycans at Ser-121, core-1 glycans at Ser-138, and putative sites unoccupied by any glycan.
16880503	8	102	from	Ser-121	1180:1186	arg1	N-glycans					1125:1133	N-glycans	1125:1133	N-glycans at Asn-13 and Asn-30 as well as O-glycans at Ser-121, Ser-127, Ser-132, and Ser-138	1125:1217	N-glycans at Asn-13 and Asn-30 as well as O-glycans at Ser-121, Ser-127, Ser-132, and Ser-138 were characterized.
16880503	8	102	from	Ser-121	1180:1186	arg1	O-glycans					1167:1175	O-glycans	1167:1175	N-glycans at Asn-13 and Asn-30 as well as O-glycans at Ser-121, Ser-127, Ser-132, and Ser-138	1125:1217	N-glycans at Asn-13 and Asn-30 as well as O-glycans at Ser-121, Ser-127, Ser-132, and Ser-138 were characterized.
16880503	10	103	theme	core-1	1569:1574	arg1	glycans					1576:1582	core-1 glycans	1569:1582	core-1 glycans at Ser-138	1569:1593	There were significant site-specific differences in the O-glycans, with constant core-2 glycans at Ser-121, core-1 glycans at Ser-138, and putative sites unoccupied by any glycan.
16880503	6	104	theme	glycan	776:781	arg1	structures					783:792	Site-specific glycan structures	762:792	Site-specific glycan structures	762:792	Site-specific glycan structures were visualized by the use of differential expression analysis software.
16880503	9	105	theme	glycan	1413:1418	arg1	Asn-30					1362:1367	Asn-30	1362:1367	Asn-30 as well as fucosylation of the Asn-13-bound glycan	1362:1418	In all samples, the major type of N-glycan was a biantennary complex-type structure, but triantennary structures linked to Asn-30 as well as fucosylation of the Asn-13-bound glycan are increased in cancer-derived hCGbeta.
16880503	9	105	theme	glycan	1413:1418	arg1	fucosylation					1380:1391	fucosylation	1380:1391	Asn-30 as well as fucosylation of the Asn-13-bound glycan	1362:1418	In all samples, the major type of N-glycan was a biantennary complex-type structure, but triantennary structures linked to Asn-30 as well as fucosylation of the Asn-13-bound glycan are increased in cancer-derived hCGbeta.
10537138	10	0	theme	plasma	2069:2074	arg1	membrane					2076:2083	the plasma membrane	2065:2083	the plasma membrane	2065:2083	Using an anti-c-Myc monoclonal antibody and confocal microscopy, all of the mutant receptors were found to be expressed and delivered to the plasma membrane.
10537138	0	1	link	N-linked	8:15	arg1	glycosylation					17:29	N-linked glycosylation	8:29	N-linked glycosylation	8:29	Role of N-linked glycosylation on the function and expression of the human secretin receptor.
10537138	8	2	theme	competitive	1579:1589	arg1	studies					1599:1605	competitive binding studies	1579:1605	competitive binding studies	1579:1605	This hypothesis was further supported by competitive binding studies, the same mutants were found to be defective in binding with [125I]secretin.
10537138	1	3	theme	pancreatic	158:167	arg1	water					169:173	pancreatic water	158:173	pancreatic water	158:173	Secretin is a 27-amino acid long peptide hormone that regulates pancreatic water, bicarbonate, enzymes, and potassium ion secretion.
10537138	9	4	from	change	1708:1713	arg1	function					1727:1734	receptor function	1718:1734	receptor function of the mutants	1718:1749	To evaluate whether the change in receptor function of the mutants is caused by the change in the process of presenting the receptor to the cell surface, the mutants and the wild-type receptor were tagged with a c-Myc epitope at the C-termini.
10537138	3	5	theme	secretin-stimulated	673:691	arg1	response					698:705	the secretin-stimulated cAMP response	669:705	the secretin-stimulated cAMP response	669:705	Through functional analysis of the hSR-transfected cells cultured in the presence of various glycosylation inhibitors, it was found that tunicamycin and castanospermine were able to significantly reduce the secretin-stimulated cAMP response.
10537138	6	6	from	values	1308:1313	arg1	assays					1351:1356	the two assays	1343:1356	the two assays	1343:1356	The ED50 values of the wild-type receptor in these two assay systems were 0.25 and 0.11 nM, respectively, and mutation at position 100, 106, or 291 did not affect either the ED50 values or the maximal responses in the two assays.
10537138	6	7	theme	receptor	1162:1169	arg1	values					1138:1143	The ED50 values	1129:1143	The ED50 values of the wild-type receptor in these two assay systems	1129:1196	The ED50 values of the wild-type receptor in these two assay systems were 0.25 and 0.11 nM, respectively, and mutation at position 100, 106, or 291 did not affect either the ED50 values or the maximal responses in the two assays.
10537138	6	7	theme	receptor	1162:1169	arg1	nM					1217:1218	0.25 and 0.11 nM	1203:1218	0.25 and 0.11 nM	1203:1218	The ED50 values of the wild-type receptor in these two assay systems were 0.25 and 0.11 nM, respectively, and mutation at position 100, 106, or 291 did not affect either the ED50 values or the maximal responses in the two assays.
10537138	10	8	theme	anti-c-Myc	1937:1946	arg1	antibody					1959:1966	an anti-c-Myc monoclonal antibody	1934:1966	an anti-c-Myc monoclonal antibody	1934:1966	Using an anti-c-Myc monoclonal antibody and confocal microscopy, all of the mutant receptors were found to be expressed and delivered to the plasma membrane.
10537138	3	9	theme	cells	517:521	arg1	analysis					485:492	functional analysis	474:492	functional analysis of the hSR-transfected cells cultured in the presence of various glycosylation inhibitors	474:582	Through functional analysis of the hSR-transfected cells cultured in the presence of various glycosylation inhibitors, it was found that tunicamycin and castanospermine were able to significantly reduce the secretin-stimulated cAMP response.
10537138	4	10	theme	mannose-type	839:850	arg1	side-chain					865:874	the high mannose-type carbohydrate side-chain	830:874	the high mannose-type carbohydrate side-chain	830:874	On the other hand, the effects of other inhibitors, swainsonine and deoxymannojirimycin, were much lower, suggesting that the high mannose-type carbohydrate side-chain is essential to the expression of a fully functional hSR.
10537138	4	10	theme	mannose-type	839:850	arg1	essential					879:887	essential	879:887	essential	879:887	On the other hand, the effects of other inhibitors, swainsonine and deoxymannojirimycin, were much lower, suggesting that the high mannose-type carbohydrate side-chain is essential to the expression of a fully functional hSR.
10537138	10	11	theme	confocal	1972:1979	arg1	microscopy					1981:1990	confocal microscopy	1972:1990	confocal microscopy	1972:1990	Using an anti-c-Myc monoclonal antibody and confocal microscopy, all of the mutant receptors were found to be expressed and delivered to the plasma membrane.
10537138	3	12	theme	various	551:557	arg1	inhibitors					573:582	various glycosylation inhibitors	551:582	various glycosylation inhibitors	551:582	Through functional analysis of the hSR-transfected cells cultured in the presence of various glycosylation inhibitors, it was found that tunicamycin and castanospermine were able to significantly reduce the secretin-stimulated cAMP response.
10537138	1	13	theme	acid	117:120	arg1	hormone					135:141	a 27-amino acid long peptide hormone	106:141	a 27-amino acid long peptide hormone that regulates pancreatic water, bicarbonate, enzymes, and potassium ion secretion	106:224	Secretin is a 27-amino acid long peptide hormone that regulates pancreatic water, bicarbonate, enzymes, and potassium ion secretion.
10537138	1	13	theme	acid	117:120	arg1	Secretin					94:101	Secretin	94:101	Secretin	94:101	Secretin is a 27-amino acid long peptide hormone that regulates pancreatic water, bicarbonate, enzymes, and potassium ion secretion.
10537138	10	14	theme	mutant	2004:2009	arg1	receptors					2011:2019	the mutant receptors	2000:2019	the mutant receptors	2000:2019	Using an anti-c-Myc monoclonal antibody and confocal microscopy, all of the mutant receptors were found to be expressed and delivered to the plasma membrane.
10537138	0	15	theme	N-linked	8:15	arg1	glycosylation					17:29	N-linked glycosylation	8:29	N-linked glycosylation	8:29	Role of N-linked glycosylation on the function and expression of the human secretin receptor.
10537138	1	16	theme	peptide	127:133	arg1	hormone					135:141	a 27-amino acid long peptide hormone	106:141	a 27-amino acid long peptide hormone that regulates pancreatic water, bicarbonate, enzymes, and potassium ion secretion	106:224	Secretin is a 27-amino acid long peptide hormone that regulates pancreatic water, bicarbonate, enzymes, and potassium ion secretion.
10537138	1	16	theme	peptide	127:133	arg1	Secretin					94:101	Secretin	94:101	Secretin	94:101	Secretin is a 27-amino acid long peptide hormone that regulates pancreatic water, bicarbonate, enzymes, and potassium ion secretion.
10537138	7	17	theme	ED50	1452:1455	arg1	values					1457:1462	the ED50 values	1448:1462	the ED50 values in both assays	1448:1477	However, the Asn72Leu and Ser74Ala mutations reduced the maximal responses and increased the ED50 values in both assays, suggesting that this site is a true glycosylation signal.
10537138	4	18	theme	hSR	929:931	arg1	expression					896:905	the expression	892:905	the expression of a fully functional hSR	892:931	On the other hand, the effects of other inhibitors, swainsonine and deoxymannojirimycin, were much lower, suggesting that the high mannose-type carbohydrate side-chain is essential to the expression of a fully functional hSR.
10537138	9	19	theme	cell	1824:1827	arg1	surface					1829:1835	the cell surface	1820:1835	the cell surface	1820:1835	To evaluate whether the change in receptor function of the mutants is caused by the change in the process of presenting the receptor to the cell surface, the mutants and the wild-type receptor were tagged with a c-Myc epitope at the C-termini.
10537138	2	20	theme	second	449:454	arg1	Asn291					441:446	Asn291	441:446	Asn291	441:446	The human secretin receptor (hSR) is a glycoprotein consisting of 440 amino acids, of which there are 5 putative N-linked glycosylation sites at positions Asn72, Asn100, Asn106, Asn128 (N-terminal ectodomain), and Asn291 (second exoloop).
10537138	2	20	theme	second	449:454	arg1	exoloop					456:462	second exoloop	449:462	second exoloop	449:462	The human secretin receptor (hSR) is a glycoprotein consisting of 440 amino acids, of which there are 5 putative N-linked glycosylation sites at positions Asn72, Asn100, Asn106, Asn128 (N-terminal ectodomain), and Asn291 (second exoloop).
10537138	0	21	from	Role	0:3	arg1	expression					51:60	expression	51:60	expression	51:60	Role of N-linked glycosylation on the function and expression of the human secretin receptor.
10537138	0	21	from	Role	0:3	arg1	function					38:45	function	38:45	function	38:45	Role of N-linked glycosylation on the function and expression of the human secretin receptor.
10537138	2	22	gly	glycosylation	349:361	arg2	sites					363:367	5 putative N-linked glycosylation sites	329:367	5 putative N-linked glycosylation sites	329:367	The human secretin receptor (hSR) is a glycoprotein consisting of 440 amino acids, of which there are 5 putative N-linked glycosylation sites at positions Asn72, Asn100, Asn106, Asn128 (N-terminal ectodomain), and Asn291 (second exoloop).
10537138	2	22	gly	glycosylation	349:361	arg2	5					329:329	5	329:329	5	329:329	The human secretin receptor (hSR) is a glycoprotein consisting of 440 amino acids, of which there are 5 putative N-linked glycosylation sites at positions Asn72, Asn100, Asn106, Asn128 (N-terminal ectodomain), and Asn291 (second exoloop).
10537138	0	23	theme	secretin	75:82	arg1	receptor					84:91	the human secretin receptor	65:91	the human secretin receptor	65:91	Role of N-linked glycosylation on the function and expression of the human secretin receptor.
10537138	2	24	theme	N-linked	340:347	arg1	sites					363:367	5 putative N-linked glycosylation sites	329:367	5 putative N-linked glycosylation sites	329:367	The human secretin receptor (hSR) is a glycoprotein consisting of 440 amino acids, of which there are 5 putative N-linked glycosylation sites at positions Asn72, Asn100, Asn106, Asn128 (N-terminal ectodomain), and Asn291 (second exoloop).
10537138	7	25	theme	glycosylation	1516:1528	arg1	signal					1530:1535	a true glycosylation signal	1509:1535	a true glycosylation signal	1509:1535	However, the Asn72Leu and Ser74Ala mutations reduced the maximal responses and increased the ED50 values in both assays, suggesting that this site is a true glycosylation signal.
10537138	7	25	theme	glycosylation	1516:1528	arg1	site					1501:1504	this site	1496:1504	this site	1496:1504	However, the Asn72Leu and Ser74Ala mutations reduced the maximal responses and increased the ED50 values in both assays, suggesting that this site is a true glycosylation signal.
10537138	6	26	theme	ED50	1303:1306	arg1	values					1308:1313	the ED50 values	1299:1313	the ED50 values	1299:1313	The ED50 values of the wild-type receptor in these two assay systems were 0.25 and 0.11 nM, respectively, and mutation at position 100, 106, or 291 did not affect either the ED50 values or the maximal responses in the two assays.
10537138	5	27	theme	acidification	1109:1121	arg1	rate					1123:1126	extracellular acidification rate	1095:1126	extracellular acidification rate	1095:1126	The role of individual N-linked glycosylation sites was studied by mutation analysis (Asn to Leu or Ser to Ala) coupled to measurements of cAMP accumulation and extracellular acidification rate.
10537138	4	28	theme	inhibitors	748:757	arg1	effects					731:737	the effects	727:737	the effects of other inhibitors, swainsonine and deoxymannojirimycin,	727:795	On the other hand, the effects of other inhibitors, swainsonine and deoxymannojirimycin, were much lower, suggesting that the high mannose-type carbohydrate side-chain is essential to the expression of a fully functional hSR.
10537138	4	28	theme	inhibitors	748:757	arg1	lower					807:811	lower	807:811	lower	807:811	On the other hand, the effects of other inhibitors, swainsonine and deoxymannojirimycin, were much lower, suggesting that the high mannose-type carbohydrate side-chain is essential to the expression of a fully functional hSR.
10537138	7	29	theme	Ser74Ala	1385:1392	arg1	mutations					1394:1402	the Asn72Leu and Ser74Ala mutations	1368:1402	the Asn72Leu and Ser74Ala mutations	1368:1402	However, the Asn72Leu and Ser74Ala mutations reduced the maximal responses and increased the ED50 values in both assays, suggesting that this site is a true glycosylation signal.
10537138	5	30	theme	N-linked	957:964	arg1	sites					980:984	individual N-linked glycosylation sites	946:984	individual N-linked glycosylation sites	946:984	The role of individual N-linked glycosylation sites was studied by mutation analysis (Asn to Leu or Ser to Ala) coupled to measurements of cAMP accumulation and extracellular acidification rate.
10537138	3	31	theme	inhibitors	573:582	arg1	presence					539:546	the presence	535:546	the presence of various glycosylation inhibitors	535:582	Through functional analysis of the hSR-transfected cells cultured in the presence of various glycosylation inhibitors, it was found that tunicamycin and castanospermine were able to significantly reduce the secretin-stimulated cAMP response.
10537138	2	32	dep	positions	372:380	arg1	Asn100					389:394	Asn100	389:394	Asn100	389:394	The human secretin receptor (hSR) is a glycoprotein consisting of 440 amino acids, of which there are 5 putative N-linked glycosylation sites at positions Asn72, Asn100, Asn106, Asn128 (N-terminal ectodomain), and Asn291 (second exoloop).
10537138	2	32	dep	positions	372:380	arg1	Asn106					397:402	Asn106	397:402	Asn106	397:402	The human secretin receptor (hSR) is a glycoprotein consisting of 440 amino acids, of which there are 5 putative N-linked glycosylation sites at positions Asn72, Asn100, Asn106, Asn128 (N-terminal ectodomain), and Asn291 (second exoloop).
10537138	5	33	theme	cAMP	1073:1076	arg1	accumulation					1078:1089	cAMP accumulation	1073:1089	cAMP accumulation	1073:1089	The role of individual N-linked glycosylation sites was studied by mutation analysis (Asn to Leu or Ser to Ala) coupled to measurements of cAMP accumulation and extracellular acidification rate.
10537138	7	34	theme	Asn72Leu	1372:1379	arg1	mutations					1394:1402	the Asn72Leu and Ser74Ala mutations	1368:1402	the Asn72Leu and Ser74Ala mutations	1368:1402	However, the Asn72Leu and Ser74Ala mutations reduced the maximal responses and increased the ED50 values in both assays, suggesting that this site is a true glycosylation signal.
10537138	5	35	theme	sites	980:984	arg1	role					938:941	The role	934:941	The role of individual N-linked glycosylation sites	934:984	The role of individual N-linked glycosylation sites was studied by mutation analysis (Asn to Leu or Ser to Ala) coupled to measurements of cAMP accumulation and extracellular acidification rate.
10537138	2	36	link	N-linked	340:347	arg1	sites					363:367	5 putative N-linked glycosylation sites	329:367	5 putative N-linked glycosylation sites	329:367	The human secretin receptor (hSR) is a glycoprotein consisting of 440 amino acids, of which there are 5 putative N-linked glycosylation sites at positions Asn72, Asn100, Asn106, Asn128 (N-terminal ectodomain), and Asn291 (second exoloop).
10537138	0	37	dep	function	38:45	arg1	the					34:36	the	34:36	the	34:36	Role of N-linked glycosylation on the function and expression of the human secretin receptor.
10537138	2	38	gly	glycoprotein	266:277	arg1	receptor					246:253	The human secretin receptor	227:253	The human secretin receptor (hSR)	227:259	The human secretin receptor (hSR) is a glycoprotein consisting of 440 amino acids, of which there are 5 putative N-linked glycosylation sites at positions Asn72, Asn100, Asn106, Asn128 (N-terminal ectodomain), and Asn291 (second exoloop).
10537138	2	38	gly	glycoprotein	266:277	arg1	glycoprotein					266:277	a glycoprotein	264:277	a glycoprotein consisting of 440 amino acids, of which there are 5 putative N-linked glycosylation sites at positions Asn72, Asn100, Asn106, Asn128 (N-terminal ectodomain), and Asn291 (second exoloop)	264:463	The human secretin receptor (hSR) is a glycoprotein consisting of 440 amino acids, of which there are 5 putative N-linked glycosylation sites at positions Asn72, Asn100, Asn106, Asn128 (N-terminal ectodomain), and Asn291 (second exoloop).
10537138	1	39	theme	ion	212:214	arg1	secretion					216:224	potassium ion secretion	202:224	potassium ion secretion	202:224	Secretin is a 27-amino acid long peptide hormone that regulates pancreatic water, bicarbonate, enzymes, and potassium ion secretion.
10537138	9	40	theme	receptor	1718:1725	arg1	function					1727:1734	receptor function	1718:1734	receptor function of the mutants	1718:1749	To evaluate whether the change in receptor function of the mutants is caused by the change in the process of presenting the receptor to the cell surface, the mutants and the wild-type receptor were tagged with a c-Myc epitope at the C-termini.
10537138	6	41	theme	maximal	1322:1328	arg1	responses					1330:1338	the maximal responses	1318:1338	the maximal responses in the two assays	1318:1356	The ED50 values of the wild-type receptor in these two assay systems were 0.25 and 0.11 nM, respectively, and mutation at position 100, 106, or 291 did not affect either the ED50 values or the maximal responses in the two assays.
10537138	9	42	theme	mutants	1743:1749	arg1	function					1727:1734	receptor function	1718:1734	receptor function of the mutants	1718:1749	To evaluate whether the change in receptor function of the mutants is caused by the change in the process of presenting the receptor to the cell surface, the mutants and the wild-type receptor were tagged with a c-Myc epitope at the C-termini.
10537138	6	43	theme	assay	1184:1188	arg1	systems					1190:1196	these two assay systems	1174:1196	these two assay systems	1174:1196	The ED50 values of the wild-type receptor in these two assay systems were 0.25 and 0.11 nM, respectively, and mutation at position 100, 106, or 291 did not affect either the ED50 values or the maximal responses in the two assays.
10537138	4	44	theme	functional	918:927	arg1	hSR					929:931	a fully functional hSR	910:931	a fully functional hSR	910:931	On the other hand, the effects of other inhibitors, swainsonine and deoxymannojirimycin, were much lower, suggesting that the high mannose-type carbohydrate side-chain is essential to the expression of a fully functional hSR.
10537138	3	45	theme	functional	474:483	arg1	analysis					485:492	functional analysis	474:492	functional analysis of the hSR-transfected cells cultured in the presence of various glycosylation inhibitors	474:582	Through functional analysis of the hSR-transfected cells cultured in the presence of various glycosylation inhibitors, it was found that tunicamycin and castanospermine were able to significantly reduce the secretin-stimulated cAMP response.
10537138	8	46	theme	binding	1591:1597	arg1	studies					1599:1605	competitive binding studies	1579:1605	competitive binding studies	1579:1605	This hypothesis was further supported by competitive binding studies, the same mutants were found to be defective in binding with [125I]secretin.
10537138	4	47	theme	carbohydrate	852:863	arg1	side-chain					865:874	the high mannose-type carbohydrate side-chain	830:874	the high mannose-type carbohydrate side-chain	830:874	On the other hand, the effects of other inhibitors, swainsonine and deoxymannojirimycin, were much lower, suggesting that the high mannose-type carbohydrate side-chain is essential to the expression of a fully functional hSR.
10537138	4	47	theme	carbohydrate	852:863	arg1	essential					879:887	essential	879:887	essential	879:887	On the other hand, the effects of other inhibitors, swainsonine and deoxymannojirimycin, were much lower, suggesting that the high mannose-type carbohydrate side-chain is essential to the expression of a fully functional hSR.
10537138	10	48	theme	monoclonal	1948:1957	arg1	antibody					1959:1966	an anti-c-Myc monoclonal antibody	1934:1966	an anti-c-Myc monoclonal antibody	1934:1966	Using an anti-c-Myc monoclonal antibody and confocal microscopy, all of the mutant receptors were found to be expressed and delivered to the plasma membrane.
10537138	3	49	theme	cAMP	693:696	arg1	response					698:705	the secretin-stimulated cAMP response	669:705	the secretin-stimulated cAMP response	669:705	Through functional analysis of the hSR-transfected cells cultured in the presence of various glycosylation inhibitors, it was found that tunicamycin and castanospermine were able to significantly reduce the secretin-stimulated cAMP response.
10537138	6	50	theme	wild-type	1152:1160	arg1	receptor					1162:1169	the wild-type receptor	1148:1169	the wild-type receptor	1148:1169	The ED50 values of the wild-type receptor in these two assay systems were 0.25 and 0.11 nM, respectively, and mutation at position 100, 106, or 291 did not affect either the ED50 values or the maximal responses in the two assays.
10537138	3	51	theme	hSR-transfected	501:515	arg1	cells					517:521	the hSR-transfected cells	497:521	the hSR-transfected cells cultured in the presence of various glycosylation inhibitors	497:582	Through functional analysis of the hSR-transfected cells cultured in the presence of various glycosylation inhibitors, it was found that tunicamycin and castanospermine were able to significantly reduce the secretin-stimulated cAMP response.
10537138	8	52	theme	same	1612:1615	arg1	defective					1642:1650	defective	1642:1650	defective	1642:1650	This hypothesis was further supported by competitive binding studies, the same mutants were found to be defective in binding with [125I]secretin.
10537138	8	52	theme	same	1612:1615	arg1	mutants					1617:1623	the same mutants	1608:1623	the same mutants	1608:1623	This hypothesis was further supported by competitive binding studies, the same mutants were found to be defective in binding with [125I]secretin.
10537138	5	53	link	N-linked	957:964	arg1	sites					980:984	individual N-linked glycosylation sites	946:984	individual N-linked glycosylation sites	946:984	The role of individual N-linked glycosylation sites was studied by mutation analysis (Asn to Leu or Ser to Ala) coupled to measurements of cAMP accumulation and extracellular acidification rate.
10537138	9	54	from	change	1768:1773	arg1	process					1782:1788	the process	1778:1788	the process of presenting the receptor to the cell surface	1778:1835	To evaluate whether the change in receptor function of the mutants is caused by the change in the process of presenting the receptor to the cell surface, the mutants and the wild-type receptor were tagged with a c-Myc epitope at the C-termini.
10537138	2	55	theme	secretin	237:244	arg1	hSR					256:258	hSR	256:258	hSR	256:258	The human secretin receptor (hSR) is a glycoprotein consisting of 440 amino acids, of which there are 5 putative N-linked glycosylation sites at positions Asn72, Asn100, Asn106, Asn128 (N-terminal ectodomain), and Asn291 (second exoloop).
10537138	2	55	theme	secretin	237:244	arg1	receptor					246:253	The human secretin receptor	227:253	The human secretin receptor (hSR)	227:259	The human secretin receptor (hSR) is a glycoprotein consisting of 440 amino acids, of which there are 5 putative N-linked glycosylation sites at positions Asn72, Asn100, Asn106, Asn128 (N-terminal ectodomain), and Asn291 (second exoloop).
10537138	2	55	theme	secretin	237:244	arg1	glycoprotein					266:277	a glycoprotein	264:277	a glycoprotein consisting of 440 amino acids, of which there are 5 putative N-linked glycosylation sites at positions Asn72, Asn100, Asn106, Asn128 (N-terminal ectodomain), and Asn291 (second exoloop)	264:463	The human secretin receptor (hSR) is a glycoprotein consisting of 440 amino acids, of which there are 5 putative N-linked glycosylation sites at positions Asn72, Asn100, Asn106, Asn128 (N-terminal ectodomain), and Asn291 (second exoloop).
10537138	1	56	theme	27-amino	108:115	arg1	hormone					135:141	a 27-amino acid long peptide hormone	106:141	a 27-amino acid long peptide hormone that regulates pancreatic water, bicarbonate, enzymes, and potassium ion secretion	106:224	Secretin is a 27-amino acid long peptide hormone that regulates pancreatic water, bicarbonate, enzymes, and potassium ion secretion.
10537138	1	56	theme	27-amino	108:115	arg1	Secretin					94:101	Secretin	94:101	Secretin	94:101	Secretin is a 27-amino acid long peptide hormone that regulates pancreatic water, bicarbonate, enzymes, and potassium ion secretion.
10537138	4	57	theme	high	834:837	arg1	side-chain					865:874	the high mannose-type carbohydrate side-chain	830:874	the high mannose-type carbohydrate side-chain	830:874	On the other hand, the effects of other inhibitors, swainsonine and deoxymannojirimycin, were much lower, suggesting that the high mannose-type carbohydrate side-chain is essential to the expression of a fully functional hSR.
10537138	4	57	theme	high	834:837	arg1	essential					879:887	essential	879:887	essential	879:887	On the other hand, the effects of other inhibitors, swainsonine and deoxymannojirimycin, were much lower, suggesting that the high mannose-type carbohydrate side-chain is essential to the expression of a fully functional hSR.
10537138	6	58	theme	ED50	1133:1136	arg1	values					1138:1143	The ED50 values	1129:1143	The ED50 values of the wild-type receptor in these two assay systems	1129:1196	The ED50 values of the wild-type receptor in these two assay systems were 0.25 and 0.11 nM, respectively, and mutation at position 100, 106, or 291 did not affect either the ED50 values or the maximal responses in the two assays.
10537138	6	58	theme	ED50	1133:1136	arg1	nM					1217:1218	0.25 and 0.11 nM	1203:1218	0.25 and 0.11 nM	1203:1218	The ED50 values of the wild-type receptor in these two assay systems were 0.25 and 0.11 nM, respectively, and mutation at position 100, 106, or 291 did not affect either the ED50 values or the maximal responses in the two assays.
10537138	5	59	theme	mutation	1001:1008	arg1	analysis					1010:1017	mutation analysis	1001:1017	mutation analysis (Asn to Leu or Ser to Ala) coupled to measurements of cAMP accumulation and extracellular acidification rate	1001:1126	The role of individual N-linked glycosylation sites was studied by mutation analysis (Asn to Leu or Ser to Ala) coupled to measurements of cAMP accumulation and extracellular acidification rate.
10537138	1	60	theme	long	122:125	arg1	hormone					135:141	a 27-amino acid long peptide hormone	106:141	a 27-amino acid long peptide hormone that regulates pancreatic water, bicarbonate, enzymes, and potassium ion secretion	106:224	Secretin is a 27-amino acid long peptide hormone that regulates pancreatic water, bicarbonate, enzymes, and potassium ion secretion.
10537138	1	60	theme	long	122:125	arg1	Secretin					94:101	Secretin	94:101	Secretin	94:101	Secretin is a 27-amino acid long peptide hormone that regulates pancreatic water, bicarbonate, enzymes, and potassium ion secretion.
10537138	2	61	theme	human	231:235	arg1	hSR					256:258	hSR	256:258	hSR	256:258	The human secretin receptor (hSR) is a glycoprotein consisting of 440 amino acids, of which there are 5 putative N-linked glycosylation sites at positions Asn72, Asn100, Asn106, Asn128 (N-terminal ectodomain), and Asn291 (second exoloop).
10537138	2	61	theme	human	231:235	arg1	receptor					246:253	The human secretin receptor	227:253	The human secretin receptor (hSR)	227:259	The human secretin receptor (hSR) is a glycoprotein consisting of 440 amino acids, of which there are 5 putative N-linked glycosylation sites at positions Asn72, Asn100, Asn106, Asn128 (N-terminal ectodomain), and Asn291 (second exoloop).
10537138	2	61	theme	human	231:235	arg1	glycoprotein					266:277	a glycoprotein	264:277	a glycoprotein consisting of 440 amino acids, of which there are 5 putative N-linked glycosylation sites at positions Asn72, Asn100, Asn106, Asn128 (N-terminal ectodomain), and Asn291 (second exoloop)	264:463	The human secretin receptor (hSR) is a glycoprotein consisting of 440 amino acids, of which there are 5 putative N-linked glycosylation sites at positions Asn72, Asn100, Asn106, Asn128 (N-terminal ectodomain), and Asn291 (second exoloop).
10537138	0	62	theme	human	69:73	arg1	receptor					84:91	the human secretin receptor	65:91	the human secretin receptor	65:91	Role of N-linked glycosylation on the function and expression of the human secretin receptor.
10537138	2	63	theme	N-terminal	413:422	arg1	Asn128					405:410	Asn128	405:410	Asn128 (N-terminal ectodomain)	405:434	The human secretin receptor (hSR) is a glycoprotein consisting of 440 amino acids, of which there are 5 putative N-linked glycosylation sites at positions Asn72, Asn100, Asn106, Asn128 (N-terminal ectodomain), and Asn291 (second exoloop).
10537138	2	63	theme	N-terminal	413:422	arg1	ectodomain					424:433	N-terminal ectodomain	413:433	N-terminal ectodomain	413:433	The human secretin receptor (hSR) is a glycoprotein consisting of 440 amino acids, of which there are 5 putative N-linked glycosylation sites at positions Asn72, Asn100, Asn106, Asn128 (N-terminal ectodomain), and Asn291 (second exoloop).
10537138	6	64	from	values	1138:1143	arg1	systems					1190:1196	these two assay systems	1174:1196	these two assay systems	1174:1196	The ED50 values of the wild-type receptor in these two assay systems were 0.25 and 0.11 nM, respectively, and mutation at position 100, 106, or 291 did not affect either the ED50 values or the maximal responses in the two assays.
10537138	0	65	theme	receptor	84:91	arg1	expression					51:60	expression	51:60	expression	51:60	Role of N-linked glycosylation on the function and expression of the human secretin receptor.
10537138	0	65	theme	receptor	84:91	arg1	function					38:45	function	38:45	function	38:45	Role of N-linked glycosylation on the function and expression of the human secretin receptor.
10537138	7	66	theme	maximal	1416:1422	arg1	responses					1424:1432	the maximal responses	1412:1432	the maximal responses	1412:1432	However, the Asn72Leu and Ser74Ala mutations reduced the maximal responses and increased the ED50 values in both assays, suggesting that this site is a true glycosylation signal.
10537138	6	67	from	position	1251:1258	arg1	mutation					1239:1246	mutation	1239:1246	mutation at position 100, 106, or 291	1239:1275	The ED50 values of the wild-type receptor in these two assay systems were 0.25 and 0.11 nM, respectively, and mutation at position 100, 106, or 291 did not affect either the ED50 values or the maximal responses in the two assays.
10537138	4	68	theme	other	715:719	arg1	hand					721:724	the other hand	711:724	the other hand	711:724	On the other hand, the effects of other inhibitors, swainsonine and deoxymannojirimycin, were much lower, suggesting that the high mannose-type carbohydrate side-chain is essential to the expression of a fully functional hSR.
10537138	2	69	theme	putative	331:338	arg1	sites					363:367	5 putative N-linked glycosylation sites	329:367	5 putative N-linked glycosylation sites	329:367	The human secretin receptor (hSR) is a glycoprotein consisting of 440 amino acids, of which there are 5 putative N-linked glycosylation sites at positions Asn72, Asn100, Asn106, Asn128 (N-terminal ectodomain), and Asn291 (second exoloop).
10537138	9	70	theme	wild-type	1858:1866	arg1	receptor					1868:1875	the wild-type receptor	1854:1875	the wild-type receptor	1854:1875	To evaluate whether the change in receptor function of the mutants is caused by the change in the process of presenting the receptor to the cell surface, the mutants and the wild-type receptor were tagged with a c-Myc epitope at the C-termini.
10537138	0	71	theme	glycosylation	17:29	arg1	Role					0:3	Role	0:3	Role of N-linked glycosylation on the function and expression of the human secretin receptor.	0:92	Role of N-linked glycosylation on the function and expression of the human secretin receptor.
10537138	5	72	theme	extracellular	1095:1107	arg1	rate					1123:1126	extracellular acidification rate	1095:1126	extracellular acidification rate	1095:1126	The role of individual N-linked glycosylation sites was studied by mutation analysis (Asn to Leu or Ser to Ala) coupled to measurements of cAMP accumulation and extracellular acidification rate.
10537138	5	73	gly	glycosylation	966:978	arg2	sites					980:984	individual N-linked glycosylation sites	946:984	individual N-linked glycosylation sites	946:984	The role of individual N-linked glycosylation sites was studied by mutation analysis (Asn to Leu or Ser to Ala) coupled to measurements of cAMP accumulation and extracellular acidification rate.
10537138	5	74	theme	rate	1123:1126	arg1	measurements					1057:1068	measurements	1057:1068	measurements of cAMP accumulation and extracellular acidification rate	1057:1126	The role of individual N-linked glycosylation sites was studied by mutation analysis (Asn to Leu or Ser to Ala) coupled to measurements of cAMP accumulation and extracellular acidification rate.
10537138	5	75	theme	individual	946:955	arg1	sites					980:984	individual N-linked glycosylation sites	946:984	individual N-linked glycosylation sites	946:984	The role of individual N-linked glycosylation sites was studied by mutation analysis (Asn to Leu or Ser to Ala) coupled to measurements of cAMP accumulation and extracellular acidification rate.
10537138	7	76	theme	true	1511:1514	arg1	signal					1530:1535	a true glycosylation signal	1509:1535	a true glycosylation signal	1509:1535	However, the Asn72Leu and Ser74Ala mutations reduced the maximal responses and increased the ED50 values in both assays, suggesting that this site is a true glycosylation signal.
10537138	7	76	theme	true	1511:1514	arg1	site					1501:1504	this site	1496:1504	this site	1496:1504	However, the Asn72Leu and Ser74Ala mutations reduced the maximal responses and increased the ED50 values in both assays, suggesting that this site is a true glycosylation signal.
10537138	3	77	theme	glycosylation	559:571	arg1	inhibitors					573:582	various glycosylation inhibitors	551:582	various glycosylation inhibitors	551:582	Through functional analysis of the hSR-transfected cells cultured in the presence of various glycosylation inhibitors, it was found that tunicamycin and castanospermine were able to significantly reduce the secretin-stimulated cAMP response.
10537138	4	78	theme	other	742:746	arg1	inhibitors					748:757	other inhibitors	742:757	other inhibitors	742:757	On the other hand, the effects of other inhibitors, swainsonine and deoxymannojirimycin, were much lower, suggesting that the high mannose-type carbohydrate side-chain is essential to the expression of a fully functional hSR.
10537138	4	78	theme	other	742:746	arg1	deoxymannojirimycin					776:794	deoxymannojirimycin	776:794	deoxymannojirimycin	776:794	On the other hand, the effects of other inhibitors, swainsonine and deoxymannojirimycin, were much lower, suggesting that the high mannose-type carbohydrate side-chain is essential to the expression of a fully functional hSR.
10537138	4	78	theme	other	742:746	arg1	swainsonine					760:770	swainsonine	760:770	swainsonine	760:770	On the other hand, the effects of other inhibitors, swainsonine and deoxymannojirimycin, were much lower, suggesting that the high mannose-type carbohydrate side-chain is essential to the expression of a fully functional hSR.
10537138	2	79	theme	glycosylation	349:361	arg1	sites					363:367	5 putative N-linked glycosylation sites	329:367	5 putative N-linked glycosylation sites	329:367	The human secretin receptor (hSR) is a glycoprotein consisting of 440 amino acids, of which there are 5 putative N-linked glycosylation sites at positions Asn72, Asn100, Asn106, Asn128 (N-terminal ectodomain), and Asn291 (second exoloop).
10537138	9	80	from	C-termini	1917:1925	arg1	epitope					1902:1908	a c-Myc epitope	1894:1908	a c-Myc epitope at the C-termini	1894:1925	To evaluate whether the change in receptor function of the mutants is caused by the change in the process of presenting the receptor to the cell surface, the mutants and the wild-type receptor were tagged with a c-Myc epitope at the C-termini.
10537138	5	81	theme	glycosylation	966:978	arg1	sites					980:984	individual N-linked glycosylation sites	946:984	individual N-linked glycosylation sites	946:984	The role of individual N-linked glycosylation sites was studied by mutation analysis (Asn to Leu or Ser to Ala) coupled to measurements of cAMP accumulation and extracellular acidification rate.
10537138	9	82	theme	c-Myc	1896:1900	arg1	epitope					1902:1908	a c-Myc epitope	1894:1908	a c-Myc epitope at the C-termini	1894:1925	To evaluate whether the change in receptor function of the mutants is caused by the change in the process of presenting the receptor to the cell surface, the mutants and the wild-type receptor were tagged with a c-Myc epitope at the C-termini.
10537138	2	83	theme	amino	297:301	arg1	acids					303:307	440 amino acids	293:307	440 amino acids	293:307	The human secretin receptor (hSR) is a glycoprotein consisting of 440 amino acids, of which there are 5 putative N-linked glycosylation sites at positions Asn72, Asn100, Asn106, Asn128 (N-terminal ectodomain), and Asn291 (second exoloop).
10537138	5	84	theme	accumulation	1078:1089	arg1	measurements					1057:1068	measurements	1057:1068	measurements of cAMP accumulation and extracellular acidification rate	1057:1126	The role of individual N-linked glycosylation sites was studied by mutation analysis (Asn to Leu or Ser to Ala) coupled to measurements of cAMP accumulation and extracellular acidification rate.
10537138	7	85	from	values	1457:1462	arg1	assays					1472:1477	both assays	1467:1477	both assays	1467:1477	However, the Asn72Leu and Ser74Ala mutations reduced the maximal responses and increased the ED50 values in both assays, suggesting that this site is a true glycosylation signal.
10537138	6	86	from	responses	1330:1338	arg1	assays					1351:1356	the two assays	1343:1356	the two assays	1343:1356	The ED50 values of the wild-type receptor in these two assay systems were 0.25 and 0.11 nM, respectively, and mutation at position 100, 106, or 291 did not affect either the ED50 values or the maximal responses in the two assays.
10537138	1	87	theme	potassium	202:210	arg1	secretion					216:224	potassium ion secretion	202:224	potassium ion secretion	202:224	Secretin is a 27-amino acid long peptide hormone that regulates pancreatic water, bicarbonate, enzymes, and potassium ion secretion.
10537138	5	88	dep	analysis	1010:1017	arg1	Asn					1020:1022	Asn	1020:1022	Asn to Leu or Ser to Ala	1020:1043	The role of individual N-linked glycosylation sites was studied by mutation analysis (Asn to Leu or Ser to Ala) coupled to measurements of cAMP accumulation and extracellular acidification rate.
12063277	0	0	theme	potassium	71:79	arg1	channels					81:88	HERG potassium channels	66:88	HERG potassium channels	66:88	Role of glycosylation in cell surface expression and stability of HERG potassium channels.
12063277	4	1	theme	site-directed	477:489	arg1	mutagenesis					491:501	site-directed mutagenesis	477:501	site-directed mutagenesis	477:501	In this study, we used the approaches of site-directed mutagenesis and biochemical modification to inhibit N-linked glycosylation and studied the role of glycosylation in the cell surface expression and turnover of HERG channels.
12063277	0	2	theme	HERG	66:69	arg1	channels					81:88	HERG potassium channels	66:88	HERG potassium channels	66:88	Role of glycosylation in cell surface expression and stability of HERG potassium channels.
12063277	4	3	theme	biochemical	507:517	arg1	modification					519:530	biochemical modification	507:530	biochemical modification	507:530	In this study, we used the approaches of site-directed mutagenesis and biochemical modification to inhibit N-linked glycosylation and studied the role of glycosylation in the cell surface expression and turnover of HERG channels.
12063277	1	4	theme	pore-forming	147:158	arg1	subunit					160:166	the pore-forming subunit	143:166	the pore-forming subunit of the rapidly activating delayed rectifier potassium channel in the heart	143:241	The human ether-à-go-go-related gene (HERG) encodes the pore-forming subunit of the rapidly activating delayed rectifier potassium channel in the heart.
12063277	1	4	theme	pore-forming	147:158	arg1	gene					123:126	human ether-à-go-go-related gene	95:126	The human ether-à-go-go-related gene (HERG)	91:133	The human ether-à-go-go-related gene (HERG) encodes the pore-forming subunit of the rapidly activating delayed rectifier potassium channel in the heart.
12063277	4	5	theme	N-linked	543:550	arg1	glycosylation					552:564	N-linked glycosylation	543:564	N-linked glycosylation	543:564	In this study, we used the approaches of site-directed mutagenesis and biochemical modification to inhibit N-linked glycosylation and studied the role of glycosylation in the cell surface expression and turnover of HERG channels.
12063277	5	6	theme	N-linked	714:721	arg1	glycosylation					723:735	N-linked glycosylation	714:735	N-linked glycosylation	714:735	Our results show that N598 is the only site for N-linked glycosylation and that glycosylation is not required for the cell surface expression of functional HERG channels.
12063277	0	7	from	Role	0:3	arg1	expression					38:47	cell surface expression	25:47	cell surface expression	25:47	Role of glycosylation in cell surface expression and stability of HERG potassium channels.
12063277	0	8	theme	channels	81:88	arg1	Role					0:3	Role	0:3	Role of glycosylation in cell surface expression	0:47	Role of glycosylation in cell surface expression and stability of HERG potassium channels.
12063277	0	8	theme	channels	81:88	arg1	stability					53:61	stability	53:61	stability of HERG potassium channels	53:88	Role of glycosylation in cell surface expression and stability of HERG potassium channels.
12063277	4	9	link	N-linked	543:550	arg1	glycosylation					552:564	N-linked glycosylation	543:564	N-linked glycosylation	543:564	In this study, we used the approaches of site-directed mutagenesis and biochemical modification to inhibit N-linked glycosylation and studied the role of glycosylation in the cell surface expression and turnover of HERG channels.
12063277	5	10	gly	glycosylation	746:758	arg1	cell					784:787	the cell surface expression	780:806	the cell surface expression of functional HERG channels	780:834	Our results show that N598 is the only site for N-linked glycosylation and that glycosylation is not required for the cell surface expression of functional HERG channels.
12063277	5	10	gly	glycosylation	746:758	arg1	channels					827:834	functional HERG channels	811:834	functional HERG channels	811:834	Our results show that N598 is the only site for N-linked glycosylation and that glycosylation is not required for the cell surface expression of functional HERG channels.
12063277	5	10	gly	glycosylation	746:758	arg1	surface					789:795	the cell surface expression	780:806	the cell surface expression of functional HERG channels	780:834	Our results show that N598 is the only site for N-linked glycosylation and that glycosylation is not required for the cell surface expression of functional HERG channels.
12063277	7	11	theme	glycosylated	1114:1125	arg1	form					1127:1130	the glycosylated form	1110:1130	the glycosylated form	1110:1130	Pulse-chase experiments show that the turnover rate of nonglycosylated HERG channel is faster than that of the glycosylated form, suggesting that N-linked glycosylation plays an important role in HERG channel stability.
12063277	2	12	theme	channel	275:281	arg1	protein					283:289	HERG channel protein	270:289	HERG channel protein	270:289	We previously showed that HERG channel protein is modified by N-linked glycosylation.
12063277	4	13	theme	glycosylation	590:602	arg1	role					582:585	the role	578:585	the role of glycosylation in the cell surface expression and turnover of HERG channels	578:663	In this study, we used the approaches of site-directed mutagenesis and biochemical modification to inhibit N-linked glycosylation and studied the role of glycosylation in the cell surface expression and turnover of HERG channels.
12063277	3	14	dep	glycosylation	408:420	arg1	N629					429:432	N629	429:432	N629	429:432	HERG protein sequence contains two extracellular consensus sites for N-linked glycosylation (N598, N629).
12063277	3	14	dep	glycosylation	408:420	arg1	N598					423:426	N598	423:426	N598	423:426	HERG protein sequence contains two extracellular consensus sites for N-linked glycosylation (N598, N629).
12063277	2	15	theme	HERG	270:273	arg1	protein					283:289	HERG channel protein	270:289	HERG channel protein	270:289	We previously showed that HERG channel protein is modified by N-linked glycosylation.
12063277	5	16	theme	only	700:703	arg1	N598					688:691	N598	688:691	N598	688:691	Our results show that N598 is the only site for N-linked glycosylation and that glycosylation is not required for the cell surface expression of functional HERG channels.
12063277	5	16	theme	only	700:703	arg1	site					705:708	the only site	696:708	the only site for N-linked glycosylation	696:735	Our results show that N598 is the only site for N-linked glycosylation and that glycosylation is not required for the cell surface expression of functional HERG channels.
12063277	4	17	from	role	582:585	arg1	turnover					639:646	turnover	639:646	turnover	639:646	In this study, we used the approaches of site-directed mutagenesis and biochemical modification to inhibit N-linked glycosylation and studied the role of glycosylation in the cell surface expression and turnover of HERG channels.
12063277	4	17	from	role	582:585	arg1	expression					624:633	cell surface expression	611:633	cell surface expression	611:633	In this study, we used the approaches of site-directed mutagenesis and biochemical modification to inhibit N-linked glycosylation and studied the role of glycosylation in the cell surface expression and turnover of HERG channels.
12063277	7	18	theme	channel	1079:1085	arg1	faster					1090:1095	faster	1090:1095	faster	1090:1095	Pulse-chase experiments show that the turnover rate of nonglycosylated HERG channel is faster than that of the glycosylated form, suggesting that N-linked glycosylation plays an important role in HERG channel stability.
12063277	7	18	theme	channel	1079:1085	arg1	rate					1050:1053	the turnover rate	1037:1053	the turnover rate of nonglycosylated HERG channel	1037:1085	Pulse-chase experiments show that the turnover rate of nonglycosylated HERG channel is faster than that of the glycosylated form, suggesting that N-linked glycosylation plays an important role in HERG channel stability.
12063277	7	19	theme	N-linked	1149:1156	arg1	glycosylation					1158:1170	N-linked glycosylation	1149:1170	N-linked glycosylation	1149:1170	Pulse-chase experiments show that the turnover rate of nonglycosylated HERG channel is faster than that of the glycosylated form, suggesting that N-linked glycosylation plays an important role in HERG channel stability.
12063277	4	20	theme	channels	656:663	arg1	turnover					639:646	turnover	639:646	turnover	639:646	In this study, we used the approaches of site-directed mutagenesis and biochemical modification to inhibit N-linked glycosylation and studied the role of glycosylation in the cell surface expression and turnover of HERG channels.
12063277	4	20	theme	channels	656:663	arg1	expression					624:633	cell surface expression	611:633	cell surface expression	611:633	In this study, we used the approaches of site-directed mutagenesis and biochemical modification to inhibit N-linked glycosylation and studied the role of glycosylation in the cell surface expression and turnover of HERG channels.
12063277	2	21	mod	modified	294:301	arg3	glycosylation					315:327	N-linked glycosylation	306:327	N-linked glycosylation	306:327	We previously showed that HERG channel protein is modified by N-linked glycosylation.
12063277	2	21	mod	modified	294:301	arg1	protein					283:289	HERG channel protein	270:289	HERG channel protein	270:289	We previously showed that HERG channel protein is modified by N-linked glycosylation.
12063277	2	22	theme	N-linked	306:313	arg1	glycosylation					315:327	N-linked glycosylation	306:327	N-linked glycosylation	306:327	We previously showed that HERG channel protein is modified by N-linked glycosylation.
12063277	7	23	gly	nonglycosylated	1058:1072	arg1	channel					1079:1085	nonglycosylated HERG channel	1058:1085	nonglycosylated HERG channel	1058:1085	Pulse-chase experiments show that the turnover rate of nonglycosylated HERG channel is faster than that of the glycosylated form, suggesting that N-linked glycosylation plays an important role in HERG channel stability.
12063277	3	24	theme	N-linked	399:406	arg1	glycosylation					408:420	N-linked glycosylation	399:420	N-linked glycosylation (N598, N629)	399:433	HERG protein sequence contains two extracellular consensus sites for N-linked glycosylation (N598, N629).
12063277	6	25	theme	trafficking	937:947	arg1	defect					949:954	a protein trafficking defect	927:954	a protein trafficking defect	927:954	In contrast, N629 is not used for glycosylation, but mutation of this site (N629Q) causes a protein trafficking defect, which results in its intracellular retention.
12063277	7	26	theme	nonglycosylated	1058:1072	arg1	channel					1079:1085	nonglycosylated HERG channel	1058:1085	nonglycosylated HERG channel	1058:1085	Pulse-chase experiments show that the turnover rate of nonglycosylated HERG channel is faster than that of the glycosylated form, suggesting that N-linked glycosylation plays an important role in HERG channel stability.
12063277	4	27	gly	glycosylation	590:602	arg1	cell					611:614	cell surface expression	611:633	cell surface expression	611:633	In this study, we used the approaches of site-directed mutagenesis and biochemical modification to inhibit N-linked glycosylation and studied the role of glycosylation in the cell surface expression and turnover of HERG channels.
12063277	4	27	gly	glycosylation	590:602	arg1	surface					616:622	cell surface expression	611:633	cell surface expression	611:633	In this study, we used the approaches of site-directed mutagenesis and biochemical modification to inhibit N-linked glycosylation and studied the role of glycosylation in the cell surface expression and turnover of HERG channels.
12063277	4	27	gly	glycosylation	590:602	arg1	channels					656:663	HERG channels	651:663	HERG channels	651:663	In this study, we used the approaches of site-directed mutagenesis and biochemical modification to inhibit N-linked glycosylation and studied the role of glycosylation in the cell surface expression and turnover of HERG channels.
12063277	7	28	theme	HERG	1074:1077	arg1	channel					1079:1085	nonglycosylated HERG channel	1058:1085	nonglycosylated HERG channel	1058:1085	Pulse-chase experiments show that the turnover rate of nonglycosylated HERG channel is faster than that of the glycosylated form, suggesting that N-linked glycosylation plays an important role in HERG channel stability.
12063277	3	29	theme	consensus	379:387	arg1	sites					389:393	two extracellular consensus sites	361:393	two extracellular consensus sites for N-linked glycosylation (N598, N629)	361:433	HERG protein sequence contains two extracellular consensus sites for N-linked glycosylation (N598, N629).
12063277	6	30	theme	protein	929:935	arg1	defect					949:954	a protein trafficking defect	927:954	a protein trafficking defect	927:954	In contrast, N629 is not used for glycosylation, but mutation of this site (N629Q) causes a protein trafficking defect, which results in its intracellular retention.
12063277	7	31	theme	turnover	1041:1048	arg1	faster					1090:1095	faster	1090:1095	faster	1090:1095	Pulse-chase experiments show that the turnover rate of nonglycosylated HERG channel is faster than that of the glycosylated form, suggesting that N-linked glycosylation plays an important role in HERG channel stability.
12063277	7	31	theme	turnover	1041:1048	arg1	rate					1050:1053	the turnover rate	1037:1053	the turnover rate of nonglycosylated HERG channel	1037:1085	Pulse-chase experiments show that the turnover rate of nonglycosylated HERG channel is faster than that of the glycosylated form, suggesting that N-linked glycosylation plays an important role in HERG channel stability.
12063277	5	32	theme	cell	784:787	arg1	expression					797:806	the cell surface expression	780:806	the cell surface expression of functional HERG channels	780:834	Our results show that N598 is the only site for N-linked glycosylation and that glycosylation is not required for the cell surface expression of functional HERG channels.
12063277	6	33	used	used	862:865	arg2	N629					850:853	N629	850:853	N629	850:853	In contrast, N629 is not used for glycosylation, but mutation of this site (N629Q) causes a protein trafficking defect, which results in its intracellular retention.
12063277	1	34	theme	activating	183:192	arg1	channel					222:228	the rapidly activating delayed rectifier potassium channel	171:228	the rapidly activating delayed rectifier potassium channel in the heart	171:241	The human ether-à-go-go-related gene (HERG) encodes the pore-forming subunit of the rapidly activating delayed rectifier potassium channel in the heart.
12063277	0	35	theme	glycosylation	8:20	arg1	Role					0:3	Role	0:3	Role of glycosylation in cell surface expression	0:47	Role of glycosylation in cell surface expression and stability of HERG potassium channels.
12063277	0	35	theme	glycosylation	8:20	arg1	stability					53:61	stability	53:61	stability of HERG potassium channels	53:88	Role of glycosylation in cell surface expression and stability of HERG potassium channels.
12063277	5	36	link	N-linked	714:721	arg1	glycosylation					723:735	N-linked glycosylation	714:735	N-linked glycosylation	714:735	Our results show that N598 is the only site for N-linked glycosylation and that glycosylation is not required for the cell surface expression of functional HERG channels.
12063277	1	37	theme	human	95:99	arg1	subunit					160:166	the pore-forming subunit	143:166	the pore-forming subunit of the rapidly activating delayed rectifier potassium channel in the heart	143:241	The human ether-à-go-go-related gene (HERG) encodes the pore-forming subunit of the rapidly activating delayed rectifier potassium channel in the heart.
12063277	1	37	theme	human	95:99	arg1	HERG					129:132	HERG	129:132	HERG	129:132	The human ether-à-go-go-related gene (HERG) encodes the pore-forming subunit of the rapidly activating delayed rectifier potassium channel in the heart.
12063277	1	37	theme	human	95:99	arg1	gene					123:126	human ether-à-go-go-related gene	95:126	The human ether-à-go-go-related gene (HERG)	91:133	The human ether-à-go-go-related gene (HERG) encodes the pore-forming subunit of the rapidly activating delayed rectifier potassium channel in the heart.
12063277	1	38	theme	delayed	194:200	arg1	channel					222:228	the rapidly activating delayed rectifier potassium channel	171:228	the rapidly activating delayed rectifier potassium channel in the heart	171:241	The human ether-à-go-go-related gene (HERG) encodes the pore-forming subunit of the rapidly activating delayed rectifier potassium channel in the heart.
12063277	0	39	theme	surface	30:36	arg1	expression					38:47	cell surface expression	25:47	cell surface expression	25:47	Role of glycosylation in cell surface expression and stability of HERG potassium channels.
12063277	4	40	theme	HERG	651:654	arg1	channels					656:663	HERG channels	651:663	HERG channels	651:663	In this study, we used the approaches of site-directed mutagenesis and biochemical modification to inhibit N-linked glycosylation and studied the role of glycosylation in the cell surface expression and turnover of HERG channels.
12063277	1	41	theme	rectifier	202:210	arg1	channel					222:228	the rapidly activating delayed rectifier potassium channel	171:228	the rapidly activating delayed rectifier potassium channel in the heart	171:241	The human ether-à-go-go-related gene (HERG) encodes the pore-forming subunit of the rapidly activating delayed rectifier potassium channel in the heart.
12063277	0	42	theme	cell	25:28	arg1	expression					38:47	cell surface expression	25:47	cell surface expression	25:47	Role of glycosylation in cell surface expression and stability of HERG potassium channels.
12063277	5	43	theme	functional	811:820	arg1	channels					827:834	functional HERG channels	811:834	functional HERG channels	811:834	Our results show that N598 is the only site for N-linked glycosylation and that glycosylation is not required for the cell surface expression of functional HERG channels.
12063277	3	44	contain	contains	352:359	arg2	sites					389:393	two extracellular consensus sites	361:393	two extracellular consensus sites for N-linked glycosylation (N598, N629)	361:433	HERG protein sequence contains two extracellular consensus sites for N-linked glycosylation (N598, N629).
12063277	3	44	contain	contains	352:359	arg1	sequence					343:350	HERG protein sequence	330:350	HERG protein sequence	330:350	HERG protein sequence contains two extracellular consensus sites for N-linked glycosylation (N598, N629).
12063277	1	45	theme	potassium	212:220	arg1	channel					222:228	the rapidly activating delayed rectifier potassium channel	171:228	the rapidly activating delayed rectifier potassium channel in the heart	171:241	The human ether-à-go-go-related gene (HERG) encodes the pore-forming subunit of the rapidly activating delayed rectifier potassium channel in the heart.
12063277	4	46	used	used	454:457	arg2	we					451:452	we	451:452	we	451:452	In this study, we used the approaches of site-directed mutagenesis and biochemical modification to inhibit N-linked glycosylation and studied the role of glycosylation in the cell surface expression and turnover of HERG channels.
12063277	4	47	theme	modification	519:530	arg1	approaches					463:472	the approaches	459:472	the approaches of site-directed mutagenesis and biochemical modification	459:530	In this study, we used the approaches of site-directed mutagenesis and biochemical modification to inhibit N-linked glycosylation and studied the role of glycosylation in the cell surface expression and turnover of HERG channels.
12063277	0	48	from	stability	53:61	arg1	expression					38:47	cell surface expression	25:47	cell surface expression	25:47	Role of glycosylation in cell surface expression and stability of HERG potassium channels.
12063277	0	49	gly	glycosylation	8:20	arg1	surface					30:36	cell surface expression	25:47	cell surface expression	25:47	Role of glycosylation in cell surface expression and stability of HERG potassium channels.
12063277	0	49	gly	glycosylation	8:20	arg1	cell					25:28	cell surface expression	25:47	cell surface expression	25:47	Role of glycosylation in cell surface expression and stability of HERG potassium channels.
12063277	4	50	theme	surface	616:622	arg1	expression					624:633	cell surface expression	611:633	cell surface expression	611:633	In this study, we used the approaches of site-directed mutagenesis and biochemical modification to inhibit N-linked glycosylation and studied the role of glycosylation in the cell surface expression and turnover of HERG channels.
12063277	1	51	theme	ether-à-go-go-related	101:121	arg1	subunit					160:166	the pore-forming subunit	143:166	the pore-forming subunit of the rapidly activating delayed rectifier potassium channel in the heart	143:241	The human ether-à-go-go-related gene (HERG) encodes the pore-forming subunit of the rapidly activating delayed rectifier potassium channel in the heart.
12063277	1	51	theme	ether-à-go-go-related	101:121	arg1	HERG					129:132	HERG	129:132	HERG	129:132	The human ether-à-go-go-related gene (HERG) encodes the pore-forming subunit of the rapidly activating delayed rectifier potassium channel in the heart.
12063277	1	51	theme	ether-à-go-go-related	101:121	arg1	gene					123:126	human ether-à-go-go-related gene	95:126	The human ether-à-go-go-related gene (HERG)	91:133	The human ether-à-go-go-related gene (HERG) encodes the pore-forming subunit of the rapidly activating delayed rectifier potassium channel in the heart.
12063277	5	52	theme	surface	789:795	arg1	expression					797:806	the cell surface expression	780:806	the cell surface expression of functional HERG channels	780:834	Our results show that N598 is the only site for N-linked glycosylation and that glycosylation is not required for the cell surface expression of functional HERG channels.
12063277	2	53	link	N-linked	306:313	arg1	glycosylation					315:327	N-linked glycosylation	306:327	N-linked glycosylation	306:327	We previously showed that HERG channel protein is modified by N-linked glycosylation.
12063277	1	54	from	heart	237:241	arg1	subunit					160:166	the pore-forming subunit	143:166	the pore-forming subunit of the rapidly activating delayed rectifier potassium channel in the heart	143:241	The human ether-à-go-go-related gene (HERG) encodes the pore-forming subunit of the rapidly activating delayed rectifier potassium channel in the heart.
12063277	1	54	from	heart	237:241	arg1	gene					123:126	human ether-à-go-go-related gene	95:126	The human ether-à-go-go-related gene (HERG)	91:133	The human ether-à-go-go-related gene (HERG) encodes the pore-forming subunit of the rapidly activating delayed rectifier potassium channel in the heart.
12063277	4	55	dep	expression	624:633	arg1	the					607:609	the	607:609	the	607:609	In this study, we used the approaches of site-directed mutagenesis and biochemical modification to inhibit N-linked glycosylation and studied the role of glycosylation in the cell surface expression and turnover of HERG channels.
12063277	7	56	theme	important	1181:1189	arg1	role					1191:1194	an important role	1178:1194	an important role	1178:1194	Pulse-chase experiments show that the turnover rate of nonglycosylated HERG channel is faster than that of the glycosylated form, suggesting that N-linked glycosylation plays an important role in HERG channel stability.
12063277	7	57	theme	HERG	1199:1202	arg1	stability					1212:1220	HERG channel stability	1199:1220	HERG channel stability	1199:1220	Pulse-chase experiments show that the turnover rate of nonglycosylated HERG channel is faster than that of the glycosylated form, suggesting that N-linked glycosylation plays an important role in HERG channel stability.
12063277	6	58	theme	site	907:910	arg1	mutation					890:897	mutation	890:897	mutation of this site (N629Q)	890:918	In contrast, N629 is not used for glycosylation, but mutation of this site (N629Q) causes a protein trafficking defect, which results in its intracellular retention.
12063277	1	59	from	channel	222:228	arg1	heart					237:241	the heart	233:241	the heart	233:241	The human ether-à-go-go-related gene (HERG) encodes the pore-forming subunit of the rapidly activating delayed rectifier potassium channel in the heart.
12063277	7	60	gly	glycosylated	1114:1125	arg1	form					1127:1130	the glycosylated form	1110:1130	the glycosylated form	1110:1130	Pulse-chase experiments show that the turnover rate of nonglycosylated HERG channel is faster than that of the glycosylated form, suggesting that N-linked glycosylation plays an important role in HERG channel stability.
12063277	1	61	theme	channel	222:228	arg1	subunit					160:166	the pore-forming subunit	143:166	the pore-forming subunit of the rapidly activating delayed rectifier potassium channel in the heart	143:241	The human ether-à-go-go-related gene (HERG) encodes the pore-forming subunit of the rapidly activating delayed rectifier potassium channel in the heart.
12063277	1	61	theme	channel	222:228	arg1	gene					123:126	human ether-à-go-go-related gene	95:126	The human ether-à-go-go-related gene (HERG)	91:133	The human ether-à-go-go-related gene (HERG) encodes the pore-forming subunit of the rapidly activating delayed rectifier potassium channel in the heart.
12063277	7	62	theme	Pulse-chase	1003:1013	arg1	experiments					1015:1025	Pulse-chase experiments	1003:1025	Pulse-chase experiments	1003:1025	Pulse-chase experiments show that the turnover rate of nonglycosylated HERG channel is faster than that of the glycosylated form, suggesting that N-linked glycosylation plays an important role in HERG channel stability.
12063277	5	63	theme	HERG	822:825	arg1	channels					827:834	functional HERG channels	811:834	functional HERG channels	811:834	Our results show that N598 is the only site for N-linked glycosylation and that glycosylation is not required for the cell surface expression of functional HERG channels.
12063277	6	64	theme	intracellular	978:990	arg1	retention					992:1000	its intracellular retention	974:1000	its intracellular retention	974:1000	In contrast, N629 is not used for glycosylation, but mutation of this site (N629Q) causes a protein trafficking defect, which results in its intracellular retention.
12063277	3	65	theme	HERG	330:333	arg1	sequence					343:350	HERG protein sequence	330:350	HERG protein sequence	330:350	HERG protein sequence contains two extracellular consensus sites for N-linked glycosylation (N598, N629).
12063277	7	66	link	N-linked	1149:1156	arg1	glycosylation					1158:1170	N-linked glycosylation	1149:1170	N-linked glycosylation	1149:1170	Pulse-chase experiments show that the turnover rate of nonglycosylated HERG channel is faster than that of the glycosylated form, suggesting that N-linked glycosylation plays an important role in HERG channel stability.
12063277	5	67	theme	channels	827:834	arg1	expression					797:806	the cell surface expression	780:806	the cell surface expression of functional HERG channels	780:834	Our results show that N598 is the only site for N-linked glycosylation and that glycosylation is not required for the cell surface expression of functional HERG channels.
12063277	7	68	theme	channel	1204:1210	arg1	stability					1212:1220	HERG channel stability	1199:1220	HERG channel stability	1199:1220	Pulse-chase experiments show that the turnover rate of nonglycosylated HERG channel is faster than that of the glycosylated form, suggesting that N-linked glycosylation plays an important role in HERG channel stability.
12063277	3	69	theme	protein	335:341	arg1	sequence					343:350	HERG protein sequence	330:350	HERG protein sequence	330:350	HERG protein sequence contains two extracellular consensus sites for N-linked glycosylation (N598, N629).
12063277	4	70	theme	mutagenesis	491:501	arg1	approaches					463:472	the approaches	459:472	the approaches of site-directed mutagenesis and biochemical modification	459:530	In this study, we used the approaches of site-directed mutagenesis and biochemical modification to inhibit N-linked glycosylation and studied the role of glycosylation in the cell surface expression and turnover of HERG channels.
12063277	3	71	link	N-linked	399:406	arg1	glycosylation					408:420	N-linked glycosylation	399:420	N-linked glycosylation (N598, N629)	399:433	HERG protein sequence contains two extracellular consensus sites for N-linked glycosylation (N598, N629).
12063277	1	72	from	subunit	160:166	arg1	heart					237:241	the heart	233:241	the heart	233:241	The human ether-à-go-go-related gene (HERG) encodes the pore-forming subunit of the rapidly activating delayed rectifier potassium channel in the heart.
12063277	4	73	theme	cell	611:614	arg1	expression					624:633	cell surface expression	611:633	cell surface expression	611:633	In this study, we used the approaches of site-directed mutagenesis and biochemical modification to inhibit N-linked glycosylation and studied the role of glycosylation in the cell surface expression and turnover of HERG channels.
12063277	3	74	theme	extracellular	365:377	arg1	sites					389:393	two extracellular consensus sites	361:393	two extracellular consensus sites for N-linked glycosylation (N598, N629)	361:433	HERG protein sequence contains two extracellular consensus sites for N-linked glycosylation (N598, N629).
29470411	11	0	theme	CaV2.1	1454:1459	arg1	channel					1461:1467	the CaV2.1 channel	1450:1467	the CaV2.1 channel	1450:1467	Hypoglycosylation of the α₂δ subunit also participates in the gain-of-function effect by promoting voltage-dependent opening of the CaV2.1 channel.
29470411	11	1	theme	α₂δ	1347:1349	arg1	subunit					1351:1357	the α₂δ subunit	1343:1357	the α₂δ subunit	1343:1357	Hypoglycosylation of the α₂δ subunit also participates in the gain-of-function effect by promoting voltage-dependent opening of the CaV2.1 channel.
29470411	9	2	theme	gain-of-function	1079:1094	arg1	effects					1096:1102	gain-of-function effects	1079:1102	gain-of-function effects on channel gating that mirrored those reported for pathogenic CACNA1A mutations linked to FHM and ataxia	1079:1207	Hypoglycosylation of both CaV2.1 subunits (α1A and α2α) induced gain-of-function effects on channel gating that mirrored those reported for pathogenic CACNA1A mutations linked to FHM and ataxia.
29470411	1	3	theme	channelopathies	254:268	arg1	course					244:249	the course	240:249	the course of channelopathies related to Familial Hemiplegic Migraine (FHM) caused by mutations in CACNA1A (encoding CaV2.1 channel)	240:371	Stroke-like episodes (SLE) occur in phosphomannomutase deficiency (PMM2-CDG), and may complicate the course of channelopathies related to Familial Hemiplegic Migraine (FHM) caused by mutations in CACNA1A (encoding CaV2.1 channel).
29470411	11	4	theme	channel	1461:1467	arg1	opening					1439:1445	voltage-dependent opening	1421:1445	voltage-dependent opening of the CaV2.1 channel	1421:1467	Hypoglycosylation of the α₂δ subunit also participates in the gain-of-function effect by promoting voltage-dependent opening of the CaV2.1 channel.
29470411	0	5	from	Episodes	12:19	arg1	Deficiency					67:76	Phosphomannomutase Deficiency	48:76	Phosphomannomutase Deficiency	48:76	Stroke-Like Episodes and Cerebellar Syndrome in Phosphomannomutase Deficiency (PMM2-CDG): Evidence for Hypoglycosylation-Driven Channelopathy.
29470411	1	6	from	mutations	326:334	arg1	CACNA1A					339:345	CACNA1A	339:345	CACNA1A (encoding CaV2.1 channel)	339:371	Stroke-like episodes (SLE) occur in phosphomannomutase deficiency (PMM2-CDG), and may complicate the course of channelopathies related to Familial Hemiplegic Migraine (FHM) caused by mutations in CACNA1A (encoding CaV2.1 channel).
29470411	3	7	theme	PMM2-CDG	497:504	arg1	patients					506:513	43 PMM2-CDG patients	494:513	43 PMM2-CDG patients	494:513	We analyze clinical variables to detect risk factors for SLE in a series of 43 PMM2-CDG patients.
29470411	1	8	theme	related	270:276	arg1	channelopathies					254:268	channelopathies	254:268	channelopathies related to Familial Hemiplegic Migraine (FHM) caused by mutations in CACNA1A (encoding CaV2.1 channel)	254:371	Stroke-like episodes (SLE) occur in phosphomannomutase deficiency (PMM2-CDG), and may complicate the course of channelopathies related to Familial Hemiplegic Migraine (FHM) caused by mutations in CACNA1A (encoding CaV2.1 channel).
29470411	9	9	theme	pathogenic	1155:1164	arg1	mutations					1174:1182	pathogenic CACNA1A mutations	1155:1182	pathogenic CACNA1A mutations linked to FHM and ataxia	1155:1207	Hypoglycosylation of both CaV2.1 subunits (α1A and α2α) induced gain-of-function effects on channel gating that mirrored those reported for pathogenic CACNA1A mutations linked to FHM and ataxia.
29470411	10	10	theme	N-glycosylation	1221:1235	arg1	site					1237:1240	Unoccupied N-glycosylation site N283	1210:1245	Unoccupied N-glycosylation site N283 at α1A	1210:1252	Unoccupied N-glycosylation site N283 at α1A contributes to a gain-of-function by lessening CaV2.1 inactivation.
29470411	9	11	from	effects	1096:1102	arg1	gating					1115:1120	channel gating	1107:1120	channel gating that mirrored those reported for pathogenic CACNA1A mutations linked to FHM and ataxia	1107:1207	Hypoglycosylation of both CaV2.1 subunits (α1A and α2α) induced gain-of-function effects on channel gating that mirrored those reported for pathogenic CACNA1A mutations linked to FHM and ataxia.
29470411	10	12	theme	CaV2.1	1301:1306	arg1	inactivation					1308:1319	CaV2.1 inactivation	1301:1319	CaV2.1 inactivation	1301:1319	Unoccupied N-glycosylation site N283 at α1A contributes to a gain-of-function by lessening CaV2.1 inactivation.
29470411	1	13	theme	CaV2.1	357:362	arg1	channel					364:370	CaV2.1 channel	357:370	CaV2.1 channel	357:370	Stroke-like episodes (SLE) occur in phosphomannomutase deficiency (PMM2-CDG), and may complicate the course of channelopathies related to Familial Hemiplegic Migraine (FHM) caused by mutations in CACNA1A (encoding CaV2.1 channel).
29470411	9	14	theme	channel	1107:1113	arg1	gating					1115:1120	channel gating	1107:1120	channel gating that mirrored those reported for pathogenic CACNA1A mutations linked to FHM and ataxia	1107:1207	Hypoglycosylation of both CaV2.1 subunits (α1A and α2α) induced gain-of-function effects on channel gating that mirrored those reported for pathogenic CACNA1A mutations linked to FHM and ataxia.
29470411	1	15	theme	Familial	281:288	arg1	FHM					311:313	FHM	311:313	FHM	311:313	Stroke-like episodes (SLE) occur in phosphomannomutase deficiency (PMM2-CDG), and may complicate the course of channelopathies related to Familial Hemiplegic Migraine (FHM) caused by mutations in CACNA1A (encoding CaV2.1 channel).
29470411	1	15	theme	Familial	281:288	arg1	Migraine					301:308	Familial Hemiplegic Migraine	281:308	Familial Hemiplegic Migraine (FHM) caused by mutations in CACNA1A (encoding CaV2.1 channel)	281:371	Stroke-like episodes (SLE) occur in phosphomannomutase deficiency (PMM2-CDG), and may complicate the course of channelopathies related to Familial Hemiplegic Migraine (FHM) caused by mutations in CACNA1A (encoding CaV2.1 channel).
29470411	9	16	dep	subunits	1048:1055	arg1	α2α					1066:1068	α2α	1066:1068	α2α	1066:1068	Hypoglycosylation of both CaV2.1 subunits (α1A and α2α) induced gain-of-function effects on channel gating that mirrored those reported for pathogenic CACNA1A mutations linked to FHM and ataxia.
29470411	9	16	dep	subunits	1048:1055	arg1	α1A					1058:1060	α1A	1058:1060	α1A	1058:1060	Hypoglycosylation of both CaV2.1 subunits (α1A and α2α) induced gain-of-function effects on channel gating that mirrored those reported for pathogenic CACNA1A mutations linked to FHM and ataxia.
29470411	9	17	gly	Hypoglycosylation	1015:1031	arg1	subunits					1048:1055	both CaV2.1 subunits	1036:1055	both CaV2.1 subunits (α1A and α2α)	1036:1069	Hypoglycosylation of both CaV2.1 subunits (α1A and α2α) induced gain-of-function effects on channel gating that mirrored those reported for pathogenic CACNA1A mutations linked to FHM and ataxia.
29470411	3	18	theme	clinical	429:436	arg1	variables					438:446	clinical variables	429:446	clinical variables	429:446	We analyze clinical variables to detect risk factors for SLE in a series of 43 PMM2-CDG patients.
29470411	1	19	theme	phosphomannomutase	179:196	arg1	PMM2-CDG					210:217	PMM2-CDG	210:217	PMM2-CDG	210:217	Stroke-like episodes (SLE) occur in phosphomannomutase deficiency (PMM2-CDG), and may complicate the course of channelopathies related to Familial Hemiplegic Migraine (FHM) caused by mutations in CACNA1A (encoding CaV2.1 channel).
29470411	1	19	theme	phosphomannomutase	179:196	arg1	deficiency					198:207	phosphomannomutase deficiency	179:207	phosphomannomutase deficiency (PMM2-CDG)	179:218	Stroke-like episodes (SLE) occur in phosphomannomutase deficiency (PMM2-CDG), and may complicate the course of channelopathies related to Familial Hemiplegic Migraine (FHM) caused by mutations in CACNA1A (encoding CaV2.1 channel).
29470411	4	20	theme	aberrant	577:584	arg1	N-glycosylation					586:600	aberrant N-glycosylation	577:600	aberrant N-glycosylation	577:600	We explore the hypothesis of abnormal CaV2.1 function due to aberrant N-glycosylation as a potential novel pathomechanism of SLE and ataxia in PMM2-CDG by using whole-cell patch-clamp, N-glycosylation blockade and mutagenesis.
29470411	12	21	theme	PMM2-CDG	1524:1531	arg1	patients					1533:1540	PMM2-CDG patients	1524:1540	PMM2-CDG patients	1524:1540	CaV2.1 hypoglycosylation may cause ataxia and SLEs in PMM2-CDG patients.
29470411	6	22	theme	stroke	800:805	arg1	signs					791:795	no signs	788:795	no signs of stroke	788:805	Neuroimages showed no signs of stroke.
29470411	7	23	theme	negative	866:873	arg1	patients					875:882	SLE positive versus negative patients	846:882	SLE positive versus negative patients' group	846:889	Comparison of characteristics between SLE positive versus negative patients' group showed no differences.
29470411	4	24	theme	ataxia	649:654	arg1	pathomechanism					623:636	a potential novel pathomechanism	605:636	a potential novel pathomechanism of SLE and ataxia in PMM2-CDG	605:666	We explore the hypothesis of abnormal CaV2.1 function due to aberrant N-glycosylation as a potential novel pathomechanism of SLE and ataxia in PMM2-CDG by using whole-cell patch-clamp, N-glycosylation blockade and mutagenesis.
29470411	4	24	theme	ataxia	649:654	arg1	hypothesis					531:540	the hypothesis	527:540	the hypothesis of abnormal CaV2.1 function due to aberrant N-glycosylation	527:600	We explore the hypothesis of abnormal CaV2.1 function due to aberrant N-glycosylation as a potential novel pathomechanism of SLE and ataxia in PMM2-CDG by using whole-cell patch-clamp, N-glycosylation blockade and mutagenesis.
29470411	0	25	from	Syndrome	36:43	arg1	Deficiency					67:76	Phosphomannomutase Deficiency	48:76	Phosphomannomutase Deficiency	48:76	Stroke-Like Episodes and Cerebellar Syndrome in Phosphomannomutase Deficiency (PMM2-CDG): Evidence for Hypoglycosylation-Driven Channelopathy.
29470411	4	26	theme	abnormal	545:552	arg1	function					561:568	abnormal CaV2.1 function	545:568	abnormal CaV2.1 function	545:568	We explore the hypothesis of abnormal CaV2.1 function due to aberrant N-glycosylation as a potential novel pathomechanism of SLE and ataxia in PMM2-CDG by using whole-cell patch-clamp, N-glycosylation blockade and mutagenesis.
29470411	8	27	theme	chronic	924:930	arg1	phenotypes					932:941	Acute and chronic phenotypes	914:941	Acute and chronic phenotypes of patients with PMM2-CDG or CACNA1A channelopathies	914:994	Acute and chronic phenotypes of patients with PMM2-CDG or CACNA1A channelopathies show similarities.
29470411	2	28	theme	underlying	378:387	arg1	pathomechanisms					389:403	The underlying pathomechanisms	374:403	The underlying pathomechanisms	374:403	The underlying pathomechanisms are unknown.
29470411	2	28	theme	underlying	378:387	arg1	unknown					409:415	unknown	409:415	unknown	409:415	The underlying pathomechanisms are unknown.
29470411	0	29	theme	Stroke-Like	0:10	arg1	Episodes					12:19	Stroke-Like Episodes	0:19	Stroke-Like Episodes	0:19	Stroke-Like Episodes and Cerebellar Syndrome in Phosphomannomutase Deficiency (PMM2-CDG): Evidence for Hypoglycosylation-Driven Channelopathy.
29470411	0	29	theme	Stroke-Like	0:10	arg1	PMM2-CDG					79:86	PMM2-CDG	79:86	PMM2-CDG	79:86	Stroke-Like Episodes and Cerebellar Syndrome in Phosphomannomutase Deficiency (PMM2-CDG): Evidence for Hypoglycosylation-Driven Channelopathy.
29470411	1	30	theme	Hemiplegic	290:299	arg1	FHM					311:313	FHM	311:313	FHM	311:313	Stroke-like episodes (SLE) occur in phosphomannomutase deficiency (PMM2-CDG), and may complicate the course of channelopathies related to Familial Hemiplegic Migraine (FHM) caused by mutations in CACNA1A (encoding CaV2.1 channel).
29470411	1	30	theme	Hemiplegic	290:299	arg1	Migraine					301:308	Familial Hemiplegic Migraine	281:308	Familial Hemiplegic Migraine (FHM) caused by mutations in CACNA1A (encoding CaV2.1 channel)	281:371	Stroke-like episodes (SLE) occur in phosphomannomutase deficiency (PMM2-CDG), and may complicate the course of channelopathies related to Familial Hemiplegic Migraine (FHM) caused by mutations in CACNA1A (encoding CaV2.1 channel).
29470411	13	31	theme	new	1619:1621	arg1	possibilities					1635:1647	new therapeutic possibilities	1619:1647	new therapeutic possibilities	1619:1647	Aberrant CaV2.1 N-glycosylation as a novel pathomechanism in PMM2-CDG opens new therapeutic possibilities.
29470411	7	32	theme	positive	850:857	arg1	patients					875:882	SLE positive versus negative patients	846:882	SLE positive versus negative patients' group	846:889	Comparison of characteristics between SLE positive versus negative patients' group showed no differences.
29470411	11	33	theme	subunit	1351:1357	arg1	Hypoglycosylation					1322:1338	Hypoglycosylation	1322:1338	Hypoglycosylation of the α₂δ subunit	1322:1357	Hypoglycosylation of the α₂δ subunit also participates in the gain-of-function effect by promoting voltage-dependent opening of the CaV2.1 channel.
29470411	0	34	theme	Cerebellar	25:34	arg1	Syndrome					36:43	Cerebellar Syndrome	25:43	Cerebellar Syndrome	25:43	Stroke-Like Episodes and Cerebellar Syndrome in Phosphomannomutase Deficiency (PMM2-CDG): Evidence for Hypoglycosylation-Driven Channelopathy.
29470411	7	35	theme	characteristics	822:836	arg1	Comparison					808:817	Comparison	808:817	Comparison of characteristics between SLE positive versus negative patients' group	808:889	Comparison of characteristics between SLE positive versus negative patients' group showed no differences.
29470411	12	36	theme	CaV2.1	1470:1475	arg1	hypoglycosylation					1477:1493	CaV2.1 hypoglycosylation	1470:1493	CaV2.1 hypoglycosylation	1470:1493	CaV2.1 hypoglycosylation may cause ataxia and SLEs in PMM2-CDG patients.
29470411	8	37	theme	Acute	914:918	arg1	phenotypes					932:941	Acute and chronic phenotypes	914:941	Acute and chronic phenotypes of patients with PMM2-CDG or CACNA1A channelopathies	914:994	Acute and chronic phenotypes of patients with PMM2-CDG or CACNA1A channelopathies show similarities.
29470411	4	38	theme	CaV2.1	554:559	arg1	function					561:568	abnormal CaV2.1 function	545:568	abnormal CaV2.1 function	545:568	We explore the hypothesis of abnormal CaV2.1 function due to aberrant N-glycosylation as a potential novel pathomechanism of SLE and ataxia in PMM2-CDG by using whole-cell patch-clamp, N-glycosylation blockade and mutagenesis.
29470411	4	39	theme	function	561:568	arg1	pathomechanism					623:636	a potential novel pathomechanism	605:636	a potential novel pathomechanism of SLE and ataxia in PMM2-CDG	605:666	We explore the hypothesis of abnormal CaV2.1 function due to aberrant N-glycosylation as a potential novel pathomechanism of SLE and ataxia in PMM2-CDG by using whole-cell patch-clamp, N-glycosylation blockade and mutagenesis.
29470411	4	39	theme	function	561:568	arg1	hypothesis					531:540	the hypothesis	527:540	the hypothesis of abnormal CaV2.1 function due to aberrant N-glycosylation	527:600	We explore the hypothesis of abnormal CaV2.1 function due to aberrant N-glycosylation as a potential novel pathomechanism of SLE and ataxia in PMM2-CDG by using whole-cell patch-clamp, N-glycosylation blockade and mutagenesis.
29470411	7	40	theme	SLE	846:848	arg1	patients					875:882	SLE positive versus negative patients	846:882	SLE positive versus negative patients' group	846:889	Comparison of characteristics between SLE positive versus negative patients' group showed no differences.
29470411	11	41	theme	gain-of-function	1384:1399	arg1	effect					1401:1406	the gain-of-function effect	1380:1406	the gain-of-function effect	1380:1406	Hypoglycosylation of the α₂δ subunit also participates in the gain-of-function effect by promoting voltage-dependent opening of the CaV2.1 channel.
29470411	4	42	theme	whole-cell	677:686	arg1	patch-clamp					688:698	whole-cell patch-clamp	677:698	whole-cell patch-clamp	677:698	We explore the hypothesis of abnormal CaV2.1 function due to aberrant N-glycosylation as a potential novel pathomechanism of SLE and ataxia in PMM2-CDG by using whole-cell patch-clamp, N-glycosylation blockade and mutagenesis.
29470411	4	43	theme	N-glycosylation	701:715	arg1	blockade					717:724	N-glycosylation blockade	701:724	N-glycosylation blockade	701:724	We explore the hypothesis of abnormal CaV2.1 function due to aberrant N-glycosylation as a potential novel pathomechanism of SLE and ataxia in PMM2-CDG by using whole-cell patch-clamp, N-glycosylation blockade and mutagenesis.
29470411	4	44	from	pathomechanism	623:636	arg1	PMM2-CDG					659:666	PMM2-CDG	659:666	PMM2-CDG	659:666	We explore the hypothesis of abnormal CaV2.1 function due to aberrant N-glycosylation as a potential novel pathomechanism of SLE and ataxia in PMM2-CDG by using whole-cell patch-clamp, N-glycosylation blockade and mutagenesis.
29470411	3	45	theme	risk	458:461	arg1	factors					463:469	risk factors	458:469	risk factors for SLE	458:477	We analyze clinical variables to detect risk factors for SLE in a series of 43 PMM2-CDG patients.
29470411	9	46	theme	CaV2.1	1041:1046	arg1	subunits					1048:1055	both CaV2.1 subunits	1036:1055	both CaV2.1 subunits (α1A and α2α)	1036:1069	Hypoglycosylation of both CaV2.1 subunits (α1A and α2α) induced gain-of-function effects on channel gating that mirrored those reported for pathogenic CACNA1A mutations linked to FHM and ataxia.
29470411	13	47	theme	therapeutic	1623:1633	arg1	possibilities					1635:1647	new therapeutic possibilities	1619:1647	new therapeutic possibilities	1619:1647	Aberrant CaV2.1 N-glycosylation as a novel pathomechanism in PMM2-CDG opens new therapeutic possibilities.
29470411	8	48	with	patients	946:953	arg1	CACNA1A					972:978	CACNA1A	972:978	CACNA1A	972:978	Acute and chronic phenotypes of patients with PMM2-CDG or CACNA1A channelopathies show similarities.
29470411	8	48	with	patients	946:953	arg1	PMM2-CDG					960:967	PMM2-CDG	960:967	PMM2-CDG	960:967	Acute and chronic phenotypes of patients with PMM2-CDG or CACNA1A channelopathies show similarities.
29470411	8	49	theme	patients	946:953	arg1	phenotypes					932:941	Acute and chronic phenotypes	914:941	Acute and chronic phenotypes of patients with PMM2-CDG or CACNA1A channelopathies	914:994	Acute and chronic phenotypes of patients with PMM2-CDG or CACNA1A channelopathies show similarities.
29470411	4	50	theme	SLE	641:643	arg1	pathomechanism					623:636	a potential novel pathomechanism	605:636	a potential novel pathomechanism of SLE and ataxia in PMM2-CDG	605:666	We explore the hypothesis of abnormal CaV2.1 function due to aberrant N-glycosylation as a potential novel pathomechanism of SLE and ataxia in PMM2-CDG by using whole-cell patch-clamp, N-glycosylation blockade and mutagenesis.
29470411	4	50	theme	SLE	641:643	arg1	hypothesis					531:540	the hypothesis	527:540	the hypothesis of abnormal CaV2.1 function due to aberrant N-glycosylation	527:600	We explore the hypothesis of abnormal CaV2.1 function due to aberrant N-glycosylation as a potential novel pathomechanism of SLE and ataxia in PMM2-CDG by using whole-cell patch-clamp, N-glycosylation blockade and mutagenesis.
29470411	9	51	theme	subunits	1048:1055	arg1	Hypoglycosylation					1015:1031	Hypoglycosylation	1015:1031	Hypoglycosylation of both CaV2.1 subunits (α1A and α2α)	1015:1069	Hypoglycosylation of both CaV2.1 subunits (α1A and α2α) induced gain-of-function effects on channel gating that mirrored those reported for pathogenic CACNA1A mutations linked to FHM and ataxia.
29470411	10	52	from	α1A	1250:1252	arg1	site					1237:1240	Unoccupied N-glycosylation site N283	1210:1245	Unoccupied N-glycosylation site N283 at α1A	1210:1252	Unoccupied N-glycosylation site N283 at α1A contributes to a gain-of-function by lessening CaV2.1 inactivation.
29470411	10	53	theme	Unoccupied	1210:1219	arg1	site					1237:1240	Unoccupied N-glycosylation site N283	1210:1245	Unoccupied N-glycosylation site N283 at α1A	1210:1252	Unoccupied N-glycosylation site N283 at α1A contributes to a gain-of-function by lessening CaV2.1 inactivation.
29470411	0	54	theme	Phosphomannomutase	48:65	arg1	Deficiency					67:76	Phosphomannomutase Deficiency	48:76	Phosphomannomutase Deficiency	48:76	Stroke-Like Episodes and Cerebellar Syndrome in Phosphomannomutase Deficiency (PMM2-CDG): Evidence for Hypoglycosylation-Driven Channelopathy.
29470411	13	55	from	N-glycosylation	1559:1573	arg1	PMM2-CDG					1604:1611	PMM2-CDG	1604:1611	PMM2-CDG	1604:1611	Aberrant CaV2.1 N-glycosylation as a novel pathomechanism in PMM2-CDG opens new therapeutic possibilities.
29470411	1	56	theme	Stroke-like	143:153	arg1	episodes					155:162	Stroke-like episodes	143:162	Stroke-like episodes (SLE)	143:168	Stroke-like episodes (SLE) occur in phosphomannomutase deficiency (PMM2-CDG), and may complicate the course of channelopathies related to Familial Hemiplegic Migraine (FHM) caused by mutations in CACNA1A (encoding CaV2.1 channel).
29470411	1	56	theme	Stroke-like	143:153	arg1	SLE					165:167	SLE	165:167	SLE	165:167	Stroke-like episodes (SLE) occur in phosphomannomutase deficiency (PMM2-CDG), and may complicate the course of channelopathies related to Familial Hemiplegic Migraine (FHM) caused by mutations in CACNA1A (encoding CaV2.1 channel).
29470411	11	57	gly	Hypoglycosylation	1322:1338	arg1	subunit					1351:1357	the α₂δ subunit	1343:1357	the α₂δ subunit	1343:1357	Hypoglycosylation of the α₂δ subunit also participates in the gain-of-function effect by promoting voltage-dependent opening of the CaV2.1 channel.
29470411	13	58	gly	N-glycosylation	1559:1573	arg1	PMM2-CDG					1604:1611	PMM2-CDG	1604:1611	PMM2-CDG	1604:1611	Aberrant CaV2.1 N-glycosylation as a novel pathomechanism in PMM2-CDG opens new therapeutic possibilities.
29470411	9	59	attach	linked	1184:1189	arg1	ataxia					1202:1207	ataxia	1202:1207	ataxia	1202:1207	Hypoglycosylation of both CaV2.1 subunits (α1A and α2α) induced gain-of-function effects on channel gating that mirrored those reported for pathogenic CACNA1A mutations linked to FHM and ataxia.
29470411	9	59	attach	linked	1184:1189	arg1	FHM					1194:1196	FHM	1194:1196	FHM	1194:1196	Hypoglycosylation of both CaV2.1 subunits (α1A and α2α) induced gain-of-function effects on channel gating that mirrored those reported for pathogenic CACNA1A mutations linked to FHM and ataxia.
29470411	9	59	attach	linked	1184:1189	arg2	mutations					1174:1182	pathogenic CACNA1A mutations	1155:1182	pathogenic CACNA1A mutations linked to FHM and ataxia	1155:1207	Hypoglycosylation of both CaV2.1 subunits (α1A and α2α) induced gain-of-function effects on channel gating that mirrored those reported for pathogenic CACNA1A mutations linked to FHM and ataxia.
29470411	13	60	theme	Aberrant	1543:1550	arg1	N-glycosylation					1559:1573	Aberrant CaV2.1 N-glycosylation	1543:1573	Aberrant CaV2.1 N-glycosylation as a novel pathomechanism in PMM2-CDG	1543:1611	Aberrant CaV2.1 N-glycosylation as a novel pathomechanism in PMM2-CDG opens new therapeutic possibilities.
29470411	9	61	theme	CACNA1A	1166:1172	arg1	mutations					1174:1182	pathogenic CACNA1A mutations	1155:1182	pathogenic CACNA1A mutations linked to FHM and ataxia	1155:1207	Hypoglycosylation of both CaV2.1 subunits (α1A and α2α) induced gain-of-function effects on channel gating that mirrored those reported for pathogenic CACNA1A mutations linked to FHM and ataxia.
29470411	13	62	theme	CaV2.1	1552:1557	arg1	N-glycosylation					1559:1573	Aberrant CaV2.1 N-glycosylation	1543:1573	Aberrant CaV2.1 N-glycosylation as a novel pathomechanism in PMM2-CDG	1543:1611	Aberrant CaV2.1 N-glycosylation as a novel pathomechanism in PMM2-CDG opens new therapeutic possibilities.
29470411	13	63	theme	novel	1580:1584	arg1	pathomechanism					1586:1599	a novel pathomechanism	1578:1599	a novel pathomechanism	1578:1599	Aberrant CaV2.1 N-glycosylation as a novel pathomechanism in PMM2-CDG opens new therapeutic possibilities.
29470411	0	64	dep	Episodes	12:19	arg1	Evidence					90:97	Evidence	90:97	Stroke-Like Episodes and Cerebellar Syndrome in Phosphomannomutase Deficiency (PMM2-CDG): Evidence for Hypoglycosylation-Driven Channelopathy.	0:141	Stroke-Like Episodes and Cerebellar Syndrome in Phosphomannomutase Deficiency (PMM2-CDG): Evidence for Hypoglycosylation-Driven Channelopathy.
29470411	3	65	theme	patients	506:513	arg1	series					484:489	a series	482:489	a series of 43 PMM2-CDG patients	482:513	We analyze clinical variables to detect risk factors for SLE in a series of 43 PMM2-CDG patients.
29470411	4	66	theme	novel	617:621	arg1	pathomechanism					623:636	a potential novel pathomechanism	605:636	a potential novel pathomechanism of SLE and ataxia in PMM2-CDG	605:666	We explore the hypothesis of abnormal CaV2.1 function due to aberrant N-glycosylation as a potential novel pathomechanism of SLE and ataxia in PMM2-CDG by using whole-cell patch-clamp, N-glycosylation blockade and mutagenesis.
29470411	4	66	theme	novel	617:621	arg1	hypothesis					531:540	the hypothesis	527:540	the hypothesis of abnormal CaV2.1 function due to aberrant N-glycosylation	527:600	We explore the hypothesis of abnormal CaV2.1 function due to aberrant N-glycosylation as a potential novel pathomechanism of SLE and ataxia in PMM2-CDG by using whole-cell patch-clamp, N-glycosylation blockade and mutagenesis.
29470411	11	67	theme	voltage-dependent	1421:1437	arg1	opening					1439:1445	voltage-dependent opening	1421:1445	voltage-dependent opening of the CaV2.1 channel	1421:1467	Hypoglycosylation of the α₂δ subunit also participates in the gain-of-function effect by promoting voltage-dependent opening of the CaV2.1 channel.
29470411	10	68	gly	N-glycosylation	1221:1235	arg2	α1A					1250:1252	α1A	1250:1252	α1A	1250:1252	Unoccupied N-glycosylation site N283 at α1A contributes to a gain-of-function by lessening CaV2.1 inactivation.
29470411	10	68	gly	N-glycosylation	1221:1235	arg2	N283					1242:1245	N283	1242:1245	N283	1242:1245	Unoccupied N-glycosylation site N283 at α1A contributes to a gain-of-function by lessening CaV2.1 inactivation.
29470411	10	68	gly	N-glycosylation	1221:1235	arg2	site					1237:1240	Unoccupied N-glycosylation site N283	1210:1245	Unoccupied N-glycosylation site N283 at α1A	1210:1252	Unoccupied N-glycosylation site N283 at α1A contributes to a gain-of-function by lessening CaV2.1 inactivation.
29470411	8	69	dep	PMM2-CDG	960:967	arg1	channelopathies					980:994	channelopathies	980:994	channelopathies	980:994	Acute and chronic phenotypes of patients with PMM2-CDG or CACNA1A channelopathies show similarities.
29470411	4	70	theme	potential	607:615	arg1	pathomechanism					623:636	a potential novel pathomechanism	605:636	a potential novel pathomechanism of SLE and ataxia in PMM2-CDG	605:666	We explore the hypothesis of abnormal CaV2.1 function due to aberrant N-glycosylation as a potential novel pathomechanism of SLE and ataxia in PMM2-CDG by using whole-cell patch-clamp, N-glycosylation blockade and mutagenesis.
29470411	4	70	theme	potential	607:615	arg1	hypothesis					531:540	the hypothesis	527:540	the hypothesis of abnormal CaV2.1 function due to aberrant N-glycosylation	527:600	We explore the hypothesis of abnormal CaV2.1 function due to aberrant N-glycosylation as a potential novel pathomechanism of SLE and ataxia in PMM2-CDG by using whole-cell patch-clamp, N-glycosylation blockade and mutagenesis.
23345538	4	0	theme	hybrid	903:908	arg1	spectrometer					940:951	a hybrid linear ion trap-orbitrap mass spectrometer	901:951	a hybrid linear ion trap-orbitrap mass spectrometer	901:951	Glycopeptides were enriched by zwitterionic hydrophilic interaction liquid chromatography resins and were either treated with PNGase F and H2(18)O or directly analyzed using a recently developed workflow combining higher-energy C-trap dissociation (HCD) with electron-transfer dissociation (ETD) for a hybrid linear ion trap-orbitrap mass spectrometer.
23345538	6	1	gly	glycopeptides	1207:1219	arg1	sites					1260:1264	118 glycosylation sites	1242:1264	118 glycosylation sites	1242:1264	Direct glycopeptide analysis via HCD-ETD identified 131 glycopeptides from 59 proteins and 118 glycosylation sites, of which 41 were known, 51 were predicted, and 26 were novel.
23345538	6	1	gly	glycopeptides	1207:1219	arg1	proteins					1229:1236	59 proteins	1226:1236	59 proteins	1226:1236	Direct glycopeptide analysis via HCD-ETD identified 131 glycopeptides from 59 proteins and 118 glycosylation sites, of which 41 were known, 51 were predicted, and 26 were novel.
23345538	6	1	gly	glycopeptides	1207:1219	arg2	glycopeptides					1207:1219	131 glycopeptides	1203:1219	131 glycopeptides	1203:1219	Direct glycopeptide analysis via HCD-ETD identified 131 glycopeptides from 59 proteins and 118 glycosylation sites, of which 41 were known, 51 were predicted, and 26 were novel.
23345538	2	2	theme	serum-free	355:364	arg1	medium					366:371	serum-free medium	355:371	serum-free medium	355:371	In this study, human umbilical vein endothelial cells were kept in serum-free medium before activation by phorbol-12-myristate-13 acetate, a commonly used secretagogue that induces exocytosis of endothelial vesicles.
23345538	1	3	theme	cell	268:271	arg1	communication					273:285	cell communication	268:285	cell communication	268:285	Previous proteomics studies have partially unraveled the complexity of endothelial protein secretion but have not investigated glycosylation, a key modification of secreted and membrane proteins for cell communication.
23345538	4	4	theme	ion	917:919	arg1	spectrometer					940:951	a hybrid linear ion trap-orbitrap mass spectrometer	901:951	a hybrid linear ion trap-orbitrap mass spectrometer	901:951	Glycopeptides were enriched by zwitterionic hydrophilic interaction liquid chromatography resins and were either treated with PNGase F and H2(18)O or directly analyzed using a recently developed workflow combining higher-energy C-trap dissociation (HCD) with electron-transfer dissociation (ETD) for a hybrid linear ion trap-orbitrap mass spectrometer.
23345538	4	5	theme	zwitterionic	632:643	arg1	chromatography					676:689	zwitterionic hydrophilic interaction liquid chromatography	632:689	zwitterionic hydrophilic interaction liquid chromatography resins	632:696	Glycopeptides were enriched by zwitterionic hydrophilic interaction liquid chromatography resins and were either treated with PNGase F and H2(18)O or directly analyzed using a recently developed workflow combining higher-energy C-trap dissociation (HCD) with electron-transfer dissociation (ETD) for a hybrid linear ion trap-orbitrap mass spectrometer.
23345538	6	6	gly	glycosylation	1246:1258	arg2	sites					1260:1264	118 glycosylation sites	1242:1264	118 glycosylation sites	1242:1264	Direct glycopeptide analysis via HCD-ETD identified 131 glycopeptides from 59 proteins and 118 glycosylation sites, of which 41 were known, 51 were predicted, and 26 were novel.
23345538	6	6	gly	glycosylation	1246:1258	arg2	118					1242:1244	118	1242:1244	118	1242:1244	Direct glycopeptide analysis via HCD-ETD identified 131 glycopeptides from 59 proteins and 118 glycosylation sites, of which 41 were known, 51 were predicted, and 26 were novel.
23345538	10	7	theme	secretion	1805:1813	arg1	characterization					1765:1780	the most comprehensive characterization	1742:1780	the most comprehensive characterization of endothelial protein secretion to date	1742:1821	This study represents the most comprehensive characterization of endothelial protein secretion to date and demonstrates the potential of new HCD-ETD workflows for determining the glycosylation status of complex biological samples.
23345538	10	8	theme	endothelial	1785:1795	arg1	secretion					1805:1813	endothelial protein secretion	1785:1813	endothelial protein secretion to date	1785:1821	This study represents the most comprehensive characterization of endothelial protein secretion to date and demonstrates the potential of new HCD-ETD workflows for determining the glycosylation status of complex biological samples.
23345538	9	9	theme	fraction	1710:1717	arg1	analysis					1655:1662	analysis	1655:1662	analysis of the input, the flow-through, and the bound fraction	1655:1717	Validation was performed by means of glycoprotein enrichment and analysis of the input, the flow-through, and the bound fraction.
23345538	9	9	theme	fraction	1710:1717	arg1	enrichment					1640:1649	glycoprotein enrichment	1627:1649	glycoprotein enrichment	1627:1649	Validation was performed by means of glycoprotein enrichment and analysis of the input, the flow-through, and the bound fraction.
23345538	6	10	theme	glycopeptide	1158:1169	arg1	analysis					1171:1178	Direct glycopeptide analysis	1151:1178	Direct glycopeptide analysis via HCD-ETD	1151:1190	Direct glycopeptide analysis via HCD-ETD identified 131 glycopeptides from 59 proteins and 118 glycosylation sites, of which 41 were known, 51 were predicted, and 26 were novel.
23345538	6	11	gly	glycopeptide	1158:1169	arg2	glycopeptide					1158:1169	Direct glycopeptide analysis	1151:1178	Direct glycopeptide analysis via HCD-ETD	1151:1190	Direct glycopeptide analysis via HCD-ETD identified 131 glycopeptides from 59 proteins and 118 glycosylation sites, of which 41 were known, 51 were predicted, and 26 were novel.
23345538	2	12	theme	vein	319:322	arg1	cells					336:340	human umbilical vein endothelial cells	303:340	human umbilical vein endothelial cells	303:340	In this study, human umbilical vein endothelial cells were kept in serum-free medium before activation by phorbol-12-myristate-13 acetate, a commonly used secretagogue that induces exocytosis of endothelial vesicles.
23345538	5	13	gly	deglycosylation	960:974	arg1	presence					997:1004	the presence	993:1004	the presence of H2(18)O	993:1015	After deglycosylation with PNGase F in the presence of H2(18)O, 123 unique peptides displayed (18)O-deamidation of asparagine, corresponding to 86 proteins with a total of 121 glycosylation sites.
23345538	5	14	theme	asparagine	1069:1078	arg1	O-deamidation					1052:1064	(18)O-deamidation	1048:1064	(18)O-deamidation of asparagine	1048:1078	After deglycosylation with PNGase F in the presence of H2(18)O, 123 unique peptides displayed (18)O-deamidation of asparagine, corresponding to 86 proteins with a total of 121 glycosylation sites.
23345538	2	15	theme	human	303:307	arg1	cells					336:340	human umbilical vein endothelial cells	303:340	human umbilical vein endothelial cells	303:340	In this study, human umbilical vein endothelial cells were kept in serum-free medium before activation by phorbol-12-myristate-13 acetate, a commonly used secretagogue that induces exocytosis of endothelial vesicles.
23345538	1	16	theme	key	213:215	arg1	glycosylation					196:208	glycosylation	196:208	glycosylation	196:208	Previous proteomics studies have partially unraveled the complexity of endothelial protein secretion but have not investigated glycosylation, a key modification of secreted and membrane proteins for cell communication.
23345538	1	16	theme	key	213:215	arg1	modification					217:228	a key modification	211:228	a key modification of secreted and membrane proteins for cell communication	211:285	Previous proteomics studies have partially unraveled the complexity of endothelial protein secretion but have not investigated glycosylation, a key modification of secreted and membrane proteins for cell communication.
23345538	8	17	theme	high-intensity	1441:1454	arg1	glycopeptides					1474:1486	predominantly high-intensity, multiply charged glycopeptides	1427:1486	predominantly high-intensity, multiply charged glycopeptides	1427:1486	The former detected predominantly high-intensity, multiply charged glycopeptides, whereas the latter preferentially selected precursors with complex/hybrid glycans for fragmentation.
23345538	6	18	theme	glycosylation	1246:1258	arg1	sites					1260:1264	118 glycosylation sites	1242:1264	118 glycosylation sites	1242:1264	Direct glycopeptide analysis via HCD-ETD identified 131 glycopeptides from 59 proteins and 118 glycosylation sites, of which 41 were known, 51 were predicted, and 26 were novel.
23345538	6	19	from	sites	1260:1264	arg1	glycopeptides					1207:1219	131 glycopeptides	1203:1219	131 glycopeptides	1203:1219	Direct glycopeptide analysis via HCD-ETD identified 131 glycopeptides from 59 proteins and 118 glycosylation sites, of which 41 were known, 51 were predicted, and 26 were novel.
23345538	10	20	theme	new	1857:1859	arg1	workflows					1869:1877	new HCD-ETD workflows	1857:1877	new HCD-ETD workflows	1857:1877	This study represents the most comprehensive characterization of endothelial protein secretion to date and demonstrates the potential of new HCD-ETD workflows for determining the glycosylation status of complex biological samples.
23345538	4	21	theme	mass	935:938	arg1	spectrometer					940:951	a hybrid linear ion trap-orbitrap mass spectrometer	901:951	a hybrid linear ion trap-orbitrap mass spectrometer	901:951	Glycopeptides were enriched by zwitterionic hydrophilic interaction liquid chromatography resins and were either treated with PNGase F and H2(18)O or directly analyzed using a recently developed workflow combining higher-energy C-trap dissociation (HCD) with electron-transfer dissociation (ETD) for a hybrid linear ion trap-orbitrap mass spectrometer.
23345538	8	22	dep	detected	1418:1425	arg1	whereas					1489:1495	whereas	1489:1495	whereas	1489:1495	The former detected predominantly high-intensity, multiply charged glycopeptides, whereas the latter preferentially selected precursors with complex/hybrid glycans for fragmentation.
23345538	6	23	from	proteins	1229:1236	arg1	glycopeptides					1207:1219	131 glycopeptides	1203:1219	131 glycopeptides	1203:1219	Direct glycopeptide analysis via HCD-ETD identified 131 glycopeptides from 59 proteins and 118 glycosylation sites, of which 41 were known, 51 were predicted, and 26 were novel.
23345538	5	24	theme	PNGase	981:986	arg1	F					988:988	PNGase F	981:988	PNGase F	981:988	After deglycosylation with PNGase F in the presence of H2(18)O, 123 unique peptides displayed (18)O-deamidation of asparagine, corresponding to 86 proteins with a total of 121 glycosylation sites.
23345538	4	25	theme	H2	740:741	arg1	O					746:746	H2(18)O	740:746	H2(18)O	740:746	Glycopeptides were enriched by zwitterionic hydrophilic interaction liquid chromatography resins and were either treated with PNGase F and H2(18)O or directly analyzed using a recently developed workflow combining higher-energy C-trap dissociation (HCD) with electron-transfer dissociation (ETD) for a hybrid linear ion trap-orbitrap mass spectrometer.
23345538	5	26	with	proteins	1101:1108	arg1	total					1117:1121	a total	1115:1121	a total of 121 glycosylation sites	1115:1148	After deglycosylation with PNGase F in the presence of H2(18)O, 123 unique peptides displayed (18)O-deamidation of asparagine, corresponding to 86 proteins with a total of 121 glycosylation sites.
23345538	0	27	theme	cells	62:66	arg1	secretome					31:39	the secretome	27:39	the secretome of human endothelial cells	27:66	Glycoproteomic analysis of the secretome of human endothelial cells.
23345538	10	28	theme	workflows	1869:1877	arg1	potential					1844:1852	the potential	1840:1852	the potential of new HCD-ETD workflows for determining the glycosylation status of complex biological samples	1840:1948	This study represents the most comprehensive characterization of endothelial protein secretion to date and demonstrates the potential of new HCD-ETD workflows for determining the glycosylation status of complex biological samples.
23345538	1	29	theme	secretion	160:168	arg1	complexity					126:135	the complexity	122:135	the complexity of endothelial protein secretion	122:168	Previous proteomics studies have partially unraveled the complexity of endothelial protein secretion but have not investigated glycosylation, a key modification of secreted and membrane proteins for cell communication.
23345538	5	30	theme	121	1126:1128	arg1	sites					1144:1148	121 glycosylation sites	1126:1148	121 glycosylation sites	1126:1148	After deglycosylation with PNGase F in the presence of H2(18)O, 123 unique peptides displayed (18)O-deamidation of asparagine, corresponding to 86 proteins with a total of 121 glycosylation sites.
23345538	5	31	theme	H2	1009:1010	arg1	O					1015:1015	H2(18)O	1009:1015	H2(18)O	1009:1015	After deglycosylation with PNGase F in the presence of H2(18)O, 123 unique peptides displayed (18)O-deamidation of asparagine, corresponding to 86 proteins with a total of 121 glycosylation sites.
23345538	1	32	theme	endothelial	140:150	arg1	secretion					160:168	endothelial protein secretion	140:168	endothelial protein secretion	140:168	Previous proteomics studies have partially unraveled the complexity of endothelial protein secretion but have not investigated glycosylation, a key modification of secreted and membrane proteins for cell communication.
23345538	4	33	theme	higher-energy	815:827	arg1	HCD					850:852	HCD	850:852	HCD	850:852	Glycopeptides were enriched by zwitterionic hydrophilic interaction liquid chromatography resins and were either treated with PNGase F and H2(18)O or directly analyzed using a recently developed workflow combining higher-energy C-trap dissociation (HCD) with electron-transfer dissociation (ETD) for a hybrid linear ion trap-orbitrap mass spectrometer.
23345538	4	33	theme	higher-energy	815:827	arg1	dissociation					836:847	higher-energy C-trap dissociation	815:847	higher-energy C-trap dissociation (HCD)	815:853	Glycopeptides were enriched by zwitterionic hydrophilic interaction liquid chromatography resins and were either treated with PNGase F and H2(18)O or directly analyzed using a recently developed workflow combining higher-energy C-trap dissociation (HCD) with electron-transfer dissociation (ETD) for a hybrid linear ion trap-orbitrap mass spectrometer.
23345538	8	34	with	precursors	1532:1541	arg1	glycans					1563:1569	complex/hybrid glycans	1548:1569	complex/hybrid glycans	1548:1569	The former detected predominantly high-intensity, multiply charged glycopeptides, whereas the latter preferentially selected precursors with complex/hybrid glycans for fragmentation.
23345538	1	35	theme	proteomics	78:87	arg1	studies					89:95	Previous proteomics studies	69:95	Previous proteomics studies	69:95	Previous proteomics studies have partially unraveled the complexity of endothelial protein secretion but have not investigated glycosylation, a key modification of secreted and membrane proteins for cell communication.
23345538	2	36	theme	phorbol-12-myristate-13	394:416	arg1	acetate					418:424	phorbol-12-myristate-13 acetate	394:424	phorbol-12-myristate-13 acetate	394:424	In this study, human umbilical vein endothelial cells were kept in serum-free medium before activation by phorbol-12-myristate-13 acetate, a commonly used secretagogue that induces exocytosis of endothelial vesicles.
23345538	2	36	theme	phorbol-12-myristate-13	394:416	arg1	secretagogue					443:454	a commonly used secretagogue	427:454	a commonly used secretagogue that induces exocytosis of endothelial vesicles	427:502	In this study, human umbilical vein endothelial cells were kept in serum-free medium before activation by phorbol-12-myristate-13 acetate, a commonly used secretagogue that induces exocytosis of endothelial vesicles.
23345538	0	37	theme	Glycoproteomic	0:13	arg1	analysis					15:22	Glycoproteomic analysis	0:22	Glycoproteomic analysis of the secretome of human endothelial cells	0:66	Glycoproteomic analysis of the secretome of human endothelial cells.
23345538	5	38	theme	unique	1022:1027	arg1	peptides					1029:1036	123 unique peptides	1018:1036	123 unique peptides	1018:1036	After deglycosylation with PNGase F in the presence of H2(18)O, 123 unique peptides displayed (18)O-deamidation of asparagine, corresponding to 86 proteins with a total of 121 glycosylation sites.
23345538	0	39	theme	secretome	31:39	arg1	analysis					15:22	Glycoproteomic analysis	0:22	Glycoproteomic analysis of the secretome of human endothelial cells	0:66	Glycoproteomic analysis of the secretome of human endothelial cells.
23345538	5	40	theme	sites	1144:1148	arg1	total					1117:1121	a total	1115:1121	a total of 121 glycosylation sites	1115:1148	After deglycosylation with PNGase F in the presence of H2(18)O, 123 unique peptides displayed (18)O-deamidation of asparagine, corresponding to 86 proteins with a total of 121 glycosylation sites.
23345538	2	41	theme	vesicles	495:502	arg1	exocytosis					469:478	exocytosis	469:478	exocytosis of endothelial vesicles	469:502	In this study, human umbilical vein endothelial cells were kept in serum-free medium before activation by phorbol-12-myristate-13 acetate, a commonly used secretagogue that induces exocytosis of endothelial vesicles.
23345538	10	42	theme	glycosylation	1899:1911	arg1	status					1913:1918	the glycosylation status	1895:1918	the glycosylation status of complex biological samples	1895:1948	This study represents the most comprehensive characterization of endothelial protein secretion to date and demonstrates the potential of new HCD-ETD workflows for determining the glycosylation status of complex biological samples.
23345538	0	43	theme	human	44:48	arg1	cells					62:66	human endothelial cells	44:66	human endothelial cells	44:66	Glycoproteomic analysis of the secretome of human endothelial cells.
23345538	1	44	theme	secreted	233:240	arg1	glycosylation					196:208	glycosylation	196:208	glycosylation	196:208	Previous proteomics studies have partially unraveled the complexity of endothelial protein secretion but have not investigated glycosylation, a key modification of secreted and membrane proteins for cell communication.
23345538	1	44	theme	secreted	233:240	arg1	modification					217:228	a key modification	211:228	a key modification of secreted and membrane proteins for cell communication	211:285	Previous proteomics studies have partially unraveled the complexity of endothelial protein secretion but have not investigated glycosylation, a key modification of secreted and membrane proteins for cell communication.
23345538	5	45	theme	O	1015:1015	arg1	presence					997:1004	the presence	993:1004	the presence of H2(18)O	993:1015	After deglycosylation with PNGase F in the presence of H2(18)O, 123 unique peptides displayed (18)O-deamidation of asparagine, corresponding to 86 proteins with a total of 121 glycosylation sites.
23345538	4	46	theme	hydrophilic	645:655	arg1	chromatography					676:689	zwitterionic hydrophilic interaction liquid chromatography	632:689	zwitterionic hydrophilic interaction liquid chromatography resins	632:696	Glycopeptides were enriched by zwitterionic hydrophilic interaction liquid chromatography resins and were either treated with PNGase F and H2(18)O or directly analyzed using a recently developed workflow combining higher-energy C-trap dissociation (HCD) with electron-transfer dissociation (ETD) for a hybrid linear ion trap-orbitrap mass spectrometer.
23345538	10	47	theme	biological	1931:1940	arg1	samples					1942:1948	complex biological samples	1923:1948	complex biological samples	1923:1948	This study represents the most comprehensive characterization of endothelial protein secretion to date and demonstrates the potential of new HCD-ETD workflows for determining the glycosylation status of complex biological samples.
23345538	1	48	theme	membrane	246:253	arg1	proteins					255:262	membrane proteins	246:262	membrane proteins	246:262	Previous proteomics studies have partially unraveled the complexity of endothelial protein secretion but have not investigated glycosylation, a key modification of secreted and membrane proteins for cell communication.
23345538	4	49	theme	liquid	669:674	arg1	chromatography					676:689	zwitterionic hydrophilic interaction liquid chromatography	632:689	zwitterionic hydrophilic interaction liquid chromatography resins	632:696	Glycopeptides were enriched by zwitterionic hydrophilic interaction liquid chromatography resins and were either treated with PNGase F and H2(18)O or directly analyzed using a recently developed workflow combining higher-energy C-trap dissociation (HCD) with electron-transfer dissociation (ETD) for a hybrid linear ion trap-orbitrap mass spectrometer.
23345538	10	50	theme	comprehensive	1751:1763	arg1	characterization					1765:1780	the most comprehensive characterization	1742:1780	the most comprehensive characterization of endothelial protein secretion to date	1742:1821	This study represents the most comprehensive characterization of endothelial protein secretion to date and demonstrates the potential of new HCD-ETD workflows for determining the glycosylation status of complex biological samples.
23345538	9	51	theme	flow-through	1682:1693	arg1	analysis					1655:1662	analysis	1655:1662	analysis of the input, the flow-through, and the bound fraction	1655:1717	Validation was performed by means of glycoprotein enrichment and analysis of the input, the flow-through, and the bound fraction.
23345538	9	51	theme	flow-through	1682:1693	arg1	enrichment					1640:1649	glycoprotein enrichment	1627:1649	glycoprotein enrichment	1627:1649	Validation was performed by means of glycoprotein enrichment and analysis of the input, the flow-through, and the bound fraction.
23345538	4	52	theme	linear	910:915	arg1	spectrometer					940:951	a hybrid linear ion trap-orbitrap mass spectrometer	901:951	a hybrid linear ion trap-orbitrap mass spectrometer	901:951	Glycopeptides were enriched by zwitterionic hydrophilic interaction liquid chromatography resins and were either treated with PNGase F and H2(18)O or directly analyzed using a recently developed workflow combining higher-energy C-trap dissociation (HCD) with electron-transfer dissociation (ETD) for a hybrid linear ion trap-orbitrap mass spectrometer.
23345538	10	53	theme	protein	1797:1803	arg1	secretion					1805:1813	endothelial protein secretion	1785:1813	endothelial protein secretion to date	1785:1821	This study represents the most comprehensive characterization of endothelial protein secretion to date and demonstrates the potential of new HCD-ETD workflows for determining the glycosylation status of complex biological samples.
23345538	9	54	theme	bound	1704:1708	arg1	fraction					1710:1717	the bound fraction	1700:1717	the bound fraction	1700:1717	Validation was performed by means of glycoprotein enrichment and analysis of the input, the flow-through, and the bound fraction.
23345538	5	55	gly	glycosylation	1130:1142	arg2	sites					1144:1148	121 glycosylation sites	1126:1148	121 glycosylation sites	1126:1148	After deglycosylation with PNGase F in the presence of H2(18)O, 123 unique peptides displayed (18)O-deamidation of asparagine, corresponding to 86 proteins with a total of 121 glycosylation sites.
23345538	2	56	theme	endothelial	324:334	arg1	cells					336:340	human umbilical vein endothelial cells	303:340	human umbilical vein endothelial cells	303:340	In this study, human umbilical vein endothelial cells were kept in serum-free medium before activation by phorbol-12-myristate-13 acetate, a commonly used secretagogue that induces exocytosis of endothelial vesicles.
23345538	6	57	theme	Direct	1151:1156	arg1	analysis					1171:1178	Direct glycopeptide analysis	1151:1178	Direct glycopeptide analysis via HCD-ETD	1151:1190	Direct glycopeptide analysis via HCD-ETD identified 131 glycopeptides from 59 proteins and 118 glycosylation sites, of which 41 were known, 51 were predicted, and 26 were novel.
23345538	4	58	theme	PNGase	727:732	arg1	F					734:734	PNGase F	727:734	PNGase F	727:734	Glycopeptides were enriched by zwitterionic hydrophilic interaction liquid chromatography resins and were either treated with PNGase F and H2(18)O or directly analyzed using a recently developed workflow combining higher-energy C-trap dissociation (HCD) with electron-transfer dissociation (ETD) for a hybrid linear ion trap-orbitrap mass spectrometer.
23345538	2	59	theme	umbilical	309:317	arg1	cells					336:340	human umbilical vein endothelial cells	303:340	human umbilical vein endothelial cells	303:340	In this study, human umbilical vein endothelial cells were kept in serum-free medium before activation by phorbol-12-myristate-13 acetate, a commonly used secretagogue that induces exocytosis of endothelial vesicles.
23345538	8	60	gly	glycopeptides	1474:1486	arg2	glycopeptides					1474:1486	predominantly high-intensity, multiply charged glycopeptides	1427:1486	predominantly high-intensity, multiply charged glycopeptides	1427:1486	The former detected predominantly high-intensity, multiply charged glycopeptides, whereas the latter preferentially selected precursors with complex/hybrid glycans for fragmentation.
23345538	7	61	theme	HCD-product-dependent	1380:1400	arg1	ETD					1402:1404	HCD-product-dependent ETD	1380:1404	HCD-product-dependent ETD	1380:1404	Two methods were compared: alternating HCD-ETD and HCD-product-dependent ETD.
23345538	10	62	theme	HCD-ETD	1861:1867	arg1	workflows					1869:1877	new HCD-ETD workflows	1857:1877	new HCD-ETD workflows	1857:1877	This study represents the most comprehensive characterization of endothelial protein secretion to date and demonstrates the potential of new HCD-ETD workflows for determining the glycosylation status of complex biological samples.
23345538	10	63	gly	glycosylation	1899:1911	arg1	samples					1942:1948	complex biological samples	1923:1948	complex biological samples	1923:1948	This study represents the most comprehensive characterization of endothelial protein secretion to date and demonstrates the potential of new HCD-ETD workflows for determining the glycosylation status of complex biological samples.
23345538	4	64	theme	trap-orbitrap	921:933	arg1	spectrometer					940:951	a hybrid linear ion trap-orbitrap mass spectrometer	901:951	a hybrid linear ion trap-orbitrap mass spectrometer	901:951	Glycopeptides were enriched by zwitterionic hydrophilic interaction liquid chromatography resins and were either treated with PNGase F and H2(18)O or directly analyzed using a recently developed workflow combining higher-energy C-trap dissociation (HCD) with electron-transfer dissociation (ETD) for a hybrid linear ion trap-orbitrap mass spectrometer.
23345538	3	65	theme	membrane	582:589	arg1	proteins					591:598	membrane proteins	582:598	membrane proteins	582:598	In addition to 123 secreted proteins, the secretome was particularly rich in membrane proteins.
23345538	1	66	theme	protein	152:158	arg1	secretion					160:168	endothelial protein secretion	140:168	endothelial protein secretion	140:168	Previous proteomics studies have partially unraveled the complexity of endothelial protein secretion but have not investigated glycosylation, a key modification of secreted and membrane proteins for cell communication.
23345538	3	67	from	rich	574:577	arg1	proteins					591:598	membrane proteins	582:598	membrane proteins	582:598	In addition to 123 secreted proteins, the secretome was particularly rich in membrane proteins.
23345538	5	68	theme	glycosylation	1130:1142	arg1	sites					1144:1148	121 glycosylation sites	1126:1148	121 glycosylation sites	1126:1148	After deglycosylation with PNGase F in the presence of H2(18)O, 123 unique peptides displayed (18)O-deamidation of asparagine, corresponding to 86 proteins with a total of 121 glycosylation sites.
23345538	8	69	theme	complex/hybrid	1548:1561	arg1	glycans					1563:1569	complex/hybrid glycans	1548:1569	complex/hybrid glycans	1548:1569	The former detected predominantly high-intensity, multiply charged glycopeptides, whereas the latter preferentially selected precursors with complex/hybrid glycans for fragmentation.
23345538	4	70	theme	developed	786:794	arg1	workflow					796:803	a recently developed workflow	775:803	a recently developed workflow combining higher-energy C-trap dissociation (HCD) with electron-transfer dissociation (ETD) for a hybrid linear ion trap-orbitrap mass spectrometer	775:951	Glycopeptides were enriched by zwitterionic hydrophilic interaction liquid chromatography resins and were either treated with PNGase F and H2(18)O or directly analyzed using a recently developed workflow combining higher-energy C-trap dissociation (HCD) with electron-transfer dissociation (ETD) for a hybrid linear ion trap-orbitrap mass spectrometer.
23345538	1	71	theme	Previous	69:76	arg1	studies					89:95	Previous proteomics studies	69:95	Previous proteomics studies	69:95	Previous proteomics studies have partially unraveled the complexity of endothelial protein secretion but have not investigated glycosylation, a key modification of secreted and membrane proteins for cell communication.
23345538	9	72	gly	glycoprotein	1627:1638	arg1	glycoprotein					1627:1638	glycoprotein enrichment	1627:1649	glycoprotein enrichment	1627:1649	Validation was performed by means of glycoprotein enrichment and analysis of the input, the flow-through, and the bound fraction.
23345538	5	73	with	deglycosylation	960:974	arg1	F					988:988	PNGase F	981:988	PNGase F	981:988	After deglycosylation with PNGase F in the presence of H2(18)O, 123 unique peptides displayed (18)O-deamidation of asparagine, corresponding to 86 proteins with a total of 121 glycosylation sites.
23345538	3	74	from	proteins	591:598	arg1	rich					574:577	rich	574:577	rich	574:577	In addition to 123 secreted proteins, the secretome was particularly rich in membrane proteins.
23345538	3	74	from	proteins	591:598	arg1	secretome					547:555	the secretome	543:555	the secretome	543:555	In addition to 123 secreted proteins, the secretome was particularly rich in membrane proteins.
23345538	5	75	from	deglycosylation	960:974	arg1	presence					997:1004	the presence	993:1004	the presence of H2(18)O	993:1015	After deglycosylation with PNGase F in the presence of H2(18)O, 123 unique peptides displayed (18)O-deamidation of asparagine, corresponding to 86 proteins with a total of 121 glycosylation sites.
23345538	10	76	theme	complex	1923:1929	arg1	samples					1942:1948	complex biological samples	1923:1948	complex biological samples	1923:1948	This study represents the most comprehensive characterization of endothelial protein secretion to date and demonstrates the potential of new HCD-ETD workflows for determining the glycosylation status of complex biological samples.
23345538	2	77	theme	used	438:441	arg1	acetate					418:424	phorbol-12-myristate-13 acetate	394:424	phorbol-12-myristate-13 acetate	394:424	In this study, human umbilical vein endothelial cells were kept in serum-free medium before activation by phorbol-12-myristate-13 acetate, a commonly used secretagogue that induces exocytosis of endothelial vesicles.
23345538	2	77	theme	used	438:441	arg1	secretagogue					443:454	a commonly used secretagogue	427:454	a commonly used secretagogue that induces exocytosis of endothelial vesicles	427:502	In this study, human umbilical vein endothelial cells were kept in serum-free medium before activation by phorbol-12-myristate-13 acetate, a commonly used secretagogue that induces exocytosis of endothelial vesicles.
23345538	9	78	theme	glycoprotein	1627:1638	arg1	enrichment					1640:1649	glycoprotein enrichment	1627:1649	glycoprotein enrichment	1627:1649	Validation was performed by means of glycoprotein enrichment and analysis of the input, the flow-through, and the bound fraction.
23345538	0	79	theme	endothelial	50:60	arg1	cells					62:66	human endothelial cells	44:66	human endothelial cells	44:66	Glycoproteomic analysis of the secretome of human endothelial cells.
23345538	2	80	theme	endothelial	483:493	arg1	vesicles					495:502	endothelial vesicles	483:502	endothelial vesicles	483:502	In this study, human umbilical vein endothelial cells were kept in serum-free medium before activation by phorbol-12-myristate-13 acetate, a commonly used secretagogue that induces exocytosis of endothelial vesicles.
23345538	4	81	theme	electron-transfer	860:876	arg1	ETD					892:894	ETD	892:894	ETD	892:894	Glycopeptides were enriched by zwitterionic hydrophilic interaction liquid chromatography resins and were either treated with PNGase F and H2(18)O or directly analyzed using a recently developed workflow combining higher-energy C-trap dissociation (HCD) with electron-transfer dissociation (ETD) for a hybrid linear ion trap-orbitrap mass spectrometer.
23345538	4	81	theme	electron-transfer	860:876	arg1	dissociation					878:889	electron-transfer dissociation	860:889	electron-transfer dissociation (ETD) for a hybrid linear ion trap-orbitrap mass spectrometer	860:951	Glycopeptides were enriched by zwitterionic hydrophilic interaction liquid chromatography resins and were either treated with PNGase F and H2(18)O or directly analyzed using a recently developed workflow combining higher-energy C-trap dissociation (HCD) with electron-transfer dissociation (ETD) for a hybrid linear ion trap-orbitrap mass spectrometer.
23345538	3	82	theme	secreted	524:531	arg1	proteins					533:540	123 secreted proteins	520:540	123 secreted proteins	520:540	In addition to 123 secreted proteins, the secretome was particularly rich in membrane proteins.
23345538	8	83	dep	high-intensity	1441:1454	arg1	charged					1466:1472	charged	1466:1472	charged	1466:1472	The former detected predominantly high-intensity, multiply charged glycopeptides, whereas the latter preferentially selected precursors with complex/hybrid glycans for fragmentation.
23345538	4	84	theme	interaction	657:667	arg1	chromatography					676:689	zwitterionic hydrophilic interaction liquid chromatography	632:689	zwitterionic hydrophilic interaction liquid chromatography resins	632:696	Glycopeptides were enriched by zwitterionic hydrophilic interaction liquid chromatography resins and were either treated with PNGase F and H2(18)O or directly analyzed using a recently developed workflow combining higher-energy C-trap dissociation (HCD) with electron-transfer dissociation (ETD) for a hybrid linear ion trap-orbitrap mass spectrometer.
23345538	10	85	theme	samples	1942:1948	arg1	status					1913:1918	the glycosylation status	1895:1918	the glycosylation status of complex biological samples	1895:1948	This study represents the most comprehensive characterization of endothelial protein secretion to date and demonstrates the potential of new HCD-ETD workflows for determining the glycosylation status of complex biological samples.
23345538	4	86	theme	C-trap	829:834	arg1	HCD					850:852	HCD	850:852	HCD	850:852	Glycopeptides were enriched by zwitterionic hydrophilic interaction liquid chromatography resins and were either treated with PNGase F and H2(18)O or directly analyzed using a recently developed workflow combining higher-energy C-trap dissociation (HCD) with electron-transfer dissociation (ETD) for a hybrid linear ion trap-orbitrap mass spectrometer.
23345538	4	86	theme	C-trap	829:834	arg1	dissociation					836:847	higher-energy C-trap dissociation	815:847	higher-energy C-trap dissociation (HCD)	815:853	Glycopeptides were enriched by zwitterionic hydrophilic interaction liquid chromatography resins and were either treated with PNGase F and H2(18)O or directly analyzed using a recently developed workflow combining higher-energy C-trap dissociation (HCD) with electron-transfer dissociation (ETD) for a hybrid linear ion trap-orbitrap mass spectrometer.
23345538	9	87	theme	input	1671:1675	arg1	analysis					1655:1662	analysis	1655:1662	analysis of the input, the flow-through, and the bound fraction	1655:1717	Validation was performed by means of glycoprotein enrichment and analysis of the input, the flow-through, and the bound fraction.
23345538	9	87	theme	input	1671:1675	arg1	enrichment					1640:1649	glycoprotein enrichment	1627:1649	glycoprotein enrichment	1627:1649	Validation was performed by means of glycoprotein enrichment and analysis of the input, the flow-through, and the bound fraction.
23345538	4	88	theme	chromatography	676:689	arg1	resins					691:696	zwitterionic hydrophilic interaction liquid chromatography resins	632:696	zwitterionic hydrophilic interaction liquid chromatography resins	632:696	Glycopeptides were enriched by zwitterionic hydrophilic interaction liquid chromatography resins and were either treated with PNGase F and H2(18)O or directly analyzed using a recently developed workflow combining higher-energy C-trap dissociation (HCD) with electron-transfer dissociation (ETD) for a hybrid linear ion trap-orbitrap mass spectrometer.
23345538	1	89	theme	proteins	255:262	arg1	glycosylation					196:208	glycosylation	196:208	glycosylation	196:208	Previous proteomics studies have partially unraveled the complexity of endothelial protein secretion but have not investigated glycosylation, a key modification of secreted and membrane proteins for cell communication.
23345538	1	89	theme	proteins	255:262	arg1	modification					217:228	a key modification	211:228	a key modification of secreted and membrane proteins for cell communication	211:285	Previous proteomics studies have partially unraveled the complexity of endothelial protein secretion but have not investigated glycosylation, a key modification of secreted and membrane proteins for cell communication.
14977046	0	0	theme	optimal	75:81	arg1	expression					96:105	optimal cell-surface expression	75:105	optimal cell-surface expression	75:105	N-linked glycosylation of the human bradykinin B2 receptor is required for optimal cell-surface expression and coupling.
14977046	1	1	theme	glycosylation	340:352	arg1	sites					354:358	the three potential N-linked glycosylation sites	311:358	the three potential N-linked glycosylation sites	311:358	To investigate the glycosylation of the human bradykinin B2 receptor and the functional significance of this modification, we studied receptors mutated at single or multiple combinations of the three potential N-linked glycosylation sites, asparagines N3, N12 and N180, in COS-7, HEK 293 and CHO-K1 cells.
14977046	1	1	theme	glycosylation	340:352	arg1	asparagines					361:371	asparagines N3, N12 and N180	361:388	asparagines N3, N12 and N180	361:388	To investigate the glycosylation of the human bradykinin B2 receptor and the functional significance of this modification, we studied receptors mutated at single or multiple combinations of the three potential N-linked glycosylation sites, asparagines N3, N12 and N180, in COS-7, HEK 293 and CHO-K1 cells.
14977046	5	2	theme	B2	929:930	arg1	receptor					932:939	the human bradykinin B2 receptor	908:939	the human bradykinin B2 receptor	908:939	These results indicate that, for the human bradykinin B2 receptor, glycosylation is not required for optimal ligand binding, but plays an important role in cell-surface addressing and receptor function.
14977046	1	3	theme	sites	354:358	arg1	combinations					295:306	single or multiple combinations	276:306	single or multiple combinations of the three potential N-linked glycosylation sites, asparagines N3, N12 and N180, in COS-7, HEK 293 and CHO-K1 cells	276:424	To investigate the glycosylation of the human bradykinin B2 receptor and the functional significance of this modification, we studied receptors mutated at single or multiple combinations of the three potential N-linked glycosylation sites, asparagines N3, N12 and N180, in COS-7, HEK 293 and CHO-K1 cells.
14977046	1	4	theme	human	161:165	arg1	receptor					181:188	the human bradykinin B2 receptor	157:188	the human bradykinin B2 receptor	157:188	To investigate the glycosylation of the human bradykinin B2 receptor and the functional significance of this modification, we studied receptors mutated at single or multiple combinations of the three potential N-linked glycosylation sites, asparagines N3, N12 and N180, in COS-7, HEK 293 and CHO-K1 cells.
14977046	4	5	theme	non-glycosylated	751:766	arg1	receptor					768:775	the non-glycosylated receptor	747:775	the non-glycosylated receptor	747:775	However, the glycosylated receptors were expressed at the cell-surface to a much greater extent than the non-glycosylated receptor and coupling to phospholipase C was less efficient for receptor lacking N-terminal glycosylation.
14977046	4	5	theme	non-glycosylated	751:766	arg1	efficient					818:826	efficient	818:826	efficient	818:826	However, the glycosylated receptors were expressed at the cell-surface to a much greater extent than the non-glycosylated receptor and coupling to phospholipase C was less efficient for receptor lacking N-terminal glycosylation.
14977046	1	6	theme	CHO-K1	413:418	arg1	cells					420:424	COS-7, HEK 293 and CHO-K1 cells	394:424	cells	420:424	To investigate the glycosylation of the human bradykinin B2 receptor and the functional significance of this modification, we studied receptors mutated at single or multiple combinations of the three potential N-linked glycosylation sites, asparagines N3, N12 and N180, in COS-7, HEK 293 and CHO-K1 cells.
14977046	2	7	gly	glycosylated	510:521	arg1	asparagines					494:504	all three extracellular asparagines	470:504	all three extracellular asparagines	470:504	Western blot experiments demonstrated that all three extracellular asparagines are glycosylated.
14977046	0	8	theme	cell-surface	83:94	arg1	expression					96:105	optimal cell-surface expression	75:105	optimal cell-surface expression	75:105	N-linked glycosylation of the human bradykinin B2 receptor is required for optimal cell-surface expression and coupling.
14977046	3	9	theme	bradykinin	540:549	arg1	binding					551:557	bradykinin binding	540:557	bradykinin binding	540:557	The kinetics of bradykinin binding and receptor sequestration remained unchanged after glycosylation had been suppressed.
14977046	1	10	gly	glycosylation	340:352	arg2	three					315:319	three	315:319	three	315:319	To investigate the glycosylation of the human bradykinin B2 receptor and the functional significance of this modification, we studied receptors mutated at single or multiple combinations of the three potential N-linked glycosylation sites, asparagines N3, N12 and N180, in COS-7, HEK 293 and CHO-K1 cells.
14977046	1	10	gly	glycosylation	340:352	arg2	asparagines					361:371	asparagines N3, N12 and N180	361:388	asparagines N3, N12 and N180	361:388	To investigate the glycosylation of the human bradykinin B2 receptor and the functional significance of this modification, we studied receptors mutated at single or multiple combinations of the three potential N-linked glycosylation sites, asparagines N3, N12 and N180, in COS-7, HEK 293 and CHO-K1 cells.
14977046	1	10	gly	glycosylation	340:352	arg2	sites					354:358	the three potential N-linked glycosylation sites	311:358	the three potential N-linked glycosylation sites	311:358	To investigate the glycosylation of the human bradykinin B2 receptor and the functional significance of this modification, we studied receptors mutated at single or multiple combinations of the three potential N-linked glycosylation sites, asparagines N3, N12 and N180, in COS-7, HEK 293 and CHO-K1 cells.
14977046	0	11	link	N-linked	0:7	arg1	glycosylation					9:21	N-linked glycosylation	0:21	N-linked glycosylation of the human bradykinin B2 receptor	0:57	N-linked glycosylation of the human bradykinin B2 receptor is required for optimal cell-surface expression and coupling.
14977046	1	12	theme	bradykinin	167:176	arg1	receptor					181:188	the human bradykinin B2 receptor	157:188	the human bradykinin B2 receptor	157:188	To investigate the glycosylation of the human bradykinin B2 receptor and the functional significance of this modification, we studied receptors mutated at single or multiple combinations of the three potential N-linked glycosylation sites, asparagines N3, N12 and N180, in COS-7, HEK 293 and CHO-K1 cells.
14977046	2	13	theme	Western	427:433	arg1	experiments					440:450	Western blot experiments	427:450	Western blot experiments	427:450	Western blot experiments demonstrated that all three extracellular asparagines are glycosylated.
14977046	1	14	from	combinations	295:306	arg1	cells					420:424	COS-7, HEK 293 and CHO-K1 cells	394:424	cells	420:424	To investigate the glycosylation of the human bradykinin B2 receptor and the functional significance of this modification, we studied receptors mutated at single or multiple combinations of the three potential N-linked glycosylation sites, asparagines N3, N12 and N180, in COS-7, HEK 293 and CHO-K1 cells.
14977046	1	14	from	combinations	295:306	arg1	HEK					401:403	COS-7, HEK 293 and CHO-K1 cells	394:424	HEK	401:403	To investigate the glycosylation of the human bradykinin B2 receptor and the functional significance of this modification, we studied receptors mutated at single or multiple combinations of the three potential N-linked glycosylation sites, asparagines N3, N12 and N180, in COS-7, HEK 293 and CHO-K1 cells.
14977046	4	15	theme	phospholipase	793:805	arg1	C					807:807	phospholipase C	793:807	phospholipase C	793:807	However, the glycosylated receptors were expressed at the cell-surface to a much greater extent than the non-glycosylated receptor and coupling to phospholipase C was less efficient for receptor lacking N-terminal glycosylation.
14977046	1	16	theme	B2	178:179	arg1	receptor					181:188	the human bradykinin B2 receptor	157:188	the human bradykinin B2 receptor	157:188	To investigate the glycosylation of the human bradykinin B2 receptor and the functional significance of this modification, we studied receptors mutated at single or multiple combinations of the three potential N-linked glycosylation sites, asparagines N3, N12 and N180, in COS-7, HEK 293 and CHO-K1 cells.
14977046	2	17	theme	extracellular	480:492	arg1	asparagines					494:504	all three extracellular asparagines	470:504	all three extracellular asparagines	470:504	Western blot experiments demonstrated that all three extracellular asparagines are glycosylated.
14977046	3	18	theme	receptor	563:570	arg1	sequestration					572:584	receptor sequestration	563:584	receptor sequestration	563:584	The kinetics of bradykinin binding and receptor sequestration remained unchanged after glycosylation had been suppressed.
14977046	1	19	theme	receptor	181:188	arg1	significance					209:220	the functional significance	194:220	the functional significance of this modification	194:241	To investigate the glycosylation of the human bradykinin B2 receptor and the functional significance of this modification, we studied receptors mutated at single or multiple combinations of the three potential N-linked glycosylation sites, asparagines N3, N12 and N180, in COS-7, HEK 293 and CHO-K1 cells.
14977046	1	19	theme	receptor	181:188	arg1	glycosylation					140:152	the glycosylation	136:152	the glycosylation of the human bradykinin B2 receptor	136:188	To investigate the glycosylation of the human bradykinin B2 receptor and the functional significance of this modification, we studied receptors mutated at single or multiple combinations of the three potential N-linked glycosylation sites, asparagines N3, N12 and N180, in COS-7, HEK 293 and CHO-K1 cells.
14977046	0	20	theme	N-linked	0:7	arg1	glycosylation					9:21	N-linked glycosylation	0:21	N-linked glycosylation of the human bradykinin B2 receptor	0:57	N-linked glycosylation of the human bradykinin B2 receptor is required for optimal cell-surface expression and coupling.
14977046	1	21	theme	single	276:281	arg1	combinations					295:306	single or multiple combinations	276:306	single or multiple combinations of the three potential N-linked glycosylation sites, asparagines N3, N12 and N180, in COS-7, HEK 293 and CHO-K1 cells	276:424	To investigate the glycosylation of the human bradykinin B2 receptor and the functional significance of this modification, we studied receptors mutated at single or multiple combinations of the three potential N-linked glycosylation sites, asparagines N3, N12 and N180, in COS-7, HEK 293 and CHO-K1 cells.
14977046	4	22	gly	glycosylated	659:670	arg1	receptors					672:680	the glycosylated receptors	655:680	the glycosylated receptors	655:680	However, the glycosylated receptors were expressed at the cell-surface to a much greater extent than the non-glycosylated receptor and coupling to phospholipase C was less efficient for receptor lacking N-terminal glycosylation.
14977046	3	23	theme	sequestration	572:584	arg1	kinetics					528:535	The kinetics	524:535	The kinetics of bradykinin binding and receptor sequestration	524:584	The kinetics of bradykinin binding and receptor sequestration remained unchanged after glycosylation had been suppressed.
14977046	5	24	gly	glycosylation	942:954	arg1	B2					929:930	the human bradykinin B2 receptor	908:939	the human bradykinin B2 receptor	908:939	These results indicate that, for the human bradykinin B2 receptor, glycosylation is not required for optimal ligand binding, but plays an important role in cell-surface addressing and receptor function.
14977046	5	24	gly	glycosylation	942:954	arg1	ligand					984:989	optimal ligand binding	976:997	optimal ligand binding	976:997	These results indicate that, for the human bradykinin B2 receptor, glycosylation is not required for optimal ligand binding, but plays an important role in cell-surface addressing and receptor function.
14977046	5	24	gly	glycosylation	942:954	arg1	bradykinin					918:927	the human bradykinin B2 receptor	908:939	the human bradykinin B2 receptor	908:939	These results indicate that, for the human bradykinin B2 receptor, glycosylation is not required for optimal ligand binding, but plays an important role in cell-surface addressing and receptor function.
14977046	5	25	theme	receptor	1059:1066	arg1	function					1068:1075	receptor function	1059:1075	receptor function	1059:1075	These results indicate that, for the human bradykinin B2 receptor, glycosylation is not required for optimal ligand binding, but plays an important role in cell-surface addressing and receptor function.
14977046	3	26	theme	binding	551:557	arg1	kinetics					528:535	The kinetics	524:535	The kinetics of bradykinin binding and receptor sequestration	524:584	The kinetics of bradykinin binding and receptor sequestration remained unchanged after glycosylation had been suppressed.
14977046	4	27	dep	extent	735:740	arg1	efficient					818:826	efficient	818:826	efficient	818:826	However, the glycosylated receptors were expressed at the cell-surface to a much greater extent than the non-glycosylated receptor and coupling to phospholipase C was less efficient for receptor lacking N-terminal glycosylation.
14977046	4	27	dep	extent	735:740	arg1	receptor					768:775	the non-glycosylated receptor	747:775	the non-glycosylated receptor	747:775	However, the glycosylated receptors were expressed at the cell-surface to a much greater extent than the non-glycosylated receptor and coupling to phospholipase C was less efficient for receptor lacking N-terminal glycosylation.
14977046	1	28	theme	multiple	286:293	arg1	combinations					295:306	single or multiple combinations	276:306	single or multiple combinations of the three potential N-linked glycosylation sites, asparagines N3, N12 and N180, in COS-7, HEK 293 and CHO-K1 cells	276:424	To investigate the glycosylation of the human bradykinin B2 receptor and the functional significance of this modification, we studied receptors mutated at single or multiple combinations of the three potential N-linked glycosylation sites, asparagines N3, N12 and N180, in COS-7, HEK 293 and CHO-K1 cells.
14977046	5	29	theme	ligand	984:989	arg1	binding					991:997	optimal ligand binding	976:997	optimal ligand binding	976:997	These results indicate that, for the human bradykinin B2 receptor, glycosylation is not required for optimal ligand binding, but plays an important role in cell-surface addressing and receptor function.
14977046	1	30	link	N-linked	331:338	arg1	sites					354:358	the three potential N-linked glycosylation sites	311:358	the three potential N-linked glycosylation sites	311:358	To investigate the glycosylation of the human bradykinin B2 receptor and the functional significance of this modification, we studied receptors mutated at single or multiple combinations of the three potential N-linked glycosylation sites, asparagines N3, N12 and N180, in COS-7, HEK 293 and CHO-K1 cells.
14977046	1	30	link	N-linked	331:338	arg1	asparagines					361:371	asparagines N3, N12 and N180	361:388	asparagines N3, N12 and N180	361:388	To investigate the glycosylation of the human bradykinin B2 receptor and the functional significance of this modification, we studied receptors mutated at single or multiple combinations of the three potential N-linked glycosylation sites, asparagines N3, N12 and N180, in COS-7, HEK 293 and CHO-K1 cells.
14977046	1	31	theme	functional	198:207	arg1	significance					209:220	the functional significance	194:220	the functional significance of this modification	194:241	To investigate the glycosylation of the human bradykinin B2 receptor and the functional significance of this modification, we studied receptors mutated at single or multiple combinations of the three potential N-linked glycosylation sites, asparagines N3, N12 and N180, in COS-7, HEK 293 and CHO-K1 cells.
14977046	0	32	theme	bradykinin	36:45	arg1	receptor					50:57	the human bradykinin B2 receptor	26:57	the human bradykinin B2 receptor	26:57	N-linked glycosylation of the human bradykinin B2 receptor is required for optimal cell-surface expression and coupling.
14977046	5	33	theme	cell-surface	1031:1042	arg1	addressing					1044:1053	cell-surface addressing	1031:1053	cell-surface addressing	1031:1053	These results indicate that, for the human bradykinin B2 receptor, glycosylation is not required for optimal ligand binding, but plays an important role in cell-surface addressing and receptor function.
14977046	4	34	theme	glycosylated	659:670	arg1	receptors					672:680	the glycosylated receptors	655:680	the glycosylated receptors	655:680	However, the glycosylated receptors were expressed at the cell-surface to a much greater extent than the non-glycosylated receptor and coupling to phospholipase C was less efficient for receptor lacking N-terminal glycosylation.
14977046	0	35	theme	human	30:34	arg1	receptor					50:57	the human bradykinin B2 receptor	26:57	the human bradykinin B2 receptor	26:57	N-linked glycosylation of the human bradykinin B2 receptor is required for optimal cell-surface expression and coupling.
14977046	0	36	gly	glycosylation	9:21	arg1	receptor					50:57	the human bradykinin B2 receptor	26:57	the human bradykinin B2 receptor	26:57	N-linked glycosylation of the human bradykinin B2 receptor is required for optimal cell-surface expression and coupling.
14977046	0	37	theme	receptor	50:57	arg1	glycosylation					9:21	N-linked glycosylation	0:21	N-linked glycosylation of the human bradykinin B2 receptor	0:57	N-linked glycosylation of the human bradykinin B2 receptor is required for optimal cell-surface expression and coupling.
14977046	5	38	theme	human	912:916	arg1	receptor					932:939	the human bradykinin B2 receptor	908:939	the human bradykinin B2 receptor	908:939	These results indicate that, for the human bradykinin B2 receptor, glycosylation is not required for optimal ligand binding, but plays an important role in cell-surface addressing and receptor function.
14977046	4	39	theme	greater	727:733	arg1	extent					735:740	a much greater extent	720:740	a much greater extent than the non-glycosylated receptor and coupling to phospholipase C was less efficient for receptor lacking N-terminal glycosylation	720:872	However, the glycosylated receptors were expressed at the cell-surface to a much greater extent than the non-glycosylated receptor and coupling to phospholipase C was less efficient for receptor lacking N-terminal glycosylation.
14977046	0	40	theme	B2	47:48	arg1	receptor					50:57	the human bradykinin B2 receptor	26:57	the human bradykinin B2 receptor	26:57	N-linked glycosylation of the human bradykinin B2 receptor is required for optimal cell-surface expression and coupling.
14977046	1	41	dep	asparagines	361:371	arg1	N3					373:374	N3	373:374	N3	373:374	To investigate the glycosylation of the human bradykinin B2 receptor and the functional significance of this modification, we studied receptors mutated at single or multiple combinations of the three potential N-linked glycosylation sites, asparagines N3, N12 and N180, in COS-7, HEK 293 and CHO-K1 cells.
14977046	1	41	dep	asparagines	361:371	arg1	N180					385:388	N180	385:388	N180	385:388	To investigate the glycosylation of the human bradykinin B2 receptor and the functional significance of this modification, we studied receptors mutated at single or multiple combinations of the three potential N-linked glycosylation sites, asparagines N3, N12 and N180, in COS-7, HEK 293 and CHO-K1 cells.
14977046	1	41	dep	asparagines	361:371	arg1	asparagines					361:371	asparagines N3, N12 and N180	361:388	asparagines N3, N12 and N180	361:388	To investigate the glycosylation of the human bradykinin B2 receptor and the functional significance of this modification, we studied receptors mutated at single or multiple combinations of the three potential N-linked glycosylation sites, asparagines N3, N12 and N180, in COS-7, HEK 293 and CHO-K1 cells.
14977046	1	41	dep	asparagines	361:371	arg1	N12					377:379	N12	377:379	N12	377:379	To investigate the glycosylation of the human bradykinin B2 receptor and the functional significance of this modification, we studied receptors mutated at single or multiple combinations of the three potential N-linked glycosylation sites, asparagines N3, N12 and N180, in COS-7, HEK 293 and CHO-K1 cells.
14977046	1	42	gly	glycosylation	140:152	arg1	receptor					181:188	the human bradykinin B2 receptor	157:188	the human bradykinin B2 receptor	157:188	To investigate the glycosylation of the human bradykinin B2 receptor and the functional significance of this modification, we studied receptors mutated at single or multiple combinations of the three potential N-linked glycosylation sites, asparagines N3, N12 and N180, in COS-7, HEK 293 and CHO-K1 cells.
14977046	1	42	gly	glycosylation	140:152	arg1	modification					230:241	this modification	225:241	this modification	225:241	To investigate the glycosylation of the human bradykinin B2 receptor and the functional significance of this modification, we studied receptors mutated at single or multiple combinations of the three potential N-linked glycosylation sites, asparagines N3, N12 and N180, in COS-7, HEK 293 and CHO-K1 cells.
14977046	1	43	theme	COS-7	394:398	arg1	HEK					401:403	COS-7, HEK 293 and CHO-K1 cells	394:424	HEK	401:403	To investigate the glycosylation of the human bradykinin B2 receptor and the functional significance of this modification, we studied receptors mutated at single or multiple combinations of the three potential N-linked glycosylation sites, asparagines N3, N12 and N180, in COS-7, HEK 293 and CHO-K1 cells.
14977046	4	44	theme	N-terminal	849:858	arg1	glycosylation					860:872	N-terminal glycosylation	849:872	N-terminal glycosylation	849:872	However, the glycosylated receptors were expressed at the cell-surface to a much greater extent than the non-glycosylated receptor and coupling to phospholipase C was less efficient for receptor lacking N-terminal glycosylation.
14977046	1	45	theme	potential	321:329	arg1	sites					354:358	the three potential N-linked glycosylation sites	311:358	the three potential N-linked glycosylation sites	311:358	To investigate the glycosylation of the human bradykinin B2 receptor and the functional significance of this modification, we studied receptors mutated at single or multiple combinations of the three potential N-linked glycosylation sites, asparagines N3, N12 and N180, in COS-7, HEK 293 and CHO-K1 cells.
14977046	1	45	theme	potential	321:329	arg1	asparagines					361:371	asparagines N3, N12 and N180	361:388	asparagines N3, N12 and N180	361:388	To investigate the glycosylation of the human bradykinin B2 receptor and the functional significance of this modification, we studied receptors mutated at single or multiple combinations of the three potential N-linked glycosylation sites, asparagines N3, N12 and N180, in COS-7, HEK 293 and CHO-K1 cells.
14977046	1	46	from	sites	354:358	arg1	cells					420:424	COS-7, HEK 293 and CHO-K1 cells	394:424	cells	420:424	To investigate the glycosylation of the human bradykinin B2 receptor and the functional significance of this modification, we studied receptors mutated at single or multiple combinations of the three potential N-linked glycosylation sites, asparagines N3, N12 and N180, in COS-7, HEK 293 and CHO-K1 cells.
14977046	1	46	from	sites	354:358	arg1	HEK					401:403	COS-7, HEK 293 and CHO-K1 cells	394:424	HEK	401:403	To investigate the glycosylation of the human bradykinin B2 receptor and the functional significance of this modification, we studied receptors mutated at single or multiple combinations of the three potential N-linked glycosylation sites, asparagines N3, N12 and N180, in COS-7, HEK 293 and CHO-K1 cells.
14977046	5	47	theme	optimal	976:982	arg1	binding					991:997	optimal ligand binding	976:997	optimal ligand binding	976:997	These results indicate that, for the human bradykinin B2 receptor, glycosylation is not required for optimal ligand binding, but plays an important role in cell-surface addressing and receptor function.
14977046	5	48	theme	important	1013:1021	arg1	role					1023:1026	an important role	1010:1026	an important role	1010:1026	These results indicate that, for the human bradykinin B2 receptor, glycosylation is not required for optimal ligand binding, but plays an important role in cell-surface addressing and receptor function.
14977046	1	49	theme	modification	230:241	arg1	significance					209:220	the functional significance	194:220	the functional significance of this modification	194:241	To investigate the glycosylation of the human bradykinin B2 receptor and the functional significance of this modification, we studied receptors mutated at single or multiple combinations of the three potential N-linked glycosylation sites, asparagines N3, N12 and N180, in COS-7, HEK 293 and CHO-K1 cells.
14977046	1	49	theme	modification	230:241	arg1	glycosylation					140:152	the glycosylation	136:152	the glycosylation of the human bradykinin B2 receptor	136:188	To investigate the glycosylation of the human bradykinin B2 receptor and the functional significance of this modification, we studied receptors mutated at single or multiple combinations of the three potential N-linked glycosylation sites, asparagines N3, N12 and N180, in COS-7, HEK 293 and CHO-K1 cells.
14977046	1	50	from	HEK	401:403	arg1	combinations					295:306	single or multiple combinations	276:306	single or multiple combinations of the three potential N-linked glycosylation sites, asparagines N3, N12 and N180, in COS-7, HEK 293 and CHO-K1 cells	276:424	To investigate the glycosylation of the human bradykinin B2 receptor and the functional significance of this modification, we studied receptors mutated at single or multiple combinations of the three potential N-linked glycosylation sites, asparagines N3, N12 and N180, in COS-7, HEK 293 and CHO-K1 cells.
14977046	1	51	from	cells	420:424	arg1	combinations					295:306	single or multiple combinations	276:306	single or multiple combinations of the three potential N-linked glycosylation sites, asparagines N3, N12 and N180, in COS-7, HEK 293 and CHO-K1 cells	276:424	To investigate the glycosylation of the human bradykinin B2 receptor and the functional significance of this modification, we studied receptors mutated at single or multiple combinations of the three potential N-linked glycosylation sites, asparagines N3, N12 and N180, in COS-7, HEK 293 and CHO-K1 cells.
14977046	2	52	theme	blot	435:438	arg1	experiments					440:450	Western blot experiments	427:450	Western blot experiments	427:450	Western blot experiments demonstrated that all three extracellular asparagines are glycosylated.
14977046	1	53	theme	N-linked	331:338	arg1	sites					354:358	the three potential N-linked glycosylation sites	311:358	the three potential N-linked glycosylation sites	311:358	To investigate the glycosylation of the human bradykinin B2 receptor and the functional significance of this modification, we studied receptors mutated at single or multiple combinations of the three potential N-linked glycosylation sites, asparagines N3, N12 and N180, in COS-7, HEK 293 and CHO-K1 cells.
14977046	1	53	theme	N-linked	331:338	arg1	asparagines					361:371	asparagines N3, N12 and N180	361:388	asparagines N3, N12 and N180	361:388	To investigate the glycosylation of the human bradykinin B2 receptor and the functional significance of this modification, we studied receptors mutated at single or multiple combinations of the three potential N-linked glycosylation sites, asparagines N3, N12 and N180, in COS-7, HEK 293 and CHO-K1 cells.
14977046	5	54	theme	bradykinin	918:927	arg1	receptor					932:939	the human bradykinin B2 receptor	908:939	the human bradykinin B2 receptor	908:939	These results indicate that, for the human bradykinin B2 receptor, glycosylation is not required for optimal ligand binding, but plays an important role in cell-surface addressing and receptor function.
14977046	4	55	gly	non-glycosylated	751:766	arg1	receptor					768:775	the non-glycosylated receptor	747:775	the non-glycosylated receptor	747:775	However, the glycosylated receptors were expressed at the cell-surface to a much greater extent than the non-glycosylated receptor and coupling to phospholipase C was less efficient for receptor lacking N-terminal glycosylation.
14977046	4	55	gly	non-glycosylated	751:766	arg1	efficient					818:826	efficient	818:826	efficient	818:826	However, the glycosylated receptors were expressed at the cell-surface to a much greater extent than the non-glycosylated receptor and coupling to phospholipase C was less efficient for receptor lacking N-terminal glycosylation.
14573609	0	0	theme	cell	77:80	arg1	lines					82:86	human tumor cell lines	65:86	human tumor cell lines	65:86	Secretion of heparanase protein is regulated by glycosylation in human tumor cell lines.
14573609	4	1	from	residues	602:609	arg1	lines					631:635	human tumor cell lines	614:635	human tumor cell lines	614:635	Heparanase protein was glycosylated at six Asn residues in human tumor cell lines.
14573609	5	2	gly	glycosylation	697:709	arg1	heparanase					748:757	heparanase	748:757	heparanase	748:757	Treatment with a glycosylation inhibitor demonstrated that glycosylation was not required for the activity of heparanase.
14573609	0	3	theme	tumor	71:75	arg1	lines					82:86	human tumor cell lines	65:86	human tumor cell lines	65:86	Secretion of heparanase protein is regulated by glycosylation in human tumor cell lines.
14573609	5	4	theme	glycosylation	655:667	arg1	inhibitor					669:677	a glycosylation inhibitor	653:677	a glycosylation inhibitor	653:677	Treatment with a glycosylation inhibitor demonstrated that glycosylation was not required for the activity of heparanase.
14573609	1	5	theme	tumor	251:255	arg1	cells					257:261	tumor cells	251:261	tumor cells	251:261	The endo-beta-d-glucuronidase, heparanase, is capable of specifically degrading heparan sulfate, and this activity is associated with the metastatic potential of tumor cells.
14573609	2	6	gly	glycosylated	398:409	arg1	heparanase					411:420	glycosylated heparanase	398:420	glycosylated heparanase	398:420	The predicted amino acid sequence of heparanase includes six putative N-glycosylation sites; however, the precise biochemical role of glycosylated heparanase remains unknown.
14573609	3	7	from	function	505:512	arg1	lines					548:552	human tumor cell lines	531:552	human tumor cell lines	531:552	In this study, we examined the link between glycosylation and the function of heparanase in human tumor cell lines.
14573609	2	8	theme	acid	284:287	arg1	sequence					289:296	The predicted amino acid sequence	264:296	The predicted amino acid sequence of heparanase	264:310	The predicted amino acid sequence of heparanase includes six putative N-glycosylation sites; however, the precise biochemical role of glycosylated heparanase remains unknown.
14573609	1	9	theme	cells	257:261	arg1	potential					238:246	the metastatic potential	223:246	the metastatic potential of tumor cells	223:261	The endo-beta-d-glucuronidase, heparanase, is capable of specifically degrading heparan sulfate, and this activity is associated with the metastatic potential of tumor cells.
14573609	3	10	theme	cell	543:546	arg1	lines					548:552	human tumor cell lines	531:552	human tumor cell lines	531:552	In this study, we examined the link between glycosylation and the function of heparanase in human tumor cell lines.
14573609	6	11	theme	reticulum-to-Golgi	820:837	arg1	transport					839:847	endoplasmic reticulum-to-Golgi transport	808:847	endoplasmic reticulum-to-Golgi transport	808:847	However, glycosylation affected the kinetics of endoplasmic reticulum-to-Golgi transport and of secretion of the enzyme.
14573609	2	12	theme	amino	278:282	arg1	sequence					289:296	The predicted amino acid sequence	264:296	The predicted amino acid sequence of heparanase	264:310	The predicted amino acid sequence of heparanase includes six putative N-glycosylation sites; however, the precise biochemical role of glycosylated heparanase remains unknown.
14573609	6	13	theme	endoplasmic	808:818	arg1	transport					839:847	endoplasmic reticulum-to-Golgi transport	808:847	endoplasmic reticulum-to-Golgi transport	808:847	However, glycosylation affected the kinetics of endoplasmic reticulum-to-Golgi transport and of secretion of the enzyme.
14573609	2	14	theme	predicted	268:276	arg1	sequence					289:296	The predicted amino acid sequence	264:296	The predicted amino acid sequence of heparanase	264:310	The predicted amino acid sequence of heparanase includes six putative N-glycosylation sites; however, the precise biochemical role of glycosylated heparanase remains unknown.
14573609	1	15	theme	heparan	169:175	arg1	sulfate					177:183	heparan sulfate	169:183	heparan sulfate	169:183	The endo-beta-d-glucuronidase, heparanase, is capable of specifically degrading heparan sulfate, and this activity is associated with the metastatic potential of tumor cells.
14573609	5	16	theme	heparanase	748:757	arg1	activity					736:743	the activity	732:743	the activity of heparanase	732:757	Treatment with a glycosylation inhibitor demonstrated that glycosylation was not required for the activity of heparanase.
14573609	3	17	theme	human	531:535	arg1	lines					548:552	human tumor cell lines	531:552	human tumor cell lines	531:552	In this study, we examined the link between glycosylation and the function of heparanase in human tumor cell lines.
14573609	4	18	gly	glycosylated	578:589	arg2	residues					602:609	six Asn residues	594:609	six Asn residues in human tumor cell lines	594:635	Heparanase protein was glycosylated at six Asn residues in human tumor cell lines.
14573609	4	18	gly	glycosylated	578:589	arg1	protein					566:572	Heparanase protein	555:572	Heparanase protein	555:572	Heparanase protein was glycosylated at six Asn residues in human tumor cell lines.
14573609	2	19	theme	biochemical	378:388	arg1	role					390:393	the precise biochemical role	366:393	the precise biochemical role of glycosylated heparanase	366:420	The predicted amino acid sequence of heparanase includes six putative N-glycosylation sites; however, the precise biochemical role of glycosylated heparanase remains unknown.
14573609	3	20	from	glycosylation	483:495	arg1	lines					548:552	human tumor cell lines	531:552	human tumor cell lines	531:552	In this study, we examined the link between glycosylation and the function of heparanase in human tumor cell lines.
14573609	3	21	gly	glycosylation	483:495	arg1	lines					548:552	human tumor cell lines	531:552	human tumor cell lines	531:552	In this study, we examined the link between glycosylation and the function of heparanase in human tumor cell lines.
14573609	3	21	gly	glycosylation	483:495	arg1	heparanase					517:526	heparanase	517:526	heparanase	517:526	In this study, we examined the link between glycosylation and the function of heparanase in human tumor cell lines.
14573609	2	22	theme	precise	370:376	arg1	role					390:393	the precise biochemical role	366:393	the precise biochemical role of glycosylated heparanase	366:420	The predicted amino acid sequence of heparanase includes six putative N-glycosylation sites; however, the precise biochemical role of glycosylated heparanase remains unknown.
14573609	0	23	theme	protein	24:30	arg1	Secretion					0:8	Secretion	0:8	Secretion of heparanase protein	0:30	Secretion of heparanase protein is regulated by glycosylation in human tumor cell lines.
14573609	4	24	theme	cell	626:629	arg1	lines					631:635	human tumor cell lines	614:635	human tumor cell lines	614:635	Heparanase protein was glycosylated at six Asn residues in human tumor cell lines.
14573609	2	25	theme	heparanase	301:310	arg1	sequence					289:296	The predicted amino acid sequence	264:296	The predicted amino acid sequence of heparanase	264:310	The predicted amino acid sequence of heparanase includes six putative N-glycosylation sites; however, the precise biochemical role of glycosylated heparanase remains unknown.
14573609	4	26	theme	tumor	620:624	arg1	lines					631:635	human tumor cell lines	614:635	human tumor cell lines	614:635	Heparanase protein was glycosylated at six Asn residues in human tumor cell lines.
14573609	4	27	theme	Heparanase	555:564	arg1	protein					566:572	Heparanase protein	555:572	Heparanase protein	555:572	Heparanase protein was glycosylated at six Asn residues in human tumor cell lines.
14573609	2	28	theme	heparanase	411:420	arg1	role					390:393	the precise biochemical role	366:393	the precise biochemical role of glycosylated heparanase	366:420	The predicted amino acid sequence of heparanase includes six putative N-glycosylation sites; however, the precise biochemical role of glycosylated heparanase remains unknown.
14573609	5	29	with	Treatment	638:646	arg1	inhibitor					669:677	a glycosylation inhibitor	653:677	a glycosylation inhibitor	653:677	Treatment with a glycosylation inhibitor demonstrated that glycosylation was not required for the activity of heparanase.
14573609	6	30	gly	glycosylation	769:781	arg1	transport					839:847	endoplasmic reticulum-to-Golgi transport	808:847	endoplasmic reticulum-to-Golgi transport	808:847	However, glycosylation affected the kinetics of endoplasmic reticulum-to-Golgi transport and of secretion of the enzyme.
14573609	6	30	gly	glycosylation	769:781	arg1	secretion					856:864	secretion	856:864	secretion of the enzyme	856:878	However, glycosylation affected the kinetics of endoplasmic reticulum-to-Golgi transport and of secretion of the enzyme.
14573609	4	31	theme	human	614:618	arg1	lines					631:635	human tumor cell lines	614:635	human tumor cell lines	614:635	Heparanase protein was glycosylated at six Asn residues in human tumor cell lines.
14573609	2	32	theme	glycosylated	398:409	arg1	heparanase					411:420	glycosylated heparanase	398:420	glycosylated heparanase	398:420	The predicted amino acid sequence of heparanase includes six putative N-glycosylation sites; however, the precise biochemical role of glycosylated heparanase remains unknown.
14573609	2	33	gly	N-glycosylation	334:348	arg2	six					321:323	six	321:323	six	321:323	The predicted amino acid sequence of heparanase includes six putative N-glycosylation sites; however, the precise biochemical role of glycosylated heparanase remains unknown.
14573609	2	33	gly	N-glycosylation	334:348	arg2	sites					350:354	six putative N-glycosylation sites	321:354	six putative N-glycosylation sites	321:354	The predicted amino acid sequence of heparanase includes six putative N-glycosylation sites; however, the precise biochemical role of glycosylated heparanase remains unknown.
14573609	6	34	theme	enzyme	873:878	arg1	secretion					856:864	secretion	856:864	secretion of the enzyme	856:878	However, glycosylation affected the kinetics of endoplasmic reticulum-to-Golgi transport and of secretion of the enzyme.
14573609	2	35	theme	N-glycosylation	334:348	arg1	sites					350:354	six putative N-glycosylation sites	321:354	six putative N-glycosylation sites	321:354	The predicted amino acid sequence of heparanase includes six putative N-glycosylation sites; however, the precise biochemical role of glycosylated heparanase remains unknown.
14573609	6	36	theme	transport	839:847	arg1	kinetics					796:803	the kinetics	792:803	the kinetics of endoplasmic reticulum-to-Golgi transport and of secretion of the enzyme	792:878	However, glycosylation affected the kinetics of endoplasmic reticulum-to-Golgi transport and of secretion of the enzyme.
14573609	2	37	theme	putative	325:332	arg1	sites					350:354	six putative N-glycosylation sites	321:354	six putative N-glycosylation sites	321:354	The predicted amino acid sequence of heparanase includes six putative N-glycosylation sites; however, the precise biochemical role of glycosylated heparanase remains unknown.
14573609	6	38	theme	secretion	856:864	arg1	kinetics					796:803	the kinetics	792:803	the kinetics of endoplasmic reticulum-to-Golgi transport and of secretion of the enzyme	792:878	However, glycosylation affected the kinetics of endoplasmic reticulum-to-Golgi transport and of secretion of the enzyme.
14573609	3	39	theme	tumor	537:541	arg1	lines					548:552	human tumor cell lines	531:552	human tumor cell lines	531:552	In this study, we examined the link between glycosylation and the function of heparanase in human tumor cell lines.
14573609	4	40	theme	Asn	598:600	arg1	residues					602:609	six Asn residues	594:609	six Asn residues in human tumor cell lines	594:635	Heparanase protein was glycosylated at six Asn residues in human tumor cell lines.
14573609	0	41	theme	human	65:69	arg1	lines					82:86	human tumor cell lines	65:86	human tumor cell lines	65:86	Secretion of heparanase protein is regulated by glycosylation in human tumor cell lines.
14573609	1	42	theme	metastatic	227:236	arg1	potential					238:246	the metastatic potential	223:246	the metastatic potential of tumor cells	223:261	The endo-beta-d-glucuronidase, heparanase, is capable of specifically degrading heparan sulfate, and this activity is associated with the metastatic potential of tumor cells.
14573609	0	43	theme	heparanase	13:22	arg1	protein					24:30	heparanase protein	13:30	heparanase protein	13:30	Secretion of heparanase protein is regulated by glycosylation in human tumor cell lines.
14573609	3	44	theme	heparanase	517:526	arg1	glycosylation					483:495	glycosylation	483:495	glycosylation	483:495	In this study, we examined the link between glycosylation and the function of heparanase in human tumor cell lines.
14573609	3	44	theme	heparanase	517:526	arg1	function					505:512	the function	501:512	the function of heparanase in human tumor cell lines	501:552	In this study, we examined the link between glycosylation and the function of heparanase in human tumor cell lines.
16371009	1	0	theme	extracellular	232:244	arg1	loop					246:249	the large extracellular loop	222:249	the large extracellular loop	222:249	The role of conserved polar glutamine, asparagine and threonine residues in the large extracellular loop, and glycosylation, to agonist action at human P2X1 receptors was tested by generating alanine substitution mutants.
16371009	3	1	dep	agonists	621:628	arg1	agonists					621:628	the partial agonists	609:628	the partial agonists BzATP and Ap5A	609:643	The mutants Q95A, Q112A, Q114A and T158A showed changes in efficacy for the partial agonists BzATP and Ap5A, suggesting that these polar residues may contribute to the gating of the channel.
16371009	3	1	dep	agonists	621:628	arg1	Ap5A					640:643	Ap5A	640:643	Ap5A	640:643	The mutants Q95A, Q112A, Q114A and T158A showed changes in efficacy for the partial agonists BzATP and Ap5A, suggesting that these polar residues may contribute to the gating of the channel.
16371009	3	1	dep	agonists	621:628	arg1	BzATP					630:634	BzATP	630:634	BzATP	630:634	The mutants Q95A, Q112A, Q114A and T158A showed changes in efficacy for the partial agonists BzATP and Ap5A, suggesting that these polar residues may contribute to the gating of the channel.
16371009	6	2	theme	endoplasmic	1056:1066	arg1	reticulum					1068:1076	the endoplasmic reticulum	1052:1076	the endoplasmic reticulum	1052:1076	N153, N184 and N242 are glycosylated in the endoplasmic reticulum and N300 acquires complex glycosylation in the golgi.
16371009	4	3	from	decreases	792:800	arg1	potency					809:815	ATP potency	805:815	ATP potency	805:815	The mutants T186A, N204A and N290A had six-, three- and 60-fold decreases in ATP potency, respectively.
16371009	0	4	theme	agonist	98:104	arg1	action					106:111	agonist action	98:111	agonist action at human P2X1 receptors for ATP	98:143	Contribution of conserved polar glutamine, asparagine and threonine residues and glycosylation to agonist action at human P2X1 receptors for ATP.
16371009	7	5	theme	triplet	1254:1260	arg1	N290F291R292					1262:1273	the conserved triplet N290F291R292	1240:1273	the conserved triplet N290F291R292	1240:1273	These results aid in refining a model for ATP binding at the P2X1 receptor where the residues F185T186, and the conserved triplet N290F291R292, are likely to play a role in ATP action at the receptor.
16371009	7	5	theme	triplet	1254:1260	arg1	likely					1280:1285	likely	1280:1285	likely	1280:1285	These results aid in refining a model for ATP binding at the P2X1 receptor where the residues F185T186, and the conserved triplet N290F291R292, are likely to play a role in ATP action at the receptor.
16371009	2	6	theme	alanine	486:492	arg1	substitution					494:505	alanine substitution	486:505	alanine substitution	486:505	For the majority of mutants (Q56A, Q95A, T104A, T109A, Q112A, Q114A, T146A, N153A, T158A, N184A, N191A, N242A, N300A) alanine substitution had no effect on ATP potency.
16371009	1	7	from	role	150:153	arg1	loop					246:249	the large extracellular loop	222:249	the large extracellular loop	222:249	The role of conserved polar glutamine, asparagine and threonine residues in the large extracellular loop, and glycosylation, to agonist action at human P2X1 receptors was tested by generating alanine substitution mutants.
16371009	1	7	from	role	150:153	arg1	receptors					303:311	human P2X1 receptors	292:311	human P2X1 receptors	292:311	The role of conserved polar glutamine, asparagine and threonine residues in the large extracellular loop, and glycosylation, to agonist action at human P2X1 receptors was tested by generating alanine substitution mutants.
16371009	5	8	dep	agonists	865:872	arg1	agonists					865:872	the partial agonists	853:872	the partial agonists BzATP and Ap5A	853:887	For T186A and N290A, the partial agonists BzATP and Ap5A were no longer agonists but still bind to the receptor as shown by the ability to modulate the response to co-applied ATP.
16371009	5	8	dep	agonists	865:872	arg1	Ap5A					884:887	Ap5A	884:887	Ap5A	884:887	For T186A and N290A, the partial agonists BzATP and Ap5A were no longer agonists but still bind to the receptor as shown by the ability to modulate the response to co-applied ATP.
16371009	5	8	dep	agonists	865:872	arg1	BzATP					874:878	BzATP	874:878	BzATP	874:878	For T186A and N290A, the partial agonists BzATP and Ap5A were no longer agonists but still bind to the receptor as shown by the ability to modulate the response to co-applied ATP.
16371009	1	9	from	threonine	200:208	arg1	loop					246:249	the large extracellular loop	222:249	the large extracellular loop	222:249	The role of conserved polar glutamine, asparagine and threonine residues in the large extracellular loop, and glycosylation, to agonist action at human P2X1 receptors was tested by generating alanine substitution mutants.
16371009	3	10	dep	mutants	541:547	arg1	T158A					572:576	T158A	572:576	T158A	572:576	The mutants Q95A, Q112A, Q114A and T158A showed changes in efficacy for the partial agonists BzATP and Ap5A, suggesting that these polar residues may contribute to the gating of the channel.
16371009	3	10	dep	mutants	541:547	arg1	Q114A					562:566	Q114A	562:566	Q114A	562:566	The mutants Q95A, Q112A, Q114A and T158A showed changes in efficacy for the partial agonists BzATP and Ap5A, suggesting that these polar residues may contribute to the gating of the channel.
16371009	3	10	dep	mutants	541:547	arg1	mutants					541:547	The mutants	537:547	The mutants Q95A, Q112A, Q114A and T158A	537:576	The mutants Q95A, Q112A, Q114A and T158A showed changes in efficacy for the partial agonists BzATP and Ap5A, suggesting that these polar residues may contribute to the gating of the channel.
16371009	3	10	dep	mutants	541:547	arg1	Q112A					555:559	Q112A	555:559	Q112A	555:559	The mutants Q95A, Q112A, Q114A and T158A showed changes in efficacy for the partial agonists BzATP and Ap5A, suggesting that these polar residues may contribute to the gating of the channel.
16371009	7	11	dep	residues	1217:1224	arg1	F185T186					1226:1233	F185T186	1226:1233	F185T186	1226:1233	These results aid in refining a model for ATP binding at the P2X1 receptor where the residues F185T186, and the conserved triplet N290F291R292, are likely to play a role in ATP action at the receptor.
16371009	1	12	theme	alanine	338:344	arg1	mutants					359:365	alanine substitution mutants	338:365	alanine substitution mutants	338:365	The role of conserved polar glutamine, asparagine and threonine residues in the large extracellular loop, and glycosylation, to agonist action at human P2X1 receptors was tested by generating alanine substitution mutants.
16371009	2	13	theme	ATP	524:526	arg1	potency					528:534	ATP potency	524:534	ATP potency	524:534	For the majority of mutants (Q56A, Q95A, T104A, T109A, Q112A, Q114A, T146A, N153A, T158A, N184A, N191A, N242A, N300A) alanine substitution had no effect on ATP potency.
16371009	6	14	gly	glycosylation	1104:1116	arg1	reticulum					1068:1076	the endoplasmic reticulum	1052:1076	the endoplasmic reticulum	1052:1076	N153, N184 and N242 are glycosylated in the endoplasmic reticulum and N300 acquires complex glycosylation in the golgi.
16371009	6	14	gly	glycosylation	1104:1116	arg1	golgi					1125:1129	the golgi	1121:1129	the golgi	1121:1129	N153, N184 and N242 are glycosylated in the endoplasmic reticulum and N300 acquires complex glycosylation in the golgi.
16371009	1	15	theme	substitution	346:357	arg1	mutants					359:365	alanine substitution mutants	338:365	alanine substitution mutants	338:365	The role of conserved polar glutamine, asparagine and threonine residues in the large extracellular loop, and glycosylation, to agonist action at human P2X1 receptors was tested by generating alanine substitution mutants.
16371009	5	16	theme	co-applied	996:1005	arg1	ATP					1007:1009	co-applied ATP	996:1009	co-applied ATP	996:1009	For T186A and N290A, the partial agonists BzATP and Ap5A were no longer agonists but still bind to the receptor as shown by the ability to modulate the response to co-applied ATP.
16371009	0	17	gly	glycosylation	81:93	arg1	residues					68:75	conserved polar glutamine, asparagine and threonine residues	16:75	conserved polar glutamine, asparagine and threonine residues	16:75	Contribution of conserved polar glutamine, asparagine and threonine residues and glycosylation to agonist action at human P2X1 receptors for ATP.
16371009	1	18	theme	conserved	158:166	arg1	glutamine					174:182	conserved polar glutamine	158:182	conserved polar glutamine	158:182	The role of conserved polar glutamine, asparagine and threonine residues in the large extracellular loop, and glycosylation, to agonist action at human P2X1 receptors was tested by generating alanine substitution mutants.
16371009	3	19	from	changes	585:591	arg1	efficacy					596:603	efficacy	596:603	efficacy	596:603	The mutants Q95A, Q112A, Q114A and T158A showed changes in efficacy for the partial agonists BzATP and Ap5A, suggesting that these polar residues may contribute to the gating of the channel.
16371009	3	20	theme	partial	613:619	arg1	agonists					621:628	the partial agonists	609:628	the partial agonists BzATP and Ap5A	609:643	The mutants Q95A, Q112A, Q114A and T158A showed changes in efficacy for the partial agonists BzATP and Ap5A, suggesting that these polar residues may contribute to the gating of the channel.
16371009	3	20	theme	partial	613:619	arg1	Ap5A					640:643	Ap5A	640:643	Ap5A	640:643	The mutants Q95A, Q112A, Q114A and T158A showed changes in efficacy for the partial agonists BzATP and Ap5A, suggesting that these polar residues may contribute to the gating of the channel.
16371009	3	20	theme	partial	613:619	arg1	BzATP					630:634	BzATP	630:634	BzATP	630:634	The mutants Q95A, Q112A, Q114A and T158A showed changes in efficacy for the partial agonists BzATP and Ap5A, suggesting that these polar residues may contribute to the gating of the channel.
16371009	1	21	from	glycosylation	256:268	arg1	loop					246:249	the large extracellular loop	222:249	the large extracellular loop	222:249	The role of conserved polar glutamine, asparagine and threonine residues in the large extracellular loop, and glycosylation, to agonist action at human P2X1 receptors was tested by generating alanine substitution mutants.
16371009	1	22	theme	polar	168:172	arg1	glutamine					174:182	conserved polar glutamine	158:182	conserved polar glutamine	158:182	The role of conserved polar glutamine, asparagine and threonine residues in the large extracellular loop, and glycosylation, to agonist action at human P2X1 receptors was tested by generating alanine substitution mutants.
16371009	7	23	theme	conserved	1244:1252	arg1	N290F291R292					1262:1273	the conserved triplet N290F291R292	1240:1273	the conserved triplet N290F291R292	1240:1273	These results aid in refining a model for ATP binding at the P2X1 receptor where the residues F185T186, and the conserved triplet N290F291R292, are likely to play a role in ATP action at the receptor.
16371009	7	23	theme	conserved	1244:1252	arg1	likely					1280:1285	likely	1280:1285	likely	1280:1285	These results aid in refining a model for ATP binding at the P2X1 receptor where the residues F185T186, and the conserved triplet N290F291R292, are likely to play a role in ATP action at the receptor.
16371009	1	24	theme	glycosylation	256:268	arg1	role					150:153	The role	146:153	The role of conserved polar glutamine, asparagine and threonine residues in the large extracellular loop, and glycosylation, to agonist action at human P2X1 receptors	146:311	The role of conserved polar glutamine, asparagine and threonine residues in the large extracellular loop, and glycosylation, to agonist action at human P2X1 receptors was tested by generating alanine substitution mutants.
16371009	7	25	from	receptor	1323:1330	arg1	action					1309:1314	ATP action	1305:1314	ATP action at the receptor	1305:1330	These results aid in refining a model for ATP binding at the P2X1 receptor where the residues F185T186, and the conserved triplet N290F291R292, are likely to play a role in ATP action at the receptor.
16371009	7	26	theme	P2X1	1193:1196	arg1	receptor					1198:1205	the P2X1 receptor	1189:1205	the P2X1 receptor where the residues F185T186, and the conserved triplet N290F291R292, are likely to play a role in ATP action at the receptor	1189:1330	These results aid in refining a model for ATP binding at the P2X1 receptor where the residues F185T186, and the conserved triplet N290F291R292, are likely to play a role in ATP action at the receptor.
16371009	1	27	theme	glutamine	174:182	arg1	role					150:153	The role	146:153	The role of conserved polar glutamine, asparagine and threonine residues in the large extracellular loop, and glycosylation, to agonist action at human P2X1 receptors	146:311	The role of conserved polar glutamine, asparagine and threonine residues in the large extracellular loop, and glycosylation, to agonist action at human P2X1 receptors was tested by generating alanine substitution mutants.
16371009	0	28	theme	polar	26:30	arg1	residues					68:75	conserved polar glutamine, asparagine and threonine residues	16:75	conserved polar glutamine, asparagine and threonine residues	16:75	Contribution of conserved polar glutamine, asparagine and threonine residues and glycosylation to agonist action at human P2X1 receptors for ATP.
16371009	0	29	theme	P2X1	122:125	arg1	receptors					127:135	human P2X1 receptors	116:135	human P2X1 receptors for ATP	116:143	Contribution of conserved polar glutamine, asparagine and threonine residues and glycosylation to agonist action at human P2X1 receptors for ATP.
16371009	0	30	theme	conserved	16:24	arg1	residues					68:75	conserved polar glutamine, asparagine and threonine residues	16:75	conserved polar glutamine, asparagine and threonine residues	16:75	Contribution of conserved polar glutamine, asparagine and threonine residues and glycosylation to agonist action at human P2X1 receptors for ATP.
16371009	0	31	theme	human	116:120	arg1	receptors					127:135	human P2X1 receptors	116:135	human P2X1 receptors for ATP	116:143	Contribution of conserved polar glutamine, asparagine and threonine residues and glycosylation to agonist action at human P2X1 receptors for ATP.
16371009	4	32	contain	had	763:765	arg2	six-					767:770	six-	767:770	six-	767:770	The mutants T186A, N204A and N290A had six-, three- and 60-fold decreases in ATP potency, respectively.
16371009	4	32	contain	had	763:765	arg1	N204A					747:751	N204A	747:751	N204A	747:751	The mutants T186A, N204A and N290A had six-, three- and 60-fold decreases in ATP potency, respectively.
16371009	4	32	contain	had	763:765	arg2	decreases					792:800	60-fold decreases	784:800	60-fold decreases in ATP potency	784:815	The mutants T186A, N204A and N290A had six-, three- and 60-fold decreases in ATP potency, respectively.
16371009	4	32	contain	had	763:765	arg2	three-					773:778	three-	773:778	three-	773:778	The mutants T186A, N204A and N290A had six-, three- and 60-fold decreases in ATP potency, respectively.
16371009	4	32	contain	had	763:765	arg1	N290A					757:761	N290A	757:761	N290A	757:761	The mutants T186A, N204A and N290A had six-, three- and 60-fold decreases in ATP potency, respectively.
16371009	4	32	contain	had	763:765	arg1	mutants					732:738	The mutants	728:738	The mutants T186A, N204A and N290A	728:761	The mutants T186A, N204A and N290A had six-, three- and 60-fold decreases in ATP potency, respectively.
16371009	1	33	theme	asparagine	185:194	arg1	role					150:153	The role	146:153	The role of conserved polar glutamine, asparagine and threonine residues in the large extracellular loop, and glycosylation, to agonist action at human P2X1 receptors	146:311	The role of conserved polar glutamine, asparagine and threonine residues in the large extracellular loop, and glycosylation, to agonist action at human P2X1 receptors was tested by generating alanine substitution mutants.
16371009	1	34	theme	agonist	274:280	arg1	action					282:287	agonist action	274:287	agonist action	274:287	The role of conserved polar glutamine, asparagine and threonine residues in the large extracellular loop, and glycosylation, to agonist action at human P2X1 receptors was tested by generating alanine substitution mutants.
16371009	7	35	theme	ATP	1305:1307	arg1	action					1309:1314	ATP action	1305:1314	ATP action at the receptor	1305:1330	These results aid in refining a model for ATP binding at the P2X1 receptor where the residues F185T186, and the conserved triplet N290F291R292, are likely to play a role in ATP action at the receptor.
16371009	2	36	dep	mutants	388:394	arg1	T158A					451:455	T158A	451:455	T158A	451:455	For the majority of mutants (Q56A, Q95A, T104A, T109A, Q112A, Q114A, T146A, N153A, T158A, N184A, N191A, N242A, N300A) alanine substitution had no effect on ATP potency.
16371009	2	36	dep	mutants	388:394	arg1	Q95A					403:406	Q95A	403:406	Q95A	403:406	For the majority of mutants (Q56A, Q95A, T104A, T109A, Q112A, Q114A, T146A, N153A, T158A, N184A, N191A, N242A, N300A) alanine substitution had no effect on ATP potency.
16371009	2	36	dep	mutants	388:394	arg1	N300A					479:483	N300A	479:483	N300A	479:483	For the majority of mutants (Q56A, Q95A, T104A, T109A, Q112A, Q114A, T146A, N153A, T158A, N184A, N191A, N242A, N300A) alanine substitution had no effect on ATP potency.
16371009	2	36	dep	mutants	388:394	arg1	Q114A					430:434	Q114A	430:434	Q114A	430:434	For the majority of mutants (Q56A, Q95A, T104A, T109A, Q112A, Q114A, T146A, N153A, T158A, N184A, N191A, N242A, N300A) alanine substitution had no effect on ATP potency.
16371009	2	37	theme	mutants	388:394	arg1	majority					376:383	the majority	372:383	the majority of mutants (Q56A, Q95A, T104A, T109A, Q112A, Q114A, T146A, N153A, T158A, N184A, N191A, N242A, N300A)	372:484	For the majority of mutants (Q56A, Q95A, T104A, T109A, Q112A, Q114A, T146A, N153A, T158A, N184A, N191A, N242A, N300A) alanine substitution had no effect on ATP potency.
16371009	0	38	theme	glutamine	32:40	arg1	residues					68:75	conserved polar glutamine, asparagine and threonine residues	16:75	conserved polar glutamine, asparagine and threonine residues	16:75	Contribution of conserved polar glutamine, asparagine and threonine residues and glycosylation to agonist action at human P2X1 receptors for ATP.
16371009	1	39	from	loop	246:249	arg1	role					150:153	The role	146:153	The role of conserved polar glutamine, asparagine and threonine residues in the large extracellular loop, and glycosylation, to agonist action at human P2X1 receptors	146:311	The role of conserved polar glutamine, asparagine and threonine residues in the large extracellular loop, and glycosylation, to agonist action at human P2X1 receptors was tested by generating alanine substitution mutants.
16371009	5	40	theme	longer	897:902	arg1	agonists					865:872	the partial agonists	853:872	the partial agonists BzATP and Ap5A	853:887	For T186A and N290A, the partial agonists BzATP and Ap5A were no longer agonists but still bind to the receptor as shown by the ability to modulate the response to co-applied ATP.
16371009	5	40	theme	longer	897:902	arg1	agonists					904:911	no longer agonists	894:911	no longer agonists	894:911	For T186A and N290A, the partial agonists BzATP and Ap5A were no longer agonists but still bind to the receptor as shown by the ability to modulate the response to co-applied ATP.
16371009	7	41	theme	ATP	1174:1176	arg1	binding					1178:1184	ATP binding	1174:1184	ATP binding at the P2X1 receptor where the residues F185T186, and the conserved triplet N290F291R292, are likely to play a role in ATP action at the receptor	1174:1330	These results aid in refining a model for ATP binding at the P2X1 receptor where the residues F185T186, and the conserved triplet N290F291R292, are likely to play a role in ATP action at the receptor.
16371009	1	42	from	receptors	303:311	arg1	asparagine					185:194	asparagine	185:194	asparagine	185:194	The role of conserved polar glutamine, asparagine and threonine residues in the large extracellular loop, and glycosylation, to agonist action at human P2X1 receptors was tested by generating alanine substitution mutants.
16371009	1	42	from	receptors	303:311	arg1	threonine					200:208	threonine	200:208	threonine	200:208	The role of conserved polar glutamine, asparagine and threonine residues in the large extracellular loop, and glycosylation, to agonist action at human P2X1 receptors was tested by generating alanine substitution mutants.
16371009	1	42	from	receptors	303:311	arg1	glutamine					174:182	conserved polar glutamine	158:182	conserved polar glutamine	158:182	The role of conserved polar glutamine, asparagine and threonine residues in the large extracellular loop, and glycosylation, to agonist action at human P2X1 receptors was tested by generating alanine substitution mutants.
16371009	1	42	from	receptors	303:311	arg1	glycosylation					256:268	glycosylation	256:268	glycosylation	256:268	The role of conserved polar glutamine, asparagine and threonine residues in the large extracellular loop, and glycosylation, to agonist action at human P2X1 receptors was tested by generating alanine substitution mutants.
16371009	1	42	from	receptors	303:311	arg1	role					150:153	The role	146:153	The role of conserved polar glutamine, asparagine and threonine residues in the large extracellular loop, and glycosylation, to agonist action at human P2X1 receptors	146:311	The role of conserved polar glutamine, asparagine and threonine residues in the large extracellular loop, and glycosylation, to agonist action at human P2X1 receptors was tested by generating alanine substitution mutants.
16371009	4	43	theme	60-fold	784:790	arg1	decreases					792:800	60-fold decreases	784:800	60-fold decreases in ATP potency	784:815	The mutants T186A, N204A and N290A had six-, three- and 60-fold decreases in ATP potency, respectively.
16371009	2	44	dep	Q114A	430:434	arg1	T109A					416:420	T104A, T109A, Q112A, Q114A	409:434	T109A	416:420	For the majority of mutants (Q56A, Q95A, T104A, T109A, Q112A, Q114A, T146A, N153A, T158A, N184A, N191A, N242A, N300A) alanine substitution had no effect on ATP potency.
16371009	2	44	dep	Q114A	430:434	arg1	Q112A					423:427	Q112A	423:427	Q112A	423:427	For the majority of mutants (Q56A, Q95A, T104A, T109A, Q112A, Q114A, T146A, N153A, T158A, N184A, N191A, N242A, N300A) alanine substitution had no effect on ATP potency.
16371009	4	45	theme	ATP	805:807	arg1	potency					809:815	ATP potency	805:815	ATP potency	805:815	The mutants T186A, N204A and N290A had six-, three- and 60-fold decreases in ATP potency, respectively.
16371009	1	46	gly	glycosylation	256:268	arg1	loop					246:249	the large extracellular loop	222:249	the large extracellular loop	222:249	The role of conserved polar glutamine, asparagine and threonine residues in the large extracellular loop, and glycosylation, to agonist action at human P2X1 receptors was tested by generating alanine substitution mutants.
16371009	1	46	gly	glycosylation	256:268	arg1	receptors					303:311	human P2X1 receptors	292:311	human P2X1 receptors	292:311	The role of conserved polar glutamine, asparagine and threonine residues in the large extracellular loop, and glycosylation, to agonist action at human P2X1 receptors was tested by generating alanine substitution mutants.
16371009	1	46	gly	glycosylation	256:268	arg2	receptors					303:311	human P2X1 receptors	292:311	human P2X1 receptors	292:311	The role of conserved polar glutamine, asparagine and threonine residues in the large extracellular loop, and glycosylation, to agonist action at human P2X1 receptors was tested by generating alanine substitution mutants.
16371009	0	47	theme	asparagine	43:52	arg1	residues					68:75	conserved polar glutamine, asparagine and threonine residues	16:75	conserved polar glutamine, asparagine and threonine residues	16:75	Contribution of conserved polar glutamine, asparagine and threonine residues and glycosylation to agonist action at human P2X1 receptors for ATP.
16371009	1	48	theme	human	292:296	arg1	receptors					303:311	human P2X1 receptors	292:311	human P2X1 receptors	292:311	The role of conserved polar glutamine, asparagine and threonine residues in the large extracellular loop, and glycosylation, to agonist action at human P2X1 receptors was tested by generating alanine substitution mutants.
16371009	5	49	theme	partial	857:863	arg1	agonists					865:872	the partial agonists	853:872	the partial agonists BzATP and Ap5A	853:887	For T186A and N290A, the partial agonists BzATP and Ap5A were no longer agonists but still bind to the receptor as shown by the ability to modulate the response to co-applied ATP.
16371009	5	49	theme	partial	857:863	arg1	Ap5A					884:887	Ap5A	884:887	Ap5A	884:887	For T186A and N290A, the partial agonists BzATP and Ap5A were no longer agonists but still bind to the receptor as shown by the ability to modulate the response to co-applied ATP.
16371009	5	49	theme	partial	857:863	arg1	BzATP					874:878	BzATP	874:878	BzATP	874:878	For T186A and N290A, the partial agonists BzATP and Ap5A were no longer agonists but still bind to the receptor as shown by the ability to modulate the response to co-applied ATP.
16371009	5	49	theme	partial	857:863	arg1	agonists					904:911	no longer agonists	894:911	no longer agonists	894:911	For T186A and N290A, the partial agonists BzATP and Ap5A were no longer agonists but still bind to the receptor as shown by the ability to modulate the response to co-applied ATP.
16371009	4	50	dep	mutants	732:738	arg1	N290A					757:761	N290A	757:761	N290A	757:761	The mutants T186A, N204A and N290A had six-, three- and 60-fold decreases in ATP potency, respectively.
16371009	4	50	dep	mutants	732:738	arg1	mutants					732:738	The mutants	728:738	The mutants T186A, N204A and N290A	728:761	The mutants T186A, N204A and N290A had six-, three- and 60-fold decreases in ATP potency, respectively.
16371009	4	50	dep	mutants	732:738	arg1	N204A					747:751	N204A	747:751	N204A	747:751	The mutants T186A, N204A and N290A had six-, three- and 60-fold decreases in ATP potency, respectively.
16371009	1	51	theme	P2X1	298:301	arg1	receptors					303:311	human P2X1 receptors	292:311	human P2X1 receptors	292:311	The role of conserved polar glutamine, asparagine and threonine residues in the large extracellular loop, and glycosylation, to agonist action at human P2X1 receptors was tested by generating alanine substitution mutants.
16371009	6	52	theme	complex	1096:1102	arg1	glycosylation					1104:1116	complex glycosylation	1096:1116	complex glycosylation	1096:1116	N153, N184 and N242 are glycosylated in the endoplasmic reticulum and N300 acquires complex glycosylation in the golgi.
16371009	1	53	from	asparagine	185:194	arg1	loop					246:249	the large extracellular loop	222:249	the large extracellular loop	222:249	The role of conserved polar glutamine, asparagine and threonine residues in the large extracellular loop, and glycosylation, to agonist action at human P2X1 receptors was tested by generating alanine substitution mutants.
16371009	3	54	theme	channel	719:725	arg1	gating					705:710	the gating	701:710	the gating of the channel	701:725	The mutants Q95A, Q112A, Q114A and T158A showed changes in efficacy for the partial agonists BzATP and Ap5A, suggesting that these polar residues may contribute to the gating of the channel.
16371009	3	55	theme	polar	668:672	arg1	residues					674:681	these polar residues	662:681	these polar residues	662:681	The mutants Q95A, Q112A, Q114A and T158A showed changes in efficacy for the partial agonists BzATP and Ap5A, suggesting that these polar residues may contribute to the gating of the channel.
16371009	6	56	gly	glycosylated	1036:1047	arg2	N242					1027:1030	N242	1027:1030	N242	1027:1030	N153, N184 and N242 are glycosylated in the endoplasmic reticulum and N300 acquires complex glycosylation in the golgi.
16371009	6	56	gly	glycosylated	1036:1047	arg1	N153					1012:1015	N153	1012:1015	N153	1012:1015	N153, N184 and N242 are glycosylated in the endoplasmic reticulum and N300 acquires complex glycosylation in the golgi.
16371009	6	56	gly	glycosylated	1036:1047	arg1	N184					1018:1021	N184	1018:1021	N184	1018:1021	N153, N184 and N242 are glycosylated in the endoplasmic reticulum and N300 acquires complex glycosylation in the golgi.
16371009	6	56	gly	glycosylated	1036:1047	arg2	N153					1012:1015	N153	1012:1015	N153	1012:1015	N153, N184 and N242 are glycosylated in the endoplasmic reticulum and N300 acquires complex glycosylation in the golgi.
16371009	6	56	gly	glycosylated	1036:1047	arg1	N242					1027:1030	N242	1027:1030	N242	1027:1030	N153, N184 and N242 are glycosylated in the endoplasmic reticulum and N300 acquires complex glycosylation in the golgi.
16371009	6	56	gly	glycosylated	1036:1047	arg1	reticulum					1068:1076	the endoplasmic reticulum	1052:1076	the endoplasmic reticulum	1052:1076	N153, N184 and N242 are glycosylated in the endoplasmic reticulum and N300 acquires complex glycosylation in the golgi.
16371009	6	56	gly	glycosylated	1036:1047	arg2	N184					1018:1021	N184	1018:1021	N184	1018:1021	N153, N184 and N242 are glycosylated in the endoplasmic reticulum and N300 acquires complex glycosylation in the golgi.
16371009	0	57	from	receptors	127:135	arg1	action					106:111	agonist action	98:111	agonist action at human P2X1 receptors for ATP	98:143	Contribution of conserved polar glutamine, asparagine and threonine residues and glycosylation to agonist action at human P2X1 receptors for ATP.
16371009	0	58	theme	residues	68:75	arg1	Contribution					0:11	Contribution	0:11	Contribution of conserved polar glutamine, asparagine and threonine residues	0:75	Contribution of conserved polar glutamine, asparagine and threonine residues and glycosylation to agonist action at human P2X1 receptors for ATP.
16371009	0	58	theme	residues	68:75	arg1	glycosylation					81:93	glycosylation	81:93	glycosylation to agonist action at human P2X1 receptors for ATP	81:143	Contribution of conserved polar glutamine, asparagine and threonine residues and glycosylation to agonist action at human P2X1 receptors for ATP.
16371009	1	59	from	glutamine	174:182	arg1	loop					246:249	the large extracellular loop	222:249	the large extracellular loop	222:249	The role of conserved polar glutamine, asparagine and threonine residues in the large extracellular loop, and glycosylation, to agonist action at human P2X1 receptors was tested by generating alanine substitution mutants.
16371009	2	60	contain	had	507:509	arg1	substitution					494:505	alanine substitution	486:505	alanine substitution	486:505	For the majority of mutants (Q56A, Q95A, T104A, T109A, Q112A, Q114A, T146A, N153A, T158A, N184A, N191A, N242A, N300A) alanine substitution had no effect on ATP potency.
16371009	2	60	contain	had	507:509	arg2	effect					514:519	no effect	511:519	no effect	511:519	For the majority of mutants (Q56A, Q95A, T104A, T109A, Q112A, Q114A, T146A, N153A, T158A, N184A, N191A, N242A, N300A) alanine substitution had no effect on ATP potency.
16371009	0	61	theme	threonine	58:66	arg1	residues					68:75	conserved polar glutamine, asparagine and threonine residues	16:75	conserved polar glutamine, asparagine and threonine residues	16:75	Contribution of conserved polar glutamine, asparagine and threonine residues and glycosylation to agonist action at human P2X1 receptors for ATP.
16371009	1	62	dep	asparagine	185:194	arg1	residues					210:217	residues	210:217	residues	210:217	The role of conserved polar glutamine, asparagine and threonine residues in the large extracellular loop, and glycosylation, to agonist action at human P2X1 receptors was tested by generating alanine substitution mutants.
16371009	7	63	from	receptor	1198:1205	arg1	binding					1178:1184	ATP binding	1174:1184	ATP binding at the P2X1 receptor where the residues F185T186, and the conserved triplet N290F291R292, are likely to play a role in ATP action at the receptor	1174:1330	These results aid in refining a model for ATP binding at the P2X1 receptor where the residues F185T186, and the conserved triplet N290F291R292, are likely to play a role in ATP action at the receptor.
16371009	1	64	theme	large	226:230	arg1	loop					246:249	the large extracellular loop	222:249	the large extracellular loop	222:249	The role of conserved polar glutamine, asparagine and threonine residues in the large extracellular loop, and glycosylation, to agonist action at human P2X1 receptors was tested by generating alanine substitution mutants.
12171601	2	0	dep	[ECL2	457:461	arg1	N222A					504:508	hPAR(2)N222A	497:508	hPAR(2)N222A	497:508	Epitope-tagged wild-type hPAR(2) (wt-hPAR(2)) or hPAR(2) that lacked glycosylation sequons (following site-directed mutagenesis) in either the N-terminus [hPAR(2)N30A (Asn(30)-->Ala)], extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)] or both (hPAR(2)N30A,N222A or hPAR(2)N30A,N222Q) were expressed in the Chinese-hamster ovary (CHO) fibroblast cell line, Pro5.
12171601	2	0	dep	[ECL2	457:461	arg1	-->Ala					519:524	Asn(222)-->Ala	511:524	Asn(222)-->Ala	511:524	Epitope-tagged wild-type hPAR(2) (wt-hPAR(2)) or hPAR(2) that lacked glycosylation sequons (following site-directed mutagenesis) in either the N-terminus [hPAR(2)N30A (Asn(30)-->Ala)], extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)] or both (hPAR(2)N30A,N222A or hPAR(2)N30A,N222Q) were expressed in the Chinese-hamster ovary (CHO) fibroblast cell line, Pro5.
12171601	2	0	dep	[ECL2	457:461	arg1	hPAR					464:467	hPAR(2)N222Q (Asn(222)-->Gln)	464:492	hPAR(2)N222Q (Asn(222)-->Gln)	464:492	Epitope-tagged wild-type hPAR(2) (wt-hPAR(2)) or hPAR(2) that lacked glycosylation sequons (following site-directed mutagenesis) in either the N-terminus [hPAR(2)N30A (Asn(30)-->Ala)], extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)] or both (hPAR(2)N30A,N222A or hPAR(2)N30A,N222Q) were expressed in the Chinese-hamster ovary (CHO) fibroblast cell line, Pro5.
12171601	2	0	dep	[ECL2	457:461	arg1	Asn					478:480	Asn(222)-->Gln	478:491	Asn(222)-->Gln	478:491	Epitope-tagged wild-type hPAR(2) (wt-hPAR(2)) or hPAR(2) that lacked glycosylation sequons (following site-directed mutagenesis) in either the N-terminus [hPAR(2)N30A (Asn(30)-->Ala)], extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)] or both (hPAR(2)N30A,N222A or hPAR(2)N30A,N222Q) were expressed in the Chinese-hamster ovary (CHO) fibroblast cell line, Pro5.
12171601	3	1	theme	N	780:780	arg1	deglycosylation					797:811	N -glycosidase F deglycosylation	780:811	N -glycosidase F deglycosylation	780:811	Western blot analysis of wt-hPAR(2) showed mature wt-hPAR(2) to have a molecular mass of 55-100 kDa, and 33-48 kDa following N -glycosidase F deglycosylation.
12171601	3	2	theme	Western	655:661	arg1	analysis					668:675	Western blot analysis	655:675	Western blot analysis of wt-hPAR(2)	655:689	Western blot analysis of wt-hPAR(2) showed mature wt-hPAR(2) to have a molecular mass of 55-100 kDa, and 33-48 kDa following N -glycosidase F deglycosylation.
12171601	9	3	theme	synthetic	1606:1614	arg1	2					1634:1634	2	1634:1634	2	1634:1634	hPAR(2)N30A,N222Q displayed increased sensitivity towards tryptase, but a loss in sensitivity towards trypsin and the synthetic peptide SLIGRL-NH(2), although this loss in sensitivity towards trypsin and SLIGRL-NH(2) was secondary to changes in cell-surface expression.
12171601	9	3	theme	synthetic	1606:1614	arg1	SLIGRL-NH					1624:1632	the synthetic peptide SLIGRL-NH	1602:1632	the synthetic peptide SLIGRL-NH(2)	1602:1635	hPAR(2)N30A,N222Q displayed increased sensitivity towards tryptase, but a loss in sensitivity towards trypsin and the synthetic peptide SLIGRL-NH(2), although this loss in sensitivity towards trypsin and SLIGRL-NH(2) was secondary to changes in cell-surface expression.
12171601	1	4	gly	glycosylation	150:162	arg1	receptor-2					205:214	human proteinase-activated receptor-2	178:214	human proteinase-activated receptor-2 (hPAR(2)) expression	178:235	We have analysed the role of N-linked glycosylation in regulating human proteinase-activated receptor-2 (hPAR(2)) expression and function.
12171601	1	4	gly	glycosylation	150:162	arg1	hPAR					217:220	hPAR(2)	217:223	hPAR(2)	217:223	We have analysed the role of N-linked glycosylation in regulating human proteinase-activated receptor-2 (hPAR(2)) expression and function.
12171601	5	5	theme	Western	1006:1012	arg1	analysis					1019:1026	Western blot analysis	1006:1026	Western blot analysis	1006:1026	Western blot analysis indicated that both N-linked sites are glycosylated.
12171601	11	6	theme	N-linked	2017:2024	arg1	glycosylation					2026:2038	hPAR(2) N-linked glycosylation	2009:2038	hPAR(2) N-linked glycosylation	2009:2038	We conclude that hPAR(2) N-linked glycosylation and sialylation regulates receptor expression and/or signalling.
12171601	8	7	theme	substitution	1410:1421	arg1	N222Q					1430:1434	the more conservative substitution hPAR(2)N222Q	1388:1434	the more conservative substitution hPAR(2)N222Q	1388:1434	However, further analysis revealed receptor sensitivity to alanine mutations in this domain, as the more conservative substitution hPAR(2)N222Q displayed no change in response to PAR(2) agonists.
12171601	3	8	theme	wt-hPAR	680:686	arg1	analysis					668:675	Western blot analysis	655:675	Western blot analysis of wt-hPAR(2)	655:689	Western blot analysis of wt-hPAR(2) showed mature wt-hPAR(2) to have a molecular mass of 55-100 kDa, and 33-48 kDa following N -glycosidase F deglycosylation.
12171601	5	9	link	N-linked	1048:1055	arg1	sites					1057:1061	both N-linked sites	1043:1061	both N-linked sites	1043:1061	Western blot analysis indicated that both N-linked sites are glycosylated.
12171601	9	10	from	loss	1652:1655	arg1	sensitivity					1660:1670	sensitivity	1660:1670	sensitivity towards trypsin and SLIGRL-NH(2)	1660:1703	hPAR(2)N30A,N222Q displayed increased sensitivity towards tryptase, but a loss in sensitivity towards trypsin and the synthetic peptide SLIGRL-NH(2), although this loss in sensitivity towards trypsin and SLIGRL-NH(2) was secondary to changes in cell-surface expression.
12171601	2	11	theme	Epitope-tagged	251:264	arg1	hPAR					276:279	Epitope-tagged wild-type hPAR	251:279	Epitope-tagged wild-type hPAR(2) (wt-hPAR(2))	251:295	Epitope-tagged wild-type hPAR(2) (wt-hPAR(2)) or hPAR(2) that lacked glycosylation sequons (following site-directed mutagenesis) in either the N-terminus [hPAR(2)N30A (Asn(30)-->Ala)], extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)] or both (hPAR(2)N30A,N222A or hPAR(2)N30A,N222Q) were expressed in the Chinese-hamster ovary (CHO) fibroblast cell line, Pro5.
12171601	2	11	theme	Epitope-tagged	251:264	arg1	2					281:281	2	281:281	2	281:281	Epitope-tagged wild-type hPAR(2) (wt-hPAR(2)) or hPAR(2) that lacked glycosylation sequons (following site-directed mutagenesis) in either the N-terminus [hPAR(2)N30A (Asn(30)-->Ala)], extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)] or both (hPAR(2)N30A,N222A or hPAR(2)N30A,N222Q) were expressed in the Chinese-hamster ovary (CHO) fibroblast cell line, Pro5.
12171601	2	11	theme	Epitope-tagged	251:264	arg1	wt-hPAR					285:291	wt-hPAR(2)	285:294	wt-hPAR(2)	285:294	Epitope-tagged wild-type hPAR(2) (wt-hPAR(2)) or hPAR(2) that lacked glycosylation sequons (following site-directed mutagenesis) in either the N-terminus [hPAR(2)N30A (Asn(30)-->Ala)], extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)] or both (hPAR(2)N30A,N222A or hPAR(2)N30A,N222Q) were expressed in the Chinese-hamster ovary (CHO) fibroblast cell line, Pro5.
12171601	6	12	theme	hPAR	1104:1107	arg1	N30A					1111:1114	hPAR(2)N30A	1104:1114	hPAR(2)N30A	1104:1114	In functional studies, hPAR(2)N30A displayed a selective and significant increase in sensitivity towards tryptase.
12171601	1	13	theme	human	178:182	arg1	receptor-2					205:214	human proteinase-activated receptor-2	178:214	human proteinase-activated receptor-2 (hPAR(2)) expression	178:235	We have analysed the role of N-linked glycosylation in regulating human proteinase-activated receptor-2 (hPAR(2)) expression and function.
12171601	1	13	theme	human	178:182	arg1	hPAR					217:220	hPAR(2)	217:223	hPAR(2)	217:223	We have analysed the role of N-linked glycosylation in regulating human proteinase-activated receptor-2 (hPAR(2)) expression and function.
12171601	9	14	dep	hPAR	1488:1491	arg1	N222Q					1500:1504	N222Q	1500:1504	N222Q	1500:1504	hPAR(2)N30A,N222Q displayed increased sensitivity towards tryptase, but a loss in sensitivity towards trypsin and the synthetic peptide SLIGRL-NH(2), although this loss in sensitivity towards trypsin and SLIGRL-NH(2) was secondary to changes in cell-surface expression.
12171601	9	14	dep	hPAR	1488:1491	arg1	2					1493:1493	2	1493:1493	2	1493:1493	hPAR(2)N30A,N222Q displayed increased sensitivity towards tryptase, but a loss in sensitivity towards trypsin and the synthetic peptide SLIGRL-NH(2), although this loss in sensitivity towards trypsin and SLIGRL-NH(2) was secondary to changes in cell-surface expression.
12171601	1	15	theme	receptor-2	205:214	arg1	expression					226:235	human proteinase-activated receptor-2 (hPAR(2)) expression	178:235	human proteinase-activated receptor-2 (hPAR(2)) expression	178:235	We have analysed the role of N-linked glycosylation in regulating human proteinase-activated receptor-2 (hPAR(2)) expression and function.
12171601	2	16	dep	hPAR	464:467	arg1	N222Q					471:475	N222Q	471:475	N222Q	471:475	Epitope-tagged wild-type hPAR(2) (wt-hPAR(2)) or hPAR(2) that lacked glycosylation sequons (following site-directed mutagenesis) in either the N-terminus [hPAR(2)N30A (Asn(30)-->Ala)], extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)] or both (hPAR(2)N30A,N222A or hPAR(2)N30A,N222Q) were expressed in the Chinese-hamster ovary (CHO) fibroblast cell line, Pro5.
12171601	2	16	dep	hPAR	464:467	arg1	2					469:469	2	469:469	2	469:469	Epitope-tagged wild-type hPAR(2) (wt-hPAR(2)) or hPAR(2) that lacked glycosylation sequons (following site-directed mutagenesis) in either the N-terminus [hPAR(2)N30A (Asn(30)-->Ala)], extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)] or both (hPAR(2)N30A,N222A or hPAR(2)N30A,N222Q) were expressed in the Chinese-hamster ovary (CHO) fibroblast cell line, Pro5.
12171601	7	17	theme	hPAR	1211:1214	arg1	N222A					1218:1222	hPAR(2)N222A	1211:1222	hPAR(2)N222A	1211:1222	Interestingly, hPAR(2)N222A displayed a loss in sensitivity towards all PAR(2) agonists tested.
12171601	10	18	theme	sialic-acid-deficient	1781:1801	arg1	wt-hPAR					1803:1809	sialic-acid-deficient wt-hPAR	1781:1809	sialic-acid-deficient wt-hPAR(2) in the CHO Lec2 glycosylation-deficient mutant cell line	1781:1869	Finally, expression of sialic-acid-deficient wt-hPAR(2) in the CHO Lec2 glycosylation-deficient mutant cell line, showed a 40 kDa loss in molecular mass, in addition to a marked and selective increase in sensitivity towards tryptase.
12171601	10	18	theme	sialic-acid-deficient	1781:1801	arg1	2					1811:1811	2	1811:1811	2	1811:1811	Finally, expression of sialic-acid-deficient wt-hPAR(2) in the CHO Lec2 glycosylation-deficient mutant cell line, showed a 40 kDa loss in molecular mass, in addition to a marked and selective increase in sensitivity towards tryptase.
12171601	4	19	dep	decreases	951:959	arg1	wt-hPAR					969:975	wt-hPAR	969:975	wt-hPAR	969:975	FACS analysis and immunocytochemistry of the wt-hPAR(2) and PAR(2) mutant cell lines revealed that removal of both glycosylation sequons decreases (50% of wt-hPAR(2)) cell surface expression.
12171601	4	19	dep	decreases	951:959	arg1	%					964:964	50%	962:964	50% of wt-hPAR	962:975	FACS analysis and immunocytochemistry of the wt-hPAR(2) and PAR(2) mutant cell lines revealed that removal of both glycosylation sequons decreases (50% of wt-hPAR(2)) cell surface expression.
12171601	4	20	theme	wt-hPAR	969:975	arg1	wt-hPAR					969:975	wt-hPAR	969:975	wt-hPAR	969:975	FACS analysis and immunocytochemistry of the wt-hPAR(2) and PAR(2) mutant cell lines revealed that removal of both glycosylation sequons decreases (50% of wt-hPAR(2)) cell surface expression.
12171601	4	20	theme	wt-hPAR	969:975	arg1	%					964:964	50%	962:964	50% of wt-hPAR	962:975	FACS analysis and immunocytochemistry of the wt-hPAR(2) and PAR(2) mutant cell lines revealed that removal of both glycosylation sequons decreases (50% of wt-hPAR(2)) cell surface expression.
12171601	2	21	theme	loop	450:453	arg1	[ECL2					457:461	extracellular loop 2 [ECL2	436:461	extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)	436:525	Epitope-tagged wild-type hPAR(2) (wt-hPAR(2)) or hPAR(2) that lacked glycosylation sequons (following site-directed mutagenesis) in either the N-terminus [hPAR(2)N30A (Asn(30)-->Ala)], extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)] or both (hPAR(2)N30A,N222A or hPAR(2)N30A,N222Q) were expressed in the Chinese-hamster ovary (CHO) fibroblast cell line, Pro5.
12171601	7	22	from	loss	1236:1239	arg1	sensitivity					1244:1254	sensitivity	1244:1254	sensitivity towards all PAR(2) agonists tested	1244:1289	Interestingly, hPAR(2)N222A displayed a loss in sensitivity towards all PAR(2) agonists tested.
12171601	8	23	from	mutations	1359:1367	arg1	domain					1377:1382	this domain	1372:1382	this domain	1372:1382	However, further analysis revealed receptor sensitivity to alanine mutations in this domain, as the more conservative substitution hPAR(2)N222Q displayed no change in response to PAR(2) agonists.
12171601	8	24	theme	PAR	1471:1473	arg1	agonists					1478:1485	PAR(2) agonists	1471:1485	PAR(2) agonists	1471:1485	However, further analysis revealed receptor sensitivity to alanine mutations in this domain, as the more conservative substitution hPAR(2)N222Q displayed no change in response to PAR(2) agonists.
12171601	8	25	theme	receptor	1327:1334	arg1	sensitivity					1336:1346	receptor sensitivity	1327:1346	receptor sensitivity to alanine mutations in this domain	1327:1382	However, further analysis revealed receptor sensitivity to alanine mutations in this domain, as the more conservative substitution hPAR(2)N222Q displayed no change in response to PAR(2) agonists.
12171601	10	26	theme	mutant	1854:1859	arg1	line					1866:1869	the CHO Lec2 glycosylation-deficient mutant cell line	1817:1869	the CHO Lec2 glycosylation-deficient mutant cell line	1817:1869	Finally, expression of sialic-acid-deficient wt-hPAR(2) in the CHO Lec2 glycosylation-deficient mutant cell line, showed a 40 kDa loss in molecular mass, in addition to a marked and selective increase in sensitivity towards tryptase.
12171601	2	27	theme	222	515:517	arg1	-->Ala					519:524	Asn(222)-->Ala	511:524	Asn(222)-->Ala	511:524	Epitope-tagged wild-type hPAR(2) (wt-hPAR(2)) or hPAR(2) that lacked glycosylation sequons (following site-directed mutagenesis) in either the N-terminus [hPAR(2)N30A (Asn(30)-->Ala)], extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)] or both (hPAR(2)N30A,N222A or hPAR(2)N30A,N222Q) were expressed in the Chinese-hamster ovary (CHO) fibroblast cell line, Pro5.
12171601	2	27	theme	222	515:517	arg1	hPAR					464:467	hPAR(2)N222Q (Asn(222)-->Gln)	464:492	hPAR(2)N222Q (Asn(222)-->Gln)	464:492	Epitope-tagged wild-type hPAR(2) (wt-hPAR(2)) or hPAR(2) that lacked glycosylation sequons (following site-directed mutagenesis) in either the N-terminus [hPAR(2)N30A (Asn(30)-->Ala)], extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)] or both (hPAR(2)N30A,N222A or hPAR(2)N30A,N222Q) were expressed in the Chinese-hamster ovary (CHO) fibroblast cell line, Pro5.
12171601	9	28	from	changes	1722:1728	arg1	expression					1746:1755	cell-surface expression	1733:1755	cell-surface expression	1733:1755	hPAR(2)N30A,N222Q displayed increased sensitivity towards tryptase, but a loss in sensitivity towards trypsin and the synthetic peptide SLIGRL-NH(2), although this loss in sensitivity towards trypsin and SLIGRL-NH(2) was secondary to changes in cell-surface expression.
12171601	10	29	theme	Lec2	1825:1828	arg1	line					1866:1869	the CHO Lec2 glycosylation-deficient mutant cell line	1817:1869	the CHO Lec2 glycosylation-deficient mutant cell line	1817:1869	Finally, expression of sialic-acid-deficient wt-hPAR(2) in the CHO Lec2 glycosylation-deficient mutant cell line, showed a 40 kDa loss in molecular mass, in addition to a marked and selective increase in sensitivity towards tryptase.
12171601	2	30	theme	Asn	511:513	arg1	-->Ala					519:524	Asn(222)-->Ala	511:524	Asn(222)-->Ala	511:524	Epitope-tagged wild-type hPAR(2) (wt-hPAR(2)) or hPAR(2) that lacked glycosylation sequons (following site-directed mutagenesis) in either the N-terminus [hPAR(2)N30A (Asn(30)-->Ala)], extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)] or both (hPAR(2)N30A,N222A or hPAR(2)N30A,N222Q) were expressed in the Chinese-hamster ovary (CHO) fibroblast cell line, Pro5.
12171601	2	30	theme	Asn	511:513	arg1	hPAR					464:467	hPAR(2)N222Q (Asn(222)-->Gln)	464:492	hPAR(2)N222Q (Asn(222)-->Gln)	464:492	Epitope-tagged wild-type hPAR(2) (wt-hPAR(2)) or hPAR(2) that lacked glycosylation sequons (following site-directed mutagenesis) in either the N-terminus [hPAR(2)N30A (Asn(30)-->Ala)], extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)] or both (hPAR(2)N30A,N222A or hPAR(2)N30A,N222Q) were expressed in the Chinese-hamster ovary (CHO) fibroblast cell line, Pro5.
12171601	4	31	theme	surface	986:992	arg1	expression					994:1003	cell surface expression	981:1003	cell surface expression	981:1003	FACS analysis and immunocytochemistry of the wt-hPAR(2) and PAR(2) mutant cell lines revealed that removal of both glycosylation sequons decreases (50% of wt-hPAR(2)) cell surface expression.
12171601	1	32	theme	N-linked	141:148	arg1	glycosylation					150:162	N-linked glycosylation	141:162	N-linked glycosylation	141:162	We have analysed the role of N-linked glycosylation in regulating human proteinase-activated receptor-2 (hPAR(2)) expression and function.
12171601	2	33	theme	cell	638:641	arg1	Pro5					649:652	Pro5	649:652	Pro5	649:652	Epitope-tagged wild-type hPAR(2) (wt-hPAR(2)) or hPAR(2) that lacked glycosylation sequons (following site-directed mutagenesis) in either the N-terminus [hPAR(2)N30A (Asn(30)-->Ala)], extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)] or both (hPAR(2)N30A,N222A or hPAR(2)N30A,N222Q) were expressed in the Chinese-hamster ovary (CHO) fibroblast cell line, Pro5.
12171601	2	33	theme	cell	638:641	arg1	line					643:646	the Chinese-hamster ovary (CHO) fibroblast cell line	595:646	the Chinese-hamster ovary (CHO) fibroblast cell line	595:646	Epitope-tagged wild-type hPAR(2) (wt-hPAR(2)) or hPAR(2) that lacked glycosylation sequons (following site-directed mutagenesis) in either the N-terminus [hPAR(2)N30A (Asn(30)-->Ala)], extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)] or both (hPAR(2)N30A,N222A or hPAR(2)N30A,N222Q) were expressed in the Chinese-hamster ovary (CHO) fibroblast cell line, Pro5.
12171601	0	34	theme	surface	77:83	arg1	expression					85:94	cell surface expression	72:94	cell surface expression	72:94	Glycosylation of human proteinase-activated receptor-2 (hPAR2): role in cell surface expression and signalling.
12171601	2	35	dep	[hPAR	405:409	arg1	N30A					413:416	N30A	413:416	N30A	413:416	Epitope-tagged wild-type hPAR(2) (wt-hPAR(2)) or hPAR(2) that lacked glycosylation sequons (following site-directed mutagenesis) in either the N-terminus [hPAR(2)N30A (Asn(30)-->Ala)], extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)] or both (hPAR(2)N30A,N222A or hPAR(2)N30A,N222Q) were expressed in the Chinese-hamster ovary (CHO) fibroblast cell line, Pro5.
12171601	2	35	dep	[hPAR	405:409	arg1	2					411:411	2	411:411	2	411:411	Epitope-tagged wild-type hPAR(2) (wt-hPAR(2)) or hPAR(2) that lacked glycosylation sequons (following site-directed mutagenesis) in either the N-terminus [hPAR(2)N30A (Asn(30)-->Ala)], extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)] or both (hPAR(2)N30A,N222A or hPAR(2)N30A,N222Q) were expressed in the Chinese-hamster ovary (CHO) fibroblast cell line, Pro5.
12171601	2	35	dep	[hPAR	405:409	arg1	[ECL2					457:461	extracellular loop 2 [ECL2	436:461	extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)	436:525	Epitope-tagged wild-type hPAR(2) (wt-hPAR(2)) or hPAR(2) that lacked glycosylation sequons (following site-directed mutagenesis) in either the N-terminus [hPAR(2)N30A (Asn(30)-->Ala)], extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)] or both (hPAR(2)N30A,N222A or hPAR(2)N30A,N222Q) were expressed in the Chinese-hamster ovary (CHO) fibroblast cell line, Pro5.
12171601	5	36	gly	glycosylated	1067:1078	arg1	sites					1057:1061	both N-linked sites	1043:1061	both N-linked sites	1043:1061	Western blot analysis indicated that both N-linked sites are glycosylated.
12171601	5	37	theme	N-linked	1048:1055	arg1	sites					1057:1061	both N-linked sites	1043:1061	both N-linked sites	1043:1061	Western blot analysis indicated that both N-linked sites are glycosylated.
12171601	2	38	theme	hPAR	497:500	arg1	N222A					504:508	hPAR(2)N222A	497:508	hPAR(2)N222A	497:508	Epitope-tagged wild-type hPAR(2) (wt-hPAR(2)) or hPAR(2) that lacked glycosylation sequons (following site-directed mutagenesis) in either the N-terminus [hPAR(2)N30A (Asn(30)-->Ala)], extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)] or both (hPAR(2)N30A,N222A or hPAR(2)N30A,N222Q) were expressed in the Chinese-hamster ovary (CHO) fibroblast cell line, Pro5.
12171601	9	39	theme	cell-surface	1733:1744	arg1	expression					1746:1755	cell-surface expression	1733:1755	cell-surface expression	1733:1755	hPAR(2)N30A,N222Q displayed increased sensitivity towards tryptase, but a loss in sensitivity towards trypsin and the synthetic peptide SLIGRL-NH(2), although this loss in sensitivity towards trypsin and SLIGRL-NH(2) was secondary to changes in cell-surface expression.
12171601	10	40	theme	40	1881:1882	arg1	kDa					1884:1886	kDa	1884:1886	kDa	1884:1886	Finally, expression of sialic-acid-deficient wt-hPAR(2) in the CHO Lec2 glycosylation-deficient mutant cell line, showed a 40 kDa loss in molecular mass, in addition to a marked and selective increase in sensitivity towards tryptase.
12171601	2	41	theme	Chinese-hamster	599:613	arg1	Pro5					649:652	Pro5	649:652	Pro5	649:652	Epitope-tagged wild-type hPAR(2) (wt-hPAR(2)) or hPAR(2) that lacked glycosylation sequons (following site-directed mutagenesis) in either the N-terminus [hPAR(2)N30A (Asn(30)-->Ala)], extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)] or both (hPAR(2)N30A,N222A or hPAR(2)N30A,N222Q) were expressed in the Chinese-hamster ovary (CHO) fibroblast cell line, Pro5.
12171601	2	41	theme	Chinese-hamster	599:613	arg1	line					643:646	the Chinese-hamster ovary (CHO) fibroblast cell line	595:646	the Chinese-hamster ovary (CHO) fibroblast cell line	595:646	Epitope-tagged wild-type hPAR(2) (wt-hPAR(2)) or hPAR(2) that lacked glycosylation sequons (following site-directed mutagenesis) in either the N-terminus [hPAR(2)N30A (Asn(30)-->Ala)], extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)] or both (hPAR(2)N30A,N222A or hPAR(2)N30A,N222Q) were expressed in the Chinese-hamster ovary (CHO) fibroblast cell line, Pro5.
12171601	2	42	theme	site-directed	353:365	arg1	mutagenesis					367:377	site-directed mutagenesis	353:377	site-directed mutagenesis	353:377	Epitope-tagged wild-type hPAR(2) (wt-hPAR(2)) or hPAR(2) that lacked glycosylation sequons (following site-directed mutagenesis) in either the N-terminus [hPAR(2)N30A (Asn(30)-->Ala)], extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)] or both (hPAR(2)N30A,N222A or hPAR(2)N30A,N222Q) were expressed in the Chinese-hamster ovary (CHO) fibroblast cell line, Pro5.
12171601	0	43	theme	human	17:21	arg1	hPAR2					56:60	hPAR2	56:60	hPAR2	56:60	Glycosylation of human proteinase-activated receptor-2 (hPAR2): role in cell surface expression and signalling.
12171601	0	43	theme	human	17:21	arg1	receptor-2					44:53	human proteinase-activated receptor-2	17:53	human proteinase-activated receptor-2 (hPAR2)	17:61	Glycosylation of human proteinase-activated receptor-2 (hPAR2): role in cell surface expression and signalling.
12171601	11	44	theme	receptor	2066:2073	arg1	expression					2075:2084	receptor expression	2066:2084	receptor expression	2066:2084	We conclude that hPAR(2) N-linked glycosylation and sialylation regulates receptor expression and/or signalling.
12171601	4	45	theme	mutant	881:886	arg1	lines					893:897	mutant cell lines	881:897	mutant cell lines	881:897	FACS analysis and immunocytochemistry of the wt-hPAR(2) and PAR(2) mutant cell lines revealed that removal of both glycosylation sequons decreases (50% of wt-hPAR(2)) cell surface expression.
12171601	0	46	theme	receptor-2	44:53	arg1	Glycosylation					0:12	Glycosylation	0:12	Glycosylation of human proteinase-activated receptor-2 (hPAR2): role in cell surface expression and signalling.	0:110	Glycosylation of human proteinase-activated receptor-2 (hPAR2): role in cell surface expression and signalling.
12171601	2	47	theme	N-terminus	394:403	arg1	-->Ala					426:431	Asn(30)-->Ala	419:431	Asn(30)-->Ala	419:431	Epitope-tagged wild-type hPAR(2) (wt-hPAR(2)) or hPAR(2) that lacked glycosylation sequons (following site-directed mutagenesis) in either the N-terminus [hPAR(2)N30A (Asn(30)-->Ala)], extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)] or both (hPAR(2)N30A,N222A or hPAR(2)N30A,N222Q) were expressed in the Chinese-hamster ovary (CHO) fibroblast cell line, Pro5.
12171601	2	47	theme	N-terminus	394:403	arg1	[hPAR					405:409	the N-terminus [hPAR(2)N30A (Asn(30)-->Ala)]	390:433	the N-terminus [hPAR(2)N30A (Asn(30)-->Ala)], extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)]	390:526	Epitope-tagged wild-type hPAR(2) (wt-hPAR(2)) or hPAR(2) that lacked glycosylation sequons (following site-directed mutagenesis) in either the N-terminus [hPAR(2)N30A (Asn(30)-->Ala)], extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)] or both (hPAR(2)N30A,N222A or hPAR(2)N30A,N222Q) were expressed in the Chinese-hamster ovary (CHO) fibroblast cell line, Pro5.
12171601	4	48	theme	PAR	874:876	arg1	immunocytochemistry					832:850	immunocytochemistry	832:850	immunocytochemistry	832:850	FACS analysis and immunocytochemistry of the wt-hPAR(2) and PAR(2) mutant cell lines revealed that removal of both glycosylation sequons decreases (50% of wt-hPAR(2)) cell surface expression.
12171601	4	48	theme	PAR	874:876	arg1	analysis					819:826	FACS analysis	814:826	FACS analysis	814:826	FACS analysis and immunocytochemistry of the wt-hPAR(2) and PAR(2) mutant cell lines revealed that removal of both glycosylation sequons decreases (50% of wt-hPAR(2)) cell surface expression.
12171601	3	49	theme	blot	663:666	arg1	analysis					668:675	Western blot analysis	655:675	Western blot analysis of wt-hPAR(2)	655:689	Western blot analysis of wt-hPAR(2) showed mature wt-hPAR(2) to have a molecular mass of 55-100 kDa, and 33-48 kDa following N -glycosidase F deglycosylation.
12171601	10	50	theme	molecular	1896:1904	arg1	mass					1906:1909	molecular mass	1896:1909	molecular mass	1896:1909	Finally, expression of sialic-acid-deficient wt-hPAR(2) in the CHO Lec2 glycosylation-deficient mutant cell line, showed a 40 kDa loss in molecular mass, in addition to a marked and selective increase in sensitivity towards tryptase.
12171601	0	51	dep	Glycosylation	0:12	arg1	role					64:67	role	64:67	Glycosylation of human proteinase-activated receptor-2 (hPAR2): role in cell surface expression and signalling.	0:110	Glycosylation of human proteinase-activated receptor-2 (hPAR2): role in cell surface expression and signalling.
12171601	10	52	from	wt-hPAR	1803:1809	arg1	line					1866:1869	the CHO Lec2 glycosylation-deficient mutant cell line	1817:1869	the CHO Lec2 glycosylation-deficient mutant cell line	1817:1869	Finally, expression of sialic-acid-deficient wt-hPAR(2) in the CHO Lec2 glycosylation-deficient mutant cell line, showed a 40 kDa loss in molecular mass, in addition to a marked and selective increase in sensitivity towards tryptase.
12171601	4	53	theme	glycosylation	929:941	arg1	sequons					943:949	both glycosylation sequons	924:949	both glycosylation sequons	924:949	FACS analysis and immunocytochemistry of the wt-hPAR(2) and PAR(2) mutant cell lines revealed that removal of both glycosylation sequons decreases (50% of wt-hPAR(2)) cell surface expression.
12171601	8	54	theme	conservative	1397:1408	arg1	N222Q					1430:1434	the more conservative substitution hPAR(2)N222Q	1388:1434	the more conservative substitution hPAR(2)N222Q	1388:1434	However, further analysis revealed receptor sensitivity to alanine mutations in this domain, as the more conservative substitution hPAR(2)N222Q displayed no change in response to PAR(2) agonists.
12171601	3	55	theme	-glycosidase	782:793	arg1	deglycosylation					797:811	N -glycosidase F deglycosylation	780:811	N -glycosidase F deglycosylation	780:811	Western blot analysis of wt-hPAR(2) showed mature wt-hPAR(2) to have a molecular mass of 55-100 kDa, and 33-48 kDa following N -glycosidase F deglycosylation.
12171601	4	56	dep	%	964:964	arg1	2					977:977	2	977:977	2	977:977	FACS analysis and immunocytochemistry of the wt-hPAR(2) and PAR(2) mutant cell lines revealed that removal of both glycosylation sequons decreases (50% of wt-hPAR(2)) cell surface expression.
12171601	11	57	link	N-linked	2017:2024	arg1	glycosylation					2026:2038	hPAR(2) N-linked glycosylation	2009:2038	hPAR(2) N-linked glycosylation	2009:2038	We conclude that hPAR(2) N-linked glycosylation and sialylation regulates receptor expression and/or signalling.
12171601	9	58	theme	peptide	1616:1622	arg1	2					1634:1634	2	1634:1634	2	1634:1634	hPAR(2)N30A,N222Q displayed increased sensitivity towards tryptase, but a loss in sensitivity towards trypsin and the synthetic peptide SLIGRL-NH(2), although this loss in sensitivity towards trypsin and SLIGRL-NH(2) was secondary to changes in cell-surface expression.
12171601	9	58	theme	peptide	1616:1622	arg1	SLIGRL-NH					1624:1632	the synthetic peptide SLIGRL-NH	1602:1632	the synthetic peptide SLIGRL-NH(2)	1602:1635	hPAR(2)N30A,N222Q displayed increased sensitivity towards tryptase, but a loss in sensitivity towards trypsin and the synthetic peptide SLIGRL-NH(2), although this loss in sensitivity towards trypsin and SLIGRL-NH(2) was secondary to changes in cell-surface expression.
12171601	8	59	theme	hPAR	1423:1426	arg1	N222Q					1430:1434	the more conservative substitution hPAR(2)N222Q	1388:1434	the more conservative substitution hPAR(2)N222Q	1388:1434	However, further analysis revealed receptor sensitivity to alanine mutations in this domain, as the more conservative substitution hPAR(2)N222Q displayed no change in response to PAR(2) agonists.
12171601	5	60	theme	blot	1014:1017	arg1	analysis					1019:1026	Western blot analysis	1006:1026	Western blot analysis	1006:1026	Western blot analysis indicated that both N-linked sites are glycosylated.
12171601	2	61	theme	wild-type	266:274	arg1	hPAR					276:279	Epitope-tagged wild-type hPAR	251:279	Epitope-tagged wild-type hPAR(2) (wt-hPAR(2))	251:295	Epitope-tagged wild-type hPAR(2) (wt-hPAR(2)) or hPAR(2) that lacked glycosylation sequons (following site-directed mutagenesis) in either the N-terminus [hPAR(2)N30A (Asn(30)-->Ala)], extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)] or both (hPAR(2)N30A,N222A or hPAR(2)N30A,N222Q) were expressed in the Chinese-hamster ovary (CHO) fibroblast cell line, Pro5.
12171601	2	61	theme	wild-type	266:274	arg1	2					281:281	2	281:281	2	281:281	Epitope-tagged wild-type hPAR(2) (wt-hPAR(2)) or hPAR(2) that lacked glycosylation sequons (following site-directed mutagenesis) in either the N-terminus [hPAR(2)N30A (Asn(30)-->Ala)], extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)] or both (hPAR(2)N30A,N222A or hPAR(2)N30A,N222Q) were expressed in the Chinese-hamster ovary (CHO) fibroblast cell line, Pro5.
12171601	2	61	theme	wild-type	266:274	arg1	wt-hPAR					285:291	wt-hPAR(2)	285:294	wt-hPAR(2)	285:294	Epitope-tagged wild-type hPAR(2) (wt-hPAR(2)) or hPAR(2) that lacked glycosylation sequons (following site-directed mutagenesis) in either the N-terminus [hPAR(2)N30A (Asn(30)-->Ala)], extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)] or both (hPAR(2)N30A,N222A or hPAR(2)N30A,N222Q) were expressed in the Chinese-hamster ovary (CHO) fibroblast cell line, Pro5.
12171601	1	62	theme	glycosylation	150:162	arg1	role					133:136	the role	129:136	the role of N-linked glycosylation in regulating human proteinase-activated receptor-2 (hPAR(2)) expression and function	129:248	We have analysed the role of N-linked glycosylation in regulating human proteinase-activated receptor-2 (hPAR(2)) expression and function.
12171601	8	63	dep	agonists	1478:1485	arg1	response					1459:1466	response	1459:1466	response	1459:1466	However, further analysis revealed receptor sensitivity to alanine mutations in this domain, as the more conservative substitution hPAR(2)N222Q displayed no change in response to PAR(2) agonists.
12171601	10	64	from	expression	1767:1776	arg1	line					1866:1869	the CHO Lec2 glycosylation-deficient mutant cell line	1817:1869	the CHO Lec2 glycosylation-deficient mutant cell line	1817:1869	Finally, expression of sialic-acid-deficient wt-hPAR(2) in the CHO Lec2 glycosylation-deficient mutant cell line, showed a 40 kDa loss in molecular mass, in addition to a marked and selective increase in sensitivity towards tryptase.
12171601	1	65	theme	proteinase-activated	184:203	arg1	receptor-2					205:214	human proteinase-activated receptor-2	178:214	human proteinase-activated receptor-2 (hPAR(2)) expression	178:235	We have analysed the role of N-linked glycosylation in regulating human proteinase-activated receptor-2 (hPAR(2)) expression and function.
12171601	1	65	theme	proteinase-activated	184:203	arg1	hPAR					217:220	hPAR(2)	217:223	hPAR(2)	217:223	We have analysed the role of N-linked glycosylation in regulating human proteinase-activated receptor-2 (hPAR(2)) expression and function.
12171601	10	66	theme	wt-hPAR	1803:1809	arg1	expression					1767:1776	expression	1767:1776	expression	1767:1776	Finally, expression of sialic-acid-deficient wt-hPAR(2) in the CHO Lec2 glycosylation-deficient mutant cell line, showed a 40 kDa loss in molecular mass, in addition to a marked and selective increase in sensitivity towards tryptase.
12171601	10	67	theme	selective	1940:1948	arg1	increase					1950:1957	a marked and selective increase	1927:1957	a marked and selective increase in sensitivity towards tryptase	1927:1989	Finally, expression of sialic-acid-deficient wt-hPAR(2) in the CHO Lec2 glycosylation-deficient mutant cell line, showed a 40 kDa loss in molecular mass, in addition to a marked and selective increase in sensitivity towards tryptase.
12171601	6	68	theme	functional	1084:1093	arg1	studies					1095:1101	functional studies	1084:1101	functional studies	1084:1101	In functional studies, hPAR(2)N30A displayed a selective and significant increase in sensitivity towards tryptase.
12171601	0	69	from	role	64:67	arg1	expression					85:94	cell surface expression	72:94	cell surface expression	72:94	Glycosylation of human proteinase-activated receptor-2 (hPAR2): role in cell surface expression and signalling.
12171601	0	69	from	role	64:67	arg1	signalling					100:109	signalling	100:109	signalling	100:109	Glycosylation of human proteinase-activated receptor-2 (hPAR2): role in cell surface expression and signalling.
12171601	4	70	theme	FACS	814:817	arg1	analysis					819:826	FACS analysis	814:826	FACS analysis	814:826	FACS analysis and immunocytochemistry of the wt-hPAR(2) and PAR(2) mutant cell lines revealed that removal of both glycosylation sequons decreases (50% of wt-hPAR(2)) cell surface expression.
12171601	10	71	theme	marked	1929:1934	arg1	increase					1950:1957	a marked and selective increase	1927:1957	a marked and selective increase in sensitivity towards tryptase	1927:1989	Finally, expression of sialic-acid-deficient wt-hPAR(2) in the CHO Lec2 glycosylation-deficient mutant cell line, showed a 40 kDa loss in molecular mass, in addition to a marked and selective increase in sensitivity towards tryptase.
12171601	10	72	dep	increase	1950:1957	arg1	addition					1915:1922	addition	1915:1922	addition	1915:1922	Finally, expression of sialic-acid-deficient wt-hPAR(2) in the CHO Lec2 glycosylation-deficient mutant cell line, showed a 40 kDa loss in molecular mass, in addition to a marked and selective increase in sensitivity towards tryptase.
12171601	6	73	from	increase	1154:1161	arg1	sensitivity					1166:1176	sensitivity	1166:1176	sensitivity towards tryptase	1166:1193	In functional studies, hPAR(2)N30A displayed a selective and significant increase in sensitivity towards tryptase.
12171601	10	74	from	line	1866:1869	arg1	expression					1767:1776	expression	1767:1776	expression	1767:1776	Finally, expression of sialic-acid-deficient wt-hPAR(2) in the CHO Lec2 glycosylation-deficient mutant cell line, showed a 40 kDa loss in molecular mass, in addition to a marked and selective increase in sensitivity towards tryptase.
12171601	6	75	theme	significant	1142:1152	arg1	increase					1154:1161	a selective and significant increase	1126:1161	a selective and significant increase in sensitivity towards tryptase	1126:1193	In functional studies, hPAR(2)N30A displayed a selective and significant increase in sensitivity towards tryptase.
12171601	2	76	theme	extracellular	436:448	arg1	[ECL2					457:461	extracellular loop 2 [ECL2	436:461	extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)	436:525	Epitope-tagged wild-type hPAR(2) (wt-hPAR(2)) or hPAR(2) that lacked glycosylation sequons (following site-directed mutagenesis) in either the N-terminus [hPAR(2)N30A (Asn(30)-->Ala)], extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)] or both (hPAR(2)N30A,N222A or hPAR(2)N30A,N222Q) were expressed in the Chinese-hamster ovary (CHO) fibroblast cell line, Pro5.
12171601	6	77	theme	selective	1128:1136	arg1	increase					1154:1161	a selective and significant increase	1126:1161	a selective and significant increase in sensitivity towards tryptase	1126:1193	In functional studies, hPAR(2)N30A displayed a selective and significant increase in sensitivity towards tryptase.
12171601	10	78	theme	glycosylation-deficient	1830:1852	arg1	line					1866:1869	the CHO Lec2 glycosylation-deficient mutant cell line	1817:1869	the CHO Lec2 glycosylation-deficient mutant cell line	1817:1869	Finally, expression of sialic-acid-deficient wt-hPAR(2) in the CHO Lec2 glycosylation-deficient mutant cell line, showed a 40 kDa loss in molecular mass, in addition to a marked and selective increase in sensitivity towards tryptase.
12171601	10	79	from	increase	1950:1957	arg1	sensitivity					1962:1972	sensitivity	1962:1972	sensitivity towards tryptase	1962:1989	Finally, expression of sialic-acid-deficient wt-hPAR(2) in the CHO Lec2 glycosylation-deficient mutant cell line, showed a 40 kDa loss in molecular mass, in addition to a marked and selective increase in sensitivity towards tryptase.
12171601	9	80	from	loss	1562:1565	arg1	sensitivity					1570:1580	sensitivity	1570:1580	sensitivity towards trypsin and the synthetic peptide SLIGRL-NH(2)	1570:1635	hPAR(2)N30A,N222Q displayed increased sensitivity towards tryptase, but a loss in sensitivity towards trypsin and the synthetic peptide SLIGRL-NH(2), although this loss in sensitivity towards trypsin and SLIGRL-NH(2) was secondary to changes in cell-surface expression.
12171601	0	81	theme	cell	72:75	arg1	expression					85:94	cell surface expression	72:94	cell surface expression	72:94	Glycosylation of human proteinase-activated receptor-2 (hPAR2): role in cell surface expression and signalling.
12171601	10	82	theme	CHO	1821:1823	arg1	line					1866:1869	the CHO Lec2 glycosylation-deficient mutant cell line	1817:1869	the CHO Lec2 glycosylation-deficient mutant cell line	1817:1869	Finally, expression of sialic-acid-deficient wt-hPAR(2) in the CHO Lec2 glycosylation-deficient mutant cell line, showed a 40 kDa loss in molecular mass, in addition to a marked and selective increase in sensitivity towards tryptase.
12171601	10	83	from	loss	1888:1891	arg1	mass					1906:1909	molecular mass	1896:1909	molecular mass	1896:1909	Finally, expression of sialic-acid-deficient wt-hPAR(2) in the CHO Lec2 glycosylation-deficient mutant cell line, showed a 40 kDa loss in molecular mass, in addition to a marked and selective increase in sensitivity towards tryptase.
12171601	4	84	theme	cell	981:984	arg1	expression					994:1003	cell surface expression	981:1003	cell surface expression	981:1003	FACS analysis and immunocytochemistry of the wt-hPAR(2) and PAR(2) mutant cell lines revealed that removal of both glycosylation sequons decreases (50% of wt-hPAR(2)) cell surface expression.
12171601	8	85	theme	alanine	1351:1357	arg1	mutations					1359:1367	alanine mutations	1351:1367	alanine mutations in this domain	1351:1382	However, further analysis revealed receptor sensitivity to alanine mutations in this domain, as the more conservative substitution hPAR(2)N222Q displayed no change in response to PAR(2) agonists.
12171601	7	86	theme	PAR	1268:1270	arg1	agonists					1275:1282	all PAR(2) agonists	1264:1282	all PAR(2) agonists tested	1264:1289	Interestingly, hPAR(2)N222A displayed a loss in sensitivity towards all PAR(2) agonists tested.
12171601	4	87	gly	glycosylation	929:941	arg2	sequons					943:949	both glycosylation sequons	924:949	both glycosylation sequons	924:949	FACS analysis and immunocytochemistry of the wt-hPAR(2) and PAR(2) mutant cell lines revealed that removal of both glycosylation sequons decreases (50% of wt-hPAR(2)) cell surface expression.
12171601	3	88	theme	molecular	726:734	arg1	mass					736:739	a molecular mass	724:739	a molecular mass of 55-100 kDa, and 33-48 kDa	724:768	Western blot analysis of wt-hPAR(2) showed mature wt-hPAR(2) to have a molecular mass of 55-100 kDa, and 33-48 kDa following N -glycosidase F deglycosylation.
12171601	2	89	theme	Asn	419:421	arg1	-->Ala					426:431	Asn(30)-->Ala	419:431	Asn(30)-->Ala	419:431	Epitope-tagged wild-type hPAR(2) (wt-hPAR(2)) or hPAR(2) that lacked glycosylation sequons (following site-directed mutagenesis) in either the N-terminus [hPAR(2)N30A (Asn(30)-->Ala)], extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)] or both (hPAR(2)N30A,N222A or hPAR(2)N30A,N222Q) were expressed in the Chinese-hamster ovary (CHO) fibroblast cell line, Pro5.
12171601	2	89	theme	Asn	419:421	arg1	[hPAR					405:409	the N-terminus [hPAR(2)N30A (Asn(30)-->Ala)]	390:433	the N-terminus [hPAR(2)N30A (Asn(30)-->Ala)], extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)]	390:526	Epitope-tagged wild-type hPAR(2) (wt-hPAR(2)) or hPAR(2) that lacked glycosylation sequons (following site-directed mutagenesis) in either the N-terminus [hPAR(2)N30A (Asn(30)-->Ala)], extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)] or both (hPAR(2)N30A,N222A or hPAR(2)N30A,N222Q) were expressed in the Chinese-hamster ovary (CHO) fibroblast cell line, Pro5.
12171601	2	90	gly	glycosylation	320:332	arg2	sequons					334:340	glycosylation sequons	320:340	glycosylation sequons (following site-directed mutagenesis)	320:378	Epitope-tagged wild-type hPAR(2) (wt-hPAR(2)) or hPAR(2) that lacked glycosylation sequons (following site-directed mutagenesis) in either the N-terminus [hPAR(2)N30A (Asn(30)-->Ala)], extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)] or both (hPAR(2)N30A,N222A or hPAR(2)N30A,N222Q) were expressed in the Chinese-hamster ovary (CHO) fibroblast cell line, Pro5.
12171601	9	91	theme	increased	1516:1524	arg1	sensitivity					1526:1536	increased sensitivity	1516:1536	increased sensitivity towards tryptase	1516:1553	hPAR(2)N30A,N222Q displayed increased sensitivity towards tryptase, but a loss in sensitivity towards trypsin and the synthetic peptide SLIGRL-NH(2), although this loss in sensitivity towards trypsin and SLIGRL-NH(2) was secondary to changes in cell-surface expression.
12171601	10	92	theme	kDa	1884:1886	arg1	loss					1888:1891	a 40 kDa loss	1879:1891	a 40 kDa loss in molecular mass	1879:1909	Finally, expression of sialic-acid-deficient wt-hPAR(2) in the CHO Lec2 glycosylation-deficient mutant cell line, showed a 40 kDa loss in molecular mass, in addition to a marked and selective increase in sensitivity towards tryptase.
12171601	2	93	theme	ovary	615:619	arg1	Pro5					649:652	Pro5	649:652	Pro5	649:652	Epitope-tagged wild-type hPAR(2) (wt-hPAR(2)) or hPAR(2) that lacked glycosylation sequons (following site-directed mutagenesis) in either the N-terminus [hPAR(2)N30A (Asn(30)-->Ala)], extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)] or both (hPAR(2)N30A,N222A or hPAR(2)N30A,N222Q) were expressed in the Chinese-hamster ovary (CHO) fibroblast cell line, Pro5.
12171601	2	93	theme	ovary	615:619	arg1	line					643:646	the Chinese-hamster ovary (CHO) fibroblast cell line	595:646	the Chinese-hamster ovary (CHO) fibroblast cell line	595:646	Epitope-tagged wild-type hPAR(2) (wt-hPAR(2)) or hPAR(2) that lacked glycosylation sequons (following site-directed mutagenesis) in either the N-terminus [hPAR(2)N30A (Asn(30)-->Ala)], extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)] or both (hPAR(2)N30A,N222A or hPAR(2)N30A,N222Q) were expressed in the Chinese-hamster ovary (CHO) fibroblast cell line, Pro5.
12171601	8	94	theme	further	1301:1307	arg1	analysis					1309:1316	further analysis	1301:1316	further analysis	1301:1316	However, further analysis revealed receptor sensitivity to alanine mutations in this domain, as the more conservative substitution hPAR(2)N222Q displayed no change in response to PAR(2) agonists.
12171601	4	95	theme	wt-hPAR	859:865	arg1	immunocytochemistry					832:850	immunocytochemistry	832:850	immunocytochemistry	832:850	FACS analysis and immunocytochemistry of the wt-hPAR(2) and PAR(2) mutant cell lines revealed that removal of both glycosylation sequons decreases (50% of wt-hPAR(2)) cell surface expression.
12171601	4	95	theme	wt-hPAR	859:865	arg1	analysis					819:826	FACS analysis	814:826	FACS analysis	814:826	FACS analysis and immunocytochemistry of the wt-hPAR(2) and PAR(2) mutant cell lines revealed that removal of both glycosylation sequons decreases (50% of wt-hPAR(2)) cell surface expression.
12171601	0	96	theme	proteinase-activated	23:42	arg1	hPAR2					56:60	hPAR2	56:60	hPAR2	56:60	Glycosylation of human proteinase-activated receptor-2 (hPAR2): role in cell surface expression and signalling.
12171601	0	96	theme	proteinase-activated	23:42	arg1	receptor-2					44:53	human proteinase-activated receptor-2	17:53	human proteinase-activated receptor-2 (hPAR2)	17:61	Glycosylation of human proteinase-activated receptor-2 (hPAR2): role in cell surface expression and signalling.
12171601	3	97	theme	kDa	751:753	arg1	mass					736:739	a molecular mass	724:739	a molecular mass of 55-100 kDa, and 33-48 kDa	724:768	Western blot analysis of wt-hPAR(2) showed mature wt-hPAR(2) to have a molecular mass of 55-100 kDa, and 33-48 kDa following N -glycosidase F deglycosylation.
12171601	1	98	link	N-linked	141:148	arg1	glycosylation					150:162	N-linked glycosylation	141:162	N-linked glycosylation	141:162	We have analysed the role of N-linked glycosylation in regulating human proteinase-activated receptor-2 (hPAR(2)) expression and function.
12171601	4	99	theme	cell	888:891	arg1	lines					893:897	mutant cell lines	881:897	mutant cell lines	881:897	FACS analysis and immunocytochemistry of the wt-hPAR(2) and PAR(2) mutant cell lines revealed that removal of both glycosylation sequons decreases (50% of wt-hPAR(2)) cell surface expression.
12171601	0	100	gly	Glycosylation	0:12	arg1	hPAR2					56:60	hPAR2	56:60	hPAR2	56:60	Glycosylation of human proteinase-activated receptor-2 (hPAR2): role in cell surface expression and signalling.
12171601	0	100	gly	Glycosylation	0:12	arg1	receptor-2					44:53	human proteinase-activated receptor-2	17:53	human proteinase-activated receptor-2 (hPAR2)	17:61	Glycosylation of human proteinase-activated receptor-2 (hPAR2): role in cell surface expression and signalling.
12171601	2	101	dep	N222A	504:508	arg1	2					502:502	2	502:502	2	502:502	Epitope-tagged wild-type hPAR(2) (wt-hPAR(2)) or hPAR(2) that lacked glycosylation sequons (following site-directed mutagenesis) in either the N-terminus [hPAR(2)N30A (Asn(30)-->Ala)], extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)] or both (hPAR(2)N30A,N222A or hPAR(2)N30A,N222Q) were expressed in the Chinese-hamster ovary (CHO) fibroblast cell line, Pro5.
12171601	2	102	theme	glycosylation	320:332	arg1	sequons					334:340	glycosylation sequons	320:340	glycosylation sequons (following site-directed mutagenesis)	320:378	Epitope-tagged wild-type hPAR(2) (wt-hPAR(2)) or hPAR(2) that lacked glycosylation sequons (following site-directed mutagenesis) in either the N-terminus [hPAR(2)N30A (Asn(30)-->Ala)], extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)] or both (hPAR(2)N30A,N222A or hPAR(2)N30A,N222Q) were expressed in the Chinese-hamster ovary (CHO) fibroblast cell line, Pro5.
12171601	2	103	theme	fibroblast	627:636	arg1	Pro5					649:652	Pro5	649:652	Pro5	649:652	Epitope-tagged wild-type hPAR(2) (wt-hPAR(2)) or hPAR(2) that lacked glycosylation sequons (following site-directed mutagenesis) in either the N-terminus [hPAR(2)N30A (Asn(30)-->Ala)], extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)] or both (hPAR(2)N30A,N222A or hPAR(2)N30A,N222Q) were expressed in the Chinese-hamster ovary (CHO) fibroblast cell line, Pro5.
12171601	2	103	theme	fibroblast	627:636	arg1	line					643:646	the Chinese-hamster ovary (CHO) fibroblast cell line	595:646	the Chinese-hamster ovary (CHO) fibroblast cell line	595:646	Epitope-tagged wild-type hPAR(2) (wt-hPAR(2)) or hPAR(2) that lacked glycosylation sequons (following site-directed mutagenesis) in either the N-terminus [hPAR(2)N30A (Asn(30)-->Ala)], extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)] or both (hPAR(2)N30A,N222A or hPAR(2)N30A,N222Q) were expressed in the Chinese-hamster ovary (CHO) fibroblast cell line, Pro5.
12171601	2	104	dep	sequons	334:340	arg1	following					343:351	following	343:351	following site-directed mutagenesis	343:377	Epitope-tagged wild-type hPAR(2) (wt-hPAR(2)) or hPAR(2) that lacked glycosylation sequons (following site-directed mutagenesis) in either the N-terminus [hPAR(2)N30A (Asn(30)-->Ala)], extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)] or both (hPAR(2)N30A,N222A or hPAR(2)N30A,N222Q) were expressed in the Chinese-hamster ovary (CHO) fibroblast cell line, Pro5.
12171601	10	105	theme	cell	1861:1864	arg1	line					1866:1869	the CHO Lec2 glycosylation-deficient mutant cell line	1817:1869	the CHO Lec2 glycosylation-deficient mutant cell line	1817:1869	Finally, expression of sialic-acid-deficient wt-hPAR(2) in the CHO Lec2 glycosylation-deficient mutant cell line, showed a 40 kDa loss in molecular mass, in addition to a marked and selective increase in sensitivity towards tryptase.
12171601	3	106	theme	kDa	766:768	arg1	mass					736:739	a molecular mass	724:739	a molecular mass of 55-100 kDa, and 33-48 kDa	724:768	Western blot analysis of wt-hPAR(2) showed mature wt-hPAR(2) to have a molecular mass of 55-100 kDa, and 33-48 kDa following N -glycosidase F deglycosylation.
12171601	2	107	theme	CHO	622:624	arg1	Pro5					649:652	Pro5	649:652	Pro5	649:652	Epitope-tagged wild-type hPAR(2) (wt-hPAR(2)) or hPAR(2) that lacked glycosylation sequons (following site-directed mutagenesis) in either the N-terminus [hPAR(2)N30A (Asn(30)-->Ala)], extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)] or both (hPAR(2)N30A,N222A or hPAR(2)N30A,N222Q) were expressed in the Chinese-hamster ovary (CHO) fibroblast cell line, Pro5.
12171601	2	107	theme	CHO	622:624	arg1	line					643:646	the Chinese-hamster ovary (CHO) fibroblast cell line	595:646	the Chinese-hamster ovary (CHO) fibroblast cell line	595:646	Epitope-tagged wild-type hPAR(2) (wt-hPAR(2)) or hPAR(2) that lacked glycosylation sequons (following site-directed mutagenesis) in either the N-terminus [hPAR(2)N30A (Asn(30)-->Ala)], extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)] or both (hPAR(2)N30A,N222A or hPAR(2)N30A,N222Q) were expressed in the Chinese-hamster ovary (CHO) fibroblast cell line, Pro5.
12171601	4	108	dep	wt-hPAR	859:865	arg1	lines					893:897	mutant cell lines	881:897	mutant cell lines	881:897	FACS analysis and immunocytochemistry of the wt-hPAR(2) and PAR(2) mutant cell lines revealed that removal of both glycosylation sequons decreases (50% of wt-hPAR(2)) cell surface expression.
12171601	2	109	dep	hPAR	537:540	arg1	2					542:542	2	542:542	2	542:542	Epitope-tagged wild-type hPAR(2) (wt-hPAR(2)) or hPAR(2) that lacked glycosylation sequons (following site-directed mutagenesis) in either the N-terminus [hPAR(2)N30A (Asn(30)-->Ala)], extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)] or both (hPAR(2)N30A,N222A or hPAR(2)N30A,N222Q) were expressed in the Chinese-hamster ovary (CHO) fibroblast cell line, Pro5.
12171601	2	109	dep	hPAR	537:540	arg1	N222Q					570:574	N222Q	570:574	N222Q	570:574	Epitope-tagged wild-type hPAR(2) (wt-hPAR(2)) or hPAR(2) that lacked glycosylation sequons (following site-directed mutagenesis) in either the N-terminus [hPAR(2)N30A (Asn(30)-->Ala)], extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)] or both (hPAR(2)N30A,N222A or hPAR(2)N30A,N222Q) were expressed in the Chinese-hamster ovary (CHO) fibroblast cell line, Pro5.
12171601	2	109	dep	hPAR	537:540	arg1	N222A					549:553	N222A	549:553	N222A	549:553	Epitope-tagged wild-type hPAR(2) (wt-hPAR(2)) or hPAR(2) that lacked glycosylation sequons (following site-directed mutagenesis) in either the N-terminus [hPAR(2)N30A (Asn(30)-->Ala)], extracellular loop 2 [ECL2; hPAR(2)N222Q (Asn(222)-->Gln) or hPAR(2)N222A (Asn(222)-->Ala)] or both (hPAR(2)N30A,N222A or hPAR(2)N30A,N222Q) were expressed in the Chinese-hamster ovary (CHO) fibroblast cell line, Pro5.
12171601	3	110	theme	F	795:795	arg1	deglycosylation					797:811	N -glycosidase F deglycosylation	780:811	N -glycosidase F deglycosylation	780:811	Western blot analysis of wt-hPAR(2) showed mature wt-hPAR(2) to have a molecular mass of 55-100 kDa, and 33-48 kDa following N -glycosidase F deglycosylation.
12171601	11	111	theme	hPAR	2009:2012	arg1	glycosylation					2026:2038	hPAR(2) N-linked glycosylation	2009:2038	hPAR(2) N-linked glycosylation	2009:2038	We conclude that hPAR(2) N-linked glycosylation and sialylation regulates receptor expression and/or signalling.
12171601	4	112	theme	sequons	943:949	arg1	removal					913:919	removal	913:919	removal of both glycosylation sequons	913:949	FACS analysis and immunocytochemistry of the wt-hPAR(2) and PAR(2) mutant cell lines revealed that removal of both glycosylation sequons decreases (50% of wt-hPAR(2)) cell surface expression.
11069924	6	0	with	doublet	929:935	arg1	glycans					969:975	six or seven N-linked core glycans	942:975	six or seven N-linked core glycans	942:975	However, glycosylation at Asn-290 (Asn-Gly-Thr-Pro) was suppressed, particularly when translation proceeded rapidly, producing a protein doublet with six or seven N-linked core glycans.
11069924	9	1	link	N-linked	1464:1471	arg1	glycosylation					1473:1485	tyrosinase N-linked glycosylation	1453:1485	tyrosinase N-linked glycosylation	1453:1485	Therefore, the rate of protein translation can regulate the level of tyrosinase N-linked glycosylation, as well as other potential cotranslational maturation events.
11069924	5	2	used	utilized	762:769	arg2	sites					752:756	all seven N-linked consensus sites	723:756	all seven N-linked consensus sites	723:756	Site-directed mutagenesis revealed that all seven N-linked consensus sites are utilized in human tyrosinase.
11069924	2	3	theme	ubiquitin-proteasomal	334:354	arg1	pathway					356:362	the cytosolic ubiquitin-proteasomal pathway	320:362	the cytosolic ubiquitin-proteasomal pathway	320:362	Mutations in tyrosinase lead to albinism due, at least in part, to aberrant retention of the protein in the endoplasmic reticulum and subsequent degradation by the cytosolic ubiquitin-proteasomal pathway.
11069924	9	4	theme	potential	1505:1513	arg1	events					1542:1547	other potential cotranslational maturation events	1499:1547	other potential cotranslational maturation events	1499:1547	Therefore, the rate of protein translation can regulate the level of tyrosinase N-linked glycosylation, as well as other potential cotranslational maturation events.
11069924	4	5	theme	normal	587:592	arg1	melanocytes					594:604	normal melanocytes	587:604	normal melanocytes	587:604	To understand critical cotranslational events, the glycosylation and rate of translation of tyrosinase was studied in normal melanocytes, melanoma cells, an in vitro cell-free system, and semi-permeabilized cells.
11069924	7	6	dep	2-3-fold	1101:1108	arg1	faster					1110:1115	faster	1110:1115	faster	1110:1115	The inefficient glycosylation of Asn-290, due to the presence of a proximal Pro, was enhanced in melanoma cells possessing 2-3-fold faster (7.7-10.0 amino acids/s) protein translation rates compared with normal melanocytes (3.5 amino acids/s).
11069924	7	6	dep	2-3-fold	1101:1108	arg1	acids/s					1133:1139	7.7-10.0 amino acids/s	1118:1139	7.7-10.0 amino acids/s	1118:1139	The inefficient glycosylation of Asn-290, due to the presence of a proximal Pro, was enhanced in melanoma cells possessing 2-3-fold faster (7.7-10.0 amino acids/s) protein translation rates compared with normal melanocytes (3.5 amino acids/s).
11069924	2	7	from	degradation	305:315	arg1	part					218:221	part	218:221	part	218:221	Mutations in tyrosinase lead to albinism due, at least in part, to aberrant retention of the protein in the endoplasmic reticulum and subsequent degradation by the cytosolic ubiquitin-proteasomal pathway.
11069924	2	7	from	degradation	305:315	arg1	reticulum					280:288	the endoplasmic reticulum	264:288	the endoplasmic reticulum	264:288	Mutations in tyrosinase lead to albinism due, at least in part, to aberrant retention of the protein in the endoplasmic reticulum and subsequent degradation by the cytosolic ubiquitin-proteasomal pathway.
11069924	8	8	theme	cell-free	1366:1374	arg1	system					1376:1381	the cell-free system	1362:1381	the cell-free system	1362:1381	Slowing the translation rate with the protein synthesis inhibitor cycloheximide increased the glycosylation efficiency in live cells and in the cell-free system.
11069924	2	9	theme	endoplasmic	268:278	arg1	reticulum					280:288	the endoplasmic reticulum	264:288	the endoplasmic reticulum	264:288	Mutations in tyrosinase lead to albinism due, at least in part, to aberrant retention of the protein in the endoplasmic reticulum and subsequent degradation by the cytosolic ubiquitin-proteasomal pathway.
11069924	4	10	theme	melanoma	607:614	arg1	cells					616:620	melanoma cells	607:620	melanoma cells	607:620	To understand critical cotranslational events, the glycosylation and rate of translation of tyrosinase was studied in normal melanocytes, melanoma cells, an in vitro cell-free system, and semi-permeabilized cells.
11069924	7	11	theme	amino	1206:1210	arg1	acids/s					1212:1218	3.5 amino acids/s	1202:1218	3.5 amino acids/s	1202:1218	The inefficient glycosylation of Asn-290, due to the presence of a proximal Pro, was enhanced in melanoma cells possessing 2-3-fold faster (7.7-10.0 amino acids/s) protein translation rates compared with normal melanocytes (3.5 amino acids/s).
11069924	7	11	theme	amino	1206:1210	arg1	melanocytes					1189:1199	normal melanocytes	1182:1199	normal melanocytes (3.5 amino acids/s)	1182:1219	The inefficient glycosylation of Asn-290, due to the presence of a proximal Pro, was enhanced in melanoma cells possessing 2-3-fold faster (7.7-10.0 amino acids/s) protein translation rates compared with normal melanocytes (3.5 amino acids/s).
11069924	4	12	theme	critical	483:490	arg1	events					508:513	critical cotranslational events	483:513	critical cotranslational events	483:513	To understand critical cotranslational events, the glycosylation and rate of translation of tyrosinase was studied in normal melanocytes, melanoma cells, an in vitro cell-free system, and semi-permeabilized cells.
11069924	7	13	theme	amino	1127:1131	arg1	acids/s					1133:1139	7.7-10.0 amino acids/s	1118:1139	7.7-10.0 amino acids/s	1118:1139	The inefficient glycosylation of Asn-290, due to the presence of a proximal Pro, was enhanced in melanoma cells possessing 2-3-fold faster (7.7-10.0 amino acids/s) protein translation rates compared with normal melanocytes (3.5 amino acids/s).
11069924	9	14	theme	translation	1415:1425	arg1	rate					1399:1402	the rate	1395:1402	the rate of protein translation	1395:1425	Therefore, the rate of protein translation can regulate the level of tyrosinase N-linked glycosylation, as well as other potential cotranslational maturation events.
11069924	1	15	theme	membrane	105:112	arg1	Tyrosinase					82:91	Tyrosinase	82:91	Tyrosinase	82:91	Tyrosinase is a type I membrane glycoprotein essential for melanin synthesis.
11069924	1	15	theme	membrane	105:112	arg1	glycoprotein					114:125	a type I membrane glycoprotein	96:125	a type I membrane glycoprotein essential for melanin synthesis	96:157	Tyrosinase is a type I membrane glycoprotein essential for melanin synthesis.
11069924	7	16	theme	inefficient	982:992	arg1	glycosylation					994:1006	The inefficient glycosylation	978:1006	The inefficient glycosylation	978:1006	The inefficient glycosylation of Asn-290, due to the presence of a proximal Pro, was enhanced in melanoma cells possessing 2-3-fold faster (7.7-10.0 amino acids/s) protein translation rates compared with normal melanocytes (3.5 amino acids/s).
11069924	2	17	theme	protein	253:259	arg1	degradation					305:315	subsequent degradation	294:315	subsequent degradation by the cytosolic ubiquitin-proteasomal pathway	294:362	Mutations in tyrosinase lead to albinism due, at least in part, to aberrant retention of the protein in the endoplasmic reticulum and subsequent degradation by the cytosolic ubiquitin-proteasomal pathway.
11069924	2	17	theme	protein	253:259	arg1	retention					236:244	aberrant retention	227:244	aberrant retention of the protein in the endoplasmic reticulum	227:288	Mutations in tyrosinase lead to albinism due, at least in part, to aberrant retention of the protein in the endoplasmic reticulum and subsequent degradation by the cytosolic ubiquitin-proteasomal pathway.
11069924	9	18	theme	glycosylation	1473:1485	arg1	events					1542:1547	other potential cotranslational maturation events	1499:1547	other potential cotranslational maturation events	1499:1547	Therefore, the rate of protein translation can regulate the level of tyrosinase N-linked glycosylation, as well as other potential cotranslational maturation events.
11069924	9	18	theme	glycosylation	1473:1485	arg1	level					1444:1448	the level	1440:1448	the level of tyrosinase N-linked glycosylation	1440:1485	Therefore, the rate of protein translation can regulate the level of tyrosinase N-linked glycosylation, as well as other potential cotranslational maturation events.
11069924	4	19	theme	semi-permeabilized	657:674	arg1	cells					676:680	semi-permeabilized cells	657:680	semi-permeabilized cells	657:680	To understand critical cotranslational events, the glycosylation and rate of translation of tyrosinase was studied in normal melanocytes, melanoma cells, an in vitro cell-free system, and semi-permeabilized cells.
11069924	7	20	theme	protein	1142:1148	arg1	rates					1162:1166	2-3-fold faster (7.7-10.0 amino acids/s) protein translation rates	1101:1166	2-3-fold faster (7.7-10.0 amino acids/s) protein translation rates	1101:1166	The inefficient glycosylation of Asn-290, due to the presence of a proximal Pro, was enhanced in melanoma cells possessing 2-3-fold faster (7.7-10.0 amino acids/s) protein translation rates compared with normal melanocytes (3.5 amino acids/s).
11069924	0	21	link	N-linked	52:59	arg1	level					75:79	its N-linked glycosylation level	48:79	its N-linked glycosylation level	48:79	Translation rate of human tyrosinase determines its N-linked glycosylation level.
11069924	9	22	theme	protein	1407:1413	arg1	translation					1415:1425	protein translation	1407:1425	protein translation	1407:1425	Therefore, the rate of protein translation can regulate the level of tyrosinase N-linked glycosylation, as well as other potential cotranslational maturation events.
11069924	4	23	gly	glycosylation	520:532	arg1	system					645:650	an in vitro cell-free system	623:650	an in vitro cell-free system	623:650	To understand critical cotranslational events, the glycosylation and rate of translation of tyrosinase was studied in normal melanocytes, melanoma cells, an in vitro cell-free system, and semi-permeabilized cells.
11069924	4	23	gly	glycosylation	520:532	arg1	translation					546:556	translation	546:556	translation of tyrosinase	546:570	To understand critical cotranslational events, the glycosylation and rate of translation of tyrosinase was studied in normal melanocytes, melanoma cells, an in vitro cell-free system, and semi-permeabilized cells.
11069924	4	23	gly	glycosylation	520:532	arg1	cells					676:680	semi-permeabilized cells	657:680	semi-permeabilized cells	657:680	To understand critical cotranslational events, the glycosylation and rate of translation of tyrosinase was studied in normal melanocytes, melanoma cells, an in vitro cell-free system, and semi-permeabilized cells.
11069924	4	23	gly	glycosylation	520:532	arg1	melanocytes					594:604	normal melanocytes	587:604	normal melanocytes	587:604	To understand critical cotranslational events, the glycosylation and rate of translation of tyrosinase was studied in normal melanocytes, melanoma cells, an in vitro cell-free system, and semi-permeabilized cells.
11069924	4	23	gly	glycosylation	520:532	arg1	cells					616:620	melanoma cells	607:620	melanoma cells	607:620	To understand critical cotranslational events, the glycosylation and rate of translation of tyrosinase was studied in normal melanocytes, melanoma cells, an in vitro cell-free system, and semi-permeabilized cells.
11069924	3	24	theme	amelanotic	442:451	arg1	cells					462:466	amelanotic melanoma cells	442:466	amelanotic melanoma cells	442:466	A similar premature degradative fate for wild type tyrosinase also occurs in amelanotic melanoma cells.
11069924	3	25	theme	degradative	385:395	arg1	fate					397:400	A similar premature degradative fate	365:400	A similar premature degradative fate for wild type tyrosinase	365:425	A similar premature degradative fate for wild type tyrosinase also occurs in amelanotic melanoma cells.
11069924	4	26	theme	cotranslational	492:506	arg1	events					508:513	critical cotranslational events	483:513	critical cotranslational events	483:513	To understand critical cotranslational events, the glycosylation and rate of translation of tyrosinase was studied in normal melanocytes, melanoma cells, an in vitro cell-free system, and semi-permeabilized cells.
11069924	2	27	theme	subsequent	294:303	arg1	degradation					305:315	subsequent degradation	294:315	subsequent degradation by the cytosolic ubiquitin-proteasomal pathway	294:362	Mutations in tyrosinase lead to albinism due, at least in part, to aberrant retention of the protein in the endoplasmic reticulum and subsequent degradation by the cytosolic ubiquitin-proteasomal pathway.
11069924	6	28	theme	protein	921:927	arg1	doublet					929:935	a protein doublet	919:935	a protein doublet with six or seven N-linked core glycans	919:975	However, glycosylation at Asn-290 (Asn-Gly-Thr-Pro) was suppressed, particularly when translation proceeded rapidly, producing a protein doublet with six or seven N-linked core glycans.
11069924	8	29	theme	protein	1260:1266	arg1	cycloheximide					1288:1300	the protein synthesis inhibitor cycloheximide	1256:1300	the protein synthesis inhibitor cycloheximide	1256:1300	Slowing the translation rate with the protein synthesis inhibitor cycloheximide increased the glycosylation efficiency in live cells and in the cell-free system.
11069924	0	30	theme	Translation	0:10	arg1	rate					12:15	Translation rate	0:15	Translation rate of human tyrosinase	0:35	Translation rate of human tyrosinase determines its N-linked glycosylation level.
11069924	7	31	theme	2-3-fold	1101:1108	arg1	rates					1162:1166	2-3-fold faster (7.7-10.0 amino acids/s) protein translation rates	1101:1166	2-3-fold faster (7.7-10.0 amino acids/s) protein translation rates	1101:1166	The inefficient glycosylation of Asn-290, due to the presence of a proximal Pro, was enhanced in melanoma cells possessing 2-3-fold faster (7.7-10.0 amino acids/s) protein translation rates compared with normal melanocytes (3.5 amino acids/s).
11069924	8	32	theme	synthesis	1268:1276	arg1	cycloheximide					1288:1300	the protein synthesis inhibitor cycloheximide	1256:1300	the protein synthesis inhibitor cycloheximide	1256:1300	Slowing the translation rate with the protein synthesis inhibitor cycloheximide increased the glycosylation efficiency in live cells and in the cell-free system.
11069924	0	33	theme	human	20:24	arg1	tyrosinase					26:35	human tyrosinase	20:35	human tyrosinase	20:35	Translation rate of human tyrosinase determines its N-linked glycosylation level.
11069924	4	34	theme	tyrosinase	561:570	arg1	translation					546:556	translation	546:556	translation of tyrosinase	546:570	To understand critical cotranslational events, the glycosylation and rate of translation of tyrosinase was studied in normal melanocytes, melanoma cells, an in vitro cell-free system, and semi-permeabilized cells.
11069924	1	35	gly	glycoprotein	114:125	arg1	Tyrosinase					82:91	Tyrosinase	82:91	Tyrosinase	82:91	Tyrosinase is a type I membrane glycoprotein essential for melanin synthesis.
11069924	1	35	gly	glycoprotein	114:125	arg1	glycoprotein					114:125	a type I membrane glycoprotein	96:125	a type I membrane glycoprotein essential for melanin synthesis	96:157	Tyrosinase is a type I membrane glycoprotein essential for melanin synthesis.
11069924	8	36	theme	glycosylation	1316:1328	arg1	efficiency					1330:1339	the glycosylation efficiency	1312:1339	the glycosylation efficiency	1312:1339	Slowing the translation rate with the protein synthesis inhibitor cycloheximide increased the glycosylation efficiency in live cells and in the cell-free system.
11069924	1	37	theme	type	98:101	arg1	Tyrosinase					82:91	Tyrosinase	82:91	Tyrosinase	82:91	Tyrosinase is a type I membrane glycoprotein essential for melanin synthesis.
11069924	1	37	theme	type	98:101	arg1	glycoprotein					114:125	a type I membrane glycoprotein	96:125	a type I membrane glycoprotein essential for melanin synthesis	96:157	Tyrosinase is a type I membrane glycoprotein essential for melanin synthesis.
11069924	4	38	theme	cell-free	635:643	arg1	system					645:650	an in vitro cell-free system	623:650	an in vitro cell-free system	623:650	To understand critical cotranslational events, the glycosylation and rate of translation of tyrosinase was studied in normal melanocytes, melanoma cells, an in vitro cell-free system, and semi-permeabilized cells.
11069924	3	39	theme	premature	375:383	arg1	fate					397:400	A similar premature degradative fate	365:400	A similar premature degradative fate for wild type tyrosinase	365:425	A similar premature degradative fate for wild type tyrosinase also occurs in amelanotic melanoma cells.
11069924	1	40	theme	I	103:103	arg1	Tyrosinase					82:91	Tyrosinase	82:91	Tyrosinase	82:91	Tyrosinase is a type I membrane glycoprotein essential for melanin synthesis.
11069924	1	40	theme	I	103:103	arg1	glycoprotein					114:125	a type I membrane glycoprotein	96:125	a type I membrane glycoprotein essential for melanin synthesis	96:157	Tyrosinase is a type I membrane glycoprotein essential for melanin synthesis.
11069924	5	41	link	N-linked	733:740	arg1	sites					752:756	all seven N-linked consensus sites	723:756	all seven N-linked consensus sites	723:756	Site-directed mutagenesis revealed that all seven N-linked consensus sites are utilized in human tyrosinase.
11069924	3	42	theme	type	411:414	arg1	tyrosinase					416:425	wild type tyrosinase	406:425	wild type tyrosinase	406:425	A similar premature degradative fate for wild type tyrosinase also occurs in amelanotic melanoma cells.
11069924	6	43	gly	glycosylation	801:813	arg1	Asn-Gly-Thr-Pro					827:841	Asn-Gly-Thr-Pro	827:841	Asn-Gly-Thr-Pro	827:841	However, glycosylation at Asn-290 (Asn-Gly-Thr-Pro) was suppressed, particularly when translation proceeded rapidly, producing a protein doublet with six or seven N-linked core glycans.
11069924	6	43	gly	glycosylation	801:813	arg2	Asn-Gly-Thr-Pro					827:841	Asn-Gly-Thr-Pro	827:841	Asn-Gly-Thr-Pro	827:841	However, glycosylation at Asn-290 (Asn-Gly-Thr-Pro) was suppressed, particularly when translation proceeded rapidly, producing a protein doublet with six or seven N-linked core glycans.
11069924	6	43	gly	glycosylation	801:813	arg1	Asn-290					818:824	Asn-290	818:824	Asn-290 (Asn-Gly-Thr-Pro)	818:842	However, glycosylation at Asn-290 (Asn-Gly-Thr-Pro) was suppressed, particularly when translation proceeded rapidly, producing a protein doublet with six or seven N-linked core glycans.
11069924	6	43	gly	glycosylation	801:813	arg2	Asn-290					818:824	Asn-290	818:824	Asn-290 (Asn-Gly-Thr-Pro)	818:842	However, glycosylation at Asn-290 (Asn-Gly-Thr-Pro) was suppressed, particularly when translation proceeded rapidly, producing a protein doublet with six or seven N-linked core glycans.
11069924	5	44	theme	N-linked	733:740	arg1	sites					752:756	all seven N-linked consensus sites	723:756	all seven N-linked consensus sites	723:756	Site-directed mutagenesis revealed that all seven N-linked consensus sites are utilized in human tyrosinase.
11069924	6	45	from	Asn-290	818:824	arg1	glycosylation					801:813	glycosylation	801:813	glycosylation at Asn-290 (Asn-Gly-Thr-Pro)	801:842	However, glycosylation at Asn-290 (Asn-Gly-Thr-Pro) was suppressed, particularly when translation proceeded rapidly, producing a protein doublet with six or seven N-linked core glycans.
11069924	2	46	from	retention	236:244	arg1	part					218:221	part	218:221	part	218:221	Mutations in tyrosinase lead to albinism due, at least in part, to aberrant retention of the protein in the endoplasmic reticulum and subsequent degradation by the cytosolic ubiquitin-proteasomal pathway.
11069924	2	46	from	retention	236:244	arg1	reticulum					280:288	the endoplasmic reticulum	264:288	the endoplasmic reticulum	264:288	Mutations in tyrosinase lead to albinism due, at least in part, to aberrant retention of the protein in the endoplasmic reticulum and subsequent degradation by the cytosolic ubiquitin-proteasomal pathway.
11069924	3	47	theme	melanoma	453:460	arg1	cells					462:466	amelanotic melanoma cells	442:466	amelanotic melanoma cells	442:466	A similar premature degradative fate for wild type tyrosinase also occurs in amelanotic melanoma cells.
11069924	0	48	theme	tyrosinase	26:35	arg1	rate					12:15	Translation rate	0:15	Translation rate of human tyrosinase	0:35	Translation rate of human tyrosinase determines its N-linked glycosylation level.
11069924	5	49	theme	consensus	742:750	arg1	sites					752:756	all seven N-linked consensus sites	723:756	all seven N-linked consensus sites	723:756	Site-directed mutagenesis revealed that all seven N-linked consensus sites are utilized in human tyrosinase.
11069924	3	50	theme	similar	367:373	arg1	fate					397:400	A similar premature degradative fate	365:400	A similar premature degradative fate for wild type tyrosinase	365:425	A similar premature degradative fate for wild type tyrosinase also occurs in amelanotic melanoma cells.
11069924	6	51	theme	N-linked	955:962	arg1	glycans					969:975	six or seven N-linked core glycans	942:975	six or seven N-linked core glycans	942:975	However, glycosylation at Asn-290 (Asn-Gly-Thr-Pro) was suppressed, particularly when translation proceeded rapidly, producing a protein doublet with six or seven N-linked core glycans.
11069924	2	52	from	Mutations	160:168	arg1	tyrosinase					173:182	tyrosinase	173:182	tyrosinase	173:182	Mutations in tyrosinase lead to albinism due, at least in part, to aberrant retention of the protein in the endoplasmic reticulum and subsequent degradation by the cytosolic ubiquitin-proteasomal pathway.
11069924	4	53	dep	glycosylation	520:532	arg1	the					516:518	the	516:518	the	516:518	To understand critical cotranslational events, the glycosylation and rate of translation of tyrosinase was studied in normal melanocytes, melanoma cells, an in vitro cell-free system, and semi-permeabilized cells.
11069924	5	54	theme	Site-directed	683:695	arg1	mutagenesis					697:707	Site-directed mutagenesis	683:707	Site-directed mutagenesis	683:707	Site-directed mutagenesis revealed that all seven N-linked consensus sites are utilized in human tyrosinase.
11069924	0	55	theme	glycosylation	61:73	arg1	level					75:79	its N-linked glycosylation level	48:79	its N-linked glycosylation level	48:79	Translation rate of human tyrosinase determines its N-linked glycosylation level.
11069924	7	56	gly	glycosylation	994:1006	arg1	Asn-290					1011:1017	Asn-290	1011:1017	Asn-290	1011:1017	The inefficient glycosylation of Asn-290, due to the presence of a proximal Pro, was enhanced in melanoma cells possessing 2-3-fold faster (7.7-10.0 amino acids/s) protein translation rates compared with normal melanocytes (3.5 amino acids/s).
11069924	7	56	gly	glycosylation	994:1006	arg1	cells					1084:1088	melanoma cells	1075:1088	melanoma cells possessing 2-3-fold faster (7.7-10.0 amino acids/s) protein translation rates compared with normal melanocytes (3.5 amino acids/s)	1075:1219	The inefficient glycosylation of Asn-290, due to the presence of a proximal Pro, was enhanced in melanoma cells possessing 2-3-fold faster (7.7-10.0 amino acids/s) protein translation rates compared with normal melanocytes (3.5 amino acids/s).
11069924	9	57	theme	tyrosinase	1453:1462	arg1	glycosylation					1473:1485	tyrosinase N-linked glycosylation	1453:1485	tyrosinase N-linked glycosylation	1453:1485	Therefore, the rate of protein translation can regulate the level of tyrosinase N-linked glycosylation, as well as other potential cotranslational maturation events.
11069924	2	58	theme	cytosolic	324:332	arg1	pathway					356:362	the cytosolic ubiquitin-proteasomal pathway	320:362	the cytosolic ubiquitin-proteasomal pathway	320:362	Mutations in tyrosinase lead to albinism due, at least in part, to aberrant retention of the protein in the endoplasmic reticulum and subsequent degradation by the cytosolic ubiquitin-proteasomal pathway.
11069924	3	59	theme	wild	406:409	arg1	tyrosinase					416:425	wild type tyrosinase	406:425	wild type tyrosinase	406:425	A similar premature degradative fate for wild type tyrosinase also occurs in amelanotic melanoma cells.
11069924	6	60	theme	core	964:967	arg1	glycans					969:975	six or seven N-linked core glycans	942:975	six or seven N-linked core glycans	942:975	However, glycosylation at Asn-290 (Asn-Gly-Thr-Pro) was suppressed, particularly when translation proceeded rapidly, producing a protein doublet with six or seven N-linked core glycans.
11069924	7	61	theme	melanoma	1075:1082	arg1	cells					1084:1088	melanoma cells	1075:1088	melanoma cells possessing 2-3-fold faster (7.7-10.0 amino acids/s) protein translation rates compared with normal melanocytes (3.5 amino acids/s)	1075:1219	The inefficient glycosylation of Asn-290, due to the presence of a proximal Pro, was enhanced in melanoma cells possessing 2-3-fold faster (7.7-10.0 amino acids/s) protein translation rates compared with normal melanocytes (3.5 amino acids/s).
11069924	4	62	dep	in	626:627	arg1	vitro					629:633	vitro	629:633	vitro	629:633	To understand critical cotranslational events, the glycosylation and rate of translation of tyrosinase was studied in normal melanocytes, melanoma cells, an in vitro cell-free system, and semi-permeabilized cells.
11069924	9	63	theme	cotranslational	1515:1529	arg1	events					1542:1547	other potential cotranslational maturation events	1499:1547	other potential cotranslational maturation events	1499:1547	Therefore, the rate of protein translation can regulate the level of tyrosinase N-linked glycosylation, as well as other potential cotranslational maturation events.
11069924	4	64	theme	translation	546:556	arg1	rate					538:541	rate	538:541	rate	538:541	To understand critical cotranslational events, the glycosylation and rate of translation of tyrosinase was studied in normal melanocytes, melanoma cells, an in vitro cell-free system, and semi-permeabilized cells.
11069924	4	64	theme	translation	546:556	arg1	glycosylation					520:532	glycosylation	520:532	glycosylation	520:532	To understand critical cotranslational events, the glycosylation and rate of translation of tyrosinase was studied in normal melanocytes, melanoma cells, an in vitro cell-free system, and semi-permeabilized cells.
11069924	7	65	theme	proximal	1045:1052	arg1	Pro					1054:1056	a proximal Pro	1043:1056	a proximal Pro	1043:1056	The inefficient glycosylation of Asn-290, due to the presence of a proximal Pro, was enhanced in melanoma cells possessing 2-3-fold faster (7.7-10.0 amino acids/s) protein translation rates compared with normal melanocytes (3.5 amino acids/s).
11069924	7	66	theme	translation	1150:1160	arg1	rates					1162:1166	2-3-fold faster (7.7-10.0 amino acids/s) protein translation rates	1101:1166	2-3-fold faster (7.7-10.0 amino acids/s) protein translation rates	1101:1166	The inefficient glycosylation of Asn-290, due to the presence of a proximal Pro, was enhanced in melanoma cells possessing 2-3-fold faster (7.7-10.0 amino acids/s) protein translation rates compared with normal melanocytes (3.5 amino acids/s).
11069924	1	67	theme	essential	127:135	arg1	Tyrosinase					82:91	Tyrosinase	82:91	Tyrosinase	82:91	Tyrosinase is a type I membrane glycoprotein essential for melanin synthesis.
11069924	1	67	theme	essential	127:135	arg1	glycoprotein					114:125	a type I membrane glycoprotein	96:125	a type I membrane glycoprotein essential for melanin synthesis	96:157	Tyrosinase is a type I membrane glycoprotein essential for melanin synthesis.
11069924	7	68	contain	possessing	1090:1099	arg2	rates					1162:1166	2-3-fold faster (7.7-10.0 amino acids/s) protein translation rates	1101:1166	2-3-fold faster (7.7-10.0 amino acids/s) protein translation rates	1101:1166	The inefficient glycosylation of Asn-290, due to the presence of a proximal Pro, was enhanced in melanoma cells possessing 2-3-fold faster (7.7-10.0 amino acids/s) protein translation rates compared with normal melanocytes (3.5 amino acids/s).
11069924	7	68	contain	possessing	1090:1099	arg1	cells					1084:1088	melanoma cells	1075:1088	melanoma cells possessing 2-3-fold faster (7.7-10.0 amino acids/s) protein translation rates compared with normal melanocytes (3.5 amino acids/s)	1075:1219	The inefficient glycosylation of Asn-290, due to the presence of a proximal Pro, was enhanced in melanoma cells possessing 2-3-fold faster (7.7-10.0 amino acids/s) protein translation rates compared with normal melanocytes (3.5 amino acids/s).
11069924	7	69	theme	Pro	1054:1056	arg1	presence					1031:1038	the presence	1027:1038	the presence of a proximal Pro	1027:1056	The inefficient glycosylation of Asn-290, due to the presence of a proximal Pro, was enhanced in melanoma cells possessing 2-3-fold faster (7.7-10.0 amino acids/s) protein translation rates compared with normal melanocytes (3.5 amino acids/s).
11069924	6	70	link	N-linked	955:962	arg1	glycans					969:975	six or seven N-linked core glycans	942:975	six or seven N-linked core glycans	942:975	However, glycosylation at Asn-290 (Asn-Gly-Thr-Pro) was suppressed, particularly when translation proceeded rapidly, producing a protein doublet with six or seven N-linked core glycans.
11069924	7	71	theme	due	1020:1022	arg1	glycosylation					994:1006	The inefficient glycosylation	978:1006	The inefficient glycosylation	978:1006	The inefficient glycosylation of Asn-290, due to the presence of a proximal Pro, was enhanced in melanoma cells possessing 2-3-fold faster (7.7-10.0 amino acids/s) protein translation rates compared with normal melanocytes (3.5 amino acids/s).
11069924	8	72	theme	translation	1234:1244	arg1	rate					1246:1249	the translation rate	1230:1249	the translation rate	1230:1249	Slowing the translation rate with the protein synthesis inhibitor cycloheximide increased the glycosylation efficiency in live cells and in the cell-free system.
11069924	9	73	theme	maturation	1531:1540	arg1	events					1542:1547	other potential cotranslational maturation events	1499:1547	other potential cotranslational maturation events	1499:1547	Therefore, the rate of protein translation can regulate the level of tyrosinase N-linked glycosylation, as well as other potential cotranslational maturation events.
11069924	5	74	theme	human	774:778	arg1	tyrosinase					780:789	human tyrosinase	774:789	human tyrosinase	774:789	Site-directed mutagenesis revealed that all seven N-linked consensus sites are utilized in human tyrosinase.
11069924	9	75	theme	other	1499:1503	arg1	events					1542:1547	other potential cotranslational maturation events	1499:1547	other potential cotranslational maturation events	1499:1547	Therefore, the rate of protein translation can regulate the level of tyrosinase N-linked glycosylation, as well as other potential cotranslational maturation events.
11069924	2	76	theme	aberrant	227:234	arg1	retention					236:244	aberrant retention	227:244	aberrant retention of the protein in the endoplasmic reticulum	227:288	Mutations in tyrosinase lead to albinism due, at least in part, to aberrant retention of the protein in the endoplasmic reticulum and subsequent degradation by the cytosolic ubiquitin-proteasomal pathway.
11069924	8	77	theme	inhibitor	1278:1286	arg1	cycloheximide					1288:1300	the protein synthesis inhibitor cycloheximide	1256:1300	the protein synthesis inhibitor cycloheximide	1256:1300	Slowing the translation rate with the protein synthesis inhibitor cycloheximide increased the glycosylation efficiency in live cells and in the cell-free system.
11069924	1	78	theme	melanin	141:147	arg1	synthesis					149:157	melanin synthesis	141:157	melanin synthesis	141:157	Tyrosinase is a type I membrane glycoprotein essential for melanin synthesis.
11069924	9	79	theme	N-linked	1464:1471	arg1	glycosylation					1473:1485	tyrosinase N-linked glycosylation	1453:1485	tyrosinase N-linked glycosylation	1453:1485	Therefore, the rate of protein translation can regulate the level of tyrosinase N-linked glycosylation, as well as other potential cotranslational maturation events.
11069924	4	80	theme	in	626:627	arg1	system					645:650	an in vitro cell-free system	623:650	an in vitro cell-free system	623:650	To understand critical cotranslational events, the glycosylation and rate of translation of tyrosinase was studied in normal melanocytes, melanoma cells, an in vitro cell-free system, and semi-permeabilized cells.
11069924	0	81	theme	N-linked	52:59	arg1	level					75:79	its N-linked glycosylation level	48:79	its N-linked glycosylation level	48:79	Translation rate of human tyrosinase determines its N-linked glycosylation level.
11069924	7	82	theme	normal	1182:1187	arg1	acids/s					1212:1218	3.5 amino acids/s	1202:1218	3.5 amino acids/s	1202:1218	The inefficient glycosylation of Asn-290, due to the presence of a proximal Pro, was enhanced in melanoma cells possessing 2-3-fold faster (7.7-10.0 amino acids/s) protein translation rates compared with normal melanocytes (3.5 amino acids/s).
11069924	7	82	theme	normal	1182:1187	arg1	melanocytes					1189:1199	normal melanocytes	1182:1199	normal melanocytes (3.5 amino acids/s)	1182:1219	The inefficient glycosylation of Asn-290, due to the presence of a proximal Pro, was enhanced in melanoma cells possessing 2-3-fold faster (7.7-10.0 amino acids/s) protein translation rates compared with normal melanocytes (3.5 amino acids/s).
11069924	7	83	theme	Asn-290	1011:1017	arg1	glycosylation					994:1006	The inefficient glycosylation	978:1006	The inefficient glycosylation	978:1006	The inefficient glycosylation of Asn-290, due to the presence of a proximal Pro, was enhanced in melanoma cells possessing 2-3-fold faster (7.7-10.0 amino acids/s) protein translation rates compared with normal melanocytes (3.5 amino acids/s).
11069924	8	84	theme	live	1344:1347	arg1	cells					1349:1353	live cells	1344:1353	live cells	1344:1353	Slowing the translation rate with the protein synthesis inhibitor cycloheximide increased the glycosylation efficiency in live cells and in the cell-free system.
17868453	5	0	theme	PSGL-1	694:699	arg1	sequences					712:720	PSGL-1 amino acid sequences	694:720	PSGL-1 amino acid sequences of 14 mammals (human, chimpanzee, rhesus monkey, bovine, pig, rat, tree-shrew, bushbaby, mouse, bat, horse, cat, sheep and dog)	694:848	Therefore, we performed multiple sequence alignment of PSGL-1 amino acid sequences of 14 mammals (human, chimpanzee, rhesus monkey, bovine, pig, rat, tree-shrew, bushbaby, mouse, bat, horse, cat, sheep and dog) and examined mammalian PSGL-1 interactions with human selectins.
17868453	2	1	theme	P-selectin	394:403	arg1	binding					405:411	L- and P-selectin binding	387:411	L- and P-selectin binding	387:411	Core-2 O-glycosylation of a N-terminal threonine and sulfation of at least one tyrosine residue of PSGL-1 are required for L- and P-selectin binding.
17868453	2	2	theme	N-terminal	292:301	arg1	threonine					303:311	a N-terminal threonine	290:311	a N-terminal threonine	290:311	Core-2 O-glycosylation of a N-terminal threonine and sulfation of at least one tyrosine residue of PSGL-1 are required for L- and P-selectin binding.
17868453	9	3	theme	studied	1328:1334	arg1	species					1336:1342	all studied species	1324:1342	all studied species	1324:1342	A mucin-like domain of 250-280 amino acids long was disclosed in all studied species.
17868453	8	4	theme	sulfation	1122:1130	arg1	site					1132:1135	at least one tyrosine sulfation site	1100:1135	at least one tyrosine sulfation site	1100:1135	However, each species exhibits at least one tyrosine sulfation site and, except in horse and dog, a T [D/E]PP [D/E] motif associated to the core-2 O-glycosylation of a N-terminal threonine.
17868453	12	5	theme	domain	1634:1639	arg1	sequences					1641:1649	Transmembrane and cytoplasmic domain sequences	1604:1649	Transmembrane and cytoplasmic domain sequences	1604:1649	Transmembrane and cytoplasmic domain sequences are well conserved.
17868453	5	6	theme	multiple	663:670	arg1	alignment					681:689	multiple sequence alignment	663:689	multiple sequence alignment of PSGL-1 amino acid sequences of 14 mammals (human, chimpanzee, rhesus monkey, bovine, pig, rat, tree-shrew, bushbaby, mouse, bat, horse, cat, sheep and dog)	663:848	Therefore, we performed multiple sequence alignment of PSGL-1 amino acid sequences of 14 mammals (human, chimpanzee, rhesus monkey, bovine, pig, rat, tree-shrew, bushbaby, mouse, bat, horse, cat, sheep and dog) and examined mammalian PSGL-1 interactions with human selectins.
17868453	13	7	theme	mammalian	1855:1863	arg1	sequences					1865:1873	all analyzed mammalian sequences	1842:1873	all analyzed mammalian sequences	1842:1873	The moesin binding residues that serve as adaptor between PSGL-1 and Syk, and are involved in regulating PSGL-1-dependent rolling on P-selectin are perfectly conserved in all analyzed mammalian sequences.
17868453	1	8	theme	inflammatory	198:209	arg1	lesions					211:217	inflammatory lesions	198:217	inflammatory lesions	198:217	BACKGROUND: P-selectin glycoprotein ligand-1 (PSGL-1) plays a critical role in recruiting leukocytes in inflammatory lesions by mediating leukocyte rolling on selectins.
17868453	17	9	theme	selectin	2364:2371	arg1	binding					2373:2379	selectin binding	2364:2379	selectin binding	2364:2379	In all five species, tyrosine sulfation of PSGL-1 was required for selectin binding.
17868453	8	10	theme	[D/E	1171:1174	arg1	motif					1185:1189	a T [D/E]PP [D/E] motif	1167:1189	a T [D/E]PP [D/E] motif associated to the core-2 O-glycosylation of a N-terminal threonine	1167:1256	However, each species exhibits at least one tyrosine sulfation site and, except in horse and dog, a T [D/E]PP [D/E] motif associated to the core-2 O-glycosylation of a N-terminal threonine.
17868453	13	11	theme	moesin	1675:1680	arg1	residues					1690:1697	The moesin binding residues	1671:1697	The moesin binding residues that serve as adaptor between PSGL-1 and Syk, and are involved in regulating PSGL-1-dependent rolling on P-selectin	1671:1813	The moesin binding residues that serve as adaptor between PSGL-1 and Syk, and are involved in regulating PSGL-1-dependent rolling on P-selectin are perfectly conserved in all analyzed mammalian sequences.
17868453	5	12	theme	mammals	728:734	arg1	sequences					712:720	PSGL-1 amino acid sequences	694:720	PSGL-1 amino acid sequences of 14 mammals (human, chimpanzee, rhesus monkey, bovine, pig, rat, tree-shrew, bushbaby, mouse, bat, horse, cat, sheep and dog)	694:848	Therefore, we performed multiple sequence alignment of PSGL-1 amino acid sequences of 14 mammals (human, chimpanzee, rhesus monkey, bovine, pig, rat, tree-shrew, bushbaby, mouse, bat, horse, cat, sheep and dog) and examined mammalian PSGL-1 interactions with human selectins.
17868453	8	13	theme	PP	1176:1177	arg1	motif					1185:1189	a T [D/E]PP [D/E] motif	1167:1189	a T [D/E]PP [D/E] motif associated to the core-2 O-glycosylation of a N-terminal threonine	1167:1256	However, each species exhibits at least one tyrosine sulfation site and, except in horse and dog, a T [D/E]PP [D/E] motif associated to the core-2 O-glycosylation of a N-terminal threonine.
17868453	18	14	theme	cytoplasmic	2475:2485	arg1	domains					2487:2493	the transmembrane and cytoplasmic domains	2453:2493	the transmembrane and cytoplasmic domains	2453:2493	CONCLUSION: These observations show that PSGL-1 amino acid sequence of the transmembrane and cytoplasmic domains are well conserved and that, despite a poor conservation of PSGL-1 N-terminus, L- and P-selectin binding sites are evolutionary conserved.
17868453	1	15	theme	leukocyte	232:240	arg1	rolling					242:248	leukocyte rolling	232:248	leukocyte rolling on selectins	232:261	BACKGROUND: P-selectin glycoprotein ligand-1 (PSGL-1) plays a critical role in recruiting leukocytes in inflammatory lesions by mediating leukocyte rolling on selectins.
17868453	1	16	from	rolling	242:248	arg1	selectins					253:261	selectins	253:261	selectins	253:261	BACKGROUND: P-selectin glycoprotein ligand-1 (PSGL-1) plays a critical role in recruiting leukocytes in inflammatory lesions by mediating leukocyte rolling on selectins.
17868453	18	17	theme	transmembrane	2457:2469	arg1	domains					2487:2493	the transmembrane and cytoplasmic domains	2453:2493	the transmembrane and cytoplasmic domains	2453:2493	CONCLUSION: These observations show that PSGL-1 amino acid sequence of the transmembrane and cytoplasmic domains are well conserved and that, despite a poor conservation of PSGL-1 N-terminus, L- and P-selectin binding sites are evolutionary conserved.
17868453	5	18	theme	acid	707:710	arg1	sequences					712:720	PSGL-1 amino acid sequences	694:720	PSGL-1 amino acid sequences of 14 mammals (human, chimpanzee, rhesus monkey, bovine, pig, rat, tree-shrew, bushbaby, mouse, bat, horse, cat, sheep and dog)	694:848	Therefore, we performed multiple sequence alignment of PSGL-1 amino acid sequences of 14 mammals (human, chimpanzee, rhesus monkey, bovine, pig, rat, tree-shrew, bushbaby, mouse, bat, horse, cat, sheep and dog) and examined mammalian PSGL-1 interactions with human selectins.
17868453	19	19	theme	PSGL-1	2736:2741	arg1	interactions					2743:2754	mammalian PSGL-1 interactions	2726:2754	mammalian PSGL-1 interactions with selectins	2726:2769	Functional assays reveal a critical role for post-translational modifications in regulating mammalian PSGL-1 interactions with selectins.
17868453	12	20	theme	Transmembrane	1604:1616	arg1	sequences					1641:1649	Transmembrane and cytoplasmic domain sequences	1604:1649	Transmembrane and cytoplasmic domain sequences	1604:1649	Transmembrane and cytoplasmic domain sequences are well conserved.
17868453	16	21	theme	equine	2234:2239	arg1	glycosyltransferases					2241:2260	human or equine glycosyltransferases	2225:2260	human or equine glycosyltransferases	2225:2260	Horse PSGL-1, glycosylated by human or equine glycosyltransferases, did not interact with P-selectin.
17868453	5	22	theme	human	898:902	arg1	selectins					904:912	human selectins	898:912	human selectins	898:912	Therefore, we performed multiple sequence alignment of PSGL-1 amino acid sequences of 14 mammals (human, chimpanzee, rhesus monkey, bovine, pig, rat, tree-shrew, bushbaby, mouse, bat, horse, cat, sheep and dog) and examined mammalian PSGL-1 interactions with human selectins.
17868453	5	23	theme	PSGL-1	873:878	arg1	interactions					880:891	mammalian PSGL-1 interactions	863:891	mammalian PSGL-1 interactions with human selectins	863:912	Therefore, we performed multiple sequence alignment of PSGL-1 amino acid sequences of 14 mammals (human, chimpanzee, rhesus monkey, bovine, pig, rat, tree-shrew, bushbaby, mouse, bat, horse, cat, sheep and dog) and examined mammalian PSGL-1 interactions with human selectins.
17868453	12	24	theme	cytoplasmic	1622:1632	arg1	sequences					1641:1649	Transmembrane and cytoplasmic domain sequences	1604:1649	Transmembrane and cytoplasmic domain sequences	1604:1649	Transmembrane and cytoplasmic domain sequences are well conserved.
17868453	18	25	theme	P-selectin	2581:2590	arg1	sites					2600:2604	L- and P-selectin binding sites	2574:2604	L- and P-selectin binding sites	2574:2604	CONCLUSION: These observations show that PSGL-1 amino acid sequence of the transmembrane and cytoplasmic domains are well conserved and that, despite a poor conservation of PSGL-1 N-terminus, L- and P-selectin binding sites are evolutionary conserved.
17868453	2	26	theme	Core-2	264:269	arg1	O-glycosylation					271:285	Core-2 O-glycosylation	264:285	Core-2 O-glycosylation of a N-terminal threonine	264:311	Core-2 O-glycosylation of a N-terminal threonine and sulfation of at least one tyrosine residue of PSGL-1 are required for L- and P-selectin binding.
17868453	1	27	theme	critical	156:163	arg1	role					165:168	a critical role	154:168	a critical role	154:168	BACKGROUND: P-selectin glycoprotein ligand-1 (PSGL-1) plays a critical role in recruiting leukocytes in inflammatory lesions by mediating leukocyte rolling on selectins.
17868453	14	28	theme	human	2045:2049	arg1	L-					2051:2052	human L-	2045:2052	human L-	2045:2052	Despite a poor conservation of PSGL-1 N-terminal sequence, CHO cells co-expressing human glycosyltransferases and human, bovine, pig or rat PSGL-1 efficiently rolled on human L- or P-selectin.
17868453	15	29	theme	rat	2089:2091	arg1	neutrophils					2093:2103	pig or rat neutrophils	2082:2103	pig or rat neutrophils	2082:2103	By contrast, pig or rat neutrophils were much less efficiently recruited than human or bovine neutrophils on human selectins.
17868453	16	30	theme	human	2225:2229	arg1	glycosyltransferases					2241:2260	human or equine glycosyltransferases	2225:2260	human or equine glycosyltransferases	2225:2260	Horse PSGL-1, glycosylated by human or equine glycosyltransferases, did not interact with P-selectin.
17868453	19	31	theme	critical	2661:2668	arg1	role					2670:2673	a critical role	2659:2673	a critical role for post-translational modifications in regulating mammalian PSGL-1 interactions with selectins	2659:2769	Functional assays reveal a critical role for post-translational modifications in regulating mammalian PSGL-1 interactions with selectins.
17868453	14	32	theme	CHO	1935:1937	arg1	cells					1939:1943	CHO cells	1935:1943	CHO cells co-expressing human glycosyltransferases and human, bovine, pig or rat PSGL-1	1935:2021	Despite a poor conservation of PSGL-1 N-terminal sequence, CHO cells co-expressing human glycosyltransferases and human, bovine, pig or rat PSGL-1 efficiently rolled on human L- or P-selectin.
17868453	6	33	theme	signal	926:931	arg1	peptide					933:939	A signal peptide	924:939	A signal peptide	924:939	RESULTS: A signal peptide was predicted in each sequence and a propeptide cleavage site was found in 9/14 species.
17868453	18	34	theme	amino	2430:2434	arg1	sequence					2441:2448	PSGL-1 amino acid sequence	2423:2448	PSGL-1 amino acid sequence of the transmembrane and cytoplasmic domains	2423:2493	CONCLUSION: These observations show that PSGL-1 amino acid sequence of the transmembrane and cytoplasmic domains are well conserved and that, despite a poor conservation of PSGL-1 N-terminus, L- and P-selectin binding sites are evolutionary conserved.
17868453	8	35	theme	threonine	1248:1256	arg1	O-glycosylation					1216:1230	the core-2 O-glycosylation	1205:1230	the core-2 O-glycosylation of a N-terminal threonine	1205:1256	However, each species exhibits at least one tyrosine sulfation site and, except in horse and dog, a T [D/E]PP [D/E] motif associated to the core-2 O-glycosylation of a N-terminal threonine.
17868453	3	36	theme	intra-	453:458	arg1	evolution					478:486	the intra- and inter-species evolution	449:486	the intra- and inter-species evolution of PSGL-1 primary structure	449:514	Little information is available on the intra- and inter-species evolution of PSGL-1 primary structure.
17868453	5	37	theme	rhesus	756:761	arg1	chimpanzee					744:753	chimpanzee	744:753	chimpanzee	744:753	Therefore, we performed multiple sequence alignment of PSGL-1 amino acid sequences of 14 mammals (human, chimpanzee, rhesus monkey, bovine, pig, rat, tree-shrew, bushbaby, mouse, bat, horse, cat, sheep and dog) and examined mammalian PSGL-1 interactions with human selectins.
17868453	5	37	theme	rhesus	756:761	arg1	monkey					763:768	rhesus monkey	756:768	rhesus monkey	756:768	Therefore, we performed multiple sequence alignment of PSGL-1 amino acid sequences of 14 mammals (human, chimpanzee, rhesus monkey, bovine, pig, rat, tree-shrew, bushbaby, mouse, bat, horse, cat, sheep and dog) and examined mammalian PSGL-1 interactions with human selectins.
17868453	13	38	from	rolling	1793:1799	arg1	P-selectin					1804:1813	P-selectin	1804:1813	P-selectin	1804:1813	The moesin binding residues that serve as adaptor between PSGL-1 and Syk, and are involved in regulating PSGL-1-dependent rolling on P-selectin are perfectly conserved in all analyzed mammalian sequences.
17868453	6	39	located	found	1007:1011	arg1	species					1021:1027	9/14 species	1016:1027	9/14 species	1016:1027	RESULTS: A signal peptide was predicted in each sequence and a propeptide cleavage site was found in 9/14 species.
17868453	6	39	located	found	1007:1011	arg2	site					998:1001	a propeptide cleavage site	976:1001	a propeptide cleavage site	976:1001	RESULTS: A signal peptide was predicted in each sequence and a propeptide cleavage site was found in 9/14 species.
17868453	18	40	theme	poor	2534:2537	arg1	conservation					2539:2550	a poor conservation	2532:2550	a poor conservation of PSGL-1 N-terminus	2532:2571	CONCLUSION: These observations show that PSGL-1 amino acid sequence of the transmembrane and cytoplasmic domains are well conserved and that, despite a poor conservation of PSGL-1 N-terminus, L- and P-selectin binding sites are evolutionary conserved.
17868453	10	41	theme	repeats	1531:1537	arg1	number					1511:1516	a variable number	1500:1516	a variable number of decameric repeats (DR)	1500:1542	It lies between the conserved N-terminal O-glycosylated threonine (Thr-57 in human) and the transmembrane domain, and contains a central region exhibiting a variable number of decameric repeats (DR).
17868453	0	42	theme	Evolutionary	0:11	arg1	conservation					13:24	Evolutionary conservation	0:24	Evolutionary conservation of P-selectin glycoprotein ligand-1	0:60	Evolutionary conservation of P-selectin glycoprotein ligand-1 primary structure and function.
17868453	15	43	theme	human	2178:2182	arg1	selectins					2184:2192	human selectins	2178:2192	human selectins	2178:2192	By contrast, pig or rat neutrophils were much less efficiently recruited than human or bovine neutrophils on human selectins.
17868453	1	44	theme	P-selectin	106:115	arg1	PSGL-1					140:145	PSGL-1	140:145	PSGL-1	140:145	BACKGROUND: P-selectin glycoprotein ligand-1 (PSGL-1) plays a critical role in recruiting leukocytes in inflammatory lesions by mediating leukocyte rolling on selectins.
17868453	1	44	theme	P-selectin	106:115	arg1	ligand-1					130:137	P-selectin glycoprotein ligand-1	106:137	P-selectin glycoprotein ligand-1 (PSGL-1)	106:146	BACKGROUND: P-selectin glycoprotein ligand-1 (PSGL-1) plays a critical role in recruiting leukocytes in inflammatory lesions by mediating leukocyte rolling on selectins.
17868453	4	45	theme	site	580:583	arg1	conservation					547:558	the evolutionary conservation	530:558	the evolutionary conservation of selectin binding site on PSGL-1	530:593	In addition, the evolutionary conservation of selectin binding site on PSGL-1 has not been previously examined in detail.
17868453	18	46	theme	L-	2574:2575	arg1	sites					2600:2604	L- and P-selectin binding sites	2574:2604	L- and P-selectin binding sites	2574:2604	CONCLUSION: These observations show that PSGL-1 amino acid sequence of the transmembrane and cytoplasmic domains are well conserved and that, despite a poor conservation of PSGL-1 N-terminus, L- and P-selectin binding sites are evolutionary conserved.
17868453	10	47	contain	contains	1463:1470	arg1	It					1345:1346	It	1345:1346	It	1345:1346	It lies between the conserved N-terminal O-glycosylated threonine (Thr-57 in human) and the transmembrane domain, and contains a central region exhibiting a variable number of decameric repeats (DR).
17868453	10	47	contain	contains	1463:1470	arg2	region					1482:1487	a central region	1472:1487	a central region exhibiting a variable number of decameric repeats (DR)	1472:1542	It lies between the conserved N-terminal O-glycosylated threonine (Thr-57 in human) and the transmembrane domain, and contains a central region exhibiting a variable number of decameric repeats (DR).
17868453	6	48	theme	cleavage	989:996	arg1	site					998:1001	a propeptide cleavage site	976:1001	a propeptide cleavage site	976:1001	RESULTS: A signal peptide was predicted in each sequence and a propeptide cleavage site was found in 9/14 species.
17868453	17	49	theme	PSGL-1	2340:2345	arg1	sulfation					2327:2335	tyrosine sulfation	2318:2335	tyrosine sulfation of PSGL-1	2318:2345	In all five species, tyrosine sulfation of PSGL-1 was required for selectin binding.
17868453	10	50	theme	N-terminal	1375:1384	arg1	threonine					1401:1409	the conserved N-terminal O-glycosylated threonine	1361:1409	the conserved N-terminal O-glycosylated threonine (Thr-57 in human)	1361:1427	It lies between the conserved N-terminal O-glycosylated threonine (Thr-57 in human) and the transmembrane domain, and contains a central region exhibiting a variable number of decameric repeats (DR).
17868453	18	51	theme	N-terminus	2562:2571	arg1	conservation					2539:2550	a poor conservation	2532:2550	a poor conservation of PSGL-1 N-terminus	2532:2571	CONCLUSION: These observations show that PSGL-1 amino acid sequence of the transmembrane and cytoplasmic domains are well conserved and that, despite a poor conservation of PSGL-1 N-terminus, L- and P-selectin binding sites are evolutionary conserved.
17868453	3	52	theme	inter-species	464:476	arg1	evolution					478:486	the intra- and inter-species evolution	449:486	the intra- and inter-species evolution of PSGL-1 primary structure	449:514	Little information is available on the intra- and inter-species evolution of PSGL-1 primary structure.
17868453	0	53	theme	glycoprotein	40:51	arg1	ligand-1					53:60	P-selectin glycoprotein ligand-1	29:60	P-selectin glycoprotein ligand-1	29:60	Evolutionary conservation of P-selectin glycoprotein ligand-1 primary structure and function.
17868453	3	54	theme	Little	414:419	arg1	information					421:431	Little information	414:431	Little information	414:431	Little information is available on the intra- and inter-species evolution of PSGL-1 primary structure.
17868453	2	55	theme	PSGL-1	363:368	arg1	PSGL-1					363:368	PSGL-1	363:368	PSGL-1	363:368	Core-2 O-glycosylation of a N-terminal threonine and sulfation of at least one tyrosine residue of PSGL-1 are required for L- and P-selectin binding.
17868453	2	55	theme	PSGL-1	363:368	arg1	residue					352:358	at least one tyrosine residue	330:358	at least one tyrosine residue of PSGL-1	330:368	Core-2 O-glycosylation of a N-terminal threonine and sulfation of at least one tyrosine residue of PSGL-1 are required for L- and P-selectin binding.
17868453	4	56	from	conservation	547:558	arg1	PSGL-1					588:593	PSGL-1	588:593	PSGL-1	588:593	In addition, the evolutionary conservation of selectin binding site on PSGL-1 has not been previously examined in detail.
17868453	11	57	dep	Interspecies	1545:1556	arg1	polymorphisms					1575:1587	polymorphisms	1575:1587	polymorphisms	1575:1587	Interspecies and intraspecies polymorphisms were observed.
17868453	16	58	gly	glycosylated	2209:2220	arg1	PSGL-1					2201:2206	Horse PSGL-1	2195:2206	Horse PSGL-1	2195:2206	Horse PSGL-1, glycosylated by human or equine glycosyltransferases, did not interact with P-selectin.
17868453	4	59	theme	selectin	563:570	arg1	site					580:583	selectin binding site	563:583	selectin binding site	563:583	In addition, the evolutionary conservation of selectin binding site on PSGL-1 has not been previously examined in detail.
17868453	14	60	theme	human	1959:1963	arg1	glycosyltransferases					1965:1984	human glycosyltransferases	1959:1984	human glycosyltransferases	1959:1984	Despite a poor conservation of PSGL-1 N-terminal sequence, CHO cells co-expressing human glycosyltransferases and human, bovine, pig or rat PSGL-1 efficiently rolled on human L- or P-selectin.
17868453	2	61	theme	residue	352:358	arg1	O-glycosylation					271:285	Core-2 O-glycosylation	264:285	Core-2 O-glycosylation of a N-terminal threonine	264:311	Core-2 O-glycosylation of a N-terminal threonine and sulfation of at least one tyrosine residue of PSGL-1 are required for L- and P-selectin binding.
17868453	2	61	theme	residue	352:358	arg1	sulfation					317:325	sulfation	317:325	sulfation of at least one tyrosine residue of PSGL-1	317:368	Core-2 O-glycosylation of a N-terminal threonine and sulfation of at least one tyrosine residue of PSGL-1 are required for L- and P-selectin binding.
17868453	19	62	theme	Functional	2634:2643	arg1	assays					2645:2650	Functional assays	2634:2650	Functional assays	2634:2650	Functional assays reveal a critical role for post-translational modifications in regulating mammalian PSGL-1 interactions with selectins.
17868453	10	63	theme	transmembrane	1437:1449	arg1	domain					1451:1456	the transmembrane domain	1433:1456	the transmembrane domain	1433:1456	It lies between the conserved N-terminal O-glycosylated threonine (Thr-57 in human) and the transmembrane domain, and contains a central region exhibiting a variable number of decameric repeats (DR).
17868453	2	64	theme	L-	387:388	arg1	binding					405:411	L- and P-selectin binding	387:411	L- and P-selectin binding	387:411	Core-2 O-glycosylation of a N-terminal threonine and sulfation of at least one tyrosine residue of PSGL-1 are required for L- and P-selectin binding.
17868453	15	65	theme	pig	2082:2084	arg1	neutrophils					2093:2103	pig or rat neutrophils	2082:2103	pig or rat neutrophils	2082:2103	By contrast, pig or rat neutrophils were much less efficiently recruited than human or bovine neutrophils on human selectins.
17868453	9	66	theme	amino	1290:1294	arg1	acids					1296:1300	250-280 amino acids long	1282:1305	250-280 amino acids long	1282:1305	A mucin-like domain of 250-280 amino acids long was disclosed in all studied species.
17868453	5	67	theme	sequence	672:679	arg1	alignment					681:689	multiple sequence alignment	663:689	multiple sequence alignment of PSGL-1 amino acid sequences of 14 mammals (human, chimpanzee, rhesus monkey, bovine, pig, rat, tree-shrew, bushbaby, mouse, bat, horse, cat, sheep and dog)	663:848	Therefore, we performed multiple sequence alignment of PSGL-1 amino acid sequences of 14 mammals (human, chimpanzee, rhesus monkey, bovine, pig, rat, tree-shrew, bushbaby, mouse, bat, horse, cat, sheep and dog) and examined mammalian PSGL-1 interactions with human selectins.
17868453	9	68	theme	long	1302:1305	arg1	acids					1296:1300	250-280 amino acids long	1282:1305	250-280 amino acids long	1282:1305	A mucin-like domain of 250-280 amino acids long was disclosed in all studied species.
17868453	18	69	dep	conserved	2623:2631	arg1	evolutionary					2610:2621	evolutionary	2610:2621	evolutionary	2610:2621	CONCLUSION: These observations show that PSGL-1 amino acid sequence of the transmembrane and cytoplasmic domains are well conserved and that, despite a poor conservation of PSGL-1 N-terminus, L- and P-selectin binding sites are evolutionary conserved.
17868453	13	70	theme	binding	1682:1688	arg1	residues					1690:1697	The moesin binding residues	1671:1697	The moesin binding residues that serve as adaptor between PSGL-1 and Syk, and are involved in regulating PSGL-1-dependent rolling on P-selectin	1671:1813	The moesin binding residues that serve as adaptor between PSGL-1 and Syk, and are involved in regulating PSGL-1-dependent rolling on P-selectin are perfectly conserved in all analyzed mammalian sequences.
17868453	14	71	theme	PSGL-1	1907:1912	arg1	sequence					1925:1932	PSGL-1 N-terminal sequence	1907:1932	PSGL-1 N-terminal sequence	1907:1932	Despite a poor conservation of PSGL-1 N-terminal sequence, CHO cells co-expressing human glycosyltransferases and human, bovine, pig or rat PSGL-1 efficiently rolled on human L- or P-selectin.
17868453	17	72	theme	tyrosine	2318:2325	arg1	sulfation					2327:2335	tyrosine sulfation	2318:2335	tyrosine sulfation of PSGL-1	2318:2345	In all five species, tyrosine sulfation of PSGL-1 was required for selectin binding.
17868453	7	73	theme	PSGL-1	1030:1035	arg1	N-terminus					1037:1046	PSGL-1 N-terminus	1030:1046	PSGL-1 N-terminus	1030:1046	PSGL-1 N-terminus is poorly conserved.
17868453	2	74	theme	threonine	303:311	arg1	O-glycosylation					271:285	Core-2 O-glycosylation	264:285	Core-2 O-glycosylation of a N-terminal threonine	264:311	Core-2 O-glycosylation of a N-terminal threonine and sulfation of at least one tyrosine residue of PSGL-1 are required for L- and P-selectin binding.
17868453	2	74	theme	threonine	303:311	arg1	sulfation					317:325	sulfation	317:325	sulfation of at least one tyrosine residue of PSGL-1	317:368	Core-2 O-glycosylation of a N-terminal threonine and sulfation of at least one tyrosine residue of PSGL-1 are required for L- and P-selectin binding.
17868453	9	75	theme	mucin-like	1261:1270	arg1	acids					1296:1300	250-280 amino acids long	1282:1305	250-280 amino acids long	1282:1305	A mucin-like domain of 250-280 amino acids long was disclosed in all studied species.
17868453	9	75	theme	mucin-like	1261:1270	arg1	domain					1272:1277	A mucin-like domain	1259:1277	A mucin-like domain of 250-280 amino acids long	1259:1305	A mucin-like domain of 250-280 amino acids long was disclosed in all studied species.
17868453	13	76	theme	analyzed	1846:1853	arg1	sequences					1865:1873	all analyzed mammalian sequences	1842:1873	all analyzed mammalian sequences	1842:1873	The moesin binding residues that serve as adaptor between PSGL-1 and Syk, and are involved in regulating PSGL-1-dependent rolling on P-selectin are perfectly conserved in all analyzed mammalian sequences.
17868453	8	77	theme	tyrosine	1113:1120	arg1	site					1132:1135	at least one tyrosine sulfation site	1100:1135	at least one tyrosine sulfation site	1100:1135	However, each species exhibits at least one tyrosine sulfation site and, except in horse and dog, a T [D/E]PP [D/E] motif associated to the core-2 O-glycosylation of a N-terminal threonine.
17868453	10	78	gly	O-glycosylated	1386:1399	arg1	threonine					1401:1409	the conserved N-terminal O-glycosylated threonine	1361:1409	the conserved N-terminal O-glycosylated threonine (Thr-57 in human)	1361:1427	It lies between the conserved N-terminal O-glycosylated threonine (Thr-57 in human) and the transmembrane domain, and contains a central region exhibiting a variable number of decameric repeats (DR).
17868453	10	79	theme	central	1474:1480	arg1	region					1482:1487	a central region	1472:1487	a central region exhibiting a variable number of decameric repeats (DR)	1472:1542	It lies between the conserved N-terminal O-glycosylated threonine (Thr-57 in human) and the transmembrane domain, and contains a central region exhibiting a variable number of decameric repeats (DR).
17868453	19	80	theme	post-translational	2679:2696	arg1	modifications					2698:2710	post-translational modifications	2679:2710	post-translational modifications	2679:2710	Functional assays reveal a critical role for post-translational modifications in regulating mammalian PSGL-1 interactions with selectins.
17868453	8	81	theme	T	1169:1169	arg1	motif					1185:1189	a T [D/E]PP [D/E] motif	1167:1189	a T [D/E]PP [D/E] motif associated to the core-2 O-glycosylation of a N-terminal threonine	1167:1256	However, each species exhibits at least one tyrosine sulfation site and, except in horse and dog, a T [D/E]PP [D/E] motif associated to the core-2 O-glycosylation of a N-terminal threonine.
17868453	18	82	theme	domains	2487:2493	arg1	sequence					2441:2448	PSGL-1 amino acid sequence	2423:2448	PSGL-1 amino acid sequence of the transmembrane and cytoplasmic domains	2423:2493	CONCLUSION: These observations show that PSGL-1 amino acid sequence of the transmembrane and cytoplasmic domains are well conserved and that, despite a poor conservation of PSGL-1 N-terminus, L- and P-selectin binding sites are evolutionary conserved.
17868453	5	83	with	interactions	880:891	arg1	selectins					904:912	human selectins	898:912	human selectins	898:912	Therefore, we performed multiple sequence alignment of PSGL-1 amino acid sequences of 14 mammals (human, chimpanzee, rhesus monkey, bovine, pig, rat, tree-shrew, bushbaby, mouse, bat, horse, cat, sheep and dog) and examined mammalian PSGL-1 interactions with human selectins.
17868453	10	84	theme	variable	1502:1509	arg1	number					1511:1516	a variable number	1500:1516	a variable number of decameric repeats (DR)	1500:1542	It lies between the conserved N-terminal O-glycosylated threonine (Thr-57 in human) and the transmembrane domain, and contains a central region exhibiting a variable number of decameric repeats (DR).
17868453	5	85	theme	amino	701:705	arg1	sequences					712:720	PSGL-1 amino acid sequences	694:720	PSGL-1 amino acid sequences of 14 mammals (human, chimpanzee, rhesus monkey, bovine, pig, rat, tree-shrew, bushbaby, mouse, bat, horse, cat, sheep and dog)	694:848	Therefore, we performed multiple sequence alignment of PSGL-1 amino acid sequences of 14 mammals (human, chimpanzee, rhesus monkey, bovine, pig, rat, tree-shrew, bushbaby, mouse, bat, horse, cat, sheep and dog) and examined mammalian PSGL-1 interactions with human selectins.
17868453	19	86	theme	mammalian	2726:2734	arg1	interactions					2743:2754	mammalian PSGL-1 interactions	2726:2754	mammalian PSGL-1 interactions with selectins	2726:2769	Functional assays reveal a critical role for post-translational modifications in regulating mammalian PSGL-1 interactions with selectins.
17868453	14	87	dep	human	1990:1994	arg1	PSGL-1					2016:2021	PSGL-1	2016:2021	PSGL-1	2016:2021	Despite a poor conservation of PSGL-1 N-terminal sequence, CHO cells co-expressing human glycosyltransferases and human, bovine, pig or rat PSGL-1 efficiently rolled on human L- or P-selectin.
17868453	8	88	theme	[D/E	1179:1182	arg1	motif					1185:1189	a T [D/E]PP [D/E] motif	1167:1189	a T [D/E]PP [D/E] motif associated to the core-2 O-glycosylation of a N-terminal threonine	1167:1256	However, each species exhibits at least one tyrosine sulfation site and, except in horse and dog, a T [D/E]PP [D/E] motif associated to the core-2 O-glycosylation of a N-terminal threonine.
17868453	16	89	theme	Horse	2195:2199	arg1	PSGL-1					2201:2206	Horse PSGL-1	2195:2206	Horse PSGL-1	2195:2206	Horse PSGL-1, glycosylated by human or equine glycosyltransferases, did not interact with P-selectin.
17868453	5	90	theme	sequences	712:720	arg1	alignment					681:689	multiple sequence alignment	663:689	multiple sequence alignment of PSGL-1 amino acid sequences of 14 mammals (human, chimpanzee, rhesus monkey, bovine, pig, rat, tree-shrew, bushbaby, mouse, bat, horse, cat, sheep and dog)	663:848	Therefore, we performed multiple sequence alignment of PSGL-1 amino acid sequences of 14 mammals (human, chimpanzee, rhesus monkey, bovine, pig, rat, tree-shrew, bushbaby, mouse, bat, horse, cat, sheep and dog) and examined mammalian PSGL-1 interactions with human selectins.
17868453	5	91	theme	mammalian	863:871	arg1	interactions					880:891	mammalian PSGL-1 interactions	863:891	mammalian PSGL-1 interactions with human selectins	863:912	Therefore, we performed multiple sequence alignment of PSGL-1 amino acid sequences of 14 mammals (human, chimpanzee, rhesus monkey, bovine, pig, rat, tree-shrew, bushbaby, mouse, bat, horse, cat, sheep and dog) and examined mammalian PSGL-1 interactions with human selectins.
17868453	18	92	theme	binding	2592:2598	arg1	sites					2600:2604	L- and P-selectin binding sites	2574:2604	L- and P-selectin binding sites	2574:2604	CONCLUSION: These observations show that PSGL-1 amino acid sequence of the transmembrane and cytoplasmic domains are well conserved and that, despite a poor conservation of PSGL-1 N-terminus, L- and P-selectin binding sites are evolutionary conserved.
17868453	3	93	theme	primary	498:504	arg1	structure					506:514	PSGL-1 primary structure	491:514	PSGL-1 primary structure	491:514	Little information is available on the intra- and inter-species evolution of PSGL-1 primary structure.
17868453	5	94	dep	human	737:741	arg1	rat					784:786	rat	784:786	rat	784:786	Therefore, we performed multiple sequence alignment of PSGL-1 amino acid sequences of 14 mammals (human, chimpanzee, rhesus monkey, bovine, pig, rat, tree-shrew, bushbaby, mouse, bat, horse, cat, sheep and dog) and examined mammalian PSGL-1 interactions with human selectins.
17868453	5	94	dep	human	737:741	arg1	mouse					811:815	mouse	811:815	mouse	811:815	Therefore, we performed multiple sequence alignment of PSGL-1 amino acid sequences of 14 mammals (human, chimpanzee, rhesus monkey, bovine, pig, rat, tree-shrew, bushbaby, mouse, bat, horse, cat, sheep and dog) and examined mammalian PSGL-1 interactions with human selectins.
17868453	5	94	dep	human	737:741	arg1	monkey					763:768	rhesus monkey	756:768	rhesus monkey	756:768	Therefore, we performed multiple sequence alignment of PSGL-1 amino acid sequences of 14 mammals (human, chimpanzee, rhesus monkey, bovine, pig, rat, tree-shrew, bushbaby, mouse, bat, horse, cat, sheep and dog) and examined mammalian PSGL-1 interactions with human selectins.
17868453	5	94	dep	human	737:741	arg1	bat					818:820	bat	818:820	bat	818:820	Therefore, we performed multiple sequence alignment of PSGL-1 amino acid sequences of 14 mammals (human, chimpanzee, rhesus monkey, bovine, pig, rat, tree-shrew, bushbaby, mouse, bat, horse, cat, sheep and dog) and examined mammalian PSGL-1 interactions with human selectins.
17868453	5	94	dep	human	737:741	arg1	sheep					835:839	sheep	835:839	sheep	835:839	Therefore, we performed multiple sequence alignment of PSGL-1 amino acid sequences of 14 mammals (human, chimpanzee, rhesus monkey, bovine, pig, rat, tree-shrew, bushbaby, mouse, bat, horse, cat, sheep and dog) and examined mammalian PSGL-1 interactions with human selectins.
17868453	5	94	dep	human	737:741	arg1	bovine					771:776	bovine	771:776	bovine	771:776	Therefore, we performed multiple sequence alignment of PSGL-1 amino acid sequences of 14 mammals (human, chimpanzee, rhesus monkey, bovine, pig, rat, tree-shrew, bushbaby, mouse, bat, horse, cat, sheep and dog) and examined mammalian PSGL-1 interactions with human selectins.
17868453	5	94	dep	human	737:741	arg1	tree-shrew					789:798	tree-shrew	789:798	tree-shrew	789:798	Therefore, we performed multiple sequence alignment of PSGL-1 amino acid sequences of 14 mammals (human, chimpanzee, rhesus monkey, bovine, pig, rat, tree-shrew, bushbaby, mouse, bat, horse, cat, sheep and dog) and examined mammalian PSGL-1 interactions with human selectins.
17868453	5	94	dep	human	737:741	arg1	dog					845:847	dog	845:847	dog	845:847	Therefore, we performed multiple sequence alignment of PSGL-1 amino acid sequences of 14 mammals (human, chimpanzee, rhesus monkey, bovine, pig, rat, tree-shrew, bushbaby, mouse, bat, horse, cat, sheep and dog) and examined mammalian PSGL-1 interactions with human selectins.
17868453	5	94	dep	human	737:741	arg1	bushbaby					801:808	bushbaby	801:808	bushbaby	801:808	Therefore, we performed multiple sequence alignment of PSGL-1 amino acid sequences of 14 mammals (human, chimpanzee, rhesus monkey, bovine, pig, rat, tree-shrew, bushbaby, mouse, bat, horse, cat, sheep and dog) and examined mammalian PSGL-1 interactions with human selectins.
17868453	5	94	dep	human	737:741	arg1	chimpanzee					744:753	chimpanzee	744:753	chimpanzee	744:753	Therefore, we performed multiple sequence alignment of PSGL-1 amino acid sequences of 14 mammals (human, chimpanzee, rhesus monkey, bovine, pig, rat, tree-shrew, bushbaby, mouse, bat, horse, cat, sheep and dog) and examined mammalian PSGL-1 interactions with human selectins.
17868453	5	94	dep	human	737:741	arg1	horse					823:827	horse	823:827	horse	823:827	Therefore, we performed multiple sequence alignment of PSGL-1 amino acid sequences of 14 mammals (human, chimpanzee, rhesus monkey, bovine, pig, rat, tree-shrew, bushbaby, mouse, bat, horse, cat, sheep and dog) and examined mammalian PSGL-1 interactions with human selectins.
17868453	5	94	dep	human	737:741	arg1	pig					779:781	pig	779:781	pig	779:781	Therefore, we performed multiple sequence alignment of PSGL-1 amino acid sequences of 14 mammals (human, chimpanzee, rhesus monkey, bovine, pig, rat, tree-shrew, bushbaby, mouse, bat, horse, cat, sheep and dog) and examined mammalian PSGL-1 interactions with human selectins.
17868453	5	94	dep	human	737:741	arg1	cat					830:832	cat	830:832	cat	830:832	Therefore, we performed multiple sequence alignment of PSGL-1 amino acid sequences of 14 mammals (human, chimpanzee, rhesus monkey, bovine, pig, rat, tree-shrew, bushbaby, mouse, bat, horse, cat, sheep and dog) and examined mammalian PSGL-1 interactions with human selectins.
17868453	2	95	gly	O-glycosylation	271:285	arg1	threonine					303:311	a N-terminal threonine	290:311	a N-terminal threonine	290:311	Core-2 O-glycosylation of a N-terminal threonine and sulfation of at least one tyrosine residue of PSGL-1 are required for L- and P-selectin binding.
17868453	2	95	gly	O-glycosylation	271:285	arg1	residue					352:358	at least one tyrosine residue	330:358	at least one tyrosine residue of PSGL-1	330:368	Core-2 O-glycosylation of a N-terminal threonine and sulfation of at least one tyrosine residue of PSGL-1 are required for L- and P-selectin binding.
17868453	2	95	gly	O-glycosylation	271:285	arg1	PSGL-1					363:368	PSGL-1	363:368	PSGL-1	363:368	Core-2 O-glycosylation of a N-terminal threonine and sulfation of at least one tyrosine residue of PSGL-1 are required for L- and P-selectin binding.
17868453	2	95	gly	O-glycosylation	271:285	arg1	P-selectin					394:403	P-selectin	394:403	P-selectin	394:403	Core-2 O-glycosylation of a N-terminal threonine and sulfation of at least one tyrosine residue of PSGL-1 are required for L- and P-selectin binding.
17868453	2	95	gly	O-glycosylation	271:285	arg1	L-					387:388	L-	387:388	L-	387:388	Core-2 O-glycosylation of a N-terminal threonine and sulfation of at least one tyrosine residue of PSGL-1 are required for L- and P-selectin binding.
17868453	13	96	theme	PSGL-1-dependent	1776:1791	arg1	rolling					1793:1799	PSGL-1-dependent rolling	1776:1799	PSGL-1-dependent rolling on P-selectin	1776:1813	The moesin binding residues that serve as adaptor between PSGL-1 and Syk, and are involved in regulating PSGL-1-dependent rolling on P-selectin are perfectly conserved in all analyzed mammalian sequences.
17868453	19	97	with	interactions	2743:2754	arg1	selectins					2761:2769	selectins	2761:2769	selectins	2761:2769	Functional assays reveal a critical role for post-translational modifications in regulating mammalian PSGL-1 interactions with selectins.
17868453	1	98	from	leukocytes	184:193	arg1	lesions					211:217	inflammatory lesions	198:217	inflammatory lesions	198:217	BACKGROUND: P-selectin glycoprotein ligand-1 (PSGL-1) plays a critical role in recruiting leukocytes in inflammatory lesions by mediating leukocyte rolling on selectins.
17868453	10	99	from	Thr-57	1412:1417	arg1	human					1422:1426	human	1422:1426	human	1422:1426	It lies between the conserved N-terminal O-glycosylated threonine (Thr-57 in human) and the transmembrane domain, and contains a central region exhibiting a variable number of decameric repeats (DR).
17868453	5	100	dep	mammals	728:734	arg1	human					737:741	human	737:741	human	737:741	Therefore, we performed multiple sequence alignment of PSGL-1 amino acid sequences of 14 mammals (human, chimpanzee, rhesus monkey, bovine, pig, rat, tree-shrew, bushbaby, mouse, bat, horse, cat, sheep and dog) and examined mammalian PSGL-1 interactions with human selectins.
17868453	4	101	theme	evolutionary	534:545	arg1	conservation					547:558	the evolutionary conservation	530:558	the evolutionary conservation of selectin binding site on PSGL-1	530:593	In addition, the evolutionary conservation of selectin binding site on PSGL-1 has not been previously examined in detail.
17868453	8	102	theme	core-2	1209:1214	arg1	O-glycosylation					1216:1230	the core-2 O-glycosylation	1205:1230	the core-2 O-glycosylation of a N-terminal threonine	1205:1256	However, each species exhibits at least one tyrosine sulfation site and, except in horse and dog, a T [D/E]PP [D/E] motif associated to the core-2 O-glycosylation of a N-terminal threonine.
17868453	18	103	theme	PSGL-1	2555:2560	arg1	N-terminus					2562:2571	PSGL-1 N-terminus	2555:2571	PSGL-1 N-terminus	2555:2571	CONCLUSION: These observations show that PSGL-1 amino acid sequence of the transmembrane and cytoplasmic domains are well conserved and that, despite a poor conservation of PSGL-1 N-terminus, L- and P-selectin binding sites are evolutionary conserved.
17868453	2	104	theme	tyrosine	343:350	arg1	PSGL-1					363:368	PSGL-1	363:368	PSGL-1	363:368	Core-2 O-glycosylation of a N-terminal threonine and sulfation of at least one tyrosine residue of PSGL-1 are required for L- and P-selectin binding.
17868453	2	104	theme	tyrosine	343:350	arg1	residue					352:358	at least one tyrosine residue	330:358	at least one tyrosine residue of PSGL-1	330:368	Core-2 O-glycosylation of a N-terminal threonine and sulfation of at least one tyrosine residue of PSGL-1 are required for L- and P-selectin binding.
17868453	10	105	dep	threonine	1401:1409	arg1	Thr-57					1412:1417	Thr-57	1412:1417	Thr-57	1412:1417	It lies between the conserved N-terminal O-glycosylated threonine (Thr-57 in human) and the transmembrane domain, and contains a central region exhibiting a variable number of decameric repeats (DR).
17868453	6	106	theme	9/14	1016:1019	arg1	species					1021:1027	9/14 species	1016:1027	9/14 species	1016:1027	RESULTS: A signal peptide was predicted in each sequence and a propeptide cleavage site was found in 9/14 species.
17868453	18	107	theme	PSGL-1	2423:2428	arg1	sequence					2441:2448	PSGL-1 amino acid sequence	2423:2448	PSGL-1 amino acid sequence of the transmembrane and cytoplasmic domains	2423:2493	CONCLUSION: These observations show that PSGL-1 amino acid sequence of the transmembrane and cytoplasmic domains are well conserved and that, despite a poor conservation of PSGL-1 N-terminus, L- and P-selectin binding sites are evolutionary conserved.
17868453	8	108	theme	N-terminal	1237:1246	arg1	threonine					1248:1256	a N-terminal threonine	1235:1256	a N-terminal threonine	1235:1256	However, each species exhibits at least one tyrosine sulfation site and, except in horse and dog, a T [D/E]PP [D/E] motif associated to the core-2 O-glycosylation of a N-terminal threonine.
17868453	8	109	gly	O-glycosylation	1216:1230	arg1	threonine					1248:1256	a N-terminal threonine	1235:1256	a N-terminal threonine	1235:1256	However, each species exhibits at least one tyrosine sulfation site and, except in horse and dog, a T [D/E]PP [D/E] motif associated to the core-2 O-glycosylation of a N-terminal threonine.
17868453	14	110	theme	N-terminal	1914:1923	arg1	sequence					1925:1932	PSGL-1 N-terminal sequence	1907:1932	PSGL-1 N-terminal sequence	1907:1932	Despite a poor conservation of PSGL-1 N-terminal sequence, CHO cells co-expressing human glycosyltransferases and human, bovine, pig or rat PSGL-1 efficiently rolled on human L- or P-selectin.
17868453	10	111	theme	decameric	1521:1529	arg1	DR					1540:1541	DR	1540:1541	DR	1540:1541	It lies between the conserved N-terminal O-glycosylated threonine (Thr-57 in human) and the transmembrane domain, and contains a central region exhibiting a variable number of decameric repeats (DR).
17868453	10	111	theme	decameric	1521:1529	arg1	repeats					1531:1537	decameric repeats	1521:1537	decameric repeats (DR)	1521:1542	It lies between the conserved N-terminal O-glycosylated threonine (Thr-57 in human) and the transmembrane domain, and contains a central region exhibiting a variable number of decameric repeats (DR).
17868453	0	112	theme	P-selectin	29:38	arg1	ligand-1					53:60	P-selectin glycoprotein ligand-1	29:60	P-selectin glycoprotein ligand-1	29:60	Evolutionary conservation of P-selectin glycoprotein ligand-1 primary structure and function.
17868453	1	113	theme	glycoprotein	117:128	arg1	PSGL-1					140:145	PSGL-1	140:145	PSGL-1	140:145	BACKGROUND: P-selectin glycoprotein ligand-1 (PSGL-1) plays a critical role in recruiting leukocytes in inflammatory lesions by mediating leukocyte rolling on selectins.
17868453	1	113	theme	glycoprotein	117:128	arg1	ligand-1					130:137	P-selectin glycoprotein ligand-1	106:137	P-selectin glycoprotein ligand-1 (PSGL-1)	106:146	BACKGROUND: P-selectin glycoprotein ligand-1 (PSGL-1) plays a critical role in recruiting leukocytes in inflammatory lesions by mediating leukocyte rolling on selectins.
17868453	10	114	theme	O-glycosylated	1386:1399	arg1	threonine					1401:1409	the conserved N-terminal O-glycosylated threonine	1361:1409	the conserved N-terminal O-glycosylated threonine (Thr-57 in human)	1361:1427	It lies between the conserved N-terminal O-glycosylated threonine (Thr-57 in human) and the transmembrane domain, and contains a central region exhibiting a variable number of decameric repeats (DR).
17868453	3	115	theme	PSGL-1	491:496	arg1	structure					506:514	PSGL-1 primary structure	491:514	PSGL-1 primary structure	491:514	Little information is available on the intra- and inter-species evolution of PSGL-1 primary structure.
17868453	0	116	theme	ligand-1	53:60	arg1	conservation					13:24	Evolutionary conservation	0:24	Evolutionary conservation of P-selectin glycoprotein ligand-1	0:60	Evolutionary conservation of P-selectin glycoprotein ligand-1 primary structure and function.
17868453	14	117	theme	poor	1886:1889	arg1	conservation					1891:1902	a poor conservation	1884:1902	a poor conservation of PSGL-1 N-terminal sequence	1884:1932	Despite a poor conservation of PSGL-1 N-terminal sequence, CHO cells co-expressing human glycosyltransferases and human, bovine, pig or rat PSGL-1 efficiently rolled on human L- or P-selectin.
17868453	6	118	theme	propeptide	978:987	arg1	site					998:1001	a propeptide cleavage site	976:1001	a propeptide cleavage site	976:1001	RESULTS: A signal peptide was predicted in each sequence and a propeptide cleavage site was found in 9/14 species.
17868453	10	119	theme	conserved	1365:1373	arg1	threonine					1401:1409	the conserved N-terminal O-glycosylated threonine	1361:1409	the conserved N-terminal O-glycosylated threonine (Thr-57 in human)	1361:1427	It lies between the conserved N-terminal O-glycosylated threonine (Thr-57 in human) and the transmembrane domain, and contains a central region exhibiting a variable number of decameric repeats (DR).
17868453	1	120	gly	glycoprotein	117:128	arg1	glycoprotein					117:128	P-selectin glycoprotein ligand-1	106:137	P-selectin glycoprotein ligand-1 (PSGL-1)	106:146	BACKGROUND: P-selectin glycoprotein ligand-1 (PSGL-1) plays a critical role in recruiting leukocytes in inflammatory lesions by mediating leukocyte rolling on selectins.
17868453	15	121	theme	bovine	2156:2161	arg1	neutrophils					2163:2173	human or bovine neutrophils	2147:2173	human or bovine neutrophils	2147:2173	By contrast, pig or rat neutrophils were much less efficiently recruited than human or bovine neutrophils on human selectins.
17868453	4	122	theme	binding	572:578	arg1	site					580:583	selectin binding site	563:583	selectin binding site	563:583	In addition, the evolutionary conservation of selectin binding site on PSGL-1 has not been previously examined in detail.
17868453	15	123	theme	human	2147:2151	arg1	neutrophils					2163:2173	human or bovine neutrophils	2147:2173	human or bovine neutrophils	2147:2173	By contrast, pig or rat neutrophils were much less efficiently recruited than human or bovine neutrophils on human selectins.
17868453	0	124	gly	glycoprotein	40:51	arg1	glycoprotein					40:51	P-selectin glycoprotein ligand-1	29:60	P-selectin glycoprotein ligand-1	29:60	Evolutionary conservation of P-selectin glycoprotein ligand-1 primary structure and function.
17868453	14	125	theme	sequence	1925:1932	arg1	conservation					1891:1902	a poor conservation	1884:1902	a poor conservation of PSGL-1 N-terminal sequence	1884:1932	Despite a poor conservation of PSGL-1 N-terminal sequence, CHO cells co-expressing human glycosyltransferases and human, bovine, pig or rat PSGL-1 efficiently rolled on human L- or P-selectin.
17868453	3	126	theme	structure	506:514	arg1	evolution					478:486	the intra- and inter-species evolution	449:486	the intra- and inter-species evolution of PSGL-1 primary structure	449:514	Little information is available on the intra- and inter-species evolution of PSGL-1 primary structure.
17868453	18	127	theme	acid	2436:2439	arg1	sequence					2441:2448	PSGL-1 amino acid sequence	2423:2448	PSGL-1 amino acid sequence of the transmembrane and cytoplasmic domains	2423:2493	CONCLUSION: These observations show that PSGL-1 amino acid sequence of the transmembrane and cytoplasmic domains are well conserved and that, despite a poor conservation of PSGL-1 N-terminus, L- and P-selectin binding sites are evolutionary conserved.
17868453	9	128	theme	acids	1296:1300	arg1	acids					1296:1300	250-280 amino acids long	1282:1305	250-280 amino acids long	1282:1305	A mucin-like domain of 250-280 amino acids long was disclosed in all studied species.
17868453	9	128	theme	acids	1296:1300	arg1	domain					1272:1277	A mucin-like domain	1259:1277	A mucin-like domain of 250-280 amino acids long	1259:1305	A mucin-like domain of 250-280 amino acids long was disclosed in all studied species.
21186285	3	0	theme	protein	605:611	arg1	stability					613:621	protein stability	605:621	protein stability	605:621	Here, we used site-directed mutagenesis to the four predicted N-glycosylation sites of P2X(3) receptor (Asn(139), Asn(170), Asn(194) and Asn(290)) and performed comparative analysis of the role of N-glycans on protein stability, plasma membrane delivery, trimer formation and inward currents.
21186285	7	1	theme	/Asn	1267:1270	arg1	mutant					1284:1289	the Asn(139)/Asn(290) double mutant	1255:1289	the Asn(139)/Asn(290) double mutant	1255:1289	All double mutants containing Asn(170) mutation or the Asn(139)/Asn(290) double mutant are instead almost unable to assemble into a functional trimeric structure.
21186285	7	1	theme	/Asn	1267:1270	arg1	unable					1310:1315	unable	1310:1315	unable	1310:1315	All double mutants containing Asn(170) mutation or the Asn(139)/Asn(290) double mutant are instead almost unable to assemble into a functional trimeric structure.
21186285	1	2	theme	opening	251:257	arg1	level					171:175	the level	167:175	the level of multisubunit assembly, protein trafficking, ligand binding and channel opening	167:257	N-Glycosylation affects the function of ion channels at the level of multisubunit assembly, protein trafficking, ligand binding and channel opening.
21186285	0	3	theme	receptor	79:86	arg1	assembly					36:43	oligomeric assembly	25:43	oligomeric assembly	25:43	N-Glycans mutations rule oligomeric assembly and functional expression of P2X3 receptor for extracellular ATP.
21186285	0	3	theme	receptor	79:86	arg1	expression					60:69	functional expression	49:69	functional expression	49:69	N-Glycans mutations rule oligomeric assembly and functional expression of P2X3 receptor for extracellular ATP.
21186285	9	4	from	role	1580:1583	arg1	folding					1614:1620	proper folding	1607:1620	proper folding	1607:1620	These results improve our knowledge about the role of N-glycosylation in proper folding and oligomeric association of P2X(3) receptor.
21186285	9	4	from	role	1580:1583	arg1	association					1637:1647	oligomeric association	1626:1647	oligomeric association	1626:1647	These results improve our knowledge about the role of N-glycosylation in proper folding and oligomeric association of P2X(3) receptor.
21186285	3	5	theme	N-glycans	592:600	arg1	role					584:587	the role	580:587	the role of N-glycans	580:600	Here, we used site-directed mutagenesis to the four predicted N-glycosylation sites of P2X(3) receptor (Asn(139), Asn(170), Asn(194) and Asn(290)) and performed comparative analysis of the role of N-glycans on protein stability, plasma membrane delivery, trimer formation and inward currents.
21186285	8	6	dep	residue	1504:1510	arg1	170					1516:1518	170	1516:1518	170	1516:1518	The main emerging finding is that the inability to assemble into trimers might account for the impaired function in P2X(3) mutants where residue Asn(170) is replaced.
21186285	8	6	dep	residue	1504:1510	arg1	Asn					1512:1514	Asn	1512:1514	residue Asn(170)	1504:1519	The main emerging finding is that the inability to assemble into trimers might account for the impaired function in P2X(3) mutants where residue Asn(170) is replaced.
21186285	2	7	theme	proteins	290:297	arg1	majority					269:276	the majority	265:276	the majority of membrane proteins	265:297	Like the majority of membrane proteins, ionotropic P2X receptors for extracellular ATP are glycosylated in their extracellular moiety.
21186285	3	8	theme	role	584:587	arg1	analysis					568:575	comparative analysis	556:575	comparative analysis of the role of N-glycans	556:600	Here, we used site-directed mutagenesis to the four predicted N-glycosylation sites of P2X(3) receptor (Asn(139), Asn(170), Asn(194) and Asn(290)) and performed comparative analysis of the role of N-glycans on protein stability, plasma membrane delivery, trimer formation and inward currents.
21186285	7	9	contain	containing	1223:1232	arg1	mutants					1215:1221	All double mutants	1204:1221	All double mutants containing Asn(170) mutation	1204:1250	All double mutants containing Asn(170) mutation or the Asn(139)/Asn(290) double mutant are instead almost unable to assemble into a functional trimeric structure.
21186285	7	9	contain	containing	1223:1232	arg2	mutation					1243:1250	Asn(170) mutation	1234:1250	Asn(170) mutation	1234:1250	All double mutants containing Asn(170) mutation or the Asn(139)/Asn(290) double mutant are instead almost unable to assemble into a functional trimeric structure.
21186285	0	10	theme	extracellular	92:104	arg1	ATP					106:108	extracellular ATP	92:108	extracellular ATP	92:108	N-Glycans mutations rule oligomeric assembly and functional expression of P2X3 receptor for extracellular ATP.
21186285	3	11	theme	plasma	624:629	arg1	delivery					640:647	plasma membrane delivery	624:647	plasma membrane delivery	624:647	Here, we used site-directed mutagenesis to the four predicted N-glycosylation sites of P2X(3) receptor (Asn(139), Asn(170), Asn(194) and Asn(290)) and performed comparative analysis of the role of N-glycans on protein stability, plasma membrane delivery, trimer formation and inward currents.
21186285	7	12	theme	Asn	1259:1261	arg1	mutant					1284:1289	the Asn(139)/Asn(290) double mutant	1255:1289	the Asn(139)/Asn(290) double mutant	1255:1289	All double mutants containing Asn(170) mutation or the Asn(139)/Asn(290) double mutant are instead almost unable to assemble into a functional trimeric structure.
21186285	7	12	theme	Asn	1259:1261	arg1	unable					1310:1315	unable	1310:1315	unable	1310:1315	All double mutants containing Asn(170) mutation or the Asn(139)/Asn(290) double mutant are instead almost unable to assemble into a functional trimeric structure.
21186285	2	13	theme	membrane	281:288	arg1	proteins					290:297	membrane proteins	281:297	membrane proteins	281:297	Like the majority of membrane proteins, ionotropic P2X receptors for extracellular ATP are glycosylated in their extracellular moiety.
21186285	7	14	theme	functional	1336:1345	arg1	structure					1356:1364	a functional trimeric structure	1334:1364	a functional trimeric structure	1334:1364	All double mutants containing Asn(170) mutation or the Asn(139)/Asn(290) double mutant are instead almost unable to assemble into a functional trimeric structure.
21186285	6	15	theme	receptor	1186:1193	arg1	feature					1195:1201	any tested receptor feature	1175:1201	any tested receptor feature	1175:1201	Asn(194) and Asn(290) are the most dispensable, since even their simultaneous mutation does not affect any tested receptor feature.
21186285	3	16	theme	membrane	631:638	arg1	delivery					640:647	plasma membrane delivery	624:647	plasma membrane delivery	624:647	Here, we used site-directed mutagenesis to the four predicted N-glycosylation sites of P2X(3) receptor (Asn(139), Asn(170), Asn(194) and Asn(290)) and performed comparative analysis of the role of N-glycans on protein stability, plasma membrane delivery, trimer formation and inward currents.
21186285	3	17	theme	P2X	482:484	arg1	receptor					489:496	P2X(3) receptor	482:496	P2X(3) receptor (Asn(139), Asn(170), Asn(194) and Asn(290))	482:540	Here, we used site-directed mutagenesis to the four predicted N-glycosylation sites of P2X(3) receptor (Asn(139), Asn(170), Asn(194) and Asn(290)) and performed comparative analysis of the role of N-glycans on protein stability, plasma membrane delivery, trimer formation and inward currents.
21186285	8	18	theme	P2X	1483:1485	arg1	mutants					1490:1496	P2X(3) mutants	1483:1496	P2X(3) mutants where residue Asn(170) is replaced	1483:1531	The main emerging finding is that the inability to assemble into trimers might account for the impaired function in P2X(3) mutants where residue Asn(170) is replaced.
21186285	6	19	theme	tested	1179:1184	arg1	feature					1195:1201	any tested receptor feature	1175:1201	any tested receptor feature	1175:1201	Asn(194) and Asn(290) are the most dispensable, since even their simultaneous mutation does not affect any tested receptor feature.
21186285	7	20	theme	trimeric	1347:1354	arg1	structure					1356:1364	a functional trimeric structure	1334:1364	a functional trimeric structure	1334:1364	All double mutants containing Asn(170) mutation or the Asn(139)/Asn(290) double mutant are instead almost unable to assemble into a functional trimeric structure.
21186285	3	21	dep	receptor	489:496	arg1	Asn					509:511	Asn(170)	509:516	Asn(170)	509:516	Here, we used site-directed mutagenesis to the four predicted N-glycosylation sites of P2X(3) receptor (Asn(139), Asn(170), Asn(194) and Asn(290)) and performed comparative analysis of the role of N-glycans on protein stability, plasma membrane delivery, trimer formation and inward currents.
21186285	3	21	dep	receptor	489:496	arg1	Asn					499:501	Asn(139)	499:506	Asn(139)	499:506	Here, we used site-directed mutagenesis to the four predicted N-glycosylation sites of P2X(3) receptor (Asn(139), Asn(170), Asn(194) and Asn(290)) and performed comparative analysis of the role of N-glycans on protein stability, plasma membrane delivery, trimer formation and inward currents.
21186285	3	21	dep	receptor	489:496	arg1	Asn					532:534	Asn(290)	532:539	Asn(290)	532:539	Here, we used site-directed mutagenesis to the four predicted N-glycosylation sites of P2X(3) receptor (Asn(139), Asn(170), Asn(194) and Asn(290)) and performed comparative analysis of the role of N-glycans on protein stability, plasma membrane delivery, trimer formation and inward currents.
21186285	3	21	dep	receptor	489:496	arg1	Asn					519:521	Asn(194)	519:526	Asn(194)	519:526	Here, we used site-directed mutagenesis to the four predicted N-glycosylation sites of P2X(3) receptor (Asn(139), Asn(170), Asn(194) and Asn(290)) and performed comparative analysis of the role of N-glycans on protein stability, plasma membrane delivery, trimer formation and inward currents.
21186285	3	22	theme	predicted	447:455	arg1	sites					473:477	the four predicted N-glycosylation sites	438:477	the four predicted N-glycosylation sites of P2X(3) receptor (Asn(139), Asn(170), Asn(194) and Asn(290))	438:540	Here, we used site-directed mutagenesis to the four predicted N-glycosylation sites of P2X(3) receptor (Asn(139), Asn(170), Asn(194) and Asn(290)) and performed comparative analysis of the role of N-glycans on protein stability, plasma membrane delivery, trimer formation and inward currents.
21186285	3	22	theme	predicted	447:455	arg1	receptor					489:496	P2X(3) receptor	482:496	P2X(3) receptor (Asn(139), Asn(170), Asn(194) and Asn(290))	482:540	Here, we used site-directed mutagenesis to the four predicted N-glycosylation sites of P2X(3) receptor (Asn(139), Asn(170), Asn(194) and Asn(290)) and performed comparative analysis of the role of N-glycans on protein stability, plasma membrane delivery, trimer formation and inward currents.
21186285	3	23	theme	comparative	556:566	arg1	analysis					568:575	comparative analysis	556:575	comparative analysis of the role of N-glycans	556:600	Here, we used site-directed mutagenesis to the four predicted N-glycosylation sites of P2X(3) receptor (Asn(139), Asn(170), Asn(194) and Asn(290)) and performed comparative analysis of the role of N-glycans on protein stability, plasma membrane delivery, trimer formation and inward currents.
21186285	4	24	theme	primary	847:853	arg1	loss					855:858	a primary loss	845:858	a primary loss in protein content	845:877	We have found that in transiently transfected HEK293 cells, Asn(170) is apparently the most important site for receptor stability, since its mutation causes a primary loss in protein content and indirect failure in membrane expression, oligomeric association and inward current responses.
21186285	5	25	theme	stronger	982:989	arg1	effects					991:997	Even stronger effects	977:997	Even stronger effects	977:997	Even stronger effects are obtained when mutating Thr(172) in the same glycosylation consensus.
21186285	1	26	theme	multisubunit	180:191	arg1	assembly					193:200	multisubunit assembly	180:200	multisubunit assembly	180:200	N-Glycosylation affects the function of ion channels at the level of multisubunit assembly, protein trafficking, ligand binding and channel opening.
21186285	0	27	theme	N-Glycans	0:8	arg1	mutations					10:18	N-Glycans mutations	0:18	N-Glycans mutations	0:18	N-Glycans mutations rule oligomeric assembly and functional expression of P2X3 receptor for extracellular ATP.
21186285	3	28	theme	trimer	650:655	arg1	formation					657:665	trimer formation	650:665	trimer formation	650:665	Here, we used site-directed mutagenesis to the four predicted N-glycosylation sites of P2X(3) receptor (Asn(139), Asn(170), Asn(194) and Asn(290)) and performed comparative analysis of the role of N-glycans on protein stability, plasma membrane delivery, trimer formation and inward currents.
21186285	7	29	theme	double	1277:1282	arg1	mutant					1284:1289	the Asn(139)/Asn(290) double mutant	1255:1289	the Asn(139)/Asn(290) double mutant	1255:1289	All double mutants containing Asn(170) mutation or the Asn(139)/Asn(290) double mutant are instead almost unable to assemble into a functional trimeric structure.
21186285	7	29	theme	double	1277:1282	arg1	unable					1310:1315	unable	1310:1315	unable	1310:1315	All double mutants containing Asn(170) mutation or the Asn(139)/Asn(290) double mutant are instead almost unable to assemble into a functional trimeric structure.
21186285	2	30	theme	P2X	311:313	arg1	receptors					315:323	ionotropic P2X receptors	300:323	ionotropic P2X receptors for extracellular ATP	300:345	Like the majority of membrane proteins, ionotropic P2X receptors for extracellular ATP are glycosylated in their extracellular moiety.
21186285	1	31	theme	assembly	193:200	arg1	level					171:175	the level	167:175	the level of multisubunit assembly, protein trafficking, ligand binding and channel opening	167:257	N-Glycosylation affects the function of ion channels at the level of multisubunit assembly, protein trafficking, ligand binding and channel opening.
21186285	0	32	theme	oligomeric	25:34	arg1	assembly					36:43	oligomeric assembly	25:43	oligomeric assembly	25:43	N-Glycans mutations rule oligomeric assembly and functional expression of P2X3 receptor for extracellular ATP.
21186285	5	33	theme	same	1042:1045	arg1	consensus					1061:1069	the same glycosylation consensus	1038:1069	the same glycosylation consensus	1038:1069	Even stronger effects are obtained when mutating Thr(172) in the same glycosylation consensus.
21186285	4	34	theme	receptor	799:806	arg1	stability					808:816	receptor stability	799:816	receptor stability	799:816	We have found that in transiently transfected HEK293 cells, Asn(170) is apparently the most important site for receptor stability, since its mutation causes a primary loss in protein content and indirect failure in membrane expression, oligomeric association and inward current responses.
21186285	4	35	theme	transfected	722:732	arg1	cells					741:745	transiently transfected HEK293 cells	710:745	transiently transfected HEK293 cells	710:745	We have found that in transiently transfected HEK293 cells, Asn(170) is apparently the most important site for receptor stability, since its mutation causes a primary loss in protein content and indirect failure in membrane expression, oligomeric association and inward current responses.
21186285	2	36	theme	ionotropic	300:309	arg1	receptors					315:323	ionotropic P2X receptors	300:323	ionotropic P2X receptors for extracellular ATP	300:345	Like the majority of membrane proteins, ionotropic P2X receptors for extracellular ATP are glycosylated in their extracellular moiety.
21186285	9	37	theme	N-glycosylation	1588:1602	arg1	role					1580:1583	the role	1576:1583	the role of N-glycosylation in proper folding and oligomeric association of P2X(3) receptor	1576:1666	These results improve our knowledge about the role of N-glycosylation in proper folding and oligomeric association of P2X(3) receptor.
21186285	4	38	theme	membrane	903:910	arg1	expression					912:921	membrane expression	903:921	membrane expression	903:921	We have found that in transiently transfected HEK293 cells, Asn(170) is apparently the most important site for receptor stability, since its mutation causes a primary loss in protein content and indirect failure in membrane expression, oligomeric association and inward current responses.
21186285	5	39	theme	glycosylation	1047:1059	arg1	consensus					1061:1069	the same glycosylation consensus	1038:1069	the same glycosylation consensus	1038:1069	Even stronger effects are obtained when mutating Thr(172) in the same glycosylation consensus.
21186285	9	40	theme	oligomeric	1626:1635	arg1	association					1637:1647	oligomeric association	1626:1647	oligomeric association	1626:1647	These results improve our knowledge about the role of N-glycosylation in proper folding and oligomeric association of P2X(3) receptor.
21186285	1	41	theme	protein	203:209	arg1	trafficking					211:221	protein trafficking	203:221	protein trafficking	203:221	N-Glycosylation affects the function of ion channels at the level of multisubunit assembly, protein trafficking, ligand binding and channel opening.
21186285	3	42	theme	site-directed	409:421	arg1	mutagenesis					423:433	site-directed mutagenesis	409:433	site-directed mutagenesis	409:433	Here, we used site-directed mutagenesis to the four predicted N-glycosylation sites of P2X(3) receptor (Asn(139), Asn(170), Asn(194) and Asn(290)) and performed comparative analysis of the role of N-glycans on protein stability, plasma membrane delivery, trimer formation and inward currents.
21186285	4	43	from	failure	892:898	arg1	content					871:877	protein content	863:877	protein content	863:877	We have found that in transiently transfected HEK293 cells, Asn(170) is apparently the most important site for receptor stability, since its mutation causes a primary loss in protein content and indirect failure in membrane expression, oligomeric association and inward current responses.
21186285	2	44	gly	glycosylated	351:362	arg2	receptors					315:323	ionotropic P2X receptors	300:323	ionotropic P2X receptors for extracellular ATP	300:345	Like the majority of membrane proteins, ionotropic P2X receptors for extracellular ATP are glycosylated in their extracellular moiety.
21186285	2	44	gly	glycosylated	351:362	arg1	moiety					387:392	their extracellular moiety	367:392	their extracellular moiety	367:392	Like the majority of membrane proteins, ionotropic P2X receptors for extracellular ATP are glycosylated in their extracellular moiety.
21186285	2	44	gly	glycosylated	351:362	arg1	receptors					315:323	ionotropic P2X receptors	300:323	ionotropic P2X receptors for extracellular ATP	300:345	Like the majority of membrane proteins, ionotropic P2X receptors for extracellular ATP are glycosylated in their extracellular moiety.
21186285	3	45	theme	N-glycosylation	457:471	arg1	sites					473:477	the four predicted N-glycosylation sites	438:477	the four predicted N-glycosylation sites of P2X(3) receptor (Asn(139), Asn(170), Asn(194) and Asn(290))	438:540	Here, we used site-directed mutagenesis to the four predicted N-glycosylation sites of P2X(3) receptor (Asn(139), Asn(170), Asn(194) and Asn(290)) and performed comparative analysis of the role of N-glycans on protein stability, plasma membrane delivery, trimer formation and inward currents.
21186285	3	45	theme	N-glycosylation	457:471	arg1	receptor					489:496	P2X(3) receptor	482:496	P2X(3) receptor (Asn(139), Asn(170), Asn(194) and Asn(290))	482:540	Here, we used site-directed mutagenesis to the four predicted N-glycosylation sites of P2X(3) receptor (Asn(139), Asn(170), Asn(194) and Asn(290)) and performed comparative analysis of the role of N-glycans on protein stability, plasma membrane delivery, trimer formation and inward currents.
21186285	7	46	theme	Asn	1234:1236	arg1	mutation					1243:1250	Asn(170) mutation	1234:1250	Asn(170) mutation	1234:1250	All double mutants containing Asn(170) mutation or the Asn(139)/Asn(290) double mutant are instead almost unable to assemble into a functional trimeric structure.
21186285	1	47	theme	trafficking	211:221	arg1	level					171:175	the level	167:175	the level of multisubunit assembly, protein trafficking, ligand binding and channel opening	167:257	N-Glycosylation affects the function of ion channels at the level of multisubunit assembly, protein trafficking, ligand binding and channel opening.
21186285	4	48	theme	protein	863:869	arg1	content					871:877	protein content	863:877	protein content	863:877	We have found that in transiently transfected HEK293 cells, Asn(170) is apparently the most important site for receptor stability, since its mutation causes a primary loss in protein content and indirect failure in membrane expression, oligomeric association and inward current responses.
21186285	5	49	from	Thr	1026:1028	arg1	consensus					1061:1069	the same glycosylation consensus	1038:1069	the same glycosylation consensus	1038:1069	Even stronger effects are obtained when mutating Thr(172) in the same glycosylation consensus.
21186285	7	50	theme	double	1208:1213	arg1	mutants					1215:1221	All double mutants	1204:1221	All double mutants containing Asn(170) mutation	1204:1250	All double mutants containing Asn(170) mutation or the Asn(139)/Asn(290) double mutant are instead almost unable to assemble into a functional trimeric structure.
21186285	8	51	theme	main	1371:1374	arg1	finding					1385:1391	The main emerging finding	1367:1391	The main emerging finding	1367:1391	The main emerging finding is that the inability to assemble into trimers might account for the impaired function in P2X(3) mutants where residue Asn(170) is replaced.
21186285	4	52	theme	indirect	883:890	arg1	failure					892:898	indirect failure	883:898	indirect failure	883:898	We have found that in transiently transfected HEK293 cells, Asn(170) is apparently the most important site for receptor stability, since its mutation causes a primary loss in protein content and indirect failure in membrane expression, oligomeric association and inward current responses.
21186285	3	53	used	used	404:407	arg2	we					401:402	we	401:402	we	401:402	Here, we used site-directed mutagenesis to the four predicted N-glycosylation sites of P2X(3) receptor (Asn(139), Asn(170), Asn(194) and Asn(290)) and performed comparative analysis of the role of N-glycans on protein stability, plasma membrane delivery, trimer formation and inward currents.
21186285	4	54	theme	HEK293	734:739	arg1	cells					741:745	transiently transfected HEK293 cells	710:745	transiently transfected HEK293 cells	710:745	We have found that in transiently transfected HEK293 cells, Asn(170) is apparently the most important site for receptor stability, since its mutation causes a primary loss in protein content and indirect failure in membrane expression, oligomeric association and inward current responses.
21186285	0	55	theme	functional	49:58	arg1	expression					60:69	functional expression	49:69	functional expression	49:69	N-Glycans mutations rule oligomeric assembly and functional expression of P2X3 receptor for extracellular ATP.
21186285	8	56	theme	emerging	1376:1383	arg1	finding					1385:1391	The main emerging finding	1367:1391	The main emerging finding	1367:1391	The main emerging finding is that the inability to assemble into trimers might account for the impaired function in P2X(3) mutants where residue Asn(170) is replaced.
21186285	6	57	theme	simultaneous	1137:1148	arg1	mutation					1150:1157	even their simultaneous mutation	1126:1157	even their simultaneous mutation	1126:1157	Asn(194) and Asn(290) are the most dispensable, since even their simultaneous mutation does not affect any tested receptor feature.
21186285	4	58	from	site	790:793	arg1	cells					741:745	transiently transfected HEK293 cells	710:745	transiently transfected HEK293 cells	710:745	We have found that in transiently transfected HEK293 cells, Asn(170) is apparently the most important site for receptor stability, since its mutation causes a primary loss in protein content and indirect failure in membrane expression, oligomeric association and inward current responses.
21186285	3	59	gly	N-glycosylation	457:471	arg2	sites					473:477	the four predicted N-glycosylation sites	438:477	the four predicted N-glycosylation sites of P2X(3) receptor (Asn(139), Asn(170), Asn(194) and Asn(290))	438:540	Here, we used site-directed mutagenesis to the four predicted N-glycosylation sites of P2X(3) receptor (Asn(139), Asn(170), Asn(194) and Asn(290)) and performed comparative analysis of the role of N-glycans on protein stability, plasma membrane delivery, trimer formation and inward currents.
21186285	3	59	gly	N-glycosylation	457:471	arg1	receptor					489:496	P2X(3) receptor	482:496	P2X(3) receptor (Asn(139), Asn(170), Asn(194) and Asn(290))	482:540	Here, we used site-directed mutagenesis to the four predicted N-glycosylation sites of P2X(3) receptor (Asn(139), Asn(170), Asn(194) and Asn(290)) and performed comparative analysis of the role of N-glycans on protein stability, plasma membrane delivery, trimer formation and inward currents.
21186285	3	59	gly	N-glycosylation	457:471	arg2	receptor					489:496	P2X(3) receptor	482:496	P2X(3) receptor (Asn(139), Asn(170), Asn(194) and Asn(290))	482:540	Here, we used site-directed mutagenesis to the four predicted N-glycosylation sites of P2X(3) receptor (Asn(139), Asn(170), Asn(194) and Asn(290)) and performed comparative analysis of the role of N-glycans on protein stability, plasma membrane delivery, trimer formation and inward currents.
21186285	3	59	gly	N-glycosylation	457:471	arg2	four					442:445	four	442:445	four	442:445	Here, we used site-directed mutagenesis to the four predicted N-glycosylation sites of P2X(3) receptor (Asn(139), Asn(170), Asn(194) and Asn(290)) and performed comparative analysis of the role of N-glycans on protein stability, plasma membrane delivery, trimer formation and inward currents.
21186285	3	60	theme	receptor	489:496	arg1	sites					473:477	the four predicted N-glycosylation sites	438:477	the four predicted N-glycosylation sites of P2X(3) receptor (Asn(139), Asn(170), Asn(194) and Asn(290))	438:540	Here, we used site-directed mutagenesis to the four predicted N-glycosylation sites of P2X(3) receptor (Asn(139), Asn(170), Asn(194) and Asn(290)) and performed comparative analysis of the role of N-glycans on protein stability, plasma membrane delivery, trimer formation and inward currents.
21186285	3	60	theme	receptor	489:496	arg1	receptor					489:496	P2X(3) receptor	482:496	P2X(3) receptor (Asn(139), Asn(170), Asn(194) and Asn(290))	482:540	Here, we used site-directed mutagenesis to the four predicted N-glycosylation sites of P2X(3) receptor (Asn(139), Asn(170), Asn(194) and Asn(290)) and performed comparative analysis of the role of N-glycans on protein stability, plasma membrane delivery, trimer formation and inward currents.
21186285	4	61	theme	current	958:964	arg1	responses					966:974	inward current responses	951:974	inward current responses	951:974	We have found that in transiently transfected HEK293 cells, Asn(170) is apparently the most important site for receptor stability, since its mutation causes a primary loss in protein content and indirect failure in membrane expression, oligomeric association and inward current responses.
21186285	3	62	theme	inward	671:676	arg1	currents					678:685	inward currents	671:685	inward currents	671:685	Here, we used site-directed mutagenesis to the four predicted N-glycosylation sites of P2X(3) receptor (Asn(139), Asn(170), Asn(194) and Asn(290)) and performed comparative analysis of the role of N-glycans on protein stability, plasma membrane delivery, trimer formation and inward currents.
21186285	1	63	theme	ion	151:153	arg1	channels					155:162	ion channels	151:162	ion channels	151:162	N-Glycosylation affects the function of ion channels at the level of multisubunit assembly, protein trafficking, ligand binding and channel opening.
21186285	2	64	theme	extracellular	329:341	arg1	ATP					343:345	extracellular ATP	329:345	extracellular ATP	329:345	Like the majority of membrane proteins, ionotropic P2X receptors for extracellular ATP are glycosylated in their extracellular moiety.
21186285	4	65	theme	inward	951:956	arg1	responses					966:974	inward current responses	951:974	inward current responses	951:974	We have found that in transiently transfected HEK293 cells, Asn(170) is apparently the most important site for receptor stability, since its mutation causes a primary loss in protein content and indirect failure in membrane expression, oligomeric association and inward current responses.
21186285	1	66	theme	ligand	224:229	arg1	binding					231:237	ligand binding	224:237	ligand binding	224:237	N-Glycosylation affects the function of ion channels at the level of multisubunit assembly, protein trafficking, ligand binding and channel opening.
21186285	4	67	theme	important	780:788	arg1	Asn					748:750	Asn	748:750	Asn(170)	748:755	We have found that in transiently transfected HEK293 cells, Asn(170) is apparently the most important site for receptor stability, since its mutation causes a primary loss in protein content and indirect failure in membrane expression, oligomeric association and inward current responses.
21186285	4	67	theme	important	780:788	arg1	site					790:793	the most important site	771:793	the most important site for receptor stability	771:816	We have found that in transiently transfected HEK293 cells, Asn(170) is apparently the most important site for receptor stability, since its mutation causes a primary loss in protein content and indirect failure in membrane expression, oligomeric association and inward current responses.
21186285	8	68	from	function	1471:1478	arg1	mutants					1490:1496	P2X(3) mutants	1483:1496	P2X(3) mutants where residue Asn(170) is replaced	1483:1531	The main emerging finding is that the inability to assemble into trimers might account for the impaired function in P2X(3) mutants where residue Asn(170) is replaced.
21186285	4	69	from	loss	855:858	arg1	content					871:877	protein content	863:877	protein content	863:877	We have found that in transiently transfected HEK293 cells, Asn(170) is apparently the most important site for receptor stability, since its mutation causes a primary loss in protein content and indirect failure in membrane expression, oligomeric association and inward current responses.
21186285	1	70	theme	binding	231:237	arg1	level					171:175	the level	167:175	the level of multisubunit assembly, protein trafficking, ligand binding and channel opening	167:257	N-Glycosylation affects the function of ion channels at the level of multisubunit assembly, protein trafficking, ligand binding and channel opening.
21186285	0	71	theme	P2X3	74:77	arg1	receptor					79:86	P2X3 receptor	74:86	P2X3 receptor for extracellular ATP	74:108	N-Glycans mutations rule oligomeric assembly and functional expression of P2X3 receptor for extracellular ATP.
21186285	9	72	theme	P2X	1652:1654	arg1	receptor					1659:1666	P2X(3) receptor	1652:1666	P2X(3) receptor	1652:1666	These results improve our knowledge about the role of N-glycosylation in proper folding and oligomeric association of P2X(3) receptor.
21186285	8	73	theme	impaired	1462:1469	arg1	function					1471:1478	the impaired function	1458:1478	the impaired function in P2X(3) mutants where residue Asn(170) is replaced	1458:1531	The main emerging finding is that the inability to assemble into trimers might account for the impaired function in P2X(3) mutants where residue Asn(170) is replaced.
21186285	2	74	theme	extracellular	373:385	arg1	moiety					387:392	their extracellular moiety	367:392	their extracellular moiety	367:392	Like the majority of membrane proteins, ionotropic P2X receptors for extracellular ATP are glycosylated in their extracellular moiety.
21186285	9	75	theme	proper	1607:1612	arg1	folding					1614:1620	proper folding	1607:1620	proper folding	1607:1620	These results improve our knowledge about the role of N-glycosylation in proper folding and oligomeric association of P2X(3) receptor.
21186285	9	76	theme	receptor	1659:1666	arg1	folding					1614:1620	proper folding	1607:1620	proper folding	1607:1620	These results improve our knowledge about the role of N-glycosylation in proper folding and oligomeric association of P2X(3) receptor.
21186285	9	76	theme	receptor	1659:1666	arg1	association					1637:1647	oligomeric association	1626:1647	oligomeric association	1626:1647	These results improve our knowledge about the role of N-glycosylation in proper folding and oligomeric association of P2X(3) receptor.
21186285	9	77	gly	N-glycosylation	1588:1602	arg1	receptor					1659:1666	P2X(3) receptor	1652:1666	P2X(3) receptor	1652:1666	These results improve our knowledge about the role of N-glycosylation in proper folding and oligomeric association of P2X(3) receptor.
21186285	1	78	theme	channels	155:162	arg1	function					139:146	the function	135:146	the function of ion channels	135:162	N-Glycosylation affects the function of ion channels at the level of multisubunit assembly, protein trafficking, ligand binding and channel opening.
21186285	4	79	theme	oligomeric	924:933	arg1	association					935:945	oligomeric association	924:945	oligomeric association	924:945	We have found that in transiently transfected HEK293 cells, Asn(170) is apparently the most important site for receptor stability, since its mutation causes a primary loss in protein content and indirect failure in membrane expression, oligomeric association and inward current responses.
21186285	1	80	theme	channel	243:249	arg1	opening					251:257	channel opening	243:257	channel opening	243:257	N-Glycosylation affects the function of ion channels at the level of multisubunit assembly, protein trafficking, ligand binding and channel opening.
28531887	8	0	theme	kDa	1112:1114	arg1	masses					1091:1096	molecular masses	1081:1096	molecular masses of 45 kDa, 58 kDa and 69 kDa	1081:1125	Three forms of MT4-MMP with molecular masses of 45 kDa, 58 kDa and 69 kDa were detected.
28531887	0	1	from	Characterization	15:30	arg1	Melanoma					113:120	Melanoma	113:120	Melanoma	113:120	Expression and Characterization of Membrane-Type 4 Matrix Metalloproteinase (MT4-MMP) and its Different Forms in Melanoma.
28531887	9	2	theme	kDa	1244:1246	arg1	form					1248:1251	the 69 kDa form	1237:1251	the 69 kDa form	1237:1251	Further, we demonstrate that the 58 kDa form is the mature protein in the cell membrane, while the 69 kDa form is its precursor found in intracellular compartments.
28531887	9	2	theme	kDa	1244:1246	arg1	precursor					1260:1268	its precursor	1256:1268	its precursor found in intracellular compartments	1256:1304	Further, we demonstrate that the 58 kDa form is the mature protein in the cell membrane, while the 69 kDa form is its precursor found in intracellular compartments.
28531887	12	3	theme	MT4-MMP	1509:1515	arg1	expression					1495:1504	the novel expression	1485:1504	the novel expression of MT4-MMP in melanocytic tissues	1485:1538	CONCLUSION: We demonstrate the novel expression of MT4-MMP in melanocytic tissues and propose a precursor/product-relationship of the different forms of MT4-MMP in melanoma cells.
28531887	5	4	theme	SK-Mel-28	722:730	arg1	cells					732:736	SK-Mel-28 cells	722:736	SK-Mel-28 cells	722:736	Organelles of SK-Mel-28 cells were separated using continuous Iodixanol gradients.
28531887	9	5	theme	cell	1216:1219	arg1	membrane					1221:1228	the cell membrane	1212:1228	the cell membrane	1212:1228	Further, we demonstrate that the 58 kDa form is the mature protein in the cell membrane, while the 69 kDa form is its precursor found in intracellular compartments.
28531887	6	6	theme	SK-Mel-28	812:820	arg1	protein					822:828	the SK-Mel-28 protein	808:828	the SK-Mel-28 protein	808:828	Glycosylation of the SK-Mel-28 protein was studied via glucosidases and site directed mutagenesis of the MT4-MMP cDNA prior to transfection.
28531887	10	7	theme	furin	1341:1345	arg1	cleavage					1347:1354	furin cleavage	1341:1354	furin cleavage in the Golgi apparatus	1341:1377	The 69 kDa forms are processed by furin cleavage in the Golgi apparatus.
28531887	12	8	theme	melanoma	1622:1629	arg1	cells					1631:1635	melanoma cells	1622:1635	melanoma cells	1622:1635	CONCLUSION: We demonstrate the novel expression of MT4-MMP in melanocytic tissues and propose a precursor/product-relationship of the different forms of MT4-MMP in melanoma cells.
28531887	9	9	theme	58	1175:1176	arg1	kDa					1178:1180	kDa	1178:1180	kDa	1178:1180	Further, we demonstrate that the 58 kDa form is the mature protein in the cell membrane, while the 69 kDa form is its precursor found in intracellular compartments.
28531887	0	10	theme	Different	94:102	arg1	Forms					104:108	its Different Forms	90:108	its Different Forms	90:108	Expression and Characterization of Membrane-Type 4 Matrix Metalloproteinase (MT4-MMP) and its Different Forms in Melanoma.
28531887	0	11	from	Expression	0:9	arg1	Melanoma					113:120	Melanoma	113:120	Melanoma	113:120	Expression and Characterization of Membrane-Type 4 Matrix Metalloproteinase (MT4-MMP) and its Different Forms in Melanoma.
28531887	6	12	theme	site	863:866	arg1	mutagenesis					877:887	glucosidases and site directed mutagenesis	846:887	mutagenesis	877:887	Glycosylation of the SK-Mel-28 protein was studied via glucosidases and site directed mutagenesis of the MT4-MMP cDNA prior to transfection.
28531887	1	13	theme	signaling	274:282	arg1	molecules					284:292	signaling molecules	274:292	signaling molecules	274:292	BACKGROUND/AIMS: Membrane-type matrix metalloproteinases (MT-MMPs) are expressed on the cell surface and hydrolyze extracellular matrix components and signaling molecules by which they influence cancer cell migration and metastasis.
28531887	6	14	theme	MT4-MMP	896:902	arg1	cDNA					904:907	the MT4-MMP cDNA	892:907	the MT4-MMP cDNA	892:907	Glycosylation of the SK-Mel-28 protein was studied via glucosidases and site directed mutagenesis of the MT4-MMP cDNA prior to transfection.
28531887	4	15	theme	quantitative	660:671	arg1	PCR					673:675	quantitative PCR	660:675	quantitative PCR	660:675	METHODS: We analyzed several human cancer cell lines as well as tissue homogenates using Western blotting and quantitative PCR for the expression of MT4-MMP.
28531887	8	16	theme	kDa	1104:1106	arg1	masses					1091:1096	molecular masses	1081:1096	molecular masses of 45 kDa, 58 kDa and 69 kDa	1081:1125	Three forms of MT4-MMP with molecular masses of 45 kDa, 58 kDa and 69 kDa were detected.
28531887	11	17	theme	N-glycosylation	1425:1439	arg1	MT4-MMP					1449:1455	MT4-MMP	1449:1455	MT4-MMP	1449:1455	Moreover, we identified Asn318 as the single N-glycosylation site of MT4-MMP.
28531887	11	17	theme	N-glycosylation	1425:1439	arg1	site					1441:1444	the single N-glycosylation site	1414:1444	the single N-glycosylation site of MT4-MMP	1414:1455	Moreover, we identified Asn318 as the single N-glycosylation site of MT4-MMP.
28531887	11	17	theme	N-glycosylation	1425:1439	arg1	Asn318					1404:1409	Asn318	1404:1409	Asn318	1404:1409	Moreover, we identified Asn318 as the single N-glycosylation site of MT4-MMP.
28531887	0	18	theme	Forms	104:108	arg1	Characterization					15:30	Characterization	15:30	Characterization	15:30	Expression and Characterization of Membrane-Type 4 Matrix Metalloproteinase (MT4-MMP) and its Different Forms in Melanoma.
28531887	0	18	theme	Forms	104:108	arg1	Expression					0:9	Expression	0:9	Expression	0:9	Expression and Characterization of Membrane-Type 4 Matrix Metalloproteinase (MT4-MMP) and its Different Forms in Melanoma.
28531887	9	19	theme	69	1241:1242	arg1	kDa					1244:1246	kDa	1244:1246	kDa	1244:1246	Further, we demonstrate that the 58 kDa form is the mature protein in the cell membrane, while the 69 kDa form is its precursor found in intracellular compartments.
28531887	11	20	theme	single	1418:1423	arg1	MT4-MMP					1449:1455	MT4-MMP	1449:1455	MT4-MMP	1449:1455	Moreover, we identified Asn318 as the single N-glycosylation site of MT4-MMP.
28531887	11	20	theme	single	1418:1423	arg1	site					1441:1444	the single N-glycosylation site	1414:1444	the single N-glycosylation site of MT4-MMP	1414:1455	Moreover, we identified Asn318 as the single N-glycosylation site of MT4-MMP.
28531887	11	20	theme	single	1418:1423	arg1	Asn318					1404:1409	Asn318	1404:1409	Asn318	1404:1409	Moreover, we identified Asn318 as the single N-glycosylation site of MT4-MMP.
28531887	9	21	theme	kDa	1178:1180	arg1	form					1182:1185	the 58 kDa form	1171:1185	the 58 kDa form	1171:1185	Further, we demonstrate that the 58 kDa form is the mature protein in the cell membrane, while the 69 kDa form is its precursor found in intracellular compartments.
28531887	9	21	theme	kDa	1178:1180	arg1	protein					1201:1207	the mature protein	1190:1207	the mature protein in the cell membrane	1190:1228	Further, we demonstrate that the 58 kDa form is the mature protein in the cell membrane, while the 69 kDa form is its precursor found in intracellular compartments.
28531887	12	22	theme	different	1592:1600	arg1	forms					1602:1606	the different forms	1588:1606	the different forms of MT4-MMP	1588:1617	CONCLUSION: We demonstrate the novel expression of MT4-MMP in melanocytic tissues and propose a precursor/product-relationship of the different forms of MT4-MMP in melanoma cells.
28531887	12	23	theme	forms	1602:1606	arg1	precursor/product-relationship					1554:1583	a precursor/product-relationship	1552:1583	a precursor/product-relationship of the different forms of MT4-MMP in melanoma cells	1552:1635	CONCLUSION: We demonstrate the novel expression of MT4-MMP in melanocytic tissues and propose a precursor/product-relationship of the different forms of MT4-MMP in melanoma cells.
28531887	9	24	theme	intracellular	1279:1291	arg1	compartments					1293:1304	intracellular compartments	1279:1304	intracellular compartments	1279:1304	Further, we demonstrate that the 58 kDa form is the mature protein in the cell membrane, while the 69 kDa form is its precursor found in intracellular compartments.
28531887	12	25	from	expression	1495:1504	arg1	tissues					1532:1538	melanocytic tissues	1520:1538	melanocytic tissues	1520:1538	CONCLUSION: We demonstrate the novel expression of MT4-MMP in melanocytic tissues and propose a precursor/product-relationship of the different forms of MT4-MMP in melanoma cells.
28531887	1	26	dep	cell	325:328	arg1	migration					330:338	migration	330:338	migration	330:338	BACKGROUND/AIMS: Membrane-type matrix metalloproteinases (MT-MMPs) are expressed on the cell surface and hydrolyze extracellular matrix components and signaling molecules by which they influence cancer cell migration and metastasis.
28531887	9	27	from	protein	1201:1207	arg1	membrane					1221:1228	the cell membrane	1212:1228	the cell membrane	1212:1228	Further, we demonstrate that the 58 kDa form is the mature protein in the cell membrane, while the 69 kDa form is its precursor found in intracellular compartments.
28531887	12	28	from	precursor/product-relationship	1554:1583	arg1	cells					1631:1635	melanoma cells	1622:1635	melanoma cells	1622:1635	CONCLUSION: We demonstrate the novel expression of MT4-MMP in melanocytic tissues and propose a precursor/product-relationship of the different forms of MT4-MMP in melanoma cells.
28531887	8	29	theme	molecular	1081:1089	arg1	masses					1091:1096	molecular masses	1081:1096	molecular masses of 45 kDa, 58 kDa and 69 kDa	1081:1125	Three forms of MT4-MMP with molecular masses of 45 kDa, 58 kDa and 69 kDa were detected.
28531887	10	30	from	cleavage	1347:1354	arg1	apparatus					1369:1377	the Golgi apparatus	1359:1377	the Golgi apparatus	1359:1377	The 69 kDa forms are processed by furin cleavage in the Golgi apparatus.
28531887	10	31	theme	Golgi	1363:1367	arg1	apparatus					1369:1377	the Golgi apparatus	1359:1377	the Golgi apparatus	1359:1377	The 69 kDa forms are processed by furin cleavage in the Golgi apparatus.
28531887	4	32	theme	Western	639:645	arg1	blotting					647:654	Western blotting	639:654	Western blotting	639:654	METHODS: We analyzed several human cancer cell lines as well as tissue homogenates using Western blotting and quantitative PCR for the expression of MT4-MMP.
28531887	2	33	theme	anchor	431:436	arg1	one					439:441	one	439:441	one	439:441	Two of the six known MT-MMPs are anchored to the plasma membrane via a GPI anchor, one of which is MT4-MMP.
28531887	2	33	theme	anchor	431:436	arg1	anchor					431:436	a GPI anchor	425:436	a GPI anchor	425:436	Two of the six known MT-MMPs are anchored to the plasma membrane via a GPI anchor, one of which is MT4-MMP.
28531887	8	34	theme	kDa	1123:1125	arg1	masses					1091:1096	molecular masses	1081:1096	molecular masses of 45 kDa, 58 kDa and 69 kDa	1081:1125	Three forms of MT4-MMP with molecular masses of 45 kDa, 58 kDa and 69 kDa were detected.
28531887	11	35	gly	N-glycosylation	1425:1439	arg1	MT4-MMP					1449:1455	MT4-MMP	1449:1455	MT4-MMP	1449:1455	Moreover, we identified Asn318 as the single N-glycosylation site of MT4-MMP.
28531887	11	35	gly	N-glycosylation	1425:1439	arg2	site					1441:1444	the single N-glycosylation site	1414:1444	the single N-glycosylation site of MT4-MMP	1414:1455	Moreover, we identified Asn318 as the single N-glycosylation site of MT4-MMP.
28531887	11	35	gly	N-glycosylation	1425:1439	arg2	Asn318					1404:1409	Asn318	1404:1409	Asn318	1404:1409	Moreover, we identified Asn318 as the single N-glycosylation site of MT4-MMP.
28531887	11	35	gly	N-glycosylation	1425:1439	arg2	MT4-MMP					1449:1455	MT4-MMP	1449:1455	MT4-MMP	1449:1455	Moreover, we identified Asn318 as the single N-glycosylation site of MT4-MMP.
28531887	10	36	theme	kDa	1314:1316	arg1	forms					1318:1322	The 69 kDa forms	1307:1322	The 69 kDa forms	1307:1322	The 69 kDa forms are processed by furin cleavage in the Golgi apparatus.
28531887	6	37	theme	cDNA	904:907	arg1	mutagenesis					877:887	glucosidases and site directed mutagenesis	846:887	mutagenesis	877:887	Glycosylation of the SK-Mel-28 protein was studied via glucosidases and site directed mutagenesis of the MT4-MMP cDNA prior to transfection.
28531887	2	38	theme	GPI	427:429	arg1	anchor					431:436	a GPI anchor	425:436	a GPI anchor	425:436	Two of the six known MT-MMPs are anchored to the plasma membrane via a GPI anchor, one of which is MT4-MMP.
28531887	6	39	theme	directed	868:875	arg1	mutagenesis					877:887	glucosidases and site directed mutagenesis	846:887	mutagenesis	877:887	Glycosylation of the SK-Mel-28 protein was studied via glucosidases and site directed mutagenesis of the MT4-MMP cDNA prior to transfection.
28531887	3	40	theme	MT4-MMP	491:497	arg1	expression					499:508	MT4-MMP expression	491:508	MT4-MMP expression	491:508	Only little is known about MT4-MMP expression, synthesis, regulation and degradation.
28531887	5	41	theme	continuous	759:768	arg1	gradients					780:788	continuous Iodixanol gradients	759:788	continuous Iodixanol gradients	759:788	Organelles of SK-Mel-28 cells were separated using continuous Iodixanol gradients.
28531887	12	42	theme	melanocytic	1520:1530	arg1	tissues					1532:1538	melanocytic tissues	1520:1538	melanocytic tissues	1520:1538	CONCLUSION: We demonstrate the novel expression of MT4-MMP in melanocytic tissues and propose a precursor/product-relationship of the different forms of MT4-MMP in melanoma cells.
28531887	7	43	theme	tissue	1037:1042	arg1	samples					1044:1050	skin and melanoma tissue samples	1019:1050	human melanoma cell lines as well as skin and melanoma tissue samples	982:1050	RESULTS: We found the MT4-MMP highly expressed in human melanoma cell lines as well as skin and melanoma tissue samples.
28531887	4	44	theme	tissue	614:619	arg1	homogenates					621:631	tissue homogenates	614:631	several human cancer cell lines as well as tissue homogenates using Western blotting and quantitative PCR for the expression of MT4-MMP	571:705	METHODS: We analyzed several human cancer cell lines as well as tissue homogenates using Western blotting and quantitative PCR for the expression of MT4-MMP.
28531887	11	45	theme	MT4-MMP	1449:1455	arg1	MT4-MMP					1449:1455	MT4-MMP	1449:1455	MT4-MMP	1449:1455	Moreover, we identified Asn318 as the single N-glycosylation site of MT4-MMP.
28531887	11	45	theme	MT4-MMP	1449:1455	arg1	site					1441:1444	the single N-glycosylation site	1414:1444	the single N-glycosylation site of MT4-MMP	1414:1455	Moreover, we identified Asn318 as the single N-glycosylation site of MT4-MMP.
28531887	11	45	theme	MT4-MMP	1449:1455	arg1	Asn318					1404:1409	Asn318	1404:1409	Asn318	1404:1409	Moreover, we identified Asn318 as the single N-glycosylation site of MT4-MMP.
28531887	1	46	theme	cell	211:214	arg1	surface					216:222	the cell surface	207:222	the cell surface	207:222	BACKGROUND/AIMS: Membrane-type matrix metalloproteinases (MT-MMPs) are expressed on the cell surface and hydrolyze extracellular matrix components and signaling molecules by which they influence cancer cell migration and metastasis.
28531887	0	47	theme	Membrane-Type	35:47	arg1	MT4-MMP					77:83	MT4-MMP	77:83	MT4-MMP	77:83	Expression and Characterization of Membrane-Type 4 Matrix Metalloproteinase (MT4-MMP) and its Different Forms in Melanoma.
28531887	0	47	theme	Membrane-Type	35:47	arg1	Metalloproteinase					58:74	Membrane-Type 4 Matrix Metalloproteinase	35:74	Membrane-Type 4 Matrix Metalloproteinase (MT4-MMP)	35:84	Expression and Characterization of Membrane-Type 4 Matrix Metalloproteinase (MT4-MMP) and its Different Forms in Melanoma.
28531887	1	48	theme	cancer	318:323	arg1	cell					325:328	cancer cell migration and metastasis	318:353	cell	325:328	BACKGROUND/AIMS: Membrane-type matrix metalloproteinases (MT-MMPs) are expressed on the cell surface and hydrolyze extracellular matrix components and signaling molecules by which they influence cancer cell migration and metastasis.
28531887	5	49	theme	Iodixanol	770:778	arg1	gradients					780:788	continuous Iodixanol gradients	759:788	continuous Iodixanol gradients	759:788	Organelles of SK-Mel-28 cells were separated using continuous Iodixanol gradients.
28531887	2	50	theme	plasma	405:410	arg1	membrane					412:419	the plasma membrane	401:419	the plasma membrane	401:419	Two of the six known MT-MMPs are anchored to the plasma membrane via a GPI anchor, one of which is MT4-MMP.
28531887	0	51	theme	Metalloproteinase	58:74	arg1	Characterization					15:30	Characterization	15:30	Characterization	15:30	Expression and Characterization of Membrane-Type 4 Matrix Metalloproteinase (MT4-MMP) and its Different Forms in Melanoma.
28531887	0	51	theme	Metalloproteinase	58:74	arg1	Expression					0:9	Expression	0:9	Expression	0:9	Expression and Characterization of Membrane-Type 4 Matrix Metalloproteinase (MT4-MMP) and its Different Forms in Melanoma.
28531887	12	52	theme	novel	1489:1493	arg1	expression					1495:1504	the novel expression	1485:1504	the novel expression of MT4-MMP in melanocytic tissues	1485:1538	CONCLUSION: We demonstrate the novel expression of MT4-MMP in melanocytic tissues and propose a precursor/product-relationship of the different forms of MT4-MMP in melanoma cells.
28531887	6	53	theme	glucosidases	846:857	arg1	mutagenesis					877:887	glucosidases and site directed mutagenesis	846:887	mutagenesis	877:887	Glycosylation of the SK-Mel-28 protein was studied via glucosidases and site directed mutagenesis of the MT4-MMP cDNA prior to transfection.
28531887	0	54	theme	Matrix	51:56	arg1	MT4-MMP					77:83	MT4-MMP	77:83	MT4-MMP	77:83	Expression and Characterization of Membrane-Type 4 Matrix Metalloproteinase (MT4-MMP) and its Different Forms in Melanoma.
28531887	0	54	theme	Matrix	51:56	arg1	Metalloproteinase					58:74	Membrane-Type 4 Matrix Metalloproteinase	35:74	Membrane-Type 4 Matrix Metalloproteinase (MT4-MMP)	35:84	Expression and Characterization of Membrane-Type 4 Matrix Metalloproteinase (MT4-MMP) and its Different Forms in Melanoma.
28531887	6	55	gly	Glycosylation	791:803	arg1	protein					822:828	the SK-Mel-28 protein	808:828	the SK-Mel-28 protein	808:828	Glycosylation of the SK-Mel-28 protein was studied via glucosidases and site directed mutagenesis of the MT4-MMP cDNA prior to transfection.
28531887	7	56	theme	melanoma	1028:1035	arg1	samples					1044:1050	skin and melanoma tissue samples	1019:1050	human melanoma cell lines as well as skin and melanoma tissue samples	982:1050	RESULTS: We found the MT4-MMP highly expressed in human melanoma cell lines as well as skin and melanoma tissue samples.
28531887	9	57	theme	mature	1194:1199	arg1	form					1182:1185	the 58 kDa form	1171:1185	the 58 kDa form	1171:1185	Further, we demonstrate that the 58 kDa form is the mature protein in the cell membrane, while the 69 kDa form is its precursor found in intracellular compartments.
28531887	9	57	theme	mature	1194:1199	arg1	protein					1201:1207	the mature protein	1190:1207	the mature protein in the cell membrane	1190:1228	Further, we demonstrate that the 58 kDa form is the mature protein in the cell membrane, while the 69 kDa form is its precursor found in intracellular compartments.
28531887	7	58	theme	cell	997:1000	arg1	lines					1002:1006	human melanoma cell lines	982:1006	human melanoma cell lines as well as skin and melanoma tissue samples	982:1050	RESULTS: We found the MT4-MMP highly expressed in human melanoma cell lines as well as skin and melanoma tissue samples.
28531887	1	59	theme	Membrane-type	140:152	arg1	MT-MMPs					181:187	MT-MMPs	181:187	MT-MMPs	181:187	BACKGROUND/AIMS: Membrane-type matrix metalloproteinases (MT-MMPs) are expressed on the cell surface and hydrolyze extracellular matrix components and signaling molecules by which they influence cancer cell migration and metastasis.
28531887	1	59	theme	Membrane-type	140:152	arg1	metalloproteinases					161:178	Membrane-type matrix metalloproteinases	140:178	Membrane-type matrix metalloproteinases (MT-MMPs)	140:188	BACKGROUND/AIMS: Membrane-type matrix metalloproteinases (MT-MMPs) are expressed on the cell surface and hydrolyze extracellular matrix components and signaling molecules by which they influence cancer cell migration and metastasis.
28531887	4	60	theme	MT4-MMP	699:705	arg1	expression					685:694	the expression	681:694	the expression of MT4-MMP	681:705	METHODS: We analyzed several human cancer cell lines as well as tissue homogenates using Western blotting and quantitative PCR for the expression of MT4-MMP.
28531887	4	61	theme	cancer	585:590	arg1	lines					597:601	several human cancer cell lines	571:601	several human cancer cell lines as well as tissue homogenates using Western blotting and quantitative PCR for the expression of MT4-MMP	571:705	METHODS: We analyzed several human cancer cell lines as well as tissue homogenates using Western blotting and quantitative PCR for the expression of MT4-MMP.
28531887	7	62	theme	skin	1019:1022	arg1	samples					1044:1050	skin and melanoma tissue samples	1019:1050	human melanoma cell lines as well as skin and melanoma tissue samples	982:1050	RESULTS: We found the MT4-MMP highly expressed in human melanoma cell lines as well as skin and melanoma tissue samples.
28531887	12	63	theme	MT4-MMP	1611:1617	arg1	forms					1602:1606	the different forms	1588:1606	the different forms of MT4-MMP	1588:1617	CONCLUSION: We demonstrate the novel expression of MT4-MMP in melanocytic tissues and propose a precursor/product-relationship of the different forms of MT4-MMP in melanoma cells.
28531887	9	64	located	found	1270:1274	arg2	form					1248:1251	the 69 kDa form	1237:1251	the 69 kDa form	1237:1251	Further, we demonstrate that the 58 kDa form is the mature protein in the cell membrane, while the 69 kDa form is its precursor found in intracellular compartments.
28531887	9	64	located	found	1270:1274	arg2	precursor					1260:1268	its precursor	1256:1268	its precursor found in intracellular compartments	1256:1304	Further, we demonstrate that the 58 kDa form is the mature protein in the cell membrane, while the 69 kDa form is its precursor found in intracellular compartments.
28531887	9	64	located	found	1270:1274	arg1	compartments					1293:1304	intracellular compartments	1279:1304	intracellular compartments	1279:1304	Further, we demonstrate that the 58 kDa form is the mature protein in the cell membrane, while the 69 kDa form is its precursor found in intracellular compartments.
28531887	7	65	theme	human	982:986	arg1	lines					1002:1006	human melanoma cell lines	982:1006	human melanoma cell lines as well as skin and melanoma tissue samples	982:1050	RESULTS: We found the MT4-MMP highly expressed in human melanoma cell lines as well as skin and melanoma tissue samples.
28531887	1	66	theme	matrix	154:159	arg1	MT-MMPs					181:187	MT-MMPs	181:187	MT-MMPs	181:187	BACKGROUND/AIMS: Membrane-type matrix metalloproteinases (MT-MMPs) are expressed on the cell surface and hydrolyze extracellular matrix components and signaling molecules by which they influence cancer cell migration and metastasis.
28531887	1	66	theme	matrix	154:159	arg1	metalloproteinases					161:178	Membrane-type matrix metalloproteinases	140:178	Membrane-type matrix metalloproteinases (MT-MMPs)	140:188	BACKGROUND/AIMS: Membrane-type matrix metalloproteinases (MT-MMPs) are expressed on the cell surface and hydrolyze extracellular matrix components and signaling molecules by which they influence cancer cell migration and metastasis.
28531887	4	67	theme	human	579:583	arg1	lines					597:601	several human cancer cell lines	571:601	several human cancer cell lines as well as tissue homogenates using Western blotting and quantitative PCR for the expression of MT4-MMP	571:705	METHODS: We analyzed several human cancer cell lines as well as tissue homogenates using Western blotting and quantitative PCR for the expression of MT4-MMP.
28531887	5	68	theme	cells	732:736	arg1	Organelles					708:717	Organelles	708:717	Organelles of SK-Mel-28 cells	708:736	Organelles of SK-Mel-28 cells were separated using continuous Iodixanol gradients.
28531887	6	69	theme	protein	822:828	arg1	Glycosylation					791:803	Glycosylation	791:803	Glycosylation of the SK-Mel-28 protein	791:828	Glycosylation of the SK-Mel-28 protein was studied via glucosidases and site directed mutagenesis of the MT4-MMP cDNA prior to transfection.
28531887	7	70	theme	melanoma	988:995	arg1	lines					1002:1006	human melanoma cell lines	982:1006	human melanoma cell lines as well as skin and melanoma tissue samples	982:1050	RESULTS: We found the MT4-MMP highly expressed in human melanoma cell lines as well as skin and melanoma tissue samples.
28531887	2	71	theme	MT-MMPs	377:383	arg1	Two					356:358	Two	356:358	Two	356:358	Two of the six known MT-MMPs are anchored to the plasma membrane via a GPI anchor, one of which is MT4-MMP.
28531887	2	71	theme	MT-MMPs	377:383	arg1	MT-MMPs					377:383	the six known MT-MMPs	363:383	the six known MT-MMPs	363:383	Two of the six known MT-MMPs are anchored to the plasma membrane via a GPI anchor, one of which is MT4-MMP.
28531887	8	72	with	forms	1059:1063	arg1	masses					1091:1096	molecular masses	1081:1096	molecular masses of 45 kDa, 58 kDa and 69 kDa	1081:1125	Three forms of MT4-MMP with molecular masses of 45 kDa, 58 kDa and 69 kDa were detected.
28531887	1	73	theme	extracellular	238:250	arg1	components					259:268	extracellular matrix components	238:268	extracellular matrix components	238:268	BACKGROUND/AIMS: Membrane-type matrix metalloproteinases (MT-MMPs) are expressed on the cell surface and hydrolyze extracellular matrix components and signaling molecules by which they influence cancer cell migration and metastasis.
28531887	4	74	theme	several	571:577	arg1	lines					597:601	several human cancer cell lines	571:601	several human cancer cell lines as well as tissue homogenates using Western blotting and quantitative PCR for the expression of MT4-MMP	571:705	METHODS: We analyzed several human cancer cell lines as well as tissue homogenates using Western blotting and quantitative PCR for the expression of MT4-MMP.
28531887	4	75	theme	cell	592:595	arg1	lines					597:601	several human cancer cell lines	571:601	several human cancer cell lines as well as tissue homogenates using Western blotting and quantitative PCR for the expression of MT4-MMP	571:705	METHODS: We analyzed several human cancer cell lines as well as tissue homogenates using Western blotting and quantitative PCR for the expression of MT4-MMP.
28531887	2	76	theme	known	371:375	arg1	MT-MMPs					377:383	the six known MT-MMPs	363:383	the six known MT-MMPs	363:383	Two of the six known MT-MMPs are anchored to the plasma membrane via a GPI anchor, one of which is MT4-MMP.
28531887	8	77	theme	MT4-MMP	1068:1074	arg1	forms					1059:1063	Three forms	1053:1063	Three forms of MT4-MMP with molecular masses of 45 kDa, 58 kDa and 69 kDa	1053:1125	Three forms of MT4-MMP with molecular masses of 45 kDa, 58 kDa and 69 kDa were detected.
28531887	1	78	theme	matrix	252:257	arg1	components					259:268	extracellular matrix components	238:268	extracellular matrix components	238:268	BACKGROUND/AIMS: Membrane-type matrix metalloproteinases (MT-MMPs) are expressed on the cell surface and hydrolyze extracellular matrix components and signaling molecules by which they influence cancer cell migration and metastasis.
11258925	3	0	from	masses	653:658	arg1	presence					603:610	the presence	599:610	the presence of three glycoforms at average molecular masses of 71.4, 72.7, and 73.9 kDa	599:686	This paper reports on the glycosylation site analysis of recombinant COX-2 using matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS) and nanoelectrospray (nanoESI) quadrupole-TOF (Q-TOF) MS. The nanoESI MS analysis of COX-2 revealed the presence of three glycoforms at average molecular masses of 71.4, 72.7, and 73.9 kDa.
11258925	3	1	theme	nanoESI	521:527	arg1	Q-TOF					546:550	Q-TOF	546:550	Q-TOF	546:550	This paper reports on the glycosylation site analysis of recombinant COX-2 using matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS) and nanoelectrospray (nanoESI) quadrupole-TOF (Q-TOF) MS. The nanoESI MS analysis of COX-2 revealed the presence of three glycoforms at average molecular masses of 71.4, 72.7, and 73.9 kDa.
11258925	3	1	theme	nanoESI	521:527	arg1	quadrupole-TOF					530:543	nanoelectrospray (nanoESI) quadrupole-TOF	503:543	nanoelectrospray (nanoESI) quadrupole-TOF (Q-TOF)	503:551	This paper reports on the glycosylation site analysis of recombinant COX-2 using matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS) and nanoelectrospray (nanoESI) quadrupole-TOF (Q-TOF) MS. The nanoESI MS analysis of COX-2 revealed the presence of three glycoforms at average molecular masses of 71.4, 72.7, and 73.9 kDa.
11258925	4	2	theme	high-mannose	808:819	arg1	sugars					821:826	high-mannose sugars	808:826	high-mannose sugars	808:826	Each glycoform contained a number of peaks differing by 162 Da indicating heterogeneity and suggesting the presence of high-mannose sugars.
11258925	9	3	theme	glycopeptides	1561:1573	arg1	presence					1545:1552	the presence	1541:1552	the presence of the glycopeptides	1541:1573	It was not possible to conclusively determine whether the Asn 396 site was glycosylated via an MS/MS experiment, so the tryptic digest was deglycosylated to confirm the presence of the glycopeptides.
11258925	6	4	theme	glycopeptides	1076:1088	arg1	number					1056:1061	a number	1054:1061	a number of potential glycopeptides	1054:1088	The MALDI MS analysis of a tryptic digest of the protein showed a number of potential glycopeptides.
11258925	6	5	gly	glycopeptides	1076:1088	arg2	glycopeptides					1076:1088	potential glycopeptides	1066:1088	potential glycopeptides	1066:1088	The MALDI MS analysis of a tryptic digest of the protein showed a number of potential glycopeptides.
11258925	10	6	gly	non-glycosylated	1587:1602	arg1	peptide					1612:1618	a non-glycosylated tryptic peptide	1585:1618	a non-glycosylated tryptic peptide	1585:1618	Finally, a non-glycosylated tryptic peptide was observed containing the Asn 592.
11258925	8	7	dep	peptides	1293:1300	arg1	414					1314:1316	Asn 396-Arg 414 + GlcNAc and Thr 576-Arg 587	1302:1345	414	1314:1316	Nanoelectrospray MS/MS experiments confirmed glycosylation at the Asn 53 and Asn 130 sites and confirmed the presence of the peptides Asn 396-Arg 414 + GlcNAc and Thr 576-Arg 587 + GlcNAc containing Asn 580.
11258925	8	7	dep	peptides	1293:1300	arg1	GlcNAc					1320:1325	Asn 396-Arg 414 + GlcNAc and Thr 576-Arg 587	1302:1345	GlcNAc	1320:1325	Nanoelectrospray MS/MS experiments confirmed glycosylation at the Asn 53 and Asn 130 sites and confirmed the presence of the peptides Asn 396-Arg 414 + GlcNAc and Thr 576-Arg 587 + GlcNAc containing Asn 580.
11258925	8	7	dep	peptides	1293:1300	arg1	587					1343:1345	Asn 396-Arg 414 + GlcNAc and Thr 576-Arg 587	1302:1345	587	1343:1345	Nanoelectrospray MS/MS experiments confirmed glycosylation at the Asn 53 and Asn 130 sites and confirmed the presence of the peptides Asn 396-Arg 414 + GlcNAc and Thr 576-Arg 587 + GlcNAc containing Asn 580.
11258925	8	7	dep	peptides	1293:1300	arg1	Asn					1367:1369	GlcNAc containing Asn 580	1349:1373	GlcNAc containing Asn 580	1349:1373	Nanoelectrospray MS/MS experiments confirmed glycosylation at the Asn 53 and Asn 130 sites and confirmed the presence of the peptides Asn 396-Arg 414 + GlcNAc and Thr 576-Arg 587 + GlcNAc containing Asn 580.
11258925	2	8	theme	nuclear	237:243	arg1	envelope					245:252	the nuclear envelope	233:252	the nuclear envelope	233:252	It is a glycoprotein located in the endoplasmic reticulum and in the nuclear envelope, and it has been found to have two isoforms termed COX-1 and COX-2.
11258925	8	9	theme	Nanoelectrospray	1168:1183	arg1	experiments					1191:1201	Nanoelectrospray MS/MS experiments	1168:1201	Nanoelectrospray MS/MS experiments	1168:1201	Nanoelectrospray MS/MS experiments confirmed glycosylation at the Asn 53 and Asn 130 sites and confirmed the presence of the peptides Asn 396-Arg 414 + GlcNAc and Thr 576-Arg 587 + GlcNAc containing Asn 580.
11258925	8	10	theme	Asn	1245:1247	arg1	sites					1253:1257	the Asn 53 and Asn 130 sites	1230:1257	sites	1253:1257	Nanoelectrospray MS/MS experiments confirmed glycosylation at the Asn 53 and Asn 130 sites and confirmed the presence of the peptides Asn 396-Arg 414 + GlcNAc and Thr 576-Arg 587 + GlcNAc containing Asn 580.
11258925	3	11	theme	nanoESI	561:567	arg1	analysis					572:579	The nanoESI MS analysis	557:579	The nanoESI MS analysis of COX-2	557:588	This paper reports on the glycosylation site analysis of recombinant COX-2 using matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS) and nanoelectrospray (nanoESI) quadrupole-TOF (Q-TOF) MS. The nanoESI MS analysis of COX-2 revealed the presence of three glycoforms at average molecular masses of 71.4, 72.7, and 73.9 kDa.
11258925	9	12	theme	Asn	1434:1436	arg1	site					1442:1445	the Asn 396 site	1430:1445	the Asn 396 site	1430:1445	It was not possible to conclusively determine whether the Asn 396 site was glycosylated via an MS/MS experiment, so the tryptic digest was deglycosylated to confirm the presence of the glycopeptides.
11258925	5	13	theme	N-acetylglucosamine	927:945	arg1	residue					956:962	a single N-acetylglucosamine (GlcNAc) residue	918:962	a single N-acetylglucosamine (GlcNAc) residue	918:962	The masses of the glycoforms indicate that oligosaccharides occupy two to four sites and a single N-acetylglucosamine (GlcNAc) residue occupied up to two sites.
11258925	5	14	dep	sites	908:912	arg1	to					900:901	to	900:901	to	900:901	The masses of the glycoforms indicate that oligosaccharides occupy two to four sites and a single N-acetylglucosamine (GlcNAc) residue occupied up to two sites.
11258925	0	15	theme	mass	70:73	arg1	spectrometry					75:86	mass spectrometry	70:86	mass spectrometry	70:86	Characterization of the glycosylation sites in cyclooxygenase-2 using mass spectrometry.
11258925	3	16	theme	COX-2	584:588	arg1	analysis					572:579	The nanoESI MS analysis	557:579	The nanoESI MS analysis of COX-2	557:588	This paper reports on the glycosylation site analysis of recombinant COX-2 using matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS) and nanoelectrospray (nanoESI) quadrupole-TOF (Q-TOF) MS. The nanoESI MS analysis of COX-2 revealed the presence of three glycoforms at average molecular masses of 71.4, 72.7, and 73.9 kDa.
11258925	8	17	from	sites	1253:1257	arg1	glycosylation					1213:1225	glycosylation	1213:1225	glycosylation at the Asn 53 and Asn 130 sites	1213:1257	Nanoelectrospray MS/MS experiments confirmed glycosylation at the Asn 53 and Asn 130 sites and confirmed the presence of the peptides Asn 396-Arg 414 + GlcNAc and Thr 576-Arg 587 + GlcNAc containing Asn 580.
11258925	0	18	from	Characterization	0:15	arg1	cyclooxygenase-2					47:62	cyclooxygenase-2	47:62	cyclooxygenase-2 using mass spectrometry	47:86	Characterization of the glycosylation sites in cyclooxygenase-2 using mass spectrometry.
11258925	2	19	gly	glycoprotein	176:187	arg1	It					168:169	It	168:169	It	168:169	It is a glycoprotein located in the endoplasmic reticulum and in the nuclear envelope, and it has been found to have two isoforms termed COX-1 and COX-2.
11258925	2	19	gly	glycoprotein	176:187	arg1	glycoprotein					176:187	a glycoprotein	174:187	a glycoprotein located in the endoplasmic reticulum and in the nuclear envelope	174:252	It is a glycoprotein located in the endoplasmic reticulum and in the nuclear envelope, and it has been found to have two isoforms termed COX-1 and COX-2.
11258925	5	20	theme	single	920:925	arg1	residue					956:962	a single N-acetylglucosamine (GlcNAc) residue	918:962	a single N-acetylglucosamine (GlcNAc) residue	918:962	The masses of the glycoforms indicate that oligosaccharides occupy two to four sites and a single N-acetylglucosamine (GlcNAc) residue occupied up to two sites.
11258925	0	21	from	cyclooxygenase-2	47:62	arg1	Characterization					0:15	Characterization	0:15	Characterization of the glycosylation sites in cyclooxygenase-2 using mass spectrometry.	0:87	Characterization of the glycosylation sites in cyclooxygenase-2 using mass spectrometry.
11258925	3	22	theme	TOF	471:473	arg1	spectrometry					481:492	matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry	403:492	matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS)	403:497	This paper reports on the glycosylation site analysis of recombinant COX-2 using matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS) and nanoelectrospray (nanoESI) quadrupole-TOF (Q-TOF) MS. The nanoESI MS analysis of COX-2 revealed the presence of three glycoforms at average molecular masses of 71.4, 72.7, and 73.9 kDa.
11258925	3	22	theme	TOF	471:473	arg1	MS					495:496	MS	495:496	MS	495:496	This paper reports on the glycosylation site analysis of recombinant COX-2 using matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS) and nanoelectrospray (nanoESI) quadrupole-TOF (Q-TOF) MS. The nanoESI MS analysis of COX-2 revealed the presence of three glycoforms at average molecular masses of 71.4, 72.7, and 73.9 kDa.
11258925	1	23	dep	biosynthesis	123:134	arg1	the					119:121	the	119:121	the	119:121	Cyclooxygenase is involved in the biosynthesis and function of prostaglandins.
11258925	2	24	from	envelope	245:252	arg1	located					189:195	located	189:195	located	189:195	It is a glycoprotein located in the endoplasmic reticulum and in the nuclear envelope, and it has been found to have two isoforms termed COX-1 and COX-2.
11258925	0	25	from	sites	38:42	arg1	cyclooxygenase-2					47:62	cyclooxygenase-2	47:62	cyclooxygenase-2 using mass spectrometry	47:86	Characterization of the glycosylation sites in cyclooxygenase-2 using mass spectrometry.
11258925	3	26	theme	laser	419:423	arg1	spectrometry					481:492	matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry	403:492	matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS)	403:497	This paper reports on the glycosylation site analysis of recombinant COX-2 using matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS) and nanoelectrospray (nanoESI) quadrupole-TOF (Q-TOF) MS. The nanoESI MS analysis of COX-2 revealed the presence of three glycoforms at average molecular masses of 71.4, 72.7, and 73.9 kDa.
11258925	3	26	theme	laser	419:423	arg1	MS					495:496	MS	495:496	MS	495:496	This paper reports on the glycosylation site analysis of recombinant COX-2 using matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS) and nanoelectrospray (nanoESI) quadrupole-TOF (Q-TOF) MS. The nanoESI MS analysis of COX-2 revealed the presence of three glycoforms at average molecular masses of 71.4, 72.7, and 73.9 kDa.
11258925	7	27	theme	162	1116:1118	arg1	Da					1120:1121	162 Da	1116:1121	162 Da which further suggested high-mannose sugars	1116:1165	The peptides differed by 162 Da which further suggested high-mannose sugars.
11258925	3	28	gly	glycosylation	348:360	arg1	COX-2					391:395	recombinant COX-2	379:395	recombinant COX-2	379:395	This paper reports on the glycosylation site analysis of recombinant COX-2 using matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS) and nanoelectrospray (nanoESI) quadrupole-TOF (Q-TOF) MS. The nanoESI MS analysis of COX-2 revealed the presence of three glycoforms at average molecular masses of 71.4, 72.7, and 73.9 kDa.
11258925	3	28	gly	glycosylation	348:360	arg2	site					362:365	the glycosylation site analysis	344:374	the glycosylation site analysis of recombinant COX-2 using matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS) and nanoelectrospray (nanoESI) quadrupole-TOF (Q-TOF)	344:551	This paper reports on the glycosylation site analysis of recombinant COX-2 using matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS) and nanoelectrospray (nanoESI) quadrupole-TOF (Q-TOF) MS. The nanoESI MS analysis of COX-2 revealed the presence of three glycoforms at average molecular masses of 71.4, 72.7, and 73.9 kDa.
11258925	3	28	gly	glycosylation	348:360	arg2	analysis					367:374	the glycosylation site analysis	344:374	the glycosylation site analysis of recombinant COX-2 using matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS) and nanoelectrospray (nanoESI) quadrupole-TOF (Q-TOF)	344:551	This paper reports on the glycosylation site analysis of recombinant COX-2 using matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS) and nanoelectrospray (nanoESI) quadrupole-TOF (Q-TOF) MS. The nanoESI MS analysis of COX-2 revealed the presence of three glycoforms at average molecular masses of 71.4, 72.7, and 73.9 kDa.
11258925	2	29	theme	located	189:195	arg1	It					168:169	It	168:169	It	168:169	It is a glycoprotein located in the endoplasmic reticulum and in the nuclear envelope, and it has been found to have two isoforms termed COX-1 and COX-2.
11258925	2	29	theme	located	189:195	arg1	glycoprotein					176:187	a glycoprotein	174:187	a glycoprotein located in the endoplasmic reticulum and in the nuclear envelope	174:252	It is a glycoprotein located in the endoplasmic reticulum and in the nuclear envelope, and it has been found to have two isoforms termed COX-1 and COX-2.
11258925	3	30	theme	glycosylation	348:360	arg1	analysis					367:374	the glycosylation site analysis	344:374	the glycosylation site analysis of recombinant COX-2 using matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS) and nanoelectrospray (nanoESI) quadrupole-TOF (Q-TOF)	344:551	This paper reports on the glycosylation site analysis of recombinant COX-2 using matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS) and nanoelectrospray (nanoESI) quadrupole-TOF (Q-TOF) MS. The nanoESI MS analysis of COX-2 revealed the presence of three glycoforms at average molecular masses of 71.4, 72.7, and 73.9 kDa.
11258925	10	31	theme	tryptic	1604:1610	arg1	peptide					1612:1618	a non-glycosylated tryptic peptide	1585:1618	a non-glycosylated tryptic peptide	1585:1618	Finally, a non-glycosylated tryptic peptide was observed containing the Asn 592.
11258925	9	32	theme	tryptic	1496:1502	arg1	digest					1504:1509	the tryptic digest	1492:1509	the tryptic digest	1492:1509	It was not possible to conclusively determine whether the Asn 396 site was glycosylated via an MS/MS experiment, so the tryptic digest was deglycosylated to confirm the presence of the glycopeptides.
11258925	6	33	theme	MALDI	994:998	arg1	analysis					1003:1010	The MALDI MS analysis	990:1010	The MALDI MS analysis of a tryptic digest of the protein	990:1045	The MALDI MS analysis of a tryptic digest of the protein showed a number of potential glycopeptides.
11258925	3	34	theme	glycoforms	621:630	arg1	presence					603:610	the presence	599:610	the presence of three glycoforms at average molecular masses of 71.4, 72.7, and 73.9 kDa	599:686	This paper reports on the glycosylation site analysis of recombinant COX-2 using matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS) and nanoelectrospray (nanoESI) quadrupole-TOF (Q-TOF) MS. The nanoESI MS analysis of COX-2 revealed the presence of three glycoforms at average molecular masses of 71.4, 72.7, and 73.9 kDa.
11258925	8	35	theme	Thr	1331:1333	arg1	587					1343:1345	Asn 396-Arg 414 + GlcNAc and Thr 576-Arg 587	1302:1345	587	1343:1345	Nanoelectrospray MS/MS experiments confirmed glycosylation at the Asn 53 and Asn 130 sites and confirmed the presence of the peptides Asn 396-Arg 414 + GlcNAc and Thr 576-Arg 587 + GlcNAc containing Asn 580.
11258925	0	36	theme	sites	38:42	arg1	Characterization					0:15	Characterization	0:15	Characterization of the glycosylation sites in cyclooxygenase-2 using mass spectrometry.	0:87	Characterization of the glycosylation sites in cyclooxygenase-2 using mass spectrometry.
11258925	3	37	theme	recombinant	379:389	arg1	COX-2					391:395	recombinant COX-2	379:395	recombinant COX-2	379:395	This paper reports on the glycosylation site analysis of recombinant COX-2 using matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS) and nanoelectrospray (nanoESI) quadrupole-TOF (Q-TOF) MS. The nanoESI MS analysis of COX-2 revealed the presence of three glycoforms at average molecular masses of 71.4, 72.7, and 73.9 kDa.
11258925	0	38	gly	glycosylation	24:36	arg2	sites					38:42	the glycosylation sites	20:42	the glycosylation sites in cyclooxygenase-2 using mass spectrometry	20:86	Characterization of the glycosylation sites in cyclooxygenase-2 using mass spectrometry.
11258925	8	39	theme	GlcNAc	1349:1354	arg1	Asn					1367:1369	GlcNAc containing Asn 580	1349:1373	GlcNAc containing Asn 580	1349:1373	Nanoelectrospray MS/MS experiments confirmed glycosylation at the Asn 53 and Asn 130 sites and confirmed the presence of the peptides Asn 396-Arg 414 + GlcNAc and Thr 576-Arg 587 + GlcNAc containing Asn 580.
11258925	3	40	theme	average	635:641	arg1	masses					653:658	average molecular masses	635:658	average molecular masses of 71.4, 72.7, and 73.9 kDa	635:686	This paper reports on the glycosylation site analysis of recombinant COX-2 using matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS) and nanoelectrospray (nanoESI) quadrupole-TOF (Q-TOF) MS. The nanoESI MS analysis of COX-2 revealed the presence of three glycoforms at average molecular masses of 71.4, 72.7, and 73.9 kDa.
11258925	9	41	gly	deglycosylated	1515:1528	arg1	digest					1504:1509	the tryptic digest	1492:1509	the tryptic digest	1492:1509	It was not possible to conclusively determine whether the Asn 396 site was glycosylated via an MS/MS experiment, so the tryptic digest was deglycosylated to confirm the presence of the glycopeptides.
11258925	10	42	theme	Asn	1648:1650	arg1	592					1652:1654	the Asn 592	1644:1654	the Asn 592	1644:1654	Finally, a non-glycosylated tryptic peptide was observed containing the Asn 592.
11258925	2	43	from	located	189:195	arg1	envelope					245:252	the nuclear envelope	233:252	the nuclear envelope	233:252	It is a glycoprotein located in the endoplasmic reticulum and in the nuclear envelope, and it has been found to have two isoforms termed COX-1 and COX-2.
11258925	2	43	from	located	189:195	arg1	reticulum					216:224	the endoplasmic reticulum	200:224	the endoplasmic reticulum	200:224	It is a glycoprotein located in the endoplasmic reticulum and in the nuclear envelope, and it has been found to have two isoforms termed COX-1 and COX-2.
11258925	4	44	theme	sugars	821:826	arg1	presence					796:803	the presence	792:803	the presence of high-mannose sugars	792:826	Each glycoform contained a number of peaks differing by 162 Da indicating heterogeneity and suggesting the presence of high-mannose sugars.
11258925	6	45	theme	digest	1025:1030	arg1	analysis					1003:1010	The MALDI MS analysis	990:1010	The MALDI MS analysis of a tryptic digest of the protein	990:1045	The MALDI MS analysis of a tryptic digest of the protein showed a number of potential glycopeptides.
11258925	3	46	theme	kDa	684:686	arg1	masses					653:658	average molecular masses	635:658	average molecular masses of 71.4, 72.7, and 73.9 kDa	635:686	This paper reports on the glycosylation site analysis of recombinant COX-2 using matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS) and nanoelectrospray (nanoESI) quadrupole-TOF (Q-TOF) MS. The nanoESI MS analysis of COX-2 revealed the presence of three glycoforms at average molecular masses of 71.4, 72.7, and 73.9 kDa.
11258925	4	47	dep	Da	749:750	arg1	indicating					752:761	indicating	752:761	indicating heterogeneity	752:775	Each glycoform contained a number of peaks differing by 162 Da indicating heterogeneity and suggesting the presence of high-mannose sugars.
11258925	4	47	dep	Da	749:750	arg1	suggesting					781:790	suggesting	781:790	suggesting the presence of high-mannose sugars	781:826	Each glycoform contained a number of peaks differing by 162 Da indicating heterogeneity and suggesting the presence of high-mannose sugars.
11258925	2	48	from	reticulum	216:224	arg1	located					189:195	located	189:195	located	189:195	It is a glycoprotein located in the endoplasmic reticulum and in the nuclear envelope, and it has been found to have two isoforms termed COX-1 and COX-2.
11258925	8	49	theme	MS/MS	1185:1189	arg1	experiments					1191:1201	Nanoelectrospray MS/MS experiments	1168:1201	Nanoelectrospray MS/MS experiments	1168:1201	Nanoelectrospray MS/MS experiments confirmed glycosylation at the Asn 53 and Asn 130 sites and confirmed the presence of the peptides Asn 396-Arg 414 + GlcNAc and Thr 576-Arg 587 + GlcNAc containing Asn 580.
11258925	4	50	contain	contained	704:712	arg1	glycoform					694:702	Each glycoform	689:702	Each glycoform	689:702	Each glycoform contained a number of peaks differing by 162 Da indicating heterogeneity and suggesting the presence of high-mannose sugars.
11258925	4	50	contain	contained	704:712	arg2	number					716:721	a number	714:721	a number of peaks differing by 162 Da indicating heterogeneity and suggesting the presence of high-mannose sugars	714:826	Each glycoform contained a number of peaks differing by 162 Da indicating heterogeneity and suggesting the presence of high-mannose sugars.
11258925	6	51	theme	potential	1066:1074	arg1	glycopeptides					1076:1088	potential glycopeptides	1066:1088	potential glycopeptides	1066:1088	The MALDI MS analysis of a tryptic digest of the protein showed a number of potential glycopeptides.
11258925	1	52	theme	prostaglandins	152:165	arg1	function					140:147	function	140:147	function	140:147	Cyclooxygenase is involved in the biosynthesis and function of prostaglandins.
11258925	1	52	theme	prostaglandins	152:165	arg1	biosynthesis					123:134	biosynthesis	123:134	biosynthesis	123:134	Cyclooxygenase is involved in the biosynthesis and function of prostaglandins.
11258925	3	53	theme	MS	569:570	arg1	analysis					572:579	The nanoESI MS analysis	557:579	The nanoESI MS analysis of COX-2	557:588	This paper reports on the glycosylation site analysis of recombinant COX-2 using matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS) and nanoelectrospray (nanoESI) quadrupole-TOF (Q-TOF) MS. The nanoESI MS analysis of COX-2 revealed the presence of three glycoforms at average molecular masses of 71.4, 72.7, and 73.9 kDa.
11258925	8	54	gly	glycosylation	1213:1225	arg2	sites					1253:1257	the Asn 53 and Asn 130 sites	1230:1257	sites	1253:1257	Nanoelectrospray MS/MS experiments confirmed glycosylation at the Asn 53 and Asn 130 sites and confirmed the presence of the peptides Asn 396-Arg 414 + GlcNAc and Thr 576-Arg 587 + GlcNAc containing Asn 580.
11258925	8	54	gly	glycosylation	1213:1225	arg2	Asn					1234:1236	the Asn 53 and Asn 130 sites	1230:1257	Asn	1234:1236	Nanoelectrospray MS/MS experiments confirmed glycosylation at the Asn 53 and Asn 130 sites and confirmed the presence of the peptides Asn 396-Arg 414 + GlcNAc and Thr 576-Arg 587 + GlcNAc containing Asn 580.
11258925	8	54	gly	glycosylation	1213:1225	arg1	sites					1253:1257	the Asn 53 and Asn 130 sites	1230:1257	sites	1253:1257	Nanoelectrospray MS/MS experiments confirmed glycosylation at the Asn 53 and Asn 130 sites and confirmed the presence of the peptides Asn 396-Arg 414 + GlcNAc and Thr 576-Arg 587 + GlcNAc containing Asn 580.
11258925	8	54	gly	glycosylation	1213:1225	arg1	Asn					1234:1236	the Asn 53 and Asn 130 sites	1230:1257	Asn	1234:1236	Nanoelectrospray MS/MS experiments confirmed glycosylation at the Asn 53 and Asn 130 sites and confirmed the presence of the peptides Asn 396-Arg 414 + GlcNAc and Thr 576-Arg 587 + GlcNAc containing Asn 580.
11258925	3	55	attach	presence	603:610	arg2	glycoforms					621:630	three glycoforms	615:630	three glycoforms	615:630	This paper reports on the glycosylation site analysis of recombinant COX-2 using matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS) and nanoelectrospray (nanoESI) quadrupole-TOF (Q-TOF) MS. The nanoESI MS analysis of COX-2 revealed the presence of three glycoforms at average molecular masses of 71.4, 72.7, and 73.9 kDa.
11258925	3	55	attach	presence	603:610	arg1	masses					653:658	average molecular masses	635:658	average molecular masses of 71.4, 72.7, and 73.9 kDa	635:686	This paper reports on the glycosylation site analysis of recombinant COX-2 using matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS) and nanoelectrospray (nanoESI) quadrupole-TOF (Q-TOF) MS. The nanoESI MS analysis of COX-2 revealed the presence of three glycoforms at average molecular masses of 71.4, 72.7, and 73.9 kDa.
11258925	4	56	theme	peaks	726:730	arg1	number					716:721	a number	714:721	a number of peaks differing by 162 Da indicating heterogeneity and suggesting the presence of high-mannose sugars	714:826	Each glycoform contained a number of peaks differing by 162 Da indicating heterogeneity and suggesting the presence of high-mannose sugars.
11258925	8	57	from	Asn	1234:1236	arg1	glycosylation					1213:1225	glycosylation	1213:1225	glycosylation at the Asn 53 and Asn 130 sites	1213:1257	Nanoelectrospray MS/MS experiments confirmed glycosylation at the Asn 53 and Asn 130 sites and confirmed the presence of the peptides Asn 396-Arg 414 + GlcNAc and Thr 576-Arg 587 + GlcNAc containing Asn 580.
11258925	9	58	theme	396	1438:1440	arg1	site					1442:1445	the Asn 396 site	1430:1445	the Asn 396 site	1430:1445	It was not possible to conclusively determine whether the Asn 396 site was glycosylated via an MS/MS experiment, so the tryptic digest was deglycosylated to confirm the presence of the glycopeptides.
11258925	7	59	theme	high-mannose	1147:1158	arg1	sugars					1160:1165	high-mannose sugars	1147:1165	high-mannose sugars	1147:1165	The peptides differed by 162 Da which further suggested high-mannose sugars.
11258925	5	60	theme	glycoforms	847:856	arg1	masses					833:838	The masses	829:838	The masses of the glycoforms	829:856	The masses of the glycoforms indicate that oligosaccharides occupy two to four sites and a single N-acetylglucosamine (GlcNAc) residue occupied up to two sites.
11258925	9	61	theme	MS/MS	1471:1475	arg1	experiment					1477:1486	an MS/MS experiment	1468:1486	an MS/MS experiment	1468:1486	It was not possible to conclusively determine whether the Asn 396 site was glycosylated via an MS/MS experiment, so the tryptic digest was deglycosylated to confirm the presence of the glycopeptides.
11258925	6	62	theme	tryptic	1017:1023	arg1	digest					1025:1030	a tryptic digest	1015:1030	a tryptic digest of the protein	1015:1045	The MALDI MS analysis of a tryptic digest of the protein showed a number of potential glycopeptides.
11258925	9	63	gly	glycosylated	1451:1462	arg1	site					1442:1445	the Asn 396 site	1430:1445	the Asn 396 site	1430:1445	It was not possible to conclusively determine whether the Asn 396 site was glycosylated via an MS/MS experiment, so the tryptic digest was deglycosylated to confirm the presence of the glycopeptides.
11258925	8	64	theme	peptides	1293:1300	arg1	presence					1277:1284	the presence	1273:1284	the presence of the peptides Asn 396-Arg 414 + GlcNAc and Thr 576-Arg 587 + GlcNAc containing Asn 580	1273:1373	Nanoelectrospray MS/MS experiments confirmed glycosylation at the Asn 53 and Asn 130 sites and confirmed the presence of the peptides Asn 396-Arg 414 + GlcNAc and Thr 576-Arg 587 + GlcNAc containing Asn 580.
11258925	3	65	theme	MALDI	448:452	arg1	spectrometry					481:492	matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry	403:492	matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS)	403:497	This paper reports on the glycosylation site analysis of recombinant COX-2 using matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS) and nanoelectrospray (nanoESI) quadrupole-TOF (Q-TOF) MS. The nanoESI MS analysis of COX-2 revealed the presence of three glycoforms at average molecular masses of 71.4, 72.7, and 73.9 kDa.
11258925	3	65	theme	MALDI	448:452	arg1	MS					495:496	MS	495:496	MS	495:496	This paper reports on the glycosylation site analysis of recombinant COX-2 using matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS) and nanoelectrospray (nanoESI) quadrupole-TOF (Q-TOF) MS. The nanoESI MS analysis of COX-2 revealed the presence of three glycoforms at average molecular masses of 71.4, 72.7, and 73.9 kDa.
11258925	8	66	theme	396-Arg	1306:1312	arg1	414					1314:1316	Asn 396-Arg 414 + GlcNAc and Thr 576-Arg 587	1302:1345	414	1314:1316	Nanoelectrospray MS/MS experiments confirmed glycosylation at the Asn 53 and Asn 130 sites and confirmed the presence of the peptides Asn 396-Arg 414 + GlcNAc and Thr 576-Arg 587 + GlcNAc containing Asn 580.
11258925	3	67	theme	desorption/ionization	425:445	arg1	spectrometry					481:492	matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry	403:492	matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS)	403:497	This paper reports on the glycosylation site analysis of recombinant COX-2 using matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS) and nanoelectrospray (nanoESI) quadrupole-TOF (Q-TOF) MS. The nanoESI MS analysis of COX-2 revealed the presence of three glycoforms at average molecular masses of 71.4, 72.7, and 73.9 kDa.
11258925	3	67	theme	desorption/ionization	425:445	arg1	MS					495:496	MS	495:496	MS	495:496	This paper reports on the glycosylation site analysis of recombinant COX-2 using matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS) and nanoelectrospray (nanoESI) quadrupole-TOF (Q-TOF) MS. The nanoESI MS analysis of COX-2 revealed the presence of three glycoforms at average molecular masses of 71.4, 72.7, and 73.9 kDa.
11258925	0	68	theme	glycosylation	24:36	arg1	sites					38:42	the glycosylation sites	20:42	the glycosylation sites in cyclooxygenase-2 using mass spectrometry	20:86	Characterization of the glycosylation sites in cyclooxygenase-2 using mass spectrometry.
11258925	6	69	theme	MS	1000:1001	arg1	analysis					1003:1010	The MALDI MS analysis	990:1010	The MALDI MS analysis of a tryptic digest of the protein	990:1045	The MALDI MS analysis of a tryptic digest of the protein showed a number of potential glycopeptides.
11258925	3	70	theme	site	362:365	arg1	analysis					367:374	the glycosylation site analysis	344:374	the glycosylation site analysis of recombinant COX-2 using matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS) and nanoelectrospray (nanoESI) quadrupole-TOF (Q-TOF)	344:551	This paper reports on the glycosylation site analysis of recombinant COX-2 using matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS) and nanoelectrospray (nanoESI) quadrupole-TOF (Q-TOF) MS. The nanoESI MS analysis of COX-2 revealed the presence of three glycoforms at average molecular masses of 71.4, 72.7, and 73.9 kDa.
11258925	8	71	theme	Asn	1302:1304	arg1	414					1314:1316	Asn 396-Arg 414 + GlcNAc and Thr 576-Arg 587	1302:1345	414	1314:1316	Nanoelectrospray MS/MS experiments confirmed glycosylation at the Asn 53 and Asn 130 sites and confirmed the presence of the peptides Asn 396-Arg 414 + GlcNAc and Thr 576-Arg 587 + GlcNAc containing Asn 580.
11258925	10	72	theme	non-glycosylated	1587:1602	arg1	peptide					1612:1618	a non-glycosylated tryptic peptide	1585:1618	a non-glycosylated tryptic peptide	1585:1618	Finally, a non-glycosylated tryptic peptide was observed containing the Asn 592.
11258925	2	73	contain	have	280:283	arg2	isoforms					289:296	two isoforms	285:296	two isoforms termed COX-1 and COX-2	285:319	It is a glycoprotein located in the endoplasmic reticulum and in the nuclear envelope, and it has been found to have two isoforms termed COX-1 and COX-2.
11258925	2	73	contain	have	280:283	arg1	it					259:260	it	259:260	it	259:260	It is a glycoprotein located in the endoplasmic reticulum and in the nuclear envelope, and it has been found to have two isoforms termed COX-1 and COX-2.
11258925	3	74	theme	matrix-assisted	403:417	arg1	spectrometry					481:492	matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry	403:492	matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS)	403:497	This paper reports on the glycosylation site analysis of recombinant COX-2 using matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS) and nanoelectrospray (nanoESI) quadrupole-TOF (Q-TOF) MS. The nanoESI MS analysis of COX-2 revealed the presence of three glycoforms at average molecular masses of 71.4, 72.7, and 73.9 kDa.
11258925	3	74	theme	matrix-assisted	403:417	arg1	MS					495:496	MS	495:496	MS	495:496	This paper reports on the glycosylation site analysis of recombinant COX-2 using matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS) and nanoelectrospray (nanoESI) quadrupole-TOF (Q-TOF) MS. The nanoESI MS analysis of COX-2 revealed the presence of three glycoforms at average molecular masses of 71.4, 72.7, and 73.9 kDa.
11258925	3	75	theme	time-of-flight	455:468	arg1	spectrometry					481:492	matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry	403:492	matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS)	403:497	This paper reports on the glycosylation site analysis of recombinant COX-2 using matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS) and nanoelectrospray (nanoESI) quadrupole-TOF (Q-TOF) MS. The nanoESI MS analysis of COX-2 revealed the presence of three glycoforms at average molecular masses of 71.4, 72.7, and 73.9 kDa.
11258925	3	75	theme	time-of-flight	455:468	arg1	MS					495:496	MS	495:496	MS	495:496	This paper reports on the glycosylation site analysis of recombinant COX-2 using matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS) and nanoelectrospray (nanoESI) quadrupole-TOF (Q-TOF) MS. The nanoESI MS analysis of COX-2 revealed the presence of three glycoforms at average molecular masses of 71.4, 72.7, and 73.9 kDa.
11258925	3	76	theme	COX-2	391:395	arg1	analysis					367:374	the glycosylation site analysis	344:374	the glycosylation site analysis of recombinant COX-2 using matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS) and nanoelectrospray (nanoESI) quadrupole-TOF (Q-TOF)	344:551	This paper reports on the glycosylation site analysis of recombinant COX-2 using matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS) and nanoelectrospray (nanoESI) quadrupole-TOF (Q-TOF) MS. The nanoESI MS analysis of COX-2 revealed the presence of three glycoforms at average molecular masses of 71.4, 72.7, and 73.9 kDa.
11258925	3	77	theme	molecular	643:651	arg1	masses					653:658	average molecular masses	635:658	average molecular masses of 71.4, 72.7, and 73.9 kDa	635:686	This paper reports on the glycosylation site analysis of recombinant COX-2 using matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS) and nanoelectrospray (nanoESI) quadrupole-TOF (Q-TOF) MS. The nanoESI MS analysis of COX-2 revealed the presence of three glycoforms at average molecular masses of 71.4, 72.7, and 73.9 kDa.
11258925	8	78	theme	576-Arg	1335:1341	arg1	587					1343:1345	Asn 396-Arg 414 + GlcNAc and Thr 576-Arg 587	1302:1345	587	1343:1345	Nanoelectrospray MS/MS experiments confirmed glycosylation at the Asn 53 and Asn 130 sites and confirmed the presence of the peptides Asn 396-Arg 414 + GlcNAc and Thr 576-Arg 587 + GlcNAc containing Asn 580.
11258925	9	79	gly	glycopeptides	1561:1573	arg2	glycopeptides					1561:1573	the glycopeptides	1557:1573	the glycopeptides	1557:1573	It was not possible to conclusively determine whether the Asn 396 site was glycosylated via an MS/MS experiment, so the tryptic digest was deglycosylated to confirm the presence of the glycopeptides.
11258925	4	80	theme	162	745:747	arg1	Da					749:750	162 Da	745:750	162 Da indicating heterogeneity and suggesting the presence of high-mannose sugars	745:826	Each glycoform contained a number of peaks differing by 162 Da indicating heterogeneity and suggesting the presence of high-mannose sugars.
11258925	5	81	theme	GlcNAc	948:953	arg1	residue					956:962	a single N-acetylglucosamine (GlcNAc) residue	918:962	a single N-acetylglucosamine (GlcNAc) residue	918:962	The masses of the glycoforms indicate that oligosaccharides occupy two to four sites and a single N-acetylglucosamine (GlcNAc) residue occupied up to two sites.
11258925	2	82	theme	endoplasmic	204:214	arg1	reticulum					216:224	the endoplasmic reticulum	200:224	the endoplasmic reticulum	200:224	It is a glycoprotein located in the endoplasmic reticulum and in the nuclear envelope, and it has been found to have two isoforms termed COX-1 and COX-2.
11258925	3	83	theme	mass	476:479	arg1	spectrometry					481:492	matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry	403:492	matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS)	403:497	This paper reports on the glycosylation site analysis of recombinant COX-2 using matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS) and nanoelectrospray (nanoESI) quadrupole-TOF (Q-TOF) MS. The nanoESI MS analysis of COX-2 revealed the presence of three glycoforms at average molecular masses of 71.4, 72.7, and 73.9 kDa.
11258925	3	83	theme	mass	476:479	arg1	MS					495:496	MS	495:496	MS	495:496	This paper reports on the glycosylation site analysis of recombinant COX-2 using matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS) and nanoelectrospray (nanoESI) quadrupole-TOF (Q-TOF) MS. The nanoESI MS analysis of COX-2 revealed the presence of three glycoforms at average molecular masses of 71.4, 72.7, and 73.9 kDa.
11258925	6	84	theme	protein	1039:1045	arg1	digest					1025:1030	a tryptic digest	1015:1030	a tryptic digest of the protein	1015:1045	The MALDI MS analysis of a tryptic digest of the protein showed a number of potential glycopeptides.
11258925	8	85	theme	containing	1356:1365	arg1	Asn					1367:1369	GlcNAc containing Asn 580	1349:1373	GlcNAc containing Asn 580	1349:1373	Nanoelectrospray MS/MS experiments confirmed glycosylation at the Asn 53 and Asn 130 sites and confirmed the presence of the peptides Asn 396-Arg 414 + GlcNAc and Thr 576-Arg 587 + GlcNAc containing Asn 580.
11258925	3	86	theme	nanoelectrospray	503:518	arg1	Q-TOF					546:550	Q-TOF	546:550	Q-TOF	546:550	This paper reports on the glycosylation site analysis of recombinant COX-2 using matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS) and nanoelectrospray (nanoESI) quadrupole-TOF (Q-TOF) MS. The nanoESI MS analysis of COX-2 revealed the presence of three glycoforms at average molecular masses of 71.4, 72.7, and 73.9 kDa.
11258925	3	86	theme	nanoelectrospray	503:518	arg1	quadrupole-TOF					530:543	nanoelectrospray (nanoESI) quadrupole-TOF	503:543	nanoelectrospray (nanoESI) quadrupole-TOF (Q-TOF)	503:551	This paper reports on the glycosylation site analysis of recombinant COX-2 using matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS) and nanoelectrospray (nanoESI) quadrupole-TOF (Q-TOF) MS. The nanoESI MS analysis of COX-2 revealed the presence of three glycoforms at average molecular masses of 71.4, 72.7, and 73.9 kDa.
26764097	10	0	theme	DPY19L3-mediated	1418:1433	arg1	C-mannosylation					1435:1449	DPY19L3-mediated C-mannosylation	1418:1449	DPY19L3-mediated C-mannosylation of Rspo1 at W(156)	1418:1468	In conclusion, we identified DPY19L3 as the C-mannosyltransferase of Rspo1 at W(156) and found that DPY19L3-mediated C-mannosylation of Rspo1 at W(156) is required for its secretion.
26764097	1	1	theme	Wnt	140:142	arg1	signaling					144:152	Wnt signaling	140:152	Wnt signaling	140:152	R-spondin1 (Rspo1) is a secreted protein that enhances Wnt signaling, which has crucial functions in embryonic development and several cancers.
26764097	9	2	theme	Rspo1	1311:1315	arg1	secretion					1298:1306	the secretion	1294:1306	the secretion of Rspo1	1294:1315	Moreover, knockdown of DPY19L3 inhibited the secretion of Rspo1.
26764097	3	3	from	effects	498:504	arg1	protein					514:520	this protein	509:520	this protein	509:520	Although human Rspo1 contains 2 predicted C-mannosylation sites, C-mannosylation of Rspo1 has not been reported, nor have its functional effects on this protein.
26764097	2	4	theme	enzymatic	341:349	arg1	activity					351:358	enzymatic activity	341:358	enzymatic activity	341:358	C-mannosylation is a rare type of glycosylation and might regulate secretion, protein-protein interactions, and enzymatic activity.
26764097	10	5	theme	Rspo1	1454:1458	arg1	C-mannosylation					1435:1449	DPY19L3-mediated C-mannosylation	1418:1449	DPY19L3-mediated C-mannosylation of Rspo1 at W(156)	1418:1468	In conclusion, we identified DPY19L3 as the C-mannosyltransferase of Rspo1 at W(156) and found that DPY19L3-mediated C-mannosylation of Rspo1 at W(156) is required for its secretion.
26764097	4	6	theme	mass	556:559	arg1	spectrometry					561:572	mass spectrometry	556:572	mass spectrometry	556:572	In this study, we demonstrate by mass spectrometry that Rspo1 is C-mannosylated at W(153) and W(156).
26764097	5	7	theme	synthesis	684:692	arg1	activity					694:701	dolichol-phosphate-mannose synthesis activity	657:701	dolichol-phosphate-mannose synthesis activity	657:701	Using Lec15.2 cells, which lack dolichol-phosphate-mannose synthesis activity, and mutant Rspo1-expressing cells that replace W(153) and W(156) by alanine residues, we observed that C-mannosylation of Rspo1 is required for its secretion.
26764097	3	8	gly	C-mannosylation	403:417	arg2	sites					419:423	2 predicted C-mannosylation sites	391:423	2 predicted C-mannosylation sites	391:423	Although human Rspo1 contains 2 predicted C-mannosylation sites, C-mannosylation of Rspo1 has not been reported, nor have its functional effects on this protein.
26764097	4	9	gly	C-mannosylated	588:601	arg2	W					606:606	W(153)	606:611	W(153)	606:611	In this study, we demonstrate by mass spectrometry that Rspo1 is C-mannosylated at W(153) and W(156).
26764097	4	9	gly	C-mannosylated	588:601	arg1	Rspo1					579:583	Rspo1	579:583	Rspo1	579:583	In this study, we demonstrate by mass spectrometry that Rspo1 is C-mannosylated at W(153) and W(156).
26764097	4	9	gly	C-mannosylated	588:601	arg2	W					617:617	W	617:617	W(156)	617:622	In this study, we demonstrate by mass spectrometry that Rspo1 is C-mannosylated at W(153) and W(156).
26764097	4	9	gly	C-mannosylated	588:601	arg2	156					619:621	156	619:621	156	619:621	In this study, we demonstrate by mass spectrometry that Rspo1 is C-mannosylated at W(153) and W(156).
26764097	6	10	theme	signaling	905:913	arg1	enhancement					876:886	the enhancement	872:886	the enhancement of canonical Wnt signaling by Rspo1	872:922	Further, the enhancement of canonical Wnt signaling by Rspo1 is regulated by C-mannosylation.
26764097	3	11	contain	have	478:481	arg1	C-mannosylation					426:440	C-mannosylation	426:440	C-mannosylation of Rspo1	426:449	Although human Rspo1 contains 2 predicted C-mannosylation sites, C-mannosylation of Rspo1 has not been reported, nor have its functional effects on this protein.
26764097	3	11	contain	have	478:481	arg2	effects					498:504	its functional effects	483:504	its functional effects on this protein	483:520	Although human Rspo1 contains 2 predicted C-mannosylation sites, C-mannosylation of Rspo1 has not been reported, nor have its functional effects on this protein.
26764097	8	12	theme	mass	1234:1237	arg1	spectrometry					1239:1250	mass spectrometry	1234:1250	mass spectrometry	1234:1250	In gain- and loss-of-function experiments, human DPY19L3 selectively modified Rspo1 at W(156) but not W(153) based on mass spectrometry.
26764097	2	13	theme	glycosylation	263:275	arg1	type					255:258	a rare type	248:258	a rare type of glycosylation	248:275	C-mannosylation is a rare type of glycosylation and might regulate secretion, protein-protein interactions, and enzymatic activity.
26764097	2	13	theme	glycosylation	263:275	arg1	C-mannosylation					229:243	C-mannosylation	229:243	C-mannosylation	229:243	C-mannosylation is a rare type of glycosylation and might regulate secretion, protein-protein interactions, and enzymatic activity.
26764097	6	14	theme	Wnt	901:903	arg1	signaling					905:913	canonical Wnt signaling	891:913	canonical Wnt signaling	891:913	Further, the enhancement of canonical Wnt signaling by Rspo1 is regulated by C-mannosylation.
26764097	7	15	theme	Caenorhabditis	1018:1031	arg1	elegans					1033:1039	Caenorhabditis elegans	1018:1039	Caenorhabditis elegans	1018:1039	Recently DPY19 was reported to be a C-mannosyltransferase in Caenorhabditis elegans, but no C-mannosyltransferases have been identified in any other organism.
26764097	7	16	from	C-mannosyltransferase	993:1013	arg1	elegans					1033:1039	Caenorhabditis elegans	1018:1039	Caenorhabditis elegans	1018:1039	Recently DPY19 was reported to be a C-mannosyltransferase in Caenorhabditis elegans, but no C-mannosyltransferases have been identified in any other organism.
26764097	3	17	theme	Rspo1	445:449	arg1	C-mannosylation					426:440	C-mannosylation	426:440	C-mannosylation of Rspo1	426:449	Although human Rspo1 contains 2 predicted C-mannosylation sites, C-mannosylation of Rspo1 has not been reported, nor have its functional effects on this protein.
26764097	8	18	theme	human	1159:1163	arg1	DPY19L3					1165:1171	human DPY19L3	1159:1171	human DPY19L3	1159:1171	In gain- and loss-of-function experiments, human DPY19L3 selectively modified Rspo1 at W(156) but not W(153) based on mass spectrometry.
26764097	0	19	from	C-mannosyltransferase	33:53	arg1	cells					78:82	human cells	72:82	human cells	72:82	Identification of DPY19L3 as the C-mannosyltransferase of R-spondin1 in human cells.
26764097	10	20	theme	Rspo1	1387:1391	arg1	DPY19L3					1347:1353	DPY19L3	1347:1353	DPY19L3	1347:1353	In conclusion, we identified DPY19L3 as the C-mannosyltransferase of Rspo1 at W(156) and found that DPY19L3-mediated C-mannosylation of Rspo1 at W(156) is required for its secretion.
26764097	10	20	theme	Rspo1	1387:1391	arg1	C-mannosyltransferase					1362:1382	the C-mannosyltransferase	1358:1382	the C-mannosyltransferase of Rspo1 at W(156)	1358:1401	In conclusion, we identified DPY19L3 as the C-mannosyltransferase of Rspo1 at W(156) and found that DPY19L3-mediated C-mannosylation of Rspo1 at W(156) is required for its secretion.
26764097	8	21	theme	gain-	1119:1123	arg1	experiments					1146:1156	gain- and loss-of-function experiments	1119:1156	gain- and loss-of-function experiments	1119:1156	In gain- and loss-of-function experiments, human DPY19L3 selectively modified Rspo1 at W(156) but not W(153) based on mass spectrometry.
26764097	4	22	from	W	606:606	arg1	C-mannosylated					588:601	C-mannosylated	588:601	C-mannosylated	588:601	In this study, we demonstrate by mass spectrometry that Rspo1 is C-mannosylated at W(153) and W(156).
26764097	4	23	from	W	617:617	arg1	C-mannosylated					588:601	C-mannosylated	588:601	C-mannosylated	588:601	In this study, we demonstrate by mass spectrometry that Rspo1 is C-mannosylated at W(153) and W(156).
26764097	6	24	theme	canonical	891:899	arg1	signaling					905:913	canonical Wnt signaling	891:913	canonical Wnt signaling	891:913	Further, the enhancement of canonical Wnt signaling by Rspo1 is regulated by C-mannosylation.
26764097	1	25	theme	crucial	165:171	arg1	functions					173:181	crucial functions	165:181	crucial functions	165:181	R-spondin1 (Rspo1) is a secreted protein that enhances Wnt signaling, which has crucial functions in embryonic development and several cancers.
26764097	3	26	theme	human	370:374	arg1	Rspo1					376:380	human Rspo1	370:380	human Rspo1	370:380	Although human Rspo1 contains 2 predicted C-mannosylation sites, C-mannosylation of Rspo1 has not been reported, nor have its functional effects on this protein.
26764097	3	27	contain	contains	382:389	arg2	sites					419:423	2 predicted C-mannosylation sites	391:423	2 predicted C-mannosylation sites	391:423	Although human Rspo1 contains 2 predicted C-mannosylation sites, C-mannosylation of Rspo1 has not been reported, nor have its functional effects on this protein.
26764097	3	27	contain	contains	382:389	arg1	Rspo1					376:380	human Rspo1	370:380	human Rspo1	370:380	Although human Rspo1 contains 2 predicted C-mannosylation sites, C-mannosylation of Rspo1 has not been reported, nor have its functional effects on this protein.
26764097	0	28	theme	DPY19L3	18:24	arg1	Identification					0:13	Identification	0:13	Identification of DPY19L3 as the C-mannosyltransferase of R-spondin1 in human cells.	0:83	Identification of DPY19L3 as the C-mannosyltransferase of R-spondin1 in human cells.
26764097	5	29	theme	Rspo1	826:830	arg1	C-mannosylation					807:821	C-mannosylation	807:821	C-mannosylation of Rspo1	807:830	Using Lec15.2 cells, which lack dolichol-phosphate-mannose synthesis activity, and mutant Rspo1-expressing cells that replace W(153) and W(156) by alanine residues, we observed that C-mannosylation of Rspo1 is required for its secretion.
26764097	1	30	contain	has	161:163	arg2	functions					173:181	crucial functions	165:181	crucial functions	165:181	R-spondin1 (Rspo1) is a secreted protein that enhances Wnt signaling, which has crucial functions in embryonic development and several cancers.
26764097	1	30	contain	has	161:163	arg1	signaling					144:152	Wnt signaling	140:152	Wnt signaling	140:152	R-spondin1 (Rspo1) is a secreted protein that enhances Wnt signaling, which has crucial functions in embryonic development and several cancers.
26764097	1	31	theme	embryonic	186:194	arg1	development					196:206	embryonic development	186:206	embryonic development	186:206	R-spondin1 (Rspo1) is a secreted protein that enhances Wnt signaling, which has crucial functions in embryonic development and several cancers.
26764097	5	32	theme	mutant	708:713	arg1	cells					732:736	mutant Rspo1-expressing cells	708:736	mutant Rspo1-expressing cells that replace W(153) and W(156) by alanine residues	708:787	Using Lec15.2 cells, which lack dolichol-phosphate-mannose synthesis activity, and mutant Rspo1-expressing cells that replace W(153) and W(156) by alanine residues, we observed that C-mannosylation of Rspo1 is required for its secretion.
26764097	5	33	theme	dolichol-phosphate-mannose	657:682	arg1	activity					694:701	dolichol-phosphate-mannose synthesis activity	657:701	dolichol-phosphate-mannose synthesis activity	657:701	Using Lec15.2 cells, which lack dolichol-phosphate-mannose synthesis activity, and mutant Rspo1-expressing cells that replace W(153) and W(156) by alanine residues, we observed that C-mannosylation of Rspo1 is required for its secretion.
26764097	8	34	theme	loss-of-function	1129:1144	arg1	experiments					1146:1156	gain- and loss-of-function experiments	1119:1156	gain- and loss-of-function experiments	1119:1156	In gain- and loss-of-function experiments, human DPY19L3 selectively modified Rspo1 at W(156) but not W(153) based on mass spectrometry.
26764097	5	35	theme	alanine	772:778	arg1	residues					780:787	alanine residues	772:787	alanine residues	772:787	Using Lec15.2 cells, which lack dolichol-phosphate-mannose synthesis activity, and mutant Rspo1-expressing cells that replace W(153) and W(156) by alanine residues, we observed that C-mannosylation of Rspo1 is required for its secretion.
26764097	3	36	theme	predicted	393:401	arg1	sites					419:423	2 predicted C-mannosylation sites	391:423	2 predicted C-mannosylation sites	391:423	Although human Rspo1 contains 2 predicted C-mannosylation sites, C-mannosylation of Rspo1 has not been reported, nor have its functional effects on this protein.
26764097	5	37	gly	C-mannosylation	807:821	arg1	Rspo1					826:830	Rspo1	826:830	Rspo1	826:830	Using Lec15.2 cells, which lack dolichol-phosphate-mannose synthesis activity, and mutant Rspo1-expressing cells that replace W(153) and W(156) by alanine residues, we observed that C-mannosylation of Rspo1 is required for its secretion.
26764097	5	38	theme	Rspo1-expressing	715:730	arg1	cells					732:736	mutant Rspo1-expressing cells	708:736	mutant Rspo1-expressing cells that replace W(153) and W(156) by alanine residues	708:787	Using Lec15.2 cells, which lack dolichol-phosphate-mannose synthesis activity, and mutant Rspo1-expressing cells that replace W(153) and W(156) by alanine residues, we observed that C-mannosylation of Rspo1 is required for its secretion.
26764097	3	39	theme	C-mannosylation	403:417	arg1	sites					419:423	2 predicted C-mannosylation sites	391:423	2 predicted C-mannosylation sites	391:423	Although human Rspo1 contains 2 predicted C-mannosylation sites, C-mannosylation of Rspo1 has not been reported, nor have its functional effects on this protein.
26764097	3	40	theme	functional	487:496	arg1	effects					498:504	its functional effects	483:504	its functional effects on this protein	483:520	Although human Rspo1 contains 2 predicted C-mannosylation sites, C-mannosylation of Rspo1 has not been reported, nor have its functional effects on this protein.
26764097	9	41	theme	DPY19L3	1276:1282	arg1	knockdown					1263:1271	knockdown	1263:1271	knockdown of DPY19L3	1263:1282	Moreover, knockdown of DPY19L3 inhibited the secretion of Rspo1.
26764097	5	42	theme	Lec15.2	631:637	arg1	cells					639:643	Lec15.2 cells	631:643	Lec15.2 cells	631:643	Using Lec15.2 cells, which lack dolichol-phosphate-mannose synthesis activity, and mutant Rspo1-expressing cells that replace W(153) and W(156) by alanine residues, we observed that C-mannosylation of Rspo1 is required for its secretion.
26764097	2	43	theme	rare	250:253	arg1	type					255:258	a rare type	248:258	a rare type of glycosylation	248:275	C-mannosylation is a rare type of glycosylation and might regulate secretion, protein-protein interactions, and enzymatic activity.
26764097	2	43	theme	rare	250:253	arg1	C-mannosylation					229:243	C-mannosylation	229:243	C-mannosylation	229:243	C-mannosylation is a rare type of glycosylation and might regulate secretion, protein-protein interactions, and enzymatic activity.
26764097	1	44	theme	secreted	109:116	arg1	protein					118:124	a secreted protein	107:124	a secreted protein that enhances Wnt signaling, which has crucial functions in embryonic development and several cancers	107:226	R-spondin1 (Rspo1) is a secreted protein that enhances Wnt signaling, which has crucial functions in embryonic development and several cancers.
26764097	1	44	theme	secreted	109:116	arg1	R-spondin1					85:94	R-spondin1	85:94	R-spondin1 (Rspo1)	85:102	R-spondin1 (Rspo1) is a secreted protein that enhances Wnt signaling, which has crucial functions in embryonic development and several cancers.
26764097	10	45	gly	C-mannosylation	1435:1449	arg1	156					1465:1467	156	1465:1467	156	1465:1467	In conclusion, we identified DPY19L3 as the C-mannosyltransferase of Rspo1 at W(156) and found that DPY19L3-mediated C-mannosylation of Rspo1 at W(156) is required for its secretion.
26764097	10	45	gly	C-mannosylation	1435:1449	arg1	W					1463:1463	W	1463:1463	W(156)	1463:1468	In conclusion, we identified DPY19L3 as the C-mannosyltransferase of Rspo1 at W(156) and found that DPY19L3-mediated C-mannosylation of Rspo1 at W(156) is required for its secretion.
26764097	10	45	gly	C-mannosylation	1435:1449	arg1	Rspo1					1454:1458	Rspo1	1454:1458	Rspo1	1454:1458	In conclusion, we identified DPY19L3 as the C-mannosyltransferase of Rspo1 at W(156) and found that DPY19L3-mediated C-mannosylation of Rspo1 at W(156) is required for its secretion.
26764097	2	46	theme	protein-protein	307:321	arg1	interactions					323:334	protein-protein interactions	307:334	protein-protein interactions	307:334	C-mannosylation is a rare type of glycosylation and might regulate secretion, protein-protein interactions, and enzymatic activity.
26764097	1	47	theme	several	212:218	arg1	cancers					220:226	several cancers	212:226	several cancers	212:226	R-spondin1 (Rspo1) is a secreted protein that enhances Wnt signaling, which has crucial functions in embryonic development and several cancers.
26764097	0	48	theme	human	72:76	arg1	cells					78:82	human cells	72:82	human cells	72:82	Identification of DPY19L3 as the C-mannosyltransferase of R-spondin1 in human cells.
26764097	10	49	from	W	1463:1463	arg1	C-mannosylation					1435:1449	DPY19L3-mediated C-mannosylation	1418:1449	DPY19L3-mediated C-mannosylation of Rspo1 at W(156)	1418:1468	In conclusion, we identified DPY19L3 as the C-mannosyltransferase of Rspo1 at W(156) and found that DPY19L3-mediated C-mannosylation of Rspo1 at W(156) is required for its secretion.
26764097	0	50	theme	R-spondin1	58:67	arg1	C-mannosyltransferase					33:53	the C-mannosyltransferase	29:53	the C-mannosyltransferase of R-spondin1 in human cells	29:82	Identification of DPY19L3 as the C-mannosyltransferase of R-spondin1 in human cells.
26764097	3	51	gly	C-mannosylation	426:440	arg1	Rspo1					445:449	Rspo1	445:449	Rspo1	445:449	Although human Rspo1 contains 2 predicted C-mannosylation sites, C-mannosylation of Rspo1 has not been reported, nor have its functional effects on this protein.
26764097	7	52	theme	other	1100:1104	arg1	organism					1106:1113	any other organism	1096:1113	any other organism	1096:1113	Recently DPY19 was reported to be a C-mannosyltransferase in Caenorhabditis elegans, but no C-mannosyltransferases have been identified in any other organism.
26764097	10	53	from	W	1396:1396	arg1	DPY19L3					1347:1353	DPY19L3	1347:1353	DPY19L3	1347:1353	In conclusion, we identified DPY19L3 as the C-mannosyltransferase of Rspo1 at W(156) and found that DPY19L3-mediated C-mannosylation of Rspo1 at W(156) is required for its secretion.
26764097	10	53	from	W	1396:1396	arg1	C-mannosyltransferase					1362:1382	the C-mannosyltransferase	1358:1382	the C-mannosyltransferase of Rspo1 at W(156)	1358:1401	In conclusion, we identified DPY19L3 as the C-mannosyltransferase of Rspo1 at W(156) and found that DPY19L3-mediated C-mannosylation of Rspo1 at W(156) is required for its secretion.
11502878	10	0	theme	specific	1297:1304	arg1	Q					1287:1287	Q(78)	1287:1291	Q(78) (no specific binding)	1287:1313	Binding to N(78)-Q(78) (B(max) = 0.27 +/- 0.03 fmol/mg of protein, n = 3; K(d) = 149.1 +/- 11.1, n = 3) and N(7),N(78)-Q(7),Q(78) (no specific binding) was further impaired.
11502878	10	0	theme	specific	1297:1304	arg1	binding					1306:1312	no specific binding	1294:1312	no specific binding	1294:1312	Binding to N(78)-Q(78) (B(max) = 0.27 +/- 0.03 fmol/mg of protein, n = 3; K(d) = 149.1 +/- 11.1, n = 3) and N(7),N(78)-Q(7),Q(78) (no specific binding) was further impaired.
11502878	7	1	theme	concomitant	740:750	arg1	mutant					733:738	each mutant	728:738	each mutant concomitant with impaired glycosylation	728:778	Membrane localization was reduced for each mutant concomitant with impaired glycosylation.
11502878	8	2	from	function	889:896	arg1	examination					840:850	direct examination	833:850	direct examination of the effect of glycosylation on IP function	833:896	Partial localization to the plasma membrane allowed direct examination of the effect of glycosylation on IP function.
11502878	2	3	theme	h	259:259	arg1	IP					262:263	The human (h) IP	248:263	The human (h) IP	248:263	The human (h) IP contains two consensus sites for N-linked glycosylation (N(7) and N(78)).
11502878	2	4	theme	human	252:256	arg1	IP					262:263	The human (h) IP	248:263	The human (h) IP	248:263	The human (h) IP contains two consensus sites for N-linked glycosylation (N(7) and N(78)).
11502878	8	5	theme	Partial	781:787	arg1	localization					789:800	Partial localization	781:800	Partial localization to the plasma membrane	781:823	Partial localization to the plasma membrane allowed direct examination of the effect of glycosylation on IP function.
11502878	1	6	theme	cell-surface	187:198	arg1	IP					242:243	IP	242:243	IP	242:243	Prostacyclin, a potent vasodilator and inhibitor of platelet aggregation, acts through a cell-surface G protein-coupled receptor [prostacyclin (IP)].
11502878	1	6	theme	cell-surface	187:198	arg1	[prostacyclin					227:239	a cell-surface G protein-coupled receptor [prostacyclin	185:239	a cell-surface G protein-coupled receptor [prostacyclin (IP)	185:244	Prostacyclin, a potent vasodilator and inhibitor of platelet aggregation, acts through a cell-surface G protein-coupled receptor [prostacyclin (IP)].
11502878	11	7	theme	iloprost	1480:1487	arg1	concentrations					1462:1475	high concentrations	1457:1475	high concentrations of iloprost	1457:1487	Agonist-induced adenylyl cyclase activation was reduced in N(7)-Q(7) cells, whereas N(78)-Q(78) cells responded only to high concentrations of iloprost and N(7),N(78)-Q(7),Q(78) were unresponsive.
11502878	1	8	theme	protein-coupled	202:216	arg1	IP					242:243	IP	242:243	IP	242:243	Prostacyclin, a potent vasodilator and inhibitor of platelet aggregation, acts through a cell-surface G protein-coupled receptor [prostacyclin (IP)].
11502878	1	8	theme	protein-coupled	202:216	arg1	[prostacyclin					227:239	a cell-surface G protein-coupled receptor [prostacyclin	185:239	a cell-surface G protein-coupled receptor [prostacyclin (IP)	185:244	Prostacyclin, a potent vasodilator and inhibitor of platelet aggregation, acts through a cell-surface G protein-coupled receptor [prostacyclin (IP)].
11502878	8	9	theme	plasma	809:814	arg1	membrane					816:823	the plasma membrane	805:823	the plasma membrane	805:823	Partial localization to the plasma membrane allowed direct examination of the effect of glycosylation on IP function.
11502878	10	10	theme	=	1194:1194	arg1	N					1174:1174	N(78)-Q(78)	1174:1184	N(78)-Q(78) (B(max) = 0.27 +/- 0.03 fmol/mg	1174:1216	Binding to N(78)-Q(78) (B(max) = 0.27 +/- 0.03 fmol/mg of protein, n = 3; K(d) = 149.1 +/- 11.1, n = 3) and N(7),N(78)-Q(7),Q(78) (no specific binding) was further impaired.
11502878	9	11	theme	=	952:952	arg1	nM					967:968	K(d) = 21.7 +/- 1.7 nM	947:968	K(d) = 21.7 +/- 1.7 nM	947:968	High-affinity binding to N(7)-Q(7) was similar (K(d) = 21.7 +/- 1.7 nM, n = 4) to that of the wild-type receptor (K(d) = 24.3 +/- 3.6 nM, n = 4), despite a reduced value for B(max) (0.35 +/- 0.03 fmol/mg of protein versus 3.34 +/- 0.52 fmol/mg of protein, n = 4).
11502878	12	12	theme	phosphate	1543:1551	arg1	generation					1553:1562	Inositol phosphate generation	1534:1562	Inositol phosphate generation	1534:1562	Inositol phosphate generation was evident only with the wild-type.
11502878	10	13	theme	protein	1221:1227	arg1	Binding					1163:1169	Binding	1163:1169	Binding to N(78)-Q(78) (B(max) = 0.27 +/- 0.03 fmol/mg of protein	1163:1227	Binding to N(78)-Q(78) (B(max) = 0.27 +/- 0.03 fmol/mg of protein, n = 3; K(d) = 149.1 +/- 11.1, n = 3) and N(7),N(78)-Q(7),Q(78) (no specific binding) was further impaired.
11502878	14	14	theme	greater	1710:1716	arg1	glycosylation					1718:1730	greater glycosylation	1710:1730	greater glycosylation at N(78)	1710:1739	Our findings demonstrate greater glycosylation at N(78) compared with N(7).
11502878	14	15	from	N	1735:1735	arg1	glycosylation					1718:1730	greater glycosylation	1710:1730	greater glycosylation at N(78)	1710:1739	Our findings demonstrate greater glycosylation at N(78) compared with N(7).
11502878	12	16	with	evident	1568:1574	arg1	wild-type					1590:1598	wild-type	1590:1598	wild-type	1590:1598	Inositol phosphate generation was evident only with the wild-type.
11502878	13	17	theme	agonist-induced	1654:1668	arg1	sequestration					1670:1682	agonist-induced sequestration	1654:1682	agonist-induced sequestration	1654:1682	Only the wild-type and N(7)-Q(7) receptors underwent agonist-induced sequestration.
11502878	15	18	gly	glycosylation	1784:1796	arg1	hIP					1801:1803	hIP	1801:1803	hIP	1801:1803	The extent of N-linked glycosylation of hIP may be important for membrane localization, ligand binding, and signal transduction.
11502878	5	19	from	N	565:565	arg1	similar					536:542	similar	536:542	similar	536:542	Receptor glycosylation was similar in the wild-type and N(7)-Q(7) and was inhibited with tunicamycin.
11502878	1	20	theme	platelet	150:157	arg1	aggregation					159:169	platelet aggregation	150:169	platelet aggregation	150:169	Prostacyclin, a potent vasodilator and inhibitor of platelet aggregation, acts through a cell-surface G protein-coupled receptor [prostacyclin (IP)].
11502878	0	21	theme	signal	77:82	arg1	transduction					84:95	signal transduction	77:95	signal transduction	77:95	Glycosylation of the human prostacyclin receptor: role in ligand binding and signal transduction.
11502878	5	22	from	wild-type	551:559	arg1	similar					536:542	similar	536:542	similar	536:542	Receptor glycosylation was similar in the wild-type and N(7)-Q(7) and was inhibited with tunicamycin.
11502878	11	23	theme	N	1396:1396	arg1	cells					1406:1410	N(7)-Q(7) cells	1396:1410	N(7)-Q(7) cells	1396:1410	Agonist-induced adenylyl cyclase activation was reduced in N(7)-Q(7) cells, whereas N(78)-Q(78) cells responded only to high concentrations of iloprost and N(7),N(78)-Q(7),Q(78) were unresponsive.
11502878	7	24	theme	Membrane	690:697	arg1	localization					699:710	Membrane localization	690:710	Membrane localization	690:710	Membrane localization was reduced for each mutant concomitant with impaired glycosylation.
11502878	14	25	gly	glycosylation	1718:1730	arg1	N					1735:1735	N(78)	1735:1739	N(78)	1735:1739	Our findings demonstrate greater glycosylation at N(78) compared with N(7).
11502878	14	25	gly	glycosylation	1718:1730	arg2	N					1735:1735	N(78)	1735:1739	N(78)	1735:1739	Our findings demonstrate greater glycosylation at N(78) compared with N(7).
11502878	9	26	theme	protein	1106:1112	arg1	B					1073:1073	B	1073:1073	B(max) (0.35 +/- 0.03 fmol/mg of protein versus 3.34 +/- 0.52 fmol/mg of protein, n = 4)	1073:1160	High-affinity binding to N(7)-Q(7) was similar (K(d) = 21.7 +/- 1.7 nM, n = 4) to that of the wild-type receptor (K(d) = 24.3 +/- 3.6 nM, n = 4), despite a reduced value for B(max) (0.35 +/- 0.03 fmol/mg of protein versus 3.34 +/- 0.52 fmol/mg of protein, n = 4).
11502878	9	26	theme	protein	1106:1112	arg1	fmol/mg					1095:1101	0.35 +/- 0.03 fmol/mg	1081:1101	0.35 +/- 0.03 fmol/mg of protein	1081:1112	High-affinity binding to N(7)-Q(7) was similar (K(d) = 21.7 +/- 1.7 nM, n = 4) to that of the wild-type receptor (K(d) = 24.3 +/- 3.6 nM, n = 4), despite a reduced value for B(max) (0.35 +/- 0.03 fmol/mg of protein versus 3.34 +/- 0.52 fmol/mg of protein, n = 4).
11502878	8	27	from	examination	840:850	arg1	function					889:896	IP function	886:896	IP function	886:896	Partial localization to the plasma membrane allowed direct examination of the effect of glycosylation on IP function.
11502878	2	28	dep	glycosylation	307:319	arg1	N					331:331	N(78)	331:335	N(78)	331:335	The human (h) IP contains two consensus sites for N-linked glycosylation (N(7) and N(78)).
11502878	2	28	dep	glycosylation	307:319	arg1	N					322:322	N(7)	322:325	N(7)	322:325	The human (h) IP contains two consensus sites for N-linked glycosylation (N(7) and N(78)).
11502878	8	29	gly	glycosylation	869:881	arg1	IP					886:887	IP function	886:896	IP function	886:896	Partial localization to the plasma membrane allowed direct examination of the effect of glycosylation on IP function.
11502878	9	30	theme	wild-type	993:1001	arg1	nM					1033:1034	K(d) = 24.3 +/- 3.6 nM	1013:1034	K(d) = 24.3 +/- 3.6 nM	1013:1034	High-affinity binding to N(7)-Q(7) was similar (K(d) = 21.7 +/- 1.7 nM, n = 4) to that of the wild-type receptor (K(d) = 24.3 +/- 3.6 nM, n = 4), despite a reduced value for B(max) (0.35 +/- 0.03 fmol/mg of protein versus 3.34 +/- 0.52 fmol/mg of protein, n = 4).
11502878	9	30	theme	wild-type	993:1001	arg1	receptor					1003:1010	the wild-type receptor	989:1010	the wild-type receptor (K(d) = 24.3 +/- 3.6 nM, n = 4)	989:1042	High-affinity binding to N(7)-Q(7) was similar (K(d) = 21.7 +/- 1.7 nM, n = 4) to that of the wild-type receptor (K(d) = 24.3 +/- 3.6 nM, n = 4), despite a reduced value for B(max) (0.35 +/- 0.03 fmol/mg of protein versus 3.34 +/- 0.52 fmol/mg of protein, n = 4).
11502878	0	31	theme	prostacyclin	27:38	arg1	receptor					40:47	the human prostacyclin receptor	17:47	the human prostacyclin receptor	17:47	Glycosylation of the human prostacyclin receptor: role in ligand binding and signal transduction.
11502878	15	32	theme	N-linked	1775:1782	arg1	glycosylation					1784:1796	N-linked glycosylation	1775:1796	N-linked glycosylation of hIP	1775:1803	The extent of N-linked glycosylation of hIP may be important for membrane localization, ligand binding, and signal transduction.
11502878	11	33	theme	Agonist-induced	1337:1351	arg1	activation					1370:1379	Agonist-induced adenylyl cyclase activation	1337:1379	Agonist-induced adenylyl cyclase activation	1337:1379	Agonist-induced adenylyl cyclase activation was reduced in N(7)-Q(7) cells, whereas N(78)-Q(78) cells responded only to high concentrations of iloprost and N(7),N(78)-Q(7),Q(78) were unresponsive.
11502878	1	34	theme	receptor	218:225	arg1	IP					242:243	IP	242:243	IP	242:243	Prostacyclin, a potent vasodilator and inhibitor of platelet aggregation, acts through a cell-surface G protein-coupled receptor [prostacyclin (IP)].
11502878	1	34	theme	receptor	218:225	arg1	[prostacyclin					227:239	a cell-surface G protein-coupled receptor [prostacyclin	185:239	a cell-surface G protein-coupled receptor [prostacyclin (IP)	185:244	Prostacyclin, a potent vasodilator and inhibitor of platelet aggregation, acts through a cell-surface G protein-coupled receptor [prostacyclin (IP)].
11502878	9	35	theme	=	1157:1157	arg1	n					1155:1155	n = 4	1155:1159	n = 4	1155:1159	High-affinity binding to N(7)-Q(7) was similar (K(d) = 21.7 +/- 1.7 nM, n = 4) to that of the wild-type receptor (K(d) = 24.3 +/- 3.6 nM, n = 4), despite a reduced value for B(max) (0.35 +/- 0.03 fmol/mg of protein versus 3.34 +/- 0.52 fmol/mg of protein, n = 4).
11502878	8	36	from	effect	859:864	arg1	function					889:896	IP function	886:896	IP function	886:896	Partial localization to the plasma membrane allowed direct examination of the effect of glycosylation on IP function.
11502878	0	37	dep	Glycosylation	0:12	arg1	role					50:53	role	50:53	Glycosylation of the human prostacyclin receptor: role in ligand binding and signal transduction.	0:96	Glycosylation of the human prostacyclin receptor: role in ligand binding and signal transduction.
11502878	7	38	with	concomitant	740:750	arg1	glycosylation					766:778	impaired glycosylation	757:778	impaired glycosylation	757:778	Membrane localization was reduced for each mutant concomitant with impaired glycosylation.
11502878	15	39	link	N-linked	1775:1782	arg1	glycosylation					1784:1796	N-linked glycosylation	1775:1796	N-linked glycosylation of hIP	1775:1803	The extent of N-linked glycosylation of hIP may be important for membrane localization, ligand binding, and signal transduction.
11502878	15	40	theme	membrane	1826:1833	arg1	localization					1835:1846	membrane localization	1826:1846	membrane localization	1826:1846	The extent of N-linked glycosylation of hIP may be important for membrane localization, ligand binding, and signal transduction.
11502878	11	41	theme	cyclase	1362:1368	arg1	activation					1370:1379	Agonist-induced adenylyl cyclase activation	1337:1379	Agonist-induced adenylyl cyclase activation	1337:1379	Agonist-induced adenylyl cyclase activation was reduced in N(7)-Q(7) cells, whereas N(78)-Q(78) cells responded only to high concentrations of iloprost and N(7),N(78)-Q(7),Q(78) were unresponsive.
11502878	2	42	link	N-linked	298:305	arg1	glycosylation					307:319	N-linked glycosylation	298:319	N-linked glycosylation (N(7) and N(78))	298:336	The human (h) IP contains two consensus sites for N-linked glycosylation (N(7) and N(78)).
11502878	6	43	theme	no	672:673	arg1	glycosylation					675:687	no glycosylation	672:687	no glycosylation	672:687	N(78)-Q(78) and N(7),N(78)-Q(7),Q(78) demonstrated little or no glycosylation.
11502878	1	44	theme	aggregation	159:169	arg1	inhibitor					137:145	a potent vasodilator and inhibitor	112:145	inhibitor	137:145	Prostacyclin, a potent vasodilator and inhibitor of platelet aggregation, acts through a cell-surface G protein-coupled receptor [prostacyclin (IP)].
11502878	1	44	theme	aggregation	159:169	arg1	vasodilator					121:131	a potent vasodilator and inhibitor	112:145	vasodilator	121:131	Prostacyclin, a potent vasodilator and inhibitor of platelet aggregation, acts through a cell-surface G protein-coupled receptor [prostacyclin (IP)].
11502878	1	44	theme	aggregation	159:169	arg1	Prostacyclin					98:109	Prostacyclin	98:109	Prostacyclin	98:109	Prostacyclin, a potent vasodilator and inhibitor of platelet aggregation, acts through a cell-surface G protein-coupled receptor [prostacyclin (IP)].
11502878	9	45	theme	=	1039:1039	arg1	n					1037:1037	n = 4	1037:1041	n = 4	1037:1041	High-affinity binding to N(7)-Q(7) was similar (K(d) = 21.7 +/- 1.7 nM, n = 4) to that of the wild-type receptor (K(d) = 24.3 +/- 3.6 nM, n = 4), despite a reduced value for B(max) (0.35 +/- 0.03 fmol/mg of protein versus 3.34 +/- 0.52 fmol/mg of protein, n = 4).
11502878	2	46	theme	consensus	278:286	arg1	sites					288:292	two consensus sites	274:292	two consensus sites for N-linked glycosylation (N(7) and N(78))	274:336	The human (h) IP contains two consensus sites for N-linked glycosylation (N(7) and N(78)).
11502878	11	47	dep	reduced	1385:1391	arg1	whereas					1413:1419	whereas	1413:1419	whereas	1413:1419	Agonist-induced adenylyl cyclase activation was reduced in N(7)-Q(7) cells, whereas N(78)-Q(78) cells responded only to high concentrations of iloprost and N(7),N(78)-Q(7),Q(78) were unresponsive.
11502878	5	48	theme	Receptor	509:516	arg1	glycosylation					518:530	Receptor glycosylation	509:530	Receptor glycosylation	509:530	Receptor glycosylation was similar in the wild-type and N(7)-Q(7) and was inhibited with tunicamycin.
11502878	9	49	theme	reduced	1055:1061	arg1	value					1063:1067	a reduced value	1053:1067	a reduced value for B(max) (0.35 +/- 0.03 fmol/mg of protein versus 3.34 +/- 0.52 fmol/mg of protein, n = 4)	1053:1160	High-affinity binding to N(7)-Q(7) was similar (K(d) = 21.7 +/- 1.7 nM, n = 4) to that of the wild-type receptor (K(d) = 24.3 +/- 3.6 nM, n = 4), despite a reduced value for B(max) (0.35 +/- 0.03 fmol/mg of protein versus 3.34 +/- 0.52 fmol/mg of protein, n = 4).
11502878	11	50	theme	high	1457:1460	arg1	concentrations					1462:1475	high concentrations	1457:1475	high concentrations of iloprost	1457:1487	Agonist-induced adenylyl cyclase activation was reduced in N(7)-Q(7) cells, whereas N(78)-Q(78) cells responded only to high concentrations of iloprost and N(7),N(78)-Q(7),Q(78) were unresponsive.
11502878	4	51	dep	N	404:404	arg1	N					435:435	N(78)-Q(7)	435:444	N(78)-Q(7)	435:444	Mutant receptors (N(7)-Q(7),N(78)-Q(78) and N(7),N(78)-Q(7),Q(78)) were generated by replacing N(7) and/or N(78) with Q's.
11502878	4	51	dep	N	404:404	arg1	Q					446:446	Q(78)	446:450	Q(78)	446:450	Mutant receptors (N(7)-Q(7),N(78)-Q(78) and N(7),N(78)-Q(7),Q(78)) were generated by replacing N(7) and/or N(78) with Q's.
11502878	9	52	dep	fmol/mg	1095:1101	arg1	n					1155:1155	n = 4	1155:1159	n = 4	1155:1159	High-affinity binding to N(7)-Q(7) was similar (K(d) = 21.7 +/- 1.7 nM, n = 4) to that of the wild-type receptor (K(d) = 24.3 +/- 3.6 nM, n = 4), despite a reduced value for B(max) (0.35 +/- 0.03 fmol/mg of protein versus 3.34 +/- 0.52 fmol/mg of protein, n = 4).
11502878	15	53	theme	signal	1869:1874	arg1	transduction					1876:1887	signal transduction	1869:1887	signal transduction	1869:1887	The extent of N-linked glycosylation of hIP may be important for membrane localization, ligand binding, and signal transduction.
11502878	1	54	theme	potent	114:119	arg1	vasodilator					121:131	a potent vasodilator and inhibitor	112:145	vasodilator	121:131	Prostacyclin, a potent vasodilator and inhibitor of platelet aggregation, acts through a cell-surface G protein-coupled receptor [prostacyclin (IP)].
11502878	1	54	theme	potent	114:119	arg1	Prostacyclin					98:109	Prostacyclin	98:109	Prostacyclin	98:109	Prostacyclin, a potent vasodilator and inhibitor of platelet aggregation, acts through a cell-surface G protein-coupled receptor [prostacyclin (IP)].
11502878	12	55	theme	Inositol	1534:1541	arg1	generation					1553:1562	Inositol phosphate generation	1534:1562	Inositol phosphate generation	1534:1562	Inositol phosphate generation was evident only with the wild-type.
11502878	0	56	theme	ligand	58:63	arg1	binding					65:71	ligand binding	58:71	ligand binding	58:71	Glycosylation of the human prostacyclin receptor: role in ligand binding and signal transduction.
11502878	10	57	dep	=	1194:1194	arg1	fmol/mg					1210:1216	0.27 +/- 0.03 fmol/mg	1196:1216	0.27 +/- 0.03 fmol/mg	1196:1216	Binding to N(78)-Q(78) (B(max) = 0.27 +/- 0.03 fmol/mg of protein, n = 3; K(d) = 149.1 +/- 11.1, n = 3) and N(7),N(78)-Q(7),Q(78) (no specific binding) was further impaired.
11502878	11	58	theme	N	1421:1421	arg1	cells					1433:1437	N(78)-Q(78) cells	1421:1437	N(78)-Q(78) cells	1421:1437	Agonist-induced adenylyl cyclase activation was reduced in N(7)-Q(7) cells, whereas N(78)-Q(78) cells responded only to high concentrations of iloprost and N(7),N(78)-Q(7),Q(78) were unresponsive.
11502878	8	59	theme	direct	833:838	arg1	examination					840:850	direct examination	833:850	direct examination of the effect of glycosylation on IP function	833:896	Partial localization to the plasma membrane allowed direct examination of the effect of glycosylation on IP function.
11502878	5	60	from	similar	536:542	arg1	N					565:565	N(7)-Q	565:570	N(7)-Q(7)	565:573	Receptor glycosylation was similar in the wild-type and N(7)-Q(7) and was inhibited with tunicamycin.
11502878	5	60	from	similar	536:542	arg1	wild-type					551:559	wild-type	551:559	wild-type	551:559	Receptor glycosylation was similar in the wild-type and N(7)-Q(7) and was inhibited with tunicamycin.
11502878	5	60	from	similar	536:542	arg1	7					572:572	7	572:572	7	572:572	Receptor glycosylation was similar in the wild-type and N(7)-Q(7) and was inhibited with tunicamycin.
11502878	0	61	from	role	50:53	arg1	binding					65:71	ligand binding	58:71	ligand binding	58:71	Glycosylation of the human prostacyclin receptor: role in ligand binding and signal transduction.
11502878	0	61	from	role	50:53	arg1	transduction					84:95	signal transduction	77:95	signal transduction	77:95	Glycosylation of the human prostacyclin receptor: role in ligand binding and signal transduction.
11502878	13	62	dep	wild-type	1610:1618	arg1	receptors					1634:1642	receptors	1634:1642	receptors	1634:1642	Only the wild-type and N(7)-Q(7) receptors underwent agonist-induced sequestration.
11502878	9	63	theme	=	973:973	arg1	n					971:971	n = 4	971:975	n = 4	971:975	High-affinity binding to N(7)-Q(7) was similar (K(d) = 21.7 +/- 1.7 nM, n = 4) to that of the wild-type receptor (K(d) = 24.3 +/- 3.6 nM, n = 4), despite a reduced value for B(max) (0.35 +/- 0.03 fmol/mg of protein versus 3.34 +/- 0.52 fmol/mg of protein, n = 4).
11502878	4	64	theme	Mutant	386:391	arg1	receptors					393:401	Mutant receptors	386:401	Mutant receptors (N(7)-Q(7),N(78)-Q(78) and N(7),N(78)-Q(7),Q(78))	386:451	Mutant receptors (N(7)-Q(7),N(78)-Q(78) and N(7),N(78)-Q(7),Q(78)) were generated by replacing N(7) and/or N(78) with Q's.
11502878	4	64	theme	Mutant	386:391	arg1	N					414:414	N(78)-Q(78)	414:424	N(78)-Q(78)	414:424	Mutant receptors (N(7)-Q(7),N(78)-Q(78) and N(7),N(78)-Q(7),Q(78)) were generated by replacing N(7) and/or N(78) with Q's.
11502878	4	64	theme	Mutant	386:391	arg1	N					430:430	N(7)	430:433	N(7)	430:433	Mutant receptors (N(7)-Q(7),N(78)-Q(78) and N(7),N(78)-Q(7),Q(78)) were generated by replacing N(7) and/or N(78) with Q's.
11502878	4	64	theme	Mutant	386:391	arg1	N					404:404	N(7)-Q(7)	404:412	N(7)-Q(7)	404:412	Mutant receptors (N(7)-Q(7),N(78)-Q(78) and N(7),N(78)-Q(7),Q(78)) were generated by replacing N(7) and/or N(78) with Q's.
11502878	8	65	theme	effect	859:864	arg1	examination					840:850	direct examination	833:850	direct examination of the effect of glycosylation on IP function	833:896	Partial localization to the plasma membrane allowed direct examination of the effect of glycosylation on IP function.
11502878	8	66	theme	glycosylation	869:881	arg1	effect					859:864	the effect	855:864	the effect of glycosylation on IP function	855:896	Partial localization to the plasma membrane allowed direct examination of the effect of glycosylation on IP function.
11502878	9	67	dep	nM	1033:1034	arg1	n					1037:1037	n = 4	1037:1041	n = 4	1037:1041	High-affinity binding to N(7)-Q(7) was similar (K(d) = 21.7 +/- 1.7 nM, n = 4) to that of the wild-type receptor (K(d) = 24.3 +/- 3.6 nM, n = 4), despite a reduced value for B(max) (0.35 +/- 0.03 fmol/mg of protein versus 3.34 +/- 0.52 fmol/mg of protein, n = 4).
11502878	15	68	theme	hIP	1801:1803	arg1	glycosylation					1784:1796	N-linked glycosylation	1775:1796	N-linked glycosylation of hIP	1775:1803	The extent of N-linked glycosylation of hIP may be important for membrane localization, ligand binding, and signal transduction.
11502878	8	69	theme	IP	886:887	arg1	function					889:896	IP function	886:896	IP function	886:896	Partial localization to the plasma membrane allowed direct examination of the effect of glycosylation on IP function.
11502878	0	70	theme	human	21:25	arg1	receptor					40:47	the human prostacyclin receptor	17:47	the human prostacyclin receptor	17:47	Glycosylation of the human prostacyclin receptor: role in ligand binding and signal transduction.
11502878	4	71	dep	receptors	393:401	arg1	receptors					393:401	Mutant receptors	386:401	Mutant receptors (N(7)-Q(7),N(78)-Q(78) and N(7),N(78)-Q(7),Q(78))	386:451	Mutant receptors (N(7)-Q(7),N(78)-Q(78) and N(7),N(78)-Q(7),Q(78)) were generated by replacing N(7) and/or N(78) with Q's.
11502878	4	71	dep	receptors	393:401	arg1	N					414:414	N(78)-Q(78)	414:424	N(78)-Q(78)	414:424	Mutant receptors (N(7)-Q(7),N(78)-Q(78) and N(7),N(78)-Q(7),Q(78)) were generated by replacing N(7) and/or N(78) with Q's.
11502878	4	71	dep	receptors	393:401	arg1	N					430:430	N(7)	430:433	N(7)	430:433	Mutant receptors (N(7)-Q(7),N(78)-Q(78) and N(7),N(78)-Q(7),Q(78)) were generated by replacing N(7) and/or N(78) with Q's.
11502878	4	71	dep	receptors	393:401	arg1	N					404:404	N(7)-Q(7)	404:412	N(7)-Q(7)	404:412	Mutant receptors (N(7)-Q(7),N(78)-Q(78) and N(7),N(78)-Q(7),Q(78)) were generated by replacing N(7) and/or N(78) with Q's.
11502878	15	72	theme	glycosylation	1784:1796	arg1	important					1812:1820	important	1812:1820	important	1812:1820	The extent of N-linked glycosylation of hIP may be important for membrane localization, ligand binding, and signal transduction.
11502878	15	72	theme	glycosylation	1784:1796	arg1	extent					1765:1770	The extent	1761:1770	The extent of N-linked glycosylation of hIP	1761:1803	The extent of N-linked glycosylation of hIP may be important for membrane localization, ligand binding, and signal transduction.
11502878	9	73	dep	nM	967:968	arg1	n					971:971	n = 4	971:975	n = 4	971:975	High-affinity binding to N(7)-Q(7) was similar (K(d) = 21.7 +/- 1.7 nM, n = 4) to that of the wild-type receptor (K(d) = 24.3 +/- 3.6 nM, n = 4), despite a reduced value for B(max) (0.35 +/- 0.03 fmol/mg of protein versus 3.34 +/- 0.52 fmol/mg of protein, n = 4).
11502878	0	74	theme	receptor	40:47	arg1	Glycosylation					0:12	Glycosylation	0:12	Glycosylation of the human prostacyclin receptor: role in ligand binding and signal transduction.	0:96	Glycosylation of the human prostacyclin receptor: role in ligand binding and signal transduction.
11502878	0	75	gly	Glycosylation	0:12	arg1	receptor					40:47	the human prostacyclin receptor	17:47	the human prostacyclin receptor	17:47	Glycosylation of the human prostacyclin receptor: role in ligand binding and signal transduction.
11502878	9	76	dep	similar	938:944	arg1	nM					967:968	K(d) = 21.7 +/- 1.7 nM	947:968	K(d) = 21.7 +/- 1.7 nM	947:968	High-affinity binding to N(7)-Q(7) was similar (K(d) = 21.7 +/- 1.7 nM, n = 4) to that of the wild-type receptor (K(d) = 24.3 +/- 3.6 nM, n = 4), despite a reduced value for B(max) (0.35 +/- 0.03 fmol/mg of protein versus 3.34 +/- 0.52 fmol/mg of protein, n = 4).
11502878	3	77	theme	glycosylation	360:372	arg1	role					352:355	the role	348:355	the role of glycosylation	348:372	However, the role of glycosylation is unknown.
11502878	3	77	theme	glycosylation	360:372	arg1	unknown					377:383	unknown	377:383	unknown	377:383	However, the role of glycosylation is unknown.
11502878	2	78	contain	contains	265:272	arg2	sites					288:292	two consensus sites	274:292	two consensus sites for N-linked glycosylation (N(7) and N(78))	274:336	The human (h) IP contains two consensus sites for N-linked glycosylation (N(7) and N(78)).
11502878	2	78	contain	contains	265:272	arg1	IP					262:263	The human (h) IP	248:263	The human (h) IP	248:263	The human (h) IP contains two consensus sites for N-linked glycosylation (N(7) and N(78)).
11502878	9	79	theme	K	1013:1013	arg1	nM					1033:1034	K(d) = 24.3 +/- 3.6 nM	1013:1034	K(d) = 24.3 +/- 3.6 nM	1013:1034	High-affinity binding to N(7)-Q(7) was similar (K(d) = 21.7 +/- 1.7 nM, n = 4) to that of the wild-type receptor (K(d) = 24.3 +/- 3.6 nM, n = 4), despite a reduced value for B(max) (0.35 +/- 0.03 fmol/mg of protein versus 3.34 +/- 0.52 fmol/mg of protein, n = 4).
11502878	9	79	theme	K	1013:1013	arg1	receptor					1003:1010	the wild-type receptor	989:1010	the wild-type receptor (K(d) = 24.3 +/- 3.6 nM, n = 4)	989:1042	High-affinity binding to N(7)-Q(7) was similar (K(d) = 21.7 +/- 1.7 nM, n = 4) to that of the wild-type receptor (K(d) = 24.3 +/- 3.6 nM, n = 4), despite a reduced value for B(max) (0.35 +/- 0.03 fmol/mg of protein versus 3.34 +/- 0.52 fmol/mg of protein, n = 4).
11502878	10	80	dep	3	1264:1264	arg1	K					1237:1237	K	1237:1237	K	1237:1237	Binding to N(78)-Q(78) (B(max) = 0.27 +/- 0.03 fmol/mg of protein, n = 3; K(d) = 149.1 +/- 11.1, n = 3) and N(7),N(78)-Q(7),Q(78) (no specific binding) was further impaired.
11502878	10	80	dep	3	1264:1264	arg1	149.1					1244:1248	149.1	1244:1248	149.1	1244:1248	Binding to N(78)-Q(78) (B(max) = 0.27 +/- 0.03 fmol/mg of protein, n = 3; K(d) = 149.1 +/- 11.1, n = 3) and N(7),N(78)-Q(7),Q(78) (no specific binding) was further impaired.
11502878	10	80	dep	3	1264:1264	arg1	d					1239:1239	d	1239:1239	d	1239:1239	Binding to N(78)-Q(78) (B(max) = 0.27 +/- 0.03 fmol/mg of protein, n = 3; K(d) = 149.1 +/- 11.1, n = 3) and N(7),N(78)-Q(7),Q(78) (no specific binding) was further impaired.
11502878	10	80	dep	3	1264:1264	arg1	n					1260:1260	n	1260:1260	n	1260:1260	Binding to N(78)-Q(78) (B(max) = 0.27 +/- 0.03 fmol/mg of protein, n = 3; K(d) = 149.1 +/- 11.1, n = 3) and N(7),N(78)-Q(7),Q(78) (no specific binding) was further impaired.
11502878	10	80	dep	3	1264:1264	arg1	n					1230:1230	n	1230:1230	n	1230:1230	Binding to N(78)-Q(78) (B(max) = 0.27 +/- 0.03 fmol/mg of protein, n = 3; K(d) = 149.1 +/- 11.1, n = 3) and N(7),N(78)-Q(7),Q(78) (no specific binding) was further impaired.
11502878	10	80	dep	3	1264:1264	arg1	=					1262:1262	=	1262:1262	=	1262:1262	Binding to N(78)-Q(78) (B(max) = 0.27 +/- 0.03 fmol/mg of protein, n = 3; K(d) = 149.1 +/- 11.1, n = 3) and N(7),N(78)-Q(7),Q(78) (no specific binding) was further impaired.
11502878	10	80	dep	3	1264:1264	arg1	=					1232:1232	=	1232:1232	=	1232:1232	Binding to N(78)-Q(78) (B(max) = 0.27 +/- 0.03 fmol/mg of protein, n = 3; K(d) = 149.1 +/- 11.1, n = 3) and N(7),N(78)-Q(7),Q(78) (no specific binding) was further impaired.
11502878	10	80	dep	3	1264:1264	arg1	3					1234:1234	3	1234:1234	3	1234:1234	Binding to N(78)-Q(78) (B(max) = 0.27 +/- 0.03 fmol/mg of protein, n = 3; K(d) = 149.1 +/- 11.1, n = 3) and N(7),N(78)-Q(7),Q(78) (no specific binding) was further impaired.
11502878	10	80	dep	3	1264:1264	arg1	=					1242:1242	=	1242:1242	=	1242:1242	Binding to N(78)-Q(78) (B(max) = 0.27 +/- 0.03 fmol/mg of protein, n = 3; K(d) = 149.1 +/- 11.1, n = 3) and N(7),N(78)-Q(7),Q(78) (no specific binding) was further impaired.
11502878	10	80	dep	3	1264:1264	arg1	Binding					1163:1169	Binding	1163:1169	Binding to N(78)-Q(78) (B(max) = 0.27 +/- 0.03 fmol/mg of protein	1163:1227	Binding to N(78)-Q(78) (B(max) = 0.27 +/- 0.03 fmol/mg of protein, n = 3; K(d) = 149.1 +/- 11.1, n = 3) and N(7),N(78)-Q(7),Q(78) (no specific binding) was further impaired.
11502878	9	81	theme	protein	1146:1152	arg1	fmol/mg					1135:1141	3.34 +/- 0.52 fmol/mg	1121:1141	3.34 +/- 0.52 fmol/mg of protein	1121:1152	High-affinity binding to N(7)-Q(7) was similar (K(d) = 21.7 +/- 1.7 nM, n = 4) to that of the wild-type receptor (K(d) = 24.3 +/- 3.6 nM, n = 4), despite a reduced value for B(max) (0.35 +/- 0.03 fmol/mg of protein versus 3.34 +/- 0.52 fmol/mg of protein, n = 4).
11502878	9	81	theme	protein	1146:1152	arg1	B					1073:1073	B	1073:1073	B(max) (0.35 +/- 0.03 fmol/mg of protein versus 3.34 +/- 0.52 fmol/mg of protein, n = 4)	1073:1160	High-affinity binding to N(7)-Q(7) was similar (K(d) = 21.7 +/- 1.7 nM, n = 4) to that of the wild-type receptor (K(d) = 24.3 +/- 3.6 nM, n = 4), despite a reduced value for B(max) (0.35 +/- 0.03 fmol/mg of protein versus 3.34 +/- 0.52 fmol/mg of protein, n = 4).
11502878	2	82	theme	N-linked	298:305	arg1	glycosylation					307:319	N-linked glycosylation	298:319	N-linked glycosylation (N(7) and N(78))	298:336	The human (h) IP contains two consensus sites for N-linked glycosylation (N(7) and N(78)).
11502878	9	83	theme	High-affinity	899:911	arg1	binding					913:919	High-affinity binding	899:919	High-affinity binding to N(7)-Q(7)	899:932	High-affinity binding to N(7)-Q(7) was similar (K(d) = 21.7 +/- 1.7 nM, n = 4) to that of the wild-type receptor (K(d) = 24.3 +/- 3.6 nM, n = 4), despite a reduced value for B(max) (0.35 +/- 0.03 fmol/mg of protein versus 3.34 +/- 0.52 fmol/mg of protein, n = 4).
11502878	9	84	theme	d	1015:1015	arg1	nM					1033:1034	K(d) = 24.3 +/- 3.6 nM	1013:1034	K(d) = 24.3 +/- 3.6 nM	1013:1034	High-affinity binding to N(7)-Q(7) was similar (K(d) = 21.7 +/- 1.7 nM, n = 4) to that of the wild-type receptor (K(d) = 24.3 +/- 3.6 nM, n = 4), despite a reduced value for B(max) (0.35 +/- 0.03 fmol/mg of protein versus 3.34 +/- 0.52 fmol/mg of protein, n = 4).
11502878	9	84	theme	d	1015:1015	arg1	receptor					1003:1010	the wild-type receptor	989:1010	the wild-type receptor (K(d) = 24.3 +/- 3.6 nM, n = 4)	989:1042	High-affinity binding to N(7)-Q(7) was similar (K(d) = 21.7 +/- 1.7 nM, n = 4) to that of the wild-type receptor (K(d) = 24.3 +/- 3.6 nM, n = 4), despite a reduced value for B(max) (0.35 +/- 0.03 fmol/mg of protein versus 3.34 +/- 0.52 fmol/mg of protein, n = 4).
11502878	15	85	theme	ligand	1849:1854	arg1	binding					1856:1862	ligand binding	1849:1862	ligand binding	1849:1862	The extent of N-linked glycosylation of hIP may be important for membrane localization, ligand binding, and signal transduction.
11502878	11	86	theme	adenylyl	1353:1360	arg1	activation					1370:1379	Agonist-induced adenylyl cyclase activation	1337:1379	Agonist-induced adenylyl cyclase activation	1337:1379	Agonist-induced adenylyl cyclase activation was reduced in N(7)-Q(7) cells, whereas N(78)-Q(78) cells responded only to high concentrations of iloprost and N(7),N(78)-Q(7),Q(78) were unresponsive.
11502878	9	87	theme	=	1018:1018	arg1	nM					1033:1034	K(d) = 24.3 +/- 3.6 nM	1013:1034	K(d) = 24.3 +/- 3.6 nM	1013:1034	High-affinity binding to N(7)-Q(7) was similar (K(d) = 21.7 +/- 1.7 nM, n = 4) to that of the wild-type receptor (K(d) = 24.3 +/- 3.6 nM, n = 4), despite a reduced value for B(max) (0.35 +/- 0.03 fmol/mg of protein versus 3.34 +/- 0.52 fmol/mg of protein, n = 4).
11502878	9	87	theme	=	1018:1018	arg1	receptor					1003:1010	the wild-type receptor	989:1010	the wild-type receptor (K(d) = 24.3 +/- 3.6 nM, n = 4)	989:1042	High-affinity binding to N(7)-Q(7) was similar (K(d) = 21.7 +/- 1.7 nM, n = 4) to that of the wild-type receptor (K(d) = 24.3 +/- 3.6 nM, n = 4), despite a reduced value for B(max) (0.35 +/- 0.03 fmol/mg of protein versus 3.34 +/- 0.52 fmol/mg of protein, n = 4).
11502878	7	88	theme	impaired	757:764	arg1	glycosylation					766:778	impaired glycosylation	757:778	impaired glycosylation	757:778	Membrane localization was reduced for each mutant concomitant with impaired glycosylation.
17803183	12	0	theme	beta-chain	1947:1956	arg1	region					1933:1938	a defined peptide region	1915:1938	a defined peptide region of its beta-chain	1915:1956	In summary, levels of haptoglobin are enhanced in sera of prostate cancer patients, and the N-glycans attached to a defined peptide region of its beta-chain are characterized by enhanced branching as well as antenna fucosylation.
17803183	1	1	gly	glycosylation	155:167	arg1	haptoglobin					179:189	haptoglobin	179:189	haptoglobin	179:189	We studied chemical level and glycosylation status of haptoglobin in sera of patients with prostate cancer, as compared to benign prostate disease and normal subjects, with the following results.
17803183	10	2	theme	mass	1643:1646	arg1	analysis					1662:1669	mass spectrometric analysis	1643:1669	mass spectrometric analysis	1643:1669	Mono- and disialyl core Type 1 O-linked structures were identified after reductive beta-elimination followed by methylation and mass spectrometric analysis.
17803183	4	3	theme	N-linked	553:560	arg1	bi-antennary					595:606	bi-antennary	595:606	bi-antennary	595:606	The N-linked glycans at N184 were exclusively bi-antennary, and showed no difference between prostate cancer vs. benign prostate disease.
17803183	4	3	theme	N-linked	553:560	arg1	glycans					562:568	The N-linked glycans	549:568	The N-linked glycans at N184	549:576	The N-linked glycans at N184 were exclusively bi-antennary, and showed no difference between prostate cancer vs. benign prostate disease.
17803183	9	4	theme	cancer	1476:1481	arg1	haptoglobin					1483:1493	prostate cancer haptoglobin	1467:1493	prostate cancer haptoglobin	1467:1493	(v) Minor levels of O-glycosylation were identified in prostate cancer haptoglobin for the first time.
17803183	1	5	theme	benign	248:253	arg1	disease					264:270	benign prostate disease	248:270	benign prostate disease	248:270	We studied chemical level and glycosylation status of haptoglobin in sera of patients with prostate cancer, as compared to benign prostate disease and normal subjects, with the following results.
17803183	12	6	theme	peptide	1925:1931	arg1	region					1933:1938	a defined peptide region	1915:1938	a defined peptide region of its beta-chain	1915:1956	In summary, levels of haptoglobin are enhanced in sera of prostate cancer patients, and the N-glycans attached to a defined peptide region of its beta-chain are characterized by enhanced branching as well as antenna fucosylation.
17803183	7	7	theme	N-linked	1031:1038	arg1	glycan					1040:1045	A minor tri-antennary N-linked glycan	1009:1045	A minor tri-antennary N-linked glycan	1009:1045	A minor tri-antennary N-linked glycan was observed at N241 of the beta-chain in prostate cancer, which was absent in benign prostate disease.
17803183	5	8	theme	sialyl-Lewis	759:770	arg1	antenna					777:783	at least 1 sialyl-Lewis(x/a) antenna	748:783	at least 1 sialyl-Lewis(x/a) antenna	748:783	(iii) Tri-antennary, N-linked, fucosylated glycans, carrying at least 1 sialyl-Lewis(x/a) antenna, were predominantly located on N207 or N211 within the amino acid 203-215 sequence of the beta-chain of prostate cancer, and were minimal in benign prostate disease.
17803183	7	9	theme	minor	1011:1015	arg1	glycan					1040:1045	A minor tri-antennary N-linked glycan	1009:1045	A minor tri-antennary N-linked glycan	1009:1045	A minor tri-antennary N-linked glycan was observed at N241 of the beta-chain in prostate cancer, which was absent in benign prostate disease.
17803183	3	10	from	structures	453:462	arg1	sources					491:497	all 3 sources	485:497	all 3 sources	485:497	(ii) Sialylated bi-antennary glycans were the dominant structures in haptoglobins from all 3 sources, regardless of different site of N-linked glycan.
17803183	3	10	from	structures	453:462	arg1	haptoglobins					467:478	haptoglobins	467:478	haptoglobins from all 3 sources	467:497	(ii) Sialylated bi-antennary glycans were the dominant structures in haptoglobins from all 3 sources, regardless of different site of N-linked glycan.
17803183	3	11	theme	N-linked	532:539	arg1	glycan					541:546	N-linked glycan	532:546	N-linked glycan	532:546	(ii) Sialylated bi-antennary glycans were the dominant structures in haptoglobins from all 3 sources, regardless of different site of N-linked glycan.
17803183	1	12	theme	haptoglobin	179:189	arg1	level					145:149	chemical level	136:149	chemical level	136:149	We studied chemical level and glycosylation status of haptoglobin in sera of patients with prostate cancer, as compared to benign prostate disease and normal subjects, with the following results.
17803183	1	12	theme	haptoglobin	179:189	arg1	status					169:174	glycosylation status	155:174	glycosylation status of haptoglobin	155:189	We studied chemical level and glycosylation status of haptoglobin in sera of patients with prostate cancer, as compared to benign prostate disease and normal subjects, with the following results.
17803183	11	13	theme	specific	1714:1721	arg1	RM2					1723:1725	specific RM2	1714:1725	specific RM2	1714:1725	No evidence was found for the presence of specific RM2 or other tumor-associated glycosyl epitopes linked to this O-glycan core.
17803183	0	14	theme	normal	108:113	arg1	subjects					115:122	normal subjects	108:122	normal subjects	108:122	Glycosylation status of haptoglobin in sera of patients with prostate cancer vs. benign prostate disease or normal subjects.
17803183	5	15	located	located	805:811	arg2	glycans					730:736	(iii) Tri-antennary, N-linked, fucosylated glycans	687:736	glycans	730:736	(iii) Tri-antennary, N-linked, fucosylated glycans, carrying at least 1 sialyl-Lewis(x/a) antenna, were predominantly located on N207 or N211 within the amino acid 203-215 sequence of the beta-chain of prostate cancer, and were minimal in benign prostate disease.
17803183	5	15	located	located	805:811	arg1	N207					816:819	N207	816:819	N207	816:819	(iii) Tri-antennary, N-linked, fucosylated glycans, carrying at least 1 sialyl-Lewis(x/a) antenna, were predominantly located on N207 or N211 within the amino acid 203-215 sequence of the beta-chain of prostate cancer, and were minimal in benign prostate disease.
17803183	5	15	located	located	805:811	arg1	N211					824:827	N211	824:827	N211	824:827	(iii) Tri-antennary, N-linked, fucosylated glycans, carrying at least 1 sialyl-Lewis(x/a) antenna, were predominantly located on N207 or N211 within the amino acid 203-215 sequence of the beta-chain of prostate cancer, and were minimal in benign prostate disease.
17803183	5	15	located	located	805:811	arg1	sequence					859:866	the amino acid 203-215 sequence	836:866	the amino acid 203-215 sequence of the beta-chain of prostate cancer	836:903	(iii) Tri-antennary, N-linked, fucosylated glycans, carrying at least 1 sialyl-Lewis(x/a) antenna, were predominantly located on N207 or N211 within the amino acid 203-215 sequence of the beta-chain of prostate cancer, and were minimal in benign prostate disease.
17803183	12	16	theme	cancer	1868:1873	arg1	patients					1875:1882	prostate cancer patients	1859:1882	prostate cancer patients	1859:1882	In summary, levels of haptoglobin are enhanced in sera of prostate cancer patients, and the N-glycans attached to a defined peptide region of its beta-chain are characterized by enhanced branching as well as antenna fucosylation.
17803183	8	17	theme	structures	1179:1188	arg1	None					1156:1159	(iv) None	1151:1159	(iv) None of these N-linked structures	1151:1188	(iv) None of these N-linked structures showed the expected presence of disialylated antennae with GalNAcbeta4(NeuAcalpha3)Galbeta3(NeuAcalpha6)GlcNAcbetaGal, or its analogue, despite cross-reactivity of prostate cancer haptoglobin with monoclonal antibody RM2.
17803183	10	18	theme	core	1534:1537	arg1	structures					1555:1564	Mono- and disialyl core Type 1 O-linked structures	1515:1564	Mono- and disialyl core Type 1 O-linked structures	1515:1564	Mono- and disialyl core Type 1 O-linked structures were identified after reductive beta-elimination followed by methylation and mass spectrometric analysis.
17803183	8	19	with	cross-reactivity	1334:1349	arg1	RM2					1407:1409	monoclonal antibody RM2	1387:1409	monoclonal antibody RM2	1387:1409	(iv) None of these N-linked structures showed the expected presence of disialylated antennae with GalNAcbeta4(NeuAcalpha3)Galbeta3(NeuAcalpha6)GlcNAcbetaGal, or its analogue, despite cross-reactivity of prostate cancer haptoglobin with monoclonal antibody RM2.
17803183	1	20	theme	patients	202:209	arg1	sera					194:197	sera	194:197	sera of patients with prostate cancer	194:230	We studied chemical level and glycosylation status of haptoglobin in sera of patients with prostate cancer, as compared to benign prostate disease and normal subjects, with the following results.
17803183	8	21	theme	cancer	1363:1368	arg1	haptoglobin					1370:1380	prostate cancer haptoglobin	1354:1380	prostate cancer haptoglobin	1354:1380	(iv) None of these N-linked structures showed the expected presence of disialylated antennae with GalNAcbeta4(NeuAcalpha3)Galbeta3(NeuAcalpha6)GlcNAcbetaGal, or its analogue, despite cross-reactivity of prostate cancer haptoglobin with monoclonal antibody RM2.
17803183	11	22	theme	tumor-associated	1736:1751	arg1	epitopes					1762:1769	other tumor-associated glycosyl epitopes	1730:1769	other tumor-associated glycosyl epitopes	1730:1769	No evidence was found for the presence of specific RM2 or other tumor-associated glycosyl epitopes linked to this O-glycan core.
17803183	12	23	attach	attached	1903:1910	arg2	N-glycans					1893:1901	the N-glycans	1889:1901	the N-glycans attached to a defined peptide region of its beta-chain	1889:1956	In summary, levels of haptoglobin are enhanced in sera of prostate cancer patients, and the N-glycans attached to a defined peptide region of its beta-chain are characterized by enhanced branching as well as antenna fucosylation.
17803183	12	23	attach	attached	1903:1910	arg1	region					1933:1938	a defined peptide region	1915:1938	a defined peptide region of its beta-chain	1915:1956	In summary, levels of haptoglobin are enhanced in sera of prostate cancer patients, and the N-glycans attached to a defined peptide region of its beta-chain are characterized by enhanced branching as well as antenna fucosylation.
17803183	5	24	theme	acid	846:849	arg1	sequence					859:866	the amino acid 203-215 sequence	836:866	the amino acid 203-215 sequence of the beta-chain of prostate cancer	836:903	(iii) Tri-antennary, N-linked, fucosylated glycans, carrying at least 1 sialyl-Lewis(x/a) antenna, were predominantly located on N207 or N211 within the amino acid 203-215 sequence of the beta-chain of prostate cancer, and were minimal in benign prostate disease.
17803183	8	25	theme	antibody	1398:1405	arg1	RM2					1407:1409	monoclonal antibody RM2	1387:1409	monoclonal antibody RM2	1387:1409	(iv) None of these N-linked structures showed the expected presence of disialylated antennae with GalNAcbeta4(NeuAcalpha3)Galbeta3(NeuAcalpha6)GlcNAcbetaGal, or its analogue, despite cross-reactivity of prostate cancer haptoglobin with monoclonal antibody RM2.
17803183	8	26	theme	disialylated	1222:1233	arg1	antennae					1235:1242	disialylated antennae	1222:1242	disialylated antennae with GalNAcbeta4(NeuAcalpha3)Galbeta3(NeuAcalpha6)GlcNAcbetaGal	1222:1306	(iv) None of these N-linked structures showed the expected presence of disialylated antennae with GalNAcbeta4(NeuAcalpha3)Galbeta3(NeuAcalpha6)GlcNAcbetaGal, or its analogue, despite cross-reactivity of prostate cancer haptoglobin with monoclonal antibody RM2.
17803183	4	27	from	N184	573:576	arg1	bi-antennary					595:606	bi-antennary	595:606	bi-antennary	595:606	The N-linked glycans at N184 were exclusively bi-antennary, and showed no difference between prostate cancer vs. benign prostate disease.
17803183	4	27	from	N184	573:576	arg1	glycans					562:568	The N-linked glycans	549:568	The N-linked glycans at N184	549:576	The N-linked glycans at N184 were exclusively bi-antennary, and showed no difference between prostate cancer vs. benign prostate disease.
17803183	1	28	theme	following	302:310	arg1	results					312:318	the following results	298:318	the following results	298:318	We studied chemical level and glycosylation status of haptoglobin in sera of patients with prostate cancer, as compared to benign prostate disease and normal subjects, with the following results.
17803183	5	29	theme	x/a	772:774	arg1	antenna					777:783	at least 1 sialyl-Lewis(x/a) antenna	748:783	at least 1 sialyl-Lewis(x/a) antenna	748:783	(iii) Tri-antennary, N-linked, fucosylated glycans, carrying at least 1 sialyl-Lewis(x/a) antenna, were predominantly located on N207 or N211 within the amino acid 203-215 sequence of the beta-chain of prostate cancer, and were minimal in benign prostate disease.
17803183	1	30	theme	chemical	136:143	arg1	level					145:149	chemical level	136:149	chemical level	136:149	We studied chemical level and glycosylation status of haptoglobin in sera of patients with prostate cancer, as compared to benign prostate disease and normal subjects, with the following results.
17803183	6	31	located	observed	980:987	arg2	glycans					963:969	Fucosylated glycans	951:969	Fucosylated glycans	951:969	Fucosylated glycans were not observed in normal subjects.
17803183	6	31	located	observed	980:987	arg1	subjects					999:1006	normal subjects	992:1006	normal subjects	992:1006	Fucosylated glycans were not observed in normal subjects.
17803183	4	32	theme	benign	662:667	arg1	disease					678:684	benign prostate disease	662:684	benign prostate disease	662:684	The N-linked glycans at N184 were exclusively bi-antennary, and showed no difference between prostate cancer vs. benign prostate disease.
17803183	7	33	located	observed	1051:1058	arg1	N241					1063:1066	N241	1063:1066	N241	1063:1066	A minor tri-antennary N-linked glycan was observed at N241 of the beta-chain in prostate cancer, which was absent in benign prostate disease.
17803183	7	33	located	observed	1051:1058	arg2	glycan					1040:1045	A minor tri-antennary N-linked glycan	1009:1045	A minor tri-antennary N-linked glycan	1009:1045	A minor tri-antennary N-linked glycan was observed at N241 of the beta-chain in prostate cancer, which was absent in benign prostate disease.
17803183	7	34	theme	prostate	1133:1140	arg1	disease					1142:1148	benign prostate disease	1126:1148	benign prostate disease	1126:1148	A minor tri-antennary N-linked glycan was observed at N241 of the beta-chain in prostate cancer, which was absent in benign prostate disease.
17803183	5	35	contain	carrying	739:746	arg2	antenna					777:783	at least 1 sialyl-Lewis(x/a) antenna	748:783	at least 1 sialyl-Lewis(x/a) antenna	748:783	(iii) Tri-antennary, N-linked, fucosylated glycans, carrying at least 1 sialyl-Lewis(x/a) antenna, were predominantly located on N207 or N211 within the amino acid 203-215 sequence of the beta-chain of prostate cancer, and were minimal in benign prostate disease.
17803183	5	35	contain	carrying	739:746	arg1	glycans					730:736	(iii) Tri-antennary, N-linked, fucosylated glycans	687:736	glycans	730:736	(iii) Tri-antennary, N-linked, fucosylated glycans, carrying at least 1 sialyl-Lewis(x/a) antenna, were predominantly located on N207 or N211 within the amino acid 203-215 sequence of the beta-chain of prostate cancer, and were minimal in benign prostate disease.
17803183	11	36	attach	linked	1771:1776	arg1	core					1795:1798	this O-glycan core	1781:1798	this O-glycan core	1781:1798	No evidence was found for the presence of specific RM2 or other tumor-associated glycosyl epitopes linked to this O-glycan core.
17803183	11	36	attach	linked	1771:1776	arg2	RM2					1723:1725	specific RM2	1714:1725	specific RM2	1714:1725	No evidence was found for the presence of specific RM2 or other tumor-associated glycosyl epitopes linked to this O-glycan core.
17803183	9	37	theme	O-glycosylation	1432:1446	arg1	levels					1422:1427	Minor levels	1416:1427	Minor levels of O-glycosylation	1416:1446	(v) Minor levels of O-glycosylation were identified in prostate cancer haptoglobin for the first time.
17803183	7	38	from	beta-chain	1075:1084	arg1	cancer					1098:1103	prostate cancer	1089:1103	prostate cancer	1089:1103	A minor tri-antennary N-linked glycan was observed at N241 of the beta-chain in prostate cancer, which was absent in benign prostate disease.
17803183	0	39	theme	benign	81:86	arg1	disease					97:103	benign prostate disease	81:103	benign prostate disease	81:103	Glycosylation status of haptoglobin in sera of patients with prostate cancer vs. benign prostate disease or normal subjects.
17803183	5	40	theme	cancer	898:903	arg1	beta-chain					875:884	the beta-chain	871:884	the beta-chain of prostate cancer	871:903	(iii) Tri-antennary, N-linked, fucosylated glycans, carrying at least 1 sialyl-Lewis(x/a) antenna, were predominantly located on N207 or N211 within the amino acid 203-215 sequence of the beta-chain of prostate cancer, and were minimal in benign prostate disease.
17803183	9	41	dep	identified	1453:1462	arg1	v					1413:1413	v	1413:1413	v	1413:1413	(v) Minor levels of O-glycosylation were identified in prostate cancer haptoglobin for the first time.
17803183	10	42	theme	reductive	1588:1596	arg1	beta-elimination					1598:1613	reductive beta-elimination	1588:1613	reductive beta-elimination followed by methylation and mass spectrometric analysis	1588:1669	Mono- and disialyl core Type 1 O-linked structures were identified after reductive beta-elimination followed by methylation and mass spectrometric analysis.
17803183	2	43	dep	level	337:341	arg1	i					322:322	i	322:322	i	322:322	(i) Haptoglobin level was enhanced significantly in sera of prostate cancer.
17803183	9	44	theme	prostate	1467:1474	arg1	haptoglobin					1483:1493	prostate cancer haptoglobin	1467:1493	prostate cancer haptoglobin	1467:1493	(v) Minor levels of O-glycosylation were identified in prostate cancer haptoglobin for the first time.
17803183	0	45	theme	prostate	61:68	arg1	cancer					70:75	prostate cancer	61:75	prostate cancer	61:75	Glycosylation status of haptoglobin in sera of patients with prostate cancer vs. benign prostate disease or normal subjects.
17803183	10	46	theme	O-linked	1546:1553	arg1	structures					1555:1564	Mono- and disialyl core Type 1 O-linked structures	1515:1564	Mono- and disialyl core Type 1 O-linked structures	1515:1564	Mono- and disialyl core Type 1 O-linked structures were identified after reductive beta-elimination followed by methylation and mass spectrometric analysis.
17803183	0	47	theme	Glycosylation	0:12	arg1	status					14:19	Glycosylation status	0:19	Glycosylation status of haptoglobin in sera of patients with prostate cancer vs. benign prostate disease or normal subjects.	0:123	Glycosylation status of haptoglobin in sera of patients with prostate cancer vs. benign prostate disease or normal subjects.
17803183	1	48	theme	prostate	255:262	arg1	disease					264:270	benign prostate disease	248:270	benign prostate disease	248:270	We studied chemical level and glycosylation status of haptoglobin in sera of patients with prostate cancer, as compared to benign prostate disease and normal subjects, with the following results.
17803183	12	49	theme	haptoglobin	1823:1833	arg1	levels					1813:1818	levels	1813:1818	levels of haptoglobin	1813:1833	In summary, levels of haptoglobin are enhanced in sera of prostate cancer patients, and the N-glycans attached to a defined peptide region of its beta-chain are characterized by enhanced branching as well as antenna fucosylation.
17803183	9	50	theme	first	1503:1507	arg1	time					1509:1512	the first time	1499:1512	the first time	1499:1512	(v) Minor levels of O-glycosylation were identified in prostate cancer haptoglobin for the first time.
17803183	2	51	theme	cancer	390:395	arg1	sera					373:376	sera	373:376	sera of prostate cancer	373:395	(i) Haptoglobin level was enhanced significantly in sera of prostate cancer.
17803183	7	52	theme	prostate	1089:1096	arg1	cancer					1098:1103	prostate cancer	1089:1103	prostate cancer	1089:1103	A minor tri-antennary N-linked glycan was observed at N241 of the beta-chain in prostate cancer, which was absent in benign prostate disease.
17803183	1	53	with	patients	202:209	arg1	cancer					225:230	prostate cancer	216:230	prostate cancer	216:230	We studied chemical level and glycosylation status of haptoglobin in sera of patients with prostate cancer, as compared to benign prostate disease and normal subjects, with the following results.
17803183	3	54	theme	Sialylated	403:412	arg1	structures					453:462	the dominant structures	440:462	the dominant structures in haptoglobins from all 3 sources	440:497	(ii) Sialylated bi-antennary glycans were the dominant structures in haptoglobins from all 3 sources, regardless of different site of N-linked glycan.
17803183	3	54	theme	Sialylated	403:412	arg1	glycans					427:433	Sialylated bi-antennary glycans	403:433	Sialylated bi-antennary glycans	403:433	(ii) Sialylated bi-antennary glycans were the dominant structures in haptoglobins from all 3 sources, regardless of different site of N-linked glycan.
17803183	7	55	theme	beta-chain	1075:1084	arg1	N241					1063:1066	N241	1063:1066	N241	1063:1066	A minor tri-antennary N-linked glycan was observed at N241 of the beta-chain in prostate cancer, which was absent in benign prostate disease.
17803183	11	56	theme	O-glycan	1786:1793	arg1	core					1795:1798	this O-glycan core	1781:1798	this O-glycan core	1781:1798	No evidence was found for the presence of specific RM2 or other tumor-associated glycosyl epitopes linked to this O-glycan core.
17803183	4	57	link	N-linked	553:560	arg1	bi-antennary					595:606	bi-antennary	595:606	bi-antennary	595:606	The N-linked glycans at N184 were exclusively bi-antennary, and showed no difference between prostate cancer vs. benign prostate disease.
17803183	4	57	link	N-linked	553:560	arg1	glycans					562:568	The N-linked glycans	549:568	The N-linked glycans at N184	549:576	The N-linked glycans at N184 were exclusively bi-antennary, and showed no difference between prostate cancer vs. benign prostate disease.
17803183	8	58	with	antennae	1235:1242	arg1	GlcNAcbetaGal					1294:1306	GalNAcbeta4(NeuAcalpha3)Galbeta3(NeuAcalpha6)GlcNAcbetaGal	1249:1306	GalNAcbeta4(NeuAcalpha3)Galbeta3(NeuAcalpha6)GlcNAcbetaGal	1249:1306	(iv) None of these N-linked structures showed the expected presence of disialylated antennae with GalNAcbeta4(NeuAcalpha3)Galbeta3(NeuAcalpha6)GlcNAcbetaGal, or its analogue, despite cross-reactivity of prostate cancer haptoglobin with monoclonal antibody RM2.
17803183	5	59	theme	benign	926:931	arg1	disease					942:948	benign prostate disease	926:948	benign prostate disease	926:948	(iii) Tri-antennary, N-linked, fucosylated glycans, carrying at least 1 sialyl-Lewis(x/a) antenna, were predominantly located on N207 or N211 within the amino acid 203-215 sequence of the beta-chain of prostate cancer, and were minimal in benign prostate disease.
17803183	7	60	theme	benign	1126:1131	arg1	disease					1142:1148	benign prostate disease	1126:1148	benign prostate disease	1126:1148	A minor tri-antennary N-linked glycan was observed at N241 of the beta-chain in prostate cancer, which was absent in benign prostate disease.
17803183	10	61	theme	spectrometric	1648:1660	arg1	analysis					1662:1669	mass spectrometric analysis	1643:1669	mass spectrometric analysis	1643:1669	Mono- and disialyl core Type 1 O-linked structures were identified after reductive beta-elimination followed by methylation and mass spectrometric analysis.
17803183	12	62	theme	enhanced	1979:1986	arg1	branching					1988:1996	enhanced branching	1979:1996	enhanced branching as well as antenna fucosylation	1979:2028	In summary, levels of haptoglobin are enhanced in sera of prostate cancer patients, and the N-glycans attached to a defined peptide region of its beta-chain are characterized by enhanced branching as well as antenna fucosylation.
17803183	7	63	theme	tri-antennary	1017:1029	arg1	glycan					1040:1045	A minor tri-antennary N-linked glycan	1009:1045	A minor tri-antennary N-linked glycan	1009:1045	A minor tri-antennary N-linked glycan was observed at N241 of the beta-chain in prostate cancer, which was absent in benign prostate disease.
17803183	1	64	theme	glycosylation	155:167	arg1	status					169:174	glycosylation status	155:174	glycosylation status of haptoglobin	155:189	We studied chemical level and glycosylation status of haptoglobin in sera of patients with prostate cancer, as compared to benign prostate disease and normal subjects, with the following results.
17803183	12	65	theme	defined	1917:1923	arg1	region					1933:1938	a defined peptide region	1915:1938	a defined peptide region of its beta-chain	1915:1956	In summary, levels of haptoglobin are enhanced in sera of prostate cancer patients, and the N-glycans attached to a defined peptide region of its beta-chain are characterized by enhanced branching as well as antenna fucosylation.
17803183	10	66	theme	Mono-	1515:1519	arg1	structures					1555:1564	Mono- and disialyl core Type 1 O-linked structures	1515:1564	Mono- and disialyl core Type 1 O-linked structures	1515:1564	Mono- and disialyl core Type 1 O-linked structures were identified after reductive beta-elimination followed by methylation and mass spectrometric analysis.
17803183	5	67	from	minimal	915:921	arg1	disease					942:948	benign prostate disease	926:948	benign prostate disease	926:948	(iii) Tri-antennary, N-linked, fucosylated glycans, carrying at least 1 sialyl-Lewis(x/a) antenna, were predominantly located on N207 or N211 within the amino acid 203-215 sequence of the beta-chain of prostate cancer, and were minimal in benign prostate disease.
17803183	11	68	theme	other	1730:1734	arg1	epitopes					1762:1769	other tumor-associated glycosyl epitopes	1730:1769	other tumor-associated glycosyl epitopes	1730:1769	No evidence was found for the presence of specific RM2 or other tumor-associated glycosyl epitopes linked to this O-glycan core.
17803183	0	69	theme	subjects	115:122	arg1	sera					39:42	sera	39:42	sera of patients with prostate cancer vs. benign prostate disease or normal subjects	39:122	Glycosylation status of haptoglobin in sera of patients with prostate cancer vs. benign prostate disease or normal subjects.
17803183	3	70	theme	different	514:522	arg1	site					524:527	different site	514:527	different site of N-linked glycan	514:546	(ii) Sialylated bi-antennary glycans were the dominant structures in haptoglobins from all 3 sources, regardless of different site of N-linked glycan.
17803183	3	70	theme	different	514:522	arg1	glycan					541:546	N-linked glycan	532:546	N-linked glycan	532:546	(ii) Sialylated bi-antennary glycans were the dominant structures in haptoglobins from all 3 sources, regardless of different site of N-linked glycan.
17803183	5	71	dep	glycans	730:736	arg1	iii					688:690	iii	688:690	iii	688:690	(iii) Tri-antennary, N-linked, fucosylated glycans, carrying at least 1 sialyl-Lewis(x/a) antenna, were predominantly located on N207 or N211 within the amino acid 203-215 sequence of the beta-chain of prostate cancer, and were minimal in benign prostate disease.
17803183	8	72	theme	prostate	1354:1361	arg1	haptoglobin					1370:1380	prostate cancer haptoglobin	1354:1380	prostate cancer haptoglobin	1354:1380	(iv) None of these N-linked structures showed the expected presence of disialylated antennae with GalNAcbeta4(NeuAcalpha3)Galbeta3(NeuAcalpha6)GlcNAcbetaGal, or its analogue, despite cross-reactivity of prostate cancer haptoglobin with monoclonal antibody RM2.
17803183	12	73	theme	antenna	2009:2015	arg1	fucosylation					2017:2028	antenna fucosylation	2009:2028	enhanced branching as well as antenna fucosylation	1979:2028	In summary, levels of haptoglobin are enhanced in sera of prostate cancer patients, and the N-glycans attached to a defined peptide region of its beta-chain are characterized by enhanced branching as well as antenna fucosylation.
17803183	10	74	theme	Type	1539:1542	arg1	structures					1555:1564	Mono- and disialyl core Type 1 O-linked structures	1515:1564	Mono- and disialyl core Type 1 O-linked structures	1515:1564	Mono- and disialyl core Type 1 O-linked structures were identified after reductive beta-elimination followed by methylation and mass spectrometric analysis.
17803183	11	75	theme	RM2	1723:1725	arg1	presence					1702:1709	the presence	1698:1709	the presence of specific RM2 or other tumor-associated glycosyl epitopes linked to this O-glycan core	1698:1798	No evidence was found for the presence of specific RM2 or other tumor-associated glycosyl epitopes linked to this O-glycan core.
17803183	5	76	from	disease	942:948	arg1	minimal					915:921	minimal	915:921	minimal	915:921	(iii) Tri-antennary, N-linked, fucosylated glycans, carrying at least 1 sialyl-Lewis(x/a) antenna, were predominantly located on N207 or N211 within the amino acid 203-215 sequence of the beta-chain of prostate cancer, and were minimal in benign prostate disease.
17803183	12	77	theme	prostate	1859:1866	arg1	patients					1875:1882	prostate cancer patients	1859:1882	prostate cancer patients	1859:1882	In summary, levels of haptoglobin are enhanced in sera of prostate cancer patients, and the N-glycans attached to a defined peptide region of its beta-chain are characterized by enhanced branching as well as antenna fucosylation.
17803183	7	78	from	absent	1116:1121	arg1	disease					1142:1148	benign prostate disease	1126:1148	benign prostate disease	1126:1148	A minor tri-antennary N-linked glycan was observed at N241 of the beta-chain in prostate cancer, which was absent in benign prostate disease.
17803183	8	79	theme	N-linked	1170:1177	arg1	structures					1179:1188	these N-linked structures	1164:1188	these N-linked structures	1164:1188	(iv) None of these N-linked structures showed the expected presence of disialylated antennae with GalNAcbeta4(NeuAcalpha3)Galbeta3(NeuAcalpha6)GlcNAcbetaGal, or its analogue, despite cross-reactivity of prostate cancer haptoglobin with monoclonal antibody RM2.
17803183	10	80	theme	disialyl	1525:1532	arg1	structures					1555:1564	Mono- and disialyl core Type 1 O-linked structures	1515:1564	Mono- and disialyl core Type 1 O-linked structures	1515:1564	Mono- and disialyl core Type 1 O-linked structures were identified after reductive beta-elimination followed by methylation and mass spectrometric analysis.
17803183	3	81	theme	glycan	541:546	arg1	site					524:527	different site	514:527	different site of N-linked glycan	514:546	(ii) Sialylated bi-antennary glycans were the dominant structures in haptoglobins from all 3 sources, regardless of different site of N-linked glycan.
17803183	3	81	theme	glycan	541:546	arg1	glycan					541:546	N-linked glycan	532:546	N-linked glycan	532:546	(ii) Sialylated bi-antennary glycans were the dominant structures in haptoglobins from all 3 sources, regardless of different site of N-linked glycan.
17803183	5	82	theme	amino	840:844	arg1	sequence					859:866	the amino acid 203-215 sequence	836:866	the amino acid 203-215 sequence of the beta-chain of prostate cancer	836:903	(iii) Tri-antennary, N-linked, fucosylated glycans, carrying at least 1 sialyl-Lewis(x/a) antenna, were predominantly located on N207 or N211 within the amino acid 203-215 sequence of the beta-chain of prostate cancer, and were minimal in benign prostate disease.
17803183	12	83	theme	patients	1875:1882	arg1	sera					1851:1854	sera	1851:1854	sera of prostate cancer patients	1851:1882	In summary, levels of haptoglobin are enhanced in sera of prostate cancer patients, and the N-glycans attached to a defined peptide region of its beta-chain are characterized by enhanced branching as well as antenna fucosylation.
17803183	8	84	theme	monoclonal	1387:1396	arg1	antibody					1398:1405	monoclonal antibody	1387:1405	monoclonal antibody RM2	1387:1409	(iv) None of these N-linked structures showed the expected presence of disialylated antennae with GalNAcbeta4(NeuAcalpha3)Galbeta3(NeuAcalpha6)GlcNAcbetaGal, or its analogue, despite cross-reactivity of prostate cancer haptoglobin with monoclonal antibody RM2.
17803183	4	85	theme	prostate	669:676	arg1	disease					678:684	benign prostate disease	662:684	benign prostate disease	662:684	The N-linked glycans at N184 were exclusively bi-antennary, and showed no difference between prostate cancer vs. benign prostate disease.
17803183	11	86	theme	glycosyl	1753:1760	arg1	epitopes					1762:1769	other tumor-associated glycosyl epitopes	1730:1769	other tumor-associated glycosyl epitopes	1730:1769	No evidence was found for the presence of specific RM2 or other tumor-associated glycosyl epitopes linked to this O-glycan core.
17803183	5	87	theme	203-215	851:857	arg1	sequence					859:866	the amino acid 203-215 sequence	836:866	the amino acid 203-215 sequence of the beta-chain of prostate cancer	836:903	(iii) Tri-antennary, N-linked, fucosylated glycans, carrying at least 1 sialyl-Lewis(x/a) antenna, were predominantly located on N207 or N211 within the amino acid 203-215 sequence of the beta-chain of prostate cancer, and were minimal in benign prostate disease.
17803183	5	88	link	N-linked	708:715	arg1	glycans					730:736	(iii) Tri-antennary, N-linked, fucosylated glycans	687:736	glycans	730:736	(iii) Tri-antennary, N-linked, fucosylated glycans, carrying at least 1 sialyl-Lewis(x/a) antenna, were predominantly located on N207 or N211 within the amino acid 203-215 sequence of the beta-chain of prostate cancer, and were minimal in benign prostate disease.
17803183	6	89	theme	Fucosylated	951:961	arg1	glycans					963:969	Fucosylated glycans	951:969	Fucosylated glycans	951:969	Fucosylated glycans were not observed in normal subjects.
17803183	7	90	from	disease	1142:1148	arg1	absent					1116:1121	absent	1116:1121	absent	1116:1121	A minor tri-antennary N-linked glycan was observed at N241 of the beta-chain in prostate cancer, which was absent in benign prostate disease.
17803183	8	91	theme	expected	1201:1208	arg1	presence					1210:1217	the expected presence	1197:1217	the expected presence of disialylated antennae with GalNAcbeta4(NeuAcalpha3)Galbeta3(NeuAcalpha6)GlcNAcbetaGal	1197:1306	(iv) None of these N-linked structures showed the expected presence of disialylated antennae with GalNAcbeta4(NeuAcalpha3)Galbeta3(NeuAcalpha6)GlcNAcbetaGal, or its analogue, despite cross-reactivity of prostate cancer haptoglobin with monoclonal antibody RM2.
17803183	0	92	with	subjects	115:122	arg1	cancer					70:75	prostate cancer	61:75	prostate cancer	61:75	Glycosylation status of haptoglobin in sera of patients with prostate cancer vs. benign prostate disease or normal subjects.
17803183	0	92	with	subjects	115:122	arg1	disease					97:103	benign prostate disease	81:103	benign prostate disease	81:103	Glycosylation status of haptoglobin in sera of patients with prostate cancer vs. benign prostate disease or normal subjects.
17803183	5	93	theme	N-linked	708:715	arg1	glycans					730:736	(iii) Tri-antennary, N-linked, fucosylated glycans	687:736	glycans	730:736	(iii) Tri-antennary, N-linked, fucosylated glycans, carrying at least 1 sialyl-Lewis(x/a) antenna, were predominantly located on N207 or N211 within the amino acid 203-215 sequence of the beta-chain of prostate cancer, and were minimal in benign prostate disease.
17803183	9	94	theme	Minor	1416:1420	arg1	levels					1422:1427	Minor levels	1416:1427	Minor levels of O-glycosylation	1416:1446	(v) Minor levels of O-glycosylation were identified in prostate cancer haptoglobin for the first time.
17803183	7	95	from	N241	1063:1066	arg1	cancer					1098:1103	prostate cancer	1089:1103	prostate cancer	1089:1103	A minor tri-antennary N-linked glycan was observed at N241 of the beta-chain in prostate cancer, which was absent in benign prostate disease.
17803183	4	96	theme	prostate	642:649	arg1	cancer					651:656	prostate cancer	642:656	prostate cancer	642:656	The N-linked glycans at N184 were exclusively bi-antennary, and showed no difference between prostate cancer vs. benign prostate disease.
17803183	3	97	from	sources	491:497	arg1	structures					453:462	the dominant structures	440:462	the dominant structures in haptoglobins from all 3 sources	440:497	(ii) Sialylated bi-antennary glycans were the dominant structures in haptoglobins from all 3 sources, regardless of different site of N-linked glycan.
17803183	3	97	from	sources	491:497	arg1	glycans					427:433	Sialylated bi-antennary glycans	403:433	Sialylated bi-antennary glycans	403:433	(ii) Sialylated bi-antennary glycans were the dominant structures in haptoglobins from all 3 sources, regardless of different site of N-linked glycan.
17803183	3	97	from	sources	491:497	arg1	haptoglobins					467:478	haptoglobins	467:478	haptoglobins from all 3 sources	467:497	(ii) Sialylated bi-antennary glycans were the dominant structures in haptoglobins from all 3 sources, regardless of different site of N-linked glycan.
17803183	5	98	theme	fucosylated	718:728	arg1	glycans					730:736	(iii) Tri-antennary, N-linked, fucosylated glycans	687:736	glycans	730:736	(iii) Tri-antennary, N-linked, fucosylated glycans, carrying at least 1 sialyl-Lewis(x/a) antenna, were predominantly located on N207 or N211 within the amino acid 203-215 sequence of the beta-chain of prostate cancer, and were minimal in benign prostate disease.
17803183	3	99	link	N-linked	532:539	arg1	glycan					541:546	N-linked glycan	532:546	N-linked glycan	532:546	(ii) Sialylated bi-antennary glycans were the dominant structures in haptoglobins from all 3 sources, regardless of different site of N-linked glycan.
17803183	0	100	from	status	14:19	arg1	sera					39:42	sera	39:42	sera of patients with prostate cancer vs. benign prostate disease or normal subjects	39:122	Glycosylation status of haptoglobin in sera of patients with prostate cancer vs. benign prostate disease or normal subjects.
17803183	8	101	theme	antennae	1235:1242	arg1	presence					1210:1217	the expected presence	1197:1217	the expected presence of disialylated antennae with GalNAcbeta4(NeuAcalpha3)Galbeta3(NeuAcalpha6)GlcNAcbetaGal	1197:1306	(iv) None of these N-linked structures showed the expected presence of disialylated antennae with GalNAcbeta4(NeuAcalpha3)Galbeta3(NeuAcalpha6)GlcNAcbetaGal, or its analogue, despite cross-reactivity of prostate cancer haptoglobin with monoclonal antibody RM2.
17803183	8	101	theme	antennae	1235:1242	arg1	analogue					1316:1323	its analogue	1312:1323	its analogue	1312:1323	(iv) None of these N-linked structures showed the expected presence of disialylated antennae with GalNAcbeta4(NeuAcalpha3)Galbeta3(NeuAcalpha6)GlcNAcbetaGal, or its analogue, despite cross-reactivity of prostate cancer haptoglobin with monoclonal antibody RM2.
17803183	0	102	theme	prostate	88:95	arg1	disease					97:103	benign prostate disease	81:103	benign prostate disease	81:103	Glycosylation status of haptoglobin in sera of patients with prostate cancer vs. benign prostate disease or normal subjects.
17803183	5	103	theme	prostate	889:896	arg1	cancer					898:903	prostate cancer	889:903	prostate cancer	889:903	(iii) Tri-antennary, N-linked, fucosylated glycans, carrying at least 1 sialyl-Lewis(x/a) antenna, were predominantly located on N207 or N211 within the amino acid 203-215 sequence of the beta-chain of prostate cancer, and were minimal in benign prostate disease.
17803183	8	104	theme	GalNAcbeta4	1249:1259	arg1	GlcNAcbetaGal					1294:1306	GalNAcbeta4(NeuAcalpha3)Galbeta3(NeuAcalpha6)GlcNAcbetaGal	1249:1306	GalNAcbeta4(NeuAcalpha3)Galbeta3(NeuAcalpha6)GlcNAcbetaGal	1249:1306	(iv) None of these N-linked structures showed the expected presence of disialylated antennae with GalNAcbeta4(NeuAcalpha3)Galbeta3(NeuAcalpha6)GlcNAcbetaGal, or its analogue, despite cross-reactivity of prostate cancer haptoglobin with monoclonal antibody RM2.
17803183	5	105	theme	Tri-antennary	693:705	arg1	glycans					730:736	(iii) Tri-antennary, N-linked, fucosylated glycans	687:736	glycans	730:736	(iii) Tri-antennary, N-linked, fucosylated glycans, carrying at least 1 sialyl-Lewis(x/a) antenna, were predominantly located on N207 or N211 within the amino acid 203-215 sequence of the beta-chain of prostate cancer, and were minimal in benign prostate disease.
17803183	8	106	gly	disialylated	1222:1233	arg1	antennae					1235:1242	disialylated antennae	1222:1242	disialylated antennae with GalNAcbeta4(NeuAcalpha3)Galbeta3(NeuAcalpha6)GlcNAcbetaGal	1222:1306	(iv) None of these N-linked structures showed the expected presence of disialylated antennae with GalNAcbeta4(NeuAcalpha3)Galbeta3(NeuAcalpha6)GlcNAcbetaGal, or its analogue, despite cross-reactivity of prostate cancer haptoglobin with monoclonal antibody RM2.
17803183	3	107	dep	structures	453:462	arg1	ii					399:400	ii	399:400	ii	399:400	(ii) Sialylated bi-antennary glycans were the dominant structures in haptoglobins from all 3 sources, regardless of different site of N-linked glycan.
17803183	7	108	from	cancer	1098:1103	arg1	N241					1063:1066	N241	1063:1066	N241	1063:1066	A minor tri-antennary N-linked glycan was observed at N241 of the beta-chain in prostate cancer, which was absent in benign prostate disease.
17803183	8	109	theme	NeuAcalpha3	1261:1271	arg1	GlcNAcbetaGal					1294:1306	GalNAcbeta4(NeuAcalpha3)Galbeta3(NeuAcalpha6)GlcNAcbetaGal	1249:1306	GalNAcbeta4(NeuAcalpha3)Galbeta3(NeuAcalpha6)GlcNAcbetaGal	1249:1306	(iv) None of these N-linked structures showed the expected presence of disialylated antennae with GalNAcbeta4(NeuAcalpha3)Galbeta3(NeuAcalpha6)GlcNAcbetaGal, or its analogue, despite cross-reactivity of prostate cancer haptoglobin with monoclonal antibody RM2.
17803183	8	110	dep	None	1156:1159	arg1	iv					1152:1153	iv	1152:1153	iv	1152:1153	(iv) None of these N-linked structures showed the expected presence of disialylated antennae with GalNAcbeta4(NeuAcalpha3)Galbeta3(NeuAcalpha6)GlcNAcbetaGal, or its analogue, despite cross-reactivity of prostate cancer haptoglobin with monoclonal antibody RM2.
17803183	6	111	theme	normal	992:997	arg1	subjects					999:1006	normal subjects	992:1006	normal subjects	992:1006	Fucosylated glycans were not observed in normal subjects.
17803183	8	112	theme	Galbeta3	1273:1280	arg1	GlcNAcbetaGal					1294:1306	GalNAcbeta4(NeuAcalpha3)Galbeta3(NeuAcalpha6)GlcNAcbetaGal	1249:1306	GalNAcbeta4(NeuAcalpha3)Galbeta3(NeuAcalpha6)GlcNAcbetaGal	1249:1306	(iv) None of these N-linked structures showed the expected presence of disialylated antennae with GalNAcbeta4(NeuAcalpha3)Galbeta3(NeuAcalpha6)GlcNAcbetaGal, or its analogue, despite cross-reactivity of prostate cancer haptoglobin with monoclonal antibody RM2.
17803183	7	113	link	N-linked	1031:1038	arg1	glycan					1040:1045	A minor tri-antennary N-linked glycan	1009:1045	A minor tri-antennary N-linked glycan	1009:1045	A minor tri-antennary N-linked glycan was observed at N241 of the beta-chain in prostate cancer, which was absent in benign prostate disease.
17803183	0	114	theme	haptoglobin	24:34	arg1	status					14:19	Glycosylation status	0:19	Glycosylation status of haptoglobin in sera of patients with prostate cancer vs. benign prostate disease or normal subjects.	0:123	Glycosylation status of haptoglobin in sera of patients with prostate cancer vs. benign prostate disease or normal subjects.
17803183	5	115	theme	beta-chain	875:884	arg1	sequence					859:866	the amino acid 203-215 sequence	836:866	the amino acid 203-215 sequence of the beta-chain of prostate cancer	836:903	(iii) Tri-antennary, N-linked, fucosylated glycans, carrying at least 1 sialyl-Lewis(x/a) antenna, were predominantly located on N207 or N211 within the amino acid 203-215 sequence of the beta-chain of prostate cancer, and were minimal in benign prostate disease.
17803183	10	116	link	O-linked	1546:1553	arg1	structures					1555:1564	Mono- and disialyl core Type 1 O-linked structures	1515:1564	Mono- and disialyl core Type 1 O-linked structures	1515:1564	Mono- and disialyl core Type 1 O-linked structures were identified after reductive beta-elimination followed by methylation and mass spectrometric analysis.
17803183	8	117	theme	NeuAcalpha6	1282:1292	arg1	GlcNAcbetaGal					1294:1306	GalNAcbeta4(NeuAcalpha3)Galbeta3(NeuAcalpha6)GlcNAcbetaGal	1249:1306	GalNAcbeta4(NeuAcalpha3)Galbeta3(NeuAcalpha6)GlcNAcbetaGal	1249:1306	(iv) None of these N-linked structures showed the expected presence of disialylated antennae with GalNAcbeta4(NeuAcalpha3)Galbeta3(NeuAcalpha6)GlcNAcbetaGal, or its analogue, despite cross-reactivity of prostate cancer haptoglobin with monoclonal antibody RM2.
17803183	2	118	theme	prostate	381:388	arg1	cancer					390:395	prostate cancer	381:395	prostate cancer	381:395	(i) Haptoglobin level was enhanced significantly in sera of prostate cancer.
17803183	1	119	theme	normal	276:281	arg1	subjects					283:290	normal subjects	276:290	normal subjects	276:290	We studied chemical level and glycosylation status of haptoglobin in sera of patients with prostate cancer, as compared to benign prostate disease and normal subjects, with the following results.
17803183	5	120	theme	prostate	933:940	arg1	disease					942:948	benign prostate disease	926:948	benign prostate disease	926:948	(iii) Tri-antennary, N-linked, fucosylated glycans, carrying at least 1 sialyl-Lewis(x/a) antenna, were predominantly located on N207 or N211 within the amino acid 203-215 sequence of the beta-chain of prostate cancer, and were minimal in benign prostate disease.
17803183	3	121	theme	bi-antennary	414:425	arg1	structures					453:462	the dominant structures	440:462	the dominant structures in haptoglobins from all 3 sources	440:497	(ii) Sialylated bi-antennary glycans were the dominant structures in haptoglobins from all 3 sources, regardless of different site of N-linked glycan.
17803183	3	121	theme	bi-antennary	414:425	arg1	glycans					427:433	Sialylated bi-antennary glycans	403:433	Sialylated bi-antennary glycans	403:433	(ii) Sialylated bi-antennary glycans were the dominant structures in haptoglobins from all 3 sources, regardless of different site of N-linked glycan.
17803183	0	122	theme	patients	47:54	arg1	sera					39:42	sera	39:42	sera of patients with prostate cancer vs. benign prostate disease or normal subjects	39:122	Glycosylation status of haptoglobin in sera of patients with prostate cancer vs. benign prostate disease or normal subjects.
17803183	11	123	theme	epitopes	1762:1769	arg1	presence					1702:1709	the presence	1698:1709	the presence of specific RM2 or other tumor-associated glycosyl epitopes linked to this O-glycan core	1698:1798	No evidence was found for the presence of specific RM2 or other tumor-associated glycosyl epitopes linked to this O-glycan core.
17803183	8	124	theme	haptoglobin	1370:1380	arg1	cross-reactivity					1334:1349	cross-reactivity	1334:1349	cross-reactivity of prostate cancer haptoglobin with monoclonal antibody RM2	1334:1409	(iv) None of these N-linked structures showed the expected presence of disialylated antennae with GalNAcbeta4(NeuAcalpha3)Galbeta3(NeuAcalpha6)GlcNAcbetaGal, or its analogue, despite cross-reactivity of prostate cancer haptoglobin with monoclonal antibody RM2.
17803183	8	125	link	N-linked	1170:1177	arg1	structures					1179:1188	these N-linked structures	1164:1188	these N-linked structures	1164:1188	(iv) None of these N-linked structures showed the expected presence of disialylated antennae with GalNAcbeta4(NeuAcalpha3)Galbeta3(NeuAcalpha6)GlcNAcbetaGal, or its analogue, despite cross-reactivity of prostate cancer haptoglobin with monoclonal antibody RM2.
17803183	5	126	gly	fucosylated	718:728	arg1	glycans					730:736	(iii) Tri-antennary, N-linked, fucosylated glycans	687:736	glycans	730:736	(iii) Tri-antennary, N-linked, fucosylated glycans, carrying at least 1 sialyl-Lewis(x/a) antenna, were predominantly located on N207 or N211 within the amino acid 203-215 sequence of the beta-chain of prostate cancer, and were minimal in benign prostate disease.
17803183	0	127	with	patients	47:54	arg1	cancer					70:75	prostate cancer	61:75	prostate cancer	61:75	Glycosylation status of haptoglobin in sera of patients with prostate cancer vs. benign prostate disease or normal subjects.
17803183	0	127	with	patients	47:54	arg1	disease					97:103	benign prostate disease	81:103	benign prostate disease	81:103	Glycosylation status of haptoglobin in sera of patients with prostate cancer vs. benign prostate disease or normal subjects.
17803183	3	128	theme	dominant	444:451	arg1	structures					453:462	the dominant structures	440:462	the dominant structures in haptoglobins from all 3 sources	440:497	(ii) Sialylated bi-antennary glycans were the dominant structures in haptoglobins from all 3 sources, regardless of different site of N-linked glycan.
17803183	3	128	theme	dominant	444:451	arg1	glycans					427:433	Sialylated bi-antennary glycans	403:433	Sialylated bi-antennary glycans	403:433	(ii) Sialylated bi-antennary glycans were the dominant structures in haptoglobins from all 3 sources, regardless of different site of N-linked glycan.
17803183	1	129	theme	prostate	216:223	arg1	cancer					225:230	prostate cancer	216:230	prostate cancer	216:230	We studied chemical level and glycosylation status of haptoglobin in sera of patients with prostate cancer, as compared to benign prostate disease and normal subjects, with the following results.
17803183	2	130	theme	Haptoglobin	325:335	arg1	level					337:341	(i) Haptoglobin level	321:341	(i) Haptoglobin level	321:341	(i) Haptoglobin level was enhanced significantly in sera of prostate cancer.
28474680	1	0	gly	O-GlcNAcylation	90:104	arg1	tumorigenesis					133:145	the tumorigenesis	129:145	the tumorigenesis of various tissue origins	129:171	O-GlcNAcylation has been implicated in the tumorigenesis of various tissue origins, but its function in liver tumorigenesis is not clear.
28474680	0	1	from	role	14:17	arg1	tumorigenesis					75:87	high-glucose-stimulated liver tumorigenesis	45:87	high-glucose-stimulated liver tumorigenesis	45:87	The essential role of YAP O-GlcNAcylation in high-glucose-stimulated liver tumorigenesis.
28474680	7	2	theme	glucose	1161:1167	arg1	levels					1169:1174	high blood glucose levels	1150:1174	high blood glucose levels	1150:1174	We conclude that YAP O-GlcNAcylation is a potential therapeutic intervention point for treating liver cancer associated with high blood glucose levels and possibly diabetes.
28474680	1	3	from	function	182:189	arg1	tumorigenesis					200:212	liver tumorigenesis	194:212	liver tumorigenesis	194:212	O-GlcNAcylation has been implicated in the tumorigenesis of various tissue origins, but its function in liver tumorigenesis is not clear.
28474680	3	4	theme	liver	516:520	arg1	cells					529:533	liver cancer cells	516:533	liver cancer cells	516:533	O-GlcNAcylation induces transformative phenotypes of liver cancer cells in a YAP-dependent manner.
28474680	7	5	theme	blood	1155:1159	arg1	levels					1169:1174	high blood glucose levels	1150:1174	high blood glucose levels	1150:1174	We conclude that YAP O-GlcNAcylation is a potential therapeutic intervention point for treating liver cancer associated with high blood glucose levels and possibly diabetes.
28474680	7	6	theme	liver	1121:1125	arg1	cancer					1127:1132	liver cancer	1121:1132	liver cancer associated with high blood glucose levels	1121:1174	We conclude that YAP O-GlcNAcylation is a potential therapeutic intervention point for treating liver cancer associated with high blood glucose levels and possibly diabetes.
28474680	2	7	dep	expression	286:295	arg1	the					282:284	the	282:284	the	282:284	Here, we demonstrate that O-GlcNAcylation can enhance the expression, stability and function of Yes-associated protein (YAP), the downstream transcriptional regulator of the Hippo pathway and a potent oncogenic factor in liver cancer.
28474680	4	8	theme	YAP	582:584	arg1	YAP					582:584	YAP	582:584	YAP	582:584	An O-GlcNAc site of YAP was identified at Thr241, and mutating this site decreased the O-GlcNAcylation, stability, and pro-tumorigenic capacities of YAP, while increasing YAP phosphorylation.
28474680	4	8	theme	YAP	582:584	arg1	site					574:577	An O-GlcNAc site	562:577	An O-GlcNAc site of YAP	562:584	An O-GlcNAc site of YAP was identified at Thr241, and mutating this site decreased the O-GlcNAcylation, stability, and pro-tumorigenic capacities of YAP, while increasing YAP phosphorylation.
28474680	2	9	from	factor	439:444	arg1	cancer					455:460	liver cancer	449:460	liver cancer	449:460	Here, we demonstrate that O-GlcNAcylation can enhance the expression, stability and function of Yes-associated protein (YAP), the downstream transcriptional regulator of the Hippo pathway and a potent oncogenic factor in liver cancer.
28474680	5	10	dep	in	804:805	arg1	vivo					807:810	vivo	807:810	vivo	807:810	Importantly, we found via in vitro cell-based and in vivo mouse model experiments that O-GlcNAcylation of YAP was required for high-glucose-induced liver tumorigenesis.
28474680	3	11	theme	cells	529:533	arg1	phenotypes					502:511	transformative phenotypes	487:511	transformative phenotypes of liver cancer cells	487:533	O-GlcNAcylation induces transformative phenotypes of liver cancer cells in a YAP-dependent manner.
28474680	5	12	theme	liver	902:906	arg1	tumorigenesis					908:920	high-glucose-induced liver tumorigenesis	881:920	high-glucose-induced liver tumorigenesis	881:920	Importantly, we found via in vitro cell-based and in vivo mouse model experiments that O-GlcNAcylation of YAP was required for high-glucose-induced liver tumorigenesis.
28474680	4	13	theme	pro-tumorigenic	681:695	arg1	capacities					697:706	pro-tumorigenic capacities	681:706	pro-tumorigenic capacities	681:706	An O-GlcNAc site of YAP was identified at Thr241, and mutating this site decreased the O-GlcNAcylation, stability, and pro-tumorigenic capacities of YAP, while increasing YAP phosphorylation.
28474680	1	14	theme	various	150:156	arg1	origins					165:171	various tissue origins	150:171	various tissue origins	150:171	O-GlcNAcylation has been implicated in the tumorigenesis of various tissue origins, but its function in liver tumorigenesis is not clear.
28474680	7	15	dep	potential	1067:1075	arg1	therapeutic					1077:1087	therapeutic	1077:1087	therapeutic	1077:1087	We conclude that YAP O-GlcNAcylation is a potential therapeutic intervention point for treating liver cancer associated with high blood glucose levels and possibly diabetes.
28474680	5	16	theme	in	804:805	arg1	experiments					824:834	in vitro cell-based and in vivo mouse model experiments	780:834	in vitro cell-based and in vivo mouse model experiments	780:834	Importantly, we found via in vitro cell-based and in vivo mouse model experiments that O-GlcNAcylation of YAP was required for high-glucose-induced liver tumorigenesis.
28474680	5	17	theme	YAP	860:862	arg1	O-GlcNAcylation					841:855	O-GlcNAcylation	841:855	O-GlcNAcylation of YAP	841:862	Importantly, we found via in vitro cell-based and in vivo mouse model experiments that O-GlcNAcylation of YAP was required for high-glucose-induced liver tumorigenesis.
28474680	7	18	theme	YAP	1042:1044	arg1	point					1102:1106	a potential therapeutic intervention point	1065:1106	a potential therapeutic intervention point for treating liver cancer associated with high blood glucose levels and possibly diabetes	1065:1196	We conclude that YAP O-GlcNAcylation is a potential therapeutic intervention point for treating liver cancer associated with high blood glucose levels and possibly diabetes.
28474680	7	18	theme	YAP	1042:1044	arg1	O-GlcNAcylation					1046:1060	YAP O-GlcNAcylation	1042:1060	YAP O-GlcNAcylation	1042:1060	We conclude that YAP O-GlcNAcylation is a potential therapeutic intervention point for treating liver cancer associated with high blood glucose levels and possibly diabetes.
28474680	5	19	theme	in	780:781	arg1	experiments					824:834	in vitro cell-based and in vivo mouse model experiments	780:834	in vitro cell-based and in vivo mouse model experiments	780:834	Importantly, we found via in vitro cell-based and in vivo mouse model experiments that O-GlcNAcylation of YAP was required for high-glucose-induced liver tumorigenesis.
28474680	3	20	theme	YAP-dependent	540:552	arg1	manner					554:559	a YAP-dependent manner	538:559	a YAP-dependent manner	538:559	O-GlcNAcylation induces transformative phenotypes of liver cancer cells in a YAP-dependent manner.
28474680	0	21	theme	essential	4:12	arg1	role					14:17	The essential role	0:17	The essential role of YAP O-GlcNAcylation in high-glucose-stimulated liver tumorigenesis	0:87	The essential role of YAP O-GlcNAcylation in high-glucose-stimulated liver tumorigenesis.
28474680	5	22	dep	in	780:781	arg1	cell-based					789:798	cell-based	789:798	cell-based	789:798	Importantly, we found via in vitro cell-based and in vivo mouse model experiments that O-GlcNAcylation of YAP was required for high-glucose-induced liver tumorigenesis.
28474680	5	22	dep	in	780:781	arg1	vitro					783:787	vitro	783:787	vitro	783:787	Importantly, we found via in vitro cell-based and in vivo mouse model experiments that O-GlcNAcylation of YAP was required for high-glucose-induced liver tumorigenesis.
28474680	4	23	theme	O-GlcNAc	565:572	arg1	YAP					582:584	YAP	582:584	YAP	582:584	An O-GlcNAc site of YAP was identified at Thr241, and mutating this site decreased the O-GlcNAcylation, stability, and pro-tumorigenic capacities of YAP, while increasing YAP phosphorylation.
28474680	4	23	theme	O-GlcNAc	565:572	arg1	site					574:577	An O-GlcNAc site	562:577	An O-GlcNAc site of YAP	562:584	An O-GlcNAc site of YAP was identified at Thr241, and mutating this site decreased the O-GlcNAcylation, stability, and pro-tumorigenic capacities of YAP, while increasing YAP phosphorylation.
28474680	4	24	theme	YAP	733:735	arg1	phosphorylation					737:751	YAP phosphorylation	733:751	YAP phosphorylation	733:751	An O-GlcNAc site of YAP was identified at Thr241, and mutating this site decreased the O-GlcNAcylation, stability, and pro-tumorigenic capacities of YAP, while increasing YAP phosphorylation.
28474680	2	25	theme	transcriptional	369:383	arg1	regulator					385:393	the downstream transcriptional regulator	354:393	the downstream transcriptional regulator of the Hippo pathway	354:414	Here, we demonstrate that O-GlcNAcylation can enhance the expression, stability and function of Yes-associated protein (YAP), the downstream transcriptional regulator of the Hippo pathway and a potent oncogenic factor in liver cancer.
28474680	2	25	theme	transcriptional	369:383	arg1	protein					339:345	Yes-associated protein	324:345	Yes-associated protein (YAP)	324:351	Here, we demonstrate that O-GlcNAcylation can enhance the expression, stability and function of Yes-associated protein (YAP), the downstream transcriptional regulator of the Hippo pathway and a potent oncogenic factor in liver cancer.
28474680	2	26	theme	oncogenic	429:437	arg1	factor					439:444	a potent oncogenic factor	420:444	a potent oncogenic factor in liver cancer	420:460	Here, we demonstrate that O-GlcNAcylation can enhance the expression, stability and function of Yes-associated protein (YAP), the downstream transcriptional regulator of the Hippo pathway and a potent oncogenic factor in liver cancer.
28474680	2	26	theme	oncogenic	429:437	arg1	protein					339:345	Yes-associated protein	324:345	Yes-associated protein (YAP)	324:351	Here, we demonstrate that O-GlcNAcylation can enhance the expression, stability and function of Yes-associated protein (YAP), the downstream transcriptional regulator of the Hippo pathway and a potent oncogenic factor in liver cancer.
28474680	2	27	theme	potent	422:427	arg1	factor					439:444	a potent oncogenic factor	420:444	a potent oncogenic factor in liver cancer	420:460	Here, we demonstrate that O-GlcNAcylation can enhance the expression, stability and function of Yes-associated protein (YAP), the downstream transcriptional regulator of the Hippo pathway and a potent oncogenic factor in liver cancer.
28474680	2	27	theme	potent	422:427	arg1	protein					339:345	Yes-associated protein	324:345	Yes-associated protein (YAP)	324:351	Here, we demonstrate that O-GlcNAcylation can enhance the expression, stability and function of Yes-associated protein (YAP), the downstream transcriptional regulator of the Hippo pathway and a potent oncogenic factor in liver cancer.
28474680	6	28	theme	cellular	981:988	arg1	O-GlcNAcylation					990:1004	global cellular O-GlcNAcylation	974:1004	global cellular O-GlcNAcylation	974:1004	Interestingly, a positive feedback between YAP and global cellular O-GlcNAcylation is also uncovered.
28474680	3	29	theme	cancer	522:527	arg1	cells					529:533	liver cancer cells	516:533	liver cancer cells	516:533	O-GlcNAcylation induces transformative phenotypes of liver cancer cells in a YAP-dependent manner.
28474680	1	30	theme	tissue	158:163	arg1	origins					165:171	various tissue origins	150:171	various tissue origins	150:171	O-GlcNAcylation has been implicated in the tumorigenesis of various tissue origins, but its function in liver tumorigenesis is not clear.
28474680	0	31	theme	O-GlcNAcylation	26:40	arg1	role					14:17	The essential role	0:17	The essential role of YAP O-GlcNAcylation in high-glucose-stimulated liver tumorigenesis	0:87	The essential role of YAP O-GlcNAcylation in high-glucose-stimulated liver tumorigenesis.
28474680	6	32	theme	global	974:979	arg1	O-GlcNAcylation					990:1004	global cellular O-GlcNAcylation	974:1004	global cellular O-GlcNAcylation	974:1004	Interestingly, a positive feedback between YAP and global cellular O-GlcNAcylation is also uncovered.
28474680	7	33	theme	intervention	1089:1100	arg1	point					1102:1106	a potential therapeutic intervention point	1065:1106	a potential therapeutic intervention point for treating liver cancer associated with high blood glucose levels and possibly diabetes	1065:1196	We conclude that YAP O-GlcNAcylation is a potential therapeutic intervention point for treating liver cancer associated with high blood glucose levels and possibly diabetes.
28474680	7	33	theme	intervention	1089:1100	arg1	O-GlcNAcylation					1046:1060	YAP O-GlcNAcylation	1042:1060	YAP O-GlcNAcylation	1042:1060	We conclude that YAP O-GlcNAcylation is a potential therapeutic intervention point for treating liver cancer associated with high blood glucose levels and possibly diabetes.
28474680	1	34	theme	liver	194:198	arg1	tumorigenesis					200:212	liver tumorigenesis	194:212	liver tumorigenesis	194:212	O-GlcNAcylation has been implicated in the tumorigenesis of various tissue origins, but its function in liver tumorigenesis is not clear.
28474680	2	35	theme	pathway	408:414	arg1	factor					439:444	a potent oncogenic factor	420:444	a potent oncogenic factor in liver cancer	420:460	Here, we demonstrate that O-GlcNAcylation can enhance the expression, stability and function of Yes-associated protein (YAP), the downstream transcriptional regulator of the Hippo pathway and a potent oncogenic factor in liver cancer.
28474680	2	35	theme	pathway	408:414	arg1	regulator					385:393	the downstream transcriptional regulator	354:393	the downstream transcriptional regulator of the Hippo pathway	354:414	Here, we demonstrate that O-GlcNAcylation can enhance the expression, stability and function of Yes-associated protein (YAP), the downstream transcriptional regulator of the Hippo pathway and a potent oncogenic factor in liver cancer.
28474680	2	35	theme	pathway	408:414	arg1	protein					339:345	Yes-associated protein	324:345	Yes-associated protein (YAP)	324:351	Here, we demonstrate that O-GlcNAcylation can enhance the expression, stability and function of Yes-associated protein (YAP), the downstream transcriptional regulator of the Hippo pathway and a potent oncogenic factor in liver cancer.
28474680	0	36	theme	YAP	22:24	arg1	O-GlcNAcylation					26:40	YAP O-GlcNAcylation	22:40	YAP O-GlcNAcylation	22:40	The essential role of YAP O-GlcNAcylation in high-glucose-stimulated liver tumorigenesis.
28474680	5	37	theme	mouse	812:816	arg1	experiments					824:834	in vitro cell-based and in vivo mouse model experiments	780:834	in vitro cell-based and in vivo mouse model experiments	780:834	Importantly, we found via in vitro cell-based and in vivo mouse model experiments that O-GlcNAcylation of YAP was required for high-glucose-induced liver tumorigenesis.
28474680	2	38	from	regulator	385:393	arg1	cancer					455:460	liver cancer	449:460	liver cancer	449:460	Here, we demonstrate that O-GlcNAcylation can enhance the expression, stability and function of Yes-associated protein (YAP), the downstream transcriptional regulator of the Hippo pathway and a potent oncogenic factor in liver cancer.
28474680	2	39	theme	Hippo	402:406	arg1	pathway					408:414	the Hippo pathway	398:414	the Hippo pathway	398:414	Here, we demonstrate that O-GlcNAcylation can enhance the expression, stability and function of Yes-associated protein (YAP), the downstream transcriptional regulator of the Hippo pathway and a potent oncogenic factor in liver cancer.
28474680	0	40	theme	high-glucose-stimulated	45:67	arg1	tumorigenesis					75:87	high-glucose-stimulated liver tumorigenesis	45:87	high-glucose-stimulated liver tumorigenesis	45:87	The essential role of YAP O-GlcNAcylation in high-glucose-stimulated liver tumorigenesis.
28474680	5	41	theme	high-glucose-induced	881:900	arg1	tumorigenesis					908:920	high-glucose-induced liver tumorigenesis	881:920	high-glucose-induced liver tumorigenesis	881:920	Importantly, we found via in vitro cell-based and in vivo mouse model experiments that O-GlcNAcylation of YAP was required for high-glucose-induced liver tumorigenesis.
28474680	7	42	theme	potential	1067:1075	arg1	point					1102:1106	a potential therapeutic intervention point	1065:1106	a potential therapeutic intervention point for treating liver cancer associated with high blood glucose levels and possibly diabetes	1065:1196	We conclude that YAP O-GlcNAcylation is a potential therapeutic intervention point for treating liver cancer associated with high blood glucose levels and possibly diabetes.
28474680	7	42	theme	potential	1067:1075	arg1	O-GlcNAcylation					1046:1060	YAP O-GlcNAcylation	1042:1060	YAP O-GlcNAcylation	1042:1060	We conclude that YAP O-GlcNAcylation is a potential therapeutic intervention point for treating liver cancer associated with high blood glucose levels and possibly diabetes.
28474680	2	43	theme	liver	449:453	arg1	cancer					455:460	liver cancer	449:460	liver cancer	449:460	Here, we demonstrate that O-GlcNAcylation can enhance the expression, stability and function of Yes-associated protein (YAP), the downstream transcriptional regulator of the Hippo pathway and a potent oncogenic factor in liver cancer.
28474680	4	44	theme	YAP	711:713	arg1	capacities					697:706	pro-tumorigenic capacities	681:706	pro-tumorigenic capacities	681:706	An O-GlcNAc site of YAP was identified at Thr241, and mutating this site decreased the O-GlcNAcylation, stability, and pro-tumorigenic capacities of YAP, while increasing YAP phosphorylation.
28474680	4	44	theme	YAP	711:713	arg1	stability					666:674	stability	666:674	stability	666:674	An O-GlcNAc site of YAP was identified at Thr241, and mutating this site decreased the O-GlcNAcylation, stability, and pro-tumorigenic capacities of YAP, while increasing YAP phosphorylation.
28474680	4	44	theme	YAP	711:713	arg1	O-GlcNAcylation					649:663	O-GlcNAcylation	649:663	O-GlcNAcylation	649:663	An O-GlcNAc site of YAP was identified at Thr241, and mutating this site decreased the O-GlcNAcylation, stability, and pro-tumorigenic capacities of YAP, while increasing YAP phosphorylation.
28474680	2	45	theme	protein	339:345	arg1	expression					286:295	expression	286:295	expression	286:295	Here, we demonstrate that O-GlcNAcylation can enhance the expression, stability and function of Yes-associated protein (YAP), the downstream transcriptional regulator of the Hippo pathway and a potent oncogenic factor in liver cancer.
28474680	2	45	theme	protein	339:345	arg1	function					312:319	function	312:319	function	312:319	Here, we demonstrate that O-GlcNAcylation can enhance the expression, stability and function of Yes-associated protein (YAP), the downstream transcriptional regulator of the Hippo pathway and a potent oncogenic factor in liver cancer.
28474680	2	45	theme	protein	339:345	arg1	stability					298:306	stability	298:306	stability	298:306	Here, we demonstrate that O-GlcNAcylation can enhance the expression, stability and function of Yes-associated protein (YAP), the downstream transcriptional regulator of the Hippo pathway and a potent oncogenic factor in liver cancer.
28474680	5	46	theme	model	818:822	arg1	experiments					824:834	in vitro cell-based and in vivo mouse model experiments	780:834	in vitro cell-based and in vivo mouse model experiments	780:834	Importantly, we found via in vitro cell-based and in vivo mouse model experiments that O-GlcNAcylation of YAP was required for high-glucose-induced liver tumorigenesis.
28474680	7	47	theme	high	1150:1153	arg1	levels					1169:1174	high blood glucose levels	1150:1174	high blood glucose levels	1150:1174	We conclude that YAP O-GlcNAcylation is a potential therapeutic intervention point for treating liver cancer associated with high blood glucose levels and possibly diabetes.
28474680	2	48	theme	Yes-associated	324:337	arg1	factor					439:444	a potent oncogenic factor	420:444	a potent oncogenic factor in liver cancer	420:460	Here, we demonstrate that O-GlcNAcylation can enhance the expression, stability and function of Yes-associated protein (YAP), the downstream transcriptional regulator of the Hippo pathway and a potent oncogenic factor in liver cancer.
28474680	2	48	theme	Yes-associated	324:337	arg1	YAP					348:350	YAP	348:350	YAP	348:350	Here, we demonstrate that O-GlcNAcylation can enhance the expression, stability and function of Yes-associated protein (YAP), the downstream transcriptional regulator of the Hippo pathway and a potent oncogenic factor in liver cancer.
28474680	2	48	theme	Yes-associated	324:337	arg1	protein					339:345	Yes-associated protein	324:345	Yes-associated protein (YAP)	324:351	Here, we demonstrate that O-GlcNAcylation can enhance the expression, stability and function of Yes-associated protein (YAP), the downstream transcriptional regulator of the Hippo pathway and a potent oncogenic factor in liver cancer.
28474680	2	48	theme	Yes-associated	324:337	arg1	regulator					385:393	the downstream transcriptional regulator	354:393	the downstream transcriptional regulator of the Hippo pathway	354:414	Here, we demonstrate that O-GlcNAcylation can enhance the expression, stability and function of Yes-associated protein (YAP), the downstream transcriptional regulator of the Hippo pathway and a potent oncogenic factor in liver cancer.
28474680	2	49	theme	downstream	358:367	arg1	regulator					385:393	the downstream transcriptional regulator	354:393	the downstream transcriptional regulator of the Hippo pathway	354:414	Here, we demonstrate that O-GlcNAcylation can enhance the expression, stability and function of Yes-associated protein (YAP), the downstream transcriptional regulator of the Hippo pathway and a potent oncogenic factor in liver cancer.
28474680	2	49	theme	downstream	358:367	arg1	protein					339:345	Yes-associated protein	324:345	Yes-associated protein (YAP)	324:351	Here, we demonstrate that O-GlcNAcylation can enhance the expression, stability and function of Yes-associated protein (YAP), the downstream transcriptional regulator of the Hippo pathway and a potent oncogenic factor in liver cancer.
28474680	3	50	theme	transformative	487:500	arg1	phenotypes					502:511	transformative phenotypes	487:511	transformative phenotypes of liver cancer cells	487:533	O-GlcNAcylation induces transformative phenotypes of liver cancer cells in a YAP-dependent manner.
28474680	0	51	theme	liver	69:73	arg1	tumorigenesis					75:87	high-glucose-stimulated liver tumorigenesis	45:87	high-glucose-stimulated liver tumorigenesis	45:87	The essential role of YAP O-GlcNAcylation in high-glucose-stimulated liver tumorigenesis.
28474680	6	52	theme	positive	940:947	arg1	feedback					949:956	a positive feedback	938:956	a positive feedback between YAP and global cellular O-GlcNAcylation	938:1004	Interestingly, a positive feedback between YAP and global cellular O-GlcNAcylation is also uncovered.
28474680	4	53	dep	O-GlcNAcylation	649:663	arg1	the					645:647	the	645:647	the	645:647	An O-GlcNAc site of YAP was identified at Thr241, and mutating this site decreased the O-GlcNAcylation, stability, and pro-tumorigenic capacities of YAP, while increasing YAP phosphorylation.
28474680	1	54	theme	origins	165:171	arg1	tumorigenesis					133:145	the tumorigenesis	129:145	the tumorigenesis of various tissue origins	129:171	O-GlcNAcylation has been implicated in the tumorigenesis of various tissue origins, but its function in liver tumorigenesis is not clear.
21327254	5	0	theme	precise	847:853	arg1	localization					855:866	the precise localization	843:866	the precise localization of the O-GlcNAc sites on Tau, except for the S400 site that was very recently identified on the basis of ETD-FT-MS	843:981	Moreover, analytical difficulties have hampered the precise localization of the O-GlcNAc sites on Tau, except for the S400 site that was very recently identified on the basis of ETD-FT-MS.
21327254	4	1	theme	precise	763:769	arg1	mechanism					771:779	the precise mechanism	759:779	the precise mechanism	759:779	Another post-translational modification, the O-linked β-N-acetylglucosaminylation (O-GlcNAcylation), controls the phosphorylation state of Tau, although the precise mechanism is not known.
21327254	6	2	theme	microtubule-associated	1095:1116	arg1	repeats					1118:1124	the microtubule-associated repeats	1091:1124	the microtubule-associated repeats	1091:1124	Here, we identify three O-GlcNAc sites by screening a library of small peptides sampling the proline-rich, the microtubule-associated repeats and the carboxy-terminal domains of Tau as potential substrates for the O-β-N-acetylglucosaminyltransferase (OGT).
21327254	6	2	theme	microtubule-associated	1095:1116	arg1	Tau					1162:1164	Tau	1162:1164	Tau	1162:1164	Here, we identify three O-GlcNAc sites by screening a library of small peptides sampling the proline-rich, the microtubule-associated repeats and the carboxy-terminal domains of Tau as potential substrates for the O-β-N-acetylglucosaminyltransferase (OGT).
21327254	6	2	theme	microtubule-associated	1095:1116	arg1	substrates					1179:1188	potential substrates	1169:1188	potential substrates for the O-β-N-acetylglucosaminyltransferase (OGT)	1169:1238	Here, we identify three O-GlcNAc sites by screening a library of small peptides sampling the proline-rich, the microtubule-associated repeats and the carboxy-terminal domains of Tau as potential substrates for the O-β-N-acetylglucosaminyltransferase (OGT).
21327254	6	2	theme	microtubule-associated	1095:1116	arg1	domains					1151:1157	the carboxy-terminal domains	1130:1157	the carboxy-terminal domains	1130:1157	Here, we identify three O-GlcNAc sites by screening a library of small peptides sampling the proline-rich, the microtubule-associated repeats and the carboxy-terminal domains of Tau as potential substrates for the O-β-N-acetylglucosaminyltransferase (OGT).
21327254	2	3	theme	proteins	396:403	arg1	hyperphosphorylation					368:387	the hyperphosphorylation	364:387	the hyperphosphorylation of Tau proteins in neurons	364:414	A dysregulation of the phosphorylation/dephosphorylation balance leading to the hyperphosphorylation of Tau proteins in neurons is thought to favor their aggregation into insoluble filaments.
21327254	1	4	theme	stabilization	249:261	arg1	activity					207:214	its activity	203:214	its activity of tubulin polymerization and/or stabilization of microtubule assembly	203:285	Phosphorylation of the microtubule-associated Tau protein plays a major role in the regulation of its activity of tubulin polymerization and/or stabilization of microtubule assembly.
21327254	5	5	from	sites	884:888	arg1	Tau					893:895	Tau	893:895	Tau	893:895	Moreover, analytical difficulties have hampered the precise localization of the O-GlcNAc sites on Tau, except for the S400 site that was very recently identified on the basis of ETD-FT-MS.
21327254	7	6	dep	in	1245:1246	arg1	vitro					1248:1252	vitro	1248:1252	vitro	1248:1252	The in vitro activity of the nucleocytoplasmic OGT was assessed by tandem mass spectrometry and NMR spectroscopy.
21327254	2	7	theme	Tau	392:394	arg1	proteins					396:403	Tau proteins	392:403	Tau proteins	392:403	A dysregulation of the phosphorylation/dephosphorylation balance leading to the hyperphosphorylation of Tau proteins in neurons is thought to favor their aggregation into insoluble filaments.
21327254	8	8	from	sites	1470:1474	arg1	relationship					1403:1414	the relationship	1399:1414	the relationship between phosphate and O-GlcNAc incorporation at these sites	1399:1474	Using phosphorylated peptides, we establish the relationship between phosphate and O-GlcNAc incorporation at these sites.
21327254	6	9	theme	Tau	1162:1164	arg1	repeats					1118:1124	the microtubule-associated repeats	1091:1124	the microtubule-associated repeats	1091:1124	Here, we identify three O-GlcNAc sites by screening a library of small peptides sampling the proline-rich, the microtubule-associated repeats and the carboxy-terminal domains of Tau as potential substrates for the O-β-N-acetylglucosaminyltransferase (OGT).
21327254	6	9	theme	Tau	1162:1164	arg1	Tau					1162:1164	Tau	1162:1164	Tau	1162:1164	Here, we identify three O-GlcNAc sites by screening a library of small peptides sampling the proline-rich, the microtubule-associated repeats and the carboxy-terminal domains of Tau as potential substrates for the O-β-N-acetylglucosaminyltransferase (OGT).
21327254	6	9	theme	Tau	1162:1164	arg1	substrates					1179:1188	potential substrates	1169:1188	potential substrates for the O-β-N-acetylglucosaminyltransferase (OGT)	1169:1238	Here, we identify three O-GlcNAc sites by screening a library of small peptides sampling the proline-rich, the microtubule-associated repeats and the carboxy-terminal domains of Tau as potential substrates for the O-β-N-acetylglucosaminyltransferase (OGT).
21327254	6	9	theme	Tau	1162:1164	arg1	domains					1151:1157	the carboxy-terminal domains	1130:1157	the carboxy-terminal domains	1130:1157	Here, we identify three O-GlcNAc sites by screening a library of small peptides sampling the proline-rich, the microtubule-associated repeats and the carboxy-terminal domains of Tau as potential substrates for the O-β-N-acetylglucosaminyltransferase (OGT).
21327254	0	10	from	Identification	0:13	arg1	phosphorylation					88:102	phosphorylation	88:102	phosphorylation	88:102	Identification of O-GlcNAc sites within peptides of the Tau protein and their impact on phosphorylation.
21327254	8	11	theme	O-GlcNAc	1438:1445	arg1	incorporation					1447:1459	O-GlcNAc incorporation	1438:1459	O-GlcNAc incorporation	1438:1459	Using phosphorylated peptides, we establish the relationship between phosphate and O-GlcNAc incorporation at these sites.
21327254	1	12	theme	microtubule	266:276	arg1	assembly					278:285	microtubule assembly	266:285	microtubule assembly	266:285	Phosphorylation of the microtubule-associated Tau protein plays a major role in the regulation of its activity of tubulin polymerization and/or stabilization of microtubule assembly.
21327254	5	13	theme	analytical	805:814	arg1	difficulties					816:827	analytical difficulties	805:827	analytical difficulties	805:827	Moreover, analytical difficulties have hampered the precise localization of the O-GlcNAc sites on Tau, except for the S400 site that was very recently identified on the basis of ETD-FT-MS.
21327254	3	14	theme	many	541:544	arg1	disease					597:603	Alzheimer's disease	585:603	Alzheimer's disease	585:603	This in turn might underlie neuronal death as encountered in many neurodegenerative disorders, including Alzheimer's disease.
21327254	3	14	theme	many	541:544	arg1	disorders					564:572	many neurodegenerative disorders	541:572	many neurodegenerative disorders	541:572	This in turn might underlie neuronal death as encountered in many neurodegenerative disorders, including Alzheimer's disease.
21327254	1	15	theme	assembly	278:285	arg1	stabilization					249:261	stabilization	249:261	stabilization of microtubule assembly	249:285	Phosphorylation of the microtubule-associated Tau protein plays a major role in the regulation of its activity of tubulin polymerization and/or stabilization of microtubule assembly.
21327254	10	16	theme	sequential	1715:1724	arg1	process					1742:1748	the GSK3β-mediated sequential phosphorylation process	1696:1748	the GSK3β-mediated sequential phosphorylation process	1696:1748	Reciprocally, S400 O-GlcNAcylation reduces S404 phosphorylation by the CDK2/cyclinA3 kinase and interrupts the GSK3β-mediated sequential phosphorylation process.
21327254	2	17	from	hyperphosphorylation	368:387	arg1	neurons					408:414	neurons	408:414	neurons	408:414	A dysregulation of the phosphorylation/dephosphorylation balance leading to the hyperphosphorylation of Tau proteins in neurons is thought to favor their aggregation into insoluble filaments.
21327254	6	18	dep	repeats	1118:1124	arg1	the					1073:1075	the	1073:1075	the	1073:1075	Here, we identify three O-GlcNAc sites by screening a library of small peptides sampling the proline-rich, the microtubule-associated repeats and the carboxy-terminal domains of Tau as potential substrates for the O-β-N-acetylglucosaminyltransferase (OGT).
21327254	1	19	theme	major	171:175	arg1	role					177:180	a major role	169:180	a major role	169:180	Phosphorylation of the microtubule-associated Tau protein plays a major role in the regulation of its activity of tubulin polymerization and/or stabilization of microtubule assembly.
21327254	4	20	theme	O-linked	651:658	arg1	O-GlcNAcylation					689:703	O-GlcNAcylation	689:703	O-GlcNAcylation	689:703	Another post-translational modification, the O-linked β-N-acetylglucosaminylation (O-GlcNAcylation), controls the phosphorylation state of Tau, although the precise mechanism is not known.
21327254	4	20	theme	O-linked	651:658	arg1	β-N-acetylglucosaminylation					660:686	the O-linked β-N-acetylglucosaminylation	647:686	the O-linked β-N-acetylglucosaminylation (O-GlcNAcylation)	647:704	Another post-translational modification, the O-linked β-N-acetylglucosaminylation (O-GlcNAcylation), controls the phosphorylation state of Tau, although the precise mechanism is not known.
21327254	4	20	theme	O-linked	651:658	arg1	modification					633:644	Another post-translational modification	606:644	Another post-translational modification	606:644	Another post-translational modification, the O-linked β-N-acetylglucosaminylation (O-GlcNAcylation), controls the phosphorylation state of Tau, although the precise mechanism is not known.
21327254	6	21	theme	small	1049:1053	arg1	peptides					1055:1062	small peptides	1049:1062	small peptides sampling the proline-rich, the microtubule-associated repeats and the carboxy-terminal domains of Tau as potential substrates for the O-β-N-acetylglucosaminyltransferase (OGT)	1049:1238	Here, we identify three O-GlcNAc sites by screening a library of small peptides sampling the proline-rich, the microtubule-associated repeats and the carboxy-terminal domains of Tau as potential substrates for the O-β-N-acetylglucosaminyltransferase (OGT).
21327254	9	22	theme	neighboring	1496:1506	arg1	residues					1508:1515	neighboring residues	1496:1515	neighboring residues S396 and S404	1496:1529	Phosphorylation of neighboring residues S396 and S404 was found to decrease significantly S400 O-GlcNAcylation.
21327254	9	22	theme	neighboring	1496:1506	arg1	S404					1526:1529	S404	1526:1529	S404	1526:1529	Phosphorylation of neighboring residues S396 and S404 was found to decrease significantly S400 O-GlcNAcylation.
21327254	9	22	theme	neighboring	1496:1506	arg1	S396					1517:1520	S396	1517:1520	S396	1517:1520	Phosphorylation of neighboring residues S396 and S404 was found to decrease significantly S400 O-GlcNAcylation.
21327254	6	23	theme	O-GlcNAc	1008:1015	arg1	sites					1017:1021	three O-GlcNAc sites	1002:1021	three O-GlcNAc sites	1002:1021	Here, we identify three O-GlcNAc sites by screening a library of small peptides sampling the proline-rich, the microtubule-associated repeats and the carboxy-terminal domains of Tau as potential substrates for the O-β-N-acetylglucosaminyltransferase (OGT).
21327254	6	24	theme	carboxy-terminal	1134:1149	arg1	repeats					1118:1124	the microtubule-associated repeats	1091:1124	the microtubule-associated repeats	1091:1124	Here, we identify three O-GlcNAc sites by screening a library of small peptides sampling the proline-rich, the microtubule-associated repeats and the carboxy-terminal domains of Tau as potential substrates for the O-β-N-acetylglucosaminyltransferase (OGT).
21327254	6	24	theme	carboxy-terminal	1134:1149	arg1	Tau					1162:1164	Tau	1162:1164	Tau	1162:1164	Here, we identify three O-GlcNAc sites by screening a library of small peptides sampling the proline-rich, the microtubule-associated repeats and the carboxy-terminal domains of Tau as potential substrates for the O-β-N-acetylglucosaminyltransferase (OGT).
21327254	6	24	theme	carboxy-terminal	1134:1149	arg1	substrates					1179:1188	potential substrates	1169:1188	potential substrates for the O-β-N-acetylglucosaminyltransferase (OGT)	1169:1238	Here, we identify three O-GlcNAc sites by screening a library of small peptides sampling the proline-rich, the microtubule-associated repeats and the carboxy-terminal domains of Tau as potential substrates for the O-β-N-acetylglucosaminyltransferase (OGT).
21327254	6	24	theme	carboxy-terminal	1134:1149	arg1	domains					1151:1157	the carboxy-terminal domains	1130:1157	the carboxy-terminal domains	1130:1157	Here, we identify three O-GlcNAc sites by screening a library of small peptides sampling the proline-rich, the microtubule-associated repeats and the carboxy-terminal domains of Tau as potential substrates for the O-β-N-acetylglucosaminyltransferase (OGT).
21327254	5	25	from	Tau	893:895	arg1	localization					855:866	the precise localization	843:866	the precise localization of the O-GlcNAc sites on Tau, except for the S400 site that was very recently identified on the basis of ETD-FT-MS	843:981	Moreover, analytical difficulties have hampered the precise localization of the O-GlcNAc sites on Tau, except for the S400 site that was very recently identified on the basis of ETD-FT-MS.
21327254	10	26	theme	phosphorylation	1726:1740	arg1	process					1742:1748	the GSK3β-mediated sequential phosphorylation process	1696:1748	the GSK3β-mediated sequential phosphorylation process	1696:1748	Reciprocally, S400 O-GlcNAcylation reduces S404 phosphorylation by the CDK2/cyclinA3 kinase and interrupts the GSK3β-mediated sequential phosphorylation process.
21327254	2	27	theme	balance	345:351	arg1	dysregulation					290:302	A dysregulation	288:302	A dysregulation of the phosphorylation/dephosphorylation balance leading to the hyperphosphorylation of Tau proteins in neurons	288:414	A dysregulation of the phosphorylation/dephosphorylation balance leading to the hyperphosphorylation of Tau proteins in neurons is thought to favor their aggregation into insoluble filaments.
21327254	9	28	theme	S400	1567:1570	arg1	O-GlcNAcylation					1572:1586	S400 O-GlcNAcylation	1567:1586	S400 O-GlcNAcylation	1567:1586	Phosphorylation of neighboring residues S396 and S404 was found to decrease significantly S400 O-GlcNAcylation.
21327254	0	29	theme	sites	27:31	arg1	Identification					0:13	Identification	0:13	Identification of O-GlcNAc sites within peptides of the Tau protein	0:66	Identification of O-GlcNAc sites within peptides of the Tau protein and their impact on phosphorylation.
21327254	0	29	theme	sites	27:31	arg1	impact					78:83	their impact	72:83	their impact on phosphorylation	72:102	Identification of O-GlcNAc sites within peptides of the Tau protein and their impact on phosphorylation.
21327254	10	30	theme	S404	1632:1635	arg1	phosphorylation					1637:1651	S404 phosphorylation	1632:1651	S404 phosphorylation by the CDK2/cyclinA3 kinase	1632:1679	Reciprocally, S400 O-GlcNAcylation reduces S404 phosphorylation by the CDK2/cyclinA3 kinase and interrupts the GSK3β-mediated sequential phosphorylation process.
21327254	2	31	theme	phosphorylation/dephosphorylation	311:343	arg1	balance					345:351	the phosphorylation/dephosphorylation balance	307:351	the phosphorylation/dephosphorylation balance leading to the hyperphosphorylation of Tau proteins in neurons	307:414	A dysregulation of the phosphorylation/dephosphorylation balance leading to the hyperphosphorylation of Tau proteins in neurons is thought to favor their aggregation into insoluble filaments.
21327254	2	32	theme	insoluble	459:467	arg1	filaments					469:477	insoluble filaments	459:477	insoluble filaments	459:477	A dysregulation of the phosphorylation/dephosphorylation balance leading to the hyperphosphorylation of Tau proteins in neurons is thought to favor their aggregation into insoluble filaments.
21327254	0	33	theme	O-GlcNAc	18:25	arg1	sites					27:31	O-GlcNAc sites	18:31	O-GlcNAc sites within peptides of the Tau protein	18:66	Identification of O-GlcNAc sites within peptides of the Tau protein and their impact on phosphorylation.
21327254	9	34	dep	residues	1508:1515	arg1	residues					1508:1515	neighboring residues	1496:1515	neighboring residues S396 and S404	1496:1529	Phosphorylation of neighboring residues S396 and S404 was found to decrease significantly S400 O-GlcNAcylation.
21327254	9	34	dep	residues	1508:1515	arg1	S404					1526:1529	S404	1526:1529	S404	1526:1529	Phosphorylation of neighboring residues S396 and S404 was found to decrease significantly S400 O-GlcNAcylation.
21327254	9	34	dep	residues	1508:1515	arg1	S396					1517:1520	S396	1517:1520	S396	1517:1520	Phosphorylation of neighboring residues S396 and S404 was found to decrease significantly S400 O-GlcNAcylation.
21327254	3	35	theme	neurodegenerative	546:562	arg1	disease					597:603	Alzheimer's disease	585:603	Alzheimer's disease	585:603	This in turn might underlie neuronal death as encountered in many neurodegenerative disorders, including Alzheimer's disease.
21327254	3	35	theme	neurodegenerative	546:562	arg1	disorders					564:572	many neurodegenerative disorders	541:572	many neurodegenerative disorders	541:572	This in turn might underlie neuronal death as encountered in many neurodegenerative disorders, including Alzheimer's disease.
21327254	3	36	theme	neuronal	508:515	arg1	death					517:521	neuronal death	508:521	neuronal death	508:521	This in turn might underlie neuronal death as encountered in many neurodegenerative disorders, including Alzheimer's disease.
21327254	10	37	theme	GSK3β-mediated	1700:1713	arg1	process					1742:1748	the GSK3β-mediated sequential phosphorylation process	1696:1748	the GSK3β-mediated sequential phosphorylation process	1696:1748	Reciprocally, S400 O-GlcNAcylation reduces S404 phosphorylation by the CDK2/cyclinA3 kinase and interrupts the GSK3β-mediated sequential phosphorylation process.
21327254	4	38	theme	post-translational	614:631	arg1	β-N-acetylglucosaminylation					660:686	the O-linked β-N-acetylglucosaminylation	647:686	the O-linked β-N-acetylglucosaminylation (O-GlcNAcylation)	647:704	Another post-translational modification, the O-linked β-N-acetylglucosaminylation (O-GlcNAcylation), controls the phosphorylation state of Tau, although the precise mechanism is not known.
21327254	4	38	theme	post-translational	614:631	arg1	modification					633:644	Another post-translational modification	606:644	Another post-translational modification	606:644	Another post-translational modification, the O-linked β-N-acetylglucosaminylation (O-GlcNAcylation), controls the phosphorylation state of Tau, although the precise mechanism is not known.
21327254	8	39	theme	phosphorylated	1361:1374	arg1	peptides					1376:1383	phosphorylated peptides	1361:1383	phosphorylated peptides	1361:1383	Using phosphorylated peptides, we establish the relationship between phosphate and O-GlcNAc incorporation at these sites.
21327254	4	40	theme	phosphorylation	720:734	arg1	state					736:740	the phosphorylation state	716:740	the phosphorylation state of Tau	716:747	Another post-translational modification, the O-linked β-N-acetylglucosaminylation (O-GlcNAcylation), controls the phosphorylation state of Tau, although the precise mechanism is not known.
21327254	5	41	theme	S400	913:916	arg1	site					918:921	the S400 site	909:921	the S400 site that was very recently identified on the basis of ETD-FT-MS	909:981	Moreover, analytical difficulties have hampered the precise localization of the O-GlcNAc sites on Tau, except for the S400 site that was very recently identified on the basis of ETD-FT-MS.
21327254	4	42	theme	Tau	745:747	arg1	state					736:740	the phosphorylation state	716:740	the phosphorylation state of Tau	716:747	Another post-translational modification, the O-linked β-N-acetylglucosaminylation (O-GlcNAcylation), controls the phosphorylation state of Tau, although the precise mechanism is not known.
21327254	10	43	theme	S400	1603:1606	arg1	O-GlcNAcylation					1608:1622	S400 O-GlcNAcylation	1603:1622	S400 O-GlcNAcylation	1603:1622	Reciprocally, S400 O-GlcNAcylation reduces S404 phosphorylation by the CDK2/cyclinA3 kinase and interrupts the GSK3β-mediated sequential phosphorylation process.
21327254	9	44	theme	residues	1508:1515	arg1	Phosphorylation					1477:1491	Phosphorylation	1477:1491	Phosphorylation of neighboring residues S396 and S404	1477:1529	Phosphorylation of neighboring residues S396 and S404 was found to decrease significantly S400 O-GlcNAcylation.
21327254	1	45	theme	activity	207:214	arg1	regulation					189:198	the regulation	185:198	the regulation of its activity of tubulin polymerization and/or stabilization of microtubule assembly	185:285	Phosphorylation of the microtubule-associated Tau protein plays a major role in the regulation of its activity of tubulin polymerization and/or stabilization of microtubule assembly.
21327254	5	46	theme	O-GlcNAc	875:882	arg1	sites					884:888	the O-GlcNAc sites	871:888	the O-GlcNAc sites	871:888	Moreover, analytical difficulties have hampered the precise localization of the O-GlcNAc sites on Tau, except for the S400 site that was very recently identified on the basis of ETD-FT-MS.
21327254	7	47	theme	nucleocytoplasmic	1270:1286	arg1	OGT					1288:1290	the nucleocytoplasmic OGT	1266:1290	the nucleocytoplasmic OGT	1266:1290	The in vitro activity of the nucleocytoplasmic OGT was assessed by tandem mass spectrometry and NMR spectroscopy.
21327254	10	48	theme	CDK2/cyclinA3	1660:1672	arg1	kinase					1674:1679	the CDK2/cyclinA3 kinase	1656:1679	the CDK2/cyclinA3 kinase	1656:1679	Reciprocally, S400 O-GlcNAcylation reduces S404 phosphorylation by the CDK2/cyclinA3 kinase and interrupts the GSK3β-mediated sequential phosphorylation process.
21327254	7	49	theme	tandem	1308:1313	arg1	spectrometry					1320:1331	tandem mass spectrometry	1308:1331	tandem mass spectrometry	1308:1331	The in vitro activity of the nucleocytoplasmic OGT was assessed by tandem mass spectrometry and NMR spectroscopy.
21327254	6	50	theme	potential	1169:1177	arg1	repeats					1118:1124	the microtubule-associated repeats	1091:1124	the microtubule-associated repeats	1091:1124	Here, we identify three O-GlcNAc sites by screening a library of small peptides sampling the proline-rich, the microtubule-associated repeats and the carboxy-terminal domains of Tau as potential substrates for the O-β-N-acetylglucosaminyltransferase (OGT).
21327254	6	50	theme	potential	1169:1177	arg1	Tau					1162:1164	Tau	1162:1164	Tau	1162:1164	Here, we identify three O-GlcNAc sites by screening a library of small peptides sampling the proline-rich, the microtubule-associated repeats and the carboxy-terminal domains of Tau as potential substrates for the O-β-N-acetylglucosaminyltransferase (OGT).
21327254	6	50	theme	potential	1169:1177	arg1	substrates					1179:1188	potential substrates	1169:1188	potential substrates for the O-β-N-acetylglucosaminyltransferase (OGT)	1169:1238	Here, we identify three O-GlcNAc sites by screening a library of small peptides sampling the proline-rich, the microtubule-associated repeats and the carboxy-terminal domains of Tau as potential substrates for the O-β-N-acetylglucosaminyltransferase (OGT).
21327254	6	50	theme	potential	1169:1177	arg1	domains					1151:1157	the carboxy-terminal domains	1130:1157	the carboxy-terminal domains	1130:1157	Here, we identify three O-GlcNAc sites by screening a library of small peptides sampling the proline-rich, the microtubule-associated repeats and the carboxy-terminal domains of Tau as potential substrates for the O-β-N-acetylglucosaminyltransferase (OGT).
21327254	5	51	theme	sites	884:888	arg1	localization					855:866	the precise localization	843:866	the precise localization of the O-GlcNAc sites on Tau, except for the S400 site that was very recently identified on the basis of ETD-FT-MS	843:981	Moreover, analytical difficulties have hampered the precise localization of the O-GlcNAc sites on Tau, except for the S400 site that was very recently identified on the basis of ETD-FT-MS.
21327254	5	52	from	localization	855:866	arg1	Tau					893:895	Tau	893:895	Tau	893:895	Moreover, analytical difficulties have hampered the precise localization of the O-GlcNAc sites on Tau, except for the S400 site that was very recently identified on the basis of ETD-FT-MS.
21327254	7	53	theme	OGT	1288:1290	arg1	activity					1254:1261	The in vitro activity	1241:1261	The in vitro activity of the nucleocytoplasmic OGT	1241:1290	The in vitro activity of the nucleocytoplasmic OGT was assessed by tandem mass spectrometry and NMR spectroscopy.
21327254	5	54	theme	ETD-FT-MS	973:981	arg1	basis					964:968	the basis	960:968	the basis of ETD-FT-MS	960:981	Moreover, analytical difficulties have hampered the precise localization of the O-GlcNAc sites on Tau, except for the S400 site that was very recently identified on the basis of ETD-FT-MS.
21327254	7	55	theme	NMR	1337:1339	arg1	spectroscopy					1341:1352	NMR spectroscopy	1337:1352	NMR spectroscopy	1337:1352	The in vitro activity of the nucleocytoplasmic OGT was assessed by tandem mass spectrometry and NMR spectroscopy.
21327254	4	56	link	O-linked	651:658	arg1	O-GlcNAcylation					689:703	O-GlcNAcylation	689:703	O-GlcNAcylation	689:703	Another post-translational modification, the O-linked β-N-acetylglucosaminylation (O-GlcNAcylation), controls the phosphorylation state of Tau, although the precise mechanism is not known.
21327254	4	56	link	O-linked	651:658	arg1	β-N-acetylglucosaminylation					660:686	the O-linked β-N-acetylglucosaminylation	647:686	the O-linked β-N-acetylglucosaminylation (O-GlcNAcylation)	647:704	Another post-translational modification, the O-linked β-N-acetylglucosaminylation (O-GlcNAcylation), controls the phosphorylation state of Tau, although the precise mechanism is not known.
21327254	4	56	link	O-linked	651:658	arg1	modification					633:644	Another post-translational modification	606:644	Another post-translational modification	606:644	Another post-translational modification, the O-linked β-N-acetylglucosaminylation (O-GlcNAcylation), controls the phosphorylation state of Tau, although the precise mechanism is not known.
21327254	6	57	theme	proline-rich	1077:1088	arg1	repeats					1118:1124	the microtubule-associated repeats	1091:1124	the microtubule-associated repeats	1091:1124	Here, we identify three O-GlcNAc sites by screening a library of small peptides sampling the proline-rich, the microtubule-associated repeats and the carboxy-terminal domains of Tau as potential substrates for the O-β-N-acetylglucosaminyltransferase (OGT).
21327254	6	57	theme	proline-rich	1077:1088	arg1	Tau					1162:1164	Tau	1162:1164	Tau	1162:1164	Here, we identify three O-GlcNAc sites by screening a library of small peptides sampling the proline-rich, the microtubule-associated repeats and the carboxy-terminal domains of Tau as potential substrates for the O-β-N-acetylglucosaminyltransferase (OGT).
21327254	6	57	theme	proline-rich	1077:1088	arg1	substrates					1179:1188	potential substrates	1169:1188	potential substrates for the O-β-N-acetylglucosaminyltransferase (OGT)	1169:1238	Here, we identify three O-GlcNAc sites by screening a library of small peptides sampling the proline-rich, the microtubule-associated repeats and the carboxy-terminal domains of Tau as potential substrates for the O-β-N-acetylglucosaminyltransferase (OGT).
21327254	6	57	theme	proline-rich	1077:1088	arg1	domains					1151:1157	the carboxy-terminal domains	1130:1157	the carboxy-terminal domains	1130:1157	Here, we identify three O-GlcNAc sites by screening a library of small peptides sampling the proline-rich, the microtubule-associated repeats and the carboxy-terminal domains of Tau as potential substrates for the O-β-N-acetylglucosaminyltransferase (OGT).
21327254	1	58	theme	microtubule-associated	128:149	arg1	protein					155:161	the microtubule-associated Tau protein	124:161	the microtubule-associated Tau protein	124:161	Phosphorylation of the microtubule-associated Tau protein plays a major role in the regulation of its activity of tubulin polymerization and/or stabilization of microtubule assembly.
21327254	1	59	theme	tubulin	219:225	arg1	polymerization					227:240	tubulin polymerization	219:240	tubulin polymerization	219:240	Phosphorylation of the microtubule-associated Tau protein plays a major role in the regulation of its activity of tubulin polymerization and/or stabilization of microtubule assembly.
21327254	0	60	theme	protein	60:66	arg1	peptides					40:47	peptides	40:47	peptides of the Tau protein	40:66	Identification of O-GlcNAc sites within peptides of the Tau protein and their impact on phosphorylation.
21327254	0	61	from	impact	78:83	arg1	phosphorylation					88:102	phosphorylation	88:102	phosphorylation	88:102	Identification of O-GlcNAc sites within peptides of the Tau protein and their impact on phosphorylation.
21327254	1	62	theme	Tau	151:153	arg1	protein					155:161	the microtubule-associated Tau protein	124:161	the microtubule-associated Tau protein	124:161	Phosphorylation of the microtubule-associated Tau protein plays a major role in the regulation of its activity of tubulin polymerization and/or stabilization of microtubule assembly.
21327254	1	63	theme	polymerization	227:240	arg1	activity					207:214	its activity	203:214	its activity of tubulin polymerization and/or stabilization of microtubule assembly	203:285	Phosphorylation of the microtubule-associated Tau protein plays a major role in the regulation of its activity of tubulin polymerization and/or stabilization of microtubule assembly.
21327254	0	64	theme	Tau	56:58	arg1	protein					60:66	the Tau protein	52:66	the Tau protein	52:66	Identification of O-GlcNAc sites within peptides of the Tau protein and their impact on phosphorylation.
21327254	7	65	theme	in	1245:1246	arg1	activity					1254:1261	The in vitro activity	1241:1261	The in vitro activity of the nucleocytoplasmic OGT	1241:1290	The in vitro activity of the nucleocytoplasmic OGT was assessed by tandem mass spectrometry and NMR spectroscopy.
21327254	1	66	theme	protein	155:161	arg1	Phosphorylation					105:119	Phosphorylation	105:119	Phosphorylation of the microtubule-associated Tau protein	105:161	Phosphorylation of the microtubule-associated Tau protein plays a major role in the regulation of its activity of tubulin polymerization and/or stabilization of microtubule assembly.
21327254	7	67	theme	mass	1315:1318	arg1	spectrometry					1320:1331	tandem mass spectrometry	1308:1331	tandem mass spectrometry	1308:1331	The in vitro activity of the nucleocytoplasmic OGT was assessed by tandem mass spectrometry and NMR spectroscopy.
21327254	6	68	theme	peptides	1055:1062	arg1	library					1038:1044	a library	1036:1044	a library of small peptides sampling the proline-rich, the microtubule-associated repeats and the carboxy-terminal domains of Tau as potential substrates for the O-β-N-acetylglucosaminyltransferase (OGT)	1036:1238	Here, we identify three O-GlcNAc sites by screening a library of small peptides sampling the proline-rich, the microtubule-associated repeats and the carboxy-terminal domains of Tau as potential substrates for the O-β-N-acetylglucosaminyltransferase (OGT).
23399548	4	0	theme	affinity-enriched	956:972	arg1	glycopeptides					974:986	affinity-enriched glycopeptides	956:986	affinity-enriched glycopeptides	956:986	Here, we demonstrate a substantial improvement in the SimpleCell strategy by including an additional stage of lectin affinity chromatography on secreted glycoproteins from culture media (secretome) and by incorporating pre-fractionation of affinity-enriched glycopeptides via IEF before nLC-MS/MS.
23399548	10	1	theme	≈	1984:1984	arg1	O-glycosites					1990:2001	≈ 220 O-glycosites	1984:2001	≈ 220 O-glycosites	1984:2001	Furthermore, we uncovered ≈ 220 O-glycosites wherein the peptides were clearly identified, but the glycosites could not be unambiguously assigned to specific positions.
23399548	2	2	theme	zinc	362:365	arg1	lines					412:416	zinc finger nuclease gene-engineered "SimpleCell" lines	362:416	zinc finger nuclease gene-engineered "SimpleCell" lines producing homogeneous truncated O-glycosylation	362:464	Recently, we presented a novel strategy for high throughput identification of O-GalNAc glycosites using zinc finger nuclease gene-engineered "SimpleCell" lines producing homogeneous truncated O-glycosylation.
23399548	4	3	from	improvement	751:761	arg1	strategy					781:788	the SimpleCell strategy	766:788	the SimpleCell strategy	766:788	Here, we demonstrate a substantial improvement in the SimpleCell strategy by including an additional stage of lectin affinity chromatography on secreted glycoproteins from culture media (secretome) and by incorporating pre-fractionation of affinity-enriched glycopeptides via IEF before nLC-MS/MS.
23399548	9	4	theme	individual	1759:1768	arg1	glycosites					1770:1779	individual glycosites	1759:1779	individual glycosites	1759:1779	With respect to individual glycosites, we identified a total of 856 sites, of which 508 (59%) were novel compared with our previous strategy; this includes four new identifications of O-GalNAc attached to tyrosine.
23399548	3	5	gly	O-glycosylation	699:713	arg2	sites					690:694	sites	690:694	sites of O-glycosylation	690:713	Total lysates of cells were trypsinized and subjected to lectin affinity chromatography enrichment, followed by identification of GalNAc O-glycopeptides by nLC-MS/MS, with electron transfer dissociation employed to specify sites of O-glycosylation.
23399548	3	5	gly	O-glycosylation	699:713	arg2	O-glycosylation					699:713	O-glycosylation	699:713	O-glycosylation	699:713	Total lysates of cells were trypsinized and subjected to lectin affinity chromatography enrichment, followed by identification of GalNAc O-glycopeptides by nLC-MS/MS, with electron transfer dissociation employed to specify sites of O-glycosylation.
23399548	6	6	theme	fractions	1411:1419	arg1	analysis					1377:1384	analysis	1377:1384	analysis of subcellular organelle fractions	1377:1419	We found that analysis of the secretome was an important independent factor for increasing identifications, suggesting that further substantial improvements can also be sought through analysis of subcellular organelle fractions.
23399548	3	7	theme	GalNAc	597:602	arg1	O-glycopeptides					604:618	GalNAc O-glycopeptides	597:618	GalNAc O-glycopeptides	597:618	Total lysates of cells were trypsinized and subjected to lectin affinity chromatography enrichment, followed by identification of GalNAc O-glycopeptides by nLC-MS/MS, with electron transfer dissociation employed to specify sites of O-glycosylation.
23399548	6	8	theme	subcellular	1389:1399	arg1	fractions					1411:1419	subcellular organelle fractions	1389:1419	subcellular organelle fractions	1389:1419	We found that analysis of the secretome was an important independent factor for increasing identifications, suggesting that further substantial improvements can also be sought through analysis of subcellular organelle fractions.
23399548	9	9	theme	total	1798:1802	arg1	novel					1842:1846	novel	1842:1846	novel	1842:1846	With respect to individual glycosites, we identified a total of 856 sites, of which 508 (59%) were novel compared with our previous strategy; this includes four new identifications of O-GalNAc attached to tyrosine.
23399548	6	10	theme	increasing	1273:1282	arg1	identifications					1284:1298	increasing identifications	1273:1298	increasing identifications	1273:1298	We found that analysis of the secretome was an important independent factor for increasing identifications, suggesting that further substantial improvements can also be sought through analysis of subcellular organelle fractions.
23399548	2	11	theme	throughput	307:316	arg1	identification					318:331	high throughput identification	302:331	high throughput identification of O-GalNAc glycosites using zinc finger nuclease gene-engineered "SimpleCell" lines producing homogeneous truncated O-glycosylation	302:464	Recently, we presented a novel strategy for high throughput identification of O-GalNAc glycosites using zinc finger nuclease gene-engineered "SimpleCell" lines producing homogeneous truncated O-glycosylation.
23399548	11	12	theme	O-glycoproteome	2233:2247	arg1	characterization					2191:2206	high throughput characterization	2175:2206	high throughput characterization of the human GalNAc-type O-glycoproteome	2175:2247	The improved strategy should greatly facilitate high throughput characterization of the human GalNAc-type O-glycoproteome as well as be applicable to analysis of other O-glycoproteomes.
23399548	5	13	from	increase	1122:1129	arg1	number					1138:1143	the number	1134:1143	the number of O-glycoproteins and O-glycosites identified	1134:1190	We applied these improvements to three human SimpleCells studied previously, and each yielded a substantial increase in the number of O-glycoproteins and O-glycosites identified.
23399548	11	14	theme	improved	2131:2138	arg1	strategy					2140:2147	The improved strategy	2127:2147	The improved strategy	2127:2147	The improved strategy should greatly facilitate high throughput characterization of the human GalNAc-type O-glycoproteome as well as be applicable to analysis of other O-glycoproteomes.
23399548	11	14	theme	improved	2131:2138	arg1	applicable					2263:2272	applicable	2263:2272	applicable	2263:2272	The improved strategy should greatly facilitate high throughput characterization of the human GalNAc-type O-glycoproteome as well as be applicable to analysis of other O-glycoproteomes.
23399548	7	15	theme	protease	1538:1545	arg1	chymotrypsin					1558:1569	chymotrypsin	1558:1569	chymotrypsin	1558:1569	In addition, we uncovered a substantial nonoverlapping set of O-glycoproteins and O-glycosites using an alternative protease digestion (chymotrypsin).
23399548	7	15	theme	protease	1538:1545	arg1	digestion					1547:1555	an alternative protease digestion	1523:1555	an alternative protease digestion (chymotrypsin)	1523:1570	In addition, we uncovered a substantial nonoverlapping set of O-glycoproteins and O-glycosites using an alternative protease digestion (chymotrypsin).
23399548	11	16	theme	throughput	2180:2189	arg1	characterization					2191:2206	high throughput characterization	2175:2206	high throughput characterization of the human GalNAc-type O-glycoproteome	2175:2247	The improved strategy should greatly facilitate high throughput characterization of the human GalNAc-type O-glycoproteome as well as be applicable to analysis of other O-glycoproteomes.
23399548	3	17	theme	electron	639:646	arg1	dissociation					657:668	electron transfer dissociation	639:668	electron transfer dissociation employed to specify sites of O-glycosylation	639:713	Total lysates of cells were trypsinized and subjected to lectin affinity chromatography enrichment, followed by identification of GalNAc O-glycopeptides by nLC-MS/MS, with electron transfer dissociation employed to specify sites of O-glycosylation.
23399548	7	18	theme	O-glycosites	1504:1515	arg1	O-glycosites					1504:1515	O-glycosites	1504:1515	O-glycosites	1504:1515	In addition, we uncovered a substantial nonoverlapping set of O-glycoproteins and O-glycosites using an alternative protease digestion (chymotrypsin).
23399548	7	18	theme	O-glycosites	1504:1515	arg1	O-glycoproteins					1484:1498	O-glycoproteins	1484:1498	O-glycoproteins	1484:1498	In addition, we uncovered a substantial nonoverlapping set of O-glycoproteins and O-glycosites using an alternative protease digestion (chymotrypsin).
23399548	7	18	theme	O-glycosites	1504:1515	arg1	set					1477:1479	a substantial nonoverlapping set	1448:1479	a substantial nonoverlapping set of O-glycoproteins and O-glycosites	1448:1515	In addition, we uncovered a substantial nonoverlapping set of O-glycoproteins and O-glycosites using an alternative protease digestion (chymotrypsin).
23399548	1	19	theme	GalNAc-type	118:128	arg1	challenge					168:176	a major challenge	160:176	a major challenge	160:176	Characterizing protein GalNAc-type O-glycosylation has long been a major challenge, and as a result, our understanding of this glycoproteome is particularly poor.
23399548	1	19	theme	GalNAc-type	118:128	arg1	O-glycosylation					130:144	Characterizing protein GalNAc-type O-glycosylation	95:144	Characterizing protein GalNAc-type O-glycosylation	95:144	Characterizing protein GalNAc-type O-glycosylation has long been a major challenge, and as a result, our understanding of this glycoproteome is particularly poor.
23399548	8	20	theme	glycoproteins	1629:1641	arg1	novel					1668:1672	novel	1668:1672	novel	1668:1672	In total, the improvements led to identification of 259 glycoproteins, of which 152 (59%) were novel compared with our previous strategy using the same three cell lines.
23399548	8	20	theme	glycoproteins	1629:1641	arg1	identification					1607:1620	identification	1607:1620	identification of 259 glycoproteins, of which 152 (59%) were novel compared with our previous strategy using the same three cell lines	1607:1740	In total, the improvements led to identification of 259 glycoproteins, of which 152 (59%) were novel compared with our previous strategy using the same three cell lines.
23399548	6	21	theme	substantial	1325:1335	arg1	improvements					1337:1348	further substantial improvements	1317:1348	further substantial improvements	1317:1348	We found that analysis of the secretome was an important independent factor for increasing identifications, suggesting that further substantial improvements can also be sought through analysis of subcellular organelle fractions.
23399548	0	22	theme	O-glycoproteome	61:75	arg1	mapping					28:34	mass spectrometric mapping	9:34	mass spectrometric mapping of the human GalNAc-type O-glycoproteome with SimpleCells	9:92	Enhanced mass spectrometric mapping of the human GalNAc-type O-glycoproteome with SimpleCells.
23399548	9	23	dep	glycosites	1770:1779	arg1	respect					1748:1754	respect	1748:1754	respect	1748:1754	With respect to individual glycosites, we identified a total of 856 sites, of which 508 (59%) were novel compared with our previous strategy; this includes four new identifications of O-GalNAc attached to tyrosine.
23399548	10	24	gly	O-glycosites	1990:2001	arg2	O-glycosites					1990:2001	≈ 220 O-glycosites	1984:2001	≈ 220 O-glycosites	1984:2001	Furthermore, we uncovered ≈ 220 O-glycosites wherein the peptides were clearly identified, but the glycosites could not be unambiguously assigned to specific positions.
23399548	4	25	theme	affinity	833:840	arg1	chromatography					842:855	lectin affinity chromatography	826:855	lectin affinity chromatography	826:855	Here, we demonstrate a substantial improvement in the SimpleCell strategy by including an additional stage of lectin affinity chromatography on secreted glycoproteins from culture media (secretome) and by incorporating pre-fractionation of affinity-enriched glycopeptides via IEF before nLC-MS/MS.
23399548	2	26	theme	novel	283:287	arg1	strategy					289:296	a novel strategy	281:296	a novel strategy for high throughput identification of O-GalNAc glycosites using zinc finger nuclease gene-engineered "SimpleCell" lines producing homogeneous truncated O-glycosylation	281:464	Recently, we presented a novel strategy for high throughput identification of O-GalNAc glycosites using zinc finger nuclease gene-engineered "SimpleCell" lines producing homogeneous truncated O-glycosylation.
23399548	11	27	theme	human	2215:2219	arg1	O-glycoproteome					2233:2247	the human GalNAc-type O-glycoproteome	2211:2247	the human GalNAc-type O-glycoproteome	2211:2247	The improved strategy should greatly facilitate high throughput characterization of the human GalNAc-type O-glycoproteome as well as be applicable to analysis of other O-glycoproteomes.
23399548	10	28	gly	glycosites	2057:2066	arg2	glycosites					2057:2066	the glycosites	2053:2066	the glycosites	2053:2066	Furthermore, we uncovered ≈ 220 O-glycosites wherein the peptides were clearly identified, but the glycosites could not be unambiguously assigned to specific positions.
23399548	4	29	theme	additional	806:815	arg1	stage					817:821	an additional stage	803:821	an additional stage of lectin affinity chromatography	803:855	Here, we demonstrate a substantial improvement in the SimpleCell strategy by including an additional stage of lectin affinity chromatography on secreted glycoproteins from culture media (secretome) and by incorporating pre-fractionation of affinity-enriched glycopeptides via IEF before nLC-MS/MS.
23399548	2	30	theme	SimpleCell	400:409	arg1	lines					412:416	zinc finger nuclease gene-engineered "SimpleCell" lines	362:416	zinc finger nuclease gene-engineered "SimpleCell" lines producing homogeneous truncated O-glycosylation	362:464	Recently, we presented a novel strategy for high throughput identification of O-GalNAc glycosites using zinc finger nuclease gene-engineered "SimpleCell" lines producing homogeneous truncated O-glycosylation.
23399548	1	31	theme	protein	110:116	arg1	challenge					168:176	a major challenge	160:176	a major challenge	160:176	Characterizing protein GalNAc-type O-glycosylation has long been a major challenge, and as a result, our understanding of this glycoproteome is particularly poor.
23399548	1	31	theme	protein	110:116	arg1	O-glycosylation					130:144	Characterizing protein GalNAc-type O-glycosylation	95:144	Characterizing protein GalNAc-type O-glycosylation	95:144	Characterizing protein GalNAc-type O-glycosylation has long been a major challenge, and as a result, our understanding of this glycoproteome is particularly poor.
23399548	7	32	theme	nonoverlapping	1462:1475	arg1	O-glycosites					1504:1515	O-glycosites	1504:1515	O-glycosites	1504:1515	In addition, we uncovered a substantial nonoverlapping set of O-glycoproteins and O-glycosites using an alternative protease digestion (chymotrypsin).
23399548	7	32	theme	nonoverlapping	1462:1475	arg1	O-glycoproteins					1484:1498	O-glycoproteins	1484:1498	O-glycoproteins	1484:1498	In addition, we uncovered a substantial nonoverlapping set of O-glycoproteins and O-glycosites using an alternative protease digestion (chymotrypsin).
23399548	7	32	theme	nonoverlapping	1462:1475	arg1	set					1477:1479	a substantial nonoverlapping set	1448:1479	a substantial nonoverlapping set of O-glycoproteins and O-glycosites	1448:1515	In addition, we uncovered a substantial nonoverlapping set of O-glycoproteins and O-glycosites using an alternative protease digestion (chymotrypsin).
23399548	7	33	theme	O-glycoproteins	1484:1498	arg1	O-glycosites					1504:1515	O-glycosites	1504:1515	O-glycosites	1504:1515	In addition, we uncovered a substantial nonoverlapping set of O-glycoproteins and O-glycosites using an alternative protease digestion (chymotrypsin).
23399548	7	33	theme	O-glycoproteins	1484:1498	arg1	O-glycoproteins					1484:1498	O-glycoproteins	1484:1498	O-glycoproteins	1484:1498	In addition, we uncovered a substantial nonoverlapping set of O-glycoproteins and O-glycosites using an alternative protease digestion (chymotrypsin).
23399548	7	33	theme	O-glycoproteins	1484:1498	arg1	set					1477:1479	a substantial nonoverlapping set	1448:1479	a substantial nonoverlapping set of O-glycoproteins and O-glycosites	1448:1515	In addition, we uncovered a substantial nonoverlapping set of O-glycoproteins and O-glycosites using an alternative protease digestion (chymotrypsin).
23399548	0	34	theme	spectrometric	14:26	arg1	mapping					28:34	mass spectrometric mapping	9:34	mass spectrometric mapping of the human GalNAc-type O-glycoproteome with SimpleCells	9:92	Enhanced mass spectrometric mapping of the human GalNAc-type O-glycoproteome with SimpleCells.
23399548	11	35	theme	O-glycoproteomes	2295:2310	arg1	analysis					2277:2284	analysis	2277:2284	analysis of other O-glycoproteomes	2277:2310	The improved strategy should greatly facilitate high throughput characterization of the human GalNAc-type O-glycoproteome as well as be applicable to analysis of other O-glycoproteomes.
23399548	2	36	theme	homogeneous	428:438	arg1	O-glycosylation					450:464	homogeneous truncated O-glycosylation	428:464	homogeneous truncated O-glycosylation	428:464	Recently, we presented a novel strategy for high throughput identification of O-GalNAc glycosites using zinc finger nuclease gene-engineered "SimpleCell" lines producing homogeneous truncated O-glycosylation.
23399548	3	37	theme	cells	484:488	arg1	lysates					473:479	Total lysates	467:479	Total lysates of cells	467:488	Total lysates of cells were trypsinized and subjected to lectin affinity chromatography enrichment, followed by identification of GalNAc O-glycopeptides by nLC-MS/MS, with electron transfer dissociation employed to specify sites of O-glycosylation.
23399548	4	38	gly	glycoproteins	869:881	arg1	glycoproteins					869:881	secreted glycoproteins	860:881	secreted glycoproteins from culture media (secretome)	860:912	Here, we demonstrate a substantial improvement in the SimpleCell strategy by including an additional stage of lectin affinity chromatography on secreted glycoproteins from culture media (secretome) and by incorporating pre-fractionation of affinity-enriched glycopeptides via IEF before nLC-MS/MS.
23399548	8	39	theme	previous	1692:1699	arg1	strategy					1701:1708	our previous strategy	1688:1708	our previous strategy using the same three cell lines	1688:1740	In total, the improvements led to identification of 259 glycoproteins, of which 152 (59%) were novel compared with our previous strategy using the same three cell lines.
23399548	2	40	gly	glycosites	345:354	arg2	glycosites					345:354	O-GalNAc glycosites	336:354	O-GalNAc glycosites using zinc finger nuclease gene-engineered "SimpleCell" lines producing homogeneous truncated O-glycosylation	336:464	Recently, we presented a novel strategy for high throughput identification of O-GalNAc glycosites using zinc finger nuclease gene-engineered "SimpleCell" lines producing homogeneous truncated O-glycosylation.
23399548	3	41	theme	O-glycosylation	699:713	arg1	O-glycosylation					699:713	O-glycosylation	699:713	O-glycosylation	699:713	Total lysates of cells were trypsinized and subjected to lectin affinity chromatography enrichment, followed by identification of GalNAc O-glycopeptides by nLC-MS/MS, with electron transfer dissociation employed to specify sites of O-glycosylation.
23399548	3	41	theme	O-glycosylation	699:713	arg1	sites					690:694	sites	690:694	sites of O-glycosylation	690:713	Total lysates of cells were trypsinized and subjected to lectin affinity chromatography enrichment, followed by identification of GalNAc O-glycopeptides by nLC-MS/MS, with electron transfer dissociation employed to specify sites of O-glycosylation.
23399548	3	42	theme	lectin	524:529	arg1	chromatography					540:553	lectin affinity chromatography	524:553	lectin affinity chromatography enrichment	524:564	Total lysates of cells were trypsinized and subjected to lectin affinity chromatography enrichment, followed by identification of GalNAc O-glycopeptides by nLC-MS/MS, with electron transfer dissociation employed to specify sites of O-glycosylation.
23399548	0	43	theme	human	43:47	arg1	O-glycoproteome					61:75	the human GalNAc-type O-glycoproteome	39:75	the human GalNAc-type O-glycoproteome	39:75	Enhanced mass spectrometric mapping of the human GalNAc-type O-glycoproteome with SimpleCells.
23399548	9	44	theme	O-GalNAc	1927:1934	arg1	identifications					1908:1922	four new identifications	1899:1922	four new identifications of O-GalNAc attached to tyrosine	1899:1955	With respect to individual glycosites, we identified a total of 856 sites, of which 508 (59%) were novel compared with our previous strategy; this includes four new identifications of O-GalNAc attached to tyrosine.
23399548	2	45	theme	O-GalNAc	336:343	arg1	glycosites					345:354	O-GalNAc glycosites	336:354	O-GalNAc glycosites using zinc finger nuclease gene-engineered "SimpleCell" lines producing homogeneous truncated O-glycosylation	336:464	Recently, we presented a novel strategy for high throughput identification of O-GalNAc glycosites using zinc finger nuclease gene-engineered "SimpleCell" lines producing homogeneous truncated O-glycosylation.
23399548	1	46	theme	glycoproteome	222:234	arg1	understanding					200:212	our understanding	196:212	our understanding of this glycoproteome	196:234	Characterizing protein GalNAc-type O-glycosylation has long been a major challenge, and as a result, our understanding of this glycoproteome is particularly poor.
23399548	4	47	dep	demonstrate	725:735	arg1	incorporating					921:933	incorporating	921:933	incorporating pre-fractionation of affinity-enriched glycopeptides via IEF before nLC-MS/MS	921:1011	Here, we demonstrate a substantial improvement in the SimpleCell strategy by including an additional stage of lectin affinity chromatography on secreted glycoproteins from culture media (secretome) and by incorporating pre-fractionation of affinity-enriched glycopeptides via IEF before nLC-MS/MS.
23399548	4	47	dep	demonstrate	725:735	arg1	including					793:801	including	793:801	including an additional stage of lectin affinity chromatography on secreted glycoproteins from culture media (secretome)	793:912	Here, we demonstrate a substantial improvement in the SimpleCell strategy by including an additional stage of lectin affinity chromatography on secreted glycoproteins from culture media (secretome) and by incorporating pre-fractionation of affinity-enriched glycopeptides via IEF before nLC-MS/MS.
23399548	6	48	theme	secretome	1223:1231	arg1	analysis					1207:1214	analysis	1207:1214	analysis of the secretome	1207:1231	We found that analysis of the secretome was an important independent factor for increasing identifications, suggesting that further substantial improvements can also be sought through analysis of subcellular organelle fractions.
23399548	6	48	theme	secretome	1223:1231	arg1	factor					1262:1267	an important independent factor	1237:1267	an important independent factor for increasing identifications	1237:1298	We found that analysis of the secretome was an important independent factor for increasing identifications, suggesting that further substantial improvements can also be sought through analysis of subcellular organelle fractions.
23399548	8	49	theme	same	1720:1723	arg1	lines					1736:1740	the same three cell lines	1716:1740	the same three cell lines	1716:1740	In total, the improvements led to identification of 259 glycoproteins, of which 152 (59%) were novel compared with our previous strategy using the same three cell lines.
23399548	4	50	theme	culture	888:894	arg1	secretome					903:911	secretome	903:911	secretome	903:911	Here, we demonstrate a substantial improvement in the SimpleCell strategy by including an additional stage of lectin affinity chromatography on secreted glycoproteins from culture media (secretome) and by incorporating pre-fractionation of affinity-enriched glycopeptides via IEF before nLC-MS/MS.
23399548	4	50	theme	culture	888:894	arg1	media					896:900	culture media	888:900	culture media (secretome)	888:912	Here, we demonstrate a substantial improvement in the SimpleCell strategy by including an additional stage of lectin affinity chromatography on secreted glycoproteins from culture media (secretome) and by incorporating pre-fractionation of affinity-enriched glycopeptides via IEF before nLC-MS/MS.
23399548	2	51	theme	gene-engineered	383:397	arg1	lines					412:416	zinc finger nuclease gene-engineered "SimpleCell" lines	362:416	zinc finger nuclease gene-engineered "SimpleCell" lines producing homogeneous truncated O-glycosylation	362:464	Recently, we presented a novel strategy for high throughput identification of O-GalNAc glycosites using zinc finger nuclease gene-engineered "SimpleCell" lines producing homogeneous truncated O-glycosylation.
23399548	5	52	theme	substantial	1110:1120	arg1	increase					1122:1129	a substantial increase	1108:1129	a substantial increase in the number of O-glycoproteins and O-glycosites identified	1108:1190	We applied these improvements to three human SimpleCells studied previously, and each yielded a substantial increase in the number of O-glycoproteins and O-glycosites identified.
23399548	5	53	gly	O-glycoproteins	1148:1162	arg1	O-glycoproteins					1148:1162	O-glycoproteins	1148:1162	O-glycoproteins	1148:1162	We applied these improvements to three human SimpleCells studied previously, and each yielded a substantial increase in the number of O-glycoproteins and O-glycosites identified.
23399548	8	54	theme	cell	1731:1734	arg1	lines					1736:1740	the same three cell lines	1716:1740	the same three cell lines	1716:1740	In total, the improvements led to identification of 259 glycoproteins, of which 152 (59%) were novel compared with our previous strategy using the same three cell lines.
23399548	2	55	theme	finger	367:372	arg1	lines					412:416	zinc finger nuclease gene-engineered "SimpleCell" lines	362:416	zinc finger nuclease gene-engineered "SimpleCell" lines producing homogeneous truncated O-glycosylation	362:464	Recently, we presented a novel strategy for high throughput identification of O-GalNAc glycosites using zinc finger nuclease gene-engineered "SimpleCell" lines producing homogeneous truncated O-glycosylation.
23399548	11	56	theme	GalNAc-type	2221:2231	arg1	O-glycoproteome					2233:2247	the human GalNAc-type O-glycoproteome	2211:2247	the human GalNAc-type O-glycoproteome	2211:2247	The improved strategy should greatly facilitate high throughput characterization of the human GalNAc-type O-glycoproteome as well as be applicable to analysis of other O-glycoproteomes.
23399548	5	57	gly	O-glycosites	1168:1179	arg2	O-glycosites					1168:1179	O-glycosites	1168:1179	O-glycosites	1168:1179	We applied these improvements to three human SimpleCells studied previously, and each yielded a substantial increase in the number of O-glycoproteins and O-glycosites identified.
23399548	4	58	theme	glycopeptides	974:986	arg1	pre-fractionation					935:951	pre-fractionation	935:951	pre-fractionation of affinity-enriched glycopeptides	935:986	Here, we demonstrate a substantial improvement in the SimpleCell strategy by including an additional stage of lectin affinity chromatography on secreted glycoproteins from culture media (secretome) and by incorporating pre-fractionation of affinity-enriched glycopeptides via IEF before nLC-MS/MS.
23399548	6	59	theme	organelle	1401:1409	arg1	fractions					1411:1419	subcellular organelle fractions	1389:1419	subcellular organelle fractions	1389:1419	We found that analysis of the secretome was an important independent factor for increasing identifications, suggesting that further substantial improvements can also be sought through analysis of subcellular organelle fractions.
23399548	4	60	gly	glycopeptides	974:986	arg2	glycopeptides					974:986	affinity-enriched glycopeptides	956:986	affinity-enriched glycopeptides	956:986	Here, we demonstrate a substantial improvement in the SimpleCell strategy by including an additional stage of lectin affinity chromatography on secreted glycoproteins from culture media (secretome) and by incorporating pre-fractionation of affinity-enriched glycopeptides via IEF before nLC-MS/MS.
23399548	7	61	gly	O-glycosites	1504:1515	arg2	O-glycosites					1504:1515	O-glycosites	1504:1515	O-glycosites	1504:1515	In addition, we uncovered a substantial nonoverlapping set of O-glycoproteins and O-glycosites using an alternative protease digestion (chymotrypsin).
23399548	2	62	theme	high	302:305	arg1	identification					318:331	high throughput identification	302:331	high throughput identification of O-GalNAc glycosites using zinc finger nuclease gene-engineered "SimpleCell" lines producing homogeneous truncated O-glycosylation	302:464	Recently, we presented a novel strategy for high throughput identification of O-GalNAc glycosites using zinc finger nuclease gene-engineered "SimpleCell" lines producing homogeneous truncated O-glycosylation.
23399548	7	63	gly	O-glycoproteins	1484:1498	arg1	O-glycoproteins					1484:1498	O-glycoproteins	1484:1498	O-glycoproteins	1484:1498	In addition, we uncovered a substantial nonoverlapping set of O-glycoproteins and O-glycosites using an alternative protease digestion (chymotrypsin).
23399548	9	64	theme	sites	1811:1815	arg1	total					1798:1802	a total	1796:1802	a total	1796:1802	With respect to individual glycosites, we identified a total of 856 sites, of which 508 (59%) were novel compared with our previous strategy; this includes four new identifications of O-GalNAc attached to tyrosine.
23399548	6	65	theme	independent	1250:1260	arg1	factor					1262:1267	an important independent factor	1237:1267	an important independent factor for increasing identifications	1237:1298	We found that analysis of the secretome was an important independent factor for increasing identifications, suggesting that further substantial improvements can also be sought through analysis of subcellular organelle fractions.
23399548	6	65	theme	independent	1250:1260	arg1	analysis					1207:1214	analysis	1207:1214	analysis of the secretome	1207:1231	We found that analysis of the secretome was an important independent factor for increasing identifications, suggesting that further substantial improvements can also be sought through analysis of subcellular organelle fractions.
23399548	3	66	theme	chromatography	540:553	arg1	enrichment					555:564	lectin affinity chromatography enrichment	524:564	lectin affinity chromatography enrichment	524:564	Total lysates of cells were trypsinized and subjected to lectin affinity chromatography enrichment, followed by identification of GalNAc O-glycopeptides by nLC-MS/MS, with electron transfer dissociation employed to specify sites of O-glycosylation.
23399548	2	67	theme	glycosites	345:354	arg1	identification					318:331	high throughput identification	302:331	high throughput identification of O-GalNAc glycosites using zinc finger nuclease gene-engineered "SimpleCell" lines producing homogeneous truncated O-glycosylation	302:464	Recently, we presented a novel strategy for high throughput identification of O-GalNAc glycosites using zinc finger nuclease gene-engineered "SimpleCell" lines producing homogeneous truncated O-glycosylation.
23399548	3	68	theme	transfer	648:655	arg1	dissociation					657:668	electron transfer dissociation	639:668	electron transfer dissociation employed to specify sites of O-glycosylation	639:713	Total lysates of cells were trypsinized and subjected to lectin affinity chromatography enrichment, followed by identification of GalNAc O-glycopeptides by nLC-MS/MS, with electron transfer dissociation employed to specify sites of O-glycosylation.
23399548	8	69	gly	glycoproteins	1629:1641	arg1	glycoproteins					1629:1641	259 glycoproteins	1625:1641	259 glycoproteins	1625:1641	In total, the improvements led to identification of 259 glycoproteins, of which 152 (59%) were novel compared with our previous strategy using the same three cell lines.
23399548	7	70	theme	alternative	1526:1536	arg1	chymotrypsin					1558:1569	chymotrypsin	1558:1569	chymotrypsin	1558:1569	In addition, we uncovered a substantial nonoverlapping set of O-glycoproteins and O-glycosites using an alternative protease digestion (chymotrypsin).
23399548	7	70	theme	alternative	1526:1536	arg1	digestion					1547:1555	an alternative protease digestion	1523:1555	an alternative protease digestion (chymotrypsin)	1523:1570	In addition, we uncovered a substantial nonoverlapping set of O-glycoproteins and O-glycosites using an alternative protease digestion (chymotrypsin).
23399548	4	71	theme	SimpleCell	770:779	arg1	strategy					781:788	the SimpleCell strategy	766:788	the SimpleCell strategy	766:788	Here, we demonstrate a substantial improvement in the SimpleCell strategy by including an additional stage of lectin affinity chromatography on secreted glycoproteins from culture media (secretome) and by incorporating pre-fractionation of affinity-enriched glycopeptides via IEF before nLC-MS/MS.
23399548	5	72	theme	O-glycoproteins	1148:1162	arg1	number					1138:1143	the number	1134:1143	the number of O-glycoproteins and O-glycosites identified	1134:1190	We applied these improvements to three human SimpleCells studied previously, and each yielded a substantial increase in the number of O-glycoproteins and O-glycosites identified.
23399548	4	73	from	media	896:900	arg1	glycoproteins					869:881	secreted glycoproteins	860:881	secreted glycoproteins from culture media (secretome)	860:912	Here, we demonstrate a substantial improvement in the SimpleCell strategy by including an additional stage of lectin affinity chromatography on secreted glycoproteins from culture media (secretome) and by incorporating pre-fractionation of affinity-enriched glycopeptides via IEF before nLC-MS/MS.
23399548	3	74	theme	O-glycopeptides	604:618	arg1	identification					579:592	identification	579:592	identification of GalNAc O-glycopeptides	579:618	Total lysates of cells were trypsinized and subjected to lectin affinity chromatography enrichment, followed by identification of GalNAc O-glycopeptides by nLC-MS/MS, with electron transfer dissociation employed to specify sites of O-glycosylation.
23399548	11	75	theme	high	2175:2178	arg1	throughput					2180:2189	high throughput	2175:2189	high throughput characterization of the human GalNAc-type O-glycoproteome	2175:2247	The improved strategy should greatly facilitate high throughput characterization of the human GalNAc-type O-glycoproteome as well as be applicable to analysis of other O-glycoproteomes.
23399548	3	76	gly	O-glycopeptides	604:618	arg2	O-glycopeptides					604:618	GalNAc O-glycopeptides	597:618	GalNAc O-glycopeptides	597:618	Total lysates of cells were trypsinized and subjected to lectin affinity chromatography enrichment, followed by identification of GalNAc O-glycopeptides by nLC-MS/MS, with electron transfer dissociation employed to specify sites of O-glycosylation.
23399548	5	77	theme	O-glycosites	1168:1179	arg1	number					1138:1143	the number	1134:1143	the number of O-glycoproteins and O-glycosites identified	1134:1190	We applied these improvements to three human SimpleCells studied previously, and each yielded a substantial increase in the number of O-glycoproteins and O-glycosites identified.
23399548	1	78	theme	major	162:166	arg1	challenge					168:176	a major challenge	160:176	a major challenge	160:176	Characterizing protein GalNAc-type O-glycosylation has long been a major challenge, and as a result, our understanding of this glycoproteome is particularly poor.
23399548	1	78	theme	major	162:166	arg1	O-glycosylation					130:144	Characterizing protein GalNAc-type O-glycosylation	95:144	Characterizing protein GalNAc-type O-glycosylation	95:144	Characterizing protein GalNAc-type O-glycosylation has long been a major challenge, and as a result, our understanding of this glycoproteome is particularly poor.
23399548	6	79	theme	further	1317:1323	arg1	improvements					1337:1348	further substantial improvements	1317:1348	further substantial improvements	1317:1348	We found that analysis of the secretome was an important independent factor for increasing identifications, suggesting that further substantial improvements can also be sought through analysis of subcellular organelle fractions.
23399548	4	80	theme	substantial	739:749	arg1	improvement					751:761	a substantial improvement	737:761	a substantial improvement in the SimpleCell strategy	737:788	Here, we demonstrate a substantial improvement in the SimpleCell strategy by including an additional stage of lectin affinity chromatography on secreted glycoproteins from culture media (secretome) and by incorporating pre-fractionation of affinity-enriched glycopeptides via IEF before nLC-MS/MS.
23399548	4	81	theme	lectin	826:831	arg1	chromatography					842:855	lectin affinity chromatography	826:855	lectin affinity chromatography	826:855	Here, we demonstrate a substantial improvement in the SimpleCell strategy by including an additional stage of lectin affinity chromatography on secreted glycoproteins from culture media (secretome) and by incorporating pre-fractionation of affinity-enriched glycopeptides via IEF before nLC-MS/MS.
23399548	10	82	theme	specific	2107:2114	arg1	positions					2116:2124	specific positions	2107:2124	specific positions	2107:2124	Furthermore, we uncovered ≈ 220 O-glycosites wherein the peptides were clearly identified, but the glycosites could not be unambiguously assigned to specific positions.
23399548	9	83	theme	previous	1866:1873	arg1	strategy					1875:1882	our previous strategy	1862:1882	our previous strategy	1862:1882	With respect to individual glycosites, we identified a total of 856 sites, of which 508 (59%) were novel compared with our previous strategy; this includes four new identifications of O-GalNAc attached to tyrosine.
23399548	4	84	theme	chromatography	842:855	arg1	stage					817:821	an additional stage	803:821	an additional stage of lectin affinity chromatography	803:855	Here, we demonstrate a substantial improvement in the SimpleCell strategy by including an additional stage of lectin affinity chromatography on secreted glycoproteins from culture media (secretome) and by incorporating pre-fractionation of affinity-enriched glycopeptides via IEF before nLC-MS/MS.
23399548	2	85	theme	"	410:410	arg1	lines					412:416	zinc finger nuclease gene-engineered "SimpleCell" lines	362:416	zinc finger nuclease gene-engineered "SimpleCell" lines producing homogeneous truncated O-glycosylation	362:464	Recently, we presented a novel strategy for high throughput identification of O-GalNAc glycosites using zinc finger nuclease gene-engineered "SimpleCell" lines producing homogeneous truncated O-glycosylation.
23399548	0	86	theme	mass	9:12	arg1	mapping					28:34	mass spectrometric mapping	9:34	mass spectrometric mapping of the human GalNAc-type O-glycoproteome with SimpleCells	9:92	Enhanced mass spectrometric mapping of the human GalNAc-type O-glycoproteome with SimpleCells.
23399548	1	87	theme	Characterizing	95:108	arg1	challenge					168:176	a major challenge	160:176	a major challenge	160:176	Characterizing protein GalNAc-type O-glycosylation has long been a major challenge, and as a result, our understanding of this glycoproteome is particularly poor.
23399548	1	87	theme	Characterizing	95:108	arg1	O-glycosylation					130:144	Characterizing protein GalNAc-type O-glycosylation	95:144	Characterizing protein GalNAc-type O-glycosylation	95:144	Characterizing protein GalNAc-type O-glycosylation has long been a major challenge, and as a result, our understanding of this glycoproteome is particularly poor.
23399548	7	88	theme	substantial	1450:1460	arg1	O-glycosites					1504:1515	O-glycosites	1504:1515	O-glycosites	1504:1515	In addition, we uncovered a substantial nonoverlapping set of O-glycoproteins and O-glycosites using an alternative protease digestion (chymotrypsin).
23399548	7	88	theme	substantial	1450:1460	arg1	O-glycoproteins					1484:1498	O-glycoproteins	1484:1498	O-glycoproteins	1484:1498	In addition, we uncovered a substantial nonoverlapping set of O-glycoproteins and O-glycosites using an alternative protease digestion (chymotrypsin).
23399548	7	88	theme	substantial	1450:1460	arg1	set					1477:1479	a substantial nonoverlapping set	1448:1479	a substantial nonoverlapping set of O-glycoproteins and O-glycosites	1448:1515	In addition, we uncovered a substantial nonoverlapping set of O-glycoproteins and O-glycosites using an alternative protease digestion (chymotrypsin).
23399548	10	89	dep	uncovered	1974:1982	arg1	wherein					2003:2009	wherein	2003:2009	wherein the peptides were clearly identified, but the glycosites could not be unambiguously assigned to specific positions	2003:2124	Furthermore, we uncovered ≈ 220 O-glycosites wherein the peptides were clearly identified, but the glycosites could not be unambiguously assigned to specific positions.
23399548	3	90	theme	Total	467:471	arg1	lysates					473:479	Total lysates	467:479	Total lysates of cells	467:488	Total lysates of cells were trypsinized and subjected to lectin affinity chromatography enrichment, followed by identification of GalNAc O-glycopeptides by nLC-MS/MS, with electron transfer dissociation employed to specify sites of O-glycosylation.
23399548	5	91	theme	human	1053:1057	arg1	SimpleCells					1059:1069	three human SimpleCells	1047:1069	three human SimpleCells studied previously	1047:1088	We applied these improvements to three human SimpleCells studied previously, and each yielded a substantial increase in the number of O-glycoproteins and O-glycosites identified.
23399548	9	92	attach	attached	1936:1943	arg2	O-GalNAc					1927:1934	O-GalNAc	1927:1934	O-GalNAc attached to tyrosine	1927:1955	With respect to individual glycosites, we identified a total of 856 sites, of which 508 (59%) were novel compared with our previous strategy; this includes four new identifications of O-GalNAc attached to tyrosine.
23399548	9	92	attach	attached	1936:1943	arg1	tyrosine					1948:1955	tyrosine	1948:1955	tyrosine	1948:1955	With respect to individual glycosites, we identified a total of 856 sites, of which 508 (59%) were novel compared with our previous strategy; this includes four new identifications of O-GalNAc attached to tyrosine.
23399548	2	93	theme	truncated	440:448	arg1	O-glycosylation					450:464	homogeneous truncated O-glycosylation	428:464	homogeneous truncated O-glycosylation	428:464	Recently, we presented a novel strategy for high throughput identification of O-GalNAc glycosites using zinc finger nuclease gene-engineered "SimpleCell" lines producing homogeneous truncated O-glycosylation.
23399548	9	94	theme	new	1904:1906	arg1	identifications					1908:1922	four new identifications	1899:1922	four new identifications of O-GalNAc attached to tyrosine	1899:1955	With respect to individual glycosites, we identified a total of 856 sites, of which 508 (59%) were novel compared with our previous strategy; this includes four new identifications of O-GalNAc attached to tyrosine.
23399548	0	95	with	mapping	28:34	arg1	SimpleCells					82:92	SimpleCells	82:92	SimpleCells	82:92	Enhanced mass spectrometric mapping of the human GalNAc-type O-glycoproteome with SimpleCells.
23399548	0	96	theme	GalNAc-type	49:59	arg1	O-glycoproteome					61:75	the human GalNAc-type O-glycoproteome	39:75	the human GalNAc-type O-glycoproteome	39:75	Enhanced mass spectrometric mapping of the human GalNAc-type O-glycoproteome with SimpleCells.
23399548	6	97	theme	important	1240:1248	arg1	factor					1262:1267	an important independent factor	1237:1267	an important independent factor for increasing identifications	1237:1298	We found that analysis of the secretome was an important independent factor for increasing identifications, suggesting that further substantial improvements can also be sought through analysis of subcellular organelle fractions.
23399548	6	97	theme	important	1240:1248	arg1	analysis					1207:1214	analysis	1207:1214	analysis of the secretome	1207:1231	We found that analysis of the secretome was an important independent factor for increasing identifications, suggesting that further substantial improvements can also be sought through analysis of subcellular organelle fractions.
23399548	11	98	theme	other	2289:2293	arg1	O-glycoproteomes					2295:2310	other O-glycoproteomes	2289:2310	other O-glycoproteomes	2289:2310	The improved strategy should greatly facilitate high throughput characterization of the human GalNAc-type O-glycoproteome as well as be applicable to analysis of other O-glycoproteomes.
23399548	3	99	theme	affinity	531:538	arg1	chromatography					540:553	lectin affinity chromatography	524:553	lectin affinity chromatography enrichment	524:564	Total lysates of cells were trypsinized and subjected to lectin affinity chromatography enrichment, followed by identification of GalNAc O-glycopeptides by nLC-MS/MS, with electron transfer dissociation employed to specify sites of O-glycosylation.
23399548	9	100	gly	glycosites	1770:1779	arg2	glycosites					1770:1779	individual glycosites	1759:1779	individual glycosites	1759:1779	With respect to individual glycosites, we identified a total of 856 sites, of which 508 (59%) were novel compared with our previous strategy; this includes four new identifications of O-GalNAc attached to tyrosine.
23399548	4	101	theme	secreted	860:867	arg1	glycoproteins					869:881	secreted glycoproteins	860:881	secreted glycoproteins from culture media (secretome)	860:912	Here, we demonstrate a substantial improvement in the SimpleCell strategy by including an additional stage of lectin affinity chromatography on secreted glycoproteins from culture media (secretome) and by incorporating pre-fractionation of affinity-enriched glycopeptides via IEF before nLC-MS/MS.
23399548	2	102	theme	nuclease	374:381	arg1	lines					412:416	zinc finger nuclease gene-engineered "SimpleCell" lines	362:416	zinc finger nuclease gene-engineered "SimpleCell" lines producing homogeneous truncated O-glycosylation	362:464	Recently, we presented a novel strategy for high throughput identification of O-GalNAc glycosites using zinc finger nuclease gene-engineered "SimpleCell" lines producing homogeneous truncated O-glycosylation.
17960739	4	0	from	conversion	565:574	arg1	unit					599:602	1 mass unit	592:602	1 mass unit	592:602	After immunoprecipitation, CD9P-1 was subjected to enzymatic PNGase F cleavage of N-glycans, resulting in Asn to Asp conversion and increase in 1 mass unit.
17960739	8	1	theme	complex	1120:1126	arg1	structures					1150:1159	complex and high mannose-type structures	1120:1159	complex and high mannose-type structures	1120:1159	CD9P-1 was shown to exhibit more than 40 different N-glycans, essentially composed of complex and high mannose-type structures.
17960739	1	2	from	interactions	149:160	arg1	membrane					176:183	the plasma membrane	165:183	the plasma membrane	165:183	The membrane protein CD9P-1 is a major component of the tetraspanin web, a network of molecular interactions in the plasma membrane, in which it specifically associates with tetraspanins CD9 and CD81.
17960739	5	3	gly	deglycosylated	641:654	arg1	peptides					656:663	deglycosylated peptides	641:663	deglycosylated peptides	641:663	Thus, following protease digestion, deglycosylated peptides were selectively identified by high mass accuracy FTICR-MS, using this conversion as a signature.
17960739	7	4	theme	GC-MS	1018:1022	arg1	analysis					1024:1031	GC-MS analysis	1018:1031	GC-MS analysis	1018:1031	On the other hand, the N-glycan structures were determined combining chemical derivatization and exoglycosidase digestions followed by MALDI-TOF MS, ESI-MS/MS, and GC-MS analysis.
17960739	9	5	theme	isoforms	1261:1268	arg1	presence					1224:1231	the presence	1220:1231	the presence of at least 17 glycosylated isoforms of CD9P-1 at cell surface	1220:1294	Finally, 2-D PAGE and lectino-blot analyses have revealed the presence of at least 17 glycosylated isoforms of CD9P-1 at cell surface.
17960739	10	6	theme	tetraspanin	1409:1419	arg1	web					1421:1423	the tetraspanin web	1405:1423	the tetraspanin web	1405:1423	All CD9P-1 isoforms associate with CD9 leading to additional level of complexity of this primary complex in the tetraspanin web.
17960739	1	7	from	network	128:134	arg1	membrane					176:183	the plasma membrane	165:183	the plasma membrane	165:183	The membrane protein CD9P-1 is a major component of the tetraspanin web, a network of molecular interactions in the plasma membrane, in which it specifically associates with tetraspanins CD9 and CD81.
17960739	6	8	theme	N-glycosylation	809:823	arg1	sites					825:829	all nine potential N-glycosylation sites	790:829	all nine potential N-glycosylation sites	790:829	This has demonstrated that all nine potential N-glycosylation sites were actually engaged.
17960739	8	9	theme	high	1132:1135	arg1	structures					1150:1159	complex and high mannose-type structures	1120:1159	complex and high mannose-type structures	1120:1159	CD9P-1 was shown to exhibit more than 40 different N-glycans, essentially composed of complex and high mannose-type structures.
17960739	9	10	theme	CD9P-1	1273:1278	arg1	isoforms					1261:1268	at least 17 glycosylated isoforms	1236:1268	at least 17 glycosylated isoforms of CD9P-1	1236:1278	Finally, 2-D PAGE and lectino-blot analyses have revealed the presence of at least 17 glycosylated isoforms of CD9P-1 at cell surface.
17960739	10	11	theme	additional	1347:1356	arg1	level					1358:1362	additional level	1347:1362	additional level of complexity of this primary complex in the tetraspanin web	1347:1423	All CD9P-1 isoforms associate with CD9 leading to additional level of complexity of this primary complex in the tetraspanin web.
17960739	2	12	theme	various	258:264	arg1	effects					277:283	The various functional effects	254:283	The various functional effects of CD9 and CD81	254:299	The various functional effects of CD9 and CD81 may be related to their partners.
17960739	2	12	theme	various	258:264	arg1	related					308:314	related	308:314	related	308:314	The various functional effects of CD9 and CD81 may be related to their partners.
17960739	5	13	theme	high	696:699	arg1	accuracy					706:713	high mass accuracy	696:713	high mass accuracy FTICR-MS	696:722	Thus, following protease digestion, deglycosylated peptides were selectively identified by high mass accuracy FTICR-MS, using this conversion as a signature.
17960739	8	14	theme	different	1075:1083	arg1	N-glycans					1085:1093	more than 40 different N-glycans	1062:1093	more than 40 different N-glycans	1062:1093	CD9P-1 was shown to exhibit more than 40 different N-glycans, essentially composed of complex and high mannose-type structures.
17960739	1	15	theme	membrane	57:64	arg1	CD9P-1					74:79	The membrane protein CD9P-1	53:79	The membrane protein CD9P-1	53:79	The membrane protein CD9P-1 is a major component of the tetraspanin web, a network of molecular interactions in the plasma membrane, in which it specifically associates with tetraspanins CD9 and CD81.
17960739	1	15	theme	membrane	57:64	arg1	component					92:100	a major component	84:100	a major component of the tetraspanin web	84:123	The membrane protein CD9P-1 is a major component of the tetraspanin web, a network of molecular interactions in the plasma membrane, in which it specifically associates with tetraspanins CD9 and CD81.
17960739	5	16	theme	mass	701:704	arg1	accuracy					706:713	high mass accuracy	696:713	high mass accuracy FTICR-MS	696:722	Thus, following protease digestion, deglycosylated peptides were selectively identified by high mass accuracy FTICR-MS, using this conversion as a signature.
17960739	9	17	theme	cell	1283:1286	arg1	surface					1288:1294	cell surface	1283:1294	cell surface	1283:1294	Finally, 2-D PAGE and lectino-blot analyses have revealed the presence of at least 17 glycosylated isoforms of CD9P-1 at cell surface.
17960739	7	18	theme	chemical	923:930	arg1	derivatization					932:945	chemical derivatization	923:945	chemical derivatization	923:945	On the other hand, the N-glycan structures were determined combining chemical derivatization and exoglycosidase digestions followed by MALDI-TOF MS, ESI-MS/MS, and GC-MS analysis.
17960739	1	19	theme	protein	66:72	arg1	CD9P-1					74:79	The membrane protein CD9P-1	53:79	The membrane protein CD9P-1	53:79	The membrane protein CD9P-1 is a major component of the tetraspanin web, a network of molecular interactions in the plasma membrane, in which it specifically associates with tetraspanins CD9 and CD81.
17960739	1	19	theme	protein	66:72	arg1	component					92:100	a major component	84:100	a major component of the tetraspanin web	84:123	The membrane protein CD9P-1 is a major component of the tetraspanin web, a network of molecular interactions in the plasma membrane, in which it specifically associates with tetraspanins CD9 and CD81.
17960739	9	20	attach	presence	1224:1231	arg1	surface					1288:1294	cell surface	1283:1294	cell surface	1283:1294	Finally, 2-D PAGE and lectino-blot analyses have revealed the presence of at least 17 glycosylated isoforms of CD9P-1 at cell surface.
17960739	9	20	attach	presence	1224:1231	arg2	isoforms					1261:1268	at least 17 glycosylated isoforms	1236:1268	at least 17 glycosylated isoforms of CD9P-1	1236:1278	Finally, 2-D PAGE and lectino-blot analyses have revealed the presence of at least 17 glycosylated isoforms of CD9P-1 at cell surface.
17960739	1	21	theme	molecular	139:147	arg1	interactions					149:160	molecular interactions	139:160	molecular interactions	139:160	The membrane protein CD9P-1 is a major component of the tetraspanin web, a network of molecular interactions in the plasma membrane, in which it specifically associates with tetraspanins CD9 and CD81.
17960739	5	22	theme	accuracy	706:713	arg1	FTICR-MS					715:722	high mass accuracy FTICR-MS	696:722	high mass accuracy FTICR-MS	696:722	Thus, following protease digestion, deglycosylated peptides were selectively identified by high mass accuracy FTICR-MS, using this conversion as a signature.
17960739	9	23	theme	PAGE	1175:1178	arg1	analyses					1197:1204	2-D PAGE and lectino-blot analyses	1171:1204	2-D PAGE and lectino-blot analyses	1171:1204	Finally, 2-D PAGE and lectino-blot analyses have revealed the presence of at least 17 glycosylated isoforms of CD9P-1 at cell surface.
17960739	4	24	theme	Asp	561:563	arg1	conversion					565:574	Asp conversion	561:574	Asp conversion	561:574	After immunoprecipitation, CD9P-1 was subjected to enzymatic PNGase F cleavage of N-glycans, resulting in Asn to Asp conversion and increase in 1 mass unit.
17960739	1	25	theme	interactions	149:160	arg1	network					128:134	a network	126:134	a network of molecular interactions in the plasma membrane, in which it specifically associates with tetraspanins CD9 and CD81	126:251	The membrane protein CD9P-1 is a major component of the tetraspanin web, a network of molecular interactions in the plasma membrane, in which it specifically associates with tetraspanins CD9 and CD81.
17960739	1	25	theme	interactions	149:160	arg1	component					92:100	a major component	84:100	a major component of the tetraspanin web	84:123	The membrane protein CD9P-1 is a major component of the tetraspanin web, a network of molecular interactions in the plasma membrane, in which it specifically associates with tetraspanins CD9 and CD81.
17960739	9	26	from	surface	1288:1294	arg1	presence					1224:1231	the presence	1220:1231	the presence of at least 17 glycosylated isoforms of CD9P-1 at cell surface	1220:1294	Finally, 2-D PAGE and lectino-blot analyses have revealed the presence of at least 17 glycosylated isoforms of CD9P-1 at cell surface.
17960739	10	27	theme	primary	1386:1392	arg1	complex					1394:1400	this primary complex	1381:1400	this primary complex	1381:1400	All CD9P-1 isoforms associate with CD9 leading to additional level of complexity of this primary complex in the tetraspanin web.
17960739	2	28	theme	CD9	288:290	arg1	effects					277:283	The various functional effects	254:283	The various functional effects of CD9 and CD81	254:299	The various functional effects of CD9 and CD81 may be related to their partners.
17960739	2	28	theme	CD9	288:290	arg1	related					308:314	related	308:314	related	308:314	The various functional effects of CD9 and CD81 may be related to their partners.
17960739	0	29	theme	Glycosylation	0:12	arg1	status					14:19	Glycosylation status	0:19	Glycosylation status of the membrane protein CD9P-1	0:50	Glycosylation status of the membrane protein CD9P-1.
17960739	7	30	theme	N-glycan	877:884	arg1	structures					886:895	the N-glycan structures	873:895	the N-glycan structures	873:895	On the other hand, the N-glycan structures were determined combining chemical derivatization and exoglycosidase digestions followed by MALDI-TOF MS, ESI-MS/MS, and GC-MS analysis.
17960739	10	31	from	complexity	1367:1376	arg1	web					1421:1423	the tetraspanin web	1405:1423	the tetraspanin web	1405:1423	All CD9P-1 isoforms associate with CD9 leading to additional level of complexity of this primary complex in the tetraspanin web.
17960739	8	32	theme	mannose-type	1137:1148	arg1	structures					1150:1159	complex and high mannose-type structures	1120:1159	complex and high mannose-type structures	1120:1159	CD9P-1 was shown to exhibit more than 40 different N-glycans, essentially composed of complex and high mannose-type structures.
17960739	9	33	theme	2-D	1171:1173	arg1	PAGE					1175:1178	2-D PAGE	1171:1178	2-D PAGE	1171:1178	Finally, 2-D PAGE and lectino-blot analyses have revealed the presence of at least 17 glycosylated isoforms of CD9P-1 at cell surface.
17960739	1	34	theme	major	86:90	arg1	CD9P-1					74:79	The membrane protein CD9P-1	53:79	The membrane protein CD9P-1	53:79	The membrane protein CD9P-1 is a major component of the tetraspanin web, a network of molecular interactions in the plasma membrane, in which it specifically associates with tetraspanins CD9 and CD81.
17960739	1	34	theme	major	86:90	arg1	network					128:134	a network	126:134	a network of molecular interactions in the plasma membrane, in which it specifically associates with tetraspanins CD9 and CD81	126:251	The membrane protein CD9P-1 is a major component of the tetraspanin web, a network of molecular interactions in the plasma membrane, in which it specifically associates with tetraspanins CD9 and CD81.
17960739	1	34	theme	major	86:90	arg1	component					92:100	a major component	84:100	a major component of the tetraspanin web	84:123	The membrane protein CD9P-1 is a major component of the tetraspanin web, a network of molecular interactions in the plasma membrane, in which it specifically associates with tetraspanins CD9 and CD81.
17960739	10	35	theme	complexity	1367:1376	arg1	level					1358:1362	additional level	1347:1362	additional level of complexity of this primary complex in the tetraspanin web	1347:1423	All CD9P-1 isoforms associate with CD9 leading to additional level of complexity of this primary complex in the tetraspanin web.
17960739	1	36	theme	plasma	169:174	arg1	membrane					176:183	the plasma membrane	165:183	the plasma membrane	165:183	The membrane protein CD9P-1 is a major component of the tetraspanin web, a network of molecular interactions in the plasma membrane, in which it specifically associates with tetraspanins CD9 and CD81.
17960739	9	37	theme	lectino-blot	1184:1195	arg1	analyses					1197:1204	2-D PAGE and lectino-blot analyses	1171:1204	2-D PAGE and lectino-blot analyses	1171:1204	Finally, 2-D PAGE and lectino-blot analyses have revealed the presence of at least 17 glycosylated isoforms of CD9P-1 at cell surface.
17960739	10	38	from	web	1421:1423	arg1	level					1358:1362	additional level	1347:1362	additional level of complexity of this primary complex in the tetraspanin web	1347:1423	All CD9P-1 isoforms associate with CD9 leading to additional level of complexity of this primary complex in the tetraspanin web.
17960739	10	39	theme	CD9P-1	1301:1306	arg1	isoforms					1308:1315	All CD9P-1 isoforms	1297:1315	All CD9P-1 isoforms	1297:1315	All CD9P-1 isoforms associate with CD9 leading to additional level of complexity of this primary complex in the tetraspanin web.
17960739	2	40	theme	functional	266:275	arg1	effects					277:283	The various functional effects	254:283	The various functional effects of CD9 and CD81	254:299	The various functional effects of CD9 and CD81 may be related to their partners.
17960739	2	40	theme	functional	266:275	arg1	related					308:314	related	308:314	related	308:314	The various functional effects of CD9 and CD81 may be related to their partners.
17960739	6	41	gly	N-glycosylation	809:823	arg2	sites					825:829	all nine potential N-glycosylation sites	790:829	all nine potential N-glycosylation sites	790:829	This has demonstrated that all nine potential N-glycosylation sites were actually engaged.
17960739	6	41	gly	N-glycosylation	809:823	arg2	nine					794:797	nine	794:797	nine	794:797	This has demonstrated that all nine potential N-glycosylation sites were actually engaged.
17960739	3	42	theme	HEK-293	433:439	arg1	cells					441:445	stably transfected HEK-293 cells	414:445	stably transfected HEK-293 cells	414:445	Thus, we have addressed the characterization of the CD9P-1 glycosylation using stably transfected HEK-293 cells.
17960739	0	43	theme	protein	37:43	arg1	CD9P-1					45:50	the membrane protein CD9P-1	24:50	the membrane protein CD9P-1	24:50	Glycosylation status of the membrane protein CD9P-1.
17960739	4	44	theme	N-glycans	530:538	arg1	cleavage					518:525	enzymatic PNGase F cleavage	499:525	enzymatic PNGase F cleavage of N-glycans	499:538	After immunoprecipitation, CD9P-1 was subjected to enzymatic PNGase F cleavage of N-glycans, resulting in Asn to Asp conversion and increase in 1 mass unit.
17960739	0	45	theme	membrane	28:35	arg1	CD9P-1					45:50	the membrane protein CD9P-1	24:50	the membrane protein CD9P-1	24:50	Glycosylation status of the membrane protein CD9P-1.
17960739	4	46	theme	enzymatic	499:507	arg1	F					516:516	enzymatic PNGase F	499:516	enzymatic PNGase F cleavage of N-glycans	499:538	After immunoprecipitation, CD9P-1 was subjected to enzymatic PNGase F cleavage of N-glycans, resulting in Asn to Asp conversion and increase in 1 mass unit.
17960739	4	47	theme	mass	594:597	arg1	unit					599:602	1 mass unit	592:602	1 mass unit	592:602	After immunoprecipitation, CD9P-1 was subjected to enzymatic PNGase F cleavage of N-glycans, resulting in Asn to Asp conversion and increase in 1 mass unit.
17960739	5	48	theme	protease	621:628	arg1	digestion					630:638	protease digestion	621:638	protease digestion	621:638	Thus, following protease digestion, deglycosylated peptides were selectively identified by high mass accuracy FTICR-MS, using this conversion as a signature.
17960739	3	49	theme	CD9P-1	387:392	arg1	glycosylation					394:406	the CD9P-1 glycosylation	383:406	the CD9P-1 glycosylation	383:406	Thus, we have addressed the characterization of the CD9P-1 glycosylation using stably transfected HEK-293 cells.
17960739	10	50	from	level	1358:1362	arg1	web					1421:1423	the tetraspanin web	1405:1423	the tetraspanin web	1405:1423	All CD9P-1 isoforms associate with CD9 leading to additional level of complexity of this primary complex in the tetraspanin web.
17960739	0	51	theme	CD9P-1	45:50	arg1	status					14:19	Glycosylation status	0:19	Glycosylation status of the membrane protein CD9P-1	0:50	Glycosylation status of the membrane protein CD9P-1.
17960739	4	52	theme	F	516:516	arg1	cleavage					518:525	enzymatic PNGase F cleavage	499:525	enzymatic PNGase F cleavage of N-glycans	499:538	After immunoprecipitation, CD9P-1 was subjected to enzymatic PNGase F cleavage of N-glycans, resulting in Asn to Asp conversion and increase in 1 mass unit.
17960739	6	53	theme	potential	799:807	arg1	sites					825:829	all nine potential N-glycosylation sites	790:829	all nine potential N-glycosylation sites	790:829	This has demonstrated that all nine potential N-glycosylation sites were actually engaged.
17960739	7	54	theme	MALDI-TOF	989:997	arg1	MS					999:1000	MALDI-TOF MS	989:1000	MALDI-TOF MS	989:1000	On the other hand, the N-glycan structures were determined combining chemical derivatization and exoglycosidase digestions followed by MALDI-TOF MS, ESI-MS/MS, and GC-MS analysis.
17960739	9	55	gly	glycosylated	1248:1259	arg1	CD9P-1					1273:1278	CD9P-1	1273:1278	CD9P-1	1273:1278	Finally, 2-D PAGE and lectino-blot analyses have revealed the presence of at least 17 glycosylated isoforms of CD9P-1 at cell surface.
17960739	9	55	gly	glycosylated	1248:1259	arg1	isoforms					1261:1268	at least 17 glycosylated isoforms	1236:1268	at least 17 glycosylated isoforms of CD9P-1	1236:1278	Finally, 2-D PAGE and lectino-blot analyses have revealed the presence of at least 17 glycosylated isoforms of CD9P-1 at cell surface.
17960739	4	56	theme	PNGase	509:514	arg1	F					516:516	enzymatic PNGase F	499:516	enzymatic PNGase F cleavage of N-glycans	499:538	After immunoprecipitation, CD9P-1 was subjected to enzymatic PNGase F cleavage of N-glycans, resulting in Asn to Asp conversion and increase in 1 mass unit.
17960739	10	57	theme	complex	1394:1400	arg1	complexity					1367:1376	complexity	1367:1376	complexity of this primary complex in the tetraspanin web	1367:1423	All CD9P-1 isoforms associate with CD9 leading to additional level of complexity of this primary complex in the tetraspanin web.
17960739	1	58	from	membrane	176:183	arg1	network					128:134	a network	126:134	a network of molecular interactions in the plasma membrane, in which it specifically associates with tetraspanins CD9 and CD81	126:251	The membrane protein CD9P-1 is a major component of the tetraspanin web, a network of molecular interactions in the plasma membrane, in which it specifically associates with tetraspanins CD9 and CD81.
17960739	1	58	from	membrane	176:183	arg1	component					92:100	a major component	84:100	a major component of the tetraspanin web	84:123	The membrane protein CD9P-1 is a major component of the tetraspanin web, a network of molecular interactions in the plasma membrane, in which it specifically associates with tetraspanins CD9 and CD81.
17960739	1	59	theme	tetraspanin	109:119	arg1	web					121:123	the tetraspanin web	105:123	the tetraspanin web	105:123	The membrane protein CD9P-1 is a major component of the tetraspanin web, a network of molecular interactions in the plasma membrane, in which it specifically associates with tetraspanins CD9 and CD81.
17960739	5	60	theme	deglycosylated	641:654	arg1	peptides					656:663	deglycosylated peptides	641:663	deglycosylated peptides	641:663	Thus, following protease digestion, deglycosylated peptides were selectively identified by high mass accuracy FTICR-MS, using this conversion as a signature.
17960739	4	61	dep	conversion	565:574	arg1	Asn					554:556	Asn	554:556	Asn	554:556	After immunoprecipitation, CD9P-1 was subjected to enzymatic PNGase F cleavage of N-glycans, resulting in Asn to Asp conversion and increase in 1 mass unit.
17960739	1	62	theme	web	121:123	arg1	CD9P-1					74:79	The membrane protein CD9P-1	53:79	The membrane protein CD9P-1	53:79	The membrane protein CD9P-1 is a major component of the tetraspanin web, a network of molecular interactions in the plasma membrane, in which it specifically associates with tetraspanins CD9 and CD81.
17960739	1	62	theme	web	121:123	arg1	network					128:134	a network	126:134	a network of molecular interactions in the plasma membrane, in which it specifically associates with tetraspanins CD9 and CD81	126:251	The membrane protein CD9P-1 is a major component of the tetraspanin web, a network of molecular interactions in the plasma membrane, in which it specifically associates with tetraspanins CD9 and CD81.
17960739	1	62	theme	web	121:123	arg1	component					92:100	a major component	84:100	a major component of the tetraspanin web	84:123	The membrane protein CD9P-1 is a major component of the tetraspanin web, a network of molecular interactions in the plasma membrane, in which it specifically associates with tetraspanins CD9 and CD81.
17960739	7	63	theme	other	861:865	arg1	hand					867:870	the other hand	857:870	the other hand	857:870	On the other hand, the N-glycan structures were determined combining chemical derivatization and exoglycosidase digestions followed by MALDI-TOF MS, ESI-MS/MS, and GC-MS analysis.
17960739	2	64	theme	CD81	296:299	arg1	effects					277:283	The various functional effects	254:283	The various functional effects of CD9 and CD81	254:299	The various functional effects of CD9 and CD81 may be related to their partners.
17960739	2	64	theme	CD81	296:299	arg1	related					308:314	related	308:314	related	308:314	The various functional effects of CD9 and CD81 may be related to their partners.
17960739	4	65	from	increase	580:587	arg1	unit					599:602	1 mass unit	592:602	1 mass unit	592:602	After immunoprecipitation, CD9P-1 was subjected to enzymatic PNGase F cleavage of N-glycans, resulting in Asn to Asp conversion and increase in 1 mass unit.
17960739	1	66	dep	tetraspanins	227:238	arg1	tetraspanins					227:238	tetraspanins CD9 and CD81	227:251	tetraspanins CD9 and CD81	227:251	The membrane protein CD9P-1 is a major component of the tetraspanin web, a network of molecular interactions in the plasma membrane, in which it specifically associates with tetraspanins CD9 and CD81.
17960739	1	66	dep	tetraspanins	227:238	arg1	CD81					248:251	CD81	248:251	CD81	248:251	The membrane protein CD9P-1 is a major component of the tetraspanin web, a network of molecular interactions in the plasma membrane, in which it specifically associates with tetraspanins CD9 and CD81.
17960739	1	66	dep	tetraspanins	227:238	arg1	CD9					240:242	CD9	240:242	CD9	240:242	The membrane protein CD9P-1 is a major component of the tetraspanin web, a network of molecular interactions in the plasma membrane, in which it specifically associates with tetraspanins CD9 and CD81.
17960739	3	67	theme	transfected	421:431	arg1	cells					441:445	stably transfected HEK-293 cells	414:445	stably transfected HEK-293 cells	414:445	Thus, we have addressed the characterization of the CD9P-1 glycosylation using stably transfected HEK-293 cells.
17960739	3	68	theme	glycosylation	394:406	arg1	characterization					363:378	the characterization	359:378	the characterization of the CD9P-1 glycosylation	359:406	Thus, we have addressed the characterization of the CD9P-1 glycosylation using stably transfected HEK-293 cells.
17960739	9	69	theme	glycosylated	1248:1259	arg1	isoforms					1261:1268	at least 17 glycosylated isoforms	1236:1268	at least 17 glycosylated isoforms of CD9P-1	1236:1278	Finally, 2-D PAGE and lectino-blot analyses have revealed the presence of at least 17 glycosylated isoforms of CD9P-1 at cell surface.
17960739	7	70	theme	exoglycosidase	951:964	arg1	digestions					966:975	exoglycosidase digestions	951:975	exoglycosidase digestions	951:975	On the other hand, the N-glycan structures were determined combining chemical derivatization and exoglycosidase digestions followed by MALDI-TOF MS, ESI-MS/MS, and GC-MS analysis.
16037490	2	0	theme	long	637:640	arg1	backbone					650:657	a long peptide backbone	635:657	a long peptide backbone exceeding 50 amino acid residues	635:690	In this study, recovery of glycopeptides was improved by including divalent cations or increasing the organic solvent in the binding solution, without losing specificity, whereas it was still less effective for those with a long peptide backbone exceeding 50 amino acid residues.
16037490	1	1	gly	glycoproteins	360:372	arg1	glycoproteins					360:372	glycoproteins	360:372	glycoproteins	360:372	Isolation of glycopeptides utilizing hydrogen bonding between glycopeptide glycans and a carbohydrate-gel matrix in the organic phase is useful for site-specific characterization of oligosaccharides of glycoproteins, when combined with mass spectrometry.
16037490	8	2	theme	site-specific	1860:1872	arg1	analysis					1874:1881	site-specific analysis	1860:1881	site-specific analysis of oligosaccharides in glycoproteomics	1860:1920	The results also demonstrated that the enriched glycopeptide provides resources for site-specific analysis of oligosaccharides in glycoproteomics.
16037490	1	3	theme	organic	278:284	arg1	phase					286:290	the organic phase	274:290	the organic phase	274:290	Isolation of glycopeptides utilizing hydrogen bonding between glycopeptide glycans and a carbohydrate-gel matrix in the organic phase is useful for site-specific characterization of oligosaccharides of glycoproteins, when combined with mass spectrometry.
16037490	6	4	theme	FN	1444:1445	arg1	O-glycosylation					1425:1439	the O-glycosylation	1421:1439	the O-glycosylation of FN	1421:1445	Considering that another mucin-type O-glycosylation site lies within a different connecting segment, the O-glycosylation of FN was suggested to play a significant role in segregating the neighboring domains and thus maintaining the topology of FN and the domain functions.
16037490	0	5	from	analysis	13:20	arg1	plasma					50:55	plasma	50:55	plasma	50:55	Differential analysis of site-specific glycans on plasma and cellular fibronectins: application of a hydrophilic affinity method for glycopeptide enrichment.
16037490	0	5	from	analysis	13:20	arg1	fibronectins					70:81	cellular fibronectins	61:81	cellular fibronectins	61:81	Differential analysis of site-specific glycans on plasma and cellular fibronectins: application of a hydrophilic affinity method for glycopeptide enrichment.
16037490	4	6	theme	site-specific	872:884	arg1	difference					886:895	a remarkable site-specific difference	859:895	a remarkable site-specific difference in fucosylation between these isoforms	859:934	There was a remarkable site-specific difference in fucosylation between these isoforms; Asn1244 selectively escaped the global fucosylation of cellular FN, whereas only Asn1007 and Asn2108 of the plasma isoform underwent modification.
16037490	5	7	gly	glycopeptide	1263:1274	arg2	reactive					1280:1287	reactive	1280:1287	reactive	1280:1287	In addition, a new O-glycosylation site was identified at Thr279 in the connecting segment between the fibrin- and heparin-binding domain and the collagen-binding domain, and the glycopeptide was reactive to a peanut agglutinin lectin.
16037490	5	7	gly	glycopeptide	1263:1274	arg2	glycopeptide					1263:1274	the glycopeptide	1259:1274	the glycopeptide	1259:1274	In addition, a new O-glycosylation site was identified at Thr279 in the connecting segment between the fibrin- and heparin-binding domain and the collagen-binding domain, and the glycopeptide was reactive to a peanut agglutinin lectin.
16037490	1	8	theme	glycopeptides	171:183	arg1	Isolation					158:166	Isolation	158:166	Isolation of glycopeptides utilizing hydrogen bonding between glycopeptide glycans and a carbohydrate-gel matrix in the organic phase	158:290	Isolation of glycopeptides utilizing hydrogen bonding between glycopeptide glycans and a carbohydrate-gel matrix in the organic phase is useful for site-specific characterization of oligosaccharides of glycoproteins, when combined with mass spectrometry.
16037490	5	9	theme	peanut	1294:1299	arg1	lectin					1312:1317	a peanut agglutinin lectin	1292:1317	a peanut agglutinin lectin	1292:1317	In addition, a new O-glycosylation site was identified at Thr279 in the connecting segment between the fibrin- and heparin-binding domain and the collagen-binding domain, and the glycopeptide was reactive to a peanut agglutinin lectin.
16037490	1	10	theme	mass	394:397	arg1	spectrometry					399:410	mass spectrometry	394:410	mass spectrometry	394:410	Isolation of glycopeptides utilizing hydrogen bonding between glycopeptide glycans and a carbohydrate-gel matrix in the organic phase is useful for site-specific characterization of oligosaccharides of glycoproteins, when combined with mass spectrometry.
16037490	2	11	gly	glycopeptides	440:452	arg2	glycopeptides					440:452	glycopeptides	440:452	glycopeptides	440:452	In this study, recovery of glycopeptides was improved by including divalent cations or increasing the organic solvent in the binding solution, without losing specificity, whereas it was still less effective for those with a long peptide backbone exceeding 50 amino acid residues.
16037490	3	12	dep	plasma	809:814	arg1	the					805:807	the	805:807	the	805:807	The method was then applied to the analysis of glycan heterogeneities at seven N-glycosylation sites in each of the plasma and cellular fibronectins (FNs).
16037490	5	13	theme	agglutinin	1301:1310	arg1	lectin					1312:1317	a peanut agglutinin lectin	1292:1317	a peanut agglutinin lectin	1292:1317	In addition, a new O-glycosylation site was identified at Thr279 in the connecting segment between the fibrin- and heparin-binding domain and the collagen-binding domain, and the glycopeptide was reactive to a peanut agglutinin lectin.
16037490	4	14	theme	cellular	992:999	arg1	FN					1001:1002	cellular FN	992:1002	cellular FN	992:1002	There was a remarkable site-specific difference in fucosylation between these isoforms; Asn1244 selectively escaped the global fucosylation of cellular FN, whereas only Asn1007 and Asn2108 of the plasma isoform underwent modification.
16037490	8	15	theme	enriched	1815:1822	arg1	glycopeptide					1824:1835	the enriched glycopeptide	1811:1835	the enriched glycopeptide	1811:1835	The results also demonstrated that the enriched glycopeptide provides resources for site-specific analysis of oligosaccharides in glycoproteomics.
16037490	3	16	theme	heterogeneities	747:761	arg1	analysis					728:735	the analysis	724:735	the analysis of glycan heterogeneities at seven N-glycosylation sites in each of the plasma and cellular fibronectins (FNs)	724:846	The method was then applied to the analysis of glycan heterogeneities at seven N-glycosylation sites in each of the plasma and cellular fibronectins (FNs).
16037490	4	17	theme	isoform	1052:1058	arg1	isoform					1052:1058	the plasma isoform	1041:1058	the plasma isoform	1041:1058	There was a remarkable site-specific difference in fucosylation between these isoforms; Asn1244 selectively escaped the global fucosylation of cellular FN, whereas only Asn1007 and Asn2108 of the plasma isoform underwent modification.
16037490	4	17	theme	isoform	1052:1058	arg1	Asn1007					1018:1024	Asn1007	1018:1024	Asn1007	1018:1024	There was a remarkable site-specific difference in fucosylation between these isoforms; Asn1244 selectively escaped the global fucosylation of cellular FN, whereas only Asn1007 and Asn2108 of the plasma isoform underwent modification.
16037490	2	18	theme	acid	678:681	arg1	residues					683:690	50 amino acid residues	669:690	50 amino acid residues	669:690	In this study, recovery of glycopeptides was improved by including divalent cations or increasing the organic solvent in the binding solution, without losing specificity, whereas it was still less effective for those with a long peptide backbone exceeding 50 amino acid residues.
16037490	8	19	from	oligosaccharides	1886:1901	arg1	glycoproteomics					1906:1920	glycoproteomics	1906:1920	glycoproteomics	1906:1920	The results also demonstrated that the enriched glycopeptide provides resources for site-specific analysis of oligosaccharides in glycoproteomics.
16037490	0	20	theme	affinity	113:120	arg1	method					122:127	a hydrophilic affinity method	99:127	a hydrophilic affinity method for glycopeptide enrichment	99:155	Differential analysis of site-specific glycans on plasma and cellular fibronectins: application of a hydrophilic affinity method for glycopeptide enrichment.
16037490	6	21	theme	mucin-type	1345:1354	arg1	site					1372:1375	another mucin-type O-glycosylation site	1337:1375	another mucin-type O-glycosylation site	1337:1375	Considering that another mucin-type O-glycosylation site lies within a different connecting segment, the O-glycosylation of FN was suggested to play a significant role in segregating the neighboring domains and thus maintaining the topology of FN and the domain functions.
16037490	5	22	theme	collagen-binding	1230:1245	arg1	domain					1247:1252	the collagen-binding domain	1226:1252	the collagen-binding domain	1226:1252	In addition, a new O-glycosylation site was identified at Thr279 in the connecting segment between the fibrin- and heparin-binding domain and the collagen-binding domain, and the glycopeptide was reactive to a peanut agglutinin lectin.
16037490	2	23	theme	amino	672:676	arg1	residues					683:690	50 amino acid residues	669:690	50 amino acid residues	669:690	In this study, recovery of glycopeptides was improved by including divalent cations or increasing the organic solvent in the binding solution, without losing specificity, whereas it was still less effective for those with a long peptide backbone exceeding 50 amino acid residues.
16037490	6	24	theme	O-glycosylation	1356:1370	arg1	site					1372:1375	another mucin-type O-glycosylation site	1337:1375	another mucin-type O-glycosylation site	1337:1375	Considering that another mucin-type O-glycosylation site lies within a different connecting segment, the O-glycosylation of FN was suggested to play a significant role in segregating the neighboring domains and thus maintaining the topology of FN and the domain functions.
16037490	6	25	gly	O-glycosylation	1356:1370	arg2	site					1372:1375	another mucin-type O-glycosylation site	1337:1375	another mucin-type O-glycosylation site	1337:1375	Considering that another mucin-type O-glycosylation site lies within a different connecting segment, the O-glycosylation of FN was suggested to play a significant role in segregating the neighboring domains and thus maintaining the topology of FN and the domain functions.
16037490	0	26	theme	hydrophilic	101:111	arg1	method					122:127	a hydrophilic affinity method	99:127	a hydrophilic affinity method for glycopeptide enrichment	99:155	Differential analysis of site-specific glycans on plasma and cellular fibronectins: application of a hydrophilic affinity method for glycopeptide enrichment.
16037490	2	27	from	solvent	523:529	arg1	solution					546:553	the binding solution	534:553	the binding solution	534:553	In this study, recovery of glycopeptides was improved by including divalent cations or increasing the organic solvent in the binding solution, without losing specificity, whereas it was still less effective for those with a long peptide backbone exceeding 50 amino acid residues.
16037490	1	28	gly	glycopeptide	220:231	arg2	glycopeptide					220:231	glycopeptide	220:231	glycopeptide	220:231	Isolation of glycopeptides utilizing hydrogen bonding between glycopeptide glycans and a carbohydrate-gel matrix in the organic phase is useful for site-specific characterization of oligosaccharides of glycoproteins, when combined with mass spectrometry.
16037490	8	29	theme	oligosaccharides	1886:1901	arg1	analysis					1874:1881	site-specific analysis	1860:1881	site-specific analysis of oligosaccharides in glycoproteomics	1860:1920	The results also demonstrated that the enriched glycopeptide provides resources for site-specific analysis of oligosaccharides in glycoproteomics.
16037490	4	30	theme	plasma	1045:1050	arg1	isoform					1052:1058	the plasma isoform	1041:1058	the plasma isoform	1041:1058	There was a remarkable site-specific difference in fucosylation between these isoforms; Asn1244 selectively escaped the global fucosylation of cellular FN, whereas only Asn1007 and Asn2108 of the plasma isoform underwent modification.
16037490	1	31	theme	hydrogen	195:202	arg1	bonding					204:210	hydrogen bonding	195:210	hydrogen bonding between glycopeptide glycans and a carbohydrate-gel matrix in the organic phase	195:290	Isolation of glycopeptides utilizing hydrogen bonding between glycopeptide glycans and a carbohydrate-gel matrix in the organic phase is useful for site-specific characterization of oligosaccharides of glycoproteins, when combined with mass spectrometry.
16037490	2	32	theme	organic	515:521	arg1	solvent					523:529	the organic solvent	511:529	the organic solvent in the binding solution	511:553	In this study, recovery of glycopeptides was improved by including divalent cations or increasing the organic solvent in the binding solution, without losing specificity, whereas it was still less effective for those with a long peptide backbone exceeding 50 amino acid residues.
16037490	3	33	theme	glycan	740:745	arg1	heterogeneities					747:761	glycan heterogeneities	740:761	glycan heterogeneities at seven N-glycosylation sites in each of the plasma and cellular fibronectins (FNs)	740:846	The method was then applied to the analysis of glycan heterogeneities at seven N-glycosylation sites in each of the plasma and cellular fibronectins (FNs).
16037490	3	34	from	sites	788:792	arg1	analysis					728:735	the analysis	724:735	the analysis of glycan heterogeneities at seven N-glycosylation sites in each of the plasma and cellular fibronectins (FNs)	724:846	The method was then applied to the analysis of glycan heterogeneities at seven N-glycosylation sites in each of the plasma and cellular fibronectins (FNs).
16037490	3	34	from	sites	788:792	arg1	heterogeneities					747:761	glycan heterogeneities	740:761	glycan heterogeneities at seven N-glycosylation sites in each of the plasma and cellular fibronectins (FNs)	740:846	The method was then applied to the analysis of glycan heterogeneities at seven N-glycosylation sites in each of the plasma and cellular fibronectins (FNs).
16037490	3	34	from	sites	788:792	arg1	FNs					843:845	cellular fibronectins (FNs)	820:846	cellular fibronectins (FNs)	820:846	The method was then applied to the analysis of glycan heterogeneities at seven N-glycosylation sites in each of the plasma and cellular fibronectins (FNs).
16037490	3	34	from	sites	788:792	arg1	each					797:800	each	797:800	each	797:800	The method was then applied to the analysis of glycan heterogeneities at seven N-glycosylation sites in each of the plasma and cellular fibronectins (FNs).
16037490	3	34	from	sites	788:792	arg1	plasma					809:814	plasma	809:814	plasma	809:814	The method was then applied to the analysis of glycan heterogeneities at seven N-glycosylation sites in each of the plasma and cellular fibronectins (FNs).
16037490	5	35	theme	fibrin-	1187:1193	arg1	domain					1215:1220	the fibrin- and heparin-binding domain	1183:1220	domain	1215:1220	In addition, a new O-glycosylation site was identified at Thr279 in the connecting segment between the fibrin- and heparin-binding domain and the collagen-binding domain, and the glycopeptide was reactive to a peanut agglutinin lectin.
16037490	4	36	gly	fucosylation	976:987	arg1	FN					1001:1002	cellular FN	992:1002	cellular FN	992:1002	There was a remarkable site-specific difference in fucosylation between these isoforms; Asn1244 selectively escaped the global fucosylation of cellular FN, whereas only Asn1007 and Asn2108 of the plasma isoform underwent modification.
16037490	6	37	theme	domain	1575:1580	arg1	functions					1582:1590	the domain functions	1571:1590	the domain functions	1571:1590	Considering that another mucin-type O-glycosylation site lies within a different connecting segment, the O-glycosylation of FN was suggested to play a significant role in segregating the neighboring domains and thus maintaining the topology of FN and the domain functions.
16037490	0	38	theme	Differential	0:11	arg1	analysis					13:20	Differential analysis	0:20	Differential analysis of site-specific glycans on plasma and cellular fibronectins: application of a hydrophilic affinity method for glycopeptide enrichment.	0:156	Differential analysis of site-specific glycans on plasma and cellular fibronectins: application of a hydrophilic affinity method for glycopeptide enrichment.
16037490	5	39	theme	heparin-binding	1199:1213	arg1	domain					1215:1220	the fibrin- and heparin-binding domain	1183:1220	domain	1215:1220	In addition, a new O-glycosylation site was identified at Thr279 in the connecting segment between the fibrin- and heparin-binding domain and the collagen-binding domain, and the glycopeptide was reactive to a peanut agglutinin lectin.
16037490	2	40	theme	peptide	642:648	arg1	backbone					650:657	a long peptide backbone	635:657	a long peptide backbone exceeding 50 amino acid residues	635:690	In this study, recovery of glycopeptides was improved by including divalent cations or increasing the organic solvent in the binding solution, without losing specificity, whereas it was still less effective for those with a long peptide backbone exceeding 50 amino acid residues.
16037490	0	41	theme	site-specific	25:37	arg1	glycans					39:45	site-specific glycans	25:45	site-specific glycans	25:45	Differential analysis of site-specific glycans on plasma and cellular fibronectins: application of a hydrophilic affinity method for glycopeptide enrichment.
16037490	1	42	theme	site-specific	306:318	arg1	characterization					320:335	site-specific characterization	306:335	site-specific characterization of oligosaccharides of glycoproteins	306:372	Isolation of glycopeptides utilizing hydrogen bonding between glycopeptide glycans and a carbohydrate-gel matrix in the organic phase is useful for site-specific characterization of oligosaccharides of glycoproteins, when combined with mass spectrometry.
16037490	6	43	theme	different	1391:1399	arg1	segment					1412:1418	a different connecting segment	1389:1418	a different connecting segment	1389:1418	Considering that another mucin-type O-glycosylation site lies within a different connecting segment, the O-glycosylation of FN was suggested to play a significant role in segregating the neighboring domains and thus maintaining the topology of FN and the domain functions.
16037490	6	44	theme	connecting	1401:1410	arg1	segment					1412:1418	a different connecting segment	1389:1418	a different connecting segment	1389:1418	Considering that another mucin-type O-glycosylation site lies within a different connecting segment, the O-glycosylation of FN was suggested to play a significant role in segregating the neighboring domains and thus maintaining the topology of FN and the domain functions.
16037490	6	45	theme	neighboring	1507:1517	arg1	domains					1519:1525	the neighboring domains	1503:1525	the neighboring domains	1503:1525	Considering that another mucin-type O-glycosylation site lies within a different connecting segment, the O-glycosylation of FN was suggested to play a significant role in segregating the neighboring domains and thus maintaining the topology of FN and the domain functions.
16037490	1	46	theme	glycopeptide	220:231	arg1	glycans					233:239	glycopeptide glycans	220:239	glycopeptide glycans	220:239	Isolation of glycopeptides utilizing hydrogen bonding between glycopeptide glycans and a carbohydrate-gel matrix in the organic phase is useful for site-specific characterization of oligosaccharides of glycoproteins, when combined with mass spectrometry.
16037490	6	47	theme	significant	1471:1481	arg1	role					1483:1486	a significant role	1469:1486	a significant role	1469:1486	Considering that another mucin-type O-glycosylation site lies within a different connecting segment, the O-glycosylation of FN was suggested to play a significant role in segregating the neighboring domains and thus maintaining the topology of FN and the domain functions.
16037490	0	48	theme	method	122:127	arg1	application					84:94	application	84:94	Differential analysis of site-specific glycans on plasma and cellular fibronectins: application of a hydrophilic affinity method for glycopeptide enrichment.	0:156	Differential analysis of site-specific glycans on plasma and cellular fibronectins: application of a hydrophilic affinity method for glycopeptide enrichment.
16037490	6	49	theme	FN	1564:1565	arg1	functions					1582:1590	the domain functions	1571:1590	the domain functions	1571:1590	Considering that another mucin-type O-glycosylation site lies within a different connecting segment, the O-glycosylation of FN was suggested to play a significant role in segregating the neighboring domains and thus maintaining the topology of FN and the domain functions.
16037490	6	49	theme	FN	1564:1565	arg1	topology					1552:1559	the topology	1548:1559	the topology of FN	1548:1565	Considering that another mucin-type O-glycosylation site lies within a different connecting segment, the O-glycosylation of FN was suggested to play a significant role in segregating the neighboring domains and thus maintaining the topology of FN and the domain functions.
16037490	3	50	theme	N-glycosylation	772:786	arg1	sites					788:792	seven N-glycosylation sites	766:792	seven N-glycosylation sites in each of the plasma and cellular fibronectins (FNs)	766:846	The method was then applied to the analysis of glycan heterogeneities at seven N-glycosylation sites in each of the plasma and cellular fibronectins (FNs).
16037490	4	51	theme	global	969:974	arg1	fucosylation					976:987	the global fucosylation	965:987	the global fucosylation of cellular FN	965:1002	There was a remarkable site-specific difference in fucosylation between these isoforms; Asn1244 selectively escaped the global fucosylation of cellular FN, whereas only Asn1007 and Asn2108 of the plasma isoform underwent modification.
16037490	5	52	theme	new	1099:1101	arg1	site					1119:1122	a new O-glycosylation site	1097:1122	a new O-glycosylation site	1097:1122	In addition, a new O-glycosylation site was identified at Thr279 in the connecting segment between the fibrin- and heparin-binding domain and the collagen-binding domain, and the glycopeptide was reactive to a peanut agglutinin lectin.
16037490	0	53	theme	glycans	39:45	arg1	analysis					13:20	Differential analysis	0:20	Differential analysis of site-specific glycans on plasma and cellular fibronectins: application of a hydrophilic affinity method for glycopeptide enrichment.	0:156	Differential analysis of site-specific glycans on plasma and cellular fibronectins: application of a hydrophilic affinity method for glycopeptide enrichment.
16037490	1	54	theme	oligosaccharides	340:355	arg1	characterization					320:335	site-specific characterization	306:335	site-specific characterization of oligosaccharides of glycoproteins	306:372	Isolation of glycopeptides utilizing hydrogen bonding between glycopeptide glycans and a carbohydrate-gel matrix in the organic phase is useful for site-specific characterization of oligosaccharides of glycoproteins, when combined with mass spectrometry.
16037490	0	55	theme	glycopeptide	133:144	arg1	enrichment					146:155	glycopeptide enrichment	133:155	glycopeptide enrichment	133:155	Differential analysis of site-specific glycans on plasma and cellular fibronectins: application of a hydrophilic affinity method for glycopeptide enrichment.
16037490	5	56	theme	O-glycosylation	1103:1117	arg1	site					1119:1122	a new O-glycosylation site	1097:1122	a new O-glycosylation site	1097:1122	In addition, a new O-glycosylation site was identified at Thr279 in the connecting segment between the fibrin- and heparin-binding domain and the collagen-binding domain, and the glycopeptide was reactive to a peanut agglutinin lectin.
16037490	2	57	theme	divalent	480:487	arg1	cations					489:495	divalent cations	480:495	divalent cations	480:495	In this study, recovery of glycopeptides was improved by including divalent cations or increasing the organic solvent in the binding solution, without losing specificity, whereas it was still less effective for those with a long peptide backbone exceeding 50 amino acid residues.
16037490	2	58	theme	glycopeptides	440:452	arg1	recovery					428:435	recovery	428:435	recovery of glycopeptides	428:452	In this study, recovery of glycopeptides was improved by including divalent cations or increasing the organic solvent in the binding solution, without losing specificity, whereas it was still less effective for those with a long peptide backbone exceeding 50 amino acid residues.
16037490	8	59	from	analysis	1874:1881	arg1	glycoproteomics					1906:1920	glycoproteomics	1906:1920	glycoproteomics	1906:1920	The results also demonstrated that the enriched glycopeptide provides resources for site-specific analysis of oligosaccharides in glycoproteomics.
16037490	2	60	theme	binding	538:544	arg1	solution					546:553	the binding solution	534:553	the binding solution	534:553	In this study, recovery of glycopeptides was improved by including divalent cations or increasing the organic solvent in the binding solution, without losing specificity, whereas it was still less effective for those with a long peptide backbone exceeding 50 amino acid residues.
16037490	8	61	gly	glycopeptide	1824:1835	arg2	glycopeptide					1824:1835	the enriched glycopeptide	1811:1835	the enriched glycopeptide	1811:1835	The results also demonstrated that the enriched glycopeptide provides resources for site-specific analysis of oligosaccharides in glycoproteomics.
16037490	3	62	gly	N-glycosylation	772:786	arg2	seven					766:770	seven	766:770	seven	766:770	The method was then applied to the analysis of glycan heterogeneities at seven N-glycosylation sites in each of the plasma and cellular fibronectins (FNs).
16037490	3	62	gly	N-glycosylation	772:786	arg2	sites					788:792	seven N-glycosylation sites	766:792	seven N-glycosylation sites in each of the plasma and cellular fibronectins (FNs)	766:846	The method was then applied to the analysis of glycan heterogeneities at seven N-glycosylation sites in each of the plasma and cellular fibronectins (FNs).
16037490	5	63	theme	connecting	1156:1165	arg1	segment					1167:1173	the connecting segment	1152:1173	the connecting segment between the fibrin- and heparin-binding domain and the collagen-binding domain	1152:1252	In addition, a new O-glycosylation site was identified at Thr279 in the connecting segment between the fibrin- and heparin-binding domain and the collagen-binding domain, and the glycopeptide was reactive to a peanut agglutinin lectin.
16037490	3	64	from	analysis	728:735	arg1	sites					788:792	seven N-glycosylation sites	766:792	seven N-glycosylation sites in each of the plasma and cellular fibronectins (FNs)	766:846	The method was then applied to the analysis of glycan heterogeneities at seven N-glycosylation sites in each of the plasma and cellular fibronectins (FNs).
16037490	1	65	theme	glycoproteins	360:372	arg1	oligosaccharides					340:355	oligosaccharides	340:355	oligosaccharides of glycoproteins	340:372	Isolation of glycopeptides utilizing hydrogen bonding between glycopeptide glycans and a carbohydrate-gel matrix in the organic phase is useful for site-specific characterization of oligosaccharides of glycoproteins, when combined with mass spectrometry.
16037490	6	66	gly	O-glycosylation	1425:1439	arg1	FN					1444:1445	FN	1444:1445	FN	1444:1445	Considering that another mucin-type O-glycosylation site lies within a different connecting segment, the O-glycosylation of FN was suggested to play a significant role in segregating the neighboring domains and thus maintaining the topology of FN and the domain functions.
16037490	4	67	theme	FN	1001:1002	arg1	fucosylation					976:987	the global fucosylation	965:987	the global fucosylation of cellular FN	965:1002	There was a remarkable site-specific difference in fucosylation between these isoforms; Asn1244 selectively escaped the global fucosylation of cellular FN, whereas only Asn1007 and Asn2108 of the plasma isoform underwent modification.
16037490	1	68	gly	glycopeptides	171:183	arg2	glycopeptides					171:183	glycopeptides	171:183	glycopeptides utilizing hydrogen bonding between glycopeptide glycans and a carbohydrate-gel matrix in the organic phase	171:290	Isolation of glycopeptides utilizing hydrogen bonding between glycopeptide glycans and a carbohydrate-gel matrix in the organic phase is useful for site-specific characterization of oligosaccharides of glycoproteins, when combined with mass spectrometry.
16037490	7	69	theme	N-glycan	1669:1676	arg1	structures					1678:1687	N-glycan structures	1669:1687	N-glycan structures at 17 of 19 potential sites	1669:1715	In addition, the method was applied to apolipoprotein B-100 (apoB100) whose N-glycan structures at 17 of 19 potential sites have been reported, and characterized the remaining sites.
16037490	7	70	from	sites	1711:1715	arg1	structures					1678:1687	N-glycan structures	1669:1687	N-glycan structures at 17 of 19 potential sites	1669:1715	In addition, the method was applied to apolipoprotein B-100 (apoB100) whose N-glycan structures at 17 of 19 potential sites have been reported, and characterized the remaining sites.
16037490	0	71	gly	glycopeptide	133:144	arg2	glycopeptide					133:144	glycopeptide enrichment	133:155	glycopeptide enrichment	133:155	Differential analysis of site-specific glycans on plasma and cellular fibronectins: application of a hydrophilic affinity method for glycopeptide enrichment.
16037490	1	72	theme	carbohydrate-gel	247:262	arg1	matrix					264:269	a carbohydrate-gel matrix	245:269	a carbohydrate-gel matrix	245:269	Isolation of glycopeptides utilizing hydrogen bonding between glycopeptide glycans and a carbohydrate-gel matrix in the organic phase is useful for site-specific characterization of oligosaccharides of glycoproteins, when combined with mass spectrometry.
16037490	1	73	from	bonding	204:210	arg1	phase					286:290	the organic phase	274:290	the organic phase	274:290	Isolation of glycopeptides utilizing hydrogen bonding between glycopeptide glycans and a carbohydrate-gel matrix in the organic phase is useful for site-specific characterization of oligosaccharides of glycoproteins, when combined with mass spectrometry.
16037490	7	74	theme	potential	1701:1709	arg1	sites					1711:1715	17 of 19 potential sites	1692:1715	17 of 19 potential sites	1692:1715	In addition, the method was applied to apolipoprotein B-100 (apoB100) whose N-glycan structures at 17 of 19 potential sites have been reported, and characterized the remaining sites.
16037490	7	75	theme	remaining	1759:1767	arg1	sites					1769:1773	the remaining sites	1755:1773	the remaining sites	1755:1773	In addition, the method was applied to apolipoprotein B-100 (apoB100) whose N-glycan structures at 17 of 19 potential sites have been reported, and characterized the remaining sites.
16037490	7	76	theme	apolipoprotein	1632:1645	arg1	apoB100					1654:1660	apoB100	1654:1660	apoB100	1654:1660	In addition, the method was applied to apolipoprotein B-100 (apoB100) whose N-glycan structures at 17 of 19 potential sites have been reported, and characterized the remaining sites.
16037490	7	76	theme	apolipoprotein	1632:1645	arg1	B-100					1647:1651	apolipoprotein B-100	1632:1651	apolipoprotein B-100 (apoB100) whose N-glycan structures at 17 of 19 potential sites have been reported, and characterized the remaining sites	1632:1773	In addition, the method was applied to apolipoprotein B-100 (apoB100) whose N-glycan structures at 17 of 19 potential sites have been reported, and characterized the remaining sites.
16037490	0	77	dep	analysis	13:20	arg1	application					84:94	application	84:94	Differential analysis of site-specific glycans on plasma and cellular fibronectins: application of a hydrophilic affinity method for glycopeptide enrichment.	0:156	Differential analysis of site-specific glycans on plasma and cellular fibronectins: application of a hydrophilic affinity method for glycopeptide enrichment.
16037490	8	78	from	glycoproteomics	1906:1920	arg1	analysis					1874:1881	site-specific analysis	1860:1881	site-specific analysis of oligosaccharides in glycoproteomics	1860:1920	The results also demonstrated that the enriched glycopeptide provides resources for site-specific analysis of oligosaccharides in glycoproteomics.
16037490	5	79	gly	O-glycosylation	1103:1117	arg2	site					1119:1122	a new O-glycosylation site	1097:1122	a new O-glycosylation site	1097:1122	In addition, a new O-glycosylation site was identified at Thr279 in the connecting segment between the fibrin- and heparin-binding domain and the collagen-binding domain, and the glycopeptide was reactive to a peanut agglutinin lectin.
16037490	0	80	theme	cellular	61:68	arg1	fibronectins					70:81	cellular fibronectins	61:81	cellular fibronectins	61:81	Differential analysis of site-specific glycans on plasma and cellular fibronectins: application of a hydrophilic affinity method for glycopeptide enrichment.
16037490	4	81	theme	remarkable	861:870	arg1	difference					886:895	a remarkable site-specific difference	859:895	a remarkable site-specific difference in fucosylation between these isoforms	859:934	There was a remarkable site-specific difference in fucosylation between these isoforms; Asn1244 selectively escaped the global fucosylation of cellular FN, whereas only Asn1007 and Asn2108 of the plasma isoform underwent modification.
16037490	3	82	theme	fibronectins	829:840	arg1	FNs					843:845	cellular fibronectins (FNs)	820:846	cellular fibronectins (FNs)	820:846	The method was then applied to the analysis of glycan heterogeneities at seven N-glycosylation sites in each of the plasma and cellular fibronectins (FNs).
16037490	4	83	from	difference	886:895	arg1	fucosylation					900:911	fucosylation	900:911	fucosylation	900:911	There was a remarkable site-specific difference in fucosylation between these isoforms; Asn1244 selectively escaped the global fucosylation of cellular FN, whereas only Asn1007 and Asn2108 of the plasma isoform underwent modification.
16037490	3	84	theme	cellular	820:827	arg1	FNs					843:845	cellular fibronectins (FNs)	820:846	cellular fibronectins (FNs)	820:846	The method was then applied to the analysis of glycan heterogeneities at seven N-glycosylation sites in each of the plasma and cellular fibronectins (FNs).
23319596	5	0	theme	tropoelastin	787:798	arg1	oxidation					800:808	tropoelastin oxidation	787:808	tropoelastin oxidation	787:808	The recombinant proteins also show activity in tropoelastin oxidation.
23319596	7	1	theme	inclusion	1202:1210	arg1	bodies					1212:1217	inclusion bodies	1202:1217	inclusion bodies	1202:1217	Disruption of N-glycosylation by site-directed mutagenesis or tunicamycin treatment completely inhibited secretion so that only small quantities of inclusion bodies were detected.
23319596	8	2	theme	∼50	1385:1387	arg1	%					1388:1388	%	1388:1388	%	1388:1388	The N-glycosylation site at Asn-644 in the LOX catalytic domain is not conserved in human LOX (hLOX), although the LOX catalytic domain of hLOX shares ∼50% identity and ∼70% homology with hLOXL2.
23319596	1	3	theme	epithelial-to-mesenchymal	237:261	arg1	transition					263:272	epithelial-to-mesenchymal transition	237:272	epithelial-to-mesenchymal transition	237:272	Human lysyl oxidase-like 2 (hLOXL2) is highly up-regulated in metastatic breast cancer cells and tissues and induces epithelial-to-mesenchymal transition, the first step of metastasis/invasion.
23319596	1	3	theme	epithelial-to-mesenchymal	237:261	arg1	step					285:288	the first step	275:288	the first step of metastasis/invasion	275:311	Human lysyl oxidase-like 2 (hLOXL2) is highly up-regulated in metastatic breast cancer cells and tissues and induces epithelial-to-mesenchymal transition, the first step of metastasis/invasion.
23319596	10	4	theme	at	1564:1565	arg1	Asn-644					1567:1573	the N-glycan at Asn-644	1551:1573	the N-glycan at Asn-644 of hLOXL2	1551:1583	These results suggest that the N-glycan at Asn-644 of hLOXL2 enhances the solubility and stability of the LOX catalytic domain.
23319596	7	5	theme	bodies	1212:1217	arg1	quantities					1188:1197	only small quantities	1177:1197	only small quantities of inclusion bodies	1177:1217	Disruption of N-glycosylation by site-directed mutagenesis or tunicamycin treatment completely inhibited secretion so that only small quantities of inclusion bodies were detected.
23319596	3	6	theme	hLOXL2	532:537	arg1	modifications					515:527	the post-translational modifications	492:527	the post-translational modifications of hLOXL2	492:537	Here, we assessed the extent of the post-translational modifications of hLOXL2 using truncated recombinant proteins produced in Drosophila S2 cells.
23319596	8	7	theme	human	1318:1322	arg1	LOX					1324:1326	human LOX	1318:1326	human LOX (hLOX)	1318:1333	The N-glycosylation site at Asn-644 in the LOX catalytic domain is not conserved in human LOX (hLOX), although the LOX catalytic domain of hLOX shares ∼50% identity and ∼70% homology with hLOXL2.
23319596	8	7	theme	human	1318:1322	arg1	hLOX					1329:1332	hLOX	1329:1332	hLOX	1329:1332	The N-glycosylation site at Asn-644 in the LOX catalytic domain is not conserved in human LOX (hLOX), although the LOX catalytic domain of hLOX shares ∼50% identity and ∼70% homology with hLOXL2.
23319596	9	8	theme	hLOX	1454:1457	arg1	hLOX					1454:1457	hLOX	1454:1457	hLOX	1454:1457	The catalytic domain of hLOX was not secreted from S2 cells using the same expression system.
23319596	9	8	theme	hLOX	1454:1457	arg1	domain					1444:1449	The catalytic domain	1430:1449	The catalytic domain of hLOX	1430:1457	The catalytic domain of hLOX was not secreted from S2 cells using the same expression system.
23319596	0	9	theme	Drosophila	99:108	arg1	cells					113:117	Drosophila S2 cells	99:117	Drosophila S2 cells	99:117	Post-translational modifications of recombinant human lysyl oxidase-like 2 (rhLOXL2) secreted from Drosophila S2 cells.
23319596	10	10	theme	hLOXL2	1578:1583	arg1	Asn-644					1567:1573	the N-glycan at Asn-644	1551:1573	the N-glycan at Asn-644 of hLOXL2	1551:1583	These results suggest that the N-glycan at Asn-644 of hLOXL2 enhances the solubility and stability of the LOX catalytic domain.
23319596	10	11	theme	catalytic	1634:1642	arg1	domain					1644:1649	the LOX catalytic domain	1626:1649	the LOX catalytic domain	1626:1649	These results suggest that the N-glycan at Asn-644 of hLOXL2 enhances the solubility and stability of the LOX catalytic domain.
23319596	8	12	with	homology	1408:1415	arg1	hLOXL2					1422:1427	hLOXL2	1422:1427	hLOXL2	1422:1427	The N-glycosylation site at Asn-644 in the LOX catalytic domain is not conserved in human LOX (hLOX), although the LOX catalytic domain of hLOX shares ∼50% identity and ∼70% homology with hLOXL2.
23319596	8	13	theme	N-glycosylation	1238:1252	arg1	site					1254:1257	The N-glycosylation site	1234:1257	The N-glycosylation site at Asn-644 in the LOX catalytic domain	1234:1296	The N-glycosylation site at Asn-644 in the LOX catalytic domain is not conserved in human LOX (hLOX), although the LOX catalytic domain of hLOX shares ∼50% identity and ∼70% homology with hLOXL2.
23319596	6	14	theme	tyrosylquinone	952:965	arg1	cross-link					967:976	the derivatized lysine tyrosylquinone cross-link	929:976	the derivatized lysine tyrosylquinone cross-link	929:976	After phenylhydrazine derivatization and trypsin digestion, we used mass spectrometry to identify peptides containing the derivatized lysine tyrosylquinone cross-link at Lys-653 and Tyr-689, as well as N-linked glycans at Asn-455 and Asn-644.
23319596	6	15	theme	trypsin	852:858	arg1	digestion					860:868	trypsin digestion	852:868	trypsin digestion	852:868	After phenylhydrazine derivatization and trypsin digestion, we used mass spectrometry to identify peptides containing the derivatized lysine tyrosylquinone cross-link at Lys-653 and Tyr-689, as well as N-linked glycans at Asn-455 and Asn-644.
23319596	8	16	theme	%	1388:1388	arg1	identity					1390:1397	∼50% identity	1385:1397	∼50% identity	1385:1397	The N-glycosylation site at Asn-644 in the LOX catalytic domain is not conserved in human LOX (hLOX), although the LOX catalytic domain of hLOX shares ∼50% identity and ∼70% homology with hLOXL2.
23319596	1	17	theme	oxidase-like	132:143	arg1	lysyl					126:130	Human lysyl oxidase-like 2	120:145	Human lysyl oxidase-like 2 (hLOXL2)	120:154	Human lysyl oxidase-like 2 (hLOXL2) is highly up-regulated in metastatic breast cancer cells and tissues and induces epithelial-to-mesenchymal transition, the first step of metastasis/invasion.
23319596	1	17	theme	oxidase-like	132:143	arg1	hLOXL2					148:153	hLOXL2	148:153	hLOXL2	148:153	Human lysyl oxidase-like 2 (hLOXL2) is highly up-regulated in metastatic breast cancer cells and tissues and induces epithelial-to-mesenchymal transition, the first step of metastasis/invasion.
23319596	4	18	theme	m	713:713	arg1	urea					715:718	2-6 m urea	709:718	2-6 m urea	709:718	The recombinant proteins are soluble, in contrast to LOX, which is consistently reported to require 2-6 m urea for solubilization.
23319596	3	19	theme	post-translational	496:513	arg1	modifications					515:527	the post-translational modifications	492:527	the post-translational modifications of hLOXL2	492:537	Here, we assessed the extent of the post-translational modifications of hLOXL2 using truncated recombinant proteins produced in Drosophila S2 cells.
23319596	3	20	theme	recombinant	555:565	arg1	proteins					567:574	truncated recombinant proteins	545:574	truncated recombinant proteins produced in Drosophila S2 cells	545:606	Here, we assessed the extent of the post-translational modifications of hLOXL2 using truncated recombinant proteins produced in Drosophila S2 cells.
23319596	9	21	theme	S2	1481:1482	arg1	cells					1484:1488	S2 cells	1481:1488	S2 cells using the same expression system	1481:1521	The catalytic domain of hLOX was not secreted from S2 cells using the same expression system.
23319596	2	22	theme	oxidase	428:434	arg1	hloxl2					314:319	hloxl2	314:319	hloxl2	314:319	hloxl2 encodes four N-terminal scavenger receptor cysteine-rich domains and the highly conserved C-terminal lysyl oxidase (LOX) catalytic domain.
23319596	2	22	theme	oxidase	428:434	arg1	domain					452:457	the highly conserved C-terminal lysyl oxidase (LOX) catalytic domain	390:457	the highly conserved C-terminal lysyl oxidase (LOX) catalytic domain	390:457	hloxl2 encodes four N-terminal scavenger receptor cysteine-rich domains and the highly conserved C-terminal lysyl oxidase (LOX) catalytic domain.
23319596	0	23	theme	S2	110:111	arg1	cells					113:117	Drosophila S2 cells	99:117	Drosophila S2 cells	99:117	Post-translational modifications of recombinant human lysyl oxidase-like 2 (rhLOXL2) secreted from Drosophila S2 cells.
23319596	6	24	theme	derivatized	933:943	arg1	cross-link					967:976	the derivatized lysine tyrosylquinone cross-link	929:976	the derivatized lysine tyrosylquinone cross-link	929:976	After phenylhydrazine derivatization and trypsin digestion, we used mass spectrometry to identify peptides containing the derivatized lysine tyrosylquinone cross-link at Lys-653 and Tyr-689, as well as N-linked glycans at Asn-455 and Asn-644.
23319596	4	25	theme	recombinant	613:623	arg1	proteins					625:632	The recombinant proteins	609:632	The recombinant proteins	609:632	The recombinant proteins are soluble, in contrast to LOX, which is consistently reported to require 2-6 m urea for solubilization.
23319596	4	25	theme	recombinant	613:623	arg1	soluble					638:644	soluble	638:644	soluble	638:644	The recombinant proteins are soluble, in contrast to LOX, which is consistently reported to require 2-6 m urea for solubilization.
23319596	6	26	used	used	874:877	arg2	we					871:872	we	871:872	we	871:872	After phenylhydrazine derivatization and trypsin digestion, we used mass spectrometry to identify peptides containing the derivatized lysine tyrosylquinone cross-link at Lys-653 and Tyr-689, as well as N-linked glycans at Asn-455 and Asn-644.
23319596	2	27	theme	lysyl	422:426	arg1	hloxl2					314:319	hloxl2	314:319	hloxl2	314:319	hloxl2 encodes four N-terminal scavenger receptor cysteine-rich domains and the highly conserved C-terminal lysyl oxidase (LOX) catalytic domain.
23319596	2	27	theme	lysyl	422:426	arg1	domain					452:457	the highly conserved C-terminal lysyl oxidase (LOX) catalytic domain	390:457	the highly conserved C-terminal lysyl oxidase (LOX) catalytic domain	390:457	hloxl2 encodes four N-terminal scavenger receptor cysteine-rich domains and the highly conserved C-terminal lysyl oxidase (LOX) catalytic domain.
23319596	10	28	theme	LOX	1630:1632	arg1	domain					1644:1649	the LOX catalytic domain	1626:1649	the LOX catalytic domain	1626:1649	These results suggest that the N-glycan at Asn-644 of hLOXL2 enhances the solubility and stability of the LOX catalytic domain.
23319596	6	29	theme	phenylhydrazine	817:831	arg1	derivatization					833:846	phenylhydrazine derivatization	817:846	phenylhydrazine derivatization	817:846	After phenylhydrazine derivatization and trypsin digestion, we used mass spectrometry to identify peptides containing the derivatized lysine tyrosylquinone cross-link at Lys-653 and Tyr-689, as well as N-linked glycans at Asn-455 and Asn-644.
23319596	6	30	theme	lysine	945:950	arg1	cross-link					967:976	the derivatized lysine tyrosylquinone cross-link	929:976	the derivatized lysine tyrosylquinone cross-link	929:976	After phenylhydrazine derivatization and trypsin digestion, we used mass spectrometry to identify peptides containing the derivatized lysine tyrosylquinone cross-link at Lys-653 and Tyr-689, as well as N-linked glycans at Asn-455 and Asn-644.
23319596	2	31	theme	C-terminal	411:420	arg1	hloxl2					314:319	hloxl2	314:319	hloxl2	314:319	hloxl2 encodes four N-terminal scavenger receptor cysteine-rich domains and the highly conserved C-terminal lysyl oxidase (LOX) catalytic domain.
23319596	2	31	theme	C-terminal	411:420	arg1	domain					452:457	the highly conserved C-terminal lysyl oxidase (LOX) catalytic domain	390:457	the highly conserved C-terminal lysyl oxidase (LOX) catalytic domain	390:457	hloxl2 encodes four N-terminal scavenger receptor cysteine-rich domains and the highly conserved C-terminal lysyl oxidase (LOX) catalytic domain.
23319596	0	32	theme	Post-translational	0:17	arg1	modifications					19:31	Post-translational modifications	0:31	Post-translational modifications of recombinant human lysyl oxidase-like 2 (rhLOXL2)	0:83	Post-translational modifications of recombinant human lysyl oxidase-like 2 (rhLOXL2) secreted from Drosophila S2 cells.
23319596	1	33	theme	first	279:283	arg1	transition					263:272	epithelial-to-mesenchymal transition	237:272	epithelial-to-mesenchymal transition	237:272	Human lysyl oxidase-like 2 (hLOXL2) is highly up-regulated in metastatic breast cancer cells and tissues and induces epithelial-to-mesenchymal transition, the first step of metastasis/invasion.
23319596	1	33	theme	first	279:283	arg1	step					285:288	the first step	275:288	the first step of metastasis/invasion	275:311	Human lysyl oxidase-like 2 (hLOXL2) is highly up-regulated in metastatic breast cancer cells and tissues and induces epithelial-to-mesenchymal transition, the first step of metastasis/invasion.
23319596	6	34	from	Asn-644	1045:1051	arg1	glycans					1022:1028	N-linked glycans	1013:1028	N-linked glycans at Asn-455 and Asn-644	1013:1051	After phenylhydrazine derivatization and trypsin digestion, we used mass spectrometry to identify peptides containing the derivatized lysine tyrosylquinone cross-link at Lys-653 and Tyr-689, as well as N-linked glycans at Asn-455 and Asn-644.
23319596	6	34	from	Asn-644	1045:1051	arg1	peptides					909:916	peptides	909:916	peptides containing the derivatized lysine tyrosylquinone cross-link at Lys-653 and Tyr-689	909:999	After phenylhydrazine derivatization and trypsin digestion, we used mass spectrometry to identify peptides containing the derivatized lysine tyrosylquinone cross-link at Lys-653 and Tyr-689, as well as N-linked glycans at Asn-455 and Asn-644.
23319596	8	35	theme	%	1406:1406	arg1	homology					1408:1415	∼70% homology	1403:1415	∼70% homology with hLOXL2	1403:1427	The N-glycosylation site at Asn-644 in the LOX catalytic domain is not conserved in human LOX (hLOX), although the LOX catalytic domain of hLOX shares ∼50% identity and ∼70% homology with hLOXL2.
23319596	2	36	theme	conserved	401:409	arg1	hloxl2					314:319	hloxl2	314:319	hloxl2	314:319	hloxl2 encodes four N-terminal scavenger receptor cysteine-rich domains and the highly conserved C-terminal lysyl oxidase (LOX) catalytic domain.
23319596	2	36	theme	conserved	401:409	arg1	domain					452:457	the highly conserved C-terminal lysyl oxidase (LOX) catalytic domain	390:457	the highly conserved C-terminal lysyl oxidase (LOX) catalytic domain	390:457	hloxl2 encodes four N-terminal scavenger receptor cysteine-rich domains and the highly conserved C-terminal lysyl oxidase (LOX) catalytic domain.
23319596	0	37	theme	recombinant	36:46	arg1	lysyl					54:58	recombinant human lysyl oxidase-like 2	36:73	recombinant human lysyl oxidase-like 2 (rhLOXL2)	36:83	Post-translational modifications of recombinant human lysyl oxidase-like 2 (rhLOXL2) secreted from Drosophila S2 cells.
23319596	0	37	theme	recombinant	36:46	arg1	rhLOXL2					76:82	rhLOXL2	76:82	rhLOXL2	76:82	Post-translational modifications of recombinant human lysyl oxidase-like 2 (rhLOXL2) secreted from Drosophila S2 cells.
23319596	8	38	theme	catalytic	1353:1361	arg1	hLOX					1373:1376	hLOX	1373:1376	hLOX	1373:1376	The N-glycosylation site at Asn-644 in the LOX catalytic domain is not conserved in human LOX (hLOX), although the LOX catalytic domain of hLOX shares ∼50% identity and ∼70% homology with hLOXL2.
23319596	8	38	theme	catalytic	1353:1361	arg1	domain					1363:1368	the LOX catalytic domain	1345:1368	the LOX catalytic domain of hLOX	1345:1376	The N-glycosylation site at Asn-644 in the LOX catalytic domain is not conserved in human LOX (hLOX), although the LOX catalytic domain of hLOX shares ∼50% identity and ∼70% homology with hLOXL2.
23319596	3	39	theme	Drosophila	588:597	arg1	cells					602:606	Drosophila S2 cells	588:606	Drosophila S2 cells	588:606	Here, we assessed the extent of the post-translational modifications of hLOXL2 using truncated recombinant proteins produced in Drosophila S2 cells.
23319596	7	40	theme	small	1182:1186	arg1	quantities					1188:1197	only small quantities	1177:1197	only small quantities of inclusion bodies	1177:1217	Disruption of N-glycosylation by site-directed mutagenesis or tunicamycin treatment completely inhibited secretion so that only small quantities of inclusion bodies were detected.
23319596	1	41	theme	metastatic	182:191	arg1	cells					207:211	metastatic breast cancer cells	182:211	metastatic breast cancer cells	182:211	Human lysyl oxidase-like 2 (hLOXL2) is highly up-regulated in metastatic breast cancer cells and tissues and induces epithelial-to-mesenchymal transition, the first step of metastasis/invasion.
23319596	8	42	theme	LOX	1277:1279	arg1	domain					1291:1296	the LOX catalytic domain	1273:1296	the LOX catalytic domain	1273:1296	The N-glycosylation site at Asn-644 in the LOX catalytic domain is not conserved in human LOX (hLOX), although the LOX catalytic domain of hLOX shares ∼50% identity and ∼70% homology with hLOXL2.
23319596	6	43	theme	N-linked	1013:1020	arg1	glycans					1022:1028	N-linked glycans	1013:1028	N-linked glycans at Asn-455 and Asn-644	1013:1051	After phenylhydrazine derivatization and trypsin digestion, we used mass spectrometry to identify peptides containing the derivatized lysine tyrosylquinone cross-link at Lys-653 and Tyr-689, as well as N-linked glycans at Asn-455 and Asn-644.
23319596	8	44	theme	∼70	1403:1405	arg1	%					1406:1406	%	1406:1406	%	1406:1406	The N-glycosylation site at Asn-644 in the LOX catalytic domain is not conserved in human LOX (hLOX), although the LOX catalytic domain of hLOX shares ∼50% identity and ∼70% homology with hLOXL2.
23319596	10	45	from	Asn-644	1567:1573	arg1	at					1564:1565	the N-glycan at Asn-644	1551:1573	the N-glycan at Asn-644 of hLOXL2	1551:1583	These results suggest that the N-glycan at Asn-644 of hLOXL2 enhances the solubility and stability of the LOX catalytic domain.
23319596	10	45	from	Asn-644	1567:1573	arg1	N-glycan					1555:1562	the N-glycan at Asn-644	1551:1573	the N-glycan at Asn-644 of hLOXL2	1551:1583	These results suggest that the N-glycan at Asn-644 of hLOXL2 enhances the solubility and stability of the LOX catalytic domain.
23319596	3	46	theme	S2	599:600	arg1	cells					602:606	Drosophila S2 cells	588:606	Drosophila S2 cells	588:606	Here, we assessed the extent of the post-translational modifications of hLOXL2 using truncated recombinant proteins produced in Drosophila S2 cells.
23319596	1	47	theme	breast	193:198	arg1	cells					207:211	metastatic breast cancer cells	182:211	metastatic breast cancer cells	182:211	Human lysyl oxidase-like 2 (hLOXL2) is highly up-regulated in metastatic breast cancer cells and tissues and induces epithelial-to-mesenchymal transition, the first step of metastasis/invasion.
23319596	0	48	theme	lysyl	54:58	arg1	modifications					19:31	Post-translational modifications	0:31	Post-translational modifications of recombinant human lysyl oxidase-like 2 (rhLOXL2)	0:83	Post-translational modifications of recombinant human lysyl oxidase-like 2 (rhLOXL2) secreted from Drosophila S2 cells.
23319596	1	49	theme	metastasis/invasion	293:311	arg1	transition					263:272	epithelial-to-mesenchymal transition	237:272	epithelial-to-mesenchymal transition	237:272	Human lysyl oxidase-like 2 (hLOXL2) is highly up-regulated in metastatic breast cancer cells and tissues and induces epithelial-to-mesenchymal transition, the first step of metastasis/invasion.
23319596	1	49	theme	metastasis/invasion	293:311	arg1	step					285:288	the first step	275:288	the first step of metastasis/invasion	275:311	Human lysyl oxidase-like 2 (hLOXL2) is highly up-regulated in metastatic breast cancer cells and tissues and induces epithelial-to-mesenchymal transition, the first step of metastasis/invasion.
23319596	1	50	theme	cancer	200:205	arg1	cells					207:211	metastatic breast cancer cells	182:211	metastatic breast cancer cells	182:211	Human lysyl oxidase-like 2 (hLOXL2) is highly up-regulated in metastatic breast cancer cells and tissues and induces epithelial-to-mesenchymal transition, the first step of metastasis/invasion.
23319596	6	51	link	N-linked	1013:1020	arg1	glycans					1022:1028	N-linked glycans	1013:1028	N-linked glycans at Asn-455 and Asn-644	1013:1051	After phenylhydrazine derivatization and trypsin digestion, we used mass spectrometry to identify peptides containing the derivatized lysine tyrosylquinone cross-link at Lys-653 and Tyr-689, as well as N-linked glycans at Asn-455 and Asn-644.
23319596	2	52	theme	LOX	437:439	arg1	hloxl2					314:319	hloxl2	314:319	hloxl2	314:319	hloxl2 encodes four N-terminal scavenger receptor cysteine-rich domains and the highly conserved C-terminal lysyl oxidase (LOX) catalytic domain.
23319596	2	52	theme	LOX	437:439	arg1	domain					452:457	the highly conserved C-terminal lysyl oxidase (LOX) catalytic domain	390:457	the highly conserved C-terminal lysyl oxidase (LOX) catalytic domain	390:457	hloxl2 encodes four N-terminal scavenger receptor cysteine-rich domains and the highly conserved C-terminal lysyl oxidase (LOX) catalytic domain.
23319596	0	53	theme	human	48:52	arg1	lysyl					54:58	recombinant human lysyl oxidase-like 2	36:73	recombinant human lysyl oxidase-like 2 (rhLOXL2)	36:83	Post-translational modifications of recombinant human lysyl oxidase-like 2 (rhLOXL2) secreted from Drosophila S2 cells.
23319596	0	53	theme	human	48:52	arg1	rhLOXL2					76:82	rhLOXL2	76:82	rhLOXL2	76:82	Post-translational modifications of recombinant human lysyl oxidase-like 2 (rhLOXL2) secreted from Drosophila S2 cells.
23319596	10	54	dep	solubility	1598:1607	arg1	the					1594:1596	the	1594:1596	the	1594:1596	These results suggest that the N-glycan at Asn-644 of hLOXL2 enhances the solubility and stability of the LOX catalytic domain.
23319596	8	55	theme	catalytic	1281:1289	arg1	domain					1291:1296	the LOX catalytic domain	1273:1296	the LOX catalytic domain	1273:1296	The N-glycosylation site at Asn-644 in the LOX catalytic domain is not conserved in human LOX (hLOX), although the LOX catalytic domain of hLOX shares ∼50% identity and ∼70% homology with hLOXL2.
23319596	7	56	theme	N-glycosylation	1068:1082	arg1	Disruption					1054:1063	Disruption	1054:1063	Disruption of N-glycosylation by site-directed mutagenesis or tunicamycin treatment	1054:1136	Disruption of N-glycosylation by site-directed mutagenesis or tunicamycin treatment completely inhibited secretion so that only small quantities of inclusion bodies were detected.
23319596	6	57	contain	containing	918:927	arg1	peptides					909:916	peptides	909:916	peptides containing the derivatized lysine tyrosylquinone cross-link at Lys-653 and Tyr-689	909:999	After phenylhydrazine derivatization and trypsin digestion, we used mass spectrometry to identify peptides containing the derivatized lysine tyrosylquinone cross-link at Lys-653 and Tyr-689, as well as N-linked glycans at Asn-455 and Asn-644.
23319596	6	57	contain	containing	918:927	arg2	cross-link					967:976	the derivatized lysine tyrosylquinone cross-link	929:976	the derivatized lysine tyrosylquinone cross-link	929:976	After phenylhydrazine derivatization and trypsin digestion, we used mass spectrometry to identify peptides containing the derivatized lysine tyrosylquinone cross-link at Lys-653 and Tyr-689, as well as N-linked glycans at Asn-455 and Asn-644.
23319596	8	58	theme	LOX	1349:1351	arg1	hLOX					1373:1376	hLOX	1373:1376	hLOX	1373:1376	The N-glycosylation site at Asn-644 in the LOX catalytic domain is not conserved in human LOX (hLOX), although the LOX catalytic domain of hLOX shares ∼50% identity and ∼70% homology with hLOXL2.
23319596	8	58	theme	LOX	1349:1351	arg1	domain					1363:1368	the LOX catalytic domain	1345:1368	the LOX catalytic domain of hLOX	1345:1376	The N-glycosylation site at Asn-644 in the LOX catalytic domain is not conserved in human LOX (hLOX), although the LOX catalytic domain of hLOX shares ∼50% identity and ∼70% homology with hLOXL2.
23319596	5	59	theme	recombinant	744:754	arg1	proteins					756:763	The recombinant proteins	740:763	The recombinant proteins	740:763	The recombinant proteins also show activity in tropoelastin oxidation.
23319596	10	60	theme	N-glycan	1555:1562	arg1	Asn-644					1567:1573	the N-glycan at Asn-644	1551:1573	the N-glycan at Asn-644 of hLOXL2	1551:1583	These results suggest that the N-glycan at Asn-644 of hLOXL2 enhances the solubility and stability of the LOX catalytic domain.
23319596	4	61	dep	LOX	662:664	arg1	contrast					650:657	contrast	650:657	contrast	650:657	The recombinant proteins are soluble, in contrast to LOX, which is consistently reported to require 2-6 m urea for solubilization.
23319596	2	62	theme	cysteine-rich	364:376	arg1	hloxl2					314:319	hloxl2	314:319	hloxl2	314:319	hloxl2 encodes four N-terminal scavenger receptor cysteine-rich domains and the highly conserved C-terminal lysyl oxidase (LOX) catalytic domain.
23319596	2	62	theme	cysteine-rich	364:376	arg1	domains					378:384	four N-terminal scavenger receptor cysteine-rich domains	329:384	four N-terminal scavenger receptor cysteine-rich domains	329:384	hloxl2 encodes four N-terminal scavenger receptor cysteine-rich domains and the highly conserved C-terminal lysyl oxidase (LOX) catalytic domain.
23319596	0	63	theme	oxidase-like	60:71	arg1	lysyl					54:58	recombinant human lysyl oxidase-like 2	36:73	recombinant human lysyl oxidase-like 2 (rhLOXL2)	36:83	Post-translational modifications of recombinant human lysyl oxidase-like 2 (rhLOXL2) secreted from Drosophila S2 cells.
23319596	0	63	theme	oxidase-like	60:71	arg1	rhLOXL2					76:82	rhLOXL2	76:82	rhLOXL2	76:82	Post-translational modifications of recombinant human lysyl oxidase-like 2 (rhLOXL2) secreted from Drosophila S2 cells.
23319596	7	64	theme	tunicamycin	1116:1126	arg1	treatment					1128:1136	tunicamycin treatment	1116:1136	tunicamycin treatment	1116:1136	Disruption of N-glycosylation by site-directed mutagenesis or tunicamycin treatment completely inhibited secretion so that only small quantities of inclusion bodies were detected.
23319596	8	65	from	Asn-644	1262:1268	arg1	site					1254:1257	The N-glycosylation site	1234:1257	The N-glycosylation site at Asn-644 in the LOX catalytic domain	1234:1296	The N-glycosylation site at Asn-644 in the LOX catalytic domain is not conserved in human LOX (hLOX), although the LOX catalytic domain of hLOX shares ∼50% identity and ∼70% homology with hLOXL2.
23319596	6	66	from	Asn-455	1033:1039	arg1	glycans					1022:1028	N-linked glycans	1013:1028	N-linked glycans at Asn-455 and Asn-644	1013:1051	After phenylhydrazine derivatization and trypsin digestion, we used mass spectrometry to identify peptides containing the derivatized lysine tyrosylquinone cross-link at Lys-653 and Tyr-689, as well as N-linked glycans at Asn-455 and Asn-644.
23319596	6	66	from	Asn-455	1033:1039	arg1	peptides					909:916	peptides	909:916	peptides containing the derivatized lysine tyrosylquinone cross-link at Lys-653 and Tyr-689	909:999	After phenylhydrazine derivatization and trypsin digestion, we used mass spectrometry to identify peptides containing the derivatized lysine tyrosylquinone cross-link at Lys-653 and Tyr-689, as well as N-linked glycans at Asn-455 and Asn-644.
23319596	10	67	theme	domain	1644:1649	arg1	stability					1613:1621	stability	1613:1621	stability	1613:1621	These results suggest that the N-glycan at Asn-644 of hLOXL2 enhances the solubility and stability of the LOX catalytic domain.
23319596	10	67	theme	domain	1644:1649	arg1	solubility					1598:1607	solubility	1598:1607	solubility	1598:1607	These results suggest that the N-glycan at Asn-644 of hLOXL2 enhances the solubility and stability of the LOX catalytic domain.
23319596	1	68	theme	Human	120:124	arg1	lysyl					126:130	Human lysyl oxidase-like 2	120:145	Human lysyl oxidase-like 2 (hLOXL2)	120:154	Human lysyl oxidase-like 2 (hLOXL2) is highly up-regulated in metastatic breast cancer cells and tissues and induces epithelial-to-mesenchymal transition, the first step of metastasis/invasion.
23319596	1	68	theme	Human	120:124	arg1	hLOXL2					148:153	hLOXL2	148:153	hLOXL2	148:153	Human lysyl oxidase-like 2 (hLOXL2) is highly up-regulated in metastatic breast cancer cells and tissues and induces epithelial-to-mesenchymal transition, the first step of metastasis/invasion.
23319596	7	69	theme	site-directed	1087:1099	arg1	mutagenesis					1101:1111	site-directed mutagenesis	1087:1111	site-directed mutagenesis	1087:1111	Disruption of N-glycosylation by site-directed mutagenesis or tunicamycin treatment completely inhibited secretion so that only small quantities of inclusion bodies were detected.
23319596	6	70	theme	mass	879:882	arg1	spectrometry					884:895	mass spectrometry	879:895	mass spectrometry	879:895	After phenylhydrazine derivatization and trypsin digestion, we used mass spectrometry to identify peptides containing the derivatized lysine tyrosylquinone cross-link at Lys-653 and Tyr-689, as well as N-linked glycans at Asn-455 and Asn-644.
23319596	2	71	theme	scavenger	345:353	arg1	hloxl2					314:319	hloxl2	314:319	hloxl2	314:319	hloxl2 encodes four N-terminal scavenger receptor cysteine-rich domains and the highly conserved C-terminal lysyl oxidase (LOX) catalytic domain.
23319596	2	71	theme	scavenger	345:353	arg1	domains					378:384	four N-terminal scavenger receptor cysteine-rich domains	329:384	four N-terminal scavenger receptor cysteine-rich domains	329:384	hloxl2 encodes four N-terminal scavenger receptor cysteine-rich domains and the highly conserved C-terminal lysyl oxidase (LOX) catalytic domain.
23319596	8	72	from	site	1254:1257	arg1	domain					1291:1296	the LOX catalytic domain	1273:1296	the LOX catalytic domain	1273:1296	The N-glycosylation site at Asn-644 in the LOX catalytic domain is not conserved in human LOX (hLOX), although the LOX catalytic domain of hLOX shares ∼50% identity and ∼70% homology with hLOXL2.
23319596	8	73	theme	hLOX	1373:1376	arg1	hLOX					1373:1376	hLOX	1373:1376	hLOX	1373:1376	The N-glycosylation site at Asn-644 in the LOX catalytic domain is not conserved in human LOX (hLOX), although the LOX catalytic domain of hLOX shares ∼50% identity and ∼70% homology with hLOXL2.
23319596	8	73	theme	hLOX	1373:1376	arg1	domain					1363:1368	the LOX catalytic domain	1345:1368	the LOX catalytic domain of hLOX	1345:1376	The N-glycosylation site at Asn-644 in the LOX catalytic domain is not conserved in human LOX (hLOX), although the LOX catalytic domain of hLOX shares ∼50% identity and ∼70% homology with hLOXL2.
23319596	8	74	gly	N-glycosylation	1238:1252	arg2	Asn-644					1262:1268	Asn-644	1262:1268	Asn-644	1262:1268	The N-glycosylation site at Asn-644 in the LOX catalytic domain is not conserved in human LOX (hLOX), although the LOX catalytic domain of hLOX shares ∼50% identity and ∼70% homology with hLOXL2.
23319596	8	74	gly	N-glycosylation	1238:1252	arg2	site					1254:1257	The N-glycosylation site	1234:1257	The N-glycosylation site at Asn-644 in the LOX catalytic domain	1234:1296	The N-glycosylation site at Asn-644 in the LOX catalytic domain is not conserved in human LOX (hLOX), although the LOX catalytic domain of hLOX shares ∼50% identity and ∼70% homology with hLOXL2.
23319596	2	75	theme	N-terminal	334:343	arg1	hloxl2					314:319	hloxl2	314:319	hloxl2	314:319	hloxl2 encodes four N-terminal scavenger receptor cysteine-rich domains and the highly conserved C-terminal lysyl oxidase (LOX) catalytic domain.
23319596	2	75	theme	N-terminal	334:343	arg1	domains					378:384	four N-terminal scavenger receptor cysteine-rich domains	329:384	four N-terminal scavenger receptor cysteine-rich domains	329:384	hloxl2 encodes four N-terminal scavenger receptor cysteine-rich domains and the highly conserved C-terminal lysyl oxidase (LOX) catalytic domain.
23319596	9	76	theme	expression	1505:1514	arg1	system					1516:1521	the same expression system	1496:1521	the same expression system	1496:1521	The catalytic domain of hLOX was not secreted from S2 cells using the same expression system.
23319596	2	77	theme	receptor	355:362	arg1	hloxl2					314:319	hloxl2	314:319	hloxl2	314:319	hloxl2 encodes four N-terminal scavenger receptor cysteine-rich domains and the highly conserved C-terminal lysyl oxidase (LOX) catalytic domain.
23319596	2	77	theme	receptor	355:362	arg1	domains					378:384	four N-terminal scavenger receptor cysteine-rich domains	329:384	four N-terminal scavenger receptor cysteine-rich domains	329:384	hloxl2 encodes four N-terminal scavenger receptor cysteine-rich domains and the highly conserved C-terminal lysyl oxidase (LOX) catalytic domain.
23319596	2	78	theme	catalytic	442:450	arg1	hloxl2					314:319	hloxl2	314:319	hloxl2	314:319	hloxl2 encodes four N-terminal scavenger receptor cysteine-rich domains and the highly conserved C-terminal lysyl oxidase (LOX) catalytic domain.
23319596	2	78	theme	catalytic	442:450	arg1	domain					452:457	the highly conserved C-terminal lysyl oxidase (LOX) catalytic domain	390:457	the highly conserved C-terminal lysyl oxidase (LOX) catalytic domain	390:457	hloxl2 encodes four N-terminal scavenger receptor cysteine-rich domains and the highly conserved C-terminal lysyl oxidase (LOX) catalytic domain.
23319596	4	79	theme	2-6	709:711	arg1	m					713:713	m	713:713	m	713:713	The recombinant proteins are soluble, in contrast to LOX, which is consistently reported to require 2-6 m urea for solubilization.
23319596	8	80	with	identity	1390:1397	arg1	hLOXL2					1422:1427	hLOXL2	1422:1427	hLOXL2	1422:1427	The N-glycosylation site at Asn-644 in the LOX catalytic domain is not conserved in human LOX (hLOX), although the LOX catalytic domain of hLOX shares ∼50% identity and ∼70% homology with hLOXL2.
23319596	9	81	theme	catalytic	1434:1442	arg1	hLOX					1454:1457	hLOX	1454:1457	hLOX	1454:1457	The catalytic domain of hLOX was not secreted from S2 cells using the same expression system.
23319596	9	81	theme	catalytic	1434:1442	arg1	domain					1444:1449	The catalytic domain	1430:1449	The catalytic domain of hLOX	1430:1457	The catalytic domain of hLOX was not secreted from S2 cells using the same expression system.
23319596	9	82	theme	same	1500:1503	arg1	system					1516:1521	the same expression system	1496:1521	the same expression system	1496:1521	The catalytic domain of hLOX was not secreted from S2 cells using the same expression system.
23319596	3	83	theme	truncated	545:553	arg1	proteins					567:574	truncated recombinant proteins	545:574	truncated recombinant proteins produced in Drosophila S2 cells	545:606	Here, we assessed the extent of the post-translational modifications of hLOXL2 using truncated recombinant proteins produced in Drosophila S2 cells.
23319596	3	84	theme	modifications	515:527	arg1	extent					482:487	the extent	478:487	the extent of the post-translational modifications of hLOXL2	478:537	Here, we assessed the extent of the post-translational modifications of hLOXL2 using truncated recombinant proteins produced in Drosophila S2 cells.
22678432	2	0	gly	glycopeptides	345:357	arg2	glycopeptides					345:357	glycopeptides	345:357	glycopeptides	345:357	This protocol describes workflows for the characterization of glycopeptides and their site-specific heterogeneity, showing examples of the analysis of recombinant human erythropoietin (rHuEPO), α1-proteinase inhibitor (A1PI) and immunoglobulin (IgG).
22678432	7	1	theme	detailed	1313:1320	arg1	information					1340:1350	complementary detailed glycan structural information	1299:1350	complementary detailed glycan structural information that facilitates characterization of the glycopeptides	1299:1405	The data obtained from analyzing released glycans of rHuEPO and IgG, described in the second protocol of this series (10.1038/nprot.2012.063), provide complementary detailed glycan structural information that facilitates characterization of the glycopeptides.
22678432	3	2	theme	interest	551:558	arg1	Glycoproteins					534:546	Glycoproteins	534:546	Glycoproteins of interest	534:558	Glycoproteins of interest can be proteolytically digested either in solution or in-gel after electrophoretic separation, and the (glyco)peptides are analyzed by capillary/nano-liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS).
22678432	7	3	theme	glycan	1322:1327	arg1	information					1340:1350	complementary detailed glycan structural information	1299:1350	complementary detailed glycan structural information that facilitates characterization of the glycopeptides	1299:1405	The data obtained from analyzing released glycans of rHuEPO and IgG, described in the second protocol of this series (10.1038/nprot.2012.063), provide complementary detailed glycan structural information that facilitates characterization of the glycopeptides.
22678432	1	4	gly	glycoprotein	256:267	arg1	glycoprotein					256:267	recombinant glycoprotein therapeutics	244:280	recombinant glycoprotein therapeutics	244:280	The comprehensive analysis of protein glycosylation is a major requirement for understanding glycoprotein function in biological systems, and is a prerequisite for producing recombinant glycoprotein therapeutics.
22678432	1	5	theme	biological	188:197	arg1	systems					199:205	biological systems	188:205	biological systems	188:205	The comprehensive analysis of protein glycosylation is a major requirement for understanding glycoprotein function in biological systems, and is a prerequisite for producing recombinant glycoprotein therapeutics.
22678432	4	6	theme	glycopeptide	819:830	arg1	chromatography					889:902	hydrophilic interaction liquid chromatography	858:902	hydrophilic interaction liquid chromatography (HILIC)	858:910	If required, specific glycopeptide enrichment steps, such as hydrophilic interaction liquid chromatography (HILIC), can also be performed.
22678432	4	6	theme	glycopeptide	819:830	arg1	steps					843:847	specific glycopeptide enrichment steps	810:847	specific glycopeptide enrichment steps	810:847	If required, specific glycopeptide enrichment steps, such as hydrophilic interaction liquid chromatography (HILIC), can also be performed.
22678432	0	7	from	Determination	0:12	arg1	glycoproteins					55:67	glycoproteins	55:67	glycoproteins	55:67	Determination of site-specific glycan heterogeneity on glycoproteins.
22678432	7	8	theme	IgG	1212:1214	arg1	glycans					1190:1196	released glycans	1181:1196	released glycans of rHuEPO and IgG, described in the second protocol of this series (10.1038/nprot.2012.063),	1181:1289	The data obtained from analyzing released glycans of rHuEPO and IgG, described in the second protocol of this series (10.1038/nprot.2012.063), provide complementary detailed glycan structural information that facilitates characterization of the glycopeptides.
22678432	5	9	theme	data	969:972	arg1	interpretation					974:987	data interpretation	969:987	data interpretation	969:987	Particular emphasis is placed on data interpretation and the determination of site-specific glycan heterogeneity.
22678432	4	10	theme	enrichment	832:841	arg1	chromatography					889:902	hydrophilic interaction liquid chromatography	858:902	hydrophilic interaction liquid chromatography (HILIC)	858:910	If required, specific glycopeptide enrichment steps, such as hydrophilic interaction liquid chromatography (HILIC), can also be performed.
22678432	4	10	theme	enrichment	832:841	arg1	steps					843:847	specific glycopeptide enrichment steps	810:847	specific glycopeptide enrichment steps	810:847	If required, specific glycopeptide enrichment steps, such as hydrophilic interaction liquid chromatography (HILIC), can also be performed.
22678432	2	11	theme	site-specific	369:381	arg1	heterogeneity					383:395	their site-specific heterogeneity	363:395	their site-specific heterogeneity	363:395	This protocol describes workflows for the characterization of glycopeptides and their site-specific heterogeneity, showing examples of the analysis of recombinant human erythropoietin (rHuEPO), α1-proteinase inhibitor (A1PI) and immunoglobulin (IgG).
22678432	1	12	theme	comprehensive	74:86	arg1	analysis					88:95	The comprehensive analysis	70:95	The comprehensive analysis of protein glycosylation	70:120	The comprehensive analysis of protein glycosylation is a major requirement for understanding glycoprotein function in biological systems, and is a prerequisite for producing recombinant glycoprotein therapeutics.
22678432	1	12	theme	comprehensive	74:86	arg1	requirement					133:143	a major requirement	125:143	a major requirement for understanding glycoprotein function in biological systems	125:205	The comprehensive analysis of protein glycosylation is a major requirement for understanding glycoprotein function in biological systems, and is a prerequisite for producing recombinant glycoprotein therapeutics.
22678432	5	13	theme	site-specific	1014:1026	arg1	heterogeneity					1035:1047	site-specific glycan heterogeneity	1014:1047	site-specific glycan heterogeneity	1014:1047	Particular emphasis is placed on data interpretation and the determination of site-specific glycan heterogeneity.
22678432	7	14	theme	rHuEPO	1201:1206	arg1	glycans					1190:1196	released glycans	1181:1196	released glycans of rHuEPO and IgG, described in the second protocol of this series (10.1038/nprot.2012.063),	1181:1289	The data obtained from analyzing released glycans of rHuEPO and IgG, described in the second protocol of this series (10.1038/nprot.2012.063), provide complementary detailed glycan structural information that facilitates characterization of the glycopeptides.
22678432	1	15	from	function	176:183	arg1	systems					199:205	biological systems	188:205	biological systems	188:205	The comprehensive analysis of protein glycosylation is a major requirement for understanding glycoprotein function in biological systems, and is a prerequisite for producing recombinant glycoprotein therapeutics.
22678432	4	16	theme	hydrophilic	858:868	arg1	chromatography					889:902	hydrophilic interaction liquid chromatography	858:902	hydrophilic interaction liquid chromatography (HILIC)	858:910	If required, specific glycopeptide enrichment steps, such as hydrophilic interaction liquid chromatography (HILIC), can also be performed.
22678432	4	16	theme	hydrophilic	858:868	arg1	HILIC					905:909	HILIC	905:909	HILIC	905:909	If required, specific glycopeptide enrichment steps, such as hydrophilic interaction liquid chromatography (HILIC), can also be performed.
22678432	5	17	theme	Particular	936:945	arg1	emphasis					947:954	Particular emphasis	936:954	Particular emphasis	936:954	Particular emphasis is placed on data interpretation and the determination of site-specific glycan heterogeneity.
22678432	7	18	theme	released	1181:1188	arg1	glycans					1190:1196	released glycans	1181:1196	released glycans of rHuEPO and IgG, described in the second protocol of this series (10.1038/nprot.2012.063),	1181:1289	The data obtained from analyzing released glycans of rHuEPO and IgG, described in the second protocol of this series (10.1038/nprot.2012.063), provide complementary detailed glycan structural information that facilitates characterization of the glycopeptides.
22678432	5	19	theme	glycan	1028:1033	arg1	heterogeneity					1035:1047	site-specific glycan heterogeneity	1014:1047	site-specific glycan heterogeneity	1014:1047	Particular emphasis is placed on data interpretation and the determination of site-specific glycan heterogeneity.
22678432	2	20	theme	erythropoietin	452:465	arg1	analysis					422:429	the analysis	418:429	the analysis of recombinant human erythropoietin (rHuEPO), α1-proteinase inhibitor (A1PI) and immunoglobulin (IgG)	418:531	This protocol describes workflows for the characterization of glycopeptides and their site-specific heterogeneity, showing examples of the analysis of recombinant human erythropoietin (rHuEPO), α1-proteinase inhibitor (A1PI) and immunoglobulin (IgG).
22678432	1	21	theme	protein	100:106	arg1	glycosylation					108:120	protein glycosylation	100:120	protein glycosylation	100:120	The comprehensive analysis of protein glycosylation is a major requirement for understanding glycoprotein function in biological systems, and is a prerequisite for producing recombinant glycoprotein therapeutics.
22678432	7	22	theme	glycopeptides	1393:1405	arg1	characterization					1369:1384	characterization	1369:1384	characterization of the glycopeptides	1369:1405	The data obtained from analyzing released glycans of rHuEPO and IgG, described in the second protocol of this series (10.1038/nprot.2012.063), provide complementary detailed glycan structural information that facilitates characterization of the glycopeptides.
22678432	2	23	theme	human	446:450	arg1	erythropoietin					452:465	recombinant human erythropoietin	434:465	recombinant human erythropoietin (rHuEPO)	434:474	This protocol describes workflows for the characterization of glycopeptides and their site-specific heterogeneity, showing examples of the analysis of recombinant human erythropoietin (rHuEPO), α1-proteinase inhibitor (A1PI) and immunoglobulin (IgG).
22678432	2	23	theme	human	446:450	arg1	rHuEPO					468:473	rHuEPO	468:473	rHuEPO	468:473	This protocol describes workflows for the characterization of glycopeptides and their site-specific heterogeneity, showing examples of the analysis of recombinant human erythropoietin (rHuEPO), α1-proteinase inhibitor (A1PI) and immunoglobulin (IgG).
22678432	6	24	theme	data	1133:1136	arg1	analysis					1138:1145	data analysis	1133:1145	data analysis	1133:1145	The described workflow takes approximately 3-5 d, including sample preparation and data analysis.
22678432	1	25	theme	glycosylation	108:120	arg1	analysis					88:95	The comprehensive analysis	70:95	The comprehensive analysis of protein glycosylation	70:120	The comprehensive analysis of protein glycosylation is a major requirement for understanding glycoprotein function in biological systems, and is a prerequisite for producing recombinant glycoprotein therapeutics.
22678432	1	25	theme	glycosylation	108:120	arg1	requirement					133:143	a major requirement	125:143	a major requirement for understanding glycoprotein function in biological systems	125:205	The comprehensive analysis of protein glycosylation is a major requirement for understanding glycoprotein function in biological systems, and is a prerequisite for producing recombinant glycoprotein therapeutics.
22678432	2	26	theme	recombinant	434:444	arg1	erythropoietin					452:465	recombinant human erythropoietin	434:465	recombinant human erythropoietin (rHuEPO)	434:474	This protocol describes workflows for the characterization of glycopeptides and their site-specific heterogeneity, showing examples of the analysis of recombinant human erythropoietin (rHuEPO), α1-proteinase inhibitor (A1PI) and immunoglobulin (IgG).
22678432	2	26	theme	recombinant	434:444	arg1	rHuEPO					468:473	rHuEPO	468:473	rHuEPO	468:473	This protocol describes workflows for the characterization of glycopeptides and their site-specific heterogeneity, showing examples of the analysis of recombinant human erythropoietin (rHuEPO), α1-proteinase inhibitor (A1PI) and immunoglobulin (IgG).
22678432	0	27	theme	glycan	31:36	arg1	heterogeneity					38:50	site-specific glycan heterogeneity	17:50	site-specific glycan heterogeneity	17:50	Determination of site-specific glycan heterogeneity on glycoproteins.
22678432	4	28	theme	specific	810:817	arg1	chromatography					889:902	hydrophilic interaction liquid chromatography	858:902	hydrophilic interaction liquid chromatography (HILIC)	858:910	If required, specific glycopeptide enrichment steps, such as hydrophilic interaction liquid chromatography (HILIC), can also be performed.
22678432	4	28	theme	specific	810:817	arg1	steps					843:847	specific glycopeptide enrichment steps	810:847	specific glycopeptide enrichment steps	810:847	If required, specific glycopeptide enrichment steps, such as hydrophilic interaction liquid chromatography (HILIC), can also be performed.
22678432	2	29	theme	α1-proteinase	477:489	arg1	A1PI					502:505	A1PI	502:505	A1PI	502:505	This protocol describes workflows for the characterization of glycopeptides and their site-specific heterogeneity, showing examples of the analysis of recombinant human erythropoietin (rHuEPO), α1-proteinase inhibitor (A1PI) and immunoglobulin (IgG).
22678432	2	29	theme	α1-proteinase	477:489	arg1	inhibitor					491:499	α1-proteinase inhibitor	477:499	α1-proteinase inhibitor (A1PI)	477:506	This protocol describes workflows for the characterization of glycopeptides and their site-specific heterogeneity, showing examples of the analysis of recombinant human erythropoietin (rHuEPO), α1-proteinase inhibitor (A1PI) and immunoglobulin (IgG).
22678432	2	30	theme	inhibitor	491:499	arg1	analysis					422:429	the analysis	418:429	the analysis of recombinant human erythropoietin (rHuEPO), α1-proteinase inhibitor (A1PI) and immunoglobulin (IgG)	418:531	This protocol describes workflows for the characterization of glycopeptides and their site-specific heterogeneity, showing examples of the analysis of recombinant human erythropoietin (rHuEPO), α1-proteinase inhibitor (A1PI) and immunoglobulin (IgG).
22678432	5	31	theme	heterogeneity	1035:1047	arg1	interpretation					974:987	data interpretation	969:987	data interpretation	969:987	Particular emphasis is placed on data interpretation and the determination of site-specific glycan heterogeneity.
22678432	5	31	theme	heterogeneity	1035:1047	arg1	determination					997:1009	the determination	993:1009	the determination of site-specific glycan heterogeneity	993:1047	Particular emphasis is placed on data interpretation and the determination of site-specific glycan heterogeneity.
22678432	2	32	theme	glycopeptides	345:357	arg1	characterization					325:340	the characterization	321:340	the characterization of glycopeptides and their site-specific heterogeneity	321:395	This protocol describes workflows for the characterization of glycopeptides and their site-specific heterogeneity, showing examples of the analysis of recombinant human erythropoietin (rHuEPO), α1-proteinase inhibitor (A1PI) and immunoglobulin (IgG).
22678432	6	33	theme	described	1054:1062	arg1	workflow					1064:1071	The described workflow	1050:1071	The described workflow	1050:1071	The described workflow takes approximately 3-5 d, including sample preparation and data analysis.
22678432	3	34	theme	capillary/nano-liquid	695:715	arg1	LC-ESI-MS/MS					782:793	LC-ESI-MS/MS	782:793	LC-ESI-MS/MS	782:793	Glycoproteins of interest can be proteolytically digested either in solution or in-gel after electrophoretic separation, and the (glyco)peptides are analyzed by capillary/nano-liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS).
22678432	3	34	theme	capillary/nano-liquid	695:715	arg1	spectrometry					768:779	capillary/nano-liquid chromatography-electrospray ionization tandem mass spectrometry	695:779	capillary/nano-liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS)	695:794	Glycoproteins of interest can be proteolytically digested either in solution or in-gel after electrophoretic separation, and the (glyco)peptides are analyzed by capillary/nano-liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS).
22678432	3	35	theme	electrophoretic	627:641	arg1	separation					643:652	electrophoretic separation	627:652	electrophoretic separation	627:652	Glycoproteins of interest can be proteolytically digested either in solution or in-gel after electrophoretic separation, and the (glyco)peptides are analyzed by capillary/nano-liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS).
22678432	0	36	theme	heterogeneity	38:50	arg1	Determination					0:12	Determination	0:12	Determination of site-specific glycan heterogeneity on glycoproteins	0:67	Determination of site-specific glycan heterogeneity on glycoproteins.
22678432	6	37	theme	sample	1110:1115	arg1	preparation					1117:1127	sample preparation	1110:1127	sample preparation	1110:1127	The described workflow takes approximately 3-5 d, including sample preparation and data analysis.
22678432	2	38	theme	immunoglobulin	512:525	arg1	analysis					422:429	the analysis	418:429	the analysis of recombinant human erythropoietin (rHuEPO), α1-proteinase inhibitor (A1PI) and immunoglobulin (IgG)	418:531	This protocol describes workflows for the characterization of glycopeptides and their site-specific heterogeneity, showing examples of the analysis of recombinant human erythropoietin (rHuEPO), α1-proteinase inhibitor (A1PI) and immunoglobulin (IgG).
22678432	7	39	theme	complementary	1299:1311	arg1	information					1340:1350	complementary detailed glycan structural information	1299:1350	complementary detailed glycan structural information that facilitates characterization of the glycopeptides	1299:1405	The data obtained from analyzing released glycans of rHuEPO and IgG, described in the second protocol of this series (10.1038/nprot.2012.063), provide complementary detailed glycan structural information that facilitates characterization of the glycopeptides.
22678432	1	40	theme	major	127:131	arg1	analysis					88:95	The comprehensive analysis	70:95	The comprehensive analysis of protein glycosylation	70:120	The comprehensive analysis of protein glycosylation is a major requirement for understanding glycoprotein function in biological systems, and is a prerequisite for producing recombinant glycoprotein therapeutics.
22678432	1	40	theme	major	127:131	arg1	requirement					133:143	a major requirement	125:143	a major requirement for understanding glycoprotein function in biological systems	125:205	The comprehensive analysis of protein glycosylation is a major requirement for understanding glycoprotein function in biological systems, and is a prerequisite for producing recombinant glycoprotein therapeutics.
22678432	7	41	theme	second	1234:1239	arg1	protocol					1241:1248	the second protocol	1230:1248	the second protocol of this series (10.1038/nprot.2012.063)	1230:1288	The data obtained from analyzing released glycans of rHuEPO and IgG, described in the second protocol of this series (10.1038/nprot.2012.063), provide complementary detailed glycan structural information that facilitates characterization of the glycopeptides.
22678432	1	42	gly	glycoprotein	163:174	arg1	glycoprotein					163:174	glycoprotein function	163:183	glycoprotein function in biological systems	163:205	The comprehensive analysis of protein glycosylation is a major requirement for understanding glycoprotein function in biological systems, and is a prerequisite for producing recombinant glycoprotein therapeutics.
22678432	3	43	theme	tandem	756:761	arg1	LC-ESI-MS/MS					782:793	LC-ESI-MS/MS	782:793	LC-ESI-MS/MS	782:793	Glycoproteins of interest can be proteolytically digested either in solution or in-gel after electrophoretic separation, and the (glyco)peptides are analyzed by capillary/nano-liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS).
22678432	3	43	theme	tandem	756:761	arg1	spectrometry					768:779	capillary/nano-liquid chromatography-electrospray ionization tandem mass spectrometry	695:779	capillary/nano-liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS)	695:794	Glycoproteins of interest can be proteolytically digested either in solution or in-gel after electrophoretic separation, and the (glyco)peptides are analyzed by capillary/nano-liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS).
22678432	7	44	theme	series	1258:1263	arg1	protocol					1241:1248	the second protocol	1230:1248	the second protocol of this series (10.1038/nprot.2012.063)	1230:1288	The data obtained from analyzing released glycans of rHuEPO and IgG, described in the second protocol of this series (10.1038/nprot.2012.063), provide complementary detailed glycan structural information that facilitates characterization of the glycopeptides.
22678432	3	45	theme	glyco	664:668	arg1	peptides					670:677	the (glyco)peptides	659:677	the (glyco)peptides	659:677	Glycoproteins of interest can be proteolytically digested either in solution or in-gel after electrophoretic separation, and the (glyco)peptides are analyzed by capillary/nano-liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS).
22678432	7	46	gly	glycopeptides	1393:1405	arg2	glycopeptides					1393:1405	the glycopeptides	1389:1405	the glycopeptides	1389:1405	The data obtained from analyzing released glycans of rHuEPO and IgG, described in the second protocol of this series (10.1038/nprot.2012.063), provide complementary detailed glycan structural information that facilitates characterization of the glycopeptides.
22678432	3	47	theme	mass	763:766	arg1	LC-ESI-MS/MS					782:793	LC-ESI-MS/MS	782:793	LC-ESI-MS/MS	782:793	Glycoproteins of interest can be proteolytically digested either in solution or in-gel after electrophoretic separation, and the (glyco)peptides are analyzed by capillary/nano-liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS).
22678432	3	47	theme	mass	763:766	arg1	spectrometry					768:779	capillary/nano-liquid chromatography-electrospray ionization tandem mass spectrometry	695:779	capillary/nano-liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS)	695:794	Glycoproteins of interest can be proteolytically digested either in solution or in-gel after electrophoretic separation, and the (glyco)peptides are analyzed by capillary/nano-liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS).
22678432	4	48	theme	liquid	882:887	arg1	chromatography					889:902	hydrophilic interaction liquid chromatography	858:902	hydrophilic interaction liquid chromatography (HILIC)	858:910	If required, specific glycopeptide enrichment steps, such as hydrophilic interaction liquid chromatography (HILIC), can also be performed.
22678432	4	48	theme	liquid	882:887	arg1	HILIC					905:909	HILIC	905:909	HILIC	905:909	If required, specific glycopeptide enrichment steps, such as hydrophilic interaction liquid chromatography (HILIC), can also be performed.
22678432	1	49	theme	recombinant	244:254	arg1	therapeutics					269:280	recombinant glycoprotein therapeutics	244:280	recombinant glycoprotein therapeutics	244:280	The comprehensive analysis of protein glycosylation is a major requirement for understanding glycoprotein function in biological systems, and is a prerequisite for producing recombinant glycoprotein therapeutics.
22678432	3	50	theme	chromatography-electrospray	717:743	arg1	LC-ESI-MS/MS					782:793	LC-ESI-MS/MS	782:793	LC-ESI-MS/MS	782:793	Glycoproteins of interest can be proteolytically digested either in solution or in-gel after electrophoretic separation, and the (glyco)peptides are analyzed by capillary/nano-liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS).
22678432	3	50	theme	chromatography-electrospray	717:743	arg1	spectrometry					768:779	capillary/nano-liquid chromatography-electrospray ionization tandem mass spectrometry	695:779	capillary/nano-liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS)	695:794	Glycoproteins of interest can be proteolytically digested either in solution or in-gel after electrophoretic separation, and the (glyco)peptides are analyzed by capillary/nano-liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS).
22678432	4	51	theme	interaction	870:880	arg1	chromatography					889:902	hydrophilic interaction liquid chromatography	858:902	hydrophilic interaction liquid chromatography (HILIC)	858:910	If required, specific glycopeptide enrichment steps, such as hydrophilic interaction liquid chromatography (HILIC), can also be performed.
22678432	4	51	theme	interaction	870:880	arg1	HILIC					905:909	HILIC	905:909	HILIC	905:909	If required, specific glycopeptide enrichment steps, such as hydrophilic interaction liquid chromatography (HILIC), can also be performed.
22678432	2	52	theme	heterogeneity	383:395	arg1	characterization					325:340	the characterization	321:340	the characterization of glycopeptides and their site-specific heterogeneity	321:395	This protocol describes workflows for the characterization of glycopeptides and their site-specific heterogeneity, showing examples of the analysis of recombinant human erythropoietin (rHuEPO), α1-proteinase inhibitor (A1PI) and immunoglobulin (IgG).
22678432	1	53	theme	glycoprotein	256:267	arg1	therapeutics					269:280	recombinant glycoprotein therapeutics	244:280	recombinant glycoprotein therapeutics	244:280	The comprehensive analysis of protein glycosylation is a major requirement for understanding glycoprotein function in biological systems, and is a prerequisite for producing recombinant glycoprotein therapeutics.
22678432	7	54	theme	structural	1329:1338	arg1	information					1340:1350	complementary detailed glycan structural information	1299:1350	complementary detailed glycan structural information that facilitates characterization of the glycopeptides	1299:1405	The data obtained from analyzing released glycans of rHuEPO and IgG, described in the second protocol of this series (10.1038/nprot.2012.063), provide complementary detailed glycan structural information that facilitates characterization of the glycopeptides.
22678432	3	55	theme	ionization	745:754	arg1	LC-ESI-MS/MS					782:793	LC-ESI-MS/MS	782:793	LC-ESI-MS/MS	782:793	Glycoproteins of interest can be proteolytically digested either in solution or in-gel after electrophoretic separation, and the (glyco)peptides are analyzed by capillary/nano-liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS).
22678432	3	55	theme	ionization	745:754	arg1	spectrometry					768:779	capillary/nano-liquid chromatography-electrospray ionization tandem mass spectrometry	695:779	capillary/nano-liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS)	695:794	Glycoproteins of interest can be proteolytically digested either in solution or in-gel after electrophoretic separation, and the (glyco)peptides are analyzed by capillary/nano-liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS).
22678432	0	56	gly	glycoproteins	55:67	arg1	glycoproteins					55:67	glycoproteins	55:67	glycoproteins	55:67	Determination of site-specific glycan heterogeneity on glycoproteins.
22678432	1	57	theme	glycoprotein	163:174	arg1	function					176:183	glycoprotein function	163:183	glycoprotein function in biological systems	163:205	The comprehensive analysis of protein glycosylation is a major requirement for understanding glycoprotein function in biological systems, and is a prerequisite for producing recombinant glycoprotein therapeutics.
22678432	0	58	theme	site-specific	17:29	arg1	heterogeneity					38:50	site-specific glycan heterogeneity	17:50	site-specific glycan heterogeneity	17:50	Determination of site-specific glycan heterogeneity on glycoproteins.
22678432	2	59	theme	analysis	422:429	arg1	examples					406:413	examples	406:413	examples of the analysis of recombinant human erythropoietin (rHuEPO), α1-proteinase inhibitor (A1PI) and immunoglobulin (IgG)	406:531	This protocol describes workflows for the characterization of glycopeptides and their site-specific heterogeneity, showing examples of the analysis of recombinant human erythropoietin (rHuEPO), α1-proteinase inhibitor (A1PI) and immunoglobulin (IgG).
22678432	4	60	gly	glycopeptide	819:830	arg2	glycopeptide					819:830	specific glycopeptide enrichment steps	810:847	specific glycopeptide enrichment steps	810:847	If required, specific glycopeptide enrichment steps, such as hydrophilic interaction liquid chromatography (HILIC), can also be performed.
11320094	3	0	gly	glycosylation	664:676	arg2	sites					678:682	the exocytoplasmic (extracellular/lumen) N-linked glycosylation sites	614:682	the exocytoplasmic (extracellular/lumen) N-linked glycosylation sites on ABCR	614:690	To delineate between several proposed membrane topological models, we have identified the exocytoplasmic (extracellular/lumen) N-linked glycosylation sites on ABCR.
11320094	1	1	theme	transporters	233:244	arg1	subclass					200:207	the ABCA subclass	191:207	the ABCA subclass of ATP binding cassette transporters	191:244	ABCR is a member of the ABCA subclass of ATP binding cassette transporters that is responsible for Stargardt macular disease and implicated in retinal transport across photoreceptor disc membranes.
11320094	6	2	theme	large	1249:1253	arg1	domain					1270:1275	a large exocytoplasmic domain	1247:1275	a large exocytoplasmic domain	1247:1275	This leads to a model in which each half has a transmembrane segment followed by a large exocytoplasmic domain, a multi-spanning membrane domain, and a nucleotide binding domain.
11320094	0	3	theme	Membrane	0:7	arg1	topology					9:16	Membrane topology	0:16	Membrane topology of the ATP binding cassette transporter ABCR and its relationship to ABC1 and related ABCA transporters: identification of N-linked glycosylation sites.	0:169	Membrane topology of the ATP binding cassette transporter ABCR and its relationship to ABC1 and related ABCA transporters: identification of N-linked glycosylation sites.
11320094	5	4	theme	600-amino	877:885	arg1	domain					907:912	a 600-amino acid exocytoplasmic domain	875:912	a 600-amino acid exocytoplasmic domain of the N-terminal half between the first transmembrane segment H1 and the first multi-spanning membrane domain	875:1023	Four sites reside in a 600-amino acid exocytoplasmic domain of the N-terminal half between the first transmembrane segment H1 and the first multi-spanning membrane domain, and four sites are in a 275-amino acid domain of the C half between transmembrane segment H7 and the second multi-spanning membrane domain.
11320094	5	4	theme	600-amino	877:885	arg1	half					932:935	the N-terminal half	917:935	the N-terminal half between the first transmembrane segment H1 and the first multi-spanning membrane domain	917:1023	Four sites reside in a 600-amino acid exocytoplasmic domain of the N-terminal half between the first transmembrane segment H1 and the first multi-spanning membrane domain, and four sites are in a 275-amino acid domain of the C half between transmembrane segment H7 and the second multi-spanning membrane domain.
11320094	7	5	theme	similar	1435:1441	arg1	topology					1452:1459	a similar membrane topology	1433:1459	a similar membrane topology based on sequence similarity to ABCR	1433:1496	Other ABCA transporters, including ABC1 linked to Tangier disease, are proposed to have a similar membrane topology based on sequence similarity to ABCR.
11320094	3	6	theme	topological	575:585	arg1	models					587:592	several proposed membrane topological models	549:592	several proposed membrane topological models	549:592	To delineate between several proposed membrane topological models, we have identified the exocytoplasmic (extracellular/lumen) N-linked glycosylation sites on ABCR.
11320094	5	7	theme	exocytoplasmic	892:905	arg1	domain					907:912	a 600-amino acid exocytoplasmic domain	875:912	a 600-amino acid exocytoplasmic domain of the N-terminal half between the first transmembrane segment H1 and the first multi-spanning membrane domain	875:1023	Four sites reside in a 600-amino acid exocytoplasmic domain of the N-terminal half between the first transmembrane segment H1 and the first multi-spanning membrane domain, and four sites are in a 275-amino acid domain of the C half between transmembrane segment H7 and the second multi-spanning membrane domain.
11320094	5	7	theme	exocytoplasmic	892:905	arg1	half					932:935	the N-terminal half	917:935	the N-terminal half between the first transmembrane segment H1 and the first multi-spanning membrane domain	917:1023	Four sites reside in a 600-amino acid exocytoplasmic domain of the N-terminal half between the first transmembrane segment H1 and the first multi-spanning membrane domain, and four sites are in a 275-amino acid domain of the C half between transmembrane segment H7 and the second multi-spanning membrane domain.
11320094	0	8	theme	ABCA	104:107	arg1	transporters					109:120	related ABCA transporters	96:120	related ABCA transporters	96:120	Membrane topology of the ATP binding cassette transporter ABCR and its relationship to ABC1 and related ABCA transporters: identification of N-linked glycosylation sites.
11320094	3	9	theme	proposed	557:564	arg1	models					587:592	several proposed membrane topological models	549:592	several proposed membrane topological models	549:592	To delineate between several proposed membrane topological models, we have identified the exocytoplasmic (extracellular/lumen) N-linked glycosylation sites on ABCR.
11320094	5	10	theme	half	1081:1084	arg1	domain					1065:1070	a 275-amino acid domain	1048:1070	a 275-amino acid domain of the C half between transmembrane segment H7	1048:1117	Four sites reside in a 600-amino acid exocytoplasmic domain of the N-terminal half between the first transmembrane segment H1 and the first multi-spanning membrane domain, and four sites are in a 275-amino acid domain of the C half between transmembrane segment H7 and the second multi-spanning membrane domain.
11320094	5	10	theme	half	1081:1084	arg1	domain					1158:1163	the second multi-spanning membrane domain	1123:1163	the second multi-spanning membrane domain	1123:1163	Four sites reside in a 600-amino acid exocytoplasmic domain of the N-terminal half between the first transmembrane segment H1 and the first multi-spanning membrane domain, and four sites are in a 275-amino acid domain of the C half between transmembrane segment H7 and the second multi-spanning membrane domain.
11320094	5	10	theme	half	1081:1084	arg1	half					1081:1084	the C half	1075:1084	the C half between transmembrane segment H7	1075:1117	Four sites reside in a 600-amino acid exocytoplasmic domain of the N-terminal half between the first transmembrane segment H1 and the first multi-spanning membrane domain, and four sites are in a 275-amino acid domain of the C half between transmembrane segment H7 and the second multi-spanning membrane domain.
11320094	1	11	theme	ABCA	195:198	arg1	subclass					200:207	the ABCA subclass	191:207	the ABCA subclass of ATP binding cassette transporters	191:244	ABCR is a member of the ABCA subclass of ATP binding cassette transporters that is responsible for Stargardt macular disease and implicated in retinal transport across photoreceptor disc membranes.
11320094	6	12	theme	transmembrane	1213:1225	arg1	segment					1227:1233	a transmembrane segment	1211:1233	a transmembrane segment followed by a large exocytoplasmic domain, a multi-spanning membrane domain, and a nucleotide binding domain	1211:1342	This leads to a model in which each half has a transmembrane segment followed by a large exocytoplasmic domain, a multi-spanning membrane domain, and a nucleotide binding domain.
11320094	5	13	theme	275-amino	1050:1058	arg1	domain					1065:1070	a 275-amino acid domain	1048:1070	a 275-amino acid domain of the C half between transmembrane segment H7	1048:1117	Four sites reside in a 600-amino acid exocytoplasmic domain of the N-terminal half between the first transmembrane segment H1 and the first multi-spanning membrane domain, and four sites are in a 275-amino acid domain of the C half between transmembrane segment H7 and the second multi-spanning membrane domain.
11320094	5	13	theme	275-amino	1050:1058	arg1	half					1081:1084	the C half	1075:1084	the C half between transmembrane segment H7	1075:1117	Four sites reside in a 600-amino acid exocytoplasmic domain of the N-terminal half between the first transmembrane segment H1 and the first multi-spanning membrane domain, and four sites are in a 275-amino acid domain of the C half between transmembrane segment H7 and the second multi-spanning membrane domain.
11320094	7	14	theme	ABCA	1351:1354	arg1	transporters					1356:1367	Other ABCA transporters	1345:1367	Other ABCA transporters	1345:1367	Other ABCA transporters, including ABC1 linked to Tangier disease, are proposed to have a similar membrane topology based on sequence similarity to ABCR.
11320094	7	14	theme	ABCA	1351:1354	arg1	ABC1					1380:1383	ABC1	1380:1383	ABC1 linked to Tangier disease	1380:1409	Other ABCA transporters, including ABC1 linked to Tangier disease, are proposed to have a similar membrane topology based on sequence similarity to ABCR.
11320094	4	15	theme	concanavalin	745:756	arg1	A					758:758	concanavalin A binding	745:766	concanavalin A binding	745:766	Using trypsin digestion, site-directed mutagenesis, concanavalin A binding, and endoglycosidase digestion, we show that ABCR contains eight glycosylation sites.
11320094	6	16	theme	membrane	1295:1302	arg1	domain					1304:1309	a multi-spanning membrane domain	1278:1309	a multi-spanning membrane domain	1278:1309	This leads to a model in which each half has a transmembrane segment followed by a large exocytoplasmic domain, a multi-spanning membrane domain, and a nucleotide binding domain.
11320094	5	17	theme	first	949:953	arg1	segment					969:975	the first transmembrane segment H1 and the first multi-spanning membrane domain	945:1023	segment	969:975	Four sites reside in a 600-amino acid exocytoplasmic domain of the N-terminal half between the first transmembrane segment H1 and the first multi-spanning membrane domain, and four sites are in a 275-amino acid domain of the C half between transmembrane segment H7 and the second multi-spanning membrane domain.
11320094	4	18	theme	trypsin	699:705	arg1	digestion					707:715	trypsin digestion	699:715	trypsin digestion	699:715	Using trypsin digestion, site-directed mutagenesis, concanavalin A binding, and endoglycosidase digestion, we show that ABCR contains eight glycosylation sites.
11320094	0	19	theme	ABCR	58:61	arg1	topology					9:16	Membrane topology	0:16	Membrane topology of the ATP binding cassette transporter ABCR and its relationship to ABC1 and related ABCA transporters: identification of N-linked glycosylation sites.	0:169	Membrane topology of the ATP binding cassette transporter ABCR and its relationship to ABC1 and related ABCA transporters: identification of N-linked glycosylation sites.
11320094	1	20	theme	retinal	314:320	arg1	transport					322:330	retinal transport	314:330	retinal transport across photoreceptor disc membranes	314:366	ABCR is a member of the ABCA subclass of ATP binding cassette transporters that is responsible for Stargardt macular disease and implicated in retinal transport across photoreceptor disc membranes.
11320094	0	21	theme	glycosylation	150:162	arg1	sites					164:168	N-linked glycosylation sites	141:168	N-linked glycosylation sites	141:168	Membrane topology of the ATP binding cassette transporter ABCR and its relationship to ABC1 and related ABCA transporters: identification of N-linked glycosylation sites.
11320094	7	22	attach	linked	1385:1390	arg1	disease					1403:1409	Tangier disease	1395:1409	Tangier disease	1395:1409	Other ABCA transporters, including ABC1 linked to Tangier disease, are proposed to have a similar membrane topology based on sequence similarity to ABCR.
11320094	7	22	attach	linked	1385:1390	arg2	ABC1					1380:1383	ABC1	1380:1383	ABC1 linked to Tangier disease	1380:1409	Other ABCA transporters, including ABC1 linked to Tangier disease, are proposed to have a similar membrane topology based on sequence similarity to ABCR.
11320094	5	23	theme	multi-spanning	1134:1147	arg1	domain					1158:1163	the second multi-spanning membrane domain	1123:1163	the second multi-spanning membrane domain	1123:1163	Four sites reside in a 600-amino acid exocytoplasmic domain of the N-terminal half between the first transmembrane segment H1 and the first multi-spanning membrane domain, and four sites are in a 275-amino acid domain of the C half between transmembrane segment H7 and the second multi-spanning membrane domain.
11320094	5	23	theme	multi-spanning	1134:1147	arg1	half					1081:1084	the C half	1075:1084	the C half between transmembrane segment H7	1075:1117	Four sites reside in a 600-amino acid exocytoplasmic domain of the N-terminal half between the first transmembrane segment H1 and the first multi-spanning membrane domain, and four sites are in a 275-amino acid domain of the C half between transmembrane segment H7 and the second multi-spanning membrane domain.
11320094	5	24	theme	N-terminal	921:930	arg1	half					932:935	the N-terminal half	917:935	the N-terminal half between the first transmembrane segment H1 and the first multi-spanning membrane domain	917:1023	Four sites reside in a 600-amino acid exocytoplasmic domain of the N-terminal half between the first transmembrane segment H1 and the first multi-spanning membrane domain, and four sites are in a 275-amino acid domain of the C half between transmembrane segment H7 and the second multi-spanning membrane domain.
11320094	5	25	theme	transmembrane	1094:1106	arg1	H7					1116:1117	transmembrane segment H7	1094:1117	transmembrane segment H7	1094:1117	Four sites reside in a 600-amino acid exocytoplasmic domain of the N-terminal half between the first transmembrane segment H1 and the first multi-spanning membrane domain, and four sites are in a 275-amino acid domain of the C half between transmembrane segment H7 and the second multi-spanning membrane domain.
11320094	5	26	theme	first	988:992	arg1	domain					1018:1023	the first multi-spanning membrane domain	984:1023	the first multi-spanning membrane domain	984:1023	Four sites reside in a 600-amino acid exocytoplasmic domain of the N-terminal half between the first transmembrane segment H1 and the first multi-spanning membrane domain, and four sites are in a 275-amino acid domain of the C half between transmembrane segment H7 and the second multi-spanning membrane domain.
11320094	2	27	theme	nucleotide	501:510	arg1	domain					520:525	a nucleotide binding domain	499:525	a nucleotide binding domain	499:525	It consists of a single polypeptide chain arranged in two tandem halves, each having a multi-spanning membrane domain followed by a nucleotide binding domain.
11320094	2	28	theme	single	386:391	arg1	chain					405:409	a single polypeptide chain	384:409	a single polypeptide chain arranged in two tandem halves, each having a multi-spanning membrane domain followed by a nucleotide binding domain	384:525	It consists of a single polypeptide chain arranged in two tandem halves, each having a multi-spanning membrane domain followed by a nucleotide binding domain.
11320094	5	29	theme	membrane	1009:1016	arg1	domain					1018:1023	the first multi-spanning membrane domain	984:1023	the first multi-spanning membrane domain	984:1023	Four sites reside in a 600-amino acid exocytoplasmic domain of the N-terminal half between the first transmembrane segment H1 and the first multi-spanning membrane domain, and four sites are in a 275-amino acid domain of the C half between transmembrane segment H7 and the second multi-spanning membrane domain.
11320094	4	30	theme	binding	760:766	arg1	A					758:758	concanavalin A binding	745:766	concanavalin A binding	745:766	Using trypsin digestion, site-directed mutagenesis, concanavalin A binding, and endoglycosidase digestion, we show that ABCR contains eight glycosylation sites.
11320094	4	31	gly	glycosylation	833:845	arg2	sites					847:851	eight glycosylation sites	827:851	eight glycosylation sites	827:851	Using trypsin digestion, site-directed mutagenesis, concanavalin A binding, and endoglycosidase digestion, we show that ABCR contains eight glycosylation sites.
11320094	4	31	gly	glycosylation	833:845	arg2	eight					827:831	eight	827:831	eight	827:831	Using trypsin digestion, site-directed mutagenesis, concanavalin A binding, and endoglycosidase digestion, we show that ABCR contains eight glycosylation sites.
11320094	6	32	theme	binding	1329:1335	arg1	domain					1337:1342	a nucleotide binding domain	1316:1342	a nucleotide binding domain	1316:1342	This leads to a model in which each half has a transmembrane segment followed by a large exocytoplasmic domain, a multi-spanning membrane domain, and a nucleotide binding domain.
11320094	2	33	theme	tandem	427:432	arg1	halves					434:439	two tandem halves	423:439	two tandem halves	423:439	It consists of a single polypeptide chain arranged in two tandem halves, each having a multi-spanning membrane domain followed by a nucleotide binding domain.
11320094	2	33	theme	tandem	427:432	arg1	each					442:445	each	442:445	each	442:445	It consists of a single polypeptide chain arranged in two tandem halves, each having a multi-spanning membrane domain followed by a nucleotide binding domain.
11320094	8	34	theme	N	1529:1529	arg1	halves					1537:1542	the N and C halves	1525:1542	the N and C halves of ABCR	1525:1550	Studies also suggest that the N and C halves of ABCR are linked through disulfide bonds.
11320094	1	35	theme	Stargardt	270:278	arg1	disease					288:294	Stargardt macular disease	270:294	Stargardt macular disease	270:294	ABCR is a member of the ABCA subclass of ATP binding cassette transporters that is responsible for Stargardt macular disease and implicated in retinal transport across photoreceptor disc membranes.
11320094	0	36	link	N-linked	141:148	arg1	sites					164:168	N-linked glycosylation sites	141:168	N-linked glycosylation sites	141:168	Membrane topology of the ATP binding cassette transporter ABCR and its relationship to ABC1 and related ABCA transporters: identification of N-linked glycosylation sites.
11320094	2	37	theme	multi-spanning	456:469	arg1	domain					480:485	a multi-spanning membrane domain	454:485	a multi-spanning membrane domain followed by a nucleotide binding domain	454:525	It consists of a single polypeptide chain arranged in two tandem halves, each having a multi-spanning membrane domain followed by a nucleotide binding domain.
11320094	8	38	theme	C	1535:1535	arg1	halves					1537:1542	the N and C halves	1525:1542	the N and C halves of ABCR	1525:1550	Studies also suggest that the N and C halves of ABCR are linked through disulfide bonds.
11320094	3	39	theme	glycosylation	664:676	arg1	sites					678:682	the exocytoplasmic (extracellular/lumen) N-linked glycosylation sites	614:682	the exocytoplasmic (extracellular/lumen) N-linked glycosylation sites on ABCR	614:690	To delineate between several proposed membrane topological models, we have identified the exocytoplasmic (extracellular/lumen) N-linked glycosylation sites on ABCR.
11320094	4	40	theme	glycosylation	833:845	arg1	sites					847:851	eight glycosylation sites	827:851	eight glycosylation sites	827:851	Using trypsin digestion, site-directed mutagenesis, concanavalin A binding, and endoglycosidase digestion, we show that ABCR contains eight glycosylation sites.
11320094	0	41	theme	ATP	25:27	arg1	ABCR					58:61	the ATP binding cassette transporter ABCR	21:61	the ATP binding cassette transporter ABCR	21:61	Membrane topology of the ATP binding cassette transporter ABCR and its relationship to ABC1 and related ABCA transporters: identification of N-linked glycosylation sites.
11320094	0	42	theme	cassette	37:44	arg1	ABCR					58:61	the ATP binding cassette transporter ABCR	21:61	the ATP binding cassette transporter ABCR	21:61	Membrane topology of the ATP binding cassette transporter ABCR and its relationship to ABC1 and related ABCA transporters: identification of N-linked glycosylation sites.
11320094	7	43	contain	have	1428:1431	arg1	ABC1					1380:1383	ABC1	1380:1383	ABC1 linked to Tangier disease	1380:1409	Other ABCA transporters, including ABC1 linked to Tangier disease, are proposed to have a similar membrane topology based on sequence similarity to ABCR.
11320094	7	43	contain	have	1428:1431	arg1	transporters					1356:1367	Other ABCA transporters	1345:1367	Other ABCA transporters	1345:1367	Other ABCA transporters, including ABC1 linked to Tangier disease, are proposed to have a similar membrane topology based on sequence similarity to ABCR.
11320094	7	43	contain	have	1428:1431	arg2	topology					1452:1459	a similar membrane topology	1433:1459	a similar membrane topology based on sequence similarity to ABCR	1433:1496	Other ABCA transporters, including ABC1 linked to Tangier disease, are proposed to have a similar membrane topology based on sequence similarity to ABCR.
11320094	6	44	contain	has	1207:1209	arg1	half					1202:1205	each half	1197:1205	each half	1197:1205	This leads to a model in which each half has a transmembrane segment followed by a large exocytoplasmic domain, a multi-spanning membrane domain, and a nucleotide binding domain.
11320094	6	44	contain	has	1207:1209	arg2	segment					1227:1233	a transmembrane segment	1211:1233	a transmembrane segment followed by a large exocytoplasmic domain, a multi-spanning membrane domain, and a nucleotide binding domain	1211:1342	This leads to a model in which each half has a transmembrane segment followed by a large exocytoplasmic domain, a multi-spanning membrane domain, and a nucleotide binding domain.
11320094	1	45	theme	subclass	200:207	arg1	responsible					254:264	responsible	254:264	responsible	254:264	ABCR is a member of the ABCA subclass of ATP binding cassette transporters that is responsible for Stargardt macular disease and implicated in retinal transport across photoreceptor disc membranes.
11320094	1	45	theme	subclass	200:207	arg1	ABCR					171:174	ABCR	171:174	ABCR	171:174	ABCR is a member of the ABCA subclass of ATP binding cassette transporters that is responsible for Stargardt macular disease and implicated in retinal transport across photoreceptor disc membranes.
11320094	1	45	theme	subclass	200:207	arg1	member					181:186	a member	179:186	a member of the ABCA subclass of ATP binding cassette transporters that is responsible for Stargardt macular disease and implicated in retinal transport across photoreceptor disc membranes	179:366	ABCR is a member of the ABCA subclass of ATP binding cassette transporters that is responsible for Stargardt macular disease and implicated in retinal transport across photoreceptor disc membranes.
11320094	3	46	from	sites	678:682	arg1	ABCR					687:690	ABCR	687:690	ABCR	687:690	To delineate between several proposed membrane topological models, we have identified the exocytoplasmic (extracellular/lumen) N-linked glycosylation sites on ABCR.
11320094	1	47	theme	ATP	212:214	arg1	transporters					233:244	ATP binding cassette transporters	212:244	ATP binding cassette transporters	212:244	ABCR is a member of the ABCA subclass of ATP binding cassette transporters that is responsible for Stargardt macular disease and implicated in retinal transport across photoreceptor disc membranes.
11320094	7	48	theme	sequence	1470:1477	arg1	similarity					1479:1488	sequence similarity	1470:1488	sequence similarity to ABCR	1470:1496	Other ABCA transporters, including ABC1 linked to Tangier disease, are proposed to have a similar membrane topology based on sequence similarity to ABCR.
11320094	6	49	theme	multi-spanning	1280:1293	arg1	domain					1304:1309	a multi-spanning membrane domain	1278:1309	a multi-spanning membrane domain	1278:1309	This leads to a model in which each half has a transmembrane segment followed by a large exocytoplasmic domain, a multi-spanning membrane domain, and a nucleotide binding domain.
11320094	1	50	theme	cassette	224:231	arg1	transporters					233:244	ATP binding cassette transporters	212:244	ATP binding cassette transporters	212:244	ABCR is a member of the ABCA subclass of ATP binding cassette transporters that is responsible for Stargardt macular disease and implicated in retinal transport across photoreceptor disc membranes.
11320094	3	51	link	N-linked	655:662	arg1	sites					678:682	the exocytoplasmic (extracellular/lumen) N-linked glycosylation sites	614:682	the exocytoplasmic (extracellular/lumen) N-linked glycosylation sites on ABCR	614:690	To delineate between several proposed membrane topological models, we have identified the exocytoplasmic (extracellular/lumen) N-linked glycosylation sites on ABCR.
11320094	7	52	theme	membrane	1443:1450	arg1	topology					1452:1459	a similar membrane topology	1433:1459	a similar membrane topology based on sequence similarity to ABCR	1433:1496	Other ABCA transporters, including ABC1 linked to Tangier disease, are proposed to have a similar membrane topology based on sequence similarity to ABCR.
11320094	6	53	theme	exocytoplasmic	1255:1268	arg1	domain					1270:1275	a large exocytoplasmic domain	1247:1275	a large exocytoplasmic domain	1247:1275	This leads to a model in which each half has a transmembrane segment followed by a large exocytoplasmic domain, a multi-spanning membrane domain, and a nucleotide binding domain.
11320094	2	54	contain	having	447:452	arg1	halves					434:439	two tandem halves	423:439	two tandem halves	423:439	It consists of a single polypeptide chain arranged in two tandem halves, each having a multi-spanning membrane domain followed by a nucleotide binding domain.
11320094	2	54	contain	having	447:452	arg2	domain					480:485	a multi-spanning membrane domain	454:485	a multi-spanning membrane domain followed by a nucleotide binding domain	454:525	It consists of a single polypeptide chain arranged in two tandem halves, each having a multi-spanning membrane domain followed by a nucleotide binding domain.
11320094	2	54	contain	having	447:452	arg1	each					442:445	each	442:445	each	442:445	It consists of a single polypeptide chain arranged in two tandem halves, each having a multi-spanning membrane domain followed by a nucleotide binding domain.
11320094	3	55	theme	membrane	566:573	arg1	models					587:592	several proposed membrane topological models	549:592	several proposed membrane topological models	549:592	To delineate between several proposed membrane topological models, we have identified the exocytoplasmic (extracellular/lumen) N-linked glycosylation sites on ABCR.
11320094	5	56	theme	acid	887:890	arg1	domain					907:912	a 600-amino acid exocytoplasmic domain	875:912	a 600-amino acid exocytoplasmic domain of the N-terminal half between the first transmembrane segment H1 and the first multi-spanning membrane domain	875:1023	Four sites reside in a 600-amino acid exocytoplasmic domain of the N-terminal half between the first transmembrane segment H1 and the first multi-spanning membrane domain, and four sites are in a 275-amino acid domain of the C half between transmembrane segment H7 and the second multi-spanning membrane domain.
11320094	5	56	theme	acid	887:890	arg1	half					932:935	the N-terminal half	917:935	the N-terminal half between the first transmembrane segment H1 and the first multi-spanning membrane domain	917:1023	Four sites reside in a 600-amino acid exocytoplasmic domain of the N-terminal half between the first transmembrane segment H1 and the first multi-spanning membrane domain, and four sites are in a 275-amino acid domain of the C half between transmembrane segment H7 and the second multi-spanning membrane domain.
11320094	3	57	theme	several	549:555	arg1	models					587:592	several proposed membrane topological models	549:592	several proposed membrane topological models	549:592	To delineate between several proposed membrane topological models, we have identified the exocytoplasmic (extracellular/lumen) N-linked glycosylation sites on ABCR.
11320094	7	58	theme	Tangier	1395:1401	arg1	disease					1403:1409	Tangier disease	1395:1409	Tangier disease	1395:1409	Other ABCA transporters, including ABC1 linked to Tangier disease, are proposed to have a similar membrane topology based on sequence similarity to ABCR.
11320094	6	59	theme	nucleotide	1318:1327	arg1	domain					1337:1342	a nucleotide binding domain	1316:1342	a nucleotide binding domain	1316:1342	This leads to a model in which each half has a transmembrane segment followed by a large exocytoplasmic domain, a multi-spanning membrane domain, and a nucleotide binding domain.
11320094	5	60	theme	C	1079:1079	arg1	half					1081:1084	the C half	1075:1084	the C half between transmembrane segment H7	1075:1117	Four sites reside in a 600-amino acid exocytoplasmic domain of the N-terminal half between the first transmembrane segment H1 and the first multi-spanning membrane domain, and four sites are in a 275-amino acid domain of the C half between transmembrane segment H7 and the second multi-spanning membrane domain.
11320094	0	61	theme	N-linked	141:148	arg1	sites					164:168	N-linked glycosylation sites	141:168	N-linked glycosylation sites	141:168	Membrane topology of the ATP binding cassette transporter ABCR and its relationship to ABC1 and related ABCA transporters: identification of N-linked glycosylation sites.
11320094	5	62	theme	half	932:935	arg1	domain					907:912	a 600-amino acid exocytoplasmic domain	875:912	a 600-amino acid exocytoplasmic domain of the N-terminal half between the first transmembrane segment H1 and the first multi-spanning membrane domain	875:1023	Four sites reside in a 600-amino acid exocytoplasmic domain of the N-terminal half between the first transmembrane segment H1 and the first multi-spanning membrane domain, and four sites are in a 275-amino acid domain of the C half between transmembrane segment H7 and the second multi-spanning membrane domain.
11320094	5	62	theme	half	932:935	arg1	half					932:935	the N-terminal half	917:935	the N-terminal half between the first transmembrane segment H1 and the first multi-spanning membrane domain	917:1023	Four sites reside in a 600-amino acid exocytoplasmic domain of the N-terminal half between the first transmembrane segment H1 and the first multi-spanning membrane domain, and four sites are in a 275-amino acid domain of the C half between transmembrane segment H7 and the second multi-spanning membrane domain.
11320094	5	63	theme	membrane	1149:1156	arg1	domain					1158:1163	the second multi-spanning membrane domain	1123:1163	the second multi-spanning membrane domain	1123:1163	Four sites reside in a 600-amino acid exocytoplasmic domain of the N-terminal half between the first transmembrane segment H1 and the first multi-spanning membrane domain, and four sites are in a 275-amino acid domain of the C half between transmembrane segment H7 and the second multi-spanning membrane domain.
11320094	5	63	theme	membrane	1149:1156	arg1	half					1081:1084	the C half	1075:1084	the C half between transmembrane segment H7	1075:1117	Four sites reside in a 600-amino acid exocytoplasmic domain of the N-terminal half between the first transmembrane segment H1 and the first multi-spanning membrane domain, and four sites are in a 275-amino acid domain of the C half between transmembrane segment H7 and the second multi-spanning membrane domain.
11320094	4	64	theme	site-directed	718:730	arg1	mutagenesis					732:742	site-directed mutagenesis	718:742	site-directed mutagenesis	718:742	Using trypsin digestion, site-directed mutagenesis, concanavalin A binding, and endoglycosidase digestion, we show that ABCR contains eight glycosylation sites.
11320094	0	65	theme	sites	164:168	arg1	identification					123:136	identification	123:136	Membrane topology of the ATP binding cassette transporter ABCR and its relationship to ABC1 and related ABCA transporters: identification of N-linked glycosylation sites.	0:169	Membrane topology of the ATP binding cassette transporter ABCR and its relationship to ABC1 and related ABCA transporters: identification of N-linked glycosylation sites.
11320094	5	66	theme	acid	1060:1063	arg1	domain					1065:1070	a 275-amino acid domain	1048:1070	a 275-amino acid domain of the C half between transmembrane segment H7	1048:1117	Four sites reside in a 600-amino acid exocytoplasmic domain of the N-terminal half between the first transmembrane segment H1 and the first multi-spanning membrane domain, and four sites are in a 275-amino acid domain of the C half between transmembrane segment H7 and the second multi-spanning membrane domain.
11320094	5	66	theme	acid	1060:1063	arg1	half					1081:1084	the C half	1075:1084	the C half between transmembrane segment H7	1075:1117	Four sites reside in a 600-amino acid exocytoplasmic domain of the N-terminal half between the first transmembrane segment H1 and the first multi-spanning membrane domain, and four sites are in a 275-amino acid domain of the C half between transmembrane segment H7 and the second multi-spanning membrane domain.
11320094	3	67	theme	exocytoplasmic	618:631	arg1	sites					678:682	the exocytoplasmic (extracellular/lumen) N-linked glycosylation sites	614:682	the exocytoplasmic (extracellular/lumen) N-linked glycosylation sites on ABCR	614:690	To delineate between several proposed membrane topological models, we have identified the exocytoplasmic (extracellular/lumen) N-linked glycosylation sites on ABCR.
11320094	4	68	contain	contains	818:825	arg1	ABCR					813:816	ABCR	813:816	ABCR	813:816	Using trypsin digestion, site-directed mutagenesis, concanavalin A binding, and endoglycosidase digestion, we show that ABCR contains eight glycosylation sites.
11320094	4	68	contain	contains	818:825	arg2	sites					847:851	eight glycosylation sites	827:851	eight glycosylation sites	827:851	Using trypsin digestion, site-directed mutagenesis, concanavalin A binding, and endoglycosidase digestion, we show that ABCR contains eight glycosylation sites.
11320094	7	69	theme	Other	1345:1349	arg1	transporters					1356:1367	Other ABCA transporters	1345:1367	Other ABCA transporters	1345:1367	Other ABCA transporters, including ABC1 linked to Tangier disease, are proposed to have a similar membrane topology based on sequence similarity to ABCR.
11320094	7	69	theme	Other	1345:1349	arg1	ABC1					1380:1383	ABC1	1380:1383	ABC1 linked to Tangier disease	1380:1409	Other ABCA transporters, including ABC1 linked to Tangier disease, are proposed to have a similar membrane topology based on sequence similarity to ABCR.
11320094	0	70	theme	relationship	71:82	arg1	topology					9:16	Membrane topology	0:16	Membrane topology of the ATP binding cassette transporter ABCR and its relationship to ABC1 and related ABCA transporters: identification of N-linked glycosylation sites.	0:169	Membrane topology of the ATP binding cassette transporter ABCR and its relationship to ABC1 and related ABCA transporters: identification of N-linked glycosylation sites.
11320094	5	71	theme	second	1127:1132	arg1	domain					1158:1163	the second multi-spanning membrane domain	1123:1163	the second multi-spanning membrane domain	1123:1163	Four sites reside in a 600-amino acid exocytoplasmic domain of the N-terminal half between the first transmembrane segment H1 and the first multi-spanning membrane domain, and four sites are in a 275-amino acid domain of the C half between transmembrane segment H7 and the second multi-spanning membrane domain.
11320094	5	71	theme	second	1127:1132	arg1	half					1081:1084	the C half	1075:1084	the C half between transmembrane segment H7	1075:1117	Four sites reside in a 600-amino acid exocytoplasmic domain of the N-terminal half between the first transmembrane segment H1 and the first multi-spanning membrane domain, and four sites are in a 275-amino acid domain of the C half between transmembrane segment H7 and the second multi-spanning membrane domain.
11320094	0	72	gly	glycosylation	150:162	arg2	sites					164:168	N-linked glycosylation sites	141:168	N-linked glycosylation sites	141:168	Membrane topology of the ATP binding cassette transporter ABCR and its relationship to ABC1 and related ABCA transporters: identification of N-linked glycosylation sites.
11320094	1	73	theme	disc	353:356	arg1	membranes					358:366	photoreceptor disc membranes	339:366	photoreceptor disc membranes	339:366	ABCR is a member of the ABCA subclass of ATP binding cassette transporters that is responsible for Stargardt macular disease and implicated in retinal transport across photoreceptor disc membranes.
11320094	2	74	theme	membrane	471:478	arg1	domain					480:485	a multi-spanning membrane domain	454:485	a multi-spanning membrane domain followed by a nucleotide binding domain	454:525	It consists of a single polypeptide chain arranged in two tandem halves, each having a multi-spanning membrane domain followed by a nucleotide binding domain.
11320094	5	75	dep	segment	969:975	arg1	H1					977:978	H1	977:978	H1	977:978	Four sites reside in a 600-amino acid exocytoplasmic domain of the N-terminal half between the first transmembrane segment H1 and the first multi-spanning membrane domain, and four sites are in a 275-amino acid domain of the C half between transmembrane segment H7 and the second multi-spanning membrane domain.
11320094	1	76	theme	photoreceptor	339:351	arg1	membranes					358:366	photoreceptor disc membranes	339:366	photoreceptor disc membranes	339:366	ABCR is a member of the ABCA subclass of ATP binding cassette transporters that is responsible for Stargardt macular disease and implicated in retinal transport across photoreceptor disc membranes.
11320094	2	77	theme	binding	512:518	arg1	domain					520:525	a nucleotide binding domain	499:525	a nucleotide binding domain	499:525	It consists of a single polypeptide chain arranged in two tandem halves, each having a multi-spanning membrane domain followed by a nucleotide binding domain.
11320094	4	78	theme	endoglycosidase	773:787	arg1	digestion					789:797	endoglycosidase digestion	773:797	endoglycosidase digestion	773:797	Using trypsin digestion, site-directed mutagenesis, concanavalin A binding, and endoglycosidase digestion, we show that ABCR contains eight glycosylation sites.
11320094	0	79	theme	related	96:102	arg1	transporters					109:120	related ABCA transporters	96:120	related ABCA transporters	96:120	Membrane topology of the ATP binding cassette transporter ABCR and its relationship to ABC1 and related ABCA transporters: identification of N-linked glycosylation sites.
11320094	5	80	theme	segment	1108:1114	arg1	H7					1116:1117	transmembrane segment H7	1094:1117	transmembrane segment H7	1094:1117	Four sites reside in a 600-amino acid exocytoplasmic domain of the N-terminal half between the first transmembrane segment H1 and the first multi-spanning membrane domain, and four sites are in a 275-amino acid domain of the C half between transmembrane segment H7 and the second multi-spanning membrane domain.
11320094	5	81	theme	multi-spanning	994:1007	arg1	domain					1018:1023	the first multi-spanning membrane domain	984:1023	the first multi-spanning membrane domain	984:1023	Four sites reside in a 600-amino acid exocytoplasmic domain of the N-terminal half between the first transmembrane segment H1 and the first multi-spanning membrane domain, and four sites are in a 275-amino acid domain of the C half between transmembrane segment H7 and the second multi-spanning membrane domain.
11320094	5	82	theme	transmembrane	955:967	arg1	segment					969:975	the first transmembrane segment H1 and the first multi-spanning membrane domain	945:1023	segment	969:975	Four sites reside in a 600-amino acid exocytoplasmic domain of the N-terminal half between the first transmembrane segment H1 and the first multi-spanning membrane domain, and four sites are in a 275-amino acid domain of the C half between transmembrane segment H7 and the second multi-spanning membrane domain.
11320094	3	83	theme	N-linked	655:662	arg1	sites					678:682	the exocytoplasmic (extracellular/lumen) N-linked glycosylation sites	614:682	the exocytoplasmic (extracellular/lumen) N-linked glycosylation sites on ABCR	614:690	To delineate between several proposed membrane topological models, we have identified the exocytoplasmic (extracellular/lumen) N-linked glycosylation sites on ABCR.
11320094	0	84	theme	binding	29:35	arg1	ABCR					58:61	the ATP binding cassette transporter ABCR	21:61	the ATP binding cassette transporter ABCR	21:61	Membrane topology of the ATP binding cassette transporter ABCR and its relationship to ABC1 and related ABCA transporters: identification of N-linked glycosylation sites.
11320094	1	85	theme	macular	280:286	arg1	disease					288:294	Stargardt macular disease	270:294	Stargardt macular disease	270:294	ABCR is a member of the ABCA subclass of ATP binding cassette transporters that is responsible for Stargardt macular disease and implicated in retinal transport across photoreceptor disc membranes.
11320094	8	86	theme	ABCR	1547:1550	arg1	halves					1537:1542	the N and C halves	1525:1542	the N and C halves of ABCR	1525:1550	Studies also suggest that the N and C halves of ABCR are linked through disulfide bonds.
11320094	3	87	theme	extracellular/lumen	634:652	arg1	sites					678:682	the exocytoplasmic (extracellular/lumen) N-linked glycosylation sites	614:682	the exocytoplasmic (extracellular/lumen) N-linked glycosylation sites on ABCR	614:690	To delineate between several proposed membrane topological models, we have identified the exocytoplasmic (extracellular/lumen) N-linked glycosylation sites on ABCR.
11320094	2	88	theme	polypeptide	393:403	arg1	chain					405:409	a single polypeptide chain	384:409	a single polypeptide chain arranged in two tandem halves, each having a multi-spanning membrane domain followed by a nucleotide binding domain	384:525	It consists of a single polypeptide chain arranged in two tandem halves, each having a multi-spanning membrane domain followed by a nucleotide binding domain.
11320094	0	89	theme	transporter	46:56	arg1	ABCR					58:61	the ATP binding cassette transporter ABCR	21:61	the ATP binding cassette transporter ABCR	21:61	Membrane topology of the ATP binding cassette transporter ABCR and its relationship to ABC1 and related ABCA transporters: identification of N-linked glycosylation sites.
11320094	8	90	theme	disulfide	1571:1579	arg1	bonds					1581:1585	disulfide bonds	1571:1585	disulfide bonds	1571:1585	Studies also suggest that the N and C halves of ABCR are linked through disulfide bonds.
11320094	0	91	dep	topology	9:16	arg1	identification					123:136	identification	123:136	Membrane topology of the ATP binding cassette transporter ABCR and its relationship to ABC1 and related ABCA transporters: identification of N-linked glycosylation sites.	0:169	Membrane topology of the ATP binding cassette transporter ABCR and its relationship to ABC1 and related ABCA transporters: identification of N-linked glycosylation sites.
11320094	1	92	theme	binding	216:222	arg1	transporters					233:244	ATP binding cassette transporters	212:244	ATP binding cassette transporters	212:244	ABCR is a member of the ABCA subclass of ATP binding cassette transporters that is responsible for Stargardt macular disease and implicated in retinal transport across photoreceptor disc membranes.
24744147	3	0	theme	high-carbohydrate	354:370	arg1	diets					372:376	high-carbohydrate diets	354:376	high-carbohydrate diets	354:376	Human colon tumors and colons from mice fed high-carbohydrate diets exhibited higher amounts of β-catenin and O-GlcNAc relative to healthy tissues and mice fed a standard diet, respectively.
24744147	4	1	theme	G	553:553	arg1	Administration					501:514	Administration	501:514	Administration of the O-GlcNAcase inhibitor thiamet G to mice	501:561	Administration of the O-GlcNAcase inhibitor thiamet G to mice also increased colonic expression of β-catenin.
24744147	8	2	theme	crucial	1079:1085	arg1	residue					1087:1093	the most crucial residue	1070:1093	the most crucial residue that controls the β-catenin degradation rate	1070:1138	Analyses of β-catenin O-GlcNAcylation mutants reinforced T41 as the most crucial residue that controls the β-catenin degradation rate.
24744147	8	2	theme	crucial	1079:1085	arg1	T41					1063:1065	T41	1063:1065	T41	1063:1065	Analyses of β-catenin O-GlcNAcylation mutants reinforced T41 as the most crucial residue that controls the β-catenin degradation rate.
24744147	10	3	theme	adherens	1452:1459	arg1	junctions					1461:1469	adherens junctions	1452:1469	adherens junctions	1452:1469	These results suggest that O-GlcNAcylation regulates not only the stability of β-catenin, but also affects its localization at the level of adherens junctions.
24744147	7	4	from	O-GlcNAcylation	856:870	arg1	lines					892:896	human colon cell lines	875:896	human colon cell lines	875:896	Interestingly, elevating O-GlcNAcylation in human colon cell lines drastically reduced phosphorylation at T41, a key residue of the D box responsible for β-catenin stability.
24744147	5	5	theme	O-GlcNAcylation	641:655	arg1	sites					657:661	4 O-GlcNAcylation sites	639:661	4 O-GlcNAcylation sites	639:661	By ETD-MS/MS, we identified 4 O-GlcNAcylation sites at the N terminus of β-catenin (S23/T40/T41/T112).
24744147	3	6	theme	β-catenin	406:414	arg1	β-catenin					406:414	β-catenin	406:414	β-catenin	406:414	Human colon tumors and colons from mice fed high-carbohydrate diets exhibited higher amounts of β-catenin and O-GlcNAc relative to healthy tissues and mice fed a standard diet, respectively.
24744147	3	6	theme	β-catenin	406:414	arg1	O-GlcNAc					420:427	O-GlcNAc	420:427	O-GlcNAc	420:427	Human colon tumors and colons from mice fed high-carbohydrate diets exhibited higher amounts of β-catenin and O-GlcNAc relative to healthy tissues and mice fed a standard diet, respectively.
24744147	3	6	theme	β-catenin	406:414	arg1	mice					461:464	mice	461:464	mice fed a standard diet	461:484	Human colon tumors and colons from mice fed high-carbohydrate diets exhibited higher amounts of β-catenin and O-GlcNAc relative to healthy tissues and mice fed a standard diet, respectively.
24744147	3	6	theme	β-catenin	406:414	arg1	amounts					395:401	higher amounts	388:401	higher amounts of β-catenin and O-GlcNAc relative to healthy tissues	388:455	Human colon tumors and colons from mice fed high-carbohydrate diets exhibited higher amounts of β-catenin and O-GlcNAc relative to healthy tissues and mice fed a standard diet, respectively.
24744147	8	7	theme	mutants	1044:1050	arg1	Analyses					1006:1013	Analyses	1006:1013	Analyses of β-catenin O-GlcNAcylation mutants	1006:1050	Analyses of β-catenin O-GlcNAcylation mutants reinforced T41 as the most crucial residue that controls the β-catenin degradation rate.
24744147	8	8	theme	β-catenin	1113:1121	arg1	rate					1135:1138	the β-catenin degradation rate	1109:1138	the β-catenin degradation rate	1109:1138	Analyses of β-catenin O-GlcNAcylation mutants reinforced T41 as the most crucial residue that controls the β-catenin degradation rate.
24744147	4	9	theme	O-GlcNAcase	523:533	arg1	G					553:553	the O-GlcNAcase inhibitor thiamet G	519:553	the O-GlcNAcase inhibitor thiamet G	519:553	Administration of the O-GlcNAcase inhibitor thiamet G to mice also increased colonic expression of β-catenin.
24744147	7	10	theme	β-catenin	985:993	arg1	stability					995:1003	β-catenin stability	985:1003	β-catenin stability	985:1003	Interestingly, elevating O-GlcNAcylation in human colon cell lines drastically reduced phosphorylation at T41, a key residue of the D box responsible for β-catenin stability.
24744147	7	11	from	T41	937:939	arg1	phosphorylation					918:932	phosphorylation	918:932	phosphorylation at T41, a key residue of the D box responsible for β-catenin stability	918:1003	Interestingly, elevating O-GlcNAcylation in human colon cell lines drastically reduced phosphorylation at T41, a key residue of the D box responsible for β-catenin stability.
24744147	8	12	theme	β-catenin	1018:1026	arg1	mutants					1044:1050	β-catenin O-GlcNAcylation mutants	1018:1050	β-catenin O-GlcNAcylation mutants	1018:1050	Analyses of β-catenin O-GlcNAcylation mutants reinforced T41 as the most crucial residue that controls the β-catenin degradation rate.
24744147	11	13	theme	missing	1535:1541	arg1	link					1543:1546	a missing link	1533:1546	a missing link between the glucose metabolism deregulation observed in metabolic disorders and the development of cancer	1533:1652	Accordingly, we propose that O-GlcNAcylation of β-catenin is a missing link between the glucose metabolism deregulation observed in metabolic disorders and the development of cancer.
24744147	11	13	theme	missing	1535:1541	arg1	O-GlcNAcylation					1501:1515	O-GlcNAcylation	1501:1515	O-GlcNAcylation of β-catenin	1501:1528	Accordingly, we propose that O-GlcNAcylation of β-catenin is a missing link between the glucose metabolism deregulation observed in metabolic disorders and the development of cancer.
24744147	5	14	theme	N	670:670	arg1	terminus					672:679	the N terminus	666:679	the N terminus of β-catenin (S23/T40/T41/T112)	666:711	By ETD-MS/MS, we identified 4 O-GlcNAcylation sites at the N terminus of β-catenin (S23/T40/T41/T112).
24744147	8	15	theme	O-GlcNAcylation	1028:1042	arg1	mutants					1044:1050	β-catenin O-GlcNAcylation mutants	1018:1050	β-catenin O-GlcNAcylation mutants	1018:1050	Analyses of β-catenin O-GlcNAcylation mutants reinforced T41 as the most crucial residue that controls the β-catenin degradation rate.
24744147	6	16	theme	threonine	750:758	arg1	mutation					727:734	mutation	727:734	mutation of serine and threonine residues within the D box of β-catenin	727:797	Furthermore, mutation of serine and threonine residues within the D box of β-catenin reduced O-GlcNAcylation by 75%.
24744147	9	17	theme	O-GlcNAcase	1263:1273	arg1	silencing					1275:1283	O-GlcNAcase silencing	1263:1283	O-GlcNAcase silencing	1263:1283	Finally, inhibiting O-GlcNAcylation decreased the β-catenin/α-catenin interaction necessary for mucosa integrity, whereas O-GlcNAcase silencing improved this interaction.
24744147	4	18	theme	thiamet	545:551	arg1	G					553:553	the O-GlcNAcase inhibitor thiamet G	519:553	the O-GlcNAcase inhibitor thiamet G	519:553	Administration of the O-GlcNAcase inhibitor thiamet G to mice also increased colonic expression of β-catenin.
24744147	7	19	theme	responsible	969:979	arg1	box					965:967	the D box	959:967	the D box responsible for β-catenin stability	959:1003	Interestingly, elevating O-GlcNAcylation in human colon cell lines drastically reduced phosphorylation at T41, a key residue of the D box responsible for β-catenin stability.
24744147	11	20	dep	metabolism	1568:1577	arg1	deregulation					1579:1590	deregulation	1579:1590	the glucose metabolism deregulation observed in metabolic disorders and the development of cancer	1556:1652	Accordingly, we propose that O-GlcNAcylation of β-catenin is a missing link between the glucose metabolism deregulation observed in metabolic disorders and the development of cancer.
24744147	10	21	theme	β-catenin	1391:1399	arg1	stability					1378:1386	the stability	1374:1386	the stability of β-catenin	1374:1399	These results suggest that O-GlcNAcylation regulates not only the stability of β-catenin, but also affects its localization at the level of adherens junctions.
24744147	4	22	theme	inhibitor	535:543	arg1	G					553:553	the O-GlcNAcase inhibitor thiamet G	519:553	the O-GlcNAcase inhibitor thiamet G	519:553	Administration of the O-GlcNAcase inhibitor thiamet G to mice also increased colonic expression of β-catenin.
24744147	8	23	theme	degradation	1123:1133	arg1	rate					1135:1138	the β-catenin degradation rate	1109:1138	the β-catenin degradation rate	1109:1138	Analyses of β-catenin O-GlcNAcylation mutants reinforced T41 as the most crucial residue that controls the β-catenin degradation rate.
24744147	6	24	dep	serine	739:744	arg1	residues					760:767	residues	760:767	residues	760:767	Furthermore, mutation of serine and threonine residues within the D box of β-catenin reduced O-GlcNAcylation by 75%.
24744147	6	25	theme	serine	739:744	arg1	mutation					727:734	mutation	727:734	mutation of serine and threonine residues within the D box of β-catenin	727:797	Furthermore, mutation of serine and threonine residues within the D box of β-catenin reduced O-GlcNAcylation by 75%.
24744147	1	26	theme	colorectal	204:213	arg1	cancer					215:220	colorectal cancer	204:220	colorectal cancer	204:220	Dysfunctions in Wnt signaling increase β-catenin stability and are associated with cancers, including colorectal cancer.
24744147	3	27	theme	healthy	441:447	arg1	tissues					449:455	healthy tissues	441:455	healthy tissues	441:455	Human colon tumors and colons from mice fed high-carbohydrate diets exhibited higher amounts of β-catenin and O-GlcNAc relative to healthy tissues and mice fed a standard diet, respectively.
24744147	5	28	theme	β-catenin	684:692	arg1	terminus					672:679	the N terminus	666:679	the N terminus of β-catenin (S23/T40/T41/T112)	666:711	By ETD-MS/MS, we identified 4 O-GlcNAcylation sites at the N terminus of β-catenin (S23/T40/T41/T112).
24744147	7	29	theme	D	963:963	arg1	box					965:967	the D box	959:967	the D box responsible for β-catenin stability	959:1003	Interestingly, elevating O-GlcNAcylation in human colon cell lines drastically reduced phosphorylation at T41, a key residue of the D box responsible for β-catenin stability.
24744147	7	30	theme	key	944:946	arg1	residue					948:954	a key residue	942:954	a key residue of the D box responsible for β-catenin stability	942:1003	Interestingly, elevating O-GlcNAcylation in human colon cell lines drastically reduced phosphorylation at T41, a key residue of the D box responsible for β-catenin stability.
24744147	7	30	theme	key	944:946	arg1	T41					937:939	T41	937:939	T41	937:939	Interestingly, elevating O-GlcNAcylation in human colon cell lines drastically reduced phosphorylation at T41, a key residue of the D box responsible for β-catenin stability.
24744147	7	30	theme	key	944:946	arg1	box					965:967	the D box	959:967	the D box responsible for β-catenin stability	959:1003	Interestingly, elevating O-GlcNAcylation in human colon cell lines drastically reduced phosphorylation at T41, a key residue of the D box responsible for β-catenin stability.
24744147	7	31	theme	colon	881:885	arg1	lines					892:896	human colon cell lines	875:896	human colon cell lines	875:896	Interestingly, elevating O-GlcNAcylation in human colon cell lines drastically reduced phosphorylation at T41, a key residue of the D box responsible for β-catenin stability.
24744147	3	32	theme	standard	472:479	arg1	diet					481:484	a standard diet	470:484	a standard diet	470:484	Human colon tumors and colons from mice fed high-carbohydrate diets exhibited higher amounts of β-catenin and O-GlcNAc relative to healthy tissues and mice fed a standard diet, respectively.
24744147	3	33	theme	O-GlcNAc	420:427	arg1	β-catenin					406:414	β-catenin	406:414	β-catenin	406:414	Human colon tumors and colons from mice fed high-carbohydrate diets exhibited higher amounts of β-catenin and O-GlcNAc relative to healthy tissues and mice fed a standard diet, respectively.
24744147	3	33	theme	O-GlcNAc	420:427	arg1	O-GlcNAc					420:427	O-GlcNAc	420:427	O-GlcNAc	420:427	Human colon tumors and colons from mice fed high-carbohydrate diets exhibited higher amounts of β-catenin and O-GlcNAc relative to healthy tissues and mice fed a standard diet, respectively.
24744147	3	33	theme	O-GlcNAc	420:427	arg1	mice					461:464	mice	461:464	mice fed a standard diet	461:484	Human colon tumors and colons from mice fed high-carbohydrate diets exhibited higher amounts of β-catenin and O-GlcNAc relative to healthy tissues and mice fed a standard diet, respectively.
24744147	3	33	theme	O-GlcNAc	420:427	arg1	amounts					395:401	higher amounts	388:401	higher amounts of β-catenin and O-GlcNAc relative to healthy tissues	388:455	Human colon tumors and colons from mice fed high-carbohydrate diets exhibited higher amounts of β-catenin and O-GlcNAc relative to healthy tissues and mice fed a standard diet, respectively.
24744147	4	34	theme	β-catenin	600:608	arg1	expression					586:595	colonic expression	578:595	colonic expression of β-catenin	578:608	Administration of the O-GlcNAcase inhibitor thiamet G to mice also increased colonic expression of β-catenin.
24744147	7	35	theme	box	965:967	arg1	residue					948:954	a key residue	942:954	a key residue of the D box responsible for β-catenin stability	942:1003	Interestingly, elevating O-GlcNAcylation in human colon cell lines drastically reduced phosphorylation at T41, a key residue of the D box responsible for β-catenin stability.
24744147	7	35	theme	box	965:967	arg1	T41					937:939	T41	937:939	T41	937:939	Interestingly, elevating O-GlcNAcylation in human colon cell lines drastically reduced phosphorylation at T41, a key residue of the D box responsible for β-catenin stability.
24744147	7	35	theme	box	965:967	arg1	box					965:967	the D box	959:967	the D box responsible for β-catenin stability	959:1003	Interestingly, elevating O-GlcNAcylation in human colon cell lines drastically reduced phosphorylation at T41, a key residue of the D box responsible for β-catenin stability.
24744147	1	36	theme	Wnt	118:120	arg1	signaling					122:130	Wnt signaling	118:130	Wnt signaling	118:130	Dysfunctions in Wnt signaling increase β-catenin stability and are associated with cancers, including colorectal cancer.
24744147	7	37	theme	cell	887:890	arg1	lines					892:896	human colon cell lines	875:896	human colon cell lines	875:896	Interestingly, elevating O-GlcNAcylation in human colon cell lines drastically reduced phosphorylation at T41, a key residue of the D box responsible for β-catenin stability.
24744147	3	38	theme	relative	429:436	arg1	β-catenin					406:414	β-catenin	406:414	β-catenin	406:414	Human colon tumors and colons from mice fed high-carbohydrate diets exhibited higher amounts of β-catenin and O-GlcNAc relative to healthy tissues and mice fed a standard diet, respectively.
24744147	9	39	theme	necessary	1223:1231	arg1	interaction					1211:1221	the β-catenin/α-catenin interaction	1187:1221	the β-catenin/α-catenin interaction necessary for mucosa integrity	1187:1252	Finally, inhibiting O-GlcNAcylation decreased the β-catenin/α-catenin interaction necessary for mucosa integrity, whereas O-GlcNAcase silencing improved this interaction.
24744147	11	40	theme	glucose	1560:1566	arg1	metabolism					1568:1577	the glucose metabolism deregulation	1556:1590	the glucose metabolism deregulation observed in metabolic disorders and the development of cancer	1556:1652	Accordingly, we propose that O-GlcNAcylation of β-catenin is a missing link between the glucose metabolism deregulation observed in metabolic disorders and the development of cancer.
24744147	9	41	theme	inhibiting	1150:1159	arg1	O-GlcNAcylation					1161:1175	inhibiting O-GlcNAcylation	1150:1175	inhibiting O-GlcNAcylation	1150:1175	Finally, inhibiting O-GlcNAcylation decreased the β-catenin/α-catenin interaction necessary for mucosa integrity, whereas O-GlcNAcase silencing improved this interaction.
24744147	3	42	theme	Human	310:314	arg1	tumors					322:327	Human colon tumors	310:327	Human colon tumors	310:327	Human colon tumors and colons from mice fed high-carbohydrate diets exhibited higher amounts of β-catenin and O-GlcNAc relative to healthy tissues and mice fed a standard diet, respectively.
24744147	7	43	theme	human	875:879	arg1	lines					892:896	human colon cell lines	875:896	human colon cell lines	875:896	Interestingly, elevating O-GlcNAcylation in human colon cell lines drastically reduced phosphorylation at T41, a key residue of the D box responsible for β-catenin stability.
24744147	0	44	theme	direct	45:50	arg1	competition					52:62	direct competition	45:62	direct competition with phosphorylation at threonine 41	45:99	O-GlcNAcylation stabilizes β-catenin through direct competition with phosphorylation at threonine 41.
24744147	4	45	theme	colonic	578:584	arg1	expression					586:595	colonic expression	578:595	colonic expression of β-catenin	578:608	Administration of the O-GlcNAcase inhibitor thiamet G to mice also increased colonic expression of β-catenin.
24744147	3	46	theme	colon	316:320	arg1	tumors					322:327	Human colon tumors	310:327	Human colon tumors	310:327	Human colon tumors and colons from mice fed high-carbohydrate diets exhibited higher amounts of β-catenin and O-GlcNAc relative to healthy tissues and mice fed a standard diet, respectively.
24744147	0	47	from	threonine	88:96	arg1	phosphorylation					69:83	phosphorylation	69:83	phosphorylation at threonine 41	69:99	O-GlcNAcylation stabilizes β-catenin through direct competition with phosphorylation at threonine 41.
24744147	9	48	theme	β-catenin/α-catenin	1191:1209	arg1	interaction					1211:1221	the β-catenin/α-catenin interaction	1187:1221	the β-catenin/α-catenin interaction necessary for mucosa integrity	1187:1252	Finally, inhibiting O-GlcNAcylation decreased the β-catenin/α-catenin interaction necessary for mucosa integrity, whereas O-GlcNAcase silencing improved this interaction.
24744147	11	49	theme	β-catenin	1520:1528	arg1	link					1543:1546	a missing link	1533:1546	a missing link between the glucose metabolism deregulation observed in metabolic disorders and the development of cancer	1533:1652	Accordingly, we propose that O-GlcNAcylation of β-catenin is a missing link between the glucose metabolism deregulation observed in metabolic disorders and the development of cancer.
24744147	11	49	theme	β-catenin	1520:1528	arg1	O-GlcNAcylation					1501:1515	O-GlcNAcylation	1501:1515	O-GlcNAcylation of β-catenin	1501:1528	Accordingly, we propose that O-GlcNAcylation of β-catenin is a missing link between the glucose metabolism deregulation observed in metabolic disorders and the development of cancer.
24744147	11	50	located	observed	1592:1599	arg1	disorders					1614:1622	metabolic disorders	1604:1622	metabolic disorders	1604:1622	Accordingly, we propose that O-GlcNAcylation of β-catenin is a missing link between the glucose metabolism deregulation observed in metabolic disorders and the development of cancer.
24744147	11	50	located	observed	1592:1599	arg1	development					1632:1642	the development	1628:1642	the development of cancer	1628:1652	Accordingly, we propose that O-GlcNAcylation of β-catenin is a missing link between the glucose metabolism deregulation observed in metabolic disorders and the development of cancer.
24744147	11	50	located	observed	1592:1599	arg2	metabolism					1568:1577	the glucose metabolism deregulation	1556:1590	the glucose metabolism deregulation observed in metabolic disorders and the development of cancer	1556:1652	Accordingly, we propose that O-GlcNAcylation of β-catenin is a missing link between the glucose metabolism deregulation observed in metabolic disorders and the development of cancer.
24744147	2	51	theme	β-catenin	236:244	arg1	degradation					246:256	β-catenin degradation	236:256	β-catenin degradation	236:256	In addition, β-catenin degradation is decreased by nutrient-dependent O-GlcNAcylation.
24744147	6	52	theme	β-catenin	789:797	arg1	box					782:784	the D box	776:784	the D box of β-catenin	776:797	Furthermore, mutation of serine and threonine residues within the D box of β-catenin reduced O-GlcNAcylation by 75%.
24744147	1	53	theme	β-catenin	141:149	arg1	stability					151:159	β-catenin stability	141:159	β-catenin stability	141:159	Dysfunctions in Wnt signaling increase β-catenin stability and are associated with cancers, including colorectal cancer.
24744147	11	54	theme	metabolic	1604:1612	arg1	disorders					1614:1622	metabolic disorders	1604:1622	metabolic disorders	1604:1622	Accordingly, we propose that O-GlcNAcylation of β-catenin is a missing link between the glucose metabolism deregulation observed in metabolic disorders and the development of cancer.
24744147	11	55	theme	cancer	1647:1652	arg1	disorders					1614:1622	metabolic disorders	1604:1622	metabolic disorders	1604:1622	Accordingly, we propose that O-GlcNAcylation of β-catenin is a missing link between the glucose metabolism deregulation observed in metabolic disorders and the development of cancer.
24744147	11	55	theme	cancer	1647:1652	arg1	development					1632:1642	the development	1628:1642	the development of cancer	1628:1652	Accordingly, we propose that O-GlcNAcylation of β-catenin is a missing link between the glucose metabolism deregulation observed in metabolic disorders and the development of cancer.
24744147	10	56	theme	junctions	1461:1469	arg1	level					1443:1447	the level	1439:1447	the level of adherens junctions	1439:1469	These results suggest that O-GlcNAcylation regulates not only the stability of β-catenin, but also affects its localization at the level of adherens junctions.
24744147	9	57	theme	mucosa	1237:1242	arg1	integrity					1244:1252	mucosa integrity	1237:1252	mucosa integrity	1237:1252	Finally, inhibiting O-GlcNAcylation decreased the β-catenin/α-catenin interaction necessary for mucosa integrity, whereas O-GlcNAcase silencing improved this interaction.
24744147	1	58	from	Dysfunctions	102:113	arg1	signaling					122:130	Wnt signaling	118:130	Wnt signaling	118:130	Dysfunctions in Wnt signaling increase β-catenin stability and are associated with cancers, including colorectal cancer.
24744147	10	59	dep	regulates	1355:1363	arg1	only					1369:1372	only	1369:1372	only	1369:1372	These results suggest that O-GlcNAcylation regulates not only the stability of β-catenin, but also affects its localization at the level of adherens junctions.
24744147	2	60	theme	nutrient-dependent	274:291	arg1	O-GlcNAcylation					293:307	nutrient-dependent O-GlcNAcylation	274:307	nutrient-dependent O-GlcNAcylation	274:307	In addition, β-catenin degradation is decreased by nutrient-dependent O-GlcNAcylation.
24744147	6	61	theme	D	780:780	arg1	box					782:784	the D box	776:784	the D box of β-catenin	776:797	Furthermore, mutation of serine and threonine residues within the D box of β-catenin reduced O-GlcNAcylation by 75%.
24744147	3	62	from	mice	345:348	arg1	tumors					322:327	Human colon tumors	310:327	Human colon tumors	310:327	Human colon tumors and colons from mice fed high-carbohydrate diets exhibited higher amounts of β-catenin and O-GlcNAc relative to healthy tissues and mice fed a standard diet, respectively.
24744147	3	62	from	mice	345:348	arg1	colons					333:338	colons	333:338	colons	333:338	Human colon tumors and colons from mice fed high-carbohydrate diets exhibited higher amounts of β-catenin and O-GlcNAc relative to healthy tissues and mice fed a standard diet, respectively.
24744147	3	63	theme	higher	388:393	arg1	O-GlcNAc					420:427	O-GlcNAc	420:427	O-GlcNAc	420:427	Human colon tumors and colons from mice fed high-carbohydrate diets exhibited higher amounts of β-catenin and O-GlcNAc relative to healthy tissues and mice fed a standard diet, respectively.
24744147	3	63	theme	higher	388:393	arg1	β-catenin					406:414	β-catenin	406:414	β-catenin	406:414	Human colon tumors and colons from mice fed high-carbohydrate diets exhibited higher amounts of β-catenin and O-GlcNAc relative to healthy tissues and mice fed a standard diet, respectively.
24744147	3	63	theme	higher	388:393	arg1	amounts					395:401	higher amounts	388:401	higher amounts of β-catenin and O-GlcNAc relative to healthy tissues	388:455	Human colon tumors and colons from mice fed high-carbohydrate diets exhibited higher amounts of β-catenin and O-GlcNAc relative to healthy tissues and mice fed a standard diet, respectively.
24744147	0	64	with	competition	52:62	arg1	phosphorylation					69:83	phosphorylation	69:83	phosphorylation at threonine 41	69:99	O-GlcNAcylation stabilizes β-catenin through direct competition with phosphorylation at threonine 41.
24744147	10	65	from	level	1443:1447	arg1	localization					1423:1434	its localization	1419:1434	its localization at the level of adherens junctions	1419:1469	These results suggest that O-GlcNAcylation regulates not only the stability of β-catenin, but also affects its localization at the level of adherens junctions.
14670950	8	0	gly	glycosylation	1702:1714	arg1	MT1-MMP					1719:1725	MT1-MMP	1719:1725	MT1-MMP	1719:1725	These data provide evidence for an additional mechanism for post-translational control of MT1-MMP activity and suggest that glycosylation of MT1-MMP may regulate its substrate targeting.
14670950	6	1	theme	mature	1298:1303	arg1	enzyme					1305:1310	the mature enzyme	1294:1310	the mature enzyme	1294:1310	The inability of carbohydrate-free MT1-MMP to activate proMMP-2 was not a result of defective MT1-MMP zymogen activation, aberrant protein stability, or inability of the mature enzyme to oligomerize.
14670950	1	2	theme	cancer	253:258	arg1	metastasis					260:269	cancer metastasis	253:269	cancer metastasis	253:269	Membrane type 1 matrix metalloproteinase (MT1-MMP) is a collagenolytic enzyme that has been implicated in normal development and in pathological processes such as cancer metastasis.
14670950	1	3	theme	Membrane	90:97	arg1	MT1-MMP					132:138	MT1-MMP	132:138	MT1-MMP	132:138	Membrane type 1 matrix metalloproteinase (MT1-MMP) is a collagenolytic enzyme that has been implicated in normal development and in pathological processes such as cancer metastasis.
14670950	1	3	theme	Membrane	90:97	arg1	metalloproteinase					113:129	Membrane type 1 matrix metalloproteinase	90:129	Membrane type 1 matrix metalloproteinase (MT1-MMP)	90:139	Membrane type 1 matrix metalloproteinase (MT1-MMP) is a collagenolytic enzyme that has been implicated in normal development and in pathological processes such as cancer metastasis.
14670950	1	3	theme	Membrane	90:97	arg1	enzyme					161:166	a collagenolytic enzyme	144:166	a collagenolytic enzyme that has been implicated in normal development and in pathological processes such as cancer metastasis	144:269	Membrane type 1 matrix metalloproteinase (MT1-MMP) is a collagenolytic enzyme that has been implicated in normal development and in pathological processes such as cancer metastasis.
14670950	7	4	gly	glycosylation	1373:1385	arg1	inhibitor					1421:1429	tissue inhibitor	1414:1429	tissue inhibitor of metalloproteinases-2 (TIMP-2)	1414:1462	Rather, our data support a mechanism whereby glycosylation affects the recruitment of tissue inhibitor of metalloproteinases-2 (TIMP-2) to the cell surface, resulting in defective formation of the MT1-MMP/TIMP-2/proMMP-2 trimeric activation complex.
14670950	7	5	theme	cell	1471:1474	arg1	surface					1476:1482	the cell surface	1467:1482	the cell surface	1467:1482	Rather, our data support a mechanism whereby glycosylation affects the recruitment of tissue inhibitor of metalloproteinases-2 (TIMP-2) to the cell surface, resulting in defective formation of the MT1-MMP/TIMP-2/proMMP-2 trimeric activation complex.
14670950	3	6	from	residues	668:675	arg1	region					704:709	the proline-rich linker region	680:709	the proline-rich linker region	680:709	Enzymatic deglycosylation, site-directed mutagenesis, and lectin precipitation assays were used to demonstrate that MT1-MMP contains O-linked complex carbohydrates on the Thr(291), Thr(299), Thr(300), and/or Ser(301) residues in the proline-rich linker region.
14670950	6	7	theme	stability	1267:1275	arg1	inability					1132:1140	The inability	1128:1140	The inability of carbohydrate-free MT1-MMP to activate proMMP-2	1128:1190	The inability of carbohydrate-free MT1-MMP to activate proMMP-2 was not a result of defective MT1-MMP zymogen activation, aberrant protein stability, or inability of the mature enzyme to oligomerize.
14670950	6	7	theme	stability	1267:1275	arg1	result					1202:1207	a result	1200:1207	a result of defective MT1-MMP zymogen activation, aberrant protein stability, or inability of the mature enzyme to oligomerize	1200:1325	The inability of carbohydrate-free MT1-MMP to activate proMMP-2 was not a result of defective MT1-MMP zymogen activation, aberrant protein stability, or inability of the mature enzyme to oligomerize.
14670950	7	8	theme	tissue	1414:1419	arg1	inhibitor					1421:1429	tissue inhibitor	1414:1429	tissue inhibitor of metalloproteinases-2 (TIMP-2)	1414:1462	Rather, our data support a mechanism whereby glycosylation affects the recruitment of tissue inhibitor of metalloproteinases-2 (TIMP-2) to the cell surface, resulting in defective formation of the MT1-MMP/TIMP-2/proMMP-2 trimeric activation complex.
14670950	5	9	gly	glycosylation	1102:1114	arg1	MT1-MMP					1119:1125	MT1-MMP	1119:1125	MT1-MMP	1119:1125	Although the autolytic processing and interstitial collagenase activity of MT1-MMP were not impaired in glycosylation-deficient mutants, cell surface MT1-MMP-catalyzed activation of pro-matrix metalloproteinase-2 (proMMP-2) required proper glycosylation of MT1-MMP.
14670950	5	10	theme	collagenase	913:923	arg1	activity					925:932	interstitial collagenase activity	900:932	interstitial collagenase activity	900:932	Although the autolytic processing and interstitial collagenase activity of MT1-MMP were not impaired in glycosylation-deficient mutants, cell surface MT1-MMP-catalyzed activation of pro-matrix metalloproteinase-2 (proMMP-2) required proper glycosylation of MT1-MMP.
14670950	3	11	theme	proline-rich	684:695	arg1	region					704:709	the proline-rich linker region	680:709	the proline-rich linker region	680:709	Enzymatic deglycosylation, site-directed mutagenesis, and lectin precipitation assays were used to demonstrate that MT1-MMP contains O-linked complex carbohydrates on the Thr(291), Thr(299), Thr(300), and/or Ser(301) residues in the proline-rich linker region.
14670950	3	12	theme	complex	593:599	arg1	carbohydrates					601:613	O-linked complex carbohydrates	584:613	O-linked complex carbohydrates on the Thr(291), Thr(299), Thr(300), and/or Ser(301) residues in the proline-rich linker region	584:709	Enzymatic deglycosylation, site-directed mutagenesis, and lectin precipitation assays were used to demonstrate that MT1-MMP contains O-linked complex carbohydrates on the Thr(291), Thr(299), Thr(300), and/or Ser(301) residues in the proline-rich linker region.
14670950	1	13	theme	normal	196:201	arg1	development					203:213	normal development	196:213	normal development	196:213	Membrane type 1 matrix metalloproteinase (MT1-MMP) is a collagenolytic enzyme that has been implicated in normal development and in pathological processes such as cancer metastasis.
14670950	6	14	theme	protein	1259:1265	arg1	stability					1267:1275	aberrant protein stability	1250:1275	aberrant protein stability	1250:1275	The inability of carbohydrate-free MT1-MMP to activate proMMP-2 was not a result of defective MT1-MMP zymogen activation, aberrant protein stability, or inability of the mature enzyme to oligomerize.
14670950	3	15	theme	Thr	622:624	arg1	residues					668:675	the Thr(291), Thr(299), Thr(300), and/or Ser(301) residues	618:675	the Thr(291), Thr(299), Thr(300), and/or Ser(301) residues in the proline-rich linker region	618:709	Enzymatic deglycosylation, site-directed mutagenesis, and lectin precipitation assays were used to demonstrate that MT1-MMP contains O-linked complex carbohydrates on the Thr(291), Thr(299), Thr(300), and/or Ser(301) residues in the proline-rich linker region.
14670950	5	16	theme	autolytic	875:883	arg1	processing					885:894	autolytic processing	875:894	autolytic processing	875:894	Although the autolytic processing and interstitial collagenase activity of MT1-MMP were not impaired in glycosylation-deficient mutants, cell surface MT1-MMP-catalyzed activation of pro-matrix metalloproteinase-2 (proMMP-2) required proper glycosylation of MT1-MMP.
14670950	6	17	theme	zymogen	1230:1236	arg1	activation					1238:1247	defective MT1-MMP zymogen activation	1212:1247	defective MT1-MMP zymogen activation	1212:1247	The inability of carbohydrate-free MT1-MMP to activate proMMP-2 was not a result of defective MT1-MMP zymogen activation, aberrant protein stability, or inability of the mature enzyme to oligomerize.
14670950	5	18	theme	metalloproteinase-2	1055:1073	arg1	activation					1030:1039	cell surface MT1-MMP-catalyzed activation	999:1039	cell surface MT1-MMP-catalyzed activation of pro-matrix metalloproteinase-2 (proMMP-2)	999:1084	Although the autolytic processing and interstitial collagenase activity of MT1-MMP were not impaired in glycosylation-deficient mutants, cell surface MT1-MMP-catalyzed activation of pro-matrix metalloproteinase-2 (proMMP-2) required proper glycosylation of MT1-MMP.
14670950	3	19	link	O-linked	584:591	arg1	carbohydrates					601:613	O-linked complex carbohydrates	584:613	O-linked complex carbohydrates on the Thr(291), Thr(299), Thr(300), and/or Ser(301) residues in the proline-rich linker region	584:709	Enzymatic deglycosylation, site-directed mutagenesis, and lectin precipitation assays were used to demonstrate that MT1-MMP contains O-linked complex carbohydrates on the Thr(291), Thr(299), Thr(300), and/or Ser(301) residues in the proline-rich linker region.
14670950	6	20	theme	defective	1212:1220	arg1	activation					1238:1247	defective MT1-MMP zymogen activation	1212:1247	defective MT1-MMP zymogen activation	1212:1247	The inability of carbohydrate-free MT1-MMP to activate proMMP-2 was not a result of defective MT1-MMP zymogen activation, aberrant protein stability, or inability of the mature enzyme to oligomerize.
14670950	4	21	gly	glycoforms	720:729	arg1	MT1-MMP					712:718	MT1-MMP glycoforms	712:729	MT1-MMP glycoforms	712:729	MT1-MMP glycoforms were detected in human cancer cell lines, suggesting that MT1-MMP activity may be regulated by differential glycosylation in vivo.
14670950	0	22	theme	metalloproteinase	71:87	arg1	profile					37:43	the substrate profile	23:43	the substrate profile of membrane type 1 matrix metalloproteinase	23:87	Glycosylation broadens the substrate profile of membrane type 1 matrix metalloproteinase.
14670950	5	23	dep	processing	885:894	arg1	the					871:873	the	871:873	the	871:873	Although the autolytic processing and interstitial collagenase activity of MT1-MMP were not impaired in glycosylation-deficient mutants, cell surface MT1-MMP-catalyzed activation of pro-matrix metalloproteinase-2 (proMMP-2) required proper glycosylation of MT1-MMP.
14670950	5	24	theme	MT1-MMP	1119:1125	arg1	glycosylation					1102:1114	proper glycosylation	1095:1114	proper glycosylation of MT1-MMP	1095:1125	Although the autolytic processing and interstitial collagenase activity of MT1-MMP were not impaired in glycosylation-deficient mutants, cell surface MT1-MMP-catalyzed activation of pro-matrix metalloproteinase-2 (proMMP-2) required proper glycosylation of MT1-MMP.
14670950	1	25	theme	type	99:102	arg1	MT1-MMP					132:138	MT1-MMP	132:138	MT1-MMP	132:138	Membrane type 1 matrix metalloproteinase (MT1-MMP) is a collagenolytic enzyme that has been implicated in normal development and in pathological processes such as cancer metastasis.
14670950	1	25	theme	type	99:102	arg1	metalloproteinase					113:129	Membrane type 1 matrix metalloproteinase	90:129	Membrane type 1 matrix metalloproteinase (MT1-MMP)	90:139	Membrane type 1 matrix metalloproteinase (MT1-MMP) is a collagenolytic enzyme that has been implicated in normal development and in pathological processes such as cancer metastasis.
14670950	1	25	theme	type	99:102	arg1	enzyme					161:166	a collagenolytic enzyme	144:166	a collagenolytic enzyme that has been implicated in normal development and in pathological processes such as cancer metastasis	144:269	Membrane type 1 matrix metalloproteinase (MT1-MMP) is a collagenolytic enzyme that has been implicated in normal development and in pathological processes such as cancer metastasis.
14670950	3	26	theme	site-directed	478:490	arg1	mutagenesis					492:502	site-directed mutagenesis	478:502	site-directed mutagenesis	478:502	Enzymatic deglycosylation, site-directed mutagenesis, and lectin precipitation assays were used to demonstrate that MT1-MMP contains O-linked complex carbohydrates on the Thr(291), Thr(299), Thr(300), and/or Ser(301) residues in the proline-rich linker region.
14670950	1	27	theme	matrix	106:111	arg1	MT1-MMP					132:138	MT1-MMP	132:138	MT1-MMP	132:138	Membrane type 1 matrix metalloproteinase (MT1-MMP) is a collagenolytic enzyme that has been implicated in normal development and in pathological processes such as cancer metastasis.
14670950	1	27	theme	matrix	106:111	arg1	metalloproteinase					113:129	Membrane type 1 matrix metalloproteinase	90:129	Membrane type 1 matrix metalloproteinase (MT1-MMP)	90:139	Membrane type 1 matrix metalloproteinase (MT1-MMP) is a collagenolytic enzyme that has been implicated in normal development and in pathological processes such as cancer metastasis.
14670950	1	27	theme	matrix	106:111	arg1	enzyme					161:166	a collagenolytic enzyme	144:166	a collagenolytic enzyme that has been implicated in normal development and in pathological processes such as cancer metastasis	144:269	Membrane type 1 matrix metalloproteinase (MT1-MMP) is a collagenolytic enzyme that has been implicated in normal development and in pathological processes such as cancer metastasis.
14670950	4	28	located	detected	736:743	arg2	glycoforms					720:729	MT1-MMP glycoforms	712:729	MT1-MMP glycoforms	712:729	MT1-MMP glycoforms were detected in human cancer cell lines, suggesting that MT1-MMP activity may be regulated by differential glycosylation in vivo.
14670950	4	28	located	detected	736:743	arg1	lines					766:770	human cancer cell lines	748:770	human cancer cell lines	748:770	MT1-MMP glycoforms were detected in human cancer cell lines, suggesting that MT1-MMP activity may be regulated by differential glycosylation in vivo.
14670950	3	29	theme	Thr	642:644	arg1	residues					668:675	the Thr(291), Thr(299), Thr(300), and/or Ser(301) residues	618:675	the Thr(291), Thr(299), Thr(300), and/or Ser(301) residues in the proline-rich linker region	618:709	Enzymatic deglycosylation, site-directed mutagenesis, and lectin precipitation assays were used to demonstrate that MT1-MMP contains O-linked complex carbohydrates on the Thr(291), Thr(299), Thr(300), and/or Ser(301) residues in the proline-rich linker region.
14670950	3	30	theme	deglycosylation	461:475	arg1	assays					530:535	Enzymatic deglycosylation, site-directed mutagenesis, and lectin precipitation assays	451:535	Enzymatic deglycosylation, site-directed mutagenesis, and lectin precipitation assays	451:535	Enzymatic deglycosylation, site-directed mutagenesis, and lectin precipitation assays were used to demonstrate that MT1-MMP contains O-linked complex carbohydrates on the Thr(291), Thr(299), Thr(300), and/or Ser(301) residues in the proline-rich linker region.
14670950	7	31	theme	activation	1558:1567	arg1	complex					1569:1575	the MT1-MMP/TIMP-2/proMMP-2 trimeric activation complex	1521:1575	the MT1-MMP/TIMP-2/proMMP-2 trimeric activation complex	1521:1575	Rather, our data support a mechanism whereby glycosylation affects the recruitment of tissue inhibitor of metalloproteinases-2 (TIMP-2) to the cell surface, resulting in defective formation of the MT1-MMP/TIMP-2/proMMP-2 trimeric activation complex.
14670950	5	32	theme	surface	1004:1010	arg1	activation					1030:1039	cell surface MT1-MMP-catalyzed activation	999:1039	cell surface MT1-MMP-catalyzed activation of pro-matrix metalloproteinase-2 (proMMP-2)	999:1084	Although the autolytic processing and interstitial collagenase activity of MT1-MMP were not impaired in glycosylation-deficient mutants, cell surface MT1-MMP-catalyzed activation of pro-matrix metalloproteinase-2 (proMMP-2) required proper glycosylation of MT1-MMP.
14670950	3	33	theme	lectin	509:514	arg1	assays					530:535	Enzymatic deglycosylation, site-directed mutagenesis, and lectin precipitation assays	451:535	Enzymatic deglycosylation, site-directed mutagenesis, and lectin precipitation assays	451:535	Enzymatic deglycosylation, site-directed mutagenesis, and lectin precipitation assays were used to demonstrate that MT1-MMP contains O-linked complex carbohydrates on the Thr(291), Thr(299), Thr(300), and/or Ser(301) residues in the proline-rich linker region.
14670950	0	34	theme	membrane	48:55	arg1	metalloproteinase					71:87	membrane type 1 matrix metalloproteinase	48:87	membrane type 1 matrix metalloproteinase	48:87	Glycosylation broadens the substrate profile of membrane type 1 matrix metalloproteinase.
14670950	7	35	theme	MT1-MMP/TIMP-2/proMMP-2	1525:1547	arg1	complex					1569:1575	the MT1-MMP/TIMP-2/proMMP-2 trimeric activation complex	1521:1575	the MT1-MMP/TIMP-2/proMMP-2 trimeric activation complex	1521:1575	Rather, our data support a mechanism whereby glycosylation affects the recruitment of tissue inhibitor of metalloproteinases-2 (TIMP-2) to the cell surface, resulting in defective formation of the MT1-MMP/TIMP-2/proMMP-2 trimeric activation complex.
14670950	4	36	theme	human	748:752	arg1	lines					766:770	human cancer cell lines	748:770	human cancer cell lines	748:770	MT1-MMP glycoforms were detected in human cancer cell lines, suggesting that MT1-MMP activity may be regulated by differential glycosylation in vivo.
14670950	2	37	theme	post-translational	328:345	arg1	level					347:351	the post-translational level	324:351	the post-translational level	324:351	The activity of MT1-MMP is regulated extensively at the post-translational level, and the current data support the hypothesis that MT1-MMP activity is modulated by glycosylation.
14670950	5	38	theme	glycosylation-deficient	966:988	arg1	mutants					990:996	glycosylation-deficient mutants	966:996	glycosylation-deficient mutants	966:996	Although the autolytic processing and interstitial collagenase activity of MT1-MMP were not impaired in glycosylation-deficient mutants, cell surface MT1-MMP-catalyzed activation of pro-matrix metalloproteinase-2 (proMMP-2) required proper glycosylation of MT1-MMP.
14670950	8	39	theme	post-translational	1638:1655	arg1	control					1657:1663	post-translational control	1638:1663	post-translational control of MT1-MMP activity	1638:1683	These data provide evidence for an additional mechanism for post-translational control of MT1-MMP activity and suggest that glycosylation of MT1-MMP may regulate its substrate targeting.
14670950	4	40	theme	cell	761:764	arg1	lines					766:770	human cancer cell lines	748:770	human cancer cell lines	748:770	MT1-MMP glycoforms were detected in human cancer cell lines, suggesting that MT1-MMP activity may be regulated by differential glycosylation in vivo.
14670950	8	41	theme	MT1-MMP	1719:1725	arg1	glycosylation					1702:1714	glycosylation	1702:1714	glycosylation of MT1-MMP	1702:1725	These data provide evidence for an additional mechanism for post-translational control of MT1-MMP activity and suggest that glycosylation of MT1-MMP may regulate its substrate targeting.
14670950	7	42	theme	defective	1498:1506	arg1	formation					1508:1516	defective formation	1498:1516	defective formation of the MT1-MMP/TIMP-2/proMMP-2 trimeric activation complex	1498:1575	Rather, our data support a mechanism whereby glycosylation affects the recruitment of tissue inhibitor of metalloproteinases-2 (TIMP-2) to the cell surface, resulting in defective formation of the MT1-MMP/TIMP-2/proMMP-2 trimeric activation complex.
14670950	6	43	theme	enzyme	1305:1310	arg1	stability					1267:1275	aberrant protein stability	1250:1275	aberrant protein stability	1250:1275	The inability of carbohydrate-free MT1-MMP to activate proMMP-2 was not a result of defective MT1-MMP zymogen activation, aberrant protein stability, or inability of the mature enzyme to oligomerize.
14670950	6	43	theme	enzyme	1305:1310	arg1	inability					1281:1289	inability	1281:1289	inability of the mature enzyme to oligomerize	1281:1325	The inability of carbohydrate-free MT1-MMP to activate proMMP-2 was not a result of defective MT1-MMP zymogen activation, aberrant protein stability, or inability of the mature enzyme to oligomerize.
14670950	6	43	theme	enzyme	1305:1310	arg1	activation					1238:1247	defective MT1-MMP zymogen activation	1212:1247	defective MT1-MMP zymogen activation	1212:1247	The inability of carbohydrate-free MT1-MMP to activate proMMP-2 was not a result of defective MT1-MMP zymogen activation, aberrant protein stability, or inability of the mature enzyme to oligomerize.
14670950	8	44	theme	activity	1676:1683	arg1	control					1657:1663	post-translational control	1638:1663	post-translational control of MT1-MMP activity	1638:1683	These data provide evidence for an additional mechanism for post-translational control of MT1-MMP activity and suggest that glycosylation of MT1-MMP may regulate its substrate targeting.
14670950	3	45	theme	Ser	659:661	arg1	residues					668:675	the Thr(291), Thr(299), Thr(300), and/or Ser(301) residues	618:675	the Thr(291), Thr(299), Thr(300), and/or Ser(301) residues in the proline-rich linker region	618:709	Enzymatic deglycosylation, site-directed mutagenesis, and lectin precipitation assays were used to demonstrate that MT1-MMP contains O-linked complex carbohydrates on the Thr(291), Thr(299), Thr(300), and/or Ser(301) residues in the proline-rich linker region.
14670950	2	46	theme	MT1-MMP	288:294	arg1	activity					276:283	The activity	272:283	The activity of MT1-MMP	272:294	The activity of MT1-MMP is regulated extensively at the post-translational level, and the current data support the hypothesis that MT1-MMP activity is modulated by glycosylation.
14670950	8	47	theme	substrate	1744:1752	arg1	targeting					1754:1762	its substrate targeting	1740:1762	its substrate targeting	1740:1762	These data provide evidence for an additional mechanism for post-translational control of MT1-MMP activity and suggest that glycosylation of MT1-MMP may regulate its substrate targeting.
14670950	4	48	theme	differential	826:837	arg1	glycosylation					839:851	differential glycosylation	826:851	differential glycosylation	826:851	MT1-MMP glycoforms were detected in human cancer cell lines, suggesting that MT1-MMP activity may be regulated by differential glycosylation in vivo.
14670950	6	49	theme	inability	1281:1289	arg1	inability					1132:1140	The inability	1128:1140	The inability of carbohydrate-free MT1-MMP to activate proMMP-2	1128:1190	The inability of carbohydrate-free MT1-MMP to activate proMMP-2 was not a result of defective MT1-MMP zymogen activation, aberrant protein stability, or inability of the mature enzyme to oligomerize.
14670950	6	49	theme	inability	1281:1289	arg1	result					1202:1207	a result	1200:1207	a result of defective MT1-MMP zymogen activation, aberrant protein stability, or inability of the mature enzyme to oligomerize	1200:1325	The inability of carbohydrate-free MT1-MMP to activate proMMP-2 was not a result of defective MT1-MMP zymogen activation, aberrant protein stability, or inability of the mature enzyme to oligomerize.
14670950	4	50	theme	MT1-MMP	789:795	arg1	activity					797:804	MT1-MMP activity	789:804	MT1-MMP activity	789:804	MT1-MMP glycoforms were detected in human cancer cell lines, suggesting that MT1-MMP activity may be regulated by differential glycosylation in vivo.
14670950	7	51	theme	metalloproteinases-2	1434:1453	arg1	inhibitor					1421:1429	tissue inhibitor	1414:1429	tissue inhibitor of metalloproteinases-2 (TIMP-2)	1414:1462	Rather, our data support a mechanism whereby glycosylation affects the recruitment of tissue inhibitor of metalloproteinases-2 (TIMP-2) to the cell surface, resulting in defective formation of the MT1-MMP/TIMP-2/proMMP-2 trimeric activation complex.
14670950	3	52	theme	O-linked	584:591	arg1	carbohydrates					601:613	O-linked complex carbohydrates	584:613	O-linked complex carbohydrates on the Thr(291), Thr(299), Thr(300), and/or Ser(301) residues in the proline-rich linker region	584:709	Enzymatic deglycosylation, site-directed mutagenesis, and lectin precipitation assays were used to demonstrate that MT1-MMP contains O-linked complex carbohydrates on the Thr(291), Thr(299), Thr(300), and/or Ser(301) residues in the proline-rich linker region.
14670950	7	53	theme	inhibitor	1421:1429	arg1	recruitment					1399:1409	the recruitment	1395:1409	the recruitment of tissue inhibitor of metalloproteinases-2 (TIMP-2) to the cell surface	1395:1482	Rather, our data support a mechanism whereby glycosylation affects the recruitment of tissue inhibitor of metalloproteinases-2 (TIMP-2) to the cell surface, resulting in defective formation of the MT1-MMP/TIMP-2/proMMP-2 trimeric activation complex.
14670950	3	54	theme	linker	697:702	arg1	region					704:709	the proline-rich linker region	680:709	the proline-rich linker region	680:709	Enzymatic deglycosylation, site-directed mutagenesis, and lectin precipitation assays were used to demonstrate that MT1-MMP contains O-linked complex carbohydrates on the Thr(291), Thr(299), Thr(300), and/or Ser(301) residues in the proline-rich linker region.
14670950	6	55	theme	aberrant	1250:1257	arg1	stability					1267:1275	aberrant protein stability	1250:1275	aberrant protein stability	1250:1275	The inability of carbohydrate-free MT1-MMP to activate proMMP-2 was not a result of defective MT1-MMP zymogen activation, aberrant protein stability, or inability of the mature enzyme to oligomerize.
14670950	5	56	theme	proper	1095:1100	arg1	glycosylation					1102:1114	proper glycosylation	1095:1114	proper glycosylation of MT1-MMP	1095:1125	Although the autolytic processing and interstitial collagenase activity of MT1-MMP were not impaired in glycosylation-deficient mutants, cell surface MT1-MMP-catalyzed activation of pro-matrix metalloproteinase-2 (proMMP-2) required proper glycosylation of MT1-MMP.
14670950	6	57	theme	activation	1238:1247	arg1	inability					1132:1140	The inability	1128:1140	The inability of carbohydrate-free MT1-MMP to activate proMMP-2	1128:1190	The inability of carbohydrate-free MT1-MMP to activate proMMP-2 was not a result of defective MT1-MMP zymogen activation, aberrant protein stability, or inability of the mature enzyme to oligomerize.
14670950	6	57	theme	activation	1238:1247	arg1	result					1202:1207	a result	1200:1207	a result of defective MT1-MMP zymogen activation, aberrant protein stability, or inability of the mature enzyme to oligomerize	1200:1325	The inability of carbohydrate-free MT1-MMP to activate proMMP-2 was not a result of defective MT1-MMP zymogen activation, aberrant protein stability, or inability of the mature enzyme to oligomerize.
14670950	5	58	theme	pro-matrix	1044:1053	arg1	metalloproteinase-2					1055:1073	pro-matrix metalloproteinase-2	1044:1073	pro-matrix metalloproteinase-2 (proMMP-2)	1044:1084	Although the autolytic processing and interstitial collagenase activity of MT1-MMP were not impaired in glycosylation-deficient mutants, cell surface MT1-MMP-catalyzed activation of pro-matrix metalloproteinase-2 (proMMP-2) required proper glycosylation of MT1-MMP.
14670950	5	58	theme	pro-matrix	1044:1053	arg1	proMMP-2					1076:1083	proMMP-2	1076:1083	proMMP-2	1076:1083	Although the autolytic processing and interstitial collagenase activity of MT1-MMP were not impaired in glycosylation-deficient mutants, cell surface MT1-MMP-catalyzed activation of pro-matrix metalloproteinase-2 (proMMP-2) required proper glycosylation of MT1-MMP.
14670950	3	59	theme	Thr	632:634	arg1	residues					668:675	the Thr(291), Thr(299), Thr(300), and/or Ser(301) residues	618:675	the Thr(291), Thr(299), Thr(300), and/or Ser(301) residues in the proline-rich linker region	618:709	Enzymatic deglycosylation, site-directed mutagenesis, and lectin precipitation assays were used to demonstrate that MT1-MMP contains O-linked complex carbohydrates on the Thr(291), Thr(299), Thr(300), and/or Ser(301) residues in the proline-rich linker region.
14670950	6	60	theme	MT1-MMP	1222:1228	arg1	activation					1238:1247	defective MT1-MMP zymogen activation	1212:1247	defective MT1-MMP zymogen activation	1212:1247	The inability of carbohydrate-free MT1-MMP to activate proMMP-2 was not a result of defective MT1-MMP zymogen activation, aberrant protein stability, or inability of the mature enzyme to oligomerize.
14670950	3	61	from	carbohydrates	601:613	arg1	residues					668:675	the Thr(291), Thr(299), Thr(300), and/or Ser(301) residues	618:675	the Thr(291), Thr(299), Thr(300), and/or Ser(301) residues in the proline-rich linker region	618:709	Enzymatic deglycosylation, site-directed mutagenesis, and lectin precipitation assays were used to demonstrate that MT1-MMP contains O-linked complex carbohydrates on the Thr(291), Thr(299), Thr(300), and/or Ser(301) residues in the proline-rich linker region.
14670950	0	62	theme	matrix	64:69	arg1	metalloproteinase					71:87	membrane type 1 matrix metalloproteinase	48:87	membrane type 1 matrix metalloproteinase	48:87	Glycosylation broadens the substrate profile of membrane type 1 matrix metalloproteinase.
14670950	1	63	theme	collagenolytic	146:159	arg1	metalloproteinase					113:129	Membrane type 1 matrix metalloproteinase	90:129	Membrane type 1 matrix metalloproteinase (MT1-MMP)	90:139	Membrane type 1 matrix metalloproteinase (MT1-MMP) is a collagenolytic enzyme that has been implicated in normal development and in pathological processes such as cancer metastasis.
14670950	1	63	theme	collagenolytic	146:159	arg1	enzyme					161:166	a collagenolytic enzyme	144:166	a collagenolytic enzyme that has been implicated in normal development and in pathological processes such as cancer metastasis	144:269	Membrane type 1 matrix metalloproteinase (MT1-MMP) is a collagenolytic enzyme that has been implicated in normal development and in pathological processes such as cancer metastasis.
14670950	5	64	theme	MT1-MMP	937:943	arg1	activity					925:932	interstitial collagenase activity	900:932	interstitial collagenase activity	900:932	Although the autolytic processing and interstitial collagenase activity of MT1-MMP were not impaired in glycosylation-deficient mutants, cell surface MT1-MMP-catalyzed activation of pro-matrix metalloproteinase-2 (proMMP-2) required proper glycosylation of MT1-MMP.
14670950	5	64	theme	MT1-MMP	937:943	arg1	processing					885:894	autolytic processing	875:894	autolytic processing	875:894	Although the autolytic processing and interstitial collagenase activity of MT1-MMP were not impaired in glycosylation-deficient mutants, cell surface MT1-MMP-catalyzed activation of pro-matrix metalloproteinase-2 (proMMP-2) required proper glycosylation of MT1-MMP.
14670950	6	65	theme	MT1-MMP	1163:1169	arg1	inability					1132:1140	The inability	1128:1140	The inability of carbohydrate-free MT1-MMP to activate proMMP-2	1128:1190	The inability of carbohydrate-free MT1-MMP to activate proMMP-2 was not a result of defective MT1-MMP zymogen activation, aberrant protein stability, or inability of the mature enzyme to oligomerize.
14670950	6	65	theme	MT1-MMP	1163:1169	arg1	result					1202:1207	a result	1200:1207	a result of defective MT1-MMP zymogen activation, aberrant protein stability, or inability of the mature enzyme to oligomerize	1200:1325	The inability of carbohydrate-free MT1-MMP to activate proMMP-2 was not a result of defective MT1-MMP zymogen activation, aberrant protein stability, or inability of the mature enzyme to oligomerize.
14670950	4	66	theme	MT1-MMP	712:718	arg1	glycoforms					720:729	MT1-MMP glycoforms	712:729	MT1-MMP glycoforms	712:729	MT1-MMP glycoforms were detected in human cancer cell lines, suggesting that MT1-MMP activity may be regulated by differential glycosylation in vivo.
14670950	3	67	theme	Enzymatic	451:459	arg1	deglycosylation					461:475	Enzymatic deglycosylation	451:475	Enzymatic deglycosylation	451:475	Enzymatic deglycosylation, site-directed mutagenesis, and lectin precipitation assays were used to demonstrate that MT1-MMP contains O-linked complex carbohydrates on the Thr(291), Thr(299), Thr(300), and/or Ser(301) residues in the proline-rich linker region.
14670950	5	68	theme	interstitial	900:911	arg1	collagenase					913:923	interstitial collagenase	900:923	interstitial collagenase activity	900:932	Although the autolytic processing and interstitial collagenase activity of MT1-MMP were not impaired in glycosylation-deficient mutants, cell surface MT1-MMP-catalyzed activation of pro-matrix metalloproteinase-2 (proMMP-2) required proper glycosylation of MT1-MMP.
14670950	0	69	theme	substrate	27:35	arg1	profile					37:43	the substrate profile	23:43	the substrate profile of membrane type 1 matrix metalloproteinase	23:87	Glycosylation broadens the substrate profile of membrane type 1 matrix metalloproteinase.
14670950	3	70	theme	mutagenesis	492:502	arg1	assays					530:535	Enzymatic deglycosylation, site-directed mutagenesis, and lectin precipitation assays	451:535	Enzymatic deglycosylation, site-directed mutagenesis, and lectin precipitation assays	451:535	Enzymatic deglycosylation, site-directed mutagenesis, and lectin precipitation assays were used to demonstrate that MT1-MMP contains O-linked complex carbohydrates on the Thr(291), Thr(299), Thr(300), and/or Ser(301) residues in the proline-rich linker region.
14670950	5	71	theme	cell	999:1002	arg1	activation					1030:1039	cell surface MT1-MMP-catalyzed activation	999:1039	cell surface MT1-MMP-catalyzed activation of pro-matrix metalloproteinase-2 (proMMP-2)	999:1084	Although the autolytic processing and interstitial collagenase activity of MT1-MMP were not impaired in glycosylation-deficient mutants, cell surface MT1-MMP-catalyzed activation of pro-matrix metalloproteinase-2 (proMMP-2) required proper glycosylation of MT1-MMP.
14670950	8	72	theme	additional	1613:1622	arg1	mechanism					1624:1632	an additional mechanism	1610:1632	an additional mechanism for post-translational control of MT1-MMP activity	1610:1683	These data provide evidence for an additional mechanism for post-translational control of MT1-MMP activity and suggest that glycosylation of MT1-MMP may regulate its substrate targeting.
14670950	2	73	theme	MT1-MMP	403:409	arg1	activity					411:418	MT1-MMP activity	403:418	MT1-MMP activity	403:418	The activity of MT1-MMP is regulated extensively at the post-translational level, and the current data support the hypothesis that MT1-MMP activity is modulated by glycosylation.
14670950	0	74	theme	type	57:60	arg1	metalloproteinase					71:87	membrane type 1 matrix metalloproteinase	48:87	membrane type 1 matrix metalloproteinase	48:87	Glycosylation broadens the substrate profile of membrane type 1 matrix metalloproteinase.
14670950	7	75	theme	complex	1569:1575	arg1	formation					1508:1516	defective formation	1498:1516	defective formation of the MT1-MMP/TIMP-2/proMMP-2 trimeric activation complex	1498:1575	Rather, our data support a mechanism whereby glycosylation affects the recruitment of tissue inhibitor of metalloproteinases-2 (TIMP-2) to the cell surface, resulting in defective formation of the MT1-MMP/TIMP-2/proMMP-2 trimeric activation complex.
14670950	5	76	theme	MT1-MMP-catalyzed	1012:1028	arg1	activation					1030:1039	cell surface MT1-MMP-catalyzed activation	999:1039	cell surface MT1-MMP-catalyzed activation of pro-matrix metalloproteinase-2 (proMMP-2)	999:1084	Although the autolytic processing and interstitial collagenase activity of MT1-MMP were not impaired in glycosylation-deficient mutants, cell surface MT1-MMP-catalyzed activation of pro-matrix metalloproteinase-2 (proMMP-2) required proper glycosylation of MT1-MMP.
14670950	6	77	theme	carbohydrate-free	1145:1161	arg1	MT1-MMP					1163:1169	carbohydrate-free MT1-MMP	1145:1169	carbohydrate-free MT1-MMP	1145:1169	The inability of carbohydrate-free MT1-MMP to activate proMMP-2 was not a result of defective MT1-MMP zymogen activation, aberrant protein stability, or inability of the mature enzyme to oligomerize.
14670950	3	78	contain	contains	575:582	arg1	MT1-MMP					567:573	MT1-MMP	567:573	MT1-MMP	567:573	Enzymatic deglycosylation, site-directed mutagenesis, and lectin precipitation assays were used to demonstrate that MT1-MMP contains O-linked complex carbohydrates on the Thr(291), Thr(299), Thr(300), and/or Ser(301) residues in the proline-rich linker region.
14670950	3	78	contain	contains	575:582	arg2	carbohydrates					601:613	O-linked complex carbohydrates	584:613	O-linked complex carbohydrates on the Thr(291), Thr(299), Thr(300), and/or Ser(301) residues in the proline-rich linker region	584:709	Enzymatic deglycosylation, site-directed mutagenesis, and lectin precipitation assays were used to demonstrate that MT1-MMP contains O-linked complex carbohydrates on the Thr(291), Thr(299), Thr(300), and/or Ser(301) residues in the proline-rich linker region.
14670950	3	79	theme	precipitation	516:528	arg1	assays					530:535	Enzymatic deglycosylation, site-directed mutagenesis, and lectin precipitation assays	451:535	Enzymatic deglycosylation, site-directed mutagenesis, and lectin precipitation assays	451:535	Enzymatic deglycosylation, site-directed mutagenesis, and lectin precipitation assays were used to demonstrate that MT1-MMP contains O-linked complex carbohydrates on the Thr(291), Thr(299), Thr(300), and/or Ser(301) residues in the proline-rich linker region.
14670950	3	80	used	used	542:545	arg2	assays					530:535	Enzymatic deglycosylation, site-directed mutagenesis, and lectin precipitation assays	451:535	Enzymatic deglycosylation, site-directed mutagenesis, and lectin precipitation assays	451:535	Enzymatic deglycosylation, site-directed mutagenesis, and lectin precipitation assays were used to demonstrate that MT1-MMP contains O-linked complex carbohydrates on the Thr(291), Thr(299), Thr(300), and/or Ser(301) residues in the proline-rich linker region.
14670950	7	81	theme	trimeric	1549:1556	arg1	complex					1569:1575	the MT1-MMP/TIMP-2/proMMP-2 trimeric activation complex	1521:1575	the MT1-MMP/TIMP-2/proMMP-2 trimeric activation complex	1521:1575	Rather, our data support a mechanism whereby glycosylation affects the recruitment of tissue inhibitor of metalloproteinases-2 (TIMP-2) to the cell surface, resulting in defective formation of the MT1-MMP/TIMP-2/proMMP-2 trimeric activation complex.
14670950	1	82	theme	pathological	222:233	arg1	processes					235:243	pathological processes	222:243	pathological processes such as cancer metastasis	222:269	Membrane type 1 matrix metalloproteinase (MT1-MMP) is a collagenolytic enzyme that has been implicated in normal development and in pathological processes such as cancer metastasis.
14670950	1	82	theme	pathological	222:233	arg1	metastasis					260:269	cancer metastasis	253:269	cancer metastasis	253:269	Membrane type 1 matrix metalloproteinase (MT1-MMP) is a collagenolytic enzyme that has been implicated in normal development and in pathological processes such as cancer metastasis.
14670950	8	83	theme	MT1-MMP	1668:1674	arg1	activity					1676:1683	MT1-MMP activity	1668:1683	MT1-MMP activity	1668:1683	These data provide evidence for an additional mechanism for post-translational control of MT1-MMP activity and suggest that glycosylation of MT1-MMP may regulate its substrate targeting.
14670950	4	84	theme	cancer	754:759	arg1	lines					766:770	human cancer cell lines	748:770	human cancer cell lines	748:770	MT1-MMP glycoforms were detected in human cancer cell lines, suggesting that MT1-MMP activity may be regulated by differential glycosylation in vivo.
14670950	2	85	theme	current	362:368	arg1	data					370:373	the current data	358:373	the current data	358:373	The activity of MT1-MMP is regulated extensively at the post-translational level, and the current data support the hypothesis that MT1-MMP activity is modulated by glycosylation.
26197318	5	0	theme	NOS1AP	761:766	arg1	O-GlcNAc					749:756	Higher O-GlcNAc	742:756	Higher O-GlcNAc of NOS1AP	742:766	Higher O-GlcNAc of NOS1AP was detected during glutamate-induced neuronal apoptosis.
26197318	6	1	theme	oxide	924:928	arg1	interaction					882:892	the interaction	878:892	the interaction of NOS1AP and neuronal nitric oxide syntheses (nNOS)	878:945	Furthermore, with O-GlcNAc sites of NOS1AP mutated, the interaction of NOS1AP and neuronal nitric oxide syntheses (nNOS) decreases.
26197318	7	2	theme	neuronal	992:999	arg1	apoptosis					1001:1009	glutamate-induced neuronal apoptosis	974:1009	glutamate-induced neuronal apoptosis	974:1009	Finally, during glutamate-induced neuronal apoptosis, decreasing the O-GlcNAc modification of NOS1AP results in more severe neuronal apoptosis.
26197318	3	3	theme	synthase	511:518	arg1	adaptor					520:526	nitric oxide synthase adaptor	498:526	nitric oxide synthase adaptor (NOS1AP)	498:535	Here we found that nitric oxide synthase adaptor (NOS1AP), which plays an important part in glutamate-induced neuronal apoptosis, carries the modification of O-GlcNAc.
26197318	3	3	theme	synthase	511:518	arg1	NOS1AP					529:534	NOS1AP	529:534	NOS1AP	529:534	Here we found that nitric oxide synthase adaptor (NOS1AP), which plays an important part in glutamate-induced neuronal apoptosis, carries the modification of O-GlcNAc.
26197318	5	4	theme	Higher	742:747	arg1	O-GlcNAc					749:756	Higher O-GlcNAc	742:756	Higher O-GlcNAc of NOS1AP	742:766	Higher O-GlcNAc of NOS1AP was detected during glutamate-induced neuronal apoptosis.
26197318	6	5	theme	nitric	917:922	arg1	oxide					924:928	neuronal nitric oxide	908:928	neuronal nitric oxide	908:928	Furthermore, with O-GlcNAc sites of NOS1AP mutated, the interaction of NOS1AP and neuronal nitric oxide syntheses (nNOS) decreases.
26197318	8	6	mod	modification	1142:1153	arg1	NOS1AP					1158:1163	NOS1AP	1158:1163	NOS1AP	1158:1163	All these results suggest that O-GlcNAc modification of NOS1AP exerts protective effects during glutamate-induced neuronal apoptosis.
26197318	8	6	mod	modification	1142:1153	arg3	O-GlcNAc					1133:1140	O-GlcNAc modification	1133:1153	O-GlcNAc modification of NOS1AP	1133:1163	All these results suggest that O-GlcNAc modification of NOS1AP exerts protective effects during glutamate-induced neuronal apoptosis.
26197318	6	7	theme	neuronal	908:915	arg1	oxide					924:928	neuronal nitric oxide	908:928	neuronal nitric oxide	908:928	Furthermore, with O-GlcNAc sites of NOS1AP mutated, the interaction of NOS1AP and neuronal nitric oxide syntheses (nNOS) decreases.
26197318	1	8	from	cycles	178:183	arg1	and					188:190	and	188:190	and	188:190	O-Linked N-acetylglucosamine, or O-GlcNAc, is a dynamic post-translational modification that cycles on and off serine and threonine residues of nucleocytoplasmic and mitochondrial proteins.
26197318	8	9	theme	neuronal	1216:1223	arg1	apoptosis					1225:1233	glutamate-induced neuronal apoptosis	1198:1233	glutamate-induced neuronal apoptosis	1198:1233	All these results suggest that O-GlcNAc modification of NOS1AP exerts protective effects during glutamate-induced neuronal apoptosis.
26197318	3	10	theme	nitric	498:503	arg1	synthase					511:518	nitric oxide synthase	498:518	nitric oxide synthase adaptor (NOS1AP)	498:535	Here we found that nitric oxide synthase adaptor (NOS1AP), which plays an important part in glutamate-induced neuronal apoptosis, carries the modification of O-GlcNAc.
26197318	5	11	theme	neuronal	806:813	arg1	apoptosis					815:823	glutamate-induced neuronal apoptosis	788:823	glutamate-induced neuronal apoptosis	788:823	Higher O-GlcNAc of NOS1AP was detected during glutamate-induced neuronal apoptosis.
26197318	1	12	theme	O-Linked	85:92	arg1	modification					160:171	a dynamic post-translational modification	131:171	a dynamic post-translational modification that cycles on and off serine and threonine residues of nucleocytoplasmic and mitochondrial proteins	131:272	O-Linked N-acetylglucosamine, or O-GlcNAc, is a dynamic post-translational modification that cycles on and off serine and threonine residues of nucleocytoplasmic and mitochondrial proteins.
26197318	1	12	theme	O-Linked	85:92	arg1	N-acetylglucosamine					94:112	O-Linked N-acetylglucosamine	85:112	O-Linked N-acetylglucosamine	85:112	O-Linked N-acetylglucosamine, or O-GlcNAc, is a dynamic post-translational modification that cycles on and off serine and threonine residues of nucleocytoplasmic and mitochondrial proteins.
26197318	1	12	theme	O-Linked	85:92	arg1	O-GlcNAc					118:125	O-GlcNAc	118:125	O-GlcNAc	118:125	O-Linked N-acetylglucosamine, or O-GlcNAc, is a dynamic post-translational modification that cycles on and off serine and threonine residues of nucleocytoplasmic and mitochondrial proteins.
26197318	0	13	theme	O-GlcNAc	7:14	arg1	Modification					16:27	NOS1AP O-GlcNAc Modification	0:27	NOS1AP O-GlcNAc Modification	0:27	NOS1AP O-GlcNAc Modification Involved in Neuron Apoptosis Induced by Excitotoxicity.
26197318	6	14	theme	NOS1AP	897:902	arg1	interaction					882:892	the interaction	878:892	the interaction of NOS1AP and neuronal nitric oxide syntheses (nNOS)	878:945	Furthermore, with O-GlcNAc sites of NOS1AP mutated, the interaction of NOS1AP and neuronal nitric oxide syntheses (nNOS) decreases.
26197318	2	15	theme	stress	404:409	arg1	response					411:418	stress response	404:418	stress response	404:418	In addition to cancer and inflammation diseases, O-GlcNAc modification appears to play a critical role during cell apoptosis and stress response, although the precise mechanisms are still not very clear.
26197318	0	16	theme	NOS1AP	0:5	arg1	Modification					16:27	NOS1AP O-GlcNAc Modification	0:27	NOS1AP O-GlcNAc Modification	0:27	NOS1AP O-GlcNAc Modification Involved in Neuron Apoptosis Induced by Excitotoxicity.
26197318	1	17	dep	cycles	178:183	arg1	modification					160:171	a dynamic post-translational modification	131:171	a dynamic post-translational modification that cycles on and off serine and threonine residues of nucleocytoplasmic and mitochondrial proteins	131:272	O-Linked N-acetylglucosamine, or O-GlcNAc, is a dynamic post-translational modification that cycles on and off serine and threonine residues of nucleocytoplasmic and mitochondrial proteins.
26197318	1	17	dep	cycles	178:183	arg1	N-acetylglucosamine					94:112	O-Linked N-acetylglucosamine	85:112	O-Linked N-acetylglucosamine	85:112	O-Linked N-acetylglucosamine, or O-GlcNAc, is a dynamic post-translational modification that cycles on and off serine and threonine residues of nucleocytoplasmic and mitochondrial proteins.
26197318	1	17	dep	cycles	178:183	arg1	O-GlcNAc					118:125	O-GlcNAc	118:125	O-GlcNAc	118:125	O-Linked N-acetylglucosamine, or O-GlcNAc, is a dynamic post-translational modification that cycles on and off serine and threonine residues of nucleocytoplasmic and mitochondrial proteins.
26197318	8	18	theme	protective	1172:1181	arg1	effects					1183:1189	protective effects	1172:1189	protective effects	1172:1189	All these results suggest that O-GlcNAc modification of NOS1AP exerts protective effects during glutamate-induced neuronal apoptosis.
26197318	8	19	theme	glutamate-induced	1198:1214	arg1	apoptosis					1225:1233	glutamate-induced neuronal apoptosis	1198:1233	glutamate-induced neuronal apoptosis	1198:1233	All these results suggest that O-GlcNAc modification of NOS1AP exerts protective effects during glutamate-induced neuronal apoptosis.
26197318	7	20	theme	neuronal	1082:1089	arg1	apoptosis					1091:1099	more severe neuronal apoptosis	1070:1099	more severe neuronal apoptosis	1070:1099	Finally, during glutamate-induced neuronal apoptosis, decreasing the O-GlcNAc modification of NOS1AP results in more severe neuronal apoptosis.
26197318	2	21	theme	O-GlcNAc	324:331	arg1	modification					333:344	O-GlcNAc modification	324:344	O-GlcNAc modification	324:344	In addition to cancer and inflammation diseases, O-GlcNAc modification appears to play a critical role during cell apoptosis and stress response, although the precise mechanisms are still not very clear.
26197318	4	22	theme	O-GlcNAc	726:733	arg1	Ser47					685:689	Ser47	685:689	Ser47	685:689	Mass spectrometry analysis identified Ser47, Ser183, Ser204, Ser269, Ser271 as O-GlcNAc sites.
26197318	4	22	theme	O-GlcNAc	726:733	arg1	sites					735:739	O-GlcNAc sites	726:739	O-GlcNAc sites	726:739	Mass spectrometry analysis identified Ser47, Ser183, Ser204, Ser269, Ser271 as O-GlcNAc sites.
26197318	3	23	theme	important	553:561	arg1	part					563:566	an important part	550:566	an important part	550:566	Here we found that nitric oxide synthase adaptor (NOS1AP), which plays an important part in glutamate-induced neuronal apoptosis, carries the modification of O-GlcNAc.
26197318	2	24	theme	precise	434:440	arg1	clear					472:476	clear	472:476	clear	472:476	In addition to cancer and inflammation diseases, O-GlcNAc modification appears to play a critical role during cell apoptosis and stress response, although the precise mechanisms are still not very clear.
26197318	2	24	theme	precise	434:440	arg1	mechanisms					442:451	the precise mechanisms	430:451	the precise mechanisms	430:451	In addition to cancer and inflammation diseases, O-GlcNAc modification appears to play a critical role during cell apoptosis and stress response, although the precise mechanisms are still not very clear.
26197318	0	25	theme	Neuron	41:46	arg1	Apoptosis					48:56	Neuron Apoptosis	41:56	Neuron Apoptosis Induced by Excitotoxicity	41:82	NOS1AP O-GlcNAc Modification Involved in Neuron Apoptosis Induced by Excitotoxicity.
26197318	4	26	theme	spectrometry	652:663	arg1	analysis					665:672	Mass spectrometry analysis	647:672	Mass spectrometry analysis	647:672	Mass spectrometry analysis identified Ser47, Ser183, Ser204, Ser269, Ser271 as O-GlcNAc sites.
26197318	7	27	theme	severe	1075:1080	arg1	apoptosis					1091:1099	more severe neuronal apoptosis	1070:1099	more severe neuronal apoptosis	1070:1099	Finally, during glutamate-induced neuronal apoptosis, decreasing the O-GlcNAc modification of NOS1AP results in more severe neuronal apoptosis.
26197318	3	28	theme	O-GlcNAc	637:644	arg1	modification					621:632	the modification	617:632	the modification of O-GlcNAc	617:644	Here we found that nitric oxide synthase adaptor (NOS1AP), which plays an important part in glutamate-induced neuronal apoptosis, carries the modification of O-GlcNAc.
26197318	1	29	dep	serine	196:201	arg1	off					192:194	off	192:194	off	192:194	O-Linked N-acetylglucosamine, or O-GlcNAc, is a dynamic post-translational modification that cycles on and off serine and threonine residues of nucleocytoplasmic and mitochondrial proteins.
26197318	1	29	dep	serine	196:201	arg1	residues					217:224	residues	217:224	residues	217:224	O-Linked N-acetylglucosamine, or O-GlcNAc, is a dynamic post-translational modification that cycles on and off serine and threonine residues of nucleocytoplasmic and mitochondrial proteins.
26197318	7	30	theme	O-GlcNAc	1027:1034	arg1	modification					1036:1047	the O-GlcNAc modification	1023:1047	the O-GlcNAc modification of NOS1AP results in more severe neuronal apoptosis	1023:1099	Finally, during glutamate-induced neuronal apoptosis, decreasing the O-GlcNAc modification of NOS1AP results in more severe neuronal apoptosis.
26197318	4	31	theme	Mass	647:650	arg1	analysis					665:672	Mass spectrometry analysis	647:672	Mass spectrometry analysis	647:672	Mass spectrometry analysis identified Ser47, Ser183, Ser204, Ser269, Ser271 as O-GlcNAc sites.
26197318	5	32	theme	glutamate-induced	788:804	arg1	apoptosis					815:823	glutamate-induced neuronal apoptosis	788:823	glutamate-induced neuronal apoptosis	788:823	Higher O-GlcNAc of NOS1AP was detected during glutamate-induced neuronal apoptosis.
26197318	7	33	theme	results	1059:1065	arg1	modification					1036:1047	the O-GlcNAc modification	1023:1047	the O-GlcNAc modification of NOS1AP results in more severe neuronal apoptosis	1023:1099	Finally, during glutamate-induced neuronal apoptosis, decreasing the O-GlcNAc modification of NOS1AP results in more severe neuronal apoptosis.
26197318	6	34	theme	NOS1AP	862:867	arg1	sites					853:857	O-GlcNAc sites	844:857	O-GlcNAc sites of NOS1AP mutated	844:875	Furthermore, with O-GlcNAc sites of NOS1AP mutated, the interaction of NOS1AP and neuronal nitric oxide syntheses (nNOS) decreases.
26197318	6	34	theme	NOS1AP	862:867	arg1	NOS1AP					862:867	NOS1AP	862:867	NOS1AP mutated	862:875	Furthermore, with O-GlcNAc sites of NOS1AP mutated, the interaction of NOS1AP and neuronal nitric oxide syntheses (nNOS) decreases.
26197318	3	35	theme	glutamate-induced	571:587	arg1	apoptosis					598:606	glutamate-induced neuronal apoptosis	571:606	glutamate-induced neuronal apoptosis	571:606	Here we found that nitric oxide synthase adaptor (NOS1AP), which plays an important part in glutamate-induced neuronal apoptosis, carries the modification of O-GlcNAc.
26197318	2	36	theme	critical	364:371	arg1	role					373:376	a critical role	362:376	a critical role	362:376	In addition to cancer and inflammation diseases, O-GlcNAc modification appears to play a critical role during cell apoptosis and stress response, although the precise mechanisms are still not very clear.
26197318	2	37	theme	cell	385:388	arg1	apoptosis					390:398	cell apoptosis	385:398	cell apoptosis	385:398	In addition to cancer and inflammation diseases, O-GlcNAc modification appears to play a critical role during cell apoptosis and stress response, although the precise mechanisms are still not very clear.
26197318	3	38	theme	neuronal	589:596	arg1	apoptosis					598:606	glutamate-induced neuronal apoptosis	571:606	glutamate-induced neuronal apoptosis	571:606	Here we found that nitric oxide synthase adaptor (NOS1AP), which plays an important part in glutamate-induced neuronal apoptosis, carries the modification of O-GlcNAc.
26197318	3	39	theme	oxide	505:509	arg1	synthase					511:518	nitric oxide synthase	498:518	nitric oxide synthase adaptor (NOS1AP)	498:535	Here we found that nitric oxide synthase adaptor (NOS1AP), which plays an important part in glutamate-induced neuronal apoptosis, carries the modification of O-GlcNAc.
26197318	8	40	theme	O-GlcNAc	1133:1140	arg1	modification					1142:1153	O-GlcNAc modification	1133:1153	O-GlcNAc modification of NOS1AP	1133:1163	All these results suggest that O-GlcNAc modification of NOS1AP exerts protective effects during glutamate-induced neuronal apoptosis.
26197318	1	41	theme	nucleocytoplasmic	229:245	arg1	proteins					265:272	nucleocytoplasmic and mitochondrial proteins	229:272	nucleocytoplasmic and mitochondrial proteins	229:272	O-Linked N-acetylglucosamine, or O-GlcNAc, is a dynamic post-translational modification that cycles on and off serine and threonine residues of nucleocytoplasmic and mitochondrial proteins.
26197318	7	42	theme	NOS1AP	1052:1057	arg1	results					1059:1065	NOS1AP results	1052:1065	NOS1AP results	1052:1065	Finally, during glutamate-induced neuronal apoptosis, decreasing the O-GlcNAc modification of NOS1AP results in more severe neuronal apoptosis.
26197318	6	43	theme	O-GlcNAc	844:851	arg1	sites					853:857	O-GlcNAc sites	844:857	O-GlcNAc sites of NOS1AP mutated	844:875	Furthermore, with O-GlcNAc sites of NOS1AP mutated, the interaction of NOS1AP and neuronal nitric oxide syntheses (nNOS) decreases.
26197318	6	43	theme	O-GlcNAc	844:851	arg1	NOS1AP					862:867	NOS1AP	862:867	NOS1AP mutated	862:875	Furthermore, with O-GlcNAc sites of NOS1AP mutated, the interaction of NOS1AP and neuronal nitric oxide syntheses (nNOS) decreases.
26197318	1	44	theme	dynamic	133:139	arg1	modification					160:171	a dynamic post-translational modification	131:171	a dynamic post-translational modification that cycles on and off serine and threonine residues of nucleocytoplasmic and mitochondrial proteins	131:272	O-Linked N-acetylglucosamine, or O-GlcNAc, is a dynamic post-translational modification that cycles on and off serine and threonine residues of nucleocytoplasmic and mitochondrial proteins.
26197318	1	44	theme	dynamic	133:139	arg1	N-acetylglucosamine					94:112	O-Linked N-acetylglucosamine	85:112	O-Linked N-acetylglucosamine	85:112	O-Linked N-acetylglucosamine, or O-GlcNAc, is a dynamic post-translational modification that cycles on and off serine and threonine residues of nucleocytoplasmic and mitochondrial proteins.
26197318	1	44	theme	dynamic	133:139	arg1	O-GlcNAc					118:125	O-GlcNAc	118:125	O-GlcNAc	118:125	O-Linked N-acetylglucosamine, or O-GlcNAc, is a dynamic post-translational modification that cycles on and off serine and threonine residues of nucleocytoplasmic and mitochondrial proteins.
26197318	3	45	contain	carries	609:615	arg1	adaptor					520:526	nitric oxide synthase adaptor	498:526	nitric oxide synthase adaptor (NOS1AP)	498:535	Here we found that nitric oxide synthase adaptor (NOS1AP), which plays an important part in glutamate-induced neuronal apoptosis, carries the modification of O-GlcNAc.
26197318	3	45	contain	carries	609:615	arg2	modification					621:632	the modification	617:632	the modification of O-GlcNAc	617:644	Here we found that nitric oxide synthase adaptor (NOS1AP), which plays an important part in glutamate-induced neuronal apoptosis, carries the modification of O-GlcNAc.
26197318	3	45	contain	carries	609:615	arg1	NOS1AP					529:534	NOS1AP	529:534	NOS1AP	529:534	Here we found that nitric oxide synthase adaptor (NOS1AP), which plays an important part in glutamate-induced neuronal apoptosis, carries the modification of O-GlcNAc.
26197318	8	46	theme	NOS1AP	1158:1163	arg1	modification					1142:1153	O-GlcNAc modification	1133:1153	O-GlcNAc modification of NOS1AP	1133:1163	All these results suggest that O-GlcNAc modification of NOS1AP exerts protective effects during glutamate-induced neuronal apoptosis.
26197318	7	47	from	modification	1036:1047	arg1	apoptosis					1091:1099	more severe neuronal apoptosis	1070:1099	more severe neuronal apoptosis	1070:1099	Finally, during glutamate-induced neuronal apoptosis, decreasing the O-GlcNAc modification of NOS1AP results in more severe neuronal apoptosis.
26197318	1	48	theme	post-translational	141:158	arg1	modification					160:171	a dynamic post-translational modification	131:171	a dynamic post-translational modification that cycles on and off serine and threonine residues of nucleocytoplasmic and mitochondrial proteins	131:272	O-Linked N-acetylglucosamine, or O-GlcNAc, is a dynamic post-translational modification that cycles on and off serine and threonine residues of nucleocytoplasmic and mitochondrial proteins.
26197318	1	48	theme	post-translational	141:158	arg1	N-acetylglucosamine					94:112	O-Linked N-acetylglucosamine	85:112	O-Linked N-acetylglucosamine	85:112	O-Linked N-acetylglucosamine, or O-GlcNAc, is a dynamic post-translational modification that cycles on and off serine and threonine residues of nucleocytoplasmic and mitochondrial proteins.
26197318	1	48	theme	post-translational	141:158	arg1	O-GlcNAc					118:125	O-GlcNAc	118:125	O-GlcNAc	118:125	O-Linked N-acetylglucosamine, or O-GlcNAc, is a dynamic post-translational modification that cycles on and off serine and threonine residues of nucleocytoplasmic and mitochondrial proteins.
26197318	1	49	theme	mitochondrial	251:263	arg1	proteins					265:272	nucleocytoplasmic and mitochondrial proteins	229:272	nucleocytoplasmic and mitochondrial proteins	229:272	O-Linked N-acetylglucosamine, or O-GlcNAc, is a dynamic post-translational modification that cycles on and off serine and threonine residues of nucleocytoplasmic and mitochondrial proteins.
26197318	6	50	dep	NOS1AP	897:902	arg1	nNOS					941:944	nNOS	941:944	nNOS	941:944	Furthermore, with O-GlcNAc sites of NOS1AP mutated, the interaction of NOS1AP and neuronal nitric oxide syntheses (nNOS) decreases.
26197318	6	50	dep	NOS1AP	897:902	arg1	syntheses					930:938	syntheses	930:938	syntheses (nNOS)	930:945	Furthermore, with O-GlcNAc sites of NOS1AP mutated, the interaction of NOS1AP and neuronal nitric oxide syntheses (nNOS) decreases.
26197318	7	51	theme	glutamate-induced	974:990	arg1	apoptosis					1001:1009	glutamate-induced neuronal apoptosis	974:1009	glutamate-induced neuronal apoptosis	974:1009	Finally, during glutamate-induced neuronal apoptosis, decreasing the O-GlcNAc modification of NOS1AP results in more severe neuronal apoptosis.
26197318	2	52	dep	cancer	290:295	arg1	diseases					314:321	diseases	314:321	diseases	314:321	In addition to cancer and inflammation diseases, O-GlcNAc modification appears to play a critical role during cell apoptosis and stress response, although the precise mechanisms are still not very clear.
26197318	2	52	dep	cancer	290:295	arg1	addition					278:285	addition	278:285	addition	278:285	In addition to cancer and inflammation diseases, O-GlcNAc modification appears to play a critical role during cell apoptosis and stress response, although the precise mechanisms are still not very clear.
26197318	1	53	theme	proteins	265:272	arg1	cycles					178:183	cycles	178:183	cycles on and off serine and threonine residues of nucleocytoplasmic and mitochondrial proteins	178:272	O-Linked N-acetylglucosamine, or O-GlcNAc, is a dynamic post-translational modification that cycles on and off serine and threonine residues of nucleocytoplasmic and mitochondrial proteins.
12927779	9	0	theme	inhibitors	1659:1668	arg1	designing					1646:1654	designing	1646:1654	designing	1646:1654	Similarly differences at S2 (Leu-->Phe), S3 (Ser-->Gly), and S4 (Arg-->Asn) subsites are quite apparent and appear to hold the potential for selective designing of inhibitors for possible therapeutic applications.
12927779	12	1	theme	complexation	2389:2400	arg1	rate					2381:2384	the rate	2377:2384	the rate of complexation and binding affinity with proteoglycans	2377:2440	Thus, glycosylation at Ser160 in granzyme M may influence the net charge of the enzyme, resulting in altered substrate binding as compared to granzyme B. Also this modification may influence the rate of complexation and binding affinity with proteoglycans.
12927779	12	2	with	complexation	2389:2400	arg1	proteoglycans					2428:2440	proteoglycans	2428:2440	proteoglycans	2428:2440	Thus, glycosylation at Ser160 in granzyme M may influence the net charge of the enzyme, resulting in altered substrate binding as compared to granzyme B. Also this modification may influence the rate of complexation and binding affinity with proteoglycans.
12927779	3	3	theme	particular	570:579	arg1	h					587:587	h	587:587	h	587:587	In the present communication, we describe the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h)).
12927779	3	3	theme	particular	570:579	arg1	A					585:585	particular Gzm A	570:585	particular Gzm A(h)	570:588	In the present communication, we describe the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h)).
12927779	1	4	contain	containing	275:284	arg2	proteases					296:304	granzyme (proteases)	286:305	granzyme (proteases)	286:305	Cytotoxic lymphocytes (CTLs), the key players of cell mediated immunity, induce apoptosis by engaging death receptors or through exocytosis of cytolytic granules containing granzyme (proteases) and pore-forming protein (perforin).
12927779	1	4	contain	containing	275:284	arg2	perforin					333:340	pore-forming protein (perforin)	311:341	pore-forming protein (perforin)	311:341	Cytotoxic lymphocytes (CTLs), the key players of cell mediated immunity, induce apoptosis by engaging death receptors or through exocytosis of cytolytic granules containing granzyme (proteases) and pore-forming protein (perforin).
12927779	1	4	contain	containing	275:284	arg1	granules					266:273	cytolytic granules	256:273	cytolytic granules containing granzyme (proteases) and pore-forming protein (perforin)	256:341	Cytotoxic lymphocytes (CTLs), the key players of cell mediated immunity, induce apoptosis by engaging death receptors or through exocytosis of cytolytic granules containing granzyme (proteases) and pore-forming protein (perforin).
12927779	11	5	dep	myristoylation	1994:2007	arg1	131					2026:2028	131	2026:2028	131	2026:2028	Additionally the different posttranslational modification sites such as phosphorylation (e.g., in granzyme M Thr101, Ser109), myristoylation (Gly22, 117, and 131), and glycosylation (Ser160) have been identified, as very little is known about the functional significance of these modifications in the granzyme family.
12927779	11	5	dep	myristoylation	1994:2007	arg1	Gly22					2010:2014	Gly22	2010:2014	Gly22	2010:2014	Additionally the different posttranslational modification sites such as phosphorylation (e.g., in granzyme M Thr101, Ser109), myristoylation (Gly22, 117, and 131), and glycosylation (Ser160) have been identified, as very little is known about the functional significance of these modifications in the granzyme family.
12927779	11	5	dep	myristoylation	1994:2007	arg1	117					2017:2019	117	2017:2019	117	2017:2019	Additionally the different posttranslational modification sites such as phosphorylation (e.g., in granzyme M Thr101, Ser109), myristoylation (Gly22, 117, and 131), and glycosylation (Ser160) have been identified, as very little is known about the functional significance of these modifications in the granzyme family.
12927779	2	6	dep	K	446:446	arg1	K					449:449	K	449:449	K(h)	449:452	The crystal structure of granzyme B from human (B(h)) and rat (B(r)), as well as that of pro-granzyme K (K(h)) has been reported recently.
12927779	2	6	dep	K	446:446	arg1	h					451:451	h	451:451	h	451:451	The crystal structure of granzyme B from human (B(h)) and rat (B(r)), as well as that of pro-granzyme K (K(h)) has been reported recently.
12927779	4	7	theme	phylogenetic	777:788	arg1	relationship					790:801	phylogenetic relationship	777:801	phylogenetic relationship	777:801	These models have been used for establishing phylogenetic relationship as well as identifying characteristic features for designing specific inhibitors.
12927779	8	8	theme	S1	1463:1464	arg1	subsite					1466:1472	the S1 subsite	1459:1472	the S1 subsite instead of arginine	1459:1492	For example, in granzyme M(h), valine is present at the S1 subsite instead of arginine.
12927779	8	8	theme	S1	1463:1464	arg1	arginine					1485:1492	arginine	1485:1492	arginine	1485:1492	For example, in granzyme M(h), valine is present at the S1 subsite instead of arginine.
12927779	10	9	theme	clear	1828:1832	arg1	differences					1834:1844	clear differences	1828:1844	clear differences	1828:1844	Furthermore, analysis of the electrostatic surface potential on the shape of granzyme-inhibitor binding groove reveals clear differences at the reactive site.
12927779	6	10	theme	N-terminal	1156:1165	arg1	domain					1167:1172	an N-terminal domain	1153:1172	an N-terminal domain	1153:1172	The predicted 3D homology models show a conserved two similar domain structure, i.e., an N-terminal domain and a C-terminal domain comprising predominantly of beta-sheet structure with a little alpha-helical content.
12927779	3	11	from	C	607:607	arg1	modeling					538:545	the homology modeling	525:545	the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h))	525:729	In the present communication, we describe the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h)).
12927779	5	12	theme	enzyme	1052:1057	arg1	family					1059:1064	this enzyme family	1047:1064	this enzyme family	1047:1064	The paper also highlights key residues at the S1, S2, and S2(') binding subsites in all granzyme, which may be involved in the structure-function relationship of this enzyme family.
12927779	1	13	theme	mediated	167:174	arg1	immunity					176:183	cell mediated immunity	162:183	cell mediated immunity	162:183	Cytotoxic lymphocytes (CTLs), the key players of cell mediated immunity, induce apoptosis by engaging death receptors or through exocytosis of cytolytic granules containing granzyme (proteases) and pore-forming protein (perforin).
12927779	11	14	theme	granzyme	1966:1973	arg1	M					1975:1975	granzyme M	1966:1975	granzyme M Thr101, Ser109	1966:1990	Additionally the different posttranslational modification sites such as phosphorylation (e.g., in granzyme M Thr101, Ser109), myristoylation (Gly22, 117, and 131), and glycosylation (Ser160) have been identified, as very little is known about the functional significance of these modifications in the granzyme family.
12927779	12	15	theme	granzyme	2219:2226	arg1	M					2228:2228	granzyme M	2219:2228	granzyme M	2219:2228	Thus, glycosylation at Ser160 in granzyme M may influence the net charge of the enzyme, resulting in altered substrate binding as compared to granzyme B. Also this modification may influence the rate of complexation and binding affinity with proteoglycans.
12927779	6	16	dep	domain	1167:1172	arg1	i.e.					1147:1150	i.e.	1147:1150	i.e.	1147:1150	The predicted 3D homology models show a conserved two similar domain structure, i.e., an N-terminal domain and a C-terminal domain comprising predominantly of beta-sheet structure with a little alpha-helical content.
12927779	9	17	theme	S2	1520:1521	arg1	subsites					1571:1578	S2 (Leu-->Phe), S3 (Ser-->Gly), and S4 (Arg-->Asn) subsites	1520:1578	S2 (Leu-->Phe), S3 (Ser-->Gly), and S4 (Arg-->Asn) subsites	1520:1578	Similarly differences at S2 (Leu-->Phe), S3 (Ser-->Gly), and S4 (Arg-->Asn) subsites are quite apparent and appear to hold the potential for selective designing of inhibitors for possible therapeutic applications.
12927779	8	18	theme	arginine	1485:1492	arg1	subsite					1466:1472	the S1 subsite	1459:1472	the S1 subsite instead of arginine	1459:1492	For example, in granzyme M(h), valine is present at the S1 subsite instead of arginine.
12927779	8	18	theme	arginine	1485:1492	arg1	arginine					1485:1492	arginine	1485:1492	arginine	1485:1492	For example, in granzyme M(h), valine is present at the S1 subsite instead of arginine.
12927779	7	19	located	observed	1316:1323	arg2	Micro-heterogeneities					1284:1304	Micro-heterogeneities	1284:1304	Micro-heterogeneities	1284:1304	Micro-heterogeneities have been observed in the vicinity of the active site in all granzymes as compared to granzyme B(h).
12927779	7	19	located	observed	1316:1323	arg1	vicinity					1332:1339	the vicinity	1328:1339	the vicinity of the active site in all granzymes	1328:1375	Micro-heterogeneities have been observed in the vicinity of the active site in all granzymes as compared to granzyme B(h).
12927779	10	20	from	potential	1760:1768	arg1	shape					1777:1781	the shape	1773:1781	the shape of granzyme-inhibitor binding groove	1773:1818	Furthermore, analysis of the electrostatic surface potential on the shape of granzyme-inhibitor binding groove reveals clear differences at the reactive site.
12927779	0	21	from	studies	64:70	arg1	family					84:89	granzyme family	75:89	granzyme family by homology modeling	75:110	Bioinformatics of granzymes: sequence comparison and structural studies on granzyme family by homology modeling.
12927779	3	22	from	family	559:564	arg1	B					597:597	B	597:597	B(m)	597:600	In the present communication, we describe the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h)).
12927779	3	22	from	family	559:564	arg1	C					607:607	C	607:607	C(m)	607:610	In the present communication, we describe the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h)).
12927779	3	22	from	family	559:564	arg1	m					609:609	m	609:609	m	609:609	In the present communication, we describe the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h)).
12927779	3	22	from	family	559:564	arg1	M					591:591	M	591:591	M(h)	591:594	In the present communication, we describe the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h)).
12927779	3	22	from	family	559:564	arg1	m					599:599	m	599:599	m	599:599	In the present communication, we describe the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h)).
12927779	3	22	from	family	559:564	arg1	h					593:593	h	593:593	h	593:593	In the present communication, we describe the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h)).
12927779	3	22	from	family	559:564	arg1	A					585:585	particular Gzm A	570:585	particular Gzm A(h)	570:588	In the present communication, we describe the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h)).
12927779	3	22	from	family	559:564	arg1	h					587:587	h	587:587	h	587:587	In the present communication, we describe the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h)).
12927779	3	22	from	family	559:564	arg1	human					617:621	human	617:621	human	617:621	In the present communication, we describe the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h)).
12927779	3	22	from	family	559:564	arg1	mouse					627:631	mouse	627:631	mouse	627:631	In the present communication, we describe the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h)).
12927779	7	23	from	vicinity	1332:1339	arg1	granzymes					1367:1375	all granzymes	1363:1375	all granzymes	1363:1375	Micro-heterogeneities have been observed in the vicinity of the active site in all granzymes as compared to granzyme B(h).
12927779	4	24	theme	specific	864:871	arg1	inhibitors					873:882	specific inhibitors	864:882	specific inhibitors	864:882	These models have been used for establishing phylogenetic relationship as well as identifying characteristic features for designing specific inhibitors.
12927779	13	25	theme	associations	2530:2541	arg1	understanding					2502:2514	the basic understanding	2492:2514	the basic understanding of functional associations of the granzymes with other molecules	2492:2579	These studies are expected to contribute towards the basic understanding of functional associations of the granzymes with other molecules and their possible role in apoptosis.
12927779	13	25	theme	associations	2530:2541	arg1	role					2600:2603	their possible role	2585:2603	their possible role in apoptosis	2585:2616	These studies are expected to contribute towards the basic understanding of functional associations of the granzymes with other molecules and their possible role in apoptosis.
12927779	10	26	theme	surface	1752:1758	arg1	potential					1760:1768	the electrostatic surface potential	1734:1768	the electrostatic surface potential on the shape of granzyme-inhibitor binding groove	1734:1818	Furthermore, analysis of the electrostatic surface potential on the shape of granzyme-inhibitor binding groove reveals clear differences at the reactive site.
12927779	1	27	theme	pore-forming	311:322	arg1	perforin					333:340	pore-forming protein (perforin)	311:341	pore-forming protein (perforin)	311:341	Cytotoxic lymphocytes (CTLs), the key players of cell mediated immunity, induce apoptosis by engaging death receptors or through exocytosis of cytolytic granules containing granzyme (proteases) and pore-forming protein (perforin).
12927779	12	28	dep	influence	2234:2242	arg1	influence					2367:2375	influence	2367:2375	may influence the rate of complexation and binding affinity with proteoglycans	2363:2440	Thus, glycosylation at Ser160 in granzyme M may influence the net charge of the enzyme, resulting in altered substrate binding as compared to granzyme B. Also this modification may influence the rate of complexation and binding affinity with proteoglycans.
12927779	6	29	theme	C-terminal	1180:1189	arg1	domain					1191:1196	a C-terminal domain	1178:1196	a C-terminal domain comprising predominantly of beta-sheet structure with a little alpha-helical content	1178:1281	The predicted 3D homology models show a conserved two similar domain structure, i.e., an N-terminal domain and a C-terminal domain comprising predominantly of beta-sheet structure with a little alpha-helical content.
12927779	4	30	theme	characteristic	826:839	arg1	features					841:848	characteristic features	826:848	characteristic features	826:848	These models have been used for establishing phylogenetic relationship as well as identifying characteristic features for designing specific inhibitors.
12927779	5	31	theme	S1	931:932	arg1	subsites					957:964	the S1, S2, and S2(') binding subsites	927:964	the S1, S2, and S2(') binding subsites in all granzyme, which may be involved in the structure-function relationship of this enzyme family	927:1064	The paper also highlights key residues at the S1, S2, and S2(') binding subsites in all granzyme, which may be involved in the structure-function relationship of this enzyme family.
12927779	0	32	theme	granzyme	75:82	arg1	family					84:89	granzyme family	75:89	granzyme family by homology modeling	75:110	Bioinformatics of granzymes: sequence comparison and structural studies on granzyme family by homology modeling.
12927779	8	33	theme	granzyme	1423:1430	arg1	h					1434:1434	granzyme M(h)	1423:1435	granzyme M(h)	1423:1435	For example, in granzyme M(h), valine is present at the S1 subsite instead of arginine.
12927779	1	34	theme	key	147:149	arg1	players					151:157	the key players	143:157	the key players of cell mediated immunity	143:183	Cytotoxic lymphocytes (CTLs), the key players of cell mediated immunity, induce apoptosis by engaging death receptors or through exocytosis of cytolytic granules containing granzyme (proteases) and pore-forming protein (perforin).
12927779	1	34	theme	key	147:149	arg1	lymphocytes					123:133	Cytotoxic lymphocytes	113:133	Cytotoxic lymphocytes (CTLs)	113:140	Cytotoxic lymphocytes (CTLs), the key players of cell mediated immunity, induce apoptosis by engaging death receptors or through exocytosis of cytolytic granules containing granzyme (proteases) and pore-forming protein (perforin).
12927779	7	35	theme	site	1355:1358	arg1	vicinity					1332:1339	the vicinity	1328:1339	the vicinity of the active site in all granzymes	1328:1375	Micro-heterogeneities have been observed in the vicinity of the active site in all granzymes as compared to granzyme B(h).
12927779	13	36	theme	basic	2496:2500	arg1	understanding					2502:2514	the basic understanding	2492:2514	the basic understanding of functional associations of the granzymes with other molecules	2492:2579	These studies are expected to contribute towards the basic understanding of functional associations of the granzymes with other molecules and their possible role in apoptosis.
12927779	5	37	theme	S2	935:936	arg1	subsites					957:964	the S1, S2, and S2(') binding subsites	927:964	the S1, S2, and S2(') binding subsites in all granzyme, which may be involved in the structure-function relationship of this enzyme family	927:1064	The paper also highlights key residues at the S1, S2, and S2(') binding subsites in all granzyme, which may be involved in the structure-function relationship of this enzyme family.
12927779	12	38	with	affinity	2414:2421	arg1	proteoglycans					2428:2440	proteoglycans	2428:2440	proteoglycans	2428:2440	Thus, glycosylation at Ser160 in granzyme M may influence the net charge of the enzyme, resulting in altered substrate binding as compared to granzyme B. Also this modification may influence the rate of complexation and binding affinity with proteoglycans.
12927779	3	39	from	A	585:585	arg1	modeling					538:545	the homology modeling	525:545	the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h))	525:729	In the present communication, we describe the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h)).
12927779	2	40	theme	B	378:378	arg1	structure					356:364	The crystal structure	344:364	The crystal structure of granzyme B from human (B(h)) and rat (B(r)), as well as that of pro-granzyme K (K(h))	344:453	The crystal structure of granzyme B from human (B(h)) and rat (B(r)), as well as that of pro-granzyme K (K(h)) has been reported recently.
12927779	6	41	theme	alpha-helical	1261:1273	arg1	content					1275:1281	a little alpha-helical content	1252:1281	a little alpha-helical content	1252:1281	The predicted 3D homology models show a conserved two similar domain structure, i.e., an N-terminal domain and a C-terminal domain comprising predominantly of beta-sheet structure with a little alpha-helical content.
12927779	8	42	located	present	1448:1454	arg2	valine					1438:1443	valine	1438:1443	valine	1438:1443	For example, in granzyme M(h), valine is present at the S1 subsite instead of arginine.
12927779	8	42	located	present	1448:1454	arg1	subsite					1466:1472	the S1 subsite	1459:1472	the S1 subsite instead of arginine	1459:1492	For example, in granzyme M(h), valine is present at the S1 subsite instead of arginine.
12927779	8	42	located	present	1448:1454	arg1	arginine					1485:1492	arginine	1485:1492	arginine	1485:1492	For example, in granzyme M(h), valine is present at the S1 subsite instead of arginine.
12927779	8	42	located	present	1448:1454	arg1	h					1434:1434	granzyme M(h)	1423:1435	granzyme M(h)	1423:1435	For example, in granzyme M(h), valine is present at the S1 subsite instead of arginine.
12927779	10	43	theme	groove	1813:1818	arg1	shape					1777:1781	the shape	1773:1781	the shape of granzyme-inhibitor binding groove	1773:1818	Furthermore, analysis of the electrostatic surface potential on the shape of granzyme-inhibitor binding groove reveals clear differences at the reactive site.
12927779	9	44	theme	therapeutic	1683:1693	arg1	applications					1695:1706	possible therapeutic applications	1674:1706	possible therapeutic applications	1674:1706	Similarly differences at S2 (Leu-->Phe), S3 (Ser-->Gly), and S4 (Arg-->Asn) subsites are quite apparent and appear to hold the potential for selective designing of inhibitors for possible therapeutic applications.
12927779	6	45	theme	predicted	1071:1079	arg1	models					1093:1098	The predicted 3D homology models	1067:1098	The predicted 3D homology models	1067:1098	The predicted 3D homology models show a conserved two similar domain structure, i.e., an N-terminal domain and a C-terminal domain comprising predominantly of beta-sheet structure with a little alpha-helical content.
12927779	1	46	theme	cytolytic	256:264	arg1	granules					266:273	cytolytic granules	256:273	cytolytic granules containing granzyme (proteases) and pore-forming protein (perforin)	256:341	Cytotoxic lymphocytes (CTLs), the key players of cell mediated immunity, induce apoptosis by engaging death receptors or through exocytosis of cytolytic granules containing granzyme (proteases) and pore-forming protein (perforin).
12927779	10	47	theme	granzyme-inhibitor	1786:1803	arg1	groove					1813:1818	granzyme-inhibitor binding groove	1786:1818	granzyme-inhibitor binding groove	1786:1818	Furthermore, analysis of the electrostatic surface potential on the shape of granzyme-inhibitor binding groove reveals clear differences at the reactive site.
12927779	2	48	theme	B	392:392	arg1	human					385:389	human	385:389	human	385:389	The crystal structure of granzyme B from human (B(h)) and rat (B(r)), as well as that of pro-granzyme K (K(h)) has been reported recently.
12927779	2	48	theme	B	392:392	arg1	h					394:394	B(h)	392:395	B(h)	392:395	The crystal structure of granzyme B from human (B(h)) and rat (B(r)), as well as that of pro-granzyme K (K(h)) has been reported recently.
12927779	0	49	theme	granzymes	18:26	arg1	Bioinformatics					0:13	Bioinformatics	0:13	Bioinformatics of granzymes: sequence comparison and structural studies on granzyme family by homology modeling.	0:111	Bioinformatics of granzymes: sequence comparison and structural studies on granzyme family by homology modeling.
12927779	3	50	theme	crystal	647:653	arg1	coordinates					666:676	the crystal structural coordinates	643:676	the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h))	643:729	In the present communication, we describe the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h)).
12927779	2	51	theme	B	407:407	arg1	rat					402:404	rat	402:404	rat (B(r))	402:411	The crystal structure of granzyme B from human (B(h)) and rat (B(r)), as well as that of pro-granzyme K (K(h)) has been reported recently.
12927779	2	51	theme	B	407:407	arg1	r					409:409	B(r)	407:410	B(r)	407:410	The crystal structure of granzyme B from human (B(h)) and rat (B(r)), as well as that of pro-granzyme K (K(h)) has been reported recently.
12927779	11	52	theme	modifications	2148:2160	arg1	significance					2126:2137	the functional significance	2111:2137	the functional significance of these modifications in the granzyme family	2111:2183	Additionally the different posttranslational modification sites such as phosphorylation (e.g., in granzyme M Thr101, Ser109), myristoylation (Gly22, 117, and 131), and glycosylation (Ser160) have been identified, as very little is known about the functional significance of these modifications in the granzyme family.
12927779	0	53	theme	sequence	29:36	arg1	comparison					38:47	sequence comparison	29:47	sequence comparison	29:47	Bioinformatics of granzymes: sequence comparison and structural studies on granzyme family by homology modeling.
12927779	12	54	from	Ser160	2209:2214	arg1	glycosylation					2192:2204	glycosylation	2192:2204	glycosylation at Ser160 in granzyme M	2192:2228	Thus, glycosylation at Ser160 in granzyme M may influence the net charge of the enzyme, resulting in altered substrate binding as compared to granzyme B. Also this modification may influence the rate of complexation and binding affinity with proteoglycans.
12927779	12	55	theme	enzyme	2266:2271	arg1	charge					2252:2257	the net charge	2244:2257	the net charge	2244:2257	Thus, glycosylation at Ser160 in granzyme M may influence the net charge of the enzyme, resulting in altered substrate binding as compared to granzyme B. Also this modification may influence the rate of complexation and binding affinity with proteoglycans.
12927779	3	56	theme	granzyme	690:697	arg1	K					699:699	granzyme K	690:699	granzyme K (K(h))	690:706	In the present communication, we describe the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h)).
12927779	12	57	theme	substrate	2295:2303	arg1	binding					2305:2311	altered substrate binding	2287:2311	altered substrate binding	2287:2311	Thus, glycosylation at Ser160 in granzyme M may influence the net charge of the enzyme, resulting in altered substrate binding as compared to granzyme B. Also this modification may influence the rate of complexation and binding affinity with proteoglycans.
12927779	3	58	theme	present	490:496	arg1	communication					498:510	the present communication	486:510	the present communication	486:510	In the present communication, we describe the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h)).
12927779	9	59	theme	possible	1674:1681	arg1	applications					1695:1706	possible therapeutic applications	1674:1706	possible therapeutic applications	1674:1706	Similarly differences at S2 (Leu-->Phe), S3 (Ser-->Gly), and S4 (Arg-->Asn) subsites are quite apparent and appear to hold the potential for selective designing of inhibitors for possible therapeutic applications.
12927779	12	60	from	glycosylation	2192:2204	arg1	M					2228:2228	granzyme M	2219:2228	granzyme M	2219:2228	Thus, glycosylation at Ser160 in granzyme M may influence the net charge of the enzyme, resulting in altered substrate binding as compared to granzyme B. Also this modification may influence the rate of complexation and binding affinity with proteoglycans.
12927779	13	61	from	role	2600:2603	arg1	apoptosis					2608:2616	apoptosis	2608:2616	apoptosis	2608:2616	These studies are expected to contribute towards the basic understanding of functional associations of the granzymes with other molecules and their possible role in apoptosis.
12927779	3	62	theme	trypsin	681:687	arg1	coordinates					666:676	the crystal structural coordinates	643:676	the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h))	643:729	In the present communication, we describe the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h)).
12927779	11	63	theme	posttranslational	1895:1911	arg1	modification					1913:1924	posttranslational modification	1895:1924	the different posttranslational modification sites such as phosphorylation (e.g., in granzyme M Thr101, Ser109), myristoylation (Gly22, 117, and 131), and glycosylation (Ser160)	1881:2057	Additionally the different posttranslational modification sites such as phosphorylation (e.g., in granzyme M Thr101, Ser109), myristoylation (Gly22, 117, and 131), and glycosylation (Ser160) have been identified, as very little is known about the functional significance of these modifications in the granzyme family.
12927779	3	64	from	B	597:597	arg1	modeling					538:545	the homology modeling	525:545	the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h))	525:729	In the present communication, we describe the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h)).
12927779	3	65	theme	homology	529:536	arg1	modeling					538:545	the homology modeling	525:545	the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h))	525:729	In the present communication, we describe the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h)).
12927779	6	66	theme	similar	1121:1127	arg1	structure					1136:1144	a conserved two similar domain structure	1105:1144	a conserved two similar domain structure	1105:1144	The predicted 3D homology models show a conserved two similar domain structure, i.e., an N-terminal domain and a C-terminal domain comprising predominantly of beta-sheet structure with a little alpha-helical content.
12927779	2	67	from	human	385:389	arg1	structure					356:364	The crystal structure	344:364	The crystal structure of granzyme B from human (B(h)) and rat (B(r)), as well as that of pro-granzyme K (K(h))	344:453	The crystal structure of granzyme B from human (B(h)) and rat (B(r)), as well as that of pro-granzyme K (K(h)) has been reported recently.
12927779	2	67	from	human	385:389	arg1	B					378:378	granzyme B	369:378	granzyme B from human (B(h)) and rat (B(r))	369:411	The crystal structure of granzyme B from human (B(h)) and rat (B(r)), as well as that of pro-granzyme K (K(h)) has been reported recently.
12927779	2	68	theme	crystal	348:354	arg1	structure					356:364	The crystal structure	344:364	The crystal structure of granzyme B from human (B(h)) and rat (B(r)), as well as that of pro-granzyme K (K(h))	344:453	The crystal structure of granzyme B from human (B(h)) and rat (B(r)), as well as that of pro-granzyme K (K(h)) has been reported recently.
12927779	6	69	theme	conserved	1107:1115	arg1	structure					1136:1144	a conserved two similar domain structure	1105:1144	a conserved two similar domain structure	1105:1144	The predicted 3D homology models show a conserved two similar domain structure, i.e., an N-terminal domain and a C-terminal domain comprising predominantly of beta-sheet structure with a little alpha-helical content.
12927779	1	70	theme	death	215:219	arg1	receptors					221:229	death receptors	215:229	death receptors	215:229	Cytotoxic lymphocytes (CTLs), the key players of cell mediated immunity, induce apoptosis by engaging death receptors or through exocytosis of cytolytic granules containing granzyme (proteases) and pore-forming protein (perforin).
12927779	4	71	used	used	755:758	arg2	models					738:743	These models	732:743	These models	732:743	These models have been used for establishing phylogenetic relationship as well as identifying characteristic features for designing specific inhibitors.
12927779	3	72	theme	family	559:564	arg1	modeling					538:545	the homology modeling	525:545	the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h))	525:729	In the present communication, we describe the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h)).
12927779	3	73	dep	B	722:722	arg1	h					727:727	h	727:727	h	727:727	In the present communication, we describe the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h)).
12927779	3	73	dep	B	722:722	arg1	B					725:725	B	725:725	B(h)	725:728	In the present communication, we describe the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h)).
12927779	6	74	theme	homology	1084:1091	arg1	models					1093:1098	The predicted 3D homology models	1067:1098	The predicted 3D homology models	1067:1098	The predicted 3D homology models show a conserved two similar domain structure, i.e., an N-terminal domain and a C-terminal domain comprising predominantly of beta-sheet structure with a little alpha-helical content.
12927779	2	75	from	structure	356:364	arg1	rat					402:404	rat	402:404	rat (B(r))	402:411	The crystal structure of granzyme B from human (B(h)) and rat (B(r)), as well as that of pro-granzyme K (K(h)) has been reported recently.
12927779	2	75	from	structure	356:364	arg1	r					409:409	B(r)	407:410	B(r)	407:410	The crystal structure of granzyme B from human (B(h)) and rat (B(r)), as well as that of pro-granzyme K (K(h)) has been reported recently.
12927779	2	75	from	structure	356:364	arg1	h					394:394	B(h)	392:395	B(h)	392:395	The crystal structure of granzyme B from human (B(h)) and rat (B(r)), as well as that of pro-granzyme K (K(h)) has been reported recently.
12927779	2	75	from	structure	356:364	arg1	human					385:389	human	385:389	human	385:389	The crystal structure of granzyme B from human (B(h)) and rat (B(r)), as well as that of pro-granzyme K (K(h)) has been reported recently.
12927779	3	76	from	human	617:621	arg1	B					597:597	B	597:597	B(m)	597:600	In the present communication, we describe the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h)).
12927779	3	76	from	human	617:621	arg1	C					607:607	C	607:607	C(m)	607:610	In the present communication, we describe the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h)).
12927779	3	76	from	human	617:621	arg1	m					609:609	m	609:609	m	609:609	In the present communication, we describe the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h)).
12927779	3	76	from	human	617:621	arg1	M					591:591	M	591:591	M(h)	591:594	In the present communication, we describe the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h)).
12927779	3	76	from	human	617:621	arg1	m					599:599	m	599:599	m	599:599	In the present communication, we describe the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h)).
12927779	3	76	from	human	617:621	arg1	h					593:593	h	593:593	h	593:593	In the present communication, we describe the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h)).
12927779	3	76	from	human	617:621	arg1	A					585:585	particular Gzm A	570:585	particular Gzm A(h)	570:588	In the present communication, we describe the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h)).
12927779	3	76	from	human	617:621	arg1	family					559:564	granzyme family	550:564	granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse)	550:632	In the present communication, we describe the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h)).
12927779	3	76	from	human	617:621	arg1	h					587:587	h	587:587	h	587:587	In the present communication, we describe the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h)).
12927779	3	76	from	human	617:621	arg1	mouse					627:631	mouse	627:631	mouse	627:631	In the present communication, we describe the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h)).
12927779	11	77	theme	functional	2115:2124	arg1	significance					2126:2137	the functional significance	2111:2137	the functional significance of these modifications in the granzyme family	2111:2183	Additionally the different posttranslational modification sites such as phosphorylation (e.g., in granzyme M Thr101, Ser109), myristoylation (Gly22, 117, and 131), and glycosylation (Ser160) have been identified, as very little is known about the functional significance of these modifications in the granzyme family.
12927779	3	78	theme	Gzm	581:583	arg1	h					587:587	h	587:587	h	587:587	In the present communication, we describe the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h)).
12927779	3	78	theme	Gzm	581:583	arg1	A					585:585	particular Gzm A	570:585	particular Gzm A(h)	570:588	In the present communication, we describe the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h)).
12927779	11	79	dep	M	1975:1975	arg1	Ser109					1985:1990	Ser109	1985:1990	Ser109	1985:1990	Additionally the different posttranslational modification sites such as phosphorylation (e.g., in granzyme M Thr101, Ser109), myristoylation (Gly22, 117, and 131), and glycosylation (Ser160) have been identified, as very little is known about the functional significance of these modifications in the granzyme family.
12927779	3	80	from	mouse	627:631	arg1	modeling					538:545	the homology modeling	525:545	the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h))	525:729	In the present communication, we describe the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h)).
12927779	8	81	attach	present	1448:1454	arg2	valine					1438:1443	valine	1438:1443	valine	1438:1443	For example, in granzyme M(h), valine is present at the S1 subsite instead of arginine.
12927779	8	81	attach	present	1448:1454	arg1	subsite					1466:1472	the S1 subsite	1459:1472	the S1 subsite instead of arginine	1459:1492	For example, in granzyme M(h), valine is present at the S1 subsite instead of arginine.
12927779	8	81	attach	present	1448:1454	arg1	arginine					1485:1492	arginine	1485:1492	arginine	1485:1492	For example, in granzyme M(h), valine is present at the S1 subsite instead of arginine.
12927779	8	81	attach	present	1448:1454	arg1	h					1434:1434	granzyme M(h)	1423:1435	granzyme M(h)	1423:1435	For example, in granzyme M(h), valine is present at the S1 subsite instead of arginine.
12927779	3	82	dep	K	699:699	arg1	K					702:702	K	702:702	K(h)	702:705	In the present communication, we describe the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h)).
12927779	3	82	dep	K	699:699	arg1	h					704:704	h	704:704	h	704:704	In the present communication, we describe the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h)).
12927779	1	83	theme	cell	162:165	arg1	immunity					176:183	cell mediated immunity	162:183	cell mediated immunity	162:183	Cytotoxic lymphocytes (CTLs), the key players of cell mediated immunity, induce apoptosis by engaging death receptors or through exocytosis of cytolytic granules containing granzyme (proteases) and pore-forming protein (perforin).
12927779	10	84	theme	reactive	1853:1860	arg1	site					1862:1865	the reactive site	1849:1865	the reactive site	1849:1865	Furthermore, analysis of the electrostatic surface potential on the shape of granzyme-inhibitor binding groove reveals clear differences at the reactive site.
12927779	3	85	theme	granzyme	713:720	arg1	B					722:722	granzyme B	713:722	granzyme B (B(h))	713:729	In the present communication, we describe the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h)).
12927779	10	86	from	analysis	1722:1729	arg1	shape					1777:1781	the shape	1773:1781	the shape of granzyme-inhibitor binding groove	1773:1818	Furthermore, analysis of the electrostatic surface potential on the shape of granzyme-inhibitor binding groove reveals clear differences at the reactive site.
12927779	12	87	theme	net	2248:2250	arg1	charge					2252:2257	the net charge	2244:2257	the net charge	2244:2257	Thus, glycosylation at Ser160 in granzyme M may influence the net charge of the enzyme, resulting in altered substrate binding as compared to granzyme B. Also this modification may influence the rate of complexation and binding affinity with proteoglycans.
12927779	13	88	from	understanding	2502:2514	arg1	apoptosis					2608:2616	apoptosis	2608:2616	apoptosis	2608:2616	These studies are expected to contribute towards the basic understanding of functional associations of the granzymes with other molecules and their possible role in apoptosis.
12927779	5	89	theme	family	1059:1064	arg1	relationship					1031:1042	the structure-function relationship	1008:1042	the structure-function relationship of this enzyme family	1008:1064	The paper also highlights key residues at the S1, S2, and S2(') binding subsites in all granzyme, which may be involved in the structure-function relationship of this enzyme family.
12927779	12	90	gly	glycosylation	2192:2204	arg2	Ser160					2209:2214	Ser160	2209:2214	Ser160	2209:2214	Thus, glycosylation at Ser160 in granzyme M may influence the net charge of the enzyme, resulting in altered substrate binding as compared to granzyme B. Also this modification may influence the rate of complexation and binding affinity with proteoglycans.
12927779	12	90	gly	glycosylation	2192:2204	arg1	Ser160					2209:2214	Ser160	2209:2214	Ser160	2209:2214	Thus, glycosylation at Ser160 in granzyme M may influence the net charge of the enzyme, resulting in altered substrate binding as compared to granzyme B. Also this modification may influence the rate of complexation and binding affinity with proteoglycans.
12927779	12	90	gly	glycosylation	2192:2204	arg1	M					2228:2228	granzyme M	2219:2228	granzyme M	2219:2228	Thus, glycosylation at Ser160 in granzyme M may influence the net charge of the enzyme, resulting in altered substrate binding as compared to granzyme B. Also this modification may influence the rate of complexation and binding affinity with proteoglycans.
12927779	1	91	theme	immunity	176:183	arg1	players					151:157	the key players	143:157	the key players of cell mediated immunity	143:183	Cytotoxic lymphocytes (CTLs), the key players of cell mediated immunity, induce apoptosis by engaging death receptors or through exocytosis of cytolytic granules containing granzyme (proteases) and pore-forming protein (perforin).
12927779	1	91	theme	immunity	176:183	arg1	lymphocytes					123:133	Cytotoxic lymphocytes	113:133	Cytotoxic lymphocytes (CTLs)	113:140	Cytotoxic lymphocytes (CTLs), the key players of cell mediated immunity, induce apoptosis by engaging death receptors or through exocytosis of cytolytic granules containing granzyme (proteases) and pore-forming protein (perforin).
12927779	13	92	theme	possible	2591:2598	arg1	role					2600:2603	their possible role	2585:2603	their possible role in apoptosis	2585:2616	These studies are expected to contribute towards the basic understanding of functional associations of the granzymes with other molecules and their possible role in apoptosis.
12927779	2	93	theme	pro-granzyme	433:444	arg1	K					446:446	pro-granzyme K	433:446	pro-granzyme K (K(h))	433:453	The crystal structure of granzyme B from human (B(h)) and rat (B(r)), as well as that of pro-granzyme K (K(h)) has been reported recently.
12927779	3	94	from	modeling	538:545	arg1	B					597:597	B	597:597	B(m)	597:600	In the present communication, we describe the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h)).
12927779	3	94	from	modeling	538:545	arg1	C					607:607	C	607:607	C(m)	607:610	In the present communication, we describe the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h)).
12927779	3	94	from	modeling	538:545	arg1	m					609:609	m	609:609	m	609:609	In the present communication, we describe the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h)).
12927779	3	94	from	modeling	538:545	arg1	M					591:591	M	591:591	M(h)	591:594	In the present communication, we describe the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h)).
12927779	3	94	from	modeling	538:545	arg1	m					599:599	m	599:599	m	599:599	In the present communication, we describe the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h)).
12927779	3	94	from	modeling	538:545	arg1	h					593:593	h	593:593	h	593:593	In the present communication, we describe the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h)).
12927779	3	94	from	modeling	538:545	arg1	A					585:585	particular Gzm A	570:585	particular Gzm A(h)	570:588	In the present communication, we describe the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h)).
12927779	3	94	from	modeling	538:545	arg1	h					587:587	h	587:587	h	587:587	In the present communication, we describe the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h)).
12927779	3	94	from	modeling	538:545	arg1	mouse					627:631	mouse	627:631	mouse	627:631	In the present communication, we describe the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h)).
12927779	13	95	theme	granzymes	2550:2558	arg1	associations					2530:2541	functional associations	2519:2541	functional associations of the granzymes with other molecules	2519:2579	These studies are expected to contribute towards the basic understanding of functional associations of the granzymes with other molecules and their possible role in apoptosis.
12927779	2	96	theme	that	425:428	arg1	structure					356:364	The crystal structure	344:364	The crystal structure of granzyme B from human (B(h)) and rat (B(r)), as well as that of pro-granzyme K (K(h))	344:453	The crystal structure of granzyme B from human (B(h)) and rat (B(r)), as well as that of pro-granzyme K (K(h)) has been reported recently.
12927779	5	97	from	subsites	957:964	arg1	granzyme					973:980	all granzyme	969:980	all granzyme	969:980	The paper also highlights key residues at the S1, S2, and S2(') binding subsites in all granzyme, which may be involved in the structure-function relationship of this enzyme family.
12927779	5	97	from	subsites	957:964	arg1	residues					915:922	key residues	911:922	key residues at the S1, S2, and S2(') binding subsites in all granzyme, which may be involved in the structure-function relationship of this enzyme family	911:1064	The paper also highlights key residues at the S1, S2, and S2(') binding subsites in all granzyme, which may be involved in the structure-function relationship of this enzyme family.
12927779	6	98	theme	beta-sheet	1226:1235	arg1	structure					1237:1245	beta-sheet structure	1226:1245	beta-sheet structure with a little alpha-helical content	1226:1281	The predicted 3D homology models show a conserved two similar domain structure, i.e., an N-terminal domain and a C-terminal domain comprising predominantly of beta-sheet structure with a little alpha-helical content.
12927779	1	99	theme	Cytotoxic	113:121	arg1	players					151:157	the key players	143:157	the key players of cell mediated immunity	143:183	Cytotoxic lymphocytes (CTLs), the key players of cell mediated immunity, induce apoptosis by engaging death receptors or through exocytosis of cytolytic granules containing granzyme (proteases) and pore-forming protein (perforin).
12927779	1	99	theme	Cytotoxic	113:121	arg1	CTLs					136:139	CTLs	136:139	CTLs	136:139	Cytotoxic lymphocytes (CTLs), the key players of cell mediated immunity, induce apoptosis by engaging death receptors or through exocytosis of cytolytic granules containing granzyme (proteases) and pore-forming protein (perforin).
12927779	1	99	theme	Cytotoxic	113:121	arg1	lymphocytes					123:133	Cytotoxic lymphocytes	113:133	Cytotoxic lymphocytes (CTLs)	113:140	Cytotoxic lymphocytes (CTLs), the key players of cell mediated immunity, induce apoptosis by engaging death receptors or through exocytosis of cytolytic granules containing granzyme (proteases) and pore-forming protein (perforin).
12927779	13	100	theme	other	2565:2569	arg1	molecules					2571:2579	other molecules	2565:2579	other molecules	2565:2579	These studies are expected to contribute towards the basic understanding of functional associations of the granzymes with other molecules and their possible role in apoptosis.
12927779	9	101	theme	S3	1536:1537	arg1	subsites					1571:1578	S2 (Leu-->Phe), S3 (Ser-->Gly), and S4 (Arg-->Asn) subsites	1520:1578	S2 (Leu-->Phe), S3 (Ser-->Gly), and S4 (Arg-->Asn) subsites	1520:1578	Similarly differences at S2 (Leu-->Phe), S3 (Ser-->Gly), and S4 (Arg-->Asn) subsites are quite apparent and appear to hold the potential for selective designing of inhibitors for possible therapeutic applications.
12927779	3	102	theme	B	722:722	arg1	coordinates					666:676	the crystal structural coordinates	643:676	the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h))	643:729	In the present communication, we describe the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h)).
12927779	5	103	dep	S1	931:932	arg1	'					946:946	'	946:946	'	946:946	The paper also highlights key residues at the S1, S2, and S2(') binding subsites in all granzyme, which may be involved in the structure-function relationship of this enzyme family.
12927779	7	104	theme	granzyme	1392:1399	arg1	h					1403:1403	h	1403:1403	h	1403:1403	Micro-heterogeneities have been observed in the vicinity of the active site in all granzymes as compared to granzyme B(h).
12927779	7	104	theme	granzyme	1392:1399	arg1	B					1401:1401	granzyme B	1392:1401	granzyme B(h)	1392:1404	Micro-heterogeneities have been observed in the vicinity of the active site in all granzymes as compared to granzyme B(h).
12927779	13	105	theme	functional	2519:2528	arg1	associations					2530:2541	functional associations	2519:2541	functional associations of the granzymes with other molecules	2519:2579	These studies are expected to contribute towards the basic understanding of functional associations of the granzymes with other molecules and their possible role in apoptosis.
12927779	10	106	theme	potential	1760:1768	arg1	analysis					1722:1729	analysis	1722:1729	analysis of the electrostatic surface potential on the shape of granzyme-inhibitor binding groove	1722:1818	Furthermore, analysis of the electrostatic surface potential on the shape of granzyme-inhibitor binding groove reveals clear differences at the reactive site.
12927779	10	107	from	shape	1777:1781	arg1	analysis					1722:1729	analysis	1722:1729	analysis of the electrostatic surface potential on the shape of granzyme-inhibitor binding groove	1722:1818	Furthermore, analysis of the electrostatic surface potential on the shape of granzyme-inhibitor binding groove reveals clear differences at the reactive site.
12927779	5	108	theme	S2	943:944	arg1	subsites					957:964	the S1, S2, and S2(') binding subsites	927:964	the S1, S2, and S2(') binding subsites in all granzyme, which may be involved in the structure-function relationship of this enzyme family	927:1064	The paper also highlights key residues at the S1, S2, and S2(') binding subsites in all granzyme, which may be involved in the structure-function relationship of this enzyme family.
12927779	10	109	theme	electrostatic	1738:1750	arg1	potential					1760:1768	the electrostatic surface potential	1734:1768	the electrostatic surface potential on the shape of granzyme-inhibitor binding groove	1734:1818	Furthermore, analysis of the electrostatic surface potential on the shape of granzyme-inhibitor binding groove reveals clear differences at the reactive site.
12927779	6	110	with	structure	1237:1245	arg1	content					1275:1281	a little alpha-helical content	1252:1281	a little alpha-helical content	1252:1281	The predicted 3D homology models show a conserved two similar domain structure, i.e., an N-terminal domain and a C-terminal domain comprising predominantly of beta-sheet structure with a little alpha-helical content.
12927779	1	111	theme	protein	324:330	arg1	perforin					333:340	pore-forming protein (perforin)	311:341	pore-forming protein (perforin)	311:341	Cytotoxic lymphocytes (CTLs), the key players of cell mediated immunity, induce apoptosis by engaging death receptors or through exocytosis of cytolytic granules containing granzyme (proteases) and pore-forming protein (perforin).
12927779	9	112	dep	S2	1520:1521	arg1	Leu-->Phe					1524:1532	Leu-->Phe	1524:1532	Leu-->Phe	1524:1532	Similarly differences at S2 (Leu-->Phe), S3 (Ser-->Gly), and S4 (Arg-->Asn) subsites are quite apparent and appear to hold the potential for selective designing of inhibitors for possible therapeutic applications.
12927779	3	113	from	M	591:591	arg1	modeling					538:545	the homology modeling	525:545	the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h))	525:729	In the present communication, we describe the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h)).
12927779	9	114	theme	S4	1556:1557	arg1	subsites					1571:1578	S2 (Leu-->Phe), S3 (Ser-->Gly), and S4 (Arg-->Asn) subsites	1520:1578	S2 (Leu-->Phe), S3 (Ser-->Gly), and S4 (Arg-->Asn) subsites	1520:1578	Similarly differences at S2 (Leu-->Phe), S3 (Ser-->Gly), and S4 (Arg-->Asn) subsites are quite apparent and appear to hold the potential for selective designing of inhibitors for possible therapeutic applications.
12927779	8	115	from	h	1434:1434	arg1	present					1448:1454	present	1448:1454	present	1448:1454	For example, in granzyme M(h), valine is present at the S1 subsite instead of arginine.
12927779	11	116	theme	granzyme	2169:2176	arg1	family					2178:2183	the granzyme family	2165:2183	the granzyme family	2165:2183	Additionally the different posttranslational modification sites such as phosphorylation (e.g., in granzyme M Thr101, Ser109), myristoylation (Gly22, 117, and 131), and glycosylation (Ser160) have been identified, as very little is known about the functional significance of these modifications in the granzyme family.
12927779	0	117	theme	homology	94:101	arg1	modeling					103:110	homology modeling	94:110	homology modeling	94:110	Bioinformatics of granzymes: sequence comparison and structural studies on granzyme family by homology modeling.
12927779	2	118	from	rat	402:404	arg1	structure					356:364	The crystal structure	344:364	The crystal structure of granzyme B from human (B(h)) and rat (B(r)), as well as that of pro-granzyme K (K(h))	344:453	The crystal structure of granzyme B from human (B(h)) and rat (B(r)), as well as that of pro-granzyme K (K(h)) has been reported recently.
12927779	2	118	from	rat	402:404	arg1	B					378:378	granzyme B	369:378	granzyme B from human (B(h)) and rat (B(r))	369:411	The crystal structure of granzyme B from human (B(h)) and rat (B(r)), as well as that of pro-granzyme K (K(h)) has been reported recently.
12927779	13	119	with	granzymes	2550:2558	arg1	molecules					2571:2579	other molecules	2565:2579	other molecules	2565:2579	These studies are expected to contribute towards the basic understanding of functional associations of the granzymes with other molecules and their possible role in apoptosis.
12927779	8	120	theme	M	1432:1432	arg1	h					1434:1434	granzyme M(h)	1423:1435	granzyme M(h)	1423:1435	For example, in granzyme M(h), valine is present at the S1 subsite instead of arginine.
12927779	7	121	theme	active	1348:1353	arg1	site					1355:1358	the active site	1344:1358	the active site	1344:1358	Micro-heterogeneities have been observed in the vicinity of the active site in all granzymes as compared to granzyme B(h).
12927779	0	122	from	comparison	38:47	arg1	family					84:89	granzyme family	75:89	granzyme family by homology modeling	75:110	Bioinformatics of granzymes: sequence comparison and structural studies on granzyme family by homology modeling.
12927779	12	123	theme	affinity	2414:2421	arg1	rate					2381:2384	the rate	2377:2384	the rate of complexation and binding affinity with proteoglycans	2377:2440	Thus, glycosylation at Ser160 in granzyme M may influence the net charge of the enzyme, resulting in altered substrate binding as compared to granzyme B. Also this modification may influence the rate of complexation and binding affinity with proteoglycans.
12927779	2	124	theme	granzyme	369:376	arg1	B					378:378	granzyme B	369:378	granzyme B from human (B(h)) and rat (B(r))	369:411	The crystal structure of granzyme B from human (B(h)) and rat (B(r)), as well as that of pro-granzyme K (K(h)) has been reported recently.
12927779	6	125	theme	3D	1081:1082	arg1	models					1093:1098	The predicted 3D homology models	1067:1098	The predicted 3D homology models	1067:1098	The predicted 3D homology models show a conserved two similar domain structure, i.e., an N-terminal domain and a C-terminal domain comprising predominantly of beta-sheet structure with a little alpha-helical content.
12927779	6	126	theme	little	1254:1259	arg1	content					1275:1281	a little alpha-helical content	1252:1281	a little alpha-helical content	1252:1281	The predicted 3D homology models show a conserved two similar domain structure, i.e., an N-terminal domain and a C-terminal domain comprising predominantly of beta-sheet structure with a little alpha-helical content.
12927779	10	127	theme	binding	1805:1811	arg1	groove					1813:1818	granzyme-inhibitor binding groove	1786:1818	granzyme-inhibitor binding groove	1786:1818	Furthermore, analysis of the electrostatic surface potential on the shape of granzyme-inhibitor binding groove reveals clear differences at the reactive site.
12927779	1	128	theme	granules	266:273	arg1	exocytosis					242:251	exocytosis	242:251	exocytosis of cytolytic granules containing granzyme (proteases) and pore-forming protein (perforin)	242:341	Cytotoxic lymphocytes (CTLs), the key players of cell mediated immunity, induce apoptosis by engaging death receptors or through exocytosis of cytolytic granules containing granzyme (proteases) and pore-forming protein (perforin).
12927779	8	129	from	present	1448:1454	arg1	h					1434:1434	granzyme M(h)	1423:1435	granzyme M(h)	1423:1435	For example, in granzyme M(h), valine is present at the S1 subsite instead of arginine.
12927779	5	130	theme	binding	949:955	arg1	subsites					957:964	the S1, S2, and S2(') binding subsites	927:964	the S1, S2, and S2(') binding subsites in all granzyme, which may be involved in the structure-function relationship of this enzyme family	927:1064	The paper also highlights key residues at the S1, S2, and S2(') binding subsites in all granzyme, which may be involved in the structure-function relationship of this enzyme family.
12927779	1	131	theme	granzyme	286:293	arg1	proteases					296:304	granzyme (proteases)	286:305	granzyme (proteases)	286:305	Cytotoxic lymphocytes (CTLs), the key players of cell mediated immunity, induce apoptosis by engaging death receptors or through exocytosis of cytolytic granules containing granzyme (proteases) and pore-forming protein (perforin).
12927779	11	132	from	significance	2126:2137	arg1	family					2178:2183	the granzyme family	2165:2183	the granzyme family	2165:2183	Additionally the different posttranslational modification sites such as phosphorylation (e.g., in granzyme M Thr101, Ser109), myristoylation (Gly22, 117, and 131), and glycosylation (Ser160) have been identified, as very little is known about the functional significance of these modifications in the granzyme family.
12927779	3	133	theme	structural	655:664	arg1	coordinates					666:676	the crystal structural coordinates	643:676	the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h))	643:729	In the present communication, we describe the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h)).
12927779	0	134	theme	structural	53:62	arg1	studies					64:70	structural studies	53:70	structural studies on granzyme family by homology modeling	53:110	Bioinformatics of granzymes: sequence comparison and structural studies on granzyme family by homology modeling.
12927779	3	135	theme	K	699:699	arg1	coordinates					666:676	the crystal structural coordinates	643:676	the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h))	643:729	In the present communication, we describe the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h)).
12927779	12	136	theme	altered	2287:2293	arg1	binding					2305:2311	altered substrate binding	2287:2311	altered substrate binding	2287:2311	Thus, glycosylation at Ser160 in granzyme M may influence the net charge of the enzyme, resulting in altered substrate binding as compared to granzyme B. Also this modification may influence the rate of complexation and binding affinity with proteoglycans.
12927779	8	137	from	subsite	1466:1472	arg1	present					1448:1454	present	1448:1454	present	1448:1454	For example, in granzyme M(h), valine is present at the S1 subsite instead of arginine.
12927779	5	138	theme	structure-function	1012:1029	arg1	relationship					1031:1042	the structure-function relationship	1008:1042	the structure-function relationship of this enzyme family	1008:1064	The paper also highlights key residues at the S1, S2, and S2(') binding subsites in all granzyme, which may be involved in the structure-function relationship of this enzyme family.
12927779	12	139	theme	binding	2406:2412	arg1	affinity					2414:2421	binding affinity	2406:2421	binding affinity	2406:2421	Thus, glycosylation at Ser160 in granzyme M may influence the net charge of the enzyme, resulting in altered substrate binding as compared to granzyme B. Also this modification may influence the rate of complexation and binding affinity with proteoglycans.
12927779	6	140	theme	domain	1129:1134	arg1	structure					1136:1144	a conserved two similar domain structure	1105:1144	a conserved two similar domain structure	1105:1144	The predicted 3D homology models show a conserved two similar domain structure, i.e., an N-terminal domain and a C-terminal domain comprising predominantly of beta-sheet structure with a little alpha-helical content.
12927779	0	141	dep	Bioinformatics	0:13	arg1	comparison					38:47	sequence comparison	29:47	sequence comparison	29:47	Bioinformatics of granzymes: sequence comparison and structural studies on granzyme family by homology modeling.
12927779	0	141	dep	Bioinformatics	0:13	arg1	studies					64:70	structural studies	53:70	structural studies on granzyme family by homology modeling	53:110	Bioinformatics of granzymes: sequence comparison and structural studies on granzyme family by homology modeling.
12927779	9	142	from	subsites	1571:1578	arg1	differences					1505:1515	differences	1505:1515	differences at S2 (Leu-->Phe), S3 (Ser-->Gly), and S4 (Arg-->Asn) subsites	1505:1578	Similarly differences at S2 (Leu-->Phe), S3 (Ser-->Gly), and S4 (Arg-->Asn) subsites are quite apparent and appear to hold the potential for selective designing of inhibitors for possible therapeutic applications.
12927779	11	143	theme	modification	1913:1924	arg1	myristoylation					1994:2007	myristoylation	1994:2007	myristoylation (Gly22, 117, and 131)	1994:2029	Additionally the different posttranslational modification sites such as phosphorylation (e.g., in granzyme M Thr101, Ser109), myristoylation (Gly22, 117, and 131), and glycosylation (Ser160) have been identified, as very little is known about the functional significance of these modifications in the granzyme family.
12927779	11	143	theme	modification	1913:1924	arg1	glycosylation					2036:2048	glycosylation	2036:2048	glycosylation (Ser160)	2036:2057	Additionally the different posttranslational modification sites such as phosphorylation (e.g., in granzyme M Thr101, Ser109), myristoylation (Gly22, 117, and 131), and glycosylation (Ser160) have been identified, as very little is known about the functional significance of these modifications in the granzyme family.
12927779	11	143	theme	modification	1913:1924	arg1	sites					1926:1930	the different posttranslational modification sites	1881:1930	the different posttranslational modification sites such as phosphorylation (e.g., in granzyme M Thr101, Ser109), myristoylation (Gly22, 117, and 131), and glycosylation (Ser160)	1881:2057	Additionally the different posttranslational modification sites such as phosphorylation (e.g., in granzyme M Thr101, Ser109), myristoylation (Gly22, 117, and 131), and glycosylation (Ser160) have been identified, as very little is known about the functional significance of these modifications in the granzyme family.
12927779	11	143	theme	modification	1913:1924	arg1	phosphorylation					1940:1954	phosphorylation	1940:1954	phosphorylation (e.g., in granzyme M Thr101, Ser109)	1940:1991	Additionally the different posttranslational modification sites such as phosphorylation (e.g., in granzyme M Thr101, Ser109), myristoylation (Gly22, 117, and 131), and glycosylation (Ser160) have been identified, as very little is known about the functional significance of these modifications in the granzyme family.
12927779	5	144	theme	key	911:913	arg1	residues					915:922	key residues	911:922	key residues at the S1, S2, and S2(') binding subsites in all granzyme, which may be involved in the structure-function relationship of this enzyme family	911:1064	The paper also highlights key residues at the S1, S2, and S2(') binding subsites in all granzyme, which may be involved in the structure-function relationship of this enzyme family.
12927779	11	145	theme	different	1885:1893	arg1	myristoylation					1994:2007	myristoylation	1994:2007	myristoylation (Gly22, 117, and 131)	1994:2029	Additionally the different posttranslational modification sites such as phosphorylation (e.g., in granzyme M Thr101, Ser109), myristoylation (Gly22, 117, and 131), and glycosylation (Ser160) have been identified, as very little is known about the functional significance of these modifications in the granzyme family.
12927779	11	145	theme	different	1885:1893	arg1	glycosylation					2036:2048	glycosylation	2036:2048	glycosylation (Ser160)	2036:2057	Additionally the different posttranslational modification sites such as phosphorylation (e.g., in granzyme M Thr101, Ser109), myristoylation (Gly22, 117, and 131), and glycosylation (Ser160) have been identified, as very little is known about the functional significance of these modifications in the granzyme family.
12927779	11	145	theme	different	1885:1893	arg1	sites					1926:1930	the different posttranslational modification sites	1881:1930	the different posttranslational modification sites such as phosphorylation (e.g., in granzyme M Thr101, Ser109), myristoylation (Gly22, 117, and 131), and glycosylation (Ser160)	1881:2057	Additionally the different posttranslational modification sites such as phosphorylation (e.g., in granzyme M Thr101, Ser109), myristoylation (Gly22, 117, and 131), and glycosylation (Ser160) have been identified, as very little is known about the functional significance of these modifications in the granzyme family.
12927779	11	145	theme	different	1885:1893	arg1	phosphorylation					1940:1954	phosphorylation	1940:1954	phosphorylation (e.g., in granzyme M Thr101, Ser109)	1940:1991	Additionally the different posttranslational modification sites such as phosphorylation (e.g., in granzyme M Thr101, Ser109), myristoylation (Gly22, 117, and 131), and glycosylation (Ser160) have been identified, as very little is known about the functional significance of these modifications in the granzyme family.
12927779	3	146	theme	granzyme	550:557	arg1	family					559:564	granzyme family	550:564	granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse)	550:632	In the present communication, we describe the homology modeling of granzyme family (in particular Gzm A(h), M(h), B(m), and C(m) from human and mouse) based on the crystal structural coordinates of trypsin, granzyme K (K(h)), and granzyme B (B(h)).
12356334	2	0	theme	lung	325:328	arg1	types					335:339	specific lung cell types	316:339	specific lung cell types	316:339	SP-B is expressed and secreted by specific lung cell types, i.e. alveolar type II and Clara cells, of the respiratory epithelium.
12356334	7	1	theme	Asn129-Gln-Thr131	1329:1345	arg1	site					1347:1350	the Asn129-Gln-Thr131 site	1325:1350	the Asn129-Gln-Thr131 site	1325:1350	Using both the stably transfected cell lines and fetal lung explants, we observed that the C allele variant is indeed glycosylated at the Asn129-Gln-Thr131 site, whereas the T allele variant, which served as a control, is not.
12356334	0	2	link	N-linked	15:22	arg1	glycosylation					24:36	N-linked glycosylation	15:36	N-linked glycosylation	15:36	Differences in N-linked glycosylation between human surfactant protein-B variants of the C or T allele at the single-nucleotide polymorphism at position 1580: implications for disease.
12356334	7	3	theme	allele	1284:1289	arg1	variant					1291:1297	the C allele variant	1278:1297	the C allele variant	1278:1297	Using both the stably transfected cell lines and fetal lung explants, we observed that the C allele variant is indeed glycosylated at the Asn129-Gln-Thr131 site, whereas the T allele variant, which served as a control, is not.
12356334	10	4	theme	disease	1911:1917	arg1	conditions					1919:1928	certain disease conditions	1903:1928	certain disease conditions	1903:1928	Further, we speculate that, given the fact that this SNP is found frequently in the general population, N-linked glycosylation at residue Asn129 interferes with SP-B processing, secretion and folding under certain disease conditions.
12356334	8	5	theme	SP-B	1459:1462	arg1	variants					1464:1471	both SP-B variants	1454:1471	both SP-B variants	1454:1471	In addition, we also confirmed that both SP-B variants contain another N-linked glycosylation site, Asn311-Ser-Ser313.
12356334	3	6	theme	kDa	497:499	arg1	SP-B					508:511	an 8 kDa mature SP-B	492:511	an 8 kDa mature SP-B	492:511	The SP-B precursor (42 kDa) undergoes post-translational processing to generate an 8 kDa mature SP-B.
12356334	10	7	located	found	1757:1761	arg1	population					1789:1798	the general population	1777:1798	the general population	1777:1798	Further, we speculate that, given the fact that this SNP is found frequently in the general population, N-linked glycosylation at residue Asn129 interferes with SP-B processing, secretion and folding under certain disease conditions.
12356334	10	7	located	found	1757:1761	arg2	SNP					1750:1752	this SNP	1745:1752	this SNP	1745:1752	Further, we speculate that, given the fact that this SNP is found frequently in the general population, N-linked glycosylation at residue Asn129 interferes with SP-B processing, secretion and folding under certain disease conditions.
12356334	8	8	gly	glycosylation	1498:1510	arg2	Asn311-Ser-Ser313					1518:1534	Asn311-Ser-Ser313	1518:1534	Asn311-Ser-Ser313	1518:1534	In addition, we also confirmed that both SP-B variants contain another N-linked glycosylation site, Asn311-Ser-Ser313.
12356334	8	8	gly	glycosylation	1498:1510	arg2	site					1512:1515	another N-linked glycosylation site	1481:1515	another N-linked glycosylation site	1481:1515	In addition, we also confirmed that both SP-B variants contain another N-linked glycosylation site, Asn311-Ser-Ser313.
12356334	5	9	attach	present	828:834	arg2	present					828:834	present	828:834	present	828:834	The Thr131-->Ile substitution can eliminate a potential N-linked glycosylation site, Asn129-Gln-Thr131, which is present in the SP-B variant of the C allele (ACT/Thr) but not in that of the T allele (ATT/Ile).
12356334	5	9	attach	present	828:834	arg2	Asn129-Gln-Thr131					800:816	Asn129-Gln-Thr131	800:816	Asn129-Gln-Thr131	800:816	The Thr131-->Ile substitution can eliminate a potential N-linked glycosylation site, Asn129-Gln-Thr131, which is present in the SP-B variant of the C allele (ACT/Thr) but not in that of the T allele (ATT/Ile).
12356334	5	9	attach	present	828:834	arg1	variant					848:854	the SP-B variant	839:854	the SP-B variant of the C allele (ACT/Thr)	839:880	The Thr131-->Ile substitution can eliminate a potential N-linked glycosylation site, Asn129-Gln-Thr131, which is present in the SP-B variant of the C allele (ACT/Thr) but not in that of the T allele (ATT/Ile).
12356334	5	9	attach	present	828:834	arg2	site					794:797	a potential N-linked glycosylation site	759:797	a potential N-linked glycosylation site	759:797	The Thr131-->Ile substitution can eliminate a potential N-linked glycosylation site, Asn129-Gln-Thr131, which is present in the SP-B variant of the C allele (ACT/Thr) but not in that of the T allele (ATT/Ile).
12356334	5	9	attach	present	828:834	arg1	that					893:896	that	893:896	that	893:896	The Thr131-->Ile substitution can eliminate a potential N-linked glycosylation site, Asn129-Gln-Thr131, which is present in the SP-B variant of the C allele (ACT/Thr) but not in that of the T allele (ATT/Ile).
12356334	5	10	gly	glycosylation	780:792	arg2	present					828:834	present	828:834	present	828:834	The Thr131-->Ile substitution can eliminate a potential N-linked glycosylation site, Asn129-Gln-Thr131, which is present in the SP-B variant of the C allele (ACT/Thr) but not in that of the T allele (ATT/Ile).
12356334	5	10	gly	glycosylation	780:792	arg2	Asn129-Gln-Thr131					800:816	Asn129-Gln-Thr131	800:816	Asn129-Gln-Thr131	800:816	The Thr131-->Ile substitution can eliminate a potential N-linked glycosylation site, Asn129-Gln-Thr131, which is present in the SP-B variant of the C allele (ACT/Thr) but not in that of the T allele (ATT/Ile).
12356334	5	10	gly	glycosylation	780:792	arg1	variant					848:854	the SP-B variant	839:854	the SP-B variant of the C allele (ACT/Thr)	839:880	The Thr131-->Ile substitution can eliminate a potential N-linked glycosylation site, Asn129-Gln-Thr131, which is present in the SP-B variant of the C allele (ACT/Thr) but not in that of the T allele (ATT/Ile).
12356334	5	10	gly	glycosylation	780:792	arg2	site					794:797	a potential N-linked glycosylation site	759:797	a potential N-linked glycosylation site	759:797	The Thr131-->Ile substitution can eliminate a potential N-linked glycosylation site, Asn129-Gln-Thr131, which is present in the SP-B variant of the C allele (ACT/Thr) but not in that of the T allele (ATT/Ile).
12356334	5	10	gly	glycosylation	780:792	arg1	that					893:896	that	893:896	that	893:896	The Thr131-->Ile substitution can eliminate a potential N-linked glycosylation site, Asn129-Gln-Thr131, which is present in the SP-B variant of the C allele (ACT/Thr) but not in that of the T allele (ATT/Ile).
12356334	4	11	theme	SP-B	591:594	arg1	exon					581:584	exon 4	581:586	exon 4 of SP-B	581:594	A single-nucleotide polymorphism (SNP) at nucleotide 1580 (C/T) in exon 4 of SP-B that changes amino acid 131 from threonine to isoleucine (Thr131-->Ile) is associated with several pulmonary diseases.
12356334	1	12	theme	Human	185:189	arg1	protein-B					202:210	Human surfactant protein-B	185:210	Human surfactant protein-B (SP-B)	185:217	Human surfactant protein-B (SP-B), a hydrophobic protein, is essential for normal lung function.
12356334	1	12	theme	Human	185:189	arg1	protein					234:240	a hydrophobic protein	220:240	a hydrophobic protein	220:240	Human surfactant protein-B (SP-B), a hydrophobic protein, is essential for normal lung function.
12356334	1	12	theme	Human	185:189	arg1	SP-B					213:216	SP-B	213:216	SP-B	213:216	Human surfactant protein-B (SP-B), a hydrophobic protein, is essential for normal lung function.
12356334	6	13	theme	cell	1079:1082	arg1	lines					1084:1088	stably transfected Chinese hamster ovary cell lines	1038:1088	stably transfected Chinese hamster ovary cell lines that expressed each version of SP-B, and developed specific SP-B polyclonal anti-peptide antibodies	1038:1188	To determine whether the C allele SP-B variant is indeed glycosylated at Asn(129)-Gln-Thr131, we first generated stably transfected Chinese hamster ovary cell lines that expressed each version of SP-B, and developed specific SP-B polyclonal anti-peptide antibodies.
12356334	3	14	theme	post-translational	450:467	arg1	processing					469:478	post-translational processing	450:478	post-translational processing	450:478	The SP-B precursor (42 kDa) undergoes post-translational processing to generate an 8 kDa mature SP-B.
12356334	5	15	theme	potential	761:769	arg1	present					828:834	present	828:834	present	828:834	The Thr131-->Ile substitution can eliminate a potential N-linked glycosylation site, Asn129-Gln-Thr131, which is present in the SP-B variant of the C allele (ACT/Thr) but not in that of the T allele (ATT/Ile).
12356334	5	15	theme	potential	761:769	arg1	Asn129-Gln-Thr131					800:816	Asn129-Gln-Thr131	800:816	Asn129-Gln-Thr131	800:816	The Thr131-->Ile substitution can eliminate a potential N-linked glycosylation site, Asn129-Gln-Thr131, which is present in the SP-B variant of the C allele (ACT/Thr) but not in that of the T allele (ATT/Ile).
12356334	5	15	theme	potential	761:769	arg1	site					794:797	a potential N-linked glycosylation site	759:797	a potential N-linked glycosylation site	759:797	The Thr131-->Ile substitution can eliminate a potential N-linked glycosylation site, Asn129-Gln-Thr131, which is present in the SP-B variant of the C allele (ACT/Thr) but not in that of the T allele (ATT/Ile).
12356334	7	16	theme	lung	1246:1249	arg1	explants					1251:1258	fetal lung explants	1240:1258	fetal lung explants	1240:1258	Using both the stably transfected cell lines and fetal lung explants, we observed that the C allele variant is indeed glycosylated at the Asn129-Gln-Thr131 site, whereas the T allele variant, which served as a control, is not.
12356334	5	17	theme	glycosylation	780:792	arg1	present					828:834	present	828:834	present	828:834	The Thr131-->Ile substitution can eliminate a potential N-linked glycosylation site, Asn129-Gln-Thr131, which is present in the SP-B variant of the C allele (ACT/Thr) but not in that of the T allele (ATT/Ile).
12356334	5	17	theme	glycosylation	780:792	arg1	Asn129-Gln-Thr131					800:816	Asn129-Gln-Thr131	800:816	Asn129-Gln-Thr131	800:816	The Thr131-->Ile substitution can eliminate a potential N-linked glycosylation site, Asn129-Gln-Thr131, which is present in the SP-B variant of the C allele (ACT/Thr) but not in that of the T allele (ATT/Ile).
12356334	5	17	theme	glycosylation	780:792	arg1	site					794:797	a potential N-linked glycosylation site	759:797	a potential N-linked glycosylation site	759:797	The Thr131-->Ile substitution can eliminate a potential N-linked glycosylation site, Asn129-Gln-Thr131, which is present in the SP-B variant of the C allele (ACT/Thr) but not in that of the T allele (ATT/Ile).
12356334	0	18	from	variants	73:80	arg1	polymorphism					128:139	the single-nucleotide polymorphism	106:139	the single-nucleotide polymorphism at position 1580	106:156	Differences in N-linked glycosylation between human surfactant protein-B variants of the C or T allele at the single-nucleotide polymorphism at position 1580: implications for disease.
12356334	10	19	theme	N-linked	1801:1808	arg1	glycosylation					1810:1822	N-linked glycosylation	1801:1822	N-linked glycosylation at residue Asn129	1801:1840	Further, we speculate that, given the fact that this SNP is found frequently in the general population, N-linked glycosylation at residue Asn129 interferes with SP-B processing, secretion and folding under certain disease conditions.
12356334	6	20	theme	anti-peptide	1166:1177	arg1	antibodies					1179:1188	specific SP-B polyclonal anti-peptide antibodies	1141:1188	specific SP-B polyclonal anti-peptide antibodies	1141:1188	To determine whether the C allele SP-B variant is indeed glycosylated at Asn(129)-Gln-Thr131, we first generated stably transfected Chinese hamster ovary cell lines that expressed each version of SP-B, and developed specific SP-B polyclonal anti-peptide antibodies.
12356334	5	21	theme	SP-B	843:846	arg1	variant					848:854	the SP-B variant	839:854	the SP-B variant of the C allele (ACT/Thr)	839:880	The Thr131-->Ile substitution can eliminate a potential N-linked glycosylation site, Asn129-Gln-Thr131, which is present in the SP-B variant of the C allele (ACT/Thr) but not in that of the T allele (ATT/Ile).
12356334	9	22	theme	pulmonary	1572:1580	arg1	diseases					1582:1589	several pulmonary diseases	1564:1589	several pulmonary diseases	1564:1589	Given its association with several pulmonary diseases, this finding provides useful information for future studies in disease systems associated with this SNP.
12356334	6	23	theme	ovary	1073:1077	arg1	lines					1084:1088	stably transfected Chinese hamster ovary cell lines	1038:1088	stably transfected Chinese hamster ovary cell lines that expressed each version of SP-B, and developed specific SP-B polyclonal anti-peptide antibodies	1038:1188	To determine whether the C allele SP-B variant is indeed glycosylated at Asn(129)-Gln-Thr131, we first generated stably transfected Chinese hamster ovary cell lines that expressed each version of SP-B, and developed specific SP-B polyclonal anti-peptide antibodies.
12356334	7	24	theme	cell	1225:1228	arg1	lines					1230:1234	the stably transfected cell lines	1202:1234	the stably transfected cell lines	1202:1234	Using both the stably transfected cell lines and fetal lung explants, we observed that the C allele variant is indeed glycosylated at the Asn129-Gln-Thr131 site, whereas the T allele variant, which served as a control, is not.
12356334	6	25	theme	SP-B	1150:1153	arg1	antibodies					1179:1188	specific SP-B polyclonal anti-peptide antibodies	1141:1188	specific SP-B polyclonal anti-peptide antibodies	1141:1188	To determine whether the C allele SP-B variant is indeed glycosylated at Asn(129)-Gln-Thr131, we first generated stably transfected Chinese hamster ovary cell lines that expressed each version of SP-B, and developed specific SP-B polyclonal anti-peptide antibodies.
12356334	6	26	theme	Chinese	1057:1063	arg1	lines					1084:1088	stably transfected Chinese hamster ovary cell lines	1038:1088	stably transfected Chinese hamster ovary cell lines that expressed each version of SP-B, and developed specific SP-B polyclonal anti-peptide antibodies	1038:1188	To determine whether the C allele SP-B variant is indeed glycosylated at Asn(129)-Gln-Thr131, we first generated stably transfected Chinese hamster ovary cell lines that expressed each version of SP-B, and developed specific SP-B polyclonal anti-peptide antibodies.
12356334	4	27	from	nucleotide	556:565	arg1	SNP					548:550	SNP	548:550	SNP	548:550	A single-nucleotide polymorphism (SNP) at nucleotide 1580 (C/T) in exon 4 of SP-B that changes amino acid 131 from threonine to isoleucine (Thr131-->Ile) is associated with several pulmonary diseases.
12356334	4	27	from	nucleotide	556:565	arg1	polymorphism					534:545	A single-nucleotide polymorphism	514:545	A single-nucleotide polymorphism (SNP) at nucleotide 1580 (C/T) in exon 4 of SP-B that changes amino acid 131 from threonine to isoleucine (Thr131-->Ile)	514:666	A single-nucleotide polymorphism (SNP) at nucleotide 1580 (C/T) in exon 4 of SP-B that changes amino acid 131 from threonine to isoleucine (Thr131-->Ile) is associated with several pulmonary diseases.
12356334	4	27	from	nucleotide	556:565	arg1	C/T					573:575	C/T	573:575	C/T	573:575	A single-nucleotide polymorphism (SNP) at nucleotide 1580 (C/T) in exon 4 of SP-B that changes amino acid 131 from threonine to isoleucine (Thr131-->Ile) is associated with several pulmonary diseases.
12356334	5	28	from	present	828:834	arg1	variant					848:854	the SP-B variant	839:854	the SP-B variant of the C allele (ACT/Thr)	839:880	The Thr131-->Ile substitution can eliminate a potential N-linked glycosylation site, Asn129-Gln-Thr131, which is present in the SP-B variant of the C allele (ACT/Thr) but not in that of the T allele (ATT/Ile).
12356334	5	28	from	present	828:834	arg1	that					893:896	that	893:896	that	893:896	The Thr131-->Ile substitution can eliminate a potential N-linked glycosylation site, Asn129-Gln-Thr131, which is present in the SP-B variant of the C allele (ACT/Thr) but not in that of the T allele (ATT/Ile).
12356334	9	29	theme	useful	1614:1619	arg1	information					1621:1631	useful information	1614:1631	useful information for future studies in disease systems associated with this SNP	1614:1694	Given its association with several pulmonary diseases, this finding provides useful information for future studies in disease systems associated with this SNP.
12356334	0	30	from	Differences	0:10	arg1	glycosylation					24:36	N-linked glycosylation	15:36	N-linked glycosylation	15:36	Differences in N-linked glycosylation between human surfactant protein-B variants of the C or T allele at the single-nucleotide polymorphism at position 1580: implications for disease.
12356334	4	31	theme	several	687:693	arg1	diseases					705:712	several pulmonary diseases	687:712	several pulmonary diseases	687:712	A single-nucleotide polymorphism (SNP) at nucleotide 1580 (C/T) in exon 4 of SP-B that changes amino acid 131 from threonine to isoleucine (Thr131-->Ile) is associated with several pulmonary diseases.
12356334	0	32	theme	allele	96:101	arg1	variants					73:80	human surfactant protein-B variants	46:80	human surfactant protein-B variants of the C or T allele at the single-nucleotide polymorphism at position 1580	46:156	Differences in N-linked glycosylation between human surfactant protein-B variants of the C or T allele at the single-nucleotide polymorphism at position 1580: implications for disease.
12356334	5	33	from	variant	848:854	arg1	present					828:834	present	828:834	present	828:834	The Thr131-->Ile substitution can eliminate a potential N-linked glycosylation site, Asn129-Gln-Thr131, which is present in the SP-B variant of the C allele (ACT/Thr) but not in that of the T allele (ATT/Ile).
12356334	5	33	from	variant	848:854	arg1	site					794:797	a potential N-linked glycosylation site	759:797	a potential N-linked glycosylation site	759:797	The Thr131-->Ile substitution can eliminate a potential N-linked glycosylation site, Asn129-Gln-Thr131, which is present in the SP-B variant of the C allele (ACT/Thr) but not in that of the T allele (ATT/Ile).
12356334	6	34	theme	C	950:950	arg1	variant					964:970	the C allele SP-B variant	946:970	the C allele SP-B variant	946:970	To determine whether the C allele SP-B variant is indeed glycosylated at Asn(129)-Gln-Thr131, we first generated stably transfected Chinese hamster ovary cell lines that expressed each version of SP-B, and developed specific SP-B polyclonal anti-peptide antibodies.
12356334	2	35	theme	epithelium	400:409	arg1	types					335:339	specific lung cell types	316:339	specific lung cell types	316:339	SP-B is expressed and secreted by specific lung cell types, i.e. alveolar type II and Clara cells, of the respiratory epithelium.
12356334	6	36	gly	glycosylated	982:993	arg2	Asn					998:1000	Asn(129)-Gln-Thr131	998:1016	Asn(129)-Gln-Thr131	998:1016	To determine whether the C allele SP-B variant is indeed glycosylated at Asn(129)-Gln-Thr131, we first generated stably transfected Chinese hamster ovary cell lines that expressed each version of SP-B, and developed specific SP-B polyclonal anti-peptide antibodies.
12356334	6	36	gly	glycosylated	982:993	arg1	variant					964:970	the C allele SP-B variant	946:970	the C allele SP-B variant	946:970	To determine whether the C allele SP-B variant is indeed glycosylated at Asn(129)-Gln-Thr131, we first generated stably transfected Chinese hamster ovary cell lines that expressed each version of SP-B, and developed specific SP-B polyclonal anti-peptide antibodies.
12356334	2	37	theme	alveolar	347:354	arg1	type					356:359	alveolar type II and Clara cells	347:378	type	356:359	SP-B is expressed and secreted by specific lung cell types, i.e. alveolar type II and Clara cells, of the respiratory epithelium.
12356334	5	38	theme	C	863:863	arg1	allele					865:870	the C allele	859:870	the C allele (ACT/Thr)	859:880	The Thr131-->Ile substitution can eliminate a potential N-linked glycosylation site, Asn129-Gln-Thr131, which is present in the SP-B variant of the C allele (ACT/Thr) but not in that of the T allele (ATT/Ile).
12356334	5	38	theme	C	863:863	arg1	ACT/Thr					873:879	ACT/Thr	873:879	ACT/Thr	873:879	The Thr131-->Ile substitution can eliminate a potential N-linked glycosylation site, Asn129-Gln-Thr131, which is present in the SP-B variant of the C allele (ACT/Thr) but not in that of the T allele (ATT/Ile).
12356334	9	39	theme	disease	1655:1661	arg1	systems					1663:1669	disease systems	1655:1669	disease systems associated with this SNP	1655:1694	Given its association with several pulmonary diseases, this finding provides useful information for future studies in disease systems associated with this SNP.
12356334	3	40	theme	SP-B	416:419	arg1	kDa					435:437	42 kDa	432:437	42 kDa	432:437	The SP-B precursor (42 kDa) undergoes post-translational processing to generate an 8 kDa mature SP-B.
12356334	3	40	theme	SP-B	416:419	arg1	precursor					421:429	The SP-B precursor	412:429	The SP-B precursor (42 kDa)	412:438	The SP-B precursor (42 kDa) undergoes post-translational processing to generate an 8 kDa mature SP-B.
12356334	0	41	theme	N-linked	15:22	arg1	glycosylation					24:36	N-linked glycosylation	15:36	N-linked glycosylation	15:36	Differences in N-linked glycosylation between human surfactant protein-B variants of the C or T allele at the single-nucleotide polymorphism at position 1580: implications for disease.
12356334	1	42	theme	lung	267:270	arg1	function					272:279	normal lung function	260:279	normal lung function	260:279	Human surfactant protein-B (SP-B), a hydrophobic protein, is essential for normal lung function.
12356334	10	43	from	residue	1827:1833	arg1	glycosylation					1810:1822	N-linked glycosylation	1801:1822	N-linked glycosylation at residue Asn129	1801:1840	Further, we speculate that, given the fact that this SNP is found frequently in the general population, N-linked glycosylation at residue Asn129 interferes with SP-B processing, secretion and folding under certain disease conditions.
12356334	2	44	theme	Clara	368:372	arg1	cells					374:378	alveolar type II and Clara cells	347:378	cells	374:378	SP-B is expressed and secreted by specific lung cell types, i.e. alveolar type II and Clara cells, of the respiratory epithelium.
12356334	2	45	theme	specific	316:323	arg1	types					335:339	specific lung cell types	316:339	specific lung cell types	316:339	SP-B is expressed and secreted by specific lung cell types, i.e. alveolar type II and Clara cells, of the respiratory epithelium.
12356334	0	46	theme	surfactant	52:61	arg1	variants					73:80	human surfactant protein-B variants	46:80	human surfactant protein-B variants of the C or T allele at the single-nucleotide polymorphism at position 1580	46:156	Differences in N-linked glycosylation between human surfactant protein-B variants of the C or T allele at the single-nucleotide polymorphism at position 1580: implications for disease.
12356334	7	47	dep	glycosylated	1309:1320	arg1	whereas					1353:1359	whereas	1353:1359	whereas	1353:1359	Using both the stably transfected cell lines and fetal lung explants, we observed that the C allele variant is indeed glycosylated at the Asn129-Gln-Thr131 site, whereas the T allele variant, which served as a control, is not.
12356334	7	48	theme	T	1365:1365	arg1	control					1401:1407	a control	1399:1407	a control	1399:1407	Using both the stably transfected cell lines and fetal lung explants, we observed that the C allele variant is indeed glycosylated at the Asn129-Gln-Thr131 site, whereas the T allele variant, which served as a control, is not.
12356334	7	48	theme	T	1365:1365	arg1	variant					1374:1380	the T allele variant	1361:1380	the T allele variant	1361:1380	Using both the stably transfected cell lines and fetal lung explants, we observed that the C allele variant is indeed glycosylated at the Asn129-Gln-Thr131 site, whereas the T allele variant, which served as a control, is not.
12356334	10	49	theme	certain	1903:1909	arg1	conditions					1919:1928	certain disease conditions	1903:1928	certain disease conditions	1903:1928	Further, we speculate that, given the fact that this SNP is found frequently in the general population, N-linked glycosylation at residue Asn129 interferes with SP-B processing, secretion and folding under certain disease conditions.
12356334	6	50	theme	transfected	1045:1055	arg1	lines					1084:1088	stably transfected Chinese hamster ovary cell lines	1038:1088	stably transfected Chinese hamster ovary cell lines that expressed each version of SP-B, and developed specific SP-B polyclonal anti-peptide antibodies	1038:1188	To determine whether the C allele SP-B variant is indeed glycosylated at Asn(129)-Gln-Thr131, we first generated stably transfected Chinese hamster ovary cell lines that expressed each version of SP-B, and developed specific SP-B polyclonal anti-peptide antibodies.
12356334	0	51	from	polymorphism	128:139	arg1	variants					73:80	human surfactant protein-B variants	46:80	human surfactant protein-B variants of the C or T allele at the single-nucleotide polymorphism at position 1580	46:156	Differences in N-linked glycosylation between human surfactant protein-B variants of the C or T allele at the single-nucleotide polymorphism at position 1580: implications for disease.
12356334	0	51	from	polymorphism	128:139	arg1	allele					96:101	the C or T allele	85:101	allele	96:101	Differences in N-linked glycosylation between human surfactant protein-B variants of the C or T allele at the single-nucleotide polymorphism at position 1580: implications for disease.
12356334	0	52	dep	Differences	0:10	arg1	implications					159:170	implications	159:170	Differences in N-linked glycosylation between human surfactant protein-B variants of the C or T allele at the single-nucleotide polymorphism at position 1580: implications for disease.	0:183	Differences in N-linked glycosylation between human surfactant protein-B variants of the C or T allele at the single-nucleotide polymorphism at position 1580: implications for disease.
12356334	6	53	theme	specific	1141:1148	arg1	antibodies					1179:1188	specific SP-B polyclonal anti-peptide antibodies	1141:1188	specific SP-B polyclonal anti-peptide antibodies	1141:1188	To determine whether the C allele SP-B variant is indeed glycosylated at Asn(129)-Gln-Thr131, we first generated stably transfected Chinese hamster ovary cell lines that expressed each version of SP-B, and developed specific SP-B polyclonal anti-peptide antibodies.
12356334	2	54	theme	cell	330:333	arg1	types					335:339	specific lung cell types	316:339	specific lung cell types	316:339	SP-B is expressed and secreted by specific lung cell types, i.e. alveolar type II and Clara cells, of the respiratory epithelium.
12356334	8	55	theme	glycosylation	1498:1510	arg1	site					1512:1515	another N-linked glycosylation site	1481:1515	another N-linked glycosylation site	1481:1515	In addition, we also confirmed that both SP-B variants contain another N-linked glycosylation site, Asn311-Ser-Ser313.
12356334	8	55	theme	glycosylation	1498:1510	arg1	Asn311-Ser-Ser313					1518:1534	Asn311-Ser-Ser313	1518:1534	Asn311-Ser-Ser313	1518:1534	In addition, we also confirmed that both SP-B variants contain another N-linked glycosylation site, Asn311-Ser-Ser313.
12356334	6	56	theme	SP-B	959:962	arg1	variant					964:970	the C allele SP-B variant	946:970	the C allele SP-B variant	946:970	To determine whether the C allele SP-B variant is indeed glycosylated at Asn(129)-Gln-Thr131, we first generated stably transfected Chinese hamster ovary cell lines that expressed each version of SP-B, and developed specific SP-B polyclonal anti-peptide antibodies.
12356334	4	57	theme	single-nucleotide	516:532	arg1	SNP					548:550	SNP	548:550	SNP	548:550	A single-nucleotide polymorphism (SNP) at nucleotide 1580 (C/T) in exon 4 of SP-B that changes amino acid 131 from threonine to isoleucine (Thr131-->Ile) is associated with several pulmonary diseases.
12356334	4	57	theme	single-nucleotide	516:532	arg1	polymorphism					534:545	A single-nucleotide polymorphism	514:545	A single-nucleotide polymorphism (SNP) at nucleotide 1580 (C/T) in exon 4 of SP-B that changes amino acid 131 from threonine to isoleucine (Thr131-->Ile)	514:666	A single-nucleotide polymorphism (SNP) at nucleotide 1580 (C/T) in exon 4 of SP-B that changes amino acid 131 from threonine to isoleucine (Thr131-->Ile) is associated with several pulmonary diseases.
12356334	4	57	theme	single-nucleotide	516:532	arg1	C/T					573:575	C/T	573:575	C/T	573:575	A single-nucleotide polymorphism (SNP) at nucleotide 1580 (C/T) in exon 4 of SP-B that changes amino acid 131 from threonine to isoleucine (Thr131-->Ile) is associated with several pulmonary diseases.
12356334	3	58	theme	8	495:495	arg1	kDa					497:499	kDa	497:499	kDa	497:499	The SP-B precursor (42 kDa) undergoes post-translational processing to generate an 8 kDa mature SP-B.
12356334	0	59	from	position	144:151	arg1	polymorphism					128:139	the single-nucleotide polymorphism	106:139	the single-nucleotide polymorphism at position 1580	106:156	Differences in N-linked glycosylation between human surfactant protein-B variants of the C or T allele at the single-nucleotide polymorphism at position 1580: implications for disease.
12356334	6	60	theme	SP-B	1121:1124	arg1	version					1110:1116	each version	1105:1116	each version of SP-B	1105:1124	To determine whether the C allele SP-B variant is indeed glycosylated at Asn(129)-Gln-Thr131, we first generated stably transfected Chinese hamster ovary cell lines that expressed each version of SP-B, and developed specific SP-B polyclonal anti-peptide antibodies.
12356334	9	61	from	studies	1644:1650	arg1	systems					1663:1669	disease systems	1655:1669	disease systems associated with this SNP	1655:1694	Given its association with several pulmonary diseases, this finding provides useful information for future studies in disease systems associated with this SNP.
12356334	7	62	theme	C	1282:1282	arg1	variant					1291:1297	the C allele variant	1278:1297	the C allele variant	1278:1297	Using both the stably transfected cell lines and fetal lung explants, we observed that the C allele variant is indeed glycosylated at the Asn129-Gln-Thr131 site, whereas the T allele variant, which served as a control, is not.
12356334	10	63	link	N-linked	1801:1808	arg1	glycosylation					1810:1822	N-linked glycosylation	1801:1822	N-linked glycosylation at residue Asn129	1801:1840	Further, we speculate that, given the fact that this SNP is found frequently in the general population, N-linked glycosylation at residue Asn129 interferes with SP-B processing, secretion and folding under certain disease conditions.
12356334	5	64	from	that	893:896	arg1	present					828:834	present	828:834	present	828:834	The Thr131-->Ile substitution can eliminate a potential N-linked glycosylation site, Asn129-Gln-Thr131, which is present in the SP-B variant of the C allele (ACT/Thr) but not in that of the T allele (ATT/Ile).
12356334	10	65	theme	general	1781:1787	arg1	population					1789:1798	the general population	1777:1798	the general population	1777:1798	Further, we speculate that, given the fact that this SNP is found frequently in the general population, N-linked glycosylation at residue Asn129 interferes with SP-B processing, secretion and folding under certain disease conditions.
12356334	0	66	theme	single-nucleotide	110:126	arg1	polymorphism					128:139	the single-nucleotide polymorphism	106:139	the single-nucleotide polymorphism at position 1580	106:156	Differences in N-linked glycosylation between human surfactant protein-B variants of the C or T allele at the single-nucleotide polymorphism at position 1580: implications for disease.
12356334	3	67	theme	mature	501:506	arg1	SP-B					508:511	an 8 kDa mature SP-B	492:511	an 8 kDa mature SP-B	492:511	The SP-B precursor (42 kDa) undergoes post-translational processing to generate an 8 kDa mature SP-B.
12356334	1	68	theme	surfactant	191:200	arg1	protein-B					202:210	Human surfactant protein-B	185:210	Human surfactant protein-B (SP-B)	185:217	Human surfactant protein-B (SP-B), a hydrophobic protein, is essential for normal lung function.
12356334	1	68	theme	surfactant	191:200	arg1	protein					234:240	a hydrophobic protein	220:240	a hydrophobic protein	220:240	Human surfactant protein-B (SP-B), a hydrophobic protein, is essential for normal lung function.
12356334	1	68	theme	surfactant	191:200	arg1	SP-B					213:216	SP-B	213:216	SP-B	213:216	Human surfactant protein-B (SP-B), a hydrophobic protein, is essential for normal lung function.
12356334	5	69	theme	N-linked	771:778	arg1	present					828:834	present	828:834	present	828:834	The Thr131-->Ile substitution can eliminate a potential N-linked glycosylation site, Asn129-Gln-Thr131, which is present in the SP-B variant of the C allele (ACT/Thr) but not in that of the T allele (ATT/Ile).
12356334	5	69	theme	N-linked	771:778	arg1	Asn129-Gln-Thr131					800:816	Asn129-Gln-Thr131	800:816	Asn129-Gln-Thr131	800:816	The Thr131-->Ile substitution can eliminate a potential N-linked glycosylation site, Asn129-Gln-Thr131, which is present in the SP-B variant of the C allele (ACT/Thr) but not in that of the T allele (ATT/Ile).
12356334	5	69	theme	N-linked	771:778	arg1	site					794:797	a potential N-linked glycosylation site	759:797	a potential N-linked glycosylation site	759:797	The Thr131-->Ile substitution can eliminate a potential N-linked glycosylation site, Asn129-Gln-Thr131, which is present in the SP-B variant of the C allele (ACT/Thr) but not in that of the T allele (ATT/Ile).
12356334	9	70	theme	several	1564:1570	arg1	diseases					1582:1589	several pulmonary diseases	1564:1589	several pulmonary diseases	1564:1589	Given its association with several pulmonary diseases, this finding provides useful information for future studies in disease systems associated with this SNP.
12356334	7	71	theme	fetal	1240:1244	arg1	explants					1251:1258	fetal lung explants	1240:1258	fetal lung explants	1240:1258	Using both the stably transfected cell lines and fetal lung explants, we observed that the C allele variant is indeed glycosylated at the Asn129-Gln-Thr131 site, whereas the T allele variant, which served as a control, is not.
12356334	6	72	theme	polyclonal	1155:1164	arg1	antibodies					1179:1188	specific SP-B polyclonal anti-peptide antibodies	1141:1188	specific SP-B polyclonal anti-peptide antibodies	1141:1188	To determine whether the C allele SP-B variant is indeed glycosylated at Asn(129)-Gln-Thr131, we first generated stably transfected Chinese hamster ovary cell lines that expressed each version of SP-B, and developed specific SP-B polyclonal anti-peptide antibodies.
12356334	6	73	theme	hamster	1065:1071	arg1	lines					1084:1088	stably transfected Chinese hamster ovary cell lines	1038:1088	stably transfected Chinese hamster ovary cell lines that expressed each version of SP-B, and developed specific SP-B polyclonal anti-peptide antibodies	1038:1188	To determine whether the C allele SP-B variant is indeed glycosylated at Asn(129)-Gln-Thr131, we first generated stably transfected Chinese hamster ovary cell lines that expressed each version of SP-B, and developed specific SP-B polyclonal anti-peptide antibodies.
12356334	8	74	link	N-linked	1489:1496	arg1	site					1512:1515	another N-linked glycosylation site	1481:1515	another N-linked glycosylation site	1481:1515	In addition, we also confirmed that both SP-B variants contain another N-linked glycosylation site, Asn311-Ser-Ser313.
12356334	8	74	link	N-linked	1489:1496	arg1	Asn311-Ser-Ser313					1518:1534	Asn311-Ser-Ser313	1518:1534	Asn311-Ser-Ser313	1518:1534	In addition, we also confirmed that both SP-B variants contain another N-linked glycosylation site, Asn311-Ser-Ser313.
12356334	8	75	contain	contain	1473:1479	arg2	Asn311-Ser-Ser313					1518:1534	Asn311-Ser-Ser313	1518:1534	Asn311-Ser-Ser313	1518:1534	In addition, we also confirmed that both SP-B variants contain another N-linked glycosylation site, Asn311-Ser-Ser313.
12356334	8	75	contain	contain	1473:1479	arg1	variants					1464:1471	both SP-B variants	1454:1471	both SP-B variants	1454:1471	In addition, we also confirmed that both SP-B variants contain another N-linked glycosylation site, Asn311-Ser-Ser313.
12356334	8	75	contain	contain	1473:1479	arg2	site					1512:1515	another N-linked glycosylation site	1481:1515	another N-linked glycosylation site	1481:1515	In addition, we also confirmed that both SP-B variants contain another N-linked glycosylation site, Asn311-Ser-Ser313.
12356334	7	76	theme	transfected	1213:1223	arg1	lines					1230:1234	the stably transfected cell lines	1202:1234	the stably transfected cell lines	1202:1234	Using both the stably transfected cell lines and fetal lung explants, we observed that the C allele variant is indeed glycosylated at the Asn129-Gln-Thr131 site, whereas the T allele variant, which served as a control, is not.
12356334	0	77	theme	C	89:89	arg1	allele					96:101	the C or T allele	85:101	allele	96:101	Differences in N-linked glycosylation between human surfactant protein-B variants of the C or T allele at the single-nucleotide polymorphism at position 1580: implications for disease.
12356334	5	78	link	N-linked	771:778	arg1	present					828:834	present	828:834	present	828:834	The Thr131-->Ile substitution can eliminate a potential N-linked glycosylation site, Asn129-Gln-Thr131, which is present in the SP-B variant of the C allele (ACT/Thr) but not in that of the T allele (ATT/Ile).
12356334	5	78	link	N-linked	771:778	arg1	Asn129-Gln-Thr131					800:816	Asn129-Gln-Thr131	800:816	Asn129-Gln-Thr131	800:816	The Thr131-->Ile substitution can eliminate a potential N-linked glycosylation site, Asn129-Gln-Thr131, which is present in the SP-B variant of the C allele (ACT/Thr) but not in that of the T allele (ATT/Ile).
12356334	5	78	link	N-linked	771:778	arg1	site					794:797	a potential N-linked glycosylation site	759:797	a potential N-linked glycosylation site	759:797	The Thr131-->Ile substitution can eliminate a potential N-linked glycosylation site, Asn129-Gln-Thr131, which is present in the SP-B variant of the C allele (ACT/Thr) but not in that of the T allele (ATT/Ile).
12356334	4	79	theme	amino	609:613	arg1	acid					615:618	amino acid 131	609:622	amino acid 131	609:622	A single-nucleotide polymorphism (SNP) at nucleotide 1580 (C/T) in exon 4 of SP-B that changes amino acid 131 from threonine to isoleucine (Thr131-->Ile) is associated with several pulmonary diseases.
12356334	0	80	theme	T	94:94	arg1	allele					96:101	the C or T allele	85:101	allele	96:101	Differences in N-linked glycosylation between human surfactant protein-B variants of the C or T allele at the single-nucleotide polymorphism at position 1580: implications for disease.
12356334	10	81	gly	glycosylation	1810:1822	arg2	residue					1827:1833	residue Asn129	1827:1840	residue Asn129	1827:1840	Further, we speculate that, given the fact that this SNP is found frequently in the general population, N-linked glycosylation at residue Asn129 interferes with SP-B processing, secretion and folding under certain disease conditions.
12356334	10	81	gly	glycosylation	1810:1822	arg1	residue					1827:1833	residue Asn129	1827:1840	residue Asn129	1827:1840	Further, we speculate that, given the fact that this SNP is found frequently in the general population, N-linked glycosylation at residue Asn129 interferes with SP-B processing, secretion and folding under certain disease conditions.
12356334	10	82	theme	SP-B	1858:1861	arg1	processing					1863:1872	SP-B processing	1858:1872	SP-B processing	1858:1872	Further, we speculate that, given the fact that this SNP is found frequently in the general population, N-linked glycosylation at residue Asn129 interferes with SP-B processing, secretion and folding under certain disease conditions.
12356334	4	83	from	polymorphism	534:545	arg1	exon					581:584	exon 4	581:586	exon 4 of SP-B	581:594	A single-nucleotide polymorphism (SNP) at nucleotide 1580 (C/T) in exon 4 of SP-B that changes amino acid 131 from threonine to isoleucine (Thr131-->Ile) is associated with several pulmonary diseases.
12356334	7	84	gly	glycosylated	1309:1320	arg2	site					1347:1350	the Asn129-Gln-Thr131 site	1325:1350	the Asn129-Gln-Thr131 site	1325:1350	Using both the stably transfected cell lines and fetal lung explants, we observed that the C allele variant is indeed glycosylated at the Asn129-Gln-Thr131 site, whereas the T allele variant, which served as a control, is not.
12356334	7	84	gly	glycosylated	1309:1320	arg1	variant					1291:1297	the C allele variant	1278:1297	the C allele variant	1278:1297	Using both the stably transfected cell lines and fetal lung explants, we observed that the C allele variant is indeed glycosylated at the Asn129-Gln-Thr131 site, whereas the T allele variant, which served as a control, is not.
12356334	6	85	theme	allele	952:957	arg1	variant					964:970	the C allele SP-B variant	946:970	the C allele SP-B variant	946:970	To determine whether the C allele SP-B variant is indeed glycosylated at Asn(129)-Gln-Thr131, we first generated stably transfected Chinese hamster ovary cell lines that expressed each version of SP-B, and developed specific SP-B polyclonal anti-peptide antibodies.
12356334	9	86	theme	future	1637:1642	arg1	studies					1644:1650	future studies	1637:1650	future studies in disease systems associated with this SNP	1637:1694	Given its association with several pulmonary diseases, this finding provides useful information for future studies in disease systems associated with this SNP.
12356334	5	87	theme	Thr131-->Ile	719:730	arg1	substitution					732:743	The Thr131-->Ile substitution	715:743	The Thr131-->Ile substitution	715:743	The Thr131-->Ile substitution can eliminate a potential N-linked glycosylation site, Asn129-Gln-Thr131, which is present in the SP-B variant of the C allele (ACT/Thr) but not in that of the T allele (ATT/Ile).
12356334	5	88	located	present	828:834	arg2	Asn129-Gln-Thr131					800:816	Asn129-Gln-Thr131	800:816	Asn129-Gln-Thr131	800:816	The Thr131-->Ile substitution can eliminate a potential N-linked glycosylation site, Asn129-Gln-Thr131, which is present in the SP-B variant of the C allele (ACT/Thr) but not in that of the T allele (ATT/Ile).
12356334	5	88	located	present	828:834	arg1	variant					848:854	the SP-B variant	839:854	the SP-B variant of the C allele (ACT/Thr)	839:880	The Thr131-->Ile substitution can eliminate a potential N-linked glycosylation site, Asn129-Gln-Thr131, which is present in the SP-B variant of the C allele (ACT/Thr) but not in that of the T allele (ATT/Ile).
12356334	5	88	located	present	828:834	arg2	site					794:797	a potential N-linked glycosylation site	759:797	a potential N-linked glycosylation site	759:797	The Thr131-->Ile substitution can eliminate a potential N-linked glycosylation site, Asn129-Gln-Thr131, which is present in the SP-B variant of the C allele (ACT/Thr) but not in that of the T allele (ATT/Ile).
12356334	5	88	located	present	828:834	arg2	present					828:834	present	828:834	present	828:834	The Thr131-->Ile substitution can eliminate a potential N-linked glycosylation site, Asn129-Gln-Thr131, which is present in the SP-B variant of the C allele (ACT/Thr) but not in that of the T allele (ATT/Ile).
12356334	2	89	theme	respiratory	388:398	arg1	epithelium					400:409	the respiratory epithelium	384:409	the respiratory epithelium	384:409	SP-B is expressed and secreted by specific lung cell types, i.e. alveolar type II and Clara cells, of the respiratory epithelium.
12356334	1	90	theme	normal	260:265	arg1	function					272:279	normal lung function	260:279	normal lung function	260:279	Human surfactant protein-B (SP-B), a hydrophobic protein, is essential for normal lung function.
12356334	5	91	theme	allele	865:870	arg1	variant					848:854	the SP-B variant	839:854	the SP-B variant of the C allele (ACT/Thr)	839:880	The Thr131-->Ile substitution can eliminate a potential N-linked glycosylation site, Asn129-Gln-Thr131, which is present in the SP-B variant of the C allele (ACT/Thr) but not in that of the T allele (ATT/Ile).
12356334	9	92	with	association	1547:1557	arg1	diseases					1582:1589	several pulmonary diseases	1564:1589	several pulmonary diseases	1564:1589	Given its association with several pulmonary diseases, this finding provides useful information for future studies in disease systems associated with this SNP.
12356334	0	93	theme	human	46:50	arg1	variants					73:80	human surfactant protein-B variants	46:80	human surfactant protein-B variants of the C or T allele at the single-nucleotide polymorphism at position 1580	46:156	Differences in N-linked glycosylation between human surfactant protein-B variants of the C or T allele at the single-nucleotide polymorphism at position 1580: implications for disease.
12356334	5	94	theme	T	905:905	arg1	allele					907:912	the T allele	901:912	the T allele (ATT/Ile)	901:922	The Thr131-->Ile substitution can eliminate a potential N-linked glycosylation site, Asn129-Gln-Thr131, which is present in the SP-B variant of the C allele (ACT/Thr) but not in that of the T allele (ATT/Ile).
12356334	5	94	theme	T	905:905	arg1	ATT/Ile					915:921	ATT/Ile	915:921	ATT/Ile	915:921	The Thr131-->Ile substitution can eliminate a potential N-linked glycosylation site, Asn129-Gln-Thr131, which is present in the SP-B variant of the C allele (ACT/Thr) but not in that of the T allele (ATT/Ile).
12356334	0	95	theme	protein-B	63:71	arg1	variants					73:80	human surfactant protein-B variants	46:80	human surfactant protein-B variants of the C or T allele at the single-nucleotide polymorphism at position 1580	46:156	Differences in N-linked glycosylation between human surfactant protein-B variants of the C or T allele at the single-nucleotide polymorphism at position 1580: implications for disease.
12356334	7	96	theme	allele	1367:1372	arg1	control					1401:1407	a control	1399:1407	a control	1399:1407	Using both the stably transfected cell lines and fetal lung explants, we observed that the C allele variant is indeed glycosylated at the Asn129-Gln-Thr131 site, whereas the T allele variant, which served as a control, is not.
12356334	7	96	theme	allele	1367:1372	arg1	variant					1374:1380	the T allele variant	1361:1380	the T allele variant	1361:1380	Using both the stably transfected cell lines and fetal lung explants, we observed that the C allele variant is indeed glycosylated at the Asn129-Gln-Thr131 site, whereas the T allele variant, which served as a control, is not.
12356334	4	97	theme	pulmonary	695:703	arg1	diseases					705:712	several pulmonary diseases	687:712	several pulmonary diseases	687:712	A single-nucleotide polymorphism (SNP) at nucleotide 1580 (C/T) in exon 4 of SP-B that changes amino acid 131 from threonine to isoleucine (Thr131-->Ile) is associated with several pulmonary diseases.
12356334	8	98	theme	N-linked	1489:1496	arg1	site					1512:1515	another N-linked glycosylation site	1481:1515	another N-linked glycosylation site	1481:1515	In addition, we also confirmed that both SP-B variants contain another N-linked glycosylation site, Asn311-Ser-Ser313.
12356334	8	98	theme	N-linked	1489:1496	arg1	Asn311-Ser-Ser313					1518:1534	Asn311-Ser-Ser313	1518:1534	Asn311-Ser-Ser313	1518:1534	In addition, we also confirmed that both SP-B variants contain another N-linked glycosylation site, Asn311-Ser-Ser313.
12356334	2	99	dep	type	356:359	arg1	i.e.					342:345	i.e.	342:345	i.e.	342:345	SP-B is expressed and secreted by specific lung cell types, i.e. alveolar type II and Clara cells, of the respiratory epithelium.
12356334	1	100	theme	hydrophobic	222:232	arg1	protein-B					202:210	Human surfactant protein-B	185:210	Human surfactant protein-B (SP-B)	185:217	Human surfactant protein-B (SP-B), a hydrophobic protein, is essential for normal lung function.
12356334	1	100	theme	hydrophobic	222:232	arg1	protein					234:240	a hydrophobic protein	220:240	a hydrophobic protein	220:240	Human surfactant protein-B (SP-B), a hydrophobic protein, is essential for normal lung function.
11595658	6	0	dep	mutants	829:835	arg1	mutants					829:835	the double mutants A40/A47 and A80/A100	818:856	the double mutants A40/A47 and A80/A100	818:856	The single mutants Q38, Q45, Q78, Q90, Q98, A40, A47, A80, A92, and A100 and the double mutants A40/A47 and A80/A100 were well expressed, bound CRF, sauvagine (SVG), and urotensin-I (UTS-I) with a normal affinity, and increased cAMP accumulation with a high efficiency.
11595658	6	0	dep	mutants	829:835	arg1	A80/A100					849:856	A80/A100	849:856	A80/A100	849:856	The single mutants Q38, Q45, Q78, Q90, Q98, A40, A47, A80, A92, and A100 and the double mutants A40/A47 and A80/A100 were well expressed, bound CRF, sauvagine (SVG), and urotensin-I (UTS-I) with a normal affinity, and increased cAMP accumulation with a high efficiency.
11595658	6	0	dep	mutants	829:835	arg1	A40/A47					837:843	A40/A47	837:843	A40/A47	837:843	The single mutants Q38, Q45, Q78, Q90, Q98, A40, A47, A80, A92, and A100 and the double mutants A40/A47 and A80/A100 were well expressed, bound CRF, sauvagine (SVG), and urotensin-I (UTS-I) with a normal affinity, and increased cAMP accumulation with a high efficiency.
11595658	0	1	theme	ligand-specific	60:74	arg1	interaction					76:86	its ligand-specific interaction	56:86	its ligand-specific interaction	56:86	N-glycosylation of CRF receptor type 1 is important for its ligand-specific interaction.
11595658	4	2	theme	polysaccharide	465:478	arg1	chain					480:484	polysaccharide chain	465:484	the polysaccharide chain(s)	461:487	To determine which of the polysaccharide chain(s) is/are involved in ligand interaction, the polysaccharide chains were deleted using site-directed mutagenesis of the glycosylation consensus, N-X-S/T.
11595658	6	3	theme	single	745:750	arg1	A47					790:792	A47	790:792	A47	790:792	The single mutants Q38, Q45, Q78, Q90, Q98, A40, A47, A80, A92, and A100 and the double mutants A40/A47 and A80/A100 were well expressed, bound CRF, sauvagine (SVG), and urotensin-I (UTS-I) with a normal affinity, and increased cAMP accumulation with a high efficiency.
11595658	6	3	theme	single	745:750	arg1	mutants					752:758	The single mutants	741:758	The single mutants Q38, Q45, Q78, Q90, Q98, A40, A47, A80, A92, and A100	741:812	The single mutants Q38, Q45, Q78, Q90, Q98, A40, A47, A80, A92, and A100 and the double mutants A40/A47 and A80/A100 were well expressed, bound CRF, sauvagine (SVG), and urotensin-I (UTS-I) with a normal affinity, and increased cAMP accumulation with a high efficiency.
11595658	6	3	theme	single	745:750	arg1	A100					809:812	A100	809:812	A100	809:812	The single mutants Q38, Q45, Q78, Q90, Q98, A40, A47, A80, A92, and A100 and the double mutants A40/A47 and A80/A100 were well expressed, bound CRF, sauvagine (SVG), and urotensin-I (UTS-I) with a normal affinity, and increased cAMP accumulation with a high efficiency.
11595658	6	3	theme	single	745:750	arg1	Q45					765:767	Q45	765:767	Q45	765:767	The single mutants Q38, Q45, Q78, Q90, Q98, A40, A47, A80, A92, and A100 and the double mutants A40/A47 and A80/A100 were well expressed, bound CRF, sauvagine (SVG), and urotensin-I (UTS-I) with a normal affinity, and increased cAMP accumulation with a high efficiency.
11595658	6	3	theme	single	745:750	arg1	Q98					780:782	Q98	780:782	Q98	780:782	The single mutants Q38, Q45, Q78, Q90, Q98, A40, A47, A80, A92, and A100 and the double mutants A40/A47 and A80/A100 were well expressed, bound CRF, sauvagine (SVG), and urotensin-I (UTS-I) with a normal affinity, and increased cAMP accumulation with a high efficiency.
11595658	6	3	theme	single	745:750	arg1	A40					785:787	A40	785:787	A40	785:787	The single mutants Q38, Q45, Q78, Q90, Q98, A40, A47, A80, A92, and A100 and the double mutants A40/A47 and A80/A100 were well expressed, bound CRF, sauvagine (SVG), and urotensin-I (UTS-I) with a normal affinity, and increased cAMP accumulation with a high efficiency.
11595658	6	3	theme	single	745:750	arg1	A92					800:802	A92	800:802	A92	800:802	The single mutants Q38, Q45, Q78, Q90, Q98, A40, A47, A80, A92, and A100 and the double mutants A40/A47 and A80/A100 were well expressed, bound CRF, sauvagine (SVG), and urotensin-I (UTS-I) with a normal affinity, and increased cAMP accumulation with a high efficiency.
11595658	6	3	theme	single	745:750	arg1	Q90					775:777	Q90	775:777	Q90	775:777	The single mutants Q38, Q45, Q78, Q90, Q98, A40, A47, A80, A92, and A100 and the double mutants A40/A47 and A80/A100 were well expressed, bound CRF, sauvagine (SVG), and urotensin-I (UTS-I) with a normal affinity, and increased cAMP accumulation with a high efficiency.
11595658	7	4	contain	had	1168:1170	arg2	stimulation					1189:1199	a decreased cAMP stimulation	1172:1199	a decreased cAMP stimulation	1172:1199	In contrast, the combined mutations A80/A92/A100, A40/A80/A92/A100, and A40/A47/A80/A92/A100 had low levels of expression, did not bind the radioligand, and had a decreased cAMP stimulation.
11595658	7	4	contain	had	1168:1170	arg1	mutations					1037:1045	the combined mutations	1024:1045	the combined mutations A80/A92/A100, A40/A80/A92/A100, and A40/A47/A80/A92/A100	1024:1102	In contrast, the combined mutations A80/A92/A100, A40/A80/A92/A100, and A40/A47/A80/A92/A100 had low levels of expression, did not bind the radioligand, and had a decreased cAMP stimulation.
11595658	7	4	contain	had	1168:1170	arg1	A40/A80/A92/A100					1061:1076	A40/A80/A92/A100	1061:1076	A40/A80/A92/A100	1061:1076	In contrast, the combined mutations A80/A92/A100, A40/A80/A92/A100, and A40/A47/A80/A92/A100 had low levels of expression, did not bind the radioligand, and had a decreased cAMP stimulation.
11595658	7	4	contain	had	1168:1170	arg1	A40/A47/A80/A92/A100					1083:1102	A40/A47/A80/A92/A100	1083:1102	A40/A47/A80/A92/A100	1083:1102	In contrast, the combined mutations A80/A92/A100, A40/A80/A92/A100, and A40/A47/A80/A92/A100 had low levels of expression, did not bind the radioligand, and had a decreased cAMP stimulation.
11595658	7	4	contain	had	1168:1170	arg1	A80/A92/A100					1047:1058	A80/A92/A100	1047:1058	A80/A92/A100	1047:1058	In contrast, the combined mutations A80/A92/A100, A40/A80/A92/A100, and A40/A47/A80/A92/A100 had low levels of expression, did not bind the radioligand, and had a decreased cAMP stimulation.
11595658	3	5	dep	CRF	434:436	arg1	response					422:429	response	422:429	response	422:429	The nonglycosylated receptor did not bind the radioligand and had a decreased cAMP stimulation potency in response to CRF.
11595658	4	6	theme	consensus	620:628	arg1	N-X-S/T					631:637	the glycosylation consensus, N-X-S/T	602:637	N-X-S/T	631:637	To determine which of the polysaccharide chain(s) is/are involved in ligand interaction, the polysaccharide chains were deleted using site-directed mutagenesis of the glycosylation consensus, N-X-S/T.
11595658	4	7	theme	polysaccharide	532:545	arg1	chains					547:552	the polysaccharide chains	528:552	the polysaccharide chains	528:552	To determine which of the polysaccharide chain(s) is/are involved in ligand interaction, the polysaccharide chains were deleted using site-directed mutagenesis of the glycosylation consensus, N-X-S/T.
11595658	3	8	theme	nonglycosylated	320:334	arg1	receptor					336:343	The nonglycosylated receptor	316:343	The nonglycosylated receptor	316:343	The nonglycosylated receptor did not bind the radioligand and had a decreased cAMP stimulation potency in response to CRF.
11595658	3	9	contain	had	378:380	arg1	receptor					336:343	The nonglycosylated receptor	316:343	The nonglycosylated receptor	316:343	The nonglycosylated receptor did not bind the radioligand and had a decreased cAMP stimulation potency in response to CRF.
11595658	3	9	contain	had	378:380	arg2	potency					411:417	a decreased cAMP stimulation potency	382:417	a decreased cAMP stimulation potency	382:417	The nonglycosylated receptor did not bind the radioligand and had a decreased cAMP stimulation potency in response to CRF.
11595658	6	10	theme	normal	938:943	arg1	affinity					945:952	a normal affinity	936:952	a normal affinity	936:952	The single mutants Q38, Q45, Q78, Q90, Q98, A40, A47, A80, A92, and A100 and the double mutants A40/A47 and A80/A100 were well expressed, bound CRF, sauvagine (SVG), and urotensin-I (UTS-I) with a normal affinity, and increased cAMP accumulation with a high efficiency.
11595658	5	11	dep	A	724:724	arg1	to					721:722	to	721:722	to	721:722	Two sets of mutations were performed for each glycosylation site: N to Q and S/T to A, respectively.
11595658	7	12	theme	expression	1122:1131	arg1	levels					1112:1117	low levels	1108:1117	low levels of expression	1108:1131	In contrast, the combined mutations A80/A92/A100, A40/A80/A92/A100, and A40/A47/A80/A92/A100 had low levels of expression, did not bind the radioligand, and had a decreased cAMP stimulation.
11595658	6	13	dep	sauvagine	890:898	arg1	SVG					901:903	SVG	901:903	SVG	901:903	The single mutants Q38, Q45, Q78, Q90, Q98, A40, A47, A80, A92, and A100 and the double mutants A40/A47 and A80/A100 were well expressed, bound CRF, sauvagine (SVG), and urotensin-I (UTS-I) with a normal affinity, and increased cAMP accumulation with a high efficiency.
11595658	3	14	theme	cAMP	394:397	arg1	potency					411:417	a decreased cAMP stimulation potency	382:417	a decreased cAMP stimulation potency	382:417	The nonglycosylated receptor did not bind the radioligand and had a decreased cAMP stimulation potency in response to CRF.
11595658	7	15	contain	had	1104:1106	arg1	mutations					1037:1045	the combined mutations	1024:1045	the combined mutations A80/A92/A100, A40/A80/A92/A100, and A40/A47/A80/A92/A100	1024:1102	In contrast, the combined mutations A80/A92/A100, A40/A80/A92/A100, and A40/A47/A80/A92/A100 had low levels of expression, did not bind the radioligand, and had a decreased cAMP stimulation.
11595658	7	15	contain	had	1104:1106	arg1	A40/A80/A92/A100					1061:1076	A40/A80/A92/A100	1061:1076	A40/A80/A92/A100	1061:1076	In contrast, the combined mutations A80/A92/A100, A40/A80/A92/A100, and A40/A47/A80/A92/A100 had low levels of expression, did not bind the radioligand, and had a decreased cAMP stimulation.
11595658	7	15	contain	had	1104:1106	arg1	A40/A47/A80/A92/A100					1083:1102	A40/A47/A80/A92/A100	1083:1102	A40/A47/A80/A92/A100	1083:1102	In contrast, the combined mutations A80/A92/A100, A40/A80/A92/A100, and A40/A47/A80/A92/A100 had low levels of expression, did not bind the radioligand, and had a decreased cAMP stimulation.
11595658	7	15	contain	had	1104:1106	arg1	A80/A92/A100					1047:1058	A80/A92/A100	1047:1058	A80/A92/A100	1047:1058	In contrast, the combined mutations A80/A92/A100, A40/A80/A92/A100, and A40/A47/A80/A92/A100 had low levels of expression, did not bind the radioligand, and had a decreased cAMP stimulation.
11595658	7	15	contain	had	1104:1106	arg2	levels					1112:1117	low levels	1108:1117	low levels of expression	1108:1131	In contrast, the combined mutations A80/A92/A100, A40/A80/A92/A100, and A40/A47/A80/A92/A100 had low levels of expression, did not bind the radioligand, and had a decreased cAMP stimulation.
11595658	1	16	gly	N-glycosylation	178:192	arg2	N38					201:203	N38	201:203	N38	201:203	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	16	gly	N-glycosylation	178:192	arg2	N98					225:227	N98	225:227	N98	225:227	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	16	gly	N-glycosylation	178:192	arg2	N90					216:218	N90	216:218	N90	216:218	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	16	gly	N-glycosylation	178:192	arg2	N45					206:208	N45	206:208	N45	206:208	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	16	gly	N-glycosylation	178:192	arg2	five					163:166	five	163:166	five	163:166	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	16	gly	N-glycosylation	178:192	arg2	sites					194:198	five potential N-glycosylation sites	163:198	five potential N-glycosylation sites: N38, N45, N78, N90, and N98	163:227	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	16	gly	N-glycosylation	178:192	arg2	N78					211:213	N78	211:213	N78	211:213	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	6	17	theme	cAMP	969:972	arg1	accumulation					974:985	cAMP accumulation	969:985	cAMP accumulation	969:985	The single mutants Q38, Q45, Q78, Q90, Q98, A40, A47, A80, A92, and A100 and the double mutants A40/A47 and A80/A100 were well expressed, bound CRF, sauvagine (SVG), and urotensin-I (UTS-I) with a normal affinity, and increased cAMP accumulation with a high efficiency.
11595658	3	18	theme	stimulation	399:409	arg1	potency					411:417	a decreased cAMP stimulation potency	382:417	a decreased cAMP stimulation potency	382:417	The nonglycosylated receptor did not bind the radioligand and had a decreased cAMP stimulation potency in response to CRF.
11595658	4	19	dep	is/are	489:494	arg1	involved					496:503	involved	496:503	is/are involved in ligand interaction	489:525	To determine which of the polysaccharide chain(s) is/are involved in ligand interaction, the polysaccharide chains were deleted using site-directed mutagenesis of the glycosylation consensus, N-X-S/T.
11595658	6	20	theme	double	822:827	arg1	mutants					829:835	the double mutants A40/A47 and A80/A100	818:856	the double mutants A40/A47 and A80/A100	818:856	The single mutants Q38, Q45, Q78, Q90, Q98, A40, A47, A80, A92, and A100 and the double mutants A40/A47 and A80/A100 were well expressed, bound CRF, sauvagine (SVG), and urotensin-I (UTS-I) with a normal affinity, and increased cAMP accumulation with a high efficiency.
11595658	6	20	theme	double	822:827	arg1	A80/A100					849:856	A80/A100	849:856	A80/A100	849:856	The single mutants Q38, Q45, Q78, Q90, Q98, A40, A47, A80, A92, and A100 and the double mutants A40/A47 and A80/A100 were well expressed, bound CRF, sauvagine (SVG), and urotensin-I (UTS-I) with a normal affinity, and increased cAMP accumulation with a high efficiency.
11595658	6	20	theme	double	822:827	arg1	A40/A47					837:843	A40/A47	837:843	A40/A47	837:843	The single mutants Q38, Q45, Q78, Q90, Q98, A40, A47, A80, A92, and A100 and the double mutants A40/A47 and A80/A100 were well expressed, bound CRF, sauvagine (SVG), and urotensin-I (UTS-I) with a normal affinity, and increased cAMP accumulation with a high efficiency.
11595658	5	21	gly	glycosylation	686:698	arg2	site					700:703	each glycosylation site	681:703	each glycosylation site	681:703	Two sets of mutations were performed for each glycosylation site: N to Q and S/T to A, respectively.
11595658	4	22	theme	N-X-S/T	631:637	arg1	mutagenesis					587:597	site-directed mutagenesis	573:597	site-directed mutagenesis of the glycosylation consensus, N-X-S/T	573:637	To determine which of the polysaccharide chain(s) is/are involved in ligand interaction, the polysaccharide chains were deleted using site-directed mutagenesis of the glycosylation consensus, N-X-S/T.
11595658	5	23	dep	Q	711:711	arg1	to					708:709	to	708:709	to	708:709	Two sets of mutations were performed for each glycosylation site: N to Q and S/T to A, respectively.
11595658	7	24	dep	mutations	1037:1045	arg1	mutations					1037:1045	the combined mutations	1024:1045	the combined mutations A80/A92/A100, A40/A80/A92/A100, and A40/A47/A80/A92/A100	1024:1102	In contrast, the combined mutations A80/A92/A100, A40/A80/A92/A100, and A40/A47/A80/A92/A100 had low levels of expression, did not bind the radioligand, and had a decreased cAMP stimulation.
11595658	7	24	dep	mutations	1037:1045	arg1	A40/A80/A92/A100					1061:1076	A40/A80/A92/A100	1061:1076	A40/A80/A92/A100	1061:1076	In contrast, the combined mutations A80/A92/A100, A40/A80/A92/A100, and A40/A47/A80/A92/A100 had low levels of expression, did not bind the radioligand, and had a decreased cAMP stimulation.
11595658	7	24	dep	mutations	1037:1045	arg1	A40/A47/A80/A92/A100					1083:1102	A40/A47/A80/A92/A100	1083:1102	A40/A47/A80/A92/A100	1083:1102	In contrast, the combined mutations A80/A92/A100, A40/A80/A92/A100, and A40/A47/A80/A92/A100 had low levels of expression, did not bind the radioligand, and had a decreased cAMP stimulation.
11595658	7	24	dep	mutations	1037:1045	arg1	A80/A92/A100					1047:1058	A80/A92/A100	1047:1058	A80/A92/A100	1047:1058	In contrast, the combined mutations A80/A92/A100, A40/A80/A92/A100, and A40/A47/A80/A92/A100 had low levels of expression, did not bind the radioligand, and had a decreased cAMP stimulation.
11595658	3	25	theme	decreased	384:392	arg1	potency					411:417	a decreased cAMP stimulation potency	382:417	a decreased cAMP stimulation potency	382:417	The nonglycosylated receptor did not bind the radioligand and had a decreased cAMP stimulation potency in response to CRF.
11595658	0	26	theme	receptor	23:30	arg1	type					32:35	CRF receptor type 1	19:37	CRF receptor type 1	19:37	N-glycosylation of CRF receptor type 1 is important for its ligand-specific interaction.
11595658	6	27	dep	mutants	752:758	arg1	A47					790:792	A47	790:792	A47	790:792	The single mutants Q38, Q45, Q78, Q90, Q98, A40, A47, A80, A92, and A100 and the double mutants A40/A47 and A80/A100 were well expressed, bound CRF, sauvagine (SVG), and urotensin-I (UTS-I) with a normal affinity, and increased cAMP accumulation with a high efficiency.
11595658	6	27	dep	mutants	752:758	arg1	mutants					752:758	The single mutants	741:758	The single mutants Q38, Q45, Q78, Q90, Q98, A40, A47, A80, A92, and A100	741:812	The single mutants Q38, Q45, Q78, Q90, Q98, A40, A47, A80, A92, and A100 and the double mutants A40/A47 and A80/A100 were well expressed, bound CRF, sauvagine (SVG), and urotensin-I (UTS-I) with a normal affinity, and increased cAMP accumulation with a high efficiency.
11595658	6	27	dep	mutants	752:758	arg1	A100					809:812	A100	809:812	A100	809:812	The single mutants Q38, Q45, Q78, Q90, Q98, A40, A47, A80, A92, and A100 and the double mutants A40/A47 and A80/A100 were well expressed, bound CRF, sauvagine (SVG), and urotensin-I (UTS-I) with a normal affinity, and increased cAMP accumulation with a high efficiency.
11595658	6	27	dep	mutants	752:758	arg1	Q45					765:767	Q45	765:767	Q45	765:767	The single mutants Q38, Q45, Q78, Q90, Q98, A40, A47, A80, A92, and A100 and the double mutants A40/A47 and A80/A100 were well expressed, bound CRF, sauvagine (SVG), and urotensin-I (UTS-I) with a normal affinity, and increased cAMP accumulation with a high efficiency.
11595658	6	27	dep	mutants	752:758	arg1	Q98					780:782	Q98	780:782	Q98	780:782	The single mutants Q38, Q45, Q78, Q90, Q98, A40, A47, A80, A92, and A100 and the double mutants A40/A47 and A80/A100 were well expressed, bound CRF, sauvagine (SVG), and urotensin-I (UTS-I) with a normal affinity, and increased cAMP accumulation with a high efficiency.
11595658	6	27	dep	mutants	752:758	arg1	A40					785:787	A40	785:787	A40	785:787	The single mutants Q38, Q45, Q78, Q90, Q98, A40, A47, A80, A92, and A100 and the double mutants A40/A47 and A80/A100 were well expressed, bound CRF, sauvagine (SVG), and urotensin-I (UTS-I) with a normal affinity, and increased cAMP accumulation with a high efficiency.
11595658	6	27	dep	mutants	752:758	arg1	A92					800:802	A92	800:802	A92	800:802	The single mutants Q38, Q45, Q78, Q90, Q98, A40, A47, A80, A92, and A100 and the double mutants A40/A47 and A80/A100 were well expressed, bound CRF, sauvagine (SVG), and urotensin-I (UTS-I) with a normal affinity, and increased cAMP accumulation with a high efficiency.
11595658	6	27	dep	mutants	752:758	arg1	Q90					775:777	Q90	775:777	Q90	775:777	The single mutants Q38, Q45, Q78, Q90, Q98, A40, A47, A80, A92, and A100 and the double mutants A40/A47 and A80/A100 were well expressed, bound CRF, sauvagine (SVG), and urotensin-I (UTS-I) with a normal affinity, and increased cAMP accumulation with a high efficiency.
11595658	3	28	gly	nonglycosylated	320:334	arg1	receptor					336:343	The nonglycosylated receptor	316:343	The nonglycosylated receptor	316:343	The nonglycosylated receptor did not bind the radioligand and had a decreased cAMP stimulation potency in response to CRF.
11595658	1	29	theme	corticotropin-releasing	93:115	arg1	receptor					130:137	The corticotropin-releasing factor (CRF) receptor	89:137	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1)	89:152	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	7	30	theme	decreased	1174:1182	arg1	stimulation					1189:1199	a decreased cAMP stimulation	1172:1199	a decreased cAMP stimulation	1172:1199	In contrast, the combined mutations A80/A92/A100, A40/A80/A92/A100, and A40/A47/A80/A92/A100 had low levels of expression, did not bind the radioligand, and had a decreased cAMP stimulation.
11595658	1	31	theme	N-glycosylation	178:192	arg1	N45					206:208	N45	206:208	N45	206:208	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	31	theme	N-glycosylation	178:192	arg1	N98					225:227	N98	225:227	N98	225:227	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	31	theme	N-glycosylation	178:192	arg1	N78					211:213	N78	211:213	N78	211:213	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	31	theme	N-glycosylation	178:192	arg1	sites					194:198	five potential N-glycosylation sites	163:198	five potential N-glycosylation sites: N38, N45, N78, N90, and N98	163:227	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	31	theme	N-glycosylation	178:192	arg1	N38					201:203	N38	201:203	N38	201:203	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	31	theme	N-glycosylation	178:192	arg1	N90					216:218	N90	216:218	N90	216:218	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	0	32	theme	CRF	19:21	arg1	type					32:35	CRF receptor type 1	19:37	CRF receptor type 1	19:37	N-glycosylation of CRF receptor type 1 is important for its ligand-specific interaction.
11595658	4	33	theme	ligand	508:513	arg1	interaction					515:525	ligand interaction	508:525	ligand interaction	508:525	To determine which of the polysaccharide chain(s) is/are involved in ligand interaction, the polysaccharide chains were deleted using site-directed mutagenesis of the glycosylation consensus, N-X-S/T.
11595658	8	34	theme	polysaccharide	1256:1269	arg1	chains					1271:1276	three or more polysaccharide chains	1242:1276	three or more polysaccharide chains	1242:1276	These data indicate the requirement for three or more polysaccharide chains for normal CRFR1 function.
11595658	1	35	theme	factor	117:122	arg1	receptor					130:137	The corticotropin-releasing factor (CRF) receptor	89:137	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1)	89:152	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	4	36	theme	site-directed	573:585	arg1	mutagenesis					587:597	site-directed mutagenesis	573:597	site-directed mutagenesis of the glycosylation consensus, N-X-S/T	573:637	To determine which of the polysaccharide chain(s) is/are involved in ligand interaction, the polysaccharide chains were deleted using site-directed mutagenesis of the glycosylation consensus, N-X-S/T.
11595658	5	37	theme	S/T	717:719	arg1	A					724:724	S/T to A	717:724	S/T to A	717:724	Two sets of mutations were performed for each glycosylation site: N to Q and S/T to A, respectively.
11595658	0	38	gly	N-glycosylation	0:14	arg1	type					32:35	CRF receptor type 1	19:37	CRF receptor type 1	19:37	N-glycosylation of CRF receptor type 1 is important for its ligand-specific interaction.
11595658	1	39	theme	potential	168:176	arg1	N45					206:208	N45	206:208	N45	206:208	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	39	theme	potential	168:176	arg1	N98					225:227	N98	225:227	N98	225:227	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	39	theme	potential	168:176	arg1	N78					211:213	N78	211:213	N78	211:213	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	39	theme	potential	168:176	arg1	sites					194:198	five potential N-glycosylation sites	163:198	five potential N-glycosylation sites: N38, N45, N78, N90, and N98	163:227	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	39	theme	potential	168:176	arg1	N38					201:203	N38	201:203	N38	201:203	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	39	theme	potential	168:176	arg1	N90					216:218	N90	216:218	N90	216:218	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	7	40	theme	low	1108:1110	arg1	levels					1112:1117	low levels	1108:1117	low levels of expression	1108:1131	In contrast, the combined mutations A80/A92/A100, A40/A80/A92/A100, and A40/A47/A80/A92/A100 had low levels of expression, did not bind the radioligand, and had a decreased cAMP stimulation.
11595658	0	41	theme	type	32:35	arg1	N-glycosylation					0:14	N-glycosylation	0:14	N-glycosylation of CRF receptor type 1	0:37	N-glycosylation of CRF receptor type 1 is important for its ligand-specific interaction.
11595658	1	42	contain	contains	154:161	arg2	N38					201:203	N38	201:203	N38	201:203	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	42	contain	contains	154:161	arg2	N98					225:227	N98	225:227	N98	225:227	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	42	contain	contains	154:161	arg2	N90					216:218	N90	216:218	N90	216:218	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	42	contain	contains	154:161	arg1	type					139:142	The corticotropin-releasing factor (CRF) receptor type 1	89:144	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1)	89:152	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	42	contain	contains	154:161	arg1	CRFR1					147:151	CRFR1	147:151	CRFR1	147:151	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	42	contain	contains	154:161	arg2	N45					206:208	N45	206:208	N45	206:208	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	42	contain	contains	154:161	arg2	sites					194:198	five potential N-glycosylation sites	163:198	five potential N-glycosylation sites: N38, N45, N78, N90, and N98	163:227	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	42	contain	contains	154:161	arg2	N78					211:213	N78	211:213	N78	211:213	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	7	43	theme	cAMP	1184:1187	arg1	stimulation					1189:1199	a decreased cAMP stimulation	1172:1199	a decreased cAMP stimulation	1172:1199	In contrast, the combined mutations A80/A92/A100, A40/A80/A92/A100, and A40/A47/A80/A92/A100 had low levels of expression, did not bind the radioligand, and had a decreased cAMP stimulation.
11595658	4	44	theme	chain	480:484	arg1	s					486:486	the polysaccharide chain(s)	461:487	the polysaccharide chain(s)	461:487	To determine which of the polysaccharide chain(s) is/are involved in ligand interaction, the polysaccharide chains were deleted using site-directed mutagenesis of the glycosylation consensus, N-X-S/T.
11595658	2	45	theme	receptor	292:299	arg1	glycosylation					301:313	receptor glycosylation	292:313	receptor glycosylation	292:313	Cells expressing CRFR1 were treated with tunicamycin to block receptor glycosylation.
11595658	5	46	theme	mutations	652:660	arg1	sets					644:647	Two sets	640:647	Two sets of mutations	640:660	Two sets of mutations were performed for each glycosylation site: N to Q and S/T to A, respectively.
11595658	5	46	theme	mutations	652:660	arg1	mutations					652:660	mutations	652:660	mutations	652:660	Two sets of mutations were performed for each glycosylation site: N to Q and S/T to A, respectively.
11595658	1	47	theme	CRF	125:127	arg1	receptor					130:137	The corticotropin-releasing factor (CRF) receptor	89:137	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1)	89:152	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	6	48	theme	high	994:997	arg1	efficiency					999:1008	a high efficiency	992:1008	a high efficiency	992:1008	The single mutants Q38, Q45, Q78, Q90, Q98, A40, A47, A80, A92, and A100 and the double mutants A40/A47 and A80/A100 were well expressed, bound CRF, sauvagine (SVG), and urotensin-I (UTS-I) with a normal affinity, and increased cAMP accumulation with a high efficiency.
11595658	8	49	theme	CRFR1	1289:1293	arg1	function					1295:1302	normal CRFR1 function	1282:1302	normal CRFR1 function	1282:1302	These data indicate the requirement for three or more polysaccharide chains for normal CRFR1 function.
11595658	1	50	theme	receptor	130:137	arg1	type					139:142	The corticotropin-releasing factor (CRF) receptor type 1	89:144	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1)	89:152	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	50	theme	receptor	130:137	arg1	CRFR1					147:151	CRFR1	147:151	CRFR1	147:151	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	5	51	theme	N	706:706	arg1	Q					711:711	N to Q	706:711	N to Q	706:711	Two sets of mutations were performed for each glycosylation site: N to Q and S/T to A, respectively.
11595658	8	52	theme	normal	1282:1287	arg1	function					1295:1302	normal CRFR1 function	1282:1302	normal CRFR1 function	1282:1302	These data indicate the requirement for three or more polysaccharide chains for normal CRFR1 function.
11595658	4	53	theme	glycosylation	606:618	arg1	N-X-S/T					631:637	the glycosylation consensus, N-X-S/T	602:637	N-X-S/T	631:637	To determine which of the polysaccharide chain(s) is/are involved in ligand interaction, the polysaccharide chains were deleted using site-directed mutagenesis of the glycosylation consensus, N-X-S/T.
11595658	7	54	theme	combined	1028:1035	arg1	mutations					1037:1045	the combined mutations	1024:1045	the combined mutations A80/A92/A100, A40/A80/A92/A100, and A40/A47/A80/A92/A100	1024:1102	In contrast, the combined mutations A80/A92/A100, A40/A80/A92/A100, and A40/A47/A80/A92/A100 had low levels of expression, did not bind the radioligand, and had a decreased cAMP stimulation.
11595658	7	54	theme	combined	1028:1035	arg1	A40/A80/A92/A100					1061:1076	A40/A80/A92/A100	1061:1076	A40/A80/A92/A100	1061:1076	In contrast, the combined mutations A80/A92/A100, A40/A80/A92/A100, and A40/A47/A80/A92/A100 had low levels of expression, did not bind the radioligand, and had a decreased cAMP stimulation.
11595658	7	54	theme	combined	1028:1035	arg1	A40/A47/A80/A92/A100					1083:1102	A40/A47/A80/A92/A100	1083:1102	A40/A47/A80/A92/A100	1083:1102	In contrast, the combined mutations A80/A92/A100, A40/A80/A92/A100, and A40/A47/A80/A92/A100 had low levels of expression, did not bind the radioligand, and had a decreased cAMP stimulation.
11595658	7	54	theme	combined	1028:1035	arg1	A80/A92/A100					1047:1058	A80/A92/A100	1047:1058	A80/A92/A100	1047:1058	In contrast, the combined mutations A80/A92/A100, A40/A80/A92/A100, and A40/A47/A80/A92/A100 had low levels of expression, did not bind the radioligand, and had a decreased cAMP stimulation.
11595658	1	55	dep	sites	194:198	arg1	N45					206:208	N45	206:208	N45	206:208	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	55	dep	sites	194:198	arg1	N98					225:227	N98	225:227	N98	225:227	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	55	dep	sites	194:198	arg1	N78					211:213	N78	211:213	N78	211:213	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	55	dep	sites	194:198	arg1	sites					194:198	five potential N-glycosylation sites	163:198	five potential N-glycosylation sites: N38, N45, N78, N90, and N98	163:227	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	55	dep	sites	194:198	arg1	N38					201:203	N38	201:203	N38	201:203	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	1	55	dep	sites	194:198	arg1	N90					216:218	N90	216:218	N90	216:218	The corticotropin-releasing factor (CRF) receptor type 1 (CRFR1) contains five potential N-glycosylation sites: N38, N45, N78, N90, and N98.
11595658	5	56	theme	glycosylation	686:698	arg1	site					700:703	each glycosylation site	681:703	each glycosylation site	681:703	Two sets of mutations were performed for each glycosylation site: N to Q and S/T to A, respectively.
11389975	5	0	from	sites	823:827	arg1	domain					866:871	the extracellular, amino terminal domain	832:871	domain	866:871	There are three putative Asn-linked glycosylation sites in the extracellular, amino terminal domain of CRLR at positions 66, 118 and 123.
11389975	5	0	from	sites	823:827	arg1	positions					884:892	positions 66, 118 and 123	884:908	positions 66, 118 and 123	884:908	There are three putative Asn-linked glycosylation sites in the extracellular, amino terminal domain of CRLR at positions 66, 118 and 123.
11389975	5	0	from	sites	823:827	arg1	CRLR					876:879	CRLR	876:879	CRLR	876:879	There are three putative Asn-linked glycosylation sites in the extracellular, amino terminal domain of CRLR at positions 66, 118 and 123.
11389975	7	1	theme	Substituting	1114:1125	arg1	Asn66					1127:1131	Asn66	1127:1131	Asn66	1127:1131	Substituting Asn66 or Asn118 had no effect.
11389975	11	2	from	conformation	1877:1888	arg1	surface					1902:1908	the cell surface	1893:1908	the cell surface	1893:1908	It thus appears that glycosylation of Asn123 is required for CRLR to assume the appropriate conformation on the cell surface through its interaction with RAMPs.
11389975	2	3	theme	CRLR	341:344	arg1	status					331:336	the glycosylation status	313:336	the glycosylation status of CRLR	313:344	RAMP proteins modify the glycosylation status of CRLR and determine their receptor specificity; when treated with tunicamycin, a glycosylation inhibitor, CHO-K1 cells constitutively expressing both RAMP2 and CRLR lost the capacity to bind adrenomedullin.
11389975	10	4	theme	surface	1765:1771	arg1	expression					1773:1782	cell surface expression	1760:1782	cell surface expression	1760:1782	Our data shows that glycosylation of Asn66 and Asn118 is not essential for ligand binding, signal transduction and cell surface expression, and Asn123 is important for ligand binding and signal transduction rather than cell surface expression.
11389975	8	5	theme	FLAG-tagged	1192:1202	arg1	CRLRs					1204:1208	FLAG-tagged CRLRs	1192:1208	FLAG-tagged CRLRs	1192:1208	FACS analysis of cells expressing FLAG-tagged CRLRs showed that disrupting Asn-linked glycosylation severely affected the transport of the CRLR protein to the cell surface on N66/118/123Q mutant, and slightly reduced the level of the cell surface expression of N123Q mutant compared with wild-type CRLR.
11389975	1	6	theme	CGRP	146:149	arg1	receptor					151:158	a CGRP receptor	144:158	a CGRP receptor when complexed with receptor activity-modifying protein 1 (RAMP1)	144:224	Calcitonin receptor-like receptor (CRLR) constitutes either a CGRP receptor when complexed with receptor activity-modifying protein 1 (RAMP1) or an adrenomedullin receptor when complexed with RAMP2 or RAMP3.
11389975	1	7	theme	adrenomedullin	232:245	arg1	receptor					247:254	an adrenomedullin receptor	229:254	an adrenomedullin receptor	229:254	Calcitonin receptor-like receptor (CRLR) constitutes either a CGRP receptor when complexed with receptor activity-modifying protein 1 (RAMP1) or an adrenomedullin receptor when complexed with RAMP2 or RAMP3.
11389975	8	8	theme	expression	1405:1414	arg1	level					1379:1383	the level	1375:1383	the level of the cell surface expression of N123Q mutant	1375:1430	FACS analysis of cells expressing FLAG-tagged CRLRs showed that disrupting Asn-linked glycosylation severely affected the transport of the CRLR protein to the cell surface on N66/118/123Q mutant, and slightly reduced the level of the cell surface expression of N123Q mutant compared with wild-type CRLR.
11389975	8	9	theme	mutant	1425:1430	arg1	expression					1405:1414	the cell surface expression	1388:1414	the cell surface expression of N123Q mutant	1388:1430	FACS analysis of cells expressing FLAG-tagged CRLRs showed that disrupting Asn-linked glycosylation severely affected the transport of the CRLR protein to the cell surface on N66/118/123Q mutant, and slightly reduced the level of the cell surface expression of N123Q mutant compared with wild-type CRLR.
11389975	9	10	theme	other	1519:1523	arg1	mutants					1532:1538	other single mutants	1519:1538	other single mutants	1519:1538	But other single mutants (N66Q, N118Q) had no effect for other single mutants.
11389975	10	11	theme	Asn118	1588:1593	arg1	glycosylation					1561:1573	glycosylation	1561:1573	glycosylation of Asn66 and Asn118	1561:1593	Our data shows that glycosylation of Asn66 and Asn118 is not essential for ligand binding, signal transduction and cell surface expression, and Asn123 is important for ligand binding and signal transduction rather than cell surface expression.
11389975	8	12	theme	N66/118/123Q	1333:1344	arg1	mutant					1346:1351	N66/118/123Q mutant	1333:1351	N66/118/123Q mutant	1333:1351	FACS analysis of cells expressing FLAG-tagged CRLRs showed that disrupting Asn-linked glycosylation severely affected the transport of the CRLR protein to the cell surface on N66/118/123Q mutant, and slightly reduced the level of the cell surface expression of N123Q mutant compared with wild-type CRLR.
11389975	11	13	with	interaction	1922:1932	arg1	RAMPs					1939:1943	RAMPs	1939:1943	RAMPs	1939:1943	It thus appears that glycosylation of Asn123 is required for CRLR to assume the appropriate conformation on the cell surface through its interaction with RAMPs.
11389975	6	14	theme	Asn	978:980	arg1	residues					982:989	selected Asn residues	969:989	selected Asn residues	969:989	Analysis of CRLR mutants in which Gln was substituted for selected Asn residues showed that glycosylation of Asn123 is required for both the binding of adrenomedullin and the transduction of its signal.
11389975	10	15	theme	Asn66	1578:1582	arg1	glycosylation					1561:1573	glycosylation	1561:1573	glycosylation of Asn66 and Asn118	1561:1593	Our data shows that glycosylation of Asn66 and Asn118 is not essential for ligand binding, signal transduction and cell surface expression, and Asn123 is important for ligand binding and signal transduction rather than cell surface expression.
11389975	11	16	theme	Asn123	1823:1828	arg1	glycosylation					1806:1818	glycosylation	1806:1818	glycosylation of Asn123	1806:1828	It thus appears that glycosylation of Asn123 is required for CRLR to assume the appropriate conformation on the cell surface through its interaction with RAMPs.
11389975	5	17	theme	terminal	857:864	arg1	domain					866:871	the extracellular, amino terminal domain	832:871	domain	866:871	There are three putative Asn-linked glycosylation sites in the extracellular, amino terminal domain of CRLR at positions 66, 118 and 123.
11389975	5	17	theme	terminal	857:864	arg1	CRLR					876:879	CRLR	876:879	CRLR	876:879	There are three putative Asn-linked glycosylation sites in the extracellular, amino terminal domain of CRLR at positions 66, 118 and 123.
11389975	9	18	theme	single	1525:1530	arg1	mutants					1532:1538	other single mutants	1519:1538	other single mutants	1519:1538	But other single mutants (N66Q, N118Q) had no effect for other single mutants.
11389975	10	19	theme	ligand	1616:1621	arg1	binding					1623:1629	ligand binding	1616:1629	ligand binding	1616:1629	Our data shows that glycosylation of Asn66 and Asn118 is not essential for ligand binding, signal transduction and cell surface expression, and Asn123 is important for ligand binding and signal transduction rather than cell surface expression.
11389975	4	20	theme	Whichever	672:680	arg1	protein					687:693	Whichever RAMP protein	672:693	Whichever RAMP protein	672:693	Whichever RAMP protein was co-expressing with CRLR, the ligand binding was sensitive to tunicamycin.
11389975	8	21	theme	FACS	1158:1161	arg1	analysis					1163:1170	FACS analysis	1158:1170	FACS analysis of cells expressing FLAG-tagged CRLRs	1158:1208	FACS analysis of cells expressing FLAG-tagged CRLRs showed that disrupting Asn-linked glycosylation severely affected the transport of the CRLR protein to the cell surface on N66/118/123Q mutant, and slightly reduced the level of the cell surface expression of N123Q mutant compared with wild-type CRLR.
11389975	0	22	from	Asn123	31:36	arg1	Glycosylation					0:12	Glycosylation	0:12	Glycosylation of human CRLR at Asn123	0:36	Glycosylation of human CRLR at Asn123 is required for ligand binding and signaling.
11389975	10	23	theme	cell	1656:1659	arg1	expression					1669:1678	cell surface expression	1656:1678	cell surface expression	1656:1678	Our data shows that glycosylation of Asn66 and Asn118 is not essential for ligand binding, signal transduction and cell surface expression, and Asn123 is important for ligand binding and signal transduction rather than cell surface expression.
11389975	6	24	theme	adrenomedullin	1063:1076	arg1	transduction					1086:1097	the transduction	1082:1097	the transduction of its signal	1082:1111	Analysis of CRLR mutants in which Gln was substituted for selected Asn residues showed that glycosylation of Asn123 is required for both the binding of adrenomedullin and the transduction of its signal.
11389975	6	24	theme	adrenomedullin	1063:1076	arg1	binding					1052:1058	the binding	1048:1058	the binding of adrenomedullin	1048:1076	Analysis of CRLR mutants in which Gln was substituted for selected Asn residues showed that glycosylation of Asn123 is required for both the binding of adrenomedullin and the transduction of its signal.
11389975	8	25	theme	cells	1175:1179	arg1	analysis					1163:1170	FACS analysis	1158:1170	FACS analysis of cells expressing FLAG-tagged CRLRs	1158:1208	FACS analysis of cells expressing FLAG-tagged CRLRs showed that disrupting Asn-linked glycosylation severely affected the transport of the CRLR protein to the cell surface on N66/118/123Q mutant, and slightly reduced the level of the cell surface expression of N123Q mutant compared with wild-type CRLR.
11389975	2	26	theme	receptor	366:373	arg1	specificity					375:385	their receptor specificity	360:385	their receptor specificity	360:385	RAMP proteins modify the glycosylation status of CRLR and determine their receptor specificity; when treated with tunicamycin, a glycosylation inhibitor, CHO-K1 cells constitutively expressing both RAMP2 and CRLR lost the capacity to bind adrenomedullin.
11389975	2	27	theme	glycosylation	421:433	arg1	inhibitor					435:443	a glycosylation inhibitor	419:443	a glycosylation inhibitor	419:443	RAMP proteins modify the glycosylation status of CRLR and determine their receptor specificity; when treated with tunicamycin, a glycosylation inhibitor, CHO-K1 cells constitutively expressing both RAMP2 and CRLR lost the capacity to bind adrenomedullin.
11389975	2	27	theme	glycosylation	421:433	arg1	tunicamycin					406:416	tunicamycin	406:416	tunicamycin	406:416	RAMP proteins modify the glycosylation status of CRLR and determine their receptor specificity; when treated with tunicamycin, a glycosylation inhibitor, CHO-K1 cells constitutively expressing both RAMP2 and CRLR lost the capacity to bind adrenomedullin.
11389975	6	28	theme	selected	969:976	arg1	residues					982:989	selected Asn residues	969:989	selected Asn residues	969:989	Analysis of CRLR mutants in which Gln was substituted for selected Asn residues showed that glycosylation of Asn123 is required for both the binding of adrenomedullin and the transduction of its signal.
11389975	8	29	from	surface	1322:1328	arg1	mutant					1346:1351	N66/118/123Q mutant	1333:1351	N66/118/123Q mutant	1333:1351	FACS analysis of cells expressing FLAG-tagged CRLRs showed that disrupting Asn-linked glycosylation severely affected the transport of the CRLR protein to the cell surface on N66/118/123Q mutant, and slightly reduced the level of the cell surface expression of N123Q mutant compared with wild-type CRLR.
11389975	2	30	theme	RAMP	292:295	arg1	proteins					297:304	RAMP proteins	292:304	RAMP proteins	292:304	RAMP proteins modify the glycosylation status of CRLR and determine their receptor specificity; when treated with tunicamycin, a glycosylation inhibitor, CHO-K1 cells constitutively expressing both RAMP2 and CRLR lost the capacity to bind adrenomedullin.
11389975	4	31	theme	RAMP	682:685	arg1	protein					687:693	Whichever RAMP protein	672:693	Whichever RAMP protein	672:693	Whichever RAMP protein was co-expressing with CRLR, the ligand binding was sensitive to tunicamycin.
11389975	0	32	theme	CRLR	23:26	arg1	Glycosylation					0:12	Glycosylation	0:12	Glycosylation of human CRLR at Asn123	0:36	Glycosylation of human CRLR at Asn123 is required for ligand binding and signaling.
11389975	7	33	contain	had	1143:1145	arg2	effect					1150:1155	no effect	1147:1155	no effect	1147:1155	Substituting Asn66 or Asn118 had no effect.
11389975	7	33	contain	had	1143:1145	arg1	Asn118					1136:1141	Asn118	1136:1141	Asn118	1136:1141	Substituting Asn66 or Asn118 had no effect.
11389975	7	33	contain	had	1143:1145	arg1	Asn66					1127:1131	Asn66	1127:1131	Asn66	1127:1131	Substituting Asn66 or Asn118 had no effect.
11389975	1	34	theme	Calcitonin	84:93	arg1	CRLR					119:122	CRLR	119:122	CRLR	119:122	Calcitonin receptor-like receptor (CRLR) constitutes either a CGRP receptor when complexed with receptor activity-modifying protein 1 (RAMP1) or an adrenomedullin receptor when complexed with RAMP2 or RAMP3.
11389975	1	34	theme	Calcitonin	84:93	arg1	receptor					109:116	Calcitonin receptor-like receptor	84:116	Calcitonin receptor-like receptor (CRLR)	84:123	Calcitonin receptor-like receptor (CRLR) constitutes either a CGRP receptor when complexed with receptor activity-modifying protein 1 (RAMP1) or an adrenomedullin receptor when complexed with RAMP2 or RAMP3.
11389975	8	35	theme	cell	1392:1395	arg1	expression					1405:1414	the cell surface expression	1388:1414	the cell surface expression of N123Q mutant	1388:1430	FACS analysis of cells expressing FLAG-tagged CRLRs showed that disrupting Asn-linked glycosylation severely affected the transport of the CRLR protein to the cell surface on N66/118/123Q mutant, and slightly reduced the level of the cell surface expression of N123Q mutant compared with wild-type CRLR.
11389975	1	36	theme	receptor	180:187	arg1	protein					208:214	receptor activity-modifying protein 1	180:216	receptor activity-modifying protein 1 (RAMP1)	180:224	Calcitonin receptor-like receptor (CRLR) constitutes either a CGRP receptor when complexed with receptor activity-modifying protein 1 (RAMP1) or an adrenomedullin receptor when complexed with RAMP2 or RAMP3.
11389975	1	36	theme	receptor	180:187	arg1	RAMP1					219:223	RAMP1	219:223	RAMP1	219:223	Calcitonin receptor-like receptor (CRLR) constitutes either a CGRP receptor when complexed with receptor activity-modifying protein 1 (RAMP1) or an adrenomedullin receptor when complexed with RAMP2 or RAMP3.
11389975	3	37	theme	HEK293	561:566	arg1	cells					573:577	HEK293 EBNA cells	561:577	HEK293 EBNA cells constitutively expressing RAMP1/CRLR receptor	561:623	Similarly, in HEK293 EBNA cells constitutively expressing RAMP1/CRLR receptor complex CGRP binding was remarkably inhibited.
11389975	11	38	theme	cell	1897:1900	arg1	surface					1902:1908	the cell surface	1893:1908	the cell surface	1893:1908	It thus appears that glycosylation of Asn123 is required for CRLR to assume the appropriate conformation on the cell surface through its interaction with RAMPs.
11389975	10	39	theme	ligand	1709:1714	arg1	binding					1716:1722	ligand binding	1709:1722	ligand binding	1709:1722	Our data shows that glycosylation of Asn66 and Asn118 is not essential for ligand binding, signal transduction and cell surface expression, and Asn123 is important for ligand binding and signal transduction rather than cell surface expression.
11389975	8	40	theme	wild-type	1446:1454	arg1	CRLR					1456:1459	wild-type CRLR	1446:1459	wild-type CRLR	1446:1459	FACS analysis of cells expressing FLAG-tagged CRLRs showed that disrupting Asn-linked glycosylation severely affected the transport of the CRLR protein to the cell surface on N66/118/123Q mutant, and slightly reduced the level of the cell surface expression of N123Q mutant compared with wild-type CRLR.
11389975	1	41	theme	receptor-like	95:107	arg1	CRLR					119:122	CRLR	119:122	CRLR	119:122	Calcitonin receptor-like receptor (CRLR) constitutes either a CGRP receptor when complexed with receptor activity-modifying protein 1 (RAMP1) or an adrenomedullin receptor when complexed with RAMP2 or RAMP3.
11389975	1	41	theme	receptor-like	95:107	arg1	receptor					109:116	Calcitonin receptor-like receptor	84:116	Calcitonin receptor-like receptor (CRLR)	84:123	Calcitonin receptor-like receptor (CRLR) constitutes either a CGRP receptor when complexed with receptor activity-modifying protein 1 (RAMP1) or an adrenomedullin receptor when complexed with RAMP2 or RAMP3.
11389975	1	42	theme	activity-modifying	189:206	arg1	protein					208:214	receptor activity-modifying protein 1	180:216	receptor activity-modifying protein 1 (RAMP1)	180:224	Calcitonin receptor-like receptor (CRLR) constitutes either a CGRP receptor when complexed with receptor activity-modifying protein 1 (RAMP1) or an adrenomedullin receptor when complexed with RAMP2 or RAMP3.
11389975	1	42	theme	activity-modifying	189:206	arg1	RAMP1					219:223	RAMP1	219:223	RAMP1	219:223	Calcitonin receptor-like receptor (CRLR) constitutes either a CGRP receptor when complexed with receptor activity-modifying protein 1 (RAMP1) or an adrenomedullin receptor when complexed with RAMP2 or RAMP3.
11389975	5	43	theme	putative	789:796	arg1	sites					823:827	three putative Asn-linked glycosylation sites	783:827	three putative Asn-linked glycosylation sites in the extracellular, amino terminal domain of CRLR at positions 66, 118 and 123	783:908	There are three putative Asn-linked glycosylation sites in the extracellular, amino terminal domain of CRLR at positions 66, 118 and 123.
11389975	8	44	theme	CRLR	1297:1300	arg1	protein					1302:1308	the CRLR protein	1293:1308	the CRLR protein	1293:1308	FACS analysis of cells expressing FLAG-tagged CRLRs showed that disrupting Asn-linked glycosylation severely affected the transport of the CRLR protein to the cell surface on N66/118/123Q mutant, and slightly reduced the level of the cell surface expression of N123Q mutant compared with wild-type CRLR.
11389975	10	45	theme	cell	1760:1763	arg1	expression					1773:1782	cell surface expression	1760:1782	cell surface expression	1760:1782	Our data shows that glycosylation of Asn66 and Asn118 is not essential for ligand binding, signal transduction and cell surface expression, and Asn123 is important for ligand binding and signal transduction rather than cell surface expression.
11389975	10	46	theme	signal	1632:1637	arg1	transduction					1639:1650	signal transduction	1632:1650	signal transduction	1632:1650	Our data shows that glycosylation of Asn66 and Asn118 is not essential for ligand binding, signal transduction and cell surface expression, and Asn123 is important for ligand binding and signal transduction rather than cell surface expression.
11389975	0	47	gly	Glycosylation	0:12	arg2	Asn123					31:36	Asn123	31:36	Asn123	31:36	Glycosylation of human CRLR at Asn123 is required for ligand binding and signaling.
11389975	0	47	gly	Glycosylation	0:12	arg1	CRLR					23:26	human CRLR	17:26	human CRLR	17:26	Glycosylation of human CRLR at Asn123 is required for ligand binding and signaling.
11389975	9	48	theme	single	1472:1477	arg1	N118Q					1494:1498	N118Q	1494:1498	N118Q	1494:1498	But other single mutants (N66Q, N118Q) had no effect for other single mutants.
11389975	9	48	theme	single	1472:1477	arg1	mutants					1479:1485	other single mutants	1466:1485	other single mutants (N66Q, N118Q)	1466:1499	But other single mutants (N66Q, N118Q) had no effect for other single mutants.
11389975	5	49	theme	CRLR	876:879	arg1	domain					866:871	the extracellular, amino terminal domain	832:871	domain	866:871	There are three putative Asn-linked glycosylation sites in the extracellular, amino terminal domain of CRLR at positions 66, 118 and 123.
11389975	5	49	theme	CRLR	876:879	arg1	CRLR					876:879	CRLR	876:879	CRLR	876:879	There are three putative Asn-linked glycosylation sites in the extracellular, amino terminal domain of CRLR at positions 66, 118 and 123.
11389975	5	50	theme	Asn-linked	798:807	arg1	sites					823:827	three putative Asn-linked glycosylation sites	783:827	three putative Asn-linked glycosylation sites in the extracellular, amino terminal domain of CRLR at positions 66, 118 and 123	783:908	There are three putative Asn-linked glycosylation sites in the extracellular, amino terminal domain of CRLR at positions 66, 118 and 123.
11389975	5	51	theme	extracellular	836:848	arg1	domain					866:871	the extracellular, amino terminal domain	832:871	domain	866:871	There are three putative Asn-linked glycosylation sites in the extracellular, amino terminal domain of CRLR at positions 66, 118 and 123.
11389975	5	51	theme	extracellular	836:848	arg1	CRLR					876:879	CRLR	876:879	CRLR	876:879	There are three putative Asn-linked glycosylation sites in the extracellular, amino terminal domain of CRLR at positions 66, 118 and 123.
11389975	6	52	theme	mutants	928:934	arg1	Analysis					911:918	Analysis	911:918	Analysis of CRLR mutants in which Gln was substituted for selected Asn residues	911:989	Analysis of CRLR mutants in which Gln was substituted for selected Asn residues showed that glycosylation of Asn123 is required for both the binding of adrenomedullin and the transduction of its signal.
11389975	2	53	theme	CHO-K1	446:451	arg1	cells					453:457	CHO-K1 cells	446:457	CHO-K1 cells constitutively expressing both RAMP2 and CRLR	446:503	RAMP proteins modify the glycosylation status of CRLR and determine their receptor specificity; when treated with tunicamycin, a glycosylation inhibitor, CHO-K1 cells constitutively expressing both RAMP2 and CRLR lost the capacity to bind adrenomedullin.
11389975	2	54	gly	glycosylation	317:329	arg1	CRLR					341:344	CRLR	341:344	CRLR	341:344	RAMP proteins modify the glycosylation status of CRLR and determine their receptor specificity; when treated with tunicamycin, a glycosylation inhibitor, CHO-K1 cells constitutively expressing both RAMP2 and CRLR lost the capacity to bind adrenomedullin.
11389975	8	55	link	Asn-linked	1233:1242	arg1	glycosylation					1244:1256	Asn-linked glycosylation	1233:1256	Asn-linked glycosylation	1233:1256	FACS analysis of cells expressing FLAG-tagged CRLRs showed that disrupting Asn-linked glycosylation severely affected the transport of the CRLR protein to the cell surface on N66/118/123Q mutant, and slightly reduced the level of the cell surface expression of N123Q mutant compared with wild-type CRLR.
11389975	3	56	theme	EBNA	568:571	arg1	cells					573:577	HEK293 EBNA cells	561:577	HEK293 EBNA cells constitutively expressing RAMP1/CRLR receptor	561:623	Similarly, in HEK293 EBNA cells constitutively expressing RAMP1/CRLR receptor complex CGRP binding was remarkably inhibited.
11389975	8	57	theme	protein	1302:1308	arg1	transport					1280:1288	the transport	1276:1288	the transport of the CRLR protein to the cell surface on N66/118/123Q mutant	1276:1351	FACS analysis of cells expressing FLAG-tagged CRLRs showed that disrupting Asn-linked glycosylation severely affected the transport of the CRLR protein to the cell surface on N66/118/123Q mutant, and slightly reduced the level of the cell surface expression of N123Q mutant compared with wild-type CRLR.
11389975	5	58	link	Asn-linked	798:807	arg1	sites					823:827	three putative Asn-linked glycosylation sites	783:827	three putative Asn-linked glycosylation sites in the extracellular, amino terminal domain of CRLR at positions 66, 118 and 123	783:908	There are three putative Asn-linked glycosylation sites in the extracellular, amino terminal domain of CRLR at positions 66, 118 and 123.
11389975	9	59	theme	other	1466:1470	arg1	N118Q					1494:1498	N118Q	1494:1498	N118Q	1494:1498	But other single mutants (N66Q, N118Q) had no effect for other single mutants.
11389975	9	59	theme	other	1466:1470	arg1	mutants					1479:1485	other single mutants	1466:1485	other single mutants (N66Q, N118Q)	1466:1499	But other single mutants (N66Q, N118Q) had no effect for other single mutants.
11389975	2	60	theme	glycosylation	317:329	arg1	status					331:336	the glycosylation status	313:336	the glycosylation status of CRLR	313:344	RAMP proteins modify the glycosylation status of CRLR and determine their receptor specificity; when treated with tunicamycin, a glycosylation inhibitor, CHO-K1 cells constitutively expressing both RAMP2 and CRLR lost the capacity to bind adrenomedullin.
11389975	10	61	theme	signal	1728:1733	arg1	transduction					1735:1746	signal transduction	1728:1746	signal transduction	1728:1746	Our data shows that glycosylation of Asn66 and Asn118 is not essential for ligand binding, signal transduction and cell surface expression, and Asn123 is important for ligand binding and signal transduction rather than cell surface expression.
11389975	5	62	gly	glycosylation	809:821	arg2	three					783:787	three	783:787	three	783:787	There are three putative Asn-linked glycosylation sites in the extracellular, amino terminal domain of CRLR at positions 66, 118 and 123.
11389975	5	62	gly	glycosylation	809:821	arg2	positions					884:892	positions 66, 118 and 123	884:908	positions 66, 118 and 123	884:908	There are three putative Asn-linked glycosylation sites in the extracellular, amino terminal domain of CRLR at positions 66, 118 and 123.
11389975	5	62	gly	glycosylation	809:821	arg2	sites					823:827	three putative Asn-linked glycosylation sites	783:827	three putative Asn-linked glycosylation sites in the extracellular, amino terminal domain of CRLR at positions 66, 118 and 123	783:908	There are three putative Asn-linked glycosylation sites in the extracellular, amino terminal domain of CRLR at positions 66, 118 and 123.
11389975	9	63	contain	had	1501:1503	arg2	effect					1508:1513	no effect	1505:1513	no effect	1505:1513	But other single mutants (N66Q, N118Q) had no effect for other single mutants.
11389975	9	63	contain	had	1501:1503	arg1	N118Q					1494:1498	N118Q	1494:1498	N118Q	1494:1498	But other single mutants (N66Q, N118Q) had no effect for other single mutants.
11389975	9	63	contain	had	1501:1503	arg1	mutants					1479:1485	other single mutants	1466:1485	other single mutants (N66Q, N118Q)	1466:1499	But other single mutants (N66Q, N118Q) had no effect for other single mutants.
11389975	8	64	theme	N123Q	1419:1423	arg1	mutant					1425:1430	N123Q mutant	1419:1430	N123Q mutant	1419:1430	FACS analysis of cells expressing FLAG-tagged CRLRs showed that disrupting Asn-linked glycosylation severely affected the transport of the CRLR protein to the cell surface on N66/118/123Q mutant, and slightly reduced the level of the cell surface expression of N123Q mutant compared with wild-type CRLR.
11389975	3	65	theme	complex	625:631	arg1	binding					638:644	complex CGRP binding	625:644	complex CGRP binding	625:644	Similarly, in HEK293 EBNA cells constitutively expressing RAMP1/CRLR receptor complex CGRP binding was remarkably inhibited.
11389975	10	66	theme	surface	1661:1667	arg1	expression					1669:1678	cell surface expression	1656:1678	cell surface expression	1656:1678	Our data shows that glycosylation of Asn66 and Asn118 is not essential for ligand binding, signal transduction and cell surface expression, and Asn123 is important for ligand binding and signal transduction rather than cell surface expression.
11389975	6	67	theme	signal	1106:1111	arg1	transduction					1086:1097	the transduction	1082:1097	the transduction of its signal	1082:1111	Analysis of CRLR mutants in which Gln was substituted for selected Asn residues showed that glycosylation of Asn123 is required for both the binding of adrenomedullin and the transduction of its signal.
11389975	6	67	theme	signal	1106:1111	arg1	binding					1052:1058	the binding	1048:1058	the binding of adrenomedullin	1048:1076	Analysis of CRLR mutants in which Gln was substituted for selected Asn residues showed that glycosylation of Asn123 is required for both the binding of adrenomedullin and the transduction of its signal.
11389975	3	68	theme	CGRP	633:636	arg1	binding					638:644	complex CGRP binding	625:644	complex CGRP binding	625:644	Similarly, in HEK293 EBNA cells constitutively expressing RAMP1/CRLR receptor complex CGRP binding was remarkably inhibited.
11389975	5	69	from	positions	884:892	arg1	domain					866:871	the extracellular, amino terminal domain	832:871	domain	866:871	There are three putative Asn-linked glycosylation sites in the extracellular, amino terminal domain of CRLR at positions 66, 118 and 123.
11389975	5	69	from	positions	884:892	arg1	sites					823:827	three putative Asn-linked glycosylation sites	783:827	three putative Asn-linked glycosylation sites in the extracellular, amino terminal domain of CRLR at positions 66, 118 and 123	783:908	There are three putative Asn-linked glycosylation sites in the extracellular, amino terminal domain of CRLR at positions 66, 118 and 123.
11389975	5	69	from	positions	884:892	arg1	CRLR					876:879	CRLR	876:879	CRLR	876:879	There are three putative Asn-linked glycosylation sites in the extracellular, amino terminal domain of CRLR at positions 66, 118 and 123.
11389975	4	70	theme	ligand	728:733	arg1	sensitive					747:755	sensitive	747:755	sensitive	747:755	Whichever RAMP protein was co-expressing with CRLR, the ligand binding was sensitive to tunicamycin.
11389975	4	70	theme	ligand	728:733	arg1	binding					735:741	the ligand binding	724:741	the ligand binding	724:741	Whichever RAMP protein was co-expressing with CRLR, the ligand binding was sensitive to tunicamycin.
11389975	10	71	gly	glycosylation	1561:1573	arg1	Asn66					1578:1582	Asn66	1578:1582	Asn66	1578:1582	Our data shows that glycosylation of Asn66 and Asn118 is not essential for ligand binding, signal transduction and cell surface expression, and Asn123 is important for ligand binding and signal transduction rather than cell surface expression.
11389975	10	71	gly	glycosylation	1561:1573	arg1	ligand					1616:1621	ligand binding	1616:1629	ligand binding	1616:1629	Our data shows that glycosylation of Asn66 and Asn118 is not essential for ligand binding, signal transduction and cell surface expression, and Asn123 is important for ligand binding and signal transduction rather than cell surface expression.
11389975	10	71	gly	glycosylation	1561:1573	arg1	cell					1656:1659	cell surface expression	1656:1678	cell surface expression	1656:1678	Our data shows that glycosylation of Asn66 and Asn118 is not essential for ligand binding, signal transduction and cell surface expression, and Asn123 is important for ligand binding and signal transduction rather than cell surface expression.
11389975	10	71	gly	glycosylation	1561:1573	arg1	surface					1661:1667	cell surface expression	1656:1678	cell surface expression	1656:1678	Our data shows that glycosylation of Asn66 and Asn118 is not essential for ligand binding, signal transduction and cell surface expression, and Asn123 is important for ligand binding and signal transduction rather than cell surface expression.
11389975	10	71	gly	glycosylation	1561:1573	arg1	Asn118					1588:1593	Asn118	1588:1593	Asn118	1588:1593	Our data shows that glycosylation of Asn66 and Asn118 is not essential for ligand binding, signal transduction and cell surface expression, and Asn123 is important for ligand binding and signal transduction rather than cell surface expression.
11389975	10	71	gly	glycosylation	1561:1573	arg1	signal					1632:1637	signal transduction	1632:1650	signal transduction	1632:1650	Our data shows that glycosylation of Asn66 and Asn118 is not essential for ligand binding, signal transduction and cell surface expression, and Asn123 is important for ligand binding and signal transduction rather than cell surface expression.
11389975	6	72	theme	Asn123	1020:1025	arg1	glycosylation					1003:1015	glycosylation	1003:1015	glycosylation of Asn123	1003:1025	Analysis of CRLR mutants in which Gln was substituted for selected Asn residues showed that glycosylation of Asn123 is required for both the binding of adrenomedullin and the transduction of its signal.
11389975	0	73	theme	ligand	54:59	arg1	binding					61:67	ligand binding	54:67	ligand binding	54:67	Glycosylation of human CRLR at Asn123 is required for ligand binding and signaling.
11389975	11	74	gly	glycosylation	1806:1818	arg1	Asn123					1823:1828	Asn123	1823:1828	Asn123	1823:1828	It thus appears that glycosylation of Asn123 is required for CRLR to assume the appropriate conformation on the cell surface through its interaction with RAMPs.
11389975	3	75	theme	RAMP1/CRLR	605:614	arg1	receptor					616:623	RAMP1/CRLR receptor	605:623	RAMP1/CRLR receptor	605:623	Similarly, in HEK293 EBNA cells constitutively expressing RAMP1/CRLR receptor complex CGRP binding was remarkably inhibited.
11389975	5	76	theme	amino	851:855	arg1	domain					866:871	the extracellular, amino terminal domain	832:871	domain	866:871	There are three putative Asn-linked glycosylation sites in the extracellular, amino terminal domain of CRLR at positions 66, 118 and 123.
11389975	5	76	theme	amino	851:855	arg1	CRLR					876:879	CRLR	876:879	CRLR	876:879	There are three putative Asn-linked glycosylation sites in the extracellular, amino terminal domain of CRLR at positions 66, 118 and 123.
11389975	8	77	theme	surface	1397:1403	arg1	expression					1405:1414	the cell surface expression	1388:1414	the cell surface expression of N123Q mutant	1388:1430	FACS analysis of cells expressing FLAG-tagged CRLRs showed that disrupting Asn-linked glycosylation severely affected the transport of the CRLR protein to the cell surface on N66/118/123Q mutant, and slightly reduced the level of the cell surface expression of N123Q mutant compared with wild-type CRLR.
11389975	8	78	theme	Asn-linked	1233:1242	arg1	glycosylation					1244:1256	Asn-linked glycosylation	1233:1256	Asn-linked glycosylation	1233:1256	FACS analysis of cells expressing FLAG-tagged CRLRs showed that disrupting Asn-linked glycosylation severely affected the transport of the CRLR protein to the cell surface on N66/118/123Q mutant, and slightly reduced the level of the cell surface expression of N123Q mutant compared with wild-type CRLR.
11389975	5	79	theme	glycosylation	809:821	arg1	sites					823:827	three putative Asn-linked glycosylation sites	783:827	three putative Asn-linked glycosylation sites in the extracellular, amino terminal domain of CRLR at positions 66, 118 and 123	783:908	There are three putative Asn-linked glycosylation sites in the extracellular, amino terminal domain of CRLR at positions 66, 118 and 123.
11389975	6	80	theme	CRLR	923:926	arg1	mutants					928:934	CRLR mutants	923:934	CRLR mutants in which Gln was substituted for selected Asn residues	923:989	Analysis of CRLR mutants in which Gln was substituted for selected Asn residues showed that glycosylation of Asn123 is required for both the binding of adrenomedullin and the transduction of its signal.
11389975	0	81	theme	human	17:21	arg1	CRLR					23:26	human CRLR	17:26	human CRLR	17:26	Glycosylation of human CRLR at Asn123 is required for ligand binding and signaling.
11389975	6	82	gly	glycosylation	1003:1015	arg1	Asn123					1020:1025	Asn123	1020:1025	Asn123	1020:1025	Analysis of CRLR mutants in which Gln was substituted for selected Asn residues showed that glycosylation of Asn123 is required for both the binding of adrenomedullin and the transduction of its signal.
11389975	6	82	gly	glycosylation	1003:1015	arg1	adrenomedullin					1063:1076	adrenomedullin	1063:1076	adrenomedullin	1063:1076	Analysis of CRLR mutants in which Gln was substituted for selected Asn residues showed that glycosylation of Asn123 is required for both the binding of adrenomedullin and the transduction of its signal.
11389975	6	82	gly	glycosylation	1003:1015	arg1	signal					1106:1111	its signal	1102:1111	its signal	1102:1111	Analysis of CRLR mutants in which Gln was substituted for selected Asn residues showed that glycosylation of Asn123 is required for both the binding of adrenomedullin and the transduction of its signal.
11389975	8	83	theme	cell	1317:1320	arg1	surface					1322:1328	the cell surface	1313:1328	the cell surface on N66/118/123Q mutant	1313:1351	FACS analysis of cells expressing FLAG-tagged CRLRs showed that disrupting Asn-linked glycosylation severely affected the transport of the CRLR protein to the cell surface on N66/118/123Q mutant, and slightly reduced the level of the cell surface expression of N123Q mutant compared with wild-type CRLR.
11389975	11	84	theme	appropriate	1865:1875	arg1	conformation					1877:1888	the appropriate conformation	1861:1888	the appropriate conformation on the cell surface	1861:1908	It thus appears that glycosylation of Asn123 is required for CRLR to assume the appropriate conformation on the cell surface through its interaction with RAMPs.
16014566	5	0	theme	Dami	1227:1230	arg1	cells					1232:1236	transfected Dami cells	1215:1236	transfected Dami cells	1215:1236	Neither N92A nor S94A affected the expression of GPVI, based on the direct binding of murine anti-human GPVI monoclonal antibody 204-11 to transfected Dami cells.
16014566	3	1	dep	%	874:874	arg1	%					867:867	%	867:867	%	867:867	In stably transfected Dami cells, the substitutions N92A or S94A, but not L95H, resulted in a 30% to 40% decrease in adhesion to CVX, but a 90% or greater decrease in adhesion to CRP and a 65% to 70% decrease in adhesion to type I collagen.
16014566	2	2	theme	COS-7	636:640	arg1	binding					647:653	transfected COS-7 cell binding	624:653	transfected COS-7 cell binding to both CRP and CVX	624:673	In COS-7 cells transiently transfected with GPVI, deglycosylation with peptide-N-glycosidase F (PNGase F; specific for complex N-linked glycans) or tunicamycin decreases the molecular weight of GPVI and reduces transfected COS-7 cell binding to both CRP and CVX.
16014566	2	3	theme	molecular	587:595	arg1	weight					597:602	the molecular weight	583:602	the molecular weight of GPVI	583:610	In COS-7 cells transiently transfected with GPVI, deglycosylation with peptide-N-glycosidase F (PNGase F; specific for complex N-linked glycans) or tunicamycin decreases the molecular weight of GPVI and reduces transfected COS-7 cell binding to both CRP and CVX.
16014566	1	4	gly	glycosylation	169:181	arg1	receptor					282:289	this platelet-specific receptor	259:289	this platelet-specific receptor	259:289	Using recombinant human glycoprotein VI (GPVI), we evaluated the effect of N-linked glycosylation at the consensus site Asparagine92-Glycine-Serine94 (N92GS94) on binding of this platelet-specific receptor to its ligands, human type I collagen, collagen-related peptide (CRP), and the snake venom C-type lectin convulxin (CVX).
16014566	1	4	gly	glycosylation	169:181	arg1	N92GS94					236:242	N92GS94	236:242	N92GS94	236:242	Using recombinant human glycoprotein VI (GPVI), we evaluated the effect of N-linked glycosylation at the consensus site Asparagine92-Glycine-Serine94 (N92GS94) on binding of this platelet-specific receptor to its ligands, human type I collagen, collagen-related peptide (CRP), and the snake venom C-type lectin convulxin (CVX).
16014566	1	4	gly	glycosylation	169:181	arg2	N92GS94					236:242	N92GS94	236:242	N92GS94	236:242	Using recombinant human glycoprotein VI (GPVI), we evaluated the effect of N-linked glycosylation at the consensus site Asparagine92-Glycine-Serine94 (N92GS94) on binding of this platelet-specific receptor to its ligands, human type I collagen, collagen-related peptide (CRP), and the snake venom C-type lectin convulxin (CVX).
16014566	1	4	gly	glycosylation	169:181	arg1	Asparagine92-Glycine-Serine94					205:233	the consensus site Asparagine92-Glycine-Serine94	186:233	the consensus site Asparagine92-Glycine-Serine94 (N92GS94)	186:243	Using recombinant human glycoprotein VI (GPVI), we evaluated the effect of N-linked glycosylation at the consensus site Asparagine92-Glycine-Serine94 (N92GS94) on binding of this platelet-specific receptor to its ligands, human type I collagen, collagen-related peptide (CRP), and the snake venom C-type lectin convulxin (CVX).
16014566	1	4	gly	glycosylation	169:181	arg2	Asparagine92-Glycine-Serine94					205:233	the consensus site Asparagine92-Glycine-Serine94	186:233	the consensus site Asparagine92-Glycine-Serine94 (N92GS94)	186:243	Using recombinant human glycoprotein VI (GPVI), we evaluated the effect of N-linked glycosylation at the consensus site Asparagine92-Glycine-Serine94 (N92GS94) on binding of this platelet-specific receptor to its ligands, human type I collagen, collagen-related peptide (CRP), and the snake venom C-type lectin convulxin (CVX).
16014566	5	5	theme	antibody	1196:1203	arg1	binding					1151:1157	the direct binding	1140:1157	the direct binding of murine anti-human GPVI monoclonal antibody 204-11 to transfected Dami cells	1140:1236	Neither N92A nor S94A affected the expression of GPVI, based on the direct binding of murine anti-human GPVI monoclonal antibody 204-11 to transfected Dami cells.
16014566	4	6	theme	Endoglycosidase	950:964	arg1	H					974:974	Endo H	969:974	Endo H	969:974	Treatment with PNGase F, but not Endoglycosidase H (Endo H) (specific for high-mannose N-linked glycans), produced an equivalent decrease in molecular weight.
16014566	4	6	theme	Endoglycosidase	950:964	arg1	H					966:966	Endoglycosidase H	950:966	Endoglycosidase H (Endo H) (specific for high-mannose N-linked glycans)	950:1020	Treatment with PNGase F, but not Endoglycosidase H (Endo H) (specific for high-mannose N-linked glycans), produced an equivalent decrease in molecular weight.
16014566	3	7	theme	Dami	698:701	arg1	cells					703:707	stably transfected Dami cells	679:707	stably transfected Dami cells	679:707	In stably transfected Dami cells, the substitutions N92A or S94A, but not L95H, resulted in a 30% to 40% decrease in adhesion to CVX, but a 90% or greater decrease in adhesion to CRP and a 65% to 70% decrease in adhesion to type I collagen.
16014566	1	8	theme	N-linked	160:167	arg1	glycosylation					169:181	N-linked glycosylation	160:181	N-linked glycosylation at the consensus site Asparagine92-Glycine-Serine94 (N92GS94)	160:243	Using recombinant human glycoprotein VI (GPVI), we evaluated the effect of N-linked glycosylation at the consensus site Asparagine92-Glycine-Serine94 (N92GS94) on binding of this platelet-specific receptor to its ligands, human type I collagen, collagen-related peptide (CRP), and the snake venom C-type lectin convulxin (CVX).
16014566	3	9	theme	70	872:873	arg1	%					867:867	%	867:867	%	867:867	In stably transfected Dami cells, the substitutions N92A or S94A, but not L95H, resulted in a 30% to 40% decrease in adhesion to CVX, but a 90% or greater decrease in adhesion to CRP and a 65% to 70% decrease in adhesion to type I collagen.
16014566	3	10	theme	65	865:866	arg1	%					867:867	%	867:867	%	867:867	In stably transfected Dami cells, the substitutions N92A or S94A, but not L95H, resulted in a 30% to 40% decrease in adhesion to CVX, but a 90% or greater decrease in adhesion to CRP and a 65% to 70% decrease in adhesion to type I collagen.
16014566	1	11	gly	glycoprotein	109:120	arg1	glycoprotein					109:120	human glycoprotein VI (GPVI)	103:130	recombinant human glycoprotein VI (GPVI)	91:130	Using recombinant human glycoprotein VI (GPVI), we evaluated the effect of N-linked glycosylation at the consensus site Asparagine92-Glycine-Serine94 (N92GS94) on binding of this platelet-specific receptor to its ligands, human type I collagen, collagen-related peptide (CRP), and the snake venom C-type lectin convulxin (CVX).
16014566	6	12	theme	type	1391:1394	arg1	collagen					1398:1405	type I collagen	1391:1405	type I collagen	1391:1405	These findings indicate that N-linked glycosylation at N92 in human GPVI is not required for surface expression, but contributes to maximal adhesion to type I collagen, CRP and, to a lesser extent, CVX.
16014566	1	13	theme	consensus	190:198	arg1	N92GS94					236:242	N92GS94	236:242	N92GS94	236:242	Using recombinant human glycoprotein VI (GPVI), we evaluated the effect of N-linked glycosylation at the consensus site Asparagine92-Glycine-Serine94 (N92GS94) on binding of this platelet-specific receptor to its ligands, human type I collagen, collagen-related peptide (CRP), and the snake venom C-type lectin convulxin (CVX).
16014566	1	13	theme	consensus	190:198	arg1	Asparagine92-Glycine-Serine94					205:233	the consensus site Asparagine92-Glycine-Serine94	186:233	the consensus site Asparagine92-Glycine-Serine94 (N92GS94)	186:243	Using recombinant human glycoprotein VI (GPVI), we evaluated the effect of N-linked glycosylation at the consensus site Asparagine92-Glycine-Serine94 (N92GS94) on binding of this platelet-specific receptor to its ligands, human type I collagen, collagen-related peptide (CRP), and the snake venom C-type lectin convulxin (CVX).
16014566	2	14	theme	complex	532:538	arg1	glycans					549:555	complex N-linked glycans	532:555	complex N-linked glycans	532:555	In COS-7 cells transiently transfected with GPVI, deglycosylation with peptide-N-glycosidase F (PNGase F; specific for complex N-linked glycans) or tunicamycin decreases the molecular weight of GPVI and reduces transfected COS-7 cell binding to both CRP and CVX.
16014566	6	15	link	N-linked	1268:1275	arg1	glycosylation					1277:1289	N-linked glycosylation	1268:1289	N-linked glycosylation at N92 in human GPVI	1268:1310	These findings indicate that N-linked glycosylation at N92 in human GPVI is not required for surface expression, but contributes to maximal adhesion to type I collagen, CRP and, to a lesser extent, CVX.
16014566	1	16	theme	snake	370:374	arg1	CVX					407:409	CVX	407:409	CVX	407:409	Using recombinant human glycoprotein VI (GPVI), we evaluated the effect of N-linked glycosylation at the consensus site Asparagine92-Glycine-Serine94 (N92GS94) on binding of this platelet-specific receptor to its ligands, human type I collagen, collagen-related peptide (CRP), and the snake venom C-type lectin convulxin (CVX).
16014566	1	16	theme	snake	370:374	arg1	ligands					298:304	its ligands	294:304	its ligands	294:304	Using recombinant human glycoprotein VI (GPVI), we evaluated the effect of N-linked glycosylation at the consensus site Asparagine92-Glycine-Serine94 (N92GS94) on binding of this platelet-specific receptor to its ligands, human type I collagen, collagen-related peptide (CRP), and the snake venom C-type lectin convulxin (CVX).
16014566	1	16	theme	snake	370:374	arg1	convulxin					396:404	the snake venom C-type lectin convulxin	366:404	the snake venom C-type lectin convulxin (CVX)	366:410	Using recombinant human glycoprotein VI (GPVI), we evaluated the effect of N-linked glycosylation at the consensus site Asparagine92-Glycine-Serine94 (N92GS94) on binding of this platelet-specific receptor to its ligands, human type I collagen, collagen-related peptide (CRP), and the snake venom C-type lectin convulxin (CVX).
16014566	3	17	theme	30	770:771	arg1	%					772:772	%	772:772	%	772:772	In stably transfected Dami cells, the substitutions N92A or S94A, but not L95H, resulted in a 30% to 40% decrease in adhesion to CVX, but a 90% or greater decrease in adhesion to CRP and a 65% to 70% decrease in adhesion to type I collagen.
16014566	6	18	theme	I	1396:1396	arg1	collagen					1398:1405	type I collagen	1391:1405	type I collagen	1391:1405	These findings indicate that N-linked glycosylation at N92 in human GPVI is not required for surface expression, but contributes to maximal adhesion to type I collagen, CRP and, to a lesser extent, CVX.
16014566	2	19	theme	specific	519:526	arg1	F					506:506	peptide-N-glycosidase F	484:506	peptide-N-glycosidase F (PNGase F; specific for complex N-linked glycans)	484:556	In COS-7 cells transiently transfected with GPVI, deglycosylation with peptide-N-glycosidase F (PNGase F; specific for complex N-linked glycans) or tunicamycin decreases the molecular weight of GPVI and reduces transfected COS-7 cell binding to both CRP and CVX.
16014566	2	19	theme	specific	519:526	arg1	F					516:516	PNGase F	509:516	PNGase F; specific for complex N-linked glycans	509:555	In COS-7 cells transiently transfected with GPVI, deglycosylation with peptide-N-glycosidase F (PNGase F; specific for complex N-linked glycans) or tunicamycin decreases the molecular weight of GPVI and reduces transfected COS-7 cell binding to both CRP and CVX.
16014566	1	20	from	Asparagine92-Glycine-Serine94	205:233	arg1	effect					150:155	the effect	146:155	the effect of N-linked glycosylation at the consensus site Asparagine92-Glycine-Serine94 (N92GS94) on binding of this platelet-specific receptor to its ligands, human type I collagen, collagen-related peptide (CRP), and the snake venom C-type lectin convulxin (CVX)	146:410	Using recombinant human glycoprotein VI (GPVI), we evaluated the effect of N-linked glycosylation at the consensus site Asparagine92-Glycine-Serine94 (N92GS94) on binding of this platelet-specific receptor to its ligands, human type I collagen, collagen-related peptide (CRP), and the snake venom C-type lectin convulxin (CVX).
16014566	1	20	from	Asparagine92-Glycine-Serine94	205:233	arg1	glycosylation					169:181	N-linked glycosylation	160:181	N-linked glycosylation at the consensus site Asparagine92-Glycine-Serine94 (N92GS94)	160:243	Using recombinant human glycoprotein VI (GPVI), we evaluated the effect of N-linked glycosylation at the consensus site Asparagine92-Glycine-Serine94 (N92GS94) on binding of this platelet-specific receptor to its ligands, human type I collagen, collagen-related peptide (CRP), and the snake venom C-type lectin convulxin (CVX).
16014566	1	21	theme	C-type	382:387	arg1	CVX					407:409	CVX	407:409	CVX	407:409	Using recombinant human glycoprotein VI (GPVI), we evaluated the effect of N-linked glycosylation at the consensus site Asparagine92-Glycine-Serine94 (N92GS94) on binding of this platelet-specific receptor to its ligands, human type I collagen, collagen-related peptide (CRP), and the snake venom C-type lectin convulxin (CVX).
16014566	1	21	theme	C-type	382:387	arg1	ligands					298:304	its ligands	294:304	its ligands	294:304	Using recombinant human glycoprotein VI (GPVI), we evaluated the effect of N-linked glycosylation at the consensus site Asparagine92-Glycine-Serine94 (N92GS94) on binding of this platelet-specific receptor to its ligands, human type I collagen, collagen-related peptide (CRP), and the snake venom C-type lectin convulxin (CVX).
16014566	1	21	theme	C-type	382:387	arg1	convulxin					396:404	the snake venom C-type lectin convulxin	366:404	the snake venom C-type lectin convulxin (CVX)	366:410	Using recombinant human glycoprotein VI (GPVI), we evaluated the effect of N-linked glycosylation at the consensus site Asparagine92-Glycine-Serine94 (N92GS94) on binding of this platelet-specific receptor to its ligands, human type I collagen, collagen-related peptide (CRP), and the snake venom C-type lectin convulxin (CVX).
16014566	4	22	dep	H	966:966	arg1	specific					978:985	specific	978:985	specific	978:985	Treatment with PNGase F, but not Endoglycosidase H (Endo H) (specific for high-mannose N-linked glycans), produced an equivalent decrease in molecular weight.
16014566	6	23	theme	lesser	1422:1427	arg1	extent					1429:1434	a lesser extent	1420:1434	a lesser extent	1420:1434	These findings indicate that N-linked glycosylation at N92 in human GPVI is not required for surface expression, but contributes to maximal adhesion to type I collagen, CRP and, to a lesser extent, CVX.
16014566	1	24	theme	type	313:316	arg1	collagen					320:327	human type I collagen	307:327	human type I collagen	307:327	Using recombinant human glycoprotein VI (GPVI), we evaluated the effect of N-linked glycosylation at the consensus site Asparagine92-Glycine-Serine94 (N92GS94) on binding of this platelet-specific receptor to its ligands, human type I collagen, collagen-related peptide (CRP), and the snake venom C-type lectin convulxin (CVX).
16014566	1	24	theme	type	313:316	arg1	ligands					298:304	its ligands	294:304	its ligands	294:304	Using recombinant human glycoprotein VI (GPVI), we evaluated the effect of N-linked glycosylation at the consensus site Asparagine92-Glycine-Serine94 (N92GS94) on binding of this platelet-specific receptor to its ligands, human type I collagen, collagen-related peptide (CRP), and the snake venom C-type lectin convulxin (CVX).
16014566	0	25	theme	glycoprotein	68:79	arg1	function					47:54	the function	43:54	the function of platelet glycoprotein VI	43:82	The influence of N-linked glycosylation on the function of platelet glycoprotein VI.
16014566	3	26	theme	type	900:903	arg1	collagen					907:914	type I collagen	900:914	type I collagen	900:914	In stably transfected Dami cells, the substitutions N92A or S94A, but not L95H, resulted in a 30% to 40% decrease in adhesion to CVX, but a 90% or greater decrease in adhesion to CRP and a 65% to 70% decrease in adhesion to type I collagen.
16014566	2	27	theme	peptide-N-glycosidase	484:504	arg1	F					506:506	peptide-N-glycosidase F	484:506	peptide-N-glycosidase F (PNGase F; specific for complex N-linked glycans)	484:556	In COS-7 cells transiently transfected with GPVI, deglycosylation with peptide-N-glycosidase F (PNGase F; specific for complex N-linked glycans) or tunicamycin decreases the molecular weight of GPVI and reduces transfected COS-7 cell binding to both CRP and CVX.
16014566	2	27	theme	peptide-N-glycosidase	484:504	arg1	F					516:516	PNGase F	509:516	PNGase F; specific for complex N-linked glycans	509:555	In COS-7 cells transiently transfected with GPVI, deglycosylation with peptide-N-glycosidase F (PNGase F; specific for complex N-linked glycans) or tunicamycin decreases the molecular weight of GPVI and reduces transfected COS-7 cell binding to both CRP and CVX.
16014566	2	28	theme	GPVI	607:610	arg1	weight					597:602	the molecular weight	583:602	the molecular weight of GPVI	583:610	In COS-7 cells transiently transfected with GPVI, deglycosylation with peptide-N-glycosidase F (PNGase F; specific for complex N-linked glycans) or tunicamycin decreases the molecular weight of GPVI and reduces transfected COS-7 cell binding to both CRP and CVX.
16014566	4	29	link	N-linked	1004:1011	arg1	glycans					1013:1019	high-mannose N-linked glycans	991:1019	high-mannose N-linked glycans	991:1019	Treatment with PNGase F, but not Endoglycosidase H (Endo H) (specific for high-mannose N-linked glycans), produced an equivalent decrease in molecular weight.
16014566	1	30	theme	collagen-related	330:345	arg1	peptide					347:353	collagen-related peptide	330:353	collagen-related peptide (CRP)	330:359	Using recombinant human glycoprotein VI (GPVI), we evaluated the effect of N-linked glycosylation at the consensus site Asparagine92-Glycine-Serine94 (N92GS94) on binding of this platelet-specific receptor to its ligands, human type I collagen, collagen-related peptide (CRP), and the snake venom C-type lectin convulxin (CVX).
16014566	1	30	theme	collagen-related	330:345	arg1	ligands					298:304	its ligands	294:304	its ligands	294:304	Using recombinant human glycoprotein VI (GPVI), we evaluated the effect of N-linked glycosylation at the consensus site Asparagine92-Glycine-Serine94 (N92GS94) on binding of this platelet-specific receptor to its ligands, human type I collagen, collagen-related peptide (CRP), and the snake venom C-type lectin convulxin (CVX).
16014566	1	30	theme	collagen-related	330:345	arg1	CRP					356:358	CRP	356:358	CRP	356:358	Using recombinant human glycoprotein VI (GPVI), we evaluated the effect of N-linked glycosylation at the consensus site Asparagine92-Glycine-Serine94 (N92GS94) on binding of this platelet-specific receptor to its ligands, human type I collagen, collagen-related peptide (CRP), and the snake venom C-type lectin convulxin (CVX).
16014566	4	31	theme	equivalent	1035:1044	arg1	decrease					1046:1053	an equivalent decrease	1032:1053	an equivalent decrease in molecular weight	1032:1073	Treatment with PNGase F, but not Endoglycosidase H (Endo H) (specific for high-mannose N-linked glycans), produced an equivalent decrease in molecular weight.
16014566	1	32	dep	glycoprotein	109:120	arg1	VI					122:123	VI	122:123	VI	122:123	Using recombinant human glycoprotein VI (GPVI), we evaluated the effect of N-linked glycosylation at the consensus site Asparagine92-Glycine-Serine94 (N92GS94) on binding of this platelet-specific receptor to its ligands, human type I collagen, collagen-related peptide (CRP), and the snake venom C-type lectin convulxin (CVX).
16014566	3	33	dep	substitutions	714:726	arg1	L95H					750:753	L95H	750:753	L95H	750:753	In stably transfected Dami cells, the substitutions N92A or S94A, but not L95H, resulted in a 30% to 40% decrease in adhesion to CVX, but a 90% or greater decrease in adhesion to CRP and a 65% to 70% decrease in adhesion to type I collagen.
16014566	3	33	dep	substitutions	714:726	arg1	substitutions					714:726	the substitutions N92A or S94A, but not L95H,	710:754	the substitutions N92A or S94A, but not L95H,	710:754	In stably transfected Dami cells, the substitutions N92A or S94A, but not L95H, resulted in a 30% to 40% decrease in adhesion to CVX, but a 90% or greater decrease in adhesion to CRP and a 65% to 70% decrease in adhesion to type I collagen.
16014566	3	33	dep	substitutions	714:726	arg1	S94A					736:739	S94A	736:739	S94A	736:739	In stably transfected Dami cells, the substitutions N92A or S94A, but not L95H, resulted in a 30% to 40% decrease in adhesion to CVX, but a 90% or greater decrease in adhesion to CRP and a 65% to 70% decrease in adhesion to type I collagen.
16014566	3	33	dep	substitutions	714:726	arg1	N92A					728:731	N92A	728:731	N92A	728:731	In stably transfected Dami cells, the substitutions N92A or S94A, but not L95H, resulted in a 30% to 40% decrease in adhesion to CVX, but a 90% or greater decrease in adhesion to CRP and a 65% to 70% decrease in adhesion to type I collagen.
16014566	2	34	with	deglycosylation	463:477	arg1	F					506:506	peptide-N-glycosidase F	484:506	peptide-N-glycosidase F (PNGase F; specific for complex N-linked glycans)	484:556	In COS-7 cells transiently transfected with GPVI, deglycosylation with peptide-N-glycosidase F (PNGase F; specific for complex N-linked glycans) or tunicamycin decreases the molecular weight of GPVI and reduces transfected COS-7 cell binding to both CRP and CVX.
16014566	2	34	with	deglycosylation	463:477	arg1	F					516:516	PNGase F	509:516	PNGase F; specific for complex N-linked glycans	509:555	In COS-7 cells transiently transfected with GPVI, deglycosylation with peptide-N-glycosidase F (PNGase F; specific for complex N-linked glycans) or tunicamycin decreases the molecular weight of GPVI and reduces transfected COS-7 cell binding to both CRP and CVX.
16014566	2	34	with	deglycosylation	463:477	arg1	tunicamycin					561:571	tunicamycin	561:571	tunicamycin	561:571	In COS-7 cells transiently transfected with GPVI, deglycosylation with peptide-N-glycosidase F (PNGase F; specific for complex N-linked glycans) or tunicamycin decreases the molecular weight of GPVI and reduces transfected COS-7 cell binding to both CRP and CVX.
16014566	4	35	theme	N-linked	1004:1011	arg1	glycans					1013:1019	high-mannose N-linked glycans	991:1019	high-mannose N-linked glycans	991:1019	Treatment with PNGase F, but not Endoglycosidase H (Endo H) (specific for high-mannose N-linked glycans), produced an equivalent decrease in molecular weight.
16014566	3	36	dep	%	779:779	arg1	%					772:772	%	772:772	%	772:772	In stably transfected Dami cells, the substitutions N92A or S94A, but not L95H, resulted in a 30% to 40% decrease in adhesion to CVX, but a 90% or greater decrease in adhesion to CRP and a 65% to 70% decrease in adhesion to type I collagen.
16014566	0	37	dep	glycoprotein	68:79	arg1	VI					81:82	VI	81:82	VI	81:82	The influence of N-linked glycosylation on the function of platelet glycoprotein VI.
16014566	1	38	theme	receptor	282:289	arg1	binding					248:254	binding	248:254	binding of this platelet-specific receptor to its ligands, human type I collagen, collagen-related peptide (CRP), and the snake venom C-type lectin convulxin (CVX)	248:410	Using recombinant human glycoprotein VI (GPVI), we evaluated the effect of N-linked glycosylation at the consensus site Asparagine92-Glycine-Serine94 (N92GS94) on binding of this platelet-specific receptor to its ligands, human type I collagen, collagen-related peptide (CRP), and the snake venom C-type lectin convulxin (CVX).
16014566	1	39	theme	human	103:107	arg1	glycoprotein					109:120	human glycoprotein VI (GPVI)	103:130	recombinant human glycoprotein VI (GPVI)	91:130	Using recombinant human glycoprotein VI (GPVI), we evaluated the effect of N-linked glycosylation at the consensus site Asparagine92-Glycine-Serine94 (N92GS94) on binding of this platelet-specific receptor to its ligands, human type I collagen, collagen-related peptide (CRP), and the snake venom C-type lectin convulxin (CVX).
16014566	0	40	theme	glycosylation	26:38	arg1	influence					4:12	The influence	0:12	The influence of N-linked glycosylation on the function of platelet glycoprotein VI	0:82	The influence of N-linked glycosylation on the function of platelet glycoprotein VI.
16014566	6	41	from	glycosylation	1277:1289	arg1	GPVI					1307:1310	human GPVI	1301:1310	human GPVI	1301:1310	These findings indicate that N-linked glycosylation at N92 in human GPVI is not required for surface expression, but contributes to maximal adhesion to type I collagen, CRP and, to a lesser extent, CVX.
16014566	3	42	theme	greater	823:829	arg1	decrease					831:838	a 90% or greater decrease	814:838	a 90% or greater decrease in adhesion to CRP	814:857	In stably transfected Dami cells, the substitutions N92A or S94A, but not L95H, resulted in a 30% to 40% decrease in adhesion to CVX, but a 90% or greater decrease in adhesion to CRP and a 65% to 70% decrease in adhesion to type I collagen.
16014566	3	43	from	decrease	831:838	arg1	adhesion					843:850	adhesion	843:850	adhesion to CRP	843:857	In stably transfected Dami cells, the substitutions N92A or S94A, but not L95H, resulted in a 30% to 40% decrease in adhesion to CVX, but a 90% or greater decrease in adhesion to CRP and a 65% to 70% decrease in adhesion to type I collagen.
16014566	5	44	theme	anti-human	1169:1178	arg1	antibody					1196:1203	murine anti-human GPVI monoclonal antibody 204-11	1162:1210	murine anti-human GPVI monoclonal antibody 204-11	1162:1210	Neither N92A nor S94A affected the expression of GPVI, based on the direct binding of murine anti-human GPVI monoclonal antibody 204-11 to transfected Dami cells.
16014566	6	45	from	N92	1294:1296	arg1	glycosylation					1277:1289	N-linked glycosylation	1268:1289	N-linked glycosylation at N92 in human GPVI	1268:1310	These findings indicate that N-linked glycosylation at N92 in human GPVI is not required for surface expression, but contributes to maximal adhesion to type I collagen, CRP and, to a lesser extent, CVX.
16014566	3	46	theme	%	818:818	arg1	decrease					831:838	a 90% or greater decrease	814:838	a 90% or greater decrease in adhesion to CRP	814:857	In stably transfected Dami cells, the substitutions N92A or S94A, but not L95H, resulted in a 30% to 40% decrease in adhesion to CVX, but a 90% or greater decrease in adhesion to CRP and a 65% to 70% decrease in adhesion to type I collagen.
16014566	5	47	theme	monoclonal	1185:1194	arg1	antibody					1196:1203	murine anti-human GPVI monoclonal antibody 204-11	1162:1210	murine anti-human GPVI monoclonal antibody 204-11	1162:1210	Neither N92A nor S94A affected the expression of GPVI, based on the direct binding of murine anti-human GPVI monoclonal antibody 204-11 to transfected Dami cells.
16014566	1	48	theme	site	200:203	arg1	N92GS94					236:242	N92GS94	236:242	N92GS94	236:242	Using recombinant human glycoprotein VI (GPVI), we evaluated the effect of N-linked glycosylation at the consensus site Asparagine92-Glycine-Serine94 (N92GS94) on binding of this platelet-specific receptor to its ligands, human type I collagen, collagen-related peptide (CRP), and the snake venom C-type lectin convulxin (CVX).
16014566	1	48	theme	site	200:203	arg1	Asparagine92-Glycine-Serine94					205:233	the consensus site Asparagine92-Glycine-Serine94	186:233	the consensus site Asparagine92-Glycine-Serine94 (N92GS94)	186:243	Using recombinant human glycoprotein VI (GPVI), we evaluated the effect of N-linked glycosylation at the consensus site Asparagine92-Glycine-Serine94 (N92GS94) on binding of this platelet-specific receptor to its ligands, human type I collagen, collagen-related peptide (CRP), and the snake venom C-type lectin convulxin (CVX).
16014566	3	49	from	decrease	876:883	arg1	adhesion					888:895	adhesion	888:895	adhesion to type I collagen	888:914	In stably transfected Dami cells, the substitutions N92A or S94A, but not L95H, resulted in a 30% to 40% decrease in adhesion to CVX, but a 90% or greater decrease in adhesion to CRP and a 65% to 70% decrease in adhesion to type I collagen.
16014566	5	50	theme	direct	1144:1149	arg1	binding					1151:1157	the direct binding	1140:1157	the direct binding of murine anti-human GPVI monoclonal antibody 204-11 to transfected Dami cells	1140:1236	Neither N92A nor S94A affected the expression of GPVI, based on the direct binding of murine anti-human GPVI monoclonal antibody 204-11 to transfected Dami cells.
16014566	3	51	dep	%	867:867	arg1	to					869:870	to	869:870	to	869:870	In stably transfected Dami cells, the substitutions N92A or S94A, but not L95H, resulted in a 30% to 40% decrease in adhesion to CVX, but a 90% or greater decrease in adhesion to CRP and a 65% to 70% decrease in adhesion to type I collagen.
16014566	0	52	link	N-linked	17:24	arg1	glycosylation					26:38	N-linked glycosylation	17:38	N-linked glycosylation	17:38	The influence of N-linked glycosylation on the function of platelet glycoprotein VI.
16014566	3	53	dep	decrease	876:883	arg1	%					874:874	%	874:874	%	874:874	In stably transfected Dami cells, the substitutions N92A or S94A, but not L95H, resulted in a 30% to 40% decrease in adhesion to CVX, but a 90% or greater decrease in adhesion to CRP and a 65% to 70% decrease in adhesion to type I collagen.
16014566	2	54	theme	N-linked	540:547	arg1	glycans					549:555	complex N-linked glycans	532:555	complex N-linked glycans	532:555	In COS-7 cells transiently transfected with GPVI, deglycosylation with peptide-N-glycosidase F (PNGase F; specific for complex N-linked glycans) or tunicamycin decreases the molecular weight of GPVI and reduces transfected COS-7 cell binding to both CRP and CVX.
16014566	6	55	theme	surface	1332:1338	arg1	expression					1340:1349	surface expression	1332:1349	surface expression	1332:1349	These findings indicate that N-linked glycosylation at N92 in human GPVI is not required for surface expression, but contributes to maximal adhesion to type I collagen, CRP and, to a lesser extent, CVX.
16014566	3	56	from	decrease	781:788	arg1	adhesion					793:800	adhesion	793:800	adhesion to CVX	793:807	In stably transfected Dami cells, the substitutions N92A or S94A, but not L95H, resulted in a 30% to 40% decrease in adhesion to CVX, but a 90% or greater decrease in adhesion to CRP and a 65% to 70% decrease in adhesion to type I collagen.
16014566	4	57	theme	PNGase	932:937	arg1	F					939:939	PNGase F	932:939	PNGase F	932:939	Treatment with PNGase F, but not Endoglycosidase H (Endo H) (specific for high-mannose N-linked glycans), produced an equivalent decrease in molecular weight.
16014566	5	58	theme	transfected	1215:1225	arg1	cells					1232:1236	transfected Dami cells	1215:1236	transfected Dami cells	1215:1236	Neither N92A nor S94A affected the expression of GPVI, based on the direct binding of murine anti-human GPVI monoclonal antibody 204-11 to transfected Dami cells.
16014566	1	59	theme	glycosylation	169:181	arg1	effect					150:155	the effect	146:155	the effect of N-linked glycosylation at the consensus site Asparagine92-Glycine-Serine94 (N92GS94) on binding of this platelet-specific receptor to its ligands, human type I collagen, collagen-related peptide (CRP), and the snake venom C-type lectin convulxin (CVX)	146:410	Using recombinant human glycoprotein VI (GPVI), we evaluated the effect of N-linked glycosylation at the consensus site Asparagine92-Glycine-Serine94 (N92GS94) on binding of this platelet-specific receptor to its ligands, human type I collagen, collagen-related peptide (CRP), and the snake venom C-type lectin convulxin (CVX).
16014566	2	60	theme	PNGase	509:514	arg1	F					506:506	peptide-N-glycosidase F	484:506	peptide-N-glycosidase F (PNGase F; specific for complex N-linked glycans)	484:556	In COS-7 cells transiently transfected with GPVI, deglycosylation with peptide-N-glycosidase F (PNGase F; specific for complex N-linked glycans) or tunicamycin decreases the molecular weight of GPVI and reduces transfected COS-7 cell binding to both CRP and CVX.
16014566	2	60	theme	PNGase	509:514	arg1	F					516:516	PNGase F	509:516	PNGase F; specific for complex N-linked glycans	509:555	In COS-7 cells transiently transfected with GPVI, deglycosylation with peptide-N-glycosidase F (PNGase F; specific for complex N-linked glycans) or tunicamycin decreases the molecular weight of GPVI and reduces transfected COS-7 cell binding to both CRP and CVX.
16014566	3	61	theme	transfected	686:696	arg1	cells					703:707	stably transfected Dami cells	679:707	stably transfected Dami cells	679:707	In stably transfected Dami cells, the substitutions N92A or S94A, but not L95H, resulted in a 30% to 40% decrease in adhesion to CVX, but a 90% or greater decrease in adhesion to CRP and a 65% to 70% decrease in adhesion to type I collagen.
16014566	6	62	theme	human	1301:1305	arg1	GPVI					1307:1310	human GPVI	1301:1310	human GPVI	1301:1310	These findings indicate that N-linked glycosylation at N92 in human GPVI is not required for surface expression, but contributes to maximal adhesion to type I collagen, CRP and, to a lesser extent, CVX.
16014566	4	63	theme	high-mannose	991:1002	arg1	glycans					1013:1019	high-mannose N-linked glycans	991:1019	high-mannose N-linked glycans	991:1019	Treatment with PNGase F, but not Endoglycosidase H (Endo H) (specific for high-mannose N-linked glycans), produced an equivalent decrease in molecular weight.
16014566	1	64	theme	venom	376:380	arg1	CVX					407:409	CVX	407:409	CVX	407:409	Using recombinant human glycoprotein VI (GPVI), we evaluated the effect of N-linked glycosylation at the consensus site Asparagine92-Glycine-Serine94 (N92GS94) on binding of this platelet-specific receptor to its ligands, human type I collagen, collagen-related peptide (CRP), and the snake venom C-type lectin convulxin (CVX).
16014566	1	64	theme	venom	376:380	arg1	ligands					298:304	its ligands	294:304	its ligands	294:304	Using recombinant human glycoprotein VI (GPVI), we evaluated the effect of N-linked glycosylation at the consensus site Asparagine92-Glycine-Serine94 (N92GS94) on binding of this platelet-specific receptor to its ligands, human type I collagen, collagen-related peptide (CRP), and the snake venom C-type lectin convulxin (CVX).
16014566	1	64	theme	venom	376:380	arg1	convulxin					396:404	the snake venom C-type lectin convulxin	366:404	the snake venom C-type lectin convulxin (CVX)	366:410	Using recombinant human glycoprotein VI (GPVI), we evaluated the effect of N-linked glycosylation at the consensus site Asparagine92-Glycine-Serine94 (N92GS94) on binding of this platelet-specific receptor to its ligands, human type I collagen, collagen-related peptide (CRP), and the snake venom C-type lectin convulxin (CVX).
16014566	6	65	theme	maximal	1371:1377	arg1	adhesion					1379:1386	maximal adhesion	1371:1386	maximal adhesion to type I collagen	1371:1405	These findings indicate that N-linked glycosylation at N92 in human GPVI is not required for surface expression, but contributes to maximal adhesion to type I collagen, CRP and, to a lesser extent, CVX.
16014566	4	66	theme	Endo	969:972	arg1	H					974:974	Endo H	969:974	Endo H	969:974	Treatment with PNGase F, but not Endoglycosidase H (Endo H) (specific for high-mannose N-linked glycans), produced an equivalent decrease in molecular weight.
16014566	4	66	theme	Endo	969:972	arg1	H					966:966	Endoglycosidase H	950:966	Endoglycosidase H (Endo H) (specific for high-mannose N-linked glycans)	950:1020	Treatment with PNGase F, but not Endoglycosidase H (Endo H) (specific for high-mannose N-linked glycans), produced an equivalent decrease in molecular weight.
16014566	0	67	theme	platelet	59:66	arg1	glycoprotein					68:79	platelet glycoprotein VI	59:82	platelet glycoprotein VI	59:82	The influence of N-linked glycosylation on the function of platelet glycoprotein VI.
16014566	1	68	theme	lectin	389:394	arg1	CVX					407:409	CVX	407:409	CVX	407:409	Using recombinant human glycoprotein VI (GPVI), we evaluated the effect of N-linked glycosylation at the consensus site Asparagine92-Glycine-Serine94 (N92GS94) on binding of this platelet-specific receptor to its ligands, human type I collagen, collagen-related peptide (CRP), and the snake venom C-type lectin convulxin (CVX).
16014566	1	68	theme	lectin	389:394	arg1	ligands					298:304	its ligands	294:304	its ligands	294:304	Using recombinant human glycoprotein VI (GPVI), we evaluated the effect of N-linked glycosylation at the consensus site Asparagine92-Glycine-Serine94 (N92GS94) on binding of this platelet-specific receptor to its ligands, human type I collagen, collagen-related peptide (CRP), and the snake venom C-type lectin convulxin (CVX).
16014566	1	68	theme	lectin	389:394	arg1	convulxin					396:404	the snake venom C-type lectin convulxin	366:404	the snake venom C-type lectin convulxin (CVX)	366:410	Using recombinant human glycoprotein VI (GPVI), we evaluated the effect of N-linked glycosylation at the consensus site Asparagine92-Glycine-Serine94 (N92GS94) on binding of this platelet-specific receptor to its ligands, human type I collagen, collagen-related peptide (CRP), and the snake venom C-type lectin convulxin (CVX).
16014566	1	69	theme	I	318:318	arg1	collagen					320:327	human type I collagen	307:327	human type I collagen	307:327	Using recombinant human glycoprotein VI (GPVI), we evaluated the effect of N-linked glycosylation at the consensus site Asparagine92-Glycine-Serine94 (N92GS94) on binding of this platelet-specific receptor to its ligands, human type I collagen, collagen-related peptide (CRP), and the snake venom C-type lectin convulxin (CVX).
16014566	1	69	theme	I	318:318	arg1	ligands					298:304	its ligands	294:304	its ligands	294:304	Using recombinant human glycoprotein VI (GPVI), we evaluated the effect of N-linked glycosylation at the consensus site Asparagine92-Glycine-Serine94 (N92GS94) on binding of this platelet-specific receptor to its ligands, human type I collagen, collagen-related peptide (CRP), and the snake venom C-type lectin convulxin (CVX).
16014566	4	70	with	Treatment	917:925	arg1	F					939:939	PNGase F	932:939	PNGase F	932:939	Treatment with PNGase F, but not Endoglycosidase H (Endo H) (specific for high-mannose N-linked glycans), produced an equivalent decrease in molecular weight.
16014566	4	70	with	Treatment	917:925	arg1	H					974:974	Endo H	969:974	Endo H	969:974	Treatment with PNGase F, but not Endoglycosidase H (Endo H) (specific for high-mannose N-linked glycans), produced an equivalent decrease in molecular weight.
16014566	4	70	with	Treatment	917:925	arg1	H					966:966	Endoglycosidase H	950:966	Endoglycosidase H (Endo H) (specific for high-mannose N-linked glycans)	950:1020	Treatment with PNGase F, but not Endoglycosidase H (Endo H) (specific for high-mannose N-linked glycans), produced an equivalent decrease in molecular weight.
16014566	1	71	from	effect	150:155	arg1	N92GS94					236:242	N92GS94	236:242	N92GS94	236:242	Using recombinant human glycoprotein VI (GPVI), we evaluated the effect of N-linked glycosylation at the consensus site Asparagine92-Glycine-Serine94 (N92GS94) on binding of this platelet-specific receptor to its ligands, human type I collagen, collagen-related peptide (CRP), and the snake venom C-type lectin convulxin (CVX).
16014566	1	71	from	effect	150:155	arg1	binding					248:254	binding	248:254	binding of this platelet-specific receptor to its ligands, human type I collagen, collagen-related peptide (CRP), and the snake venom C-type lectin convulxin (CVX)	248:410	Using recombinant human glycoprotein VI (GPVI), we evaluated the effect of N-linked glycosylation at the consensus site Asparagine92-Glycine-Serine94 (N92GS94) on binding of this platelet-specific receptor to its ligands, human type I collagen, collagen-related peptide (CRP), and the snake venom C-type lectin convulxin (CVX).
16014566	1	71	from	effect	150:155	arg1	Asparagine92-Glycine-Serine94					205:233	the consensus site Asparagine92-Glycine-Serine94	186:233	the consensus site Asparagine92-Glycine-Serine94 (N92GS94)	186:243	Using recombinant human glycoprotein VI (GPVI), we evaluated the effect of N-linked glycosylation at the consensus site Asparagine92-Glycine-Serine94 (N92GS94) on binding of this platelet-specific receptor to its ligands, human type I collagen, collagen-related peptide (CRP), and the snake venom C-type lectin convulxin (CVX).
16014566	0	72	from	influence	4:12	arg1	function					47:54	the function	43:54	the function of platelet glycoprotein VI	43:82	The influence of N-linked glycosylation on the function of platelet glycoprotein VI.
16014566	4	73	from	decrease	1046:1053	arg1	weight					1068:1073	molecular weight	1058:1073	molecular weight	1058:1073	Treatment with PNGase F, but not Endoglycosidase H (Endo H) (specific for high-mannose N-linked glycans), produced an equivalent decrease in molecular weight.
16014566	3	74	theme	40	777:778	arg1	%					772:772	%	772:772	%	772:772	In stably transfected Dami cells, the substitutions N92A or S94A, but not L95H, resulted in a 30% to 40% decrease in adhesion to CVX, but a 90% or greater decrease in adhesion to CRP and a 65% to 70% decrease in adhesion to type I collagen.
16014566	5	75	theme	GPVI	1125:1128	arg1	expression					1111:1120	the expression	1107:1120	the expression	1107:1120	Neither N92A nor S94A affected the expression of GPVI, based on the direct binding of murine anti-human GPVI monoclonal antibody 204-11 to transfected Dami cells.
16014566	3	76	dep	%	772:772	arg1	to					774:775	to	774:775	to	774:775	In stably transfected Dami cells, the substitutions N92A or S94A, but not L95H, resulted in a 30% to 40% decrease in adhesion to CVX, but a 90% or greater decrease in adhesion to CRP and a 65% to 70% decrease in adhesion to type I collagen.
16014566	0	77	gly	glycoprotein	68:79	arg1	glycoprotein					68:79	platelet glycoprotein VI	59:82	platelet glycoprotein VI	59:82	The influence of N-linked glycosylation on the function of platelet glycoprotein VI.
16014566	1	78	link	N-linked	160:167	arg1	glycosylation					169:181	N-linked glycosylation	160:181	N-linked glycosylation at the consensus site Asparagine92-Glycine-Serine94 (N92GS94)	160:243	Using recombinant human glycoprotein VI (GPVI), we evaluated the effect of N-linked glycosylation at the consensus site Asparagine92-Glycine-Serine94 (N92GS94) on binding of this platelet-specific receptor to its ligands, human type I collagen, collagen-related peptide (CRP), and the snake venom C-type lectin convulxin (CVX).
16014566	2	79	theme	cell	642:645	arg1	binding					647:653	transfected COS-7 cell binding	624:653	transfected COS-7 cell binding to both CRP and CVX	624:673	In COS-7 cells transiently transfected with GPVI, deglycosylation with peptide-N-glycosidase F (PNGase F; specific for complex N-linked glycans) or tunicamycin decreases the molecular weight of GPVI and reduces transfected COS-7 cell binding to both CRP and CVX.
16014566	3	80	theme	I	905:905	arg1	collagen					907:914	type I collagen	900:914	type I collagen	900:914	In stably transfected Dami cells, the substitutions N92A or S94A, but not L95H, resulted in a 30% to 40% decrease in adhesion to CVX, but a 90% or greater decrease in adhesion to CRP and a 65% to 70% decrease in adhesion to type I collagen.
16014566	2	81	theme	transfected	624:634	arg1	binding					647:653	transfected COS-7 cell binding	624:653	transfected COS-7 cell binding to both CRP and CVX	624:673	In COS-7 cells transiently transfected with GPVI, deglycosylation with peptide-N-glycosidase F (PNGase F; specific for complex N-linked glycans) or tunicamycin decreases the molecular weight of GPVI and reduces transfected COS-7 cell binding to both CRP and CVX.
16014566	0	82	theme	N-linked	17:24	arg1	glycosylation					26:38	N-linked glycosylation	17:38	N-linked glycosylation	17:38	The influence of N-linked glycosylation on the function of platelet glycoprotein VI.
16014566	1	83	theme	platelet-specific	264:280	arg1	receptor					282:289	this platelet-specific receptor	259:289	this platelet-specific receptor	259:289	Using recombinant human glycoprotein VI (GPVI), we evaluated the effect of N-linked glycosylation at the consensus site Asparagine92-Glycine-Serine94 (N92GS94) on binding of this platelet-specific receptor to its ligands, human type I collagen, collagen-related peptide (CRP), and the snake venom C-type lectin convulxin (CVX).
16014566	3	84	dep	decrease	781:788	arg1	%					779:779	%	779:779	%	779:779	In stably transfected Dami cells, the substitutions N92A or S94A, but not L95H, resulted in a 30% to 40% decrease in adhesion to CVX, but a 90% or greater decrease in adhesion to CRP and a 65% to 70% decrease in adhesion to type I collagen.
16014566	1	85	theme	recombinant	91:101	arg1	glycoprotein					109:120	human glycoprotein VI (GPVI)	103:130	recombinant human glycoprotein VI (GPVI)	91:130	Using recombinant human glycoprotein VI (GPVI), we evaluated the effect of N-linked glycosylation at the consensus site Asparagine92-Glycine-Serine94 (N92GS94) on binding of this platelet-specific receptor to its ligands, human type I collagen, collagen-related peptide (CRP), and the snake venom C-type lectin convulxin (CVX).
16014566	3	86	theme	90	816:817	arg1	%					818:818	%	818:818	%	818:818	In stably transfected Dami cells, the substitutions N92A or S94A, but not L95H, resulted in a 30% to 40% decrease in adhesion to CVX, but a 90% or greater decrease in adhesion to CRP and a 65% to 70% decrease in adhesion to type I collagen.
16014566	2	87	theme	COS-7	416:420	arg1	cells					422:426	COS-7 cells	416:426	COS-7 cells transiently transfected with GPVI	416:460	In COS-7 cells transiently transfected with GPVI, deglycosylation with peptide-N-glycosidase F (PNGase F; specific for complex N-linked glycans) or tunicamycin decreases the molecular weight of GPVI and reduces transfected COS-7 cell binding to both CRP and CVX.
16014566	5	88	theme	murine	1162:1167	arg1	antibody					1196:1203	murine anti-human GPVI monoclonal antibody 204-11	1162:1210	murine anti-human GPVI monoclonal antibody 204-11	1162:1210	Neither N92A nor S94A affected the expression of GPVI, based on the direct binding of murine anti-human GPVI monoclonal antibody 204-11 to transfected Dami cells.
16014566	6	89	gly	glycosylation	1277:1289	arg1	N92					1294:1296	N92	1294:1296	N92	1294:1296	These findings indicate that N-linked glycosylation at N92 in human GPVI is not required for surface expression, but contributes to maximal adhesion to type I collagen, CRP and, to a lesser extent, CVX.
16014566	6	89	gly	glycosylation	1277:1289	arg2	N92					1294:1296	N92	1294:1296	N92	1294:1296	These findings indicate that N-linked glycosylation at N92 in human GPVI is not required for surface expression, but contributes to maximal adhesion to type I collagen, CRP and, to a lesser extent, CVX.
16014566	6	89	gly	glycosylation	1277:1289	arg1	surface					1332:1338	surface expression	1332:1349	surface expression	1332:1349	These findings indicate that N-linked glycosylation at N92 in human GPVI is not required for surface expression, but contributes to maximal adhesion to type I collagen, CRP and, to a lesser extent, CVX.
16014566	6	89	gly	glycosylation	1277:1289	arg1	GPVI					1307:1310	human GPVI	1301:1310	human GPVI	1301:1310	These findings indicate that N-linked glycosylation at N92 in human GPVI is not required for surface expression, but contributes to maximal adhesion to type I collagen, CRP and, to a lesser extent, CVX.
16014566	4	90	theme	molecular	1058:1066	arg1	weight					1068:1073	molecular weight	1058:1073	molecular weight	1058:1073	Treatment with PNGase F, but not Endoglycosidase H (Endo H) (specific for high-mannose N-linked glycans), produced an equivalent decrease in molecular weight.
16014566	5	91	theme	GPVI	1180:1183	arg1	antibody					1196:1203	murine anti-human GPVI monoclonal antibody 204-11	1162:1210	murine anti-human GPVI monoclonal antibody 204-11	1162:1210	Neither N92A nor S94A affected the expression of GPVI, based on the direct binding of murine anti-human GPVI monoclonal antibody 204-11 to transfected Dami cells.
16014566	1	92	theme	human	307:311	arg1	collagen					320:327	human type I collagen	307:327	human type I collagen	307:327	Using recombinant human glycoprotein VI (GPVI), we evaluated the effect of N-linked glycosylation at the consensus site Asparagine92-Glycine-Serine94 (N92GS94) on binding of this platelet-specific receptor to its ligands, human type I collagen, collagen-related peptide (CRP), and the snake venom C-type lectin convulxin (CVX).
16014566	1	92	theme	human	307:311	arg1	ligands					298:304	its ligands	294:304	its ligands	294:304	Using recombinant human glycoprotein VI (GPVI), we evaluated the effect of N-linked glycosylation at the consensus site Asparagine92-Glycine-Serine94 (N92GS94) on binding of this platelet-specific receptor to its ligands, human type I collagen, collagen-related peptide (CRP), and the snake venom C-type lectin convulxin (CVX).
16014566	0	93	gly	glycosylation	26:38	arg1	glycoprotein					68:79	platelet glycoprotein VI	59:82	platelet glycoprotein VI	59:82	The influence of N-linked glycosylation on the function of platelet glycoprotein VI.
16014566	2	94	link	N-linked	540:547	arg1	glycans					549:555	complex N-linked glycans	532:555	complex N-linked glycans	532:555	In COS-7 cells transiently transfected with GPVI, deglycosylation with peptide-N-glycosidase F (PNGase F; specific for complex N-linked glycans) or tunicamycin decreases the molecular weight of GPVI and reduces transfected COS-7 cell binding to both CRP and CVX.
16014566	6	95	theme	N-linked	1268:1275	arg1	glycosylation					1277:1289	N-linked glycosylation	1268:1289	N-linked glycosylation at N92 in human GPVI	1268:1310	These findings indicate that N-linked glycosylation at N92 in human GPVI is not required for surface expression, but contributes to maximal adhesion to type I collagen, CRP and, to a lesser extent, CVX.
17975018	5	0	theme	blood	691:695	arg1	sugars					703:708	ABO(H) blood group sugars	684:708	ABO(H) blood group sugars	684:708	Occupancy of the N-linked glycan sites at N1515 and N1574 and their presentation of ABO(H) blood group sugars were confirmed with an isolated tryptic fragment.
17975018	1	1	with	interaction	136:146	arg1	ADAMTS13					153:160	ADAMTS13	153:160	ADAMTS13	153:160	We examined the role of N-linked glycan structures of VWF on its interaction with ADAMTS13.
17975018	7	2	theme	proteolysis	907:917	arg1	rate					890:893	rate	890:893	rate of ADAMTS13 proteolysis	890:917	Mutation of N1515 did not alter ADAMTS13 binding or increase rate of ADAMTS13 proteolysis.
17975018	8	3	theme	urea	1037:1040	arg1	absence					1026:1032	the absence	1022:1032	the absence of urea	1022:1040	Mutation of N1574 increased the susceptibility of VWF to ADAMTS13 proteolysis and allowed cleavage in the absence of urea.
17975018	5	4	theme	group	697:701	arg1	sugars					703:708	ABO(H) blood group sugars	684:708	ABO(H) blood group sugars	684:708	Occupancy of the N-linked glycan sites at N1515 and N1574 and their presentation of ABO(H) blood group sugars were confirmed with an isolated tryptic fragment.
17975018	8	5	theme	VWF	970:972	arg1	susceptibility					952:965	the susceptibility	948:965	the susceptibility of VWF to ADAMTS13 proteolysis	948:996	Mutation of N1574 increased the susceptibility of VWF to ADAMTS13 proteolysis and allowed cleavage in the absence of urea.
17975018	4	6	theme	control	539:545	arg1	VWF					547:549	control VWF	539:549	control VWF	539:549	PNG-VWF was cleaved by ADAMTS13 faster than control VWF and was also proteolysed in the absence of urea.
17975018	2	7	theme	chains	265:270	arg1	chains					265:270	VWF N-linked glycan chains	245:270	VWF N-linked glycan chains	245:270	PNGase F digestion followed by lectin analysis demonstrated that more than 90% of VWF N-linked glycan chains could be removed from the molecule (PNG-VWF) without disruption of its multimeric structure or its ability to bind to collagen.
17975018	2	7	theme	chains	265:270	arg1	%					240:240	more than 90%	228:240	more than 90% of VWF N-linked glycan chains	228:270	PNGase F digestion followed by lectin analysis demonstrated that more than 90% of VWF N-linked glycan chains could be removed from the molecule (PNG-VWF) without disruption of its multimeric structure or its ability to bind to collagen.
17975018	10	8	theme	N-linked	1184:1191	arg1	glycans					1193:1199	the N-linked glycans	1180:1199	the N-linked glycans of VWF	1180:1206	These data demonstrate that the N-linked glycans of VWF have a modulatory effect on the interaction with ADAMTS13.
17975018	5	9	theme	N-linked	617:624	arg1	sites					633:637	the N-linked glycan sites	613:637	the N-linked glycan sites at N1515 and N1574	613:656	Occupancy of the N-linked glycan sites at N1515 and N1574 and their presentation of ABO(H) blood group sugars were confirmed with an isolated tryptic fragment.
17975018	2	10	theme	glycan	258:263	arg1	chains					265:270	VWF N-linked glycan chains	245:270	VWF N-linked glycan chains	245:270	PNGase F digestion followed by lectin analysis demonstrated that more than 90% of VWF N-linked glycan chains could be removed from the molecule (PNG-VWF) without disruption of its multimeric structure or its ability to bind to collagen.
17975018	5	11	from	N1574	652:656	arg1	presentation					668:679	their presentation	662:679	their presentation of ABO(H) blood group sugars	662:708	Occupancy of the N-linked glycan sites at N1515 and N1574 and their presentation of ABO(H) blood group sugars were confirmed with an isolated tryptic fragment.
17975018	5	11	from	N1574	652:656	arg1	sites					633:637	the N-linked glycan sites	613:637	the N-linked glycan sites at N1515 and N1574	613:656	Occupancy of the N-linked glycan sites at N1515 and N1574 and their presentation of ABO(H) blood group sugars were confirmed with an isolated tryptic fragment.
17975018	5	11	from	N1574	652:656	arg1	Occupancy					600:608	Occupancy	600:608	Occupancy of the N-linked glycan sites at N1515 and N1574	600:656	Occupancy of the N-linked glycan sites at N1515 and N1574 and their presentation of ABO(H) blood group sugars were confirmed with an isolated tryptic fragment.
17975018	5	12	theme	ABO	684:686	arg1	sugars					703:708	ABO(H) blood group sugars	684:708	ABO(H) blood group sugars	684:708	Occupancy of the N-linked glycan sites at N1515 and N1574 and their presentation of ABO(H) blood group sugars were confirmed with an isolated tryptic fragment.
17975018	0	13	link	N-linked	0:7	arg1	glycosylation					9:21	N-linked glycosylation	0:21	N-linked glycosylation of VWF	0:28	N-linked glycosylation of VWF modulates its interaction with ADAMTS13.
17975018	2	14	theme	N-linked	249:256	arg1	chains					265:270	VWF N-linked glycan chains	245:270	VWF N-linked glycan chains	245:270	PNGase F digestion followed by lectin analysis demonstrated that more than 90% of VWF N-linked glycan chains could be removed from the molecule (PNG-VWF) without disruption of its multimeric structure or its ability to bind to collagen.
17975018	10	15	theme	modulatory	1215:1224	arg1	effect					1226:1231	a modulatory effect	1213:1231	a modulatory effect	1213:1231	These data demonstrate that the N-linked glycans of VWF have a modulatory effect on the interaction with ADAMTS13.
17975018	8	16	theme	ADAMTS13	977:984	arg1	proteolysis					986:996	ADAMTS13 proteolysis	977:996	ADAMTS13 proteolysis	977:996	Mutation of N1574 increased the susceptibility of VWF to ADAMTS13 proteolysis and allowed cleavage in the absence of urea.
17975018	7	17	theme	ADAMTS13	861:868	arg1	binding					870:876	ADAMTS13 binding	861:876	ADAMTS13 binding	861:876	Mutation of N1515 did not alter ADAMTS13 binding or increase rate of ADAMTS13 proteolysis.
17975018	2	18	theme	VWF	245:247	arg1	chains					265:270	VWF N-linked glycan chains	245:270	VWF N-linked glycan chains	245:270	PNGase F digestion followed by lectin analysis demonstrated that more than 90% of VWF N-linked glycan chains could be removed from the molecule (PNG-VWF) without disruption of its multimeric structure or its ability to bind to collagen.
17975018	2	19	theme	structure	354:362	arg1	ability					371:377	its ability to bind to collagen	367:397	its ability to bind to collagen	367:397	PNGase F digestion followed by lectin analysis demonstrated that more than 90% of VWF N-linked glycan chains could be removed from the molecule (PNG-VWF) without disruption of its multimeric structure or its ability to bind to collagen.
17975018	2	19	theme	structure	354:362	arg1	disruption					325:334	disruption	325:334	disruption of its multimeric structure	325:362	PNGase F digestion followed by lectin analysis demonstrated that more than 90% of VWF N-linked glycan chains could be removed from the molecule (PNG-VWF) without disruption of its multimeric structure or its ability to bind to collagen.
17975018	9	20	theme	ADAMTS13	1130:1137	arg1	proteolysis					1139:1149	ADAMTS13 proteolysis	1130:1149	ADAMTS13 proteolysis	1130:1149	Mutation of N1574 in the isolated recombinant VWF-A2 domain also increased binding and ADAMTS13 proteolysis.
17975018	2	21	link	N-linked	249:256	arg1	chains					265:270	VWF N-linked glycan chains	245:270	VWF N-linked glycan chains	245:270	PNGase F digestion followed by lectin analysis demonstrated that more than 90% of VWF N-linked glycan chains could be removed from the molecule (PNG-VWF) without disruption of its multimeric structure or its ability to bind to collagen.
17975018	2	22	theme	multimeric	343:352	arg1	structure					354:362	its multimeric structure	339:362	its multimeric structure	339:362	PNGase F digestion followed by lectin analysis demonstrated that more than 90% of VWF N-linked glycan chains could be removed from the molecule (PNG-VWF) without disruption of its multimeric structure or its ability to bind to collagen.
17975018	0	23	theme	N-linked	0:7	arg1	glycosylation					9:21	N-linked glycosylation	0:21	N-linked glycosylation of VWF	0:28	N-linked glycosylation of VWF modulates its interaction with ADAMTS13.
17975018	2	24	attach	removed	281:287	arg1	PNG-VWF					308:314	PNG-VWF	308:314	PNG-VWF	308:314	PNGase F digestion followed by lectin analysis demonstrated that more than 90% of VWF N-linked glycan chains could be removed from the molecule (PNG-VWF) without disruption of its multimeric structure or its ability to bind to collagen.
17975018	2	24	attach	removed	281:287	arg2	%					240:240	more than 90%	228:240	more than 90% of VWF N-linked glycan chains	228:270	PNGase F digestion followed by lectin analysis demonstrated that more than 90% of VWF N-linked glycan chains could be removed from the molecule (PNG-VWF) without disruption of its multimeric structure or its ability to bind to collagen.
17975018	2	24	attach	removed	281:287	arg2	chains					265:270	VWF N-linked glycan chains	245:270	VWF N-linked glycan chains	245:270	PNGase F digestion followed by lectin analysis demonstrated that more than 90% of VWF N-linked glycan chains could be removed from the molecule (PNG-VWF) without disruption of its multimeric structure or its ability to bind to collagen.
17975018	2	24	attach	removed	281:287	arg1	molecule					298:305	the molecule	294:305	the molecule (PNG-VWF)	294:315	PNGase F digestion followed by lectin analysis demonstrated that more than 90% of VWF N-linked glycan chains could be removed from the molecule (PNG-VWF) without disruption of its multimeric structure or its ability to bind to collagen.
17975018	10	25	with	interaction	1240:1250	arg1	ADAMTS13					1257:1264	ADAMTS13	1257:1264	ADAMTS13	1257:1264	These data demonstrate that the N-linked glycans of VWF have a modulatory effect on the interaction with ADAMTS13.
17975018	11	26	theme	steric	1319:1324	arg1	hindrance					1326:1334	steric hindrance	1319:1334	steric hindrance	1319:1334	At least part of this effect is conformational, but steric hindrance may also be important.
17975018	3	27	contain	had	408:410	arg1	PNG-VWF					400:406	PNG-VWF	400:406	PNG-VWF	400:406	PNG-VWF had an approximately 4-fold increased affinity for ADAMTS13 compared with control VWF.
17975018	3	27	contain	had	408:410	arg2	affinity					446:453	an approximately 4-fold increased affinity	412:453	an approximately 4-fold increased affinity for ADAMTS13	412:466	PNG-VWF had an approximately 4-fold increased affinity for ADAMTS13 compared with control VWF.
17975018	0	28	theme	VWF	26:28	arg1	glycosylation					9:21	N-linked glycosylation	0:21	N-linked glycosylation of VWF	0:28	N-linked glycosylation of VWF modulates its interaction with ADAMTS13.
17975018	5	29	theme	isolated	733:740	arg1	fragment					750:757	an isolated tryptic fragment	730:757	an isolated tryptic fragment	730:757	Occupancy of the N-linked glycan sites at N1515 and N1574 and their presentation of ABO(H) blood group sugars were confirmed with an isolated tryptic fragment.
17975018	5	30	link	N-linked	617:624	arg1	sites					633:637	the N-linked glycan sites	613:637	the N-linked glycan sites at N1515 and N1574	613:656	Occupancy of the N-linked glycan sites at N1515 and N1574 and their presentation of ABO(H) blood group sugars were confirmed with an isolated tryptic fragment.
17975018	6	31	gly	glycosylation	799:811	arg1	sites					822:826	these sites	816:826	these sites	816:826	Recombinant VWF was mutated to prevent glycosylation at these sites.
17975018	9	32	theme	recombinant	1077:1087	arg1	domain					1096:1101	the isolated recombinant VWF-A2 domain	1064:1101	the isolated recombinant VWF-A2 domain	1064:1101	Mutation of N1574 in the isolated recombinant VWF-A2 domain also increased binding and ADAMTS13 proteolysis.
17975018	2	33	theme	F	170:170	arg1	digestion					172:180	PNGase F digestion	163:180	PNGase F digestion followed by lectin analysis	163:208	PNGase F digestion followed by lectin analysis demonstrated that more than 90% of VWF N-linked glycan chains could be removed from the molecule (PNG-VWF) without disruption of its multimeric structure or its ability to bind to collagen.
17975018	1	34	theme	N-linked	95:102	arg1	structures					111:120	N-linked glycan structures	95:120	N-linked glycan structures of VWF	95:127	We examined the role of N-linked glycan structures of VWF on its interaction with ADAMTS13.
17975018	3	35	theme	4-fold	429:434	arg1	affinity					446:453	an approximately 4-fold increased affinity	412:453	an approximately 4-fold increased affinity for ADAMTS13	412:466	PNG-VWF had an approximately 4-fold increased affinity for ADAMTS13 compared with control VWF.
17975018	5	36	theme	sugars	703:708	arg1	presentation					668:679	their presentation	662:679	their presentation of ABO(H) blood group sugars	662:708	Occupancy of the N-linked glycan sites at N1515 and N1574 and their presentation of ABO(H) blood group sugars were confirmed with an isolated tryptic fragment.
17975018	5	36	theme	sugars	703:708	arg1	Occupancy					600:608	Occupancy	600:608	Occupancy of the N-linked glycan sites at N1515 and N1574	600:656	Occupancy of the N-linked glycan sites at N1515 and N1574 and their presentation of ABO(H) blood group sugars were confirmed with an isolated tryptic fragment.
17975018	4	37	theme	faster	527:532	arg1	ADAMTS13					518:525	ADAMTS13	518:525	ADAMTS13 faster than control VWF	518:549	PNG-VWF was cleaved by ADAMTS13 faster than control VWF and was also proteolysed in the absence of urea.
17975018	2	38	theme	PNGase	163:168	arg1	digestion					172:180	PNGase F digestion	163:180	PNGase F digestion followed by lectin analysis	163:208	PNGase F digestion followed by lectin analysis demonstrated that more than 90% of VWF N-linked glycan chains could be removed from the molecule (PNG-VWF) without disruption of its multimeric structure or its ability to bind to collagen.
17975018	11	39	theme	effect	1289:1294	arg1	part					1276:1279	At least part	1267:1279	At least part of this effect	1267:1294	At least part of this effect is conformational, but steric hindrance may also be important.
17975018	5	40	from	presentation	668:679	arg1	N1574					652:656	N1574	652:656	N1574	652:656	Occupancy of the N-linked glycan sites at N1515 and N1574 and their presentation of ABO(H) blood group sugars were confirmed with an isolated tryptic fragment.
17975018	5	40	from	presentation	668:679	arg1	N1515					642:646	N1515	642:646	N1515	642:646	Occupancy of the N-linked glycan sites at N1515 and N1574 and their presentation of ABO(H) blood group sugars were confirmed with an isolated tryptic fragment.
17975018	0	41	gly	glycosylation	9:21	arg1	VWF					26:28	VWF	26:28	VWF	26:28	N-linked glycosylation of VWF modulates its interaction with ADAMTS13.
17975018	4	42	theme	urea	594:597	arg1	absence					583:589	the absence	579:589	the absence of urea	579:597	PNG-VWF was cleaved by ADAMTS13 faster than control VWF and was also proteolysed in the absence of urea.
17975018	5	43	theme	glycan	626:631	arg1	sites					633:637	the N-linked glycan sites	613:637	the N-linked glycan sites at N1515 and N1574	613:656	Occupancy of the N-linked glycan sites at N1515 and N1574 and their presentation of ABO(H) blood group sugars were confirmed with an isolated tryptic fragment.
17975018	9	44	theme	N1574	1055:1059	arg1	Mutation					1043:1050	Mutation	1043:1050	Mutation of N1574 in the isolated recombinant VWF-A2 domain	1043:1101	Mutation of N1574 in the isolated recombinant VWF-A2 domain also increased binding and ADAMTS13 proteolysis.
17975018	1	45	theme	glycan	104:109	arg1	structures					111:120	N-linked glycan structures	95:120	N-linked glycan structures of VWF	95:127	We examined the role of N-linked glycan structures of VWF on its interaction with ADAMTS13.
17975018	10	46	link	N-linked	1184:1191	arg1	glycans					1193:1199	the N-linked glycans	1180:1199	the N-linked glycans of VWF	1180:1206	These data demonstrate that the N-linked glycans of VWF have a modulatory effect on the interaction with ADAMTS13.
17975018	5	47	from	Occupancy	600:608	arg1	N1574					652:656	N1574	652:656	N1574	652:656	Occupancy of the N-linked glycan sites at N1515 and N1574 and their presentation of ABO(H) blood group sugars were confirmed with an isolated tryptic fragment.
17975018	5	47	from	Occupancy	600:608	arg1	N1515					642:646	N1515	642:646	N1515	642:646	Occupancy of the N-linked glycan sites at N1515 and N1574 and their presentation of ABO(H) blood group sugars were confirmed with an isolated tryptic fragment.
17975018	5	48	theme	sites	633:637	arg1	presentation					668:679	their presentation	662:679	their presentation of ABO(H) blood group sugars	662:708	Occupancy of the N-linked glycan sites at N1515 and N1574 and their presentation of ABO(H) blood group sugars were confirmed with an isolated tryptic fragment.
17975018	5	48	theme	sites	633:637	arg1	Occupancy					600:608	Occupancy	600:608	Occupancy of the N-linked glycan sites at N1515 and N1574	600:656	Occupancy of the N-linked glycan sites at N1515 and N1574 and their presentation of ABO(H) blood group sugars were confirmed with an isolated tryptic fragment.
17975018	2	49	theme	lectin	194:199	arg1	analysis					201:208	lectin analysis	194:208	lectin analysis	194:208	PNGase F digestion followed by lectin analysis demonstrated that more than 90% of VWF N-linked glycan chains could be removed from the molecule (PNG-VWF) without disruption of its multimeric structure or its ability to bind to collagen.
17975018	5	50	theme	tryptic	742:748	arg1	fragment					750:757	an isolated tryptic fragment	730:757	an isolated tryptic fragment	730:757	Occupancy of the N-linked glycan sites at N1515 and N1574 and their presentation of ABO(H) blood group sugars were confirmed with an isolated tryptic fragment.
17975018	1	51	theme	structures	111:120	arg1	role					87:90	the role	83:90	the role of N-linked glycan structures of VWF on its interaction with ADAMTS13	83:160	We examined the role of N-linked glycan structures of VWF on its interaction with ADAMTS13.
17975018	7	52	theme	N1515	841:845	arg1	Mutation					829:836	Mutation	829:836	Mutation of N1515	829:845	Mutation of N1515 did not alter ADAMTS13 binding or increase rate of ADAMTS13 proteolysis.
17975018	8	53	theme	N1574	932:936	arg1	Mutation					920:927	Mutation	920:927	Mutation of N1574	920:936	Mutation of N1574 increased the susceptibility of VWF to ADAMTS13 proteolysis and allowed cleavage in the absence of urea.
17975018	9	54	from	Mutation	1043:1050	arg1	domain					1096:1101	the isolated recombinant VWF-A2 domain	1064:1101	the isolated recombinant VWF-A2 domain	1064:1101	Mutation of N1574 in the isolated recombinant VWF-A2 domain also increased binding and ADAMTS13 proteolysis.
17975018	3	55	theme	increased	436:444	arg1	affinity					446:453	an approximately 4-fold increased affinity	412:453	an approximately 4-fold increased affinity for ADAMTS13	412:466	PNG-VWF had an approximately 4-fold increased affinity for ADAMTS13 compared with control VWF.
17975018	9	56	theme	VWF-A2	1089:1094	arg1	domain					1096:1101	the isolated recombinant VWF-A2 domain	1064:1101	the isolated recombinant VWF-A2 domain	1064:1101	Mutation of N1574 in the isolated recombinant VWF-A2 domain also increased binding and ADAMTS13 proteolysis.
17975018	6	57	theme	Recombinant	760:770	arg1	VWF					772:774	Recombinant VWF	760:774	Recombinant VWF	760:774	Recombinant VWF was mutated to prevent glycosylation at these sites.
17975018	9	58	theme	isolated	1068:1075	arg1	domain					1096:1101	the isolated recombinant VWF-A2 domain	1064:1101	the isolated recombinant VWF-A2 domain	1064:1101	Mutation of N1574 in the isolated recombinant VWF-A2 domain also increased binding and ADAMTS13 proteolysis.
17975018	1	59	theme	VWF	125:127	arg1	structures					111:120	N-linked glycan structures	95:120	N-linked glycan structures of VWF	95:127	We examined the role of N-linked glycan structures of VWF on its interaction with ADAMTS13.
17975018	5	60	from	N1515	642:646	arg1	presentation					668:679	their presentation	662:679	their presentation of ABO(H) blood group sugars	662:708	Occupancy of the N-linked glycan sites at N1515 and N1574 and their presentation of ABO(H) blood group sugars were confirmed with an isolated tryptic fragment.
17975018	5	60	from	N1515	642:646	arg1	sites					633:637	the N-linked glycan sites	613:637	the N-linked glycan sites at N1515 and N1574	613:656	Occupancy of the N-linked glycan sites at N1515 and N1574 and their presentation of ABO(H) blood group sugars were confirmed with an isolated tryptic fragment.
17975018	5	60	from	N1515	642:646	arg1	Occupancy					600:608	Occupancy	600:608	Occupancy of the N-linked glycan sites at N1515 and N1574	600:656	Occupancy of the N-linked glycan sites at N1515 and N1574 and their presentation of ABO(H) blood group sugars were confirmed with an isolated tryptic fragment.
17975018	5	61	theme	H	688:688	arg1	sugars					703:708	ABO(H) blood group sugars	684:708	ABO(H) blood group sugars	684:708	Occupancy of the N-linked glycan sites at N1515 and N1574 and their presentation of ABO(H) blood group sugars were confirmed with an isolated tryptic fragment.
17975018	0	62	with	interaction	44:54	arg1	ADAMTS13					61:68	ADAMTS13	61:68	ADAMTS13	61:68	N-linked glycosylation of VWF modulates its interaction with ADAMTS13.
17975018	3	63	theme	control	482:488	arg1	VWF					490:492	control VWF	482:492	control VWF	482:492	PNG-VWF had an approximately 4-fold increased affinity for ADAMTS13 compared with control VWF.
17975018	1	64	from	role	87:90	arg1	interaction					136:146	its interaction	132:146	its interaction with ADAMTS13	132:160	We examined the role of N-linked glycan structures of VWF on its interaction with ADAMTS13.
17975018	1	65	link	N-linked	95:102	arg1	structures					111:120	N-linked glycan structures	95:120	N-linked glycan structures of VWF	95:127	We examined the role of N-linked glycan structures of VWF on its interaction with ADAMTS13.
17975018	10	66	contain	have	1208:1211	arg1	glycans					1193:1199	the N-linked glycans	1180:1199	the N-linked glycans of VWF	1180:1206	These data demonstrate that the N-linked glycans of VWF have a modulatory effect on the interaction with ADAMTS13.
17975018	10	66	contain	have	1208:1211	arg2	effect					1226:1231	a modulatory effect	1213:1231	a modulatory effect	1213:1231	These data demonstrate that the N-linked glycans of VWF have a modulatory effect on the interaction with ADAMTS13.
17975018	7	67	theme	ADAMTS13	898:905	arg1	proteolysis					907:917	ADAMTS13 proteolysis	898:917	ADAMTS13 proteolysis	898:917	Mutation of N1515 did not alter ADAMTS13 binding or increase rate of ADAMTS13 proteolysis.
17975018	10	68	theme	VWF	1204:1206	arg1	glycans					1193:1199	the N-linked glycans	1180:1199	the N-linked glycans of VWF	1180:1206	These data demonstrate that the N-linked glycans of VWF have a modulatory effect on the interaction with ADAMTS13.
28074064	5	0	theme	STAT5	855:859	arg1	expression					796:805	The expression	792:805	The expression of a mutated hyperactive gain-of-function (GOF) STAT5 without O-GlcNAcylation	792:883	The expression of a mutated hyperactive gain-of-function (GOF) STAT5 without O-GlcNAcylation resulted in decreased tyrosine phosphorylation, oligomerization and transactivation potential and complete loss of oncogenic transformation capacity.
28074064	6	1	theme	O-GlcNAcylation	1047:1061	arg1	lack					1039:1042	The lack	1035:1042	The lack of O-GlcNAcylation	1035:1061	The lack of O-GlcNAcylation diminished phospho-ERK and phospho-AKT levels.
28074064	0	2	theme	STAT5-dependent	90:104	arg1	malignancies					106:117	STAT5-dependent malignancies	90:117	STAT5-dependent malignancies	90:117	O-GlcNAcylation of STAT5 controls tyrosine phosphorylation and oncogenic transcription in STAT5-dependent malignancies.
28074064	2	3	theme	neoplastic	376:385	arg1	cells					387:391	diverse neoplastic cells	368:391	diverse neoplastic cells	368:391	Upon cytokine stimulation, STAT5 tyrosine phosphorylation (pYSTAT5) is transient, while in diverse neoplastic cells persistent overexpression and enhanced pYSTAT5 are frequently found.
28074064	5	4	theme	mutated	812:818	arg1	STAT5					855:859	a mutated hyperactive gain-of-function (GOF) STAT5	810:859	a mutated hyperactive gain-of-function (GOF) STAT5 without O-GlcNAcylation	810:883	The expression of a mutated hyperactive gain-of-function (GOF) STAT5 without O-GlcNAcylation resulted in decreased tyrosine phosphorylation, oligomerization and transactivation potential and complete loss of oncogenic transformation capacity.
28074064	5	5	theme	capacity	1025:1032	arg1	potential					969:977	transactivation potential	953:977	transactivation potential	953:977	The expression of a mutated hyperactive gain-of-function (GOF) STAT5 without O-GlcNAcylation resulted in decreased tyrosine phosphorylation, oligomerization and transactivation potential and complete loss of oncogenic transformation capacity.
28074064	5	5	theme	capacity	1025:1032	arg1	phosphorylation					916:930	decreased tyrosine phosphorylation	897:930	decreased tyrosine phosphorylation	897:930	The expression of a mutated hyperactive gain-of-function (GOF) STAT5 without O-GlcNAcylation resulted in decreased tyrosine phosphorylation, oligomerization and transactivation potential and complete loss of oncogenic transformation capacity.
28074064	5	5	theme	capacity	1025:1032	arg1	oligomerization					933:947	oligomerization	933:947	oligomerization	933:947	The expression of a mutated hyperactive gain-of-function (GOF) STAT5 without O-GlcNAcylation resulted in decreased tyrosine phosphorylation, oligomerization and transactivation potential and complete loss of oncogenic transformation capacity.
28074064	5	5	theme	capacity	1025:1032	arg1	loss					992:995	complete loss	983:995	complete loss of oncogenic transformation capacity	983:1032	The expression of a mutated hyperactive gain-of-function (GOF) STAT5 without O-GlcNAcylation resulted in decreased tyrosine phosphorylation, oligomerization and transactivation potential and complete loss of oncogenic transformation capacity.
28074064	5	6	theme	hyperactive	820:830	arg1	gain-of-function					832:847	hyperactive gain-of-function	820:847	a mutated hyperactive gain-of-function (GOF) STAT5 without O-GlcNAcylation	810:883	The expression of a mutated hyperactive gain-of-function (GOF) STAT5 without O-GlcNAcylation resulted in decreased tyrosine phosphorylation, oligomerization and transactivation potential and complete loss of oncogenic transformation capacity.
28074064	5	6	theme	hyperactive	820:830	arg1	GOF					850:852	GOF	850:852	GOF	850:852	The expression of a mutated hyperactive gain-of-function (GOF) STAT5 without O-GlcNAcylation resulted in decreased tyrosine phosphorylation, oligomerization and transactivation potential and complete loss of oncogenic transformation capacity.
28074064	7	7	theme	myeloid	1298:1304	arg1	transformation					1306:1319	myeloid transformation	1298:1319	myeloid transformation	1298:1319	Our data show that O-GlcNAcylation of STAT5 is an important process that contributes to oncogenic transcription through enhanced STAT5 tyrosine phosphorylation and oligomerization driving myeloid transformation.
28074064	3	8	theme	pYSTAT5	608:614	arg1	duration					596:603	duration	596:603	duration	596:603	Post-translational modifications might contribute to enhanced STAT5 activation in the context of transformation, but the strength and duration of pYSTAT5 are incompletely understood.
28074064	3	8	theme	pYSTAT5	608:614	arg1	strength					583:590	strength	583:590	strength	583:590	Post-translational modifications might contribute to enhanced STAT5 activation in the context of transformation, but the strength and duration of pYSTAT5 are incompletely understood.
28074064	4	9	from	transcription	757:769	arg1	cells					785:789	neoplastic cells	774:789	neoplastic cells	774:789	We found that O-GlcNAcylation and tyrosine phosphorylation act together to trigger pYSTAT5 levels and oncogenic transcription in neoplastic cells.
28074064	5	10	theme	gain-of-function	832:847	arg1	STAT5					855:859	a mutated hyperactive gain-of-function (GOF) STAT5	810:859	a mutated hyperactive gain-of-function (GOF) STAT5 without O-GlcNAcylation	810:883	The expression of a mutated hyperactive gain-of-function (GOF) STAT5 without O-GlcNAcylation resulted in decreased tyrosine phosphorylation, oligomerization and transactivation potential and complete loss of oncogenic transformation capacity.
28074064	5	11	theme	transactivation	953:967	arg1	potential					969:977	transactivation potential	953:977	transactivation potential	953:977	The expression of a mutated hyperactive gain-of-function (GOF) STAT5 without O-GlcNAcylation resulted in decreased tyrosine phosphorylation, oligomerization and transactivation potential and complete loss of oncogenic transformation capacity.
28074064	5	12	theme	tyrosine	907:914	arg1	phosphorylation					916:930	decreased tyrosine phosphorylation	897:930	decreased tyrosine phosphorylation	897:930	The expression of a mutated hyperactive gain-of-function (GOF) STAT5 without O-GlcNAcylation resulted in decreased tyrosine phosphorylation, oligomerization and transactivation potential and complete loss of oncogenic transformation capacity.
28074064	2	13	theme	tyrosine	310:317	arg1	phosphorylation					319:333	STAT5 tyrosine phosphorylation	304:333	STAT5 tyrosine phosphorylation (pYSTAT5)	304:343	Upon cytokine stimulation, STAT5 tyrosine phosphorylation (pYSTAT5) is transient, while in diverse neoplastic cells persistent overexpression and enhanced pYSTAT5 are frequently found.
28074064	2	13	theme	tyrosine	310:317	arg1	pYSTAT5					336:342	pYSTAT5	336:342	pYSTAT5	336:342	Upon cytokine stimulation, STAT5 tyrosine phosphorylation (pYSTAT5) is transient, while in diverse neoplastic cells persistent overexpression and enhanced pYSTAT5 are frequently found.
28074064	5	14	theme	complete	983:990	arg1	loss					992:995	complete loss	983:995	complete loss of oncogenic transformation capacity	983:1032	The expression of a mutated hyperactive gain-of-function (GOF) STAT5 without O-GlcNAcylation resulted in decreased tyrosine phosphorylation, oligomerization and transactivation potential and complete loss of oncogenic transformation capacity.
28074064	0	15	from	phosphorylation	43:57	arg1	malignancies					106:117	STAT5-dependent malignancies	90:117	STAT5-dependent malignancies	90:117	O-GlcNAcylation of STAT5 controls tyrosine phosphorylation and oncogenic transcription in STAT5-dependent malignancies.
28074064	2	16	theme	STAT5	304:308	arg1	phosphorylation					319:333	STAT5 tyrosine phosphorylation	304:333	STAT5 tyrosine phosphorylation (pYSTAT5)	304:343	Upon cytokine stimulation, STAT5 tyrosine phosphorylation (pYSTAT5) is transient, while in diverse neoplastic cells persistent overexpression and enhanced pYSTAT5 are frequently found.
28074064	2	16	theme	STAT5	304:308	arg1	pYSTAT5					336:342	pYSTAT5	336:342	pYSTAT5	336:342	Upon cytokine stimulation, STAT5 tyrosine phosphorylation (pYSTAT5) is transient, while in diverse neoplastic cells persistent overexpression and enhanced pYSTAT5 are frequently found.
28074064	8	17	theme	nutrient	1369:1376	arg1	sensing					1378:1384	sensing	1378:1384	sensing	1378:1384	O-GlcNAcylation of STAT5 could be required for nutrient sensing and metabolism of cancer cells.
28074064	0	18	from	transcription	73:85	arg1	malignancies					106:117	STAT5-dependent malignancies	90:117	STAT5-dependent malignancies	90:117	O-GlcNAcylation of STAT5 controls tyrosine phosphorylation and oncogenic transcription in STAT5-dependent malignancies.
28074064	8	19	theme	STAT5	1341:1345	arg1	O-GlcNAcylation					1322:1336	O-GlcNAcylation	1322:1336	O-GlcNAcylation of STAT5	1322:1345	O-GlcNAcylation of STAT5 could be required for nutrient sensing and metabolism of cancer cells.
28074064	7	20	theme	tyrosine	1245:1252	arg1	phosphorylation					1254:1268	enhanced STAT5 tyrosine phosphorylation	1230:1268	enhanced STAT5 tyrosine phosphorylation	1230:1268	Our data show that O-GlcNAcylation of STAT5 is an important process that contributes to oncogenic transcription through enhanced STAT5 tyrosine phosphorylation and oligomerization driving myeloid transformation.
28074064	4	21	from	levels	736:741	arg1	cells					785:789	neoplastic cells	774:789	neoplastic cells	774:789	We found that O-GlcNAcylation and tyrosine phosphorylation act together to trigger pYSTAT5 levels and oncogenic transcription in neoplastic cells.
28074064	2	22	theme	enhanced	423:430	arg1	pYSTAT5					432:438	enhanced pYSTAT5	423:438	enhanced pYSTAT5	423:438	Upon cytokine stimulation, STAT5 tyrosine phosphorylation (pYSTAT5) is transient, while in diverse neoplastic cells persistent overexpression and enhanced pYSTAT5 are frequently found.
28074064	4	23	theme	oncogenic	747:755	arg1	transcription					757:769	oncogenic transcription	747:769	oncogenic transcription	747:769	We found that O-GlcNAcylation and tyrosine phosphorylation act together to trigger pYSTAT5 levels and oncogenic transcription in neoplastic cells.
28074064	7	24	theme	enhanced	1230:1237	arg1	phosphorylation					1254:1268	enhanced STAT5 tyrosine phosphorylation	1230:1268	enhanced STAT5 tyrosine phosphorylation	1230:1268	Our data show that O-GlcNAcylation of STAT5 is an important process that contributes to oncogenic transcription through enhanced STAT5 tyrosine phosphorylation and oligomerization driving myeloid transformation.
28074064	1	25	theme	signal	124:129	arg1	STAT5					176:180	STAT5	176:180	STAT5	176:180	The signal transducer and activator of transcription 5 (STAT5) regulates differentiation, survival, proliferation and transformation of hematopoietic cells.
28074064	1	25	theme	signal	124:129	arg1	transducer					131:140	The signal transducer	120:140	The signal transducer	120:140	The signal transducer and activator of transcription 5 (STAT5) regulates differentiation, survival, proliferation and transformation of hematopoietic cells.
28074064	0	26	theme	STAT5	19:23	arg1	O-GlcNAcylation					0:14	O-GlcNAcylation	0:14	O-GlcNAcylation of STAT5	0:23	O-GlcNAcylation of STAT5 controls tyrosine phosphorylation and oncogenic transcription in STAT5-dependent malignancies.
28074064	7	27	theme	STAT5	1239:1243	arg1	phosphorylation					1254:1268	enhanced STAT5 tyrosine phosphorylation	1230:1268	enhanced STAT5 tyrosine phosphorylation	1230:1268	Our data show that O-GlcNAcylation of STAT5 is an important process that contributes to oncogenic transcription through enhanced STAT5 tyrosine phosphorylation and oligomerization driving myeloid transformation.
28074064	3	28	dep	strength	583:590	arg1	the					579:581	the	579:581	the	579:581	Post-translational modifications might contribute to enhanced STAT5 activation in the context of transformation, but the strength and duration of pYSTAT5 are incompletely understood.
28074064	5	29	theme	transformation	1010:1023	arg1	capacity					1025:1032	oncogenic transformation capacity	1000:1032	oncogenic transformation capacity	1000:1032	The expression of a mutated hyperactive gain-of-function (GOF) STAT5 without O-GlcNAcylation resulted in decreased tyrosine phosphorylation, oligomerization and transactivation potential and complete loss of oncogenic transformation capacity.
28074064	8	30	theme	cells	1411:1415	arg1	metabolism					1390:1399	metabolism	1390:1399	metabolism	1390:1399	O-GlcNAcylation of STAT5 could be required for nutrient sensing and metabolism of cancer cells.
28074064	8	30	theme	cells	1411:1415	arg1	sensing					1378:1384	sensing	1378:1384	sensing	1378:1384	O-GlcNAcylation of STAT5 could be required for nutrient sensing and metabolism of cancer cells.
28074064	4	31	theme	pYSTAT5	728:734	arg1	levels					736:741	pYSTAT5 levels	728:741	pYSTAT5 levels	728:741	We found that O-GlcNAcylation and tyrosine phosphorylation act together to trigger pYSTAT5 levels and oncogenic transcription in neoplastic cells.
28074064	5	32	theme	oncogenic	1000:1008	arg1	transformation					1010:1023	oncogenic transformation	1000:1023	oncogenic transformation capacity	1000:1032	The expression of a mutated hyperactive gain-of-function (GOF) STAT5 without O-GlcNAcylation resulted in decreased tyrosine phosphorylation, oligomerization and transactivation potential and complete loss of oncogenic transformation capacity.
28074064	3	33	theme	enhanced	515:522	arg1	activation					530:539	enhanced STAT5 activation	515:539	enhanced STAT5 activation	515:539	Post-translational modifications might contribute to enhanced STAT5 activation in the context of transformation, but the strength and duration of pYSTAT5 are incompletely understood.
28074064	0	34	theme	tyrosine	34:41	arg1	phosphorylation					43:57	tyrosine phosphorylation	34:57	tyrosine phosphorylation	34:57	O-GlcNAcylation of STAT5 controls tyrosine phosphorylation and oncogenic transcription in STAT5-dependent malignancies.
28074064	3	35	theme	Post-translational	462:479	arg1	modifications					481:493	Post-translational modifications	462:493	Post-translational modifications	462:493	Post-translational modifications might contribute to enhanced STAT5 activation in the context of transformation, but the strength and duration of pYSTAT5 are incompletely understood.
28074064	7	36	theme	important	1160:1168	arg1	O-GlcNAcylation					1129:1143	O-GlcNAcylation	1129:1143	O-GlcNAcylation of STAT5	1129:1152	Our data show that O-GlcNAcylation of STAT5 is an important process that contributes to oncogenic transcription through enhanced STAT5 tyrosine phosphorylation and oligomerization driving myeloid transformation.
28074064	7	36	theme	important	1160:1168	arg1	process					1170:1176	an important process	1157:1176	an important process that contributes to oncogenic transcription through enhanced STAT5 tyrosine phosphorylation and oligomerization driving myeloid transformation	1157:1319	Our data show that O-GlcNAcylation of STAT5 is an important process that contributes to oncogenic transcription through enhanced STAT5 tyrosine phosphorylation and oligomerization driving myeloid transformation.
28074064	3	37	theme	STAT5	524:528	arg1	activation					530:539	enhanced STAT5 activation	515:539	enhanced STAT5 activation	515:539	Post-translational modifications might contribute to enhanced STAT5 activation in the context of transformation, but the strength and duration of pYSTAT5 are incompletely understood.
28074064	0	38	theme	oncogenic	63:71	arg1	transcription					73:85	oncogenic transcription	63:85	oncogenic transcription	63:85	O-GlcNAcylation of STAT5 controls tyrosine phosphorylation and oncogenic transcription in STAT5-dependent malignancies.
28074064	6	39	theme	phospho-AKT	1090:1100	arg1	levels					1102:1107	phospho-ERK and phospho-AKT levels	1074:1107	levels	1102:1107	The lack of O-GlcNAcylation diminished phospho-ERK and phospho-AKT levels.
28074064	8	40	theme	cancer	1404:1409	arg1	cells					1411:1415	cancer cells	1404:1415	cancer cells	1404:1415	O-GlcNAcylation of STAT5 could be required for nutrient sensing and metabolism of cancer cells.
28074064	2	41	located	found	455:459	arg2	overexpression					404:417	persistent overexpression	393:417	persistent overexpression	393:417	Upon cytokine stimulation, STAT5 tyrosine phosphorylation (pYSTAT5) is transient, while in diverse neoplastic cells persistent overexpression and enhanced pYSTAT5 are frequently found.
28074064	2	41	located	found	455:459	arg1	cells					387:391	diverse neoplastic cells	368:391	diverse neoplastic cells	368:391	Upon cytokine stimulation, STAT5 tyrosine phosphorylation (pYSTAT5) is transient, while in diverse neoplastic cells persistent overexpression and enhanced pYSTAT5 are frequently found.
28074064	2	41	located	found	455:459	arg2	pYSTAT5					432:438	enhanced pYSTAT5	423:438	enhanced pYSTAT5	423:438	Upon cytokine stimulation, STAT5 tyrosine phosphorylation (pYSTAT5) is transient, while in diverse neoplastic cells persistent overexpression and enhanced pYSTAT5 are frequently found.
28074064	2	42	theme	diverse	368:374	arg1	cells					387:391	diverse neoplastic cells	368:391	diverse neoplastic cells	368:391	Upon cytokine stimulation, STAT5 tyrosine phosphorylation (pYSTAT5) is transient, while in diverse neoplastic cells persistent overexpression and enhanced pYSTAT5 are frequently found.
28074064	5	43	theme	decreased	897:905	arg1	phosphorylation					916:930	decreased tyrosine phosphorylation	897:930	decreased tyrosine phosphorylation	897:930	The expression of a mutated hyperactive gain-of-function (GOF) STAT5 without O-GlcNAcylation resulted in decreased tyrosine phosphorylation, oligomerization and transactivation potential and complete loss of oncogenic transformation capacity.
28074064	7	44	theme	oncogenic	1198:1206	arg1	transcription					1208:1220	oncogenic transcription	1198:1220	oncogenic transcription	1198:1220	Our data show that O-GlcNAcylation of STAT5 is an important process that contributes to oncogenic transcription through enhanced STAT5 tyrosine phosphorylation and oligomerization driving myeloid transformation.
28074064	3	45	theme	transformation	559:572	arg1	context					548:554	the context	544:554	the context of transformation	544:572	Post-translational modifications might contribute to enhanced STAT5 activation in the context of transformation, but the strength and duration of pYSTAT5 are incompletely understood.
28074064	6	46	theme	phospho-ERK	1074:1084	arg1	levels					1102:1107	phospho-ERK and phospho-AKT levels	1074:1107	levels	1102:1107	The lack of O-GlcNAcylation diminished phospho-ERK and phospho-AKT levels.
28074064	4	47	theme	tyrosine	679:686	arg1	phosphorylation					688:702	tyrosine phosphorylation	679:702	tyrosine phosphorylation	679:702	We found that O-GlcNAcylation and tyrosine phosphorylation act together to trigger pYSTAT5 levels and oncogenic transcription in neoplastic cells.
28074064	1	48	theme	transcription	159:171	arg1	STAT5					176:180	STAT5	176:180	STAT5	176:180	The signal transducer and activator of transcription 5 (STAT5) regulates differentiation, survival, proliferation and transformation of hematopoietic cells.
28074064	1	48	theme	transcription	159:171	arg1	activator					146:154	activator	146:154	activator of transcription 5	146:173	The signal transducer and activator of transcription 5 (STAT5) regulates differentiation, survival, proliferation and transformation of hematopoietic cells.
28074064	1	48	theme	transcription	159:171	arg1	transducer					131:140	The signal transducer	120:140	The signal transducer	120:140	The signal transducer and activator of transcription 5 (STAT5) regulates differentiation, survival, proliferation and transformation of hematopoietic cells.
28074064	1	49	theme	hematopoietic	256:268	arg1	cells					270:274	hematopoietic cells	256:274	hematopoietic cells	256:274	The signal transducer and activator of transcription 5 (STAT5) regulates differentiation, survival, proliferation and transformation of hematopoietic cells.
28074064	2	50	theme	cytokine	282:289	arg1	stimulation					291:301	cytokine stimulation	282:301	cytokine stimulation	282:301	Upon cytokine stimulation, STAT5 tyrosine phosphorylation (pYSTAT5) is transient, while in diverse neoplastic cells persistent overexpression and enhanced pYSTAT5 are frequently found.
28074064	7	51	theme	STAT5	1148:1152	arg1	O-GlcNAcylation					1129:1143	O-GlcNAcylation	1129:1143	O-GlcNAcylation of STAT5	1129:1152	Our data show that O-GlcNAcylation of STAT5 is an important process that contributes to oncogenic transcription through enhanced STAT5 tyrosine phosphorylation and oligomerization driving myeloid transformation.
28074064	7	51	theme	STAT5	1148:1152	arg1	process					1170:1176	an important process	1157:1176	an important process that contributes to oncogenic transcription through enhanced STAT5 tyrosine phosphorylation and oligomerization driving myeloid transformation	1157:1319	Our data show that O-GlcNAcylation of STAT5 is an important process that contributes to oncogenic transcription through enhanced STAT5 tyrosine phosphorylation and oligomerization driving myeloid transformation.
28074064	4	52	theme	neoplastic	774:783	arg1	cells					785:789	neoplastic cells	774:789	neoplastic cells	774:789	We found that O-GlcNAcylation and tyrosine phosphorylation act together to trigger pYSTAT5 levels and oncogenic transcription in neoplastic cells.
28074064	1	53	theme	cells	270:274	arg1	proliferation					220:232	proliferation	220:232	proliferation	220:232	The signal transducer and activator of transcription 5 (STAT5) regulates differentiation, survival, proliferation and transformation of hematopoietic cells.
28074064	1	53	theme	cells	270:274	arg1	survival					210:217	survival	210:217	survival	210:217	The signal transducer and activator of transcription 5 (STAT5) regulates differentiation, survival, proliferation and transformation of hematopoietic cells.
28074064	1	53	theme	cells	270:274	arg1	differentiation					193:207	differentiation	193:207	differentiation	193:207	The signal transducer and activator of transcription 5 (STAT5) regulates differentiation, survival, proliferation and transformation of hematopoietic cells.
28074064	1	53	theme	cells	270:274	arg1	transformation					238:251	transformation	238:251	transformation	238:251	The signal transducer and activator of transcription 5 (STAT5) regulates differentiation, survival, proliferation and transformation of hematopoietic cells.
28074064	2	54	theme	persistent	393:402	arg1	overexpression					404:417	persistent overexpression	393:417	persistent overexpression	393:417	Upon cytokine stimulation, STAT5 tyrosine phosphorylation (pYSTAT5) is transient, while in diverse neoplastic cells persistent overexpression and enhanced pYSTAT5 are frequently found.
19838169	3	0	theme	fragment	344:351	arg1	analysis					353:360	Mass spectrometric fragment analysis	325:360	Mass spectrometric fragment analysis	325:360	Mass spectrometric fragment analysis allowed identification of glycan structures, and additional fragmentation of deglycosylated ions yielded peptide sequence information, which allowed glycan attachment site and protein identification.
19838169	4	1	gly	glycosylation	604:616	arg2	36					576:577	36	576:577	36	576:577	We identified 36 N-linked and 44 O-linked glycosylation sites on glycoproteins from human cerebrospinal fluid.
19838169	4	1	gly	glycosylation	604:616	arg2	sites					618:622	36 N-linked and 44 O-linked glycosylation sites	576:622	36 N-linked and 44 O-linked glycosylation sites	576:622	We identified 36 N-linked and 44 O-linked glycosylation sites on glycoproteins from human cerebrospinal fluid.
19838169	4	2	theme	cerebrospinal	652:664	arg1	fluid					666:670	human cerebrospinal fluid	646:670	human cerebrospinal fluid	646:670	We identified 36 N-linked and 44 O-linked glycosylation sites on glycoproteins from human cerebrospinal fluid.
19838169	4	3	theme	N-linked	579:586	arg1	sites					618:622	36 N-linked and 44 O-linked glycosylation sites	576:622	36 N-linked and 44 O-linked glycosylation sites	576:622	We identified 36 N-linked and 44 O-linked glycosylation sites on glycoproteins from human cerebrospinal fluid.
19838169	2	4	gly	glycoproteins	168:180	arg1	glycoproteins					168:180	Sialylated glycoproteins	157:180	Sialylated glycoproteins	157:180	Sialylated glycoproteins were selectively periodate-oxidized, captured on hydrazide beads, trypsinized and released by acid hydrolysis of sialic acid glycosidic bonds.
19838169	4	5	theme	human	646:650	arg1	fluid					666:670	human cerebrospinal fluid	646:670	human cerebrospinal fluid	646:670	We identified 36 N-linked and 44 O-linked glycosylation sites on glycoproteins from human cerebrospinal fluid.
19838169	3	6	theme	structures	395:404	arg1	identification					370:383	identification	370:383	identification of glycan structures	370:404	Mass spectrometric fragment analysis allowed identification of glycan structures, and additional fragmentation of deglycosylated ions yielded peptide sequence information, which allowed glycan attachment site and protein identification.
19838169	2	7	theme	glycosidic	307:316	arg1	bonds					318:322	sialic acid glycosidic bonds	295:322	sialic acid glycosidic bonds	295:322	Sialylated glycoproteins were selectively periodate-oxidized, captured on hydrazide beads, trypsinized and released by acid hydrolysis of sialic acid glycosidic bonds.
19838169	4	8	from	fluid	666:670	arg1	glycoproteins					627:639	glycoproteins	627:639	glycoproteins from human cerebrospinal fluid	627:670	We identified 36 N-linked and 44 O-linked glycosylation sites on glycoproteins from human cerebrospinal fluid.
19838169	2	9	theme	Sialylated	157:166	arg1	glycoproteins					168:180	Sialylated glycoproteins	157:180	Sialylated glycoproteins	157:180	Sialylated glycoproteins were selectively periodate-oxidized, captured on hydrazide beads, trypsinized and released by acid hydrolysis of sialic acid glycosidic bonds.
19838169	3	10	gly	deglycosylated	439:452	arg1	ions					454:457	deglycosylated ions	439:457	deglycosylated ions	439:457	Mass spectrometric fragment analysis allowed identification of glycan structures, and additional fragmentation of deglycosylated ions yielded peptide sequence information, which allowed glycan attachment site and protein identification.
19838169	2	11	theme	acid	302:305	arg1	bonds					318:322	sialic acid glycosidic bonds	295:322	sialic acid glycosidic bonds	295:322	Sialylated glycoproteins were selectively periodate-oxidized, captured on hydrazide beads, trypsinized and released by acid hydrolysis of sialic acid glycosidic bonds.
19838169	4	12	link	O-linked	595:602	arg1	sites					618:622	36 N-linked and 44 O-linked glycosylation sites	576:622	36 N-linked and 44 O-linked glycosylation sites	576:622	We identified 36 N-linked and 44 O-linked glycosylation sites on glycoproteins from human cerebrospinal fluid.
19838169	1	13	from	samples	148:154	arg1	glycoproteins					119:131	glycoproteins	119:131	glycoproteins from proteomic samples	119:154	We present a method to enrich for glycoproteins from proteomic samples.
19838169	2	14	theme	sialic	295:300	arg1	bonds					318:322	sialic acid glycosidic bonds	295:322	sialic acid glycosidic bonds	295:322	Sialylated glycoproteins were selectively periodate-oxidized, captured on hydrazide beads, trypsinized and released by acid hydrolysis of sialic acid glycosidic bonds.
19838169	3	15	theme	glycan	388:393	arg1	structures					395:404	glycan structures	388:404	glycan structures	388:404	Mass spectrometric fragment analysis allowed identification of glycan structures, and additional fragmentation of deglycosylated ions yielded peptide sequence information, which allowed glycan attachment site and protein identification.
19838169	3	16	theme	sequence	475:482	arg1	information					484:494	peptide sequence information	467:494	peptide sequence information	467:494	Mass spectrometric fragment analysis allowed identification of glycan structures, and additional fragmentation of deglycosylated ions yielded peptide sequence information, which allowed glycan attachment site and protein identification.
19838169	4	17	link	N-linked	579:586	arg1	sites					618:622	36 N-linked and 44 O-linked glycosylation sites	576:622	36 N-linked and 44 O-linked glycosylation sites	576:622	We identified 36 N-linked and 44 O-linked glycosylation sites on glycoproteins from human cerebrospinal fluid.
19838169	0	18	dep	identification	69:82	arg1	Enrichment					0:9	Enrichment	0:9	Enrichment of glycopeptides for glycan structure and attachment site	0:67	Enrichment of glycopeptides for glycan structure and attachment site identification.
19838169	3	19	theme	attachment	518:527	arg1	site					529:532	glycan attachment site	511:532	glycan attachment site	511:532	Mass spectrometric fragment analysis allowed identification of glycan structures, and additional fragmentation of deglycosylated ions yielded peptide sequence information, which allowed glycan attachment site and protein identification.
19838169	0	20	theme	glycopeptides	14:26	arg1	Enrichment					0:9	Enrichment	0:9	Enrichment of glycopeptides for glycan structure and attachment site	0:67	Enrichment of glycopeptides for glycan structure and attachment site identification.
19838169	2	21	theme	bonds	318:322	arg1	hydrolysis					281:290	acid hydrolysis	276:290	acid hydrolysis of sialic acid glycosidic bonds	276:322	Sialylated glycoproteins were selectively periodate-oxidized, captured on hydrazide beads, trypsinized and released by acid hydrolysis of sialic acid glycosidic bonds.
19838169	0	22	theme	glycan	32:37	arg1	structure					39:47	glycan structure	32:47	glycan structure	32:47	Enrichment of glycopeptides for glycan structure and attachment site identification.
19838169	1	23	gly	glycoproteins	119:131	arg1	glycoproteins					119:131	glycoproteins	119:131	glycoproteins from proteomic samples	119:154	We present a method to enrich for glycoproteins from proteomic samples.
19838169	3	24	theme	glycan	511:516	arg1	site					529:532	glycan attachment site	511:532	glycan attachment site	511:532	Mass spectrometric fragment analysis allowed identification of glycan structures, and additional fragmentation of deglycosylated ions yielded peptide sequence information, which allowed glycan attachment site and protein identification.
19838169	0	25	theme	attachment	53:62	arg1	site					64:67	attachment site	53:67	attachment site	53:67	Enrichment of glycopeptides for glycan structure and attachment site identification.
19838169	3	26	theme	Mass	325:328	arg1	analysis					353:360	Mass spectrometric fragment analysis	325:360	Mass spectrometric fragment analysis	325:360	Mass spectrometric fragment analysis allowed identification of glycan structures, and additional fragmentation of deglycosylated ions yielded peptide sequence information, which allowed glycan attachment site and protein identification.
19838169	0	27	gly	glycopeptides	14:26	arg2	glycopeptides					14:26	glycopeptides	14:26	glycopeptides	14:26	Enrichment of glycopeptides for glycan structure and attachment site identification.
19838169	3	28	theme	ions	454:457	arg1	fragmentation					422:434	additional fragmentation	411:434	additional fragmentation of deglycosylated ions	411:457	Mass spectrometric fragment analysis allowed identification of glycan structures, and additional fragmentation of deglycosylated ions yielded peptide sequence information, which allowed glycan attachment site and protein identification.
19838169	4	29	theme	glycosylation	604:616	arg1	sites					618:622	36 N-linked and 44 O-linked glycosylation sites	576:622	36 N-linked and 44 O-linked glycosylation sites	576:622	We identified 36 N-linked and 44 O-linked glycosylation sites on glycoproteins from human cerebrospinal fluid.
19838169	3	30	theme	spectrometric	330:342	arg1	analysis					353:360	Mass spectrometric fragment analysis	325:360	Mass spectrometric fragment analysis	325:360	Mass spectrometric fragment analysis allowed identification of glycan structures, and additional fragmentation of deglycosylated ions yielded peptide sequence information, which allowed glycan attachment site and protein identification.
19838169	2	31	theme	hydrazide	231:239	arg1	beads					241:245	hydrazide beads	231:245	hydrazide beads	231:245	Sialylated glycoproteins were selectively periodate-oxidized, captured on hydrazide beads, trypsinized and released by acid hydrolysis of sialic acid glycosidic bonds.
19838169	4	32	gly	glycoproteins	627:639	arg1	glycoproteins					627:639	glycoproteins	627:639	glycoproteins from human cerebrospinal fluid	627:670	We identified 36 N-linked and 44 O-linked glycosylation sites on glycoproteins from human cerebrospinal fluid.
19838169	4	33	theme	O-linked	595:602	arg1	sites					618:622	36 N-linked and 44 O-linked glycosylation sites	576:622	36 N-linked and 44 O-linked glycosylation sites	576:622	We identified 36 N-linked and 44 O-linked glycosylation sites on glycoproteins from human cerebrospinal fluid.
19838169	2	34	theme	acid	276:279	arg1	hydrolysis					281:290	acid hydrolysis	276:290	acid hydrolysis of sialic acid glycosidic bonds	276:322	Sialylated glycoproteins were selectively periodate-oxidized, captured on hydrazide beads, trypsinized and released by acid hydrolysis of sialic acid glycosidic bonds.
19838169	3	35	theme	protein	538:544	arg1	identification					546:559	protein identification	538:559	protein identification	538:559	Mass spectrometric fragment analysis allowed identification of glycan structures, and additional fragmentation of deglycosylated ions yielded peptide sequence information, which allowed glycan attachment site and protein identification.
19838169	1	36	theme	proteomic	138:146	arg1	samples					148:154	proteomic samples	138:154	proteomic samples	138:154	We present a method to enrich for glycoproteins from proteomic samples.
19838169	3	37	theme	deglycosylated	439:452	arg1	ions					454:457	deglycosylated ions	439:457	deglycosylated ions	439:457	Mass spectrometric fragment analysis allowed identification of glycan structures, and additional fragmentation of deglycosylated ions yielded peptide sequence information, which allowed glycan attachment site and protein identification.
19838169	3	38	theme	peptide	467:473	arg1	information					484:494	peptide sequence information	467:494	peptide sequence information	467:494	Mass spectrometric fragment analysis allowed identification of glycan structures, and additional fragmentation of deglycosylated ions yielded peptide sequence information, which allowed glycan attachment site and protein identification.
19838169	3	39	theme	additional	411:420	arg1	fragmentation					422:434	additional fragmentation	411:434	additional fragmentation of deglycosylated ions	411:457	Mass spectrometric fragment analysis allowed identification of glycan structures, and additional fragmentation of deglycosylated ions yielded peptide sequence information, which allowed glycan attachment site and protein identification.
18702514	9	0	theme	structural	1729:1738	arg1	properties					1752:1761	the structural and kinetic properties	1725:1761	the structural and kinetic properties of HPLRP2	1725:1771	Most of the structural and kinetic properties of HPLRP2 were found to be different from those of rat PLRP2, the structure of which was previously obtained with the lid in a closed conformation.
18702514	10	1	theme	lid	1961:1963	arg1	role					1949:1952	the essential role	1935:1952	the essential role of the lid in determining the substrate specificity and the mechanism of action of lipases	1935:2043	Our findings illustrate the essential role of the lid in determining the substrate specificity and the mechanism of action of lipases.
18702514	9	2	theme	closed	1890:1895	arg1	conformation					1897:1908	a closed conformation	1888:1908	a closed conformation	1888:1908	Most of the structural and kinetic properties of HPLRP2 were found to be different from those of rat PLRP2, the structure of which was previously obtained with the lid in a closed conformation.
18702514	1	3	theme	lipase	133:138	arg1	site					114:117	the active site	103:117	the active site of pancreatic lipase (PL)	103:143	Access to the active site of pancreatic lipase (PL) is controlled by a surface loop, the lid, which normally undergoes conformational changes only upon addition of lipids or amphiphiles.
18702514	1	3	theme	lipase	133:138	arg1	lipase					133:138	pancreatic lipase	122:138	pancreatic lipase (PL)	122:143	Access to the active site of pancreatic lipase (PL) is controlled by a surface loop, the lid, which normally undergoes conformational changes only upon addition of lipids or amphiphiles.
18702514	8	4	theme	guinea	1665:1670	arg1	pig					1672:1674	the guinea pig	1661:1674	the guinea pig PLRP2	1661:1680	This open conformation generates a large cavity capable of accommodating the digalactose polar head of galactolipids, similar to that previously observed in the active site of the guinea pig PLRP2, but absent from the classical PL.
18702514	3	5	theme	human	473:477	arg1	protein					505:511	human pancreatic lipase-related protein 2	473:513	wild-type and unglycosylated human pancreatic lipase-related protein 2 (HPLRP2)	444:522	Here we report two crystal structures of wild-type and unglycosylated human pancreatic lipase-related protein 2 (HPLRP2) with the lid in an open conformation in the absence of amphiphiles.
18702514	3	5	theme	human	473:477	arg1	HPLRP2					516:521	HPLRP2	516:521	HPLRP2	516:521	Here we report two crystal structures of wild-type and unglycosylated human pancreatic lipase-related protein 2 (HPLRP2) with the lid in an open conformation in the absence of amphiphiles.
18702514	9	6	theme	rat	1814:1816	arg1	PLRP2					1818:1822	rat PLRP2	1814:1822	rat PLRP2	1814:1822	Most of the structural and kinetic properties of HPLRP2 were found to be different from those of rat PLRP2, the structure of which was previously obtained with the lid in a closed conformation.
18702514	10	7	theme	substrate	1984:1992	arg1	specificity					1994:2004	the substrate specificity	1980:2004	the substrate specificity	1980:2004	Our findings illustrate the essential role of the lid in determining the substrate specificity and the mechanism of action of lipases.
18702514	9	8	theme	kinetic	1744:1750	arg1	properties					1752:1761	the structural and kinetic properties	1725:1761	the structural and kinetic properties of HPLRP2	1725:1771	Most of the structural and kinetic properties of HPLRP2 were found to be different from those of rat PLRP2, the structure of which was previously obtained with the lid in a closed conformation.
18702514	0	9	from	Structure	0:8	arg1	conformation					79:90	an open conformation	71:90	an open conformation	71:90	Structure of human pancreatic lipase-related protein 2 with the lid in an open conformation.
18702514	6	10	theme	unsoluble	1235:1243	arg1	substrates					1245:1254	unsoluble substrates	1235:1254	unsoluble substrates like triglycerides and diglycerides forming oil-in-water interfaces	1235:1322	Here we show that the HPLRP2 is directly inhibited by E600, does not present interfacial activation, and acts preferentially on substrates forming monomers or small aggregates (micelles) dispersed in solution like monoglycerides, phospholipids and galactolipids, whereas classical PL displays reverse properties and a high specificity for unsoluble substrates like triglycerides and diglycerides forming oil-in-water interfaces.
18702514	4	11	theme	electron-density	712:727	arg1	map					729:731	the electron-density map	708:731	the electron-density map	708:731	These structures solved independently are strikingly similar, with some residues of the lid being poorly defined in the electron-density map.
18702514	8	12	theme	PLRP2	1676:1680	arg1	PLRP2					1676:1680	the guinea pig PLRP2	1661:1680	the guinea pig PLRP2	1661:1680	This open conformation generates a large cavity capable of accommodating the digalactose polar head of galactolipids, similar to that previously observed in the active site of the guinea pig PLRP2, but absent from the classical PL.
18702514	8	12	theme	PLRP2	1676:1680	arg1	site					1653:1656	the active site	1642:1656	the active site of the guinea pig PLRP2	1642:1680	This open conformation generates a large cavity capable of accommodating the digalactose polar head of galactolipids, similar to that previously observed in the active site of the guinea pig PLRP2, but absent from the classical PL.
18702514	0	13	theme	open	74:77	arg1	conformation					79:90	an open conformation	71:90	an open conformation	71:90	Structure of human pancreatic lipase-related protein 2 with the lid in an open conformation.
18702514	8	14	theme	large	1520:1524	arg1	cavity					1526:1531	a large cavity	1518:1531	a large cavity capable of accommodating the digalactose polar head of galactolipids	1518:1600	This open conformation generates a large cavity capable of accommodating the digalactose polar head of galactolipids, similar to that previously observed in the active site of the guinea pig PLRP2, but absent from the classical PL.
18702514	7	15	theme	open	1432:1435	arg1	conformation					1437:1448	the open conformation	1428:1448	the open conformation observed in the crystal structure	1428:1482	These biochemical properties imply that the lid of HPLRP2 is likely to spontaneously adopt in solution the open conformation observed in the crystal structure.
18702514	10	16	theme	action	2027:2032	arg1	mechanism					2014:2022	the mechanism	2010:2022	the mechanism of action of lipases	2010:2043	Our findings illustrate the essential role of the lid in determining the substrate specificity and the mechanism of action of lipases.
18702514	10	16	theme	action	2027:2032	arg1	specificity					1994:2004	the substrate specificity	1980:2004	the substrate specificity	1980:2004	Our findings illustrate the essential role of the lid in determining the substrate specificity and the mechanism of action of lipases.
18702514	3	17	theme	unglycosylated	458:471	arg1	protein					505:511	human pancreatic lipase-related protein 2	473:513	wild-type and unglycosylated human pancreatic lipase-related protein 2 (HPLRP2)	444:522	Here we report two crystal structures of wild-type and unglycosylated human pancreatic lipase-related protein 2 (HPLRP2) with the lid in an open conformation in the absence of amphiphiles.
18702514	3	17	theme	unglycosylated	458:471	arg1	HPLRP2					516:521	HPLRP2	516:521	HPLRP2	516:521	Here we report two crystal structures of wild-type and unglycosylated human pancreatic lipase-related protein 2 (HPLRP2) with the lid in an open conformation in the absence of amphiphiles.
18702514	1	18	theme	conformational	212:225	arg1	changes					227:233	conformational changes	212:233	conformational changes	212:233	Access to the active site of pancreatic lipase (PL) is controlled by a surface loop, the lid, which normally undergoes conformational changes only upon addition of lipids or amphiphiles.
18702514	3	19	theme	wild-type	444:452	arg1	protein					505:511	human pancreatic lipase-related protein 2	473:513	wild-type and unglycosylated human pancreatic lipase-related protein 2 (HPLRP2)	444:522	Here we report two crystal structures of wild-type and unglycosylated human pancreatic lipase-related protein 2 (HPLRP2) with the lid in an open conformation in the absence of amphiphiles.
18702514	3	19	theme	wild-type	444:452	arg1	HPLRP2					516:521	HPLRP2	516:521	HPLRP2	516:521	Here we report two crystal structures of wild-type and unglycosylated human pancreatic lipase-related protein 2 (HPLRP2) with the lid in an open conformation in the absence of amphiphiles.
18702514	3	20	with	structures	430:439	arg1	lid					533:535	the lid	529:535	the lid in an open conformation in the absence of amphiphiles	529:589	Here we report two crystal structures of wild-type and unglycosylated human pancreatic lipase-related protein 2 (HPLRP2) with the lid in an open conformation in the absence of amphiphiles.
18702514	6	21	theme	substrates	1024:1033	arg1	monomers					1043:1050	substrates forming monomers	1024:1050	substrates forming monomers	1024:1050	Here we show that the HPLRP2 is directly inhibited by E600, does not present interfacial activation, and acts preferentially on substrates forming monomers or small aggregates (micelles) dispersed in solution like monoglycerides, phospholipids and galactolipids, whereas classical PL displays reverse properties and a high specificity for unsoluble substrates like triglycerides and diglycerides forming oil-in-water interfaces.
18702514	3	22	theme	protein	505:511	arg1	structures					430:439	two crystal structures	418:439	two crystal structures of wild-type and unglycosylated human pancreatic lipase-related protein 2 (HPLRP2) with the lid in an open conformation in the absence of amphiphiles	418:589	Here we report two crystal structures of wild-type and unglycosylated human pancreatic lipase-related protein 2 (HPLRP2) with the lid in an open conformation in the absence of amphiphiles.
18702514	5	23	theme	classical	821:829	arg1	PL					840:841	classical liganded PL	821:841	classical liganded PL	821:841	The open conformation of the lid is however different from that previously observed in classical liganded PL, suggesting different kinetic properties for HPLRP2.
18702514	2	24	theme	functional	329:338	arg1	conformation					340:351	the open and functional conformation	316:351	the open and functional conformation	316:351	Structures of PL with their lids in the open and functional conformation have required cocrystallization with amphiphiles.
18702514	9	25	theme	HPLRP2	1766:1771	arg1	properties					1752:1761	the structural and kinetic properties	1725:1761	the structural and kinetic properties of HPLRP2	1725:1771	Most of the structural and kinetic properties of HPLRP2 were found to be different from those of rat PLRP2, the structure of which was previously obtained with the lid in a closed conformation.
18702514	2	26	with	cocrystallization	367:383	arg1	amphiphiles					390:400	amphiphiles	390:400	amphiphiles	390:400	Structures of PL with their lids in the open and functional conformation have required cocrystallization with amphiphiles.
18702514	6	27	theme	high	1214:1217	arg1	specificity					1219:1229	a high specificity	1212:1229	a high specificity for unsoluble substrates like triglycerides and diglycerides forming oil-in-water interfaces	1212:1322	Here we show that the HPLRP2 is directly inhibited by E600, does not present interfacial activation, and acts preferentially on substrates forming monomers or small aggregates (micelles) dispersed in solution like monoglycerides, phospholipids and galactolipids, whereas classical PL displays reverse properties and a high specificity for unsoluble substrates like triglycerides and diglycerides forming oil-in-water interfaces.
18702514	9	28	from	those	1805:1809	arg1	different					1790:1798	different	1790:1798	different	1790:1798	Most of the structural and kinetic properties of HPLRP2 were found to be different from those of rat PLRP2, the structure of which was previously obtained with the lid in a closed conformation.
18702514	3	29	gly	unglycosylated	458:471	arg1	protein					505:511	human pancreatic lipase-related protein 2	473:513	wild-type and unglycosylated human pancreatic lipase-related protein 2 (HPLRP2)	444:522	Here we report two crystal structures of wild-type and unglycosylated human pancreatic lipase-related protein 2 (HPLRP2) with the lid in an open conformation in the absence of amphiphiles.
18702514	3	29	gly	unglycosylated	458:471	arg1	HPLRP2					516:521	HPLRP2	516:521	HPLRP2	516:521	Here we report two crystal structures of wild-type and unglycosylated human pancreatic lipase-related protein 2 (HPLRP2) with the lid in an open conformation in the absence of amphiphiles.
18702514	6	30	theme	forming	1035:1041	arg1	monomers					1043:1050	substrates forming monomers	1024:1050	substrates forming monomers	1024:1050	Here we show that the HPLRP2 is directly inhibited by E600, does not present interfacial activation, and acts preferentially on substrates forming monomers or small aggregates (micelles) dispersed in solution like monoglycerides, phospholipids and galactolipids, whereas classical PL displays reverse properties and a high specificity for unsoluble substrates like triglycerides and diglycerides forming oil-in-water interfaces.
18702514	8	31	located	observed	1630:1637	arg1	PLRP2					1676:1680	the guinea pig PLRP2	1661:1680	the guinea pig PLRP2	1661:1680	This open conformation generates a large cavity capable of accommodating the digalactose polar head of galactolipids, similar to that previously observed in the active site of the guinea pig PLRP2, but absent from the classical PL.
18702514	8	31	located	observed	1630:1637	arg2	that					1614:1617	that	1614:1617	that	1614:1617	This open conformation generates a large cavity capable of accommodating the digalactose polar head of galactolipids, similar to that previously observed in the active site of the guinea pig PLRP2, but absent from the classical PL.
18702514	8	31	located	observed	1630:1637	arg1	site					1653:1656	the active site	1642:1656	the active site of the guinea pig PLRP2	1642:1680	This open conformation generates a large cavity capable of accommodating the digalactose polar head of galactolipids, similar to that previously observed in the active site of the guinea pig PLRP2, but absent from the classical PL.
18702514	2	32	theme	open	320:323	arg1	conformation					340:351	the open and functional conformation	316:351	the open and functional conformation	316:351	Structures of PL with their lids in the open and functional conformation have required cocrystallization with amphiphiles.
18702514	5	33	theme	lid	763:765	arg1	conformation					743:754	The open conformation	734:754	The open conformation of the lid	734:765	The open conformation of the lid is however different from that previously observed in classical liganded PL, suggesting different kinetic properties for HPLRP2.
18702514	5	33	theme	lid	763:765	arg1	different					778:786	different	778:786	different	778:786	The open conformation of the lid is however different from that previously observed in classical liganded PL, suggesting different kinetic properties for HPLRP2.
18702514	10	34	theme	essential	1939:1947	arg1	role					1949:1952	the essential role	1935:1952	the essential role of the lid in determining the substrate specificity and the mechanism of action of lipases	1935:2043	Our findings illustrate the essential role of the lid in determining the substrate specificity and the mechanism of action of lipases.
18702514	5	35	theme	liganded	831:838	arg1	PL					840:841	classical liganded PL	821:841	classical liganded PL	821:841	The open conformation of the lid is however different from that previously observed in classical liganded PL, suggesting different kinetic properties for HPLRP2.
18702514	0	36	theme	pancreatic	19:28	arg1	protein					45:51	human pancreatic lipase-related protein 2	13:53	human pancreatic lipase-related protein 2 with the lid	13:66	Structure of human pancreatic lipase-related protein 2 with the lid in an open conformation.
18702514	8	37	from	PL	1713:1714	arg1	absent					1687:1692	absent	1687:1692	absent	1687:1692	This open conformation generates a large cavity capable of accommodating the digalactose polar head of galactolipids, similar to that previously observed in the active site of the guinea pig PLRP2, but absent from the classical PL.
18702514	2	38	from	lids	308:311	arg1	conformation					340:351	the open and functional conformation	316:351	the open and functional conformation	316:351	Structures of PL with their lids in the open and functional conformation have required cocrystallization with amphiphiles.
18702514	8	39	theme	classical	1703:1711	arg1	PL					1713:1714	the classical PL	1699:1714	the classical PL	1699:1714	This open conformation generates a large cavity capable of accommodating the digalactose polar head of galactolipids, similar to that previously observed in the active site of the guinea pig PLRP2, but absent from the classical PL.
18702514	0	40	theme	human	13:17	arg1	protein					45:51	human pancreatic lipase-related protein 2	13:53	human pancreatic lipase-related protein 2 with the lid	13:66	Structure of human pancreatic lipase-related protein 2 with the lid in an open conformation.
18702514	8	41	theme	digalactose	1562:1572	arg1	head					1580:1583	the digalactose polar head	1558:1583	the digalactose polar head of galactolipids	1558:1600	This open conformation generates a large cavity capable of accommodating the digalactose polar head of galactolipids, similar to that previously observed in the active site of the guinea pig PLRP2, but absent from the classical PL.
18702514	2	42	with	Structures	280:289	arg1	lids					308:311	their lids	302:311	their lids in the open and functional conformation	302:351	Structures of PL with their lids in the open and functional conformation have required cocrystallization with amphiphiles.
18702514	5	43	theme	different	855:863	arg1	properties					873:882	different kinetic properties	855:882	different kinetic properties for HPLRP2	855:893	The open conformation of the lid is however different from that previously observed in classical liganded PL, suggesting different kinetic properties for HPLRP2.
18702514	8	44	theme	capable	1533:1539	arg1	cavity					1526:1531	a large cavity	1518:1531	a large cavity capable of accommodating the digalactose polar head of galactolipids	1518:1600	This open conformation generates a large cavity capable of accommodating the digalactose polar head of galactolipids, similar to that previously observed in the active site of the guinea pig PLRP2, but absent from the classical PL.
18702514	3	45	theme	crystal	422:428	arg1	structures					430:439	two crystal structures	418:439	two crystal structures of wild-type and unglycosylated human pancreatic lipase-related protein 2 (HPLRP2) with the lid in an open conformation in the absence of amphiphiles	418:589	Here we report two crystal structures of wild-type and unglycosylated human pancreatic lipase-related protein 2 (HPLRP2) with the lid in an open conformation in the absence of amphiphiles.
18702514	0	46	theme	protein	45:51	arg1	Structure					0:8	Structure	0:8	Structure of human pancreatic lipase-related protein 2 with the lid in an open conformation.	0:91	Structure of human pancreatic lipase-related protein 2 with the lid in an open conformation.
18702514	5	47	located	observed	809:816	arg1	PL					840:841	classical liganded PL	821:841	classical liganded PL	821:841	The open conformation of the lid is however different from that previously observed in classical liganded PL, suggesting different kinetic properties for HPLRP2.
18702514	5	47	located	observed	809:816	arg2	that					793:796	that	793:796	that	793:796	The open conformation of the lid is however different from that previously observed in classical liganded PL, suggesting different kinetic properties for HPLRP2.
18702514	3	48	theme	open	543:546	arg1	conformation					548:559	an open conformation	540:559	an open conformation in the absence of amphiphiles	540:589	Here we report two crystal structures of wild-type and unglycosylated human pancreatic lipase-related protein 2 (HPLRP2) with the lid in an open conformation in the absence of amphiphiles.
18702514	3	49	from	conformation	548:559	arg1	absence					568:574	the absence	564:574	the absence of amphiphiles	564:589	Here we report two crystal structures of wild-type and unglycosylated human pancreatic lipase-related protein 2 (HPLRP2) with the lid in an open conformation in the absence of amphiphiles.
18702514	1	50	theme	surface	164:170	arg1	lid					182:184	the lid	178:184	the lid	178:184	Access to the active site of pancreatic lipase (PL) is controlled by a surface loop, the lid, which normally undergoes conformational changes only upon addition of lipids or amphiphiles.
18702514	1	50	theme	surface	164:170	arg1	loop					172:175	a surface loop	162:175	a surface loop	162:175	Access to the active site of pancreatic lipase (PL) is controlled by a surface loop, the lid, which normally undergoes conformational changes only upon addition of lipids or amphiphiles.
18702514	0	51	theme	lipase-related	30:43	arg1	protein					45:51	human pancreatic lipase-related protein 2	13:53	human pancreatic lipase-related protein 2 with the lid	13:66	Structure of human pancreatic lipase-related protein 2 with the lid in an open conformation.
18702514	5	52	theme	open	738:741	arg1	conformation					743:754	The open conformation	734:754	The open conformation of the lid	734:765	The open conformation of the lid is however different from that previously observed in classical liganded PL, suggesting different kinetic properties for HPLRP2.
18702514	5	52	theme	open	738:741	arg1	different					778:786	different	778:786	different	778:786	The open conformation of the lid is however different from that previously observed in classical liganded PL, suggesting different kinetic properties for HPLRP2.
18702514	3	53	theme	amphiphiles	579:589	arg1	absence					568:574	the absence	564:574	the absence of amphiphiles	564:589	Here we report two crystal structures of wild-type and unglycosylated human pancreatic lipase-related protein 2 (HPLRP2) with the lid in an open conformation in the absence of amphiphiles.
18702514	6	54	theme	reverse	1189:1195	arg1	properties					1197:1206	reverse properties	1189:1206	reverse properties	1189:1206	Here we show that the HPLRP2 is directly inhibited by E600, does not present interfacial activation, and acts preferentially on substrates forming monomers or small aggregates (micelles) dispersed in solution like monoglycerides, phospholipids and galactolipids, whereas classical PL displays reverse properties and a high specificity for unsoluble substrates like triglycerides and diglycerides forming oil-in-water interfaces.
18702514	5	55	from	that	793:796	arg1	conformation					743:754	The open conformation	734:754	The open conformation of the lid	734:765	The open conformation of the lid is however different from that previously observed in classical liganded PL, suggesting different kinetic properties for HPLRP2.
18702514	5	55	from	that	793:796	arg1	different					778:786	different	778:786	different	778:786	The open conformation of the lid is however different from that previously observed in classical liganded PL, suggesting different kinetic properties for HPLRP2.
18702514	6	56	theme	interfacial	973:983	arg1	activation					985:994	interfacial activation	973:994	interfacial activation	973:994	Here we show that the HPLRP2 is directly inhibited by E600, does not present interfacial activation, and acts preferentially on substrates forming monomers or small aggregates (micelles) dispersed in solution like monoglycerides, phospholipids and galactolipids, whereas classical PL displays reverse properties and a high specificity for unsoluble substrates like triglycerides and diglycerides forming oil-in-water interfaces.
18702514	1	57	theme	lipids	257:262	arg1	addition					245:252	addition	245:252	addition of lipids or amphiphiles	245:277	Access to the active site of pancreatic lipase (PL) is controlled by a surface loop, the lid, which normally undergoes conformational changes only upon addition of lipids or amphiphiles.
18702514	9	58	from	lid	1881:1883	arg1	conformation					1897:1908	a closed conformation	1888:1908	a closed conformation	1888:1908	Most of the structural and kinetic properties of HPLRP2 were found to be different from those of rat PLRP2, the structure of which was previously obtained with the lid in a closed conformation.
18702514	6	59	theme	small	1055:1059	arg1	micelles					1073:1080	micelles	1073:1080	micelles	1073:1080	Here we show that the HPLRP2 is directly inhibited by E600, does not present interfacial activation, and acts preferentially on substrates forming monomers or small aggregates (micelles) dispersed in solution like monoglycerides, phospholipids and galactolipids, whereas classical PL displays reverse properties and a high specificity for unsoluble substrates like triglycerides and diglycerides forming oil-in-water interfaces.
18702514	6	59	theme	small	1055:1059	arg1	aggregates					1061:1070	small aggregates	1055:1070	small aggregates (micelles)	1055:1081	Here we show that the HPLRP2 is directly inhibited by E600, does not present interfacial activation, and acts preferentially on substrates forming monomers or small aggregates (micelles) dispersed in solution like monoglycerides, phospholipids and galactolipids, whereas classical PL displays reverse properties and a high specificity for unsoluble substrates like triglycerides and diglycerides forming oil-in-water interfaces.
18702514	2	60	theme	PL	294:295	arg1	Structures					280:289	Structures	280:289	Structures of PL with their lids in the open and functional conformation	280:351	Structures of PL with their lids in the open and functional conformation have required cocrystallization with amphiphiles.
18702514	6	61	theme	oil-in-water	1300:1311	arg1	interfaces					1313:1322	oil-in-water interfaces	1300:1322	oil-in-water interfaces	1300:1322	Here we show that the HPLRP2 is directly inhibited by E600, does not present interfacial activation, and acts preferentially on substrates forming monomers or small aggregates (micelles) dispersed in solution like monoglycerides, phospholipids and galactolipids, whereas classical PL displays reverse properties and a high specificity for unsoluble substrates like triglycerides and diglycerides forming oil-in-water interfaces.
18702514	8	62	theme	galactolipids	1588:1600	arg1	head					1580:1583	the digalactose polar head	1558:1583	the digalactose polar head of galactolipids	1558:1600	This open conformation generates a large cavity capable of accommodating the digalactose polar head of galactolipids, similar to that previously observed in the active site of the guinea pig PLRP2, but absent from the classical PL.
18702514	8	63	theme	open	1490:1493	arg1	conformation					1495:1506	This open conformation	1485:1506	This open conformation	1485:1506	This open conformation generates a large cavity capable of accommodating the digalactose polar head of galactolipids, similar to that previously observed in the active site of the guinea pig PLRP2, but absent from the classical PL.
18702514	7	64	located	observed	1450:1457	arg1	structure					1474:1482	the crystal structure	1462:1482	the crystal structure	1462:1482	These biochemical properties imply that the lid of HPLRP2 is likely to spontaneously adopt in solution the open conformation observed in the crystal structure.
18702514	7	64	located	observed	1450:1457	arg2	conformation					1437:1448	the open conformation	1428:1448	the open conformation observed in the crystal structure	1428:1482	These biochemical properties imply that the lid of HPLRP2 is likely to spontaneously adopt in solution the open conformation observed in the crystal structure.
18702514	7	65	theme	crystal	1466:1472	arg1	structure					1474:1482	the crystal structure	1462:1482	the crystal structure	1462:1482	These biochemical properties imply that the lid of HPLRP2 is likely to spontaneously adopt in solution the open conformation observed in the crystal structure.
18702514	1	66	theme	amphiphiles	267:277	arg1	addition					245:252	addition	245:252	addition of lipids or amphiphiles	245:277	Access to the active site of pancreatic lipase (PL) is controlled by a surface loop, the lid, which normally undergoes conformational changes only upon addition of lipids or amphiphiles.
18702514	6	67	theme	classical	1167:1175	arg1	PL					1177:1178	classical PL	1167:1178	classical PL	1167:1178	Here we show that the HPLRP2 is directly inhibited by E600, does not present interfacial activation, and acts preferentially on substrates forming monomers or small aggregates (micelles) dispersed in solution like monoglycerides, phospholipids and galactolipids, whereas classical PL displays reverse properties and a high specificity for unsoluble substrates like triglycerides and diglycerides forming oil-in-water interfaces.
18702514	7	68	theme	HPLRP2	1376:1381	arg1	lid					1369:1371	the lid	1365:1371	the lid of HPLRP2	1365:1381	These biochemical properties imply that the lid of HPLRP2 is likely to spontaneously adopt in solution the open conformation observed in the crystal structure.
18702514	7	68	theme	HPLRP2	1376:1381	arg1	likely					1386:1391	likely	1386:1391	likely	1386:1391	These biochemical properties imply that the lid of HPLRP2 is likely to spontaneously adopt in solution the open conformation observed in the crystal structure.
18702514	1	69	theme	active	107:112	arg1	site					114:117	the active site	103:117	the active site of pancreatic lipase (PL)	103:143	Access to the active site of pancreatic lipase (PL) is controlled by a surface loop, the lid, which normally undergoes conformational changes only upon addition of lipids or amphiphiles.
18702514	1	69	theme	active	107:112	arg1	lipase					133:138	pancreatic lipase	122:138	pancreatic lipase (PL)	122:143	Access to the active site of pancreatic lipase (PL) is controlled by a surface loop, the lid, which normally undergoes conformational changes only upon addition of lipids or amphiphiles.
18702514	8	70	theme	active	1646:1651	arg1	PLRP2					1676:1680	the guinea pig PLRP2	1661:1680	the guinea pig PLRP2	1661:1680	This open conformation generates a large cavity capable of accommodating the digalactose polar head of galactolipids, similar to that previously observed in the active site of the guinea pig PLRP2, but absent from the classical PL.
18702514	8	70	theme	active	1646:1651	arg1	site					1653:1656	the active site	1642:1656	the active site of the guinea pig PLRP2	1642:1680	This open conformation generates a large cavity capable of accommodating the digalactose polar head of galactolipids, similar to that previously observed in the active site of the guinea pig PLRP2, but absent from the classical PL.
18702514	5	71	theme	kinetic	865:871	arg1	properties					873:882	different kinetic properties	855:882	different kinetic properties for HPLRP2	855:893	The open conformation of the lid is however different from that previously observed in classical liganded PL, suggesting different kinetic properties for HPLRP2.
18702514	3	72	theme	lipase-related	490:503	arg1	protein					505:511	human pancreatic lipase-related protein 2	473:513	wild-type and unglycosylated human pancreatic lipase-related protein 2 (HPLRP2)	444:522	Here we report two crystal structures of wild-type and unglycosylated human pancreatic lipase-related protein 2 (HPLRP2) with the lid in an open conformation in the absence of amphiphiles.
18702514	3	72	theme	lipase-related	490:503	arg1	HPLRP2					516:521	HPLRP2	516:521	HPLRP2	516:521	Here we report two crystal structures of wild-type and unglycosylated human pancreatic lipase-related protein 2 (HPLRP2) with the lid in an open conformation in the absence of amphiphiles.
18702514	4	73	theme	lid	680:682	arg1	residues					664:671	some residues	659:671	some residues of the lid	659:682	These structures solved independently are strikingly similar, with some residues of the lid being poorly defined in the electron-density map.
18702514	4	73	theme	lid	680:682	arg1	lid					680:682	the lid	676:682	the lid	676:682	These structures solved independently are strikingly similar, with some residues of the lid being poorly defined in the electron-density map.
18702514	9	74	theme	PLRP2	1818:1822	arg1	structure					1829:1837	the structure	1825:1837	the structure	1825:1837	Most of the structural and kinetic properties of HPLRP2 were found to be different from those of rat PLRP2, the structure of which was previously obtained with the lid in a closed conformation.
18702514	7	75	theme	biochemical	1331:1341	arg1	properties					1343:1352	These biochemical properties	1325:1352	These biochemical properties	1325:1352	These biochemical properties imply that the lid of HPLRP2 is likely to spontaneously adopt in solution the open conformation observed in the crystal structure.
18702514	3	76	theme	pancreatic	479:488	arg1	protein					505:511	human pancreatic lipase-related protein 2	473:513	wild-type and unglycosylated human pancreatic lipase-related protein 2 (HPLRP2)	444:522	Here we report two crystal structures of wild-type and unglycosylated human pancreatic lipase-related protein 2 (HPLRP2) with the lid in an open conformation in the absence of amphiphiles.
18702514	3	76	theme	pancreatic	479:488	arg1	HPLRP2					516:521	HPLRP2	516:521	HPLRP2	516:521	Here we report two crystal structures of wild-type and unglycosylated human pancreatic lipase-related protein 2 (HPLRP2) with the lid in an open conformation in the absence of amphiphiles.
18702514	3	77	from	lid	533:535	arg1	conformation					548:559	an open conformation	540:559	an open conformation in the absence of amphiphiles	540:589	Here we report two crystal structures of wild-type and unglycosylated human pancreatic lipase-related protein 2 (HPLRP2) with the lid in an open conformation in the absence of amphiphiles.
18702514	10	78	theme	lipases	2037:2043	arg1	action					2027:2032	action	2027:2032	action of lipases	2027:2043	Our findings illustrate the essential role of the lid in determining the substrate specificity and the mechanism of action of lipases.
18702514	6	79	dep	inhibited	937:945	arg1	whereas					1159:1165	whereas	1159:1165	whereas	1159:1165	Here we show that the HPLRP2 is directly inhibited by E600, does not present interfacial activation, and acts preferentially on substrates forming monomers or small aggregates (micelles) dispersed in solution like monoglycerides, phospholipids and galactolipids, whereas classical PL displays reverse properties and a high specificity for unsoluble substrates like triglycerides and diglycerides forming oil-in-water interfaces.
18702514	0	80	with	protein	45:51	arg1	lid					64:66	the lid	60:66	the lid	60:66	Structure of human pancreatic lipase-related protein 2 with the lid in an open conformation.
18702514	1	81	theme	pancreatic	122:131	arg1	PL					141:142	PL	141:142	PL	141:142	Access to the active site of pancreatic lipase (PL) is controlled by a surface loop, the lid, which normally undergoes conformational changes only upon addition of lipids or amphiphiles.
18702514	1	81	theme	pancreatic	122:131	arg1	lipase					133:138	pancreatic lipase	122:138	pancreatic lipase (PL)	122:143	Access to the active site of pancreatic lipase (PL) is controlled by a surface loop, the lid, which normally undergoes conformational changes only upon addition of lipids or amphiphiles.
18702514	8	82	theme	pig	1672:1674	arg1	PLRP2					1676:1680	the guinea pig PLRP2	1661:1680	the guinea pig PLRP2	1661:1680	This open conformation generates a large cavity capable of accommodating the digalactose polar head of galactolipids, similar to that previously observed in the active site of the guinea pig PLRP2, but absent from the classical PL.
18702514	8	83	theme	polar	1574:1578	arg1	head					1580:1583	the digalactose polar head	1558:1583	the digalactose polar head of galactolipids	1558:1600	This open conformation generates a large cavity capable of accommodating the digalactose polar head of galactolipids, similar to that previously observed in the active site of the guinea pig PLRP2, but absent from the classical PL.
17105447	0	0	theme	hypothetical	96:107	arg1	p76					91:93	the mannose-6-phosphate protein p76	59:93	the mannose-6-phosphate protein p76 (hypothetical protein LOC196463)	59:126	Biochemical characterization and lysosomal localization of the mannose-6-phosphate protein p76 (hypothetical protein LOC196463).
17105447	0	0	theme	hypothetical	96:107	arg1	protein					109:115	hypothetical protein LOC196463	96:125	hypothetical protein LOC196463	96:125	Biochemical characterization and lysosomal localization of the mannose-6-phosphate protein p76 (hypothetical protein LOC196463).
17105447	8	1	gly	N-glycosylation	1175:1189	arg2	six					1171:1173	six	1171:1173	six	1171:1173	The presence of six N-glycosylation sites was validated by progressive peptide-N-glycosidase F deglycosylation.
17105447	8	1	gly	N-glycosylation	1175:1189	arg2	sites					1191:1195	six N-glycosylation sites	1171:1195	six N-glycosylation sites	1171:1195	The presence of six N-glycosylation sites was validated by progressive peptide-N-glycosidase F deglycosylation.
17105447	7	2	theme	Man6P	1017:1021	arg1	sugars					1023:1028	Man6P sugars	1017:1028	Man6P sugars	1017:1028	The presence of Man6P sugars was confirmed by an MPR overlay experiment, which showed the direct and Man6P-dependent interaction between p76 and the MPR.
17105447	9	3	dep	N-	1285:1286	arg1	antibodies					1320:1329	directed anti-p76 antibodies	1302:1329	directed anti-p76 antibodies	1302:1329	Experiments using N- and C-termini directed anti-p76 antibodies provided insights into p76 maturation.
17105447	5	4	theme	NCBI	813:816	arg1	database					826:833	the NCBI protein database	809:833	the NCBI protein database	809:833	We named this protein 'p76' and it appeared later in the NCBI protein database as the 'hypothetical protein LOC196463'.
17105447	1	5	theme	cellular	257:264	arg1	MPRs					266:269	cellular MPRs	257:269	cellular MPRs (Man6P receptors)	257:287	Most soluble lysosomal proteins carry Man6P (mannose 6-phosphate), a specific carbohydrate marker that enables their binding to cellular MPRs (Man6P receptors) and their subsequent targeting towards the lysosome.
17105447	1	5	theme	cellular	257:264	arg1	receptors					278:286	Man6P receptors	272:286	Man6P receptors	272:286	Most soluble lysosomal proteins carry Man6P (mannose 6-phosphate), a specific carbohydrate marker that enables their binding to cellular MPRs (Man6P receptors) and their subsequent targeting towards the lysosome.
17105447	7	6	theme	Man6P-dependent	1102:1116	arg1	interaction					1118:1128	the direct and Man6P-dependent interaction	1087:1128	the direct and Man6P-dependent interaction between p76 and the MPR	1087:1152	The presence of Man6P sugars was confirmed by an MPR overlay experiment, which showed the direct and Man6P-dependent interaction between p76 and the MPR.
17105447	7	7	theme	sugars	1023:1028	arg1	presence					1005:1012	The presence	1001:1012	The presence of Man6P sugars	1001:1028	The presence of Man6P sugars was confirmed by an MPR overlay experiment, which showed the direct and Man6P-dependent interaction between p76 and the MPR.
17105447	1	8	theme	mannose	174:180	arg1	Man6P					167:171	Man6P	167:171	Man6P (mannose 6-phosphate)	167:193	Most soluble lysosomal proteins carry Man6P (mannose 6-phosphate), a specific carbohydrate marker that enables their binding to cellular MPRs (Man6P receptors) and their subsequent targeting towards the lysosome.
17105447	1	8	theme	mannose	174:180	arg1	6-phosphate					182:192	mannose 6-phosphate	174:192	mannose 6-phosphate	174:192	Most soluble lysosomal proteins carry Man6P (mannose 6-phosphate), a specific carbohydrate marker that enables their binding to cellular MPRs (Man6P receptors) and their subsequent targeting towards the lysosome.
17105447	6	9	theme	characteristics	984:998	arg1	several					957:963	several	957:963	several	957:963	In the present paper, we describe the identification of p76 by MS and we analyse several of its biochemical characteristics.
17105447	3	10	theme	latter	549:554	arg1	[Journet					562:569	the latter study [Journet	545:569	the latter study [Journet	545:569	Among the proteins identified during the course of the latter study [Journet, Chapel, Kieffer, Roux and Garin (2002) Proteomics, 2, 1026-1040], some had not been previously described as lysosomal proteins.
17105447	9	11	theme	p76	1354:1356	arg1	maturation					1358:1367	p76 maturation	1354:1367	p76 maturation	1354:1367	Experiments using N- and C-termini directed anti-p76 antibodies provided insights into p76 maturation.
17105447	5	12	theme	hypothetical	843:854	arg1	LOC196463					864:872	the 'hypothetical protein LOC196463'	838:873	the 'hypothetical protein LOC196463'	838:873	We named this protein 'p76' and it appeared later in the NCBI protein database as the 'hypothetical protein LOC196463'.
17105447	3	13	theme	lysosomal	680:688	arg1	some					638:641	some	638:641	some	638:641	Among the proteins identified during the course of the latter study [Journet, Chapel, Kieffer, Roux and Garin (2002) Proteomics, 2, 1026-1040], some had not been previously described as lysosomal proteins.
17105447	3	13	theme	lysosomal	680:688	arg1	proteins					690:697	lysosomal proteins	680:697	lysosomal proteins	680:697	Among the proteins identified during the course of the latter study [Journet, Chapel, Kieffer, Roux and Garin (2002) Proteomics, 2, 1026-1040], some had not been previously described as lysosomal proteins.
17105447	8	14	theme	F	1248:1248	arg1	deglycosylation					1250:1264	progressive peptide-N-glycosidase F deglycosylation	1214:1264	progressive peptide-N-glycosidase F deglycosylation	1214:1264	The presence of six N-glycosylation sites was validated by progressive peptide-N-glycosidase F deglycosylation.
17105447	10	15	theme	sub-cellular	1540:1551	arg1	fractionation					1553:1565	sub-cellular fractionation	1540:1565	sub-cellular fractionation of mouse liver homogenates	1540:1592	Most importantly, we were able to demonstrate the lysosomal localization of this protein, which was initially suggested by its Man6P tags, by both immunofluorescence and sub-cellular fractionation of mouse liver homogenates.
17105447	3	16	theme	study	556:560	arg1	[Journet					562:569	the latter study [Journet	545:569	the latter study [Journet	545:569	Among the proteins identified during the course of the latter study [Journet, Chapel, Kieffer, Roux and Garin (2002) Proteomics, 2, 1026-1040], some had not been previously described as lysosomal proteins.
17105447	1	17	theme	Man6P	272:276	arg1	MPRs					266:269	cellular MPRs	257:269	cellular MPRs (Man6P receptors)	257:287	Most soluble lysosomal proteins carry Man6P (mannose 6-phosphate), a specific carbohydrate marker that enables their binding to cellular MPRs (Man6P receptors) and their subsequent targeting towards the lysosome.
17105447	1	17	theme	Man6P	272:276	arg1	receptors					278:286	Man6P receptors	272:286	Man6P receptors	272:286	Most soluble lysosomal proteins carry Man6P (mannose 6-phosphate), a specific carbohydrate marker that enables their binding to cellular MPRs (Man6P receptors) and their subsequent targeting towards the lysosome.
17105447	8	18	theme	N-glycosylation	1175:1189	arg1	sites					1191:1195	six N-glycosylation sites	1171:1195	six N-glycosylation sites	1171:1195	The presence of six N-glycosylation sites was validated by progressive peptide-N-glycosidase F deglycosylation.
17105447	10	19	theme	liver	1576:1580	arg1	homogenates					1582:1592	mouse liver homogenates	1570:1592	mouse liver homogenates	1570:1592	Most importantly, we were able to demonstrate the lysosomal localization of this protein, which was initially suggested by its Man6P tags, by both immunofluorescence and sub-cellular fractionation of mouse liver homogenates.
17105447	3	20	dep	Kieffer	580:586	arg1	Proteomics					611:620	Proteomics	611:620	Proteomics	611:620	Among the proteins identified during the course of the latter study [Journet, Chapel, Kieffer, Roux and Garin (2002) Proteomics, 2, 1026-1040], some had not been previously described as lysosomal proteins.
17105447	6	21	theme	biochemical	972:982	arg1	characteristics					984:998	its biochemical characteristics	968:998	its biochemical characteristics	968:998	In the present paper, we describe the identification of p76 by MS and we analyse several of its biochemical characteristics.
17105447	2	22	theme	lysosomal	402:410	arg1	proteins					412:419	novel soluble lysosomal proteins	388:419	novel soluble lysosomal proteins	388:419	This characteristic was exploited to identify novel soluble lysosomal proteins by proteomic analysis of Man6P proteins purified from a human cell line.
17105447	1	23	contain	carry	161:165	arg2	6-phosphate					182:192	mannose 6-phosphate	174:192	mannose 6-phosphate	174:192	Most soluble lysosomal proteins carry Man6P (mannose 6-phosphate), a specific carbohydrate marker that enables their binding to cellular MPRs (Man6P receptors) and their subsequent targeting towards the lysosome.
17105447	1	23	contain	carry	161:165	arg2	Man6P					167:171	Man6P	167:171	Man6P (mannose 6-phosphate)	167:193	Most soluble lysosomal proteins carry Man6P (mannose 6-phosphate), a specific carbohydrate marker that enables their binding to cellular MPRs (Man6P receptors) and their subsequent targeting towards the lysosome.
17105447	1	23	contain	carry	161:165	arg1	proteins					152:159	Most soluble lysosomal proteins	129:159	Most soluble lysosomal proteins	129:159	Most soluble lysosomal proteins carry Man6P (mannose 6-phosphate), a specific carbohydrate marker that enables their binding to cellular MPRs (Man6P receptors) and their subsequent targeting towards the lysosome.
17105447	1	23	contain	carry	161:165	arg2	marker					220:225	a specific carbohydrate marker	196:225	a specific carbohydrate marker that enables their binding to cellular MPRs (Man6P receptors) and their subsequent targeting towards the lysosome	196:339	Most soluble lysosomal proteins carry Man6P (mannose 6-phosphate), a specific carbohydrate marker that enables their binding to cellular MPRs (Man6P receptors) and their subsequent targeting towards the lysosome.
17105447	10	24	theme	Man6P	1497:1501	arg1	tags					1503:1506	its Man6P tags	1493:1506	its Man6P tags	1493:1506	Most importantly, we were able to demonstrate the lysosomal localization of this protein, which was initially suggested by its Man6P tags, by both immunofluorescence and sub-cellular fractionation of mouse liver homogenates.
17105447	3	25	dep	identified	513:522	arg1	Roux					589:592	Roux	589:592	Roux	589:592	Among the proteins identified during the course of the latter study [Journet, Chapel, Kieffer, Roux and Garin (2002) Proteomics, 2, 1026-1040], some had not been previously described as lysosomal proteins.
17105447	3	25	dep	identified	513:522	arg1	Kieffer					580:586	Kieffer	580:586	Kieffer	580:586	Among the proteins identified during the course of the latter study [Journet, Chapel, Kieffer, Roux and Garin (2002) Proteomics, 2, 1026-1040], some had not been previously described as lysosomal proteins.
17105447	3	25	dep	identified	513:522	arg1	proteins					504:511	the proteins	500:511	the proteins identified during the course of the latter study [Journet, Chapel, Kieffer, Roux and Garin (2002) Proteomics, 2, 1026-1040]	500:635	Among the proteins identified during the course of the latter study [Journet, Chapel, Kieffer, Roux and Garin (2002) Proteomics, 2, 1026-1040], some had not been previously described as lysosomal proteins.
17105447	3	25	dep	identified	513:522	arg1	2002					605:608	2002	605:608	2002	605:608	Among the proteins identified during the course of the latter study [Journet, Chapel, Kieffer, Roux and Garin (2002) Proteomics, 2, 1026-1040], some had not been previously described as lysosomal proteins.
17105447	3	25	dep	identified	513:522	arg1	Garin					598:602	Garin	598:602	Garin	598:602	Among the proteins identified during the course of the latter study [Journet, Chapel, Kieffer, Roux and Garin (2002) Proteomics, 2, 1026-1040], some had not been previously described as lysosomal proteins.
17105447	2	26	theme	soluble	394:400	arg1	proteins					412:419	novel soluble lysosomal proteins	388:419	novel soluble lysosomal proteins	388:419	This characteristic was exploited to identify novel soluble lysosomal proteins by proteomic analysis of Man6P proteins purified from a human cell line.
17105447	0	27	theme	Biochemical	0:10	arg1	characterization					12:27	Biochemical characterization	0:27	Biochemical characterization	0:27	Biochemical characterization and lysosomal localization of the mannose-6-phosphate protein p76 (hypothetical protein LOC196463).
17105447	6	28	theme	present	883:889	arg1	paper					891:895	the present paper	879:895	the present paper	879:895	In the present paper, we describe the identification of p76 by MS and we analyse several of its biochemical characteristics.
17105447	5	29	theme	protein	856:862	arg1	LOC196463					864:872	the 'hypothetical protein LOC196463'	838:873	the 'hypothetical protein LOC196463'	838:873	We named this protein 'p76' and it appeared later in the NCBI protein database as the 'hypothetical protein LOC196463'.
17105447	2	30	theme	novel	388:392	arg1	proteins					412:419	novel soluble lysosomal proteins	388:419	novel soluble lysosomal proteins	388:419	This characteristic was exploited to identify novel soluble lysosomal proteins by proteomic analysis of Man6P proteins purified from a human cell line.
17105447	2	31	theme	proteins	452:459	arg1	analysis					434:441	proteomic analysis	424:441	proteomic analysis of Man6P proteins purified from a human cell line	424:491	This characteristic was exploited to identify novel soluble lysosomal proteins by proteomic analysis of Man6P proteins purified from a human cell line.
17105447	3	32	theme	[Journet	562:569	arg1	course					535:540	the course	531:540	the course of the latter study [Journet	531:569	Among the proteins identified during the course of the latter study [Journet, Chapel, Kieffer, Roux and Garin (2002) Proteomics, 2, 1026-1040], some had not been previously described as lysosomal proteins.
17105447	1	33	theme	specific	198:205	arg1	Man6P					167:171	Man6P	167:171	Man6P (mannose 6-phosphate)	167:193	Most soluble lysosomal proteins carry Man6P (mannose 6-phosphate), a specific carbohydrate marker that enables their binding to cellular MPRs (Man6P receptors) and their subsequent targeting towards the lysosome.
17105447	1	33	theme	specific	198:205	arg1	marker					220:225	a specific carbohydrate marker	196:225	a specific carbohydrate marker that enables their binding to cellular MPRs (Man6P receptors) and their subsequent targeting towards the lysosome	196:339	Most soluble lysosomal proteins carry Man6P (mannose 6-phosphate), a specific carbohydrate marker that enables their binding to cellular MPRs (Man6P receptors) and their subsequent targeting towards the lysosome.
17105447	2	34	theme	Man6P	446:450	arg1	proteins					452:459	Man6P proteins	446:459	Man6P proteins purified from a human cell line	446:491	This characteristic was exploited to identify novel soluble lysosomal proteins by proteomic analysis of Man6P proteins purified from a human cell line.
17105447	4	35	located	detected	724:731	arg2	protein					716:722	a protein	714:722	a protein detected at 76 kDa by SDS/PAGE	714:753	We focused on a protein detected at 76 kDa by SDS/PAGE.
17105447	4	35	located	detected	724:731	arg1	kDa					739:741	76 kDa	736:741	76 kDa	736:741	We focused on a protein detected at 76 kDa by SDS/PAGE.
17105447	10	36	theme	lysosomal	1420:1428	arg1	localization					1430:1441	the lysosomal localization	1416:1441	the lysosomal localization of this protein, which was initially suggested by its Man6P tags, by both immunofluorescence and sub-cellular fractionation of mouse liver homogenates	1416:1592	Most importantly, we were able to demonstrate the lysosomal localization of this protein, which was initially suggested by its Man6P tags, by both immunofluorescence and sub-cellular fractionation of mouse liver homogenates.
17105447	5	37	theme	protein	818:824	arg1	database					826:833	the NCBI protein database	809:833	the NCBI protein database	809:833	We named this protein 'p76' and it appeared later in the NCBI protein database as the 'hypothetical protein LOC196463'.
17105447	1	38	theme	carbohydrate	207:218	arg1	Man6P					167:171	Man6P	167:171	Man6P (mannose 6-phosphate)	167:193	Most soluble lysosomal proteins carry Man6P (mannose 6-phosphate), a specific carbohydrate marker that enables their binding to cellular MPRs (Man6P receptors) and their subsequent targeting towards the lysosome.
17105447	1	38	theme	carbohydrate	207:218	arg1	marker					220:225	a specific carbohydrate marker	196:225	a specific carbohydrate marker that enables their binding to cellular MPRs (Man6P receptors) and their subsequent targeting towards the lysosome	196:339	Most soluble lysosomal proteins carry Man6P (mannose 6-phosphate), a specific carbohydrate marker that enables their binding to cellular MPRs (Man6P receptors) and their subsequent targeting towards the lysosome.
17105447	8	39	theme	progressive	1214:1224	arg1	deglycosylation					1250:1264	progressive peptide-N-glycosidase F deglycosylation	1214:1264	progressive peptide-N-glycosidase F deglycosylation	1214:1264	The presence of six N-glycosylation sites was validated by progressive peptide-N-glycosidase F deglycosylation.
17105447	10	40	theme	mouse	1570:1574	arg1	homogenates					1582:1592	mouse liver homogenates	1570:1592	mouse liver homogenates	1570:1592	Most importantly, we were able to demonstrate the lysosomal localization of this protein, which was initially suggested by its Man6P tags, by both immunofluorescence and sub-cellular fractionation of mouse liver homogenates.
17105447	2	41	theme	proteomic	424:432	arg1	analysis					434:441	proteomic analysis	424:441	proteomic analysis of Man6P proteins purified from a human cell line	424:491	This characteristic was exploited to identify novel soluble lysosomal proteins by proteomic analysis of Man6P proteins purified from a human cell line.
17105447	2	42	theme	cell	483:486	arg1	line					488:491	a human cell line	475:491	a human cell line	475:491	This characteristic was exploited to identify novel soluble lysosomal proteins by proteomic analysis of Man6P proteins purified from a human cell line.
17105447	1	43	theme	subsequent	299:308	arg1	targeting					310:318	their subsequent targeting	293:318	their subsequent targeting	293:318	Most soluble lysosomal proteins carry Man6P (mannose 6-phosphate), a specific carbohydrate marker that enables their binding to cellular MPRs (Man6P receptors) and their subsequent targeting towards the lysosome.
17105447	0	44	theme	lysosomal	33:41	arg1	localization					43:54	lysosomal localization	33:54	lysosomal localization	33:54	Biochemical characterization and lysosomal localization of the mannose-6-phosphate protein p76 (hypothetical protein LOC196463).
17105447	2	45	theme	human	477:481	arg1	line					488:491	a human cell line	475:491	a human cell line	475:491	This characteristic was exploited to identify novel soluble lysosomal proteins by proteomic analysis of Man6P proteins purified from a human cell line.
17105447	0	46	theme	protein	83:89	arg1	p76					91:93	the mannose-6-phosphate protein p76	59:93	the mannose-6-phosphate protein p76 (hypothetical protein LOC196463)	59:126	Biochemical characterization and lysosomal localization of the mannose-6-phosphate protein p76 (hypothetical protein LOC196463).
17105447	0	46	theme	protein	83:89	arg1	protein					109:115	hypothetical protein LOC196463	96:125	hypothetical protein LOC196463	96:125	Biochemical characterization and lysosomal localization of the mannose-6-phosphate protein p76 (hypothetical protein LOC196463).
17105447	1	47	theme	Most	129:132	arg1	proteins					152:159	Most soluble lysosomal proteins	129:159	Most soluble lysosomal proteins	129:159	Most soluble lysosomal proteins carry Man6P (mannose 6-phosphate), a specific carbohydrate marker that enables their binding to cellular MPRs (Man6P receptors) and their subsequent targeting towards the lysosome.
17105447	10	48	theme	protein	1451:1457	arg1	localization					1430:1441	the lysosomal localization	1416:1441	the lysosomal localization of this protein, which was initially suggested by its Man6P tags, by both immunofluorescence and sub-cellular fractionation of mouse liver homogenates	1416:1592	Most importantly, we were able to demonstrate the lysosomal localization of this protein, which was initially suggested by its Man6P tags, by both immunofluorescence and sub-cellular fractionation of mouse liver homogenates.
17105447	1	49	theme	soluble	134:140	arg1	proteins					152:159	Most soluble lysosomal proteins	129:159	Most soluble lysosomal proteins	129:159	Most soluble lysosomal proteins carry Man6P (mannose 6-phosphate), a specific carbohydrate marker that enables their binding to cellular MPRs (Man6P receptors) and their subsequent targeting towards the lysosome.
17105447	7	50	theme	MPR	1050:1052	arg1	experiment					1062:1071	an MPR overlay experiment	1047:1071	an MPR overlay experiment	1047:1071	The presence of Man6P sugars was confirmed by an MPR overlay experiment, which showed the direct and Man6P-dependent interaction between p76 and the MPR.
17105447	1	51	theme	lysosomal	142:150	arg1	proteins					152:159	Most soluble lysosomal proteins	129:159	Most soluble lysosomal proteins	129:159	Most soluble lysosomal proteins carry Man6P (mannose 6-phosphate), a specific carbohydrate marker that enables their binding to cellular MPRs (Man6P receptors) and their subsequent targeting towards the lysosome.
17105447	6	52	theme	p76	932:934	arg1	identification					914:927	the identification	910:927	the identification of p76 by MS	910:940	In the present paper, we describe the identification of p76 by MS and we analyse several of its biochemical characteristics.
17105447	8	53	theme	sites	1191:1195	arg1	presence					1159:1166	The presence	1155:1166	The presence of six N-glycosylation sites	1155:1195	The presence of six N-glycosylation sites was validated by progressive peptide-N-glycosidase F deglycosylation.
17105447	8	54	theme	peptide-N-glycosidase	1226:1246	arg1	deglycosylation					1250:1264	progressive peptide-N-glycosidase F deglycosylation	1214:1264	progressive peptide-N-glycosidase F deglycosylation	1214:1264	The presence of six N-glycosylation sites was validated by progressive peptide-N-glycosidase F deglycosylation.
17105447	9	55	theme	anti-p76	1311:1318	arg1	antibodies					1320:1329	directed anti-p76 antibodies	1302:1329	directed anti-p76 antibodies	1302:1329	Experiments using N- and C-termini directed anti-p76 antibodies provided insights into p76 maturation.
17105447	0	56	theme	p76	91:93	arg1	characterization					12:27	Biochemical characterization	0:27	Biochemical characterization	0:27	Biochemical characterization and lysosomal localization of the mannose-6-phosphate protein p76 (hypothetical protein LOC196463).
17105447	0	56	theme	p76	91:93	arg1	localization					43:54	lysosomal localization	33:54	lysosomal localization	33:54	Biochemical characterization and lysosomal localization of the mannose-6-phosphate protein p76 (hypothetical protein LOC196463).
17105447	5	57	theme	protein	770:776	arg1	p76					779:781	this protein 'p76'	765:782	this protein 'p76'	765:782	We named this protein 'p76' and it appeared later in the NCBI protein database as the 'hypothetical protein LOC196463'.
17105447	10	58	theme	homogenates	1582:1592	arg1	immunofluorescence					1517:1534	immunofluorescence	1517:1534	immunofluorescence	1517:1534	Most importantly, we were able to demonstrate the lysosomal localization of this protein, which was initially suggested by its Man6P tags, by both immunofluorescence and sub-cellular fractionation of mouse liver homogenates.
17105447	10	58	theme	homogenates	1582:1592	arg1	fractionation					1553:1565	sub-cellular fractionation	1540:1565	sub-cellular fractionation of mouse liver homogenates	1540:1592	Most importantly, we were able to demonstrate the lysosomal localization of this protein, which was initially suggested by its Man6P tags, by both immunofluorescence and sub-cellular fractionation of mouse liver homogenates.
17105447	0	59	theme	mannose-6-phosphate	63:81	arg1	p76					91:93	the mannose-6-phosphate protein p76	59:93	the mannose-6-phosphate protein p76 (hypothetical protein LOC196463)	59:126	Biochemical characterization and lysosomal localization of the mannose-6-phosphate protein p76 (hypothetical protein LOC196463).
17105447	0	59	theme	mannose-6-phosphate	63:81	arg1	protein					109:115	hypothetical protein LOC196463	96:125	hypothetical protein LOC196463	96:125	Biochemical characterization and lysosomal localization of the mannose-6-phosphate protein p76 (hypothetical protein LOC196463).
17105447	7	60	theme	overlay	1054:1060	arg1	experiment					1062:1071	an MPR overlay experiment	1047:1071	an MPR overlay experiment	1047:1071	The presence of Man6P sugars was confirmed by an MPR overlay experiment, which showed the direct and Man6P-dependent interaction between p76 and the MPR.
17105447	9	61	theme	directed	1302:1309	arg1	antibodies					1320:1329	directed anti-p76 antibodies	1302:1329	directed anti-p76 antibodies	1302:1329	Experiments using N- and C-termini directed anti-p76 antibodies provided insights into p76 maturation.
17105447	7	62	theme	direct	1091:1096	arg1	interaction					1118:1128	the direct and Man6P-dependent interaction	1087:1128	the direct and Man6P-dependent interaction between p76 and the MPR	1087:1152	The presence of Man6P sugars was confirmed by an MPR overlay experiment, which showed the direct and Man6P-dependent interaction between p76 and the MPR.
11098061	0	0	theme	domain	88:93	arg1	domain					88:93	the extracellular domain	70:93	the extracellular domain of the human signal transducer gp130	70:130	Determination of the disulfide structure and N-glycosylation sites of the extracellular domain of the human signal transducer gp130.
11098061	0	0	theme	domain	88:93	arg1	structure					31:39	disulfide structure	21:39	disulfide structure	21:39	Determination of the disulfide structure and N-glycosylation sites of the extracellular domain of the human signal transducer gp130.
11098061	0	0	theme	domain	88:93	arg1	sites					61:65	N-glycosylation sites	45:65	N-glycosylation sites	45:65	Determination of the disulfide structure and N-glycosylation sites of the extracellular domain of the human signal transducer gp130.
11098061	5	1	theme	disulfide	729:737	arg1	cysteines					702:710	the 13 cysteines	695:710	the 13 cysteines present	695:718	Of the 13 cysteines present, 10 form disulfide bonds, two are present as free cysteines (Cys(279) and Cys(469)), and one (Cys(397)) is modified by S-cysteinylation.
11098061	5	1	theme	disulfide	729:737	arg1	bonds					739:743	10 form disulfide bonds	721:743	10 form disulfide bonds	721:743	Of the 13 cysteines present, 10 form disulfide bonds, two are present as free cysteines (Cys(279) and Cys(469)), and one (Cys(397)) is modified by S-cysteinylation.
11098061	4	2	theme	mass	673:676	arg1	spectrometry					678:689	mass spectrometry	673:689	mass spectrometry	673:689	Here we determine the disulfide structure of human sgp130 by peptide mapping, in the absence and presence of reducing agent, in combination with Edman degradation and mass spectrometry.
11098061	1	3	theme	common	146:151	arg1	subunit					181:187	the common signal transducing receptor subunit	142:187	the common signal transducing receptor subunit for the interleukin-6-type family of cytokines	142:234	gp130 is the common signal transducing receptor subunit for the interleukin-6-type family of cytokines.
11098061	1	3	theme	common	146:151	arg1	gp130					133:137	gp130	133:137	gp130	133:137	gp130 is the common signal transducing receptor subunit for the interleukin-6-type family of cytokines.
11098061	4	4	theme	peptide	567:573	arg1	mapping					575:581	peptide mapping	567:581	peptide mapping	567:581	Here we determine the disulfide structure of human sgp130 by peptide mapping, in the absence and presence of reducing agent, in combination with Edman degradation and mass spectrometry.
11098061	0	5	theme	extracellular	74:86	arg1	domain					88:93	the extracellular domain	70:93	the extracellular domain of the human signal transducer gp130	70:130	Determination of the disulfide structure and N-glycosylation sites of the extracellular domain of the human signal transducer gp130.
11098061	0	5	theme	extracellular	74:86	arg1	gp130					126:130	the human signal transducer gp130	98:130	the human signal transducer gp130	98:130	Determination of the disulfide structure and N-glycosylation sites of the extracellular domain of the human signal transducer gp130.
11098061	8	6	theme	known	1348:1352	arg1	superfamily					1354:1364	known superfamily	1348:1364	known superfamily of Ig-like domains	1348:1383	Unlike granulocyte colony-stimulating factor receptor, the connectivities of the four cysteines in the NH2-terminal domain of gp130 (Cys(6)-Cys(32) and Cys(26)-Cys(81)) are consistent with known superfamily of Ig-like domains.
11098061	1	7	theme	signal	153:158	arg1	subunit					181:187	the common signal transducing receptor subunit	142:187	the common signal transducing receptor subunit for the interleukin-6-type family of cytokines	142:234	gp130 is the common signal transducing receptor subunit for the interleukin-6-type family of cytokines.
11098061	1	7	theme	signal	153:158	arg1	gp130					133:137	gp130	133:137	gp130	133:137	gp130 is the common signal transducing receptor subunit for the interleukin-6-type family of cytokines.
11098061	5	8	dep	cysteines	770:778	arg1	Cys					794:796	Cys	794:796	Cys(469)	794:801	Of the 13 cysteines present, 10 form disulfide bonds, two are present as free cysteines (Cys(279) and Cys(469)), and one (Cys(397)) is modified by S-cysteinylation.
11098061	5	8	dep	cysteines	770:778	arg1	Cys					781:783	Cys(279)	781:788	Cys(279)	781:788	Of the 13 cysteines present, 10 form disulfide bonds, two are present as free cysteines (Cys(279) and Cys(469)), and one (Cys(397)) is modified by S-cysteinylation.
11098061	5	8	dep	cysteines	770:778	arg1	cysteines					770:778	free cysteines	765:778	free cysteines (Cys(279) and Cys(469))	765:802	Of the 13 cysteines present, 10 form disulfide bonds, two are present as free cysteines (Cys(279) and Cys(469)), and one (Cys(397)) is modified by S-cysteinylation.
11098061	5	8	dep	cysteines	770:778	arg1	469					798:800	469	798:800	469	798:800	Of the 13 cysteines present, 10 form disulfide bonds, two are present as free cysteines (Cys(279) and Cys(469)), and one (Cys(397)) is modified by S-cysteinylation.
11098061	8	9	theme	Ig-like	1369:1375	arg1	domains					1377:1383	Ig-like domains	1369:1383	Ig-like domains	1369:1383	Unlike granulocyte colony-stimulating factor receptor, the connectivities of the four cysteines in the NH2-terminal domain of gp130 (Cys(6)-Cys(32) and Cys(26)-Cys(81)) are consistent with known superfamily of Ig-like domains.
11098061	9	10	from	loop	1403:1406	arg1	domain					1411:1416	domain 5	1411:1418	domain 5	1411:1418	An eight-residue loop in domain 5 is tethered by Cys(436)-Cys(444).
11098061	8	11	from	cysteines	1245:1253	arg1	gp130					1285:1289	gp130	1285:1289	gp130 (Cys(6)-Cys(32) and Cys(26)-Cys(81))	1285:1326	Unlike granulocyte colony-stimulating factor receptor, the connectivities of the four cysteines in the NH2-terminal domain of gp130 (Cys(6)-Cys(32) and Cys(26)-Cys(81)) are consistent with known superfamily of Ig-like domains.
11098061	8	11	from	cysteines	1245:1253	arg1	domain					1275:1280	the NH2-terminal domain	1258:1280	the NH2-terminal domain of gp130 (Cys(6)-Cys(32) and Cys(26)-Cys(81))	1258:1326	Unlike granulocyte colony-stimulating factor receptor, the connectivities of the four cysteines in the NH2-terminal domain of gp130 (Cys(6)-Cys(32) and Cys(26)-Cys(81)) are consistent with known superfamily of Ig-like domains.
11098061	8	12	theme	NH2-terminal	1262:1273	arg1	gp130					1285:1289	gp130	1285:1289	gp130 (Cys(6)-Cys(32) and Cys(26)-Cys(81))	1285:1326	Unlike granulocyte colony-stimulating factor receptor, the connectivities of the four cysteines in the NH2-terminal domain of gp130 (Cys(6)-Cys(32) and Cys(26)-Cys(81)) are consistent with known superfamily of Ig-like domains.
11098061	8	12	theme	NH2-terminal	1262:1273	arg1	domain					1275:1280	the NH2-terminal domain	1258:1280	the NH2-terminal domain of gp130 (Cys(6)-Cys(32) and Cys(26)-Cys(81))	1258:1326	Unlike granulocyte colony-stimulating factor receptor, the connectivities of the four cysteines in the NH2-terminal domain of gp130 (Cys(6)-Cys(32) and Cys(26)-Cys(81)) are consistent with known superfamily of Ig-like domains.
11098061	5	13	theme	cysteines	702:710	arg1	present					754:760	present	754:760	present	754:760	Of the 13 cysteines present, 10 form disulfide bonds, two are present as free cysteines (Cys(279) and Cys(469)), and one (Cys(397)) is modified by S-cysteinylation.
11098061	11	14	link	disulfide-linked	1675:1690	arg1	process					1724:1730	the disulfide-linked homodimerization and activation process	1671:1730	the disulfide-linked homodimerization and activation process of gp130	1671:1739	Furthermore, we postulate that domain 5 may play a role in the disulfide-linked homodimerization and activation process of gp130.
11098061	2	15	theme	Ig-like	357:363	arg1	domain					365:370	an NH2-terminal Ig-like domain	341:370	an NH2-terminal Ig-like domain	341:370	Its extracellular region (sgp130) is predicted to consist of five fibronectin type III-like domains and an NH2-terminal Ig-like domain.
11098061	8	16	theme	gp130	1285:1289	arg1	gp130					1285:1289	gp130	1285:1289	gp130 (Cys(6)-Cys(32) and Cys(26)-Cys(81))	1285:1326	Unlike granulocyte colony-stimulating factor receptor, the connectivities of the four cysteines in the NH2-terminal domain of gp130 (Cys(6)-Cys(32) and Cys(26)-Cys(81)) are consistent with known superfamily of Ig-like domains.
11098061	8	16	theme	gp130	1285:1289	arg1	domain					1275:1280	the NH2-terminal domain	1258:1280	the NH2-terminal domain of gp130 (Cys(6)-Cys(32) and Cys(26)-Cys(81))	1258:1326	Unlike granulocyte colony-stimulating factor receptor, the connectivities of the four cysteines in the NH2-terminal domain of gp130 (Cys(6)-Cys(32) and Cys(26)-Cys(81)) are consistent with known superfamily of Ig-like domains.
11098061	10	17	theme	reduced	1528:1534	arg1	form					1536:1539	a reduced form	1526:1539	a reduced form	1526:1539	We have created a model predicting that this loop maintains Cys(469) in a reduced form, available for ligand-induced intramolecular disulfide bond formation.
11098061	0	18	theme	signal	108:113	arg1	gp130					126:130	the human signal transducer gp130	98:130	the human signal transducer gp130	98:130	Determination of the disulfide structure and N-glycosylation sites of the extracellular domain of the human signal transducer gp130.
11098061	10	19	theme	available	1542:1550	arg1	form					1536:1539	a reduced form	1526:1539	a reduced form	1526:1539	We have created a model predicting that this loop maintains Cys(469) in a reduced form, available for ligand-induced intramolecular disulfide bond formation.
11098061	3	20	theme	cysteines	463:471	arg1	set					441:443	a set	439:443	a set of four conserved cysteines	439:471	Domains 2 and 3 constitute the cytokine-binding region defined by a set of four conserved cysteines and a WSXWS motif, respectively.
11098061	3	20	theme	cysteines	463:471	arg1	cysteines					463:471	four conserved cysteines	448:471	four conserved cysteines	448:471	Domains 2 and 3 constitute the cytokine-binding region defined by a set of four conserved cysteines and a WSXWS motif, respectively.
11098061	11	21	theme	activation	1713:1722	arg1	process					1724:1730	the disulfide-linked homodimerization and activation process	1671:1730	the disulfide-linked homodimerization and activation process of gp130	1671:1739	Furthermore, we postulate that domain 5 may play a role in the disulfide-linked homodimerization and activation process of gp130.
11098061	1	22	theme	transducing	160:170	arg1	subunit					181:187	the common signal transducing receptor subunit	142:187	the common signal transducing receptor subunit for the interleukin-6-type family of cytokines	142:234	gp130 is the common signal transducing receptor subunit for the interleukin-6-type family of cytokines.
11098061	1	22	theme	transducing	160:170	arg1	gp130					133:137	gp130	133:137	gp130	133:137	gp130 is the common signal transducing receptor subunit for the interleukin-6-type family of cytokines.
11098061	0	23	theme	human	102:106	arg1	gp130					126:130	the human signal transducer gp130	98:130	the human signal transducer gp130	98:130	Determination of the disulfide structure and N-glycosylation sites of the extracellular domain of the human signal transducer gp130.
11098061	6	24	theme	potential	867:875	arg1	Asn					928:930	Asn(135)	928:935	Asn(135)	928:935	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	24	theme	potential	867:875	arg1	Asn					958:960	Asn(361)	958:965	Asn(361)	958:965	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	24	theme	potential	867:875	arg1	Asn					968:970	Asn(531)	968:975	Asn(531)	968:975	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	24	theme	potential	867:875	arg1	Asn					982:984	Asn(542)	982:989	Asn(542)	982:989	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	24	theme	potential	867:875	arg1	Asn					918:920	Asn(109)	918:925	Asn(109)	918:925	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	24	theme	potential	867:875	arg1	sites					893:897	the 11 potential N-glycosylation sites	860:897	the 11 potential N-glycosylation sites	860:897	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	24	theme	potential	867:875	arg1	Asn					909:911	Asn(61)	909:915	Asn(61)	909:915	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	24	theme	potential	867:875	arg1	Asn					900:902	Asn(21)	900:906	Asn(21)	900:906	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	24	theme	potential	867:875	arg1	Asn					948:950	Asn(357)	948:955	Asn(357)	948:955	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	24	theme	potential	867:875	arg1	Asn					938:940	Asn(205)	938:945	Asn(205)	938:945	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	5	25	mod	modified	827:834	arg1	Cys					814:816	Cys(397)	814:821	Cys(397)	814:821	Of the 13 cysteines present, 10 form disulfide bonds, two are present as free cysteines (Cys(279) and Cys(469)), and one (Cys(397)) is modified by S-cysteinylation.
11098061	5	25	mod	modified	827:834	arg3	S-cysteinylation					839:854	S-cysteinylation	839:854	S-cysteinylation	839:854	Of the 13 cysteines present, 10 form disulfide bonds, two are present as free cysteines (Cys(279) and Cys(469)), and one (Cys(397)) is modified by S-cysteinylation.
11098061	5	25	mod	modified	827:834	arg1	one					809:811	one	809:811	one	809:811	Of the 13 cysteines present, 10 form disulfide bonds, two are present as free cysteines (Cys(279) and Cys(469)), and one (Cys(397)) is modified by S-cysteinylation.
11098061	8	26	theme	Cys	1292:1294	arg1	32					1303:1304	32	1303:1304	32	1303:1304	Unlike granulocyte colony-stimulating factor receptor, the connectivities of the four cysteines in the NH2-terminal domain of gp130 (Cys(6)-Cys(32) and Cys(26)-Cys(81)) are consistent with known superfamily of Ig-like domains.
11098061	8	26	theme	Cys	1292:1294	arg1	-Cys					1298:1301	Cys(6)-Cys	1292:1301	Cys(6)-Cys(32)	1292:1305	Unlike granulocyte colony-stimulating factor receptor, the connectivities of the four cysteines in the NH2-terminal domain of gp130 (Cys(6)-Cys(32) and Cys(26)-Cys(81)) are consistent with known superfamily of Ig-like domains.
11098061	1	27	theme	receptor	172:179	arg1	subunit					181:187	the common signal transducing receptor subunit	142:187	the common signal transducing receptor subunit for the interleukin-6-type family of cytokines	142:234	gp130 is the common signal transducing receptor subunit for the interleukin-6-type family of cytokines.
11098061	1	27	theme	receptor	172:179	arg1	gp130					133:137	gp130	133:137	gp130	133:137	gp130 is the common signal transducing receptor subunit for the interleukin-6-type family of cytokines.
11098061	8	28	with	consistent	1332:1341	arg1	superfamily					1354:1364	known superfamily	1348:1364	known superfamily of Ig-like domains	1348:1383	Unlike granulocyte colony-stimulating factor receptor, the connectivities of the four cysteines in the NH2-terminal domain of gp130 (Cys(6)-Cys(32) and Cys(26)-Cys(81)) are consistent with known superfamily of Ig-like domains.
11098061	8	29	from	domain	1275:1280	arg1	consistent					1332:1341	consistent	1332:1341	consistent	1332:1341	Unlike granulocyte colony-stimulating factor receptor, the connectivities of the four cysteines in the NH2-terminal domain of gp130 (Cys(6)-Cys(32) and Cys(26)-Cys(81)) are consistent with known superfamily of Ig-like domains.
11098061	8	29	from	domain	1275:1280	arg1	connectivities					1218:1231	the connectivities	1214:1231	the connectivities of the four cysteines in the NH2-terminal domain of gp130 (Cys(6)-Cys(32) and Cys(26)-Cys(81))	1214:1326	Unlike granulocyte colony-stimulating factor receptor, the connectivities of the four cysteines in the NH2-terminal domain of gp130 (Cys(6)-Cys(32) and Cys(26)-Cys(81)) are consistent with known superfamily of Ig-like domains.
11098061	8	30	theme	colony-stimulating	1178:1195	arg1	factor					1197:1202	granulocyte colony-stimulating factor	1166:1202	granulocyte colony-stimulating factor receptor	1166:1211	Unlike granulocyte colony-stimulating factor receptor, the connectivities of the four cysteines in the NH2-terminal domain of gp130 (Cys(6)-Cys(32) and Cys(26)-Cys(81)) are consistent with known superfamily of Ig-like domains.
11098061	5	31	theme	free	765:768	arg1	Cys					794:796	Cys	794:796	Cys(469)	794:801	Of the 13 cysteines present, 10 form disulfide bonds, two are present as free cysteines (Cys(279) and Cys(469)), and one (Cys(397)) is modified by S-cysteinylation.
11098061	5	31	theme	free	765:768	arg1	Cys					781:783	Cys(279)	781:788	Cys(279)	781:788	Of the 13 cysteines present, 10 form disulfide bonds, two are present as free cysteines (Cys(279) and Cys(469)), and one (Cys(397)) is modified by S-cysteinylation.
11098061	5	31	theme	free	765:768	arg1	cysteines					770:778	free cysteines	765:778	free cysteines (Cys(279) and Cys(469))	765:802	Of the 13 cysteines present, 10 form disulfide bonds, two are present as free cysteines (Cys(279) and Cys(469)), and one (Cys(397)) is modified by S-cysteinylation.
11098061	8	32	theme	domains	1377:1383	arg1	superfamily					1354:1364	known superfamily	1348:1364	known superfamily of Ig-like domains	1348:1383	Unlike granulocyte colony-stimulating factor receptor, the connectivities of the four cysteines in the NH2-terminal domain of gp130 (Cys(6)-Cys(32) and Cys(26)-Cys(81)) are consistent with known superfamily of Ig-like domains.
11098061	7	33	theme	disulfide	1043:1051	arg1	Cys					1060:1062	Cys(112)-Cys	1060:1071	Cys(112)-Cys(122)	1060:1076	The disulfide bonds, Cys(112)-Cys(122) and Cys(150)-Cys(160), are consistent with known cytokine-binding region motifs.
11098061	7	33	theme	disulfide	1043:1051	arg1	consistent					1105:1114	consistent	1105:1114	consistent	1105:1114	The disulfide bonds, Cys(112)-Cys(122) and Cys(150)-Cys(160), are consistent with known cytokine-binding region motifs.
11098061	7	33	theme	disulfide	1043:1051	arg1	bonds					1053:1057	The disulfide bonds	1039:1057	The disulfide bonds	1039:1057	The disulfide bonds, Cys(112)-Cys(122) and Cys(150)-Cys(160), are consistent with known cytokine-binding region motifs.
11098061	7	33	theme	disulfide	1043:1051	arg1	Cys					1082:1084	Cys(150)-Cys	1082:1093	Cys(150)-Cys(160)	1082:1098	The disulfide bonds, Cys(112)-Cys(122) and Cys(150)-Cys(160), are consistent with known cytokine-binding region motifs.
11098061	10	34	theme	disulfide	1586:1594	arg1	formation					1601:1609	ligand-induced intramolecular disulfide bond formation	1556:1609	ligand-induced intramolecular disulfide bond formation	1556:1609	We have created a model predicting that this loop maintains Cys(469) in a reduced form, available for ligand-induced intramolecular disulfide bond formation.
11098061	0	35	theme	disulfide	21:29	arg1	structure					31:39	disulfide structure	21:39	disulfide structure	21:39	Determination of the disulfide structure and N-glycosylation sites of the extracellular domain of the human signal transducer gp130.
11098061	8	36	dep	gp130	1285:1289	arg1	81					1323:1324	81	1323:1324	81	1323:1324	Unlike granulocyte colony-stimulating factor receptor, the connectivities of the four cysteines in the NH2-terminal domain of gp130 (Cys(6)-Cys(32) and Cys(26)-Cys(81)) are consistent with known superfamily of Ig-like domains.
11098061	8	36	dep	gp130	1285:1289	arg1	-Cys					1318:1321	Cys(26)-Cys	1311:1321	Cys(26)-Cys(81)	1311:1325	Unlike granulocyte colony-stimulating factor receptor, the connectivities of the four cysteines in the NH2-terminal domain of gp130 (Cys(6)-Cys(32) and Cys(26)-Cys(81)) are consistent with known superfamily of Ig-like domains.
11098061	8	36	dep	gp130	1285:1289	arg1	32					1303:1304	32	1303:1304	32	1303:1304	Unlike granulocyte colony-stimulating factor receptor, the connectivities of the four cysteines in the NH2-terminal domain of gp130 (Cys(6)-Cys(32) and Cys(26)-Cys(81)) are consistent with known superfamily of Ig-like domains.
11098061	8	36	dep	gp130	1285:1289	arg1	-Cys					1298:1301	Cys(6)-Cys	1292:1301	Cys(6)-Cys(32)	1292:1305	Unlike granulocyte colony-stimulating factor receptor, the connectivities of the four cysteines in the NH2-terminal domain of gp130 (Cys(6)-Cys(32) and Cys(26)-Cys(81)) are consistent with known superfamily of Ig-like domains.
11098061	0	37	theme	gp130	126:130	arg1	domain					88:93	the extracellular domain	70:93	the extracellular domain of the human signal transducer gp130	70:130	Determination of the disulfide structure and N-glycosylation sites of the extracellular domain of the human signal transducer gp130.
11098061	0	37	theme	gp130	126:130	arg1	gp130					126:130	the human signal transducer gp130	98:130	the human signal transducer gp130	98:130	Determination of the disulfide structure and N-glycosylation sites of the extracellular domain of the human signal transducer gp130.
11098061	10	38	theme	intramolecular	1571:1584	arg1	formation					1601:1609	ligand-induced intramolecular disulfide bond formation	1556:1609	ligand-induced intramolecular disulfide bond formation	1556:1609	We have created a model predicting that this loop maintains Cys(469) in a reduced form, available for ligand-induced intramolecular disulfide bond formation.
11098061	3	39	theme	conserved	453:461	arg1	cysteines					463:471	four conserved cysteines	448:471	four conserved cysteines	448:471	Domains 2 and 3 constitute the cytokine-binding region defined by a set of four conserved cysteines and a WSXWS motif, respectively.
11098061	8	40	theme	Cys	1311:1313	arg1	81					1323:1324	81	1323:1324	81	1323:1324	Unlike granulocyte colony-stimulating factor receptor, the connectivities of the four cysteines in the NH2-terminal domain of gp130 (Cys(6)-Cys(32) and Cys(26)-Cys(81)) are consistent with known superfamily of Ig-like domains.
11098061	8	40	theme	Cys	1311:1313	arg1	-Cys					1318:1321	Cys(26)-Cys	1311:1321	Cys(26)-Cys(81)	1311:1325	Unlike granulocyte colony-stimulating factor receptor, the connectivities of the four cysteines in the NH2-terminal domain of gp130 (Cys(6)-Cys(32) and Cys(26)-Cys(81)) are consistent with known superfamily of Ig-like domains.
11098061	4	41	theme	sgp130	557:562	arg1	structure					538:546	the disulfide structure	524:546	the disulfide structure of human sgp130	524:562	Here we determine the disulfide structure of human sgp130 by peptide mapping, in the absence and presence of reducing agent, in combination with Edman degradation and mass spectrometry.
11098061	0	42	theme	transducer	115:124	arg1	gp130					126:130	the human signal transducer gp130	98:130	the human signal transducer gp130	98:130	Determination of the disulfide structure and N-glycosylation sites of the extracellular domain of the human signal transducer gp130.
11098061	2	43	theme	NH2-terminal	344:355	arg1	domain					365:370	an NH2-terminal Ig-like domain	341:370	an NH2-terminal Ig-like domain	341:370	Its extracellular region (sgp130) is predicted to consist of five fibronectin type III-like domains and an NH2-terminal Ig-like domain.
11098061	10	44	theme	ligand-induced	1556:1569	arg1	formation					1601:1609	ligand-induced intramolecular disulfide bond formation	1556:1609	ligand-induced intramolecular disulfide bond formation	1556:1609	We have created a model predicting that this loop maintains Cys(469) in a reduced form, available for ligand-induced intramolecular disulfide bond formation.
11098061	1	45	theme	interleukin-6-type	197:214	arg1	family					216:221	the interleukin-6-type family	193:221	the interleukin-6-type family of cytokines	193:234	gp130 is the common signal transducing receptor subunit for the interleukin-6-type family of cytokines.
11098061	3	46	theme	cytokine-binding	404:419	arg1	region					421:426	the cytokine-binding region	400:426	the cytokine-binding region defined by a set of four conserved cysteines	400:471	Domains 2 and 3 constitute the cytokine-binding region defined by a set of four conserved cysteines and a WSXWS motif, respectively.
11098061	4	47	theme	human	551:555	arg1	sgp130					557:562	human sgp130	551:562	human sgp130	551:562	Here we determine the disulfide structure of human sgp130 by peptide mapping, in the absence and presence of reducing agent, in combination with Edman degradation and mass spectrometry.
11098061	4	48	with	combination	634:644	arg1	degradation					657:667	Edman degradation	651:667	Edman degradation	651:667	Here we determine the disulfide structure of human sgp130 by peptide mapping, in the absence and presence of reducing agent, in combination with Edman degradation and mass spectrometry.
11098061	4	48	with	combination	634:644	arg1	spectrometry					678:689	mass spectrometry	673:689	mass spectrometry	673:689	Here we determine the disulfide structure of human sgp130 by peptide mapping, in the absence and presence of reducing agent, in combination with Edman degradation and mass spectrometry.
11098061	2	49	theme	extracellular	241:253	arg1	sgp130					263:268	sgp130	263:268	sgp130	263:268	Its extracellular region (sgp130) is predicted to consist of five fibronectin type III-like domains and an NH2-terminal Ig-like domain.
11098061	2	49	theme	extracellular	241:253	arg1	region					255:260	Its extracellular region	237:260	Its extracellular region (sgp130)	237:269	Its extracellular region (sgp130) is predicted to consist of five fibronectin type III-like domains and an NH2-terminal Ig-like domain.
11098061	9	50	theme	Cys	1435:1437	arg1	444					1448:1450	444	1448:1450	444	1448:1450	An eight-residue loop in domain 5 is tethered by Cys(436)-Cys(444).
11098061	9	50	theme	Cys	1435:1437	arg1	-Cys					1443:1446	Cys(436)-Cys	1435:1446	Cys(436)-Cys(444)	1435:1451	An eight-residue loop in domain 5 is tethered by Cys(436)-Cys(444).
11098061	4	51	theme	agent	624:628	arg1	presence					603:610	presence	603:610	presence	603:610	Here we determine the disulfide structure of human sgp130 by peptide mapping, in the absence and presence of reducing agent, in combination with Edman degradation and mass spectrometry.
11098061	4	51	theme	agent	624:628	arg1	absence					591:597	absence	591:597	absence	591:597	Here we determine the disulfide structure of human sgp130 by peptide mapping, in the absence and presence of reducing agent, in combination with Edman degradation and mass spectrometry.
11098061	0	52	theme	structure	31:39	arg1	Determination					0:12	Determination	0:12	Determination of the disulfide structure and N-glycosylation sites of the extracellular domain of the human signal transducer gp130	0:130	Determination of the disulfide structure and N-glycosylation sites of the extracellular domain of the human signal transducer gp130.
11098061	7	53	theme	known	1121:1125	arg1	motifs					1151:1156	known cytokine-binding region motifs	1121:1156	known cytokine-binding region motifs	1121:1156	The disulfide bonds, Cys(112)-Cys(122) and Cys(150)-Cys(160), are consistent with known cytokine-binding region motifs.
11098061	8	54	theme	factor	1197:1202	arg1	receptor					1204:1211	granulocyte colony-stimulating factor receptor	1166:1211	granulocyte colony-stimulating factor receptor	1166:1211	Unlike granulocyte colony-stimulating factor receptor, the connectivities of the four cysteines in the NH2-terminal domain of gp130 (Cys(6)-Cys(32) and Cys(26)-Cys(81)) are consistent with known superfamily of Ig-like domains.
11098061	4	55	theme	reducing	615:622	arg1	agent					624:628	reducing agent	615:628	reducing agent	615:628	Here we determine the disulfide structure of human sgp130 by peptide mapping, in the absence and presence of reducing agent, in combination with Edman degradation and mass spectrometry.
11098061	0	56	theme	sites	61:65	arg1	Determination					0:12	Determination	0:12	Determination of the disulfide structure and N-glycosylation sites of the extracellular domain of the human signal transducer gp130	0:130	Determination of the disulfide structure and N-glycosylation sites of the extracellular domain of the human signal transducer gp130.
11098061	8	57	from	connectivities	1218:1231	arg1	gp130					1285:1289	gp130	1285:1289	gp130 (Cys(6)-Cys(32) and Cys(26)-Cys(81))	1285:1326	Unlike granulocyte colony-stimulating factor receptor, the connectivities of the four cysteines in the NH2-terminal domain of gp130 (Cys(6)-Cys(32) and Cys(26)-Cys(81)) are consistent with known superfamily of Ig-like domains.
11098061	8	57	from	connectivities	1218:1231	arg1	domain					1275:1280	the NH2-terminal domain	1258:1280	the NH2-terminal domain of gp130 (Cys(6)-Cys(32) and Cys(26)-Cys(81))	1258:1326	Unlike granulocyte colony-stimulating factor receptor, the connectivities of the four cysteines in the NH2-terminal domain of gp130 (Cys(6)-Cys(32) and Cys(26)-Cys(81)) are consistent with known superfamily of Ig-like domains.
11098061	7	58	with	consistent	1105:1114	arg1	motifs					1151:1156	known cytokine-binding region motifs	1121:1156	known cytokine-binding region motifs	1121:1156	The disulfide bonds, Cys(112)-Cys(122) and Cys(150)-Cys(160), are consistent with known cytokine-binding region motifs.
11098061	3	59	theme	WSXWS	479:483	arg1	motif					485:489	a WSXWS motif	477:489	a WSXWS motif	477:489	Domains 2 and 3 constitute the cytokine-binding region defined by a set of four conserved cysteines and a WSXWS motif, respectively.
11098061	0	60	theme	N-glycosylation	45:59	arg1	domain					88:93	the extracellular domain	70:93	the extracellular domain of the human signal transducer gp130	70:130	Determination of the disulfide structure and N-glycosylation sites of the extracellular domain of the human signal transducer gp130.
11098061	0	60	theme	N-glycosylation	45:59	arg1	sites					61:65	N-glycosylation sites	45:65	N-glycosylation sites	45:65	Determination of the disulfide structure and N-glycosylation sites of the extracellular domain of the human signal transducer gp130.
11098061	4	61	theme	disulfide	528:536	arg1	structure					538:546	the disulfide structure	524:546	the disulfide structure of human sgp130	524:562	Here we determine the disulfide structure of human sgp130 by peptide mapping, in the absence and presence of reducing agent, in combination with Edman degradation and mass spectrometry.
11098061	0	62	dep	structure	31:39	arg1	the					17:19	the	17:19	the	17:19	Determination of the disulfide structure and N-glycosylation sites of the extracellular domain of the human signal transducer gp130.
11098061	8	63	theme	granulocyte	1166:1176	arg1	factor					1197:1202	granulocyte colony-stimulating factor	1166:1202	granulocyte colony-stimulating factor receptor	1166:1211	Unlike granulocyte colony-stimulating factor receptor, the connectivities of the four cysteines in the NH2-terminal domain of gp130 (Cys(6)-Cys(32) and Cys(26)-Cys(81)) are consistent with known superfamily of Ig-like domains.
11098061	4	64	dep	absence	591:597	arg1	the					587:589	the	587:589	the	587:589	Here we determine the disulfide structure of human sgp130 by peptide mapping, in the absence and presence of reducing agent, in combination with Edman degradation and mass spectrometry.
11098061	11	65	theme	homodimerization	1692:1707	arg1	process					1724:1730	the disulfide-linked homodimerization and activation process	1671:1730	the disulfide-linked homodimerization and activation process of gp130	1671:1739	Furthermore, we postulate that domain 5 may play a role in the disulfide-linked homodimerization and activation process of gp130.
11098061	10	66	theme	bond	1596:1599	arg1	formation					1601:1609	ligand-induced intramolecular disulfide bond formation	1556:1609	ligand-induced intramolecular disulfide bond formation	1556:1609	We have created a model predicting that this loop maintains Cys(469) in a reduced form, available for ligand-induced intramolecular disulfide bond formation.
11098061	1	67	theme	cytokines	226:234	arg1	family					216:221	the interleukin-6-type family	193:221	the interleukin-6-type family of cytokines	193:234	gp130 is the common signal transducing receptor subunit for the interleukin-6-type family of cytokines.
11098061	2	68	theme	III-like	320:327	arg1	domains					329:335	five fibronectin type III-like domains	298:335	five fibronectin type III-like domains	298:335	Its extracellular region (sgp130) is predicted to consist of five fibronectin type III-like domains and an NH2-terminal Ig-like domain.
11098061	8	69	theme	cysteines	1245:1253	arg1	consistent					1332:1341	consistent	1332:1341	consistent	1332:1341	Unlike granulocyte colony-stimulating factor receptor, the connectivities of the four cysteines in the NH2-terminal domain of gp130 (Cys(6)-Cys(32) and Cys(26)-Cys(81)) are consistent with known superfamily of Ig-like domains.
11098061	8	69	theme	cysteines	1245:1253	arg1	connectivities					1218:1231	the connectivities	1214:1231	the connectivities of the four cysteines in the NH2-terminal domain of gp130 (Cys(6)-Cys(32) and Cys(26)-Cys(81))	1214:1326	Unlike granulocyte colony-stimulating factor receptor, the connectivities of the four cysteines in the NH2-terminal domain of gp130 (Cys(6)-Cys(32) and Cys(26)-Cys(81)) are consistent with known superfamily of Ig-like domains.
11098061	11	70	theme	disulfide-linked	1675:1690	arg1	process					1724:1730	the disulfide-linked homodimerization and activation process	1671:1730	the disulfide-linked homodimerization and activation process of gp130	1671:1739	Furthermore, we postulate that domain 5 may play a role in the disulfide-linked homodimerization and activation process of gp130.
11098061	9	71	theme	eight-residue	1389:1401	arg1	loop					1403:1406	An eight-residue loop	1386:1406	An eight-residue loop in domain 5	1386:1418	An eight-residue loop in domain 5 is tethered by Cys(436)-Cys(444).
11098061	0	72	gly	N-glycosylation	45:59	arg2	sites					61:65	N-glycosylation sites	45:65	N-glycosylation sites	45:65	Determination of the disulfide structure and N-glycosylation sites of the extracellular domain of the human signal transducer gp130.
11098061	0	72	gly	N-glycosylation	45:59	arg1	domain					88:93	the extracellular domain	70:93	the extracellular domain of the human signal transducer gp130	70:130	Determination of the disulfide structure and N-glycosylation sites of the extracellular domain of the human signal transducer gp130.
11098061	0	72	gly	N-glycosylation	45:59	arg2	domain					88:93	the extracellular domain	70:93	the extracellular domain of the human signal transducer gp130	70:130	Determination of the disulfide structure and N-glycosylation sites of the extracellular domain of the human signal transducer gp130.
11098061	0	72	gly	N-glycosylation	45:59	arg1	gp130					126:130	the human signal transducer gp130	98:130	the human signal transducer gp130	98:130	Determination of the disulfide structure and N-glycosylation sites of the extracellular domain of the human signal transducer gp130.
11098061	7	73	theme	region	1144:1149	arg1	motifs					1151:1156	known cytokine-binding region motifs	1121:1156	known cytokine-binding region motifs	1121:1156	The disulfide bonds, Cys(112)-Cys(122) and Cys(150)-Cys(160), are consistent with known cytokine-binding region motifs.
11098061	11	74	theme	gp130	1735:1739	arg1	process					1724:1730	the disulfide-linked homodimerization and activation process	1671:1730	the disulfide-linked homodimerization and activation process of gp130	1671:1739	Furthermore, we postulate that domain 5 may play a role in the disulfide-linked homodimerization and activation process of gp130.
11098061	7	75	theme	cytokine-binding	1127:1142	arg1	motifs					1151:1156	known cytokine-binding region motifs	1121:1156	known cytokine-binding region motifs	1121:1156	The disulfide bonds, Cys(112)-Cys(122) and Cys(150)-Cys(160), are consistent with known cytokine-binding region motifs.
11098061	5	76	theme	form	724:727	arg1	cysteines					702:710	the 13 cysteines	695:710	the 13 cysteines present	695:718	Of the 13 cysteines present, 10 form disulfide bonds, two are present as free cysteines (Cys(279) and Cys(469)), and one (Cys(397)) is modified by S-cysteinylation.
11098061	5	76	theme	form	724:727	arg1	bonds					739:743	10 form disulfide bonds	721:743	10 form disulfide bonds	721:743	Of the 13 cysteines present, 10 form disulfide bonds, two are present as free cysteines (Cys(279) and Cys(469)), and one (Cys(397)) is modified by S-cysteinylation.
11098061	6	77	theme	N-glycosylation	877:891	arg1	Asn					928:930	Asn(135)	928:935	Asn(135)	928:935	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	77	theme	N-glycosylation	877:891	arg1	Asn					958:960	Asn(361)	958:965	Asn(361)	958:965	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	77	theme	N-glycosylation	877:891	arg1	Asn					968:970	Asn(531)	968:975	Asn(531)	968:975	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	77	theme	N-glycosylation	877:891	arg1	Asn					982:984	Asn(542)	982:989	Asn(542)	982:989	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	77	theme	N-glycosylation	877:891	arg1	Asn					918:920	Asn(109)	918:925	Asn(109)	918:925	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	77	theme	N-glycosylation	877:891	arg1	sites					893:897	the 11 potential N-glycosylation sites	860:897	the 11 potential N-glycosylation sites	860:897	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	77	theme	N-glycosylation	877:891	arg1	Asn					909:911	Asn(61)	909:915	Asn(61)	909:915	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	77	theme	N-glycosylation	877:891	arg1	Asn					900:902	Asn(21)	900:906	Asn(21)	900:906	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	77	theme	N-glycosylation	877:891	arg1	Asn					948:950	Asn(357)	948:955	Asn(357)	948:955	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	77	theme	N-glycosylation	877:891	arg1	Asn					938:940	Asn(205)	938:945	Asn(205)	938:945	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	78	gly	N-glycosylation	877:891	arg2	Asn					900:902	Asn(21)	900:906	Asn(21)	900:906	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	78	gly	N-glycosylation	877:891	arg2	Asn					982:984	Asn(542)	982:989	Asn(542)	982:989	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	78	gly	N-glycosylation	877:891	arg2	Asn					909:911	Asn(61)	909:915	Asn(61)	909:915	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	78	gly	N-glycosylation	877:891	arg2	Asn					938:940	Asn(205)	938:945	Asn(205)	938:945	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	78	gly	N-glycosylation	877:891	arg2	Asn					948:950	Asn(357)	948:955	Asn(357)	948:955	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	78	gly	N-glycosylation	877:891	arg2	Asn					928:930	Asn(135)	928:935	Asn(135)	928:935	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	78	gly	N-glycosylation	877:891	arg2	11					864:865	11	864:865	11	864:865	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	78	gly	N-glycosylation	877:891	arg2	sites					893:897	the 11 potential N-glycosylation sites	860:897	the 11 potential N-glycosylation sites	860:897	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	78	gly	N-glycosylation	877:891	arg2	Asn					958:960	Asn(361)	958:965	Asn(361)	958:965	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	78	gly	N-glycosylation	877:891	arg2	Asn					918:920	Asn(109)	918:925	Asn(109)	918:925	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	6	78	gly	N-glycosylation	877:891	arg2	Asn					968:970	Asn(531)	968:975	Asn(531)	968:975	Of the 11 potential N-glycosylation sites, Asn(21), Asn(61), Asn(109), Asn(135), Asn(205), Asn(357), Asn(361), Asn(531), and Asn(542) are glycosylated but not Asn(224) and Asn(368).
11098061	4	79	theme	Edman	651:655	arg1	degradation					657:667	Edman degradation	651:667	Edman degradation	651:667	Here we determine the disulfide structure of human sgp130 by peptide mapping, in the absence and presence of reducing agent, in combination with Edman degradation and mass spectrometry.
11098061	5	80	theme	present	712:718	arg1	cysteines					702:710	the 13 cysteines	695:710	the 13 cysteines present	695:718	Of the 13 cysteines present, 10 form disulfide bonds, two are present as free cysteines (Cys(279) and Cys(469)), and one (Cys(397)) is modified by S-cysteinylation.
11098061	5	80	theme	present	712:718	arg1	bonds					739:743	10 form disulfide bonds	721:743	10 form disulfide bonds	721:743	Of the 13 cysteines present, 10 form disulfide bonds, two are present as free cysteines (Cys(279) and Cys(469)), and one (Cys(397)) is modified by S-cysteinylation.
9925876	11	0	theme	patch	1497:1501	arg1	analysis					1509:1516	patch clamp analysis	1497:1516	patch clamp analysis	1497:1516	Furthermore, patch clamp analysis revealed that there was a virtual absence of HERG current in the N-glycosylation mutants.
9925876	7	1	theme	N-linked	839:846	arg1	glycosylation					848:860	N-linked glycosylation	839:860	N-linked glycosylation	839:860	Tunicamycin, an inhibitor of N-linked glycosylation, blocked normal surface membrane expression of a HERG-green fluorescent protein (GFP) fusion protein (HERGGFP) transiently expressed in human embryonic kidney (HEK 293) cells imaged with confocal microscopy.
9925876	4	2	from	LQT	381:383	arg1	patients					393:400	some patients	388:400	some patients	388:400	While a recent report indicates that LQT in some patients is associated with a mutation of HERG at a consensus extracellular N-linked glycosylation site (N629), earlier studies failed to identify a role for N-linked glycosylation in the functional expression of voltage-gated K+ channels.
9925876	9	3	theme	molecular	1135:1143	arg1	mass					1145:1148	the molecular mass	1131:1148	the molecular mass	1131:1148	Immunoblot analysis revealed that N-glycosidase F shifted the molecular mass of HERGGFP, stably expressed in HEK 293 cells, indicating the presence of N-linked carbohydrate moieties.
9925876	9	4	theme	HERGGFP	1153:1159	arg1	mass					1145:1148	the molecular mass	1131:1148	the molecular mass	1131:1148	Immunoblot analysis revealed that N-glycosidase F shifted the molecular mass of HERGGFP, stably expressed in HEK 293 cells, indicating the presence of N-linked carbohydrate moieties.
9925876	10	5	dep	sites	1331:1335	arg1	sites					1331:1335	the two putative extracellular N-linked glycosylation sites	1277:1335	the two putative extracellular N-linked glycosylation sites (N598Q and N629Q)	1277:1353	Mutations at each of the two putative extracellular N-linked glycosylation sites (N598Q and N629Q) led to a perinuclear subcellular localization of HERGGFP stably expressed in HEK 293 cells, with no surface membrane expression.
9925876	10	5	dep	sites	1331:1335	arg1	N629Q					1348:1352	N629Q	1348:1352	N629Q	1348:1352	Mutations at each of the two putative extracellular N-linked glycosylation sites (N598Q and N629Q) led to a perinuclear subcellular localization of HERGGFP stably expressed in HEK 293 cells, with no surface membrane expression.
9925876	10	5	dep	sites	1331:1335	arg1	N598Q					1338:1342	N598Q	1338:1342	N598Q	1338:1342	Mutations at each of the two putative extracellular N-linked glycosylation sites (N598Q and N629Q) led to a perinuclear subcellular localization of HERGGFP stably expressed in HEK 293 cells, with no surface membrane expression.
9925876	0	6	link	N-linked	0:7	arg1	sites					23:27	N-linked glycosylation sites	0:27	N-linked glycosylation sites	0:27	N-linked glycosylation sites determine HERG channel surface membrane expression.
9925876	4	7	theme	K+	620:621	arg1	channels					623:630	voltage-gated K+ channels	606:630	voltage-gated K+ channels	606:630	While a recent report indicates that LQT in some patients is associated with a mutation of HERG at a consensus extracellular N-linked glycosylation site (N629), earlier studies failed to identify a role for N-linked glycosylation in the functional expression of voltage-gated K+ channels.
9925876	10	8	theme	subcellular	1376:1386	arg1	localization					1388:1399	a perinuclear subcellular localization	1362:1399	a perinuclear subcellular localization of HERGGFP stably expressed in HEK 293 cells, with no surface membrane expression	1362:1481	Mutations at each of the two putative extracellular N-linked glycosylation sites (N598Q and N629Q) led to a perinuclear subcellular localization of HERGGFP stably expressed in HEK 293 cells, with no surface membrane expression.
9925876	5	9	link	N-linked	738:745	arg1	glycosylation					747:759	N-linked glycosylation	738:759	N-linked glycosylation	738:759	In this study we used pharmacological agents and site-directed mutagenesis to assess the contribution of N-linked glycosylation to the surface localization of HERG channels.
9925876	4	10	link	N-linked	469:476	arg1	N629					498:501	N629	498:501	N629	498:501	While a recent report indicates that LQT in some patients is associated with a mutation of HERG at a consensus extracellular N-linked glycosylation site (N629), earlier studies failed to identify a role for N-linked glycosylation in the functional expression of voltage-gated K+ channels.
9925876	4	10	link	N-linked	469:476	arg1	site					492:495	a consensus extracellular N-linked glycosylation site	443:495	a consensus extracellular N-linked glycosylation site (N629)	443:502	While a recent report indicates that LQT in some patients is associated with a mutation of HERG at a consensus extracellular N-linked glycosylation site (N629), earlier studies failed to identify a role for N-linked glycosylation in the functional expression of voltage-gated K+ channels.
9925876	4	11	theme	functional	581:590	arg1	expression					592:601	the functional expression	577:601	the functional expression of voltage-gated K+ channels	577:630	While a recent report indicates that LQT in some patients is associated with a mutation of HERG at a consensus extracellular N-linked glycosylation site (N629), earlier studies failed to identify a role for N-linked glycosylation in the functional expression of voltage-gated K+ channels.
9925876	13	12	theme	HERG	1733:1736	arg1	expression					1719:1728	surface membrane expression	1702:1728	surface membrane expression of HERG	1702:1736	Taken together, these results strongly suggest that N-linked glycosylation is required for surface membrane expression of HERG.
9925876	5	13	theme	pharmacological	655:669	arg1	agents					671:676	pharmacological agents	655:676	pharmacological agents	655:676	In this study we used pharmacological agents and site-directed mutagenesis to assess the contribution of N-linked glycosylation to the surface localization of HERG channels.
9925876	14	14	theme	HERG	1863:1866	arg1	mutations					1850:1858	N-linked glycosylation-related mutations	1819:1858	N-linked glycosylation-related mutations of HERG	1819:1866	These findings may provide insight into a mechanism responsible for LQT2 due to N-linked glycosylation-related mutations of HERG.
9925876	11	15	from	absence	1552:1558	arg1	mutants					1599:1605	the N-glycosylation mutants	1579:1605	the N-glycosylation mutants	1579:1605	Furthermore, patch clamp analysis revealed that there was a virtual absence of HERG current in the N-glycosylation mutants.
9925876	4	16	from	site	492:495	arg1	mutation					423:430	a mutation	421:430	a mutation of HERG at a consensus extracellular N-linked glycosylation site (N629)	421:502	While a recent report indicates that LQT in some patients is associated with a mutation of HERG at a consensus extracellular N-linked glycosylation site (N629), earlier studies failed to identify a role for N-linked glycosylation in the functional expression of voltage-gated K+ channels.
9925876	13	17	theme	surface	1702:1708	arg1	expression					1719:1728	surface membrane expression	1702:1728	surface membrane expression of HERG	1702:1736	Taken together, these results strongly suggest that N-linked glycosylation is required for surface membrane expression of HERG.
9925876	2	18	theme	QT	89:90	arg1	disorder					134:141	an electrophysiological disorder	110:141	an electrophysiological disorder that can lead to sudden death from cardiac arrhythmias	110:196	Long QT syndrome (LQT) is an electrophysiological disorder that can lead to sudden death from cardiac arrhythmias.
9925876	2	18	theme	QT	89:90	arg1	LQT					102:104	LQT	102:104	LQT	102:104	Long QT syndrome (LQT) is an electrophysiological disorder that can lead to sudden death from cardiac arrhythmias.
9925876	2	18	theme	QT	89:90	arg1	syndrome					92:99	Long QT syndrome	84:99	Long QT syndrome (LQT)	84:105	Long QT syndrome (LQT) is an electrophysiological disorder that can lead to sudden death from cardiac arrhythmias.
9925876	14	19	theme	N-linked	1819:1826	arg1	mutations					1850:1858	N-linked glycosylation-related mutations	1819:1858	N-linked glycosylation-related mutations of HERG	1819:1866	These findings may provide insight into a mechanism responsible for LQT2 due to N-linked glycosylation-related mutations of HERG.
9925876	3	20	theme	ether-a-go-go-related	261:281	arg1	gene					283:286	the human ether-a-go-go-related gene	251:286	the human ether-a-go-go-related gene (HERG) that encodes a voltage-gated cardiac K+ channel	251:341	One form of LQT has been attributed to mutations in the human ether-a-go-go-related gene (HERG) that encodes a voltage-gated cardiac K+ channel.
9925876	3	20	theme	ether-a-go-go-related	261:281	arg1	channel					335:341	a voltage-gated cardiac K+ channel	308:341	a voltage-gated cardiac K+ channel	308:341	One form of LQT has been attributed to mutations in the human ether-a-go-go-related gene (HERG) that encodes a voltage-gated cardiac K+ channel.
9925876	3	20	theme	ether-a-go-go-related	261:281	arg1	HERG					289:292	HERG	289:292	HERG	289:292	One form of LQT has been attributed to mutations in the human ether-a-go-go-related gene (HERG) that encodes a voltage-gated cardiac K+ channel.
9925876	10	21	from	each	1269:1272	arg1	Mutations					1256:1264	Mutations	1256:1264	Mutations at each of the two putative extracellular N-linked glycosylation sites (N598Q and N629Q)	1256:1353	Mutations at each of the two putative extracellular N-linked glycosylation sites (N598Q and N629Q) led to a perinuclear subcellular localization of HERGGFP stably expressed in HEK 293 cells, with no surface membrane expression.
9925876	7	22	theme	embryonic	1004:1012	arg1	kidney					1014:1019	human embryonic kidney	998:1019	human embryonic kidney (HEK 293) cells imaged with confocal microscopy	998:1067	Tunicamycin, an inhibitor of N-linked glycosylation, blocked normal surface membrane expression of a HERG-green fluorescent protein (GFP) fusion protein (HERGGFP) transiently expressed in human embryonic kidney (HEK 293) cells imaged with confocal microscopy.
9925876	7	22	theme	embryonic	1004:1012	arg1	HEK					1022:1024	HEK 293	1022:1028	HEK 293	1022:1028	Tunicamycin, an inhibitor of N-linked glycosylation, blocked normal surface membrane expression of a HERG-green fluorescent protein (GFP) fusion protein (HERGGFP) transiently expressed in human embryonic kidney (HEK 293) cells imaged with confocal microscopy.
9925876	13	23	gly	glycosylation	1672:1684	arg1	surface					1702:1708	surface membrane expression	1702:1728	surface membrane expression of HERG	1702:1736	Taken together, these results strongly suggest that N-linked glycosylation is required for surface membrane expression of HERG.
9925876	13	23	gly	glycosylation	1672:1684	arg1	membrane					1710:1717	surface membrane expression	1702:1728	surface membrane expression of HERG	1702:1736	Taken together, these results strongly suggest that N-linked glycosylation is required for surface membrane expression of HERG.
9925876	13	23	gly	glycosylation	1672:1684	arg1	HERG					1733:1736	HERG	1733:1736	HERG	1733:1736	Taken together, these results strongly suggest that N-linked glycosylation is required for surface membrane expression of HERG.
9925876	9	24	theme	carbohydrate	1233:1244	arg1	moieties					1246:1253	N-linked carbohydrate moieties	1224:1253	N-linked carbohydrate moieties	1224:1253	Immunoblot analysis revealed that N-glycosidase F shifted the molecular mass of HERGGFP, stably expressed in HEK 293 cells, indicating the presence of N-linked carbohydrate moieties.
9925876	7	25	theme	fusion	948:953	arg1	HERGGFP					964:970	HERGGFP	964:970	HERGGFP	964:970	Tunicamycin, an inhibitor of N-linked glycosylation, blocked normal surface membrane expression of a HERG-green fluorescent protein (GFP) fusion protein (HERGGFP) transiently expressed in human embryonic kidney (HEK 293) cells imaged with confocal microscopy.
9925876	7	25	theme	fusion	948:953	arg1	protein					955:961	a HERG-green fluorescent protein (GFP) fusion protein	909:961	a HERG-green fluorescent protein (GFP) fusion protein (HERGGFP) transiently expressed in human embryonic kidney (HEK 293) cells imaged with confocal microscopy	909:1067	Tunicamycin, an inhibitor of N-linked glycosylation, blocked normal surface membrane expression of a HERG-green fluorescent protein (GFP) fusion protein (HERGGFP) transiently expressed in human embryonic kidney (HEK 293) cells imaged with confocal microscopy.
9925876	10	26	gly	glycosylation	1317:1329	arg2	N598Q					1338:1342	N598Q	1338:1342	N598Q	1338:1342	Mutations at each of the two putative extracellular N-linked glycosylation sites (N598Q and N629Q) led to a perinuclear subcellular localization of HERGGFP stably expressed in HEK 293 cells, with no surface membrane expression.
9925876	10	26	gly	glycosylation	1317:1329	arg2	two					1281:1283	two	1281:1283	two	1281:1283	Mutations at each of the two putative extracellular N-linked glycosylation sites (N598Q and N629Q) led to a perinuclear subcellular localization of HERGGFP stably expressed in HEK 293 cells, with no surface membrane expression.
9925876	10	26	gly	glycosylation	1317:1329	arg2	sites					1331:1335	the two putative extracellular N-linked glycosylation sites	1277:1335	the two putative extracellular N-linked glycosylation sites (N598Q and N629Q)	1277:1353	Mutations at each of the two putative extracellular N-linked glycosylation sites (N598Q and N629Q) led to a perinuclear subcellular localization of HERGGFP stably expressed in HEK 293 cells, with no surface membrane expression.
9925876	10	26	gly	glycosylation	1317:1329	arg2	N629Q					1348:1352	N629Q	1348:1352	N629Q	1348:1352	Mutations at each of the two putative extracellular N-linked glycosylation sites (N598Q and N629Q) led to a perinuclear subcellular localization of HERGGFP stably expressed in HEK 293 cells, with no surface membrane expression.
9925876	4	27	theme	consensus	445:453	arg1	N629					498:501	N629	498:501	N629	498:501	While a recent report indicates that LQT in some patients is associated with a mutation of HERG at a consensus extracellular N-linked glycosylation site (N629), earlier studies failed to identify a role for N-linked glycosylation in the functional expression of voltage-gated K+ channels.
9925876	4	27	theme	consensus	445:453	arg1	site					492:495	a consensus extracellular N-linked glycosylation site	443:495	a consensus extracellular N-linked glycosylation site (N629)	443:502	While a recent report indicates that LQT in some patients is associated with a mutation of HERG at a consensus extracellular N-linked glycosylation site (N629), earlier studies failed to identify a role for N-linked glycosylation in the functional expression of voltage-gated K+ channels.
9925876	5	28	theme	N-linked	738:745	arg1	glycosylation					747:759	N-linked glycosylation	738:759	N-linked glycosylation	738:759	In this study we used pharmacological agents and site-directed mutagenesis to assess the contribution of N-linked glycosylation to the surface localization of HERG channels.
9925876	7	29	theme	GFP	943:945	arg1	HERGGFP					964:970	HERGGFP	964:970	HERGGFP	964:970	Tunicamycin, an inhibitor of N-linked glycosylation, blocked normal surface membrane expression of a HERG-green fluorescent protein (GFP) fusion protein (HERGGFP) transiently expressed in human embryonic kidney (HEK 293) cells imaged with confocal microscopy.
9925876	7	29	theme	GFP	943:945	arg1	protein					955:961	a HERG-green fluorescent protein (GFP) fusion protein	909:961	a HERG-green fluorescent protein (GFP) fusion protein (HERGGFP) transiently expressed in human embryonic kidney (HEK 293) cells imaged with confocal microscopy	909:1067	Tunicamycin, an inhibitor of N-linked glycosylation, blocked normal surface membrane expression of a HERG-green fluorescent protein (GFP) fusion protein (HERGGFP) transiently expressed in human embryonic kidney (HEK 293) cells imaged with confocal microscopy.
9925876	3	30	theme	K+	332:333	arg1	gene					283:286	the human ether-a-go-go-related gene	251:286	the human ether-a-go-go-related gene (HERG) that encodes a voltage-gated cardiac K+ channel	251:341	One form of LQT has been attributed to mutations in the human ether-a-go-go-related gene (HERG) that encodes a voltage-gated cardiac K+ channel.
9925876	3	30	theme	K+	332:333	arg1	channel					335:341	a voltage-gated cardiac K+ channel	308:341	a voltage-gated cardiac K+ channel	308:341	One form of LQT has been attributed to mutations in the human ether-a-go-go-related gene (HERG) that encodes a voltage-gated cardiac K+ channel.
9925876	4	31	theme	N-linked	469:476	arg1	N629					498:501	N629	498:501	N629	498:501	While a recent report indicates that LQT in some patients is associated with a mutation of HERG at a consensus extracellular N-linked glycosylation site (N629), earlier studies failed to identify a role for N-linked glycosylation in the functional expression of voltage-gated K+ channels.
9925876	4	31	theme	N-linked	469:476	arg1	site					492:495	a consensus extracellular N-linked glycosylation site	443:495	a consensus extracellular N-linked glycosylation site (N629)	443:502	While a recent report indicates that LQT in some patients is associated with a mutation of HERG at a consensus extracellular N-linked glycosylation site (N629), earlier studies failed to identify a role for N-linked glycosylation in the functional expression of voltage-gated K+ channels.
9925876	13	32	theme	N-linked	1663:1670	arg1	glycosylation					1672:1684	N-linked glycosylation	1663:1684	N-linked glycosylation	1663:1684	Taken together, these results strongly suggest that N-linked glycosylation is required for surface membrane expression of HERG.
9925876	7	33	theme	protein	934:940	arg1	HERGGFP					964:970	HERGGFP	964:970	HERGGFP	964:970	Tunicamycin, an inhibitor of N-linked glycosylation, blocked normal surface membrane expression of a HERG-green fluorescent protein (GFP) fusion protein (HERGGFP) transiently expressed in human embryonic kidney (HEK 293) cells imaged with confocal microscopy.
9925876	7	33	theme	protein	934:940	arg1	protein					955:961	a HERG-green fluorescent protein (GFP) fusion protein	909:961	a HERG-green fluorescent protein (GFP) fusion protein (HERGGFP) transiently expressed in human embryonic kidney (HEK 293) cells imaged with confocal microscopy	909:1067	Tunicamycin, an inhibitor of N-linked glycosylation, blocked normal surface membrane expression of a HERG-green fluorescent protein (GFP) fusion protein (HERGGFP) transiently expressed in human embryonic kidney (HEK 293) cells imaged with confocal microscopy.
9925876	3	34	theme	voltage-gated	310:322	arg1	gene					283:286	the human ether-a-go-go-related gene	251:286	the human ether-a-go-go-related gene (HERG) that encodes a voltage-gated cardiac K+ channel	251:341	One form of LQT has been attributed to mutations in the human ether-a-go-go-related gene (HERG) that encodes a voltage-gated cardiac K+ channel.
9925876	3	34	theme	voltage-gated	310:322	arg1	channel					335:341	a voltage-gated cardiac K+ channel	308:341	a voltage-gated cardiac K+ channel	308:341	One form of LQT has been attributed to mutations in the human ether-a-go-go-related gene (HERG) that encodes a voltage-gated cardiac K+ channel.
9925876	0	35	theme	channel	44:50	arg1	expression					69:78	HERG channel surface membrane expression	39:78	HERG channel surface membrane expression	39:78	N-linked glycosylation sites determine HERG channel surface membrane expression.
9925876	7	36	theme	HERG-green	911:920	arg1	HERGGFP					964:970	HERGGFP	964:970	HERGGFP	964:970	Tunicamycin, an inhibitor of N-linked glycosylation, blocked normal surface membrane expression of a HERG-green fluorescent protein (GFP) fusion protein (HERGGFP) transiently expressed in human embryonic kidney (HEK 293) cells imaged with confocal microscopy.
9925876	7	36	theme	HERG-green	911:920	arg1	protein					955:961	a HERG-green fluorescent protein (GFP) fusion protein	909:961	a HERG-green fluorescent protein (GFP) fusion protein (HERGGFP) transiently expressed in human embryonic kidney (HEK 293) cells imaged with confocal microscopy	909:1067	Tunicamycin, an inhibitor of N-linked glycosylation, blocked normal surface membrane expression of a HERG-green fluorescent protein (GFP) fusion protein (HERGGFP) transiently expressed in human embryonic kidney (HEK 293) cells imaged with confocal microscopy.
9925876	0	37	theme	N-linked	0:7	arg1	sites					23:27	N-linked glycosylation sites	0:27	N-linked glycosylation sites	0:27	N-linked glycosylation sites determine HERG channel surface membrane expression.
9925876	5	38	theme	channels	797:804	arg1	localization					776:787	the surface localization	764:787	the surface localization of HERG channels	764:804	In this study we used pharmacological agents and site-directed mutagenesis to assess the contribution of N-linked glycosylation to the surface localization of HERG channels.
9925876	14	39	link	N-linked	1819:1826	arg1	mutations					1850:1858	N-linked glycosylation-related mutations	1819:1858	N-linked glycosylation-related mutations of HERG	1819:1866	These findings may provide insight into a mechanism responsible for LQT2 due to N-linked glycosylation-related mutations of HERG.
9925876	2	40	theme	sudden	160:165	arg1	death					167:171	sudden death	160:171	sudden death from cardiac arrhythmias	160:196	Long QT syndrome (LQT) is an electrophysiological disorder that can lead to sudden death from cardiac arrhythmias.
9925876	9	41	theme	Immunoblot	1073:1082	arg1	analysis					1084:1091	Immunoblot analysis	1073:1091	Immunoblot analysis	1073:1091	Immunoblot analysis revealed that N-glycosidase F shifted the molecular mass of HERGGFP, stably expressed in HEK 293 cells, indicating the presence of N-linked carbohydrate moieties.
9925876	0	42	theme	HERG	39:42	arg1	expression					69:78	HERG channel surface membrane expression	39:78	HERG channel surface membrane expression	39:78	N-linked glycosylation sites determine HERG channel surface membrane expression.
9925876	4	43	link	N-linked	551:558	arg1	glycosylation					560:572	N-linked glycosylation	551:572	N-linked glycosylation	551:572	While a recent report indicates that LQT in some patients is associated with a mutation of HERG at a consensus extracellular N-linked glycosylation site (N629), earlier studies failed to identify a role for N-linked glycosylation in the functional expression of voltage-gated K+ channels.
9925876	0	44	gly	glycosylation	9:21	arg2	sites					23:27	N-linked glycosylation sites	0:27	N-linked glycosylation sites	0:27	N-linked glycosylation sites determine HERG channel surface membrane expression.
9925876	10	45	theme	extracellular	1294:1306	arg1	sites					1331:1335	the two putative extracellular N-linked glycosylation sites	1277:1335	the two putative extracellular N-linked glycosylation sites (N598Q and N629Q)	1277:1353	Mutations at each of the two putative extracellular N-linked glycosylation sites (N598Q and N629Q) led to a perinuclear subcellular localization of HERGGFP stably expressed in HEK 293 cells, with no surface membrane expression.
9925876	10	45	theme	extracellular	1294:1306	arg1	N629Q					1348:1352	N629Q	1348:1352	N629Q	1348:1352	Mutations at each of the two putative extracellular N-linked glycosylation sites (N598Q and N629Q) led to a perinuclear subcellular localization of HERGGFP stably expressed in HEK 293 cells, with no surface membrane expression.
9925876	10	45	theme	extracellular	1294:1306	arg1	N598Q					1338:1342	N598Q	1338:1342	N598Q	1338:1342	Mutations at each of the two putative extracellular N-linked glycosylation sites (N598Q and N629Q) led to a perinuclear subcellular localization of HERGGFP stably expressed in HEK 293 cells, with no surface membrane expression.
9925876	5	46	theme	surface	768:774	arg1	localization					776:787	the surface localization	764:787	the surface localization of HERG channels	764:804	In this study we used pharmacological agents and site-directed mutagenesis to assess the contribution of N-linked glycosylation to the surface localization of HERG channels.
9925876	10	47	theme	membrane	1463:1470	arg1	expression					1472:1481	no surface membrane expression	1452:1481	no surface membrane expression	1452:1481	Mutations at each of the two putative extracellular N-linked glycosylation sites (N598Q and N629Q) led to a perinuclear subcellular localization of HERGGFP stably expressed in HEK 293 cells, with no surface membrane expression.
9925876	9	48	theme	N-glycosidase	1107:1119	arg1	F					1121:1121	N-glycosidase F	1107:1121	N-glycosidase F	1107:1121	Immunoblot analysis revealed that N-glycosidase F shifted the molecular mass of HERGGFP, stably expressed in HEK 293 cells, indicating the presence of N-linked carbohydrate moieties.
9925876	11	49	theme	virtual	1544:1550	arg1	absence					1552:1558	a virtual absence	1542:1558	a virtual absence of HERG current in the N-glycosylation mutants	1542:1605	Furthermore, patch clamp analysis revealed that there was a virtual absence of HERG current in the N-glycosylation mutants.
9925876	7	50	theme	surface	878:884	arg1	expression					895:904	normal surface membrane expression	871:904	normal surface membrane expression of a HERG-green fluorescent protein (GFP) fusion protein (HERGGFP) transiently expressed in human embryonic kidney (HEK 293) cells imaged with confocal microscopy	871:1067	Tunicamycin, an inhibitor of N-linked glycosylation, blocked normal surface membrane expression of a HERG-green fluorescent protein (GFP) fusion protein (HERGGFP) transiently expressed in human embryonic kidney (HEK 293) cells imaged with confocal microscopy.
9925876	10	51	link	N-linked	1308:1315	arg1	sites					1331:1335	the two putative extracellular N-linked glycosylation sites	1277:1335	the two putative extracellular N-linked glycosylation sites (N598Q and N629Q)	1277:1353	Mutations at each of the two putative extracellular N-linked glycosylation sites (N598Q and N629Q) led to a perinuclear subcellular localization of HERGGFP stably expressed in HEK 293 cells, with no surface membrane expression.
9925876	10	51	link	N-linked	1308:1315	arg1	N629Q					1348:1352	N629Q	1348:1352	N629Q	1348:1352	Mutations at each of the two putative extracellular N-linked glycosylation sites (N598Q and N629Q) led to a perinuclear subcellular localization of HERGGFP stably expressed in HEK 293 cells, with no surface membrane expression.
9925876	10	51	link	N-linked	1308:1315	arg1	N598Q					1338:1342	N598Q	1338:1342	N598Q	1338:1342	Mutations at each of the two putative extracellular N-linked glycosylation sites (N598Q and N629Q) led to a perinuclear subcellular localization of HERGGFP stably expressed in HEK 293 cells, with no surface membrane expression.
9925876	10	52	theme	glycosylation	1317:1329	arg1	sites					1331:1335	the two putative extracellular N-linked glycosylation sites	1277:1335	the two putative extracellular N-linked glycosylation sites (N598Q and N629Q)	1277:1353	Mutations at each of the two putative extracellular N-linked glycosylation sites (N598Q and N629Q) led to a perinuclear subcellular localization of HERGGFP stably expressed in HEK 293 cells, with no surface membrane expression.
9925876	10	52	theme	glycosylation	1317:1329	arg1	N629Q					1348:1352	N629Q	1348:1352	N629Q	1348:1352	Mutations at each of the two putative extracellular N-linked glycosylation sites (N598Q and N629Q) led to a perinuclear subcellular localization of HERGGFP stably expressed in HEK 293 cells, with no surface membrane expression.
9925876	10	52	theme	glycosylation	1317:1329	arg1	N598Q					1338:1342	N598Q	1338:1342	N598Q	1338:1342	Mutations at each of the two putative extracellular N-linked glycosylation sites (N598Q and N629Q) led to a perinuclear subcellular localization of HERGGFP stably expressed in HEK 293 cells, with no surface membrane expression.
9925876	3	53	from	mutations	238:246	arg1	gene					283:286	the human ether-a-go-go-related gene	251:286	the human ether-a-go-go-related gene (HERG) that encodes a voltage-gated cardiac K+ channel	251:341	One form of LQT has been attributed to mutations in the human ether-a-go-go-related gene (HERG) that encodes a voltage-gated cardiac K+ channel.
9925876	3	53	from	mutations	238:246	arg1	channel					335:341	a voltage-gated cardiac K+ channel	308:341	a voltage-gated cardiac K+ channel	308:341	One form of LQT has been attributed to mutations in the human ether-a-go-go-related gene (HERG) that encodes a voltage-gated cardiac K+ channel.
9925876	3	53	from	mutations	238:246	arg1	HERG					289:292	HERG	289:292	HERG	289:292	One form of LQT has been attributed to mutations in the human ether-a-go-go-related gene (HERG) that encodes a voltage-gated cardiac K+ channel.
9925876	3	54	theme	LQT	211:213	arg1	form					203:206	One form	199:206	One form of LQT	199:213	One form of LQT has been attributed to mutations in the human ether-a-go-go-related gene (HERG) that encodes a voltage-gated cardiac K+ channel.
9925876	11	55	theme	N-glycosylation	1583:1597	arg1	mutants					1599:1605	the N-glycosylation mutants	1579:1605	the N-glycosylation mutants	1579:1605	Furthermore, patch clamp analysis revealed that there was a virtual absence of HERG current in the N-glycosylation mutants.
9925876	11	56	theme	clamp	1503:1507	arg1	analysis					1509:1516	patch clamp analysis	1497:1516	patch clamp analysis	1497:1516	Furthermore, patch clamp analysis revealed that there was a virtual absence of HERG current in the N-glycosylation mutants.
9925876	7	57	theme	glycosylation	848:860	arg1	Tunicamycin					810:820	Tunicamycin	810:820	Tunicamycin	810:820	Tunicamycin, an inhibitor of N-linked glycosylation, blocked normal surface membrane expression of a HERG-green fluorescent protein (GFP) fusion protein (HERGGFP) transiently expressed in human embryonic kidney (HEK 293) cells imaged with confocal microscopy.
9925876	7	57	theme	glycosylation	848:860	arg1	inhibitor					826:834	an inhibitor	823:834	an inhibitor of N-linked glycosylation	823:860	Tunicamycin, an inhibitor of N-linked glycosylation, blocked normal surface membrane expression of a HERG-green fluorescent protein (GFP) fusion protein (HERGGFP) transiently expressed in human embryonic kidney (HEK 293) cells imaged with confocal microscopy.
9925876	11	58	theme	HERG	1563:1566	arg1	current					1568:1574	HERG current	1563:1574	HERG current	1563:1574	Furthermore, patch clamp analysis revealed that there was a virtual absence of HERG current in the N-glycosylation mutants.
9925876	7	59	theme	confocal	1049:1056	arg1	microscopy					1058:1067	confocal microscopy	1049:1067	confocal microscopy	1049:1067	Tunicamycin, an inhibitor of N-linked glycosylation, blocked normal surface membrane expression of a HERG-green fluorescent protein (GFP) fusion protein (HERGGFP) transiently expressed in human embryonic kidney (HEK 293) cells imaged with confocal microscopy.
9925876	2	60	from	arrhythmias	186:196	arg1	death					167:171	sudden death	160:171	sudden death from cardiac arrhythmias	160:196	Long QT syndrome (LQT) is an electrophysiological disorder that can lead to sudden death from cardiac arrhythmias.
9925876	4	61	theme	voltage-gated	606:618	arg1	channels					623:630	voltage-gated K+ channels	606:630	voltage-gated K+ channels	606:630	While a recent report indicates that LQT in some patients is associated with a mutation of HERG at a consensus extracellular N-linked glycosylation site (N629), earlier studies failed to identify a role for N-linked glycosylation in the functional expression of voltage-gated K+ channels.
9925876	13	62	theme	membrane	1710:1717	arg1	expression					1719:1728	surface membrane expression	1702:1728	surface membrane expression of HERG	1702:1736	Taken together, these results strongly suggest that N-linked glycosylation is required for surface membrane expression of HERG.
9925876	2	63	theme	electrophysiological	113:132	arg1	disorder					134:141	an electrophysiological disorder	110:141	an electrophysiological disorder that can lead to sudden death from cardiac arrhythmias	110:196	Long QT syndrome (LQT) is an electrophysiological disorder that can lead to sudden death from cardiac arrhythmias.
9925876	2	63	theme	electrophysiological	113:132	arg1	syndrome					92:99	Long QT syndrome	84:99	Long QT syndrome (LQT)	84:105	Long QT syndrome (LQT) is an electrophysiological disorder that can lead to sudden death from cardiac arrhythmias.
9925876	10	64	theme	perinuclear	1364:1374	arg1	localization					1388:1399	a perinuclear subcellular localization	1362:1399	a perinuclear subcellular localization of HERGGFP stably expressed in HEK 293 cells, with no surface membrane expression	1362:1481	Mutations at each of the two putative extracellular N-linked glycosylation sites (N598Q and N629Q) led to a perinuclear subcellular localization of HERGGFP stably expressed in HEK 293 cells, with no surface membrane expression.
9925876	4	65	gly	glycosylation	478:490	arg2	site					492:495	a consensus extracellular N-linked glycosylation site	443:495	a consensus extracellular N-linked glycosylation site (N629)	443:502	While a recent report indicates that LQT in some patients is associated with a mutation of HERG at a consensus extracellular N-linked glycosylation site (N629), earlier studies failed to identify a role for N-linked glycosylation in the functional expression of voltage-gated K+ channels.
9925876	4	65	gly	glycosylation	478:490	arg2	N629					498:501	N629	498:501	N629	498:501	While a recent report indicates that LQT in some patients is associated with a mutation of HERG at a consensus extracellular N-linked glycosylation site (N629), earlier studies failed to identify a role for N-linked glycosylation in the functional expression of voltage-gated K+ channels.
9925876	4	66	theme	recent	352:357	arg1	report					359:364	a recent report	350:364	a recent report	350:364	While a recent report indicates that LQT in some patients is associated with a mutation of HERG at a consensus extracellular N-linked glycosylation site (N629), earlier studies failed to identify a role for N-linked glycosylation in the functional expression of voltage-gated K+ channels.
9925876	0	67	theme	surface	52:58	arg1	expression					69:78	HERG channel surface membrane expression	39:78	HERG channel surface membrane expression	39:78	N-linked glycosylation sites determine HERG channel surface membrane expression.
9925876	4	68	theme	channels	623:630	arg1	expression					592:601	the functional expression	577:601	the functional expression of voltage-gated K+ channels	577:630	While a recent report indicates that LQT in some patients is associated with a mutation of HERG at a consensus extracellular N-linked glycosylation site (N629), earlier studies failed to identify a role for N-linked glycosylation in the functional expression of voltage-gated K+ channels.
9925876	9	69	theme	HEK	1182:1184	arg1	cells					1190:1194	HEK 293 cells	1182:1194	HEK 293 cells	1182:1194	Immunoblot analysis revealed that N-glycosidase F shifted the molecular mass of HERGGFP, stably expressed in HEK 293 cells, indicating the presence of N-linked carbohydrate moieties.
9925876	13	70	link	N-linked	1663:1670	arg1	glycosylation					1672:1684	N-linked glycosylation	1663:1684	N-linked glycosylation	1663:1684	Taken together, these results strongly suggest that N-linked glycosylation is required for surface membrane expression of HERG.
9925876	3	71	theme	human	255:259	arg1	gene					283:286	the human ether-a-go-go-related gene	251:286	the human ether-a-go-go-related gene (HERG) that encodes a voltage-gated cardiac K+ channel	251:341	One form of LQT has been attributed to mutations in the human ether-a-go-go-related gene (HERG) that encodes a voltage-gated cardiac K+ channel.
9925876	3	71	theme	human	255:259	arg1	channel					335:341	a voltage-gated cardiac K+ channel	308:341	a voltage-gated cardiac K+ channel	308:341	One form of LQT has been attributed to mutations in the human ether-a-go-go-related gene (HERG) that encodes a voltage-gated cardiac K+ channel.
9925876	3	71	theme	human	255:259	arg1	HERG					289:292	HERG	289:292	HERG	289:292	One form of LQT has been attributed to mutations in the human ether-a-go-go-related gene (HERG) that encodes a voltage-gated cardiac K+ channel.
9925876	4	72	from	role	542:545	arg1	expression					592:601	the functional expression	577:601	the functional expression of voltage-gated K+ channels	577:630	While a recent report indicates that LQT in some patients is associated with a mutation of HERG at a consensus extracellular N-linked glycosylation site (N629), earlier studies failed to identify a role for N-linked glycosylation in the functional expression of voltage-gated K+ channels.
9925876	7	73	theme	kidney	1014:1019	arg1	cells					1031:1035	human embryonic kidney (HEK 293) cells	998:1035	human embryonic kidney (HEK 293) cells imaged with confocal microscopy	998:1067	Tunicamycin, an inhibitor of N-linked glycosylation, blocked normal surface membrane expression of a HERG-green fluorescent protein (GFP) fusion protein (HERGGFP) transiently expressed in human embryonic kidney (HEK 293) cells imaged with confocal microscopy.
9925876	14	74	theme	glycosylation-related	1828:1848	arg1	mutations					1850:1858	N-linked glycosylation-related mutations	1819:1858	N-linked glycosylation-related mutations of HERG	1819:1866	These findings may provide insight into a mechanism responsible for LQT2 due to N-linked glycosylation-related mutations of HERG.
9925876	5	75	used	used	650:653	arg2	we					647:648	we	647:648	we	647:648	In this study we used pharmacological agents and site-directed mutagenesis to assess the contribution of N-linked glycosylation to the surface localization of HERG channels.
9925876	2	76	theme	Long	84:87	arg1	disorder					134:141	an electrophysiological disorder	110:141	an electrophysiological disorder that can lead to sudden death from cardiac arrhythmias	110:196	Long QT syndrome (LQT) is an electrophysiological disorder that can lead to sudden death from cardiac arrhythmias.
9925876	2	76	theme	Long	84:87	arg1	LQT					102:104	LQT	102:104	LQT	102:104	Long QT syndrome (LQT) is an electrophysiological disorder that can lead to sudden death from cardiac arrhythmias.
9925876	2	76	theme	Long	84:87	arg1	syndrome					92:99	Long QT syndrome	84:99	Long QT syndrome (LQT)	84:105	Long QT syndrome (LQT) is an electrophysiological disorder that can lead to sudden death from cardiac arrhythmias.
9925876	7	77	theme	human	998:1002	arg1	kidney					1014:1019	human embryonic kidney	998:1019	human embryonic kidney (HEK 293) cells imaged with confocal microscopy	998:1067	Tunicamycin, an inhibitor of N-linked glycosylation, blocked normal surface membrane expression of a HERG-green fluorescent protein (GFP) fusion protein (HERGGFP) transiently expressed in human embryonic kidney (HEK 293) cells imaged with confocal microscopy.
9925876	7	77	theme	human	998:1002	arg1	HEK					1022:1024	HEK 293	1022:1028	HEK 293	1022:1028	Tunicamycin, an inhibitor of N-linked glycosylation, blocked normal surface membrane expression of a HERG-green fluorescent protein (GFP) fusion protein (HERGGFP) transiently expressed in human embryonic kidney (HEK 293) cells imaged with confocal microscopy.
9925876	9	78	link	N-linked	1224:1231	arg1	moieties					1246:1253	N-linked carbohydrate moieties	1224:1253	N-linked carbohydrate moieties	1224:1253	Immunoblot analysis revealed that N-glycosidase F shifted the molecular mass of HERGGFP, stably expressed in HEK 293 cells, indicating the presence of N-linked carbohydrate moieties.
9925876	9	79	theme	N-linked	1224:1231	arg1	moieties					1246:1253	N-linked carbohydrate moieties	1224:1253	N-linked carbohydrate moieties	1224:1253	Immunoblot analysis revealed that N-glycosidase F shifted the molecular mass of HERGGFP, stably expressed in HEK 293 cells, indicating the presence of N-linked carbohydrate moieties.
9925876	4	80	theme	extracellular	455:467	arg1	N629					498:501	N629	498:501	N629	498:501	While a recent report indicates that LQT in some patients is associated with a mutation of HERG at a consensus extracellular N-linked glycosylation site (N629), earlier studies failed to identify a role for N-linked glycosylation in the functional expression of voltage-gated K+ channels.
9925876	4	80	theme	extracellular	455:467	arg1	site					492:495	a consensus extracellular N-linked glycosylation site	443:495	a consensus extracellular N-linked glycosylation site (N629)	443:502	While a recent report indicates that LQT in some patients is associated with a mutation of HERG at a consensus extracellular N-linked glycosylation site (N629), earlier studies failed to identify a role for N-linked glycosylation in the functional expression of voltage-gated K+ channels.
9925876	9	81	theme	moieties	1246:1253	arg1	presence					1212:1219	the presence	1208:1219	the presence of N-linked carbohydrate moieties	1208:1253	Immunoblot analysis revealed that N-glycosidase F shifted the molecular mass of HERGGFP, stably expressed in HEK 293 cells, indicating the presence of N-linked carbohydrate moieties.
9925876	7	82	theme	protein	955:961	arg1	expression					895:904	normal surface membrane expression	871:904	normal surface membrane expression of a HERG-green fluorescent protein (GFP) fusion protein (HERGGFP) transiently expressed in human embryonic kidney (HEK 293) cells imaged with confocal microscopy	871:1067	Tunicamycin, an inhibitor of N-linked glycosylation, blocked normal surface membrane expression of a HERG-green fluorescent protein (GFP) fusion protein (HERGGFP) transiently expressed in human embryonic kidney (HEK 293) cells imaged with confocal microscopy.
9925876	14	83	theme	responsible	1791:1801	arg1	mechanism					1781:1789	a mechanism	1779:1789	a mechanism responsible for LQT2 due to N-linked glycosylation-related mutations of HERG	1779:1866	These findings may provide insight into a mechanism responsible for LQT2 due to N-linked glycosylation-related mutations of HERG.
9925876	4	84	theme	glycosylation	478:490	arg1	N629					498:501	N629	498:501	N629	498:501	While a recent report indicates that LQT in some patients is associated with a mutation of HERG at a consensus extracellular N-linked glycosylation site (N629), earlier studies failed to identify a role for N-linked glycosylation in the functional expression of voltage-gated K+ channels.
9925876	4	84	theme	glycosylation	478:490	arg1	site					492:495	a consensus extracellular N-linked glycosylation site	443:495	a consensus extracellular N-linked glycosylation site (N629)	443:502	While a recent report indicates that LQT in some patients is associated with a mutation of HERG at a consensus extracellular N-linked glycosylation site (N629), earlier studies failed to identify a role for N-linked glycosylation in the functional expression of voltage-gated K+ channels.
9925876	10	85	theme	HERGGFP	1404:1410	arg1	localization					1388:1399	a perinuclear subcellular localization	1362:1399	a perinuclear subcellular localization of HERGGFP stably expressed in HEK 293 cells, with no surface membrane expression	1362:1481	Mutations at each of the two putative extracellular N-linked glycosylation sites (N598Q and N629Q) led to a perinuclear subcellular localization of HERGGFP stably expressed in HEK 293 cells, with no surface membrane expression.
9925876	5	86	theme	site-directed	682:694	arg1	mutagenesis					696:706	site-directed mutagenesis	682:706	site-directed mutagenesis	682:706	In this study we used pharmacological agents and site-directed mutagenesis to assess the contribution of N-linked glycosylation to the surface localization of HERG channels.
9925876	4	87	theme	HERG	435:438	arg1	mutation					423:430	a mutation	421:430	a mutation of HERG at a consensus extracellular N-linked glycosylation site (N629)	421:502	While a recent report indicates that LQT in some patients is associated with a mutation of HERG at a consensus extracellular N-linked glycosylation site (N629), earlier studies failed to identify a role for N-linked glycosylation in the functional expression of voltage-gated K+ channels.
9925876	3	88	theme	cardiac	324:330	arg1	gene					283:286	the human ether-a-go-go-related gene	251:286	the human ether-a-go-go-related gene (HERG) that encodes a voltage-gated cardiac K+ channel	251:341	One form of LQT has been attributed to mutations in the human ether-a-go-go-related gene (HERG) that encodes a voltage-gated cardiac K+ channel.
9925876	3	88	theme	cardiac	324:330	arg1	channel					335:341	a voltage-gated cardiac K+ channel	308:341	a voltage-gated cardiac K+ channel	308:341	One form of LQT has been attributed to mutations in the human ether-a-go-go-related gene (HERG) that encodes a voltage-gated cardiac K+ channel.
9925876	10	89	theme	HEK	1432:1434	arg1	cells					1440:1444	HEK 293 cells	1432:1444	HEK 293 cells	1432:1444	Mutations at each of the two putative extracellular N-linked glycosylation sites (N598Q and N629Q) led to a perinuclear subcellular localization of HERGGFP stably expressed in HEK 293 cells, with no surface membrane expression.
9925876	0	90	theme	glycosylation	9:21	arg1	sites					23:27	N-linked glycosylation sites	0:27	N-linked glycosylation sites	0:27	N-linked glycosylation sites determine HERG channel surface membrane expression.
9925876	7	91	theme	fluorescent	922:932	arg1	HERGGFP					964:970	HERGGFP	964:970	HERGGFP	964:970	Tunicamycin, an inhibitor of N-linked glycosylation, blocked normal surface membrane expression of a HERG-green fluorescent protein (GFP) fusion protein (HERGGFP) transiently expressed in human embryonic kidney (HEK 293) cells imaged with confocal microscopy.
9925876	7	91	theme	fluorescent	922:932	arg1	protein					955:961	a HERG-green fluorescent protein (GFP) fusion protein	909:961	a HERG-green fluorescent protein (GFP) fusion protein (HERGGFP) transiently expressed in human embryonic kidney (HEK 293) cells imaged with confocal microscopy	909:1067	Tunicamycin, an inhibitor of N-linked glycosylation, blocked normal surface membrane expression of a HERG-green fluorescent protein (GFP) fusion protein (HERGGFP) transiently expressed in human embryonic kidney (HEK 293) cells imaged with confocal microscopy.
9925876	10	92	with	HERGGFP	1404:1410	arg1	expression					1472:1481	no surface membrane expression	1452:1481	no surface membrane expression	1452:1481	Mutations at each of the two putative extracellular N-linked glycosylation sites (N598Q and N629Q) led to a perinuclear subcellular localization of HERGGFP stably expressed in HEK 293 cells, with no surface membrane expression.
9925876	4	93	theme	earlier	505:511	arg1	studies					513:519	earlier studies	505:519	earlier studies	505:519	While a recent report indicates that LQT in some patients is associated with a mutation of HERG at a consensus extracellular N-linked glycosylation site (N629), earlier studies failed to identify a role for N-linked glycosylation in the functional expression of voltage-gated K+ channels.
9925876	5	94	theme	HERG	792:795	arg1	channels					797:804	HERG channels	792:804	HERG channels	792:804	In this study we used pharmacological agents and site-directed mutagenesis to assess the contribution of N-linked glycosylation to the surface localization of HERG channels.
9925876	7	95	link	N-linked	839:846	arg1	glycosylation					848:860	N-linked glycosylation	839:860	N-linked glycosylation	839:860	Tunicamycin, an inhibitor of N-linked glycosylation, blocked normal surface membrane expression of a HERG-green fluorescent protein (GFP) fusion protein (HERGGFP) transiently expressed in human embryonic kidney (HEK 293) cells imaged with confocal microscopy.
9925876	5	96	theme	glycosylation	747:759	arg1	contribution					722:733	the contribution	718:733	the contribution of N-linked glycosylation to the surface localization of HERG channels	718:804	In this study we used pharmacological agents and site-directed mutagenesis to assess the contribution of N-linked glycosylation to the surface localization of HERG channels.
9925876	10	97	theme	N-linked	1308:1315	arg1	sites					1331:1335	the two putative extracellular N-linked glycosylation sites	1277:1335	the two putative extracellular N-linked glycosylation sites (N598Q and N629Q)	1277:1353	Mutations at each of the two putative extracellular N-linked glycosylation sites (N598Q and N629Q) led to a perinuclear subcellular localization of HERGGFP stably expressed in HEK 293 cells, with no surface membrane expression.
9925876	10	97	theme	N-linked	1308:1315	arg1	N629Q					1348:1352	N629Q	1348:1352	N629Q	1348:1352	Mutations at each of the two putative extracellular N-linked glycosylation sites (N598Q and N629Q) led to a perinuclear subcellular localization of HERGGFP stably expressed in HEK 293 cells, with no surface membrane expression.
9925876	10	97	theme	N-linked	1308:1315	arg1	N598Q					1338:1342	N598Q	1338:1342	N598Q	1338:1342	Mutations at each of the two putative extracellular N-linked glycosylation sites (N598Q and N629Q) led to a perinuclear subcellular localization of HERGGFP stably expressed in HEK 293 cells, with no surface membrane expression.
9925876	0	98	theme	membrane	60:67	arg1	expression					69:78	HERG channel surface membrane expression	39:78	HERG channel surface membrane expression	39:78	N-linked glycosylation sites determine HERG channel surface membrane expression.
9925876	10	99	theme	putative	1285:1292	arg1	sites					1331:1335	the two putative extracellular N-linked glycosylation sites	1277:1335	the two putative extracellular N-linked glycosylation sites (N598Q and N629Q)	1277:1353	Mutations at each of the two putative extracellular N-linked glycosylation sites (N598Q and N629Q) led to a perinuclear subcellular localization of HERGGFP stably expressed in HEK 293 cells, with no surface membrane expression.
9925876	10	99	theme	putative	1285:1292	arg1	N629Q					1348:1352	N629Q	1348:1352	N629Q	1348:1352	Mutations at each of the two putative extracellular N-linked glycosylation sites (N598Q and N629Q) led to a perinuclear subcellular localization of HERGGFP stably expressed in HEK 293 cells, with no surface membrane expression.
9925876	10	99	theme	putative	1285:1292	arg1	N598Q					1338:1342	N598Q	1338:1342	N598Q	1338:1342	Mutations at each of the two putative extracellular N-linked glycosylation sites (N598Q and N629Q) led to a perinuclear subcellular localization of HERGGFP stably expressed in HEK 293 cells, with no surface membrane expression.
9925876	7	100	theme	membrane	886:893	arg1	expression					895:904	normal surface membrane expression	871:904	normal surface membrane expression of a HERG-green fluorescent protein (GFP) fusion protein (HERGGFP) transiently expressed in human embryonic kidney (HEK 293) cells imaged with confocal microscopy	871:1067	Tunicamycin, an inhibitor of N-linked glycosylation, blocked normal surface membrane expression of a HERG-green fluorescent protein (GFP) fusion protein (HERGGFP) transiently expressed in human embryonic kidney (HEK 293) cells imaged with confocal microscopy.
9925876	4	101	theme	N-linked	551:558	arg1	glycosylation					560:572	N-linked glycosylation	551:572	N-linked glycosylation	551:572	While a recent report indicates that LQT in some patients is associated with a mutation of HERG at a consensus extracellular N-linked glycosylation site (N629), earlier studies failed to identify a role for N-linked glycosylation in the functional expression of voltage-gated K+ channels.
9925876	10	102	theme	surface	1455:1461	arg1	expression					1472:1481	no surface membrane expression	1452:1481	no surface membrane expression	1452:1481	Mutations at each of the two putative extracellular N-linked glycosylation sites (N598Q and N629Q) led to a perinuclear subcellular localization of HERGGFP stably expressed in HEK 293 cells, with no surface membrane expression.
9925876	2	103	theme	cardiac	178:184	arg1	arrhythmias					186:196	cardiac arrhythmias	178:196	cardiac arrhythmias	178:196	Long QT syndrome (LQT) is an electrophysiological disorder that can lead to sudden death from cardiac arrhythmias.
9925876	11	104	theme	current	1568:1574	arg1	absence					1552:1558	a virtual absence	1542:1558	a virtual absence of HERG current in the N-glycosylation mutants	1542:1605	Furthermore, patch clamp analysis revealed that there was a virtual absence of HERG current in the N-glycosylation mutants.
9925876	7	105	theme	normal	871:876	arg1	expression					895:904	normal surface membrane expression	871:904	normal surface membrane expression of a HERG-green fluorescent protein (GFP) fusion protein (HERGGFP) transiently expressed in human embryonic kidney (HEK 293) cells imaged with confocal microscopy	871:1067	Tunicamycin, an inhibitor of N-linked glycosylation, blocked normal surface membrane expression of a HERG-green fluorescent protein (GFP) fusion protein (HERGGFP) transiently expressed in human embryonic kidney (HEK 293) cells imaged with confocal microscopy.
21740066	3	0	theme	fragmentation	800:812	arg1	techniques					814:823	fragmentation techniques	800:823	fragmentation techniques	800:823	By taking advantage of the recently characterized O-GlcNAc-specific IgG monoclonal antibodies and the combination of HCD and ETD fragmentation techniques, O-GlcNAc modified proteins were enriched from HEK293T cells and subsequently characterized using the LTQ Orbitrap Velos ETD (Thermo Fisher Scientific) mass spectrometer.
21740066	6	1	theme	sequence	1613:1620	arg1	stretches					1592:1600	short stretches	1586:1600	short stretches of primary sequence of the glycosylated polypeptides	1586:1653	Furthermore, this report illustrates that the O-GlcNAc transferase appears to demonstrate promiscuity with regards to the hydroxyl-containing amino acid modified in short stretches of primary sequence of the glycosylated polypeptides.
21740066	3	2	theme	Orbitrap	931:938	arg1	spectrometer					982:993	the LTQ Orbitrap Velos ETD (Thermo Fisher Scientific) mass spectrometer	923:993	the LTQ Orbitrap Velos ETD (Thermo Fisher Scientific) mass spectrometer	923:993	By taking advantage of the recently characterized O-GlcNAc-specific IgG monoclonal antibodies and the combination of HCD and ETD fragmentation techniques, O-GlcNAc modified proteins were enriched from HEK293T cells and subsequently characterized using the LTQ Orbitrap Velos ETD (Thermo Fisher Scientific) mass spectrometer.
21740066	0	3	theme	O-GlcNAc	89:96	arg1	modification					98:109	protein O-GlcNAc modification site assignment	81:125	protein O-GlcNAc modification site assignment	81:125	Combining high-energy C-trap dissociation and electron transfer dissociation for protein O-GlcNAc modification site assignment.
21740066	3	4	theme	combination	773:783	arg1	advantage					681:689	advantage	681:689	advantage of the recently characterized O-GlcNAc-specific IgG monoclonal antibodies and the combination of HCD	681:790	By taking advantage of the recently characterized O-GlcNAc-specific IgG monoclonal antibodies and the combination of HCD and ETD fragmentation techniques, O-GlcNAc modified proteins were enriched from HEK293T cells and subsequently characterized using the LTQ Orbitrap Velos ETD (Thermo Fisher Scientific) mass spectrometer.
21740066	5	5	theme	ETD	1231:1233	arg1	fragmentation					1235:1247	ETD fragmentation	1231:1247	ETD fragmentation	1231:1247	Realizing HCD triggered ETD fragmentation on a linear ion trap/Orbitrap platform for more in-depth analysis and application of this technique to other post-translationally modified proteins are currently underway.
21740066	5	6	theme	modified	1379:1386	arg1	proteins					1388:1395	other post-translationally modified proteins	1352:1395	other post-translationally modified proteins	1352:1395	Realizing HCD triggered ETD fragmentation on a linear ion trap/Orbitrap platform for more in-depth analysis and application of this technique to other post-translationally modified proteins are currently underway.
21740066	3	7	theme	Velos	940:944	arg1	spectrometer					982:993	the LTQ Orbitrap Velos ETD (Thermo Fisher Scientific) mass spectrometer	923:993	the LTQ Orbitrap Velos ETD (Thermo Fisher Scientific) mass spectrometer	923:993	By taking advantage of the recently characterized O-GlcNAc-specific IgG monoclonal antibodies and the combination of HCD and ETD fragmentation techniques, O-GlcNAc modified proteins were enriched from HEK293T cells and subsequently characterized using the LTQ Orbitrap Velos ETD (Thermo Fisher Scientific) mass spectrometer.
21740066	4	8	theme	O-GlcNAc	1025:1032	arg1	modification					1034:1045	O-GlcNAc modification	1025:1045	O-GlcNAc modification	1025:1045	In our data set, 83 sites of O-GlcNAc modification are reported with high confidence confirming that the HCD/ETD combined approach is amenable to the detection and site assignment of O-GlcNAc modified peptides.
21740066	4	9	dep	detection	1146:1154	arg1	the					1142:1144	the	1142:1144	the	1142:1144	In our data set, 83 sites of O-GlcNAc modification are reported with high confidence confirming that the HCD/ETD combined approach is amenable to the detection and site assignment of O-GlcNAc modified peptides.
21740066	1	10	theme	modification	311:322	arg1	modification					311:322	modification	311:322	modification	311:322	Mass spectrometry-based studies of proteins that are post-translationally modified by O-linked β-N-acetylglucosamine (O-GlcNAc) are challenged in effectively identifying the sites of modification while simultaneously sequencing the peptides.
21740066	1	10	theme	modification	311:322	arg1	sites					302:306	the sites	298:306	the sites of modification	298:322	Mass spectrometry-based studies of proteins that are post-translationally modified by O-linked β-N-acetylglucosamine (O-GlcNAc) are challenged in effectively identifying the sites of modification while simultaneously sequencing the peptides.
21740066	0	11	theme	site	111:114	arg1	assignment					116:125	site assignment	111:125	protein O-GlcNAc modification site assignment	81:125	Combining high-energy C-trap dissociation and electron transfer dissociation for protein O-GlcNAc modification site assignment.
21740066	2	12	theme	site	654:657	arg1	assignment					659:668	accurate site assignment	645:668	accurate site assignment	645:668	Here we tested the hypothesis that a combination of high-energy C-trap dissociation (HCD) and electron transfer dissociation (ETD) could specifically target the O-GlcNAc modified peptides and elucidate the amino acid sequence while preserving the attached GlcNAc residue for accurate site assignment.
21740066	3	13	theme	LTQ	927:929	arg1	spectrometer					982:993	the LTQ Orbitrap Velos ETD (Thermo Fisher Scientific) mass spectrometer	923:993	the LTQ Orbitrap Velos ETD (Thermo Fisher Scientific) mass spectrometer	923:993	By taking advantage of the recently characterized O-GlcNAc-specific IgG monoclonal antibodies and the combination of HCD and ETD fragmentation techniques, O-GlcNAc modified proteins were enriched from HEK293T cells and subsequently characterized using the LTQ Orbitrap Velos ETD (Thermo Fisher Scientific) mass spectrometer.
21740066	2	14	theme	amino	576:580	arg1	sequence					587:594	the amino acid sequence	572:594	the amino acid sequence	572:594	Here we tested the hypothesis that a combination of high-energy C-trap dissociation (HCD) and electron transfer dissociation (ETD) could specifically target the O-GlcNAc modified peptides and elucidate the amino acid sequence while preserving the attached GlcNAc residue for accurate site assignment.
21740066	5	15	theme	other	1352:1356	arg1	proteins					1388:1395	other post-translationally modified proteins	1352:1395	other post-translationally modified proteins	1352:1395	Realizing HCD triggered ETD fragmentation on a linear ion trap/Orbitrap platform for more in-depth analysis and application of this technique to other post-translationally modified proteins are currently underway.
21740066	6	16	theme	glycosylated	1629:1640	arg1	polypeptides					1642:1653	the glycosylated polypeptides	1625:1653	the glycosylated polypeptides	1625:1653	Furthermore, this report illustrates that the O-GlcNAc transferase appears to demonstrate promiscuity with regards to the hydroxyl-containing amino acid modified in short stretches of primary sequence of the glycosylated polypeptides.
21740066	4	17	theme	modification	1034:1045	arg1	modification					1034:1045	O-GlcNAc modification	1025:1045	O-GlcNAc modification	1025:1045	In our data set, 83 sites of O-GlcNAc modification are reported with high confidence confirming that the HCD/ETD combined approach is amenable to the detection and site assignment of O-GlcNAc modified peptides.
21740066	4	17	theme	modification	1034:1045	arg1	sites					1016:1020	83 sites	1013:1020	83 sites of O-GlcNAc modification	1013:1045	In our data set, 83 sites of O-GlcNAc modification are reported with high confidence confirming that the HCD/ETD combined approach is amenable to the detection and site assignment of O-GlcNAc modified peptides.
21740066	5	18	theme	in-depth	1297:1304	arg1	analysis					1306:1313	more in-depth analysis	1292:1313	more in-depth analysis	1292:1313	Realizing HCD triggered ETD fragmentation on a linear ion trap/Orbitrap platform for more in-depth analysis and application of this technique to other post-translationally modified proteins are currently underway.
21740066	6	19	theme	short	1586:1590	arg1	stretches					1592:1600	short stretches	1586:1600	short stretches of primary sequence of the glycosylated polypeptides	1586:1653	Furthermore, this report illustrates that the O-GlcNAc transferase appears to demonstrate promiscuity with regards to the hydroxyl-containing amino acid modified in short stretches of primary sequence of the glycosylated polypeptides.
21740066	6	20	theme	O-GlcNAc	1467:1474	arg1	transferase					1476:1486	the O-GlcNAc transferase	1463:1486	the O-GlcNAc transferase	1463:1486	Furthermore, this report illustrates that the O-GlcNAc transferase appears to demonstrate promiscuity with regards to the hydroxyl-containing amino acid modified in short stretches of primary sequence of the glycosylated polypeptides.
21740066	1	21	theme	O-linked	214:221	arg1	β-N-acetylglucosamine					223:243	O-linked β-N-acetylglucosamine	214:243	O-linked β-N-acetylglucosamine (O-GlcNAc)	214:254	Mass spectrometry-based studies of proteins that are post-translationally modified by O-linked β-N-acetylglucosamine (O-GlcNAc) are challenged in effectively identifying the sites of modification while simultaneously sequencing the peptides.
21740066	1	21	theme	O-linked	214:221	arg1	O-GlcNAc					246:253	O-GlcNAc	246:253	O-GlcNAc	246:253	Mass spectrometry-based studies of proteins that are post-translationally modified by O-linked β-N-acetylglucosamine (O-GlcNAc) are challenged in effectively identifying the sites of modification while simultaneously sequencing the peptides.
21740066	0	22	theme	high-energy	10:20	arg1	dissociation					29:40	high-energy C-trap dissociation	10:40	high-energy C-trap dissociation	10:40	Combining high-energy C-trap dissociation and electron transfer dissociation for protein O-GlcNAc modification site assignment.
21740066	2	23	theme	modified	540:547	arg1	peptides					549:556	the O-GlcNAc modified peptides	527:556	the O-GlcNAc modified peptides	527:556	Here we tested the hypothesis that a combination of high-energy C-trap dissociation (HCD) and electron transfer dissociation (ETD) could specifically target the O-GlcNAc modified peptides and elucidate the amino acid sequence while preserving the attached GlcNAc residue for accurate site assignment.
21740066	0	24	dep	modification	98:109	arg1	assignment					116:125	site assignment	111:125	protein O-GlcNAc modification site assignment	81:125	Combining high-energy C-trap dissociation and electron transfer dissociation for protein O-GlcNAc modification site assignment.
21740066	6	25	theme	hydroxyl-containing	1543:1561	arg1	acid					1569:1572	the hydroxyl-containing amino acid	1539:1572	the hydroxyl-containing amino acid modified in short stretches of primary sequence of the glycosylated polypeptides	1539:1653	Furthermore, this report illustrates that the O-GlcNAc transferase appears to demonstrate promiscuity with regards to the hydroxyl-containing amino acid modified in short stretches of primary sequence of the glycosylated polypeptides.
21740066	4	26	theme	combined	1109:1116	arg1	approach					1118:1125	the HCD/ETD combined approach	1097:1125	the HCD/ETD combined approach	1097:1125	In our data set, 83 sites of O-GlcNAc modification are reported with high confidence confirming that the HCD/ETD combined approach is amenable to the detection and site assignment of O-GlcNAc modified peptides.
21740066	4	26	theme	combined	1109:1116	arg1	amenable					1130:1137	amenable	1130:1137	amenable	1130:1137	In our data set, 83 sites of O-GlcNAc modification are reported with high confidence confirming that the HCD/ETD combined approach is amenable to the detection and site assignment of O-GlcNAc modified peptides.
21740066	5	27	theme	trap/Orbitrap	1265:1277	arg1	platform					1279:1286	a linear ion trap/Orbitrap platform	1252:1286	a linear ion trap/Orbitrap platform for more in-depth analysis and application of this technique to other post-translationally modified proteins	1252:1395	Realizing HCD triggered ETD fragmentation on a linear ion trap/Orbitrap platform for more in-depth analysis and application of this technique to other post-translationally modified proteins are currently underway.
21740066	1	28	link	O-linked	214:221	arg1	β-N-acetylglucosamine					223:243	O-linked β-N-acetylglucosamine	214:243	O-linked β-N-acetylglucosamine (O-GlcNAc)	214:254	Mass spectrometry-based studies of proteins that are post-translationally modified by O-linked β-N-acetylglucosamine (O-GlcNAc) are challenged in effectively identifying the sites of modification while simultaneously sequencing the peptides.
21740066	1	28	link	O-linked	214:221	arg1	O-GlcNAc					246:253	O-GlcNAc	246:253	O-GlcNAc	246:253	Mass spectrometry-based studies of proteins that are post-translationally modified by O-linked β-N-acetylglucosamine (O-GlcNAc) are challenged in effectively identifying the sites of modification while simultaneously sequencing the peptides.
21740066	6	29	theme	primary	1605:1611	arg1	sequence					1613:1620	primary sequence	1605:1620	primary sequence of the glycosylated polypeptides	1605:1653	Furthermore, this report illustrates that the O-GlcNAc transferase appears to demonstrate promiscuity with regards to the hydroxyl-containing amino acid modified in short stretches of primary sequence of the glycosylated polypeptides.
21740066	4	30	theme	peptides	1197:1204	arg1	detection					1146:1154	detection	1146:1154	detection	1146:1154	In our data set, 83 sites of O-GlcNAc modification are reported with high confidence confirming that the HCD/ETD combined approach is amenable to the detection and site assignment of O-GlcNAc modified peptides.
21740066	4	30	theme	peptides	1197:1204	arg1	assignment					1165:1174	site assignment	1160:1174	site assignment	1160:1174	In our data set, 83 sites of O-GlcNAc modification are reported with high confidence confirming that the HCD/ETD combined approach is amenable to the detection and site assignment of O-GlcNAc modified peptides.
21740066	2	31	theme	dissociation	441:452	arg1	combination					407:417	a combination	405:417	a combination of high-energy C-trap dissociation (HCD) and electron transfer dissociation (ETD)	405:499	Here we tested the hypothesis that a combination of high-energy C-trap dissociation (HCD) and electron transfer dissociation (ETD) could specifically target the O-GlcNAc modified peptides and elucidate the amino acid sequence while preserving the attached GlcNAc residue for accurate site assignment.
21740066	2	32	theme	attached	617:624	arg1	residue					633:639	the attached GlcNAc residue	613:639	the attached GlcNAc residue for accurate site assignment	613:668	Here we tested the hypothesis that a combination of high-energy C-trap dissociation (HCD) and electron transfer dissociation (ETD) could specifically target the O-GlcNAc modified peptides and elucidate the amino acid sequence while preserving the attached GlcNAc residue for accurate site assignment.
21740066	3	33	dep	spectrometer	982:993	arg1	Fisher					958:963	Fisher	958:963	Fisher	958:963	By taking advantage of the recently characterized O-GlcNAc-specific IgG monoclonal antibodies and the combination of HCD and ETD fragmentation techniques, O-GlcNAc modified proteins were enriched from HEK293T cells and subsequently characterized using the LTQ Orbitrap Velos ETD (Thermo Fisher Scientific) mass spectrometer.
21740066	4	34	theme	modified	1188:1195	arg1	peptides					1197:1204	O-GlcNAc modified peptides	1179:1204	O-GlcNAc modified peptides	1179:1204	In our data set, 83 sites of O-GlcNAc modification are reported with high confidence confirming that the HCD/ETD combined approach is amenable to the detection and site assignment of O-GlcNAc modified peptides.
21740066	1	35	mod	modified	202:209	arg3	β-N-acetylglucosamine					223:243	O-linked β-N-acetylglucosamine	214:243	O-linked β-N-acetylglucosamine (O-GlcNAc)	214:254	Mass spectrometry-based studies of proteins that are post-translationally modified by O-linked β-N-acetylglucosamine (O-GlcNAc) are challenged in effectively identifying the sites of modification while simultaneously sequencing the peptides.
21740066	1	35	mod	modified	202:209	arg1	proteins					163:170	proteins	163:170	proteins that are post-translationally modified by O-linked β-N-acetylglucosamine (O-GlcNAc)	163:254	Mass spectrometry-based studies of proteins that are post-translationally modified by O-linked β-N-acetylglucosamine (O-GlcNAc) are challenged in effectively identifying the sites of modification while simultaneously sequencing the peptides.
21740066	1	35	mod	modified	202:209	arg3	O-GlcNAc					246:253	O-GlcNAc	246:253	O-GlcNAc	246:253	Mass spectrometry-based studies of proteins that are post-translationally modified by O-linked β-N-acetylglucosamine (O-GlcNAc) are challenged in effectively identifying the sites of modification while simultaneously sequencing the peptides.
21740066	0	36	theme	C-trap	22:27	arg1	dissociation					29:40	high-energy C-trap dissociation	10:40	high-energy C-trap dissociation	10:40	Combining high-energy C-trap dissociation and electron transfer dissociation for protein O-GlcNAc modification site assignment.
21740066	3	37	theme	O-GlcNAc-specific	721:737	arg1	antibodies					754:763	the recently characterized O-GlcNAc-specific IgG monoclonal antibodies	694:763	the recently characterized O-GlcNAc-specific IgG monoclonal antibodies	694:763	By taking advantage of the recently characterized O-GlcNAc-specific IgG monoclonal antibodies and the combination of HCD and ETD fragmentation techniques, O-GlcNAc modified proteins were enriched from HEK293T cells and subsequently characterized using the LTQ Orbitrap Velos ETD (Thermo Fisher Scientific) mass spectrometer.
21740066	1	38	theme	Mass	128:131	arg1	studies					152:158	Mass spectrometry-based studies	128:158	Mass spectrometry-based studies of proteins that are post-translationally modified by O-linked β-N-acetylglucosamine (O-GlcNAc)	128:254	Mass spectrometry-based studies of proteins that are post-translationally modified by O-linked β-N-acetylglucosamine (O-GlcNAc) are challenged in effectively identifying the sites of modification while simultaneously sequencing the peptides.
21740066	2	39	theme	transfer	473:480	arg1	ETD					496:498	ETD	496:498	ETD	496:498	Here we tested the hypothesis that a combination of high-energy C-trap dissociation (HCD) and electron transfer dissociation (ETD) could specifically target the O-GlcNAc modified peptides and elucidate the amino acid sequence while preserving the attached GlcNAc residue for accurate site assignment.
21740066	2	39	theme	transfer	473:480	arg1	dissociation					482:493	electron transfer dissociation	464:493	electron transfer dissociation (ETD)	464:499	Here we tested the hypothesis that a combination of high-energy C-trap dissociation (HCD) and electron transfer dissociation (ETD) could specifically target the O-GlcNAc modified peptides and elucidate the amino acid sequence while preserving the attached GlcNAc residue for accurate site assignment.
21740066	0	40	theme	electron	46:53	arg1	dissociation					64:75	electron transfer dissociation	46:75	electron transfer dissociation	46:75	Combining high-energy C-trap dissociation and electron transfer dissociation for protein O-GlcNAc modification site assignment.
21740066	3	41	theme	modified	835:842	arg1	proteins					844:851	O-GlcNAc modified proteins	826:851	O-GlcNAc modified proteins	826:851	By taking advantage of the recently characterized O-GlcNAc-specific IgG monoclonal antibodies and the combination of HCD and ETD fragmentation techniques, O-GlcNAc modified proteins were enriched from HEK293T cells and subsequently characterized using the LTQ Orbitrap Velos ETD (Thermo Fisher Scientific) mass spectrometer.
21740066	3	42	theme	IgG	739:741	arg1	antibodies					754:763	the recently characterized O-GlcNAc-specific IgG monoclonal antibodies	694:763	the recently characterized O-GlcNAc-specific IgG monoclonal antibodies	694:763	By taking advantage of the recently characterized O-GlcNAc-specific IgG monoclonal antibodies and the combination of HCD and ETD fragmentation techniques, O-GlcNAc modified proteins were enriched from HEK293T cells and subsequently characterized using the LTQ Orbitrap Velos ETD (Thermo Fisher Scientific) mass spectrometer.
21740066	2	43	theme	electron	464:471	arg1	ETD					496:498	ETD	496:498	ETD	496:498	Here we tested the hypothesis that a combination of high-energy C-trap dissociation (HCD) and electron transfer dissociation (ETD) could specifically target the O-GlcNAc modified peptides and elucidate the amino acid sequence while preserving the attached GlcNAc residue for accurate site assignment.
21740066	2	43	theme	electron	464:471	arg1	dissociation					482:493	electron transfer dissociation	464:493	electron transfer dissociation (ETD)	464:499	Here we tested the hypothesis that a combination of high-energy C-trap dissociation (HCD) and electron transfer dissociation (ETD) could specifically target the O-GlcNAc modified peptides and elucidate the amino acid sequence while preserving the attached GlcNAc residue for accurate site assignment.
21740066	6	44	theme	amino	1563:1567	arg1	acid					1569:1572	the hydroxyl-containing amino acid	1539:1572	the hydroxyl-containing amino acid modified in short stretches of primary sequence of the glycosylated polypeptides	1539:1653	Furthermore, this report illustrates that the O-GlcNAc transferase appears to demonstrate promiscuity with regards to the hydroxyl-containing amino acid modified in short stretches of primary sequence of the glycosylated polypeptides.
21740066	3	45	theme	HEK293T	872:878	arg1	cells					880:884	HEK293T cells	872:884	HEK293T cells	872:884	By taking advantage of the recently characterized O-GlcNAc-specific IgG monoclonal antibodies and the combination of HCD and ETD fragmentation techniques, O-GlcNAc modified proteins were enriched from HEK293T cells and subsequently characterized using the LTQ Orbitrap Velos ETD (Thermo Fisher Scientific) mass spectrometer.
21740066	5	46	theme	more	1292:1295	arg1	analysis					1306:1313	more in-depth analysis	1292:1313	more in-depth analysis	1292:1313	Realizing HCD triggered ETD fragmentation on a linear ion trap/Orbitrap platform for more in-depth analysis and application of this technique to other post-translationally modified proteins are currently underway.
21740066	4	47	theme	HCD/ETD	1101:1107	arg1	approach					1118:1125	the HCD/ETD combined approach	1097:1125	the HCD/ETD combined approach	1097:1125	In our data set, 83 sites of O-GlcNAc modification are reported with high confidence confirming that the HCD/ETD combined approach is amenable to the detection and site assignment of O-GlcNAc modified peptides.
21740066	4	47	theme	HCD/ETD	1101:1107	arg1	amenable					1130:1137	amenable	1130:1137	amenable	1130:1137	In our data set, 83 sites of O-GlcNAc modification are reported with high confidence confirming that the HCD/ETD combined approach is amenable to the detection and site assignment of O-GlcNAc modified peptides.
21740066	2	48	theme	accurate	645:652	arg1	assignment					659:668	accurate site assignment	645:668	accurate site assignment	645:668	Here we tested the hypothesis that a combination of high-energy C-trap dissociation (HCD) and electron transfer dissociation (ETD) could specifically target the O-GlcNAc modified peptides and elucidate the amino acid sequence while preserving the attached GlcNAc residue for accurate site assignment.
21740066	3	49	theme	characterized	707:719	arg1	antibodies					754:763	the recently characterized O-GlcNAc-specific IgG monoclonal antibodies	694:763	the recently characterized O-GlcNAc-specific IgG monoclonal antibodies	694:763	By taking advantage of the recently characterized O-GlcNAc-specific IgG monoclonal antibodies and the combination of HCD and ETD fragmentation techniques, O-GlcNAc modified proteins were enriched from HEK293T cells and subsequently characterized using the LTQ Orbitrap Velos ETD (Thermo Fisher Scientific) mass spectrometer.
21740066	6	50	with	promiscuity	1511:1521	arg1	regards					1528:1534	regards	1528:1534	regards	1528:1534	Furthermore, this report illustrates that the O-GlcNAc transferase appears to demonstrate promiscuity with regards to the hydroxyl-containing amino acid modified in short stretches of primary sequence of the glycosylated polypeptides.
21740066	1	51	theme	spectrometry-based	133:150	arg1	studies					152:158	Mass spectrometry-based studies	128:158	Mass spectrometry-based studies of proteins that are post-translationally modified by O-linked β-N-acetylglucosamine (O-GlcNAc)	128:254	Mass spectrometry-based studies of proteins that are post-translationally modified by O-linked β-N-acetylglucosamine (O-GlcNAc) are challenged in effectively identifying the sites of modification while simultaneously sequencing the peptides.
21740066	0	52	theme	transfer	55:62	arg1	dissociation					64:75	electron transfer dissociation	46:75	electron transfer dissociation	46:75	Combining high-energy C-trap dissociation and electron transfer dissociation for protein O-GlcNAc modification site assignment.
21740066	5	53	theme	linear	1254:1259	arg1	platform					1279:1286	a linear ion trap/Orbitrap platform	1252:1286	a linear ion trap/Orbitrap platform for more in-depth analysis and application of this technique to other post-translationally modified proteins	1252:1395	Realizing HCD triggered ETD fragmentation on a linear ion trap/Orbitrap platform for more in-depth analysis and application of this technique to other post-translationally modified proteins are currently underway.
21740066	5	54	theme	Realizing	1207:1215	arg1	HCD					1217:1219	Realizing HCD	1207:1219	Realizing HCD triggered ETD fragmentation on a linear ion trap/Orbitrap platform for more in-depth analysis and application of this technique to other post-translationally modified proteins	1207:1395	Realizing HCD triggered ETD fragmentation on a linear ion trap/Orbitrap platform for more in-depth analysis and application of this technique to other post-translationally modified proteins are currently underway.
21740066	5	55	theme	ion	1261:1263	arg1	platform					1279:1286	a linear ion trap/Orbitrap platform	1252:1286	a linear ion trap/Orbitrap platform for more in-depth analysis and application of this technique to other post-translationally modified proteins	1252:1395	Realizing HCD triggered ETD fragmentation on a linear ion trap/Orbitrap platform for more in-depth analysis and application of this technique to other post-translationally modified proteins are currently underway.
21740066	4	56	theme	data	1003:1006	arg1	set					1008:1010	our data set	999:1010	our data set	999:1010	In our data set, 83 sites of O-GlcNAc modification are reported with high confidence confirming that the HCD/ETD combined approach is amenable to the detection and site assignment of O-GlcNAc modified peptides.
21740066	4	57	theme	site	1160:1163	arg1	assignment					1165:1174	site assignment	1160:1174	site assignment	1160:1174	In our data set, 83 sites of O-GlcNAc modification are reported with high confidence confirming that the HCD/ETD combined approach is amenable to the detection and site assignment of O-GlcNAc modified peptides.
21740066	4	58	theme	high	1065:1068	arg1	confidence					1070:1079	high confidence	1065:1079	high confidence confirming that the HCD/ETD combined approach is amenable to the detection and site assignment of O-GlcNAc modified peptides	1065:1204	In our data set, 83 sites of O-GlcNAc modification are reported with high confidence confirming that the HCD/ETD combined approach is amenable to the detection and site assignment of O-GlcNAc modified peptides.
21740066	2	59	theme	GlcNAc	626:631	arg1	residue					633:639	the attached GlcNAc residue	613:639	the attached GlcNAc residue for accurate site assignment	613:668	Here we tested the hypothesis that a combination of high-energy C-trap dissociation (HCD) and electron transfer dissociation (ETD) could specifically target the O-GlcNAc modified peptides and elucidate the amino acid sequence while preserving the attached GlcNAc residue for accurate site assignment.
21740066	3	60	theme	monoclonal	743:752	arg1	antibodies					754:763	the recently characterized O-GlcNAc-specific IgG monoclonal antibodies	694:763	the recently characterized O-GlcNAc-specific IgG monoclonal antibodies	694:763	By taking advantage of the recently characterized O-GlcNAc-specific IgG monoclonal antibodies and the combination of HCD and ETD fragmentation techniques, O-GlcNAc modified proteins were enriched from HEK293T cells and subsequently characterized using the LTQ Orbitrap Velos ETD (Thermo Fisher Scientific) mass spectrometer.
21740066	1	61	theme	proteins	163:170	arg1	studies					152:158	Mass spectrometry-based studies	128:158	Mass spectrometry-based studies of proteins that are post-translationally modified by O-linked β-N-acetylglucosamine (O-GlcNAc)	128:254	Mass spectrometry-based studies of proteins that are post-translationally modified by O-linked β-N-acetylglucosamine (O-GlcNAc) are challenged in effectively identifying the sites of modification while simultaneously sequencing the peptides.
21740066	3	62	theme	ETD	946:948	arg1	spectrometer					982:993	the LTQ Orbitrap Velos ETD (Thermo Fisher Scientific) mass spectrometer	923:993	the LTQ Orbitrap Velos ETD (Thermo Fisher Scientific) mass spectrometer	923:993	By taking advantage of the recently characterized O-GlcNAc-specific IgG monoclonal antibodies and the combination of HCD and ETD fragmentation techniques, O-GlcNAc modified proteins were enriched from HEK293T cells and subsequently characterized using the LTQ Orbitrap Velos ETD (Thermo Fisher Scientific) mass spectrometer.
21740066	0	63	theme	protein	81:87	arg1	modification					98:109	protein O-GlcNAc modification site assignment	81:125	protein O-GlcNAc modification site assignment	81:125	Combining high-energy C-trap dissociation and electron transfer dissociation for protein O-GlcNAc modification site assignment.
21740066	3	64	theme	antibodies	754:763	arg1	advantage					681:689	advantage	681:689	advantage of the recently characterized O-GlcNAc-specific IgG monoclonal antibodies and the combination of HCD	681:790	By taking advantage of the recently characterized O-GlcNAc-specific IgG monoclonal antibodies and the combination of HCD and ETD fragmentation techniques, O-GlcNAc modified proteins were enriched from HEK293T cells and subsequently characterized using the LTQ Orbitrap Velos ETD (Thermo Fisher Scientific) mass spectrometer.
21740066	2	65	theme	dissociation	482:493	arg1	combination					407:417	a combination	405:417	a combination of high-energy C-trap dissociation (HCD) and electron transfer dissociation (ETD)	405:499	Here we tested the hypothesis that a combination of high-energy C-trap dissociation (HCD) and electron transfer dissociation (ETD) could specifically target the O-GlcNAc modified peptides and elucidate the amino acid sequence while preserving the attached GlcNAc residue for accurate site assignment.
21740066	2	66	theme	C-trap	434:439	arg1	HCD					455:457	HCD	455:457	HCD	455:457	Here we tested the hypothesis that a combination of high-energy C-trap dissociation (HCD) and electron transfer dissociation (ETD) could specifically target the O-GlcNAc modified peptides and elucidate the amino acid sequence while preserving the attached GlcNAc residue for accurate site assignment.
21740066	2	66	theme	C-trap	434:439	arg1	dissociation					441:452	high-energy C-trap dissociation	422:452	high-energy C-trap dissociation (HCD)	422:458	Here we tested the hypothesis that a combination of high-energy C-trap dissociation (HCD) and electron transfer dissociation (ETD) could specifically target the O-GlcNAc modified peptides and elucidate the amino acid sequence while preserving the attached GlcNAc residue for accurate site assignment.
21740066	6	67	theme	polypeptides	1642:1653	arg1	sequence					1613:1620	primary sequence	1605:1620	primary sequence of the glycosylated polypeptides	1605:1653	Furthermore, this report illustrates that the O-GlcNAc transferase appears to demonstrate promiscuity with regards to the hydroxyl-containing amino acid modified in short stretches of primary sequence of the glycosylated polypeptides.
21740066	5	68	theme	technique	1339:1347	arg1	application					1319:1329	application	1319:1329	application of this technique to other post-translationally modified proteins	1319:1395	Realizing HCD triggered ETD fragmentation on a linear ion trap/Orbitrap platform for more in-depth analysis and application of this technique to other post-translationally modified proteins are currently underway.
21740066	5	68	theme	technique	1339:1347	arg1	analysis					1306:1313	more in-depth analysis	1292:1313	more in-depth analysis	1292:1313	Realizing HCD triggered ETD fragmentation on a linear ion trap/Orbitrap platform for more in-depth analysis and application of this technique to other post-translationally modified proteins are currently underway.
21740066	6	69	gly	glycosylated	1629:1640	arg1	polypeptides					1642:1653	the glycosylated polypeptides	1625:1653	the glycosylated polypeptides	1625:1653	Furthermore, this report illustrates that the O-GlcNAc transferase appears to demonstrate promiscuity with regards to the hydroxyl-containing amino acid modified in short stretches of primary sequence of the glycosylated polypeptides.
21740066	3	70	theme	HCD	788:790	arg1	antibodies					754:763	the recently characterized O-GlcNAc-specific IgG monoclonal antibodies	694:763	the recently characterized O-GlcNAc-specific IgG monoclonal antibodies	694:763	By taking advantage of the recently characterized O-GlcNAc-specific IgG monoclonal antibodies and the combination of HCD and ETD fragmentation techniques, O-GlcNAc modified proteins were enriched from HEK293T cells and subsequently characterized using the LTQ Orbitrap Velos ETD (Thermo Fisher Scientific) mass spectrometer.
21740066	3	70	theme	HCD	788:790	arg1	combination					773:783	the combination	769:783	the combination of HCD	769:790	By taking advantage of the recently characterized O-GlcNAc-specific IgG monoclonal antibodies and the combination of HCD and ETD fragmentation techniques, O-GlcNAc modified proteins were enriched from HEK293T cells and subsequently characterized using the LTQ Orbitrap Velos ETD (Thermo Fisher Scientific) mass spectrometer.
21740066	2	71	theme	high-energy	422:432	arg1	HCD					455:457	HCD	455:457	HCD	455:457	Here we tested the hypothesis that a combination of high-energy C-trap dissociation (HCD) and electron transfer dissociation (ETD) could specifically target the O-GlcNAc modified peptides and elucidate the amino acid sequence while preserving the attached GlcNAc residue for accurate site assignment.
21740066	2	71	theme	high-energy	422:432	arg1	dissociation					441:452	high-energy C-trap dissociation	422:452	high-energy C-trap dissociation (HCD)	422:458	Here we tested the hypothesis that a combination of high-energy C-trap dissociation (HCD) and electron transfer dissociation (ETD) could specifically target the O-GlcNAc modified peptides and elucidate the amino acid sequence while preserving the attached GlcNAc residue for accurate site assignment.
21740066	3	72	theme	mass	977:980	arg1	spectrometer					982:993	the LTQ Orbitrap Velos ETD (Thermo Fisher Scientific) mass spectrometer	923:993	the LTQ Orbitrap Velos ETD (Thermo Fisher Scientific) mass spectrometer	923:993	By taking advantage of the recently characterized O-GlcNAc-specific IgG monoclonal antibodies and the combination of HCD and ETD fragmentation techniques, O-GlcNAc modified proteins were enriched from HEK293T cells and subsequently characterized using the LTQ Orbitrap Velos ETD (Thermo Fisher Scientific) mass spectrometer.
21740066	2	73	theme	acid	582:585	arg1	sequence					587:594	the amino acid sequence	572:594	the amino acid sequence	572:594	Here we tested the hypothesis that a combination of high-energy C-trap dissociation (HCD) and electron transfer dissociation (ETD) could specifically target the O-GlcNAc modified peptides and elucidate the amino acid sequence while preserving the attached GlcNAc residue for accurate site assignment.
12565836	0	0	theme	formyl	76:81	arg1	receptor					91:98	the human formyl peptide receptor	66:98	the human formyl peptide receptor	66:98	Critical role of N-terminal N-glycosylation for proper folding of the human formyl peptide receptor.
12565836	3	1	theme	FPR	518:520	arg1	function					522:529	FPR function	518:529	FPR function	518:529	The aim of our study was to analyze the role of N-glycosylation in FPR function.
12565836	5	2	theme	GTPgammaS	721:729	arg1	binding					731:737	GTPgammaS binding	721:737	GTPgammaS binding	721:737	However, in terms of high-affinity agonist binding, kinetics of GTPgammaS binding, number of G(i)-proteins activated, and constitutive activity, non-glycosylated FPR was much less active than native FPR.
12565836	2	3	theme	agonist	365:371	arg1	effects					343:349	strong inhibitory effects	325:349	strong inhibitory effects of an inverse agonist and Na(+) on basal guanosine 5(')-O-(3-thiotriphosphate) (GTPgammaS) binding	325:448	The FPR expressed with G(i)alpha(2)beta(1)gamma(2) in Sf9 insect cells exhibits high constitutive activity as assessed by strong inhibitory effects of an inverse agonist and Na(+) on basal guanosine 5(')-O-(3-thiotriphosphate) (GTPgammaS) binding.
12565836	1	4	gly	N-glycosylated	144:157	arg1	FPR					136:138	FPR	136:138	FPR	136:138	The human formyl peptide receptor (FPR) is N-glycosylated and activates phagocytes via G(i)-proteins.
12565836	1	4	gly	N-glycosylated	144:157	arg1	N-glycosylated					144:157	N-glycosylated	144:157	N-glycosylated	144:157	The human formyl peptide receptor (FPR) is N-glycosylated and activates phagocytes via G(i)-proteins.
12565836	1	4	gly	N-glycosylated	144:157	arg1	receptor					126:133	The human formyl peptide receptor	101:133	The human formyl peptide receptor (FPR)	101:139	The human formyl peptide receptor (FPR) is N-glycosylated and activates phagocytes via G(i)-proteins.
12565836	5	5	theme	binding	731:737	arg1	kinetics					709:716	kinetics	709:716	kinetics of GTPgammaS binding, number of G(i)-proteins activated, and constitutive activity, non-glycosylated FPR	709:821	However, in terms of high-affinity agonist binding, kinetics of GTPgammaS binding, number of G(i)-proteins activated, and constitutive activity, non-glycosylated FPR was much less active than native FPR.
12565836	0	6	theme	receptor	91:98	arg1	folding					55:61	proper folding	48:61	proper folding of the human formyl peptide receptor	48:98	Critical role of N-terminal N-glycosylation for proper folding of the human formyl peptide receptor.
12565836	3	7	theme	N-glycosylation	499:513	arg1	role					491:494	the role	487:494	the role of N-glycosylation in FPR function	487:529	The aim of our study was to analyze the role of N-glycosylation in FPR function.
12565836	2	8	theme	alpha	230:234	arg1	gamma					245:249	G(i)alpha(2)beta(1)gamma(2)	226:252	G(i)alpha(2)beta(1)gamma(2) in Sf9 insect cells	226:272	The FPR expressed with G(i)alpha(2)beta(1)gamma(2) in Sf9 insect cells exhibits high constitutive activity as assessed by strong inhibitory effects of an inverse agonist and Na(+) on basal guanosine 5(')-O-(3-thiotriphosphate) (GTPgammaS) binding.
12565836	5	9	theme	-proteins	754:762	arg1	number					740:745	number	740:745	number of G(i)-proteins activated	740:772	However, in terms of high-affinity agonist binding, kinetics of GTPgammaS binding, number of G(i)-proteins activated, and constitutive activity, non-glycosylated FPR was much less active than native FPR.
12565836	5	9	theme	-proteins	754:762	arg1	activity					792:799	constitutive activity	779:799	constitutive activity	779:799	However, in terms of high-affinity agonist binding, kinetics of GTPgammaS binding, number of G(i)-proteins activated, and constitutive activity, non-glycosylated FPR was much less active than native FPR.
12565836	5	9	theme	-proteins	754:762	arg1	binding					731:737	GTPgammaS binding	721:737	GTPgammaS binding	721:737	However, in terms of high-affinity agonist binding, kinetics of GTPgammaS binding, number of G(i)-proteins activated, and constitutive activity, non-glycosylated FPR was much less active than native FPR.
12565836	5	9	theme	-proteins	754:762	arg1	FPR					819:821	non-glycosylated FPR	802:821	non-glycosylated FPR	802:821	However, in terms of high-affinity agonist binding, kinetics of GTPgammaS binding, number of G(i)-proteins activated, and constitutive activity, non-glycosylated FPR was much less active than native FPR.
12565836	0	10	theme	peptide	83:89	arg1	receptor					91:98	the human formyl peptide receptor	66:98	the human formyl peptide receptor	66:98	Critical role of N-terminal N-glycosylation for proper folding of the human formyl peptide receptor.
12565836	2	11	from	gamma	245:249	arg1	cells					268:272	Sf9 insect cells	257:272	Sf9 insect cells	257:272	The FPR expressed with G(i)alpha(2)beta(1)gamma(2) in Sf9 insect cells exhibits high constitutive activity as assessed by strong inhibitory effects of an inverse agonist and Na(+) on basal guanosine 5(')-O-(3-thiotriphosphate) (GTPgammaS) binding.
12565836	5	12	theme	activity	792:799	arg1	kinetics					709:716	kinetics	709:716	kinetics of GTPgammaS binding, number of G(i)-proteins activated, and constitutive activity, non-glycosylated FPR	709:821	However, in terms of high-affinity agonist binding, kinetics of GTPgammaS binding, number of G(i)-proteins activated, and constitutive activity, non-glycosylated FPR was much less active than native FPR.
12565836	5	13	theme	G	750:750	arg1	-proteins					754:762	G(i)-proteins	750:762	G(i)-proteins activated	750:772	However, in terms of high-affinity agonist binding, kinetics of GTPgammaS binding, number of G(i)-proteins activated, and constitutive activity, non-glycosylated FPR was much less active than native FPR.
12565836	7	14	theme	Asn179	1024:1029	arg1	N-glycosylation					968:982	N-glycosylation	968:982	N-glycosylation of N-terminal Asn4 and Asn10 but not of Asn179 in the second extracellular loop	968:1062	Our data indicate that N-glycosylation of N-terminal Asn4 and Asn10 but not of Asn179 in the second extracellular loop is essential for proper folding and, hence, function of FPR.
12565836	2	15	from	effects	343:349	arg1	binding					442:448	basal guanosine 5(')-O-(3-thiotriphosphate) (GTPgammaS) binding	386:448	basal guanosine 5(')-O-(3-thiotriphosphate) (GTPgammaS) binding	386:448	The FPR expressed with G(i)alpha(2)beta(1)gamma(2) in Sf9 insect cells exhibits high constitutive activity as assessed by strong inhibitory effects of an inverse agonist and Na(+) on basal guanosine 5(')-O-(3-thiotriphosphate) (GTPgammaS) binding.
12565836	4	16	theme	extracellular	561:573	arg1	residues					579:586	extracellular Asn residues	561:586	extracellular Asn residues	561:586	Site-directed mutagenesis of extracellular Asn residues prevented FPR glycosylation but not FPR expression in Sf9 membranes.
12565836	2	17	theme	i	228:228	arg1	gamma					245:249	G(i)alpha(2)beta(1)gamma(2)	226:252	G(i)alpha(2)beta(1)gamma(2) in Sf9 insect cells	226:272	The FPR expressed with G(i)alpha(2)beta(1)gamma(2) in Sf9 insect cells exhibits high constitutive activity as assessed by strong inhibitory effects of an inverse agonist and Na(+) on basal guanosine 5(')-O-(3-thiotriphosphate) (GTPgammaS) binding.
12565836	5	18	theme	binding	700:706	arg1	terms					669:673	terms	669:673	terms of high-affinity agonist binding	669:706	However, in terms of high-affinity agonist binding, kinetics of GTPgammaS binding, number of G(i)-proteins activated, and constitutive activity, non-glycosylated FPR was much less active than native FPR.
12565836	5	19	theme	high-affinity	678:690	arg1	binding					700:706	high-affinity agonist binding	678:706	high-affinity agonist binding	678:706	However, in terms of high-affinity agonist binding, kinetics of GTPgammaS binding, number of G(i)-proteins activated, and constitutive activity, non-glycosylated FPR was much less active than native FPR.
12565836	5	20	gly	non-glycosylated	802:817	arg1	FPR					819:821	non-glycosylated FPR	802:821	non-glycosylated FPR	802:821	However, in terms of high-affinity agonist binding, kinetics of GTPgammaS binding, number of G(i)-proteins activated, and constitutive activity, non-glycosylated FPR was much less active than native FPR.
12565836	7	21	theme	Asn4	998:1001	arg1	N-glycosylation					968:982	N-glycosylation	968:982	N-glycosylation of N-terminal Asn4 and Asn10 but not of Asn179 in the second extracellular loop	968:1062	Our data indicate that N-glycosylation of N-terminal Asn4 and Asn10 but not of Asn179 in the second extracellular loop is essential for proper folding and, hence, function of FPR.
12565836	8	22	theme	bacterial	1148:1156	arg1	glycosidases					1158:1169	bacterial glycosidases	1148:1169	bacterial glycosidases	1148:1169	FPR deglycosylation by bacterial glycosidases could be a mechanism by which bacteria compromise host defense.
12565836	2	23	theme	strong	325:330	arg1	effects					343:349	strong inhibitory effects	325:349	strong inhibitory effects of an inverse agonist and Na(+) on basal guanosine 5(')-O-(3-thiotriphosphate) (GTPgammaS) binding	325:448	The FPR expressed with G(i)alpha(2)beta(1)gamma(2) in Sf9 insect cells exhibits high constitutive activity as assessed by strong inhibitory effects of an inverse agonist and Na(+) on basal guanosine 5(')-O-(3-thiotriphosphate) (GTPgammaS) binding.
12565836	6	24	theme	similar	928:934	arg1	defects					936:942	similar defects	928:942	similar defects	928:942	FPR-Asn4Gln/Asn10Gln/Asn179Gln and FPR-Asn4Gln/Asn10/Gln exhibited similar defects.
12565836	5	25	theme	agonist	692:698	arg1	binding					700:706	high-affinity agonist binding	678:706	high-affinity agonist binding	678:706	However, in terms of high-affinity agonist binding, kinetics of GTPgammaS binding, number of G(i)-proteins activated, and constitutive activity, non-glycosylated FPR was much less active than native FPR.
12565836	2	26	theme	inhibitory	332:341	arg1	effects					343:349	strong inhibitory effects	325:349	strong inhibitory effects of an inverse agonist and Na(+) on basal guanosine 5(')-O-(3-thiotriphosphate) (GTPgammaS) binding	325:448	The FPR expressed with G(i)alpha(2)beta(1)gamma(2) in Sf9 insect cells exhibits high constitutive activity as assessed by strong inhibitory effects of an inverse agonist and Na(+) on basal guanosine 5(')-O-(3-thiotriphosphate) (GTPgammaS) binding.
12565836	0	27	theme	human	70:74	arg1	receptor					91:98	the human formyl peptide receptor	66:98	the human formyl peptide receptor	66:98	Critical role of N-terminal N-glycosylation for proper folding of the human formyl peptide receptor.
12565836	2	28	theme	beta	238:241	arg1	gamma					245:249	G(i)alpha(2)beta(1)gamma(2)	226:252	G(i)alpha(2)beta(1)gamma(2) in Sf9 insect cells	226:272	The FPR expressed with G(i)alpha(2)beta(1)gamma(2) in Sf9 insect cells exhibits high constitutive activity as assessed by strong inhibitory effects of an inverse agonist and Na(+) on basal guanosine 5(')-O-(3-thiotriphosphate) (GTPgammaS) binding.
12565836	2	29	theme	insect	261:266	arg1	cells					268:272	Sf9 insect cells	257:272	Sf9 insect cells	257:272	The FPR expressed with G(i)alpha(2)beta(1)gamma(2) in Sf9 insect cells exhibits high constitutive activity as assessed by strong inhibitory effects of an inverse agonist and Na(+) on basal guanosine 5(')-O-(3-thiotriphosphate) (GTPgammaS) binding.
12565836	0	30	theme	Critical	0:7	arg1	role					9:12	Critical role	0:12	Critical role of N-terminal N-glycosylation for proper folding of the human formyl peptide receptor.	0:99	Critical role of N-terminal N-glycosylation for proper folding of the human formyl peptide receptor.
12565836	5	31	theme	i	752:752	arg1	-proteins					754:762	G(i)-proteins	750:762	G(i)-proteins activated	750:772	However, in terms of high-affinity agonist binding, kinetics of GTPgammaS binding, number of G(i)-proteins activated, and constitutive activity, non-glycosylated FPR was much less active than native FPR.
12565836	2	32	theme	Sf9	257:259	arg1	cells					268:272	Sf9 insect cells	257:272	Sf9 insect cells	257:272	The FPR expressed with G(i)alpha(2)beta(1)gamma(2) in Sf9 insect cells exhibits high constitutive activity as assessed by strong inhibitory effects of an inverse agonist and Na(+) on basal guanosine 5(')-O-(3-thiotriphosphate) (GTPgammaS) binding.
12565836	0	33	theme	N-terminal	17:26	arg1	N-glycosylation					28:42	N-terminal N-glycosylation	17:42	N-terminal N-glycosylation	17:42	Critical role of N-terminal N-glycosylation for proper folding of the human formyl peptide receptor.
12565836	2	34	dep	gamma	245:249	arg1	1					243:243	1	243:243	1	243:243	The FPR expressed with G(i)alpha(2)beta(1)gamma(2) in Sf9 insect cells exhibits high constitutive activity as assessed by strong inhibitory effects of an inverse agonist and Na(+) on basal guanosine 5(')-O-(3-thiotriphosphate) (GTPgammaS) binding.
12565836	5	35	from	active	837:842	arg1	terms					669:673	terms	669:673	terms of high-affinity agonist binding	669:706	However, in terms of high-affinity agonist binding, kinetics of GTPgammaS binding, number of G(i)-proteins activated, and constitutive activity, non-glycosylated FPR was much less active than native FPR.
12565836	7	36	gly	N-glycosylation	968:982	arg1	Asn4					998:1001	N-terminal Asn4	987:1001	N-terminal Asn4	987:1001	Our data indicate that N-glycosylation of N-terminal Asn4 and Asn10 but not of Asn179 in the second extracellular loop is essential for proper folding and, hence, function of FPR.
12565836	7	36	gly	N-glycosylation	968:982	arg1	loop					1059:1062	the second extracellular loop	1034:1062	the second extracellular loop	1034:1062	Our data indicate that N-glycosylation of N-terminal Asn4 and Asn10 but not of Asn179 in the second extracellular loop is essential for proper folding and, hence, function of FPR.
12565836	7	36	gly	N-glycosylation	968:982	arg1	Asn179					1024:1029	Asn179	1024:1029	Asn179	1024:1029	Our data indicate that N-glycosylation of N-terminal Asn4 and Asn10 but not of Asn179 in the second extracellular loop is essential for proper folding and, hence, function of FPR.
12565836	7	36	gly	N-glycosylation	968:982	arg1	FPR					1120:1122	FPR	1120:1122	FPR	1120:1122	Our data indicate that N-glycosylation of N-terminal Asn4 and Asn10 but not of Asn179 in the second extracellular loop is essential for proper folding and, hence, function of FPR.
12565836	7	37	theme	FPR	1120:1122	arg1	folding					1088:1094	proper folding	1081:1094	proper folding	1081:1094	Our data indicate that N-glycosylation of N-terminal Asn4 and Asn10 but not of Asn179 in the second extracellular loop is essential for proper folding and, hence, function of FPR.
12565836	7	37	theme	FPR	1120:1122	arg1	function					1108:1115	function	1108:1115	function	1108:1115	Our data indicate that N-glycosylation of N-terminal Asn4 and Asn10 but not of Asn179 in the second extracellular loop is essential for proper folding and, hence, function of FPR.
12565836	3	38	theme	study	466:470	arg1	aim					455:457	The aim	451:457	The aim of our study	451:470	The aim of our study was to analyze the role of N-glycosylation in FPR function.
12565836	4	39	theme	Asn	575:577	arg1	residues					579:586	extracellular Asn residues	561:586	extracellular Asn residues	561:586	Site-directed mutagenesis of extracellular Asn residues prevented FPR glycosylation but not FPR expression in Sf9 membranes.
12565836	1	40	theme	G	188:188	arg1	-proteins					192:200	G(i)-proteins	188:200	G(i)-proteins	188:200	The human formyl peptide receptor (FPR) is N-glycosylated and activates phagocytes via G(i)-proteins.
12565836	2	41	theme	inverse	357:363	arg1	agonist					365:371	an inverse agonist	354:371	an inverse agonist	354:371	The FPR expressed with G(i)alpha(2)beta(1)gamma(2) in Sf9 insect cells exhibits high constitutive activity as assessed by strong inhibitory effects of an inverse agonist and Na(+) on basal guanosine 5(')-O-(3-thiotriphosphate) (GTPgammaS) binding.
12565836	5	42	theme	number	740:745	arg1	kinetics					709:716	kinetics	709:716	kinetics of GTPgammaS binding, number of G(i)-proteins activated, and constitutive activity, non-glycosylated FPR	709:821	However, in terms of high-affinity agonist binding, kinetics of GTPgammaS binding, number of G(i)-proteins activated, and constitutive activity, non-glycosylated FPR was much less active than native FPR.
12565836	3	43	from	role	491:494	arg1	function					522:529	FPR function	518:529	FPR function	518:529	The aim of our study was to analyze the role of N-glycosylation in FPR function.
12565836	2	44	theme	constitutive	288:299	arg1	activity					301:308	high constitutive activity	283:308	high constitutive activity	283:308	The FPR expressed with G(i)alpha(2)beta(1)gamma(2) in Sf9 insect cells exhibits high constitutive activity as assessed by strong inhibitory effects of an inverse agonist and Na(+) on basal guanosine 5(')-O-(3-thiotriphosphate) (GTPgammaS) binding.
12565836	2	45	theme	GTPgammaS	431:439	arg1	binding					442:448	basal guanosine 5(')-O-(3-thiotriphosphate) (GTPgammaS) binding	386:448	basal guanosine 5(')-O-(3-thiotriphosphate) (GTPgammaS) binding	386:448	The FPR expressed with G(i)alpha(2)beta(1)gamma(2) in Sf9 insect cells exhibits high constitutive activity as assessed by strong inhibitory effects of an inverse agonist and Na(+) on basal guanosine 5(')-O-(3-thiotriphosphate) (GTPgammaS) binding.
12565836	0	46	theme	N-glycosylation	28:42	arg1	role					9:12	Critical role	0:12	Critical role of N-terminal N-glycosylation for proper folding of the human formyl peptide receptor.	0:99	Critical role of N-terminal N-glycosylation for proper folding of the human formyl peptide receptor.
12565836	7	47	theme	N-terminal	987:996	arg1	Asn4					998:1001	N-terminal Asn4	987:1001	N-terminal Asn4	987:1001	Our data indicate that N-glycosylation of N-terminal Asn4 and Asn10 but not of Asn179 in the second extracellular loop is essential for proper folding and, hence, function of FPR.
12565836	4	48	theme	Sf9	642:644	arg1	membranes					646:654	Sf9 membranes	642:654	Sf9 membranes	642:654	Site-directed mutagenesis of extracellular Asn residues prevented FPR glycosylation but not FPR expression in Sf9 membranes.
12565836	5	49	from	terms	669:673	arg1	active					837:842	active	837:842	active	837:842	However, in terms of high-affinity agonist binding, kinetics of GTPgammaS binding, number of G(i)-proteins activated, and constitutive activity, non-glycosylated FPR was much less active than native FPR.
12565836	1	50	theme	i	190:190	arg1	-proteins					192:200	G(i)-proteins	188:200	G(i)-proteins	188:200	The human formyl peptide receptor (FPR) is N-glycosylated and activates phagocytes via G(i)-proteins.
12565836	2	51	theme	basal	386:390	arg1	binding					442:448	basal guanosine 5(')-O-(3-thiotriphosphate) (GTPgammaS) binding	386:448	basal guanosine 5(')-O-(3-thiotriphosphate) (GTPgammaS) binding	386:448	The FPR expressed with G(i)alpha(2)beta(1)gamma(2) in Sf9 insect cells exhibits high constitutive activity as assessed by strong inhibitory effects of an inverse agonist and Na(+) on basal guanosine 5(')-O-(3-thiotriphosphate) (GTPgammaS) binding.
12565836	1	52	theme	human	105:109	arg1	FPR					136:138	FPR	136:138	FPR	136:138	The human formyl peptide receptor (FPR) is N-glycosylated and activates phagocytes via G(i)-proteins.
12565836	1	52	theme	human	105:109	arg1	N-glycosylated					144:157	N-glycosylated	144:157	N-glycosylated	144:157	The human formyl peptide receptor (FPR) is N-glycosylated and activates phagocytes via G(i)-proteins.
12565836	1	52	theme	human	105:109	arg1	receptor					126:133	The human formyl peptide receptor	101:133	The human formyl peptide receptor (FPR)	101:139	The human formyl peptide receptor (FPR) is N-glycosylated and activates phagocytes via G(i)-proteins.
12565836	0	53	theme	proper	48:53	arg1	folding					55:61	proper folding	48:61	proper folding of the human formyl peptide receptor	48:98	Critical role of N-terminal N-glycosylation for proper folding of the human formyl peptide receptor.
12565836	3	54	gly	N-glycosylation	499:513	arg1	FPR					518:520	FPR function	518:529	FPR function	518:529	The aim of our study was to analyze the role of N-glycosylation in FPR function.
12565836	7	55	theme	proper	1081:1086	arg1	folding					1088:1094	proper folding	1081:1094	proper folding	1081:1094	Our data indicate that N-glycosylation of N-terminal Asn4 and Asn10 but not of Asn179 in the second extracellular loop is essential for proper folding and, hence, function of FPR.
12565836	5	56	theme	native	849:854	arg1	FPR					856:858	native FPR	849:858	native FPR	849:858	However, in terms of high-affinity agonist binding, kinetics of GTPgammaS binding, number of G(i)-proteins activated, and constitutive activity, non-glycosylated FPR was much less active than native FPR.
12565836	1	57	theme	formyl	111:116	arg1	FPR					136:138	FPR	136:138	FPR	136:138	The human formyl peptide receptor (FPR) is N-glycosylated and activates phagocytes via G(i)-proteins.
12565836	1	57	theme	formyl	111:116	arg1	N-glycosylated					144:157	N-glycosylated	144:157	N-glycosylated	144:157	The human formyl peptide receptor (FPR) is N-glycosylated and activates phagocytes via G(i)-proteins.
12565836	1	57	theme	formyl	111:116	arg1	receptor					126:133	The human formyl peptide receptor	101:133	The human formyl peptide receptor (FPR)	101:139	The human formyl peptide receptor (FPR) is N-glycosylated and activates phagocytes via G(i)-proteins.
12565836	7	58	from	N-glycosylation	968:982	arg1	loop					1059:1062	the second extracellular loop	1034:1062	the second extracellular loop	1034:1062	Our data indicate that N-glycosylation of N-terminal Asn4 and Asn10 but not of Asn179 in the second extracellular loop is essential for proper folding and, hence, function of FPR.
12565836	2	59	theme	-O-	406:408	arg1	binding					442:448	basal guanosine 5(')-O-(3-thiotriphosphate) (GTPgammaS) binding	386:448	basal guanosine 5(')-O-(3-thiotriphosphate) (GTPgammaS) binding	386:448	The FPR expressed with G(i)alpha(2)beta(1)gamma(2) in Sf9 insect cells exhibits high constitutive activity as assessed by strong inhibitory effects of an inverse agonist and Na(+) on basal guanosine 5(')-O-(3-thiotriphosphate) (GTPgammaS) binding.
12565836	4	60	theme	FPR	624:626	arg1	expression					628:637	FPR expression	624:637	FPR glycosylation but not FPR expression in Sf9 membranes	598:654	Site-directed mutagenesis of extracellular Asn residues prevented FPR glycosylation but not FPR expression in Sf9 membranes.
12565836	2	61	theme	G	226:226	arg1	gamma					245:249	G(i)alpha(2)beta(1)gamma(2)	226:252	G(i)alpha(2)beta(1)gamma(2) in Sf9 insect cells	226:272	The FPR expressed with G(i)alpha(2)beta(1)gamma(2) in Sf9 insect cells exhibits high constitutive activity as assessed by strong inhibitory effects of an inverse agonist and Na(+) on basal guanosine 5(')-O-(3-thiotriphosphate) (GTPgammaS) binding.
12565836	8	62	theme	host	1221:1224	arg1	defense					1226:1232	host defense	1221:1232	host defense	1221:1232	FPR deglycosylation by bacterial glycosidases could be a mechanism by which bacteria compromise host defense.
12565836	1	63	theme	peptide	118:124	arg1	FPR					136:138	FPR	136:138	FPR	136:138	The human formyl peptide receptor (FPR) is N-glycosylated and activates phagocytes via G(i)-proteins.
12565836	1	63	theme	peptide	118:124	arg1	N-glycosylated					144:157	N-glycosylated	144:157	N-glycosylated	144:157	The human formyl peptide receptor (FPR) is N-glycosylated and activates phagocytes via G(i)-proteins.
12565836	1	63	theme	peptide	118:124	arg1	receptor					126:133	The human formyl peptide receptor	101:133	The human formyl peptide receptor (FPR)	101:139	The human formyl peptide receptor (FPR) is N-glycosylated and activates phagocytes via G(i)-proteins.
12565836	4	64	theme	residues	579:586	arg1	mutagenesis					546:556	Site-directed mutagenesis	532:556	Site-directed mutagenesis of extracellular Asn residues	532:586	Site-directed mutagenesis of extracellular Asn residues prevented FPR glycosylation but not FPR expression in Sf9 membranes.
12565836	5	65	theme	constitutive	779:790	arg1	activity					792:799	constitutive activity	779:799	constitutive activity	779:799	However, in terms of high-affinity agonist binding, kinetics of GTPgammaS binding, number of G(i)-proteins activated, and constitutive activity, non-glycosylated FPR was much less active than native FPR.
12565836	4	66	theme	FPR	598:600	arg1	glycosylation					602:614	FPR glycosylation	598:614	FPR glycosylation but not FPR expression in Sf9 membranes	598:654	Site-directed mutagenesis of extracellular Asn residues prevented FPR glycosylation but not FPR expression in Sf9 membranes.
12565836	7	67	theme	extracellular	1045:1057	arg1	loop					1059:1062	the second extracellular loop	1034:1062	the second extracellular loop	1034:1062	Our data indicate that N-glycosylation of N-terminal Asn4 and Asn10 but not of Asn179 in the second extracellular loop is essential for proper folding and, hence, function of FPR.
12565836	4	68	theme	Site-directed	532:544	arg1	mutagenesis					546:556	Site-directed mutagenesis	532:556	Site-directed mutagenesis of extracellular Asn residues	532:586	Site-directed mutagenesis of extracellular Asn residues prevented FPR glycosylation but not FPR expression in Sf9 membranes.
12565836	8	69	theme	FPR	1125:1127	arg1	mechanism					1182:1190	a mechanism	1180:1190	a mechanism by which bacteria compromise host defense	1180:1232	FPR deglycosylation by bacterial glycosidases could be a mechanism by which bacteria compromise host defense.
12565836	8	69	theme	FPR	1125:1127	arg1	deglycosylation					1129:1143	FPR deglycosylation	1125:1143	FPR deglycosylation by bacterial glycosidases	1125:1169	FPR deglycosylation by bacterial glycosidases could be a mechanism by which bacteria compromise host defense.
12565836	2	70	dep	-O-	406:408	arg1	3-thiotriphosphate					410:427	3-thiotriphosphate	410:427	3-thiotriphosphate	410:427	The FPR expressed with G(i)alpha(2)beta(1)gamma(2) in Sf9 insect cells exhibits high constitutive activity as assessed by strong inhibitory effects of an inverse agonist and Na(+) on basal guanosine 5(')-O-(3-thiotriphosphate) (GTPgammaS) binding.
12565836	2	71	theme	high	283:286	arg1	activity					301:308	high constitutive activity	283:308	high constitutive activity	283:308	The FPR expressed with G(i)alpha(2)beta(1)gamma(2) in Sf9 insect cells exhibits high constitutive activity as assessed by strong inhibitory effects of an inverse agonist and Na(+) on basal guanosine 5(')-O-(3-thiotriphosphate) (GTPgammaS) binding.
12565836	5	72	theme	non-glycosylated	802:817	arg1	FPR					819:821	non-glycosylated FPR	802:821	non-glycosylated FPR	802:821	However, in terms of high-affinity agonist binding, kinetics of GTPgammaS binding, number of G(i)-proteins activated, and constitutive activity, non-glycosylated FPR was much less active than native FPR.
12565836	4	73	from	expression	628:637	arg1	membranes					646:654	Sf9 membranes	642:654	Sf9 membranes	642:654	Site-directed mutagenesis of extracellular Asn residues prevented FPR glycosylation but not FPR expression in Sf9 membranes.
12565836	2	74	theme	Na	377:378	arg1	effects					343:349	strong inhibitory effects	325:349	strong inhibitory effects of an inverse agonist and Na(+) on basal guanosine 5(')-O-(3-thiotriphosphate) (GTPgammaS) binding	325:448	The FPR expressed with G(i)alpha(2)beta(1)gamma(2) in Sf9 insect cells exhibits high constitutive activity as assessed by strong inhibitory effects of an inverse agonist and Na(+) on basal guanosine 5(')-O-(3-thiotriphosphate) (GTPgammaS) binding.
12565836	5	75	theme	FPR	819:821	arg1	kinetics					709:716	kinetics	709:716	kinetics of GTPgammaS binding, number of G(i)-proteins activated, and constitutive activity, non-glycosylated FPR	709:821	However, in terms of high-affinity agonist binding, kinetics of GTPgammaS binding, number of G(i)-proteins activated, and constitutive activity, non-glycosylated FPR was much less active than native FPR.
12565836	7	76	theme	second	1038:1043	arg1	loop					1059:1062	the second extracellular loop	1034:1062	the second extracellular loop	1034:1062	Our data indicate that N-glycosylation of N-terminal Asn4 and Asn10 but not of Asn179 in the second extracellular loop is essential for proper folding and, hence, function of FPR.
9442070	7	0	theme	triantennary	1298:1309	arg1	structures					1311:1320	triantennary structures	1298:1320	triantennary structures	1298:1320	Analysis of the N-glycans attached to recombinant IgA1 indicated that the Cα 2 N-glycosylation site contained mostly biantennary glycans, while the tailpiece site, absent in IgG, contained mostly triantennary structures.
9442070	3	1	theme	N-glycosylation	580:594	arg1	mutants					596:602	two N-glycosylation mutants	576:602	two N-glycosylation mutants	576:602	In this paper, we have analyzed the glycosylation of IgA1 and IgA1 Fab and Fc as well as three recombinant IgA1 molecules, including two N-glycosylation mutants.
9442070	9	2	theme	recombinant	1470:1480	arg1	IgA1					1482:1485	recombinant IgA1	1470:1485	recombinant IgA1	1470:1485	Neutrophil Fcα R binding studies, using recombinant IgA1, indicated that neither the tailpiece region nor the N-glycans in the C alpha 2 domain contribute to IgA1-neutrophil Fcα R binding.
9442070	7	3	theme	tailpiece	1250:1258	arg1	site					1260:1263	the tailpiece site	1246:1263	the tailpiece site	1246:1263	Analysis of the N-glycans attached to recombinant IgA1 indicated that the Cα 2 N-glycosylation site contained mostly biantennary glycans, while the tailpiece site, absent in IgG, contained mostly triantennary structures.
9442070	4	4	located	located	704:710	arg2	O-glycans					690:698	O-glycans	690:698	O-glycans	690:698	Amino acid sequencing data of the IgA1 Fc O-glycosylated hinge region indicated that O-glycans are located at Thr228, Ser230, and Ser232, while O-glycan sites at Thr225 and Thr236 are partially occupied.
9442070	4	4	located	located	704:710	arg1	Ser230					723:728	Ser230	723:728	Ser230	723:728	Amino acid sequencing data of the IgA1 Fc O-glycosylated hinge region indicated that O-glycans are located at Thr228, Ser230, and Ser232, while O-glycan sites at Thr225 and Thr236 are partially occupied.
9442070	4	4	located	located	704:710	arg1	Ser232					735:740	Ser232	735:740	Ser232	735:740	Amino acid sequencing data of the IgA1 Fc O-glycosylated hinge region indicated that O-glycans are located at Thr228, Ser230, and Ser232, while O-glycan sites at Thr225 and Thr236 are partially occupied.
9442070	4	4	located	located	704:710	arg1	Thr228					715:720	Thr228	715:720	Thr228	715:720	Amino acid sequencing data of the IgA1 Fc O-glycosylated hinge region indicated that O-glycans are located at Thr228, Ser230, and Ser232, while O-glycan sites at Thr225 and Thr236 are partially occupied.
9442070	12	5	theme	primary	1941:1947	arg1	sequence					1949:1956	the primary sequence	1937:1956	the primary sequence	1937:1956	As a consequence of both the primary sequence and S-S bond pattern, the N-glycans in IgA1 Fc are not confined within the inter-α-chain space.
9442070	2	6	with	interaction	374:384	arg1	receptors					402:410	various Fc receptors	391:410	various Fc receptors (Fc Rs)	391:418	In contrast to IgA1, the glycosylation of IgG has been well characterized, and its interaction with various Fc receptors (Fc Rs) has been well studied.
9442070	2	6	with	interaction	374:384	arg1	Rs					416:417	Fc Rs	413:417	Fc Rs	413:417	In contrast to IgA1, the glycosylation of IgG has been well characterized, and its interaction with various Fc receptors (Fc Rs) has been well studied.
9442070	11	7	theme	molecular	1887:1895	arg1	model					1897:1901	a molecular model	1885:1901	a molecular model of IgA1	1885:1909	The primary sequence and disulfide bond pattern of IgA1, together with the crystal structures of IgG1 Fc and mouse IgA Fab and the glycan sequencing data, were used to generate a molecular model of IgA1.
9442070	8	8	from	site	1406:1409	arg1	at					1380:1381	processing at one Fc N-glycosylation site	1369:1409	processing at one Fc N-glycosylation site	1369:1409	Further analysis of these data suggested that processing at one Fc N-glycosylation site affects the other.
9442070	8	8	from	site	1406:1409	arg1	N-glycosylation					1390:1404	processing at one Fc N-glycosylation site	1369:1409	processing at one Fc N-glycosylation site	1369:1409	Further analysis of these data suggested that processing at one Fc N-glycosylation site affects the other.
9442070	8	8	from	site	1406:1409	arg1	processing					1369:1378	processing at one Fc N-glycosylation site	1369:1409	processing at one Fc N-glycosylation site	1369:1409	Further analysis of these data suggested that processing at one Fc N-glycosylation site affects the other.
9442070	8	8	from	site	1406:1409	arg1	Fc					1387:1388	processing at one Fc N-glycosylation site	1369:1409	processing at one Fc N-glycosylation site	1369:1409	Further analysis of these data suggested that processing at one Fc N-glycosylation site affects the other.
9442070	1	9	theme	human	139:143	arg1	immunoglobulins					151:165	The human serum immunoglobulins IgG and IgA1	135:178	The human serum immunoglobulins IgG and IgA1	135:178	The human serum immunoglobulins IgG and IgA1 are produced in bone marrow and both interact with specific cellular receptors that mediate biological events.
9442070	1	9	theme	human	139:143	arg1	IgA1					175:178	IgA1	175:178	IgA1	175:178	The human serum immunoglobulins IgG and IgA1 are produced in bone marrow and both interact with specific cellular receptors that mediate biological events.
9442070	1	9	theme	human	139:143	arg1	IgG					167:169	IgG	167:169	IgG	167:169	The human serum immunoglobulins IgG and IgA1 are produced in bone marrow and both interact with specific cellular receptors that mediate biological events.
9442070	7	10	theme	absent	1266:1271	arg1	site					1260:1263	the tailpiece site	1246:1263	the tailpiece site	1246:1263	Analysis of the N-glycans attached to recombinant IgA1 indicated that the Cα 2 N-glycosylation site contained mostly biantennary glycans, while the tailpiece site, absent in IgG, contained mostly triantennary structures.
9442070	6	11	link	N-linked	1029:1036	arg1	glycans					1038:1044	only N-linked glycans	1024:1044	only N-linked glycans	1024:1044	This paper contains the first report of Fab glycosylation in IgA1, and (in contrast to IgG Fab, which contains only N-linked glycans) both N- and O-linked oligosaccharides were identified.
9442070	11	12	theme	Fab	1827:1829	arg1	structures					1791:1800	the crystal structures	1779:1800	the crystal structures of IgG1 Fc and mouse IgA Fab and the glycan sequencing data	1779:1860	The primary sequence and disulfide bond pattern of IgA1, together with the crystal structures of IgG1 Fc and mouse IgA Fab and the glycan sequencing data, were used to generate a molecular model of IgA1.
9442070	13	13	theme	increased	2126:2134	arg1	sialylation					2136:2146	sialylation	2136:2146	sialylation	2136:2146	The accessibility of the Cα 2 N-glycans provides an explanation for the increased sialylation and galactosylation of IgA1 Fc over that of IgG Fc N-glycans, which are confined in the space between the two Cγ 2 domains.
9442070	11	14	theme	IgG1	1805:1808	arg1	Fc					1810:1811	IgG1 Fc	1805:1811	IgG1 Fc	1805:1811	The primary sequence and disulfide bond pattern of IgA1, together with the crystal structures of IgG1 Fc and mouse IgA Fab and the glycan sequencing data, were used to generate a molecular model of IgA1.
9442070	3	15	gly	glycosylation	479:491	arg1	paper					451:455	this paper	446:455	this paper	446:455	In this paper, we have analyzed the glycosylation of IgA1 and IgA1 Fab and Fc as well as three recombinant IgA1 molecules, including two N-glycosylation mutants.
9442070	3	15	gly	glycosylation	479:491	arg1	Fab					510:512	IgA1 Fab	505:512	IgA1 Fab	505:512	In this paper, we have analyzed the glycosylation of IgA1 and IgA1 Fab and Fc as well as three recombinant IgA1 molecules, including two N-glycosylation mutants.
9442070	3	15	gly	glycosylation	479:491	arg1	IgA1					496:499	IgA1	496:499	IgA1	496:499	In this paper, we have analyzed the glycosylation of IgA1 and IgA1 Fab and Fc as well as three recombinant IgA1 molecules, including two N-glycosylation mutants.
9442070	11	16	theme	mouse	1817:1821	arg1	IgA					1823:1825	mouse IgA	1817:1825	mouse IgA	1817:1825	The primary sequence and disulfide bond pattern of IgA1, together with the crystal structures of IgG1 Fc and mouse IgA Fab and the glycan sequencing data, were used to generate a molecular model of IgA1.
9442070	9	17	theme	binding	1447:1453	arg1	studies					1455:1461	Neutrophil Fcα R binding studies	1430:1461	Neutrophil Fcα R binding studies	1430:1461	Neutrophil Fcα R binding studies, using recombinant IgA1, indicated that neither the tailpiece region nor the N-glycans in the C alpha 2 domain contribute to IgA1-neutrophil Fcα R binding.
9442070	0	18	theme	N-glycosylation	89:103	arg1	role					81:84	the role	77:84	the role of N-glycosylation on Fcα receptor interactions	77:132	The glycosylation and structure of human serum IgA1, Fab, and Fc regions and the role of N-glycosylation on Fcα receptor interactions.
9442070	0	18	theme	N-glycosylation	89:103	arg1	structure					22:30	structure	22:30	structure	22:30	The glycosylation and structure of human serum IgA1, Fab, and Fc regions and the role of N-glycosylation on Fcα receptor interactions.
9442070	0	18	theme	N-glycosylation	89:103	arg1	glycosylation					4:16	glycosylation	4:16	glycosylation	4:16	The glycosylation and structure of human serum IgA1, Fab, and Fc regions and the role of N-glycosylation on Fcα receptor interactions.
9442070	3	19	theme	Fab	510:512	arg1	glycosylation					479:491	the glycosylation	475:491	the glycosylation of IgA1 and IgA1 Fab and Fc as well as three recombinant IgA1 molecules, including two N-glycosylation mutants	475:602	In this paper, we have analyzed the glycosylation of IgA1 and IgA1 Fab and Fc as well as three recombinant IgA1 molecules, including two N-glycosylation mutants.
9442070	3	19	theme	Fab	510:512	arg1	mutants					596:602	two N-glycosylation mutants	576:602	two N-glycosylation mutants	576:602	In this paper, we have analyzed the glycosylation of IgA1 and IgA1 Fab and Fc as well as three recombinant IgA1 molecules, including two N-glycosylation mutants.
9442070	3	19	theme	Fab	510:512	arg1	molecules					555:563	three recombinant IgA1 molecules	532:563	three recombinant IgA1 molecules	532:563	In this paper, we have analyzed the glycosylation of IgA1 and IgA1 Fab and Fc as well as three recombinant IgA1 molecules, including two N-glycosylation mutants.
9442070	11	20	dep	together	1765:1772	arg1	with					1774:1777	with	1774:1777	with	1774:1777	The primary sequence and disulfide bond pattern of IgA1, together with the crystal structures of IgG1 Fc and mouse IgA Fab and the glycan sequencing data, were used to generate a molecular model of IgA1.
9442070	7	21	gly	N-glycosylation	1181:1195	arg2	site					1197:1200	the Cα 2 N-glycosylation site	1172:1200	the Cα 2 N-glycosylation site	1172:1200	Analysis of the N-glycans attached to recombinant IgA1 indicated that the Cα 2 N-glycosylation site contained mostly biantennary glycans, while the tailpiece site, absent in IgG, contained mostly triantennary structures.
9442070	7	21	gly	N-glycosylation	1181:1195	arg2	2					1179:1179	2	1179:1179	2	1179:1179	Analysis of the N-glycans attached to recombinant IgA1 indicated that the Cα 2 N-glycosylation site contained mostly biantennary glycans, while the tailpiece site, absent in IgG, contained mostly triantennary structures.
9442070	11	22	theme	sequencing	1846:1855	arg1	data					1857:1860	the glycan sequencing data	1835:1860	the glycan sequencing data	1835:1860	The primary sequence and disulfide bond pattern of IgA1, together with the crystal structures of IgG1 Fc and mouse IgA Fab and the glycan sequencing data, were used to generate a molecular model of IgA1.
9442070	6	23	theme	N-linked	1029:1036	arg1	glycans					1038:1044	only N-linked glycans	1024:1044	only N-linked glycans	1024:1044	This paper contains the first report of Fab glycosylation in IgA1, and (in contrast to IgG Fab, which contains only N-linked glycans) both N- and O-linked oligosaccharides were identified.
9442070	4	24	theme	sequencing	616:625	arg1	data					627:630	Amino acid sequencing data	605:630	Amino acid sequencing data of the IgA1 Fc O-glycosylated hinge region	605:673	Amino acid sequencing data of the IgA1 Fc O-glycosylated hinge region indicated that O-glycans are located at Thr228, Ser230, and Ser232, while O-glycan sites at Thr225 and Thr236 are partially occupied.
9442070	0	25	theme	Fcα	108:110	arg1	interactions					121:132	Fcα receptor interactions	108:132	Fcα receptor interactions	108:132	The glycosylation and structure of human serum IgA1, Fab, and Fc regions and the role of N-glycosylation on Fcα receptor interactions.
9442070	11	26	theme	disulfide	1733:1741	arg1	pattern					1748:1754	disulfide bond pattern	1733:1754	disulfide bond pattern	1733:1754	The primary sequence and disulfide bond pattern of IgA1, together with the crystal structures of IgG1 Fc and mouse IgA Fab and the glycan sequencing data, were used to generate a molecular model of IgA1.
9442070	4	27	theme	O-glycosylated	647:660	arg1	region					668:673	the IgA1 Fc O-glycosylated hinge region	635:673	the IgA1 Fc O-glycosylated hinge region	635:673	Amino acid sequencing data of the IgA1 Fc O-glycosylated hinge region indicated that O-glycans are located at Thr228, Ser230, and Ser232, while O-glycan sites at Thr225 and Thr236 are partially occupied.
9442070	13	28	theme	IgG	2192:2194	arg1	N-glycans					2199:2207	IgG Fc N-glycans	2192:2207	IgG Fc N-glycans	2192:2207	The accessibility of the Cα 2 N-glycans provides an explanation for the increased sialylation and galactosylation of IgA1 Fc over that of IgG Fc N-glycans, which are confined in the space between the two Cγ 2 domains.
9442070	4	29	from	Thr236	778:783	arg1	sites					758:762	O-glycan sites	749:762	O-glycan sites at Thr225 and Thr236	749:783	Amino acid sequencing data of the IgA1 Fc O-glycosylated hinge region indicated that O-glycans are located at Thr228, Ser230, and Ser232, while O-glycan sites at Thr225 and Thr236 are partially occupied.
9442070	6	30	theme	IgG	1000:1002	arg1	Fab					1004:1006	IgG Fab	1000:1006	IgG Fab	1000:1006	This paper contains the first report of Fab glycosylation in IgA1, and (in contrast to IgG Fab, which contains only N-linked glycans) both N- and O-linked oligosaccharides were identified.
9442070	9	31	theme	C	1557:1557	arg1	domain					1567:1572	the C alpha 2 domain	1553:1572	the C alpha 2 domain	1553:1572	Neutrophil Fcα R binding studies, using recombinant IgA1, indicated that neither the tailpiece region nor the N-glycans in the C alpha 2 domain contribute to IgA1-neutrophil Fcα R binding.
9442070	12	32	theme	inter-α-chain	2033:2045	arg1	space					2047:2051	the inter-α-chain space	2029:2051	the inter-α-chain space	2029:2051	As a consequence of both the primary sequence and S-S bond pattern, the N-glycans in IgA1 Fc are not confined within the inter-α-chain space.
9442070	4	33	from	Thr225	767:772	arg1	sites					758:762	O-glycan sites	749:762	O-glycan sites at Thr225 and Thr236	749:783	Amino acid sequencing data of the IgA1 Fc O-glycosylated hinge region indicated that O-glycans are located at Thr228, Ser230, and Ser232, while O-glycan sites at Thr225 and Thr236 are partially occupied.
9442070	11	34	theme	IgA1	1759:1762	arg1	pattern					1748:1754	disulfide bond pattern	1733:1754	disulfide bond pattern	1733:1754	The primary sequence and disulfide bond pattern of IgA1, together with the crystal structures of IgG1 Fc and mouse IgA Fab and the glycan sequencing data, were used to generate a molecular model of IgA1.
9442070	11	34	theme	IgA1	1759:1762	arg1	sequence					1720:1727	primary sequence	1712:1727	primary sequence	1712:1727	The primary sequence and disulfide bond pattern of IgA1, together with the crystal structures of IgG1 Fc and mouse IgA Fab and the glycan sequencing data, were used to generate a molecular model of IgA1.
9442070	11	35	used	used	1868:1871	arg2	sequence					1720:1727	primary sequence	1712:1727	primary sequence	1712:1727	The primary sequence and disulfide bond pattern of IgA1, together with the crystal structures of IgG1 Fc and mouse IgA Fab and the glycan sequencing data, were used to generate a molecular model of IgA1.
9442070	11	35	used	used	1868:1871	arg2	structures					1791:1800	the crystal structures	1779:1800	the crystal structures of IgG1 Fc and mouse IgA Fab and the glycan sequencing data	1779:1860	The primary sequence and disulfide bond pattern of IgA1, together with the crystal structures of IgG1 Fc and mouse IgA Fab and the glycan sequencing data, were used to generate a molecular model of IgA1.
9442070	11	35	used	used	1868:1871	arg2	pattern					1748:1754	disulfide bond pattern	1733:1754	disulfide bond pattern	1733:1754	The primary sequence and disulfide bond pattern of IgA1, together with the crystal structures of IgG1 Fc and mouse IgA Fab and the glycan sequencing data, were used to generate a molecular model of IgA1.
9442070	9	36	from	N-glycans	1540:1548	arg1	domain					1567:1572	the C alpha 2 domain	1553:1572	the C alpha 2 domain	1553:1572	Neutrophil Fcα R binding studies, using recombinant IgA1, indicated that neither the tailpiece region nor the N-glycans in the C alpha 2 domain contribute to IgA1-neutrophil Fcα R binding.
9442070	5	37	gly	sialylated	848:857	arg1	%					816:816	Over 90%	809:816	Over 90% of the N-glycans in IgA1	809:841	Over 90% of the N-glycans in IgA1 were sialylated, in contrast to IgG, where < 10% contain sialic acid.
9442070	5	37	gly	sialylated	848:857	arg1	N-glycans					825:833	the N-glycans	821:833	the N-glycans in IgA1	821:841	Over 90% of the N-glycans in IgA1 were sialylated, in contrast to IgG, where < 10% contain sialic acid.
9442070	4	38	theme	Amino	605:609	arg1	data					627:630	Amino acid sequencing data	605:630	Amino acid sequencing data of the IgA1 Fc O-glycosylated hinge region	605:673	Amino acid sequencing data of the IgA1 Fc O-glycosylated hinge region indicated that O-glycans are located at Thr228, Ser230, and Ser232, while O-glycan sites at Thr225 and Thr236 are partially occupied.
9442070	8	39	theme	Further	1323:1329	arg1	analysis					1331:1338	Further analysis	1323:1338	Further analysis of these data	1323:1352	Further analysis of these data suggested that processing at one Fc N-glycosylation site affects the other.
9442070	4	40	theme	region	668:673	arg1	data					627:630	Amino acid sequencing data	605:630	Amino acid sequencing data of the IgA1 Fc O-glycosylated hinge region	605:673	Amino acid sequencing data of the IgA1 Fc O-glycosylated hinge region indicated that O-glycans are located at Thr228, Ser230, and Ser232, while O-glycan sites at Thr225 and Thr236 are partially occupied.
9442070	12	41	theme	sequence	1949:1956	arg1	consequence					1917:1927	a consequence	1915:1927	a consequence of both the primary sequence and S-S bond pattern	1915:1977	As a consequence of both the primary sequence and S-S bond pattern, the N-glycans in IgA1 Fc are not confined within the inter-α-chain space.
9442070	12	41	theme	sequence	1949:1956	arg1	N-glycans					1984:1992	the N-glycans	1980:1992	the N-glycans in IgA1 Fc	1980:2003	As a consequence of both the primary sequence and S-S bond pattern, the N-glycans in IgA1 Fc are not confined within the inter-α-chain space.
9442070	0	42	theme	Fc	62:63	arg1	regions					65:71	Fc regions	62:71	Fc regions	62:71	The glycosylation and structure of human serum IgA1, Fab, and Fc regions and the role of N-glycosylation on Fcα receptor interactions.
9442070	9	43	theme	IgA1-neutrophil	1588:1602	arg1	R					1608:1608	IgA1-neutrophil Fcα R	1588:1608	IgA1-neutrophil Fcα R binding	1588:1616	Neutrophil Fcα R binding studies, using recombinant IgA1, indicated that neither the tailpiece region nor the N-glycans in the C alpha 2 domain contribute to IgA1-neutrophil Fcα R binding.
9442070	4	44	from	Ser232	735:740	arg1	located					704:710	located	704:710	located	704:710	Amino acid sequencing data of the IgA1 Fc O-glycosylated hinge region indicated that O-glycans are located at Thr228, Ser230, and Ser232, while O-glycan sites at Thr225 and Thr236 are partially occupied.
9442070	13	45	theme	Cγ	2258:2259	arg1	domains					2263:2269	the two Cγ 2 domains	2250:2269	the two Cγ 2 domains	2250:2269	The accessibility of the Cα 2 N-glycans provides an explanation for the increased sialylation and galactosylation of IgA1 Fc over that of IgG Fc N-glycans, which are confined in the space between the two Cγ 2 domains.
9442070	13	46	theme	Fc	2176:2177	arg1	sialylation					2136:2146	sialylation	2136:2146	sialylation	2136:2146	The accessibility of the Cα 2 N-glycans provides an explanation for the increased sialylation and galactosylation of IgA1 Fc over that of IgG Fc N-glycans, which are confined in the space between the two Cγ 2 domains.
9442070	13	46	theme	Fc	2176:2177	arg1	galactosylation					2152:2166	galactosylation	2152:2166	galactosylation	2152:2166	The accessibility of the Cα 2 N-glycans provides an explanation for the increased sialylation and galactosylation of IgA1 Fc over that of IgG Fc N-glycans, which are confined in the space between the two Cγ 2 domains.
9442070	2	47	theme	Fc	399:400	arg1	receptors					402:410	various Fc receptors	391:410	various Fc receptors (Fc Rs)	391:418	In contrast to IgA1, the glycosylation of IgG has been well characterized, and its interaction with various Fc receptors (Fc Rs) has been well studied.
9442070	2	47	theme	Fc	399:400	arg1	Rs					416:417	Fc Rs	413:417	Fc Rs	413:417	In contrast to IgA1, the glycosylation of IgG has been well characterized, and its interaction with various Fc receptors (Fc Rs) has been well studied.
9442070	8	48	theme	data	1349:1352	arg1	analysis					1331:1338	Further analysis	1323:1338	Further analysis of these data	1323:1352	Further analysis of these data suggested that processing at one Fc N-glycosylation site affects the other.
9442070	4	49	theme	IgA1	639:642	arg1	region					668:673	the IgA1 Fc O-glycosylated hinge region	635:673	the IgA1 Fc O-glycosylated hinge region	635:673	Amino acid sequencing data of the IgA1 Fc O-glycosylated hinge region indicated that O-glycans are located at Thr228, Ser230, and Ser232, while O-glycan sites at Thr225 and Thr236 are partially occupied.
9442070	1	50	theme	specific	231:238	arg1	receptors					249:257	specific cellular receptors	231:257	specific cellular receptors that mediate biological events	231:288	The human serum immunoglobulins IgG and IgA1 are produced in bone marrow and both interact with specific cellular receptors that mediate biological events.
9442070	8	51	gly	N-glycosylation	1390:1404	arg2	one					1383:1385	one	1383:1385	one	1383:1385	Further analysis of these data suggested that processing at one Fc N-glycosylation site affects the other.
9442070	8	51	gly	N-glycosylation	1390:1404	arg2	site					1406:1409	processing at one Fc N-glycosylation site	1369:1409	processing at one Fc N-glycosylation site	1369:1409	Further analysis of these data suggested that processing at one Fc N-glycosylation site affects the other.
9442070	8	51	gly	N-glycosylation	1390:1404	arg1	site					1406:1409	processing at one Fc N-glycosylation site	1369:1409	processing at one Fc N-glycosylation site	1369:1409	Further analysis of these data suggested that processing at one Fc N-glycosylation site affects the other.
9442070	2	52	gly	glycosylation	316:328	arg1	IgG					333:335	IgG	333:335	IgG	333:335	In contrast to IgA1, the glycosylation of IgG has been well characterized, and its interaction with various Fc receptors (Fc Rs) has been well studied.
9442070	2	53	dep	IgA1	306:309	arg1	contrast					294:301	contrast	294:301	contrast	294:301	In contrast to IgA1, the glycosylation of IgG has been well characterized, and its interaction with various Fc receptors (Fc Rs) has been well studied.
9442070	11	54	theme	primary	1712:1718	arg1	sequence					1720:1727	primary sequence	1712:1727	primary sequence	1712:1727	The primary sequence and disulfide bond pattern of IgA1, together with the crystal structures of IgG1 Fc and mouse IgA Fab and the glycan sequencing data, were used to generate a molecular model of IgA1.
9442070	5	55	theme	N-glycans	825:833	arg1	%					816:816	Over 90%	809:816	Over 90% of the N-glycans in IgA1	809:841	Over 90% of the N-glycans in IgA1 were sialylated, in contrast to IgG, where < 10% contain sialic acid.
9442070	5	55	theme	N-glycans	825:833	arg1	N-glycans					825:833	the N-glycans	821:833	the N-glycans in IgA1	821:841	Over 90% of the N-glycans in IgA1 were sialylated, in contrast to IgG, where < 10% contain sialic acid.
9442070	7	56	theme	N-glycans	1118:1126	arg1	Analysis					1102:1109	Analysis	1102:1109	Analysis of the N-glycans attached to recombinant IgA1	1102:1155	Analysis of the N-glycans attached to recombinant IgA1 indicated that the Cα 2 N-glycosylation site contained mostly biantennary glycans, while the tailpiece site, absent in IgG, contained mostly triantennary structures.
9442070	8	57	theme	at	1380:1381	arg1	site					1406:1409	processing at one Fc N-glycosylation site	1369:1409	processing at one Fc N-glycosylation site	1369:1409	Further analysis of these data suggested that processing at one Fc N-glycosylation site affects the other.
9442070	3	58	theme	IgA1	550:553	arg1	mutants					596:602	two N-glycosylation mutants	576:602	two N-glycosylation mutants	576:602	In this paper, we have analyzed the glycosylation of IgA1 and IgA1 Fab and Fc as well as three recombinant IgA1 molecules, including two N-glycosylation mutants.
9442070	3	58	theme	IgA1	550:553	arg1	molecules					555:563	three recombinant IgA1 molecules	532:563	three recombinant IgA1 molecules	532:563	In this paper, we have analyzed the glycosylation of IgA1 and IgA1 Fab and Fc as well as three recombinant IgA1 molecules, including two N-glycosylation mutants.
9442070	5	59	contain	contain	892:898	arg1	%					890:890	< 10%	886:890	< 10%	886:890	Over 90% of the N-glycans in IgA1 were sialylated, in contrast to IgG, where < 10% contain sialic acid.
9442070	5	59	contain	contain	892:898	arg2	acid					907:910	sialic acid	900:910	sialic acid	900:910	Over 90% of the N-glycans in IgA1 were sialylated, in contrast to IgG, where < 10% contain sialic acid.
9442070	0	60	gly	glycosylation	4:16	arg1	N-glycosylation					89:103	N-glycosylation	89:103	N-glycosylation	89:103	The glycosylation and structure of human serum IgA1, Fab, and Fc regions and the role of N-glycosylation on Fcα receptor interactions.
9442070	0	60	gly	glycosylation	4:16	arg1	regions					65:71	Fc regions	62:71	Fc regions	62:71	The glycosylation and structure of human serum IgA1, Fab, and Fc regions and the role of N-glycosylation on Fcα receptor interactions.
9442070	0	60	gly	glycosylation	4:16	arg1	interactions					121:132	Fcα receptor interactions	108:132	Fcα receptor interactions	108:132	The glycosylation and structure of human serum IgA1, Fab, and Fc regions and the role of N-glycosylation on Fcα receptor interactions.
9442070	0	60	gly	glycosylation	4:16	arg1	Fab					53:55	Fab	53:55	Fab	53:55	The glycosylation and structure of human serum IgA1, Fab, and Fc regions and the role of N-glycosylation on Fcα receptor interactions.
9442070	0	60	gly	glycosylation	4:16	arg1	IgA1					47:50	human serum IgA1	35:50	human serum IgA1	35:50	The glycosylation and structure of human serum IgA1, Fab, and Fc regions and the role of N-glycosylation on Fcα receptor interactions.
9442070	8	61	theme	Fc	1387:1388	arg1	site					1406:1409	processing at one Fc N-glycosylation site	1369:1409	processing at one Fc N-glycosylation site	1369:1409	Further analysis of these data suggested that processing at one Fc N-glycosylation site affects the other.
9442070	0	62	theme	serum	41:45	arg1	IgA1					47:50	human serum IgA1	35:50	human serum IgA1	35:50	The glycosylation and structure of human serum IgA1, Fab, and Fc regions and the role of N-glycosylation on Fcα receptor interactions.
9442070	5	63	theme	<	886:886	arg1	%					890:890	< 10%	886:890	< 10%	886:890	Over 90% of the N-glycans in IgA1 were sialylated, in contrast to IgG, where < 10% contain sialic acid.
9442070	6	64	theme	glycosylation	957:969	arg1	report					943:948	the first report	933:948	the first report of Fab glycosylation in IgA1	933:977	This paper contains the first report of Fab glycosylation in IgA1, and (in contrast to IgG Fab, which contains only N-linked glycans) both N- and O-linked oligosaccharides were identified.
9442070	6	65	contain	contains	1015:1022	arg1	contrast					988:995	contrast	988:995	contrast	988:995	This paper contains the first report of Fab glycosylation in IgA1, and (in contrast to IgG Fab, which contains only N-linked glycans) both N- and O-linked oligosaccharides were identified.
9442070	6	65	contain	contains	1015:1022	arg2	glycans					1038:1044	only N-linked glycans	1024:1044	only N-linked glycans	1024:1044	This paper contains the first report of Fab glycosylation in IgA1, and (in contrast to IgG Fab, which contains only N-linked glycans) both N- and O-linked oligosaccharides were identified.
9442070	5	66	from	N-glycans	825:833	arg1	IgA1					838:841	IgA1	838:841	IgA1	838:841	Over 90% of the N-glycans in IgA1 were sialylated, in contrast to IgG, where < 10% contain sialic acid.
9442070	9	67	theme	R	1445:1445	arg1	studies					1455:1461	Neutrophil Fcα R binding studies	1430:1461	Neutrophil Fcα R binding studies	1430:1461	Neutrophil Fcα R binding studies, using recombinant IgA1, indicated that neither the tailpiece region nor the N-glycans in the C alpha 2 domain contribute to IgA1-neutrophil Fcα R binding.
9442070	7	68	attach	attached	1128:1135	arg2	N-glycans					1118:1126	the N-glycans	1114:1126	the N-glycans attached to recombinant IgA1	1114:1155	Analysis of the N-glycans attached to recombinant IgA1 indicated that the Cα 2 N-glycosylation site contained mostly biantennary glycans, while the tailpiece site, absent in IgG, contained mostly triantennary structures.
9442070	7	68	attach	attached	1128:1135	arg1	IgA1					1152:1155	recombinant IgA1	1140:1155	recombinant IgA1	1140:1155	Analysis of the N-glycans attached to recombinant IgA1 indicated that the Cα 2 N-glycosylation site contained mostly biantennary glycans, while the tailpiece site, absent in IgG, contained mostly triantennary structures.
9442070	1	69	theme	bone	196:199	arg1	marrow					201:206	bone marrow	196:206	bone marrow	196:206	The human serum immunoglobulins IgG and IgA1 are produced in bone marrow and both interact with specific cellular receptors that mediate biological events.
9442070	11	70	dep	sequence	1720:1727	arg1	The					1708:1710	The	1708:1710	The	1708:1710	The primary sequence and disulfide bond pattern of IgA1, together with the crystal structures of IgG1 Fc and mouse IgA Fab and the glycan sequencing data, were used to generate a molecular model of IgA1.
9442070	6	71	theme	first	937:941	arg1	report					943:948	the first report	933:948	the first report of Fab glycosylation in IgA1	933:977	This paper contains the first report of Fab glycosylation in IgA1, and (in contrast to IgG Fab, which contains only N-linked glycans) both N- and O-linked oligosaccharides were identified.
9442070	0	72	from	role	81:84	arg1	interactions					121:132	Fcα receptor interactions	108:132	Fcα receptor interactions	108:132	The glycosylation and structure of human serum IgA1, Fab, and Fc regions and the role of N-glycosylation on Fcα receptor interactions.
9442070	10	73	theme	Fcγ	1701:1703	arg1	R					1705:1705	the Fcγ R	1697:1705	the Fcγ R	1697:1705	This contrasts with IgG, where removal of the Fc N-glycans reduces binding to the Fcγ R.
9442070	6	74	from	N-	1052:1053	arg1	contrast					988:995	contrast	988:995	contrast	988:995	This paper contains the first report of Fab glycosylation in IgA1, and (in contrast to IgG Fab, which contains only N-linked glycans) both N- and O-linked oligosaccharides were identified.
9442070	4	75	theme	O-glycan	749:756	arg1	sites					758:762	O-glycan sites	749:762	O-glycan sites at Thr225 and Thr236	749:783	Amino acid sequencing data of the IgA1 Fc O-glycosylated hinge region indicated that O-glycans are located at Thr228, Ser230, and Ser232, while O-glycan sites at Thr225 and Thr236 are partially occupied.
9442070	11	76	theme	crystal	1783:1789	arg1	structures					1791:1800	the crystal structures	1779:1800	the crystal structures of IgG1 Fc and mouse IgA Fab and the glycan sequencing data	1779:1860	The primary sequence and disulfide bond pattern of IgA1, together with the crystal structures of IgG1 Fc and mouse IgA Fab and the glycan sequencing data, were used to generate a molecular model of IgA1.
9442070	5	77	from	IgA1	838:841	arg1	%					816:816	Over 90%	809:816	Over 90% of the N-glycans in IgA1	809:841	Over 90% of the N-glycans in IgA1 were sialylated, in contrast to IgG, where < 10% contain sialic acid.
9442070	5	77	from	IgA1	838:841	arg1	N-glycans					825:833	the N-glycans	821:833	the N-glycans in IgA1	821:841	Over 90% of the N-glycans in IgA1 were sialylated, in contrast to IgG, where < 10% contain sialic acid.
9442070	7	78	contain	contained	1202:1210	arg1	site					1197:1200	the Cα 2 N-glycosylation site	1172:1200	the Cα 2 N-glycosylation site	1172:1200	Analysis of the N-glycans attached to recombinant IgA1 indicated that the Cα 2 N-glycosylation site contained mostly biantennary glycans, while the tailpiece site, absent in IgG, contained mostly triantennary structures.
9442070	7	78	contain	contained	1202:1210	arg2	glycans					1231:1237	biantennary glycans	1219:1237	biantennary glycans	1219:1237	Analysis of the N-glycans attached to recombinant IgA1 indicated that the Cα 2 N-glycosylation site contained mostly biantennary glycans, while the tailpiece site, absent in IgG, contained mostly triantennary structures.
9442070	6	79	theme	O-linked	1059:1066	arg1	oligosaccharides					1068:1083	O-linked oligosaccharides	1059:1083	O-linked oligosaccharides	1059:1083	This paper contains the first report of Fab glycosylation in IgA1, and (in contrast to IgG Fab, which contains only N-linked glycans) both N- and O-linked oligosaccharides were identified.
9442070	11	80	theme	Fc	1810:1811	arg1	Fab					1827:1829	IgG1 Fc and mouse IgA Fab	1805:1829	IgG1 Fc and mouse IgA Fab	1805:1829	The primary sequence and disulfide bond pattern of IgA1, together with the crystal structures of IgG1 Fc and mouse IgA Fab and the glycan sequencing data, were used to generate a molecular model of IgA1.
9442070	1	81	theme	serum	145:149	arg1	immunoglobulins					151:165	The human serum immunoglobulins IgG and IgA1	135:178	The human serum immunoglobulins IgG and IgA1	135:178	The human serum immunoglobulins IgG and IgA1 are produced in bone marrow and both interact with specific cellular receptors that mediate biological events.
9442070	1	81	theme	serum	145:149	arg1	IgA1					175:178	IgA1	175:178	IgA1	175:178	The human serum immunoglobulins IgG and IgA1 are produced in bone marrow and both interact with specific cellular receptors that mediate biological events.
9442070	1	81	theme	serum	145:149	arg1	IgG					167:169	IgG	167:169	IgG	167:169	The human serum immunoglobulins IgG and IgA1 are produced in bone marrow and both interact with specific cellular receptors that mediate biological events.
9442070	7	82	from	absent	1266:1271	arg1	IgG					1276:1278	IgG	1276:1278	IgG	1276:1278	Analysis of the N-glycans attached to recombinant IgA1 indicated that the Cα 2 N-glycosylation site contained mostly biantennary glycans, while the tailpiece site, absent in IgG, contained mostly triantennary structures.
9442070	14	83	theme	IgA1	2322:2325	arg1	N-glycans					2327:2335	the IgA1 N-glycans	2318:2335	the IgA1 N-glycans	2318:2335	This also suggests why in contrast to IgG Fc, the IgA1 N-glycans are not undergalactosylated in rheumatoid arthritis.
9442070	13	84	theme	Fc	2196:2197	arg1	N-glycans					2199:2207	IgG Fc N-glycans	2192:2207	IgG Fc N-glycans	2192:2207	The accessibility of the Cα 2 N-glycans provides an explanation for the increased sialylation and galactosylation of IgA1 Fc over that of IgG Fc N-glycans, which are confined in the space between the two Cγ 2 domains.
9442070	9	85	theme	Neutrophil	1430:1439	arg1	studies					1455:1461	Neutrophil Fcα R binding studies	1430:1461	Neutrophil Fcα R binding studies	1430:1461	Neutrophil Fcα R binding studies, using recombinant IgA1, indicated that neither the tailpiece region nor the N-glycans in the C alpha 2 domain contribute to IgA1-neutrophil Fcα R binding.
9442070	7	86	from	IgG	1276:1278	arg1	absent					1266:1271	absent	1266:1271	absent	1266:1271	Analysis of the N-glycans attached to recombinant IgA1 indicated that the Cα 2 N-glycosylation site contained mostly biantennary glycans, while the tailpiece site, absent in IgG, contained mostly triantennary structures.
9442070	9	87	theme	tailpiece	1515:1523	arg1	region					1525:1530	the tailpiece region	1511:1530	the tailpiece region	1511:1530	Neutrophil Fcα R binding studies, using recombinant IgA1, indicated that neither the tailpiece region nor the N-glycans in the C alpha 2 domain contribute to IgA1-neutrophil Fcα R binding.
9442070	7	88	theme	biantennary	1219:1229	arg1	glycans					1231:1237	biantennary glycans	1219:1237	biantennary glycans	1219:1237	Analysis of the N-glycans attached to recombinant IgA1 indicated that the Cα 2 N-glycosylation site contained mostly biantennary glycans, while the tailpiece site, absent in IgG, contained mostly triantennary structures.
9442070	6	89	link	O-linked	1059:1066	arg1	oligosaccharides					1068:1083	O-linked oligosaccharides	1059:1083	O-linked oligosaccharides	1059:1083	This paper contains the first report of Fab glycosylation in IgA1, and (in contrast to IgG Fab, which contains only N-linked glycans) both N- and O-linked oligosaccharides were identified.
9442070	3	90	theme	IgA1	505:508	arg1	Fab					510:512	IgA1 Fab	505:512	IgA1 Fab	505:512	In this paper, we have analyzed the glycosylation of IgA1 and IgA1 Fab and Fc as well as three recombinant IgA1 molecules, including two N-glycosylation mutants.
9442070	14	91	theme	IgG	2310:2312	arg1	Fc					2314:2315	IgG Fc	2310:2315	IgG Fc	2310:2315	This also suggests why in contrast to IgG Fc, the IgA1 N-glycans are not undergalactosylated in rheumatoid arthritis.
9442070	11	92	theme	IgA	1823:1825	arg1	Fab					1827:1829	IgG1 Fc and mouse IgA Fab	1805:1829	IgG1 Fc and mouse IgA Fab	1805:1829	The primary sequence and disulfide bond pattern of IgA1, together with the crystal structures of IgG1 Fc and mouse IgA Fab and the glycan sequencing data, were used to generate a molecular model of IgA1.
9442070	13	93	gly	sialylation	2136:2146	arg1	Fc					2176:2177	IgA1 Fc	2171:2177	IgA1 Fc	2171:2177	The accessibility of the Cα 2 N-glycans provides an explanation for the increased sialylation and galactosylation of IgA1 Fc over that of IgG Fc N-glycans, which are confined in the space between the two Cγ 2 domains.
9442070	0	94	theme	receptor	112:119	arg1	interactions					121:132	Fcα receptor interactions	108:132	Fcα receptor interactions	108:132	The glycosylation and structure of human serum IgA1, Fab, and Fc regions and the role of N-glycosylation on Fcα receptor interactions.
9442070	3	95	theme	IgA1	496:499	arg1	glycosylation					479:491	the glycosylation	475:491	the glycosylation of IgA1 and IgA1 Fab and Fc as well as three recombinant IgA1 molecules, including two N-glycosylation mutants	475:602	In this paper, we have analyzed the glycosylation of IgA1 and IgA1 Fab and Fc as well as three recombinant IgA1 molecules, including two N-glycosylation mutants.
9442070	3	95	theme	IgA1	496:499	arg1	mutants					596:602	two N-glycosylation mutants	576:602	two N-glycosylation mutants	576:602	In this paper, we have analyzed the glycosylation of IgA1 and IgA1 Fab and Fc as well as three recombinant IgA1 molecules, including two N-glycosylation mutants.
9442070	3	95	theme	IgA1	496:499	arg1	molecules					555:563	three recombinant IgA1 molecules	532:563	three recombinant IgA1 molecules	532:563	In this paper, we have analyzed the glycosylation of IgA1 and IgA1 Fab and Fc as well as three recombinant IgA1 molecules, including two N-glycosylation mutants.
9442070	4	96	from	Ser230	723:728	arg1	located					704:710	located	704:710	located	704:710	Amino acid sequencing data of the IgA1 Fc O-glycosylated hinge region indicated that O-glycans are located at Thr228, Ser230, and Ser232, while O-glycan sites at Thr225 and Thr236 are partially occupied.
9442070	11	97	theme	data	1857:1860	arg1	structures					1791:1800	the crystal structures	1779:1800	the crystal structures of IgG1 Fc and mouse IgA Fab and the glycan sequencing data	1779:1860	The primary sequence and disulfide bond pattern of IgA1, together with the crystal structures of IgG1 Fc and mouse IgA Fab and the glycan sequencing data, were used to generate a molecular model of IgA1.
9442070	6	98	contain	contains	924:931	arg2	report					943:948	the first report	933:948	the first report of Fab glycosylation in IgA1	933:977	This paper contains the first report of Fab glycosylation in IgA1, and (in contrast to IgG Fab, which contains only N-linked glycans) both N- and O-linked oligosaccharides were identified.
9442070	6	98	contain	contains	924:931	arg1	paper					918:922	This paper	913:922	This paper	913:922	This paper contains the first report of Fab glycosylation in IgA1, and (in contrast to IgG Fab, which contains only N-linked glycans) both N- and O-linked oligosaccharides were identified.
9442070	7	99	theme	N-glycosylation	1181:1195	arg1	site					1197:1200	the Cα 2 N-glycosylation site	1172:1200	the Cα 2 N-glycosylation site	1172:1200	Analysis of the N-glycans attached to recombinant IgA1 indicated that the Cα 2 N-glycosylation site contained mostly biantennary glycans, while the tailpiece site, absent in IgG, contained mostly triantennary structures.
9442070	4	100	theme	acid	611:614	arg1	data					627:630	Amino acid sequencing data	605:630	Amino acid sequencing data of the IgA1 Fc O-glycosylated hinge region	605:673	Amino acid sequencing data of the IgA1 Fc O-glycosylated hinge region indicated that O-glycans are located at Thr228, Ser230, and Ser232, while O-glycan sites at Thr225 and Thr236 are partially occupied.
9442070	4	101	from	Thr228	715:720	arg1	located					704:710	located	704:710	located	704:710	Amino acid sequencing data of the IgA1 Fc O-glycosylated hinge region indicated that O-glycans are located at Thr228, Ser230, and Ser232, while O-glycan sites at Thr225 and Thr236 are partially occupied.
9442070	11	102	theme	glycan	1839:1844	arg1	data					1857:1860	the glycan sequencing data	1835:1860	the glycan sequencing data	1835:1860	The primary sequence and disulfide bond pattern of IgA1, together with the crystal structures of IgG1 Fc and mouse IgA Fab and the glycan sequencing data, were used to generate a molecular model of IgA1.
9442070	7	103	theme	Cα	1176:1177	arg1	site					1197:1200	the Cα 2 N-glycosylation site	1172:1200	the Cα 2 N-glycosylation site	1172:1200	Analysis of the N-glycans attached to recombinant IgA1 indicated that the Cα 2 N-glycosylation site contained mostly biantennary glycans, while the tailpiece site, absent in IgG, contained mostly triantennary structures.
9442070	14	104	theme	rheumatoid	2368:2377	arg1	arthritis					2379:2387	rheumatoid arthritis	2368:2387	rheumatoid arthritis	2368:2387	This also suggests why in contrast to IgG Fc, the IgA1 N-glycans are not undergalactosylated in rheumatoid arthritis.
9442070	0	105	theme	Fab	53:55	arg1	role					81:84	the role	77:84	the role of N-glycosylation on Fcα receptor interactions	77:132	The glycosylation and structure of human serum IgA1, Fab, and Fc regions and the role of N-glycosylation on Fcα receptor interactions.
9442070	0	105	theme	Fab	53:55	arg1	structure					22:30	structure	22:30	structure	22:30	The glycosylation and structure of human serum IgA1, Fab, and Fc regions and the role of N-glycosylation on Fcα receptor interactions.
9442070	0	105	theme	Fab	53:55	arg1	glycosylation					4:16	glycosylation	4:16	glycosylation	4:16	The glycosylation and structure of human serum IgA1, Fab, and Fc regions and the role of N-glycosylation on Fcα receptor interactions.
9442070	5	106	theme	sialic	900:905	arg1	acid					907:910	sialic acid	900:910	sialic acid	900:910	Over 90% of the N-glycans in IgA1 were sialylated, in contrast to IgG, where < 10% contain sialic acid.
9442070	7	107	contain	contained	1281:1289	arg2	structures					1311:1320	triantennary structures	1298:1320	triantennary structures	1298:1320	Analysis of the N-glycans attached to recombinant IgA1 indicated that the Cα 2 N-glycosylation site contained mostly biantennary glycans, while the tailpiece site, absent in IgG, contained mostly triantennary structures.
9442070	7	107	contain	contained	1281:1289	arg1	site					1260:1263	the tailpiece site	1246:1263	the tailpiece site	1246:1263	Analysis of the N-glycans attached to recombinant IgA1 indicated that the Cα 2 N-glycosylation site contained mostly biantennary glycans, while the tailpiece site, absent in IgG, contained mostly triantennary structures.
9442070	9	108	theme	alpha	1559:1563	arg1	domain					1567:1572	the C alpha 2 domain	1553:1572	the C alpha 2 domain	1553:1572	Neutrophil Fcα R binding studies, using recombinant IgA1, indicated that neither the tailpiece region nor the N-glycans in the C alpha 2 domain contribute to IgA1-neutrophil Fcα R binding.
9442070	0	109	from	structure	22:30	arg1	interactions					121:132	Fcα receptor interactions	108:132	Fcα receptor interactions	108:132	The glycosylation and structure of human serum IgA1, Fab, and Fc regions and the role of N-glycosylation on Fcα receptor interactions.
9442070	4	110	used	occupied	799:806	arg2	Thr225					767:772	Thr225	767:772	Thr225	767:772	Amino acid sequencing data of the IgA1 Fc O-glycosylated hinge region indicated that O-glycans are located at Thr228, Ser230, and Ser232, while O-glycan sites at Thr225 and Thr236 are partially occupied.
9442070	4	110	used	occupied	799:806	arg2	sites					758:762	O-glycan sites	749:762	O-glycan sites at Thr225 and Thr236	749:783	Amino acid sequencing data of the IgA1 Fc O-glycosylated hinge region indicated that O-glycans are located at Thr228, Ser230, and Ser232, while O-glycan sites at Thr225 and Thr236 are partially occupied.
9442070	4	110	used	occupied	799:806	arg2	Thr236					778:783	Thr236	778:783	Thr236	778:783	Amino acid sequencing data of the IgA1 Fc O-glycosylated hinge region indicated that O-glycans are located at Thr228, Ser230, and Ser232, while O-glycan sites at Thr225 and Thr236 are partially occupied.
9442070	0	111	from	glycosylation	4:16	arg1	interactions					121:132	Fcα receptor interactions	108:132	Fcα receptor interactions	108:132	The glycosylation and structure of human serum IgA1, Fab, and Fc regions and the role of N-glycosylation on Fcα receptor interactions.
9442070	0	112	theme	regions	65:71	arg1	role					81:84	the role	77:84	the role of N-glycosylation on Fcα receptor interactions	77:132	The glycosylation and structure of human serum IgA1, Fab, and Fc regions and the role of N-glycosylation on Fcα receptor interactions.
9442070	0	112	theme	regions	65:71	arg1	structure					22:30	structure	22:30	structure	22:30	The glycosylation and structure of human serum IgA1, Fab, and Fc regions and the role of N-glycosylation on Fcα receptor interactions.
9442070	0	112	theme	regions	65:71	arg1	glycosylation					4:16	glycosylation	4:16	glycosylation	4:16	The glycosylation and structure of human serum IgA1, Fab, and Fc regions and the role of N-glycosylation on Fcα receptor interactions.
9442070	13	113	theme	Cα	2079:2080	arg1	N-glycans					2084:2092	the Cα 2 N-glycans	2075:2092	the Cα 2 N-glycans	2075:2092	The accessibility of the Cα 2 N-glycans provides an explanation for the increased sialylation and galactosylation of IgA1 Fc over that of IgG Fc N-glycans, which are confined in the space between the two Cγ 2 domains.
9442070	12	114	theme	bond	1966:1969	arg1	pattern					1971:1977	S-S bond pattern	1962:1977	S-S bond pattern	1962:1977	As a consequence of both the primary sequence and S-S bond pattern, the N-glycans in IgA1 Fc are not confined within the inter-α-chain space.
9442070	12	115	theme	S-S	1962:1964	arg1	pattern					1971:1977	S-S bond pattern	1962:1977	S-S bond pattern	1962:1977	As a consequence of both the primary sequence and S-S bond pattern, the N-glycans in IgA1 Fc are not confined within the inter-α-chain space.
9442070	4	116	theme	hinge	662:666	arg1	region					668:673	the IgA1 Fc O-glycosylated hinge region	635:673	the IgA1 Fc O-glycosylated hinge region	635:673	Amino acid sequencing data of the IgA1 Fc O-glycosylated hinge region indicated that O-glycans are located at Thr228, Ser230, and Ser232, while O-glycan sites at Thr225 and Thr236 are partially occupied.
9442070	12	117	from	N-glycans	1984:1992	arg1	Fc					2002:2003	IgA1 Fc	1997:2003	IgA1 Fc	1997:2003	As a consequence of both the primary sequence and S-S bond pattern, the N-glycans in IgA1 Fc are not confined within the inter-α-chain space.
9442070	13	118	theme	IgA1	2171:2174	arg1	Fc					2176:2177	IgA1 Fc	2171:2177	IgA1 Fc	2171:2177	The accessibility of the Cα 2 N-glycans provides an explanation for the increased sialylation and galactosylation of IgA1 Fc over that of IgG Fc N-glycans, which are confined in the space between the two Cγ 2 domains.
9442070	7	119	theme	recombinant	1140:1150	arg1	IgA1					1152:1155	recombinant IgA1	1140:1155	recombinant IgA1	1140:1155	Analysis of the N-glycans attached to recombinant IgA1 indicated that the Cα 2 N-glycosylation site contained mostly biantennary glycans, while the tailpiece site, absent in IgG, contained mostly triantennary structures.
9442070	9	120	theme	Fcα	1604:1606	arg1	R					1608:1608	IgA1-neutrophil Fcα R	1588:1608	IgA1-neutrophil Fcα R binding	1588:1616	Neutrophil Fcα R binding studies, using recombinant IgA1, indicated that neither the tailpiece region nor the N-glycans in the C alpha 2 domain contribute to IgA1-neutrophil Fcα R binding.
9442070	12	121	theme	IgA1	1997:2000	arg1	Fc					2002:2003	IgA1 Fc	1997:2003	IgA1 Fc	1997:2003	As a consequence of both the primary sequence and S-S bond pattern, the N-glycans in IgA1 Fc are not confined within the inter-α-chain space.
9442070	12	122	theme	pattern	1971:1977	arg1	consequence					1917:1927	a consequence	1915:1927	a consequence of both the primary sequence and S-S bond pattern	1915:1977	As a consequence of both the primary sequence and S-S bond pattern, the N-glycans in IgA1 Fc are not confined within the inter-α-chain space.
9442070	12	122	theme	pattern	1971:1977	arg1	N-glycans					1984:1992	the N-glycans	1980:1992	the N-glycans in IgA1 Fc	1980:2003	As a consequence of both the primary sequence and S-S bond pattern, the N-glycans in IgA1 Fc are not confined within the inter-α-chain space.
9442070	2	123	theme	various	391:397	arg1	receptors					402:410	various Fc receptors	391:410	various Fc receptors (Fc Rs)	391:418	In contrast to IgA1, the glycosylation of IgG has been well characterized, and its interaction with various Fc receptors (Fc Rs) has been well studied.
9442070	2	123	theme	various	391:397	arg1	Rs					416:417	Fc Rs	413:417	Fc Rs	413:417	In contrast to IgA1, the glycosylation of IgG has been well characterized, and its interaction with various Fc receptors (Fc Rs) has been well studied.
9442070	8	124	theme	processing	1369:1378	arg1	site					1406:1409	processing at one Fc N-glycosylation site	1369:1409	processing at one Fc N-glycosylation site	1369:1409	Further analysis of these data suggested that processing at one Fc N-glycosylation site affects the other.
9442070	10	125	theme	Fc	1665:1666	arg1	N-glycans					1668:1676	the Fc N-glycans	1661:1676	the Fc N-glycans	1661:1676	This contrasts with IgG, where removal of the Fc N-glycans reduces binding to the Fcγ R.
9442070	2	126	theme	IgG	333:335	arg1	glycosylation					316:328	the glycosylation	312:328	the glycosylation of IgG	312:335	In contrast to IgA1, the glycosylation of IgG has been well characterized, and its interaction with various Fc receptors (Fc Rs) has been well studied.
9442070	1	127	theme	cellular	240:247	arg1	receptors					249:257	specific cellular receptors	231:257	specific cellular receptors that mediate biological events	231:288	The human serum immunoglobulins IgG and IgA1 are produced in bone marrow and both interact with specific cellular receptors that mediate biological events.
9442070	11	128	theme	bond	1743:1746	arg1	pattern					1748:1754	disulfide bond pattern	1733:1754	disulfide bond pattern	1733:1754	The primary sequence and disulfide bond pattern of IgA1, together with the crystal structures of IgG1 Fc and mouse IgA Fab and the glycan sequencing data, were used to generate a molecular model of IgA1.
9442070	11	129	theme	IgA1	1906:1909	arg1	model					1897:1901	a molecular model	1885:1901	a molecular model of IgA1	1885:1909	The primary sequence and disulfide bond pattern of IgA1, together with the crystal structures of IgG1 Fc and mouse IgA Fab and the glycan sequencing data, were used to generate a molecular model of IgA1.
9442070	3	130	theme	recombinant	538:548	arg1	mutants					596:602	two N-glycosylation mutants	576:602	two N-glycosylation mutants	576:602	In this paper, we have analyzed the glycosylation of IgA1 and IgA1 Fab and Fc as well as three recombinant IgA1 molecules, including two N-glycosylation mutants.
9442070	3	130	theme	recombinant	538:548	arg1	molecules					555:563	three recombinant IgA1 molecules	532:563	three recombinant IgA1 molecules	532:563	In this paper, we have analyzed the glycosylation of IgA1 and IgA1 Fab and Fc as well as three recombinant IgA1 molecules, including two N-glycosylation mutants.
9442070	4	131	theme	Fc	644:645	arg1	region					668:673	the IgA1 Fc O-glycosylated hinge region	635:673	the IgA1 Fc O-glycosylated hinge region	635:673	Amino acid sequencing data of the IgA1 Fc O-glycosylated hinge region indicated that O-glycans are located at Thr228, Ser230, and Ser232, while O-glycan sites at Thr225 and Thr236 are partially occupied.
9442070	0	132	theme	human	35:39	arg1	IgA1					47:50	human serum IgA1	35:50	human serum IgA1	35:50	The glycosylation and structure of human serum IgA1, Fab, and Fc regions and the role of N-glycosylation on Fcα receptor interactions.
9442070	2	133	theme	Fc	413:414	arg1	receptors					402:410	various Fc receptors	391:410	various Fc receptors (Fc Rs)	391:418	In contrast to IgA1, the glycosylation of IgG has been well characterized, and its interaction with various Fc receptors (Fc Rs) has been well studied.
9442070	2	133	theme	Fc	413:414	arg1	Rs					416:417	Fc Rs	413:417	Fc Rs	413:417	In contrast to IgA1, the glycosylation of IgG has been well characterized, and its interaction with various Fc receptors (Fc Rs) has been well studied.
9442070	8	134	theme	N-glycosylation	1390:1404	arg1	site					1406:1409	processing at one Fc N-glycosylation site	1369:1409	processing at one Fc N-glycosylation site	1369:1409	Further analysis of these data suggested that processing at one Fc N-glycosylation site affects the other.
9442070	1	135	dep	immunoglobulins	151:165	arg1	immunoglobulins					151:165	The human serum immunoglobulins IgG and IgA1	135:178	The human serum immunoglobulins IgG and IgA1	135:178	The human serum immunoglobulins IgG and IgA1 are produced in bone marrow and both interact with specific cellular receptors that mediate biological events.
9442070	1	135	dep	immunoglobulins	151:165	arg1	IgA1					175:178	IgA1	175:178	IgA1	175:178	The human serum immunoglobulins IgG and IgA1 are produced in bone marrow and both interact with specific cellular receptors that mediate biological events.
9442070	1	135	dep	immunoglobulins	151:165	arg1	IgG					167:169	IgG	167:169	IgG	167:169	The human serum immunoglobulins IgG and IgA1 are produced in bone marrow and both interact with specific cellular receptors that mediate biological events.
9442070	0	136	theme	IgA1	47:50	arg1	role					81:84	the role	77:84	the role of N-glycosylation on Fcα receptor interactions	77:132	The glycosylation and structure of human serum IgA1, Fab, and Fc regions and the role of N-glycosylation on Fcα receptor interactions.
9442070	0	136	theme	IgA1	47:50	arg1	structure					22:30	structure	22:30	structure	22:30	The glycosylation and structure of human serum IgA1, Fab, and Fc regions and the role of N-glycosylation on Fcα receptor interactions.
9442070	0	136	theme	IgA1	47:50	arg1	glycosylation					4:16	glycosylation	4:16	glycosylation	4:16	The glycosylation and structure of human serum IgA1, Fab, and Fc regions and the role of N-glycosylation on Fcα receptor interactions.
9442070	1	137	theme	biological	272:281	arg1	events					283:288	biological events	272:288	biological events	272:288	The human serum immunoglobulins IgG and IgA1 are produced in bone marrow and both interact with specific cellular receptors that mediate biological events.
9442070	13	138	theme	N-glycans	2084:2092	arg1	accessibility					2058:2070	The accessibility	2054:2070	The accessibility of the Cα 2 N-glycans	2054:2092	The accessibility of the Cα 2 N-glycans provides an explanation for the increased sialylation and galactosylation of IgA1 Fc over that of IgG Fc N-glycans, which are confined in the space between the two Cγ 2 domains.
9442070	9	139	theme	Fcα	1441:1443	arg1	studies					1455:1461	Neutrophil Fcα R binding studies	1430:1461	Neutrophil Fcα R binding studies	1430:1461	Neutrophil Fcα R binding studies, using recombinant IgA1, indicated that neither the tailpiece region nor the N-glycans in the C alpha 2 domain contribute to IgA1-neutrophil Fcα R binding.
9442070	6	140	theme	Fab	953:955	arg1	glycosylation					957:969	Fab glycosylation	953:969	Fab glycosylation	953:969	This paper contains the first report of Fab glycosylation in IgA1, and (in contrast to IgG Fab, which contains only N-linked glycans) both N- and O-linked oligosaccharides were identified.
9442070	10	141	theme	N-glycans	1668:1676	arg1	removal					1650:1656	removal	1650:1656	removal of the Fc N-glycans	1650:1676	This contrasts with IgG, where removal of the Fc N-glycans reduces binding to the Fcγ R.
9442070	5	142	from	%	816:816	arg1	IgA1					838:841	IgA1	838:841	IgA1	838:841	Over 90% of the N-glycans in IgA1 were sialylated, in contrast to IgG, where < 10% contain sialic acid.
9442070	6	143	from	oligosaccharides	1068:1083	arg1	contrast					988:995	contrast	988:995	contrast	988:995	This paper contains the first report of Fab glycosylation in IgA1, and (in contrast to IgG Fab, which contains only N-linked glycans) both N- and O-linked oligosaccharides were identified.
9442070	0	144	dep	glycosylation	4:16	arg1	The					0:2	The	0:2	The	0:2	The glycosylation and structure of human serum IgA1, Fab, and Fc regions and the role of N-glycosylation on Fcα receptor interactions.
9442070	6	145	from	report	943:948	arg1	IgA1					974:977	IgA1	974:977	IgA1	974:977	This paper contains the first report of Fab glycosylation in IgA1, and (in contrast to IgG Fab, which contains only N-linked glycans) both N- and O-linked oligosaccharides were identified.
9442070	9	146	theme	R	1608:1608	arg1	binding					1610:1616	IgA1-neutrophil Fcα R binding	1588:1616	IgA1-neutrophil Fcα R binding	1588:1616	Neutrophil Fcα R binding studies, using recombinant IgA1, indicated that neither the tailpiece region nor the N-glycans in the C alpha 2 domain contribute to IgA1-neutrophil Fcα R binding.
29301793	4	0	theme	tumor	679:683	arg1	suppressor					685:694	the FOXO tumor suppressor	670:694	the FOXO tumor suppressor	670:694	Overexpression of either O-GlcNAcylated FOXO3 (FOX-OV) or a Ser-to-Ala mutant (S284A) in PANC-1 cells indicated that S284 O-GlcNAc acts as a critical block of the FOXO tumor suppressor and induces proliferation in PANC-1 cancer cells by stimulating the MDM2-p53-p21 axis.
29301793	4	1	theme	FOXO	674:677	arg1	suppressor					685:694	the FOXO tumor suppressor	670:694	the FOXO tumor suppressor	670:694	Overexpression of either O-GlcNAcylated FOXO3 (FOX-OV) or a Ser-to-Ala mutant (S284A) in PANC-1 cells indicated that S284 O-GlcNAc acts as a critical block of the FOXO tumor suppressor and induces proliferation in PANC-1 cancer cells by stimulating the MDM2-p53-p21 axis.
29301793	4	2	theme	mutant	582:587	arg1	Overexpression					511:524	Overexpression	511:524	Overexpression of either O-GlcNAcylated FOXO3 (FOX-OV) or a Ser-to-Ala mutant (S284A) in PANC-1 cells	511:611	Overexpression of either O-GlcNAcylated FOXO3 (FOX-OV) or a Ser-to-Ala mutant (S284A) in PANC-1 cells indicated that S284 O-GlcNAc acts as a critical block of the FOXO tumor suppressor and induces proliferation in PANC-1 cancer cells by stimulating the MDM2-p53-p21 axis.
29301793	3	3	theme	O-GlcNAcylation	343:357	arg1	sites					359:363	seven O-GlcNAcylation sites	337:363	seven O-GlcNAcylation sites identified within the FOXO3 transactivation domain	337:414	Of seven O-GlcNAcylation sites identified within the FOXO3 transactivation domain, we found that changes in O-GlcNAcylation at Ser284 modulated p21-mediated cancer cell growth.
29301793	4	4	from	Overexpression	511:524	arg1	cells					607:611	PANC-1 cells	600:611	PANC-1 cells	600:611	Overexpression of either O-GlcNAcylated FOXO3 (FOX-OV) or a Ser-to-Ala mutant (S284A) in PANC-1 cells indicated that S284 O-GlcNAc acts as a critical block of the FOXO tumor suppressor and induces proliferation in PANC-1 cancer cells by stimulating the MDM2-p53-p21 axis.
29301793	2	5	theme	pathway	283:289	arg1	part					267:270	a part	265:270	a part of the p53 pathway	265:289	Here, we identify site-specific O-GlcNAcylation as a critical block of FOXO3 that may abrogate a part of the p53 pathway, resulting in aberrant cancer cell growth.
29301793	4	6	theme	cancer	732:737	arg1	cells					739:743	PANC-1 cancer cells	725:743	PANC-1 cancer cells	725:743	Overexpression of either O-GlcNAcylated FOXO3 (FOX-OV) or a Ser-to-Ala mutant (S284A) in PANC-1 cells indicated that S284 O-GlcNAc acts as a critical block of the FOXO tumor suppressor and induces proliferation in PANC-1 cancer cells by stimulating the MDM2-p53-p21 axis.
29301793	3	7	theme	transactivation	393:407	arg1	domain					409:414	the FOXO3 transactivation domain	383:414	the FOXO3 transactivation domain	383:414	Of seven O-GlcNAcylation sites identified within the FOXO3 transactivation domain, we found that changes in O-GlcNAcylation at Ser284 modulated p21-mediated cancer cell growth.
29301793	2	8	theme	aberrant	305:312	arg1	growth					326:331	aberrant cancer cell growth	305:331	aberrant cancer cell growth	305:331	Here, we identify site-specific O-GlcNAcylation as a critical block of FOXO3 that may abrogate a part of the p53 pathway, resulting in aberrant cancer cell growth.
29301793	2	9	theme	p53	279:281	arg1	pathway					283:289	the p53 pathway	275:289	the p53 pathway	275:289	Here, we identify site-specific O-GlcNAcylation as a critical block of FOXO3 that may abrogate a part of the p53 pathway, resulting in aberrant cancer cell growth.
29301793	2	10	theme	cancer	314:319	arg1	growth					326:331	aberrant cancer cell growth	305:331	aberrant cancer cell growth	305:331	Here, we identify site-specific O-GlcNAcylation as a critical block of FOXO3 that may abrogate a part of the p53 pathway, resulting in aberrant cancer cell growth.
29301793	3	11	theme	cell	498:501	arg1	growth					503:508	p21-mediated cancer cell growth	478:508	p21-mediated cancer cell growth	478:508	Of seven O-GlcNAcylation sites identified within the FOXO3 transactivation domain, we found that changes in O-GlcNAcylation at Ser284 modulated p21-mediated cancer cell growth.
29301793	6	12	theme	cancer	1068:1073	arg1	growth					1080:1085	subsequent cancer cell growth	1057:1085	subsequent cancer cell growth	1057:1085	Thus, our study provides evidence to support a role for S284 O-GlcNAc as a critical block of FOXO3 to induce subsequent cancer cell growth via abrogation of the p53 regulatory circuit.Significance: These findings highlight a posttranslational mechanism for indirect abrogation of the p53 pathway, one that may occur with some frequency in human cancer cells.
29301793	4	13	theme	PANC-1	725:730	arg1	cells					739:743	PANC-1 cancer cells	725:743	PANC-1 cancer cells	725:743	Overexpression of either O-GlcNAcylated FOXO3 (FOX-OV) or a Ser-to-Ala mutant (S284A) in PANC-1 cells indicated that S284 O-GlcNAc acts as a critical block of the FOXO tumor suppressor and induces proliferation in PANC-1 cancer cells by stimulating the MDM2-p53-p21 axis.
29301793	4	14	theme	MDM2-p53-p21	764:775	arg1	axis					777:780	the MDM2-p53-p21 axis	760:780	the MDM2-p53-p21 axis	760:780	Overexpression of either O-GlcNAcylated FOXO3 (FOX-OV) or a Ser-to-Ala mutant (S284A) in PANC-1 cells indicated that S284 O-GlcNAc acts as a critical block of the FOXO tumor suppressor and induces proliferation in PANC-1 cancer cells by stimulating the MDM2-p53-p21 axis.
29301793	5	15	theme	mRNA	923:926	arg1	levels					940:945	both the mRNA and protein levels	914:945	levels	940:945	Furthermore, S284A mutant cells lacking S284 O-GlcNAc and FOX-OV cells exhibited opposing MDM2-p53-p21 axis expression patterns at both the mRNA and protein levels.
29301793	6	16	theme	critical	1023:1030	arg1	block					1032:1036	a critical block	1021:1036	a critical block of FOXO3 to induce subsequent cancer cell growth via abrogation of the p53 regulatory circuit.Significance	1021:1143	Thus, our study provides evidence to support a role for S284 O-GlcNAc as a critical block of FOXO3 to induce subsequent cancer cell growth via abrogation of the p53 regulatory circuit.Significance: These findings highlight a posttranslational mechanism for indirect abrogation of the p53 pathway, one that may occur with some frequency in human cancer cells.
29301793	5	17	theme	protein	932:938	arg1	levels					940:945	both the mRNA and protein levels	914:945	levels	940:945	Furthermore, S284A mutant cells lacking S284 O-GlcNAc and FOX-OV cells exhibited opposing MDM2-p53-p21 axis expression patterns at both the mRNA and protein levels.
29301793	6	18	theme	subsequent	1057:1066	arg1	growth					1080:1085	subsequent cancer cell growth	1057:1085	subsequent cancer cell growth	1057:1085	Thus, our study provides evidence to support a role for S284 O-GlcNAc as a critical block of FOXO3 to induce subsequent cancer cell growth via abrogation of the p53 regulatory circuit.Significance: These findings highlight a posttranslational mechanism for indirect abrogation of the p53 pathway, one that may occur with some frequency in human cancer cells.
29301793	5	19	theme	S284A	796:800	arg1	cells					809:813	S284A mutant cells	796:813	S284A mutant cells lacking S284 O-GlcNAc and FOX-OV cells	796:852	Furthermore, S284A mutant cells lacking S284 O-GlcNAc and FOX-OV cells exhibited opposing MDM2-p53-p21 axis expression patterns at both the mRNA and protein levels.
29301793	1	20	theme	Posttranslational	84:100	arg1	modifications					102:114	Posttranslational modifications	84:114	Posttranslational modifications of tumor suppressors	84:135	Posttranslational modifications of tumor suppressors can induce abnormal cell growth.
29301793	6	21	theme	FOXO3	1041:1045	arg1	block					1032:1036	a critical block	1021:1036	a critical block of FOXO3 to induce subsequent cancer cell growth via abrogation of the p53 regulatory circuit.Significance	1021:1143	Thus, our study provides evidence to support a role for S284 O-GlcNAc as a critical block of FOXO3 to induce subsequent cancer cell growth via abrogation of the p53 regulatory circuit.Significance: These findings highlight a posttranslational mechanism for indirect abrogation of the p53 pathway, one that may occur with some frequency in human cancer cells.
29301793	5	22	theme	opposing	864:871	arg1	patterns					902:909	opposing MDM2-p53-p21 axis expression patterns	864:909	opposing MDM2-p53-p21 axis expression patterns at both the mRNA and protein levels	864:945	Furthermore, S284A mutant cells lacking S284 O-GlcNAc and FOX-OV cells exhibited opposing MDM2-p53-p21 axis expression patterns at both the mRNA and protein levels.
29301793	3	23	theme	FOXO3	387:391	arg1	domain					409:414	the FOXO3 transactivation domain	383:414	the FOXO3 transactivation domain	383:414	Of seven O-GlcNAcylation sites identified within the FOXO3 transactivation domain, we found that changes in O-GlcNAcylation at Ser284 modulated p21-mediated cancer cell growth.
29301793	6	24	theme	pathway	1236:1242	arg1	one					1245:1247	one	1245:1247	one	1245:1247	Thus, our study provides evidence to support a role for S284 O-GlcNAc as a critical block of FOXO3 to induce subsequent cancer cell growth via abrogation of the p53 regulatory circuit.Significance: These findings highlight a posttranslational mechanism for indirect abrogation of the p53 pathway, one that may occur with some frequency in human cancer cells.
29301793	6	24	theme	pathway	1236:1242	arg1	abrogation					1214:1223	indirect abrogation	1205:1223	indirect abrogation of the p53 pathway	1205:1242	Thus, our study provides evidence to support a role for S284 O-GlcNAc as a critical block of FOXO3 to induce subsequent cancer cell growth via abrogation of the p53 regulatory circuit.Significance: These findings highlight a posttranslational mechanism for indirect abrogation of the p53 pathway, one that may occur with some frequency in human cancer cells.
29301793	6	25	theme	circuit.Significance	1124:1143	arg1	abrogation					1091:1100	abrogation	1091:1100	abrogation of the p53 regulatory circuit.Significance	1091:1143	Thus, our study provides evidence to support a role for S284 O-GlcNAc as a critical block of FOXO3 to induce subsequent cancer cell growth via abrogation of the p53 regulatory circuit.Significance: These findings highlight a posttranslational mechanism for indirect abrogation of the p53 pathway, one that may occur with some frequency in human cancer cells.
29301793	4	26	theme	critical	652:659	arg1	O-GlcNAc					633:640	S284 O-GlcNAc	628:640	S284 O-GlcNAc	628:640	Overexpression of either O-GlcNAcylated FOXO3 (FOX-OV) or a Ser-to-Ala mutant (S284A) in PANC-1 cells indicated that S284 O-GlcNAc acts as a critical block of the FOXO tumor suppressor and induces proliferation in PANC-1 cancer cells by stimulating the MDM2-p53-p21 axis.
29301793	4	26	theme	critical	652:659	arg1	proliferation					708:720	proliferation	708:720	proliferation in PANC-1 cancer cells	708:743	Overexpression of either O-GlcNAcylated FOXO3 (FOX-OV) or a Ser-to-Ala mutant (S284A) in PANC-1 cells indicated that S284 O-GlcNAc acts as a critical block of the FOXO tumor suppressor and induces proliferation in PANC-1 cancer cells by stimulating the MDM2-p53-p21 axis.
29301793	4	26	theme	critical	652:659	arg1	block					661:665	a critical block	650:665	a critical block of the FOXO tumor suppressor	650:694	Overexpression of either O-GlcNAcylated FOXO3 (FOX-OV) or a Ser-to-Ala mutant (S284A) in PANC-1 cells indicated that S284 O-GlcNAc acts as a critical block of the FOXO tumor suppressor and induces proliferation in PANC-1 cancer cells by stimulating the MDM2-p53-p21 axis.
29301793	0	27	theme	Tumor	23:27	arg1	FOXO3					40:44	the Tumor Suppressor FOXO3	19:44	the Tumor Suppressor FOXO3	19:44	O-GlcNAcylation of the Tumor Suppressor FOXO3 Triggers Aberrant Cancer Cell Growth.
29301793	5	28	theme	mutant	802:807	arg1	cells					809:813	S284A mutant cells	796:813	S284A mutant cells lacking S284 O-GlcNAc and FOX-OV cells	796:852	Furthermore, S284A mutant cells lacking S284 O-GlcNAc and FOX-OV cells exhibited opposing MDM2-p53-p21 axis expression patterns at both the mRNA and protein levels.
29301793	7	29	dep	Res	1314:1316	arg1	1214-24					1326:1332	1214-24	1326:1332	1214-24	1326:1332	Cancer Res; 78(5); 1214-24.
29301793	7	29	dep	Res	1314:1316	arg1	Cancer					1307:1312	Cancer	1307:1312	Cancer	1307:1312	Cancer Res; 78(5); 1214-24.
29301793	6	30	theme	regulatory	1113:1122	arg1	circuit.Significance					1124:1143	the p53 regulatory circuit.Significance	1105:1143	the p53 regulatory circuit.Significance	1105:1143	Thus, our study provides evidence to support a role for S284 O-GlcNAc as a critical block of FOXO3 to induce subsequent cancer cell growth via abrogation of the p53 regulatory circuit.Significance: These findings highlight a posttranslational mechanism for indirect abrogation of the p53 pathway, one that may occur with some frequency in human cancer cells.
29301793	4	31	theme	S284	628:631	arg1	O-GlcNAc					633:640	S284 O-GlcNAc	628:640	S284 O-GlcNAc	628:640	Overexpression of either O-GlcNAcylated FOXO3 (FOX-OV) or a Ser-to-Ala mutant (S284A) in PANC-1 cells indicated that S284 O-GlcNAc acts as a critical block of the FOXO tumor suppressor and induces proliferation in PANC-1 cancer cells by stimulating the MDM2-p53-p21 axis.
29301793	4	31	theme	S284	628:631	arg1	proliferation					708:720	proliferation	708:720	proliferation in PANC-1 cancer cells	708:743	Overexpression of either O-GlcNAcylated FOXO3 (FOX-OV) or a Ser-to-Ala mutant (S284A) in PANC-1 cells indicated that S284 O-GlcNAc acts as a critical block of the FOXO tumor suppressor and induces proliferation in PANC-1 cancer cells by stimulating the MDM2-p53-p21 axis.
29301793	4	31	theme	S284	628:631	arg1	block					661:665	a critical block	650:665	a critical block of the FOXO tumor suppressor	650:694	Overexpression of either O-GlcNAcylated FOXO3 (FOX-OV) or a Ser-to-Ala mutant (S284A) in PANC-1 cells indicated that S284 O-GlcNAc acts as a critical block of the FOXO tumor suppressor and induces proliferation in PANC-1 cancer cells by stimulating the MDM2-p53-p21 axis.
29301793	4	32	theme	Ser-to-Ala	571:580	arg1	S284A					590:594	S284A	590:594	S284A	590:594	Overexpression of either O-GlcNAcylated FOXO3 (FOX-OV) or a Ser-to-Ala mutant (S284A) in PANC-1 cells indicated that S284 O-GlcNAc acts as a critical block of the FOXO tumor suppressor and induces proliferation in PANC-1 cancer cells by stimulating the MDM2-p53-p21 axis.
29301793	4	32	theme	Ser-to-Ala	571:580	arg1	mutant					582:587	a Ser-to-Ala mutant	569:587	a Ser-to-Ala mutant (S284A)	569:595	Overexpression of either O-GlcNAcylated FOXO3 (FOX-OV) or a Ser-to-Ala mutant (S284A) in PANC-1 cells indicated that S284 O-GlcNAc acts as a critical block of the FOXO tumor suppressor and induces proliferation in PANC-1 cancer cells by stimulating the MDM2-p53-p21 axis.
29301793	2	33	theme	site-specific	188:200	arg1	block					232:236	a critical block	221:236	a critical block of FOXO3 that may abrogate a part of the p53 pathway	221:289	Here, we identify site-specific O-GlcNAcylation as a critical block of FOXO3 that may abrogate a part of the p53 pathway, resulting in aberrant cancer cell growth.
29301793	2	33	theme	site-specific	188:200	arg1	O-GlcNAcylation					202:216	site-specific O-GlcNAcylation	188:216	site-specific O-GlcNAcylation	188:216	Here, we identify site-specific O-GlcNAcylation as a critical block of FOXO3 that may abrogate a part of the p53 pathway, resulting in aberrant cancer cell growth.
29301793	1	34	theme	tumor	119:123	arg1	suppressors					125:135	tumor suppressors	119:135	tumor suppressors	119:135	Posttranslational modifications of tumor suppressors can induce abnormal cell growth.
29301793	5	35	theme	axis	886:889	arg1	patterns					902:909	opposing MDM2-p53-p21 axis expression patterns	864:909	opposing MDM2-p53-p21 axis expression patterns at both the mRNA and protein levels	864:945	Furthermore, S284A mutant cells lacking S284 O-GlcNAc and FOX-OV cells exhibited opposing MDM2-p53-p21 axis expression patterns at both the mRNA and protein levels.
29301793	0	36	theme	FOXO3	40:44	arg1	O-GlcNAcylation					0:14	O-GlcNAcylation	0:14	O-GlcNAcylation of the Tumor Suppressor FOXO3	0:44	O-GlcNAcylation of the Tumor Suppressor FOXO3 Triggers Aberrant Cancer Cell Growth.
29301793	6	37	theme	p53	1232:1234	arg1	pathway					1236:1242	the p53 pathway	1228:1242	the p53 pathway	1228:1242	Thus, our study provides evidence to support a role for S284 O-GlcNAc as a critical block of FOXO3 to induce subsequent cancer cell growth via abrogation of the p53 regulatory circuit.Significance: These findings highlight a posttranslational mechanism for indirect abrogation of the p53 pathway, one that may occur with some frequency in human cancer cells.
29301793	5	38	theme	MDM2-p53-p21	873:884	arg1	patterns					902:909	opposing MDM2-p53-p21 axis expression patterns	864:909	opposing MDM2-p53-p21 axis expression patterns at both the mRNA and protein levels	864:945	Furthermore, S284A mutant cells lacking S284 O-GlcNAc and FOX-OV cells exhibited opposing MDM2-p53-p21 axis expression patterns at both the mRNA and protein levels.
29301793	0	39	theme	Suppressor	29:38	arg1	FOXO3					40:44	the Tumor Suppressor FOXO3	19:44	the Tumor Suppressor FOXO3	19:44	O-GlcNAcylation of the Tumor Suppressor FOXO3 Triggers Aberrant Cancer Cell Growth.
29301793	4	40	theme	FOXO3	551:555	arg1	Overexpression					511:524	Overexpression	511:524	Overexpression of either O-GlcNAcylated FOXO3 (FOX-OV) or a Ser-to-Ala mutant (S284A) in PANC-1 cells	511:611	Overexpression of either O-GlcNAcylated FOXO3 (FOX-OV) or a Ser-to-Ala mutant (S284A) in PANC-1 cells indicated that S284 O-GlcNAc acts as a critical block of the FOXO tumor suppressor and induces proliferation in PANC-1 cancer cells by stimulating the MDM2-p53-p21 axis.
29301793	2	41	theme	FOXO3	241:245	arg1	block					232:236	a critical block	221:236	a critical block of FOXO3 that may abrogate a part of the p53 pathway	221:289	Here, we identify site-specific O-GlcNAcylation as a critical block of FOXO3 that may abrogate a part of the p53 pathway, resulting in aberrant cancer cell growth.
29301793	2	41	theme	FOXO3	241:245	arg1	O-GlcNAcylation					202:216	site-specific O-GlcNAcylation	188:216	site-specific O-GlcNAcylation	188:216	Here, we identify site-specific O-GlcNAcylation as a critical block of FOXO3 that may abrogate a part of the p53 pathway, resulting in aberrant cancer cell growth.
29301793	5	42	theme	FOX-OV	841:846	arg1	cells					848:852	FOX-OV cells	841:852	FOX-OV cells	841:852	Furthermore, S284A mutant cells lacking S284 O-GlcNAc and FOX-OV cells exhibited opposing MDM2-p53-p21 axis expression patterns at both the mRNA and protein levels.
29301793	0	43	theme	Aberrant	55:62	arg1	Growth					76:81	Aberrant Cancer Cell Growth	55:81	Aberrant Cancer Cell Growth	55:81	O-GlcNAcylation of the Tumor Suppressor FOXO3 Triggers Aberrant Cancer Cell Growth.
29301793	4	44	theme	O-GlcNAcylated	536:549	arg1	FOX-OV					558:563	FOX-OV	558:563	FOX-OV	558:563	Overexpression of either O-GlcNAcylated FOXO3 (FOX-OV) or a Ser-to-Ala mutant (S284A) in PANC-1 cells indicated that S284 O-GlcNAc acts as a critical block of the FOXO tumor suppressor and induces proliferation in PANC-1 cancer cells by stimulating the MDM2-p53-p21 axis.
29301793	4	44	theme	O-GlcNAcylated	536:549	arg1	FOXO3					551:555	O-GlcNAcylated FOXO3	536:555	O-GlcNAcylated FOXO3 (FOX-OV)	536:564	Overexpression of either O-GlcNAcylated FOXO3 (FOX-OV) or a Ser-to-Ala mutant (S284A) in PANC-1 cells indicated that S284 O-GlcNAc acts as a critical block of the FOXO tumor suppressor and induces proliferation in PANC-1 cancer cells by stimulating the MDM2-p53-p21 axis.
29301793	6	45	theme	cancer	1293:1298	arg1	cells					1300:1304	human cancer cells	1287:1304	human cancer cells	1287:1304	Thus, our study provides evidence to support a role for S284 O-GlcNAc as a critical block of FOXO3 to induce subsequent cancer cell growth via abrogation of the p53 regulatory circuit.Significance: These findings highlight a posttranslational mechanism for indirect abrogation of the p53 pathway, one that may occur with some frequency in human cancer cells.
29301793	1	46	theme	suppressors	125:135	arg1	modifications					102:114	Posttranslational modifications	84:114	Posttranslational modifications of tumor suppressors	84:135	Posttranslational modifications of tumor suppressors can induce abnormal cell growth.
29301793	6	47	theme	human	1287:1291	arg1	cells					1300:1304	human cancer cells	1287:1304	human cancer cells	1287:1304	Thus, our study provides evidence to support a role for S284 O-GlcNAc as a critical block of FOXO3 to induce subsequent cancer cell growth via abrogation of the p53 regulatory circuit.Significance: These findings highlight a posttranslational mechanism for indirect abrogation of the p53 pathway, one that may occur with some frequency in human cancer cells.
29301793	2	48	theme	critical	223:230	arg1	block					232:236	a critical block	221:236	a critical block of FOXO3 that may abrogate a part of the p53 pathway	221:289	Here, we identify site-specific O-GlcNAcylation as a critical block of FOXO3 that may abrogate a part of the p53 pathway, resulting in aberrant cancer cell growth.
29301793	2	48	theme	critical	223:230	arg1	O-GlcNAcylation					202:216	site-specific O-GlcNAcylation	188:216	site-specific O-GlcNAcylation	188:216	Here, we identify site-specific O-GlcNAcylation as a critical block of FOXO3 that may abrogate a part of the p53 pathway, resulting in aberrant cancer cell growth.
29301793	5	49	from	levels	940:945	arg1	patterns					902:909	opposing MDM2-p53-p21 axis expression patterns	864:909	opposing MDM2-p53-p21 axis expression patterns at both the mRNA and protein levels	864:945	Furthermore, S284A mutant cells lacking S284 O-GlcNAc and FOX-OV cells exhibited opposing MDM2-p53-p21 axis expression patterns at both the mRNA and protein levels.
29301793	3	50	from	Ser284	461:466	arg1	changes					431:437	changes	431:437	changes in O-GlcNAcylation at Ser284	431:466	Of seven O-GlcNAcylation sites identified within the FOXO3 transactivation domain, we found that changes in O-GlcNAcylation at Ser284 modulated p21-mediated cancer cell growth.
29301793	4	51	theme	suppressor	685:694	arg1	O-GlcNAc					633:640	S284 O-GlcNAc	628:640	S284 O-GlcNAc	628:640	Overexpression of either O-GlcNAcylated FOXO3 (FOX-OV) or a Ser-to-Ala mutant (S284A) in PANC-1 cells indicated that S284 O-GlcNAc acts as a critical block of the FOXO tumor suppressor and induces proliferation in PANC-1 cancer cells by stimulating the MDM2-p53-p21 axis.
29301793	4	51	theme	suppressor	685:694	arg1	proliferation					708:720	proliferation	708:720	proliferation in PANC-1 cancer cells	708:743	Overexpression of either O-GlcNAcylated FOXO3 (FOX-OV) or a Ser-to-Ala mutant (S284A) in PANC-1 cells indicated that S284 O-GlcNAc acts as a critical block of the FOXO tumor suppressor and induces proliferation in PANC-1 cancer cells by stimulating the MDM2-p53-p21 axis.
29301793	4	51	theme	suppressor	685:694	arg1	block					661:665	a critical block	650:665	a critical block of the FOXO tumor suppressor	650:694	Overexpression of either O-GlcNAcylated FOXO3 (FOX-OV) or a Ser-to-Ala mutant (S284A) in PANC-1 cells indicated that S284 O-GlcNAc acts as a critical block of the FOXO tumor suppressor and induces proliferation in PANC-1 cancer cells by stimulating the MDM2-p53-p21 axis.
29301793	4	52	from	proliferation	708:720	arg1	cells					739:743	PANC-1 cancer cells	725:743	PANC-1 cancer cells	725:743	Overexpression of either O-GlcNAcylated FOXO3 (FOX-OV) or a Ser-to-Ala mutant (S284A) in PANC-1 cells indicated that S284 O-GlcNAc acts as a critical block of the FOXO tumor suppressor and induces proliferation in PANC-1 cancer cells by stimulating the MDM2-p53-p21 axis.
29301793	6	53	theme	indirect	1205:1212	arg1	one					1245:1247	one	1245:1247	one	1245:1247	Thus, our study provides evidence to support a role for S284 O-GlcNAc as a critical block of FOXO3 to induce subsequent cancer cell growth via abrogation of the p53 regulatory circuit.Significance: These findings highlight a posttranslational mechanism for indirect abrogation of the p53 pathway, one that may occur with some frequency in human cancer cells.
29301793	6	53	theme	indirect	1205:1212	arg1	abrogation					1214:1223	indirect abrogation	1205:1223	indirect abrogation of the p53 pathway	1205:1242	Thus, our study provides evidence to support a role for S284 O-GlcNAc as a critical block of FOXO3 to induce subsequent cancer cell growth via abrogation of the p53 regulatory circuit.Significance: These findings highlight a posttranslational mechanism for indirect abrogation of the p53 pathway, one that may occur with some frequency in human cancer cells.
29301793	8	54	theme	©2018	1335:1339	arg1	AACR					1341:1344	©2018 AACR	1335:1344	©2018 AACR.	1335:1345	©2018 AACR.
29301793	2	55	theme	cell	321:324	arg1	growth					326:331	aberrant cancer cell growth	305:331	aberrant cancer cell growth	305:331	Here, we identify site-specific O-GlcNAcylation as a critical block of FOXO3 that may abrogate a part of the p53 pathway, resulting in aberrant cancer cell growth.
29301793	4	56	theme	PANC-1	600:605	arg1	cells					607:611	PANC-1 cells	600:611	PANC-1 cells	600:611	Overexpression of either O-GlcNAcylated FOXO3 (FOX-OV) or a Ser-to-Ala mutant (S284A) in PANC-1 cells indicated that S284 O-GlcNAc acts as a critical block of the FOXO tumor suppressor and induces proliferation in PANC-1 cancer cells by stimulating the MDM2-p53-p21 axis.
29301793	1	57	theme	abnormal	148:155	arg1	growth					162:167	abnormal cell growth	148:167	abnormal cell growth	148:167	Posttranslational modifications of tumor suppressors can induce abnormal cell growth.
29301793	3	58	theme	p21-mediated	478:489	arg1	growth					503:508	p21-mediated cancer cell growth	478:508	p21-mediated cancer cell growth	478:508	Of seven O-GlcNAcylation sites identified within the FOXO3 transactivation domain, we found that changes in O-GlcNAcylation at Ser284 modulated p21-mediated cancer cell growth.
29301793	0	59	theme	Cell	71:74	arg1	Growth					76:81	Aberrant Cancer Cell Growth	55:81	Aberrant Cancer Cell Growth	55:81	O-GlcNAcylation of the Tumor Suppressor FOXO3 Triggers Aberrant Cancer Cell Growth.
29301793	6	60	theme	cell	1075:1078	arg1	growth					1080:1085	subsequent cancer cell growth	1057:1085	subsequent cancer cell growth	1057:1085	Thus, our study provides evidence to support a role for S284 O-GlcNAc as a critical block of FOXO3 to induce subsequent cancer cell growth via abrogation of the p53 regulatory circuit.Significance: These findings highlight a posttranslational mechanism for indirect abrogation of the p53 pathway, one that may occur with some frequency in human cancer cells.
29301793	5	61	theme	S284	823:826	arg1	O-GlcNAc					828:835	S284 O-GlcNAc	823:835	S284 O-GlcNAc	823:835	Furthermore, S284A mutant cells lacking S284 O-GlcNAc and FOX-OV cells exhibited opposing MDM2-p53-p21 axis expression patterns at both the mRNA and protein levels.
29301793	1	62	theme	cell	157:160	arg1	growth					162:167	abnormal cell growth	148:167	abnormal cell growth	148:167	Posttranslational modifications of tumor suppressors can induce abnormal cell growth.
29301793	3	63	theme	cancer	491:496	arg1	growth					503:508	p21-mediated cancer cell growth	478:508	p21-mediated cancer cell growth	478:508	Of seven O-GlcNAcylation sites identified within the FOXO3 transactivation domain, we found that changes in O-GlcNAcylation at Ser284 modulated p21-mediated cancer cell growth.
29301793	0	64	theme	Cancer	64:69	arg1	Growth					76:81	Aberrant Cancer Cell Growth	55:81	Aberrant Cancer Cell Growth	55:81	O-GlcNAcylation of the Tumor Suppressor FOXO3 Triggers Aberrant Cancer Cell Growth.
29301793	6	65	theme	p53	1109:1111	arg1	circuit.Significance					1124:1143	the p53 regulatory circuit.Significance	1105:1143	the p53 regulatory circuit.Significance	1105:1143	Thus, our study provides evidence to support a role for S284 O-GlcNAc as a critical block of FOXO3 to induce subsequent cancer cell growth via abrogation of the p53 regulatory circuit.Significance: These findings highlight a posttranslational mechanism for indirect abrogation of the p53 pathway, one that may occur with some frequency in human cancer cells.
29301793	6	66	theme	posttranslational	1173:1189	arg1	mechanism					1191:1199	a posttranslational mechanism	1171:1199	a posttranslational mechanism for indirect abrogation of the p53 pathway, one that may occur with some frequency in human cancer cells	1171:1304	Thus, our study provides evidence to support a role for S284 O-GlcNAc as a critical block of FOXO3 to induce subsequent cancer cell growth via abrogation of the p53 regulatory circuit.Significance: These findings highlight a posttranslational mechanism for indirect abrogation of the p53 pathway, one that may occur with some frequency in human cancer cells.
29301793	3	67	from	changes	431:437	arg1	O-GlcNAcylation					442:456	O-GlcNAcylation	442:456	O-GlcNAcylation	442:456	Of seven O-GlcNAcylation sites identified within the FOXO3 transactivation domain, we found that changes in O-GlcNAcylation at Ser284 modulated p21-mediated cancer cell growth.
29301793	5	68	theme	expression	891:900	arg1	patterns					902:909	opposing MDM2-p53-p21 axis expression patterns	864:909	opposing MDM2-p53-p21 axis expression patterns at both the mRNA and protein levels	864:945	Furthermore, S284A mutant cells lacking S284 O-GlcNAc and FOX-OV cells exhibited opposing MDM2-p53-p21 axis expression patterns at both the mRNA and protein levels.
29301793	6	69	from	frequency	1274:1282	arg1	cells					1300:1304	human cancer cells	1287:1304	human cancer cells	1287:1304	Thus, our study provides evidence to support a role for S284 O-GlcNAc as a critical block of FOXO3 to induce subsequent cancer cell growth via abrogation of the p53 regulatory circuit.Significance: These findings highlight a posttranslational mechanism for indirect abrogation of the p53 pathway, one that may occur with some frequency in human cancer cells.
19690161	0	0	from	glycans	17:23	arg1	Asn-89					28:33	Asn-89	28:33	Asn-89 of Kaposi sarcoma herpes virus-encoded interleukin-6	28:86	Complex N-linked glycans on Asn-89 of Kaposi sarcoma herpes virus-encoded interleukin-6 mediate optimal function by affecting cytokine protein conformation.
19690161	7	1	theme	antibody	982:989	arg1	use					951:953	the use	947:953	the use of a conformation-specific antibody	947:989	With the use of a conformation-specific antibody and tryptic digestion assays, we showed that glycosylation at the Asn-89 site of vIL-6 affected protein conformation.
19690161	7	1	theme	antibody	982:989	arg1	digestion					1003:1011	tryptic digestion	995:1011	tryptic digestion	995:1011	With the use of a conformation-specific antibody and tryptic digestion assays, we showed that glycosylation at the Asn-89 site of vIL-6 affected protein conformation.
19690161	1	2	theme	herpesvirus-encoded	183:201	arg1	vIL-6					218:222	vIL-6	218:222	vIL-6	218:222	Kaposi sarcoma-associated herpesvirus-encoded interleukin-6 (vIL-6) and its human cellular homologue (huIL-6) share similar biological functions.
19690161	1	2	theme	herpesvirus-encoded	183:201	arg1	interleukin-6					203:215	Kaposi sarcoma-associated herpesvirus-encoded interleukin-6	157:215	Kaposi sarcoma-associated herpesvirus-encoded interleukin-6 (vIL-6)	157:223	Kaposi sarcoma-associated herpesvirus-encoded interleukin-6 (vIL-6) and its human cellular homologue (huIL-6) share similar biological functions.
19690161	1	3	theme	similar	273:279	arg1	functions					292:300	similar biological functions	273:300	similar biological functions	273:300	Kaposi sarcoma-associated herpesvirus-encoded interleukin-6 (vIL-6) and its human cellular homologue (huIL-6) share similar biological functions.
19690161	10	4	theme	complex	1370:1376	arg1	glycans					1387:1393	additional complex N-linked glycans	1359:1393	additional complex N-linked glycans	1359:1393	Two mutants of huIL-6, made to contain additional complex N-linked glycans in the region that interacts with IL-6Ralpha, did not confer binding to gp130 independently of IL-6Ralpha.
19690161	3	5	theme	vIL-6	512:516	arg1	vIL-6					512:516	vIL-6	512:516	vIL-6	512:516	Here we describe heterogeneity in the composition of the glycans of the two N-linked sites of vIL-6.
19690161	3	5	theme	vIL-6	512:516	arg1	sites					503:507	the two N-linked sites	486:507	the two N-linked sites of vIL-6	486:516	Here we describe heterogeneity in the composition of the glycans of the two N-linked sites of vIL-6.
19690161	1	6	theme	biological	281:290	arg1	functions					292:300	similar biological functions	273:300	similar biological functions	273:300	Kaposi sarcoma-associated herpesvirus-encoded interleukin-6 (vIL-6) and its human cellular homologue (huIL-6) share similar biological functions.
19690161	7	7	from	site	1064:1067	arg1	glycosylation					1036:1048	glycosylation	1036:1048	glycosylation at the Asn-89 site of vIL-6	1036:1076	With the use of a conformation-specific antibody and tryptic digestion assays, we showed that glycosylation at the Asn-89 site of vIL-6 affected protein conformation.
19690161	6	8	theme	intracellular	786:798	arg1	production					800:809	intracellular production	786:809	intracellular production of functional vIL-6	786:829	N-Linked glycosylation at the Asn-89 site was required for intracellular production of functional vIL-6, but endoglycosidase-mediated removal of N-linked glycans from secreted vIL-6 did not impair protein function.
19690161	4	9	theme	cytokine	578:585	arg1	function					587:594	optimal cytokine function	570:594	optimal cytokine function	570:594	The Asn-89 site of vIL-6, found to be required for optimal cytokine function, is composed of complex glycans.
19690161	0	10	theme	optimal	96:102	arg1	function					104:111	optimal function	96:111	optimal function	96:111	Complex N-linked glycans on Asn-89 of Kaposi sarcoma herpes virus-encoded interleukin-6 mediate optimal function by affecting cytokine protein conformation.
19690161	6	11	theme	secreted	894:901	arg1	vIL-6					903:907	secreted vIL-6	894:907	secreted vIL-6	894:907	N-Linked glycosylation at the Asn-89 site was required for intracellular production of functional vIL-6, but endoglycosidase-mediated removal of N-linked glycans from secreted vIL-6 did not impair protein function.
19690161	11	12	theme	vIL-6	1572:1576	arg1	Asn-89					1562:1567	Asn-89	1562:1567	Asn-89 of vIL-6	1562:1576	Our findings support the conclusion that complex glycans on Asn-89 of vIL-6 specifically promote a protein conformation that allows the viral cytokine to bind gp130 independently of IL-6Ralpha.
19690161	0	13	link	N-linked	8:15	arg1	glycans					17:23	Complex N-linked glycans	0:23	Complex N-linked glycans on Asn-89 of Kaposi sarcoma herpes virus-encoded interleukin-6	0:86	Complex N-linked glycans on Asn-89 of Kaposi sarcoma herpes virus-encoded interleukin-6 mediate optimal function by affecting cytokine protein conformation.
19690161	2	14	theme	vIL6	393:396	arg1	function					381:388	optimal function	373:388	optimal function of vIL6 but not huIL-6 (1)	373:415	Our previous work showed that N-linked glycosylation was required for optimal function of vIL6 but not huIL-6 (1).
19690161	11	15	theme	complex	1543:1549	arg1	glycans					1551:1557	complex glycans	1543:1557	complex glycans on Asn-89 of vIL-6	1543:1576	Our findings support the conclusion that complex glycans on Asn-89 of vIL-6 specifically promote a protein conformation that allows the viral cytokine to bind gp130 independently of IL-6Ralpha.
19690161	4	16	theme	optimal	570:576	arg1	function					587:594	optimal cytokine function	570:594	optimal cytokine function	570:594	The Asn-89 site of vIL-6, found to be required for optimal cytokine function, is composed of complex glycans.
19690161	5	17	theme	cytokine	708:715	arg1	function					717:724	cytokine function	708:724	cytokine function	708:724	The Asn-78 site is composed of high mannose glycans, which are dispensable for cytokine function.
19690161	7	18	theme	protein	1087:1093	arg1	conformation					1095:1106	protein conformation	1087:1106	protein conformation	1087:1106	With the use of a conformation-specific antibody and tryptic digestion assays, we showed that glycosylation at the Asn-89 site of vIL-6 affected protein conformation.
19690161	6	19	link	N-linked	872:879	arg1	glycans					881:887	N-linked glycans	872:887	N-linked glycans	872:887	N-Linked glycosylation at the Asn-89 site was required for intracellular production of functional vIL-6, but endoglycosidase-mediated removal of N-linked glycans from secreted vIL-6 did not impair protein function.
19690161	2	20	theme	previous	307:314	arg1	work					316:319	Our previous work	303:319	Our previous work	303:319	Our previous work showed that N-linked glycosylation was required for optimal function of vIL6 but not huIL-6 (1).
19690161	10	21	theme	huIL-6	1335:1340	arg1	mutants					1324:1330	Two mutants	1320:1330	Two mutants	1320:1330	Two mutants of huIL-6, made to contain additional complex N-linked glycans in the region that interacts with IL-6Ralpha, did not confer binding to gp130 independently of IL-6Ralpha.
19690161	6	22	theme	glycans	881:887	arg1	removal					861:867	endoglycosidase-mediated removal	836:867	endoglycosidase-mediated removal of N-linked glycans from secreted vIL-6	836:907	N-Linked glycosylation at the Asn-89 site was required for intracellular production of functional vIL-6, but endoglycosidase-mediated removal of N-linked glycans from secreted vIL-6 did not impair protein function.
19690161	6	23	gly	glycosylation	736:748	arg1	vIL-6					825:829	functional vIL-6	814:829	functional vIL-6	814:829	N-Linked glycosylation at the Asn-89 site was required for intracellular production of functional vIL-6, but endoglycosidase-mediated removal of N-linked glycans from secreted vIL-6 did not impair protein function.
19690161	6	23	gly	glycosylation	736:748	arg1	site					764:767	the Asn-89 site	753:767	the Asn-89 site	753:767	N-Linked glycosylation at the Asn-89 site was required for intracellular production of functional vIL-6, but endoglycosidase-mediated removal of N-linked glycans from secreted vIL-6 did not impair protein function.
19690161	6	23	gly	glycosylation	736:748	arg2	site					764:767	the Asn-89 site	753:767	the Asn-89 site	753:767	N-Linked glycosylation at the Asn-89 site was required for intracellular production of functional vIL-6, but endoglycosidase-mediated removal of N-linked glycans from secreted vIL-6 did not impair protein function.
19690161	11	24	theme	protein	1601:1607	arg1	conformation					1609:1620	a protein conformation	1599:1620	a protein conformation that allows the viral cytokine to bind gp130 independently of IL-6Ralpha	1599:1693	Our findings support the conclusion that complex glycans on Asn-89 of vIL-6 specifically promote a protein conformation that allows the viral cytokine to bind gp130 independently of IL-6Ralpha.
19690161	7	25	theme	tryptic	995:1001	arg1	digestion					1003:1011	tryptic digestion	995:1011	tryptic digestion	995:1011	With the use of a conformation-specific antibody and tryptic digestion assays, we showed that glycosylation at the Asn-89 site of vIL-6 affected protein conformation.
19690161	9	26	theme	complex	1219:1225	arg1	sufficient					1253:1262	sufficient	1253:1262	sufficient	1253:1262	We tested the hypothesis that the Asn-89 complex glycan of vIL-6 alone was sufficient to confer binding to gp130 independently of IL-6Ralpha.
19690161	9	26	theme	complex	1219:1225	arg1	glycan					1227:1232	the Asn-89 complex glycan	1208:1232	the Asn-89 complex glycan of vIL-6	1208:1241	We tested the hypothesis that the Asn-89 complex glycan of vIL-6 alone was sufficient to confer binding to gp130 independently of IL-6Ralpha.
19690161	0	27	theme	N-linked	8:15	arg1	glycans					17:23	Complex N-linked glycans	0:23	Complex N-linked glycans on Asn-89 of Kaposi sarcoma herpes virus-encoded interleukin-6	0:86	Complex N-linked glycans on Asn-89 of Kaposi sarcoma herpes virus-encoded interleukin-6 mediate optimal function by affecting cytokine protein conformation.
19690161	6	28	theme	N-linked	872:879	arg1	glycans					881:887	N-linked glycans	872:887	N-linked glycans	872:887	N-Linked glycosylation at the Asn-89 site was required for intracellular production of functional vIL-6, but endoglycosidase-mediated removal of N-linked glycans from secreted vIL-6 did not impair protein function.
19690161	7	29	theme	vIL-6	1072:1076	arg1	vIL-6					1072:1076	vIL-6	1072:1076	vIL-6	1072:1076	With the use of a conformation-specific antibody and tryptic digestion assays, we showed that glycosylation at the Asn-89 site of vIL-6 affected protein conformation.
19690161	7	29	theme	vIL-6	1072:1076	arg1	site					1064:1067	the Asn-89 site	1053:1067	the Asn-89 site of vIL-6	1053:1076	With the use of a conformation-specific antibody and tryptic digestion assays, we showed that glycosylation at the Asn-89 site of vIL-6 affected protein conformation.
19690161	0	30	theme	virus-encoded	60:72	arg1	interleukin-6					74:86	herpes virus-encoded interleukin-6	53:86	Kaposi sarcoma herpes virus-encoded interleukin-6	38:86	Complex N-linked glycans on Asn-89 of Kaposi sarcoma herpes virus-encoded interleukin-6 mediate optimal function by affecting cytokine protein conformation.
19690161	0	31	theme	Complex	0:6	arg1	glycans					17:23	Complex N-linked glycans	0:23	Complex N-linked glycans on Asn-89 of Kaposi sarcoma herpes virus-encoded interleukin-6	0:86	Complex N-linked glycans on Asn-89 of Kaposi sarcoma herpes virus-encoded interleukin-6 mediate optimal function by affecting cytokine protein conformation.
19690161	6	32	theme	Asn-89	757:762	arg1	site					764:767	the Asn-89 site	753:767	the Asn-89 site	753:767	N-Linked glycosylation at the Asn-89 site was required for intracellular production of functional vIL-6, but endoglycosidase-mediated removal of N-linked glycans from secreted vIL-6 did not impair protein function.
19690161	2	33	theme	huIL-6	406:411	arg1	function					381:388	optimal function	373:388	optimal function of vIL6 but not huIL-6 (1)	373:415	Our previous work showed that N-linked glycosylation was required for optimal function of vIL6 but not huIL-6 (1).
19690161	0	34	theme	protein	135:141	arg1	conformation					143:154	cytokine protein conformation	126:154	cytokine protein conformation	126:154	Complex N-linked glycans on Asn-89 of Kaposi sarcoma herpes virus-encoded interleukin-6 mediate optimal function by affecting cytokine protein conformation.
19690161	10	35	theme	N-linked	1378:1385	arg1	glycans					1387:1393	additional complex N-linked glycans	1359:1393	additional complex N-linked glycans	1359:1393	Two mutants of huIL-6, made to contain additional complex N-linked glycans in the region that interacts with IL-6Ralpha, did not confer binding to gp130 independently of IL-6Ralpha.
19690161	2	36	theme	N-linked	333:340	arg1	glycosylation					342:354	N-linked glycosylation	333:354	N-linked glycosylation	333:354	Our previous work showed that N-linked glycosylation was required for optimal function of vIL6 but not huIL-6 (1).
19690161	3	37	theme	glycans	475:481	arg1	composition					456:466	the composition	452:466	the composition of the glycans of the two N-linked sites of vIL-6	452:516	Here we describe heterogeneity in the composition of the glycans of the two N-linked sites of vIL-6.
19690161	7	38	gly	glycosylation	1036:1048	arg1	protein					1087:1093	protein conformation	1087:1106	protein conformation	1087:1106	With the use of a conformation-specific antibody and tryptic digestion assays, we showed that glycosylation at the Asn-89 site of vIL-6 affected protein conformation.
19690161	7	38	gly	glycosylation	1036:1048	arg2	vIL-6					1072:1076	vIL-6	1072:1076	vIL-6	1072:1076	With the use of a conformation-specific antibody and tryptic digestion assays, we showed that glycosylation at the Asn-89 site of vIL-6 affected protein conformation.
19690161	7	38	gly	glycosylation	1036:1048	arg1	vIL-6					1072:1076	vIL-6	1072:1076	vIL-6	1072:1076	With the use of a conformation-specific antibody and tryptic digestion assays, we showed that glycosylation at the Asn-89 site of vIL-6 affected protein conformation.
19690161	7	38	gly	glycosylation	1036:1048	arg2	site					1064:1067	the Asn-89 site	1053:1067	the Asn-89 site of vIL-6	1053:1076	With the use of a conformation-specific antibody and tryptic digestion assays, we showed that glycosylation at the Asn-89 site of vIL-6 affected protein conformation.
19690161	7	38	gly	glycosylation	1036:1048	arg1	site					1064:1067	the Asn-89 site	1053:1067	the Asn-89 site of vIL-6	1053:1076	With the use of a conformation-specific antibody and tryptic digestion assays, we showed that glycosylation at the Asn-89 site of vIL-6 affected protein conformation.
19690161	0	39	theme	cytokine	126:133	arg1	conformation					143:154	cytokine protein conformation	126:154	cytokine protein conformation	126:154	Complex N-linked glycans on Asn-89 of Kaposi sarcoma herpes virus-encoded interleukin-6 mediate optimal function by affecting cytokine protein conformation.
19690161	1	40	theme	human	233:237	arg1	huIL-6					259:264	huIL-6	259:264	huIL-6	259:264	Kaposi sarcoma-associated herpesvirus-encoded interleukin-6 (vIL-6) and its human cellular homologue (huIL-6) share similar biological functions.
19690161	1	40	theme	human	233:237	arg1	homologue					248:256	its human cellular homologue	229:256	its human cellular homologue (huIL-6)	229:265	Kaposi sarcoma-associated herpesvirus-encoded interleukin-6 (vIL-6) and its human cellular homologue (huIL-6) share similar biological functions.
19690161	3	41	theme	sites	503:507	arg1	glycans					475:481	the glycans	471:481	the glycans of the two N-linked sites of vIL-6	471:516	Here we describe heterogeneity in the composition of the glycans of the two N-linked sites of vIL-6.
19690161	9	42	theme	Asn-89	1212:1217	arg1	sufficient					1253:1262	sufficient	1253:1262	sufficient	1253:1262	We tested the hypothesis that the Asn-89 complex glycan of vIL-6 alone was sufficient to confer binding to gp130 independently of IL-6Ralpha.
19690161	9	42	theme	Asn-89	1212:1217	arg1	glycan					1227:1232	the Asn-89 complex glycan	1208:1232	the Asn-89 complex glycan of vIL-6	1208:1241	We tested the hypothesis that the Asn-89 complex glycan of vIL-6 alone was sufficient to confer binding to gp130 independently of IL-6Ralpha.
19690161	0	43	dep	sarcoma	45:51	arg1	interleukin-6					74:86	herpes virus-encoded interleukin-6	53:86	Kaposi sarcoma herpes virus-encoded interleukin-6	38:86	Complex N-linked glycans on Asn-89 of Kaposi sarcoma herpes virus-encoded interleukin-6 mediate optimal function by affecting cytokine protein conformation.
19690161	1	44	theme	cellular	239:246	arg1	huIL-6					259:264	huIL-6	259:264	huIL-6	259:264	Kaposi sarcoma-associated herpesvirus-encoded interleukin-6 (vIL-6) and its human cellular homologue (huIL-6) share similar biological functions.
19690161	1	44	theme	cellular	239:246	arg1	homologue					248:256	its human cellular homologue	229:256	its human cellular homologue (huIL-6)	229:265	Kaposi sarcoma-associated herpesvirus-encoded interleukin-6 (vIL-6) and its human cellular homologue (huIL-6) share similar biological functions.
19690161	10	45	link	N-linked	1378:1385	arg1	glycans					1387:1393	additional complex N-linked glycans	1359:1393	additional complex N-linked glycans	1359:1393	Two mutants of huIL-6, made to contain additional complex N-linked glycans in the region that interacts with IL-6Ralpha, did not confer binding to gp130 independently of IL-6Ralpha.
19690161	2	46	link	N-linked	333:340	arg1	glycosylation					342:354	N-linked glycosylation	333:354	N-linked glycosylation	333:354	Our previous work showed that N-linked glycosylation was required for optimal function of vIL6 but not huIL-6 (1).
19690161	7	47	theme	Asn-89	1057:1062	arg1	vIL-6					1072:1076	vIL-6	1072:1076	vIL-6	1072:1076	With the use of a conformation-specific antibody and tryptic digestion assays, we showed that glycosylation at the Asn-89 site of vIL-6 affected protein conformation.
19690161	7	47	theme	Asn-89	1057:1062	arg1	site					1064:1067	the Asn-89 site	1053:1067	the Asn-89 site of vIL-6	1053:1076	With the use of a conformation-specific antibody and tryptic digestion assays, we showed that glycosylation at the Asn-89 site of vIL-6 affected protein conformation.
19690161	6	48	theme	endoglycosidase-mediated	836:859	arg1	removal					861:867	endoglycosidase-mediated removal	836:867	endoglycosidase-mediated removal of N-linked glycans from secreted vIL-6	836:907	N-Linked glycosylation at the Asn-89 site was required for intracellular production of functional vIL-6, but endoglycosidase-mediated removal of N-linked glycans from secreted vIL-6 did not impair protein function.
19690161	6	49	from	site	764:767	arg1	glycosylation					736:748	N-Linked glycosylation	727:748	N-Linked glycosylation at the Asn-89 site	727:767	N-Linked glycosylation at the Asn-89 site was required for intracellular production of functional vIL-6, but endoglycosidase-mediated removal of N-linked glycans from secreted vIL-6 did not impair protein function.
19690161	0	50	theme	sarcoma	45:51	arg1	Asn-89					28:33	Asn-89	28:33	Asn-89 of Kaposi sarcoma herpes virus-encoded interleukin-6	28:86	Complex N-linked glycans on Asn-89 of Kaposi sarcoma herpes virus-encoded interleukin-6 mediate optimal function by affecting cytokine protein conformation.
19690161	4	51	theme	Asn-89	523:528	arg1	vIL-6					538:542	vIL-6	538:542	vIL-6	538:542	The Asn-89 site of vIL-6, found to be required for optimal cytokine function, is composed of complex glycans.
19690161	4	51	theme	Asn-89	523:528	arg1	site					530:533	The Asn-89 site	519:533	The Asn-89 site	519:533	The Asn-89 site of vIL-6, found to be required for optimal cytokine function, is composed of complex glycans.
19690161	8	52	theme	Human	1109:1113	arg1	IL-6					1115:1118	Human IL-6	1109:1118	Human IL-6	1109:1118	Human IL-6, but not vIL-6, requires IL-6Ralpha for binding to gp130.
19690161	6	53	from	vIL-6	903:907	arg1	removal					861:867	endoglycosidase-mediated removal	836:867	endoglycosidase-mediated removal of N-linked glycans from secreted vIL-6	836:907	N-Linked glycosylation at the Asn-89 site was required for intracellular production of functional vIL-6, but endoglycosidase-mediated removal of N-linked glycans from secreted vIL-6 did not impair protein function.
19690161	11	54	theme	viral	1638:1642	arg1	cytokine					1644:1651	the viral cytokine	1634:1651	the viral cytokine to bind gp130 independently of IL-6Ralpha	1634:1693	Our findings support the conclusion that complex glycans on Asn-89 of vIL-6 specifically promote a protein conformation that allows the viral cytokine to bind gp130 independently of IL-6Ralpha.
19690161	5	55	theme	high	660:663	arg1	glycans					673:679	high mannose glycans	660:679	high mannose glycans	660:679	The Asn-78 site is composed of high mannose glycans, which are dispensable for cytokine function.
19690161	3	56	theme	N-linked	494:501	arg1	vIL-6					512:516	vIL-6	512:516	vIL-6	512:516	Here we describe heterogeneity in the composition of the glycans of the two N-linked sites of vIL-6.
19690161	3	56	theme	N-linked	494:501	arg1	sites					503:507	the two N-linked sites	486:507	the two N-linked sites of vIL-6	486:516	Here we describe heterogeneity in the composition of the glycans of the two N-linked sites of vIL-6.
19690161	0	57	theme	Kaposi	38:43	arg1	sarcoma					45:51	Kaposi sarcoma herpes virus-encoded interleukin-6	38:86	Kaposi sarcoma herpes virus-encoded interleukin-6	38:86	Complex N-linked glycans on Asn-89 of Kaposi sarcoma herpes virus-encoded interleukin-6 mediate optimal function by affecting cytokine protein conformation.
19690161	4	58	theme	vIL-6	538:542	arg1	vIL-6					538:542	vIL-6	538:542	vIL-6	538:542	The Asn-89 site of vIL-6, found to be required for optimal cytokine function, is composed of complex glycans.
19690161	4	58	theme	vIL-6	538:542	arg1	site					530:533	The Asn-89 site	519:533	The Asn-89 site	519:533	The Asn-89 site of vIL-6, found to be required for optimal cytokine function, is composed of complex glycans.
19690161	9	59	theme	vIL-6	1237:1241	arg1	sufficient					1253:1262	sufficient	1253:1262	sufficient	1253:1262	We tested the hypothesis that the Asn-89 complex glycan of vIL-6 alone was sufficient to confer binding to gp130 independently of IL-6Ralpha.
19690161	9	59	theme	vIL-6	1237:1241	arg1	glycan					1227:1232	the Asn-89 complex glycan	1208:1232	the Asn-89 complex glycan of vIL-6	1208:1241	We tested the hypothesis that the Asn-89 complex glycan of vIL-6 alone was sufficient to confer binding to gp130 independently of IL-6Ralpha.
19690161	6	60	theme	N-Linked	727:734	arg1	glycosylation					736:748	N-Linked glycosylation	727:748	N-Linked glycosylation at the Asn-89 site	727:767	N-Linked glycosylation at the Asn-89 site was required for intracellular production of functional vIL-6, but endoglycosidase-mediated removal of N-linked glycans from secreted vIL-6 did not impair protein function.
19690161	2	61	theme	optimal	373:379	arg1	function					381:388	optimal function	373:388	optimal function of vIL6 but not huIL-6 (1)	373:415	Our previous work showed that N-linked glycosylation was required for optimal function of vIL6 but not huIL-6 (1).
19690161	6	62	theme	protein	924:930	arg1	function					932:939	protein function	924:939	protein function	924:939	N-Linked glycosylation at the Asn-89 site was required for intracellular production of functional vIL-6, but endoglycosidase-mediated removal of N-linked glycans from secreted vIL-6 did not impair protein function.
19690161	3	63	link	N-linked	494:501	arg1	vIL-6					512:516	vIL-6	512:516	vIL-6	512:516	Here we describe heterogeneity in the composition of the glycans of the two N-linked sites of vIL-6.
19690161	3	63	link	N-linked	494:501	arg1	sites					503:507	the two N-linked sites	486:507	the two N-linked sites of vIL-6	486:516	Here we describe heterogeneity in the composition of the glycans of the two N-linked sites of vIL-6.
19690161	6	64	theme	vIL-6	825:829	arg1	production					800:809	intracellular production	786:809	intracellular production of functional vIL-6	786:829	N-Linked glycosylation at the Asn-89 site was required for intracellular production of functional vIL-6, but endoglycosidase-mediated removal of N-linked glycans from secreted vIL-6 did not impair protein function.
19690161	10	65	theme	additional	1359:1368	arg1	glycans					1387:1393	additional complex N-linked glycans	1359:1393	additional complex N-linked glycans	1359:1393	Two mutants of huIL-6, made to contain additional complex N-linked glycans in the region that interacts with IL-6Ralpha, did not confer binding to gp130 independently of IL-6Ralpha.
19690161	7	66	dep	use	951:953	arg1	assays					1013:1018	assays	1013:1018	assays	1013:1018	With the use of a conformation-specific antibody and tryptic digestion assays, we showed that glycosylation at the Asn-89 site of vIL-6 affected protein conformation.
19690161	5	67	theme	mannose	665:671	arg1	glycans					673:679	high mannose glycans	660:679	high mannose glycans	660:679	The Asn-78 site is composed of high mannose glycans, which are dispensable for cytokine function.
19690161	6	68	theme	functional	814:823	arg1	vIL-6					825:829	functional vIL-6	814:829	functional vIL-6	814:829	N-Linked glycosylation at the Asn-89 site was required for intracellular production of functional vIL-6, but endoglycosidase-mediated removal of N-linked glycans from secreted vIL-6 did not impair protein function.
19690161	3	69	from	heterogeneity	435:447	arg1	composition					456:466	the composition	452:466	the composition of the glycans of the two N-linked sites of vIL-6	452:516	Here we describe heterogeneity in the composition of the glycans of the two N-linked sites of vIL-6.
19690161	11	70	from	glycans	1551:1557	arg1	Asn-89					1562:1567	Asn-89	1562:1567	Asn-89 of vIL-6	1562:1576	Our findings support the conclusion that complex glycans on Asn-89 of vIL-6 specifically promote a protein conformation that allows the viral cytokine to bind gp130 independently of IL-6Ralpha.
19690161	2	71	gly	glycosylation	342:354	arg1	vIL6					393:396	vIL6	393:396	vIL6 but not huIL-6 (1)	393:415	Our previous work showed that N-linked glycosylation was required for optimal function of vIL6 but not huIL-6 (1).
19690161	2	71	gly	glycosylation	342:354	arg1	huIL-6					406:411	huIL-6 (1)	406:415	vIL6 but not huIL-6 (1)	393:415	Our previous work showed that N-linked glycosylation was required for optimal function of vIL6 but not huIL-6 (1).
19690161	4	72	theme	complex	612:618	arg1	glycans					620:626	complex glycans	612:626	complex glycans	612:626	The Asn-89 site of vIL-6, found to be required for optimal cytokine function, is composed of complex glycans.
19690161	1	73	theme	Kaposi	157:162	arg1	vIL-6					218:222	vIL-6	218:222	vIL-6	218:222	Kaposi sarcoma-associated herpesvirus-encoded interleukin-6 (vIL-6) and its human cellular homologue (huIL-6) share similar biological functions.
19690161	1	73	theme	Kaposi	157:162	arg1	interleukin-6					203:215	Kaposi sarcoma-associated herpesvirus-encoded interleukin-6	157:215	Kaposi sarcoma-associated herpesvirus-encoded interleukin-6 (vIL-6)	157:223	Kaposi sarcoma-associated herpesvirus-encoded interleukin-6 (vIL-6) and its human cellular homologue (huIL-6) share similar biological functions.
19690161	0	74	theme	herpes	53:58	arg1	interleukin-6					74:86	herpes virus-encoded interleukin-6	53:86	Kaposi sarcoma herpes virus-encoded interleukin-6	38:86	Complex N-linked glycans on Asn-89 of Kaposi sarcoma herpes virus-encoded interleukin-6 mediate optimal function by affecting cytokine protein conformation.
19690161	7	75	theme	conformation-specific	960:980	arg1	antibody					982:989	a conformation-specific antibody	958:989	a conformation-specific antibody	958:989	With the use of a conformation-specific antibody and tryptic digestion assays, we showed that glycosylation at the Asn-89 site of vIL-6 affected protein conformation.
19690161	1	76	theme	sarcoma-associated	164:181	arg1	vIL-6					218:222	vIL-6	218:222	vIL-6	218:222	Kaposi sarcoma-associated herpesvirus-encoded interleukin-6 (vIL-6) and its human cellular homologue (huIL-6) share similar biological functions.
19690161	1	76	theme	sarcoma-associated	164:181	arg1	interleukin-6					203:215	Kaposi sarcoma-associated herpesvirus-encoded interleukin-6	157:215	Kaposi sarcoma-associated herpesvirus-encoded interleukin-6 (vIL-6)	157:223	Kaposi sarcoma-associated herpesvirus-encoded interleukin-6 (vIL-6) and its human cellular homologue (huIL-6) share similar biological functions.
16491292	5	0	theme	affected	605:612	arg1	members					614:620	affected members	605:620	affected members	605:620	We recently reported a family with JPD in which affected members were homozygous for an in-frame mutation resulting in the deletion of aspartate 182 in OPG.
16491292	10	1	theme	conditioned	1370:1380	arg1	media					1382:1386	conditioned media	1370:1386	conditioned media	1370:1386	ELISA and Western blots were used to determine OPG concentrations in cell lysates and conditioned media from transiently transfected cells.
16491292	9	2	theme	adjacent	1225:1232	arg1	sites					1219:1223	two potential glycosylation sites	1191:1223	two potential glycosylation sites adjacent to the deleted aspartate residue at position 182	1191:1281	Site-directed mutagenesis was used to study the glycosylation of OPGdeltaD182 in two potential glycosylation sites adjacent to the deleted aspartate residue at position 182.
16491292	6	3	theme	functional	748:757	arg1	characterization					759:774	the structural and functional characterization	729:774	the structural and functional characterization of the OPGdeltaD182 mutant protein	729:809	Here we report the structural and functional characterization of the OPGdeltaD182 mutant protein.
16491292	2	4	theme	mutant	254:259	arg1	OPG					261:263	the mutant OPG	250:263	the mutant OPG	250:263	We characterized the effects of one such mutation and found that the mutant OPG is poorly secreted and has reduced biological activity compared with the wildtype protein.
16491292	9	5	gly	glycosylation	1205:1217	arg2	two					1191:1193	two	1191:1193	two	1191:1193	Site-directed mutagenesis was used to study the glycosylation of OPGdeltaD182 in two potential glycosylation sites adjacent to the deleted aspartate residue at position 182.
16491292	9	5	gly	glycosylation	1205:1217	arg2	sites					1219:1223	two potential glycosylation sites	1191:1223	two potential glycosylation sites adjacent to the deleted aspartate residue at position 182	1191:1281	Site-directed mutagenesis was used to study the glycosylation of OPGdeltaD182 in two potential glycosylation sites adjacent to the deleted aspartate residue at position 182.
16491292	13	6	theme	OPG	1787:1789	arg1	structure					1791:1799	OPG structure	1787:1799	OPG structure	1787:1799	Glycosylation at N183 has the potential to disrupt OPG structure by interfering with disulphide bond formation and correct protein folding.
16491292	6	7	theme	structural	733:742	arg1	characterization					759:774	the structural and functional characterization	729:774	the structural and functional characterization of the OPGdeltaD182 mutant protein	729:809	Here we report the structural and functional characterization of the OPGdeltaD182 mutant protein.
16491292	5	8	from	OPG	709:711	arg1	deletion					680:687	the deletion	676:687	the deletion of aspartate 182 in OPG	676:711	We recently reported a family with JPD in which affected members were homozygous for an in-frame mutation resulting in the deletion of aspartate 182 in OPG.
16491292	8	9	theme	wildtype	956:963	arg1	OPG					976:978	wildtype and mutant OPG	956:978	wildtype and mutant OPG	956:978	Binding of wildtype and mutant OPG to RANKL was measured in two experimental systems: glutathione-S-transferase (GST) pull-down assay and surface plasmon resonance.
16491292	1	10	theme	idiopathic	155:164	arg1	hyperphosphatasia					166:182	idiopathic hyperphosphatasia	155:182	idiopathic hyperphosphatasia	155:182	Mutations in the OPG gene cause idiopathic hyperphosphatasia.
16491292	9	11	gly	glycosylation	1158:1170	arg1	sites					1219:1223	two potential glycosylation sites	1191:1223	two potential glycosylation sites adjacent to the deleted aspartate residue at position 182	1191:1281	Site-directed mutagenesis was used to study the glycosylation of OPGdeltaD182 in two potential glycosylation sites adjacent to the deleted aspartate residue at position 182.
16491292	9	11	gly	glycosylation	1158:1170	arg1	OPGdeltaD182					1175:1186	OPGdeltaD182	1175:1186	OPGdeltaD182	1175:1186	Site-directed mutagenesis was used to study the glycosylation of OPGdeltaD182 in two potential glycosylation sites adjacent to the deleted aspartate residue at position 182.
16491292	12	12	theme	higher	1586:1591	arg1	weight					1603:1608	higher molecular weight	1586:1608	The apparent higher molecular weight of OPGdeltaD182 compared with the wildtype	1573:1651	The apparent higher molecular weight of OPGdeltaD182 compared with the wildtype is a result of hyperglycosylation of asparagine residues at positions 178 and 183.
16491292	12	12	theme	higher	1586:1591	arg1	result					1658:1663	a result	1656:1663	a result of hyperglycosylation of asparagine residues at positions 178 and 183	1656:1733	The apparent higher molecular weight of OPGdeltaD182 compared with the wildtype is a result of hyperglycosylation of asparagine residues at positions 178 and 183.
16491292	8	13	theme	mutant	969:974	arg1	OPG					976:978	wildtype and mutant OPG	956:978	wildtype and mutant OPG	956:978	Binding of wildtype and mutant OPG to RANKL was measured in two experimental systems: glutathione-S-transferase (GST) pull-down assay and surface plasmon resonance.
16491292	9	14	theme	potential	1195:1203	arg1	sites					1219:1223	two potential glycosylation sites	1191:1223	two potential glycosylation sites adjacent to the deleted aspartate residue at position 182	1191:1281	Site-directed mutagenesis was used to study the glycosylation of OPGdeltaD182 in two potential glycosylation sites adjacent to the deleted aspartate residue at position 182.
16491292	13	15	theme	disulphide	1821:1830	arg1	formation					1837:1845	disulphide bond formation	1821:1845	disulphide bond formation	1821:1845	Glycosylation at N183 has the potential to disrupt OPG structure by interfering with disulphide bond formation and correct protein folding.
16491292	9	16	from	position	1270:1277	arg1	residue					1259:1265	the deleted aspartate residue	1237:1265	the deleted aspartate residue at position 182	1237:1281	Site-directed mutagenesis was used to study the glycosylation of OPGdeltaD182 in two potential glycosylation sites adjacent to the deleted aspartate residue at position 182.
16491292	5	17	from	deletion	680:687	arg1	OPG					709:711	OPG	709:711	OPG	709:711	We recently reported a family with JPD in which affected members were homozygous for an in-frame mutation resulting in the deletion of aspartate 182 in OPG.
16491292	14	18	theme	Transient	1876:1884	arg1	experiments					1899:1909	Transient transfection experiments	1876:1909	Transient transfection experiments in SaOS2 cells	1876:1924	Transient transfection experiments in SaOS2 cells suggest that OPGdeltaD182 is retained within the cell, a typical response to unstable or incorrect protein folding.
16491292	5	19	theme	in-frame	645:652	arg1	mutation					654:661	an in-frame mutation	642:661	an in-frame mutation resulting in the deletion of aspartate 182 in OPG	642:711	We recently reported a family with JPD in which affected members were homozygous for an in-frame mutation resulting in the deletion of aspartate 182 in OPG.
16491292	9	20	theme	deleted	1241:1247	arg1	residue					1259:1265	the deleted aspartate residue	1237:1265	the deleted aspartate residue at position 182	1237:1281	Site-directed mutagenesis was used to study the glycosylation of OPGdeltaD182 in two potential glycosylation sites adjacent to the deleted aspartate residue at position 182.
16491292	12	21	from	hyperglycosylation	1668:1685	arg1	positions					1713:1721	positions 178 and 183	1713:1733	positions 178 and 183	1713:1733	The apparent higher molecular weight of OPGdeltaD182 compared with the wildtype is a result of hyperglycosylation of asparagine residues at positions 178 and 183.
16491292	11	22	theme	osteoclasts	1474:1484	arg1	generation					1460:1469	the generation	1456:1469	the generation of osteoclasts	1456:1484	RESULTS: OPGdeltaD182 inhibited the generation of osteoclasts less effectively than the wildtype protein and had a reduced ability to bind to RANKL.
16491292	2	23	contain	has	288:290	arg1	OPG					261:263	the mutant OPG	250:263	the mutant OPG	250:263	We characterized the effects of one such mutation and found that the mutant OPG is poorly secreted and has reduced biological activity compared with the wildtype protein.
16491292	2	23	contain	has	288:290	arg2	activity					311:318	reduced biological activity	292:318	reduced biological activity	292:318	We characterized the effects of one such mutation and found that the mutant OPG is poorly secreted and has reduced biological activity compared with the wildtype protein.
16491292	2	24	theme	such	221:224	arg1	mutation					226:233	one such mutation	217:233	one such mutation	217:233	We characterized the effects of one such mutation and found that the mutant OPG is poorly secreted and has reduced biological activity compared with the wildtype protein.
16491292	12	25	theme	hyperglycosylation	1668:1685	arg1	weight					1603:1608	higher molecular weight	1586:1608	The apparent higher molecular weight of OPGdeltaD182 compared with the wildtype	1573:1651	The apparent higher molecular weight of OPGdeltaD182 compared with the wildtype is a result of hyperglycosylation of asparagine residues at positions 178 and 183.
16491292	12	25	theme	hyperglycosylation	1668:1685	arg1	result					1658:1663	a result	1656:1663	a result of hyperglycosylation of asparagine residues at positions 178 and 183	1656:1733	The apparent higher molecular weight of OPGdeltaD182 compared with the wildtype is a result of hyperglycosylation of asparagine residues at positions 178 and 183.
16491292	4	26	theme	Inactivating	471:482	arg1	mutations					484:492	Inactivating mutations	471:492	Inactivating mutations in osteoprotegerin (OPG)	471:517	INTRODUCTION: Inactivating mutations in osteoprotegerin (OPG) cause juvenile Paget's disease (JPD).
16491292	7	27	theme	bone	924:927	arg1	culture					936:942	a murine bone marrow culture	915:942	a murine bone marrow culture	915:942	MATERIALS AND METHODS: Inhibition of osteoclastogenesis by the recombinant OPG proteins was studied in a murine bone marrow culture.
16491292	12	28	theme	asparagine	1690:1699	arg1	residues					1701:1708	asparagine residues	1690:1708	asparagine residues at positions 178 and 183	1690:1733	The apparent higher molecular weight of OPGdeltaD182 compared with the wildtype is a result of hyperglycosylation of asparagine residues at positions 178 and 183.
16491292	0	29	from	Deletion	0:7	arg1	OPG					29:31	OPG	29:31	OPG	29:31	Deletion of aspartate 182 in OPG causes juvenile Paget's disease by impairing both protein secretion and binding to RANKL.
16491292	14	30	theme	protein	2025:2031	arg1	folding					2033:2039	unstable or incorrect protein folding	2003:2039	unstable or incorrect protein folding	2003:2039	Transient transfection experiments in SaOS2 cells suggest that OPGdeltaD182 is retained within the cell, a typical response to unstable or incorrect protein folding.
16491292	13	31	theme	protein	1859:1865	arg1	folding					1867:1873	correct protein folding	1851:1873	correct protein folding	1851:1873	Glycosylation at N183 has the potential to disrupt OPG structure by interfering with disulphide bond formation and correct protein folding.
16491292	3	32	theme	OPG	412:414	arg1	structure					375:383	correct structure	367:383	correct structure	367:383	Therefore, correct structure and cellular processing of OPG is essential for normal bone remodeling.
16491292	3	32	theme	OPG	412:414	arg1	processing					398:407	cellular processing	389:407	cellular processing	389:407	Therefore, correct structure and cellular processing of OPG is essential for normal bone remodeling.
16491292	0	33	theme	protein	83:89	arg1	secretion					91:99	protein secretion	83:99	protein secretion	83:99	Deletion of aspartate 182 in OPG causes juvenile Paget's disease by impairing both protein secretion and binding to RANKL.
16491292	15	34	theme	bone	2257:2260	arg1	turnover					2262:2269	high bone turnover	2252:2269	high bone turnover	2252:2269	CONCLUSIONS: Taken together, these data suggest that the deletion of aspartate 182 impairs both the secretion and activity of OPG, which in turn provides an explanation for the increased osteoclastogenesis and high bone turnover observed in JPD patients with this mutation.
16491292	8	35	theme	experimental	1009:1020	arg1	resonance					1099:1107	surface plasmon resonance	1083:1107	surface plasmon resonance	1083:1107	Binding of wildtype and mutant OPG to RANKL was measured in two experimental systems: glutathione-S-transferase (GST) pull-down assay and surface plasmon resonance.
16491292	8	35	theme	experimental	1009:1020	arg1	assay					1073:1077	glutathione-S-transferase (GST) pull-down assay	1031:1077	glutathione-S-transferase (GST) pull-down assay	1031:1077	Binding of wildtype and mutant OPG to RANKL was measured in two experimental systems: glutathione-S-transferase (GST) pull-down assay and surface plasmon resonance.
16491292	8	35	theme	experimental	1009:1020	arg1	systems					1022:1028	two experimental systems	1005:1028	two experimental systems: glutathione-S-transferase (GST) pull-down assay and surface plasmon resonance	1005:1107	Binding of wildtype and mutant OPG to RANKL was measured in two experimental systems: glutathione-S-transferase (GST) pull-down assay and surface plasmon resonance.
16491292	4	36	theme	juvenile	525:532	arg1	JPD					551:553	JPD	551:553	JPD	551:553	INTRODUCTION: Inactivating mutations in osteoprotegerin (OPG) cause juvenile Paget's disease (JPD).
16491292	4	36	theme	juvenile	525:532	arg1	disease					542:548	juvenile Paget's disease	525:548	juvenile Paget's disease (JPD)	525:554	INTRODUCTION: Inactivating mutations in osteoprotegerin (OPG) cause juvenile Paget's disease (JPD).
16491292	13	37	theme	bond	1832:1835	arg1	formation					1837:1845	disulphide bond formation	1821:1845	disulphide bond formation	1821:1845	Glycosylation at N183 has the potential to disrupt OPG structure by interfering with disulphide bond formation and correct protein folding.
16491292	3	38	theme	normal	433:438	arg1	remodeling					445:454	normal bone remodeling	433:454	normal bone remodeling	433:454	Therefore, correct structure and cellular processing of OPG is essential for normal bone remodeling.
16491292	0	39	theme	aspartate	12:20	arg1	Deletion					0:7	Deletion	0:7	Deletion of aspartate 182 in OPG	0:31	Deletion of aspartate 182 in OPG causes juvenile Paget's disease by impairing both protein secretion and binding to RANKL.
16491292	5	40	from	family	580:585	arg1	homozygous					627:636	homozygous	627:636	homozygous	627:636	We recently reported a family with JPD in which affected members were homozygous for an in-frame mutation resulting in the deletion of aspartate 182 in OPG.
16491292	15	41	dep	secretion	2142:2150	arg1	the					2138:2140	the	2138:2140	the	2138:2140	CONCLUSIONS: Taken together, these data suggest that the deletion of aspartate 182 impairs both the secretion and activity of OPG, which in turn provides an explanation for the increased osteoclastogenesis and high bone turnover observed in JPD patients with this mutation.
16491292	14	42	theme	typical	1983:1989	arg1	response					1991:1998	a typical response	1981:1998	a typical response to unstable or incorrect protein folding	1981:2039	Transient transfection experiments in SaOS2 cells suggest that OPGdeltaD182 is retained within the cell, a typical response to unstable or incorrect protein folding.
16491292	9	43	used	used	1140:1143	arg2	mutagenesis					1124:1134	Site-directed mutagenesis	1110:1134	Site-directed mutagenesis	1110:1134	Site-directed mutagenesis was used to study the glycosylation of OPGdeltaD182 in two potential glycosylation sites adjacent to the deleted aspartate residue at position 182.
16491292	15	44	theme	OPG	2168:2170	arg1	secretion					2142:2150	secretion	2142:2150	secretion	2142:2150	CONCLUSIONS: Taken together, these data suggest that the deletion of aspartate 182 impairs both the secretion and activity of OPG, which in turn provides an explanation for the increased osteoclastogenesis and high bone turnover observed in JPD patients with this mutation.
16491292	15	44	theme	OPG	2168:2170	arg1	activity					2156:2163	activity	2156:2163	activity	2156:2163	CONCLUSIONS: Taken together, these data suggest that the deletion of aspartate 182 impairs both the secretion and activity of OPG, which in turn provides an explanation for the increased osteoclastogenesis and high bone turnover observed in JPD patients with this mutation.
16491292	10	45	from	concentrations	1335:1348	arg1	cells					1417:1421	transiently transfected cells	1393:1421	transiently transfected cells	1393:1421	ELISA and Western blots were used to determine OPG concentrations in cell lysates and conditioned media from transiently transfected cells.
16491292	10	45	from	concentrations	1335:1348	arg1	lysates					1358:1364	cell lysates	1353:1364	cell lysates	1353:1364	ELISA and Western blots were used to determine OPG concentrations in cell lysates and conditioned media from transiently transfected cells.
16491292	10	45	from	concentrations	1335:1348	arg1	media					1382:1386	conditioned media	1370:1386	conditioned media	1370:1386	ELISA and Western blots were used to determine OPG concentrations in cell lysates and conditioned media from transiently transfected cells.
16491292	3	46	theme	correct	367:373	arg1	structure					375:383	correct structure	367:383	correct structure	367:383	Therefore, correct structure and cellular processing of OPG is essential for normal bone remodeling.
16491292	7	47	dep	MATERIALS	812:820	arg1	studied					904:910	studied	904:910	was studied in a murine bone marrow culture	900:942	MATERIALS AND METHODS: Inhibition of osteoclastogenesis by the recombinant OPG proteins was studied in a murine bone marrow culture.
16491292	15	48	theme	increased	2219:2227	arg1	osteoclastogenesis					2229:2246	the increased osteoclastogenesis	2215:2246	the increased osteoclastogenesis	2215:2246	CONCLUSIONS: Taken together, these data suggest that the deletion of aspartate 182 impairs both the secretion and activity of OPG, which in turn provides an explanation for the increased osteoclastogenesis and high bone turnover observed in JPD patients with this mutation.
16491292	6	49	theme	protein	803:809	arg1	characterization					759:774	the structural and functional characterization	729:774	the structural and functional characterization of the OPGdeltaD182 mutant protein	729:809	Here we report the structural and functional characterization of the OPGdeltaD182 mutant protein.
16491292	15	50	theme	aspartate	2111:2119	arg1	deletion					2099:2106	the deletion	2095:2106	the deletion of aspartate 182	2095:2123	CONCLUSIONS: Taken together, these data suggest that the deletion of aspartate 182 impairs both the secretion and activity of OPG, which in turn provides an explanation for the increased osteoclastogenesis and high bone turnover observed in JPD patients with this mutation.
16491292	10	51	theme	transfected	1405:1415	arg1	cells					1417:1421	transiently transfected cells	1393:1421	transiently transfected cells	1393:1421	ELISA and Western blots were used to determine OPG concentrations in cell lysates and conditioned media from transiently transfected cells.
16491292	2	52	theme	reduced	292:298	arg1	activity					311:318	reduced biological activity	292:318	reduced biological activity	292:318	We characterized the effects of one such mutation and found that the mutant OPG is poorly secreted and has reduced biological activity compared with the wildtype protein.
16491292	7	53	theme	OPG	887:889	arg1	proteins					891:898	the recombinant OPG proteins	871:898	the recombinant OPG proteins	871:898	MATERIALS AND METHODS: Inhibition of osteoclastogenesis by the recombinant OPG proteins was studied in a murine bone marrow culture.
16491292	6	54	theme	OPGdeltaD182	783:794	arg1	protein					803:809	the OPGdeltaD182 mutant protein	779:809	the OPGdeltaD182 mutant protein	779:809	Here we report the structural and functional characterization of the OPGdeltaD182 mutant protein.
16491292	8	55	dep	systems	1022:1028	arg1	resonance					1099:1107	surface plasmon resonance	1083:1107	surface plasmon resonance	1083:1107	Binding of wildtype and mutant OPG to RANKL was measured in two experimental systems: glutathione-S-transferase (GST) pull-down assay and surface plasmon resonance.
16491292	8	55	dep	systems	1022:1028	arg1	assay					1073:1077	glutathione-S-transferase (GST) pull-down assay	1031:1077	glutathione-S-transferase (GST) pull-down assay	1031:1077	Binding of wildtype and mutant OPG to RANKL was measured in two experimental systems: glutathione-S-transferase (GST) pull-down assay and surface plasmon resonance.
16491292	8	55	dep	systems	1022:1028	arg1	systems					1022:1028	two experimental systems	1005:1028	two experimental systems: glutathione-S-transferase (GST) pull-down assay and surface plasmon resonance	1005:1107	Binding of wildtype and mutant OPG to RANKL was measured in two experimental systems: glutathione-S-transferase (GST) pull-down assay and surface plasmon resonance.
16491292	2	56	theme	wildtype	338:345	arg1	protein					347:353	the wildtype protein	334:353	the wildtype protein	334:353	We characterized the effects of one such mutation and found that the mutant OPG is poorly secreted and has reduced biological activity compared with the wildtype protein.
16491292	5	57	from	homozygous	627:636	arg1	family					580:585	a family	578:585	a family with JPD in which affected members were homozygous for an in-frame mutation resulting in the deletion of aspartate 182 in OPG	578:711	We recently reported a family with JPD in which affected members were homozygous for an in-frame mutation resulting in the deletion of aspartate 182 in OPG.
16491292	8	58	theme	surface	1083:1089	arg1	resonance					1099:1107	surface plasmon resonance	1083:1107	surface plasmon resonance	1083:1107	Binding of wildtype and mutant OPG to RANKL was measured in two experimental systems: glutathione-S-transferase (GST) pull-down assay and surface plasmon resonance.
16491292	8	58	theme	surface	1083:1089	arg1	systems					1022:1028	two experimental systems	1005:1028	two experimental systems: glutathione-S-transferase (GST) pull-down assay and surface plasmon resonance	1005:1107	Binding of wildtype and mutant OPG to RANKL was measured in two experimental systems: glutathione-S-transferase (GST) pull-down assay and surface plasmon resonance.
16491292	7	59	theme	osteoclastogenesis	849:866	arg1	Inhibition					835:844	Inhibition	835:844	Inhibition of osteoclastogenesis by the recombinant OPG proteins	835:898	MATERIALS AND METHODS: Inhibition of osteoclastogenesis by the recombinant OPG proteins was studied in a murine bone marrow culture.
16491292	10	60	used	used	1313:1316	arg2	blots					1302:1306	Western blots	1294:1306	Western blots	1294:1306	ELISA and Western blots were used to determine OPG concentrations in cell lysates and conditioned media from transiently transfected cells.
16491292	10	60	used	used	1313:1316	arg2	ELISA					1284:1288	ELISA	1284:1288	ELISA	1284:1288	ELISA and Western blots were used to determine OPG concentrations in cell lysates and conditioned media from transiently transfected cells.
16491292	4	61	from	mutations	484:492	arg1	OPG					514:516	OPG	514:516	OPG	514:516	INTRODUCTION: Inactivating mutations in osteoprotegerin (OPG) cause juvenile Paget's disease (JPD).
16491292	4	61	from	mutations	484:492	arg1	osteoprotegerin					497:511	osteoprotegerin	497:511	osteoprotegerin (OPG)	497:517	INTRODUCTION: Inactivating mutations in osteoprotegerin (OPG) cause juvenile Paget's disease (JPD).
16491292	11	62	theme	reduced	1539:1545	arg1	ability					1547:1553	a reduced ability	1537:1553	a reduced ability to bind to RANKL	1537:1570	RESULTS: OPGdeltaD182 inhibited the generation of osteoclasts less effectively than the wildtype protein and had a reduced ability to bind to RANKL.
16491292	15	63	theme	JPD	2283:2285	arg1	patients					2287:2294	JPD patients	2283:2294	JPD patients with this mutation	2283:2313	CONCLUSIONS: Taken together, these data suggest that the deletion of aspartate 182 impairs both the secretion and activity of OPG, which in turn provides an explanation for the increased osteoclastogenesis and high bone turnover observed in JPD patients with this mutation.
16491292	15	64	with	patients	2287:2294	arg1	mutation					2306:2313	this mutation	2301:2313	this mutation	2301:2313	CONCLUSIONS: Taken together, these data suggest that the deletion of aspartate 182 impairs both the secretion and activity of OPG, which in turn provides an explanation for the increased osteoclastogenesis and high bone turnover observed in JPD patients with this mutation.
16491292	10	65	theme	cell	1353:1356	arg1	lysates					1358:1364	cell lysates	1353:1364	cell lysates	1353:1364	ELISA and Western blots were used to determine OPG concentrations in cell lysates and conditioned media from transiently transfected cells.
16491292	1	66	theme	OPG	140:142	arg1	gene					144:147	the OPG gene	136:147	the OPG gene	136:147	Mutations in the OPG gene cause idiopathic hyperphosphatasia.
16491292	9	67	theme	OPGdeltaD182	1175:1186	arg1	glycosylation					1158:1170	the glycosylation	1154:1170	the glycosylation of OPGdeltaD182 in two potential glycosylation sites adjacent to the deleted aspartate residue at position 182	1154:1281	Site-directed mutagenesis was used to study the glycosylation of OPGdeltaD182 in two potential glycosylation sites adjacent to the deleted aspartate residue at position 182.
16491292	12	68	theme	molecular	1593:1601	arg1	weight					1603:1608	higher molecular weight	1586:1608	The apparent higher molecular weight of OPGdeltaD182 compared with the wildtype	1573:1651	The apparent higher molecular weight of OPGdeltaD182 compared with the wildtype is a result of hyperglycosylation of asparagine residues at positions 178 and 183.
16491292	12	68	theme	molecular	1593:1601	arg1	result					1658:1663	a result	1656:1663	a result of hyperglycosylation of asparagine residues at positions 178 and 183	1656:1733	The apparent higher molecular weight of OPGdeltaD182 compared with the wildtype is a result of hyperglycosylation of asparagine residues at positions 178 and 183.
16491292	13	69	gly	Glycosylation	1736:1748	arg2	N183					1753:1756	N183	1753:1756	N183	1753:1756	Glycosylation at N183 has the potential to disrupt OPG structure by interfering with disulphide bond formation and correct protein folding.
16491292	15	70	located	observed	2271:2278	arg1	patients					2287:2294	JPD patients	2283:2294	JPD patients with this mutation	2283:2313	CONCLUSIONS: Taken together, these data suggest that the deletion of aspartate 182 impairs both the secretion and activity of OPG, which in turn provides an explanation for the increased osteoclastogenesis and high bone turnover observed in JPD patients with this mutation.
16491292	15	70	located	observed	2271:2278	arg2	osteoclastogenesis					2229:2246	the increased osteoclastogenesis	2215:2246	the increased osteoclastogenesis	2215:2246	CONCLUSIONS: Taken together, these data suggest that the deletion of aspartate 182 impairs both the secretion and activity of OPG, which in turn provides an explanation for the increased osteoclastogenesis and high bone turnover observed in JPD patients with this mutation.
16491292	8	71	theme	OPG	976:978	arg1	Binding					945:951	Binding	945:951	Binding of wildtype and mutant OPG to RANKL	945:987	Binding of wildtype and mutant OPG to RANKL was measured in two experimental systems: glutathione-S-transferase (GST) pull-down assay and surface plasmon resonance.
16491292	9	72	theme	glycosylation	1205:1217	arg1	sites					1219:1223	two potential glycosylation sites	1191:1223	two potential glycosylation sites adjacent to the deleted aspartate residue at position 182	1191:1281	Site-directed mutagenesis was used to study the glycosylation of OPGdeltaD182 in two potential glycosylation sites adjacent to the deleted aspartate residue at position 182.
16491292	14	73	theme	SaOS2	1914:1918	arg1	cells					1920:1924	SaOS2 cells	1914:1924	SaOS2 cells	1914:1924	Transient transfection experiments in SaOS2 cells suggest that OPGdeltaD182 is retained within the cell, a typical response to unstable or incorrect protein folding.
16491292	14	74	theme	transfection	1886:1897	arg1	experiments					1899:1909	Transient transfection experiments	1876:1909	Transient transfection experiments in SaOS2 cells	1876:1924	Transient transfection experiments in SaOS2 cells suggest that OPGdeltaD182 is retained within the cell, a typical response to unstable or incorrect protein folding.
16491292	12	75	from	positions	1713:1721	arg1	hyperglycosylation					1668:1685	hyperglycosylation	1668:1685	hyperglycosylation of asparagine residues at positions 178 and 183	1668:1733	The apparent higher molecular weight of OPGdeltaD182 compared with the wildtype is a result of hyperglycosylation of asparagine residues at positions 178 and 183.
16491292	12	75	from	positions	1713:1721	arg1	residues					1701:1708	asparagine residues	1690:1708	asparagine residues at positions 178 and 183	1690:1733	The apparent higher molecular weight of OPGdeltaD182 compared with the wildtype is a result of hyperglycosylation of asparagine residues at positions 178 and 183.
16491292	10	76	from	cells	1417:1421	arg1	concentrations					1335:1348	OPG concentrations	1331:1348	OPG concentrations in cell lysates and conditioned media from transiently transfected cells	1331:1421	ELISA and Western blots were used to determine OPG concentrations in cell lysates and conditioned media from transiently transfected cells.
16491292	10	76	from	cells	1417:1421	arg1	lysates					1358:1364	cell lysates	1353:1364	cell lysates	1353:1364	ELISA and Western blots were used to determine OPG concentrations in cell lysates and conditioned media from transiently transfected cells.
16491292	10	76	from	cells	1417:1421	arg1	media					1382:1386	conditioned media	1370:1386	conditioned media	1370:1386	ELISA and Western blots were used to determine OPG concentrations in cell lysates and conditioned media from transiently transfected cells.
16491292	12	77	theme	apparent	1577:1584	arg1	weight					1603:1608	higher molecular weight	1586:1608	The apparent higher molecular weight of OPGdeltaD182 compared with the wildtype	1573:1651	The apparent higher molecular weight of OPGdeltaD182 compared with the wildtype is a result of hyperglycosylation of asparagine residues at positions 178 and 183.
16491292	12	77	theme	apparent	1577:1584	arg1	result					1658:1663	a result	1656:1663	a result of hyperglycosylation of asparagine residues at positions 178 and 183	1656:1733	The apparent higher molecular weight of OPGdeltaD182 compared with the wildtype is a result of hyperglycosylation of asparagine residues at positions 178 and 183.
16491292	14	78	dep	cell	1975:1978	arg1	response					1991:1998	a typical response	1981:1998	a typical response to unstable or incorrect protein folding	1981:2039	Transient transfection experiments in SaOS2 cells suggest that OPGdeltaD182 is retained within the cell, a typical response to unstable or incorrect protein folding.
16491292	12	79	theme	residues	1701:1708	arg1	hyperglycosylation					1668:1685	hyperglycosylation	1668:1685	hyperglycosylation of asparagine residues at positions 178 and 183	1668:1733	The apparent higher molecular weight of OPGdeltaD182 compared with the wildtype is a result of hyperglycosylation of asparagine residues at positions 178 and 183.
16491292	9	80	theme	aspartate	1249:1257	arg1	residue					1259:1265	the deleted aspartate residue	1237:1265	the deleted aspartate residue at position 182	1237:1281	Site-directed mutagenesis was used to study the glycosylation of OPGdeltaD182 in two potential glycosylation sites adjacent to the deleted aspartate residue at position 182.
16491292	2	81	theme	mutation	226:233	arg1	effects					206:212	the effects	202:212	the effects of one such mutation	202:233	We characterized the effects of one such mutation and found that the mutant OPG is poorly secreted and has reduced biological activity compared with the wildtype protein.
16491292	9	82	from	glycosylation	1158:1170	arg1	sites					1219:1223	two potential glycosylation sites	1191:1223	two potential glycosylation sites adjacent to the deleted aspartate residue at position 182	1191:1281	Site-directed mutagenesis was used to study the glycosylation of OPGdeltaD182 in two potential glycosylation sites adjacent to the deleted aspartate residue at position 182.
16491292	11	83	theme	wildtype	1512:1519	arg1	protein					1521:1527	the wildtype protein	1508:1527	the wildtype protein	1508:1527	RESULTS: OPGdeltaD182 inhibited the generation of osteoclasts less effectively than the wildtype protein and had a reduced ability to bind to RANKL.
16491292	11	84	contain	had	1533:1535	arg2	ability					1547:1553	a reduced ability	1537:1553	a reduced ability to bind to RANKL	1537:1570	RESULTS: OPGdeltaD182 inhibited the generation of osteoclasts less effectively than the wildtype protein and had a reduced ability to bind to RANKL.
16491292	11	84	contain	had	1533:1535	arg1	OPGdeltaD182					1433:1444	OPGdeltaD182	1433:1444	OPGdeltaD182	1433:1444	RESULTS: OPGdeltaD182 inhibited the generation of osteoclasts less effectively than the wildtype protein and had a reduced ability to bind to RANKL.
16491292	5	85	from	aspartate	692:700	arg1	OPG					709:711	OPG	709:711	OPG	709:711	We recently reported a family with JPD in which affected members were homozygous for an in-frame mutation resulting in the deletion of aspartate 182 in OPG.
16491292	7	86	theme	marrow	929:934	arg1	culture					936:942	a murine bone marrow culture	915:942	a murine bone marrow culture	915:942	MATERIALS AND METHODS: Inhibition of osteoclastogenesis by the recombinant OPG proteins was studied in a murine bone marrow culture.
16491292	13	87	contain	has	1758:1760	arg2	potential					1766:1774	the potential to disrupt OPG structure by interfering with disulphide bond formation and correct protein folding	1762:1873	the potential to disrupt OPG structure by interfering with disulphide bond formation and correct protein folding	1762:1873	Glycosylation at N183 has the potential to disrupt OPG structure by interfering with disulphide bond formation and correct protein folding.
16491292	13	87	contain	has	1758:1760	arg1	Glycosylation					1736:1748	Glycosylation	1736:1748	Glycosylation at N183	1736:1756	Glycosylation at N183 has the potential to disrupt OPG structure by interfering with disulphide bond formation and correct protein folding.
16491292	13	88	theme	correct	1851:1857	arg1	folding					1867:1873	correct protein folding	1851:1873	correct protein folding	1851:1873	Glycosylation at N183 has the potential to disrupt OPG structure by interfering with disulphide bond formation and correct protein folding.
16491292	5	89	theme	aspartate	692:700	arg1	deletion					680:687	the deletion	676:687	the deletion of aspartate 182 in OPG	676:711	We recently reported a family with JPD in which affected members were homozygous for an in-frame mutation resulting in the deletion of aspartate 182 in OPG.
16491292	1	90	from	Mutations	123:131	arg1	gene					144:147	the OPG gene	136:147	the OPG gene	136:147	Mutations in the OPG gene cause idiopathic hyperphosphatasia.
16491292	14	91	theme	incorrect	2015:2023	arg1	folding					2033:2039	unstable or incorrect protein folding	2003:2039	unstable or incorrect protein folding	2003:2039	Transient transfection experiments in SaOS2 cells suggest that OPGdeltaD182 is retained within the cell, a typical response to unstable or incorrect protein folding.
16491292	12	92	gly	hyperglycosylation	1668:1685	arg1	residues					1701:1708	asparagine residues	1690:1708	asparagine residues at positions 178 and 183	1690:1733	The apparent higher molecular weight of OPGdeltaD182 compared with the wildtype is a result of hyperglycosylation of asparagine residues at positions 178 and 183.
16491292	13	93	from	N183	1753:1756	arg1	Glycosylation					1736:1748	Glycosylation	1736:1748	Glycosylation at N183	1736:1756	Glycosylation at N183 has the potential to disrupt OPG structure by interfering with disulphide bond formation and correct protein folding.
16491292	14	94	theme	unstable	2003:2010	arg1	folding					2033:2039	unstable or incorrect protein folding	2003:2039	unstable or incorrect protein folding	2003:2039	Transient transfection experiments in SaOS2 cells suggest that OPGdeltaD182 is retained within the cell, a typical response to unstable or incorrect protein folding.
16491292	10	95	theme	Western	1294:1300	arg1	blots					1302:1306	Western blots	1294:1306	Western blots	1294:1306	ELISA and Western blots were used to determine OPG concentrations in cell lysates and conditioned media from transiently transfected cells.
16491292	7	96	theme	murine	917:922	arg1	culture					936:942	a murine bone marrow culture	915:942	a murine bone marrow culture	915:942	MATERIALS AND METHODS: Inhibition of osteoclastogenesis by the recombinant OPG proteins was studied in a murine bone marrow culture.
16491292	12	97	theme	OPGdeltaD182	1613:1624	arg1	weight					1603:1608	higher molecular weight	1586:1608	The apparent higher molecular weight of OPGdeltaD182 compared with the wildtype	1573:1651	The apparent higher molecular weight of OPGdeltaD182 compared with the wildtype is a result of hyperglycosylation of asparagine residues at positions 178 and 183.
16491292	12	97	theme	OPGdeltaD182	1613:1624	arg1	result					1658:1663	a result	1656:1663	a result of hyperglycosylation of asparagine residues at positions 178 and 183	1656:1733	The apparent higher molecular weight of OPGdeltaD182 compared with the wildtype is a result of hyperglycosylation of asparagine residues at positions 178 and 183.
16491292	14	98	from	experiments	1899:1909	arg1	cells					1920:1924	SaOS2 cells	1914:1924	SaOS2 cells	1914:1924	Transient transfection experiments in SaOS2 cells suggest that OPGdeltaD182 is retained within the cell, a typical response to unstable or incorrect protein folding.
16491292	3	99	theme	bone	440:443	arg1	remodeling					445:454	normal bone remodeling	433:454	normal bone remodeling	433:454	Therefore, correct structure and cellular processing of OPG is essential for normal bone remodeling.
16491292	3	100	theme	cellular	389:396	arg1	processing					398:407	cellular processing	389:407	cellular processing	389:407	Therefore, correct structure and cellular processing of OPG is essential for normal bone remodeling.
16491292	0	101	theme	juvenile	40:47	arg1	disease					57:63	juvenile Paget's disease	40:63	juvenile Paget's disease	40:63	Deletion of aspartate 182 in OPG causes juvenile Paget's disease by impairing both protein secretion and binding to RANKL.
16491292	15	102	theme	high	2252:2255	arg1	turnover					2262:2269	high bone turnover	2252:2269	high bone turnover	2252:2269	CONCLUSIONS: Taken together, these data suggest that the deletion of aspartate 182 impairs both the secretion and activity of OPG, which in turn provides an explanation for the increased osteoclastogenesis and high bone turnover observed in JPD patients with this mutation.
16491292	8	103	theme	pull-down	1063:1071	arg1	assay					1073:1077	glutathione-S-transferase (GST) pull-down assay	1031:1077	glutathione-S-transferase (GST) pull-down assay	1031:1077	Binding of wildtype and mutant OPG to RANKL was measured in two experimental systems: glutathione-S-transferase (GST) pull-down assay and surface plasmon resonance.
16491292	8	103	theme	pull-down	1063:1071	arg1	systems					1022:1028	two experimental systems	1005:1028	two experimental systems: glutathione-S-transferase (GST) pull-down assay and surface plasmon resonance	1005:1107	Binding of wildtype and mutant OPG to RANKL was measured in two experimental systems: glutathione-S-transferase (GST) pull-down assay and surface plasmon resonance.
16491292	2	104	theme	biological	300:309	arg1	activity					311:318	reduced biological activity	292:318	reduced biological activity	292:318	We characterized the effects of one such mutation and found that the mutant OPG is poorly secreted and has reduced biological activity compared with the wildtype protein.
16491292	7	105	theme	recombinant	875:885	arg1	proteins					891:898	the recombinant OPG proteins	871:898	the recombinant OPG proteins	871:898	MATERIALS AND METHODS: Inhibition of osteoclastogenesis by the recombinant OPG proteins was studied in a murine bone marrow culture.
16491292	6	106	theme	mutant	796:801	arg1	protein					803:809	the OPGdeltaD182 mutant protein	779:809	the OPGdeltaD182 mutant protein	779:809	Here we report the structural and functional characterization of the OPGdeltaD182 mutant protein.
16491292	5	107	with	family	580:585	arg1	JPD					592:594	JPD	592:594	JPD	592:594	We recently reported a family with JPD in which affected members were homozygous for an in-frame mutation resulting in the deletion of aspartate 182 in OPG.
16491292	9	108	theme	Site-directed	1110:1122	arg1	mutagenesis					1124:1134	Site-directed mutagenesis	1110:1134	Site-directed mutagenesis	1110:1134	Site-directed mutagenesis was used to study the glycosylation of OPGdeltaD182 in two potential glycosylation sites adjacent to the deleted aspartate residue at position 182.
16491292	8	109	theme	plasmon	1091:1097	arg1	resonance					1099:1107	surface plasmon resonance	1083:1107	surface plasmon resonance	1083:1107	Binding of wildtype and mutant OPG to RANKL was measured in two experimental systems: glutathione-S-transferase (GST) pull-down assay and surface plasmon resonance.
16491292	8	109	theme	plasmon	1091:1097	arg1	systems					1022:1028	two experimental systems	1005:1028	two experimental systems: glutathione-S-transferase (GST) pull-down assay and surface plasmon resonance	1005:1107	Binding of wildtype and mutant OPG to RANKL was measured in two experimental systems: glutathione-S-transferase (GST) pull-down assay and surface plasmon resonance.
16491292	10	110	theme	OPG	1331:1333	arg1	concentrations					1335:1348	OPG concentrations	1331:1348	OPG concentrations in cell lysates and conditioned media from transiently transfected cells	1331:1421	ELISA and Western blots were used to determine OPG concentrations in cell lysates and conditioned media from transiently transfected cells.
18180093	0	0	theme	mutagenesis	73:83	arg1	study					85:89	a site-directed mutagenesis study	57:89	a site-directed mutagenesis study	57:89	Effects of mutations and glycosylations on STS activity: a site-directed mutagenesis study.
18180093	4	1	theme	located	480:486	arg1	Histidine					465:473	Histidine 136	465:477	Histidine 136	465:477	Histidine 136, located inside the active site, is crucial for STS activity whereas proline 212, which allows the protein turn into the membrane, is not.
18180093	0	2	theme	site-directed	59:71	arg1	study					85:89	a site-directed mutagenesis study	57:89	a site-directed mutagenesis study	57:89	Effects of mutations and glycosylations on STS activity: a site-directed mutagenesis study.
18180093	4	3	theme	active	499:504	arg1	site					506:509	the active site	495:509	the active site	495:509	Histidine 136, located inside the active site, is crucial for STS activity whereas proline 212, which allows the protein turn into the membrane, is not.
18180093	6	4	theme	immunoblot	763:772	arg1	studies					774:780	immunoblot studies	763:780	immunoblot studies	763:780	However, immunoblot studies revealed that all four N-linked sites are glycosylated to some extent.
18180093	1	5	theme	active	144:149	arg1	steroids					151:158	active steroids	144:158	active steroids	144:158	Steroid sulphatase (STS) catalyses the formation of active steroids from inactive steroid sulphates.
18180093	2	6	with	patients	288:295	arg1	cancer					337:342	oestrogen receptor positive breast cancer	302:342	oestrogen receptor positive breast cancer	302:342	High levels of intra-tumoural STS mRNA are associated with a poor prognosis in post-menopausal patients with oestrogen receptor positive breast cancer.
18180093	5	7	theme	STS	683:685	arg1	activity					687:694	STS activity	683:694	STS activity	683:694	Mutations in glycosylation sites asparagine 47 and 259 decreased STS activity while asparagine 333 and 459 mutations did not affect it.
18180093	0	8	from	Effects	0:6	arg1	activity					47:54	STS activity	43:54	STS activity	43:54	Effects of mutations and glycosylations on STS activity: a site-directed mutagenesis study.
18180093	7	9	theme	human	914:918	arg1	STS					920:922	human STS	914:922	human STS	914:922	In addition, a polyclonal antibody raised in rabbits against human STS was developed and characterised.
18180093	2	10	theme	post-menopausal	272:286	arg1	patients					288:295	post-menopausal patients	272:295	post-menopausal patients with oestrogen receptor positive breast cancer	272:342	High levels of intra-tumoural STS mRNA are associated with a poor prognosis in post-menopausal patients with oestrogen receptor positive breast cancer.
18180093	8	11	theme	STS	998:1000	arg1	structure					1009:1017	the STS enzyme structure	994:1017	the STS enzyme structure	994:1017	These data increase our knowledge of the STS enzyme structure and may help design new STS inhibitors.
18180093	1	12	theme	steroids	151:158	arg1	formation					131:139	the formation	127:139	the formation of active steroids from inactive steroid sulphates	127:190	Steroid sulphatase (STS) catalyses the formation of active steroids from inactive steroid sulphates.
18180093	3	13	theme	protein	388:394	arg1	analysis					360:367	analysis	360:367	analysis of the mutated STS protein	360:394	In this study, analysis of the mutated STS protein showed that N- and C-terminal truncated STS constructs are inactive.
18180093	0	14	dep	study	85:89	arg1	Effects					0:6	Effects	0:6	Effects of mutations and glycosylations on STS activity	0:54	Effects of mutations and glycosylations on STS activity: a site-directed mutagenesis study.
18180093	3	15	theme	truncated	426:434	arg1	constructs					440:449	truncated STS constructs	426:449	truncated STS constructs	426:449	In this study, analysis of the mutated STS protein showed that N- and C-terminal truncated STS constructs are inactive.
18180093	8	16	theme	structure	1009:1017	arg1	knowledge					981:989	our knowledge	977:989	our knowledge of the STS enzyme structure	977:1017	These data increase our knowledge of the STS enzyme structure and may help design new STS inhibitors.
18180093	8	17	theme	new	1039:1041	arg1	inhibitors					1047:1056	design new STS inhibitors	1032:1056	design new STS inhibitors	1032:1056	These data increase our knowledge of the STS enzyme structure and may help design new STS inhibitors.
18180093	1	18	theme	inactive	165:172	arg1	sulphates					182:190	inactive steroid sulphates	165:190	inactive steroid sulphates	165:190	Steroid sulphatase (STS) catalyses the formation of active steroids from inactive steroid sulphates.
18180093	3	19	theme	mutated	376:382	arg1	protein					388:394	the mutated STS protein	372:394	the mutated STS protein	372:394	In this study, analysis of the mutated STS protein showed that N- and C-terminal truncated STS constructs are inactive.
18180093	4	20	theme	STS	527:529	arg1	activity					531:538	STS activity	527:538	STS activity	527:538	Histidine 136, located inside the active site, is crucial for STS activity whereas proline 212, which allows the protein turn into the membrane, is not.
18180093	8	21	theme	enzyme	1002:1007	arg1	structure					1009:1017	the STS enzyme structure	994:1017	the STS enzyme structure	994:1017	These data increase our knowledge of the STS enzyme structure and may help design new STS inhibitors.
18180093	1	22	theme	steroid	174:180	arg1	sulphates					182:190	inactive steroid sulphates	165:190	inactive steroid sulphates	165:190	Steroid sulphatase (STS) catalyses the formation of active steroids from inactive steroid sulphates.
18180093	7	23	theme	polyclonal	868:877	arg1	antibody					879:886	a polyclonal antibody	866:886	a polyclonal antibody raised in rabbits against human STS	866:922	In addition, a polyclonal antibody raised in rabbits against human STS was developed and characterised.
18180093	1	24	theme	Steroid	92:98	arg1	STS					112:114	STS	112:114	STS	112:114	Steroid sulphatase (STS) catalyses the formation of active steroids from inactive steroid sulphates.
18180093	1	24	theme	Steroid	92:98	arg1	sulphatase					100:109	Steroid sulphatase	92:109	Steroid sulphatase (STS)	92:115	Steroid sulphatase (STS) catalyses the formation of active steroids from inactive steroid sulphates.
18180093	3	25	dep	N-	408:409	arg1	constructs					440:449	truncated STS constructs	426:449	truncated STS constructs	426:449	In this study, analysis of the mutated STS protein showed that N- and C-terminal truncated STS constructs are inactive.
18180093	0	26	theme	mutations	11:19	arg1	Effects					0:6	Effects	0:6	Effects of mutations and glycosylations on STS activity	0:54	Effects of mutations and glycosylations on STS activity: a site-directed mutagenesis study.
18180093	8	27	theme	design	1032:1037	arg1	inhibitors					1047:1056	design new STS inhibitors	1032:1056	design new STS inhibitors	1032:1056	These data increase our knowledge of the STS enzyme structure and may help design new STS inhibitors.
18180093	2	28	theme	mRNA	227:230	arg1	levels					198:203	High levels	193:203	High levels of intra-tumoural STS mRNA	193:230	High levels of intra-tumoural STS mRNA are associated with a poor prognosis in post-menopausal patients with oestrogen receptor positive breast cancer.
18180093	3	29	theme	STS	436:438	arg1	constructs					440:449	truncated STS constructs	426:449	truncated STS constructs	426:449	In this study, analysis of the mutated STS protein showed that N- and C-terminal truncated STS constructs are inactive.
18180093	0	30	theme	glycosylations	25:38	arg1	Effects					0:6	Effects	0:6	Effects of mutations and glycosylations on STS activity	0:54	Effects of mutations and glycosylations on STS activity: a site-directed mutagenesis study.
18180093	5	31	dep	sites	645:649	arg1	asparagine					651:660	asparagine 47	651:663	asparagine 47	651:663	Mutations in glycosylation sites asparagine 47 and 259 decreased STS activity while asparagine 333 and 459 mutations did not affect it.
18180093	5	31	dep	sites	645:649	arg1	259					669:671	259	669:671	259	669:671	Mutations in glycosylation sites asparagine 47 and 259 decreased STS activity while asparagine 333 and 459 mutations did not affect it.
18180093	6	32	theme	N-linked	805:812	arg1	sites					814:818	all four N-linked sites	796:818	all four N-linked sites	796:818	However, immunoblot studies revealed that all four N-linked sites are glycosylated to some extent.
18180093	2	33	theme	STS	223:225	arg1	mRNA					227:230	intra-tumoural STS mRNA	208:230	intra-tumoural STS mRNA	208:230	High levels of intra-tumoural STS mRNA are associated with a poor prognosis in post-menopausal patients with oestrogen receptor positive breast cancer.
18180093	3	34	theme	STS	384:386	arg1	protein					388:394	the mutated STS protein	372:394	the mutated STS protein	372:394	In this study, analysis of the mutated STS protein showed that N- and C-terminal truncated STS constructs are inactive.
18180093	5	35	from	Mutations	618:626	arg1	sites					645:649	glycosylation sites asparagine 47 and 259	631:671	glycosylation sites asparagine 47 and 259	631:671	Mutations in glycosylation sites asparagine 47 and 259 decreased STS activity while asparagine 333 and 459 mutations did not affect it.
18180093	8	36	theme	STS	1043:1045	arg1	inhibitors					1047:1056	design new STS inhibitors	1032:1056	design new STS inhibitors	1032:1056	These data increase our knowledge of the STS enzyme structure and may help design new STS inhibitors.
18180093	2	37	theme	intra-tumoural	208:221	arg1	mRNA					227:230	intra-tumoural STS mRNA	208:230	intra-tumoural STS mRNA	208:230	High levels of intra-tumoural STS mRNA are associated with a poor prognosis in post-menopausal patients with oestrogen receptor positive breast cancer.
18180093	6	38	link	N-linked	805:812	arg1	sites					814:818	all four N-linked sites	796:818	all four N-linked sites	796:818	However, immunoblot studies revealed that all four N-linked sites are glycosylated to some extent.
18180093	0	39	theme	STS	43:45	arg1	activity					47:54	STS activity	43:54	STS activity	43:54	Effects of mutations and glycosylations on STS activity: a site-directed mutagenesis study.
18180093	5	40	theme	glycosylation	631:643	arg1	sites					645:649	glycosylation sites asparagine 47 and 259	631:671	glycosylation sites asparagine 47 and 259	631:671	Mutations in glycosylation sites asparagine 47 and 259 decreased STS activity while asparagine 333 and 459 mutations did not affect it.
18180093	1	41	from	sulphates	182:190	arg1	formation					131:139	the formation	127:139	the formation of active steroids from inactive steroid sulphates	127:190	Steroid sulphatase (STS) catalyses the formation of active steroids from inactive steroid sulphates.
18180093	2	42	from	prognosis	259:267	arg1	patients					288:295	post-menopausal patients	272:295	post-menopausal patients with oestrogen receptor positive breast cancer	272:342	High levels of intra-tumoural STS mRNA are associated with a poor prognosis in post-menopausal patients with oestrogen receptor positive breast cancer.
18180093	4	43	dep	located	480:486	arg1	inside					488:493	inside	488:493	inside the active site	488:509	Histidine 136, located inside the active site, is crucial for STS activity whereas proline 212, which allows the protein turn into the membrane, is not.
18180093	2	44	theme	High	193:196	arg1	levels					198:203	High levels	193:203	High levels of intra-tumoural STS mRNA	193:230	High levels of intra-tumoural STS mRNA are associated with a poor prognosis in post-menopausal patients with oestrogen receptor positive breast cancer.
18180093	2	45	theme	breast	330:335	arg1	cancer					337:342	oestrogen receptor positive breast cancer	302:342	oestrogen receptor positive breast cancer	302:342	High levels of intra-tumoural STS mRNA are associated with a poor prognosis in post-menopausal patients with oestrogen receptor positive breast cancer.
18180093	2	46	theme	poor	254:257	arg1	prognosis					259:267	a poor prognosis	252:267	a poor prognosis in post-menopausal patients with oestrogen receptor positive breast cancer	252:342	High levels of intra-tumoural STS mRNA are associated with a poor prognosis in post-menopausal patients with oestrogen receptor positive breast cancer.
18180093	2	47	theme	positive	321:328	arg1	cancer					337:342	oestrogen receptor positive breast cancer	302:342	oestrogen receptor positive breast cancer	302:342	High levels of intra-tumoural STS mRNA are associated with a poor prognosis in post-menopausal patients with oestrogen receptor positive breast cancer.
18180093	6	48	gly	glycosylated	824:835	arg1	sites					814:818	all four N-linked sites	796:818	all four N-linked sites	796:818	However, immunoblot studies revealed that all four N-linked sites are glycosylated to some extent.
18180093	5	49	gly	glycosylation	631:643	arg2	sites					645:649	glycosylation sites asparagine 47 and 259	631:671	glycosylation sites asparagine 47 and 259	631:671	Mutations in glycosylation sites asparagine 47 and 259 decreased STS activity while asparagine 333 and 459 mutations did not affect it.
18180093	4	50	theme	protein	578:584	arg1	turn					586:589	the protein turn	574:589	the protein turn	574:589	Histidine 136, located inside the active site, is crucial for STS activity whereas proline 212, which allows the protein turn into the membrane, is not.
26424659	3	0	from	Thr	335:337	arg1	O-fucosylated					318:330	O-fucosylated	318:330	O-fucosylated	318:330	In this report, we demonstrated that CCN1 is O-fucosylated at Thr(242) using mass spectrometry.
26424659	4	1	theme	surface	436:442	arg1	localization					444:455	the cell surface localization	427:455	the cell surface localization	427:455	Deficiency of O-fucosylation resulted in the decrement of the cell surface localization and the secretion of CCN1.
26424659	5	2	theme	O-fucosyltransferase	518:537	arg1	knockdown					497:505	knockdown	497:505	knockdown of protein O-fucosyltransferase 2, which modifies a specific Ser/Thr residue in the TSR1 domain,	497:602	Furthermore, knockdown of protein O-fucosyltransferase 2, which modifies a specific Ser/Thr residue in the TSR1 domain, decreased secreted levels of CCN1.
26424659	4	3	theme	cell	431:434	arg1	localization					444:455	the cell surface localization	427:455	the cell surface localization	427:455	Deficiency of O-fucosylation resulted in the decrement of the cell surface localization and the secretion of CCN1.
26424659	6	4	gly	O-fucosylation	671:684	arg1	242					701:703	242	701:703	242	701:703	These results demonstrated that O-fucosylation of CCN1 at Thr(242) regulates its secretion.
26424659	6	4	gly	O-fucosylation	671:684	arg1	Thr					697:699	Thr	697:699	Thr(242)	697:704	These results demonstrated that O-fucosylation of CCN1 at Thr(242) regulates its secretion.
26424659	6	4	gly	O-fucosylation	671:684	arg1	CCN1					689:692	CCN1	689:692	CCN1	689:692	These results demonstrated that O-fucosylation of CCN1 at Thr(242) regulates its secretion.
26424659	5	5	theme	TSR1	591:594	arg1	domain					596:601	the TSR1 domain	587:601	the TSR1 domain	587:601	Furthermore, knockdown of protein O-fucosyltransferase 2, which modifies a specific Ser/Thr residue in the TSR1 domain, decreased secreted levels of CCN1.
26424659	3	6	gly	O-fucosylated	318:330	arg2	Thr					335:337	Thr(242)	335:342	Thr(242) using mass spectrometry	335:366	In this report, we demonstrated that CCN1 is O-fucosylated at Thr(242) using mass spectrometry.
26424659	3	6	gly	O-fucosylated	318:330	arg1	CCN1					310:313	CCN1	310:313	CCN1	310:313	In this report, we demonstrated that CCN1 is O-fucosylated at Thr(242) using mass spectrometry.
26424659	1	7	theme	matricellular	58:70	arg1	ligand					121:126	a secreted ligand	110:126	a secreted ligand	110:126	The matricellular protein CCN1, also known as Cyr61, is a secreted ligand and has numerous functions.
26424659	1	7	theme	matricellular	58:70	arg1	CCN1					80:83	The matricellular protein CCN1	54:83	The matricellular protein CCN1	54:83	The matricellular protein CCN1, also known as Cyr61, is a secreted ligand and has numerous functions.
26424659	3	8	theme	mass	350:353	arg1	spectrometry					355:366	mass spectrometry	350:366	mass spectrometry	350:366	In this report, we demonstrated that CCN1 is O-fucosylated at Thr(242) using mass spectrometry.
26424659	1	9	theme	protein	72:78	arg1	ligand					121:126	a secreted ligand	110:126	a secreted ligand	110:126	The matricellular protein CCN1, also known as Cyr61, is a secreted ligand and has numerous functions.
26424659	1	9	theme	protein	72:78	arg1	CCN1					80:83	The matricellular protein CCN1	54:83	The matricellular protein CCN1	54:83	The matricellular protein CCN1, also known as Cyr61, is a secreted ligand and has numerous functions.
26424659	1	10	theme	numerous	136:143	arg1	functions					145:153	numerous functions	136:153	numerous functions	136:153	The matricellular protein CCN1, also known as Cyr61, is a secreted ligand and has numerous functions.
26424659	5	11	theme	specific	559:566	arg1	residue					576:582	a specific Ser/Thr residue	557:582	a specific Ser/Thr residue in the TSR1 domain	557:601	Furthermore, knockdown of protein O-fucosyltransferase 2, which modifies a specific Ser/Thr residue in the TSR1 domain, decreased secreted levels of CCN1.
26424659	2	12	from	site	205:208	arg1	domain					253:258	the thrombospondin type-1 repeat (TSR1) domain	213:258	the thrombospondin type-1 repeat (TSR1) domain	213:258	Human CCN1 contains one predicted O-fucosylation site in the thrombospondin type-1 repeat (TSR1) domain at Thr(242).
26424659	4	13	theme	CCN1	478:481	arg1	secretion					465:473	the secretion	461:473	the secretion of CCN1	461:481	Deficiency of O-fucosylation resulted in the decrement of the cell surface localization and the secretion of CCN1.
26424659	4	13	theme	CCN1	478:481	arg1	decrement					414:422	the decrement	410:422	the decrement of the cell surface localization	410:455	Deficiency of O-fucosylation resulted in the decrement of the cell surface localization and the secretion of CCN1.
26424659	5	14	theme	Ser/Thr	568:574	arg1	residue					576:582	a specific Ser/Thr residue	557:582	a specific Ser/Thr residue in the TSR1 domain	557:601	Furthermore, knockdown of protein O-fucosyltransferase 2, which modifies a specific Ser/Thr residue in the TSR1 domain, decreased secreted levels of CCN1.
26424659	5	15	theme	protein	510:516	arg1	O-fucosyltransferase					518:537	protein O-fucosyltransferase 2	510:539	protein O-fucosyltransferase 2	510:539	Furthermore, knockdown of protein O-fucosyltransferase 2, which modifies a specific Ser/Thr residue in the TSR1 domain, decreased secreted levels of CCN1.
26424659	0	16	theme	CCN1	18:21	arg1	O-Fucosylation					0:13	O-Fucosylation	0:13	O-Fucosylation of CCN1	0:21	O-Fucosylation of CCN1 is required for its secretion.
26424659	2	17	theme	TSR1	247:250	arg1	domain					253:258	the thrombospondin type-1 repeat (TSR1) domain	213:258	the thrombospondin type-1 repeat (TSR1) domain	213:258	Human CCN1 contains one predicted O-fucosylation site in the thrombospondin type-1 repeat (TSR1) domain at Thr(242).
26424659	6	18	from	Thr	697:699	arg1	O-fucosylation					671:684	O-fucosylation	671:684	O-fucosylation of CCN1 at Thr(242)	671:704	These results demonstrated that O-fucosylation of CCN1 at Thr(242) regulates its secretion.
26424659	5	19	theme	CCN1	633:636	arg1	levels					623:628	secreted levels	614:628	secreted levels of CCN1	614:636	Furthermore, knockdown of protein O-fucosyltransferase 2, which modifies a specific Ser/Thr residue in the TSR1 domain, decreased secreted levels of CCN1.
26424659	0	20	gly	O-Fucosylation	0:13	arg1	CCN1					18:21	CCN1	18:21	CCN1	18:21	O-Fucosylation of CCN1 is required for its secretion.
26424659	2	21	contain	contains	167:174	arg1	CCN1					162:165	Human CCN1	156:165	Human CCN1	156:165	Human CCN1 contains one predicted O-fucosylation site in the thrombospondin type-1 repeat (TSR1) domain at Thr(242).
26424659	2	21	contain	contains	167:174	arg2	CCN1					162:165	Human CCN1	156:165	Human CCN1	156:165	Human CCN1 contains one predicted O-fucosylation site in the thrombospondin type-1 repeat (TSR1) domain at Thr(242).
26424659	2	21	contain	contains	167:174	arg1	242					267:269	242	267:269	242	267:269	Human CCN1 contains one predicted O-fucosylation site in the thrombospondin type-1 repeat (TSR1) domain at Thr(242).
26424659	2	21	contain	contains	167:174	arg1	Thr					263:265	Thr	263:265	Thr(242)	263:270	Human CCN1 contains one predicted O-fucosylation site in the thrombospondin type-1 repeat (TSR1) domain at Thr(242).
26424659	2	21	contain	contains	167:174	arg2	site					205:208	one predicted O-fucosylation site	176:208	one predicted O-fucosylation site in the thrombospondin type-1 repeat (TSR1) domain	176:258	Human CCN1 contains one predicted O-fucosylation site in the thrombospondin type-1 repeat (TSR1) domain at Thr(242).
26424659	4	22	theme	O-fucosylation	383:396	arg1	Deficiency					369:378	Deficiency	369:378	Deficiency of O-fucosylation	369:396	Deficiency of O-fucosylation resulted in the decrement of the cell surface localization and the secretion of CCN1.
26424659	4	23	theme	localization	444:455	arg1	secretion					465:473	the secretion	461:473	the secretion of CCN1	461:481	Deficiency of O-fucosylation resulted in the decrement of the cell surface localization and the secretion of CCN1.
26424659	4	23	theme	localization	444:455	arg1	decrement					414:422	the decrement	410:422	the decrement of the cell surface localization	410:455	Deficiency of O-fucosylation resulted in the decrement of the cell surface localization and the secretion of CCN1.
26424659	1	24	contain	has	132:134	arg1	ligand					121:126	a secreted ligand	110:126	a secreted ligand	110:126	The matricellular protein CCN1, also known as Cyr61, is a secreted ligand and has numerous functions.
26424659	1	24	contain	has	132:134	arg1	CCN1					80:83	The matricellular protein CCN1	54:83	The matricellular protein CCN1	54:83	The matricellular protein CCN1, also known as Cyr61, is a secreted ligand and has numerous functions.
26424659	1	24	contain	has	132:134	arg2	functions					145:153	numerous functions	136:153	numerous functions	136:153	The matricellular protein CCN1, also known as Cyr61, is a secreted ligand and has numerous functions.
26424659	2	25	theme	O-fucosylation	190:203	arg1	site					205:208	one predicted O-fucosylation site	176:208	one predicted O-fucosylation site in the thrombospondin type-1 repeat (TSR1) domain	176:258	Human CCN1 contains one predicted O-fucosylation site in the thrombospondin type-1 repeat (TSR1) domain at Thr(242).
26424659	6	26	theme	CCN1	689:692	arg1	O-fucosylation					671:684	O-fucosylation	671:684	O-fucosylation of CCN1 at Thr(242)	671:704	These results demonstrated that O-fucosylation of CCN1 at Thr(242) regulates its secretion.
26424659	2	27	gly	O-fucosylation	190:203	arg2	site					205:208	one predicted O-fucosylation site	176:208	one predicted O-fucosylation site in the thrombospondin type-1 repeat (TSR1) domain	176:258	Human CCN1 contains one predicted O-fucosylation site in the thrombospondin type-1 repeat (TSR1) domain at Thr(242).
26424659	5	28	from	residue	576:582	arg1	domain					596:601	the TSR1 domain	587:601	the TSR1 domain	587:601	Furthermore, knockdown of protein O-fucosyltransferase 2, which modifies a specific Ser/Thr residue in the TSR1 domain, decreased secreted levels of CCN1.
26424659	2	29	theme	predicted	180:188	arg1	site					205:208	one predicted O-fucosylation site	176:208	one predicted O-fucosylation site in the thrombospondin type-1 repeat (TSR1) domain	176:258	Human CCN1 contains one predicted O-fucosylation site in the thrombospondin type-1 repeat (TSR1) domain at Thr(242).
26424659	2	30	theme	repeat	239:244	arg1	domain					253:258	the thrombospondin type-1 repeat (TSR1) domain	213:258	the thrombospondin type-1 repeat (TSR1) domain	213:258	Human CCN1 contains one predicted O-fucosylation site in the thrombospondin type-1 repeat (TSR1) domain at Thr(242).
26424659	5	31	theme	secreted	614:621	arg1	levels					623:628	secreted levels	614:628	secreted levels of CCN1	614:636	Furthermore, knockdown of protein O-fucosyltransferase 2, which modifies a specific Ser/Thr residue in the TSR1 domain, decreased secreted levels of CCN1.
26424659	2	32	theme	type-1	232:237	arg1	domain					253:258	the thrombospondin type-1 repeat (TSR1) domain	213:258	the thrombospondin type-1 repeat (TSR1) domain	213:258	Human CCN1 contains one predicted O-fucosylation site in the thrombospondin type-1 repeat (TSR1) domain at Thr(242).
26424659	2	33	theme	Human	156:160	arg1	CCN1					162:165	Human CCN1	156:165	Human CCN1	156:165	Human CCN1 contains one predicted O-fucosylation site in the thrombospondin type-1 repeat (TSR1) domain at Thr(242).
26424659	2	34	theme	thrombospondin	217:230	arg1	domain					253:258	the thrombospondin type-1 repeat (TSR1) domain	213:258	the thrombospondin type-1 repeat (TSR1) domain	213:258	Human CCN1 contains one predicted O-fucosylation site in the thrombospondin type-1 repeat (TSR1) domain at Thr(242).
26424659	1	35	theme	secreted	112:119	arg1	ligand					121:126	a secreted ligand	110:126	a secreted ligand	110:126	The matricellular protein CCN1, also known as Cyr61, is a secreted ligand and has numerous functions.
26424659	1	35	theme	secreted	112:119	arg1	CCN1					80:83	The matricellular protein CCN1	54:83	The matricellular protein CCN1	54:83	The matricellular protein CCN1, also known as Cyr61, is a secreted ligand and has numerous functions.
17082223	3	0	gly	glycosylated	795:806	arg1	site					786:789	each site	781:789	each site	781:789	Immunoblot and glycosidase cleavage analysis demonstrated that each site was glycosylated.
17082223	4	1	theme	taurocholate	838:849	arg1	activity					861:868	taurocholate transport activity	838:868	taurocholate transport activity	838:868	Removal of glycans decreased taurocholate transport activity as determined in polarized MDCK II cells.
17082223	8	2	theme	glycans	1502:1508	arg1	critical					1514:1521	critical	1514:1521	critical	1514:1521	To determine whether a specific glycosylation site or the number of glycans was critical for protein stability, we studied the protein expression of combinations of N-glycan-deficient mutants and observed that Bsep with one glycan was considerably unstable compared with Bsep harboring two or more glycans.
17082223	8	2	theme	glycans	1502:1508	arg1	glycans					1502:1508	glycans	1502:1508	glycans	1502:1508	To determine whether a specific glycosylation site or the number of glycans was critical for protein stability, we studied the protein expression of combinations of N-glycan-deficient mutants and observed that Bsep with one glycan was considerably unstable compared with Bsep harboring two or more glycans.
17082223	8	2	theme	glycans	1502:1508	arg1	site					1480:1483	a specific glycosylation site	1455:1483	a specific glycosylation site	1455:1483	To determine whether a specific glycosylation site or the number of glycans was critical for protein stability, we studied the protein expression of combinations of N-glycan-deficient mutants and observed that Bsep with one glycan was considerably unstable compared with Bsep harboring two or more glycans.
17082223	8	2	theme	glycans	1502:1508	arg1	number					1492:1497	the number	1488:1497	the number of glycans	1488:1508	To determine whether a specific glycosylation site or the number of glycans was critical for protein stability, we studied the protein expression of combinations of N-glycan-deficient mutants and observed that Bsep with one glycan was considerably unstable compared with Bsep harboring two or more glycans.
17082223	2	3	theme	glycosylation	458:470	arg1	Asn					513:515	Asn(125)	513:520	Asn(125)	513:520	Rat Bsep was fused with yellow fluorescent protein, and the following mutants, in which Asn residues of putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125)) were sequentially replaced with Gln, were constructed by site-directed mutagenesis: single N109Q, double N109Q + N116Q, triple N109Q + N116Q + N122Q, and quadruple N109Q + N116Q + N122Q + N125Q.
17082223	2	3	theme	glycosylation	458:470	arg1	Asn					499:501	Asn(122)	499:506	Asn(122)	499:506	Rat Bsep was fused with yellow fluorescent protein, and the following mutants, in which Asn residues of putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125)) were sequentially replaced with Gln, were constructed by site-directed mutagenesis: single N109Q, double N109Q + N116Q, triple N109Q + N116Q + N122Q, and quadruple N109Q + N116Q + N122Q + N125Q.
17082223	2	3	theme	glycosylation	458:470	arg1	Asn					489:491	Asn(116)	489:496	Asn(116)	489:496	Rat Bsep was fused with yellow fluorescent protein, and the following mutants, in which Asn residues of putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125)) were sequentially replaced with Gln, were constructed by site-directed mutagenesis: single N109Q, double N109Q + N116Q, triple N109Q + N116Q + N122Q, and quadruple N109Q + N116Q + N122Q + N125Q.
17082223	2	3	theme	glycosylation	458:470	arg1	Asn					479:481	Asn(109)	479:486	Asn(109)	479:486	Rat Bsep was fused with yellow fluorescent protein, and the following mutants, in which Asn residues of putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125)) were sequentially replaced with Gln, were constructed by site-directed mutagenesis: single N109Q, double N109Q + N116Q, triple N109Q + N116Q + N122Q, and quadruple N109Q + N116Q + N122Q + N125Q.
17082223	2	3	theme	glycosylation	458:470	arg1	sites					472:476	putative glycosylation sites	449:476	putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125))	449:521	Rat Bsep was fused with yellow fluorescent protein, and the following mutants, in which Asn residues of putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125)) were sequentially replaced with Gln, were constructed by site-directed mutagenesis: single N109Q, double N109Q + N116Q, triple N109Q + N116Q + N122Q, and quadruple N109Q + N116Q + N122Q + N125Q.
17082223	5	4	from	h	1041:1041	arg1	cells					1123:1127	quadruple-mutant cells	1106:1127	quadruple-mutant cells	1106:1127	This decrease resulted from rapid decay of the mutant Bsep protein; biochemical half-lives were 3.76, 3.65, 3.24, 1.35, and 0.52 h in wild-type, single-mutant, double-mutant, triple-mutant, and quadruple-mutant cells, respectively.
17082223	5	4	from	h	1041:1041	arg1	single-mutant					1057:1069	single-mutant	1057:1069	single-mutant	1057:1069	This decrease resulted from rapid decay of the mutant Bsep protein; biochemical half-lives were 3.76, 3.65, 3.24, 1.35, and 0.52 h in wild-type, single-mutant, double-mutant, triple-mutant, and quadruple-mutant cells, respectively.
17082223	4	5	theme	II	902:903	arg1	cells					905:909	polarized MDCK II cells	887:909	polarized MDCK II cells	887:909	Removal of glycans decreased taurocholate transport activity as determined in polarized MDCK II cells.
17082223	8	6	theme	protein	1527:1533	arg1	stability					1535:1543	protein stability	1527:1543	protein stability	1527:1543	To determine whether a specific glycosylation site or the number of glycans was critical for protein stability, we studied the protein expression of combinations of N-glycan-deficient mutants and observed that Bsep with one glycan was considerably unstable compared with Bsep harboring two or more glycans.
17082223	9	7	link	N-linked	1769:1776	arg1	glycans					1778:1784	at least two N-linked glycans	1756:1784	at least two N-linked glycans	1756:1784	In conclusion, at least two N-linked glycans are required for Bsep protein stability, intracellular trafficking, and function in the apical membrane.
17082223	2	8	theme	site-directed	580:592	arg1	mutagenesis					594:604	site-directed mutagenesis	580:604	site-directed mutagenesis	580:604	Rat Bsep was fused with yellow fluorescent protein, and the following mutants, in which Asn residues of putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125)) were sequentially replaced with Gln, were constructed by site-directed mutagenesis: single N109Q, double N109Q + N116Q, triple N109Q + N116Q + N122Q, and quadruple N109Q + N116Q + N122Q + N125Q.
17082223	1	9	theme	cassette	329:336	arg1	B11					338:340	ATP-binding cassette B11	317:340	ATP-binding cassette B11	317:340	The aim of this study was to determine the role of N-linked glycosylation in protein stability, intracellular trafficking, and bile acid transport activity of the bile salt export pump [Bsep (ATP-binding cassette B11)].
17082223	1	9	theme	cassette	329:336	arg1	pump					305:308	the bile salt export pump [Bsep	284:314	the bile salt export pump [Bsep (ATP-binding cassette B11)]	284:342	The aim of this study was to determine the role of N-linked glycosylation in protein stability, intracellular trafficking, and bile acid transport activity of the bile salt export pump [Bsep (ATP-binding cassette B11)].
17082223	1	10	theme	intracellular	221:233	arg1	trafficking					235:245	intracellular trafficking	221:245	intracellular trafficking	221:245	The aim of this study was to determine the role of N-linked glycosylation in protein stability, intracellular trafficking, and bile acid transport activity of the bile salt export pump [Bsep (ATP-binding cassette B11)].
17082223	0	11	theme	MDCK	110:113	arg1	cells					118:122	MDCK II cells	110:122	MDCK II cells	110:122	Two N-linked glycans are required to maintain the transport activity of the bile salt export pump (ABCB11) in MDCK II cells.
17082223	1	12	from	role	168:171	arg1	trafficking					235:245	intracellular trafficking	221:245	intracellular trafficking	221:245	The aim of this study was to determine the role of N-linked glycosylation in protein stability, intracellular trafficking, and bile acid transport activity of the bile salt export pump [Bsep (ATP-binding cassette B11)].
17082223	1	12	from	role	168:171	arg1	activity					272:279	bile acid transport activity	252:279	bile acid transport activity	252:279	The aim of this study was to determine the role of N-linked glycosylation in protein stability, intracellular trafficking, and bile acid transport activity of the bile salt export pump [Bsep (ATP-binding cassette B11)].
17082223	1	12	from	role	168:171	arg1	stability					210:218	protein stability	202:218	protein stability	202:218	The aim of this study was to determine the role of N-linked glycosylation in protein stability, intracellular trafficking, and bile acid transport activity of the bile salt export pump [Bsep (ATP-binding cassette B11)].
17082223	8	13	theme	protein	1561:1567	arg1	expression					1569:1578	the protein expression	1557:1578	the protein expression of combinations of N-glycan-deficient mutants	1557:1624	To determine whether a specific glycosylation site or the number of glycans was critical for protein stability, we studied the protein expression of combinations of N-glycan-deficient mutants and observed that Bsep with one glycan was considerably unstable compared with Bsep harboring two or more glycans.
17082223	9	14	theme	N-linked	1769:1776	arg1	glycans					1778:1784	at least two N-linked glycans	1756:1784	at least two N-linked glycans	1756:1784	In conclusion, at least two N-linked glycans are required for Bsep protein stability, intracellular trafficking, and function in the apical membrane.
17082223	6	15	theme	single-	1158:1164	arg1	proteins					1184:1191	Wild-type and single- and double-mutant proteins	1144:1191	Wild-type and single- and double-mutant proteins	1144:1191	Wild-type and single- and double-mutant proteins were distributed exclusively along the apical membranes, whereas triple- and quadruple-mutant proteins remained intracellular.
17082223	2	16	gly	glycosylation	458:470	arg2	Asn					499:501	Asn(122)	499:506	Asn(122)	499:506	Rat Bsep was fused with yellow fluorescent protein, and the following mutants, in which Asn residues of putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125)) were sequentially replaced with Gln, were constructed by site-directed mutagenesis: single N109Q, double N109Q + N116Q, triple N109Q + N116Q + N122Q, and quadruple N109Q + N116Q + N122Q + N125Q.
17082223	2	16	gly	glycosylation	458:470	arg2	Asn					479:481	Asn(109)	479:486	Asn(109)	479:486	Rat Bsep was fused with yellow fluorescent protein, and the following mutants, in which Asn residues of putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125)) were sequentially replaced with Gln, were constructed by site-directed mutagenesis: single N109Q, double N109Q + N116Q, triple N109Q + N116Q + N122Q, and quadruple N109Q + N116Q + N122Q + N125Q.
17082223	2	16	gly	glycosylation	458:470	arg2	Asn					489:491	Asn(116)	489:496	Asn(116)	489:496	Rat Bsep was fused with yellow fluorescent protein, and the following mutants, in which Asn residues of putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125)) were sequentially replaced with Gln, were constructed by site-directed mutagenesis: single N109Q, double N109Q + N116Q, triple N109Q + N116Q + N122Q, and quadruple N109Q + N116Q + N122Q + N125Q.
17082223	2	16	gly	glycosylation	458:470	arg2	sites					472:476	putative glycosylation sites	449:476	putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125))	449:521	Rat Bsep was fused with yellow fluorescent protein, and the following mutants, in which Asn residues of putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125)) were sequentially replaced with Gln, were constructed by site-directed mutagenesis: single N109Q, double N109Q + N116Q, triple N109Q + N116Q + N122Q, and quadruple N109Q + N116Q + N122Q + N125Q.
17082223	2	16	gly	glycosylation	458:470	arg2	Asn					513:515	Asn(125)	513:520	Asn(125)	513:520	Rat Bsep was fused with yellow fluorescent protein, and the following mutants, in which Asn residues of putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125)) were sequentially replaced with Gln, were constructed by site-directed mutagenesis: single N109Q, double N109Q + N116Q, triple N109Q + N116Q + N122Q, and quadruple N109Q + N116Q + N122Q + N125Q.
17082223	6	17	theme	Wild-type	1144:1152	arg1	proteins					1184:1191	Wild-type and single- and double-mutant proteins	1144:1191	Wild-type and single- and double-mutant proteins	1144:1191	Wild-type and single- and double-mutant proteins were distributed exclusively along the apical membranes, whereas triple- and quadruple-mutant proteins remained intracellular.
17082223	2	18	theme	Asn	433:435	arg1	residues					437:444	Asn residues	433:444	Asn residues of putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125))	433:521	Rat Bsep was fused with yellow fluorescent protein, and the following mutants, in which Asn residues of putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125)) were sequentially replaced with Gln, were constructed by site-directed mutagenesis: single N109Q, double N109Q + N116Q, triple N109Q + N116Q + N122Q, and quadruple N109Q + N116Q + N122Q + N125Q.
17082223	2	18	theme	Asn	433:435	arg1	sites					472:476	putative glycosylation sites	449:476	putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125))	449:521	Rat Bsep was fused with yellow fluorescent protein, and the following mutants, in which Asn residues of putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125)) were sequentially replaced with Gln, were constructed by site-directed mutagenesis: single N109Q, double N109Q + N116Q, triple N109Q + N116Q + N122Q, and quadruple N109Q + N116Q + N122Q + N125Q.
17082223	0	19	theme	bile	76:79	arg1	ABCB11					99:104	ABCB11	99:104	ABCB11	99:104	Two N-linked glycans are required to maintain the transport activity of the bile salt export pump (ABCB11) in MDCK II cells.
17082223	0	19	theme	bile	76:79	arg1	pump					93:96	the bile salt export pump	72:96	the bile salt export pump (ABCB11)	72:105	Two N-linked glycans are required to maintain the transport activity of the bile salt export pump (ABCB11) in MDCK II cells.
17082223	1	20	theme	salt	293:296	arg1	B11					338:340	ATP-binding cassette B11	317:340	ATP-binding cassette B11	317:340	The aim of this study was to determine the role of N-linked glycosylation in protein stability, intracellular trafficking, and bile acid transport activity of the bile salt export pump [Bsep (ATP-binding cassette B11)].
17082223	1	20	theme	salt	293:296	arg1	pump					305:308	the bile salt export pump [Bsep	284:314	the bile salt export pump [Bsep (ATP-binding cassette B11)]	284:342	The aim of this study was to determine the role of N-linked glycosylation in protein stability, intracellular trafficking, and bile acid transport activity of the bile salt export pump [Bsep (ATP-binding cassette B11)].
17082223	8	21	theme	mutants	1618:1624	arg1	combinations					1583:1594	combinations	1583:1594	combinations of N-glycan-deficient mutants	1583:1624	To determine whether a specific glycosylation site or the number of glycans was critical for protein stability, we studied the protein expression of combinations of N-glycan-deficient mutants and observed that Bsep with one glycan was considerably unstable compared with Bsep harboring two or more glycans.
17082223	9	22	theme	protein	1808:1814	arg1	stability					1816:1824	Bsep protein stability	1803:1824	Bsep protein stability	1803:1824	In conclusion, at least two N-linked glycans are required for Bsep protein stability, intracellular trafficking, and function in the apical membrane.
17082223	0	23	theme	export	86:91	arg1	ABCB11					99:104	ABCB11	99:104	ABCB11	99:104	Two N-linked glycans are required to maintain the transport activity of the bile salt export pump (ABCB11) in MDCK II cells.
17082223	0	23	theme	export	86:91	arg1	pump					93:96	the bile salt export pump	72:96	the bile salt export pump (ABCB11)	72:105	Two N-linked glycans are required to maintain the transport activity of the bile salt export pump (ABCB11) in MDCK II cells.
17082223	1	24	theme	pump	305:308	arg1	trafficking					235:245	intracellular trafficking	221:245	intracellular trafficking	221:245	The aim of this study was to determine the role of N-linked glycosylation in protein stability, intracellular trafficking, and bile acid transport activity of the bile salt export pump [Bsep (ATP-binding cassette B11)].
17082223	1	24	theme	pump	305:308	arg1	activity					272:279	bile acid transport activity	252:279	bile acid transport activity	252:279	The aim of this study was to determine the role of N-linked glycosylation in protein stability, intracellular trafficking, and bile acid transport activity of the bile salt export pump [Bsep (ATP-binding cassette B11)].
17082223	1	24	theme	pump	305:308	arg1	stability					210:218	protein stability	202:218	protein stability	202:218	The aim of this study was to determine the role of N-linked glycosylation in protein stability, intracellular trafficking, and bile acid transport activity of the bile salt export pump [Bsep (ATP-binding cassette B11)].
17082223	5	25	theme	quadruple-mutant	1106:1121	arg1	cells					1123:1127	quadruple-mutant cells	1106:1127	quadruple-mutant cells	1106:1127	This decrease resulted from rapid decay of the mutant Bsep protein; biochemical half-lives were 3.76, 3.65, 3.24, 1.35, and 0.52 h in wild-type, single-mutant, double-mutant, triple-mutant, and quadruple-mutant cells, respectively.
17082223	5	26	theme	Bsep	966:969	arg1	protein					971:977	the mutant Bsep protein	955:977	the mutant Bsep protein	955:977	This decrease resulted from rapid decay of the mutant Bsep protein; biochemical half-lives were 3.76, 3.65, 3.24, 1.35, and 0.52 h in wild-type, single-mutant, double-mutant, triple-mutant, and quadruple-mutant cells, respectively.
17082223	2	27	theme	Rat	345:347	arg1	Bsep					349:352	Rat Bsep	345:352	Rat Bsep	345:352	Rat Bsep was fused with yellow fluorescent protein, and the following mutants, in which Asn residues of putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125)) were sequentially replaced with Gln, were constructed by site-directed mutagenesis: single N109Q, double N109Q + N116Q, triple N109Q + N116Q + N122Q, and quadruple N109Q + N116Q + N122Q + N125Q.
17082223	3	28	theme	glycosidase	733:743	arg1	analysis					754:761	glycosidase cleavage analysis	733:761	glycosidase cleavage analysis	733:761	Immunoblot and glycosidase cleavage analysis demonstrated that each site was glycosylated.
17082223	2	29	theme	fluorescent	376:386	arg1	protein					388:394	yellow fluorescent protein	369:394	yellow fluorescent protein	369:394	Rat Bsep was fused with yellow fluorescent protein, and the following mutants, in which Asn residues of putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125)) were sequentially replaced with Gln, were constructed by site-directed mutagenesis: single N109Q, double N109Q + N116Q, triple N109Q + N116Q + N122Q, and quadruple N109Q + N116Q + N122Q + N125Q.
17082223	0	30	theme	transport	50:58	arg1	activity					60:67	the transport activity	46:67	the transport activity of the bile salt export pump (ABCB11) in MDCK II cells	46:122	Two N-linked glycans are required to maintain the transport activity of the bile salt export pump (ABCB11) in MDCK II cells.
17082223	6	31	theme	double-mutant	1170:1182	arg1	proteins					1184:1191	Wild-type and single- and double-mutant proteins	1144:1191	Wild-type and single- and double-mutant proteins	1144:1191	Wild-type and single- and double-mutant proteins were distributed exclusively along the apical membranes, whereas triple- and quadruple-mutant proteins remained intracellular.
17082223	1	32	theme	acid	257:260	arg1	activity					272:279	bile acid transport activity	252:279	bile acid transport activity	252:279	The aim of this study was to determine the role of N-linked glycosylation in protein stability, intracellular trafficking, and bile acid transport activity of the bile salt export pump [Bsep (ATP-binding cassette B11)].
17082223	9	33	from	trafficking	1841:1851	arg1	membrane					1881:1888	the apical membrane	1870:1888	the apical membrane	1870:1888	In conclusion, at least two N-linked glycans are required for Bsep protein stability, intracellular trafficking, and function in the apical membrane.
17082223	9	34	theme	apical	1874:1879	arg1	membrane					1881:1888	the apical membrane	1870:1888	the apical membrane	1870:1888	In conclusion, at least two N-linked glycans are required for Bsep protein stability, intracellular trafficking, and function in the apical membrane.
17082223	4	35	theme	MDCK	897:900	arg1	cells					905:909	polarized MDCK II cells	887:909	polarized MDCK II cells	887:909	Removal of glycans decreased taurocholate transport activity as determined in polarized MDCK II cells.
17082223	2	36	dep	sites	472:476	arg1	Asn					513:515	Asn(125)	513:520	Asn(125)	513:520	Rat Bsep was fused with yellow fluorescent protein, and the following mutants, in which Asn residues of putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125)) were sequentially replaced with Gln, were constructed by site-directed mutagenesis: single N109Q, double N109Q + N116Q, triple N109Q + N116Q + N122Q, and quadruple N109Q + N116Q + N122Q + N125Q.
17082223	2	36	dep	sites	472:476	arg1	Asn					499:501	Asn(122)	499:506	Asn(122)	499:506	Rat Bsep was fused with yellow fluorescent protein, and the following mutants, in which Asn residues of putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125)) were sequentially replaced with Gln, were constructed by site-directed mutagenesis: single N109Q, double N109Q + N116Q, triple N109Q + N116Q + N122Q, and quadruple N109Q + N116Q + N122Q + N125Q.
17082223	2	36	dep	sites	472:476	arg1	Asn					489:491	Asn(116)	489:496	Asn(116)	489:496	Rat Bsep was fused with yellow fluorescent protein, and the following mutants, in which Asn residues of putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125)) were sequentially replaced with Gln, were constructed by site-directed mutagenesis: single N109Q, double N109Q + N116Q, triple N109Q + N116Q + N122Q, and quadruple N109Q + N116Q + N122Q + N125Q.
17082223	2	36	dep	sites	472:476	arg1	Asn					479:481	Asn(109)	479:486	Asn(109)	479:486	Rat Bsep was fused with yellow fluorescent protein, and the following mutants, in which Asn residues of putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125)) were sequentially replaced with Gln, were constructed by site-directed mutagenesis: single N109Q, double N109Q + N116Q, triple N109Q + N116Q + N122Q, and quadruple N109Q + N116Q + N122Q + N125Q.
17082223	2	36	dep	sites	472:476	arg1	sites					472:476	putative glycosylation sites	449:476	putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125))	449:521	Rat Bsep was fused with yellow fluorescent protein, and the following mutants, in which Asn residues of putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125)) were sequentially replaced with Gln, were constructed by site-directed mutagenesis: single N109Q, double N109Q + N116Q, triple N109Q + N116Q + N122Q, and quadruple N109Q + N116Q + N122Q + N125Q.
17082223	5	37	dep	single-mutant	1057:1069	arg1	double-mutant					1072:1084	double-mutant	1072:1084	double-mutant	1072:1084	This decrease resulted from rapid decay of the mutant Bsep protein; biochemical half-lives were 3.76, 3.65, 3.24, 1.35, and 0.52 h in wild-type, single-mutant, double-mutant, triple-mutant, and quadruple-mutant cells, respectively.
17082223	5	37	dep	single-mutant	1057:1069	arg1	triple-mutant					1087:1099	triple-mutant	1087:1099	triple-mutant	1087:1099	This decrease resulted from rapid decay of the mutant Bsep protein; biochemical half-lives were 3.76, 3.65, 3.24, 1.35, and 0.52 h in wild-type, single-mutant, double-mutant, triple-mutant, and quadruple-mutant cells, respectively.
17082223	4	38	theme	transport	851:859	arg1	activity					861:868	taurocholate transport activity	838:868	taurocholate transport activity	838:868	Removal of glycans decreased taurocholate transport activity as determined in polarized MDCK II cells.
17082223	8	39	theme	specific	1457:1464	arg1	critical					1514:1521	critical	1514:1521	critical	1514:1521	To determine whether a specific glycosylation site or the number of glycans was critical for protein stability, we studied the protein expression of combinations of N-glycan-deficient mutants and observed that Bsep with one glycan was considerably unstable compared with Bsep harboring two or more glycans.
17082223	8	39	theme	specific	1457:1464	arg1	glycans					1502:1508	glycans	1502:1508	glycans	1502:1508	To determine whether a specific glycosylation site or the number of glycans was critical for protein stability, we studied the protein expression of combinations of N-glycan-deficient mutants and observed that Bsep with one glycan was considerably unstable compared with Bsep harboring two or more glycans.
17082223	8	39	theme	specific	1457:1464	arg1	site					1480:1483	a specific glycosylation site	1455:1483	a specific glycosylation site	1455:1483	To determine whether a specific glycosylation site or the number of glycans was critical for protein stability, we studied the protein expression of combinations of N-glycan-deficient mutants and observed that Bsep with one glycan was considerably unstable compared with Bsep harboring two or more glycans.
17082223	1	40	theme	glycosylation	185:197	arg1	role					168:171	the role	164:171	the role of N-linked glycosylation in protein stability, intracellular trafficking, and bile acid transport activity of the bile salt export pump [Bsep (ATP-binding cassette B11)]	164:342	The aim of this study was to determine the role of N-linked glycosylation in protein stability, intracellular trafficking, and bile acid transport activity of the bile salt export pump [Bsep (ATP-binding cassette B11)].
17082223	8	41	with	Bsep	1644:1647	arg1	glycan					1658:1663	one glycan	1654:1663	one glycan	1654:1663	To determine whether a specific glycosylation site or the number of glycans was critical for protein stability, we studied the protein expression of combinations of N-glycan-deficient mutants and observed that Bsep with one glycan was considerably unstable compared with Bsep harboring two or more glycans.
17082223	1	42	theme	protein	202:208	arg1	stability					210:218	protein stability	202:218	protein stability	202:218	The aim of this study was to determine the role of N-linked glycosylation in protein stability, intracellular trafficking, and bile acid transport activity of the bile salt export pump [Bsep (ATP-binding cassette B11)].
17082223	0	43	link	N-linked	4:11	arg1	glycans					13:19	Two N-linked glycans	0:19	Two N-linked glycans	0:19	Two N-linked glycans are required to maintain the transport activity of the bile salt export pump (ABCB11) in MDCK II cells.
17082223	8	44	gly	glycosylation	1466:1478	arg2	critical					1514:1521	critical	1514:1521	critical	1514:1521	To determine whether a specific glycosylation site or the number of glycans was critical for protein stability, we studied the protein expression of combinations of N-glycan-deficient mutants and observed that Bsep with one glycan was considerably unstable compared with Bsep harboring two or more glycans.
17082223	8	44	gly	glycosylation	1466:1478	arg2	site					1480:1483	a specific glycosylation site	1455:1483	a specific glycosylation site	1455:1483	To determine whether a specific glycosylation site or the number of glycans was critical for protein stability, we studied the protein expression of combinations of N-glycan-deficient mutants and observed that Bsep with one glycan was considerably unstable compared with Bsep harboring two or more glycans.
17082223	8	44	gly	glycosylation	1466:1478	arg2	glycans					1502:1508	glycans	1502:1508	glycans	1502:1508	To determine whether a specific glycosylation site or the number of glycans was critical for protein stability, we studied the protein expression of combinations of N-glycan-deficient mutants and observed that Bsep with one glycan was considerably unstable compared with Bsep harboring two or more glycans.
17082223	8	44	gly	glycosylation	1466:1478	arg1	glycans					1502:1508	glycans	1502:1508	glycans	1502:1508	To determine whether a specific glycosylation site or the number of glycans was critical for protein stability, we studied the protein expression of combinations of N-glycan-deficient mutants and observed that Bsep with one glycan was considerably unstable compared with Bsep harboring two or more glycans.
17082223	1	45	link	N-linked	176:183	arg1	glycosylation					185:197	N-linked glycosylation	176:197	N-linked glycosylation	176:197	The aim of this study was to determine the role of N-linked glycosylation in protein stability, intracellular trafficking, and bile acid transport activity of the bile salt export pump [Bsep (ATP-binding cassette B11)].
17082223	2	46	theme	single	607:612	arg1	N109Q					614:618	single N109Q	607:618	the following mutants, in which Asn residues of putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125)) were sequentially replaced with Gln, were constructed by site-directed mutagenesis: single N109Q	401:618	Rat Bsep was fused with yellow fluorescent protein, and the following mutants, in which Asn residues of putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125)) were sequentially replaced with Gln, were constructed by site-directed mutagenesis: single N109Q, double N109Q + N116Q, triple N109Q + N116Q + N122Q, and quadruple N109Q + N116Q + N122Q + N125Q.
17082223	1	47	theme	study	141:145	arg1	aim					129:131	The aim	125:131	The aim of this study	125:145	The aim of this study was to determine the role of N-linked glycosylation in protein stability, intracellular trafficking, and bile acid transport activity of the bile salt export pump [Bsep (ATP-binding cassette B11)].
17082223	2	48	theme	putative	449:456	arg1	Asn					513:515	Asn(125)	513:520	Asn(125)	513:520	Rat Bsep was fused with yellow fluorescent protein, and the following mutants, in which Asn residues of putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125)) were sequentially replaced with Gln, were constructed by site-directed mutagenesis: single N109Q, double N109Q + N116Q, triple N109Q + N116Q + N122Q, and quadruple N109Q + N116Q + N122Q + N125Q.
17082223	2	48	theme	putative	449:456	arg1	Asn					499:501	Asn(122)	499:506	Asn(122)	499:506	Rat Bsep was fused with yellow fluorescent protein, and the following mutants, in which Asn residues of putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125)) were sequentially replaced with Gln, were constructed by site-directed mutagenesis: single N109Q, double N109Q + N116Q, triple N109Q + N116Q + N122Q, and quadruple N109Q + N116Q + N122Q + N125Q.
17082223	2	48	theme	putative	449:456	arg1	Asn					489:491	Asn(116)	489:496	Asn(116)	489:496	Rat Bsep was fused with yellow fluorescent protein, and the following mutants, in which Asn residues of putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125)) were sequentially replaced with Gln, were constructed by site-directed mutagenesis: single N109Q, double N109Q + N116Q, triple N109Q + N116Q + N122Q, and quadruple N109Q + N116Q + N122Q + N125Q.
17082223	2	48	theme	putative	449:456	arg1	Asn					479:481	Asn(109)	479:486	Asn(109)	479:486	Rat Bsep was fused with yellow fluorescent protein, and the following mutants, in which Asn residues of putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125)) were sequentially replaced with Gln, were constructed by site-directed mutagenesis: single N109Q, double N109Q + N116Q, triple N109Q + N116Q + N122Q, and quadruple N109Q + N116Q + N122Q + N125Q.
17082223	2	48	theme	putative	449:456	arg1	sites					472:476	putative glycosylation sites	449:476	putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125))	449:521	Rat Bsep was fused with yellow fluorescent protein, and the following mutants, in which Asn residues of putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125)) were sequentially replaced with Gln, were constructed by site-directed mutagenesis: single N109Q, double N109Q + N116Q, triple N109Q + N116Q + N122Q, and quadruple N109Q + N116Q + N122Q + N125Q.
17082223	1	49	theme	ATP-binding	317:327	arg1	B11					338:340	ATP-binding cassette B11	317:340	ATP-binding cassette B11	317:340	The aim of this study was to determine the role of N-linked glycosylation in protein stability, intracellular trafficking, and bile acid transport activity of the bile salt export pump [Bsep (ATP-binding cassette B11)].
17082223	1	49	theme	ATP-binding	317:327	arg1	pump					305:308	the bile salt export pump [Bsep	284:314	the bile salt export pump [Bsep (ATP-binding cassette B11)]	284:342	The aim of this study was to determine the role of N-linked glycosylation in protein stability, intracellular trafficking, and bile acid transport activity of the bile salt export pump [Bsep (ATP-binding cassette B11)].
17082223	0	50	from	activity	60:67	arg1	cells					118:122	MDCK II cells	110:122	MDCK II cells	110:122	Two N-linked glycans are required to maintain the transport activity of the bile salt export pump (ABCB11) in MDCK II cells.
17082223	1	51	theme	transport	262:270	arg1	activity					272:279	bile acid transport activity	252:279	bile acid transport activity	252:279	The aim of this study was to determine the role of N-linked glycosylation in protein stability, intracellular trafficking, and bile acid transport activity of the bile salt export pump [Bsep (ATP-binding cassette B11)].
17082223	0	52	theme	salt	81:84	arg1	ABCB11					99:104	ABCB11	99:104	ABCB11	99:104	Two N-linked glycans are required to maintain the transport activity of the bile salt export pump (ABCB11) in MDCK II cells.
17082223	0	52	theme	salt	81:84	arg1	pump					93:96	the bile salt export pump	72:96	the bile salt export pump (ABCB11)	72:105	Two N-linked glycans are required to maintain the transport activity of the bile salt export pump (ABCB11) in MDCK II cells.
17082223	0	53	theme	II	115:116	arg1	cells					118:122	MDCK II cells	110:122	MDCK II cells	110:122	Two N-linked glycans are required to maintain the transport activity of the bile salt export pump (ABCB11) in MDCK II cells.
17082223	5	54	theme	rapid	940:944	arg1	decay					946:950	rapid decay	940:950	rapid decay of the mutant Bsep protein	940:977	This decrease resulted from rapid decay of the mutant Bsep protein; biochemical half-lives were 3.76, 3.65, 3.24, 1.35, and 0.52 h in wild-type, single-mutant, double-mutant, triple-mutant, and quadruple-mutant cells, respectively.
17082223	2	55	theme	sites	472:476	arg1	residues					437:444	Asn residues	433:444	Asn residues of putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125))	433:521	Rat Bsep was fused with yellow fluorescent protein, and the following mutants, in which Asn residues of putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125)) were sequentially replaced with Gln, were constructed by site-directed mutagenesis: single N109Q, double N109Q + N116Q, triple N109Q + N116Q + N122Q, and quadruple N109Q + N116Q + N122Q + N125Q.
17082223	2	55	theme	sites	472:476	arg1	sites					472:476	putative glycosylation sites	449:476	putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125))	449:521	Rat Bsep was fused with yellow fluorescent protein, and the following mutants, in which Asn residues of putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125)) were sequentially replaced with Gln, were constructed by site-directed mutagenesis: single N109Q, double N109Q + N116Q, triple N109Q + N116Q + N122Q, and quadruple N109Q + N116Q + N122Q + N125Q.
17082223	2	56	theme	following	405:413	arg1	N116Q					636:640	N116Q	636:640	N116Q	636:640	Rat Bsep was fused with yellow fluorescent protein, and the following mutants, in which Asn residues of putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125)) were sequentially replaced with Gln, were constructed by site-directed mutagenesis: single N109Q, double N109Q + N116Q, triple N109Q + N116Q + N122Q, and quadruple N109Q + N116Q + N122Q + N125Q.
17082223	2	56	theme	following	405:413	arg1	mutants					415:421	the following mutants	401:421	the following mutants	401:421	Rat Bsep was fused with yellow fluorescent protein, and the following mutants, in which Asn residues of putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125)) were sequentially replaced with Gln, were constructed by site-directed mutagenesis: single N109Q, double N109Q + N116Q, triple N109Q + N116Q + N122Q, and quadruple N109Q + N116Q + N122Q + N125Q.
17082223	2	56	theme	following	405:413	arg1	N109Q					628:632	N109Q	628:632	N109Q	628:632	Rat Bsep was fused with yellow fluorescent protein, and the following mutants, in which Asn residues of putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125)) were sequentially replaced with Gln, were constructed by site-directed mutagenesis: single N109Q, double N109Q + N116Q, triple N109Q + N116Q + N122Q, and quadruple N109Q + N116Q + N122Q + N125Q.
17082223	7	57	from	role	1389:1392	arg1	degradation					1421:1431	Bsep degradation	1416:1431	Bsep degradation	1416:1431	MG-132 but not bafilomycin A(1) extended the half-life, suggesting a role for the proteasome in Bsep degradation.
17082223	9	58	from	function	1858:1865	arg1	membrane					1881:1888	the apical membrane	1870:1888	the apical membrane	1870:1888	In conclusion, at least two N-linked glycans are required for Bsep protein stability, intracellular trafficking, and function in the apical membrane.
17082223	1	59	theme	bile	288:291	arg1	B11					338:340	ATP-binding cassette B11	317:340	ATP-binding cassette B11	317:340	The aim of this study was to determine the role of N-linked glycosylation in protein stability, intracellular trafficking, and bile acid transport activity of the bile salt export pump [Bsep (ATP-binding cassette B11)].
17082223	1	59	theme	bile	288:291	arg1	pump					305:308	the bile salt export pump [Bsep	284:314	the bile salt export pump [Bsep (ATP-binding cassette B11)]	284:342	The aim of this study was to determine the role of N-linked glycosylation in protein stability, intracellular trafficking, and bile acid transport activity of the bile salt export pump [Bsep (ATP-binding cassette B11)].
17082223	8	60	theme	combinations	1583:1594	arg1	expression					1569:1578	the protein expression	1557:1578	the protein expression of combinations of N-glycan-deficient mutants	1557:1624	To determine whether a specific glycosylation site or the number of glycans was critical for protein stability, we studied the protein expression of combinations of N-glycan-deficient mutants and observed that Bsep with one glycan was considerably unstable compared with Bsep harboring two or more glycans.
17082223	9	61	theme	Bsep	1803:1806	arg1	stability					1816:1824	Bsep protein stability	1803:1824	Bsep protein stability	1803:1824	In conclusion, at least two N-linked glycans are required for Bsep protein stability, intracellular trafficking, and function in the apical membrane.
17082223	0	62	theme	pump	93:96	arg1	activity					60:67	the transport activity	46:67	the transport activity of the bile salt export pump (ABCB11) in MDCK II cells	46:122	Two N-linked glycans are required to maintain the transport activity of the bile salt export pump (ABCB11) in MDCK II cells.
17082223	1	63	theme	export	298:303	arg1	B11					338:340	ATP-binding cassette B11	317:340	ATP-binding cassette B11	317:340	The aim of this study was to determine the role of N-linked glycosylation in protein stability, intracellular trafficking, and bile acid transport activity of the bile salt export pump [Bsep (ATP-binding cassette B11)].
17082223	1	63	theme	export	298:303	arg1	pump					305:308	the bile salt export pump [Bsep	284:314	the bile salt export pump [Bsep (ATP-binding cassette B11)]	284:342	The aim of this study was to determine the role of N-linked glycosylation in protein stability, intracellular trafficking, and bile acid transport activity of the bile salt export pump [Bsep (ATP-binding cassette B11)].
17082223	8	64	theme	N-glycan-deficient	1599:1616	arg1	mutants					1618:1624	N-glycan-deficient mutants	1599:1624	N-glycan-deficient mutants	1599:1624	To determine whether a specific glycosylation site or the number of glycans was critical for protein stability, we studied the protein expression of combinations of N-glycan-deficient mutants and observed that Bsep with one glycan was considerably unstable compared with Bsep harboring two or more glycans.
17082223	0	65	theme	N-linked	4:11	arg1	glycans					13:19	Two N-linked glycans	0:19	Two N-linked glycans	0:19	Two N-linked glycans are required to maintain the transport activity of the bile salt export pump (ABCB11) in MDCK II cells.
17082223	7	66	theme	Bsep	1416:1419	arg1	degradation					1421:1431	Bsep degradation	1416:1431	Bsep degradation	1416:1431	MG-132 but not bafilomycin A(1) extended the half-life, suggesting a role for the proteasome in Bsep degradation.
17082223	1	67	gly	glycosylation	185:197	arg1	bile					252:255	bile acid transport activity	252:279	bile acid transport activity	252:279	The aim of this study was to determine the role of N-linked glycosylation in protein stability, intracellular trafficking, and bile acid transport activity of the bile salt export pump [Bsep (ATP-binding cassette B11)].
17082223	1	67	gly	glycosylation	185:197	arg1	B11					338:340	ATP-binding cassette B11	317:340	ATP-binding cassette B11	317:340	The aim of this study was to determine the role of N-linked glycosylation in protein stability, intracellular trafficking, and bile acid transport activity of the bile salt export pump [Bsep (ATP-binding cassette B11)].
17082223	1	67	gly	glycosylation	185:197	arg1	acid					257:260	bile acid transport activity	252:279	bile acid transport activity	252:279	The aim of this study was to determine the role of N-linked glycosylation in protein stability, intracellular trafficking, and bile acid transport activity of the bile salt export pump [Bsep (ATP-binding cassette B11)].
17082223	1	67	gly	glycosylation	185:197	arg1	transport					262:270	bile acid transport activity	252:279	bile acid transport activity	252:279	The aim of this study was to determine the role of N-linked glycosylation in protein stability, intracellular trafficking, and bile acid transport activity of the bile salt export pump [Bsep (ATP-binding cassette B11)].
17082223	1	67	gly	glycosylation	185:197	arg1	pump					305:308	the bile salt export pump [Bsep	284:314	the bile salt export pump [Bsep (ATP-binding cassette B11)]	284:342	The aim of this study was to determine the role of N-linked glycosylation in protein stability, intracellular trafficking, and bile acid transport activity of the bile salt export pump [Bsep (ATP-binding cassette B11)].
17082223	1	67	gly	glycosylation	185:197	arg1	protein					202:208	protein stability	202:218	protein stability	202:218	The aim of this study was to determine the role of N-linked glycosylation in protein stability, intracellular trafficking, and bile acid transport activity of the bile salt export pump [Bsep (ATP-binding cassette B11)].
17082223	9	68	theme	intracellular	1827:1839	arg1	trafficking					1841:1851	intracellular trafficking	1827:1851	intracellular trafficking	1827:1851	In conclusion, at least two N-linked glycans are required for Bsep protein stability, intracellular trafficking, and function in the apical membrane.
17082223	5	69	theme	protein	971:977	arg1	decay					946:950	rapid decay	940:950	rapid decay of the mutant Bsep protein	940:977	This decrease resulted from rapid decay of the mutant Bsep protein; biochemical half-lives were 3.76, 3.65, 3.24, 1.35, and 0.52 h in wild-type, single-mutant, double-mutant, triple-mutant, and quadruple-mutant cells, respectively.
17082223	4	70	theme	glycans	820:826	arg1	Removal					809:815	Removal	809:815	Removal of glycans	809:826	Removal of glycans decreased taurocholate transport activity as determined in polarized MDCK II cells.
17082223	5	71	theme	biochemical	980:990	arg1	half-lives					992:1001	biochemical half-lives	980:1001	biochemical half-lives	980:1001	This decrease resulted from rapid decay of the mutant Bsep protein; biochemical half-lives were 3.76, 3.65, 3.24, 1.35, and 0.52 h in wild-type, single-mutant, double-mutant, triple-mutant, and quadruple-mutant cells, respectively.
17082223	6	72	dep	distributed	1198:1208	arg1	whereas					1250:1256	whereas	1250:1256	whereas	1250:1256	Wild-type and single- and double-mutant proteins were distributed exclusively along the apical membranes, whereas triple- and quadruple-mutant proteins remained intracellular.
17082223	1	73	theme	bile	252:255	arg1	activity					272:279	bile acid transport activity	252:279	bile acid transport activity	252:279	The aim of this study was to determine the role of N-linked glycosylation in protein stability, intracellular trafficking, and bile acid transport activity of the bile salt export pump [Bsep (ATP-binding cassette B11)].
17082223	7	74	theme	bafilomycin	1335:1345	arg1	1					1349:1349	1	1349:1349	1	1349:1349	MG-132 but not bafilomycin A(1) extended the half-life, suggesting a role for the proteasome in Bsep degradation.
17082223	7	74	theme	bafilomycin	1335:1345	arg1	A					1347:1347	bafilomycin A	1335:1347	MG-132 but not bafilomycin A(1)	1320:1350	MG-132 but not bafilomycin A(1) extended the half-life, suggesting a role for the proteasome in Bsep degradation.
17082223	3	75	theme	cleavage	745:752	arg1	analysis					754:761	glycosidase cleavage analysis	733:761	glycosidase cleavage analysis	733:761	Immunoblot and glycosidase cleavage analysis demonstrated that each site was glycosylated.
17082223	2	76	theme	yellow	369:374	arg1	protein					388:394	yellow fluorescent protein	369:394	yellow fluorescent protein	369:394	Rat Bsep was fused with yellow fluorescent protein, and the following mutants, in which Asn residues of putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125)) were sequentially replaced with Gln, were constructed by site-directed mutagenesis: single N109Q, double N109Q + N116Q, triple N109Q + N116Q + N122Q, and quadruple N109Q + N116Q + N122Q + N125Q.
17082223	5	77	theme	mutant	959:964	arg1	protein					971:977	the mutant Bsep protein	955:977	the mutant Bsep protein	955:977	This decrease resulted from rapid decay of the mutant Bsep protein; biochemical half-lives were 3.76, 3.65, 3.24, 1.35, and 0.52 h in wild-type, single-mutant, double-mutant, triple-mutant, and quadruple-mutant cells, respectively.
17082223	2	78	dep	mutants	415:421	arg1	N109Q					614:618	single N109Q	607:618	the following mutants, in which Asn residues of putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125)) were sequentially replaced with Gln, were constructed by site-directed mutagenesis: single N109Q	401:618	Rat Bsep was fused with yellow fluorescent protein, and the following mutants, in which Asn residues of putative glycosylation sites (Asn(109), Asn(116), Asn(122), and Asn(125)) were sequentially replaced with Gln, were constructed by site-directed mutagenesis: single N109Q, double N109Q + N116Q, triple N109Q + N116Q + N122Q, and quadruple N109Q + N116Q + N122Q + N125Q.
17082223	9	79	from	stability	1816:1824	arg1	membrane					1881:1888	the apical membrane	1870:1888	the apical membrane	1870:1888	In conclusion, at least two N-linked glycans are required for Bsep protein stability, intracellular trafficking, and function in the apical membrane.
17082223	6	80	theme	quadruple-mutant	1270:1285	arg1	proteins					1287:1294	triple- and quadruple-mutant proteins	1258:1294	triple- and quadruple-mutant proteins	1258:1294	Wild-type and single- and double-mutant proteins were distributed exclusively along the apical membranes, whereas triple- and quadruple-mutant proteins remained intracellular.
17082223	8	81	theme	glycosylation	1466:1478	arg1	critical					1514:1521	critical	1514:1521	critical	1514:1521	To determine whether a specific glycosylation site or the number of glycans was critical for protein stability, we studied the protein expression of combinations of N-glycan-deficient mutants and observed that Bsep with one glycan was considerably unstable compared with Bsep harboring two or more glycans.
17082223	8	81	theme	glycosylation	1466:1478	arg1	glycans					1502:1508	glycans	1502:1508	glycans	1502:1508	To determine whether a specific glycosylation site or the number of glycans was critical for protein stability, we studied the protein expression of combinations of N-glycan-deficient mutants and observed that Bsep with one glycan was considerably unstable compared with Bsep harboring two or more glycans.
17082223	8	81	theme	glycosylation	1466:1478	arg1	site					1480:1483	a specific glycosylation site	1455:1483	a specific glycosylation site	1455:1483	To determine whether a specific glycosylation site or the number of glycans was critical for protein stability, we studied the protein expression of combinations of N-glycan-deficient mutants and observed that Bsep with one glycan was considerably unstable compared with Bsep harboring two or more glycans.
17082223	4	82	theme	polarized	887:895	arg1	cells					905:909	polarized MDCK II cells	887:909	polarized MDCK II cells	887:909	Removal of glycans decreased taurocholate transport activity as determined in polarized MDCK II cells.
17082223	6	83	theme	apical	1232:1237	arg1	membranes					1239:1247	the apical membranes	1228:1247	the apical membranes	1228:1247	Wild-type and single- and double-mutant proteins were distributed exclusively along the apical membranes, whereas triple- and quadruple-mutant proteins remained intracellular.
17082223	6	84	theme	triple-	1258:1264	arg1	proteins					1287:1294	triple- and quadruple-mutant proteins	1258:1294	triple- and quadruple-mutant proteins	1258:1294	Wild-type and single- and double-mutant proteins were distributed exclusively along the apical membranes, whereas triple- and quadruple-mutant proteins remained intracellular.
17082223	1	85	theme	N-linked	176:183	arg1	glycosylation					185:197	N-linked glycosylation	176:197	N-linked glycosylation	176:197	The aim of this study was to determine the role of N-linked glycosylation in protein stability, intracellular trafficking, and bile acid transport activity of the bile salt export pump [Bsep (ATP-binding cassette B11)].
7538124	9	0	theme	other	1631:1635	arg1	proteins					1659:1666	other intermediate filament proteins	1631:1666	other intermediate filament proteins	1631:1666	Our results show that K18 glycosylation sites share some features with other already identified O-GlcNAc sites and may together help predict glycosylation sites of other intermediate filament proteins.
7538124	9	1	gly	glycosylation	1608:1620	arg2	sites					1622:1626	glycosylation sites	1608:1626	glycosylation sites of other intermediate filament proteins	1608:1666	Our results show that K18 glycosylation sites share some features with other already identified O-GlcNAc sites and may together help predict glycosylation sites of other intermediate filament proteins.
7538124	9	1	gly	glycosylation	1608:1620	arg2	proteins					1659:1666	other intermediate filament proteins	1631:1666	other intermediate filament proteins	1631:1666	Our results show that K18 glycosylation sites share some features with other already identified O-GlcNAc sites and may together help predict glycosylation sites of other intermediate filament proteins.
7538124	9	1	gly	glycosylation	1608:1620	arg1	proteins					1659:1666	other intermediate filament proteins	1631:1666	other intermediate filament proteins	1631:1666	Our results show that K18 glycosylation sites share some features with other already identified O-GlcNAc sites and may together help predict glycosylation sites of other intermediate filament proteins.
7538124	1	2	gly	phosphoglycoproteins	151:170	arg1	phosphoglycoproteins					151:170	intermediate filament phosphoglycoproteins	129:170	intermediate filament phosphoglycoproteins that are expressed preferentially in glandular epithelia	129:227	Keratin polypeptides 8 and 18 (K8/18) are intermediate filament phosphoglycoproteins that are expressed preferentially in glandular epithelia.
7538124	1	2	gly	phosphoglycoproteins	151:170	arg1	polypeptides					95:106	Keratin polypeptides 8 and 18 (K8/18)	87:123	Keratin polypeptides 8 and 18 (K8/18)	87:123	Keratin polypeptides 8 and 18 (K8/18) are intermediate filament phosphoglycoproteins that are expressed preferentially in glandular epithelia.
7538124	9	3	theme	filament	1650:1657	arg1	proteins					1659:1666	other intermediate filament proteins	1631:1666	other intermediate filament proteins	1631:1666	Our results show that K18 glycosylation sites share some features with other already identified O-GlcNAc sites and may together help predict glycosylation sites of other intermediate filament proteins.
7538124	7	4	gly	glycosylation	1177:1189	arg1	construct					1200:1208	a K18 construct	1194:1208	a K18 construct that was mutated at the molecularly identified sites then transfected into NIH-3T3 cells	1194:1297	The precise modified residues in human cells were verified using Edman degradation and confirmed further by the lack of glycosylation of a K18 construct that was mutated at the molecularly identified sites then transfected into NIH-3T3 cells.
7538124	7	5	theme	precise	1061:1067	arg1	residues					1078:1085	The precise modified residues	1057:1085	The precise modified residues in human cells	1057:1100	The precise modified residues in human cells were verified using Edman degradation and confirmed further by the lack of glycosylation of a K18 construct that was mutated at the molecularly identified sites then transfected into NIH-3T3 cells.
7538124	5	6	from	K18	958:960	arg1	cells					979:983	human colonic cells	965:983	human colonic cells	965:983	We identified the major glycosylation sites of K18 by comparing the tryptic 3H-glycopeptide pattern of the panel of mutant and wild type K18 expressed in the insect cells with the glycopeptides of K18 in human colonic cells.
7538124	4	7	theme	Ser	642:644	arg1	panel					629:633	a panel	627:633	a panel of K18 Ser and Thr-->Ala mutants	627:666	For this, we generated a panel of K18 Ser and Thr-->Ala mutants at potential glycosylation sites followed by expression in a baculovirus-insect cell system.
7538124	5	8	with	cells	926:930	arg1	glycopeptides					941:953	the glycopeptides	937:953	the glycopeptides of K18 in human colonic cells	937:983	We identified the major glycosylation sites of K18 by comparing the tryptic 3H-glycopeptide pattern of the panel of mutant and wild type K18 expressed in the insect cells with the glycopeptides of K18 in human colonic cells.
7538124	9	9	theme	intermediate	1637:1648	arg1	proteins					1659:1666	other intermediate filament proteins	1631:1666	other intermediate filament proteins	1631:1666	Our results show that K18 glycosylation sites share some features with other already identified O-GlcNAc sites and may together help predict glycosylation sites of other intermediate filament proteins.
7538124	9	10	theme	identified	1552:1561	arg1	sites					1572:1576	other already identified O-GlcNAc sites	1538:1576	other already identified O-GlcNAc sites	1538:1576	Our results show that K18 glycosylation sites share some features with other already identified O-GlcNAc sites and may together help predict glycosylation sites of other intermediate filament proteins.
7538124	4	11	gly	glycosylation	681:693	arg2	sites					695:699	potential glycosylation sites	671:699	potential glycosylation sites followed by expression in a baculovirus-insect cell system	671:758	For this, we generated a panel of K18 Ser and Thr-->Ala mutants at potential glycosylation sites followed by expression in a baculovirus-insect cell system.
7538124	5	12	from	cells	979:983	arg1	glycopeptides					941:953	the glycopeptides	937:953	the glycopeptides of K18 in human colonic cells	937:983	We identified the major glycosylation sites of K18 by comparing the tryptic 3H-glycopeptide pattern of the panel of mutant and wild type K18 expressed in the insect cells with the glycopeptides of K18 in human colonic cells.
7538124	3	13	theme	filament	585:592	arg1	assembly					594:601	keratin filament assembly	577:601	keratin filament assembly	577:601	Since the function of these modifications is unknown, we sought as a first step to identify the precise modification sites and asked if they play a role in keratin filament assembly.
7538124	5	14	theme	tryptic	829:835	arg1	pattern					853:859	the tryptic 3H-glycopeptide pattern	825:859	the tryptic 3H-glycopeptide pattern of the panel of mutant and wild type K18 expressed in the insect cells with the glycopeptides of K18 in human colonic cells	825:983	We identified the major glycosylation sites of K18 by comparing the tryptic 3H-glycopeptide pattern of the panel of mutant and wild type K18 expressed in the insect cells with the glycopeptides of K18 in human colonic cells.
7538124	4	15	theme	glycosylation	681:693	arg1	sites					695:699	potential glycosylation sites	671:699	potential glycosylation sites followed by expression in a baculovirus-insect cell system	671:758	For this, we generated a panel of K18 Ser and Thr-->Ala mutants at potential glycosylation sites followed by expression in a baculovirus-insect cell system.
7538124	9	16	with	features	1524:1531	arg1	sites					1572:1576	other already identified O-GlcNAc sites	1538:1576	other already identified O-GlcNAc sites	1538:1576	Our results show that K18 glycosylation sites share some features with other already identified O-GlcNAc sites and may together help predict glycosylation sites of other intermediate filament proteins.
7538124	5	17	theme	type	893:896	arg1	K18					898:900	mutant and wild type K18	877:900	K18	898:900	We identified the major glycosylation sites of K18 by comparing the tryptic 3H-glycopeptide pattern of the panel of mutant and wild type K18 expressed in the insect cells with the glycopeptides of K18 in human colonic cells.
7538124	8	18	theme	wild	1450:1453	arg1	K8/18					1460:1464	wild type K8/18	1450:1464	wild type K8/18	1450:1464	Partial or total K18 glycosylation mutants transfected into mammalian cells manifested nondistinguishable filament assembly to cells transfected with wild type K8/18.
7538124	7	19	theme	human	1090:1094	arg1	cells					1096:1100	human cells	1090:1100	human cells	1090:1100	The precise modified residues in human cells were verified using Edman degradation and confirmed further by the lack of glycosylation of a K18 construct that was mutated at the molecularly identified sites then transfected into NIH-3T3 cells.
7538124	5	20	theme	insect	919:924	arg1	cells					926:930	the insect cells	915:930	the insect cells with the glycopeptides of K18 in human colonic cells	915:983	We identified the major glycosylation sites of K18 by comparing the tryptic 3H-glycopeptide pattern of the panel of mutant and wild type K18 expressed in the insect cells with the glycopeptides of K18 in human colonic cells.
7538124	4	21	theme	Thr-->Ala	650:658	arg1	mutants					660:666	Thr-->Ala mutants	650:666	Thr-->Ala mutants	650:666	For this, we generated a panel of K18 Ser and Thr-->Ala mutants at potential glycosylation sites followed by expression in a baculovirus-insect cell system.
7538124	7	22	theme	glycosylation	1177:1189	arg1	lack					1169:1172	the lack	1165:1172	the lack of glycosylation of a K18 construct that was mutated at the molecularly identified sites then transfected into NIH-3T3 cells	1165:1297	The precise modified residues in human cells were verified using Edman degradation and confirmed further by the lack of glycosylation of a K18 construct that was mutated at the molecularly identified sites then transfected into NIH-3T3 cells.
7538124	5	23	theme	K18	808:810	arg1	sites					799:803	the major glycosylation sites	775:803	the major glycosylation sites of K18	775:810	We identified the major glycosylation sites of K18 by comparing the tryptic 3H-glycopeptide pattern of the panel of mutant and wild type K18 expressed in the insect cells with the glycopeptides of K18 in human colonic cells.
7538124	5	23	theme	K18	808:810	arg1	K18					808:810	K18	808:810	K18	808:810	We identified the major glycosylation sites of K18 by comparing the tryptic 3H-glycopeptide pattern of the panel of mutant and wild type K18 expressed in the insect cells with the glycopeptides of K18 in human colonic cells.
7538124	9	24	theme	glycosylation	1493:1505	arg1	sites					1507:1511	K18 glycosylation sites	1489:1511	K18 glycosylation sites	1489:1511	Our results show that K18 glycosylation sites share some features with other already identified O-GlcNAc sites and may together help predict glycosylation sites of other intermediate filament proteins.
7538124	0	25	theme	keratin	75:81	arg1	keratin					75:81	human keratin 18	69:84	human keratin 18	69:84	Identification and mutational analysis of the glycosylation sites of human keratin 18.
7538124	0	25	theme	keratin	75:81	arg1	sites					60:64	the glycosylation sites	42:64	the glycosylation sites of human keratin 18	42:84	Identification and mutational analysis of the glycosylation sites of human keratin 18.
7538124	1	26	theme	filament	142:149	arg1	phosphoglycoproteins					151:170	intermediate filament phosphoglycoproteins	129:170	intermediate filament phosphoglycoproteins that are expressed preferentially in glandular epithelia	129:227	Keratin polypeptides 8 and 18 (K8/18) are intermediate filament phosphoglycoproteins that are expressed preferentially in glandular epithelia.
7538124	1	26	theme	filament	142:149	arg1	polypeptides					95:106	Keratin polypeptides 8 and 18 (K8/18)	87:123	Keratin polypeptides 8 and 18 (K8/18)	87:123	Keratin polypeptides 8 and 18 (K8/18) are intermediate filament phosphoglycoproteins that are expressed preferentially in glandular epithelia.
7538124	4	27	theme	cell	748:751	arg1	system					753:758	a baculovirus-insect cell system	727:758	a baculovirus-insect cell system	727:758	For this, we generated a panel of K18 Ser and Thr-->Ala mutants at potential glycosylation sites followed by expression in a baculovirus-insect cell system.
7538124	3	28	theme	modifications	449:461	arg1	unknown					466:472	unknown	466:472	unknown	466:472	Since the function of these modifications is unknown, we sought as a first step to identify the precise modification sites and asked if they play a role in keratin filament assembly.
7538124	3	28	theme	modifications	449:461	arg1	function					431:438	the function	427:438	the function of these modifications	427:461	Since the function of these modifications is unknown, we sought as a first step to identify the precise modification sites and asked if they play a role in keratin filament assembly.
7538124	9	29	theme	other	1538:1542	arg1	sites					1572:1576	other already identified O-GlcNAc sites	1538:1576	other already identified O-GlcNAc sites	1538:1576	Our results show that K18 glycosylation sites share some features with other already identified O-GlcNAc sites and may together help predict glycosylation sites of other intermediate filament proteins.
7538124	7	30	theme	NIH-3T3	1285:1291	arg1	cells					1293:1297	NIH-3T3 cells	1285:1297	NIH-3T3 cells	1285:1297	The precise modified residues in human cells were verified using Edman degradation and confirmed further by the lack of glycosylation of a K18 construct that was mutated at the molecularly identified sites then transfected into NIH-3T3 cells.
7538124	3	31	theme	precise	517:523	arg1	sites					538:542	the precise modification sites	513:542	the precise modification sites	513:542	Since the function of these modifications is unknown, we sought as a first step to identify the precise modification sites and asked if they play a role in keratin filament assembly.
7538124	8	32	theme	K18	1317:1319	arg1	mutants					1335:1341	Partial or total K18 glycosylation mutants	1300:1341	Partial or total K18 glycosylation mutants transfected into mammalian cells manifested	1300:1385	Partial or total K18 glycosylation mutants transfected into mammalian cells manifested nondistinguishable filament assembly to cells transfected with wild type K8/18.
7538124	4	33	from	expression	713:722	arg1	system					753:758	a baculovirus-insect cell system	727:758	a baculovirus-insect cell system	727:758	For this, we generated a panel of K18 Ser and Thr-->Ala mutants at potential glycosylation sites followed by expression in a baculovirus-insect cell system.
7538124	1	34	theme	Keratin	87:93	arg1	phosphoglycoproteins					151:170	intermediate filament phosphoglycoproteins	129:170	intermediate filament phosphoglycoproteins that are expressed preferentially in glandular epithelia	129:227	Keratin polypeptides 8 and 18 (K8/18) are intermediate filament phosphoglycoproteins that are expressed preferentially in glandular epithelia.
7538124	1	34	theme	Keratin	87:93	arg1	polypeptides					95:106	Keratin polypeptides 8 and 18 (K8/18)	87:123	Keratin polypeptides 8 and 18 (K8/18)	87:123	Keratin polypeptides 8 and 18 (K8/18) are intermediate filament phosphoglycoproteins that are expressed preferentially in glandular epithelia.
7538124	0	35	theme	mutational	19:28	arg1	analysis					30:37	mutational analysis	19:37	mutational analysis	19:37	Identification and mutational analysis of the glycosylation sites of human keratin 18.
7538124	3	36	theme	modification	525:536	arg1	sites					538:542	the precise modification sites	513:542	the precise modification sites	513:542	Since the function of these modifications is unknown, we sought as a first step to identify the precise modification sites and asked if they play a role in keratin filament assembly.
7538124	9	37	theme	K18	1489:1491	arg1	sites					1507:1511	K18 glycosylation sites	1489:1511	K18 glycosylation sites	1489:1511	Our results show that K18 glycosylation sites share some features with other already identified O-GlcNAc sites and may together help predict glycosylation sites of other intermediate filament proteins.
7538124	3	38	theme	first	490:494	arg1	step					496:499	a first step	488:499	a first step to identify the precise modification sites	488:542	Since the function of these modifications is unknown, we sought as a first step to identify the precise modification sites and asked if they play a role in keratin filament assembly.
7538124	5	39	theme	major	779:783	arg1	sites					799:803	the major glycosylation sites	775:803	the major glycosylation sites of K18	775:810	We identified the major glycosylation sites of K18 by comparing the tryptic 3H-glycopeptide pattern of the panel of mutant and wild type K18 expressed in the insect cells with the glycopeptides of K18 in human colonic cells.
7538124	5	39	theme	major	779:783	arg1	K18					808:810	K18	808:810	K18	808:810	We identified the major glycosylation sites of K18 by comparing the tryptic 3H-glycopeptide pattern of the panel of mutant and wild type K18 expressed in the insect cells with the glycopeptides of K18 in human colonic cells.
7538124	7	40	from	residues	1078:1085	arg1	cells					1096:1100	human cells	1090:1100	human cells	1090:1100	The precise modified residues in human cells were verified using Edman degradation and confirmed further by the lack of glycosylation of a K18 construct that was mutated at the molecularly identified sites then transfected into NIH-3T3 cells.
7538124	2	41	theme	O-linked	345:352	arg1	O-GlcNAc					383:390	O-GlcNAc	383:390	O-GlcNAc	383:390	We previously showed that K8/18 phosphorylation occurs on serine residues and that K8/18 glycosylation consists of O-linked single N-acetylglucosamines (O-GlcNAc) that are linked to Ser/Thr.
7538124	2	41	theme	O-linked	345:352	arg1	N-acetylglucosamines					361:380	O-linked single N-acetylglucosamines	345:380	O-linked single N-acetylglucosamines (O-GlcNAc) that are linked to Ser/Thr	345:418	We previously showed that K8/18 phosphorylation occurs on serine residues and that K8/18 glycosylation consists of O-linked single N-acetylglucosamines (O-GlcNAc) that are linked to Ser/Thr.
7538124	9	42	theme	glycosylation	1608:1620	arg1	proteins					1659:1666	other intermediate filament proteins	1631:1666	other intermediate filament proteins	1631:1666	Our results show that K18 glycosylation sites share some features with other already identified O-GlcNAc sites and may together help predict glycosylation sites of other intermediate filament proteins.
7538124	9	42	theme	glycosylation	1608:1620	arg1	sites					1622:1626	glycosylation sites	1608:1626	glycosylation sites of other intermediate filament proteins	1608:1666	Our results show that K18 glycosylation sites share some features with other already identified O-GlcNAc sites and may together help predict glycosylation sites of other intermediate filament proteins.
7538124	5	43	theme	colonic	971:977	arg1	cells					979:983	human colonic cells	965:983	human colonic cells	965:983	We identified the major glycosylation sites of K18 by comparing the tryptic 3H-glycopeptide pattern of the panel of mutant and wild type K18 expressed in the insect cells with the glycopeptides of K18 in human colonic cells.
7538124	7	44	theme	construct	1200:1208	arg1	glycosylation					1177:1189	glycosylation	1177:1189	glycosylation of a K18 construct that was mutated at the molecularly identified sites then transfected into NIH-3T3 cells	1177:1297	The precise modified residues in human cells were verified using Edman degradation and confirmed further by the lack of glycosylation of a K18 construct that was mutated at the molecularly identified sites then transfected into NIH-3T3 cells.
7538124	7	45	theme	modified	1069:1076	arg1	residues					1078:1085	The precise modified residues	1057:1085	The precise modified residues in human cells	1057:1100	The precise modified residues in human cells were verified using Edman degradation and confirmed further by the lack of glycosylation of a K18 construct that was mutated at the molecularly identified sites then transfected into NIH-3T3 cells.
7538124	5	46	gly	3H-glycopeptide	837:851	arg2	3H-glycopeptide					837:851	the tryptic 3H-glycopeptide pattern	825:859	the tryptic 3H-glycopeptide pattern of the panel of mutant and wild type K18 expressed in the insect cells with the glycopeptides of K18 in human colonic cells	825:983	We identified the major glycosylation sites of K18 by comparing the tryptic 3H-glycopeptide pattern of the panel of mutant and wild type K18 expressed in the insect cells with the glycopeptides of K18 in human colonic cells.
7538124	6	47	from	serines	1022:1028	arg1	K18					1052:1054	K18	1052:1054	K18	1052:1054	The identified sites occur on three serines in the head domain of K18.
7538124	6	47	from	serines	1022:1028	arg1	domain					1042:1047	the head domain	1033:1047	the head domain of K18	1033:1054	The identified sites occur on three serines in the head domain of K18.
7538124	9	48	theme	proteins	1659:1666	arg1	proteins					1659:1666	other intermediate filament proteins	1631:1666	other intermediate filament proteins	1631:1666	Our results show that K18 glycosylation sites share some features with other already identified O-GlcNAc sites and may together help predict glycosylation sites of other intermediate filament proteins.
7538124	9	48	theme	proteins	1659:1666	arg1	sites					1622:1626	glycosylation sites	1608:1626	glycosylation sites of other intermediate filament proteins	1608:1666	Our results show that K18 glycosylation sites share some features with other already identified O-GlcNAc sites and may together help predict glycosylation sites of other intermediate filament proteins.
7538124	5	49	theme	mutant	877:882	arg1	K18					898:900	mutant and wild type K18	877:900	K18	898:900	We identified the major glycosylation sites of K18 by comparing the tryptic 3H-glycopeptide pattern of the panel of mutant and wild type K18 expressed in the insect cells with the glycopeptides of K18 in human colonic cells.
7538124	2	50	theme	serine	288:293	arg1	residues					295:302	serine residues	288:302	serine residues	288:302	We previously showed that K8/18 phosphorylation occurs on serine residues and that K8/18 glycosylation consists of O-linked single N-acetylglucosamines (O-GlcNAc) that are linked to Ser/Thr.
7538124	5	51	theme	3H-glycopeptide	837:851	arg1	pattern					853:859	the tryptic 3H-glycopeptide pattern	825:859	the tryptic 3H-glycopeptide pattern of the panel of mutant and wild type K18 expressed in the insect cells with the glycopeptides of K18 in human colonic cells	825:983	We identified the major glycosylation sites of K18 by comparing the tryptic 3H-glycopeptide pattern of the panel of mutant and wild type K18 expressed in the insect cells with the glycopeptides of K18 in human colonic cells.
7538124	0	52	theme	glycosylation	46:58	arg1	keratin					75:81	human keratin 18	69:84	human keratin 18	69:84	Identification and mutational analysis of the glycosylation sites of human keratin 18.
7538124	0	52	theme	glycosylation	46:58	arg1	sites					60:64	the glycosylation sites	42:64	the glycosylation sites of human keratin 18	42:84	Identification and mutational analysis of the glycosylation sites of human keratin 18.
7538124	4	53	theme	K18	638:640	arg1	Ser					642:644	K18 Ser	638:644	K18 Ser	638:644	For this, we generated a panel of K18 Ser and Thr-->Ala mutants at potential glycosylation sites followed by expression in a baculovirus-insect cell system.
7538124	2	54	theme	K8/18	313:317	arg1	glycosylation					319:331	K8/18 glycosylation	313:331	K8/18 glycosylation	313:331	We previously showed that K8/18 phosphorylation occurs on serine residues and that K8/18 glycosylation consists of O-linked single N-acetylglucosamines (O-GlcNAc) that are linked to Ser/Thr.
7538124	1	55	dep	polypeptides	95:106	arg1	K8/18					118:122	K8/18	118:122	K8/18	118:122	Keratin polypeptides 8 and 18 (K8/18) are intermediate filament phosphoglycoproteins that are expressed preferentially in glandular epithelia.
7538124	1	55	dep	polypeptides	95:106	arg1	18					114:115	18	114:115	18	114:115	Keratin polypeptides 8 and 18 (K8/18) are intermediate filament phosphoglycoproteins that are expressed preferentially in glandular epithelia.
7538124	1	55	dep	polypeptides	95:106	arg1	8					108:108	8	108:108	8	108:108	Keratin polypeptides 8 and 18 (K8/18) are intermediate filament phosphoglycoproteins that are expressed preferentially in glandular epithelia.
7538124	3	56	theme	keratin	577:583	arg1	assembly					594:601	keratin filament assembly	577:601	keratin filament assembly	577:601	Since the function of these modifications is unknown, we sought as a first step to identify the precise modification sites and asked if they play a role in keratin filament assembly.
7538124	1	57	theme	glandular	209:217	arg1	epithelia					219:227	glandular epithelia	209:227	glandular epithelia	209:227	Keratin polypeptides 8 and 18 (K8/18) are intermediate filament phosphoglycoproteins that are expressed preferentially in glandular epithelia.
7538124	5	58	theme	wild	888:891	arg1	K18					898:900	mutant and wild type K18	877:900	K18	898:900	We identified the major glycosylation sites of K18 by comparing the tryptic 3H-glycopeptide pattern of the panel of mutant and wild type K18 expressed in the insect cells with the glycopeptides of K18 in human colonic cells.
7538124	8	59	theme	type	1455:1458	arg1	K8/18					1460:1464	wild type K8/18	1450:1464	wild type K8/18	1450:1464	Partial or total K18 glycosylation mutants transfected into mammalian cells manifested nondistinguishable filament assembly to cells transfected with wild type K8/18.
7538124	4	60	theme	potential	671:679	arg1	sites					695:699	potential glycosylation sites	671:699	potential glycosylation sites followed by expression in a baculovirus-insect cell system	671:758	For this, we generated a panel of K18 Ser and Thr-->Ala mutants at potential glycosylation sites followed by expression in a baculovirus-insect cell system.
7538124	5	61	theme	K18	898:900	arg1	panel					868:872	the panel	864:872	the panel of mutant and wild type K18 expressed in the insect cells with the glycopeptides of K18 in human colonic cells	864:983	We identified the major glycosylation sites of K18 by comparing the tryptic 3H-glycopeptide pattern of the panel of mutant and wild type K18 expressed in the insect cells with the glycopeptides of K18 in human colonic cells.
7538124	6	62	theme	identified	990:999	arg1	sites					1001:1005	The identified sites	986:1005	The identified sites	986:1005	The identified sites occur on three serines in the head domain of K18.
7538124	0	63	theme	human	69:73	arg1	keratin					75:81	human keratin 18	69:84	human keratin 18	69:84	Identification and mutational analysis of the glycosylation sites of human keratin 18.
7538124	2	64	theme	K8/18	256:260	arg1	phosphorylation					262:276	K8/18 phosphorylation	256:276	K8/18 phosphorylation	256:276	We previously showed that K8/18 phosphorylation occurs on serine residues and that K8/18 glycosylation consists of O-linked single N-acetylglucosamines (O-GlcNAc) that are linked to Ser/Thr.
7538124	5	65	theme	panel	868:872	arg1	pattern					853:859	the tryptic 3H-glycopeptide pattern	825:859	the tryptic 3H-glycopeptide pattern of the panel of mutant and wild type K18 expressed in the insect cells with the glycopeptides of K18 in human colonic cells	825:983	We identified the major glycosylation sites of K18 by comparing the tryptic 3H-glycopeptide pattern of the panel of mutant and wild type K18 expressed in the insect cells with the glycopeptides of K18 in human colonic cells.
7538124	1	66	theme	intermediate	129:140	arg1	phosphoglycoproteins					151:170	intermediate filament phosphoglycoproteins	129:170	intermediate filament phosphoglycoproteins that are expressed preferentially in glandular epithelia	129:227	Keratin polypeptides 8 and 18 (K8/18) are intermediate filament phosphoglycoproteins that are expressed preferentially in glandular epithelia.
7538124	1	66	theme	intermediate	129:140	arg1	polypeptides					95:106	Keratin polypeptides 8 and 18 (K8/18)	87:123	Keratin polypeptides 8 and 18 (K8/18)	87:123	Keratin polypeptides 8 and 18 (K8/18) are intermediate filament phosphoglycoproteins that are expressed preferentially in glandular epithelia.
7538124	5	67	gly	glycopeptides	941:953	arg1	K18					958:960	K18	958:960	K18 in human colonic cells	958:983	We identified the major glycosylation sites of K18 by comparing the tryptic 3H-glycopeptide pattern of the panel of mutant and wild type K18 expressed in the insect cells with the glycopeptides of K18 in human colonic cells.
7538124	5	67	gly	glycopeptides	941:953	arg2	glycopeptides					941:953	the glycopeptides	937:953	the glycopeptides of K18 in human colonic cells	937:983	We identified the major glycosylation sites of K18 by comparing the tryptic 3H-glycopeptide pattern of the panel of mutant and wild type K18 expressed in the insect cells with the glycopeptides of K18 in human colonic cells.
7538124	4	68	theme	mutants	660:666	arg1	panel					629:633	a panel	627:633	a panel of K18 Ser and Thr-->Ala mutants	627:666	For this, we generated a panel of K18 Ser and Thr-->Ala mutants at potential glycosylation sites followed by expression in a baculovirus-insect cell system.
7538124	9	69	gly	glycosylation	1493:1505	arg2	sites					1507:1511	K18 glycosylation sites	1489:1511	K18 glycosylation sites	1489:1511	Our results show that K18 glycosylation sites share some features with other already identified O-GlcNAc sites and may together help predict glycosylation sites of other intermediate filament proteins.
7538124	4	70	theme	baculovirus-insect	729:746	arg1	system					753:758	a baculovirus-insect cell system	727:758	a baculovirus-insect cell system	727:758	For this, we generated a panel of K18 Ser and Thr-->Ala mutants at potential glycosylation sites followed by expression in a baculovirus-insect cell system.
7538124	6	71	theme	head	1037:1040	arg1	K18					1052:1054	K18	1052:1054	K18	1052:1054	The identified sites occur on three serines in the head domain of K18.
7538124	6	71	theme	head	1037:1040	arg1	domain					1042:1047	the head domain	1033:1047	the head domain of K18	1033:1054	The identified sites occur on three serines in the head domain of K18.
7538124	8	72	theme	Partial	1300:1306	arg1	mutants					1335:1341	Partial or total K18 glycosylation mutants	1300:1341	Partial or total K18 glycosylation mutants transfected into mammalian cells manifested	1300:1385	Partial or total K18 glycosylation mutants transfected into mammalian cells manifested nondistinguishable filament assembly to cells transfected with wild type K8/18.
7538124	5	73	theme	glycosylation	785:797	arg1	sites					799:803	the major glycosylation sites	775:803	the major glycosylation sites of K18	775:810	We identified the major glycosylation sites of K18 by comparing the tryptic 3H-glycopeptide pattern of the panel of mutant and wild type K18 expressed in the insect cells with the glycopeptides of K18 in human colonic cells.
7538124	5	73	theme	glycosylation	785:797	arg1	K18					808:810	K18	808:810	K18	808:810	We identified the major glycosylation sites of K18 by comparing the tryptic 3H-glycopeptide pattern of the panel of mutant and wild type K18 expressed in the insect cells with the glycopeptides of K18 in human colonic cells.
7538124	8	74	theme	total	1311:1315	arg1	mutants					1335:1341	Partial or total K18 glycosylation mutants	1300:1341	Partial or total K18 glycosylation mutants transfected into mammalian cells manifested	1300:1385	Partial or total K18 glycosylation mutants transfected into mammalian cells manifested nondistinguishable filament assembly to cells transfected with wild type K8/18.
7538124	0	75	gly	glycosylation	46:58	arg2	sites					60:64	the glycosylation sites	42:64	the glycosylation sites of human keratin 18	42:84	Identification and mutational analysis of the glycosylation sites of human keratin 18.
7538124	0	75	gly	glycosylation	46:58	arg1	keratin					75:81	human keratin 18	69:84	human keratin 18	69:84	Identification and mutational analysis of the glycosylation sites of human keratin 18.
7538124	0	75	gly	glycosylation	46:58	arg2	keratin					75:81	human keratin 18	69:84	human keratin 18	69:84	Identification and mutational analysis of the glycosylation sites of human keratin 18.
7538124	9	76	theme	O-GlcNAc	1563:1570	arg1	sites					1572:1576	other already identified O-GlcNAc sites	1538:1576	other already identified O-GlcNAc sites	1538:1576	Our results show that K18 glycosylation sites share some features with other already identified O-GlcNAc sites and may together help predict glycosylation sites of other intermediate filament proteins.
7538124	7	77	theme	identified	1246:1255	arg1	sites					1257:1261	the molecularly identified sites	1230:1261	the molecularly identified sites then transfected into NIH-3T3 cells	1230:1297	The precise modified residues in human cells were verified using Edman degradation and confirmed further by the lack of glycosylation of a K18 construct that was mutated at the molecularly identified sites then transfected into NIH-3T3 cells.
7538124	8	78	theme	glycosylation	1321:1333	arg1	mutants					1335:1341	Partial or total K18 glycosylation mutants	1300:1341	Partial or total K18 glycosylation mutants transfected into mammalian cells manifested	1300:1385	Partial or total K18 glycosylation mutants transfected into mammalian cells manifested nondistinguishable filament assembly to cells transfected with wild type K8/18.
7538124	5	79	gly	glycosylation	785:797	arg2	K18					808:810	K18	808:810	K18	808:810	We identified the major glycosylation sites of K18 by comparing the tryptic 3H-glycopeptide pattern of the panel of mutant and wild type K18 expressed in the insect cells with the glycopeptides of K18 in human colonic cells.
7538124	5	79	gly	glycosylation	785:797	arg2	sites					799:803	the major glycosylation sites	775:803	the major glycosylation sites of K18	775:810	We identified the major glycosylation sites of K18 by comparing the tryptic 3H-glycopeptide pattern of the panel of mutant and wild type K18 expressed in the insect cells with the glycopeptides of K18 in human colonic cells.
7538124	5	79	gly	glycosylation	785:797	arg1	K18					808:810	K18	808:810	K18	808:810	We identified the major glycosylation sites of K18 by comparing the tryptic 3H-glycopeptide pattern of the panel of mutant and wild type K18 expressed in the insect cells with the glycopeptides of K18 in human colonic cells.
7538124	0	80	theme	sites	60:64	arg1	Identification					0:13	Identification	0:13	Identification	0:13	Identification and mutational analysis of the glycosylation sites of human keratin 18.
7538124	0	80	theme	sites	60:64	arg1	analysis					30:37	mutational analysis	19:37	mutational analysis	19:37	Identification and mutational analysis of the glycosylation sites of human keratin 18.
7538124	8	81	theme	mammalian	1360:1368	arg1	cells					1370:1374	mammalian cells	1360:1374	mammalian cells manifested	1360:1385	Partial or total K18 glycosylation mutants transfected into mammalian cells manifested nondistinguishable filament assembly to cells transfected with wild type K8/18.
7538124	2	82	theme	single	354:359	arg1	O-GlcNAc					383:390	O-GlcNAc	383:390	O-GlcNAc	383:390	We previously showed that K8/18 phosphorylation occurs on serine residues and that K8/18 glycosylation consists of O-linked single N-acetylglucosamines (O-GlcNAc) that are linked to Ser/Thr.
7538124	2	82	theme	single	354:359	arg1	N-acetylglucosamines					361:380	O-linked single N-acetylglucosamines	345:380	O-linked single N-acetylglucosamines (O-GlcNAc) that are linked to Ser/Thr	345:418	We previously showed that K8/18 phosphorylation occurs on serine residues and that K8/18 glycosylation consists of O-linked single N-acetylglucosamines (O-GlcNAc) that are linked to Ser/Thr.
7538124	5	83	theme	K18	958:960	arg1	glycopeptides					941:953	the glycopeptides	937:953	the glycopeptides of K18 in human colonic cells	937:983	We identified the major glycosylation sites of K18 by comparing the tryptic 3H-glycopeptide pattern of the panel of mutant and wild type K18 expressed in the insect cells with the glycopeptides of K18 in human colonic cells.
7538124	6	84	theme	K18	1052:1054	arg1	K18					1052:1054	K18	1052:1054	K18	1052:1054	The identified sites occur on three serines in the head domain of K18.
7538124	6	84	theme	K18	1052:1054	arg1	domain					1042:1047	the head domain	1033:1047	the head domain of K18	1033:1054	The identified sites occur on three serines in the head domain of K18.
7538124	2	85	attach	linked	402:407	arg2	O-GlcNAc					383:390	O-GlcNAc	383:390	O-GlcNAc	383:390	We previously showed that K8/18 phosphorylation occurs on serine residues and that K8/18 glycosylation consists of O-linked single N-acetylglucosamines (O-GlcNAc) that are linked to Ser/Thr.
7538124	2	85	attach	linked	402:407	arg1	Ser/Thr					412:418	Ser/Thr	412:418	Ser/Thr	412:418	We previously showed that K8/18 phosphorylation occurs on serine residues and that K8/18 glycosylation consists of O-linked single N-acetylglucosamines (O-GlcNAc) that are linked to Ser/Thr.
7538124	2	85	attach	linked	402:407	arg2	N-acetylglucosamines					361:380	O-linked single N-acetylglucosamines	345:380	O-linked single N-acetylglucosamines (O-GlcNAc) that are linked to Ser/Thr	345:418	We previously showed that K8/18 phosphorylation occurs on serine residues and that K8/18 glycosylation consists of O-linked single N-acetylglucosamines (O-GlcNAc) that are linked to Ser/Thr.
7538124	5	86	theme	human	965:969	arg1	cells					979:983	human colonic cells	965:983	human colonic cells	965:983	We identified the major glycosylation sites of K18 by comparing the tryptic 3H-glycopeptide pattern of the panel of mutant and wild type K18 expressed in the insect cells with the glycopeptides of K18 in human colonic cells.
7538124	7	87	theme	K18	1196:1198	arg1	construct					1200:1208	a K18 construct	1194:1208	a K18 construct that was mutated at the molecularly identified sites then transfected into NIH-3T3 cells	1194:1297	The precise modified residues in human cells were verified using Edman degradation and confirmed further by the lack of glycosylation of a K18 construct that was mutated at the molecularly identified sites then transfected into NIH-3T3 cells.
7538124	2	88	link	O-linked	345:352	arg1	O-GlcNAc					383:390	O-GlcNAc	383:390	O-GlcNAc	383:390	We previously showed that K8/18 phosphorylation occurs on serine residues and that K8/18 glycosylation consists of O-linked single N-acetylglucosamines (O-GlcNAc) that are linked to Ser/Thr.
7538124	2	88	link	O-linked	345:352	arg1	N-acetylglucosamines					361:380	O-linked single N-acetylglucosamines	345:380	O-linked single N-acetylglucosamines (O-GlcNAc) that are linked to Ser/Thr	345:418	We previously showed that K8/18 phosphorylation occurs on serine residues and that K8/18 glycosylation consists of O-linked single N-acetylglucosamines (O-GlcNAc) that are linked to Ser/Thr.
7538124	8	89	theme	filament	1406:1413	arg1	assembly					1415:1422	filament assembly	1406:1422	filament assembly	1406:1422	Partial or total K18 glycosylation mutants transfected into mammalian cells manifested nondistinguishable filament assembly to cells transfected with wild type K8/18.
7538124	7	90	theme	Edman	1122:1126	arg1	degradation					1128:1138	Edman degradation	1122:1138	Edman degradation	1122:1138	The precise modified residues in human cells were verified using Edman degradation and confirmed further by the lack of glycosylation of a K18 construct that was mutated at the molecularly identified sites then transfected into NIH-3T3 cells.
7538124	5	91	from	glycopeptides	941:953	arg1	cells					979:983	human colonic cells	965:983	human colonic cells	965:983	We identified the major glycosylation sites of K18 by comparing the tryptic 3H-glycopeptide pattern of the panel of mutant and wild type K18 expressed in the insect cells with the glycopeptides of K18 in human colonic cells.
21917917	2	0	theme	membrane	450:457	arg1	structure					471:479	the membrane topological structure	446:479	the membrane topological structure of SNAT4, a transporter expressed predominantly in liver	446:536	By using chemical labeling, glycosylation, immunofluorescence combined with molecular modeling approaches, we resolved the membrane topological structure of SNAT4, a transporter expressed predominantly in liver.
21917917	9	1	gly	N-glycosylated	1478:1491	arg1	domain					1513:1518	a large N-glycosylated, extracellular loop domain	1470:1518	a large N-glycosylated, extracellular loop domain	1470:1518	Together, we showed that SNAT4 contains 10 transmembrane domains with extracellular N and C termini and a large N-glycosylated, extracellular loop domain.
21917917	1	2	theme	transporter	128:138	arg1	family					147:152	system N/A amino acid transporter (SNAT) family	106:152	system N/A amino acid transporter (SNAT) family	106:152	Members of system N/A amino acid transporter (SNAT) family mediate transport of neutral amino acids, including l-alanine, l-glutamine, and l-histidine, across the plasma membrane and are involved in a variety of cellular functions.
21917917	3	3	theme	SNAT4	647:651	arg1	mutant					637:642	the "Cys-null" mutant	622:642	the "Cys-null" mutant of SNAT4	622:651	To analyze the orientation using the chemical labeling and biotinylation approach, the "Cys-null" mutant of SNAT4 was first generated by mutating all five endogenous cysteine residues.
21917917	4	4	theme	nontransmembrane	839:854	arg1	domains					856:862	all possible nontransmembrane domains	826:862	all possible nontransmembrane domains of the Cys-null mutant	826:885	Based on predicted topological structures, a single cysteine residue was introduced individually into all possible nontransmembrane domains of the Cys-null mutant.
21917917	4	4	theme	nontransmembrane	839:854	arg1	mutant					880:885	the Cys-null mutant	867:885	the Cys-null mutant	867:885	Based on predicted topological structures, a single cysteine residue was introduced individually into all possible nontransmembrane domains of the Cys-null mutant.
21917917	9	5	contain	contains	1397:1404	arg1	SNAT4					1391:1395	SNAT4	1391:1395	SNAT4	1391:1395	Together, we showed that SNAT4 contains 10 transmembrane domains with extracellular N and C termini and a large N-glycosylated, extracellular loop domain.
21917917	9	5	contain	contains	1397:1404	arg2	domains					1423:1429	10 transmembrane domains	1406:1429	10 transmembrane domains with extracellular N and C termini	1406:1464	Together, we showed that SNAT4 contains 10 transmembrane domains with extracellular N and C termini and a large N-glycosylated, extracellular loop domain.
21917917	9	5	contain	contains	1397:1404	arg2	domain					1513:1518	a large N-glycosylated, extracellular loop domain	1470:1518	a large N-glycosylated, extracellular loop domain	1470:1518	Together, we showed that SNAT4 contains 10 transmembrane domains with extracellular N and C termini and a large N-glycosylated, extracellular loop domain.
21917917	8	6	theme	N-glycosylated	1320:1333	arg1	Asn-264					1357:1363	Asn-264	1357:1363	Asn-264	1357:1363	The orientation of this domain was further confirmed by the identification of two N-glycosylated residues, Asn-260 and Asn-264.
21917917	8	6	theme	N-glycosylated	1320:1333	arg1	Asn-260					1345:1351	Asn-260	1345:1351	Asn-260	1345:1351	The orientation of this domain was further confirmed by the identification of two N-glycosylated residues, Asn-260 and Asn-264.
21917917	8	6	theme	N-glycosylated	1320:1333	arg1	residues					1335:1342	two N-glycosylated residues	1316:1342	two N-glycosylated residues	1316:1342	The orientation of this domain was further confirmed by the identification of two N-glycosylated residues, Asn-260 and Asn-264.
21917917	5	7	theme	membrane-impermeable	986:1005	arg1	reagent					1025:1031	a membrane-impermeable cysteine-directed reagent	984:1031	a membrane-impermeable cysteine-directed reagent	984:1031	The cells expressing these mutants were labeled with N-biotinylaminoethyl methanethiosulfonate, a membrane-impermeable cysteine-directed reagent.
21917917	5	7	theme	membrane-impermeable	986:1005	arg1	methanethiosulfonate					962:981	N-biotinylaminoethyl methanethiosulfonate	941:981	N-biotinylaminoethyl methanethiosulfonate	941:981	The cells expressing these mutants were labeled with N-biotinylaminoethyl methanethiosulfonate, a membrane-impermeable cysteine-directed reagent.
21917917	7	8	theme	amino	1205:1209	arg1	residue					1216:1222	amino acid residue ∼242 to ∼335	1205:1235	amino acid residue ∼242 to ∼335	1205:1235	There are three extracellular loop domains, and among them, the second loop domain is the largest that spans from amino acid residue ∼242 to ∼335.
21917917	9	9	with	domain	1513:1518	arg1	C					1456:1456	C	1456:1456	C	1456:1456	Together, we showed that SNAT4 contains 10 transmembrane domains with extracellular N and C termini and a large N-glycosylated, extracellular loop domain.
21917917	9	9	with	domain	1513:1518	arg1	N					1450:1450	extracellular N	1436:1450	extracellular N	1436:1450	Together, we showed that SNAT4 contains 10 transmembrane domains with extracellular N and C termini and a large N-glycosylated, extracellular loop domain.
21917917	10	10	from	members	1713:1719	arg1	family					1752:1757	this amino acid transporter family	1724:1757	this amino acid transporter family	1724:1757	This is the first report concerning membrane topological structure of mammalian SNAT transporters, which will provide important implications for our understanding of structure-function of the members in this amino acid transporter family.
21917917	10	11	theme	transporter	1740:1750	arg1	family					1752:1757	this amino acid transporter family	1724:1757	this amino acid transporter family	1724:1757	This is the first report concerning membrane topological structure of mammalian SNAT transporters, which will provide important implications for our understanding of structure-function of the members in this amino acid transporter family.
21917917	7	12	theme	acid	1211:1214	arg1	residue					1216:1222	amino acid residue ∼242 to ∼335	1205:1235	amino acid residue ∼242 to ∼335	1205:1235	There are three extracellular loop domains, and among them, the second loop domain is the largest that spans from amino acid residue ∼242 to ∼335.
21917917	8	13	theme	residues	1335:1342	arg1	identification					1298:1311	the identification	1294:1311	the identification of two N-glycosylated residues, Asn-260 and Asn-264	1294:1363	The orientation of this domain was further confirmed by the identification of two N-glycosylated residues, Asn-260 and Asn-264.
21917917	9	14	theme	loop	1508:1511	arg1	domain					1513:1518	a large N-glycosylated, extracellular loop domain	1470:1518	a large N-glycosylated, extracellular loop domain	1470:1518	Together, we showed that SNAT4 contains 10 transmembrane domains with extracellular N and C termini and a large N-glycosylated, extracellular loop domain.
21917917	2	15	theme	SNAT4	484:488	arg1	structure					471:479	the membrane topological structure	446:479	the membrane topological structure of SNAT4, a transporter expressed predominantly in liver	446:536	By using chemical labeling, glycosylation, immunofluorescence combined with molecular modeling approaches, we resolved the membrane topological structure of SNAT4, a transporter expressed predominantly in liver.
21917917	1	16	theme	cellular	307:314	arg1	functions					316:324	cellular functions	307:324	cellular functions	307:324	Members of system N/A amino acid transporter (SNAT) family mediate transport of neutral amino acids, including l-alanine, l-glutamine, and l-histidine, across the plasma membrane and are involved in a variety of cellular functions.
21917917	10	17	theme	transporters	1606:1617	arg1	structure					1578:1586	membrane topological structure	1557:1586	membrane topological structure of mammalian SNAT transporters, which will provide important implications for our understanding of structure-function of the members in this amino acid transporter family	1557:1757	This is the first report concerning membrane topological structure of mammalian SNAT transporters, which will provide important implications for our understanding of structure-function of the members in this amino acid transporter family.
21917917	4	18	theme	topological	743:753	arg1	structures					755:764	predicted topological structures	733:764	predicted topological structures	733:764	Based on predicted topological structures, a single cysteine residue was introduced individually into all possible nontransmembrane domains of the Cys-null mutant.
21917917	1	19	theme	SNAT	141:144	arg1	family					147:152	system N/A amino acid transporter (SNAT) family	106:152	system N/A amino acid transporter (SNAT) family	106:152	Members of system N/A amino acid transporter (SNAT) family mediate transport of neutral amino acids, including l-alanine, l-glutamine, and l-histidine, across the plasma membrane and are involved in a variety of cellular functions.
21917917	0	20	theme	protein	86:92	arg1	structure					21:29	Membrane topological structure	0:29	Membrane topological structure of neutral system N/A amino acid transporter 4 (SNAT4) protein.	0:93	Membrane topological structure of neutral system N/A amino acid transporter 4 (SNAT4) protein.
21917917	1	21	theme	functions	316:324	arg1	variety					296:302	a variety	294:302	a variety of cellular functions	294:324	Members of system N/A amino acid transporter (SNAT) family mediate transport of neutral amino acids, including l-alanine, l-glutamine, and l-histidine, across the plasma membrane and are involved in a variety of cellular functions.
21917917	1	21	theme	functions	316:324	arg1	functions					316:324	cellular functions	307:324	cellular functions	307:324	Members of system N/A amino acid transporter (SNAT) family mediate transport of neutral amino acids, including l-alanine, l-glutamine, and l-histidine, across the plasma membrane and are involved in a variety of cellular functions.
21917917	7	22	theme	loop	1162:1165	arg1	domain					1167:1172	the second loop domain	1151:1172	the second loop domain	1151:1172	There are three extracellular loop domains, and among them, the second loop domain is the largest that spans from amino acid residue ∼242 to ∼335.
21917917	7	22	theme	loop	1162:1165	arg1	largest					1181:1187	largest	1181:1187	largest	1181:1187	There are three extracellular loop domains, and among them, the second loop domain is the largest that spans from amino acid residue ∼242 to ∼335.
21917917	2	23	theme	modeling	413:420	arg1	approaches					422:431	molecular modeling approaches	403:431	molecular modeling approaches	403:431	By using chemical labeling, glycosylation, immunofluorescence combined with molecular modeling approaches, we resolved the membrane topological structure of SNAT4, a transporter expressed predominantly in liver.
21917917	2	24	theme	chemical	336:343	arg1	glycosylation					355:367	glycosylation	355:367	glycosylation	355:367	By using chemical labeling, glycosylation, immunofluorescence combined with molecular modeling approaches, we resolved the membrane topological structure of SNAT4, a transporter expressed predominantly in liver.
21917917	2	24	theme	chemical	336:343	arg1	labeling					345:352	chemical labeling	336:352	chemical labeling	336:352	By using chemical labeling, glycosylation, immunofluorescence combined with molecular modeling approaches, we resolved the membrane topological structure of SNAT4, a transporter expressed predominantly in liver.
21917917	2	24	theme	chemical	336:343	arg1	immunofluorescence					370:387	immunofluorescence	370:387	immunofluorescence	370:387	By using chemical labeling, glycosylation, immunofluorescence combined with molecular modeling approaches, we resolved the membrane topological structure of SNAT4, a transporter expressed predominantly in liver.
21917917	0	25	theme	topological	9:19	arg1	structure					21:29	Membrane topological structure	0:29	Membrane topological structure of neutral system N/A amino acid transporter 4 (SNAT4) protein.	0:93	Membrane topological structure of neutral system N/A amino acid transporter 4 (SNAT4) protein.
21917917	6	26	theme	N-	1064:1065	arg1	orientations					1048:1059	the orientations	1044:1059	the orientations of N- and C-terminal domains	1044:1088	We mapped the orientations of N- and C-terminal domains.
21917917	4	27	theme	possible	830:837	arg1	domains					856:862	all possible nontransmembrane domains	826:862	all possible nontransmembrane domains of the Cys-null mutant	826:885	Based on predicted topological structures, a single cysteine residue was introduced individually into all possible nontransmembrane domains of the Cys-null mutant.
21917917	4	27	theme	possible	830:837	arg1	mutant					880:885	the Cys-null mutant	867:885	the Cys-null mutant	867:885	Based on predicted topological structures, a single cysteine residue was introduced individually into all possible nontransmembrane domains of the Cys-null mutant.
21917917	1	28	theme	family	147:152	arg1	Members					95:101	Members	95:101	Members of system N/A amino acid transporter (SNAT) family	95:152	Members of system N/A amino acid transporter (SNAT) family mediate transport of neutral amino acids, including l-alanine, l-glutamine, and l-histidine, across the plasma membrane and are involved in a variety of cellular functions.
21917917	0	29	theme	Membrane	0:7	arg1	structure					21:29	Membrane topological structure	0:29	Membrane topological structure of neutral system N/A amino acid transporter 4 (SNAT4) protein.	0:93	Membrane topological structure of neutral system N/A amino acid transporter 4 (SNAT4) protein.
21917917	7	30	theme	loop	1121:1124	arg1	domains					1126:1132	three extracellular loop domains	1101:1132	three extracellular loop domains	1101:1132	There are three extracellular loop domains, and among them, the second loop domain is the largest that spans from amino acid residue ∼242 to ∼335.
21917917	10	31	theme	members	1713:1719	arg1	structure-function					1687:1704	structure-function	1687:1704	structure-function	1687:1704	This is the first report concerning membrane topological structure of mammalian SNAT transporters, which will provide important implications for our understanding of structure-function of the members in this amino acid transporter family.
21917917	7	32	theme	extracellular	1107:1119	arg1	domains					1126:1132	three extracellular loop domains	1101:1132	three extracellular loop domains	1101:1132	There are three extracellular loop domains, and among them, the second loop domain is the largest that spans from amino acid residue ∼242 to ∼335.
21917917	10	33	theme	SNAT	1601:1604	arg1	transporters					1606:1617	mammalian SNAT transporters	1591:1617	mammalian SNAT transporters	1591:1617	This is the first report concerning membrane topological structure of mammalian SNAT transporters, which will provide important implications for our understanding of structure-function of the members in this amino acid transporter family.
21917917	4	34	theme	single	769:774	arg1	residue					785:791	a single cysteine residue	767:791	a single cysteine residue	767:791	Based on predicted topological structures, a single cysteine residue was introduced individually into all possible nontransmembrane domains of the Cys-null mutant.
21917917	7	35	dep	residue	1216:1222	arg1	to					1229:1230	to	1229:1230	to	1229:1230	There are three extracellular loop domains, and among them, the second loop domain is the largest that spans from amino acid residue ∼242 to ∼335.
21917917	9	36	theme	extracellular	1436:1448	arg1	N					1450:1450	extracellular N	1436:1450	extracellular N	1436:1450	Together, we showed that SNAT4 contains 10 transmembrane domains with extracellular N and C termini and a large N-glycosylated, extracellular loop domain.
21917917	6	37	theme	domains	1082:1088	arg1	orientations					1048:1059	the orientations	1044:1059	the orientations of N- and C-terminal domains	1044:1088	We mapped the orientations of N- and C-terminal domains.
21917917	10	38	theme	mammalian	1591:1599	arg1	transporters					1606:1617	mammalian SNAT transporters	1591:1617	mammalian SNAT transporters	1591:1617	This is the first report concerning membrane topological structure of mammalian SNAT transporters, which will provide important implications for our understanding of structure-function of the members in this amino acid transporter family.
21917917	3	39	theme	endogenous	694:703	arg1	residues					714:721	all five endogenous cysteine residues	685:721	all five endogenous cysteine residues	685:721	To analyze the orientation using the chemical labeling and biotinylation approach, the "Cys-null" mutant of SNAT4 was first generated by mutating all five endogenous cysteine residues.
21917917	2	40	theme	molecular	403:411	arg1	approaches					422:431	molecular modeling approaches	403:431	molecular modeling approaches	403:431	By using chemical labeling, glycosylation, immunofluorescence combined with molecular modeling approaches, we resolved the membrane topological structure of SNAT4, a transporter expressed predominantly in liver.
21917917	5	41	theme	N-biotinylaminoethyl	941:960	arg1	reagent					1025:1031	a membrane-impermeable cysteine-directed reagent	984:1031	a membrane-impermeable cysteine-directed reagent	984:1031	The cells expressing these mutants were labeled with N-biotinylaminoethyl methanethiosulfonate, a membrane-impermeable cysteine-directed reagent.
21917917	5	41	theme	N-biotinylaminoethyl	941:960	arg1	methanethiosulfonate					962:981	N-biotinylaminoethyl methanethiosulfonate	941:981	N-biotinylaminoethyl methanethiosulfonate	941:981	The cells expressing these mutants were labeled with N-biotinylaminoethyl methanethiosulfonate, a membrane-impermeable cysteine-directed reagent.
21917917	6	42	theme	C-terminal	1071:1080	arg1	domains					1082:1088	C-terminal domains	1071:1088	C-terminal domains	1071:1088	We mapped the orientations of N- and C-terminal domains.
21917917	0	43	theme	system	42:47	arg1	transporter					64:74	neutral system N/A amino acid transporter 4	34:76	neutral system N/A amino acid transporter 4 (SNAT4) protein	34:92	Membrane topological structure of neutral system N/A amino acid transporter 4 (SNAT4) protein.
21917917	3	44	theme	cysteine	705:712	arg1	residues					714:721	all five endogenous cysteine residues	685:721	all five endogenous cysteine residues	685:721	To analyze the orientation using the chemical labeling and biotinylation approach, the "Cys-null" mutant of SNAT4 was first generated by mutating all five endogenous cysteine residues.
21917917	10	45	theme	structure-function	1687:1704	arg1	understanding					1670:1682	our understanding	1666:1682	our understanding of structure-function of the members in this amino acid transporter family	1666:1757	This is the first report concerning membrane topological structure of mammalian SNAT transporters, which will provide important implications for our understanding of structure-function of the members in this amino acid transporter family.
21917917	1	46	theme	neutral	175:181	arg1	l-glutamine					217:227	l-glutamine	217:227	l-glutamine	217:227	Members of system N/A amino acid transporter (SNAT) family mediate transport of neutral amino acids, including l-alanine, l-glutamine, and l-histidine, across the plasma membrane and are involved in a variety of cellular functions.
21917917	1	46	theme	neutral	175:181	arg1	acids					189:193	neutral amino acids	175:193	neutral amino acids	175:193	Members of system N/A amino acid transporter (SNAT) family mediate transport of neutral amino acids, including l-alanine, l-glutamine, and l-histidine, across the plasma membrane and are involved in a variety of cellular functions.
21917917	1	46	theme	neutral	175:181	arg1	l-alanine					206:214	l-alanine	206:214	l-alanine	206:214	Members of system N/A amino acid transporter (SNAT) family mediate transport of neutral amino acids, including l-alanine, l-glutamine, and l-histidine, across the plasma membrane and are involved in a variety of cellular functions.
21917917	1	46	theme	neutral	175:181	arg1	l-histidine					234:244	l-histidine	234:244	l-histidine	234:244	Members of system N/A amino acid transporter (SNAT) family mediate transport of neutral amino acids, including l-alanine, l-glutamine, and l-histidine, across the plasma membrane and are involved in a variety of cellular functions.
21917917	0	47	theme	neutral	34:40	arg1	transporter					64:74	neutral system N/A amino acid transporter 4	34:76	neutral system N/A amino acid transporter 4 (SNAT4) protein	34:92	Membrane topological structure of neutral system N/A amino acid transporter 4 (SNAT4) protein.
21917917	1	48	theme	plasma	258:263	arg1	membrane					265:272	the plasma membrane	254:272	the plasma membrane	254:272	Members of system N/A amino acid transporter (SNAT) family mediate transport of neutral amino acids, including l-alanine, l-glutamine, and l-histidine, across the plasma membrane and are involved in a variety of cellular functions.
21917917	9	49	theme	transmembrane	1409:1421	arg1	domains					1423:1429	10 transmembrane domains	1406:1429	10 transmembrane domains with extracellular N and C termini	1406:1464	Together, we showed that SNAT4 contains 10 transmembrane domains with extracellular N and C termini and a large N-glycosylated, extracellular loop domain.
21917917	9	50	theme	large	1472:1476	arg1	domain					1513:1518	a large N-glycosylated, extracellular loop domain	1470:1518	a large N-glycosylated, extracellular loop domain	1470:1518	Together, we showed that SNAT4 contains 10 transmembrane domains with extracellular N and C termini and a large N-glycosylated, extracellular loop domain.
21917917	4	51	theme	cysteine	776:783	arg1	residue					785:791	a single cysteine residue	767:791	a single cysteine residue	767:791	Based on predicted topological structures, a single cysteine residue was introduced individually into all possible nontransmembrane domains of the Cys-null mutant.
21917917	9	52	with	domains	1423:1429	arg1	C					1456:1456	C	1456:1456	C	1456:1456	Together, we showed that SNAT4 contains 10 transmembrane domains with extracellular N and C termini and a large N-glycosylated, extracellular loop domain.
21917917	9	52	with	domains	1423:1429	arg1	N					1450:1450	extracellular N	1436:1450	extracellular N	1436:1450	Together, we showed that SNAT4 contains 10 transmembrane domains with extracellular N and C termini and a large N-glycosylated, extracellular loop domain.
21917917	1	53	theme	amino	183:187	arg1	l-glutamine					217:227	l-glutamine	217:227	l-glutamine	217:227	Members of system N/A amino acid transporter (SNAT) family mediate transport of neutral amino acids, including l-alanine, l-glutamine, and l-histidine, across the plasma membrane and are involved in a variety of cellular functions.
21917917	1	53	theme	amino	183:187	arg1	acids					189:193	neutral amino acids	175:193	neutral amino acids	175:193	Members of system N/A amino acid transporter (SNAT) family mediate transport of neutral amino acids, including l-alanine, l-glutamine, and l-histidine, across the plasma membrane and are involved in a variety of cellular functions.
21917917	1	53	theme	amino	183:187	arg1	l-alanine					206:214	l-alanine	206:214	l-alanine	206:214	Members of system N/A amino acid transporter (SNAT) family mediate transport of neutral amino acids, including l-alanine, l-glutamine, and l-histidine, across the plasma membrane and are involved in a variety of cellular functions.
21917917	1	53	theme	amino	183:187	arg1	l-histidine					234:244	l-histidine	234:244	l-histidine	234:244	Members of system N/A amino acid transporter (SNAT) family mediate transport of neutral amino acids, including l-alanine, l-glutamine, and l-histidine, across the plasma membrane and are involved in a variety of cellular functions.
21917917	0	54	theme	amino	53:57	arg1	transporter					64:74	neutral system N/A amino acid transporter 4	34:76	neutral system N/A amino acid transporter 4 (SNAT4) protein	34:92	Membrane topological structure of neutral system N/A amino acid transporter 4 (SNAT4) protein.
21917917	4	55	theme	mutant	880:885	arg1	domains					856:862	all possible nontransmembrane domains	826:862	all possible nontransmembrane domains of the Cys-null mutant	826:885	Based on predicted topological structures, a single cysteine residue was introduced individually into all possible nontransmembrane domains of the Cys-null mutant.
21917917	4	55	theme	mutant	880:885	arg1	mutant					880:885	the Cys-null mutant	867:885	the Cys-null mutant	867:885	Based on predicted topological structures, a single cysteine residue was introduced individually into all possible nontransmembrane domains of the Cys-null mutant.
21917917	2	56	theme	topological	459:469	arg1	structure					471:479	the membrane topological structure	446:479	the membrane topological structure of SNAT4, a transporter expressed predominantly in liver	446:536	By using chemical labeling, glycosylation, immunofluorescence combined with molecular modeling approaches, we resolved the membrane topological structure of SNAT4, a transporter expressed predominantly in liver.
21917917	10	57	theme	amino	1729:1733	arg1	family					1752:1757	this amino acid transporter family	1724:1757	this amino acid transporter family	1724:1757	This is the first report concerning membrane topological structure of mammalian SNAT transporters, which will provide important implications for our understanding of structure-function of the members in this amino acid transporter family.
21917917	8	58	gly	N-glycosylated	1320:1333	arg1	Asn-264					1357:1363	Asn-264	1357:1363	Asn-264	1357:1363	The orientation of this domain was further confirmed by the identification of two N-glycosylated residues, Asn-260 and Asn-264.
21917917	8	58	gly	N-glycosylated	1320:1333	arg1	Asn-260					1345:1351	Asn-260	1345:1351	Asn-260	1345:1351	The orientation of this domain was further confirmed by the identification of two N-glycosylated residues, Asn-260 and Asn-264.
21917917	8	58	gly	N-glycosylated	1320:1333	arg1	residues					1335:1342	two N-glycosylated residues	1316:1342	two N-glycosylated residues	1316:1342	The orientation of this domain was further confirmed by the identification of two N-glycosylated residues, Asn-260 and Asn-264.
21917917	9	59	theme	N-glycosylated	1478:1491	arg1	domain					1513:1518	a large N-glycosylated, extracellular loop domain	1470:1518	a large N-glycosylated, extracellular loop domain	1470:1518	Together, we showed that SNAT4 contains 10 transmembrane domains with extracellular N and C termini and a large N-glycosylated, extracellular loop domain.
21917917	0	60	theme	N/A	49:51	arg1	transporter					64:74	neutral system N/A amino acid transporter 4	34:76	neutral system N/A amino acid transporter 4 (SNAT4) protein	34:92	Membrane topological structure of neutral system N/A amino acid transporter 4 (SNAT4) protein.
21917917	4	61	theme	Cys-null	871:878	arg1	mutant					880:885	the Cys-null mutant	867:885	the Cys-null mutant	867:885	Based on predicted topological structures, a single cysteine residue was introduced individually into all possible nontransmembrane domains of the Cys-null mutant.
21917917	10	62	theme	first	1533:1537	arg1	report					1539:1544	the first report	1529:1544	the first report concerning membrane topological structure of mammalian SNAT transporters, which will provide important implications for our understanding of structure-function of the members in this amino acid transporter family	1529:1757	This is the first report concerning membrane topological structure of mammalian SNAT transporters, which will provide important implications for our understanding of structure-function of the members in this amino acid transporter family.
21917917	10	62	theme	first	1533:1537	arg1	This					1521:1524	This	1521:1524	This	1521:1524	This is the first report concerning membrane topological structure of mammalian SNAT transporters, which will provide important implications for our understanding of structure-function of the members in this amino acid transporter family.
21917917	9	63	dep	N	1450:1450	arg1	termini					1458:1464	termini	1458:1464	termini	1458:1464	Together, we showed that SNAT4 contains 10 transmembrane domains with extracellular N and C termini and a large N-glycosylated, extracellular loop domain.
21917917	10	64	theme	membrane	1557:1564	arg1	structure					1578:1586	membrane topological structure	1557:1586	membrane topological structure of mammalian SNAT transporters, which will provide important implications for our understanding of structure-function of the members in this amino acid transporter family	1557:1757	This is the first report concerning membrane topological structure of mammalian SNAT transporters, which will provide important implications for our understanding of structure-function of the members in this amino acid transporter family.
21917917	10	65	theme	important	1639:1647	arg1	implications					1649:1660	important implications	1639:1660	important implications for our understanding of structure-function of the members in this amino acid transporter family	1639:1757	This is the first report concerning membrane topological structure of mammalian SNAT transporters, which will provide important implications for our understanding of structure-function of the members in this amino acid transporter family.
21917917	7	66	theme	second	1155:1160	arg1	domain					1167:1172	the second loop domain	1151:1172	the second loop domain	1151:1172	There are three extracellular loop domains, and among them, the second loop domain is the largest that spans from amino acid residue ∼242 to ∼335.
21917917	7	66	theme	second	1155:1160	arg1	largest					1181:1187	largest	1181:1187	largest	1181:1187	There are three extracellular loop domains, and among them, the second loop domain is the largest that spans from amino acid residue ∼242 to ∼335.
21917917	5	67	theme	cysteine-directed	1007:1023	arg1	reagent					1025:1031	a membrane-impermeable cysteine-directed reagent	984:1031	a membrane-impermeable cysteine-directed reagent	984:1031	The cells expressing these mutants were labeled with N-biotinylaminoethyl methanethiosulfonate, a membrane-impermeable cysteine-directed reagent.
21917917	5	67	theme	cysteine-directed	1007:1023	arg1	methanethiosulfonate					962:981	N-biotinylaminoethyl methanethiosulfonate	941:981	N-biotinylaminoethyl methanethiosulfonate	941:981	The cells expressing these mutants were labeled with N-biotinylaminoethyl methanethiosulfonate, a membrane-impermeable cysteine-directed reagent.
21917917	1	68	theme	system	106:111	arg1	family					147:152	system N/A amino acid transporter (SNAT) family	106:152	system N/A amino acid transporter (SNAT) family	106:152	Members of system N/A amino acid transporter (SNAT) family mediate transport of neutral amino acids, including l-alanine, l-glutamine, and l-histidine, across the plasma membrane and are involved in a variety of cellular functions.
21917917	10	69	theme	topological	1566:1576	arg1	structure					1578:1586	membrane topological structure	1557:1586	membrane topological structure of mammalian SNAT transporters, which will provide important implications for our understanding of structure-function of the members in this amino acid transporter family	1557:1757	This is the first report concerning membrane topological structure of mammalian SNAT transporters, which will provide important implications for our understanding of structure-function of the members in this amino acid transporter family.
21917917	1	70	theme	acids	189:193	arg1	transport					162:170	transport	162:170	transport of neutral amino acids, including l-alanine, l-glutamine, and l-histidine, across the plasma membrane	162:272	Members of system N/A amino acid transporter (SNAT) family mediate transport of neutral amino acids, including l-alanine, l-glutamine, and l-histidine, across the plasma membrane and are involved in a variety of cellular functions.
21917917	4	71	theme	predicted	733:741	arg1	structures					755:764	predicted topological structures	733:764	predicted topological structures	733:764	Based on predicted topological structures, a single cysteine residue was introduced individually into all possible nontransmembrane domains of the Cys-null mutant.
21917917	3	72	theme	Cys-null	627:634	arg1	mutant					637:642	the "Cys-null" mutant	622:642	the "Cys-null" mutant of SNAT4	622:651	To analyze the orientation using the chemical labeling and biotinylation approach, the "Cys-null" mutant of SNAT4 was first generated by mutating all five endogenous cysteine residues.
21917917	3	73	theme	biotinylation	598:610	arg1	approach					612:619	biotinylation approach	598:619	biotinylation approach	598:619	To analyze the orientation using the chemical labeling and biotinylation approach, the "Cys-null" mutant of SNAT4 was first generated by mutating all five endogenous cysteine residues.
21917917	1	74	theme	N/A	113:115	arg1	family					147:152	system N/A amino acid transporter (SNAT) family	106:152	system N/A amino acid transporter (SNAT) family	106:152	Members of system N/A amino acid transporter (SNAT) family mediate transport of neutral amino acids, including l-alanine, l-glutamine, and l-histidine, across the plasma membrane and are involved in a variety of cellular functions.
21917917	0	75	theme	transporter	64:74	arg1	protein					86:92	neutral system N/A amino acid transporter 4 (SNAT4) protein	34:92	neutral system N/A amino acid transporter 4 (SNAT4) protein	34:92	Membrane topological structure of neutral system N/A amino acid transporter 4 (SNAT4) protein.
21917917	0	75	theme	transporter	64:74	arg1	SNAT4					79:83	SNAT4	79:83	SNAT4	79:83	Membrane topological structure of neutral system N/A amino acid transporter 4 (SNAT4) protein.
21917917	3	76	theme	"	635:635	arg1	mutant					637:642	the "Cys-null" mutant	622:642	the "Cys-null" mutant of SNAT4	622:651	To analyze the orientation using the chemical labeling and biotinylation approach, the "Cys-null" mutant of SNAT4 was first generated by mutating all five endogenous cysteine residues.
21917917	3	77	theme	chemical	576:583	arg1	labeling					585:592	the chemical labeling	572:592	the chemical labeling	572:592	To analyze the orientation using the chemical labeling and biotinylation approach, the "Cys-null" mutant of SNAT4 was first generated by mutating all five endogenous cysteine residues.
21917917	8	78	theme	domain	1262:1267	arg1	orientation					1242:1252	The orientation	1238:1252	The orientation of this domain	1238:1267	The orientation of this domain was further confirmed by the identification of two N-glycosylated residues, Asn-260 and Asn-264.
21917917	1	79	theme	amino	117:121	arg1	family					147:152	system N/A amino acid transporter (SNAT) family	106:152	system N/A amino acid transporter (SNAT) family	106:152	Members of system N/A amino acid transporter (SNAT) family mediate transport of neutral amino acids, including l-alanine, l-glutamine, and l-histidine, across the plasma membrane and are involved in a variety of cellular functions.
21917917	0	80	theme	acid	59:62	arg1	transporter					64:74	neutral system N/A amino acid transporter 4	34:76	neutral system N/A amino acid transporter 4 (SNAT4) protein	34:92	Membrane topological structure of neutral system N/A amino acid transporter 4 (SNAT4) protein.
21917917	10	81	theme	acid	1735:1738	arg1	family					1752:1757	this amino acid transporter family	1724:1757	this amino acid transporter family	1724:1757	This is the first report concerning membrane topological structure of mammalian SNAT transporters, which will provide important implications for our understanding of structure-function of the members in this amino acid transporter family.
21917917	9	82	dep	N-glycosylated	1478:1491	arg1	extracellular					1494:1506	extracellular	1494:1506	extracellular	1494:1506	Together, we showed that SNAT4 contains 10 transmembrane domains with extracellular N and C termini and a large N-glycosylated, extracellular loop domain.
21917917	1	83	theme	acid	123:126	arg1	family					147:152	system N/A amino acid transporter (SNAT) family	106:152	system N/A amino acid transporter (SNAT) family	106:152	Members of system N/A amino acid transporter (SNAT) family mediate transport of neutral amino acids, including l-alanine, l-glutamine, and l-histidine, across the plasma membrane and are involved in a variety of cellular functions.
21158410	5	0	theme	protein	871:877	arg1	preparation					879:889	a soluble protein preparation	861:889	a soluble protein preparation of mouse brain tissue	861:911	The enrichment method was developed and optimized using an alpha-crystallin standard protein and then applied to a soluble protein preparation of mouse brain tissue and a nuclear preparation generated from HeLa cells.
21158410	1	1	theme	selective	184:192	arg1	method					194:199	A selective method	182:199	A selective method for the enrichment of O-GlcNAcylated peptides using a novel CLICK chemistry reagent	182:283	A selective method for the enrichment of O-GlcNAcylated peptides using a novel CLICK chemistry reagent is described.
21158410	4	2	theme	electron	672:679	arg1	dissociation					690:701	electron transfer dissociation	672:701	electron transfer dissociation	672:701	Modified peptides were analyzed using a combination of higher energy collision dissociation for identification and electron transfer dissociation to localize the site of O-GlcNAc attachment.
21158410	5	3	theme	enrichment	752:761	arg1	method					763:768	The enrichment method	748:768	The enrichment method	748:768	The enrichment method was developed and optimized using an alpha-crystallin standard protein and then applied to a soluble protein preparation of mouse brain tissue and a nuclear preparation generated from HeLa cells.
21158410	6	4	theme	peptides	1002:1009	arg1	total					968:972	A total	966:972	A total of 42 unique O-GlcNAcylated peptides	966:1009	A total of 42 unique O-GlcNAcylated peptides were identified, including 7 novel O-GlcNAc sites.
21158410	4	5	theme	transfer	681:688	arg1	dissociation					690:701	electron transfer dissociation	672:701	electron transfer dissociation	672:701	Modified peptides were analyzed using a combination of higher energy collision dissociation for identification and electron transfer dissociation to localize the site of O-GlcNAc attachment.
21158410	0	6	theme	dioxide	136:142	arg1	chromatography					144:157	titanium dioxide chromatography	127:157	titanium dioxide chromatography	127:157	Purification and identification of O-GlcNAc-modified peptides using phosphate-based alkyne CLICK chemistry in combination with titanium dioxide chromatography and mass spectrometry.
21158410	6	7	theme	O-GlcNAcylated	987:1000	arg1	peptides					1002:1009	42 unique O-GlcNAcylated peptides	977:1009	42 unique O-GlcNAcylated peptides	977:1009	A total of 42 unique O-GlcNAcylated peptides were identified, including 7 novel O-GlcNAc sites.
21158410	3	8	theme	dioxide	533:539	arg1	chromatography					541:554	titanium dioxide chromatography	524:554	titanium dioxide chromatography	524:554	The azide was then reacted with a phospho-alkyne using CLICK chemistry and O-GlcNAcGalNAzPO(4)-containing peptides were enriched using titanium dioxide chromatography.
21158410	5	9	theme	mouse	894:898	arg1	tissue					906:911	mouse brain tissue	894:911	mouse brain tissue	894:911	The enrichment method was developed and optimized using an alpha-crystallin standard protein and then applied to a soluble protein preparation of mouse brain tissue and a nuclear preparation generated from HeLa cells.
21158410	0	10	theme	titanium	127:134	arg1	chromatography					144:157	titanium dioxide chromatography	127:157	titanium dioxide chromatography	127:157	Purification and identification of O-GlcNAc-modified peptides using phosphate-based alkyne CLICK chemistry in combination with titanium dioxide chromatography and mass spectrometry.
21158410	6	11	theme	unique	980:985	arg1	peptides					1002:1009	42 unique O-GlcNAcylated peptides	977:1009	42 unique O-GlcNAcylated peptides	977:1009	A total of 42 unique O-GlcNAcylated peptides were identified, including 7 novel O-GlcNAc sites.
21158410	6	12	theme	novel	1040:1044	arg1	sites					1055:1059	7 novel O-GlcNAc sites	1038:1059	7 novel O-GlcNAc sites	1038:1059	A total of 42 unique O-GlcNAcylated peptides were identified, including 7 novel O-GlcNAc sites.
21158410	3	13	theme	CLICK	444:448	arg1	chemistry					450:458	CLICK chemistry	444:458	CLICK chemistry	444:458	The azide was then reacted with a phospho-alkyne using CLICK chemistry and O-GlcNAcGalNAzPO(4)-containing peptides were enriched using titanium dioxide chromatography.
21158410	4	14	theme	Modified	557:564	arg1	peptides					566:573	Modified peptides	557:573	Modified peptides	557:573	Modified peptides were analyzed using a combination of higher energy collision dissociation for identification and electron transfer dissociation to localize the site of O-GlcNAc attachment.
21158410	4	15	theme	dissociation	636:647	arg1	combination					597:607	a combination	595:607	a combination of higher energy collision dissociation for identification and electron transfer dissociation	595:701	Modified peptides were analyzed using a combination of higher energy collision dissociation for identification and electron transfer dissociation to localize the site of O-GlcNAc attachment.
21158410	3	16	theme	-containing	483:493	arg1	peptides					495:502	O-GlcNAcGalNAzPO(4)-containing peptides	464:502	O-GlcNAcGalNAzPO(4)-containing peptides	464:502	The azide was then reacted with a phospho-alkyne using CLICK chemistry and O-GlcNAcGalNAzPO(4)-containing peptides were enriched using titanium dioxide chromatography.
21158410	5	17	theme	nuclear	919:925	arg1	preparation					927:937	a nuclear preparation	917:937	a nuclear preparation generated from HeLa cells	917:963	The enrichment method was developed and optimized using an alpha-crystallin standard protein and then applied to a soluble protein preparation of mouse brain tissue and a nuclear preparation generated from HeLa cells.
21158410	4	18	theme	collision	626:634	arg1	dissociation					636:647	higher energy collision dissociation	612:647	higher energy collision dissociation for identification and electron transfer dissociation	612:701	Modified peptides were analyzed using a combination of higher energy collision dissociation for identification and electron transfer dissociation to localize the site of O-GlcNAc attachment.
21158410	0	19	with	combination	110:120	arg1	chromatography					144:157	titanium dioxide chromatography	127:157	titanium dioxide chromatography	127:157	Purification and identification of O-GlcNAc-modified peptides using phosphate-based alkyne CLICK chemistry in combination with titanium dioxide chromatography and mass spectrometry.
21158410	0	19	with	combination	110:120	arg1	spectrometry					168:179	mass spectrometry	163:179	mass spectrometry	163:179	Purification and identification of O-GlcNAc-modified peptides using phosphate-based alkyne CLICK chemistry in combination with titanium dioxide chromatography and mass spectrometry.
21158410	5	20	theme	brain	900:904	arg1	tissue					906:911	mouse brain tissue	894:911	mouse brain tissue	894:911	The enrichment method was developed and optimized using an alpha-crystallin standard protein and then applied to a soluble protein preparation of mouse brain tissue and a nuclear preparation generated from HeLa cells.
21158410	3	21	theme	titanium	524:531	arg1	dioxide					533:539	titanium dioxide	524:539	titanium dioxide chromatography	524:554	The azide was then reacted with a phospho-alkyne using CLICK chemistry and O-GlcNAcGalNAzPO(4)-containing peptides were enriched using titanium dioxide chromatography.
21158410	5	22	theme	alpha-crystallin	807:822	arg1	protein					833:839	an alpha-crystallin standard protein	804:839	an alpha-crystallin standard protein	804:839	The enrichment method was developed and optimized using an alpha-crystallin standard protein and then applied to a soluble protein preparation of mouse brain tissue and a nuclear preparation generated from HeLa cells.
21158410	1	23	theme	peptides	238:245	arg1	enrichment					209:218	the enrichment	205:218	the enrichment of O-GlcNAcylated peptides	205:245	A selective method for the enrichment of O-GlcNAcylated peptides using a novel CLICK chemistry reagent is described.
21158410	0	24	theme	peptides	53:60	arg1	identification					17:30	identification	17:30	identification	17:30	Purification and identification of O-GlcNAc-modified peptides using phosphate-based alkyne CLICK chemistry in combination with titanium dioxide chromatography and mass spectrometry.
21158410	0	24	theme	peptides	53:60	arg1	Purification					0:11	Purification	0:11	Purification	0:11	Purification and identification of O-GlcNAc-modified peptides using phosphate-based alkyne CLICK chemistry in combination with titanium dioxide chromatography and mass spectrometry.
21158410	5	25	theme	standard	824:831	arg1	protein					833:839	an alpha-crystallin standard protein	804:839	an alpha-crystallin standard protein	804:839	The enrichment method was developed and optimized using an alpha-crystallin standard protein and then applied to a soluble protein preparation of mouse brain tissue and a nuclear preparation generated from HeLa cells.
21158410	0	26	from	chemistry	97:105	arg1	combination					110:120	combination	110:120	combination with titanium dioxide chromatography and mass spectrometry	110:179	Purification and identification of O-GlcNAc-modified peptides using phosphate-based alkyne CLICK chemistry in combination with titanium dioxide chromatography and mass spectrometry.
21158410	5	27	theme	HeLa	954:957	arg1	cells					959:963	HeLa cells	954:963	HeLa cells	954:963	The enrichment method was developed and optimized using an alpha-crystallin standard protein and then applied to a soluble protein preparation of mouse brain tissue and a nuclear preparation generated from HeLa cells.
21158410	0	28	theme	O-GlcNAc-modified	35:51	arg1	peptides					53:60	O-GlcNAc-modified peptides	35:60	O-GlcNAc-modified peptides using phosphate-based alkyne CLICK chemistry in combination with titanium dioxide chromatography and mass spectrometry	35:179	Purification and identification of O-GlcNAc-modified peptides using phosphate-based alkyne CLICK chemistry in combination with titanium dioxide chromatography and mass spectrometry.
21158410	0	29	theme	mass	163:166	arg1	spectrometry					168:179	mass spectrometry	163:179	mass spectrometry	163:179	Purification and identification of O-GlcNAc-modified peptides using phosphate-based alkyne CLICK chemistry in combination with titanium dioxide chromatography and mass spectrometry.
21158410	4	30	theme	attachment	736:745	arg1	attachment					736:745	O-GlcNAc attachment	727:745	O-GlcNAc attachment	727:745	Modified peptides were analyzed using a combination of higher energy collision dissociation for identification and electron transfer dissociation to localize the site of O-GlcNAc attachment.
21158410	4	30	theme	attachment	736:745	arg1	site					719:722	the site	715:722	the site of O-GlcNAc attachment	715:745	Modified peptides were analyzed using a combination of higher energy collision dissociation for identification and electron transfer dissociation to localize the site of O-GlcNAc attachment.
21158410	0	31	theme	phosphate-based	68:82	arg1	chemistry					97:105	phosphate-based alkyne CLICK chemistry	68:105	phosphate-based alkyne CLICK chemistry in combination with titanium dioxide chromatography and mass spectrometry	68:179	Purification and identification of O-GlcNAc-modified peptides using phosphate-based alkyne CLICK chemistry in combination with titanium dioxide chromatography and mass spectrometry.
21158410	6	32	theme	O-GlcNAc	1046:1053	arg1	sites					1055:1059	7 novel O-GlcNAc sites	1038:1059	7 novel O-GlcNAc sites	1038:1059	A total of 42 unique O-GlcNAcylated peptides were identified, including 7 novel O-GlcNAc sites.
21158410	5	33	theme	soluble	863:869	arg1	preparation					879:889	a soluble protein preparation	861:889	a soluble protein preparation of mouse brain tissue	861:911	The enrichment method was developed and optimized using an alpha-crystallin standard protein and then applied to a soluble protein preparation of mouse brain tissue and a nuclear preparation generated from HeLa cells.
21158410	5	34	theme	tissue	906:911	arg1	preparation					927:937	a nuclear preparation	917:937	a nuclear preparation generated from HeLa cells	917:963	The enrichment method was developed and optimized using an alpha-crystallin standard protein and then applied to a soluble protein preparation of mouse brain tissue and a nuclear preparation generated from HeLa cells.
21158410	5	34	theme	tissue	906:911	arg1	preparation					879:889	a soluble protein preparation	861:889	a soluble protein preparation of mouse brain tissue	861:911	The enrichment method was developed and optimized using an alpha-crystallin standard protein and then applied to a soluble protein preparation of mouse brain tissue and a nuclear preparation generated from HeLa cells.
21158410	4	35	theme	energy	619:624	arg1	dissociation					636:647	higher energy collision dissociation	612:647	higher energy collision dissociation for identification and electron transfer dissociation	612:701	Modified peptides were analyzed using a combination of higher energy collision dissociation for identification and electron transfer dissociation to localize the site of O-GlcNAc attachment.
21158410	4	36	theme	higher	612:617	arg1	dissociation					636:647	higher energy collision dissociation	612:647	higher energy collision dissociation for identification and electron transfer dissociation	612:701	Modified peptides were analyzed using a combination of higher energy collision dissociation for identification and electron transfer dissociation to localize the site of O-GlcNAc attachment.
21158410	1	37	theme	novel	255:259	arg1	reagent					277:283	a novel CLICK chemistry reagent	253:283	a novel CLICK chemistry reagent	253:283	A selective method for the enrichment of O-GlcNAcylated peptides using a novel CLICK chemistry reagent is described.
21158410	1	38	theme	CLICK	261:265	arg1	reagent					277:283	a novel CLICK chemistry reagent	253:283	a novel CLICK chemistry reagent	253:283	A selective method for the enrichment of O-GlcNAcylated peptides using a novel CLICK chemistry reagent is described.
21158410	0	39	theme	CLICK	91:95	arg1	chemistry					97:105	phosphate-based alkyne CLICK chemistry	68:105	phosphate-based alkyne CLICK chemistry in combination with titanium dioxide chromatography and mass spectrometry	68:179	Purification and identification of O-GlcNAc-modified peptides using phosphate-based alkyne CLICK chemistry in combination with titanium dioxide chromatography and mass spectrometry.
21158410	1	40	theme	O-GlcNAcylated	223:236	arg1	peptides					238:245	O-GlcNAcylated peptides	223:245	O-GlcNAcylated peptides	223:245	A selective method for the enrichment of O-GlcNAcylated peptides using a novel CLICK chemistry reagent is described.
21158410	1	41	theme	chemistry	267:275	arg1	reagent					277:283	a novel CLICK chemistry reagent	253:283	a novel CLICK chemistry reagent	253:283	A selective method for the enrichment of O-GlcNAcylated peptides using a novel CLICK chemistry reagent is described.
21158410	0	42	theme	alkyne	84:89	arg1	chemistry					97:105	phosphate-based alkyne CLICK chemistry	68:105	phosphate-based alkyne CLICK chemistry in combination with titanium dioxide chromatography and mass spectrometry	68:179	Purification and identification of O-GlcNAc-modified peptides using phosphate-based alkyne CLICK chemistry in combination with titanium dioxide chromatography and mass spectrometry.
21158410	4	43	theme	O-GlcNAc	727:734	arg1	attachment					736:745	O-GlcNAc attachment	727:745	O-GlcNAc attachment	727:745	Modified peptides were analyzed using a combination of higher energy collision dissociation for identification and electron transfer dissociation to localize the site of O-GlcNAc attachment.
9336835	8	0	theme	sites	1261:1265	arg1	total					1225:1229	A total	1223:1229	A total of six N-linked glycosylation sites	1223:1265	A total of six N-linked glycosylation sites were identified, three in the alpha subunit (alpha 64N, alpha 81N, alpha 123N) and three in the beta subunit (beta 64N, beta 127N, and beta 147N).
9336835	9	1	with	structure	1698:1706	arg1	fucose					1717:1722	two fucose	1713:1722	two fucose	1713:1722	Seven different possible types of oligosaccharide structures were identified by mass including: a monosialobiantennary structure, bisialobiantennary structures without or with one fucose, trisialotriantennary structures without or with one fucose, and possibly a trisialotriantennary structure with two fucose and/or a tetrasialotriantennary structure.
9336835	9	1	with	structure	1698:1706	arg1	structure					1756:1764	a tetrasialotriantennary structure	1731:1764	a tetrasialotriantennary structure	1731:1764	Seven different possible types of oligosaccharide structures were identified by mass including: a monosialobiantennary structure, bisialobiantennary structures without or with one fucose, trisialotriantennary structures without or with one fucose, and possibly a trisialotriantennary structure with two fucose and/or a tetrasialotriantennary structure.
9336835	14	2	theme	clusterin	2523:2531	arg1	relationships					2552:2564	clusterin structure-function relationships	2523:2564	clusterin structure-function relationships	2523:2564	The results provide a molecular basis for developing a better understanding of clusterin structure-function relationships and the role clusterin glycosylation plays in physiological function.
9336835	10	3	theme	glycosylation	1801:1813	arg1	diversity					1815:1823	the least glycosylation diversity	1791:1823	the least glycosylation diversity	1791:1823	Site beta 64N exhibited the least glycosylation diversity, with two detected types of oligosaccharides, and site beta 147N exhibited the greatest diversity, with five or six detected types of oligosaccharides.
9336835	9	4	theme	oligosaccharide	1448:1462	arg1	structures					1464:1473	oligosaccharide structures	1448:1473	oligosaccharide structures	1448:1473	Seven different possible types of oligosaccharide structures were identified by mass including: a monosialobiantennary structure, bisialobiantennary structures without or with one fucose, trisialotriantennary structures without or with one fucose, and possibly a trisialotriantennary structure with two fucose and/or a tetrasialotriantennary structure.
9336835	2	5	from	Identification	217:230	arg1	clusterin					335:343	human serum clusterin	323:343	human serum clusterin	323:343	Identification of oligosaccharide attachment sites and structural characterization of oligosaccharides in human serum clusterin has been performed by mass spectrometry and Edman degradation.
9336835	2	6	theme	sites	262:266	arg1	Identification					217:230	Identification	217:230	Identification of oligosaccharide attachment sites	217:266	Identification of oligosaccharide attachment sites and structural characterization of oligosaccharides in human serum clusterin has been performed by mass spectrometry and Edman degradation.
9336835	2	6	theme	sites	262:266	arg1	characterization					283:298	structural characterization	272:298	structural characterization of oligosaccharides	272:318	Identification of oligosaccharide attachment sites and structural characterization of oligosaccharides in human serum clusterin has been performed by mass spectrometry and Edman degradation.
9336835	4	7	theme	clusterin	670:678	arg1	subunits					658:665	both the alpha and beta subunits	634:665	subunits	658:665	Mass spectrometry also revealed molecular heterogeneity associated with both the alpha and beta subunits of clusterin, consistent with the presence of multiple glycoforms.
9336835	2	8	theme	human	323:327	arg1	clusterin					335:343	human serum clusterin	323:343	human serum clusterin	323:343	Identification of oligosaccharide attachment sites and structural characterization of oligosaccharides in human serum clusterin has been performed by mass spectrometry and Edman degradation.
9336835	6	9	theme	collision	970:978	arg1	scanning					987:994	stepped collision energy scanning	962:994	stepped collision energy scanning	962:994	Liquid chromatography electrospray mass spectrometry with stepped collision energy scanning was used to selectively identify and preparatively fractionate tryptic glycopeptides.
9336835	8	10	theme	alpha	1334:1338	arg1	64N					1318:1320	alpha 64N	1312:1320	alpha 64N	1312:1320	A total of six N-linked glycosylation sites were identified, three in the alpha subunit (alpha 64N, alpha 81N, alpha 123N) and three in the beta subunit (beta 64N, beta 127N, and beta 147N).
9336835	8	10	theme	alpha	1334:1338	arg1	123N					1340:1343	alpha 123N	1334:1343	alpha 123N	1334:1343	A total of six N-linked glycosylation sites were identified, three in the alpha subunit (alpha 64N, alpha 81N, alpha 123N) and three in the beta subunit (beta 64N, beta 127N, and beta 147N).
9336835	6	11	gly	glycopeptides	1067:1079	arg2	glycopeptides					1067:1079	tryptic glycopeptides	1059:1079	tryptic glycopeptides	1059:1079	Liquid chromatography electrospray mass spectrometry with stepped collision energy scanning was used to selectively identify and preparatively fractionate tryptic glycopeptides.
9336835	10	12	theme	beta	1880:1883	arg1	147N					1885:1888	site beta 147N	1875:1888	site beta 147N	1875:1888	Site beta 64N exhibited the least glycosylation diversity, with two detected types of oligosaccharides, and site beta 147N exhibited the greatest diversity, with five or six detected types of oligosaccharides.
9336835	12	13	theme	primary	2226:2232	arg1	structure					2234:2242	the primary structure	2222:2242	the primary structure	2222:2242	Clusterin peptides accounting for 99% of the primary structure were identified from analysis of the isolated alpha and beta subunits, including all Ser- and Thr-containing peptides.
9336835	7	14	theme	attachment	1185:1194	arg1	sites					1196:1200	the attachment sites	1181:1200	the attachment sites within each peptide	1181:1220	Edman sequence analysis was then used to confirm the identities of the glycopeptides and to define the attachment sites within each peptide.
9336835	10	15	theme	oligosaccharides	1853:1868	arg1	types					1844:1848	two detected types	1831:1848	two detected types of oligosaccharides	1831:1868	Site beta 64N exhibited the least glycosylation diversity, with two detected types of oligosaccharides, and site beta 147N exhibited the greatest diversity, with five or six detected types of oligosaccharides.
9336835	13	16	theme	oligosaccharides	2426:2441	arg1	presence					2393:2400	the presence	2389:2400	the presence of O-linked or sulfated oligosaccharides	2389:2441	No evidence was found for the presence of O-linked or sulfated oligosaccharides.
9336835	8	17	theme	alpha	1312:1316	arg1	64N					1318:1320	alpha 64N	1312:1320	alpha 64N	1312:1320	A total of six N-linked glycosylation sites were identified, three in the alpha subunit (alpha 64N, alpha 81N, alpha 123N) and three in the beta subunit (beta 64N, beta 127N, and beta 147N).
9336835	8	17	theme	alpha	1312:1316	arg1	81N					1329:1331	alpha 81N	1323:1331	alpha 81N	1323:1331	A total of six N-linked glycosylation sites were identified, three in the alpha subunit (alpha 64N, alpha 81N, alpha 123N) and three in the beta subunit (beta 64N, beta 127N, and beta 147N).
9336835	8	17	theme	alpha	1312:1316	arg1	123N					1340:1343	alpha 123N	1334:1343	alpha 123N	1334:1343	A total of six N-linked glycosylation sites were identified, three in the alpha subunit (alpha 64N, alpha 81N, alpha 123N) and three in the beta subunit (beta 64N, beta 127N, and beta 147N).
9336835	4	18	theme	glycoforms	722:731	arg1	presence					701:708	the presence	697:708	the presence of multiple glycoforms	697:731	Mass spectrometry also revealed molecular heterogeneity associated with both the alpha and beta subunits of clusterin, consistent with the presence of multiple glycoforms.
9336835	5	19	contain	contains	874:881	arg2	carbohydrate					890:901	27-30% carbohydrate	883:901	27-30% carbohydrate	883:901	The data indicate that clusterin contains 17-27% carbohydrate by weight, the alpha subunit contains 0-30% carbohydrate and the beta subunit contains 27-30% carbohydrate.
9336835	5	19	contain	contains	874:881	arg1	subunit					866:872	the beta subunit	857:872	the beta subunit	857:872	The data indicate that clusterin contains 17-27% carbohydrate by weight, the alpha subunit contains 0-30% carbohydrate and the beta subunit contains 27-30% carbohydrate.
9336835	2	20	theme	attachment	251:260	arg1	sites					262:266	oligosaccharide attachment sites	235:266	oligosaccharide attachment sites	235:266	Identification of oligosaccharide attachment sites and structural characterization of oligosaccharides in human serum clusterin has been performed by mass spectrometry and Edman degradation.
9336835	8	21	link	N-linked	1238:1245	arg1	sites					1261:1265	six N-linked glycosylation sites	1234:1265	six N-linked glycosylation sites	1234:1265	A total of six N-linked glycosylation sites were identified, three in the alpha subunit (alpha 64N, alpha 81N, alpha 123N) and three in the beta subunit (beta 64N, beta 127N, and beta 147N).
9336835	9	22	theme	bisialobiantennary	1544:1561	arg1	structures					1563:1572	bisialobiantennary structures	1544:1572	bisialobiantennary structures without or with one fucose	1544:1599	Seven different possible types of oligosaccharide structures were identified by mass including: a monosialobiantennary structure, bisialobiantennary structures without or with one fucose, trisialotriantennary structures without or with one fucose, and possibly a trisialotriantennary structure with two fucose and/or a tetrasialotriantennary structure.
9336835	9	22	theme	bisialobiantennary	1544:1561	arg1	structure					1533:1541	a monosialobiantennary structure	1510:1541	a monosialobiantennary structure	1510:1541	Seven different possible types of oligosaccharide structures were identified by mass including: a monosialobiantennary structure, bisialobiantennary structures without or with one fucose, trisialotriantennary structures without or with one fucose, and possibly a trisialotriantennary structure with two fucose and/or a tetrasialotriantennary structure.
9336835	2	23	theme	oligosaccharides	303:318	arg1	Identification					217:230	Identification	217:230	Identification of oligosaccharide attachment sites	217:266	Identification of oligosaccharide attachment sites and structural characterization of oligosaccharides in human serum clusterin has been performed by mass spectrometry and Edman degradation.
9336835	2	23	theme	oligosaccharides	303:318	arg1	characterization					283:298	structural characterization	272:298	structural characterization of oligosaccharides	272:318	Identification of oligosaccharide attachment sites and structural characterization of oligosaccharides in human serum clusterin has been performed by mass spectrometry and Edman degradation.
9336835	8	24	from	three	1350:1354	arg1	subunit					1368:1374	the beta subunit	1359:1374	the beta subunit (beta 64N, beta 127N, and beta 147N)	1359:1411	A total of six N-linked glycosylation sites were identified, three in the alpha subunit (alpha 64N, alpha 81N, alpha 123N) and three in the beta subunit (beta 64N, beta 127N, and beta 147N).
9336835	1	25	theme	multiple	144:151	arg1	functions					162:170	multiple possible functions	144:170	multiple possible functions that are likely influenced by glycosylation	144:214	Clusterin is a ubiquitous, heterodimeric glycoprotein with multiple possible functions that are likely influenced by glycosylation.
9336835	14	26	dep	role	2574:2577	arg1	plays					2603:2607	plays	2603:2607	plays in physiological function	2603:2633	The results provide a molecular basis for developing a better understanding of clusterin structure-function relationships and the role clusterin glycosylation plays in physiological function.
9336835	1	27	dep	ubiquitous	100:109	arg1	heterodimeric					112:124	heterodimeric	112:124	heterodimeric	112:124	Clusterin is a ubiquitous, heterodimeric glycoprotein with multiple possible functions that are likely influenced by glycosylation.
9336835	5	28	theme	0-30	834:837	arg1	%					838:838	%	838:838	%	838:838	The data indicate that clusterin contains 17-27% carbohydrate by weight, the alpha subunit contains 0-30% carbohydrate and the beta subunit contains 27-30% carbohydrate.
9336835	10	29	theme	greatest	1904:1911	arg1	diversity					1913:1921	the greatest diversity	1900:1921	the greatest diversity	1900:1921	Site beta 64N exhibited the least glycosylation diversity, with two detected types of oligosaccharides, and site beta 147N exhibited the greatest diversity, with five or six detected types of oligosaccharides.
9336835	0	30	from	characterization	19:34	arg1	clusterin					74:82	human serum clusterin	62:82	human serum clusterin	62:82	Identification and characterization of glycosylation sites in human serum clusterin.
9336835	7	31	theme	Edman	1082:1086	arg1	analysis					1097:1104	Edman sequence analysis	1082:1104	Edman sequence analysis	1082:1104	Edman sequence analysis was then used to confirm the identities of the glycopeptides and to define the attachment sites within each peptide.
9336835	7	32	used	used	1115:1118	arg2	analysis					1097:1104	Edman sequence analysis	1082:1104	Edman sequence analysis	1082:1104	Edman sequence analysis was then used to confirm the identities of the glycopeptides and to define the attachment sites within each peptide.
9336835	3	33	theme	laser	424:428	arg1	spectrometry					457:468	Matrix-assisted laser desorption ionization mass spectrometry	408:468	Matrix-assisted laser desorption ionization mass spectrometry	408:468	Matrix-assisted laser desorption ionization mass spectrometry revealed two molecular weight species of holoclusterin (58,505 +/- 250 and 63,507 +/- 200).
9336835	0	34	from	Identification	0:13	arg1	clusterin					74:82	human serum clusterin	62:82	human serum clusterin	62:82	Identification and characterization of glycosylation sites in human serum clusterin.
9336835	9	35	theme	trisialotriantennary	1602:1621	arg1	structures					1623:1632	trisialotriantennary structures	1602:1632	trisialotriantennary structures without or with one fucose	1602:1659	Seven different possible types of oligosaccharide structures were identified by mass including: a monosialobiantennary structure, bisialobiantennary structures without or with one fucose, trisialotriantennary structures without or with one fucose, and possibly a trisialotriantennary structure with two fucose and/or a tetrasialotriantennary structure.
9336835	9	35	theme	trisialotriantennary	1602:1621	arg1	structure					1533:1541	a monosialobiantennary structure	1510:1541	a monosialobiantennary structure	1510:1541	Seven different possible types of oligosaccharide structures were identified by mass including: a monosialobiantennary structure, bisialobiantennary structures without or with one fucose, trisialotriantennary structures without or with one fucose, and possibly a trisialotriantennary structure with two fucose and/or a tetrasialotriantennary structure.
9336835	9	36	with	structures	1563:1572	arg1	fucose					1717:1722	two fucose	1713:1722	two fucose	1713:1722	Seven different possible types of oligosaccharide structures were identified by mass including: a monosialobiantennary structure, bisialobiantennary structures without or with one fucose, trisialotriantennary structures without or with one fucose, and possibly a trisialotriantennary structure with two fucose and/or a tetrasialotriantennary structure.
9336835	9	36	with	structures	1563:1572	arg1	structure					1756:1764	a tetrasialotriantennary structure	1731:1764	a tetrasialotriantennary structure	1731:1764	Seven different possible types of oligosaccharide structures were identified by mass including: a monosialobiantennary structure, bisialobiantennary structures without or with one fucose, trisialotriantennary structures without or with one fucose, and possibly a trisialotriantennary structure with two fucose and/or a tetrasialotriantennary structure.
9336835	12	37	theme	Ser-	2329:2332	arg1	peptides					2353:2360	all Ser- and Thr-containing peptides	2325:2360	all Ser- and Thr-containing peptides	2325:2360	Clusterin peptides accounting for 99% of the primary structure were identified from analysis of the isolated alpha and beta subunits, including all Ser- and Thr-containing peptides.
9336835	5	38	theme	27-30	883:887	arg1	%					888:888	%	888:888	%	888:888	The data indicate that clusterin contains 17-27% carbohydrate by weight, the alpha subunit contains 0-30% carbohydrate and the beta subunit contains 27-30% carbohydrate.
9336835	1	39	with	glycoprotein	126:137	arg1	functions					162:170	multiple possible functions	144:170	multiple possible functions that are likely influenced by glycosylation	144:214	Clusterin is a ubiquitous, heterodimeric glycoprotein with multiple possible functions that are likely influenced by glycosylation.
9336835	3	40	theme	ionization	441:450	arg1	spectrometry					457:468	Matrix-assisted laser desorption ionization mass spectrometry	408:468	Matrix-assisted laser desorption ionization mass spectrometry	408:468	Matrix-assisted laser desorption ionization mass spectrometry revealed two molecular weight species of holoclusterin (58,505 +/- 250 and 63,507 +/- 200).
9336835	12	41	theme	Thr-containing	2338:2351	arg1	peptides					2353:2360	all Ser- and Thr-containing peptides	2325:2360	all Ser- and Thr-containing peptides	2325:2360	Clusterin peptides accounting for 99% of the primary structure were identified from analysis of the isolated alpha and beta subunits, including all Ser- and Thr-containing peptides.
9336835	10	42	theme	beta	1772:1775	arg1	64N					1777:1779	Site beta 64N	1767:1779	Site beta 64N	1767:1779	Site beta 64N exhibited the least glycosylation diversity, with two detected types of oligosaccharides, and site beta 147N exhibited the greatest diversity, with five or six detected types of oligosaccharides.
9336835	10	43	theme	detected	1835:1842	arg1	types					1844:1848	two detected types	1831:1848	two detected types of oligosaccharides	1831:1868	Site beta 64N exhibited the least glycosylation diversity, with two detected types of oligosaccharides, and site beta 147N exhibited the greatest diversity, with five or six detected types of oligosaccharides.
9336835	6	44	theme	stepped	962:968	arg1	scanning					987:994	stepped collision energy scanning	962:994	stepped collision energy scanning	962:994	Liquid chromatography electrospray mass spectrometry with stepped collision energy scanning was used to selectively identify and preparatively fractionate tryptic glycopeptides.
9336835	8	45	theme	beta	1377:1380	arg1	64N					1382:1384	beta 64N	1377:1384	beta 64N	1377:1384	A total of six N-linked glycosylation sites were identified, three in the alpha subunit (alpha 64N, alpha 81N, alpha 123N) and three in the beta subunit (beta 64N, beta 127N, and beta 147N).
9336835	3	46	theme	weight	493:498	arg1	species					500:506	two molecular weight species	479:506	two molecular weight species of holoclusterin	479:523	Matrix-assisted laser desorption ionization mass spectrometry revealed two molecular weight species of holoclusterin (58,505 +/- 250 and 63,507 +/- 200).
9336835	4	47	theme	alpha	643:647	arg1	subunits					658:665	both the alpha and beta subunits	634:665	subunits	658:665	Mass spectrometry also revealed molecular heterogeneity associated with both the alpha and beta subunits of clusterin, consistent with the presence of multiple glycoforms.
9336835	12	48	theme	subunits	2305:2312	arg1	analysis					2265:2272	analysis	2265:2272	analysis of the isolated alpha and beta subunits	2265:2312	Clusterin peptides accounting for 99% of the primary structure were identified from analysis of the isolated alpha and beta subunits, including all Ser- and Thr-containing peptides.
9336835	11	49	theme	abundant	1995:2002	arg1	glycoforms					2004:2013	the most abundant glycoforms	1986:2013	the most abundant glycoforms detected	1986:2022	Overall, the most abundant glycoforms detected were bisialobiantennary without fucose and the least abundant were monosialobiantennary, trisialotriantennary with two fucose and/or tetrasialotriantennary.
9336835	11	49	theme	abundant	1995:2002	arg1	bisialobiantennary					2029:2046	bisialobiantennary	2029:2046	bisialobiantennary	2029:2046	Overall, the most abundant glycoforms detected were bisialobiantennary without fucose and the least abundant were monosialobiantennary, trisialotriantennary with two fucose and/or tetrasialotriantennary.
9336835	0	50	theme	glycosylation	39:51	arg1	sites					53:57	glycosylation sites	39:57	glycosylation sites	39:57	Identification and characterization of glycosylation sites in human serum clusterin.
9336835	5	51	contain	contains	767:774	arg2	carbohydrate					783:794	17-27% carbohydrate	776:794	17-27% carbohydrate by weight	776:804	The data indicate that clusterin contains 17-27% carbohydrate by weight, the alpha subunit contains 0-30% carbohydrate and the beta subunit contains 27-30% carbohydrate.
9336835	5	51	contain	contains	767:774	arg1	clusterin					757:765	clusterin	757:765	clusterin	757:765	The data indicate that clusterin contains 17-27% carbohydrate by weight, the alpha subunit contains 0-30% carbohydrate and the beta subunit contains 27-30% carbohydrate.
9336835	8	52	dep	subunit	1303:1309	arg1	64N					1318:1320	alpha 64N	1312:1320	alpha 64N	1312:1320	A total of six N-linked glycosylation sites were identified, three in the alpha subunit (alpha 64N, alpha 81N, alpha 123N) and three in the beta subunit (beta 64N, beta 127N, and beta 147N).
9336835	8	52	dep	subunit	1303:1309	arg1	81N					1329:1331	alpha 81N	1323:1331	alpha 81N	1323:1331	A total of six N-linked glycosylation sites were identified, three in the alpha subunit (alpha 64N, alpha 81N, alpha 123N) and three in the beta subunit (beta 64N, beta 127N, and beta 147N).
9336835	8	52	dep	subunit	1303:1309	arg1	123N					1340:1343	alpha 123N	1334:1343	alpha 123N	1334:1343	A total of six N-linked glycosylation sites were identified, three in the alpha subunit (alpha 64N, alpha 81N, alpha 123N) and three in the beta subunit (beta 64N, beta 127N, and beta 147N).
9336835	0	53	theme	serum	68:72	arg1	clusterin					74:82	human serum clusterin	62:82	human serum clusterin	62:82	Identification and characterization of glycosylation sites in human serum clusterin.
9336835	14	54	theme	physiological	2612:2624	arg1	function					2626:2633	physiological function	2612:2633	physiological function	2612:2633	The results provide a molecular basis for developing a better understanding of clusterin structure-function relationships and the role clusterin glycosylation plays in physiological function.
9336835	10	55	theme	least	1795:1799	arg1	diversity					1815:1823	the least glycosylation diversity	1791:1823	the least glycosylation diversity	1791:1823	Site beta 64N exhibited the least glycosylation diversity, with two detected types of oligosaccharides, and site beta 147N exhibited the greatest diversity, with five or six detected types of oligosaccharides.
9336835	6	56	theme	electrospray	926:937	arg1	spectrometry					944:955	Liquid chromatography electrospray mass spectrometry	904:955	Liquid chromatography electrospray mass spectrometry with stepped collision energy scanning	904:994	Liquid chromatography electrospray mass spectrometry with stepped collision energy scanning was used to selectively identify and preparatively fractionate tryptic glycopeptides.
9336835	10	57	theme	oligosaccharides	1959:1974	arg1	types					1950:1954	five or six detected types	1929:1954	five or six detected types of oligosaccharides	1929:1974	Site beta 64N exhibited the least glycosylation diversity, with two detected types of oligosaccharides, and site beta 147N exhibited the greatest diversity, with five or six detected types of oligosaccharides.
9336835	12	58	theme	isolated	2281:2288	arg1	subunits					2305:2312	the isolated alpha and beta subunits	2277:2312	the isolated alpha and beta subunits	2277:2312	Clusterin peptides accounting for 99% of the primary structure were identified from analysis of the isolated alpha and beta subunits, including all Ser- and Thr-containing peptides.
9336835	6	59	theme	Liquid	904:909	arg1	spectrometry					944:955	Liquid chromatography electrospray mass spectrometry	904:955	Liquid chromatography electrospray mass spectrometry with stepped collision energy scanning	904:994	Liquid chromatography electrospray mass spectrometry with stepped collision energy scanning was used to selectively identify and preparatively fractionate tryptic glycopeptides.
9336835	9	60	theme	possible	1430:1437	arg1	types					1439:1443	Seven different possible types	1414:1443	Seven different possible types of oligosaccharide structures	1414:1473	Seven different possible types of oligosaccharide structures were identified by mass including: a monosialobiantennary structure, bisialobiantennary structures without or with one fucose, trisialotriantennary structures without or with one fucose, and possibly a trisialotriantennary structure with two fucose and/or a tetrasialotriantennary structure.
9336835	0	61	theme	human	62:66	arg1	clusterin					74:82	human serum clusterin	62:82	human serum clusterin	62:82	Identification and characterization of glycosylation sites in human serum clusterin.
9336835	4	62	theme	molecular	594:602	arg1	heterogeneity					604:616	molecular heterogeneity	594:616	molecular heterogeneity associated with both the alpha and beta subunits of clusterin, consistent with the presence of multiple glycoforms	594:731	Mass spectrometry also revealed molecular heterogeneity associated with both the alpha and beta subunits of clusterin, consistent with the presence of multiple glycoforms.
9336835	14	63	theme	structure-function	2533:2550	arg1	relationships					2552:2564	clusterin structure-function relationships	2523:2564	clusterin structure-function relationships	2523:2564	The results provide a molecular basis for developing a better understanding of clusterin structure-function relationships and the role clusterin glycosylation plays in physiological function.
9336835	13	64	link	O-linked	2405:2412	arg1	oligosaccharides					2426:2441	O-linked or sulfated oligosaccharides	2405:2441	O-linked or sulfated oligosaccharides	2405:2441	No evidence was found for the presence of O-linked or sulfated oligosaccharides.
9336835	4	65	theme	Mass	562:565	arg1	spectrometry					567:578	Mass spectrometry	562:578	Mass spectrometry	562:578	Mass spectrometry also revealed molecular heterogeneity associated with both the alpha and beta subunits of clusterin, consistent with the presence of multiple glycoforms.
9336835	4	66	theme	beta	653:656	arg1	subunits					658:665	both the alpha and beta subunits	634:665	subunits	658:665	Mass spectrometry also revealed molecular heterogeneity associated with both the alpha and beta subunits of clusterin, consistent with the presence of multiple glycoforms.
9336835	9	67	theme	structures	1464:1473	arg1	types					1439:1443	Seven different possible types	1414:1443	Seven different possible types of oligosaccharide structures	1414:1473	Seven different possible types of oligosaccharide structures were identified by mass including: a monosialobiantennary structure, bisialobiantennary structures without or with one fucose, trisialotriantennary structures without or with one fucose, and possibly a trisialotriantennary structure with two fucose and/or a tetrasialotriantennary structure.
9336835	10	68	theme	site	1875:1878	arg1	147N					1885:1888	site beta 147N	1875:1888	site beta 147N	1875:1888	Site beta 64N exhibited the least glycosylation diversity, with two detected types of oligosaccharides, and site beta 147N exhibited the greatest diversity, with five or six detected types of oligosaccharides.
9336835	9	69	theme	tetrasialotriantennary	1733:1754	arg1	structure					1756:1764	a tetrasialotriantennary structure	1731:1764	a tetrasialotriantennary structure	1731:1764	Seven different possible types of oligosaccharide structures were identified by mass including: a monosialobiantennary structure, bisialobiantennary structures without or with one fucose, trisialotriantennary structures without or with one fucose, and possibly a trisialotriantennary structure with two fucose and/or a tetrasialotriantennary structure.
9336835	9	70	theme	trisialotriantennary	1677:1696	arg1	structure					1698:1706	a trisialotriantennary structure	1675:1706	a trisialotriantennary structure with two fucose and/or a tetrasialotriantennary structure	1675:1764	Seven different possible types of oligosaccharide structures were identified by mass including: a monosialobiantennary structure, bisialobiantennary structures without or with one fucose, trisialotriantennary structures without or with one fucose, and possibly a trisialotriantennary structure with two fucose and/or a tetrasialotriantennary structure.
9336835	9	70	theme	trisialotriantennary	1677:1696	arg1	structure					1533:1541	a monosialobiantennary structure	1510:1541	a monosialobiantennary structure	1510:1541	Seven different possible types of oligosaccharide structures were identified by mass including: a monosialobiantennary structure, bisialobiantennary structures without or with one fucose, trisialotriantennary structures without or with one fucose, and possibly a trisialotriantennary structure with two fucose and/or a tetrasialotriantennary structure.
9336835	14	71	theme	better	2499:2504	arg1	understanding					2506:2518	a better understanding	2497:2518	a better understanding of clusterin structure-function relationships	2497:2564	The results provide a molecular basis for developing a better understanding of clusterin structure-function relationships and the role clusterin glycosylation plays in physiological function.
9336835	2	72	theme	serum	329:333	arg1	clusterin					335:343	human serum clusterin	323:343	human serum clusterin	323:343	Identification of oligosaccharide attachment sites and structural characterization of oligosaccharides in human serum clusterin has been performed by mass spectrometry and Edman degradation.
9336835	6	73	theme	energy	980:985	arg1	scanning					987:994	stepped collision energy scanning	962:994	stepped collision energy scanning	962:994	Liquid chromatography electrospray mass spectrometry with stepped collision energy scanning was used to selectively identify and preparatively fractionate tryptic glycopeptides.
9336835	8	74	theme	alpha	1323:1327	arg1	64N					1318:1320	alpha 64N	1312:1320	alpha 64N	1312:1320	A total of six N-linked glycosylation sites were identified, three in the alpha subunit (alpha 64N, alpha 81N, alpha 123N) and three in the beta subunit (beta 64N, beta 127N, and beta 147N).
9336835	8	74	theme	alpha	1323:1327	arg1	81N					1329:1331	alpha 81N	1323:1331	alpha 81N	1323:1331	A total of six N-linked glycosylation sites were identified, three in the alpha subunit (alpha 64N, alpha 81N, alpha 123N) and three in the beta subunit (beta 64N, beta 127N, and beta 147N).
9336835	12	75	theme	Clusterin	2181:2189	arg1	peptides					2191:2198	Clusterin peptides	2181:2198	Clusterin peptides accounting for 99% of the primary structure	2181:2242	Clusterin peptides accounting for 99% of the primary structure were identified from analysis of the isolated alpha and beta subunits, including all Ser- and Thr-containing peptides.
9336835	2	76	theme	mass	367:370	arg1	spectrometry					372:383	mass spectrometry	367:383	mass spectrometry	367:383	Identification of oligosaccharide attachment sites and structural characterization of oligosaccharides in human serum clusterin has been performed by mass spectrometry and Edman degradation.
9336835	8	77	from	three	1284:1288	arg1	subunit					1303:1309	the alpha subunit	1293:1309	the alpha subunit (alpha 64N, alpha 81N, alpha 123N)	1293:1344	A total of six N-linked glycosylation sites were identified, three in the alpha subunit (alpha 64N, alpha 81N, alpha 123N) and three in the beta subunit (beta 64N, beta 127N, and beta 147N).
9336835	1	78	gly	glycoprotein	126:137	arg1	Clusterin					85:93	Clusterin	85:93	Clusterin	85:93	Clusterin is a ubiquitous, heterodimeric glycoprotein with multiple possible functions that are likely influenced by glycosylation.
9336835	1	78	gly	glycoprotein	126:137	arg1	glycoprotein					126:137	a ubiquitous, heterodimeric glycoprotein	98:137	a ubiquitous, heterodimeric glycoprotein with multiple possible functions that are likely influenced by glycosylation	98:214	Clusterin is a ubiquitous, heterodimeric glycoprotein with multiple possible functions that are likely influenced by glycosylation.
9336835	13	79	theme	sulfated	2417:2424	arg1	oligosaccharides					2426:2441	O-linked or sulfated oligosaccharides	2405:2441	O-linked or sulfated oligosaccharides	2405:2441	No evidence was found for the presence of O-linked or sulfated oligosaccharides.
9336835	8	80	theme	alpha	1297:1301	arg1	subunit					1303:1309	the alpha subunit	1293:1309	the alpha subunit (alpha 64N, alpha 81N, alpha 123N)	1293:1344	A total of six N-linked glycosylation sites were identified, three in the alpha subunit (alpha 64N, alpha 81N, alpha 123N) and three in the beta subunit (beta 64N, beta 127N, and beta 147N).
9336835	14	81	theme	clusterin	2579:2587	arg1	glycosylation					2589:2601	clusterin glycosylation	2579:2601	clusterin glycosylation	2579:2601	The results provide a molecular basis for developing a better understanding of clusterin structure-function relationships and the role clusterin glycosylation plays in physiological function.
9336835	9	82	with	structures	1623:1632	arg1	fucose					1717:1722	two fucose	1713:1722	two fucose	1713:1722	Seven different possible types of oligosaccharide structures were identified by mass including: a monosialobiantennary structure, bisialobiantennary structures without or with one fucose, trisialotriantennary structures without or with one fucose, and possibly a trisialotriantennary structure with two fucose and/or a tetrasialotriantennary structure.
9336835	9	82	with	structures	1623:1632	arg1	structure					1756:1764	a tetrasialotriantennary structure	1731:1764	a tetrasialotriantennary structure	1731:1764	Seven different possible types of oligosaccharide structures were identified by mass including: a monosialobiantennary structure, bisialobiantennary structures without or with one fucose, trisialotriantennary structures without or with one fucose, and possibly a trisialotriantennary structure with two fucose and/or a tetrasialotriantennary structure.
9336835	2	83	theme	structural	272:281	arg1	characterization					283:298	structural characterization	272:298	structural characterization of oligosaccharides	272:318	Identification of oligosaccharide attachment sites and structural characterization of oligosaccharides in human serum clusterin has been performed by mass spectrometry and Edman degradation.
9336835	9	84	theme	monosialobiantennary	1512:1531	arg1	structures					1563:1572	bisialobiantennary structures	1544:1572	bisialobiantennary structures without or with one fucose	1544:1599	Seven different possible types of oligosaccharide structures were identified by mass including: a monosialobiantennary structure, bisialobiantennary structures without or with one fucose, trisialotriantennary structures without or with one fucose, and possibly a trisialotriantennary structure with two fucose and/or a tetrasialotriantennary structure.
9336835	9	84	theme	monosialobiantennary	1512:1531	arg1	structure					1698:1706	a trisialotriantennary structure	1675:1706	a trisialotriantennary structure with two fucose and/or a tetrasialotriantennary structure	1675:1764	Seven different possible types of oligosaccharide structures were identified by mass including: a monosialobiantennary structure, bisialobiantennary structures without or with one fucose, trisialotriantennary structures without or with one fucose, and possibly a trisialotriantennary structure with two fucose and/or a tetrasialotriantennary structure.
9336835	9	84	theme	monosialobiantennary	1512:1531	arg1	structures					1623:1632	trisialotriantennary structures	1602:1632	trisialotriantennary structures without or with one fucose	1602:1659	Seven different possible types of oligosaccharide structures were identified by mass including: a monosialobiantennary structure, bisialobiantennary structures without or with one fucose, trisialotriantennary structures without or with one fucose, and possibly a trisialotriantennary structure with two fucose and/or a tetrasialotriantennary structure.
9336835	9	84	theme	monosialobiantennary	1512:1531	arg1	structure					1533:1541	a monosialobiantennary structure	1510:1541	a monosialobiantennary structure	1510:1541	Seven different possible types of oligosaccharide structures were identified by mass including: a monosialobiantennary structure, bisialobiantennary structures without or with one fucose, trisialotriantennary structures without or with one fucose, and possibly a trisialotriantennary structure with two fucose and/or a tetrasialotriantennary structure.
9336835	6	85	theme	tryptic	1059:1065	arg1	glycopeptides					1067:1079	tryptic glycopeptides	1059:1079	tryptic glycopeptides	1059:1079	Liquid chromatography electrospray mass spectrometry with stepped collision energy scanning was used to selectively identify and preparatively fractionate tryptic glycopeptides.
9336835	8	86	theme	glycosylation	1247:1259	arg1	sites					1261:1265	six N-linked glycosylation sites	1234:1265	six N-linked glycosylation sites	1234:1265	A total of six N-linked glycosylation sites were identified, three in the alpha subunit (alpha 64N, alpha 81N, alpha 123N) and three in the beta subunit (beta 64N, beta 127N, and beta 147N).
9336835	4	87	theme	multiple	713:720	arg1	glycoforms					722:731	multiple glycoforms	713:731	multiple glycoforms	713:731	Mass spectrometry also revealed molecular heterogeneity associated with both the alpha and beta subunits of clusterin, consistent with the presence of multiple glycoforms.
9336835	7	88	theme	glycopeptides	1153:1165	arg1	identities					1135:1144	the identities	1131:1144	the identities of the glycopeptides	1131:1165	Edman sequence analysis was then used to confirm the identities of the glycopeptides and to define the attachment sites within each peptide.
9336835	4	89	with	consistent	681:690	arg1	presence					701:708	the presence	697:708	the presence of multiple glycoforms	697:731	Mass spectrometry also revealed molecular heterogeneity associated with both the alpha and beta subunits of clusterin, consistent with the presence of multiple glycoforms.
9336835	5	90	contain	contains	825:832	arg2	carbohydrate					840:851	0-30% carbohydrate	834:851	0-30% carbohydrate	834:851	The data indicate that clusterin contains 17-27% carbohydrate by weight, the alpha subunit contains 0-30% carbohydrate and the beta subunit contains 27-30% carbohydrate.
9336835	5	90	contain	contains	825:832	arg1	subunit					817:823	the alpha subunit	807:823	the alpha subunit	807:823	The data indicate that clusterin contains 17-27% carbohydrate by weight, the alpha subunit contains 0-30% carbohydrate and the beta subunit contains 27-30% carbohydrate.
9336835	5	91	theme	%	781:781	arg1	carbohydrate					783:794	17-27% carbohydrate	776:794	17-27% carbohydrate by weight	776:804	The data indicate that clusterin contains 17-27% carbohydrate by weight, the alpha subunit contains 0-30% carbohydrate and the beta subunit contains 27-30% carbohydrate.
9336835	7	92	gly	glycopeptides	1153:1165	arg2	glycopeptides					1153:1165	the glycopeptides	1149:1165	the glycopeptides	1149:1165	Edman sequence analysis was then used to confirm the identities of the glycopeptides and to define the attachment sites within each peptide.
9336835	14	93	theme	molecular	2466:2474	arg1	basis					2476:2480	a molecular basis	2464:2480	a molecular basis for developing a better understanding of clusterin structure-function relationships and the role clusterin glycosylation plays in physiological function	2464:2633	The results provide a molecular basis for developing a better understanding of clusterin structure-function relationships and the role clusterin glycosylation plays in physiological function.
9336835	0	94	gly	glycosylation	39:51	arg2	sites					53:57	glycosylation sites	39:57	glycosylation sites	39:57	Identification and characterization of glycosylation sites in human serum clusterin.
9336835	13	95	theme	O-linked	2405:2412	arg1	oligosaccharides					2426:2441	O-linked or sulfated oligosaccharides	2405:2441	O-linked or sulfated oligosaccharides	2405:2441	No evidence was found for the presence of O-linked or sulfated oligosaccharides.
9336835	11	96	with	trisialotriantennary	2113:2132	arg1	fucose					2143:2148	two fucose	2139:2148	two fucose	2139:2148	Overall, the most abundant glycoforms detected were bisialobiantennary without fucose and the least abundant were monosialobiantennary, trisialotriantennary with two fucose and/or tetrasialotriantennary.
9336835	11	96	with	trisialotriantennary	2113:2132	arg1	tetrasialotriantennary					2157:2178	tetrasialotriantennary	2157:2178	tetrasialotriantennary	2157:2178	Overall, the most abundant glycoforms detected were bisialobiantennary without fucose and the least abundant were monosialobiantennary, trisialotriantennary with two fucose and/or tetrasialotriantennary.
9336835	8	97	theme	beta	1363:1366	arg1	subunit					1368:1374	the beta subunit	1359:1374	the beta subunit (beta 64N, beta 127N, and beta 147N)	1359:1411	A total of six N-linked glycosylation sites were identified, three in the alpha subunit (alpha 64N, alpha 81N, alpha 123N) and three in the beta subunit (beta 64N, beta 127N, and beta 147N).
9336835	1	98	theme	possible	153:160	arg1	functions					162:170	multiple possible functions	144:170	multiple possible functions that are likely influenced by glycosylation	144:214	Clusterin is a ubiquitous, heterodimeric glycoprotein with multiple possible functions that are likely influenced by glycosylation.
9336835	5	99	theme	%	838:838	arg1	carbohydrate					840:851	0-30% carbohydrate	834:851	0-30% carbohydrate	834:851	The data indicate that clusterin contains 17-27% carbohydrate by weight, the alpha subunit contains 0-30% carbohydrate and the beta subunit contains 27-30% carbohydrate.
9336835	6	100	used	used	1000:1003	arg2	spectrometry					944:955	Liquid chromatography electrospray mass spectrometry	904:955	Liquid chromatography electrospray mass spectrometry with stepped collision energy scanning	904:994	Liquid chromatography electrospray mass spectrometry with stepped collision energy scanning was used to selectively identify and preparatively fractionate tryptic glycopeptides.
9336835	7	101	theme	sequence	1088:1095	arg1	analysis					1097:1104	Edman sequence analysis	1082:1104	Edman sequence analysis	1082:1104	Edman sequence analysis was then used to confirm the identities of the glycopeptides and to define the attachment sites within each peptide.
9336835	3	102	theme	desorption	430:439	arg1	spectrometry					457:468	Matrix-assisted laser desorption ionization mass spectrometry	408:468	Matrix-assisted laser desorption ionization mass spectrometry	408:468	Matrix-assisted laser desorption ionization mass spectrometry revealed two molecular weight species of holoclusterin (58,505 +/- 250 and 63,507 +/- 200).
9336835	3	103	dep	revealed	470:477	arg1	250					537:539	250	537:539	250	537:539	Matrix-assisted laser desorption ionization mass spectrometry revealed two molecular weight species of holoclusterin (58,505 +/- 250 and 63,507 +/- 200).
9336835	3	103	dep	revealed	470:477	arg1	58,505					526:531	58,505	526:531	58,505	526:531	Matrix-assisted laser desorption ionization mass spectrometry revealed two molecular weight species of holoclusterin (58,505 +/- 250 and 63,507 +/- 200).
9336835	3	103	dep	revealed	470:477	arg1	63,507					545:550	63,507	545:550	63,507	545:550	Matrix-assisted laser desorption ionization mass spectrometry revealed two molecular weight species of holoclusterin (58,505 +/- 250 and 63,507 +/- 200).
9336835	8	104	theme	beta	1387:1390	arg1	127N					1392:1395	beta 127N	1387:1395	beta 127N	1387:1395	A total of six N-linked glycosylation sites were identified, three in the alpha subunit (alpha 64N, alpha 81N, alpha 123N) and three in the beta subunit (beta 64N, beta 127N, and beta 147N).
9336835	5	105	theme	alpha	811:815	arg1	subunit					817:823	the alpha subunit	807:823	the alpha subunit	807:823	The data indicate that clusterin contains 17-27% carbohydrate by weight, the alpha subunit contains 0-30% carbohydrate and the beta subunit contains 27-30% carbohydrate.
9336835	6	106	with	spectrometry	944:955	arg1	scanning					987:994	stepped collision energy scanning	962:994	stepped collision energy scanning	962:994	Liquid chromatography electrospray mass spectrometry with stepped collision energy scanning was used to selectively identify and preparatively fractionate tryptic glycopeptides.
9336835	3	107	theme	Matrix-assisted	408:422	arg1	spectrometry					457:468	Matrix-assisted laser desorption ionization mass spectrometry	408:468	Matrix-assisted laser desorption ionization mass spectrometry	408:468	Matrix-assisted laser desorption ionization mass spectrometry revealed two molecular weight species of holoclusterin (58,505 +/- 250 and 63,507 +/- 200).
9336835	8	108	theme	beta	1402:1405	arg1	147N					1407:1410	beta 147N	1402:1410	beta 147N	1402:1410	A total of six N-linked glycosylation sites were identified, three in the alpha subunit (alpha 64N, alpha 81N, alpha 123N) and three in the beta subunit (beta 64N, beta 127N, and beta 147N).
9336835	3	109	theme	holoclusterin	511:523	arg1	species					500:506	two molecular weight species	479:506	two molecular weight species of holoclusterin	479:523	Matrix-assisted laser desorption ionization mass spectrometry revealed two molecular weight species of holoclusterin (58,505 +/- 250 and 63,507 +/- 200).
9336835	5	110	theme	%	888:888	arg1	carbohydrate					890:901	27-30% carbohydrate	883:901	27-30% carbohydrate	883:901	The data indicate that clusterin contains 17-27% carbohydrate by weight, the alpha subunit contains 0-30% carbohydrate and the beta subunit contains 27-30% carbohydrate.
9336835	1	111	theme	ubiquitous	100:109	arg1	Clusterin					85:93	Clusterin	85:93	Clusterin	85:93	Clusterin is a ubiquitous, heterodimeric glycoprotein with multiple possible functions that are likely influenced by glycosylation.
9336835	1	111	theme	ubiquitous	100:109	arg1	glycoprotein					126:137	a ubiquitous, heterodimeric glycoprotein	98:137	a ubiquitous, heterodimeric glycoprotein with multiple possible functions that are likely influenced by glycosylation	98:214	Clusterin is a ubiquitous, heterodimeric glycoprotein with multiple possible functions that are likely influenced by glycosylation.
9336835	2	112	from	characterization	283:298	arg1	clusterin					335:343	human serum clusterin	323:343	human serum clusterin	323:343	Identification of oligosaccharide attachment sites and structural characterization of oligosaccharides in human serum clusterin has been performed by mass spectrometry and Edman degradation.
9336835	3	113	theme	mass	452:455	arg1	spectrometry					457:468	Matrix-assisted laser desorption ionization mass spectrometry	408:468	Matrix-assisted laser desorption ionization mass spectrometry	408:468	Matrix-assisted laser desorption ionization mass spectrometry revealed two molecular weight species of holoclusterin (58,505 +/- 250 and 63,507 +/- 200).
9336835	10	114	theme	detected	1941:1948	arg1	types					1950:1954	five or six detected types	1929:1954	five or six detected types of oligosaccharides	1929:1974	Site beta 64N exhibited the least glycosylation diversity, with two detected types of oligosaccharides, and site beta 147N exhibited the greatest diversity, with five or six detected types of oligosaccharides.
9336835	10	115	theme	Site	1767:1770	arg1	64N					1777:1779	Site beta 64N	1767:1779	Site beta 64N	1767:1779	Site beta 64N exhibited the least glycosylation diversity, with two detected types of oligosaccharides, and site beta 147N exhibited the greatest diversity, with five or six detected types of oligosaccharides.
9336835	0	116	theme	sites	53:57	arg1	characterization					19:34	characterization	19:34	characterization	19:34	Identification and characterization of glycosylation sites in human serum clusterin.
9336835	0	116	theme	sites	53:57	arg1	Identification					0:13	Identification	0:13	Identification	0:13	Identification and characterization of glycosylation sites in human serum clusterin.
9336835	12	117	theme	beta	2300:2303	arg1	subunits					2305:2312	the isolated alpha and beta subunits	2277:2312	the isolated alpha and beta subunits	2277:2312	Clusterin peptides accounting for 99% of the primary structure were identified from analysis of the isolated alpha and beta subunits, including all Ser- and Thr-containing peptides.
9336835	5	118	theme	beta	861:864	arg1	subunit					866:872	the beta subunit	857:872	the beta subunit	857:872	The data indicate that clusterin contains 17-27% carbohydrate by weight, the alpha subunit contains 0-30% carbohydrate and the beta subunit contains 27-30% carbohydrate.
9336835	6	119	theme	mass	939:942	arg1	spectrometry					944:955	Liquid chromatography electrospray mass spectrometry	904:955	Liquid chromatography electrospray mass spectrometry with stepped collision energy scanning	904:994	Liquid chromatography electrospray mass spectrometry with stepped collision energy scanning was used to selectively identify and preparatively fractionate tryptic glycopeptides.
9336835	3	120	theme	molecular	483:491	arg1	species					500:506	two molecular weight species	479:506	two molecular weight species of holoclusterin	479:523	Matrix-assisted laser desorption ionization mass spectrometry revealed two molecular weight species of holoclusterin (58,505 +/- 250 and 63,507 +/- 200).
9336835	2	121	theme	oligosaccharide	235:249	arg1	sites					262:266	oligosaccharide attachment sites	235:266	oligosaccharide attachment sites	235:266	Identification of oligosaccharide attachment sites and structural characterization of oligosaccharides in human serum clusterin has been performed by mass spectrometry and Edman degradation.
9336835	8	122	gly	glycosylation	1247:1259	arg2	six					1234:1236	six	1234:1236	six	1234:1236	A total of six N-linked glycosylation sites were identified, three in the alpha subunit (alpha 64N, alpha 81N, alpha 123N) and three in the beta subunit (beta 64N, beta 127N, and beta 147N).
9336835	8	122	gly	glycosylation	1247:1259	arg2	sites					1261:1265	six N-linked glycosylation sites	1234:1265	six N-linked glycosylation sites	1234:1265	A total of six N-linked glycosylation sites were identified, three in the alpha subunit (alpha 64N, alpha 81N, alpha 123N) and three in the beta subunit (beta 64N, beta 127N, and beta 147N).
9336835	2	123	theme	Edman	389:393	arg1	degradation					395:405	Edman degradation	389:405	Edman degradation	389:405	Identification of oligosaccharide attachment sites and structural characterization of oligosaccharides in human serum clusterin has been performed by mass spectrometry and Edman degradation.
9336835	6	124	theme	chromatography	911:924	arg1	spectrometry					944:955	Liquid chromatography electrospray mass spectrometry	904:955	Liquid chromatography electrospray mass spectrometry with stepped collision energy scanning	904:994	Liquid chromatography electrospray mass spectrometry with stepped collision energy scanning was used to selectively identify and preparatively fractionate tryptic glycopeptides.
9336835	8	125	dep	subunit	1368:1374	arg1	147N					1407:1410	beta 147N	1402:1410	beta 147N	1402:1410	A total of six N-linked glycosylation sites were identified, three in the alpha subunit (alpha 64N, alpha 81N, alpha 123N) and three in the beta subunit (beta 64N, beta 127N, and beta 147N).
9336835	8	125	dep	subunit	1368:1374	arg1	64N					1382:1384	beta 64N	1377:1384	beta 64N	1377:1384	A total of six N-linked glycosylation sites were identified, three in the alpha subunit (alpha 64N, alpha 81N, alpha 123N) and three in the beta subunit (beta 64N, beta 127N, and beta 147N).
9336835	8	125	dep	subunit	1368:1374	arg1	127N					1392:1395	beta 127N	1387:1395	beta 127N	1387:1395	A total of six N-linked glycosylation sites were identified, three in the alpha subunit (alpha 64N, alpha 81N, alpha 123N) and three in the beta subunit (beta 64N, beta 127N, and beta 147N).
9336835	9	126	theme	different	1420:1428	arg1	types					1439:1443	Seven different possible types	1414:1443	Seven different possible types of oligosaccharide structures	1414:1473	Seven different possible types of oligosaccharide structures were identified by mass including: a monosialobiantennary structure, bisialobiantennary structures without or with one fucose, trisialotriantennary structures without or with one fucose, and possibly a trisialotriantennary structure with two fucose and/or a tetrasialotriantennary structure.
9336835	8	127	theme	N-linked	1238:1245	arg1	sites					1261:1265	six N-linked glycosylation sites	1234:1265	six N-linked glycosylation sites	1234:1265	A total of six N-linked glycosylation sites were identified, three in the alpha subunit (alpha 64N, alpha 81N, alpha 123N) and three in the beta subunit (beta 64N, beta 127N, and beta 147N).
9336835	12	128	theme	structure	2234:2242	arg1	structure					2234:2242	the primary structure	2222:2242	the primary structure	2222:2242	Clusterin peptides accounting for 99% of the primary structure were identified from analysis of the isolated alpha and beta subunits, including all Ser- and Thr-containing peptides.
9336835	12	128	theme	structure	2234:2242	arg1	%					2217:2217	99%	2215:2217	99% of the primary structure	2215:2242	Clusterin peptides accounting for 99% of the primary structure were identified from analysis of the isolated alpha and beta subunits, including all Ser- and Thr-containing peptides.
9336835	12	129	theme	alpha	2290:2294	arg1	subunits					2305:2312	the isolated alpha and beta subunits	2277:2312	the isolated alpha and beta subunits	2277:2312	Clusterin peptides accounting for 99% of the primary structure were identified from analysis of the isolated alpha and beta subunits, including all Ser- and Thr-containing peptides.
9336835	14	130	theme	relationships	2552:2564	arg1	understanding					2506:2518	a better understanding	2497:2518	a better understanding of clusterin structure-function relationships	2497:2564	The results provide a molecular basis for developing a better understanding of clusterin structure-function relationships and the role clusterin glycosylation plays in physiological function.
9336835	14	130	theme	relationships	2552:2564	arg1	role					2574:2577	the role	2570:2577	the role clusterin glycosylation plays in physiological function	2570:2633	The results provide a molecular basis for developing a better understanding of clusterin structure-function relationships and the role clusterin glycosylation plays in physiological function.
20587416	12	0	theme	surface	1857:1863	arg1	ARs					1872:1874	cell surface beta(1)ARs	1852:1874	cell surface beta(1)ARs	1852:1874	We hypothesize that the N-terminal cleavage represents a novel regulatory mechanism of cell surface beta(1)ARs.
20587416	5	1	theme	mucin-type	791:800	arg1	O-glycosylation					802:816	sialylated mucin-type O-glycosylation	780:816	sialylated mucin-type O-glycosylation in addition to one N-glycan attached to Asn(15)	780:864	The N terminus of the mature receptor is extensively modified by sialylated mucin-type O-glycosylation in addition to one N-glycan attached to Asn(15).
20587416	3	2	theme	relevant	450:457	arg1	features					441:448	novel features	435:448	novel features relevant to its regulation using an inducible heterologous expression system in HEK293(i) cells	435:544	We describe here the biosynthetic profile of the human beta(1)AR and reveal novel features relevant to its regulation using an inducible heterologous expression system in HEK293(i) cells.
20587416	1	3	theme	catecholamine-stimulated	192:215	arg1	increase					217:224	the catecholamine-stimulated increase	188:224	the catecholamine-stimulated increase in cardiac rate and force of contraction	188:265	The beta(1)-adrenergic receptor (beta(1)AR) is the predominant betaAR in the heart, mediating the catecholamine-stimulated increase in cardiac rate and force of contraction.
20587416	2	4	theme	receptor	315:322	arg1	Regulation					268:277	Regulation	268:277	Regulation of this important G protein-coupled receptor	268:322	Regulation of this important G protein-coupled receptor is nevertheless poorly understood.
20587416	5	5	gly	sialylated	780:789	arg1	O-glycosylation					802:816	sialylated mucin-type O-glycosylation	780:816	sialylated mucin-type O-glycosylation in addition to one N-glycan attached to Asn(15)	780:864	The N terminus of the mature receptor is extensively modified by sialylated mucin-type O-glycosylation in addition to one N-glycan attached to Asn(15).
20587416	3	6	theme	inducible	486:494	arg1	system					520:525	an inducible heterologous expression system	483:525	an inducible heterologous expression system in HEK293(i) cells	483:544	We describe here the biosynthetic profile of the human beta(1)AR and reveal novel features relevant to its regulation using an inducible heterologous expression system in HEK293(i) cells.
20587416	6	7	theme	limited	922:928	arg1	proteolysis					930:940	limited proteolysis	922:940	limited proteolysis	922:940	Furthermore, the N terminus was found to be subject to limited proteolysis, resulting in two membrane-bound C-terminal fragments.
20587416	10	8	theme	kinase	1656:1661	arg1	C					1663:1663	protein kinase C	1648:1663	protein kinase C	1648:1663	Receptor activation mediated by the betaAR agonist isoproterenol enhanced the cleavage in a concentration- and time-dependent manner, and it was also enhanced by direct stimulation of protein kinase C and adenylyl cyclase.
20587416	9	9	dep	in	1437:1438	arg1	vitro					1440:1444	vitro	1440:1444	vitro	1440:1444	Most importantly, the N-terminal cleavage was found to occur not only in vitro but also in vivo.
20587416	3	10	theme	heterologous	496:507	arg1	system					520:525	an inducible heterologous expression system	483:525	an inducible heterologous expression system in HEK293(i) cells	483:544	We describe here the biosynthetic profile of the human beta(1)AR and reveal novel features relevant to its regulation using an inducible heterologous expression system in HEK293(i) cells.
20587416	1	11	theme	cardiac	229:235	arg1	rate					237:240	cardiac rate	229:240	cardiac rate	229:240	The beta(1)-adrenergic receptor (beta(1)AR) is the predominant betaAR in the heart, mediating the catecholamine-stimulated increase in cardiac rate and force of contraction.
20587416	12	12	theme	cell	1852:1855	arg1	ARs					1872:1874	cell surface beta(1)ARs	1852:1874	cell surface beta(1)ARs	1852:1874	We hypothesize that the N-terminal cleavage represents a novel regulatory mechanism of cell surface beta(1)ARs.
20587416	3	13	theme	novel	435:439	arg1	features					441:448	novel features	435:448	novel features relevant to its regulation using an inducible heterologous expression system in HEK293(i) cells	435:544	We describe here the biosynthetic profile of the human beta(1)AR and reveal novel features relevant to its regulation using an inducible heterologous expression system in HEK293(i) cells.
20587416	7	14	theme	cleavage	1051:1058	arg1	sites					1060:1064	two cleavage sites	1047:1064	two cleavage sites	1047:1064	N-terminal sequencing of the fragments identified two cleavage sites between Arg(31) and Leu(32) and Pro(52) and Leu(53), which were confirmed by cleavage site and truncation mutants.
20587416	6	15	theme	membrane-bound	960:973	arg1	fragments					986:994	two membrane-bound C-terminal fragments	956:994	two membrane-bound C-terminal fragments	956:994	Furthermore, the N terminus was found to be subject to limited proteolysis, resulting in two membrane-bound C-terminal fragments.
20587416	11	16	theme	cleavage	1719:1726	arg1	site					1728:1731	the Arg(31)-Leu(32) cleavage site	1699:1731	the Arg(31)-Leu(32) cleavage site	1699:1731	Mutation of the Arg(31)-Leu(32) cleavage site stabilized the mature receptor.
20587416	3	17	theme	human	408:412	arg1	AR					421:422	the human beta(1)AR	404:422	the human beta(1)AR	404:422	We describe here the biosynthetic profile of the human beta(1)AR and reveal novel features relevant to its regulation using an inducible heterologous expression system in HEK293(i) cells.
20587416	12	18	theme	ARs	1872:1874	arg1	mechanism					1839:1847	a novel regulatory mechanism	1820:1847	a novel regulatory mechanism of cell surface beta(1)ARs	1820:1874	We hypothesize that the N-terminal cleavage represents a novel regulatory mechanism of cell surface beta(1)ARs.
20587416	8	19	theme	ADAM	1346:1349	arg1	member					1359:1364	a disintegrin and metalloproteinase (ADAM) family member	1309:1364	a disintegrin and metalloproteinase (ADAM) family member	1309:1364	Metalloproteinase inhibitors were able to inhibit the cleavage, suggesting that it is mediated by a matrix metalloproteinase or a disintegrin and metalloproteinase (ADAM) family member.
20587416	9	20	theme	N-terminal	1389:1398	arg1	cleavage					1400:1407	the N-terminal cleavage	1385:1407	the N-terminal cleavage	1385:1407	Most importantly, the N-terminal cleavage was found to occur not only in vitro but also in vivo.
20587416	10	21	theme	concentration-	1556:1569	arg1	manner					1590:1595	a concentration- and time-dependent manner	1554:1595	a concentration- and time-dependent manner	1554:1595	Receptor activation mediated by the betaAR agonist isoproterenol enhanced the cleavage in a concentration- and time-dependent manner, and it was also enhanced by direct stimulation of protein kinase C and adenylyl cyclase.
20587416	3	22	theme	beta	414:417	arg1	AR					421:422	the human beta(1)AR	404:422	the human beta(1)AR	404:422	We describe here the biosynthetic profile of the human beta(1)AR and reveal novel features relevant to its regulation using an inducible heterologous expression system in HEK293(i) cells.
20587416	0	23	theme	beta1-adrenergic	6:21	arg1	receptor					23:30	Human beta1-adrenergic receptor	0:30	Human beta1-adrenergic receptor	0:30	Human beta1-adrenergic receptor is subject to constitutive and regulated N-terminal cleavage.
20587416	11	24	theme	Arg	1703:1705	arg1	site					1728:1731	the Arg(31)-Leu(32) cleavage site	1699:1731	the Arg(31)-Leu(32) cleavage site	1699:1731	Mutation of the Arg(31)-Leu(32) cleavage site stabilized the mature receptor.
20587416	10	25	theme	protein	1648:1654	arg1	C					1663:1663	protein kinase C	1648:1663	protein kinase C	1648:1663	Receptor activation mediated by the betaAR agonist isoproterenol enhanced the cleavage in a concentration- and time-dependent manner, and it was also enhanced by direct stimulation of protein kinase C and adenylyl cyclase.
20587416	4	26	theme	cell	701:704	arg1	surface					706:712	the cell surface	697:712	the cell surface	697:712	Metabolic pulse-chase labeling and cell surface biotinylation assays showed that the synthesized receptors are efficiently and rapidly transported to the cell surface.
20587416	11	27	theme	mature	1748:1753	arg1	receptor					1755:1762	the mature receptor	1744:1762	the mature receptor	1744:1762	Mutation of the Arg(31)-Leu(32) cleavage site stabilized the mature receptor.
20587416	10	28	theme	agonist	1507:1513	arg1	isoproterenol					1515:1527	the betaAR agonist isoproterenol	1496:1527	the betaAR agonist isoproterenol	1496:1527	Receptor activation mediated by the betaAR agonist isoproterenol enhanced the cleavage in a concentration- and time-dependent manner, and it was also enhanced by direct stimulation of protein kinase C and adenylyl cyclase.
20587416	0	29	theme	Human	0:4	arg1	receptor					23:30	Human beta1-adrenergic receptor	0:30	Human beta1-adrenergic receptor	0:30	Human beta1-adrenergic receptor is subject to constitutive and regulated N-terminal cleavage.
20587416	3	30	theme	HEK293	530:535	arg1	cells					540:544	HEK293(i) cells	530:544	HEK293(i) cells	530:544	We describe here the biosynthetic profile of the human beta(1)AR and reveal novel features relevant to its regulation using an inducible heterologous expression system in HEK293(i) cells.
20587416	10	31	theme	betaAR	1500:1505	arg1	isoproterenol					1515:1527	the betaAR agonist isoproterenol	1496:1527	the betaAR agonist isoproterenol	1496:1527	Receptor activation mediated by the betaAR agonist isoproterenol enhanced the cleavage in a concentration- and time-dependent manner, and it was also enhanced by direct stimulation of protein kinase C and adenylyl cyclase.
20587416	5	32	mod	modified	768:775	arg3	O-glycosylation					802:816	sialylated mucin-type O-glycosylation	780:816	sialylated mucin-type O-glycosylation in addition to one N-glycan attached to Asn(15)	780:864	The N terminus of the mature receptor is extensively modified by sialylated mucin-type O-glycosylation in addition to one N-glycan attached to Asn(15).
20587416	5	32	mod	modified	768:775	arg1	terminus					721:728	The N terminus	715:728	The N terminus of the mature receptor	715:751	The N terminus of the mature receptor is extensively modified by sialylated mucin-type O-glycosylation in addition to one N-glycan attached to Asn(15).
20587416	12	33	theme	novel	1822:1826	arg1	mechanism					1839:1847	a novel regulatory mechanism	1820:1847	a novel regulatory mechanism of cell surface beta(1)ARs	1820:1874	We hypothesize that the N-terminal cleavage represents a novel regulatory mechanism of cell surface beta(1)ARs.
20587416	3	34	theme	expression	509:518	arg1	system					520:525	an inducible heterologous expression system	483:525	an inducible heterologous expression system in HEK293(i) cells	483:544	We describe here the biosynthetic profile of the human beta(1)AR and reveal novel features relevant to its regulation using an inducible heterologous expression system in HEK293(i) cells.
20587416	8	35	theme	matrix	1281:1286	arg1	metalloproteinase					1288:1304	a matrix metalloproteinase	1279:1304	a matrix metalloproteinase	1279:1304	Metalloproteinase inhibitors were able to inhibit the cleavage, suggesting that it is mediated by a matrix metalloproteinase or a disintegrin and metalloproteinase (ADAM) family member.
20587416	1	36	theme	predominant	145:155	arg1	receptor					117:124	The beta(1)-adrenergic receptor	94:124	The beta(1)-adrenergic receptor (beta(1)AR)	94:136	The beta(1)-adrenergic receptor (beta(1)AR) is the predominant betaAR in the heart, mediating the catecholamine-stimulated increase in cardiac rate and force of contraction.
20587416	1	36	theme	predominant	145:155	arg1	betaAR					157:162	the predominant betaAR	141:162	the predominant betaAR in the heart	141:175	The beta(1)-adrenergic receptor (beta(1)AR) is the predominant betaAR in the heart, mediating the catecholamine-stimulated increase in cardiac rate and force of contraction.
20587416	5	37	theme	sialylated	780:789	arg1	O-glycosylation					802:816	sialylated mucin-type O-glycosylation	780:816	sialylated mucin-type O-glycosylation in addition to one N-glycan attached to Asn(15)	780:864	The N terminus of the mature receptor is extensively modified by sialylated mucin-type O-glycosylation in addition to one N-glycan attached to Asn(15).
20587416	7	38	theme	fragments	1026:1034	arg1	sequencing					1008:1017	N-terminal sequencing	997:1017	N-terminal sequencing of the fragments	997:1034	N-terminal sequencing of the fragments identified two cleavage sites between Arg(31) and Leu(32) and Pro(52) and Leu(53), which were confirmed by cleavage site and truncation mutants.
20587416	8	39	theme	metalloproteinase	1327:1343	arg1	ADAM					1346:1349	metalloproteinase (ADAM)	1327:1350	metalloproteinase (ADAM)	1327:1350	Metalloproteinase inhibitors were able to inhibit the cleavage, suggesting that it is mediated by a matrix metalloproteinase or a disintegrin and metalloproteinase (ADAM) family member.
20587416	12	40	theme	regulatory	1828:1837	arg1	mechanism					1839:1847	a novel regulatory mechanism	1820:1847	a novel regulatory mechanism of cell surface beta(1)ARs	1820:1874	We hypothesize that the N-terminal cleavage represents a novel regulatory mechanism of cell surface beta(1)ARs.
20587416	3	41	theme	AR	421:422	arg1	profile					393:399	the biosynthetic profile	376:399	the biosynthetic profile of the human beta(1)AR	376:422	We describe here the biosynthetic profile of the human beta(1)AR and reveal novel features relevant to its regulation using an inducible heterologous expression system in HEK293(i) cells.
20587416	3	42	theme	biosynthetic	380:391	arg1	profile					393:399	the biosynthetic profile	376:399	the biosynthetic profile of the human beta(1)AR	376:422	We describe here the biosynthetic profile of the human beta(1)AR and reveal novel features relevant to its regulation using an inducible heterologous expression system in HEK293(i) cells.
20587416	10	43	theme	time-dependent	1575:1588	arg1	manner					1590:1595	a concentration- and time-dependent manner	1554:1595	a concentration- and time-dependent manner	1554:1595	Receptor activation mediated by the betaAR agonist isoproterenol enhanced the cleavage in a concentration- and time-dependent manner, and it was also enhanced by direct stimulation of protein kinase C and adenylyl cyclase.
20587416	7	44	theme	truncation	1161:1170	arg1	mutants					1172:1178	truncation mutants	1161:1178	truncation mutants	1161:1178	N-terminal sequencing of the fragments identified two cleavage sites between Arg(31) and Leu(32) and Pro(52) and Leu(53), which were confirmed by cleavage site and truncation mutants.
20587416	10	45	theme	cyclase	1678:1684	arg1	stimulation					1633:1643	direct stimulation	1626:1643	direct stimulation of protein kinase C and adenylyl cyclase	1626:1684	Receptor activation mediated by the betaAR agonist isoproterenol enhanced the cleavage in a concentration- and time-dependent manner, and it was also enhanced by direct stimulation of protein kinase C and adenylyl cyclase.
20587416	11	46	theme	site	1728:1731	arg1	Mutation					1687:1694	Mutation	1687:1694	Mutation of the Arg(31)-Leu(32) cleavage site	1687:1731	Mutation of the Arg(31)-Leu(32) cleavage site stabilized the mature receptor.
20587416	4	47	theme	biotinylation	595:607	arg1	assays					609:614	cell surface biotinylation assays	582:614	cell surface biotinylation assays	582:614	Metabolic pulse-chase labeling and cell surface biotinylation assays showed that the synthesized receptors are efficiently and rapidly transported to the cell surface.
20587416	5	48	theme	mature	737:742	arg1	receptor					744:751	the mature receptor	733:751	the mature receptor	733:751	The N terminus of the mature receptor is extensively modified by sialylated mucin-type O-glycosylation in addition to one N-glycan attached to Asn(15).
20587416	1	49	theme	contraction	255:265	arg1	force					246:250	force	246:250	force	246:250	The beta(1)-adrenergic receptor (beta(1)AR) is the predominant betaAR in the heart, mediating the catecholamine-stimulated increase in cardiac rate and force of contraction.
20587416	1	49	theme	contraction	255:265	arg1	rate					237:240	cardiac rate	229:240	cardiac rate	229:240	The beta(1)-adrenergic receptor (beta(1)AR) is the predominant betaAR in the heart, mediating the catecholamine-stimulated increase in cardiac rate and force of contraction.
20587416	1	50	from	increase	217:224	arg1	force					246:250	force	246:250	force	246:250	The beta(1)-adrenergic receptor (beta(1)AR) is the predominant betaAR in the heart, mediating the catecholamine-stimulated increase in cardiac rate and force of contraction.
20587416	1	50	from	increase	217:224	arg1	rate					237:240	cardiac rate	229:240	cardiac rate	229:240	The beta(1)-adrenergic receptor (beta(1)AR) is the predominant betaAR in the heart, mediating the catecholamine-stimulated increase in cardiac rate and force of contraction.
20587416	5	51	attach	attached	846:853	arg1	15					862:863	15	862:863	15	862:863	The N terminus of the mature receptor is extensively modified by sialylated mucin-type O-glycosylation in addition to one N-glycan attached to Asn(15).
20587416	5	51	attach	attached	846:853	arg2	N-glycan					837:844	one N-glycan	833:844	one N-glycan attached to Asn(15)	833:864	The N terminus of the mature receptor is extensively modified by sialylated mucin-type O-glycosylation in addition to one N-glycan attached to Asn(15).
20587416	5	51	attach	attached	846:853	arg1	Asn					858:860	Asn	858:860	Asn(15)	858:864	The N terminus of the mature receptor is extensively modified by sialylated mucin-type O-glycosylation in addition to one N-glycan attached to Asn(15).
20587416	10	52	theme	adenylyl	1669:1676	arg1	cyclase					1678:1684	adenylyl cyclase	1669:1684	adenylyl cyclase	1669:1684	Receptor activation mediated by the betaAR agonist isoproterenol enhanced the cleavage in a concentration- and time-dependent manner, and it was also enhanced by direct stimulation of protein kinase C and adenylyl cyclase.
20587416	4	53	theme	surface	587:593	arg1	assays					609:614	cell surface biotinylation assays	582:614	cell surface biotinylation assays	582:614	Metabolic pulse-chase labeling and cell surface biotinylation assays showed that the synthesized receptors are efficiently and rapidly transported to the cell surface.
20587416	5	54	theme	receptor	744:751	arg1	terminus					721:728	The N terminus	715:728	The N terminus of the mature receptor	715:751	The N terminus of the mature receptor is extensively modified by sialylated mucin-type O-glycosylation in addition to one N-glycan attached to Asn(15).
20587416	5	55	theme	N	719:719	arg1	terminus					721:728	The N terminus	715:728	The N terminus of the mature receptor	715:751	The N terminus of the mature receptor is extensively modified by sialylated mucin-type O-glycosylation in addition to one N-glycan attached to Asn(15).
20587416	1	56	dep	AR	134:135	arg1	1					132:132	1	132:132	1	132:132	The beta(1)-adrenergic receptor (beta(1)AR) is the predominant betaAR in the heart, mediating the catecholamine-stimulated increase in cardiac rate and force of contraction.
20587416	2	57	theme	protein-coupled	299:313	arg1	receptor					315:322	this important G protein-coupled receptor	282:322	this important G protein-coupled receptor	282:322	Regulation of this important G protein-coupled receptor is nevertheless poorly understood.
20587416	0	58	theme	constitutive	46:57	arg1	cleavage					84:91	constitutive and regulated N-terminal cleavage	46:91	constitutive and regulated N-terminal cleavage	46:91	Human beta1-adrenergic receptor is subject to constitutive and regulated N-terminal cleavage.
20587416	6	59	theme	N	884:884	arg1	terminus					886:893	the N terminus	880:893	the N terminus	880:893	Furthermore, the N terminus was found to be subject to limited proteolysis, resulting in two membrane-bound C-terminal fragments.
20587416	6	59	theme	N	884:884	arg1	subject					911:917	subject	911:917	subject	911:917	Furthermore, the N terminus was found to be subject to limited proteolysis, resulting in two membrane-bound C-terminal fragments.
20587416	7	60	theme	N-terminal	997:1006	arg1	sequencing					1008:1017	N-terminal sequencing	997:1017	N-terminal sequencing of the fragments	997:1034	N-terminal sequencing of the fragments identified two cleavage sites between Arg(31) and Leu(32) and Pro(52) and Leu(53), which were confirmed by cleavage site and truncation mutants.
20587416	8	61	theme	family	1352:1357	arg1	member					1359:1364	a disintegrin and metalloproteinase (ADAM) family member	1309:1364	a disintegrin and metalloproteinase (ADAM) family member	1309:1364	Metalloproteinase inhibitors were able to inhibit the cleavage, suggesting that it is mediated by a matrix metalloproteinase or a disintegrin and metalloproteinase (ADAM) family member.
20587416	10	62	theme	C	1663:1663	arg1	stimulation					1633:1643	direct stimulation	1626:1643	direct stimulation of protein kinase C and adenylyl cyclase	1626:1684	Receptor activation mediated by the betaAR agonist isoproterenol enhanced the cleavage in a concentration- and time-dependent manner, and it was also enhanced by direct stimulation of protein kinase C and adenylyl cyclase.
20587416	1	63	theme	-adrenergic	105:115	arg1	receptor					117:124	The beta(1)-adrenergic receptor	94:124	The beta(1)-adrenergic receptor (beta(1)AR)	94:136	The beta(1)-adrenergic receptor (beta(1)AR) is the predominant betaAR in the heart, mediating the catecholamine-stimulated increase in cardiac rate and force of contraction.
20587416	1	63	theme	-adrenergic	105:115	arg1	betaAR					157:162	the predominant betaAR	141:162	the predominant betaAR in the heart	141:175	The beta(1)-adrenergic receptor (beta(1)AR) is the predominant betaAR in the heart, mediating the catecholamine-stimulated increase in cardiac rate and force of contraction.
20587416	1	63	theme	-adrenergic	105:115	arg1	AR					134:135	beta(1)AR	127:135	beta(1)AR	127:135	The beta(1)-adrenergic receptor (beta(1)AR) is the predominant betaAR in the heart, mediating the catecholamine-stimulated increase in cardiac rate and force of contraction.
20587416	12	64	theme	N-terminal	1789:1798	arg1	cleavage					1800:1807	the N-terminal cleavage	1785:1807	the N-terminal cleavage	1785:1807	We hypothesize that the N-terminal cleavage represents a novel regulatory mechanism of cell surface beta(1)ARs.
20587416	11	65	theme	-Leu	1710:1713	arg1	site					1728:1731	the Arg(31)-Leu(32) cleavage site	1699:1731	the Arg(31)-Leu(32) cleavage site	1699:1731	Mutation of the Arg(31)-Leu(32) cleavage site stabilized the mature receptor.
20587416	1	66	from	betaAR	157:162	arg1	heart					171:175	the heart	167:175	the heart	167:175	The beta(1)-adrenergic receptor (beta(1)AR) is the predominant betaAR in the heart, mediating the catecholamine-stimulated increase in cardiac rate and force of contraction.
20587416	2	67	theme	important	287:295	arg1	receptor					315:322	this important G protein-coupled receptor	282:322	this important G protein-coupled receptor	282:322	Regulation of this important G protein-coupled receptor is nevertheless poorly understood.
20587416	3	68	from	system	520:525	arg1	cells					540:544	HEK293(i) cells	530:544	HEK293(i) cells	530:544	We describe here the biosynthetic profile of the human beta(1)AR and reveal novel features relevant to its regulation using an inducible heterologous expression system in HEK293(i) cells.
20587416	4	69	theme	Metabolic	547:555	arg1	labeling					569:576	Metabolic pulse-chase labeling	547:576	Metabolic pulse-chase labeling	547:576	Metabolic pulse-chase labeling and cell surface biotinylation assays showed that the synthesized receptors are efficiently and rapidly transported to the cell surface.
20587416	10	70	theme	direct	1626:1631	arg1	stimulation					1633:1643	direct stimulation	1626:1643	direct stimulation of protein kinase C and adenylyl cyclase	1626:1684	Receptor activation mediated by the betaAR agonist isoproterenol enhanced the cleavage in a concentration- and time-dependent manner, and it was also enhanced by direct stimulation of protein kinase C and adenylyl cyclase.
20587416	7	71	theme	cleavage	1143:1150	arg1	site					1152:1155	cleavage site	1143:1155	cleavage site	1143:1155	N-terminal sequencing of the fragments identified two cleavage sites between Arg(31) and Leu(32) and Pro(52) and Leu(53), which were confirmed by cleavage site and truncation mutants.
20587416	12	72	theme	beta	1865:1868	arg1	ARs					1872:1874	cell surface beta(1)ARs	1852:1874	cell surface beta(1)ARs	1852:1874	We hypothesize that the N-terminal cleavage represents a novel regulatory mechanism of cell surface beta(1)ARs.
20587416	8	73	theme	Metalloproteinase	1181:1197	arg1	inhibitors					1199:1208	Metalloproteinase inhibitors	1181:1208	Metalloproteinase inhibitors	1181:1208	Metalloproteinase inhibitors were able to inhibit the cleavage, suggesting that it is mediated by a matrix metalloproteinase or a disintegrin and metalloproteinase (ADAM) family member.
20587416	0	74	theme	N-terminal	73:82	arg1	cleavage					84:91	constitutive and regulated N-terminal cleavage	46:91	constitutive and regulated N-terminal cleavage	46:91	Human beta1-adrenergic receptor is subject to constitutive and regulated N-terminal cleavage.
20587416	6	75	theme	C-terminal	975:984	arg1	fragments					986:994	two membrane-bound C-terminal fragments	956:994	two membrane-bound C-terminal fragments	956:994	Furthermore, the N terminus was found to be subject to limited proteolysis, resulting in two membrane-bound C-terminal fragments.
20587416	8	76	theme	disintegrin	1311:1321	arg1	member					1359:1364	a disintegrin and metalloproteinase (ADAM) family member	1309:1364	a disintegrin and metalloproteinase (ADAM) family member	1309:1364	Metalloproteinase inhibitors were able to inhibit the cleavage, suggesting that it is mediated by a matrix metalloproteinase or a disintegrin and metalloproteinase (ADAM) family member.
20587416	4	77	theme	cell	582:585	arg1	assays					609:614	cell surface biotinylation assays	582:614	cell surface biotinylation assays	582:614	Metabolic pulse-chase labeling and cell surface biotinylation assays showed that the synthesized receptors are efficiently and rapidly transported to the cell surface.
20587416	1	78	theme	beta	127:130	arg1	receptor					117:124	The beta(1)-adrenergic receptor	94:124	The beta(1)-adrenergic receptor (beta(1)AR)	94:136	The beta(1)-adrenergic receptor (beta(1)AR) is the predominant betaAR in the heart, mediating the catecholamine-stimulated increase in cardiac rate and force of contraction.
20587416	1	78	theme	beta	127:130	arg1	AR					134:135	beta(1)AR	127:135	beta(1)AR	127:135	The beta(1)-adrenergic receptor (beta(1)AR) is the predominant betaAR in the heart, mediating the catecholamine-stimulated increase in cardiac rate and force of contraction.
20587416	9	79	dep	also	1450:1453	arg1	vivo					1458:1461	vivo	1458:1461	vivo	1458:1461	Most importantly, the N-terminal cleavage was found to occur not only in vitro but also in vivo.
20587416	0	80	theme	regulated	63:71	arg1	cleavage					84:91	constitutive and regulated N-terminal cleavage	46:91	constitutive and regulated N-terminal cleavage	46:91	Human beta1-adrenergic receptor is subject to constitutive and regulated N-terminal cleavage.
20587416	10	81	theme	Receptor	1464:1471	arg1	activation					1473:1482	Receptor activation	1464:1482	Receptor activation mediated by the betaAR agonist isoproterenol	1464:1527	Receptor activation mediated by the betaAR agonist isoproterenol enhanced the cleavage in a concentration- and time-dependent manner, and it was also enhanced by direct stimulation of protein kinase C and adenylyl cyclase.
20587416	4	82	theme	synthesized	632:642	arg1	receptors					644:652	the synthesized receptors	628:652	the synthesized receptors	628:652	Metabolic pulse-chase labeling and cell surface biotinylation assays showed that the synthesized receptors are efficiently and rapidly transported to the cell surface.
20587416	4	83	theme	pulse-chase	557:567	arg1	labeling					569:576	Metabolic pulse-chase labeling	547:576	Metabolic pulse-chase labeling	547:576	Metabolic pulse-chase labeling and cell surface biotinylation assays showed that the synthesized receptors are efficiently and rapidly transported to the cell surface.
15183061	7	0	theme	-1alpha	1094:1100	arg1	ligand					1115:1120	the natural ligand	1103:1120	the natural ligand of CXCR4	1103:1129	Binding of stromal cell-derived factor (SDF)-1alpha, the natural ligand of CXCR4, and SDF-1alpha-induced signaling were reduced by the N11Q mutation.
15183061	7	0	theme	-1alpha	1094:1100	arg1	signaling					1155:1163	SDF-1alpha-induced signaling	1136:1163	SDF-1alpha-induced signaling	1136:1163	Binding of stromal cell-derived factor (SDF)-1alpha, the natural ligand of CXCR4, and SDF-1alpha-induced signaling were reduced by the N11Q mutation.
15183061	7	0	theme	-1alpha	1094:1100	arg1	Binding					1050:1056	Binding	1050:1056	Binding of stromal cell-derived factor (SDF)-1alpha	1050:1100	Binding of stromal cell-derived factor (SDF)-1alpha, the natural ligand of CXCR4, and SDF-1alpha-induced signaling were reduced by the N11Q mutation.
15183061	6	1	theme	R5	878:879	arg1	viruses					887:893	R5 HIV-1 viruses	878:893	R5 HIV-1 viruses	878:893	However, the binding of R5 gp120 to N11Q-CXCR4 and entry of R5 HIV-1 viruses into cells expressing N11Q-CXCR4 were 20- and 100- to 1000-fold less efficient, respectively, than the levels achieved using X4 gp120 or X4 HIV-1 viruses.
15183061	5	2	theme	N11	641:643	arg1	Mutation					604:611	Mutation	604:611	Mutation of the N-glycosylation site N11 in CXCR4 (N11Q-CXCR4)	604:665	Mutation of the N-glycosylation site N11 in CXCR4 (N11Q-CXCR4) enhanced CD4-dependent binding of X4 and R5 gp120s and allowed more efficient entry of viruses pseudotyped with X4 or R5 HIV-1 envelope glycoproteins.
15183061	5	3	theme	CD4-dependent	676:688	arg1	binding					690:696	CD4-dependent binding	676:696	CD4-dependent binding of X4 and R5 gp120s	676:716	Mutation of the N-glycosylation site N11 in CXCR4 (N11Q-CXCR4) enhanced CD4-dependent binding of X4 and R5 gp120s and allowed more efficient entry of viruses pseudotyped with X4 or R5 HIV-1 envelope glycoproteins.
15183061	1	4	theme	immunodeficiency	145:160	arg1	type					168:171	human immunodeficiency virus type 1	139:173	human immunodeficiency virus type 1 (HIV-1)	139:181	CXCR4 is a co-receptor along with CD4 for human immunodeficiency virus type 1 (HIV-1).
15183061	1	4	theme	immunodeficiency	145:160	arg1	HIV-1					176:180	HIV-1	176:180	HIV-1	176:180	CXCR4 is a co-receptor along with CD4 for human immunodeficiency virus type 1 (HIV-1).
15183061	4	5	theme	N-glycosylated	563:576	arg1	CXCR4					578:582	non-N-glycosylated or N-glycosylated CXCR4	541:582	non-N-glycosylated or N-glycosylated CXCR4 expressed on cells	541:601	Similar results were observed in binding studies using non-N-glycosylated or N-glycosylated CXCR4 expressed on cells.
15183061	0	6	theme	envelope	73:80	arg1	glycoproteins					82:94	HIV-1 envelope glycoproteins	67:94	HIV-1 envelope glycoproteins	67:94	N-linked glycosylation in the CXCR4 N-terminus inhibits binding to HIV-1 envelope glycoproteins.
15183061	0	7	from	glycosylation	9:21	arg1	N-terminus					36:45	the CXCR4 N-terminus	26:45	the CXCR4 N-terminus	26:45	N-linked glycosylation in the CXCR4 N-terminus inhibits binding to HIV-1 envelope glycoproteins.
15183061	7	8	theme	cell-derived	1069:1080	arg1	-1alpha					1094:1100	stromal cell-derived factor (SDF)-1alpha	1061:1100	stromal cell-derived factor (SDF)-1alpha	1061:1100	Binding of stromal cell-derived factor (SDF)-1alpha, the natural ligand of CXCR4, and SDF-1alpha-induced signaling were reduced by the N11Q mutation.
15183061	1	9	theme	virus	162:166	arg1	type					168:171	human immunodeficiency virus type 1	139:173	human immunodeficiency virus type 1 (HIV-1)	139:181	CXCR4 is a co-receptor along with CD4 for human immunodeficiency virus type 1 (HIV-1).
15183061	1	9	theme	virus	162:166	arg1	HIV-1					176:180	HIV-1	176:180	HIV-1	176:180	CXCR4 is a co-receptor along with CD4 for human immunodeficiency virus type 1 (HIV-1).
15183061	6	10	theme	R5	842:843	arg1	gp120					845:849	R5 gp120	842:849	R5 gp120	842:849	However, the binding of R5 gp120 to N11Q-CXCR4 and entry of R5 HIV-1 viruses into cells expressing N11Q-CXCR4 were 20- and 100- to 1000-fold less efficient, respectively, than the levels achieved using X4 gp120 or X4 HIV-1 viruses.
15183061	5	11	theme	R5	708:709	arg1	binding					690:696	CD4-dependent binding	676:696	CD4-dependent binding of X4 and R5 gp120s	676:716	Mutation of the N-glycosylation site N11 in CXCR4 (N11Q-CXCR4) enhanced CD4-dependent binding of X4 and R5 gp120s and allowed more efficient entry of viruses pseudotyped with X4 or R5 HIV-1 envelope glycoproteins.
15183061	4	12	gly	N-glycosylated	563:576	arg1	CXCR4					578:582	non-N-glycosylated or N-glycosylated CXCR4	541:582	non-N-glycosylated or N-glycosylated CXCR4 expressed on cells	541:601	Similar results were observed in binding studies using non-N-glycosylated or N-glycosylated CXCR4 expressed on cells.
15183061	8	13	theme	CXCR4	1279:1283	arg1	binding					1268:1274	the binding	1264:1274	the binding of CXCR4 to X4 and R5 HIV-1 gp120	1264:1308	These findings demonstrate that N-glycosylation at N11 inhibits the binding of CXCR4 to X4 and R5 HIV-1 gp120, and provide a better understanding of the structural elements of CXCR4 involved in HIV-1 Env-co-receptor interactions.
15183061	8	14	theme	HIV-1	1298:1302	arg1	gp120					1304:1308	R5 HIV-1 gp120	1295:1308	R5 HIV-1 gp120	1295:1308	These findings demonstrate that N-glycosylation at N11 inhibits the binding of CXCR4 to X4 and R5 HIV-1 gp120, and provide a better understanding of the structural elements of CXCR4 involved in HIV-1 Env-co-receptor interactions.
15183061	7	15	theme	N11Q	1185:1188	arg1	mutation					1190:1197	the N11Q mutation	1181:1197	the N11Q mutation	1181:1197	Binding of stromal cell-derived factor (SDF)-1alpha, the natural ligand of CXCR4, and SDF-1alpha-induced signaling were reduced by the N11Q mutation.
15183061	7	16	theme	SDF-1alpha-induced	1136:1153	arg1	signaling					1155:1163	SDF-1alpha-induced signaling	1136:1163	SDF-1alpha-induced signaling	1136:1163	Binding of stromal cell-derived factor (SDF)-1alpha, the natural ligand of CXCR4, and SDF-1alpha-induced signaling were reduced by the N11Q mutation.
15183061	7	17	theme	SDF	1090:1092	arg1	-1alpha					1094:1100	stromal cell-derived factor (SDF)-1alpha	1061:1100	stromal cell-derived factor (SDF)-1alpha	1061:1100	Binding of stromal cell-derived factor (SDF)-1alpha, the natural ligand of CXCR4, and SDF-1alpha-induced signaling were reduced by the N11Q mutation.
15183061	3	18	theme	CD4-dependent	464:476	arg1	manner					478:483	a CD4-dependent manner	462:483	a CD4-dependent manner	462:483	Gp120s from CXCR4 (X4) and CCR5 (R5) using HIV-1 strains bound more efficiently to non-N-glycosylated than to N-glycosylated CXCR4 proteoliposomes in a CD4-dependent manner.
15183061	2	19	from	role	204:207	arg1	N-terminus					242:251	the N-terminus	238:251	the N-terminus of CXCR4	238:260	We investigated the role of N-linked glycosylation in the N-terminus of CXCR4 in binding to HIV-1 gp120 envelope glycoproteins.
15183061	3	20	from	CCR5	339:342	arg1	Gp120s					312:317	Gp120s	312:317	Gp120s from CXCR4 (X4) and CCR5 (R5) using HIV-1 strains	312:367	Gp120s from CXCR4 (X4) and CCR5 (R5) using HIV-1 strains bound more efficiently to non-N-glycosylated than to N-glycosylated CXCR4 proteoliposomes in a CD4-dependent manner.
15183061	6	21	theme	HIV-1	1035:1039	arg1	viruses					1041:1047	X4 gp120 or X4 HIV-1 viruses	1020:1047	X4 gp120 or X4 HIV-1 viruses	1020:1047	However, the binding of R5 gp120 to N11Q-CXCR4 and entry of R5 HIV-1 viruses into cells expressing N11Q-CXCR4 were 20- and 100- to 1000-fold less efficient, respectively, than the levels achieved using X4 gp120 or X4 HIV-1 viruses.
15183061	0	22	link	N-linked	0:7	arg1	glycosylation					9:21	N-linked glycosylation	0:21	N-linked glycosylation in the CXCR4 N-terminus	0:45	N-linked glycosylation in the CXCR4 N-terminus inhibits binding to HIV-1 envelope glycoproteins.
15183061	2	23	theme	CXCR4	256:260	arg1	N-terminus					242:251	the N-terminus	238:251	the N-terminus of CXCR4	238:260	We investigated the role of N-linked glycosylation in the N-terminus of CXCR4 in binding to HIV-1 gp120 envelope glycoproteins.
15183061	8	24	theme	HIV-1	1394:1398	arg1	interactions					1416:1427	HIV-1 Env-co-receptor interactions	1394:1427	HIV-1 Env-co-receptor interactions	1394:1427	These findings demonstrate that N-glycosylation at N11 inhibits the binding of CXCR4 to X4 and R5 HIV-1 gp120, and provide a better understanding of the structural elements of CXCR4 involved in HIV-1 Env-co-receptor interactions.
15183061	5	25	gly	glycoproteins	803:815	arg1	glycoproteins					803:815	HIV-1 envelope glycoproteins	788:815	HIV-1 envelope glycoproteins	788:815	Mutation of the N-glycosylation site N11 in CXCR4 (N11Q-CXCR4) enhanced CD4-dependent binding of X4 and R5 gp120s and allowed more efficient entry of viruses pseudotyped with X4 or R5 HIV-1 envelope glycoproteins.
15183061	0	26	gly	glycoproteins	82:94	arg1	glycoproteins					82:94	HIV-1 envelope glycoproteins	67:94	HIV-1 envelope glycoproteins	67:94	N-linked glycosylation in the CXCR4 N-terminus inhibits binding to HIV-1 envelope glycoproteins.
15183061	6	27	theme	X4	1032:1033	arg1	HIV-1					1035:1039	X4 gp120 or X4 HIV-1	1020:1039	HIV-1	1035:1039	However, the binding of R5 gp120 to N11Q-CXCR4 and entry of R5 HIV-1 viruses into cells expressing N11Q-CXCR4 were 20- and 100- to 1000-fold less efficient, respectively, than the levels achieved using X4 gp120 or X4 HIV-1 viruses.
15183061	6	28	theme	gp120	1023:1027	arg1	viruses					1041:1047	X4 gp120 or X4 HIV-1 viruses	1020:1047	X4 gp120 or X4 HIV-1 viruses	1020:1047	However, the binding of R5 gp120 to N11Q-CXCR4 and entry of R5 HIV-1 viruses into cells expressing N11Q-CXCR4 were 20- and 100- to 1000-fold less efficient, respectively, than the levels achieved using X4 gp120 or X4 HIV-1 viruses.
15183061	8	29	gly	N-glycosylation	1232:1246	arg2	N11					1251:1253	N11	1251:1253	N11	1251:1253	These findings demonstrate that N-glycosylation at N11 inhibits the binding of CXCR4 to X4 and R5 HIV-1 gp120, and provide a better understanding of the structural elements of CXCR4 involved in HIV-1 Env-co-receptor interactions.
15183061	8	29	gly	N-glycosylation	1232:1246	arg1	N11					1251:1253	N11	1251:1253	N11	1251:1253	These findings demonstrate that N-glycosylation at N11 inhibits the binding of CXCR4 to X4 and R5 HIV-1 gp120, and provide a better understanding of the structural elements of CXCR4 involved in HIV-1 Env-co-receptor interactions.
15183061	6	30	theme	gp120	845:849	arg1	binding					831:837	the binding	827:837	the binding of R5 gp120 to N11Q-CXCR4	827:863	However, the binding of R5 gp120 to N11Q-CXCR4 and entry of R5 HIV-1 viruses into cells expressing N11Q-CXCR4 were 20- and 100- to 1000-fold less efficient, respectively, than the levels achieved using X4 gp120 or X4 HIV-1 viruses.
15183061	6	30	theme	gp120	845:849	arg1	100-					941:944	100-	941:944	100-	941:944	However, the binding of R5 gp120 to N11Q-CXCR4 and entry of R5 HIV-1 viruses into cells expressing N11Q-CXCR4 were 20- and 100- to 1000-fold less efficient, respectively, than the levels achieved using X4 gp120 or X4 HIV-1 viruses.
15183061	6	30	theme	gp120	845:849	arg1	20-					933:935	20-	933:935	20-	933:935	However, the binding of R5 gp120 to N11Q-CXCR4 and entry of R5 HIV-1 viruses into cells expressing N11Q-CXCR4 were 20- and 100- to 1000-fold less efficient, respectively, than the levels achieved using X4 gp120 or X4 HIV-1 viruses.
15183061	6	30	theme	gp120	845:849	arg1	efficient					964:972	efficient	964:972	efficient	964:972	However, the binding of R5 gp120 to N11Q-CXCR4 and entry of R5 HIV-1 viruses into cells expressing N11Q-CXCR4 were 20- and 100- to 1000-fold less efficient, respectively, than the levels achieved using X4 gp120 or X4 HIV-1 viruses.
15183061	6	30	theme	gp120	845:849	arg1	entry					869:873	entry	869:873	entry of R5 HIV-1 viruses into cells expressing N11Q-CXCR4	869:926	However, the binding of R5 gp120 to N11Q-CXCR4 and entry of R5 HIV-1 viruses into cells expressing N11Q-CXCR4 were 20- and 100- to 1000-fold less efficient, respectively, than the levels achieved using X4 gp120 or X4 HIV-1 viruses.
15183061	5	31	theme	N-glycosylation	620:634	arg1	N11					641:643	the N-glycosylation site N11	616:643	the N-glycosylation site N11	616:643	Mutation of the N-glycosylation site N11 in CXCR4 (N11Q-CXCR4) enhanced CD4-dependent binding of X4 and R5 gp120s and allowed more efficient entry of viruses pseudotyped with X4 or R5 HIV-1 envelope glycoproteins.
15183061	3	32	from	proteoliposomes	443:457	arg1	manner					478:483	a CD4-dependent manner	462:483	a CD4-dependent manner	462:483	Gp120s from CXCR4 (X4) and CCR5 (R5) using HIV-1 strains bound more efficiently to non-N-glycosylated than to N-glycosylated CXCR4 proteoliposomes in a CD4-dependent manner.
15183061	2	33	theme	envelope	288:295	arg1	glycoproteins					297:309	HIV-1 gp120 envelope glycoproteins	276:309	HIV-1 gp120 envelope glycoproteins	276:309	We investigated the role of N-linked glycosylation in the N-terminus of CXCR4 in binding to HIV-1 gp120 envelope glycoproteins.
15183061	6	34	dep	efficient	964:972	arg1	binding					831:837	the binding	827:837	the binding of R5 gp120 to N11Q-CXCR4	827:863	However, the binding of R5 gp120 to N11Q-CXCR4 and entry of R5 HIV-1 viruses into cells expressing N11Q-CXCR4 were 20- and 100- to 1000-fold less efficient, respectively, than the levels achieved using X4 gp120 or X4 HIV-1 viruses.
15183061	6	34	dep	efficient	964:972	arg1	100-					941:944	100-	941:944	100-	941:944	However, the binding of R5 gp120 to N11Q-CXCR4 and entry of R5 HIV-1 viruses into cells expressing N11Q-CXCR4 were 20- and 100- to 1000-fold less efficient, respectively, than the levels achieved using X4 gp120 or X4 HIV-1 viruses.
15183061	6	34	dep	efficient	964:972	arg1	20-					933:935	20-	933:935	20-	933:935	However, the binding of R5 gp120 to N11Q-CXCR4 and entry of R5 HIV-1 viruses into cells expressing N11Q-CXCR4 were 20- and 100- to 1000-fold less efficient, respectively, than the levels achieved using X4 gp120 or X4 HIV-1 viruses.
15183061	6	34	dep	efficient	964:972	arg1	efficient					964:972	efficient	964:972	efficient	964:972	However, the binding of R5 gp120 to N11Q-CXCR4 and entry of R5 HIV-1 viruses into cells expressing N11Q-CXCR4 were 20- and 100- to 1000-fold less efficient, respectively, than the levels achieved using X4 gp120 or X4 HIV-1 viruses.
15183061	6	35	theme	X4	1020:1021	arg1	gp120					1023:1027	X4 gp120 or X4 HIV-1	1020:1039	gp120	1023:1027	However, the binding of R5 gp120 to N11Q-CXCR4 and entry of R5 HIV-1 viruses into cells expressing N11Q-CXCR4 were 20- and 100- to 1000-fold less efficient, respectively, than the levels achieved using X4 gp120 or X4 HIV-1 viruses.
15183061	0	36	theme	N-linked	0:7	arg1	glycosylation					9:21	N-linked glycosylation	0:21	N-linked glycosylation in the CXCR4 N-terminus	0:45	N-linked glycosylation in the CXCR4 N-terminus inhibits binding to HIV-1 envelope glycoproteins.
15183061	5	37	theme	site	636:639	arg1	N11					641:643	the N-glycosylation site N11	616:643	the N-glycosylation site N11	616:643	Mutation of the N-glycosylation site N11 in CXCR4 (N11Q-CXCR4) enhanced CD4-dependent binding of X4 and R5 gp120s and allowed more efficient entry of viruses pseudotyped with X4 or R5 HIV-1 envelope glycoproteins.
15183061	2	38	theme	gp120	282:286	arg1	glycoproteins					297:309	HIV-1 gp120 envelope glycoproteins	276:309	HIV-1 gp120 envelope glycoproteins	276:309	We investigated the role of N-linked glycosylation in the N-terminus of CXCR4 in binding to HIV-1 gp120 envelope glycoproteins.
15183061	8	39	theme	elements	1364:1371	arg1	understanding					1332:1344	a better understanding	1323:1344	a better understanding of the structural elements of CXCR4 involved in HIV-1 Env-co-receptor interactions	1323:1427	These findings demonstrate that N-glycosylation at N11 inhibits the binding of CXCR4 to X4 and R5 HIV-1 gp120, and provide a better understanding of the structural elements of CXCR4 involved in HIV-1 Env-co-receptor interactions.
15183061	2	40	gly	glycosylation	221:233	arg1	CXCR4					256:260	CXCR4	256:260	CXCR4	256:260	We investigated the role of N-linked glycosylation in the N-terminus of CXCR4 in binding to HIV-1 gp120 envelope glycoproteins.
15183061	4	41	theme	binding	519:525	arg1	studies					527:533	binding studies	519:533	binding studies using non-N-glycosylated or N-glycosylated CXCR4 expressed on cells	519:601	Similar results were observed in binding studies using non-N-glycosylated or N-glycosylated CXCR4 expressed on cells.
15183061	7	42	theme	stromal	1061:1067	arg1	-1alpha					1094:1100	stromal cell-derived factor (SDF)-1alpha	1061:1100	stromal cell-derived factor (SDF)-1alpha	1061:1100	Binding of stromal cell-derived factor (SDF)-1alpha, the natural ligand of CXCR4, and SDF-1alpha-induced signaling were reduced by the N11Q mutation.
15183061	8	43	from	N11	1251:1253	arg1	N-glycosylation					1232:1246	N-glycosylation	1232:1246	N-glycosylation at N11	1232:1253	These findings demonstrate that N-glycosylation at N11 inhibits the binding of CXCR4 to X4 and R5 HIV-1 gp120, and provide a better understanding of the structural elements of CXCR4 involved in HIV-1 Env-co-receptor interactions.
15183061	2	44	theme	HIV-1	276:280	arg1	glycoproteins					297:309	HIV-1 gp120 envelope glycoproteins	276:309	HIV-1 gp120 envelope glycoproteins	276:309	We investigated the role of N-linked glycosylation in the N-terminus of CXCR4 in binding to HIV-1 gp120 envelope glycoproteins.
15183061	3	45	gly	N-glycosylated	422:435	arg1	proteoliposomes					443:457	N-glycosylated CXCR4 proteoliposomes	422:457	N-glycosylated CXCR4 proteoliposomes in a CD4-dependent manner	422:483	Gp120s from CXCR4 (X4) and CCR5 (R5) using HIV-1 strains bound more efficiently to non-N-glycosylated than to N-glycosylated CXCR4 proteoliposomes in a CD4-dependent manner.
15183061	5	46	theme	envelope	794:801	arg1	glycoproteins					803:815	HIV-1 envelope glycoproteins	788:815	HIV-1 envelope glycoproteins	788:815	Mutation of the N-glycosylation site N11 in CXCR4 (N11Q-CXCR4) enhanced CD4-dependent binding of X4 and R5 gp120s and allowed more efficient entry of viruses pseudotyped with X4 or R5 HIV-1 envelope glycoproteins.
15183061	4	47	theme	non-N-glycosylated	541:558	arg1	CXCR4					578:582	non-N-glycosylated or N-glycosylated CXCR4	541:582	non-N-glycosylated or N-glycosylated CXCR4 expressed on cells	541:601	Similar results were observed in binding studies using non-N-glycosylated or N-glycosylated CXCR4 expressed on cells.
15183061	3	48	from	CXCR4	324:328	arg1	Gp120s					312:317	Gp120s	312:317	Gp120s from CXCR4 (X4) and CCR5 (R5) using HIV-1 strains	312:367	Gp120s from CXCR4 (X4) and CCR5 (R5) using HIV-1 strains bound more efficiently to non-N-glycosylated than to N-glycosylated CXCR4 proteoliposomes in a CD4-dependent manner.
15183061	5	49	theme	HIV-1	788:792	arg1	glycoproteins					803:815	HIV-1 envelope glycoproteins	788:815	HIV-1 envelope glycoproteins	788:815	Mutation of the N-glycosylation site N11 in CXCR4 (N11Q-CXCR4) enhanced CD4-dependent binding of X4 and R5 gp120s and allowed more efficient entry of viruses pseudotyped with X4 or R5 HIV-1 envelope glycoproteins.
15183061	8	50	theme	R5	1295:1296	arg1	gp120					1304:1308	R5 HIV-1 gp120	1295:1308	R5 HIV-1 gp120	1295:1308	These findings demonstrate that N-glycosylation at N11 inhibits the binding of CXCR4 to X4 and R5 HIV-1 gp120, and provide a better understanding of the structural elements of CXCR4 involved in HIV-1 Env-co-receptor interactions.
15183061	3	51	theme	N-glycosylated	422:435	arg1	proteoliposomes					443:457	N-glycosylated CXCR4 proteoliposomes	422:457	N-glycosylated CXCR4 proteoliposomes in a CD4-dependent manner	422:483	Gp120s from CXCR4 (X4) and CCR5 (R5) using HIV-1 strains bound more efficiently to non-N-glycosylated than to N-glycosylated CXCR4 proteoliposomes in a CD4-dependent manner.
15183061	3	52	theme	HIV-1	355:359	arg1	strains					361:367	HIV-1 strains	355:367	HIV-1 strains	355:367	Gp120s from CXCR4 (X4) and CCR5 (R5) using HIV-1 strains bound more efficiently to non-N-glycosylated than to N-glycosylated CXCR4 proteoliposomes in a CD4-dependent manner.
15183061	5	53	theme	X4	701:702	arg1	binding					690:696	CD4-dependent binding	676:696	CD4-dependent binding of X4 and R5 gp120s	676:716	Mutation of the N-glycosylation site N11 in CXCR4 (N11Q-CXCR4) enhanced CD4-dependent binding of X4 and R5 gp120s and allowed more efficient entry of viruses pseudotyped with X4 or R5 HIV-1 envelope glycoproteins.
15183061	7	54	theme	natural	1107:1113	arg1	ligand					1115:1120	the natural ligand	1103:1120	the natural ligand of CXCR4	1103:1129	Binding of stromal cell-derived factor (SDF)-1alpha, the natural ligand of CXCR4, and SDF-1alpha-induced signaling were reduced by the N11Q mutation.
15183061	2	55	theme	N-linked	212:219	arg1	glycosylation					221:233	N-linked glycosylation	212:233	N-linked glycosylation	212:233	We investigated the role of N-linked glycosylation in the N-terminus of CXCR4 in binding to HIV-1 gp120 envelope glycoproteins.
15183061	0	56	theme	CXCR4	30:34	arg1	N-terminus					36:45	the CXCR4 N-terminus	26:45	the CXCR4 N-terminus	26:45	N-linked glycosylation in the CXCR4 N-terminus inhibits binding to HIV-1 envelope glycoproteins.
15183061	8	57	theme	CXCR4	1376:1380	arg1	elements					1364:1371	the structural elements	1349:1371	the structural elements of CXCR4 involved in HIV-1 Env-co-receptor interactions	1349:1427	These findings demonstrate that N-glycosylation at N11 inhibits the binding of CXCR4 to X4 and R5 HIV-1 gp120, and provide a better understanding of the structural elements of CXCR4 involved in HIV-1 Env-co-receptor interactions.
15183061	0	58	gly	glycosylation	9:21	arg1	N-terminus					36:45	the CXCR4 N-terminus	26:45	the CXCR4 N-terminus	26:45	N-linked glycosylation in the CXCR4 N-terminus inhibits binding to HIV-1 envelope glycoproteins.
15183061	4	59	theme	Similar	486:492	arg1	results					494:500	Similar results	486:500	Similar results	486:500	Similar results were observed in binding studies using non-N-glycosylated or N-glycosylated CXCR4 expressed on cells.
15183061	5	60	gly	N-glycosylation	620:634	arg2	site					636:639	the N-glycosylation site N11	616:643	the N-glycosylation site N11	616:643	Mutation of the N-glycosylation site N11 in CXCR4 (N11Q-CXCR4) enhanced CD4-dependent binding of X4 and R5 gp120s and allowed more efficient entry of viruses pseudotyped with X4 or R5 HIV-1 envelope glycoproteins.
15183061	5	60	gly	N-glycosylation	620:634	arg2	N11					641:643	the N-glycosylation site N11	616:643	the N-glycosylation site N11	616:643	Mutation of the N-glycosylation site N11 in CXCR4 (N11Q-CXCR4) enhanced CD4-dependent binding of X4 and R5 gp120s and allowed more efficient entry of viruses pseudotyped with X4 or R5 HIV-1 envelope glycoproteins.
15183061	7	61	theme	factor	1082:1087	arg1	-1alpha					1094:1100	stromal cell-derived factor (SDF)-1alpha	1061:1100	stromal cell-derived factor (SDF)-1alpha	1061:1100	Binding of stromal cell-derived factor (SDF)-1alpha, the natural ligand of CXCR4, and SDF-1alpha-induced signaling were reduced by the N11Q mutation.
15183061	7	62	theme	CXCR4	1125:1129	arg1	ligand					1115:1120	the natural ligand	1103:1120	the natural ligand of CXCR4	1103:1129	Binding of stromal cell-derived factor (SDF)-1alpha, the natural ligand of CXCR4, and SDF-1alpha-induced signaling were reduced by the N11Q mutation.
15183061	7	62	theme	CXCR4	1125:1129	arg1	signaling					1155:1163	SDF-1alpha-induced signaling	1136:1163	SDF-1alpha-induced signaling	1136:1163	Binding of stromal cell-derived factor (SDF)-1alpha, the natural ligand of CXCR4, and SDF-1alpha-induced signaling were reduced by the N11Q mutation.
15183061	7	62	theme	CXCR4	1125:1129	arg1	Binding					1050:1056	Binding	1050:1056	Binding of stromal cell-derived factor (SDF)-1alpha	1050:1100	Binding of stromal cell-derived factor (SDF)-1alpha, the natural ligand of CXCR4, and SDF-1alpha-induced signaling were reduced by the N11Q mutation.
15183061	6	63	dep	100-	941:944	arg1	to					946:947	to	946:947	to	946:947	However, the binding of R5 gp120 to N11Q-CXCR4 and entry of R5 HIV-1 viruses into cells expressing N11Q-CXCR4 were 20- and 100- to 1000-fold less efficient, respectively, than the levels achieved using X4 gp120 or X4 HIV-1 viruses.
15183061	5	64	dep	X4	779:780	arg1	glycoproteins					803:815	HIV-1 envelope glycoproteins	788:815	HIV-1 envelope glycoproteins	788:815	Mutation of the N-glycosylation site N11 in CXCR4 (N11Q-CXCR4) enhanced CD4-dependent binding of X4 and R5 gp120s and allowed more efficient entry of viruses pseudotyped with X4 or R5 HIV-1 envelope glycoproteins.
15183061	8	65	theme	structural	1353:1362	arg1	elements					1364:1371	the structural elements	1349:1371	the structural elements of CXCR4 involved in HIV-1 Env-co-receptor interactions	1349:1427	These findings demonstrate that N-glycosylation at N11 inhibits the binding of CXCR4 to X4 and R5 HIV-1 gp120, and provide a better understanding of the structural elements of CXCR4 involved in HIV-1 Env-co-receptor interactions.
15183061	6	66	theme	viruses	887:893	arg1	binding					831:837	the binding	827:837	the binding of R5 gp120 to N11Q-CXCR4	827:863	However, the binding of R5 gp120 to N11Q-CXCR4 and entry of R5 HIV-1 viruses into cells expressing N11Q-CXCR4 were 20- and 100- to 1000-fold less efficient, respectively, than the levels achieved using X4 gp120 or X4 HIV-1 viruses.
15183061	6	66	theme	viruses	887:893	arg1	100-					941:944	100-	941:944	100-	941:944	However, the binding of R5 gp120 to N11Q-CXCR4 and entry of R5 HIV-1 viruses into cells expressing N11Q-CXCR4 were 20- and 100- to 1000-fold less efficient, respectively, than the levels achieved using X4 gp120 or X4 HIV-1 viruses.
15183061	6	66	theme	viruses	887:893	arg1	20-					933:935	20-	933:935	20-	933:935	However, the binding of R5 gp120 to N11Q-CXCR4 and entry of R5 HIV-1 viruses into cells expressing N11Q-CXCR4 were 20- and 100- to 1000-fold less efficient, respectively, than the levels achieved using X4 gp120 or X4 HIV-1 viruses.
15183061	6	66	theme	viruses	887:893	arg1	efficient					964:972	efficient	964:972	efficient	964:972	However, the binding of R5 gp120 to N11Q-CXCR4 and entry of R5 HIV-1 viruses into cells expressing N11Q-CXCR4 were 20- and 100- to 1000-fold less efficient, respectively, than the levels achieved using X4 gp120 or X4 HIV-1 viruses.
15183061	6	66	theme	viruses	887:893	arg1	entry					869:873	entry	869:873	entry of R5 HIV-1 viruses into cells expressing N11Q-CXCR4	869:926	However, the binding of R5 gp120 to N11Q-CXCR4 and entry of R5 HIV-1 viruses into cells expressing N11Q-CXCR4 were 20- and 100- to 1000-fold less efficient, respectively, than the levels achieved using X4 gp120 or X4 HIV-1 viruses.
15183061	2	67	gly	glycoproteins	297:309	arg1	glycoproteins					297:309	HIV-1 gp120 envelope glycoproteins	276:309	HIV-1 gp120 envelope glycoproteins	276:309	We investigated the role of N-linked glycosylation in the N-terminus of CXCR4 in binding to HIV-1 gp120 envelope glycoproteins.
15183061	5	68	dep	X4	701:702	arg1	gp120s					711:716	gp120s	711:716	gp120s	711:716	Mutation of the N-glycosylation site N11 in CXCR4 (N11Q-CXCR4) enhanced CD4-dependent binding of X4 and R5 gp120s and allowed more efficient entry of viruses pseudotyped with X4 or R5 HIV-1 envelope glycoproteins.
15183061	4	69	gly	non-N-glycosylated	541:558	arg1	CXCR4					578:582	non-N-glycosylated or N-glycosylated CXCR4	541:582	non-N-glycosylated or N-glycosylated CXCR4 expressed on cells	541:601	Similar results were observed in binding studies using non-N-glycosylated or N-glycosylated CXCR4 expressed on cells.
15183061	3	70	theme	CXCR4	437:441	arg1	proteoliposomes					443:457	N-glycosylated CXCR4 proteoliposomes	422:457	N-glycosylated CXCR4 proteoliposomes in a CD4-dependent manner	422:483	Gp120s from CXCR4 (X4) and CCR5 (R5) using HIV-1 strains bound more efficiently to non-N-glycosylated than to N-glycosylated CXCR4 proteoliposomes in a CD4-dependent manner.
15183061	4	71	located	observed	507:514	arg1	studies					527:533	binding studies	519:533	binding studies using non-N-glycosylated or N-glycosylated CXCR4 expressed on cells	519:601	Similar results were observed in binding studies using non-N-glycosylated or N-glycosylated CXCR4 expressed on cells.
15183061	4	71	located	observed	507:514	arg2	results					494:500	Similar results	486:500	Similar results	486:500	Similar results were observed in binding studies using non-N-glycosylated or N-glycosylated CXCR4 expressed on cells.
15183061	5	72	theme	viruses	754:760	arg1	entry					745:749	more efficient entry	730:749	more efficient entry of viruses pseudotyped with X4 or R5 HIV-1 envelope glycoproteins	730:815	Mutation of the N-glycosylation site N11 in CXCR4 (N11Q-CXCR4) enhanced CD4-dependent binding of X4 and R5 gp120s and allowed more efficient entry of viruses pseudotyped with X4 or R5 HIV-1 envelope glycoproteins.
15183061	8	73	theme	Env-co-receptor	1400:1414	arg1	interactions					1416:1427	HIV-1 Env-co-receptor interactions	1394:1427	HIV-1 Env-co-receptor interactions	1394:1427	These findings demonstrate that N-glycosylation at N11 inhibits the binding of CXCR4 to X4 and R5 HIV-1 gp120, and provide a better understanding of the structural elements of CXCR4 involved in HIV-1 Env-co-receptor interactions.
15183061	8	74	theme	better	1325:1330	arg1	understanding					1332:1344	a better understanding	1323:1344	a better understanding of the structural elements of CXCR4 involved in HIV-1 Env-co-receptor interactions	1323:1427	These findings demonstrate that N-glycosylation at N11 inhibits the binding of CXCR4 to X4 and R5 HIV-1 gp120, and provide a better understanding of the structural elements of CXCR4 involved in HIV-1 Env-co-receptor interactions.
15183061	5	75	from	Mutation	604:611	arg1	N11Q-CXCR4					655:664	N11Q-CXCR4	655:664	N11Q-CXCR4	655:664	Mutation of the N-glycosylation site N11 in CXCR4 (N11Q-CXCR4) enhanced CD4-dependent binding of X4 and R5 gp120s and allowed more efficient entry of viruses pseudotyped with X4 or R5 HIV-1 envelope glycoproteins.
15183061	5	75	from	Mutation	604:611	arg1	CXCR4					648:652	CXCR4	648:652	CXCR4 (N11Q-CXCR4)	648:665	Mutation of the N-glycosylation site N11 in CXCR4 (N11Q-CXCR4) enhanced CD4-dependent binding of X4 and R5 gp120s and allowed more efficient entry of viruses pseudotyped with X4 or R5 HIV-1 envelope glycoproteins.
15183061	0	76	theme	HIV-1	67:71	arg1	glycoproteins					82:94	HIV-1 envelope glycoproteins	67:94	HIV-1 envelope glycoproteins	67:94	N-linked glycosylation in the CXCR4 N-terminus inhibits binding to HIV-1 envelope glycoproteins.
15183061	7	77	link	cell-derived	1069:1080	arg1	-1alpha					1094:1100	stromal cell-derived factor (SDF)-1alpha	1061:1100	stromal cell-derived factor (SDF)-1alpha	1061:1100	Binding of stromal cell-derived factor (SDF)-1alpha, the natural ligand of CXCR4, and SDF-1alpha-induced signaling were reduced by the N11Q mutation.
15183061	2	78	link	N-linked	212:219	arg1	glycosylation					221:233	N-linked glycosylation	212:233	N-linked glycosylation	212:233	We investigated the role of N-linked glycosylation in the N-terminus of CXCR4 in binding to HIV-1 gp120 envelope glycoproteins.
15183061	5	79	theme	efficient	735:743	arg1	entry					745:749	more efficient entry	730:749	more efficient entry of viruses pseudotyped with X4 or R5 HIV-1 envelope glycoproteins	730:815	Mutation of the N-glycosylation site N11 in CXCR4 (N11Q-CXCR4) enhanced CD4-dependent binding of X4 and R5 gp120s and allowed more efficient entry of viruses pseudotyped with X4 or R5 HIV-1 envelope glycoproteins.
15183061	6	80	theme	HIV-1	881:885	arg1	viruses					887:893	R5 HIV-1 viruses	878:893	R5 HIV-1 viruses	878:893	However, the binding of R5 gp120 to N11Q-CXCR4 and entry of R5 HIV-1 viruses into cells expressing N11Q-CXCR4 were 20- and 100- to 1000-fold less efficient, respectively, than the levels achieved using X4 gp120 or X4 HIV-1 viruses.
15183061	2	81	theme	glycosylation	221:233	arg1	role					204:207	the role	200:207	the role of N-linked glycosylation in the N-terminus of CXCR4	200:260	We investigated the role of N-linked glycosylation in the N-terminus of CXCR4 in binding to HIV-1 gp120 envelope glycoproteins.
15183061	1	82	theme	human	139:143	arg1	type					168:171	human immunodeficiency virus type 1	139:173	human immunodeficiency virus type 1 (HIV-1)	139:181	CXCR4 is a co-receptor along with CD4 for human immunodeficiency virus type 1 (HIV-1).
15183061	1	82	theme	human	139:143	arg1	HIV-1					176:180	HIV-1	176:180	HIV-1	176:180	CXCR4 is a co-receptor along with CD4 for human immunodeficiency virus type 1 (HIV-1).
9620884	8	0	theme	enzyme	1521:1526	arg1	polypeptide					1528:1538	the enzyme polypeptide	1517:1538	the enzyme polypeptide	1517:1538	Absence of the site 3 hybrid-type oligosaccharide exposed an adjacent, normally protected, hydrophobic region, resulting in aggregation of the enzyme polypeptide in the endoplasmic reticulum.
9620884	4	1	gly	glycosylation	714:726	arg2	site					728:731	glycosylation site 1 or 2	714:738	site	728:731	When expressed in COS-1 cells, glycoforms with glycosylation site 1 or 2 obliterated had more than 70% of wild-type activity, and both glycoforms were secreted.
9620884	4	1	gly	glycosylation	714:726	arg2	1					733:733	1	733:733	1	733:733	When expressed in COS-1 cells, glycoforms with glycosylation site 1 or 2 obliterated had more than 70% of wild-type activity, and both glycoforms were secreted.
9620884	2	2	from	function	293:300	arg1	hydrolase					359:367	this lysosomal hydrolase	344:367	this lysosomal hydrolase	344:367	The type, site occupancy and function of the N-linked oligosaccharide chains on this lysosomal hydrolase were determined.
9620884	0	3	theme	enzyme	67:72	arg1	solubility					74:83	enzyme solubility	67:83	enzyme solubility	67:83	Human alpha-galactosidase A: glycosylation site 3 is essential for enzyme solubility.
9620884	6	4	contain	had	1030:1032	arg1	glycoforms					970:979	Expressed mutant glycoforms	953:979	Expressed mutant glycoforms in which site 3 and site 1 or 2 were obliterated	953:1028	Expressed mutant glycoforms in which site 3 and site 1 or 2 were obliterated had little, if any, intracellular or secreted enzymic activity, and immunofluorescence microscopy revealed that the expressed mutant glycoforms were retained in the endoplasmic reticulum, presumably where they were degraded.
9620884	6	4	contain	had	1030:1032	arg2	little					1034:1039	little	1034:1039	little	1034:1039	Expressed mutant glycoforms in which site 3 and site 1 or 2 were obliterated had little, if any, intracellular or secreted enzymic activity, and immunofluorescence microscopy revealed that the expressed mutant glycoforms were retained in the endoplasmic reticulum, presumably where they were degraded.
9620884	6	4	contain	had	1030:1032	arg2	activity					1084:1091	intracellular or secreted enzymic activity	1050:1091	intracellular or secreted enzymic activity	1050:1091	Expressed mutant glycoforms in which site 3 and site 1 or 2 were obliterated had little, if any, intracellular or secreted enzymic activity, and immunofluorescence microscopy revealed that the expressed mutant glycoforms were retained in the endoplasmic reticulum, presumably where they were degraded.
9620884	9	5	theme	concept	1589:1595	arg1	support					1573:1579	support	1573:1579	support of this concept	1573:1595	In support of this concept, endoglycosidase H-treated enzyme or mannose-terminated enzyme expressed in Autographa californica cells also aggregated when concentrated, emphasizing that site 3 occupancy by a hybrid-type oligosaccharide was required for enzyme solubility.
9620884	2	6	from	chains	334:339	arg1	hydrolase					359:367	this lysosomal hydrolase	344:367	this lysosomal hydrolase	344:367	The type, site occupancy and function of the N-linked oligosaccharide chains on this lysosomal hydrolase were determined.
9620884	2	7	theme	lysosomal	349:357	arg1	hydrolase					359:367	this lysosomal hydrolase	344:367	this lysosomal hydrolase	344:367	The type, site occupancy and function of the N-linked oligosaccharide chains on this lysosomal hydrolase were determined.
9620884	8	8	from	aggregation	1502:1512	arg1	reticulum					1559:1567	the endoplasmic reticulum	1543:1567	the endoplasmic reticulum	1543:1567	Absence of the site 3 hybrid-type oligosaccharide exposed an adjacent, normally protected, hydrophobic region, resulting in aggregation of the enzyme polypeptide in the endoplasmic reticulum.
9620884	2	9	gly	occupancy	279:287	arg2	site					274:277	site occupancy	274:287	site occupancy	274:287	The type, site occupancy and function of the N-linked oligosaccharide chains on this lysosomal hydrolase were determined.
9620884	2	9	gly	occupancy	279:287	arg2	chains					334:339	the N-linked oligosaccharide chains	305:339	the N-linked oligosaccharide chains on this lysosomal hydrolase	305:367	The type, site occupancy and function of the N-linked oligosaccharide chains on this lysosomal hydrolase were determined.
9620884	2	9	gly	occupancy	279:287	arg1	chains					334:339	the N-linked oligosaccharide chains	305:339	the N-linked oligosaccharide chains on this lysosomal hydrolase	305:367	The type, site occupancy and function of the N-linked oligosaccharide chains on this lysosomal hydrolase were determined.
9620884	3	10	dep	three	486:490	arg1	Asn-215					514:520	Asn-215	514:520	Asn-215	514:520	Endoglycosidase treatment of the purified recombinant enzyme and mutagenesis studies indicated that three (Asn-139, Asn-192 and Asn-215) of the four potential N-glycosylation consensus sequences were occupied by complex, high-mannose and hybrid-type oligosaccharides respectively.
9620884	3	10	dep	three	486:490	arg1	Asn-192					502:508	Asn-192	502:508	Asn-192	502:508	Endoglycosidase treatment of the purified recombinant enzyme and mutagenesis studies indicated that three (Asn-139, Asn-192 and Asn-215) of the four potential N-glycosylation consensus sequences were occupied by complex, high-mannose and hybrid-type oligosaccharides respectively.
9620884	3	10	dep	three	486:490	arg1	Asn-139					493:499	Asn-139	493:499	Asn-139	493:499	Endoglycosidase treatment of the purified recombinant enzyme and mutagenesis studies indicated that three (Asn-139, Asn-192 and Asn-215) of the four potential N-glycosylation consensus sequences were occupied by complex, high-mannose and hybrid-type oligosaccharides respectively.
9620884	7	11	gly	glycosylation	1260:1272	arg1	site					1277:1280	site 3	1277:1282	site 3	1277:1282	Thus glycosylation at site 3 was crucial to the formation of soluble, active enzyme, as well as transport to the lysosome.
9620884	7	11	gly	glycosylation	1260:1272	arg2	site					1277:1280	site 3	1277:1282	site 3	1277:1282	Thus glycosylation at site 3 was crucial to the formation of soluble, active enzyme, as well as transport to the lysosome.
9620884	3	12	theme	consensus	561:569	arg1	sequences					571:579	the four potential N-glycosylation consensus sequences	526:579	the four potential N-glycosylation consensus sequences	526:579	Endoglycosidase treatment of the purified recombinant enzyme and mutagenesis studies indicated that three (Asn-139, Asn-192 and Asn-215) of the four potential N-glycosylation consensus sequences were occupied by complex, high-mannose and hybrid-type oligosaccharides respectively.
9620884	6	13	theme	mutant	963:968	arg1	glycoforms					970:979	Expressed mutant glycoforms	953:979	Expressed mutant glycoforms in which site 3 and site 1 or 2 were obliterated	953:1028	Expressed mutant glycoforms in which site 3 and site 1 or 2 were obliterated had little, if any, intracellular or secreted enzymic activity, and immunofluorescence microscopy revealed that the expressed mutant glycoforms were retained in the endoplasmic reticulum, presumably where they were degraded.
9620884	6	14	theme	immunofluorescence	1098:1115	arg1	microscopy					1117:1126	immunofluorescence microscopy	1098:1126	immunofluorescence microscopy	1098:1126	Expressed mutant glycoforms in which site 3 and site 1 or 2 were obliterated had little, if any, intracellular or secreted enzymic activity, and immunofluorescence microscopy revealed that the expressed mutant glycoforms were retained in the endoplasmic reticulum, presumably where they were degraded.
9620884	1	15	gly	glycoprotein	160:171	arg1	glycoprotein					160:171	the homodimeric glycoprotein	144:171	the homodimeric glycoprotein that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins	144:261	Human alpha-galactosidase A (EC 3.2.1.22; alpha-Gal A) is the homodimeric glycoprotein that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins.
9620884	1	15	gly	glycoprotein	160:171	arg1	A					112:112	Human alpha-galactosidase A	86:112	Human alpha-galactosidase A (EC 3.2.1.22; alpha-Gal A)	86:139	Human alpha-galactosidase A (EC 3.2.1.22; alpha-Gal A) is the homodimeric glycoprotein that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins.
9620884	9	16	theme	H-treated	1614:1622	arg1	enzyme					1624:1629	endoglycosidase H-treated enzyme	1598:1629	endoglycosidase H-treated enzyme	1598:1629	In support of this concept, endoglycosidase H-treated enzyme or mannose-terminated enzyme expressed in Autographa californica cells also aggregated when concentrated, emphasizing that site 3 occupancy by a hybrid-type oligosaccharide was required for enzyme solubility.
9620884	3	17	theme	sequences	571:579	arg1	three					486:490	three	486:490	three	486:490	Endoglycosidase treatment of the purified recombinant enzyme and mutagenesis studies indicated that three (Asn-139, Asn-192 and Asn-215) of the four potential N-glycosylation consensus sequences were occupied by complex, high-mannose and hybrid-type oligosaccharides respectively.
9620884	3	17	theme	sequences	571:579	arg1	sequences					571:579	the four potential N-glycosylation consensus sequences	526:579	the four potential N-glycosylation consensus sequences	526:579	Endoglycosidase treatment of the purified recombinant enzyme and mutagenesis studies indicated that three (Asn-139, Asn-192 and Asn-215) of the four potential N-glycosylation consensus sequences were occupied by complex, high-mannose and hybrid-type oligosaccharides respectively.
9620884	6	18	theme	Expressed	953:961	arg1	glycoforms					970:979	Expressed mutant glycoforms	953:979	Expressed mutant glycoforms in which site 3 and site 1 or 2 were obliterated	953:1028	Expressed mutant glycoforms in which site 3 and site 1 or 2 were obliterated had little, if any, intracellular or secreted enzymic activity, and immunofluorescence microscopy revealed that the expressed mutant glycoforms were retained in the endoplasmic reticulum, presumably where they were degraded.
9620884	9	19	theme	californica	1684:1694	arg1	cells					1696:1700	Autographa californica cells	1673:1700	Autographa californica cells	1673:1700	In support of this concept, endoglycosidase H-treated enzyme or mannose-terminated enzyme expressed in Autographa californica cells also aggregated when concentrated, emphasizing that site 3 occupancy by a hybrid-type oligosaccharide was required for enzyme solubility.
9620884	2	20	theme	site	274:277	arg1	occupancy					279:287	site occupancy	274:287	site occupancy	274:287	The type, site occupancy and function of the N-linked oligosaccharide chains on this lysosomal hydrolase were determined.
9620884	7	21	dep	soluble	1316:1322	arg1	active					1325:1330	active	1325:1330	active	1325:1330	Thus glycosylation at site 3 was crucial to the formation of soluble, active enzyme, as well as transport to the lysosome.
9620884	9	22	theme	enzyme	1821:1826	arg1	solubility					1828:1837	enzyme solubility	1821:1837	enzyme solubility	1821:1837	In support of this concept, endoglycosidase H-treated enzyme or mannose-terminated enzyme expressed in Autographa californica cells also aggregated when concentrated, emphasizing that site 3 occupancy by a hybrid-type oligosaccharide was required for enzyme solubility.
9620884	2	23	from	hydrolase	359:367	arg1	occupancy					279:287	site occupancy	274:287	site occupancy	274:287	The type, site occupancy and function of the N-linked oligosaccharide chains on this lysosomal hydrolase were determined.
9620884	2	23	from	hydrolase	359:367	arg1	function					293:300	function	293:300	function	293:300	The type, site occupancy and function of the N-linked oligosaccharide chains on this lysosomal hydrolase were determined.
9620884	2	23	from	hydrolase	359:367	arg1	type					268:271	The type	264:271	The type	264:271	The type, site occupancy and function of the N-linked oligosaccharide chains on this lysosomal hydrolase were determined.
9620884	1	24	dep	EC	115:116	arg1	A					138:138	alpha-Gal A	128:138	EC 3.2.1.22; alpha-Gal A	115:138	Human alpha-galactosidase A (EC 3.2.1.22; alpha-Gal A) is the homodimeric glycoprotein that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins.
9620884	1	25	theme	homodimeric	148:158	arg1	glycoprotein					160:171	the homodimeric glycoprotein	144:171	the homodimeric glycoprotein that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins	144:261	Human alpha-galactosidase A (EC 3.2.1.22; alpha-Gal A) is the homodimeric glycoprotein that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins.
9620884	1	25	theme	homodimeric	148:158	arg1	A					112:112	Human alpha-galactosidase A	86:112	Human alpha-galactosidase A (EC 3.2.1.22; alpha-Gal A)	86:139	Human alpha-galactosidase A (EC 3.2.1.22; alpha-Gal A) is the homodimeric glycoprotein that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins.
9620884	0	26	theme	alpha-galactosidase	6:24	arg1	A					26:26	Human alpha-galactosidase A	0:26	Human alpha-galactosidase A: glycosylation site 3	0:48	Human alpha-galactosidase A: glycosylation site 3 is essential for enzyme solubility.
9620884	8	27	theme	polypeptide	1528:1538	arg1	aggregation					1502:1512	aggregation	1502:1512	aggregation of the enzyme polypeptide in the endoplasmic reticulum	1502:1567	Absence of the site 3 hybrid-type oligosaccharide exposed an adjacent, normally protected, hydrophobic region, resulting in aggregation of the enzyme polypeptide in the endoplasmic reticulum.
9620884	1	28	gly	glycoproteins	249:261	arg1	glycoproteins					249:261	glycoproteins	249:261	glycoproteins	249:261	Human alpha-galactosidase A (EC 3.2.1.22; alpha-Gal A) is the homodimeric glycoprotein that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins.
9620884	2	29	theme	N-linked	309:316	arg1	chains					334:339	the N-linked oligosaccharide chains	305:339	the N-linked oligosaccharide chains on this lysosomal hydrolase	305:367	The type, site occupancy and function of the N-linked oligosaccharide chains on this lysosomal hydrolase were determined.
9620884	4	30	theme	glycosylation	714:726	arg1	site					728:731	glycosylation site 1 or 2	714:738	site	728:731	When expressed in COS-1 cells, glycoforms with glycosylation site 1 or 2 obliterated had more than 70% of wild-type activity, and both glycoforms were secreted.
9620884	0	31	theme	Human	0:4	arg1	A					26:26	Human alpha-galactosidase A	0:26	Human alpha-galactosidase A: glycosylation site 3	0:48	Human alpha-galactosidase A: glycosylation site 3 is essential for enzyme solubility.
9620884	9	32	theme	Autographa	1673:1682	arg1	cells					1696:1700	Autographa californica cells	1673:1700	Autographa californica cells	1673:1700	In support of this concept, endoglycosidase H-treated enzyme or mannose-terminated enzyme expressed in Autographa californica cells also aggregated when concentrated, emphasizing that site 3 occupancy by a hybrid-type oligosaccharide was required for enzyme solubility.
9620884	8	33	theme	oligosaccharide	1412:1426	arg1	Absence					1378:1384	Absence	1378:1384	Absence of the site 3 hybrid-type oligosaccharide	1378:1426	Absence of the site 3 hybrid-type oligosaccharide exposed an adjacent, normally protected, hydrophobic region, resulting in aggregation of the enzyme polypeptide in the endoplasmic reticulum.
9620884	1	34	theme	Human	86:90	arg1	glycoprotein					160:171	the homodimeric glycoprotein	144:171	the homodimeric glycoprotein that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins	144:261	Human alpha-galactosidase A (EC 3.2.1.22; alpha-Gal A) is the homodimeric glycoprotein that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins.
9620884	1	34	theme	Human	86:90	arg1	A					112:112	Human alpha-galactosidase A	86:112	Human alpha-galactosidase A (EC 3.2.1.22; alpha-Gal A)	86:139	Human alpha-galactosidase A (EC 3.2.1.22; alpha-Gal A) is the homodimeric glycoprotein that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins.
9620884	3	35	theme	mutagenesis	451:461	arg1	studies					463:469	mutagenesis studies	451:469	mutagenesis studies	451:469	Endoglycosidase treatment of the purified recombinant enzyme and mutagenesis studies indicated that three (Asn-139, Asn-192 and Asn-215) of the four potential N-glycosylation consensus sequences were occupied by complex, high-mannose and hybrid-type oligosaccharides respectively.
9620884	9	36	theme	site	1754:1757	arg1	occupancy					1761:1769	site 3 occupancy	1754:1769	site 3 occupancy by a hybrid-type oligosaccharide	1754:1802	In support of this concept, endoglycosidase H-treated enzyme or mannose-terminated enzyme expressed in Autographa californica cells also aggregated when concentrated, emphasizing that site 3 occupancy by a hybrid-type oligosaccharide was required for enzyme solubility.
9620884	9	37	theme	hybrid-type	1776:1786	arg1	oligosaccharide					1788:1802	a hybrid-type oligosaccharide	1774:1802	a hybrid-type oligosaccharide	1774:1802	In support of this concept, endoglycosidase H-treated enzyme or mannose-terminated enzyme expressed in Autographa californica cells also aggregated when concentrated, emphasizing that site 3 occupancy by a hybrid-type oligosaccharide was required for enzyme solubility.
9620884	1	38	theme	alpha-galactosidase	92:110	arg1	glycoprotein					160:171	the homodimeric glycoprotein	144:171	the homodimeric glycoprotein that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins	144:261	Human alpha-galactosidase A (EC 3.2.1.22; alpha-Gal A) is the homodimeric glycoprotein that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins.
9620884	1	38	theme	alpha-galactosidase	92:110	arg1	A					112:112	Human alpha-galactosidase A	86:112	Human alpha-galactosidase A (EC 3.2.1.22; alpha-Gal A)	86:139	Human alpha-galactosidase A (EC 3.2.1.22; alpha-Gal A) is the homodimeric glycoprotein that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins.
9620884	7	39	theme	enzyme	1332:1337	arg1	formation					1303:1311	the formation	1299:1311	the formation of soluble, active enzyme	1299:1337	Thus glycosylation at site 3 was crucial to the formation of soluble, active enzyme, as well as transport to the lysosome.
9620884	3	40	used	occupied	586:593	arg2	three					486:490	three	486:490	three	486:490	Endoglycosidase treatment of the purified recombinant enzyme and mutagenesis studies indicated that three (Asn-139, Asn-192 and Asn-215) of the four potential N-glycosylation consensus sequences were occupied by complex, high-mannose and hybrid-type oligosaccharides respectively.
9620884	3	40	used	occupied	586:593	arg2	sequences					571:579	the four potential N-glycosylation consensus sequences	526:579	the four potential N-glycosylation consensus sequences	526:579	Endoglycosidase treatment of the purified recombinant enzyme and mutagenesis studies indicated that three (Asn-139, Asn-192 and Asn-215) of the four potential N-glycosylation consensus sequences were occupied by complex, high-mannose and hybrid-type oligosaccharides respectively.
9620884	3	41	theme	Endoglycosidase	386:400	arg1	treatment					402:410	Endoglycosidase treatment	386:410	Endoglycosidase treatment of the purified recombinant enzyme	386:445	Endoglycosidase treatment of the purified recombinant enzyme and mutagenesis studies indicated that three (Asn-139, Asn-192 and Asn-215) of the four potential N-glycosylation consensus sequences were occupied by complex, high-mannose and hybrid-type oligosaccharides respectively.
9620884	3	42	theme	potential	535:543	arg1	sequences					571:579	the four potential N-glycosylation consensus sequences	526:579	the four potential N-glycosylation consensus sequences	526:579	Endoglycosidase treatment of the purified recombinant enzyme and mutagenesis studies indicated that three (Asn-139, Asn-192 and Asn-215) of the four potential N-glycosylation consensus sequences were occupied by complex, high-mannose and hybrid-type oligosaccharides respectively.
9620884	4	43	dep	obliterated	740:750	arg1	had					752:754	had	752:754	obliterated had more than 70% of wild-type activity	740:790	When expressed in COS-1 cells, glycoforms with glycosylation site 1 or 2 obliterated had more than 70% of wild-type activity, and both glycoforms were secreted.
9620884	2	44	from	type	268:271	arg1	hydrolase					359:367	this lysosomal hydrolase	344:367	this lysosomal hydrolase	344:367	The type, site occupancy and function of the N-linked oligosaccharide chains on this lysosomal hydrolase were determined.
9620884	7	45	theme	soluble	1316:1322	arg1	enzyme					1332:1337	soluble, active enzyme	1316:1337	soluble, active enzyme	1316:1337	Thus glycosylation at site 3 was crucial to the formation of soluble, active enzyme, as well as transport to the lysosome.
9620884	3	46	theme	recombinant	428:438	arg1	enzyme					440:445	the purified recombinant enzyme	415:445	the purified recombinant enzyme	415:445	Endoglycosidase treatment of the purified recombinant enzyme and mutagenesis studies indicated that three (Asn-139, Asn-192 and Asn-215) of the four potential N-glycosylation consensus sequences were occupied by complex, high-mannose and hybrid-type oligosaccharides respectively.
9620884	6	47	theme	secreted	1067:1074	arg1	activity					1084:1091	intracellular or secreted enzymic activity	1050:1091	intracellular or secreted enzymic activity	1050:1091	Expressed mutant glycoforms in which site 3 and site 1 or 2 were obliterated had little, if any, intracellular or secreted enzymic activity, and immunofluorescence microscopy revealed that the expressed mutant glycoforms were retained in the endoplasmic reticulum, presumably where they were degraded.
9620884	1	48	from	glycoproteins	249:261	arg1	moieties					219:226	the terminal alpha-galactosyl moieties	189:226	the terminal alpha-galactosyl moieties from glycolipids and glycoproteins	189:261	Human alpha-galactosidase A (EC 3.2.1.22; alpha-Gal A) is the homodimeric glycoprotein that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins.
9620884	9	49	theme	mannose-terminated	1634:1651	arg1	enzyme					1653:1658	mannose-terminated enzyme	1634:1658	mannose-terminated enzyme	1634:1658	In support of this concept, endoglycosidase H-treated enzyme or mannose-terminated enzyme expressed in Autographa californica cells also aggregated when concentrated, emphasizing that site 3 occupancy by a hybrid-type oligosaccharide was required for enzyme solubility.
9620884	6	50	theme	endoplasmic	1195:1205	arg1	reticulum					1207:1215	the endoplasmic reticulum	1191:1215	the endoplasmic reticulum	1191:1215	Expressed mutant glycoforms in which site 3 and site 1 or 2 were obliterated had little, if any, intracellular or secreted enzymic activity, and immunofluorescence microscopy revealed that the expressed mutant glycoforms were retained in the endoplasmic reticulum, presumably where they were degraded.
9620884	5	51	theme	decreased	887:895	arg1	%					919:919	less than 40%	907:919	less than 40%	907:919	In contrast, the glycoform with only site 3 eliminated had decreased activity (less than 40%); little, if any, was secreted.
9620884	5	51	theme	decreased	887:895	arg1	activity					897:904	decreased activity	887:904	decreased activity (less than 40%);	887:921	In contrast, the glycoform with only site 3 eliminated had decreased activity (less than 40%); little, if any, was secreted.
9620884	1	52	theme	terminal	193:200	arg1	moieties					219:226	the terminal alpha-galactosyl moieties	189:226	the terminal alpha-galactosyl moieties from glycolipids and glycoproteins	189:261	Human alpha-galactosidase A (EC 3.2.1.22; alpha-Gal A) is the homodimeric glycoprotein that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins.
9620884	0	53	theme	glycosylation	29:41	arg1	site					43:46	glycosylation site 3	29:48	Human alpha-galactosidase A: glycosylation site 3	0:48	Human alpha-galactosidase A: glycosylation site 3 is essential for enzyme solubility.
9620884	3	54	theme	enzyme	440:445	arg1	treatment					402:410	Endoglycosidase treatment	386:410	Endoglycosidase treatment of the purified recombinant enzyme	386:445	Endoglycosidase treatment of the purified recombinant enzyme and mutagenesis studies indicated that three (Asn-139, Asn-192 and Asn-215) of the four potential N-glycosylation consensus sequences were occupied by complex, high-mannose and hybrid-type oligosaccharides respectively.
9620884	3	54	theme	enzyme	440:445	arg1	studies					463:469	mutagenesis studies	451:469	mutagenesis studies	451:469	Endoglycosidase treatment of the purified recombinant enzyme and mutagenesis studies indicated that three (Asn-139, Asn-192 and Asn-215) of the four potential N-glycosylation consensus sequences were occupied by complex, high-mannose and hybrid-type oligosaccharides respectively.
9620884	4	55	theme	activity	783:790	arg1	%					768:768	more than 70%	756:768	more than 70% of wild-type activity	756:790	When expressed in COS-1 cells, glycoforms with glycosylation site 1 or 2 obliterated had more than 70% of wild-type activity, and both glycoforms were secreted.
9620884	4	55	theme	activity	783:790	arg1	activity					783:790	wild-type activity	773:790	wild-type activity	773:790	When expressed in COS-1 cells, glycoforms with glycosylation site 1 or 2 obliterated had more than 70% of wild-type activity, and both glycoforms were secreted.
9620884	3	56	theme	hybrid-type	624:634	arg1	oligosaccharides					636:651	hybrid-type oligosaccharides	624:651	hybrid-type oligosaccharides respectively	624:664	Endoglycosidase treatment of the purified recombinant enzyme and mutagenesis studies indicated that three (Asn-139, Asn-192 and Asn-215) of the four potential N-glycosylation consensus sequences were occupied by complex, high-mannose and hybrid-type oligosaccharides respectively.
9620884	1	57	theme	alpha-galactosyl	202:217	arg1	moieties					219:226	the terminal alpha-galactosyl moieties	189:226	the terminal alpha-galactosyl moieties from glycolipids and glycoproteins	189:261	Human alpha-galactosidase A (EC 3.2.1.22; alpha-Gal A) is the homodimeric glycoprotein that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins.
9620884	1	58	from	glycolipids	233:243	arg1	moieties					219:226	the terminal alpha-galactosyl moieties	189:226	the terminal alpha-galactosyl moieties from glycolipids and glycoproteins	189:261	Human alpha-galactosidase A (EC 3.2.1.22; alpha-Gal A) is the homodimeric glycoprotein that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins.
9620884	6	59	theme	enzymic	1076:1082	arg1	activity					1084:1091	intracellular or secreted enzymic activity	1050:1091	intracellular or secreted enzymic activity	1050:1091	Expressed mutant glycoforms in which site 3 and site 1 or 2 were obliterated had little, if any, intracellular or secreted enzymic activity, and immunofluorescence microscopy revealed that the expressed mutant glycoforms were retained in the endoplasmic reticulum, presumably where they were degraded.
9620884	3	60	theme	purified	419:426	arg1	enzyme					440:445	the purified recombinant enzyme	415:445	the purified recombinant enzyme	415:445	Endoglycosidase treatment of the purified recombinant enzyme and mutagenesis studies indicated that three (Asn-139, Asn-192 and Asn-215) of the four potential N-glycosylation consensus sequences were occupied by complex, high-mannose and hybrid-type oligosaccharides respectively.
9620884	2	61	link	N-linked	309:316	arg1	chains					334:339	the N-linked oligosaccharide chains	305:339	the N-linked oligosaccharide chains on this lysosomal hydrolase	305:367	The type, site occupancy and function of the N-linked oligosaccharide chains on this lysosomal hydrolase were determined.
9620884	8	62	theme	hybrid-type	1400:1410	arg1	oligosaccharide					1412:1426	the site 3 hybrid-type oligosaccharide	1389:1426	the site 3 hybrid-type oligosaccharide	1389:1426	Absence of the site 3 hybrid-type oligosaccharide exposed an adjacent, normally protected, hydrophobic region, resulting in aggregation of the enzyme polypeptide in the endoplasmic reticulum.
9620884	5	63	dep	eliminated	872:881	arg1	had					883:885	had	883:885	eliminated had decreased activity (less than 40%); little, if any	872:936	In contrast, the glycoform with only site 3 eliminated had decreased activity (less than 40%); little, if any, was secreted.
9620884	9	64	theme	endoglycosidase	1598:1612	arg1	enzyme					1624:1629	endoglycosidase H-treated enzyme	1598:1629	endoglycosidase H-treated enzyme	1598:1629	In support of this concept, endoglycosidase H-treated enzyme or mannose-terminated enzyme expressed in Autographa californica cells also aggregated when concentrated, emphasizing that site 3 occupancy by a hybrid-type oligosaccharide was required for enzyme solubility.
9620884	4	65	with	glycoforms	698:707	arg1	site					728:731	glycosylation site 1 or 2	714:738	site	728:731	When expressed in COS-1 cells, glycoforms with glycosylation site 1 or 2 obliterated had more than 70% of wild-type activity, and both glycoforms were secreted.
9620884	4	65	with	glycoforms	698:707	arg1	2					738:738	2	738:738	2	738:738	When expressed in COS-1 cells, glycoforms with glycosylation site 1 or 2 obliterated had more than 70% of wild-type activity, and both glycoforms were secreted.
9620884	6	66	theme	expressed	1146:1154	arg1	glycoforms					1163:1172	the expressed mutant glycoforms	1142:1172	the expressed mutant glycoforms	1142:1172	Expressed mutant glycoforms in which site 3 and site 1 or 2 were obliterated had little, if any, intracellular or secreted enzymic activity, and immunofluorescence microscopy revealed that the expressed mutant glycoforms were retained in the endoplasmic reticulum, presumably where they were degraded.
9620884	0	67	gly	glycosylation	29:41	arg2	site					43:46	glycosylation site 3	29:48	Human alpha-galactosidase A: glycosylation site 3	0:48	Human alpha-galactosidase A: glycosylation site 3 is essential for enzyme solubility.
9620884	0	67	gly	glycosylation	29:41	arg2	3					48:48	3	48:48	3	48:48	Human alpha-galactosidase A: glycosylation site 3 is essential for enzyme solubility.
9620884	7	68	from	site	1277:1280	arg1	glycosylation					1260:1272	glycosylation	1260:1272	glycosylation at site 3	1260:1282	Thus glycosylation at site 3 was crucial to the formation of soluble, active enzyme, as well as transport to the lysosome.
9620884	2	69	theme	chains	334:339	arg1	occupancy					279:287	site occupancy	274:287	site occupancy	274:287	The type, site occupancy and function of the N-linked oligosaccharide chains on this lysosomal hydrolase were determined.
9620884	2	69	theme	chains	334:339	arg1	function					293:300	function	293:300	function	293:300	The type, site occupancy and function of the N-linked oligosaccharide chains on this lysosomal hydrolase were determined.
9620884	2	69	theme	chains	334:339	arg1	type					268:271	The type	264:271	The type	264:271	The type, site occupancy and function of the N-linked oligosaccharide chains on this lysosomal hydrolase were determined.
9620884	4	70	theme	wild-type	773:781	arg1	activity					783:790	wild-type activity	773:790	wild-type activity	773:790	When expressed in COS-1 cells, glycoforms with glycosylation site 1 or 2 obliterated had more than 70% of wild-type activity, and both glycoforms were secreted.
9620884	3	71	theme	N-glycosylation	545:559	arg1	sequences					571:579	the four potential N-glycosylation consensus sequences	526:579	the four potential N-glycosylation consensus sequences	526:579	Endoglycosidase treatment of the purified recombinant enzyme and mutagenesis studies indicated that three (Asn-139, Asn-192 and Asn-215) of the four potential N-glycosylation consensus sequences were occupied by complex, high-mannose and hybrid-type oligosaccharides respectively.
9620884	0	72	dep	A	26:26	arg1	site					43:46	glycosylation site 3	29:48	Human alpha-galactosidase A: glycosylation site 3	0:48	Human alpha-galactosidase A: glycosylation site 3 is essential for enzyme solubility.
9620884	2	73	theme	oligosaccharide	318:332	arg1	chains					334:339	the N-linked oligosaccharide chains	305:339	the N-linked oligosaccharide chains on this lysosomal hydrolase	305:367	The type, site occupancy and function of the N-linked oligosaccharide chains on this lysosomal hydrolase were determined.
9620884	8	74	theme	site	1393:1396	arg1	oligosaccharide					1412:1426	the site 3 hybrid-type oligosaccharide	1389:1426	the site 3 hybrid-type oligosaccharide	1389:1426	Absence of the site 3 hybrid-type oligosaccharide exposed an adjacent, normally protected, hydrophobic region, resulting in aggregation of the enzyme polypeptide in the endoplasmic reticulum.
9620884	4	75	theme	COS-1	685:689	arg1	cells					691:695	COS-1 cells	685:695	COS-1 cells	685:695	When expressed in COS-1 cells, glycoforms with glycosylation site 1 or 2 obliterated had more than 70% of wild-type activity, and both glycoforms were secreted.
9620884	6	76	theme	mutant	1156:1161	arg1	glycoforms					1163:1172	the expressed mutant glycoforms	1142:1172	the expressed mutant glycoforms	1142:1172	Expressed mutant glycoforms in which site 3 and site 1 or 2 were obliterated had little, if any, intracellular or secreted enzymic activity, and immunofluorescence microscopy revealed that the expressed mutant glycoforms were retained in the endoplasmic reticulum, presumably where they were degraded.
9620884	1	77	theme	alpha-Gal	128:136	arg1	A					138:138	alpha-Gal A	128:138	EC 3.2.1.22; alpha-Gal A	115:138	Human alpha-galactosidase A (EC 3.2.1.22; alpha-Gal A) is the homodimeric glycoprotein that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins.
9620884	2	78	from	occupancy	279:287	arg1	hydrolase					359:367	this lysosomal hydrolase	344:367	this lysosomal hydrolase	344:367	The type, site occupancy and function of the N-linked oligosaccharide chains on this lysosomal hydrolase were determined.
9620884	8	79	dep	adjacent	1439:1446	arg1	hydrophobic					1469:1479	hydrophobic	1469:1479	hydrophobic	1469:1479	Absence of the site 3 hybrid-type oligosaccharide exposed an adjacent, normally protected, hydrophobic region, resulting in aggregation of the enzyme polypeptide in the endoplasmic reticulum.
9620884	8	79	dep	adjacent	1439:1446	arg1	protected					1458:1466	protected	1458:1466	protected	1458:1466	Absence of the site 3 hybrid-type oligosaccharide exposed an adjacent, normally protected, hydrophobic region, resulting in aggregation of the enzyme polypeptide in the endoplasmic reticulum.
9620884	8	80	theme	adjacent	1439:1446	arg1	region					1481:1486	an adjacent, normally protected, hydrophobic region	1436:1486	an adjacent, normally protected, hydrophobic region	1436:1486	Absence of the site 3 hybrid-type oligosaccharide exposed an adjacent, normally protected, hydrophobic region, resulting in aggregation of the enzyme polypeptide in the endoplasmic reticulum.
9620884	6	81	theme	intracellular	1050:1062	arg1	activity					1084:1091	intracellular or secreted enzymic activity	1050:1091	intracellular or secreted enzymic activity	1050:1091	Expressed mutant glycoforms in which site 3 and site 1 or 2 were obliterated had little, if any, intracellular or secreted enzymic activity, and immunofluorescence microscopy revealed that the expressed mutant glycoforms were retained in the endoplasmic reticulum, presumably where they were degraded.
9620884	1	82	dep	A	112:112	arg1	EC					115:116	EC 3.2.1.22	115:125	EC 3.2.1.22; alpha-Gal A	115:138	Human alpha-galactosidase A (EC 3.2.1.22; alpha-Gal A) is the homodimeric glycoprotein that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins.
9620884	8	83	theme	endoplasmic	1547:1557	arg1	reticulum					1559:1567	the endoplasmic reticulum	1543:1567	the endoplasmic reticulum	1543:1567	Absence of the site 3 hybrid-type oligosaccharide exposed an adjacent, normally protected, hydrophobic region, resulting in aggregation of the enzyme polypeptide in the endoplasmic reticulum.
28808029	4	0	theme	generic	495:501	arg1	mechanisms					513:522	two generic crosstalk mechanisms	491:522	two generic crosstalk mechanisms	491:522	We demonstrate two generic crosstalk mechanisms.
28808029	6	1	theme	substrates	888:897	arg1	hundreds					840:847	hundreds	840:847	hundreds of putative O-GlcNAc transferase (OGT) substrates	840:897	Strikingly, this stringent motif is substantially enriched in the human (phospho)proteome, allowing us to predict hundreds of putative O-GlcNAc transferase (OGT) substrates.
28808029	5	2	theme	phosphorylation/O-GlcNAcylation	594:624	arg1	P					650:650	(pSp/T)P	643:650	(pSp/T)P(V/A/T)(gS/gT)	643:664	First, we define a frequently occurring, very specific and stringent phosphorylation/O-GlcNAcylation interplay motif, (pSp/T)P(V/A/T)(gS/gT), whereby phosphorylation strongly inhibits O-GlcNAcylation.
28808029	5	2	theme	phosphorylation/O-GlcNAcylation	594:624	arg1	motif					636:640	a frequently occurring, very specific and stringent phosphorylation/O-GlcNAcylation interplay motif	542:640	a frequently occurring, very specific and stringent phosphorylation/O-GlcNAcylation interplay motif	542:640	First, we define a frequently occurring, very specific and stringent phosphorylation/O-GlcNAcylation interplay motif, (pSp/T)P(V/A/T)(gS/gT), whereby phosphorylation strongly inhibits O-GlcNAcylation.
28808029	7	3	dep	these	909:913	arg1	we					915:916	we	915:916	we	915:916	A set of these we investigate further and show them to be decent substrates of OGT, exhibiting a negative feedback loop when phosphorylated at the P-3 site.
28808029	3	4	theme	spectrometry-based	336:353	arg1	assays					355:360	mass spectrometry-based assays	331:360	mass spectrometry-based assays	331:360	Here, using mass spectrometry-based assays, we focus on the most common PTMs-phosphorylation and O-GlcNAcylation-and investigate how they affect each other.
28808029	5	5	theme	interplay	626:634	arg1	P					650:650	(pSp/T)P	643:650	(pSp/T)P(V/A/T)(gS/gT)	643:664	First, we define a frequently occurring, very specific and stringent phosphorylation/O-GlcNAcylation interplay motif, (pSp/T)P(V/A/T)(gS/gT), whereby phosphorylation strongly inhibits O-GlcNAcylation.
28808029	5	5	theme	interplay	626:634	arg1	motif					636:640	a frequently occurring, very specific and stringent phosphorylation/O-GlcNAcylation interplay motif	542:640	a frequently occurring, very specific and stringent phosphorylation/O-GlcNAcylation interplay motif	542:640	First, we define a frequently occurring, very specific and stringent phosphorylation/O-GlcNAcylation interplay motif, (pSp/T)P(V/A/T)(gS/gT), whereby phosphorylation strongly inhibits O-GlcNAcylation.
28808029	2	6	theme	molecular	300:308	arg1	biology					310:316	molecular biology	300:316	molecular biology	300:316	Unraveling this complex PTM code is one of the great challenges in molecular biology.
28808029	6	7	theme	phospho	799:805	arg1	proteome					807:814	the human (phospho)proteome	788:814	the human (phospho)proteome	788:814	Strikingly, this stringent motif is substantially enriched in the human (phospho)proteome, allowing us to predict hundreds of putative O-GlcNAc transferase (OGT) substrates.
28808029	8	8	theme	vertebrate	1239:1248	arg1	phosphoproteomes					1250:1265	the vertebrate phosphoproteomes	1235:1265	the vertebrate phosphoproteomes	1235:1265	Second, we demonstrate that reciprocal crosstalk does not occur at PX(S/T)P sites, i.e., at sites phosphorylated by proline-directed kinases, which represent 40% of all sites in the vertebrate phosphoproteomes.
28808029	5	9	dep	occurring	555:563	arg1	stringent					584:592	stringent	584:592	stringent	584:592	First, we define a frequently occurring, very specific and stringent phosphorylation/O-GlcNAcylation interplay motif, (pSp/T)P(V/A/T)(gS/gT), whereby phosphorylation strongly inhibits O-GlcNAcylation.
28808029	5	9	dep	occurring	555:563	arg1	specific					571:578	specific	571:578	specific	571:578	First, we define a frequently occurring, very specific and stringent phosphorylation/O-GlcNAcylation interplay motif, (pSp/T)P(V/A/T)(gS/gT), whereby phosphorylation strongly inhibits O-GlcNAcylation.
28808029	8	10	theme	PX	1124:1125	arg1	sites					1133:1137	PX(S/T)P sites	1124:1137	PX(S/T)P sites	1124:1137	Second, we demonstrate that reciprocal crosstalk does not occur at PX(S/T)P sites, i.e., at sites phosphorylated by proline-directed kinases, which represent 40% of all sites in the vertebrate phosphoproteomes.
28808029	8	11	theme	proline-directed	1173:1188	arg1	kinases					1190:1196	proline-directed kinases	1173:1196	proline-directed kinases	1173:1196	Second, we demonstrate that reciprocal crosstalk does not occur at PX(S/T)P sites, i.e., at sites phosphorylated by proline-directed kinases, which represent 40% of all sites in the vertebrate phosphoproteomes.
28808029	6	12	theme	transferase	870:880	arg1	substrates					888:897	putative O-GlcNAc transferase (OGT) substrates	852:897	putative O-GlcNAc transferase (OGT) substrates	852:897	Strikingly, this stringent motif is substantially enriched in the human (phospho)proteome, allowing us to predict hundreds of putative O-GlcNAc transferase (OGT) substrates.
28808029	5	13	theme	pSp/T	644:648	arg1	V/A/T					652:656	V/A/T	652:656	V/A/T	652:656	First, we define a frequently occurring, very specific and stringent phosphorylation/O-GlcNAcylation interplay motif, (pSp/T)P(V/A/T)(gS/gT), whereby phosphorylation strongly inhibits O-GlcNAcylation.
28808029	5	13	theme	pSp/T	644:648	arg1	gS/gT					659:663	gS/gT	659:663	gS/gT	659:663	First, we define a frequently occurring, very specific and stringent phosphorylation/O-GlcNAcylation interplay motif, (pSp/T)P(V/A/T)(gS/gT), whereby phosphorylation strongly inhibits O-GlcNAcylation.
28808029	5	13	theme	pSp/T	644:648	arg1	P					650:650	(pSp/T)P	643:650	(pSp/T)P(V/A/T)(gS/gT)	643:664	First, we define a frequently occurring, very specific and stringent phosphorylation/O-GlcNAcylation interplay motif, (pSp/T)P(V/A/T)(gS/gT), whereby phosphorylation strongly inhibits O-GlcNAcylation.
28808029	5	13	theme	pSp/T	644:648	arg1	motif					636:640	a frequently occurring, very specific and stringent phosphorylation/O-GlcNAcylation interplay motif	542:640	a frequently occurring, very specific and stringent phosphorylation/O-GlcNAcylation interplay motif	542:640	First, we define a frequently occurring, very specific and stringent phosphorylation/O-GlcNAcylation interplay motif, (pSp/T)P(V/A/T)(gS/gT), whereby phosphorylation strongly inhibits O-GlcNAcylation.
28808029	6	14	theme	human	792:796	arg1	proteome					807:814	the human (phospho)proteome	788:814	the human (phospho)proteome	788:814	Strikingly, this stringent motif is substantially enriched in the human (phospho)proteome, allowing us to predict hundreds of putative O-GlcNAc transferase (OGT) substrates.
28808029	0	15	theme	crosstalk	12:20	arg1	mechanisms					22:31	crosstalk mechanisms	12:31	crosstalk mechanisms between phosphorylation and O-GlcNAcylation	12:75	Elucidating crosstalk mechanisms between phosphorylation and O-GlcNAcylation.
28808029	6	16	theme	O-GlcNAc	861:868	arg1	OGT					883:885	OGT	883:885	OGT	883:885	Strikingly, this stringent motif is substantially enriched in the human (phospho)proteome, allowing us to predict hundreds of putative O-GlcNAc transferase (OGT) substrates.
28808029	6	16	theme	O-GlcNAc	861:868	arg1	transferase					870:880	O-GlcNAc transferase	861:880	putative O-GlcNAc transferase (OGT) substrates	852:897	Strikingly, this stringent motif is substantially enriched in the human (phospho)proteome, allowing us to predict hundreds of putative O-GlcNAc transferase (OGT) substrates.
28808029	1	17	dep	PTM	166:168	arg1	code					170:173	code	170:173	code	170:173	Proteins can be modified by multiple posttranslational modifications (PTMs), creating a PTM code that controls the function of proteins in space and time.
28808029	3	18	dep	PTMs-phosphorylation	391:410	arg1	investigate					436:446	investigate	436:446	investigate how they affect each other	436:473	Here, using mass spectrometry-based assays, we focus on the most common PTMs-phosphorylation and O-GlcNAcylation-and investigate how they affect each other.
28808029	1	19	theme	multiple	106:113	arg1	PTMs					148:151	PTMs	148:151	PTMs	148:151	Proteins can be modified by multiple posttranslational modifications (PTMs), creating a PTM code that controls the function of proteins in space and time.
28808029	1	19	theme	multiple	106:113	arg1	modifications					133:145	multiple posttranslational modifications	106:145	multiple posttranslational modifications (PTMs)	106:152	Proteins can be modified by multiple posttranslational modifications (PTMs), creating a PTM code that controls the function of proteins in space and time.
28808029	8	20	theme	P	1131:1131	arg1	sites					1133:1137	PX(S/T)P sites	1124:1137	PX(S/T)P sites	1124:1137	Second, we demonstrate that reciprocal crosstalk does not occur at PX(S/T)P sites, i.e., at sites phosphorylated by proline-directed kinases, which represent 40% of all sites in the vertebrate phosphoproteomes.
28808029	2	21	theme	challenges	286:295	arg1	challenges					286:295	the great challenges	276:295	the great challenges in molecular biology	276:316	Unraveling this complex PTM code is one of the great challenges in molecular biology.
28808029	2	21	theme	challenges	286:295	arg1	one					269:271	one	269:271	one	269:271	Unraveling this complex PTM code is one of the great challenges in molecular biology.
28808029	7	22	theme	decent	958:963	arg1	substrates					965:974	decent substrates	958:974	decent substrates of OGT	958:981	A set of these we investigate further and show them to be decent substrates of OGT, exhibiting a negative feedback loop when phosphorylated at the P-3 site.
28808029	6	23	theme	putative	852:859	arg1	substrates					888:897	putative O-GlcNAc transferase (OGT) substrates	852:897	putative O-GlcNAc transferase (OGT) substrates	852:897	Strikingly, this stringent motif is substantially enriched in the human (phospho)proteome, allowing us to predict hundreds of putative O-GlcNAc transferase (OGT) substrates.
28808029	2	24	theme	great	280:284	arg1	challenges					286:295	the great challenges	276:295	the great challenges in molecular biology	276:316	Unraveling this complex PTM code is one of the great challenges in molecular biology.
28808029	1	25	theme	proteins	205:212	arg1	function					193:200	the function	189:200	the function of proteins in space and time	189:230	Proteins can be modified by multiple posttranslational modifications (PTMs), creating a PTM code that controls the function of proteins in space and time.
28808029	3	26	theme	common	384:389	arg1	PTMs-phosphorylation					391:410	PTMs-phosphorylation	391:410	PTMs-phosphorylation	391:410	Here, using mass spectrometry-based assays, we focus on the most common PTMs-phosphorylation and O-GlcNAcylation-and investigate how they affect each other.
28808029	1	27	mod	modified	94:101	arg3	modifications					133:145	multiple posttranslational modifications	106:145	multiple posttranslational modifications (PTMs)	106:152	Proteins can be modified by multiple posttranslational modifications (PTMs), creating a PTM code that controls the function of proteins in space and time.
28808029	1	27	mod	modified	94:101	arg1	Proteins					78:85	Proteins	78:85	Proteins	78:85	Proteins can be modified by multiple posttranslational modifications (PTMs), creating a PTM code that controls the function of proteins in space and time.
28808029	1	27	mod	modified	94:101	arg3	PTMs					148:151	PTMs	148:151	PTMs	148:151	Proteins can be modified by multiple posttranslational modifications (PTMs), creating a PTM code that controls the function of proteins in space and time.
28808029	7	28	theme	OGT	979:981	arg1	substrates					965:974	decent substrates	958:974	decent substrates of OGT	958:981	A set of these we investigate further and show them to be decent substrates of OGT, exhibiting a negative feedback loop when phosphorylated at the P-3 site.
28808029	7	29	theme	negative	997:1004	arg1	loop					1015:1018	a negative feedback loop	995:1018	a negative feedback loop when phosphorylated at the P-3 site	995:1054	A set of these we investigate further and show them to be decent substrates of OGT, exhibiting a negative feedback loop when phosphorylated at the P-3 site.
28808029	7	30	theme	feedback	1006:1013	arg1	loop					1015:1018	a negative feedback loop	995:1018	a negative feedback loop when phosphorylated at the P-3 site	995:1054	A set of these we investigate further and show them to be decent substrates of OGT, exhibiting a negative feedback loop when phosphorylated at the P-3 site.
28808029	5	31	theme	occurring	555:563	arg1	P					650:650	(pSp/T)P	643:650	(pSp/T)P(V/A/T)(gS/gT)	643:664	First, we define a frequently occurring, very specific and stringent phosphorylation/O-GlcNAcylation interplay motif, (pSp/T)P(V/A/T)(gS/gT), whereby phosphorylation strongly inhibits O-GlcNAcylation.
28808029	5	31	theme	occurring	555:563	arg1	motif					636:640	a frequently occurring, very specific and stringent phosphorylation/O-GlcNAcylation interplay motif	542:640	a frequently occurring, very specific and stringent phosphorylation/O-GlcNAcylation interplay motif	542:640	First, we define a frequently occurring, very specific and stringent phosphorylation/O-GlcNAcylation interplay motif, (pSp/T)P(V/A/T)(gS/gT), whereby phosphorylation strongly inhibits O-GlcNAcylation.
28808029	7	32	theme	these	909:913	arg1	these					909:913	these	909:913	these	909:913	A set of these we investigate further and show them to be decent substrates of OGT, exhibiting a negative feedback loop when phosphorylated at the P-3 site.
28808029	7	32	theme	these	909:913	arg1	set					902:904	A set	900:904	A set of these we	900:916	A set of these we investigate further and show them to be decent substrates of OGT, exhibiting a negative feedback loop when phosphorylated at the P-3 site.
28808029	6	33	theme	stringent	743:751	arg1	motif					753:757	this stringent motif	738:757	this stringent motif	738:757	Strikingly, this stringent motif is substantially enriched in the human (phospho)proteome, allowing us to predict hundreds of putative O-GlcNAc transferase (OGT) substrates.
28808029	1	34	theme	posttranslational	115:131	arg1	PTMs					148:151	PTMs	148:151	PTMs	148:151	Proteins can be modified by multiple posttranslational modifications (PTMs), creating a PTM code that controls the function of proteins in space and time.
28808029	1	34	theme	posttranslational	115:131	arg1	modifications					133:145	multiple posttranslational modifications	106:145	multiple posttranslational modifications (PTMs)	106:152	Proteins can be modified by multiple posttranslational modifications (PTMs), creating a PTM code that controls the function of proteins in space and time.
28808029	7	35	theme	P-3	1047:1049	arg1	site					1051:1054	the P-3 site	1043:1054	the P-3 site	1043:1054	A set of these we investigate further and show them to be decent substrates of OGT, exhibiting a negative feedback loop when phosphorylated at the P-3 site.
28808029	8	36	theme	reciprocal	1085:1094	arg1	crosstalk					1096:1104	reciprocal crosstalk	1085:1104	reciprocal crosstalk	1085:1104	Second, we demonstrate that reciprocal crosstalk does not occur at PX(S/T)P sites, i.e., at sites phosphorylated by proline-directed kinases, which represent 40% of all sites in the vertebrate phosphoproteomes.
28808029	2	37	theme	complex	249:255	arg1	PTM					257:259	this complex PTM	244:259	this complex PTM	244:259	Unraveling this complex PTM code is one of the great challenges in molecular biology.
28808029	1	38	from	function	193:200	arg1	time					227:230	time	227:230	time	227:230	Proteins can be modified by multiple posttranslational modifications (PTMs), creating a PTM code that controls the function of proteins in space and time.
28808029	1	38	from	function	193:200	arg1	space					217:221	space	217:221	space	217:221	Proteins can be modified by multiple posttranslational modifications (PTMs), creating a PTM code that controls the function of proteins in space and time.
28808029	8	39	theme	sites	1226:1230	arg1	%					1217:1217	40%	1215:1217	40% of all sites	1215:1230	Second, we demonstrate that reciprocal crosstalk does not occur at PX(S/T)P sites, i.e., at sites phosphorylated by proline-directed kinases, which represent 40% of all sites in the vertebrate phosphoproteomes.
28808029	8	39	theme	sites	1226:1230	arg1	sites					1226:1230	all sites	1222:1230	all sites	1222:1230	Second, we demonstrate that reciprocal crosstalk does not occur at PX(S/T)P sites, i.e., at sites phosphorylated by proline-directed kinases, which represent 40% of all sites in the vertebrate phosphoproteomes.
28808029	4	40	theme	crosstalk	503:511	arg1	mechanisms					513:522	two generic crosstalk mechanisms	491:522	two generic crosstalk mechanisms	491:522	We demonstrate two generic crosstalk mechanisms.
28808029	8	41	theme	S/T	1127:1129	arg1	sites					1133:1137	PX(S/T)P sites	1124:1137	PX(S/T)P sites	1124:1137	Second, we demonstrate that reciprocal crosstalk does not occur at PX(S/T)P sites, i.e., at sites phosphorylated by proline-directed kinases, which represent 40% of all sites in the vertebrate phosphoproteomes.
28808029	2	42	from	challenges	286:295	arg1	biology					310:316	molecular biology	300:316	molecular biology	300:316	Unraveling this complex PTM code is one of the great challenges in molecular biology.
14970177	0	0	theme	herpesvirus-encoded	76:94	arg1	interleukin					115:125	Kaposi's sarcoma herpesvirus-encoded, but not cellular, interleukin 6	59:127	Kaposi's sarcoma herpesvirus-encoded, but not cellular, interleukin 6	59:127	N-linked glycosylation is required for optimal function of Kaposi's sarcoma herpesvirus-encoded, but not cellular, interleukin 6.
14970177	1	1	theme	sarcoma-associated	139:156	arg1	vIL-6					185:189	vIL-6	185:189	vIL-6	185:189	Kaposi's sarcoma-associated herpesvirus interleukin-6 (vIL-6) is a structural and functional homologue of the human cytokine IL-6 (hIL-6).
14970177	1	1	theme	sarcoma-associated	139:156	arg1	interleukin-6					170:182	Kaposi's sarcoma-associated herpesvirus interleukin-6	130:182	Kaposi's sarcoma-associated herpesvirus interleukin-6 (vIL-6)	130:190	Kaposi's sarcoma-associated herpesvirus interleukin-6 (vIL-6) is a structural and functional homologue of the human cytokine IL-6 (hIL-6).
14970177	1	1	theme	sarcoma-associated	139:156	arg1	homologue					223:231	a structural and functional homologue	195:231	a structural and functional homologue of the human cytokine IL-6 (hIL-6)	195:266	Kaposi's sarcoma-associated herpesvirus interleukin-6 (vIL-6) is a structural and functional homologue of the human cytokine IL-6 (hIL-6).
14970177	1	2	theme	human	240:244	arg1	hIL-6					261:265	hIL-6	261:265	hIL-6	261:265	Kaposi's sarcoma-associated herpesvirus interleukin-6 (vIL-6) is a structural and functional homologue of the human cytokine IL-6 (hIL-6).
14970177	1	2	theme	human	240:244	arg1	IL-6					255:258	the human cytokine IL-6	236:258	the human cytokine IL-6 (hIL-6)	236:266	Kaposi's sarcoma-associated herpesvirus interleukin-6 (vIL-6) is a structural and functional homologue of the human cytokine IL-6 (hIL-6).
14970177	2	3	theme	activator	437:445	arg1	pathway					474:480	signal transducer and activator of transcription (STAT)1/3 pathway	415:480	signal transducer and activator of transcription (STAT)1/3 pathway	415:480	hIL-6 and vIL-6 exhibit similar biological functions and both act via the gp130 receptor subunit to activate the Janus tyrosine kinase (JAK)1 and signal transducer and activator of transcription (STAT)1/3 pathway.
14970177	1	4	theme	herpesvirus	158:168	arg1	vIL-6					185:189	vIL-6	185:189	vIL-6	185:189	Kaposi's sarcoma-associated herpesvirus interleukin-6 (vIL-6) is a structural and functional homologue of the human cytokine IL-6 (hIL-6).
14970177	1	4	theme	herpesvirus	158:168	arg1	interleukin-6					170:182	Kaposi's sarcoma-associated herpesvirus interleukin-6	130:182	Kaposi's sarcoma-associated herpesvirus interleukin-6 (vIL-6)	130:190	Kaposi's sarcoma-associated herpesvirus interleukin-6 (vIL-6) is a structural and functional homologue of the human cytokine IL-6 (hIL-6).
14970177	1	4	theme	herpesvirus	158:168	arg1	homologue					223:231	a structural and functional homologue	195:231	a structural and functional homologue of the human cytokine IL-6 (hIL-6)	195:266	Kaposi's sarcoma-associated herpesvirus interleukin-6 (vIL-6) is a structural and functional homologue of the human cytokine IL-6 (hIL-6).
14970177	1	5	theme	cytokine	246:253	arg1	hIL-6					261:265	hIL-6	261:265	hIL-6	261:265	Kaposi's sarcoma-associated herpesvirus interleukin-6 (vIL-6) is a structural and functional homologue of the human cytokine IL-6 (hIL-6).
14970177	1	5	theme	cytokine	246:253	arg1	IL-6					255:258	the human cytokine IL-6	236:258	the human cytokine IL-6 (hIL-6)	236:266	Kaposi's sarcoma-associated herpesvirus interleukin-6 (vIL-6) is a structural and functional homologue of the human cytokine IL-6 (hIL-6).
14970177	4	6	theme	N-linked	840:847	arg1	glycosylation					862:874	neither N-linked nor O-linked glycosylation	832:874	neither N-linked nor O-linked glycosylation	832:874	Although hIL-6 is also N-glycosylated at N73 and multiply O-glycosylated, neither N-linked nor O-linked glycosylation is necessary for IL-6 receptor alpha-dependent binding to gp130 or signaling through JAK1-STAT1/3.
14970177	3	7	gly	glycosylation	577:589	arg2	N89					599:601	site N89	594:601	site N89 of vIL-6	594:610	Here we show that vIL-6 is N-linked glycosylated at N78 and N89 and demonstrate that N-linked glycosylation at site N89 of vIL-6 markedly enhances binding to gp130, signaling through the JAK1-STAT1/3 pathway and functions in a cytokine-dependent cell proliferation bioassay.
14970177	3	7	gly	glycosylation	577:589	arg1	N89					599:601	site N89	594:601	site N89 of vIL-6	594:610	Here we show that vIL-6 is N-linked glycosylated at N78 and N89 and demonstrate that N-linked glycosylation at site N89 of vIL-6 markedly enhances binding to gp130, signaling through the JAK1-STAT1/3 pathway and functions in a cytokine-dependent cell proliferation bioassay.
14970177	1	8	theme	IL-6	255:258	arg1	interleukin-6					170:182	Kaposi's sarcoma-associated herpesvirus interleukin-6	130:182	Kaposi's sarcoma-associated herpesvirus interleukin-6 (vIL-6)	130:190	Kaposi's sarcoma-associated herpesvirus interleukin-6 (vIL-6) is a structural and functional homologue of the human cytokine IL-6 (hIL-6).
14970177	1	8	theme	IL-6	255:258	arg1	homologue					223:231	a structural and functional homologue	195:231	a structural and functional homologue of the human cytokine IL-6 (hIL-6)	195:266	Kaposi's sarcoma-associated herpesvirus interleukin-6 (vIL-6) is a structural and functional homologue of the human cytokine IL-6 (hIL-6).
14970177	4	9	theme	alpha-dependent	907:921	arg1	binding					923:929	IL-6 receptor alpha-dependent binding	893:929	IL-6 receptor alpha-dependent binding to gp130 or signaling through JAK1-STAT1/3	893:972	Although hIL-6 is also N-glycosylated at N73 and multiply O-glycosylated, neither N-linked nor O-linked glycosylation is necessary for IL-6 receptor alpha-dependent binding to gp130 or signaling through JAK1-STAT1/3.
14970177	5	10	theme	B	1070:1070	arg1	proliferation					1077:1089	B cell proliferation	1070:1089	B cell proliferation	1070:1089	As distinct from vIL-6, unglycosylated hIL-6 is as potent as glycosylated hIL-6 in stimulating B cell proliferation.
14970177	6	11	link	N-linked	1146:1153	arg1	glycosylation					1155:1167	N-linked glycosylation	1146:1167	N-linked glycosylation	1146:1167	These findings highlight distinct functional roles of N-linked glycosylation in viral and cellular IL-6.
14970177	3	12	attach	N-linked	510:517	arg1	vIL-6					501:505	vIL-6	501:505	vIL-6	501:505	Here we show that vIL-6 is N-linked glycosylated at N78 and N89 and demonstrate that N-linked glycosylation at site N89 of vIL-6 markedly enhances binding to gp130, signaling through the JAK1-STAT1/3 pathway and functions in a cytokine-dependent cell proliferation bioassay.
14970177	3	12	attach	N-linked	510:517	arg2	N89					543:545	N89	543:545	N89	543:545	Here we show that vIL-6 is N-linked glycosylated at N78 and N89 and demonstrate that N-linked glycosylation at site N89 of vIL-6 markedly enhances binding to gp130, signaling through the JAK1-STAT1/3 pathway and functions in a cytokine-dependent cell proliferation bioassay.
14970177	3	12	attach	N-linked	510:517	arg2	N78					535:537	N78	535:537	N78	535:537	Here we show that vIL-6 is N-linked glycosylated at N78 and N89 and demonstrate that N-linked glycosylation at site N89 of vIL-6 markedly enhances binding to gp130, signaling through the JAK1-STAT1/3 pathway and functions in a cytokine-dependent cell proliferation bioassay.
14970177	0	13	theme	cellular	105:112	arg1	interleukin					115:125	Kaposi's sarcoma herpesvirus-encoded, but not cellular, interleukin 6	59:127	Kaposi's sarcoma herpesvirus-encoded, but not cellular, interleukin 6	59:127	N-linked glycosylation is required for optimal function of Kaposi's sarcoma herpesvirus-encoded, but not cellular, interleukin 6.
14970177	5	14	theme	cell	1072:1075	arg1	proliferation					1077:1089	B cell proliferation	1070:1089	B cell proliferation	1070:1089	As distinct from vIL-6, unglycosylated hIL-6 is as potent as glycosylated hIL-6 in stimulating B cell proliferation.
14970177	0	15	link	N-linked	0:7	arg1	glycosylation					9:21	N-linked glycosylation	0:21	N-linked glycosylation	0:21	N-linked glycosylation is required for optimal function of Kaposi's sarcoma herpesvirus-encoded, but not cellular, interleukin 6.
14970177	4	16	gly	O-glycosylated	816:829	arg1	hIL-6					767:771	hIL-6	767:771	hIL-6	767:771	Although hIL-6 is also N-glycosylated at N73 and multiply O-glycosylated, neither N-linked nor O-linked glycosylation is necessary for IL-6 receptor alpha-dependent binding to gp130 or signaling through JAK1-STAT1/3.
14970177	4	17	from	N73	799:801	arg1	N-glycosylated					781:794	N-glycosylated	781:794	N-glycosylated	781:794	Although hIL-6 is also N-glycosylated at N73 and multiply O-glycosylated, neither N-linked nor O-linked glycosylation is necessary for IL-6 receptor alpha-dependent binding to gp130 or signaling through JAK1-STAT1/3.
14970177	6	18	theme	glycosylation	1155:1167	arg1	roles					1137:1141	distinct functional roles	1117:1141	distinct functional roles of N-linked glycosylation in viral and cellular IL-6	1117:1194	These findings highlight distinct functional roles of N-linked glycosylation in viral and cellular IL-6.
14970177	4	19	link	O-linked	853:860	arg1	glycosylation					862:874	neither N-linked nor O-linked glycosylation	832:874	neither N-linked nor O-linked glycosylation	832:874	Although hIL-6 is also N-glycosylated at N73 and multiply O-glycosylated, neither N-linked nor O-linked glycosylation is necessary for IL-6 receptor alpha-dependent binding to gp130 or signaling through JAK1-STAT1/3.
14970177	3	20	theme	site	594:597	arg1	N89					599:601	site N89	594:601	site N89 of vIL-6	594:610	Here we show that vIL-6 is N-linked glycosylated at N78 and N89 and demonstrate that N-linked glycosylation at site N89 of vIL-6 markedly enhances binding to gp130, signaling through the JAK1-STAT1/3 pathway and functions in a cytokine-dependent cell proliferation bioassay.
14970177	6	21	theme	N-linked	1146:1153	arg1	glycosylation					1155:1167	N-linked glycosylation	1146:1167	N-linked glycosylation	1146:1167	These findings highlight distinct functional roles of N-linked glycosylation in viral and cellular IL-6.
14970177	2	22	theme	similar	293:299	arg1	functions					312:320	similar biological functions	293:320	similar biological functions	293:320	hIL-6 and vIL-6 exhibit similar biological functions and both act via the gp130 receptor subunit to activate the Janus tyrosine kinase (JAK)1 and signal transducer and activator of transcription (STAT)1/3 pathway.
14970177	0	23	theme	N-linked	0:7	arg1	glycosylation					9:21	N-linked glycosylation	0:21	N-linked glycosylation	0:21	N-linked glycosylation is required for optimal function of Kaposi's sarcoma herpesvirus-encoded, but not cellular, interleukin 6.
14970177	6	24	from	roles	1137:1141	arg1	viral					1172:1176	viral	1172:1176	viral	1172:1176	These findings highlight distinct functional roles of N-linked glycosylation in viral and cellular IL-6.
14970177	6	24	from	roles	1137:1141	arg1	IL-6					1191:1194	cellular IL-6	1182:1194	cellular IL-6	1182:1194	These findings highlight distinct functional roles of N-linked glycosylation in viral and cellular IL-6.
14970177	2	25	theme	receptor	349:356	arg1	subunit					358:364	the gp130 receptor subunit	339:364	the gp130 receptor subunit	339:364	hIL-6 and vIL-6 exhibit similar biological functions and both act via the gp130 receptor subunit to activate the Janus tyrosine kinase (JAK)1 and signal transducer and activator of transcription (STAT)1/3 pathway.
14970177	0	26	theme	interleukin	115:125	arg1	function					47:54	optimal function	39:54	optimal function of Kaposi's sarcoma herpesvirus-encoded, but not cellular, interleukin 6	39:127	N-linked glycosylation is required for optimal function of Kaposi's sarcoma herpesvirus-encoded, but not cellular, interleukin 6.
14970177	2	27	theme	kinase	397:402	arg1	JAK					405:407	the Janus tyrosine kinase (JAK)1	378:409	the Janus tyrosine kinase (JAK)1	378:409	hIL-6 and vIL-6 exhibit similar biological functions and both act via the gp130 receptor subunit to activate the Janus tyrosine kinase (JAK)1 and signal transducer and activator of transcription (STAT)1/3 pathway.
14970177	4	28	gly	N-glycosylated	781:794	arg2	N73					799:801	N73	799:801	N73	799:801	Although hIL-6 is also N-glycosylated at N73 and multiply O-glycosylated, neither N-linked nor O-linked glycosylation is necessary for IL-6 receptor alpha-dependent binding to gp130 or signaling through JAK1-STAT1/3.
14970177	4	28	gly	N-glycosylated	781:794	arg1	hIL-6					767:771	hIL-6	767:771	hIL-6	767:771	Although hIL-6 is also N-glycosylated at N73 and multiply O-glycosylated, neither N-linked nor O-linked glycosylation is necessary for IL-6 receptor alpha-dependent binding to gp130 or signaling through JAK1-STAT1/3.
14970177	3	29	theme	JAK1-STAT1/3	670:681	arg1	pathway					683:689	the JAK1-STAT1/3 pathway	666:689	the JAK1-STAT1/3 pathway	666:689	Here we show that vIL-6 is N-linked glycosylated at N78 and N89 and demonstrate that N-linked glycosylation at site N89 of vIL-6 markedly enhances binding to gp130, signaling through the JAK1-STAT1/3 pathway and functions in a cytokine-dependent cell proliferation bioassay.
14970177	5	30	theme	glycosylated	1036:1047	arg1	hIL-6					1049:1053	glycosylated hIL-6	1036:1053	glycosylated hIL-6 in stimulating B cell proliferation	1036:1089	As distinct from vIL-6, unglycosylated hIL-6 is as potent as glycosylated hIL-6 in stimulating B cell proliferation.
14970177	6	31	theme	functional	1126:1135	arg1	roles					1137:1141	distinct functional roles	1117:1141	distinct functional roles of N-linked glycosylation in viral and cellular IL-6	1117:1194	These findings highlight distinct functional roles of N-linked glycosylation in viral and cellular IL-6.
14970177	5	32	from	vIL-6	992:996	arg1	distinct					978:985	distinct	978:985	distinct	978:985	As distinct from vIL-6, unglycosylated hIL-6 is as potent as glycosylated hIL-6 in stimulating B cell proliferation.
14970177	2	33	theme	tyrosine	388:395	arg1	JAK					405:407	the Janus tyrosine kinase (JAK)1	378:409	the Janus tyrosine kinase (JAK)1	378:409	hIL-6 and vIL-6 exhibit similar biological functions and both act via the gp130 receptor subunit to activate the Janus tyrosine kinase (JAK)1 and signal transducer and activator of transcription (STAT)1/3 pathway.
14970177	0	34	theme	optimal	39:45	arg1	function					47:54	optimal function	39:54	optimal function of Kaposi's sarcoma herpesvirus-encoded, but not cellular, interleukin 6	39:127	N-linked glycosylation is required for optimal function of Kaposi's sarcoma herpesvirus-encoded, but not cellular, interleukin 6.
14970177	4	35	theme	receptor	898:905	arg1	binding					923:929	IL-6 receptor alpha-dependent binding	893:929	IL-6 receptor alpha-dependent binding to gp130 or signaling through JAK1-STAT1/3	893:972	Although hIL-6 is also N-glycosylated at N73 and multiply O-glycosylated, neither N-linked nor O-linked glycosylation is necessary for IL-6 receptor alpha-dependent binding to gp130 or signaling through JAK1-STAT1/3.
14970177	1	36	theme	structural	197:206	arg1	interleukin-6					170:182	Kaposi's sarcoma-associated herpesvirus interleukin-6	130:182	Kaposi's sarcoma-associated herpesvirus interleukin-6 (vIL-6)	130:190	Kaposi's sarcoma-associated herpesvirus interleukin-6 (vIL-6) is a structural and functional homologue of the human cytokine IL-6 (hIL-6).
14970177	1	36	theme	structural	197:206	arg1	homologue					223:231	a structural and functional homologue	195:231	a structural and functional homologue of the human cytokine IL-6 (hIL-6)	195:266	Kaposi's sarcoma-associated herpesvirus interleukin-6 (vIL-6) is a structural and functional homologue of the human cytokine IL-6 (hIL-6).
14970177	2	37	theme	Janus	382:386	arg1	JAK					405:407	the Janus tyrosine kinase (JAK)1	378:409	the Janus tyrosine kinase (JAK)1	378:409	hIL-6 and vIL-6 exhibit similar biological functions and both act via the gp130 receptor subunit to activate the Janus tyrosine kinase (JAK)1 and signal transducer and activator of transcription (STAT)1/3 pathway.
14970177	2	38	theme	transducer	422:431	arg1	pathway					474:480	signal transducer and activator of transcription (STAT)1/3 pathway	415:480	signal transducer and activator of transcription (STAT)1/3 pathway	415:480	hIL-6 and vIL-6 exhibit similar biological functions and both act via the gp130 receptor subunit to activate the Janus tyrosine kinase (JAK)1 and signal transducer and activator of transcription (STAT)1/3 pathway.
14970177	3	39	theme	cytokine-dependent	710:727	arg1	bioassay					748:755	a cytokine-dependent cell proliferation bioassay	708:755	a cytokine-dependent cell proliferation bioassay	708:755	Here we show that vIL-6 is N-linked glycosylated at N78 and N89 and demonstrate that N-linked glycosylation at site N89 of vIL-6 markedly enhances binding to gp130, signaling through the JAK1-STAT1/3 pathway and functions in a cytokine-dependent cell proliferation bioassay.
14970177	4	40	theme	IL-6	893:896	arg1	binding					923:929	IL-6 receptor alpha-dependent binding	893:929	IL-6 receptor alpha-dependent binding to gp130 or signaling through JAK1-STAT1/3	893:972	Although hIL-6 is also N-glycosylated at N73 and multiply O-glycosylated, neither N-linked nor O-linked glycosylation is necessary for IL-6 receptor alpha-dependent binding to gp130 or signaling through JAK1-STAT1/3.
14970177	3	41	theme	N-linked	568:575	arg1	glycosylation					577:589	N-linked glycosylation	568:589	N-linked glycosylation at site N89 of vIL-6	568:610	Here we show that vIL-6 is N-linked glycosylated at N78 and N89 and demonstrate that N-linked glycosylation at site N89 of vIL-6 markedly enhances binding to gp130, signaling through the JAK1-STAT1/3 pathway and functions in a cytokine-dependent cell proliferation bioassay.
14970177	0	42	gly	glycosylation	9:21	arg1	interleukin					115:125	Kaposi's sarcoma herpesvirus-encoded, but not cellular, interleukin 6	59:127	Kaposi's sarcoma herpesvirus-encoded, but not cellular, interleukin 6	59:127	N-linked glycosylation is required for optimal function of Kaposi's sarcoma herpesvirus-encoded, but not cellular, interleukin 6.
14970177	2	43	theme	signal	415:420	arg1	transducer					422:431	signal transducer	415:431	signal transducer	415:431	hIL-6 and vIL-6 exhibit similar biological functions and both act via the gp130 receptor subunit to activate the Janus tyrosine kinase (JAK)1 and signal transducer and activator of transcription (STAT)1/3 pathway.
14970177	2	43	theme	signal	415:420	arg1	STAT					465:468	STAT	465:468	STAT	465:468	hIL-6 and vIL-6 exhibit similar biological functions and both act via the gp130 receptor subunit to activate the Janus tyrosine kinase (JAK)1 and signal transducer and activator of transcription (STAT)1/3 pathway.
14970177	3	44	theme	cell	729:732	arg1	bioassay					748:755	a cytokine-dependent cell proliferation bioassay	708:755	a cytokine-dependent cell proliferation bioassay	708:755	Here we show that vIL-6 is N-linked glycosylated at N78 and N89 and demonstrate that N-linked glycosylation at site N89 of vIL-6 markedly enhances binding to gp130, signaling through the JAK1-STAT1/3 pathway and functions in a cytokine-dependent cell proliferation bioassay.
14970177	4	45	theme	O-linked	853:860	arg1	glycosylation					862:874	neither N-linked nor O-linked glycosylation	832:874	neither N-linked nor O-linked glycosylation	832:874	Although hIL-6 is also N-glycosylated at N73 and multiply O-glycosylated, neither N-linked nor O-linked glycosylation is necessary for IL-6 receptor alpha-dependent binding to gp130 or signaling through JAK1-STAT1/3.
14970177	5	46	theme	unglycosylated	999:1012	arg1	hIL-6					1014:1018	unglycosylated hIL-6	999:1018	unglycosylated hIL-6	999:1018	As distinct from vIL-6, unglycosylated hIL-6 is as potent as glycosylated hIL-6 in stimulating B cell proliferation.
14970177	6	47	theme	distinct	1117:1124	arg1	roles					1137:1141	distinct functional roles	1117:1141	distinct functional roles of N-linked glycosylation in viral and cellular IL-6	1117:1194	These findings highlight distinct functional roles of N-linked glycosylation in viral and cellular IL-6.
14970177	3	48	theme	vIL-6	606:610	arg1	N89					599:601	site N89	594:601	site N89 of vIL-6	594:610	Here we show that vIL-6 is N-linked glycosylated at N78 and N89 and demonstrate that N-linked glycosylation at site N89 of vIL-6 markedly enhances binding to gp130, signaling through the JAK1-STAT1/3 pathway and functions in a cytokine-dependent cell proliferation bioassay.
14970177	6	49	theme	cellular	1182:1189	arg1	IL-6					1191:1194	cellular IL-6	1182:1194	cellular IL-6	1182:1194	These findings highlight distinct functional roles of N-linked glycosylation in viral and cellular IL-6.
14970177	5	50	gly	glycosylated	1036:1047	arg1	hIL-6					1049:1053	glycosylated hIL-6	1036:1053	glycosylated hIL-6 in stimulating B cell proliferation	1036:1089	As distinct from vIL-6, unglycosylated hIL-6 is as potent as glycosylated hIL-6 in stimulating B cell proliferation.
14970177	1	51	theme	functional	212:221	arg1	interleukin-6					170:182	Kaposi's sarcoma-associated herpesvirus interleukin-6	130:182	Kaposi's sarcoma-associated herpesvirus interleukin-6 (vIL-6)	130:190	Kaposi's sarcoma-associated herpesvirus interleukin-6 (vIL-6) is a structural and functional homologue of the human cytokine IL-6 (hIL-6).
14970177	1	51	theme	functional	212:221	arg1	homologue					223:231	a structural and functional homologue	195:231	a structural and functional homologue of the human cytokine IL-6 (hIL-6)	195:266	Kaposi's sarcoma-associated herpesvirus interleukin-6 (vIL-6) is a structural and functional homologue of the human cytokine IL-6 (hIL-6).
14970177	2	52	theme	biological	301:310	arg1	functions					312:320	similar biological functions	293:320	similar biological functions	293:320	hIL-6 and vIL-6 exhibit similar biological functions and both act via the gp130 receptor subunit to activate the Janus tyrosine kinase (JAK)1 and signal transducer and activator of transcription (STAT)1/3 pathway.
14970177	3	53	from	N89	599:601	arg1	glycosylation					577:589	N-linked glycosylation	568:589	N-linked glycosylation at site N89 of vIL-6	568:610	Here we show that vIL-6 is N-linked glycosylated at N78 and N89 and demonstrate that N-linked glycosylation at site N89 of vIL-6 markedly enhances binding to gp130, signaling through the JAK1-STAT1/3 pathway and functions in a cytokine-dependent cell proliferation bioassay.
14970177	4	54	dep	N-glycosylated	781:794	arg1	O-glycosylated					816:829	O-glycosylated	816:829	O-glycosylated	816:829	Although hIL-6 is also N-glycosylated at N73 and multiply O-glycosylated, neither N-linked nor O-linked glycosylation is necessary for IL-6 receptor alpha-dependent binding to gp130 or signaling through JAK1-STAT1/3.
14970177	2	55	theme	gp130	343:347	arg1	subunit					358:364	the gp130 receptor subunit	339:364	the gp130 receptor subunit	339:364	hIL-6 and vIL-6 exhibit similar biological functions and both act via the gp130 receptor subunit to activate the Janus tyrosine kinase (JAK)1 and signal transducer and activator of transcription (STAT)1/3 pathway.
14970177	3	56	theme	proliferation	734:746	arg1	bioassay					748:755	a cytokine-dependent cell proliferation bioassay	708:755	a cytokine-dependent cell proliferation bioassay	708:755	Here we show that vIL-6 is N-linked glycosylated at N78 and N89 and demonstrate that N-linked glycosylation at site N89 of vIL-6 markedly enhances binding to gp130, signaling through the JAK1-STAT1/3 pathway and functions in a cytokine-dependent cell proliferation bioassay.
14970177	2	57	theme	transcription	450:462	arg1	activator					437:445	activator	437:445	activator	437:445	hIL-6 and vIL-6 exhibit similar biological functions and both act via the gp130 receptor subunit to activate the Janus tyrosine kinase (JAK)1 and signal transducer and activator of transcription (STAT)1/3 pathway.
14970177	2	57	theme	transcription	450:462	arg1	transducer					422:431	signal transducer	415:431	signal transducer	415:431	hIL-6 and vIL-6 exhibit similar biological functions and both act via the gp130 receptor subunit to activate the Janus tyrosine kinase (JAK)1 and signal transducer and activator of transcription (STAT)1/3 pathway.
14970177	2	57	theme	transcription	450:462	arg1	STAT					465:468	STAT	465:468	STAT	465:468	hIL-6 and vIL-6 exhibit similar biological functions and both act via the gp130 receptor subunit to activate the Janus tyrosine kinase (JAK)1 and signal transducer and activator of transcription (STAT)1/3 pathway.
14970177	5	58	gly	unglycosylated	999:1012	arg1	hIL-6					1014:1018	unglycosylated hIL-6	999:1018	unglycosylated hIL-6	999:1018	As distinct from vIL-6, unglycosylated hIL-6 is as potent as glycosylated hIL-6 in stimulating B cell proliferation.
14970177	4	59	link	N-linked	840:847	arg1	glycosylation					862:874	neither N-linked nor O-linked glycosylation	832:874	neither N-linked nor O-linked glycosylation	832:874	Although hIL-6 is also N-glycosylated at N73 and multiply O-glycosylated, neither N-linked nor O-linked glycosylation is necessary for IL-6 receptor alpha-dependent binding to gp130 or signaling through JAK1-STAT1/3.
14970177	3	60	link	N-linked	568:575	arg1	glycosylation					577:589	N-linked glycosylation	568:589	N-linked glycosylation at site N89 of vIL-6	568:610	Here we show that vIL-6 is N-linked glycosylated at N78 and N89 and demonstrate that N-linked glycosylation at site N89 of vIL-6 markedly enhances binding to gp130, signaling through the JAK1-STAT1/3 pathway and functions in a cytokine-dependent cell proliferation bioassay.
17259069	0	0	theme	site-directed	108:120	arg1	mutagenesis					122:132	site-directed mutagenesis	108:132	site-directed mutagenesis	108:132	Post-translational modification regulates prostaglandin D2 synthase apoptotic activity: characterization by site-directed mutagenesis.
17259069	5	1	theme	enzymatic	841:849	arg1	Cys65					864:868	Cys65	864:868	Cys65	864:868	Point mutations created in a glycosylation site (Asn51), a protein kinase C phosphorylation site (Ser106), and the enzymatic active site (Cys65) all inhibited L-PGDS-induced apoptosis as determined by both terminal deoxynucleotidyl transferase (TdT)-mediated dUTP nick end-labeling (TUNEL) and caspase3 activity.
17259069	5	1	theme	enzymatic	841:849	arg1	site					858:861	the enzymatic active site	837:861	the enzymatic active site (Cys65)	837:869	Point mutations created in a glycosylation site (Asn51), a protein kinase C phosphorylation site (Ser106), and the enzymatic active site (Cys65) all inhibited L-PGDS-induced apoptosis as determined by both terminal deoxynucleotidyl transferase (TdT)-mediated dUTP nick end-labeling (TUNEL) and caspase3 activity.
17259069	2	2	with	patients	308:315	arg1	impairment					328:337	renal impairment	322:337	renal impairment	322:337	Elevated L-PGDS levels have been observed in the serum of patients with renal impairment, diabetes mellitus, and hypertension.
17259069	2	2	with	patients	308:315	arg1	mellitus					349:356	diabetes mellitus	340:356	diabetes mellitus	340:356	Elevated L-PGDS levels have been observed in the serum of patients with renal impairment, diabetes mellitus, and hypertension.
17259069	2	2	with	patients	308:315	arg1	hypertension					363:374	hypertension	363:374	hypertension	363:374	Elevated L-PGDS levels have been observed in the serum of patients with renal impairment, diabetes mellitus, and hypertension.
17259069	3	3	theme	neuronal	500:507	arg1	cells					509:513	neuronal cells	500:513	neuronal cells	500:513	Recently, we demonstrated the ability of L-PGDS to induce apoptosis in a variety of cell types including epithelial cells, neuronal cells, and vascular smooth muscle cells (VSMCs).
17259069	7	4	theme	L-PGDS	1301:1306	arg1	modification					1285:1296	post-translational modification	1266:1296	post-translational modification	1266:1296	We conclude that post-translational modification of L-PGDS, by either glycosylation or phosphorylation, enhances its apoptotic activity and inhibits VSMC hyperproliferation and postulate that this process is altered in type 2 diabetes.
17259069	5	5	gly	glycosylation	755:767	arg2	Asn51					775:779	Asn51	775:779	Asn51	775:779	Point mutations created in a glycosylation site (Asn51), a protein kinase C phosphorylation site (Ser106), and the enzymatic active site (Cys65) all inhibited L-PGDS-induced apoptosis as determined by both terminal deoxynucleotidyl transferase (TdT)-mediated dUTP nick end-labeling (TUNEL) and caspase3 activity.
17259069	5	5	gly	glycosylation	755:767	arg2	site					769:772	a glycosylation site	753:772	a glycosylation site (Asn51)	753:780	Point mutations created in a glycosylation site (Asn51), a protein kinase C phosphorylation site (Ser106), and the enzymatic active site (Cys65) all inhibited L-PGDS-induced apoptosis as determined by both terminal deoxynucleotidyl transferase (TdT)-mediated dUTP nick end-labeling (TUNEL) and caspase3 activity.
17259069	1	6	gly	glycosylated	199:210	arg1	synthase					169:176	Lipocalin-type prostaglandin D(2) synthase	135:176	Lipocalin-type prostaglandin D(2) synthase (L-PGDS)	135:185	Lipocalin-type prostaglandin D(2) synthase (L-PGDS) is a highly glycosylated protein found in several body fluids.
17259069	1	6	gly	glycosylated	199:210	arg1	protein					212:218	a highly glycosylated protein	190:218	a highly glycosylated protein found in several body fluids	190:247	Lipocalin-type prostaglandin D(2) synthase (L-PGDS) is a highly glycosylated protein found in several body fluids.
17259069	3	7	theme	smooth	529:534	arg1	VSMCs					550:554	VSMCs	550:554	VSMCs	550:554	Recently, we demonstrated the ability of L-PGDS to induce apoptosis in a variety of cell types including epithelial cells, neuronal cells, and vascular smooth muscle cells (VSMCs).
17259069	3	7	theme	smooth	529:534	arg1	cells					543:547	vascular smooth muscle cells	520:547	vascular smooth muscle cells (VSMCs)	520:555	Recently, we demonstrated the ability of L-PGDS to induce apoptosis in a variety of cell types including epithelial cells, neuronal cells, and vascular smooth muscle cells (VSMCs).
17259069	5	8	theme	deoxynucleotidyl	941:956	arg1	TUNEL					1009:1013	TUNEL	1009:1013	TUNEL	1009:1013	Point mutations created in a glycosylation site (Asn51), a protein kinase C phosphorylation site (Ser106), and the enzymatic active site (Cys65) all inhibited L-PGDS-induced apoptosis as determined by both terminal deoxynucleotidyl transferase (TdT)-mediated dUTP nick end-labeling (TUNEL) and caspase3 activity.
17259069	5	8	theme	deoxynucleotidyl	941:956	arg1	end-labeling					995:1006	terminal deoxynucleotidyl transferase (TdT)-mediated dUTP nick end-labeling	932:1006	terminal deoxynucleotidyl transferase (TdT)-mediated dUTP nick end-labeling (TUNEL)	932:1014	Point mutations created in a glycosylation site (Asn51), a protein kinase C phosphorylation site (Ser106), and the enzymatic active site (Cys65) all inhibited L-PGDS-induced apoptosis as determined by both terminal deoxynucleotidyl transferase (TdT)-mediated dUTP nick end-labeling (TUNEL) and caspase3 activity.
17259069	4	9	theme	regulation	714:723	arg1	regulation					714:723	regulation	714:723	regulation	714:723	The aim of this study was to investigate the effect several site-directed mutations had on L-PGDS-induced apoptosis in order to identify potential sites of regulation.
17259069	4	9	theme	regulation	714:723	arg1	sites					705:709	potential sites	695:709	potential sites of regulation	695:723	The aim of this study was to investigate the effect several site-directed mutations had on L-PGDS-induced apoptosis in order to identify potential sites of regulation.
17259069	6	10	theme	rat	1090:1092	arg1	serum					1094:1098	GK rat serum	1087:1098	GK rat serum to WKY control serum using two-dimensional gel electrophoresis	1087:1161	We also compared the L-PGDS isoforms present in GK rat serum to WKY control serum using two-dimensional gel electrophoresis and observed distinct differences which vanished after PNGase F glycolytic digestion.
17259069	6	11	theme	control	1107:1113	arg1	serum					1115:1119	WKY control serum	1103:1119	WKY control serum using two-dimensional gel electrophoresis	1103:1161	We also compared the L-PGDS isoforms present in GK rat serum to WKY control serum using two-dimensional gel electrophoresis and observed distinct differences which vanished after PNGase F glycolytic digestion.
17259069	6	12	theme	F	1225:1225	arg1	digestion					1238:1246	PNGase F glycolytic digestion	1218:1246	PNGase F glycolytic digestion	1218:1246	We also compared the L-PGDS isoforms present in GK rat serum to WKY control serum using two-dimensional gel electrophoresis and observed distinct differences which vanished after PNGase F glycolytic digestion.
17259069	3	13	theme	muscle	536:541	arg1	VSMCs					550:554	VSMCs	550:554	VSMCs	550:554	Recently, we demonstrated the ability of L-PGDS to induce apoptosis in a variety of cell types including epithelial cells, neuronal cells, and vascular smooth muscle cells (VSMCs).
17259069	3	13	theme	muscle	536:541	arg1	cells					543:547	vascular smooth muscle cells	520:547	vascular smooth muscle cells (VSMCs)	520:555	Recently, we demonstrated the ability of L-PGDS to induce apoptosis in a variety of cell types including epithelial cells, neuronal cells, and vascular smooth muscle cells (VSMCs).
17259069	4	14	theme	potential	695:703	arg1	regulation					714:723	regulation	714:723	regulation	714:723	The aim of this study was to investigate the effect several site-directed mutations had on L-PGDS-induced apoptosis in order to identify potential sites of regulation.
17259069	4	14	theme	potential	695:703	arg1	sites					705:709	potential sites	695:709	potential sites of regulation	695:723	The aim of this study was to investigate the effect several site-directed mutations had on L-PGDS-induced apoptosis in order to identify potential sites of regulation.
17259069	3	15	theme	epithelial	482:491	arg1	cells					493:497	epithelial cells	482:497	epithelial cells	482:497	Recently, we demonstrated the ability of L-PGDS to induce apoptosis in a variety of cell types including epithelial cells, neuronal cells, and vascular smooth muscle cells (VSMCs).
17259069	6	16	theme	PNGase	1218:1223	arg1	digestion					1238:1246	PNGase F glycolytic digestion	1218:1246	PNGase F glycolytic digestion	1218:1246	We also compared the L-PGDS isoforms present in GK rat serum to WKY control serum using two-dimensional gel electrophoresis and observed distinct differences which vanished after PNGase F glycolytic digestion.
17259069	5	17	theme	C	800:800	arg1	Ser106					824:829	Ser106	824:829	Ser106	824:829	Point mutations created in a glycosylation site (Asn51), a protein kinase C phosphorylation site (Ser106), and the enzymatic active site (Cys65) all inhibited L-PGDS-induced apoptosis as determined by both terminal deoxynucleotidyl transferase (TdT)-mediated dUTP nick end-labeling (TUNEL) and caspase3 activity.
17259069	5	17	theme	C	800:800	arg1	site					818:821	a protein kinase C phosphorylation site	783:821	a protein kinase C phosphorylation site (Ser106)	783:830	Point mutations created in a glycosylation site (Asn51), a protein kinase C phosphorylation site (Ser106), and the enzymatic active site (Cys65) all inhibited L-PGDS-induced apoptosis as determined by both terminal deoxynucleotidyl transferase (TdT)-mediated dUTP nick end-labeling (TUNEL) and caspase3 activity.
17259069	6	18	theme	WKY	1103:1105	arg1	serum					1115:1119	WKY control serum	1103:1119	WKY control serum using two-dimensional gel electrophoresis	1103:1161	We also compared the L-PGDS isoforms present in GK rat serum to WKY control serum using two-dimensional gel electrophoresis and observed distinct differences which vanished after PNGase F glycolytic digestion.
17259069	6	19	theme	gel	1143:1145	arg1	electrophoresis					1147:1161	two-dimensional gel electrophoresis	1127:1161	two-dimensional gel electrophoresis	1127:1161	We also compared the L-PGDS isoforms present in GK rat serum to WKY control serum using two-dimensional gel electrophoresis and observed distinct differences which vanished after PNGase F glycolytic digestion.
17259069	5	20	theme	Point	726:730	arg1	mutations					732:740	Point mutations	726:740	Point mutations created in a glycosylation site (Asn51), a protein kinase C phosphorylation site (Ser106), and the enzymatic active site (Cys65)	726:869	Point mutations created in a glycosylation site (Asn51), a protein kinase C phosphorylation site (Ser106), and the enzymatic active site (Cys65) all inhibited L-PGDS-induced apoptosis as determined by both terminal deoxynucleotidyl transferase (TdT)-mediated dUTP nick end-labeling (TUNEL) and caspase3 activity.
17259069	5	21	theme	active	851:856	arg1	Cys65					864:868	Cys65	864:868	Cys65	864:868	Point mutations created in a glycosylation site (Asn51), a protein kinase C phosphorylation site (Ser106), and the enzymatic active site (Cys65) all inhibited L-PGDS-induced apoptosis as determined by both terminal deoxynucleotidyl transferase (TdT)-mediated dUTP nick end-labeling (TUNEL) and caspase3 activity.
17259069	5	21	theme	active	851:856	arg1	site					858:861	the enzymatic active site	837:861	the enzymatic active site (Cys65)	837:869	Point mutations created in a glycosylation site (Asn51), a protein kinase C phosphorylation site (Ser106), and the enzymatic active site (Cys65) all inhibited L-PGDS-induced apoptosis as determined by both terminal deoxynucleotidyl transferase (TdT)-mediated dUTP nick end-labeling (TUNEL) and caspase3 activity.
17259069	5	22	theme	glycosylation	755:767	arg1	Asn51					775:779	Asn51	775:779	Asn51	775:779	Point mutations created in a glycosylation site (Asn51), a protein kinase C phosphorylation site (Ser106), and the enzymatic active site (Cys65) all inhibited L-PGDS-induced apoptosis as determined by both terminal deoxynucleotidyl transferase (TdT)-mediated dUTP nick end-labeling (TUNEL) and caspase3 activity.
17259069	5	22	theme	glycosylation	755:767	arg1	site					769:772	a glycosylation site	753:772	a glycosylation site (Asn51)	753:780	Point mutations created in a glycosylation site (Asn51), a protein kinase C phosphorylation site (Ser106), and the enzymatic active site (Cys65) all inhibited L-PGDS-induced apoptosis as determined by both terminal deoxynucleotidyl transferase (TdT)-mediated dUTP nick end-labeling (TUNEL) and caspase3 activity.
17259069	6	23	theme	GK	1087:1088	arg1	serum					1094:1098	GK rat serum	1087:1098	GK rat serum to WKY control serum using two-dimensional gel electrophoresis	1087:1161	We also compared the L-PGDS isoforms present in GK rat serum to WKY control serum using two-dimensional gel electrophoresis and observed distinct differences which vanished after PNGase F glycolytic digestion.
17259069	3	24	theme	vascular	520:527	arg1	VSMCs					550:554	VSMCs	550:554	VSMCs	550:554	Recently, we demonstrated the ability of L-PGDS to induce apoptosis in a variety of cell types including epithelial cells, neuronal cells, and vascular smooth muscle cells (VSMCs).
17259069	3	24	theme	vascular	520:527	arg1	cells					543:547	vascular smooth muscle cells	520:547	vascular smooth muscle cells (VSMCs)	520:555	Recently, we demonstrated the ability of L-PGDS to induce apoptosis in a variety of cell types including epithelial cells, neuronal cells, and vascular smooth muscle cells (VSMCs).
17259069	4	25	theme	site-directed	618:630	arg1	mutations					632:640	several site-directed mutations	610:640	several site-directed mutations	610:640	The aim of this study was to investigate the effect several site-directed mutations had on L-PGDS-induced apoptosis in order to identify potential sites of regulation.
17259069	2	26	theme	renal	322:326	arg1	impairment					328:337	renal impairment	322:337	renal impairment	322:337	Elevated L-PGDS levels have been observed in the serum of patients with renal impairment, diabetes mellitus, and hypertension.
17259069	0	27	theme	Post-translational	0:17	arg1	modification					19:30	Post-translational modification	0:30	Post-translational modification	0:30	Post-translational modification regulates prostaglandin D2 synthase apoptotic activity: characterization by site-directed mutagenesis.
17259069	5	28	theme	nick	990:993	arg1	TUNEL					1009:1013	TUNEL	1009:1013	TUNEL	1009:1013	Point mutations created in a glycosylation site (Asn51), a protein kinase C phosphorylation site (Ser106), and the enzymatic active site (Cys65) all inhibited L-PGDS-induced apoptosis as determined by both terminal deoxynucleotidyl transferase (TdT)-mediated dUTP nick end-labeling (TUNEL) and caspase3 activity.
17259069	5	28	theme	nick	990:993	arg1	end-labeling					995:1006	terminal deoxynucleotidyl transferase (TdT)-mediated dUTP nick end-labeling	932:1006	terminal deoxynucleotidyl transferase (TdT)-mediated dUTP nick end-labeling (TUNEL)	932:1014	Point mutations created in a glycosylation site (Asn51), a protein kinase C phosphorylation site (Ser106), and the enzymatic active site (Cys65) all inhibited L-PGDS-induced apoptosis as determined by both terminal deoxynucleotidyl transferase (TdT)-mediated dUTP nick end-labeling (TUNEL) and caspase3 activity.
17259069	1	29	theme	glycosylated	199:210	arg1	synthase					169:176	Lipocalin-type prostaglandin D(2) synthase	135:176	Lipocalin-type prostaglandin D(2) synthase (L-PGDS)	135:185	Lipocalin-type prostaglandin D(2) synthase (L-PGDS) is a highly glycosylated protein found in several body fluids.
17259069	1	29	theme	glycosylated	199:210	arg1	protein					212:218	a highly glycosylated protein	190:218	a highly glycosylated protein found in several body fluids	190:247	Lipocalin-type prostaglandin D(2) synthase (L-PGDS) is a highly glycosylated protein found in several body fluids.
17259069	0	30	theme	prostaglandin	42:54	arg1	activity					78:85	prostaglandin D2 synthase apoptotic activity	42:85	prostaglandin D2 synthase apoptotic activity	42:85	Post-translational modification regulates prostaglandin D2 synthase apoptotic activity: characterization by site-directed mutagenesis.
17259069	6	31	theme	two-dimensional	1127:1141	arg1	electrophoresis					1147:1161	two-dimensional gel electrophoresis	1127:1161	two-dimensional gel electrophoresis	1127:1161	We also compared the L-PGDS isoforms present in GK rat serum to WKY control serum using two-dimensional gel electrophoresis and observed distinct differences which vanished after PNGase F glycolytic digestion.
17259069	2	32	theme	patients	308:315	arg1	serum					299:303	the serum	295:303	the serum of patients with renal impairment, diabetes mellitus, and hypertension	295:374	Elevated L-PGDS levels have been observed in the serum of patients with renal impairment, diabetes mellitus, and hypertension.
17259069	5	33	theme	TdT	971:973	arg1	TUNEL					1009:1013	TUNEL	1009:1013	TUNEL	1009:1013	Point mutations created in a glycosylation site (Asn51), a protein kinase C phosphorylation site (Ser106), and the enzymatic active site (Cys65) all inhibited L-PGDS-induced apoptosis as determined by both terminal deoxynucleotidyl transferase (TdT)-mediated dUTP nick end-labeling (TUNEL) and caspase3 activity.
17259069	5	33	theme	TdT	971:973	arg1	end-labeling					995:1006	terminal deoxynucleotidyl transferase (TdT)-mediated dUTP nick end-labeling	932:1006	terminal deoxynucleotidyl transferase (TdT)-mediated dUTP nick end-labeling (TUNEL)	932:1014	Point mutations created in a glycosylation site (Asn51), a protein kinase C phosphorylation site (Ser106), and the enzymatic active site (Cys65) all inhibited L-PGDS-induced apoptosis as determined by both terminal deoxynucleotidyl transferase (TdT)-mediated dUTP nick end-labeling (TUNEL) and caspase3 activity.
17259069	5	34	theme	kinase	793:798	arg1	Ser106					824:829	Ser106	824:829	Ser106	824:829	Point mutations created in a glycosylation site (Asn51), a protein kinase C phosphorylation site (Ser106), and the enzymatic active site (Cys65) all inhibited L-PGDS-induced apoptosis as determined by both terminal deoxynucleotidyl transferase (TdT)-mediated dUTP nick end-labeling (TUNEL) and caspase3 activity.
17259069	5	34	theme	kinase	793:798	arg1	site					818:821	a protein kinase C phosphorylation site	783:821	a protein kinase C phosphorylation site (Ser106)	783:830	Point mutations created in a glycosylation site (Asn51), a protein kinase C phosphorylation site (Ser106), and the enzymatic active site (Cys65) all inhibited L-PGDS-induced apoptosis as determined by both terminal deoxynucleotidyl transferase (TdT)-mediated dUTP nick end-labeling (TUNEL) and caspase3 activity.
17259069	5	35	theme	protein	785:791	arg1	Ser106					824:829	Ser106	824:829	Ser106	824:829	Point mutations created in a glycosylation site (Asn51), a protein kinase C phosphorylation site (Ser106), and the enzymatic active site (Cys65) all inhibited L-PGDS-induced apoptosis as determined by both terminal deoxynucleotidyl transferase (TdT)-mediated dUTP nick end-labeling (TUNEL) and caspase3 activity.
17259069	5	35	theme	protein	785:791	arg1	site					818:821	a protein kinase C phosphorylation site	783:821	a protein kinase C phosphorylation site (Ser106)	783:830	Point mutations created in a glycosylation site (Asn51), a protein kinase C phosphorylation site (Ser106), and the enzymatic active site (Cys65) all inhibited L-PGDS-induced apoptosis as determined by both terminal deoxynucleotidyl transferase (TdT)-mediated dUTP nick end-labeling (TUNEL) and caspase3 activity.
17259069	7	36	theme	VSMC	1398:1401	arg1	hyperproliferation					1403:1420	VSMC hyperproliferation	1398:1420	VSMC hyperproliferation	1398:1420	We conclude that post-translational modification of L-PGDS, by either glycosylation or phosphorylation, enhances its apoptotic activity and inhibits VSMC hyperproliferation and postulate that this process is altered in type 2 diabetes.
17259069	5	37	theme	L-PGDS-induced	885:898	arg1	apoptosis					900:908	L-PGDS-induced apoptosis	885:908	L-PGDS-induced apoptosis	885:908	Point mutations created in a glycosylation site (Asn51), a protein kinase C phosphorylation site (Ser106), and the enzymatic active site (Cys65) all inhibited L-PGDS-induced apoptosis as determined by both terminal deoxynucleotidyl transferase (TdT)-mediated dUTP nick end-labeling (TUNEL) and caspase3 activity.
17259069	1	38	theme	prostaglandin	150:162	arg1	L-PGDS					179:184	L-PGDS	179:184	L-PGDS	179:184	Lipocalin-type prostaglandin D(2) synthase (L-PGDS) is a highly glycosylated protein found in several body fluids.
17259069	1	38	theme	prostaglandin	150:162	arg1	protein					212:218	a highly glycosylated protein	190:218	a highly glycosylated protein found in several body fluids	190:247	Lipocalin-type prostaglandin D(2) synthase (L-PGDS) is a highly glycosylated protein found in several body fluids.
17259069	1	38	theme	prostaglandin	150:162	arg1	synthase					169:176	Lipocalin-type prostaglandin D(2) synthase	135:176	Lipocalin-type prostaglandin D(2) synthase (L-PGDS)	135:185	Lipocalin-type prostaglandin D(2) synthase (L-PGDS) is a highly glycosylated protein found in several body fluids.
17259069	6	39	from	serum	1094:1098	arg1	present					1076:1082	present	1076:1082	present	1076:1082	We also compared the L-PGDS isoforms present in GK rat serum to WKY control serum using two-dimensional gel electrophoresis and observed distinct differences which vanished after PNGase F glycolytic digestion.
17259069	3	40	theme	cell	461:464	arg1	types					466:470	cell types	461:470	cell types including epithelial cells, neuronal cells, and vascular smooth muscle cells (VSMCs)	461:555	Recently, we demonstrated the ability of L-PGDS to induce apoptosis in a variety of cell types including epithelial cells, neuronal cells, and vascular smooth muscle cells (VSMCs).
17259069	3	40	theme	cell	461:464	arg1	cells					493:497	epithelial cells	482:497	epithelial cells	482:497	Recently, we demonstrated the ability of L-PGDS to induce apoptosis in a variety of cell types including epithelial cells, neuronal cells, and vascular smooth muscle cells (VSMCs).
17259069	3	40	theme	cell	461:464	arg1	cells					509:513	neuronal cells	500:513	neuronal cells	500:513	Recently, we demonstrated the ability of L-PGDS to induce apoptosis in a variety of cell types including epithelial cells, neuronal cells, and vascular smooth muscle cells (VSMCs).
17259069	3	40	theme	cell	461:464	arg1	cells					543:547	vascular smooth muscle cells	520:547	vascular smooth muscle cells (VSMCs)	520:555	Recently, we demonstrated the ability of L-PGDS to induce apoptosis in a variety of cell types including epithelial cells, neuronal cells, and vascular smooth muscle cells (VSMCs).
17259069	0	41	theme	synthase	59:66	arg1	activity					78:85	prostaglandin D2 synthase apoptotic activity	42:85	prostaglandin D2 synthase apoptotic activity	42:85	Post-translational modification regulates prostaglandin D2 synthase apoptotic activity: characterization by site-directed mutagenesis.
17259069	5	42	theme	phosphorylation	802:816	arg1	Ser106					824:829	Ser106	824:829	Ser106	824:829	Point mutations created in a glycosylation site (Asn51), a protein kinase C phosphorylation site (Ser106), and the enzymatic active site (Cys65) all inhibited L-PGDS-induced apoptosis as determined by both terminal deoxynucleotidyl transferase (TdT)-mediated dUTP nick end-labeling (TUNEL) and caspase3 activity.
17259069	5	42	theme	phosphorylation	802:816	arg1	site					818:821	a protein kinase C phosphorylation site	783:821	a protein kinase C phosphorylation site (Ser106)	783:830	Point mutations created in a glycosylation site (Asn51), a protein kinase C phosphorylation site (Ser106), and the enzymatic active site (Cys65) all inhibited L-PGDS-induced apoptosis as determined by both terminal deoxynucleotidyl transferase (TdT)-mediated dUTP nick end-labeling (TUNEL) and caspase3 activity.
17259069	2	43	theme	Elevated	250:257	arg1	levels					266:271	Elevated L-PGDS levels	250:271	Elevated L-PGDS levels	250:271	Elevated L-PGDS levels have been observed in the serum of patients with renal impairment, diabetes mellitus, and hypertension.
17259069	7	44	theme	apoptotic	1366:1374	arg1	activity					1376:1383	its apoptotic activity	1362:1383	its apoptotic activity	1362:1383	We conclude that post-translational modification of L-PGDS, by either glycosylation or phosphorylation, enhances its apoptotic activity and inhibits VSMC hyperproliferation and postulate that this process is altered in type 2 diabetes.
17259069	4	45	theme	several	610:616	arg1	mutations					632:640	several site-directed mutations	610:640	several site-directed mutations	610:640	The aim of this study was to investigate the effect several site-directed mutations had on L-PGDS-induced apoptosis in order to identify potential sites of regulation.
17259069	0	46	theme	D2	56:57	arg1	activity					78:85	prostaglandin D2 synthase apoptotic activity	42:85	prostaglandin D2 synthase apoptotic activity	42:85	Post-translational modification regulates prostaglandin D2 synthase apoptotic activity: characterization by site-directed mutagenesis.
17259069	3	47	theme	L-PGDS	418:423	arg1	ability					407:413	the ability	403:413	the ability of L-PGDS to induce apoptosis in a variety of cell types including epithelial cells, neuronal cells, and vascular smooth muscle cells (VSMCs)	403:555	Recently, we demonstrated the ability of L-PGDS to induce apoptosis in a variety of cell types including epithelial cells, neuronal cells, and vascular smooth muscle cells (VSMCs).
17259069	5	48	theme	caspase3	1020:1027	arg1	activity					1029:1036	caspase3 activity	1020:1036	caspase3 activity	1020:1036	Point mutations created in a glycosylation site (Asn51), a protein kinase C phosphorylation site (Ser106), and the enzymatic active site (Cys65) all inhibited L-PGDS-induced apoptosis as determined by both terminal deoxynucleotidyl transferase (TdT)-mediated dUTP nick end-labeling (TUNEL) and caspase3 activity.
17259069	4	49	dep	effect	603:608	arg1	had					642:644	had	642:644	had on L-PGDS-induced apoptosis in order to identify potential sites of regulation	642:723	The aim of this study was to investigate the effect several site-directed mutations had on L-PGDS-induced apoptosis in order to identify potential sites of regulation.
17259069	1	50	theme	several	229:235	arg1	fluids					242:247	several body fluids	229:247	several body fluids	229:247	Lipocalin-type prostaglandin D(2) synthase (L-PGDS) is a highly glycosylated protein found in several body fluids.
17259069	5	51	theme	-mediated	975:983	arg1	TUNEL					1009:1013	TUNEL	1009:1013	TUNEL	1009:1013	Point mutations created in a glycosylation site (Asn51), a protein kinase C phosphorylation site (Ser106), and the enzymatic active site (Cys65) all inhibited L-PGDS-induced apoptosis as determined by both terminal deoxynucleotidyl transferase (TdT)-mediated dUTP nick end-labeling (TUNEL) and caspase3 activity.
17259069	5	51	theme	-mediated	975:983	arg1	end-labeling					995:1006	terminal deoxynucleotidyl transferase (TdT)-mediated dUTP nick end-labeling	932:1006	terminal deoxynucleotidyl transferase (TdT)-mediated dUTP nick end-labeling (TUNEL)	932:1014	Point mutations created in a glycosylation site (Asn51), a protein kinase C phosphorylation site (Ser106), and the enzymatic active site (Cys65) all inhibited L-PGDS-induced apoptosis as determined by both terminal deoxynucleotidyl transferase (TdT)-mediated dUTP nick end-labeling (TUNEL) and caspase3 activity.
17259069	1	52	theme	D	164:164	arg1	L-PGDS					179:184	L-PGDS	179:184	L-PGDS	179:184	Lipocalin-type prostaglandin D(2) synthase (L-PGDS) is a highly glycosylated protein found in several body fluids.
17259069	1	52	theme	D	164:164	arg1	protein					212:218	a highly glycosylated protein	190:218	a highly glycosylated protein found in several body fluids	190:247	Lipocalin-type prostaglandin D(2) synthase (L-PGDS) is a highly glycosylated protein found in several body fluids.
17259069	1	52	theme	D	164:164	arg1	synthase					169:176	Lipocalin-type prostaglandin D(2) synthase	135:176	Lipocalin-type prostaglandin D(2) synthase (L-PGDS)	135:185	Lipocalin-type prostaglandin D(2) synthase (L-PGDS) is a highly glycosylated protein found in several body fluids.
17259069	0	53	theme	apoptotic	68:76	arg1	activity					78:85	prostaglandin D2 synthase apoptotic activity	42:85	prostaglandin D2 synthase apoptotic activity	42:85	Post-translational modification regulates prostaglandin D2 synthase apoptotic activity: characterization by site-directed mutagenesis.
17259069	2	54	located	observed	283:290	arg2	levels					266:271	Elevated L-PGDS levels	250:271	Elevated L-PGDS levels	250:271	Elevated L-PGDS levels have been observed in the serum of patients with renal impairment, diabetes mellitus, and hypertension.
17259069	2	54	located	observed	283:290	arg1	serum					299:303	the serum	295:303	the serum of patients with renal impairment, diabetes mellitus, and hypertension	295:374	Elevated L-PGDS levels have been observed in the serum of patients with renal impairment, diabetes mellitus, and hypertension.
17259069	1	55	located	found	220:224	arg1	fluids					242:247	several body fluids	229:247	several body fluids	229:247	Lipocalin-type prostaglandin D(2) synthase (L-PGDS) is a highly glycosylated protein found in several body fluids.
17259069	1	55	located	found	220:224	arg2	synthase					169:176	Lipocalin-type prostaglandin D(2) synthase	135:176	Lipocalin-type prostaglandin D(2) synthase (L-PGDS)	135:185	Lipocalin-type prostaglandin D(2) synthase (L-PGDS) is a highly glycosylated protein found in several body fluids.
17259069	1	55	located	found	220:224	arg2	protein					212:218	a highly glycosylated protein	190:218	a highly glycosylated protein found in several body fluids	190:247	Lipocalin-type prostaglandin D(2) synthase (L-PGDS) is a highly glycosylated protein found in several body fluids.
17259069	5	56	theme	dUTP	985:988	arg1	TUNEL					1009:1013	TUNEL	1009:1013	TUNEL	1009:1013	Point mutations created in a glycosylation site (Asn51), a protein kinase C phosphorylation site (Ser106), and the enzymatic active site (Cys65) all inhibited L-PGDS-induced apoptosis as determined by both terminal deoxynucleotidyl transferase (TdT)-mediated dUTP nick end-labeling (TUNEL) and caspase3 activity.
17259069	5	56	theme	dUTP	985:988	arg1	end-labeling					995:1006	terminal deoxynucleotidyl transferase (TdT)-mediated dUTP nick end-labeling	932:1006	terminal deoxynucleotidyl transferase (TdT)-mediated dUTP nick end-labeling (TUNEL)	932:1014	Point mutations created in a glycosylation site (Asn51), a protein kinase C phosphorylation site (Ser106), and the enzymatic active site (Cys65) all inhibited L-PGDS-induced apoptosis as determined by both terminal deoxynucleotidyl transferase (TdT)-mediated dUTP nick end-labeling (TUNEL) and caspase3 activity.
17259069	6	57	from	present	1076:1082	arg1	serum					1094:1098	GK rat serum	1087:1098	GK rat serum to WKY control serum using two-dimensional gel electrophoresis	1087:1161	We also compared the L-PGDS isoforms present in GK rat serum to WKY control serum using two-dimensional gel electrophoresis and observed distinct differences which vanished after PNGase F glycolytic digestion.
17259069	2	58	theme	diabetes	340:347	arg1	mellitus					349:356	diabetes mellitus	340:356	diabetes mellitus	340:356	Elevated L-PGDS levels have been observed in the serum of patients with renal impairment, diabetes mellitus, and hypertension.
17259069	6	59	attach	present	1076:1082	arg1	serum					1094:1098	GK rat serum	1087:1098	GK rat serum to WKY control serum using two-dimensional gel electrophoresis	1087:1161	We also compared the L-PGDS isoforms present in GK rat serum to WKY control serum using two-dimensional gel electrophoresis and observed distinct differences which vanished after PNGase F glycolytic digestion.
17259069	6	59	attach	present	1076:1082	arg2	isoforms					1067:1074	the L-PGDS isoforms	1056:1074	the L-PGDS isoforms present in GK rat serum to WKY control serum using two-dimensional gel electrophoresis	1056:1161	We also compared the L-PGDS isoforms present in GK rat serum to WKY control serum using two-dimensional gel electrophoresis and observed distinct differences which vanished after PNGase F glycolytic digestion.
17259069	5	60	theme	terminal	932:939	arg1	TUNEL					1009:1013	TUNEL	1009:1013	TUNEL	1009:1013	Point mutations created in a glycosylation site (Asn51), a protein kinase C phosphorylation site (Ser106), and the enzymatic active site (Cys65) all inhibited L-PGDS-induced apoptosis as determined by both terminal deoxynucleotidyl transferase (TdT)-mediated dUTP nick end-labeling (TUNEL) and caspase3 activity.
17259069	5	60	theme	terminal	932:939	arg1	end-labeling					995:1006	terminal deoxynucleotidyl transferase (TdT)-mediated dUTP nick end-labeling	932:1006	terminal deoxynucleotidyl transferase (TdT)-mediated dUTP nick end-labeling (TUNEL)	932:1014	Point mutations created in a glycosylation site (Asn51), a protein kinase C phosphorylation site (Ser106), and the enzymatic active site (Cys65) all inhibited L-PGDS-induced apoptosis as determined by both terminal deoxynucleotidyl transferase (TdT)-mediated dUTP nick end-labeling (TUNEL) and caspase3 activity.
17259069	6	61	theme	distinct	1176:1183	arg1	differences					1185:1195	distinct differences	1176:1195	distinct differences which vanished after PNGase F glycolytic digestion	1176:1246	We also compared the L-PGDS isoforms present in GK rat serum to WKY control serum using two-dimensional gel electrophoresis and observed distinct differences which vanished after PNGase F glycolytic digestion.
17259069	3	62	theme	types	466:470	arg1	variety					450:456	a variety	448:456	a variety of cell types including epithelial cells, neuronal cells, and vascular smooth muscle cells (VSMCs)	448:555	Recently, we demonstrated the ability of L-PGDS to induce apoptosis in a variety of cell types including epithelial cells, neuronal cells, and vascular smooth muscle cells (VSMCs).
17259069	3	62	theme	types	466:470	arg1	types					466:470	cell types	461:470	cell types including epithelial cells, neuronal cells, and vascular smooth muscle cells (VSMCs)	461:555	Recently, we demonstrated the ability of L-PGDS to induce apoptosis in a variety of cell types including epithelial cells, neuronal cells, and vascular smooth muscle cells (VSMCs).
17259069	3	62	theme	types	466:470	arg1	cells					493:497	epithelial cells	482:497	epithelial cells	482:497	Recently, we demonstrated the ability of L-PGDS to induce apoptosis in a variety of cell types including epithelial cells, neuronal cells, and vascular smooth muscle cells (VSMCs).
17259069	3	62	theme	types	466:470	arg1	cells					509:513	neuronal cells	500:513	neuronal cells	500:513	Recently, we demonstrated the ability of L-PGDS to induce apoptosis in a variety of cell types including epithelial cells, neuronal cells, and vascular smooth muscle cells (VSMCs).
17259069	3	62	theme	types	466:470	arg1	cells					543:547	vascular smooth muscle cells	520:547	vascular smooth muscle cells (VSMCs)	520:555	Recently, we demonstrated the ability of L-PGDS to induce apoptosis in a variety of cell types including epithelial cells, neuronal cells, and vascular smooth muscle cells (VSMCs).
17259069	1	63	theme	Lipocalin-type	135:148	arg1	L-PGDS					179:184	L-PGDS	179:184	L-PGDS	179:184	Lipocalin-type prostaglandin D(2) synthase (L-PGDS) is a highly glycosylated protein found in several body fluids.
17259069	1	63	theme	Lipocalin-type	135:148	arg1	protein					212:218	a highly glycosylated protein	190:218	a highly glycosylated protein found in several body fluids	190:247	Lipocalin-type prostaglandin D(2) synthase (L-PGDS) is a highly glycosylated protein found in several body fluids.
17259069	1	63	theme	Lipocalin-type	135:148	arg1	synthase					169:176	Lipocalin-type prostaglandin D(2) synthase	135:176	Lipocalin-type prostaglandin D(2) synthase (L-PGDS)	135:185	Lipocalin-type prostaglandin D(2) synthase (L-PGDS) is a highly glycosylated protein found in several body fluids.
17259069	1	64	theme	body	237:240	arg1	fluids					242:247	several body fluids	229:247	several body fluids	229:247	Lipocalin-type prostaglandin D(2) synthase (L-PGDS) is a highly glycosylated protein found in several body fluids.
17259069	0	65	dep	regulates	32:40	arg1	characterization					88:103	characterization	88:103	characterization by site-directed mutagenesis	88:132	Post-translational modification regulates prostaglandin D2 synthase apoptotic activity: characterization by site-directed mutagenesis.
17259069	4	66	theme	L-PGDS-induced	649:662	arg1	apoptosis					664:672	L-PGDS-induced apoptosis	649:672	L-PGDS-induced apoptosis in order to identify potential sites of regulation	649:723	The aim of this study was to investigate the effect several site-directed mutations had on L-PGDS-induced apoptosis in order to identify potential sites of regulation.
17259069	6	67	theme	present	1076:1082	arg1	isoforms					1067:1074	the L-PGDS isoforms	1056:1074	the L-PGDS isoforms present in GK rat serum to WKY control serum using two-dimensional gel electrophoresis	1056:1161	We also compared the L-PGDS isoforms present in GK rat serum to WKY control serum using two-dimensional gel electrophoresis and observed distinct differences which vanished after PNGase F glycolytic digestion.
17259069	6	68	theme	L-PGDS	1060:1065	arg1	isoforms					1067:1074	the L-PGDS isoforms	1056:1074	the L-PGDS isoforms present in GK rat serum to WKY control serum using two-dimensional gel electrophoresis	1056:1161	We also compared the L-PGDS isoforms present in GK rat serum to WKY control serum using two-dimensional gel electrophoresis and observed distinct differences which vanished after PNGase F glycolytic digestion.
17259069	7	69	theme	post-translational	1266:1283	arg1	modification					1285:1296	post-translational modification	1266:1296	post-translational modification	1266:1296	We conclude that post-translational modification of L-PGDS, by either glycosylation or phosphorylation, enhances its apoptotic activity and inhibits VSMC hyperproliferation and postulate that this process is altered in type 2 diabetes.
17259069	5	70	theme	transferase	958:968	arg1	TUNEL					1009:1013	TUNEL	1009:1013	TUNEL	1009:1013	Point mutations created in a glycosylation site (Asn51), a protein kinase C phosphorylation site (Ser106), and the enzymatic active site (Cys65) all inhibited L-PGDS-induced apoptosis as determined by both terminal deoxynucleotidyl transferase (TdT)-mediated dUTP nick end-labeling (TUNEL) and caspase3 activity.
17259069	5	70	theme	transferase	958:968	arg1	end-labeling					995:1006	terminal deoxynucleotidyl transferase (TdT)-mediated dUTP nick end-labeling	932:1006	terminal deoxynucleotidyl transferase (TdT)-mediated dUTP nick end-labeling (TUNEL)	932:1014	Point mutations created in a glycosylation site (Asn51), a protein kinase C phosphorylation site (Ser106), and the enzymatic active site (Cys65) all inhibited L-PGDS-induced apoptosis as determined by both terminal deoxynucleotidyl transferase (TdT)-mediated dUTP nick end-labeling (TUNEL) and caspase3 activity.
17259069	7	71	theme	type	1468:1471	arg1	diabetes					1475:1482	type 2 diabetes	1468:1482	type 2 diabetes	1468:1482	We conclude that post-translational modification of L-PGDS, by either glycosylation or phosphorylation, enhances its apoptotic activity and inhibits VSMC hyperproliferation and postulate that this process is altered in type 2 diabetes.
17259069	2	72	theme	L-PGDS	259:264	arg1	levels					266:271	Elevated L-PGDS levels	250:271	Elevated L-PGDS levels	250:271	Elevated L-PGDS levels have been observed in the serum of patients with renal impairment, diabetes mellitus, and hypertension.
17259069	4	73	theme	study	574:578	arg1	aim					562:564	The aim	558:564	The aim of this study	558:578	The aim of this study was to investigate the effect several site-directed mutations had on L-PGDS-induced apoptosis in order to identify potential sites of regulation.
17259069	6	74	theme	glycolytic	1227:1236	arg1	digestion					1238:1246	PNGase F glycolytic digestion	1218:1246	PNGase F glycolytic digestion	1218:1246	We also compared the L-PGDS isoforms present in GK rat serum to WKY control serum using two-dimensional gel electrophoresis and observed distinct differences which vanished after PNGase F glycolytic digestion.
28628081	5	0	theme	FH	748:749	arg1	O-GlcNAcylation					751:765	FH O-GlcNAcylation	748:765	FH O-GlcNAcylation	748:765	On the other hand, FH is found to be O-GlcNAcylated at the AMPK phosphorylation site; FH-ATF2-mediated downstream events are impeded by FH O-GlcNAcylation, especially in cancer cells that display robust O-GlcNAc transferase (OGT) activity.
28628081	4	1	theme	KDM2A	488:492	arg1	activity					506:513	KDM2A demethylase activity	488:513	KDM2A demethylase activity	488:513	FH-catalysed fumarate in promoter regions inhibits KDM2A demethylase activity, and thus maintains the H3K36me2 profile and facilitates gene expression for cell growth arrest.
28628081	6	2	theme	phosphorylation	879:893	arg1	level					895:899	the FH-Ser75 phosphorylation level	866:899	the FH-Ser75 phosphorylation level	866:899	Consistently, the FH-Ser75 phosphorylation level inversely correlates with the OGT level and poor prognosis in pancreatic cancer patients.
28628081	5	3	from	site	692:695	arg1	O-GlcNAcylated					649:662	O-GlcNAcylated	649:662	O-GlcNAcylated	649:662	On the other hand, FH is found to be O-GlcNAcylated at the AMPK phosphorylation site; FH-ATF2-mediated downstream events are impeded by FH O-GlcNAcylation, especially in cancer cells that display robust O-GlcNAc transferase (OGT) activity.
28628081	7	4	theme	growth	1149:1154	arg1	advantage					1156:1164	growth advantage	1149:1164	growth advantage of cancer cells	1149:1180	These findings uncover a previously uncharacterized mechanism underlying transcription regulation by FH and the linkage between dysregulated OGT activity and growth advantage of cancer cells under glucose deficiency.
28628081	6	5	dep	level	935:939	arg1	the					927:929	the	927:929	the	927:929	Consistently, the FH-Ser75 phosphorylation level inversely correlates with the OGT level and poor prognosis in pancreatic cancer patients.
28628081	4	6	theme	gene	572:575	arg1	expression					577:586	gene expression	572:586	gene expression for cell growth arrest	572:609	FH-catalysed fumarate in promoter regions inhibits KDM2A demethylase activity, and thus maintains the H3K36me2 profile and facilitates gene expression for cell growth arrest.
28628081	5	7	theme	FH-ATF2-mediated	698:713	arg1	events					726:731	FH-ATF2-mediated downstream events	698:731	FH-ATF2-mediated downstream events	698:731	On the other hand, FH is found to be O-GlcNAcylated at the AMPK phosphorylation site; FH-ATF2-mediated downstream events are impeded by FH O-GlcNAcylation, especially in cancer cells that display robust O-GlcNAc transferase (OGT) activity.
28628081	7	8	theme	OGT	1132:1134	arg1	activity					1136:1143	dysregulated OGT activity	1119:1143	dysregulated OGT activity	1119:1143	These findings uncover a previously uncharacterized mechanism underlying transcription regulation by FH and the linkage between dysregulated OGT activity and growth advantage of cancer cells under glucose deficiency.
28628081	4	9	theme	cell	592:595	arg1	arrest					604:609	cell growth arrest	592:609	cell growth arrest	592:609	FH-catalysed fumarate in promoter regions inhibits KDM2A demethylase activity, and thus maintains the H3K36me2 profile and facilitates gene expression for cell growth arrest.
28628081	5	10	theme	downstream	715:724	arg1	events					726:731	FH-ATF2-mediated downstream events	698:731	FH-ATF2-mediated downstream events	698:731	On the other hand, FH is found to be O-GlcNAcylated at the AMPK phosphorylation site; FH-ATF2-mediated downstream events are impeded by FH O-GlcNAcylation, especially in cancer cells that display robust O-GlcNAc transferase (OGT) activity.
28628081	4	11	theme	promoter	462:469	arg1	regions					471:477	promoter regions	462:477	promoter regions	462:477	FH-catalysed fumarate in promoter regions inhibits KDM2A demethylase activity, and thus maintains the H3K36me2 profile and facilitates gene expression for cell growth arrest.
28628081	3	12	with	complex	378:384	arg1	ATF2					391:394	ATF2	391:394	ATF2	391:394	In this study, we show that under glucose deprivation conditions, AMPK phosphorylates FH at Ser75, which in turn forms a complex with ATF2 and participates in promoter activation.
28628081	6	13	theme	cancer	974:979	arg1	patients					981:988	pancreatic cancer patients	963:988	pancreatic cancer patients	963:988	Consistently, the FH-Ser75 phosphorylation level inversely correlates with the OGT level and poor prognosis in pancreatic cancer patients.
28628081	6	14	theme	FH-Ser75	870:877	arg1	level					895:899	the FH-Ser75 phosphorylation level	866:899	the FH-Ser75 phosphorylation level	866:899	Consistently, the FH-Ser75 phosphorylation level inversely correlates with the OGT level and poor prognosis in pancreatic cancer patients.
28628081	1	15	theme	Chromatin-associated	78:97	arg1	FH					109:110	FH	109:110	FH	109:110	Chromatin-associated fumarase (FH) affects histone methylation via its metabolic activity.
28628081	1	15	theme	Chromatin-associated	78:97	arg1	fumarase					99:106	Chromatin-associated fumarase	78:106	Chromatin-associated fumarase (FH)	78:111	Chromatin-associated fumarase (FH) affects histone methylation via its metabolic activity.
28628081	5	16	from	cells	789:793	arg1	impeded					737:743	impeded	737:743	impeded	737:743	On the other hand, FH is found to be O-GlcNAcylated at the AMPK phosphorylation site; FH-ATF2-mediated downstream events are impeded by FH O-GlcNAcylation, especially in cancer cells that display robust O-GlcNAc transferase (OGT) activity.
28628081	5	17	theme	other	619:623	arg1	hand					625:628	the other hand	615:628	the other hand	615:628	On the other hand, FH is found to be O-GlcNAcylated at the AMPK phosphorylation site; FH-ATF2-mediated downstream events are impeded by FH O-GlcNAcylation, especially in cancer cells that display robust O-GlcNAc transferase (OGT) activity.
28628081	3	18	theme	promoter	416:423	arg1	activation					425:434	promoter activation	416:434	promoter activation	416:434	In this study, we show that under glucose deprivation conditions, AMPK phosphorylates FH at Ser75, which in turn forms a complex with ATF2 and participates in promoter activation.
28628081	7	19	theme	transcription	1064:1076	arg1	regulation					1078:1087	transcription regulation	1064:1087	transcription regulation by FH and the linkage between dysregulated OGT activity	1064:1143	These findings uncover a previously uncharacterized mechanism underlying transcription regulation by FH and the linkage between dysregulated OGT activity and growth advantage of cancer cells under glucose deficiency.
28628081	3	20	theme	deprivation	299:309	arg1	conditions					311:320	glucose deprivation conditions	291:320	glucose deprivation conditions	291:320	In this study, we show that under glucose deprivation conditions, AMPK phosphorylates FH at Ser75, which in turn forms a complex with ATF2 and participates in promoter activation.
28628081	6	21	theme	pancreatic	963:972	arg1	patients					981:988	pancreatic cancer patients	963:988	pancreatic cancer patients	963:988	Consistently, the FH-Ser75 phosphorylation level inversely correlates with the OGT level and poor prognosis in pancreatic cancer patients.
28628081	4	22	theme	H3K36me2	539:546	arg1	profile					548:554	the H3K36me2 profile	535:554	the H3K36me2 profile	535:554	FH-catalysed fumarate in promoter regions inhibits KDM2A demethylase activity, and thus maintains the H3K36me2 profile and facilitates gene expression for cell growth arrest.
28628081	5	23	theme	AMPK	671:674	arg1	site					692:695	the AMPK phosphorylation site	667:695	the AMPK phosphorylation site	667:695	On the other hand, FH is found to be O-GlcNAcylated at the AMPK phosphorylation site; FH-ATF2-mediated downstream events are impeded by FH O-GlcNAcylation, especially in cancer cells that display robust O-GlcNAc transferase (OGT) activity.
28628081	5	24	theme	O-GlcNAc	815:822	arg1	OGT					837:839	OGT	837:839	OGT	837:839	On the other hand, FH is found to be O-GlcNAcylated at the AMPK phosphorylation site; FH-ATF2-mediated downstream events are impeded by FH O-GlcNAcylation, especially in cancer cells that display robust O-GlcNAc transferase (OGT) activity.
28628081	5	24	theme	O-GlcNAc	815:822	arg1	transferase					824:834	O-GlcNAc transferase	815:834	robust O-GlcNAc transferase (OGT) activity	808:849	On the other hand, FH is found to be O-GlcNAcylated at the AMPK phosphorylation site; FH-ATF2-mediated downstream events are impeded by FH O-GlcNAcylation, especially in cancer cells that display robust O-GlcNAc transferase (OGT) activity.
28628081	0	25	theme	fumarase	19:26	arg1	O-GlcNAcylation					0:14	O-GlcNAcylation	0:14	O-GlcNAcylation of fumarase	0:26	O-GlcNAcylation of fumarase maintains tumour growth under glucose deficiency.
28628081	5	26	theme	phosphorylation	676:690	arg1	site					692:695	the AMPK phosphorylation site	667:695	the AMPK phosphorylation site	667:695	On the other hand, FH is found to be O-GlcNAcylated at the AMPK phosphorylation site; FH-ATF2-mediated downstream events are impeded by FH O-GlcNAcylation, especially in cancer cells that display robust O-GlcNAc transferase (OGT) activity.
28628081	5	27	theme	transferase	824:834	arg1	activity					842:849	robust O-GlcNAc transferase (OGT) activity	808:849	robust O-GlcNAc transferase (OGT) activity	808:849	On the other hand, FH is found to be O-GlcNAcylated at the AMPK phosphorylation site; FH-ATF2-mediated downstream events are impeded by FH O-GlcNAcylation, especially in cancer cells that display robust O-GlcNAc transferase (OGT) activity.
28628081	7	28	theme	cancer	1169:1174	arg1	cells					1176:1180	cancer cells	1169:1180	cancer cells	1169:1180	These findings uncover a previously uncharacterized mechanism underlying transcription regulation by FH and the linkage between dysregulated OGT activity and growth advantage of cancer cells under glucose deficiency.
28628081	6	29	theme	poor	945:948	arg1	prognosis					950:958	poor prognosis	945:958	poor prognosis	945:958	Consistently, the FH-Ser75 phosphorylation level inversely correlates with the OGT level and poor prognosis in pancreatic cancer patients.
28628081	0	30	theme	tumour	38:43	arg1	growth					45:50	tumour growth	38:50	tumour growth	38:50	O-GlcNAcylation of fumarase maintains tumour growth under glucose deficiency.
28628081	7	31	theme	cells	1176:1180	arg1	advantage					1156:1164	growth advantage	1149:1164	growth advantage of cancer cells	1149:1180	These findings uncover a previously uncharacterized mechanism underlying transcription regulation by FH and the linkage between dysregulated OGT activity and growth advantage of cancer cells under glucose deficiency.
28628081	7	31	theme	cells	1176:1180	arg1	regulation					1078:1087	transcription regulation	1064:1087	transcription regulation by FH and the linkage between dysregulated OGT activity	1064:1143	These findings uncover a previously uncharacterized mechanism underlying transcription regulation by FH and the linkage between dysregulated OGT activity and growth advantage of cancer cells under glucose deficiency.
28628081	0	32	theme	glucose	58:64	arg1	deficiency					66:75	glucose deficiency	58:75	glucose deficiency	58:75	O-GlcNAcylation of fumarase maintains tumour growth under glucose deficiency.
28628081	3	33	theme	glucose	291:297	arg1	conditions					311:320	glucose deprivation conditions	291:320	glucose deprivation conditions	291:320	In this study, we show that under glucose deprivation conditions, AMPK phosphorylates FH at Ser75, which in turn forms a complex with ATF2 and participates in promoter activation.
28628081	4	34	theme	FH-catalysed	437:448	arg1	fumarate					450:457	FH-catalysed fumarate	437:457	FH-catalysed fumarate in promoter regions	437:477	FH-catalysed fumarate in promoter regions inhibits KDM2A demethylase activity, and thus maintains the H3K36me2 profile and facilitates gene expression for cell growth arrest.
28628081	1	35	theme	histone	121:127	arg1	methylation					129:139	histone methylation	121:139	histone methylation	121:139	Chromatin-associated fumarase (FH) affects histone methylation via its metabolic activity.
28628081	5	36	theme	cancer	782:787	arg1	cells					789:793	cancer cells	782:793	cancer cells that display robust O-GlcNAc transferase (OGT) activity	782:849	On the other hand, FH is found to be O-GlcNAcylated at the AMPK phosphorylation site; FH-ATF2-mediated downstream events are impeded by FH O-GlcNAcylation, especially in cancer cells that display robust O-GlcNAc transferase (OGT) activity.
28628081	6	37	theme	OGT	931:933	arg1	level					935:939	OGT level	931:939	OGT level	931:939	Consistently, the FH-Ser75 phosphorylation level inversely correlates with the OGT level and poor prognosis in pancreatic cancer patients.
28628081	4	38	from	fumarate	450:457	arg1	regions					471:477	promoter regions	462:477	promoter regions	462:477	FH-catalysed fumarate in promoter regions inhibits KDM2A demethylase activity, and thus maintains the H3K36me2 profile and facilitates gene expression for cell growth arrest.
28628081	2	39	theme	gene	213:216	arg1	transcription					218:230	gene transcription	213:230	gene transcription	213:230	However, whether this effect is involved in gene transcription remains to be clarified.
28628081	7	40	theme	dysregulated	1119:1130	arg1	activity					1136:1143	dysregulated OGT activity	1119:1143	dysregulated OGT activity	1119:1143	These findings uncover a previously uncharacterized mechanism underlying transcription regulation by FH and the linkage between dysregulated OGT activity and growth advantage of cancer cells under glucose deficiency.
28628081	7	41	theme	uncharacterized	1027:1041	arg1	mechanism					1043:1051	a previously uncharacterized mechanism	1014:1051	a previously uncharacterized mechanism underlying transcription regulation by FH and the linkage between dysregulated OGT activity and growth advantage of cancer cells under glucose deficiency	1014:1205	These findings uncover a previously uncharacterized mechanism underlying transcription regulation by FH and the linkage between dysregulated OGT activity and growth advantage of cancer cells under glucose deficiency.
28628081	6	42	from	level	935:939	arg1	patients					981:988	pancreatic cancer patients	963:988	pancreatic cancer patients	963:988	Consistently, the FH-Ser75 phosphorylation level inversely correlates with the OGT level and poor prognosis in pancreatic cancer patients.
28628081	5	43	from	impeded	737:743	arg1	cells					789:793	cancer cells	782:793	cancer cells that display robust O-GlcNAc transferase (OGT) activity	782:849	On the other hand, FH is found to be O-GlcNAcylated at the AMPK phosphorylation site; FH-ATF2-mediated downstream events are impeded by FH O-GlcNAcylation, especially in cancer cells that display robust O-GlcNAc transferase (OGT) activity.
28628081	4	44	theme	growth	597:602	arg1	arrest					604:609	cell growth arrest	592:609	cell growth arrest	592:609	FH-catalysed fumarate in promoter regions inhibits KDM2A demethylase activity, and thus maintains the H3K36me2 profile and facilitates gene expression for cell growth arrest.
28628081	1	45	theme	metabolic	149:157	arg1	activity					159:166	its metabolic activity	145:166	its metabolic activity	145:166	Chromatin-associated fumarase (FH) affects histone methylation via its metabolic activity.
28628081	5	46	located	found	637:641	arg1	hand					625:628	the other hand	615:628	the other hand	615:628	On the other hand, FH is found to be O-GlcNAcylated at the AMPK phosphorylation site; FH-ATF2-mediated downstream events are impeded by FH O-GlcNAcylation, especially in cancer cells that display robust O-GlcNAc transferase (OGT) activity.
28628081	5	46	located	found	637:641	arg2	FH					631:632	FH	631:632	FH	631:632	On the other hand, FH is found to be O-GlcNAcylated at the AMPK phosphorylation site; FH-ATF2-mediated downstream events are impeded by FH O-GlcNAcylation, especially in cancer cells that display robust O-GlcNAc transferase (OGT) activity.
28628081	4	47	theme	demethylase	494:504	arg1	activity					506:513	KDM2A demethylase activity	488:513	KDM2A demethylase activity	488:513	FH-catalysed fumarate in promoter regions inhibits KDM2A demethylase activity, and thus maintains the H3K36me2 profile and facilitates gene expression for cell growth arrest.
28628081	5	48	theme	robust	808:813	arg1	activity					842:849	robust O-GlcNAc transferase (OGT) activity	808:849	robust O-GlcNAc transferase (OGT) activity	808:849	On the other hand, FH is found to be O-GlcNAcylated at the AMPK phosphorylation site; FH-ATF2-mediated downstream events are impeded by FH O-GlcNAcylation, especially in cancer cells that display robust O-GlcNAc transferase (OGT) activity.
28628081	6	49	from	prognosis	950:958	arg1	patients					981:988	pancreatic cancer patients	963:988	pancreatic cancer patients	963:988	Consistently, the FH-Ser75 phosphorylation level inversely correlates with the OGT level and poor prognosis in pancreatic cancer patients.
28628081	7	50	theme	glucose	1188:1194	arg1	deficiency					1196:1205	glucose deficiency	1188:1205	glucose deficiency	1188:1205	These findings uncover a previously uncharacterized mechanism underlying transcription regulation by FH and the linkage between dysregulated OGT activity and growth advantage of cancer cells under glucose deficiency.
23776238	4	0	theme	B-cell-activating	945:961	arg1	BAFF					971:974	BAFF	971:974	BAFF	971:974	We then investigated the effect of N-glycosylation on the function of BCMA and found that the dexamethasone-induced apoptosis in malignant plasma cells can be rescued by treatment with BCMA ligands, such as a proliferation-inducing ligand (APRIL) and B-cell-activating factor (BAFF), whereas removal of terminal sialic acid on plasma cells further potentiated the ligand-mediated protection.
23776238	4	0	theme	B-cell-activating	945:961	arg1	factor					963:968	B-cell-activating factor	945:968	B-cell-activating factor (BAFF)	945:975	We then investigated the effect of N-glycosylation on the function of BCMA and found that the dexamethasone-induced apoptosis in malignant plasma cells can be rescued by treatment with BCMA ligands, such as a proliferation-inducing ligand (APRIL) and B-cell-activating factor (BAFF), whereas removal of terminal sialic acid on plasma cells further potentiated the ligand-mediated protection.
23776238	1	1	theme	plasma	275:280	arg1	cells					282:286	plasma cells	275:286	plasma cells	275:286	Glycosylation, an important posttranslational modification process, can modulate the structure and function of proteins, but its effect on the properties of plasma cells is largely unknown.
23776238	1	2	theme	posttranslational	146:162	arg1	Glycosylation					118:130	Glycosylation	118:130	Glycosylation	118:130	Glycosylation, an important posttranslational modification process, can modulate the structure and function of proteins, but its effect on the properties of plasma cells is largely unknown.
23776238	1	2	theme	posttranslational	146:162	arg1	process					177:183	an important posttranslational modification process	133:183	an important posttranslational modification process	133:183	Glycosylation, an important posttranslational modification process, can modulate the structure and function of proteins, but its effect on the properties of plasma cells is largely unknown.
23776238	4	3	theme	terminal	997:1004	arg1	acid					1013:1016	terminal sialic acid	997:1016	terminal sialic acid on plasma cells	997:1032	We then investigated the effect of N-glycosylation on the function of BCMA and found that the dexamethasone-induced apoptosis in malignant plasma cells can be rescued by treatment with BCMA ligands, such as a proliferation-inducing ligand (APRIL) and B-cell-activating factor (BAFF), whereas removal of terminal sialic acid on plasma cells further potentiated the ligand-mediated protection.
23776238	7	4	theme	plasma	1476:1481	arg1	cells					1483:1487	plasma cells	1476:1487	plasma cells	1476:1487	Together, our results highlight the importance of N-glycosylation on BCMA in the regulation of ligand binding and functions of plasma cells.
23776238	6	5	theme	BCMA	1301:1304	arg1	binding					1290:1296	the binding	1286:1296	the binding of BCMA with ligands	1286:1317	In addition, the α1-3,-4 fucosylation, but not the terminal sialylation, assists the binding of BCMA with ligands in an in vitro binding assay.
23776238	3	6	theme	single	650:655	arg1	site					673:676	a single N-glycosylation site	648:676	a single N-glycosylation site	648:676	The B-cell maturation antigen (BCMA), an essential membrane protein for maintaining the survival of plasma cells, was identified as a glycoprotein exhibiting complex-type N-glycans at a single N-glycosylation site, asparagine 42.
23776238	3	6	theme	single	650:655	arg1	asparagine					679:688	asparagine 42	679:691	asparagine 42	679:691	The B-cell maturation antigen (BCMA), an essential membrane protein for maintaining the survival of plasma cells, was identified as a glycoprotein exhibiting complex-type N-glycans at a single N-glycosylation site, asparagine 42.
23776238	1	7	theme	modification	164:175	arg1	Glycosylation					118:130	Glycosylation	118:130	Glycosylation	118:130	Glycosylation, an important posttranslational modification process, can modulate the structure and function of proteins, but its effect on the properties of plasma cells is largely unknown.
23776238	1	7	theme	modification	164:175	arg1	process					177:183	an important posttranslational modification process	133:183	an important posttranslational modification process	133:183	Glycosylation, an important posttranslational modification process, can modulate the structure and function of proteins, but its effect on the properties of plasma cells is largely unknown.
23776238	3	8	gly	glycoprotein	598:609	arg1	glycoprotein					598:609	a glycoprotein	596:609	a glycoprotein exhibiting complex-type N-glycans at a single N-glycosylation site, asparagine 42	596:691	The B-cell maturation antigen (BCMA), an essential membrane protein for maintaining the survival of plasma cells, was identified as a glycoprotein exhibiting complex-type N-glycans at a single N-glycosylation site, asparagine 42.
23776238	3	8	gly	glycoprotein	598:609	arg1	antigen					486:492	B-cell maturation antigen	468:492	The B-cell maturation antigen (BCMA)	464:499	The B-cell maturation antigen (BCMA), an essential membrane protein for maintaining the survival of plasma cells, was identified as a glycoprotein exhibiting complex-type N-glycans at a single N-glycosylation site, asparagine 42.
23776238	4	9	theme	proliferation-inducing	903:924	arg1	ligand					926:931	a proliferation-inducing ligand	901:931	a proliferation-inducing ligand (APRIL)	901:939	We then investigated the effect of N-glycosylation on the function of BCMA and found that the dexamethasone-induced apoptosis in malignant plasma cells can be rescued by treatment with BCMA ligands, such as a proliferation-inducing ligand (APRIL) and B-cell-activating factor (BAFF), whereas removal of terminal sialic acid on plasma cells further potentiated the ligand-mediated protection.
23776238	4	9	theme	proliferation-inducing	903:924	arg1	APRIL					934:938	APRIL	934:938	APRIL	934:938	We then investigated the effect of N-glycosylation on the function of BCMA and found that the dexamethasone-induced apoptosis in malignant plasma cells can be rescued by treatment with BCMA ligands, such as a proliferation-inducing ligand (APRIL) and B-cell-activating factor (BAFF), whereas removal of terminal sialic acid on plasma cells further potentiated the ligand-mediated protection.
23776238	3	10	theme	N-glycosylation	657:671	arg1	site					673:676	a single N-glycosylation site	648:676	a single N-glycosylation site	648:676	The B-cell maturation antigen (BCMA), an essential membrane protein for maintaining the survival of plasma cells, was identified as a glycoprotein exhibiting complex-type N-glycans at a single N-glycosylation site, asparagine 42.
23776238	3	10	theme	N-glycosylation	657:671	arg1	asparagine					679:688	asparagine 42	679:691	asparagine 42	679:691	The B-cell maturation antigen (BCMA), an essential membrane protein for maintaining the survival of plasma cells, was identified as a glycoprotein exhibiting complex-type N-glycans at a single N-glycosylation site, asparagine 42.
23776238	6	11	theme	α1-3	1222:1225	arg1	fucosylation					1230:1241	the α1-3,-4 fucosylation	1218:1241	fucosylation	1230:1241	In addition, the α1-3,-4 fucosylation, but not the terminal sialylation, assists the binding of BCMA with ligands in an in vitro binding assay.
23776238	4	12	theme	N-glycosylation	729:743	arg1	effect					719:724	the effect	715:724	the effect of N-glycosylation on the function of BCMA	715:767	We then investigated the effect of N-glycosylation on the function of BCMA and found that the dexamethasone-induced apoptosis in malignant plasma cells can be rescued by treatment with BCMA ligands, such as a proliferation-inducing ligand (APRIL) and B-cell-activating factor (BAFF), whereas removal of terminal sialic acid on plasma cells further potentiated the ligand-mediated protection.
23776238	4	13	theme	acid	1013:1016	arg1	removal					986:992	removal	986:992	removal of terminal sialic acid on plasma cells	986:1032	We then investigated the effect of N-glycosylation on the function of BCMA and found that the dexamethasone-induced apoptosis in malignant plasma cells can be rescued by treatment with BCMA ligands, such as a proliferation-inducing ligand (APRIL) and B-cell-activating factor (BAFF), whereas removal of terminal sialic acid on plasma cells further potentiated the ligand-mediated protection.
23776238	7	14	theme	functions	1463:1471	arg1	regulation					1430:1439	the regulation	1426:1439	the regulation of ligand binding and functions of plasma cells	1426:1487	Together, our results highlight the importance of N-glycosylation on BCMA in the regulation of ligand binding and functions of plasma cells.
23776238	0	15	theme	ligand	80:85	arg1	binding					87:93	ligand binding	80:93	ligand binding	80:93	B-cell maturation antigen is modified by a single N-glycan chain that modulates ligand binding and surface retention.
23776238	7	16	theme	ligand	1444:1449	arg1	binding					1451:1457	ligand binding	1444:1457	ligand binding	1444:1457	Together, our results highlight the importance of N-glycosylation on BCMA in the regulation of ligand binding and functions of plasma cells.
23776238	3	17	theme	essential	505:513	arg1	protein					524:530	an essential membrane protein	502:530	an essential membrane protein for maintaining the survival of plasma cells	502:575	The B-cell maturation antigen (BCMA), an essential membrane protein for maintaining the survival of plasma cells, was identified as a glycoprotein exhibiting complex-type N-glycans at a single N-glycosylation site, asparagine 42.
23776238	3	17	theme	essential	505:513	arg1	antigen					486:492	B-cell maturation antigen	468:492	The B-cell maturation antigen (BCMA)	464:499	The B-cell maturation antigen (BCMA), an essential membrane protein for maintaining the survival of plasma cells, was identified as a glycoprotein exhibiting complex-type N-glycans at a single N-glycosylation site, asparagine 42.
23776238	3	18	theme	maturation	475:484	arg1	glycoprotein					598:609	a glycoprotein	596:609	a glycoprotein exhibiting complex-type N-glycans at a single N-glycosylation site, asparagine 42	596:691	The B-cell maturation antigen (BCMA), an essential membrane protein for maintaining the survival of plasma cells, was identified as a glycoprotein exhibiting complex-type N-glycans at a single N-glycosylation site, asparagine 42.
23776238	3	18	theme	maturation	475:484	arg1	antigen					486:492	B-cell maturation antigen	468:492	The B-cell maturation antigen (BCMA)	464:499	The B-cell maturation antigen (BCMA), an essential membrane protein for maintaining the survival of plasma cells, was identified as a glycoprotein exhibiting complex-type N-glycans at a single N-glycosylation site, asparagine 42.
23776238	3	18	theme	maturation	475:484	arg1	protein					524:530	an essential membrane protein	502:530	an essential membrane protein for maintaining the survival of plasma cells	502:575	The B-cell maturation antigen (BCMA), an essential membrane protein for maintaining the survival of plasma cells, was identified as a glycoprotein exhibiting complex-type N-glycans at a single N-glycosylation site, asparagine 42.
23776238	3	18	theme	maturation	475:484	arg1	BCMA					495:498	BCMA	495:498	BCMA	495:498	The B-cell maturation antigen (BCMA), an essential membrane protein for maintaining the survival of plasma cells, was identified as a glycoprotein exhibiting complex-type N-glycans at a single N-glycosylation site, asparagine 42.
23776238	7	19	theme	cells	1483:1487	arg1	functions					1463:1471	functions	1463:1471	functions of plasma cells	1463:1487	Together, our results highlight the importance of N-glycosylation on BCMA in the regulation of ligand binding and functions of plasma cells.
23776238	7	19	theme	cells	1483:1487	arg1	binding					1451:1457	ligand binding	1444:1457	ligand binding	1444:1457	Together, our results highlight the importance of N-glycosylation on BCMA in the regulation of ligand binding and functions of plasma cells.
23776238	5	20	theme	elevated	1173:1180	arg1	level					1182:1186	its elevated level	1169:1186	its elevated level on cell surface	1169:1202	This effect is associated with the increased surface retention of BCMA, leading to its elevated level on cell surface.
23776238	0	21	theme	surface	99:105	arg1	retention					107:115	surface retention	99:115	surface retention	99:115	B-cell maturation antigen is modified by a single N-glycan chain that modulates ligand binding and surface retention.
23776238	2	22	with	reaction	371:378	arg1	analogs					399:405	alkynyl sugar analogs	385:405	alkynyl sugar analogs	385:405	In this study, we identified a panel of glycoproteins by click reaction with alkynyl sugar analogs in plasma cells coupled with mass spectrometry analysis.
23776238	2	23	theme	click	365:369	arg1	reaction					371:378	click reaction	365:378	click reaction with alkynyl sugar analogs in plasma cells coupled with mass spectrometry analysis	365:461	In this study, we identified a panel of glycoproteins by click reaction with alkynyl sugar analogs in plasma cells coupled with mass spectrometry analysis.
23776238	6	24	theme	binding	1334:1340	arg1	assay					1342:1346	an in vitro binding assay	1322:1346	an in vitro binding assay	1322:1346	In addition, the α1-3,-4 fucosylation, but not the terminal sialylation, assists the binding of BCMA with ligands in an in vitro binding assay.
23776238	4	25	from	effect	719:724	arg1	function					752:759	the function	748:759	the function of BCMA	748:767	We then investigated the effect of N-glycosylation on the function of BCMA and found that the dexamethasone-induced apoptosis in malignant plasma cells can be rescued by treatment with BCMA ligands, such as a proliferation-inducing ligand (APRIL) and B-cell-activating factor (BAFF), whereas removal of terminal sialic acid on plasma cells further potentiated the ligand-mediated protection.
23776238	0	26	theme	B-cell	0:5	arg1	antigen					18:24	B-cell maturation antigen	0:24	B-cell maturation antigen	0:24	B-cell maturation antigen is modified by a single N-glycan chain that modulates ligand binding and surface retention.
23776238	5	27	theme	increased	1121:1129	arg1	retention					1139:1147	the increased surface retention	1117:1147	the increased surface retention of BCMA	1117:1155	This effect is associated with the increased surface retention of BCMA, leading to its elevated level on cell surface.
23776238	0	28	theme	maturation	7:16	arg1	antigen					18:24	B-cell maturation antigen	0:24	B-cell maturation antigen	0:24	B-cell maturation antigen is modified by a single N-glycan chain that modulates ligand binding and surface retention.
23776238	4	29	from	apoptosis	810:818	arg1	cells					840:844	malignant plasma cells	823:844	malignant plasma cells	823:844	We then investigated the effect of N-glycosylation on the function of BCMA and found that the dexamethasone-induced apoptosis in malignant plasma cells can be rescued by treatment with BCMA ligands, such as a proliferation-inducing ligand (APRIL) and B-cell-activating factor (BAFF), whereas removal of terminal sialic acid on plasma cells further potentiated the ligand-mediated protection.
23776238	4	30	theme	plasma	833:838	arg1	cells					840:844	malignant plasma cells	823:844	malignant plasma cells	823:844	We then investigated the effect of N-glycosylation on the function of BCMA and found that the dexamethasone-induced apoptosis in malignant plasma cells can be rescued by treatment with BCMA ligands, such as a proliferation-inducing ligand (APRIL) and B-cell-activating factor (BAFF), whereas removal of terminal sialic acid on plasma cells further potentiated the ligand-mediated protection.
23776238	6	31	with	BCMA	1301:1304	arg1	ligands					1311:1317	ligands	1311:1317	ligands	1311:1317	In addition, the α1-3,-4 fucosylation, but not the terminal sialylation, assists the binding of BCMA with ligands in an in vitro binding assay.
23776238	2	32	theme	glycoproteins	348:360	arg1	panel					339:343	a panel	337:343	a panel of glycoproteins	337:360	In this study, we identified a panel of glycoproteins by click reaction with alkynyl sugar analogs in plasma cells coupled with mass spectrometry analysis.
23776238	2	33	theme	plasma	410:415	arg1	cells					417:421	plasma cells	410:421	plasma cells coupled with mass spectrometry analysis	410:461	In this study, we identified a panel of glycoproteins by click reaction with alkynyl sugar analogs in plasma cells coupled with mass spectrometry analysis.
23776238	2	34	gly	glycoproteins	348:360	arg1	glycoproteins					348:360	glycoproteins	348:360	glycoproteins	348:360	In this study, we identified a panel of glycoproteins by click reaction with alkynyl sugar analogs in plasma cells coupled with mass spectrometry analysis.
23776238	5	35	from	level	1182:1186	arg1	surface					1196:1202	cell surface	1191:1202	cell surface	1191:1202	This effect is associated with the increased surface retention of BCMA, leading to its elevated level on cell surface.
23776238	4	36	theme	ligand-mediated	1058:1072	arg1	protection					1074:1083	the ligand-mediated protection	1054:1083	the ligand-mediated protection	1054:1083	We then investigated the effect of N-glycosylation on the function of BCMA and found that the dexamethasone-induced apoptosis in malignant plasma cells can be rescued by treatment with BCMA ligands, such as a proliferation-inducing ligand (APRIL) and B-cell-activating factor (BAFF), whereas removal of terminal sialic acid on plasma cells further potentiated the ligand-mediated protection.
23776238	6	37	theme	in	1325:1326	arg1	assay					1342:1346	an in vitro binding assay	1322:1346	an in vitro binding assay	1322:1346	In addition, the α1-3,-4 fucosylation, but not the terminal sialylation, assists the binding of BCMA with ligands in an in vitro binding assay.
23776238	4	38	from	removal	986:992	arg1	cells					1028:1032	plasma cells	1021:1032	plasma cells	1021:1032	We then investigated the effect of N-glycosylation on the function of BCMA and found that the dexamethasone-induced apoptosis in malignant plasma cells can be rescued by treatment with BCMA ligands, such as a proliferation-inducing ligand (APRIL) and B-cell-activating factor (BAFF), whereas removal of terminal sialic acid on plasma cells further potentiated the ligand-mediated protection.
23776238	6	39	dep	in	1325:1326	arg1	vitro					1328:1332	vitro	1328:1332	vitro	1328:1332	In addition, the α1-3,-4 fucosylation, but not the terminal sialylation, assists the binding of BCMA with ligands in an in vitro binding assay.
23776238	3	40	theme	membrane	515:522	arg1	protein					524:530	an essential membrane protein	502:530	an essential membrane protein for maintaining the survival of plasma cells	502:575	The B-cell maturation antigen (BCMA), an essential membrane protein for maintaining the survival of plasma cells, was identified as a glycoprotein exhibiting complex-type N-glycans at a single N-glycosylation site, asparagine 42.
23776238	3	40	theme	membrane	515:522	arg1	antigen					486:492	B-cell maturation antigen	468:492	The B-cell maturation antigen (BCMA)	464:499	The B-cell maturation antigen (BCMA), an essential membrane protein for maintaining the survival of plasma cells, was identified as a glycoprotein exhibiting complex-type N-glycans at a single N-glycosylation site, asparagine 42.
23776238	2	41	theme	sugar	393:397	arg1	analogs					399:405	alkynyl sugar analogs	385:405	alkynyl sugar analogs	385:405	In this study, we identified a panel of glycoproteins by click reaction with alkynyl sugar analogs in plasma cells coupled with mass spectrometry analysis.
23776238	0	42	mod	modified	29:36	arg1	antigen					18:24	B-cell maturation antigen	0:24	B-cell maturation antigen	0:24	B-cell maturation antigen is modified by a single N-glycan chain that modulates ligand binding and surface retention.
23776238	0	42	mod	modified	29:36	arg3	chain					59:63	a single N-glycan chain	41:63	a single N-glycan chain that modulates ligand binding and surface retention	41:115	B-cell maturation antigen is modified by a single N-glycan chain that modulates ligand binding and surface retention.
23776238	5	43	theme	BCMA	1152:1155	arg1	retention					1139:1147	the increased surface retention	1117:1147	the increased surface retention of BCMA	1117:1155	This effect is associated with the increased surface retention of BCMA, leading to its elevated level on cell surface.
23776238	4	44	with	treatment	864:872	arg1	ligand					926:931	a proliferation-inducing ligand	901:931	a proliferation-inducing ligand (APRIL)	901:939	We then investigated the effect of N-glycosylation on the function of BCMA and found that the dexamethasone-induced apoptosis in malignant plasma cells can be rescued by treatment with BCMA ligands, such as a proliferation-inducing ligand (APRIL) and B-cell-activating factor (BAFF), whereas removal of terminal sialic acid on plasma cells further potentiated the ligand-mediated protection.
23776238	4	44	with	treatment	864:872	arg1	factor					963:968	B-cell-activating factor	945:968	B-cell-activating factor (BAFF)	945:975	We then investigated the effect of N-glycosylation on the function of BCMA and found that the dexamethasone-induced apoptosis in malignant plasma cells can be rescued by treatment with BCMA ligands, such as a proliferation-inducing ligand (APRIL) and B-cell-activating factor (BAFF), whereas removal of terminal sialic acid on plasma cells further potentiated the ligand-mediated protection.
23776238	4	44	with	treatment	864:872	arg1	ligands					884:890	BCMA ligands	879:890	BCMA ligands	879:890	We then investigated the effect of N-glycosylation on the function of BCMA and found that the dexamethasone-induced apoptosis in malignant plasma cells can be rescued by treatment with BCMA ligands, such as a proliferation-inducing ligand (APRIL) and B-cell-activating factor (BAFF), whereas removal of terminal sialic acid on plasma cells further potentiated the ligand-mediated protection.
23776238	2	45	theme	alkynyl	385:391	arg1	analogs					399:405	alkynyl sugar analogs	385:405	alkynyl sugar analogs	385:405	In this study, we identified a panel of glycoproteins by click reaction with alkynyl sugar analogs in plasma cells coupled with mass spectrometry analysis.
23776238	2	46	theme	spectrometry	441:452	arg1	analysis					454:461	mass spectrometry analysis	436:461	mass spectrometry analysis	436:461	In this study, we identified a panel of glycoproteins by click reaction with alkynyl sugar analogs in plasma cells coupled with mass spectrometry analysis.
23776238	1	47	theme	cells	282:286	arg1	properties					261:270	the properties	257:270	the properties of plasma cells	257:286	Glycosylation, an important posttranslational modification process, can modulate the structure and function of proteins, but its effect on the properties of plasma cells is largely unknown.
23776238	6	48	theme	terminal	1256:1263	arg1	sialylation					1265:1275	the terminal sialylation	1252:1275	the terminal sialylation	1252:1275	In addition, the α1-3,-4 fucosylation, but not the terminal sialylation, assists the binding of BCMA with ligands in an in vitro binding assay.
23776238	7	49	from	importance	1385:1394	arg1	BCMA					1418:1421	BCMA	1418:1421	BCMA	1418:1421	Together, our results highlight the importance of N-glycosylation on BCMA in the regulation of ligand binding and functions of plasma cells.
23776238	2	50	theme	mass	436:439	arg1	spectrometry					441:452	mass spectrometry	436:452	mass spectrometry analysis	436:461	In this study, we identified a panel of glycoproteins by click reaction with alkynyl sugar analogs in plasma cells coupled with mass spectrometry analysis.
23776238	1	51	from	effect	247:252	arg1	properties					261:270	the properties	257:270	the properties of plasma cells	257:286	Glycosylation, an important posttranslational modification process, can modulate the structure and function of proteins, but its effect on the properties of plasma cells is largely unknown.
23776238	3	52	theme	plasma	564:569	arg1	cells					571:575	plasma cells	564:575	plasma cells	564:575	The B-cell maturation antigen (BCMA), an essential membrane protein for maintaining the survival of plasma cells, was identified as a glycoprotein exhibiting complex-type N-glycans at a single N-glycosylation site, asparagine 42.
23776238	5	53	theme	surface	1131:1137	arg1	retention					1139:1147	the increased surface retention	1117:1147	the increased surface retention of BCMA	1117:1155	This effect is associated with the increased surface retention of BCMA, leading to its elevated level on cell surface.
23776238	0	54	theme	single	43:48	arg1	chain					59:63	a single N-glycan chain	41:63	a single N-glycan chain that modulates ligand binding and surface retention	41:115	B-cell maturation antigen is modified by a single N-glycan chain that modulates ligand binding and surface retention.
23776238	4	55	gly	N-glycosylation	729:743	arg1	BCMA					764:767	BCMA	764:767	BCMA	764:767	We then investigated the effect of N-glycosylation on the function of BCMA and found that the dexamethasone-induced apoptosis in malignant plasma cells can be rescued by treatment with BCMA ligands, such as a proliferation-inducing ligand (APRIL) and B-cell-activating factor (BAFF), whereas removal of terminal sialic acid on plasma cells further potentiated the ligand-mediated protection.
23776238	4	56	theme	dexamethasone-induced	788:808	arg1	apoptosis					810:818	the dexamethasone-induced apoptosis	784:818	the dexamethasone-induced apoptosis in malignant plasma cells	784:844	We then investigated the effect of N-glycosylation on the function of BCMA and found that the dexamethasone-induced apoptosis in malignant plasma cells can be rescued by treatment with BCMA ligands, such as a proliferation-inducing ligand (APRIL) and B-cell-activating factor (BAFF), whereas removal of terminal sialic acid on plasma cells further potentiated the ligand-mediated protection.
23776238	4	57	theme	malignant	823:831	arg1	cells					840:844	malignant plasma cells	823:844	malignant plasma cells	823:844	We then investigated the effect of N-glycosylation on the function of BCMA and found that the dexamethasone-induced apoptosis in malignant plasma cells can be rescued by treatment with BCMA ligands, such as a proliferation-inducing ligand (APRIL) and B-cell-activating factor (BAFF), whereas removal of terminal sialic acid on plasma cells further potentiated the ligand-mediated protection.
23776238	3	58	gly	N-glycosylation	657:671	arg2	asparagine					679:688	asparagine 42	679:691	asparagine 42	679:691	The B-cell maturation antigen (BCMA), an essential membrane protein for maintaining the survival of plasma cells, was identified as a glycoprotein exhibiting complex-type N-glycans at a single N-glycosylation site, asparagine 42.
23776238	3	58	gly	N-glycosylation	657:671	arg2	site					673:676	a single N-glycosylation site	648:676	a single N-glycosylation site	648:676	The B-cell maturation antigen (BCMA), an essential membrane protein for maintaining the survival of plasma cells, was identified as a glycoprotein exhibiting complex-type N-glycans at a single N-glycosylation site, asparagine 42.
23776238	3	59	theme	B-cell	468:473	arg1	glycoprotein					598:609	a glycoprotein	596:609	a glycoprotein exhibiting complex-type N-glycans at a single N-glycosylation site, asparagine 42	596:691	The B-cell maturation antigen (BCMA), an essential membrane protein for maintaining the survival of plasma cells, was identified as a glycoprotein exhibiting complex-type N-glycans at a single N-glycosylation site, asparagine 42.
23776238	3	59	theme	B-cell	468:473	arg1	antigen					486:492	B-cell maturation antigen	468:492	The B-cell maturation antigen (BCMA)	464:499	The B-cell maturation antigen (BCMA), an essential membrane protein for maintaining the survival of plasma cells, was identified as a glycoprotein exhibiting complex-type N-glycans at a single N-glycosylation site, asparagine 42.
23776238	3	59	theme	B-cell	468:473	arg1	protein					524:530	an essential membrane protein	502:530	an essential membrane protein for maintaining the survival of plasma cells	502:575	The B-cell maturation antigen (BCMA), an essential membrane protein for maintaining the survival of plasma cells, was identified as a glycoprotein exhibiting complex-type N-glycans at a single N-glycosylation site, asparagine 42.
23776238	3	59	theme	B-cell	468:473	arg1	BCMA					495:498	BCMA	495:498	BCMA	495:498	The B-cell maturation antigen (BCMA), an essential membrane protein for maintaining the survival of plasma cells, was identified as a glycoprotein exhibiting complex-type N-glycans at a single N-glycosylation site, asparagine 42.
23776238	4	60	theme	BCMA	764:767	arg1	function					752:759	the function	748:759	the function of BCMA	748:767	We then investigated the effect of N-glycosylation on the function of BCMA and found that the dexamethasone-induced apoptosis in malignant plasma cells can be rescued by treatment with BCMA ligands, such as a proliferation-inducing ligand (APRIL) and B-cell-activating factor (BAFF), whereas removal of terminal sialic acid on plasma cells further potentiated the ligand-mediated protection.
23776238	4	61	theme	BCMA	879:882	arg1	ligand					926:931	a proliferation-inducing ligand	901:931	a proliferation-inducing ligand (APRIL)	901:939	We then investigated the effect of N-glycosylation on the function of BCMA and found that the dexamethasone-induced apoptosis in malignant plasma cells can be rescued by treatment with BCMA ligands, such as a proliferation-inducing ligand (APRIL) and B-cell-activating factor (BAFF), whereas removal of terminal sialic acid on plasma cells further potentiated the ligand-mediated protection.
23776238	4	61	theme	BCMA	879:882	arg1	factor					963:968	B-cell-activating factor	945:968	B-cell-activating factor (BAFF)	945:975	We then investigated the effect of N-glycosylation on the function of BCMA and found that the dexamethasone-induced apoptosis in malignant plasma cells can be rescued by treatment with BCMA ligands, such as a proliferation-inducing ligand (APRIL) and B-cell-activating factor (BAFF), whereas removal of terminal sialic acid on plasma cells further potentiated the ligand-mediated protection.
23776238	4	61	theme	BCMA	879:882	arg1	ligands					884:890	BCMA ligands	879:890	BCMA ligands	879:890	We then investigated the effect of N-glycosylation on the function of BCMA and found that the dexamethasone-induced apoptosis in malignant plasma cells can be rescued by treatment with BCMA ligands, such as a proliferation-inducing ligand (APRIL) and B-cell-activating factor (BAFF), whereas removal of terminal sialic acid on plasma cells further potentiated the ligand-mediated protection.
23776238	4	62	from	cells	1028:1032	arg1	removal					986:992	removal	986:992	removal of terminal sialic acid on plasma cells	986:1032	We then investigated the effect of N-glycosylation on the function of BCMA and found that the dexamethasone-induced apoptosis in malignant plasma cells can be rescued by treatment with BCMA ligands, such as a proliferation-inducing ligand (APRIL) and B-cell-activating factor (BAFF), whereas removal of terminal sialic acid on plasma cells further potentiated the ligand-mediated protection.
23776238	4	63	theme	plasma	1021:1026	arg1	cells					1028:1032	plasma cells	1021:1032	plasma cells	1021:1032	We then investigated the effect of N-glycosylation on the function of BCMA and found that the dexamethasone-induced apoptosis in malignant plasma cells can be rescued by treatment with BCMA ligands, such as a proliferation-inducing ligand (APRIL) and B-cell-activating factor (BAFF), whereas removal of terminal sialic acid on plasma cells further potentiated the ligand-mediated protection.
23776238	3	64	theme	complex-type	622:633	arg1	N-glycans					635:643	complex-type N-glycans	622:643	complex-type N-glycans	622:643	The B-cell maturation antigen (BCMA), an essential membrane protein for maintaining the survival of plasma cells, was identified as a glycoprotein exhibiting complex-type N-glycans at a single N-glycosylation site, asparagine 42.
23776238	4	65	from	acid	1013:1016	arg1	cells					1028:1032	plasma cells	1021:1032	plasma cells	1021:1032	We then investigated the effect of N-glycosylation on the function of BCMA and found that the dexamethasone-induced apoptosis in malignant plasma cells can be rescued by treatment with BCMA ligands, such as a proliferation-inducing ligand (APRIL) and B-cell-activating factor (BAFF), whereas removal of terminal sialic acid on plasma cells further potentiated the ligand-mediated protection.
23776238	1	66	theme	proteins	229:236	arg1	structure					203:211	structure	203:211	structure	203:211	Glycosylation, an important posttranslational modification process, can modulate the structure and function of proteins, but its effect on the properties of plasma cells is largely unknown.
23776238	1	66	theme	proteins	229:236	arg1	function					217:224	function	217:224	function	217:224	Glycosylation, an important posttranslational modification process, can modulate the structure and function of proteins, but its effect on the properties of plasma cells is largely unknown.
23776238	3	67	theme	cells	571:575	arg1	survival					552:559	the survival	548:559	the survival of plasma cells	548:575	The B-cell maturation antigen (BCMA), an essential membrane protein for maintaining the survival of plasma cells, was identified as a glycoprotein exhibiting complex-type N-glycans at a single N-glycosylation site, asparagine 42.
23776238	2	68	from	reaction	371:378	arg1	cells					417:421	plasma cells	410:421	plasma cells coupled with mass spectrometry analysis	410:461	In this study, we identified a panel of glycoproteins by click reaction with alkynyl sugar analogs in plasma cells coupled with mass spectrometry analysis.
23776238	5	69	theme	cell	1191:1194	arg1	surface					1196:1202	cell surface	1191:1202	cell surface	1191:1202	This effect is associated with the increased surface retention of BCMA, leading to its elevated level on cell surface.
23776238	0	70	theme	N-glycan	50:57	arg1	chain					59:63	a single N-glycan chain	41:63	a single N-glycan chain that modulates ligand binding and surface retention	41:115	B-cell maturation antigen is modified by a single N-glycan chain that modulates ligand binding and surface retention.
23776238	7	71	theme	N-glycosylation	1399:1413	arg1	importance					1385:1394	the importance	1381:1394	the importance of N-glycosylation on BCMA	1381:1421	Together, our results highlight the importance of N-glycosylation on BCMA in the regulation of ligand binding and functions of plasma cells.
23776238	1	72	dep	structure	203:211	arg1	the					199:201	the	199:201	the	199:201	Glycosylation, an important posttranslational modification process, can modulate the structure and function of proteins, but its effect on the properties of plasma cells is largely unknown.
23776238	1	73	theme	important	136:144	arg1	Glycosylation					118:130	Glycosylation	118:130	Glycosylation	118:130	Glycosylation, an important posttranslational modification process, can modulate the structure and function of proteins, but its effect on the properties of plasma cells is largely unknown.
23776238	1	73	theme	important	136:144	arg1	process					177:183	an important posttranslational modification process	133:183	an important posttranslational modification process	133:183	Glycosylation, an important posttranslational modification process, can modulate the structure and function of proteins, but its effect on the properties of plasma cells is largely unknown.
23776238	4	74	theme	sialic	1006:1011	arg1	acid					1013:1016	terminal sialic acid	997:1016	terminal sialic acid on plasma cells	997:1032	We then investigated the effect of N-glycosylation on the function of BCMA and found that the dexamethasone-induced apoptosis in malignant plasma cells can be rescued by treatment with BCMA ligands, such as a proliferation-inducing ligand (APRIL) and B-cell-activating factor (BAFF), whereas removal of terminal sialic acid on plasma cells further potentiated the ligand-mediated protection.
23776238	7	75	theme	binding	1451:1457	arg1	regulation					1430:1439	the regulation	1426:1439	the regulation of ligand binding and functions of plasma cells	1426:1487	Together, our results highlight the importance of N-glycosylation on BCMA in the regulation of ligand binding and functions of plasma cells.
25855029	6	0	theme	FA2G2S2	1119:1125	arg1	glycan					1128:1133	a core fucosylated biantennary digalactosylated disialylated (FA2G2S2) glycan	1057:1133	a core fucosylated biantennary digalactosylated disialylated (FA2G2S2) glycan	1057:1133	We determined the levels of targeted clusterin glycoforms containing either a biantennary digalactosylated disialylated (A2G2S2) glycan or a core fucosylated biantennary digalactosylated disialylated (FA2G2S2) glycan at N-glycosite N374.
25855029	8	1	from	levels	1382:1387	arg1	clusterin					1434:1442	plasma clusterin	1427:1442	plasma clusterin	1427:1442	Removal of ccRCC led to a significant increase in the levels of both FA2G2S2 and A2G2S2 glycans in plasma clusterin.
25855029	1	2	theme	disease	278:284	arg1	progression					286:296	disease progression	278:296	disease progression	278:296	Cancer-related alterations in protein glycosylation may serve as diagnostic or prognostic biomarkers or may be used for monitoring disease progression.
25855029	7	3	theme	patients	1258:1265	arg1	plasma					1248:1253	the plasma	1244:1253	the plasma of patients prior to	1244:1274	We showed that the presence of these two clusterin glycoforms differed significantly in the plasma of patients prior to and after curative nephrectomy for localized ccRCC.
25855029	10	4	theme	achievable	1674:1683	arg1	levels					1657:1662	levels	1657:1662	levels currently achievable	1657:1683	It is envisioned that these identified glycan alterations may provide an additional level of therapeutic or biomarker sensitivity than levels currently achievable by monitoring expression differences alone.
25855029	3	5	theme	patients	536:543	arg1	plasma					520:525	the plasma	516:525	the plasma of ccRCC patients	516:543	We recently reported that the N-glycan profile of clusterin is altered in the plasma of ccRCC patients.
25855029	5	6	theme	samples	850:856	arg1	spectrometry					803:814	tandem mass spectrometry	791:814	tandem mass spectrometry of immunoaffinity-enriched plasma samples	791:856	To this end, we used tandem mass spectrometry of immunoaffinity-enriched plasma samples to analyze the individual glycosylation sites in clusterin.
25855029	10	7	theme	therapeutic	1615:1625	arg1	level					1606:1610	an additional level	1592:1610	an additional level of therapeutic or biomarker sensitivity than levels currently achievable	1592:1683	It is envisioned that these identified glycan alterations may provide an additional level of therapeutic or biomarker sensitivity than levels currently achievable by monitoring expression differences alone.
25855029	1	8	theme	diagnostic	212:221	arg1	biomarkers					237:246	diagnostic or prognostic biomarkers	212:246	diagnostic or prognostic biomarkers	212:246	Cancer-related alterations in protein glycosylation may serve as diagnostic or prognostic biomarkers or may be used for monitoring disease progression.
25855029	1	8	theme	diagnostic	212:221	arg1	alterations					162:172	Cancer-related alterations	147:172	Cancer-related alterations in protein glycosylation	147:197	Cancer-related alterations in protein glycosylation may serve as diagnostic or prognostic biomarkers or may be used for monitoring disease progression.
25855029	6	9	theme	glycoforms	965:974	arg1	levels					936:941	the levels	932:941	the levels of targeted clusterin glycoforms containing either a biantennary digalactosylated disialylated (A2G2S2) glycan or a core fucosylated biantennary digalactosylated disialylated (FA2G2S2) glycan at N-glycosite N374	932:1153	We determined the levels of targeted clusterin glycoforms containing either a biantennary digalactosylated disialylated (A2G2S2) glycan or a core fucosylated biantennary digalactosylated disialylated (FA2G2S2) glycan at N-glycosite N374.
25855029	4	10	theme	sites	645:649	arg1	heterogeneity					601:613	heterogeneity	601:613	heterogeneity of individual N-glycosylation sites of clusterin	601:662	Here, we characterized the occupancy and the degree of heterogeneity of individual N-glycosylation sites of clusterin in the plasma of patients diagnosed with localized ccRCC, before and after curative nephrectomy (n = 40).
25855029	0	11	theme	cell	131:134	arg1	carcinoma					136:144	clear cell renal cell carcinoma	114:144	clear cell renal cell carcinoma	114:144	Clusterin glycopeptide variant characterization reveals significant site-specific glycan changes in the plasma of clear cell renal cell carcinoma.
25855029	1	12	theme	prognostic	226:235	arg1	biomarkers					237:246	diagnostic or prognostic biomarkers	212:246	diagnostic or prognostic biomarkers	212:246	Cancer-related alterations in protein glycosylation may serve as diagnostic or prognostic biomarkers or may be used for monitoring disease progression.
25855029	1	12	theme	prognostic	226:235	arg1	alterations					162:172	Cancer-related alterations	147:172	Cancer-related alterations in protein glycosylation	147:197	Cancer-related alterations in protein glycosylation may serve as diagnostic or prognostic biomarkers or may be used for monitoring disease progression.
25855029	6	13	theme	targeted	946:953	arg1	glycoforms					965:974	targeted clusterin glycoforms	946:974	targeted clusterin glycoforms containing either a biantennary digalactosylated disialylated (A2G2S2) glycan or a core fucosylated biantennary digalactosylated disialylated (FA2G2S2) glycan at N-glycosite N374	946:1153	We determined the levels of targeted clusterin glycoforms containing either a biantennary digalactosylated disialylated (A2G2S2) glycan or a core fucosylated biantennary digalactosylated disialylated (FA2G2S2) glycan at N-glycosite N374.
25855029	4	14	theme	clusterin	654:662	arg1	clusterin					654:662	clusterin	654:662	clusterin	654:662	Here, we characterized the occupancy and the degree of heterogeneity of individual N-glycosylation sites of clusterin in the plasma of patients diagnosed with localized ccRCC, before and after curative nephrectomy (n = 40).
25855029	4	14	theme	clusterin	654:662	arg1	sites					645:649	individual N-glycosylation sites	618:649	individual N-glycosylation sites of clusterin	618:662	Here, we characterized the occupancy and the degree of heterogeneity of individual N-glycosylation sites of clusterin in the plasma of patients diagnosed with localized ccRCC, before and after curative nephrectomy (n = 40).
25855029	5	15	theme	immunoaffinity-enriched	819:841	arg1	samples					850:856	immunoaffinity-enriched plasma samples	819:856	immunoaffinity-enriched plasma samples	819:856	To this end, we used tandem mass spectrometry of immunoaffinity-enriched plasma samples to analyze the individual glycosylation sites in clusterin.
25855029	0	16	from	changes	89:95	arg1	plasma					104:109	the plasma	100:109	the plasma of clear cell renal cell carcinoma	100:144	Clusterin glycopeptide variant characterization reveals significant site-specific glycan changes in the plasma of clear cell renal cell carcinoma.
25855029	10	17	theme	biomarker	1630:1638	arg1	sensitivity					1640:1650	biomarker sensitivity	1630:1650	biomarker sensitivity	1630:1650	It is envisioned that these identified glycan alterations may provide an additional level of therapeutic or biomarker sensitivity than levels currently achievable by monitoring expression differences alone.
25855029	9	18	theme	plasma	1504:1509	arg1	clusterin					1511:1519	plasma clusterin	1504:1519	plasma clusterin	1504:1519	These changes were further confirmed by lectin blotting of plasma clusterin.
25855029	1	19	theme	Cancer-related	147:160	arg1	biomarkers					237:246	diagnostic or prognostic biomarkers	212:246	diagnostic or prognostic biomarkers	212:246	Cancer-related alterations in protein glycosylation may serve as diagnostic or prognostic biomarkers or may be used for monitoring disease progression.
25855029	1	19	theme	Cancer-related	147:160	arg1	alterations					162:172	Cancer-related alterations	147:172	Cancer-related alterations in protein glycosylation	147:197	Cancer-related alterations in protein glycosylation may serve as diagnostic or prognostic biomarkers or may be used for monitoring disease progression.
25855029	8	20	theme	ccRCC	1339:1343	arg1	Removal					1328:1334	Removal	1328:1334	Removal of ccRCC	1328:1343	Removal of ccRCC led to a significant increase in the levels of both FA2G2S2 and A2G2S2 glycans in plasma clusterin.
25855029	5	21	theme	tandem	791:796	arg1	spectrometry					803:814	tandem mass spectrometry	791:814	tandem mass spectrometry of immunoaffinity-enriched plasma samples	791:856	To this end, we used tandem mass spectrometry of immunoaffinity-enriched plasma samples to analyze the individual glycosylation sites in clusterin.
25855029	5	22	theme	individual	873:882	arg1	sites					898:902	the individual glycosylation sites	869:902	the individual glycosylation sites in clusterin	869:915	To this end, we used tandem mass spectrometry of immunoaffinity-enriched plasma samples to analyze the individual glycosylation sites in clusterin.
25855029	6	23	theme	disialylated	1025:1036	arg1	glycan					1047:1052	a biantennary digalactosylated disialylated (A2G2S2) glycan	994:1052	a biantennary digalactosylated disialylated (A2G2S2) glycan	994:1052	We determined the levels of targeted clusterin glycoforms containing either a biantennary digalactosylated disialylated (A2G2S2) glycan or a core fucosylated biantennary digalactosylated disialylated (FA2G2S2) glycan at N-glycosite N374.
25855029	6	23	theme	disialylated	1025:1036	arg1	A2G2S2					1039:1044	A2G2S2	1039:1044	A2G2S2	1039:1044	We determined the levels of targeted clusterin glycoforms containing either a biantennary digalactosylated disialylated (A2G2S2) glycan or a core fucosylated biantennary digalactosylated disialylated (FA2G2S2) glycan at N-glycosite N374.
25855029	4	24	theme	localized	705:713	arg1	ccRCC					715:719	localized ccRCC	705:719	localized ccRCC	705:719	Here, we characterized the occupancy and the degree of heterogeneity of individual N-glycosylation sites of clusterin in the plasma of patients diagnosed with localized ccRCC, before and after curative nephrectomy (n = 40).
25855029	6	25	theme	biantennary	996:1006	arg1	glycan					1047:1052	a biantennary digalactosylated disialylated (A2G2S2) glycan	994:1052	a biantennary digalactosylated disialylated (A2G2S2) glycan	994:1052	We determined the levels of targeted clusterin glycoforms containing either a biantennary digalactosylated disialylated (A2G2S2) glycan or a core fucosylated biantennary digalactosylated disialylated (FA2G2S2) glycan at N-glycosite N374.
25855029	6	25	theme	biantennary	996:1006	arg1	A2G2S2					1039:1044	A2G2S2	1039:1044	A2G2S2	1039:1044	We determined the levels of targeted clusterin glycoforms containing either a biantennary digalactosylated disialylated (A2G2S2) glycan or a core fucosylated biantennary digalactosylated disialylated (FA2G2S2) glycan at N-glycosite N374.
25855029	8	26	theme	significant	1354:1364	arg1	increase					1366:1373	a significant increase	1352:1373	a significant increase in the levels of both FA2G2S2 and A2G2S2 glycans in plasma clusterin	1352:1442	Removal of ccRCC led to a significant increase in the levels of both FA2G2S2 and A2G2S2 glycans in plasma clusterin.
25855029	1	27	from	alterations	162:172	arg1	glycosylation					185:197	protein glycosylation	177:197	protein glycosylation	177:197	Cancer-related alterations in protein glycosylation may serve as diagnostic or prognostic biomarkers or may be used for monitoring disease progression.
25855029	2	28	theme	carcinoma	416:424	arg1	tumors					434:439	clear cell renal cell carcinoma (ccRCC) tumors	394:439	clear cell renal cell carcinoma (ccRCC) tumors	394:439	Clusterin is a medium abundance, yet heavily glycosylated, glycoprotein that is upregulated in clear cell renal cell carcinoma (ccRCC) tumors.
25855029	7	29	theme	glycoforms	1207:1216	arg1	presence					1175:1182	the presence	1171:1182	the presence of these two clusterin glycoforms	1171:1216	We showed that the presence of these two clusterin glycoforms differed significantly in the plasma of patients prior to and after curative nephrectomy for localized ccRCC.
25855029	4	30	gly	occupancy	573:581	arg2	heterogeneity					601:613	heterogeneity	601:613	heterogeneity of individual N-glycosylation sites of clusterin	601:662	Here, we characterized the occupancy and the degree of heterogeneity of individual N-glycosylation sites of clusterin in the plasma of patients diagnosed with localized ccRCC, before and after curative nephrectomy (n = 40).
25855029	4	31	dep	patients	681:688	arg1	the					667:669	the	667:669	the	667:669	Here, we characterized the occupancy and the degree of heterogeneity of individual N-glycosylation sites of clusterin in the plasma of patients diagnosed with localized ccRCC, before and after curative nephrectomy (n = 40).
25855029	4	31	dep	patients	681:688	arg1	plasma					671:676	plasma	671:676	plasma	671:676	Here, we characterized the occupancy and the degree of heterogeneity of individual N-glycosylation sites of clusterin in the plasma of patients diagnosed with localized ccRCC, before and after curative nephrectomy (n = 40).
25855029	6	32	theme	digalactosylated	1088:1103	arg1	glycan					1128:1133	a core fucosylated biantennary digalactosylated disialylated (FA2G2S2) glycan	1057:1133	a core fucosylated biantennary digalactosylated disialylated (FA2G2S2) glycan	1057:1133	We determined the levels of targeted clusterin glycoforms containing either a biantennary digalactosylated disialylated (A2G2S2) glycan or a core fucosylated biantennary digalactosylated disialylated (FA2G2S2) glycan at N-glycosite N374.
25855029	4	33	theme	curative	739:746	arg1	nephrectomy					748:758	curative nephrectomy	739:758	curative nephrectomy (n = 40)	739:767	Here, we characterized the occupancy and the degree of heterogeneity of individual N-glycosylation sites of clusterin in the plasma of patients diagnosed with localized ccRCC, before and after curative nephrectomy (n = 40).
25855029	4	33	theme	curative	739:746	arg1	n					761:761	n = 40	761:766	n = 40	761:766	Here, we characterized the occupancy and the degree of heterogeneity of individual N-glycosylation sites of clusterin in the plasma of patients diagnosed with localized ccRCC, before and after curative nephrectomy (n = 40).
25855029	2	34	theme	renal	405:409	arg1	ccRCC					427:431	ccRCC	427:431	ccRCC	427:431	Clusterin is a medium abundance, yet heavily glycosylated, glycoprotein that is upregulated in clear cell renal cell carcinoma (ccRCC) tumors.
25855029	2	34	theme	renal	405:409	arg1	carcinoma					416:424	clear cell renal cell carcinoma	394:424	clear cell renal cell carcinoma (ccRCC) tumors	394:439	Clusterin is a medium abundance, yet heavily glycosylated, glycoprotein that is upregulated in clear cell renal cell carcinoma (ccRCC) tumors.
25855029	0	35	theme	Clusterin	0:8	arg1	characterization					31:46	Clusterin glycopeptide variant characterization	0:46	Clusterin glycopeptide variant characterization	0:46	Clusterin glycopeptide variant characterization reveals significant site-specific glycan changes in the plasma of clear cell renal cell carcinoma.
25855029	7	36	dep	prior	1267:1271	arg1	to					1273:1274	to	1273:1274	to	1273:1274	We showed that the presence of these two clusterin glycoforms differed significantly in the plasma of patients prior to and after curative nephrectomy for localized ccRCC.
25855029	6	37	theme	fucosylated	1064:1074	arg1	glycan					1128:1133	a core fucosylated biantennary digalactosylated disialylated (FA2G2S2) glycan	1057:1133	a core fucosylated biantennary digalactosylated disialylated (FA2G2S2) glycan	1057:1133	We determined the levels of targeted clusterin glycoforms containing either a biantennary digalactosylated disialylated (A2G2S2) glycan or a core fucosylated biantennary digalactosylated disialylated (FA2G2S2) glycan at N-glycosite N374.
25855029	3	38	theme	N-glycan	472:479	arg1	profile					481:487	the N-glycan profile	468:487	the N-glycan profile of clusterin	468:500	We recently reported that the N-glycan profile of clusterin is altered in the plasma of ccRCC patients.
25855029	0	39	theme	variant	23:29	arg1	characterization					31:46	Clusterin glycopeptide variant characterization	0:46	Clusterin glycopeptide variant characterization	0:46	Clusterin glycopeptide variant characterization reveals significant site-specific glycan changes in the plasma of clear cell renal cell carcinoma.
25855029	0	40	gly	glycopeptide	10:21	arg2	glycopeptide					10:21	Clusterin glycopeptide variant characterization	0:46	Clusterin glycopeptide variant characterization	0:46	Clusterin glycopeptide variant characterization reveals significant site-specific glycan changes in the plasma of clear cell renal cell carcinoma.
25855029	2	41	gly	glycoprotein	358:369	arg1	glycoprotein					358:369	yet heavily glycosylated, glycoprotein	332:369	yet heavily glycosylated, glycoprotein that is upregulated in clear cell renal cell carcinoma (ccRCC) tumors	332:439	Clusterin is a medium abundance, yet heavily glycosylated, glycoprotein that is upregulated in clear cell renal cell carcinoma (ccRCC) tumors.
25855029	2	41	gly	glycoprotein	358:369	arg1	abundance					321:329	a medium abundance	312:329	a medium abundance	312:329	Clusterin is a medium abundance, yet heavily glycosylated, glycoprotein that is upregulated in clear cell renal cell carcinoma (ccRCC) tumors.
25855029	8	42	theme	glycans	1416:1422	arg1	levels					1382:1387	the levels	1378:1387	the levels of both FA2G2S2 and A2G2S2 glycans in plasma clusterin	1378:1442	Removal of ccRCC led to a significant increase in the levels of both FA2G2S2 and A2G2S2 glycans in plasma clusterin.
25855029	0	43	theme	site-specific	68:80	arg1	changes					89:95	significant site-specific glycan changes	56:95	significant site-specific glycan changes in the plasma of clear cell renal cell carcinoma	56:144	Clusterin glycopeptide variant characterization reveals significant site-specific glycan changes in the plasma of clear cell renal cell carcinoma.
25855029	5	44	used	used	786:789	arg2	we					783:784	we	783:784	we	783:784	To this end, we used tandem mass spectrometry of immunoaffinity-enriched plasma samples to analyze the individual glycosylation sites in clusterin.
25855029	6	45	gly	fucosylated	1064:1074	arg1	glycan					1128:1133	a core fucosylated biantennary digalactosylated disialylated (FA2G2S2) glycan	1057:1133	a core fucosylated biantennary digalactosylated disialylated (FA2G2S2) glycan	1057:1133	We determined the levels of targeted clusterin glycoforms containing either a biantennary digalactosylated disialylated (A2G2S2) glycan or a core fucosylated biantennary digalactosylated disialylated (FA2G2S2) glycan at N-glycosite N374.
25855029	8	46	theme	plasma	1427:1432	arg1	clusterin					1434:1442	plasma clusterin	1427:1442	plasma clusterin	1427:1442	Removal of ccRCC led to a significant increase in the levels of both FA2G2S2 and A2G2S2 glycans in plasma clusterin.
25855029	8	47	from	increase	1366:1373	arg1	levels					1382:1387	the levels	1378:1387	the levels of both FA2G2S2 and A2G2S2 glycans in plasma clusterin	1378:1442	Removal of ccRCC led to a significant increase in the levels of both FA2G2S2 and A2G2S2 glycans in plasma clusterin.
25855029	7	48	theme	curative	1286:1293	arg1	nephrectomy					1295:1305	curative nephrectomy	1286:1305	curative nephrectomy for localized ccRCC	1286:1325	We showed that the presence of these two clusterin glycoforms differed significantly in the plasma of patients prior to and after curative nephrectomy for localized ccRCC.
25855029	10	49	theme	expression	1699:1708	arg1	differences					1710:1720	expression differences	1699:1720	expression differences alone	1699:1726	It is envisioned that these identified glycan alterations may provide an additional level of therapeutic or biomarker sensitivity than levels currently achievable by monitoring expression differences alone.
25855029	2	50	theme	clear	394:398	arg1	ccRCC					427:431	ccRCC	427:431	ccRCC	427:431	Clusterin is a medium abundance, yet heavily glycosylated, glycoprotein that is upregulated in clear cell renal cell carcinoma (ccRCC) tumors.
25855029	2	50	theme	clear	394:398	arg1	carcinoma					416:424	clear cell renal cell carcinoma	394:424	clear cell renal cell carcinoma (ccRCC) tumors	394:439	Clusterin is a medium abundance, yet heavily glycosylated, glycoprotein that is upregulated in clear cell renal cell carcinoma (ccRCC) tumors.
25855029	7	51	theme	clusterin	1197:1205	arg1	glycoforms					1207:1216	these two clusterin glycoforms	1187:1216	these two clusterin glycoforms	1187:1216	We showed that the presence of these two clusterin glycoforms differed significantly in the plasma of patients prior to and after curative nephrectomy for localized ccRCC.
25855029	10	52	theme	identified	1550:1559	arg1	alterations					1568:1578	these identified glycan alterations	1544:1578	these identified glycan alterations	1544:1578	It is envisioned that these identified glycan alterations may provide an additional level of therapeutic or biomarker sensitivity than levels currently achievable by monitoring expression differences alone.
25855029	10	53	theme	additional	1595:1604	arg1	level					1606:1610	an additional level	1592:1610	an additional level of therapeutic or biomarker sensitivity than levels currently achievable	1592:1683	It is envisioned that these identified glycan alterations may provide an additional level of therapeutic or biomarker sensitivity than levels currently achievable by monitoring expression differences alone.
25855029	2	54	theme	medium	314:319	arg1	glycoprotein					358:369	yet heavily glycosylated, glycoprotein	332:369	yet heavily glycosylated, glycoprotein that is upregulated in clear cell renal cell carcinoma (ccRCC) tumors	332:439	Clusterin is a medium abundance, yet heavily glycosylated, glycoprotein that is upregulated in clear cell renal cell carcinoma (ccRCC) tumors.
25855029	2	54	theme	medium	314:319	arg1	Clusterin					299:307	Clusterin	299:307	Clusterin	299:307	Clusterin is a medium abundance, yet heavily glycosylated, glycoprotein that is upregulated in clear cell renal cell carcinoma (ccRCC) tumors.
25855029	2	54	theme	medium	314:319	arg1	abundance					321:329	a medium abundance	312:329	a medium abundance	312:329	Clusterin is a medium abundance, yet heavily glycosylated, glycoprotein that is upregulated in clear cell renal cell carcinoma (ccRCC) tumors.
25855029	5	55	theme	glycosylation	884:896	arg1	sites					898:902	the individual glycosylation sites	869:902	the individual glycosylation sites in clusterin	869:915	To this end, we used tandem mass spectrometry of immunoaffinity-enriched plasma samples to analyze the individual glycosylation sites in clusterin.
25855029	4	56	gly	N-glycosylation	629:643	arg1	clusterin					654:662	clusterin	654:662	clusterin	654:662	Here, we characterized the occupancy and the degree of heterogeneity of individual N-glycosylation sites of clusterin in the plasma of patients diagnosed with localized ccRCC, before and after curative nephrectomy (n = 40).
25855029	4	56	gly	N-glycosylation	629:643	arg2	clusterin					654:662	clusterin	654:662	clusterin	654:662	Here, we characterized the occupancy and the degree of heterogeneity of individual N-glycosylation sites of clusterin in the plasma of patients diagnosed with localized ccRCC, before and after curative nephrectomy (n = 40).
25855029	4	56	gly	N-glycosylation	629:643	arg2	sites					645:649	individual N-glycosylation sites	618:649	individual N-glycosylation sites of clusterin	618:662	Here, we characterized the occupancy and the degree of heterogeneity of individual N-glycosylation sites of clusterin in the plasma of patients diagnosed with localized ccRCC, before and after curative nephrectomy (n = 40).
25855029	3	57	theme	ccRCC	530:534	arg1	patients					536:543	ccRCC patients	530:543	ccRCC patients	530:543	We recently reported that the N-glycan profile of clusterin is altered in the plasma of ccRCC patients.
25855029	5	58	theme	plasma	843:848	arg1	samples					850:856	immunoaffinity-enriched plasma samples	819:856	immunoaffinity-enriched plasma samples	819:856	To this end, we used tandem mass spectrometry of immunoaffinity-enriched plasma samples to analyze the individual glycosylation sites in clusterin.
25855029	0	59	theme	carcinoma	136:144	arg1	plasma					104:109	the plasma	100:109	the plasma of clear cell renal cell carcinoma	100:144	Clusterin glycopeptide variant characterization reveals significant site-specific glycan changes in the plasma of clear cell renal cell carcinoma.
25855029	6	60	contain	containing	976:985	arg2	glycan					1047:1052	a biantennary digalactosylated disialylated (A2G2S2) glycan	994:1052	a biantennary digalactosylated disialylated (A2G2S2) glycan	994:1052	We determined the levels of targeted clusterin glycoforms containing either a biantennary digalactosylated disialylated (A2G2S2) glycan or a core fucosylated biantennary digalactosylated disialylated (FA2G2S2) glycan at N-glycosite N374.
25855029	6	60	contain	containing	976:985	arg2	A2G2S2					1039:1044	A2G2S2	1039:1044	A2G2S2	1039:1044	We determined the levels of targeted clusterin glycoforms containing either a biantennary digalactosylated disialylated (A2G2S2) glycan or a core fucosylated biantennary digalactosylated disialylated (FA2G2S2) glycan at N-glycosite N374.
25855029	6	60	contain	containing	976:985	arg1	glycoforms					965:974	targeted clusterin glycoforms	946:974	targeted clusterin glycoforms containing either a biantennary digalactosylated disialylated (A2G2S2) glycan or a core fucosylated biantennary digalactosylated disialylated (FA2G2S2) glycan at N-glycosite N374	946:1153	We determined the levels of targeted clusterin glycoforms containing either a biantennary digalactosylated disialylated (A2G2S2) glycan or a core fucosylated biantennary digalactosylated disialylated (FA2G2S2) glycan at N-glycosite N374.
25855029	6	60	contain	containing	976:985	arg2	glycan					1128:1133	a core fucosylated biantennary digalactosylated disialylated (FA2G2S2) glycan	1057:1133	a core fucosylated biantennary digalactosylated disialylated (FA2G2S2) glycan	1057:1133	We determined the levels of targeted clusterin glycoforms containing either a biantennary digalactosylated disialylated (A2G2S2) glycan or a core fucosylated biantennary digalactosylated disialylated (FA2G2S2) glycan at N-glycosite N374.
25855029	5	61	theme	mass	798:801	arg1	spectrometry					803:814	tandem mass spectrometry	791:814	tandem mass spectrometry of immunoaffinity-enriched plasma samples	791:856	To this end, we used tandem mass spectrometry of immunoaffinity-enriched plasma samples to analyze the individual glycosylation sites in clusterin.
25855029	6	62	theme	clusterin	955:963	arg1	glycoforms					965:974	targeted clusterin glycoforms	946:974	targeted clusterin glycoforms containing either a biantennary digalactosylated disialylated (A2G2S2) glycan or a core fucosylated biantennary digalactosylated disialylated (FA2G2S2) glycan at N-glycosite N374	946:1153	We determined the levels of targeted clusterin glycoforms containing either a biantennary digalactosylated disialylated (A2G2S2) glycan or a core fucosylated biantennary digalactosylated disialylated (FA2G2S2) glycan at N-glycosite N374.
25855029	4	63	theme	N-glycosylation	629:643	arg1	clusterin					654:662	clusterin	654:662	clusterin	654:662	Here, we characterized the occupancy and the degree of heterogeneity of individual N-glycosylation sites of clusterin in the plasma of patients diagnosed with localized ccRCC, before and after curative nephrectomy (n = 40).
25855029	4	63	theme	N-glycosylation	629:643	arg1	sites					645:649	individual N-glycosylation sites	618:649	individual N-glycosylation sites of clusterin	618:662	Here, we characterized the occupancy and the degree of heterogeneity of individual N-glycosylation sites of clusterin in the plasma of patients diagnosed with localized ccRCC, before and after curative nephrectomy (n = 40).
25855029	9	64	theme	lectin	1485:1490	arg1	blotting					1492:1499	lectin blotting	1485:1499	lectin blotting of plasma clusterin	1485:1519	These changes were further confirmed by lectin blotting of plasma clusterin.
25855029	10	65	theme	sensitivity	1640:1650	arg1	level					1606:1610	an additional level	1592:1610	an additional level of therapeutic or biomarker sensitivity than levels currently achievable	1592:1683	It is envisioned that these identified glycan alterations may provide an additional level of therapeutic or biomarker sensitivity than levels currently achievable by monitoring expression differences alone.
25855029	2	66	gly	glycosylated	344:355	arg1	glycoprotein					358:369	yet heavily glycosylated, glycoprotein	332:369	yet heavily glycosylated, glycoprotein that is upregulated in clear cell renal cell carcinoma (ccRCC) tumors	332:439	Clusterin is a medium abundance, yet heavily glycosylated, glycoprotein that is upregulated in clear cell renal cell carcinoma (ccRCC) tumors.
25855029	2	66	gly	glycosylated	344:355	arg1	abundance					321:329	a medium abundance	312:329	a medium abundance	312:329	Clusterin is a medium abundance, yet heavily glycosylated, glycoprotein that is upregulated in clear cell renal cell carcinoma (ccRCC) tumors.
25855029	5	67	from	sites	898:902	arg1	clusterin					907:915	clusterin	907:915	clusterin	907:915	To this end, we used tandem mass spectrometry of immunoaffinity-enriched plasma samples to analyze the individual glycosylation sites in clusterin.
25855029	9	68	theme	clusterin	1511:1519	arg1	blotting					1492:1499	lectin blotting	1485:1499	lectin blotting of plasma clusterin	1485:1519	These changes were further confirmed by lectin blotting of plasma clusterin.
25855029	5	69	gly	glycosylation	884:896	arg2	sites					898:902	the individual glycosylation sites	869:902	the individual glycosylation sites in clusterin	869:915	To this end, we used tandem mass spectrometry of immunoaffinity-enriched plasma samples to analyze the individual glycosylation sites in clusterin.
25855029	4	70	theme	=	763:763	arg1	nephrectomy					748:758	curative nephrectomy	739:758	curative nephrectomy (n = 40)	739:767	Here, we characterized the occupancy and the degree of heterogeneity of individual N-glycosylation sites of clusterin in the plasma of patients diagnosed with localized ccRCC, before and after curative nephrectomy (n = 40).
25855029	4	70	theme	=	763:763	arg1	n					761:761	n = 40	761:766	n = 40	761:766	Here, we characterized the occupancy and the degree of heterogeneity of individual N-glycosylation sites of clusterin in the plasma of patients diagnosed with localized ccRCC, before and after curative nephrectomy (n = 40).
25855029	1	71	theme	protein	177:183	arg1	glycosylation					185:197	protein glycosylation	177:197	protein glycosylation	177:197	Cancer-related alterations in protein glycosylation may serve as diagnostic or prognostic biomarkers or may be used for monitoring disease progression.
25855029	6	72	theme	digalactosylated	1008:1023	arg1	glycan					1047:1052	a biantennary digalactosylated disialylated (A2G2S2) glycan	994:1052	a biantennary digalactosylated disialylated (A2G2S2) glycan	994:1052	We determined the levels of targeted clusterin glycoforms containing either a biantennary digalactosylated disialylated (A2G2S2) glycan or a core fucosylated biantennary digalactosylated disialylated (FA2G2S2) glycan at N-glycosite N374.
25855029	6	72	theme	digalactosylated	1008:1023	arg1	A2G2S2					1039:1044	A2G2S2	1039:1044	A2G2S2	1039:1044	We determined the levels of targeted clusterin glycoforms containing either a biantennary digalactosylated disialylated (A2G2S2) glycan or a core fucosylated biantennary digalactosylated disialylated (FA2G2S2) glycan at N-glycosite N374.
25855029	0	73	theme	clear	114:118	arg1	carcinoma					136:144	clear cell renal cell carcinoma	114:144	clear cell renal cell carcinoma	114:144	Clusterin glycopeptide variant characterization reveals significant site-specific glycan changes in the plasma of clear cell renal cell carcinoma.
25855029	4	74	gly	heterogeneity	601:613	arg1	clusterin					654:662	clusterin	654:662	clusterin	654:662	Here, we characterized the occupancy and the degree of heterogeneity of individual N-glycosylation sites of clusterin in the plasma of patients diagnosed with localized ccRCC, before and after curative nephrectomy (n = 40).
25855029	4	74	gly	heterogeneity	601:613	arg1	sites					645:649	individual N-glycosylation sites	618:649	individual N-glycosylation sites of clusterin	618:662	Here, we characterized the occupancy and the degree of heterogeneity of individual N-glycosylation sites of clusterin in the plasma of patients diagnosed with localized ccRCC, before and after curative nephrectomy (n = 40).
25855029	3	75	theme	clusterin	492:500	arg1	profile					481:487	the N-glycan profile	468:487	the N-glycan profile of clusterin	468:500	We recently reported that the N-glycan profile of clusterin is altered in the plasma of ccRCC patients.
25855029	0	76	theme	renal	125:129	arg1	carcinoma					136:144	clear cell renal cell carcinoma	114:144	clear cell renal cell carcinoma	114:144	Clusterin glycopeptide variant characterization reveals significant site-specific glycan changes in the plasma of clear cell renal cell carcinoma.
25855029	6	77	theme	disialylated	1105:1116	arg1	glycan					1128:1133	a core fucosylated biantennary digalactosylated disialylated (FA2G2S2) glycan	1057:1133	a core fucosylated biantennary digalactosylated disialylated (FA2G2S2) glycan	1057:1133	We determined the levels of targeted clusterin glycoforms containing either a biantennary digalactosylated disialylated (A2G2S2) glycan or a core fucosylated biantennary digalactosylated disialylated (FA2G2S2) glycan at N-glycosite N374.
25855029	2	78	theme	cell	411:414	arg1	ccRCC					427:431	ccRCC	427:431	ccRCC	427:431	Clusterin is a medium abundance, yet heavily glycosylated, glycoprotein that is upregulated in clear cell renal cell carcinoma (ccRCC) tumors.
25855029	2	78	theme	cell	411:414	arg1	carcinoma					416:424	clear cell renal cell carcinoma	394:424	clear cell renal cell carcinoma (ccRCC) tumors	394:439	Clusterin is a medium abundance, yet heavily glycosylated, glycoprotein that is upregulated in clear cell renal cell carcinoma (ccRCC) tumors.
25855029	0	79	theme	glycopeptide	10:21	arg1	characterization					31:46	Clusterin glycopeptide variant characterization	0:46	Clusterin glycopeptide variant characterization	0:46	Clusterin glycopeptide variant characterization reveals significant site-specific glycan changes in the plasma of clear cell renal cell carcinoma.
25855029	6	80	theme	biantennary	1076:1086	arg1	glycan					1128:1133	a core fucosylated biantennary digalactosylated disialylated (FA2G2S2) glycan	1057:1133	a core fucosylated biantennary digalactosylated disialylated (FA2G2S2) glycan	1057:1133	We determined the levels of targeted clusterin glycoforms containing either a biantennary digalactosylated disialylated (A2G2S2) glycan or a core fucosylated biantennary digalactosylated disialylated (FA2G2S2) glycan at N-glycosite N374.
25855029	6	81	gly	N-glycosite	1138:1148	arg2	N-glycosite					1138:1148	N-glycosite N374	1138:1153	N-glycosite N374	1138:1153	We determined the levels of targeted clusterin glycoforms containing either a biantennary digalactosylated disialylated (A2G2S2) glycan or a core fucosylated biantennary digalactosylated disialylated (FA2G2S2) glycan at N-glycosite N374.
25855029	2	82	theme	cell	400:403	arg1	ccRCC					427:431	ccRCC	427:431	ccRCC	427:431	Clusterin is a medium abundance, yet heavily glycosylated, glycoprotein that is upregulated in clear cell renal cell carcinoma (ccRCC) tumors.
25855029	2	82	theme	cell	400:403	arg1	carcinoma					416:424	clear cell renal cell carcinoma	394:424	clear cell renal cell carcinoma (ccRCC) tumors	394:439	Clusterin is a medium abundance, yet heavily glycosylated, glycoprotein that is upregulated in clear cell renal cell carcinoma (ccRCC) tumors.
25855029	6	83	theme	core	1059:1062	arg1	glycan					1128:1133	a core fucosylated biantennary digalactosylated disialylated (FA2G2S2) glycan	1057:1133	a core fucosylated biantennary digalactosylated disialylated (FA2G2S2) glycan	1057:1133	We determined the levels of targeted clusterin glycoforms containing either a biantennary digalactosylated disialylated (A2G2S2) glycan or a core fucosylated biantennary digalactosylated disialylated (FA2G2S2) glycan at N-glycosite N374.
25855029	0	84	theme	significant	56:66	arg1	changes					89:95	significant site-specific glycan changes	56:95	significant site-specific glycan changes in the plasma of clear cell renal cell carcinoma	56:144	Clusterin glycopeptide variant characterization reveals significant site-specific glycan changes in the plasma of clear cell renal cell carcinoma.
25855029	7	85	theme	localized	1311:1319	arg1	ccRCC					1321:1325	localized ccRCC	1311:1325	localized ccRCC	1311:1325	We showed that the presence of these two clusterin glycoforms differed significantly in the plasma of patients prior to and after curative nephrectomy for localized ccRCC.
25855029	8	86	theme	FA2G2S2	1397:1403	arg1	glycans					1416:1422	both FA2G2S2 and A2G2S2 glycans	1392:1422	both FA2G2S2 and A2G2S2 glycans	1392:1422	Removal of ccRCC led to a significant increase in the levels of both FA2G2S2 and A2G2S2 glycans in plasma clusterin.
25855029	0	87	theme	cell	120:123	arg1	carcinoma					136:144	clear cell renal cell carcinoma	114:144	clear cell renal cell carcinoma	114:144	Clusterin glycopeptide variant characterization reveals significant site-specific glycan changes in the plasma of clear cell renal cell carcinoma.
25855029	0	88	theme	glycan	82:87	arg1	changes					89:95	significant site-specific glycan changes	56:95	significant site-specific glycan changes in the plasma of clear cell renal cell carcinoma	56:144	Clusterin glycopeptide variant characterization reveals significant site-specific glycan changes in the plasma of clear cell renal cell carcinoma.
25855029	6	89	gly	disialylated	1105:1116	arg1	glycan					1128:1133	a core fucosylated biantennary digalactosylated disialylated (FA2G2S2) glycan	1057:1133	a core fucosylated biantennary digalactosylated disialylated (FA2G2S2) glycan	1057:1133	We determined the levels of targeted clusterin glycoforms containing either a biantennary digalactosylated disialylated (A2G2S2) glycan or a core fucosylated biantennary digalactosylated disialylated (FA2G2S2) glycan at N-glycosite N374.
25855029	8	90	theme	A2G2S2	1409:1414	arg1	glycans					1416:1422	both FA2G2S2 and A2G2S2 glycans	1392:1422	both FA2G2S2 and A2G2S2 glycans	1392:1422	Removal of ccRCC led to a significant increase in the levels of both FA2G2S2 and A2G2S2 glycans in plasma clusterin.
25855029	1	91	used	used	258:261	arg2	biomarkers					237:246	diagnostic or prognostic biomarkers	212:246	diagnostic or prognostic biomarkers	212:246	Cancer-related alterations in protein glycosylation may serve as diagnostic or prognostic biomarkers or may be used for monitoring disease progression.
25855029	1	91	used	used	258:261	arg2	alterations					162:172	Cancer-related alterations	147:172	Cancer-related alterations in protein glycosylation	147:197	Cancer-related alterations in protein glycosylation may serve as diagnostic or prognostic biomarkers or may be used for monitoring disease progression.
25855029	6	92	theme	N-glycosite	1138:1148	arg1	N374					1150:1153	N-glycosite N374	1138:1153	N-glycosite N374	1138:1153	We determined the levels of targeted clusterin glycoforms containing either a biantennary digalactosylated disialylated (A2G2S2) glycan or a core fucosylated biantennary digalactosylated disialylated (FA2G2S2) glycan at N-glycosite N374.
25855029	4	93	theme	heterogeneity	601:613	arg1	occupancy					573:581	the occupancy	569:581	the occupancy	569:581	Here, we characterized the occupancy and the degree of heterogeneity of individual N-glycosylation sites of clusterin in the plasma of patients diagnosed with localized ccRCC, before and after curative nephrectomy (n = 40).
25855029	4	93	theme	heterogeneity	601:613	arg1	degree					591:596	the degree	587:596	the degree of heterogeneity of individual N-glycosylation sites of clusterin	587:662	Here, we characterized the occupancy and the degree of heterogeneity of individual N-glycosylation sites of clusterin in the plasma of patients diagnosed with localized ccRCC, before and after curative nephrectomy (n = 40).
25855029	2	94	theme	glycosylated	344:355	arg1	glycoprotein					358:369	yet heavily glycosylated, glycoprotein	332:369	yet heavily glycosylated, glycoprotein that is upregulated in clear cell renal cell carcinoma (ccRCC) tumors	332:439	Clusterin is a medium abundance, yet heavily glycosylated, glycoprotein that is upregulated in clear cell renal cell carcinoma (ccRCC) tumors.
25855029	2	94	theme	glycosylated	344:355	arg1	abundance					321:329	a medium abundance	312:329	a medium abundance	312:329	Clusterin is a medium abundance, yet heavily glycosylated, glycoprotein that is upregulated in clear cell renal cell carcinoma (ccRCC) tumors.
25855029	4	95	theme	individual	618:627	arg1	clusterin					654:662	clusterin	654:662	clusterin	654:662	Here, we characterized the occupancy and the degree of heterogeneity of individual N-glycosylation sites of clusterin in the plasma of patients diagnosed with localized ccRCC, before and after curative nephrectomy (n = 40).
25855029	4	95	theme	individual	618:627	arg1	sites					645:649	individual N-glycosylation sites	618:649	individual N-glycosylation sites of clusterin	618:662	Here, we characterized the occupancy and the degree of heterogeneity of individual N-glycosylation sites of clusterin in the plasma of patients diagnosed with localized ccRCC, before and after curative nephrectomy (n = 40).
25855029	10	96	theme	glycan	1561:1566	arg1	alterations					1568:1578	these identified glycan alterations	1544:1578	these identified glycan alterations	1544:1578	It is envisioned that these identified glycan alterations may provide an additional level of therapeutic or biomarker sensitivity than levels currently achievable by monitoring expression differences alone.
25855029	6	97	gly	disialylated	1025:1036	arg1	glycan					1047:1052	a biantennary digalactosylated disialylated (A2G2S2) glycan	994:1052	a biantennary digalactosylated disialylated (A2G2S2) glycan	994:1052	We determined the levels of targeted clusterin glycoforms containing either a biantennary digalactosylated disialylated (A2G2S2) glycan or a core fucosylated biantennary digalactosylated disialylated (FA2G2S2) glycan at N-glycosite N374.
25855029	6	97	gly	disialylated	1025:1036	arg1	A2G2S2					1039:1044	A2G2S2	1039:1044	A2G2S2	1039:1044	We determined the levels of targeted clusterin glycoforms containing either a biantennary digalactosylated disialylated (A2G2S2) glycan or a core fucosylated biantennary digalactosylated disialylated (FA2G2S2) glycan at N-glycosite N374.
20410138	0	0	theme	ribosomal	84:92	arg1	proteins					94:101	core ribosomal proteins	79:101	core ribosomal proteins	79:101	O-GlcNAc cycling enzymes associate with the translational machinery and modify core ribosomal proteins.
20410138	7	1	theme	target	718:723	arg1	RPS6					683:686	RPS6	683:686	RPS6	683:686	RPS6, a component of the mammalian target of rapamycin (mTOR) signaling pathway, follows different dynamics of O-GlcNAcylation than nutrient-induced phosphorylation.
20410138	7	1	theme	target	718:723	arg1	component					691:699	a component	689:699	a component of the mammalian target of rapamycin (mTOR) signaling pathway	689:761	RPS6, a component of the mammalian target of rapamycin (mTOR) signaling pathway, follows different dynamics of O-GlcNAcylation than nutrient-induced phosphorylation.
20410138	0	2	theme	core	79:82	arg1	proteins					94:101	core ribosomal proteins	79:101	core ribosomal proteins	79:101	O-GlcNAc cycling enzymes associate with the translational machinery and modify core ribosomal proteins.
20410138	9	3	dep	present	1013:1019	arg1	whereas					1055:1061	whereas	1055:1061	whereas	1055:1061	Immunofluorescence experiments demonstrate that OGAse is present uniformly throughout the nucleus, whereas OGT is excluded from the nucleolus.
20410138	1	4	theme	initiation	187:196	arg1	factors					213:219	initiation and elongation factors	187:219	initiation and elongation factors	187:219	Protein synthesis is globally regulated through posttranslational modifications of initiation and elongation factors.
20410138	11	5	theme	adenovirus-mediated	1192:1210	arg1	overexpression					1212:1225	adenovirus-mediated overexpression	1192:1225	adenovirus-mediated overexpression of OGT, but not of OGAse or GFP control,	1192:1266	Lastly, adenovirus-mediated overexpression of OGT, but not of OGAse or GFP control, causes an accumulation of 60S subunits and 80S monosomes.
20410138	9	6	theme	Immunofluorescence	956:973	arg1	experiments					975:985	Immunofluorescence experiments	956:985	Immunofluorescence experiments	956:985	Immunofluorescence experiments demonstrate that OGAse is present uniformly throughout the nucleus, whereas OGT is excluded from the nucleolus.
20410138	10	7	theme	OGAse	1138:1142	arg1	staining					1152:1159	OGAse nuclear staining	1138:1159	OGAse nuclear staining	1138:1159	Moreover, nucleolar stress only alters OGAse nuclear staining, but not OGT staining.
20410138	5	8	theme	O-GlcNAcylated	548:561	arg1	RPs					568:570	twenty O-GlcNAcylated core RPs	541:570	twenty O-GlcNAcylated core RPs	541:570	We identify twenty O-GlcNAcylated core RPs, of which eight are newly reported.
20410138	7	9	theme	mammalian	708:716	arg1	target					718:723	the mammalian target	704:723	the mammalian target of rapamycin (mTOR) signaling pathway	704:761	RPS6, a component of the mammalian target of rapamycin (mTOR) signaling pathway, follows different dynamics of O-GlcNAcylation than nutrient-induced phosphorylation.
20410138	8	10	theme	O-GlcNAc	872:879	arg1	enzymes					889:895	O-GlcNAc cycling enzymes	872:895	both O-GlcNAc cycling enzymes OGT and OGAse	867:909	We also show that both O-GlcNAc cycling enzymes OGT and OGAse strongly associate with cytosolic ribosomes.
20410138	8	10	theme	O-GlcNAc	872:879	arg1	OGAse					905:909	OGAse	905:909	OGAse	905:909	We also show that both O-GlcNAc cycling enzymes OGT and OGAse strongly associate with cytosolic ribosomes.
20410138	8	10	theme	O-GlcNAc	872:879	arg1	OGT					897:899	OGT	897:899	OGT	897:899	We also show that both O-GlcNAc cycling enzymes OGT and OGAse strongly associate with cytosolic ribosomes.
20410138	11	11	theme	80S	1311:1313	arg1	monosomes					1315:1323	80S monosomes	1311:1323	80S monosomes	1311:1323	Lastly, adenovirus-mediated overexpression of OGT, but not of OGAse or GFP control, causes an accumulation of 60S subunits and 80S monosomes.
20410138	5	12	theme	core	563:566	arg1	RPs					568:570	twenty O-GlcNAcylated core RPs	541:570	twenty O-GlcNAcylated core RPs	541:570	We identify twenty O-GlcNAcylated core RPs, of which eight are newly reported.
20410138	11	13	theme	monosomes	1315:1323	arg1	accumulation					1278:1289	an accumulation	1275:1289	an accumulation of 60S subunits and 80S monosomes	1275:1323	Lastly, adenovirus-mediated overexpression of OGT, but not of OGAse or GFP control, causes an accumulation of 60S subunits and 80S monosomes.
20410138	8	14	dep	enzymes	889:895	arg1	enzymes					889:895	O-GlcNAc cycling enzymes	872:895	both O-GlcNAc cycling enzymes OGT and OGAse	867:909	We also show that both O-GlcNAc cycling enzymes OGT and OGAse strongly associate with cytosolic ribosomes.
20410138	8	14	dep	enzymes	889:895	arg1	OGAse					905:909	OGAse	905:909	OGAse	905:909	We also show that both O-GlcNAc cycling enzymes OGT and OGAse strongly associate with cytosolic ribosomes.
20410138	8	14	dep	enzymes	889:895	arg1	OGT					897:899	OGT	897:899	OGT	897:899	We also show that both O-GlcNAc cycling enzymes OGT and OGAse strongly associate with cytosolic ribosomes.
20410138	3	15	theme	translational	436:448	arg1	preparations					450:461	translational preparations	436:461	translational preparations	436:461	Here we determine the extent and abundance of O-GlcNAcylated proteins in translational preparations.
20410138	6	16	theme	modification	633:644	arg1	sites					615:619	sites	615:619	sites of O-GlcNAc modification	615:644	We map sites of O-GlcNAc modification on four RPs (L6, L29, L32, and L36).
20410138	6	16	theme	modification	633:644	arg1	modification					633:644	O-GlcNAc modification	624:644	O-GlcNAc modification	624:644	We map sites of O-GlcNAc modification on four RPs (L6, L29, L32, and L36).
20410138	1	17	theme	elongation	202:211	arg1	factors					213:219	initiation and elongation factors	187:219	initiation and elongation factors	187:219	Protein synthesis is globally regulated through posttranslational modifications of initiation and elongation factors.
20410138	0	18	theme	cycling	9:15	arg1	enzymes					17:23	O-GlcNAc cycling enzymes	0:23	O-GlcNAc cycling enzymes	0:23	O-GlcNAc cycling enzymes associate with the translational machinery and modify core ribosomal proteins.
20410138	12	19	theme	important	1440:1448	arg1	roles					1450:1454	important roles	1440:1454	important roles	1440:1454	Our results not only establish that O-GlcNAcylation extensively modifies RPs, but also suggest that O-GlcNAc play important roles in regulating translation and ribosome biogenesis.
20410138	11	20	theme	subunits	1298:1305	arg1	accumulation					1278:1289	an accumulation	1275:1289	an accumulation of 60S subunits and 80S monosomes	1275:1323	Lastly, adenovirus-mediated overexpression of OGT, but not of OGAse or GFP control, causes an accumulation of 60S subunits and 80S monosomes.
20410138	8	21	theme	cycling	881:887	arg1	enzymes					889:895	O-GlcNAc cycling enzymes	872:895	both O-GlcNAc cycling enzymes OGT and OGAse	867:909	We also show that both O-GlcNAc cycling enzymes OGT and OGAse strongly associate with cytosolic ribosomes.
20410138	8	21	theme	cycling	881:887	arg1	OGAse					905:909	OGAse	905:909	OGAse	905:909	We also show that both O-GlcNAc cycling enzymes OGT and OGAse strongly associate with cytosolic ribosomes.
20410138	8	21	theme	cycling	881:887	arg1	OGT					897:899	OGT	897:899	OGT	897:899	We also show that both O-GlcNAc cycling enzymes OGT and OGAse strongly associate with cytosolic ribosomes.
20410138	1	22	theme	factors	213:219	arg1	modifications					170:182	posttranslational modifications	152:182	posttranslational modifications of initiation and elongation factors	152:219	Protein synthesis is globally regulated through posttranslational modifications of initiation and elongation factors.
20410138	0	23	theme	O-GlcNAc	0:7	arg1	enzymes					17:23	O-GlcNAc cycling enzymes	0:23	O-GlcNAc cycling enzymes	0:23	O-GlcNAc cycling enzymes associate with the translational machinery and modify core ribosomal proteins.
20410138	4	24	theme	many	487:490	arg1	proteins					492:499	many proteins	487:499	many proteins that form active polysomes	487:526	O-GlcNAc is present on many proteins that form active polysomes.
20410138	11	25	theme	60S	1294:1296	arg1	subunits					1298:1305	60S subunits	1294:1305	60S subunits	1294:1305	Lastly, adenovirus-mediated overexpression of OGT, but not of OGAse or GFP control, causes an accumulation of 60S subunits and 80S monosomes.
20410138	3	26	theme	O-GlcNAcylated	409:422	arg1	proteins					424:431	O-GlcNAcylated proteins	409:431	O-GlcNAcylated proteins	409:431	Here we determine the extent and abundance of O-GlcNAcylated proteins in translational preparations.
20410138	7	27	theme	O-GlcNAcylation	794:808	arg1	dynamics					782:789	different dynamics	772:789	different dynamics of O-GlcNAcylation than nutrient-induced phosphorylation	772:846	RPS6, a component of the mammalian target of rapamycin (mTOR) signaling pathway, follows different dynamics of O-GlcNAcylation than nutrient-induced phosphorylation.
20410138	11	28	theme	OGAse	1246:1250	arg1	overexpression					1212:1225	adenovirus-mediated overexpression	1192:1225	adenovirus-mediated overexpression of OGT, but not of OGAse or GFP control,	1192:1266	Lastly, adenovirus-mediated overexpression of OGT, but not of OGAse or GFP control, causes an accumulation of 60S subunits and 80S monosomes.
20410138	2	29	theme	O-GlcNAc	340:347	arg1	modification					349:360	the O-GlcNAc modification	336:360	the O-GlcNAc modification	336:360	Recent high-throughput studies have identified translation factors and ribosomal proteins (RPs) as substrates for the O-GlcNAc modification.
20410138	4	30	attach	present	476:482	arg1	proteins					492:499	many proteins	487:499	many proteins that form active polysomes	487:526	O-GlcNAc is present on many proteins that form active polysomes.
20410138	4	30	attach	present	476:482	arg2	O-GlcNAc					464:471	O-GlcNAc	464:471	O-GlcNAc	464:471	O-GlcNAc is present on many proteins that form active polysomes.
20410138	3	31	theme	proteins	424:431	arg1	abundance					396:404	abundance	396:404	abundance	396:404	Here we determine the extent and abundance of O-GlcNAcylated proteins in translational preparations.
20410138	3	31	theme	proteins	424:431	arg1	extent					385:390	extent	385:390	extent	385:390	Here we determine the extent and abundance of O-GlcNAcylated proteins in translational preparations.
20410138	7	32	theme	different	772:780	arg1	dynamics					782:789	different dynamics	772:789	different dynamics of O-GlcNAcylation than nutrient-induced phosphorylation	772:846	RPS6, a component of the mammalian target of rapamycin (mTOR) signaling pathway, follows different dynamics of O-GlcNAcylation than nutrient-induced phosphorylation.
20410138	3	33	from	extent	385:390	arg1	preparations					450:461	translational preparations	436:461	translational preparations	436:461	Here we determine the extent and abundance of O-GlcNAcylated proteins in translational preparations.
20410138	11	34	theme	OGT	1230:1232	arg1	overexpression					1212:1225	adenovirus-mediated overexpression	1192:1225	adenovirus-mediated overexpression of OGT, but not of OGAse or GFP control,	1192:1266	Lastly, adenovirus-mediated overexpression of OGT, but not of OGAse or GFP control, causes an accumulation of 60S subunits and 80S monosomes.
20410138	6	35	theme	O-GlcNAc	624:631	arg1	modification					633:644	O-GlcNAc modification	624:644	O-GlcNAc modification	624:644	We map sites of O-GlcNAc modification on four RPs (L6, L29, L32, and L36).
20410138	10	36	theme	nuclear	1144:1150	arg1	staining					1152:1159	OGAse nuclear staining	1138:1159	OGAse nuclear staining	1138:1159	Moreover, nucleolar stress only alters OGAse nuclear staining, but not OGT staining.
20410138	7	37	theme	nutrient-induced	815:830	arg1	phosphorylation					832:846	nutrient-induced phosphorylation	815:846	nutrient-induced phosphorylation	815:846	RPS6, a component of the mammalian target of rapamycin (mTOR) signaling pathway, follows different dynamics of O-GlcNAcylation than nutrient-induced phosphorylation.
20410138	3	38	from	abundance	396:404	arg1	preparations					450:461	translational preparations	436:461	translational preparations	436:461	Here we determine the extent and abundance of O-GlcNAcylated proteins in translational preparations.
20410138	10	39	theme	OGT	1170:1172	arg1	staining					1174:1181	OGT staining	1170:1181	OGT staining	1170:1181	Moreover, nucleolar stress only alters OGAse nuclear staining, but not OGT staining.
20410138	3	40	dep	extent	385:390	arg1	the					381:383	the	381:383	the	381:383	Here we determine the extent and abundance of O-GlcNAcylated proteins in translational preparations.
20410138	4	41	theme	active	511:516	arg1	polysomes					518:526	active polysomes	511:526	active polysomes	511:526	O-GlcNAc is present on many proteins that form active polysomes.
20410138	2	42	theme	translation	269:279	arg1	factors					281:287	translation factors	269:287	translation factors	269:287	Recent high-throughput studies have identified translation factors and ribosomal proteins (RPs) as substrates for the O-GlcNAc modification.
20410138	2	42	theme	translation	269:279	arg1	substrates					321:330	substrates	321:330	substrates for the O-GlcNAc modification	321:360	Recent high-throughput studies have identified translation factors and ribosomal proteins (RPs) as substrates for the O-GlcNAc modification.
20410138	2	42	theme	translation	269:279	arg1	proteins					303:310	ribosomal proteins	293:310	ribosomal proteins (RPs)	293:316	Recent high-throughput studies have identified translation factors and ribosomal proteins (RPs) as substrates for the O-GlcNAc modification.
20410138	11	43	theme	GFP	1255:1257	arg1	control					1259:1265	GFP control	1255:1265	GFP control	1255:1265	Lastly, adenovirus-mediated overexpression of OGT, but not of OGAse or GFP control, causes an accumulation of 60S subunits and 80S monosomes.
20410138	0	44	theme	translational	44:56	arg1	machinery					58:66	the translational machinery	40:66	the translational machinery	40:66	O-GlcNAc cycling enzymes associate with the translational machinery and modify core ribosomal proteins.
20410138	7	45	theme	signaling	745:753	arg1	pathway					755:761	rapamycin (mTOR) signaling pathway	728:761	rapamycin (mTOR) signaling pathway	728:761	RPS6, a component of the mammalian target of rapamycin (mTOR) signaling pathway, follows different dynamics of O-GlcNAcylation than nutrient-induced phosphorylation.
20410138	7	46	theme	pathway	755:761	arg1	target					718:723	the mammalian target	704:723	the mammalian target of rapamycin (mTOR) signaling pathway	704:761	RPS6, a component of the mammalian target of rapamycin (mTOR) signaling pathway, follows different dynamics of O-GlcNAcylation than nutrient-induced phosphorylation.
20410138	6	47	dep	RPs	654:656	arg1	L32					668:670	L32	668:670	L32	668:670	We map sites of O-GlcNAc modification on four RPs (L6, L29, L32, and L36).
20410138	6	47	dep	RPs	654:656	arg1	L36					677:679	L36	677:679	L36	677:679	We map sites of O-GlcNAc modification on four RPs (L6, L29, L32, and L36).
20410138	6	47	dep	RPs	654:656	arg1	L29					663:665	L29	663:665	L29	663:665	We map sites of O-GlcNAc modification on four RPs (L6, L29, L32, and L36).
20410138	6	47	dep	RPs	654:656	arg1	L6					659:660	L6	659:660	L6	659:660	We map sites of O-GlcNAc modification on four RPs (L6, L29, L32, and L36).
20410138	6	47	dep	RPs	654:656	arg1	RPs					654:656	four RPs	649:656	four RPs (L6, L29, L32, and L36)	649:680	We map sites of O-GlcNAc modification on four RPs (L6, L29, L32, and L36).
20410138	12	48	theme	ribosome	1486:1493	arg1	biogenesis					1495:1504	ribosome biogenesis	1486:1504	ribosome biogenesis	1486:1504	Our results not only establish that O-GlcNAcylation extensively modifies RPs, but also suggest that O-GlcNAc play important roles in regulating translation and ribosome biogenesis.
20410138	8	49	theme	cytosolic	935:943	arg1	ribosomes					945:953	cytosolic ribosomes	935:953	cytosolic ribosomes	935:953	We also show that both O-GlcNAc cycling enzymes OGT and OGAse strongly associate with cytosolic ribosomes.
20410138	1	50	theme	Protein	104:110	arg1	synthesis					112:120	Protein synthesis	104:120	Protein synthesis	104:120	Protein synthesis is globally regulated through posttranslational modifications of initiation and elongation factors.
20410138	11	51	theme	control	1259:1265	arg1	overexpression					1212:1225	adenovirus-mediated overexpression	1192:1225	adenovirus-mediated overexpression of OGT, but not of OGAse or GFP control,	1192:1266	Lastly, adenovirus-mediated overexpression of OGT, but not of OGAse or GFP control, causes an accumulation of 60S subunits and 80S monosomes.
20410138	2	52	theme	high-throughput	229:243	arg1	studies					245:251	Recent high-throughput studies	222:251	Recent high-throughput studies	222:251	Recent high-throughput studies have identified translation factors and ribosomal proteins (RPs) as substrates for the O-GlcNAc modification.
20410138	2	53	theme	Recent	222:227	arg1	studies					245:251	Recent high-throughput studies	222:251	Recent high-throughput studies	222:251	Recent high-throughput studies have identified translation factors and ribosomal proteins (RPs) as substrates for the O-GlcNAc modification.
20410138	4	54	located	present	476:482	arg1	proteins					492:499	many proteins	487:499	many proteins that form active polysomes	487:526	O-GlcNAc is present on many proteins that form active polysomes.
20410138	4	54	located	present	476:482	arg2	O-GlcNAc					464:471	O-GlcNAc	464:471	O-GlcNAc	464:471	O-GlcNAc is present on many proteins that form active polysomes.
20410138	1	55	theme	posttranslational	152:168	arg1	modifications					170:182	posttranslational modifications	152:182	posttranslational modifications of initiation and elongation factors	152:219	Protein synthesis is globally regulated through posttranslational modifications of initiation and elongation factors.
20410138	7	56	theme	rapamycin	728:736	arg1	pathway					755:761	rapamycin (mTOR) signaling pathway	728:761	rapamycin (mTOR) signaling pathway	728:761	RPS6, a component of the mammalian target of rapamycin (mTOR) signaling pathway, follows different dynamics of O-GlcNAcylation than nutrient-induced phosphorylation.
20410138	10	57	theme	nucleolar	1109:1117	arg1	stress					1119:1124	nucleolar stress	1109:1124	nucleolar stress	1109:1124	Moreover, nucleolar stress only alters OGAse nuclear staining, but not OGT staining.
20410138	2	58	theme	ribosomal	293:301	arg1	substrates					321:330	substrates	321:330	substrates for the O-GlcNAc modification	321:360	Recent high-throughput studies have identified translation factors and ribosomal proteins (RPs) as substrates for the O-GlcNAc modification.
20410138	2	58	theme	ribosomal	293:301	arg1	proteins					303:310	ribosomal proteins	293:310	ribosomal proteins (RPs)	293:316	Recent high-throughput studies have identified translation factors and ribosomal proteins (RPs) as substrates for the O-GlcNAc modification.
20410138	2	58	theme	ribosomal	293:301	arg1	factors					281:287	translation factors	269:287	translation factors	269:287	Recent high-throughput studies have identified translation factors and ribosomal proteins (RPs) as substrates for the O-GlcNAc modification.
20410138	2	58	theme	ribosomal	293:301	arg1	RPs					313:315	RPs	313:315	RPs	313:315	Recent high-throughput studies have identified translation factors and ribosomal proteins (RPs) as substrates for the O-GlcNAc modification.
20863279	5	0	dep	acids	716:720	arg1	lining					722:727	lining	722:727	lining	722:727	Guided by this structure, conserved amino acids lining this groove in human OGA were mutated and the activity on three different substrate proteins [TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)] was tested in an in vitro deglycosylation assay.
20863279	3	1	theme	substrate	515:523	arg1	recognition					525:535	substrate recognition	515:535	substrate recognition by human OGA	515:548	In the present study, we uncovered the first insights into the mechanism of substrate recognition by human OGA.
20863279	4	2	theme	orthologue	590:599	arg1	structure					555:563	The structure	551:563	The structure of a novel bacterial OGA orthologue	551:599	The structure of a novel bacterial OGA orthologue reveals a putative substrate-binding groove, conserved in metazoan OGAs.
20863279	6	3	theme	first	1052:1056	arg1	evidence					1058:1065	the first evidence that human OGA may possess a substrate-recognition mechanism that involves interactions with O-GlcNAcylated proteins beyond the GlcNAc-binding site, with possible implications for differential regulation of cycling of O-GlcNAc on different proteins	1048:1314	the first evidence that human OGA may possess a substrate-recognition mechanism that involves interactions with O-GlcNAcylated proteins beyond the GlcNAc-binding site, with possible implications for differential regulation of cycling of O-GlcNAc on different proteins	1048:1314	The results provide the first evidence that human OGA may possess a substrate-recognition mechanism that involves interactions with O-GlcNAcylated proteins beyond the GlcNAc-binding site, with possible implications for differential regulation of cycling of O-GlcNAc on different proteins.
20863279	6	4	with	interactions	1142:1153	arg1	proteins					1175:1182	O-GlcNAcylated proteins	1160:1182	O-GlcNAcylated proteins beyond the GlcNAc-binding site	1160:1213	The results provide the first evidence that human OGA may possess a substrate-recognition mechanism that involves interactions with O-GlcNAcylated proteins beyond the GlcNAc-binding site, with possible implications for differential regulation of cycling of O-GlcNAc on different proteins.
20863279	3	5	theme	recognition	525:535	arg1	mechanism					502:510	the mechanism	498:510	the mechanism of substrate recognition by human OGA	498:548	In the present study, we uncovered the first insights into the mechanism of substrate recognition by human OGA.
20863279	4	6	theme	OGA	586:588	arg1	orthologue					590:599	a novel bacterial OGA orthologue	568:599	a novel bacterial OGA orthologue	568:599	The structure of a novel bacterial OGA orthologue reveals a putative substrate-binding groove, conserved in metazoan OGAs.
20863279	5	7	dep	proteins	813:820	arg1	O1					925:926	forkhead box O1	912:926	forkhead box O1	912:926	Guided by this structure, conserved amino acids lining this groove in human OGA were mutated and the activity on three different substrate proteins [TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)] was tested in an in vitro deglycosylation assay.
20863279	5	7	dep	proteins	813:820	arg1	FoxO1					905:909	FoxO1	905:909	FoxO1 (forkhead box O1)	905:927	Guided by this structure, conserved amino acids lining this groove in human OGA were mutated and the activity on three different substrate proteins [TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)] was tested in an in vitro deglycosylation assay.
20863279	5	7	dep	proteins	813:820	arg1	proteins					813:820	three different substrate proteins [TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)]	787:977	three different substrate proteins [TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)]	787:977	Guided by this structure, conserved amino acids lining this groove in human OGA were mutated and the activity on three different substrate proteins [TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)] was tested in an in vitro deglycosylation assay.
20863279	5	7	dep	proteins	813:820	arg1	[TAB1					822:826	[TAB1	822:826	[TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1)	822:902	Guided by this structure, conserved amino acids lining this groove in human OGA were mutated and the activity on three different substrate proteins [TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)] was tested in an in vitro deglycosylation assay.
20863279	5	7	dep	proteins	813:820	arg1	CREB					933:936	CREB	933:936	CREB (cAMP-response-element-binding protein)	933:976	Guided by this structure, conserved amino acids lining this groove in human OGA were mutated and the activity on three different substrate proteins [TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)] was tested in an in vitro deglycosylation assay.
20863279	5	7	dep	proteins	813:820	arg1	protein					893:899	transforming growth factor-β-activated protein kinase 1-binding protein 1	829:901	transforming growth factor-β-activated protein kinase 1-binding protein 1	829:901	Guided by this structure, conserved amino acids lining this groove in human OGA were mutated and the activity on three different substrate proteins [TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)] was tested in an in vitro deglycosylation assay.
20863279	5	7	dep	proteins	813:820	arg1	protein					969:975	cAMP-response-element-binding protein	939:975	cAMP-response-element-binding protein	939:975	Guided by this structure, conserved amino acids lining this groove in human OGA were mutated and the activity on three different substrate proteins [TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)] was tested in an in vitro deglycosylation assay.
20863279	5	8	theme	different	793:801	arg1	[TAB1					822:826	[TAB1	822:826	[TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1)	822:902	Guided by this structure, conserved amino acids lining this groove in human OGA were mutated and the activity on three different substrate proteins [TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)] was tested in an in vitro deglycosylation assay.
20863279	5	8	theme	different	793:801	arg1	CREB					933:936	CREB	933:936	CREB (cAMP-response-element-binding protein)	933:976	Guided by this structure, conserved amino acids lining this groove in human OGA were mutated and the activity on three different substrate proteins [TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)] was tested in an in vitro deglycosylation assay.
20863279	5	8	theme	different	793:801	arg1	FoxO1					905:909	FoxO1	905:909	FoxO1 (forkhead box O1)	905:927	Guided by this structure, conserved amino acids lining this groove in human OGA were mutated and the activity on three different substrate proteins [TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)] was tested in an in vitro deglycosylation assay.
20863279	5	8	theme	different	793:801	arg1	proteins					813:820	three different substrate proteins [TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)]	787:977	three different substrate proteins [TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)]	787:977	Guided by this structure, conserved amino acids lining this groove in human OGA were mutated and the activity on three different substrate proteins [TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)] was tested in an in vitro deglycosylation assay.
20863279	5	9	theme	human	744:748	arg1	OGA					750:752	human OGA	744:752	human OGA	744:752	Guided by this structure, conserved amino acids lining this groove in human OGA were mutated and the activity on three different substrate proteins [TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)] was tested in an in vitro deglycosylation assay.
20863279	5	10	dep	in	996:997	arg1	vitro					999:1003	vitro	999:1003	vitro	999:1003	Guided by this structure, conserved amino acids lining this groove in human OGA were mutated and the activity on three different substrate proteins [TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)] was tested in an in vitro deglycosylation assay.
20863279	5	11	theme	1-binding	883:891	arg1	protein					893:899	transforming growth factor-β-activated protein kinase 1-binding protein 1	829:901	transforming growth factor-β-activated protein kinase 1-binding protein 1	829:901	Guided by this structure, conserved amino acids lining this groove in human OGA were mutated and the activity on three different substrate proteins [TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)] was tested in an in vitro deglycosylation assay.
20863279	5	11	theme	1-binding	883:891	arg1	[TAB1					822:826	[TAB1	822:826	[TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1)	822:902	Guided by this structure, conserved amino acids lining this groove in human OGA were mutated and the activity on three different substrate proteins [TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)] was tested in an in vitro deglycosylation assay.
20863279	6	12	theme	different	1297:1305	arg1	proteins					1307:1314	different proteins	1297:1314	different proteins	1297:1314	The results provide the first evidence that human OGA may possess a substrate-recognition mechanism that involves interactions with O-GlcNAcylated proteins beyond the GlcNAc-binding site, with possible implications for differential regulation of cycling of O-GlcNAc on different proteins.
20863279	2	13	theme	O-GlcNAc	292:299	arg1	transferase					301:311	O-GlcNAc transferase	292:311	O-GlcNAc transferase	292:311	O-GlcNAcylation is orchestrated by two opposing enzymes, O-GlcNAc transferase and OGA (O-GlcNAcase or β-N-acetylglucosaminidase), which recognize their target proteins via as yet unidentified mechanisms.
20863279	2	13	theme	O-GlcNAc	292:299	arg1	enzymes					283:289	two opposing enzymes	270:289	two opposing enzymes	270:289	O-GlcNAcylation is orchestrated by two opposing enzymes, O-GlcNAc transferase and OGA (O-GlcNAcase or β-N-acetylglucosaminidase), which recognize their target proteins via as yet unidentified mechanisms.
20863279	2	14	theme	unidentified	414:425	arg1	mechanisms					427:436	as yet unidentified mechanisms	407:436	as yet unidentified mechanisms	407:436	O-GlcNAcylation is orchestrated by two opposing enzymes, O-GlcNAc transferase and OGA (O-GlcNAcase or β-N-acetylglucosaminidase), which recognize their target proteins via as yet unidentified mechanisms.
20863279	5	15	theme	substrate	803:811	arg1	[TAB1					822:826	[TAB1	822:826	[TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1)	822:902	Guided by this structure, conserved amino acids lining this groove in human OGA were mutated and the activity on three different substrate proteins [TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)] was tested in an in vitro deglycosylation assay.
20863279	5	15	theme	substrate	803:811	arg1	CREB					933:936	CREB	933:936	CREB (cAMP-response-element-binding protein)	933:976	Guided by this structure, conserved amino acids lining this groove in human OGA were mutated and the activity on three different substrate proteins [TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)] was tested in an in vitro deglycosylation assay.
20863279	5	15	theme	substrate	803:811	arg1	FoxO1					905:909	FoxO1	905:909	FoxO1 (forkhead box O1)	905:927	Guided by this structure, conserved amino acids lining this groove in human OGA were mutated and the activity on three different substrate proteins [TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)] was tested in an in vitro deglycosylation assay.
20863279	5	15	theme	substrate	803:811	arg1	proteins					813:820	three different substrate proteins [TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)]	787:977	three different substrate proteins [TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)]	787:977	Guided by this structure, conserved amino acids lining this groove in human OGA were mutated and the activity on three different substrate proteins [TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)] was tested in an in vitro deglycosylation assay.
20863279	5	16	theme	forkhead	912:919	arg1	O1					925:926	forkhead box O1	912:926	forkhead box O1	912:926	Guided by this structure, conserved amino acids lining this groove in human OGA were mutated and the activity on three different substrate proteins [TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)] was tested in an in vitro deglycosylation assay.
20863279	5	16	theme	forkhead	912:919	arg1	FoxO1					905:909	FoxO1	905:909	FoxO1 (forkhead box O1)	905:927	Guided by this structure, conserved amino acids lining this groove in human OGA were mutated and the activity on three different substrate proteins [TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)] was tested in an in vitro deglycosylation assay.
20863279	6	17	theme	O-GlcNAcylated	1160:1173	arg1	proteins					1175:1182	O-GlcNAcylated proteins	1160:1182	O-GlcNAcylated proteins beyond the GlcNAc-binding site	1160:1213	The results provide the first evidence that human OGA may possess a substrate-recognition mechanism that involves interactions with O-GlcNAcylated proteins beyond the GlcNAc-binding site, with possible implications for differential regulation of cycling of O-GlcNAc on different proteins.
20863279	6	18	from	proteins	1307:1314	arg1	regulation					1260:1269	differential regulation	1247:1269	differential regulation of cycling of O-GlcNAc on different proteins	1247:1314	The results provide the first evidence that human OGA may possess a substrate-recognition mechanism that involves interactions with O-GlcNAcylated proteins beyond the GlcNAc-binding site, with possible implications for differential regulation of cycling of O-GlcNAc on different proteins.
20863279	6	19	theme	human	1072:1076	arg1	OGA					1078:1080	human OGA	1072:1080	human OGA	1072:1080	The results provide the first evidence that human OGA may possess a substrate-recognition mechanism that involves interactions with O-GlcNAcylated proteins beyond the GlcNAc-binding site, with possible implications for differential regulation of cycling of O-GlcNAc on different proteins.
20863279	6	20	theme	O-GlcNAc	1285:1292	arg1	cycling					1274:1280	cycling	1274:1280	cycling of O-GlcNAc on different proteins	1274:1314	The results provide the first evidence that human OGA may possess a substrate-recognition mechanism that involves interactions with O-GlcNAcylated proteins beyond the GlcNAc-binding site, with possible implications for differential regulation of cycling of O-GlcNAc on different proteins.
20863279	3	21	theme	present	446:452	arg1	study					454:458	the present study	442:458	the present study	442:458	In the present study, we uncovered the first insights into the mechanism of substrate recognition by human OGA.
20863279	0	22	theme	Human	0:4	arg1	OGA					6:8	Human OGA	0:8	Human OGA	0:8	Human OGA binds substrates in a conserved peptide recognition groove.
20863279	1	23	theme	cellular	86:93	arg1	proteins					95:102	cellular proteins	86:102	cellular proteins	86:102	Modification of cellular proteins with O-GlcNAc (O-linked N-acetylglucosamine) competes with protein phosphorylation and regulates a plethora of cellular processes.
20863279	6	24	theme	possible	1221:1228	arg1	implications					1230:1241	possible implications	1221:1241	possible implications for differential regulation of cycling of O-GlcNAc on different proteins	1221:1314	The results provide the first evidence that human OGA may possess a substrate-recognition mechanism that involves interactions with O-GlcNAcylated proteins beyond the GlcNAc-binding site, with possible implications for differential regulation of cycling of O-GlcNAc on different proteins.
20863279	6	25	theme	differential	1247:1258	arg1	regulation					1260:1269	differential regulation	1247:1269	differential regulation of cycling of O-GlcNAc on different proteins	1247:1314	The results provide the first evidence that human OGA may possess a substrate-recognition mechanism that involves interactions with O-GlcNAcylated proteins beyond the GlcNAc-binding site, with possible implications for differential regulation of cycling of O-GlcNAc on different proteins.
20863279	1	26	theme	proteins	95:102	arg1	Modification					70:81	Modification	70:81	Modification of cellular proteins with O-GlcNAc (O-linked N-acetylglucosamine)	70:147	Modification of cellular proteins with O-GlcNAc (O-linked N-acetylglucosamine) competes with protein phosphorylation and regulates a plethora of cellular processes.
20863279	6	27	theme	cycling	1274:1280	arg1	regulation					1260:1269	differential regulation	1247:1269	differential regulation of cycling of O-GlcNAc on different proteins	1247:1314	The results provide the first evidence that human OGA may possess a substrate-recognition mechanism that involves interactions with O-GlcNAcylated proteins beyond the GlcNAc-binding site, with possible implications for differential regulation of cycling of O-GlcNAc on different proteins.
20863279	3	28	theme	first	478:482	arg1	insights					484:491	the first insights	474:491	the first insights into the mechanism of substrate recognition by human OGA	474:548	In the present study, we uncovered the first insights into the mechanism of substrate recognition by human OGA.
20863279	5	29	theme	transforming	829:840	arg1	protein					893:899	transforming growth factor-β-activated protein kinase 1-binding protein 1	829:901	transforming growth factor-β-activated protein kinase 1-binding protein 1	829:901	Guided by this structure, conserved amino acids lining this groove in human OGA were mutated and the activity on three different substrate proteins [TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)] was tested in an in vitro deglycosylation assay.
20863279	5	29	theme	transforming	829:840	arg1	[TAB1					822:826	[TAB1	822:826	[TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1)	822:902	Guided by this structure, conserved amino acids lining this groove in human OGA were mutated and the activity on three different substrate proteins [TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)] was tested in an in vitro deglycosylation assay.
20863279	4	30	theme	bacterial	576:584	arg1	orthologue					590:599	a novel bacterial OGA orthologue	568:599	a novel bacterial OGA orthologue	568:599	The structure of a novel bacterial OGA orthologue reveals a putative substrate-binding groove, conserved in metazoan OGAs.
20863279	6	31	theme	GlcNAc-binding	1195:1208	arg1	site					1210:1213	the GlcNAc-binding site	1191:1213	the GlcNAc-binding site	1191:1213	The results provide the first evidence that human OGA may possess a substrate-recognition mechanism that involves interactions with O-GlcNAcylated proteins beyond the GlcNAc-binding site, with possible implications for differential regulation of cycling of O-GlcNAc on different proteins.
20863279	5	32	from	OGA	750:752	arg1	lining					722:727	lining	722:727	lining	722:727	Guided by this structure, conserved amino acids lining this groove in human OGA were mutated and the activity on three different substrate proteins [TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)] was tested in an in vitro deglycosylation assay.
20863279	1	33	theme	protein	163:169	arg1	phosphorylation					171:185	protein phosphorylation	163:185	protein phosphorylation	163:185	Modification of cellular proteins with O-GlcNAc (O-linked N-acetylglucosamine) competes with protein phosphorylation and regulates a plethora of cellular processes.
20863279	5	34	theme	factor-β-activated	849:866	arg1	protein					893:899	transforming growth factor-β-activated protein kinase 1-binding protein 1	829:901	transforming growth factor-β-activated protein kinase 1-binding protein 1	829:901	Guided by this structure, conserved amino acids lining this groove in human OGA were mutated and the activity on three different substrate proteins [TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)] was tested in an in vitro deglycosylation assay.
20863279	5	34	theme	factor-β-activated	849:866	arg1	[TAB1					822:826	[TAB1	822:826	[TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1)	822:902	Guided by this structure, conserved amino acids lining this groove in human OGA were mutated and the activity on three different substrate proteins [TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)] was tested in an in vitro deglycosylation assay.
20863279	4	35	theme	novel	570:574	arg1	orthologue					590:599	a novel bacterial OGA orthologue	568:599	a novel bacterial OGA orthologue	568:599	The structure of a novel bacterial OGA orthologue reveals a putative substrate-binding groove, conserved in metazoan OGAs.
20863279	5	36	theme	protein	868:874	arg1	protein					893:899	transforming growth factor-β-activated protein kinase 1-binding protein 1	829:901	transforming growth factor-β-activated protein kinase 1-binding protein 1	829:901	Guided by this structure, conserved amino acids lining this groove in human OGA were mutated and the activity on three different substrate proteins [TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)] was tested in an in vitro deglycosylation assay.
20863279	5	36	theme	protein	868:874	arg1	[TAB1					822:826	[TAB1	822:826	[TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1)	822:902	Guided by this structure, conserved amino acids lining this groove in human OGA were mutated and the activity on three different substrate proteins [TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)] was tested in an in vitro deglycosylation assay.
20863279	5	37	theme	deglycosylation	1005:1019	arg1	assay					1021:1025	an in vitro deglycosylation assay	993:1025	an in vitro deglycosylation assay	993:1025	Guided by this structure, conserved amino acids lining this groove in human OGA were mutated and the activity on three different substrate proteins [TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)] was tested in an in vitro deglycosylation assay.
20863279	1	38	theme	cellular	215:222	arg1	processes					224:232	cellular processes	215:232	cellular processes	215:232	Modification of cellular proteins with O-GlcNAc (O-linked N-acetylglucosamine) competes with protein phosphorylation and regulates a plethora of cellular processes.
20863279	1	39	with	Modification	70:81	arg1	O-GlcNAc					109:116	O-GlcNAc	109:116	O-GlcNAc (O-linked N-acetylglucosamine)	109:147	Modification of cellular proteins with O-GlcNAc (O-linked N-acetylglucosamine) competes with protein phosphorylation and regulates a plethora of cellular processes.
20863279	1	39	with	Modification	70:81	arg1	N-acetylglucosamine					128:146	O-linked N-acetylglucosamine	119:146	O-linked N-acetylglucosamine	119:146	Modification of cellular proteins with O-GlcNAc (O-linked N-acetylglucosamine) competes with protein phosphorylation and regulates a plethora of cellular processes.
20863279	5	40	theme	kinase	876:881	arg1	protein					893:899	transforming growth factor-β-activated protein kinase 1-binding protein 1	829:901	transforming growth factor-β-activated protein kinase 1-binding protein 1	829:901	Guided by this structure, conserved amino acids lining this groove in human OGA were mutated and the activity on three different substrate proteins [TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)] was tested in an in vitro deglycosylation assay.
20863279	5	40	theme	kinase	876:881	arg1	[TAB1					822:826	[TAB1	822:826	[TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1)	822:902	Guided by this structure, conserved amino acids lining this groove in human OGA were mutated and the activity on three different substrate proteins [TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)] was tested in an in vitro deglycosylation assay.
20863279	1	41	theme	processes	224:232	arg1	plethora					203:210	a plethora	201:210	a plethora of cellular processes	201:232	Modification of cellular proteins with O-GlcNAc (O-linked N-acetylglucosamine) competes with protein phosphorylation and regulates a plethora of cellular processes.
20863279	0	42	theme	peptide	42:48	arg1	groove					62:67	a conserved peptide recognition groove	30:67	a conserved peptide recognition groove	30:67	Human OGA binds substrates in a conserved peptide recognition groove.
20863279	1	43	link	O-linked	119:126	arg1	O-GlcNAc					109:116	O-GlcNAc	109:116	O-GlcNAc (O-linked N-acetylglucosamine)	109:147	Modification of cellular proteins with O-GlcNAc (O-linked N-acetylglucosamine) competes with protein phosphorylation and regulates a plethora of cellular processes.
20863279	1	43	link	O-linked	119:126	arg1	N-acetylglucosamine					128:146	O-linked N-acetylglucosamine	119:146	O-linked N-acetylglucosamine	119:146	Modification of cellular proteins with O-GlcNAc (O-linked N-acetylglucosamine) competes with protein phosphorylation and regulates a plethora of cellular processes.
20863279	5	44	theme	box	921:923	arg1	O1					925:926	forkhead box O1	912:926	forkhead box O1	912:926	Guided by this structure, conserved amino acids lining this groove in human OGA were mutated and the activity on three different substrate proteins [TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)] was tested in an in vitro deglycosylation assay.
20863279	5	44	theme	box	921:923	arg1	FoxO1					905:909	FoxO1	905:909	FoxO1 (forkhead box O1)	905:927	Guided by this structure, conserved amino acids lining this groove in human OGA were mutated and the activity on three different substrate proteins [TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)] was tested in an in vitro deglycosylation assay.
20863279	0	45	theme	conserved	32:40	arg1	groove					62:67	a conserved peptide recognition groove	30:67	a conserved peptide recognition groove	30:67	Human OGA binds substrates in a conserved peptide recognition groove.
20863279	5	46	from	lining	722:727	arg1	OGA					750:752	human OGA	744:752	human OGA	744:752	Guided by this structure, conserved amino acids lining this groove in human OGA were mutated and the activity on three different substrate proteins [TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)] was tested in an in vitro deglycosylation assay.
20863279	6	47	contain	possess	1086:1092	arg2	mechanism					1118:1126	a substrate-recognition mechanism	1094:1126	a substrate-recognition mechanism that involves interactions with O-GlcNAcylated proteins beyond the GlcNAc-binding site, with possible implications for differential regulation of cycling of O-GlcNAc on different proteins	1094:1314	The results provide the first evidence that human OGA may possess a substrate-recognition mechanism that involves interactions with O-GlcNAcylated proteins beyond the GlcNAc-binding site, with possible implications for differential regulation of cycling of O-GlcNAc on different proteins.
20863279	6	47	contain	possess	1086:1092	arg1	OGA					1078:1080	human OGA	1072:1080	human OGA	1072:1080	The results provide the first evidence that human OGA may possess a substrate-recognition mechanism that involves interactions with O-GlcNAcylated proteins beyond the GlcNAc-binding site, with possible implications for differential regulation of cycling of O-GlcNAc on different proteins.
20863279	2	48	dep	OGA	317:319	arg1	β-N-acetylglucosaminidase					337:361	β-N-acetylglucosaminidase	337:361	β-N-acetylglucosaminidase	337:361	O-GlcNAcylation is orchestrated by two opposing enzymes, O-GlcNAc transferase and OGA (O-GlcNAcase or β-N-acetylglucosaminidase), which recognize their target proteins via as yet unidentified mechanisms.
20863279	2	48	dep	OGA	317:319	arg1	O-GlcNAcase					322:332	O-GlcNAcase	322:332	O-GlcNAcase	322:332	O-GlcNAcylation is orchestrated by two opposing enzymes, O-GlcNAc transferase and OGA (O-GlcNAcase or β-N-acetylglucosaminidase), which recognize their target proteins via as yet unidentified mechanisms.
20863279	6	49	from	regulation	1260:1269	arg1	proteins					1307:1314	different proteins	1297:1314	different proteins	1297:1314	The results provide the first evidence that human OGA may possess a substrate-recognition mechanism that involves interactions with O-GlcNAcylated proteins beyond the GlcNAc-binding site, with possible implications for differential regulation of cycling of O-GlcNAc on different proteins.
20863279	5	50	theme	conserved	700:708	arg1	acids					716:720	conserved amino acids	700:720	conserved amino acids lining this groove in human OGA	700:752	Guided by this structure, conserved amino acids lining this groove in human OGA were mutated and the activity on three different substrate proteins [TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)] was tested in an in vitro deglycosylation assay.
20863279	5	51	from	activity	775:782	arg1	[TAB1					822:826	[TAB1	822:826	[TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1)	822:902	Guided by this structure, conserved amino acids lining this groove in human OGA were mutated and the activity on three different substrate proteins [TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)] was tested in an in vitro deglycosylation assay.
20863279	5	51	from	activity	775:782	arg1	CREB					933:936	CREB	933:936	CREB (cAMP-response-element-binding protein)	933:976	Guided by this structure, conserved amino acids lining this groove in human OGA were mutated and the activity on three different substrate proteins [TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)] was tested in an in vitro deglycosylation assay.
20863279	5	51	from	activity	775:782	arg1	FoxO1					905:909	FoxO1	905:909	FoxO1 (forkhead box O1)	905:927	Guided by this structure, conserved amino acids lining this groove in human OGA were mutated and the activity on three different substrate proteins [TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)] was tested in an in vitro deglycosylation assay.
20863279	5	51	from	activity	775:782	arg1	proteins					813:820	three different substrate proteins [TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)]	787:977	three different substrate proteins [TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)]	787:977	Guided by this structure, conserved amino acids lining this groove in human OGA were mutated and the activity on three different substrate proteins [TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)] was tested in an in vitro deglycosylation assay.
20863279	1	52	theme	O-linked	119:126	arg1	O-GlcNAc					109:116	O-GlcNAc	109:116	O-GlcNAc (O-linked N-acetylglucosamine)	109:147	Modification of cellular proteins with O-GlcNAc (O-linked N-acetylglucosamine) competes with protein phosphorylation and regulates a plethora of cellular processes.
20863279	1	52	theme	O-linked	119:126	arg1	N-acetylglucosamine					128:146	O-linked N-acetylglucosamine	119:146	O-linked N-acetylglucosamine	119:146	Modification of cellular proteins with O-GlcNAc (O-linked N-acetylglucosamine) competes with protein phosphorylation and regulates a plethora of cellular processes.
20863279	5	53	theme	cAMP-response-element-binding	939:967	arg1	CREB					933:936	CREB	933:936	CREB (cAMP-response-element-binding protein)	933:976	Guided by this structure, conserved amino acids lining this groove in human OGA were mutated and the activity on three different substrate proteins [TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)] was tested in an in vitro deglycosylation assay.
20863279	5	53	theme	cAMP-response-element-binding	939:967	arg1	protein					969:975	cAMP-response-element-binding protein	939:975	cAMP-response-element-binding protein	939:975	Guided by this structure, conserved amino acids lining this groove in human OGA were mutated and the activity on three different substrate proteins [TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)] was tested in an in vitro deglycosylation assay.
20863279	4	54	theme	substrate-binding	620:636	arg1	groove					638:643	a putative substrate-binding groove	609:643	a putative substrate-binding groove	609:643	The structure of a novel bacterial OGA orthologue reveals a putative substrate-binding groove, conserved in metazoan OGAs.
20863279	5	55	theme	amino	710:714	arg1	acids					716:720	conserved amino acids	700:720	conserved amino acids lining this groove in human OGA	700:752	Guided by this structure, conserved amino acids lining this groove in human OGA were mutated and the activity on three different substrate proteins [TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)] was tested in an in vitro deglycosylation assay.
20863279	2	56	theme	opposing	274:281	arg1	transferase					301:311	O-GlcNAc transferase	292:311	O-GlcNAc transferase	292:311	O-GlcNAcylation is orchestrated by two opposing enzymes, O-GlcNAc transferase and OGA (O-GlcNAcase or β-N-acetylglucosaminidase), which recognize their target proteins via as yet unidentified mechanisms.
20863279	2	56	theme	opposing	274:281	arg1	OGA					317:319	OGA	317:319	OGA (O-GlcNAcase or β-N-acetylglucosaminidase)	317:362	O-GlcNAcylation is orchestrated by two opposing enzymes, O-GlcNAc transferase and OGA (O-GlcNAcase or β-N-acetylglucosaminidase), which recognize their target proteins via as yet unidentified mechanisms.
20863279	2	56	theme	opposing	274:281	arg1	enzymes					283:289	two opposing enzymes	270:289	two opposing enzymes	270:289	O-GlcNAcylation is orchestrated by two opposing enzymes, O-GlcNAc transferase and OGA (O-GlcNAcase or β-N-acetylglucosaminidase), which recognize their target proteins via as yet unidentified mechanisms.
20863279	3	57	theme	human	540:544	arg1	OGA					546:548	human OGA	540:548	human OGA	540:548	In the present study, we uncovered the first insights into the mechanism of substrate recognition by human OGA.
20863279	6	58	from	cycling	1274:1280	arg1	proteins					1307:1314	different proteins	1297:1314	different proteins	1297:1314	The results provide the first evidence that human OGA may possess a substrate-recognition mechanism that involves interactions with O-GlcNAcylated proteins beyond the GlcNAc-binding site, with possible implications for differential regulation of cycling of O-GlcNAc on different proteins.
20863279	4	59	theme	putative	611:618	arg1	groove					638:643	a putative substrate-binding groove	609:643	a putative substrate-binding groove	609:643	The structure of a novel bacterial OGA orthologue reveals a putative substrate-binding groove, conserved in metazoan OGAs.
20863279	4	60	theme	metazoan	659:666	arg1	OGAs					668:671	metazoan OGAs	659:671	metazoan OGAs	659:671	The structure of a novel bacterial OGA orthologue reveals a putative substrate-binding groove, conserved in metazoan OGAs.
20863279	5	61	theme	in	996:997	arg1	assay					1021:1025	an in vitro deglycosylation assay	993:1025	an in vitro deglycosylation assay	993:1025	Guided by this structure, conserved amino acids lining this groove in human OGA were mutated and the activity on three different substrate proteins [TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)] was tested in an in vitro deglycosylation assay.
20863279	5	62	theme	growth	842:847	arg1	protein					893:899	transforming growth factor-β-activated protein kinase 1-binding protein 1	829:901	transforming growth factor-β-activated protein kinase 1-binding protein 1	829:901	Guided by this structure, conserved amino acids lining this groove in human OGA were mutated and the activity on three different substrate proteins [TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)] was tested in an in vitro deglycosylation assay.
20863279	5	62	theme	growth	842:847	arg1	[TAB1					822:826	[TAB1	822:826	[TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1)	822:902	Guided by this structure, conserved amino acids lining this groove in human OGA were mutated and the activity on three different substrate proteins [TAB1 (transforming growth factor-β-activated protein kinase 1-binding protein 1), FoxO1 (forkhead box O1) and CREB (cAMP-response-element-binding protein)] was tested in an in vitro deglycosylation assay.
20863279	6	63	theme	substrate-recognition	1096:1116	arg1	mechanism					1118:1126	a substrate-recognition mechanism	1094:1126	a substrate-recognition mechanism that involves interactions with O-GlcNAcylated proteins beyond the GlcNAc-binding site, with possible implications for differential regulation of cycling of O-GlcNAc on different proteins	1094:1314	The results provide the first evidence that human OGA may possess a substrate-recognition mechanism that involves interactions with O-GlcNAcylated proteins beyond the GlcNAc-binding site, with possible implications for differential regulation of cycling of O-GlcNAc on different proteins.
20863279	0	64	theme	recognition	50:60	arg1	groove					62:67	a conserved peptide recognition groove	30:67	a conserved peptide recognition groove	30:67	Human OGA binds substrates in a conserved peptide recognition groove.
20863279	2	65	theme	target	387:392	arg1	proteins					394:401	their target proteins	381:401	their target proteins	381:401	O-GlcNAcylation is orchestrated by two opposing enzymes, O-GlcNAc transferase and OGA (O-GlcNAcase or β-N-acetylglucosaminidase), which recognize their target proteins via as yet unidentified mechanisms.
22875940	9	0	theme	variable	1694:1701	arg1	role					1703:1706	a variable role	1692:1706	a variable role	1692:1706	The staining pattern of mutant receptors is similar across subgroups of patients, indicating consistent immunogenicity, although we have identified one region that has a variable role in epitope formation.
22875940	10	1	theme	detailed	1763:1770	arg1	comparison					1772:1781	detailed comparison	1763:1781	detailed comparison of antibodies across patients	1763:1811	These findings provide tools for detailed comparison of antibodies across patients and suggest an interaction between antibody binding and channel function.
22875940	4	2	theme	antigenic	805:813	arg1	region					815:820	the antigenic region	801:820	the antigenic region of the NMDAR	801:833	Here, we use human CSF to explore the antigenic region of the NMDAR.
22875940	8	3	theme	acute	1464:1468	arg1	exposure					1479:1486	acute antibody exposure	1464:1486	acute antibody exposure	1464:1486	Mutations of residues N368/G369 change the closed time of the receptor in single channel recordings; more frequent channel openings correlates with the degree of antibody staining, and acute antibody exposure prolongs open time of the receptor.
22875940	1	4	theme	Anti-NMDA	143:151	arg1	NMDAR					163:167	NMDAR	163:167	NMDAR	163:167	Anti-NMDA receptor (NMDAR) encephalitis is a newly identified autoimmune disorder that targets NMDARs, causing severe neurological symptoms including hallucinations, psychosis, and seizures, and may result in death (Dalmau et al., 2008).
22875940	1	4	theme	Anti-NMDA	143:151	arg1	receptor					153:160	Anti-NMDA receptor	143:160	Anti-NMDA receptor (NMDAR) encephalitis	143:181	Anti-NMDA receptor (NMDAR) encephalitis is a newly identified autoimmune disorder that targets NMDARs, causing severe neurological symptoms including hallucinations, psychosis, and seizures, and may result in death (Dalmau et al., 2008).
22875940	8	5	theme	staining	1450:1457	arg1	degree					1431:1436	the degree	1427:1436	the degree of antibody staining	1427:1457	Mutations of residues N368/G369 change the closed time of the receptor in single channel recordings; more frequent channel openings correlates with the degree of antibody staining, and acute antibody exposure prolongs open time of the receptor.
22875940	1	6	theme	receptor	153:160	arg1	encephalitis					170:181	Anti-NMDA receptor (NMDAR) encephalitis	143:181	Anti-NMDA receptor (NMDAR) encephalitis	143:181	Anti-NMDA receptor (NMDAR) encephalitis is a newly identified autoimmune disorder that targets NMDARs, causing severe neurological symptoms including hallucinations, psychosis, and seizures, and may result in death (Dalmau et al., 2008).
22875940	1	6	theme	receptor	153:160	arg1	disorder					216:223	a newly identified autoimmune disorder	186:223	a newly identified autoimmune disorder that targets NMDARs, causing severe neurological symptoms including hallucinations, psychosis, and seizures	186:331	Anti-NMDA receptor (NMDAR) encephalitis is a newly identified autoimmune disorder that targets NMDARs, causing severe neurological symptoms including hallucinations, psychosis, and seizures, and may result in death (Dalmau et al., 2008).
22875940	9	7	theme	epitope	1711:1717	arg1	formation					1719:1727	epitope formation	1711:1727	epitope formation	1711:1727	The staining pattern of mutant receptors is similar across subgroups of patients, indicating consistent immunogenicity, although we have identified one region that has a variable role in epitope formation.
22875940	0	8	theme	small	90:94	arg1	region					96:101	a small region	88:101	a small region within the GluN1 amino terminal domain	88:140	Anti-NMDA receptor encephalitis antibody binding is dependent on amino acid identity of a small region within the GluN1 amino terminal domain.
22875940	8	9	theme	antibody	1441:1448	arg1	staining					1450:1457	antibody staining	1441:1457	antibody staining	1441:1457	Mutations of residues N368/G369 change the closed time of the receptor in single channel recordings; more frequent channel openings correlates with the degree of antibody staining, and acute antibody exposure prolongs open time of the receptor.
22875940	8	10	theme	receptor	1341:1348	arg1	time					1329:1332	the closed time	1318:1332	the closed time of the receptor in single channel recordings	1318:1377	Mutations of residues N368/G369 change the closed time of the receptor in single channel recordings; more frequent channel openings correlates with the degree of antibody staining, and acute antibody exposure prolongs open time of the receptor.
22875940	5	11	theme	terminal	884:891	arg1	domain					893:898	the amino terminal domain	874:898	the amino terminal domain of GluN1 that change patient antibody binding in transfected cells in stereotyped ways	874:985	We created a series of mutants within the amino terminal domain of GluN1 that change patient antibody binding in transfected cells in stereotyped ways.
22875940	5	11	theme	terminal	884:891	arg1	GluN1					903:907	GluN1	903:907	GluN1 that change patient antibody binding in transfected cells in stereotyped ways	903:985	We created a series of mutants within the amino terminal domain of GluN1 that change patient antibody binding in transfected cells in stereotyped ways.
22875940	7	12	gly	glycosylated	1146:1157	arg1	N368					1138:1141	N368	1138:1141	N368	1138:1141	Mass spectrometry experiments show that N368 is glycosylated in transfected cells and rat brain regions; however, this glycosylation is not directly required for epitope formation.
22875940	7	12	gly	glycosylated	1146:1157	arg2	N368					1138:1141	N368	1138:1141	N368	1138:1141	Mass spectrometry experiments show that N368 is glycosylated in transfected cells and rat brain regions; however, this glycosylation is not directly required for epitope formation.
22875940	7	12	gly	glycosylated	1146:1157	arg1	regions					1194:1200	rat brain regions	1184:1200	rat brain regions	1184:1200	Mass spectrometry experiments show that N368 is glycosylated in transfected cells and rat brain regions; however, this glycosylation is not directly required for epitope formation.
22875940	7	12	gly	glycosylated	1146:1157	arg1	cells					1174:1178	transfected cells	1162:1178	transfected cells	1162:1178	Mass spectrometry experiments show that N368 is glycosylated in transfected cells and rat brain regions; however, this glycosylation is not directly required for epitope formation.
22875940	6	13	theme	immunoreactivity	1080:1095	arg1	creation					1068:1075	the creation	1064:1075	the creation of immunoreactivity	1064:1095	These mutants demonstrate that the N368/G369 region of GluN1 is crucial for the creation of immunoreactivity.
22875940	7	14	gly	glycosylation	1217:1229	arg1	epitope					1260:1266	epitope formation	1260:1276	epitope formation	1260:1276	Mass spectrometry experiments show that N368 is glycosylated in transfected cells and rat brain regions; however, this glycosylation is not directly required for epitope formation.
22875940	7	15	theme	rat	1184:1186	arg1	regions					1194:1200	rat brain regions	1184:1200	rat brain regions	1184:1200	Mass spectrometry experiments show that N368 is glycosylated in transfected cells and rat brain regions; however, this glycosylation is not directly required for epitope formation.
22875940	6	16	theme	N368/G369	1023:1031	arg1	region					1033:1038	the N368/G369 region	1019:1038	the N368/G369 region of GluN1	1019:1047	These mutants demonstrate that the N368/G369 region of GluN1 is crucial for the creation of immunoreactivity.
22875940	6	16	theme	N368/G369	1023:1031	arg1	crucial					1052:1058	crucial	1052:1058	crucial	1052:1058	These mutants demonstrate that the N368/G369 region of GluN1 is crucial for the creation of immunoreactivity.
22875940	1	17	theme	severe	254:259	arg1	psychosis					309:317	psychosis	309:317	psychosis	309:317	Anti-NMDA receptor (NMDAR) encephalitis is a newly identified autoimmune disorder that targets NMDARs, causing severe neurological symptoms including hallucinations, psychosis, and seizures, and may result in death (Dalmau et al., 2008).
22875940	1	17	theme	severe	254:259	arg1	seizures					324:331	seizures	324:331	seizures	324:331	Anti-NMDA receptor (NMDAR) encephalitis is a newly identified autoimmune disorder that targets NMDARs, causing severe neurological symptoms including hallucinations, psychosis, and seizures, and may result in death (Dalmau et al., 2008).
22875940	1	17	theme	severe	254:259	arg1	hallucinations					293:306	hallucinations	293:306	hallucinations	293:306	Anti-NMDA receptor (NMDAR) encephalitis is a newly identified autoimmune disorder that targets NMDARs, causing severe neurological symptoms including hallucinations, psychosis, and seizures, and may result in death (Dalmau et al., 2008).
22875940	1	17	theme	severe	254:259	arg1	symptoms					274:281	severe neurological symptoms	254:281	severe neurological symptoms including hallucinations, psychosis, and seizures	254:331	Anti-NMDA receptor (NMDAR) encephalitis is a newly identified autoimmune disorder that targets NMDARs, causing severe neurological symptoms including hallucinations, psychosis, and seizures, and may result in death (Dalmau et al., 2008).
22875940	7	18	theme	Mass	1098:1101	arg1	spectrometry					1103:1114	Mass spectrometry	1098:1114	Mass spectrometry experiments	1098:1126	Mass spectrometry experiments show that N368 is glycosylated in transfected cells and rat brain regions; however, this glycosylation is not directly required for epitope formation.
22875940	8	19	theme	residues	1292:1299	arg1	Mutations					1279:1287	Mutations	1279:1287	Mutations of residues N368/G369	1279:1309	Mutations of residues N368/G369 change the closed time of the receptor in single channel recordings; more frequent channel openings correlates with the degree of antibody staining, and acute antibody exposure prolongs open time of the receptor.
22875940	7	20	theme	epitope	1260:1266	arg1	formation					1268:1276	epitope formation	1260:1276	epitope formation	1260:1276	Mass spectrometry experiments show that N368 is glycosylated in transfected cells and rat brain regions; however, this glycosylation is not directly required for epitope formation.
22875940	0	21	theme	region	96:101	arg1	identity					76:83	amino acid identity	65:83	amino acid identity of a small region within the GluN1 amino terminal domain	65:140	Anti-NMDA receptor encephalitis antibody binding is dependent on amino acid identity of a small region within the GluN1 amino terminal domain.
22875940	8	22	theme	antibody	1470:1477	arg1	exposure					1479:1486	acute antibody exposure	1464:1486	acute antibody exposure	1464:1486	Mutations of residues N368/G369 change the closed time of the receptor in single channel recordings; more frequent channel openings correlates with the degree of antibody staining, and acute antibody exposure prolongs open time of the receptor.
22875940	4	23	theme	human	780:784	arg1	CSF					786:788	human CSF	780:788	human CSF	780:788	Here, we use human CSF to explore the antigenic region of the NMDAR.
22875940	0	24	theme	Anti-NMDA	0:8	arg1	binding					41:47	Anti-NMDA receptor encephalitis antibody binding	0:47	Anti-NMDA receptor encephalitis antibody binding	0:47	Anti-NMDA receptor encephalitis antibody binding is dependent on amino acid identity of a small region within the GluN1 amino terminal domain.
22875940	3	25	dep	patients	688:695	arg1	antibodies					698:707	antibodies	698:707	patients' antibodies	688:707	A clearly defined antigenic region could provide more precise testing, allow for comparison of immunogenicity between patients to explore potential clinically relevant variations, elucidate the functional effects of antibodies, and make patients' antibodies a more effective tool with which to study NMDAR function.
22875940	0	26	theme	receptor	10:17	arg1	binding					41:47	Anti-NMDA receptor encephalitis antibody binding	0:47	Anti-NMDA receptor encephalitis antibody binding	0:47	Anti-NMDA receptor encephalitis antibody binding is dependent on amino acid identity of a small region within the GluN1 amino terminal domain.
22875940	8	27	theme	open	1497:1500	arg1	time					1502:1505	open time	1497:1505	open time of the receptor	1497:1521	Mutations of residues N368/G369 change the closed time of the receptor in single channel recordings; more frequent channel openings correlates with the degree of antibody staining, and acute antibody exposure prolongs open time of the receptor.
22875940	9	28	theme	consistent	1617:1626	arg1	immunogenicity					1628:1641	consistent immunogenicity	1617:1641	consistent immunogenicity	1617:1641	The staining pattern of mutant receptors is similar across subgroups of patients, indicating consistent immunogenicity, although we have identified one region that has a variable role in epitope formation.
22875940	7	29	theme	transfected	1162:1172	arg1	cells					1174:1178	transfected cells	1162:1178	transfected cells	1162:1178	Mass spectrometry experiments show that N368 is glycosylated in transfected cells and rat brain regions; however, this glycosylation is not directly required for epitope formation.
22875940	5	30	theme	mutants	859:865	arg1	series					849:854	a series	847:854	a series of mutants	847:865	We created a series of mutants within the amino terminal domain of GluN1 that change patient antibody binding in transfected cells in stereotyped ways.
22875940	7	31	theme	spectrometry	1103:1114	arg1	experiments					1116:1126	Mass spectrometry experiments	1098:1126	Mass spectrometry experiments	1098:1126	Mass spectrometry experiments show that N368 is glycosylated in transfected cells and rat brain regions; however, this glycosylation is not directly required for epitope formation.
22875940	2	32	theme	exact	394:398	arg1	unknown					442:448	unknown	442:448	unknown	442:448	However, the exact epitope to which these antibodies bind is unknown.
22875940	2	32	theme	exact	394:398	arg1	epitope					400:406	the exact epitope	390:406	the exact epitope to which these antibodies bind	390:437	However, the exact epitope to which these antibodies bind is unknown.
22875940	1	33	theme	neurological	261:272	arg1	psychosis					309:317	psychosis	309:317	psychosis	309:317	Anti-NMDA receptor (NMDAR) encephalitis is a newly identified autoimmune disorder that targets NMDARs, causing severe neurological symptoms including hallucinations, psychosis, and seizures, and may result in death (Dalmau et al., 2008).
22875940	1	33	theme	neurological	261:272	arg1	seizures					324:331	seizures	324:331	seizures	324:331	Anti-NMDA receptor (NMDAR) encephalitis is a newly identified autoimmune disorder that targets NMDARs, causing severe neurological symptoms including hallucinations, psychosis, and seizures, and may result in death (Dalmau et al., 2008).
22875940	1	33	theme	neurological	261:272	arg1	hallucinations					293:306	hallucinations	293:306	hallucinations	293:306	Anti-NMDA receptor (NMDAR) encephalitis is a newly identified autoimmune disorder that targets NMDARs, causing severe neurological symptoms including hallucinations, psychosis, and seizures, and may result in death (Dalmau et al., 2008).
22875940	1	33	theme	neurological	261:272	arg1	symptoms					274:281	severe neurological symptoms	254:281	severe neurological symptoms including hallucinations, psychosis, and seizures	254:331	Anti-NMDA receptor (NMDAR) encephalitis is a newly identified autoimmune disorder that targets NMDARs, causing severe neurological symptoms including hallucinations, psychosis, and seizures, and may result in death (Dalmau et al., 2008).
22875940	10	34	theme	antibodies	1786:1795	arg1	comparison					1772:1781	detailed comparison	1763:1781	detailed comparison of antibodies across patients	1763:1811	These findings provide tools for detailed comparison of antibodies across patients and suggest an interaction between antibody binding and channel function.
22875940	0	35	theme	antibody	32:39	arg1	binding					41:47	Anti-NMDA receptor encephalitis antibody binding	0:47	Anti-NMDA receptor encephalitis antibody binding	0:47	Anti-NMDA receptor encephalitis antibody binding is dependent on amino acid identity of a small region within the GluN1 amino terminal domain.
22875940	3	36	theme	effective	716:724	arg1	tool					726:729	a more effective tool	709:729	a more effective tool with which to study NMDAR function	709:764	A clearly defined antigenic region could provide more precise testing, allow for comparison of immunogenicity between patients to explore potential clinically relevant variations, elucidate the functional effects of antibodies, and make patients' antibodies a more effective tool with which to study NMDAR function.
22875940	0	37	theme	GluN1	114:118	arg1	domain					135:140	the GluN1 amino terminal domain	110:140	the GluN1 amino terminal domain	110:140	Anti-NMDA receptor encephalitis antibody binding is dependent on amino acid identity of a small region within the GluN1 amino terminal domain.
22875940	3	38	theme	precise	505:511	arg1	testing					513:519	more precise testing	500:519	more precise testing	500:519	A clearly defined antigenic region could provide more precise testing, allow for comparison of immunogenicity between patients to explore potential clinically relevant variations, elucidate the functional effects of antibodies, and make patients' antibodies a more effective tool with which to study NMDAR function.
22875940	5	39	from	cells	961:965	arg1	ways					982:985	stereotyped ways	970:985	stereotyped ways	970:985	We created a series of mutants within the amino terminal domain of GluN1 that change patient antibody binding in transfected cells in stereotyped ways.
22875940	9	40	theme	mutant	1548:1553	arg1	receptors					1555:1563	mutant receptors	1548:1563	mutant receptors	1548:1563	The staining pattern of mutant receptors is similar across subgroups of patients, indicating consistent immunogenicity, although we have identified one region that has a variable role in epitope formation.
22875940	0	41	theme	encephalitis	19:30	arg1	binding					41:47	Anti-NMDA receptor encephalitis antibody binding	0:47	Anti-NMDA receptor encephalitis antibody binding	0:47	Anti-NMDA receptor encephalitis antibody binding is dependent on amino acid identity of a small region within the GluN1 amino terminal domain.
22875940	3	42	theme	relevant	610:617	arg1	variations					619:628	potential clinically relevant variations	589:628	potential clinically relevant variations	589:628	A clearly defined antigenic region could provide more precise testing, allow for comparison of immunogenicity between patients to explore potential clinically relevant variations, elucidate the functional effects of antibodies, and make patients' antibodies a more effective tool with which to study NMDAR function.
22875940	5	43	theme	amino	878:882	arg1	domain					893:898	the amino terminal domain	874:898	the amino terminal domain of GluN1 that change patient antibody binding in transfected cells in stereotyped ways	874:985	We created a series of mutants within the amino terminal domain of GluN1 that change patient antibody binding in transfected cells in stereotyped ways.
22875940	5	43	theme	amino	878:882	arg1	GluN1					903:907	GluN1	903:907	GluN1 that change patient antibody binding in transfected cells in stereotyped ways	903:985	We created a series of mutants within the amino terminal domain of GluN1 that change patient antibody binding in transfected cells in stereotyped ways.
22875940	7	44	theme	brain	1188:1192	arg1	regions					1194:1200	rat brain regions	1184:1200	rat brain regions	1184:1200	Mass spectrometry experiments show that N368 is glycosylated in transfected cells and rat brain regions; however, this glycosylation is not directly required for epitope formation.
22875940	8	45	theme	receptor	1514:1521	arg1	time					1502:1505	open time	1497:1505	open time of the receptor	1497:1521	Mutations of residues N368/G369 change the closed time of the receptor in single channel recordings; more frequent channel openings correlates with the degree of antibody staining, and acute antibody exposure prolongs open time of the receptor.
22875940	0	46	theme	terminal	126:133	arg1	domain					135:140	the GluN1 amino terminal domain	110:140	the GluN1 amino terminal domain	110:140	Anti-NMDA receptor encephalitis antibody binding is dependent on amino acid identity of a small region within the GluN1 amino terminal domain.
22875940	9	47	contain	has	1688:1690	arg2	role					1703:1706	a variable role	1692:1706	a variable role	1692:1706	The staining pattern of mutant receptors is similar across subgroups of patients, indicating consistent immunogenicity, although we have identified one region that has a variable role in epitope formation.
22875940	9	47	contain	has	1688:1690	arg1	region					1676:1681	one region	1672:1681	one region that has a variable role in epitope formation	1672:1727	The staining pattern of mutant receptors is similar across subgroups of patients, indicating consistent immunogenicity, although we have identified one region that has a variable role in epitope formation.
22875940	0	48	theme	amino	120:124	arg1	domain					135:140	the GluN1 amino terminal domain	110:140	the GluN1 amino terminal domain	110:140	Anti-NMDA receptor encephalitis antibody binding is dependent on amino acid identity of a small region within the GluN1 amino terminal domain.
22875940	3	49	theme	potential	589:597	arg1	variations					619:628	potential clinically relevant variations	589:628	potential clinically relevant variations	589:628	A clearly defined antigenic region could provide more precise testing, allow for comparison of immunogenicity between patients to explore potential clinically relevant variations, elucidate the functional effects of antibodies, and make patients' antibodies a more effective tool with which to study NMDAR function.
22875940	3	50	theme	immunogenicity	546:559	arg1	comparison					532:541	comparison	532:541	comparison of immunogenicity between patients	532:576	A clearly defined antigenic region could provide more precise testing, allow for comparison of immunogenicity between patients to explore potential clinically relevant variations, elucidate the functional effects of antibodies, and make patients' antibodies a more effective tool with which to study NMDAR function.
22875940	1	51	theme	identified	194:203	arg1	encephalitis					170:181	Anti-NMDA receptor (NMDAR) encephalitis	143:181	Anti-NMDA receptor (NMDAR) encephalitis	143:181	Anti-NMDA receptor (NMDAR) encephalitis is a newly identified autoimmune disorder that targets NMDARs, causing severe neurological symptoms including hallucinations, psychosis, and seizures, and may result in death (Dalmau et al., 2008).
22875940	1	51	theme	identified	194:203	arg1	disorder					216:223	a newly identified autoimmune disorder	186:223	a newly identified autoimmune disorder that targets NMDARs, causing severe neurological symptoms including hallucinations, psychosis, and seizures	186:331	Anti-NMDA receptor (NMDAR) encephalitis is a newly identified autoimmune disorder that targets NMDARs, causing severe neurological symptoms including hallucinations, psychosis, and seizures, and may result in death (Dalmau et al., 2008).
22875940	4	52	theme	NMDAR	829:833	arg1	region					815:820	the antigenic region	801:820	the antigenic region of the NMDAR	801:833	Here, we use human CSF to explore the antigenic region of the NMDAR.
22875940	8	53	theme	frequent	1385:1392	arg1	openings					1402:1409	more frequent channel openings	1380:1409	more frequent channel openings	1380:1409	Mutations of residues N368/G369 change the closed time of the receptor in single channel recordings; more frequent channel openings correlates with the degree of antibody staining, and acute antibody exposure prolongs open time of the receptor.
22875940	5	54	theme	transfected	949:959	arg1	cells					961:965	transfected cells	949:965	transfected cells in stereotyped ways	949:985	We created a series of mutants within the amino terminal domain of GluN1 that change patient antibody binding in transfected cells in stereotyped ways.
22875940	10	55	theme	antibody	1848:1855	arg1	binding					1857:1863	antibody binding	1848:1863	antibody binding	1848:1863	These findings provide tools for detailed comparison of antibodies across patients and suggest an interaction between antibody binding and channel function.
22875940	1	56	dep	result	342:347	arg1	Dalmau					359:364	Dalmau	359:364	Dalmau	359:364	Anti-NMDA receptor (NMDAR) encephalitis is a newly identified autoimmune disorder that targets NMDARs, causing severe neurological symptoms including hallucinations, psychosis, and seizures, and may result in death (Dalmau et al., 2008).
22875940	10	57	theme	channel	1869:1875	arg1	function					1877:1884	channel function	1869:1884	channel function	1869:1884	These findings provide tools for detailed comparison of antibodies across patients and suggest an interaction between antibody binding and channel function.
22875940	5	58	theme	stereotyped	970:980	arg1	ways					982:985	stereotyped ways	970:985	stereotyped ways	970:985	We created a series of mutants within the amino terminal domain of GluN1 that change patient antibody binding in transfected cells in stereotyped ways.
22875940	9	59	theme	patients	1596:1603	arg1	subgroups					1583:1591	subgroups	1583:1591	subgroups of patients	1583:1603	The staining pattern of mutant receptors is similar across subgroups of patients, indicating consistent immunogenicity, although we have identified one region that has a variable role in epitope formation.
22875940	8	60	theme	channel	1394:1400	arg1	openings					1402:1409	more frequent channel openings	1380:1409	more frequent channel openings	1380:1409	Mutations of residues N368/G369 change the closed time of the receptor in single channel recordings; more frequent channel openings correlates with the degree of antibody staining, and acute antibody exposure prolongs open time of the receptor.
22875940	8	61	theme	channel	1360:1366	arg1	recordings					1368:1377	single channel recordings	1353:1377	single channel recordings	1353:1377	Mutations of residues N368/G369 change the closed time of the receptor in single channel recordings; more frequent channel openings correlates with the degree of antibody staining, and acute antibody exposure prolongs open time of the receptor.
22875940	3	62	theme	functional	645:654	arg1	effects					656:662	the functional effects	641:662	the functional effects of antibodies	641:676	A clearly defined antigenic region could provide more precise testing, allow for comparison of immunogenicity between patients to explore potential clinically relevant variations, elucidate the functional effects of antibodies, and make patients' antibodies a more effective tool with which to study NMDAR function.
22875940	8	63	theme	single	1353:1358	arg1	recordings					1368:1377	single channel recordings	1353:1377	single channel recordings	1353:1377	Mutations of residues N368/G369 change the closed time of the receptor in single channel recordings; more frequent channel openings correlates with the degree of antibody staining, and acute antibody exposure prolongs open time of the receptor.
22875940	9	64	theme	staining	1528:1535	arg1	pattern					1537:1543	The staining pattern	1524:1543	The staining pattern of mutant receptors	1524:1563	The staining pattern of mutant receptors is similar across subgroups of patients, indicating consistent immunogenicity, although we have identified one region that has a variable role in epitope formation.
22875940	9	64	theme	staining	1528:1535	arg1	similar					1568:1574	similar	1568:1574	similar	1568:1574	The staining pattern of mutant receptors is similar across subgroups of patients, indicating consistent immunogenicity, although we have identified one region that has a variable role in epitope formation.
22875940	8	65	theme	closed	1322:1327	arg1	time					1329:1332	the closed time	1318:1332	the closed time of the receptor in single channel recordings	1318:1377	Mutations of residues N368/G369 change the closed time of the receptor in single channel recordings; more frequent channel openings correlates with the degree of antibody staining, and acute antibody exposure prolongs open time of the receptor.
22875940	1	66	theme	autoimmune	205:214	arg1	encephalitis					170:181	Anti-NMDA receptor (NMDAR) encephalitis	143:181	Anti-NMDA receptor (NMDAR) encephalitis	143:181	Anti-NMDA receptor (NMDAR) encephalitis is a newly identified autoimmune disorder that targets NMDARs, causing severe neurological symptoms including hallucinations, psychosis, and seizures, and may result in death (Dalmau et al., 2008).
22875940	1	66	theme	autoimmune	205:214	arg1	disorder					216:223	a newly identified autoimmune disorder	186:223	a newly identified autoimmune disorder that targets NMDARs, causing severe neurological symptoms including hallucinations, psychosis, and seizures	186:331	Anti-NMDA receptor (NMDAR) encephalitis is a newly identified autoimmune disorder that targets NMDARs, causing severe neurological symptoms including hallucinations, psychosis, and seizures, and may result in death (Dalmau et al., 2008).
22875940	5	67	theme	GluN1	903:907	arg1	domain					893:898	the amino terminal domain	874:898	the amino terminal domain of GluN1 that change patient antibody binding in transfected cells in stereotyped ways	874:985	We created a series of mutants within the amino terminal domain of GluN1 that change patient antibody binding in transfected cells in stereotyped ways.
22875940	5	67	theme	GluN1	903:907	arg1	GluN1					903:907	GluN1	903:907	GluN1 that change patient antibody binding in transfected cells in stereotyped ways	903:985	We created a series of mutants within the amino terminal domain of GluN1 that change patient antibody binding in transfected cells in stereotyped ways.
22875940	9	68	theme	receptors	1555:1563	arg1	pattern					1537:1543	The staining pattern	1524:1543	The staining pattern of mutant receptors	1524:1563	The staining pattern of mutant receptors is similar across subgroups of patients, indicating consistent immunogenicity, although we have identified one region that has a variable role in epitope formation.
22875940	9	68	theme	receptors	1555:1563	arg1	similar					1568:1574	similar	1568:1574	similar	1568:1574	The staining pattern of mutant receptors is similar across subgroups of patients, indicating consistent immunogenicity, although we have identified one region that has a variable role in epitope formation.
22875940	6	69	theme	GluN1	1043:1047	arg1	region					1033:1038	the N368/G369 region	1019:1038	the N368/G369 region of GluN1	1019:1047	These mutants demonstrate that the N368/G369 region of GluN1 is crucial for the creation of immunoreactivity.
22875940	6	69	theme	GluN1	1043:1047	arg1	crucial					1052:1058	crucial	1052:1058	crucial	1052:1058	These mutants demonstrate that the N368/G369 region of GluN1 is crucial for the creation of immunoreactivity.
22875940	0	70	theme	acid	71:74	arg1	identity					76:83	amino acid identity	65:83	amino acid identity of a small region within the GluN1 amino terminal domain	65:140	Anti-NMDA receptor encephalitis antibody binding is dependent on amino acid identity of a small region within the GluN1 amino terminal domain.
22875940	5	71	theme	patient	921:927	arg1	binding					938:944	patient antibody binding	921:944	patient antibody binding	921:944	We created a series of mutants within the amino terminal domain of GluN1 that change patient antibody binding in transfected cells in stereotyped ways.
22875940	3	72	theme	defined	461:467	arg1	region					479:484	A clearly defined antigenic region	451:484	A clearly defined antigenic region	451:484	A clearly defined antigenic region could provide more precise testing, allow for comparison of immunogenicity between patients to explore potential clinically relevant variations, elucidate the functional effects of antibodies, and make patients' antibodies a more effective tool with which to study NMDAR function.
22875940	8	73	from	time	1329:1332	arg1	recordings					1368:1377	single channel recordings	1353:1377	single channel recordings	1353:1377	Mutations of residues N368/G369 change the closed time of the receptor in single channel recordings; more frequent channel openings correlates with the degree of antibody staining, and acute antibody exposure prolongs open time of the receptor.
22875940	0	74	theme	amino	65:69	arg1	identity					76:83	amino acid identity	65:83	amino acid identity of a small region within the GluN1 amino terminal domain	65:140	Anti-NMDA receptor encephalitis antibody binding is dependent on amino acid identity of a small region within the GluN1 amino terminal domain.
22875940	3	75	theme	antibodies	667:676	arg1	effects					656:662	the functional effects	641:662	the functional effects of antibodies	641:676	A clearly defined antigenic region could provide more precise testing, allow for comparison of immunogenicity between patients to explore potential clinically relevant variations, elucidate the functional effects of antibodies, and make patients' antibodies a more effective tool with which to study NMDAR function.
22875940	5	76	theme	antibody	929:936	arg1	binding					938:944	patient antibody binding	921:944	patient antibody binding	921:944	We created a series of mutants within the amino terminal domain of GluN1 that change patient antibody binding in transfected cells in stereotyped ways.
22875940	3	77	theme	antigenic	469:477	arg1	region					479:484	A clearly defined antigenic region	451:484	A clearly defined antigenic region	451:484	A clearly defined antigenic region could provide more precise testing, allow for comparison of immunogenicity between patients to explore potential clinically relevant variations, elucidate the functional effects of antibodies, and make patients' antibodies a more effective tool with which to study NMDAR function.
22875940	3	78	theme	NMDAR	751:755	arg1	function					757:764	NMDAR function	751:764	NMDAR function	751:764	A clearly defined antigenic region could provide more precise testing, allow for comparison of immunogenicity between patients to explore potential clinically relevant variations, elucidate the functional effects of antibodies, and make patients' antibodies a more effective tool with which to study NMDAR function.
26510530	1	0	theme	abundant	154:161	arg1	glycoproteins					163:175	the top eight abundant glycoproteins	140:175	the top eight abundant glycoproteins in plasma	140:185	A comprehensive glycan map was constructed for the top eight abundant glycoproteins in plasma using both specific and nonspecific enzyme digestions followed by nano liquid chromatography (LC)-chip/quadrupole time-of-flight mass spectrometry (MS) analysis.
26510530	8	1	theme	protein	1219:1225	arg1	quantitation					1227:1238	The absolute protein quantitation	1206:1238	The absolute protein quantitation	1206:1238	The absolute protein quantitation has a wide linear range (3-4 orders of magnitude) and low limit of quantitation (femtomole level).
26510530	1	2	theme	liquid	258:263	arg1	MS					335:336	MS	335:336	MS	335:336	A comprehensive glycan map was constructed for the top eight abundant glycoproteins in plasma using both specific and nonspecific enzyme digestions followed by nano liquid chromatography (LC)-chip/quadrupole time-of-flight mass spectrometry (MS) analysis.
26510530	1	2	theme	liquid	258:263	arg1	spectrometry					321:332	nano liquid chromatography (LC)-chip/quadrupole time-of-flight mass spectrometry	253:332	nano liquid chromatography (LC)-chip/quadrupole time-of-flight mass spectrometry (MS) analysis	253:346	A comprehensive glycan map was constructed for the top eight abundant glycoproteins in plasma using both specific and nonspecific enzyme digestions followed by nano liquid chromatography (LC)-chip/quadrupole time-of-flight mass spectrometry (MS) analysis.
26510530	0	3	theme	Glycoproteins	78:90	arg1	Method					2:7	A Method	0:7	A Method for Comprehensive Glycosite-Mapping	0:43	A Method for Comprehensive Glycosite-Mapping and Direct Quantitation of Serum Glycoproteins.
26510530	0	3	theme	Glycoproteins	78:90	arg1	Quantitation					56:67	Direct Quantitation	49:67	Direct Quantitation of Serum Glycoproteins	49:90	A Method for Comprehensive Glycosite-Mapping and Direct Quantitation of Serum Glycoproteins.
26510530	9	4	theme	biomarker	1494:1502	arg1	discoveries					1504:1514	disease biomarker discoveries	1486:1514	disease biomarker discoveries	1486:1514	This rapid and robust quantitation technique, which provides quantitative information for both proteins and glycosylation, will further facilitate disease biomarker discoveries.
26510530	6	5	gly	glycopeptide	915:926	arg2	glycopeptide					915:926	The glycopeptide ion abundances	911:941	The glycopeptide ion abundances	911:941	The glycopeptide ion abundances were normalized to the respective protein abundances to separate protein glycosylation from protein expression.
26510530	8	6	theme	femtomole	1321:1329	arg1	limit					1298:1302	low limit	1294:1302	low limit of quantitation (femtomole level)	1294:1336	The absolute protein quantitation has a wide linear range (3-4 orders of magnitude) and low limit of quantitation (femtomole level).
26510530	8	6	theme	femtomole	1321:1329	arg1	level					1331:1335	femtomole level	1321:1335	femtomole level	1321:1335	The absolute protein quantitation has a wide linear range (3-4 orders of magnitude) and low limit of quantitation (femtomole level).
26510530	1	7	theme	chromatography	265:278	arg1	MS					335:336	MS	335:336	MS	335:336	A comprehensive glycan map was constructed for the top eight abundant glycoproteins in plasma using both specific and nonspecific enzyme digestions followed by nano liquid chromatography (LC)-chip/quadrupole time-of-flight mass spectrometry (MS) analysis.
26510530	1	7	theme	chromatography	265:278	arg1	spectrometry					321:332	nano liquid chromatography (LC)-chip/quadrupole time-of-flight mass spectrometry	253:332	nano liquid chromatography (LC)-chip/quadrupole time-of-flight mass spectrometry (MS) analysis	253:346	A comprehensive glycan map was constructed for the top eight abundant glycoproteins in plasma using both specific and nonspecific enzyme digestions followed by nano liquid chromatography (LC)-chip/quadrupole time-of-flight mass spectrometry (MS) analysis.
26510530	3	8	theme	MRM	481:483	arg1	technique					486:494	A sensitive and reproducible multiple reaction monitoring (MRM) technique	422:494	A sensitive and reproducible multiple reaction monitoring (MRM) technique on a triple quadrupole MS	422:520	A sensitive and reproducible multiple reaction monitoring (MRM) technique on a triple quadrupole MS was developed and applied to quantify immunoglobulins G, A, M, and their site-specific glycans simultaneously and directly from human serum/plasma without protein enrichments.
26510530	7	9	theme	sample	1116:1121	arg1	loss					1123:1126	less sample loss	1111:1126	less sample loss	1111:1126	This technique yields higher method reproducibility and less sample loss when compared with the quantitation method that involves protein enrichments.
26510530	1	10	from	glycoproteins	163:175	arg1	plasma					180:185	plasma	180:185	plasma	180:185	A comprehensive glycan map was constructed for the top eight abundant glycoproteins in plasma using both specific and nonspecific enzyme digestions followed by nano liquid chromatography (LC)-chip/quadrupole time-of-flight mass spectrometry (MS) analysis.
26510530	7	11	dep	method	1084:1089	arg1	reproducibility					1091:1105	reproducibility	1091:1105	reproducibility	1091:1105	This technique yields higher method reproducibility and less sample loss when compared with the quantitation method that involves protein enrichments.
26510530	6	12	theme	respective	966:975	arg1	glycosylation					1016:1028	the respective protein abundances to separate protein glycosylation	962:1028	the respective protein abundances to separate protein glycosylation from protein expression	962:1052	The glycopeptide ion abundances were normalized to the respective protein abundances to separate protein glycosylation from protein expression.
26510530	9	13	theme	robust	1354:1359	arg1	technique					1374:1382	This rapid and robust quantitation technique	1339:1382	This rapid and robust quantitation technique	1339:1382	This rapid and robust quantitation technique, which provides quantitative information for both proteins and glycosylation, will further facilitate disease biomarker discoveries.
26510530	7	14	theme	quantitation	1151:1162	arg1	method					1164:1169	the quantitation method	1147:1169	the quantitation method that involves protein enrichments	1147:1203	This technique yields higher method reproducibility and less sample loss when compared with the quantitation method that involves protein enrichments.
26510530	8	15	contain	has	1240:1242	arg2	level					1331:1335	femtomole level	1321:1335	femtomole level	1321:1335	The absolute protein quantitation has a wide linear range (3-4 orders of magnitude) and low limit of quantitation (femtomole level).
26510530	8	15	contain	has	1240:1242	arg2	range					1258:1262	a wide linear range	1244:1262	a wide linear range (3-4 orders of magnitude)	1244:1288	The absolute protein quantitation has a wide linear range (3-4 orders of magnitude) and low limit of quantitation (femtomole level).
26510530	8	15	contain	has	1240:1242	arg1	quantitation					1227:1238	The absolute protein quantitation	1206:1238	The absolute protein quantitation	1206:1238	The absolute protein quantitation has a wide linear range (3-4 orders of magnitude) and low limit of quantitation (femtomole level).
26510530	8	15	contain	has	1240:1242	arg2	limit					1298:1302	low limit	1294:1302	low limit of quantitation (femtomole level)	1294:1336	The absolute protein quantitation has a wide linear range (3-4 orders of magnitude) and low limit of quantitation (femtomole level).
26510530	1	16	theme	LC	281:282	arg1	MS					335:336	MS	335:336	MS	335:336	A comprehensive glycan map was constructed for the top eight abundant glycoproteins in plasma using both specific and nonspecific enzyme digestions followed by nano liquid chromatography (LC)-chip/quadrupole time-of-flight mass spectrometry (MS) analysis.
26510530	1	16	theme	LC	281:282	arg1	spectrometry					321:332	nano liquid chromatography (LC)-chip/quadrupole time-of-flight mass spectrometry	253:332	nano liquid chromatography (LC)-chip/quadrupole time-of-flight mass spectrometry (MS) analysis	253:346	A comprehensive glycan map was constructed for the top eight abundant glycoproteins in plasma using both specific and nonspecific enzyme digestions followed by nano liquid chromatography (LC)-chip/quadrupole time-of-flight mass spectrometry (MS) analysis.
26510530	9	17	theme	disease	1486:1492	arg1	discoveries					1504:1514	disease biomarker discoveries	1486:1514	disease biomarker discoveries	1486:1514	This rapid and robust quantitation technique, which provides quantitative information for both proteins and glycosylation, will further facilitate disease biomarker discoveries.
26510530	8	18	theme	low	1294:1296	arg1	limit					1298:1302	low limit	1294:1302	low limit of quantitation (femtomole level)	1294:1336	The absolute protein quantitation has a wide linear range (3-4 orders of magnitude) and low limit of quantitation (femtomole level).
26510530	8	18	theme	low	1294:1296	arg1	level					1331:1335	femtomole level	1321:1335	femtomole level	1321:1335	The absolute protein quantitation has a wide linear range (3-4 orders of magnitude) and low limit of quantitation (femtomole level).
26510530	4	19	theme	UP	815:816	arg1	gradient					821:828	a 20 min ultra high performance (UP)LC gradient	782:828	a 20 min ultra high performance (UP)LC gradient	782:828	A total of 64 glycopeptides and 15 peptides were monitored for IgG, IgA, and IgM in a 20 min ultra high performance (UP)LC gradient.
26510530	8	20	theme	3-4	1265:1267	arg1	orders					1269:1274	3-4 orders	1265:1274	3-4 orders of magnitude	1265:1287	The absolute protein quantitation has a wide linear range (3-4 orders of magnitude) and low limit of quantitation (femtomole level).
26510530	3	21	theme	reaction	460:467	arg1	technique					486:494	A sensitive and reproducible multiple reaction monitoring (MRM) technique	422:494	A sensitive and reproducible multiple reaction monitoring (MRM) technique on a triple quadrupole MS	422:520	A sensitive and reproducible multiple reaction monitoring (MRM) technique on a triple quadrupole MS was developed and applied to quantify immunoglobulins G, A, M, and their site-specific glycans simultaneously and directly from human serum/plasma without protein enrichments.
26510530	3	22	from	serum/plasma	656:667	arg1	M					582:582	M	582:582	M	582:582	A sensitive and reproducible multiple reaction monitoring (MRM) technique on a triple quadrupole MS was developed and applied to quantify immunoglobulins G, A, M, and their site-specific glycans simultaneously and directly from human serum/plasma without protein enrichments.
26510530	3	22	from	serum/plasma	656:667	arg1	immunoglobulins					560:574	immunoglobulins G, A, M, and their site-specific glycans	560:615	immunoglobulins G, A, M, and their site-specific glycans simultaneously and directly from human serum/plasma without protein enrichments	560:695	A sensitive and reproducible multiple reaction monitoring (MRM) technique on a triple quadrupole MS was developed and applied to quantify immunoglobulins G, A, M, and their site-specific glycans simultaneously and directly from human serum/plasma without protein enrichments.
26510530	3	22	from	serum/plasma	656:667	arg1	A					579:579	A	579:579	A	579:579	A sensitive and reproducible multiple reaction monitoring (MRM) technique on a triple quadrupole MS was developed and applied to quantify immunoglobulins G, A, M, and their site-specific glycans simultaneously and directly from human serum/plasma without protein enrichments.
26510530	3	22	from	serum/plasma	656:667	arg1	G					576:576	G	576:576	G	576:576	A sensitive and reproducible multiple reaction monitoring (MRM) technique on a triple quadrupole MS was developed and applied to quantify immunoglobulins G, A, M, and their site-specific glycans simultaneously and directly from human serum/plasma without protein enrichments.
26510530	6	23	dep	glycosylation	1016:1028	arg1	to					996:997	to	996:997	to	996:997	The glycopeptide ion abundances were normalized to the respective protein abundances to separate protein glycosylation from protein expression.
26510530	4	24	theme	20	784:785	arg1	min					787:789	min	787:789	min	787:789	A total of 64 glycopeptides and 15 peptides were monitored for IgG, IgA, and IgM in a 20 min ultra high performance (UP)LC gradient.
26510530	6	25	theme	protein	1008:1014	arg1	glycosylation					1016:1028	the respective protein abundances to separate protein glycosylation	962:1028	the respective protein abundances to separate protein glycosylation from protein expression	962:1052	The glycopeptide ion abundances were normalized to the respective protein abundances to separate protein glycosylation from protein expression.
26510530	3	26	theme	monitoring	469:478	arg1	technique					486:494	A sensitive and reproducible multiple reaction monitoring (MRM) technique	422:494	A sensitive and reproducible multiple reaction monitoring (MRM) technique on a triple quadrupole MS	422:520	A sensitive and reproducible multiple reaction monitoring (MRM) technique on a triple quadrupole MS was developed and applied to quantify immunoglobulins G, A, M, and their site-specific glycans simultaneously and directly from human serum/plasma without protein enrichments.
26510530	7	27	theme	protein	1185:1191	arg1	enrichments					1193:1203	protein enrichments	1185:1203	protein enrichments	1185:1203	This technique yields higher method reproducibility and less sample loss when compared with the quantitation method that involves protein enrichments.
26510530	9	28	theme	rapid	1344:1348	arg1	technique					1374:1382	This rapid and robust quantitation technique	1339:1382	This rapid and robust quantitation technique	1339:1382	This rapid and robust quantitation technique, which provides quantitative information for both proteins and glycosylation, will further facilitate disease biomarker discoveries.
26510530	4	29	theme	LC	818:819	arg1	gradient					821:828	a 20 min ultra high performance (UP)LC gradient	782:828	a 20 min ultra high performance (UP)LC gradient	782:828	A total of 64 glycopeptides and 15 peptides were monitored for IgG, IgA, and IgM in a 20 min ultra high performance (UP)LC gradient.
26510530	3	30	theme	reproducible	438:449	arg1	technique					486:494	A sensitive and reproducible multiple reaction monitoring (MRM) technique	422:494	A sensitive and reproducible multiple reaction monitoring (MRM) technique on a triple quadrupole MS	422:520	A sensitive and reproducible multiple reaction monitoring (MRM) technique on a triple quadrupole MS was developed and applied to quantify immunoglobulins G, A, M, and their site-specific glycans simultaneously and directly from human serum/plasma without protein enrichments.
26510530	1	31	theme	comprehensive	95:107	arg1	map					116:118	A comprehensive glycan map	93:118	A comprehensive glycan map	93:118	A comprehensive glycan map was constructed for the top eight abundant glycoproteins in plasma using both specific and nonspecific enzyme digestions followed by nano liquid chromatography (LC)-chip/quadrupole time-of-flight mass spectrometry (MS) analysis.
26510530	6	32	theme	abundances	985:994	arg1	glycosylation					1016:1028	the respective protein abundances to separate protein glycosylation	962:1028	the respective protein abundances to separate protein glycosylation from protein expression	962:1052	The glycopeptide ion abundances were normalized to the respective protein abundances to separate protein glycosylation from protein expression.
26510530	2	33	theme	software	397:404	arg1	GPFinder					412:419	GPFinder	412:419	GPFinder	412:419	Glycopeptides were identified using an in-house software tool, GPFinder.
26510530	2	33	theme	software	397:404	arg1	tool					406:409	an in-house software tool	385:409	an in-house software tool	385:409	Glycopeptides were identified using an in-house software tool, GPFinder.
26510530	0	34	theme	Comprehensive	13:25	arg1	Glycosite-Mapping					27:43	Comprehensive Glycosite-Mapping	13:43	Comprehensive Glycosite-Mapping	13:43	A Method for Comprehensive Glycosite-Mapping and Direct Quantitation of Serum Glycoproteins.
26510530	1	35	theme	-chip/quadrupole	284:299	arg1	MS					335:336	MS	335:336	MS	335:336	A comprehensive glycan map was constructed for the top eight abundant glycoproteins in plasma using both specific and nonspecific enzyme digestions followed by nano liquid chromatography (LC)-chip/quadrupole time-of-flight mass spectrometry (MS) analysis.
26510530	1	35	theme	-chip/quadrupole	284:299	arg1	spectrometry					321:332	nano liquid chromatography (LC)-chip/quadrupole time-of-flight mass spectrometry	253:332	nano liquid chromatography (LC)-chip/quadrupole time-of-flight mass spectrometry (MS) analysis	253:346	A comprehensive glycan map was constructed for the top eight abundant glycoproteins in plasma using both specific and nonspecific enzyme digestions followed by nano liquid chromatography (LC)-chip/quadrupole time-of-flight mass spectrometry (MS) analysis.
26510530	4	36	gly	glycopeptides	712:724	arg2	glycopeptides					712:724	64 glycopeptides	709:724	64 glycopeptides	709:724	A total of 64 glycopeptides and 15 peptides were monitored for IgG, IgA, and IgM in a 20 min ultra high performance (UP)LC gradient.
26510530	6	37	from	expression	1043:1052	arg1	glycosylation					1016:1028	the respective protein abundances to separate protein glycosylation	962:1028	the respective protein abundances to separate protein glycosylation from protein expression	962:1052	The glycopeptide ion abundances were normalized to the respective protein abundances to separate protein glycosylation from protein expression.
26510530	1	38	theme	glycan	109:114	arg1	map					116:118	A comprehensive glycan map	93:118	A comprehensive glycan map	93:118	A comprehensive glycan map was constructed for the top eight abundant glycoproteins in plasma using both specific and nonspecific enzyme digestions followed by nano liquid chromatography (LC)-chip/quadrupole time-of-flight mass spectrometry (MS) analysis.
26510530	1	39	theme	specific	198:205	arg1	digestions					230:239	both specific and nonspecific enzyme digestions	193:239	both specific and nonspecific enzyme digestions followed by nano liquid chromatography (LC)-chip/quadrupole time-of-flight mass spectrometry (MS) analysis	193:346	A comprehensive glycan map was constructed for the top eight abundant glycoproteins in plasma using both specific and nonspecific enzyme digestions followed by nano liquid chromatography (LC)-chip/quadrupole time-of-flight mass spectrometry (MS) analysis.
26510530	5	40	theme	peptide	883:889	arg1	curves					903:908	peptide calibration curves	883:908	peptide calibration curves	883:908	The absolute protein contents were quantified using peptide calibration curves.
26510530	1	41	theme	time-of-flight	301:314	arg1	MS					335:336	MS	335:336	MS	335:336	A comprehensive glycan map was constructed for the top eight abundant glycoproteins in plasma using both specific and nonspecific enzyme digestions followed by nano liquid chromatography (LC)-chip/quadrupole time-of-flight mass spectrometry (MS) analysis.
26510530	1	41	theme	time-of-flight	301:314	arg1	spectrometry					321:332	nano liquid chromatography (LC)-chip/quadrupole time-of-flight mass spectrometry	253:332	nano liquid chromatography (LC)-chip/quadrupole time-of-flight mass spectrometry (MS) analysis	253:346	A comprehensive glycan map was constructed for the top eight abundant glycoproteins in plasma using both specific and nonspecific enzyme digestions followed by nano liquid chromatography (LC)-chip/quadrupole time-of-flight mass spectrometry (MS) analysis.
26510530	7	42	theme	higher	1077:1082	arg1	method					1084:1089	higher method reproducibility and less sample loss	1077:1126	method	1084:1089	This technique yields higher method reproducibility and less sample loss when compared with the quantitation method that involves protein enrichments.
26510530	3	43	theme	human	650:654	arg1	serum/plasma					656:667	human serum/plasma	650:667	human serum/plasma without protein enrichments	650:695	A sensitive and reproducible multiple reaction monitoring (MRM) technique on a triple quadrupole MS was developed and applied to quantify immunoglobulins G, A, M, and their site-specific glycans simultaneously and directly from human serum/plasma without protein enrichments.
26510530	2	44	theme	in-house	388:395	arg1	GPFinder					412:419	GPFinder	412:419	GPFinder	412:419	Glycopeptides were identified using an in-house software tool, GPFinder.
26510530	2	44	theme	in-house	388:395	arg1	tool					406:409	an in-house software tool	385:409	an in-house software tool	385:409	Glycopeptides were identified using an in-house software tool, GPFinder.
26510530	3	45	theme	sensitive	424:432	arg1	technique					486:494	A sensitive and reproducible multiple reaction monitoring (MRM) technique	422:494	A sensitive and reproducible multiple reaction monitoring (MRM) technique on a triple quadrupole MS	422:520	A sensitive and reproducible multiple reaction monitoring (MRM) technique on a triple quadrupole MS was developed and applied to quantify immunoglobulins G, A, M, and their site-specific glycans simultaneously and directly from human serum/plasma without protein enrichments.
26510530	1	46	theme	mass	316:319	arg1	MS					335:336	MS	335:336	MS	335:336	A comprehensive glycan map was constructed for the top eight abundant glycoproteins in plasma using both specific and nonspecific enzyme digestions followed by nano liquid chromatography (LC)-chip/quadrupole time-of-flight mass spectrometry (MS) analysis.
26510530	1	46	theme	mass	316:319	arg1	spectrometry					321:332	nano liquid chromatography (LC)-chip/quadrupole time-of-flight mass spectrometry	253:332	nano liquid chromatography (LC)-chip/quadrupole time-of-flight mass spectrometry (MS) analysis	253:346	A comprehensive glycan map was constructed for the top eight abundant glycoproteins in plasma using both specific and nonspecific enzyme digestions followed by nano liquid chromatography (LC)-chip/quadrupole time-of-flight mass spectrometry (MS) analysis.
26510530	6	47	theme	protein	1035:1041	arg1	expression					1043:1052	protein expression	1035:1052	protein expression	1035:1052	The glycopeptide ion abundances were normalized to the respective protein abundances to separate protein glycosylation from protein expression.
26510530	4	48	theme	ultra	791:795	arg1	gradient					821:828	a 20 min ultra high performance (UP)LC gradient	782:828	a 20 min ultra high performance (UP)LC gradient	782:828	A total of 64 glycopeptides and 15 peptides were monitored for IgG, IgA, and IgM in a 20 min ultra high performance (UP)LC gradient.
26510530	3	49	theme	multiple	451:458	arg1	technique					486:494	A sensitive and reproducible multiple reaction monitoring (MRM) technique	422:494	A sensitive and reproducible multiple reaction monitoring (MRM) technique on a triple quadrupole MS	422:520	A sensitive and reproducible multiple reaction monitoring (MRM) technique on a triple quadrupole MS was developed and applied to quantify immunoglobulins G, A, M, and their site-specific glycans simultaneously and directly from human serum/plasma without protein enrichments.
26510530	1	50	theme	nonspecific	211:221	arg1	digestions					230:239	both specific and nonspecific enzyme digestions	193:239	both specific and nonspecific enzyme digestions followed by nano liquid chromatography (LC)-chip/quadrupole time-of-flight mass spectrometry (MS) analysis	193:346	A comprehensive glycan map was constructed for the top eight abundant glycoproteins in plasma using both specific and nonspecific enzyme digestions followed by nano liquid chromatography (LC)-chip/quadrupole time-of-flight mass spectrometry (MS) analysis.
26510530	1	51	theme	spectrometry	321:332	arg1	analysis					339:346	nano liquid chromatography (LC)-chip/quadrupole time-of-flight mass spectrometry (MS) analysis	253:346	nano liquid chromatography (LC)-chip/quadrupole time-of-flight mass spectrometry (MS) analysis	253:346	A comprehensive glycan map was constructed for the top eight abundant glycoproteins in plasma using both specific and nonspecific enzyme digestions followed by nano liquid chromatography (LC)-chip/quadrupole time-of-flight mass spectrometry (MS) analysis.
26510530	6	52	theme	protein	977:983	arg1	glycosylation					1016:1028	the respective protein abundances to separate protein glycosylation	962:1028	the respective protein abundances to separate protein glycosylation from protein expression	962:1052	The glycopeptide ion abundances were normalized to the respective protein abundances to separate protein glycosylation from protein expression.
26510530	4	53	theme	glycopeptides	712:724	arg1	total					700:704	A total	698:704	A total of 64 glycopeptides and 15 peptides	698:740	A total of 64 glycopeptides and 15 peptides were monitored for IgG, IgA, and IgM in a 20 min ultra high performance (UP)LC gradient.
26510530	4	54	theme	min	787:789	arg1	gradient					821:828	a 20 min ultra high performance (UP)LC gradient	782:828	a 20 min ultra high performance (UP)LC gradient	782:828	A total of 64 glycopeptides and 15 peptides were monitored for IgG, IgA, and IgM in a 20 min ultra high performance (UP)LC gradient.
26510530	1	55	theme	enzyme	223:228	arg1	digestions					230:239	both specific and nonspecific enzyme digestions	193:239	both specific and nonspecific enzyme digestions followed by nano liquid chromatography (LC)-chip/quadrupole time-of-flight mass spectrometry (MS) analysis	193:346	A comprehensive glycan map was constructed for the top eight abundant glycoproteins in plasma using both specific and nonspecific enzyme digestions followed by nano liquid chromatography (LC)-chip/quadrupole time-of-flight mass spectrometry (MS) analysis.
26510530	8	56	theme	wide	1246:1249	arg1	range					1258:1262	a wide linear range	1244:1262	a wide linear range (3-4 orders of magnitude)	1244:1288	The absolute protein quantitation has a wide linear range (3-4 orders of magnitude) and low limit of quantitation (femtomole level).
26510530	5	57	theme	protein	844:850	arg1	contents					852:859	The absolute protein contents	831:859	The absolute protein contents	831:859	The absolute protein contents were quantified using peptide calibration curves.
26510530	4	58	theme	performance	802:812	arg1	gradient					821:828	a 20 min ultra high performance (UP)LC gradient	782:828	a 20 min ultra high performance (UP)LC gradient	782:828	A total of 64 glycopeptides and 15 peptides were monitored for IgG, IgA, and IgM in a 20 min ultra high performance (UP)LC gradient.
26510530	9	59	theme	quantitative	1400:1411	arg1	information					1413:1423	quantitative information	1400:1423	quantitative information for both proteins and glycosylation	1400:1459	This rapid and robust quantitation technique, which provides quantitative information for both proteins and glycosylation, will further facilitate disease biomarker discoveries.
26510530	3	60	theme	triple	501:506	arg1	quadrupole					508:517	a triple quadrupole	499:517	a triple quadrupole MS	499:520	A sensitive and reproducible multiple reaction monitoring (MRM) technique on a triple quadrupole MS was developed and applied to quantify immunoglobulins G, A, M, and their site-specific glycans simultaneously and directly from human serum/plasma without protein enrichments.
26510530	0	61	theme	Direct	49:54	arg1	Quantitation					56:67	Direct Quantitation	49:67	Direct Quantitation of Serum Glycoproteins	49:90	A Method for Comprehensive Glycosite-Mapping and Direct Quantitation of Serum Glycoproteins.
26510530	9	62	theme	quantitation	1361:1372	arg1	technique					1374:1382	This rapid and robust quantitation technique	1339:1382	This rapid and robust quantitation technique	1339:1382	This rapid and robust quantitation technique, which provides quantitative information for both proteins and glycosylation, will further facilitate disease biomarker discoveries.
26510530	4	63	theme	high	797:800	arg1	gradient					821:828	a 20 min ultra high performance (UP)LC gradient	782:828	a 20 min ultra high performance (UP)LC gradient	782:828	A total of 64 glycopeptides and 15 peptides were monitored for IgG, IgA, and IgM in a 20 min ultra high performance (UP)LC gradient.
26510530	3	64	theme	quadrupole	508:517	arg1	MS					519:520	a triple quadrupole MS	499:520	a triple quadrupole MS	499:520	A sensitive and reproducible multiple reaction monitoring (MRM) technique on a triple quadrupole MS was developed and applied to quantify immunoglobulins G, A, M, and their site-specific glycans simultaneously and directly from human serum/plasma without protein enrichments.
26510530	6	65	theme	ion	928:930	arg1	abundances					932:941	The glycopeptide ion abundances	911:941	The glycopeptide ion abundances	911:941	The glycopeptide ion abundances were normalized to the respective protein abundances to separate protein glycosylation from protein expression.
26510530	1	66	gly	glycoproteins	163:175	arg1	glycoproteins					163:175	the top eight abundant glycoproteins	140:175	the top eight abundant glycoproteins in plasma	140:185	A comprehensive glycan map was constructed for the top eight abundant glycoproteins in plasma using both specific and nonspecific enzyme digestions followed by nano liquid chromatography (LC)-chip/quadrupole time-of-flight mass spectrometry (MS) analysis.
26510530	3	67	from	technique	486:494	arg1	MS					519:520	a triple quadrupole MS	499:520	a triple quadrupole MS	499:520	A sensitive and reproducible multiple reaction monitoring (MRM) technique on a triple quadrupole MS was developed and applied to quantify immunoglobulins G, A, M, and their site-specific glycans simultaneously and directly from human serum/plasma without protein enrichments.
26510530	4	68	theme	peptides	733:740	arg1	total					700:704	A total	698:704	A total of 64 glycopeptides and 15 peptides	698:740	A total of 64 glycopeptides and 15 peptides were monitored for IgG, IgA, and IgM in a 20 min ultra high performance (UP)LC gradient.
26510530	5	69	theme	absolute	835:842	arg1	contents					852:859	The absolute protein contents	831:859	The absolute protein contents	831:859	The absolute protein contents were quantified using peptide calibration curves.
26510530	8	70	theme	magnitude	1279:1287	arg1	orders					1269:1274	3-4 orders	1265:1274	3-4 orders of magnitude	1265:1287	The absolute protein quantitation has a wide linear range (3-4 orders of magnitude) and low limit of quantitation (femtomole level).
26510530	3	71	dep	immunoglobulins	560:574	arg1	glycans					609:615	their site-specific glycans	589:615	their site-specific glycans	589:615	A sensitive and reproducible multiple reaction monitoring (MRM) technique on a triple quadrupole MS was developed and applied to quantify immunoglobulins G, A, M, and their site-specific glycans simultaneously and directly from human serum/plasma without protein enrichments.
26510530	3	71	dep	immunoglobulins	560:574	arg1	M					582:582	M	582:582	M	582:582	A sensitive and reproducible multiple reaction monitoring (MRM) technique on a triple quadrupole MS was developed and applied to quantify immunoglobulins G, A, M, and their site-specific glycans simultaneously and directly from human serum/plasma without protein enrichments.
26510530	3	71	dep	immunoglobulins	560:574	arg1	immunoglobulins					560:574	immunoglobulins G, A, M, and their site-specific glycans	560:615	immunoglobulins G, A, M, and their site-specific glycans simultaneously and directly from human serum/plasma without protein enrichments	560:695	A sensitive and reproducible multiple reaction monitoring (MRM) technique on a triple quadrupole MS was developed and applied to quantify immunoglobulins G, A, M, and their site-specific glycans simultaneously and directly from human serum/plasma without protein enrichments.
26510530	3	71	dep	immunoglobulins	560:574	arg1	A					579:579	A	579:579	A	579:579	A sensitive and reproducible multiple reaction monitoring (MRM) technique on a triple quadrupole MS was developed and applied to quantify immunoglobulins G, A, M, and their site-specific glycans simultaneously and directly from human serum/plasma without protein enrichments.
26510530	3	71	dep	immunoglobulins	560:574	arg1	G					576:576	G	576:576	G	576:576	A sensitive and reproducible multiple reaction monitoring (MRM) technique on a triple quadrupole MS was developed and applied to quantify immunoglobulins G, A, M, and their site-specific glycans simultaneously and directly from human serum/plasma without protein enrichments.
26510530	5	72	theme	calibration	891:901	arg1	curves					903:908	peptide calibration curves	883:908	peptide calibration curves	883:908	The absolute protein contents were quantified using peptide calibration curves.
26510530	0	73	theme	Serum	72:76	arg1	Glycoproteins					78:90	Serum Glycoproteins	72:90	Serum Glycoproteins	72:90	A Method for Comprehensive Glycosite-Mapping and Direct Quantitation of Serum Glycoproteins.
26510530	3	74	theme	protein	677:683	arg1	enrichments					685:695	protein enrichments	677:695	protein enrichments	677:695	A sensitive and reproducible multiple reaction monitoring (MRM) technique on a triple quadrupole MS was developed and applied to quantify immunoglobulins G, A, M, and their site-specific glycans simultaneously and directly from human serum/plasma without protein enrichments.
26510530	3	75	theme	site-specific	595:607	arg1	glycans					609:615	their site-specific glycans	589:615	their site-specific glycans	589:615	A sensitive and reproducible multiple reaction monitoring (MRM) technique on a triple quadrupole MS was developed and applied to quantify immunoglobulins G, A, M, and their site-specific glycans simultaneously and directly from human serum/plasma without protein enrichments.
26510530	1	76	theme	top	144:146	arg1	glycoproteins					163:175	the top eight abundant glycoproteins	140:175	the top eight abundant glycoproteins in plasma	140:185	A comprehensive glycan map was constructed for the top eight abundant glycoproteins in plasma using both specific and nonspecific enzyme digestions followed by nano liquid chromatography (LC)-chip/quadrupole time-of-flight mass spectrometry (MS) analysis.
26510530	8	77	theme	linear	1251:1256	arg1	range					1258:1262	a wide linear range	1244:1262	a wide linear range (3-4 orders of magnitude)	1244:1288	The absolute protein quantitation has a wide linear range (3-4 orders of magnitude) and low limit of quantitation (femtomole level).
26510530	6	78	theme	separate	999:1006	arg1	glycosylation					1016:1028	the respective protein abundances to separate protein glycosylation	962:1028	the respective protein abundances to separate protein glycosylation from protein expression	962:1052	The glycopeptide ion abundances were normalized to the respective protein abundances to separate protein glycosylation from protein expression.
26510530	8	79	dep	range	1258:1262	arg1	orders					1269:1274	3-4 orders	1265:1274	3-4 orders of magnitude	1265:1287	The absolute protein quantitation has a wide linear range (3-4 orders of magnitude) and low limit of quantitation (femtomole level).
26510530	8	80	theme	absolute	1210:1217	arg1	quantitation					1227:1238	The absolute protein quantitation	1206:1238	The absolute protein quantitation	1206:1238	The absolute protein quantitation has a wide linear range (3-4 orders of magnitude) and low limit of quantitation (femtomole level).
26510530	8	81	theme	quantitation	1307:1318	arg1	limit					1298:1302	low limit	1294:1302	low limit of quantitation (femtomole level)	1294:1336	The absolute protein quantitation has a wide linear range (3-4 orders of magnitude) and low limit of quantitation (femtomole level).
26510530	8	81	theme	quantitation	1307:1318	arg1	range					1258:1262	a wide linear range	1244:1262	a wide linear range (3-4 orders of magnitude)	1244:1288	The absolute protein quantitation has a wide linear range (3-4 orders of magnitude) and low limit of quantitation (femtomole level).
26510530	8	81	theme	quantitation	1307:1318	arg1	level					1331:1335	femtomole level	1321:1335	femtomole level	1321:1335	The absolute protein quantitation has a wide linear range (3-4 orders of magnitude) and low limit of quantitation (femtomole level).
26510530	6	82	theme	glycopeptide	915:926	arg1	abundances					932:941	The glycopeptide ion abundances	911:941	The glycopeptide ion abundances	911:941	The glycopeptide ion abundances were normalized to the respective protein abundances to separate protein glycosylation from protein expression.
26510530	1	83	theme	nano	253:256	arg1	MS					335:336	MS	335:336	MS	335:336	A comprehensive glycan map was constructed for the top eight abundant glycoproteins in plasma using both specific and nonspecific enzyme digestions followed by nano liquid chromatography (LC)-chip/quadrupole time-of-flight mass spectrometry (MS) analysis.
26510530	1	83	theme	nano	253:256	arg1	spectrometry					321:332	nano liquid chromatography (LC)-chip/quadrupole time-of-flight mass spectrometry	253:332	nano liquid chromatography (LC)-chip/quadrupole time-of-flight mass spectrometry (MS) analysis	253:346	A comprehensive glycan map was constructed for the top eight abundant glycoproteins in plasma using both specific and nonspecific enzyme digestions followed by nano liquid chromatography (LC)-chip/quadrupole time-of-flight mass spectrometry (MS) analysis.
23090970	8	0	theme	glycoprotein	1109:1120	arg1	dynamics					1122:1129	glycoprotein dynamics	1109:1129	glycoprotein dynamics	1109:1129	Five different profiles of glycoprotein dynamics during cancer development were detected, and they contained several proteins with known roles in breast cancer.
23090970	9	1	theme	body	1400:1403	arg1	fluid					1405:1409	this important body fluid	1385:1409	this important body fluid	1385:1409	We then used the super-SILAC mix in plasma, which led to the quantification of a large number of the previously identified N-glycopeptides in this important body fluid.
23090970	8	2	theme	breast	1228:1233	arg1	cancer					1235:1240	breast cancer	1228:1240	breast cancer	1228:1240	Five different profiles of glycoprotein dynamics during cancer development were detected, and they contained several proteins with known roles in breast cancer.
23090970	9	3	theme	identified	1355:1364	arg1	N-glycopeptides					1366:1380	the previously identified N-glycopeptides	1340:1380	the previously identified N-glycopeptides in this important body fluid	1340:1409	We then used the super-SILAC mix in plasma, which led to the quantification of a large number of the previously identified N-glycopeptides in this important body fluid.
23090970	10	4	theme	super-SILAC	1505:1515	arg1	approach					1517:1524	a super-SILAC approach	1503:1524	a super-SILAC approach	1503:1524	The combination of quantifying the secretome of cancer cell lines and of human plasma with a super-SILAC approach appears to be a promising new approach for finding markers of disease.
23090970	10	5	theme	lines	1472:1476	arg1	secretome					1447:1455	the secretome	1443:1455	the secretome of cancer cell lines and of human plasma	1443:1496	The combination of quantifying the secretome of cancer cell lines and of human plasma with a super-SILAC approach appears to be a promising new approach for finding markers of disease.
23090970	1	6	theme	proteins	155:162	arg1	number					145:150	a large number	137:150	a large number of proteins to communicate with their surroundings	137:201	Cells secrete a large number of proteins to communicate with their surroundings.
23090970	8	7	with	proteins	1199:1206	arg1	roles					1219:1223	known roles	1213:1223	known roles in breast cancer	1213:1240	Five different profiles of glycoprotein dynamics during cancer development were detected, and they contained several proteins with known roles in breast cancer.
23090970	4	8	theme	super-SILAC	607:617	arg1	mix					619:621	a super-SILAC mix	605:621	a super-SILAC mix from several labeled breast cancer cell lines	605:667	For accurate quantification we developed a super-SILAC mix from several labeled breast cancer cell lines and used it as an internal standard for all samples.
23090970	0	9	theme	human	102:106	arg1	samples					114:120	human blood samples	102:120	human blood samples	102:120	Quantification of the N-glycosylated secretome by super-SILAC during breast cancer progression and in human blood samples.
23090970	9	10	theme	N-glycopeptides	1366:1380	arg1	number					1330:1335	a large number	1322:1335	a large number of the previously identified N-glycopeptides in this important body fluid	1322:1409	We then used the super-SILAC mix in plasma, which led to the quantification of a large number of the previously identified N-glycopeptides in this important body fluid.
23090970	9	11	theme	super-SILAC	1260:1270	arg1	mix					1272:1274	the super-SILAC mix	1256:1274	the super-SILAC mix in plasma, which led to the quantification of a large number of the previously identified N-glycopeptides in this important body fluid	1256:1409	We then used the super-SILAC mix in plasma, which led to the quantification of a large number of the previously identified N-glycopeptides in this important body fluid.
23090970	2	12	theme	extracellular	294:306	arg1	space					308:312	the extracellular space	290:312	the extracellular space	290:312	Furthermore, plasma membrane proteins and intracellular proteins can be released into the extracellular space by regulated or non-regulated processes.
23090970	4	13	theme	several	628:634	arg1	lines					663:667	several labeled breast cancer cell lines	628:667	several labeled breast cancer cell lines	628:667	For accurate quantification we developed a super-SILAC mix from several labeled breast cancer cell lines and used it as an internal standard for all samples.
23090970	5	14	theme	N-glycosylation	744:758	arg1	sites					760:764	1398 unique N-glycosylation sites	732:764	1398 unique N-glycosylation sites	732:764	In total, 1398 unique N-glycosylation sites were identified and quantified.
23090970	8	15	theme	dynamics	1122:1129	arg1	profiles					1097:1104	Five different profiles	1082:1104	Five different profiles of glycoprotein dynamics during cancer development	1082:1155	Five different profiles of glycoprotein dynamics during cancer development were detected, and they contained several proteins with known roles in breast cancer.
23090970	10	16	theme	cancer	1460:1465	arg1	lines					1472:1476	cancer cell lines	1460:1476	cancer cell lines	1460:1476	The combination of quantifying the secretome of cancer cell lines and of human plasma with a super-SILAC approach appears to be a promising new approach for finding markers of disease.
23090970	7	17	theme	N-glycosylated	904:917	arg1	profiles					929:936	N-glycosylated secretome profiles	904:936	N-glycosylated secretome profiles	904:936	N-glycosylated secretome profiles correctly clustered the different cell lines to their respective cancer stage, suggesting that biologically relevant differences were detected.
23090970	7	18	gly	N-glycosylated	904:917	arg1	profiles					929:936	N-glycosylated secretome profiles	904:936	N-glycosylated secretome profiles	904:936	N-glycosylated secretome profiles correctly clustered the different cell lines to their respective cancer stage, suggesting that biologically relevant differences were detected.
23090970	7	19	theme	secretome	919:927	arg1	profiles					929:936	N-glycosylated secretome profiles	904:936	N-glycosylated secretome profiles	904:936	N-glycosylated secretome profiles correctly clustered the different cell lines to their respective cancer stage, suggesting that biologically relevant differences were detected.
23090970	3	20	theme	stages	443:448	arg1	representative					415:428	representative	415:428	representative	415:428	Here, we profiled the supernatant of 11 cell lines that are representative of different stages of breast cancer development by specifically capturing N-glycosylated peptides using the N-glyco FASP technology.
23090970	0	21	theme	blood	108:112	arg1	samples					114:120	human blood samples	102:120	human blood samples	102:120	Quantification of the N-glycosylated secretome by super-SILAC during breast cancer progression and in human blood samples.
23090970	9	22	theme	important	1390:1398	arg1	fluid					1405:1409	this important body fluid	1385:1409	this important body fluid	1385:1409	We then used the super-SILAC mix in plasma, which led to the quantification of a large number of the previously identified N-glycopeptides in this important body fluid.
23090970	8	23	theme	cancer	1138:1143	arg1	development					1145:1155	cancer development	1138:1155	cancer development	1138:1155	Five different profiles of glycoprotein dynamics during cancer development were detected, and they contained several proteins with known roles in breast cancer.
23090970	7	24	theme	cancer	1003:1008	arg1	stage					1010:1014	their respective cancer stage	986:1014	their respective cancer stage	986:1014	N-glycosylated secretome profiles correctly clustered the different cell lines to their respective cancer stage, suggesting that biologically relevant differences were detected.
23090970	10	25	theme	plasma	1491:1496	arg1	secretome					1447:1455	the secretome	1443:1455	the secretome of cancer cell lines and of human plasma	1443:1496	The combination of quantifying the secretome of cancer cell lines and of human plasma with a super-SILAC approach appears to be a promising new approach for finding markers of disease.
23090970	8	26	contain	contained	1181:1189	arg1	they					1176:1179	they	1176:1179	they	1176:1179	Five different profiles of glycoprotein dynamics during cancer development were detected, and they contained several proteins with known roles in breast cancer.
23090970	8	26	contain	contained	1181:1189	arg2	proteins					1199:1206	several proteins	1191:1206	several proteins with known roles in breast cancer	1191:1240	Five different profiles of glycoprotein dynamics during cancer development were detected, and they contained several proteins with known roles in breast cancer.
23090970	9	27	from	fluid	1405:1409	arg1	number					1330:1335	a large number	1322:1335	a large number of the previously identified N-glycopeptides in this important body fluid	1322:1409	We then used the super-SILAC mix in plasma, which led to the quantification of a large number of the previously identified N-glycopeptides in this important body fluid.
23090970	6	28	theme	N-glycosylated	812:825	arg1	peptides					827:834	N-glycosylated peptides	812:834	N-glycosylated peptides	812:834	Enriching for N-glycosylated peptides focused the analysis on classically secreted and membrane proteins.
23090970	5	29	gly	N-glycosylation	744:758	arg2	1398					732:735	1398	732:735	1398	732:735	In total, 1398 unique N-glycosylation sites were identified and quantified.
23090970	5	29	gly	N-glycosylation	744:758	arg2	sites					760:764	1398 unique N-glycosylation sites	732:764	1398 unique N-glycosylation sites	732:764	In total, 1398 unique N-glycosylation sites were identified and quantified.
23090970	3	30	theme	cell	395:398	arg1	lines					400:404	11 cell lines	392:404	11 cell lines that are representative of different stages of breast cancer development by specifically capturing N-glycosylated peptides using the N-glyco FASP technology	392:561	Here, we profiled the supernatant of 11 cell lines that are representative of different stages of breast cancer development by specifically capturing N-glycosylated peptides using the N-glyco FASP technology.
23090970	6	31	gly	N-glycosylated	812:825	arg1	peptides					827:834	N-glycosylated peptides	812:834	N-glycosylated peptides	812:834	Enriching for N-glycosylated peptides focused the analysis on classically secreted and membrane proteins.
23090970	3	32	gly	N-glycosylated	505:518	arg1	peptides					520:527	N-glycosylated peptides	505:527	N-glycosylated peptides using the N-glyco FASP technology	505:561	Here, we profiled the supernatant of 11 cell lines that are representative of different stages of breast cancer development by specifically capturing N-glycosylated peptides using the N-glyco FASP technology.
23090970	3	33	theme	different	433:441	arg1	stages					443:448	different stages	433:448	different stages of breast cancer development	433:477	Here, we profiled the supernatant of 11 cell lines that are representative of different stages of breast cancer development by specifically capturing N-glycosylated peptides using the N-glyco FASP technology.
23090970	0	34	theme	N-glycosylated	22:35	arg1	Quantification					0:13	Quantification	0:13	Quantification of the N-glycosylated	0:35	Quantification of the N-glycosylated secretome by super-SILAC during breast cancer progression and in human blood samples.
23090970	7	35	theme	respective	992:1001	arg1	stage					1010:1014	their respective cancer stage	986:1014	their respective cancer stage	986:1014	N-glycosylated secretome profiles correctly clustered the different cell lines to their respective cancer stage, suggesting that biologically relevant differences were detected.
23090970	3	36	theme	development	467:477	arg1	stages					443:448	different stages	433:448	different stages of breast cancer development	433:477	Here, we profiled the supernatant of 11 cell lines that are representative of different stages of breast cancer development by specifically capturing N-glycosylated peptides using the N-glyco FASP technology.
23090970	2	37	theme	regulated	317:325	arg1	processes					344:352	regulated or non-regulated processes	317:352	regulated or non-regulated processes	317:352	Furthermore, plasma membrane proteins and intracellular proteins can be released into the extracellular space by regulated or non-regulated processes.
23090970	1	38	theme	large	139:143	arg1	number					145:150	a large number	137:150	a large number of proteins to communicate with their surroundings	137:201	Cells secrete a large number of proteins to communicate with their surroundings.
23090970	10	39	theme	human	1485:1489	arg1	plasma					1491:1496	human plasma	1485:1496	human plasma	1485:1496	The combination of quantifying the secretome of cancer cell lines and of human plasma with a super-SILAC approach appears to be a promising new approach for finding markers of disease.
23090970	10	40	theme	new	1552:1554	arg1	approach					1556:1563	a promising new approach	1540:1563	a promising new approach for finding markers of disease	1540:1594	The combination of quantifying the secretome of cancer cell lines and of human plasma with a super-SILAC approach appears to be a promising new approach for finding markers of disease.
23090970	10	40	theme	new	1552:1554	arg1	combination					1416:1426	The combination	1412:1426	The combination of quantifying the secretome of cancer cell lines and of human plasma with a super-SILAC approach	1412:1524	The combination of quantifying the secretome of cancer cell lines and of human plasma with a super-SILAC approach appears to be a promising new approach for finding markers of disease.
23090970	9	41	used	used	1251:1254	arg2	We					1243:1244	We	1243:1244	We	1243:1244	We then used the super-SILAC mix in plasma, which led to the quantification of a large number of the previously identified N-glycopeptides in this important body fluid.
23090970	4	42	from	lines	663:667	arg1	mix					619:621	a super-SILAC mix	605:621	a super-SILAC mix from several labeled breast cancer cell lines	605:667	For accurate quantification we developed a super-SILAC mix from several labeled breast cancer cell lines and used it as an internal standard for all samples.
23090970	3	43	theme	breast	453:458	arg1	development					467:477	breast cancer development	453:477	breast cancer development	453:477	Here, we profiled the supernatant of 11 cell lines that are representative of different stages of breast cancer development by specifically capturing N-glycosylated peptides using the N-glyco FASP technology.
23090970	9	44	from	mix	1272:1274	arg1	plasma					1279:1284	plasma	1279:1284	plasma	1279:1284	We then used the super-SILAC mix in plasma, which led to the quantification of a large number of the previously identified N-glycopeptides in this important body fluid.
23090970	9	45	from	N-glycopeptides	1366:1380	arg1	fluid					1405:1409	this important body fluid	1385:1409	this important body fluid	1385:1409	We then used the super-SILAC mix in plasma, which led to the quantification of a large number of the previously identified N-glycopeptides in this important body fluid.
23090970	3	46	theme	cancer	460:465	arg1	development					467:477	breast cancer development	453:477	breast cancer development	453:477	Here, we profiled the supernatant of 11 cell lines that are representative of different stages of breast cancer development by specifically capturing N-glycosylated peptides using the N-glyco FASP technology.
23090970	3	47	theme	lines	400:404	arg1	supernatant					377:387	the supernatant	373:387	the supernatant of 11 cell lines that are representative of different stages of breast cancer development by specifically capturing N-glycosylated peptides using the N-glyco FASP technology	373:561	Here, we profiled the supernatant of 11 cell lines that are representative of different stages of breast cancer development by specifically capturing N-glycosylated peptides using the N-glyco FASP technology.
23090970	5	48	theme	unique	737:742	arg1	sites					760:764	1398 unique N-glycosylation sites	732:764	1398 unique N-glycosylation sites	732:764	In total, 1398 unique N-glycosylation sites were identified and quantified.
23090970	10	49	theme	disease	1588:1594	arg1	markers					1577:1583	markers	1577:1583	markers of disease	1577:1594	The combination of quantifying the secretome of cancer cell lines and of human plasma with a super-SILAC approach appears to be a promising new approach for finding markers of disease.
23090970	8	50	from	roles	1219:1223	arg1	cancer					1235:1240	breast cancer	1228:1240	breast cancer	1228:1240	Five different profiles of glycoprotein dynamics during cancer development were detected, and they contained several proteins with known roles in breast cancer.
23090970	2	51	theme	membrane	224:231	arg1	proteins					233:240	plasma membrane proteins	217:240	plasma membrane proteins	217:240	Furthermore, plasma membrane proteins and intracellular proteins can be released into the extracellular space by regulated or non-regulated processes.
23090970	3	52	theme	N-glycosylated	505:518	arg1	peptides					520:527	N-glycosylated peptides	505:527	N-glycosylated peptides using the N-glyco FASP technology	505:561	Here, we profiled the supernatant of 11 cell lines that are representative of different stages of breast cancer development by specifically capturing N-glycosylated peptides using the N-glyco FASP technology.
23090970	10	53	theme	promising	1542:1550	arg1	approach					1556:1563	a promising new approach	1540:1563	a promising new approach for finding markers of disease	1540:1594	The combination of quantifying the secretome of cancer cell lines and of human plasma with a super-SILAC approach appears to be a promising new approach for finding markers of disease.
23090970	10	53	theme	promising	1542:1550	arg1	combination					1416:1426	The combination	1412:1426	The combination of quantifying the secretome of cancer cell lines and of human plasma with a super-SILAC approach	1412:1524	The combination of quantifying the secretome of cancer cell lines and of human plasma with a super-SILAC approach appears to be a promising new approach for finding markers of disease.
23090970	4	54	theme	accurate	568:575	arg1	quantification					577:590	accurate quantification	568:590	accurate quantification	568:590	For accurate quantification we developed a super-SILAC mix from several labeled breast cancer cell lines and used it as an internal standard for all samples.
23090970	8	55	theme	several	1191:1197	arg1	proteins					1199:1206	several proteins	1191:1206	several proteins with known roles in breast cancer	1191:1240	Five different profiles of glycoprotein dynamics during cancer development were detected, and they contained several proteins with known roles in breast cancer.
23090970	6	56	theme	membrane	885:892	arg1	proteins					894:901	membrane proteins	885:901	membrane proteins	885:901	Enriching for N-glycosylated peptides focused the analysis on classically secreted and membrane proteins.
23090970	2	57	theme	plasma	217:222	arg1	proteins					233:240	plasma membrane proteins	217:240	plasma membrane proteins	217:240	Furthermore, plasma membrane proteins and intracellular proteins can be released into the extracellular space by regulated or non-regulated processes.
23090970	9	58	from	number	1330:1335	arg1	fluid					1405:1409	this important body fluid	1385:1409	this important body fluid	1385:1409	We then used the super-SILAC mix in plasma, which led to the quantification of a large number of the previously identified N-glycopeptides in this important body fluid.
23090970	8	59	theme	different	1087:1095	arg1	profiles					1097:1104	Five different profiles	1082:1104	Five different profiles of glycoprotein dynamics during cancer development	1082:1155	Five different profiles of glycoprotein dynamics during cancer development were detected, and they contained several proteins with known roles in breast cancer.
23090970	8	60	theme	known	1213:1217	arg1	roles					1219:1223	known roles	1213:1223	known roles in breast cancer	1213:1240	Five different profiles of glycoprotein dynamics during cancer development were detected, and they contained several proteins with known roles in breast cancer.
23090970	9	61	theme	large	1324:1328	arg1	number					1330:1335	a large number	1322:1335	a large number of the previously identified N-glycopeptides in this important body fluid	1322:1409	We then used the super-SILAC mix in plasma, which led to the quantification of a large number of the previously identified N-glycopeptides in this important body fluid.
23090970	10	62	theme	cell	1467:1470	arg1	lines					1472:1476	cancer cell lines	1460:1476	cancer cell lines	1460:1476	The combination of quantifying the secretome of cancer cell lines and of human plasma with a super-SILAC approach appears to be a promising new approach for finding markers of disease.
23090970	9	63	gly	N-glycopeptides	1366:1380	arg2	N-glycopeptides					1366:1380	the previously identified N-glycopeptides	1340:1380	the previously identified N-glycopeptides in this important body fluid	1340:1409	We then used the super-SILAC mix in plasma, which led to the quantification of a large number of the previously identified N-glycopeptides in this important body fluid.
23090970	8	64	gly	glycoprotein	1109:1120	arg1	glycoprotein					1109:1120	glycoprotein dynamics	1109:1129	glycoprotein dynamics	1109:1129	Five different profiles of glycoprotein dynamics during cancer development were detected, and they contained several proteins with known roles in breast cancer.
23090970	4	65	theme	breast	644:649	arg1	lines					663:667	several labeled breast cancer cell lines	628:667	several labeled breast cancer cell lines	628:667	For accurate quantification we developed a super-SILAC mix from several labeled breast cancer cell lines and used it as an internal standard for all samples.
23090970	9	66	theme	number	1330:1335	arg1	quantification					1304:1317	the quantification	1300:1317	the quantification of a large number of the previously identified N-glycopeptides in this important body fluid	1300:1409	We then used the super-SILAC mix in plasma, which led to the quantification of a large number of the previously identified N-glycopeptides in this important body fluid.
23090970	4	67	used	used	673:676	arg2	we					592:593	we	592:593	we	592:593	For accurate quantification we developed a super-SILAC mix from several labeled breast cancer cell lines and used it as an internal standard for all samples.
23090970	2	68	theme	non-regulated	330:342	arg1	processes					344:352	regulated or non-regulated processes	317:352	regulated or non-regulated processes	317:352	Furthermore, plasma membrane proteins and intracellular proteins can be released into the extracellular space by regulated or non-regulated processes.
23090970	7	69	theme	different	962:970	arg1	lines					977:981	the different cell lines	958:981	the different cell lines to their respective cancer stage	958:1014	N-glycosylated secretome profiles correctly clustered the different cell lines to their respective cancer stage, suggesting that biologically relevant differences were detected.
23090970	4	70	theme	labeled	636:642	arg1	lines					663:667	several labeled breast cancer cell lines	628:667	several labeled breast cancer cell lines	628:667	For accurate quantification we developed a super-SILAC mix from several labeled breast cancer cell lines and used it as an internal standard for all samples.
23090970	0	71	theme	cancer	76:81	arg1	progression					83:93	breast cancer progression	69:93	breast cancer progression	69:93	Quantification of the N-glycosylated secretome by super-SILAC during breast cancer progression and in human blood samples.
23090970	3	72	theme	N-glyco	539:545	arg1	technology					552:561	the N-glyco FASP technology	535:561	the N-glyco FASP technology	535:561	Here, we profiled the supernatant of 11 cell lines that are representative of different stages of breast cancer development by specifically capturing N-glycosylated peptides using the N-glyco FASP technology.
23090970	7	73	theme	cell	972:975	arg1	lines					977:981	the different cell lines	958:981	the different cell lines to their respective cancer stage	958:1014	N-glycosylated secretome profiles correctly clustered the different cell lines to their respective cancer stage, suggesting that biologically relevant differences were detected.
23090970	4	74	theme	cell	658:661	arg1	lines					663:667	several labeled breast cancer cell lines	628:667	several labeled breast cancer cell lines	628:667	For accurate quantification we developed a super-SILAC mix from several labeled breast cancer cell lines and used it as an internal standard for all samples.
23090970	0	75	theme	breast	69:74	arg1	progression					83:93	breast cancer progression	69:93	breast cancer progression	69:93	Quantification of the N-glycosylated secretome by super-SILAC during breast cancer progression and in human blood samples.
23090970	2	76	theme	intracellular	246:258	arg1	proteins					260:267	intracellular proteins	246:267	intracellular proteins	246:267	Furthermore, plasma membrane proteins and intracellular proteins can be released into the extracellular space by regulated or non-regulated processes.
23090970	7	77	theme	relevant	1046:1053	arg1	differences					1055:1065	biologically relevant differences	1033:1065	biologically relevant differences	1033:1065	N-glycosylated secretome profiles correctly clustered the different cell lines to their respective cancer stage, suggesting that biologically relevant differences were detected.
23090970	3	78	theme	FASP	547:550	arg1	technology					552:561	the N-glyco FASP technology	535:561	the N-glyco FASP technology	535:561	Here, we profiled the supernatant of 11 cell lines that are representative of different stages of breast cancer development by specifically capturing N-glycosylated peptides using the N-glyco FASP technology.
23090970	4	79	theme	cancer	651:656	arg1	lines					663:667	several labeled breast cancer cell lines	628:667	several labeled breast cancer cell lines	628:667	For accurate quantification we developed a super-SILAC mix from several labeled breast cancer cell lines and used it as an internal standard for all samples.
9852066	1	0	link	chromogranin-derived	191:210	arg1	fragments					212:220	chromogranin-derived fragments	191:220	chromogranin-derived fragments	191:220	Because of their water-soluble properties, chromogranins (CGs) and chromogranin-derived fragments are released together with catecholamines from adrenal chromaffin cells during stress situations and can be detected in the blood by radiochemical and enzyme assays.
9852066	1	1	theme	water-soluble	141:153	arg1	properties					155:164	their water-soluble properties	135:164	their water-soluble properties	135:164	Because of their water-soluble properties, chromogranins (CGs) and chromogranin-derived fragments are released together with catecholamines from adrenal chromaffin cells during stress situations and can be detected in the blood by radiochemical and enzyme assays.
9852066	5	2	theme	protein	1158:1164	arg1	core					1146:1149	the core	1142:1149	the core of the protein on Thr163, Thr165, and Thr233	1142:1194	Three O-linked glycosylation sites were located in the core of the protein on Thr163, Thr165, and Thr233, consisting in di-, tri-, and tetrasaccharides.
9852066	4	3	link	CGA-derived	1059:1069	arg1	CGA79-439					1080:1088	the C-terminal CGA-derived fragment CGA79-439	1044:1088	the C-terminal CGA-derived fragment CGA79-439	1044:1088	Using mild proteolysis of peptidic material, high performance liquid chromatography, sequencing, and mass spectrometry analysis, six post-translational modifications were detected along the C-terminal CGA-derived fragment CGA79-439.
9852066	7	4	theme	bovine	1542:1547	arg1	CGA					1549:1551	bovine CGA	1542:1551	bovine CGA	1542:1551	These modified sites were compared with sequences of others species and discussed in relation with the post-translational modifications that we have reported previously for bovine CGA.
9852066	4	5	theme	high	903:906	arg1	chromatography					927:940	high performance liquid chromatography	903:940	high performance liquid chromatography	903:940	Using mild proteolysis of peptidic material, high performance liquid chromatography, sequencing, and mass spectrometry analysis, six post-translational modifications were detected along the C-terminal CGA-derived fragment CGA79-439.
9852066	4	6	theme	liquid	920:925	arg1	chromatography					927:940	high performance liquid chromatography	903:940	high performance liquid chromatography	903:940	Using mild proteolysis of peptidic material, high performance liquid chromatography, sequencing, and mass spectrometry analysis, six post-translational modifications were detected along the C-terminal CGA-derived fragment CGA79-439.
9852066	4	7	theme	mild	864:867	arg1	proteolysis					869:879	mild proteolysis	864:879	mild proteolysis of peptidic material	864:900	Using mild proteolysis of peptidic material, high performance liquid chromatography, sequencing, and mass spectrometry analysis, six post-translational modifications were detected along the C-terminal CGA-derived fragment CGA79-439.
9852066	5	8	located	located	1131:1137	arg1	core					1146:1149	the core	1142:1149	the core of the protein on Thr163, Thr165, and Thr233	1142:1194	Three O-linked glycosylation sites were located in the core of the protein on Thr163, Thr165, and Thr233, consisting in di-, tri-, and tetrasaccharides.
9852066	5	8	located	located	1131:1137	arg2	sites					1120:1124	Three O-linked glycosylation sites	1091:1124	Three O-linked glycosylation sites	1091:1124	Three O-linked glycosylation sites were located in the core of the protein on Thr163, Thr165, and Thr233, consisting in di-, tri-, and tetrasaccharides.
9852066	7	9	theme	others	1422:1427	arg1	species					1429:1435	others species	1422:1435	others species	1422:1435	These modified sites were compared with sequences of others species and discussed in relation with the post-translational modifications that we have reported previously for bovine CGA.
9852066	1	10	theme	adrenal	269:275	arg1	cells					288:292	adrenal chromaffin cells	269:292	adrenal chromaffin cells	269:292	Because of their water-soluble properties, chromogranins (CGs) and chromogranin-derived fragments are released together with catecholamines from adrenal chromaffin cells during stress situations and can be detected in the blood by radiochemical and enzyme assays.
9852066	3	11	theme	post-translational	721:738	arg1	O-glycosylation					775:789	O-glycosylation	775:789	O-glycosylation	775:789	In 1993, large CGA-derived fragments have been shown to be excreted into the urine in patients with carcinoid tumors and the present study deals with the characterization of the post-translational modifications (phosphorylation and O-glycosylation) located along the largest natural CGA-derived fragment CGA79-439.
9852066	3	11	theme	post-translational	721:738	arg1	phosphorylation					755:769	phosphorylation	755:769	phosphorylation	755:769	In 1993, large CGA-derived fragments have been shown to be excreted into the urine in patients with carcinoid tumors and the present study deals with the characterization of the post-translational modifications (phosphorylation and O-glycosylation) located along the largest natural CGA-derived fragment CGA79-439.
9852066	3	11	theme	post-translational	721:738	arg1	modifications					740:752	the post-translational modifications	717:752	the post-translational modifications (phosphorylation and O-glycosylation) located along the largest natural CGA-derived fragment CGA79-439	717:855	In 1993, large CGA-derived fragments have been shown to be excreted into the urine in patients with carcinoid tumors and the present study deals with the characterization of the post-translational modifications (phosphorylation and O-glycosylation) located along the largest natural CGA-derived fragment CGA79-439.
9852066	4	12	theme	performance	908:918	arg1	chromatography					927:940	high performance liquid chromatography	903:940	high performance liquid chromatography	903:940	Using mild proteolysis of peptidic material, high performance liquid chromatography, sequencing, and mass spectrometry analysis, six post-translational modifications were detected along the C-terminal CGA-derived fragment CGA79-439.
9852066	3	13	theme	large	552:556	arg1	fragments					570:578	large CGA-derived fragments	552:578	large CGA-derived fragments	552:578	In 1993, large CGA-derived fragments have been shown to be excreted into the urine in patients with carcinoid tumors and the present study deals with the characterization of the post-translational modifications (phosphorylation and O-glycosylation) located along the largest natural CGA-derived fragment CGA79-439.
9852066	1	14	theme	chromaffin	277:286	arg1	cells					288:292	adrenal chromaffin cells	269:292	adrenal chromaffin cells	269:292	Because of their water-soluble properties, chromogranins (CGs) and chromogranin-derived fragments are released together with catecholamines from adrenal chromaffin cells during stress situations and can be detected in the blood by radiochemical and enzyme assays.
9852066	2	15	theme	neuroendocrine	520:533	arg1	tumors					535:540	neuroendocrine tumors	520:540	neuroendocrine tumors	520:540	It is well known that chromogranins can serve as immunocytochemical markers for neuroendocrine tissues and as a diagnostic tool for neuroendocrine tumors.
9852066	3	16	theme	modifications	740:752	arg1	characterization					697:712	the characterization	693:712	the characterization of the post-translational modifications (phosphorylation and O-glycosylation) located along the largest natural CGA-derived fragment CGA79-439	693:855	In 1993, large CGA-derived fragments have been shown to be excreted into the urine in patients with carcinoid tumors and the present study deals with the characterization of the post-translational modifications (phosphorylation and O-glycosylation) located along the largest natural CGA-derived fragment CGA79-439.
9852066	6	17	theme	C-terminal	1303:1312	arg1	domain					1314:1319	the middle and C-terminal domain	1288:1319	the middle and C-terminal domain	1288:1319	Three phosphorylation sites were located in the middle and C-terminal domain, on serine residues Ser200, Ser252, and Ser315.
9852066	0	18	theme	patients	92:99	arg1	urine					83:87	urine	83:87	urine of patients with carcinoid tumors	83:121	Phosphorylation and O-glycosylation sites of human chromogranin A (CGA79-439) from urine of patients with carcinoid tumors.
9852066	1	19	theme	enzyme	373:378	arg1	assays					380:385	enzyme assays	373:385	enzyme assays	373:385	Because of their water-soluble properties, chromogranins (CGs) and chromogranin-derived fragments are released together with catecholamines from adrenal chromaffin cells during stress situations and can be detected in the blood by radiochemical and enzyme assays.
9852066	4	20	theme	CGA-derived	1059:1069	arg1	CGA79-439					1080:1088	the C-terminal CGA-derived fragment CGA79-439	1044:1088	the C-terminal CGA-derived fragment CGA79-439	1044:1088	Using mild proteolysis of peptidic material, high performance liquid chromatography, sequencing, and mass spectrometry analysis, six post-translational modifications were detected along the C-terminal CGA-derived fragment CGA79-439.
9852066	0	21	theme	Phosphorylation	0:14	arg1	sites					36:40	Phosphorylation and O-glycosylation sites	0:40	sites	36:40	Phosphorylation and O-glycosylation sites of human chromogranin A (CGA79-439) from urine of patients with carcinoid tumors.
9852066	0	21	theme	Phosphorylation	0:14	arg1	A					64:64	human chromogranin A	45:64	human chromogranin A (CGA79-439) from urine of patients with carcinoid tumors	45:121	Phosphorylation and O-glycosylation sites of human chromogranin A (CGA79-439) from urine of patients with carcinoid tumors.
9852066	5	22	from	Thr163	1169:1174	arg1	core					1146:1149	the core	1142:1149	the core of the protein on Thr163, Thr165, and Thr233	1142:1194	Three O-linked glycosylation sites were located in the core of the protein on Thr163, Thr165, and Thr233, consisting in di-, tri-, and tetrasaccharides.
9852066	1	23	from	cells	288:292	arg1	catecholamines					249:262	catecholamines	249:262	catecholamines from adrenal chromaffin cells	249:292	Because of their water-soluble properties, chromogranins (CGs) and chromogranin-derived fragments are released together with catecholamines from adrenal chromaffin cells during stress situations and can be detected in the blood by radiochemical and enzyme assays.
9852066	0	24	with	patients	92:99	arg1	tumors					116:121	carcinoid tumors	106:121	carcinoid tumors	106:121	Phosphorylation and O-glycosylation sites of human chromogranin A (CGA79-439) from urine of patients with carcinoid tumors.
9852066	2	25	theme	immunocytochemical	437:454	arg1	markers					456:462	immunocytochemical markers	437:462	immunocytochemical markers for neuroendocrine tissues and as a diagnostic tool for neuroendocrine tumors	437:540	It is well known that chromogranins can serve as immunocytochemical markers for neuroendocrine tissues and as a diagnostic tool for neuroendocrine tumors.
9852066	2	25	theme	immunocytochemical	437:454	arg1	chromogranins					410:422	chromogranins	410:422	chromogranins	410:422	It is well known that chromogranins can serve as immunocytochemical markers for neuroendocrine tissues and as a diagnostic tool for neuroendocrine tumors.
9852066	4	26	theme	peptidic	884:891	arg1	material					893:900	peptidic material	884:900	peptidic material	884:900	Using mild proteolysis of peptidic material, high performance liquid chromatography, sequencing, and mass spectrometry analysis, six post-translational modifications were detected along the C-terminal CGA-derived fragment CGA79-439.
9852066	3	27	link	CGA-derived	826:836	arg1	CGA79-439					847:855	the largest natural CGA-derived fragment CGA79-439	806:855	the largest natural CGA-derived fragment CGA79-439	806:855	In 1993, large CGA-derived fragments have been shown to be excreted into the urine in patients with carcinoid tumors and the present study deals with the characterization of the post-translational modifications (phosphorylation and O-glycosylation) located along the largest natural CGA-derived fragment CGA79-439.
9852066	3	28	with	patients	629:636	arg1	tumors					653:658	carcinoid tumors	643:658	carcinoid tumors	643:658	In 1993, large CGA-derived fragments have been shown to be excreted into the urine in patients with carcinoid tumors and the present study deals with the characterization of the post-translational modifications (phosphorylation and O-glycosylation) located along the largest natural CGA-derived fragment CGA79-439.
9852066	3	28	with	patients	629:636	arg1	characterization					697:712	the characterization	693:712	the characterization of the post-translational modifications (phosphorylation and O-glycosylation) located along the largest natural CGA-derived fragment CGA79-439	693:855	In 1993, large CGA-derived fragments have been shown to be excreted into the urine in patients with carcinoid tumors and the present study deals with the characterization of the post-translational modifications (phosphorylation and O-glycosylation) located along the largest natural CGA-derived fragment CGA79-439.
9852066	5	29	gly	glycosylation	1106:1118	arg2	sites					1120:1124	Three O-linked glycosylation sites	1091:1124	Three O-linked glycosylation sites	1091:1124	Three O-linked glycosylation sites were located in the core of the protein on Thr163, Thr165, and Thr233, consisting in di-, tri-, and tetrasaccharides.
9852066	5	29	gly	glycosylation	1106:1118	arg2	Three					1091:1095	Three	1091:1095	Three	1091:1095	Three O-linked glycosylation sites were located in the core of the protein on Thr163, Thr165, and Thr233, consisting in di-, tri-, and tetrasaccharides.
9852066	4	30	theme	mass	959:962	arg1	analysis					977:984	mass spectrometry analysis	959:984	mass spectrometry analysis	959:984	Using mild proteolysis of peptidic material, high performance liquid chromatography, sequencing, and mass spectrometry analysis, six post-translational modifications were detected along the C-terminal CGA-derived fragment CGA79-439.
9852066	1	31	located	detected	330:337	arg1	blood					346:350	the blood	342:350	the blood	342:350	Because of their water-soluble properties, chromogranins (CGs) and chromogranin-derived fragments are released together with catecholamines from adrenal chromaffin cells during stress situations and can be detected in the blood by radiochemical and enzyme assays.
9852066	1	31	located	detected	330:337	arg2	CGs					182:184	CGs	182:184	CGs	182:184	Because of their water-soluble properties, chromogranins (CGs) and chromogranin-derived fragments are released together with catecholamines from adrenal chromaffin cells during stress situations and can be detected in the blood by radiochemical and enzyme assays.
9852066	1	31	located	detected	330:337	arg2	chromogranins					167:179	chromogranins	167:179	chromogranins (CGs)	167:185	Because of their water-soluble properties, chromogranins (CGs) and chromogranin-derived fragments are released together with catecholamines from adrenal chromaffin cells during stress situations and can be detected in the blood by radiochemical and enzyme assays.
9852066	6	32	dep	residues	1332:1339	arg1	residues					1332:1339	serine residues Ser200, Ser252, and Ser315	1325:1366	serine residues Ser200, Ser252, and Ser315	1325:1366	Three phosphorylation sites were located in the middle and C-terminal domain, on serine residues Ser200, Ser252, and Ser315.
9852066	6	32	dep	residues	1332:1339	arg1	Ser252					1349:1354	Ser252	1349:1354	Ser252	1349:1354	Three phosphorylation sites were located in the middle and C-terminal domain, on serine residues Ser200, Ser252, and Ser315.
9852066	6	32	dep	residues	1332:1339	arg1	Ser315					1361:1366	Ser315	1361:1366	Ser315	1361:1366	Three phosphorylation sites were located in the middle and C-terminal domain, on serine residues Ser200, Ser252, and Ser315.
9852066	6	32	dep	residues	1332:1339	arg1	Ser200					1341:1346	Ser200	1341:1346	Ser200	1341:1346	Three phosphorylation sites were located in the middle and C-terminal domain, on serine residues Ser200, Ser252, and Ser315.
9852066	0	33	theme	O-glycosylation	20:34	arg1	sites					36:40	Phosphorylation and O-glycosylation sites	0:40	sites	36:40	Phosphorylation and O-glycosylation sites of human chromogranin A (CGA79-439) from urine of patients with carcinoid tumors.
9852066	0	33	theme	O-glycosylation	20:34	arg1	A					64:64	human chromogranin A	45:64	human chromogranin A (CGA79-439) from urine of patients with carcinoid tumors	45:121	Phosphorylation and O-glycosylation sites of human chromogranin A (CGA79-439) from urine of patients with carcinoid tumors.
9852066	1	34	theme	stress	301:306	arg1	situations					308:317	stress situations	301:317	stress situations	301:317	Because of their water-soluble properties, chromogranins (CGs) and chromogranin-derived fragments are released together with catecholamines from adrenal chromaffin cells during stress situations and can be detected in the blood by radiochemical and enzyme assays.
9852066	0	35	theme	carcinoid	106:114	arg1	tumors					116:121	carcinoid tumors	106:121	carcinoid tumors	106:121	Phosphorylation and O-glycosylation sites of human chromogranin A (CGA79-439) from urine of patients with carcinoid tumors.
9852066	3	36	theme	carcinoid	643:651	arg1	tumors					653:658	carcinoid tumors	643:658	carcinoid tumors	643:658	In 1993, large CGA-derived fragments have been shown to be excreted into the urine in patients with carcinoid tumors and the present study deals with the characterization of the post-translational modifications (phosphorylation and O-glycosylation) located along the largest natural CGA-derived fragment CGA79-439.
9852066	6	37	from	domain	1314:1319	arg1	located					1277:1283	located	1277:1283	located	1277:1283	Three phosphorylation sites were located in the middle and C-terminal domain, on serine residues Ser200, Ser252, and Ser315.
9852066	5	38	theme	O-linked	1097:1104	arg1	sites					1120:1124	Three O-linked glycosylation sites	1091:1124	Three O-linked glycosylation sites	1091:1124	Three O-linked glycosylation sites were located in the core of the protein on Thr163, Thr165, and Thr233, consisting in di-, tri-, and tetrasaccharides.
9852066	0	39	theme	human	45:49	arg1	CGA79-439					67:75	CGA79-439	67:75	CGA79-439	67:75	Phosphorylation and O-glycosylation sites of human chromogranin A (CGA79-439) from urine of patients with carcinoid tumors.
9852066	0	39	theme	human	45:49	arg1	A					64:64	human chromogranin A	45:64	human chromogranin A (CGA79-439) from urine of patients with carcinoid tumors	45:121	Phosphorylation and O-glycosylation sites of human chromogranin A (CGA79-439) from urine of patients with carcinoid tumors.
9852066	5	40	from	Thr165	1177:1182	arg1	core					1146:1149	the core	1142:1149	the core of the protein on Thr163, Thr165, and Thr233	1142:1194	Three O-linked glycosylation sites were located in the core of the protein on Thr163, Thr165, and Thr233, consisting in di-, tri-, and tetrasaccharides.
9852066	6	41	theme	serine	1325:1330	arg1	residues					1332:1339	serine residues Ser200, Ser252, and Ser315	1325:1366	serine residues Ser200, Ser252, and Ser315	1325:1366	Three phosphorylation sites were located in the middle and C-terminal domain, on serine residues Ser200, Ser252, and Ser315.
9852066	6	41	theme	serine	1325:1330	arg1	Ser252					1349:1354	Ser252	1349:1354	Ser252	1349:1354	Three phosphorylation sites were located in the middle and C-terminal domain, on serine residues Ser200, Ser252, and Ser315.
9852066	6	41	theme	serine	1325:1330	arg1	Ser315					1361:1366	Ser315	1361:1366	Ser315	1361:1366	Three phosphorylation sites were located in the middle and C-terminal domain, on serine residues Ser200, Ser252, and Ser315.
9852066	6	41	theme	serine	1325:1330	arg1	Ser200					1341:1346	Ser200	1341:1346	Ser200	1341:1346	Three phosphorylation sites were located in the middle and C-terminal domain, on serine residues Ser200, Ser252, and Ser315.
9852066	1	42	theme	chromogranin-derived	191:210	arg1	fragments					212:220	chromogranin-derived fragments	191:220	chromogranin-derived fragments	191:220	Because of their water-soluble properties, chromogranins (CGs) and chromogranin-derived fragments are released together with catecholamines from adrenal chromaffin cells during stress situations and can be detected in the blood by radiochemical and enzyme assays.
9852066	4	43	theme	C-terminal	1048:1057	arg1	CGA79-439					1080:1088	the C-terminal CGA-derived fragment CGA79-439	1044:1088	the C-terminal CGA-derived fragment CGA79-439	1044:1088	Using mild proteolysis of peptidic material, high performance liquid chromatography, sequencing, and mass spectrometry analysis, six post-translational modifications were detected along the C-terminal CGA-derived fragment CGA79-439.
9852066	4	44	theme	fragment	1071:1078	arg1	CGA79-439					1080:1088	the C-terminal CGA-derived fragment CGA79-439	1044:1088	the C-terminal CGA-derived fragment CGA79-439	1044:1088	Using mild proteolysis of peptidic material, high performance liquid chromatography, sequencing, and mass spectrometry analysis, six post-translational modifications were detected along the C-terminal CGA-derived fragment CGA79-439.
9852066	4	45	theme	spectrometry	964:975	arg1	analysis					977:984	mass spectrometry analysis	959:984	mass spectrometry analysis	959:984	Using mild proteolysis of peptidic material, high performance liquid chromatography, sequencing, and mass spectrometry analysis, six post-translational modifications were detected along the C-terminal CGA-derived fragment CGA79-439.
9852066	5	46	from	protein	1158:1164	arg1	Thr163					1169:1174	Thr163	1169:1174	Thr163	1169:1174	Three O-linked glycosylation sites were located in the core of the protein on Thr163, Thr165, and Thr233, consisting in di-, tri-, and tetrasaccharides.
9852066	5	46	from	protein	1158:1164	arg1	Thr165					1177:1182	Thr165	1177:1182	Thr165	1177:1182	Three O-linked glycosylation sites were located in the core of the protein on Thr163, Thr165, and Thr233, consisting in di-, tri-, and tetrasaccharides.
9852066	5	46	from	protein	1158:1164	arg1	Thr233					1189:1194	Thr233	1189:1194	Thr233	1189:1194	Three O-linked glycosylation sites were located in the core of the protein on Thr163, Thr165, and Thr233, consisting in di-, tri-, and tetrasaccharides.
9852066	5	47	from	core	1146:1149	arg1	Thr163					1169:1174	Thr163	1169:1174	Thr163	1169:1174	Three O-linked glycosylation sites were located in the core of the protein on Thr163, Thr165, and Thr233, consisting in di-, tri-, and tetrasaccharides.
9852066	5	47	from	core	1146:1149	arg1	located					1131:1137	located	1131:1137	located	1131:1137	Three O-linked glycosylation sites were located in the core of the protein on Thr163, Thr165, and Thr233, consisting in di-, tri-, and tetrasaccharides.
9852066	5	47	from	core	1146:1149	arg1	Thr165					1177:1182	Thr165	1177:1182	Thr165	1177:1182	Three O-linked glycosylation sites were located in the core of the protein on Thr163, Thr165, and Thr233, consisting in di-, tri-, and tetrasaccharides.
9852066	5	47	from	core	1146:1149	arg1	Thr233					1189:1194	Thr233	1189:1194	Thr233	1189:1194	Three O-linked glycosylation sites were located in the core of the protein on Thr163, Thr165, and Thr233, consisting in di-, tri-, and tetrasaccharides.
9852066	3	48	dep	modifications	740:752	arg1	O-glycosylation					775:789	O-glycosylation	775:789	O-glycosylation	775:789	In 1993, large CGA-derived fragments have been shown to be excreted into the urine in patients with carcinoid tumors and the present study deals with the characterization of the post-translational modifications (phosphorylation and O-glycosylation) located along the largest natural CGA-derived fragment CGA79-439.
9852066	3	48	dep	modifications	740:752	arg1	phosphorylation					755:769	phosphorylation	755:769	phosphorylation	755:769	In 1993, large CGA-derived fragments have been shown to be excreted into the urine in patients with carcinoid tumors and the present study deals with the characterization of the post-translational modifications (phosphorylation and O-glycosylation) located along the largest natural CGA-derived fragment CGA79-439.
9852066	3	48	dep	modifications	740:752	arg1	modifications					740:752	the post-translational modifications	717:752	the post-translational modifications (phosphorylation and O-glycosylation) located along the largest natural CGA-derived fragment CGA79-439	717:855	In 1993, large CGA-derived fragments have been shown to be excreted into the urine in patients with carcinoid tumors and the present study deals with the characterization of the post-translational modifications (phosphorylation and O-glycosylation) located along the largest natural CGA-derived fragment CGA79-439.
9852066	0	49	theme	A	64:64	arg1	sites					36:40	Phosphorylation and O-glycosylation sites	0:40	sites	36:40	Phosphorylation and O-glycosylation sites of human chromogranin A (CGA79-439) from urine of patients with carcinoid tumors.
9852066	0	49	theme	A	64:64	arg1	A					64:64	human chromogranin A	45:64	human chromogranin A (CGA79-439) from urine of patients with carcinoid tumors	45:121	Phosphorylation and O-glycosylation sites of human chromogranin A (CGA79-439) from urine of patients with carcinoid tumors.
9852066	6	50	located	located	1277:1283	arg1	Ser315					1361:1366	Ser315	1361:1366	Ser315	1361:1366	Three phosphorylation sites were located in the middle and C-terminal domain, on serine residues Ser200, Ser252, and Ser315.
9852066	6	50	located	located	1277:1283	arg1	residues					1332:1339	serine residues Ser200, Ser252, and Ser315	1325:1366	serine residues Ser200, Ser252, and Ser315	1325:1366	Three phosphorylation sites were located in the middle and C-terminal domain, on serine residues Ser200, Ser252, and Ser315.
9852066	6	50	located	located	1277:1283	arg1	Ser200					1341:1346	Ser200	1341:1346	Ser200	1341:1346	Three phosphorylation sites were located in the middle and C-terminal domain, on serine residues Ser200, Ser252, and Ser315.
9852066	6	50	located	located	1277:1283	arg1	Ser252					1349:1354	Ser252	1349:1354	Ser252	1349:1354	Three phosphorylation sites were located in the middle and C-terminal domain, on serine residues Ser200, Ser252, and Ser315.
9852066	6	50	located	located	1277:1283	arg1	domain					1314:1319	the middle and C-terminal domain	1288:1319	the middle and C-terminal domain	1288:1319	Three phosphorylation sites were located in the middle and C-terminal domain, on serine residues Ser200, Ser252, and Ser315.
9852066	6	50	located	located	1277:1283	arg2	sites					1266:1270	Three phosphorylation sites	1244:1270	Three phosphorylation sites	1244:1270	Three phosphorylation sites were located in the middle and C-terminal domain, on serine residues Ser200, Ser252, and Ser315.
9852066	2	51	theme	diagnostic	500:509	arg1	tool					511:514	a diagnostic tool	498:514	a diagnostic tool for neuroendocrine tumors	498:540	It is well known that chromogranins can serve as immunocytochemical markers for neuroendocrine tissues and as a diagnostic tool for neuroendocrine tumors.
9852066	0	52	gly	O-glycosylation	20:34	arg2	A					64:64	human chromogranin A	45:64	human chromogranin A (CGA79-439) from urine of patients with carcinoid tumors	45:121	Phosphorylation and O-glycosylation sites of human chromogranin A (CGA79-439) from urine of patients with carcinoid tumors.
9852066	0	52	gly	O-glycosylation	20:34	arg1	CGA79-439					67:75	CGA79-439	67:75	CGA79-439	67:75	Phosphorylation and O-glycosylation sites of human chromogranin A (CGA79-439) from urine of patients with carcinoid tumors.
9852066	0	52	gly	O-glycosylation	20:34	arg2	sites					36:40	Phosphorylation and O-glycosylation sites	0:40	sites	36:40	Phosphorylation and O-glycosylation sites of human chromogranin A (CGA79-439) from urine of patients with carcinoid tumors.
9852066	0	52	gly	O-glycosylation	20:34	arg2	urine					83:87	urine	83:87	urine of patients with carcinoid tumors	83:121	Phosphorylation and O-glycosylation sites of human chromogranin A (CGA79-439) from urine of patients with carcinoid tumors.
9852066	0	52	gly	O-glycosylation	20:34	arg1	A					64:64	human chromogranin A	45:64	human chromogranin A (CGA79-439) from urine of patients with carcinoid tumors	45:121	Phosphorylation and O-glycosylation sites of human chromogranin A (CGA79-439) from urine of patients with carcinoid tumors.
9852066	7	53	theme	post-translational	1472:1489	arg1	modifications					1491:1503	the post-translational modifications	1468:1503	the post-translational modifications that we have reported previously for bovine CGA	1468:1551	These modified sites were compared with sequences of others species and discussed in relation with the post-translational modifications that we have reported previously for bovine CGA.
9852066	0	54	theme	chromogranin	51:62	arg1	CGA79-439					67:75	CGA79-439	67:75	CGA79-439	67:75	Phosphorylation and O-glycosylation sites of human chromogranin A (CGA79-439) from urine of patients with carcinoid tumors.
9852066	0	54	theme	chromogranin	51:62	arg1	A					64:64	human chromogranin A	45:64	human chromogranin A (CGA79-439) from urine of patients with carcinoid tumors	45:121	Phosphorylation and O-glycosylation sites of human chromogranin A (CGA79-439) from urine of patients with carcinoid tumors.
9852066	5	55	link	O-linked	1097:1104	arg1	sites					1120:1124	Three O-linked glycosylation sites	1091:1124	Three O-linked glycosylation sites	1091:1124	Three O-linked glycosylation sites were located in the core of the protein on Thr163, Thr165, and Thr233, consisting in di-, tri-, and tetrasaccharides.
9852066	3	56	theme	present	668:674	arg1	deals					682:686	the present study deals	664:686	the present study deals with the characterization of the post-translational modifications (phosphorylation and O-glycosylation) located along the largest natural CGA-derived fragment CGA79-439	664:855	In 1993, large CGA-derived fragments have been shown to be excreted into the urine in patients with carcinoid tumors and the present study deals with the characterization of the post-translational modifications (phosphorylation and O-glycosylation) located along the largest natural CGA-derived fragment CGA79-439.
9852066	5	57	theme	glycosylation	1106:1118	arg1	sites					1120:1124	Three O-linked glycosylation sites	1091:1124	Three O-linked glycosylation sites	1091:1124	Three O-linked glycosylation sites were located in the core of the protein on Thr163, Thr165, and Thr233, consisting in di-, tri-, and tetrasaccharides.
9852066	5	58	from	Thr233	1189:1194	arg1	core					1146:1149	the core	1142:1149	the core of the protein on Thr163, Thr165, and Thr233	1142:1194	Three O-linked glycosylation sites were located in the core of the protein on Thr163, Thr165, and Thr233, consisting in di-, tri-, and tetrasaccharides.
9852066	3	59	theme	located	792:798	arg1	O-glycosylation					775:789	O-glycosylation	775:789	O-glycosylation	775:789	In 1993, large CGA-derived fragments have been shown to be excreted into the urine in patients with carcinoid tumors and the present study deals with the characterization of the post-translational modifications (phosphorylation and O-glycosylation) located along the largest natural CGA-derived fragment CGA79-439.
9852066	3	59	theme	located	792:798	arg1	phosphorylation					755:769	phosphorylation	755:769	phosphorylation	755:769	In 1993, large CGA-derived fragments have been shown to be excreted into the urine in patients with carcinoid tumors and the present study deals with the characterization of the post-translational modifications (phosphorylation and O-glycosylation) located along the largest natural CGA-derived fragment CGA79-439.
9852066	3	59	theme	located	792:798	arg1	modifications					740:752	the post-translational modifications	717:752	the post-translational modifications (phosphorylation and O-glycosylation) located along the largest natural CGA-derived fragment CGA79-439	717:855	In 1993, large CGA-derived fragments have been shown to be excreted into the urine in patients with carcinoid tumors and the present study deals with the characterization of the post-translational modifications (phosphorylation and O-glycosylation) located along the largest natural CGA-derived fragment CGA79-439.
9852066	3	60	theme	study	676:680	arg1	deals					682:686	the present study deals	664:686	the present study deals with the characterization of the post-translational modifications (phosphorylation and O-glycosylation) located along the largest natural CGA-derived fragment CGA79-439	664:855	In 1993, large CGA-derived fragments have been shown to be excreted into the urine in patients with carcinoid tumors and the present study deals with the characterization of the post-translational modifications (phosphorylation and O-glycosylation) located along the largest natural CGA-derived fragment CGA79-439.
9852066	6	61	theme	phosphorylation	1250:1264	arg1	sites					1266:1270	Three phosphorylation sites	1244:1270	Three phosphorylation sites	1244:1270	Three phosphorylation sites were located in the middle and C-terminal domain, on serine residues Ser200, Ser252, and Ser315.
9852066	6	62	theme	middle	1292:1297	arg1	domain					1314:1319	the middle and C-terminal domain	1288:1319	the middle and C-terminal domain	1288:1319	Three phosphorylation sites were located in the middle and C-terminal domain, on serine residues Ser200, Ser252, and Ser315.
9852066	7	63	with	relation	1454:1461	arg1	modifications					1491:1503	the post-translational modifications	1468:1503	the post-translational modifications that we have reported previously for bovine CGA	1468:1551	These modified sites were compared with sequences of others species and discussed in relation with the post-translational modifications that we have reported previously for bovine CGA.
9852066	3	64	theme	CGA-derived	558:568	arg1	fragments					570:578	large CGA-derived fragments	552:578	large CGA-derived fragments	552:578	In 1993, large CGA-derived fragments have been shown to be excreted into the urine in patients with carcinoid tumors and the present study deals with the characterization of the post-translational modifications (phosphorylation and O-glycosylation) located along the largest natural CGA-derived fragment CGA79-439.
9852066	3	65	theme	CGA-derived	826:836	arg1	CGA79-439					847:855	the largest natural CGA-derived fragment CGA79-439	806:855	the largest natural CGA-derived fragment CGA79-439	806:855	In 1993, large CGA-derived fragments have been shown to be excreted into the urine in patients with carcinoid tumors and the present study deals with the characterization of the post-translational modifications (phosphorylation and O-glycosylation) located along the largest natural CGA-derived fragment CGA79-439.
9852066	4	66	theme	material	893:900	arg1	sequencing					943:952	sequencing	943:952	sequencing	943:952	Using mild proteolysis of peptidic material, high performance liquid chromatography, sequencing, and mass spectrometry analysis, six post-translational modifications were detected along the C-terminal CGA-derived fragment CGA79-439.
9852066	4	66	theme	material	893:900	arg1	proteolysis					869:879	mild proteolysis	864:879	mild proteolysis of peptidic material	864:900	Using mild proteolysis of peptidic material, high performance liquid chromatography, sequencing, and mass spectrometry analysis, six post-translational modifications were detected along the C-terminal CGA-derived fragment CGA79-439.
9852066	4	66	theme	material	893:900	arg1	chromatography					927:940	high performance liquid chromatography	903:940	high performance liquid chromatography	903:940	Using mild proteolysis of peptidic material, high performance liquid chromatography, sequencing, and mass spectrometry analysis, six post-translational modifications were detected along the C-terminal CGA-derived fragment CGA79-439.
9852066	4	66	theme	material	893:900	arg1	analysis					977:984	mass spectrometry analysis	959:984	mass spectrometry analysis	959:984	Using mild proteolysis of peptidic material, high performance liquid chromatography, sequencing, and mass spectrometry analysis, six post-translational modifications were detected along the C-terminal CGA-derived fragment CGA79-439.
9852066	5	67	from	located	1131:1137	arg1	core					1146:1149	the core	1142:1149	the core of the protein on Thr163, Thr165, and Thr233	1142:1194	Three O-linked glycosylation sites were located in the core of the protein on Thr163, Thr165, and Thr233, consisting in di-, tri-, and tetrasaccharides.
9852066	7	68	theme	species	1429:1435	arg1	sequences					1409:1417	sequences	1409:1417	sequences of others species	1409:1435	These modified sites were compared with sequences of others species and discussed in relation with the post-translational modifications that we have reported previously for bovine CGA.
9852066	3	69	theme	fragment	838:845	arg1	CGA79-439					847:855	the largest natural CGA-derived fragment CGA79-439	806:855	the largest natural CGA-derived fragment CGA79-439	806:855	In 1993, large CGA-derived fragments have been shown to be excreted into the urine in patients with carcinoid tumors and the present study deals with the characterization of the post-translational modifications (phosphorylation and O-glycosylation) located along the largest natural CGA-derived fragment CGA79-439.
9852066	3	70	link	CGA-derived	558:568	arg1	fragments					570:578	large CGA-derived fragments	552:578	large CGA-derived fragments	552:578	In 1993, large CGA-derived fragments have been shown to be excreted into the urine in patients with carcinoid tumors and the present study deals with the characterization of the post-translational modifications (phosphorylation and O-glycosylation) located along the largest natural CGA-derived fragment CGA79-439.
9852066	0	71	from	urine	83:87	arg1	sites					36:40	Phosphorylation and O-glycosylation sites	0:40	sites	36:40	Phosphorylation and O-glycosylation sites of human chromogranin A (CGA79-439) from urine of patients with carcinoid tumors.
9852066	0	71	from	urine	83:87	arg1	CGA79-439					67:75	CGA79-439	67:75	CGA79-439	67:75	Phosphorylation and O-glycosylation sites of human chromogranin A (CGA79-439) from urine of patients with carcinoid tumors.
9852066	0	71	from	urine	83:87	arg1	A					64:64	human chromogranin A	45:64	human chromogranin A (CGA79-439) from urine of patients with carcinoid tumors	45:121	Phosphorylation and O-glycosylation sites of human chromogranin A (CGA79-439) from urine of patients with carcinoid tumors.
9852066	6	72	from	located	1277:1283	arg1	domain					1314:1319	the middle and C-terminal domain	1288:1319	the middle and C-terminal domain	1288:1319	Three phosphorylation sites were located in the middle and C-terminal domain, on serine residues Ser200, Ser252, and Ser315.
9852066	3	73	theme	largest	810:816	arg1	CGA79-439					847:855	the largest natural CGA-derived fragment CGA79-439	806:855	the largest natural CGA-derived fragment CGA79-439	806:855	In 1993, large CGA-derived fragments have been shown to be excreted into the urine in patients with carcinoid tumors and the present study deals with the characterization of the post-translational modifications (phosphorylation and O-glycosylation) located along the largest natural CGA-derived fragment CGA79-439.
9852066	2	74	theme	neuroendocrine	468:481	arg1	tissues					483:489	neuroendocrine tissues	468:489	neuroendocrine tissues	468:489	It is well known that chromogranins can serve as immunocytochemical markers for neuroendocrine tissues and as a diagnostic tool for neuroendocrine tumors.
9852066	0	75	from	sites	36:40	arg1	urine					83:87	urine	83:87	urine of patients with carcinoid tumors	83:121	Phosphorylation and O-glycosylation sites of human chromogranin A (CGA79-439) from urine of patients with carcinoid tumors.
9852066	7	76	theme	modified	1375:1382	arg1	sites					1384:1388	These modified sites	1369:1388	These modified sites	1369:1388	These modified sites were compared with sequences of others species and discussed in relation with the post-translational modifications that we have reported previously for bovine CGA.
9852066	4	77	theme	post-translational	991:1008	arg1	modifications					1010:1022	six post-translational modifications	987:1022	six post-translational modifications	987:1022	Using mild proteolysis of peptidic material, high performance liquid chromatography, sequencing, and mass spectrometry analysis, six post-translational modifications were detected along the C-terminal CGA-derived fragment CGA79-439.
9852066	3	78	with	deals	682:686	arg1	tumors					653:658	carcinoid tumors	643:658	carcinoid tumors	643:658	In 1993, large CGA-derived fragments have been shown to be excreted into the urine in patients with carcinoid tumors and the present study deals with the characterization of the post-translational modifications (phosphorylation and O-glycosylation) located along the largest natural CGA-derived fragment CGA79-439.
9852066	3	78	with	deals	682:686	arg1	characterization					697:712	the characterization	693:712	the characterization of the post-translational modifications (phosphorylation and O-glycosylation) located along the largest natural CGA-derived fragment CGA79-439	693:855	In 1993, large CGA-derived fragments have been shown to be excreted into the urine in patients with carcinoid tumors and the present study deals with the characterization of the post-translational modifications (phosphorylation and O-glycosylation) located along the largest natural CGA-derived fragment CGA79-439.
9852066	3	79	theme	natural	818:824	arg1	CGA79-439					847:855	the largest natural CGA-derived fragment CGA79-439	806:855	the largest natural CGA-derived fragment CGA79-439	806:855	In 1993, large CGA-derived fragments have been shown to be excreted into the urine in patients with carcinoid tumors and the present study deals with the characterization of the post-translational modifications (phosphorylation and O-glycosylation) located along the largest natural CGA-derived fragment CGA79-439.
12624624	7	0	theme	important	1129:1137	arg1	mutation					1114:1121	the R2-linked Asp2194Gly mutation	1089:1121	the R2-linked Asp2194Gly mutation	1089:1121	Therefore, we propose that the R2-linked Asp2194Gly mutation is an important determinant of the association of the R2-FV allele with lower FV levels.
12624624	7	0	theme	important	1129:1137	arg1	determinant					1139:1149	an important determinant	1126:1149	an important determinant of the association of the R2-FV allele with lower FV levels	1126:1209	Therefore, we propose that the R2-linked Asp2194Gly mutation is an important determinant of the association of the R2-FV allele with lower FV levels.
12624624	9	1	theme	charged	1697:1703	arg1	phospholipids					1705:1717	negatively charged phospholipids	1686:1717	negatively charged phospholipids	1686:1717	Finally, the apparent K(d) for dissociation of the FXaVa complex (K(1/2Xa)) was not higher in rFV mutants with the Asp2194Gly mutation than for rFVwt, suggesting that also the affinity for negatively charged phospholipids is not affected by substitution of Asp into Gly at position at 2194.
12624624	1	2	theme	gene	208:211	arg1	haplotype					188:196	The R2 haplotype	181:196	The R2 haplotype of the FV gene	181:211	The R2 haplotype of the FV gene spans from exon 8 through 25 and comprises several strongly linked polymorphisms in the FV gene, including some missense mutations.
12624624	7	3	link	R2-linked	1093:1101	arg1	mutation					1114:1121	the R2-linked Asp2194Gly mutation	1089:1121	the R2-linked Asp2194Gly mutation	1089:1121	Therefore, we propose that the R2-linked Asp2194Gly mutation is an important determinant of the association of the R2-FV allele with lower FV levels.
12624624	7	3	link	R2-linked	1093:1101	arg1	determinant					1139:1149	an important determinant	1126:1149	an important determinant of the association of the R2-FV allele with lower FV levels	1126:1209	Therefore, we propose that the R2-linked Asp2194Gly mutation is an important determinant of the association of the R2-FV allele with lower FV levels.
12624624	8	4	from	glycine	1471:1477	arg1	position					1482:1489	position 2194	1482:1494	position 2194	1482:1494	Furthermore, the light chains from Asp2194Gly containing rFV mutants showed similar molecular weights as the light chains of the non-glycosylated rFVwt or the plasma FV2 isoform, indicating that glycosylation at Asn2181 is not stimulated by the presence of a glycine in position 2194.
12624624	8	5	from	presence	1457:1464	arg1	position					1482:1489	position 2194	1482:1494	position 2194	1482:1494	Furthermore, the light chains from Asp2194Gly containing rFV mutants showed similar molecular weights as the light chains of the non-glycosylated rFVwt or the plasma FV2 isoform, indicating that glycosylation at Asn2181 is not stimulated by the presence of a glycine in position 2194.
12624624	0	6	gly	glycosylation	155:167	arg1	Asn2181					172:178	Asn2181	172:178	Asn2181	172:178	The R2-haplotype associated Asp2194Gly mutation in the light chain of human factor V results in lower expression levels of FV, but has no influence on the glycosylation of Asn2181.
12624624	9	7	theme	FXaVa	1548:1552	arg1	complex					1554:1560	FXaVa complex	1548:1560	the FXaVa complex (K(1/2Xa))	1544:1571	Finally, the apparent K(d) for dissociation of the FXaVa complex (K(1/2Xa)) was not higher in rFV mutants with the Asp2194Gly mutation than for rFVwt, suggesting that also the affinity for negatively charged phospholipids is not affected by substitution of Asp into Gly at position at 2194.
12624624	9	8	theme	Asp	1754:1756	arg1	substitution					1738:1749	substitution	1738:1749	substitution of Asp into Gly at position at 2194	1738:1785	Finally, the apparent K(d) for dissociation of the FXaVa complex (K(1/2Xa)) was not higher in rFV mutants with the Asp2194Gly mutation than for rFVwt, suggesting that also the affinity for negatively charged phospholipids is not affected by substitution of Asp into Gly at position at 2194.
12624624	0	9	theme	expression	102:111	arg1	levels					113:118	lower expression levels	96:118	lower expression levels of FV	96:124	The R2-haplotype associated Asp2194Gly mutation in the light chain of human factor V results in lower expression levels of FV, but has no influence on the glycosylation of Asn2181.
12624624	3	10	theme	allele	535:540	arg1	carriership					510:520	carriership	510:520	carriership of the R2-FV allele	510:540	Some studies have reported that carriership of the R2-FV allele is associated with an increased risk of venous thombosis.
12624624	8	11	theme	non-glycosylated	1341:1356	arg1	rFVwt					1358:1362	the non-glycosylated rFVwt	1337:1362	the non-glycosylated rFVwt	1337:1362	Furthermore, the light chains from Asp2194Gly containing rFV mutants showed similar molecular weights as the light chains of the non-glycosylated rFVwt or the plasma FV2 isoform, indicating that glycosylation at Asn2181 is not stimulated by the presence of a glycine in position 2194.
12624624	9	12	with	mutants	1595:1601	arg1	mutation					1623:1630	the Asp2194Gly mutation	1608:1630	the Asp2194Gly mutation	1608:1630	Finally, the apparent K(d) for dissociation of the FXaVa complex (K(1/2Xa)) was not higher in rFV mutants with the Asp2194Gly mutation than for rFVwt, suggesting that also the affinity for negatively charged phospholipids is not affected by substitution of Asp into Gly at position at 2194.
12624624	4	13	theme	R2-associated	651:663	arg1	phenotypes					665:674	the R2-associated phenotypes	647:674	the R2-associated phenotypes of the different mutations linked to the R2 haplotype of FV	647:734	At this moment, the individual contribution to the R2-associated phenotypes of the different mutations linked to the R2 haplotype of FV is unclear.
12624624	5	14	theme	Asp2194Gly	837:846	arg1	mutation					848:855	the R2-related Asp2194Gly mutation	822:855	the R2-related Asp2194Gly mutation	822:855	The main objective of our study was to obtain insight in the influence of the R2-related Asp2194Gly mutation on FV expression, FV structure and FV function using Bdomainless rFV mutants.
12624624	2	15	theme	FV1/FV2	438:444	arg1	ratios					446:451	increased FV1/FV2 ratios	428:451	increased FV1/FV2 ratios	428:451	Carriership of the R2-FV allele has been associated with reduced plasma FV levels, increased FV1/FV2 ratios and mild APC resistance.
12624624	8	16	theme	plasma	1371:1376	arg1	isoform					1382:1388	the plasma FV2 isoform	1367:1388	the plasma FV2 isoform	1367:1388	Furthermore, the light chains from Asp2194Gly containing rFV mutants showed similar molecular weights as the light chains of the non-glycosylated rFVwt or the plasma FV2 isoform, indicating that glycosylation at Asn2181 is not stimulated by the presence of a glycine in position 2194.
12624624	1	17	theme	linked	273:278	arg1	mutations					334:342	some missense mutations	320:342	some missense mutations	320:342	The R2 haplotype of the FV gene spans from exon 8 through 25 and comprises several strongly linked polymorphisms in the FV gene, including some missense mutations.
12624624	1	17	theme	linked	273:278	arg1	polymorphisms					280:292	several strongly linked polymorphisms	256:292	several strongly linked polymorphisms	256:292	The R2 haplotype of the FV gene spans from exon 8 through 25 and comprises several strongly linked polymorphisms in the FV gene, including some missense mutations.
12624624	8	18	theme	isoform	1382:1388	arg1	weights					1306:1312	similar molecular weights	1288:1312	similar molecular weights	1288:1312	Furthermore, the light chains from Asp2194Gly containing rFV mutants showed similar molecular weights as the light chains of the non-glycosylated rFVwt or the plasma FV2 isoform, indicating that glycosylation at Asn2181 is not stimulated by the presence of a glycine in position 2194.
12624624	8	18	theme	isoform	1382:1388	arg1	chains					1327:1332	the light chains	1317:1332	the light chains of the non-glycosylated rFVwt or the plasma FV2 isoform	1317:1388	Furthermore, the light chains from Asp2194Gly containing rFV mutants showed similar molecular weights as the light chains of the non-glycosylated rFVwt or the plasma FV2 isoform, indicating that glycosylation at Asn2181 is not stimulated by the presence of a glycine in position 2194.
12624624	4	19	theme	individual	620:629	arg1	unclear					739:745	unclear	739:745	unclear	739:745	At this moment, the individual contribution to the R2-associated phenotypes of the different mutations linked to the R2 haplotype of FV is unclear.
12624624	4	19	theme	individual	620:629	arg1	contribution					631:642	the individual contribution	616:642	the individual contribution to the R2-associated phenotypes of the different mutations linked to the R2 haplotype of FV	616:734	At this moment, the individual contribution to the R2-associated phenotypes of the different mutations linked to the R2 haplotype of FV is unclear.
12624624	0	20	theme	human	70:74	arg1	V					83:83	human factor V	70:83	human factor V	70:83	The R2-haplotype associated Asp2194Gly mutation in the light chain of human factor V results in lower expression levels of FV, but has no influence on the glycosylation of Asn2181.
12624624	2	21	theme	APC	462:464	arg1	resistance					466:475	mild APC resistance	457:475	mild APC resistance	457:475	Carriership of the R2-FV allele has been associated with reduced plasma FV levels, increased FV1/FV2 ratios and mild APC resistance.
12624624	8	22	theme	light	1229:1233	arg1	chains					1235:1240	the light chains	1225:1240	the light chains from Asp2194Gly containing rFV mutants	1225:1279	Furthermore, the light chains from Asp2194Gly containing rFV mutants showed similar molecular weights as the light chains of the non-glycosylated rFVwt or the plasma FV2 isoform, indicating that glycosylation at Asn2181 is not stimulated by the presence of a glycine in position 2194.
12624624	6	23	dep	resulted	973:980	arg1	compared					1035:1042	compared	1035:1042	compared to rFV wild-type	1035:1059	Replacing Asp at position 2194 by Gly resulted in a more than threefold reduction of rFV expression compared to rFV wild-type.
12624624	0	24	theme	V	83:83	arg1	mutation					39:46	The R2-haplotype associated Asp2194Gly mutation	0:46	The R2-haplotype associated Asp2194Gly mutation in the light chain of human factor V	0:83	The R2-haplotype associated Asp2194Gly mutation in the light chain of human factor V results in lower expression levels of FV, but has no influence on the glycosylation of Asn2181.
12624624	1	25	theme	FV	301:302	arg1	gene					304:307	the FV gene	297:307	the FV gene	297:307	The R2 haplotype of the FV gene spans from exon 8 through 25 and comprises several strongly linked polymorphisms in the FV gene, including some missense mutations.
12624624	5	26	from	insight	794:800	arg1	influence					809:817	the influence	805:817	the influence of the R2-related Asp2194Gly mutation on FV expression, FV structure and FV function using Bdomainless rFV mutants	805:932	The main objective of our study was to obtain insight in the influence of the R2-related Asp2194Gly mutation on FV expression, FV structure and FV function using Bdomainless rFV mutants.
12624624	5	26	from	insight	794:800	arg1	expression					863:872	FV expression	860:872	FV expression	860:872	The main objective of our study was to obtain insight in the influence of the R2-related Asp2194Gly mutation on FV expression, FV structure and FV function using Bdomainless rFV mutants.
12624624	5	26	from	insight	794:800	arg1	structure					878:886	FV structure	875:886	FV structure	875:886	The main objective of our study was to obtain insight in the influence of the R2-related Asp2194Gly mutation on FV expression, FV structure and FV function using Bdomainless rFV mutants.
12624624	5	26	from	insight	794:800	arg1	function					895:902	FV function	892:902	FV function	892:902	The main objective of our study was to obtain insight in the influence of the R2-related Asp2194Gly mutation on FV expression, FV structure and FV function using Bdomainless rFV mutants.
12624624	5	27	theme	FV	875:876	arg1	structure					878:886	FV structure	875:886	FV structure	875:886	The main objective of our study was to obtain insight in the influence of the R2-related Asp2194Gly mutation on FV expression, FV structure and FV function using Bdomainless rFV mutants.
12624624	9	28	from	2194	1782:1785	arg1	substitution					1738:1749	substitution	1738:1749	substitution of Asp into Gly at position at 2194	1738:1785	Finally, the apparent K(d) for dissociation of the FXaVa complex (K(1/2Xa)) was not higher in rFV mutants with the Asp2194Gly mutation than for rFVwt, suggesting that also the affinity for negatively charged phospholipids is not affected by substitution of Asp into Gly at position at 2194.
12624624	9	29	theme	Asp2194Gly	1612:1621	arg1	mutation					1623:1630	the Asp2194Gly mutation	1608:1630	the Asp2194Gly mutation	1608:1630	Finally, the apparent K(d) for dissociation of the FXaVa complex (K(1/2Xa)) was not higher in rFV mutants with the Asp2194Gly mutation than for rFVwt, suggesting that also the affinity for negatively charged phospholipids is not affected by substitution of Asp into Gly at position at 2194.
12624624	0	30	from	mutation	39:46	arg1	chain					61:65	the light chain	51:65	the light chain	51:65	The R2-haplotype associated Asp2194Gly mutation in the light chain of human factor V results in lower expression levels of FV, but has no influence on the glycosylation of Asn2181.
12624624	7	31	with	association	1158:1168	arg1	levels					1204:1209	lower FV levels	1195:1209	lower FV levels	1195:1209	Therefore, we propose that the R2-linked Asp2194Gly mutation is an important determinant of the association of the R2-FV allele with lower FV levels.
12624624	4	32	theme	different	683:691	arg1	mutations					693:701	the different mutations	679:701	the different mutations linked to the R2 haplotype of FV	679:734	At this moment, the individual contribution to the R2-associated phenotypes of the different mutations linked to the R2 haplotype of FV is unclear.
12624624	2	33	theme	R2-FV	364:368	arg1	allele					370:375	the R2-FV allele	360:375	the R2-FV allele	360:375	Carriership of the R2-FV allele has been associated with reduced plasma FV levels, increased FV1/FV2 ratios and mild APC resistance.
12624624	0	34	theme	associated	17:26	arg1	mutation					39:46	The R2-haplotype associated Asp2194Gly mutation	0:46	The R2-haplotype associated Asp2194Gly mutation in the light chain of human factor V	0:83	The R2-haplotype associated Asp2194Gly mutation in the light chain of human factor V results in lower expression levels of FV, but has no influence on the glycosylation of Asn2181.
12624624	7	35	theme	FV	1201:1202	arg1	levels					1204:1209	lower FV levels	1195:1209	lower FV levels	1195:1209	Therefore, we propose that the R2-linked Asp2194Gly mutation is an important determinant of the association of the R2-FV allele with lower FV levels.
12624624	2	36	theme	FV	417:418	arg1	levels					420:425	reduced plasma FV levels	402:425	reduced plasma FV levels	402:425	Carriership of the R2-FV allele has been associated with reduced plasma FV levels, increased FV1/FV2 ratios and mild APC resistance.
12624624	0	37	from	influence	138:146	arg1	glycosylation					155:167	the glycosylation	151:167	the glycosylation of Asn2181	151:178	The R2-haplotype associated Asp2194Gly mutation in the light chain of human factor V results in lower expression levels of FV, but has no influence on the glycosylation of Asn2181.
12624624	3	38	theme	venous	582:587	arg1	thombosis					589:597	venous thombosis	582:597	venous thombosis	582:597	Some studies have reported that carriership of the R2-FV allele is associated with an increased risk of venous thombosis.
12624624	8	39	theme	similar	1288:1294	arg1	weights					1306:1312	similar molecular weights	1288:1312	similar molecular weights	1288:1312	Furthermore, the light chains from Asp2194Gly containing rFV mutants showed similar molecular weights as the light chains of the non-glycosylated rFVwt or the plasma FV2 isoform, indicating that glycosylation at Asn2181 is not stimulated by the presence of a glycine in position 2194.
12624624	8	39	theme	similar	1288:1294	arg1	chains					1327:1332	the light chains	1317:1332	the light chains of the non-glycosylated rFVwt or the plasma FV2 isoform	1317:1388	Furthermore, the light chains from Asp2194Gly containing rFV mutants showed similar molecular weights as the light chains of the non-glycosylated rFVwt or the plasma FV2 isoform, indicating that glycosylation at Asn2181 is not stimulated by the presence of a glycine in position 2194.
12624624	8	40	from	Asn2181	1424:1430	arg1	glycosylation					1407:1419	glycosylation	1407:1419	glycosylation at Asn2181	1407:1430	Furthermore, the light chains from Asp2194Gly containing rFV mutants showed similar molecular weights as the light chains of the non-glycosylated rFVwt or the plasma FV2 isoform, indicating that glycosylation at Asn2181 is not stimulated by the presence of a glycine in position 2194.
12624624	8	41	from	Asp2194Gly	1247:1256	arg1	chains					1235:1240	the light chains	1225:1240	the light chains from Asp2194Gly containing rFV mutants	1225:1279	Furthermore, the light chains from Asp2194Gly containing rFV mutants showed similar molecular weights as the light chains of the non-glycosylated rFVwt or the plasma FV2 isoform, indicating that glycosylation at Asn2181 is not stimulated by the presence of a glycine in position 2194.
12624624	9	42	from	position	1770:1777	arg1	substitution					1738:1749	substitution	1738:1749	substitution of Asp into Gly at position at 2194	1738:1785	Finally, the apparent K(d) for dissociation of the FXaVa complex (K(1/2Xa)) was not higher in rFV mutants with the Asp2194Gly mutation than for rFVwt, suggesting that also the affinity for negatively charged phospholipids is not affected by substitution of Asp into Gly at position at 2194.
12624624	2	43	theme	reduced	402:408	arg1	levels					420:425	reduced plasma FV levels	402:425	reduced plasma FV levels	402:425	Carriership of the R2-FV allele has been associated with reduced plasma FV levels, increased FV1/FV2 ratios and mild APC resistance.
12624624	6	44	dep	threefold	997:1005	arg1	than					992:995	than	992:995	than	992:995	Replacing Asp at position 2194 by Gly resulted in a more than threefold reduction of rFV expression compared to rFV wild-type.
12624624	6	44	dep	threefold	997:1005	arg1	more					987:990	more	987:990	more	987:990	Replacing Asp at position 2194 by Gly resulted in a more than threefold reduction of rFV expression compared to rFV wild-type.
12624624	1	45	from	polymorphisms	280:292	arg1	gene					304:307	the FV gene	297:307	the FV gene	297:307	The R2 haplotype of the FV gene spans from exon 8 through 25 and comprises several strongly linked polymorphisms in the FV gene, including some missense mutations.
12624624	1	46	theme	several	256:262	arg1	mutations					334:342	some missense mutations	320:342	some missense mutations	320:342	The R2 haplotype of the FV gene spans from exon 8 through 25 and comprises several strongly linked polymorphisms in the FV gene, including some missense mutations.
12624624	1	46	theme	several	256:262	arg1	polymorphisms					280:292	several strongly linked polymorphisms	256:292	several strongly linked polymorphisms	256:292	The R2 haplotype of the FV gene spans from exon 8 through 25 and comprises several strongly linked polymorphisms in the FV gene, including some missense mutations.
12624624	7	47	theme	R2-FV	1177:1181	arg1	allele					1183:1188	the R2-FV allele	1173:1188	the R2-FV allele	1173:1188	Therefore, we propose that the R2-linked Asp2194Gly mutation is an important determinant of the association of the R2-FV allele with lower FV levels.
12624624	5	48	from	expression	863:872	arg1	insight					794:800	insight	794:800	insight in the influence of the R2-related Asp2194Gly mutation on FV expression, FV structure and FV function using Bdomainless rFV mutants	794:932	The main objective of our study was to obtain insight in the influence of the R2-related Asp2194Gly mutation on FV expression, FV structure and FV function using Bdomainless rFV mutants.
12624624	1	49	theme	R2	185:186	arg1	haplotype					188:196	The R2 haplotype	181:196	The R2 haplotype of the FV gene	181:211	The R2 haplotype of the FV gene spans from exon 8 through 25 and comprises several strongly linked polymorphisms in the FV gene, including some missense mutations.
12624624	4	50	theme	FV	733:734	arg1	haplotype					720:728	the R2 haplotype	713:728	the R2 haplotype of FV	713:734	At this moment, the individual contribution to the R2-associated phenotypes of the different mutations linked to the R2 haplotype of FV is unclear.
12624624	5	51	theme	Bdomainless	910:920	arg1	mutants					926:932	Bdomainless rFV mutants	910:932	Bdomainless rFV mutants	910:932	The main objective of our study was to obtain insight in the influence of the R2-related Asp2194Gly mutation on FV expression, FV structure and FV function using Bdomainless rFV mutants.
12624624	7	52	theme	Asp2194Gly	1103:1112	arg1	mutation					1114:1121	the R2-linked Asp2194Gly mutation	1089:1121	the R2-linked Asp2194Gly mutation	1089:1121	Therefore, we propose that the R2-linked Asp2194Gly mutation is an important determinant of the association of the R2-FV allele with lower FV levels.
12624624	7	52	theme	Asp2194Gly	1103:1112	arg1	determinant					1139:1149	an important determinant	1126:1149	an important determinant of the association of the R2-FV allele with lower FV levels	1126:1209	Therefore, we propose that the R2-linked Asp2194Gly mutation is an important determinant of the association of the R2-FV allele with lower FV levels.
12624624	1	53	theme	FV	205:206	arg1	gene					208:211	the FV gene	201:211	the FV gene	201:211	The R2 haplotype of the FV gene spans from exon 8 through 25 and comprises several strongly linked polymorphisms in the FV gene, including some missense mutations.
12624624	4	54	from	moment	608:613	arg1	unclear					739:745	unclear	739:745	unclear	739:745	At this moment, the individual contribution to the R2-associated phenotypes of the different mutations linked to the R2 haplotype of FV is unclear.
12624624	4	54	from	moment	608:613	arg1	contribution					631:642	the individual contribution	616:642	the individual contribution to the R2-associated phenotypes of the different mutations linked to the R2 haplotype of FV	616:734	At this moment, the individual contribution to the R2-associated phenotypes of the different mutations linked to the R2 haplotype of FV is unclear.
12624624	0	55	theme	Asn2181	172:178	arg1	glycosylation					155:167	the glycosylation	151:167	the glycosylation of Asn2181	151:178	The R2-haplotype associated Asp2194Gly mutation in the light chain of human factor V results in lower expression levels of FV, but has no influence on the glycosylation of Asn2181.
12624624	5	56	theme	study	774:778	arg1	objective					757:765	The main objective	748:765	The main objective of our study	748:778	The main objective of our study was to obtain insight in the influence of the R2-related Asp2194Gly mutation on FV expression, FV structure and FV function using Bdomainless rFV mutants.
12624624	9	57	dep	complex	1554:1560	arg1	1/2Xa					1565:1569	1/2Xa	1565:1569	1/2Xa	1565:1569	Finally, the apparent K(d) for dissociation of the FXaVa complex (K(1/2Xa)) was not higher in rFV mutants with the Asp2194Gly mutation than for rFVwt, suggesting that also the affinity for negatively charged phospholipids is not affected by substitution of Asp into Gly at position at 2194.
12624624	9	57	dep	complex	1554:1560	arg1	K					1563:1563	K	1563:1563	K(1/2Xa)	1563:1570	Finally, the apparent K(d) for dissociation of the FXaVa complex (K(1/2Xa)) was not higher in rFV mutants with the Asp2194Gly mutation than for rFVwt, suggesting that also the affinity for negatively charged phospholipids is not affected by substitution of Asp into Gly at position at 2194.
12624624	5	58	from	function	895:902	arg1	insight					794:800	insight	794:800	insight in the influence of the R2-related Asp2194Gly mutation on FV expression, FV structure and FV function using Bdomainless rFV mutants	794:932	The main objective of our study was to obtain insight in the influence of the R2-related Asp2194Gly mutation on FV expression, FV structure and FV function using Bdomainless rFV mutants.
12624624	8	59	gly	non-glycosylated	1341:1356	arg1	rFVwt					1358:1362	the non-glycosylated rFVwt	1337:1362	the non-glycosylated rFVwt	1337:1362	Furthermore, the light chains from Asp2194Gly containing rFV mutants showed similar molecular weights as the light chains of the non-glycosylated rFVwt or the plasma FV2 isoform, indicating that glycosylation at Asn2181 is not stimulated by the presence of a glycine in position 2194.
12624624	6	60	theme	rFV	1047:1049	arg1	wild-type					1051:1059	rFV wild-type	1047:1059	rFV wild-type	1047:1059	Replacing Asp at position 2194 by Gly resulted in a more than threefold reduction of rFV expression compared to rFV wild-type.
12624624	4	61	attach	linked	703:708	arg2	mutations					693:701	the different mutations	679:701	the different mutations linked to the R2 haplotype of FV	679:734	At this moment, the individual contribution to the R2-associated phenotypes of the different mutations linked to the R2 haplotype of FV is unclear.
12624624	4	61	attach	linked	703:708	arg1	haplotype					720:728	the R2 haplotype	713:728	the R2 haplotype of FV	713:734	At this moment, the individual contribution to the R2-associated phenotypes of the different mutations linked to the R2 haplotype of FV is unclear.
12624624	6	62	from	position	952:959	arg1	Asp					945:947	Asp	945:947	Asp at position 2194	945:964	Replacing Asp at position 2194 by Gly resulted in a more than threefold reduction of rFV expression compared to rFV wild-type.
12624624	5	63	theme	main	752:755	arg1	objective					757:765	The main objective	748:765	The main objective of our study	748:778	The main objective of our study was to obtain insight in the influence of the R2-related Asp2194Gly mutation on FV expression, FV structure and FV function using Bdomainless rFV mutants.
12624624	9	64	theme	complex	1554:1560	arg1	dissociation					1528:1539	dissociation	1528:1539	dissociation of the FXaVa complex (K(1/2Xa))	1528:1571	Finally, the apparent K(d) for dissociation of the FXaVa complex (K(1/2Xa)) was not higher in rFV mutants with the Asp2194Gly mutation than for rFVwt, suggesting that also the affinity for negatively charged phospholipids is not affected by substitution of Asp into Gly at position at 2194.
12624624	6	65	theme	rFV	1020:1022	arg1	expression					1024:1033	rFV expression	1020:1033	rFV expression	1020:1033	Replacing Asp at position 2194 by Gly resulted in a more than threefold reduction of rFV expression compared to rFV wild-type.
12624624	0	66	theme	FV	123:124	arg1	levels					113:118	lower expression levels	96:118	lower expression levels of FV	96:124	The R2-haplotype associated Asp2194Gly mutation in the light chain of human factor V results in lower expression levels of FV, but has no influence on the glycosylation of Asn2181.
12624624	1	67	theme	missense	325:332	arg1	mutations					334:342	some missense mutations	320:342	some missense mutations	320:342	The R2 haplotype of the FV gene spans from exon 8 through 25 and comprises several strongly linked polymorphisms in the FV gene, including some missense mutations.
12624624	3	68	theme	R2-FV	529:533	arg1	allele					535:540	the R2-FV allele	525:540	the R2-FV allele	525:540	Some studies have reported that carriership of the R2-FV allele is associated with an increased risk of venous thombosis.
12624624	8	69	theme	rFVwt	1358:1362	arg1	weights					1306:1312	similar molecular weights	1288:1312	similar molecular weights	1288:1312	Furthermore, the light chains from Asp2194Gly containing rFV mutants showed similar molecular weights as the light chains of the non-glycosylated rFVwt or the plasma FV2 isoform, indicating that glycosylation at Asn2181 is not stimulated by the presence of a glycine in position 2194.
12624624	8	69	theme	rFVwt	1358:1362	arg1	chains					1327:1332	the light chains	1317:1332	the light chains of the non-glycosylated rFVwt or the plasma FV2 isoform	1317:1388	Furthermore, the light chains from Asp2194Gly containing rFV mutants showed similar molecular weights as the light chains of the non-glycosylated rFVwt or the plasma FV2 isoform, indicating that glycosylation at Asn2181 is not stimulated by the presence of a glycine in position 2194.
12624624	9	70	theme	rFV	1591:1593	arg1	mutants					1595:1601	rFV mutants	1591:1601	rFV mutants with the Asp2194Gly mutation	1591:1630	Finally, the apparent K(d) for dissociation of the FXaVa complex (K(1/2Xa)) was not higher in rFV mutants with the Asp2194Gly mutation than for rFVwt, suggesting that also the affinity for negatively charged phospholipids is not affected by substitution of Asp into Gly at position at 2194.
12624624	5	71	theme	R2-related	826:835	arg1	mutation					848:855	the R2-related Asp2194Gly mutation	822:855	the R2-related Asp2194Gly mutation	822:855	The main objective of our study was to obtain insight in the influence of the R2-related Asp2194Gly mutation on FV expression, FV structure and FV function using Bdomainless rFV mutants.
12624624	8	72	theme	FV2	1378:1380	arg1	isoform					1382:1388	the plasma FV2 isoform	1367:1388	the plasma FV2 isoform	1367:1388	Furthermore, the light chains from Asp2194Gly containing rFV mutants showed similar molecular weights as the light chains of the non-glycosylated rFVwt or the plasma FV2 isoform, indicating that glycosylation at Asn2181 is not stimulated by the presence of a glycine in position 2194.
12624624	8	73	gly	glycosylation	1407:1419	arg2	Asn2181					1424:1430	Asn2181	1424:1430	Asn2181	1424:1430	Furthermore, the light chains from Asp2194Gly containing rFV mutants showed similar molecular weights as the light chains of the non-glycosylated rFVwt or the plasma FV2 isoform, indicating that glycosylation at Asn2181 is not stimulated by the presence of a glycine in position 2194.
12624624	8	73	gly	glycosylation	1407:1419	arg1	Asn2181					1424:1430	Asn2181	1424:1430	Asn2181	1424:1430	Furthermore, the light chains from Asp2194Gly containing rFV mutants showed similar molecular weights as the light chains of the non-glycosylated rFVwt or the plasma FV2 isoform, indicating that glycosylation at Asn2181 is not stimulated by the presence of a glycine in position 2194.
12624624	2	74	theme	increased	428:436	arg1	ratios					446:451	increased FV1/FV2 ratios	428:451	increased FV1/FV2 ratios	428:451	Carriership of the R2-FV allele has been associated with reduced plasma FV levels, increased FV1/FV2 ratios and mild APC resistance.
12624624	7	75	theme	R2-linked	1093:1101	arg1	mutation					1114:1121	the R2-linked Asp2194Gly mutation	1089:1121	the R2-linked Asp2194Gly mutation	1089:1121	Therefore, we propose that the R2-linked Asp2194Gly mutation is an important determinant of the association of the R2-FV allele with lower FV levels.
12624624	7	75	theme	R2-linked	1093:1101	arg1	determinant					1139:1149	an important determinant	1126:1149	an important determinant of the association of the R2-FV allele with lower FV levels	1126:1209	Therefore, we propose that the R2-linked Asp2194Gly mutation is an important determinant of the association of the R2-FV allele with lower FV levels.
12624624	0	76	theme	factor	76:81	arg1	V					83:83	human factor V	70:83	human factor V	70:83	The R2-haplotype associated Asp2194Gly mutation in the light chain of human factor V results in lower expression levels of FV, but has no influence on the glycosylation of Asn2181.
12624624	8	77	contain	containing	1258:1267	arg2	mutants					1273:1279	rFV mutants	1269:1279	rFV mutants	1269:1279	Furthermore, the light chains from Asp2194Gly containing rFV mutants showed similar molecular weights as the light chains of the non-glycosylated rFVwt or the plasma FV2 isoform, indicating that glycosylation at Asn2181 is not stimulated by the presence of a glycine in position 2194.
12624624	8	77	contain	containing	1258:1267	arg1	Asp2194Gly					1247:1256	Asp2194Gly	1247:1256	Asp2194Gly	1247:1256	Furthermore, the light chains from Asp2194Gly containing rFV mutants showed similar molecular weights as the light chains of the non-glycosylated rFVwt or the plasma FV2 isoform, indicating that glycosylation at Asn2181 is not stimulated by the presence of a glycine in position 2194.
12624624	5	78	from	influence	809:817	arg1	expression					863:872	FV expression	860:872	FV expression	860:872	The main objective of our study was to obtain insight in the influence of the R2-related Asp2194Gly mutation on FV expression, FV structure and FV function using Bdomainless rFV mutants.
12624624	5	78	from	influence	809:817	arg1	structure					878:886	FV structure	875:886	FV structure	875:886	The main objective of our study was to obtain insight in the influence of the R2-related Asp2194Gly mutation on FV expression, FV structure and FV function using Bdomainless rFV mutants.
12624624	5	78	from	influence	809:817	arg1	function					895:902	FV function	892:902	FV function	892:902	The main objective of our study was to obtain insight in the influence of the R2-related Asp2194Gly mutation on FV expression, FV structure and FV function using Bdomainless rFV mutants.
12624624	2	79	theme	mild	457:460	arg1	resistance					466:475	mild APC resistance	457:475	mild APC resistance	457:475	Carriership of the R2-FV allele has been associated with reduced plasma FV levels, increased FV1/FV2 ratios and mild APC resistance.
12624624	4	80	theme	mutations	693:701	arg1	phenotypes					665:674	the R2-associated phenotypes	647:674	the R2-associated phenotypes of the different mutations linked to the R2 haplotype of FV	647:734	At this moment, the individual contribution to the R2-associated phenotypes of the different mutations linked to the R2 haplotype of FV is unclear.
12624624	0	81	contain	has	131:133	arg2	influence					138:146	no influence	135:146	no influence on the glycosylation of Asn2181	135:178	The R2-haplotype associated Asp2194Gly mutation in the light chain of human factor V results in lower expression levels of FV, but has no influence on the glycosylation of Asn2181.
12624624	0	81	contain	has	131:133	arg1	mutation					39:46	The R2-haplotype associated Asp2194Gly mutation	0:46	The R2-haplotype associated Asp2194Gly mutation in the light chain of human factor V	0:83	The R2-haplotype associated Asp2194Gly mutation in the light chain of human factor V results in lower expression levels of FV, but has no influence on the glycosylation of Asn2181.
12624624	0	82	theme	lower	96:100	arg1	levels					113:118	lower expression levels	96:118	lower expression levels of FV	96:124	The R2-haplotype associated Asp2194Gly mutation in the light chain of human factor V results in lower expression levels of FV, but has no influence on the glycosylation of Asn2181.
12624624	0	83	theme	R2-haplotype	4:15	arg1	mutation					39:46	The R2-haplotype associated Asp2194Gly mutation	0:46	The R2-haplotype associated Asp2194Gly mutation in the light chain of human factor V	0:83	The R2-haplotype associated Asp2194Gly mutation in the light chain of human factor V results in lower expression levels of FV, but has no influence on the glycosylation of Asn2181.
12624624	5	84	theme	mutation	848:855	arg1	influence					809:817	the influence	805:817	the influence of the R2-related Asp2194Gly mutation on FV expression, FV structure and FV function using Bdomainless rFV mutants	805:932	The main objective of our study was to obtain insight in the influence of the R2-related Asp2194Gly mutation on FV expression, FV structure and FV function using Bdomainless rFV mutants.
12624624	8	85	from	position	1482:1489	arg1	presence					1457:1464	the presence	1453:1464	the presence of a glycine in position 2194	1453:1494	Furthermore, the light chains from Asp2194Gly containing rFV mutants showed similar molecular weights as the light chains of the non-glycosylated rFVwt or the plasma FV2 isoform, indicating that glycosylation at Asn2181 is not stimulated by the presence of a glycine in position 2194.
12624624	0	86	theme	Asp2194Gly	28:37	arg1	mutation					39:46	The R2-haplotype associated Asp2194Gly mutation	0:46	The R2-haplotype associated Asp2194Gly mutation in the light chain of human factor V	0:83	The R2-haplotype associated Asp2194Gly mutation in the light chain of human factor V results in lower expression levels of FV, but has no influence on the glycosylation of Asn2181.
12624624	5	87	theme	FV	860:861	arg1	expression					863:872	FV expression	860:872	FV expression	860:872	The main objective of our study was to obtain insight in the influence of the R2-related Asp2194Gly mutation on FV expression, FV structure and FV function using Bdomainless rFV mutants.
12624624	7	88	theme	lower	1195:1199	arg1	levels					1204:1209	lower FV levels	1195:1209	lower FV levels	1195:1209	Therefore, we propose that the R2-linked Asp2194Gly mutation is an important determinant of the association of the R2-FV allele with lower FV levels.
12624624	2	89	theme	allele	370:375	arg1	Carriership					345:355	Carriership	345:355	Carriership of the R2-FV allele	345:375	Carriership of the R2-FV allele has been associated with reduced plasma FV levels, increased FV1/FV2 ratios and mild APC resistance.
12624624	8	90	theme	rFV	1269:1271	arg1	mutants					1273:1279	rFV mutants	1269:1279	rFV mutants	1269:1279	Furthermore, the light chains from Asp2194Gly containing rFV mutants showed similar molecular weights as the light chains of the non-glycosylated rFVwt or the plasma FV2 isoform, indicating that glycosylation at Asn2181 is not stimulated by the presence of a glycine in position 2194.
12624624	1	91	link	linked	273:278	arg1	mutations					334:342	some missense mutations	320:342	some missense mutations	320:342	The R2 haplotype of the FV gene spans from exon 8 through 25 and comprises several strongly linked polymorphisms in the FV gene, including some missense mutations.
12624624	1	91	link	linked	273:278	arg1	polymorphisms					280:292	several strongly linked polymorphisms	256:292	several strongly linked polymorphisms	256:292	The R2 haplotype of the FV gene spans from exon 8 through 25 and comprises several strongly linked polymorphisms in the FV gene, including some missense mutations.
12624624	5	92	theme	rFV	922:924	arg1	mutants					926:932	Bdomainless rFV mutants	910:932	Bdomainless rFV mutants	910:932	The main objective of our study was to obtain insight in the influence of the R2-related Asp2194Gly mutation on FV expression, FV structure and FV function using Bdomainless rFV mutants.
12624624	7	93	theme	allele	1183:1188	arg1	association					1158:1168	the association	1154:1168	the association of the R2-FV allele with lower FV levels	1154:1209	Therefore, we propose that the R2-linked Asp2194Gly mutation is an important determinant of the association of the R2-FV allele with lower FV levels.
12624624	2	94	theme	plasma	410:415	arg1	levels					420:425	reduced plasma FV levels	402:425	reduced plasma FV levels	402:425	Carriership of the R2-FV allele has been associated with reduced plasma FV levels, increased FV1/FV2 ratios and mild APC resistance.
12624624	3	95	theme	increased	564:572	arg1	risk					574:577	an increased risk	561:577	an increased risk of venous thombosis	561:597	Some studies have reported that carriership of the R2-FV allele is associated with an increased risk of venous thombosis.
12624624	0	96	theme	light	55:59	arg1	chain					61:65	the light chain	51:65	the light chain	51:65	The R2-haplotype associated Asp2194Gly mutation in the light chain of human factor V results in lower expression levels of FV, but has no influence on the glycosylation of Asn2181.
12624624	6	97	theme	expression	1024:1033	arg1	reduction					1007:1015	a more than threefold reduction	985:1015	a more than threefold reduction of rFV expression	985:1033	Replacing Asp at position 2194 by Gly resulted in a more than threefold reduction of rFV expression compared to rFV wild-type.
12624624	8	98	theme	glycine	1471:1477	arg1	presence					1457:1464	the presence	1453:1464	the presence of a glycine in position 2194	1453:1494	Furthermore, the light chains from Asp2194Gly containing rFV mutants showed similar molecular weights as the light chains of the non-glycosylated rFVwt or the plasma FV2 isoform, indicating that glycosylation at Asn2181 is not stimulated by the presence of a glycine in position 2194.
12624624	8	99	theme	molecular	1296:1304	arg1	weights					1306:1312	similar molecular weights	1288:1312	similar molecular weights	1288:1312	Furthermore, the light chains from Asp2194Gly containing rFV mutants showed similar molecular weights as the light chains of the non-glycosylated rFVwt or the plasma FV2 isoform, indicating that glycosylation at Asn2181 is not stimulated by the presence of a glycine in position 2194.
12624624	8	99	theme	molecular	1296:1304	arg1	chains					1327:1332	the light chains	1317:1332	the light chains of the non-glycosylated rFVwt or the plasma FV2 isoform	1317:1388	Furthermore, the light chains from Asp2194Gly containing rFV mutants showed similar molecular weights as the light chains of the non-glycosylated rFVwt or the plasma FV2 isoform, indicating that glycosylation at Asn2181 is not stimulated by the presence of a glycine in position 2194.
12624624	9	100	theme	apparent	1510:1517	arg1	d					1521:1521	d	1521:1521	d	1521:1521	Finally, the apparent K(d) for dissociation of the FXaVa complex (K(1/2Xa)) was not higher in rFV mutants with the Asp2194Gly mutation than for rFVwt, suggesting that also the affinity for negatively charged phospholipids is not affected by substitution of Asp into Gly at position at 2194.
12624624	9	100	theme	apparent	1510:1517	arg1	higher					1581:1586	higher	1581:1586	higher	1581:1586	Finally, the apparent K(d) for dissociation of the FXaVa complex (K(1/2Xa)) was not higher in rFV mutants with the Asp2194Gly mutation than for rFVwt, suggesting that also the affinity for negatively charged phospholipids is not affected by substitution of Asp into Gly at position at 2194.
12624624	9	100	theme	apparent	1510:1517	arg1	K					1519:1519	the apparent K	1506:1519	the apparent K(d) for dissociation of the FXaVa complex (K(1/2Xa))	1506:1571	Finally, the apparent K(d) for dissociation of the FXaVa complex (K(1/2Xa)) was not higher in rFV mutants with the Asp2194Gly mutation than for rFVwt, suggesting that also the affinity for negatively charged phospholipids is not affected by substitution of Asp into Gly at position at 2194.
12624624	5	101	theme	FV	892:893	arg1	function					895:902	FV function	892:902	FV function	892:902	The main objective of our study was to obtain insight in the influence of the R2-related Asp2194Gly mutation on FV expression, FV structure and FV function using Bdomainless rFV mutants.
12624624	7	102	theme	association	1158:1168	arg1	mutation					1114:1121	the R2-linked Asp2194Gly mutation	1089:1121	the R2-linked Asp2194Gly mutation	1089:1121	Therefore, we propose that the R2-linked Asp2194Gly mutation is an important determinant of the association of the R2-FV allele with lower FV levels.
12624624	7	102	theme	association	1158:1168	arg1	determinant					1139:1149	an important determinant	1126:1149	an important determinant of the association of the R2-FV allele with lower FV levels	1126:1209	Therefore, we propose that the R2-linked Asp2194Gly mutation is an important determinant of the association of the R2-FV allele with lower FV levels.
12624624	3	103	theme	thombosis	589:597	arg1	risk					574:577	an increased risk	561:577	an increased risk of venous thombosis	561:597	Some studies have reported that carriership of the R2-FV allele is associated with an increased risk of venous thombosis.
12624624	4	104	theme	R2	717:718	arg1	haplotype					720:728	the R2 haplotype	713:728	the R2 haplotype of FV	713:734	At this moment, the individual contribution to the R2-associated phenotypes of the different mutations linked to the R2 haplotype of FV is unclear.
12624624	6	105	theme	threefold	997:1005	arg1	reduction					1007:1015	a more than threefold reduction	985:1015	a more than threefold reduction of rFV expression	985:1033	Replacing Asp at position 2194 by Gly resulted in a more than threefold reduction of rFV expression compared to rFV wild-type.
12624624	8	106	theme	light	1321:1325	arg1	weights					1306:1312	similar molecular weights	1288:1312	similar molecular weights	1288:1312	Furthermore, the light chains from Asp2194Gly containing rFV mutants showed similar molecular weights as the light chains of the non-glycosylated rFVwt or the plasma FV2 isoform, indicating that glycosylation at Asn2181 is not stimulated by the presence of a glycine in position 2194.
12624624	8	106	theme	light	1321:1325	arg1	chains					1327:1332	the light chains	1317:1332	the light chains of the non-glycosylated rFVwt or the plasma FV2 isoform	1317:1388	Furthermore, the light chains from Asp2194Gly containing rFV mutants showed similar molecular weights as the light chains of the non-glycosylated rFVwt or the plasma FV2 isoform, indicating that glycosylation at Asn2181 is not stimulated by the presence of a glycine in position 2194.
12624624	5	107	from	structure	878:886	arg1	insight					794:800	insight	794:800	insight in the influence of the R2-related Asp2194Gly mutation on FV expression, FV structure and FV function using Bdomainless rFV mutants	794:932	The main objective of our study was to obtain insight in the influence of the R2-related Asp2194Gly mutation on FV expression, FV structure and FV function using Bdomainless rFV mutants.
16834341	4	0	from	site	633:636	arg1	pattern					580:586	The characteristic pattern	561:586	The characteristic pattern of glycan distribution at each glycosylation site	561:636	The characteristic pattern of glycan distribution at each glycosylation site has been deduced and compared between horse and human FSH preparations.
16834341	5	1	theme	equine	796:801	arg1	glycoforms					772:781	glycoforms	772:781	glycoforms of human and equine FSH	772:805	The data suggest that site-specific differences exist between glycoforms of human and equine FSH.
16834341	7	2	theme	hFSH	964:967	arg1	Asn52					955:959	Asn52	955:959	Asn52 of hFSH	955:967	Also, glycoforms at Asn52 of hFSH are all complex type, whereas in eFSH, both complex and hybrid structures exist at this site.
16834341	3	3	theme	site-specific	502:514	arg1	manner					516:521	a glycosylation site-specific manner	486:521	a glycosylation site-specific manner using FT-ICR-MS and Edman sequencing	486:558	In the present study the negatively charged glycopeptides of equine and human pituitary follicle stimulating hormone (eFSH and hFSH) have been characterized in a glycosylation site-specific manner using FT-ICR-MS and Edman sequencing.
16834341	4	4	theme	distribution	598:609	arg1	pattern					580:586	The characteristic pattern	561:586	The characteristic pattern of glycan distribution at each glycosylation site	561:636	The characteristic pattern of glycan distribution at each glycosylation site has been deduced and compared between horse and human FSH preparations.
16834341	4	5	gly	glycosylation	619:631	arg2	site					633:636	each glycosylation site	614:636	each glycosylation site	614:636	The characteristic pattern of glycan distribution at each glycosylation site has been deduced and compared between horse and human FSH preparations.
16834341	7	6	from	Asn52	955:959	arg1	glycoforms					941:950	glycoforms	941:950	glycoforms at Asn52 of hFSH	941:967	Also, glycoforms at Asn52 of hFSH are all complex type, whereas in eFSH, both complex and hybrid structures exist at this site.
16834341	7	6	from	Asn52	955:959	arg1	type					985:988	all complex type	973:988	all complex type	973:988	Also, glycoforms at Asn52 of hFSH are all complex type, whereas in eFSH, both complex and hybrid structures exist at this site.
16834341	4	7	theme	glycan	591:596	arg1	distribution					598:609	glycan distribution	591:609	glycan distribution	591:609	The characteristic pattern of glycan distribution at each glycosylation site has been deduced and compared between horse and human FSH preparations.
16834341	8	8	theme	glycans	1109:1115	arg1	percentage					1086:1095	a higher percentage	1077:1095	a higher percentage of sulfated glycans in the latter site compared to the former	1077:1157	There is also a higher percentage of sulfated glycans in the latter site compared to the former.
16834341	8	9	from	percentage	1086:1095	arg1	site					1131:1134	the latter site	1120:1134	the latter site compared to the former	1120:1157	There is also a higher percentage of sulfated glycans in the latter site compared to the former.
16834341	6	10	from	site	837:840	arg1	Asn7					863:866	Asn7	863:866	Asn7	863:866	For instance, except for one site in the beta subunit (Asn7) of hFSH all other sites in both species have sulfated glycoforms.
16834341	6	10	from	site	837:840	arg1	subunit					854:860	the beta subunit	845:860	the beta subunit (Asn7) of hFSH	845:875	For instance, except for one site in the beta subunit (Asn7) of hFSH all other sites in both species have sulfated glycoforms.
16834341	7	11	gly	glycoforms	941:950	arg2	Asn52					955:959	Asn52	955:959	Asn52 of hFSH	955:967	Also, glycoforms at Asn52 of hFSH are all complex type, whereas in eFSH, both complex and hybrid structures exist at this site.
16834341	0	12	theme	isolates	97:104	arg1	analysis					85:92	glycopeptide analysis	72:92	Comparative glycomics of the glycoprotein follicle stimulating hormone: glycopeptide analysis of isolates from two mammalian species.	0:132	Comparative glycomics of the glycoprotein follicle stimulating hormone: glycopeptide analysis of isolates from two mammalian species.
16834341	9	13	used	used	1296:1299	arg2	data					1284:1287	these data	1278:1287	these data	1278:1287	This is the first study that characterizes the glycans from this hormone in a glycosylation site-specific manner, and these data can be used to begin correlative studies between glycosylation structure and hormone function.
16834341	0	14	gly	glycopeptide	72:83	arg2	glycopeptide					72:83	glycopeptide analysis	72:92	Comparative glycomics of the glycoprotein follicle stimulating hormone: glycopeptide analysis of isolates from two mammalian species.	0:132	Comparative glycomics of the glycoprotein follicle stimulating hormone: glycopeptide analysis of isolates from two mammalian species.
16834341	9	15	theme	hormone	1366:1372	arg1	function					1374:1381	hormone function	1366:1381	hormone function	1366:1381	This is the first study that characterizes the glycans from this hormone in a glycosylation site-specific manner, and these data can be used to begin correlative studies between glycosylation structure and hormone function.
16834341	0	16	theme	mammalian	115:123	arg1	species					125:131	two mammalian species	111:131	two mammalian species	111:131	Comparative glycomics of the glycoprotein follicle stimulating hormone: glycopeptide analysis of isolates from two mammalian species.
16834341	6	17	theme	other	881:885	arg1	sites					887:891	all other sites	877:891	all other sites in both species	877:907	For instance, except for one site in the beta subunit (Asn7) of hFSH all other sites in both species have sulfated glycoforms.
16834341	8	18	theme	sulfated	1100:1107	arg1	glycans					1109:1115	sulfated glycans	1100:1115	sulfated glycans	1100:1115	There is also a higher percentage of sulfated glycans in the latter site compared to the former.
16834341	4	19	theme	FSH	692:694	arg1	preparations					696:707	human FSH preparations	686:707	human FSH preparations	686:707	The characteristic pattern of glycan distribution at each glycosylation site has been deduced and compared between horse and human FSH preparations.
16834341	3	20	theme	pituitary	404:412	arg1	hormone					435:441	human pituitary follicle stimulating hormone	398:441	human pituitary follicle stimulating hormone (eFSH and hFSH)	398:457	In the present study the negatively charged glycopeptides of equine and human pituitary follicle stimulating hormone (eFSH and hFSH) have been characterized in a glycosylation site-specific manner using FT-ICR-MS and Edman sequencing.
16834341	9	21	theme	site-specific	1252:1264	arg1	manner					1266:1271	a glycosylation site-specific manner	1236:1271	a glycosylation site-specific manner	1236:1271	This is the first study that characterizes the glycans from this hormone in a glycosylation site-specific manner, and these data can be used to begin correlative studies between glycosylation structure and hormone function.
16834341	3	22	theme	follicle	414:421	arg1	hormone					435:441	human pituitary follicle stimulating hormone	398:441	human pituitary follicle stimulating hormone (eFSH and hFSH)	398:457	In the present study the negatively charged glycopeptides of equine and human pituitary follicle stimulating hormone (eFSH and hFSH) have been characterized in a glycosylation site-specific manner using FT-ICR-MS and Edman sequencing.
16834341	3	23	theme	Edman	543:547	arg1	sequencing					549:558	Edman sequencing	543:558	Edman sequencing	543:558	In the present study the negatively charged glycopeptides of equine and human pituitary follicle stimulating hormone (eFSH and hFSH) have been characterized in a glycosylation site-specific manner using FT-ICR-MS and Edman sequencing.
16834341	3	24	theme	charged	362:368	arg1	glycopeptides					370:382	the negatively charged glycopeptides	347:382	the negatively charged glycopeptides of equine and human pituitary follicle stimulating hormone (eFSH and hFSH)	347:457	In the present study the negatively charged glycopeptides of equine and human pituitary follicle stimulating hormone (eFSH and hFSH) have been characterized in a glycosylation site-specific manner using FT-ICR-MS and Edman sequencing.
16834341	6	25	from	sites	887:891	arg1	species					901:907	both species	896:907	both species	896:907	For instance, except for one site in the beta subunit (Asn7) of hFSH all other sites in both species have sulfated glycoforms.
16834341	2	26	gly	glycosylated	251:262	arg1	hormone					240:246	This hormone	235:246	This hormone	235:246	This hormone is glycosylated, and the glycans greatly influence the biological properties.
16834341	6	27	theme	hFSH	872:875	arg1	Asn7					863:866	Asn7	863:866	Asn7	863:866	For instance, except for one site in the beta subunit (Asn7) of hFSH all other sites in both species have sulfated glycoforms.
16834341	6	27	theme	hFSH	872:875	arg1	subunit					854:860	the beta subunit	845:860	the beta subunit (Asn7) of hFSH	845:875	For instance, except for one site in the beta subunit (Asn7) of hFSH all other sites in both species have sulfated glycoforms.
16834341	5	28	theme	human	786:790	arg1	glycoforms					772:781	glycoforms	772:781	glycoforms of human and equine FSH	772:805	The data suggest that site-specific differences exist between glycoforms of human and equine FSH.
16834341	9	29	theme	glycosylation	1238:1250	arg1	manner					1266:1271	a glycosylation site-specific manner	1236:1271	a glycosylation site-specific manner	1236:1271	This is the first study that characterizes the glycans from this hormone in a glycosylation site-specific manner, and these data can be used to begin correlative studies between glycosylation structure and hormone function.
16834341	3	30	theme	hormone	435:441	arg1	glycopeptides					370:382	the negatively charged glycopeptides	347:382	the negatively charged glycopeptides of equine and human pituitary follicle stimulating hormone (eFSH and hFSH)	347:457	In the present study the negatively charged glycopeptides of equine and human pituitary follicle stimulating hormone (eFSH and hFSH) have been characterized in a glycosylation site-specific manner using FT-ICR-MS and Edman sequencing.
16834341	0	31	theme	Comparative	0:10	arg1	glycomics					12:20	Comparative glycomics	0:20	Comparative glycomics of the glycoprotein follicle stimulating hormone: glycopeptide analysis of isolates from two mammalian species.	0:132	Comparative glycomics of the glycoprotein follicle stimulating hormone: glycopeptide analysis of isolates from two mammalian species.
16834341	4	32	theme	characteristic	565:578	arg1	pattern					580:586	The characteristic pattern	561:586	The characteristic pattern of glycan distribution at each glycosylation site	561:636	The characteristic pattern of glycan distribution at each glycosylation site has been deduced and compared between horse and human FSH preparations.
16834341	3	33	gly	glycopeptides	370:382	arg1	equine					387:392	equine	387:392	equine	387:392	In the present study the negatively charged glycopeptides of equine and human pituitary follicle stimulating hormone (eFSH and hFSH) have been characterized in a glycosylation site-specific manner using FT-ICR-MS and Edman sequencing.
16834341	3	33	gly	glycopeptides	370:382	arg2	glycopeptides					370:382	the negatively charged glycopeptides	347:382	the negatively charged glycopeptides of equine and human pituitary follicle stimulating hormone (eFSH and hFSH)	347:457	In the present study the negatively charged glycopeptides of equine and human pituitary follicle stimulating hormone (eFSH and hFSH) have been characterized in a glycosylation site-specific manner using FT-ICR-MS and Edman sequencing.
16834341	3	33	gly	glycopeptides	370:382	arg1	hormone					435:441	human pituitary follicle stimulating hormone	398:441	human pituitary follicle stimulating hormone (eFSH and hFSH)	398:457	In the present study the negatively charged glycopeptides of equine and human pituitary follicle stimulating hormone (eFSH and hFSH) have been characterized in a glycosylation site-specific manner using FT-ICR-MS and Edman sequencing.
16834341	2	34	theme	biological	303:312	arg1	properties					314:323	the biological properties	299:323	the biological properties	299:323	This hormone is glycosylated, and the glycans greatly influence the biological properties.
16834341	4	35	theme	human	686:690	arg1	preparations					696:707	human FSH preparations	686:707	human FSH preparations	686:707	The characteristic pattern of glycan distribution at each glycosylation site has been deduced and compared between horse and human FSH preparations.
16834341	7	36	theme	hybrid	1025:1030	arg1	structures					1032:1041	both complex and hybrid structures	1008:1041	structures	1032:1041	Also, glycoforms at Asn52 of hFSH are all complex type, whereas in eFSH, both complex and hybrid structures exist at this site.
16834341	1	37	theme	important	183:191	arg1	hormones					193:200	the important hormones	179:200	the important hormones	179:200	Follicle stimulating hormone (FSH) is one of the important hormones that regulate gonadal functions.
16834341	8	38	theme	higher	1079:1084	arg1	percentage					1086:1095	a higher percentage	1077:1095	a higher percentage of sulfated glycans in the latter site compared to the former	1077:1157	There is also a higher percentage of sulfated glycans in the latter site compared to the former.
16834341	7	39	theme	complex	1013:1019	arg1	structures					1032:1041	both complex and hybrid structures	1008:1041	structures	1032:1041	Also, glycoforms at Asn52 of hFSH are all complex type, whereas in eFSH, both complex and hybrid structures exist at this site.
16834341	9	40	from	hormone	1225:1231	arg1	glycans					1207:1213	the glycans	1203:1213	the glycans from this hormone	1203:1231	This is the first study that characterizes the glycans from this hormone in a glycosylation site-specific manner, and these data can be used to begin correlative studies between glycosylation structure and hormone function.
16834341	1	41	theme	hormones	193:200	arg1	hormones					193:200	the important hormones	179:200	the important hormones	179:200	Follicle stimulating hormone (FSH) is one of the important hormones that regulate gonadal functions.
16834341	1	41	theme	hormones	193:200	arg1	one					172:174	one	172:174	one	172:174	Follicle stimulating hormone (FSH) is one of the important hormones that regulate gonadal functions.
16834341	0	42	theme	follicle	42:49	arg1	hormone					63:69	the glycoprotein follicle stimulating hormone	25:69	the glycoprotein follicle stimulating hormone	25:69	Comparative glycomics of the glycoprotein follicle stimulating hormone: glycopeptide analysis of isolates from two mammalian species.
16834341	7	43	dep	type	985:988	arg1	whereas					991:997	whereas	991:997	whereas	991:997	Also, glycoforms at Asn52 of hFSH are all complex type, whereas in eFSH, both complex and hybrid structures exist at this site.
16834341	5	44	theme	site-specific	732:744	arg1	differences					746:756	site-specific differences	732:756	site-specific differences	732:756	The data suggest that site-specific differences exist between glycoforms of human and equine FSH.
16834341	0	45	from	analysis	85:92	arg1	species					125:131	two mammalian species	111:131	two mammalian species	111:131	Comparative glycomics of the glycoprotein follicle stimulating hormone: glycopeptide analysis of isolates from two mammalian species.
16834341	3	46	dep	hormone	435:441	arg1	eFSH					444:447	eFSH	444:447	eFSH	444:447	In the present study the negatively charged glycopeptides of equine and human pituitary follicle stimulating hormone (eFSH and hFSH) have been characterized in a glycosylation site-specific manner using FT-ICR-MS and Edman sequencing.
16834341	3	46	dep	hormone	435:441	arg1	hFSH					453:456	hFSH	453:456	hFSH	453:456	In the present study the negatively charged glycopeptides of equine and human pituitary follicle stimulating hormone (eFSH and hFSH) have been characterized in a glycosylation site-specific manner using FT-ICR-MS and Edman sequencing.
16834341	6	47	contain	have	909:912	arg1	sites					887:891	all other sites	877:891	all other sites in both species	877:907	For instance, except for one site in the beta subunit (Asn7) of hFSH all other sites in both species have sulfated glycoforms.
16834341	6	47	contain	have	909:912	arg2	glycoforms					923:932	sulfated glycoforms	914:932	sulfated glycoforms	914:932	For instance, except for one site in the beta subunit (Asn7) of hFSH all other sites in both species have sulfated glycoforms.
16834341	0	48	theme	glycoprotein	29:40	arg1	hormone					63:69	the glycoprotein follicle stimulating hormone	25:69	the glycoprotein follicle stimulating hormone	25:69	Comparative glycomics of the glycoprotein follicle stimulating hormone: glycopeptide analysis of isolates from two mammalian species.
16834341	3	49	theme	stimulating	423:433	arg1	hormone					435:441	human pituitary follicle stimulating hormone	398:441	human pituitary follicle stimulating hormone (eFSH and hFSH)	398:457	In the present study the negatively charged glycopeptides of equine and human pituitary follicle stimulating hormone (eFSH and hFSH) have been characterized in a glycosylation site-specific manner using FT-ICR-MS and Edman sequencing.
16834341	9	50	theme	first	1172:1176	arg1	study					1178:1182	the first study	1168:1182	the first study that characterizes the glycans from this hormone in a glycosylation site-specific manner	1168:1271	This is the first study that characterizes the glycans from this hormone in a glycosylation site-specific manner, and these data can be used to begin correlative studies between glycosylation structure and hormone function.
16834341	9	50	theme	first	1172:1176	arg1	This					1160:1163	This	1160:1163	This	1160:1163	This is the first study that characterizes the glycans from this hormone in a glycosylation site-specific manner, and these data can be used to begin correlative studies between glycosylation structure and hormone function.
16834341	9	51	theme	glycosylation	1338:1350	arg1	structure					1352:1360	glycosylation structure	1338:1360	glycosylation structure	1338:1360	This is the first study that characterizes the glycans from this hormone in a glycosylation site-specific manner, and these data can be used to begin correlative studies between glycosylation structure and hormone function.
16834341	0	52	theme	hormone	63:69	arg1	glycomics					12:20	Comparative glycomics	0:20	Comparative glycomics of the glycoprotein follicle stimulating hormone: glycopeptide analysis of isolates from two mammalian species.	0:132	Comparative glycomics of the glycoprotein follicle stimulating hormone: glycopeptide analysis of isolates from two mammalian species.
16834341	3	53	theme	present	333:339	arg1	study					341:345	the present study	329:345	the present study	329:345	In the present study the negatively charged glycopeptides of equine and human pituitary follicle stimulating hormone (eFSH and hFSH) have been characterized in a glycosylation site-specific manner using FT-ICR-MS and Edman sequencing.
16834341	0	54	theme	stimulating	51:61	arg1	hormone					63:69	the glycoprotein follicle stimulating hormone	25:69	the glycoprotein follicle stimulating hormone	25:69	Comparative glycomics of the glycoprotein follicle stimulating hormone: glycopeptide analysis of isolates from two mammalian species.
16834341	9	55	theme	correlative	1310:1320	arg1	studies					1322:1328	correlative studies	1310:1328	correlative studies between glycosylation structure and hormone function	1310:1381	This is the first study that characterizes the glycans from this hormone in a glycosylation site-specific manner, and these data can be used to begin correlative studies between glycosylation structure and hormone function.
16834341	7	56	theme	complex	977:983	arg1	type					985:988	all complex type	973:988	all complex type	973:988	Also, glycoforms at Asn52 of hFSH are all complex type, whereas in eFSH, both complex and hybrid structures exist at this site.
16834341	7	56	theme	complex	977:983	arg1	glycoforms					941:950	glycoforms	941:950	glycoforms at Asn52 of hFSH	941:967	Also, glycoforms at Asn52 of hFSH are all complex type, whereas in eFSH, both complex and hybrid structures exist at this site.
16834341	3	57	theme	glycosylation	488:500	arg1	manner					516:521	a glycosylation site-specific manner	486:521	a glycosylation site-specific manner using FT-ICR-MS and Edman sequencing	486:558	In the present study the negatively charged glycopeptides of equine and human pituitary follicle stimulating hormone (eFSH and hFSH) have been characterized in a glycosylation site-specific manner using FT-ICR-MS and Edman sequencing.
16834341	6	58	theme	sulfated	914:921	arg1	glycoforms					923:932	sulfated glycoforms	914:932	sulfated glycoforms	914:932	For instance, except for one site in the beta subunit (Asn7) of hFSH all other sites in both species have sulfated glycoforms.
16834341	6	59	theme	beta	849:852	arg1	Asn7					863:866	Asn7	863:866	Asn7	863:866	For instance, except for one site in the beta subunit (Asn7) of hFSH all other sites in both species have sulfated glycoforms.
16834341	6	59	theme	beta	849:852	arg1	subunit					854:860	the beta subunit	845:860	the beta subunit (Asn7) of hFSH	845:875	For instance, except for one site in the beta subunit (Asn7) of hFSH all other sites in both species have sulfated glycoforms.
16834341	0	60	gly	glycoprotein	29:40	arg1	glycoprotein					29:40	the glycoprotein follicle stimulating hormone	25:69	the glycoprotein follicle stimulating hormone	25:69	Comparative glycomics of the glycoprotein follicle stimulating hormone: glycopeptide analysis of isolates from two mammalian species.
16834341	1	61	theme	Follicle	134:141	arg1	FSH					164:166	FSH	164:166	FSH	164:166	Follicle stimulating hormone (FSH) is one of the important hormones that regulate gonadal functions.
16834341	1	61	theme	Follicle	134:141	arg1	hormone					155:161	Follicle stimulating hormone	134:161	Follicle stimulating hormone (FSH)	134:167	Follicle stimulating hormone (FSH) is one of the important hormones that regulate gonadal functions.
16834341	1	62	theme	gonadal	216:222	arg1	functions					224:232	gonadal functions	216:232	gonadal functions	216:232	Follicle stimulating hormone (FSH) is one of the important hormones that regulate gonadal functions.
16834341	8	63	theme	latter	1124:1129	arg1	site					1131:1134	the latter site	1120:1134	the latter site compared to the former	1120:1157	There is also a higher percentage of sulfated glycans in the latter site compared to the former.
16834341	1	64	theme	stimulating	143:153	arg1	FSH					164:166	FSH	164:166	FSH	164:166	Follicle stimulating hormone (FSH) is one of the important hormones that regulate gonadal functions.
16834341	1	64	theme	stimulating	143:153	arg1	hormone					155:161	Follicle stimulating hormone	134:161	Follicle stimulating hormone (FSH)	134:167	Follicle stimulating hormone (FSH) is one of the important hormones that regulate gonadal functions.
16834341	4	65	theme	glycosylation	619:631	arg1	site					633:636	each glycosylation site	614:636	each glycosylation site	614:636	The characteristic pattern of glycan distribution at each glycosylation site has been deduced and compared between horse and human FSH preparations.
16834341	0	66	theme	glycopeptide	72:83	arg1	analysis					85:92	glycopeptide analysis	72:92	Comparative glycomics of the glycoprotein follicle stimulating hormone: glycopeptide analysis of isolates from two mammalian species.	0:132	Comparative glycomics of the glycoprotein follicle stimulating hormone: glycopeptide analysis of isolates from two mammalian species.
16834341	0	67	dep	glycomics	12:20	arg1	analysis					85:92	glycopeptide analysis	72:92	Comparative glycomics of the glycoprotein follicle stimulating hormone: glycopeptide analysis of isolates from two mammalian species.	0:132	Comparative glycomics of the glycoprotein follicle stimulating hormone: glycopeptide analysis of isolates from two mammalian species.
16834341	3	68	theme	human	398:402	arg1	hormone					435:441	human pituitary follicle stimulating hormone	398:441	human pituitary follicle stimulating hormone (eFSH and hFSH)	398:457	In the present study the negatively charged glycopeptides of equine and human pituitary follicle stimulating hormone (eFSH and hFSH) have been characterized in a glycosylation site-specific manner using FT-ICR-MS and Edman sequencing.
16834341	5	69	dep	human	786:790	arg1	FSH					803:805	FSH	803:805	FSH	803:805	The data suggest that site-specific differences exist between glycoforms of human and equine FSH.
16834341	3	70	theme	equine	387:392	arg1	glycopeptides					370:382	the negatively charged glycopeptides	347:382	the negatively charged glycopeptides of equine and human pituitary follicle stimulating hormone (eFSH and hFSH)	347:457	In the present study the negatively charged glycopeptides of equine and human pituitary follicle stimulating hormone (eFSH and hFSH) have been characterized in a glycosylation site-specific manner using FT-ICR-MS and Edman sequencing.
16834341	0	71	from	species	125:131	arg1	analysis					85:92	glycopeptide analysis	72:92	Comparative glycomics of the glycoprotein follicle stimulating hormone: glycopeptide analysis of isolates from two mammalian species.	0:132	Comparative glycomics of the glycoprotein follicle stimulating hormone: glycopeptide analysis of isolates from two mammalian species.
16834341	0	71	from	species	125:131	arg1	isolates					97:104	isolates	97:104	isolates from two mammalian species	97:131	Comparative glycomics of the glycoprotein follicle stimulating hormone: glycopeptide analysis of isolates from two mammalian species.
7780197	8	0	theme	oligosaccharides	1396:1411	arg1	fraction					1380:1387	a fraction	1378:1387	a fraction of the oligosaccharides	1378:1411	Mass spectrometry confirmed these observations, but also showed the presence of an 80 Da anionic moiety on a fraction of the oligosaccharides.
7780197	6	1	theme	high-pH	949:955	arg1	chromatography					972:985	high-pH anion-exchange chromatography	949:985	high-pH anion-exchange chromatography with pulsed amperometric detection (HPAE-PAD)	949:1031	Glycosylation of Asn-727 found in the TfR purified from human placentae was analysed by high-pH anion-exchange chromatography with pulsed amperometric detection (HPAE-PAD) and mass spectrometry following tryptic digestion, peptide purification via reverse-phase high-performance liquid chromatography (RP-HPLC) and peptide sequencing.
7780197	1	2	gly	glycosylation	185:197	arg1	molecule					254:261	the molecule	250:261	the molecule	250:261	The human transferrin receptor (TfR) contains three N-linked oligosaccharides and glycosylation is required for the proper folding and function of the molecule.
7780197	1	3	theme	N-linked	155:162	arg1	oligosaccharides					164:179	three N-linked oligosaccharides	149:179	three N-linked oligosaccharides	149:179	The human transferrin receptor (TfR) contains three N-linked oligosaccharides and glycosylation is required for the proper folding and function of the molecule.
7780197	1	4	theme	molecule	254:261	arg1	function					238:245	function	238:245	function	238:245	The human transferrin receptor (TfR) contains three N-linked oligosaccharides and glycosylation is required for the proper folding and function of the molecule.
7780197	1	4	theme	molecule	254:261	arg1	folding					226:232	folding	226:232	folding	226:232	The human transferrin receptor (TfR) contains three N-linked oligosaccharides and glycosylation is required for the proper folding and function of the molecule.
7780197	0	5	theme	high-mannose	73:84	arg1	oligosaccharide					86:100	a high-mannose oligosaccharide	71:100	a high-mannose oligosaccharide	71:100	The critical glycosylation site of human transferrin receptor contains a high-mannose oligosaccharide.
7780197	5	6	contain	contains	794:801	arg1	site					789:792	the Asn-727 site	777:792	the Asn-727 site	777:792	These studies suggested that the Asn-727 site contains high-mannose or Endo-H-sensitive hybrid oligosaccharides.
7780197	5	6	contain	contains	794:801	arg2	oligosaccharides					843:858	high-mannose or Endo-H-sensitive hybrid oligosaccharides	803:858	high-mannose or Endo-H-sensitive hybrid oligosaccharides	803:858	These studies suggested that the Asn-727 site contains high-mannose or Endo-H-sensitive hybrid oligosaccharides.
7780197	4	7	theme	Endo-H	700:705	arg1	immunoblotting					732:745	immunoblotting	732:745	immunoblotting	732:745	Wild-type TfR and mutants containing only the Asn-727 site or missing all three sites were transfected into mouse 3T3 cells and receptors were analysed by endo-N-acetylglucosaminidase H (Endo-H) digestion, SDS-PAGE and immunoblotting.
7780197	4	7	theme	Endo-H	700:705	arg1	SDS-PAGE					719:726	SDS-PAGE	719:726	SDS-PAGE	719:726	Wild-type TfR and mutants containing only the Asn-727 site or missing all three sites were transfected into mouse 3T3 cells and receptors were analysed by endo-N-acetylglucosaminidase H (Endo-H) digestion, SDS-PAGE and immunoblotting.
7780197	4	7	theme	Endo-H	700:705	arg1	digestion					708:716	endo-N-acetylglucosaminidase H (Endo-H) digestion	668:716	endo-N-acetylglucosaminidase H (Endo-H) digestion	668:716	Wild-type TfR and mutants containing only the Asn-727 site or missing all three sites were transfected into mouse 3T3 cells and receptors were analysed by endo-N-acetylglucosaminidase H (Endo-H) digestion, SDS-PAGE and immunoblotting.
7780197	2	8	theme	Earlier	264:270	arg1	studies					272:278	Earlier studies	264:278	Earlier studies	264:278	Earlier studies demonstrated that the oligosaccharide at Asn-727 is vital for the production of fully active TfR.
7780197	2	9	theme	oligosaccharide	302:316	arg1	Asn-727					321:327	the oligosaccharide at Asn-727	298:327	the oligosaccharide at Asn-727	298:327	Earlier studies demonstrated that the oligosaccharide at Asn-727 is vital for the production of fully active TfR.
7780197	2	9	theme	oligosaccharide	302:316	arg1	vital					332:336	vital	332:336	vital	332:336	Earlier studies demonstrated that the oligosaccharide at Asn-727 is vital for the production of fully active TfR.
7780197	2	10	theme	at	318:319	arg1	Asn-727					321:327	the oligosaccharide at Asn-727	298:327	the oligosaccharide at Asn-727	298:327	Earlier studies demonstrated that the oligosaccharide at Asn-727 is vital for the production of fully active TfR.
7780197	2	10	theme	at	318:319	arg1	vital					332:336	vital	332:336	vital	332:336	Earlier studies demonstrated that the oligosaccharide at Asn-727 is vital for the production of fully active TfR.
7780197	6	11	theme	mass	1037:1040	arg1	spectrometry					1042:1053	mass spectrometry	1037:1053	mass spectrometry	1037:1053	Glycosylation of Asn-727 found in the TfR purified from human placentae was analysed by high-pH anion-exchange chromatography with pulsed amperometric detection (HPAE-PAD) and mass spectrometry following tryptic digestion, peptide purification via reverse-phase high-performance liquid chromatography (RP-HPLC) and peptide sequencing.
7780197	2	12	theme	active	366:371	arg1	TfR					373:375	fully active TfR	360:375	fully active TfR	360:375	Earlier studies demonstrated that the oligosaccharide at Asn-727 is vital for the production of fully active TfR.
7780197	7	13	theme	high-mannose	1240:1251	arg1	oligosaccharides					1253:1268	high-mannose oligosaccharides	1240:1268	high-mannose oligosaccharides	1240:1268	HPAE-PAD showed the presence of a series of high-mannose oligosaccharides.
7780197	5	14	theme	Endo-H-sensitive	819:834	arg1	oligosaccharides					843:858	high-mannose or Endo-H-sensitive hybrid oligosaccharides	803:858	high-mannose or Endo-H-sensitive hybrid oligosaccharides	803:858	These studies suggested that the Asn-727 site contains high-mannose or Endo-H-sensitive hybrid oligosaccharides.
7780197	6	15	theme	reverse-phase	1109:1121	arg1	chromatography					1147:1160	reverse-phase high-performance liquid chromatography	1109:1160	reverse-phase high-performance liquid chromatography (RP-HPLC)	1109:1170	Glycosylation of Asn-727 found in the TfR purified from human placentae was analysed by high-pH anion-exchange chromatography with pulsed amperometric detection (HPAE-PAD) and mass spectrometry following tryptic digestion, peptide purification via reverse-phase high-performance liquid chromatography (RP-HPLC) and peptide sequencing.
7780197	6	15	theme	reverse-phase	1109:1121	arg1	RP-HPLC					1163:1169	RP-HPLC	1163:1169	RP-HPLC	1163:1169	Glycosylation of Asn-727 found in the TfR purified from human placentae was analysed by high-pH anion-exchange chromatography with pulsed amperometric detection (HPAE-PAD) and mass spectrometry following tryptic digestion, peptide purification via reverse-phase high-performance liquid chromatography (RP-HPLC) and peptide sequencing.
7780197	3	16	theme	present	401:407	arg1	s					398:398	The oligosaccharide(s)	378:399	The oligosaccharide(s) present at this site	378:420	The oligosaccharide(s) present at this site have been analysed using a combination of site-directed mutagenesis and chemical analysis.
7780197	6	17	theme	human	917:921	arg1	placentae					923:931	human placentae	917:931	human placentae	917:931	Glycosylation of Asn-727 found in the TfR purified from human placentae was analysed by high-pH anion-exchange chromatography with pulsed amperometric detection (HPAE-PAD) and mass spectrometry following tryptic digestion, peptide purification via reverse-phase high-performance liquid chromatography (RP-HPLC) and peptide sequencing.
7780197	8	18	theme	Mass	1271:1274	arg1	spectrometry					1276:1287	Mass spectrometry	1271:1287	Mass spectrometry	1271:1287	Mass spectrometry confirmed these observations, but also showed the presence of an 80 Da anionic moiety on a fraction of the oligosaccharides.
7780197	6	19	gly	Glycosylation	861:873	arg1	Asn-727					878:884	Asn-727	878:884	Asn-727 found in the TfR purified from human placentae	878:931	Glycosylation of Asn-727 found in the TfR purified from human placentae was analysed by high-pH anion-exchange chromatography with pulsed amperometric detection (HPAE-PAD) and mass spectrometry following tryptic digestion, peptide purification via reverse-phase high-performance liquid chromatography (RP-HPLC) and peptide sequencing.
7780197	0	20	theme	critical	4:11	arg1	site					27:30	The critical glycosylation site	0:30	The critical glycosylation site of human transferrin receptor	0:60	The critical glycosylation site of human transferrin receptor contains a high-mannose oligosaccharide.
7780197	0	20	theme	critical	4:11	arg1	receptor					53:60	human transferrin receptor	35:60	human transferrin receptor	35:60	The critical glycosylation site of human transferrin receptor contains a high-mannose oligosaccharide.
7780197	1	21	contain	contains	140:147	arg2	oligosaccharides					164:179	three N-linked oligosaccharides	149:179	three N-linked oligosaccharides	149:179	The human transferrin receptor (TfR) contains three N-linked oligosaccharides and glycosylation is required for the proper folding and function of the molecule.
7780197	1	21	contain	contains	140:147	arg1	TfR					135:137	TfR	135:137	TfR	135:137	The human transferrin receptor (TfR) contains three N-linked oligosaccharides and glycosylation is required for the proper folding and function of the molecule.
7780197	1	21	contain	contains	140:147	arg1	receptor					125:132	The human transferrin receptor	103:132	The human transferrin receptor (TfR)	103:138	The human transferrin receptor (TfR) contains three N-linked oligosaccharides and glycosylation is required for the proper folding and function of the molecule.
7780197	7	22	theme	oligosaccharides	1253:1268	arg1	series					1230:1235	a series	1228:1235	a series of high-mannose oligosaccharides	1228:1268	HPAE-PAD showed the presence of a series of high-mannose oligosaccharides.
7780197	4	23	theme	endo-N-acetylglucosaminidase	668:695	arg1	immunoblotting					732:745	immunoblotting	732:745	immunoblotting	732:745	Wild-type TfR and mutants containing only the Asn-727 site or missing all three sites were transfected into mouse 3T3 cells and receptors were analysed by endo-N-acetylglucosaminidase H (Endo-H) digestion, SDS-PAGE and immunoblotting.
7780197	4	23	theme	endo-N-acetylglucosaminidase	668:695	arg1	SDS-PAGE					719:726	SDS-PAGE	719:726	SDS-PAGE	719:726	Wild-type TfR and mutants containing only the Asn-727 site or missing all three sites were transfected into mouse 3T3 cells and receptors were analysed by endo-N-acetylglucosaminidase H (Endo-H) digestion, SDS-PAGE and immunoblotting.
7780197	4	23	theme	endo-N-acetylglucosaminidase	668:695	arg1	digestion					708:716	endo-N-acetylglucosaminidase H (Endo-H) digestion	668:716	endo-N-acetylglucosaminidase H (Endo-H) digestion	668:716	Wild-type TfR and mutants containing only the Asn-727 site or missing all three sites were transfected into mouse 3T3 cells and receptors were analysed by endo-N-acetylglucosaminidase H (Endo-H) digestion, SDS-PAGE and immunoblotting.
7780197	5	24	theme	hybrid	836:841	arg1	oligosaccharides					843:858	high-mannose or Endo-H-sensitive hybrid oligosaccharides	803:858	high-mannose or Endo-H-sensitive hybrid oligosaccharides	803:858	These studies suggested that the Asn-727 site contains high-mannose or Endo-H-sensitive hybrid oligosaccharides.
7780197	4	25	theme	Asn-727	559:565	arg1	site					567:570	only the Asn-727 site	550:570	only the Asn-727 site	550:570	Wild-type TfR and mutants containing only the Asn-727 site or missing all three sites were transfected into mouse 3T3 cells and receptors were analysed by endo-N-acetylglucosaminidase H (Endo-H) digestion, SDS-PAGE and immunoblotting.
7780197	6	26	with	chromatography	972:985	arg1	HPAE-PAD					1023:1030	HPAE-PAD	1023:1030	HPAE-PAD	1023:1030	Glycosylation of Asn-727 found in the TfR purified from human placentae was analysed by high-pH anion-exchange chromatography with pulsed amperometric detection (HPAE-PAD) and mass spectrometry following tryptic digestion, peptide purification via reverse-phase high-performance liquid chromatography (RP-HPLC) and peptide sequencing.
7780197	6	26	with	chromatography	972:985	arg1	detection					1012:1020	pulsed amperometric detection	992:1020	pulsed amperometric detection (HPAE-PAD)	992:1031	Glycosylation of Asn-727 found in the TfR purified from human placentae was analysed by high-pH anion-exchange chromatography with pulsed amperometric detection (HPAE-PAD) and mass spectrometry following tryptic digestion, peptide purification via reverse-phase high-performance liquid chromatography (RP-HPLC) and peptide sequencing.
7780197	6	27	theme	liquid	1140:1145	arg1	chromatography					1147:1160	reverse-phase high-performance liquid chromatography	1109:1160	reverse-phase high-performance liquid chromatography (RP-HPLC)	1109:1170	Glycosylation of Asn-727 found in the TfR purified from human placentae was analysed by high-pH anion-exchange chromatography with pulsed amperometric detection (HPAE-PAD) and mass spectrometry following tryptic digestion, peptide purification via reverse-phase high-performance liquid chromatography (RP-HPLC) and peptide sequencing.
7780197	6	27	theme	liquid	1140:1145	arg1	RP-HPLC					1163:1169	RP-HPLC	1163:1169	RP-HPLC	1163:1169	Glycosylation of Asn-727 found in the TfR purified from human placentae was analysed by high-pH anion-exchange chromatography with pulsed amperometric detection (HPAE-PAD) and mass spectrometry following tryptic digestion, peptide purification via reverse-phase high-performance liquid chromatography (RP-HPLC) and peptide sequencing.
7780197	1	28	link	N-linked	155:162	arg1	oligosaccharides					164:179	three N-linked oligosaccharides	149:179	three N-linked oligosaccharides	149:179	The human transferrin receptor (TfR) contains three N-linked oligosaccharides and glycosylation is required for the proper folding and function of the molecule.
7780197	1	29	theme	human	107:111	arg1	TfR					135:137	TfR	135:137	TfR	135:137	The human transferrin receptor (TfR) contains three N-linked oligosaccharides and glycosylation is required for the proper folding and function of the molecule.
7780197	1	29	theme	human	107:111	arg1	receptor					125:132	The human transferrin receptor	103:132	The human transferrin receptor (TfR)	103:138	The human transferrin receptor (TfR) contains three N-linked oligosaccharides and glycosylation is required for the proper folding and function of the molecule.
7780197	6	30	theme	high-performance	1123:1138	arg1	chromatography					1147:1160	reverse-phase high-performance liquid chromatography	1109:1160	reverse-phase high-performance liquid chromatography (RP-HPLC)	1109:1170	Glycosylation of Asn-727 found in the TfR purified from human placentae was analysed by high-pH anion-exchange chromatography with pulsed amperometric detection (HPAE-PAD) and mass spectrometry following tryptic digestion, peptide purification via reverse-phase high-performance liquid chromatography (RP-HPLC) and peptide sequencing.
7780197	6	30	theme	high-performance	1123:1138	arg1	RP-HPLC					1163:1169	RP-HPLC	1163:1169	RP-HPLC	1163:1169	Glycosylation of Asn-727 found in the TfR purified from human placentae was analysed by high-pH anion-exchange chromatography with pulsed amperometric detection (HPAE-PAD) and mass spectrometry following tryptic digestion, peptide purification via reverse-phase high-performance liquid chromatography (RP-HPLC) and peptide sequencing.
7780197	0	31	theme	glycosylation	13:25	arg1	site					27:30	The critical glycosylation site	0:30	The critical glycosylation site of human transferrin receptor	0:60	The critical glycosylation site of human transferrin receptor contains a high-mannose oligosaccharide.
7780197	0	31	theme	glycosylation	13:25	arg1	receptor					53:60	human transferrin receptor	35:60	human transferrin receptor	35:60	The critical glycosylation site of human transferrin receptor contains a high-mannose oligosaccharide.
7780197	1	32	theme	transferrin	113:123	arg1	TfR					135:137	TfR	135:137	TfR	135:137	The human transferrin receptor (TfR) contains three N-linked oligosaccharides and glycosylation is required for the proper folding and function of the molecule.
7780197	1	32	theme	transferrin	113:123	arg1	receptor					125:132	The human transferrin receptor	103:132	The human transferrin receptor (TfR)	103:138	The human transferrin receptor (TfR) contains three N-linked oligosaccharides and glycosylation is required for the proper folding and function of the molecule.
7780197	4	33	theme	3T3	627:629	arg1	cells					631:635	mouse 3T3 cells	621:635	mouse 3T3 cells	621:635	Wild-type TfR and mutants containing only the Asn-727 site or missing all three sites were transfected into mouse 3T3 cells and receptors were analysed by endo-N-acetylglucosaminidase H (Endo-H) digestion, SDS-PAGE and immunoblotting.
7780197	0	34	theme	human	35:39	arg1	receptor					53:60	human transferrin receptor	35:60	human transferrin receptor	35:60	The critical glycosylation site of human transferrin receptor contains a high-mannose oligosaccharide.
7780197	6	35	located	found	886:890	arg1	TfR					899:901	the TfR	895:901	the TfR purified from human placentae	895:931	Glycosylation of Asn-727 found in the TfR purified from human placentae was analysed by high-pH anion-exchange chromatography with pulsed amperometric detection (HPAE-PAD) and mass spectrometry following tryptic digestion, peptide purification via reverse-phase high-performance liquid chromatography (RP-HPLC) and peptide sequencing.
7780197	6	35	located	found	886:890	arg2	Asn-727					878:884	Asn-727	878:884	Asn-727 found in the TfR purified from human placentae	878:931	Glycosylation of Asn-727 found in the TfR purified from human placentae was analysed by high-pH anion-exchange chromatography with pulsed amperometric detection (HPAE-PAD) and mass spectrometry following tryptic digestion, peptide purification via reverse-phase high-performance liquid chromatography (RP-HPLC) and peptide sequencing.
7780197	8	36	theme	anionic	1360:1366	arg1	moiety					1368:1373	an 80 Da anionic moiety	1351:1373	an 80 Da anionic moiety	1351:1373	Mass spectrometry confirmed these observations, but also showed the presence of an 80 Da anionic moiety on a fraction of the oligosaccharides.
7780197	8	37	theme	moiety	1368:1373	arg1	presence					1339:1346	the presence	1335:1346	the presence of an 80 Da anionic moiety	1335:1373	Mass spectrometry confirmed these observations, but also showed the presence of an 80 Da anionic moiety on a fraction of the oligosaccharides.
7780197	1	38	theme	proper	219:224	arg1	folding					226:232	folding	226:232	folding	226:232	The human transferrin receptor (TfR) contains three N-linked oligosaccharides and glycosylation is required for the proper folding and function of the molecule.
7780197	7	39	theme	series	1230:1235	arg1	presence					1216:1223	the presence	1212:1223	the presence of a series of high-mannose oligosaccharides	1212:1268	HPAE-PAD showed the presence of a series of high-mannose oligosaccharides.
7780197	4	40	dep	TfR	523:525	arg1	containing					539:548	containing	539:548	containing only the Asn-727 site	539:570	Wild-type TfR and mutants containing only the Asn-727 site or missing all three sites were transfected into mouse 3T3 cells and receptors were analysed by endo-N-acetylglucosaminidase H (Endo-H) digestion, SDS-PAGE and immunoblotting.
7780197	4	40	dep	TfR	523:525	arg1	missing					575:581	missing	575:581	missing all three sites	575:597	Wild-type TfR and mutants containing only the Asn-727 site or missing all three sites were transfected into mouse 3T3 cells and receptors were analysed by endo-N-acetylglucosaminidase H (Endo-H) digestion, SDS-PAGE and immunoblotting.
7780197	3	41	attach	present	401:407	arg1	site					417:420	this site	412:420	this site	412:420	The oligosaccharide(s) present at this site have been analysed using a combination of site-directed mutagenesis and chemical analysis.
7780197	3	41	attach	present	401:407	arg2	s					398:398	The oligosaccharide(s)	378:399	The oligosaccharide(s) present at this site	378:420	The oligosaccharide(s) present at this site have been analysed using a combination of site-directed mutagenesis and chemical analysis.
7780197	8	42	theme	Da	1357:1358	arg1	moiety					1368:1373	an 80 Da anionic moiety	1351:1373	an 80 Da anionic moiety	1351:1373	Mass spectrometry confirmed these observations, but also showed the presence of an 80 Da anionic moiety on a fraction of the oligosaccharides.
7780197	0	43	theme	receptor	53:60	arg1	site					27:30	The critical glycosylation site	0:30	The critical glycosylation site of human transferrin receptor	0:60	The critical glycosylation site of human transferrin receptor contains a high-mannose oligosaccharide.
7780197	0	43	theme	receptor	53:60	arg1	receptor					53:60	human transferrin receptor	35:60	human transferrin receptor	35:60	The critical glycosylation site of human transferrin receptor contains a high-mannose oligosaccharide.
7780197	3	44	theme	analysis	503:510	arg1	combination					449:459	a combination	447:459	a combination of site-directed mutagenesis and chemical analysis	447:510	The oligosaccharide(s) present at this site have been analysed using a combination of site-directed mutagenesis and chemical analysis.
7780197	0	45	gly	glycosylation	13:25	arg2	receptor					53:60	human transferrin receptor	35:60	human transferrin receptor	35:60	The critical glycosylation site of human transferrin receptor contains a high-mannose oligosaccharide.
7780197	0	45	gly	glycosylation	13:25	arg2	site					27:30	The critical glycosylation site	0:30	The critical glycosylation site of human transferrin receptor	0:60	The critical glycosylation site of human transferrin receptor contains a high-mannose oligosaccharide.
7780197	0	45	gly	glycosylation	13:25	arg1	receptor					53:60	human transferrin receptor	35:60	human transferrin receptor	35:60	The critical glycosylation site of human transferrin receptor contains a high-mannose oligosaccharide.
7780197	0	46	theme	transferrin	41:51	arg1	receptor					53:60	human transferrin receptor	35:60	human transferrin receptor	35:60	The critical glycosylation site of human transferrin receptor contains a high-mannose oligosaccharide.
7780197	3	47	theme	chemical	494:501	arg1	analysis					503:510	chemical analysis	494:510	chemical analysis	494:510	The oligosaccharide(s) present at this site have been analysed using a combination of site-directed mutagenesis and chemical analysis.
7780197	6	48	with	spectrometry	1042:1053	arg1	HPAE-PAD					1023:1030	HPAE-PAD	1023:1030	HPAE-PAD	1023:1030	Glycosylation of Asn-727 found in the TfR purified from human placentae was analysed by high-pH anion-exchange chromatography with pulsed amperometric detection (HPAE-PAD) and mass spectrometry following tryptic digestion, peptide purification via reverse-phase high-performance liquid chromatography (RP-HPLC) and peptide sequencing.
7780197	6	48	with	spectrometry	1042:1053	arg1	detection					1012:1020	pulsed amperometric detection	992:1020	pulsed amperometric detection (HPAE-PAD)	992:1031	Glycosylation of Asn-727 found in the TfR purified from human placentae was analysed by high-pH anion-exchange chromatography with pulsed amperometric detection (HPAE-PAD) and mass spectrometry following tryptic digestion, peptide purification via reverse-phase high-performance liquid chromatography (RP-HPLC) and peptide sequencing.
7780197	6	49	theme	amperometric	999:1010	arg1	HPAE-PAD					1023:1030	HPAE-PAD	1023:1030	HPAE-PAD	1023:1030	Glycosylation of Asn-727 found in the TfR purified from human placentae was analysed by high-pH anion-exchange chromatography with pulsed amperometric detection (HPAE-PAD) and mass spectrometry following tryptic digestion, peptide purification via reverse-phase high-performance liquid chromatography (RP-HPLC) and peptide sequencing.
7780197	6	49	theme	amperometric	999:1010	arg1	detection					1012:1020	pulsed amperometric detection	992:1020	pulsed amperometric detection (HPAE-PAD)	992:1031	Glycosylation of Asn-727 found in the TfR purified from human placentae was analysed by high-pH anion-exchange chromatography with pulsed amperometric detection (HPAE-PAD) and mass spectrometry following tryptic digestion, peptide purification via reverse-phase high-performance liquid chromatography (RP-HPLC) and peptide sequencing.
7780197	6	50	theme	Asn-727	878:884	arg1	Glycosylation					861:873	Glycosylation	861:873	Glycosylation of Asn-727 found in the TfR purified from human placentae	861:931	Glycosylation of Asn-727 found in the TfR purified from human placentae was analysed by high-pH anion-exchange chromatography with pulsed amperometric detection (HPAE-PAD) and mass spectrometry following tryptic digestion, peptide purification via reverse-phase high-performance liquid chromatography (RP-HPLC) and peptide sequencing.
7780197	4	51	theme	H	697:697	arg1	immunoblotting					732:745	immunoblotting	732:745	immunoblotting	732:745	Wild-type TfR and mutants containing only the Asn-727 site or missing all three sites were transfected into mouse 3T3 cells and receptors were analysed by endo-N-acetylglucosaminidase H (Endo-H) digestion, SDS-PAGE and immunoblotting.
7780197	4	51	theme	H	697:697	arg1	SDS-PAGE					719:726	SDS-PAGE	719:726	SDS-PAGE	719:726	Wild-type TfR and mutants containing only the Asn-727 site or missing all three sites were transfected into mouse 3T3 cells and receptors were analysed by endo-N-acetylglucosaminidase H (Endo-H) digestion, SDS-PAGE and immunoblotting.
7780197	4	51	theme	H	697:697	arg1	digestion					708:716	endo-N-acetylglucosaminidase H (Endo-H) digestion	668:716	endo-N-acetylglucosaminidase H (Endo-H) digestion	668:716	Wild-type TfR and mutants containing only the Asn-727 site or missing all three sites were transfected into mouse 3T3 cells and receptors were analysed by endo-N-acetylglucosaminidase H (Endo-H) digestion, SDS-PAGE and immunoblotting.
7780197	3	52	theme	site-directed	464:476	arg1	mutagenesis					478:488	site-directed mutagenesis	464:488	site-directed mutagenesis	464:488	The oligosaccharide(s) present at this site have been analysed using a combination of site-directed mutagenesis and chemical analysis.
7780197	6	53	theme	peptide	1084:1090	arg1	purification					1092:1103	peptide purification	1084:1103	peptide purification via reverse-phase high-performance liquid chromatography (RP-HPLC)	1084:1170	Glycosylation of Asn-727 found in the TfR purified from human placentae was analysed by high-pH anion-exchange chromatography with pulsed amperometric detection (HPAE-PAD) and mass spectrometry following tryptic digestion, peptide purification via reverse-phase high-performance liquid chromatography (RP-HPLC) and peptide sequencing.
7780197	6	54	theme	pulsed	992:997	arg1	HPAE-PAD					1023:1030	HPAE-PAD	1023:1030	HPAE-PAD	1023:1030	Glycosylation of Asn-727 found in the TfR purified from human placentae was analysed by high-pH anion-exchange chromatography with pulsed amperometric detection (HPAE-PAD) and mass spectrometry following tryptic digestion, peptide purification via reverse-phase high-performance liquid chromatography (RP-HPLC) and peptide sequencing.
7780197	6	54	theme	pulsed	992:997	arg1	detection					1012:1020	pulsed amperometric detection	992:1020	pulsed amperometric detection (HPAE-PAD)	992:1031	Glycosylation of Asn-727 found in the TfR purified from human placentae was analysed by high-pH anion-exchange chromatography with pulsed amperometric detection (HPAE-PAD) and mass spectrometry following tryptic digestion, peptide purification via reverse-phase high-performance liquid chromatography (RP-HPLC) and peptide sequencing.
7780197	4	55	theme	Wild-type	513:521	arg1	TfR					523:525	Wild-type TfR	513:525	Wild-type TfR	513:525	Wild-type TfR and mutants containing only the Asn-727 site or missing all three sites were transfected into mouse 3T3 cells and receptors were analysed by endo-N-acetylglucosaminidase H (Endo-H) digestion, SDS-PAGE and immunoblotting.
7780197	1	56	dep	folding	226:232	arg1	the					215:217	the	215:217	the	215:217	The human transferrin receptor (TfR) contains three N-linked oligosaccharides and glycosylation is required for the proper folding and function of the molecule.
7780197	3	57	from	site	417:420	arg1	present					401:407	present	401:407	present	401:407	The oligosaccharide(s) present at this site have been analysed using a combination of site-directed mutagenesis and chemical analysis.
7780197	3	58	theme	mutagenesis	478:488	arg1	combination					449:459	a combination	447:459	a combination of site-directed mutagenesis and chemical analysis	447:510	The oligosaccharide(s) present at this site have been analysed using a combination of site-directed mutagenesis and chemical analysis.
7780197	6	59	theme	peptide	1176:1182	arg1	sequencing					1184:1193	peptide sequencing	1176:1193	peptide sequencing	1176:1193	Glycosylation of Asn-727 found in the TfR purified from human placentae was analysed by high-pH anion-exchange chromatography with pulsed amperometric detection (HPAE-PAD) and mass spectrometry following tryptic digestion, peptide purification via reverse-phase high-performance liquid chromatography (RP-HPLC) and peptide sequencing.
7780197	8	60	theme	80	1354:1355	arg1	Da					1357:1358	Da	1357:1358	Da	1357:1358	Mass spectrometry confirmed these observations, but also showed the presence of an 80 Da anionic moiety on a fraction of the oligosaccharides.
7780197	4	61	theme	mouse	621:625	arg1	cells					631:635	mouse 3T3 cells	621:635	mouse 3T3 cells	621:635	Wild-type TfR and mutants containing only the Asn-727 site or missing all three sites were transfected into mouse 3T3 cells and receptors were analysed by endo-N-acetylglucosaminidase H (Endo-H) digestion, SDS-PAGE and immunoblotting.
7780197	5	62	theme	high-mannose	803:814	arg1	oligosaccharides					843:858	high-mannose or Endo-H-sensitive hybrid oligosaccharides	803:858	high-mannose or Endo-H-sensitive hybrid oligosaccharides	803:858	These studies suggested that the Asn-727 site contains high-mannose or Endo-H-sensitive hybrid oligosaccharides.
7780197	6	63	theme	anion-exchange	957:970	arg1	chromatography					972:985	high-pH anion-exchange chromatography	949:985	high-pH anion-exchange chromatography with pulsed amperometric detection (HPAE-PAD)	949:1031	Glycosylation of Asn-727 found in the TfR purified from human placentae was analysed by high-pH anion-exchange chromatography with pulsed amperometric detection (HPAE-PAD) and mass spectrometry following tryptic digestion, peptide purification via reverse-phase high-performance liquid chromatography (RP-HPLC) and peptide sequencing.
7780197	3	64	theme	oligosaccharide	382:396	arg1	s					398:398	The oligosaccharide(s)	378:399	The oligosaccharide(s) present at this site	378:420	The oligosaccharide(s) present at this site have been analysed using a combination of site-directed mutagenesis and chemical analysis.
7780197	0	65	contain	contains	62:69	arg1	site					27:30	The critical glycosylation site	0:30	The critical glycosylation site of human transferrin receptor	0:60	The critical glycosylation site of human transferrin receptor contains a high-mannose oligosaccharide.
7780197	0	65	contain	contains	62:69	arg2	oligosaccharide					86:100	a high-mannose oligosaccharide	71:100	a high-mannose oligosaccharide	71:100	The critical glycosylation site of human transferrin receptor contains a high-mannose oligosaccharide.
7780197	0	65	contain	contains	62:69	arg1	receptor					53:60	human transferrin receptor	35:60	human transferrin receptor	35:60	The critical glycosylation site of human transferrin receptor contains a high-mannose oligosaccharide.
7780197	2	66	theme	TfR	373:375	arg1	production					346:355	the production	342:355	the production of fully active TfR	342:375	Earlier studies demonstrated that the oligosaccharide at Asn-727 is vital for the production of fully active TfR.
7780197	2	67	from	Asn-727	321:327	arg1	oligosaccharide					302:316	the oligosaccharide at Asn-727	298:327	the oligosaccharide at Asn-727	298:327	Earlier studies demonstrated that the oligosaccharide at Asn-727 is vital for the production of fully active TfR.
7780197	2	67	from	Asn-727	321:327	arg1	at					318:319	the oligosaccharide at Asn-727	298:327	the oligosaccharide at Asn-727	298:327	Earlier studies demonstrated that the oligosaccharide at Asn-727 is vital for the production of fully active TfR.
7780197	6	68	theme	tryptic	1065:1071	arg1	digestion					1073:1081	tryptic digestion	1065:1081	tryptic digestion	1065:1081	Glycosylation of Asn-727 found in the TfR purified from human placentae was analysed by high-pH anion-exchange chromatography with pulsed amperometric detection (HPAE-PAD) and mass spectrometry following tryptic digestion, peptide purification via reverse-phase high-performance liquid chromatography (RP-HPLC) and peptide sequencing.
9694965	1	0	from	mimetics	279:286	arg1	humans					291:296	humans	291:296	humans	291:296	The alpha and beta isoforms of the thromboxane A2 receptor (TP) mediate the actions of the prostanoid thromboxane A2 and its mimetics in humans.
9694965	2	1	theme	amino	303:307	arg1	region					318:323	The amino terminal region	299:323	The amino terminal region of the TPs	299:334	The amino terminal region of the TPs contains two consensus N-linked glycosylation sites at asparagine (N) residues N4 and N16.
9694965	9	2	link	N-linked	1656:1663	arg1	glycosylation					1665:1677	N-linked glycosylation	1656:1677	N-linked glycosylation of the human TP isoforms	1656:1702	Thus, N-linked glycosylation of the human TP isoforms is important for ligand binding, efficient second messenger signaling and efficient membrane expression.
9694965	3	3	theme	N-linked	474:481	arg1	glycosylation					483:495	N-linked glycosylation	474:495	N-linked glycosylation	474:495	In this study, we explored the significance of N-linked glycosylation on the signaling and surface expression of the human TP isoforms.
9694965	7	4	theme	membrane	1333:1340	arg1	expression					1342:1351	membrane expression	1333:1351	membrane expression	1333:1351	Subcellular fractionation confirmed that, in relation to total TP expression, membrane expression was not altered in TPalphaN4-Q4 or TPalphaN16-Q16 but was reduced to levels of 55% of total expression in TPalphaN4,Q4-N16,Q16.
9694965	9	5	theme	efficient	1737:1745	arg1	signaling					1764:1772	efficient second messenger signaling	1737:1772	efficient second messenger signaling	1737:1772	Thus, N-linked glycosylation of the human TP isoforms is important for ligand binding, efficient second messenger signaling and efficient membrane expression.
9694965	1	6	theme	alpha	158:162	arg1	isoforms					173:180	The alpha and beta isoforms	154:180	The alpha and beta isoforms of the thromboxane A2 receptor (TP)	154:216	The alpha and beta isoforms of the thromboxane A2 receptor (TP) mediate the actions of the prostanoid thromboxane A2 and its mimetics in humans.
9694965	9	7	theme	messenger	1754:1762	arg1	signaling					1764:1772	efficient second messenger signaling	1737:1772	efficient second messenger signaling	1737:1772	Thus, N-linked glycosylation of the human TP isoforms is important for ligand binding, efficient second messenger signaling and efficient membrane expression.
9694965	4	8	theme	radioligand	618:628	arg1	binding					645:651	selective radioligand ([3H]SQ29,548) binding	608:651	selective radioligand ([3H]SQ29,548) binding	608:651	Inhibition of N-linked glycosylation reduced selective radioligand ([3H]SQ29,548) binding by either TP in both human erythroleukemia cells and in transfected human embryonic kidney 293 cells.
9694965	8	9	theme	intracellular	1565:1577	arg1	mobilization					1584:1595	intracellular Ca++ mobilization	1565:1595	intracellular Ca++ mobilization by TPalpha or TPbeta	1565:1616	Inhibition of glycosylation reduced, but did not abolish, agonist (U46619) mediated intracellular Ca++ mobilization by TPalpha or TPbeta and cAMP production by TPalpha.
9694965	1	10	theme	beta	168:171	arg1	isoforms					173:180	The alpha and beta isoforms	154:180	The alpha and beta isoforms of the thromboxane A2 receptor (TP)	154:216	The alpha and beta isoforms of the thromboxane A2 receptor (TP) mediate the actions of the prostanoid thromboxane A2 and its mimetics in humans.
9694965	1	11	from	actions	230:236	arg1	humans					291:296	humans	291:296	humans	291:296	The alpha and beta isoforms of the thromboxane A2 receptor (TP) mediate the actions of the prostanoid thromboxane A2 and its mimetics in humans.
9694965	5	12	theme	site-directed	765:777	arg1	mutagenesis					779:789	site-directed mutagenesis	765:789	site-directed mutagenesis of the putative glycosylation sites of TPalpha	765:836	Moreover, site-directed mutagenesis of the putative glycosylation sites of TPalpha revealed that radioligand binding also was reduced greatly for both the single (TPalphaN4-Q4, TPalphaN16-Q16) and double (TPalphaN4,N16-Q4,Q16) mutants, yielding levels of 8% binding relative to the wild-type TPalpha for the double mutants.
9694965	0	13	from	signaling	67:75	arg1	Characterization					0:15	Characterization	0:15	Characterization of the role of N-linked glycosylation on the cell signaling and expression of the human thromboxane A2 receptor alpha and beta isoforms.	0:152	Characterization of the role of N-linked glycosylation on the cell signaling and expression of the human thromboxane A2 receptor alpha and beta isoforms.
9694965	9	14	theme	membrane	1788:1795	arg1	expression					1797:1806	efficient membrane expression	1778:1806	efficient membrane expression	1778:1806	Thus, N-linked glycosylation of the human TP isoforms is important for ligand binding, efficient second messenger signaling and efficient membrane expression.
9694965	4	15	theme	N-linked	577:584	arg1	glycosylation					586:598	N-linked glycosylation	577:598	N-linked glycosylation	577:598	Inhibition of N-linked glycosylation reduced selective radioligand ([3H]SQ29,548) binding by either TP in both human erythroleukemia cells and in transfected human embryonic kidney 293 cells.
9694965	0	16	theme	receptor	120:127	arg1	alpha					129:133	the human thromboxane A2 receptor alpha	95:133	the human thromboxane A2 receptor alpha	95:133	Characterization of the role of N-linked glycosylation on the cell signaling and expression of the human thromboxane A2 receptor alpha and beta isoforms.
9694965	2	17	contain	contains	336:343	arg2	sites					382:386	two consensus N-linked glycosylation sites	345:386	two consensus N-linked glycosylation sites at asparagine (N) residues N4 and N16	345:424	The amino terminal region of the TPs contains two consensus N-linked glycosylation sites at asparagine (N) residues N4 and N16.
9694965	2	17	contain	contains	336:343	arg1	region					318:323	The amino terminal region	299:323	The amino terminal region of the TPs	299:334	The amino terminal region of the TPs contains two consensus N-linked glycosylation sites at asparagine (N) residues N4 and N16.
9694965	1	18	theme	thromboxane	189:199	arg1	A2					201:202	thromboxane A2	189:202	the thromboxane A2 receptor (TP)	185:216	The alpha and beta isoforms of the thromboxane A2 receptor (TP) mediate the actions of the prostanoid thromboxane A2 and its mimetics in humans.
9694965	6	19	theme	decreased	1123:1131	arg1	binding					1141:1147	decreased maximal binding	1123:1147	decreased maximal binding	1123:1147	Reductions in ligand binding were caused by decreased maximal binding and not by changes in affinity (Kd) or in specificity of the receptors for [3H]SQ29,548 or other ligands.
9694965	3	20	theme	surface	518:524	arg1	expression					526:535	surface expression	518:535	surface expression	518:535	In this study, we explored the significance of N-linked glycosylation on the signaling and surface expression of the human TP isoforms.
9694965	4	21	link	N-linked	577:584	arg1	glycosylation					586:598	N-linked glycosylation	577:598	N-linked glycosylation	577:598	Inhibition of N-linked glycosylation reduced selective radioligand ([3H]SQ29,548) binding by either TP in both human erythroleukemia cells and in transfected human embryonic kidney 293 cells.
9694965	0	22	theme	isoforms	144:151	arg1	signaling					67:75	cell signaling	62:75	cell signaling	62:75	Characterization of the role of N-linked glycosylation on the cell signaling and expression of the human thromboxane A2 receptor alpha and beta isoforms.
9694965	0	22	theme	isoforms	144:151	arg1	expression					81:90	expression	81:90	expression	81:90	Characterization of the role of N-linked glycosylation on the cell signaling and expression of the human thromboxane A2 receptor alpha and beta isoforms.
9694965	3	23	theme	isoforms	553:560	arg1	expression					526:535	surface expression	518:535	surface expression	518:535	In this study, we explored the significance of N-linked glycosylation on the signaling and surface expression of the human TP isoforms.
9694965	3	23	theme	isoforms	553:560	arg1	signaling					504:512	signaling	504:512	signaling	504:512	In this study, we explored the significance of N-linked glycosylation on the signaling and surface expression of the human TP isoforms.
9694965	8	24	theme	cAMP	1622:1625	arg1	production					1627:1636	cAMP production	1622:1636	cAMP production by TPalpha	1622:1647	Inhibition of glycosylation reduced, but did not abolish, agonist (U46619) mediated intracellular Ca++ mobilization by TPalpha or TPbeta and cAMP production by TPalpha.
9694965	0	25	from	expression	81:90	arg1	Characterization					0:15	Characterization	0:15	Characterization of the role of N-linked glycosylation on the cell signaling and expression of the human thromboxane A2 receptor alpha and beta isoforms.	0:152	Characterization of the role of N-linked glycosylation on the cell signaling and expression of the human thromboxane A2 receptor alpha and beta isoforms.
9694965	4	26	theme	[3H	631:633	arg1	binding					645:651	selective radioligand ([3H]SQ29,548) binding	608:651	selective radioligand ([3H]SQ29,548) binding	608:651	Inhibition of N-linked glycosylation reduced selective radioligand ([3H]SQ29,548) binding by either TP in both human erythroleukemia cells and in transfected human embryonic kidney 293 cells.
9694965	5	27	theme	relative	1021:1028	arg1	binding					1013:1019	8% binding	1010:1019	8% binding relative to the wild-type TPalpha for the double mutants	1010:1076	Moreover, site-directed mutagenesis of the putative glycosylation sites of TPalpha revealed that radioligand binding also was reduced greatly for both the single (TPalphaN4-Q4, TPalphaN16-Q16) and double (TPalphaN4,N16-Q4,Q16) mutants, yielding levels of 8% binding relative to the wild-type TPalpha for the double mutants.
9694965	3	28	theme	human	544:548	arg1	isoforms					553:560	the human TP isoforms	540:560	the human TP isoforms	540:560	In this study, we explored the significance of N-linked glycosylation on the signaling and surface expression of the human TP isoforms.
9694965	5	29	theme	TPalpha	830:836	arg1	TPalpha					830:836	TPalpha	830:836	TPalpha	830:836	Moreover, site-directed mutagenesis of the putative glycosylation sites of TPalpha revealed that radioligand binding also was reduced greatly for both the single (TPalphaN4-Q4, TPalphaN16-Q16) and double (TPalphaN4,N16-Q4,Q16) mutants, yielding levels of 8% binding relative to the wild-type TPalpha for the double mutants.
9694965	5	29	theme	TPalpha	830:836	arg1	sites					821:825	the putative glycosylation sites	794:825	the putative glycosylation sites of TPalpha	794:836	Moreover, site-directed mutagenesis of the putative glycosylation sites of TPalpha revealed that radioligand binding also was reduced greatly for both the single (TPalphaN4-Q4, TPalphaN16-Q16) and double (TPalphaN4,N16-Q4,Q16) mutants, yielding levels of 8% binding relative to the wild-type TPalpha for the double mutants.
9694965	7	30	theme	total	1439:1443	arg1	expression					1445:1454	total expression	1439:1454	total expression in TPalphaN4,Q4-N16,Q16	1439:1478	Subcellular fractionation confirmed that, in relation to total TP expression, membrane expression was not altered in TPalphaN4-Q4 or TPalphaN16-Q16 but was reduced to levels of 55% of total expression in TPalphaN4,Q4-N16,Q16.
9694965	2	31	gly	glycosylation	368:380	arg2	sites					382:386	two consensus N-linked glycosylation sites	345:386	two consensus N-linked glycosylation sites at asparagine (N) residues N4 and N16	345:424	The amino terminal region of the TPs contains two consensus N-linked glycosylation sites at asparagine (N) residues N4 and N16.
9694965	2	31	gly	glycosylation	368:380	arg2	N16					422:424	N16	422:424	N16	422:424	The amino terminal region of the TPs contains two consensus N-linked glycosylation sites at asparagine (N) residues N4 and N16.
9694965	2	31	gly	glycosylation	368:380	arg2	residues					406:413	asparagine (N) residues	391:413	asparagine (N) residues N4 and N16	391:424	The amino terminal region of the TPs contains two consensus N-linked glycosylation sites at asparagine (N) residues N4 and N16.
9694965	2	31	gly	glycosylation	368:380	arg2	N4					415:416	N4	415:416	N4	415:416	The amino terminal region of the TPs contains two consensus N-linked glycosylation sites at asparagine (N) residues N4 and N16.
9694965	2	31	gly	glycosylation	368:380	arg2	two					345:347	two	345:347	two	345:347	The amino terminal region of the TPs contains two consensus N-linked glycosylation sites at asparagine (N) residues N4 and N16.
9694965	4	32	theme	SQ29,548	635:642	arg1	binding					645:651	selective radioligand ([3H]SQ29,548) binding	608:651	selective radioligand ([3H]SQ29,548) binding	608:651	Inhibition of N-linked glycosylation reduced selective radioligand ([3H]SQ29,548) binding by either TP in both human erythroleukemia cells and in transfected human embryonic kidney 293 cells.
9694965	3	33	from	significance	458:469	arg1	expression					526:535	surface expression	518:535	surface expression	518:535	In this study, we explored the significance of N-linked glycosylation on the signaling and surface expression of the human TP isoforms.
9694965	3	33	from	significance	458:469	arg1	signaling					504:512	signaling	504:512	signaling	504:512	In this study, we explored the significance of N-linked glycosylation on the signaling and surface expression of the human TP isoforms.
9694965	6	34	theme	other	1240:1244	arg1	ligands					1246:1252	other ligands	1240:1252	other ligands	1240:1252	Reductions in ligand binding were caused by decreased maximal binding and not by changes in affinity (Kd) or in specificity of the receptors for [3H]SQ29,548 or other ligands.
9694965	3	35	dep	signaling	504:512	arg1	the					500:502	the	500:502	the	500:502	In this study, we explored the significance of N-linked glycosylation on the signaling and surface expression of the human TP isoforms.
9694965	7	36	theme	%	1434:1434	arg1	levels					1422:1427	levels	1422:1427	levels of 55% of total expression in TPalphaN4,Q4-N16,Q16	1422:1478	Subcellular fractionation confirmed that, in relation to total TP expression, membrane expression was not altered in TPalphaN4-Q4 or TPalphaN16-Q16 but was reduced to levels of 55% of total expression in TPalphaN4,Q4-N16,Q16.
9694965	0	37	from	Characterization	0:15	arg1	signaling					67:75	cell signaling	62:75	cell signaling	62:75	Characterization of the role of N-linked glycosylation on the cell signaling and expression of the human thromboxane A2 receptor alpha and beta isoforms.
9694965	0	37	from	Characterization	0:15	arg1	expression					81:90	expression	81:90	expression	81:90	Characterization of the role of N-linked glycosylation on the cell signaling and expression of the human thromboxane A2 receptor alpha and beta isoforms.
9694965	5	38	theme	single	910:915	arg1	mutants					982:988	both the single (TPalphaN4-Q4, TPalphaN16-Q16) and double (TPalphaN4,N16-Q4,Q16) mutants	901:988	mutants	982:988	Moreover, site-directed mutagenesis of the putative glycosylation sites of TPalpha revealed that radioligand binding also was reduced greatly for both the single (TPalphaN4-Q4, TPalphaN16-Q16) and double (TPalphaN4,N16-Q4,Q16) mutants, yielding levels of 8% binding relative to the wild-type TPalpha for the double mutants.
9694965	5	39	theme	%	1011:1011	arg1	binding					1013:1019	8% binding	1010:1019	8% binding relative to the wild-type TPalpha for the double mutants	1010:1076	Moreover, site-directed mutagenesis of the putative glycosylation sites of TPalpha revealed that radioligand binding also was reduced greatly for both the single (TPalphaN4-Q4, TPalphaN16-Q16) and double (TPalphaN4,N16-Q4,Q16) mutants, yielding levels of 8% binding relative to the wild-type TPalpha for the double mutants.
9694965	9	40	gly	glycosylation	1665:1677	arg1	isoforms					1695:1702	the human TP isoforms	1682:1702	the human TP isoforms	1682:1702	Thus, N-linked glycosylation of the human TP isoforms is important for ligand binding, efficient second messenger signaling and efficient membrane expression.
9694965	9	40	gly	glycosylation	1665:1677	arg1	messenger					1754:1762	efficient second messenger signaling	1737:1772	efficient second messenger signaling	1737:1772	Thus, N-linked glycosylation of the human TP isoforms is important for ligand binding, efficient second messenger signaling and efficient membrane expression.
9694965	9	40	gly	glycosylation	1665:1677	arg1	ligand					1721:1726	ligand binding	1721:1734	ligand binding	1721:1734	Thus, N-linked glycosylation of the human TP isoforms is important for ligand binding, efficient second messenger signaling and efficient membrane expression.
9694965	9	40	gly	glycosylation	1665:1677	arg1	membrane					1788:1795	efficient membrane expression	1778:1806	efficient membrane expression	1778:1806	Thus, N-linked glycosylation of the human TP isoforms is important for ligand binding, efficient second messenger signaling and efficient membrane expression.
9694965	6	41	from	Reductions	1079:1088	arg1	binding					1100:1106	ligand binding	1093:1106	ligand binding	1093:1106	Reductions in ligand binding were caused by decreased maximal binding and not by changes in affinity (Kd) or in specificity of the receptors for [3H]SQ29,548 or other ligands.
9694965	2	42	theme	TPs	332:334	arg1	region					318:323	The amino terminal region	299:323	The amino terminal region of the TPs	299:334	The amino terminal region of the TPs contains two consensus N-linked glycosylation sites at asparagine (N) residues N4 and N16.
9694965	0	43	dep	signaling	67:75	arg1	the					58:60	the	58:60	the	58:60	Characterization of the role of N-linked glycosylation on the cell signaling and expression of the human thromboxane A2 receptor alpha and beta isoforms.
9694965	2	44	theme	asparagine	391:400	arg1	residues					406:413	asparagine (N) residues	391:413	asparagine (N) residues N4 and N16	391:424	The amino terminal region of the TPs contains two consensus N-linked glycosylation sites at asparagine (N) residues N4 and N16.
9694965	2	44	theme	asparagine	391:400	arg1	N16					422:424	N16	422:424	N16	422:424	The amino terminal region of the TPs contains two consensus N-linked glycosylation sites at asparagine (N) residues N4 and N16.
9694965	2	44	theme	asparagine	391:400	arg1	N4					415:416	N4	415:416	N4	415:416	The amino terminal region of the TPs contains two consensus N-linked glycosylation sites at asparagine (N) residues N4 and N16.
9694965	4	45	theme	human	674:678	arg1	cells					696:700	both human erythroleukemia cells	669:700	both human erythroleukemia cells	669:700	Inhibition of N-linked glycosylation reduced selective radioligand ([3H]SQ29,548) binding by either TP in both human erythroleukemia cells and in transfected human embryonic kidney 293 cells.
9694965	1	46	theme	prostanoid	245:254	arg1	A2					268:269	the prostanoid thromboxane A2	241:269	the prostanoid thromboxane A2	241:269	The alpha and beta isoforms of the thromboxane A2 receptor (TP) mediate the actions of the prostanoid thromboxane A2 and its mimetics in humans.
9694965	9	47	theme	N-linked	1656:1663	arg1	glycosylation					1665:1677	N-linked glycosylation	1656:1677	N-linked glycosylation of the human TP isoforms	1656:1702	Thus, N-linked glycosylation of the human TP isoforms is important for ligand binding, efficient second messenger signaling and efficient membrane expression.
9694965	2	48	theme	N-linked	359:366	arg1	sites					382:386	two consensus N-linked glycosylation sites	345:386	two consensus N-linked glycosylation sites at asparagine (N) residues N4 and N16	345:424	The amino terminal region of the TPs contains two consensus N-linked glycosylation sites at asparagine (N) residues N4 and N16.
9694965	1	49	theme	A2	268:269	arg1	mimetics					279:286	its mimetics	275:286	its mimetics in humans	275:296	The alpha and beta isoforms of the thromboxane A2 receptor (TP) mediate the actions of the prostanoid thromboxane A2 and its mimetics in humans.
9694965	1	49	theme	A2	268:269	arg1	actions					230:236	the actions	226:236	the actions of the prostanoid thromboxane A2	226:269	The alpha and beta isoforms of the thromboxane A2 receptor (TP) mediate the actions of the prostanoid thromboxane A2 and its mimetics in humans.
9694965	7	50	from	%	1434:1434	arg1	Q4-N16					1469:1474	Q4-N16	1469:1474	Q4-N16	1469:1474	Subcellular fractionation confirmed that, in relation to total TP expression, membrane expression was not altered in TPalphaN4-Q4 or TPalphaN16-Q16 but was reduced to levels of 55% of total expression in TPalphaN4,Q4-N16,Q16.
9694965	7	50	from	%	1434:1434	arg1	Q16					1476:1478	Q16	1476:1478	Q16	1476:1478	Subcellular fractionation confirmed that, in relation to total TP expression, membrane expression was not altered in TPalphaN4-Q4 or TPalphaN16-Q16 but was reduced to levels of 55% of total expression in TPalphaN4,Q4-N16,Q16.
9694965	0	51	theme	glycosylation	41:53	arg1	role					24:27	the role	20:27	the role of N-linked glycosylation on the cell signaling and expression of the human thromboxane A2 receptor alpha and beta isoforms	20:151	Characterization of the role of N-linked glycosylation on the cell signaling and expression of the human thromboxane A2 receptor alpha and beta isoforms.
9694965	9	52	theme	human	1686:1690	arg1	isoforms					1695:1702	the human TP isoforms	1682:1702	the human TP isoforms	1682:1702	Thus, N-linked glycosylation of the human TP isoforms is important for ligand binding, efficient second messenger signaling and efficient membrane expression.
9694965	4	53	theme	human	721:725	arg1	kidney					737:742	human embryonic kidney 293	721:746	transfected human embryonic kidney 293 cells	709:752	Inhibition of N-linked glycosylation reduced selective radioligand ([3H]SQ29,548) binding by either TP in both human erythroleukemia cells and in transfected human embryonic kidney 293 cells.
9694965	8	54	theme	glycosylation	1495:1507	arg1	Inhibition					1481:1490	Inhibition	1481:1490	Inhibition of glycosylation	1481:1507	Inhibition of glycosylation reduced, but did not abolish, agonist (U46619) mediated intracellular Ca++ mobilization by TPalpha or TPbeta and cAMP production by TPalpha.
9694965	1	55	theme	A2	201:202	arg1	TP					214:215	TP	214:215	TP	214:215	The alpha and beta isoforms of the thromboxane A2 receptor (TP) mediate the actions of the prostanoid thromboxane A2 and its mimetics in humans.
9694965	1	55	theme	A2	201:202	arg1	receptor					204:211	the thromboxane A2 receptor	185:211	the thromboxane A2 receptor (TP)	185:216	The alpha and beta isoforms of the thromboxane A2 receptor (TP) mediate the actions of the prostanoid thromboxane A2 and its mimetics in humans.
9694965	9	56	theme	isoforms	1695:1702	arg1	glycosylation					1665:1677	N-linked glycosylation	1656:1677	N-linked glycosylation of the human TP isoforms	1656:1702	Thus, N-linked glycosylation of the human TP isoforms is important for ligand binding, efficient second messenger signaling and efficient membrane expression.
9694965	4	57	theme	kidney	737:742	arg1	cells					748:752	transfected human embryonic kidney 293 cells	709:752	transfected human embryonic kidney 293 cells	709:752	Inhibition of N-linked glycosylation reduced selective radioligand ([3H]SQ29,548) binding by either TP in both human erythroleukemia cells and in transfected human embryonic kidney 293 cells.
9694965	5	58	theme	putative	798:805	arg1	TPalpha					830:836	TPalpha	830:836	TPalpha	830:836	Moreover, site-directed mutagenesis of the putative glycosylation sites of TPalpha revealed that radioligand binding also was reduced greatly for both the single (TPalphaN4-Q4, TPalphaN16-Q16) and double (TPalphaN4,N16-Q4,Q16) mutants, yielding levels of 8% binding relative to the wild-type TPalpha for the double mutants.
9694965	5	58	theme	putative	798:805	arg1	sites					821:825	the putative glycosylation sites	794:825	the putative glycosylation sites of TPalpha	794:836	Moreover, site-directed mutagenesis of the putative glycosylation sites of TPalpha revealed that radioligand binding also was reduced greatly for both the single (TPalphaN4-Q4, TPalphaN16-Q16) and double (TPalphaN4,N16-Q4,Q16) mutants, yielding levels of 8% binding relative to the wild-type TPalpha for the double mutants.
9694965	2	59	theme	terminal	309:316	arg1	region					318:323	The amino terminal region	299:323	The amino terminal region of the TPs	299:334	The amino terminal region of the TPs contains two consensus N-linked glycosylation sites at asparagine (N) residues N4 and N16.
9694965	9	60	theme	ligand	1721:1726	arg1	binding					1728:1734	ligand binding	1721:1734	ligand binding	1721:1734	Thus, N-linked glycosylation of the human TP isoforms is important for ligand binding, efficient second messenger signaling and efficient membrane expression.
9694965	6	61	from	changes	1160:1166	arg1	affinity					1171:1178	affinity	1171:1178	affinity (Kd)	1171:1183	Reductions in ligand binding were caused by decreased maximal binding and not by changes in affinity (Kd) or in specificity of the receptors for [3H]SQ29,548 or other ligands.
9694965	6	61	from	changes	1160:1166	arg1	specificity					1191:1201	specificity	1191:1201	specificity of the receptors for [3H]SQ29,548 or other ligands	1191:1252	Reductions in ligand binding were caused by decreased maximal binding and not by changes in affinity (Kd) or in specificity of the receptors for [3H]SQ29,548 or other ligands.
9694965	6	61	from	changes	1160:1166	arg1	Kd					1181:1182	Kd	1181:1182	Kd	1181:1182	Reductions in ligand binding were caused by decreased maximal binding and not by changes in affinity (Kd) or in specificity of the receptors for [3H]SQ29,548 or other ligands.
9694965	5	62	gly	glycosylation	807:819	arg2	sites					821:825	the putative glycosylation sites	794:825	the putative glycosylation sites of TPalpha	794:836	Moreover, site-directed mutagenesis of the putative glycosylation sites of TPalpha revealed that radioligand binding also was reduced greatly for both the single (TPalphaN4-Q4, TPalphaN16-Q16) and double (TPalphaN4,N16-Q4,Q16) mutants, yielding levels of 8% binding relative to the wild-type TPalpha for the double mutants.
9694965	5	62	gly	glycosylation	807:819	arg1	TPalpha					830:836	TPalpha	830:836	TPalpha	830:836	Moreover, site-directed mutagenesis of the putative glycosylation sites of TPalpha revealed that radioligand binding also was reduced greatly for both the single (TPalphaN4-Q4, TPalphaN16-Q16) and double (TPalphaN4,N16-Q4,Q16) mutants, yielding levels of 8% binding relative to the wild-type TPalpha for the double mutants.
9694965	5	62	gly	glycosylation	807:819	arg2	TPalpha					830:836	TPalpha	830:836	TPalpha	830:836	Moreover, site-directed mutagenesis of the putative glycosylation sites of TPalpha revealed that radioligand binding also was reduced greatly for both the single (TPalphaN4-Q4, TPalphaN16-Q16) and double (TPalphaN4,N16-Q4,Q16) mutants, yielding levels of 8% binding relative to the wild-type TPalpha for the double mutants.
9694965	7	63	theme	total	1312:1316	arg1	expression					1321:1330	total TP expression	1312:1330	total TP expression	1312:1330	Subcellular fractionation confirmed that, in relation to total TP expression, membrane expression was not altered in TPalphaN4-Q4 or TPalphaN16-Q16 but was reduced to levels of 55% of total expression in TPalphaN4,Q4-N16,Q16.
9694965	5	64	dep	double	952:957	arg1	Q16					977:979	Q16	977:979	Q16	977:979	Moreover, site-directed mutagenesis of the putative glycosylation sites of TPalpha revealed that radioligand binding also was reduced greatly for both the single (TPalphaN4-Q4, TPalphaN16-Q16) and double (TPalphaN4,N16-Q4,Q16) mutants, yielding levels of 8% binding relative to the wild-type TPalpha for the double mutants.
9694965	5	64	dep	double	952:957	arg1	N16-Q4					970:975	N16-Q4	970:975	N16-Q4	970:975	Moreover, site-directed mutagenesis of the putative glycosylation sites of TPalpha revealed that radioligand binding also was reduced greatly for both the single (TPalphaN4-Q4, TPalphaN16-Q16) and double (TPalphaN4,N16-Q4,Q16) mutants, yielding levels of 8% binding relative to the wild-type TPalpha for the double mutants.
9694965	7	65	theme	TP	1318:1319	arg1	expression					1321:1330	total TP expression	1312:1330	total TP expression	1312:1330	Subcellular fractionation confirmed that, in relation to total TP expression, membrane expression was not altered in TPalphaN4-Q4 or TPalphaN16-Q16 but was reduced to levels of 55% of total expression in TPalphaN4,Q4-N16,Q16.
9694965	9	66	theme	second	1747:1752	arg1	signaling					1764:1772	efficient second messenger signaling	1737:1772	efficient second messenger signaling	1737:1772	Thus, N-linked glycosylation of the human TP isoforms is important for ligand binding, efficient second messenger signaling and efficient membrane expression.
9694965	4	67	theme	glycosylation	586:598	arg1	Inhibition					563:572	Inhibition	563:572	Inhibition of N-linked glycosylation	563:598	Inhibition of N-linked glycosylation reduced selective radioligand ([3H]SQ29,548) binding by either TP in both human erythroleukemia cells and in transfected human embryonic kidney 293 cells.
9694965	5	68	theme	glycosylation	807:819	arg1	TPalpha					830:836	TPalpha	830:836	TPalpha	830:836	Moreover, site-directed mutagenesis of the putative glycosylation sites of TPalpha revealed that radioligand binding also was reduced greatly for both the single (TPalphaN4-Q4, TPalphaN16-Q16) and double (TPalphaN4,N16-Q4,Q16) mutants, yielding levels of 8% binding relative to the wild-type TPalpha for the double mutants.
9694965	5	68	theme	glycosylation	807:819	arg1	sites					821:825	the putative glycosylation sites	794:825	the putative glycosylation sites of TPalpha	794:836	Moreover, site-directed mutagenesis of the putative glycosylation sites of TPalpha revealed that radioligand binding also was reduced greatly for both the single (TPalphaN4-Q4, TPalphaN16-Q16) and double (TPalphaN4,N16-Q4,Q16) mutants, yielding levels of 8% binding relative to the wild-type TPalpha for the double mutants.
9694965	0	69	link	N-linked	32:39	arg1	glycosylation					41:53	N-linked glycosylation	32:53	N-linked glycosylation	32:53	Characterization of the role of N-linked glycosylation on the cell signaling and expression of the human thromboxane A2 receptor alpha and beta isoforms.
9694965	4	70	theme	selective	608:616	arg1	binding					645:651	selective radioligand ([3H]SQ29,548) binding	608:651	selective radioligand ([3H]SQ29,548) binding	608:651	Inhibition of N-linked glycosylation reduced selective radioligand ([3H]SQ29,548) binding by either TP in both human erythroleukemia cells and in transfected human embryonic kidney 293 cells.
9694965	0	71	theme	A2	117:118	arg1	alpha					129:133	the human thromboxane A2 receptor alpha	95:133	the human thromboxane A2 receptor alpha	95:133	Characterization of the role of N-linked glycosylation on the cell signaling and expression of the human thromboxane A2 receptor alpha and beta isoforms.
9694965	3	72	theme	glycosylation	483:495	arg1	significance					458:469	the significance	454:469	the significance of N-linked glycosylation on the signaling and surface expression of the human TP isoforms	454:560	In this study, we explored the significance of N-linked glycosylation on the signaling and surface expression of the human TP isoforms.
9694965	9	73	theme	efficient	1778:1786	arg1	expression					1797:1806	efficient membrane expression	1778:1806	efficient membrane expression	1778:1806	Thus, N-linked glycosylation of the human TP isoforms is important for ligand binding, efficient second messenger signaling and efficient membrane expression.
9694965	0	74	theme	alpha	129:133	arg1	isoforms					144:151	the human thromboxane A2 receptor alpha and beta isoforms	95:151	the human thromboxane A2 receptor alpha and beta isoforms	95:151	Characterization of the role of N-linked glycosylation on the cell signaling and expression of the human thromboxane A2 receptor alpha and beta isoforms.
9694965	5	75	theme	sites	821:825	arg1	mutagenesis					779:789	site-directed mutagenesis	765:789	site-directed mutagenesis of the putative glycosylation sites of TPalpha	765:836	Moreover, site-directed mutagenesis of the putative glycosylation sites of TPalpha revealed that radioligand binding also was reduced greatly for both the single (TPalphaN4-Q4, TPalphaN16-Q16) and double (TPalphaN4,N16-Q4,Q16) mutants, yielding levels of 8% binding relative to the wild-type TPalpha for the double mutants.
9694965	6	76	theme	maximal	1133:1139	arg1	binding					1141:1147	decreased maximal binding	1123:1147	decreased maximal binding	1123:1147	Reductions in ligand binding were caused by decreased maximal binding and not by changes in affinity (Kd) or in specificity of the receptors for [3H]SQ29,548 or other ligands.
9694965	0	77	theme	beta	139:142	arg1	isoforms					144:151	the human thromboxane A2 receptor alpha and beta isoforms	95:151	the human thromboxane A2 receptor alpha and beta isoforms	95:151	Characterization of the role of N-linked glycosylation on the cell signaling and expression of the human thromboxane A2 receptor alpha and beta isoforms.
9694965	5	78	theme	radioligand	852:862	arg1	binding					864:870	radioligand binding	852:870	radioligand binding	852:870	Moreover, site-directed mutagenesis of the putative glycosylation sites of TPalpha revealed that radioligand binding also was reduced greatly for both the single (TPalphaN4-Q4, TPalphaN16-Q16) and double (TPalphaN4,N16-Q4,Q16) mutants, yielding levels of 8% binding relative to the wild-type TPalpha for the double mutants.
9694965	5	79	dep	TPalphaN4-Q4	918:929	arg1	TPalphaN16-Q16					932:945	TPalphaN16-Q16	932:945	TPalphaN16-Q16	932:945	Moreover, site-directed mutagenesis of the putative glycosylation sites of TPalpha revealed that radioligand binding also was reduced greatly for both the single (TPalphaN4-Q4, TPalphaN16-Q16) and double (TPalphaN4,N16-Q4,Q16) mutants, yielding levels of 8% binding relative to the wild-type TPalpha for the double mutants.
9694965	3	80	theme	TP	550:551	arg1	isoforms					553:560	the human TP isoforms	540:560	the human TP isoforms	540:560	In this study, we explored the significance of N-linked glycosylation on the signaling and surface expression of the human TP isoforms.
9694965	7	81	theme	expression	1445:1454	arg1	%					1434:1434	55%	1432:1434	55% of total expression in TPalphaN4,Q4-N16,Q16	1432:1478	Subcellular fractionation confirmed that, in relation to total TP expression, membrane expression was not altered in TPalphaN4-Q4 or TPalphaN16-Q16 but was reduced to levels of 55% of total expression in TPalphaN4,Q4-N16,Q16.
9694965	7	81	theme	expression	1445:1454	arg1	expression					1445:1454	total expression	1439:1454	total expression in TPalphaN4,Q4-N16,Q16	1439:1478	Subcellular fractionation confirmed that, in relation to total TP expression, membrane expression was not altered in TPalphaN4-Q4 or TPalphaN16-Q16 but was reduced to levels of 55% of total expression in TPalphaN4,Q4-N16,Q16.
9694965	5	82	dep	single	910:915	arg1	TPalphaN4-Q4					918:929	TPalphaN4-Q4	918:929	TPalphaN4-Q4	918:929	Moreover, site-directed mutagenesis of the putative glycosylation sites of TPalpha revealed that radioligand binding also was reduced greatly for both the single (TPalphaN4-Q4, TPalphaN16-Q16) and double (TPalphaN4,N16-Q4,Q16) mutants, yielding levels of 8% binding relative to the wild-type TPalpha for the double mutants.
9694965	0	83	theme	cell	62:65	arg1	signaling					67:75	cell signaling	62:75	cell signaling	62:75	Characterization of the role of N-linked glycosylation on the cell signaling and expression of the human thromboxane A2 receptor alpha and beta isoforms.
9694965	0	84	from	role	24:27	arg1	signaling					67:75	cell signaling	62:75	cell signaling	62:75	Characterization of the role of N-linked glycosylation on the cell signaling and expression of the human thromboxane A2 receptor alpha and beta isoforms.
9694965	0	84	from	role	24:27	arg1	expression					81:90	expression	81:90	expression	81:90	Characterization of the role of N-linked glycosylation on the cell signaling and expression of the human thromboxane A2 receptor alpha and beta isoforms.
9694965	6	85	theme	ligand	1093:1098	arg1	binding					1100:1106	ligand binding	1093:1106	ligand binding	1093:1106	Reductions in ligand binding were caused by decreased maximal binding and not by changes in affinity (Kd) or in specificity of the receptors for [3H]SQ29,548 or other ligands.
9694965	2	86	dep	residues	406:413	arg1	residues					406:413	asparagine (N) residues	391:413	asparagine (N) residues N4 and N16	391:424	The amino terminal region of the TPs contains two consensus N-linked glycosylation sites at asparagine (N) residues N4 and N16.
9694965	2	86	dep	residues	406:413	arg1	N16					422:424	N16	422:424	N16	422:424	The amino terminal region of the TPs contains two consensus N-linked glycosylation sites at asparagine (N) residues N4 and N16.
9694965	2	86	dep	residues	406:413	arg1	N4					415:416	N4	415:416	N4	415:416	The amino terminal region of the TPs contains two consensus N-linked glycosylation sites at asparagine (N) residues N4 and N16.
9694965	6	87	theme	receptors	1210:1218	arg1	specificity					1191:1201	specificity	1191:1201	specificity of the receptors for [3H]SQ29,548 or other ligands	1191:1252	Reductions in ligand binding were caused by decreased maximal binding and not by changes in affinity (Kd) or in specificity of the receptors for [3H]SQ29,548 or other ligands.
9694965	5	88	theme	wild-type	1037:1045	arg1	TPalpha					1047:1053	the wild-type TPalpha	1033:1053	the wild-type TPalpha for the double mutants	1033:1076	Moreover, site-directed mutagenesis of the putative glycosylation sites of TPalpha revealed that radioligand binding also was reduced greatly for both the single (TPalphaN4-Q4, TPalphaN16-Q16) and double (TPalphaN4,N16-Q4,Q16) mutants, yielding levels of 8% binding relative to the wild-type TPalpha for the double mutants.
9694965	2	89	from	residues	406:413	arg1	sites					382:386	two consensus N-linked glycosylation sites	345:386	two consensus N-linked glycosylation sites at asparagine (N) residues N4 and N16	345:424	The amino terminal region of the TPs contains two consensus N-linked glycosylation sites at asparagine (N) residues N4 and N16.
9694965	4	90	theme	erythroleukemia	680:694	arg1	cells					696:700	both human erythroleukemia cells	669:700	both human erythroleukemia cells	669:700	Inhibition of N-linked glycosylation reduced selective radioligand ([3H]SQ29,548) binding by either TP in both human erythroleukemia cells and in transfected human embryonic kidney 293 cells.
9694965	0	91	theme	human	99:103	arg1	A2					117:118	the human thromboxane A2	95:118	the human thromboxane A2 receptor alpha	95:133	Characterization of the role of N-linked glycosylation on the cell signaling and expression of the human thromboxane A2 receptor alpha and beta isoforms.
9694965	5	92	theme	8	1010:1010	arg1	%					1011:1011	%	1011:1011	%	1011:1011	Moreover, site-directed mutagenesis of the putative glycosylation sites of TPalpha revealed that radioligand binding also was reduced greatly for both the single (TPalphaN4-Q4, TPalphaN16-Q16) and double (TPalphaN4,N16-Q4,Q16) mutants, yielding levels of 8% binding relative to the wild-type TPalpha for the double mutants.
9694965	7	93	from	Q16	1476:1478	arg1	%					1434:1434	55%	1432:1434	55% of total expression in TPalphaN4,Q4-N16,Q16	1432:1478	Subcellular fractionation confirmed that, in relation to total TP expression, membrane expression was not altered in TPalphaN4-Q4 or TPalphaN16-Q16 but was reduced to levels of 55% of total expression in TPalphaN4,Q4-N16,Q16.
9694965	7	93	from	Q16	1476:1478	arg1	expression					1445:1454	total expression	1439:1454	total expression in TPalphaN4,Q4-N16,Q16	1439:1478	Subcellular fractionation confirmed that, in relation to total TP expression, membrane expression was not altered in TPalphaN4-Q4 or TPalphaN16-Q16 but was reduced to levels of 55% of total expression in TPalphaN4,Q4-N16,Q16.
9694965	3	94	link	N-linked	474:481	arg1	glycosylation					483:495	N-linked glycosylation	474:495	N-linked glycosylation	474:495	In this study, we explored the significance of N-linked glycosylation on the signaling and surface expression of the human TP isoforms.
9694965	5	95	theme	binding	1013:1019	arg1	levels					1000:1005	levels	1000:1005	levels of 8% binding relative to the wild-type TPalpha for the double mutants	1000:1076	Moreover, site-directed mutagenesis of the putative glycosylation sites of TPalpha revealed that radioligand binding also was reduced greatly for both the single (TPalphaN4-Q4, TPalphaN16-Q16) and double (TPalphaN4,N16-Q4,Q16) mutants, yielding levels of 8% binding relative to the wild-type TPalpha for the double mutants.
9694965	0	96	theme	role	24:27	arg1	Characterization					0:15	Characterization	0:15	Characterization of the role of N-linked glycosylation on the cell signaling and expression of the human thromboxane A2 receptor alpha and beta isoforms.	0:152	Characterization of the role of N-linked glycosylation on the cell signaling and expression of the human thromboxane A2 receptor alpha and beta isoforms.
9694965	8	97	theme	Ca++	1579:1582	arg1	mobilization					1584:1595	intracellular Ca++ mobilization	1565:1595	intracellular Ca++ mobilization by TPalpha or TPbeta	1565:1616	Inhibition of glycosylation reduced, but did not abolish, agonist (U46619) mediated intracellular Ca++ mobilization by TPalpha or TPbeta and cAMP production by TPalpha.
9694965	2	98	theme	glycosylation	368:380	arg1	sites					382:386	two consensus N-linked glycosylation sites	345:386	two consensus N-linked glycosylation sites at asparagine (N) residues N4 and N16	345:424	The amino terminal region of the TPs contains two consensus N-linked glycosylation sites at asparagine (N) residues N4 and N16.
9694965	0	99	theme	N-linked	32:39	arg1	glycosylation					41:53	N-linked glycosylation	32:53	N-linked glycosylation	32:53	Characterization of the role of N-linked glycosylation on the cell signaling and expression of the human thromboxane A2 receptor alpha and beta isoforms.
9694965	1	100	theme	thromboxane	256:266	arg1	A2					268:269	the prostanoid thromboxane A2	241:269	the prostanoid thromboxane A2	241:269	The alpha and beta isoforms of the thromboxane A2 receptor (TP) mediate the actions of the prostanoid thromboxane A2 and its mimetics in humans.
9694965	5	101	theme	double	952:957	arg1	mutants					982:988	both the single (TPalphaN4-Q4, TPalphaN16-Q16) and double (TPalphaN4,N16-Q4,Q16) mutants	901:988	mutants	982:988	Moreover, site-directed mutagenesis of the putative glycosylation sites of TPalpha revealed that radioligand binding also was reduced greatly for both the single (TPalphaN4-Q4, TPalphaN16-Q16) and double (TPalphaN4,N16-Q4,Q16) mutants, yielding levels of 8% binding relative to the wild-type TPalpha for the double mutants.
9694965	2	102	theme	consensus	349:357	arg1	sites					382:386	two consensus N-linked glycosylation sites	345:386	two consensus N-linked glycosylation sites at asparagine (N) residues N4 and N16	345:424	The amino terminal region of the TPs contains two consensus N-linked glycosylation sites at asparagine (N) residues N4 and N16.
9694965	7	103	dep	expression	1321:1330	arg1	relation					1300:1307	relation	1300:1307	relation	1300:1307	Subcellular fractionation confirmed that, in relation to total TP expression, membrane expression was not altered in TPalphaN4-Q4 or TPalphaN16-Q16 but was reduced to levels of 55% of total expression in TPalphaN4,Q4-N16,Q16.
9694965	2	104	link	N-linked	359:366	arg1	sites					382:386	two consensus N-linked glycosylation sites	345:386	two consensus N-linked glycosylation sites at asparagine (N) residues N4 and N16	345:424	The amino terminal region of the TPs contains two consensus N-linked glycosylation sites at asparagine (N) residues N4 and N16.
9694965	5	105	theme	double	1063:1068	arg1	mutants					1070:1076	the double mutants	1059:1076	the double mutants	1059:1076	Moreover, site-directed mutagenesis of the putative glycosylation sites of TPalpha revealed that radioligand binding also was reduced greatly for both the single (TPalphaN4-Q4, TPalphaN16-Q16) and double (TPalphaN4,N16-Q4,Q16) mutants, yielding levels of 8% binding relative to the wild-type TPalpha for the double mutants.
9694965	7	106	from	expression	1445:1454	arg1	Q4-N16					1469:1474	Q4-N16	1469:1474	Q4-N16	1469:1474	Subcellular fractionation confirmed that, in relation to total TP expression, membrane expression was not altered in TPalphaN4-Q4 or TPalphaN16-Q16 but was reduced to levels of 55% of total expression in TPalphaN4,Q4-N16,Q16.
9694965	7	106	from	expression	1445:1454	arg1	Q16					1476:1478	Q16	1476:1478	Q16	1476:1478	Subcellular fractionation confirmed that, in relation to total TP expression, membrane expression was not altered in TPalphaN4-Q4 or TPalphaN16-Q16 but was reduced to levels of 55% of total expression in TPalphaN4,Q4-N16,Q16.
9694965	7	107	theme	Subcellular	1255:1265	arg1	fractionation					1267:1279	Subcellular fractionation	1255:1279	Subcellular fractionation	1255:1279	Subcellular fractionation confirmed that, in relation to total TP expression, membrane expression was not altered in TPalphaN4-Q4 or TPalphaN16-Q16 but was reduced to levels of 55% of total expression in TPalphaN4,Q4-N16,Q16.
9694965	9	108	theme	TP	1692:1693	arg1	isoforms					1695:1702	the human TP isoforms	1682:1702	the human TP isoforms	1682:1702	Thus, N-linked glycosylation of the human TP isoforms is important for ligand binding, efficient second messenger signaling and efficient membrane expression.
9694965	4	109	theme	transfected	709:719	arg1	cells					748:752	transfected human embryonic kidney 293 cells	709:752	transfected human embryonic kidney 293 cells	709:752	Inhibition of N-linked glycosylation reduced selective radioligand ([3H]SQ29,548) binding by either TP in both human erythroleukemia cells and in transfected human embryonic kidney 293 cells.
9694965	1	110	theme	receptor	204:211	arg1	isoforms					173:180	The alpha and beta isoforms	154:180	The alpha and beta isoforms of the thromboxane A2 receptor (TP)	154:216	The alpha and beta isoforms of the thromboxane A2 receptor (TP) mediate the actions of the prostanoid thromboxane A2 and its mimetics in humans.
9694965	0	111	theme	thromboxane	105:115	arg1	A2					117:118	the human thromboxane A2	95:118	the human thromboxane A2 receptor alpha	95:133	Characterization of the role of N-linked glycosylation on the cell signaling and expression of the human thromboxane A2 receptor alpha and beta isoforms.
9694965	5	112	dep	mutants	982:988	arg1	both					901:904	both	901:904	both	901:904	Moreover, site-directed mutagenesis of the putative glycosylation sites of TPalpha revealed that radioligand binding also was reduced greatly for both the single (TPalphaN4-Q4, TPalphaN16-Q16) and double (TPalphaN4,N16-Q4,Q16) mutants, yielding levels of 8% binding relative to the wild-type TPalpha for the double mutants.
9694965	4	113	theme	embryonic	727:735	arg1	kidney					737:742	human embryonic kidney 293	721:746	transfected human embryonic kidney 293 cells	709:752	Inhibition of N-linked glycosylation reduced selective radioligand ([3H]SQ29,548) binding by either TP in both human erythroleukemia cells and in transfected human embryonic kidney 293 cells.
12270132	1	0	dep	glycosylation	240:252	arg1	the					236:238	the	236:238	the	236:238	The beta(1)-adrenergic receptor (beta(1)AR) has one predicted site of N-linked glycosylation on its extracellular amino-terminus, but the glycosylation and potential functional importance of this site have not yet been examined.
12270132	3	1	theme	agonist-promoted	720:735	arg1	internalization					737:751	agonist-promoted internalization	720:751	agonist-promoted internalization	720:751	The beta(1)AR N15A mutant exhibited significantly decreased basal surface expression relative to the wild-type receptor but had no detectable deficits in ligand binding or agonist-promoted internalization.
12270132	0	2	theme	surface	65:71	arg1	expression					73:82	receptor surface expression	56:82	receptor surface expression	56:82	Glycosylation of beta(1)-adrenergic receptors regulates receptor surface expression and dimerization.
12270132	1	3	theme	site	298:301	arg1	glycosylation					240:252	glycosylation	240:252	glycosylation	240:252	The beta(1)-adrenergic receptor (beta(1)AR) has one predicted site of N-linked glycosylation on its extracellular amino-terminus, but the glycosylation and potential functional importance of this site have not yet been examined.
12270132	1	3	theme	site	298:301	arg1	importance					279:288	potential functional importance	258:288	potential functional importance	258:288	The beta(1)-adrenergic receptor (beta(1)AR) has one predicted site of N-linked glycosylation on its extracellular amino-terminus, but the glycosylation and potential functional importance of this site have not yet been examined.
12270132	4	4	theme	Flag-tagged	795:805	arg1	receptors					821:829	Flag-tagged and HA-tagged receptors	795:829	Flag-tagged and HA-tagged receptors	795:829	Co-immunoprecipitation experiments using Flag-tagged and HA-tagged receptors demonstrated that the beta(1)AR-N15A mutant receptor exhibits a markedly reduced capacity for dimerization relative to wild-type beta(1)AR.
12270132	1	5	theme	beta	135:138	arg1	receptor					125:132	The beta(1)-adrenergic receptor	102:132	The beta(1)-adrenergic receptor (beta(1)AR)	102:144	The beta(1)-adrenergic receptor (beta(1)AR) has one predicted site of N-linked glycosylation on its extracellular amino-terminus, but the glycosylation and potential functional importance of this site have not yet been examined.
12270132	1	5	theme	beta	135:138	arg1	AR					142:143	beta(1)AR	135:143	beta(1)AR	135:143	The beta(1)-adrenergic receptor (beta(1)AR) has one predicted site of N-linked glycosylation on its extracellular amino-terminus, but the glycosylation and potential functional importance of this site have not yet been examined.
12270132	5	6	theme	beta	1088:1091	arg1	expression					1106:1115	beta(1)AR surface expression	1088:1115	beta(1)AR surface expression	1088:1115	These data reveal that the beta(1)AR is glycosylated on Asn15 and that this glycosylation plays a role in regulating beta(1)AR surface expression and dimerization.
12270132	2	7	theme	predicted	433:441	arg1	site					443:446	the single predicted site	422:446	the single predicted site of N-linked glycosylation (N15A)	422:479	We show here that the beta(1)AR is glycosylated in various cell types and that mutation of the single predicted site of N-linked glycosylation (N15A) results in the formation of receptors that are not N-glycosylated.
12270132	2	7	theme	predicted	433:441	arg1	glycosylation					460:472	N-linked glycosylation	451:472	N-linked glycosylation (N15A)	451:479	We show here that the beta(1)AR is glycosylated in various cell types and that mutation of the single predicted site of N-linked glycosylation (N15A) results in the formation of receptors that are not N-glycosylated.
12270132	2	8	gly	N-glycosylated	532:545	arg1	receptors					509:517	receptors	509:517	receptors that are not N-glycosylated	509:545	We show here that the beta(1)AR is glycosylated in various cell types and that mutation of the single predicted site of N-linked glycosylation (N15A) results in the formation of receptors that are not N-glycosylated.
12270132	2	9	theme	single	426:431	arg1	site					443:446	the single predicted site	422:446	the single predicted site of N-linked glycosylation (N15A)	422:479	We show here that the beta(1)AR is glycosylated in various cell types and that mutation of the single predicted site of N-linked glycosylation (N15A) results in the formation of receptors that are not N-glycosylated.
12270132	2	9	theme	single	426:431	arg1	glycosylation					460:472	N-linked glycosylation	451:472	N-linked glycosylation (N15A)	451:479	We show here that the beta(1)AR is glycosylated in various cell types and that mutation of the single predicted site of N-linked glycosylation (N15A) results in the formation of receptors that are not N-glycosylated.
12270132	3	10	theme	surface	614:620	arg1	expression					622:631	basal surface expression	608:631	basal surface expression	608:631	The beta(1)AR N15A mutant exhibited significantly decreased basal surface expression relative to the wild-type receptor but had no detectable deficits in ligand binding or agonist-promoted internalization.
12270132	4	11	theme	HA-tagged	811:819	arg1	receptors					821:829	Flag-tagged and HA-tagged receptors	795:829	Flag-tagged and HA-tagged receptors	795:829	Co-immunoprecipitation experiments using Flag-tagged and HA-tagged receptors demonstrated that the beta(1)AR-N15A mutant receptor exhibits a markedly reduced capacity for dimerization relative to wild-type beta(1)AR.
12270132	1	12	gly	glycosylation	181:193	arg2	site					164:167	one predicted site	150:167	one predicted site of N-linked glycosylation	150:193	The beta(1)-adrenergic receptor (beta(1)AR) has one predicted site of N-linked glycosylation on its extracellular amino-terminus, but the glycosylation and potential functional importance of this site have not yet been examined.
12270132	1	12	gly	glycosylation	181:193	arg2	glycosylation					181:193	N-linked glycosylation	172:193	N-linked glycosylation	172:193	The beta(1)-adrenergic receptor (beta(1)AR) has one predicted site of N-linked glycosylation on its extracellular amino-terminus, but the glycosylation and potential functional importance of this site have not yet been examined.
12270132	5	13	gly	glycosylated	1011:1022	arg2	Asn15					1027:1031	Asn15	1027:1031	Asn15	1027:1031	These data reveal that the beta(1)AR is glycosylated on Asn15 and that this glycosylation plays a role in regulating beta(1)AR surface expression and dimerization.
12270132	5	13	gly	glycosylated	1011:1022	arg1	AR					1005:1006	the beta(1)AR	994:1006	the beta(1)AR	994:1006	These data reveal that the beta(1)AR is glycosylated on Asn15 and that this glycosylation plays a role in regulating beta(1)AR surface expression and dimerization.
12270132	5	13	gly	glycosylated	1011:1022	arg2	AR					1005:1006	the beta(1)AR	994:1006	the beta(1)AR	994:1006	These data reveal that the beta(1)AR is glycosylated on Asn15 and that this glycosylation plays a role in regulating beta(1)AR surface expression and dimerization.
12270132	5	13	gly	glycosylated	1011:1022	arg1	Asn15					1027:1031	Asn15	1027:1031	Asn15	1027:1031	These data reveal that the beta(1)AR is glycosylated on Asn15 and that this glycosylation plays a role in regulating beta(1)AR surface expression and dimerization.
12270132	4	14	theme	Co-immunoprecipitation	754:775	arg1	experiments					777:787	Co-immunoprecipitation experiments	754:787	Co-immunoprecipitation experiments using Flag-tagged and HA-tagged receptors	754:829	Co-immunoprecipitation experiments using Flag-tagged and HA-tagged receptors demonstrated that the beta(1)AR-N15A mutant receptor exhibits a markedly reduced capacity for dimerization relative to wild-type beta(1)AR.
12270132	4	15	dep	AR	967:968	arg1	1					965:965	1	965:965	1	965:965	Co-immunoprecipitation experiments using Flag-tagged and HA-tagged receptors demonstrated that the beta(1)AR-N15A mutant receptor exhibits a markedly reduced capacity for dimerization relative to wild-type beta(1)AR.
12270132	4	16	theme	relative	938:945	arg1	dimerization					925:936	dimerization	925:936	dimerization relative to wild-type beta(1)AR	925:968	Co-immunoprecipitation experiments using Flag-tagged and HA-tagged receptors demonstrated that the beta(1)AR-N15A mutant receptor exhibits a markedly reduced capacity for dimerization relative to wild-type beta(1)AR.
12270132	1	17	link	N-linked	172:179	arg1	glycosylation					181:193	N-linked glycosylation	172:193	N-linked glycosylation	172:193	The beta(1)-adrenergic receptor (beta(1)AR) has one predicted site of N-linked glycosylation on its extracellular amino-terminus, but the glycosylation and potential functional importance of this site have not yet been examined.
12270132	4	18	theme	beta	960:963	arg1	AR					967:968	wild-type beta(1)AR	950:968	wild-type beta(1)AR	950:968	Co-immunoprecipitation experiments using Flag-tagged and HA-tagged receptors demonstrated that the beta(1)AR-N15A mutant receptor exhibits a markedly reduced capacity for dimerization relative to wild-type beta(1)AR.
12270132	3	19	theme	basal	608:612	arg1	expression					622:631	basal surface expression	608:631	basal surface expression	608:631	The beta(1)AR N15A mutant exhibited significantly decreased basal surface expression relative to the wild-type receptor but had no detectable deficits in ligand binding or agonist-promoted internalization.
12270132	5	20	theme	surface	1098:1104	arg1	expression					1106:1115	beta(1)AR surface expression	1088:1115	beta(1)AR surface expression	1088:1115	These data reveal that the beta(1)AR is glycosylated on Asn15 and that this glycosylation plays a role in regulating beta(1)AR surface expression and dimerization.
12270132	4	21	theme	reduced	904:910	arg1	capacity					912:919	a markedly reduced capacity	893:919	a markedly reduced capacity for dimerization relative to wild-type beta(1)AR	893:968	Co-immunoprecipitation experiments using Flag-tagged and HA-tagged receptors demonstrated that the beta(1)AR-N15A mutant receptor exhibits a markedly reduced capacity for dimerization relative to wild-type beta(1)AR.
12270132	2	22	link	N-linked	451:458	arg1	N15A					475:478	N15A	475:478	N15A	475:478	We show here that the beta(1)AR is glycosylated in various cell types and that mutation of the single predicted site of N-linked glycosylation (N15A) results in the formation of receptors that are not N-glycosylated.
12270132	2	22	link	N-linked	451:458	arg1	glycosylation					460:472	N-linked glycosylation	451:472	N-linked glycosylation (N15A)	451:479	We show here that the beta(1)AR is glycosylated in various cell types and that mutation of the single predicted site of N-linked glycosylation (N15A) results in the formation of receptors that are not N-glycosylated.
12270132	3	23	theme	N15A	562:565	arg1	mutant					567:572	The beta(1)AR N15A mutant	548:572	The beta(1)AR N15A mutant	548:572	The beta(1)AR N15A mutant exhibited significantly decreased basal surface expression relative to the wild-type receptor but had no detectable deficits in ligand binding or agonist-promoted internalization.
12270132	2	24	theme	receptors	509:517	arg1	formation					496:504	the formation	492:504	the formation of receptors that are not N-glycosylated	492:545	We show here that the beta(1)AR is glycosylated in various cell types and that mutation of the single predicted site of N-linked glycosylation (N15A) results in the formation of receptors that are not N-glycosylated.
12270132	4	25	theme	wild-type	950:958	arg1	AR					967:968	wild-type beta(1)AR	950:968	wild-type beta(1)AR	950:968	Co-immunoprecipitation experiments using Flag-tagged and HA-tagged receptors demonstrated that the beta(1)AR-N15A mutant receptor exhibits a markedly reduced capacity for dimerization relative to wild-type beta(1)AR.
12270132	3	26	theme	wild-type	649:657	arg1	receptor					659:666	the wild-type receptor	645:666	the wild-type receptor	645:666	The beta(1)AR N15A mutant exhibited significantly decreased basal surface expression relative to the wild-type receptor but had no detectable deficits in ligand binding or agonist-promoted internalization.
12270132	2	27	theme	glycosylation	460:472	arg1	site					443:446	the single predicted site	422:446	the single predicted site of N-linked glycosylation (N15A)	422:479	We show here that the beta(1)AR is glycosylated in various cell types and that mutation of the single predicted site of N-linked glycosylation (N15A) results in the formation of receptors that are not N-glycosylated.
12270132	2	27	theme	glycosylation	460:472	arg1	glycosylation					460:472	N-linked glycosylation	451:472	N-linked glycosylation (N15A)	451:479	We show here that the beta(1)AR is glycosylated in various cell types and that mutation of the single predicted site of N-linked glycosylation (N15A) results in the formation of receptors that are not N-glycosylated.
12270132	3	28	dep	exhibited	574:582	arg1	had					672:674	had	672:674	had no detectable deficits in ligand binding or agonist-promoted internalization	672:751	The beta(1)AR N15A mutant exhibited significantly decreased basal surface expression relative to the wild-type receptor but had no detectable deficits in ligand binding or agonist-promoted internalization.
12270132	3	28	dep	exhibited	574:582	arg1	decreased					598:606	decreased	598:606	decreased basal surface expression relative to the wild-type receptor	598:666	The beta(1)AR N15A mutant exhibited significantly decreased basal surface expression relative to the wild-type receptor but had no detectable deficits in ligand binding or agonist-promoted internalization.
12270132	2	29	theme	N-linked	451:458	arg1	N15A					475:478	N15A	475:478	N15A	475:478	We show here that the beta(1)AR is glycosylated in various cell types and that mutation of the single predicted site of N-linked glycosylation (N15A) results in the formation of receptors that are not N-glycosylated.
12270132	2	29	theme	N-linked	451:458	arg1	glycosylation					460:472	N-linked glycosylation	451:472	N-linked glycosylation (N15A)	451:479	We show here that the beta(1)AR is glycosylated in various cell types and that mutation of the single predicted site of N-linked glycosylation (N15A) results in the formation of receptors that are not N-glycosylated.
12270132	2	30	theme	beta	353:356	arg1	AR					360:361	the beta(1)AR	349:361	the beta(1)AR	349:361	We show here that the beta(1)AR is glycosylated in various cell types and that mutation of the single predicted site of N-linked glycosylation (N15A) results in the formation of receptors that are not N-glycosylated.
12270132	2	31	theme	cell	390:393	arg1	types					395:399	various cell types	382:399	various cell types	382:399	We show here that the beta(1)AR is glycosylated in various cell types and that mutation of the single predicted site of N-linked glycosylation (N15A) results in the formation of receptors that are not N-glycosylated.
12270132	4	32	theme	AR-N15A	860:866	arg1	receptor					875:882	the beta(1)AR-N15A mutant receptor	849:882	the beta(1)AR-N15A mutant receptor	849:882	Co-immunoprecipitation experiments using Flag-tagged and HA-tagged receptors demonstrated that the beta(1)AR-N15A mutant receptor exhibits a markedly reduced capacity for dimerization relative to wild-type beta(1)AR.
12270132	3	33	theme	beta	552:555	arg1	mutant					567:572	The beta(1)AR N15A mutant	548:572	The beta(1)AR N15A mutant	548:572	The beta(1)AR N15A mutant exhibited significantly decreased basal surface expression relative to the wild-type receptor but had no detectable deficits in ligand binding or agonist-promoted internalization.
12270132	0	34	gly	Glycosylation	0:12	arg1	receptors					36:44	beta(1)-adrenergic receptors	17:44	beta(1)-adrenergic receptors	17:44	Glycosylation of beta(1)-adrenergic receptors regulates receptor surface expression and dimerization.
12270132	2	35	theme	various	382:388	arg1	types					395:399	various cell types	382:399	various cell types	382:399	We show here that the beta(1)AR is glycosylated in various cell types and that mutation of the single predicted site of N-linked glycosylation (N15A) results in the formation of receptors that are not N-glycosylated.
12270132	2	36	theme	site	443:446	arg1	mutation					410:417	mutation	410:417	mutation of the single predicted site of N-linked glycosylation (N15A)	410:479	We show here that the beta(1)AR is glycosylated in various cell types and that mutation of the single predicted site of N-linked glycosylation (N15A) results in the formation of receptors that are not N-glycosylated.
12270132	1	37	dep	AR	142:143	arg1	1					140:140	1	140:140	1	140:140	The beta(1)-adrenergic receptor (beta(1)AR) has one predicted site of N-linked glycosylation on its extracellular amino-terminus, but the glycosylation and potential functional importance of this site have not yet been examined.
12270132	1	38	theme	predicted	154:162	arg1	site					164:167	one predicted site	150:167	one predicted site of N-linked glycosylation	150:193	The beta(1)-adrenergic receptor (beta(1)AR) has one predicted site of N-linked glycosylation on its extracellular amino-terminus, but the glycosylation and potential functional importance of this site have not yet been examined.
12270132	1	38	theme	predicted	154:162	arg1	glycosylation					181:193	N-linked glycosylation	172:193	N-linked glycosylation	172:193	The beta(1)-adrenergic receptor (beta(1)AR) has one predicted site of N-linked glycosylation on its extracellular amino-terminus, but the glycosylation and potential functional importance of this site have not yet been examined.
12270132	0	39	theme	receptors	36:44	arg1	Glycosylation					0:12	Glycosylation	0:12	Glycosylation of beta(1)-adrenergic receptors	0:44	Glycosylation of beta(1)-adrenergic receptors regulates receptor surface expression and dimerization.
12270132	1	40	theme	potential	258:266	arg1	importance					279:288	potential functional importance	258:288	potential functional importance	258:288	The beta(1)-adrenergic receptor (beta(1)AR) has one predicted site of N-linked glycosylation on its extracellular amino-terminus, but the glycosylation and potential functional importance of this site have not yet been examined.
12270132	5	41	theme	beta	998:1001	arg1	AR					1005:1006	the beta(1)AR	994:1006	the beta(1)AR	994:1006	These data reveal that the beta(1)AR is glycosylated on Asn15 and that this glycosylation plays a role in regulating beta(1)AR surface expression and dimerization.
12270132	2	42	gly	glycosylated	366:377	arg1	AR					360:361	the beta(1)AR	349:361	the beta(1)AR	349:361	We show here that the beta(1)AR is glycosylated in various cell types and that mutation of the single predicted site of N-linked glycosylation (N15A) results in the formation of receptors that are not N-glycosylated.
12270132	2	42	gly	glycosylated	366:377	arg1	types					395:399	various cell types	382:399	various cell types	382:399	We show here that the beta(1)AR is glycosylated in various cell types and that mutation of the single predicted site of N-linked glycosylation (N15A) results in the formation of receptors that are not N-glycosylated.
12270132	2	42	gly	glycosylated	366:377	arg2	AR					360:361	the beta(1)AR	349:361	the beta(1)AR	349:361	We show here that the beta(1)AR is glycosylated in various cell types and that mutation of the single predicted site of N-linked glycosylation (N15A) results in the formation of receptors that are not N-glycosylated.
12270132	0	43	theme	-adrenergic	24:34	arg1	receptors					36:44	beta(1)-adrenergic receptors	17:44	beta(1)-adrenergic receptors	17:44	Glycosylation of beta(1)-adrenergic receptors regulates receptor surface expression and dimerization.
12270132	1	44	theme	functional	268:277	arg1	importance					279:288	potential functional importance	258:288	potential functional importance	258:288	The beta(1)-adrenergic receptor (beta(1)AR) has one predicted site of N-linked glycosylation on its extracellular amino-terminus, but the glycosylation and potential functional importance of this site have not yet been examined.
12270132	1	45	gly	glycosylation	240:252	arg1	site					298:301	this site	293:301	this site	293:301	The beta(1)-adrenergic receptor (beta(1)AR) has one predicted site of N-linked glycosylation on its extracellular amino-terminus, but the glycosylation and potential functional importance of this site have not yet been examined.
12270132	5	46	theme	AR	1095:1096	arg1	expression					1106:1115	beta(1)AR surface expression	1088:1115	beta(1)AR surface expression	1088:1115	These data reveal that the beta(1)AR is glycosylated on Asn15 and that this glycosylation plays a role in regulating beta(1)AR surface expression and dimerization.
12270132	4	47	theme	beta	853:856	arg1	receptor					875:882	the beta(1)AR-N15A mutant receptor	849:882	the beta(1)AR-N15A mutant receptor	849:882	Co-immunoprecipitation experiments using Flag-tagged and HA-tagged receptors demonstrated that the beta(1)AR-N15A mutant receptor exhibits a markedly reduced capacity for dimerization relative to wild-type beta(1)AR.
12270132	3	48	theme	AR	559:560	arg1	mutant					567:572	The beta(1)AR N15A mutant	548:572	The beta(1)AR N15A mutant	548:572	The beta(1)AR N15A mutant exhibited significantly decreased basal surface expression relative to the wild-type receptor but had no detectable deficits in ligand binding or agonist-promoted internalization.
12270132	1	49	contain	has	146:148	arg1	receptor					125:132	The beta(1)-adrenergic receptor	102:132	The beta(1)-adrenergic receptor (beta(1)AR)	102:144	The beta(1)-adrenergic receptor (beta(1)AR) has one predicted site of N-linked glycosylation on its extracellular amino-terminus, but the glycosylation and potential functional importance of this site have not yet been examined.
12270132	1	49	contain	has	146:148	arg1	AR					142:143	beta(1)AR	135:143	beta(1)AR	135:143	The beta(1)-adrenergic receptor (beta(1)AR) has one predicted site of N-linked glycosylation on its extracellular amino-terminus, but the glycosylation and potential functional importance of this site have not yet been examined.
12270132	1	49	contain	has	146:148	arg2	glycosylation					181:193	N-linked glycosylation	172:193	N-linked glycosylation	172:193	The beta(1)-adrenergic receptor (beta(1)AR) has one predicted site of N-linked glycosylation on its extracellular amino-terminus, but the glycosylation and potential functional importance of this site have not yet been examined.
12270132	1	49	contain	has	146:148	arg2	site					164:167	one predicted site	150:167	one predicted site of N-linked glycosylation	150:193	The beta(1)-adrenergic receptor (beta(1)AR) has one predicted site of N-linked glycosylation on its extracellular amino-terminus, but the glycosylation and potential functional importance of this site have not yet been examined.
12270132	4	50	theme	mutant	868:873	arg1	receptor					875:882	the beta(1)AR-N15A mutant receptor	849:882	the beta(1)AR-N15A mutant receptor	849:882	Co-immunoprecipitation experiments using Flag-tagged and HA-tagged receptors demonstrated that the beta(1)AR-N15A mutant receptor exhibits a markedly reduced capacity for dimerization relative to wild-type beta(1)AR.
12270132	3	51	theme	ligand	702:707	arg1	binding					709:715	ligand binding	702:715	ligand binding	702:715	The beta(1)AR N15A mutant exhibited significantly decreased basal surface expression relative to the wild-type receptor but had no detectable deficits in ligand binding or agonist-promoted internalization.
12270132	0	52	theme	receptor	56:63	arg1	expression					73:82	receptor surface expression	56:82	receptor surface expression	56:82	Glycosylation of beta(1)-adrenergic receptors regulates receptor surface expression and dimerization.
12270132	1	53	theme	-adrenergic	113:123	arg1	receptor					125:132	The beta(1)-adrenergic receptor	102:132	The beta(1)-adrenergic receptor (beta(1)AR)	102:144	The beta(1)-adrenergic receptor (beta(1)AR) has one predicted site of N-linked glycosylation on its extracellular amino-terminus, but the glycosylation and potential functional importance of this site have not yet been examined.
12270132	1	53	theme	-adrenergic	113:123	arg1	AR					142:143	beta(1)AR	135:143	beta(1)AR	135:143	The beta(1)-adrenergic receptor (beta(1)AR) has one predicted site of N-linked glycosylation on its extracellular amino-terminus, but the glycosylation and potential functional importance of this site have not yet been examined.
12270132	3	54	theme	detectable	679:688	arg1	deficits					690:697	no detectable deficits	676:697	no detectable deficits	676:697	The beta(1)AR N15A mutant exhibited significantly decreased basal surface expression relative to the wild-type receptor but had no detectable deficits in ligand binding or agonist-promoted internalization.
12270132	1	55	theme	N-linked	172:179	arg1	glycosylation					181:193	N-linked glycosylation	172:193	N-linked glycosylation	172:193	The beta(1)-adrenergic receptor (beta(1)AR) has one predicted site of N-linked glycosylation on its extracellular amino-terminus, but the glycosylation and potential functional importance of this site have not yet been examined.
12270132	1	56	theme	extracellular	202:214	arg1	amino-terminus					216:229	its extracellular amino-terminus	198:229	its extracellular amino-terminus	198:229	The beta(1)-adrenergic receptor (beta(1)AR) has one predicted site of N-linked glycosylation on its extracellular amino-terminus, but the glycosylation and potential functional importance of this site have not yet been examined.
12270132	2	57	gly	glycosylation	460:472	arg2	site					443:446	the single predicted site	422:446	the single predicted site of N-linked glycosylation (N15A)	422:479	We show here that the beta(1)AR is glycosylated in various cell types and that mutation of the single predicted site of N-linked glycosylation (N15A) results in the formation of receptors that are not N-glycosylated.
12270132	2	57	gly	glycosylation	460:472	arg2	glycosylation					460:472	N-linked glycosylation	451:472	N-linked glycosylation (N15A)	451:479	We show here that the beta(1)AR is glycosylated in various cell types and that mutation of the single predicted site of N-linked glycosylation (N15A) results in the formation of receptors that are not N-glycosylated.
12270132	1	58	theme	glycosylation	181:193	arg1	site					164:167	one predicted site	150:167	one predicted site of N-linked glycosylation	150:193	The beta(1)-adrenergic receptor (beta(1)AR) has one predicted site of N-linked glycosylation on its extracellular amino-terminus, but the glycosylation and potential functional importance of this site have not yet been examined.
12270132	1	58	theme	glycosylation	181:193	arg1	glycosylation					181:193	N-linked glycosylation	172:193	N-linked glycosylation	172:193	The beta(1)-adrenergic receptor (beta(1)AR) has one predicted site of N-linked glycosylation on its extracellular amino-terminus, but the glycosylation and potential functional importance of this site have not yet been examined.
19592704	7	0	theme	NCEH	1087:1090	arg1	localization					1071:1082	the ER localization	1064:1082	the ER localization of NCEH	1064:1090	Cholesterol loading by incubation with acetyl-LDL does not change the ER localization of NCEH.
19592704	4	1	with	reticulum	705:713	arg1	domain					739:744	its catalytic domain	725:744	its catalytic domain within the lumen	725:761	The N-terminal domain serves as a type II signal anchor sequence to recruit NCEH to the endoplasmic reticulum (ER) with its catalytic domain within the lumen.
19592704	3	2	theme	single-membrane-spanning	479:502	arg1	protein					521:527	a single-membrane-spanning type II membrane protein	477:527	a single-membrane-spanning type II membrane protein comprising three domains: N-terminal, catalytic, and lipid-binding domains	477:602	NCEH is a single-membrane-spanning type II membrane protein comprising three domains: N-terminal, catalytic, and lipid-binding domains.
19592704	3	2	theme	single-membrane-spanning	479:502	arg1	NCEH					469:472	NCEH	469:472	NCEH	469:472	NCEH is a single-membrane-spanning type II membrane protein comprising three domains: N-terminal, catalytic, and lipid-binding domains.
19592704	5	3	theme	NCEH	851:854	arg1	Asn					814:816	Asn(270)	814:821	Asn(270)	814:821	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	3	theme	NCEH	851:854	arg1	Asn					838:840	Asn	838:840	Asn(389)	838:845	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	3	theme	NCEH	851:854	arg1	sites					807:811	the putative N-linked glycosylation sites	771:811	the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH	771:854	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	3	theme	NCEH	851:854	arg1	NCEH					851:854	NCEH	851:854	NCEH	851:854	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	3	theme	NCEH	851:854	arg1	Asn					824:826	Asn	824:826	Asn(367)	824:831	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	7	4	theme	Cholesterol	998:1008	arg1	loading					1010:1016	Cholesterol loading	998:1016	Cholesterol loading by incubation with acetyl-LDL	998:1046	Cholesterol loading by incubation with acetyl-LDL does not change the ER localization of NCEH.
19592704	3	5	theme	type	504:507	arg1	protein					521:527	a single-membrane-spanning type II membrane protein	477:527	a single-membrane-spanning type II membrane protein comprising three domains: N-terminal, catalytic, and lipid-binding domains	477:602	NCEH is a single-membrane-spanning type II membrane protein comprising three domains: N-terminal, catalytic, and lipid-binding domains.
19592704	3	5	theme	type	504:507	arg1	NCEH					469:472	NCEH	469:472	NCEH	469:472	NCEH is a single-membrane-spanning type II membrane protein comprising three domains: N-terminal, catalytic, and lipid-binding domains.
19592704	8	6	theme	cells	1219:1223	arg1	cholesterol					1185:1195	cholesterol	1185:1195	cholesterol for efflux out of the cells	1185:1223	In conclusion, NCEH is targeted to the ER of macrophages, where it hydrolyzes CE to deliver cholesterol for efflux out of the cells.
19592704	6	7	from	Asn	891:893	arg1	Glycosylation					874:886	Glycosylation	874:886	Glycosylation	874:886	Glycosylation at Asn(270), which is located closest to the catalytic serine motif, is important for the enzymatic activity.
19592704	7	8	with	loading	1010:1016	arg1	acetyl-LDL					1037:1046	acetyl-LDL	1037:1046	acetyl-LDL	1037:1046	Cholesterol loading by incubation with acetyl-LDL does not change the ER localization of NCEH.
19592704	3	9	theme	N-terminal	555:564	arg1	domains					596:602	N-terminal, catalytic, and lipid-binding domains	555:602	three domains: N-terminal, catalytic, and lipid-binding domains	540:602	NCEH is a single-membrane-spanning type II membrane protein comprising three domains: N-terminal, catalytic, and lipid-binding domains.
19592704	0	10	theme	N-terminal	86:95	arg1	sequence					97:104	its N-terminal sequence	82:104	its N-terminal sequence	82:104	Targeting of neutral cholesterol ester hydrolase to the endoplasmic reticulum via its N-terminal sequence.
19592704	4	11	theme	catalytic	729:737	arg1	domain					739:744	its catalytic domain	725:744	its catalytic domain within the lumen	725:761	The N-terminal domain serves as a type II signal anchor sequence to recruit NCEH to the endoplasmic reticulum (ER) with its catalytic domain within the lumen.
19592704	1	12	theme	atherosclerosis	237:251	arg1	cells					216:220	macrophage foam cells	200:220	macrophage foam cells	200:220	Neutral cholesterol ester hydrolase (NCEH) accounts for a large part of the nCEH activity in macrophage foam cells, a hallmark of atherosclerosis, but its subcellular localization and structure-function relationship are unknown.
19592704	1	12	theme	atherosclerosis	237:251	arg1	hallmark					225:232	a hallmark	223:232	a hallmark of atherosclerosis	223:251	Neutral cholesterol ester hydrolase (NCEH) accounts for a large part of the nCEH activity in macrophage foam cells, a hallmark of atherosclerosis, but its subcellular localization and structure-function relationship are unknown.
19592704	4	13	theme	endoplasmic	693:703	arg1	ER					716:717	ER	716:717	ER	716:717	The N-terminal domain serves as a type II signal anchor sequence to recruit NCEH to the endoplasmic reticulum (ER) with its catalytic domain within the lumen.
19592704	4	13	theme	endoplasmic	693:703	arg1	reticulum					705:713	the endoplasmic reticulum	689:713	the endoplasmic reticulum (ER) with its catalytic domain within the lumen	689:761	The N-terminal domain serves as a type II signal anchor sequence to recruit NCEH to the endoplasmic reticulum (ER) with its catalytic domain within the lumen.
19592704	2	14	gly	glycosylation	382:394	arg1	series					420:425	a series	418:425	a series of NCEH mutants expressed in macrophages	418:466	Here, we determined subcellular localization, glycosylation, and nCEH activity of a series of NCEH mutants expressed in macrophages.
19592704	8	15	theme	macrophages	1138:1148	arg1	ER					1132:1133	the ER	1128:1133	the ER	1128:1133	In conclusion, NCEH is targeted to the ER of macrophages, where it hydrolyzes CE to deliver cholesterol for efflux out of the cells.
19592704	6	16	theme	serine	943:948	arg1	motif					950:954	the catalytic serine motif	929:954	the catalytic serine motif	929:954	Glycosylation at Asn(270), which is located closest to the catalytic serine motif, is important for the enzymatic activity.
19592704	4	17	theme	signal	647:652	arg1	domain					620:625	The N-terminal domain	605:625	The N-terminal domain	605:625	The N-terminal domain serves as a type II signal anchor sequence to recruit NCEH to the endoplasmic reticulum (ER) with its catalytic domain within the lumen.
19592704	4	17	theme	signal	647:652	arg1	sequence					661:668	a type II signal anchor sequence	637:668	a type II signal anchor sequence	637:668	The N-terminal domain serves as a type II signal anchor sequence to recruit NCEH to the endoplasmic reticulum (ER) with its catalytic domain within the lumen.
19592704	7	18	theme	ER	1068:1069	arg1	localization					1071:1082	the ER localization	1064:1082	the ER localization of NCEH	1064:1090	Cholesterol loading by incubation with acetyl-LDL does not change the ER localization of NCEH.
19592704	1	19	theme	large	165:169	arg1	part					171:174	a large part	163:174	a large part of the nCEH activity in macrophage foam cells, a hallmark of atherosclerosis	163:251	Neutral cholesterol ester hydrolase (NCEH) accounts for a large part of the nCEH activity in macrophage foam cells, a hallmark of atherosclerosis, but its subcellular localization and structure-function relationship are unknown.
19592704	2	20	theme	NCEH	430:433	arg1	mutants					435:441	NCEH mutants	430:441	NCEH mutants expressed in macrophages	430:466	Here, we determined subcellular localization, glycosylation, and nCEH activity of a series of NCEH mutants expressed in macrophages.
19592704	6	21	gly	Glycosylation	874:886	arg2	270					895:897	270	895:897	270	895:897	Glycosylation at Asn(270), which is located closest to the catalytic serine motif, is important for the enzymatic activity.
19592704	6	21	gly	Glycosylation	874:886	arg2	Asn					891:893	Asn	891:893	Asn(270)	891:898	Glycosylation at Asn(270), which is located closest to the catalytic serine motif, is important for the enzymatic activity.
19592704	4	22	theme	type	639:642	arg1	domain					620:625	The N-terminal domain	605:625	The N-terminal domain	605:625	The N-terminal domain serves as a type II signal anchor sequence to recruit NCEH to the endoplasmic reticulum (ER) with its catalytic domain within the lumen.
19592704	4	22	theme	type	639:642	arg1	sequence					661:668	a type II signal anchor sequence	637:668	a type II signal anchor sequence	637:668	The N-terminal domain serves as a type II signal anchor sequence to recruit NCEH to the endoplasmic reticulum (ER) with its catalytic domain within the lumen.
19592704	5	23	theme	putative	775:782	arg1	Asn					814:816	Asn(270)	814:821	Asn(270)	814:821	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	23	theme	putative	775:782	arg1	Asn					838:840	Asn	838:840	Asn(389)	838:845	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	23	theme	putative	775:782	arg1	sites					807:811	the putative N-linked glycosylation sites	771:811	the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH	771:854	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	23	theme	putative	775:782	arg1	NCEH					851:854	NCEH	851:854	NCEH	851:854	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	23	theme	putative	775:782	arg1	Asn					824:826	Asn	824:826	Asn(367)	824:831	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	3	24	theme	catalytic	567:575	arg1	domains					596:602	N-terminal, catalytic, and lipid-binding domains	555:602	three domains: N-terminal, catalytic, and lipid-binding domains	540:602	NCEH is a single-membrane-spanning type II membrane protein comprising three domains: N-terminal, catalytic, and lipid-binding domains.
19592704	4	25	theme	anchor	654:659	arg1	domain					620:625	The N-terminal domain	605:625	The N-terminal domain	605:625	The N-terminal domain serves as a type II signal anchor sequence to recruit NCEH to the endoplasmic reticulum (ER) with its catalytic domain within the lumen.
19592704	4	25	theme	anchor	654:659	arg1	sequence					661:668	a type II signal anchor sequence	637:668	a type II signal anchor sequence	637:668	The N-terminal domain serves as a type II signal anchor sequence to recruit NCEH to the endoplasmic reticulum (ER) with its catalytic domain within the lumen.
19592704	0	26	theme	cholesterol	21:31	arg1	hydrolase					39:47	neutral cholesterol ester hydrolase	13:47	neutral cholesterol ester hydrolase	13:47	Targeting of neutral cholesterol ester hydrolase to the endoplasmic reticulum via its N-terminal sequence.
19592704	0	27	theme	neutral	13:19	arg1	hydrolase					39:47	neutral cholesterol ester hydrolase	13:47	neutral cholesterol ester hydrolase	13:47	Targeting of neutral cholesterol ester hydrolase to the endoplasmic reticulum via its N-terminal sequence.
19592704	1	28	theme	Neutral	107:113	arg1	hydrolase					133:141	Neutral cholesterol ester hydrolase	107:141	Neutral cholesterol ester hydrolase (NCEH)	107:148	Neutral cholesterol ester hydrolase (NCEH) accounts for a large part of the nCEH activity in macrophage foam cells, a hallmark of atherosclerosis, but its subcellular localization and structure-function relationship are unknown.
19592704	1	28	theme	Neutral	107:113	arg1	NCEH					144:147	NCEH	144:147	NCEH	144:147	Neutral cholesterol ester hydrolase (NCEH) accounts for a large part of the nCEH activity in macrophage foam cells, a hallmark of atherosclerosis, but its subcellular localization and structure-function relationship are unknown.
19592704	1	29	theme	nCEH	183:186	arg1	activity					188:195	the nCEH activity	179:195	the nCEH activity in macrophage foam cells, a hallmark of atherosclerosis	179:251	Neutral cholesterol ester hydrolase (NCEH) accounts for a large part of the nCEH activity in macrophage foam cells, a hallmark of atherosclerosis, but its subcellular localization and structure-function relationship are unknown.
19592704	0	30	theme	hydrolase	39:47	arg1	Targeting					0:8	Targeting	0:8	Targeting of neutral cholesterol ester hydrolase to the endoplasmic reticulum via its N-terminal sequence	0:104	Targeting of neutral cholesterol ester hydrolase to the endoplasmic reticulum via its N-terminal sequence.
19592704	1	31	theme	subcellular	262:272	arg1	localization					274:285	subcellular localization	262:285	subcellular localization	262:285	Neutral cholesterol ester hydrolase (NCEH) accounts for a large part of the nCEH activity in macrophage foam cells, a hallmark of atherosclerosis, but its subcellular localization and structure-function relationship are unknown.
19592704	2	32	theme	nCEH	401:404	arg1	activity					406:413	nCEH activity	401:413	nCEH activity	401:413	Here, we determined subcellular localization, glycosylation, and nCEH activity of a series of NCEH mutants expressed in macrophages.
19592704	3	33	theme	lipid-binding	582:594	arg1	domains					596:602	N-terminal, catalytic, and lipid-binding domains	555:602	three domains: N-terminal, catalytic, and lipid-binding domains	540:602	NCEH is a single-membrane-spanning type II membrane protein comprising three domains: N-terminal, catalytic, and lipid-binding domains.
19592704	6	34	theme	catalytic	933:941	arg1	motif					950:954	the catalytic serine motif	929:954	the catalytic serine motif	929:954	Glycosylation at Asn(270), which is located closest to the catalytic serine motif, is important for the enzymatic activity.
19592704	1	35	theme	activity	188:195	arg1	part					171:174	a large part	163:174	a large part of the nCEH activity in macrophage foam cells, a hallmark of atherosclerosis	163:251	Neutral cholesterol ester hydrolase (NCEH) accounts for a large part of the nCEH activity in macrophage foam cells, a hallmark of atherosclerosis, but its subcellular localization and structure-function relationship are unknown.
19592704	0	36	theme	ester	33:37	arg1	hydrolase					39:47	neutral cholesterol ester hydrolase	13:47	neutral cholesterol ester hydrolase	13:47	Targeting of neutral cholesterol ester hydrolase to the endoplasmic reticulum via its N-terminal sequence.
19592704	2	37	theme	series	420:425	arg1	glycosylation					382:394	glycosylation	382:394	glycosylation	382:394	Here, we determined subcellular localization, glycosylation, and nCEH activity of a series of NCEH mutants expressed in macrophages.
19592704	2	37	theme	series	420:425	arg1	localization					368:379	subcellular localization	356:379	subcellular localization	356:379	Here, we determined subcellular localization, glycosylation, and nCEH activity of a series of NCEH mutants expressed in macrophages.
19592704	2	37	theme	series	420:425	arg1	activity					406:413	nCEH activity	401:413	nCEH activity	401:413	Here, we determined subcellular localization, glycosylation, and nCEH activity of a series of NCEH mutants expressed in macrophages.
19592704	1	38	from	activity	188:195	arg1	cells					216:220	macrophage foam cells	200:220	macrophage foam cells	200:220	Neutral cholesterol ester hydrolase (NCEH) accounts for a large part of the nCEH activity in macrophage foam cells, a hallmark of atherosclerosis, but its subcellular localization and structure-function relationship are unknown.
19592704	1	38	from	activity	188:195	arg1	hallmark					225:232	a hallmark	223:232	a hallmark of atherosclerosis	223:251	Neutral cholesterol ester hydrolase (NCEH) accounts for a large part of the nCEH activity in macrophage foam cells, a hallmark of atherosclerosis, but its subcellular localization and structure-function relationship are unknown.
19592704	5	39	theme	N-linked	784:791	arg1	Asn					814:816	Asn(270)	814:821	Asn(270)	814:821	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	39	theme	N-linked	784:791	arg1	Asn					838:840	Asn	838:840	Asn(389)	838:845	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	39	theme	N-linked	784:791	arg1	sites					807:811	the putative N-linked glycosylation sites	771:811	the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH	771:854	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	39	theme	N-linked	784:791	arg1	NCEH					851:854	NCEH	851:854	NCEH	851:854	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	39	theme	N-linked	784:791	arg1	Asn					824:826	Asn	824:826	Asn(367)	824:831	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	1	40	from	cells	216:220	arg1	part					171:174	a large part	163:174	a large part of the nCEH activity in macrophage foam cells, a hallmark of atherosclerosis	163:251	Neutral cholesterol ester hydrolase (NCEH) accounts for a large part of the nCEH activity in macrophage foam cells, a hallmark of atherosclerosis, but its subcellular localization and structure-function relationship are unknown.
19592704	5	41	gly	glycosylation	793:805	arg2	Asn					824:826	Asn	824:826	Asn(367)	824:831	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	41	gly	glycosylation	793:805	arg2	Asn					838:840	Asn	838:840	Asn(389)	838:845	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	41	gly	glycosylation	793:805	arg2	NCEH					851:854	NCEH	851:854	NCEH	851:854	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	41	gly	glycosylation	793:805	arg2	sites					807:811	the putative N-linked glycosylation sites	771:811	the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH	771:854	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	41	gly	glycosylation	793:805	arg1	NCEH					851:854	NCEH	851:854	NCEH	851:854	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	41	gly	glycosylation	793:805	arg2	Asn					814:816	Asn(270)	814:821	Asn(270)	814:821	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	1	42	theme	cholesterol	115:125	arg1	hydrolase					133:141	Neutral cholesterol ester hydrolase	107:141	Neutral cholesterol ester hydrolase (NCEH)	107:148	Neutral cholesterol ester hydrolase (NCEH) accounts for a large part of the nCEH activity in macrophage foam cells, a hallmark of atherosclerosis, but its subcellular localization and structure-function relationship are unknown.
19592704	1	42	theme	cholesterol	115:125	arg1	NCEH					144:147	NCEH	144:147	NCEH	144:147	Neutral cholesterol ester hydrolase (NCEH) accounts for a large part of the nCEH activity in macrophage foam cells, a hallmark of atherosclerosis, but its subcellular localization and structure-function relationship are unknown.
19592704	2	43	theme	mutants	435:441	arg1	series					420:425	a series	418:425	a series of NCEH mutants expressed in macrophages	418:466	Here, we determined subcellular localization, glycosylation, and nCEH activity of a series of NCEH mutants expressed in macrophages.
19592704	1	44	theme	structure-function	291:308	arg1	relationship					310:321	structure-function relationship	291:321	structure-function relationship	291:321	Neutral cholesterol ester hydrolase (NCEH) accounts for a large part of the nCEH activity in macrophage foam cells, a hallmark of atherosclerosis, but its subcellular localization and structure-function relationship are unknown.
19592704	1	45	theme	ester	127:131	arg1	hydrolase					133:141	Neutral cholesterol ester hydrolase	107:141	Neutral cholesterol ester hydrolase (NCEH)	107:148	Neutral cholesterol ester hydrolase (NCEH) accounts for a large part of the nCEH activity in macrophage foam cells, a hallmark of atherosclerosis, but its subcellular localization and structure-function relationship are unknown.
19592704	1	45	theme	ester	127:131	arg1	NCEH					144:147	NCEH	144:147	NCEH	144:147	Neutral cholesterol ester hydrolase (NCEH) accounts for a large part of the nCEH activity in macrophage foam cells, a hallmark of atherosclerosis, but its subcellular localization and structure-function relationship are unknown.
19592704	8	46	dep	cells	1219:1223	arg1	out					1208:1210	out	1208:1210	out	1208:1210	In conclusion, NCEH is targeted to the ER of macrophages, where it hydrolyzes CE to deliver cholesterol for efflux out of the cells.
19592704	5	47	link	N-linked	784:791	arg1	Asn					814:816	Asn(270)	814:821	Asn(270)	814:821	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	47	link	N-linked	784:791	arg1	Asn					838:840	Asn	838:840	Asn(389)	838:845	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	47	link	N-linked	784:791	arg1	sites					807:811	the putative N-linked glycosylation sites	771:811	the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH	771:854	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	47	link	N-linked	784:791	arg1	NCEH					851:854	NCEH	851:854	NCEH	851:854	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	47	link	N-linked	784:791	arg1	Asn					824:826	Asn	824:826	Asn(367)	824:831	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	6	48	theme	enzymatic	978:986	arg1	activity					988:995	the enzymatic activity	974:995	the enzymatic activity	974:995	Glycosylation at Asn(270), which is located closest to the catalytic serine motif, is important for the enzymatic activity.
19592704	1	49	theme	macrophage	200:209	arg1	cells					216:220	macrophage foam cells	200:220	macrophage foam cells	200:220	Neutral cholesterol ester hydrolase (NCEH) accounts for a large part of the nCEH activity in macrophage foam cells, a hallmark of atherosclerosis, but its subcellular localization and structure-function relationship are unknown.
19592704	1	49	theme	macrophage	200:209	arg1	hallmark					225:232	a hallmark	223:232	a hallmark of atherosclerosis	223:251	Neutral cholesterol ester hydrolase (NCEH) accounts for a large part of the nCEH activity in macrophage foam cells, a hallmark of atherosclerosis, but its subcellular localization and structure-function relationship are unknown.
19592704	1	50	from	part	171:174	arg1	cells					216:220	macrophage foam cells	200:220	macrophage foam cells	200:220	Neutral cholesterol ester hydrolase (NCEH) accounts for a large part of the nCEH activity in macrophage foam cells, a hallmark of atherosclerosis, but its subcellular localization and structure-function relationship are unknown.
19592704	1	50	from	part	171:174	arg1	hallmark					225:232	a hallmark	223:232	a hallmark of atherosclerosis	223:251	Neutral cholesterol ester hydrolase (NCEH) accounts for a large part of the nCEH activity in macrophage foam cells, a hallmark of atherosclerosis, but its subcellular localization and structure-function relationship are unknown.
19592704	3	51	dep	domains	546:552	arg1	domains					596:602	N-terminal, catalytic, and lipid-binding domains	555:602	three domains: N-terminal, catalytic, and lipid-binding domains	540:602	NCEH is a single-membrane-spanning type II membrane protein comprising three domains: N-terminal, catalytic, and lipid-binding domains.
19592704	1	52	theme	foam	211:214	arg1	cells					216:220	macrophage foam cells	200:220	macrophage foam cells	200:220	Neutral cholesterol ester hydrolase (NCEH) accounts for a large part of the nCEH activity in macrophage foam cells, a hallmark of atherosclerosis, but its subcellular localization and structure-function relationship are unknown.
19592704	1	52	theme	foam	211:214	arg1	hallmark					225:232	a hallmark	223:232	a hallmark of atherosclerosis	223:251	Neutral cholesterol ester hydrolase (NCEH) accounts for a large part of the nCEH activity in macrophage foam cells, a hallmark of atherosclerosis, but its subcellular localization and structure-function relationship are unknown.
19592704	5	53	gly	glycosylated	860:871	arg1	All					764:766	All	764:766	All	764:766	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	53	gly	glycosylated	860:871	arg1	Asn					838:840	Asn	838:840	Asn(389)	838:845	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	53	gly	glycosylated	860:871	arg1	sites					807:811	the putative N-linked glycosylation sites	771:811	the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH	771:854	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	53	gly	glycosylated	860:871	arg1	Asn					814:816	Asn(270)	814:821	Asn(270)	814:821	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	53	gly	glycosylated	860:871	arg1	NCEH					851:854	NCEH	851:854	NCEH	851:854	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	53	gly	glycosylated	860:871	arg1	Asn					824:826	Asn	824:826	Asn(367)	824:831	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	54	dep	sites	807:811	arg1	Asn					838:840	Asn	838:840	Asn(389)	838:845	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	54	dep	sites	807:811	arg1	sites					807:811	the putative N-linked glycosylation sites	771:811	the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH	771:854	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	54	dep	sites	807:811	arg1	389					842:844	389	842:844	389	842:844	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	54	dep	sites	807:811	arg1	Asn					814:816	Asn(270)	814:821	Asn(270)	814:821	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	54	dep	sites	807:811	arg1	367					828:830	367	828:830	367	828:830	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	54	dep	sites	807:811	arg1	NCEH					851:854	NCEH	851:854	NCEH	851:854	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	54	dep	sites	807:811	arg1	Asn					824:826	Asn	824:826	Asn(367)	824:831	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	2	55	theme	subcellular	356:366	arg1	localization					368:379	subcellular localization	356:379	subcellular localization	356:379	Here, we determined subcellular localization, glycosylation, and nCEH activity of a series of NCEH mutants expressed in macrophages.
19592704	4	56	theme	II	644:645	arg1	domain					620:625	The N-terminal domain	605:625	The N-terminal domain	605:625	The N-terminal domain serves as a type II signal anchor sequence to recruit NCEH to the endoplasmic reticulum (ER) with its catalytic domain within the lumen.
19592704	4	56	theme	II	644:645	arg1	sequence					661:668	a type II signal anchor sequence	637:668	a type II signal anchor sequence	637:668	The N-terminal domain serves as a type II signal anchor sequence to recruit NCEH to the endoplasmic reticulum (ER) with its catalytic domain within the lumen.
19592704	0	57	theme	endoplasmic	56:66	arg1	reticulum					68:76	the endoplasmic reticulum	52:76	the endoplasmic reticulum via its N-terminal sequence	52:104	Targeting of neutral cholesterol ester hydrolase to the endoplasmic reticulum via its N-terminal sequence.
19592704	5	58	theme	glycosylation	793:805	arg1	Asn					814:816	Asn(270)	814:821	Asn(270)	814:821	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	58	theme	glycosylation	793:805	arg1	Asn					838:840	Asn	838:840	Asn(389)	838:845	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	58	theme	glycosylation	793:805	arg1	sites					807:811	the putative N-linked glycosylation sites	771:811	the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH	771:854	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	58	theme	glycosylation	793:805	arg1	NCEH					851:854	NCEH	851:854	NCEH	851:854	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	5	58	theme	glycosylation	793:805	arg1	Asn					824:826	Asn	824:826	Asn(367)	824:831	All of the putative N-linked glycosylation sites (Asn(270), Asn(367), and Asn(389)) of NCEH are glycosylated.
19592704	3	59	theme	membrane	512:519	arg1	protein					521:527	a single-membrane-spanning type II membrane protein	477:527	a single-membrane-spanning type II membrane protein comprising three domains: N-terminal, catalytic, and lipid-binding domains	477:602	NCEH is a single-membrane-spanning type II membrane protein comprising three domains: N-terminal, catalytic, and lipid-binding domains.
19592704	3	59	theme	membrane	512:519	arg1	NCEH					469:472	NCEH	469:472	NCEH	469:472	NCEH is a single-membrane-spanning type II membrane protein comprising three domains: N-terminal, catalytic, and lipid-binding domains.
19592704	4	60	theme	N-terminal	609:618	arg1	sequence					661:668	a type II signal anchor sequence	637:668	a type II signal anchor sequence	637:668	The N-terminal domain serves as a type II signal anchor sequence to recruit NCEH to the endoplasmic reticulum (ER) with its catalytic domain within the lumen.
19592704	4	60	theme	N-terminal	609:618	arg1	domain					620:625	The N-terminal domain	605:625	The N-terminal domain	605:625	The N-terminal domain serves as a type II signal anchor sequence to recruit NCEH to the endoplasmic reticulum (ER) with its catalytic domain within the lumen.
15536627	0	0	theme	mass	117:120	arg1	spectrometry					122:133	nano-flow liquid chromatography/electrospray ionization mass spectrometry	61:133	nano-flow liquid chromatography/electrospray ionization mass spectrometry	61:133	Site-specific carbohydrate profiling of human transferrin by nano-flow liquid chromatography/electrospray ionization mass spectrometry.
15536627	4	1	theme	structural	1059:1068	arg1	read-out					1070:1077	the structural read-out	1055:1077	the structural read-out of a small minority of the carbohydrate moieties	1055:1126	Nano-flow ESI tandem mass spectrometry (MS/MS) of the glycopeptides (Cys421-Lys433 and Ile619-Lys646) containing these two sites yielded predominantly ions originating from the non-reducing termini (oxonium ions) and reducing terminus, resulting from cleavage of the glycosidic bonds of the carbohydrate moieties; this permitted the structural read-out of a small minority of the carbohydrate moieties.
15536627	1	2	from	Asn630	395:400	arg1	profiles					372:379	the carbohydrate profiles	355:379	the carbohydrate profiles at Asn432 and Asn630	355:400	Glycopeptides derived from a lysylendopeptidase digest of commercially available human transferrin were analyzed by nano-flow liquid chromatography/electrospray ionization mass spectrometry (LC/ESI-MS), which permitted the carbohydrate profiles at Asn432 and Asn630 to be determined.
15536627	1	3	theme	available	207:215	arg1	transferrin					223:233	commercially available human transferrin	194:233	commercially available human transferrin	194:233	Glycopeptides derived from a lysylendopeptidase digest of commercially available human transferrin were analyzed by nano-flow liquid chromatography/electrospray ionization mass spectrometry (LC/ESI-MS), which permitted the carbohydrate profiles at Asn432 and Asn630 to be determined.
15536627	4	4	theme	moieties	1119:1126	arg1	minority					1090:1097	a small minority	1082:1097	a small minority of the carbohydrate moieties	1082:1126	Nano-flow ESI tandem mass spectrometry (MS/MS) of the glycopeptides (Cys421-Lys433 and Ile619-Lys646) containing these two sites yielded predominantly ions originating from the non-reducing termini (oxonium ions) and reducing terminus, resulting from cleavage of the glycosidic bonds of the carbohydrate moieties; this permitted the structural read-out of a small minority of the carbohydrate moieties.
15536627	0	5	theme	ionization	106:115	arg1	spectrometry					122:133	nano-flow liquid chromatography/electrospray ionization mass spectrometry	61:133	nano-flow liquid chromatography/electrospray ionization mass spectrometry	61:133	Site-specific carbohydrate profiling of human transferrin by nano-flow liquid chromatography/electrospray ionization mass spectrometry.
15536627	3	6	from	other	583:587	arg1	contents					501:508	The contents	497:508	The contents of the carbohydrates at each site	497:542	The contents of the carbohydrates at each site were significantly different from each other, and consisted of a variety of minor types of oligosaccharides in addition to the major one, a biantennary complex-type oligosaccharide.
15536627	3	6	from	other	583:587	arg1	different					563:571	different	563:571	different	563:571	The contents of the carbohydrates at each site were significantly different from each other, and consisted of a variety of minor types of oligosaccharides in addition to the major one, a biantennary complex-type oligosaccharide.
15536627	1	7	theme	human	217:221	arg1	transferrin					223:233	commercially available human transferrin	194:233	commercially available human transferrin	194:233	Glycopeptides derived from a lysylendopeptidase digest of commercially available human transferrin were analyzed by nano-flow liquid chromatography/electrospray ionization mass spectrometry (LC/ESI-MS), which permitted the carbohydrate profiles at Asn432 and Asn630 to be determined.
15536627	4	8	theme	reducing	943:950	arg1	terminus					952:959	reducing terminus	943:959	reducing terminus	943:959	Nano-flow ESI tandem mass spectrometry (MS/MS) of the glycopeptides (Cys421-Lys433 and Ile619-Lys646) containing these two sites yielded predominantly ions originating from the non-reducing termini (oxonium ions) and reducing terminus, resulting from cleavage of the glycosidic bonds of the carbohydrate moieties; this permitted the structural read-out of a small minority of the carbohydrate moieties.
15536627	4	9	theme	carbohydrate	1017:1028	arg1	moieties					1030:1037	the carbohydrate moieties	1013:1037	the carbohydrate moieties	1013:1037	Nano-flow ESI tandem mass spectrometry (MS/MS) of the glycopeptides (Cys421-Lys433 and Ile619-Lys646) containing these two sites yielded predominantly ions originating from the non-reducing termini (oxonium ions) and reducing terminus, resulting from cleavage of the glycosidic bonds of the carbohydrate moieties; this permitted the structural read-out of a small minority of the carbohydrate moieties.
15536627	2	10	located	located	429:435	arg1	Asn-Xaa-Ser/Thr					480:494	Asn-Xaa-Ser/Thr	480:494	Asn-Xaa-Ser/Thr	480:494	Both are located in a well-known motif for N-glycosylation, Asn-Xaa-Ser/Thr.
15536627	2	10	located	located	429:435	arg2	Both					420:423	Both	420:423	Both	420:423	Both are located in a well-known motif for N-glycosylation, Asn-Xaa-Ser/Thr.
15536627	2	10	located	located	429:435	arg1	motif					453:457	a well-known motif	440:457	a well-known motif for N-glycosylation	440:477	Both are located in a well-known motif for N-glycosylation, Asn-Xaa-Ser/Thr.
15536627	1	11	from	Asn432	384:389	arg1	profiles					372:379	the carbohydrate profiles	355:379	the carbohydrate profiles at Asn432 and Asn630	355:400	Glycopeptides derived from a lysylendopeptidase digest of commercially available human transferrin were analyzed by nano-flow liquid chromatography/electrospray ionization mass spectrometry (LC/ESI-MS), which permitted the carbohydrate profiles at Asn432 and Asn630 to be determined.
15536627	5	12	theme	terminal	1240:1247	arg1	fucosylation					1249:1260	outer non-reducing terminal fucosylation	1221:1260	outer non-reducing terminal fucosylation	1221:1260	In particular, the observation of oxonium ions at m/z 512.2 and 803.2 is useful for probing outer non-reducing terminal fucosylation, which represented carbohydrate structures consisting of Hex, dHex, and HexNAc, and NeuNAc, Hex, dHex, and HexNAc, respectively, from which the Lewis X structure (Galbeta1-4(Fucalpha1-3)GlcNAc) was readily deduced.
15536627	4	13	theme	ESI	736:738	arg1	MS/MS					766:770	MS/MS	766:770	MS/MS	766:770	Nano-flow ESI tandem mass spectrometry (MS/MS) of the glycopeptides (Cys421-Lys433 and Ile619-Lys646) containing these two sites yielded predominantly ions originating from the non-reducing termini (oxonium ions) and reducing terminus, resulting from cleavage of the glycosidic bonds of the carbohydrate moieties; this permitted the structural read-out of a small minority of the carbohydrate moieties.
15536627	4	13	theme	ESI	736:738	arg1	spectrometry					752:763	Nano-flow ESI tandem mass spectrometry	726:763	Nano-flow ESI tandem mass spectrometry (MS/MS) of the glycopeptides (Cys421-Lys433 and Ile619-Lys646) containing these two sites	726:853	Nano-flow ESI tandem mass spectrometry (MS/MS) of the glycopeptides (Cys421-Lys433 and Ile619-Lys646) containing these two sites yielded predominantly ions originating from the non-reducing termini (oxonium ions) and reducing terminus, resulting from cleavage of the glycosidic bonds of the carbohydrate moieties; this permitted the structural read-out of a small minority of the carbohydrate moieties.
15536627	5	14	theme	carbohydrate	1281:1292	arg1	structures					1294:1303	carbohydrate structures	1281:1303	carbohydrate structures consisting of Hex, dHex, and HexNAc, and NeuNAc, Hex, dHex, and HexNAc, respectively	1281:1388	In particular, the observation of oxonium ions at m/z 512.2 and 803.2 is useful for probing outer non-reducing terminal fucosylation, which represented carbohydrate structures consisting of Hex, dHex, and HexNAc, and NeuNAc, Hex, dHex, and HexNAc, respectively, from which the Lewis X structure (Galbeta1-4(Fucalpha1-3)GlcNAc) was readily deduced.
15536627	5	15	theme	oxonium	1163:1169	arg1	ions					1171:1174	oxonium ions	1163:1174	oxonium ions	1163:1174	In particular, the observation of oxonium ions at m/z 512.2 and 803.2 is useful for probing outer non-reducing terminal fucosylation, which represented carbohydrate structures consisting of Hex, dHex, and HexNAc, and NeuNAc, Hex, dHex, and HexNAc, respectively, from which the Lewis X structure (Galbeta1-4(Fucalpha1-3)GlcNAc) was readily deduced.
15536627	5	16	theme	ions	1171:1174	arg1	useful					1202:1207	useful	1202:1207	useful	1202:1207	In particular, the observation of oxonium ions at m/z 512.2 and 803.2 is useful for probing outer non-reducing terminal fucosylation, which represented carbohydrate structures consisting of Hex, dHex, and HexNAc, and NeuNAc, Hex, dHex, and HexNAc, respectively, from which the Lewis X structure (Galbeta1-4(Fucalpha1-3)GlcNAc) was readily deduced.
15536627	5	16	theme	ions	1171:1174	arg1	observation					1148:1158	the observation	1144:1158	the observation of oxonium ions at m/z 512.2 and 803.2	1144:1197	In particular, the observation of oxonium ions at m/z 512.2 and 803.2 is useful for probing outer non-reducing terminal fucosylation, which represented carbohydrate structures consisting of Hex, dHex, and HexNAc, and NeuNAc, Hex, dHex, and HexNAc, respectively, from which the Lewis X structure (Galbeta1-4(Fucalpha1-3)GlcNAc) was readily deduced.
15536627	4	17	theme	oxonium	925:931	arg1	ions					933:936	oxonium ions	925:936	oxonium ions	925:936	Nano-flow ESI tandem mass spectrometry (MS/MS) of the glycopeptides (Cys421-Lys433 and Ile619-Lys646) containing these two sites yielded predominantly ions originating from the non-reducing termini (oxonium ions) and reducing terminus, resulting from cleavage of the glycosidic bonds of the carbohydrate moieties; this permitted the structural read-out of a small minority of the carbohydrate moieties.
15536627	4	17	theme	oxonium	925:931	arg1	termini					916:922	the non-reducing termini	899:922	the non-reducing termini (oxonium ions)	899:937	Nano-flow ESI tandem mass spectrometry (MS/MS) of the glycopeptides (Cys421-Lys433 and Ile619-Lys646) containing these two sites yielded predominantly ions originating from the non-reducing termini (oxonium ions) and reducing terminus, resulting from cleavage of the glycosidic bonds of the carbohydrate moieties; this permitted the structural read-out of a small minority of the carbohydrate moieties.
15536627	5	18	theme	Fucalpha1-3	1436:1446	arg1	structure					1414:1422	the Lewis X structure	1402:1422	the Lewis X structure (Galbeta1-4(Fucalpha1-3)GlcNAc)	1402:1454	In particular, the observation of oxonium ions at m/z 512.2 and 803.2 is useful for probing outer non-reducing terminal fucosylation, which represented carbohydrate structures consisting of Hex, dHex, and HexNAc, and NeuNAc, Hex, dHex, and HexNAc, respectively, from which the Lewis X structure (Galbeta1-4(Fucalpha1-3)GlcNAc) was readily deduced.
15536627	5	18	theme	Fucalpha1-3	1436:1446	arg1	GlcNAc					1448:1453	Galbeta1-4(Fucalpha1-3)GlcNAc	1425:1453	Galbeta1-4(Fucalpha1-3)GlcNAc	1425:1453	In particular, the observation of oxonium ions at m/z 512.2 and 803.2 is useful for probing outer non-reducing terminal fucosylation, which represented carbohydrate structures consisting of Hex, dHex, and HexNAc, and NeuNAc, Hex, dHex, and HexNAc, respectively, from which the Lewis X structure (Galbeta1-4(Fucalpha1-3)GlcNAc) was readily deduced.
15536627	6	19	from	GlcNAc	1525:1530	arg1	fucosylation					1487:1498	fucosylation	1487:1498	fucosylation at the reducing-terminal GlcNAc (Fucalpha1-6GlcNAc)	1487:1550	Moreover, fucosylation at the reducing-terminal GlcNAc (Fucalpha1-6GlcNAc) specifically occurred at Asn630, as demonstrated by treatment of the glycopeptides with alpha1-3/4-L-fucosidase.
15536627	1	20	theme	transferrin	223:233	arg1	digest					184:189	a lysylendopeptidase digest	163:189	a lysylendopeptidase digest of commercially available human transferrin	163:233	Glycopeptides derived from a lysylendopeptidase digest of commercially available human transferrin were analyzed by nano-flow liquid chromatography/electrospray ionization mass spectrometry (LC/ESI-MS), which permitted the carbohydrate profiles at Asn432 and Asn630 to be determined.
15536627	4	21	theme	moieties	1030:1037	arg1	bonds					1004:1008	the glycosidic bonds	989:1008	the glycosidic bonds of the carbohydrate moieties	989:1037	Nano-flow ESI tandem mass spectrometry (MS/MS) of the glycopeptides (Cys421-Lys433 and Ile619-Lys646) containing these two sites yielded predominantly ions originating from the non-reducing termini (oxonium ions) and reducing terminus, resulting from cleavage of the glycosidic bonds of the carbohydrate moieties; this permitted the structural read-out of a small minority of the carbohydrate moieties.
15536627	6	22	gly	fucosylation	1487:1498	arg2	Asn630					1577:1582	Asn630	1577:1582	Asn630	1577:1582	Moreover, fucosylation at the reducing-terminal GlcNAc (Fucalpha1-6GlcNAc) specifically occurred at Asn630, as demonstrated by treatment of the glycopeptides with alpha1-3/4-L-fucosidase.
15536627	6	22	gly	fucosylation	1487:1498	arg1	Fucalpha1-6GlcNAc					1533:1549	Fucalpha1-6GlcNAc	1533:1549	Fucalpha1-6GlcNAc	1533:1549	Moreover, fucosylation at the reducing-terminal GlcNAc (Fucalpha1-6GlcNAc) specifically occurred at Asn630, as demonstrated by treatment of the glycopeptides with alpha1-3/4-L-fucosidase.
15536627	6	22	gly	fucosylation	1487:1498	arg1	GlcNAc					1525:1530	the reducing-terminal GlcNAc	1503:1530	the reducing-terminal GlcNAc (Fucalpha1-6GlcNAc)	1503:1550	Moreover, fucosylation at the reducing-terminal GlcNAc (Fucalpha1-6GlcNAc) specifically occurred at Asn630, as demonstrated by treatment of the glycopeptides with alpha1-3/4-L-fucosidase.
15536627	5	23	from	803.2	1193:1197	arg1	useful					1202:1207	useful	1202:1207	useful	1202:1207	In particular, the observation of oxonium ions at m/z 512.2 and 803.2 is useful for probing outer non-reducing terminal fucosylation, which represented carbohydrate structures consisting of Hex, dHex, and HexNAc, and NeuNAc, Hex, dHex, and HexNAc, respectively, from which the Lewis X structure (Galbeta1-4(Fucalpha1-3)GlcNAc) was readily deduced.
15536627	5	23	from	803.2	1193:1197	arg1	observation					1148:1158	the observation	1144:1158	the observation of oxonium ions at m/z 512.2 and 803.2	1144:1197	In particular, the observation of oxonium ions at m/z 512.2 and 803.2 is useful for probing outer non-reducing terminal fucosylation, which represented carbohydrate structures consisting of Hex, dHex, and HexNAc, and NeuNAc, Hex, dHex, and HexNAc, respectively, from which the Lewis X structure (Galbeta1-4(Fucalpha1-3)GlcNAc) was readily deduced.
15536627	2	24	from	located	429:435	arg1	Asn-Xaa-Ser/Thr					480:494	Asn-Xaa-Ser/Thr	480:494	Asn-Xaa-Ser/Thr	480:494	Both are located in a well-known motif for N-glycosylation, Asn-Xaa-Ser/Thr.
15536627	2	24	from	located	429:435	arg1	motif					453:457	a well-known motif	440:457	a well-known motif for N-glycosylation	440:477	Both are located in a well-known motif for N-glycosylation, Asn-Xaa-Ser/Thr.
15536627	4	25	theme	minority	1090:1097	arg1	read-out					1070:1077	the structural read-out	1055:1077	the structural read-out of a small minority of the carbohydrate moieties	1055:1126	Nano-flow ESI tandem mass spectrometry (MS/MS) of the glycopeptides (Cys421-Lys433 and Ile619-Lys646) containing these two sites yielded predominantly ions originating from the non-reducing termini (oxonium ions) and reducing terminus, resulting from cleavage of the glycosidic bonds of the carbohydrate moieties; this permitted the structural read-out of a small minority of the carbohydrate moieties.
15536627	3	26	theme	carbohydrates	517:529	arg1	contents					501:508	The contents	497:508	The contents of the carbohydrates at each site	497:542	The contents of the carbohydrates at each site were significantly different from each other, and consisted of a variety of minor types of oligosaccharides in addition to the major one, a biantennary complex-type oligosaccharide.
15536627	3	26	theme	carbohydrates	517:529	arg1	different					563:571	different	563:571	different	563:571	The contents of the carbohydrates at each site were significantly different from each other, and consisted of a variety of minor types of oligosaccharides in addition to the major one, a biantennary complex-type oligosaccharide.
15536627	0	27	theme	carbohydrate	14:25	arg1	profiling					27:35	Site-specific carbohydrate profiling	0:35	Site-specific carbohydrate profiling of human transferrin by nano-flow liquid chromatography/electrospray ionization mass spectrometry	0:133	Site-specific carbohydrate profiling of human transferrin by nano-flow liquid chromatography/electrospray ionization mass spectrometry.
15536627	4	28	theme	mass	747:750	arg1	MS/MS					766:770	MS/MS	766:770	MS/MS	766:770	Nano-flow ESI tandem mass spectrometry (MS/MS) of the glycopeptides (Cys421-Lys433 and Ile619-Lys646) containing these two sites yielded predominantly ions originating from the non-reducing termini (oxonium ions) and reducing terminus, resulting from cleavage of the glycosidic bonds of the carbohydrate moieties; this permitted the structural read-out of a small minority of the carbohydrate moieties.
15536627	4	28	theme	mass	747:750	arg1	spectrometry					752:763	Nano-flow ESI tandem mass spectrometry	726:763	Nano-flow ESI tandem mass spectrometry (MS/MS) of the glycopeptides (Cys421-Lys433 and Ile619-Lys646) containing these two sites	726:853	Nano-flow ESI tandem mass spectrometry (MS/MS) of the glycopeptides (Cys421-Lys433 and Ile619-Lys646) containing these two sites yielded predominantly ions originating from the non-reducing termini (oxonium ions) and reducing terminus, resulting from cleavage of the glycosidic bonds of the carbohydrate moieties; this permitted the structural read-out of a small minority of the carbohydrate moieties.
15536627	0	29	theme	Site-specific	0:12	arg1	profiling					27:35	Site-specific carbohydrate profiling	0:35	Site-specific carbohydrate profiling of human transferrin by nano-flow liquid chromatography/electrospray ionization mass spectrometry	0:133	Site-specific carbohydrate profiling of human transferrin by nano-flow liquid chromatography/electrospray ionization mass spectrometry.
15536627	5	30	theme	non-reducing	1227:1238	arg1	fucosylation					1249:1260	outer non-reducing terminal fucosylation	1221:1260	outer non-reducing terminal fucosylation	1221:1260	In particular, the observation of oxonium ions at m/z 512.2 and 803.2 is useful for probing outer non-reducing terminal fucosylation, which represented carbohydrate structures consisting of Hex, dHex, and HexNAc, and NeuNAc, Hex, dHex, and HexNAc, respectively, from which the Lewis X structure (Galbeta1-4(Fucalpha1-3)GlcNAc) was readily deduced.
15536627	4	31	theme	small	1084:1088	arg1	minority					1090:1097	a small minority	1082:1097	a small minority of the carbohydrate moieties	1082:1126	Nano-flow ESI tandem mass spectrometry (MS/MS) of the glycopeptides (Cys421-Lys433 and Ile619-Lys646) containing these two sites yielded predominantly ions originating from the non-reducing termini (oxonium ions) and reducing terminus, resulting from cleavage of the glycosidic bonds of the carbohydrate moieties; this permitted the structural read-out of a small minority of the carbohydrate moieties.
15536627	3	32	theme	oligosaccharides	635:650	arg1	types					626:630	minor types	620:630	minor types of oligosaccharides in addition to the major one, a biantennary complex-type oligosaccharide	620:723	The contents of the carbohydrates at each site were significantly different from each other, and consisted of a variety of minor types of oligosaccharides in addition to the major one, a biantennary complex-type oligosaccharide.
15536627	2	33	theme	well-known	442:451	arg1	Asn-Xaa-Ser/Thr					480:494	Asn-Xaa-Ser/Thr	480:494	Asn-Xaa-Ser/Thr	480:494	Both are located in a well-known motif for N-glycosylation, Asn-Xaa-Ser/Thr.
15536627	2	33	theme	well-known	442:451	arg1	motif					453:457	a well-known motif	440:457	a well-known motif for N-glycosylation	440:477	Both are located in a well-known motif for N-glycosylation, Asn-Xaa-Ser/Thr.
15536627	4	34	theme	carbohydrate	1106:1117	arg1	moieties					1119:1126	the carbohydrate moieties	1102:1126	the carbohydrate moieties	1102:1126	Nano-flow ESI tandem mass spectrometry (MS/MS) of the glycopeptides (Cys421-Lys433 and Ile619-Lys646) containing these two sites yielded predominantly ions originating from the non-reducing termini (oxonium ions) and reducing terminus, resulting from cleavage of the glycosidic bonds of the carbohydrate moieties; this permitted the structural read-out of a small minority of the carbohydrate moieties.
15536627	1	35	theme	carbohydrate	359:370	arg1	profiles					372:379	the carbohydrate profiles	355:379	the carbohydrate profiles at Asn432 and Asn630	355:400	Glycopeptides derived from a lysylendopeptidase digest of commercially available human transferrin were analyzed by nano-flow liquid chromatography/electrospray ionization mass spectrometry (LC/ESI-MS), which permitted the carbohydrate profiles at Asn432 and Asn630 to be determined.
15536627	4	36	contain	containing	828:837	arg2	sites					849:853	these two sites	839:853	these two sites	839:853	Nano-flow ESI tandem mass spectrometry (MS/MS) of the glycopeptides (Cys421-Lys433 and Ile619-Lys646) containing these two sites yielded predominantly ions originating from the non-reducing termini (oxonium ions) and reducing terminus, resulting from cleavage of the glycosidic bonds of the carbohydrate moieties; this permitted the structural read-out of a small minority of the carbohydrate moieties.
15536627	4	36	contain	containing	828:837	arg1	Ile619-Lys646					813:825	Ile619-Lys646	813:825	Ile619-Lys646	813:825	Nano-flow ESI tandem mass spectrometry (MS/MS) of the glycopeptides (Cys421-Lys433 and Ile619-Lys646) containing these two sites yielded predominantly ions originating from the non-reducing termini (oxonium ions) and reducing terminus, resulting from cleavage of the glycosidic bonds of the carbohydrate moieties; this permitted the structural read-out of a small minority of the carbohydrate moieties.
15536627	4	36	contain	containing	828:837	arg1	Cys421-Lys433					795:807	Cys421-Lys433	795:807	Cys421-Lys433	795:807	Nano-flow ESI tandem mass spectrometry (MS/MS) of the glycopeptides (Cys421-Lys433 and Ile619-Lys646) containing these two sites yielded predominantly ions originating from the non-reducing termini (oxonium ions) and reducing terminus, resulting from cleavage of the glycosidic bonds of the carbohydrate moieties; this permitted the structural read-out of a small minority of the carbohydrate moieties.
15536627	4	36	contain	containing	828:837	arg1	glycopeptides					780:792	the glycopeptides	776:792	the glycopeptides (Cys421-Lys433 and Ile619-Lys646) containing these two sites	776:853	Nano-flow ESI tandem mass spectrometry (MS/MS) of the glycopeptides (Cys421-Lys433 and Ile619-Lys646) containing these two sites yielded predominantly ions originating from the non-reducing termini (oxonium ions) and reducing terminus, resulting from cleavage of the glycosidic bonds of the carbohydrate moieties; this permitted the structural read-out of a small minority of the carbohydrate moieties.
15536627	3	37	theme	minor	620:624	arg1	types					626:630	minor types	620:630	minor types of oligosaccharides in addition to the major one, a biantennary complex-type oligosaccharide	620:723	The contents of the carbohydrates at each site were significantly different from each other, and consisted of a variety of minor types of oligosaccharides in addition to the major one, a biantennary complex-type oligosaccharide.
15536627	1	38	theme	nano-flow	252:260	arg1	LC/ESI-MS					327:335	LC/ESI-MS	327:335	LC/ESI-MS	327:335	Glycopeptides derived from a lysylendopeptidase digest of commercially available human transferrin were analyzed by nano-flow liquid chromatography/electrospray ionization mass spectrometry (LC/ESI-MS), which permitted the carbohydrate profiles at Asn432 and Asn630 to be determined.
15536627	1	38	theme	nano-flow	252:260	arg1	spectrometry					313:324	nano-flow liquid chromatography/electrospray ionization mass spectrometry	252:324	nano-flow liquid chromatography/electrospray ionization mass spectrometry (LC/ESI-MS)	252:336	Glycopeptides derived from a lysylendopeptidase digest of commercially available human transferrin were analyzed by nano-flow liquid chromatography/electrospray ionization mass spectrometry (LC/ESI-MS), which permitted the carbohydrate profiles at Asn432 and Asn630 to be determined.
15536627	4	39	dep	glycopeptides	780:792	arg1	Ile619-Lys646					813:825	Ile619-Lys646	813:825	Ile619-Lys646	813:825	Nano-flow ESI tandem mass spectrometry (MS/MS) of the glycopeptides (Cys421-Lys433 and Ile619-Lys646) containing these two sites yielded predominantly ions originating from the non-reducing termini (oxonium ions) and reducing terminus, resulting from cleavage of the glycosidic bonds of the carbohydrate moieties; this permitted the structural read-out of a small minority of the carbohydrate moieties.
15536627	4	39	dep	glycopeptides	780:792	arg1	Cys421-Lys433					795:807	Cys421-Lys433	795:807	Cys421-Lys433	795:807	Nano-flow ESI tandem mass spectrometry (MS/MS) of the glycopeptides (Cys421-Lys433 and Ile619-Lys646) containing these two sites yielded predominantly ions originating from the non-reducing termini (oxonium ions) and reducing terminus, resulting from cleavage of the glycosidic bonds of the carbohydrate moieties; this permitted the structural read-out of a small minority of the carbohydrate moieties.
15536627	4	39	dep	glycopeptides	780:792	arg1	glycopeptides					780:792	the glycopeptides	776:792	the glycopeptides (Cys421-Lys433 and Ile619-Lys646) containing these two sites	776:853	Nano-flow ESI tandem mass spectrometry (MS/MS) of the glycopeptides (Cys421-Lys433 and Ile619-Lys646) containing these two sites yielded predominantly ions originating from the non-reducing termini (oxonium ions) and reducing terminus, resulting from cleavage of the glycosidic bonds of the carbohydrate moieties; this permitted the structural read-out of a small minority of the carbohydrate moieties.
15536627	3	40	theme	types	626:630	arg1	variety					609:615	a variety	607:615	a variety of minor types of oligosaccharides in addition to the major one, a biantennary complex-type oligosaccharide	607:723	The contents of the carbohydrates at each site were significantly different from each other, and consisted of a variety of minor types of oligosaccharides in addition to the major one, a biantennary complex-type oligosaccharide.
15536627	3	40	theme	types	626:630	arg1	types					626:630	minor types	620:630	minor types of oligosaccharides in addition to the major one, a biantennary complex-type oligosaccharide	620:723	The contents of the carbohydrates at each site were significantly different from each other, and consisted of a variety of minor types of oligosaccharides in addition to the major one, a biantennary complex-type oligosaccharide.
15536627	1	41	theme	liquid	262:267	arg1	LC/ESI-MS					327:335	LC/ESI-MS	327:335	LC/ESI-MS	327:335	Glycopeptides derived from a lysylendopeptidase digest of commercially available human transferrin were analyzed by nano-flow liquid chromatography/electrospray ionization mass spectrometry (LC/ESI-MS), which permitted the carbohydrate profiles at Asn432 and Asn630 to be determined.
15536627	1	41	theme	liquid	262:267	arg1	spectrometry					313:324	nano-flow liquid chromatography/electrospray ionization mass spectrometry	252:324	nano-flow liquid chromatography/electrospray ionization mass spectrometry (LC/ESI-MS)	252:336	Glycopeptides derived from a lysylendopeptidase digest of commercially available human transferrin were analyzed by nano-flow liquid chromatography/electrospray ionization mass spectrometry (LC/ESI-MS), which permitted the carbohydrate profiles at Asn432 and Asn630 to be determined.
15536627	0	42	theme	transferrin	46:56	arg1	profiling					27:35	Site-specific carbohydrate profiling	0:35	Site-specific carbohydrate profiling of human transferrin by nano-flow liquid chromatography/electrospray ionization mass spectrometry	0:133	Site-specific carbohydrate profiling of human transferrin by nano-flow liquid chromatography/electrospray ionization mass spectrometry.
15536627	4	43	gly	glycopeptides	780:792	arg2	Cys421-Lys433					795:807	Cys421-Lys433	795:807	Cys421-Lys433	795:807	Nano-flow ESI tandem mass spectrometry (MS/MS) of the glycopeptides (Cys421-Lys433 and Ile619-Lys646) containing these two sites yielded predominantly ions originating from the non-reducing termini (oxonium ions) and reducing terminus, resulting from cleavage of the glycosidic bonds of the carbohydrate moieties; this permitted the structural read-out of a small minority of the carbohydrate moieties.
15536627	4	43	gly	glycopeptides	780:792	arg2	glycopeptides					780:792	the glycopeptides	776:792	the glycopeptides (Cys421-Lys433 and Ile619-Lys646) containing these two sites	776:853	Nano-flow ESI tandem mass spectrometry (MS/MS) of the glycopeptides (Cys421-Lys433 and Ile619-Lys646) containing these two sites yielded predominantly ions originating from the non-reducing termini (oxonium ions) and reducing terminus, resulting from cleavage of the glycosidic bonds of the carbohydrate moieties; this permitted the structural read-out of a small minority of the carbohydrate moieties.
15536627	4	43	gly	glycopeptides	780:792	arg2	Ile619-Lys646					813:825	Ile619-Lys646	813:825	Ile619-Lys646	813:825	Nano-flow ESI tandem mass spectrometry (MS/MS) of the glycopeptides (Cys421-Lys433 and Ile619-Lys646) containing these two sites yielded predominantly ions originating from the non-reducing termini (oxonium ions) and reducing terminus, resulting from cleavage of the glycosidic bonds of the carbohydrate moieties; this permitted the structural read-out of a small minority of the carbohydrate moieties.
15536627	4	44	theme	tandem	740:745	arg1	MS/MS					766:770	MS/MS	766:770	MS/MS	766:770	Nano-flow ESI tandem mass spectrometry (MS/MS) of the glycopeptides (Cys421-Lys433 and Ile619-Lys646) containing these two sites yielded predominantly ions originating from the non-reducing termini (oxonium ions) and reducing terminus, resulting from cleavage of the glycosidic bonds of the carbohydrate moieties; this permitted the structural read-out of a small minority of the carbohydrate moieties.
15536627	4	44	theme	tandem	740:745	arg1	spectrometry					752:763	Nano-flow ESI tandem mass spectrometry	726:763	Nano-flow ESI tandem mass spectrometry (MS/MS) of the glycopeptides (Cys421-Lys433 and Ile619-Lys646) containing these two sites	726:853	Nano-flow ESI tandem mass spectrometry (MS/MS) of the glycopeptides (Cys421-Lys433 and Ile619-Lys646) containing these two sites yielded predominantly ions originating from the non-reducing termini (oxonium ions) and reducing terminus, resulting from cleavage of the glycosidic bonds of the carbohydrate moieties; this permitted the structural read-out of a small minority of the carbohydrate moieties.
15536627	1	45	theme	chromatography/electrospray	269:295	arg1	LC/ESI-MS					327:335	LC/ESI-MS	327:335	LC/ESI-MS	327:335	Glycopeptides derived from a lysylendopeptidase digest of commercially available human transferrin were analyzed by nano-flow liquid chromatography/electrospray ionization mass spectrometry (LC/ESI-MS), which permitted the carbohydrate profiles at Asn432 and Asn630 to be determined.
15536627	1	45	theme	chromatography/electrospray	269:295	arg1	spectrometry					313:324	nano-flow liquid chromatography/electrospray ionization mass spectrometry	252:324	nano-flow liquid chromatography/electrospray ionization mass spectrometry (LC/ESI-MS)	252:336	Glycopeptides derived from a lysylendopeptidase digest of commercially available human transferrin were analyzed by nano-flow liquid chromatography/electrospray ionization mass spectrometry (LC/ESI-MS), which permitted the carbohydrate profiles at Asn432 and Asn630 to be determined.
15536627	0	46	theme	human	40:44	arg1	transferrin					46:56	human transferrin	40:56	human transferrin	40:56	Site-specific carbohydrate profiling of human transferrin by nano-flow liquid chromatography/electrospray ionization mass spectrometry.
15536627	4	47	theme	bonds	1004:1008	arg1	cleavage					977:984	cleavage	977:984	cleavage of the glycosidic bonds of the carbohydrate moieties	977:1037	Nano-flow ESI tandem mass spectrometry (MS/MS) of the glycopeptides (Cys421-Lys433 and Ile619-Lys646) containing these two sites yielded predominantly ions originating from the non-reducing termini (oxonium ions) and reducing terminus, resulting from cleavage of the glycosidic bonds of the carbohydrate moieties; this permitted the structural read-out of a small minority of the carbohydrate moieties.
15536627	3	48	theme	biantennary	684:694	arg1	oligosaccharide					709:723	a biantennary complex-type oligosaccharide	682:723	a biantennary complex-type oligosaccharide	682:723	The contents of the carbohydrates at each site were significantly different from each other, and consisted of a variety of minor types of oligosaccharides in addition to the major one, a biantennary complex-type oligosaccharide.
15536627	3	48	theme	biantennary	684:694	arg1	one					677:679	the major one	667:679	the major one	667:679	The contents of the carbohydrates at each site were significantly different from each other, and consisted of a variety of minor types of oligosaccharides in addition to the major one, a biantennary complex-type oligosaccharide.
15536627	1	49	gly	carbohydrate	359:370	arg2	Asn630					395:400	Asn630	395:400	Asn630	395:400	Glycopeptides derived from a lysylendopeptidase digest of commercially available human transferrin were analyzed by nano-flow liquid chromatography/electrospray ionization mass spectrometry (LC/ESI-MS), which permitted the carbohydrate profiles at Asn432 and Asn630 to be determined.
15536627	1	49	gly	carbohydrate	359:370	arg2	Asn432					384:389	Asn432	384:389	Asn432	384:389	Glycopeptides derived from a lysylendopeptidase digest of commercially available human transferrin were analyzed by nano-flow liquid chromatography/electrospray ionization mass spectrometry (LC/ESI-MS), which permitted the carbohydrate profiles at Asn432 and Asn630 to be determined.
15536627	1	50	theme	ionization	297:306	arg1	LC/ESI-MS					327:335	LC/ESI-MS	327:335	LC/ESI-MS	327:335	Glycopeptides derived from a lysylendopeptidase digest of commercially available human transferrin were analyzed by nano-flow liquid chromatography/electrospray ionization mass spectrometry (LC/ESI-MS), which permitted the carbohydrate profiles at Asn432 and Asn630 to be determined.
15536627	1	50	theme	ionization	297:306	arg1	spectrometry					313:324	nano-flow liquid chromatography/electrospray ionization mass spectrometry	252:324	nano-flow liquid chromatography/electrospray ionization mass spectrometry (LC/ESI-MS)	252:336	Glycopeptides derived from a lysylendopeptidase digest of commercially available human transferrin were analyzed by nano-flow liquid chromatography/electrospray ionization mass spectrometry (LC/ESI-MS), which permitted the carbohydrate profiles at Asn432 and Asn630 to be determined.
15536627	0	51	theme	nano-flow	61:69	arg1	spectrometry					122:133	nano-flow liquid chromatography/electrospray ionization mass spectrometry	61:133	nano-flow liquid chromatography/electrospray ionization mass spectrometry	61:133	Site-specific carbohydrate profiling of human transferrin by nano-flow liquid chromatography/electrospray ionization mass spectrometry.
15536627	5	52	from	m/z	1179:1181	arg1	useful					1202:1207	useful	1202:1207	useful	1202:1207	In particular, the observation of oxonium ions at m/z 512.2 and 803.2 is useful for probing outer non-reducing terminal fucosylation, which represented carbohydrate structures consisting of Hex, dHex, and HexNAc, and NeuNAc, Hex, dHex, and HexNAc, respectively, from which the Lewis X structure (Galbeta1-4(Fucalpha1-3)GlcNAc) was readily deduced.
15536627	5	52	from	m/z	1179:1181	arg1	observation					1148:1158	the observation	1144:1158	the observation of oxonium ions at m/z 512.2 and 803.2	1144:1197	In particular, the observation of oxonium ions at m/z 512.2 and 803.2 is useful for probing outer non-reducing terminal fucosylation, which represented carbohydrate structures consisting of Hex, dHex, and HexNAc, and NeuNAc, Hex, dHex, and HexNAc, respectively, from which the Lewis X structure (Galbeta1-4(Fucalpha1-3)GlcNAc) was readily deduced.
15536627	3	53	theme	complex-type	696:707	arg1	oligosaccharide					709:723	a biantennary complex-type oligosaccharide	682:723	a biantennary complex-type oligosaccharide	682:723	The contents of the carbohydrates at each site were significantly different from each other, and consisted of a variety of minor types of oligosaccharides in addition to the major one, a biantennary complex-type oligosaccharide.
15536627	3	53	theme	complex-type	696:707	arg1	one					677:679	the major one	667:679	the major one	667:679	The contents of the carbohydrates at each site were significantly different from each other, and consisted of a variety of minor types of oligosaccharides in addition to the major one, a biantennary complex-type oligosaccharide.
15536627	5	54	theme	X	1412:1412	arg1	structure					1414:1422	the Lewis X structure	1402:1422	the Lewis X structure (Galbeta1-4(Fucalpha1-3)GlcNAc)	1402:1454	In particular, the observation of oxonium ions at m/z 512.2 and 803.2 is useful for probing outer non-reducing terminal fucosylation, which represented carbohydrate structures consisting of Hex, dHex, and HexNAc, and NeuNAc, Hex, dHex, and HexNAc, respectively, from which the Lewis X structure (Galbeta1-4(Fucalpha1-3)GlcNAc) was readily deduced.
15536627	5	54	theme	X	1412:1412	arg1	GlcNAc					1448:1453	Galbeta1-4(Fucalpha1-3)GlcNAc	1425:1453	Galbeta1-4(Fucalpha1-3)GlcNAc	1425:1453	In particular, the observation of oxonium ions at m/z 512.2 and 803.2 is useful for probing outer non-reducing terminal fucosylation, which represented carbohydrate structures consisting of Hex, dHex, and HexNAc, and NeuNAc, Hex, dHex, and HexNAc, respectively, from which the Lewis X structure (Galbeta1-4(Fucalpha1-3)GlcNAc) was readily deduced.
15536627	1	55	attach	derived	150:156	arg2	Glycopeptides					136:148	Glycopeptides	136:148	Glycopeptides derived from a lysylendopeptidase digest of commercially available human transferrin	136:233	Glycopeptides derived from a lysylendopeptidase digest of commercially available human transferrin were analyzed by nano-flow liquid chromatography/electrospray ionization mass spectrometry (LC/ESI-MS), which permitted the carbohydrate profiles at Asn432 and Asn630 to be determined.
15536627	1	55	attach	derived	150:156	arg1	digest					184:189	a lysylendopeptidase digest	163:189	a lysylendopeptidase digest of commercially available human transferrin	163:233	Glycopeptides derived from a lysylendopeptidase digest of commercially available human transferrin were analyzed by nano-flow liquid chromatography/electrospray ionization mass spectrometry (LC/ESI-MS), which permitted the carbohydrate profiles at Asn432 and Asn630 to be determined.
15536627	4	56	theme	glycosidic	993:1002	arg1	bonds					1004:1008	the glycosidic bonds	989:1008	the glycosidic bonds of the carbohydrate moieties	989:1037	Nano-flow ESI tandem mass spectrometry (MS/MS) of the glycopeptides (Cys421-Lys433 and Ile619-Lys646) containing these two sites yielded predominantly ions originating from the non-reducing termini (oxonium ions) and reducing terminus, resulting from cleavage of the glycosidic bonds of the carbohydrate moieties; this permitted the structural read-out of a small minority of the carbohydrate moieties.
15536627	4	57	theme	non-reducing	903:914	arg1	ions					933:936	oxonium ions	925:936	oxonium ions	925:936	Nano-flow ESI tandem mass spectrometry (MS/MS) of the glycopeptides (Cys421-Lys433 and Ile619-Lys646) containing these two sites yielded predominantly ions originating from the non-reducing termini (oxonium ions) and reducing terminus, resulting from cleavage of the glycosidic bonds of the carbohydrate moieties; this permitted the structural read-out of a small minority of the carbohydrate moieties.
15536627	4	57	theme	non-reducing	903:914	arg1	termini					916:922	the non-reducing termini	899:922	the non-reducing termini (oxonium ions)	899:937	Nano-flow ESI tandem mass spectrometry (MS/MS) of the glycopeptides (Cys421-Lys433 and Ile619-Lys646) containing these two sites yielded predominantly ions originating from the non-reducing termini (oxonium ions) and reducing terminus, resulting from cleavage of the glycosidic bonds of the carbohydrate moieties; this permitted the structural read-out of a small minority of the carbohydrate moieties.
15536627	3	58	from	site	539:542	arg1	contents					501:508	The contents	497:508	The contents of the carbohydrates at each site	497:542	The contents of the carbohydrates at each site were significantly different from each other, and consisted of a variety of minor types of oligosaccharides in addition to the major one, a biantennary complex-type oligosaccharide.
15536627	3	58	from	site	539:542	arg1	carbohydrates					517:529	the carbohydrates	513:529	the carbohydrates at each site	513:542	The contents of the carbohydrates at each site were significantly different from each other, and consisted of a variety of minor types of oligosaccharides in addition to the major one, a biantennary complex-type oligosaccharide.
15536627	3	58	from	site	539:542	arg1	different					563:571	different	563:571	different	563:571	The contents of the carbohydrates at each site were significantly different from each other, and consisted of a variety of minor types of oligosaccharides in addition to the major one, a biantennary complex-type oligosaccharide.
15536627	5	59	from	useful	1202:1207	arg1	particular					1132:1141	particular	1132:1141	particular	1132:1141	In particular, the observation of oxonium ions at m/z 512.2 and 803.2 is useful for probing outer non-reducing terminal fucosylation, which represented carbohydrate structures consisting of Hex, dHex, and HexNAc, and NeuNAc, Hex, dHex, and HexNAc, respectively, from which the Lewis X structure (Galbeta1-4(Fucalpha1-3)GlcNAc) was readily deduced.
15536627	6	60	theme	reducing-terminal	1507:1523	arg1	Fucalpha1-6GlcNAc					1533:1549	Fucalpha1-6GlcNAc	1533:1549	Fucalpha1-6GlcNAc	1533:1549	Moreover, fucosylation at the reducing-terminal GlcNAc (Fucalpha1-6GlcNAc) specifically occurred at Asn630, as demonstrated by treatment of the glycopeptides with alpha1-3/4-L-fucosidase.
15536627	6	60	theme	reducing-terminal	1507:1523	arg1	GlcNAc					1525:1530	the reducing-terminal GlcNAc	1503:1530	the reducing-terminal GlcNAc (Fucalpha1-6GlcNAc)	1503:1550	Moreover, fucosylation at the reducing-terminal GlcNAc (Fucalpha1-6GlcNAc) specifically occurred at Asn630, as demonstrated by treatment of the glycopeptides with alpha1-3/4-L-fucosidase.
15536627	5	61	theme	outer	1221:1225	arg1	fucosylation					1249:1260	outer non-reducing terminal fucosylation	1221:1260	outer non-reducing terminal fucosylation	1221:1260	In particular, the observation of oxonium ions at m/z 512.2 and 803.2 is useful for probing outer non-reducing terminal fucosylation, which represented carbohydrate structures consisting of Hex, dHex, and HexNAc, and NeuNAc, Hex, dHex, and HexNAc, respectively, from which the Lewis X structure (Galbeta1-4(Fucalpha1-3)GlcNAc) was readily deduced.
15536627	5	62	theme	Galbeta1-4	1425:1434	arg1	structure					1414:1422	the Lewis X structure	1402:1422	the Lewis X structure (Galbeta1-4(Fucalpha1-3)GlcNAc)	1402:1454	In particular, the observation of oxonium ions at m/z 512.2 and 803.2 is useful for probing outer non-reducing terminal fucosylation, which represented carbohydrate structures consisting of Hex, dHex, and HexNAc, and NeuNAc, Hex, dHex, and HexNAc, respectively, from which the Lewis X structure (Galbeta1-4(Fucalpha1-3)GlcNAc) was readily deduced.
15536627	5	62	theme	Galbeta1-4	1425:1434	arg1	GlcNAc					1448:1453	Galbeta1-4(Fucalpha1-3)GlcNAc	1425:1453	Galbeta1-4(Fucalpha1-3)GlcNAc	1425:1453	In particular, the observation of oxonium ions at m/z 512.2 and 803.2 is useful for probing outer non-reducing terminal fucosylation, which represented carbohydrate structures consisting of Hex, dHex, and HexNAc, and NeuNAc, Hex, dHex, and HexNAc, respectively, from which the Lewis X structure (Galbeta1-4(Fucalpha1-3)GlcNAc) was readily deduced.
15536627	5	63	from	particular	1132:1141	arg1	useful					1202:1207	useful	1202:1207	useful	1202:1207	In particular, the observation of oxonium ions at m/z 512.2 and 803.2 is useful for probing outer non-reducing terminal fucosylation, which represented carbohydrate structures consisting of Hex, dHex, and HexNAc, and NeuNAc, Hex, dHex, and HexNAc, respectively, from which the Lewis X structure (Galbeta1-4(Fucalpha1-3)GlcNAc) was readily deduced.
15536627	5	63	from	particular	1132:1141	arg1	observation					1148:1158	the observation	1144:1158	the observation of oxonium ions at m/z 512.2 and 803.2	1144:1197	In particular, the observation of oxonium ions at m/z 512.2 and 803.2 is useful for probing outer non-reducing terminal fucosylation, which represented carbohydrate structures consisting of Hex, dHex, and HexNAc, and NeuNAc, Hex, dHex, and HexNAc, respectively, from which the Lewis X structure (Galbeta1-4(Fucalpha1-3)GlcNAc) was readily deduced.
15536627	6	64	with	treatment	1604:1612	arg1	alpha1-3/4-L-fucosidase					1640:1662	alpha1-3/4-L-fucosidase	1640:1662	alpha1-3/4-L-fucosidase	1640:1662	Moreover, fucosylation at the reducing-terminal GlcNAc (Fucalpha1-6GlcNAc) specifically occurred at Asn630, as demonstrated by treatment of the glycopeptides with alpha1-3/4-L-fucosidase.
15536627	1	65	theme	lysylendopeptidase	165:182	arg1	digest					184:189	a lysylendopeptidase digest	163:189	a lysylendopeptidase digest of commercially available human transferrin	163:233	Glycopeptides derived from a lysylendopeptidase digest of commercially available human transferrin were analyzed by nano-flow liquid chromatography/electrospray ionization mass spectrometry (LC/ESI-MS), which permitted the carbohydrate profiles at Asn432 and Asn630 to be determined.
15536627	6	66	theme	glycopeptides	1621:1633	arg1	treatment					1604:1612	treatment	1604:1612	treatment of the glycopeptides with alpha1-3/4-L-fucosidase	1604:1662	Moreover, fucosylation at the reducing-terminal GlcNAc (Fucalpha1-6GlcNAc) specifically occurred at Asn630, as demonstrated by treatment of the glycopeptides with alpha1-3/4-L-fucosidase.
15536627	1	67	theme	mass	308:311	arg1	LC/ESI-MS					327:335	LC/ESI-MS	327:335	LC/ESI-MS	327:335	Glycopeptides derived from a lysylendopeptidase digest of commercially available human transferrin were analyzed by nano-flow liquid chromatography/electrospray ionization mass spectrometry (LC/ESI-MS), which permitted the carbohydrate profiles at Asn432 and Asn630 to be determined.
15536627	1	67	theme	mass	308:311	arg1	spectrometry					313:324	nano-flow liquid chromatography/electrospray ionization mass spectrometry	252:324	nano-flow liquid chromatography/electrospray ionization mass spectrometry (LC/ESI-MS)	252:336	Glycopeptides derived from a lysylendopeptidase digest of commercially available human transferrin were analyzed by nano-flow liquid chromatography/electrospray ionization mass spectrometry (LC/ESI-MS), which permitted the carbohydrate profiles at Asn432 and Asn630 to be determined.
15536627	2	68	from	motif	453:457	arg1	located					429:435	located	429:435	located	429:435	Both are located in a well-known motif for N-glycosylation, Asn-Xaa-Ser/Thr.
15536627	3	69	from	contents	501:508	arg1	site					539:542	each site	534:542	each site	534:542	The contents of the carbohydrates at each site were significantly different from each other, and consisted of a variety of minor types of oligosaccharides in addition to the major one, a biantennary complex-type oligosaccharide.
15536627	4	70	theme	glycopeptides	780:792	arg1	MS/MS					766:770	MS/MS	766:770	MS/MS	766:770	Nano-flow ESI tandem mass spectrometry (MS/MS) of the glycopeptides (Cys421-Lys433 and Ile619-Lys646) containing these two sites yielded predominantly ions originating from the non-reducing termini (oxonium ions) and reducing terminus, resulting from cleavage of the glycosidic bonds of the carbohydrate moieties; this permitted the structural read-out of a small minority of the carbohydrate moieties.
15536627	4	70	theme	glycopeptides	780:792	arg1	spectrometry					752:763	Nano-flow ESI tandem mass spectrometry	726:763	Nano-flow ESI tandem mass spectrometry (MS/MS) of the glycopeptides (Cys421-Lys433 and Ile619-Lys646) containing these two sites	726:853	Nano-flow ESI tandem mass spectrometry (MS/MS) of the glycopeptides (Cys421-Lys433 and Ile619-Lys646) containing these two sites yielded predominantly ions originating from the non-reducing termini (oxonium ions) and reducing terminus, resulting from cleavage of the glycosidic bonds of the carbohydrate moieties; this permitted the structural read-out of a small minority of the carbohydrate moieties.
15536627	5	71	theme	Lewis	1406:1410	arg1	structure					1414:1422	the Lewis X structure	1402:1422	the Lewis X structure (Galbeta1-4(Fucalpha1-3)GlcNAc)	1402:1454	In particular, the observation of oxonium ions at m/z 512.2 and 803.2 is useful for probing outer non-reducing terminal fucosylation, which represented carbohydrate structures consisting of Hex, dHex, and HexNAc, and NeuNAc, Hex, dHex, and HexNAc, respectively, from which the Lewis X structure (Galbeta1-4(Fucalpha1-3)GlcNAc) was readily deduced.
15536627	5	71	theme	Lewis	1406:1410	arg1	GlcNAc					1448:1453	Galbeta1-4(Fucalpha1-3)GlcNAc	1425:1453	Galbeta1-4(Fucalpha1-3)GlcNAc	1425:1453	In particular, the observation of oxonium ions at m/z 512.2 and 803.2 is useful for probing outer non-reducing terminal fucosylation, which represented carbohydrate structures consisting of Hex, dHex, and HexNAc, and NeuNAc, Hex, dHex, and HexNAc, respectively, from which the Lewis X structure (Galbeta1-4(Fucalpha1-3)GlcNAc) was readily deduced.
15536627	0	72	theme	chromatography/electrospray	78:104	arg1	spectrometry					122:133	nano-flow liquid chromatography/electrospray ionization mass spectrometry	61:133	nano-flow liquid chromatography/electrospray ionization mass spectrometry	61:133	Site-specific carbohydrate profiling of human transferrin by nano-flow liquid chromatography/electrospray ionization mass spectrometry.
15536627	5	73	dep	represented	1269:1279	arg1	deduced					1468:1474	deduced	1468:1474	was readily deduced	1456:1474	In particular, the observation of oxonium ions at m/z 512.2 and 803.2 is useful for probing outer non-reducing terminal fucosylation, which represented carbohydrate structures consisting of Hex, dHex, and HexNAc, and NeuNAc, Hex, dHex, and HexNAc, respectively, from which the Lewis X structure (Galbeta1-4(Fucalpha1-3)GlcNAc) was readily deduced.
15536627	3	74	theme	major	671:675	arg1	oligosaccharide					709:723	a biantennary complex-type oligosaccharide	682:723	a biantennary complex-type oligosaccharide	682:723	The contents of the carbohydrates at each site were significantly different from each other, and consisted of a variety of minor types of oligosaccharides in addition to the major one, a biantennary complex-type oligosaccharide.
15536627	3	74	theme	major	671:675	arg1	one					677:679	the major one	667:679	the major one	667:679	The contents of the carbohydrates at each site were significantly different from each other, and consisted of a variety of minor types of oligosaccharides in addition to the major one, a biantennary complex-type oligosaccharide.
15536627	4	75	theme	Nano-flow	726:734	arg1	MS/MS					766:770	MS/MS	766:770	MS/MS	766:770	Nano-flow ESI tandem mass spectrometry (MS/MS) of the glycopeptides (Cys421-Lys433 and Ile619-Lys646) containing these two sites yielded predominantly ions originating from the non-reducing termini (oxonium ions) and reducing terminus, resulting from cleavage of the glycosidic bonds of the carbohydrate moieties; this permitted the structural read-out of a small minority of the carbohydrate moieties.
15536627	4	75	theme	Nano-flow	726:734	arg1	spectrometry					752:763	Nano-flow ESI tandem mass spectrometry	726:763	Nano-flow ESI tandem mass spectrometry (MS/MS) of the glycopeptides (Cys421-Lys433 and Ile619-Lys646) containing these two sites	726:853	Nano-flow ESI tandem mass spectrometry (MS/MS) of the glycopeptides (Cys421-Lys433 and Ile619-Lys646) containing these two sites yielded predominantly ions originating from the non-reducing termini (oxonium ions) and reducing terminus, resulting from cleavage of the glycosidic bonds of the carbohydrate moieties; this permitted the structural read-out of a small minority of the carbohydrate moieties.
15536627	0	76	theme	liquid	71:76	arg1	spectrometry					122:133	nano-flow liquid chromatography/electrospray ionization mass spectrometry	61:133	nano-flow liquid chromatography/electrospray ionization mass spectrometry	61:133	Site-specific carbohydrate profiling of human transferrin by nano-flow liquid chromatography/electrospray ionization mass spectrometry.
15536627	6	77	gly	glycopeptides	1621:1633	arg2	glycopeptides					1621:1633	the glycopeptides	1617:1633	the glycopeptides	1617:1633	Moreover, fucosylation at the reducing-terminal GlcNAc (Fucalpha1-6GlcNAc) specifically occurred at Asn630, as demonstrated by treatment of the glycopeptides with alpha1-3/4-L-fucosidase.
11983428	4	0	theme	reticulum	885:893	arg1	membrane					857:864	the membrane	853:864	the membrane of the endoplasmic reticulum such that the SAM domain resides within the endoplasmic reticulum (ER) lumen	853:970	We have confirmed that STIM1 is modified by N-linked glycosylation at two sites within the SAM domain itself, deduced as asparagine residues N131 and N171, demonstrating that STIM1 is translocated across the membrane of the endoplasmic reticulum such that the SAM domain resides within the endoplasmic reticulum (ER) lumen.
11983428	2	1	theme	motif	359:363	arg1	domain					399:404	A single sterile alpha motif (SAM) protein-protein interaction domain	336:404	A single sterile alpha motif (SAM) protein-protein interaction domain	336:404	A single sterile alpha motif (SAM) protein-protein interaction domain is modelled within its extracellular region, a subcellular localisation not previously described for other SAM domain-containing proteins.
11983428	4	2	theme	SAM	909:911	arg1	domain					913:918	the SAM domain	905:918	the SAM domain	905:918	We have confirmed that STIM1 is modified by N-linked glycosylation at two sites within the SAM domain itself, deduced as asparagine residues N131 and N171, demonstrating that STIM1 is translocated across the membrane of the endoplasmic reticulum such that the SAM domain resides within the endoplasmic reticulum (ER) lumen.
11983428	1	3	theme	surface	219:225	arg1	glycoprotein					241:252	a cell surface transmembrane glycoprotein	212:252	a cell surface transmembrane glycoprotein implicated in tumour growth control and stromal-haematopoietic cell interactions	212:333	Stromal interaction molecule 1 (STIM1) is a cell surface transmembrane glycoprotein implicated in tumour growth control and stromal-haematopoietic cell interactions.
11983428	1	3	theme	surface	219:225	arg1	molecule					190:197	Stromal interaction molecule 1	170:199	Stromal interaction molecule 1 (STIM1)	170:207	Stromal interaction molecule 1 (STIM1) is a cell surface transmembrane glycoprotein implicated in tumour growth control and stromal-haematopoietic cell interactions.
11983428	4	4	theme	endoplasmic	873:883	arg1	reticulum					885:893	the endoplasmic reticulum	869:893	the endoplasmic reticulum such that the SAM domain resides within the endoplasmic reticulum (ER) lumen	869:970	We have confirmed that STIM1 is modified by N-linked glycosylation at two sites within the SAM domain itself, deduced as asparagine residues N131 and N171, demonstrating that STIM1 is translocated across the membrane of the endoplasmic reticulum such that the SAM domain resides within the endoplasmic reticulum (ER) lumen.
11983428	5	5	link	N-linked	978:985	arg1	oligosaccharides					987:1002	Both N-linked oligosaccharides	973:1002	Both N-linked oligosaccharides	973:1002	Both N-linked oligosaccharides remain endoglycosidase H-sensitive, indicating absence of full processing within the ER and Golgi.
11983428	2	6	theme	alpha	353:357	arg1	domain					399:404	A single sterile alpha motif (SAM) protein-protein interaction domain	336:404	A single sterile alpha motif (SAM) protein-protein interaction domain	336:404	A single sterile alpha motif (SAM) protein-protein interaction domain is modelled within its extracellular region, a subcellular localisation not previously described for other SAM domain-containing proteins.
11983428	1	7	theme	transmembrane	227:239	arg1	glycoprotein					241:252	a cell surface transmembrane glycoprotein	212:252	a cell surface transmembrane glycoprotein implicated in tumour growth control and stromal-haematopoietic cell interactions	212:333	Stromal interaction molecule 1 (STIM1) is a cell surface transmembrane glycoprotein implicated in tumour growth control and stromal-haematopoietic cell interactions.
11983428	1	7	theme	transmembrane	227:239	arg1	molecule					190:197	Stromal interaction molecule 1	170:199	Stromal interaction molecule 1 (STIM1)	170:207	Stromal interaction molecule 1 (STIM1) is a cell surface transmembrane glycoprotein implicated in tumour growth control and stromal-haematopoietic cell interactions.
11983428	0	8	theme	suppressor	76:85	arg1	activity					87:94	growth suppressor activity	69:94	growth suppressor activity	69:94	Stromal interaction molecule 1 (STIM1), a transmembrane protein with growth suppressor activity, contains an extracellular SAM domain modified by N-linked glycosylation.
11983428	8	9	theme	first	1533:1537	arg1	example					1539:1545	the first example	1529:1545	the first example of a SAM domain modified by N-linked glycosylation	1529:1596	These studies provide the first evidence for an extracellular localisation of a SAM domain within any protein, and the first example of a SAM domain modified by N-linked glycosylation.
11983428	0	10	with	protein	56:62	arg1	activity					87:94	growth suppressor activity	69:94	growth suppressor activity	69:94	Stromal interaction molecule 1 (STIM1), a transmembrane protein with growth suppressor activity, contains an extracellular SAM domain modified by N-linked glycosylation.
11983428	0	11	theme	growth	69:74	arg1	activity					87:94	growth suppressor activity	69:94	growth suppressor activity	69:94	Stromal interaction molecule 1 (STIM1), a transmembrane protein with growth suppressor activity, contains an extracellular SAM domain modified by N-linked glycosylation.
11983428	3	12	gly	glycosylation	634:646	arg2	glycosylation					634:646	N-linked glycosylation	625:646	N-linked glycosylation	625:646	We have defined the transmembrane topology of STIM1 by determining the sites of N-linked glycosylation.
11983428	3	12	gly	glycosylation	634:646	arg2	sites					616:620	the sites	612:620	the sites of N-linked glycosylation	612:646	We have defined the transmembrane topology of STIM1 by determining the sites of N-linked glycosylation.
11983428	3	13	theme	transmembrane	565:577	arg1	topology					579:586	the transmembrane topology	561:586	the transmembrane topology of STIM1	561:595	We have defined the transmembrane topology of STIM1 by determining the sites of N-linked glycosylation.
11983428	8	14	theme	N-linked	1575:1582	arg1	glycosylation					1584:1596	N-linked glycosylation	1575:1596	N-linked glycosylation	1575:1596	These studies provide the first evidence for an extracellular localisation of a SAM domain within any protein, and the first example of a SAM domain modified by N-linked glycosylation.
11983428	8	15	link	N-linked	1575:1582	arg1	glycosylation					1584:1596	N-linked glycosylation	1575:1596	N-linked glycosylation	1575:1596	These studies provide the first evidence for an extracellular localisation of a SAM domain within any protein, and the first example of a SAM domain modified by N-linked glycosylation.
11983428	5	16	theme	N-linked	978:985	arg1	oligosaccharides					987:1002	Both N-linked oligosaccharides	973:1002	Both N-linked oligosaccharides	973:1002	Both N-linked oligosaccharides remain endoglycosidase H-sensitive, indicating absence of full processing within the ER and Golgi.
11983428	2	17	theme	protein-protein	371:385	arg1	domain					399:404	A single sterile alpha motif (SAM) protein-protein interaction domain	336:404	A single sterile alpha motif (SAM) protein-protein interaction domain	336:404	A single sterile alpha motif (SAM) protein-protein interaction domain is modelled within its extracellular region, a subcellular localisation not previously described for other SAM domain-containing proteins.
11983428	2	18	theme	domain-containing	517:533	arg1	proteins					535:542	other SAM domain-containing proteins	507:542	other SAM domain-containing proteins	507:542	A single sterile alpha motif (SAM) protein-protein interaction domain is modelled within its extracellular region, a subcellular localisation not previously described for other SAM domain-containing proteins.
11983428	8	19	theme	domain	1556:1561	arg1	example					1539:1545	the first example	1529:1545	the first example of a SAM domain modified by N-linked glycosylation	1529:1596	These studies provide the first evidence for an extracellular localisation of a SAM domain within any protein, and the first example of a SAM domain modified by N-linked glycosylation.
11983428	8	19	theme	domain	1556:1561	arg1	evidence					1446:1453	the first evidence	1436:1453	the first evidence for an extracellular localisation of a SAM domain within any protein	1436:1522	These studies provide the first evidence for an extracellular localisation of a SAM domain within any protein, and the first example of a SAM domain modified by N-linked glycosylation.
11983428	5	20	dep	ER	1089:1090	arg1	the					1085:1087	the	1085:1087	the	1085:1087	Both N-linked oligosaccharides remain endoglycosidase H-sensitive, indicating absence of full processing within the ER and Golgi.
11983428	6	21	theme	STIM1	1201:1205	arg1	expression					1187:1196	cell surface expression	1174:1196	cell surface expression of STIM1	1174:1205	This immature modification is nevertheless sufficient and critical for cell surface expression of STIM1.
11983428	4	22	theme	reticulum	951:959	arg1	lumen					966:970	the endoplasmic reticulum (ER) lumen	935:970	the endoplasmic reticulum (ER) lumen	935:970	We have confirmed that STIM1 is modified by N-linked glycosylation at two sites within the SAM domain itself, deduced as asparagine residues N131 and N171, demonstrating that STIM1 is translocated across the membrane of the endoplasmic reticulum such that the SAM domain resides within the endoplasmic reticulum (ER) lumen.
11983428	2	23	theme	interaction	387:397	arg1	domain					399:404	A single sterile alpha motif (SAM) protein-protein interaction domain	336:404	A single sterile alpha motif (SAM) protein-protein interaction domain	336:404	A single sterile alpha motif (SAM) protein-protein interaction domain is modelled within its extracellular region, a subcellular localisation not previously described for other SAM domain-containing proteins.
11983428	0	24	theme	interaction	8:18	arg1	molecule					20:27	Stromal interaction molecule 1	0:29	Stromal interaction molecule 1 (STIM1)	0:37	Stromal interaction molecule 1 (STIM1), a transmembrane protein with growth suppressor activity, contains an extracellular SAM domain modified by N-linked glycosylation.
11983428	0	24	theme	interaction	8:18	arg1	STIM1					32:36	STIM1	32:36	STIM1	32:36	Stromal interaction molecule 1 (STIM1), a transmembrane protein with growth suppressor activity, contains an extracellular SAM domain modified by N-linked glycosylation.
11983428	0	24	theme	interaction	8:18	arg1	protein					56:62	a transmembrane protein	40:62	a transmembrane protein with growth suppressor activity	40:94	Stromal interaction molecule 1 (STIM1), a transmembrane protein with growth suppressor activity, contains an extracellular SAM domain modified by N-linked glycosylation.
11983428	8	25	theme	SAM	1552:1554	arg1	domain					1556:1561	a SAM domain	1550:1561	a SAM domain modified by N-linked glycosylation	1550:1596	These studies provide the first evidence for an extracellular localisation of a SAM domain within any protein, and the first example of a SAM domain modified by N-linked glycosylation.
11983428	2	26	theme	SAM	513:515	arg1	proteins					535:542	other SAM domain-containing proteins	507:542	other SAM domain-containing proteins	507:542	A single sterile alpha motif (SAM) protein-protein interaction domain is modelled within its extracellular region, a subcellular localisation not previously described for other SAM domain-containing proteins.
11983428	3	27	theme	STIM1	591:595	arg1	topology					579:586	the transmembrane topology	561:586	the transmembrane topology of STIM1	561:595	We have defined the transmembrane topology of STIM1 by determining the sites of N-linked glycosylation.
11983428	6	28	theme	immature	1108:1115	arg1	modification					1117:1128	This immature modification	1103:1128	This immature modification	1103:1128	This immature modification is nevertheless sufficient and critical for cell surface expression of STIM1.
11983428	1	29	theme	Stromal	170:176	arg1	glycoprotein					241:252	a cell surface transmembrane glycoprotein	212:252	a cell surface transmembrane glycoprotein implicated in tumour growth control and stromal-haematopoietic cell interactions	212:333	Stromal interaction molecule 1 (STIM1) is a cell surface transmembrane glycoprotein implicated in tumour growth control and stromal-haematopoietic cell interactions.
11983428	1	29	theme	Stromal	170:176	arg1	molecule					190:197	Stromal interaction molecule 1	170:199	Stromal interaction molecule 1 (STIM1)	170:207	Stromal interaction molecule 1 (STIM1) is a cell surface transmembrane glycoprotein implicated in tumour growth control and stromal-haematopoietic cell interactions.
11983428	1	29	theme	Stromal	170:176	arg1	STIM1					202:206	STIM1	202:206	STIM1	202:206	Stromal interaction molecule 1 (STIM1) is a cell surface transmembrane glycoprotein implicated in tumour growth control and stromal-haematopoietic cell interactions.
11983428	0	30	theme	Stromal	0:6	arg1	molecule					20:27	Stromal interaction molecule 1	0:29	Stromal interaction molecule 1 (STIM1)	0:37	Stromal interaction molecule 1 (STIM1), a transmembrane protein with growth suppressor activity, contains an extracellular SAM domain modified by N-linked glycosylation.
11983428	0	30	theme	Stromal	0:6	arg1	STIM1					32:36	STIM1	32:36	STIM1	32:36	Stromal interaction molecule 1 (STIM1), a transmembrane protein with growth suppressor activity, contains an extracellular SAM domain modified by N-linked glycosylation.
11983428	0	30	theme	Stromal	0:6	arg1	protein					56:62	a transmembrane protein	40:62	a transmembrane protein with growth suppressor activity	40:94	Stromal interaction molecule 1 (STIM1), a transmembrane protein with growth suppressor activity, contains an extracellular SAM domain modified by N-linked glycosylation.
11983428	5	31	theme	processing	1067:1076	arg1	absence					1051:1057	absence	1051:1057	absence of full processing within the ER and Golgi	1051:1100	Both N-linked oligosaccharides remain endoglycosidase H-sensitive, indicating absence of full processing within the ER and Golgi.
11983428	0	32	link	N-linked	146:153	arg1	glycosylation					155:167	N-linked glycosylation	146:167	N-linked glycosylation	146:167	Stromal interaction molecule 1 (STIM1), a transmembrane protein with growth suppressor activity, contains an extracellular SAM domain modified by N-linked glycosylation.
11983428	1	33	theme	interaction	178:188	arg1	glycoprotein					241:252	a cell surface transmembrane glycoprotein	212:252	a cell surface transmembrane glycoprotein implicated in tumour growth control and stromal-haematopoietic cell interactions	212:333	Stromal interaction molecule 1 (STIM1) is a cell surface transmembrane glycoprotein implicated in tumour growth control and stromal-haematopoietic cell interactions.
11983428	1	33	theme	interaction	178:188	arg1	molecule					190:197	Stromal interaction molecule 1	170:199	Stromal interaction molecule 1 (STIM1)	170:207	Stromal interaction molecule 1 (STIM1) is a cell surface transmembrane glycoprotein implicated in tumour growth control and stromal-haematopoietic cell interactions.
11983428	1	33	theme	interaction	178:188	arg1	STIM1					202:206	STIM1	202:206	STIM1	202:206	Stromal interaction molecule 1 (STIM1) is a cell surface transmembrane glycoprotein implicated in tumour growth control and stromal-haematopoietic cell interactions.
11983428	1	34	theme	tumour	268:273	arg1	control					282:288	tumour growth control	268:288	tumour growth control	268:288	Stromal interaction molecule 1 (STIM1) is a cell surface transmembrane glycoprotein implicated in tumour growth control and stromal-haematopoietic cell interactions.
11983428	1	35	gly	glycoprotein	241:252	arg1	glycoprotein					241:252	a cell surface transmembrane glycoprotein	212:252	a cell surface transmembrane glycoprotein implicated in tumour growth control and stromal-haematopoietic cell interactions	212:333	Stromal interaction molecule 1 (STIM1) is a cell surface transmembrane glycoprotein implicated in tumour growth control and stromal-haematopoietic cell interactions.
11983428	1	35	gly	glycoprotein	241:252	arg1	molecule					190:197	Stromal interaction molecule 1	170:199	Stromal interaction molecule 1 (STIM1)	170:207	Stromal interaction molecule 1 (STIM1) is a cell surface transmembrane glycoprotein implicated in tumour growth control and stromal-haematopoietic cell interactions.
11983428	6	36	theme	surface	1179:1185	arg1	expression					1187:1196	cell surface expression	1174:1196	cell surface expression of STIM1	1174:1205	This immature modification is nevertheless sufficient and critical for cell surface expression of STIM1.
11983428	2	37	theme	extracellular	429:441	arg1	localisation					465:476	a subcellular localisation	451:476	a subcellular localisation not previously described for other SAM domain-containing proteins	451:542	A single sterile alpha motif (SAM) protein-protein interaction domain is modelled within its extracellular region, a subcellular localisation not previously described for other SAM domain-containing proteins.
11983428	2	37	theme	extracellular	429:441	arg1	region					443:448	its extracellular region	425:448	its extracellular region	425:448	A single sterile alpha motif (SAM) protein-protein interaction domain is modelled within its extracellular region, a subcellular localisation not previously described for other SAM domain-containing proteins.
11983428	1	38	theme	growth	275:280	arg1	control					282:288	tumour growth control	268:288	tumour growth control	268:288	Stromal interaction molecule 1 (STIM1) is a cell surface transmembrane glycoprotein implicated in tumour growth control and stromal-haematopoietic cell interactions.
11983428	8	39	theme	domain	1498:1503	arg1	localisation					1476:1487	an extracellular localisation	1459:1487	an extracellular localisation of a SAM domain within any protein	1459:1522	These studies provide the first evidence for an extracellular localisation of a SAM domain within any protein, and the first example of a SAM domain modified by N-linked glycosylation.
11983428	4	40	theme	endoplasmic	939:949	arg1	ER					962:963	ER	962:963	ER	962:963	We have confirmed that STIM1 is modified by N-linked glycosylation at two sites within the SAM domain itself, deduced as asparagine residues N131 and N171, demonstrating that STIM1 is translocated across the membrane of the endoplasmic reticulum such that the SAM domain resides within the endoplasmic reticulum (ER) lumen.
11983428	4	40	theme	endoplasmic	939:949	arg1	reticulum					951:959	the endoplasmic reticulum	935:959	the endoplasmic reticulum (ER) lumen	935:970	We have confirmed that STIM1 is modified by N-linked glycosylation at two sites within the SAM domain itself, deduced as asparagine residues N131 and N171, demonstrating that STIM1 is translocated across the membrane of the endoplasmic reticulum such that the SAM domain resides within the endoplasmic reticulum (ER) lumen.
11983428	6	41	theme	cell	1174:1177	arg1	expression					1187:1196	cell surface expression	1174:1196	cell surface expression of STIM1	1174:1205	This immature modification is nevertheless sufficient and critical for cell surface expression of STIM1.
11983428	0	42	contain	contains	97:104	arg1	molecule					20:27	Stromal interaction molecule 1	0:29	Stromal interaction molecule 1 (STIM1)	0:37	Stromal interaction molecule 1 (STIM1), a transmembrane protein with growth suppressor activity, contains an extracellular SAM domain modified by N-linked glycosylation.
11983428	0	42	contain	contains	97:104	arg1	STIM1					32:36	STIM1	32:36	STIM1	32:36	Stromal interaction molecule 1 (STIM1), a transmembrane protein with growth suppressor activity, contains an extracellular SAM domain modified by N-linked glycosylation.
11983428	0	42	contain	contains	97:104	arg1	protein					56:62	a transmembrane protein	40:62	a transmembrane protein with growth suppressor activity	40:94	Stromal interaction molecule 1 (STIM1), a transmembrane protein with growth suppressor activity, contains an extracellular SAM domain modified by N-linked glycosylation.
11983428	0	42	contain	contains	97:104	arg2	domain					127:132	an extracellular SAM domain	106:132	an extracellular SAM domain modified by N-linked glycosylation	106:167	Stromal interaction molecule 1 (STIM1), a transmembrane protein with growth suppressor activity, contains an extracellular SAM domain modified by N-linked glycosylation.
11983428	7	43	theme	essential	1349:1357	arg1	role					1359:1362	an essential role	1346:1362	an essential role for the SAM domain in these protein interactions	1346:1411	We show that STIM1-STIM1 homotypic interactions are mediated via the cytoplasmic rather than the extracellular region of STIM1, excluding an essential role for the SAM domain in these protein interactions.
11983428	7	44	theme	homotypic	1233:1241	arg1	interactions					1243:1254	STIM1-STIM1 homotypic interactions	1221:1254	STIM1-STIM1 homotypic interactions	1221:1254	We show that STIM1-STIM1 homotypic interactions are mediated via the cytoplasmic rather than the extracellular region of STIM1, excluding an essential role for the SAM domain in these protein interactions.
11983428	4	45	theme	N-linked	693:700	arg1	glycosylation					702:714	N-linked glycosylation	693:714	N-linked glycosylation at two sites within the SAM domain itself, deduced as asparagine residues N131 and N171	693:802	We have confirmed that STIM1 is modified by N-linked glycosylation at two sites within the SAM domain itself, deduced as asparagine residues N131 and N171, demonstrating that STIM1 is translocated across the membrane of the endoplasmic reticulum such that the SAM domain resides within the endoplasmic reticulum (ER) lumen.
11983428	0	46	theme	SAM	123:125	arg1	domain					127:132	an extracellular SAM domain	106:132	an extracellular SAM domain modified by N-linked glycosylation	106:167	Stromal interaction molecule 1 (STIM1), a transmembrane protein with growth suppressor activity, contains an extracellular SAM domain modified by N-linked glycosylation.
11983428	4	47	link	N-linked	693:700	arg1	glycosylation					702:714	N-linked glycosylation	693:714	N-linked glycosylation at two sites within the SAM domain itself, deduced as asparagine residues N131 and N171	693:802	We have confirmed that STIM1 is modified by N-linked glycosylation at two sites within the SAM domain itself, deduced as asparagine residues N131 and N171, demonstrating that STIM1 is translocated across the membrane of the endoplasmic reticulum such that the SAM domain resides within the endoplasmic reticulum (ER) lumen.
11983428	4	48	mod	modified	681:688	arg3	glycosylation					702:714	N-linked glycosylation	693:714	N-linked glycosylation at two sites within the SAM domain itself, deduced as asparagine residues N131 and N171	693:802	We have confirmed that STIM1 is modified by N-linked glycosylation at two sites within the SAM domain itself, deduced as asparagine residues N131 and N171, demonstrating that STIM1 is translocated across the membrane of the endoplasmic reticulum such that the SAM domain resides within the endoplasmic reticulum (ER) lumen.
11983428	4	48	mod	modified	681:688	arg1	STIM1					672:676	STIM1	672:676	STIM1	672:676	We have confirmed that STIM1 is modified by N-linked glycosylation at two sites within the SAM domain itself, deduced as asparagine residues N131 and N171, demonstrating that STIM1 is translocated across the membrane of the endoplasmic reticulum such that the SAM domain resides within the endoplasmic reticulum (ER) lumen.
11983428	8	49	theme	first	1440:1444	arg1	evidence					1446:1453	the first evidence	1436:1453	the first evidence for an extracellular localisation of a SAM domain within any protein	1436:1522	These studies provide the first evidence for an extracellular localisation of a SAM domain within any protein, and the first example of a SAM domain modified by N-linked glycosylation.
11983428	0	50	theme	extracellular	109:121	arg1	domain					127:132	an extracellular SAM domain	106:132	an extracellular SAM domain modified by N-linked glycosylation	106:167	Stromal interaction molecule 1 (STIM1), a transmembrane protein with growth suppressor activity, contains an extracellular SAM domain modified by N-linked glycosylation.
11983428	4	51	theme	asparagine	770:779	arg1	residues					781:788	asparagine residues N131 and N171	770:802	asparagine residues N131 and N171	770:802	We have confirmed that STIM1 is modified by N-linked glycosylation at two sites within the SAM domain itself, deduced as asparagine residues N131 and N171, demonstrating that STIM1 is translocated across the membrane of the endoplasmic reticulum such that the SAM domain resides within the endoplasmic reticulum (ER) lumen.
11983428	4	51	theme	asparagine	770:779	arg1	N171					799:802	N171	799:802	N171	799:802	We have confirmed that STIM1 is modified by N-linked glycosylation at two sites within the SAM domain itself, deduced as asparagine residues N131 and N171, demonstrating that STIM1 is translocated across the membrane of the endoplasmic reticulum such that the SAM domain resides within the endoplasmic reticulum (ER) lumen.
11983428	4	51	theme	asparagine	770:779	arg1	N131					790:793	N131	790:793	N131	790:793	We have confirmed that STIM1 is modified by N-linked glycosylation at two sites within the SAM domain itself, deduced as asparagine residues N131 and N171, demonstrating that STIM1 is translocated across the membrane of the endoplasmic reticulum such that the SAM domain resides within the endoplasmic reticulum (ER) lumen.
11983428	7	52	theme	STIM1-STIM1	1221:1231	arg1	interactions					1243:1254	STIM1-STIM1 homotypic interactions	1221:1254	STIM1-STIM1 homotypic interactions	1221:1254	We show that STIM1-STIM1 homotypic interactions are mediated via the cytoplasmic rather than the extracellular region of STIM1, excluding an essential role for the SAM domain in these protein interactions.
11983428	4	53	dep	reticulum	885:893	arg1	resides					920:926	resides	920:926	resides within the endoplasmic reticulum (ER) lumen	920:970	We have confirmed that STIM1 is modified by N-linked glycosylation at two sites within the SAM domain itself, deduced as asparagine residues N131 and N171, demonstrating that STIM1 is translocated across the membrane of the endoplasmic reticulum such that the SAM domain resides within the endoplasmic reticulum (ER) lumen.
11983428	1	54	theme	stromal-haematopoietic	294:315	arg1	interactions					322:333	stromal-haematopoietic cell interactions	294:333	stromal-haematopoietic cell interactions	294:333	Stromal interaction molecule 1 (STIM1) is a cell surface transmembrane glycoprotein implicated in tumour growth control and stromal-haematopoietic cell interactions.
11983428	4	55	gly	glycosylation	702:714	arg1	sites					723:727	two sites	719:727	two sites within the SAM domain itself, deduced as asparagine residues N131 and N171	719:802	We have confirmed that STIM1 is modified by N-linked glycosylation at two sites within the SAM domain itself, deduced as asparagine residues N131 and N171, demonstrating that STIM1 is translocated across the membrane of the endoplasmic reticulum such that the SAM domain resides within the endoplasmic reticulum (ER) lumen.
11983428	4	55	gly	glycosylation	702:714	arg2	sites					723:727	two sites	719:727	two sites within the SAM domain itself, deduced as asparagine residues N131 and N171	719:802	We have confirmed that STIM1 is modified by N-linked glycosylation at two sites within the SAM domain itself, deduced as asparagine residues N131 and N171, demonstrating that STIM1 is translocated across the membrane of the endoplasmic reticulum such that the SAM domain resides within the endoplasmic reticulum (ER) lumen.
11983428	8	56	theme	SAM	1494:1496	arg1	domain					1498:1503	a SAM domain	1492:1503	a SAM domain within any protein	1492:1522	These studies provide the first evidence for an extracellular localisation of a SAM domain within any protein, and the first example of a SAM domain modified by N-linked glycosylation.
11983428	2	57	theme	sterile	345:351	arg1	domain					399:404	A single sterile alpha motif (SAM) protein-protein interaction domain	336:404	A single sterile alpha motif (SAM) protein-protein interaction domain	336:404	A single sterile alpha motif (SAM) protein-protein interaction domain is modelled within its extracellular region, a subcellular localisation not previously described for other SAM domain-containing proteins.
11983428	2	58	theme	subcellular	453:463	arg1	localisation					465:476	a subcellular localisation	451:476	a subcellular localisation not previously described for other SAM domain-containing proteins	451:542	A single sterile alpha motif (SAM) protein-protein interaction domain is modelled within its extracellular region, a subcellular localisation not previously described for other SAM domain-containing proteins.
11983428	2	58	theme	subcellular	453:463	arg1	region					443:448	its extracellular region	425:448	its extracellular region	425:448	A single sterile alpha motif (SAM) protein-protein interaction domain is modelled within its extracellular region, a subcellular localisation not previously described for other SAM domain-containing proteins.
11983428	1	59	theme	cell	317:320	arg1	interactions					322:333	stromal-haematopoietic cell interactions	294:333	stromal-haematopoietic cell interactions	294:333	Stromal interaction molecule 1 (STIM1) is a cell surface transmembrane glycoprotein implicated in tumour growth control and stromal-haematopoietic cell interactions.
11983428	4	60	dep	residues	781:788	arg1	residues					781:788	asparagine residues N131 and N171	770:802	asparagine residues N131 and N171	770:802	We have confirmed that STIM1 is modified by N-linked glycosylation at two sites within the SAM domain itself, deduced as asparagine residues N131 and N171, demonstrating that STIM1 is translocated across the membrane of the endoplasmic reticulum such that the SAM domain resides within the endoplasmic reticulum (ER) lumen.
11983428	4	60	dep	residues	781:788	arg1	N171					799:802	N171	799:802	N171	799:802	We have confirmed that STIM1 is modified by N-linked glycosylation at two sites within the SAM domain itself, deduced as asparagine residues N131 and N171, demonstrating that STIM1 is translocated across the membrane of the endoplasmic reticulum such that the SAM domain resides within the endoplasmic reticulum (ER) lumen.
11983428	4	60	dep	residues	781:788	arg1	N131					790:793	N131	790:793	N131	790:793	We have confirmed that STIM1 is modified by N-linked glycosylation at two sites within the SAM domain itself, deduced as asparagine residues N131 and N171, demonstrating that STIM1 is translocated across the membrane of the endoplasmic reticulum such that the SAM domain resides within the endoplasmic reticulum (ER) lumen.
11983428	5	61	theme	full	1062:1065	arg1	processing					1067:1076	full processing	1062:1076	full processing within the ER and Golgi	1062:1100	Both N-linked oligosaccharides remain endoglycosidase H-sensitive, indicating absence of full processing within the ER and Golgi.
11983428	2	62	theme	single	338:343	arg1	domain					399:404	A single sterile alpha motif (SAM) protein-protein interaction domain	336:404	A single sterile alpha motif (SAM) protein-protein interaction domain	336:404	A single sterile alpha motif (SAM) protein-protein interaction domain is modelled within its extracellular region, a subcellular localisation not previously described for other SAM domain-containing proteins.
11983428	8	63	theme	extracellular	1462:1474	arg1	localisation					1476:1487	an extracellular localisation	1459:1487	an extracellular localisation of a SAM domain within any protein	1459:1522	These studies provide the first evidence for an extracellular localisation of a SAM domain within any protein, and the first example of a SAM domain modified by N-linked glycosylation.
11983428	0	64	theme	N-linked	146:153	arg1	glycosylation					155:167	N-linked glycosylation	146:167	N-linked glycosylation	146:167	Stromal interaction molecule 1 (STIM1), a transmembrane protein with growth suppressor activity, contains an extracellular SAM domain modified by N-linked glycosylation.
11983428	7	65	theme	extracellular	1305:1317	arg1	region					1319:1324	the extracellular region	1301:1324	the cytoplasmic rather than the extracellular region of STIM1	1273:1333	We show that STIM1-STIM1 homotypic interactions are mediated via the cytoplasmic rather than the extracellular region of STIM1, excluding an essential role for the SAM domain in these protein interactions.
11983428	4	66	dep	resides	920:926	arg1	such					895:898	such	895:898	such	895:898	We have confirmed that STIM1 is modified by N-linked glycosylation at two sites within the SAM domain itself, deduced as asparagine residues N131 and N171, demonstrating that STIM1 is translocated across the membrane of the endoplasmic reticulum such that the SAM domain resides within the endoplasmic reticulum (ER) lumen.
11983428	7	67	theme	STIM1	1329:1333	arg1	cytoplasmic					1277:1287	cytoplasmic	1277:1287	cytoplasmic	1277:1287	We show that STIM1-STIM1 homotypic interactions are mediated via the cytoplasmic rather than the extracellular region of STIM1, excluding an essential role for the SAM domain in these protein interactions.
11983428	7	68	theme	protein	1392:1398	arg1	interactions					1400:1411	these protein interactions	1386:1411	these protein interactions	1386:1411	We show that STIM1-STIM1 homotypic interactions are mediated via the cytoplasmic rather than the extracellular region of STIM1, excluding an essential role for the SAM domain in these protein interactions.
11983428	7	69	from	role	1359:1362	arg1	interactions					1400:1411	these protein interactions	1386:1411	these protein interactions	1386:1411	We show that STIM1-STIM1 homotypic interactions are mediated via the cytoplasmic rather than the extracellular region of STIM1, excluding an essential role for the SAM domain in these protein interactions.
11983428	4	70	theme	SAM	740:742	arg1	domain					744:749	the SAM domain	736:749	the SAM domain itself	736:756	We have confirmed that STIM1 is modified by N-linked glycosylation at two sites within the SAM domain itself, deduced as asparagine residues N131 and N171, demonstrating that STIM1 is translocated across the membrane of the endoplasmic reticulum such that the SAM domain resides within the endoplasmic reticulum (ER) lumen.
11983428	0	71	theme	transmembrane	42:54	arg1	protein					56:62	a transmembrane protein	40:62	a transmembrane protein with growth suppressor activity	40:94	Stromal interaction molecule 1 (STIM1), a transmembrane protein with growth suppressor activity, contains an extracellular SAM domain modified by N-linked glycosylation.
11983428	0	71	theme	transmembrane	42:54	arg1	molecule					20:27	Stromal interaction molecule 1	0:29	Stromal interaction molecule 1 (STIM1)	0:37	Stromal interaction molecule 1 (STIM1), a transmembrane protein with growth suppressor activity, contains an extracellular SAM domain modified by N-linked glycosylation.
11983428	3	72	theme	N-linked	625:632	arg1	glycosylation					634:646	N-linked glycosylation	625:646	N-linked glycosylation	625:646	We have defined the transmembrane topology of STIM1 by determining the sites of N-linked glycosylation.
11983428	2	73	theme	SAM	366:368	arg1	domain					399:404	A single sterile alpha motif (SAM) protein-protein interaction domain	336:404	A single sterile alpha motif (SAM) protein-protein interaction domain	336:404	A single sterile alpha motif (SAM) protein-protein interaction domain is modelled within its extracellular region, a subcellular localisation not previously described for other SAM domain-containing proteins.
11983428	7	74	theme	SAM	1372:1374	arg1	domain					1376:1381	the SAM domain	1368:1381	the SAM domain	1368:1381	We show that STIM1-STIM1 homotypic interactions are mediated via the cytoplasmic rather than the extracellular region of STIM1, excluding an essential role for the SAM domain in these protein interactions.
11983428	2	75	theme	other	507:511	arg1	proteins					535:542	other SAM domain-containing proteins	507:542	other SAM domain-containing proteins	507:542	A single sterile alpha motif (SAM) protein-protein interaction domain is modelled within its extracellular region, a subcellular localisation not previously described for other SAM domain-containing proteins.
11983428	3	76	theme	glycosylation	634:646	arg1	sites					616:620	the sites	612:620	the sites of N-linked glycosylation	612:646	We have defined the transmembrane topology of STIM1 by determining the sites of N-linked glycosylation.
11983428	3	76	theme	glycosylation	634:646	arg1	glycosylation					634:646	N-linked glycosylation	625:646	N-linked glycosylation	625:646	We have defined the transmembrane topology of STIM1 by determining the sites of N-linked glycosylation.
11983428	3	77	link	N-linked	625:632	arg1	glycosylation					634:646	N-linked glycosylation	625:646	N-linked glycosylation	625:646	We have defined the transmembrane topology of STIM1 by determining the sites of N-linked glycosylation.
11983428	4	78	from	sites	723:727	arg1	glycosylation					702:714	N-linked glycosylation	693:714	N-linked glycosylation at two sites within the SAM domain itself, deduced as asparagine residues N131 and N171	693:802	We have confirmed that STIM1 is modified by N-linked glycosylation at two sites within the SAM domain itself, deduced as asparagine residues N131 and N171, demonstrating that STIM1 is translocated across the membrane of the endoplasmic reticulum such that the SAM domain resides within the endoplasmic reticulum (ER) lumen.
11983428	1	79	theme	cell	214:217	arg1	glycoprotein					241:252	a cell surface transmembrane glycoprotein	212:252	a cell surface transmembrane glycoprotein implicated in tumour growth control and stromal-haematopoietic cell interactions	212:333	Stromal interaction molecule 1 (STIM1) is a cell surface transmembrane glycoprotein implicated in tumour growth control and stromal-haematopoietic cell interactions.
11983428	1	79	theme	cell	214:217	arg1	molecule					190:197	Stromal interaction molecule 1	170:199	Stromal interaction molecule 1 (STIM1)	170:207	Stromal interaction molecule 1 (STIM1) is a cell surface transmembrane glycoprotein implicated in tumour growth control and stromal-haematopoietic cell interactions.
9013598	9	0	theme	tACE	1437:1440	arg1	mutant					1442:1447	a tACE mutant	1435:1447	a tACE mutant lacking the O-glycan-rich first amino-terminal 36 residues	1435:1506	The functional significance of glycosylation was examined with a tACE mutant lacking the O-glycan-rich first amino-terminal 36 residues and truncated at Ser625.
9013598	2	1	theme	endoproteinase	628:641	arg1	Asp-N					643:647	endoproteinase Asp-N	628:647	endoproteinase Asp-N	628:647	Two of the seven potential N-linked glycosylation sites, Asn90 and Asn109, were found to be fully glycosylated by analysis of peptides before and after treatment with a series of glycosidases and with endoproteinase Asp-N.
9013598	0	2	link	N-linked	18:25	arg1	sites					41:45	N-linked glycosylation sites	18:45	N-linked glycosylation sites in human testis angiotensin-converting enzyme	18:91	Identification of N-linked glycosylation sites in human testis angiotensin-converting enzyme and expression of an active deglycosylated form.
9013598	3	3	gly	glycopeptides	674:686	arg2	glycopeptides					674:686	the glycopeptides	670:686	the glycopeptides	670:686	The mass spectra of the glycopeptides exhibit characteristic clusters of peaks which indicate the N-linked glycans in tACE to be mostly of the biantennary, fucosylated complex type.
9013598	1	4	theme	laser	297:301	arg1	desorption					303:312	matrix-assisted laser desorption	281:312	matrix-assisted laser desorption ionization/time of flight/mass spectrometry of peptides generated by proteolytic and cyanogen bromide digestion	281:424	The sites of glycosylation of Chinese hamster ovary cell expressed testicular angiotensin-converting enzyme (tACE) have been determined by matrix-assisted laser desorption ionization/time of flight/mass spectrometry of peptides generated by proteolytic and cyanogen bromide digestion.
9013598	6	5	theme	unglycosylated	1184:1197	arg1	Asn					1199:1201	six glycosylated and one unglycosylated Asn	1159:1201	six glycosylated and one unglycosylated Asn	1159:1201	Sequence analysis of tryptic peptides obtained from somatic ACE (human kidney) identified six glycosylated and one unglycosylated Asn.
9013598	10	6	theme	inhibitor	1591:1599	arg1	N-butyldeoxynojirimycin					1601:1623	the alpha-glucosidase I inhibitor N-butyldeoxynojirimycin	1567:1623	the alpha-glucosidase I inhibitor N-butyldeoxynojirimycin	1567:1623	When expressed in the presence of the alpha-glucosidase I inhibitor N-butyldeoxynojirimycin and treated with endoglycosidase H to remove all but the terminal N-acetylglucosamine residues, it retained full enzymatic activity, was electrophoretically homogeneous, and is a good candidate for crystallographic studies.
9013598	1	7	theme	ovary	188:192	arg1	cell					194:197	Chinese hamster ovary cell	172:197	Chinese hamster ovary cell	172:197	The sites of glycosylation of Chinese hamster ovary cell expressed testicular angiotensin-converting enzyme (tACE) have been determined by matrix-assisted laser desorption ionization/time of flight/mass spectrometry of peptides generated by proteolytic and cyanogen bromide digestion.
9013598	1	8	theme	expressed	199:207	arg1	tACE					251:254	tACE	251:254	tACE	251:254	The sites of glycosylation of Chinese hamster ovary cell expressed testicular angiotensin-converting enzyme (tACE) have been determined by matrix-assisted laser desorption ionization/time of flight/mass spectrometry of peptides generated by proteolytic and cyanogen bromide digestion.
9013598	1	8	theme	expressed	199:207	arg1	enzyme					243:248	expressed testicular angiotensin-converting enzyme	199:248	glycosylation of Chinese hamster ovary cell expressed testicular angiotensin-converting enzyme (tACE)	155:255	The sites of glycosylation of Chinese hamster ovary cell expressed testicular angiotensin-converting enzyme (tACE) have been determined by matrix-assisted laser desorption ionization/time of flight/mass spectrometry of peptides generated by proteolytic and cyanogen bromide digestion.
9013598	0	9	theme	form	136:139	arg1	Identification					0:13	Identification	0:13	Identification of N-linked glycosylation sites in human testis angiotensin-converting enzyme	0:91	Identification of N-linked glycosylation sites in human testis angiotensin-converting enzyme and expression of an active deglycosylated form.
9013598	0	9	theme	form	136:139	arg1	expression					97:106	expression	97:106	expression of an active deglycosylated form	97:139	Identification of N-linked glycosylation sites in human testis angiotensin-converting enzyme and expression of an active deglycosylated form.
9013598	10	10	theme	crystallographic	1823:1838	arg1	studies					1840:1846	crystallographic studies	1823:1846	crystallographic studies	1823:1846	When expressed in the presence of the alpha-glucosidase I inhibitor N-butyldeoxynojirimycin and treated with endoglycosidase H to remove all but the terminal N-acetylglucosamine residues, it retained full enzymatic activity, was electrophoretically homogeneous, and is a good candidate for crystallographic studies.
9013598	1	11	theme	angiotensin-converting	220:241	arg1	tACE					251:254	tACE	251:254	tACE	251:254	The sites of glycosylation of Chinese hamster ovary cell expressed testicular angiotensin-converting enzyme (tACE) have been determined by matrix-assisted laser desorption ionization/time of flight/mass spectrometry of peptides generated by proteolytic and cyanogen bromide digestion.
9013598	1	11	theme	angiotensin-converting	220:241	arg1	enzyme					243:248	expressed testicular angiotensin-converting enzyme	199:248	glycosylation of Chinese hamster ovary cell expressed testicular angiotensin-converting enzyme (tACE)	155:255	The sites of glycosylation of Chinese hamster ovary cell expressed testicular angiotensin-converting enzyme (tACE) have been determined by matrix-assisted laser desorption ionization/time of flight/mass spectrometry of peptides generated by proteolytic and cyanogen bromide digestion.
9013598	3	12	theme	complex	818:824	arg1	type					826:829	the biantennary, fucosylated complex type	789:829	the biantennary, fucosylated complex type	789:829	The mass spectra of the glycopeptides exhibit characteristic clusters of peaks which indicate the N-linked glycans in tACE to be mostly of the biantennary, fucosylated complex type.
9013598	6	13	gly	unglycosylated	1184:1197	arg1	Asn					1199:1201	six glycosylated and one unglycosylated Asn	1159:1201	six glycosylated and one unglycosylated Asn	1159:1201	Sequence analysis of tryptic peptides obtained from somatic ACE (human kidney) identified six glycosylated and one unglycosylated Asn.
9013598	0	14	theme	angiotensin-converting	63:84	arg1	enzyme					86:91	human testis angiotensin-converting enzyme	50:91	human testis angiotensin-converting enzyme	50:91	Identification of N-linked glycosylation sites in human testis angiotensin-converting enzyme and expression of an active deglycosylated form.
9013598	3	15	theme	mass	654:657	arg1	spectra					659:665	The mass spectra	650:665	The mass spectra of the glycopeptides	650:686	The mass spectra of the glycopeptides exhibit characteristic clusters of peaks which indicate the N-linked glycans in tACE to be mostly of the biantennary, fucosylated complex type.
9013598	1	16	theme	glycosylation	155:167	arg1	glycosylation					155:167	glycosylation	155:167	glycosylation of Chinese hamster ovary cell expressed testicular angiotensin-converting enzyme (tACE)	155:255	The sites of glycosylation of Chinese hamster ovary cell expressed testicular angiotensin-converting enzyme (tACE) have been determined by matrix-assisted laser desorption ionization/time of flight/mass spectrometry of peptides generated by proteolytic and cyanogen bromide digestion.
9013598	1	16	theme	glycosylation	155:167	arg1	sites					146:150	The sites	142:150	The sites of glycosylation of Chinese hamster ovary cell expressed testicular angiotensin-converting enzyme (tACE)	142:255	The sites of glycosylation of Chinese hamster ovary cell expressed testicular angiotensin-converting enzyme (tACE) have been determined by matrix-assisted laser desorption ionization/time of flight/mass spectrometry of peptides generated by proteolytic and cyanogen bromide digestion.
9013598	8	17	theme	N-linked	1342:1349	arg1	sites					1351:1355	amino-terminal N-linked sites	1327:1355	amino-terminal N-linked sites	1327:1355	Comparison of the two proteins reveals a pattern in which amino-terminal N-linked sites are preferred.
9013598	7	18	theme	sites	1236:1240	arg1	sites					1236:1240	these glycosylation sites	1216:1240	these glycosylation sites	1216:1240	Only one of these glycosylation sites had a counterpart in tACE.
9013598	7	18	theme	sites	1236:1240	arg1	one					1209:1211	one	1209:1211	one	1209:1211	Only one of these glycosylation sites had a counterpart in tACE.
9013598	1	19	theme	Chinese	172:178	arg1	ovary					188:192	Chinese hamster ovary	172:192	Chinese hamster ovary cell	172:197	The sites of glycosylation of Chinese hamster ovary cell expressed testicular angiotensin-converting enzyme (tACE) have been determined by matrix-assisted laser desorption ionization/time of flight/mass spectrometry of peptides generated by proteolytic and cyanogen bromide digestion.
9013598	0	20	from	Identification	0:13	arg1	enzyme					86:91	human testis angiotensin-converting enzyme	50:91	human testis angiotensin-converting enzyme	50:91	Identification of N-linked glycosylation sites in human testis angiotensin-converting enzyme and expression of an active deglycosylated form.
9013598	7	21	gly	glycosylation	1222:1234	arg2	sites					1236:1240	these glycosylation sites	1216:1240	these glycosylation sites	1216:1240	Only one of these glycosylation sites had a counterpart in tACE.
9013598	4	22	dep	glycosylated	950:961	arg1	whereas					964:970	whereas	964:970	whereas	964:970	This structural information was used to demonstrate that three other sites, Asn155, Asn337, and Asn586, are partially glycosylated, whereas Asn72 appears to be fully glycosylated.
9013598	1	23	theme	bromide	408:414	arg1	digestion					416:424	proteolytic and cyanogen bromide digestion	383:424	digestion	416:424	The sites of glycosylation of Chinese hamster ovary cell expressed testicular angiotensin-converting enzyme (tACE) have been determined by matrix-assisted laser desorption ionization/time of flight/mass spectrometry of peptides generated by proteolytic and cyanogen bromide digestion.
9013598	2	24	theme	peptides	553:560	arg1	analysis					541:548	analysis	541:548	analysis of peptides before and after treatment with a series of glycosidases and with endoproteinase Asp-N	541:647	Two of the seven potential N-linked glycosylation sites, Asn90 and Asn109, were found to be fully glycosylated by analysis of peptides before and after treatment with a series of glycosidases and with endoproteinase Asp-N.
9013598	10	25	theme	full	1733:1736	arg1	activity					1748:1755	full enzymatic activity	1733:1755	full enzymatic activity	1733:1755	When expressed in the presence of the alpha-glucosidase I inhibitor N-butyldeoxynojirimycin and treated with endoglycosidase H to remove all but the terminal N-acetylglucosamine residues, it retained full enzymatic activity, was electrophoretically homogeneous, and is a good candidate for crystallographic studies.
9013598	2	26	theme	potential	444:452	arg1	sites					477:481	the seven potential N-linked glycosylation sites	434:481	the seven potential N-linked glycosylation sites	434:481	Two of the seven potential N-linked glycosylation sites, Asn90 and Asn109, were found to be fully glycosylated by analysis of peptides before and after treatment with a series of glycosidases and with endoproteinase Asp-N.
9013598	0	27	theme	active	114:119	arg1	form					136:139	an active deglycosylated form	111:139	an active deglycosylated form	111:139	Identification of N-linked glycosylation sites in human testis angiotensin-converting enzyme and expression of an active deglycosylated form.
9013598	6	28	theme	tryptic	1090:1096	arg1	peptides					1098:1105	tryptic peptides	1090:1105	tryptic peptides obtained from somatic ACE (human kidney)	1090:1146	Sequence analysis of tryptic peptides obtained from somatic ACE (human kidney) identified six glycosylated and one unglycosylated Asn.
9013598	0	29	from	sites	41:45	arg1	enzyme					86:91	human testis angiotensin-converting enzyme	50:91	human testis angiotensin-converting enzyme	50:91	Identification of N-linked glycosylation sites in human testis angiotensin-converting enzyme and expression of an active deglycosylated form.
9013598	10	30	theme	N-acetylglucosamine	1691:1709	arg1	residues					1711:1718	the terminal N-acetylglucosamine residues	1678:1718	the terminal N-acetylglucosamine residues	1678:1718	When expressed in the presence of the alpha-glucosidase I inhibitor N-butyldeoxynojirimycin and treated with endoglycosidase H to remove all but the terminal N-acetylglucosamine residues, it retained full enzymatic activity, was electrophoretically homogeneous, and is a good candidate for crystallographic studies.
9013598	1	31	theme	desorption	303:312	arg1	ionization/time					314:328	matrix-assisted laser desorption ionization/time	281:328	matrix-assisted laser desorption ionization/time of flight/mass spectrometry of peptides generated by proteolytic and cyanogen bromide digestion	281:424	The sites of glycosylation of Chinese hamster ovary cell expressed testicular angiotensin-converting enzyme (tACE) have been determined by matrix-assisted laser desorption ionization/time of flight/mass spectrometry of peptides generated by proteolytic and cyanogen bromide digestion.
9013598	10	32	theme	enzymatic	1738:1746	arg1	activity					1748:1755	full enzymatic activity	1733:1755	full enzymatic activity	1733:1755	When expressed in the presence of the alpha-glucosidase I inhibitor N-butyldeoxynojirimycin and treated with endoglycosidase H to remove all but the terminal N-acetylglucosamine residues, it retained full enzymatic activity, was electrophoretically homogeneous, and is a good candidate for crystallographic studies.
9013598	0	33	theme	N-linked	18:25	arg1	sites					41:45	N-linked glycosylation sites	18:45	N-linked glycosylation sites in human testis angiotensin-converting enzyme	18:91	Identification of N-linked glycosylation sites in human testis angiotensin-converting enzyme and expression of an active deglycosylated form.
9013598	2	34	gly	glycosylated	525:536	arg1	Asn109					494:499	Asn109	494:499	Asn109	494:499	Two of the seven potential N-linked glycosylation sites, Asn90 and Asn109, were found to be fully glycosylated by analysis of peptides before and after treatment with a series of glycosidases and with endoproteinase Asp-N.
9013598	2	34	gly	glycosylated	525:536	arg1	Asn90					484:488	Asn90	484:488	Asn90	484:488	Two of the seven potential N-linked glycosylation sites, Asn90 and Asn109, were found to be fully glycosylated by analysis of peptides before and after treatment with a series of glycosidases and with endoproteinase Asp-N.
9013598	2	34	gly	glycosylated	525:536	arg1	sites					477:481	the seven potential N-linked glycosylation sites	434:481	the seven potential N-linked glycosylation sites	434:481	Two of the seven potential N-linked glycosylation sites, Asn90 and Asn109, were found to be fully glycosylated by analysis of peptides before and after treatment with a series of glycosidases and with endoproteinase Asp-N.
9013598	2	34	gly	glycosylated	525:536	arg1	Two					427:429	Two	427:429	Two	427:429	Two of the seven potential N-linked glycosylation sites, Asn90 and Asn109, were found to be fully glycosylated by analysis of peptides before and after treatment with a series of glycosidases and with endoproteinase Asp-N.
9013598	3	35	theme	characteristic	696:709	arg1	clusters					711:718	characteristic clusters	696:718	characteristic clusters of peaks which indicate the N-linked glycans in tACE to be mostly of the biantennary, fucosylated complex type	696:829	The mass spectra of the glycopeptides exhibit characteristic clusters of peaks which indicate the N-linked glycans in tACE to be mostly of the biantennary, fucosylated complex type.
9013598	2	36	theme	glycosylation	463:475	arg1	sites					477:481	the seven potential N-linked glycosylation sites	434:481	the seven potential N-linked glycosylation sites	434:481	Two of the seven potential N-linked glycosylation sites, Asn90 and Asn109, were found to be fully glycosylated by analysis of peptides before and after treatment with a series of glycosidases and with endoproteinase Asp-N.
9013598	0	37	theme	sites	41:45	arg1	Identification					0:13	Identification	0:13	Identification of N-linked glycosylation sites in human testis angiotensin-converting enzyme	0:91	Identification of N-linked glycosylation sites in human testis angiotensin-converting enzyme and expression of an active deglycosylated form.
9013598	0	37	theme	sites	41:45	arg1	expression					97:106	expression	97:106	expression of an active deglycosylated form	97:139	Identification of N-linked glycosylation sites in human testis angiotensin-converting enzyme and expression of an active deglycosylated form.
9013598	1	38	theme	spectrometry	345:356	arg1	ionization/time					314:328	matrix-assisted laser desorption ionization/time	281:328	matrix-assisted laser desorption ionization/time of flight/mass spectrometry of peptides generated by proteolytic and cyanogen bromide digestion	281:424	The sites of glycosylation of Chinese hamster ovary cell expressed testicular angiotensin-converting enzyme (tACE) have been determined by matrix-assisted laser desorption ionization/time of flight/mass spectrometry of peptides generated by proteolytic and cyanogen bromide digestion.
9013598	3	39	theme	glycopeptides	674:686	arg1	spectra					659:665	The mass spectra	650:665	The mass spectra of the glycopeptides	650:686	The mass spectra of the glycopeptides exhibit characteristic clusters of peaks which indicate the N-linked glycans in tACE to be mostly of the biantennary, fucosylated complex type.
9013598	0	40	theme	human	50:54	arg1	enzyme					86:91	human testis angiotensin-converting enzyme	50:91	human testis angiotensin-converting enzyme	50:91	Identification of N-linked glycosylation sites in human testis angiotensin-converting enzyme and expression of an active deglycosylated form.
9013598	1	41	theme	peptides	361:368	arg1	spectrometry					345:356	flight/mass spectrometry	333:356	flight/mass spectrometry of peptides generated by proteolytic and cyanogen bromide digestion	333:424	The sites of glycosylation of Chinese hamster ovary cell expressed testicular angiotensin-converting enzyme (tACE) have been determined by matrix-assisted laser desorption ionization/time of flight/mass spectrometry of peptides generated by proteolytic and cyanogen bromide digestion.
9013598	0	42	gly	glycosylation	27:39	arg2	sites					41:45	N-linked glycosylation sites	18:45	N-linked glycosylation sites in human testis angiotensin-converting enzyme	18:91	Identification of N-linked glycosylation sites in human testis angiotensin-converting enzyme and expression of an active deglycosylated form.
9013598	2	43	link	N-linked	454:461	arg1	sites					477:481	the seven potential N-linked glycosylation sites	434:481	the seven potential N-linked glycosylation sites	434:481	Two of the seven potential N-linked glycosylation sites, Asn90 and Asn109, were found to be fully glycosylated by analysis of peptides before and after treatment with a series of glycosidases and with endoproteinase Asp-N.
9013598	9	44	theme	glycosylation	1403:1415	arg1	significance					1387:1398	The functional significance	1372:1398	The functional significance of glycosylation	1372:1415	The functional significance of glycosylation was examined with a tACE mutant lacking the O-glycan-rich first amino-terminal 36 residues and truncated at Ser625.
9013598	5	45	theme	only	1016:1019	arg1	site					1031:1034	The only potential site	1012:1034	The only potential site that was not modified	1012:1056	The only potential site that was not modified is Asn620.
9013598	5	45	theme	only	1016:1019	arg1	Asn620					1061:1066	Asn620	1061:1066	Asn620	1061:1066	The only potential site that was not modified is Asn620.
9013598	10	46	theme	I	1589:1589	arg1	N-butyldeoxynojirimycin					1601:1623	the alpha-glucosidase I inhibitor N-butyldeoxynojirimycin	1567:1623	the alpha-glucosidase I inhibitor N-butyldeoxynojirimycin	1567:1623	When expressed in the presence of the alpha-glucosidase I inhibitor N-butyldeoxynojirimycin and treated with endoglycosidase H to remove all but the terminal N-acetylglucosamine residues, it retained full enzymatic activity, was electrophoretically homogeneous, and is a good candidate for crystallographic studies.
9013598	9	47	theme	O-glycan-rich	1461:1473	arg1	residues					1499:1506	the O-glycan-rich first amino-terminal 36 residues	1457:1506	the O-glycan-rich first amino-terminal 36 residues	1457:1506	The functional significance of glycosylation was examined with a tACE mutant lacking the O-glycan-rich first amino-terminal 36 residues and truncated at Ser625.
9013598	6	48	theme	somatic	1121:1127	arg1	ACE					1129:1131	somatic ACE	1121:1131	somatic ACE (human kidney)	1121:1146	Sequence analysis of tryptic peptides obtained from somatic ACE (human kidney) identified six glycosylated and one unglycosylated Asn.
9013598	6	48	theme	somatic	1121:1127	arg1	kidney					1140:1145	human kidney	1134:1145	human kidney	1134:1145	Sequence analysis of tryptic peptides obtained from somatic ACE (human kidney) identified six glycosylated and one unglycosylated Asn.
9013598	7	49	contain	had	1242:1244	arg2	counterpart					1248:1258	a counterpart	1246:1258	a counterpart	1246:1258	Only one of these glycosylation sites had a counterpart in tACE.
9013598	7	49	contain	had	1242:1244	arg1	one					1209:1211	one	1209:1211	one	1209:1211	Only one of these glycosylation sites had a counterpart in tACE.
9013598	7	49	contain	had	1242:1244	arg1	sites					1236:1240	these glycosylation sites	1216:1240	these glycosylation sites	1216:1240	Only one of these glycosylation sites had a counterpart in tACE.
9013598	1	50	theme	matrix-assisted	281:295	arg1	desorption					303:312	matrix-assisted laser desorption	281:312	matrix-assisted laser desorption ionization/time of flight/mass spectrometry of peptides generated by proteolytic and cyanogen bromide digestion	281:424	The sites of glycosylation of Chinese hamster ovary cell expressed testicular angiotensin-converting enzyme (tACE) have been determined by matrix-assisted laser desorption ionization/time of flight/mass spectrometry of peptides generated by proteolytic and cyanogen bromide digestion.
9013598	8	51	link	N-linked	1342:1349	arg1	sites					1351:1355	amino-terminal N-linked sites	1327:1355	amino-terminal N-linked sites	1327:1355	Comparison of the two proteins reveals a pattern in which amino-terminal N-linked sites are preferred.
9013598	10	52	theme	N-butyldeoxynojirimycin	1601:1623	arg1	presence					1555:1562	the presence	1551:1562	the presence of the alpha-glucosidase I inhibitor N-butyldeoxynojirimycin	1551:1623	When expressed in the presence of the alpha-glucosidase I inhibitor N-butyldeoxynojirimycin and treated with endoglycosidase H to remove all but the terminal N-acetylglucosamine residues, it retained full enzymatic activity, was electrophoretically homogeneous, and is a good candidate for crystallographic studies.
9013598	10	53	theme	good	1804:1807	arg1	candidate					1809:1817	a good candidate	1802:1817	a good candidate for crystallographic studies	1802:1846	When expressed in the presence of the alpha-glucosidase I inhibitor N-butyldeoxynojirimycin and treated with endoglycosidase H to remove all but the terminal N-acetylglucosamine residues, it retained full enzymatic activity, was electrophoretically homogeneous, and is a good candidate for crystallographic studies.
9013598	9	54	theme	first	1475:1479	arg1	residues					1499:1506	the O-glycan-rich first amino-terminal 36 residues	1457:1506	the O-glycan-rich first amino-terminal 36 residues	1457:1506	The functional significance of glycosylation was examined with a tACE mutant lacking the O-glycan-rich first amino-terminal 36 residues and truncated at Ser625.
9013598	1	55	theme	hamster	180:186	arg1	ovary					188:192	Chinese hamster ovary	172:192	Chinese hamster ovary cell	172:197	The sites of glycosylation of Chinese hamster ovary cell expressed testicular angiotensin-converting enzyme (tACE) have been determined by matrix-assisted laser desorption ionization/time of flight/mass spectrometry of peptides generated by proteolytic and cyanogen bromide digestion.
9013598	6	56	gly	glycosylated	1163:1174	arg1	Asn					1199:1201	six glycosylated and one unglycosylated Asn	1159:1201	six glycosylated and one unglycosylated Asn	1159:1201	Sequence analysis of tryptic peptides obtained from somatic ACE (human kidney) identified six glycosylated and one unglycosylated Asn.
9013598	4	57	used	used	864:867	arg2	information					848:858	This structural information	832:858	This structural information	832:858	This structural information was used to demonstrate that three other sites, Asn155, Asn337, and Asn586, are partially glycosylated, whereas Asn72 appears to be fully glycosylated.
9013598	1	58	theme	cell	194:197	arg1	glycosylation					155:167	glycosylation	155:167	glycosylation of Chinese hamster ovary cell expressed testicular angiotensin-converting enzyme (tACE)	155:255	The sites of glycosylation of Chinese hamster ovary cell expressed testicular angiotensin-converting enzyme (tACE) have been determined by matrix-assisted laser desorption ionization/time of flight/mass spectrometry of peptides generated by proteolytic and cyanogen bromide digestion.
9013598	4	59	theme	other	895:899	arg1	Asn586					928:933	Asn586	928:933	Asn586	928:933	This structural information was used to demonstrate that three other sites, Asn155, Asn337, and Asn586, are partially glycosylated, whereas Asn72 appears to be fully glycosylated.
9013598	4	59	theme	other	895:899	arg1	Asn155					908:913	Asn155	908:913	Asn155	908:913	This structural information was used to demonstrate that three other sites, Asn155, Asn337, and Asn586, are partially glycosylated, whereas Asn72 appears to be fully glycosylated.
9013598	4	59	theme	other	895:899	arg1	sites					901:905	three other sites	889:905	three other sites	889:905	This structural information was used to demonstrate that three other sites, Asn155, Asn337, and Asn586, are partially glycosylated, whereas Asn72 appears to be fully glycosylated.
9013598	4	59	theme	other	895:899	arg1	Asn337					916:921	Asn337	916:921	Asn337	916:921	This structural information was used to demonstrate that three other sites, Asn155, Asn337, and Asn586, are partially glycosylated, whereas Asn72 appears to be fully glycosylated.
9013598	6	60	theme	glycosylated	1163:1174	arg1	Asn					1199:1201	six glycosylated and one unglycosylated Asn	1159:1201	six glycosylated and one unglycosylated Asn	1159:1201	Sequence analysis of tryptic peptides obtained from somatic ACE (human kidney) identified six glycosylated and one unglycosylated Asn.
9013598	10	61	theme	endoglycosidase	1642:1656	arg1	H					1658:1658	endoglycosidase H	1642:1658	endoglycosidase H	1642:1658	When expressed in the presence of the alpha-glucosidase I inhibitor N-butyldeoxynojirimycin and treated with endoglycosidase H to remove all but the terminal N-acetylglucosamine residues, it retained full enzymatic activity, was electrophoretically homogeneous, and is a good candidate for crystallographic studies.
9013598	3	62	theme	biantennary	793:803	arg1	type					826:829	the biantennary, fucosylated complex type	789:829	the biantennary, fucosylated complex type	789:829	The mass spectra of the glycopeptides exhibit characteristic clusters of peaks which indicate the N-linked glycans in tACE to be mostly of the biantennary, fucosylated complex type.
9013598	1	63	theme	testicular	209:218	arg1	tACE					251:254	tACE	251:254	tACE	251:254	The sites of glycosylation of Chinese hamster ovary cell expressed testicular angiotensin-converting enzyme (tACE) have been determined by matrix-assisted laser desorption ionization/time of flight/mass spectrometry of peptides generated by proteolytic and cyanogen bromide digestion.
9013598	1	63	theme	testicular	209:218	arg1	enzyme					243:248	expressed testicular angiotensin-converting enzyme	199:248	glycosylation of Chinese hamster ovary cell expressed testicular angiotensin-converting enzyme (tACE)	155:255	The sites of glycosylation of Chinese hamster ovary cell expressed testicular angiotensin-converting enzyme (tACE) have been determined by matrix-assisted laser desorption ionization/time of flight/mass spectrometry of peptides generated by proteolytic and cyanogen bromide digestion.
9013598	0	64	from	expression	97:106	arg1	enzyme					86:91	human testis angiotensin-converting enzyme	50:91	human testis angiotensin-converting enzyme	50:91	Identification of N-linked glycosylation sites in human testis angiotensin-converting enzyme and expression of an active deglycosylated form.
9013598	3	65	link	N-linked	748:755	arg1	glycans					757:763	the N-linked glycans	744:763	the N-linked glycans in tACE to be mostly of the biantennary, fucosylated complex type	744:829	The mass spectra of the glycopeptides exhibit characteristic clusters of peaks which indicate the N-linked glycans in tACE to be mostly of the biantennary, fucosylated complex type.
9013598	9	66	theme	amino-terminal	1481:1494	arg1	residues					1499:1506	the O-glycan-rich first amino-terminal 36 residues	1457:1506	the O-glycan-rich first amino-terminal 36 residues	1457:1506	The functional significance of glycosylation was examined with a tACE mutant lacking the O-glycan-rich first amino-terminal 36 residues and truncated at Ser625.
9013598	0	67	from	enzyme	86:91	arg1	Identification					0:13	Identification	0:13	Identification of N-linked glycosylation sites in human testis angiotensin-converting enzyme	0:91	Identification of N-linked glycosylation sites in human testis angiotensin-converting enzyme and expression of an active deglycosylated form.
9013598	0	67	from	enzyme	86:91	arg1	expression					97:106	expression	97:106	expression of an active deglycosylated form	97:139	Identification of N-linked glycosylation sites in human testis angiotensin-converting enzyme and expression of an active deglycosylated form.
9013598	1	68	gly	glycosylation	155:167	arg1	cell					194:197	Chinese hamster ovary cell	172:197	Chinese hamster ovary cell	172:197	The sites of glycosylation of Chinese hamster ovary cell expressed testicular angiotensin-converting enzyme (tACE) have been determined by matrix-assisted laser desorption ionization/time of flight/mass spectrometry of peptides generated by proteolytic and cyanogen bromide digestion.
9013598	1	68	gly	glycosylation	155:167	arg2	glycosylation					155:167	glycosylation	155:167	glycosylation of Chinese hamster ovary cell expressed testicular angiotensin-converting enzyme (tACE)	155:255	The sites of glycosylation of Chinese hamster ovary cell expressed testicular angiotensin-converting enzyme (tACE) have been determined by matrix-assisted laser desorption ionization/time of flight/mass spectrometry of peptides generated by proteolytic and cyanogen bromide digestion.
9013598	1	68	gly	glycosylation	155:167	arg2	sites					146:150	The sites	142:150	The sites of glycosylation of Chinese hamster ovary cell expressed testicular angiotensin-converting enzyme (tACE)	142:255	The sites of glycosylation of Chinese hamster ovary cell expressed testicular angiotensin-converting enzyme (tACE) have been determined by matrix-assisted laser desorption ionization/time of flight/mass spectrometry of peptides generated by proteolytic and cyanogen bromide digestion.
9013598	1	69	theme	cyanogen	399:406	arg1	digestion					416:424	proteolytic and cyanogen bromide digestion	383:424	digestion	416:424	The sites of glycosylation of Chinese hamster ovary cell expressed testicular angiotensin-converting enzyme (tACE) have been determined by matrix-assisted laser desorption ionization/time of flight/mass spectrometry of peptides generated by proteolytic and cyanogen bromide digestion.
9013598	2	70	theme	glycosidases	606:617	arg1	series					596:601	a series	594:601	a series of glycosidases	594:617	Two of the seven potential N-linked glycosylation sites, Asn90 and Asn109, were found to be fully glycosylated by analysis of peptides before and after treatment with a series of glycosidases and with endoproteinase Asp-N.
9013598	8	71	theme	proteins	1291:1298	arg1	Comparison					1269:1278	Comparison	1269:1278	Comparison of the two proteins	1269:1298	Comparison of the two proteins reveals a pattern in which amino-terminal N-linked sites are preferred.
9013598	4	72	gly	glycosylated	950:961	arg1	Asn586					928:933	Asn586	928:933	Asn586	928:933	This structural information was used to demonstrate that three other sites, Asn155, Asn337, and Asn586, are partially glycosylated, whereas Asn72 appears to be fully glycosylated.
9013598	4	72	gly	glycosylated	950:961	arg1	Asn155					908:913	Asn155	908:913	Asn155	908:913	This structural information was used to demonstrate that three other sites, Asn155, Asn337, and Asn586, are partially glycosylated, whereas Asn72 appears to be fully glycosylated.
9013598	4	72	gly	glycosylated	950:961	arg1	sites					901:905	three other sites	889:905	three other sites	889:905	This structural information was used to demonstrate that three other sites, Asn155, Asn337, and Asn586, are partially glycosylated, whereas Asn72 appears to be fully glycosylated.
9013598	4	72	gly	glycosylated	950:961	arg1	Asn337					916:921	Asn337	916:921	Asn337	916:921	This structural information was used to demonstrate that three other sites, Asn155, Asn337, and Asn586, are partially glycosylated, whereas Asn72 appears to be fully glycosylated.
9013598	7	73	theme	glycosylation	1222:1234	arg1	sites					1236:1240	these glycosylation sites	1216:1240	these glycosylation sites	1216:1240	Only one of these glycosylation sites had a counterpart in tACE.
9013598	1	74	theme	proteolytic	383:393	arg1	digestion					416:424	proteolytic and cyanogen bromide digestion	383:424	digestion	416:424	The sites of glycosylation of Chinese hamster ovary cell expressed testicular angiotensin-converting enzyme (tACE) have been determined by matrix-assisted laser desorption ionization/time of flight/mass spectrometry of peptides generated by proteolytic and cyanogen bromide digestion.
9013598	8	75	theme	amino-terminal	1327:1340	arg1	sites					1351:1355	amino-terminal N-linked sites	1327:1355	amino-terminal N-linked sites	1327:1355	Comparison of the two proteins reveals a pattern in which amino-terminal N-linked sites are preferred.
9013598	3	76	dep	biantennary	793:803	arg1	fucosylated					806:816	fucosylated	806:816	fucosylated	806:816	The mass spectra of the glycopeptides exhibit characteristic clusters of peaks which indicate the N-linked glycans in tACE to be mostly of the biantennary, fucosylated complex type.
9013598	0	77	gly	deglycosylated	121:134	arg1	form					136:139	an active deglycosylated form	111:139	an active deglycosylated form	111:139	Identification of N-linked glycosylation sites in human testis angiotensin-converting enzyme and expression of an active deglycosylated form.
9013598	2	78	gly	glycosylation	463:475	arg2	sites					477:481	the seven potential N-linked glycosylation sites	434:481	the seven potential N-linked glycosylation sites	434:481	Two of the seven potential N-linked glycosylation sites, Asn90 and Asn109, were found to be fully glycosylated by analysis of peptides before and after treatment with a series of glycosidases and with endoproteinase Asp-N.
9013598	2	78	gly	glycosylation	463:475	arg2	seven					438:442	seven	438:442	seven	438:442	Two of the seven potential N-linked glycosylation sites, Asn90 and Asn109, were found to be fully glycosylated by analysis of peptides before and after treatment with a series of glycosidases and with endoproteinase Asp-N.
9013598	0	79	theme	deglycosylated	121:134	arg1	form					136:139	an active deglycosylated form	111:139	an active deglycosylated form	111:139	Identification of N-linked glycosylation sites in human testis angiotensin-converting enzyme and expression of an active deglycosylated form.
9013598	4	80	gly	glycosylated	998:1009	arg1	Asn72					972:976	Asn72	972:976	Asn72	972:976	This structural information was used to demonstrate that three other sites, Asn155, Asn337, and Asn586, are partially glycosylated, whereas Asn72 appears to be fully glycosylated.
9013598	6	81	theme	peptides	1098:1105	arg1	analysis					1078:1085	Sequence analysis	1069:1085	Sequence analysis of tryptic peptides obtained from somatic ACE (human kidney)	1069:1146	Sequence analysis of tryptic peptides obtained from somatic ACE (human kidney) identified six glycosylated and one unglycosylated Asn.
9013598	3	82	dep	type	826:829	arg1	tACE					768:771	tACE	768:771	tACE	768:771	The mass spectra of the glycopeptides exhibit characteristic clusters of peaks which indicate the N-linked glycans in tACE to be mostly of the biantennary, fucosylated complex type.
9013598	10	83	theme	terminal	1682:1689	arg1	residues					1711:1718	the terminal N-acetylglucosamine residues	1678:1718	the terminal N-acetylglucosamine residues	1678:1718	When expressed in the presence of the alpha-glucosidase I inhibitor N-butyldeoxynojirimycin and treated with endoglycosidase H to remove all but the terminal N-acetylglucosamine residues, it retained full enzymatic activity, was electrophoretically homogeneous, and is a good candidate for crystallographic studies.
9013598	0	84	theme	glycosylation	27:39	arg1	sites					41:45	N-linked glycosylation sites	18:45	N-linked glycosylation sites in human testis angiotensin-converting enzyme	18:91	Identification of N-linked glycosylation sites in human testis angiotensin-converting enzyme and expression of an active deglycosylated form.
9013598	6	85	theme	Sequence	1069:1076	arg1	analysis					1078:1085	Sequence analysis	1069:1085	Sequence analysis of tryptic peptides obtained from somatic ACE (human kidney)	1069:1146	Sequence analysis of tryptic peptides obtained from somatic ACE (human kidney) identified six glycosylated and one unglycosylated Asn.
9013598	1	86	dep	glycosylation	155:167	arg1	tACE					251:254	tACE	251:254	tACE	251:254	The sites of glycosylation of Chinese hamster ovary cell expressed testicular angiotensin-converting enzyme (tACE) have been determined by matrix-assisted laser desorption ionization/time of flight/mass spectrometry of peptides generated by proteolytic and cyanogen bromide digestion.
9013598	1	86	dep	glycosylation	155:167	arg1	enzyme					243:248	expressed testicular angiotensin-converting enzyme	199:248	glycosylation of Chinese hamster ovary cell expressed testicular angiotensin-converting enzyme (tACE)	155:255	The sites of glycosylation of Chinese hamster ovary cell expressed testicular angiotensin-converting enzyme (tACE) have been determined by matrix-assisted laser desorption ionization/time of flight/mass spectrometry of peptides generated by proteolytic and cyanogen bromide digestion.
9013598	2	87	theme	sites	477:481	arg1	Asn109					494:499	Asn109	494:499	Asn109	494:499	Two of the seven potential N-linked glycosylation sites, Asn90 and Asn109, were found to be fully glycosylated by analysis of peptides before and after treatment with a series of glycosidases and with endoproteinase Asp-N.
9013598	2	87	theme	sites	477:481	arg1	Asn90					484:488	Asn90	484:488	Asn90	484:488	Two of the seven potential N-linked glycosylation sites, Asn90 and Asn109, were found to be fully glycosylated by analysis of peptides before and after treatment with a series of glycosidases and with endoproteinase Asp-N.
9013598	2	87	theme	sites	477:481	arg1	sites					477:481	the seven potential N-linked glycosylation sites	434:481	the seven potential N-linked glycosylation sites	434:481	Two of the seven potential N-linked glycosylation sites, Asn90 and Asn109, were found to be fully glycosylated by analysis of peptides before and after treatment with a series of glycosidases and with endoproteinase Asp-N.
9013598	2	87	theme	sites	477:481	arg1	Two					427:429	Two	427:429	Two	427:429	Two of the seven potential N-linked glycosylation sites, Asn90 and Asn109, were found to be fully glycosylated by analysis of peptides before and after treatment with a series of glycosidases and with endoproteinase Asp-N.
9013598	1	88	theme	flight/mass	333:343	arg1	spectrometry					345:356	flight/mass spectrometry	333:356	flight/mass spectrometry of peptides generated by proteolytic and cyanogen bromide digestion	333:424	The sites of glycosylation of Chinese hamster ovary cell expressed testicular angiotensin-converting enzyme (tACE) have been determined by matrix-assisted laser desorption ionization/time of flight/mass spectrometry of peptides generated by proteolytic and cyanogen bromide digestion.
9013598	2	89	theme	N-linked	454:461	arg1	sites					477:481	the seven potential N-linked glycosylation sites	434:481	the seven potential N-linked glycosylation sites	434:481	Two of the seven potential N-linked glycosylation sites, Asn90 and Asn109, were found to be fully glycosylated by analysis of peptides before and after treatment with a series of glycosidases and with endoproteinase Asp-N.
9013598	0	90	theme	testis	56:61	arg1	enzyme					86:91	human testis angiotensin-converting enzyme	50:91	human testis angiotensin-converting enzyme	50:91	Identification of N-linked glycosylation sites in human testis angiotensin-converting enzyme and expression of an active deglycosylated form.
9013598	9	91	theme	functional	1376:1385	arg1	significance					1387:1398	The functional significance	1372:1398	The functional significance of glycosylation	1372:1415	The functional significance of glycosylation was examined with a tACE mutant lacking the O-glycan-rich first amino-terminal 36 residues and truncated at Ser625.
9013598	3	92	theme	peaks	723:727	arg1	clusters					711:718	characteristic clusters	696:718	characteristic clusters of peaks which indicate the N-linked glycans in tACE to be mostly of the biantennary, fucosylated complex type	696:829	The mass spectra of the glycopeptides exhibit characteristic clusters of peaks which indicate the N-linked glycans in tACE to be mostly of the biantennary, fucosylated complex type.
9013598	2	93	with	treatment	579:587	arg1	Asp-N					643:647	endoproteinase Asp-N	628:647	endoproteinase Asp-N	628:647	Two of the seven potential N-linked glycosylation sites, Asn90 and Asn109, were found to be fully glycosylated by analysis of peptides before and after treatment with a series of glycosidases and with endoproteinase Asp-N.
9013598	2	93	with	treatment	579:587	arg1	series					596:601	a series	594:601	a series of glycosidases	594:617	Two of the seven potential N-linked glycosylation sites, Asn90 and Asn109, were found to be fully glycosylated by analysis of peptides before and after treatment with a series of glycosidases and with endoproteinase Asp-N.
9013598	6	94	theme	human	1134:1138	arg1	ACE					1129:1131	somatic ACE	1121:1131	somatic ACE (human kidney)	1121:1146	Sequence analysis of tryptic peptides obtained from somatic ACE (human kidney) identified six glycosylated and one unglycosylated Asn.
9013598	6	94	theme	human	1134:1138	arg1	kidney					1140:1145	human kidney	1134:1145	human kidney	1134:1145	Sequence analysis of tryptic peptides obtained from somatic ACE (human kidney) identified six glycosylated and one unglycosylated Asn.
9013598	5	95	theme	potential	1021:1029	arg1	site					1031:1034	The only potential site	1012:1034	The only potential site that was not modified	1012:1056	The only potential site that was not modified is Asn620.
9013598	5	95	theme	potential	1021:1029	arg1	Asn620					1061:1066	Asn620	1061:1066	Asn620	1061:1066	The only potential site that was not modified is Asn620.
9013598	10	96	theme	alpha-glucosidase	1571:1587	arg1	N-butyldeoxynojirimycin					1601:1623	the alpha-glucosidase I inhibitor N-butyldeoxynojirimycin	1567:1623	the alpha-glucosidase I inhibitor N-butyldeoxynojirimycin	1567:1623	When expressed in the presence of the alpha-glucosidase I inhibitor N-butyldeoxynojirimycin and treated with endoglycosidase H to remove all but the terminal N-acetylglucosamine residues, it retained full enzymatic activity, was electrophoretically homogeneous, and is a good candidate for crystallographic studies.
9013598	3	97	theme	N-linked	748:755	arg1	glycans					757:763	the N-linked glycans	744:763	the N-linked glycans in tACE to be mostly of the biantennary, fucosylated complex type	744:829	The mass spectra of the glycopeptides exhibit characteristic clusters of peaks which indicate the N-linked glycans in tACE to be mostly of the biantennary, fucosylated complex type.
9013598	4	98	theme	structural	837:846	arg1	information					848:858	This structural information	832:858	This structural information	832:858	This structural information was used to demonstrate that three other sites, Asn155, Asn337, and Asn586, are partially glycosylated, whereas Asn72 appears to be fully glycosylated.
10764840	0	0	theme	lymphoblastoid	83:96	arg1	line					103:106	a human lymphoblastoid cell line	75:106	a human lymphoblastoid cell line	75:106	Unusual N-glycosylation of a recombinant human erythropoietin expressed in a human lymphoblastoid cell line does not alter its biological properties.
10764840	3	1	theme	human	589:593	arg1	uHuEpo					600:605	uHuEpo	600:605	uHuEpo	600:605	The structure of the glycan chains of this rHuEpo slightly differ of those of the urinary human Epo (uHuEpo), considered as the natural Epo molecule.
10764840	3	1	theme	human	589:593	arg1	Epo					595:597	the urinary human Epo	577:597	the urinary human Epo (uHuEpo)	577:606	The structure of the glycan chains of this rHuEpo slightly differ of those of the urinary human Epo (uHuEpo), considered as the natural Epo molecule.
10764840	8	2	from	motif	1285:1289	arg1	residue					1225:1231	a second fucose residue	1209:1231	a second fucose residue which is present, in a large part, in a sialyl Le(x)motif	1209:1289	Thus, 80% of N-glycans possess a bisecting GlcNAc residue, 25% bear a second fucose residue which is present, in a large part, in a sialyl Le(x)motif, and 13% contain more than three LacNAc repeats (up to five per molecule).
10764840	8	2	from	motif	1285:1289	arg1	present					1242:1248	present	1242:1248	present	1242:1248	Thus, 80% of N-glycans possess a bisecting GlcNAc residue, 25% bear a second fucose residue which is present, in a large part, in a sialyl Le(x)motif, and 13% contain more than three LacNAc repeats (up to five per molecule).
10764840	1	3	gly	glycosylation	277:289	arg2	site					291:294	1 O- glycosylation site	272:294	1 O- glycosylation site (Ser-126)	272:304	Erythropoietin (Epo) is a 166 amino acids protein containing three N-glycosylation sites (Asn-24, Asn-38, and Asn-83) and 1 O- glycosylation site (Ser-126) and involved in the regulation of the level of red blood cells.
10764840	1	3	gly	glycosylation	277:289	arg2	1					272:272	1	272:272	1	272:272	Erythropoietin (Epo) is a 166 amino acids protein containing three N-glycosylation sites (Asn-24, Asn-38, and Asn-83) and 1 O- glycosylation site (Ser-126) and involved in the regulation of the level of red blood cells.
10764840	1	3	gly	glycosylation	277:289	arg2	Ser-126					297:303	Ser-126	297:303	Ser-126	297:303	Erythropoietin (Epo) is a 166 amino acids protein containing three N-glycosylation sites (Asn-24, Asn-38, and Asn-83) and 1 O- glycosylation site (Ser-126) and involved in the regulation of the level of red blood cells.
10764840	9	4	theme	in	1453:1454	arg1	activities					1472:1481	the in vitro and in vivo biological activities	1436:1481	the in vitro and in vivo biological activities	1436:1481	Despite these unusual structural characteristics, the data concerning the in vitro and in vivo biological activities were not impaired when compared to Epo-CHO and uHuEpo.
10764840	8	5	attach	present	1242:1248	arg1	part					1262:1265	a large part	1254:1265	a large part	1254:1265	Thus, 80% of N-glycans possess a bisecting GlcNAc residue, 25% bear a second fucose residue which is present, in a large part, in a sialyl Le(x)motif, and 13% contain more than three LacNAc repeats (up to five per molecule).
10764840	8	5	attach	present	1242:1248	arg2	present					1242:1248	present	1242:1248	present	1242:1248	Thus, 80% of N-glycans possess a bisecting GlcNAc residue, 25% bear a second fucose residue which is present, in a large part, in a sialyl Le(x)motif, and 13% contain more than three LacNAc repeats (up to five per molecule).
10764840	8	5	attach	present	1242:1248	arg1	motif					1285:1289	a sialyl Le(x)motif	1271:1289	a sialyl Le(x)motif	1271:1289	Thus, 80% of N-glycans possess a bisecting GlcNAc residue, 25% bear a second fucose residue which is present, in a large part, in a sialyl Le(x)motif, and 13% contain more than three LacNAc repeats (up to five per molecule).
10764840	8	5	attach	present	1242:1248	arg2	residue					1225:1231	a second fucose residue	1209:1231	a second fucose residue which is present, in a large part, in a sialyl Le(x)motif	1209:1289	Thus, 80% of N-glycans possess a bisecting GlcNAc residue, 25% bear a second fucose residue which is present, in a large part, in a sialyl Le(x)motif, and 13% contain more than three LacNAc repeats (up to five per molecule).
10764840	8	6	theme	second	1211:1216	arg1	residue					1225:1231	a second fucose residue	1209:1231	a second fucose residue which is present, in a large part, in a sialyl Le(x)motif	1209:1289	Thus, 80% of N-glycans possess a bisecting GlcNAc residue, 25% bear a second fucose residue which is present, in a large part, in a sialyl Le(x)motif, and 13% contain more than three LacNAc repeats (up to five per molecule).
10764840	8	6	theme	second	1211:1216	arg1	present					1242:1248	present	1242:1248	present	1242:1248	Thus, 80% of N-glycans possess a bisecting GlcNAc residue, 25% bear a second fucose residue which is present, in a large part, in a sialyl Le(x)motif, and 13% contain more than three LacNAc repeats (up to five per molecule).
10764840	0	7	theme	human	77:81	arg1	line					103:106	a human lymphoblastoid cell line	75:106	a human lymphoblastoid cell line	75:106	Unusual N-glycosylation of a recombinant human erythropoietin expressed in a human lymphoblastoid cell line does not alter its biological properties.
10764840	8	8	dep	repeats	1331:1337	arg1	five					1346:1349	five	1346:1349	five	1346:1349	Thus, 80% of N-glycans possess a bisecting GlcNAc residue, 25% bear a second fucose residue which is present, in a large part, in a sialyl Le(x)motif, and 13% contain more than three LacNAc repeats (up to five per molecule).
10764840	5	9	theme	protein	877:883	arg1	skeleton					885:892	the protein skeleton	873:892	the protein skeleton as well as glycan chains	873:917	In order to fully characterize the Epo-RPMI, structural characterizations of the protein skeleton as well as glycan chains were undergone.
10764840	1	10	gly	N-glycosylation	217:231	arg2	three					211:215	three	211:215	three	211:215	Erythropoietin (Epo) is a 166 amino acids protein containing three N-glycosylation sites (Asn-24, Asn-38, and Asn-83) and 1 O- glycosylation site (Ser-126) and involved in the regulation of the level of red blood cells.
10764840	1	10	gly	N-glycosylation	217:231	arg2	Asn-38					248:253	Asn-38	248:253	Asn-38	248:253	Erythropoietin (Epo) is a 166 amino acids protein containing three N-glycosylation sites (Asn-24, Asn-38, and Asn-83) and 1 O- glycosylation site (Ser-126) and involved in the regulation of the level of red blood cells.
10764840	1	10	gly	N-glycosylation	217:231	arg2	Asn-24					240:245	Asn-24	240:245	Asn-24	240:245	Erythropoietin (Epo) is a 166 amino acids protein containing three N-glycosylation sites (Asn-24, Asn-38, and Asn-83) and 1 O- glycosylation site (Ser-126) and involved in the regulation of the level of red blood cells.
10764840	1	10	gly	N-glycosylation	217:231	arg2	Asn-83					260:265	Asn-83	260:265	Asn-83	260:265	Erythropoietin (Epo) is a 166 amino acids protein containing three N-glycosylation sites (Asn-24, Asn-38, and Asn-83) and 1 O- glycosylation site (Ser-126) and involved in the regulation of the level of red blood cells.
10764840	1	10	gly	N-glycosylation	217:231	arg2	sites					233:237	three N-glycosylation sites	211:237	three N-glycosylation sites (Asn-24, Asn-38, and Asn-83)	211:266	Erythropoietin (Epo) is a 166 amino acids protein containing three N-glycosylation sites (Asn-24, Asn-38, and Asn-83) and 1 O- glycosylation site (Ser-126) and involved in the regulation of the level of red blood cells.
10764840	8	11	theme	fucose	1218:1223	arg1	residue					1225:1231	a second fucose residue	1209:1231	a second fucose residue which is present, in a large part, in a sialyl Le(x)motif	1209:1289	Thus, 80% of N-glycans possess a bisecting GlcNAc residue, 25% bear a second fucose residue which is present, in a large part, in a sialyl Le(x)motif, and 13% contain more than three LacNAc repeats (up to five per molecule).
10764840	8	11	theme	fucose	1218:1223	arg1	present					1242:1248	present	1242:1248	present	1242:1248	Thus, 80% of N-glycans possess a bisecting GlcNAc residue, 25% bear a second fucose residue which is present, in a large part, in a sialyl Le(x)motif, and 13% contain more than three LacNAc repeats (up to five per molecule).
10764840	4	12	theme	Epo	719:721	arg1	gene					723:726	Epo gene	719:726	Epo gene	719:726	In an attempt to produce a rHuEpo as close as possible to the uHuEpo, Epo gene was expressed in a human lymphoblastoid cell line, named RPMI 1788.
10764840	0	13	theme	cell	98:101	arg1	line					103:106	a human lymphoblastoid cell line	75:106	a human lymphoblastoid cell line	75:106	Unusual N-glycosylation of a recombinant human erythropoietin expressed in a human lymphoblastoid cell line does not alter its biological properties.
10764840	5	14	theme	chains	912:917	arg1	characterizations					852:868	structural characterizations	841:868	structural characterizations of the protein skeleton as well as glycan chains	841:917	In order to fully characterize the Epo-RPMI, structural characterizations of the protein skeleton as well as glycan chains were undergone.
10764840	2	15	theme	severe	484:489	arg1	anemia					491:496	severe anemia	484:496	severe anemia	484:496	Today, only one recombinant human Epo (rHuEpo), produced in CHO cell line, is extensively used in therapy to cure severe anemia.
10764840	2	16	used	used	460:463	arg2	Today					370:374	Today	370:374	Today	370:374	Today, only one recombinant human Epo (rHuEpo), produced in CHO cell line, is extensively used in therapy to cure severe anemia.
10764840	2	16	used	used	460:463	arg2	Epo					404:406	recombinant human Epo	386:406	only one recombinant human Epo (rHuEpo)	377:415	Today, only one recombinant human Epo (rHuEpo), produced in CHO cell line, is extensively used in therapy to cure severe anemia.
10764840	2	17	theme	CHO	430:432	arg1	line					439:442	CHO cell line	430:442	CHO cell line	430:442	Today, only one recombinant human Epo (rHuEpo), produced in CHO cell line, is extensively used in therapy to cure severe anemia.
10764840	8	18	located	present	1242:1248	arg1	part					1262:1265	a large part	1254:1265	a large part	1254:1265	Thus, 80% of N-glycans possess a bisecting GlcNAc residue, 25% bear a second fucose residue which is present, in a large part, in a sialyl Le(x)motif, and 13% contain more than three LacNAc repeats (up to five per molecule).
10764840	8	18	located	present	1242:1248	arg2	present					1242:1248	present	1242:1248	present	1242:1248	Thus, 80% of N-glycans possess a bisecting GlcNAc residue, 25% bear a second fucose residue which is present, in a large part, in a sialyl Le(x)motif, and 13% contain more than three LacNAc repeats (up to five per molecule).
10764840	8	18	located	present	1242:1248	arg1	motif					1285:1289	a sialyl Le(x)motif	1271:1289	a sialyl Le(x)motif	1271:1289	Thus, 80% of N-glycans possess a bisecting GlcNAc residue, 25% bear a second fucose residue which is present, in a large part, in a sialyl Le(x)motif, and 13% contain more than three LacNAc repeats (up to five per molecule).
10764840	8	18	located	present	1242:1248	arg2	residue					1225:1231	a second fucose residue	1209:1231	a second fucose residue which is present, in a large part, in a sialyl Le(x)motif	1209:1289	Thus, 80% of N-glycans possess a bisecting GlcNAc residue, 25% bear a second fucose residue which is present, in a large part, in a sialyl Le(x)motif, and 13% contain more than three LacNAc repeats (up to five per molecule).
10764840	6	19	theme	Epo-RPMI	979:986	arg1	sequence					963:970	the amino acid sequence	948:970	the amino acid sequence of the Epo-RPMI	948:986	As expected, the amino acid sequence of the Epo-RPMI conformed to that of uHuEpo.
10764840	2	20	theme	recombinant	386:396	arg1	rHuEpo					409:414	rHuEpo	409:414	rHuEpo	409:414	Today, only one recombinant human Epo (rHuEpo), produced in CHO cell line, is extensively used in therapy to cure severe anemia.
10764840	2	20	theme	recombinant	386:396	arg1	Epo					404:406	recombinant human Epo	386:406	only one recombinant human Epo (rHuEpo)	377:415	Today, only one recombinant human Epo (rHuEpo), produced in CHO cell line, is extensively used in therapy to cure severe anemia.
10764840	2	20	theme	recombinant	386:396	arg1	Today					370:374	Today	370:374	Today	370:374	Today, only one recombinant human Epo (rHuEpo), produced in CHO cell line, is extensively used in therapy to cure severe anemia.
10764840	8	21	theme	Le	1280:1281	arg1	motif					1285:1289	a sialyl Le(x)motif	1271:1289	a sialyl Le(x)motif	1271:1289	Thus, 80% of N-glycans possess a bisecting GlcNAc residue, 25% bear a second fucose residue which is present, in a large part, in a sialyl Le(x)motif, and 13% contain more than three LacNAc repeats (up to five per molecule).
10764840	4	22	theme	close	686:690	arg1	rHuEpo					676:681	a rHuEpo	674:681	a rHuEpo as close	674:690	In an attempt to produce a rHuEpo as close as possible to the uHuEpo, Epo gene was expressed in a human lymphoblastoid cell line, named RPMI 1788.
10764840	8	23	from	part	1262:1265	arg1	residue					1225:1231	a second fucose residue	1209:1231	a second fucose residue which is present, in a large part, in a sialyl Le(x)motif	1209:1289	Thus, 80% of N-glycans possess a bisecting GlcNAc residue, 25% bear a second fucose residue which is present, in a large part, in a sialyl Le(x)motif, and 13% contain more than three LacNAc repeats (up to five per molecule).
10764840	8	23	from	part	1262:1265	arg1	present					1242:1248	present	1242:1248	present	1242:1248	Thus, 80% of N-glycans possess a bisecting GlcNAc residue, 25% bear a second fucose residue which is present, in a large part, in a sialyl Le(x)motif, and 13% contain more than three LacNAc repeats (up to five per molecule).
10764840	8	24	from	present	1242:1248	arg1	part					1262:1265	a large part	1254:1265	a large part	1254:1265	Thus, 80% of N-glycans possess a bisecting GlcNAc residue, 25% bear a second fucose residue which is present, in a large part, in a sialyl Le(x)motif, and 13% contain more than three LacNAc repeats (up to five per molecule).
10764840	8	24	from	present	1242:1248	arg1	motif					1285:1289	a sialyl Le(x)motif	1271:1289	a sialyl Le(x)motif	1271:1289	Thus, 80% of N-glycans possess a bisecting GlcNAc residue, 25% bear a second fucose residue which is present, in a large part, in a sialyl Le(x)motif, and 13% contain more than three LacNAc repeats (up to five per molecule).
10764840	3	25	theme	natural	627:633	arg1	molecule					639:646	the natural Epo molecule	623:646	the natural Epo molecule	623:646	The structure of the glycan chains of this rHuEpo slightly differ of those of the urinary human Epo (uHuEpo), considered as the natural Epo molecule.
10764840	8	26	theme	sialyl	1273:1278	arg1	motif					1285:1289	a sialyl Le(x)motif	1271:1289	a sialyl Le(x)motif	1271:1289	Thus, 80% of N-glycans possess a bisecting GlcNAc residue, 25% bear a second fucose residue which is present, in a large part, in a sialyl Le(x)motif, and 13% contain more than three LacNAc repeats (up to five per molecule).
10764840	9	27	theme	in	1440:1441	arg1	activities					1472:1481	the in vitro and in vivo biological activities	1436:1481	the in vitro and in vivo biological activities	1436:1481	Despite these unusual structural characteristics, the data concerning the in vitro and in vivo biological activities were not impaired when compared to Epo-CHO and uHuEpo.
10764840	0	28	theme	Unusual	0:6	arg1	N-glycosylation					8:22	Unusual N-glycosylation	0:22	Unusual N-glycosylation of a recombinant human erythropoietin expressed in a human lymphoblastoid cell line	0:106	Unusual N-glycosylation of a recombinant human erythropoietin expressed in a human lymphoblastoid cell line does not alter its biological properties.
10764840	8	29	theme	x	1283:1283	arg1	motif					1285:1289	a sialyl Le(x)motif	1271:1289	a sialyl Le(x)motif	1271:1289	Thus, 80% of N-glycans possess a bisecting GlcNAc residue, 25% bear a second fucose residue which is present, in a large part, in a sialyl Le(x)motif, and 13% contain more than three LacNAc repeats (up to five per molecule).
10764840	8	30	dep	%	1149:1149	arg1	possess					1164:1170	possess	1164:1170	possess a bisecting GlcNAc residue	1164:1197	Thus, 80% of N-glycans possess a bisecting GlcNAc residue, 25% bear a second fucose residue which is present, in a large part, in a sialyl Le(x)motif, and 13% contain more than three LacNAc repeats (up to five per molecule).
10764840	8	31	contain	contain	1300:1306	arg1	%					1202:1202	25%	1200:1202	25% bear a second fucose residue which is present, in a large part, in a sialyl Le(x)motif	1200:1289	Thus, 80% of N-glycans possess a bisecting GlcNAc residue, 25% bear a second fucose residue which is present, in a large part, in a sialyl Le(x)motif, and 13% contain more than three LacNAc repeats (up to five per molecule).
10764840	8	31	contain	contain	1300:1306	arg2	repeats					1331:1337	more than three LacNAc repeats	1308:1337	more than three LacNAc repeats (up to five per molecule)	1308:1363	Thus, 80% of N-glycans possess a bisecting GlcNAc residue, 25% bear a second fucose residue which is present, in a large part, in a sialyl Le(x)motif, and 13% contain more than three LacNAc repeats (up to five per molecule).
10764840	8	31	contain	contain	1300:1306	arg1	%					1149:1149	80%	1147:1149	80% of N-glycans possess a bisecting GlcNAc residue	1147:1197	Thus, 80% of N-glycans possess a bisecting GlcNAc residue, 25% bear a second fucose residue which is present, in a large part, in a sialyl Le(x)motif, and 13% contain more than three LacNAc repeats (up to five per molecule).
10764840	8	31	contain	contain	1300:1306	arg1	%					1298:1298	13%	1296:1298	13%	1296:1298	Thus, 80% of N-glycans possess a bisecting GlcNAc residue, 25% bear a second fucose residue which is present, in a large part, in a sialyl Le(x)motif, and 13% contain more than three LacNAc repeats (up to five per molecule).
10764840	7	32	theme	unusual	1116:1122	arg1	characteristics					1124:1138	some unusual characteristics	1111:1138	some unusual characteristics	1111:1138	Surprisingly, the structure of some N-glycan chains, as mainly determined by ESI-MS, revealed some unusual characteristics.
10764840	9	33	theme	biological	1461:1470	arg1	activities					1472:1481	the in vitro and in vivo biological activities	1436:1481	the in vitro and in vivo biological activities	1436:1481	Despite these unusual structural characteristics, the data concerning the in vitro and in vivo biological activities were not impaired when compared to Epo-CHO and uHuEpo.
10764840	4	34	theme	human	747:751	arg1	line					773:776	a human lymphoblastoid cell line	745:776	a human lymphoblastoid cell line	745:776	In an attempt to produce a rHuEpo as close as possible to the uHuEpo, Epo gene was expressed in a human lymphoblastoid cell line, named RPMI 1788.
10764840	6	35	theme	acid	958:961	arg1	sequence					963:970	the amino acid sequence	948:970	the amino acid sequence of the Epo-RPMI	948:986	As expected, the amino acid sequence of the Epo-RPMI conformed to that of uHuEpo.
10764840	8	36	theme	GlcNAc	1184:1189	arg1	residue					1191:1197	a bisecting GlcNAc residue	1172:1197	a bisecting GlcNAc residue	1172:1197	Thus, 80% of N-glycans possess a bisecting GlcNAc residue, 25% bear a second fucose residue which is present, in a large part, in a sialyl Le(x)motif, and 13% contain more than three LacNAc repeats (up to five per molecule).
10764840	1	37	theme	amino	180:184	arg1	acids					186:190	166 amino acids	176:190	a 166 amino acids protein containing three N-glycosylation sites (Asn-24, Asn-38, and Asn-83) and 1 O- glycosylation site (Ser-126) and involved in the regulation of the level of red blood cells	174:367	Erythropoietin (Epo) is a 166 amino acids protein containing three N-glycosylation sites (Asn-24, Asn-38, and Asn-83) and 1 O- glycosylation site (Ser-126) and involved in the regulation of the level of red blood cells.
10764840	9	38	theme	structural	1388:1397	arg1	characteristics					1399:1413	these unusual structural characteristics	1374:1413	these unusual structural characteristics	1374:1413	Despite these unusual structural characteristics, the data concerning the in vitro and in vivo biological activities were not impaired when compared to Epo-CHO and uHuEpo.
10764840	1	39	dep	sites	233:237	arg1	sites					233:237	three N-glycosylation sites	211:237	three N-glycosylation sites (Asn-24, Asn-38, and Asn-83)	211:266	Erythropoietin (Epo) is a 166 amino acids protein containing three N-glycosylation sites (Asn-24, Asn-38, and Asn-83) and 1 O- glycosylation site (Ser-126) and involved in the regulation of the level of red blood cells.
10764840	1	39	dep	sites	233:237	arg1	Asn-38					248:253	Asn-38	248:253	Asn-38	248:253	Erythropoietin (Epo) is a 166 amino acids protein containing three N-glycosylation sites (Asn-24, Asn-38, and Asn-83) and 1 O- glycosylation site (Ser-126) and involved in the regulation of the level of red blood cells.
10764840	1	39	dep	sites	233:237	arg1	Asn-83					260:265	Asn-83	260:265	Asn-83	260:265	Erythropoietin (Epo) is a 166 amino acids protein containing three N-glycosylation sites (Asn-24, Asn-38, and Asn-83) and 1 O- glycosylation site (Ser-126) and involved in the regulation of the level of red blood cells.
10764840	1	39	dep	sites	233:237	arg1	Asn-24					240:245	Asn-24	240:245	Asn-24	240:245	Erythropoietin (Epo) is a 166 amino acids protein containing three N-glycosylation sites (Asn-24, Asn-38, and Asn-83) and 1 O- glycosylation site (Ser-126) and involved in the regulation of the level of red blood cells.
10764840	6	40	theme	amino	952:956	arg1	sequence					963:970	the amino acid sequence	948:970	the amino acid sequence of the Epo-RPMI	948:986	As expected, the amino acid sequence of the Epo-RPMI conformed to that of uHuEpo.
10764840	1	41	theme	acids	186:190	arg1	Erythropoietin					150:163	Erythropoietin	150:163	Erythropoietin (Epo)	150:169	Erythropoietin (Epo) is a 166 amino acids protein containing three N-glycosylation sites (Asn-24, Asn-38, and Asn-83) and 1 O- glycosylation site (Ser-126) and involved in the regulation of the level of red blood cells.
10764840	1	41	theme	acids	186:190	arg1	protein					192:198	a 166 amino acids protein	174:198	a 166 amino acids protein containing three N-glycosylation sites (Asn-24, Asn-38, and Asn-83) and 1 O- glycosylation site (Ser-126) and involved in the regulation of the level of red blood cells	174:367	Erythropoietin (Epo) is a 166 amino acids protein containing three N-glycosylation sites (Asn-24, Asn-38, and Asn-83) and 1 O- glycosylation site (Ser-126) and involved in the regulation of the level of red blood cells.
10764840	0	42	theme	human	41:45	arg1	erythropoietin					47:60	a recombinant human erythropoietin	27:60	a recombinant human erythropoietin expressed in a human lymphoblastoid cell line	27:106	Unusual N-glycosylation of a recombinant human erythropoietin expressed in a human lymphoblastoid cell line does not alter its biological properties.
10764840	4	43	theme	cell	768:771	arg1	line					773:776	a human lymphoblastoid cell line	745:776	a human lymphoblastoid cell line	745:776	In an attempt to produce a rHuEpo as close as possible to the uHuEpo, Epo gene was expressed in a human lymphoblastoid cell line, named RPMI 1788.
10764840	3	44	theme	rHuEpo	542:547	arg1	chains					527:532	the glycan chains	516:532	the glycan chains of this rHuEpo	516:547	The structure of the glycan chains of this rHuEpo slightly differ of those of the urinary human Epo (uHuEpo), considered as the natural Epo molecule.
10764840	4	45	theme	lymphoblastoid	753:766	arg1	line					773:776	a human lymphoblastoid cell line	745:776	a human lymphoblastoid cell line	745:776	In an attempt to produce a rHuEpo as close as possible to the uHuEpo, Epo gene was expressed in a human lymphoblastoid cell line, named RPMI 1788.
10764840	0	46	theme	recombinant	29:39	arg1	erythropoietin					47:60	a recombinant human erythropoietin	27:60	a recombinant human erythropoietin expressed in a human lymphoblastoid cell line	27:106	Unusual N-glycosylation of a recombinant human erythropoietin expressed in a human lymphoblastoid cell line does not alter its biological properties.
10764840	0	47	theme	biological	127:136	arg1	properties					138:147	its biological properties	123:147	its biological properties	123:147	Unusual N-glycosylation of a recombinant human erythropoietin expressed in a human lymphoblastoid cell line does not alter its biological properties.
10764840	1	48	theme	level	344:348	arg1	regulation					326:335	the regulation	322:335	the regulation of the level of red blood cells	322:367	Erythropoietin (Epo) is a 166 amino acids protein containing three N-glycosylation sites (Asn-24, Asn-38, and Asn-83) and 1 O- glycosylation site (Ser-126) and involved in the regulation of the level of red blood cells.
10764840	0	49	gly	N-glycosylation	8:22	arg1	erythropoietin					47:60	a recombinant human erythropoietin	27:60	a recombinant human erythropoietin expressed in a human lymphoblastoid cell line	27:106	Unusual N-glycosylation of a recombinant human erythropoietin expressed in a human lymphoblastoid cell line does not alter its biological properties.
10764840	2	50	theme	human	398:402	arg1	rHuEpo					409:414	rHuEpo	409:414	rHuEpo	409:414	Today, only one recombinant human Epo (rHuEpo), produced in CHO cell line, is extensively used in therapy to cure severe anemia.
10764840	2	50	theme	human	398:402	arg1	Epo					404:406	recombinant human Epo	386:406	only one recombinant human Epo (rHuEpo)	377:415	Today, only one recombinant human Epo (rHuEpo), produced in CHO cell line, is extensively used in therapy to cure severe anemia.
10764840	2	50	theme	human	398:402	arg1	Today					370:374	Today	370:374	Today	370:374	Today, only one recombinant human Epo (rHuEpo), produced in CHO cell line, is extensively used in therapy to cure severe anemia.
10764840	1	51	theme	O-	274:275	arg1	Ser-126					297:303	Ser-126	297:303	Ser-126	297:303	Erythropoietin (Epo) is a 166 amino acids protein containing three N-glycosylation sites (Asn-24, Asn-38, and Asn-83) and 1 O- glycosylation site (Ser-126) and involved in the regulation of the level of red blood cells.
10764840	1	51	theme	O-	274:275	arg1	site					291:294	1 O- glycosylation site	272:294	1 O- glycosylation site (Ser-126)	272:304	Erythropoietin (Epo) is a 166 amino acids protein containing three N-glycosylation sites (Asn-24, Asn-38, and Asn-83) and 1 O- glycosylation site (Ser-126) and involved in the regulation of the level of red blood cells.
10764840	9	52	dep	in	1453:1454	arg1	vivo					1456:1459	vivo	1456:1459	vivo	1456:1459	Despite these unusual structural characteristics, the data concerning the in vitro and in vivo biological activities were not impaired when compared to Epo-CHO and uHuEpo.
10764840	5	53	theme	glycan	905:910	arg1	chains					912:917	glycan chains	905:917	the protein skeleton as well as glycan chains	873:917	In order to fully characterize the Epo-RPMI, structural characterizations of the protein skeleton as well as glycan chains were undergone.
10764840	5	54	theme	structural	841:850	arg1	characterizations					852:868	structural characterizations	841:868	structural characterizations of the protein skeleton as well as glycan chains	841:917	In order to fully characterize the Epo-RPMI, structural characterizations of the protein skeleton as well as glycan chains were undergone.
10764840	0	55	theme	erythropoietin	47:60	arg1	N-glycosylation					8:22	Unusual N-glycosylation	0:22	Unusual N-glycosylation of a recombinant human erythropoietin expressed in a human lymphoblastoid cell line	0:106	Unusual N-glycosylation of a recombinant human erythropoietin expressed in a human lymphoblastoid cell line does not alter its biological properties.
10764840	1	56	theme	glycosylation	277:289	arg1	Ser-126					297:303	Ser-126	297:303	Ser-126	297:303	Erythropoietin (Epo) is a 166 amino acids protein containing three N-glycosylation sites (Asn-24, Asn-38, and Asn-83) and 1 O- glycosylation site (Ser-126) and involved in the regulation of the level of red blood cells.
10764840	1	56	theme	glycosylation	277:289	arg1	site					291:294	1 O- glycosylation site	272:294	1 O- glycosylation site (Ser-126)	272:304	Erythropoietin (Epo) is a 166 amino acids protein containing three N-glycosylation sites (Asn-24, Asn-38, and Asn-83) and 1 O- glycosylation site (Ser-126) and involved in the regulation of the level of red blood cells.
10764840	8	57	theme	large	1256:1260	arg1	part					1262:1265	a large part	1254:1265	a large part	1254:1265	Thus, 80% of N-glycans possess a bisecting GlcNAc residue, 25% bear a second fucose residue which is present, in a large part, in a sialyl Le(x)motif, and 13% contain more than three LacNAc repeats (up to five per molecule).
10764840	1	58	theme	red	353:355	arg1	cells					363:367	red blood cells	353:367	red blood cells	353:367	Erythropoietin (Epo) is a 166 amino acids protein containing three N-glycosylation sites (Asn-24, Asn-38, and Asn-83) and 1 O- glycosylation site (Ser-126) and involved in the regulation of the level of red blood cells.
10764840	3	59	theme	chains	527:532	arg1	structure					503:511	The structure	499:511	The structure of the glycan chains of this rHuEpo	499:547	The structure of the glycan chains of this rHuEpo slightly differ of those of the urinary human Epo (uHuEpo), considered as the natural Epo molecule.
10764840	3	60	theme	Epo	635:637	arg1	molecule					639:646	the natural Epo molecule	623:646	the natural Epo molecule	623:646	The structure of the glycan chains of this rHuEpo slightly differ of those of the urinary human Epo (uHuEpo), considered as the natural Epo molecule.
10764840	8	61	theme	LacNAc	1324:1329	arg1	repeats					1331:1337	more than three LacNAc repeats	1308:1337	more than three LacNAc repeats (up to five per molecule)	1308:1363	Thus, 80% of N-glycans possess a bisecting GlcNAc residue, 25% bear a second fucose residue which is present, in a large part, in a sialyl Le(x)motif, and 13% contain more than three LacNAc repeats (up to five per molecule).
10764840	1	62	theme	blood	357:361	arg1	cells					363:367	red blood cells	353:367	red blood cells	353:367	Erythropoietin (Epo) is a 166 amino acids protein containing three N-glycosylation sites (Asn-24, Asn-38, and Asn-83) and 1 O- glycosylation site (Ser-126) and involved in the regulation of the level of red blood cells.
10764840	1	63	dep	protein	192:198	arg1	involved					310:317	involved	310:317	involved in the regulation of the level of red blood cells	310:367	Erythropoietin (Epo) is a 166 amino acids protein containing three N-glycosylation sites (Asn-24, Asn-38, and Asn-83) and 1 O- glycosylation site (Ser-126) and involved in the regulation of the level of red blood cells.
10764840	1	63	dep	protein	192:198	arg1	containing					200:209	containing	200:209	containing three N-glycosylation sites (Asn-24, Asn-38, and Asn-83) and 1 O- glycosylation site (Ser-126)	200:304	Erythropoietin (Epo) is a 166 amino acids protein containing three N-glycosylation sites (Asn-24, Asn-38, and Asn-83) and 1 O- glycosylation site (Ser-126) and involved in the regulation of the level of red blood cells.
10764840	8	64	theme	bisecting	1174:1182	arg1	residue					1191:1197	a bisecting GlcNAc residue	1172:1197	a bisecting GlcNAc residue	1172:1197	Thus, 80% of N-glycans possess a bisecting GlcNAc residue, 25% bear a second fucose residue which is present, in a large part, in a sialyl Le(x)motif, and 13% contain more than three LacNAc repeats (up to five per molecule).
10764840	9	65	theme	unusual	1380:1386	arg1	characteristics					1399:1413	these unusual structural characteristics	1374:1413	these unusual structural characteristics	1374:1413	Despite these unusual structural characteristics, the data concerning the in vitro and in vivo biological activities were not impaired when compared to Epo-CHO and uHuEpo.
10764840	1	66	theme	cells	363:367	arg1	level					344:348	the level	340:348	the level of red blood cells	340:367	Erythropoietin (Epo) is a 166 amino acids protein containing three N-glycosylation sites (Asn-24, Asn-38, and Asn-83) and 1 O- glycosylation site (Ser-126) and involved in the regulation of the level of red blood cells.
10764840	3	67	theme	glycan	520:525	arg1	chains					527:532	the glycan chains	516:532	the glycan chains of this rHuEpo	516:547	The structure of the glycan chains of this rHuEpo slightly differ of those of the urinary human Epo (uHuEpo), considered as the natural Epo molecule.
10764840	9	68	dep	in	1440:1441	arg1	vitro					1443:1447	vitro	1443:1447	vitro	1443:1447	Despite these unusual structural characteristics, the data concerning the in vitro and in vivo biological activities were not impaired when compared to Epo-CHO and uHuEpo.
10764840	1	69	theme	N-glycosylation	217:231	arg1	sites					233:237	three N-glycosylation sites	211:237	three N-glycosylation sites (Asn-24, Asn-38, and Asn-83)	211:266	Erythropoietin (Epo) is a 166 amino acids protein containing three N-glycosylation sites (Asn-24, Asn-38, and Asn-83) and 1 O- glycosylation site (Ser-126) and involved in the regulation of the level of red blood cells.
10764840	1	69	theme	N-glycosylation	217:231	arg1	Asn-38					248:253	Asn-38	248:253	Asn-38	248:253	Erythropoietin (Epo) is a 166 amino acids protein containing three N-glycosylation sites (Asn-24, Asn-38, and Asn-83) and 1 O- glycosylation site (Ser-126) and involved in the regulation of the level of red blood cells.
10764840	1	69	theme	N-glycosylation	217:231	arg1	Asn-83					260:265	Asn-83	260:265	Asn-83	260:265	Erythropoietin (Epo) is a 166 amino acids protein containing three N-glycosylation sites (Asn-24, Asn-38, and Asn-83) and 1 O- glycosylation site (Ser-126) and involved in the regulation of the level of red blood cells.
10764840	1	69	theme	N-glycosylation	217:231	arg1	Asn-24					240:245	Asn-24	240:245	Asn-24	240:245	Erythropoietin (Epo) is a 166 amino acids protein containing three N-glycosylation sites (Asn-24, Asn-38, and Asn-83) and 1 O- glycosylation site (Ser-126) and involved in the regulation of the level of red blood cells.
10764840	8	70	contain	possess	1164:1170	arg1	N-glycans					1154:1162	N-glycans	1154:1162	N-glycans	1154:1162	Thus, 80% of N-glycans possess a bisecting GlcNAc residue, 25% bear a second fucose residue which is present, in a large part, in a sialyl Le(x)motif, and 13% contain more than three LacNAc repeats (up to five per molecule).
10764840	8	70	contain	possess	1164:1170	arg2	residue					1191:1197	a bisecting GlcNAc residue	1172:1197	a bisecting GlcNAc residue	1172:1197	Thus, 80% of N-glycans possess a bisecting GlcNAc residue, 25% bear a second fucose residue which is present, in a large part, in a sialyl Le(x)motif, and 13% contain more than three LacNAc repeats (up to five per molecule).
10764840	5	71	theme	skeleton	885:892	arg1	characterizations					852:868	structural characterizations	841:868	structural characterizations of the protein skeleton as well as glycan chains	841:917	In order to fully characterize the Epo-RPMI, structural characterizations of the protein skeleton as well as glycan chains were undergone.
10764840	5	72	dep	characterize	814:825	arg1	to					805:806	to	805:806	to	805:806	In order to fully characterize the Epo-RPMI, structural characterizations of the protein skeleton as well as glycan chains were undergone.
10764840	7	73	theme	N-glycan	1053:1060	arg1	chains					1062:1067	some N-glycan chains	1048:1067	some N-glycan chains	1048:1067	Surprisingly, the structure of some N-glycan chains, as mainly determined by ESI-MS, revealed some unusual characteristics.
10764840	3	74	theme	urinary	581:587	arg1	uHuEpo					600:605	uHuEpo	600:605	uHuEpo	600:605	The structure of the glycan chains of this rHuEpo slightly differ of those of the urinary human Epo (uHuEpo), considered as the natural Epo molecule.
10764840	3	74	theme	urinary	581:587	arg1	Epo					595:597	the urinary human Epo	577:597	the urinary human Epo (uHuEpo)	577:606	The structure of the glycan chains of this rHuEpo slightly differ of those of the urinary human Epo (uHuEpo), considered as the natural Epo molecule.
10764840	7	75	dep	revealed	1102:1109	arg1	determined					1080:1089	determined	1080:1089	determined by ESI-MS	1080:1099	Surprisingly, the structure of some N-glycan chains, as mainly determined by ESI-MS, revealed some unusual characteristics.
10764840	8	76	dep	five	1346:1349	arg1	to					1343:1344	to	1343:1344	to	1343:1344	Thus, 80% of N-glycans possess a bisecting GlcNAc residue, 25% bear a second fucose residue which is present, in a large part, in a sialyl Le(x)motif, and 13% contain more than three LacNAc repeats (up to five per molecule).
10764840	7	77	theme	chains	1062:1067	arg1	structure					1035:1043	the structure	1031:1043	the structure of some N-glycan chains	1031:1067	Surprisingly, the structure of some N-glycan chains, as mainly determined by ESI-MS, revealed some unusual characteristics.
10764840	2	78	theme	cell	434:437	arg1	line					439:442	CHO cell line	430:442	CHO cell line	430:442	Today, only one recombinant human Epo (rHuEpo), produced in CHO cell line, is extensively used in therapy to cure severe anemia.
16096263	5	0	from	construct	1083:1091	arg1	efficiency					1054:1063	N-glycosylation efficiency	1038:1063	N-glycosylation efficiency of EC1 in the SAO construct	1038:1091	N-glycosylation efficiency of EC1 in the SAO construct was significantly lower than that of the AE1 construct, indicating that the SAO deletion impairs membrane integration of TM1 and the translocation of EC1 across the membrane.
16096263	4	1	theme	expanded	991:998	arg1	loop					1014:1017	an expanded extracellular loop 1	988:1019	an expanded extracellular loop 1 (EC1)	988:1025	AE1 or SAO constructs containing either the endogenous N-glycosylation site at Asn642 in extracellular loop 4 (EC4) or single N-glycosylation sites engineered into an expanded extracellular loop 1 (EC1) were used.
16096263	4	1	theme	expanded	991:998	arg1	EC1					1022:1024	EC1	1022:1024	EC1	1022:1024	AE1 or SAO constructs containing either the endogenous N-glycosylation site at Asn642 in extracellular loop 4 (EC4) or single N-glycosylation sites engineered into an expanded extracellular loop 1 (EC1) were used.
16096263	5	2	theme	AE1	1134:1136	arg1	construct					1138:1146	the AE1 construct	1130:1146	the AE1 construct	1130:1146	N-glycosylation efficiency of EC1 in the SAO construct was significantly lower than that of the AE1 construct, indicating that the SAO deletion impairs membrane integration of TM1 and the translocation of EC1 across the membrane.
16096263	6	3	theme	relative	1434:1441	arg1	position					1425:1432	the same position	1416:1432	the same position relative to the membrane	1416:1457	Scanning N-glycosylation mapping of EC1 in the cell-free system and in transfected cells showed that the C-terminus of both AE1 and SAO TM1 were at the same position relative to the membrane.
16096263	3	4	theme	TM1	653:655	arg1	positioning					638:648	the precise positioning	626:648	(2) the precise positioning of TM1 relative to the membrane	622:680	The effects of the SAO deletion on: (1) the efficiency of integration of TM1 into the membrane, and (2) the precise positioning of TM1 relative to the membrane were investigated using scanning N-glycosylation mutagenesis in a cell-free transcription/translation system and in transfected HEK293 cells.
16096263	3	4	theme	TM1	653:655	arg1	efficiency					566:575	the efficiency	562:575	: (1) the efficiency of integration of TM1 into the membrane	556:615	The effects of the SAO deletion on: (1) the efficiency of integration of TM1 into the membrane, and (2) the precise positioning of TM1 relative to the membrane were investigated using scanning N-glycosylation mutagenesis in a cell-free transcription/translation system and in transfected HEK293 cells.
16096263	6	5	theme	same	1420:1423	arg1	position					1425:1432	the same position	1416:1432	the same position relative to the membrane	1416:1457	Scanning N-glycosylation mapping of EC1 in the cell-free system and in transfected cells showed that the C-terminus of both AE1 and SAO TM1 were at the same position relative to the membrane.
16096263	7	6	theme	polar	1522:1526	arg1	sequence					1539:1546	the polar amino acid sequence	1518:1546	the polar amino acid sequence immediately N-terminal to the deletion	1518:1585	Thus, the SAO deletion is likely to cause a pulling-in of the polar amino acid sequence immediately N-terminal to the deletion into the lipid bilayer, allowing SAO TM1 that was inserted to assume a transmembrane disposition.
16096263	0	7	theme	erythrocyte	118:128	arg1	exchanger					136:144	ovalocytosis human erythrocyte anion exchanger 1	99:146	ovalocytosis human erythrocyte anion exchanger 1	99:146	Membrane integration and topology of the first transmembrane segment in normal and Southeast Asian ovalocytosis human erythrocyte anion exchanger 1.
16096263	4	8	theme	endogenous	868:877	arg1	site					895:898	the endogenous N-glycosylation site	864:898	the endogenous N-glycosylation site at Asn642 in extracellular loop 4 (EC4)	864:938	AE1 or SAO constructs containing either the endogenous N-glycosylation site at Asn642 in extracellular loop 4 (EC4) or single N-glycosylation sites engineered into an expanded extracellular loop 1 (EC1) were used.
16096263	3	9	theme	SAO	541:543	arg1	deletion					545:552	the SAO deletion	537:552	the SAO deletion	537:552	The effects of the SAO deletion on: (1) the efficiency of integration of TM1 into the membrane, and (2) the precise positioning of TM1 relative to the membrane were investigated using scanning N-glycosylation mutagenesis in a cell-free transcription/translation system and in transfected HEK293 cells.
16096263	7	10	theme	SAO	1620:1622	arg1	TM1					1624:1626	SAO TM1	1620:1626	SAO TM1 that was inserted to assume a transmembrane disposition	1620:1682	Thus, the SAO deletion is likely to cause a pulling-in of the polar amino acid sequence immediately N-terminal to the deletion into the lipid bilayer, allowing SAO TM1 that was inserted to assume a transmembrane disposition.
16096263	3	11	theme	scanning	706:713	arg1	mutagenesis					731:741	scanning N-glycosylation mutagenesis	706:741	scanning N-glycosylation mutagenesis	706:741	The effects of the SAO deletion on: (1) the efficiency of integration of TM1 into the membrane, and (2) the precise positioning of TM1 relative to the membrane were investigated using scanning N-glycosylation mutagenesis in a cell-free transcription/translation system and in transfected HEK293 cells.
16096263	3	12	theme	transcription/translation	758:782	arg1	system					784:789	a cell-free transcription/translation system	746:789	a cell-free transcription/translation system	746:789	The effects of the SAO deletion on: (1) the efficiency of integration of TM1 into the membrane, and (2) the precise positioning of TM1 relative to the membrane were investigated using scanning N-glycosylation mutagenesis in a cell-free transcription/translation system and in transfected HEK293 cells.
16096263	4	13	theme	extracellular	913:925	arg1	loop					927:930	extracellular loop 4	913:932	extracellular loop 4 (EC4)	913:938	AE1 or SAO constructs containing either the endogenous N-glycosylation site at Asn642 in extracellular loop 4 (EC4) or single N-glycosylation sites engineered into an expanded extracellular loop 1 (EC1) were used.
16096263	4	13	theme	extracellular	913:925	arg1	EC4					935:937	EC4	935:937	EC4	935:937	AE1 or SAO constructs containing either the endogenous N-glycosylation site at Asn642 in extracellular loop 4 (EC4) or single N-glycosylation sites engineered into an expanded extracellular loop 1 (EC1) were used.
16096263	5	14	theme	TM1	1214:1216	arg1	translocation					1226:1238	the translocation	1222:1238	the translocation of EC1 across the membrane	1222:1265	N-glycosylation efficiency of EC1 in the SAO construct was significantly lower than that of the AE1 construct, indicating that the SAO deletion impairs membrane integration of TM1 and the translocation of EC1 across the membrane.
16096263	5	14	theme	TM1	1214:1216	arg1	integration					1199:1209	membrane integration	1190:1209	membrane integration of TM1	1190:1216	N-glycosylation efficiency of EC1 in the SAO construct was significantly lower than that of the AE1 construct, indicating that the SAO deletion impairs membrane integration of TM1 and the translocation of EC1 across the membrane.
16096263	0	15	theme	segment	61:67	arg1	topology					25:32	topology	25:32	topology	25:32	Membrane integration and topology of the first transmembrane segment in normal and Southeast Asian ovalocytosis human erythrocyte anion exchanger 1.
16096263	0	15	theme	segment	61:67	arg1	integration					9:19	Membrane integration	0:19	Membrane integration	0:19	Membrane integration and topology of the first transmembrane segment in normal and Southeast Asian ovalocytosis human erythrocyte anion exchanger 1.
16096263	5	16	theme	N-glycosylation	1038:1052	arg1	efficiency					1054:1063	N-glycosylation efficiency	1038:1063	N-glycosylation efficiency of EC1 in the SAO construct	1038:1091	N-glycosylation efficiency of EC1 in the SAO construct was significantly lower than that of the AE1 construct, indicating that the SAO deletion impairs membrane integration of TM1 and the translocation of EC1 across the membrane.
16096263	1	17	theme	Anion	149:153	arg1	glycoprotein					208:219	an integral membrane glycoprotein	187:219	an integral membrane glycoprotein found in erythrocytes, responsible for the electroneutral exchange of chloride and bicarbonate ions across the plasma membrane	187:346	Anion exchanger 1 (AE1, or Band 3) is an integral membrane glycoprotein found in erythrocytes, responsible for the electroneutral exchange of chloride and bicarbonate ions across the plasma membrane.
16096263	1	17	theme	Anion	149:153	arg1	exchanger					155:163	Anion exchanger 1	149:165	Anion exchanger 1 (AE1, or Band 3)	149:182	Anion exchanger 1 (AE1, or Band 3) is an integral membrane glycoprotein found in erythrocytes, responsible for the electroneutral exchange of chloride and bicarbonate ions across the plasma membrane.
16096263	7	18	theme	lipid	1596:1600	arg1	bilayer					1602:1608	the lipid bilayer	1592:1608	the lipid bilayer	1592:1608	Thus, the SAO deletion is likely to cause a pulling-in of the polar amino acid sequence immediately N-terminal to the deletion into the lipid bilayer, allowing SAO TM1 that was inserted to assume a transmembrane disposition.
16096263	7	19	theme	SAO	1470:1472	arg1	likely					1486:1491	likely	1486:1491	likely	1486:1491	Thus, the SAO deletion is likely to cause a pulling-in of the polar amino acid sequence immediately N-terminal to the deletion into the lipid bilayer, allowing SAO TM1 that was inserted to assume a transmembrane disposition.
16096263	7	19	theme	SAO	1470:1472	arg1	deletion					1474:1481	the SAO deletion	1466:1481	the SAO deletion	1466:1481	Thus, the SAO deletion is likely to cause a pulling-in of the polar amino acid sequence immediately N-terminal to the deletion into the lipid bilayer, allowing SAO TM1 that was inserted to assume a transmembrane disposition.
16096263	5	20	theme	SAO	1169:1171	arg1	deletion					1173:1180	the SAO deletion	1165:1180	the SAO deletion	1165:1180	N-glycosylation efficiency of EC1 in the SAO construct was significantly lower than that of the AE1 construct, indicating that the SAO deletion impairs membrane integration of TM1 and the translocation of EC1 across the membrane.
16096263	3	21	theme	transfected	798:808	arg1	cells					817:821	transfected HEK293 cells	798:821	transfected HEK293 cells	798:821	The effects of the SAO deletion on: (1) the efficiency of integration of TM1 into the membrane, and (2) the precise positioning of TM1 relative to the membrane were investigated using scanning N-glycosylation mutagenesis in a cell-free transcription/translation system and in transfected HEK293 cells.
16096263	2	22	from	deletion	415:422	arg1	TM					460:461	TM	460:461	TM	460:461	Southeast Asian ovalocytosis (SAO) results from a nine-amino acid deletion in the first transmembrane segment (TM) of the AE1 protein that abolishes its transport function.
16096263	2	22	from	deletion	415:422	arg1	segment					451:457	the first transmembrane segment	427:457	the first transmembrane segment (TM) of the AE1 protein that abolishes its transport function	427:519	Southeast Asian ovalocytosis (SAO) results from a nine-amino acid deletion in the first transmembrane segment (TM) of the AE1 protein that abolishes its transport function.
16096263	6	23	theme	N-glycosylation	1277:1291	arg1	mapping					1293:1299	Scanning N-glycosylation mapping	1268:1299	Scanning N-glycosylation mapping of EC1 in the cell-free system and in transfected cells	1268:1355	Scanning N-glycosylation mapping of EC1 in the cell-free system and in transfected cells showed that the C-terminus of both AE1 and SAO TM1 were at the same position relative to the membrane.
16096263	1	24	theme	plasma	332:337	arg1	membrane					339:346	the plasma membrane	328:346	the plasma membrane	328:346	Anion exchanger 1 (AE1, or Band 3) is an integral membrane glycoprotein found in erythrocytes, responsible for the electroneutral exchange of chloride and bicarbonate ions across the plasma membrane.
16096263	1	25	gly	glycoprotein	208:219	arg1	glycoprotein					208:219	an integral membrane glycoprotein	187:219	an integral membrane glycoprotein found in erythrocytes, responsible for the electroneutral exchange of chloride and bicarbonate ions across the plasma membrane	187:346	Anion exchanger 1 (AE1, or Band 3) is an integral membrane glycoprotein found in erythrocytes, responsible for the electroneutral exchange of chloride and bicarbonate ions across the plasma membrane.
16096263	1	25	gly	glycoprotein	208:219	arg1	exchanger					155:163	Anion exchanger 1	149:165	Anion exchanger 1 (AE1, or Band 3)	149:182	Anion exchanger 1 (AE1, or Band 3) is an integral membrane glycoprotein found in erythrocytes, responsible for the electroneutral exchange of chloride and bicarbonate ions across the plasma membrane.
16096263	7	26	theme	amino	1528:1532	arg1	sequence					1539:1546	the polar amino acid sequence	1518:1546	the polar amino acid sequence immediately N-terminal to the deletion	1518:1585	Thus, the SAO deletion is likely to cause a pulling-in of the polar amino acid sequence immediately N-terminal to the deletion into the lipid bilayer, allowing SAO TM1 that was inserted to assume a transmembrane disposition.
16096263	2	27	theme	AE1	471:473	arg1	protein					475:481	the AE1 protein	467:481	the AE1 protein that abolishes its transport function	467:519	Southeast Asian ovalocytosis (SAO) results from a nine-amino acid deletion in the first transmembrane segment (TM) of the AE1 protein that abolishes its transport function.
16096263	0	28	theme	ovalocytosis	99:110	arg1	exchanger					136:144	ovalocytosis human erythrocyte anion exchanger 1	99:146	ovalocytosis human erythrocyte anion exchanger 1	99:146	Membrane integration and topology of the first transmembrane segment in normal and Southeast Asian ovalocytosis human erythrocyte anion exchanger 1.
16096263	6	29	from	mapping	1293:1299	arg1	cells					1351:1355	transfected cells	1339:1355	transfected cells	1339:1355	Scanning N-glycosylation mapping of EC1 in the cell-free system and in transfected cells showed that the C-terminus of both AE1 and SAO TM1 were at the same position relative to the membrane.
16096263	6	29	from	mapping	1293:1299	arg1	system					1325:1330	the cell-free system	1311:1330	the cell-free system	1311:1330	Scanning N-glycosylation mapping of EC1 in the cell-free system and in transfected cells showed that the C-terminus of both AE1 and SAO TM1 were at the same position relative to the membrane.
16096263	7	30	theme	N-terminal	1560:1569	arg1	sequence					1539:1546	the polar amino acid sequence	1518:1546	the polar amino acid sequence immediately N-terminal to the deletion	1518:1585	Thus, the SAO deletion is likely to cause a pulling-in of the polar amino acid sequence immediately N-terminal to the deletion into the lipid bilayer, allowing SAO TM1 that was inserted to assume a transmembrane disposition.
16096263	4	31	theme	N-glycosylation	950:964	arg1	sites					966:970	single N-glycosylation sites	943:970	single N-glycosylation sites engineered into an expanded extracellular loop 1 (EC1)	943:1025	AE1 or SAO constructs containing either the endogenous N-glycosylation site at Asn642 in extracellular loop 4 (EC4) or single N-glycosylation sites engineered into an expanded extracellular loop 1 (EC1) were used.
16096263	1	32	dep	exchanger	155:163	arg1	AE1					168:170	AE1	168:170	AE1	168:170	Anion exchanger 1 (AE1, or Band 3) is an integral membrane glycoprotein found in erythrocytes, responsible for the electroneutral exchange of chloride and bicarbonate ions across the plasma membrane.
16096263	1	32	dep	exchanger	155:163	arg1	Band					176:179	Band 3	176:181	Band 3	176:181	Anion exchanger 1 (AE1, or Band 3) is an integral membrane glycoprotein found in erythrocytes, responsible for the electroneutral exchange of chloride and bicarbonate ions across the plasma membrane.
16096263	0	33	theme	Membrane	0:7	arg1	integration					9:19	Membrane integration	0:19	Membrane integration	0:19	Membrane integration and topology of the first transmembrane segment in normal and Southeast Asian ovalocytosis human erythrocyte anion exchanger 1.
16096263	1	34	theme	responsible	244:254	arg1	erythrocytes					230:241	erythrocytes	230:241	erythrocytes	230:241	Anion exchanger 1 (AE1, or Band 3) is an integral membrane glycoprotein found in erythrocytes, responsible for the electroneutral exchange of chloride and bicarbonate ions across the plasma membrane.
16096263	0	35	dep	normal	72:77	arg1	exchanger					136:144	ovalocytosis human erythrocyte anion exchanger 1	99:146	ovalocytosis human erythrocyte anion exchanger 1	99:146	Membrane integration and topology of the first transmembrane segment in normal and Southeast Asian ovalocytosis human erythrocyte anion exchanger 1.
16096263	7	36	theme	sequence	1539:1546	arg1	pulling-in					1504:1513	a pulling-in	1502:1513	a pulling-in of the polar amino acid sequence immediately N-terminal to the deletion	1502:1585	Thus, the SAO deletion is likely to cause a pulling-in of the polar amino acid sequence immediately N-terminal to the deletion into the lipid bilayer, allowing SAO TM1 that was inserted to assume a transmembrane disposition.
16096263	2	37	theme	acid	410:413	arg1	deletion					415:422	a nine-amino acid deletion	397:422	a nine-amino acid deletion in the first transmembrane segment (TM) of the AE1 protein that abolishes its transport function	397:519	Southeast Asian ovalocytosis (SAO) results from a nine-amino acid deletion in the first transmembrane segment (TM) of the AE1 protein that abolishes its transport function.
16096263	6	38	theme	transfected	1339:1349	arg1	cells					1351:1355	transfected cells	1339:1355	transfected cells	1339:1355	Scanning N-glycosylation mapping of EC1 in the cell-free system and in transfected cells showed that the C-terminus of both AE1 and SAO TM1 were at the same position relative to the membrane.
16096263	4	39	contain	containing	846:855	arg1	constructs					835:844	AE1 or SAO constructs	824:844	AE1 or SAO constructs containing either the endogenous N-glycosylation site at Asn642 in extracellular loop 4 (EC4) or single N-glycosylation sites engineered into an expanded extracellular loop 1 (EC1)	824:1025	AE1 or SAO constructs containing either the endogenous N-glycosylation site at Asn642 in extracellular loop 4 (EC4) or single N-glycosylation sites engineered into an expanded extracellular loop 1 (EC1) were used.
16096263	4	39	contain	containing	846:855	arg2	sites					966:970	single N-glycosylation sites	943:970	single N-glycosylation sites engineered into an expanded extracellular loop 1 (EC1)	943:1025	AE1 or SAO constructs containing either the endogenous N-glycosylation site at Asn642 in extracellular loop 4 (EC4) or single N-glycosylation sites engineered into an expanded extracellular loop 1 (EC1) were used.
16096263	4	39	contain	containing	846:855	arg2	site					895:898	the endogenous N-glycosylation site	864:898	the endogenous N-glycosylation site at Asn642 in extracellular loop 4 (EC4)	864:938	AE1 or SAO constructs containing either the endogenous N-glycosylation site at Asn642 in extracellular loop 4 (EC4) or single N-glycosylation sites engineered into an expanded extracellular loop 1 (EC1) were used.
16096263	3	40	theme	integration	580:590	arg1	positioning					638:648	the precise positioning	626:648	(2) the precise positioning of TM1 relative to the membrane	622:680	The effects of the SAO deletion on: (1) the efficiency of integration of TM1 into the membrane, and (2) the precise positioning of TM1 relative to the membrane were investigated using scanning N-glycosylation mutagenesis in a cell-free transcription/translation system and in transfected HEK293 cells.
16096263	3	40	theme	integration	580:590	arg1	efficiency					566:575	the efficiency	562:575	: (1) the efficiency of integration of TM1 into the membrane	556:615	The effects of the SAO deletion on: (1) the efficiency of integration of TM1 into the membrane, and (2) the precise positioning of TM1 relative to the membrane were investigated using scanning N-glycosylation mutagenesis in a cell-free transcription/translation system and in transfected HEK293 cells.
16096263	5	41	from	EC1	1068:1070	arg1	construct					1083:1091	the SAO construct	1075:1091	the SAO construct	1075:1091	N-glycosylation efficiency of EC1 in the SAO construct was significantly lower than that of the AE1 construct, indicating that the SAO deletion impairs membrane integration of TM1 and the translocation of EC1 across the membrane.
16096263	4	42	gly	N-glycosylation	950:964	arg2	sites					966:970	single N-glycosylation sites	943:970	single N-glycosylation sites engineered into an expanded extracellular loop 1 (EC1)	943:1025	AE1 or SAO constructs containing either the endogenous N-glycosylation site at Asn642 in extracellular loop 4 (EC4) or single N-glycosylation sites engineered into an expanded extracellular loop 1 (EC1) were used.
16096263	4	42	gly	N-glycosylation	950:964	arg2	Asn642					903:908	Asn642	903:908	Asn642	903:908	AE1 or SAO constructs containing either the endogenous N-glycosylation site at Asn642 in extracellular loop 4 (EC4) or single N-glycosylation sites engineered into an expanded extracellular loop 1 (EC1) were used.
16096263	2	43	theme	first	431:435	arg1	TM					460:461	TM	460:461	TM	460:461	Southeast Asian ovalocytosis (SAO) results from a nine-amino acid deletion in the first transmembrane segment (TM) of the AE1 protein that abolishes its transport function.
16096263	2	43	theme	first	431:435	arg1	segment					451:457	the first transmembrane segment	427:457	the first transmembrane segment (TM) of the AE1 protein that abolishes its transport function	427:519	Southeast Asian ovalocytosis (SAO) results from a nine-amino acid deletion in the first transmembrane segment (TM) of the AE1 protein that abolishes its transport function.
16096263	5	44	from	efficiency	1054:1063	arg1	construct					1083:1091	the SAO construct	1075:1091	the SAO construct	1075:1091	N-glycosylation efficiency of EC1 in the SAO construct was significantly lower than that of the AE1 construct, indicating that the SAO deletion impairs membrane integration of TM1 and the translocation of EC1 across the membrane.
16096263	5	45	theme	SAO	1079:1081	arg1	construct					1083:1091	the SAO construct	1075:1091	the SAO construct	1075:1091	N-glycosylation efficiency of EC1 in the SAO construct was significantly lower than that of the AE1 construct, indicating that the SAO deletion impairs membrane integration of TM1 and the translocation of EC1 across the membrane.
16096263	3	46	dep	positioning	638:648	arg1	2					623:623	2	623:623	2	623:623	The effects of the SAO deletion on: (1) the efficiency of integration of TM1 into the membrane, and (2) the precise positioning of TM1 relative to the membrane were investigated using scanning N-glycosylation mutagenesis in a cell-free transcription/translation system and in transfected HEK293 cells.
16096263	6	47	theme	SAO	1400:1402	arg1	C-terminus					1373:1382	the C-terminus	1369:1382	the C-terminus of both AE1 and SAO TM1	1369:1406	Scanning N-glycosylation mapping of EC1 in the cell-free system and in transfected cells showed that the C-terminus of both AE1 and SAO TM1 were at the same position relative to the membrane.
16096263	1	48	located	found	221:225	arg2	glycoprotein					208:219	an integral membrane glycoprotein	187:219	an integral membrane glycoprotein found in erythrocytes, responsible for the electroneutral exchange of chloride and bicarbonate ions across the plasma membrane	187:346	Anion exchanger 1 (AE1, or Band 3) is an integral membrane glycoprotein found in erythrocytes, responsible for the electroneutral exchange of chloride and bicarbonate ions across the plasma membrane.
16096263	1	48	located	found	221:225	arg2	exchanger					155:163	Anion exchanger 1	149:165	Anion exchanger 1 (AE1, or Band 3)	149:182	Anion exchanger 1 (AE1, or Band 3) is an integral membrane glycoprotein found in erythrocytes, responsible for the electroneutral exchange of chloride and bicarbonate ions across the plasma membrane.
16096263	1	48	located	found	221:225	arg1	erythrocytes					230:241	erythrocytes	230:241	erythrocytes	230:241	Anion exchanger 1 (AE1, or Band 3) is an integral membrane glycoprotein found in erythrocytes, responsible for the electroneutral exchange of chloride and bicarbonate ions across the plasma membrane.
16096263	3	49	theme	TM1	595:597	arg1	integration					580:590	integration	580:590	integration of TM1 into the membrane	580:615	The effects of the SAO deletion on: (1) the efficiency of integration of TM1 into the membrane, and (2) the precise positioning of TM1 relative to the membrane were investigated using scanning N-glycosylation mutagenesis in a cell-free transcription/translation system and in transfected HEK293 cells.
16096263	2	50	theme	Southeast	349:357	arg1	SAO					379:381	SAO	379:381	SAO	379:381	Southeast Asian ovalocytosis (SAO) results from a nine-amino acid deletion in the first transmembrane segment (TM) of the AE1 protein that abolishes its transport function.
16096263	2	50	theme	Southeast	349:357	arg1	ovalocytosis					365:376	Southeast Asian ovalocytosis	349:376	Southeast Asian ovalocytosis (SAO)	349:382	Southeast Asian ovalocytosis (SAO) results from a nine-amino acid deletion in the first transmembrane segment (TM) of the AE1 protein that abolishes its transport function.
16096263	6	51	theme	AE1	1392:1394	arg1	C-terminus					1373:1382	the C-terminus	1369:1382	the C-terminus of both AE1 and SAO TM1	1369:1406	Scanning N-glycosylation mapping of EC1 in the cell-free system and in transfected cells showed that the C-terminus of both AE1 and SAO TM1 were at the same position relative to the membrane.
16096263	1	52	theme	membrane	199:206	arg1	glycoprotein					208:219	an integral membrane glycoprotein	187:219	an integral membrane glycoprotein found in erythrocytes, responsible for the electroneutral exchange of chloride and bicarbonate ions across the plasma membrane	187:346	Anion exchanger 1 (AE1, or Band 3) is an integral membrane glycoprotein found in erythrocytes, responsible for the electroneutral exchange of chloride and bicarbonate ions across the plasma membrane.
16096263	1	52	theme	membrane	199:206	arg1	exchanger					155:163	Anion exchanger 1	149:165	Anion exchanger 1 (AE1, or Band 3)	149:182	Anion exchanger 1 (AE1, or Band 3) is an integral membrane glycoprotein found in erythrocytes, responsible for the electroneutral exchange of chloride and bicarbonate ions across the plasma membrane.
16096263	4	53	from	Asn642	903:908	arg1	sites					966:970	single N-glycosylation sites	943:970	single N-glycosylation sites engineered into an expanded extracellular loop 1 (EC1)	943:1025	AE1 or SAO constructs containing either the endogenous N-glycosylation site at Asn642 in extracellular loop 4 (EC4) or single N-glycosylation sites engineered into an expanded extracellular loop 1 (EC1) were used.
16096263	4	53	from	Asn642	903:908	arg1	site					895:898	the endogenous N-glycosylation site	864:898	the endogenous N-glycosylation site at Asn642 in extracellular loop 4 (EC4)	864:938	AE1 or SAO constructs containing either the endogenous N-glycosylation site at Asn642 in extracellular loop 4 (EC4) or single N-glycosylation sites engineered into an expanded extracellular loop 1 (EC1) were used.
16096263	7	54	theme	transmembrane	1658:1670	arg1	disposition					1672:1682	a transmembrane disposition	1656:1682	a transmembrane disposition	1656:1682	Thus, the SAO deletion is likely to cause a pulling-in of the polar amino acid sequence immediately N-terminal to the deletion into the lipid bilayer, allowing SAO TM1 that was inserted to assume a transmembrane disposition.
16096263	4	55	theme	extracellular	1000:1012	arg1	loop					1014:1017	an expanded extracellular loop 1	988:1019	an expanded extracellular loop 1 (EC1)	988:1025	AE1 or SAO constructs containing either the endogenous N-glycosylation site at Asn642 in extracellular loop 4 (EC4) or single N-glycosylation sites engineered into an expanded extracellular loop 1 (EC1) were used.
16096263	4	55	theme	extracellular	1000:1012	arg1	EC1					1022:1024	EC1	1022:1024	EC1	1022:1024	AE1 or SAO constructs containing either the endogenous N-glycosylation site at Asn642 in extracellular loop 4 (EC4) or single N-glycosylation sites engineered into an expanded extracellular loop 1 (EC1) were used.
16096263	4	56	from	site	895:898	arg1	loop					927:930	extracellular loop 4	913:932	extracellular loop 4 (EC4)	913:938	AE1 or SAO constructs containing either the endogenous N-glycosylation site at Asn642 in extracellular loop 4 (EC4) or single N-glycosylation sites engineered into an expanded extracellular loop 1 (EC1) were used.
16096263	4	56	from	site	895:898	arg1	EC4					935:937	EC4	935:937	EC4	935:937	AE1 or SAO constructs containing either the endogenous N-glycosylation site at Asn642 in extracellular loop 4 (EC4) or single N-glycosylation sites engineered into an expanded extracellular loop 1 (EC1) were used.
16096263	3	57	theme	precise	630:636	arg1	positioning					638:648	the precise positioning	626:648	(2) the precise positioning of TM1 relative to the membrane	622:680	The effects of the SAO deletion on: (1) the efficiency of integration of TM1 into the membrane, and (2) the precise positioning of TM1 relative to the membrane were investigated using scanning N-glycosylation mutagenesis in a cell-free transcription/translation system and in transfected HEK293 cells.
16096263	0	58	theme	first	41:45	arg1	segment					61:67	the first transmembrane segment	37:67	the first transmembrane segment	37:67	Membrane integration and topology of the first transmembrane segment in normal and Southeast Asian ovalocytosis human erythrocyte anion exchanger 1.
16096263	1	59	theme	chloride	291:298	arg1	exchange					279:286	the electroneutral exchange	260:286	the electroneutral exchange of chloride and bicarbonate ions across the plasma membrane	260:346	Anion exchanger 1 (AE1, or Band 3) is an integral membrane glycoprotein found in erythrocytes, responsible for the electroneutral exchange of chloride and bicarbonate ions across the plasma membrane.
16096263	0	60	theme	anion	130:134	arg1	exchanger					136:144	ovalocytosis human erythrocyte anion exchanger 1	99:146	ovalocytosis human erythrocyte anion exchanger 1	99:146	Membrane integration and topology of the first transmembrane segment in normal and Southeast Asian ovalocytosis human erythrocyte anion exchanger 1.
16096263	2	61	theme	transport	502:510	arg1	function					512:519	its transport function	498:519	its transport function	498:519	Southeast Asian ovalocytosis (SAO) results from a nine-amino acid deletion in the first transmembrane segment (TM) of the AE1 protein that abolishes its transport function.
16096263	3	62	theme	deletion	545:552	arg1	effects					526:532	The effects	522:532	The effects of the SAO deletion on: (1) the efficiency of integration of TM1 into the membrane, and (2) the precise positioning of TM1 relative to the membrane	522:680	The effects of the SAO deletion on: (1) the efficiency of integration of TM1 into the membrane, and (2) the precise positioning of TM1 relative to the membrane were investigated using scanning N-glycosylation mutagenesis in a cell-free transcription/translation system and in transfected HEK293 cells.
16096263	4	63	theme	AE1	824:826	arg1	constructs					835:844	AE1 or SAO constructs	824:844	AE1 or SAO constructs containing either the endogenous N-glycosylation site at Asn642 in extracellular loop 4 (EC4) or single N-glycosylation sites engineered into an expanded extracellular loop 1 (EC1)	824:1025	AE1 or SAO constructs containing either the endogenous N-glycosylation site at Asn642 in extracellular loop 4 (EC4) or single N-glycosylation sites engineered into an expanded extracellular loop 1 (EC1) were used.
16096263	5	64	theme	membrane	1190:1197	arg1	integration					1199:1209	membrane integration	1190:1209	membrane integration of TM1	1190:1216	N-glycosylation efficiency of EC1 in the SAO construct was significantly lower than that of the AE1 construct, indicating that the SAO deletion impairs membrane integration of TM1 and the translocation of EC1 across the membrane.
16096263	4	65	theme	SAO	831:833	arg1	constructs					835:844	AE1 or SAO constructs	824:844	AE1 or SAO constructs containing either the endogenous N-glycosylation site at Asn642 in extracellular loop 4 (EC4) or single N-glycosylation sites engineered into an expanded extracellular loop 1 (EC1)	824:1025	AE1 or SAO constructs containing either the endogenous N-glycosylation site at Asn642 in extracellular loop 4 (EC4) or single N-glycosylation sites engineered into an expanded extracellular loop 1 (EC1) were used.
16096263	3	66	from	effects	526:532	arg1	positioning					638:648	the precise positioning	626:648	(2) the precise positioning of TM1 relative to the membrane	622:680	The effects of the SAO deletion on: (1) the efficiency of integration of TM1 into the membrane, and (2) the precise positioning of TM1 relative to the membrane were investigated using scanning N-glycosylation mutagenesis in a cell-free transcription/translation system and in transfected HEK293 cells.
16096263	3	66	from	effects	526:532	arg1	efficiency					566:575	the efficiency	562:575	: (1) the efficiency of integration of TM1 into the membrane	556:615	The effects of the SAO deletion on: (1) the efficiency of integration of TM1 into the membrane, and (2) the precise positioning of TM1 relative to the membrane were investigated using scanning N-glycosylation mutagenesis in a cell-free transcription/translation system and in transfected HEK293 cells.
16096263	3	67	theme	N-glycosylation	715:729	arg1	mutagenesis					731:741	scanning N-glycosylation mutagenesis	706:741	scanning N-glycosylation mutagenesis	706:741	The effects of the SAO deletion on: (1) the efficiency of integration of TM1 into the membrane, and (2) the precise positioning of TM1 relative to the membrane were investigated using scanning N-glycosylation mutagenesis in a cell-free transcription/translation system and in transfected HEK293 cells.
16096263	1	68	theme	bicarbonate	304:314	arg1	exchange					279:286	the electroneutral exchange	260:286	the electroneutral exchange of chloride and bicarbonate ions across the plasma membrane	260:346	Anion exchanger 1 (AE1, or Band 3) is an integral membrane glycoprotein found in erythrocytes, responsible for the electroneutral exchange of chloride and bicarbonate ions across the plasma membrane.
16096263	0	69	from	topology	25:32	arg1	normal					72:77	normal	72:77	normal	72:77	Membrane integration and topology of the first transmembrane segment in normal and Southeast Asian ovalocytosis human erythrocyte anion exchanger 1.
16096263	0	69	from	topology	25:32	arg1	Asian					93:97	Asian	93:97	Asian	93:97	Membrane integration and topology of the first transmembrane segment in normal and Southeast Asian ovalocytosis human erythrocyte anion exchanger 1.
16096263	4	70	theme	N-glycosylation	879:893	arg1	site					895:898	the endogenous N-glycosylation site	864:898	the endogenous N-glycosylation site at Asn642 in extracellular loop 4 (EC4)	864:938	AE1 or SAO constructs containing either the endogenous N-glycosylation site at Asn642 in extracellular loop 4 (EC4) or single N-glycosylation sites engineered into an expanded extracellular loop 1 (EC1) were used.
16096263	6	71	theme	EC1	1304:1306	arg1	mapping					1293:1299	Scanning N-glycosylation mapping	1268:1299	Scanning N-glycosylation mapping of EC1 in the cell-free system and in transfected cells	1268:1355	Scanning N-glycosylation mapping of EC1 in the cell-free system and in transfected cells showed that the C-terminus of both AE1 and SAO TM1 were at the same position relative to the membrane.
16096263	0	72	from	integration	9:19	arg1	normal					72:77	normal	72:77	normal	72:77	Membrane integration and topology of the first transmembrane segment in normal and Southeast Asian ovalocytosis human erythrocyte anion exchanger 1.
16096263	0	72	from	integration	9:19	arg1	Asian					93:97	Asian	93:97	Asian	93:97	Membrane integration and topology of the first transmembrane segment in normal and Southeast Asian ovalocytosis human erythrocyte anion exchanger 1.
16096263	3	73	theme	cell-free	748:756	arg1	system					784:789	a cell-free transcription/translation system	746:789	a cell-free transcription/translation system	746:789	The effects of the SAO deletion on: (1) the efficiency of integration of TM1 into the membrane, and (2) the precise positioning of TM1 relative to the membrane were investigated using scanning N-glycosylation mutagenesis in a cell-free transcription/translation system and in transfected HEK293 cells.
16096263	5	74	theme	EC1	1068:1070	arg1	efficiency					1054:1063	N-glycosylation efficiency	1038:1063	N-glycosylation efficiency of EC1 in the SAO construct	1038:1091	N-glycosylation efficiency of EC1 in the SAO construct was significantly lower than that of the AE1 construct, indicating that the SAO deletion impairs membrane integration of TM1 and the translocation of EC1 across the membrane.
16096263	3	75	theme	HEK293	810:815	arg1	cells					817:821	transfected HEK293 cells	798:821	transfected HEK293 cells	798:821	The effects of the SAO deletion on: (1) the efficiency of integration of TM1 into the membrane, and (2) the precise positioning of TM1 relative to the membrane were investigated using scanning N-glycosylation mutagenesis in a cell-free transcription/translation system and in transfected HEK293 cells.
16096263	2	76	theme	protein	475:481	arg1	TM					460:461	TM	460:461	TM	460:461	Southeast Asian ovalocytosis (SAO) results from a nine-amino acid deletion in the first transmembrane segment (TM) of the AE1 protein that abolishes its transport function.
16096263	2	76	theme	protein	475:481	arg1	segment					451:457	the first transmembrane segment	427:457	the first transmembrane segment (TM) of the AE1 protein that abolishes its transport function	427:519	Southeast Asian ovalocytosis (SAO) results from a nine-amino acid deletion in the first transmembrane segment (TM) of the AE1 protein that abolishes its transport function.
16096263	1	77	dep	chloride	291:298	arg1	ions					316:319	ions	316:319	ions	316:319	Anion exchanger 1 (AE1, or Band 3) is an integral membrane glycoprotein found in erythrocytes, responsible for the electroneutral exchange of chloride and bicarbonate ions across the plasma membrane.
16096263	5	78	theme	EC1	1243:1245	arg1	translocation					1226:1238	the translocation	1222:1238	the translocation of EC1 across the membrane	1222:1265	N-glycosylation efficiency of EC1 in the SAO construct was significantly lower than that of the AE1 construct, indicating that the SAO deletion impairs membrane integration of TM1 and the translocation of EC1 across the membrane.
16096263	5	78	theme	EC1	1243:1245	arg1	integration					1199:1209	membrane integration	1190:1209	membrane integration of TM1	1190:1216	N-glycosylation efficiency of EC1 in the SAO construct was significantly lower than that of the AE1 construct, indicating that the SAO deletion impairs membrane integration of TM1 and the translocation of EC1 across the membrane.
16096263	6	79	theme	Scanning	1268:1275	arg1	mapping					1293:1299	Scanning N-glycosylation mapping	1268:1299	Scanning N-glycosylation mapping of EC1 in the cell-free system and in transfected cells	1268:1355	Scanning N-glycosylation mapping of EC1 in the cell-free system and in transfected cells showed that the C-terminus of both AE1 and SAO TM1 were at the same position relative to the membrane.
16096263	1	80	theme	integral	190:197	arg1	glycoprotein					208:219	an integral membrane glycoprotein	187:219	an integral membrane glycoprotein found in erythrocytes, responsible for the electroneutral exchange of chloride and bicarbonate ions across the plasma membrane	187:346	Anion exchanger 1 (AE1, or Band 3) is an integral membrane glycoprotein found in erythrocytes, responsible for the electroneutral exchange of chloride and bicarbonate ions across the plasma membrane.
16096263	1	80	theme	integral	190:197	arg1	exchanger					155:163	Anion exchanger 1	149:165	Anion exchanger 1 (AE1, or Band 3)	149:182	Anion exchanger 1 (AE1, or Band 3) is an integral membrane glycoprotein found in erythrocytes, responsible for the electroneutral exchange of chloride and bicarbonate ions across the plasma membrane.
16096263	0	81	theme	human	112:116	arg1	exchanger					136:144	ovalocytosis human erythrocyte anion exchanger 1	99:146	ovalocytosis human erythrocyte anion exchanger 1	99:146	Membrane integration and topology of the first transmembrane segment in normal and Southeast Asian ovalocytosis human erythrocyte anion exchanger 1.
16096263	4	82	gly	N-glycosylation	879:893	arg2	Asn642					903:908	Asn642	903:908	Asn642	903:908	AE1 or SAO constructs containing either the endogenous N-glycosylation site at Asn642 in extracellular loop 4 (EC4) or single N-glycosylation sites engineered into an expanded extracellular loop 1 (EC1) were used.
16096263	4	82	gly	N-glycosylation	879:893	arg2	site					895:898	the endogenous N-glycosylation site	864:898	the endogenous N-glycosylation site at Asn642 in extracellular loop 4 (EC4)	864:938	AE1 or SAO constructs containing either the endogenous N-glycosylation site at Asn642 in extracellular loop 4 (EC4) or single N-glycosylation sites engineered into an expanded extracellular loop 1 (EC1) were used.
16096263	4	83	theme	single	943:948	arg1	sites					966:970	single N-glycosylation sites	943:970	single N-glycosylation sites engineered into an expanded extracellular loop 1 (EC1)	943:1025	AE1 or SAO constructs containing either the endogenous N-glycosylation site at Asn642 in extracellular loop 4 (EC4) or single N-glycosylation sites engineered into an expanded extracellular loop 1 (EC1) were used.
16096263	2	84	theme	Asian	359:363	arg1	SAO					379:381	SAO	379:381	SAO	379:381	Southeast Asian ovalocytosis (SAO) results from a nine-amino acid deletion in the first transmembrane segment (TM) of the AE1 protein that abolishes its transport function.
16096263	2	84	theme	Asian	359:363	arg1	ovalocytosis					365:376	Southeast Asian ovalocytosis	349:376	Southeast Asian ovalocytosis (SAO)	349:382	Southeast Asian ovalocytosis (SAO) results from a nine-amino acid deletion in the first transmembrane segment (TM) of the AE1 protein that abolishes its transport function.
16096263	4	85	from	sites	966:970	arg1	loop					927:930	extracellular loop 4	913:932	extracellular loop 4 (EC4)	913:938	AE1 or SAO constructs containing either the endogenous N-glycosylation site at Asn642 in extracellular loop 4 (EC4) or single N-glycosylation sites engineered into an expanded extracellular loop 1 (EC1) were used.
16096263	4	85	from	sites	966:970	arg1	EC4					935:937	EC4	935:937	EC4	935:937	AE1 or SAO constructs containing either the endogenous N-glycosylation site at Asn642 in extracellular loop 4 (EC4) or single N-glycosylation sites engineered into an expanded extracellular loop 1 (EC1) were used.
16096263	2	86	theme	nine-amino	399:408	arg1	deletion					415:422	a nine-amino acid deletion	397:422	a nine-amino acid deletion in the first transmembrane segment (TM) of the AE1 protein that abolishes its transport function	397:519	Southeast Asian ovalocytosis (SAO) results from a nine-amino acid deletion in the first transmembrane segment (TM) of the AE1 protein that abolishes its transport function.
16096263	1	87	theme	electroneutral	264:277	arg1	exchange					279:286	the electroneutral exchange	260:286	the electroneutral exchange of chloride and bicarbonate ions across the plasma membrane	260:346	Anion exchanger 1 (AE1, or Band 3) is an integral membrane glycoprotein found in erythrocytes, responsible for the electroneutral exchange of chloride and bicarbonate ions across the plasma membrane.
16096263	7	88	theme	acid	1534:1537	arg1	sequence					1539:1546	the polar amino acid sequence	1518:1546	the polar amino acid sequence immediately N-terminal to the deletion	1518:1585	Thus, the SAO deletion is likely to cause a pulling-in of the polar amino acid sequence immediately N-terminal to the deletion into the lipid bilayer, allowing SAO TM1 that was inserted to assume a transmembrane disposition.
16096263	2	89	theme	transmembrane	437:449	arg1	TM					460:461	TM	460:461	TM	460:461	Southeast Asian ovalocytosis (SAO) results from a nine-amino acid deletion in the first transmembrane segment (TM) of the AE1 protein that abolishes its transport function.
16096263	2	89	theme	transmembrane	437:449	arg1	segment					451:457	the first transmembrane segment	427:457	the first transmembrane segment (TM) of the AE1 protein that abolishes its transport function	427:519	Southeast Asian ovalocytosis (SAO) results from a nine-amino acid deletion in the first transmembrane segment (TM) of the AE1 protein that abolishes its transport function.
16096263	0	90	theme	transmembrane	47:59	arg1	segment					61:67	the first transmembrane segment	37:67	the first transmembrane segment	37:67	Membrane integration and topology of the first transmembrane segment in normal and Southeast Asian ovalocytosis human erythrocyte anion exchanger 1.
16096263	4	91	used	used	1032:1035	arg2	constructs					835:844	AE1 or SAO constructs	824:844	AE1 or SAO constructs containing either the endogenous N-glycosylation site at Asn642 in extracellular loop 4 (EC4) or single N-glycosylation sites engineered into an expanded extracellular loop 1 (EC1)	824:1025	AE1 or SAO constructs containing either the endogenous N-glycosylation site at Asn642 in extracellular loop 4 (EC4) or single N-glycosylation sites engineered into an expanded extracellular loop 1 (EC1) were used.
16096263	3	92	dep	efficiency	566:575	arg1	1					559:559	1	559:559	1	559:559	The effects of the SAO deletion on: (1) the efficiency of integration of TM1 into the membrane, and (2) the precise positioning of TM1 relative to the membrane were investigated using scanning N-glycosylation mutagenesis in a cell-free transcription/translation system and in transfected HEK293 cells.
16096263	6	93	dep	AE1	1392:1394	arg1	TM1					1404:1406	TM1	1404:1406	TM1	1404:1406	Scanning N-glycosylation mapping of EC1 in the cell-free system and in transfected cells showed that the C-terminus of both AE1 and SAO TM1 were at the same position relative to the membrane.
16096263	6	94	theme	cell-free	1315:1323	arg1	system					1325:1330	the cell-free system	1311:1330	the cell-free system	1311:1330	Scanning N-glycosylation mapping of EC1 in the cell-free system and in transfected cells showed that the C-terminus of both AE1 and SAO TM1 were at the same position relative to the membrane.
10677208	4	0	theme	insect	930:935	arg1	cells					937:941	insect cells	930:941	insect cells	930:941	When we examined the status of this N-glycosylation using MALDI-TOF mass spectrometry and enzymatic analysis, we found that CR3 is one of the rare recombinant peptides modified with complex glycans in insect cells.
10677208	2	1	theme	cell	514:517	arg1	line					519:522	another lepidopteran cell line	493:522	another lepidopteran cell line	493:522	Spodoptera frugiperda (Sf9) cells have proved a suitable cell system in which to study this association and to produce recombinant CR3, and we show here that another lepidopteran cell line, Trichoplusia niTN-5B1-4 (High-Five) cells, allows the recovery of large amounts of functional recombinant CR3.
10677208	2	1	theme	cell	514:517	arg1	cells					561:565	Trichoplusia niTN-5B1-4 (High-Five) cells	525:565	Trichoplusia niTN-5B1-4 (High-Five) cells	525:565	Spodoptera frugiperda (Sf9) cells have proved a suitable cell system in which to study this association and to produce recombinant CR3, and we show here that another lepidopteran cell line, Trichoplusia niTN-5B1-4 (High-Five) cells, allows the recovery of large amounts of functional recombinant CR3.
10677208	1	2	theme	third	243:247	arg1	module					289:294	the third eight-cysteine (also referred to as TB) module	239:294	the third eight-cysteine (also referred to as TB) module of LTBP-1, a domain designated as CR3	239:332	Covalent association of LTBP-1 (latent TGF-beta binding protein-1) to latent TGF-beta is mediated by the third eight-cysteine (also referred to as TB) module of LTBP-1, a domain designated as CR3.
10677208	2	3	theme	High-Five	550:558	arg1	line					519:522	another lepidopteran cell line	493:522	another lepidopteran cell line	493:522	Spodoptera frugiperda (Sf9) cells have proved a suitable cell system in which to study this association and to produce recombinant CR3, and we show here that another lepidopteran cell line, Trichoplusia niTN-5B1-4 (High-Five) cells, allows the recovery of large amounts of functional recombinant CR3.
10677208	2	3	theme	High-Five	550:558	arg1	cells					561:565	Trichoplusia niTN-5B1-4 (High-Five) cells	525:565	Trichoplusia niTN-5B1-4 (High-Five) cells	525:565	Spodoptera frugiperda (Sf9) cells have proved a suitable cell system in which to study this association and to produce recombinant CR3, and we show here that another lepidopteran cell line, Trichoplusia niTN-5B1-4 (High-Five) cells, allows the recovery of large amounts of functional recombinant CR3.
10677208	7	4	theme	Most	1263:1266	arg1	glycans					1268:1274	Most glycans	1263:1274	Most glycans	1263:1274	Most glycans had one or two fucose residues bound through alpha1,3 and alpha1,6 linkages to the innermost GlcNAc.
10677208	1	5	theme	LTBP-1	162:167	arg1	association					147:157	Covalent association	138:157	Covalent association of LTBP-1 (latent TGF-beta binding protein-1) to latent TGF-beta	138:222	Covalent association of LTBP-1 (latent TGF-beta binding protein-1) to latent TGF-beta is mediated by the third eight-cysteine (also referred to as TB) module of LTBP-1, a domain designated as CR3.
10677208	2	6	theme	niTN-5B1-4	538:547	arg1	line					519:522	another lepidopteran cell line	493:522	another lepidopteran cell line	493:522	Spodoptera frugiperda (Sf9) cells have proved a suitable cell system in which to study this association and to produce recombinant CR3, and we show here that another lepidopteran cell line, Trichoplusia niTN-5B1-4 (High-Five) cells, allows the recovery of large amounts of functional recombinant CR3.
10677208	2	6	theme	niTN-5B1-4	538:547	arg1	cells					561:565	Trichoplusia niTN-5B1-4 (High-Five) cells	525:565	Trichoplusia niTN-5B1-4 (High-Five) cells	525:565	Spodoptera frugiperda (Sf9) cells have proved a suitable cell system in which to study this association and to produce recombinant CR3, and we show here that another lepidopteran cell line, Trichoplusia niTN-5B1-4 (High-Five) cells, allows the recovery of large amounts of functional recombinant CR3.
10677208	0	7	attach	linked	31:36	arg1	site					71:74	the conserved N-glycosylation site	41:74	the conserved N-glycosylation site of the third eight-cysteine domain of LTBP-1 in insect cells	41:135	Hybrid and complex glycans are linked to the conserved N-glycosylation site of the third eight-cysteine domain of LTBP-1 in insect cells.
10677208	0	7	attach	linked	31:36	arg2	glycans					19:25	Hybrid and complex glycans	0:25	glycans	19:25	Hybrid and complex glycans are linked to the conserved N-glycosylation site of the third eight-cysteine domain of LTBP-1 in insect cells.
10677208	0	7	attach	linked	31:36	arg1	domain					104:109	the third eight-cysteine domain	79:109	the third eight-cysteine domain of LTBP-1 in insect cells	79:135	Hybrid and complex glycans are linked to the conserved N-glycosylation site of the third eight-cysteine domain of LTBP-1 in insect cells.
10677208	1	8	theme	latent	170:175	arg1	protein-1					194:202	latent TGF-beta binding protein-1	170:202	latent TGF-beta binding protein-1	170:202	Covalent association of LTBP-1 (latent TGF-beta binding protein-1) to latent TGF-beta is mediated by the third eight-cysteine (also referred to as TB) module of LTBP-1, a domain designated as CR3.
10677208	1	8	theme	latent	170:175	arg1	LTBP-1					162:167	LTBP-1	162:167	LTBP-1 (latent TGF-beta binding protein-1)	162:203	Covalent association of LTBP-1 (latent TGF-beta binding protein-1) to latent TGF-beta is mediated by the third eight-cysteine (also referred to as TB) module of LTBP-1, a domain designated as CR3.
10677208	4	9	theme	enzymatic	819:827	arg1	analysis					829:836	enzymatic analysis	819:836	enzymatic analysis	819:836	When we examined the status of this N-glycosylation using MALDI-TOF mass spectrometry and enzymatic analysis, we found that CR3 is one of the rare recombinant peptides modified with complex glycans in insect cells.
10677208	5	10	gly	fucosylated	975:985	arg1	Fucose					1036:1041	the fucosylated paucomannosidic structure (GlcNAc)(2)(Mannose)(3)Fucose	971:1041	the fucosylated paucomannosidic structure (GlcNAc)(2)(Mannose)(3)Fucose	971:1041	Sf9 cells mainly processed the fucosylated paucomannosidic structure (GlcNAc)(2)(Mannose)(3)Fucose, although hybrid and complex N-glycosylations were also detected.
10677208	8	11	theme	domain	1569:1574	arg1	interactions					1592:1603	eight-cysteine domain protein-protein interactions	1554:1603	eight-cysteine domain protein-protein interactions	1554:1603	On the basis of these results and on the structure of an eight-cysteine domain from fibrillin-1, we present a model of glycosylated CR3 and discuss the role of glycosylation in eight-cysteine domain protein-protein interactions.
10677208	1	12	theme	binding	186:192	arg1	protein-1					194:202	latent TGF-beta binding protein-1	170:202	latent TGF-beta binding protein-1	170:202	Covalent association of LTBP-1 (latent TGF-beta binding protein-1) to latent TGF-beta is mediated by the third eight-cysteine (also referred to as TB) module of LTBP-1, a domain designated as CR3.
10677208	1	12	theme	binding	186:192	arg1	LTBP-1					162:167	LTBP-1	162:167	LTBP-1 (latent TGF-beta binding protein-1)	162:203	Covalent association of LTBP-1 (latent TGF-beta binding protein-1) to latent TGF-beta is mediated by the third eight-cysteine (also referred to as TB) module of LTBP-1, a domain designated as CR3.
10677208	0	13	from	site	71:74	arg1	cells					131:135	insect cells	124:135	insect cells	124:135	Hybrid and complex glycans are linked to the conserved N-glycosylation site of the third eight-cysteine domain of LTBP-1 in insect cells.
10677208	8	14	from	structure	1418:1426	arg1	fibrillin-1					1461:1471	fibrillin-1	1461:1471	fibrillin-1	1461:1471	On the basis of these results and on the structure of an eight-cysteine domain from fibrillin-1, we present a model of glycosylated CR3 and discuss the role of glycosylation in eight-cysteine domain protein-protein interactions.
10677208	4	15	theme	MALDI-TOF	787:795	arg1	spectrometry					802:813	MALDI-TOF mass spectrometry	787:813	MALDI-TOF mass spectrometry	787:813	When we examined the status of this N-glycosylation using MALDI-TOF mass spectrometry and enzymatic analysis, we found that CR3 is one of the rare recombinant peptides modified with complex glycans in insect cells.
10677208	2	16	theme	functional	608:617	arg1	CR3					631:633	functional recombinant CR3	608:633	functional recombinant CR3	608:633	Spodoptera frugiperda (Sf9) cells have proved a suitable cell system in which to study this association and to produce recombinant CR3, and we show here that another lepidopteran cell line, Trichoplusia niTN-5B1-4 (High-Five) cells, allows the recovery of large amounts of functional recombinant CR3.
10677208	8	17	from	fibrillin-1	1461:1471	arg1	structure					1418:1426	the structure	1414:1426	the structure of an eight-cysteine domain from fibrillin-1	1414:1471	On the basis of these results and on the structure of an eight-cysteine domain from fibrillin-1, we present a model of glycosylated CR3 and discuss the role of glycosylation in eight-cysteine domain protein-protein interactions.
10677208	8	17	from	fibrillin-1	1461:1471	arg1	domain					1449:1454	an eight-cysteine domain	1431:1454	an eight-cysteine domain from fibrillin-1	1431:1471	On the basis of these results and on the structure of an eight-cysteine domain from fibrillin-1, we present a model of glycosylated CR3 and discuss the role of glycosylation in eight-cysteine domain protein-protein interactions.
10677208	4	18	theme	N-glycosylation	765:779	arg1	status					750:755	the status	746:755	the status of this N-glycosylation	746:779	When we examined the status of this N-glycosylation using MALDI-TOF mass spectrometry and enzymatic analysis, we found that CR3 is one of the rare recombinant peptides modified with complex glycans in insect cells.
10677208	2	19	theme	amounts	597:603	arg1	recovery					579:586	the recovery	575:586	the recovery of large amounts of functional recombinant CR3	575:633	Spodoptera frugiperda (Sf9) cells have proved a suitable cell system in which to study this association and to produce recombinant CR3, and we show here that another lepidopteran cell line, Trichoplusia niTN-5B1-4 (High-Five) cells, allows the recovery of large amounts of functional recombinant CR3.
10677208	3	20	contain	contains	640:647	arg1	CR3					636:638	CR3	636:638	CR3	636:638	CR3 contains an N-glycosylation site, which is conserved in all forms of LTBP known to date.
10677208	3	20	contain	contains	640:647	arg2	site					668:671	an N-glycosylation site	649:671	an N-glycosylation site	649:671	CR3 contains an N-glycosylation site, which is conserved in all forms of LTBP known to date.
10677208	0	21	theme	conserved	45:53	arg1	site					71:74	the conserved N-glycosylation site	41:74	the conserved N-glycosylation site of the third eight-cysteine domain of LTBP-1 in insect cells	41:135	Hybrid and complex glycans are linked to the conserved N-glycosylation site of the third eight-cysteine domain of LTBP-1 in insect cells.
10677208	0	21	theme	conserved	45:53	arg1	domain					104:109	the third eight-cysteine domain	79:109	the third eight-cysteine domain of LTBP-1 in insect cells	79:135	Hybrid and complex glycans are linked to the conserved N-glycosylation site of the third eight-cysteine domain of LTBP-1 in insect cells.
10677208	5	22	theme	GlcNAc	1014:1019	arg1	Fucose					1036:1041	the fucosylated paucomannosidic structure (GlcNAc)(2)(Mannose)(3)Fucose	971:1041	the fucosylated paucomannosidic structure (GlcNAc)(2)(Mannose)(3)Fucose	971:1041	Sf9 cells mainly processed the fucosylated paucomannosidic structure (GlcNAc)(2)(Mannose)(3)Fucose, although hybrid and complex N-glycosylations were also detected.
10677208	1	23	dep	referred	270:277	arg1	also					265:268	also	265:268	also	265:268	Covalent association of LTBP-1 (latent TGF-beta binding protein-1) to latent TGF-beta is mediated by the third eight-cysteine (also referred to as TB) module of LTBP-1, a domain designated as CR3.
10677208	2	24	theme	CR3	631:633	arg1	amounts					597:603	large amounts	591:603	large amounts of functional recombinant CR3	591:633	Spodoptera frugiperda (Sf9) cells have proved a suitable cell system in which to study this association and to produce recombinant CR3, and we show here that another lepidopteran cell line, Trichoplusia niTN-5B1-4 (High-Five) cells, allows the recovery of large amounts of functional recombinant CR3.
10677208	2	24	theme	CR3	631:633	arg1	CR3					631:633	functional recombinant CR3	608:633	functional recombinant CR3	608:633	Spodoptera frugiperda (Sf9) cells have proved a suitable cell system in which to study this association and to produce recombinant CR3, and we show here that another lepidopteran cell line, Trichoplusia niTN-5B1-4 (High-Five) cells, allows the recovery of large amounts of functional recombinant CR3.
10677208	6	25	theme	complex	1200:1206	arg1	sugars					1208:1213	hybrid and complex sugars	1189:1213	sugars	1208:1213	In High-Five cells, the peptide was found to be modified with a wide variety of hybrid and complex sugars in addition to paucomanosidic oligosaccharides.
10677208	1	26	theme	LTBP-1	299:304	arg1	module					289:294	the third eight-cysteine (also referred to as TB) module	239:294	the third eight-cysteine (also referred to as TB) module of LTBP-1, a domain designated as CR3	239:332	Covalent association of LTBP-1 (latent TGF-beta binding protein-1) to latent TGF-beta is mediated by the third eight-cysteine (also referred to as TB) module of LTBP-1, a domain designated as CR3.
10677208	2	27	theme	recombinant	454:464	arg1	CR3					466:468	recombinant CR3	454:468	recombinant CR3	454:468	Spodoptera frugiperda (Sf9) cells have proved a suitable cell system in which to study this association and to produce recombinant CR3, and we show here that another lepidopteran cell line, Trichoplusia niTN-5B1-4 (High-Five) cells, allows the recovery of large amounts of functional recombinant CR3.
10677208	6	28	theme	hybrid	1189:1194	arg1	sugars					1208:1213	hybrid and complex sugars	1189:1213	sugars	1208:1213	In High-Five cells, the peptide was found to be modified with a wide variety of hybrid and complex sugars in addition to paucomanosidic oligosaccharides.
10677208	5	29	theme	fucosylated	975:985	arg1	Fucose					1036:1041	the fucosylated paucomannosidic structure (GlcNAc)(2)(Mannose)(3)Fucose	971:1041	the fucosylated paucomannosidic structure (GlcNAc)(2)(Mannose)(3)Fucose	971:1041	Sf9 cells mainly processed the fucosylated paucomannosidic structure (GlcNAc)(2)(Mannose)(3)Fucose, although hybrid and complex N-glycosylations were also detected.
10677208	0	30	gly	N-glycosylation	55:69	arg2	domain					104:109	the third eight-cysteine domain	79:109	the third eight-cysteine domain of LTBP-1 in insect cells	79:135	Hybrid and complex glycans are linked to the conserved N-glycosylation site of the third eight-cysteine domain of LTBP-1 in insect cells.
10677208	0	30	gly	N-glycosylation	55:69	arg1	domain					104:109	the third eight-cysteine domain	79:109	the third eight-cysteine domain of LTBP-1 in insect cells	79:135	Hybrid and complex glycans are linked to the conserved N-glycosylation site of the third eight-cysteine domain of LTBP-1 in insect cells.
10677208	0	30	gly	N-glycosylation	55:69	arg2	cells					131:135	insect cells	124:135	insect cells	124:135	Hybrid and complex glycans are linked to the conserved N-glycosylation site of the third eight-cysteine domain of LTBP-1 in insect cells.
10677208	0	30	gly	N-glycosylation	55:69	arg1	LTBP-1					114:119	LTBP-1	114:119	LTBP-1	114:119	Hybrid and complex glycans are linked to the conserved N-glycosylation site of the third eight-cysteine domain of LTBP-1 in insect cells.
10677208	0	30	gly	N-glycosylation	55:69	arg2	site					71:74	the conserved N-glycosylation site	41:74	the conserved N-glycosylation site of the third eight-cysteine domain of LTBP-1 in insect cells	41:135	Hybrid and complex glycans are linked to the conserved N-glycosylation site of the third eight-cysteine domain of LTBP-1 in insect cells.
10677208	2	31	theme	frugiperda	346:355	arg1	cells					363:367	Spodoptera frugiperda (Sf9) cells	335:367	Spodoptera frugiperda (Sf9) cells	335:367	Spodoptera frugiperda (Sf9) cells have proved a suitable cell system in which to study this association and to produce recombinant CR3, and we show here that another lepidopteran cell line, Trichoplusia niTN-5B1-4 (High-Five) cells, allows the recovery of large amounts of functional recombinant CR3.
10677208	0	32	theme	eight-cysteine	89:102	arg1	LTBP-1					114:119	LTBP-1	114:119	LTBP-1	114:119	Hybrid and complex glycans are linked to the conserved N-glycosylation site of the third eight-cysteine domain of LTBP-1 in insect cells.
10677208	0	32	theme	eight-cysteine	89:102	arg1	domain					104:109	the third eight-cysteine domain	79:109	the third eight-cysteine domain of LTBP-1 in insect cells	79:135	Hybrid and complex glycans are linked to the conserved N-glycosylation site of the third eight-cysteine domain of LTBP-1 in insect cells.
10677208	5	33	theme	structure	1003:1011	arg1	Fucose					1036:1041	the fucosylated paucomannosidic structure (GlcNAc)(2)(Mannose)(3)Fucose	971:1041	the fucosylated paucomannosidic structure (GlcNAc)(2)(Mannose)(3)Fucose	971:1041	Sf9 cells mainly processed the fucosylated paucomannosidic structure (GlcNAc)(2)(Mannose)(3)Fucose, although hybrid and complex N-glycosylations were also detected.
10677208	2	34	theme	suitable	383:390	arg1	system					397:402	a suitable cell system	381:402	a suitable cell system in which to study this association and to produce recombinant CR3	381:468	Spodoptera frugiperda (Sf9) cells have proved a suitable cell system in which to study this association and to produce recombinant CR3, and we show here that another lepidopteran cell line, Trichoplusia niTN-5B1-4 (High-Five) cells, allows the recovery of large amounts of functional recombinant CR3.
10677208	0	35	theme	Hybrid	0:5	arg1	glycans					19:25	Hybrid and complex glycans	0:25	glycans	19:25	Hybrid and complex glycans are linked to the conserved N-glycosylation site of the third eight-cysteine domain of LTBP-1 in insect cells.
10677208	1	36	theme	eight-cysteine	249:262	arg1	module					289:294	the third eight-cysteine (also referred to as TB) module	239:294	the third eight-cysteine (also referred to as TB) module of LTBP-1, a domain designated as CR3	239:332	Covalent association of LTBP-1 (latent TGF-beta binding protein-1) to latent TGF-beta is mediated by the third eight-cysteine (also referred to as TB) module of LTBP-1, a domain designated as CR3.
10677208	0	37	theme	complex	11:17	arg1	glycans					19:25	Hybrid and complex glycans	0:25	glycans	19:25	Hybrid and complex glycans are linked to the conserved N-glycosylation site of the third eight-cysteine domain of LTBP-1 in insect cells.
10677208	4	38	theme	recombinant	876:886	arg1	peptides					888:895	the rare recombinant peptides	867:895	the rare recombinant peptides modified with complex glycans in insect cells	867:941	When we examined the status of this N-glycosylation using MALDI-TOF mass spectrometry and enzymatic analysis, we found that CR3 is one of the rare recombinant peptides modified with complex glycans in insect cells.
10677208	7	39	theme	innermost	1359:1367	arg1	GlcNAc					1369:1374	the innermost GlcNAc	1355:1374	the innermost GlcNAc	1355:1374	Most glycans had one or two fucose residues bound through alpha1,3 and alpha1,6 linkages to the innermost GlcNAc.
10677208	8	40	theme	results	1399:1405	arg1	basis					1384:1388	the basis	1380:1388	the basis of these results	1380:1405	On the basis of these results and on the structure of an eight-cysteine domain from fibrillin-1, we present a model of glycosylated CR3 and discuss the role of glycosylation in eight-cysteine domain protein-protein interactions.
10677208	5	41	theme	Mannose	1025:1031	arg1	Fucose					1036:1041	the fucosylated paucomannosidic structure (GlcNAc)(2)(Mannose)(3)Fucose	971:1041	the fucosylated paucomannosidic structure (GlcNAc)(2)(Mannose)(3)Fucose	971:1041	Sf9 cells mainly processed the fucosylated paucomannosidic structure (GlcNAc)(2)(Mannose)(3)Fucose, although hybrid and complex N-glycosylations were also detected.
10677208	5	42	theme	complex	1064:1070	arg1	N-glycosylations					1072:1087	complex N-glycosylations	1064:1087	complex N-glycosylations	1064:1087	Sf9 cells mainly processed the fucosylated paucomannosidic structure (GlcNAc)(2)(Mannose)(3)Fucose, although hybrid and complex N-glycosylations were also detected.
10677208	7	43	theme	alpha1,6	1334:1341	arg1	linkages					1343:1350	alpha1,6 linkages	1334:1350	alpha1,6 linkages	1334:1350	Most glycans had one or two fucose residues bound through alpha1,3 and alpha1,6 linkages to the innermost GlcNAc.
10677208	6	44	mod	modified	1157:1164	arg3	variety					1178:1184	a wide variety	1171:1184	a wide variety of hybrid and complex sugars in addition to paucomanosidic oligosaccharides	1171:1260	In High-Five cells, the peptide was found to be modified with a wide variety of hybrid and complex sugars in addition to paucomanosidic oligosaccharides.
10677208	6	44	mod	modified	1157:1164	arg3	sugars					1208:1213	hybrid and complex sugars	1189:1213	sugars	1208:1213	In High-Five cells, the peptide was found to be modified with a wide variety of hybrid and complex sugars in addition to paucomanosidic oligosaccharides.
10677208	6	44	mod	modified	1157:1164	arg1	peptide					1133:1139	the peptide	1129:1139	the peptide	1129:1139	In High-Five cells, the peptide was found to be modified with a wide variety of hybrid and complex sugars in addition to paucomanosidic oligosaccharides.
10677208	5	45	dep	Fucose	1036:1041	arg1	3					1034:1034	3	1034:1034	3	1034:1034	Sf9 cells mainly processed the fucosylated paucomannosidic structure (GlcNAc)(2)(Mannose)(3)Fucose, although hybrid and complex N-glycosylations were also detected.
10677208	8	46	theme	domain	1449:1454	arg1	structure					1418:1426	the structure	1414:1426	the structure of an eight-cysteine domain from fibrillin-1	1414:1471	On the basis of these results and on the structure of an eight-cysteine domain from fibrillin-1, we present a model of glycosylated CR3 and discuss the role of glycosylation in eight-cysteine domain protein-protein interactions.
10677208	8	47	theme	CR3	1509:1511	arg1	model					1487:1491	a model	1485:1491	a model of glycosylated CR3	1485:1511	On the basis of these results and on the structure of an eight-cysteine domain from fibrillin-1, we present a model of glycosylated CR3 and discuss the role of glycosylation in eight-cysteine domain protein-protein interactions.
10677208	7	48	theme	fucose	1291:1296	arg1	residues					1298:1305	one or two fucose residues	1280:1305	one or two fucose residues	1280:1305	Most glycans had one or two fucose residues bound through alpha1,3 and alpha1,6 linkages to the innermost GlcNAc.
10677208	2	49	theme	lepidopteran	501:512	arg1	line					519:522	another lepidopteran cell line	493:522	another lepidopteran cell line	493:522	Spodoptera frugiperda (Sf9) cells have proved a suitable cell system in which to study this association and to produce recombinant CR3, and we show here that another lepidopteran cell line, Trichoplusia niTN-5B1-4 (High-Five) cells, allows the recovery of large amounts of functional recombinant CR3.
10677208	2	49	theme	lepidopteran	501:512	arg1	cells					561:565	Trichoplusia niTN-5B1-4 (High-Five) cells	525:565	Trichoplusia niTN-5B1-4 (High-Five) cells	525:565	Spodoptera frugiperda (Sf9) cells have proved a suitable cell system in which to study this association and to produce recombinant CR3, and we show here that another lepidopteran cell line, Trichoplusia niTN-5B1-4 (High-Five) cells, allows the recovery of large amounts of functional recombinant CR3.
10677208	0	50	from	cells	131:135	arg1	site					71:74	the conserved N-glycosylation site	41:74	the conserved N-glycosylation site of the third eight-cysteine domain of LTBP-1 in insect cells	41:135	Hybrid and complex glycans are linked to the conserved N-glycosylation site of the third eight-cysteine domain of LTBP-1 in insect cells.
10677208	0	50	from	cells	131:135	arg1	domain					104:109	the third eight-cysteine domain	79:109	the third eight-cysteine domain of LTBP-1 in insect cells	79:135	Hybrid and complex glycans are linked to the conserved N-glycosylation site of the third eight-cysteine domain of LTBP-1 in insect cells.
10677208	6	51	theme	High-Five	1112:1120	arg1	cells					1122:1126	High-Five cells	1112:1126	High-Five cells	1112:1126	In High-Five cells, the peptide was found to be modified with a wide variety of hybrid and complex sugars in addition to paucomanosidic oligosaccharides.
10677208	2	52	theme	cell	392:395	arg1	system					397:402	a suitable cell system	381:402	a suitable cell system in which to study this association and to produce recombinant CR3	381:468	Spodoptera frugiperda (Sf9) cells have proved a suitable cell system in which to study this association and to produce recombinant CR3, and we show here that another lepidopteran cell line, Trichoplusia niTN-5B1-4 (High-Five) cells, allows the recovery of large amounts of functional recombinant CR3.
10677208	8	53	gly	glycosylated	1496:1507	arg1	CR3					1509:1511	glycosylated CR3	1496:1511	glycosylated CR3	1496:1511	On the basis of these results and on the structure of an eight-cysteine domain from fibrillin-1, we present a model of glycosylated CR3 and discuss the role of glycosylation in eight-cysteine domain protein-protein interactions.
10677208	2	54	theme	Trichoplusia	525:536	arg1	line					519:522	another lepidopteran cell line	493:522	another lepidopteran cell line	493:522	Spodoptera frugiperda (Sf9) cells have proved a suitable cell system in which to study this association and to produce recombinant CR3, and we show here that another lepidopteran cell line, Trichoplusia niTN-5B1-4 (High-Five) cells, allows the recovery of large amounts of functional recombinant CR3.
10677208	2	54	theme	Trichoplusia	525:536	arg1	cells					561:565	Trichoplusia niTN-5B1-4 (High-Five) cells	525:565	Trichoplusia niTN-5B1-4 (High-Five) cells	525:565	Spodoptera frugiperda (Sf9) cells have proved a suitable cell system in which to study this association and to produce recombinant CR3, and we show here that another lepidopteran cell line, Trichoplusia niTN-5B1-4 (High-Five) cells, allows the recovery of large amounts of functional recombinant CR3.
10677208	6	55	theme	wide	1173:1176	arg1	sugars					1208:1213	hybrid and complex sugars	1189:1213	sugars	1208:1213	In High-Five cells, the peptide was found to be modified with a wide variety of hybrid and complex sugars in addition to paucomanosidic oligosaccharides.
10677208	6	55	theme	wide	1173:1176	arg1	variety					1178:1184	a wide variety	1171:1184	a wide variety of hybrid and complex sugars in addition to paucomanosidic oligosaccharides	1171:1260	In High-Five cells, the peptide was found to be modified with a wide variety of hybrid and complex sugars in addition to paucomanosidic oligosaccharides.
10677208	8	56	theme	glycosylation	1537:1549	arg1	role					1529:1532	the role	1525:1532	the role of glycosylation in eight-cysteine domain protein-protein interactions	1525:1603	On the basis of these results and on the structure of an eight-cysteine domain from fibrillin-1, we present a model of glycosylated CR3 and discuss the role of glycosylation in eight-cysteine domain protein-protein interactions.
10677208	1	57	theme	TGF-beta	177:184	arg1	protein-1					194:202	latent TGF-beta binding protein-1	170:202	latent TGF-beta binding protein-1	170:202	Covalent association of LTBP-1 (latent TGF-beta binding protein-1) to latent TGF-beta is mediated by the third eight-cysteine (also referred to as TB) module of LTBP-1, a domain designated as CR3.
10677208	1	57	theme	TGF-beta	177:184	arg1	LTBP-1					162:167	LTBP-1	162:167	LTBP-1 (latent TGF-beta binding protein-1)	162:203	Covalent association of LTBP-1 (latent TGF-beta binding protein-1) to latent TGF-beta is mediated by the third eight-cysteine (also referred to as TB) module of LTBP-1, a domain designated as CR3.
10677208	3	58	theme	N-glycosylation	652:666	arg1	site					668:671	an N-glycosylation site	649:671	an N-glycosylation site	649:671	CR3 contains an N-glycosylation site, which is conserved in all forms of LTBP known to date.
10677208	0	59	theme	insect	124:129	arg1	cells					131:135	insect cells	124:135	insect cells	124:135	Hybrid and complex glycans are linked to the conserved N-glycosylation site of the third eight-cysteine domain of LTBP-1 in insect cells.
10677208	8	60	theme	eight-cysteine	1554:1567	arg1	interactions					1592:1603	eight-cysteine domain protein-protein interactions	1554:1603	eight-cysteine domain protein-protein interactions	1554:1603	On the basis of these results and on the structure of an eight-cysteine domain from fibrillin-1, we present a model of glycosylated CR3 and discuss the role of glycosylation in eight-cysteine domain protein-protein interactions.
10677208	2	61	theme	recombinant	619:629	arg1	CR3					631:633	functional recombinant CR3	608:633	functional recombinant CR3	608:633	Spodoptera frugiperda (Sf9) cells have proved a suitable cell system in which to study this association and to produce recombinant CR3, and we show here that another lepidopteran cell line, Trichoplusia niTN-5B1-4 (High-Five) cells, allows the recovery of large amounts of functional recombinant CR3.
10677208	8	62	theme	protein-protein	1576:1590	arg1	interactions					1592:1603	eight-cysteine domain protein-protein interactions	1554:1603	eight-cysteine domain protein-protein interactions	1554:1603	On the basis of these results and on the structure of an eight-cysteine domain from fibrillin-1, we present a model of glycosylated CR3 and discuss the role of glycosylation in eight-cysteine domain protein-protein interactions.
10677208	0	63	theme	LTBP-1	114:119	arg1	LTBP-1					114:119	LTBP-1	114:119	LTBP-1	114:119	Hybrid and complex glycans are linked to the conserved N-glycosylation site of the third eight-cysteine domain of LTBP-1 in insect cells.
10677208	0	63	theme	LTBP-1	114:119	arg1	domain					104:109	the third eight-cysteine domain	79:109	the third eight-cysteine domain of LTBP-1 in insect cells	79:135	Hybrid and complex glycans are linked to the conserved N-glycosylation site of the third eight-cysteine domain of LTBP-1 in insect cells.
10677208	0	64	from	domain	104:109	arg1	cells					131:135	insect cells	124:135	insect cells	124:135	Hybrid and complex glycans are linked to the conserved N-glycosylation site of the third eight-cysteine domain of LTBP-1 in insect cells.
10677208	4	65	theme	mass	797:800	arg1	spectrometry					802:813	MALDI-TOF mass spectrometry	787:813	MALDI-TOF mass spectrometry	787:813	When we examined the status of this N-glycosylation using MALDI-TOF mass spectrometry and enzymatic analysis, we found that CR3 is one of the rare recombinant peptides modified with complex glycans in insect cells.
10677208	3	66	theme	LTBP	709:712	arg1	forms					700:704	all forms	696:704	all forms of LTBP known to date	696:726	CR3 contains an N-glycosylation site, which is conserved in all forms of LTBP known to date.
10677208	0	67	theme	N-glycosylation	55:69	arg1	site					71:74	the conserved N-glycosylation site	41:74	the conserved N-glycosylation site of the third eight-cysteine domain of LTBP-1 in insect cells	41:135	Hybrid and complex glycans are linked to the conserved N-glycosylation site of the third eight-cysteine domain of LTBP-1 in insect cells.
10677208	0	67	theme	N-glycosylation	55:69	arg1	domain					104:109	the third eight-cysteine domain	79:109	the third eight-cysteine domain of LTBP-1 in insect cells	79:135	Hybrid and complex glycans are linked to the conserved N-glycosylation site of the third eight-cysteine domain of LTBP-1 in insect cells.
10677208	5	68	theme	Sf9	944:946	arg1	cells					948:952	Sf9 cells	944:952	Sf9 cells	944:952	Sf9 cells mainly processed the fucosylated paucomannosidic structure (GlcNAc)(2)(Mannose)(3)Fucose, although hybrid and complex N-glycosylations were also detected.
10677208	6	69	located	found	1145:1149	arg2	peptide					1133:1139	the peptide	1129:1139	the peptide	1129:1139	In High-Five cells, the peptide was found to be modified with a wide variety of hybrid and complex sugars in addition to paucomanosidic oligosaccharides.
10677208	6	69	located	found	1145:1149	arg1	cells					1122:1126	High-Five cells	1112:1126	High-Five cells	1112:1126	In High-Five cells, the peptide was found to be modified with a wide variety of hybrid and complex sugars in addition to paucomanosidic oligosaccharides.
10677208	6	70	theme	sugars	1208:1213	arg1	sugars					1208:1213	hybrid and complex sugars	1189:1213	sugars	1208:1213	In High-Five cells, the peptide was found to be modified with a wide variety of hybrid and complex sugars in addition to paucomanosidic oligosaccharides.
10677208	6	70	theme	sugars	1208:1213	arg1	variety					1178:1184	a wide variety	1171:1184	a wide variety of hybrid and complex sugars in addition to paucomanosidic oligosaccharides	1171:1260	In High-Five cells, the peptide was found to be modified with a wide variety of hybrid and complex sugars in addition to paucomanosidic oligosaccharides.
10677208	1	71	theme	Covalent	138:145	arg1	association					147:157	Covalent association	138:157	Covalent association of LTBP-1 (latent TGF-beta binding protein-1) to latent TGF-beta	138:222	Covalent association of LTBP-1 (latent TGF-beta binding protein-1) to latent TGF-beta is mediated by the third eight-cysteine (also referred to as TB) module of LTBP-1, a domain designated as CR3.
10677208	1	72	dep	eight-cysteine	249:262	arg1	referred					270:277	referred	270:277	referred to as TB	270:286	Covalent association of LTBP-1 (latent TGF-beta binding protein-1) to latent TGF-beta is mediated by the third eight-cysteine (also referred to as TB) module of LTBP-1, a domain designated as CR3.
10677208	0	73	theme	third	83:87	arg1	LTBP-1					114:119	LTBP-1	114:119	LTBP-1	114:119	Hybrid and complex glycans are linked to the conserved N-glycosylation site of the third eight-cysteine domain of LTBP-1 in insect cells.
10677208	0	73	theme	third	83:87	arg1	domain					104:109	the third eight-cysteine domain	79:109	the third eight-cysteine domain of LTBP-1 in insect cells	79:135	Hybrid and complex glycans are linked to the conserved N-glycosylation site of the third eight-cysteine domain of LTBP-1 in insect cells.
10677208	0	74	theme	domain	104:109	arg1	site					71:74	the conserved N-glycosylation site	41:74	the conserved N-glycosylation site of the third eight-cysteine domain of LTBP-1 in insect cells	41:135	Hybrid and complex glycans are linked to the conserved N-glycosylation site of the third eight-cysteine domain of LTBP-1 in insect cells.
10677208	0	74	theme	domain	104:109	arg1	domain					104:109	the third eight-cysteine domain	79:109	the third eight-cysteine domain of LTBP-1 in insect cells	79:135	Hybrid and complex glycans are linked to the conserved N-glycosylation site of the third eight-cysteine domain of LTBP-1 in insect cells.
10677208	5	75	theme	paucomannosidic	987:1001	arg1	Fucose					1036:1041	the fucosylated paucomannosidic structure (GlcNAc)(2)(Mannose)(3)Fucose	971:1041	the fucosylated paucomannosidic structure (GlcNAc)(2)(Mannose)(3)Fucose	971:1041	Sf9 cells mainly processed the fucosylated paucomannosidic structure (GlcNAc)(2)(Mannose)(3)Fucose, although hybrid and complex N-glycosylations were also detected.
10677208	3	76	gly	N-glycosylation	652:666	arg2	site					668:671	an N-glycosylation site	649:671	an N-glycosylation site	649:671	CR3 contains an N-glycosylation site, which is conserved in all forms of LTBP known to date.
10677208	2	77	theme	large	591:595	arg1	amounts					597:603	large amounts	591:603	large amounts of functional recombinant CR3	591:633	Spodoptera frugiperda (Sf9) cells have proved a suitable cell system in which to study this association and to produce recombinant CR3, and we show here that another lepidopteran cell line, Trichoplusia niTN-5B1-4 (High-Five) cells, allows the recovery of large amounts of functional recombinant CR3.
10677208	2	77	theme	large	591:595	arg1	CR3					631:633	functional recombinant CR3	608:633	functional recombinant CR3	608:633	Spodoptera frugiperda (Sf9) cells have proved a suitable cell system in which to study this association and to produce recombinant CR3, and we show here that another lepidopteran cell line, Trichoplusia niTN-5B1-4 (High-Five) cells, allows the recovery of large amounts of functional recombinant CR3.
10677208	2	78	theme	Spodoptera	335:344	arg1	Sf9					358:360	Sf9	358:360	Sf9	358:360	Spodoptera frugiperda (Sf9) cells have proved a suitable cell system in which to study this association and to produce recombinant CR3, and we show here that another lepidopteran cell line, Trichoplusia niTN-5B1-4 (High-Five) cells, allows the recovery of large amounts of functional recombinant CR3.
10677208	2	78	theme	Spodoptera	335:344	arg1	frugiperda					346:355	Spodoptera frugiperda	335:355	Spodoptera frugiperda (Sf9) cells	335:367	Spodoptera frugiperda (Sf9) cells have proved a suitable cell system in which to study this association and to produce recombinant CR3, and we show here that another lepidopteran cell line, Trichoplusia niTN-5B1-4 (High-Five) cells, allows the recovery of large amounts of functional recombinant CR3.
10677208	8	79	attach	present	1477:1483	arg2	we					1474:1475	we	1474:1475	we	1474:1475	On the basis of these results and on the structure of an eight-cysteine domain from fibrillin-1, we present a model of glycosylated CR3 and discuss the role of glycosylation in eight-cysteine domain protein-protein interactions.
10677208	8	79	attach	present	1477:1483	arg1	structure					1418:1426	the structure	1414:1426	the structure of an eight-cysteine domain from fibrillin-1	1414:1471	On the basis of these results and on the structure of an eight-cysteine domain from fibrillin-1, we present a model of glycosylated CR3 and discuss the role of glycosylation in eight-cysteine domain protein-protein interactions.
10677208	8	79	attach	present	1477:1483	arg1	basis					1384:1388	the basis	1380:1388	the basis of these results	1380:1405	On the basis of these results and on the structure of an eight-cysteine domain from fibrillin-1, we present a model of glycosylated CR3 and discuss the role of glycosylation in eight-cysteine domain protein-protein interactions.
10677208	4	80	from	glycans	919:925	arg1	cells					937:941	insect cells	930:941	insect cells	930:941	When we examined the status of this N-glycosylation using MALDI-TOF mass spectrometry and enzymatic analysis, we found that CR3 is one of the rare recombinant peptides modified with complex glycans in insect cells.
10677208	4	81	theme	rare	871:874	arg1	peptides					888:895	the rare recombinant peptides	867:895	the rare recombinant peptides modified with complex glycans in insect cells	867:941	When we examined the status of this N-glycosylation using MALDI-TOF mass spectrometry and enzymatic analysis, we found that CR3 is one of the rare recombinant peptides modified with complex glycans in insect cells.
10677208	8	82	from	role	1529:1532	arg1	interactions					1592:1603	eight-cysteine domain protein-protein interactions	1554:1603	eight-cysteine domain protein-protein interactions	1554:1603	On the basis of these results and on the structure of an eight-cysteine domain from fibrillin-1, we present a model of glycosylated CR3 and discuss the role of glycosylation in eight-cysteine domain protein-protein interactions.
10677208	6	83	theme	paucomanosidic	1230:1243	arg1	oligosaccharides					1245:1260	paucomanosidic oligosaccharides	1230:1260	paucomanosidic oligosaccharides	1230:1260	In High-Five cells, the peptide was found to be modified with a wide variety of hybrid and complex sugars in addition to paucomanosidic oligosaccharides.
10677208	4	84	theme	peptides	888:895	arg1	peptides					888:895	the rare recombinant peptides	867:895	the rare recombinant peptides modified with complex glycans in insect cells	867:941	When we examined the status of this N-glycosylation using MALDI-TOF mass spectrometry and enzymatic analysis, we found that CR3 is one of the rare recombinant peptides modified with complex glycans in insect cells.
10677208	4	84	theme	peptides	888:895	arg1	one					860:862	one	860:862	one	860:862	When we examined the status of this N-glycosylation using MALDI-TOF mass spectrometry and enzymatic analysis, we found that CR3 is one of the rare recombinant peptides modified with complex glycans in insect cells.
10677208	1	85	theme	latent	208:213	arg1	TGF-beta					215:222	latent TGF-beta	208:222	latent TGF-beta	208:222	Covalent association of LTBP-1 (latent TGF-beta binding protein-1) to latent TGF-beta is mediated by the third eight-cysteine (also referred to as TB) module of LTBP-1, a domain designated as CR3.
10677208	8	86	theme	eight-cysteine	1434:1447	arg1	domain					1449:1454	an eight-cysteine domain	1431:1454	an eight-cysteine domain from fibrillin-1	1431:1471	On the basis of these results and on the structure of an eight-cysteine domain from fibrillin-1, we present a model of glycosylated CR3 and discuss the role of glycosylation in eight-cysteine domain protein-protein interactions.
10677208	8	87	gly	glycosylation	1537:1549	arg1	eight-cysteine					1554:1567	eight-cysteine domain protein-protein interactions	1554:1603	eight-cysteine domain protein-protein interactions	1554:1603	On the basis of these results and on the structure of an eight-cysteine domain from fibrillin-1, we present a model of glycosylated CR3 and discuss the role of glycosylation in eight-cysteine domain protein-protein interactions.
10677208	8	87	gly	glycosylation	1537:1549	arg1	domain					1569:1574	eight-cysteine domain protein-protein interactions	1554:1603	eight-cysteine domain protein-protein interactions	1554:1603	On the basis of these results and on the structure of an eight-cysteine domain from fibrillin-1, we present a model of glycosylated CR3 and discuss the role of glycosylation in eight-cysteine domain protein-protein interactions.
10677208	4	88	theme	complex	911:917	arg1	glycans					919:925	complex glycans	911:925	complex glycans in insect cells	911:941	When we examined the status of this N-glycosylation using MALDI-TOF mass spectrometry and enzymatic analysis, we found that CR3 is one of the rare recombinant peptides modified with complex glycans in insect cells.
10677208	8	89	theme	glycosylated	1496:1507	arg1	CR3					1509:1511	glycosylated CR3	1496:1511	glycosylated CR3	1496:1511	On the basis of these results and on the structure of an eight-cysteine domain from fibrillin-1, we present a model of glycosylated CR3 and discuss the role of glycosylation in eight-cysteine domain protein-protein interactions.
21295698	3	0	theme	PRO	623:625	arg1	repeat					628:633	the HCF-1(PRO) repeat	613:633	the HCF-1(PRO) repeat	613:633	We show here that the HCF-1(PRO) repeat is recognized by O-linked β-N-acetylglucosamine transferase (OGT), which both O-GlcNAcylates the HCF-1(N) subunit and directly cleaves the HCF-1(PRO) repeat.
21295698	4	1	theme	repeats	666:672	arg1	Replacement					636:646	Replacement	636:646	Replacement of the HCF-1(PRO) repeats by a heterologous proteolytic cleavage signal	636:718	Replacement of the HCF-1(PRO) repeats by a heterologous proteolytic cleavage signal promotes HCF-1 proteolysis but fails to activate HCF-1(C)-subunit M phase functions.
21295698	1	2	theme	different	243:251	arg1	aspects					253:259	different aspects	243:259	different aspects of the cell cycle	243:277	The human epigenetic cell-cycle regulator HCF-1 undergoes an unusual proteolytic maturation process resulting in stably associated HCF-1(N) and HCF-1(C) subunits that regulate different aspects of the cell cycle.
21295698	5	3	theme	HCF-1	975:979	arg1	regulation					992:1001	HCF-1 cell-cycle regulation	975:1001	HCF-1 cell-cycle regulation	975:1001	These results reveal an unexpected role of OGT in HCF-1 proteolytic maturation and an unforeseen nexus between OGT-directed O-GlcNAcylation and proteolytic maturation in HCF-1 cell-cycle regulation.
21295698	1	4	theme	associated	187:196	arg1	subunits					220:227	stably associated HCF-1(N) and HCF-1(C) subunits	180:227	stably associated HCF-1(N) and HCF-1(C) subunits that regulate different aspects of the cell cycle	180:277	The human epigenetic cell-cycle regulator HCF-1 undergoes an unusual proteolytic maturation process resulting in stably associated HCF-1(N) and HCF-1(C) subunits that regulate different aspects of the cell cycle.
21295698	5	5	theme	proteolytic	861:871	arg1	maturation					873:882	HCF-1 proteolytic maturation	855:882	HCF-1 proteolytic maturation	855:882	These results reveal an unexpected role of OGT in HCF-1 proteolytic maturation and an unforeseen nexus between OGT-directed O-GlcNAcylation and proteolytic maturation in HCF-1 cell-cycle regulation.
21295698	3	6	theme	HCF-1	617:621	arg1	repeat					628:633	the HCF-1(PRO) repeat	613:633	the HCF-1(PRO) repeat	613:633	We show here that the HCF-1(PRO) repeat is recognized by O-linked β-N-acetylglucosamine transferase (OGT), which both O-GlcNAcylates the HCF-1(N) subunit and directly cleaves the HCF-1(PRO) repeat.
21295698	5	7	theme	OGT	848:850	arg1	role					840:843	an unexpected role	826:843	an unexpected role of OGT in HCF-1 proteolytic maturation	826:882	These results reveal an unexpected role of OGT in HCF-1 proteolytic maturation and an unforeseen nexus between OGT-directed O-GlcNAcylation and proteolytic maturation in HCF-1 cell-cycle regulation.
21295698	5	7	theme	OGT	848:850	arg1	nexus					902:906	an unforeseen nexus	888:906	an unforeseen nexus between OGT-directed O-GlcNAcylation and proteolytic maturation in HCF-1 cell-cycle regulation	888:1001	These results reveal an unexpected role of OGT in HCF-1 proteolytic maturation and an unforeseen nexus between OGT-directed O-GlcNAcylation and proteolytic maturation in HCF-1 cell-cycle regulation.
21295698	3	8	theme	O-linked	495:502	arg1	OGT					539:541	OGT	539:541	OGT	539:541	We show here that the HCF-1(PRO) repeat is recognized by O-linked β-N-acetylglucosamine transferase (OGT), which both O-GlcNAcylates the HCF-1(N) subunit and directly cleaves the HCF-1(PRO) repeat.
21295698	3	8	theme	O-linked	495:502	arg1	transferase					526:536	O-linked β-N-acetylglucosamine transferase	495:536	O-linked β-N-acetylglucosamine transferase (OGT)	495:542	We show here that the HCF-1(PRO) repeat is recognized by O-linked β-N-acetylglucosamine transferase (OGT), which both O-GlcNAcylates the HCF-1(N) subunit and directly cleaves the HCF-1(PRO) repeat.
21295698	3	9	theme	β-N-acetylglucosamine	504:524	arg1	OGT					539:541	OGT	539:541	OGT	539:541	We show here that the HCF-1(PRO) repeat is recognized by O-linked β-N-acetylglucosamine transferase (OGT), which both O-GlcNAcylates the HCF-1(N) subunit and directly cleaves the HCF-1(PRO) repeat.
21295698	3	9	theme	β-N-acetylglucosamine	504:524	arg1	transferase					526:536	O-linked β-N-acetylglucosamine transferase	495:536	O-linked β-N-acetylglucosamine transferase (OGT)	495:542	We show here that the HCF-1(PRO) repeat is recognized by O-linked β-N-acetylglucosamine transferase (OGT), which both O-GlcNAcylates the HCF-1(N) subunit and directly cleaves the HCF-1(PRO) repeat.
21295698	1	10	theme	human	71:75	arg1	HCF-1					109:113	The human epigenetic cell-cycle regulator HCF-1	67:113	The human epigenetic cell-cycle regulator HCF-1	67:113	The human epigenetic cell-cycle regulator HCF-1 undergoes an unusual proteolytic maturation process resulting in stably associated HCF-1(N) and HCF-1(C) subunits that regulate different aspects of the cell cycle.
21295698	0	11	theme	O-GlcNAc	0:7	arg1	transferase					9:19	O-GlcNAc transferase	0:19	O-GlcNAc transferase	0:19	O-GlcNAc transferase catalyzes site-specific proteolysis of HCF-1.
21295698	1	12	theme	epigenetic	77:86	arg1	HCF-1					109:113	The human epigenetic cell-cycle regulator HCF-1	67:113	The human epigenetic cell-cycle regulator HCF-1	67:113	The human epigenetic cell-cycle regulator HCF-1 undergoes an unusual proteolytic maturation process resulting in stably associated HCF-1(N) and HCF-1(C) subunits that regulate different aspects of the cell cycle.
21295698	1	13	theme	HCF-1	198:202	arg1	subunits					220:227	stably associated HCF-1(N) and HCF-1(C) subunits	180:227	stably associated HCF-1(N) and HCF-1(C) subunits that regulate different aspects of the cell cycle	180:277	The human epigenetic cell-cycle regulator HCF-1 undergoes an unusual proteolytic maturation process resulting in stably associated HCF-1(N) and HCF-1(C) subunits that regulate different aspects of the cell cycle.
21295698	0	14	theme	HCF-1	60:64	arg1	proteolysis					45:55	site-specific proteolysis	31:55	site-specific proteolysis of HCF-1	31:64	O-GlcNAc transferase catalyzes site-specific proteolysis of HCF-1.
21295698	1	15	theme	cell-cycle	88:97	arg1	HCF-1					109:113	The human epigenetic cell-cycle regulator HCF-1	67:113	The human epigenetic cell-cycle regulator HCF-1	67:113	The human epigenetic cell-cycle regulator HCF-1 undergoes an unusual proteolytic maturation process resulting in stably associated HCF-1(N) and HCF-1(C) subunits that regulate different aspects of the cell cycle.
21295698	1	16	theme	regulator	99:107	arg1	HCF-1					109:113	The human epigenetic cell-cycle regulator HCF-1	67:113	The human epigenetic cell-cycle regulator HCF-1	67:113	The human epigenetic cell-cycle regulator HCF-1 undergoes an unusual proteolytic maturation process resulting in stably associated HCF-1(N) and HCF-1(C) subunits that regulate different aspects of the cell cycle.
21295698	2	17	theme	functions	404:412	arg1	activation					373:382	activation	373:382	activation of HCF-1(C)-subunit functions in M phase progression	373:435	Proteolysis occurs at six centrally located HCF-1(PRO)-repeat sequences and is important for activation of HCF-1(C)-subunit functions in M phase progression.
21295698	1	18	theme	cell	268:271	arg1	cycle					273:277	the cell cycle	264:277	the cell cycle	264:277	The human epigenetic cell-cycle regulator HCF-1 undergoes an unusual proteolytic maturation process resulting in stably associated HCF-1(N) and HCF-1(C) subunits that regulate different aspects of the cell cycle.
21295698	2	19	dep	located	316:322	arg1	-repeat					334:340	-repeat	334:340	-repeat	334:340	Proteolysis occurs at six centrally located HCF-1(PRO)-repeat sequences and is important for activation of HCF-1(C)-subunit functions in M phase progression.
21295698	2	20	theme	-subunit	395:402	arg1	functions					404:412	HCF-1(C)-subunit functions	387:412	HCF-1(C)-subunit functions	387:412	Proteolysis occurs at six centrally located HCF-1(PRO)-repeat sequences and is important for activation of HCF-1(C)-subunit functions in M phase progression.
21295698	1	21	theme	cycle	273:277	arg1	aspects					253:259	different aspects	243:259	different aspects of the cell cycle	243:277	The human epigenetic cell-cycle regulator HCF-1 undergoes an unusual proteolytic maturation process resulting in stably associated HCF-1(N) and HCF-1(C) subunits that regulate different aspects of the cell cycle.
21295698	5	22	theme	unexpected	829:838	arg1	role					840:843	an unexpected role	826:843	an unexpected role of OGT in HCF-1 proteolytic maturation	826:882	These results reveal an unexpected role of OGT in HCF-1 proteolytic maturation and an unforeseen nexus between OGT-directed O-GlcNAcylation and proteolytic maturation in HCF-1 cell-cycle regulation.
21295698	5	23	theme	HCF-1	855:859	arg1	maturation					873:882	HCF-1 proteolytic maturation	855:882	HCF-1 proteolytic maturation	855:882	These results reveal an unexpected role of OGT in HCF-1 proteolytic maturation and an unforeseen nexus between OGT-directed O-GlcNAcylation and proteolytic maturation in HCF-1 cell-cycle regulation.
21295698	3	24	theme	N	581:581	arg1	subunit					584:590	the HCF-1(N) subunit	571:590	the HCF-1(N) subunit	571:590	We show here that the HCF-1(PRO) repeat is recognized by O-linked β-N-acetylglucosamine transferase (OGT), which both O-GlcNAcylates the HCF-1(N) subunit and directly cleaves the HCF-1(PRO) repeat.
21295698	3	25	theme	HCF-1	460:464	arg1	repeat					471:476	the HCF-1(PRO) repeat	456:476	the HCF-1(PRO) repeat	456:476	We show here that the HCF-1(PRO) repeat is recognized by O-linked β-N-acetylglucosamine transferase (OGT), which both O-GlcNAcylates the HCF-1(N) subunit and directly cleaves the HCF-1(PRO) repeat.
21295698	5	26	from	nexus	902:906	arg1	maturation					873:882	HCF-1 proteolytic maturation	855:882	HCF-1 proteolytic maturation	855:882	These results reveal an unexpected role of OGT in HCF-1 proteolytic maturation and an unforeseen nexus between OGT-directed O-GlcNAcylation and proteolytic maturation in HCF-1 cell-cycle regulation.
21295698	5	26	from	nexus	902:906	arg1	regulation					992:1001	HCF-1 cell-cycle regulation	975:1001	HCF-1 cell-cycle regulation	975:1001	These results reveal an unexpected role of OGT in HCF-1 proteolytic maturation and an unforeseen nexus between OGT-directed O-GlcNAcylation and proteolytic maturation in HCF-1 cell-cycle regulation.
21295698	1	27	theme	HCF-1	211:215	arg1	subunits					220:227	stably associated HCF-1(N) and HCF-1(C) subunits	180:227	stably associated HCF-1(N) and HCF-1(C) subunits that regulate different aspects of the cell cycle	180:277	The human epigenetic cell-cycle regulator HCF-1 undergoes an unusual proteolytic maturation process resulting in stably associated HCF-1(N) and HCF-1(C) subunits that regulate different aspects of the cell cycle.
21295698	5	28	theme	cell-cycle	981:990	arg1	regulation					992:1001	HCF-1 cell-cycle regulation	975:1001	HCF-1 cell-cycle regulation	975:1001	These results reveal an unexpected role of OGT in HCF-1 proteolytic maturation and an unforeseen nexus between OGT-directed O-GlcNAcylation and proteolytic maturation in HCF-1 cell-cycle regulation.
21295698	3	29	theme	HCF-1	575:579	arg1	subunit					584:590	the HCF-1(N) subunit	571:590	the HCF-1(N) subunit	571:590	We show here that the HCF-1(PRO) repeat is recognized by O-linked β-N-acetylglucosamine transferase (OGT), which both O-GlcNAcylates the HCF-1(N) subunit and directly cleaves the HCF-1(PRO) repeat.
21295698	0	30	theme	site-specific	31:43	arg1	proteolysis					45:55	site-specific proteolysis	31:55	site-specific proteolysis of HCF-1	31:64	O-GlcNAc transferase catalyzes site-specific proteolysis of HCF-1.
21295698	2	31	theme	phase	419:423	arg1	progression					425:435	M phase progression	417:435	M phase progression	417:435	Proteolysis occurs at six centrally located HCF-1(PRO)-repeat sequences and is important for activation of HCF-1(C)-subunit functions in M phase progression.
21295698	4	32	theme	M	786:786	arg1	functions					794:802	HCF-1(C)-subunit M phase functions	769:802	HCF-1(C)-subunit M phase functions	769:802	Replacement of the HCF-1(PRO) repeats by a heterologous proteolytic cleavage signal promotes HCF-1 proteolysis but fails to activate HCF-1(C)-subunit M phase functions.
21295698	4	33	theme	PRO	661:663	arg1	repeats					666:672	the HCF-1(PRO) repeats	651:672	the HCF-1(PRO) repeats	651:672	Replacement of the HCF-1(PRO) repeats by a heterologous proteolytic cleavage signal promotes HCF-1 proteolysis but fails to activate HCF-1(C)-subunit M phase functions.
21295698	5	34	theme	OGT-directed	916:927	arg1	O-GlcNAcylation					929:943	OGT-directed O-GlcNAcylation	916:943	OGT-directed O-GlcNAcylation	916:943	These results reveal an unexpected role of OGT in HCF-1 proteolytic maturation and an unforeseen nexus between OGT-directed O-GlcNAcylation and proteolytic maturation in HCF-1 cell-cycle regulation.
21295698	1	35	theme	unusual	128:134	arg1	process					159:165	an unusual proteolytic maturation process	125:165	an unusual proteolytic maturation process resulting in stably associated HCF-1(N) and HCF-1(C) subunits that regulate different aspects of the cell cycle	125:277	The human epigenetic cell-cycle regulator HCF-1 undergoes an unusual proteolytic maturation process resulting in stably associated HCF-1(N) and HCF-1(C) subunits that regulate different aspects of the cell cycle.
21295698	2	36	theme	M	417:417	arg1	progression					425:435	M phase progression	417:435	M phase progression	417:435	Proteolysis occurs at six centrally located HCF-1(PRO)-repeat sequences and is important for activation of HCF-1(C)-subunit functions in M phase progression.
21295698	4	37	theme	-subunit	777:784	arg1	functions					794:802	HCF-1(C)-subunit M phase functions	769:802	HCF-1(C)-subunit M phase functions	769:802	Replacement of the HCF-1(PRO) repeats by a heterologous proteolytic cleavage signal promotes HCF-1 proteolysis but fails to activate HCF-1(C)-subunit M phase functions.
21295698	4	38	theme	HCF-1	729:733	arg1	proteolysis					735:745	HCF-1 proteolysis	729:745	HCF-1 proteolysis	729:745	Replacement of the HCF-1(PRO) repeats by a heterologous proteolytic cleavage signal promotes HCF-1 proteolysis but fails to activate HCF-1(C)-subunit M phase functions.
21295698	2	39	from	activation	373:382	arg1	progression					425:435	M phase progression	417:435	M phase progression	417:435	Proteolysis occurs at six centrally located HCF-1(PRO)-repeat sequences and is important for activation of HCF-1(C)-subunit functions in M phase progression.
21295698	1	40	theme	proteolytic	136:146	arg1	process					159:165	an unusual proteolytic maturation process	125:165	an unusual proteolytic maturation process resulting in stably associated HCF-1(N) and HCF-1(C) subunits that regulate different aspects of the cell cycle	125:277	The human epigenetic cell-cycle regulator HCF-1 undergoes an unusual proteolytic maturation process resulting in stably associated HCF-1(N) and HCF-1(C) subunits that regulate different aspects of the cell cycle.
21295698	5	41	from	role	840:843	arg1	maturation					873:882	HCF-1 proteolytic maturation	855:882	HCF-1 proteolytic maturation	855:882	These results reveal an unexpected role of OGT in HCF-1 proteolytic maturation and an unforeseen nexus between OGT-directed O-GlcNAcylation and proteolytic maturation in HCF-1 cell-cycle regulation.
21295698	5	41	from	role	840:843	arg1	regulation					992:1001	HCF-1 cell-cycle regulation	975:1001	HCF-1 cell-cycle regulation	975:1001	These results reveal an unexpected role of OGT in HCF-1 proteolytic maturation and an unforeseen nexus between OGT-directed O-GlcNAcylation and proteolytic maturation in HCF-1 cell-cycle regulation.
21295698	5	42	theme	unforeseen	891:900	arg1	nexus					902:906	an unforeseen nexus	888:906	an unforeseen nexus between OGT-directed O-GlcNAcylation and proteolytic maturation in HCF-1 cell-cycle regulation	888:1001	These results reveal an unexpected role of OGT in HCF-1 proteolytic maturation and an unforeseen nexus between OGT-directed O-GlcNAcylation and proteolytic maturation in HCF-1 cell-cycle regulation.
21295698	5	43	theme	proteolytic	949:959	arg1	maturation					961:970	proteolytic maturation	949:970	proteolytic maturation	949:970	These results reveal an unexpected role of OGT in HCF-1 proteolytic maturation and an unforeseen nexus between OGT-directed O-GlcNAcylation and proteolytic maturation in HCF-1 cell-cycle regulation.
21295698	4	44	theme	heterologous	679:690	arg1	signal					713:718	a heterologous proteolytic cleavage signal	677:718	a heterologous proteolytic cleavage signal	677:718	Replacement of the HCF-1(PRO) repeats by a heterologous proteolytic cleavage signal promotes HCF-1 proteolysis but fails to activate HCF-1(C)-subunit M phase functions.
21295698	1	45	theme	maturation	148:157	arg1	process					159:165	an unusual proteolytic maturation process	125:165	an unusual proteolytic maturation process resulting in stably associated HCF-1(N) and HCF-1(C) subunits that regulate different aspects of the cell cycle	125:277	The human epigenetic cell-cycle regulator HCF-1 undergoes an unusual proteolytic maturation process resulting in stably associated HCF-1(N) and HCF-1(C) subunits that regulate different aspects of the cell cycle.
21295698	4	46	theme	phase	788:792	arg1	functions					794:802	HCF-1(C)-subunit M phase functions	769:802	HCF-1(C)-subunit M phase functions	769:802	Replacement of the HCF-1(PRO) repeats by a heterologous proteolytic cleavage signal promotes HCF-1 proteolysis but fails to activate HCF-1(C)-subunit M phase functions.
21295698	4	47	theme	HCF-1	655:659	arg1	repeats					666:672	the HCF-1(PRO) repeats	651:672	the HCF-1(PRO) repeats	651:672	Replacement of the HCF-1(PRO) repeats by a heterologous proteolytic cleavage signal promotes HCF-1 proteolysis but fails to activate HCF-1(C)-subunit M phase functions.
21295698	2	48	theme	located	316:322	arg1	sequences					342:350	six centrally located HCF-1(PRO)-repeat sequences	302:350	six centrally located HCF-1(PRO)-repeat sequences	302:350	Proteolysis occurs at six centrally located HCF-1(PRO)-repeat sequences and is important for activation of HCF-1(C)-subunit functions in M phase progression.
21295698	4	49	theme	cleavage	704:711	arg1	signal					713:718	a heterologous proteolytic cleavage signal	677:718	a heterologous proteolytic cleavage signal	677:718	Replacement of the HCF-1(PRO) repeats by a heterologous proteolytic cleavage signal promotes HCF-1 proteolysis but fails to activate HCF-1(C)-subunit M phase functions.
21295698	3	50	link	O-linked	495:502	arg1	OGT					539:541	OGT	539:541	OGT	539:541	We show here that the HCF-1(PRO) repeat is recognized by O-linked β-N-acetylglucosamine transferase (OGT), which both O-GlcNAcylates the HCF-1(N) subunit and directly cleaves the HCF-1(PRO) repeat.
21295698	3	50	link	O-linked	495:502	arg1	transferase					526:536	O-linked β-N-acetylglucosamine transferase	495:536	O-linked β-N-acetylglucosamine transferase (OGT)	495:542	We show here that the HCF-1(PRO) repeat is recognized by O-linked β-N-acetylglucosamine transferase (OGT), which both O-GlcNAcylates the HCF-1(N) subunit and directly cleaves the HCF-1(PRO) repeat.
21295698	4	51	theme	proteolytic	692:702	arg1	signal					713:718	a heterologous proteolytic cleavage signal	677:718	a heterologous proteolytic cleavage signal	677:718	Replacement of the HCF-1(PRO) repeats by a heterologous proteolytic cleavage signal promotes HCF-1 proteolysis but fails to activate HCF-1(C)-subunit M phase functions.
21295698	3	52	theme	PRO	466:468	arg1	repeat					471:476	the HCF-1(PRO) repeat	456:476	the HCF-1(PRO) repeat	456:476	We show here that the HCF-1(PRO) repeat is recognized by O-linked β-N-acetylglucosamine transferase (OGT), which both O-GlcNAcylates the HCF-1(N) subunit and directly cleaves the HCF-1(PRO) repeat.
27350215	5	0	theme	cell	679:682	arg1	lines					684:688	C-mannosylation-defective Rspo3 mutant-overexpressing cell lines	625:688	C-mannosylation-defective Rspo3 mutant-overexpressing cell lines	625:688	Using C-mannosylation-defective Rspo3 mutant-overexpressing cell lines, we found that C-mannosylation of Rspo3 promotes its secretion and activates Wnt/β-catenin signaling.
27350215	2	1	theme	unique	327:332	arg1	C-mannosylation					308:322	C-mannosylation	308:322	C-mannosylation	308:322	In this study, we focused on C-mannosylation, a unique type of glycosylation, of human Rspo3.
27350215	2	1	theme	unique	327:332	arg1	type					334:337	a unique type	325:337	a unique type of glycosylation	325:354	In this study, we focused on C-mannosylation, a unique type of glycosylation, of human Rspo3.
27350215	4	2	from	Trp	588:590	arg1	C-mannosylated					552:565	C-mannosylated	552:565	C-mannosylated	552:565	We demonstrated that Rspo3 was C-mannosylated at both Trp(153) and Trp(156) by mass spectrometry.
27350215	0	3	theme	signaling	84:92	arg1	secretion					44:52	secretion	44:52	secretion	44:52	C-mannosylation of R-spondin3 regulates its secretion and activity of Wnt/β-catenin signaling in cells.
27350215	0	3	theme	signaling	84:92	arg1	activity					58:65	activity	58:65	activity	58:65	C-mannosylation of R-spondin3 regulates its secretion and activity of Wnt/β-catenin signaling in cells.
27350215	1	4	theme	embryonic	240:248	arg1	development					250:260	embryonic development	240:260	embryonic development	240:260	R-spondin3 (Rspo3) is a secreted protein, which acts as an agonist of canonical Wnt/β-catenin signaling that plays an important role in embryonic development and homeostasis.
27350215	0	5	from	activity	58:65	arg1	cells					97:101	cells	97:101	cells	97:101	C-mannosylation of R-spondin3 regulates its secretion and activity of Wnt/β-catenin signaling in cells.
27350215	3	6	contain	has	379:381	arg2	sites					412:416	two putative C-mannosylation sites	383:416	two putative C-mannosylation sites	383:416	Rspo3 has two putative C-mannosylation sites at Trp(153) and Trp(156) ; however, it had been unclear whether these sites are C-mannosylated or not.
27350215	3	6	contain	has	379:381	arg1	Rspo3					373:377	Rspo3	373:377	Rspo3	373:377	Rspo3 has two putative C-mannosylation sites at Trp(153) and Trp(156) ; however, it had been unclear whether these sites are C-mannosylated or not.
27350215	5	7	theme	Wnt/β-catenin	767:779	arg1	signaling					781:789	Wnt/β-catenin signaling	767:789	Wnt/β-catenin signaling	767:789	Using C-mannosylation-defective Rspo3 mutant-overexpressing cell lines, we found that C-mannosylation of Rspo3 promotes its secretion and activates Wnt/β-catenin signaling.
27350215	2	8	theme	human	360:364	arg1	Rspo3					366:370	human Rspo3	360:370	human Rspo3	360:370	In this study, we focused on C-mannosylation, a unique type of glycosylation, of human Rspo3.
27350215	5	9	theme	C-mannosylation-defective	625:649	arg1	lines					684:688	C-mannosylation-defective Rspo3 mutant-overexpressing cell lines	625:688	C-mannosylation-defective Rspo3 mutant-overexpressing cell lines	625:688	Using C-mannosylation-defective Rspo3 mutant-overexpressing cell lines, we found that C-mannosylation of Rspo3 promotes its secretion and activates Wnt/β-catenin signaling.
27350215	0	10	from	secretion	44:52	arg1	cells					97:101	cells	97:101	cells	97:101	C-mannosylation of R-spondin3 regulates its secretion and activity of Wnt/β-catenin signaling in cells.
27350215	4	11	from	Trp	575:577	arg1	C-mannosylated					552:565	C-mannosylated	552:565	C-mannosylated	552:565	We demonstrated that Rspo3 was C-mannosylated at both Trp(153) and Trp(156) by mass spectrometry.
27350215	4	12	gly	C-mannosylated	552:565	arg2	156					592:594	156	592:594	156	592:594	We demonstrated that Rspo3 was C-mannosylated at both Trp(153) and Trp(156) by mass spectrometry.
27350215	4	12	gly	C-mannosylated	552:565	arg1	Rspo3					542:546	Rspo3	542:546	Rspo3	542:546	We demonstrated that Rspo3 was C-mannosylated at both Trp(153) and Trp(156) by mass spectrometry.
27350215	4	12	gly	C-mannosylated	552:565	arg2	Trp					575:577	Trp(153)	575:582	Trp(153)	575:582	We demonstrated that Rspo3 was C-mannosylated at both Trp(153) and Trp(156) by mass spectrometry.
27350215	4	12	gly	C-mannosylated	552:565	arg2	Trp					588:590	Trp	588:590	Trp(156)	588:595	We demonstrated that Rspo3 was C-mannosylated at both Trp(153) and Trp(156) by mass spectrometry.
27350215	5	13	theme	Rspo3	651:655	arg1	lines					684:688	C-mannosylation-defective Rspo3 mutant-overexpressing cell lines	625:688	C-mannosylation-defective Rspo3 mutant-overexpressing cell lines	625:688	Using C-mannosylation-defective Rspo3 mutant-overexpressing cell lines, we found that C-mannosylation of Rspo3 promotes its secretion and activates Wnt/β-catenin signaling.
27350215	3	14	theme	putative	387:394	arg1	sites					412:416	two putative C-mannosylation sites	383:416	two putative C-mannosylation sites	383:416	Rspo3 has two putative C-mannosylation sites at Trp(153) and Trp(156) ; however, it had been unclear whether these sites are C-mannosylated or not.
27350215	5	15	theme	Rspo3	724:728	arg1	C-mannosylation					705:719	C-mannosylation	705:719	C-mannosylation of Rspo3	705:728	Using C-mannosylation-defective Rspo3 mutant-overexpressing cell lines, we found that C-mannosylation of Rspo3 promotes its secretion and activates Wnt/β-catenin signaling.
27350215	0	16	theme	R-spondin3	19:28	arg1	C-mannosylation					0:14	C-mannosylation	0:14	C-mannosylation of R-spondin3	0:28	C-mannosylation of R-spondin3 regulates its secretion and activity of Wnt/β-catenin signaling in cells.
27350215	1	17	theme	canonical	174:182	arg1	signaling					198:206	canonical Wnt/β-catenin signaling	174:206	canonical Wnt/β-catenin signaling that plays an important role in embryonic development and homeostasis	174:276	R-spondin3 (Rspo3) is a secreted protein, which acts as an agonist of canonical Wnt/β-catenin signaling that plays an important role in embryonic development and homeostasis.
27350215	1	18	theme	Wnt/β-catenin	184:196	arg1	signaling					198:206	canonical Wnt/β-catenin signaling	174:206	canonical Wnt/β-catenin signaling that plays an important role in embryonic development and homeostasis	174:276	R-spondin3 (Rspo3) is a secreted protein, which acts as an agonist of canonical Wnt/β-catenin signaling that plays an important role in embryonic development and homeostasis.
27350215	0	19	gly	C-mannosylation	0:14	arg1	R-spondin3					19:28	R-spondin3	19:28	R-spondin3	19:28	C-mannosylation of R-spondin3 regulates its secretion and activity of Wnt/β-catenin signaling in cells.
27350215	2	20	theme	glycosylation	342:354	arg1	C-mannosylation					308:322	C-mannosylation	308:322	C-mannosylation	308:322	In this study, we focused on C-mannosylation, a unique type of glycosylation, of human Rspo3.
27350215	2	20	theme	glycosylation	342:354	arg1	type					334:337	a unique type	325:337	a unique type of glycosylation	325:354	In this study, we focused on C-mannosylation, a unique type of glycosylation, of human Rspo3.
27350215	3	21	gly	C-mannosylated	498:511	arg1	sites					488:492	these sites	482:492	these sites	482:492	Rspo3 has two putative C-mannosylation sites at Trp(153) and Trp(156) ; however, it had been unclear whether these sites are C-mannosylated or not.
27350215	3	22	theme	C-mannosylation	396:410	arg1	sites					412:416	two putative C-mannosylation sites	383:416	two putative C-mannosylation sites	383:416	Rspo3 has two putative C-mannosylation sites at Trp(153) and Trp(156) ; however, it had been unclear whether these sites are C-mannosylated or not.
27350215	5	23	gly	C-mannosylation	705:719	arg1	Rspo3					724:728	Rspo3	724:728	Rspo3	724:728	Using C-mannosylation-defective Rspo3 mutant-overexpressing cell lines, we found that C-mannosylation of Rspo3 promotes its secretion and activates Wnt/β-catenin signaling.
27350215	1	24	theme	signaling	198:206	arg1	protein					137:143	a secreted protein	126:143	a secreted protein	126:143	R-spondin3 (Rspo3) is a secreted protein, which acts as an agonist of canonical Wnt/β-catenin signaling that plays an important role in embryonic development and homeostasis.
27350215	1	24	theme	signaling	198:206	arg1	agonist					163:169	an agonist	160:169	an agonist of canonical Wnt/β-catenin signaling that plays an important role in embryonic development and homeostasis	160:276	R-spondin3 (Rspo3) is a secreted protein, which acts as an agonist of canonical Wnt/β-catenin signaling that plays an important role in embryonic development and homeostasis.
27350215	2	25	gly	C-mannosylation	308:322	arg1	Rspo3					366:370	human Rspo3	360:370	human Rspo3	360:370	In this study, we focused on C-mannosylation, a unique type of glycosylation, of human Rspo3.
27350215	4	26	theme	mass	600:603	arg1	spectrometry					605:616	mass spectrometry	600:616	mass spectrometry	600:616	We demonstrated that Rspo3 was C-mannosylated at both Trp(153) and Trp(156) by mass spectrometry.
27350215	3	27	gly	C-mannosylation	396:410	arg2	sites					412:416	two putative C-mannosylation sites	383:416	two putative C-mannosylation sites	383:416	Rspo3 has two putative C-mannosylation sites at Trp(153) and Trp(156) ; however, it had been unclear whether these sites are C-mannosylated or not.
27350215	0	28	theme	Wnt/β-catenin	70:82	arg1	signaling					84:92	Wnt/β-catenin signaling	70:92	Wnt/β-catenin signaling	70:92	C-mannosylation of R-spondin3 regulates its secretion and activity of Wnt/β-catenin signaling in cells.
27350215	2	29	theme	Rspo3	366:370	arg1	C-mannosylation					308:322	C-mannosylation	308:322	C-mannosylation	308:322	In this study, we focused on C-mannosylation, a unique type of glycosylation, of human Rspo3.
27350215	2	29	theme	Rspo3	366:370	arg1	type					334:337	a unique type	325:337	a unique type of glycosylation	325:354	In this study, we focused on C-mannosylation, a unique type of glycosylation, of human Rspo3.
27350215	1	30	theme	secreted	128:135	arg1	protein					137:143	a secreted protein	126:143	a secreted protein	126:143	R-spondin3 (Rspo3) is a secreted protein, which acts as an agonist of canonical Wnt/β-catenin signaling that plays an important role in embryonic development and homeostasis.
27350215	1	30	theme	secreted	128:135	arg1	agonist					163:169	an agonist	160:169	an agonist of canonical Wnt/β-catenin signaling that plays an important role in embryonic development and homeostasis	160:276	R-spondin3 (Rspo3) is a secreted protein, which acts as an agonist of canonical Wnt/β-catenin signaling that plays an important role in embryonic development and homeostasis.
27350215	1	30	theme	secreted	128:135	arg1	R-spondin3					104:113	R-spondin3	104:113	R-spondin3 (Rspo3)	104:121	R-spondin3 (Rspo3) is a secreted protein, which acts as an agonist of canonical Wnt/β-catenin signaling that plays an important role in embryonic development and homeostasis.
27350215	5	31	theme	mutant-overexpressing	657:677	arg1	lines					684:688	C-mannosylation-defective Rspo3 mutant-overexpressing cell lines	625:688	C-mannosylation-defective Rspo3 mutant-overexpressing cell lines	625:688	Using C-mannosylation-defective Rspo3 mutant-overexpressing cell lines, we found that C-mannosylation of Rspo3 promotes its secretion and activates Wnt/β-catenin signaling.
27350215	1	32	theme	important	222:230	arg1	role					232:235	an important role	219:235	an important role	219:235	R-spondin3 (Rspo3) is a secreted protein, which acts as an agonist of canonical Wnt/β-catenin signaling that plays an important role in embryonic development and homeostasis.
9786864	3	0	theme	extracellular	301:313	arg1	domain					315:320	The extracellular domain	297:320	The extracellular domain of this receptor	297:337	The extracellular domain of this receptor is comprised of two immunoglobulin-like and cytokine-receptor homology domains each and type III fibronectin domains.
9786864	3	0	theme	extracellular	301:313	arg1	receptor					330:337	this receptor	325:337	this receptor	325:337	The extracellular domain of this receptor is comprised of two immunoglobulin-like and cytokine-receptor homology domains each and type III fibronectin domains.
9786864	6	1	theme	distinct	939:946	arg1	knots					956:960	several distinct cystine knots	931:960	several distinct cystine knots as well as 10 free cysteines	931:989	The determined disulfide motif of the soluble leptin receptor contained several distinct cystine knots as well as 10 free cysteines.
9786864	7	2	theme	N-glycosylation	996:1010	arg1	analysis					1012:1019	The N-glycosylation analysis	992:1019	The N-glycosylation analysis	992:1019	The N-glycosylation analysis revealed that Asn624 of the WSXWS motif (residues 622-626) within the C-terminal cytokine receptor homology domain was glycosylated, indicating that this region is solvent-exposed.
9786864	6	3	theme	receptor	912:919	arg1	motif					884:888	The determined disulfide motif	859:888	The determined disulfide motif of the soluble leptin receptor	859:919	The determined disulfide motif of the soluble leptin receptor contained several distinct cystine knots as well as 10 free cysteines.
9786864	2	4	theme	leptin	119:124	arg1	receptor					126:133	The leptin receptor	115:133	The leptin receptor (OB-R)	115:140	The leptin receptor (OB-R) is a member of the class I cytokine receptor family and mediates the weight regulatory effects of its ligand through interaction with cytoplasmic kinases.
9786864	2	4	theme	leptin	119:124	arg1	member					147:152	a member	145:152	a member of the class I cytokine receptor family	145:192	The leptin receptor (OB-R) is a member of the class I cytokine receptor family and mediates the weight regulatory effects of its ligand through interaction with cytoplasmic kinases.
9786864	2	4	theme	leptin	119:124	arg1	OB-R					136:139	OB-R	136:139	OB-R	136:139	The leptin receptor (OB-R) is a member of the class I cytokine receptor family and mediates the weight regulatory effects of its ligand through interaction with cytoplasmic kinases.
9786864	8	5	theme	WSXWS	1236:1240	arg1	motif					1242:1246	the N-terminal WSXWS motif	1221:1246	the N-terminal WSXWS motif	1221:1246	On the other hand, the N-terminal WSXWS motif was not glycosylated.
9786864	6	6	theme	determined	863:872	arg1	motif					884:888	The determined disulfide motif	859:888	The determined disulfide motif of the soluble leptin receptor	859:919	The determined disulfide motif of the soluble leptin receptor contained several distinct cystine knots as well as 10 free cysteines.
9786864	5	7	theme	145,000	724:730	arg1	weight					700:705	a molecular weight	688:705	a molecular weight of approximately 145,000	688:730	The purified protein had a molecular weight of approximately 145,000 and exhibited ligand binding ability as evidenced by formation of ligand-receptor complex, followed by chemical cross-linking.
9786864	3	8	theme	cytokine-receptor	383:399	arg1	domains					410:416	two immunoglobulin-like and cytokine-receptor homology domains	355:416	two immunoglobulin-like and cytokine-receptor homology domains each	355:421	The extracellular domain of this receptor is comprised of two immunoglobulin-like and cytokine-receptor homology domains each and type III fibronectin domains.
9786864	4	9	theme	extensive	595:603	arg1	N-glycosylation					605:619	extensive N-glycosylation	595:619	extensive N-glycosylation (approximately 36% of the total protein)	595:660	The extracellular domain of human leptin receptor was expressed in and purified from Chinese hamster ovary cells and was found to contain extensive N-glycosylation (approximately 36% of the total protein).
9786864	4	10	theme	human	485:489	arg1	receptor					498:505	human leptin receptor	485:505	human leptin receptor	485:505	The extracellular domain of human leptin receptor was expressed in and purified from Chinese hamster ovary cells and was found to contain extensive N-glycosylation (approximately 36% of the total protein).
9786864	1	11	theme	N-glycosylation	64:78	arg1	sites					80:84	N-glycosylation sites	64:84	N-glycosylation sites of the extracellular domain	64:112	Determination of disulfide structure and N-glycosylation sites of the extracellular domain.
9786864	1	11	theme	N-glycosylation	64:78	arg1	domain					107:112	the extracellular domain	89:112	the extracellular domain	89:112	Determination of disulfide structure and N-glycosylation sites of the extracellular domain.
9786864	1	11	theme	N-glycosylation	64:78	arg1	structure					50:58	disulfide structure	40:58	disulfide structure	40:58	Determination of disulfide structure and N-glycosylation sites of the extracellular domain.
9786864	8	12	theme	other	1209:1213	arg1	hand					1215:1218	the other hand	1205:1218	the other hand	1205:1218	On the other hand, the N-terminal WSXWS motif was not glycosylated.
9786864	3	13	theme	receptor	330:337	arg1	domain					315:320	The extracellular domain	297:320	The extracellular domain of this receptor	297:337	The extracellular domain of this receptor is comprised of two immunoglobulin-like and cytokine-receptor homology domains each and type III fibronectin domains.
9786864	3	13	theme	receptor	330:337	arg1	receptor					330:337	this receptor	325:337	this receptor	325:337	The extracellular domain of this receptor is comprised of two immunoglobulin-like and cytokine-receptor homology domains each and type III fibronectin domains.
9786864	6	14	theme	leptin	905:910	arg1	receptor					912:919	the soluble leptin receptor	893:919	the soluble leptin receptor	893:919	The determined disulfide motif of the soluble leptin receptor contained several distinct cystine knots as well as 10 free cysteines.
9786864	7	15	theme	receptor	1111:1118	arg1	domain					1129:1134	the C-terminal cytokine receptor homology domain	1087:1134	the C-terminal cytokine receptor homology domain	1087:1134	The N-glycosylation analysis revealed that Asn624 of the WSXWS motif (residues 622-626) within the C-terminal cytokine receptor homology domain was glycosylated, indicating that this region is solvent-exposed.
9786864	3	16	theme	fibronectin	436:446	arg1	domains					448:454	type III fibronectin domains	427:454	type III fibronectin domains	427:454	The extracellular domain of this receptor is comprised of two immunoglobulin-like and cytokine-receptor homology domains each and type III fibronectin domains.
9786864	5	17	theme	ligand	746:751	arg1	ability					761:767	ligand binding ability	746:767	ligand binding ability	746:767	The purified protein had a molecular weight of approximately 145,000 and exhibited ligand binding ability as evidenced by formation of ligand-receptor complex, followed by chemical cross-linking.
9786864	4	18	theme	receptor	498:505	arg1	receptor					498:505	human leptin receptor	485:505	human leptin receptor	485:505	The extracellular domain of human leptin receptor was expressed in and purified from Chinese hamster ovary cells and was found to contain extensive N-glycosylation (approximately 36% of the total protein).
9786864	4	18	theme	receptor	498:505	arg1	domain					475:480	The extracellular domain	457:480	The extracellular domain of human leptin receptor	457:505	The extracellular domain of human leptin receptor was expressed in and purified from Chinese hamster ovary cells and was found to contain extensive N-glycosylation (approximately 36% of the total protein).
9786864	3	19	dep	domains	410:416	arg1	each					418:421	each	418:421	each	418:421	The extracellular domain of this receptor is comprised of two immunoglobulin-like and cytokine-receptor homology domains each and type III fibronectin domains.
9786864	2	20	theme	ligand	244:249	arg1	effects					229:235	the weight regulatory effects	207:235	the weight regulatory effects of its ligand	207:249	The leptin receptor (OB-R) is a member of the class I cytokine receptor family and mediates the weight regulatory effects of its ligand through interaction with cytoplasmic kinases.
9786864	4	21	theme	protein	653:659	arg1	%					638:638	approximately 36%	622:638	approximately 36% of the total protein	622:659	The extracellular domain of human leptin receptor was expressed in and purified from Chinese hamster ovary cells and was found to contain extensive N-glycosylation (approximately 36% of the total protein).
9786864	4	21	theme	protein	653:659	arg1	protein					653:659	the total protein	643:659	the total protein	643:659	The extracellular domain of human leptin receptor was expressed in and purified from Chinese hamster ovary cells and was found to contain extensive N-glycosylation (approximately 36% of the total protein).
9786864	0	22	theme	leptin	6:11	arg1	receptor					13:20	Human leptin receptor	0:20	Human leptin receptor.	0:21	Human leptin receptor.
9786864	4	23	theme	leptin	491:496	arg1	receptor					498:505	human leptin receptor	485:505	human leptin receptor	485:505	The extracellular domain of human leptin receptor was expressed in and purified from Chinese hamster ovary cells and was found to contain extensive N-glycosylation (approximately 36% of the total protein).
9786864	7	24	theme	C-terminal	1091:1100	arg1	domain					1129:1134	the C-terminal cytokine receptor homology domain	1087:1134	the C-terminal cytokine receptor homology domain	1087:1134	The N-glycosylation analysis revealed that Asn624 of the WSXWS motif (residues 622-626) within the C-terminal cytokine receptor homology domain was glycosylated, indicating that this region is solvent-exposed.
9786864	5	25	theme	binding	753:759	arg1	ability					761:767	ligand binding ability	746:767	ligand binding ability	746:767	The purified protein had a molecular weight of approximately 145,000 and exhibited ligand binding ability as evidenced by formation of ligand-receptor complex, followed by chemical cross-linking.
9786864	6	26	theme	several	931:937	arg1	knots					956:960	several distinct cystine knots	931:960	several distinct cystine knots as well as 10 free cysteines	931:989	The determined disulfide motif of the soluble leptin receptor contained several distinct cystine knots as well as 10 free cysteines.
9786864	3	27	theme	type	427:430	arg1	domains					448:454	type III fibronectin domains	427:454	type III fibronectin domains	427:454	The extracellular domain of this receptor is comprised of two immunoglobulin-like and cytokine-receptor homology domains each and type III fibronectin domains.
9786864	0	28	theme	Human	0:4	arg1	receptor					13:20	Human leptin receptor	0:20	Human leptin receptor.	0:21	Human leptin receptor.
9786864	4	29	dep	N-glycosylation	605:619	arg1	%					638:638	approximately 36%	622:638	approximately 36% of the total protein	622:659	The extracellular domain of human leptin receptor was expressed in and purified from Chinese hamster ovary cells and was found to contain extensive N-glycosylation (approximately 36% of the total protein).
9786864	4	29	dep	N-glycosylation	605:619	arg1	protein					653:659	the total protein	643:659	the total protein	643:659	The extracellular domain of human leptin receptor was expressed in and purified from Chinese hamster ovary cells and was found to contain extensive N-glycosylation (approximately 36% of the total protein).
9786864	1	30	theme	extracellular	93:105	arg1	domain					107:112	the extracellular domain	89:112	the extracellular domain	89:112	Determination of disulfide structure and N-glycosylation sites of the extracellular domain.
9786864	4	31	theme	ovary	558:562	arg1	cells					564:568	Chinese hamster ovary cells	542:568	Chinese hamster ovary cells	542:568	The extracellular domain of human leptin receptor was expressed in and purified from Chinese hamster ovary cells and was found to contain extensive N-glycosylation (approximately 36% of the total protein).
9786864	5	32	theme	molecular	690:698	arg1	weight					700:705	a molecular weight	688:705	a molecular weight of approximately 145,000	688:730	The purified protein had a molecular weight of approximately 145,000 and exhibited ligand binding ability as evidenced by formation of ligand-receptor complex, followed by chemical cross-linking.
9786864	1	33	theme	domain	107:112	arg1	sites					80:84	N-glycosylation sites	64:84	N-glycosylation sites of the extracellular domain	64:112	Determination of disulfide structure and N-glycosylation sites of the extracellular domain.
9786864	1	33	theme	domain	107:112	arg1	domain					107:112	the extracellular domain	89:112	the extracellular domain	89:112	Determination of disulfide structure and N-glycosylation sites of the extracellular domain.
9786864	1	33	theme	domain	107:112	arg1	Determination					23:35	Determination	23:35	Determination of disulfide structure	23:58	Determination of disulfide structure and N-glycosylation sites of the extracellular domain.
9786864	1	33	theme	domain	107:112	arg1	structure					50:58	disulfide structure	40:58	disulfide structure	40:58	Determination of disulfide structure and N-glycosylation sites of the extracellular domain.
9786864	4	34	contain	contain	587:593	arg1	receptor					498:505	human leptin receptor	485:505	human leptin receptor	485:505	The extracellular domain of human leptin receptor was expressed in and purified from Chinese hamster ovary cells and was found to contain extensive N-glycosylation (approximately 36% of the total protein).
9786864	4	34	contain	contain	587:593	arg2	N-glycosylation					605:619	extensive N-glycosylation	595:619	extensive N-glycosylation (approximately 36% of the total protein)	595:660	The extracellular domain of human leptin receptor was expressed in and purified from Chinese hamster ovary cells and was found to contain extensive N-glycosylation (approximately 36% of the total protein).
9786864	4	34	contain	contain	587:593	arg1	domain					475:480	The extracellular domain	457:480	The extracellular domain of human leptin receptor	457:505	The extracellular domain of human leptin receptor was expressed in and purified from Chinese hamster ovary cells and was found to contain extensive N-glycosylation (approximately 36% of the total protein).
9786864	5	35	theme	chemical	835:842	arg1	cross-linking					844:856	chemical cross-linking	835:856	chemical cross-linking	835:856	The purified protein had a molecular weight of approximately 145,000 and exhibited ligand binding ability as evidenced by formation of ligand-receptor complex, followed by chemical cross-linking.
9786864	3	36	theme	immunoglobulin-like	359:377	arg1	domains					410:416	two immunoglobulin-like and cytokine-receptor homology domains	355:416	two immunoglobulin-like and cytokine-receptor homology domains each	355:421	The extracellular domain of this receptor is comprised of two immunoglobulin-like and cytokine-receptor homology domains each and type III fibronectin domains.
9786864	6	37	theme	free	976:979	arg1	cysteines					981:989	10 free cysteines	973:989	several distinct cystine knots as well as 10 free cysteines	931:989	The determined disulfide motif of the soluble leptin receptor contained several distinct cystine knots as well as 10 free cysteines.
9786864	2	38	theme	class	161:165	arg1	family					187:192	the class I cytokine receptor family	157:192	the class I cytokine receptor family	157:192	The leptin receptor (OB-R) is a member of the class I cytokine receptor family and mediates the weight regulatory effects of its ligand through interaction with cytoplasmic kinases.
9786864	2	39	theme	cytoplasmic	276:286	arg1	kinases					288:294	cytoplasmic kinases	276:294	cytoplasmic kinases	276:294	The leptin receptor (OB-R) is a member of the class I cytokine receptor family and mediates the weight regulatory effects of its ligand through interaction with cytoplasmic kinases.
9786864	7	40	gly	glycosylated	1140:1151	arg1	Asn624					1035:1040	Asn624	1035:1040	Asn624 of the WSXWS motif (residues 622-626) within the C-terminal cytokine receptor homology domain	1035:1134	The N-glycosylation analysis revealed that Asn624 of the WSXWS motif (residues 622-626) within the C-terminal cytokine receptor homology domain was glycosylated, indicating that this region is solvent-exposed.
9786864	8	41	theme	N-terminal	1225:1234	arg1	motif					1242:1246	the N-terminal WSXWS motif	1221:1246	the N-terminal WSXWS motif	1221:1246	On the other hand, the N-terminal WSXWS motif was not glycosylated.
9786864	2	42	theme	weight	211:216	arg1	effects					229:235	the weight regulatory effects	207:235	the weight regulatory effects of its ligand	207:249	The leptin receptor (OB-R) is a member of the class I cytokine receptor family and mediates the weight regulatory effects of its ligand through interaction with cytoplasmic kinases.
9786864	4	43	theme	total	647:651	arg1	protein					653:659	the total protein	643:659	the total protein	643:659	The extracellular domain of human leptin receptor was expressed in and purified from Chinese hamster ovary cells and was found to contain extensive N-glycosylation (approximately 36% of the total protein).
9786864	6	44	contain	contained	921:929	arg2	knots					956:960	several distinct cystine knots	931:960	several distinct cystine knots as well as 10 free cysteines	931:989	The determined disulfide motif of the soluble leptin receptor contained several distinct cystine knots as well as 10 free cysteines.
9786864	6	44	contain	contained	921:929	arg2	cysteines					981:989	10 free cysteines	973:989	several distinct cystine knots as well as 10 free cysteines	931:989	The determined disulfide motif of the soluble leptin receptor contained several distinct cystine knots as well as 10 free cysteines.
9786864	6	44	contain	contained	921:929	arg1	motif					884:888	The determined disulfide motif	859:888	The determined disulfide motif of the soluble leptin receptor	859:919	The determined disulfide motif of the soluble leptin receptor contained several distinct cystine knots as well as 10 free cysteines.
9786864	5	45	dep	had	684:686	arg1	followed					823:830	followed	823:830	followed by chemical cross-linking	823:856	The purified protein had a molecular weight of approximately 145,000 and exhibited ligand binding ability as evidenced by formation of ligand-receptor complex, followed by chemical cross-linking.
9786864	6	46	theme	disulfide	874:882	arg1	motif					884:888	The determined disulfide motif	859:888	The determined disulfide motif of the soluble leptin receptor	859:919	The determined disulfide motif of the soluble leptin receptor contained several distinct cystine knots as well as 10 free cysteines.
9786864	4	47	theme	Chinese	542:548	arg1	cells					564:568	Chinese hamster ovary cells	542:568	Chinese hamster ovary cells	542:568	The extracellular domain of human leptin receptor was expressed in and purified from Chinese hamster ovary cells and was found to contain extensive N-glycosylation (approximately 36% of the total protein).
9786864	3	48	theme	homology	401:408	arg1	domains					410:416	two immunoglobulin-like and cytokine-receptor homology domains	355:416	two immunoglobulin-like and cytokine-receptor homology domains each	355:421	The extracellular domain of this receptor is comprised of two immunoglobulin-like and cytokine-receptor homology domains each and type III fibronectin domains.
9786864	5	49	contain	had	684:686	arg2	weight					700:705	a molecular weight	688:705	a molecular weight of approximately 145,000	688:730	The purified protein had a molecular weight of approximately 145,000 and exhibited ligand binding ability as evidenced by formation of ligand-receptor complex, followed by chemical cross-linking.
9786864	5	49	contain	had	684:686	arg1	protein					676:682	The purified protein	663:682	The purified protein	663:682	The purified protein had a molecular weight of approximately 145,000 and exhibited ligand binding ability as evidenced by formation of ligand-receptor complex, followed by chemical cross-linking.
9786864	5	50	theme	purified	667:674	arg1	protein					676:682	The purified protein	663:682	The purified protein	663:682	The purified protein had a molecular weight of approximately 145,000 and exhibited ligand binding ability as evidenced by formation of ligand-receptor complex, followed by chemical cross-linking.
9786864	4	51	theme	extracellular	461:473	arg1	receptor					498:505	human leptin receptor	485:505	human leptin receptor	485:505	The extracellular domain of human leptin receptor was expressed in and purified from Chinese hamster ovary cells and was found to contain extensive N-glycosylation (approximately 36% of the total protein).
9786864	4	51	theme	extracellular	461:473	arg1	domain					475:480	The extracellular domain	457:480	The extracellular domain of human leptin receptor	457:505	The extracellular domain of human leptin receptor was expressed in and purified from Chinese hamster ovary cells and was found to contain extensive N-glycosylation (approximately 36% of the total protein).
9786864	6	52	theme	soluble	897:903	arg1	receptor					912:919	the soluble leptin receptor	893:919	the soluble leptin receptor	893:919	The determined disulfide motif of the soluble leptin receptor contained several distinct cystine knots as well as 10 free cysteines.
9786864	5	53	theme	ligand-receptor	798:812	arg1	complex					814:820	ligand-receptor complex	798:820	ligand-receptor complex	798:820	The purified protein had a molecular weight of approximately 145,000 and exhibited ligand binding ability as evidenced by formation of ligand-receptor complex, followed by chemical cross-linking.
9786864	4	54	theme	hamster	550:556	arg1	cells					564:568	Chinese hamster ovary cells	542:568	Chinese hamster ovary cells	542:568	The extracellular domain of human leptin receptor was expressed in and purified from Chinese hamster ovary cells and was found to contain extensive N-glycosylation (approximately 36% of the total protein).
9786864	2	55	theme	family	187:192	arg1	receptor					126:133	The leptin receptor	115:133	The leptin receptor (OB-R)	115:140	The leptin receptor (OB-R) is a member of the class I cytokine receptor family and mediates the weight regulatory effects of its ligand through interaction with cytoplasmic kinases.
9786864	2	55	theme	family	187:192	arg1	member					147:152	a member	145:152	a member of the class I cytokine receptor family	145:192	The leptin receptor (OB-R) is a member of the class I cytokine receptor family and mediates the weight regulatory effects of its ligand through interaction with cytoplasmic kinases.
9786864	7	56	theme	homology	1120:1127	arg1	domain					1129:1134	the C-terminal cytokine receptor homology domain	1087:1134	the C-terminal cytokine receptor homology domain	1087:1134	The N-glycosylation analysis revealed that Asn624 of the WSXWS motif (residues 622-626) within the C-terminal cytokine receptor homology domain was glycosylated, indicating that this region is solvent-exposed.
9786864	8	57	gly	glycosylated	1256:1267	arg1	hand					1215:1218	the other hand	1205:1218	the other hand	1205:1218	On the other hand, the N-terminal WSXWS motif was not glycosylated.
9786864	8	57	gly	glycosylated	1256:1267	arg2	motif					1242:1246	the N-terminal WSXWS motif	1221:1246	the N-terminal WSXWS motif	1221:1246	On the other hand, the N-terminal WSXWS motif was not glycosylated.
9786864	8	57	gly	glycosylated	1256:1267	arg2	hand					1215:1218	the other hand	1205:1218	the other hand	1205:1218	On the other hand, the N-terminal WSXWS motif was not glycosylated.
9786864	8	57	gly	glycosylated	1256:1267	arg1	motif					1242:1246	the N-terminal WSXWS motif	1221:1246	the N-terminal WSXWS motif	1221:1246	On the other hand, the N-terminal WSXWS motif was not glycosylated.
9786864	1	58	theme	structure	50:58	arg1	sites					80:84	N-glycosylation sites	64:84	N-glycosylation sites of the extracellular domain	64:112	Determination of disulfide structure and N-glycosylation sites of the extracellular domain.
9786864	1	58	theme	structure	50:58	arg1	domain					107:112	the extracellular domain	89:112	the extracellular domain	89:112	Determination of disulfide structure and N-glycosylation sites of the extracellular domain.
9786864	1	58	theme	structure	50:58	arg1	Determination					23:35	Determination	23:35	Determination of disulfide structure	23:58	Determination of disulfide structure and N-glycosylation sites of the extracellular domain.
9786864	1	58	theme	structure	50:58	arg1	structure					50:58	disulfide structure	40:58	disulfide structure	40:58	Determination of disulfide structure and N-glycosylation sites of the extracellular domain.
9786864	7	59	theme	WSXWS	1049:1053	arg1	residues					1062:1069	residues 622-626	1062:1077	residues 622-626	1062:1077	The N-glycosylation analysis revealed that Asn624 of the WSXWS motif (residues 622-626) within the C-terminal cytokine receptor homology domain was glycosylated, indicating that this region is solvent-exposed.
9786864	7	59	theme	WSXWS	1049:1053	arg1	motif					1055:1059	the WSXWS motif	1045:1059	the WSXWS motif (residues 622-626) within the C-terminal cytokine receptor homology domain	1045:1134	The N-glycosylation analysis revealed that Asn624 of the WSXWS motif (residues 622-626) within the C-terminal cytokine receptor homology domain was glycosylated, indicating that this region is solvent-exposed.
9786864	2	60	theme	receptor	178:185	arg1	family					187:192	the class I cytokine receptor family	157:192	the class I cytokine receptor family	157:192	The leptin receptor (OB-R) is a member of the class I cytokine receptor family and mediates the weight regulatory effects of its ligand through interaction with cytoplasmic kinases.
9786864	7	61	theme	motif	1055:1059	arg1	Asn624					1035:1040	Asn624	1035:1040	Asn624 of the WSXWS motif (residues 622-626) within the C-terminal cytokine receptor homology domain	1035:1134	The N-glycosylation analysis revealed that Asn624 of the WSXWS motif (residues 622-626) within the C-terminal cytokine receptor homology domain was glycosylated, indicating that this region is solvent-exposed.
9786864	2	62	theme	cytokine	169:176	arg1	family					187:192	the class I cytokine receptor family	157:192	the class I cytokine receptor family	157:192	The leptin receptor (OB-R) is a member of the class I cytokine receptor family and mediates the weight regulatory effects of its ligand through interaction with cytoplasmic kinases.
9786864	7	63	dep	residues	1062:1069	arg1	622-626					1071:1077	622-626	1071:1077	622-626	1071:1077	The N-glycosylation analysis revealed that Asn624 of the WSXWS motif (residues 622-626) within the C-terminal cytokine receptor homology domain was glycosylated, indicating that this region is solvent-exposed.
9786864	7	64	theme	cytokine	1102:1109	arg1	domain					1129:1134	the C-terminal cytokine receptor homology domain	1087:1134	the C-terminal cytokine receptor homology domain	1087:1134	The N-glycosylation analysis revealed that Asn624 of the WSXWS motif (residues 622-626) within the C-terminal cytokine receptor homology domain was glycosylated, indicating that this region is solvent-exposed.
9786864	1	65	gly	N-glycosylation	64:78	arg2	structure					50:58	disulfide structure	40:58	disulfide structure	40:58	Determination of disulfide structure and N-glycosylation sites of the extracellular domain.
9786864	1	65	gly	N-glycosylation	64:78	arg2	domain					107:112	the extracellular domain	89:112	the extracellular domain	89:112	Determination of disulfide structure and N-glycosylation sites of the extracellular domain.
9786864	1	65	gly	N-glycosylation	64:78	arg1	structure					50:58	disulfide structure	40:58	disulfide structure	40:58	Determination of disulfide structure and N-glycosylation sites of the extracellular domain.
9786864	1	65	gly	N-glycosylation	64:78	arg1	domain					107:112	the extracellular domain	89:112	the extracellular domain	89:112	Determination of disulfide structure and N-glycosylation sites of the extracellular domain.
9786864	1	65	gly	N-glycosylation	64:78	arg2	sites					80:84	N-glycosylation sites	64:84	N-glycosylation sites of the extracellular domain	64:112	Determination of disulfide structure and N-glycosylation sites of the extracellular domain.
9786864	2	66	theme	I	167:167	arg1	family					187:192	the class I cytokine receptor family	157:192	the class I cytokine receptor family	157:192	The leptin receptor (OB-R) is a member of the class I cytokine receptor family and mediates the weight regulatory effects of its ligand through interaction with cytoplasmic kinases.
9786864	1	67	theme	disulfide	40:48	arg1	structure					50:58	disulfide structure	40:58	disulfide structure	40:58	Determination of disulfide structure and N-glycosylation sites of the extracellular domain.
9786864	6	68	theme	cystine	948:954	arg1	knots					956:960	several distinct cystine knots	931:960	several distinct cystine knots as well as 10 free cysteines	931:989	The determined disulfide motif of the soluble leptin receptor contained several distinct cystine knots as well as 10 free cysteines.
9786864	2	69	theme	regulatory	218:227	arg1	effects					229:235	the weight regulatory effects	207:235	the weight regulatory effects of its ligand	207:249	The leptin receptor (OB-R) is a member of the class I cytokine receptor family and mediates the weight regulatory effects of its ligand through interaction with cytoplasmic kinases.
9786864	5	70	theme	complex	814:820	arg1	formation					785:793	formation	785:793	formation of ligand-receptor complex	785:820	The purified protein had a molecular weight of approximately 145,000 and exhibited ligand binding ability as evidenced by formation of ligand-receptor complex, followed by chemical cross-linking.
9786864	2	71	with	interaction	259:269	arg1	kinases					288:294	cytoplasmic kinases	276:294	cytoplasmic kinases	276:294	The leptin receptor (OB-R) is a member of the class I cytokine receptor family and mediates the weight regulatory effects of its ligand through interaction with cytoplasmic kinases.
8286855	2	0	theme	Ser	496:498	arg1	quantitation					465:476	quantitation	465:476	quantitation	465:476	We have revised the sites of O-glycosylation in the extracellular domain of GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues, as well as the single N-glycosylation site.
8286855	2	0	theme	Ser	496:498	arg1	identification					446:459	positive identification	437:459	positive identification	437:459	We have revised the sites of O-glycosylation in the extracellular domain of GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues, as well as the single N-glycosylation site.
8286855	5	1	theme	present	733:739	arg1	glycosyltransferases					712:731	the glycosyltransferases	708:731	the glycosyltransferases present in erythrocytes	708:755	We propose that the glycosyltransferases present in erythrocytes recognize specific flanking sequences around potential O-glycosylation sites.
8286855	2	2	dep	Ser	496:498	arg1	residues					508:515	residues	508:515	residues	508:515	We have revised the sites of O-glycosylation in the extracellular domain of GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues, as well as the single N-glycosylation site.
8286855	1	3	theme	extracellular	235:247	arg1	domain					249:254	a 'mucin-like' extensively O-glycosylated extracellular domain	193:254	a 'mucin-like' extensively O-glycosylated extracellular domain which carries the MN blood group antigens	193:296	The human red blood cell sialoglycoprotein, glycophorin A (GpA), contains a 'mucin-like' extensively O-glycosylated extracellular domain which carries the MN blood group antigens.
8286855	2	4	theme	O-glycosylated	481:494	arg1	Ser					496:498	O-glycosylated Ser	481:498	O-glycosylated Ser	481:498	We have revised the sites of O-glycosylation in the extracellular domain of GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues, as well as the single N-glycosylation site.
8286855	5	5	from	erythrocytes	744:755	arg1	present					733:739	present	733:739	present	733:739	We propose that the glycosyltransferases present in erythrocytes recognize specific flanking sequences around potential O-glycosylation sites.
8286855	1	6	theme	glycophorin	163:173	arg1	GpA					178:180	GpA	178:180	GpA	178:180	The human red blood cell sialoglycoprotein, glycophorin A (GpA), contains a 'mucin-like' extensively O-glycosylated extracellular domain which carries the MN blood group antigens.
8286855	1	6	theme	glycophorin	163:173	arg1	sialoglycoprotein					144:160	The human red blood cell sialoglycoprotein	119:160	The human red blood cell sialoglycoprotein	119:160	The human red blood cell sialoglycoprotein, glycophorin A (GpA), contains a 'mucin-like' extensively O-glycosylated extracellular domain which carries the MN blood group antigens.
8286855	1	6	theme	glycophorin	163:173	arg1	A					175:175	glycophorin A	163:175	glycophorin A (GpA)	163:181	The human red blood cell sialoglycoprotein, glycophorin A (GpA), contains a 'mucin-like' extensively O-glycosylated extracellular domain which carries the MN blood group antigens.
8286855	4	7	from	Ser23	661:665	arg1	GpA					687:689	GpA	687:689	GpA	687:689	Carbohydrate was absent on Ser1, Ser14, Ser15, Ser23, Thr28 and Thr58 in GpA.
8286855	2	8	from	site	556:559	arg1	GpA					375:377	GpA	375:377	GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues	375:515	We have revised the sites of O-glycosylation in the extracellular domain of GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues, as well as the single N-glycosylation site.
8286855	2	8	from	site	556:559	arg1	domain					365:370	the extracellular domain	347:370	the extracellular domain of GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues	347:515	We have revised the sites of O-glycosylation in the extracellular domain of GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues, as well as the single N-glycosylation site.
8286855	0	9	theme	glycophorin	104:114	arg1	A					116:116	human glycophorin A	98:116	human glycophorin A	98:116	Glycosylation sites identified by solid-phase Edman degradation: O-linked glycosylation motifs on human glycophorin A.
8286855	5	10	theme	specific	767:774	arg1	sequences					785:793	specific flanking sequences	767:793	specific flanking sequences around potential O-glycosylation sites	767:832	We propose that the glycosyltransferases present in erythrocytes recognize specific flanking sequences around potential O-glycosylation sites.
8286855	0	11	theme	human	98:102	arg1	A					116:116	human glycophorin A	98:116	human glycophorin A	98:116	Glycosylation sites identified by solid-phase Edman degradation: O-linked glycosylation motifs on human glycophorin A.
8286855	0	12	gly	glycosylation	74:86	arg2	motifs					88:93	O-linked glycosylation motifs	65:93	O-linked glycosylation motifs on human glycophorin A	65:116	Glycosylation sites identified by solid-phase Edman degradation: O-linked glycosylation motifs on human glycophorin A.
8286855	4	13	from	Ser15	654:658	arg1	GpA					687:689	GpA	687:689	GpA	687:689	Carbohydrate was absent on Ser1, Ser14, Ser15, Ser23, Thr28 and Thr58 in GpA.
8286855	2	14	theme	single	533:538	arg1	O-glycosylation					328:342	O-glycosylation	328:342	O-glycosylation	328:342	We have revised the sites of O-glycosylation in the extracellular domain of GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues, as well as the single N-glycosylation site.
8286855	2	14	theme	single	533:538	arg1	site					556:559	the single N-glycosylation site	529:559	the single N-glycosylation site	529:559	We have revised the sites of O-glycosylation in the extracellular domain of GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues, as well as the single N-glycosylation site.
8286855	2	15	from	sites	319:323	arg1	GpA					375:377	GpA	375:377	GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues	375:515	We have revised the sites of O-glycosylation in the extracellular domain of GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues, as well as the single N-glycosylation site.
8286855	2	15	from	sites	319:323	arg1	domain					365:370	the extracellular domain	347:370	the extracellular domain of GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues	347:515	We have revised the sites of O-glycosylation in the extracellular domain of GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues, as well as the single N-glycosylation site.
8286855	9	16	from	glycosylation	1234:1246	arg1	GpA					1315:1317	GpA	1315:1317	GpA	1315:1317	These simple rules explain the glycosylation (or lack of it) on 21 of 22 Ser/Thr in the extracellular domain of GpA.
8286855	9	16	from	glycosylation	1234:1246	arg1	domain					1305:1310	the extracellular domain	1287:1310	the extracellular domain of GpA	1287:1317	These simple rules explain the glycosylation (or lack of it) on 21 of 22 Ser/Thr in the extracellular domain of GpA.
8286855	9	16	from	glycosylation	1234:1246	arg1	Ser/Thr					1276:1282	21 of 22 Ser/Thr	1267:1282	21 of 22 Ser/Thr	1267:1282	These simple rules explain the glycosylation (or lack of it) on 21 of 22 Ser/Thr in the extracellular domain of GpA.
8286855	9	17	theme	it	1260:1261	arg1	lack					1252:1255	lack	1252:1255	lack of it	1252:1261	These simple rules explain the glycosylation (or lack of it) on 21 of 22 Ser/Thr in the extracellular domain of GpA.
8286855	4	18	from	Ser14	647:651	arg1	GpA					687:689	GpA	687:689	GpA	687:689	Carbohydrate was absent on Ser1, Ser14, Ser15, Ser23, Thr28 and Thr58 in GpA.
8286855	2	19	theme	GpA	375:377	arg1	GpA					375:377	GpA	375:377	GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues	375:515	We have revised the sites of O-glycosylation in the extracellular domain of GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues, as well as the single N-glycosylation site.
8286855	2	19	theme	GpA	375:377	arg1	domain					365:370	the extracellular domain	347:370	the extracellular domain of GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues	347:515	We have revised the sites of O-glycosylation in the extracellular domain of GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues, as well as the single N-glycosylation site.
8286855	2	20	theme	positive	437:444	arg1	identification					446:459	positive identification	437:459	positive identification	437:459	We have revised the sites of O-glycosylation in the extracellular domain of GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues, as well as the single N-glycosylation site.
8286855	9	21	dep	glycosylation	1234:1246	arg1	lack					1252:1255	lack	1252:1255	lack of it	1252:1261	These simple rules explain the glycosylation (or lack of it) on 21 of 22 Ser/Thr in the extracellular domain of GpA.
8286855	2	22	theme	Thr	504:506	arg1	quantitation					465:476	quantitation	465:476	quantitation	465:476	We have revised the sites of O-glycosylation in the extracellular domain of GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues, as well as the single N-glycosylation site.
8286855	2	22	theme	Thr	504:506	arg1	identification					446:459	positive identification	437:459	positive identification	437:459	We have revised the sites of O-glycosylation in the extracellular domain of GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues, as well as the single N-glycosylation site.
8286855	6	23	theme	motifs	899:904	arg1	basis					885:889	the basis	881:889	the basis of four motifs	881:904	All 16 O-glycosylation sites are explained on the basis of four motifs.
8286855	0	24	theme	Glycosylation	0:12	arg1	sites					14:18	Glycosylation sites	0:18	Glycosylation sites	0:18	Glycosylation sites identified by solid-phase Edman degradation: O-linked glycosylation motifs on human glycophorin A.
8286855	4	25	from	Ser1	641:644	arg1	GpA					687:689	GpA	687:689	GpA	687:689	Carbohydrate was absent on Ser1, Ser14, Ser15, Ser23, Thr28 and Thr58 in GpA.
8286855	5	26	theme	potential	802:810	arg1	sites					828:832	potential O-glycosylation sites	802:832	potential O-glycosylation sites	802:832	We propose that the glycosyltransferases present in erythrocytes recognize specific flanking sequences around potential O-glycosylation sites.
8286855	1	27	theme	MN	274:275	arg1	antigens					289:296	the MN blood group antigens	270:296	the MN blood group antigens	270:296	The human red blood cell sialoglycoprotein, glycophorin A (GpA), contains a 'mucin-like' extensively O-glycosylated extracellular domain which carries the MN blood group antigens.
8286855	2	28	theme	N-glycosylation	540:554	arg1	O-glycosylation					328:342	O-glycosylation	328:342	O-glycosylation	328:342	We have revised the sites of O-glycosylation in the extracellular domain of GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues, as well as the single N-glycosylation site.
8286855	2	28	theme	N-glycosylation	540:554	arg1	site					556:559	the single N-glycosylation site	529:559	the single N-glycosylation site	529:559	We have revised the sites of O-glycosylation in the extracellular domain of GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues, as well as the single N-glycosylation site.
8286855	2	29	gly	O-glycosylated	481:494	arg1	Ser					496:498	O-glycosylated Ser	481:498	O-glycosylated Ser	481:498	We have revised the sites of O-glycosylation in the extracellular domain of GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues, as well as the single N-glycosylation site.
8286855	5	30	theme	O-glycosylation	812:826	arg1	sites					828:832	potential O-glycosylation sites	802:832	potential O-glycosylation sites	802:832	We propose that the glycosyltransferases present in erythrocytes recognize specific flanking sequences around potential O-glycosylation sites.
8286855	1	31	theme	blood	277:281	arg1	antigens					289:296	the MN blood group antigens	270:296	the MN blood group antigens	270:296	The human red blood cell sialoglycoprotein, glycophorin A (GpA), contains a 'mucin-like' extensively O-glycosylated extracellular domain which carries the MN blood group antigens.
8286855	2	32	theme	extracellular	351:363	arg1	GpA					375:377	GpA	375:377	GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues	375:515	We have revised the sites of O-glycosylation in the extracellular domain of GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues, as well as the single N-glycosylation site.
8286855	2	32	theme	extracellular	351:363	arg1	domain					365:370	the extracellular domain	347:370	the extracellular domain of GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues	347:515	We have revised the sites of O-glycosylation in the extracellular domain of GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues, as well as the single N-glycosylation site.
8286855	2	33	theme	O-glycosylation	328:342	arg1	sites					319:323	the sites	315:323	the sites of O-glycosylation in the extracellular domain of GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues	315:515	We have revised the sites of O-glycosylation in the extracellular domain of GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues, as well as the single N-glycosylation site.
8286855	2	33	theme	O-glycosylation	328:342	arg1	O-glycosylation					328:342	O-glycosylation	328:342	O-glycosylation	328:342	We have revised the sites of O-glycosylation in the extracellular domain of GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues, as well as the single N-glycosylation site.
8286855	2	33	theme	O-glycosylation	328:342	arg1	site					556:559	the single N-glycosylation site	529:559	the single N-glycosylation site	529:559	We have revised the sites of O-glycosylation in the extracellular domain of GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues, as well as the single N-glycosylation site.
8286855	6	34	gly	O-glycosylation	842:856	arg2	sites					858:862	All 16 O-glycosylation sites	835:862	All 16 O-glycosylation sites	835:862	All 16 O-glycosylation sites are explained on the basis of four motifs.
8286855	6	34	gly	O-glycosylation	842:856	arg2	16					839:840	16	839:840	16	839:840	All 16 O-glycosylation sites are explained on the basis of four motifs.
8286855	2	35	theme	Edman	404:408	arg1	degradation					410:420	automated solid-phase Edman degradation	382:420	automated solid-phase Edman degradation	382:420	We have revised the sites of O-glycosylation in the extracellular domain of GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues, as well as the single N-glycosylation site.
8286855	0	36	theme	Edman	46:50	arg1	degradation					52:62	solid-phase Edman degradation	34:62	solid-phase Edman degradation	34:62	Glycosylation sites identified by solid-phase Edman degradation: O-linked glycosylation motifs on human glycophorin A.
8286855	1	37	theme	group	283:287	arg1	antigens					289:296	the MN blood group antigens	270:296	the MN blood group antigens	270:296	The human red blood cell sialoglycoprotein, glycophorin A (GpA), contains a 'mucin-like' extensively O-glycosylated extracellular domain which carries the MN blood group antigens.
8286855	2	38	gly	O-glycosylation	328:342	arg1	GpA					375:377	GpA	375:377	GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues	375:515	We have revised the sites of O-glycosylation in the extracellular domain of GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues, as well as the single N-glycosylation site.
8286855	2	38	gly	O-glycosylation	328:342	arg1	domain					365:370	the extracellular domain	347:370	the extracellular domain of GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues	347:515	We have revised the sites of O-glycosylation in the extracellular domain of GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues, as well as the single N-glycosylation site.
8286855	2	38	gly	O-glycosylation	328:342	arg2	O-glycosylation					328:342	O-glycosylation	328:342	O-glycosylation	328:342	We have revised the sites of O-glycosylation in the extracellular domain of GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues, as well as the single N-glycosylation site.
8286855	2	38	gly	O-glycosylation	328:342	arg2	site					556:559	the single N-glycosylation site	529:559	the single N-glycosylation site	529:559	We have revised the sites of O-glycosylation in the extracellular domain of GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues, as well as the single N-glycosylation site.
8286855	2	38	gly	O-glycosylation	328:342	arg2	sites					319:323	the sites	315:323	the sites of O-glycosylation in the extracellular domain of GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues	315:515	We have revised the sites of O-glycosylation in the extracellular domain of GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues, as well as the single N-glycosylation site.
8286855	0	39	from	motifs	88:93	arg1	A					116:116	human glycophorin A	98:116	human glycophorin A	98:116	Glycosylation sites identified by solid-phase Edman degradation: O-linked glycosylation motifs on human glycophorin A.
8286855	3	40	theme	O-linked	582:589	arg1	sites					591:595	16 O-linked sites	579:595	16 O-linked sites	579:595	One N-linked and 16 O-linked sites were identified.
8286855	2	41	theme	solid-phase	392:402	arg1	degradation					410:420	automated solid-phase Edman degradation	382:420	automated solid-phase Edman degradation	382:420	We have revised the sites of O-glycosylation in the extracellular domain of GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues, as well as the single N-glycosylation site.
8286855	0	42	theme	solid-phase	34:44	arg1	degradation					52:62	solid-phase Edman degradation	34:62	solid-phase Edman degradation	34:62	Glycosylation sites identified by solid-phase Edman degradation: O-linked glycosylation motifs on human glycophorin A.
8286855	1	43	dep	mucin-like	196:205	arg1	O-glycosylated					220:233	O-glycosylated	220:233	O-glycosylated	220:233	The human red blood cell sialoglycoprotein, glycophorin A (GpA), contains a 'mucin-like' extensively O-glycosylated extracellular domain which carries the MN blood group antigens.
8286855	2	44	theme	automated	382:390	arg1	degradation					410:420	automated solid-phase Edman degradation	382:420	automated solid-phase Edman degradation	382:420	We have revised the sites of O-glycosylation in the extracellular domain of GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues, as well as the single N-glycosylation site.
8286855	3	45	link	O-linked	582:589	arg1	sites					591:595	16 O-linked sites	579:595	16 O-linked sites	579:595	One N-linked and 16 O-linked sites were identified.
8286855	1	46	gly	sialoglycoprotein	144:160	arg1	sialoglycoprotein					144:160	The human red blood cell sialoglycoprotein	119:160	The human red blood cell sialoglycoprotein	119:160	The human red blood cell sialoglycoprotein, glycophorin A (GpA), contains a 'mucin-like' extensively O-glycosylated extracellular domain which carries the MN blood group antigens.
8286855	1	46	gly	sialoglycoprotein	144:160	arg1	A					175:175	glycophorin A	163:175	glycophorin A (GpA)	163:181	The human red blood cell sialoglycoprotein, glycophorin A (GpA), contains a 'mucin-like' extensively O-glycosylated extracellular domain which carries the MN blood group antigens.
8286855	6	47	theme	O-glycosylation	842:856	arg1	sites					858:862	All 16 O-glycosylation sites	835:862	All 16 O-glycosylation sites	835:862	All 16 O-glycosylation sites are explained on the basis of four motifs.
8286855	5	48	gly	O-glycosylation	812:826	arg2	sites					828:832	potential O-glycosylation sites	802:832	potential O-glycosylation sites	802:832	We propose that the glycosyltransferases present in erythrocytes recognize specific flanking sequences around potential O-glycosylation sites.
8286855	9	49	gly	glycosylation	1234:1246	arg1	GpA					1315:1317	GpA	1315:1317	GpA	1315:1317	These simple rules explain the glycosylation (or lack of it) on 21 of 22 Ser/Thr in the extracellular domain of GpA.
8286855	9	49	gly	glycosylation	1234:1246	arg1	domain					1305:1310	the extracellular domain	1287:1310	the extracellular domain of GpA	1287:1317	These simple rules explain the glycosylation (or lack of it) on 21 of 22 Ser/Thr in the extracellular domain of GpA.
8286855	9	49	gly	glycosylation	1234:1246	arg1	Ser/Thr					1276:1282	21 of 22 Ser/Thr	1267:1282	21 of 22 Ser/Thr	1267:1282	These simple rules explain the glycosylation (or lack of it) on 21 of 22 Ser/Thr in the extracellular domain of GpA.
8286855	5	50	theme	flanking	776:783	arg1	sequences					785:793	specific flanking sequences	767:793	specific flanking sequences around potential O-glycosylation sites	767:832	We propose that the glycosyltransferases present in erythrocytes recognize specific flanking sequences around potential O-glycosylation sites.
8286855	5	51	from	present	733:739	arg1	erythrocytes					744:755	erythrocytes	744:755	erythrocytes	744:755	We propose that the glycosyltransferases present in erythrocytes recognize specific flanking sequences around potential O-glycosylation sites.
8286855	1	52	theme	human	123:127	arg1	cell					139:142	human red blood cell	123:142	The human red blood cell sialoglycoprotein	119:160	The human red blood cell sialoglycoprotein, glycophorin A (GpA), contains a 'mucin-like' extensively O-glycosylated extracellular domain which carries the MN blood group antigens.
8286855	7	53	dep	Thr-glycosylation	940:956	arg1	Xaa-Xaa-Thr-Xaa					1051:1065	Xaa-Xaa-Thr-Xaa	1051:1065	Thr-glycosylation: Xaa-Pro-Xaa-Xaa where at least one Xaa = Thr; Thr-Xaa-Xaa-Xaa where at least one Xaa = Thr; Xaa-Xaa-Thr-Xaa where at least one X = Arg or Lys	940:1099	Three motifs are associated with Thr-glycosylation: Xaa-Pro-Xaa-Xaa where at least one Xaa = Thr; Thr-Xaa-Xaa-Xaa where at least one Xaa = Thr; Xaa-Xaa-Thr-Xaa where at least one X = Arg or Lys.
8286855	7	53	dep	Thr-glycosylation	940:956	arg1	Xaa-Pro-Xaa-Xaa					959:973	Xaa-Pro-Xaa-Xaa	959:973	Thr-glycosylation: Xaa-Pro-Xaa-Xaa where at least one Xaa = Thr; Thr-Xaa-Xaa-Xaa where at least one Xaa = Thr; Xaa-Xaa-Thr-Xaa where at least one X = Arg or Lys	940:1099	Three motifs are associated with Thr-glycosylation: Xaa-Pro-Xaa-Xaa where at least one Xaa = Thr; Thr-Xaa-Xaa-Xaa where at least one Xaa = Thr; Xaa-Xaa-Thr-Xaa where at least one X = Arg or Lys.
8286855	7	53	dep	Thr-glycosylation	940:956	arg1	Thr-Xaa-Xaa-Xaa					1005:1019	Thr-Xaa-Xaa-Xaa	1005:1019	Thr-glycosylation: Xaa-Pro-Xaa-Xaa where at least one Xaa = Thr; Thr-Xaa-Xaa-Xaa where at least one Xaa = Thr; Xaa-Xaa-Thr-Xaa where at least one X = Arg or Lys	940:1099	Three motifs are associated with Thr-glycosylation: Xaa-Pro-Xaa-Xaa where at least one Xaa = Thr; Thr-Xaa-Xaa-Xaa where at least one Xaa = Thr; Xaa-Xaa-Thr-Xaa where at least one X = Arg or Lys.
8286855	9	54	theme	extracellular	1291:1303	arg1	GpA					1315:1317	GpA	1315:1317	GpA	1315:1317	These simple rules explain the glycosylation (or lack of it) on 21 of 22 Ser/Thr in the extracellular domain of GpA.
8286855	9	54	theme	extracellular	1291:1303	arg1	domain					1305:1310	the extracellular domain	1287:1310	the extracellular domain of GpA	1287:1317	These simple rules explain the glycosylation (or lack of it) on 21 of 22 Ser/Thr in the extracellular domain of GpA.
8286855	9	55	theme	simple	1209:1214	arg1	rules					1216:1220	These simple rules	1203:1220	These simple rules	1203:1220	These simple rules explain the glycosylation (or lack of it) on 21 of 22 Ser/Thr in the extracellular domain of GpA.
8286855	1	56	contain	carries	262:268	arg1	domain					249:254	a 'mucin-like' extensively O-glycosylated extracellular domain	193:254	a 'mucin-like' extensively O-glycosylated extracellular domain which carries the MN blood group antigens	193:296	The human red blood cell sialoglycoprotein, glycophorin A (GpA), contains a 'mucin-like' extensively O-glycosylated extracellular domain which carries the MN blood group antigens.
8286855	1	56	contain	carries	262:268	arg2	antigens					289:296	the MN blood group antigens	270:296	the MN blood group antigens	270:296	The human red blood cell sialoglycoprotein, glycophorin A (GpA), contains a 'mucin-like' extensively O-glycosylated extracellular domain which carries the MN blood group antigens.
8286855	0	57	link	O-linked	65:72	arg1	motifs					88:93	O-linked glycosylation motifs	65:93	O-linked glycosylation motifs on human glycophorin A	65:116	Glycosylation sites identified by solid-phase Edman degradation: O-linked glycosylation motifs on human glycophorin A.
8286855	1	58	theme	red	129:131	arg1	cell					139:142	human red blood cell	123:142	The human red blood cell sialoglycoprotein	119:160	The human red blood cell sialoglycoprotein, glycophorin A (GpA), contains a 'mucin-like' extensively O-glycosylated extracellular domain which carries the MN blood group antigens.
8286855	1	59	theme	mucin-like	196:205	arg1	domain					249:254	a 'mucin-like' extensively O-glycosylated extracellular domain	193:254	a 'mucin-like' extensively O-glycosylated extracellular domain which carries the MN blood group antigens	193:296	The human red blood cell sialoglycoprotein, glycophorin A (GpA), contains a 'mucin-like' extensively O-glycosylated extracellular domain which carries the MN blood group antigens.
8286855	5	60	attach	present	733:739	arg2	glycosyltransferases					712:731	the glycosyltransferases	708:731	the glycosyltransferases present in erythrocytes	708:755	We propose that the glycosyltransferases present in erythrocytes recognize specific flanking sequences around potential O-glycosylation sites.
8286855	5	60	attach	present	733:739	arg1	erythrocytes					744:755	erythrocytes	744:755	erythrocytes	744:755	We propose that the glycosyltransferases present in erythrocytes recognize specific flanking sequences around potential O-glycosylation sites.
8286855	1	61	contain	contains	184:191	arg1	sialoglycoprotein					144:160	The human red blood cell sialoglycoprotein	119:160	The human red blood cell sialoglycoprotein	119:160	The human red blood cell sialoglycoprotein, glycophorin A (GpA), contains a 'mucin-like' extensively O-glycosylated extracellular domain which carries the MN blood group antigens.
8286855	1	61	contain	contains	184:191	arg2	domain					249:254	a 'mucin-like' extensively O-glycosylated extracellular domain	193:254	a 'mucin-like' extensively O-glycosylated extracellular domain which carries the MN blood group antigens	193:296	The human red blood cell sialoglycoprotein, glycophorin A (GpA), contains a 'mucin-like' extensively O-glycosylated extracellular domain which carries the MN blood group antigens.
8286855	1	61	contain	contains	184:191	arg1	A					175:175	glycophorin A	163:175	glycophorin A (GpA)	163:181	The human red blood cell sialoglycoprotein, glycophorin A (GpA), contains a 'mucin-like' extensively O-glycosylated extracellular domain which carries the MN blood group antigens.
8286855	1	62	theme	blood	133:137	arg1	cell					139:142	human red blood cell	123:142	The human red blood cell sialoglycoprotein	119:160	The human red blood cell sialoglycoprotein, glycophorin A (GpA), contains a 'mucin-like' extensively O-glycosylated extracellular domain which carries the MN blood group antigens.
8286855	4	63	from	Thr58	678:682	arg1	GpA					687:689	GpA	687:689	GpA	687:689	Carbohydrate was absent on Ser1, Ser14, Ser15, Ser23, Thr28 and Thr58 in GpA.
8286855	0	64	theme	glycosylation	74:86	arg1	motifs					88:93	O-linked glycosylation motifs	65:93	O-linked glycosylation motifs on human glycophorin A	65:116	Glycosylation sites identified by solid-phase Edman degradation: O-linked glycosylation motifs on human glycophorin A.
8286855	1	65	theme	cell	139:142	arg1	sialoglycoprotein					144:160	The human red blood cell sialoglycoprotein	119:160	The human red blood cell sialoglycoprotein	119:160	The human red blood cell sialoglycoprotein, glycophorin A (GpA), contains a 'mucin-like' extensively O-glycosylated extracellular domain which carries the MN blood group antigens.
8286855	1	65	theme	cell	139:142	arg1	A					175:175	glycophorin A	163:175	glycophorin A (GpA)	163:181	The human red blood cell sialoglycoprotein, glycophorin A (GpA), contains a 'mucin-like' extensively O-glycosylated extracellular domain which carries the MN blood group antigens.
8286855	9	66	theme	GpA	1315:1317	arg1	GpA					1315:1317	GpA	1315:1317	GpA	1315:1317	These simple rules explain the glycosylation (or lack of it) on 21 of 22 Ser/Thr in the extracellular domain of GpA.
8286855	9	66	theme	GpA	1315:1317	arg1	domain					1305:1310	the extracellular domain	1287:1310	the extracellular domain of GpA	1287:1317	These simple rules explain the glycosylation (or lack of it) on 21 of 22 Ser/Thr in the extracellular domain of GpA.
8286855	0	67	theme	O-linked	65:72	arg1	motifs					88:93	O-linked glycosylation motifs	65:93	O-linked glycosylation motifs on human glycophorin A	65:116	Glycosylation sites identified by solid-phase Edman degradation: O-linked glycosylation motifs on human glycophorin A.
8286855	2	68	gly	N-glycosylation	540:554	arg2	site					556:559	the single N-glycosylation site	529:559	the single N-glycosylation site	529:559	We have revised the sites of O-glycosylation in the extracellular domain of GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues, as well as the single N-glycosylation site.
8286855	2	68	gly	N-glycosylation	540:554	arg1	O-glycosylation					328:342	O-glycosylation	328:342	O-glycosylation	328:342	We have revised the sites of O-glycosylation in the extracellular domain of GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues, as well as the single N-glycosylation site.
8286855	2	68	gly	N-glycosylation	540:554	arg2	O-glycosylation					328:342	O-glycosylation	328:342	O-glycosylation	328:342	We have revised the sites of O-glycosylation in the extracellular domain of GpA by automated solid-phase Edman degradation, which allowed positive identification and quantitation of O-glycosylated Ser and Thr residues, as well as the single N-glycosylation site.
8286855	4	69	from	Thr28	668:672	arg1	GpA					687:689	GpA	687:689	GpA	687:689	Carbohydrate was absent on Ser1, Ser14, Ser15, Ser23, Thr28 and Thr58 in GpA.
8286855	8	70	theme	fourth	1106:1111	arg1	motif					1113:1117	The fourth motif	1102:1117	The fourth motif	1102:1117	The fourth motif is associated with Ser-glycosylation: Ser-Xaa-Xaa-Xaa where at least one Xaa = Ser.
24256146	1	0	theme	cell	150:153	arg1	biology					155:161	the cell biology	146:161	the cell biology of protein O-GlcNAcylation	146:188	Inhibitors of OGT (O-GlcNAc transferase) are valuable tools to study the cell biology of protein O-GlcNAcylation.
24256146	3	1	theme	micromolar	495:504	arg1	affinity					506:513	micromolar affinity	495:513	micromolar affinity	495:513	Goblin1 co-crystallizes with OGT, revealing an ordered C₃ linker and retained substrate-binding modes, and binds the enzyme with micromolar affinity, inhibiting glycosyltransfer on to protein and peptide substrates.
24256146	2	2	theme	peptide	281:287	arg1	VTPVSTA					289:295	the peptide VTPVSTA	277:295	the peptide VTPVSTA	277:295	We report OGT bisubstrate-linked inhibitors (goblins) in which the acceptor serine in the peptide VTPVSTA is covalently linked to UDP, eliminating the GlcNAc pyranoside ring.
24256146	2	3	theme	GlcNAc	342:347	arg1	ring					360:363	the GlcNAc pyranoside ring	338:363	the GlcNAc pyranoside ring	338:363	We report OGT bisubstrate-linked inhibitors (goblins) in which the acceptor serine in the peptide VTPVSTA is covalently linked to UDP, eliminating the GlcNAc pyranoside ring.
24256146	3	4	theme	ordered	413:419	arg1	linker					424:429	an ordered C₃ linker	410:429	an ordered C₃ linker	410:429	Goblin1 co-crystallizes with OGT, revealing an ordered C₃ linker and retained substrate-binding modes, and binds the enzyme with micromolar affinity, inhibiting glycosyltransfer on to protein and peptide substrates.
24256146	1	5	theme	OGT	91:93	arg1	tools					131:135	valuable tools	122:135	valuable tools to study the cell biology of protein O-GlcNAcylation	122:188	Inhibitors of OGT (O-GlcNAc transferase) are valuable tools to study the cell biology of protein O-GlcNAcylation.
24256146	1	5	theme	OGT	91:93	arg1	transferase					105:115	O-GlcNAc transferase	96:115	O-GlcNAc transferase	96:115	Inhibitors of OGT (O-GlcNAc transferase) are valuable tools to study the cell biology of protein O-GlcNAcylation.
24256146	1	5	theme	OGT	91:93	arg1	Inhibitors					77:86	Inhibitors	77:86	Inhibitors of OGT (O-GlcNAc transferase)	77:116	Inhibitors of OGT (O-GlcNAc transferase) are valuable tools to study the cell biology of protein O-GlcNAcylation.
24256146	1	6	theme	protein	166:172	arg1	O-GlcNAcylation					174:188	protein O-GlcNAcylation	166:188	protein O-GlcNAcylation	166:188	Inhibitors of OGT (O-GlcNAc transferase) are valuable tools to study the cell biology of protein O-GlcNAcylation.
24256146	3	7	theme	peptide	562:568	arg1	substrates					570:579	protein and peptide substrates	550:579	substrates	570:579	Goblin1 co-crystallizes with OGT, revealing an ordered C₃ linker and retained substrate-binding modes, and binds the enzyme with micromolar affinity, inhibiting glycosyltransfer on to protein and peptide substrates.
24256146	1	8	theme	O-GlcNAcylation	174:188	arg1	biology					155:161	the cell biology	146:161	the cell biology of protein O-GlcNAcylation	146:188	Inhibitors of OGT (O-GlcNAc transferase) are valuable tools to study the cell biology of protein O-GlcNAcylation.
24256146	0	9	theme	Bisubstrate	0:10	arg1	UDP-peptide					12:22	Bisubstrate UDP-peptide	0:22	Bisubstrate UDP-peptide	0:22	Bisubstrate UDP-peptide conjugates as human O-GlcNAc transferase inhibitors.
24256146	3	10	with	enzyme	483:488	arg1	affinity					506:513	micromolar affinity	495:513	micromolar affinity	495:513	Goblin1 co-crystallizes with OGT, revealing an ordered C₃ linker and retained substrate-binding modes, and binds the enzyme with micromolar affinity, inhibiting glycosyltransfer on to protein and peptide substrates.
24256146	1	11	theme	O-GlcNAc	96:103	arg1	transferase					105:115	O-GlcNAc transferase	96:115	O-GlcNAc transferase	96:115	Inhibitors of OGT (O-GlcNAc transferase) are valuable tools to study the cell biology of protein O-GlcNAcylation.
24256146	1	11	theme	O-GlcNAc	96:103	arg1	Inhibitors					77:86	Inhibitors	77:86	Inhibitors of OGT (O-GlcNAc transferase)	77:116	Inhibitors of OGT (O-GlcNAc transferase) are valuable tools to study the cell biology of protein O-GlcNAcylation.
24256146	3	12	theme	C₃	421:422	arg1	linker					424:429	an ordered C₃ linker	410:429	an ordered C₃ linker	410:429	Goblin1 co-crystallizes with OGT, revealing an ordered C₃ linker and retained substrate-binding modes, and binds the enzyme with micromolar affinity, inhibiting glycosyltransfer on to protein and peptide substrates.
24256146	2	13	attach	linked	311:316	arg3	inhibitors					224:233	OGT bisubstrate-linked inhibitors	201:233	OGT bisubstrate-linked inhibitors (goblins) in which the acceptor serine in the peptide VTPVSTA is covalently linked to UDP, eliminating the GlcNAc pyranoside ring	201:363	We report OGT bisubstrate-linked inhibitors (goblins) in which the acceptor serine in the peptide VTPVSTA is covalently linked to UDP, eliminating the GlcNAc pyranoside ring.
24256146	2	13	attach	linked	311:316	arg2	serine					267:272	the acceptor serine	254:272	the acceptor serine in the peptide VTPVSTA	254:295	We report OGT bisubstrate-linked inhibitors (goblins) in which the acceptor serine in the peptide VTPVSTA is covalently linked to UDP, eliminating the GlcNAc pyranoside ring.
24256146	2	13	attach	linked	311:316	arg3	goblins					236:242	goblins	236:242	goblins	236:242	We report OGT bisubstrate-linked inhibitors (goblins) in which the acceptor serine in the peptide VTPVSTA is covalently linked to UDP, eliminating the GlcNAc pyranoside ring.
24256146	2	13	attach	linked	311:316	arg1	UDP					321:323	UDP	321:323	UDP	321:323	We report OGT bisubstrate-linked inhibitors (goblins) in which the acceptor serine in the peptide VTPVSTA is covalently linked to UDP, eliminating the GlcNAc pyranoside ring.
24256146	3	14	theme	protein	550:556	arg1	substrates					570:579	protein and peptide substrates	550:579	substrates	570:579	Goblin1 co-crystallizes with OGT, revealing an ordered C₃ linker and retained substrate-binding modes, and binds the enzyme with micromolar affinity, inhibiting glycosyltransfer on to protein and peptide substrates.
24256146	0	15	theme	O-GlcNAc	44:51	arg1	inhibitors					65:74	human O-GlcNAc transferase inhibitors	38:74	human O-GlcNAc transferase inhibitors	38:74	Bisubstrate UDP-peptide conjugates as human O-GlcNAc transferase inhibitors.
24256146	3	16	theme	retained	435:442	arg1	modes					462:466	retained substrate-binding modes	435:466	retained substrate-binding modes	435:466	Goblin1 co-crystallizes with OGT, revealing an ordered C₃ linker and retained substrate-binding modes, and binds the enzyme with micromolar affinity, inhibiting glycosyltransfer on to protein and peptide substrates.
24256146	2	17	link	bisubstrate-linked	205:222	arg1	goblins					236:242	goblins	236:242	goblins	236:242	We report OGT bisubstrate-linked inhibitors (goblins) in which the acceptor serine in the peptide VTPVSTA is covalently linked to UDP, eliminating the GlcNAc pyranoside ring.
24256146	2	17	link	bisubstrate-linked	205:222	arg1	inhibitors					224:233	OGT bisubstrate-linked inhibitors	201:233	OGT bisubstrate-linked inhibitors (goblins) in which the acceptor serine in the peptide VTPVSTA is covalently linked to UDP, eliminating the GlcNAc pyranoside ring	201:363	We report OGT bisubstrate-linked inhibitors (goblins) in which the acceptor serine in the peptide VTPVSTA is covalently linked to UDP, eliminating the GlcNAc pyranoside ring.
24256146	0	18	theme	human	38:42	arg1	inhibitors					65:74	human O-GlcNAc transferase inhibitors	38:74	human O-GlcNAc transferase inhibitors	38:74	Bisubstrate UDP-peptide conjugates as human O-GlcNAc transferase inhibitors.
24256146	3	19	theme	substrate-binding	444:460	arg1	modes					462:466	retained substrate-binding modes	435:466	retained substrate-binding modes	435:466	Goblin1 co-crystallizes with OGT, revealing an ordered C₃ linker and retained substrate-binding modes, and binds the enzyme with micromolar affinity, inhibiting glycosyltransfer on to protein and peptide substrates.
24256146	0	20	theme	transferase	53:63	arg1	inhibitors					65:74	human O-GlcNAc transferase inhibitors	38:74	human O-GlcNAc transferase inhibitors	38:74	Bisubstrate UDP-peptide conjugates as human O-GlcNAc transferase inhibitors.
24256146	2	21	theme	bisubstrate-linked	205:222	arg1	goblins					236:242	goblins	236:242	goblins	236:242	We report OGT bisubstrate-linked inhibitors (goblins) in which the acceptor serine in the peptide VTPVSTA is covalently linked to UDP, eliminating the GlcNAc pyranoside ring.
24256146	2	21	theme	bisubstrate-linked	205:222	arg1	inhibitors					224:233	OGT bisubstrate-linked inhibitors	201:233	OGT bisubstrate-linked inhibitors (goblins) in which the acceptor serine in the peptide VTPVSTA is covalently linked to UDP, eliminating the GlcNAc pyranoside ring	201:363	We report OGT bisubstrate-linked inhibitors (goblins) in which the acceptor serine in the peptide VTPVSTA is covalently linked to UDP, eliminating the GlcNAc pyranoside ring.
24256146	1	22	theme	valuable	122:129	arg1	tools					131:135	valuable tools	122:135	valuable tools to study the cell biology of protein O-GlcNAcylation	122:188	Inhibitors of OGT (O-GlcNAc transferase) are valuable tools to study the cell biology of protein O-GlcNAcylation.
24256146	1	22	theme	valuable	122:129	arg1	Inhibitors					77:86	Inhibitors	77:86	Inhibitors of OGT (O-GlcNAc transferase)	77:116	Inhibitors of OGT (O-GlcNAc transferase) are valuable tools to study the cell biology of protein O-GlcNAcylation.
24256146	2	23	theme	OGT	201:203	arg1	goblins					236:242	goblins	236:242	goblins	236:242	We report OGT bisubstrate-linked inhibitors (goblins) in which the acceptor serine in the peptide VTPVSTA is covalently linked to UDP, eliminating the GlcNAc pyranoside ring.
24256146	2	23	theme	OGT	201:203	arg1	inhibitors					224:233	OGT bisubstrate-linked inhibitors	201:233	OGT bisubstrate-linked inhibitors (goblins) in which the acceptor serine in the peptide VTPVSTA is covalently linked to UDP, eliminating the GlcNAc pyranoside ring	201:363	We report OGT bisubstrate-linked inhibitors (goblins) in which the acceptor serine in the peptide VTPVSTA is covalently linked to UDP, eliminating the GlcNAc pyranoside ring.
24256146	2	24	theme	acceptor	258:265	arg1	serine					267:272	the acceptor serine	254:272	the acceptor serine in the peptide VTPVSTA	254:295	We report OGT bisubstrate-linked inhibitors (goblins) in which the acceptor serine in the peptide VTPVSTA is covalently linked to UDP, eliminating the GlcNAc pyranoside ring.
24256146	2	25	from	serine	267:272	arg1	VTPVSTA					289:295	the peptide VTPVSTA	277:295	the peptide VTPVSTA	277:295	We report OGT bisubstrate-linked inhibitors (goblins) in which the acceptor serine in the peptide VTPVSTA is covalently linked to UDP, eliminating the GlcNAc pyranoside ring.
24256146	2	26	theme	pyranoside	349:358	arg1	ring					360:363	the GlcNAc pyranoside ring	338:363	the GlcNAc pyranoside ring	338:363	We report OGT bisubstrate-linked inhibitors (goblins) in which the acceptor serine in the peptide VTPVSTA is covalently linked to UDP, eliminating the GlcNAc pyranoside ring.
16622833	6	0	theme	triantennary	914:925	arg1	structures					927:936	triantennary structures	914:936	triantennary structures	914:936	Only negligible amounts of triantennary structures were identified attached to N70, and exclusively diantennary structures were present on site N271 in each of the isoforms analyzed.
16622833	5	1	theme	antennae	707:714	arg1	number					697:702	the number	693:702	the number of antennae and hence sialic acids on glycosylation site N107	693:764	The variability of the number of antennae and hence sialic acids on glycosylation site N107, which even contained minute amounts of tetraantennary structures, emerged as a major cause for the IEF pattern of A1PI.
16622833	6	2	theme	diantennary	987:997	arg1	structures					999:1008	exclusively diantennary structures	975:1008	exclusively diantennary structures	975:1008	Only negligible amounts of triantennary structures were identified attached to N70, and exclusively diantennary structures were present on site N271 in each of the isoforms analyzed.
16622833	6	3	dep	identified	943:952	arg1	attached					954:961	attached	954:961	attached to N70	954:968	Only negligible amounts of triantennary structures were identified attached to N70, and exclusively diantennary structures were present on site N271 in each of the isoforms analyzed.
16622833	4	4	theme	cysteine	603:610	arg1	residue					612:618	The single cysteine residue	592:618	The single cysteine residue of A1PI	592:626	The single cysteine residue of A1PI formed a disulfide bridge with free cysteine.
16622833	4	4	theme	cysteine	603:610	arg1	A1PI					623:626	A1PI	623:626	A1PI	623:626	The single cysteine residue of A1PI formed a disulfide bridge with free cysteine.
16622833	7	5	theme	asialoglycans	1401:1413	arg1	2-D-HPLC					1373:1380	2-D-HPLC	1373:1380	2-D-HPLC of pyridylaminated asialoglycans	1373:1413	Exoglycosidase digests revealed alpha2,6-linked neuraminic acids on diantennary N-glycans, and triantennary contained additionally one single alpha2,3-neuraminic acid per N-glycan, which, together with a fucose, formed a sialyl Lewis X determinant on the beta1,4-linked N-acetylglucosamine, as shown by 2-D-HPLC of pyridylaminated asialoglycans.
16622833	6	6	theme	structures	927:936	arg1	amounts					903:909	Only negligible amounts	887:909	Only negligible amounts of triantennary structures	887:936	Only negligible amounts of triantennary structures were identified attached to N70, and exclusively diantennary structures were present on site N271 in each of the isoforms analyzed.
16622833	6	6	theme	structures	927:936	arg1	structures					927:936	triantennary structures	914:936	triantennary structures	914:936	Only negligible amounts of triantennary structures were identified attached to N70, and exclusively diantennary structures were present on site N271 in each of the isoforms analyzed.
16622833	1	7	theme	important	169:177	arg1	glycoprotein					140:151	a well-known glycoprotein	127:151	a well-known glycoprotein in human plasma important for the protection of tissues from proteolytic enzymes	127:232	Human alpha1-antitrypsin (A1PI) is a well-known glycoprotein in human plasma important for the protection of tissues from proteolytic enzymes.
16622833	1	7	theme	important	169:177	arg1	alpha1-antitrypsin					98:115	Human alpha1-antitrypsin	92:115	Human alpha1-antitrypsin (A1PI)	92:122	Human alpha1-antitrypsin (A1PI) is a well-known glycoprotein in human plasma important for the protection of tissues from proteolytic enzymes.
16622833	4	8	theme	single	596:601	arg1	residue					612:618	The single cysteine residue	592:618	The single cysteine residue of A1PI	592:626	The single cysteine residue of A1PI formed a disulfide bridge with free cysteine.
16622833	4	8	theme	single	596:601	arg1	A1PI					623:626	A1PI	623:626	A1PI	623:626	The single cysteine residue of A1PI formed a disulfide bridge with free cysteine.
16622833	6	9	from	each	1039:1042	arg1	present					1015:1021	present	1015:1021	present	1015:1021	Only negligible amounts of triantennary structures were identified attached to N70, and exclusively diantennary structures were present on site N271 in each of the isoforms analyzed.
16622833	7	10	link	beta1,4-linked	1325:1338	arg1	N-acetylglucosamine					1340:1358	the beta1,4-linked N-acetylglucosamine	1321:1358	the beta1,4-linked N-acetylglucosamine	1321:1358	Exoglycosidase digests revealed alpha2,6-linked neuraminic acids on diantennary N-glycans, and triantennary contained additionally one single alpha2,3-neuraminic acid per N-glycan, which, together with a fucose, formed a sialyl Lewis X determinant on the beta1,4-linked N-acetylglucosamine, as shown by 2-D-HPLC of pyridylaminated asialoglycans.
16622833	7	11	theme	beta1,4-linked	1325:1338	arg1	N-acetylglucosamine					1340:1358	the beta1,4-linked N-acetylglucosamine	1321:1358	the beta1,4-linked N-acetylglucosamine	1321:1358	Exoglycosidase digests revealed alpha2,6-linked neuraminic acids on diantennary N-glycans, and triantennary contained additionally one single alpha2,3-neuraminic acid per N-glycan, which, together with a fucose, formed a sialyl Lewis X determinant on the beta1,4-linked N-acetylglucosamine, as shown by 2-D-HPLC of pyridylaminated asialoglycans.
16622833	5	12	theme	glycosylation	742:754	arg1	site					756:759	glycosylation site N107	742:764	glycosylation site N107	742:764	The variability of the number of antennae and hence sialic acids on glycosylation site N107, which even contained minute amounts of tetraantennary structures, emerged as a major cause for the IEF pattern of A1PI.
16622833	6	13	theme	negligible	892:901	arg1	amounts					903:909	Only negligible amounts	887:909	Only negligible amounts of triantennary structures	887:936	Only negligible amounts of triantennary structures were identified attached to N70, and exclusively diantennary structures were present on site N271 in each of the isoforms analyzed.
16622833	6	13	theme	negligible	892:901	arg1	structures					927:936	triantennary structures	914:936	triantennary structures	914:936	Only negligible amounts of triantennary structures were identified attached to N70, and exclusively diantennary structures were present on site N271 in each of the isoforms analyzed.
16622833	6	14	located	present	1015:1021	arg1	site					1026:1029	site N271	1026:1034	site N271	1026:1034	Only negligible amounts of triantennary structures were identified attached to N70, and exclusively diantennary structures were present on site N271 in each of the isoforms analyzed.
16622833	6	14	located	present	1015:1021	arg1	each					1039:1042	each	1039:1042	each	1039:1042	Only negligible amounts of triantennary structures were identified attached to N70, and exclusively diantennary structures were present on site N271 in each of the isoforms analyzed.
16622833	6	14	located	present	1015:1021	arg1	isoforms					1051:1058	the isoforms	1047:1058	the isoforms analyzed	1047:1067	Only negligible amounts of triantennary structures were identified attached to N70, and exclusively diantennary structures were present on site N271 in each of the isoforms analyzed.
16622833	6	14	located	present	1015:1021	arg2	structures					999:1008	exclusively diantennary structures	975:1008	exclusively diantennary structures	975:1008	Only negligible amounts of triantennary structures were identified attached to N70, and exclusively diantennary structures were present on site N271 in each of the isoforms analyzed.
16622833	6	15	attach	present	1015:1021	arg1	site					1026:1029	site N271	1026:1034	site N271	1026:1034	Only negligible amounts of triantennary structures were identified attached to N70, and exclusively diantennary structures were present on site N271 in each of the isoforms analyzed.
16622833	6	15	attach	present	1015:1021	arg1	each					1039:1042	each	1039:1042	each	1039:1042	Only negligible amounts of triantennary structures were identified attached to N70, and exclusively diantennary structures were present on site N271 in each of the isoforms analyzed.
16622833	6	15	attach	present	1015:1021	arg1	isoforms					1051:1058	the isoforms	1047:1058	the isoforms analyzed	1047:1067	Only negligible amounts of triantennary structures were identified attached to N70, and exclusively diantennary structures were present on site N271 in each of the isoforms analyzed.
16622833	6	15	attach	present	1015:1021	arg2	structures					999:1008	exclusively diantennary structures	975:1008	exclusively diantennary structures	975:1008	Only negligible amounts of triantennary structures were identified attached to N70, and exclusively diantennary structures were present on site N271 in each of the isoforms analyzed.
16622833	2	16	contain	contain	275:281	arg2	traces					336:341	diantennary N-glycans but also triantennary and even traces	283:341	diantennary N-glycans but also triantennary and even traces of tetraantennary structures leading to the typical IEF pattern observed for A1PI	283:423	The three N-glycosylation sites of A1PI contain diantennary N-glycans but also triantennary and even traces of tetraantennary structures leading to the typical IEF pattern observed for A1PI.
16622833	2	16	contain	contain	275:281	arg1	A1PI					270:273	A1PI	270:273	A1PI	270:273	The three N-glycosylation sites of A1PI contain diantennary N-glycans but also triantennary and even traces of tetraantennary structures leading to the typical IEF pattern observed for A1PI.
16622833	2	16	contain	contain	275:281	arg1	sites					261:265	The three N-glycosylation sites	235:265	The three N-glycosylation sites of A1PI	235:273	The three N-glycosylation sites of A1PI contain diantennary N-glycans but also triantennary and even traces of tetraantennary structures leading to the typical IEF pattern observed for A1PI.
16622833	7	17	theme	diantennary	1138:1148	arg1	N-glycans					1150:1158	diantennary N-glycans	1138:1158	diantennary N-glycans	1138:1158	Exoglycosidase digests revealed alpha2,6-linked neuraminic acids on diantennary N-glycans, and triantennary contained additionally one single alpha2,3-neuraminic acid per N-glycan, which, together with a fucose, formed a sialyl Lewis X determinant on the beta1,4-linked N-acetylglucosamine, as shown by 2-D-HPLC of pyridylaminated asialoglycans.
16622833	5	18	theme	major	846:850	arg1	cause					852:856	a major cause	844:856	a major cause for the IEF pattern of A1PI	844:884	The variability of the number of antennae and hence sialic acids on glycosylation site N107, which even contained minute amounts of tetraantennary structures, emerged as a major cause for the IEF pattern of A1PI.
16622833	5	19	theme	structures	821:830	arg1	amounts					795:801	minute amounts	788:801	minute amounts of tetraantennary structures	788:830	The variability of the number of antennae and hence sialic acids on glycosylation site N107, which even contained minute amounts of tetraantennary structures, emerged as a major cause for the IEF pattern of A1PI.
16622833	5	19	theme	structures	821:830	arg1	structures					821:830	tetraantennary structures	806:830	tetraantennary structures	806:830	The variability of the number of antennae and hence sialic acids on glycosylation site N107, which even contained minute amounts of tetraantennary structures, emerged as a major cause for the IEF pattern of A1PI.
16622833	2	20	theme	N-glycans	295:303	arg1	traces					336:341	diantennary N-glycans but also triantennary and even traces	283:341	diantennary N-glycans but also triantennary and even traces of tetraantennary structures leading to the typical IEF pattern observed for A1PI	283:423	The three N-glycosylation sites of A1PI contain diantennary N-glycans but also triantennary and even traces of tetraantennary structures leading to the typical IEF pattern observed for A1PI.
16622833	5	21	theme	tetraantennary	806:819	arg1	structures					821:830	tetraantennary structures	806:830	tetraantennary structures	806:830	The variability of the number of antennae and hence sialic acids on glycosylation site N107, which even contained minute amounts of tetraantennary structures, emerged as a major cause for the IEF pattern of A1PI.
16622833	8	22	gly	Fucosylation	1416:1427	arg1	structures					1444:1453	diantennary structures	1432:1453	diantennary structures	1432:1453	Fucosylation of diantennary structures was marginal and of the core alpha1,6 type.
16622833	5	23	theme	minute	788:793	arg1	amounts					795:801	minute amounts	788:801	minute amounts of tetraantennary structures	788:830	The variability of the number of antennae and hence sialic acids on glycosylation site N107, which even contained minute amounts of tetraantennary structures, emerged as a major cause for the IEF pattern of A1PI.
16622833	5	23	theme	minute	788:793	arg1	structures					821:830	tetraantennary structures	806:830	tetraantennary structures	806:830	The variability of the number of antennae and hence sialic acids on glycosylation site N107, which even contained minute amounts of tetraantennary structures, emerged as a major cause for the IEF pattern of A1PI.
16622833	1	24	theme	Human	92:96	arg1	glycoprotein					140:151	a well-known glycoprotein	127:151	a well-known glycoprotein in human plasma important for the protection of tissues from proteolytic enzymes	127:232	Human alpha1-antitrypsin (A1PI) is a well-known glycoprotein in human plasma important for the protection of tissues from proteolytic enzymes.
16622833	1	24	theme	Human	92:96	arg1	A1PI					118:121	A1PI	118:121	A1PI	118:121	Human alpha1-antitrypsin (A1PI) is a well-known glycoprotein in human plasma important for the protection of tissues from proteolytic enzymes.
16622833	1	24	theme	Human	92:96	arg1	alpha1-antitrypsin					98:115	Human alpha1-antitrypsin	92:115	Human alpha1-antitrypsin (A1PI)	92:122	Human alpha1-antitrypsin (A1PI) is a well-known glycoprotein in human plasma important for the protection of tissues from proteolytic enzymes.
16622833	5	25	theme	IEF	866:868	arg1	pattern					870:876	the IEF pattern	862:876	the IEF pattern of A1PI	862:884	The variability of the number of antennae and hence sialic acids on glycosylation site N107, which even contained minute amounts of tetraantennary structures, emerged as a major cause for the IEF pattern of A1PI.
16622833	0	26	theme	glyco-proteomic	14:28	arg1	analysis					30:37	Comprehensive glyco-proteomic analysis	0:37	Comprehensive glyco-proteomic analysis of human alpha1-antitrypsin and its charge isoforms	0:89	Comprehensive glyco-proteomic analysis of human alpha1-antitrypsin and its charge isoforms.
16622833	6	27	from	present	1015:1021	arg1	each					1039:1042	each	1039:1042	each	1039:1042	Only negligible amounts of triantennary structures were identified attached to N70, and exclusively diantennary structures were present on site N271 in each of the isoforms analyzed.
16622833	6	27	from	present	1015:1021	arg1	isoforms					1051:1058	the isoforms	1047:1058	the isoforms analyzed	1047:1067	Only negligible amounts of triantennary structures were identified attached to N70, and exclusively diantennary structures were present on site N271 in each of the isoforms analyzed.
16622833	1	28	from	glycoprotein	140:151	arg1	plasma					162:167	human plasma	156:167	human plasma	156:167	Human alpha1-antitrypsin (A1PI) is a well-known glycoprotein in human plasma important for the protection of tissues from proteolytic enzymes.
16622833	5	29	gly	glycosylation	742:754	arg2	N107					761:764	N107	761:764	N107	761:764	The variability of the number of antennae and hence sialic acids on glycosylation site N107, which even contained minute amounts of tetraantennary structures, emerged as a major cause for the IEF pattern of A1PI.
16622833	5	29	gly	glycosylation	742:754	arg2	site					756:759	glycosylation site N107	742:764	glycosylation site N107	742:764	The variability of the number of antennae and hence sialic acids on glycosylation site N107, which even contained minute amounts of tetraantennary structures, emerged as a major cause for the IEF pattern of A1PI.
16622833	7	30	theme	Lewis	1298:1302	arg1	determinant					1306:1316	a sialyl Lewis X determinant	1289:1316	a sialyl Lewis X determinant	1289:1316	Exoglycosidase digests revealed alpha2,6-linked neuraminic acids on diantennary N-glycans, and triantennary contained additionally one single alpha2,3-neuraminic acid per N-glycan, which, together with a fucose, formed a sialyl Lewis X determinant on the beta1,4-linked N-acetylglucosamine, as shown by 2-D-HPLC of pyridylaminated asialoglycans.
16622833	5	31	theme	sialic	726:731	arg1	acids					733:737	hence sialic acids	720:737	hence sialic acids	720:737	The variability of the number of antennae and hence sialic acids on glycosylation site N107, which even contained minute amounts of tetraantennary structures, emerged as a major cause for the IEF pattern of A1PI.
16622833	0	32	theme	Comprehensive	0:12	arg1	analysis					30:37	Comprehensive glyco-proteomic analysis	0:37	Comprehensive glyco-proteomic analysis of human alpha1-antitrypsin and its charge isoforms	0:89	Comprehensive glyco-proteomic analysis of human alpha1-antitrypsin and its charge isoforms.
16622833	7	33	theme	alpha2,6-linked	1102:1116	arg1	acids					1129:1133	alpha2,6-linked neuraminic acids	1102:1133	alpha2,6-linked neuraminic acids on diantennary N-glycans	1102:1158	Exoglycosidase digests revealed alpha2,6-linked neuraminic acids on diantennary N-glycans, and triantennary contained additionally one single alpha2,3-neuraminic acid per N-glycan, which, together with a fucose, formed a sialyl Lewis X determinant on the beta1,4-linked N-acetylglucosamine, as shown by 2-D-HPLC of pyridylaminated asialoglycans.
16622833	7	34	theme	neuraminic	1118:1127	arg1	acids					1129:1133	alpha2,6-linked neuraminic acids	1102:1133	alpha2,6-linked neuraminic acids on diantennary N-glycans	1102:1158	Exoglycosidase digests revealed alpha2,6-linked neuraminic acids on diantennary N-glycans, and triantennary contained additionally one single alpha2,3-neuraminic acid per N-glycan, which, together with a fucose, formed a sialyl Lewis X determinant on the beta1,4-linked N-acetylglucosamine, as shown by 2-D-HPLC of pyridylaminated asialoglycans.
16622833	7	35	theme	Exoglycosidase	1070:1083	arg1	digests					1085:1091	Exoglycosidase digests	1070:1091	Exoglycosidase digests	1070:1091	Exoglycosidase digests revealed alpha2,6-linked neuraminic acids on diantennary N-glycans, and triantennary contained additionally one single alpha2,3-neuraminic acid per N-glycan, which, together with a fucose, formed a sialyl Lewis X determinant on the beta1,4-linked N-acetylglucosamine, as shown by 2-D-HPLC of pyridylaminated asialoglycans.
16622833	7	36	contain	contained	1178:1186	arg2	acid					1232:1235	one single alpha2,3-neuraminic acid	1201:1235	one single alpha2,3-neuraminic acid	1201:1235	Exoglycosidase digests revealed alpha2,6-linked neuraminic acids on diantennary N-glycans, and triantennary contained additionally one single alpha2,3-neuraminic acid per N-glycan, which, together with a fucose, formed a sialyl Lewis X determinant on the beta1,4-linked N-acetylglucosamine, as shown by 2-D-HPLC of pyridylaminated asialoglycans.
16622833	7	36	contain	contained	1178:1186	arg1	triantennary					1165:1176	triantennary	1165:1176	triantennary	1165:1176	Exoglycosidase digests revealed alpha2,6-linked neuraminic acids on diantennary N-glycans, and triantennary contained additionally one single alpha2,3-neuraminic acid per N-glycan, which, together with a fucose, formed a sialyl Lewis X determinant on the beta1,4-linked N-acetylglucosamine, as shown by 2-D-HPLC of pyridylaminated asialoglycans.
16622833	3	37	theme	proteolytic	569:579	arg1	digestion					581:589	proteolytic digestion	569:589	proteolytic digestion	569:589	Here we present an approach to characterize A1PI isoforms from human plasma and its PTMs by LC-ESI-MS and LC-ESI-MS/MS of peptides obtained by proteolytic digestion.
16622833	6	38	attach	attached	954:961	arg2	structures					927:936	triantennary structures	914:936	triantennary structures	914:936	Only negligible amounts of triantennary structures were identified attached to N70, and exclusively diantennary structures were present on site N271 in each of the isoforms analyzed.
16622833	6	38	attach	attached	954:961	arg2	amounts					903:909	Only negligible amounts	887:909	Only negligible amounts of triantennary structures	887:936	Only negligible amounts of triantennary structures were identified attached to N70, and exclusively diantennary structures were present on site N271 in each of the isoforms analyzed.
16622833	6	38	attach	attached	954:961	arg1	N70					966:968	N70	966:968	N70	966:968	Only negligible amounts of triantennary structures were identified attached to N70, and exclusively diantennary structures were present on site N271 in each of the isoforms analyzed.
16622833	1	39	theme	tissues	201:207	arg1	protection					187:196	the protection	183:196	the protection of tissues from proteolytic enzymes	183:232	Human alpha1-antitrypsin (A1PI) is a well-known glycoprotein in human plasma important for the protection of tissues from proteolytic enzymes.
16622833	7	40	theme	single	1205:1210	arg1	acid					1232:1235	one single alpha2,3-neuraminic acid	1201:1235	one single alpha2,3-neuraminic acid	1201:1235	Exoglycosidase digests revealed alpha2,6-linked neuraminic acids on diantennary N-glycans, and triantennary contained additionally one single alpha2,3-neuraminic acid per N-glycan, which, together with a fucose, formed a sialyl Lewis X determinant on the beta1,4-linked N-acetylglucosamine, as shown by 2-D-HPLC of pyridylaminated asialoglycans.
16622833	5	41	from	site	756:759	arg1	number					697:702	the number	693:702	the number of antennae and hence sialic acids on glycosylation site N107	693:764	The variability of the number of antennae and hence sialic acids on glycosylation site N107, which even contained minute amounts of tetraantennary structures, emerged as a major cause for the IEF pattern of A1PI.
16622833	2	42	theme	triantennary	314:325	arg1	traces					336:341	diantennary N-glycans but also triantennary and even traces	283:341	diantennary N-glycans but also triantennary and even traces of tetraantennary structures leading to the typical IEF pattern observed for A1PI	283:423	The three N-glycosylation sites of A1PI contain diantennary N-glycans but also triantennary and even traces of tetraantennary structures leading to the typical IEF pattern observed for A1PI.
16622833	3	43	theme	human	489:493	arg1	plasma					495:500	human plasma	489:500	human plasma	489:500	Here we present an approach to characterize A1PI isoforms from human plasma and its PTMs by LC-ESI-MS and LC-ESI-MS/MS of peptides obtained by proteolytic digestion.
16622833	0	44	theme	alpha1-antitrypsin	48:65	arg1	analysis					30:37	Comprehensive glyco-proteomic analysis	0:37	Comprehensive glyco-proteomic analysis of human alpha1-antitrypsin and its charge isoforms	0:89	Comprehensive glyco-proteomic analysis of human alpha1-antitrypsin and its charge isoforms.
16622833	7	45	from	acids	1129:1133	arg1	N-glycans					1150:1158	diantennary N-glycans	1138:1158	diantennary N-glycans	1138:1158	Exoglycosidase digests revealed alpha2,6-linked neuraminic acids on diantennary N-glycans, and triantennary contained additionally one single alpha2,3-neuraminic acid per N-glycan, which, together with a fucose, formed a sialyl Lewis X determinant on the beta1,4-linked N-acetylglucosamine, as shown by 2-D-HPLC of pyridylaminated asialoglycans.
16622833	1	46	gly	glycoprotein	140:151	arg1	glycoprotein					140:151	a well-known glycoprotein	127:151	a well-known glycoprotein in human plasma important for the protection of tissues from proteolytic enzymes	127:232	Human alpha1-antitrypsin (A1PI) is a well-known glycoprotein in human plasma important for the protection of tissues from proteolytic enzymes.
16622833	1	46	gly	glycoprotein	140:151	arg1	alpha1-antitrypsin					98:115	Human alpha1-antitrypsin	92:115	Human alpha1-antitrypsin (A1PI)	92:122	Human alpha1-antitrypsin (A1PI) is a well-known glycoprotein in human plasma important for the protection of tissues from proteolytic enzymes.
16622833	3	47	theme	A1PI	470:473	arg1	isoforms					475:482	A1PI isoforms	470:482	A1PI isoforms	470:482	Here we present an approach to characterize A1PI isoforms from human plasma and its PTMs by LC-ESI-MS and LC-ESI-MS/MS of peptides obtained by proteolytic digestion.
16622833	2	48	theme	N-glycosylation	245:259	arg1	A1PI					270:273	A1PI	270:273	A1PI	270:273	The three N-glycosylation sites of A1PI contain diantennary N-glycans but also triantennary and even traces of tetraantennary structures leading to the typical IEF pattern observed for A1PI.
16622833	2	48	theme	N-glycosylation	245:259	arg1	sites					261:265	The three N-glycosylation sites	235:265	The three N-glycosylation sites of A1PI	235:273	The three N-glycosylation sites of A1PI contain diantennary N-glycans but also triantennary and even traces of tetraantennary structures leading to the typical IEF pattern observed for A1PI.
16622833	1	49	theme	proteolytic	214:224	arg1	enzymes					226:232	proteolytic enzymes	214:232	proteolytic enzymes	214:232	Human alpha1-antitrypsin (A1PI) is a well-known glycoprotein in human plasma important for the protection of tissues from proteolytic enzymes.
16622833	0	50	theme	human	42:46	arg1	alpha1-antitrypsin					48:65	human alpha1-antitrypsin	42:65	human alpha1-antitrypsin	42:65	Comprehensive glyco-proteomic analysis of human alpha1-antitrypsin and its charge isoforms.
16622833	5	51	theme	acids	733:737	arg1	number					697:702	the number	693:702	the number of antennae and hence sialic acids on glycosylation site N107	693:764	The variability of the number of antennae and hence sialic acids on glycosylation site N107, which even contained minute amounts of tetraantennary structures, emerged as a major cause for the IEF pattern of A1PI.
16622833	2	52	gly	N-glycosylation	245:259	arg2	A1PI					270:273	A1PI	270:273	A1PI	270:273	The three N-glycosylation sites of A1PI contain diantennary N-glycans but also triantennary and even traces of tetraantennary structures leading to the typical IEF pattern observed for A1PI.
16622833	2	52	gly	N-glycosylation	245:259	arg1	A1PI					270:273	A1PI	270:273	A1PI	270:273	The three N-glycosylation sites of A1PI contain diantennary N-glycans but also triantennary and even traces of tetraantennary structures leading to the typical IEF pattern observed for A1PI.
16622833	2	52	gly	N-glycosylation	245:259	arg2	sites					261:265	The three N-glycosylation sites	235:265	The three N-glycosylation sites of A1PI	235:273	The three N-glycosylation sites of A1PI contain diantennary N-glycans but also triantennary and even traces of tetraantennary structures leading to the typical IEF pattern observed for A1PI.
16622833	2	52	gly	N-glycosylation	245:259	arg2	three					239:243	three	239:243	three	239:243	The three N-glycosylation sites of A1PI contain diantennary N-glycans but also triantennary and even traces of tetraantennary structures leading to the typical IEF pattern observed for A1PI.
16622833	8	53	theme	structures	1444:1453	arg1	Fucosylation					1416:1427	Fucosylation	1416:1427	Fucosylation of diantennary structures	1416:1453	Fucosylation of diantennary structures was marginal and of the core alpha1,6 type.
16622833	4	54	theme	free	659:662	arg1	cysteine					664:671	free cysteine	659:671	free cysteine	659:671	The single cysteine residue of A1PI formed a disulfide bridge with free cysteine.
16622833	5	55	theme	A1PI	881:884	arg1	pattern					870:876	the IEF pattern	862:876	the IEF pattern of A1PI	862:884	The variability of the number of antennae and hence sialic acids on glycosylation site N107, which even contained minute amounts of tetraantennary structures, emerged as a major cause for the IEF pattern of A1PI.
16622833	1	56	from	enzymes	226:232	arg1	protection					187:196	the protection	183:196	the protection of tissues from proteolytic enzymes	183:232	Human alpha1-antitrypsin (A1PI) is a well-known glycoprotein in human plasma important for the protection of tissues from proteolytic enzymes.
16622833	1	56	from	enzymes	226:232	arg1	tissues					201:207	tissues	201:207	tissues from proteolytic enzymes	201:232	Human alpha1-antitrypsin (A1PI) is a well-known glycoprotein in human plasma important for the protection of tissues from proteolytic enzymes.
16622833	7	57	theme	X	1304:1304	arg1	determinant					1306:1316	a sialyl Lewis X determinant	1289:1316	a sialyl Lewis X determinant	1289:1316	Exoglycosidase digests revealed alpha2,6-linked neuraminic acids on diantennary N-glycans, and triantennary contained additionally one single alpha2,3-neuraminic acid per N-glycan, which, together with a fucose, formed a sialyl Lewis X determinant on the beta1,4-linked N-acetylglucosamine, as shown by 2-D-HPLC of pyridylaminated asialoglycans.
16622833	4	58	theme	A1PI	623:626	arg1	residue					612:618	The single cysteine residue	592:618	The single cysteine residue of A1PI	592:626	The single cysteine residue of A1PI formed a disulfide bridge with free cysteine.
16622833	4	58	theme	A1PI	623:626	arg1	A1PI					623:626	A1PI	623:626	A1PI	623:626	The single cysteine residue of A1PI formed a disulfide bridge with free cysteine.
16622833	5	59	theme	number	697:702	arg1	variability					678:688	The variability	674:688	The variability	674:688	The variability of the number of antennae and hence sialic acids on glycosylation site N107, which even contained minute amounts of tetraantennary structures, emerged as a major cause for the IEF pattern of A1PI.
16622833	2	60	theme	structures	361:370	arg1	traces					336:341	diantennary N-glycans but also triantennary and even traces	283:341	diantennary N-glycans but also triantennary and even traces of tetraantennary structures leading to the typical IEF pattern observed for A1PI	283:423	The three N-glycosylation sites of A1PI contain diantennary N-glycans but also triantennary and even traces of tetraantennary structures leading to the typical IEF pattern observed for A1PI.
16622833	7	61	theme	alpha2,3-neuraminic	1212:1230	arg1	acid					1232:1235	one single alpha2,3-neuraminic acid	1201:1235	one single alpha2,3-neuraminic acid	1201:1235	Exoglycosidase digests revealed alpha2,6-linked neuraminic acids on diantennary N-glycans, and triantennary contained additionally one single alpha2,3-neuraminic acid per N-glycan, which, together with a fucose, formed a sialyl Lewis X determinant on the beta1,4-linked N-acetylglucosamine, as shown by 2-D-HPLC of pyridylaminated asialoglycans.
16622833	7	62	theme	pyridylaminated	1385:1399	arg1	asialoglycans					1401:1413	pyridylaminated asialoglycans	1385:1413	pyridylaminated asialoglycans	1385:1413	Exoglycosidase digests revealed alpha2,6-linked neuraminic acids on diantennary N-glycans, and triantennary contained additionally one single alpha2,3-neuraminic acid per N-glycan, which, together with a fucose, formed a sialyl Lewis X determinant on the beta1,4-linked N-acetylglucosamine, as shown by 2-D-HPLC of pyridylaminated asialoglycans.
16622833	1	63	theme	well-known	129:138	arg1	glycoprotein					140:151	a well-known glycoprotein	127:151	a well-known glycoprotein in human plasma important for the protection of tissues from proteolytic enzymes	127:232	Human alpha1-antitrypsin (A1PI) is a well-known glycoprotein in human plasma important for the protection of tissues from proteolytic enzymes.
16622833	1	63	theme	well-known	129:138	arg1	alpha1-antitrypsin					98:115	Human alpha1-antitrypsin	92:115	Human alpha1-antitrypsin (A1PI)	92:122	Human alpha1-antitrypsin (A1PI) is a well-known glycoprotein in human plasma important for the protection of tissues from proteolytic enzymes.
16622833	8	64	theme	diantennary	1432:1442	arg1	structures					1444:1453	diantennary structures	1432:1453	diantennary structures	1432:1453	Fucosylation of diantennary structures was marginal and of the core alpha1,6 type.
16622833	3	65	theme	peptides	548:555	arg1	LC-ESI-MS					518:526	LC-ESI-MS	518:526	LC-ESI-MS	518:526	Here we present an approach to characterize A1PI isoforms from human plasma and its PTMs by LC-ESI-MS and LC-ESI-MS/MS of peptides obtained by proteolytic digestion.
16622833	3	65	theme	peptides	548:555	arg1	LC-ESI-MS/MS					532:543	LC-ESI-MS/MS	532:543	LC-ESI-MS/MS	532:543	Here we present an approach to characterize A1PI isoforms from human plasma and its PTMs by LC-ESI-MS and LC-ESI-MS/MS of peptides obtained by proteolytic digestion.
16622833	5	66	from	acids	733:737	arg1	site					756:759	glycosylation site N107	742:764	glycosylation site N107	742:764	The variability of the number of antennae and hence sialic acids on glycosylation site N107, which even contained minute amounts of tetraantennary structures, emerged as a major cause for the IEF pattern of A1PI.
16622833	2	67	theme	A1PI	270:273	arg1	A1PI					270:273	A1PI	270:273	A1PI	270:273	The three N-glycosylation sites of A1PI contain diantennary N-glycans but also triantennary and even traces of tetraantennary structures leading to the typical IEF pattern observed for A1PI.
16622833	2	67	theme	A1PI	270:273	arg1	sites					261:265	The three N-glycosylation sites	235:265	The three N-glycosylation sites of A1PI	235:273	The three N-glycosylation sites of A1PI contain diantennary N-glycans but also triantennary and even traces of tetraantennary structures leading to the typical IEF pattern observed for A1PI.
16622833	1	68	from	protection	187:196	arg1	enzymes					226:232	proteolytic enzymes	214:232	proteolytic enzymes	214:232	Human alpha1-antitrypsin (A1PI) is a well-known glycoprotein in human plasma important for the protection of tissues from proteolytic enzymes.
16622833	2	69	theme	typical	387:393	arg1	pattern					399:405	the typical IEF pattern	383:405	the typical IEF pattern observed for A1PI	383:423	The three N-glycosylation sites of A1PI contain diantennary N-glycans but also triantennary and even traces of tetraantennary structures leading to the typical IEF pattern observed for A1PI.
16622833	2	70	theme	tetraantennary	346:359	arg1	structures					361:370	tetraantennary structures	346:370	tetraantennary structures leading to the typical IEF pattern observed for A1PI	346:423	The three N-glycosylation sites of A1PI contain diantennary N-glycans but also triantennary and even traces of tetraantennary structures leading to the typical IEF pattern observed for A1PI.
16622833	0	71	theme	isoforms	82:89	arg1	analysis					30:37	Comprehensive glyco-proteomic analysis	0:37	Comprehensive glyco-proteomic analysis of human alpha1-antitrypsin and its charge isoforms	0:89	Comprehensive glyco-proteomic analysis of human alpha1-antitrypsin and its charge isoforms.
16622833	4	72	with	bridge	647:652	arg1	cysteine					664:671	free cysteine	659:671	free cysteine	659:671	The single cysteine residue of A1PI formed a disulfide bridge with free cysteine.
16622833	8	73	theme	alpha1,6	1484:1491	arg1	type					1493:1496	the core alpha1,6 type	1475:1496	the core alpha1,6 type	1475:1496	Fucosylation of diantennary structures was marginal and of the core alpha1,6 type.
16622833	5	74	from	antennae	707:714	arg1	site					756:759	glycosylation site N107	742:764	glycosylation site N107	742:764	The variability of the number of antennae and hence sialic acids on glycosylation site N107, which even contained minute amounts of tetraantennary structures, emerged as a major cause for the IEF pattern of A1PI.
16622833	2	75	theme	IEF	395:397	arg1	pattern					399:405	the typical IEF pattern	383:405	the typical IEF pattern observed for A1PI	383:423	The three N-glycosylation sites of A1PI contain diantennary N-glycans but also triantennary and even traces of tetraantennary structures leading to the typical IEF pattern observed for A1PI.
16622833	7	76	link	alpha2,6-linked	1102:1116	arg1	acids					1129:1133	alpha2,6-linked neuraminic acids	1102:1133	alpha2,6-linked neuraminic acids on diantennary N-glycans	1102:1158	Exoglycosidase digests revealed alpha2,6-linked neuraminic acids on diantennary N-glycans, and triantennary contained additionally one single alpha2,3-neuraminic acid per N-glycan, which, together with a fucose, formed a sialyl Lewis X determinant on the beta1,4-linked N-acetylglucosamine, as shown by 2-D-HPLC of pyridylaminated asialoglycans.
16622833	4	77	theme	disulfide	637:645	arg1	bridge					647:652	a disulfide bridge	635:652	a disulfide bridge with free cysteine	635:671	The single cysteine residue of A1PI formed a disulfide bridge with free cysteine.
16622833	0	78	theme	charge	75:80	arg1	isoforms					82:89	its charge isoforms	71:89	its charge isoforms	71:89	Comprehensive glyco-proteomic analysis of human alpha1-antitrypsin and its charge isoforms.
16622833	5	79	contain	contained	778:786	arg1	variability					678:688	The variability	674:688	The variability	674:688	The variability of the number of antennae and hence sialic acids on glycosylation site N107, which even contained minute amounts of tetraantennary structures, emerged as a major cause for the IEF pattern of A1PI.
16622833	5	79	contain	contained	778:786	arg2	structures					821:830	tetraantennary structures	806:830	tetraantennary structures	806:830	The variability of the number of antennae and hence sialic acids on glycosylation site N107, which even contained minute amounts of tetraantennary structures, emerged as a major cause for the IEF pattern of A1PI.
16622833	5	79	contain	contained	778:786	arg2	amounts					795:801	minute amounts	788:801	minute amounts of tetraantennary structures	788:830	The variability of the number of antennae and hence sialic acids on glycosylation site N107, which even contained minute amounts of tetraantennary structures, emerged as a major cause for the IEF pattern of A1PI.
16622833	8	80	theme	core	1479:1482	arg1	type					1493:1496	the core alpha1,6 type	1475:1496	the core alpha1,6 type	1475:1496	Fucosylation of diantennary structures was marginal and of the core alpha1,6 type.
16622833	7	81	theme	sialyl	1291:1296	arg1	determinant					1306:1316	a sialyl Lewis X determinant	1289:1316	a sialyl Lewis X determinant	1289:1316	Exoglycosidase digests revealed alpha2,6-linked neuraminic acids on diantennary N-glycans, and triantennary contained additionally one single alpha2,3-neuraminic acid per N-glycan, which, together with a fucose, formed a sialyl Lewis X determinant on the beta1,4-linked N-acetylglucosamine, as shown by 2-D-HPLC of pyridylaminated asialoglycans.
16622833	1	82	theme	human	156:160	arg1	plasma					162:167	human plasma	156:167	human plasma	156:167	Human alpha1-antitrypsin (A1PI) is a well-known glycoprotein in human plasma important for the protection of tissues from proteolytic enzymes.
16622833	5	83	from	number	697:702	arg1	site					756:759	glycosylation site N107	742:764	glycosylation site N107	742:764	The variability of the number of antennae and hence sialic acids on glycosylation site N107, which even contained minute amounts of tetraantennary structures, emerged as a major cause for the IEF pattern of A1PI.
18323454	5	0	theme	HBP	840:842	arg1	importance					822:831	the importance	818:831	the importance of the HBP in the development of glucose intolerance	818:884	Decreasing amounts of O-glycosylated CRTC2 by expression of the deglycosylating enzyme O-GlcNAcase blocked effects of glucose on gluconeogenesis, demonstrating the importance of the HBP in the development of glucose intolerance.
18323454	5	1	from	importance	822:831	arg1	development					851:861	the development	847:861	the development of glucose intolerance	847:884	Decreasing amounts of O-glycosylated CRTC2 by expression of the deglycosylating enzyme O-GlcNAcase blocked effects of glucose on gluconeogenesis, demonstrating the importance of the HBP in the development of glucose intolerance.
18323454	5	2	from	effects	765:771	arg1	gluconeogenesis					787:801	gluconeogenesis	787:801	gluconeogenesis	787:801	Decreasing amounts of O-glycosylated CRTC2 by expression of the deglycosylating enzyme O-GlcNAcase blocked effects of glucose on gluconeogenesis, demonstrating the importance of the HBP in the development of glucose intolerance.
18323454	1	3	theme	Chronic	56:62	arg1	hyperglycemia					64:76	Chronic hyperglycemia	56:76	Chronic hyperglycemia	56:76	Chronic hyperglycemia contributes to the development of diabetes-associated complications.
18323454	3	4	theme	hepatic	356:362	arg1	gluconeogenesis					364:378	hepatic gluconeogenesis	356:378	hepatic gluconeogenesis	356:378	We show that OGT triggered hepatic gluconeogenesis through the O-glycosylation of the transducer of regulated cyclic adenosine monophosphate response element-binding protein (CREB) 2 (TORC2 or CRTC2).
18323454	5	5	theme	Decreasing	658:667	arg1	amounts					669:675	Decreasing amounts	658:675	Decreasing amounts of O-glycosylated CRTC2 by expression of the deglycosylating enzyme O-GlcNAcase	658:755	Decreasing amounts of O-glycosylated CRTC2 by expression of the deglycosylating enzyme O-GlcNAcase blocked effects of glucose on gluconeogenesis, demonstrating the importance of the HBP in the development of glucose intolerance.
18323454	5	5	theme	Decreasing	658:667	arg1	CRTC2					695:699	O-glycosylated CRTC2	680:699	O-glycosylated CRTC2 by expression of the deglycosylating enzyme O-GlcNAcase	680:755	Decreasing amounts of O-glycosylated CRTC2 by expression of the deglycosylating enzyme O-GlcNAcase blocked effects of glucose on gluconeogenesis, demonstrating the importance of the HBP in the development of glucose intolerance.
18323454	2	6	theme	O-glycosyl	299:308	arg1	transferase					310:320	O-glycosyl transferase	299:320	O-glycosyl transferase (OGT)	299:326	Increases in the concentration of circulating glucose activate the hexosamine biosynthetic pathway (HBP) and promote the O-glycosylation of proteins by O-glycosyl transferase (OGT).
18323454	2	6	theme	O-glycosyl	299:308	arg1	OGT					323:325	OGT	323:325	OGT	323:325	Increases in the concentration of circulating glucose activate the hexosamine biosynthetic pathway (HBP) and promote the O-glycosylation of proteins by O-glycosyl transferase (OGT).
18323454	3	7	theme	element-binding	479:493	arg1	CREB					504:507	CREB	504:507	CREB	504:507	We show that OGT triggered hepatic gluconeogenesis through the O-glycosylation of the transducer of regulated cyclic adenosine monophosphate response element-binding protein (CREB) 2 (TORC2 or CRTC2).
18323454	3	7	theme	element-binding	479:493	arg1	protein					495:501	regulated cyclic adenosine monophosphate response element-binding protein	429:501	regulated cyclic adenosine monophosphate response element-binding protein (CREB) 2 (TORC2 or CRTC2)	429:527	We show that OGT triggered hepatic gluconeogenesis through the O-glycosylation of the transducer of regulated cyclic adenosine monophosphate response element-binding protein (CREB) 2 (TORC2 or CRTC2).
18323454	0	8	theme	coactivator	37:47	arg1	CRTC2					49:53	the CREB coactivator CRTC2	28:53	the CREB coactivator CRTC2	28:53	Hepatic glucose sensing via the CREB coactivator CRTC2.
18323454	3	9	theme	cyclic	439:444	arg1	monophosphate					456:468	cyclic adenosine monophosphate	439:468	regulated cyclic adenosine monophosphate response element-binding protein (CREB) 2 (TORC2 or CRTC2)	429:527	We show that OGT triggered hepatic gluconeogenesis through the O-glycosylation of the transducer of regulated cyclic adenosine monophosphate response element-binding protein (CREB) 2 (TORC2 or CRTC2).
18323454	0	10	theme	Hepatic	0:6	arg1	glucose					8:14	Hepatic glucose	0:14	Hepatic glucose	0:14	Hepatic glucose sensing via the CREB coactivator CRTC2.
18323454	3	11	theme	protein	495:501	arg1	transducer					415:424	the transducer	411:424	the transducer of regulated cyclic adenosine monophosphate response element-binding protein (CREB) 2 (TORC2 or CRTC2)	411:527	We show that OGT triggered hepatic gluconeogenesis through the O-glycosylation of the transducer of regulated cyclic adenosine monophosphate response element-binding protein (CREB) 2 (TORC2 or CRTC2).
18323454	5	12	theme	glucose	866:872	arg1	intolerance					874:884	glucose intolerance	866:884	glucose intolerance	866:884	Decreasing amounts of O-glycosylated CRTC2 by expression of the deglycosylating enzyme O-GlcNAcase blocked effects of glucose on gluconeogenesis, demonstrating the importance of the HBP in the development of glucose intolerance.
18323454	5	13	theme	O-glycosylated	680:693	arg1	CRTC2					695:699	O-glycosylated CRTC2	680:699	O-glycosylated CRTC2 by expression of the deglycosylating enzyme O-GlcNAcase	680:755	Decreasing amounts of O-glycosylated CRTC2 by expression of the deglycosylating enzyme O-GlcNAcase blocked effects of glucose on gluconeogenesis, demonstrating the importance of the HBP in the development of glucose intolerance.
18323454	3	14	theme	monophosphate	456:468	arg1	CREB					504:507	CREB	504:507	CREB	504:507	We show that OGT triggered hepatic gluconeogenesis through the O-glycosylation of the transducer of regulated cyclic adenosine monophosphate response element-binding protein (CREB) 2 (TORC2 or CRTC2).
18323454	3	14	theme	monophosphate	456:468	arg1	protein					495:501	regulated cyclic adenosine monophosphate response element-binding protein	429:501	regulated cyclic adenosine monophosphate response element-binding protein (CREB) 2 (TORC2 or CRTC2)	429:527	We show that OGT triggered hepatic gluconeogenesis through the O-glycosylation of the transducer of regulated cyclic adenosine monophosphate response element-binding protein (CREB) 2 (TORC2 or CRTC2).
18323454	3	15	theme	transducer	415:424	arg1	O-glycosylation					392:406	the O-glycosylation	388:406	the O-glycosylation of the transducer of regulated cyclic adenosine monophosphate response element-binding protein (CREB) 2 (TORC2 or CRTC2)	388:527	We show that OGT triggered hepatic gluconeogenesis through the O-glycosylation of the transducer of regulated cyclic adenosine monophosphate response element-binding protein (CREB) 2 (TORC2 or CRTC2).
18323454	3	16	gly	O-glycosylation	392:406	arg1	transducer					415:424	the transducer	411:424	the transducer of regulated cyclic adenosine monophosphate response element-binding protein (CREB) 2 (TORC2 or CRTC2)	411:527	We show that OGT triggered hepatic gluconeogenesis through the O-glycosylation of the transducer of regulated cyclic adenosine monophosphate response element-binding protein (CREB) 2 (TORC2 or CRTC2).
18323454	3	17	theme	response	470:477	arg1	CREB					504:507	CREB	504:507	CREB	504:507	We show that OGT triggered hepatic gluconeogenesis through the O-glycosylation of the transducer of regulated cyclic adenosine monophosphate response element-binding protein (CREB) 2 (TORC2 or CRTC2).
18323454	3	17	theme	response	470:477	arg1	protein					495:501	regulated cyclic adenosine monophosphate response element-binding protein	429:501	regulated cyclic adenosine monophosphate response element-binding protein (CREB) 2 (TORC2 or CRTC2)	429:527	We show that OGT triggered hepatic gluconeogenesis through the O-glycosylation of the transducer of regulated cyclic adenosine monophosphate response element-binding protein (CREB) 2 (TORC2 or CRTC2).
18323454	2	18	from	Increases	147:155	arg1	concentration					164:176	the concentration	160:176	the concentration of circulating glucose	160:199	Increases in the concentration of circulating glucose activate the hexosamine biosynthetic pathway (HBP) and promote the O-glycosylation of proteins by O-glycosyl transferase (OGT).
18323454	5	19	theme	intolerance	874:884	arg1	development					851:861	the development	847:861	the development of glucose intolerance	847:884	Decreasing amounts of O-glycosylated CRTC2 by expression of the deglycosylating enzyme O-GlcNAcase blocked effects of glucose on gluconeogenesis, demonstrating the importance of the HBP in the development of glucose intolerance.
18323454	2	20	gly	O-glycosylation	268:282	arg1	proteins					287:294	proteins	287:294	proteins	287:294	Increases in the concentration of circulating glucose activate the hexosamine biosynthetic pathway (HBP) and promote the O-glycosylation of proteins by O-glycosyl transferase (OGT).
18323454	0	21	theme	CREB	32:35	arg1	CRTC2					49:53	the CREB coactivator CRTC2	28:53	the CREB coactivator CRTC2	28:53	Hepatic glucose sensing via the CREB coactivator CRTC2.
18323454	5	22	theme	glucose	776:782	arg1	effects					765:771	effects	765:771	effects of glucose on gluconeogenesis	765:801	Decreasing amounts of O-glycosylated CRTC2 by expression of the deglycosylating enzyme O-GlcNAcase blocked effects of glucose on gluconeogenesis, demonstrating the importance of the HBP in the development of glucose intolerance.
18323454	3	23	theme	adenosine	446:454	arg1	monophosphate					456:468	cyclic adenosine monophosphate	439:468	regulated cyclic adenosine monophosphate response element-binding protein (CREB) 2 (TORC2 or CRTC2)	429:527	We show that OGT triggered hepatic gluconeogenesis through the O-glycosylation of the transducer of regulated cyclic adenosine monophosphate response element-binding protein (CREB) 2 (TORC2 or CRTC2).
18323454	4	24	from	sites	558:562	arg1	O-glycosylated					540:553	O-glycosylated	540:553	O-glycosylated	540:553	CRTC2 was O-glycosylated at sites that normally sequester CRTC2 in the cytoplasm through a phosphorylation-dependent mechanism.
18323454	2	25	theme	glucose	193:199	arg1	concentration					164:176	the concentration	160:176	the concentration of circulating glucose	160:199	Increases in the concentration of circulating glucose activate the hexosamine biosynthetic pathway (HBP) and promote the O-glycosylation of proteins by O-glycosyl transferase (OGT).
18323454	5	26	gly	O-glycosylated	680:693	arg1	CRTC2					695:699	O-glycosylated CRTC2	680:699	O-glycosylated CRTC2 by expression of the deglycosylating enzyme O-GlcNAcase	680:755	Decreasing amounts of O-glycosylated CRTC2 by expression of the deglycosylating enzyme O-GlcNAcase blocked effects of glucose on gluconeogenesis, demonstrating the importance of the HBP in the development of glucose intolerance.
18323454	5	27	theme	deglycosylating	722:736	arg1	O-GlcNAcase					745:755	the deglycosylating enzyme O-GlcNAcase	718:755	the deglycosylating enzyme O-GlcNAcase	718:755	Decreasing amounts of O-glycosylated CRTC2 by expression of the deglycosylating enzyme O-GlcNAcase blocked effects of glucose on gluconeogenesis, demonstrating the importance of the HBP in the development of glucose intolerance.
18323454	2	28	theme	circulating	181:191	arg1	glucose					193:199	circulating glucose	181:199	circulating glucose	181:199	Increases in the concentration of circulating glucose activate the hexosamine biosynthetic pathway (HBP) and promote the O-glycosylation of proteins by O-glycosyl transferase (OGT).
18323454	1	29	theme	diabetes-associated	112:130	arg1	complications					132:144	diabetes-associated complications	112:144	diabetes-associated complications	112:144	Chronic hyperglycemia contributes to the development of diabetes-associated complications.
18323454	3	30	theme	regulated	429:437	arg1	CREB					504:507	CREB	504:507	CREB	504:507	We show that OGT triggered hepatic gluconeogenesis through the O-glycosylation of the transducer of regulated cyclic adenosine monophosphate response element-binding protein (CREB) 2 (TORC2 or CRTC2).
18323454	3	30	theme	regulated	429:437	arg1	protein					495:501	regulated cyclic adenosine monophosphate response element-binding protein	429:501	regulated cyclic adenosine monophosphate response element-binding protein (CREB) 2 (TORC2 or CRTC2)	429:527	We show that OGT triggered hepatic gluconeogenesis through the O-glycosylation of the transducer of regulated cyclic adenosine monophosphate response element-binding protein (CREB) 2 (TORC2 or CRTC2).
18323454	5	31	theme	enzyme	738:743	arg1	O-GlcNAcase					745:755	the deglycosylating enzyme O-GlcNAcase	718:755	the deglycosylating enzyme O-GlcNAcase	718:755	Decreasing amounts of O-glycosylated CRTC2 by expression of the deglycosylating enzyme O-GlcNAcase blocked effects of glucose on gluconeogenesis, demonstrating the importance of the HBP in the development of glucose intolerance.
18323454	3	32	dep	protein	495:501	arg1	CRTC2					522:526	CRTC2	522:526	CRTC2	522:526	We show that OGT triggered hepatic gluconeogenesis through the O-glycosylation of the transducer of regulated cyclic adenosine monophosphate response element-binding protein (CREB) 2 (TORC2 or CRTC2).
18323454	3	32	dep	protein	495:501	arg1	TORC2					513:517	TORC2	513:517	TORC2	513:517	We show that OGT triggered hepatic gluconeogenesis through the O-glycosylation of the transducer of regulated cyclic adenosine monophosphate response element-binding protein (CREB) 2 (TORC2 or CRTC2).
18323454	1	33	theme	complications	132:144	arg1	development					97:107	the development	93:107	the development of diabetes-associated complications	93:144	Chronic hyperglycemia contributes to the development of diabetes-associated complications.
18323454	5	34	theme	O-GlcNAcase	745:755	arg1	expression					704:713	expression	704:713	expression of the deglycosylating enzyme O-GlcNAcase	704:755	Decreasing amounts of O-glycosylated CRTC2 by expression of the deglycosylating enzyme O-GlcNAcase blocked effects of glucose on gluconeogenesis, demonstrating the importance of the HBP in the development of glucose intolerance.
18323454	2	35	theme	proteins	287:294	arg1	O-glycosylation					268:282	the O-glycosylation	264:282	the O-glycosylation of proteins by O-glycosyl transferase (OGT)	264:326	Increases in the concentration of circulating glucose activate the hexosamine biosynthetic pathway (HBP) and promote the O-glycosylation of proteins by O-glycosyl transferase (OGT).
18323454	2	36	theme	biosynthetic	225:236	arg1	HBP					247:249	HBP	247:249	HBP	247:249	Increases in the concentration of circulating glucose activate the hexosamine biosynthetic pathway (HBP) and promote the O-glycosylation of proteins by O-glycosyl transferase (OGT).
18323454	2	36	theme	biosynthetic	225:236	arg1	pathway					238:244	the hexosamine biosynthetic pathway	210:244	the hexosamine biosynthetic pathway (HBP)	210:250	Increases in the concentration of circulating glucose activate the hexosamine biosynthetic pathway (HBP) and promote the O-glycosylation of proteins by O-glycosyl transferase (OGT).
18323454	4	37	gly	O-glycosylated	540:553	arg1	CRTC2					530:534	CRTC2	530:534	CRTC2	530:534	CRTC2 was O-glycosylated at sites that normally sequester CRTC2 in the cytoplasm through a phosphorylation-dependent mechanism.
18323454	4	37	gly	O-glycosylated	540:553	arg2	sites					558:562	sites	558:562	sites that normally sequester CRTC2 in the cytoplasm through a phosphorylation-dependent mechanism	558:655	CRTC2 was O-glycosylated at sites that normally sequester CRTC2 in the cytoplasm through a phosphorylation-dependent mechanism.
18323454	5	38	gly	deglycosylating	722:736	arg0	O-GlcNAcase					745:755	the deglycosylating enzyme O-GlcNAcase	718:755	the deglycosylating enzyme O-GlcNAcase	718:755	Decreasing amounts of O-glycosylated CRTC2 by expression of the deglycosylating enzyme O-GlcNAcase blocked effects of glucose on gluconeogenesis, demonstrating the importance of the HBP in the development of glucose intolerance.
18323454	4	39	theme	phosphorylation-dependent	621:645	arg1	mechanism					647:655	a phosphorylation-dependent mechanism	619:655	a phosphorylation-dependent mechanism	619:655	CRTC2 was O-glycosylated at sites that normally sequester CRTC2 in the cytoplasm through a phosphorylation-dependent mechanism.
18323454	2	40	theme	hexosamine	214:223	arg1	HBP					247:249	HBP	247:249	HBP	247:249	Increases in the concentration of circulating glucose activate the hexosamine biosynthetic pathway (HBP) and promote the O-glycosylation of proteins by O-glycosyl transferase (OGT).
18323454	2	40	theme	hexosamine	214:223	arg1	pathway					238:244	the hexosamine biosynthetic pathway	210:244	the hexosamine biosynthetic pathway (HBP)	210:250	Increases in the concentration of circulating glucose activate the hexosamine biosynthetic pathway (HBP) and promote the O-glycosylation of proteins by O-glycosyl transferase (OGT).
18323454	5	41	theme	CRTC2	695:699	arg1	amounts					669:675	Decreasing amounts	658:675	Decreasing amounts of O-glycosylated CRTC2 by expression of the deglycosylating enzyme O-GlcNAcase	658:755	Decreasing amounts of O-glycosylated CRTC2 by expression of the deglycosylating enzyme O-GlcNAcase blocked effects of glucose on gluconeogenesis, demonstrating the importance of the HBP in the development of glucose intolerance.
18323454	5	41	theme	CRTC2	695:699	arg1	CRTC2					695:699	O-glycosylated CRTC2	680:699	O-glycosylated CRTC2 by expression of the deglycosylating enzyme O-GlcNAcase	680:755	Decreasing amounts of O-glycosylated CRTC2 by expression of the deglycosylating enzyme O-GlcNAcase blocked effects of glucose on gluconeogenesis, demonstrating the importance of the HBP in the development of glucose intolerance.
10364201	8	0	theme	truncated	1166:1174	arg1	versions					1176:1183	truncated versions	1166:1183	truncated versions of N-glycosylated AE1	1166:1205	An association of calnexin with truncated versions of N-glycosylated AE1 was detected after release of the nascent chains from ribosomes with puromycin.
10364201	6	1	theme	other	933:937	arg1	loops					954:958	other extracytosolic loops	933:958	other extracytosolic loops in AE1	933:965	Calnexin had access to novel N-glycosylated sites created in other extracytosolic loops in AE1 by site-directed or insertional mutagenesis.
10364201	9	2	theme	polytopic	1346:1354	arg1	AE1					1378:1380	the polytopic membrane glycoprotein AE1	1342:1380	the polytopic membrane glycoprotein AE1	1342:1380	The results show that the interaction of calnexin with the polytopic membrane glycoprotein AE1 was dependent on the presence but not the location of the oligosaccharide.
10364201	4	3	theme	relative	718:725	arg1	AE1					714:716	N-glycosylated AE1	699:716	N-glycosylated AE1 relative to nonglycosylated AE1 both in vitro and in vivo	699:774	Calnexin showed a preferential interaction with N-glycosylated AE1 relative to nonglycosylated AE1 both in vitro and in vivo.
10364201	1	4	theme	membrane	246:253	arg1	glycoprotein					255:266	a polytopic membrane glycoprotein	234:266	a polytopic membrane glycoprotein	234:266	The interaction of the endoplasmic reticulum chaperone calnexin with N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger (AE1), was characterized by cell-free translation and in transfected HEK293 cells, followed by co-immunoprecipitation using anti-calnexin antibody.
10364201	1	4	theme	membrane	246:253	arg1	exchanger					297:305	the human erythrocyte anion exchanger	269:305	the human erythrocyte anion exchanger (AE1)	269:311	The interaction of the endoplasmic reticulum chaperone calnexin with N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger (AE1), was characterized by cell-free translation and in transfected HEK293 cells, followed by co-immunoprecipitation using anti-calnexin antibody.
10364201	4	5	gly	nonglycosylated	730:744	arg1	AE1					746:748	nonglycosylated AE1	730:748	nonglycosylated AE1 both in vitro and in vivo	730:774	Calnexin showed a preferential interaction with N-glycosylated AE1 relative to nonglycosylated AE1 both in vitro and in vivo.
10364201	8	6	with	ribosomes	1261:1269	arg1	puromycin					1276:1284	puromycin	1276:1284	puromycin	1276:1284	An association of calnexin with truncated versions of N-glycosylated AE1 was detected after release of the nascent chains from ribosomes with puromycin.
10364201	1	7	with	interaction	142:152	arg1	mutants					223:229	N-glycosylation mutants	207:229	N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger (AE1),	207:312	The interaction of the endoplasmic reticulum chaperone calnexin with N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger (AE1), was characterized by cell-free translation and in transfected HEK293 cells, followed by co-immunoprecipitation using anti-calnexin antibody.
10364201	8	8	theme	nascent	1241:1247	arg1	chains					1249:1254	the nascent chains	1237:1254	the nascent chains	1237:1254	An association of calnexin with truncated versions of N-glycosylated AE1 was detected after release of the nascent chains from ribosomes with puromycin.
10364201	7	9	theme	same	1095:1098	arg1	loop					1100:1103	the same loop	1091:1103	the same loop	1091:1103	The interaction with AE1 was enhanced when multiple sites were introduced into the same loop or into two different loops.
10364201	1	10	theme	glycoprotein	255:266	arg1	mutants					223:229	N-glycosylation mutants	207:229	N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger (AE1),	207:312	The interaction of the endoplasmic reticulum chaperone calnexin with N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger (AE1), was characterized by cell-free translation and in transfected HEK293 cells, followed by co-immunoprecipitation using anti-calnexin antibody.
10364201	0	11	theme	erythrocyte	98:108	arg1	band					129:132	band 3	129:134	band 3	129:134	Calnexin interaction with N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger 1 (band 3).
10364201	0	11	theme	erythrocyte	98:108	arg1	glycoprotein					74:85	a polytopic membrane glycoprotein	53:85	a polytopic membrane glycoprotein	53:85	Calnexin interaction with N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger 1 (band 3).
10364201	0	11	theme	erythrocyte	98:108	arg1	exchanger					116:124	the human erythrocyte anion exchanger 1	88:126	the human erythrocyte anion exchanger 1 (band 3)	88:135	Calnexin interaction with N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger 1 (band 3).
10364201	1	12	theme	cell-free	335:343	arg1	translation					345:355	cell-free translation	335:355	cell-free translation	335:355	The interaction of the endoplasmic reticulum chaperone calnexin with N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger (AE1), was characterized by cell-free translation and in transfected HEK293 cells, followed by co-immunoprecipitation using anti-calnexin antibody.
10364201	9	13	gly	glycoprotein	1365:1376	arg1	glycoprotein					1365:1376	the polytopic membrane glycoprotein AE1	1342:1380	the polytopic membrane glycoprotein AE1	1342:1380	The results show that the interaction of calnexin with the polytopic membrane glycoprotein AE1 was dependent on the presence but not the location of the oligosaccharide.
10364201	9	14	theme	oligosaccharide	1440:1454	arg1	location					1424:1431	the location	1420:1431	the presence but not the location of the oligosaccharide	1399:1454	The results show that the interaction of calnexin with the polytopic membrane glycoprotein AE1 was dependent on the presence but not the location of the oligosaccharide.
10364201	0	15	theme	human	92:96	arg1	band					129:132	band 3	129:134	band 3	129:134	Calnexin interaction with N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger 1 (band 3).
10364201	0	15	theme	human	92:96	arg1	glycoprotein					74:85	a polytopic membrane glycoprotein	53:85	a polytopic membrane glycoprotein	53:85	Calnexin interaction with N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger 1 (band 3).
10364201	0	15	theme	human	92:96	arg1	exchanger					116:124	the human erythrocyte anion exchanger 1	88:126	the human erythrocyte anion exchanger 1 (band 3)	88:135	Calnexin interaction with N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger 1 (band 3).
10364201	9	16	theme	calnexin	1328:1335	arg1	interaction					1313:1323	the interaction	1309:1323	the interaction of calnexin with the polytopic membrane glycoprotein AE1	1309:1380	The results show that the interaction of calnexin with the polytopic membrane glycoprotein AE1 was dependent on the presence but not the location of the oligosaccharide.
10364201	9	16	theme	calnexin	1328:1335	arg1	dependent					1386:1394	dependent	1386:1394	dependent	1386:1394	The results show that the interaction of calnexin with the polytopic membrane glycoprotein AE1 was dependent on the presence but not the location of the oligosaccharide.
10364201	9	17	theme	membrane	1356:1363	arg1	AE1					1378:1380	the polytopic membrane glycoprotein AE1	1342:1380	the polytopic membrane glycoprotein AE1	1342:1380	The results show that the interaction of calnexin with the polytopic membrane glycoprotein AE1 was dependent on the presence but not the location of the oligosaccharide.
10364201	0	18	gly	glycoprotein	74:85	arg1	glycoprotein					74:85	a polytopic membrane glycoprotein	53:85	a polytopic membrane glycoprotein	53:85	Calnexin interaction with N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger 1 (band 3).
10364201	0	18	gly	glycoprotein	74:85	arg1	exchanger					116:124	the human erythrocyte anion exchanger 1	88:126	the human erythrocyte anion exchanger 1 (band 3)	88:135	Calnexin interaction with N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger 1 (band 3).
10364201	3	19	gly	nonglycosylated	626:640	arg1	protein					642:648	a nonglycosylated protein	624:648	a nonglycosylated protein	624:648	This site was mutated (N642D) to create a nonglycosylated protein.
10364201	2	20	theme	N-glycosylation	522:536	arg1	N-glycosylation					522:536	N-glycosylation	522:536	N-glycosylation at Asn-642	522:547	AE1 contains 12-14 transmembrane segments and has a single site of N-glycosylation at Asn-642 in the fourth extracytosolic loop.
10364201	2	20	theme	N-glycosylation	522:536	arg1	site					514:517	a single site	505:517	a single site of N-glycosylation at Asn-642 in the fourth extracytosolic loop	505:581	AE1 contains 12-14 transmembrane segments and has a single site of N-glycosylation at Asn-642 in the fourth extracytosolic loop.
10364201	6	21	theme	N-glycosylated	901:914	arg1	sites					916:920	novel N-glycosylated sites	895:920	novel N-glycosylated sites created in other extracytosolic loops in AE1 by site-directed or insertional mutagenesis	895:1009	Calnexin had access to novel N-glycosylated sites created in other extracytosolic loops in AE1 by site-directed or insertional mutagenesis.
10364201	5	22	theme	II	847:848	arg1	inhibition					814:823	inhibition	814:823	inhibition of glucosidases I and II with castanospermine	814:869	This interaction could be blocked by inhibition of glucosidases I and II with castanospermine.
10364201	2	23	contain	contains	459:466	arg1	AE1					455:457	AE1	455:457	AE1	455:457	AE1 contains 12-14 transmembrane segments and has a single site of N-glycosylation at Asn-642 in the fourth extracytosolic loop.
10364201	2	23	contain	contains	459:466	arg2	segments					488:495	12-14 transmembrane segments	468:495	12-14 transmembrane segments	468:495	AE1 contains 12-14 transmembrane segments and has a single site of N-glycosylation at Asn-642 in the fourth extracytosolic loop.
10364201	4	24	with	interaction	682:692	arg1	AE1					714:716	N-glycosylated AE1	699:716	N-glycosylated AE1 relative to nonglycosylated AE1 both in vitro and in vivo	699:774	Calnexin showed a preferential interaction with N-glycosylated AE1 relative to nonglycosylated AE1 both in vitro and in vivo.
10364201	0	25	theme	anion	110:114	arg1	band					129:132	band 3	129:134	band 3	129:134	Calnexin interaction with N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger 1 (band 3).
10364201	0	25	theme	anion	110:114	arg1	glycoprotein					74:85	a polytopic membrane glycoprotein	53:85	a polytopic membrane glycoprotein	53:85	Calnexin interaction with N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger 1 (band 3).
10364201	0	25	theme	anion	110:114	arg1	exchanger					116:124	the human erythrocyte anion exchanger 1	88:126	the human erythrocyte anion exchanger 1 (band 3)	88:135	Calnexin interaction with N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger 1 (band 3).
10364201	6	26	theme	novel	895:899	arg1	sites					916:920	novel N-glycosylated sites	895:920	novel N-glycosylated sites created in other extracytosolic loops in AE1 by site-directed or insertional mutagenesis	895:1009	Calnexin had access to novel N-glycosylated sites created in other extracytosolic loops in AE1 by site-directed or insertional mutagenesis.
10364201	6	27	theme	insertional	987:997	arg1	mutagenesis					999:1009	site-directed or insertional mutagenesis	970:1009	mutagenesis	999:1009	Calnexin had access to novel N-glycosylated sites created in other extracytosolic loops in AE1 by site-directed or insertional mutagenesis.
10364201	1	28	gly	glycoprotein	255:266	arg1	glycoprotein					255:266	a polytopic membrane glycoprotein	234:266	a polytopic membrane glycoprotein	234:266	The interaction of the endoplasmic reticulum chaperone calnexin with N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger (AE1), was characterized by cell-free translation and in transfected HEK293 cells, followed by co-immunoprecipitation using anti-calnexin antibody.
10364201	1	28	gly	glycoprotein	255:266	arg1	exchanger					297:305	the human erythrocyte anion exchanger	269:305	the human erythrocyte anion exchanger (AE1)	269:311	The interaction of the endoplasmic reticulum chaperone calnexin with N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger (AE1), was characterized by cell-free translation and in transfected HEK293 cells, followed by co-immunoprecipitation using anti-calnexin antibody.
10364201	2	29	gly	N-glycosylation	522:536	arg2	Asn-642					541:547	Asn-642	541:547	Asn-642	541:547	AE1 contains 12-14 transmembrane segments and has a single site of N-glycosylation at Asn-642 in the fourth extracytosolic loop.
10364201	2	29	gly	N-glycosylation	522:536	arg2	N-glycosylation					522:536	N-glycosylation	522:536	N-glycosylation at Asn-642	522:547	AE1 contains 12-14 transmembrane segments and has a single site of N-glycosylation at Asn-642 in the fourth extracytosolic loop.
10364201	2	29	gly	N-glycosylation	522:536	arg2	site					514:517	a single site	505:517	a single site of N-glycosylation at Asn-642 in the fourth extracytosolic loop	505:581	AE1 contains 12-14 transmembrane segments and has a single site of N-glycosylation at Asn-642 in the fourth extracytosolic loop.
10364201	2	29	gly	N-glycosylation	522:536	arg1	loop					578:581	the fourth extracytosolic loop	552:581	the fourth extracytosolic loop	552:581	AE1 contains 12-14 transmembrane segments and has a single site of N-glycosylation at Asn-642 in the fourth extracytosolic loop.
10364201	2	29	gly	N-glycosylation	522:536	arg1	Asn-642					541:547	Asn-642	541:547	Asn-642	541:547	AE1 contains 12-14 transmembrane segments and has a single site of N-glycosylation at Asn-642 in the fourth extracytosolic loop.
10364201	3	30	dep	mutated	598:604	arg1	N642D					607:611	N642D	607:611	N642D	607:611	This site was mutated (N642D) to create a nonglycosylated protein.
10364201	1	31	theme	transfected	364:374	arg1	cells					383:387	transfected HEK293 cells	364:387	transfected HEK293 cells	364:387	The interaction of the endoplasmic reticulum chaperone calnexin with N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger (AE1), was characterized by cell-free translation and in transfected HEK293 cells, followed by co-immunoprecipitation using anti-calnexin antibody.
10364201	8	32	theme	calnexin	1152:1159	arg1	association					1137:1147	An association	1134:1147	An association of calnexin with truncated versions of N-glycosylated AE1	1134:1205	An association of calnexin with truncated versions of N-glycosylated AE1 was detected after release of the nascent chains from ribosomes with puromycin.
10364201	9	33	with	interaction	1313:1323	arg1	AE1					1378:1380	the polytopic membrane glycoprotein AE1	1342:1380	the polytopic membrane glycoprotein AE1	1342:1380	The results show that the interaction of calnexin with the polytopic membrane glycoprotein AE1 was dependent on the presence but not the location of the oligosaccharide.
10364201	6	34	from	loops	954:958	arg1	AE1					963:965	AE1	963:965	AE1	963:965	Calnexin had access to novel N-glycosylated sites created in other extracytosolic loops in AE1 by site-directed or insertional mutagenesis.
10364201	1	35	theme	endoplasmic	161:171	arg1	reticulum					173:181	the endoplasmic reticulum	157:181	the endoplasmic reticulum chaperone calnexin	157:200	The interaction of the endoplasmic reticulum chaperone calnexin with N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger (AE1), was characterized by cell-free translation and in transfected HEK293 cells, followed by co-immunoprecipitation using anti-calnexin antibody.
10364201	0	36	theme	Calnexin	0:7	arg1	interaction					9:19	Calnexin interaction	0:19	Calnexin interaction with N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger 1 (band 3).	0:136	Calnexin interaction with N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger 1 (band 3).
10364201	1	37	theme	human	273:277	arg1	AE1					308:310	AE1	308:310	AE1	308:310	The interaction of the endoplasmic reticulum chaperone calnexin with N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger (AE1), was characterized by cell-free translation and in transfected HEK293 cells, followed by co-immunoprecipitation using anti-calnexin antibody.
10364201	1	37	theme	human	273:277	arg1	exchanger					297:305	the human erythrocyte anion exchanger	269:305	the human erythrocyte anion exchanger (AE1)	269:311	The interaction of the endoplasmic reticulum chaperone calnexin with N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger (AE1), was characterized by cell-free translation and in transfected HEK293 cells, followed by co-immunoprecipitation using anti-calnexin antibody.
10364201	1	37	theme	human	273:277	arg1	glycoprotein					255:266	a polytopic membrane glycoprotein	234:266	a polytopic membrane glycoprotein	234:266	The interaction of the endoplasmic reticulum chaperone calnexin with N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger (AE1), was characterized by cell-free translation and in transfected HEK293 cells, followed by co-immunoprecipitation using anti-calnexin antibody.
10364201	1	38	theme	reticulum	173:181	arg1	calnexin					193:200	the endoplasmic reticulum chaperone calnexin	157:200	the endoplasmic reticulum chaperone calnexin	157:200	The interaction of the endoplasmic reticulum chaperone calnexin with N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger (AE1), was characterized by cell-free translation and in transfected HEK293 cells, followed by co-immunoprecipitation using anti-calnexin antibody.
10364201	0	39	theme	N-glycosylation	26:40	arg1	mutants					42:48	N-glycosylation mutants	26:48	N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger 1 (band 3)	26:135	Calnexin interaction with N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger 1 (band 3).
10364201	1	40	theme	erythrocyte	279:289	arg1	AE1					308:310	AE1	308:310	AE1	308:310	The interaction of the endoplasmic reticulum chaperone calnexin with N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger (AE1), was characterized by cell-free translation and in transfected HEK293 cells, followed by co-immunoprecipitation using anti-calnexin antibody.
10364201	1	40	theme	erythrocyte	279:289	arg1	exchanger					297:305	the human erythrocyte anion exchanger	269:305	the human erythrocyte anion exchanger (AE1)	269:311	The interaction of the endoplasmic reticulum chaperone calnexin with N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger (AE1), was characterized by cell-free translation and in transfected HEK293 cells, followed by co-immunoprecipitation using anti-calnexin antibody.
10364201	1	40	theme	erythrocyte	279:289	arg1	glycoprotein					255:266	a polytopic membrane glycoprotein	234:266	a polytopic membrane glycoprotein	234:266	The interaction of the endoplasmic reticulum chaperone calnexin with N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger (AE1), was characterized by cell-free translation and in transfected HEK293 cells, followed by co-immunoprecipitation using anti-calnexin antibody.
10364201	2	41	theme	extracytosolic	563:576	arg1	loop					578:581	the fourth extracytosolic loop	552:581	the fourth extracytosolic loop	552:581	AE1 contains 12-14 transmembrane segments and has a single site of N-glycosylation at Asn-642 in the fourth extracytosolic loop.
10364201	5	42	with	inhibition	814:823	arg1	castanospermine					855:869	castanospermine	855:869	castanospermine	855:869	This interaction could be blocked by inhibition of glucosidases I and II with castanospermine.
10364201	1	43	theme	chaperone	183:191	arg1	calnexin					193:200	the endoplasmic reticulum chaperone calnexin	157:200	the endoplasmic reticulum chaperone calnexin	157:200	The interaction of the endoplasmic reticulum chaperone calnexin with N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger (AE1), was characterized by cell-free translation and in transfected HEK293 cells, followed by co-immunoprecipitation using anti-calnexin antibody.
10364201	1	44	theme	anion	291:295	arg1	AE1					308:310	AE1	308:310	AE1	308:310	The interaction of the endoplasmic reticulum chaperone calnexin with N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger (AE1), was characterized by cell-free translation and in transfected HEK293 cells, followed by co-immunoprecipitation using anti-calnexin antibody.
10364201	1	44	theme	anion	291:295	arg1	exchanger					297:305	the human erythrocyte anion exchanger	269:305	the human erythrocyte anion exchanger (AE1)	269:311	The interaction of the endoplasmic reticulum chaperone calnexin with N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger (AE1), was characterized by cell-free translation and in transfected HEK293 cells, followed by co-immunoprecipitation using anti-calnexin antibody.
10364201	1	44	theme	anion	291:295	arg1	glycoprotein					255:266	a polytopic membrane glycoprotein	234:266	a polytopic membrane glycoprotein	234:266	The interaction of the endoplasmic reticulum chaperone calnexin with N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger (AE1), was characterized by cell-free translation and in transfected HEK293 cells, followed by co-immunoprecipitation using anti-calnexin antibody.
10364201	2	45	theme	fourth	556:561	arg1	loop					578:581	the fourth extracytosolic loop	552:581	the fourth extracytosolic loop	552:581	AE1 contains 12-14 transmembrane segments and has a single site of N-glycosylation at Asn-642 in the fourth extracytosolic loop.
10364201	1	46	theme	HEK293	376:381	arg1	cells					383:387	transfected HEK293 cells	364:387	transfected HEK293 cells	364:387	The interaction of the endoplasmic reticulum chaperone calnexin with N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger (AE1), was characterized by cell-free translation and in transfected HEK293 cells, followed by co-immunoprecipitation using anti-calnexin antibody.
10364201	2	47	theme	transmembrane	474:486	arg1	segments					488:495	12-14 transmembrane segments	468:495	12-14 transmembrane segments	468:495	AE1 contains 12-14 transmembrane segments and has a single site of N-glycosylation at Asn-642 in the fourth extracytosolic loop.
10364201	1	48	theme	calnexin	193:200	arg1	interaction					142:152	The interaction	138:152	The interaction of the endoplasmic reticulum chaperone calnexin with N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger (AE1),	138:312	The interaction of the endoplasmic reticulum chaperone calnexin with N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger (AE1), was characterized by cell-free translation and in transfected HEK293 cells, followed by co-immunoprecipitation using anti-calnexin antibody.
10364201	1	49	dep	characterized	318:330	arg1	followed					390:397	followed	390:397	followed by co-immunoprecipitation using anti-calnexin antibody	390:452	The interaction of the endoplasmic reticulum chaperone calnexin with N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger (AE1), was characterized by cell-free translation and in transfected HEK293 cells, followed by co-immunoprecipitation using anti-calnexin antibody.
10364201	10	50	theme	AE1	1520:1522	arg1	release					1509:1515	release	1509:1515	release of AE1 from the translocation machinery	1509:1555	Furthermore, calnexin was associated with AE1 after release of AE1 from the translocation machinery.
10364201	6	51	theme	site-directed	970:982	arg1	mutagenesis					999:1009	site-directed or insertional mutagenesis	970:1009	mutagenesis	999:1009	Calnexin had access to novel N-glycosylated sites created in other extracytosolic loops in AE1 by site-directed or insertional mutagenesis.
10364201	4	52	theme	preferential	669:680	arg1	interaction					682:692	a preferential interaction	667:692	a preferential interaction with N-glycosylated AE1 relative to nonglycosylated AE1 both in vitro and in vivo	667:774	Calnexin showed a preferential interaction with N-glycosylated AE1 relative to nonglycosylated AE1 both in vitro and in vivo.
10364201	9	53	theme	glycoprotein	1365:1376	arg1	AE1					1378:1380	the polytopic membrane glycoprotein AE1	1342:1380	the polytopic membrane glycoprotein AE1	1342:1380	The results show that the interaction of calnexin with the polytopic membrane glycoprotein AE1 was dependent on the presence but not the location of the oligosaccharide.
10364201	2	54	from	site	514:517	arg1	loop					578:581	the fourth extracytosolic loop	552:581	the fourth extracytosolic loop	552:581	AE1 contains 12-14 transmembrane segments and has a single site of N-glycosylation at Asn-642 in the fourth extracytosolic loop.
10364201	2	54	from	site	514:517	arg1	Asn-642					541:547	Asn-642	541:547	Asn-642	541:547	AE1 contains 12-14 transmembrane segments and has a single site of N-glycosylation at Asn-642 in the fourth extracytosolic loop.
10364201	5	55	theme	glucosidases	828:839	arg1	inhibition					814:823	inhibition	814:823	inhibition of glucosidases I and II with castanospermine	814:869	This interaction could be blocked by inhibition of glucosidases I and II with castanospermine.
10364201	2	56	contain	has	501:503	arg1	AE1					455:457	AE1	455:457	AE1	455:457	AE1 contains 12-14 transmembrane segments and has a single site of N-glycosylation at Asn-642 in the fourth extracytosolic loop.
10364201	2	56	contain	has	501:503	arg2	N-glycosylation					522:536	N-glycosylation	522:536	N-glycosylation at Asn-642	522:547	AE1 contains 12-14 transmembrane segments and has a single site of N-glycosylation at Asn-642 in the fourth extracytosolic loop.
10364201	2	56	contain	has	501:503	arg2	site					514:517	a single site	505:517	a single site of N-glycosylation at Asn-642 in the fourth extracytosolic loop	505:581	AE1 contains 12-14 transmembrane segments and has a single site of N-glycosylation at Asn-642 in the fourth extracytosolic loop.
10364201	1	57	theme	N-glycosylation	207:221	arg1	mutants					223:229	N-glycosylation mutants	207:229	N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger (AE1),	207:312	The interaction of the endoplasmic reticulum chaperone calnexin with N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger (AE1), was characterized by cell-free translation and in transfected HEK293 cells, followed by co-immunoprecipitation using anti-calnexin antibody.
10364201	0	58	theme	polytopic	55:63	arg1	glycoprotein					74:85	a polytopic membrane glycoprotein	53:85	a polytopic membrane glycoprotein	53:85	Calnexin interaction with N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger 1 (band 3).
10364201	0	58	theme	polytopic	55:63	arg1	exchanger					116:124	the human erythrocyte anion exchanger 1	88:126	the human erythrocyte anion exchanger 1 (band 3)	88:135	Calnexin interaction with N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger 1 (band 3).
10364201	8	59	theme	N-glycosylated	1188:1201	arg1	AE1					1203:1205	N-glycosylated AE1	1188:1205	N-glycosylated AE1	1188:1205	An association of calnexin with truncated versions of N-glycosylated AE1 was detected after release of the nascent chains from ribosomes with puromycin.
10364201	2	60	theme	single	507:512	arg1	N-glycosylation					522:536	N-glycosylation	522:536	N-glycosylation at Asn-642	522:547	AE1 contains 12-14 transmembrane segments and has a single site of N-glycosylation at Asn-642 in the fourth extracytosolic loop.
10364201	2	60	theme	single	507:512	arg1	site					514:517	a single site	505:517	a single site of N-glycosylation at Asn-642 in the fourth extracytosolic loop	505:581	AE1 contains 12-14 transmembrane segments and has a single site of N-glycosylation at Asn-642 in the fourth extracytosolic loop.
10364201	10	61	theme	translocation	1533:1545	arg1	machinery					1547:1555	the translocation machinery	1529:1555	the translocation machinery	1529:1555	Furthermore, calnexin was associated with AE1 after release of AE1 from the translocation machinery.
10364201	4	62	theme	nonglycosylated	730:744	arg1	AE1					746:748	nonglycosylated AE1	730:748	nonglycosylated AE1 both in vitro and in vivo	730:774	Calnexin showed a preferential interaction with N-glycosylated AE1 relative to nonglycosylated AE1 both in vitro and in vivo.
10364201	2	63	theme	12-14	468:472	arg1	segments					488:495	12-14 transmembrane segments	468:495	12-14 transmembrane segments	468:495	AE1 contains 12-14 transmembrane segments and has a single site of N-glycosylation at Asn-642 in the fourth extracytosolic loop.
10364201	10	64	from	machinery	1547:1555	arg1	release					1509:1515	release	1509:1515	release of AE1 from the translocation machinery	1509:1555	Furthermore, calnexin was associated with AE1 after release of AE1 from the translocation machinery.
10364201	4	65	gly	N-glycosylated	699:712	arg1	AE1					714:716	N-glycosylated AE1	699:716	N-glycosylated AE1 relative to nonglycosylated AE1 both in vitro and in vivo	699:774	Calnexin showed a preferential interaction with N-glycosylated AE1 relative to nonglycosylated AE1 both in vitro and in vivo.
10364201	7	66	theme	different	1117:1125	arg1	loops					1127:1131	two different loops	1113:1131	two different loops	1113:1131	The interaction with AE1 was enhanced when multiple sites were introduced into the same loop or into two different loops.
10364201	0	67	with	interaction	9:19	arg1	mutants					42:48	N-glycosylation mutants	26:48	N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger 1 (band 3)	26:135	Calnexin interaction with N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger 1 (band 3).
10364201	3	68	theme	nonglycosylated	626:640	arg1	protein					642:648	a nonglycosylated protein	624:648	a nonglycosylated protein	624:648	This site was mutated (N642D) to create a nonglycosylated protein.
10364201	6	69	gly	N-glycosylated	901:914	arg1	sites					916:920	novel N-glycosylated sites	895:920	novel N-glycosylated sites created in other extracytosolic loops in AE1 by site-directed or insertional mutagenesis	895:1009	Calnexin had access to novel N-glycosylated sites created in other extracytosolic loops in AE1 by site-directed or insertional mutagenesis.
10364201	7	70	theme	multiple	1055:1062	arg1	sites					1064:1068	multiple sites	1055:1068	multiple sites	1055:1068	The interaction with AE1 was enhanced when multiple sites were introduced into the same loop or into two different loops.
10364201	6	71	contain	had	881:883	arg2	access					885:890	access	885:890	access	885:890	Calnexin had access to novel N-glycosylated sites created in other extracytosolic loops in AE1 by site-directed or insertional mutagenesis.
10364201	6	71	contain	had	881:883	arg1	Calnexin					872:879	Calnexin	872:879	Calnexin	872:879	Calnexin had access to novel N-glycosylated sites created in other extracytosolic loops in AE1 by site-directed or insertional mutagenesis.
10364201	8	72	from	ribosomes	1261:1269	arg1	release					1226:1232	release	1226:1232	release of the nascent chains from ribosomes with puromycin	1226:1284	An association of calnexin with truncated versions of N-glycosylated AE1 was detected after release of the nascent chains from ribosomes with puromycin.
10364201	2	73	from	Asn-642	541:547	arg1	N-glycosylation					522:536	N-glycosylation	522:536	N-glycosylation at Asn-642	522:547	AE1 contains 12-14 transmembrane segments and has a single site of N-glycosylation at Asn-642 in the fourth extracytosolic loop.
10364201	2	73	from	Asn-642	541:547	arg1	site					514:517	a single site	505:517	a single site of N-glycosylation at Asn-642 in the fourth extracytosolic loop	505:581	AE1 contains 12-14 transmembrane segments and has a single site of N-glycosylation at Asn-642 in the fourth extracytosolic loop.
10364201	8	74	theme	chains	1249:1254	arg1	release					1226:1232	release	1226:1232	release of the nascent chains from ribosomes with puromycin	1226:1284	An association of calnexin with truncated versions of N-glycosylated AE1 was detected after release of the nascent chains from ribosomes with puromycin.
10364201	0	75	theme	glycoprotein	74:85	arg1	mutants					42:48	N-glycosylation mutants	26:48	N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger 1 (band 3)	26:135	Calnexin interaction with N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger 1 (band 3).
10364201	1	76	theme	anti-calnexin	431:443	arg1	antibody					445:452	anti-calnexin antibody	431:452	anti-calnexin antibody	431:452	The interaction of the endoplasmic reticulum chaperone calnexin with N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger (AE1), was characterized by cell-free translation and in transfected HEK293 cells, followed by co-immunoprecipitation using anti-calnexin antibody.
10364201	8	77	theme	AE1	1203:1205	arg1	versions					1176:1183	truncated versions	1166:1183	truncated versions of N-glycosylated AE1	1166:1205	An association of calnexin with truncated versions of N-glycosylated AE1 was detected after release of the nascent chains from ribosomes with puromycin.
10364201	4	78	theme	N-glycosylated	699:712	arg1	AE1					714:716	N-glycosylated AE1	699:716	N-glycosylated AE1 relative to nonglycosylated AE1 both in vitro and in vivo	699:774	Calnexin showed a preferential interaction with N-glycosylated AE1 relative to nonglycosylated AE1 both in vitro and in vivo.
10364201	7	79	with	interaction	1016:1026	arg1	AE1					1033:1035	AE1	1033:1035	AE1	1033:1035	The interaction with AE1 was enhanced when multiple sites were introduced into the same loop or into two different loops.
10364201	0	80	theme	membrane	65:72	arg1	glycoprotein					74:85	a polytopic membrane glycoprotein	53:85	a polytopic membrane glycoprotein	53:85	Calnexin interaction with N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger 1 (band 3).
10364201	0	80	theme	membrane	65:72	arg1	exchanger					116:124	the human erythrocyte anion exchanger 1	88:126	the human erythrocyte anion exchanger 1 (band 3)	88:135	Calnexin interaction with N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger 1 (band 3).
10364201	6	81	theme	extracytosolic	939:952	arg1	loops					954:958	other extracytosolic loops	933:958	other extracytosolic loops in AE1	933:965	Calnexin had access to novel N-glycosylated sites created in other extracytosolic loops in AE1 by site-directed or insertional mutagenesis.
10364201	8	82	gly	N-glycosylated	1188:1201	arg1	AE1					1203:1205	N-glycosylated AE1	1188:1205	N-glycosylated AE1	1188:1205	An association of calnexin with truncated versions of N-glycosylated AE1 was detected after release of the nascent chains from ribosomes with puromycin.
10364201	8	83	with	association	1137:1147	arg1	versions					1176:1183	truncated versions	1166:1183	truncated versions of N-glycosylated AE1	1166:1205	An association of calnexin with truncated versions of N-glycosylated AE1 was detected after release of the nascent chains from ribosomes with puromycin.
10364201	1	84	theme	polytopic	236:244	arg1	glycoprotein					255:266	a polytopic membrane glycoprotein	234:266	a polytopic membrane glycoprotein	234:266	The interaction of the endoplasmic reticulum chaperone calnexin with N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger (AE1), was characterized by cell-free translation and in transfected HEK293 cells, followed by co-immunoprecipitation using anti-calnexin antibody.
10364201	1	84	theme	polytopic	236:244	arg1	exchanger					297:305	the human erythrocyte anion exchanger	269:305	the human erythrocyte anion exchanger (AE1)	269:311	The interaction of the endoplasmic reticulum chaperone calnexin with N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger (AE1), was characterized by cell-free translation and in transfected HEK293 cells, followed by co-immunoprecipitation using anti-calnexin antibody.
10889209	6	0	gly	glycosylated	1021:1032	arg2	132					1041:1043	132	1041:1043	132	1041:1043	This finding may partly account for the reason that GIRK4 is not glycosylated at Asn(132), either as a homomer or when coexpressed with GIRK1.
10889209	6	0	gly	glycosylated	1021:1032	arg2	Asn					1037:1039	Asn	1037:1039	Asn(132)	1037:1044	This finding may partly account for the reason that GIRK4 is not glycosylated at Asn(132), either as a homomer or when coexpressed with GIRK1.
10889209	6	0	gly	glycosylated	1021:1032	arg1	GIRK4					1008:1012	GIRK4	1008:1012	GIRK4	1008:1012	This finding may partly account for the reason that GIRK4 is not glycosylated at Asn(132), either as a homomer or when coexpressed with GIRK1.
10889209	0	1	contain	has	53:55	arg1	Glycosylation					0:12	Glycosylation	0:12	Glycosylation of GIRK1 at Asn119 and ROMK1 at Asn117	0:51	Glycosylation of GIRK1 at Asn119 and ROMK1 at Asn117 has different consequences in potassium channel function.
10889209	0	1	contain	has	53:55	arg2	consequences					67:78	different consequences	57:78	different consequences	57:78	Glycosylation of GIRK1 at Asn119 and ROMK1 at Asn117 has different consequences in potassium channel function.
10889209	1	2	theme	rectifier	140:148	arg1	channel					155:161	G protein-gated inward rectifier K(+) channel	117:161	G protein-gated inward rectifier K(+) channel	117:161	GIRK (G protein-gated inward rectifier K(+) channel) proteins play critical functional roles in heart and brain physiology.
10889209	1	2	theme	rectifier	140:148	arg1	GIRK					111:114	GIRK	111:114	GIRK (G protein-gated inward rectifier K(+) channel) proteins	111:171	GIRK (G protein-gated inward rectifier K(+) channel) proteins play critical functional roles in heart and brain physiology.
10889209	8	3	theme	channel	1466:1472	arg1	function					1474:1481	heteromeric channel function	1454:1481	heteromeric channel function	1454:1481	Thus, N-glycosylation of GIRK1 at Asn(119) does not appear to affect its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function, unlike the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol.
10889209	0	4	theme	different	57:65	arg1	consequences					67:78	different consequences	57:78	different consequences	57:78	Glycosylation of GIRK1 at Asn119 and ROMK1 at Asn117 has different consequences in potassium channel function.
10889209	3	5	contain	have	493:496	arg1	GIRK4					487:491	GIRK4	487:491	GIRK4	487:491	Both GIRK1 and GIRK4 have one extracellular consensus N-glycosylation site.
10889209	3	5	contain	have	493:496	arg2	site					542:545	one extracellular consensus N-glycosylation site	498:545	one extracellular consensus N-glycosylation site	498:545	Both GIRK1 and GIRK4 have one extracellular consensus N-glycosylation site.
10889209	3	5	contain	have	493:496	arg1	GIRK1					477:481	GIRK1	477:481	GIRK1	477:481	Both GIRK1 and GIRK4 have one extracellular consensus N-glycosylation site.
10889209	8	6	gly	N-glycosylation	1526:1540	arg1	ROMK1					1545:1549	ROMK1	1545:1549	ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol	1545:1635	Thus, N-glycosylation of GIRK1 at Asn(119) does not appear to affect its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function, unlike the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol.
10889209	1	7	theme	K	150:150	arg1	channel					155:161	G protein-gated inward rectifier K(+) channel	117:161	G protein-gated inward rectifier K(+) channel	117:161	GIRK (G protein-gated inward rectifier K(+) channel) proteins play critical functional roles in heart and brain physiology.
10889209	1	7	theme	K	150:150	arg1	GIRK					111:114	GIRK	111:114	GIRK (G protein-gated inward rectifier K(+) channel) proteins	111:171	GIRK (G protein-gated inward rectifier K(+) channel) proteins play critical functional roles in heart and brain physiology.
10889209	8	8	dep	Wang	1581:1584	arg1	R.					1574:1575	R.	1574:1575	R.	1574:1575	Thus, N-glycosylation of GIRK1 at Asn(119) does not appear to affect its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function, unlike the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol.
10889209	8	8	dep	Wang	1581:1584	arg1	M					1619:1619	M	1619:1619	Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol	1554:1635	Thus, N-glycosylation of GIRK1 at Asn(119) does not appear to affect its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function, unlike the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol.
10889209	8	8	dep	Wang	1581:1584	arg1	Biol					1632:1635	Biol	1632:1635	Biol	1632:1635	Thus, N-glycosylation of GIRK1 at Asn(119) does not appear to affect its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function, unlike the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol.
10889209	8	9	theme	heteromeric	1454:1464	arg1	function					1474:1481	heteromeric channel function	1454:1481	heteromeric channel function	1454:1481	Thus, N-glycosylation of GIRK1 at Asn(119) does not appear to affect its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function, unlike the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol.
10889209	0	10	theme	potassium	83:91	arg1	function					101:108	potassium channel function	83:108	potassium channel function	83:108	Glycosylation of GIRK1 at Asn119 and ROMK1 at Asn117 has different consequences in potassium channel function.
10889209	7	11	theme	agonist-induced	1235:1249	arg1	currents					1251:1258	the agonist-induced currents	1231:1258	the agonist-induced currents	1231:1258	When the GIRK1(N119Q) mutant was coexpressed with GIRK4, the biophysical properties of the heteromeric channel and the magnitude of the agonist-induced currents were similar to those of controls.
10889209	3	12	theme	consensus	516:524	arg1	site					542:545	one extracellular consensus N-glycosylation site	498:545	one extracellular consensus N-glycosylation site	498:545	Both GIRK1 and GIRK4 have one extracellular consensus N-glycosylation site.
10889209	5	13	from	Asn	804:806	arg1	glycosylation					787:799	optimal glycosylation	779:799	optimal glycosylation at Asn(119)	779:811	GIRK1 membrane-spanning domain 1 was required for optimal glycosylation at Asn(119) because a chimera that contained GIRK4 membrane-spanning domain 1 significantly reduced the addition of a carbohydrate structure at this site.
10889209	8	14	gly	N-glycosylation	1301:1315	arg1	Asn					1329:1331	Asn	1329:1331	Asn(119)	1329:1336	Thus, N-glycosylation of GIRK1 at Asn(119) does not appear to affect its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function, unlike the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol.
10889209	8	14	gly	N-glycosylation	1301:1315	arg1	GIRK1					1320:1324	GIRK1	1320:1324	GIRK1	1320:1324	Thus, N-glycosylation of GIRK1 at Asn(119) does not appear to affect its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function, unlike the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol.
10889209	8	14	gly	N-glycosylation	1301:1315	arg2	119					1333:1335	119	1333:1335	119	1333:1335	Thus, N-glycosylation of GIRK1 at Asn(119) does not appear to affect its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function, unlike the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol.
10889209	8	14	gly	N-glycosylation	1301:1315	arg1	119					1333:1335	119	1333:1335	119	1333:1335	Thus, N-glycosylation of GIRK1 at Asn(119) does not appear to affect its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function, unlike the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol.
10889209	8	14	gly	N-glycosylation	1301:1315	arg2	Asn					1329:1331	Asn	1329:1331	Asn(119)	1329:1336	Thus, N-glycosylation of GIRK1 at Asn(119) does not appear to affect its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function, unlike the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol.
10889209	3	15	theme	N-glycosylation	526:540	arg1	site					542:545	one extracellular consensus N-glycosylation site	498:545	one extracellular consensus N-glycosylation site	498:545	Both GIRK1 and GIRK4 have one extracellular consensus N-glycosylation site.
10889209	2	16	theme	specific	318:325	arg1	glycosidases					327:338	specific glycosidases	318:338	specific glycosidases	318:338	Using antibodies directed to either GIRK1 or GIRK4, site-directed mutagenesis, and specific glycosidases, we have investigated the effects of glycosylation in the biosynthesis and heteromerization of these proteins expressed in oocytes.
10889209	5	17	theme	membrane-spanning	852:868	arg1	domain					870:875	GIRK4 membrane-spanning domain 1	846:877	GIRK4 membrane-spanning domain 1	846:877	GIRK1 membrane-spanning domain 1 was required for optimal glycosylation at Asn(119) because a chimera that contained GIRK4 membrane-spanning domain 1 significantly reduced the addition of a carbohydrate structure at this site.
10889209	0	18	from	ROMK1	37:41	arg1	Glycosylation					0:12	Glycosylation	0:12	Glycosylation of GIRK1 at Asn119 and ROMK1 at Asn117	0:51	Glycosylation of GIRK1 at Asn119 and ROMK1 at Asn117 has different consequences in potassium channel function.
10889209	2	19	dep	biosynthesis	398:409	arg1	the					394:396	the	394:396	the	394:396	Using antibodies directed to either GIRK1 or GIRK4, site-directed mutagenesis, and specific glycosidases, we have investigated the effects of glycosylation in the biosynthesis and heteromerization of these proteins expressed in oocytes.
10889209	4	20	theme	GIRK1	600:604	arg1	mutant					622:627	a GIRK1 N-glycosylation mutant	598:627	GIRK1 and GIRK4 as well as a GIRK1 N-glycosylation mutant	571:627	Using chimeras between GIRK1 and GIRK4 as well as a GIRK1 N-glycosylation mutant, we report that GIRK1 was glycosylated at Asn(119), whereas GIRK4 was not glycosylated at Asn(132).
10889209	4	21	dep	glycosylated	655:666	arg1	whereas					681:687	whereas	681:687	whereas	681:687	Using chimeras between GIRK1 and GIRK4 as well as a GIRK1 N-glycosylation mutant, we report that GIRK1 was glycosylated at Asn(119), whereas GIRK4 was not glycosylated at Asn(132).
10889209	8	22	theme	ROMK1	1545:1549	arg1	N-glycosylation					1526:1540	N-glycosylation	1526:1540	N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol	1526:1635	Thus, N-glycosylation of GIRK1 at Asn(119) does not appear to affect its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function, unlike the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol.
10889209	0	23	theme	channel	93:99	arg1	function					101:108	potassium channel function	83:108	potassium channel function	83:108	Glycosylation of GIRK1 at Asn119 and ROMK1 at Asn117 has different consequences in potassium channel function.
10889209	8	24	from	Z.	1587:1588	arg1	ROMK1					1545:1549	ROMK1	1545:1549	ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol	1545:1635	Thus, N-glycosylation of GIRK1 at Asn(119) does not appear to affect its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function, unlike the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol.
10889209	8	24	from	Z.	1587:1588	arg1	N-glycosylation					1526:1540	N-glycosylation	1526:1540	N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol	1526:1635	Thus, N-glycosylation of GIRK1 at Asn(119) does not appear to affect its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function, unlike the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol.
10889209	3	25	theme	extracellular	502:514	arg1	site					542:545	one extracellular consensus N-glycosylation site	498:545	one extracellular consensus N-glycosylation site	498:545	Both GIRK1 and GIRK4 have one extracellular consensus N-glycosylation site.
10889209	10	26	dep	270	1644:1646	arg1	15336-15340					1649:1659	15336-15340	1649:1659	15336-15340	1649:1659	270, 15336-15340).
10889209	5	27	theme	membrane-spanning	735:751	arg1	domain					753:758	GIRK1 membrane-spanning domain 1	729:760	GIRK1 membrane-spanning domain 1	729:760	GIRK1 membrane-spanning domain 1 was required for optimal glycosylation at Asn(119) because a chimera that contained GIRK4 membrane-spanning domain 1 significantly reduced the addition of a carbohydrate structure at this site.
10889209	0	28	from	Asn119	26:31	arg1	Glycosylation					0:12	Glycosylation	0:12	Glycosylation of GIRK1 at Asn119 and ROMK1 at Asn117	0:51	Glycosylation of GIRK1 at Asn119 and ROMK1 at Asn117 has different consequences in potassium channel function.
10889209	5	29	gly	glycosylation	787:799	arg2	119					808:810	119	808:810	119	808:810	GIRK1 membrane-spanning domain 1 was required for optimal glycosylation at Asn(119) because a chimera that contained GIRK4 membrane-spanning domain 1 significantly reduced the addition of a carbohydrate structure at this site.
10889209	5	29	gly	glycosylation	787:799	arg1	Asn					804:806	Asn	804:806	Asn(119)	804:811	GIRK1 membrane-spanning domain 1 was required for optimal glycosylation at Asn(119) because a chimera that contained GIRK4 membrane-spanning domain 1 significantly reduced the addition of a carbohydrate structure at this site.
10889209	5	29	gly	glycosylation	787:799	arg2	Asn					804:806	Asn	804:806	Asn(119)	804:811	GIRK1 membrane-spanning domain 1 was required for optimal glycosylation at Asn(119) because a chimera that contained GIRK4 membrane-spanning domain 1 significantly reduced the addition of a carbohydrate structure at this site.
10889209	5	29	gly	glycosylation	787:799	arg1	119					808:810	119	808:810	119	808:810	GIRK1 membrane-spanning domain 1 was required for optimal glycosylation at Asn(119) because a chimera that contained GIRK4 membrane-spanning domain 1 significantly reduced the addition of a carbohydrate structure at this site.
10889209	8	30	theme	physical	1368:1375	arg1	association					1377:1387	its physical association	1364:1387	its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function	1364:1481	Thus, N-glycosylation of GIRK1 at Asn(119) does not appear to affect its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function, unlike the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol.
10889209	7	31	theme	heteromeric	1190:1200	arg1	channel					1202:1208	the heteromeric channel	1186:1208	the heteromeric channel	1186:1208	When the GIRK1(N119Q) mutant was coexpressed with GIRK4, the biophysical properties of the heteromeric channel and the magnitude of the agonist-induced currents were similar to those of controls.
10889209	8	32	from	N-glycosylation	1526:1540	arg1	A.					1616:1617	A.	1616:1617	A.	1616:1617	Thus, N-glycosylation of GIRK1 at Asn(119) does not appear to affect its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function, unlike the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol.
10889209	8	32	from	N-glycosylation	1526:1540	arg1	A.					1601:1602	A.	1601:1602	A.	1601:1602	Thus, N-glycosylation of GIRK1 at Asn(119) does not appear to affect its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function, unlike the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol.
10889209	8	32	from	N-glycosylation	1526:1540	arg1	Wang					1581:1584	Wang	1581:1584	Wang	1581:1584	Thus, N-glycosylation of GIRK1 at Asn(119) does not appear to affect its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function, unlike the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol.
10889209	8	32	from	N-glycosylation	1526:1540	arg1	Z.					1587:1588	Z.	1587:1588	Z.	1587:1588	Thus, N-glycosylation of GIRK1 at Asn(119) does not appear to affect its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function, unlike the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol.
10889209	8	32	from	N-glycosylation	1526:1540	arg1	1995					1623:1626	1995	1623:1626	1995	1623:1626	Thus, N-glycosylation of GIRK1 at Asn(119) does not appear to affect its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function, unlike the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol.
10889209	8	32	from	N-glycosylation	1526:1540	arg1	Wible					1591:1595	Wible	1591:1595	Wible	1591:1595	Thus, N-glycosylation of GIRK1 at Asn(119) does not appear to affect its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function, unlike the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol.
10889209	7	33	theme	biophysical	1160:1170	arg1	similar					1265:1271	similar	1265:1271	similar	1265:1271	When the GIRK1(N119Q) mutant was coexpressed with GIRK4, the biophysical properties of the heteromeric channel and the magnitude of the agonist-induced currents were similar to those of controls.
10889209	7	33	theme	biophysical	1160:1170	arg1	properties					1172:1181	the biophysical properties	1156:1181	the biophysical properties of the heteromeric channel	1156:1208	When the GIRK1(N119Q) mutant was coexpressed with GIRK4, the biophysical properties of the heteromeric channel and the magnitude of the agonist-induced currents were similar to those of controls.
10889209	7	34	theme	channel	1202:1208	arg1	magnitude					1218:1226	the magnitude	1214:1226	the magnitude of the agonist-induced currents	1214:1258	When the GIRK1(N119Q) mutant was coexpressed with GIRK4, the biophysical properties of the heteromeric channel and the magnitude of the agonist-induced currents were similar to those of controls.
10889209	7	34	theme	channel	1202:1208	arg1	similar					1265:1271	similar	1265:1271	similar	1265:1271	When the GIRK1(N119Q) mutant was coexpressed with GIRK4, the biophysical properties of the heteromeric channel and the magnitude of the agonist-induced currents were similar to those of controls.
10889209	7	34	theme	channel	1202:1208	arg1	properties					1172:1181	the biophysical properties	1156:1181	the biophysical properties of the heteromeric channel	1156:1208	When the GIRK1(N119Q) mutant was coexpressed with GIRK4, the biophysical properties of the heteromeric channel and the magnitude of the agonist-induced currents were similar to those of controls.
10889209	8	35	from	Wang	1581:1584	arg1	ROMK1					1545:1549	ROMK1	1545:1549	ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol	1545:1635	Thus, N-glycosylation of GIRK1 at Asn(119) does not appear to affect its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function, unlike the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol.
10889209	8	35	from	Wang	1581:1584	arg1	N-glycosylation					1526:1540	N-glycosylation	1526:1540	N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol	1526:1635	Thus, N-glycosylation of GIRK1 at Asn(119) does not appear to affect its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function, unlike the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol.
10889209	4	36	theme	N-glycosylation	606:620	arg1	mutant					622:627	a GIRK1 N-glycosylation mutant	598:627	GIRK1 and GIRK4 as well as a GIRK1 N-glycosylation mutant	571:627	Using chimeras between GIRK1 and GIRK4 as well as a GIRK1 N-glycosylation mutant, we report that GIRK1 was glycosylated at Asn(119), whereas GIRK4 was not glycosylated at Asn(132).
10889209	0	37	theme	GIRK1	17:21	arg1	Glycosylation					0:12	Glycosylation	0:12	Glycosylation of GIRK1 at Asn119 and ROMK1 at Asn117	0:51	Glycosylation of GIRK1 at Asn119 and ROMK1 at Asn117 has different consequences in potassium channel function.
10889209	8	38	from	Wible	1591:1595	arg1	ROMK1					1545:1549	ROMK1	1545:1549	ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol	1545:1635	Thus, N-glycosylation of GIRK1 at Asn(119) does not appear to affect its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function, unlike the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol.
10889209	8	38	from	Wible	1591:1595	arg1	N-glycosylation					1526:1540	N-glycosylation	1526:1540	N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol	1526:1635	Thus, N-glycosylation of GIRK1 at Asn(119) does not appear to affect its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function, unlike the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol.
10889209	5	39	from	site	950:953	arg1	addition					905:912	the addition	901:912	the addition of a carbohydrate structure at this site	901:953	GIRK1 membrane-spanning domain 1 was required for optimal glycosylation at Asn(119) because a chimera that contained GIRK4 membrane-spanning domain 1 significantly reduced the addition of a carbohydrate structure at this site.
10889209	2	40	theme	glycosylation	377:389	arg1	effects					366:372	the effects	362:372	the effects of glycosylation in the biosynthesis and heteromerization of these proteins expressed in oocytes	362:469	Using antibodies directed to either GIRK1 or GIRK4, site-directed mutagenesis, and specific glycosidases, we have investigated the effects of glycosylation in the biosynthesis and heteromerization of these proteins expressed in oocytes.
10889209	8	41	from	A.	1616:1617	arg1	ROMK1					1545:1549	ROMK1	1545:1549	ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol	1545:1635	Thus, N-glycosylation of GIRK1 at Asn(119) does not appear to affect its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function, unlike the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol.
10889209	8	41	from	A.	1616:1617	arg1	N-glycosylation					1526:1540	N-glycosylation	1526:1540	N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol	1526:1635	Thus, N-glycosylation of GIRK1 at Asn(119) does not appear to affect its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function, unlike the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol.
10889209	1	42	dep	heart	207:211	arg1	physiology					223:232	physiology	223:232	physiology	223:232	GIRK (G protein-gated inward rectifier K(+) channel) proteins play critical functional roles in heart and brain physiology.
10889209	0	43	gly	Glycosylation	0:12	arg1	GIRK1					17:21	GIRK1	17:21	GIRK1	17:21	Glycosylation of GIRK1 at Asn119 and ROMK1 at Asn117 has different consequences in potassium channel function.
10889209	0	43	gly	Glycosylation	0:12	arg2	ROMK1					37:41	ROMK1	37:41	ROMK1	37:41	Glycosylation of GIRK1 at Asn119 and ROMK1 at Asn117 has different consequences in potassium channel function.
10889209	0	43	gly	Glycosylation	0:12	arg2	Asn119					26:31	Asn119	26:31	Asn119	26:31	Glycosylation of GIRK1 at Asn119 and ROMK1 at Asn117 has different consequences in potassium channel function.
10889209	8	44	theme	dramatic	1495:1502	arg1	effects					1515:1521	the dramatic functional effects	1491:1521	the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol	1491:1635	Thus, N-glycosylation of GIRK1 at Asn(119) does not appear to affect its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function, unlike the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol.
10889209	5	45	theme	optimal	779:785	arg1	glycosylation					787:799	optimal glycosylation	779:799	optimal glycosylation at Asn(119)	779:811	GIRK1 membrane-spanning domain 1 was required for optimal glycosylation at Asn(119) because a chimera that contained GIRK4 membrane-spanning domain 1 significantly reduced the addition of a carbohydrate structure at this site.
10889209	2	46	theme	proteins	441:448	arg1	heteromerization					415:430	heteromerization	415:430	heteromerization	415:430	Using antibodies directed to either GIRK1 or GIRK4, site-directed mutagenesis, and specific glycosidases, we have investigated the effects of glycosylation in the biosynthesis and heteromerization of these proteins expressed in oocytes.
10889209	2	46	theme	proteins	441:448	arg1	biosynthesis					398:409	biosynthesis	398:409	biosynthesis	398:409	Using antibodies directed to either GIRK1 or GIRK4, site-directed mutagenesis, and specific glycosidases, we have investigated the effects of glycosylation in the biosynthesis and heteromerization of these proteins expressed in oocytes.
10889209	8	47	theme	heteromer	1420:1428	arg1	routing					1405:1411	the routing	1401:1411	the routing of the heteromer to the cell surface	1401:1448	Thus, N-glycosylation of GIRK1 at Asn(119) does not appear to affect its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function, unlike the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol.
10889209	8	47	theme	heteromer	1420:1428	arg1	function					1474:1481	heteromeric channel function	1454:1481	heteromeric channel function	1454:1481	Thus, N-glycosylation of GIRK1 at Asn(119) does not appear to affect its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function, unlike the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol.
10889209	8	47	theme	heteromer	1420:1428	arg1	GIRK4					1394:1398	GIRK4	1394:1398	GIRK4	1394:1398	Thus, N-glycosylation of GIRK1 at Asn(119) does not appear to affect its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function, unlike the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol.
10889209	8	48	from	Asn	1329:1331	arg1	N-glycosylation					1301:1315	N-glycosylation	1301:1315	N-glycosylation of GIRK1 at Asn(119)	1301:1336	Thus, N-glycosylation of GIRK1 at Asn(119) does not appear to affect its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function, unlike the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol.
10889209	1	49	theme	critical	178:185	arg1	roles					198:202	critical functional roles	178:202	critical functional roles	178:202	GIRK (G protein-gated inward rectifier K(+) channel) proteins play critical functional roles in heart and brain physiology.
10889209	0	50	from	Asn117	46:51	arg1	ROMK1					37:41	ROMK1	37:41	ROMK1	37:41	Glycosylation of GIRK1 at Asn119 and ROMK1 at Asn117 has different consequences in potassium channel function.
10889209	0	50	from	Asn117	46:51	arg1	Asn119					26:31	Asn119	26:31	Asn119	26:31	Glycosylation of GIRK1 at Asn119 and ROMK1 at Asn117 has different consequences in potassium channel function.
10889209	7	51	theme	currents	1251:1258	arg1	magnitude					1218:1226	the magnitude	1214:1226	the magnitude of the agonist-induced currents	1214:1258	When the GIRK1(N119Q) mutant was coexpressed with GIRK4, the biophysical properties of the heteromeric channel and the magnitude of the agonist-induced currents were similar to those of controls.
10889209	7	51	theme	currents	1251:1258	arg1	similar					1265:1271	similar	1265:1271	similar	1265:1271	When the GIRK1(N119Q) mutant was coexpressed with GIRK4, the biophysical properties of the heteromeric channel and the magnitude of the agonist-induced currents were similar to those of controls.
10889209	7	51	theme	currents	1251:1258	arg1	properties					1172:1181	the biophysical properties	1156:1181	the biophysical properties of the heteromeric channel	1156:1208	When the GIRK1(N119Q) mutant was coexpressed with GIRK4, the biophysical properties of the heteromeric channel and the magnitude of the agonist-induced currents were similar to those of controls.
10889209	8	52	from	A.	1601:1602	arg1	ROMK1					1545:1549	ROMK1	1545:1549	ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol	1545:1635	Thus, N-glycosylation of GIRK1 at Asn(119) does not appear to affect its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function, unlike the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol.
10889209	8	52	from	A.	1601:1602	arg1	N-glycosylation					1526:1540	N-glycosylation	1526:1540	N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol	1526:1635	Thus, N-glycosylation of GIRK1 at Asn(119) does not appear to affect its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function, unlike the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol.
10889209	5	53	theme	GIRK1	729:733	arg1	domain					753:758	GIRK1 membrane-spanning domain 1	729:760	GIRK1 membrane-spanning domain 1	729:760	GIRK1 membrane-spanning domain 1 was required for optimal glycosylation at Asn(119) because a chimera that contained GIRK4 membrane-spanning domain 1 significantly reduced the addition of a carbohydrate structure at this site.
10889209	3	54	gly	N-glycosylation	526:540	arg2	one					498:500	one	498:500	one	498:500	Both GIRK1 and GIRK4 have one extracellular consensus N-glycosylation site.
10889209	3	54	gly	N-glycosylation	526:540	arg2	site					542:545	one extracellular consensus N-glycosylation site	498:545	one extracellular consensus N-glycosylation site	498:545	Both GIRK1 and GIRK4 have one extracellular consensus N-glycosylation site.
10889209	4	55	gly	glycosylated	655:666	arg2	119					675:677	119	675:677	119	675:677	Using chimeras between GIRK1 and GIRK4 as well as a GIRK1 N-glycosylation mutant, we report that GIRK1 was glycosylated at Asn(119), whereas GIRK4 was not glycosylated at Asn(132).
10889209	4	55	gly	glycosylated	655:666	arg2	Asn					671:673	Asn	671:673	Asn(119)	671:678	Using chimeras between GIRK1 and GIRK4 as well as a GIRK1 N-glycosylation mutant, we report that GIRK1 was glycosylated at Asn(119), whereas GIRK4 was not glycosylated at Asn(132).
10889209	4	55	gly	glycosylated	655:666	arg1	GIRK1					645:649	GIRK1	645:649	GIRK1	645:649	Using chimeras between GIRK1 and GIRK4 as well as a GIRK1 N-glycosylation mutant, we report that GIRK1 was glycosylated at Asn(119), whereas GIRK4 was not glycosylated at Asn(132).
10889209	6	56	dep	glycosylated	1021:1032	arg1	or					1067:1068	or	1067:1068	or	1067:1068	This finding may partly account for the reason that GIRK4 is not glycosylated at Asn(132), either as a homomer or when coexpressed with GIRK1.
10889209	6	56	dep	glycosylated	1021:1032	arg1	either					1047:1052	either	1047:1052	either	1047:1052	This finding may partly account for the reason that GIRK4 is not glycosylated at Asn(132), either as a homomer or when coexpressed with GIRK1.
10889209	5	57	contain	contained	836:844	arg2	domain					870:875	GIRK4 membrane-spanning domain 1	846:877	GIRK4 membrane-spanning domain 1	846:877	GIRK1 membrane-spanning domain 1 was required for optimal glycosylation at Asn(119) because a chimera that contained GIRK4 membrane-spanning domain 1 significantly reduced the addition of a carbohydrate structure at this site.
10889209	5	57	contain	contained	836:844	arg1	chimera					823:829	a chimera	821:829	a chimera that contained GIRK4 membrane-spanning domain 1	821:877	GIRK1 membrane-spanning domain 1 was required for optimal glycosylation at Asn(119) because a chimera that contained GIRK4 membrane-spanning domain 1 significantly reduced the addition of a carbohydrate structure at this site.
10889209	1	58	theme	GIRK	111:114	arg1	proteins					164:171	GIRK (G protein-gated inward rectifier K(+) channel) proteins	111:171	GIRK (G protein-gated inward rectifier K(+) channel) proteins	111:171	GIRK (G protein-gated inward rectifier K(+) channel) proteins play critical functional roles in heart and brain physiology.
10889209	8	59	theme	GIRK1	1320:1324	arg1	N-glycosylation					1301:1315	N-glycosylation	1301:1315	N-glycosylation of GIRK1 at Asn(119)	1301:1336	Thus, N-glycosylation of GIRK1 at Asn(119) does not appear to affect its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function, unlike the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol.
10889209	5	60	theme	carbohydrate	919:930	arg1	structure					932:940	a carbohydrate structure	917:940	a carbohydrate structure	917:940	GIRK1 membrane-spanning domain 1 was required for optimal glycosylation at Asn(119) because a chimera that contained GIRK4 membrane-spanning domain 1 significantly reduced the addition of a carbohydrate structure at this site.
10889209	2	61	theme	site-directed	287:299	arg1	mutagenesis					301:311	site-directed mutagenesis	287:311	site-directed mutagenesis	287:311	Using antibodies directed to either GIRK1 or GIRK4, site-directed mutagenesis, and specific glycosidases, we have investigated the effects of glycosylation in the biosynthesis and heteromerization of these proteins expressed in oocytes.
10889209	1	62	theme	functional	187:196	arg1	roles					198:202	critical functional roles	178:202	critical functional roles	178:202	GIRK (G protein-gated inward rectifier K(+) channel) proteins play critical functional roles in heart and brain physiology.
10889209	6	63	dep	or	1067:1068	arg1	coexpressed					1075:1085	coexpressed	1075:1085	coexpressed with GIRK1	1075:1096	This finding may partly account for the reason that GIRK4 is not glycosylated at Asn(132), either as a homomer or when coexpressed with GIRK1.
10889209	5	64	theme	structure	932:940	arg1	addition					905:912	the addition	901:912	the addition of a carbohydrate structure at this site	901:953	GIRK1 membrane-spanning domain 1 was required for optimal glycosylation at Asn(119) because a chimera that contained GIRK4 membrane-spanning domain 1 significantly reduced the addition of a carbohydrate structure at this site.
10889209	1	65	theme	G	117:117	arg1	channel					155:161	G protein-gated inward rectifier K(+) channel	117:161	G protein-gated inward rectifier K(+) channel	117:161	GIRK (G protein-gated inward rectifier K(+) channel) proteins play critical functional roles in heart and brain physiology.
10889209	1	65	theme	G	117:117	arg1	GIRK					111:114	GIRK	111:114	GIRK (G protein-gated inward rectifier K(+) channel) proteins	111:171	GIRK (G protein-gated inward rectifier K(+) channel) proteins play critical functional roles in heart and brain physiology.
10889209	8	66	theme	functional	1504:1513	arg1	effects					1515:1521	the dramatic functional effects	1491:1521	the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol	1491:1635	Thus, N-glycosylation of GIRK1 at Asn(119) does not appear to affect its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function, unlike the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol.
10889209	5	67	theme	GIRK4	846:850	arg1	domain					870:875	GIRK4 membrane-spanning domain 1	846:877	GIRK4 membrane-spanning domain 1	846:877	GIRK1 membrane-spanning domain 1 was required for optimal glycosylation at Asn(119) because a chimera that contained GIRK4 membrane-spanning domain 1 significantly reduced the addition of a carbohydrate structure at this site.
10889209	4	68	gly	glycosylated	703:714	arg2	132					723:725	132	723:725	132	723:725	Using chimeras between GIRK1 and GIRK4 as well as a GIRK1 N-glycosylation mutant, we report that GIRK1 was glycosylated at Asn(119), whereas GIRK4 was not glycosylated at Asn(132).
10889209	4	68	gly	glycosylated	703:714	arg2	Asn					719:721	Asn	719:721	Asn(132)	719:726	Using chimeras between GIRK1 and GIRK4 as well as a GIRK1 N-glycosylation mutant, we report that GIRK1 was glycosylated at Asn(119), whereas GIRK4 was not glycosylated at Asn(132).
10889209	4	68	gly	glycosylated	703:714	arg1	GIRK4					689:693	GIRK4	689:693	GIRK4	689:693	Using chimeras between GIRK1 and GIRK4 as well as a GIRK1 N-glycosylation mutant, we report that GIRK1 was glycosylated at Asn(119), whereas GIRK4 was not glycosylated at Asn(132).
10889209	8	69	theme	N-glycosylation	1526:1540	arg1	effects					1515:1521	the dramatic functional effects	1491:1521	the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol	1491:1635	Thus, N-glycosylation of GIRK1 at Asn(119) does not appear to affect its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function, unlike the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol.
10889209	2	70	from	effects	366:372	arg1	heteromerization					415:430	heteromerization	415:430	heteromerization	415:430	Using antibodies directed to either GIRK1 or GIRK4, site-directed mutagenesis, and specific glycosidases, we have investigated the effects of glycosylation in the biosynthesis and heteromerization of these proteins expressed in oocytes.
10889209	2	70	from	effects	366:372	arg1	biosynthesis					398:409	biosynthesis	398:409	biosynthesis	398:409	Using antibodies directed to either GIRK1 or GIRK4, site-directed mutagenesis, and specific glycosidases, we have investigated the effects of glycosylation in the biosynthesis and heteromerization of these proteins expressed in oocytes.
10889209	1	71	theme	protein-gated	119:131	arg1	channel					155:161	G protein-gated inward rectifier K(+) channel	117:161	G protein-gated inward rectifier K(+) channel	117:161	GIRK (G protein-gated inward rectifier K(+) channel) proteins play critical functional roles in heart and brain physiology.
10889209	1	71	theme	protein-gated	119:131	arg1	GIRK					111:114	GIRK	111:114	GIRK (G protein-gated inward rectifier K(+) channel) proteins	111:171	GIRK (G protein-gated inward rectifier K(+) channel) proteins play critical functional roles in heart and brain physiology.
10889209	7	72	theme	N119Q	1114:1118	arg1	mutant					1121:1126	the GIRK1(N119Q) mutant	1104:1126	the GIRK1(N119Q) mutant	1104:1126	When the GIRK1(N119Q) mutant was coexpressed with GIRK4, the biophysical properties of the heteromeric channel and the magnitude of the agonist-induced currents were similar to those of controls.
10889209	7	73	theme	GIRK1	1108:1112	arg1	mutant					1121:1126	the GIRK1(N119Q) mutant	1104:1126	the GIRK1(N119Q) mutant	1104:1126	When the GIRK1(N119Q) mutant was coexpressed with GIRK4, the biophysical properties of the heteromeric channel and the magnitude of the agonist-induced currents were similar to those of controls.
10889209	8	74	theme	cell	1437:1440	arg1	surface					1442:1448	the cell surface	1433:1448	the cell surface	1433:1448	Thus, N-glycosylation of GIRK1 at Asn(119) does not appear to affect its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function, unlike the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol.
10889209	1	75	theme	inward	133:138	arg1	channel					155:161	G protein-gated inward rectifier K(+) channel	117:161	G protein-gated inward rectifier K(+) channel	117:161	GIRK (G protein-gated inward rectifier K(+) channel) proteins play critical functional roles in heart and brain physiology.
10889209	1	75	theme	inward	133:138	arg1	GIRK					111:114	GIRK	111:114	GIRK (G protein-gated inward rectifier K(+) channel) proteins	111:171	GIRK (G protein-gated inward rectifier K(+) channel) proteins play critical functional roles in heart and brain physiology.
10889209	8	76	with	association	1377:1387	arg1	routing					1405:1411	the routing	1401:1411	the routing of the heteromer to the cell surface	1401:1448	Thus, N-glycosylation of GIRK1 at Asn(119) does not appear to affect its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function, unlike the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol.
10889209	8	76	with	association	1377:1387	arg1	function					1474:1481	heteromeric channel function	1454:1481	heteromeric channel function	1454:1481	Thus, N-glycosylation of GIRK1 at Asn(119) does not appear to affect its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function, unlike the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol.
10889209	8	76	with	association	1377:1387	arg1	GIRK4					1394:1398	GIRK4	1394:1398	GIRK4	1394:1398	Thus, N-glycosylation of GIRK1 at Asn(119) does not appear to affect its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function, unlike the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. A., and Brown, A. M. (1995) J. Biol.
19931508	3	0	contain	have	503:506	arg1	positions					493:501	specific positions	484:501	specific positions	484:501	However, it remains unclear whether all positions of protein glycosylation are involved in glycan functions, or if specific positions have individual roles.
19931508	3	0	contain	have	503:506	arg2	roles					519:523	individual roles	508:523	individual roles	508:523	However, it remains unclear whether all positions of protein glycosylation are involved in glycan functions, or if specific positions have individual roles.
19931508	7	1	theme	ICOS	1222:1225	arg1	folding					1235:1241	proper ICOS protein folding	1215:1241	proper ICOS protein folding in the ER	1215:1251	These data suggest that amongst the three putative ICOS glycosylation sites, N89 is required for proper ICOS protein folding in the ER, intracellular trafficking and ligand binding activity.
19931508	4	2	theme	N-glycan	585:592	arg1	involvement					559:569	the integral involvement	546:569	the integral involvement of a specific N-glycan from amongst the three glycans present on inducible costimulator (ICOS), a T-cell costimulatory molecule, in proper protein folding and intracellular trafficking to the cell surface membrane	546:783	Here we demonstrate the integral involvement of a specific N-glycan from amongst the three glycans present on inducible costimulator (ICOS), a T-cell costimulatory molecule, in proper protein folding and intracellular trafficking to the cell surface membrane.
19931508	0	3	theme	inducible	66:74	arg1	costimulator					76:87	inducible costimulator	66:87	inducible costimulator	66:87	Definitive evidence that a single N-glycan among three glycans on inducible costimulator is required for proper protein trafficking and ligand binding.
19931508	3	4	theme	individual	508:517	arg1	roles					519:523	individual roles	508:523	individual roles	508:523	However, it remains unclear whether all positions of protein glycosylation are involved in glycan functions, or if specific positions have individual roles.
19931508	4	5	theme	specific	576:583	arg1	N-glycan					585:592	a specific N-glycan	574:592	a specific N-glycan from	574:597	Here we demonstrate the integral involvement of a specific N-glycan from amongst the three glycans present on inducible costimulator (ICOS), a T-cell costimulatory molecule, in proper protein folding and intracellular trafficking to the cell surface membrane.
19931508	7	6	from	folding	1235:1241	arg1	ER					1250:1251	the ER	1246:1251	the ER	1246:1251	These data suggest that amongst the three putative ICOS glycosylation sites, N89 is required for proper ICOS protein folding in the ER, intracellular trafficking and ligand binding activity.
19931508	4	7	theme	cell	763:766	arg1	membrane					776:783	the cell surface membrane	759:783	the cell surface membrane	759:783	Here we demonstrate the integral involvement of a specific N-glycan from amongst the three glycans present on inducible costimulator (ICOS), a T-cell costimulatory molecule, in proper protein folding and intracellular trafficking to the cell surface membrane.
19931508	8	8	theme	current	1365:1371	arg1	understanding					1385:1397	the current mechanistic understanding	1361:1397	the current mechanistic understanding of the necessity	1361:1414	This study represents a substantial contribution to the current mechanistic understanding of the necessity and potential functions of a specific N-glycan among the multiple glycans of glycoproteins.
19931508	2	9	from	trafficking	343:353	arg1	reticulum					316:324	the endoplasmic reticulum	300:324	the endoplasmic reticulum (ER)	300:329	Glycans play key roles in protein folding, quality control in the endoplasmic reticulum (ER) and protein trafficking within cells.
19931508	2	9	from	trafficking	343:353	arg1	ER					327:328	ER	327:328	ER	327:328	Glycans play key roles in protein folding, quality control in the endoplasmic reticulum (ER) and protein trafficking within cells.
19931508	5	10	located	detected	978:985	arg2	proteins					831:838	glycosylation-defective mutant proteins	800:838	glycosylation-defective mutant proteins lacking N-glycan at amino-acid position 89 (N89)	800:887	We found that glycosylation-defective mutant proteins lacking N-glycan at amino-acid position 89 (N89), but not proteins lacking either N23 or N110, were retained within the cell and were not detected on the cell surface membrane.
19931508	5	10	located	detected	978:985	arg1	membrane					1007:1014	the cell surface membrane	990:1014	the cell surface membrane	990:1014	We found that glycosylation-defective mutant proteins lacking N-glycan at amino-acid position 89 (N89), but not proteins lacking either N23 or N110, were retained within the cell and were not detected on the cell surface membrane.
19931508	0	11	theme	proper	105:110	arg1	trafficking					120:130	proper protein trafficking	105:130	proper protein trafficking	105:130	Definitive evidence that a single N-glycan among three glycans on inducible costimulator is required for proper protein trafficking and ligand binding.
19931508	4	12	theme	proper	703:708	arg1	folding					718:724	proper protein folding	703:724	proper protein folding	703:724	Here we demonstrate the integral involvement of a specific N-glycan from amongst the three glycans present on inducible costimulator (ICOS), a T-cell costimulatory molecule, in proper protein folding and intracellular trafficking to the cell surface membrane.
19931508	7	13	theme	binding	1291:1297	arg1	activity					1299:1306	ligand binding activity	1284:1306	ligand binding activity	1284:1306	These data suggest that amongst the three putative ICOS glycosylation sites, N89 is required for proper ICOS protein folding in the ER, intracellular trafficking and ligand binding activity.
19931508	3	14	theme	protein	422:428	arg1	glycosylation					430:442	protein glycosylation	422:442	protein glycosylation	422:442	However, it remains unclear whether all positions of protein glycosylation are involved in glycan functions, or if specific positions have individual roles.
19931508	8	15	theme	substantial	1333:1343	arg1	contribution					1345:1356	a substantial contribution	1331:1356	a substantial contribution to the current mechanistic understanding of the necessity	1331:1414	This study represents a substantial contribution to the current mechanistic understanding of the necessity and potential functions of a specific N-glycan among the multiple glycans of glycoproteins.
19931508	2	16	theme	quality	281:287	arg1	control					289:295	quality control	281:295	quality control in the endoplasmic reticulum (ER)	281:329	Glycans play key roles in protein folding, quality control in the endoplasmic reticulum (ER) and protein trafficking within cells.
19931508	1	17	theme	widespread	171:180	arg1	modification					201:212	a widespread post-translational modification	169:212	a widespread post-translational modification found in glycoproteins	169:235	Glycosylation is a widespread post-translational modification found in glycoproteins.
19931508	1	17	theme	widespread	171:180	arg1	Glycosylation					152:164	Glycosylation	152:164	Glycosylation	152:164	Glycosylation is a widespread post-translational modification found in glycoproteins.
19931508	5	18	theme	glycosylation-defective	800:822	arg1	proteins					831:838	glycosylation-defective mutant proteins	800:838	glycosylation-defective mutant proteins lacking N-glycan at amino-acid position 89 (N89)	800:887	We found that glycosylation-defective mutant proteins lacking N-glycan at amino-acid position 89 (N89), but not proteins lacking either N23 or N110, were retained within the cell and were not detected on the cell surface membrane.
19931508	4	19	from	trafficking	744:754	arg1	present					625:631	present	625:631	present	625:631	Here we demonstrate the integral involvement of a specific N-glycan from amongst the three glycans present on inducible costimulator (ICOS), a T-cell costimulatory molecule, in proper protein folding and intracellular trafficking to the cell surface membrane.
19931508	4	20	theme	intracellular	730:742	arg1	trafficking					744:754	intracellular trafficking	730:754	intracellular trafficking to the cell surface membrane	730:783	Here we demonstrate the integral involvement of a specific N-glycan from amongst the three glycans present on inducible costimulator (ICOS), a T-cell costimulatory molecule, in proper protein folding and intracellular trafficking to the cell surface membrane.
19931508	6	21	theme	N89	1052:1054	arg1	glycosylation					1056:1068	N89 glycosylation	1052:1068	N89 glycosylation	1052:1068	Additional evidence suggested that N89 glycosylation was indirectly involved in ICOS ligand binding.
19931508	1	22	theme	post-translational	182:199	arg1	modification					201:212	a widespread post-translational modification	169:212	a widespread post-translational modification found in glycoproteins	169:235	Glycosylation is a widespread post-translational modification found in glycoproteins.
19931508	1	22	theme	post-translational	182:199	arg1	Glycosylation					152:164	Glycosylation	152:164	Glycosylation	152:164	Glycosylation is a widespread post-translational modification found in glycoproteins.
19931508	0	23	theme	Definitive	0:9	arg1	evidence					11:18	Definitive evidence	0:18	Definitive evidence that a single N-glycan among three glycans on inducible costimulator	0:87	Definitive evidence that a single N-glycan among three glycans on inducible costimulator is required for proper protein trafficking and ligand binding.
19931508	1	24	gly	glycoproteins	223:235	arg1	glycoproteins					223:235	glycoproteins	223:235	glycoproteins	223:235	Glycosylation is a widespread post-translational modification found in glycoproteins.
19931508	8	25	theme	glycoproteins	1493:1505	arg1	glycans					1482:1488	the multiple glycans	1469:1488	the multiple glycans of glycoproteins	1469:1505	This study represents a substantial contribution to the current mechanistic understanding of the necessity and potential functions of a specific N-glycan among the multiple glycans of glycoproteins.
19931508	5	26	theme	mutant	824:829	arg1	proteins					831:838	glycosylation-defective mutant proteins	800:838	glycosylation-defective mutant proteins lacking N-glycan at amino-acid position 89 (N89)	800:887	We found that glycosylation-defective mutant proteins lacking N-glycan at amino-acid position 89 (N89), but not proteins lacking either N23 or N110, were retained within the cell and were not detected on the cell surface membrane.
19931508	3	27	theme	glycosylation	430:442	arg1	positions					409:417	all positions	405:417	all positions of protein glycosylation	405:442	However, it remains unclear whether all positions of protein glycosylation are involved in glycan functions, or if specific positions have individual roles.
19931508	4	28	theme	integral	550:557	arg1	involvement					559:569	the integral involvement	546:569	the integral involvement of a specific N-glycan from amongst the three glycans present on inducible costimulator (ICOS), a T-cell costimulatory molecule, in proper protein folding and intracellular trafficking to the cell surface membrane	546:783	Here we demonstrate the integral involvement of a specific N-glycan from amongst the three glycans present on inducible costimulator (ICOS), a T-cell costimulatory molecule, in proper protein folding and intracellular trafficking to the cell surface membrane.
19931508	8	29	theme	N-glycan	1454:1461	arg1	contribution					1345:1356	a substantial contribution	1331:1356	a substantial contribution to the current mechanistic understanding of the necessity	1331:1414	This study represents a substantial contribution to the current mechanistic understanding of the necessity and potential functions of a specific N-glycan among the multiple glycans of glycoproteins.
19931508	8	29	theme	N-glycan	1454:1461	arg1	functions					1430:1438	potential functions	1420:1438	potential functions of a specific N-glycan among the multiple glycans of glycoproteins	1420:1505	This study represents a substantial contribution to the current mechanistic understanding of the necessity and potential functions of a specific N-glycan among the multiple glycans of glycoproteins.
19931508	8	30	gly	glycoproteins	1493:1505	arg1	glycoproteins					1493:1505	glycoproteins	1493:1505	glycoproteins	1493:1505	This study represents a substantial contribution to the current mechanistic understanding of the necessity and potential functions of a specific N-glycan among the multiple glycans of glycoproteins.
19931508	4	31	theme	inducible	636:644	arg1	costimulator					646:657	inducible costimulator	636:657	inducible costimulator (ICOS)	636:664	Here we demonstrate the integral involvement of a specific N-glycan from amongst the three glycans present on inducible costimulator (ICOS), a T-cell costimulatory molecule, in proper protein folding and intracellular trafficking to the cell surface membrane.
19931508	4	31	theme	inducible	636:644	arg1	molecule					690:697	a T-cell costimulatory molecule	667:697	a T-cell costimulatory molecule	667:697	Here we demonstrate the integral involvement of a specific N-glycan from amongst the three glycans present on inducible costimulator (ICOS), a T-cell costimulatory molecule, in proper protein folding and intracellular trafficking to the cell surface membrane.
19931508	4	31	theme	inducible	636:644	arg1	ICOS					660:663	ICOS	660:663	ICOS	660:663	Here we demonstrate the integral involvement of a specific N-glycan from amongst the three glycans present on inducible costimulator (ICOS), a T-cell costimulatory molecule, in proper protein folding and intracellular trafficking to the cell surface membrane.
19931508	6	32	theme	ligand	1102:1107	arg1	binding					1109:1115	ICOS ligand binding	1097:1115	ICOS ligand binding	1097:1115	Additional evidence suggested that N89 glycosylation was indirectly involved in ICOS ligand binding.
19931508	0	33	theme	protein	112:118	arg1	trafficking					120:130	proper protein trafficking	105:130	proper protein trafficking	105:130	Definitive evidence that a single N-glycan among three glycans on inducible costimulator is required for proper protein trafficking and ligand binding.
19931508	8	34	theme	specific	1445:1452	arg1	N-glycan					1454:1461	a specific N-glycan	1443:1461	a specific N-glycan among the multiple glycans of glycoproteins	1443:1505	This study represents a substantial contribution to the current mechanistic understanding of the necessity and potential functions of a specific N-glycan among the multiple glycans of glycoproteins.
19931508	2	35	theme	endoplasmic	304:314	arg1	reticulum					316:324	the endoplasmic reticulum	300:324	the endoplasmic reticulum (ER)	300:329	Glycans play key roles in protein folding, quality control in the endoplasmic reticulum (ER) and protein trafficking within cells.
19931508	2	35	theme	endoplasmic	304:314	arg1	ER					327:328	ER	327:328	ER	327:328	Glycans play key roles in protein folding, quality control in the endoplasmic reticulum (ER) and protein trafficking within cells.
19931508	6	36	theme	ICOS	1097:1100	arg1	binding					1109:1115	ICOS ligand binding	1097:1115	ICOS ligand binding	1097:1115	Additional evidence suggested that N89 glycosylation was indirectly involved in ICOS ligand binding.
19931508	7	37	theme	intracellular	1254:1266	arg1	trafficking					1268:1278	intracellular trafficking	1254:1278	intracellular trafficking	1254:1278	These data suggest that amongst the three putative ICOS glycosylation sites, N89 is required for proper ICOS protein folding in the ER, intracellular trafficking and ligand binding activity.
19931508	0	38	theme	ligand	136:141	arg1	binding					143:149	ligand binding	136:149	ligand binding	136:149	Definitive evidence that a single N-glycan among three glycans on inducible costimulator is required for proper protein trafficking and ligand binding.
19931508	6	39	theme	Additional	1017:1026	arg1	evidence					1028:1035	Additional evidence	1017:1035	Additional evidence	1017:1035	Additional evidence suggested that N89 glycosylation was indirectly involved in ICOS ligand binding.
19931508	2	40	from	folding	272:278	arg1	reticulum					316:324	the endoplasmic reticulum	300:324	the endoplasmic reticulum (ER)	300:329	Glycans play key roles in protein folding, quality control in the endoplasmic reticulum (ER) and protein trafficking within cells.
19931508	2	40	from	folding	272:278	arg1	ER					327:328	ER	327:328	ER	327:328	Glycans play key roles in protein folding, quality control in the endoplasmic reticulum (ER) and protein trafficking within cells.
19931508	5	41	theme	amino-acid	860:869	arg1	position					871:878	amino-acid position 89	860:881	amino-acid position 89 (N89)	860:887	We found that glycosylation-defective mutant proteins lacking N-glycan at amino-acid position 89 (N89), but not proteins lacking either N23 or N110, were retained within the cell and were not detected on the cell surface membrane.
19931508	5	41	theme	amino-acid	860:869	arg1	N89					884:886	N89	884:886	N89	884:886	We found that glycosylation-defective mutant proteins lacking N-glycan at amino-acid position 89 (N89), but not proteins lacking either N23 or N110, were retained within the cell and were not detected on the cell surface membrane.
19931508	0	42	theme	single	27:32	arg1	N-glycan					34:41	a single N-glycan	25:41	a single N-glycan among three glycans on inducible costimulator	25:87	Definitive evidence that a single N-glycan among three glycans on inducible costimulator is required for proper protein trafficking and ligand binding.
19931508	2	43	theme	key	251:253	arg1	roles					255:259	key roles	251:259	key roles	251:259	Glycans play key roles in protein folding, quality control in the endoplasmic reticulum (ER) and protein trafficking within cells.
19931508	7	44	from	trafficking	1268:1278	arg1	ER					1250:1251	the ER	1246:1251	the ER	1246:1251	These data suggest that amongst the three putative ICOS glycosylation sites, N89 is required for proper ICOS protein folding in the ER, intracellular trafficking and ligand binding activity.
19931508	3	45	theme	glycan	460:465	arg1	functions					467:475	glycan functions	460:475	glycan functions	460:475	However, it remains unclear whether all positions of protein glycosylation are involved in glycan functions, or if specific positions have individual roles.
19931508	8	46	theme	multiple	1473:1480	arg1	glycans					1482:1488	the multiple glycans	1469:1488	the multiple glycans of glycoproteins	1469:1505	This study represents a substantial contribution to the current mechanistic understanding of the necessity and potential functions of a specific N-glycan among the multiple glycans of glycoproteins.
19931508	6	47	gly	glycosylation	1056:1068	arg1	binding					1109:1115	ICOS ligand binding	1097:1115	ICOS ligand binding	1097:1115	Additional evidence suggested that N89 glycosylation was indirectly involved in ICOS ligand binding.
19931508	0	48	from	glycans	55:61	arg1	costimulator					76:87	inducible costimulator	66:87	inducible costimulator	66:87	Definitive evidence that a single N-glycan among three glycans on inducible costimulator is required for proper protein trafficking and ligand binding.
19931508	5	49	theme	surface	999:1005	arg1	membrane					1007:1014	the cell surface membrane	990:1014	the cell surface membrane	990:1014	We found that glycosylation-defective mutant proteins lacking N-glycan at amino-acid position 89 (N89), but not proteins lacking either N23 or N110, were retained within the cell and were not detected on the cell surface membrane.
19931508	3	50	theme	specific	484:491	arg1	positions					493:501	specific positions	484:501	specific positions	484:501	However, it remains unclear whether all positions of protein glycosylation are involved in glycan functions, or if specific positions have individual roles.
19931508	8	51	theme	necessity	1406:1414	arg1	understanding					1385:1397	the current mechanistic understanding	1361:1397	the current mechanistic understanding of the necessity	1361:1414	This study represents a substantial contribution to the current mechanistic understanding of the necessity and potential functions of a specific N-glycan among the multiple glycans of glycoproteins.
19931508	7	52	theme	protein	1227:1233	arg1	folding					1235:1241	proper ICOS protein folding	1215:1241	proper ICOS protein folding in the ER	1215:1251	These data suggest that amongst the three putative ICOS glycosylation sites, N89 is required for proper ICOS protein folding in the ER, intracellular trafficking and ligand binding activity.
19931508	4	53	attach	present	625:631	arg2	glycans					617:623	the three glycans	607:623	the three glycans present on inducible costimulator (ICOS), a T-cell costimulatory molecule, in proper protein folding and intracellular trafficking to the cell surface membrane	607:783	Here we demonstrate the integral involvement of a specific N-glycan from amongst the three glycans present on inducible costimulator (ICOS), a T-cell costimulatory molecule, in proper protein folding and intracellular trafficking to the cell surface membrane.
19931508	4	53	attach	present	625:631	arg1	folding					718:724	proper protein folding	703:724	proper protein folding	703:724	Here we demonstrate the integral involvement of a specific N-glycan from amongst the three glycans present on inducible costimulator (ICOS), a T-cell costimulatory molecule, in proper protein folding and intracellular trafficking to the cell surface membrane.
19931508	4	53	attach	present	625:631	arg1	costimulator					646:657	inducible costimulator	636:657	inducible costimulator (ICOS)	636:664	Here we demonstrate the integral involvement of a specific N-glycan from amongst the three glycans present on inducible costimulator (ICOS), a T-cell costimulatory molecule, in proper protein folding and intracellular trafficking to the cell surface membrane.
19931508	4	53	attach	present	625:631	arg1	molecule					690:697	a T-cell costimulatory molecule	667:697	a T-cell costimulatory molecule	667:697	Here we demonstrate the integral involvement of a specific N-glycan from amongst the three glycans present on inducible costimulator (ICOS), a T-cell costimulatory molecule, in proper protein folding and intracellular trafficking to the cell surface membrane.
19931508	4	53	attach	present	625:631	arg1	ICOS					660:663	ICOS	660:663	ICOS	660:663	Here we demonstrate the integral involvement of a specific N-glycan from amongst the three glycans present on inducible costimulator (ICOS), a T-cell costimulatory molecule, in proper protein folding and intracellular trafficking to the cell surface membrane.
19931508	4	53	attach	present	625:631	arg1	trafficking					744:754	intracellular trafficking	730:754	intracellular trafficking to the cell surface membrane	730:783	Here we demonstrate the integral involvement of a specific N-glycan from amongst the three glycans present on inducible costimulator (ICOS), a T-cell costimulatory molecule, in proper protein folding and intracellular trafficking to the cell surface membrane.
19931508	2	54	theme	protein	335:341	arg1	trafficking					343:353	protein trafficking	335:353	protein trafficking within cells	335:366	Glycans play key roles in protein folding, quality control in the endoplasmic reticulum (ER) and protein trafficking within cells.
19931508	2	55	from	control	289:295	arg1	reticulum					316:324	the endoplasmic reticulum	300:324	the endoplasmic reticulum (ER)	300:329	Glycans play key roles in protein folding, quality control in the endoplasmic reticulum (ER) and protein trafficking within cells.
19931508	2	55	from	control	289:295	arg1	ER					327:328	ER	327:328	ER	327:328	Glycans play key roles in protein folding, quality control in the endoplasmic reticulum (ER) and protein trafficking within cells.
19931508	1	56	located	found	214:218	arg2	modification					201:212	a widespread post-translational modification	169:212	a widespread post-translational modification found in glycoproteins	169:235	Glycosylation is a widespread post-translational modification found in glycoproteins.
19931508	1	56	located	found	214:218	arg2	Glycosylation					152:164	Glycosylation	152:164	Glycosylation	152:164	Glycosylation is a widespread post-translational modification found in glycoproteins.
19931508	1	56	located	found	214:218	arg1	glycoproteins					223:235	glycoproteins	223:235	glycoproteins	223:235	Glycosylation is a widespread post-translational modification found in glycoproteins.
19931508	8	57	theme	potential	1420:1428	arg1	functions					1430:1438	potential functions	1420:1438	potential functions of a specific N-glycan among the multiple glycans of glycoproteins	1420:1505	This study represents a substantial contribution to the current mechanistic understanding of the necessity and potential functions of a specific N-glycan among the multiple glycans of glycoproteins.
19931508	5	58	theme	cell	994:997	arg1	membrane					1007:1014	the cell surface membrane	990:1014	the cell surface membrane	990:1014	We found that glycosylation-defective mutant proteins lacking N-glycan at amino-acid position 89 (N89), but not proteins lacking either N23 or N110, were retained within the cell and were not detected on the cell surface membrane.
19931508	8	59	theme	mechanistic	1373:1383	arg1	understanding					1385:1397	the current mechanistic understanding	1361:1397	the current mechanistic understanding of the necessity	1361:1414	This study represents a substantial contribution to the current mechanistic understanding of the necessity and potential functions of a specific N-glycan among the multiple glycans of glycoproteins.
19931508	7	60	gly	glycosylation	1174:1186	arg2	three					1154:1158	three	1154:1158	three	1154:1158	These data suggest that amongst the three putative ICOS glycosylation sites, N89 is required for proper ICOS protein folding in the ER, intracellular trafficking and ligand binding activity.
19931508	7	60	gly	glycosylation	1174:1186	arg2	sites					1188:1192	the three putative ICOS glycosylation sites	1150:1192	the three putative ICOS glycosylation sites	1150:1192	These data suggest that amongst the three putative ICOS glycosylation sites, N89 is required for proper ICOS protein folding in the ER, intracellular trafficking and ligand binding activity.
19931508	4	61	theme	surface	768:774	arg1	membrane					776:783	the cell surface membrane	759:783	the cell surface membrane	759:783	Here we demonstrate the integral involvement of a specific N-glycan from amongst the three glycans present on inducible costimulator (ICOS), a T-cell costimulatory molecule, in proper protein folding and intracellular trafficking to the cell surface membrane.
19931508	7	62	theme	putative	1160:1167	arg1	sites					1188:1192	the three putative ICOS glycosylation sites	1150:1192	the three putative ICOS glycosylation sites	1150:1192	These data suggest that amongst the three putative ICOS glycosylation sites, N89 is required for proper ICOS protein folding in the ER, intracellular trafficking and ligand binding activity.
19931508	7	63	from	activity	1299:1306	arg1	ER					1250:1251	the ER	1246:1251	the ER	1246:1251	These data suggest that amongst the three putative ICOS glycosylation sites, N89 is required for proper ICOS protein folding in the ER, intracellular trafficking and ligand binding activity.
19931508	4	64	theme	protein	710:716	arg1	folding					718:724	proper protein folding	703:724	proper protein folding	703:724	Here we demonstrate the integral involvement of a specific N-glycan from amongst the three glycans present on inducible costimulator (ICOS), a T-cell costimulatory molecule, in proper protein folding and intracellular trafficking to the cell surface membrane.
19931508	4	65	from	folding	718:724	arg1	present					625:631	present	625:631	present	625:631	Here we demonstrate the integral involvement of a specific N-glycan from amongst the three glycans present on inducible costimulator (ICOS), a T-cell costimulatory molecule, in proper protein folding and intracellular trafficking to the cell surface membrane.
19931508	4	66	from	present	625:631	arg1	trafficking					744:754	intracellular trafficking	730:754	intracellular trafficking to the cell surface membrane	730:783	Here we demonstrate the integral involvement of a specific N-glycan from amongst the three glycans present on inducible costimulator (ICOS), a T-cell costimulatory molecule, in proper protein folding and intracellular trafficking to the cell surface membrane.
19931508	4	66	from	present	625:631	arg1	folding					718:724	proper protein folding	703:724	proper protein folding	703:724	Here we demonstrate the integral involvement of a specific N-glycan from amongst the three glycans present on inducible costimulator (ICOS), a T-cell costimulatory molecule, in proper protein folding and intracellular trafficking to the cell surface membrane.
19931508	2	67	theme	protein	264:270	arg1	folding					272:278	protein folding	264:278	protein folding	264:278	Glycans play key roles in protein folding, quality control in the endoplasmic reticulum (ER) and protein trafficking within cells.
19931508	7	68	theme	ligand	1284:1289	arg1	activity					1299:1306	ligand binding activity	1284:1306	ligand binding activity	1284:1306	These data suggest that amongst the three putative ICOS glycosylation sites, N89 is required for proper ICOS protein folding in the ER, intracellular trafficking and ligand binding activity.
19931508	4	69	theme	costimulatory	676:688	arg1	molecule					690:697	a T-cell costimulatory molecule	667:697	a T-cell costimulatory molecule	667:697	Here we demonstrate the integral involvement of a specific N-glycan from amongst the three glycans present on inducible costimulator (ICOS), a T-cell costimulatory molecule, in proper protein folding and intracellular trafficking to the cell surface membrane.
19931508	4	69	theme	costimulatory	676:688	arg1	costimulator					646:657	inducible costimulator	636:657	inducible costimulator (ICOS)	636:664	Here we demonstrate the integral involvement of a specific N-glycan from amongst the three glycans present on inducible costimulator (ICOS), a T-cell costimulatory molecule, in proper protein folding and intracellular trafficking to the cell surface membrane.
19931508	4	70	theme	present	625:631	arg1	glycans					617:623	the three glycans	607:623	the three glycans present on inducible costimulator (ICOS), a T-cell costimulatory molecule, in proper protein folding and intracellular trafficking to the cell surface membrane	607:783	Here we demonstrate the integral involvement of a specific N-glycan from amongst the three glycans present on inducible costimulator (ICOS), a T-cell costimulatory molecule, in proper protein folding and intracellular trafficking to the cell surface membrane.
19931508	7	71	theme	proper	1215:1220	arg1	folding					1235:1241	proper ICOS protein folding	1215:1241	proper ICOS protein folding in the ER	1215:1251	These data suggest that amongst the three putative ICOS glycosylation sites, N89 is required for proper ICOS protein folding in the ER, intracellular trafficking and ligand binding activity.
19931508	7	72	theme	glycosylation	1174:1186	arg1	sites					1188:1192	the three putative ICOS glycosylation sites	1150:1192	the three putative ICOS glycosylation sites	1150:1192	These data suggest that amongst the three putative ICOS glycosylation sites, N89 is required for proper ICOS protein folding in the ER, intracellular trafficking and ligand binding activity.
19931508	4	73	theme	T-cell	669:674	arg1	molecule					690:697	a T-cell costimulatory molecule	667:697	a T-cell costimulatory molecule	667:697	Here we demonstrate the integral involvement of a specific N-glycan from amongst the three glycans present on inducible costimulator (ICOS), a T-cell costimulatory molecule, in proper protein folding and intracellular trafficking to the cell surface membrane.
19931508	4	73	theme	T-cell	669:674	arg1	costimulator					646:657	inducible costimulator	636:657	inducible costimulator (ICOS)	636:664	Here we demonstrate the integral involvement of a specific N-glycan from amongst the three glycans present on inducible costimulator (ICOS), a T-cell costimulatory molecule, in proper protein folding and intracellular trafficking to the cell surface membrane.
19931508	7	74	theme	ICOS	1169:1172	arg1	sites					1188:1192	the three putative ICOS glycosylation sites	1150:1192	the three putative ICOS glycosylation sites	1150:1192	These data suggest that amongst the three putative ICOS glycosylation sites, N89 is required for proper ICOS protein folding in the ER, intracellular trafficking and ligand binding activity.
16335952	7	0	theme	factor	1597:1602	arg1	ng/mL					1628:1632	approximately 2 ng/mL	1612:1632	approximately 2 ng/mL	1612:1632	This enrichment strategy significantly improved detection and enabled identification of a number of low-abundance proteins, exemplified by interleukin-1 receptor antagonist protein (approximately 200 pg/mL), cathepsin L (approximately 1 ng/mL), and transforming growth factor beta 1 (approximately 2 ng/mL).
16335952	7	0	theme	factor	1597:1602	arg1	beta					1604:1607	transforming growth factor beta 1	1577:1609	transforming growth factor beta 1 (approximately 2 ng/mL)	1577:1633	This enrichment strategy significantly improved detection and enabled identification of a number of low-abundance proteins, exemplified by interleukin-1 receptor antagonist protein (approximately 200 pg/mL), cathepsin L (approximately 1 ng/mL), and transforming growth factor beta 1 (approximately 2 ng/mL).
16335952	2	1	theme	concentration	617:629	arg1	range					631:635	the protein concentration range	605:635	the protein concentration range	605:635	Here, we describe an approach for broad analysis of human plasma N-glycoproteins using a combination of immunoaffinity subtraction and glycoprotein capture to reduce both the protein concentration range and the overall sample complexity.
16335952	8	2	theme	mass	1784:1787	arg1	measurement					1789:1799	accurate mass measurement	1775:1799	accurate mass measurement using high-resolution liquid chromatography coupled to Fourier transform ion cyclotron resonance mass spectrometry (LC-FTICR)	1775:1925	A total of 639 N-glycosylation sites were identified, and the overall high accuracy of these glycosylation site assignments as assessed by accurate mass measurement using high-resolution liquid chromatography coupled to Fourier transform ion cyclotron resonance mass spectrometry (LC-FTICR) is initially demonstrated.
16335952	4	3	theme	N-linked	915:922	arg1	glycopeptides					924:936	the bound N-linked glycopeptides	905:936	the bound N-linked glycopeptides	905:936	N-linked glycoproteins were then captured from the depleted plasma using hydrazide resin and enzymatically digested, and the bound N-linked glycopeptides were released using peptide-N-glycosidase F (PNGase F).
16335952	7	4	theme	transforming	1577:1588	arg1	ng/mL					1628:1632	approximately 2 ng/mL	1612:1632	approximately 2 ng/mL	1612:1632	This enrichment strategy significantly improved detection and enabled identification of a number of low-abundance proteins, exemplified by interleukin-1 receptor antagonist protein (approximately 200 pg/mL), cathepsin L (approximately 1 ng/mL), and transforming growth factor beta 1 (approximately 2 ng/mL).
16335952	7	4	theme	transforming	1577:1588	arg1	beta					1604:1607	transforming growth factor beta 1	1577:1609	transforming growth factor beta 1 (approximately 2 ng/mL)	1577:1633	This enrichment strategy significantly improved detection and enabled identification of a number of low-abundance proteins, exemplified by interleukin-1 receptor antagonist protein (approximately 200 pg/mL), cathepsin L (approximately 1 ng/mL), and transforming growth factor beta 1 (approximately 2 ng/mL).
16335952	6	5	theme	nonredundant	1298:1309	arg1	N-glycoproteins					1311:1325	303 nonredundant N-glycoproteins	1294:1325	303 nonredundant N-glycoproteins	1294:1325	Using stringent criteria, a total of 2053 different N-glycopeptides were confidently identified, covering 303 nonredundant N-glycoproteins.
16335952	3	6	theme	immobilized	755:765	arg1	column					776:781	a pre-packed, immobilized antibody column	741:781	column	776:781	Six high-abundance plasma proteins were simultaneously removed using a pre-packed, immobilized antibody column.
16335952	2	7	theme	overall	645:651	arg1	complexity					660:669	the overall sample complexity	641:669	the overall sample complexity	641:669	Here, we describe an approach for broad analysis of human plasma N-glycoproteins using a combination of immunoaffinity subtraction and glycoprotein capture to reduce both the protein concentration range and the overall sample complexity.
16335952	7	8	theme	cathepsin	1536:1544	arg1	L					1546:1546	cathepsin L	1536:1546	cathepsin L (approximately 1 ng/mL)	1536:1570	This enrichment strategy significantly improved detection and enabled identification of a number of low-abundance proteins, exemplified by interleukin-1 receptor antagonist protein (approximately 200 pg/mL), cathepsin L (approximately 1 ng/mL), and transforming growth factor beta 1 (approximately 2 ng/mL).
16335952	7	8	theme	cathepsin	1536:1544	arg1	ng/mL					1565:1569	approximately 1 ng/mL	1549:1569	approximately 1 ng/mL	1549:1569	This enrichment strategy significantly improved detection and enabled identification of a number of low-abundance proteins, exemplified by interleukin-1 receptor antagonist protein (approximately 200 pg/mL), cathepsin L (approximately 1 ng/mL), and transforming growth factor beta 1 (approximately 2 ng/mL).
16335952	3	9	theme	pre-packed	743:752	arg1	column					776:781	a pre-packed, immobilized antibody column	741:781	column	776:781	Six high-abundance plasma proteins were simultaneously removed using a pre-packed, immobilized antibody column.
16335952	8	10	theme	liquid	1823:1828	arg1	chromatography					1830:1843	high-resolution liquid chromatography	1807:1843	high-resolution liquid chromatography coupled to Fourier transform ion cyclotron resonance mass spectrometry (LC-FTICR)	1807:1925	A total of 639 N-glycosylation sites were identified, and the overall high accuracy of these glycosylation site assignments as assessed by accurate mass measurement using high-resolution liquid chromatography coupled to Fourier transform ion cyclotron resonance mass spectrometry (LC-FTICR) is initially demonstrated.
16335952	1	11	theme	abundances	177:186	arg1	range					151:155	wide dynamic range	138:155	wide dynamic range of relative protein abundances of interest (over 10 orders of magnitude)	138:228	The enormous complexity, wide dynamic range of relative protein abundances of interest (over 10 orders of magnitude), and tremendous heterogeneity (due to post-translational modifications, such as glycosylation) of the human blood plasma proteome severely challenge the capabilities of existing analytical methodologies.
16335952	1	11	theme	abundances	177:186	arg1	heterogeneity					246:258	tremendous heterogeneity	235:258	tremendous heterogeneity (due to post-translational modifications, such as glycosylation) of the human blood plasma proteome	235:358	The enormous complexity, wide dynamic range of relative protein abundances of interest (over 10 orders of magnitude), and tremendous heterogeneity (due to post-translational modifications, such as glycosylation) of the human blood plasma proteome severely challenge the capabilities of existing analytical methodologies.
16335952	1	11	theme	abundances	177:186	arg1	complexity					126:135	The enormous complexity	113:135	The enormous complexity	113:135	The enormous complexity, wide dynamic range of relative protein abundances of interest (over 10 orders of magnitude), and tremendous heterogeneity (due to post-translational modifications, such as glycosylation) of the human blood plasma proteome severely challenge the capabilities of existing analytical methodologies.
16335952	1	12	theme	existing	399:406	arg1	methodologies					419:431	existing analytical methodologies	399:431	existing analytical methodologies	399:431	The enormous complexity, wide dynamic range of relative protein abundances of interest (over 10 orders of magnitude), and tremendous heterogeneity (due to post-translational modifications, such as glycosylation) of the human blood plasma proteome severely challenge the capabilities of existing analytical methodologies.
16335952	1	13	theme	interest	191:198	arg1	abundances					177:186	relative protein abundances	160:186	relative protein abundances of interest (over 10 orders of magnitude)	160:228	The enormous complexity, wide dynamic range of relative protein abundances of interest (over 10 orders of magnitude), and tremendous heterogeneity (due to post-translational modifications, such as glycosylation) of the human blood plasma proteome severely challenge the capabilities of existing analytical methodologies.
16335952	4	14	theme	PNGase	983:988	arg1	F					980:980	peptide-N-glycosidase F	958:980	peptide-N-glycosidase F (PNGase F)	958:991	N-linked glycoproteins were then captured from the depleted plasma using hydrazide resin and enzymatically digested, and the bound N-linked glycopeptides were released using peptide-N-glycosidase F (PNGase F).
16335952	4	14	theme	PNGase	983:988	arg1	F					990:990	PNGase F	983:990	PNGase F	983:990	N-linked glycoproteins were then captured from the depleted plasma using hydrazide resin and enzymatically digested, and the bound N-linked glycopeptides were released using peptide-N-glycosidase F (PNGase F).
16335952	4	15	theme	bound	909:913	arg1	glycopeptides					924:936	the bound N-linked glycopeptides	905:936	the bound N-linked glycopeptides	905:936	N-linked glycoproteins were then captured from the depleted plasma using hydrazide resin and enzymatically digested, and the bound N-linked glycopeptides were released using peptide-N-glycosidase F (PNGase F).
16335952	8	16	theme	Fourier	1856:1862	arg1	spectrometry					1903:1914	Fourier transform ion cyclotron resonance mass spectrometry	1856:1914	Fourier transform ion cyclotron resonance mass spectrometry (LC-FTICR)	1856:1925	A total of 639 N-glycosylation sites were identified, and the overall high accuracy of these glycosylation site assignments as assessed by accurate mass measurement using high-resolution liquid chromatography coupled to Fourier transform ion cyclotron resonance mass spectrometry (LC-FTICR) is initially demonstrated.
16335952	8	16	theme	Fourier	1856:1862	arg1	LC-FTICR					1917:1924	LC-FTICR	1917:1924	LC-FTICR	1917:1924	A total of 639 N-glycosylation sites were identified, and the overall high accuracy of these glycosylation site assignments as assessed by accurate mass measurement using high-resolution liquid chromatography coupled to Fourier transform ion cyclotron resonance mass spectrometry (LC-FTICR) is initially demonstrated.
16335952	2	17	theme	immunoaffinity	538:551	arg1	subtraction					553:563	immunoaffinity subtraction	538:563	immunoaffinity subtraction	538:563	Here, we describe an approach for broad analysis of human plasma N-glycoproteins using a combination of immunoaffinity subtraction and glycoprotein capture to reduce both the protein concentration range and the overall sample complexity.
16335952	1	18	theme	tremendous	235:244	arg1	heterogeneity					246:258	tremendous heterogeneity	235:258	tremendous heterogeneity (due to post-translational modifications, such as glycosylation) of the human blood plasma proteome	235:358	The enormous complexity, wide dynamic range of relative protein abundances of interest (over 10 orders of magnitude), and tremendous heterogeneity (due to post-translational modifications, such as glycosylation) of the human blood plasma proteome severely challenge the capabilities of existing analytical methodologies.
16335952	5	19	theme	tandem	1151:1156	arg1	LC-MS/MS					1177:1184	LC-MS/MS	1177:1184	LC-MS/MS	1177:1184	Following strong cation exchange (SCX) fractionation, the deglycosylated peptides were analyzed by reversed-phase capillary liquid chromatography coupled to tandem mass spectrometry (LC-MS/MS).
16335952	5	19	theme	tandem	1151:1156	arg1	spectrometry					1163:1174	tandem mass spectrometry	1151:1174	tandem mass spectrometry (LC-MS/MS)	1151:1185	Following strong cation exchange (SCX) fractionation, the deglycosylated peptides were analyzed by reversed-phase capillary liquid chromatography coupled to tandem mass spectrometry (LC-MS/MS).
16335952	8	20	theme	ion	1874:1876	arg1	spectrometry					1903:1914	Fourier transform ion cyclotron resonance mass spectrometry	1856:1914	Fourier transform ion cyclotron resonance mass spectrometry (LC-FTICR)	1856:1925	A total of 639 N-glycosylation sites were identified, and the overall high accuracy of these glycosylation site assignments as assessed by accurate mass measurement using high-resolution liquid chromatography coupled to Fourier transform ion cyclotron resonance mass spectrometry (LC-FTICR) is initially demonstrated.
16335952	8	20	theme	ion	1874:1876	arg1	LC-FTICR					1917:1924	LC-FTICR	1917:1924	LC-FTICR	1917:1924	A total of 639 N-glycosylation sites were identified, and the overall high accuracy of these glycosylation site assignments as assessed by accurate mass measurement using high-resolution liquid chromatography coupled to Fourier transform ion cyclotron resonance mass spectrometry (LC-FTICR) is initially demonstrated.
16335952	7	21	theme	antagonist	1490:1499	arg1	protein					1501:1507	interleukin-1 receptor antagonist protein	1467:1507	interleukin-1 receptor antagonist protein (approximately 200 pg/mL)	1467:1533	This enrichment strategy significantly improved detection and enabled identification of a number of low-abundance proteins, exemplified by interleukin-1 receptor antagonist protein (approximately 200 pg/mL), cathepsin L (approximately 1 ng/mL), and transforming growth factor beta 1 (approximately 2 ng/mL).
16335952	7	21	theme	antagonist	1490:1499	arg1	pg/mL					1528:1532	approximately 200 pg/mL	1510:1532	approximately 200 pg/mL	1510:1532	This enrichment strategy significantly improved detection and enabled identification of a number of low-abundance proteins, exemplified by interleukin-1 receptor antagonist protein (approximately 200 pg/mL), cathepsin L (approximately 1 ng/mL), and transforming growth factor beta 1 (approximately 2 ng/mL).
16335952	5	22	theme	reversed-phase	1093:1106	arg1	chromatography					1125:1138	reversed-phase capillary liquid chromatography	1093:1138	reversed-phase capillary liquid chromatography coupled to tandem mass spectrometry (LC-MS/MS)	1093:1185	Following strong cation exchange (SCX) fractionation, the deglycosylated peptides were analyzed by reversed-phase capillary liquid chromatography coupled to tandem mass spectrometry (LC-MS/MS).
16335952	1	23	theme	analytical	408:417	arg1	methodologies					419:431	existing analytical methodologies	399:431	existing analytical methodologies	399:431	The enormous complexity, wide dynamic range of relative protein abundances of interest (over 10 orders of magnitude), and tremendous heterogeneity (due to post-translational modifications, such as glycosylation) of the human blood plasma proteome severely challenge the capabilities of existing analytical methodologies.
16335952	8	24	theme	resonance	1888:1896	arg1	spectrometry					1903:1914	Fourier transform ion cyclotron resonance mass spectrometry	1856:1914	Fourier transform ion cyclotron resonance mass spectrometry (LC-FTICR)	1856:1925	A total of 639 N-glycosylation sites were identified, and the overall high accuracy of these glycosylation site assignments as assessed by accurate mass measurement using high-resolution liquid chromatography coupled to Fourier transform ion cyclotron resonance mass spectrometry (LC-FTICR) is initially demonstrated.
16335952	8	24	theme	resonance	1888:1896	arg1	LC-FTICR					1917:1924	LC-FTICR	1917:1924	LC-FTICR	1917:1924	A total of 639 N-glycosylation sites were identified, and the overall high accuracy of these glycosylation site assignments as assessed by accurate mass measurement using high-resolution liquid chromatography coupled to Fourier transform ion cyclotron resonance mass spectrometry (LC-FTICR) is initially demonstrated.
16335952	2	25	theme	capture	582:588	arg1	combination					523:533	a combination	521:533	a combination of immunoaffinity subtraction and glycoprotein capture to reduce both the protein concentration range and the overall sample complexity	521:669	Here, we describe an approach for broad analysis of human plasma N-glycoproteins using a combination of immunoaffinity subtraction and glycoprotein capture to reduce both the protein concentration range and the overall sample complexity.
16335952	7	26	theme	interleukin-1	1467:1479	arg1	protein					1501:1507	interleukin-1 receptor antagonist protein	1467:1507	interleukin-1 receptor antagonist protein (approximately 200 pg/mL)	1467:1533	This enrichment strategy significantly improved detection and enabled identification of a number of low-abundance proteins, exemplified by interleukin-1 receptor antagonist protein (approximately 200 pg/mL), cathepsin L (approximately 1 ng/mL), and transforming growth factor beta 1 (approximately 2 ng/mL).
16335952	7	26	theme	interleukin-1	1467:1479	arg1	pg/mL					1528:1532	approximately 200 pg/mL	1510:1532	approximately 200 pg/mL	1510:1532	This enrichment strategy significantly improved detection and enabled identification of a number of low-abundance proteins, exemplified by interleukin-1 receptor antagonist protein (approximately 200 pg/mL), cathepsin L (approximately 1 ng/mL), and transforming growth factor beta 1 (approximately 2 ng/mL).
16335952	1	27	theme	methodologies	419:431	arg1	capabilities					383:394	the capabilities	379:394	the capabilities of existing analytical methodologies	379:431	The enormous complexity, wide dynamic range of relative protein abundances of interest (over 10 orders of magnitude), and tremendous heterogeneity (due to post-translational modifications, such as glycosylation) of the human blood plasma proteome severely challenge the capabilities of existing analytical methodologies.
16335952	1	28	theme	wide	138:141	arg1	range					151:155	wide dynamic range	138:155	wide dynamic range of relative protein abundances of interest (over 10 orders of magnitude)	138:228	The enormous complexity, wide dynamic range of relative protein abundances of interest (over 10 orders of magnitude), and tremendous heterogeneity (due to post-translational modifications, such as glycosylation) of the human blood plasma proteome severely challenge the capabilities of existing analytical methodologies.
16335952	2	29	theme	plasma	492:497	arg1	N-glycoproteins					499:513	human plasma N-glycoproteins	486:513	human plasma N-glycoproteins	486:513	Here, we describe an approach for broad analysis of human plasma N-glycoproteins using a combination of immunoaffinity subtraction and glycoprotein capture to reduce both the protein concentration range and the overall sample complexity.
16335952	0	30	theme	hydrazide	69:77	arg1	chemistry					79:87	hydrazide chemistry	69:87	hydrazide chemistry	69:87	Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry.
16335952	2	31	theme	glycoprotein	569:580	arg1	capture					582:588	glycoprotein capture	569:588	glycoprotein capture	569:588	Here, we describe an approach for broad analysis of human plasma N-glycoproteins using a combination of immunoaffinity subtraction and glycoprotein capture to reduce both the protein concentration range and the overall sample complexity.
16335952	8	32	dep	accuracy	1711:1718	arg1	assessed					1763:1770	assessed	1763:1770	assessed by accurate mass measurement using high-resolution liquid chromatography coupled to Fourier transform ion cyclotron resonance mass spectrometry (LC-FTICR)	1763:1925	A total of 639 N-glycosylation sites were identified, and the overall high accuracy of these glycosylation site assignments as assessed by accurate mass measurement using high-resolution liquid chromatography coupled to Fourier transform ion cyclotron resonance mass spectrometry (LC-FTICR) is initially demonstrated.
16335952	5	33	theme	liquid	1118:1123	arg1	chromatography					1125:1138	reversed-phase capillary liquid chromatography	1093:1138	reversed-phase capillary liquid chromatography coupled to tandem mass spectrometry (LC-MS/MS)	1093:1185	Following strong cation exchange (SCX) fractionation, the deglycosylated peptides were analyzed by reversed-phase capillary liquid chromatography coupled to tandem mass spectrometry (LC-MS/MS).
16335952	1	34	theme	relative	160:167	arg1	abundances					177:186	relative protein abundances	160:186	relative protein abundances of interest (over 10 orders of magnitude)	160:228	The enormous complexity, wide dynamic range of relative protein abundances of interest (over 10 orders of magnitude), and tremendous heterogeneity (due to post-translational modifications, such as glycosylation) of the human blood plasma proteome severely challenge the capabilities of existing analytical methodologies.
16335952	0	35	theme	mass	94:97	arg1	spectrometry					99:110	mass spectrometry	94:110	mass spectrometry	94:110	Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry.
16335952	1	36	theme	blood	338:342	arg1	proteome					351:358	the human blood plasma proteome	328:358	the human blood plasma proteome	328:358	The enormous complexity, wide dynamic range of relative protein abundances of interest (over 10 orders of magnitude), and tremendous heterogeneity (due to post-translational modifications, such as glycosylation) of the human blood plasma proteome severely challenge the capabilities of existing analytical methodologies.
16335952	2	37	theme	sample	653:658	arg1	complexity					660:669	the overall sample complexity	641:669	the overall sample complexity	641:669	Here, we describe an approach for broad analysis of human plasma N-glycoproteins using a combination of immunoaffinity subtraction and glycoprotein capture to reduce both the protein concentration range and the overall sample complexity.
16335952	4	38	gly	glycoproteins	793:805	arg1	glycoproteins					793:805	N-linked glycoproteins	784:805	N-linked glycoproteins	784:805	N-linked glycoproteins were then captured from the depleted plasma using hydrazide resin and enzymatically digested, and the bound N-linked glycopeptides were released using peptide-N-glycosidase F (PNGase F).
16335952	1	39	theme	proteome	351:358	arg1	range					151:155	wide dynamic range	138:155	wide dynamic range of relative protein abundances of interest (over 10 orders of magnitude)	138:228	The enormous complexity, wide dynamic range of relative protein abundances of interest (over 10 orders of magnitude), and tremendous heterogeneity (due to post-translational modifications, such as glycosylation) of the human blood plasma proteome severely challenge the capabilities of existing analytical methodologies.
16335952	1	39	theme	proteome	351:358	arg1	heterogeneity					246:258	tremendous heterogeneity	235:258	tremendous heterogeneity (due to post-translational modifications, such as glycosylation) of the human blood plasma proteome	235:358	The enormous complexity, wide dynamic range of relative protein abundances of interest (over 10 orders of magnitude), and tremendous heterogeneity (due to post-translational modifications, such as glycosylation) of the human blood plasma proteome severely challenge the capabilities of existing analytical methodologies.
16335952	1	39	theme	proteome	351:358	arg1	complexity					126:135	The enormous complexity	113:135	The enormous complexity	113:135	The enormous complexity, wide dynamic range of relative protein abundances of interest (over 10 orders of magnitude), and tremendous heterogeneity (due to post-translational modifications, such as glycosylation) of the human blood plasma proteome severely challenge the capabilities of existing analytical methodologies.
16335952	0	40	theme	Human	0:4	arg1	N-glycoproteome					13:27	Human plasma N-glycoproteome	0:27	Human plasma N-glycoproteome	0:27	Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry.
16335952	7	41	theme	low-abundance	1428:1440	arg1	proteins					1442:1449	low-abundance proteins	1428:1449	low-abundance proteins	1428:1449	This enrichment strategy significantly improved detection and enabled identification of a number of low-abundance proteins, exemplified by interleukin-1 receptor antagonist protein (approximately 200 pg/mL), cathepsin L (approximately 1 ng/mL), and transforming growth factor beta 1 (approximately 2 ng/mL).
16335952	1	42	theme	post-translational	268:285	arg1	modifications					287:299	post-translational modifications	268:299	post-translational modifications	268:299	The enormous complexity, wide dynamic range of relative protein abundances of interest (over 10 orders of magnitude), and tremendous heterogeneity (due to post-translational modifications, such as glycosylation) of the human blood plasma proteome severely challenge the capabilities of existing analytical methodologies.
16335952	6	43	theme	different	1230:1238	arg1	N-glycopeptides					1240:1254	2053 different N-glycopeptides	1225:1254	2053 different N-glycopeptides	1225:1254	Using stringent criteria, a total of 2053 different N-glycopeptides were confidently identified, covering 303 nonredundant N-glycoproteins.
16335952	8	44	gly	glycosylation	1729:1741	arg2	site					1743:1746	these glycosylation site assignments	1723:1758	these glycosylation site assignments	1723:1758	A total of 639 N-glycosylation sites were identified, and the overall high accuracy of these glycosylation site assignments as assessed by accurate mass measurement using high-resolution liquid chromatography coupled to Fourier transform ion cyclotron resonance mass spectrometry (LC-FTICR) is initially demonstrated.
16335952	8	44	gly	glycosylation	1729:1741	arg2	assignments					1748:1758	these glycosylation site assignments	1723:1758	these glycosylation site assignments	1723:1758	A total of 639 N-glycosylation sites were identified, and the overall high accuracy of these glycosylation site assignments as assessed by accurate mass measurement using high-resolution liquid chromatography coupled to Fourier transform ion cyclotron resonance mass spectrometry (LC-FTICR) is initially demonstrated.
16335952	5	45	theme	cation	1011:1016	arg1	fractionation					1033:1045	strong cation exchange (SCX) fractionation	1004:1045	strong cation exchange (SCX) fractionation	1004:1045	Following strong cation exchange (SCX) fractionation, the deglycosylated peptides were analyzed by reversed-phase capillary liquid chromatography coupled to tandem mass spectrometry (LC-MS/MS).
16335952	7	46	theme	number	1418:1423	arg1	identification					1398:1411	identification	1398:1411	identification of a number of low-abundance proteins, exemplified by interleukin-1 receptor antagonist protein (approximately 200 pg/mL), cathepsin L (approximately 1 ng/mL), and transforming growth factor beta 1 (approximately 2 ng/mL)	1398:1633	This enrichment strategy significantly improved detection and enabled identification of a number of low-abundance proteins, exemplified by interleukin-1 receptor antagonist protein (approximately 200 pg/mL), cathepsin L (approximately 1 ng/mL), and transforming growth factor beta 1 (approximately 2 ng/mL).
16335952	2	47	theme	broad	468:472	arg1	analysis					474:481	broad analysis	468:481	broad analysis of human plasma N-glycoproteins	468:513	Here, we describe an approach for broad analysis of human plasma N-glycoproteins using a combination of immunoaffinity subtraction and glycoprotein capture to reduce both the protein concentration range and the overall sample complexity.
16335952	5	48	gly	deglycosylated	1052:1065	arg1	peptides					1067:1074	the deglycosylated peptides	1048:1074	the deglycosylated peptides	1048:1074	Following strong cation exchange (SCX) fractionation, the deglycosylated peptides were analyzed by reversed-phase capillary liquid chromatography coupled to tandem mass spectrometry (LC-MS/MS).
16335952	8	49	theme	N-glycosylation	1651:1665	arg1	sites					1667:1671	639 N-glycosylation sites	1647:1671	639 N-glycosylation sites	1647:1671	A total of 639 N-glycosylation sites were identified, and the overall high accuracy of these glycosylation site assignments as assessed by accurate mass measurement using high-resolution liquid chromatography coupled to Fourier transform ion cyclotron resonance mass spectrometry (LC-FTICR) is initially demonstrated.
16335952	6	50	theme	stringent	1194:1202	arg1	criteria					1204:1211	stringent criteria	1194:1211	stringent criteria	1194:1211	Using stringent criteria, a total of 2053 different N-glycopeptides were confidently identified, covering 303 nonredundant N-glycoproteins.
16335952	4	51	theme	depleted	835:842	arg1	plasma					844:849	the depleted plasma	831:849	the depleted plasma	831:849	N-linked glycoproteins were then captured from the depleted plasma using hydrazide resin and enzymatically digested, and the bound N-linked glycopeptides were released using peptide-N-glycosidase F (PNGase F).
16335952	8	52	theme	glycosylation	1729:1741	arg1	assignments					1748:1758	these glycosylation site assignments	1723:1758	these glycosylation site assignments	1723:1758	A total of 639 N-glycosylation sites were identified, and the overall high accuracy of these glycosylation site assignments as assessed by accurate mass measurement using high-resolution liquid chromatography coupled to Fourier transform ion cyclotron resonance mass spectrometry (LC-FTICR) is initially demonstrated.
16335952	8	53	dep	spectrometry	1903:1914	arg1	transform					1864:1872	transform	1864:1872	transform	1864:1872	A total of 639 N-glycosylation sites were identified, and the overall high accuracy of these glycosylation site assignments as assessed by accurate mass measurement using high-resolution liquid chromatography coupled to Fourier transform ion cyclotron resonance mass spectrometry (LC-FTICR) is initially demonstrated.
16335952	3	54	theme	plasma	691:696	arg1	proteins					698:705	Six high-abundance plasma proteins	672:705	Six high-abundance plasma proteins	672:705	Six high-abundance plasma proteins were simultaneously removed using a pre-packed, immobilized antibody column.
16335952	8	55	theme	assignments	1748:1758	arg1	accuracy					1711:1718	the overall high accuracy	1694:1718	the overall high accuracy of these glycosylation site assignments as assessed by accurate mass measurement using high-resolution liquid chromatography coupled to Fourier transform ion cyclotron resonance mass spectrometry (LC-FTICR)	1694:1925	A total of 639 N-glycosylation sites were identified, and the overall high accuracy of these glycosylation site assignments as assessed by accurate mass measurement using high-resolution liquid chromatography coupled to Fourier transform ion cyclotron resonance mass spectrometry (LC-FTICR) is initially demonstrated.
16335952	7	56	theme	growth	1590:1595	arg1	ng/mL					1628:1632	approximately 2 ng/mL	1612:1632	approximately 2 ng/mL	1612:1632	This enrichment strategy significantly improved detection and enabled identification of a number of low-abundance proteins, exemplified by interleukin-1 receptor antagonist protein (approximately 200 pg/mL), cathepsin L (approximately 1 ng/mL), and transforming growth factor beta 1 (approximately 2 ng/mL).
16335952	7	56	theme	growth	1590:1595	arg1	beta					1604:1607	transforming growth factor beta 1	1577:1609	transforming growth factor beta 1 (approximately 2 ng/mL)	1577:1633	This enrichment strategy significantly improved detection and enabled identification of a number of low-abundance proteins, exemplified by interleukin-1 receptor antagonist protein (approximately 200 pg/mL), cathepsin L (approximately 1 ng/mL), and transforming growth factor beta 1 (approximately 2 ng/mL).
16335952	5	57	theme	deglycosylated	1052:1065	arg1	peptides					1067:1074	the deglycosylated peptides	1048:1074	the deglycosylated peptides	1048:1074	Following strong cation exchange (SCX) fractionation, the deglycosylated peptides were analyzed by reversed-phase capillary liquid chromatography coupled to tandem mass spectrometry (LC-MS/MS).
16335952	4	58	link	N-linked	784:791	arg1	glycoproteins					793:805	N-linked glycoproteins	784:805	N-linked glycoproteins	784:805	N-linked glycoproteins were then captured from the depleted plasma using hydrazide resin and enzymatically digested, and the bound N-linked glycopeptides were released using peptide-N-glycosidase F (PNGase F).
16335952	2	59	theme	protein	609:615	arg1	range					631:635	the protein concentration range	605:635	the protein concentration range	605:635	Here, we describe an approach for broad analysis of human plasma N-glycoproteins using a combination of immunoaffinity subtraction and glycoprotein capture to reduce both the protein concentration range and the overall sample complexity.
16335952	7	60	theme	enrichment	1333:1342	arg1	strategy					1344:1351	This enrichment strategy	1328:1351	This enrichment strategy	1328:1351	This enrichment strategy significantly improved detection and enabled identification of a number of low-abundance proteins, exemplified by interleukin-1 receptor antagonist protein (approximately 200 pg/mL), cathepsin L (approximately 1 ng/mL), and transforming growth factor beta 1 (approximately 2 ng/mL).
16335952	8	61	theme	high	1706:1709	arg1	accuracy					1711:1718	the overall high accuracy	1694:1718	the overall high accuracy of these glycosylation site assignments as assessed by accurate mass measurement using high-resolution liquid chromatography coupled to Fourier transform ion cyclotron resonance mass spectrometry (LC-FTICR)	1694:1925	A total of 639 N-glycosylation sites were identified, and the overall high accuracy of these glycosylation site assignments as assessed by accurate mass measurement using high-resolution liquid chromatography coupled to Fourier transform ion cyclotron resonance mass spectrometry (LC-FTICR) is initially demonstrated.
16335952	6	62	gly	N-glycoproteins	1311:1325	arg1	N-glycoproteins					1311:1325	303 nonredundant N-glycoproteins	1294:1325	303 nonredundant N-glycoproteins	1294:1325	Using stringent criteria, a total of 2053 different N-glycopeptides were confidently identified, covering 303 nonredundant N-glycoproteins.
16335952	8	63	theme	accurate	1775:1782	arg1	measurement					1789:1799	accurate mass measurement	1775:1799	accurate mass measurement using high-resolution liquid chromatography coupled to Fourier transform ion cyclotron resonance mass spectrometry (LC-FTICR)	1775:1925	A total of 639 N-glycosylation sites were identified, and the overall high accuracy of these glycosylation site assignments as assessed by accurate mass measurement using high-resolution liquid chromatography coupled to Fourier transform ion cyclotron resonance mass spectrometry (LC-FTICR) is initially demonstrated.
16335952	6	64	theme	N-glycopeptides	1240:1254	arg1	total					1216:1220	a total	1214:1220	a total of 2053 different N-glycopeptides	1214:1254	Using stringent criteria, a total of 2053 different N-glycopeptides were confidently identified, covering 303 nonredundant N-glycoproteins.
16335952	3	65	theme	antibody	767:774	arg1	column					776:781	a pre-packed, immobilized antibody column	741:781	column	776:781	Six high-abundance plasma proteins were simultaneously removed using a pre-packed, immobilized antibody column.
16335952	1	66	theme	protein	169:175	arg1	abundances					177:186	relative protein abundances	160:186	relative protein abundances of interest (over 10 orders of magnitude)	160:228	The enormous complexity, wide dynamic range of relative protein abundances of interest (over 10 orders of magnitude), and tremendous heterogeneity (due to post-translational modifications, such as glycosylation) of the human blood plasma proteome severely challenge the capabilities of existing analytical methodologies.
16335952	8	67	theme	high-resolution	1807:1821	arg1	chromatography					1830:1843	high-resolution liquid chromatography	1807:1843	high-resolution liquid chromatography coupled to Fourier transform ion cyclotron resonance mass spectrometry (LC-FTICR)	1807:1925	A total of 639 N-glycosylation sites were identified, and the overall high accuracy of these glycosylation site assignments as assessed by accurate mass measurement using high-resolution liquid chromatography coupled to Fourier transform ion cyclotron resonance mass spectrometry (LC-FTICR) is initially demonstrated.
16335952	4	68	gly	glycopeptides	924:936	arg2	glycopeptides					924:936	the bound N-linked glycopeptides	905:936	the bound N-linked glycopeptides	905:936	N-linked glycoproteins were then captured from the depleted plasma using hydrazide resin and enzymatically digested, and the bound N-linked glycopeptides were released using peptide-N-glycosidase F (PNGase F).
16335952	4	69	link	N-linked	915:922	arg1	glycopeptides					924:936	the bound N-linked glycopeptides	905:936	the bound N-linked glycopeptides	905:936	N-linked glycoproteins were then captured from the depleted plasma using hydrazide resin and enzymatically digested, and the bound N-linked glycopeptides were released using peptide-N-glycosidase F (PNGase F).
16335952	2	70	theme	subtraction	553:563	arg1	combination					523:533	a combination	521:533	a combination of immunoaffinity subtraction and glycoprotein capture to reduce both the protein concentration range and the overall sample complexity	521:669	Here, we describe an approach for broad analysis of human plasma N-glycoproteins using a combination of immunoaffinity subtraction and glycoprotein capture to reduce both the protein concentration range and the overall sample complexity.
16335952	6	71	gly	N-glycopeptides	1240:1254	arg2	N-glycopeptides					1240:1254	2053 different N-glycopeptides	1225:1254	2053 different N-glycopeptides	1225:1254	Using stringent criteria, a total of 2053 different N-glycopeptides were confidently identified, covering 303 nonredundant N-glycoproteins.
16335952	5	72	theme	mass	1158:1161	arg1	LC-MS/MS					1177:1184	LC-MS/MS	1177:1184	LC-MS/MS	1177:1184	Following strong cation exchange (SCX) fractionation, the deglycosylated peptides were analyzed by reversed-phase capillary liquid chromatography coupled to tandem mass spectrometry (LC-MS/MS).
16335952	5	72	theme	mass	1158:1161	arg1	spectrometry					1163:1174	tandem mass spectrometry	1151:1174	tandem mass spectrometry (LC-MS/MS)	1151:1185	Following strong cation exchange (SCX) fractionation, the deglycosylated peptides were analyzed by reversed-phase capillary liquid chromatography coupled to tandem mass spectrometry (LC-MS/MS).
16335952	1	73	theme	enormous	117:124	arg1	complexity					126:135	The enormous complexity	113:135	The enormous complexity	113:135	The enormous complexity, wide dynamic range of relative protein abundances of interest (over 10 orders of magnitude), and tremendous heterogeneity (due to post-translational modifications, such as glycosylation) of the human blood plasma proteome severely challenge the capabilities of existing analytical methodologies.
16335952	1	74	dep	heterogeneity	246:258	arg1	due					261:263	due	261:263	due	261:263	The enormous complexity, wide dynamic range of relative protein abundances of interest (over 10 orders of magnitude), and tremendous heterogeneity (due to post-translational modifications, such as glycosylation) of the human blood plasma proteome severely challenge the capabilities of existing analytical methodologies.
16335952	5	75	theme	capillary	1108:1116	arg1	chromatography					1125:1138	reversed-phase capillary liquid chromatography	1093:1138	reversed-phase capillary liquid chromatography coupled to tandem mass spectrometry (LC-MS/MS)	1093:1185	Following strong cation exchange (SCX) fractionation, the deglycosylated peptides were analyzed by reversed-phase capillary liquid chromatography coupled to tandem mass spectrometry (LC-MS/MS).
16335952	8	76	theme	cyclotron	1878:1886	arg1	spectrometry					1903:1914	Fourier transform ion cyclotron resonance mass spectrometry	1856:1914	Fourier transform ion cyclotron resonance mass spectrometry (LC-FTICR)	1856:1925	A total of 639 N-glycosylation sites were identified, and the overall high accuracy of these glycosylation site assignments as assessed by accurate mass measurement using high-resolution liquid chromatography coupled to Fourier transform ion cyclotron resonance mass spectrometry (LC-FTICR) is initially demonstrated.
16335952	8	76	theme	cyclotron	1878:1886	arg1	LC-FTICR					1917:1924	LC-FTICR	1917:1924	LC-FTICR	1917:1924	A total of 639 N-glycosylation sites were identified, and the overall high accuracy of these glycosylation site assignments as assessed by accurate mass measurement using high-resolution liquid chromatography coupled to Fourier transform ion cyclotron resonance mass spectrometry (LC-FTICR) is initially demonstrated.
16335952	2	77	gly	glycoprotein	569:580	arg1	glycoprotein					569:580	glycoprotein capture	569:588	glycoprotein capture	569:588	Here, we describe an approach for broad analysis of human plasma N-glycoproteins using a combination of immunoaffinity subtraction and glycoprotein capture to reduce both the protein concentration range and the overall sample complexity.
16335952	4	78	theme	peptide-N-glycosidase	958:978	arg1	F					980:980	peptide-N-glycosidase F	958:980	peptide-N-glycosidase F (PNGase F)	958:991	N-linked glycoproteins were then captured from the depleted plasma using hydrazide resin and enzymatically digested, and the bound N-linked glycopeptides were released using peptide-N-glycosidase F (PNGase F).
16335952	4	78	theme	peptide-N-glycosidase	958:978	arg1	F					990:990	PNGase F	983:990	PNGase F	983:990	N-linked glycoproteins were then captured from the depleted plasma using hydrazide resin and enzymatically digested, and the bound N-linked glycopeptides were released using peptide-N-glycosidase F (PNGase F).
16335952	7	79	theme	receptor	1481:1488	arg1	protein					1501:1507	interleukin-1 receptor antagonist protein	1467:1507	interleukin-1 receptor antagonist protein (approximately 200 pg/mL)	1467:1533	This enrichment strategy significantly improved detection and enabled identification of a number of low-abundance proteins, exemplified by interleukin-1 receptor antagonist protein (approximately 200 pg/mL), cathepsin L (approximately 1 ng/mL), and transforming growth factor beta 1 (approximately 2 ng/mL).
16335952	7	79	theme	receptor	1481:1488	arg1	pg/mL					1528:1532	approximately 200 pg/mL	1510:1532	approximately 200 pg/mL	1510:1532	This enrichment strategy significantly improved detection and enabled identification of a number of low-abundance proteins, exemplified by interleukin-1 receptor antagonist protein (approximately 200 pg/mL), cathepsin L (approximately 1 ng/mL), and transforming growth factor beta 1 (approximately 2 ng/mL).
16335952	8	80	theme	mass	1898:1901	arg1	spectrometry					1903:1914	Fourier transform ion cyclotron resonance mass spectrometry	1856:1914	Fourier transform ion cyclotron resonance mass spectrometry (LC-FTICR)	1856:1925	A total of 639 N-glycosylation sites were identified, and the overall high accuracy of these glycosylation site assignments as assessed by accurate mass measurement using high-resolution liquid chromatography coupled to Fourier transform ion cyclotron resonance mass spectrometry (LC-FTICR) is initially demonstrated.
16335952	8	80	theme	mass	1898:1901	arg1	LC-FTICR					1917:1924	LC-FTICR	1917:1924	LC-FTICR	1917:1924	A total of 639 N-glycosylation sites were identified, and the overall high accuracy of these glycosylation site assignments as assessed by accurate mass measurement using high-resolution liquid chromatography coupled to Fourier transform ion cyclotron resonance mass spectrometry (LC-FTICR) is initially demonstrated.
16335952	1	81	theme	dynamic	143:149	arg1	range					151:155	wide dynamic range	138:155	wide dynamic range of relative protein abundances of interest (over 10 orders of magnitude)	138:228	The enormous complexity, wide dynamic range of relative protein abundances of interest (over 10 orders of magnitude), and tremendous heterogeneity (due to post-translational modifications, such as glycosylation) of the human blood plasma proteome severely challenge the capabilities of existing analytical methodologies.
16335952	2	82	theme	human	486:490	arg1	N-glycoproteins					499:513	human plasma N-glycoproteins	486:513	human plasma N-glycoproteins	486:513	Here, we describe an approach for broad analysis of human plasma N-glycoproteins using a combination of immunoaffinity subtraction and glycoprotein capture to reduce both the protein concentration range and the overall sample complexity.
16335952	1	83	dep	due	261:263	arg1	such					302:305	such	302:305	such	302:305	The enormous complexity, wide dynamic range of relative protein abundances of interest (over 10 orders of magnitude), and tremendous heterogeneity (due to post-translational modifications, such as glycosylation) of the human blood plasma proteome severely challenge the capabilities of existing analytical methodologies.
16335952	1	84	theme	human	332:336	arg1	proteome					351:358	the human blood plasma proteome	328:358	the human blood plasma proteome	328:358	The enormous complexity, wide dynamic range of relative protein abundances of interest (over 10 orders of magnitude), and tremendous heterogeneity (due to post-translational modifications, such as glycosylation) of the human blood plasma proteome severely challenge the capabilities of existing analytical methodologies.
16335952	5	85	theme	exchange	1018:1025	arg1	fractionation					1033:1045	strong cation exchange (SCX) fractionation	1004:1045	strong cation exchange (SCX) fractionation	1004:1045	Following strong cation exchange (SCX) fractionation, the deglycosylated peptides were analyzed by reversed-phase capillary liquid chromatography coupled to tandem mass spectrometry (LC-MS/MS).
16335952	1	86	theme	plasma	344:349	arg1	proteome					351:358	the human blood plasma proteome	328:358	the human blood plasma proteome	328:358	The enormous complexity, wide dynamic range of relative protein abundances of interest (over 10 orders of magnitude), and tremendous heterogeneity (due to post-translational modifications, such as glycosylation) of the human blood plasma proteome severely challenge the capabilities of existing analytical methodologies.
16335952	2	87	gly	N-glycoproteins	499:513	arg1	N-glycoproteins					499:513	human plasma N-glycoproteins	486:513	human plasma N-glycoproteins	486:513	Here, we describe an approach for broad analysis of human plasma N-glycoproteins using a combination of immunoaffinity subtraction and glycoprotein capture to reduce both the protein concentration range and the overall sample complexity.
16335952	7	88	theme	proteins	1442:1449	arg1	number					1418:1423	a number	1416:1423	a number	1416:1423	This enrichment strategy significantly improved detection and enabled identification of a number of low-abundance proteins, exemplified by interleukin-1 receptor antagonist protein (approximately 200 pg/mL), cathepsin L (approximately 1 ng/mL), and transforming growth factor beta 1 (approximately 2 ng/mL).
16335952	2	89	theme	N-glycoproteins	499:513	arg1	analysis					474:481	broad analysis	468:481	broad analysis of human plasma N-glycoproteins	468:513	Here, we describe an approach for broad analysis of human plasma N-glycoproteins using a combination of immunoaffinity subtraction and glycoprotein capture to reduce both the protein concentration range and the overall sample complexity.
16335952	0	90	theme	plasma	6:11	arg1	N-glycoproteome					13:27	Human plasma N-glycoproteome	0:27	Human plasma N-glycoproteome	0:27	Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry.
16335952	8	91	gly	N-glycosylation	1651:1665	arg2	sites					1667:1671	639 N-glycosylation sites	1647:1671	639 N-glycosylation sites	1647:1671	A total of 639 N-glycosylation sites were identified, and the overall high accuracy of these glycosylation site assignments as assessed by accurate mass measurement using high-resolution liquid chromatography coupled to Fourier transform ion cyclotron resonance mass spectrometry (LC-FTICR) is initially demonstrated.
16335952	1	92	gly	heterogeneity	246:258	arg1	proteome					351:358	the human blood plasma proteome	328:358	the human blood plasma proteome	328:358	The enormous complexity, wide dynamic range of relative protein abundances of interest (over 10 orders of magnitude), and tremendous heterogeneity (due to post-translational modifications, such as glycosylation) of the human blood plasma proteome severely challenge the capabilities of existing analytical methodologies.
16335952	1	92	gly	heterogeneity	246:258	arg1	abundances					177:186	relative protein abundances	160:186	relative protein abundances of interest (over 10 orders of magnitude)	160:228	The enormous complexity, wide dynamic range of relative protein abundances of interest (over 10 orders of magnitude), and tremendous heterogeneity (due to post-translational modifications, such as glycosylation) of the human blood plasma proteome severely challenge the capabilities of existing analytical methodologies.
16335952	5	93	theme	strong	1004:1009	arg1	fractionation					1033:1045	strong cation exchange (SCX) fractionation	1004:1045	strong cation exchange (SCX) fractionation	1004:1045	Following strong cation exchange (SCX) fractionation, the deglycosylated peptides were analyzed by reversed-phase capillary liquid chromatography coupled to tandem mass spectrometry (LC-MS/MS).
16335952	8	94	theme	639	1647:1649	arg1	sites					1667:1671	639 N-glycosylation sites	1647:1671	639 N-glycosylation sites	1647:1671	A total of 639 N-glycosylation sites were identified, and the overall high accuracy of these glycosylation site assignments as assessed by accurate mass measurement using high-resolution liquid chromatography coupled to Fourier transform ion cyclotron resonance mass spectrometry (LC-FTICR) is initially demonstrated.
16335952	5	95	theme	SCX	1028:1030	arg1	fractionation					1033:1045	strong cation exchange (SCX) fractionation	1004:1045	strong cation exchange (SCX) fractionation	1004:1045	Following strong cation exchange (SCX) fractionation, the deglycosylated peptides were analyzed by reversed-phase capillary liquid chromatography coupled to tandem mass spectrometry (LC-MS/MS).
16335952	4	96	theme	N-linked	784:791	arg1	glycoproteins					793:805	N-linked glycoproteins	784:805	N-linked glycoproteins	784:805	N-linked glycoproteins were then captured from the depleted plasma using hydrazide resin and enzymatically digested, and the bound N-linked glycopeptides were released using peptide-N-glycosidase F (PNGase F).
16335952	0	97	theme	immunoaffinity	41:54	arg1	subtraction					56:66	immunoaffinity subtraction	41:66	immunoaffinity subtraction	41:66	Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry.
16335952	8	98	theme	sites	1667:1671	arg1	total					1638:1642	A total	1636:1642	A total of 639 N-glycosylation sites	1636:1671	A total of 639 N-glycosylation sites were identified, and the overall high accuracy of these glycosylation site assignments as assessed by accurate mass measurement using high-resolution liquid chromatography coupled to Fourier transform ion cyclotron resonance mass spectrometry (LC-FTICR) is initially demonstrated.
16335952	4	99	theme	hydrazide	857:865	arg1	resin					867:871	hydrazide resin	857:871	hydrazide resin	857:871	N-linked glycoproteins were then captured from the depleted plasma using hydrazide resin and enzymatically digested, and the bound N-linked glycopeptides were released using peptide-N-glycosidase F (PNGase F).
16335952	8	100	theme	site	1743:1746	arg1	assignments					1748:1758	these glycosylation site assignments	1723:1758	these glycosylation site assignments	1723:1758	A total of 639 N-glycosylation sites were identified, and the overall high accuracy of these glycosylation site assignments as assessed by accurate mass measurement using high-resolution liquid chromatography coupled to Fourier transform ion cyclotron resonance mass spectrometry (LC-FTICR) is initially demonstrated.
16335952	3	101	theme	high-abundance	676:689	arg1	proteins					698:705	Six high-abundance plasma proteins	672:705	Six high-abundance plasma proteins	672:705	Six high-abundance plasma proteins were simultaneously removed using a pre-packed, immobilized antibody column.
16335952	1	102	theme	magnitude	219:227	arg1	orders					209:214	10 orders	206:214	10 orders of magnitude	206:227	The enormous complexity, wide dynamic range of relative protein abundances of interest (over 10 orders of magnitude), and tremendous heterogeneity (due to post-translational modifications, such as glycosylation) of the human blood plasma proteome severely challenge the capabilities of existing analytical methodologies.
16335952	8	103	theme	overall	1698:1704	arg1	accuracy					1711:1718	the overall high accuracy	1694:1718	the overall high accuracy of these glycosylation site assignments as assessed by accurate mass measurement using high-resolution liquid chromatography coupled to Fourier transform ion cyclotron resonance mass spectrometry (LC-FTICR)	1694:1925	A total of 639 N-glycosylation sites were identified, and the overall high accuracy of these glycosylation site assignments as assessed by accurate mass measurement using high-resolution liquid chromatography coupled to Fourier transform ion cyclotron resonance mass spectrometry (LC-FTICR) is initially demonstrated.
28092368	5	0	theme	second	753:758	arg1	mode					781:784	multi-ion mode	771:784	multi-ion mode	771:784	The more open structure has one cation bound below the selectivity filter (single-ion mode, PC2SI), whereas multiple cations are bound along the translocation pathway in the second structure (multi-ion mode, PC2MI).
28092368	5	0	theme	second	753:758	arg1	structure					760:768	the second structure	749:768	the second structure (multi-ion mode, PC2MI)	749:792	The more open structure has one cation bound below the selectivity filter (single-ion mode, PC2SI), whereas multiple cations are bound along the translocation pathway in the second structure (multi-ion mode, PC2MI).
28092368	4	1	theme	exoplasmic	505:514	arg1	domain					516:521	the large exoplasmic domain	495:521	the large exoplasmic domain (TOP domain)	495:534	The structures reveal conformational differences in the selectivity filter and in the large exoplasmic domain (TOP domain), which displays differing N-glycosylation.
28092368	4	1	theme	exoplasmic	505:514	arg1	domain					528:533	TOP domain	524:533	TOP domain	524:533	The structures reveal conformational differences in the selectivity filter and in the large exoplasmic domain (TOP domain), which displays differing N-glycosylation.
28092368	4	2	from	differences	450:460	arg1	domain					516:521	the large exoplasmic domain	495:521	the large exoplasmic domain (TOP domain)	495:534	The structures reveal conformational differences in the selectivity filter and in the large exoplasmic domain (TOP domain), which displays differing N-glycosylation.
28092368	4	2	from	differences	450:460	arg1	domain					528:533	TOP domain	524:533	TOP domain	524:533	The structures reveal conformational differences in the selectivity filter and in the large exoplasmic domain (TOP domain), which displays differing N-glycosylation.
28092368	4	2	from	differences	450:460	arg1	filter					481:486	the selectivity filter	465:486	the selectivity filter	465:486	The structures reveal conformational differences in the selectivity filter and in the large exoplasmic domain (TOP domain), which displays differing N-glycosylation.
28092368	6	3	theme	PC2SI	964:968	arg1	state					970:974	the unblocked PC2SI state	950:974	the unblocked PC2SI state	950:974	Ca2+ binding at the entrance of the selectivity filter suggests Ca2+ blockage in PC2MI, and we observed density for the Ca2+-sensing C-terminal EF hand in the unblocked PC2SI state.
28092368	0	4	theme	Polycystin-2	74:85	arg1	regulation					44:53	lipid-assisted Ca2+ regulation	24:53	lipid-assisted Ca2+ regulation of the TRP channel Polycystin-2	24:85	Molecular insights into lipid-assisted Ca2+ regulation of the TRP channel Polycystin-2.
28092368	4	5	theme	TOP	524:526	arg1	domain					516:521	the large exoplasmic domain	495:521	the large exoplasmic domain (TOP domain)	495:534	The structures reveal conformational differences in the selectivity filter and in the large exoplasmic domain (TOP domain), which displays differing N-glycosylation.
28092368	4	5	theme	TOP	524:526	arg1	domain					528:533	TOP domain	524:533	TOP domain	524:533	The structures reveal conformational differences in the selectivity filter and in the large exoplasmic domain (TOP domain), which displays differing N-glycosylation.
28092368	5	6	theme	single-ion	654:663	arg1	filter					646:651	the selectivity filter	630:651	the selectivity filter (single-ion mode, PC2SI)	630:676	The more open structure has one cation bound below the selectivity filter (single-ion mode, PC2SI), whereas multiple cations are bound along the translocation pathway in the second structure (multi-ion mode, PC2MI).
28092368	5	6	theme	single-ion	654:663	arg1	mode					665:668	single-ion mode	654:668	single-ion mode	654:668	The more open structure has one cation bound below the selectivity filter (single-ion mode, PC2SI), whereas multiple cations are bound along the translocation pathway in the second structure (multi-ion mode, PC2MI).
28092368	6	7	theme	Ca2+	795:798	arg1	binding					800:806	Ca2+ binding	795:806	Ca2+ binding at the entrance of the selectivity filter	795:848	Ca2+ binding at the entrance of the selectivity filter suggests Ca2+ blockage in PC2MI, and we observed density for the Ca2+-sensing C-terminal EF hand in the unblocked PC2SI state.
28092368	4	8	theme	selectivity	469:479	arg1	filter					481:486	the selectivity filter	465:486	the selectivity filter	465:486	The structures reveal conformational differences in the selectivity filter and in the large exoplasmic domain (TOP domain), which displays differing N-glycosylation.
28092368	6	9	theme	unblocked	954:962	arg1	state					970:974	the unblocked PC2SI state	950:974	the unblocked PC2SI state	950:974	Ca2+ binding at the entrance of the selectivity filter suggests Ca2+ blockage in PC2MI, and we observed density for the Ca2+-sensing C-terminal EF hand in the unblocked PC2SI state.
28092368	3	10	theme	human	367:371	arg1	PC2					373:375	full-length human PC2	355:375	full-length human PC2	355:375	Here we report two cryo-EM structures of distinct channel states of full-length human PC2 in complex with lipids and cations.
28092368	6	11	theme	selectivity	831:841	arg1	filter					843:848	the selectivity filter	827:848	the selectivity filter	827:848	Ca2+ binding at the entrance of the selectivity filter suggests Ca2+ blockage in PC2MI, and we observed density for the Ca2+-sensing C-terminal EF hand in the unblocked PC2SI state.
28092368	3	12	theme	PC2	373:375	arg1	states					345:350	distinct channel states	328:350	distinct channel states of full-length human PC2	328:375	Here we report two cryo-EM structures of distinct channel states of full-length human PC2 in complex with lipids and cations.
28092368	7	13	theme	membrane	1150:1157	arg1	compositions					1159:1170	different membrane compositions	1140:1170	different membrane compositions	1140:1170	The states show altered interactions of lipids with the pore loop and TOP domain, thus reflecting the functional diversity of PC2 at different locations, owing to different membrane compositions.
28092368	2	14	from	regulation	216:225	arg1	PC2					230:232	PC2	230:232	PC2	230:232	Malfunctioning Ca2+ regulation in PC2 causes autosomal-dominant polycystic kidney disease.
28092368	5	15	theme	translocation	724:736	arg1	pathway					738:744	the translocation pathway	720:744	the translocation pathway in the second structure (multi-ion mode, PC2MI)	720:792	The more open structure has one cation bound below the selectivity filter (single-ion mode, PC2SI), whereas multiple cations are bound along the translocation pathway in the second structure (multi-ion mode, PC2MI).
28092368	5	16	dep	mode	781:784	arg1	PC2MI					787:791	PC2MI	787:791	PC2MI	787:791	The more open structure has one cation bound below the selectivity filter (single-ion mode, PC2SI), whereas multiple cations are bound along the translocation pathway in the second structure (multi-ion mode, PC2MI).
28092368	7	17	with	interactions	1001:1012	arg1	loop					1038:1041	the pore loop	1029:1041	the pore loop	1029:1041	The states show altered interactions of lipids with the pore loop and TOP domain, thus reflecting the functional diversity of PC2 at different locations, owing to different membrane compositions.
28092368	7	17	with	interactions	1001:1012	arg1	domain					1051:1056	TOP domain	1047:1056	TOP domain	1047:1056	The states show altered interactions of lipids with the pore loop and TOP domain, thus reflecting the functional diversity of PC2 at different locations, owing to different membrane compositions.
28092368	7	18	theme	TOP	1047:1049	arg1	domain					1051:1056	TOP domain	1047:1056	TOP domain	1047:1056	The states show altered interactions of lipids with the pore loop and TOP domain, thus reflecting the functional diversity of PC2 at different locations, owing to different membrane compositions.
28092368	3	19	theme	full-length	355:365	arg1	PC2					373:375	full-length human PC2	355:375	full-length human PC2	355:375	Here we report two cryo-EM structures of distinct channel states of full-length human PC2 in complex with lipids and cations.
28092368	4	20	theme	large	499:503	arg1	domain					516:521	the large exoplasmic domain	495:521	the large exoplasmic domain (TOP domain)	495:534	The structures reveal conformational differences in the selectivity filter and in the large exoplasmic domain (TOP domain), which displays differing N-glycosylation.
28092368	4	20	theme	large	499:503	arg1	domain					528:533	TOP domain	524:533	TOP domain	524:533	The structures reveal conformational differences in the selectivity filter and in the large exoplasmic domain (TOP domain), which displays differing N-glycosylation.
28092368	5	21	dep	mode	665:668	arg1	PC2SI					671:675	PC2SI	671:675	PC2SI	671:675	The more open structure has one cation bound below the selectivity filter (single-ion mode, PC2SI), whereas multiple cations are bound along the translocation pathway in the second structure (multi-ion mode, PC2MI).
28092368	3	22	theme	distinct	328:335	arg1	states					345:350	distinct channel states	328:350	distinct channel states of full-length human PC2	328:375	Here we report two cryo-EM structures of distinct channel states of full-length human PC2 in complex with lipids and cations.
28092368	5	23	theme	selectivity	634:644	arg1	filter					646:651	the selectivity filter	630:651	the selectivity filter (single-ion mode, PC2SI)	630:676	The more open structure has one cation bound below the selectivity filter (single-ion mode, PC2SI), whereas multiple cations are bound along the translocation pathway in the second structure (multi-ion mode, PC2MI).
28092368	5	23	theme	selectivity	634:644	arg1	mode					665:668	single-ion mode	654:668	single-ion mode	654:668	The more open structure has one cation bound below the selectivity filter (single-ion mode, PC2SI), whereas multiple cations are bound along the translocation pathway in the second structure (multi-ion mode, PC2MI).
28092368	0	24	theme	channel	66:72	arg1	Polycystin-2					74:85	the TRP channel Polycystin-2	58:85	the TRP channel Polycystin-2	58:85	Molecular insights into lipid-assisted Ca2+ regulation of the TRP channel Polycystin-2.
28092368	1	25	theme	diverse	163:169	arg1	pathways					186:193	diverse Ca2+ signaling pathways	163:193	diverse Ca2+ signaling pathways	163:193	Polycystin-2 (PC2), a calcium-activated cation TRP channel, is involved in diverse Ca2+ signaling pathways.
28092368	0	26	theme	Molecular	0:8	arg1	insights					10:17	Molecular insights	0:17	Molecular insights into lipid-assisted Ca2+ regulation of the TRP channel Polycystin-2	0:85	Molecular insights into lipid-assisted Ca2+ regulation of the TRP channel Polycystin-2.
28092368	7	27	theme	PC2	1103:1105	arg1	diversity					1090:1098	the functional diversity	1075:1098	the functional diversity of PC2	1075:1105	The states show altered interactions of lipids with the pore loop and TOP domain, thus reflecting the functional diversity of PC2 at different locations, owing to different membrane compositions.
28092368	5	28	theme	open	588:591	arg1	structure					593:601	The more open structure	579:601	The more open structure	579:601	The more open structure has one cation bound below the selectivity filter (single-ion mode, PC2SI), whereas multiple cations are bound along the translocation pathway in the second structure (multi-ion mode, PC2MI).
28092368	3	29	with	complex	380:386	arg1	cations					404:410	cations	404:410	cations	404:410	Here we report two cryo-EM structures of distinct channel states of full-length human PC2 in complex with lipids and cations.
28092368	3	29	with	complex	380:386	arg1	lipids					393:398	lipids	393:398	lipids	393:398	Here we report two cryo-EM structures of distinct channel states of full-length human PC2 in complex with lipids and cations.
28092368	1	30	theme	Ca2+	171:174	arg1	pathways					186:193	diverse Ca2+ signaling pathways	163:193	diverse Ca2+ signaling pathways	163:193	Polycystin-2 (PC2), a calcium-activated cation TRP channel, is involved in diverse Ca2+ signaling pathways.
28092368	0	31	theme	lipid-assisted	24:37	arg1	regulation					44:53	lipid-assisted Ca2+ regulation	24:53	lipid-assisted Ca2+ regulation of the TRP channel Polycystin-2	24:85	Molecular insights into lipid-assisted Ca2+ regulation of the TRP channel Polycystin-2.
28092368	6	32	theme	EF	939:940	arg1	hand					942:945	the Ca2+-sensing C-terminal EF hand	911:945	the Ca2+-sensing C-terminal EF hand	911:945	Ca2+ binding at the entrance of the selectivity filter suggests Ca2+ blockage in PC2MI, and we observed density for the Ca2+-sensing C-terminal EF hand in the unblocked PC2SI state.
28092368	5	33	theme	multiple	687:694	arg1	cations					696:702	multiple cations	687:702	multiple cations	687:702	The more open structure has one cation bound below the selectivity filter (single-ion mode, PC2SI), whereas multiple cations are bound along the translocation pathway in the second structure (multi-ion mode, PC2MI).
28092368	1	34	theme	signaling	176:184	arg1	pathways					186:193	diverse Ca2+ signaling pathways	163:193	diverse Ca2+ signaling pathways	163:193	Polycystin-2 (PC2), a calcium-activated cation TRP channel, is involved in diverse Ca2+ signaling pathways.
28092368	7	35	theme	different	1110:1118	arg1	locations					1120:1128	different locations	1110:1128	different locations	1110:1128	The states show altered interactions of lipids with the pore loop and TOP domain, thus reflecting the functional diversity of PC2 at different locations, owing to different membrane compositions.
28092368	6	36	theme	C-terminal	928:937	arg1	hand					942:945	the Ca2+-sensing C-terminal EF hand	911:945	the Ca2+-sensing C-terminal EF hand	911:945	Ca2+ binding at the entrance of the selectivity filter suggests Ca2+ blockage in PC2MI, and we observed density for the Ca2+-sensing C-terminal EF hand in the unblocked PC2SI state.
28092368	7	37	theme	pore	1033:1036	arg1	loop					1038:1041	the pore loop	1029:1041	the pore loop	1029:1041	The states show altered interactions of lipids with the pore loop and TOP domain, thus reflecting the functional diversity of PC2 at different locations, owing to different membrane compositions.
28092368	6	38	theme	filter	843:848	arg1	entrance					815:822	the entrance	811:822	the entrance of the selectivity filter	811:848	Ca2+ binding at the entrance of the selectivity filter suggests Ca2+ blockage in PC2MI, and we observed density for the Ca2+-sensing C-terminal EF hand in the unblocked PC2SI state.
28092368	6	39	theme	Ca2+-sensing	915:926	arg1	hand					942:945	the Ca2+-sensing C-terminal EF hand	911:945	the Ca2+-sensing C-terminal EF hand	911:945	Ca2+ binding at the entrance of the selectivity filter suggests Ca2+ blockage in PC2MI, and we observed density for the Ca2+-sensing C-terminal EF hand in the unblocked PC2SI state.
28092368	7	40	theme	lipids	1017:1022	arg1	interactions					1001:1012	altered interactions	993:1012	altered interactions of lipids with the pore loop and TOP domain	993:1056	The states show altered interactions of lipids with the pore loop and TOP domain, thus reflecting the functional diversity of PC2 at different locations, owing to different membrane compositions.
28092368	5	41	from	pathway	738:744	arg1	mode					781:784	multi-ion mode	771:784	multi-ion mode	771:784	The more open structure has one cation bound below the selectivity filter (single-ion mode, PC2SI), whereas multiple cations are bound along the translocation pathway in the second structure (multi-ion mode, PC2MI).
28092368	5	41	from	pathway	738:744	arg1	structure					760:768	the second structure	749:768	the second structure (multi-ion mode, PC2MI)	749:792	The more open structure has one cation bound below the selectivity filter (single-ion mode, PC2SI), whereas multiple cations are bound along the translocation pathway in the second structure (multi-ion mode, PC2MI).
28092368	5	42	contain	has	603:605	arg1	structure					593:601	The more open structure	579:601	The more open structure	579:601	The more open structure has one cation bound below the selectivity filter (single-ion mode, PC2SI), whereas multiple cations are bound along the translocation pathway in the second structure (multi-ion mode, PC2MI).
28092368	5	42	contain	has	603:605	arg2	cation					611:616	one cation	607:616	one cation bound below the selectivity filter (single-ion mode, PC2SI)	607:676	The more open structure has one cation bound below the selectivity filter (single-ion mode, PC2SI), whereas multiple cations are bound along the translocation pathway in the second structure (multi-ion mode, PC2MI).
28092368	7	43	theme	functional	1079:1088	arg1	diversity					1090:1098	the functional diversity	1075:1098	the functional diversity of PC2	1075:1105	The states show altered interactions of lipids with the pore loop and TOP domain, thus reflecting the functional diversity of PC2 at different locations, owing to different membrane compositions.
28092368	0	44	theme	Ca2+	39:42	arg1	regulation					44:53	lipid-assisted Ca2+ regulation	24:53	lipid-assisted Ca2+ regulation of the TRP channel Polycystin-2	24:85	Molecular insights into lipid-assisted Ca2+ regulation of the TRP channel Polycystin-2.
28092368	5	45	theme	multi-ion	771:779	arg1	mode					781:784	multi-ion mode	771:784	multi-ion mode	771:784	The more open structure has one cation bound below the selectivity filter (single-ion mode, PC2SI), whereas multiple cations are bound along the translocation pathway in the second structure (multi-ion mode, PC2MI).
28092368	5	45	theme	multi-ion	771:779	arg1	structure					760:768	the second structure	749:768	the second structure (multi-ion mode, PC2MI)	749:792	The more open structure has one cation bound below the selectivity filter (single-ion mode, PC2SI), whereas multiple cations are bound along the translocation pathway in the second structure (multi-ion mode, PC2MI).
28092368	6	46	from	blockage	864:871	arg1	PC2MI					876:880	PC2MI	876:880	PC2MI	876:880	Ca2+ binding at the entrance of the selectivity filter suggests Ca2+ blockage in PC2MI, and we observed density for the Ca2+-sensing C-terminal EF hand in the unblocked PC2SI state.
28092368	6	47	from	entrance	815:822	arg1	binding					800:806	Ca2+ binding	795:806	Ca2+ binding at the entrance of the selectivity filter	795:848	Ca2+ binding at the entrance of the selectivity filter suggests Ca2+ blockage in PC2MI, and we observed density for the Ca2+-sensing C-terminal EF hand in the unblocked PC2SI state.
28092368	7	48	theme	different	1140:1148	arg1	compositions					1159:1170	different membrane compositions	1140:1170	different membrane compositions	1140:1170	The states show altered interactions of lipids with the pore loop and TOP domain, thus reflecting the functional diversity of PC2 at different locations, owing to different membrane compositions.
28092368	3	49	theme	cryo-EM	306:312	arg1	structures					314:323	two cryo-EM structures	302:323	two cryo-EM structures of distinct channel states of full-length human PC2 in complex with lipids and cations	302:410	Here we report two cryo-EM structures of distinct channel states of full-length human PC2 in complex with lipids and cations.
28092368	0	50	theme	TRP	62:64	arg1	Polycystin-2					74:85	the TRP channel Polycystin-2	58:85	the TRP channel Polycystin-2	58:85	Molecular insights into lipid-assisted Ca2+ regulation of the TRP channel Polycystin-2.
28092368	6	51	theme	Ca2+	859:862	arg1	blockage					864:871	Ca2+ blockage	859:871	Ca2+ blockage in PC2MI	859:880	Ca2+ binding at the entrance of the selectivity filter suggests Ca2+ blockage in PC2MI, and we observed density for the Ca2+-sensing C-terminal EF hand in the unblocked PC2SI state.
28092368	2	52	theme	Malfunctioning	196:209	arg1	regulation					216:225	Malfunctioning Ca2+ regulation	196:225	Malfunctioning Ca2+ regulation in PC2	196:232	Malfunctioning Ca2+ regulation in PC2 causes autosomal-dominant polycystic kidney disease.
28092368	2	53	theme	Ca2+	211:214	arg1	regulation					216:225	Malfunctioning Ca2+ regulation	196:225	Malfunctioning Ca2+ regulation in PC2	196:232	Malfunctioning Ca2+ regulation in PC2 causes autosomal-dominant polycystic kidney disease.
28092368	6	54	from	density	899:905	arg1	state					970:974	the unblocked PC2SI state	950:974	the unblocked PC2SI state	950:974	Ca2+ binding at the entrance of the selectivity filter suggests Ca2+ blockage in PC2MI, and we observed density for the Ca2+-sensing C-terminal EF hand in the unblocked PC2SI state.
28092368	2	55	theme	kidney	271:276	arg1	disease					278:284	autosomal-dominant polycystic kidney disease	241:284	autosomal-dominant polycystic kidney disease	241:284	Malfunctioning Ca2+ regulation in PC2 causes autosomal-dominant polycystic kidney disease.
28092368	1	56	theme	calcium-activated	110:126	arg1	channel					139:145	a calcium-activated cation TRP channel	108:145	a calcium-activated cation TRP channel	108:145	Polycystin-2 (PC2), a calcium-activated cation TRP channel, is involved in diverse Ca2+ signaling pathways.
28092368	1	56	theme	calcium-activated	110:126	arg1	Polycystin-2					88:99	Polycystin-2	88:99	Polycystin-2 (PC2)	88:105	Polycystin-2 (PC2), a calcium-activated cation TRP channel, is involved in diverse Ca2+ signaling pathways.
28092368	7	57	theme	altered	993:999	arg1	interactions					1001:1012	altered interactions	993:1012	altered interactions of lipids with the pore loop and TOP domain	993:1056	The states show altered interactions of lipids with the pore loop and TOP domain, thus reflecting the functional diversity of PC2 at different locations, owing to different membrane compositions.
28092368	2	58	theme	polycystic	260:269	arg1	disease					278:284	autosomal-dominant polycystic kidney disease	241:284	autosomal-dominant polycystic kidney disease	241:284	Malfunctioning Ca2+ regulation in PC2 causes autosomal-dominant polycystic kidney disease.
28092368	1	59	theme	cation	128:133	arg1	channel					139:145	a calcium-activated cation TRP channel	108:145	a calcium-activated cation TRP channel	108:145	Polycystin-2 (PC2), a calcium-activated cation TRP channel, is involved in diverse Ca2+ signaling pathways.
28092368	1	59	theme	cation	128:133	arg1	Polycystin-2					88:99	Polycystin-2	88:99	Polycystin-2 (PC2)	88:105	Polycystin-2 (PC2), a calcium-activated cation TRP channel, is involved in diverse Ca2+ signaling pathways.
28092368	3	60	theme	channel	337:343	arg1	states					345:350	distinct channel states	328:350	distinct channel states of full-length human PC2	328:375	Here we report two cryo-EM structures of distinct channel states of full-length human PC2 in complex with lipids and cations.
28092368	4	61	theme	conformational	435:448	arg1	differences					450:460	conformational differences	435:460	conformational differences in the selectivity filter and in the large exoplasmic domain (TOP domain), which displays differing N-glycosylation	435:576	The structures reveal conformational differences in the selectivity filter and in the large exoplasmic domain (TOP domain), which displays differing N-glycosylation.
28092368	2	62	theme	autosomal-dominant	241:258	arg1	disease					278:284	autosomal-dominant polycystic kidney disease	241:284	autosomal-dominant polycystic kidney disease	241:284	Malfunctioning Ca2+ regulation in PC2 causes autosomal-dominant polycystic kidney disease.
28092368	1	63	theme	TRP	135:137	arg1	channel					139:145	a calcium-activated cation TRP channel	108:145	a calcium-activated cation TRP channel	108:145	Polycystin-2 (PC2), a calcium-activated cation TRP channel, is involved in diverse Ca2+ signaling pathways.
28092368	1	63	theme	TRP	135:137	arg1	Polycystin-2					88:99	Polycystin-2	88:99	Polycystin-2 (PC2)	88:105	Polycystin-2 (PC2), a calcium-activated cation TRP channel, is involved in diverse Ca2+ signaling pathways.
28092368	3	64	theme	states	345:350	arg1	structures					314:323	two cryo-EM structures	302:323	two cryo-EM structures of distinct channel states of full-length human PC2 in complex with lipids and cations	302:410	Here we report two cryo-EM structures of distinct channel states of full-length human PC2 in complex with lipids and cations.
28092368	3	65	from	structures	314:323	arg1	complex					380:386	complex	380:386	complex with lipids and cations	380:410	Here we report two cryo-EM structures of distinct channel states of full-length human PC2 in complex with lipids and cations.
18642129	7	0	theme	sialylated	1136:1145	arg1	glycans					1147:1153	triantennary sialylated glycans	1123:1153	triantennary sialylated glycans	1123:1153	LC-ESIMS/MS analysis revealed that both light chain and heavy chain were N-glycosylated mainly by A2S2 but also by triantennary sialylated glycans.
18642129	12	1	dep	position	1702:1709	arg1	Ser					1723:1725	Ser(52)	1723:1729	Ser(52)	1723:1729	Last, MS and MS/MS analysis revealed that FVII is O-glycosylated on the light chain at position Ser(60) and Ser(52) which are modified by oligosaccharide structures such as fucose and Glc(Xyl)(0-1-2), respectively.
18642129	12	1	dep	position	1702:1709	arg1	Ser					1711:1713	Ser(60)	1711:1717	Ser(60)	1711:1717	Last, MS and MS/MS analysis revealed that FVII is O-glycosylated on the light chain at position Ser(60) and Ser(52) which are modified by oligosaccharide structures such as fucose and Glc(Xyl)(0-1-2), respectively.
18642129	4	2	from	site	679:682	arg1	heterogeneity					643:655	their structural heterogeneity	626:655	their structural heterogeneity at each glycosylation site	626:682	Despite glycosylation of recombinant FVIIa has been fully characterized, nothing is reported on the N- and O-glycans of plasma-derived FVII (pd-FVII) and on their structural heterogeneity at each glycosylation site.
18642129	6	3	theme	kDa	908:910	arg1	glycoprotein					912:923	a 50.1 kDa glycoprotein	901:923	a 50.1 kDa glycoprotein modified on two sites by diantennary, disialylated non-fucosylated (A2S2) glycans	901:1005	A MALDI-MS analysis of the native protein indicated that FVII is a 50.1 kDa glycoprotein modified on two sites by diantennary, disialylated non-fucosylated (A2S2) glycans.
18642129	6	3	theme	kDa	908:910	arg1	FVII					893:896	FVII	893:896	FVII	893:896	A MALDI-MS analysis of the native protein indicated that FVII is a 50.1 kDa glycoprotein modified on two sites by diantennary, disialylated non-fucosylated (A2S2) glycans.
18642129	10	4	theme	isolated	1363:1370	arg1	glycans					1372:1378	the isolated glycans	1359:1378	the isolated glycans	1359:1378	In parallel, quantitative analysis of the isolated glycans by capillary electrophoresis indicated that the diantennary structures represented about 50% of the total glycan content.
18642129	8	5	theme	triantennary	1187:1198	arg1	structures					1200:1209	triantennary structures	1187:1209	triantennary structures	1187:1209	Nevertheless, lower amounts of triantennary structures were found on Asn(322) compared to Asn(145).
18642129	1	6	gly	glycoprotein	141:152	arg1	VII					105:107	Factor VII	98:107	Factor VII (FVII)	98:114	Factor VII (FVII) is a vitamin K-dependent glycoprotein which, in its activated form (FVIIa), participates in the coagulation process by activating factor X and factor IX.
18642129	1	6	gly	glycoprotein	141:152	arg1	glycoprotein					141:152	a vitamin K-dependent glycoprotein	119:152	a vitamin K-dependent glycoprotein which, in its activated form (FVIIa), participates in the coagulation process by activating factor X and factor IX	119:267	Factor VII (FVII) is a vitamin K-dependent glycoprotein which, in its activated form (FVIIa), participates in the coagulation process by activating factor X and factor IX.
18642129	6	7	gly	non-fucosylated	976:990	arg1	glycans					999:1005	diantennary, disialylated non-fucosylated (A2S2) glycans	950:1005	glycans	999:1005	A MALDI-MS analysis of the native protein indicated that FVII is a 50.1 kDa glycoprotein modified on two sites by diantennary, disialylated non-fucosylated (A2S2) glycans.
18642129	13	8	theme	plasma-derived	1887:1900	arg1	FVII					1902:1905	plasma-derived FVII	1887:1905	plasma-derived FVII	1887:1905	These latter three O-glycans coexist in equal amounts in plasma-derived FVII.
18642129	1	9	theme	activated	168:176	arg1	FVIIa					184:188	FVIIa	184:188	FVIIa	184:188	Factor VII (FVII) is a vitamin K-dependent glycoprotein which, in its activated form (FVIIa), participates in the coagulation process by activating factor X and factor IX.
18642129	1	9	theme	activated	168:176	arg1	form					178:181	its activated form	164:181	its activated form (FVIIa)	164:189	Factor VII (FVII) is a vitamin K-dependent glycoprotein which, in its activated form (FVIIa), participates in the coagulation process by activating factor X and factor IX.
18642129	6	10	theme	non-fucosylated	976:990	arg1	glycans					999:1005	diantennary, disialylated non-fucosylated (A2S2) glycans	950:1005	glycans	999:1005	A MALDI-MS analysis of the native protein indicated that FVII is a 50.1 kDa glycoprotein modified on two sites by diantennary, disialylated non-fucosylated (A2S2) glycans.
18642129	7	11	gly	sialylated	1136:1145	arg1	glycans					1147:1153	triantennary sialylated glycans	1123:1153	triantennary sialylated glycans	1123:1153	LC-ESIMS/MS analysis revealed that both light chain and heavy chain were N-glycosylated mainly by A2S2 but also by triantennary sialylated glycans.
18642129	5	12	theme	O-glycosylation	692:706	arg1	sites					708:712	N- and O-glycosylation sites	685:712	N- and O-glycosylation sites	685:712	N- and O-glycosylation sites and site specific heterogeneity of pd-FVII were studied by various complementary qualitative and quantitative techniques.
18642129	5	12	theme	O-glycosylation	692:706	arg1	pd-FVII					749:755	pd-FVII	749:755	pd-FVII	749:755	N- and O-glycosylation sites and site specific heterogeneity of pd-FVII were studied by various complementary qualitative and quantitative techniques.
18642129	4	13	gly	glycosylation	477:489	arg1	FVIIa					506:510	recombinant FVIIa	494:510	recombinant FVIIa	494:510	Despite glycosylation of recombinant FVIIa has been fully characterized, nothing is reported on the N- and O-glycans of plasma-derived FVII (pd-FVII) and on their structural heterogeneity at each glycosylation site.
18642129	5	14	gly	O-glycosylation	692:706	arg2	sites					708:712	N- and O-glycosylation sites	685:712	N- and O-glycosylation sites	685:712	N- and O-glycosylation sites and site specific heterogeneity of pd-FVII were studied by various complementary qualitative and quantitative techniques.
18642129	5	14	gly	O-glycosylation	692:706	arg2	pd-FVII					749:755	pd-FVII	749:755	pd-FVII	749:755	N- and O-glycosylation sites and site specific heterogeneity of pd-FVII were studied by various complementary qualitative and quantitative techniques.
18642129	5	14	gly	O-glycosylation	692:706	arg1	pd-FVII					749:755	pd-FVII	749:755	pd-FVII	749:755	N- and O-glycosylation sites and site specific heterogeneity of pd-FVII were studied by various complementary qualitative and quantitative techniques.
18642129	7	15	theme	LC-ESIMS/MS	1008:1018	arg1	analysis					1020:1027	LC-ESIMS/MS analysis	1008:1027	LC-ESIMS/MS analysis	1008:1027	LC-ESIMS/MS analysis revealed that both light chain and heavy chain were N-glycosylated mainly by A2S2 but also by triantennary sialylated glycans.
18642129	12	16	from	position	1702:1709	arg1	chain					1693:1697	the light chain	1683:1697	the light chain at position Ser(60) and Ser(52) which are modified by oligosaccharide structures such as fucose and Glc(Xyl)(0-1-2), respectively	1683:1827	Last, MS and MS/MS analysis revealed that FVII is O-glycosylated on the light chain at position Ser(60) and Ser(52) which are modified by oligosaccharide structures such as fucose and Glc(Xyl)(0-1-2), respectively.
18642129	5	17	theme	N-	685:686	arg1	sites					708:712	N- and O-glycosylation sites	685:712	N- and O-glycosylation sites	685:712	N- and O-glycosylation sites and site specific heterogeneity of pd-FVII were studied by various complementary qualitative and quantitative techniques.
18642129	5	17	theme	N-	685:686	arg1	pd-FVII					749:755	pd-FVII	749:755	pd-FVII	749:755	N- and O-glycosylation sites and site specific heterogeneity of pd-FVII were studied by various complementary qualitative and quantitative techniques.
18642129	3	18	link	Plasma-derived	328:341	arg1	FVII					343:346	Plasma-derived FVII	328:346	Plasma-derived FVII	328:346	Plasma-derived FVII undergoes many post-translational modifications such as gamma-carboxylation, N- and O-glycosylation, beta-hydroxylation.
18642129	10	19	theme	glycan	1486:1491	arg1	content					1493:1499	the total glycan content	1476:1499	the total glycan content	1476:1499	In parallel, quantitative analysis of the isolated glycans by capillary electrophoresis indicated that the diantennary structures represented about 50% of the total glycan content.
18642129	7	20	gly	N-glycosylated	1081:1094	arg1	chain					1054:1058	light chain	1048:1058	light chain	1048:1058	LC-ESIMS/MS analysis revealed that both light chain and heavy chain were N-glycosylated mainly by A2S2 but also by triantennary sialylated glycans.
18642129	7	20	gly	N-glycosylated	1081:1094	arg1	chain					1070:1074	heavy chain	1064:1074	heavy chain	1064:1074	LC-ESIMS/MS analysis revealed that both light chain and heavy chain were N-glycosylated mainly by A2S2 but also by triantennary sialylated glycans.
18642129	13	21	theme	equal	1870:1874	arg1	amounts					1876:1882	equal amounts	1870:1882	equal amounts in plasma-derived FVII	1870:1905	These latter three O-glycans coexist in equal amounts in plasma-derived FVII.
18642129	0	22	theme	plasma-derived	59:72	arg1	VII					93:95	plasma-derived coagulation factor VII	59:95	plasma-derived coagulation factor VII	59:95	Mass spectrometric characterization of N- and O-glycans of plasma-derived coagulation factor VII.
18642129	1	23	theme	K-dependent	129:139	arg1	VII					105:107	Factor VII	98:107	Factor VII (FVII)	98:114	Factor VII (FVII) is a vitamin K-dependent glycoprotein which, in its activated form (FVIIa), participates in the coagulation process by activating factor X and factor IX.
18642129	1	23	theme	K-dependent	129:139	arg1	glycoprotein					141:152	a vitamin K-dependent glycoprotein	119:152	a vitamin K-dependent glycoprotein which, in its activated form (FVIIa), participates in the coagulation process by activating factor X and factor IX	119:267	Factor VII (FVII) is a vitamin K-dependent glycoprotein which, in its activated form (FVIIa), participates in the coagulation process by activating factor X and factor IX.
18642129	4	24	theme	recombinant	494:504	arg1	FVIIa					506:510	recombinant FVIIa	494:510	recombinant FVIIa	494:510	Despite glycosylation of recombinant FVIIa has been fully characterized, nothing is reported on the N- and O-glycans of plasma-derived FVII (pd-FVII) and on their structural heterogeneity at each glycosylation site.
18642129	7	25	theme	light	1048:1052	arg1	chain					1054:1058	light chain	1048:1058	light chain	1048:1058	LC-ESIMS/MS analysis revealed that both light chain and heavy chain were N-glycosylated mainly by A2S2 but also by triantennary sialylated glycans.
18642129	0	26	theme	factor	86:91	arg1	VII					93:95	plasma-derived coagulation factor VII	59:95	plasma-derived coagulation factor VII	59:95	Mass spectrometric characterization of N- and O-glycans of plasma-derived coagulation factor VII.
18642129	9	27	theme	triantennary	1270:1281	arg1	glycans					1283:1289	the triantennary glycans	1266:1289	the triantennary glycans	1266:1289	Moreover, the triantennary glycans were shown to be fucosylated.
18642129	10	28	theme	diantennary	1428:1438	arg1	structures					1440:1449	the diantennary structures	1424:1449	the diantennary structures	1424:1449	In parallel, quantitative analysis of the isolated glycans by capillary electrophoresis indicated that the diantennary structures represented about 50% of the total glycan content.
18642129	11	29	theme	different	1526:1534	arg1	glycanases					1536:1545	different glycanases	1526:1545	different glycanases	1526:1545	Glycan sequencing using different glycanases led to the identification of triantennary difucosylated structures.
18642129	6	30	gly	glycoprotein	912:923	arg1	glycoprotein					912:923	a 50.1 kDa glycoprotein	901:923	a 50.1 kDa glycoprotein modified on two sites by diantennary, disialylated non-fucosylated (A2S2) glycans	901:1005	A MALDI-MS analysis of the native protein indicated that FVII is a 50.1 kDa glycoprotein modified on two sites by diantennary, disialylated non-fucosylated (A2S2) glycans.
18642129	6	30	gly	glycoprotein	912:923	arg1	FVII					893:896	FVII	893:896	FVII	893:896	A MALDI-MS analysis of the native protein indicated that FVII is a 50.1 kDa glycoprotein modified on two sites by diantennary, disialylated non-fucosylated (A2S2) glycans.
18642129	5	31	theme	specific	723:730	arg1	heterogeneity					732:744	site specific heterogeneity	718:744	site specific heterogeneity of pd-FVII	718:755	N- and O-glycosylation sites and site specific heterogeneity of pd-FVII were studied by various complementary qualitative and quantitative techniques.
18642129	6	32	theme	A2S2	993:996	arg1	glycans					999:1005	diantennary, disialylated non-fucosylated (A2S2) glycans	950:1005	glycans	999:1005	A MALDI-MS analysis of the native protein indicated that FVII is a 50.1 kDa glycoprotein modified on two sites by diantennary, disialylated non-fucosylated (A2S2) glycans.
18642129	0	33	theme	coagulation	74:84	arg1	VII					93:95	plasma-derived coagulation factor VII	59:95	plasma-derived coagulation factor VII	59:95	Mass spectrometric characterization of N- and O-glycans of plasma-derived coagulation factor VII.
18642129	0	34	theme	Mass	0:3	arg1	characterization					19:34	Mass spectrometric characterization	0:34	Mass spectrometric characterization of N- and O-glycans of plasma-derived coagulation factor VII.	0:96	Mass spectrometric characterization of N- and O-glycans of plasma-derived coagulation factor VII.
18642129	1	35	theme	factor	246:251	arg1	X					253:253	factor X	246:253	factor X	246:253	Factor VII (FVII) is a vitamin K-dependent glycoprotein which, in its activated form (FVIIa), participates in the coagulation process by activating factor X and factor IX.
18642129	1	36	theme	Factor	98:103	arg1	glycoprotein					141:152	a vitamin K-dependent glycoprotein	119:152	a vitamin K-dependent glycoprotein which, in its activated form (FVIIa), participates in the coagulation process by activating factor X and factor IX	119:267	Factor VII (FVII) is a vitamin K-dependent glycoprotein which, in its activated form (FVIIa), participates in the coagulation process by activating factor X and factor IX.
18642129	1	36	theme	Factor	98:103	arg1	FVII					110:113	FVII	110:113	FVII	110:113	Factor VII (FVII) is a vitamin K-dependent glycoprotein which, in its activated form (FVIIa), participates in the coagulation process by activating factor X and factor IX.
18642129	1	36	theme	Factor	98:103	arg1	VII					105:107	Factor VII	98:107	Factor VII (FVII)	98:114	Factor VII (FVII) is a vitamin K-dependent glycoprotein which, in its activated form (FVIIa), participates in the coagulation process by activating factor X and factor IX.
18642129	10	37	theme	content	1493:1499	arg1	content					1493:1499	the total glycan content	1476:1499	the total glycan content	1476:1499	In parallel, quantitative analysis of the isolated glycans by capillary electrophoresis indicated that the diantennary structures represented about 50% of the total glycan content.
18642129	10	37	theme	content	1493:1499	arg1	%					1471:1471	about 50%	1463:1471	about 50% of the total glycan content	1463:1499	In parallel, quantitative analysis of the isolated glycans by capillary electrophoresis indicated that the diantennary structures represented about 50% of the total glycan content.
18642129	10	38	theme	total	1480:1484	arg1	content					1493:1499	the total glycan content	1476:1499	the total glycan content	1476:1499	In parallel, quantitative analysis of the isolated glycans by capillary electrophoresis indicated that the diantennary structures represented about 50% of the total glycan content.
18642129	0	39	theme	N-	39:40	arg1	characterization					19:34	Mass spectrometric characterization	0:34	Mass spectrometric characterization of N- and O-glycans of plasma-derived coagulation factor VII.	0:96	Mass spectrometric characterization of N- and O-glycans of plasma-derived coagulation factor VII.
18642129	5	40	theme	complementary	781:793	arg1	techniques					824:833	various complementary qualitative and quantitative techniques	773:833	various complementary qualitative and quantitative techniques	773:833	N- and O-glycosylation sites and site specific heterogeneity of pd-FVII were studied by various complementary qualitative and quantitative techniques.
18642129	6	41	theme	protein	870:876	arg1	analysis					847:854	A MALDI-MS analysis	836:854	A MALDI-MS analysis of the native protein	836:876	A MALDI-MS analysis of the native protein indicated that FVII is a 50.1 kDa glycoprotein modified on two sites by diantennary, disialylated non-fucosylated (A2S2) glycans.
18642129	3	42	theme	many	358:361	arg1	modifications					382:394	many post-translational modifications	358:394	many post-translational modifications such as gamma-carboxylation, N- and O-glycosylation, beta-hydroxylation	358:466	Plasma-derived FVII undergoes many post-translational modifications such as gamma-carboxylation, N- and O-glycosylation, beta-hydroxylation.
18642129	3	42	theme	many	358:361	arg1	gamma-carboxylation					404:422	gamma-carboxylation	404:422	gamma-carboxylation	404:422	Plasma-derived FVII undergoes many post-translational modifications such as gamma-carboxylation, N- and O-glycosylation, beta-hydroxylation.
18642129	8	43	located	found	1216:1220	arg2	structures					1200:1209	triantennary structures	1187:1209	triantennary structures	1187:1209	Nevertheless, lower amounts of triantennary structures were found on Asn(322) compared to Asn(145).
18642129	8	43	located	found	1216:1220	arg2	amounts					1176:1182	lower amounts	1170:1182	lower amounts of triantennary structures	1170:1209	Nevertheless, lower amounts of triantennary structures were found on Asn(322) compared to Asn(145).
18642129	8	43	located	found	1216:1220	arg1	322					1229:1231	322	1229:1231	322	1229:1231	Nevertheless, lower amounts of triantennary structures were found on Asn(322) compared to Asn(145).
18642129	8	43	located	found	1216:1220	arg1	Asn					1225:1227	Asn	1225:1227	Asn(322)	1225:1232	Nevertheless, lower amounts of triantennary structures were found on Asn(322) compared to Asn(145).
18642129	2	44	theme	peptide	297:303	arg1	FVII					270:273	FVII	270:273	FVII	270:273	FVII is secreted as single peptide chain of 406 residues.
18642129	2	44	theme	peptide	297:303	arg1	chain					305:309	single peptide chain	290:309	single peptide chain of 406 residues	290:325	FVII is secreted as single peptide chain of 406 residues.
18642129	11	45	gly	difucosylated	1589:1601	arg1	structures					1603:1612	triantennary difucosylated structures	1576:1612	triantennary difucosylated structures	1576:1612	Glycan sequencing using different glycanases led to the identification of triantennary difucosylated structures.
18642129	11	46	theme	structures	1603:1612	arg1	identification					1558:1571	the identification	1554:1571	the identification of triantennary difucosylated structures	1554:1612	Glycan sequencing using different glycanases led to the identification of triantennary difucosylated structures.
18642129	13	47	link	plasma-derived	1887:1900	arg1	FVII					1902:1905	plasma-derived FVII	1887:1905	plasma-derived FVII	1887:1905	These latter three O-glycans coexist in equal amounts in plasma-derived FVII.
18642129	12	48	theme	oligosaccharide	1753:1767	arg1	structures					1769:1778	oligosaccharide structures	1753:1778	oligosaccharide structures such as fucose and Glc(Xyl)(0-1-2), respectively	1753:1827	Last, MS and MS/MS analysis revealed that FVII is O-glycosylated on the light chain at position Ser(60) and Ser(52) which are modified by oligosaccharide structures such as fucose and Glc(Xyl)(0-1-2), respectively.
18642129	12	48	theme	oligosaccharide	1753:1767	arg1	fucose					1788:1793	fucose	1788:1793	fucose	1788:1793	Last, MS and MS/MS analysis revealed that FVII is O-glycosylated on the light chain at position Ser(60) and Ser(52) which are modified by oligosaccharide structures such as fucose and Glc(Xyl)(0-1-2), respectively.
18642129	12	48	theme	oligosaccharide	1753:1767	arg1	Glc					1799:1801	Glc	1799:1801	Glc	1799:1801	Last, MS and MS/MS analysis revealed that FVII is O-glycosylated on the light chain at position Ser(60) and Ser(52) which are modified by oligosaccharide structures such as fucose and Glc(Xyl)(0-1-2), respectively.
18642129	4	49	theme	plasma-derived	589:602	arg1	FVII					604:607	plasma-derived FVII	589:607	plasma-derived FVII (pd-FVII)	589:617	Despite glycosylation of recombinant FVIIa has been fully characterized, nothing is reported on the N- and O-glycans of plasma-derived FVII (pd-FVII) and on their structural heterogeneity at each glycosylation site.
18642129	4	49	theme	plasma-derived	589:602	arg1	pd-FVII					610:616	pd-FVII	610:616	pd-FVII	610:616	Despite glycosylation of recombinant FVIIa has been fully characterized, nothing is reported on the N- and O-glycans of plasma-derived FVII (pd-FVII) and on their structural heterogeneity at each glycosylation site.
18642129	2	50	theme	residues	318:325	arg1	FVII					270:273	FVII	270:273	FVII	270:273	FVII is secreted as single peptide chain of 406 residues.
18642129	2	50	theme	residues	318:325	arg1	chain					305:309	single peptide chain	290:309	single peptide chain of 406 residues	290:325	FVII is secreted as single peptide chain of 406 residues.
18642129	7	51	theme	triantennary	1123:1134	arg1	glycans					1147:1153	triantennary sialylated glycans	1123:1153	triantennary sialylated glycans	1123:1153	LC-ESIMS/MS analysis revealed that both light chain and heavy chain were N-glycosylated mainly by A2S2 but also by triantennary sialylated glycans.
18642129	1	52	theme	coagulation	212:222	arg1	process					224:230	the coagulation process	208:230	the coagulation process	208:230	Factor VII (FVII) is a vitamin K-dependent glycoprotein which, in its activated form (FVIIa), participates in the coagulation process by activating factor X and factor IX.
18642129	4	53	link	plasma-derived	589:602	arg1	FVII					604:607	plasma-derived FVII	589:607	plasma-derived FVII (pd-FVII)	589:617	Despite glycosylation of recombinant FVIIa has been fully characterized, nothing is reported on the N- and O-glycans of plasma-derived FVII (pd-FVII) and on their structural heterogeneity at each glycosylation site.
18642129	4	53	link	plasma-derived	589:602	arg1	pd-FVII					610:616	pd-FVII	610:616	pd-FVII	610:616	Despite glycosylation of recombinant FVIIa has been fully characterized, nothing is reported on the N- and O-glycans of plasma-derived FVII (pd-FVII) and on their structural heterogeneity at each glycosylation site.
18642129	10	54	theme	glycans	1372:1378	arg1	analysis					1347:1354	quantitative analysis	1334:1354	quantitative analysis of the isolated glycans by capillary electrophoresis	1334:1407	In parallel, quantitative analysis of the isolated glycans by capillary electrophoresis indicated that the diantennary structures represented about 50% of the total glycan content.
18642129	8	55	theme	lower	1170:1174	arg1	amounts					1176:1182	lower amounts	1170:1182	lower amounts of triantennary structures	1170:1209	Nevertheless, lower amounts of triantennary structures were found on Asn(322) compared to Asn(145).
18642129	8	55	theme	lower	1170:1174	arg1	structures					1200:1209	triantennary structures	1187:1209	triantennary structures	1187:1209	Nevertheless, lower amounts of triantennary structures were found on Asn(322) compared to Asn(145).
18642129	6	56	theme	50.1	903:906	arg1	kDa					908:910	kDa	908:910	kDa	908:910	A MALDI-MS analysis of the native protein indicated that FVII is a 50.1 kDa glycoprotein modified on two sites by diantennary, disialylated non-fucosylated (A2S2) glycans.
18642129	0	57	theme	O-glycans	46:54	arg1	characterization					19:34	Mass spectrometric characterization	0:34	Mass spectrometric characterization of N- and O-glycans of plasma-derived coagulation factor VII.	0:96	Mass spectrometric characterization of N- and O-glycans of plasma-derived coagulation factor VII.
18642129	4	58	theme	structural	632:641	arg1	heterogeneity					643:655	their structural heterogeneity	626:655	their structural heterogeneity at each glycosylation site	626:682	Despite glycosylation of recombinant FVIIa has been fully characterized, nothing is reported on the N- and O-glycans of plasma-derived FVII (pd-FVII) and on their structural heterogeneity at each glycosylation site.
18642129	11	59	theme	triantennary	1576:1587	arg1	structures					1603:1612	triantennary difucosylated structures	1576:1612	triantennary difucosylated structures	1576:1612	Glycan sequencing using different glycanases led to the identification of triantennary difucosylated structures.
18642129	8	60	theme	structures	1200:1209	arg1	amounts					1176:1182	lower amounts	1170:1182	lower amounts of triantennary structures	1170:1209	Nevertheless, lower amounts of triantennary structures were found on Asn(322) compared to Asn(145).
18642129	8	60	theme	structures	1200:1209	arg1	structures					1200:1209	triantennary structures	1187:1209	triantennary structures	1187:1209	Nevertheless, lower amounts of triantennary structures were found on Asn(322) compared to Asn(145).
18642129	12	61	theme	MS	1621:1622	arg1	analysis					1634:1641	MS and MS/MS analysis	1621:1641	analysis	1634:1641	Last, MS and MS/MS analysis revealed that FVII is O-glycosylated on the light chain at position Ser(60) and Ser(52) which are modified by oligosaccharide structures such as fucose and Glc(Xyl)(0-1-2), respectively.
18642129	6	62	gly	disialylated	963:974	arg1	glycans					999:1005	diantennary, disialylated non-fucosylated (A2S2) glycans	950:1005	glycans	999:1005	A MALDI-MS analysis of the native protein indicated that FVII is a 50.1 kDa glycoprotein modified on two sites by diantennary, disialylated non-fucosylated (A2S2) glycans.
18642129	6	63	theme	disialylated	963:974	arg1	glycans					999:1005	diantennary, disialylated non-fucosylated (A2S2) glycans	950:1005	glycans	999:1005	A MALDI-MS analysis of the native protein indicated that FVII is a 50.1 kDa glycoprotein modified on two sites by diantennary, disialylated non-fucosylated (A2S2) glycans.
18642129	7	64	theme	heavy	1064:1068	arg1	chain					1070:1074	heavy chain	1064:1074	heavy chain	1064:1074	LC-ESIMS/MS analysis revealed that both light chain and heavy chain were N-glycosylated mainly by A2S2 but also by triantennary sialylated glycans.
18642129	6	65	theme	diantennary	950:960	arg1	glycans					999:1005	diantennary, disialylated non-fucosylated (A2S2) glycans	950:1005	glycans	999:1005	A MALDI-MS analysis of the native protein indicated that FVII is a 50.1 kDa glycoprotein modified on two sites by diantennary, disialylated non-fucosylated (A2S2) glycans.
18642129	4	66	gly	glycosylation	665:677	arg2	site					679:682	each glycosylation site	660:682	each glycosylation site	660:682	Despite glycosylation of recombinant FVIIa has been fully characterized, nothing is reported on the N- and O-glycans of plasma-derived FVII (pd-FVII) and on their structural heterogeneity at each glycosylation site.
18642129	10	67	theme	capillary	1383:1391	arg1	electrophoresis					1393:1407	capillary electrophoresis	1383:1407	capillary electrophoresis	1383:1407	In parallel, quantitative analysis of the isolated glycans by capillary electrophoresis indicated that the diantennary structures represented about 50% of the total glycan content.
18642129	13	68	from	amounts	1876:1882	arg1	FVII					1902:1905	plasma-derived FVII	1887:1905	plasma-derived FVII	1887:1905	These latter three O-glycans coexist in equal amounts in plasma-derived FVII.
18642129	5	69	theme	pd-FVII	749:755	arg1	heterogeneity					732:744	site specific heterogeneity	718:744	site specific heterogeneity of pd-FVII	718:755	N- and O-glycosylation sites and site specific heterogeneity of pd-FVII were studied by various complementary qualitative and quantitative techniques.
18642129	5	69	theme	pd-FVII	749:755	arg1	sites					708:712	N- and O-glycosylation sites	685:712	N- and O-glycosylation sites	685:712	N- and O-glycosylation sites and site specific heterogeneity of pd-FVII were studied by various complementary qualitative and quantitative techniques.
18642129	5	69	theme	pd-FVII	749:755	arg1	pd-FVII					749:755	pd-FVII	749:755	pd-FVII	749:755	N- and O-glycosylation sites and site specific heterogeneity of pd-FVII were studied by various complementary qualitative and quantitative techniques.
18642129	11	70	theme	Glycan	1502:1507	arg1	sequencing					1509:1518	Glycan sequencing	1502:1518	Glycan sequencing using different glycanases	1502:1545	Glycan sequencing using different glycanases led to the identification of triantennary difucosylated structures.
18642129	12	71	mod	modified	1741:1748	arg3	Glc					1799:1801	Glc	1799:1801	Glc	1799:1801	Last, MS and MS/MS analysis revealed that FVII is O-glycosylated on the light chain at position Ser(60) and Ser(52) which are modified by oligosaccharide structures such as fucose and Glc(Xyl)(0-1-2), respectively.
18642129	12	71	mod	modified	1741:1748	arg3	structures					1769:1778	oligosaccharide structures	1753:1778	oligosaccharide structures such as fucose and Glc(Xyl)(0-1-2), respectively	1753:1827	Last, MS and MS/MS analysis revealed that FVII is O-glycosylated on the light chain at position Ser(60) and Ser(52) which are modified by oligosaccharide structures such as fucose and Glc(Xyl)(0-1-2), respectively.
18642129	12	71	mod	modified	1741:1748	arg1	position					1702:1709	position Ser(60) and Ser(52)	1702:1729	position Ser(60) and Ser(52) which are modified by oligosaccharide structures such as fucose and Glc(Xyl)(0-1-2), respectively	1702:1827	Last, MS and MS/MS analysis revealed that FVII is O-glycosylated on the light chain at position Ser(60) and Ser(52) which are modified by oligosaccharide structures such as fucose and Glc(Xyl)(0-1-2), respectively.
18642129	12	71	mod	modified	1741:1748	arg3	fucose					1788:1793	fucose	1788:1793	fucose	1788:1793	Last, MS and MS/MS analysis revealed that FVII is O-glycosylated on the light chain at position Ser(60) and Ser(52) which are modified by oligosaccharide structures such as fucose and Glc(Xyl)(0-1-2), respectively.
18642129	1	72	theme	vitamin	121:127	arg1	VII					105:107	Factor VII	98:107	Factor VII (FVII)	98:114	Factor VII (FVII) is a vitamin K-dependent glycoprotein which, in its activated form (FVIIa), participates in the coagulation process by activating factor X and factor IX.
18642129	1	72	theme	vitamin	121:127	arg1	glycoprotein					141:152	a vitamin K-dependent glycoprotein	119:152	a vitamin K-dependent glycoprotein which, in its activated form (FVIIa), participates in the coagulation process by activating factor X and factor IX	119:267	Factor VII (FVII) is a vitamin K-dependent glycoprotein which, in its activated form (FVIIa), participates in the coagulation process by activating factor X and factor IX.
18642129	4	73	theme	FVIIa	506:510	arg1	glycosylation					477:489	glycosylation	477:489	glycosylation of recombinant FVIIa	477:510	Despite glycosylation of recombinant FVIIa has been fully characterized, nothing is reported on the N- and O-glycans of plasma-derived FVII (pd-FVII) and on their structural heterogeneity at each glycosylation site.
18642129	4	74	theme	glycosylation	665:677	arg1	site					679:682	each glycosylation site	660:682	each glycosylation site	660:682	Despite glycosylation of recombinant FVIIa has been fully characterized, nothing is reported on the N- and O-glycans of plasma-derived FVII (pd-FVII) and on their structural heterogeneity at each glycosylation site.
18642129	0	75	theme	VII	93:95	arg1	O-glycans					46:54	O-glycans	46:54	O-glycans	46:54	Mass spectrometric characterization of N- and O-glycans of plasma-derived coagulation factor VII.
18642129	0	75	theme	VII	93:95	arg1	N-					39:40	N-	39:40	N-	39:40	Mass spectrometric characterization of N- and O-glycans of plasma-derived coagulation factor VII.
18642129	12	76	theme	MS/MS	1628:1632	arg1	analysis					1634:1641	MS and MS/MS analysis	1621:1641	analysis	1634:1641	Last, MS and MS/MS analysis revealed that FVII is O-glycosylated on the light chain at position Ser(60) and Ser(52) which are modified by oligosaccharide structures such as fucose and Glc(Xyl)(0-1-2), respectively.
18642129	12	77	theme	light	1687:1691	arg1	chain					1693:1697	the light chain	1683:1697	the light chain at position Ser(60) and Ser(52) which are modified by oligosaccharide structures such as fucose and Glc(Xyl)(0-1-2), respectively	1683:1827	Last, MS and MS/MS analysis revealed that FVII is O-glycosylated on the light chain at position Ser(60) and Ser(52) which are modified by oligosaccharide structures such as fucose and Glc(Xyl)(0-1-2), respectively.
18642129	13	78	theme	latter	1836:1841	arg1	O-glycans					1849:1857	These latter three O-glycans	1830:1857	These latter three O-glycans	1830:1857	These latter three O-glycans coexist in equal amounts in plasma-derived FVII.
18642129	5	79	theme	site	718:721	arg1	heterogeneity					732:744	site specific heterogeneity	718:744	site specific heterogeneity of pd-FVII	718:755	N- and O-glycosylation sites and site specific heterogeneity of pd-FVII were studied by various complementary qualitative and quantitative techniques.
18642129	9	80	gly	fucosylated	1308:1318	arg1	glycans					1283:1289	the triantennary glycans	1266:1289	the triantennary glycans	1266:1289	Moreover, the triantennary glycans were shown to be fucosylated.
18642129	5	81	theme	quantitative	811:822	arg1	techniques					824:833	various complementary qualitative and quantitative techniques	773:833	various complementary qualitative and quantitative techniques	773:833	N- and O-glycosylation sites and site specific heterogeneity of pd-FVII were studied by various complementary qualitative and quantitative techniques.
18642129	3	82	theme	Plasma-derived	328:341	arg1	FVII					343:346	Plasma-derived FVII	328:346	Plasma-derived FVII	328:346	Plasma-derived FVII undergoes many post-translational modifications such as gamma-carboxylation, N- and O-glycosylation, beta-hydroxylation.
18642129	12	83	gly	O-glycosylated	1665:1678	arg1	FVII					1657:1660	FVII	1657:1660	FVII	1657:1660	Last, MS and MS/MS analysis revealed that FVII is O-glycosylated on the light chain at position Ser(60) and Ser(52) which are modified by oligosaccharide structures such as fucose and Glc(Xyl)(0-1-2), respectively.
18642129	12	83	gly	O-glycosylated	1665:1678	arg2	FVII					1657:1660	FVII	1657:1660	FVII	1657:1660	Last, MS and MS/MS analysis revealed that FVII is O-glycosylated on the light chain at position Ser(60) and Ser(52) which are modified by oligosaccharide structures such as fucose and Glc(Xyl)(0-1-2), respectively.
18642129	12	83	gly	O-glycosylated	1665:1678	arg1	chain					1693:1697	the light chain	1683:1697	the light chain at position Ser(60) and Ser(52) which are modified by oligosaccharide structures such as fucose and Glc(Xyl)(0-1-2), respectively	1683:1827	Last, MS and MS/MS analysis revealed that FVII is O-glycosylated on the light chain at position Ser(60) and Ser(52) which are modified by oligosaccharide structures such as fucose and Glc(Xyl)(0-1-2), respectively.
18642129	12	83	gly	O-glycosylated	1665:1678	arg2	chain					1693:1697	the light chain	1683:1697	the light chain at position Ser(60) and Ser(52) which are modified by oligosaccharide structures such as fucose and Glc(Xyl)(0-1-2), respectively	1683:1827	Last, MS and MS/MS analysis revealed that FVII is O-glycosylated on the light chain at position Ser(60) and Ser(52) which are modified by oligosaccharide structures such as fucose and Glc(Xyl)(0-1-2), respectively.
18642129	5	84	gly	heterogeneity	732:744	arg1	pd-FVII					749:755	pd-FVII	749:755	pd-FVII	749:755	N- and O-glycosylation sites and site specific heterogeneity of pd-FVII were studied by various complementary qualitative and quantitative techniques.
18642129	5	85	theme	various	773:779	arg1	techniques					824:833	various complementary qualitative and quantitative techniques	773:833	various complementary qualitative and quantitative techniques	773:833	N- and O-glycosylation sites and site specific heterogeneity of pd-FVII were studied by various complementary qualitative and quantitative techniques.
18642129	1	86	theme	factor	259:264	arg1	IX					266:267	factor IX	259:267	factor IX	259:267	Factor VII (FVII) is a vitamin K-dependent glycoprotein which, in its activated form (FVIIa), participates in the coagulation process by activating factor X and factor IX.
18642129	5	87	theme	qualitative	795:805	arg1	techniques					824:833	various complementary qualitative and quantitative techniques	773:833	various complementary qualitative and quantitative techniques	773:833	N- and O-glycosylation sites and site specific heterogeneity of pd-FVII were studied by various complementary qualitative and quantitative techniques.
18642129	6	88	theme	native	863:868	arg1	protein					870:876	the native protein	859:876	the native protein	859:876	A MALDI-MS analysis of the native protein indicated that FVII is a 50.1 kDa glycoprotein modified on two sites by diantennary, disialylated non-fucosylated (A2S2) glycans.
18642129	3	89	theme	post-translational	363:380	arg1	modifications					382:394	many post-translational modifications	358:394	many post-translational modifications such as gamma-carboxylation, N- and O-glycosylation, beta-hydroxylation	358:466	Plasma-derived FVII undergoes many post-translational modifications such as gamma-carboxylation, N- and O-glycosylation, beta-hydroxylation.
18642129	3	89	theme	post-translational	363:380	arg1	gamma-carboxylation					404:422	gamma-carboxylation	404:422	gamma-carboxylation	404:422	Plasma-derived FVII undergoes many post-translational modifications such as gamma-carboxylation, N- and O-glycosylation, beta-hydroxylation.
18642129	11	90	theme	difucosylated	1589:1601	arg1	structures					1603:1612	triantennary difucosylated structures	1576:1612	triantennary difucosylated structures	1576:1612	Glycan sequencing using different glycanases led to the identification of triantennary difucosylated structures.
18642129	2	91	theme	single	290:295	arg1	FVII					270:273	FVII	270:273	FVII	270:273	FVII is secreted as single peptide chain of 406 residues.
18642129	2	91	theme	single	290:295	arg1	chain					305:309	single peptide chain	290:309	single peptide chain of 406 residues	290:325	FVII is secreted as single peptide chain of 406 residues.
18642129	0	92	link	plasma-derived	59:72	arg1	VII					93:95	plasma-derived coagulation factor VII	59:95	plasma-derived coagulation factor VII	59:95	Mass spectrometric characterization of N- and O-glycans of plasma-derived coagulation factor VII.
18642129	4	93	theme	FVII	604:607	arg1	N-					569:570	N-	569:570	N-	569:570	Despite glycosylation of recombinant FVIIa has been fully characterized, nothing is reported on the N- and O-glycans of plasma-derived FVII (pd-FVII) and on their structural heterogeneity at each glycosylation site.
18642129	6	94	theme	MALDI-MS	838:845	arg1	analysis					847:854	A MALDI-MS analysis	836:854	A MALDI-MS analysis of the native protein	836:876	A MALDI-MS analysis of the native protein indicated that FVII is a 50.1 kDa glycoprotein modified on two sites by diantennary, disialylated non-fucosylated (A2S2) glycans.
18642129	10	95	theme	quantitative	1334:1345	arg1	analysis					1347:1354	quantitative analysis	1334:1354	quantitative analysis of the isolated glycans by capillary electrophoresis	1334:1407	In parallel, quantitative analysis of the isolated glycans by capillary electrophoresis indicated that the diantennary structures represented about 50% of the total glycan content.
18642129	0	96	theme	spectrometric	5:17	arg1	characterization					19:34	Mass spectrometric characterization	0:34	Mass spectrometric characterization of N- and O-glycans of plasma-derived coagulation factor VII.	0:96	Mass spectrometric characterization of N- and O-glycans of plasma-derived coagulation factor VII.
7613477	2	0	theme	human	719:723	arg1	preparation					738:748	a human LCAT protein preparation	717:748	a human LCAT protein preparation	717:748	A recently described mass spectrometric technique involving monitoring of carbohydrate-specific fragment ions during HPLC/ESIMS was employed to locate eight different groups of glycopeptides in a digest of a human LCAT protein preparation.
7613477	1	1	theme	electrospray	455:466	arg1	spectrometry					484:495	electrospray ionization mass spectrometry	455:495	electrospray ionization mass spectrometry (HPLC/ESIMS)	455:508	Site-specific structural characterization of the glycosylation of human lecithin:cholesterol acyltransferase (LCAT) was carried out using microbore reversed-phase high performance liquid chromatography coupled with electrospray ionization mass spectrometry (HPLC/ESIMS).
7613477	1	1	theme	electrospray	455:466	arg1	HPLC/ESIMS					498:507	HPLC/ESIMS	498:507	HPLC/ESIMS	498:507	Site-specific structural characterization of the glycosylation of human lecithin:cholesterol acyltransferase (LCAT) was carried out using microbore reversed-phase high performance liquid chromatography coupled with electrospray ionization mass spectrometry (HPLC/ESIMS).
7613477	0	2	theme	sequential	206:215	arg1	digestion					229:237	sequential glycosidase digestion	206:237	sequential glycosidase digestion	206:237	Site-specific detection and structural characterization of the glycosylation of human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D using HPLC/electrospray mass spectrometry and sequential glycosidase digestion.
7613477	4	3	theme	glycosidase	1003:1013	arg1	digestion					1015:1023	sequential glycosidase digestion	992:1023	sequential glycosidase digestion of the glycopeptides followed by HPLC/ESIMS	992:1067	Structural information on the oligosaccharides from all eight glycopeptides was obtained by sequential glycosidase digestion of the glycopeptides followed by HPLC/ESIMS.
7613477	0	4	dep	proteins	93:100	arg1	D					158:158	apolipoprotein D	143:158	apolipoprotein D	143:158	Site-specific detection and structural characterization of the glycosylation of human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D using HPLC/electrospray mass spectrometry and sequential glycosidase digestion.
7613477	0	4	dep	proteins	93:100	arg1	proteins					93:100	human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D	80:158	human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D	80:158	Site-specific detection and structural characterization of the glycosylation of human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D using HPLC/electrospray mass spectrometry and sequential glycosidase digestion.
7613477	0	4	dep	proteins	93:100	arg1	acyltransferase					123:137	lecithin:cholesterol acyltransferase	102:137	lecithin:cholesterol acyltransferase	102:137	Site-specific detection and structural characterization of the glycosylation of human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D using HPLC/electrospray mass spectrometry and sequential glycosidase digestion.
7613477	9	5	attach	removal	1815:1821	arg3	Asn272					1852:1857	Asn272	1852:1857	Asn272	1852:1857	Previous studies of LCAT indicated that removal of the glycosylation site at Asn272 converts this protein to a phospholipase (Francone OL, Evangelista L, Fielding CJ, 1993, Biochim Biophys Acta 1166:301-304).
7613477	9	5	attach	removal	1815:1821	arg2	site					1844:1847	the glycosylation site	1826:1847	the glycosylation site	1826:1847	Previous studies of LCAT indicated that removal of the glycosylation site at Asn272 converts this protein to a phospholipase (Francone OL, Evangelista L, Fielding CJ, 1993, Biochim Biophys Acta 1166:301-304).
7613477	3	6	theme	di-O-linked	818:828	arg1	glycopeptide					830:841	a di-O-linked glycopeptide	816:841	a di-O-linked glycopeptide	816:841	In addition to the four expected N-linked glycopeptides of LCAT, a di-O-linked glycopeptide was detected, as well as three additional glycopeptides.
7613477	6	7	theme	beta	1413:1416	arg1	structures					1445:1454	sialylated galactose beta 1-->3N-acetylgalactosamine structures	1392:1454	sialylated galactose beta 1-->3N-acetylgalactosamine structures	1392:1454	Two unanticipated O-linked glycosylation sites were identified at Thr407 and Ser409 of the LCAT O-linked glycopeptide, each of which contain sialylated galactose beta 1-->3N-acetylgalactosamine structures.
7613477	2	8	theme	protein	730:736	arg1	preparation					738:748	a human LCAT protein preparation	717:748	a human LCAT protein preparation	717:748	A recently described mass spectrometric technique involving monitoring of carbohydrate-specific fragment ions during HPLC/ESIMS was employed to locate eight different groups of glycopeptides in a digest of a human LCAT protein preparation.
7613477	7	9	theme	glycosylation	1594:1606	arg1	sites					1608:1612	potential N-linked glycosylation sites	1575:1612	potential N-linked glycosylation sites	1575:1612	The three additional glycopeptides were determined to be from a copurifying protein, apolipoprotein D, which contains potential N-linked glycosylation sites at Asn45 and Asn78.
7613477	6	10	theme	sialylated	1392:1401	arg1	structures					1445:1454	sialylated galactose beta 1-->3N-acetylgalactosamine structures	1392:1454	sialylated galactose beta 1-->3N-acetylgalactosamine structures	1392:1454	Two unanticipated O-linked glycosylation sites were identified at Thr407 and Ser409 of the LCAT O-linked glycopeptide, each of which contain sialylated galactose beta 1-->3N-acetylgalactosamine structures.
7613477	7	11	theme	potential	1575:1583	arg1	sites					1608:1612	potential N-linked glycosylation sites	1575:1612	potential N-linked glycosylation sites	1575:1612	The three additional glycopeptides were determined to be from a copurifying protein, apolipoprotein D, which contains potential N-linked glycosylation sites at Asn45 and Asn78.
7613477	1	12	theme	ionization	468:477	arg1	spectrometry					484:495	electrospray ionization mass spectrometry	455:495	electrospray ionization mass spectrometry (HPLC/ESIMS)	455:508	Site-specific structural characterization of the glycosylation of human lecithin:cholesterol acyltransferase (LCAT) was carried out using microbore reversed-phase high performance liquid chromatography coupled with electrospray ionization mass spectrometry (HPLC/ESIMS).
7613477	1	12	theme	ionization	468:477	arg1	HPLC/ESIMS					498:507	HPLC/ESIMS	498:507	HPLC/ESIMS	498:507	Site-specific structural characterization of the glycosylation of human lecithin:cholesterol acyltransferase (LCAT) was carried out using microbore reversed-phase high performance liquid chromatography coupled with electrospray ionization mass spectrometry (HPLC/ESIMS).
7613477	1	13	theme	structural	254:263	arg1	characterization					265:280	Site-specific structural characterization	240:280	Site-specific structural characterization of the glycosylation of human lecithin:cholesterol acyltransferase (LCAT)	240:354	Site-specific structural characterization of the glycosylation of human lecithin:cholesterol acyltransferase (LCAT) was carried out using microbore reversed-phase high performance liquid chromatography coupled with electrospray ionization mass spectrometry (HPLC/ESIMS).
7613477	6	14	link	O-linked	1347:1354	arg1	glycopeptide					1356:1367	the LCAT O-linked glycopeptide	1338:1367	the LCAT O-linked glycopeptide	1338:1367	Two unanticipated O-linked glycosylation sites were identified at Thr407 and Ser409 of the LCAT O-linked glycopeptide, each of which contain sialylated galactose beta 1-->3N-acetylgalactosamine structures.
7613477	10	15	theme	carbohydrate	2014:2025	arg1	source					2061:2066	the source	2057:2066	the source of this functional discrimination	2057:2100	Our results indicate that the carbohydrate structures themselves are not the source of this functional discrimination; rather, it must be mediated by the structural environment around Asn272.
7613477	10	15	theme	carbohydrate	2014:2025	arg1	structures					2027:2036	the carbohydrate structures	2010:2036	the carbohydrate structures themselves	2010:2047	Our results indicate that the carbohydrate structures themselves are not the source of this functional discrimination; rather, it must be mediated by the structural environment around Asn272.
7613477	8	16	gly	sialylated	1678:1687	arg1	oligosaccharides					1702:1717	sialylated triantennary oligosaccharides	1678:1717	sialylated triantennary oligosaccharides	1678:1717	These glycopeptides were determined to bear sialylated triantennary oligosaccharides or fucosylated sialylated biantennary oligosaccharides.
7613477	4	17	theme	glycopeptides	1032:1044	arg1	digestion					1015:1023	sequential glycosidase digestion	992:1023	sequential glycosidase digestion of the glycopeptides followed by HPLC/ESIMS	992:1067	Structural information on the oligosaccharides from all eight glycopeptides was obtained by sequential glycosidase digestion of the glycopeptides followed by HPLC/ESIMS.
7613477	0	18	theme	HPLC/electrospray	166:182	arg1	spectrometry					189:200	HPLC/electrospray mass spectrometry	166:200	HPLC/electrospray mass spectrometry	166:200	Site-specific detection and structural characterization of the glycosylation of human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D using HPLC/electrospray mass spectrometry and sequential glycosidase digestion.
7613477	2	19	theme	glycopeptides	688:700	arg1	glycopeptides					688:700	glycopeptides	688:700	glycopeptides	688:700	A recently described mass spectrometric technique involving monitoring of carbohydrate-specific fragment ions during HPLC/ESIMS was employed to locate eight different groups of glycopeptides in a digest of a human LCAT protein preparation.
7613477	2	19	theme	glycopeptides	688:700	arg1	groups					678:683	eight different groups	662:683	eight different groups of glycopeptides	662:700	A recently described mass spectrometric technique involving monitoring of carbohydrate-specific fragment ions during HPLC/ESIMS was employed to locate eight different groups of glycopeptides in a digest of a human LCAT protein preparation.
7613477	2	20	gly	glycopeptides	688:700	arg2	glycopeptides					688:700	glycopeptides	688:700	glycopeptides	688:700	A recently described mass spectrometric technique involving monitoring of carbohydrate-specific fragment ions during HPLC/ESIMS was employed to locate eight different groups of glycopeptides in a digest of a human LCAT protein preparation.
7613477	6	21	theme	O-linked	1347:1354	arg1	glycopeptide					1356:1367	the LCAT O-linked glycopeptide	1338:1367	the LCAT O-linked glycopeptide	1338:1367	Two unanticipated O-linked glycosylation sites were identified at Thr407 and Ser409 of the LCAT O-linked glycopeptide, each of which contain sialylated galactose beta 1-->3N-acetylgalactosamine structures.
7613477	7	22	contain	contains	1566:1573	arg2	protein					1533:1539	a copurifying protein	1519:1539	a copurifying protein	1519:1539	The three additional glycopeptides were determined to be from a copurifying protein, apolipoprotein D, which contains potential N-linked glycosylation sites at Asn45 and Asn78.
7613477	7	22	contain	contains	1566:1573	arg1	D					1557:1557	apolipoprotein D	1542:1557	apolipoprotein D	1542:1557	The three additional glycopeptides were determined to be from a copurifying protein, apolipoprotein D, which contains potential N-linked glycosylation sites at Asn45 and Asn78.
7613477	7	22	contain	contains	1566:1573	arg1	Asn45					1617:1621	Asn45	1617:1621	Asn45	1617:1621	The three additional glycopeptides were determined to be from a copurifying protein, apolipoprotein D, which contains potential N-linked glycosylation sites at Asn45 and Asn78.
7613477	7	22	contain	contains	1566:1573	arg2	sites					1608:1612	potential N-linked glycosylation sites	1575:1612	potential N-linked glycosylation sites	1575:1612	The three additional glycopeptides were determined to be from a copurifying protein, apolipoprotein D, which contains potential N-linked glycosylation sites at Asn45 and Asn78.
7613477	7	22	contain	contains	1566:1573	arg1	protein					1533:1539	a copurifying protein	1519:1539	a copurifying protein	1519:1539	The three additional glycopeptides were determined to be from a copurifying protein, apolipoprotein D, which contains potential N-linked glycosylation sites at Asn45 and Asn78.
7613477	7	22	contain	contains	1566:1573	arg1	Asn78					1627:1631	Asn78	1627:1631	Asn78	1627:1631	The three additional glycopeptides were determined to be from a copurifying protein, apolipoprotein D, which contains potential N-linked glycosylation sites at Asn45 and Asn78.
7613477	7	22	contain	contains	1566:1573	arg2	D					1557:1557	apolipoprotein D	1542:1557	apolipoprotein D	1542:1557	The three additional glycopeptides were determined to be from a copurifying protein, apolipoprotein D, which contains potential N-linked glycosylation sites at Asn45 and Asn78.
7613477	1	23	theme	reversed-phase	388:401	arg1	chromatography					427:440	microbore reversed-phase high performance liquid chromatography	378:440	microbore reversed-phase high performance liquid chromatography coupled with electrospray ionization mass spectrometry (HPLC/ESIMS)	378:508	Site-specific structural characterization of the glycosylation of human lecithin:cholesterol acyltransferase (LCAT) was carried out using microbore reversed-phase high performance liquid chromatography coupled with electrospray ionization mass spectrometry (HPLC/ESIMS).
7613477	4	24	from	information	911:921	arg1	oligosaccharides					930:945	the oligosaccharides	926:945	the oligosaccharides from all eight glycopeptides	926:974	Structural information on the oligosaccharides from all eight glycopeptides was obtained by sequential glycosidase digestion of the glycopeptides followed by HPLC/ESIMS.
7613477	4	25	gly	glycopeptides	1032:1044	arg2	glycopeptides					1032:1044	the glycopeptides	1028:1044	the glycopeptides followed by HPLC/ESIMS	1028:1067	Structural information on the oligosaccharides from all eight glycopeptides was obtained by sequential glycosidase digestion of the glycopeptides followed by HPLC/ESIMS.
7613477	2	26	theme	fragment	607:614	arg1	ions					616:619	carbohydrate-specific fragment ions	585:619	carbohydrate-specific fragment ions	585:619	A recently described mass spectrometric technique involving monitoring of carbohydrate-specific fragment ions during HPLC/ESIMS was employed to locate eight different groups of glycopeptides in a digest of a human LCAT protein preparation.
7613477	3	27	gly	glycopeptides	885:897	arg2	glycopeptides					885:897	three additional glycopeptides	868:897	three additional glycopeptides	868:897	In addition to the four expected N-linked glycopeptides of LCAT, a di-O-linked glycopeptide was detected, as well as three additional glycopeptides.
7613477	0	28	theme	plasma	86:91	arg1	D					158:158	apolipoprotein D	143:158	apolipoprotein D	143:158	Site-specific detection and structural characterization of the glycosylation of human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D using HPLC/electrospray mass spectrometry and sequential glycosidase digestion.
7613477	0	28	theme	plasma	86:91	arg1	proteins					93:100	human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D	80:158	human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D	80:158	Site-specific detection and structural characterization of the glycosylation of human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D using HPLC/electrospray mass spectrometry and sequential glycosidase digestion.
7613477	0	28	theme	plasma	86:91	arg1	acyltransferase					123:137	lecithin:cholesterol acyltransferase	102:137	lecithin:cholesterol acyltransferase	102:137	Site-specific detection and structural characterization of the glycosylation of human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D using HPLC/electrospray mass spectrometry and sequential glycosidase digestion.
7613477	1	29	theme	performance	408:418	arg1	chromatography					427:440	microbore reversed-phase high performance liquid chromatography	378:440	microbore reversed-phase high performance liquid chromatography coupled with electrospray ionization mass spectrometry (HPLC/ESIMS)	378:508	Site-specific structural characterization of the glycosylation of human lecithin:cholesterol acyltransferase (LCAT) was carried out using microbore reversed-phase high performance liquid chromatography coupled with electrospray ionization mass spectrometry (HPLC/ESIMS).
7613477	8	30	theme	sialylated	1678:1687	arg1	oligosaccharides					1702:1717	sialylated triantennary oligosaccharides	1678:1717	sialylated triantennary oligosaccharides	1678:1717	These glycopeptides were determined to bear sialylated triantennary oligosaccharides or fucosylated sialylated biantennary oligosaccharides.
7613477	1	31	gly	glycosylation	289:301	arg1	lecithin					312:319	human lecithin	306:319	human lecithin:cholesterol acyltransferase (LCAT)	306:354	Site-specific structural characterization of the glycosylation of human lecithin:cholesterol acyltransferase (LCAT) was carried out using microbore reversed-phase high performance liquid chromatography coupled with electrospray ionization mass spectrometry (HPLC/ESIMS).
7613477	10	32	theme	functional	2076:2085	arg1	discrimination					2087:2100	this functional discrimination	2071:2100	this functional discrimination	2071:2100	Our results indicate that the carbohydrate structures themselves are not the source of this functional discrimination; rather, it must be mediated by the structural environment around Asn272.
7613477	0	33	theme	lecithin	102:109	arg1	proteins					93:100	human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D	80:158	human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D	80:158	Site-specific detection and structural characterization of the glycosylation of human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D using HPLC/electrospray mass spectrometry and sequential glycosidase digestion.
7613477	0	33	theme	lecithin	102:109	arg1	acyltransferase					123:137	lecithin:cholesterol acyltransferase	102:137	lecithin:cholesterol acyltransferase	102:137	Site-specific detection and structural characterization of the glycosylation of human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D using HPLC/electrospray mass spectrometry and sequential glycosidase digestion.
7613477	5	34	theme	complex	1231:1237	arg1	structures					1239:1248	sialylated triantennary and/or biantennary complex structures	1188:1248	structures	1239:1248	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	8	35	gly	fucosylated	1722:1732	arg1	oligosaccharides					1757:1772	fucosylated sialylated biantennary oligosaccharides	1722:1772	fucosylated sialylated biantennary oligosaccharides	1722:1772	These glycopeptides were determined to bear sialylated triantennary oligosaccharides or fucosylated sialylated biantennary oligosaccharides.
7613477	8	36	theme	sialylated	1734:1743	arg1	oligosaccharides					1757:1772	fucosylated sialylated biantennary oligosaccharides	1722:1772	fucosylated sialylated biantennary oligosaccharides	1722:1772	These glycopeptides were determined to bear sialylated triantennary oligosaccharides or fucosylated sialylated biantennary oligosaccharides.
7613477	6	37	gly	glycosylation	1278:1290	arg2	sites					1292:1296	Two unanticipated O-linked glycosylation sites	1251:1296	Two unanticipated O-linked glycosylation sites	1251:1296	Two unanticipated O-linked glycosylation sites were identified at Thr407 and Ser409 of the LCAT O-linked glycopeptide, each of which contain sialylated galactose beta 1-->3N-acetylgalactosamine structures.
7613477	6	37	gly	glycosylation	1278:1290	arg2	Two					1251:1253	Two	1251:1253	Two	1251:1253	Two unanticipated O-linked glycosylation sites were identified at Thr407 and Ser409 of the LCAT O-linked glycopeptide, each of which contain sialylated galactose beta 1-->3N-acetylgalactosamine structures.
7613477	0	38	theme	cholesterol	111:121	arg1	proteins					93:100	human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D	80:158	human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D	80:158	Site-specific detection and structural characterization of the glycosylation of human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D using HPLC/electrospray mass spectrometry and sequential glycosidase digestion.
7613477	0	38	theme	cholesterol	111:121	arg1	acyltransferase					123:137	lecithin:cholesterol acyltransferase	102:137	lecithin:cholesterol acyltransferase	102:137	Site-specific detection and structural characterization of the glycosylation of human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D using HPLC/electrospray mass spectrometry and sequential glycosidase digestion.
7613477	9	39	theme	LCAT	1795:1798	arg1	studies					1784:1790	Previous studies	1775:1790	Previous studies of LCAT	1775:1798	Previous studies of LCAT indicated that removal of the glycosylation site at Asn272 converts this protein to a phospholipase (Francone OL, Evangelista L, Fielding CJ, 1993, Biochim Biophys Acta 1166:301-304).
7613477	9	40	from	Asn272	1852:1857	arg1	removal					1815:1821	removal	1815:1821	removal of the glycosylation site at Asn272	1815:1857	Previous studies of LCAT indicated that removal of the glycosylation site at Asn272 converts this protein to a phospholipase (Francone OL, Evangelista L, Fielding CJ, 1993, Biochim Biophys Acta 1166:301-304).
7613477	2	41	theme	spectrometric	537:549	arg1	technique					551:559	A recently described mass spectrometric technique	511:559	A recently described mass spectrometric technique involving monitoring of carbohydrate-specific fragment ions during HPLC/ESIMS	511:637	A recently described mass spectrometric technique involving monitoring of carbohydrate-specific fragment ions during HPLC/ESIMS was employed to locate eight different groups of glycopeptides in a digest of a human LCAT protein preparation.
7613477	0	42	theme	Site-specific	0:12	arg1	detection					14:22	Site-specific detection	0:22	Site-specific detection	0:22	Site-specific detection and structural characterization of the glycosylation of human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D using HPLC/electrospray mass spectrometry and sequential glycosidase digestion.
7613477	5	43	theme	N-linked	1089:1096	arg1	LCAT					1156:1159	LCAT	1156:1159	LCAT	1156:1159	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	43	theme	N-linked	1089:1096	arg1	sites					1112:1116	All four potential N-linked glycosylation sites	1070:1116	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT	1070:1159	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	43	theme	N-linked	1089:1096	arg1	Asn272					1133:1138	Asn272	1133:1138	Asn272	1133:1138	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	43	theme	N-linked	1089:1096	arg1	Asn384					1145:1150	Asn384	1145:1150	Asn384	1145:1150	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	43	theme	N-linked	1089:1096	arg1	Asn84					1126:1130	Asn84	1126:1130	Asn84	1126:1130	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	2	44	theme	described	522:530	arg1	technique					551:559	A recently described mass spectrometric technique	511:559	A recently described mass spectrometric technique involving monitoring of carbohydrate-specific fragment ions during HPLC/ESIMS	511:637	A recently described mass spectrometric technique involving monitoring of carbohydrate-specific fragment ions during HPLC/ESIMS was employed to locate eight different groups of glycopeptides in a digest of a human LCAT protein preparation.
7613477	7	45	theme	copurifying	1521:1531	arg1	protein					1533:1539	a copurifying protein	1519:1539	a copurifying protein	1519:1539	The three additional glycopeptides were determined to be from a copurifying protein, apolipoprotein D, which contains potential N-linked glycosylation sites at Asn45 and Asn78.
7613477	7	45	theme	copurifying	1521:1531	arg1	D					1557:1557	apolipoprotein D	1542:1557	apolipoprotein D	1542:1557	The three additional glycopeptides were determined to be from a copurifying protein, apolipoprotein D, which contains potential N-linked glycosylation sites at Asn45 and Asn78.
7613477	5	46	contain	contain	1180:1186	arg2	triantennary					1199:1210	triantennary	1199:1210	triantennary	1199:1210	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	46	contain	contain	1180:1186	arg1	Asn384					1145:1150	Asn384	1145:1150	Asn384	1145:1150	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	46	contain	contain	1180:1186	arg1	Asn84					1126:1130	Asn84	1126:1130	Asn84	1126:1130	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	46	contain	contain	1180:1186	arg1	LCAT					1156:1159	LCAT	1156:1159	LCAT	1156:1159	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	46	contain	contain	1180:1186	arg1	sites					1112:1116	All four potential N-linked glycosylation sites	1070:1116	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT	1070:1159	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	46	contain	contain	1180:1186	arg1	Asn272					1133:1138	Asn272	1133:1138	Asn272	1133:1138	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	46	contain	contain	1180:1186	arg2	structures					1239:1248	sialylated triantennary and/or biantennary complex structures	1188:1248	structures	1239:1248	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	6	47	contain	contain	1384:1390	arg1	glycopeptide					1356:1367	the LCAT O-linked glycopeptide	1338:1367	the LCAT O-linked glycopeptide	1338:1367	Two unanticipated O-linked glycosylation sites were identified at Thr407 and Ser409 of the LCAT O-linked glycopeptide, each of which contain sialylated galactose beta 1-->3N-acetylgalactosamine structures.
7613477	6	47	contain	contain	1384:1390	arg2	structures					1445:1454	sialylated galactose beta 1-->3N-acetylgalactosamine structures	1392:1454	sialylated galactose beta 1-->3N-acetylgalactosamine structures	1392:1454	Two unanticipated O-linked glycosylation sites were identified at Thr407 and Ser409 of the LCAT O-linked glycopeptide, each of which contain sialylated galactose beta 1-->3N-acetylgalactosamine structures.
7613477	6	47	contain	contain	1384:1390	arg1	each					1370:1373	each	1370:1373	each	1370:1373	Two unanticipated O-linked glycosylation sites were identified at Thr407 and Ser409 of the LCAT O-linked glycopeptide, each of which contain sialylated galactose beta 1-->3N-acetylgalactosamine structures.
7613477	9	48	theme	Evangelista	1914:1924	arg1	L					1926:1926	Evangelista L	1914:1926	Evangelista L	1914:1926	Previous studies of LCAT indicated that removal of the glycosylation site at Asn272 converts this protein to a phospholipase (Francone OL, Evangelista L, Fielding CJ, 1993, Biochim Biophys Acta 1166:301-304).
7613477	9	48	theme	Evangelista	1914:1924	arg1	Francone					1901:1908	Francone	1901:1908	Francone	1901:1908	Previous studies of LCAT indicated that removal of the glycosylation site at Asn272 converts this protein to a phospholipase (Francone OL, Evangelista L, Fielding CJ, 1993, Biochim Biophys Acta 1166:301-304).
7613477	9	49	theme	glycosylation	1830:1842	arg1	site					1844:1847	the glycosylation site	1826:1847	the glycosylation site	1826:1847	Previous studies of LCAT indicated that removal of the glycosylation site at Asn272 converts this protein to a phospholipase (Francone OL, Evangelista L, Fielding CJ, 1993, Biochim Biophys Acta 1166:301-304).
7613477	7	50	link	N-linked	1585:1592	arg1	sites					1608:1612	potential N-linked glycosylation sites	1575:1612	potential N-linked glycosylation sites	1575:1612	The three additional glycopeptides were determined to be from a copurifying protein, apolipoprotein D, which contains potential N-linked glycosylation sites at Asn45 and Asn78.
7613477	5	51	theme	LCAT	1156:1159	arg1	LCAT					1156:1159	LCAT	1156:1159	LCAT	1156:1159	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	51	theme	LCAT	1156:1159	arg1	sites					1112:1116	All four potential N-linked glycosylation sites	1070:1116	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT	1070:1159	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	51	theme	LCAT	1156:1159	arg1	Asn272					1133:1138	Asn272	1133:1138	Asn272	1133:1138	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	51	theme	LCAT	1156:1159	arg1	Asn384					1145:1150	Asn384	1145:1150	Asn384	1145:1150	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	51	theme	LCAT	1156:1159	arg1	Asn84					1126:1130	Asn84	1126:1130	Asn84	1126:1130	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	6	52	theme	glycosylation	1278:1290	arg1	sites					1292:1296	Two unanticipated O-linked glycosylation sites	1251:1296	Two unanticipated O-linked glycosylation sites	1251:1296	Two unanticipated O-linked glycosylation sites were identified at Thr407 and Ser409 of the LCAT O-linked glycopeptide, each of which contain sialylated galactose beta 1-->3N-acetylgalactosamine structures.
7613477	8	53	contain	bear	1673:1676	arg1	glycopeptides					1640:1652	These glycopeptides	1634:1652	These glycopeptides	1634:1652	These glycopeptides were determined to bear sialylated triantennary oligosaccharides or fucosylated sialylated biantennary oligosaccharides.
7613477	8	53	contain	bear	1673:1676	arg2	oligosaccharides					1757:1772	fucosylated sialylated biantennary oligosaccharides	1722:1772	fucosylated sialylated biantennary oligosaccharides	1722:1772	These glycopeptides were determined to bear sialylated triantennary oligosaccharides or fucosylated sialylated biantennary oligosaccharides.
7613477	8	53	contain	bear	1673:1676	arg2	oligosaccharides					1702:1717	sialylated triantennary oligosaccharides	1678:1717	sialylated triantennary oligosaccharides	1678:1717	These glycopeptides were determined to bear sialylated triantennary oligosaccharides or fucosylated sialylated biantennary oligosaccharides.
7613477	6	54	theme	unanticipated	1255:1267	arg1	sites					1292:1296	Two unanticipated O-linked glycosylation sites	1251:1296	Two unanticipated O-linked glycosylation sites	1251:1296	Two unanticipated O-linked glycosylation sites were identified at Thr407 and Ser409 of the LCAT O-linked glycopeptide, each of which contain sialylated galactose beta 1-->3N-acetylgalactosamine structures.
7613477	3	55	link	N-linked	784:791	arg1	glycopeptides					793:805	the four expected N-linked glycopeptides	766:805	the four expected N-linked glycopeptides of LCAT	766:813	In addition to the four expected N-linked glycopeptides of LCAT, a di-O-linked glycopeptide was detected, as well as three additional glycopeptides.
7613477	6	56	gly	glycopeptide	1356:1367	arg2	glycopeptide					1356:1367	the LCAT O-linked glycopeptide	1338:1367	the LCAT O-linked glycopeptide	1338:1367	Two unanticipated O-linked glycosylation sites were identified at Thr407 and Ser409 of the LCAT O-linked glycopeptide, each of which contain sialylated galactose beta 1-->3N-acetylgalactosamine structures.
7613477	3	57	theme	expected	775:782	arg1	glycopeptides					793:805	the four expected N-linked glycopeptides	766:805	the four expected N-linked glycopeptides of LCAT	766:813	In addition to the four expected N-linked glycopeptides of LCAT, a di-O-linked glycopeptide was detected, as well as three additional glycopeptides.
7613477	7	58	gly	glycosylation	1594:1606	arg2	sites					1608:1612	potential N-linked glycosylation sites	1575:1612	potential N-linked glycosylation sites	1575:1612	The three additional glycopeptides were determined to be from a copurifying protein, apolipoprotein D, which contains potential N-linked glycosylation sites at Asn45 and Asn78.
7613477	0	59	gly	glycosylation	63:75	arg1	D					158:158	apolipoprotein D	143:158	apolipoprotein D	143:158	Site-specific detection and structural characterization of the glycosylation of human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D using HPLC/electrospray mass spectrometry and sequential glycosidase digestion.
7613477	0	59	gly	glycosylation	63:75	arg1	proteins					93:100	human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D	80:158	human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D	80:158	Site-specific detection and structural characterization of the glycosylation of human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D using HPLC/electrospray mass spectrometry and sequential glycosidase digestion.
7613477	0	59	gly	glycosylation	63:75	arg1	acyltransferase					123:137	lecithin:cholesterol acyltransferase	102:137	lecithin:cholesterol acyltransferase	102:137	Site-specific detection and structural characterization of the glycosylation of human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D using HPLC/electrospray mass spectrometry and sequential glycosidase digestion.
7613477	5	60	dep	triantennary	1199:1210	arg1	sialylated					1188:1197	sialylated	1188:1197	sialylated	1188:1197	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	0	61	theme	glycosidase	217:227	arg1	digestion					229:237	sequential glycosidase digestion	206:237	sequential glycosidase digestion	206:237	Site-specific detection and structural characterization of the glycosylation of human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D using HPLC/electrospray mass spectrometry and sequential glycosidase digestion.
7613477	1	62	theme	lecithin	312:319	arg1	glycosylation					289:301	the glycosylation	285:301	the glycosylation of human lecithin:cholesterol acyltransferase (LCAT)	285:354	Site-specific structural characterization of the glycosylation of human lecithin:cholesterol acyltransferase (LCAT) was carried out using microbore reversed-phase high performance liquid chromatography coupled with electrospray ionization mass spectrometry (HPLC/ESIMS).
7613477	5	63	link	N-linked	1089:1096	arg1	LCAT					1156:1159	LCAT	1156:1159	LCAT	1156:1159	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	63	link	N-linked	1089:1096	arg1	sites					1112:1116	All four potential N-linked glycosylation sites	1070:1116	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT	1070:1159	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	63	link	N-linked	1089:1096	arg1	Asn272					1133:1138	Asn272	1133:1138	Asn272	1133:1138	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	63	link	N-linked	1089:1096	arg1	Asn384					1145:1150	Asn384	1145:1150	Asn384	1145:1150	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	63	link	N-linked	1089:1096	arg1	Asn84					1126:1130	Asn84	1126:1130	Asn84	1126:1130	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	4	64	theme	sequential	992:1001	arg1	digestion					1015:1023	sequential glycosidase digestion	992:1023	sequential glycosidase digestion of the glycopeptides followed by HPLC/ESIMS	992:1067	Structural information on the oligosaccharides from all eight glycopeptides was obtained by sequential glycosidase digestion of the glycopeptides followed by HPLC/ESIMS.
7613477	3	65	theme	LCAT	810:813	arg1	glycopeptides					793:805	the four expected N-linked glycopeptides	766:805	the four expected N-linked glycopeptides of LCAT	766:813	In addition to the four expected N-linked glycopeptides of LCAT, a di-O-linked glycopeptide was detected, as well as three additional glycopeptides.
7613477	9	66	theme	site	1844:1847	arg1	removal					1815:1821	removal	1815:1821	removal of the glycosylation site at Asn272	1815:1857	Previous studies of LCAT indicated that removal of the glycosylation site at Asn272 converts this protein to a phospholipase (Francone OL, Evangelista L, Fielding CJ, 1993, Biochim Biophys Acta 1166:301-304).
7613477	1	67	theme	cholesterol	321:331	arg1	LCAT					350:353	LCAT	350:353	LCAT	350:353	Site-specific structural characterization of the glycosylation of human lecithin:cholesterol acyltransferase (LCAT) was carried out using microbore reversed-phase high performance liquid chromatography coupled with electrospray ionization mass spectrometry (HPLC/ESIMS).
7613477	1	67	theme	cholesterol	321:331	arg1	acyltransferase					333:347	cholesterol acyltransferase	321:347	human lecithin:cholesterol acyltransferase (LCAT)	306:354	Site-specific structural characterization of the glycosylation of human lecithin:cholesterol acyltransferase (LCAT) was carried out using microbore reversed-phase high performance liquid chromatography coupled with electrospray ionization mass spectrometry (HPLC/ESIMS).
7613477	3	68	link	di-O-linked	818:828	arg1	glycopeptide					830:841	a di-O-linked glycopeptide	816:841	a di-O-linked glycopeptide	816:841	In addition to the four expected N-linked glycopeptides of LCAT, a di-O-linked glycopeptide was detected, as well as three additional glycopeptides.
7613477	10	69	theme	structural	2138:2147	arg1	environment					2149:2159	the structural environment	2134:2159	the structural environment around Asn272	2134:2173	Our results indicate that the carbohydrate structures themselves are not the source of this functional discrimination; rather, it must be mediated by the structural environment around Asn272.
7613477	6	70	theme	1-->3N-acetylgalactosamine	1418:1443	arg1	structures					1445:1454	sialylated galactose beta 1-->3N-acetylgalactosamine structures	1392:1454	sialylated galactose beta 1-->3N-acetylgalactosamine structures	1392:1454	Two unanticipated O-linked glycosylation sites were identified at Thr407 and Ser409 of the LCAT O-linked glycopeptide, each of which contain sialylated galactose beta 1-->3N-acetylgalactosamine structures.
7613477	2	71	theme	preparation	738:748	arg1	digest					707:712	a digest	705:712	a digest of a human LCAT protein preparation	705:748	A recently described mass spectrometric technique involving monitoring of carbohydrate-specific fragment ions during HPLC/ESIMS was employed to locate eight different groups of glycopeptides in a digest of a human LCAT protein preparation.
7613477	6	72	theme	galactose	1403:1411	arg1	structures					1445:1454	sialylated galactose beta 1-->3N-acetylgalactosamine structures	1392:1454	sialylated galactose beta 1-->3N-acetylgalactosamine structures	1392:1454	Two unanticipated O-linked glycosylation sites were identified at Thr407 and Ser409 of the LCAT O-linked glycopeptide, each of which contain sialylated galactose beta 1-->3N-acetylgalactosamine structures.
7613477	8	73	gly	glycopeptides	1640:1652	arg2	glycopeptides					1640:1652	These glycopeptides	1634:1652	These glycopeptides	1634:1652	These glycopeptides were determined to bear sialylated triantennary oligosaccharides or fucosylated sialylated biantennary oligosaccharides.
7613477	9	74	gly	glycosylation	1830:1842	arg2	site					1844:1847	the glycosylation site	1826:1847	the glycosylation site	1826:1847	Previous studies of LCAT indicated that removal of the glycosylation site at Asn272 converts this protein to a phospholipase (Francone OL, Evangelista L, Fielding CJ, 1993, Biochim Biophys Acta 1166:301-304).
7613477	2	75	theme	LCAT	725:728	arg1	preparation					738:748	a human LCAT protein preparation	717:748	a human LCAT protein preparation	717:748	A recently described mass spectrometric technique involving monitoring of carbohydrate-specific fragment ions during HPLC/ESIMS was employed to locate eight different groups of glycopeptides in a digest of a human LCAT protein preparation.
7613477	0	76	theme	apolipoprotein	143:156	arg1	D					158:158	apolipoprotein D	143:158	apolipoprotein D	143:158	Site-specific detection and structural characterization of the glycosylation of human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D using HPLC/electrospray mass spectrometry and sequential glycosidase digestion.
7613477	0	76	theme	apolipoprotein	143:156	arg1	proteins					93:100	human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D	80:158	human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D	80:158	Site-specific detection and structural characterization of the glycosylation of human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D using HPLC/electrospray mass spectrometry and sequential glycosidase digestion.
7613477	1	77	theme	Site-specific	240:252	arg1	characterization					265:280	Site-specific structural characterization	240:280	Site-specific structural characterization of the glycosylation of human lecithin:cholesterol acyltransferase (LCAT)	240:354	Site-specific structural characterization of the glycosylation of human lecithin:cholesterol acyltransferase (LCAT) was carried out using microbore reversed-phase high performance liquid chromatography coupled with electrospray ionization mass spectrometry (HPLC/ESIMS).
7613477	2	78	theme	different	668:676	arg1	glycopeptides					688:700	glycopeptides	688:700	glycopeptides	688:700	A recently described mass spectrometric technique involving monitoring of carbohydrate-specific fragment ions during HPLC/ESIMS was employed to locate eight different groups of glycopeptides in a digest of a human LCAT protein preparation.
7613477	2	78	theme	different	668:676	arg1	groups					678:683	eight different groups	662:683	eight different groups of glycopeptides	662:700	A recently described mass spectrometric technique involving monitoring of carbohydrate-specific fragment ions during HPLC/ESIMS was employed to locate eight different groups of glycopeptides in a digest of a human LCAT protein preparation.
7613477	7	79	theme	N-linked	1585:1592	arg1	sites					1608:1612	potential N-linked glycosylation sites	1575:1612	potential N-linked glycosylation sites	1575:1612	The three additional glycopeptides were determined to be from a copurifying protein, apolipoprotein D, which contains potential N-linked glycosylation sites at Asn45 and Asn78.
7613477	1	80	theme	mass	479:482	arg1	spectrometry					484:495	electrospray ionization mass spectrometry	455:495	electrospray ionization mass spectrometry (HPLC/ESIMS)	455:508	Site-specific structural characterization of the glycosylation of human lecithin:cholesterol acyltransferase (LCAT) was carried out using microbore reversed-phase high performance liquid chromatography coupled with electrospray ionization mass spectrometry (HPLC/ESIMS).
7613477	1	80	theme	mass	479:482	arg1	HPLC/ESIMS					498:507	HPLC/ESIMS	498:507	HPLC/ESIMS	498:507	Site-specific structural characterization of the glycosylation of human lecithin:cholesterol acyltransferase (LCAT) was carried out using microbore reversed-phase high performance liquid chromatography coupled with electrospray ionization mass spectrometry (HPLC/ESIMS).
7613477	0	81	theme	mass	184:187	arg1	spectrometry					189:200	HPLC/electrospray mass spectrometry	166:200	HPLC/electrospray mass spectrometry	166:200	Site-specific detection and structural characterization of the glycosylation of human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D using HPLC/electrospray mass spectrometry and sequential glycosidase digestion.
7613477	5	82	theme	biantennary	1219:1229	arg1	structures					1239:1248	sialylated triantennary and/or biantennary complex structures	1188:1248	structures	1239:1248	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	3	83	theme	additional	874:883	arg1	glycopeptides					885:897	three additional glycopeptides	868:897	three additional glycopeptides	868:897	In addition to the four expected N-linked glycopeptides of LCAT, a di-O-linked glycopeptide was detected, as well as three additional glycopeptides.
7613477	6	84	gly	sialylated	1392:1401	arg1	structures					1445:1454	sialylated galactose beta 1-->3N-acetylgalactosamine structures	1392:1454	sialylated galactose beta 1-->3N-acetylgalactosamine structures	1392:1454	Two unanticipated O-linked glycosylation sites were identified at Thr407 and Ser409 of the LCAT O-linked glycopeptide, each of which contain sialylated galactose beta 1-->3N-acetylgalactosamine structures.
7613477	1	85	dep	lecithin	312:319	arg1	LCAT					350:353	LCAT	350:353	LCAT	350:353	Site-specific structural characterization of the glycosylation of human lecithin:cholesterol acyltransferase (LCAT) was carried out using microbore reversed-phase high performance liquid chromatography coupled with electrospray ionization mass spectrometry (HPLC/ESIMS).
7613477	1	85	dep	lecithin	312:319	arg1	acyltransferase					333:347	cholesterol acyltransferase	321:347	human lecithin:cholesterol acyltransferase (LCAT)	306:354	Site-specific structural characterization of the glycosylation of human lecithin:cholesterol acyltransferase (LCAT) was carried out using microbore reversed-phase high performance liquid chromatography coupled with electrospray ionization mass spectrometry (HPLC/ESIMS).
7613477	7	86	theme	apolipoprotein	1542:1555	arg1	protein					1533:1539	a copurifying protein	1519:1539	a copurifying protein	1519:1539	The three additional glycopeptides were determined to be from a copurifying protein, apolipoprotein D, which contains potential N-linked glycosylation sites at Asn45 and Asn78.
7613477	7	86	theme	apolipoprotein	1542:1555	arg1	D					1557:1557	apolipoprotein D	1542:1557	apolipoprotein D	1542:1557	The three additional glycopeptides were determined to be from a copurifying protein, apolipoprotein D, which contains potential N-linked glycosylation sites at Asn45 and Asn78.
7613477	0	87	theme	human	80:84	arg1	D					158:158	apolipoprotein D	143:158	apolipoprotein D	143:158	Site-specific detection and structural characterization of the glycosylation of human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D using HPLC/electrospray mass spectrometry and sequential glycosidase digestion.
7613477	0	87	theme	human	80:84	arg1	proteins					93:100	human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D	80:158	human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D	80:158	Site-specific detection and structural characterization of the glycosylation of human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D using HPLC/electrospray mass spectrometry and sequential glycosidase digestion.
7613477	0	87	theme	human	80:84	arg1	acyltransferase					123:137	lecithin:cholesterol acyltransferase	102:137	lecithin:cholesterol acyltransferase	102:137	Site-specific detection and structural characterization of the glycosylation of human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D using HPLC/electrospray mass spectrometry and sequential glycosidase digestion.
7613477	4	88	gly	glycopeptides	962:974	arg2	glycopeptides					962:974	all eight glycopeptides	952:974	all eight glycopeptides	952:974	Structural information on the oligosaccharides from all eight glycopeptides was obtained by sequential glycosidase digestion of the glycopeptides followed by HPLC/ESIMS.
7613477	8	89	gly	sialylated	1734:1743	arg1	oligosaccharides					1757:1772	fucosylated sialylated biantennary oligosaccharides	1722:1772	fucosylated sialylated biantennary oligosaccharides	1722:1772	These glycopeptides were determined to bear sialylated triantennary oligosaccharides or fucosylated sialylated biantennary oligosaccharides.
7613477	2	90	theme	ions	616:619	arg1	monitoring					571:580	monitoring	571:580	monitoring of carbohydrate-specific fragment ions during HPLC/ESIMS	571:637	A recently described mass spectrometric technique involving monitoring of carbohydrate-specific fragment ions during HPLC/ESIMS was employed to locate eight different groups of glycopeptides in a digest of a human LCAT protein preparation.
7613477	6	91	theme	LCAT	1342:1345	arg1	glycopeptide					1356:1367	the LCAT O-linked glycopeptide	1338:1367	the LCAT O-linked glycopeptide	1338:1367	Two unanticipated O-linked glycosylation sites were identified at Thr407 and Ser409 of the LCAT O-linked glycopeptide, each of which contain sialylated galactose beta 1-->3N-acetylgalactosamine structures.
7613477	5	92	dep	sites	1112:1116	arg1	LCAT					1156:1159	LCAT	1156:1159	LCAT	1156:1159	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	92	dep	sites	1112:1116	arg1	sites					1112:1116	All four potential N-linked glycosylation sites	1070:1116	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT	1070:1159	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	92	dep	sites	1112:1116	arg1	Asn272					1133:1138	Asn272	1133:1138	Asn272	1133:1138	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	92	dep	sites	1112:1116	arg1	Asn384					1145:1150	Asn384	1145:1150	Asn384	1145:1150	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	92	dep	sites	1112:1116	arg1	Asn84					1126:1130	Asn84	1126:1130	Asn84	1126:1130	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	0	93	theme	proteins	93:100	arg1	glycosylation					63:75	the glycosylation	59:75	the glycosylation of human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D	59:158	Site-specific detection and structural characterization of the glycosylation of human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D using HPLC/electrospray mass spectrometry and sequential glycosidase digestion.
7613477	1	94	theme	high	403:406	arg1	chromatography					427:440	microbore reversed-phase high performance liquid chromatography	378:440	microbore reversed-phase high performance liquid chromatography coupled with electrospray ionization mass spectrometry (HPLC/ESIMS)	378:508	Site-specific structural characterization of the glycosylation of human lecithin:cholesterol acyltransferase (LCAT) was carried out using microbore reversed-phase high performance liquid chromatography coupled with electrospray ionization mass spectrometry (HPLC/ESIMS).
7613477	2	95	theme	carbohydrate-specific	585:605	arg1	ions					616:619	carbohydrate-specific fragment ions	585:619	carbohydrate-specific fragment ions	585:619	A recently described mass spectrometric technique involving monitoring of carbohydrate-specific fragment ions during HPLC/ESIMS was employed to locate eight different groups of glycopeptides in a digest of a human LCAT protein preparation.
7613477	8	96	theme	fucosylated	1722:1732	arg1	oligosaccharides					1757:1772	fucosylated sialylated biantennary oligosaccharides	1722:1772	fucosylated sialylated biantennary oligosaccharides	1722:1772	These glycopeptides were determined to bear sialylated triantennary oligosaccharides or fucosylated sialylated biantennary oligosaccharides.
7613477	1	97	theme	liquid	420:425	arg1	chromatography					427:440	microbore reversed-phase high performance liquid chromatography	378:440	microbore reversed-phase high performance liquid chromatography coupled with electrospray ionization mass spectrometry (HPLC/ESIMS)	378:508	Site-specific structural characterization of the glycosylation of human lecithin:cholesterol acyltransferase (LCAT) was carried out using microbore reversed-phase high performance liquid chromatography coupled with electrospray ionization mass spectrometry (HPLC/ESIMS).
7613477	7	98	gly	glycopeptides	1478:1490	arg2	glycopeptides					1478:1490	The three additional glycopeptides	1457:1490	The three additional glycopeptides	1457:1490	The three additional glycopeptides were determined to be from a copurifying protein, apolipoprotein D, which contains potential N-linked glycosylation sites at Asn45 and Asn78.
7613477	9	99	theme	Previous	1775:1782	arg1	studies					1784:1790	Previous studies	1775:1790	Previous studies of LCAT	1775:1798	Previous studies of LCAT indicated that removal of the glycosylation site at Asn272 converts this protein to a phospholipase (Francone OL, Evangelista L, Fielding CJ, 1993, Biochim Biophys Acta 1166:301-304).
7613477	8	100	theme	biantennary	1745:1755	arg1	oligosaccharides					1757:1772	fucosylated sialylated biantennary oligosaccharides	1722:1772	fucosylated sialylated biantennary oligosaccharides	1722:1772	These glycopeptides were determined to bear sialylated triantennary oligosaccharides or fucosylated sialylated biantennary oligosaccharides.
7613477	5	101	gly	glycosylation	1098:1110	arg2	LCAT					1156:1159	LCAT	1156:1159	LCAT	1156:1159	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	101	gly	glycosylation	1098:1110	arg2	sites					1112:1116	All four potential N-linked glycosylation sites	1070:1116	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT	1070:1159	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	101	gly	glycosylation	1098:1110	arg2	Asn272					1133:1138	Asn272	1133:1138	Asn272	1133:1138	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	101	gly	glycosylation	1098:1110	arg2	four					1074:1077	four	1074:1077	four	1074:1077	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	101	gly	glycosylation	1098:1110	arg1	LCAT					1156:1159	LCAT	1156:1159	LCAT	1156:1159	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	101	gly	glycosylation	1098:1110	arg2	Asn84					1126:1130	Asn84	1126:1130	Asn84	1126:1130	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	101	gly	glycosylation	1098:1110	arg2	Asn384					1145:1150	Asn384	1145:1150	Asn384	1145:1150	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	9	102	dep	phospholipase	1886:1898	arg1	L					1926:1926	Evangelista L	1914:1926	Evangelista L	1914:1926	Previous studies of LCAT indicated that removal of the glycosylation site at Asn272 converts this protein to a phospholipase (Francone OL, Evangelista L, Fielding CJ, 1993, Biochim Biophys Acta 1166:301-304).
7613477	9	102	dep	phospholipase	1886:1898	arg1	CJ					1938:1939	CJ	1938:1939	CJ	1938:1939	Previous studies of LCAT indicated that removal of the glycosylation site at Asn272 converts this protein to a phospholipase (Francone OL, Evangelista L, Fielding CJ, 1993, Biochim Biophys Acta 1166:301-304).
7613477	9	102	dep	phospholipase	1886:1898	arg1	Acta					1964:1967	Acta	1964:1967	Acta	1964:1967	Previous studies of LCAT indicated that removal of the glycosylation site at Asn272 converts this protein to a phospholipase (Francone OL, Evangelista L, Fielding CJ, 1993, Biochim Biophys Acta 1166:301-304).
7613477	9	102	dep	phospholipase	1886:1898	arg1	Francone					1901:1908	Francone	1901:1908	Francone	1901:1908	Previous studies of LCAT indicated that removal of the glycosylation site at Asn272 converts this protein to a phospholipase (Francone OL, Evangelista L, Fielding CJ, 1993, Biochim Biophys Acta 1166:301-304).
7613477	4	103	from	glycopeptides	962:974	arg1	oligosaccharides					930:945	the oligosaccharides	926:945	the oligosaccharides from all eight glycopeptides	926:974	Structural information on the oligosaccharides from all eight glycopeptides was obtained by sequential glycosidase digestion of the glycopeptides followed by HPLC/ESIMS.
7613477	5	104	theme	potential	1079:1087	arg1	LCAT					1156:1159	LCAT	1156:1159	LCAT	1156:1159	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	104	theme	potential	1079:1087	arg1	sites					1112:1116	All four potential N-linked glycosylation sites	1070:1116	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT	1070:1159	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	104	theme	potential	1079:1087	arg1	Asn272					1133:1138	Asn272	1133:1138	Asn272	1133:1138	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	104	theme	potential	1079:1087	arg1	Asn384					1145:1150	Asn384	1145:1150	Asn384	1145:1150	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	104	theme	potential	1079:1087	arg1	Asn84					1126:1130	Asn84	1126:1130	Asn84	1126:1130	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	2	105	theme	mass	532:535	arg1	technique					551:559	A recently described mass spectrometric technique	511:559	A recently described mass spectrometric technique involving monitoring of carbohydrate-specific fragment ions during HPLC/ESIMS	511:637	A recently described mass spectrometric technique involving monitoring of carbohydrate-specific fragment ions during HPLC/ESIMS was employed to locate eight different groups of glycopeptides in a digest of a human LCAT protein preparation.
7613477	10	106	theme	discrimination	2087:2100	arg1	source					2061:2066	the source	2057:2066	the source of this functional discrimination	2057:2100	Our results indicate that the carbohydrate structures themselves are not the source of this functional discrimination; rather, it must be mediated by the structural environment around Asn272.
7613477	10	106	theme	discrimination	2087:2100	arg1	structures					2027:2036	the carbohydrate structures	2010:2036	the carbohydrate structures themselves	2010:2047	Our results indicate that the carbohydrate structures themselves are not the source of this functional discrimination; rather, it must be mediated by the structural environment around Asn272.
7613477	0	107	theme	structural	28:37	arg1	characterization					39:54	structural characterization	28:54	structural characterization	28:54	Site-specific detection and structural characterization of the glycosylation of human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D using HPLC/electrospray mass spectrometry and sequential glycosidase digestion.
7613477	5	108	theme	glycosylation	1098:1110	arg1	LCAT					1156:1159	LCAT	1156:1159	LCAT	1156:1159	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	108	theme	glycosylation	1098:1110	arg1	sites					1112:1116	All four potential N-linked glycosylation sites	1070:1116	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT	1070:1159	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	108	theme	glycosylation	1098:1110	arg1	Asn272					1133:1138	Asn272	1133:1138	Asn272	1133:1138	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	108	theme	glycosylation	1098:1110	arg1	Asn384					1145:1150	Asn384	1145:1150	Asn384	1145:1150	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	5	108	theme	glycosylation	1098:1110	arg1	Asn84					1126:1130	Asn84	1126:1130	Asn84	1126:1130	All four potential N-linked glycosylation sites (Asn20, Asn84, Asn272, and Asn384) of LCAT were determined to contain sialylated triantennary and/or biantennary complex structures.
7613477	3	109	gly	glycopeptide	830:841	arg2	glycopeptide					830:841	a di-O-linked glycopeptide	816:841	a di-O-linked glycopeptide	816:841	In addition to the four expected N-linked glycopeptides of LCAT, a di-O-linked glycopeptide was detected, as well as three additional glycopeptides.
7613477	6	110	link	O-linked	1269:1276	arg1	sites					1292:1296	Two unanticipated O-linked glycosylation sites	1251:1296	Two unanticipated O-linked glycosylation sites	1251:1296	Two unanticipated O-linked glycosylation sites were identified at Thr407 and Ser409 of the LCAT O-linked glycopeptide, each of which contain sialylated galactose beta 1-->3N-acetylgalactosamine structures.
7613477	7	111	theme	additional	1467:1476	arg1	glycopeptides					1478:1490	The three additional glycopeptides	1457:1490	The three additional glycopeptides	1457:1490	The three additional glycopeptides were determined to be from a copurifying protein, apolipoprotein D, which contains potential N-linked glycosylation sites at Asn45 and Asn78.
7613477	0	112	theme	glycosylation	63:75	arg1	detection					14:22	Site-specific detection	0:22	Site-specific detection	0:22	Site-specific detection and structural characterization of the glycosylation of human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D using HPLC/electrospray mass spectrometry and sequential glycosidase digestion.
7613477	0	112	theme	glycosylation	63:75	arg1	characterization					39:54	structural characterization	28:54	structural characterization	28:54	Site-specific detection and structural characterization of the glycosylation of human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D using HPLC/electrospray mass spectrometry and sequential glycosidase digestion.
7613477	8	113	theme	triantennary	1689:1700	arg1	oligosaccharides					1702:1717	sialylated triantennary oligosaccharides	1678:1717	sialylated triantennary oligosaccharides	1678:1717	These glycopeptides were determined to bear sialylated triantennary oligosaccharides or fucosylated sialylated biantennary oligosaccharides.
7613477	3	114	theme	N-linked	784:791	arg1	glycopeptides					793:805	the four expected N-linked glycopeptides	766:805	the four expected N-linked glycopeptides of LCAT	766:813	In addition to the four expected N-linked glycopeptides of LCAT, a di-O-linked glycopeptide was detected, as well as three additional glycopeptides.
7613477	1	115	theme	microbore	378:386	arg1	chromatography					427:440	microbore reversed-phase high performance liquid chromatography	378:440	microbore reversed-phase high performance liquid chromatography coupled with electrospray ionization mass spectrometry (HPLC/ESIMS)	378:508	Site-specific structural characterization of the glycosylation of human lecithin:cholesterol acyltransferase (LCAT) was carried out using microbore reversed-phase high performance liquid chromatography coupled with electrospray ionization mass spectrometry (HPLC/ESIMS).
7613477	6	116	theme	O-linked	1269:1276	arg1	sites					1292:1296	Two unanticipated O-linked glycosylation sites	1251:1296	Two unanticipated O-linked glycosylation sites	1251:1296	Two unanticipated O-linked glycosylation sites were identified at Thr407 and Ser409 of the LCAT O-linked glycopeptide, each of which contain sialylated galactose beta 1-->3N-acetylgalactosamine structures.
7613477	3	117	gly	glycopeptides	793:805	arg2	glycopeptides					793:805	the four expected N-linked glycopeptides	766:805	the four expected N-linked glycopeptides of LCAT	766:813	In addition to the four expected N-linked glycopeptides of LCAT, a di-O-linked glycopeptide was detected, as well as three additional glycopeptides.
7613477	3	117	gly	glycopeptides	793:805	arg1	LCAT					810:813	LCAT	810:813	LCAT	810:813	In addition to the four expected N-linked glycopeptides of LCAT, a di-O-linked glycopeptide was detected, as well as three additional glycopeptides.
7613477	4	118	theme	Structural	900:909	arg1	information					911:921	Structural information	900:921	Structural information on the oligosaccharides from all eight glycopeptides	900:974	Structural information on the oligosaccharides from all eight glycopeptides was obtained by sequential glycosidase digestion of the glycopeptides followed by HPLC/ESIMS.
7613477	1	119	theme	glycosylation	289:301	arg1	characterization					265:280	Site-specific structural characterization	240:280	Site-specific structural characterization of the glycosylation of human lecithin:cholesterol acyltransferase (LCAT)	240:354	Site-specific structural characterization of the glycosylation of human lecithin:cholesterol acyltransferase (LCAT) was carried out using microbore reversed-phase high performance liquid chromatography coupled with electrospray ionization mass spectrometry (HPLC/ESIMS).
7613477	1	120	theme	human	306:310	arg1	lecithin					312:319	human lecithin	306:319	human lecithin:cholesterol acyltransferase (LCAT)	306:354	Site-specific structural characterization of the glycosylation of human lecithin:cholesterol acyltransferase (LCAT) was carried out using microbore reversed-phase high performance liquid chromatography coupled with electrospray ionization mass spectrometry (HPLC/ESIMS).
1456441	6	0	theme	affinity	936:943	arg1	chromatography					945:958	the corresponding lectin affinity chromatography	911:958	the corresponding lectin affinity chromatography	911:958	The other part was used to isolate the oligosaccharide by the corresponding lectin affinity chromatography and to characterize the structures of the isolated oligosaccharides by 1H NMR spectroscopy and FAB-MS.
1456441	7	1	theme	-sialyl	1146:1152	arg1	structures					1167:1176	bi-alpha(2-->6)-sialyl, diantennary structures	1131:1176	bi-alpha(2-->6)-sialyl, diantennary structures	1131:1176	The oligosaccharides in the Con A-bound fraction were shown to have bi-alpha(2-->6)-sialyl, diantennary structures.
1456441	3	2	theme	LPHA	517:520	arg1	chromatography					532:545	Phaseolus vulgaris leukoagglutinin (LPHA) affinity chromatography	481:545	Phaseolus vulgaris leukoagglutinin (LPHA) affinity chromatography	481:545	Glycopeptides in the proteolytic digests were isolated by serial concanavalin A (Con A), Sambucus nigra agglutinin (SNA), and Phaseolus vulgaris leukoagglutinin (LPHA) affinity chromatography and subjected to preliminary analysis by 1H NMR spectroscopy.
1456441	8	3	theme	SNA-bound	1183:1191	arg1	fraction					1193:1200	The SNA-bound fraction	1179:1200	The SNA-bound fraction	1179:1200	The SNA-bound fraction was shown to contain trisialyl, triantennary structures.
1456441	6	4	theme	corresponding	915:927	arg1	chromatography					945:958	the corresponding lectin affinity chromatography	911:958	the corresponding lectin affinity chromatography	911:958	The other part was used to isolate the oligosaccharide by the corresponding lectin affinity chromatography and to characterize the structures of the isolated oligosaccharides by 1H NMR spectroscopy and FAB-MS.
1456441	12	5	attach	attached	1707:1714	arg2	oligosaccharides					1690:1705	2,4-triantennary vs 2,6-triantennary oligosaccharides	1653:1705	2,4-triantennary vs 2,6-triantennary oligosaccharides attached to glycosylation site Asn413	1653:1743	The ratio of 2,4-triantennary vs 2,6-triantennary oligosaccharides attached to glycosylation site Asn413 was found to be approximately 5:1, whereas the two isomeric triantennary oligosaccharides were found to be attached to glycosylation site Asn611 in the ratio approximately 1:1.
1456441	12	5	attach	attached	1707:1714	arg1	site					1733:1736	glycosylation site Asn413	1719:1743	glycosylation site Asn413	1719:1743	The ratio of 2,4-triantennary vs 2,6-triantennary oligosaccharides attached to glycosylation site Asn413 was found to be approximately 5:1, whereas the two isomeric triantennary oligosaccharides were found to be attached to glycosylation site Asn611 in the ratio approximately 1:1.
1456441	1	6	gly	N-glycosylation	211:225	arg2	site					227:230	N-glycosylation site	211:230	the N-glycosylation site mapping of human serotransferrin (h-STF)	207:271	This report describes the N-glycosylation site mapping of human serotransferrin (h-STF).
1456441	11	7	theme	2,6-triantennary	1615:1630	arg1	glycan					1632:1637	a trisialyl 2,6-triantennary glycan	1603:1637	a trisialyl 2,6-triantennary glycan	1603:1637	Two different oligosaccharides were characterized, namely, a trisialyl 2,4-triantennary and a trisialyl 2,6-triantennary glycan.
1456441	2	8	theme	S-carboxymethylated	286:304	arg1	h-STF					306:310	Reduced and S-carboxymethylated h-STF	274:310	Reduced and S-carboxymethylated h-STF	274:310	Reduced and S-carboxymethylated h-STF was digested with trypsin or chymotrypsin.
1456441	9	9	from	sites	1352:1356	arg1	ratio					1394:1398	the ratio	1390:1398	the ratio of approximately 85:15	1390:1421	Di- and triantennary oligosaccharides were found to occur on each of the two N-glycosylation sites of h-STF (Asn413 and Asn611) in the ratio of approximately 85:15.
1456441	12	10	theme	triantennary	1805:1816	arg1	oligosaccharides					1818:1833	the two isomeric triantennary oligosaccharides	1788:1833	the two isomeric triantennary oligosaccharides	1788:1833	The ratio of 2,4-triantennary vs 2,6-triantennary oligosaccharides attached to glycosylation site Asn413 was found to be approximately 5:1, whereas the two isomeric triantennary oligosaccharides were found to be attached to glycosylation site Asn611 in the ratio approximately 1:1.
1456441	0	11	theme	magnetic	152:159	arg1	resonance					161:169	1H nuclear magnetic resonance	141:169	1H nuclear magnetic resonance spectroscopy	141:182	N-glycosylation site mapping of human serotransferrin by serial lectin affinity chromatography, fast atom bombardment-mass spectrometry, and 1H nuclear magnetic resonance spectroscopy.
1456441	3	12	theme	1H	588:589	arg1	spectroscopy					595:606	1H NMR spectroscopy	588:606	1H NMR spectroscopy	588:606	Glycopeptides in the proteolytic digests were isolated by serial concanavalin A (Con A), Sambucus nigra agglutinin (SNA), and Phaseolus vulgaris leukoagglutinin (LPHA) affinity chromatography and subjected to preliminary analysis by 1H NMR spectroscopy.
1456441	8	13	theme	trisialyl	1223:1231	arg1	structures					1247:1256	trisialyl, triantennary structures	1223:1256	trisialyl, triantennary structures	1223:1256	The SNA-bound fraction was shown to contain trisialyl, triantennary structures.
1456441	12	14	theme	2,4-triantennary	1653:1668	arg1	oligosaccharides					1690:1705	2,4-triantennary vs 2,6-triantennary oligosaccharides	1653:1705	2,4-triantennary vs 2,6-triantennary oligosaccharides attached to glycosylation site Asn413	1653:1743	The ratio of 2,4-triantennary vs 2,6-triantennary oligosaccharides attached to glycosylation site Asn413 was found to be approximately 5:1, whereas the two isomeric triantennary oligosaccharides were found to be attached to glycosylation site Asn611 in the ratio approximately 1:1.
1456441	7	15	dep	-sialyl	1146:1152	arg1	diantennary					1155:1165	diantennary	1155:1165	diantennary	1155:1165	The oligosaccharides in the Con A-bound fraction were shown to have bi-alpha(2-->6)-sialyl, diantennary structures.
1456441	1	16	theme	site	227:230	arg1	mapping					232:238	the N-glycosylation site mapping	207:238	the N-glycosylation site mapping of human serotransferrin (h-STF)	207:271	This report describes the N-glycosylation site mapping of human serotransferrin (h-STF).
1456441	12	17	theme	2,6-triantennary	1673:1688	arg1	oligosaccharides					1690:1705	2,4-triantennary vs 2,6-triantennary oligosaccharides	1653:1705	2,4-triantennary vs 2,6-triantennary oligosaccharides attached to glycosylation site Asn413	1653:1743	The ratio of 2,4-triantennary vs 2,6-triantennary oligosaccharides attached to glycosylation site Asn413 was found to be approximately 5:1, whereas the two isomeric triantennary oligosaccharides were found to be attached to glycosylation site Asn611 in the ratio approximately 1:1.
1456441	7	18	theme	A-bound	1095:1101	arg1	fraction					1103:1110	the Con A-bound fraction	1087:1110	the Con A-bound fraction	1087:1110	The oligosaccharides in the Con A-bound fraction were shown to have bi-alpha(2-->6)-sialyl, diantennary structures.
1456441	9	19	theme	triantennary	1267:1278	arg1	oligosaccharides					1280:1295	triantennary oligosaccharides	1267:1295	triantennary oligosaccharides	1267:1295	Di- and triantennary oligosaccharides were found to occur on each of the two N-glycosylation sites of h-STF (Asn413 and Asn611) in the ratio of approximately 85:15.
1456441	5	20	theme	digest	702:707	arg1	part					690:693	One part	686:693	One part of the digest of each fraction	686:724	One part of the digest of each fraction was analyzed by fast atom bombardment-mass spectrometry (FAB-MS) to identify the peptide sequences of the glycosylation sites.
1456441	2	21	theme	Reduced	274:280	arg1	h-STF					306:310	Reduced and S-carboxymethylated h-STF	274:310	Reduced and S-carboxymethylated h-STF	274:310	Reduced and S-carboxymethylated h-STF was digested with trypsin or chymotrypsin.
1456441	12	22	theme	isomeric	1796:1803	arg1	oligosaccharides					1818:1833	the two isomeric triantennary oligosaccharides	1788:1833	the two isomeric triantennary oligosaccharides	1788:1833	The ratio of 2,4-triantennary vs 2,6-triantennary oligosaccharides attached to glycosylation site Asn413 was found to be approximately 5:1, whereas the two isomeric triantennary oligosaccharides were found to be attached to glycosylation site Asn611 in the ratio approximately 1:1.
1456441	9	23	gly	N-glycosylation	1336:1350	arg2	ratio					1394:1398	the ratio	1390:1398	the ratio of approximately 85:15	1390:1421	Di- and triantennary oligosaccharides were found to occur on each of the two N-glycosylation sites of h-STF (Asn413 and Asn611) in the ratio of approximately 85:15.
1456441	9	23	gly	N-glycosylation	1336:1350	arg1	h-STF					1361:1365	h-STF	1361:1365	h-STF (Asn413 and Asn611) in the ratio of approximately 85:15	1361:1421	Di- and triantennary oligosaccharides were found to occur on each of the two N-glycosylation sites of h-STF (Asn413 and Asn611) in the ratio of approximately 85:15.
1456441	9	23	gly	N-glycosylation	1336:1350	arg2	sites					1352:1356	the two N-glycosylation sites	1328:1356	the two N-glycosylation sites of h-STF (Asn413 and Asn611) in the ratio of approximately 85:15	1328:1421	Di- and triantennary oligosaccharides were found to occur on each of the two N-glycosylation sites of h-STF (Asn413 and Asn611) in the ratio of approximately 85:15.
1456441	9	23	gly	N-glycosylation	1336:1350	arg2	two					1332:1334	two	1332:1334	two	1332:1334	Di- and triantennary oligosaccharides were found to occur on each of the two N-glycosylation sites of h-STF (Asn413 and Asn611) in the ratio of approximately 85:15.
1456441	9	23	gly	N-glycosylation	1336:1350	arg2	h-STF					1361:1365	h-STF	1361:1365	h-STF (Asn413 and Asn611) in the ratio of approximately 85:15	1361:1421	Di- and triantennary oligosaccharides were found to occur on each of the two N-glycosylation sites of h-STF (Asn413 and Asn611) in the ratio of approximately 85:15.
1456441	11	24	theme	different	1515:1523	arg1	oligosaccharides					1525:1540	Two different oligosaccharides	1511:1540	Two different oligosaccharides	1511:1540	Two different oligosaccharides were characterized, namely, a trisialyl 2,4-triantennary and a trisialyl 2,6-triantennary glycan.
1456441	12	25	attach	attached	1852:1859	arg1	site					1878:1881	glycosylation site Asn611	1864:1888	glycosylation site Asn611	1864:1888	The ratio of 2,4-triantennary vs 2,6-triantennary oligosaccharides attached to glycosylation site Asn413 was found to be approximately 5:1, whereas the two isomeric triantennary oligosaccharides were found to be attached to glycosylation site Asn611 in the ratio approximately 1:1.
1456441	12	25	attach	attached	1852:1859	arg2	oligosaccharides					1818:1833	the two isomeric triantennary oligosaccharides	1788:1833	the two isomeric triantennary oligosaccharides	1788:1833	The ratio of 2,4-triantennary vs 2,6-triantennary oligosaccharides attached to glycosylation site Asn413 was found to be approximately 5:1, whereas the two isomeric triantennary oligosaccharides were found to be attached to glycosylation site Asn611 in the ratio approximately 1:1.
1456441	12	25	attach	attached	1852:1859	arg3	ratio					1897:1901	the ratio	1893:1901	the ratio approximately 1:1	1893:1919	The ratio of 2,4-triantennary vs 2,6-triantennary oligosaccharides attached to glycosylation site Asn413 was found to be approximately 5:1, whereas the two isomeric triantennary oligosaccharides were found to be attached to glycosylation site Asn611 in the ratio approximately 1:1.
1456441	0	26	theme	lectin	64:69	arg1	chromatography					80:93	serial lectin affinity chromatography	57:93	serial lectin affinity chromatography	57:93	N-glycosylation site mapping of human serotransferrin by serial lectin affinity chromatography, fast atom bombardment-mass spectrometry, and 1H nuclear magnetic resonance spectroscopy.
1456441	4	27	gly	glycopeptide	613:624	arg2	glycopeptide					613:624	glycopeptide	613:624	glycopeptide	613:624	The glycopeptide fractions were then individually digested with N-glycanase.
1456441	6	28	theme	1H	1031:1032	arg1	spectroscopy					1038:1049	1H NMR spectroscopy	1031:1049	1H NMR spectroscopy	1031:1049	The other part was used to isolate the oligosaccharide by the corresponding lectin affinity chromatography and to characterize the structures of the isolated oligosaccharides by 1H NMR spectroscopy and FAB-MS.
1456441	0	29	theme	nuclear	144:150	arg1	resonance					161:169	1H nuclear magnetic resonance	141:169	1H nuclear magnetic resonance spectroscopy	141:182	N-glycosylation site mapping of human serotransferrin by serial lectin affinity chromatography, fast atom bombardment-mass spectrometry, and 1H nuclear magnetic resonance spectroscopy.
1456441	0	30	theme	fast	96:99	arg1	spectrometry					123:134	fast atom bombardment-mass spectrometry	96:134	fast atom bombardment-mass spectrometry	96:134	N-glycosylation site mapping of human serotransferrin by serial lectin affinity chromatography, fast atom bombardment-mass spectrometry, and 1H nuclear magnetic resonance spectroscopy.
1456441	6	31	theme	oligosaccharides	1011:1026	arg1	structures					984:993	the structures	980:993	the structures of the isolated oligosaccharides	980:1026	The other part was used to isolate the oligosaccharide by the corresponding lectin affinity chromatography and to characterize the structures of the isolated oligosaccharides by 1H NMR spectroscopy and FAB-MS.
1456441	3	32	theme	proteolytic	376:386	arg1	digests					388:394	the proteolytic digests	372:394	the proteolytic digests	372:394	Glycopeptides in the proteolytic digests were isolated by serial concanavalin A (Con A), Sambucus nigra agglutinin (SNA), and Phaseolus vulgaris leukoagglutinin (LPHA) affinity chromatography and subjected to preliminary analysis by 1H NMR spectroscopy.
1456441	3	33	theme	nigra	453:457	arg1	SNA					471:473	SNA	471:473	SNA	471:473	Glycopeptides in the proteolytic digests were isolated by serial concanavalin A (Con A), Sambucus nigra agglutinin (SNA), and Phaseolus vulgaris leukoagglutinin (LPHA) affinity chromatography and subjected to preliminary analysis by 1H NMR spectroscopy.
1456441	3	33	theme	nigra	453:457	arg1	agglutinin					459:468	Sambucus nigra agglutinin	444:468	Sambucus nigra agglutinin (SNA)	444:474	Glycopeptides in the proteolytic digests were isolated by serial concanavalin A (Con A), Sambucus nigra agglutinin (SNA), and Phaseolus vulgaris leukoagglutinin (LPHA) affinity chromatography and subjected to preliminary analysis by 1H NMR spectroscopy.
1456441	0	34	theme	bombardment-mass	106:121	arg1	spectrometry					123:134	fast atom bombardment-mass spectrometry	96:134	fast atom bombardment-mass spectrometry	96:134	N-glycosylation site mapping of human serotransferrin by serial lectin affinity chromatography, fast atom bombardment-mass spectrometry, and 1H nuclear magnetic resonance spectroscopy.
1456441	3	35	theme	concanavalin	420:431	arg1	A					433:433	serial concanavalin A	413:433	serial concanavalin A (Con A)	413:441	Glycopeptides in the proteolytic digests were isolated by serial concanavalin A (Con A), Sambucus nigra agglutinin (SNA), and Phaseolus vulgaris leukoagglutinin (LPHA) affinity chromatography and subjected to preliminary analysis by 1H NMR spectroscopy.
1456441	3	35	theme	concanavalin	420:431	arg1	A					440:440	Con A	436:440	Con A	436:440	Glycopeptides in the proteolytic digests were isolated by serial concanavalin A (Con A), Sambucus nigra agglutinin (SNA), and Phaseolus vulgaris leukoagglutinin (LPHA) affinity chromatography and subjected to preliminary analysis by 1H NMR spectroscopy.
1456441	10	36	theme	affinity	1486:1493	arg1	chromatography					1495:1508	LPHA affinity chromatography	1481:1508	LPHA affinity chromatography	1481:1508	The SNA-bound glycopeptides were further fractionated by LPHA affinity chromatography.
1456441	0	37	theme	N-glycosylation	0:14	arg1	mapping					21:27	N-glycosylation site mapping	0:27	N-glycosylation site mapping of human serotransferrin by serial lectin affinity chromatography, fast atom bombardment-mass spectrometry, and 1H nuclear magnetic resonance spectroscopy	0:182	N-glycosylation site mapping of human serotransferrin by serial lectin affinity chromatography, fast atom bombardment-mass spectrometry, and 1H nuclear magnetic resonance spectroscopy.
1456441	9	38	theme	h-STF	1361:1365	arg1	h-STF					1361:1365	h-STF	1361:1365	h-STF (Asn413 and Asn611) in the ratio of approximately 85:15	1361:1421	Di- and triantennary oligosaccharides were found to occur on each of the two N-glycosylation sites of h-STF (Asn413 and Asn611) in the ratio of approximately 85:15.
1456441	9	38	theme	h-STF	1361:1365	arg1	sites					1352:1356	the two N-glycosylation sites	1328:1356	the two N-glycosylation sites of h-STF (Asn413 and Asn611) in the ratio of approximately 85:15	1328:1421	Di- and triantennary oligosaccharides were found to occur on each of the two N-glycosylation sites of h-STF (Asn413 and Asn611) in the ratio of approximately 85:15.
1456441	5	39	theme	sites	846:850	arg1	sequences					815:823	the peptide sequences	803:823	the peptide sequences of the glycosylation sites	803:850	One part of the digest of each fraction was analyzed by fast atom bombardment-mass spectrometry (FAB-MS) to identify the peptide sequences of the glycosylation sites.
1456441	7	40	contain	have	1126:1129	arg1	oligosaccharides					1067:1082	The oligosaccharides	1063:1082	The oligosaccharides in the Con A-bound fraction	1063:1110	The oligosaccharides in the Con A-bound fraction were shown to have bi-alpha(2-->6)-sialyl, diantennary structures.
1456441	7	40	contain	have	1126:1129	arg2	structures					1167:1176	bi-alpha(2-->6)-sialyl, diantennary structures	1131:1176	bi-alpha(2-->6)-sialyl, diantennary structures	1131:1176	The oligosaccharides in the Con A-bound fraction were shown to have bi-alpha(2-->6)-sialyl, diantennary structures.
1456441	0	41	theme	human	32:36	arg1	serotransferrin					38:52	human serotransferrin	32:52	human serotransferrin	32:52	N-glycosylation site mapping of human serotransferrin by serial lectin affinity chromatography, fast atom bombardment-mass spectrometry, and 1H nuclear magnetic resonance spectroscopy.
1456441	6	42	used	used	872:875	arg2	part					863:866	The other part	853:866	The other part	853:866	The other part was used to isolate the oligosaccharide by the corresponding lectin affinity chromatography and to characterize the structures of the isolated oligosaccharides by 1H NMR spectroscopy and FAB-MS.
1456441	8	43	dep	trisialyl	1223:1231	arg1	triantennary					1234:1245	triantennary	1234:1245	triantennary	1234:1245	The SNA-bound fraction was shown to contain trisialyl, triantennary structures.
1456441	3	44	theme	vulgaris	491:498	arg1	chromatography					532:545	Phaseolus vulgaris leukoagglutinin (LPHA) affinity chromatography	481:545	Phaseolus vulgaris leukoagglutinin (LPHA) affinity chromatography	481:545	Glycopeptides in the proteolytic digests were isolated by serial concanavalin A (Con A), Sambucus nigra agglutinin (SNA), and Phaseolus vulgaris leukoagglutinin (LPHA) affinity chromatography and subjected to preliminary analysis by 1H NMR spectroscopy.
1456441	12	45	theme	1:1	1917:1919	arg1	ratio					1897:1901	the ratio	1893:1901	the ratio approximately 1:1	1893:1919	The ratio of 2,4-triantennary vs 2,6-triantennary oligosaccharides attached to glycosylation site Asn413 was found to be approximately 5:1, whereas the two isomeric triantennary oligosaccharides were found to be attached to glycosylation site Asn611 in the ratio approximately 1:1.
1456441	12	46	gly	glycosylation	1719:1731	arg2	site					1733:1736	glycosylation site Asn413	1719:1743	glycosylation site Asn413	1719:1743	The ratio of 2,4-triantennary vs 2,6-triantennary oligosaccharides attached to glycosylation site Asn413 was found to be approximately 5:1, whereas the two isomeric triantennary oligosaccharides were found to be attached to glycosylation site Asn611 in the ratio approximately 1:1.
1456441	12	46	gly	glycosylation	1719:1731	arg2	Asn413					1738:1743	Asn413	1738:1743	Asn413	1738:1743	The ratio of 2,4-triantennary vs 2,6-triantennary oligosaccharides attached to glycosylation site Asn413 was found to be approximately 5:1, whereas the two isomeric triantennary oligosaccharides were found to be attached to glycosylation site Asn611 in the ratio approximately 1:1.
1456441	1	47	theme	human	243:247	arg1	h-STF					266:270	h-STF	266:270	h-STF	266:270	This report describes the N-glycosylation site mapping of human serotransferrin (h-STF).
1456441	1	47	theme	human	243:247	arg1	serotransferrin					249:263	human serotransferrin	243:263	human serotransferrin (h-STF)	243:271	This report describes the N-glycosylation site mapping of human serotransferrin (h-STF).
1456441	4	48	theme	glycopeptide	613:624	arg1	fractions					626:634	The glycopeptide fractions	609:634	The glycopeptide fractions	609:634	The glycopeptide fractions were then individually digested with N-glycanase.
1456441	12	49	dep	found	1749:1753	arg1	whereas					1780:1786	whereas	1780:1786	whereas	1780:1786	The ratio of 2,4-triantennary vs 2,6-triantennary oligosaccharides attached to glycosylation site Asn413 was found to be approximately 5:1, whereas the two isomeric triantennary oligosaccharides were found to be attached to glycosylation site Asn611 in the ratio approximately 1:1.
1456441	0	50	theme	serial	57:62	arg1	chromatography					80:93	serial lectin affinity chromatography	57:93	serial lectin affinity chromatography	57:93	N-glycosylation site mapping of human serotransferrin by serial lectin affinity chromatography, fast atom bombardment-mass spectrometry, and 1H nuclear magnetic resonance spectroscopy.
1456441	6	51	theme	lectin	929:934	arg1	chromatography					945:958	the corresponding lectin affinity chromatography	911:958	the corresponding lectin affinity chromatography	911:958	The other part was used to isolate the oligosaccharide by the corresponding lectin affinity chromatography and to characterize the structures of the isolated oligosaccharides by 1H NMR spectroscopy and FAB-MS.
1456441	12	52	gly	glycosylation	1864:1876	arg2	site					1878:1881	glycosylation site Asn611	1864:1888	glycosylation site Asn611	1864:1888	The ratio of 2,4-triantennary vs 2,6-triantennary oligosaccharides attached to glycosylation site Asn413 was found to be approximately 5:1, whereas the two isomeric triantennary oligosaccharides were found to be attached to glycosylation site Asn611 in the ratio approximately 1:1.
1456441	12	52	gly	glycosylation	1864:1876	arg2	Asn611					1883:1888	Asn611	1883:1888	Asn611	1883:1888	The ratio of 2,4-triantennary vs 2,6-triantennary oligosaccharides attached to glycosylation site Asn413 was found to be approximately 5:1, whereas the two isomeric triantennary oligosaccharides were found to be attached to glycosylation site Asn611 in the ratio approximately 1:1.
1456441	11	53	theme	trisialyl	1572:1580	arg1	2,4-triantennary					1582:1597	a trisialyl 2,4-triantennary	1570:1597	a trisialyl 2,4-triantennary	1570:1597	Two different oligosaccharides were characterized, namely, a trisialyl 2,4-triantennary and a trisialyl 2,6-triantennary glycan.
1456441	3	54	theme	Con	436:438	arg1	A					433:433	serial concanavalin A	413:433	serial concanavalin A (Con A)	413:441	Glycopeptides in the proteolytic digests were isolated by serial concanavalin A (Con A), Sambucus nigra agglutinin (SNA), and Phaseolus vulgaris leukoagglutinin (LPHA) affinity chromatography and subjected to preliminary analysis by 1H NMR spectroscopy.
1456441	3	54	theme	Con	436:438	arg1	A					440:440	Con A	436:440	Con A	436:440	Glycopeptides in the proteolytic digests were isolated by serial concanavalin A (Con A), Sambucus nigra agglutinin (SNA), and Phaseolus vulgaris leukoagglutinin (LPHA) affinity chromatography and subjected to preliminary analysis by 1H NMR spectroscopy.
1456441	10	55	theme	SNA-bound	1428:1436	arg1	glycopeptides					1438:1450	The SNA-bound glycopeptides	1424:1450	The SNA-bound glycopeptides	1424:1450	The SNA-bound glycopeptides were further fractionated by LPHA affinity chromatography.
1456441	6	56	theme	isolated	1002:1009	arg1	oligosaccharides					1011:1026	the isolated oligosaccharides	998:1026	the isolated oligosaccharides	998:1026	The other part was used to isolate the oligosaccharide by the corresponding lectin affinity chromatography and to characterize the structures of the isolated oligosaccharides by 1H NMR spectroscopy and FAB-MS.
1456441	5	57	theme	fraction	717:724	arg1	digest					702:707	the digest	698:707	the digest of each fraction	698:724	One part of the digest of each fraction was analyzed by fast atom bombardment-mass spectrometry (FAB-MS) to identify the peptide sequences of the glycosylation sites.
1456441	11	58	theme	trisialyl	1605:1613	arg1	glycan					1632:1637	a trisialyl 2,6-triantennary glycan	1603:1637	a trisialyl 2,6-triantennary glycan	1603:1637	Two different oligosaccharides were characterized, namely, a trisialyl 2,4-triantennary and a trisialyl 2,6-triantennary glycan.
1456441	3	59	theme	preliminary	564:574	arg1	analysis					576:583	preliminary analysis	564:583	preliminary analysis by 1H NMR spectroscopy	564:606	Glycopeptides in the proteolytic digests were isolated by serial concanavalin A (Con A), Sambucus nigra agglutinin (SNA), and Phaseolus vulgaris leukoagglutinin (LPHA) affinity chromatography and subjected to preliminary analysis by 1H NMR spectroscopy.
1456441	1	60	theme	N-glycosylation	211:225	arg1	site					227:230	N-glycosylation site	211:230	the N-glycosylation site mapping of human serotransferrin (h-STF)	207:271	This report describes the N-glycosylation site mapping of human serotransferrin (h-STF).
1456441	12	61	theme	oligosaccharides	1690:1705	arg1	ratio					1644:1648	The ratio	1640:1648	The ratio of 2,4-triantennary vs 2,6-triantennary oligosaccharides attached to glycosylation site Asn413	1640:1743	The ratio of 2,4-triantennary vs 2,6-triantennary oligosaccharides attached to glycosylation site Asn413 was found to be approximately 5:1, whereas the two isomeric triantennary oligosaccharides were found to be attached to glycosylation site Asn611 in the ratio approximately 1:1.
1456441	12	61	theme	oligosaccharides	1690:1705	arg1	5:1					1775:1777	5:1	1775:1777	5:1	1775:1777	The ratio of 2,4-triantennary vs 2,6-triantennary oligosaccharides attached to glycosylation site Asn413 was found to be approximately 5:1, whereas the two isomeric triantennary oligosaccharides were found to be attached to glycosylation site Asn611 in the ratio approximately 1:1.
1456441	7	62	theme	Con	1091:1093	arg1	fraction					1103:1110	the Con A-bound fraction	1087:1110	the Con A-bound fraction	1087:1110	The oligosaccharides in the Con A-bound fraction were shown to have bi-alpha(2-->6)-sialyl, diantennary structures.
1456441	5	63	theme	fast	742:745	arg1	FAB-MS					783:788	FAB-MS	783:788	FAB-MS	783:788	One part of the digest of each fraction was analyzed by fast atom bombardment-mass spectrometry (FAB-MS) to identify the peptide sequences of the glycosylation sites.
1456441	5	63	theme	fast	742:745	arg1	spectrometry					769:780	fast atom bombardment-mass spectrometry	742:780	fast atom bombardment-mass spectrometry (FAB-MS)	742:789	One part of the digest of each fraction was analyzed by fast atom bombardment-mass spectrometry (FAB-MS) to identify the peptide sequences of the glycosylation sites.
1456441	0	64	theme	resonance	161:169	arg1	spectroscopy					171:182	1H nuclear magnetic resonance spectroscopy	141:182	1H nuclear magnetic resonance spectroscopy	141:182	N-glycosylation site mapping of human serotransferrin by serial lectin affinity chromatography, fast atom bombardment-mass spectrometry, and 1H nuclear magnetic resonance spectroscopy.
1456441	3	65	theme	NMR	591:593	arg1	spectroscopy					595:606	1H NMR spectroscopy	588:606	1H NMR spectroscopy	588:606	Glycopeptides in the proteolytic digests were isolated by serial concanavalin A (Con A), Sambucus nigra agglutinin (SNA), and Phaseolus vulgaris leukoagglutinin (LPHA) affinity chromatography and subjected to preliminary analysis by 1H NMR spectroscopy.
1456441	3	66	from	Glycopeptides	355:367	arg1	digests					388:394	the proteolytic digests	372:394	the proteolytic digests	372:394	Glycopeptides in the proteolytic digests were isolated by serial concanavalin A (Con A), Sambucus nigra agglutinin (SNA), and Phaseolus vulgaris leukoagglutinin (LPHA) affinity chromatography and subjected to preliminary analysis by 1H NMR spectroscopy.
1456441	8	67	contain	contain	1215:1221	arg2	structures					1247:1256	trisialyl, triantennary structures	1223:1256	trisialyl, triantennary structures	1223:1256	The SNA-bound fraction was shown to contain trisialyl, triantennary structures.
1456441	8	67	contain	contain	1215:1221	arg1	fraction					1193:1200	The SNA-bound fraction	1179:1200	The SNA-bound fraction	1179:1200	The SNA-bound fraction was shown to contain trisialyl, triantennary structures.
1456441	0	68	theme	affinity	71:78	arg1	chromatography					80:93	serial lectin affinity chromatography	57:93	serial lectin affinity chromatography	57:93	N-glycosylation site mapping of human serotransferrin by serial lectin affinity chromatography, fast atom bombardment-mass spectrometry, and 1H nuclear magnetic resonance spectroscopy.
1456441	5	69	theme	atom	747:750	arg1	FAB-MS					783:788	FAB-MS	783:788	FAB-MS	783:788	One part of the digest of each fraction was analyzed by fast atom bombardment-mass spectrometry (FAB-MS) to identify the peptide sequences of the glycosylation sites.
1456441	5	69	theme	atom	747:750	arg1	spectrometry					769:780	fast atom bombardment-mass spectrometry	742:780	fast atom bombardment-mass spectrometry (FAB-MS)	742:789	One part of the digest of each fraction was analyzed by fast atom bombardment-mass spectrometry (FAB-MS) to identify the peptide sequences of the glycosylation sites.
1456441	6	70	theme	NMR	1034:1036	arg1	spectroscopy					1038:1049	1H NMR spectroscopy	1031:1049	1H NMR spectroscopy	1031:1049	The other part was used to isolate the oligosaccharide by the corresponding lectin affinity chromatography and to characterize the structures of the isolated oligosaccharides by 1H NMR spectroscopy and FAB-MS.
1456441	9	71	dep	h-STF	1361:1365	arg1	Asn413					1368:1373	Asn413	1368:1373	Asn413	1368:1373	Di- and triantennary oligosaccharides were found to occur on each of the two N-glycosylation sites of h-STF (Asn413 and Asn611) in the ratio of approximately 85:15.
1456441	9	71	dep	h-STF	1361:1365	arg1	Asn611					1379:1384	Asn611	1379:1384	Asn611	1379:1384	Di- and triantennary oligosaccharides were found to occur on each of the two N-glycosylation sites of h-STF (Asn413 and Asn611) in the ratio of approximately 85:15.
1456441	0	72	theme	atom	101:104	arg1	spectrometry					123:134	fast atom bombardment-mass spectrometry	96:134	fast atom bombardment-mass spectrometry	96:134	N-glycosylation site mapping of human serotransferrin by serial lectin affinity chromatography, fast atom bombardment-mass spectrometry, and 1H nuclear magnetic resonance spectroscopy.
1456441	5	73	theme	bombardment-mass	752:767	arg1	FAB-MS					783:788	FAB-MS	783:788	FAB-MS	783:788	One part of the digest of each fraction was analyzed by fast atom bombardment-mass spectrometry (FAB-MS) to identify the peptide sequences of the glycosylation sites.
1456441	5	73	theme	bombardment-mass	752:767	arg1	spectrometry					769:780	fast atom bombardment-mass spectrometry	742:780	fast atom bombardment-mass spectrometry (FAB-MS)	742:789	One part of the digest of each fraction was analyzed by fast atom bombardment-mass spectrometry (FAB-MS) to identify the peptide sequences of the glycosylation sites.
1456441	9	74	theme	N-glycosylation	1336:1350	arg1	h-STF					1361:1365	h-STF	1361:1365	h-STF (Asn413 and Asn611) in the ratio of approximately 85:15	1361:1421	Di- and triantennary oligosaccharides were found to occur on each of the two N-glycosylation sites of h-STF (Asn413 and Asn611) in the ratio of approximately 85:15.
1456441	9	74	theme	N-glycosylation	1336:1350	arg1	sites					1352:1356	the two N-glycosylation sites	1328:1356	the two N-glycosylation sites of h-STF (Asn413 and Asn611) in the ratio of approximately 85:15	1328:1421	Di- and triantennary oligosaccharides were found to occur on each of the two N-glycosylation sites of h-STF (Asn413 and Asn611) in the ratio of approximately 85:15.
1456441	7	75	from	oligosaccharides	1067:1082	arg1	fraction					1103:1110	the Con A-bound fraction	1087:1110	the Con A-bound fraction	1087:1110	The oligosaccharides in the Con A-bound fraction were shown to have bi-alpha(2-->6)-sialyl, diantennary structures.
1456441	0	76	theme	site	16:19	arg1	mapping					21:27	N-glycosylation site mapping	0:27	N-glycosylation site mapping of human serotransferrin by serial lectin affinity chromatography, fast atom bombardment-mass spectrometry, and 1H nuclear magnetic resonance spectroscopy	0:182	N-glycosylation site mapping of human serotransferrin by serial lectin affinity chromatography, fast atom bombardment-mass spectrometry, and 1H nuclear magnetic resonance spectroscopy.
1456441	9	77	from	h-STF	1361:1365	arg1	ratio					1394:1398	the ratio	1390:1398	the ratio of approximately 85:15	1390:1421	Di- and triantennary oligosaccharides were found to occur on each of the two N-glycosylation sites of h-STF (Asn413 and Asn611) in the ratio of approximately 85:15.
1456441	10	78	gly	glycopeptides	1438:1450	arg2	glycopeptides					1438:1450	The SNA-bound glycopeptides	1424:1450	The SNA-bound glycopeptides	1424:1450	The SNA-bound glycopeptides were further fractionated by LPHA affinity chromatography.
1456441	10	79	theme	LPHA	1481:1484	arg1	chromatography					1495:1508	LPHA affinity chromatography	1481:1508	LPHA affinity chromatography	1481:1508	The SNA-bound glycopeptides were further fractionated by LPHA affinity chromatography.
1456441	3	80	theme	Sambucus	444:451	arg1	SNA					471:473	SNA	471:473	SNA	471:473	Glycopeptides in the proteolytic digests were isolated by serial concanavalin A (Con A), Sambucus nigra agglutinin (SNA), and Phaseolus vulgaris leukoagglutinin (LPHA) affinity chromatography and subjected to preliminary analysis by 1H NMR spectroscopy.
1456441	3	80	theme	Sambucus	444:451	arg1	agglutinin					459:468	Sambucus nigra agglutinin	444:468	Sambucus nigra agglutinin (SNA)	444:474	Glycopeptides in the proteolytic digests were isolated by serial concanavalin A (Con A), Sambucus nigra agglutinin (SNA), and Phaseolus vulgaris leukoagglutinin (LPHA) affinity chromatography and subjected to preliminary analysis by 1H NMR spectroscopy.
1456441	5	81	theme	glycosylation	832:844	arg1	sites					846:850	the glycosylation sites	828:850	the glycosylation sites	828:850	One part of the digest of each fraction was analyzed by fast atom bombardment-mass spectrometry (FAB-MS) to identify the peptide sequences of the glycosylation sites.
1456441	3	82	theme	serial	413:418	arg1	A					433:433	serial concanavalin A	413:433	serial concanavalin A (Con A)	413:441	Glycopeptides in the proteolytic digests were isolated by serial concanavalin A (Con A), Sambucus nigra agglutinin (SNA), and Phaseolus vulgaris leukoagglutinin (LPHA) affinity chromatography and subjected to preliminary analysis by 1H NMR spectroscopy.
1456441	3	82	theme	serial	413:418	arg1	A					440:440	Con A	436:440	Con A	436:440	Glycopeptides in the proteolytic digests were isolated by serial concanavalin A (Con A), Sambucus nigra agglutinin (SNA), and Phaseolus vulgaris leukoagglutinin (LPHA) affinity chromatography and subjected to preliminary analysis by 1H NMR spectroscopy.
1456441	0	83	theme	serotransferrin	38:52	arg1	mapping					21:27	N-glycosylation site mapping	0:27	N-glycosylation site mapping of human serotransferrin by serial lectin affinity chromatography, fast atom bombardment-mass spectrometry, and 1H nuclear magnetic resonance spectroscopy	0:182	N-glycosylation site mapping of human serotransferrin by serial lectin affinity chromatography, fast atom bombardment-mass spectrometry, and 1H nuclear magnetic resonance spectroscopy.
1456441	0	84	gly	N-glycosylation	0:14	arg2	site					16:19	N-glycosylation site mapping	0:27	N-glycosylation site mapping of human serotransferrin by serial lectin affinity chromatography, fast atom bombardment-mass spectrometry, and 1H nuclear magnetic resonance spectroscopy	0:182	N-glycosylation site mapping of human serotransferrin by serial lectin affinity chromatography, fast atom bombardment-mass spectrometry, and 1H nuclear magnetic resonance spectroscopy.
1456441	0	84	gly	N-glycosylation	0:14	arg2	mapping					21:27	N-glycosylation site mapping	0:27	N-glycosylation site mapping of human serotransferrin by serial lectin affinity chromatography, fast atom bombardment-mass spectrometry, and 1H nuclear magnetic resonance spectroscopy	0:182	N-glycosylation site mapping of human serotransferrin by serial lectin affinity chromatography, fast atom bombardment-mass spectrometry, and 1H nuclear magnetic resonance spectroscopy.
1456441	12	85	theme	glycosylation	1719:1731	arg1	site					1733:1736	glycosylation site Asn413	1719:1743	glycosylation site Asn413	1719:1743	The ratio of 2,4-triantennary vs 2,6-triantennary oligosaccharides attached to glycosylation site Asn413 was found to be approximately 5:1, whereas the two isomeric triantennary oligosaccharides were found to be attached to glycosylation site Asn611 in the ratio approximately 1:1.
1456441	5	86	theme	peptide	807:813	arg1	sequences					815:823	the peptide sequences	803:823	the peptide sequences of the glycosylation sites	803:850	One part of the digest of each fraction was analyzed by fast atom bombardment-mass spectrometry (FAB-MS) to identify the peptide sequences of the glycosylation sites.
1456441	0	87	theme	1H	141:142	arg1	resonance					161:169	1H nuclear magnetic resonance	141:169	1H nuclear magnetic resonance spectroscopy	141:182	N-glycosylation site mapping of human serotransferrin by serial lectin affinity chromatography, fast atom bombardment-mass spectrometry, and 1H nuclear magnetic resonance spectroscopy.
1456441	5	88	gly	glycosylation	832:844	arg2	sites					846:850	the glycosylation sites	828:850	the glycosylation sites	828:850	One part of the digest of each fraction was analyzed by fast atom bombardment-mass spectrometry (FAB-MS) to identify the peptide sequences of the glycosylation sites.
1456441	3	89	theme	leukoagglutinin	500:514	arg1	chromatography					532:545	Phaseolus vulgaris leukoagglutinin (LPHA) affinity chromatography	481:545	Phaseolus vulgaris leukoagglutinin (LPHA) affinity chromatography	481:545	Glycopeptides in the proteolytic digests were isolated by serial concanavalin A (Con A), Sambucus nigra agglutinin (SNA), and Phaseolus vulgaris leukoagglutinin (LPHA) affinity chromatography and subjected to preliminary analysis by 1H NMR spectroscopy.
1456441	9	90	from	ratio	1394:1398	arg1	h-STF					1361:1365	h-STF	1361:1365	h-STF (Asn413 and Asn611) in the ratio of approximately 85:15	1361:1421	Di- and triantennary oligosaccharides were found to occur on each of the two N-glycosylation sites of h-STF (Asn413 and Asn611) in the ratio of approximately 85:15.
1456441	9	90	from	ratio	1394:1398	arg1	sites					1352:1356	the two N-glycosylation sites	1328:1356	the two N-glycosylation sites of h-STF (Asn413 and Asn611) in the ratio of approximately 85:15	1328:1421	Di- and triantennary oligosaccharides were found to occur on each of the two N-glycosylation sites of h-STF (Asn413 and Asn611) in the ratio of approximately 85:15.
1456441	6	91	theme	other	857:861	arg1	part					863:866	The other part	853:866	The other part	853:866	The other part was used to isolate the oligosaccharide by the corresponding lectin affinity chromatography and to characterize the structures of the isolated oligosaccharides by 1H NMR spectroscopy and FAB-MS.
1456441	3	92	theme	Phaseolus	481:489	arg1	chromatography					532:545	Phaseolus vulgaris leukoagglutinin (LPHA) affinity chromatography	481:545	Phaseolus vulgaris leukoagglutinin (LPHA) affinity chromatography	481:545	Glycopeptides in the proteolytic digests were isolated by serial concanavalin A (Con A), Sambucus nigra agglutinin (SNA), and Phaseolus vulgaris leukoagglutinin (LPHA) affinity chromatography and subjected to preliminary analysis by 1H NMR spectroscopy.
1456441	1	93	theme	serotransferrin	249:263	arg1	mapping					232:238	the N-glycosylation site mapping	207:238	the N-glycosylation site mapping of human serotransferrin (h-STF)	207:271	This report describes the N-glycosylation site mapping of human serotransferrin (h-STF).
1456441	12	94	theme	glycosylation	1864:1876	arg1	site					1878:1881	glycosylation site Asn611	1864:1888	glycosylation site Asn611	1864:1888	The ratio of 2,4-triantennary vs 2,6-triantennary oligosaccharides attached to glycosylation site Asn413 was found to be approximately 5:1, whereas the two isomeric triantennary oligosaccharides were found to be attached to glycosylation site Asn611 in the ratio approximately 1:1.
1456441	3	95	theme	affinity	523:530	arg1	chromatography					532:545	Phaseolus vulgaris leukoagglutinin (LPHA) affinity chromatography	481:545	Phaseolus vulgaris leukoagglutinin (LPHA) affinity chromatography	481:545	Glycopeptides in the proteolytic digests were isolated by serial concanavalin A (Con A), Sambucus nigra agglutinin (SNA), and Phaseolus vulgaris leukoagglutinin (LPHA) affinity chromatography and subjected to preliminary analysis by 1H NMR spectroscopy.
1456441	9	96	theme	85:15	1417:1421	arg1	ratio					1394:1398	the ratio	1390:1398	the ratio of approximately 85:15	1390:1421	Di- and triantennary oligosaccharides were found to occur on each of the two N-glycosylation sites of h-STF (Asn413 and Asn611) in the ratio of approximately 85:15.
8435067	3	0	theme	cDNA	429:432	arg1	sequence					434:441	the cDNA sequence	425:441	the cDNA sequence	425:441	The primary structure of lysosomal alpha-glucosidase, as deduced from the cDNA sequence, indicates that there are seven potential glycosylation sites.
8435067	3	1	theme	primary	359:365	arg1	structure					367:375	The primary structure	355:375	The primary structure	355:375	The primary structure of lysosomal alpha-glucosidase, as deduced from the cDNA sequence, indicates that there are seven potential glycosylation sites.
8435067	8	2	theme	mature	1092:1097	arg1	enzyme					1099:1104	mature enzyme	1092:1104	mature enzyme	1092:1104	However, removal of the second glycosylation site at Asn-233 interferes dramatically with the formation of mature enzyme.
8435067	8	3	theme	second	1009:1014	arg1	site					1030:1033	the second glycosylation site	1005:1033	the second glycosylation site	1005:1033	However, removal of the second glycosylation site at Asn-233 interferes dramatically with the formation of mature enzyme.
8435067	5	4	from	Asn-882	656:662	arg1	sites					647:651	The sites	643:651	The sites at Asn-882 and Asn-925	643:674	The sites at Asn-882 and Asn-925 were found to be located in a C-terminal propeptide which is cleaved off during maturation.
8435067	5	4	from	Asn-882	656:662	arg1	located					693:699	located	693:699	located	693:699	The sites at Asn-882 and Asn-925 were found to be located in a C-terminal propeptide which is cleaved off during maturation.
8435067	9	5	theme	mutant	1111:1116	arg1	precursor					1118:1126	The mutant precursor	1107:1126	The mutant precursor	1107:1126	The mutant precursor is synthesized normally and assembles in the endoplasmic reticulum, but immunoelectron microscopy reveals a deficiency of alpha-glucosidase in the Golgi complex and in the more distal compartments of the lysosomal transport pathway.
8435067	9	6	theme	alpha-glucosidase	1250:1266	arg1	deficiency					1236:1245	a deficiency	1234:1245	a deficiency of alpha-glucosidase in the Golgi complex and in the more distal compartments of the lysosomal transport pathway	1234:1358	The mutant precursor is synthesized normally and assembles in the endoplasmic reticulum, but immunoelectron microscopy reveals a deficiency of alpha-glucosidase in the Golgi complex and in the more distal compartments of the lysosomal transport pathway.
8435067	8	7	from	Asn-233	1038:1044	arg1	removal					994:1000	removal	994:1000	removal of the second glycosylation site at Asn-233	994:1044	However, removal of the second glycosylation site at Asn-233 interferes dramatically with the formation of mature enzyme.
8435067	5	8	located	located	693:699	arg2	sites					647:651	The sites	643:651	The sites at Asn-882 and Asn-925	643:674	The sites at Asn-882 and Asn-925 were found to be located in a C-terminal propeptide which is cleaved off during maturation.
8435067	5	8	located	located	693:699	arg2	located					693:699	located	693:699	located	693:699	The sites at Asn-882 and Asn-925 were found to be located in a C-terminal propeptide which is cleaved off during maturation.
8435067	5	8	located	located	693:699	arg1	propeptide					717:726	a C-terminal propeptide	704:726	a C-terminal propeptide which is cleaved off during maturation	704:765	The sites at Asn-882 and Asn-925 were found to be located in a C-terminal propeptide which is cleaved off during maturation.
8435067	5	9	theme	C-terminal	706:715	arg1	propeptide					717:726	a C-terminal propeptide	704:726	a C-terminal propeptide which is cleaved off during maturation	704:765	The sites at Asn-882 and Asn-925 were found to be located in a C-terminal propeptide which is cleaved off during maturation.
8435067	2	10	theme	efficient	266:274	arg1	transport					276:284	efficient transport	266:284	efficient transport of the enzyme to the lysosomes	266:315	Phosphorylation of mannose residues ensures efficient transport of the enzyme to the lysosomes via the mannose 6-phosphate receptor.
8435067	0	11	gly	glycosylation	70:82	arg2	sites					84:88	the glycosylation sites	66:88	the glycosylation sites	66:88	Human lysosomal alpha-glucosidase: functional characterization of the glycosylation sites.
8435067	9	12	from	deficiency	1236:1245	arg1	compartments					1312:1323	the more distal compartments	1296:1323	the more distal compartments of the lysosomal transport pathway	1296:1358	The mutant precursor is synthesized normally and assembles in the endoplasmic reticulum, but immunoelectron microscopy reveals a deficiency of alpha-glucosidase in the Golgi complex and in the more distal compartments of the lysosomal transport pathway.
8435067	9	12	from	deficiency	1236:1245	arg1	complex					1281:1287	the Golgi complex	1271:1287	the Golgi complex	1271:1287	The mutant precursor is synthesized normally and assembles in the endoplasmic reticulum, but immunoelectron microscopy reveals a deficiency of alpha-glucosidase in the Golgi complex and in the more distal compartments of the lysosomal transport pathway.
8435067	1	13	link	N-linked	91:98	arg1	glycosylation					100:112	N-linked glycosylation	91:112	N-linked glycosylation	91:112	N-linked glycosylation is one of the important events in the post-translational modification of human lysosomal alpha-glucosidase.
8435067	8	14	theme	enzyme	1099:1104	arg1	formation					1079:1087	the formation	1075:1087	the formation of mature enzyme	1075:1104	However, removal of the second glycosylation site at Asn-233 interferes dramatically with the formation of mature enzyme.
8435067	6	15	theme	lysosomal	852:860	arg1	alpha-glucosidase					862:878	human lysosomal alpha-glucosidase	846:878	human lysosomal alpha-glucosidase	846:878	Evidence is presented that at least two of the oligosaccharide side chains of human lysosomal alpha-glucosidase are phosphorylated.
8435067	3	16	theme	alpha-glucosidase	390:406	arg1	structure					367:375	The primary structure	355:375	The primary structure	355:375	The primary structure of lysosomal alpha-glucosidase, as deduced from the cDNA sequence, indicates that there are seven potential glycosylation sites.
8435067	6	17	theme	human	846:850	arg1	alpha-glucosidase					862:878	human lysosomal alpha-glucosidase	846:878	human lysosomal alpha-glucosidase	846:878	Evidence is presented that at least two of the oligosaccharide side chains of human lysosomal alpha-glucosidase are phosphorylated.
8435067	1	18	theme	human	187:191	arg1	alpha-glucosidase					203:219	human lysosomal alpha-glucosidase	187:219	human lysosomal alpha-glucosidase	187:219	N-linked glycosylation is one of the important events in the post-translational modification of human lysosomal alpha-glucosidase.
8435067	8	19	gly	glycosylation	1016:1028	arg2	site					1030:1033	the second glycosylation site	1005:1033	the second glycosylation site	1005:1033	However, removal of the second glycosylation site at Asn-233 interferes dramatically with the formation of mature enzyme.
8435067	1	20	from	events	138:143	arg1	modification					171:182	the post-translational modification	148:182	the post-translational modification of human lysosomal alpha-glucosidase	148:219	N-linked glycosylation is one of the important events in the post-translational modification of human lysosomal alpha-glucosidase.
8435067	1	21	theme	N-linked	91:98	arg1	glycosylation					100:112	N-linked glycosylation	91:112	N-linked glycosylation	91:112	N-linked glycosylation is one of the important events in the post-translational modification of human lysosomal alpha-glucosidase.
8435067	7	22	theme	six	915:917	arg1	Elimination					900:910	Elimination	900:910	Elimination of six of the seven sites	900:936	Elimination of six of the seven sites does not disturb enzyme synthesis or function.
8435067	1	23	theme	lysosomal	193:201	arg1	alpha-glucosidase					203:219	human lysosomal alpha-glucosidase	187:219	human lysosomal alpha-glucosidase	187:219	N-linked glycosylation is one of the important events in the post-translational modification of human lysosomal alpha-glucosidase.
8435067	0	24	theme	lysosomal	6:14	arg1	alpha-glucosidase					16:32	Human lysosomal alpha-glucosidase	0:32	Human lysosomal alpha-glucosidase	0:32	Human lysosomal alpha-glucosidase: functional characterization of the glycosylation sites.
8435067	6	25	theme	chains	836:841	arg1	chains					836:841	the oligosaccharide side chains	811:841	the oligosaccharide side chains of human lysosomal alpha-glucosidase	811:878	Evidence is presented that at least two of the oligosaccharide side chains of human lysosomal alpha-glucosidase are phosphorylated.
8435067	6	25	theme	chains	836:841	arg1	two					804:806	two	804:806	two	804:806	Evidence is presented that at least two of the oligosaccharide side chains of human lysosomal alpha-glucosidase are phosphorylated.
8435067	1	26	theme	alpha-glucosidase	203:219	arg1	modification					171:182	the post-translational modification	148:182	the post-translational modification of human lysosomal alpha-glucosidase	148:219	N-linked glycosylation is one of the important events in the post-translational modification of human lysosomal alpha-glucosidase.
8435067	0	27	theme	Human	0:4	arg1	alpha-glucosidase					16:32	Human lysosomal alpha-glucosidase	0:32	Human lysosomal alpha-glucosidase	0:32	Human lysosomal alpha-glucosidase: functional characterization of the glycosylation sites.
8435067	6	28	theme	side	831:834	arg1	chains					836:841	the oligosaccharide side chains	811:841	the oligosaccharide side chains of human lysosomal alpha-glucosidase	811:878	Evidence is presented that at least two of the oligosaccharide side chains of human lysosomal alpha-glucosidase are phosphorylated.
8435067	9	29	theme	distal	1305:1310	arg1	compartments					1312:1323	the more distal compartments	1296:1323	the more distal compartments of the lysosomal transport pathway	1296:1358	The mutant precursor is synthesized normally and assembles in the endoplasmic reticulum, but immunoelectron microscopy reveals a deficiency of alpha-glucosidase in the Golgi complex and in the more distal compartments of the lysosomal transport pathway.
8435067	5	30	from	located	693:699	arg1	propeptide					717:726	a C-terminal propeptide	704:726	a C-terminal propeptide which is cleaved off during maturation	704:765	The sites at Asn-882 and Asn-925 were found to be located in a C-terminal propeptide which is cleaved off during maturation.
8435067	6	31	theme	oligosaccharide	815:829	arg1	chains					836:841	the oligosaccharide side chains	811:841	the oligosaccharide side chains of human lysosomal alpha-glucosidase	811:878	Evidence is presented that at least two of the oligosaccharide side chains of human lysosomal alpha-glucosidase are phosphorylated.
8435067	6	32	theme	alpha-glucosidase	862:878	arg1	chains					836:841	the oligosaccharide side chains	811:841	the oligosaccharide side chains of human lysosomal alpha-glucosidase	811:878	Evidence is presented that at least two of the oligosaccharide side chains of human lysosomal alpha-glucosidase are phosphorylated.
8435067	3	33	theme	lysosomal	380:388	arg1	alpha-glucosidase					390:406	lysosomal alpha-glucosidase	380:406	lysosomal alpha-glucosidase	380:406	The primary structure of lysosomal alpha-glucosidase, as deduced from the cDNA sequence, indicates that there are seven potential glycosylation sites.
8435067	3	34	dep	structure	367:375	arg1	deduced					412:418	deduced	412:418	deduced from the cDNA sequence	412:441	The primary structure of lysosomal alpha-glucosidase, as deduced from the cDNA sequence, indicates that there are seven potential glycosylation sites.
8435067	2	35	theme	6-phosphate	333:343	arg1	receptor					345:352	the mannose 6-phosphate receptor	321:352	the mannose 6-phosphate receptor	321:352	Phosphorylation of mannose residues ensures efficient transport of the enzyme to the lysosomes via the mannose 6-phosphate receptor.
8435067	9	36	theme	endoplasmic	1173:1183	arg1	reticulum					1185:1193	the endoplasmic reticulum	1169:1193	the endoplasmic reticulum	1169:1193	The mutant precursor is synthesized normally and assembles in the endoplasmic reticulum, but immunoelectron microscopy reveals a deficiency of alpha-glucosidase in the Golgi complex and in the more distal compartments of the lysosomal transport pathway.
8435067	8	37	attach	removal	994:1000	arg2	site					1030:1033	the second glycosylation site	1005:1033	the second glycosylation site	1005:1033	However, removal of the second glycosylation site at Asn-233 interferes dramatically with the formation of mature enzyme.
8435067	8	37	attach	removal	994:1000	arg3	Asn-233					1038:1044	Asn-233	1038:1044	Asn-233	1038:1044	However, removal of the second glycosylation site at Asn-233 interferes dramatically with the formation of mature enzyme.
8435067	7	38	theme	sites	932:936	arg1	sites					932:936	the seven sites	922:936	the seven sites	922:936	Elimination of six of the seven sites does not disturb enzyme synthesis or function.
8435067	7	38	theme	sites	932:936	arg1	six					915:917	six	915:917	six	915:917	Elimination of six of the seven sites does not disturb enzyme synthesis or function.
8435067	0	39	theme	functional	35:44	arg1	characterization					46:61	functional characterization	35:61	functional characterization of the glycosylation sites	35:88	Human lysosomal alpha-glucosidase: functional characterization of the glycosylation sites.
8435067	9	40	theme	Golgi	1275:1279	arg1	complex					1281:1287	the Golgi complex	1271:1287	the Golgi complex	1271:1287	The mutant precursor is synthesized normally and assembles in the endoplasmic reticulum, but immunoelectron microscopy reveals a deficiency of alpha-glucosidase in the Golgi complex and in the more distal compartments of the lysosomal transport pathway.
8435067	5	41	from	propeptide	717:726	arg1	sites					647:651	The sites	643:651	The sites at Asn-882 and Asn-925	643:674	The sites at Asn-882 and Asn-925 were found to be located in a C-terminal propeptide which is cleaved off during maturation.
8435067	5	41	from	propeptide	717:726	arg1	located					693:699	located	693:699	located	693:699	The sites at Asn-882 and Asn-925 were found to be located in a C-terminal propeptide which is cleaved off during maturation.
8435067	8	42	theme	site	1030:1033	arg1	removal					994:1000	removal	994:1000	removal of the second glycosylation site at Asn-233	994:1044	However, removal of the second glycosylation site at Asn-233 interferes dramatically with the formation of mature enzyme.
8435067	3	43	theme	potential	475:483	arg1	sites					499:503	seven potential glycosylation sites	469:503	seven potential glycosylation sites	469:503	The primary structure of lysosomal alpha-glucosidase, as deduced from the cDNA sequence, indicates that there are seven potential glycosylation sites.
8435067	0	44	dep	characterization	46:61	arg1	alpha-glucosidase					16:32	Human lysosomal alpha-glucosidase	0:32	Human lysosomal alpha-glucosidase	0:32	Human lysosomal alpha-glucosidase: functional characterization of the glycosylation sites.
8435067	2	45	theme	residues	249:256	arg1	Phosphorylation					222:236	Phosphorylation	222:236	Phosphorylation of mannose residues	222:256	Phosphorylation of mannose residues ensures efficient transport of the enzyme to the lysosomes via the mannose 6-phosphate receptor.
8435067	9	46	theme	lysosomal	1332:1340	arg1	pathway					1352:1358	the lysosomal transport pathway	1328:1358	the lysosomal transport pathway	1328:1358	The mutant precursor is synthesized normally and assembles in the endoplasmic reticulum, but immunoelectron microscopy reveals a deficiency of alpha-glucosidase in the Golgi complex and in the more distal compartments of the lysosomal transport pathway.
8435067	9	47	theme	immunoelectron	1200:1213	arg1	microscopy					1215:1224	immunoelectron microscopy	1200:1224	immunoelectron microscopy	1200:1224	The mutant precursor is synthesized normally and assembles in the endoplasmic reticulum, but immunoelectron microscopy reveals a deficiency of alpha-glucosidase in the Golgi complex and in the more distal compartments of the lysosomal transport pathway.
8435067	1	48	theme	important	128:136	arg1	events					138:143	the important events	124:143	the important events in the post-translational modification of human lysosomal alpha-glucosidase	124:219	N-linked glycosylation is one of the important events in the post-translational modification of human lysosomal alpha-glucosidase.
8435067	2	49	theme	mannose	241:247	arg1	residues					249:256	mannose residues	241:256	mannose residues	241:256	Phosphorylation of mannose residues ensures efficient transport of the enzyme to the lysosomes via the mannose 6-phosphate receptor.
8435067	3	50	gly	glycosylation	485:497	arg2	sites					499:503	seven potential glycosylation sites	469:503	seven potential glycosylation sites	469:503	The primary structure of lysosomal alpha-glucosidase, as deduced from the cDNA sequence, indicates that there are seven potential glycosylation sites.
8435067	3	50	gly	glycosylation	485:497	arg2	seven					469:473	seven	469:473	seven	469:473	The primary structure of lysosomal alpha-glucosidase, as deduced from the cDNA sequence, indicates that there are seven potential glycosylation sites.
8435067	4	51	gly	glycosylated	629:640	arg1	sites					619:623	all seven sites	609:623	all seven sites	609:623	We have eliminated these sites individually by site-directed mutagenesis and thereby demonstrated that all seven sites are glycosylated.
8435067	1	52	theme	events	138:143	arg1	events					138:143	the important events	124:143	the important events in the post-translational modification of human lysosomal alpha-glucosidase	124:219	N-linked glycosylation is one of the important events in the post-translational modification of human lysosomal alpha-glucosidase.
8435067	1	52	theme	events	138:143	arg1	one					117:119	one	117:119	one	117:119	N-linked glycosylation is one of the important events in the post-translational modification of human lysosomal alpha-glucosidase.
8435067	9	53	theme	transport	1342:1350	arg1	pathway					1352:1358	the lysosomal transport pathway	1328:1358	the lysosomal transport pathway	1328:1358	The mutant precursor is synthesized normally and assembles in the endoplasmic reticulum, but immunoelectron microscopy reveals a deficiency of alpha-glucosidase in the Golgi complex and in the more distal compartments of the lysosomal transport pathway.
8435067	2	54	theme	mannose	325:331	arg1	receptor					345:352	the mannose 6-phosphate receptor	321:352	the mannose 6-phosphate receptor	321:352	Phosphorylation of mannose residues ensures efficient transport of the enzyme to the lysosomes via the mannose 6-phosphate receptor.
8435067	7	55	theme	enzyme	955:960	arg1	synthesis					962:970	enzyme synthesis	955:970	enzyme synthesis	955:970	Elimination of six of the seven sites does not disturb enzyme synthesis or function.
8435067	0	56	theme	sites	84:88	arg1	characterization					46:61	functional characterization	35:61	functional characterization of the glycosylation sites	35:88	Human lysosomal alpha-glucosidase: functional characterization of the glycosylation sites.
8435067	9	57	theme	pathway	1352:1358	arg1	compartments					1312:1323	the more distal compartments	1296:1323	the more distal compartments of the lysosomal transport pathway	1296:1358	The mutant precursor is synthesized normally and assembles in the endoplasmic reticulum, but immunoelectron microscopy reveals a deficiency of alpha-glucosidase in the Golgi complex and in the more distal compartments of the lysosomal transport pathway.
8435067	2	58	theme	enzyme	293:298	arg1	transport					276:284	efficient transport	266:284	efficient transport of the enzyme to the lysosomes	266:315	Phosphorylation of mannose residues ensures efficient transport of the enzyme to the lysosomes via the mannose 6-phosphate receptor.
8435067	5	59	from	Asn-925	668:674	arg1	sites					647:651	The sites	643:651	The sites at Asn-882 and Asn-925	643:674	The sites at Asn-882 and Asn-925 were found to be located in a C-terminal propeptide which is cleaved off during maturation.
8435067	5	59	from	Asn-925	668:674	arg1	located					693:699	located	693:699	located	693:699	The sites at Asn-882 and Asn-925 were found to be located in a C-terminal propeptide which is cleaved off during maturation.
8435067	3	60	theme	glycosylation	485:497	arg1	sites					499:503	seven potential glycosylation sites	469:503	seven potential glycosylation sites	469:503	The primary structure of lysosomal alpha-glucosidase, as deduced from the cDNA sequence, indicates that there are seven potential glycosylation sites.
8435067	0	61	theme	glycosylation	70:82	arg1	sites					84:88	the glycosylation sites	66:88	the glycosylation sites	66:88	Human lysosomal alpha-glucosidase: functional characterization of the glycosylation sites.
8435067	4	62	theme	site-directed	553:565	arg1	mutagenesis					567:577	site-directed mutagenesis	553:577	site-directed mutagenesis	553:577	We have eliminated these sites individually by site-directed mutagenesis and thereby demonstrated that all seven sites are glycosylated.
8435067	8	63	theme	glycosylation	1016:1028	arg1	site					1030:1033	the second glycosylation site	1005:1033	the second glycosylation site	1005:1033	However, removal of the second glycosylation site at Asn-233 interferes dramatically with the formation of mature enzyme.
8435067	1	64	theme	post-translational	152:169	arg1	modification					171:182	the post-translational modification	148:182	the post-translational modification of human lysosomal alpha-glucosidase	148:219	N-linked glycosylation is one of the important events in the post-translational modification of human lysosomal alpha-glucosidase.
1567356	3	0	theme	h.p.l.c.	315:322	arg1	profiles					324:331	Standard h.p.l.c. profiles	306:331	Standard h.p.l.c. profiles	306:331	Standard h.p.l.c. profiles have been developed to analyse the percentage and distribution of the glycoforms present at each glycosylation site in OMD and its molecular variants.
1567356	7	1	from	variants	1117:1124	arg1	biantennary					1069:1079	biantennary	1069:1079	biantennary	1069:1079	Only glycosylation site II of the five present is 100% biantennary in the retained and weakly retained variants.
1567356	3	2	dep	percentage	368:377	arg1	the					364:366	the	364:366	the	364:366	Standard h.p.l.c. profiles have been developed to analyse the percentage and distribution of the glycoforms present at each glycosylation site in OMD and its molecular variants.
1567356	10	3	theme	site	1332:1335	arg1	distribution					1337:1348	the site distribution	1328:1348	the site distribution of oligosaccharides in the variants	1328:1384	On the basis of the site distribution of oligosaccharides in the variants, efforts were made to understand the factors that control the processing of the carbohydrate chains in OMD.
1567356	1	4	theme	tetra-antennary	126:140	arg1	chains					149:154	tetra-antennary glycan chains	126:154	tetra-antennary glycan chains	126:154	Orosomucoid (OMD) contains complex bi-, tri- and tetra-antennary glycan chains.
1567356	4	5	theme	earlier	568:574	arg1	results					576:582	the earlier results	564:582	the earlier results of others	564:592	The ability to quantify the glycoforms present at each site allows us to extend the earlier results of others and resolve the remaining questions concerning the glycan structures of these variants.
1567356	0	6	theme	glycoprotein	63:74	arg1	glycoprotein					63:74	human alpha 1-acid glycoprotein	44:74	human alpha 1-acid glycoprotein	44:74	Analysis of the five glycosylation sites of human alpha 1-acid glycoprotein.
1567356	0	6	theme	glycoprotein	63:74	arg1	sites					35:39	the five glycosylation sites	12:39	the five glycosylation sites of human alpha 1-acid glycoprotein	12:74	Analysis of the five glycosylation sites of human alpha 1-acid glycoprotein.
1567356	4	7	from	site	539:542	arg1	present					523:529	present	523:529	present	523:529	The ability to quantify the glycoforms present at each site allows us to extend the earlier results of others and resolve the remaining questions concerning the glycan structures of these variants.
1567356	1	8	theme	glycan	142:147	arg1	chains					149:154	tetra-antennary glycan chains	126:154	tetra-antennary glycan chains	126:154	Orosomucoid (OMD) contains complex bi-, tri- and tetra-antennary glycan chains.
1567356	5	9	theme	bi-	721:723	arg1	proportions					706:716	the proportions	702:716	the proportions of bi-, tri- and tetra-antennary chains	702:756	Most significantly, the proportions of bi-, tri- and tetra-antennary chains differ at each site for the three molecular variants.
1567356	1	10	contain	contains	95:102	arg2	chains					149:154	tetra-antennary glycan chains	126:154	tetra-antennary glycan chains	126:154	Orosomucoid (OMD) contains complex bi-, tri- and tetra-antennary glycan chains.
1567356	1	10	contain	contains	95:102	arg1	OMD					90:92	OMD	90:92	OMD	90:92	Orosomucoid (OMD) contains complex bi-, tri- and tetra-antennary glycan chains.
1567356	1	10	contain	contains	95:102	arg2	tri-					117:120	tri-	117:120	tri-	117:120	Orosomucoid (OMD) contains complex bi-, tri- and tetra-antennary glycan chains.
1567356	1	10	contain	contains	95:102	arg1	Orosomucoid					77:87	Orosomucoid	77:87	Orosomucoid (OMD)	77:93	Orosomucoid (OMD) contains complex bi-, tri- and tetra-antennary glycan chains.
1567356	1	10	contain	contains	95:102	arg2	bi-					112:114	complex bi-	104:114	complex bi-	104:114	Orosomucoid (OMD) contains complex bi-, tri- and tetra-antennary glycan chains.
1567356	6	11	theme	concanavalin	852:863	arg1	A					865:865	concanavalin A	852:865	concanavalin A	852:865	The most strongly retained variant from concanavalin A is uniquely capable of possessing biantennary chains at all five sites, whereas the unretained variant is completely devoid of biantennary chains.
1567356	9	12	theme	matrix-assisted	1255:1269	arg1	spectrometry					1298:1309	matrix-assisted u.v. laser desorption mass spectrometry	1255:1309	matrix-assisted u.v. laser desorption mass spectrometry	1255:1309	Molecular masses of the glycoforms were verified by matrix-assisted u.v. laser desorption mass spectrometry.
1567356	9	13	theme	desorption	1282:1291	arg1	spectrometry					1298:1309	matrix-assisted u.v. laser desorption mass spectrometry	1255:1309	matrix-assisted u.v. laser desorption mass spectrometry	1255:1309	Molecular masses of the glycoforms were verified by matrix-assisted u.v. laser desorption mass spectrometry.
1567356	11	14	theme	processing	1549:1558	arg1	model					1540:1544	the 'site-directed' model	1520:1544	the 'site-directed' model of processing	1520:1558	The results indicate that the 'site-directed' model of processing offers the most consistent explanation for the structures seen at the individual glycosylation sites of OMD.
1567356	9	15	theme	mass	1293:1296	arg1	spectrometry					1298:1309	matrix-assisted u.v. laser desorption mass spectrometry	1255:1309	matrix-assisted u.v. laser desorption mass spectrometry	1255:1309	Molecular masses of the glycoforms were verified by matrix-assisted u.v. laser desorption mass spectrometry.
1567356	10	16	dep	distribution	1337:1348	arg1	the					1315:1317	the	1315:1317	the	1315:1317	On the basis of the site distribution of oligosaccharides in the variants, efforts were made to understand the factors that control the processing of the carbohydrate chains in OMD.
1567356	10	16	dep	distribution	1337:1348	arg1	basis					1319:1323	basis	1319:1323	basis	1319:1323	On the basis of the site distribution of oligosaccharides in the variants, efforts were made to understand the factors that control the processing of the carbohydrate chains in OMD.
1567356	5	17	theme	tri-	726:729	arg1	proportions					706:716	the proportions	702:716	the proportions of bi-, tri- and tetra-antennary chains	702:756	Most significantly, the proportions of bi-, tri- and tetra-antennary chains differ at each site for the three molecular variants.
1567356	4	18	theme	remaining	610:618	arg1	questions					620:628	the remaining questions	606:628	the remaining questions concerning the glycan structures of these variants	606:679	The ability to quantify the glycoforms present at each site allows us to extend the earlier results of others and resolve the remaining questions concerning the glycan structures of these variants.
1567356	0	19	gly	glycoprotein	63:74	arg1	glycoprotein					63:74	human alpha 1-acid glycoprotein	44:74	human alpha 1-acid glycoprotein	44:74	Analysis of the five glycosylation sites of human alpha 1-acid glycoprotein.
1567356	11	20	theme	individual	1630:1639	arg1	OMD					1664:1666	OMD	1664:1666	OMD	1664:1666	The results indicate that the 'site-directed' model of processing offers the most consistent explanation for the structures seen at the individual glycosylation sites of OMD.
1567356	11	20	theme	individual	1630:1639	arg1	sites					1655:1659	the individual glycosylation sites	1626:1659	the individual glycosylation sites of OMD	1626:1666	The results indicate that the 'site-directed' model of processing offers the most consistent explanation for the structures seen at the individual glycosylation sites of OMD.
1567356	3	21	theme	present	414:420	arg1	glycoforms					403:412	the glycoforms	399:412	the glycoforms present at each glycosylation site in OMD and its molecular variants	399:481	Standard h.p.l.c. profiles have been developed to analyse the percentage and distribution of the glycoforms present at each glycosylation site in OMD and its molecular variants.
1567356	8	22	theme	gene	1148:1151	arg1	products					1153:1160	the two gene products	1140:1160	the two gene products of OMD	1140:1167	In addition, the two gene products of OMD were differentially glycosylated.
1567356	4	23	theme	glycan	645:650	arg1	structures					652:661	the glycan structures	641:661	the glycan structures of these variants	641:679	The ability to quantify the glycoforms present at each site allows us to extend the earlier results of others and resolve the remaining questions concerning the glycan structures of these variants.
1567356	11	24	theme	glycosylation	1641:1653	arg1	OMD					1664:1666	OMD	1664:1666	OMD	1664:1666	The results indicate that the 'site-directed' model of processing offers the most consistent explanation for the structures seen at the individual glycosylation sites of OMD.
1567356	11	24	theme	glycosylation	1641:1653	arg1	sites					1655:1659	the individual glycosylation sites	1626:1659	the individual glycosylation sites of OMD	1626:1666	The results indicate that the 'site-directed' model of processing offers the most consistent explanation for the structures seen at the individual glycosylation sites of OMD.
1567356	6	25	dep	capable	879:885	arg1	capable					879:885	capable	879:885	capable	879:885	The most strongly retained variant from concanavalin A is uniquely capable of possessing biantennary chains at all five sites, whereas the unretained variant is completely devoid of biantennary chains.
1567356	6	25	dep	capable	879:885	arg1	variant					839:845	The most strongly retained variant	812:845	The most strongly retained variant from concanavalin A	812:865	The most strongly retained variant from concanavalin A is uniquely capable of possessing biantennary chains at all five sites, whereas the unretained variant is completely devoid of biantennary chains.
1567356	6	25	dep	capable	879:885	arg1	whereas					939:945	whereas	939:945	whereas	939:945	The most strongly retained variant from concanavalin A is uniquely capable of possessing biantennary chains at all five sites, whereas the unretained variant is completely devoid of biantennary chains.
1567356	5	26	theme	tetra-antennary	735:749	arg1	chains					751:756	tetra-antennary chains	735:756	tetra-antennary chains	735:756	Most significantly, the proportions of bi-, tri- and tetra-antennary chains differ at each site for the three molecular variants.
1567356	4	27	attach	present	523:529	arg2	glycoforms					512:521	the glycoforms	508:521	the glycoforms present at each site	508:542	The ability to quantify the glycoforms present at each site allows us to extend the earlier results of others and resolve the remaining questions concerning the glycan structures of these variants.
1567356	4	27	attach	present	523:529	arg1	site					539:542	each site	534:542	each site	534:542	The ability to quantify the glycoforms present at each site allows us to extend the earlier results of others and resolve the remaining questions concerning the glycan structures of these variants.
1567356	11	28	gly	glycosylation	1641:1653	arg2	OMD					1664:1666	OMD	1664:1666	OMD	1664:1666	The results indicate that the 'site-directed' model of processing offers the most consistent explanation for the structures seen at the individual glycosylation sites of OMD.
1567356	11	28	gly	glycosylation	1641:1653	arg1	OMD					1664:1666	OMD	1664:1666	OMD	1664:1666	The results indicate that the 'site-directed' model of processing offers the most consistent explanation for the structures seen at the individual glycosylation sites of OMD.
1567356	11	28	gly	glycosylation	1641:1653	arg2	sites					1655:1659	the individual glycosylation sites	1626:1659	the individual glycosylation sites of OMD	1626:1666	The results indicate that the 'site-directed' model of processing offers the most consistent explanation for the structures seen at the individual glycosylation sites of OMD.
1567356	5	29	theme	molecular	792:800	arg1	variants					802:809	the three molecular variants	782:809	the three molecular variants	782:809	Most significantly, the proportions of bi-, tri- and tetra-antennary chains differ at each site for the three molecular variants.
1567356	8	30	gly	glycosylated	1189:1200	arg2	products					1153:1160	the two gene products	1140:1160	the two gene products of OMD	1140:1167	In addition, the two gene products of OMD were differentially glycosylated.
1567356	8	30	gly	glycosylated	1189:1200	arg1	products					1153:1160	the two gene products	1140:1160	the two gene products of OMD	1140:1167	In addition, the two gene products of OMD were differentially glycosylated.
1567356	8	30	gly	glycosylated	1189:1200	arg1	addition					1130:1137	addition	1130:1137	addition	1130:1137	In addition, the two gene products of OMD were differentially glycosylated.
1567356	6	31	theme	retained	830:837	arg1	capable					879:885	capable	879:885	capable	879:885	The most strongly retained variant from concanavalin A is uniquely capable of possessing biantennary chains at all five sites, whereas the unretained variant is completely devoid of biantennary chains.
1567356	6	31	theme	retained	830:837	arg1	whereas					939:945	whereas	939:945	whereas	939:945	The most strongly retained variant from concanavalin A is uniquely capable of possessing biantennary chains at all five sites, whereas the unretained variant is completely devoid of biantennary chains.
1567356	6	31	theme	retained	830:837	arg1	variant					839:845	The most strongly retained variant	812:845	The most strongly retained variant from concanavalin A	812:865	The most strongly retained variant from concanavalin A is uniquely capable of possessing biantennary chains at all five sites, whereas the unretained variant is completely devoid of biantennary chains.
1567356	3	32	theme	glycosylation	430:442	arg1	site					444:447	each glycosylation site	425:447	each glycosylation site in OMD and its molecular variants	425:481	Standard h.p.l.c. profiles have been developed to analyse the percentage and distribution of the glycoforms present at each glycosylation site in OMD and its molecular variants.
1567356	6	33	from	A	865:865	arg1	capable					879:885	capable	879:885	capable	879:885	The most strongly retained variant from concanavalin A is uniquely capable of possessing biantennary chains at all five sites, whereas the unretained variant is completely devoid of biantennary chains.
1567356	6	33	from	A	865:865	arg1	whereas					939:945	whereas	939:945	whereas	939:945	The most strongly retained variant from concanavalin A is uniquely capable of possessing biantennary chains at all five sites, whereas the unretained variant is completely devoid of biantennary chains.
1567356	6	33	from	A	865:865	arg1	variant					839:845	The most strongly retained variant	812:845	The most strongly retained variant from concanavalin A	812:865	The most strongly retained variant from concanavalin A is uniquely capable of possessing biantennary chains at all five sites, whereas the unretained variant is completely devoid of biantennary chains.
1567356	6	34	theme	unretained	951:960	arg1	devoid					984:989	devoid	984:989	devoid	984:989	The most strongly retained variant from concanavalin A is uniquely capable of possessing biantennary chains at all five sites, whereas the unretained variant is completely devoid of biantennary chains.
1567356	6	34	theme	unretained	951:960	arg1	variant					962:968	the unretained variant	947:968	the unretained variant	947:968	The most strongly retained variant from concanavalin A is uniquely capable of possessing biantennary chains at all five sites, whereas the unretained variant is completely devoid of biantennary chains.
1567356	7	35	theme	present	1053:1059	arg1	present					1053:1059	the five present	1044:1059	the five present	1044:1059	Only glycosylation site II of the five present is 100% biantennary in the retained and weakly retained variants.
1567356	7	35	theme	present	1053:1059	arg1	site					1033:1036	Only glycosylation site II	1014:1039	Only glycosylation site II of the five present	1014:1059	Only glycosylation site II of the five present is 100% biantennary in the retained and weakly retained variants.
1567356	8	36	theme	OMD	1165:1167	arg1	products					1153:1160	the two gene products	1140:1160	the two gene products of OMD	1140:1167	In addition, the two gene products of OMD were differentially glycosylated.
1567356	10	37	from	distribution	1337:1348	arg1	variants					1377:1384	the variants	1373:1384	the variants	1373:1384	On the basis of the site distribution of oligosaccharides in the variants, efforts were made to understand the factors that control the processing of the carbohydrate chains in OMD.
1567356	7	38	from	biantennary	1069:1079	arg1	variants					1117:1124	weakly retained variants	1101:1124	weakly retained variants	1101:1124	Only glycosylation site II of the five present is 100% biantennary in the retained and weakly retained variants.
1567356	7	38	from	biantennary	1069:1079	arg1	the					1084:1086	the	1084:1086	the	1084:1086	Only glycosylation site II of the five present is 100% biantennary in the retained and weakly retained variants.
1567356	10	39	theme	chains	1479:1484	arg1	processing					1448:1457	the processing	1444:1457	the processing of the carbohydrate chains in OMD	1444:1491	On the basis of the site distribution of oligosaccharides in the variants, efforts were made to understand the factors that control the processing of the carbohydrate chains in OMD.
1567356	9	40	theme	Molecular	1203:1211	arg1	masses					1213:1218	Molecular masses	1203:1218	Molecular masses of the glycoforms	1203:1236	Molecular masses of the glycoforms were verified by matrix-assisted u.v. laser desorption mass spectrometry.
1567356	2	41	theme	complex	286:292	arg1	structures					294:303	these complex structures	280:303	these complex structures	280:303	Subfractionation of OMD into three molecular variants using concanavalin A lectin chromatography is based on variations in these complex structures.
1567356	3	42	theme	molecular	464:472	arg1	variants					474:481	its molecular variants	460:481	its molecular variants	460:481	Standard h.p.l.c. profiles have been developed to analyse the percentage and distribution of the glycoforms present at each glycosylation site in OMD and its molecular variants.
1567356	0	43	theme	sites	35:39	arg1	Analysis					0:7	Analysis	0:7	Analysis of the five glycosylation sites of human alpha 1-acid glycoprotein.	0:75	Analysis of the five glycosylation sites of human alpha 1-acid glycoprotein.
1567356	10	44	theme	carbohydrate	1466:1477	arg1	chains					1479:1484	the carbohydrate chains	1462:1484	the carbohydrate chains	1462:1484	On the basis of the site distribution of oligosaccharides in the variants, efforts were made to understand the factors that control the processing of the carbohydrate chains in OMD.
1567356	3	45	attach	present	414:420	arg1	site					444:447	each glycosylation site	425:447	each glycosylation site in OMD and its molecular variants	425:481	Standard h.p.l.c. profiles have been developed to analyse the percentage and distribution of the glycoforms present at each glycosylation site in OMD and its molecular variants.
1567356	3	45	attach	present	414:420	arg2	glycoforms					403:412	the glycoforms	399:412	the glycoforms present at each glycosylation site in OMD and its molecular variants	399:481	Standard h.p.l.c. profiles have been developed to analyse the percentage and distribution of the glycoforms present at each glycosylation site in OMD and its molecular variants.
1567356	2	46	theme	A	230:230	arg1	chromatography					239:252	concanavalin A lectin chromatography	217:252	concanavalin A lectin chromatography	217:252	Subfractionation of OMD into three molecular variants using concanavalin A lectin chromatography is based on variations in these complex structures.
1567356	7	47	theme	retained	1108:1115	arg1	variants					1117:1124	weakly retained variants	1101:1124	weakly retained variants	1101:1124	Only glycosylation site II of the five present is 100% biantennary in the retained and weakly retained variants.
1567356	0	48	theme	glycosylation	21:33	arg1	glycoprotein					63:74	human alpha 1-acid glycoprotein	44:74	human alpha 1-acid glycoprotein	44:74	Analysis of the five glycosylation sites of human alpha 1-acid glycoprotein.
1567356	0	48	theme	glycosylation	21:33	arg1	sites					35:39	the five glycosylation sites	12:39	the five glycosylation sites of human alpha 1-acid glycoprotein	12:74	Analysis of the five glycosylation sites of human alpha 1-acid glycoprotein.
1567356	7	49	from	the	1084:1086	arg1	biantennary					1069:1079	biantennary	1069:1079	biantennary	1069:1079	Only glycosylation site II of the five present is 100% biantennary in the retained and weakly retained variants.
1567356	11	50	theme	site-directed	1525:1537	arg1	model					1540:1544	the 'site-directed' model	1520:1544	the 'site-directed' model of processing	1520:1558	The results indicate that the 'site-directed' model of processing offers the most consistent explanation for the structures seen at the individual glycosylation sites of OMD.
1567356	11	51	theme	OMD	1664:1666	arg1	OMD					1664:1666	OMD	1664:1666	OMD	1664:1666	The results indicate that the 'site-directed' model of processing offers the most consistent explanation for the structures seen at the individual glycosylation sites of OMD.
1567356	11	51	theme	OMD	1664:1666	arg1	sites					1655:1659	the individual glycosylation sites	1626:1659	the individual glycosylation sites of OMD	1626:1666	The results indicate that the 'site-directed' model of processing offers the most consistent explanation for the structures seen at the individual glycosylation sites of OMD.
1567356	2	52	theme	concanavalin	217:228	arg1	chromatography					239:252	concanavalin A lectin chromatography	217:252	concanavalin A lectin chromatography	217:252	Subfractionation of OMD into three molecular variants using concanavalin A lectin chromatography is based on variations in these complex structures.
1567356	11	53	theme	consistent	1576:1585	arg1	explanation					1587:1597	the most consistent explanation	1567:1597	the most consistent explanation for the structures seen at the individual glycosylation sites of OMD	1567:1666	The results indicate that the 'site-directed' model of processing offers the most consistent explanation for the structures seen at the individual glycosylation sites of OMD.
1567356	0	54	theme	human	44:48	arg1	glycoprotein					63:74	human alpha 1-acid glycoprotein	44:74	human alpha 1-acid glycoprotein	44:74	Analysis of the five glycosylation sites of human alpha 1-acid glycoprotein.
1567356	4	55	theme	present	523:529	arg1	glycoforms					512:521	the glycoforms	508:521	the glycoforms present at each site	508:542	The ability to quantify the glycoforms present at each site allows us to extend the earlier results of others and resolve the remaining questions concerning the glycan structures of these variants.
1567356	5	56	theme	chains	751:756	arg1	proportions					706:716	the proportions	702:716	the proportions of bi-, tri- and tetra-antennary chains	702:756	Most significantly, the proportions of bi-, tri- and tetra-antennary chains differ at each site for the three molecular variants.
1567356	7	57	theme	Only	1014:1017	arg1	present					1053:1059	the five present	1044:1059	the five present	1044:1059	Only glycosylation site II of the five present is 100% biantennary in the retained and weakly retained variants.
1567356	7	57	theme	Only	1014:1017	arg1	site					1033:1036	Only glycosylation site II	1014:1039	Only glycosylation site II of the five present	1014:1059	Only glycosylation site II of the five present is 100% biantennary in the retained and weakly retained variants.
1567356	3	58	theme	glycoforms	403:412	arg1	distribution					383:394	distribution	383:394	distribution	383:394	Standard h.p.l.c. profiles have been developed to analyse the percentage and distribution of the glycoforms present at each glycosylation site in OMD and its molecular variants.
1567356	3	58	theme	glycoforms	403:412	arg1	percentage					368:377	percentage	368:377	percentage	368:377	Standard h.p.l.c. profiles have been developed to analyse the percentage and distribution of the glycoforms present at each glycosylation site in OMD and its molecular variants.
1567356	9	59	theme	glycoforms	1227:1236	arg1	masses					1213:1218	Molecular masses	1203:1218	Molecular masses of the glycoforms	1203:1236	Molecular masses of the glycoforms were verified by matrix-assisted u.v. laser desorption mass spectrometry.
1567356	3	60	theme	Standard	306:313	arg1	profiles					324:331	Standard h.p.l.c. profiles	306:331	Standard h.p.l.c. profiles	306:331	Standard h.p.l.c. profiles have been developed to analyse the percentage and distribution of the glycoforms present at each glycosylation site in OMD and its molecular variants.
1567356	2	61	theme	molecular	192:200	arg1	variants					202:209	three molecular variants	186:209	three molecular variants using concanavalin A lectin chromatography	186:252	Subfractionation of OMD into three molecular variants using concanavalin A lectin chromatography is based on variations in these complex structures.
1567356	9	62	theme	u.v.	1271:1274	arg1	spectrometry					1298:1309	matrix-assisted u.v. laser desorption mass spectrometry	1255:1309	matrix-assisted u.v. laser desorption mass spectrometry	1255:1309	Molecular masses of the glycoforms were verified by matrix-assisted u.v. laser desorption mass spectrometry.
1567356	1	63	theme	complex	104:110	arg1	bi-					112:114	complex bi-	104:114	complex bi-	104:114	Orosomucoid (OMD) contains complex bi-, tri- and tetra-antennary glycan chains.
1567356	2	64	from	variations	266:275	arg1	structures					294:303	these complex structures	280:303	these complex structures	280:303	Subfractionation of OMD into three molecular variants using concanavalin A lectin chromatography is based on variations in these complex structures.
1567356	10	65	from	processing	1448:1457	arg1	OMD					1489:1491	OMD	1489:1491	OMD	1489:1491	On the basis of the site distribution of oligosaccharides in the variants, efforts were made to understand the factors that control the processing of the carbohydrate chains in OMD.
1567356	7	66	theme	glycosylation	1019:1031	arg1	present					1053:1059	the five present	1044:1059	the five present	1044:1059	Only glycosylation site II of the five present is 100% biantennary in the retained and weakly retained variants.
1567356	7	66	theme	glycosylation	1019:1031	arg1	site					1033:1036	Only glycosylation site II	1014:1039	Only glycosylation site II of the five present	1014:1059	Only glycosylation site II of the five present is 100% biantennary in the retained and weakly retained variants.
1567356	0	67	gly	glycosylation	21:33	arg1	glycoprotein					63:74	human alpha 1-acid glycoprotein	44:74	human alpha 1-acid glycoprotein	44:74	Analysis of the five glycosylation sites of human alpha 1-acid glycoprotein.
1567356	0	67	gly	glycosylation	21:33	arg2	sites					35:39	the five glycosylation sites	12:39	the five glycosylation sites of human alpha 1-acid glycoprotein	12:74	Analysis of the five glycosylation sites of human alpha 1-acid glycoprotein.
1567356	0	67	gly	glycosylation	21:33	arg2	five					16:19	five	16:19	five	16:19	Analysis of the five glycosylation sites of human alpha 1-acid glycoprotein.
1567356	0	67	gly	glycosylation	21:33	arg2	glycoprotein					63:74	human alpha 1-acid glycoprotein	44:74	human alpha 1-acid glycoprotein	44:74	Analysis of the five glycosylation sites of human alpha 1-acid glycoprotein.
1567356	6	68	theme	biantennary	901:911	arg1	chains					913:918	biantennary chains	901:918	biantennary chains	901:918	The most strongly retained variant from concanavalin A is uniquely capable of possessing biantennary chains at all five sites, whereas the unretained variant is completely devoid of biantennary chains.
1567356	10	69	theme	oligosaccharides	1353:1368	arg1	distribution					1337:1348	the site distribution	1328:1348	the site distribution of oligosaccharides in the variants	1328:1384	On the basis of the site distribution of oligosaccharides in the variants, efforts were made to understand the factors that control the processing of the carbohydrate chains in OMD.
1567356	7	70	gly	glycosylation	1019:1031	arg2	present					1053:1059	the five present	1044:1059	the five present	1044:1059	Only glycosylation site II of the five present is 100% biantennary in the retained and weakly retained variants.
1567356	7	70	gly	glycosylation	1019:1031	arg1	present					1053:1059	the five present	1044:1059	the five present	1044:1059	Only glycosylation site II of the five present is 100% biantennary in the retained and weakly retained variants.
1567356	7	70	gly	glycosylation	1019:1031	arg2	site					1033:1036	Only glycosylation site II	1014:1039	Only glycosylation site II of the five present	1014:1059	Only glycosylation site II of the five present is 100% biantennary in the retained and weakly retained variants.
1567356	7	70	gly	glycosylation	1019:1031	arg2	II					1038:1039	II	1038:1039	II	1038:1039	Only glycosylation site II of the five present is 100% biantennary in the retained and weakly retained variants.
1567356	4	71	theme	others	587:592	arg1	results					576:582	the earlier results	564:582	the earlier results of others	564:592	The ability to quantify the glycoforms present at each site allows us to extend the earlier results of others and resolve the remaining questions concerning the glycan structures of these variants.
1567356	0	72	theme	1-acid	56:61	arg1	glycoprotein					63:74	human alpha 1-acid glycoprotein	44:74	human alpha 1-acid glycoprotein	44:74	Analysis of the five glycosylation sites of human alpha 1-acid glycoprotein.
1567356	2	73	theme	OMD	177:179	arg1	Subfractionation					157:172	Subfractionation	157:172	Subfractionation of OMD into three molecular variants using concanavalin A lectin chromatography	157:252	Subfractionation of OMD into three molecular variants using concanavalin A lectin chromatography is based on variations in these complex structures.
1567356	3	74	gly	glycosylation	430:442	arg2	site					444:447	each glycosylation site	425:447	each glycosylation site in OMD and its molecular variants	425:481	Standard h.p.l.c. profiles have been developed to analyse the percentage and distribution of the glycoforms present at each glycosylation site in OMD and its molecular variants.
1567356	6	75	theme	chains	1006:1011	arg1	devoid					984:989	devoid	984:989	devoid	984:989	The most strongly retained variant from concanavalin A is uniquely capable of possessing biantennary chains at all five sites, whereas the unretained variant is completely devoid of biantennary chains.
1567356	6	75	theme	chains	1006:1011	arg1	variant					962:968	the unretained variant	947:968	the unretained variant	947:968	The most strongly retained variant from concanavalin A is uniquely capable of possessing biantennary chains at all five sites, whereas the unretained variant is completely devoid of biantennary chains.
1567356	0	76	theme	alpha	50:54	arg1	glycoprotein					63:74	human alpha 1-acid glycoprotein	44:74	human alpha 1-acid glycoprotein	44:74	Analysis of the five glycosylation sites of human alpha 1-acid glycoprotein.
1567356	9	77	theme	laser	1276:1280	arg1	spectrometry					1298:1309	matrix-assisted u.v. laser desorption mass spectrometry	1255:1309	matrix-assisted u.v. laser desorption mass spectrometry	1255:1309	Molecular masses of the glycoforms were verified by matrix-assisted u.v. laser desorption mass spectrometry.
1567356	2	78	theme	lectin	232:237	arg1	chromatography					239:252	concanavalin A lectin chromatography	217:252	concanavalin A lectin chromatography	217:252	Subfractionation of OMD into three molecular variants using concanavalin A lectin chromatography is based on variations in these complex structures.
1567356	3	79	from	site	444:447	arg1	variants					474:481	its molecular variants	460:481	its molecular variants	460:481	Standard h.p.l.c. profiles have been developed to analyse the percentage and distribution of the glycoforms present at each glycosylation site in OMD and its molecular variants.
1567356	3	79	from	site	444:447	arg1	present					414:420	present	414:420	present	414:420	Standard h.p.l.c. profiles have been developed to analyse the percentage and distribution of the glycoforms present at each glycosylation site in OMD and its molecular variants.
1567356	3	79	from	site	444:447	arg1	OMD					452:454	OMD	452:454	OMD	452:454	Standard h.p.l.c. profiles have been developed to analyse the percentage and distribution of the glycoforms present at each glycosylation site in OMD and its molecular variants.
1567356	4	80	theme	variants	672:679	arg1	structures					652:661	the glycan structures	641:661	the glycan structures of these variants	641:679	The ability to quantify the glycoforms present at each site allows us to extend the earlier results of others and resolve the remaining questions concerning the glycan structures of these variants.
1567356	6	81	theme	biantennary	994:1004	arg1	chains					1006:1011	biantennary chains	994:1011	biantennary chains	994:1011	The most strongly retained variant from concanavalin A is uniquely capable of possessing biantennary chains at all five sites, whereas the unretained variant is completely devoid of biantennary chains.
1576999	5	0	theme	protein	627:633	arg1	O-D-mannosyltransferase					635:657	dolichyl-phosphate- D-mannose: protein O-D-mannosyltransferase	596:657	dolichyl-phosphate- D-mannose: protein O-D-mannosyltransferase (Man-transferase) of the yeast Saccharomyces cerevisiae	596:713	Two types of octapeptides encompassing residues 4-11 (peptide 4-11) and variants thereof, or residues 8-15 (peptide 8-15) of hGM-CSF were tested as substrates for in vitro O-glycosylation using dolichyl-phosphate- D-mannose: protein O-D-mannosyltransferase (Man-transferase) of the yeast Saccharomyces cerevisiae, or UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-transferase) of rat liver cells.
1576999	5	0	theme	protein	627:633	arg1	Man-transferase					660:674	Man-transferase	660:674	Man-transferase	660:674	Two types of octapeptides encompassing residues 4-11 (peptide 4-11) and variants thereof, or residues 8-15 (peptide 8-15) of hGM-CSF were tested as substrates for in vitro O-glycosylation using dolichyl-phosphate- D-mannose: protein O-D-mannosyltransferase (Man-transferase) of the yeast Saccharomyces cerevisiae, or UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-transferase) of rat liver cells.
1576999	8	1	theme	observed	1186:1193	arg1	differences					1195:1205	The observed differences	1182:1205	The observed differences in peptide-acceptor activities	1182:1236	The observed differences in peptide-acceptor activities indicate that the site of O-glycosylation depends on similar, but not identical protein structural features in yeast and mammalian cells.
1576999	8	2	theme	mammalian	1359:1367	arg1	cells					1369:1373	mammalian cells	1359:1373	mammalian cells	1359:1373	The observed differences in peptide-acceptor activities indicate that the site of O-glycosylation depends on similar, but not identical protein structural features in yeast and mammalian cells.
1576999	6	3	theme	reduced	944:950	arg1	efficiency					952:961	reduced efficiency	944:961	reduced efficiency	944:961	Peptide 8-15 was found to be O-glycosylated at residues Ser9 and Thr10 by GalNAc-transferase and, with reduced efficiency, also by Man-transferase.
1576999	8	4	theme	O-glycosylation	1264:1278	arg1	O-glycosylation					1264:1278	O-glycosylation	1264:1278	O-glycosylation	1264:1278	The observed differences in peptide-acceptor activities indicate that the site of O-glycosylation depends on similar, but not identical protein structural features in yeast and mammalian cells.
1576999	8	4	theme	O-glycosylation	1264:1278	arg1	site					1256:1259	the site	1252:1259	the site of O-glycosylation	1252:1278	The observed differences in peptide-acceptor activities indicate that the site of O-glycosylation depends on similar, but not identical protein structural features in yeast and mammalian cells.
1576999	1	5	theme	COS-1	305:309	arg1	cells					311:315	COS-1 cells	305:315	COS-1 cells	305:315	Human granulocyte-macrophage colony-stimulating factor (hGM-CSF) is O-glycosylated at residues Ser9 and Thr10 during secretion by yeast and COS-1 cells [Ernst, J.F., Mermod, J.-J.
1576999	5	6	theme	in	565:566	arg1	O-glycosylation					574:588	in vitro O-glycosylation	565:588	in vitro O-glycosylation using dolichyl-phosphate- D-mannose: protein O-D-mannosyltransferase (Man-transferase) of the yeast Saccharomyces cerevisiae, or UDP-N-acetyl-alpha-D-galactosamine	565:752	Two types of octapeptides encompassing residues 4-11 (peptide 4-11) and variants thereof, or residues 8-15 (peptide 8-15) of hGM-CSF were tested as substrates for in vitro O-glycosylation using dolichyl-phosphate- D-mannose: protein O-D-mannosyltransferase (Man-transferase) of the yeast Saccharomyces cerevisiae, or UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-transferase) of rat liver cells.
1576999	5	7	theme	octapeptides	415:426	arg1	substrates					550:559	substrates	550:559	substrates for in vitro O-glycosylation using dolichyl-phosphate- D-mannose: protein O-D-mannosyltransferase (Man-transferase) of the yeast Saccharomyces cerevisiae, or UDP-N-acetyl-alpha-D-galactosamine	550:752	Two types of octapeptides encompassing residues 4-11 (peptide 4-11) and variants thereof, or residues 8-15 (peptide 8-15) of hGM-CSF were tested as substrates for in vitro O-glycosylation using dolichyl-phosphate- D-mannose: protein O-D-mannosyltransferase (Man-transferase) of the yeast Saccharomyces cerevisiae, or UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-transferase) of rat liver cells.
1576999	5	7	theme	octapeptides	415:426	arg1	types					406:410	Two types	402:410	Two types of octapeptides encompassing residues 4-11 (peptide 4-11) and variants thereof, or residues 8-15 (peptide 8-15) of hGM-CSF	402:533	Two types of octapeptides encompassing residues 4-11 (peptide 4-11) and variants thereof, or residues 8-15 (peptide 8-15) of hGM-CSF were tested as substrates for in vitro O-glycosylation using dolichyl-phosphate- D-mannose: protein O-D-mannosyltransferase (Man-transferase) of the yeast Saccharomyces cerevisiae, or UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-transferase) of rat liver cells.
1576999	0	8	theme	yeast	138:142	arg1	O-glycosyltransferases					112:133	O-glycosyltransferases	112:133	O-glycosyltransferases of yeast and rat liver cells	112:162	Specific in vitro O-glycosylation of human granulocyte-macrophage colony-stimulating-factor-derived peptides by O-glycosyltransferases of yeast and rat liver cells.
1576999	1	9	gly	O-glycosylated	233:246	arg2	Thr10					269:273	Thr10	269:273	Thr10	269:273	Human granulocyte-macrophage colony-stimulating factor (hGM-CSF) is O-glycosylated at residues Ser9 and Thr10 during secretion by yeast and COS-1 cells [Ernst, J.F., Mermod, J.-J.
1576999	1	9	gly	O-glycosylated	233:246	arg1	factor					213:218	Human granulocyte-macrophage colony-stimulating factor	165:218	Human granulocyte-macrophage colony-stimulating factor (hGM-CSF)	165:228	Human granulocyte-macrophage colony-stimulating factor (hGM-CSF) is O-glycosylated at residues Ser9 and Thr10 during secretion by yeast and COS-1 cells [Ernst, J.F., Mermod, J.-J.
1576999	1	9	gly	O-glycosylated	233:246	arg2	Ser9					260:263	Ser9	260:263	Ser9	260:263	Human granulocyte-macrophage colony-stimulating factor (hGM-CSF) is O-glycosylated at residues Ser9 and Thr10 during secretion by yeast and COS-1 cells [Ernst, J.F., Mermod, J.-J.
1576999	1	9	gly	O-glycosylated	233:246	arg2	residues					251:258	residues Ser9 and Thr10	251:273	residues Ser9 and Thr10	251:273	Human granulocyte-macrophage colony-stimulating factor (hGM-CSF) is O-glycosylated at residues Ser9 and Thr10 during secretion by yeast and COS-1 cells [Ernst, J.F., Mermod, J.-J.
1576999	1	9	gly	O-glycosylated	233:246	arg1	hGM-CSF					221:227	hGM-CSF	221:227	hGM-CSF	221:227	Human granulocyte-macrophage colony-stimulating factor (hGM-CSF) is O-glycosylated at residues Ser9 and Thr10 during secretion by yeast and COS-1 cells [Ernst, J.F., Mermod, J.-J.
1576999	6	10	gly	O-glycosylated	870:883	arg2	Thr10					906:910	Thr10	906:910	Thr10	906:910	Peptide 8-15 was found to be O-glycosylated at residues Ser9 and Thr10 by GalNAc-transferase and, with reduced efficiency, also by Man-transferase.
1576999	6	10	gly	O-glycosylated	870:883	arg2	Ser9					897:900	Ser9	897:900	Ser9	897:900	Peptide 8-15 was found to be O-glycosylated at residues Ser9 and Thr10 by GalNAc-transferase and, with reduced efficiency, also by Man-transferase.
1576999	6	10	gly	O-glycosylated	870:883	arg2	residues					888:895	residues Ser9 and Thr10	888:910	residues Ser9 and Thr10	888:910	Peptide 8-15 was found to be O-glycosylated at residues Ser9 and Thr10 by GalNAc-transferase and, with reduced efficiency, also by Man-transferase.
1576999	7	11	gly	mannosylation	1061:1073	arg1	Thr10					1083:1087	only Thr10	1078:1087	only Thr10	1078:1087	Peptide 4-11 was a good substrate for yeast Man-transferase, leading to mannosylation of only Thr10, whereas it was very poorly O-glycosylated at positions Ser5 and Ser7 by GalNAc-transferase.
1576999	0	12	theme	liver	152:156	arg1	cells					158:162	rat liver cells	148:162	rat liver cells	148:162	Specific in vitro O-glycosylation of human granulocyte-macrophage colony-stimulating-factor-derived peptides by O-glycosyltransferases of yeast and rat liver cells.
1576999	8	13	theme	peptide-acceptor	1210:1225	arg1	activities					1227:1236	peptide-acceptor activities	1210:1236	peptide-acceptor activities	1210:1236	The observed differences in peptide-acceptor activities indicate that the site of O-glycosylation depends on similar, but not identical protein structural features in yeast and mammalian cells.
1576999	8	14	from	features	1337:1344	arg1	yeast					1349:1353	yeast	1349:1353	yeast	1349:1353	The observed differences in peptide-acceptor activities indicate that the site of O-glycosylation depends on similar, but not identical protein structural features in yeast and mammalian cells.
1576999	8	14	from	features	1337:1344	arg1	cells					1369:1373	mammalian cells	1359:1373	mammalian cells	1359:1373	The observed differences in peptide-acceptor activities indicate that the site of O-glycosylation depends on similar, but not identical protein structural features in yeast and mammalian cells.
1576999	8	15	theme	similar	1291:1297	arg1	features					1337:1344	similar, but not identical protein structural features	1291:1344	similar, but not identical protein structural features in yeast and mammalian cells	1291:1373	The observed differences in peptide-acceptor activities indicate that the site of O-glycosylation depends on similar, but not identical protein structural features in yeast and mammalian cells.
1576999	0	16	theme	rat	148:150	arg1	cells					158:162	rat liver cells	148:162	rat liver cells	148:162	Specific in vitro O-glycosylation of human granulocyte-macrophage colony-stimulating-factor-derived peptides by O-glycosyltransferases of yeast and rat liver cells.
1576999	5	17	theme	rat	824:826	arg1	cells					834:838	rat liver cells	824:838	rat liver cells	824:838	Two types of octapeptides encompassing residues 4-11 (peptide 4-11) and variants thereof, or residues 8-15 (peptide 8-15) of hGM-CSF were tested as substrates for in vitro O-glycosylation using dolichyl-phosphate- D-mannose: protein O-D-mannosyltransferase (Man-transferase) of the yeast Saccharomyces cerevisiae, or UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-transferase) of rat liver cells.
1576999	0	18	link	colony-stimulating-factor-derived	66:98	arg1	peptides					100:107	human granulocyte-macrophage colony-stimulating-factor-derived peptides	37:107	human granulocyte-macrophage colony-stimulating-factor-derived peptides	37:107	Specific in vitro O-glycosylation of human granulocyte-macrophage colony-stimulating-factor-derived peptides by O-glycosyltransferases of yeast and rat liver cells.
1576999	6	19	from	residues	888:895	arg1	O-glycosylated					870:883	O-glycosylated	870:883	O-glycosylated	870:883	Peptide 8-15 was found to be O-glycosylated at residues Ser9 and Thr10 by GalNAc-transferase and, with reduced efficiency, also by Man-transferase.
1576999	5	20	theme	polypeptide	754:764	arg1	GalNAc-transferase					801:818	GalNAc-transferase	801:818	GalNAc-transferase	801:818	Two types of octapeptides encompassing residues 4-11 (peptide 4-11) and variants thereof, or residues 8-15 (peptide 8-15) of hGM-CSF were tested as substrates for in vitro O-glycosylation using dolichyl-phosphate- D-mannose: protein O-D-mannosyltransferase (Man-transferase) of the yeast Saccharomyces cerevisiae, or UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-transferase) of rat liver cells.
1576999	5	20	theme	polypeptide	754:764	arg1	N-acetylgalactosaminyltransferase					766:798	polypeptide N-acetylgalactosaminyltransferase	754:798	polypeptide N-acetylgalactosaminyltransferase (GalNAc-transferase) of rat liver cells	754:838	Two types of octapeptides encompassing residues 4-11 (peptide 4-11) and variants thereof, or residues 8-15 (peptide 8-15) of hGM-CSF were tested as substrates for in vitro O-glycosylation using dolichyl-phosphate- D-mannose: protein O-D-mannosyltransferase (Man-transferase) of the yeast Saccharomyces cerevisiae, or UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-transferase) of rat liver cells.
1576999	0	21	theme	in	9:10	arg1	O-glycosylation					18:32	Specific in vitro O-glycosylation	0:32	Specific in vitro O-glycosylation of human granulocyte-macrophage colony-stimulating-factor-derived peptides by O-glycosyltransferases of yeast and rat liver cells.	0:163	Specific in vitro O-glycosylation of human granulocyte-macrophage colony-stimulating-factor-derived peptides by O-glycosyltransferases of yeast and rat liver cells.
1576999	5	22	theme	D-mannose	616:624	arg1	O-D-mannosyltransferase					635:657	dolichyl-phosphate- D-mannose: protein O-D-mannosyltransferase	596:657	dolichyl-phosphate- D-mannose: protein O-D-mannosyltransferase (Man-transferase) of the yeast Saccharomyces cerevisiae	596:713	Two types of octapeptides encompassing residues 4-11 (peptide 4-11) and variants thereof, or residues 8-15 (peptide 8-15) of hGM-CSF were tested as substrates for in vitro O-glycosylation using dolichyl-phosphate- D-mannose: protein O-D-mannosyltransferase (Man-transferase) of the yeast Saccharomyces cerevisiae, or UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-transferase) of rat liver cells.
1576999	5	22	theme	D-mannose	616:624	arg1	Man-transferase					660:674	Man-transferase	660:674	Man-transferase	660:674	Two types of octapeptides encompassing residues 4-11 (peptide 4-11) and variants thereof, or residues 8-15 (peptide 8-15) of hGM-CSF were tested as substrates for in vitro O-glycosylation using dolichyl-phosphate- D-mannose: protein O-D-mannosyltransferase (Man-transferase) of the yeast Saccharomyces cerevisiae, or UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-transferase) of rat liver cells.
1576999	5	23	theme	dolichyl-phosphate-	596:614	arg1	O-D-mannosyltransferase					635:657	dolichyl-phosphate- D-mannose: protein O-D-mannosyltransferase	596:657	dolichyl-phosphate- D-mannose: protein O-D-mannosyltransferase (Man-transferase) of the yeast Saccharomyces cerevisiae	596:713	Two types of octapeptides encompassing residues 4-11 (peptide 4-11) and variants thereof, or residues 8-15 (peptide 8-15) of hGM-CSF were tested as substrates for in vitro O-glycosylation using dolichyl-phosphate- D-mannose: protein O-D-mannosyltransferase (Man-transferase) of the yeast Saccharomyces cerevisiae, or UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-transferase) of rat liver cells.
1576999	5	23	theme	dolichyl-phosphate-	596:614	arg1	Man-transferase					660:674	Man-transferase	660:674	Man-transferase	660:674	Two types of octapeptides encompassing residues 4-11 (peptide 4-11) and variants thereof, or residues 8-15 (peptide 8-15) of hGM-CSF were tested as substrates for in vitro O-glycosylation using dolichyl-phosphate- D-mannose: protein O-D-mannosyltransferase (Man-transferase) of the yeast Saccharomyces cerevisiae, or UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-transferase) of rat liver cells.
1576999	0	24	theme	Specific	0:7	arg1	O-glycosylation					18:32	Specific in vitro O-glycosylation	0:32	Specific in vitro O-glycosylation of human granulocyte-macrophage colony-stimulating-factor-derived peptides by O-glycosyltransferases of yeast and rat liver cells.	0:163	Specific in vitro O-glycosylation of human granulocyte-macrophage colony-stimulating-factor-derived peptides by O-glycosyltransferases of yeast and rat liver cells.
1576999	8	25	gly	O-glycosylation	1264:1278	arg2	O-glycosylation					1264:1278	O-glycosylation	1264:1278	O-glycosylation	1264:1278	The observed differences in peptide-acceptor activities indicate that the site of O-glycosylation depends on similar, but not identical protein structural features in yeast and mammalian cells.
1576999	8	25	gly	O-glycosylation	1264:1278	arg2	site					1256:1259	the site	1252:1259	the site of O-glycosylation	1252:1278	The observed differences in peptide-acceptor activities indicate that the site of O-glycosylation depends on similar, but not identical protein structural features in yeast and mammalian cells.
1576999	0	26	dep	in	9:10	arg1	vitro					12:16	vitro	12:16	vitro	12:16	Specific in vitro O-glycosylation of human granulocyte-macrophage colony-stimulating-factor-derived peptides by O-glycosyltransferases of yeast and rat liver cells.
1576999	5	27	theme	Saccharomyces	690:702	arg1	yeast					684:688	the yeast Saccharomyces cerevisiae	680:713	the yeast Saccharomyces cerevisiae	680:713	Two types of octapeptides encompassing residues 4-11 (peptide 4-11) and variants thereof, or residues 8-15 (peptide 8-15) of hGM-CSF were tested as substrates for in vitro O-glycosylation using dolichyl-phosphate- D-mannose: protein O-D-mannosyltransferase (Man-transferase) of the yeast Saccharomyces cerevisiae, or UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-transferase) of rat liver cells.
1576999	5	28	theme	cells	834:838	arg1	GalNAc-transferase					801:818	GalNAc-transferase	801:818	GalNAc-transferase	801:818	Two types of octapeptides encompassing residues 4-11 (peptide 4-11) and variants thereof, or residues 8-15 (peptide 8-15) of hGM-CSF were tested as substrates for in vitro O-glycosylation using dolichyl-phosphate- D-mannose: protein O-D-mannosyltransferase (Man-transferase) of the yeast Saccharomyces cerevisiae, or UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-transferase) of rat liver cells.
1576999	5	28	theme	cells	834:838	arg1	N-acetylgalactosaminyltransferase					766:798	polypeptide N-acetylgalactosaminyltransferase	754:798	polypeptide N-acetylgalactosaminyltransferase (GalNAc-transferase) of rat liver cells	754:838	Two types of octapeptides encompassing residues 4-11 (peptide 4-11) and variants thereof, or residues 8-15 (peptide 8-15) of hGM-CSF were tested as substrates for in vitro O-glycosylation using dolichyl-phosphate- D-mannose: protein O-D-mannosyltransferase (Man-transferase) of the yeast Saccharomyces cerevisiae, or UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-transferase) of rat liver cells.
1576999	7	29	dep	substrate	1013:1021	arg1	whereas					1090:1096	whereas	1090:1096	whereas	1090:1096	Peptide 4-11 was a good substrate for yeast Man-transferase, leading to mannosylation of only Thr10, whereas it was very poorly O-glycosylated at positions Ser5 and Ser7 by GalNAc-transferase.
1576999	8	30	theme	identical	1308:1316	arg1	features					1337:1344	similar, but not identical protein structural features	1291:1344	similar, but not identical protein structural features in yeast and mammalian cells	1291:1373	The observed differences in peptide-acceptor activities indicate that the site of O-glycosylation depends on similar, but not identical protein structural features in yeast and mammalian cells.
1576999	0	31	theme	cells	158:162	arg1	O-glycosyltransferases					112:133	O-glycosyltransferases	112:133	O-glycosyltransferases of yeast and rat liver cells	112:162	Specific in vitro O-glycosylation of human granulocyte-macrophage colony-stimulating-factor-derived peptides by O-glycosyltransferases of yeast and rat liver cells.
1576999	5	32	dep	residues	495:502	arg1	8-15					504:507	8-15	504:507	8-15	504:507	Two types of octapeptides encompassing residues 4-11 (peptide 4-11) and variants thereof, or residues 8-15 (peptide 8-15) of hGM-CSF were tested as substrates for in vitro O-glycosylation using dolichyl-phosphate- D-mannose: protein O-D-mannosyltransferase (Man-transferase) of the yeast Saccharomyces cerevisiae, or UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-transferase) of rat liver cells.
1576999	0	33	theme	human	37:41	arg1	peptides					100:107	human granulocyte-macrophage colony-stimulating-factor-derived peptides	37:107	human granulocyte-macrophage colony-stimulating-factor-derived peptides	37:107	Specific in vitro O-glycosylation of human granulocyte-macrophage colony-stimulating-factor-derived peptides by O-glycosyltransferases of yeast and rat liver cells.
1576999	1	34	dep	yeast	295:299	arg1	J.-J					339:342	J.-J	339:342	J.-J	339:342	Human granulocyte-macrophage colony-stimulating factor (hGM-CSF) is O-glycosylated at residues Ser9 and Thr10 during secretion by yeast and COS-1 cells [Ernst, J.F., Mermod, J.-J.
1576999	1	34	dep	yeast	295:299	arg1	Mermod					331:336	Mermod	331:336	Mermod	331:336	Human granulocyte-macrophage colony-stimulating factor (hGM-CSF) is O-glycosylated at residues Ser9 and Thr10 during secretion by yeast and COS-1 cells [Ernst, J.F., Mermod, J.-J.
1576999	1	34	dep	yeast	295:299	arg1	[Ernst					317:322	[Ernst	317:322	[Ernst	317:322	Human granulocyte-macrophage colony-stimulating factor (hGM-CSF) is O-glycosylated at residues Ser9 and Thr10 during secretion by yeast and COS-1 cells [Ernst, J.F., Mermod, J.-J.
1576999	8	35	theme	structural	1326:1335	arg1	features					1337:1344	similar, but not identical protein structural features	1291:1344	similar, but not identical protein structural features in yeast and mammalian cells	1291:1373	The observed differences in peptide-acceptor activities indicate that the site of O-glycosylation depends on similar, but not identical protein structural features in yeast and mammalian cells.
1576999	5	36	theme	liver	828:832	arg1	cells					834:838	rat liver cells	824:838	rat liver cells	824:838	Two types of octapeptides encompassing residues 4-11 (peptide 4-11) and variants thereof, or residues 8-15 (peptide 8-15) of hGM-CSF were tested as substrates for in vitro O-glycosylation using dolichyl-phosphate- D-mannose: protein O-D-mannosyltransferase (Man-transferase) of the yeast Saccharomyces cerevisiae, or UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-transferase) of rat liver cells.
1576999	7	37	from	positions	1135:1143	arg1	O-glycosylated					1117:1130	O-glycosylated	1117:1130	O-glycosylated	1117:1130	Peptide 4-11 was a good substrate for yeast Man-transferase, leading to mannosylation of only Thr10, whereas it was very poorly O-glycosylated at positions Ser5 and Ser7 by GalNAc-transferase.
1576999	6	38	with	O-glycosylated	870:883	arg1	efficiency					952:961	reduced efficiency	944:961	reduced efficiency	944:961	Peptide 8-15 was found to be O-glycosylated at residues Ser9 and Thr10 by GalNAc-transferase and, with reduced efficiency, also by Man-transferase.
1576999	0	39	theme	colony-stimulating-factor-derived	66:98	arg1	peptides					100:107	human granulocyte-macrophage colony-stimulating-factor-derived peptides	37:107	human granulocyte-macrophage colony-stimulating-factor-derived peptides	37:107	Specific in vitro O-glycosylation of human granulocyte-macrophage colony-stimulating-factor-derived peptides by O-glycosyltransferases of yeast and rat liver cells.
1576999	6	40	dep	residues	888:895	arg1	Ser9					897:900	Ser9	897:900	Ser9	897:900	Peptide 8-15 was found to be O-glycosylated at residues Ser9 and Thr10 by GalNAc-transferase and, with reduced efficiency, also by Man-transferase.
1576999	6	40	dep	residues	888:895	arg1	residues					888:895	residues Ser9 and Thr10	888:910	residues Ser9 and Thr10	888:910	Peptide 8-15 was found to be O-glycosylated at residues Ser9 and Thr10 by GalNAc-transferase and, with reduced efficiency, also by Man-transferase.
1576999	6	40	dep	residues	888:895	arg1	Thr10					906:910	Thr10	906:910	Thr10	906:910	Peptide 8-15 was found to be O-glycosylated at residues Ser9 and Thr10 by GalNAc-transferase and, with reduced efficiency, also by Man-transferase.
1576999	7	41	theme	only	1078:1081	arg1	Thr10					1083:1087	only Thr10	1078:1087	only Thr10	1078:1087	Peptide 4-11 was a good substrate for yeast Man-transferase, leading to mannosylation of only Thr10, whereas it was very poorly O-glycosylated at positions Ser5 and Ser7 by GalNAc-transferase.
1576999	0	42	theme	granulocyte-macrophage	43:64	arg1	peptides					100:107	human granulocyte-macrophage colony-stimulating-factor-derived peptides	37:107	human granulocyte-macrophage colony-stimulating-factor-derived peptides	37:107	Specific in vitro O-glycosylation of human granulocyte-macrophage colony-stimulating-factor-derived peptides by O-glycosyltransferases of yeast and rat liver cells.
1576999	7	43	theme	Thr10	1083:1087	arg1	mannosylation					1061:1073	mannosylation	1061:1073	mannosylation of only Thr10	1061:1087	Peptide 4-11 was a good substrate for yeast Man-transferase, leading to mannosylation of only Thr10, whereas it was very poorly O-glycosylated at positions Ser5 and Ser7 by GalNAc-transferase.
1576999	0	44	gly	O-glycosylation	18:32	arg1	peptides					100:107	human granulocyte-macrophage colony-stimulating-factor-derived peptides	37:107	human granulocyte-macrophage colony-stimulating-factor-derived peptides	37:107	Specific in vitro O-glycosylation of human granulocyte-macrophage colony-stimulating-factor-derived peptides by O-glycosyltransferases of yeast and rat liver cells.
1576999	1	45	from	residues	251:258	arg1	O-glycosylated					233:246	O-glycosylated	233:246	O-glycosylated	233:246	Human granulocyte-macrophage colony-stimulating factor (hGM-CSF) is O-glycosylated at residues Ser9 and Thr10 during secretion by yeast and COS-1 cells [Ernst, J.F., Mermod, J.-J.
1576999	5	46	theme	hGM-CSF	527:533	arg1	peptide					456:462	peptide 4-11	456:467	peptide 4-11	456:467	Two types of octapeptides encompassing residues 4-11 (peptide 4-11) and variants thereof, or residues 8-15 (peptide 8-15) of hGM-CSF were tested as substrates for in vitro O-glycosylation using dolichyl-phosphate- D-mannose: protein O-D-mannosyltransferase (Man-transferase) of the yeast Saccharomyces cerevisiae, or UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-transferase) of rat liver cells.
1576999	5	46	theme	hGM-CSF	527:533	arg1	hGM-CSF					527:533	hGM-CSF	527:533	hGM-CSF	527:533	Two types of octapeptides encompassing residues 4-11 (peptide 4-11) and variants thereof, or residues 8-15 (peptide 8-15) of hGM-CSF were tested as substrates for in vitro O-glycosylation using dolichyl-phosphate- D-mannose: protein O-D-mannosyltransferase (Man-transferase) of the yeast Saccharomyces cerevisiae, or UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-transferase) of rat liver cells.
1576999	5	46	theme	hGM-CSF	527:533	arg1	residues					495:502	residues 8-15	495:507	residues 8-15 (peptide 8-15) of hGM-CSF	495:533	Two types of octapeptides encompassing residues 4-11 (peptide 4-11) and variants thereof, or residues 8-15 (peptide 8-15) of hGM-CSF were tested as substrates for in vitro O-glycosylation using dolichyl-phosphate- D-mannose: protein O-D-mannosyltransferase (Man-transferase) of the yeast Saccharomyces cerevisiae, or UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-transferase) of rat liver cells.
1576999	5	46	theme	hGM-CSF	527:533	arg1	residues					441:448	residues 4-11	441:453	residues 4-11 (peptide 4-11)	441:468	Two types of octapeptides encompassing residues 4-11 (peptide 4-11) and variants thereof, or residues 8-15 (peptide 8-15) of hGM-CSF were tested as substrates for in vitro O-glycosylation using dolichyl-phosphate- D-mannose: protein O-D-mannosyltransferase (Man-transferase) of the yeast Saccharomyces cerevisiae, or UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-transferase) of rat liver cells.
1576999	5	46	theme	hGM-CSF	527:533	arg1	peptide					510:516	peptide 8-15	510:521	peptide 8-15	510:521	Two types of octapeptides encompassing residues 4-11 (peptide 4-11) and variants thereof, or residues 8-15 (peptide 8-15) of hGM-CSF were tested as substrates for in vitro O-glycosylation using dolichyl-phosphate- D-mannose: protein O-D-mannosyltransferase (Man-transferase) of the yeast Saccharomyces cerevisiae, or UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-transferase) of rat liver cells.
1576999	5	46	theme	hGM-CSF	527:533	arg1	variants					474:481	variants	474:481	variants thereof	474:489	Two types of octapeptides encompassing residues 4-11 (peptide 4-11) and variants thereof, or residues 8-15 (peptide 8-15) of hGM-CSF were tested as substrates for in vitro O-glycosylation using dolichyl-phosphate- D-mannose: protein O-D-mannosyltransferase (Man-transferase) of the yeast Saccharomyces cerevisiae, or UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-transferase) of rat liver cells.
1576999	1	47	theme	Human	165:169	arg1	factor					213:218	Human granulocyte-macrophage colony-stimulating factor	165:218	Human granulocyte-macrophage colony-stimulating factor (hGM-CSF)	165:228	Human granulocyte-macrophage colony-stimulating factor (hGM-CSF) is O-glycosylated at residues Ser9 and Thr10 during secretion by yeast and COS-1 cells [Ernst, J.F., Mermod, J.-J.
1576999	1	47	theme	Human	165:169	arg1	hGM-CSF					221:227	hGM-CSF	221:227	hGM-CSF	221:227	Human granulocyte-macrophage colony-stimulating factor (hGM-CSF) is O-glycosylated at residues Ser9 and Thr10 during secretion by yeast and COS-1 cells [Ernst, J.F., Mermod, J.-J.
1576999	8	48	theme	protein	1318:1324	arg1	features					1337:1344	similar, but not identical protein structural features	1291:1344	similar, but not identical protein structural features in yeast and mammalian cells	1291:1373	The observed differences in peptide-acceptor activities indicate that the site of O-glycosylation depends on similar, but not identical protein structural features in yeast and mammalian cells.
1576999	5	49	theme	yeast	684:688	arg1	O-D-mannosyltransferase					635:657	dolichyl-phosphate- D-mannose: protein O-D-mannosyltransferase	596:657	dolichyl-phosphate- D-mannose: protein O-D-mannosyltransferase (Man-transferase) of the yeast Saccharomyces cerevisiae	596:713	Two types of octapeptides encompassing residues 4-11 (peptide 4-11) and variants thereof, or residues 8-15 (peptide 8-15) of hGM-CSF were tested as substrates for in vitro O-glycosylation using dolichyl-phosphate- D-mannose: protein O-D-mannosyltransferase (Man-transferase) of the yeast Saccharomyces cerevisiae, or UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-transferase) of rat liver cells.
1576999	5	49	theme	yeast	684:688	arg1	UDP-N-acetyl-alpha-D-galactosamine					719:752	UDP-N-acetyl-alpha-D-galactosamine	719:752	UDP-N-acetyl-alpha-D-galactosamine	719:752	Two types of octapeptides encompassing residues 4-11 (peptide 4-11) and variants thereof, or residues 8-15 (peptide 8-15) of hGM-CSF were tested as substrates for in vitro O-glycosylation using dolichyl-phosphate- D-mannose: protein O-D-mannosyltransferase (Man-transferase) of the yeast Saccharomyces cerevisiae, or UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-transferase) of rat liver cells.
1576999	5	49	theme	yeast	684:688	arg1	Man-transferase					660:674	Man-transferase	660:674	Man-transferase	660:674	Two types of octapeptides encompassing residues 4-11 (peptide 4-11) and variants thereof, or residues 8-15 (peptide 8-15) of hGM-CSF were tested as substrates for in vitro O-glycosylation using dolichyl-phosphate- D-mannose: protein O-D-mannosyltransferase (Man-transferase) of the yeast Saccharomyces cerevisiae, or UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-transferase) of rat liver cells.
1576999	8	50	from	differences	1195:1205	arg1	activities					1227:1236	peptide-acceptor activities	1210:1236	peptide-acceptor activities	1210:1236	The observed differences in peptide-acceptor activities indicate that the site of O-glycosylation depends on similar, but not identical protein structural features in yeast and mammalian cells.
1576999	7	51	gly	O-glycosylated	1117:1130	arg2	Ser7					1154:1157	Ser7	1154:1157	Ser7	1154:1157	Peptide 4-11 was a good substrate for yeast Man-transferase, leading to mannosylation of only Thr10, whereas it was very poorly O-glycosylated at positions Ser5 and Ser7 by GalNAc-transferase.
1576999	7	51	gly	O-glycosylated	1117:1130	arg2	Ser5					1145:1148	Ser5	1145:1148	Ser5	1145:1148	Peptide 4-11 was a good substrate for yeast Man-transferase, leading to mannosylation of only Thr10, whereas it was very poorly O-glycosylated at positions Ser5 and Ser7 by GalNAc-transferase.
1576999	7	51	gly	O-glycosylated	1117:1130	arg1	it					1098:1099	it	1098:1099	it	1098:1099	Peptide 4-11 was a good substrate for yeast Man-transferase, leading to mannosylation of only Thr10, whereas it was very poorly O-glycosylated at positions Ser5 and Ser7 by GalNAc-transferase.
1576999	7	51	gly	O-glycosylated	1117:1130	arg2	positions					1135:1143	positions Ser5 and Ser7	1135:1157	positions Ser5 and Ser7	1135:1157	Peptide 4-11 was a good substrate for yeast Man-transferase, leading to mannosylation of only Thr10, whereas it was very poorly O-glycosylated at positions Ser5 and Ser7 by GalNAc-transferase.
1576999	1	52	theme	granulocyte-macrophage	171:192	arg1	factor					213:218	Human granulocyte-macrophage colony-stimulating factor	165:218	Human granulocyte-macrophage colony-stimulating factor (hGM-CSF)	165:228	Human granulocyte-macrophage colony-stimulating factor (hGM-CSF) is O-glycosylated at residues Ser9 and Thr10 during secretion by yeast and COS-1 cells [Ernst, J.F., Mermod, J.-J.
1576999	1	52	theme	granulocyte-macrophage	171:192	arg1	hGM-CSF					221:227	hGM-CSF	221:227	hGM-CSF	221:227	Human granulocyte-macrophage colony-stimulating factor (hGM-CSF) is O-glycosylated at residues Ser9 and Thr10 during secretion by yeast and COS-1 cells [Ernst, J.F., Mermod, J.-J.
1576999	5	53	dep	tested	540:545	arg1	GalNAc-transferase					801:818	GalNAc-transferase	801:818	GalNAc-transferase	801:818	Two types of octapeptides encompassing residues 4-11 (peptide 4-11) and variants thereof, or residues 8-15 (peptide 8-15) of hGM-CSF were tested as substrates for in vitro O-glycosylation using dolichyl-phosphate- D-mannose: protein O-D-mannosyltransferase (Man-transferase) of the yeast Saccharomyces cerevisiae, or UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-transferase) of rat liver cells.
1576999	5	53	dep	tested	540:545	arg1	N-acetylgalactosaminyltransferase					766:798	polypeptide N-acetylgalactosaminyltransferase	754:798	polypeptide N-acetylgalactosaminyltransferase (GalNAc-transferase) of rat liver cells	754:838	Two types of octapeptides encompassing residues 4-11 (peptide 4-11) and variants thereof, or residues 8-15 (peptide 8-15) of hGM-CSF were tested as substrates for in vitro O-glycosylation using dolichyl-phosphate- D-mannose: protein O-D-mannosyltransferase (Man-transferase) of the yeast Saccharomyces cerevisiae, or UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-transferase) of rat liver cells.
1576999	1	54	dep	residues	251:258	arg1	Ser9					260:263	Ser9	260:263	Ser9	260:263	Human granulocyte-macrophage colony-stimulating factor (hGM-CSF) is O-glycosylated at residues Ser9 and Thr10 during secretion by yeast and COS-1 cells [Ernst, J.F., Mermod, J.-J.
1576999	1	54	dep	residues	251:258	arg1	residues					251:258	residues Ser9 and Thr10	251:273	residues Ser9 and Thr10	251:273	Human granulocyte-macrophage colony-stimulating factor (hGM-CSF) is O-glycosylated at residues Ser9 and Thr10 during secretion by yeast and COS-1 cells [Ernst, J.F., Mermod, J.-J.
1576999	1	54	dep	residues	251:258	arg1	Thr10					269:273	Thr10	269:273	Thr10	269:273	Human granulocyte-macrophage colony-stimulating factor (hGM-CSF) is O-glycosylated at residues Ser9 and Thr10 during secretion by yeast and COS-1 cells [Ernst, J.F., Mermod, J.-J.
1576999	7	55	theme	yeast	1027:1031	arg1	Man-transferase					1033:1047	yeast Man-transferase	1027:1047	yeast Man-transferase	1027:1047	Peptide 4-11 was a good substrate for yeast Man-transferase, leading to mannosylation of only Thr10, whereas it was very poorly O-glycosylated at positions Ser5 and Ser7 by GalNAc-transferase.
1576999	1	56	theme	colony-stimulating	194:211	arg1	factor					213:218	Human granulocyte-macrophage colony-stimulating factor	165:218	Human granulocyte-macrophage colony-stimulating factor (hGM-CSF)	165:228	Human granulocyte-macrophage colony-stimulating factor (hGM-CSF) is O-glycosylated at residues Ser9 and Thr10 during secretion by yeast and COS-1 cells [Ernst, J.F., Mermod, J.-J.
1576999	1	56	theme	colony-stimulating	194:211	arg1	hGM-CSF					221:227	hGM-CSF	221:227	hGM-CSF	221:227	Human granulocyte-macrophage colony-stimulating factor (hGM-CSF) is O-glycosylated at residues Ser9 and Thr10 during secretion by yeast and COS-1 cells [Ernst, J.F., Mermod, J.-J.
1576999	5	57	dep	in	565:566	arg1	vitro					568:572	vitro	568:572	vitro	568:572	Two types of octapeptides encompassing residues 4-11 (peptide 4-11) and variants thereof, or residues 8-15 (peptide 8-15) of hGM-CSF were tested as substrates for in vitro O-glycosylation using dolichyl-phosphate- D-mannose: protein O-D-mannosyltransferase (Man-transferase) of the yeast Saccharomyces cerevisiae, or UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-transferase) of rat liver cells.
1576999	0	58	theme	peptides	100:107	arg1	O-glycosylation					18:32	Specific in vitro O-glycosylation	0:32	Specific in vitro O-glycosylation of human granulocyte-macrophage colony-stimulating-factor-derived peptides by O-glycosyltransferases of yeast and rat liver cells.	0:163	Specific in vitro O-glycosylation of human granulocyte-macrophage colony-stimulating-factor-derived peptides by O-glycosyltransferases of yeast and rat liver cells.
1576999	7	59	theme	good	1008:1011	arg1	substrate					1013:1021	a good substrate	1006:1021	a good substrate for yeast Man-transferase	1006:1047	Peptide 4-11 was a good substrate for yeast Man-transferase, leading to mannosylation of only Thr10, whereas it was very poorly O-glycosylated at positions Ser5 and Ser7 by GalNAc-transferase.
1576999	7	59	theme	good	1008:1011	arg1	Peptide					989:995	Peptide 4-11	989:1000	Peptide 4-11	989:1000	Peptide 4-11 was a good substrate for yeast Man-transferase, leading to mannosylation of only Thr10, whereas it was very poorly O-glycosylated at positions Ser5 and Ser7 by GalNAc-transferase.
1576999	7	60	dep	positions	1135:1143	arg1	Ser5					1145:1148	Ser5	1145:1148	Ser5	1145:1148	Peptide 4-11 was a good substrate for yeast Man-transferase, leading to mannosylation of only Thr10, whereas it was very poorly O-glycosylated at positions Ser5 and Ser7 by GalNAc-transferase.
1576999	7	60	dep	positions	1135:1143	arg1	positions					1135:1143	positions Ser5 and Ser7	1135:1157	positions Ser5 and Ser7	1135:1157	Peptide 4-11 was a good substrate for yeast Man-transferase, leading to mannosylation of only Thr10, whereas it was very poorly O-glycosylated at positions Ser5 and Ser7 by GalNAc-transferase.
1576999	7	60	dep	positions	1135:1143	arg1	Ser7					1154:1157	Ser7	1154:1157	Ser7	1154:1157	Peptide 4-11 was a good substrate for yeast Man-transferase, leading to mannosylation of only Thr10, whereas it was very poorly O-glycosylated at positions Ser5 and Ser7 by GalNAc-transferase.
1576999	5	61	dep	yeast	684:688	arg1	cerevisiae					704:713	the yeast Saccharomyces cerevisiae	680:713	the yeast Saccharomyces cerevisiae	680:713	Two types of octapeptides encompassing residues 4-11 (peptide 4-11) and variants thereof, or residues 8-15 (peptide 8-15) of hGM-CSF were tested as substrates for in vitro O-glycosylation using dolichyl-phosphate- D-mannose: protein O-D-mannosyltransferase (Man-transferase) of the yeast Saccharomyces cerevisiae, or UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-transferase) of rat liver cells.
17534424	1	0	theme	plasma	223:228	arg1	channels					248:255	plasma membrane chloride channels	223:255	plasma membrane chloride channels	223:255	BACKGROUND: The mammalian CLC protein family comprises nine members (ClC-1 to -7 and ClC-Ka, -Kb) that function either as plasma membrane chloride channels or as intracellular chloride/proton antiporters, and that sustain a broad spectrum of cellular processes, such as membrane excitability, transepithelial transport, endocytosis and lysosomal degradation.
17534424	1	0	theme	plasma	223:228	arg1	spectrum					331:338	a broad spectrum	323:338	a broad spectrum of cellular processes, such as membrane excitability, transepithelial transport, endocytosis and lysosomal degradation	323:457	BACKGROUND: The mammalian CLC protein family comprises nine members (ClC-1 to -7 and ClC-Ka, -Kb) that function either as plasma membrane chloride channels or as intracellular chloride/proton antiporters, and that sustain a broad spectrum of cellular processes, such as membrane excitability, transepithelial transport, endocytosis and lysosomal degradation.
17534424	1	0	theme	plasma	223:228	arg1	members					161:167	nine members	156:167	nine members (ClC-1 to -7 and ClC-Ka, -Kb) that function either as plasma membrane chloride channels or as intracellular chloride/proton antiporters, and that sustain a broad spectrum of cellular processes, such as membrane excitability, transepithelial transport, endocytosis and lysosomal degradation	156:457	BACKGROUND: The mammalian CLC protein family comprises nine members (ClC-1 to -7 and ClC-Ka, -Kb) that function either as plasma membrane chloride channels or as intracellular chloride/proton antiporters, and that sustain a broad spectrum of cellular processes, such as membrane excitability, transepithelial transport, endocytosis and lysosomal degradation.
17534424	8	1	theme	COS-1	2117:2121	arg1	cells					2123:2127	COS-1 cells	2117:2127	COS-1 cells	2117:2127	Mutating a juxtamembrane string of basic amino acids (amino acids 71-75: KKGRR) disturbs the association with detergent-resistant membrane fractions and also affects the segregation of ClC-6 and ClC-7 when cotransfected in COS-1 cells.
17534424	5	2	theme	COS-1	1383:1387	arg1	cells					1397:1401	COS-1 or HeLa cells	1383:1401	cells	1397:1401	In contrast, when transiently expressed in COS-1 or HeLa cells, human ClC-6 mainly overlaps with markers for early/recycling endosomes (transferrin receptor, EEA-1, Rab5, Rab4) and not with late endosomal/lysosomal markers (LAMP-1, Rab7).
17534424	1	3	theme	chloride	239:246	arg1	channels					248:255	plasma membrane chloride channels	223:255	plasma membrane chloride channels	223:255	BACKGROUND: The mammalian CLC protein family comprises nine members (ClC-1 to -7 and ClC-Ka, -Kb) that function either as plasma membrane chloride channels or as intracellular chloride/proton antiporters, and that sustain a broad spectrum of cellular processes, such as membrane excitability, transepithelial transport, endocytosis and lysosomal degradation.
17534424	1	3	theme	chloride	239:246	arg1	spectrum					331:338	a broad spectrum	323:338	a broad spectrum of cellular processes, such as membrane excitability, transepithelial transport, endocytosis and lysosomal degradation	323:457	BACKGROUND: The mammalian CLC protein family comprises nine members (ClC-1 to -7 and ClC-Ka, -Kb) that function either as plasma membrane chloride channels or as intracellular chloride/proton antiporters, and that sustain a broad spectrum of cellular processes, such as membrane excitability, transepithelial transport, endocytosis and lysosomal degradation.
17534424	1	3	theme	chloride	239:246	arg1	members					161:167	nine members	156:167	nine members (ClC-1 to -7 and ClC-Ka, -Kb) that function either as plasma membrane chloride channels or as intracellular chloride/proton antiporters, and that sustain a broad spectrum of cellular processes, such as membrane excitability, transepithelial transport, endocytosis and lysosomal degradation	156:457	BACKGROUND: The mammalian CLC protein family comprises nine members (ClC-1 to -7 and ClC-Ka, -Kb) that function either as plasma membrane chloride channels or as intracellular chloride/proton antiporters, and that sustain a broad spectrum of cellular processes, such as membrane excitability, transepithelial transport, endocytosis and lysosomal degradation.
17534424	10	4	dep	endogenous	2283:2292	arg1	endosomal					2300:2308	endosomal	2300:2308	endosomal	2300:2308	The differential sorting of endogenous (late endosomal) versus overexpressed (early and recycling endosomal) ClC-6 is reminiscent of that of other late endosomal/lysosomal membrane proteins (e.g. LIMP II), and is consistent with a rate-limiting sorting step for ClC-6 between early endosomes and its final destination in late endosomes.
17534424	10	4	dep	endogenous	2283:2292	arg1	early					2333:2337	early	2333:2337	early	2333:2337	The differential sorting of endogenous (late endosomal) versus overexpressed (early and recycling endosomal) ClC-6 is reminiscent of that of other late endosomal/lysosomal membrane proteins (e.g. LIMP II), and is consistent with a rate-limiting sorting step for ClC-6 between early endosomes and its final destination in late endosomes.
17534424	10	4	dep	endogenous	2283:2292	arg1	endosomal					2353:2361	endosomal	2353:2361	endosomal	2353:2361	The differential sorting of endogenous (late endosomal) versus overexpressed (early and recycling endosomal) ClC-6 is reminiscent of that of other late endosomal/lysosomal membrane proteins (e.g. LIMP II), and is consistent with a rate-limiting sorting step for ClC-6 between early endosomes and its final destination in late endosomes.
17534424	0	5	theme	Human	0:4	arg1	glycoprotein					32:43	a late endosomal glycoprotein	15:43	a late endosomal glycoprotein that associates with detergent-resistant lipid domains	15:98	Human ClC-6 is a late endosomal glycoprotein that associates with detergent-resistant lipid domains.
17534424	0	5	theme	Human	0:4	arg1	ClC-6					6:10	Human ClC-6	0:10	Human ClC-6	0:10	Human ClC-6 is a late endosomal glycoprotein that associates with detergent-resistant lipid domains.
17534424	2	6	theme	late	541:544	arg1	ClC-7					564:568	the late endosomal/lysomal ClC-7	537:568	the late endosomal/lysomal ClC-7	537:568	In this study we focus on human ClC-6, which is structurally most related to the late endosomal/lysomal ClC-7.
17534424	10	7	theme	membrane	2427:2434	arg1	proteins					2436:2443	other late endosomal/lysosomal membrane proteins	2396:2443	other late endosomal/lysosomal membrane proteins (e.g. LIMP II)	2396:2458	The differential sorting of endogenous (late endosomal) versus overexpressed (early and recycling endosomal) ClC-6 is reminiscent of that of other late endosomal/lysosomal membrane proteins (e.g. LIMP II), and is consistent with a rate-limiting sorting step for ClC-6 between early endosomes and its final destination in late endosomes.
17534424	10	7	theme	membrane	2427:2434	arg1	LIMP					2451:2454	e.g. LIMP II	2446:2457	e.g. LIMP II	2446:2457	The differential sorting of endogenous (late endosomal) versus overexpressed (early and recycling endosomal) ClC-6 is reminiscent of that of other late endosomal/lysosomal membrane proteins (e.g. LIMP II), and is consistent with a rate-limiting sorting step for ClC-6 between early endosomes and its final destination in late endosomes.
17534424	3	8	dep	FINDINGS	581:588	arg1	show					707:710	show	707:710	show that human ClC-6, when transfected in COS-1 cells, is N-glycosylated in a region that is evolutionary poorly conserved between mammalian CLC proteins and that is located between the predicted helices K and M. Three asparagine residues (N410, N422 and N432)	707:967	PRINCIPAL FINDINGS: Using a polyclonal affinity-purified antibody directed against a unique epitope in the ClC-6 COOH-terminal tail, we show that human ClC-6, when transfected in COS-1 cells, is N-glycosylated in a region that is evolutionary poorly conserved between mammalian CLC proteins and that is located between the predicted helices K and M. Three asparagine residues (N410, N422 and N432) have been defined by mutagenesis as acceptor sites for N-glycosylation, but only two of the three sites seem to be simultaneously N-glycosylated.
17534424	10	9	theme	endogenous	2283:2292	arg1	ClC-6					2364:2368	endogenous (late endosomal) versus overexpressed (early and recycling endosomal) ClC-6	2283:2368	endogenous (late endosomal) versus overexpressed (early and recycling endosomal) ClC-6	2283:2368	The differential sorting of endogenous (late endosomal) versus overexpressed (early and recycling endosomal) ClC-6 is reminiscent of that of other late endosomal/lysosomal membrane proteins (e.g. LIMP II), and is consistent with a rate-limiting sorting step for ClC-6 between early endosomes and its final destination in late endosomes.
17534424	3	10	theme	human	717:721	arg1	ClC-6					723:727	human ClC-6	717:727	human ClC-6	717:727	PRINCIPAL FINDINGS: Using a polyclonal affinity-purified antibody directed against a unique epitope in the ClC-6 COOH-terminal tail, we show that human ClC-6, when transfected in COS-1 cells, is N-glycosylated in a region that is evolutionary poorly conserved between mammalian CLC proteins and that is located between the predicted helices K and M. Three asparagine residues (N410, N422 and N432) have been defined by mutagenesis as acceptor sites for N-glycosylation, but only two of the three sites seem to be simultaneously N-glycosylated.
17534424	6	11	theme	human	1610:1614	arg1	ClC-6					1616:1620	human ClC-6	1610:1620	human ClC-6	1610:1620	Analogously, overexpression of human ClC-6 in SH-SY5Y cells also leads to an early/recycling endosomal localization of the exogenously expressed ClC-6 protein.
17534424	5	12	theme	late	1530:1533	arg1	markers					1555:1561	late endosomal/lysosomal markers	1530:1561	late endosomal/lysosomal markers (LAMP-1, Rab7)	1530:1576	In contrast, when transiently expressed in COS-1 or HeLa cells, human ClC-6 mainly overlaps with markers for early/recycling endosomes (transferrin receptor, EEA-1, Rab5, Rab4) and not with late endosomal/lysosomal markers (LAMP-1, Rab7).
17534424	3	13	theme	COS-1	750:754	arg1	cells					756:760	COS-1 cells	750:760	COS-1 cells	750:760	PRINCIPAL FINDINGS: Using a polyclonal affinity-purified antibody directed against a unique epitope in the ClC-6 COOH-terminal tail, we show that human ClC-6, when transfected in COS-1 cells, is N-glycosylated in a region that is evolutionary poorly conserved between mammalian CLC proteins and that is located between the predicted helices K and M. Three asparagine residues (N410, N422 and N432) have been defined by mutagenesis as acceptor sites for N-glycosylation, but only two of the three sites seem to be simultaneously N-glycosylated.
17534424	10	14	with	consistent	2468:2477	arg1	step					2508:2511	a rate-limiting sorting step	2484:2511	a rate-limiting sorting step for ClC-6 between early endosomes and its final destination in late endosomes	2484:2589	The differential sorting of endogenous (late endosomal) versus overexpressed (early and recycling endosomal) ClC-6 is reminiscent of that of other late endosomal/lysosomal membrane proteins (e.g. LIMP II), and is consistent with a rate-limiting sorting step for ClC-6 between early endosomes and its final destination in late endosomes.
17534424	2	15	theme	endosomal/lysomal	546:562	arg1	ClC-7					564:568	the late endosomal/lysomal ClC-7	537:568	the late endosomal/lysomal ClC-7	537:568	In this study we focus on human ClC-6, which is structurally most related to the late endosomal/lysomal ClC-7.
17534424	3	16	theme	ClC-6	678:682	arg1	tail					698:701	the ClC-6 COOH-terminal tail	674:701	the ClC-6 COOH-terminal tail	674:701	PRINCIPAL FINDINGS: Using a polyclonal affinity-purified antibody directed against a unique epitope in the ClC-6 COOH-terminal tail, we show that human ClC-6, when transfected in COS-1 cells, is N-glycosylated in a region that is evolutionary poorly conserved between mammalian CLC proteins and that is located between the predicted helices K and M. Three asparagine residues (N410, N422 and N432) have been defined by mutagenesis as acceptor sites for N-glycosylation, but only two of the three sites seem to be simultaneously N-glycosylated.
17534424	1	17	theme	mammalian	117:125	arg1	family					139:144	The mammalian CLC protein family	113:144	The mammalian CLC protein family	113:144	BACKGROUND: The mammalian CLC protein family comprises nine members (ClC-1 to -7 and ClC-Ka, -Kb) that function either as plasma membrane chloride channels or as intracellular chloride/proton antiporters, and that sustain a broad spectrum of cellular processes, such as membrane excitability, transepithelial transport, endocytosis and lysosomal degradation.
17534424	8	18	dep	acids	1954:1958	arg1	KKGRR					1967:1971	KKGRR	1967:1971	amino acids 71-75: KKGRR	1948:1971	Mutating a juxtamembrane string of basic amino acids (amino acids 71-75: KKGRR) disturbs the association with detergent-resistant membrane fractions and also affects the segregation of ClC-6 and ClC-7 when cotransfected in COS-1 cells.
17534424	3	19	gly	N-glycosylated	766:779	arg1	region					786:791	a region	784:791	a region that is evolutionary poorly conserved between mammalian CLC proteins	784:860	PRINCIPAL FINDINGS: Using a polyclonal affinity-purified antibody directed against a unique epitope in the ClC-6 COOH-terminal tail, we show that human ClC-6, when transfected in COS-1 cells, is N-glycosylated in a region that is evolutionary poorly conserved between mammalian CLC proteins and that is located between the predicted helices K and M. Three asparagine residues (N410, N422 and N432) have been defined by mutagenesis as acceptor sites for N-glycosylation, but only two of the three sites seem to be simultaneously N-glycosylated.
17534424	3	19	gly	N-glycosylated	766:779	arg1	ClC-6					723:727	human ClC-6	717:727	human ClC-6	717:727	PRINCIPAL FINDINGS: Using a polyclonal affinity-purified antibody directed against a unique epitope in the ClC-6 COOH-terminal tail, we show that human ClC-6, when transfected in COS-1 cells, is N-glycosylated in a region that is evolutionary poorly conserved between mammalian CLC proteins and that is located between the predicted helices K and M. Three asparagine residues (N410, N422 and N432) have been defined by mutagenesis as acceptor sites for N-glycosylation, but only two of the three sites seem to be simultaneously N-glycosylated.
17534424	3	19	gly	N-glycosylated	766:779	arg2	ClC-6					723:727	human ClC-6	717:727	human ClC-6	717:727	PRINCIPAL FINDINGS: Using a polyclonal affinity-purified antibody directed against a unique epitope in the ClC-6 COOH-terminal tail, we show that human ClC-6, when transfected in COS-1 cells, is N-glycosylated in a region that is evolutionary poorly conserved between mammalian CLC proteins and that is located between the predicted helices K and M. Three asparagine residues (N410, N422 and N432) have been defined by mutagenesis as acceptor sites for N-glycosylation, but only two of the three sites seem to be simultaneously N-glycosylated.
17534424	4	20	theme	differentiated	1120:1133	arg1	line					1160:1163	human neuroblastoma cell line	1135:1163	a differentiated human neuroblastoma cell line (SH-SY5Y)	1118:1173	In a differentiated human neuroblastoma cell line (SH-SY5Y), endogenous ClC-6 colocalizes with LAMP-1, a late endosomal/lysosomal marker, but not with early/recycling endosomal markers such as EEA-1 and transferrin receptor.
17534424	4	20	theme	differentiated	1120:1133	arg1	SH-SY5Y					1166:1172	SH-SY5Y	1166:1172	SH-SY5Y	1166:1172	In a differentiated human neuroblastoma cell line (SH-SY5Y), endogenous ClC-6 colocalizes with LAMP-1, a late endosomal/lysosomal marker, but not with early/recycling endosomal markers such as EEA-1 and transferrin receptor.
17534424	1	21	theme	transepithelial	394:408	arg1	transport					410:418	transepithelial transport	394:418	transepithelial transport	394:418	BACKGROUND: The mammalian CLC protein family comprises nine members (ClC-1 to -7 and ClC-Ka, -Kb) that function either as plasma membrane chloride channels or as intracellular chloride/proton antiporters, and that sustain a broad spectrum of cellular processes, such as membrane excitability, transepithelial transport, endocytosis and lysosomal degradation.
17534424	3	22	theme	polyclonal	599:608	arg1	antibody					628:635	a polyclonal affinity-purified antibody	597:635	a polyclonal affinity-purified antibody directed against a unique epitope in the ClC-6 COOH-terminal tail	597:701	PRINCIPAL FINDINGS: Using a polyclonal affinity-purified antibody directed against a unique epitope in the ClC-6 COOH-terminal tail, we show that human ClC-6, when transfected in COS-1 cells, is N-glycosylated in a region that is evolutionary poorly conserved between mammalian CLC proteins and that is located between the predicted helices K and M. Three asparagine residues (N410, N422 and N432) have been defined by mutagenesis as acceptor sites for N-glycosylation, but only two of the three sites seem to be simultaneously N-glycosylated.
17534424	1	23	theme	protein	131:137	arg1	family					139:144	The mammalian CLC protein family	113:144	The mammalian CLC protein family	113:144	BACKGROUND: The mammalian CLC protein family comprises nine members (ClC-1 to -7 and ClC-Ka, -Kb) that function either as plasma membrane chloride channels or as intracellular chloride/proton antiporters, and that sustain a broad spectrum of cellular processes, such as membrane excitability, transepithelial transport, endocytosis and lysosomal degradation.
17534424	10	24	theme	sorting	2500:2506	arg1	step					2508:2511	a rate-limiting sorting step	2484:2511	a rate-limiting sorting step for ClC-6 between early endosomes and its final destination in late endosomes	2484:2589	The differential sorting of endogenous (late endosomal) versus overexpressed (early and recycling endosomal) ClC-6 is reminiscent of that of other late endosomal/lysosomal membrane proteins (e.g. LIMP II), and is consistent with a rate-limiting sorting step for ClC-6 between early endosomes and its final destination in late endosomes.
17534424	3	25	dep	helices	904:910	arg1	helices					904:910	the predicted helices K and M. Three asparagine residues (N410, N422 and N432)	890:967	the predicted helices K and M. Three asparagine residues (N410, N422 and N432)	890:967	PRINCIPAL FINDINGS: Using a polyclonal affinity-purified antibody directed against a unique epitope in the ClC-6 COOH-terminal tail, we show that human ClC-6, when transfected in COS-1 cells, is N-glycosylated in a region that is evolutionary poorly conserved between mammalian CLC proteins and that is located between the predicted helices K and M. Three asparagine residues (N410, N422 and N432) have been defined by mutagenesis as acceptor sites for N-glycosylation, but only two of the three sites seem to be simultaneously N-glycosylated.
17534424	3	25	dep	helices	904:910	arg1	M.					918:919	M.	918:919	M.	918:919	PRINCIPAL FINDINGS: Using a polyclonal affinity-purified antibody directed against a unique epitope in the ClC-6 COOH-terminal tail, we show that human ClC-6, when transfected in COS-1 cells, is N-glycosylated in a region that is evolutionary poorly conserved between mammalian CLC proteins and that is located between the predicted helices K and M. Three asparagine residues (N410, N422 and N432) have been defined by mutagenesis as acceptor sites for N-glycosylation, but only two of the three sites seem to be simultaneously N-glycosylated.
17534424	3	25	dep	helices	904:910	arg1	K					912:912	K	912:912	K	912:912	PRINCIPAL FINDINGS: Using a polyclonal affinity-purified antibody directed against a unique epitope in the ClC-6 COOH-terminal tail, we show that human ClC-6, when transfected in COS-1 cells, is N-glycosylated in a region that is evolutionary poorly conserved between mammalian CLC proteins and that is located between the predicted helices K and M. Three asparagine residues (N410, N422 and N432) have been defined by mutagenesis as acceptor sites for N-glycosylation, but only two of the three sites seem to be simultaneously N-glycosylated.
17534424	7	26	dep	fractions	1839:1847	arg1	suggesting					1850:1859	suggesting	1850:1859	suggesting its partitioning in lipid rafts	1850:1891	Finally, in transiently transfected COS-1 cells, ClC-6 copurifies with detergent-resistant membrane fractions, suggesting its partitioning in lipid rafts.
17534424	0	27	theme	detergent-resistant	66:84	arg1	domains					92:98	detergent-resistant lipid domains	66:98	detergent-resistant lipid domains	66:98	Human ClC-6 is a late endosomal glycoprotein that associates with detergent-resistant lipid domains.
17534424	3	28	theme	mammalian	839:847	arg1	proteins					853:860	mammalian CLC proteins	839:860	mammalian CLC proteins	839:860	PRINCIPAL FINDINGS: Using a polyclonal affinity-purified antibody directed against a unique epitope in the ClC-6 COOH-terminal tail, we show that human ClC-6, when transfected in COS-1 cells, is N-glycosylated in a region that is evolutionary poorly conserved between mammalian CLC proteins and that is located between the predicted helices K and M. Three asparagine residues (N410, N422 and N432) have been defined by mutagenesis as acceptor sites for N-glycosylation, but only two of the three sites seem to be simultaneously N-glycosylated.
17534424	8	29	theme	basic	1929:1933	arg1	acids					1941:1945	basic amino acids	1929:1945	basic amino acids (amino acids 71-75: KKGRR)	1929:1972	Mutating a juxtamembrane string of basic amino acids (amino acids 71-75: KKGRR) disturbs the association with detergent-resistant membrane fractions and also affects the segregation of ClC-6 and ClC-7 when cotransfected in COS-1 cells.
17534424	5	30	theme	HeLa	1392:1395	arg1	cells					1397:1401	COS-1 or HeLa cells	1383:1401	cells	1397:1401	In contrast, when transiently expressed in COS-1 or HeLa cells, human ClC-6 mainly overlaps with markers for early/recycling endosomes (transferrin receptor, EEA-1, Rab5, Rab4) and not with late endosomal/lysosomal markers (LAMP-1, Rab7).
17534424	8	31	theme	acids	1941:1945	arg1	string					1919:1924	a juxtamembrane string	1903:1924	a juxtamembrane string of basic amino acids (amino acids 71-75: KKGRR)	1903:1972	Mutating a juxtamembrane string of basic amino acids (amino acids 71-75: KKGRR) disturbs the association with detergent-resistant membrane fractions and also affects the segregation of ClC-6 and ClC-7 when cotransfected in COS-1 cells.
17534424	1	32	theme	cellular	343:350	arg1	excitability					380:391	membrane excitability	371:391	membrane excitability	371:391	BACKGROUND: The mammalian CLC protein family comprises nine members (ClC-1 to -7 and ClC-Ka, -Kb) that function either as plasma membrane chloride channels or as intracellular chloride/proton antiporters, and that sustain a broad spectrum of cellular processes, such as membrane excitability, transepithelial transport, endocytosis and lysosomal degradation.
17534424	1	32	theme	cellular	343:350	arg1	transport					410:418	transepithelial transport	394:418	transepithelial transport	394:418	BACKGROUND: The mammalian CLC protein family comprises nine members (ClC-1 to -7 and ClC-Ka, -Kb) that function either as plasma membrane chloride channels or as intracellular chloride/proton antiporters, and that sustain a broad spectrum of cellular processes, such as membrane excitability, transepithelial transport, endocytosis and lysosomal degradation.
17534424	1	32	theme	cellular	343:350	arg1	endocytosis					421:431	endocytosis	421:431	endocytosis	421:431	BACKGROUND: The mammalian CLC protein family comprises nine members (ClC-1 to -7 and ClC-Ka, -Kb) that function either as plasma membrane chloride channels or as intracellular chloride/proton antiporters, and that sustain a broad spectrum of cellular processes, such as membrane excitability, transepithelial transport, endocytosis and lysosomal degradation.
17534424	1	32	theme	cellular	343:350	arg1	degradation					447:457	lysosomal degradation	437:457	lysosomal degradation	437:457	BACKGROUND: The mammalian CLC protein family comprises nine members (ClC-1 to -7 and ClC-Ka, -Kb) that function either as plasma membrane chloride channels or as intracellular chloride/proton antiporters, and that sustain a broad spectrum of cellular processes, such as membrane excitability, transepithelial transport, endocytosis and lysosomal degradation.
17534424	1	32	theme	cellular	343:350	arg1	processes					352:360	cellular processes	343:360	cellular processes	343:360	BACKGROUND: The mammalian CLC protein family comprises nine members (ClC-1 to -7 and ClC-Ka, -Kb) that function either as plasma membrane chloride channels or as intracellular chloride/proton antiporters, and that sustain a broad spectrum of cellular processes, such as membrane excitability, transepithelial transport, endocytosis and lysosomal degradation.
17534424	5	33	dep	markers	1555:1561	arg1	LAMP-1					1564:1569	LAMP-1	1564:1569	LAMP-1	1564:1569	In contrast, when transiently expressed in COS-1 or HeLa cells, human ClC-6 mainly overlaps with markers for early/recycling endosomes (transferrin receptor, EEA-1, Rab5, Rab4) and not with late endosomal/lysosomal markers (LAMP-1, Rab7).
17534424	5	33	dep	markers	1555:1561	arg1	Rab7					1572:1575	Rab7	1572:1575	Rab7	1572:1575	In contrast, when transiently expressed in COS-1 or HeLa cells, human ClC-6 mainly overlaps with markers for early/recycling endosomes (transferrin receptor, EEA-1, Rab5, Rab4) and not with late endosomal/lysosomal markers (LAMP-1, Rab7).
17534424	4	34	theme	neuroblastoma	1141:1153	arg1	line					1160:1163	human neuroblastoma cell line	1135:1163	a differentiated human neuroblastoma cell line (SH-SY5Y)	1118:1173	In a differentiated human neuroblastoma cell line (SH-SY5Y), endogenous ClC-6 colocalizes with LAMP-1, a late endosomal/lysosomal marker, but not with early/recycling endosomal markers such as EEA-1 and transferrin receptor.
17534424	4	34	theme	neuroblastoma	1141:1153	arg1	SH-SY5Y					1166:1172	SH-SY5Y	1166:1172	SH-SY5Y	1166:1172	In a differentiated human neuroblastoma cell line (SH-SY5Y), endogenous ClC-6 colocalizes with LAMP-1, a late endosomal/lysosomal marker, but not with early/recycling endosomal markers such as EEA-1 and transferrin receptor.
17534424	9	35	theme	detergent	2220:2228	arg1	domains					2246:2252	detergent resistant lipid domains	2220:2252	detergent resistant lipid domains	2220:2252	CONCLUSIONS: We conclude that human ClC-6 is an endosomal glycoprotein that partitions in detergent resistant lipid domains.
17534424	8	36	theme	amino	1948:1952	arg1	acids					1954:1958	amino acids 71-75	1948:1964	amino acids 71-75: KKGRR	1948:1971	Mutating a juxtamembrane string of basic amino acids (amino acids 71-75: KKGRR) disturbs the association with detergent-resistant membrane fractions and also affects the segregation of ClC-6 and ClC-7 when cotransfected in COS-1 cells.
17534424	8	37	theme	detergent-resistant	2004:2022	arg1	fractions					2033:2041	detergent-resistant membrane fractions	2004:2041	detergent-resistant membrane fractions	2004:2041	Mutating a juxtamembrane string of basic amino acids (amino acids 71-75: KKGRR) disturbs the association with detergent-resistant membrane fractions and also affects the segregation of ClC-6 and ClC-7 when cotransfected in COS-1 cells.
17534424	6	38	theme	ClC-6	1724:1728	arg1	protein					1730:1736	the exogenously expressed ClC-6 protein	1698:1736	the exogenously expressed ClC-6 protein	1698:1736	Analogously, overexpression of human ClC-6 in SH-SY5Y cells also leads to an early/recycling endosomal localization of the exogenously expressed ClC-6 protein.
17534424	9	39	theme	lipid	2240:2244	arg1	domains					2246:2252	detergent resistant lipid domains	2220:2252	detergent resistant lipid domains	2220:2252	CONCLUSIONS: We conclude that human ClC-6 is an endosomal glycoprotein that partitions in detergent resistant lipid domains.
17534424	10	40	theme	late	2402:2405	arg1	proteins					2436:2443	other late endosomal/lysosomal membrane proteins	2396:2443	other late endosomal/lysosomal membrane proteins (e.g. LIMP II)	2396:2458	The differential sorting of endogenous (late endosomal) versus overexpressed (early and recycling endosomal) ClC-6 is reminiscent of that of other late endosomal/lysosomal membrane proteins (e.g. LIMP II), and is consistent with a rate-limiting sorting step for ClC-6 between early endosomes and its final destination in late endosomes.
17534424	10	40	theme	late	2402:2405	arg1	LIMP					2451:2454	e.g. LIMP II	2446:2457	e.g. LIMP II	2446:2457	The differential sorting of endogenous (late endosomal) versus overexpressed (early and recycling endosomal) ClC-6 is reminiscent of that of other late endosomal/lysosomal membrane proteins (e.g. LIMP II), and is consistent with a rate-limiting sorting step for ClC-6 between early endosomes and its final destination in late endosomes.
17534424	10	41	theme	late	2576:2579	arg1	endosomes					2581:2589	late endosomes	2576:2589	late endosomes	2576:2589	The differential sorting of endogenous (late endosomal) versus overexpressed (early and recycling endosomal) ClC-6 is reminiscent of that of other late endosomal/lysosomal membrane proteins (e.g. LIMP II), and is consistent with a rate-limiting sorting step for ClC-6 between early endosomes and its final destination in late endosomes.
17534424	0	42	theme	late	17:20	arg1	glycoprotein					32:43	a late endosomal glycoprotein	15:43	a late endosomal glycoprotein that associates with detergent-resistant lipid domains	15:98	Human ClC-6 is a late endosomal glycoprotein that associates with detergent-resistant lipid domains.
17534424	0	42	theme	late	17:20	arg1	ClC-6					6:10	Human ClC-6	0:10	Human ClC-6	0:10	Human ClC-6 is a late endosomal glycoprotein that associates with detergent-resistant lipid domains.
17534424	1	43	theme	chloride/proton	277:291	arg1	antiporters					293:303	intracellular chloride/proton antiporters	263:303	intracellular chloride/proton antiporters	263:303	BACKGROUND: The mammalian CLC protein family comprises nine members (ClC-1 to -7 and ClC-Ka, -Kb) that function either as plasma membrane chloride channels or as intracellular chloride/proton antiporters, and that sustain a broad spectrum of cellular processes, such as membrane excitability, transepithelial transport, endocytosis and lysosomal degradation.
17534424	1	43	theme	chloride/proton	277:291	arg1	members					161:167	nine members	156:167	nine members (ClC-1 to -7 and ClC-Ka, -Kb) that function either as plasma membrane chloride channels or as intracellular chloride/proton antiporters, and that sustain a broad spectrum of cellular processes, such as membrane excitability, transepithelial transport, endocytosis and lysosomal degradation	156:457	BACKGROUND: The mammalian CLC protein family comprises nine members (ClC-1 to -7 and ClC-Ka, -Kb) that function either as plasma membrane chloride channels or as intracellular chloride/proton antiporters, and that sustain a broad spectrum of cellular processes, such as membrane excitability, transepithelial transport, endocytosis and lysosomal degradation.
17534424	7	44	theme	membrane	1830:1837	arg1	fractions					1839:1847	detergent-resistant membrane fractions	1810:1847	detergent-resistant membrane fractions	1810:1847	Finally, in transiently transfected COS-1 cells, ClC-6 copurifies with detergent-resistant membrane fractions, suggesting its partitioning in lipid rafts.
17534424	7	45	theme	COS-1	1775:1779	arg1	cells					1781:1785	transiently transfected COS-1 cells	1751:1785	transiently transfected COS-1 cells	1751:1785	Finally, in transiently transfected COS-1 cells, ClC-6 copurifies with detergent-resistant membrane fractions, suggesting its partitioning in lipid rafts.
17534424	4	46	theme	late	1220:1223	arg1	marker					1245:1250	a late endosomal/lysosomal marker	1218:1250	a late endosomal/lysosomal marker	1218:1250	In a differentiated human neuroblastoma cell line (SH-SY5Y), endogenous ClC-6 colocalizes with LAMP-1, a late endosomal/lysosomal marker, but not with early/recycling endosomal markers such as EEA-1 and transferrin receptor.
17534424	4	46	theme	late	1220:1223	arg1	LAMP-1					1210:1215	LAMP-1	1210:1215	LAMP-1	1210:1215	In a differentiated human neuroblastoma cell line (SH-SY5Y), endogenous ClC-6 colocalizes with LAMP-1, a late endosomal/lysosomal marker, but not with early/recycling endosomal markers such as EEA-1 and transferrin receptor.
17534424	3	47	theme	affinity-purified	610:626	arg1	antibody					628:635	a polyclonal affinity-purified antibody	597:635	a polyclonal affinity-purified antibody directed against a unique epitope in the ClC-6 COOH-terminal tail	597:701	PRINCIPAL FINDINGS: Using a polyclonal affinity-purified antibody directed against a unique epitope in the ClC-6 COOH-terminal tail, we show that human ClC-6, when transfected in COS-1 cells, is N-glycosylated in a region that is evolutionary poorly conserved between mammalian CLC proteins and that is located between the predicted helices K and M. Three asparagine residues (N410, N422 and N432) have been defined by mutagenesis as acceptor sites for N-glycosylation, but only two of the three sites seem to be simultaneously N-glycosylated.
17534424	6	48	theme	endosomal	1672:1680	arg1	localization					1682:1693	an early/recycling endosomal localization	1653:1693	an early/recycling endosomal localization of the exogenously expressed ClC-6 protein	1653:1736	Analogously, overexpression of human ClC-6 in SH-SY5Y cells also leads to an early/recycling endosomal localization of the exogenously expressed ClC-6 protein.
17534424	5	49	theme	early/recycling	1449:1463	arg1	endosomes					1465:1473	early/recycling endosomes	1449:1473	early/recycling endosomes (transferrin receptor, EEA-1, Rab5, Rab4)	1449:1515	In contrast, when transiently expressed in COS-1 or HeLa cells, human ClC-6 mainly overlaps with markers for early/recycling endosomes (transferrin receptor, EEA-1, Rab5, Rab4) and not with late endosomal/lysosomal markers (LAMP-1, Rab7).
17534424	3	50	theme	sites	1067:1071	arg1	sites					1067:1071	the three sites	1057:1071	the three sites	1057:1071	PRINCIPAL FINDINGS: Using a polyclonal affinity-purified antibody directed against a unique epitope in the ClC-6 COOH-terminal tail, we show that human ClC-6, when transfected in COS-1 cells, is N-glycosylated in a region that is evolutionary poorly conserved between mammalian CLC proteins and that is located between the predicted helices K and M. Three asparagine residues (N410, N422 and N432) have been defined by mutagenesis as acceptor sites for N-glycosylation, but only two of the three sites seem to be simultaneously N-glycosylated.
17534424	3	50	theme	sites	1067:1071	arg1	two					1050:1052	two	1050:1052	two	1050:1052	PRINCIPAL FINDINGS: Using a polyclonal affinity-purified antibody directed against a unique epitope in the ClC-6 COOH-terminal tail, we show that human ClC-6, when transfected in COS-1 cells, is N-glycosylated in a region that is evolutionary poorly conserved between mammalian CLC proteins and that is located between the predicted helices K and M. Three asparagine residues (N410, N422 and N432) have been defined by mutagenesis as acceptor sites for N-glycosylation, but only two of the three sites seem to be simultaneously N-glycosylated.
17534424	3	51	theme	unique	656:661	arg1	epitope					663:669	a unique epitope	654:669	a unique epitope in the ClC-6 COOH-terminal tail	654:701	PRINCIPAL FINDINGS: Using a polyclonal affinity-purified antibody directed against a unique epitope in the ClC-6 COOH-terminal tail, we show that human ClC-6, when transfected in COS-1 cells, is N-glycosylated in a region that is evolutionary poorly conserved between mammalian CLC proteins and that is located between the predicted helices K and M. Three asparagine residues (N410, N422 and N432) have been defined by mutagenesis as acceptor sites for N-glycosylation, but only two of the three sites seem to be simultaneously N-glycosylated.
17534424	10	52	from	endosomes	2537:2545	arg1	endosomes					2581:2589	late endosomes	2576:2589	late endosomes	2576:2589	The differential sorting of endogenous (late endosomal) versus overexpressed (early and recycling endosomal) ClC-6 is reminiscent of that of other late endosomal/lysosomal membrane proteins (e.g. LIMP II), and is consistent with a rate-limiting sorting step for ClC-6 between early endosomes and its final destination in late endosomes.
17534424	3	53	from	epitope	663:669	arg1	tail					698:701	the ClC-6 COOH-terminal tail	674:701	the ClC-6 COOH-terminal tail	674:701	PRINCIPAL FINDINGS: Using a polyclonal affinity-purified antibody directed against a unique epitope in the ClC-6 COOH-terminal tail, we show that human ClC-6, when transfected in COS-1 cells, is N-glycosylated in a region that is evolutionary poorly conserved between mammalian CLC proteins and that is located between the predicted helices K and M. Three asparagine residues (N410, N422 and N432) have been defined by mutagenesis as acceptor sites for N-glycosylation, but only two of the three sites seem to be simultaneously N-glycosylated.
17534424	10	54	theme	overexpressed	2318:2330	arg1	ClC-6					2364:2368	endogenous (late endosomal) versus overexpressed (early and recycling endosomal) ClC-6	2283:2368	endogenous (late endosomal) versus overexpressed (early and recycling endosomal) ClC-6	2283:2368	The differential sorting of endogenous (late endosomal) versus overexpressed (early and recycling endosomal) ClC-6 is reminiscent of that of other late endosomal/lysosomal membrane proteins (e.g. LIMP II), and is consistent with a rate-limiting sorting step for ClC-6 between early endosomes and its final destination in late endosomes.
17534424	8	55	dep	acids	1941:1945	arg1	acids					1954:1958	amino acids 71-75	1948:1964	amino acids 71-75: KKGRR	1948:1971	Mutating a juxtamembrane string of basic amino acids (amino acids 71-75: KKGRR) disturbs the association with detergent-resistant membrane fractions and also affects the segregation of ClC-6 and ClC-7 when cotransfected in COS-1 cells.
17534424	4	56	theme	endosomal	1282:1290	arg1	EEA-1					1308:1312	EEA-1	1308:1312	EEA-1	1308:1312	In a differentiated human neuroblastoma cell line (SH-SY5Y), endogenous ClC-6 colocalizes with LAMP-1, a late endosomal/lysosomal marker, but not with early/recycling endosomal markers such as EEA-1 and transferrin receptor.
17534424	4	56	theme	endosomal	1282:1290	arg1	receptor					1330:1337	transferrin receptor	1318:1337	transferrin receptor	1318:1337	In a differentiated human neuroblastoma cell line (SH-SY5Y), endogenous ClC-6 colocalizes with LAMP-1, a late endosomal/lysosomal marker, but not with early/recycling endosomal markers such as EEA-1 and transferrin receptor.
17534424	4	56	theme	endosomal	1282:1290	arg1	markers					1292:1298	early/recycling endosomal markers	1266:1298	early/recycling endosomal markers such as EEA-1 and transferrin receptor	1266:1337	In a differentiated human neuroblastoma cell line (SH-SY5Y), endogenous ClC-6 colocalizes with LAMP-1, a late endosomal/lysosomal marker, but not with early/recycling endosomal markers such as EEA-1 and transferrin receptor.
17534424	1	57	theme	membrane	230:237	arg1	channels					248:255	plasma membrane chloride channels	223:255	plasma membrane chloride channels	223:255	BACKGROUND: The mammalian CLC protein family comprises nine members (ClC-1 to -7 and ClC-Ka, -Kb) that function either as plasma membrane chloride channels or as intracellular chloride/proton antiporters, and that sustain a broad spectrum of cellular processes, such as membrane excitability, transepithelial transport, endocytosis and lysosomal degradation.
17534424	1	57	theme	membrane	230:237	arg1	spectrum					331:338	a broad spectrum	323:338	a broad spectrum of cellular processes, such as membrane excitability, transepithelial transport, endocytosis and lysosomal degradation	323:457	BACKGROUND: The mammalian CLC protein family comprises nine members (ClC-1 to -7 and ClC-Ka, -Kb) that function either as plasma membrane chloride channels or as intracellular chloride/proton antiporters, and that sustain a broad spectrum of cellular processes, such as membrane excitability, transepithelial transport, endocytosis and lysosomal degradation.
17534424	1	57	theme	membrane	230:237	arg1	members					161:167	nine members	156:167	nine members (ClC-1 to -7 and ClC-Ka, -Kb) that function either as plasma membrane chloride channels or as intracellular chloride/proton antiporters, and that sustain a broad spectrum of cellular processes, such as membrane excitability, transepithelial transport, endocytosis and lysosomal degradation	156:457	BACKGROUND: The mammalian CLC protein family comprises nine members (ClC-1 to -7 and ClC-Ka, -Kb) that function either as plasma membrane chloride channels or as intracellular chloride/proton antiporters, and that sustain a broad spectrum of cellular processes, such as membrane excitability, transepithelial transport, endocytosis and lysosomal degradation.
17534424	5	58	dep	endosomes	1465:1473	arg1	EEA-1					1498:1502	EEA-1	1498:1502	EEA-1	1498:1502	In contrast, when transiently expressed in COS-1 or HeLa cells, human ClC-6 mainly overlaps with markers for early/recycling endosomes (transferrin receptor, EEA-1, Rab5, Rab4) and not with late endosomal/lysosomal markers (LAMP-1, Rab7).
17534424	5	58	dep	endosomes	1465:1473	arg1	receptor					1488:1495	transferrin receptor	1476:1495	transferrin receptor	1476:1495	In contrast, when transiently expressed in COS-1 or HeLa cells, human ClC-6 mainly overlaps with markers for early/recycling endosomes (transferrin receptor, EEA-1, Rab5, Rab4) and not with late endosomal/lysosomal markers (LAMP-1, Rab7).
17534424	5	58	dep	endosomes	1465:1473	arg1	Rab4					1511:1514	Rab4	1511:1514	Rab4	1511:1514	In contrast, when transiently expressed in COS-1 or HeLa cells, human ClC-6 mainly overlaps with markers for early/recycling endosomes (transferrin receptor, EEA-1, Rab5, Rab4) and not with late endosomal/lysosomal markers (LAMP-1, Rab7).
17534424	10	59	from	destination	2561:2571	arg1	endosomes					2581:2589	late endosomes	2576:2589	late endosomes	2576:2589	The differential sorting of endogenous (late endosomal) versus overexpressed (early and recycling endosomal) ClC-6 is reminiscent of that of other late endosomal/lysosomal membrane proteins (e.g. LIMP II), and is consistent with a rate-limiting sorting step for ClC-6 between early endosomes and its final destination in late endosomes.
17534424	1	60	theme	lysosomal	437:445	arg1	degradation					447:457	lysosomal degradation	437:457	lysosomal degradation	437:457	BACKGROUND: The mammalian CLC protein family comprises nine members (ClC-1 to -7 and ClC-Ka, -Kb) that function either as plasma membrane chloride channels or as intracellular chloride/proton antiporters, and that sustain a broad spectrum of cellular processes, such as membrane excitability, transepithelial transport, endocytosis and lysosomal degradation.
17534424	10	61	theme	that	2388:2391	arg1	reminiscent					2373:2383	reminiscent	2373:2383	reminiscent	2373:2383	The differential sorting of endogenous (late endosomal) versus overexpressed (early and recycling endosomal) ClC-6 is reminiscent of that of other late endosomal/lysosomal membrane proteins (e.g. LIMP II), and is consistent with a rate-limiting sorting step for ClC-6 between early endosomes and its final destination in late endosomes.
17534424	10	61	theme	that	2388:2391	arg1	consistent					2468:2477	consistent	2468:2477	consistent	2468:2477	The differential sorting of endogenous (late endosomal) versus overexpressed (early and recycling endosomal) ClC-6 is reminiscent of that of other late endosomal/lysosomal membrane proteins (e.g. LIMP II), and is consistent with a rate-limiting sorting step for ClC-6 between early endosomes and its final destination in late endosomes.
17534424	10	61	theme	that	2388:2391	arg1	sorting					2272:2278	The differential sorting	2255:2278	The differential sorting of endogenous (late endosomal) versus overexpressed (early and recycling endosomal) ClC-6	2255:2368	The differential sorting of endogenous (late endosomal) versus overexpressed (early and recycling endosomal) ClC-6 is reminiscent of that of other late endosomal/lysosomal membrane proteins (e.g. LIMP II), and is consistent with a rate-limiting sorting step for ClC-6 between early endosomes and its final destination in late endosomes.
17534424	10	62	theme	endosomal/lysosomal	2407:2425	arg1	proteins					2436:2443	other late endosomal/lysosomal membrane proteins	2396:2443	other late endosomal/lysosomal membrane proteins (e.g. LIMP II)	2396:2458	The differential sorting of endogenous (late endosomal) versus overexpressed (early and recycling endosomal) ClC-6 is reminiscent of that of other late endosomal/lysosomal membrane proteins (e.g. LIMP II), and is consistent with a rate-limiting sorting step for ClC-6 between early endosomes and its final destination in late endosomes.
17534424	10	62	theme	endosomal/lysosomal	2407:2425	arg1	LIMP					2451:2454	e.g. LIMP II	2446:2457	e.g. LIMP II	2446:2457	The differential sorting of endogenous (late endosomal) versus overexpressed (early and recycling endosomal) ClC-6 is reminiscent of that of other late endosomal/lysosomal membrane proteins (e.g. LIMP II), and is consistent with a rate-limiting sorting step for ClC-6 between early endosomes and its final destination in late endosomes.
17534424	4	63	theme	transferrin	1318:1328	arg1	receptor					1330:1337	transferrin receptor	1318:1337	transferrin receptor	1318:1337	In a differentiated human neuroblastoma cell line (SH-SY5Y), endogenous ClC-6 colocalizes with LAMP-1, a late endosomal/lysosomal marker, but not with early/recycling endosomal markers such as EEA-1 and transferrin receptor.
17534424	10	64	theme	final	2555:2559	arg1	destination					2561:2571	its final destination	2551:2571	its final destination in late endosomes	2551:2589	The differential sorting of endogenous (late endosomal) versus overexpressed (early and recycling endosomal) ClC-6 is reminiscent of that of other late endosomal/lysosomal membrane proteins (e.g. LIMP II), and is consistent with a rate-limiting sorting step for ClC-6 between early endosomes and its final destination in late endosomes.
17534424	7	65	from	partitioning	1865:1876	arg1	rafts					1887:1891	lipid rafts	1881:1891	lipid rafts	1881:1891	Finally, in transiently transfected COS-1 cells, ClC-6 copurifies with detergent-resistant membrane fractions, suggesting its partitioning in lipid rafts.
17534424	3	66	from	region	786:791	arg1	N-glycosylated					766:779	N-glycosylated	766:779	N-glycosylated	766:779	PRINCIPAL FINDINGS: Using a polyclonal affinity-purified antibody directed against a unique epitope in the ClC-6 COOH-terminal tail, we show that human ClC-6, when transfected in COS-1 cells, is N-glycosylated in a region that is evolutionary poorly conserved between mammalian CLC proteins and that is located between the predicted helices K and M. Three asparagine residues (N410, N422 and N432) have been defined by mutagenesis as acceptor sites for N-glycosylation, but only two of the three sites seem to be simultaneously N-glycosylated.
17534424	3	67	theme	PRINCIPAL	571:579	arg1	FINDINGS					581:588	PRINCIPAL FINDINGS	571:588	PRINCIPAL FINDINGS: Using a polyclonal affinity-purified antibody directed against a unique epitope in the ClC-6 COOH-terminal tail, we show that human ClC-6, when transfected in COS-1 cells, is N-glycosylated in a region that is evolutionary poorly conserved between mammalian CLC proteins and that is located between the predicted helices K and M. Three asparagine residues (N410, N422 and N432)	571:967	PRINCIPAL FINDINGS: Using a polyclonal affinity-purified antibody directed against a unique epitope in the ClC-6 COOH-terminal tail, we show that human ClC-6, when transfected in COS-1 cells, is N-glycosylated in a region that is evolutionary poorly conserved between mammalian CLC proteins and that is located between the predicted helices K and M. Three asparagine residues (N410, N422 and N432) have been defined by mutagenesis as acceptor sites for N-glycosylation, but only two of the three sites seem to be simultaneously N-glycosylated.
17534424	3	67	theme	PRINCIPAL	571:579	arg1	sites					1014:1018	acceptor sites	1005:1018	acceptor sites for N-glycosylation	1005:1038	PRINCIPAL FINDINGS: Using a polyclonal affinity-purified antibody directed against a unique epitope in the ClC-6 COOH-terminal tail, we show that human ClC-6, when transfected in COS-1 cells, is N-glycosylated in a region that is evolutionary poorly conserved between mammalian CLC proteins and that is located between the predicted helices K and M. Three asparagine residues (N410, N422 and N432) have been defined by mutagenesis as acceptor sites for N-glycosylation, but only two of the three sites seem to be simultaneously N-glycosylated.
17534424	9	68	theme	endosomal	2178:2186	arg1	ClC-6					2166:2170	human ClC-6	2160:2170	human ClC-6	2160:2170	CONCLUSIONS: We conclude that human ClC-6 is an endosomal glycoprotein that partitions in detergent resistant lipid domains.
17534424	9	68	theme	endosomal	2178:2186	arg1	glycoprotein					2188:2199	an endosomal glycoprotein	2175:2199	an endosomal glycoprotein that partitions in detergent resistant lipid domains	2175:2252	CONCLUSIONS: We conclude that human ClC-6 is an endosomal glycoprotein that partitions in detergent resistant lipid domains.
17534424	10	69	theme	e.g.	2446:2449	arg1	proteins					2436:2443	other late endosomal/lysosomal membrane proteins	2396:2443	other late endosomal/lysosomal membrane proteins (e.g. LIMP II)	2396:2458	The differential sorting of endogenous (late endosomal) versus overexpressed (early and recycling endosomal) ClC-6 is reminiscent of that of other late endosomal/lysosomal membrane proteins (e.g. LIMP II), and is consistent with a rate-limiting sorting step for ClC-6 between early endosomes and its final destination in late endosomes.
17534424	10	69	theme	e.g.	2446:2449	arg1	LIMP					2451:2454	e.g. LIMP II	2446:2457	e.g. LIMP II	2446:2457	The differential sorting of endogenous (late endosomal) versus overexpressed (early and recycling endosomal) ClC-6 is reminiscent of that of other late endosomal/lysosomal membrane proteins (e.g. LIMP II), and is consistent with a rate-limiting sorting step for ClC-6 between early endosomes and its final destination in late endosomes.
17534424	5	70	theme	endosomal/lysosomal	1535:1553	arg1	markers					1555:1561	late endosomal/lysosomal markers	1530:1561	late endosomal/lysosomal markers (LAMP-1, Rab7)	1530:1576	In contrast, when transiently expressed in COS-1 or HeLa cells, human ClC-6 mainly overlaps with markers for early/recycling endosomes (transferrin receptor, EEA-1, Rab5, Rab4) and not with late endosomal/lysosomal markers (LAMP-1, Rab7).
17534424	1	71	theme	membrane	371:378	arg1	excitability					380:391	membrane excitability	371:391	membrane excitability	371:391	BACKGROUND: The mammalian CLC protein family comprises nine members (ClC-1 to -7 and ClC-Ka, -Kb) that function either as plasma membrane chloride channels or as intracellular chloride/proton antiporters, and that sustain a broad spectrum of cellular processes, such as membrane excitability, transepithelial transport, endocytosis and lysosomal degradation.
17534424	3	72	from	N-glycosylated	766:779	arg1	region					786:791	a region	784:791	a region that is evolutionary poorly conserved between mammalian CLC proteins	784:860	PRINCIPAL FINDINGS: Using a polyclonal affinity-purified antibody directed against a unique epitope in the ClC-6 COOH-terminal tail, we show that human ClC-6, when transfected in COS-1 cells, is N-glycosylated in a region that is evolutionary poorly conserved between mammalian CLC proteins and that is located between the predicted helices K and M. Three asparagine residues (N410, N422 and N432) have been defined by mutagenesis as acceptor sites for N-glycosylation, but only two of the three sites seem to be simultaneously N-glycosylated.
17534424	8	73	with	association	1987:1997	arg1	fractions					2033:2041	detergent-resistant membrane fractions	2004:2041	detergent-resistant membrane fractions	2004:2041	Mutating a juxtamembrane string of basic amino acids (amino acids 71-75: KKGRR) disturbs the association with detergent-resistant membrane fractions and also affects the segregation of ClC-6 and ClC-7 when cotransfected in COS-1 cells.
17534424	3	74	gly	N-glycosylated	1099:1112	arg1	sites					1067:1071	the three sites	1057:1071	the three sites	1057:1071	PRINCIPAL FINDINGS: Using a polyclonal affinity-purified antibody directed against a unique epitope in the ClC-6 COOH-terminal tail, we show that human ClC-6, when transfected in COS-1 cells, is N-glycosylated in a region that is evolutionary poorly conserved between mammalian CLC proteins and that is located between the predicted helices K and M. Three asparagine residues (N410, N422 and N432) have been defined by mutagenesis as acceptor sites for N-glycosylation, but only two of the three sites seem to be simultaneously N-glycosylated.
17534424	3	74	gly	N-glycosylated	1099:1112	arg1	two					1050:1052	two	1050:1052	two	1050:1052	PRINCIPAL FINDINGS: Using a polyclonal affinity-purified antibody directed against a unique epitope in the ClC-6 COOH-terminal tail, we show that human ClC-6, when transfected in COS-1 cells, is N-glycosylated in a region that is evolutionary poorly conserved between mammalian CLC proteins and that is located between the predicted helices K and M. Three asparagine residues (N410, N422 and N432) have been defined by mutagenesis as acceptor sites for N-glycosylation, but only two of the three sites seem to be simultaneously N-glycosylated.
17534424	4	75	theme	human	1135:1139	arg1	line					1160:1163	human neuroblastoma cell line	1135:1163	a differentiated human neuroblastoma cell line (SH-SY5Y)	1118:1173	In a differentiated human neuroblastoma cell line (SH-SY5Y), endogenous ClC-6 colocalizes with LAMP-1, a late endosomal/lysosomal marker, but not with early/recycling endosomal markers such as EEA-1 and transferrin receptor.
17534424	4	75	theme	human	1135:1139	arg1	SH-SY5Y					1166:1172	SH-SY5Y	1166:1172	SH-SY5Y	1166:1172	In a differentiated human neuroblastoma cell line (SH-SY5Y), endogenous ClC-6 colocalizes with LAMP-1, a late endosomal/lysosomal marker, but not with early/recycling endosomal markers such as EEA-1 and transferrin receptor.
17534424	1	76	theme	CLC	127:129	arg1	family					139:144	The mammalian CLC protein family	113:144	The mammalian CLC protein family	113:144	BACKGROUND: The mammalian CLC protein family comprises nine members (ClC-1 to -7 and ClC-Ka, -Kb) that function either as plasma membrane chloride channels or as intracellular chloride/proton antiporters, and that sustain a broad spectrum of cellular processes, such as membrane excitability, transepithelial transport, endocytosis and lysosomal degradation.
17534424	9	77	theme	human	2160:2164	arg1	ClC-6					2166:2170	human ClC-6	2160:2170	human ClC-6	2160:2170	CONCLUSIONS: We conclude that human ClC-6 is an endosomal glycoprotein that partitions in detergent resistant lipid domains.
17534424	9	77	theme	human	2160:2164	arg1	glycoprotein					2188:2199	an endosomal glycoprotein	2175:2199	an endosomal glycoprotein that partitions in detergent resistant lipid domains	2175:2252	CONCLUSIONS: We conclude that human ClC-6 is an endosomal glycoprotein that partitions in detergent resistant lipid domains.
17534424	8	78	theme	juxtamembrane	1905:1917	arg1	string					1919:1924	a juxtamembrane string	1903:1924	a juxtamembrane string of basic amino acids (amino acids 71-75: KKGRR)	1903:1972	Mutating a juxtamembrane string of basic amino acids (amino acids 71-75: KKGRR) disturbs the association with detergent-resistant membrane fractions and also affects the segregation of ClC-6 and ClC-7 when cotransfected in COS-1 cells.
17534424	6	79	theme	early/recycling	1656:1670	arg1	localization					1682:1693	an early/recycling endosomal localization	1653:1693	an early/recycling endosomal localization of the exogenously expressed ClC-6 protein	1653:1736	Analogously, overexpression of human ClC-6 in SH-SY5Y cells also leads to an early/recycling endosomal localization of the exogenously expressed ClC-6 protein.
17534424	9	80	gly	glycoprotein	2188:2199	arg1	ClC-6					2166:2170	human ClC-6	2160:2170	human ClC-6	2160:2170	CONCLUSIONS: We conclude that human ClC-6 is an endosomal glycoprotein that partitions in detergent resistant lipid domains.
17534424	9	80	gly	glycoprotein	2188:2199	arg1	glycoprotein					2188:2199	an endosomal glycoprotein	2175:2199	an endosomal glycoprotein that partitions in detergent resistant lipid domains	2175:2252	CONCLUSIONS: We conclude that human ClC-6 is an endosomal glycoprotein that partitions in detergent resistant lipid domains.
17534424	10	81	theme	rate-limiting	2486:2498	arg1	step					2508:2511	a rate-limiting sorting step	2484:2511	a rate-limiting sorting step for ClC-6 between early endosomes and its final destination in late endosomes	2484:2589	The differential sorting of endogenous (late endosomal) versus overexpressed (early and recycling endosomal) ClC-6 is reminiscent of that of other late endosomal/lysosomal membrane proteins (e.g. LIMP II), and is consistent with a rate-limiting sorting step for ClC-6 between early endosomes and its final destination in late endosomes.
17534424	0	82	theme	lipid	86:90	arg1	domains					92:98	detergent-resistant lipid domains	66:98	detergent-resistant lipid domains	66:98	Human ClC-6 is a late endosomal glycoprotein that associates with detergent-resistant lipid domains.
17534424	3	83	theme	acceptor	1005:1012	arg1	FINDINGS					581:588	PRINCIPAL FINDINGS	571:588	PRINCIPAL FINDINGS: Using a polyclonal affinity-purified antibody directed against a unique epitope in the ClC-6 COOH-terminal tail, we show that human ClC-6, when transfected in COS-1 cells, is N-glycosylated in a region that is evolutionary poorly conserved between mammalian CLC proteins and that is located between the predicted helices K and M. Three asparagine residues (N410, N422 and N432)	571:967	PRINCIPAL FINDINGS: Using a polyclonal affinity-purified antibody directed against a unique epitope in the ClC-6 COOH-terminal tail, we show that human ClC-6, when transfected in COS-1 cells, is N-glycosylated in a region that is evolutionary poorly conserved between mammalian CLC proteins and that is located between the predicted helices K and M. Three asparagine residues (N410, N422 and N432) have been defined by mutagenesis as acceptor sites for N-glycosylation, but only two of the three sites seem to be simultaneously N-glycosylated.
17534424	3	83	theme	acceptor	1005:1012	arg1	sites					1014:1018	acceptor sites	1005:1018	acceptor sites for N-glycosylation	1005:1038	PRINCIPAL FINDINGS: Using a polyclonal affinity-purified antibody directed against a unique epitope in the ClC-6 COOH-terminal tail, we show that human ClC-6, when transfected in COS-1 cells, is N-glycosylated in a region that is evolutionary poorly conserved between mammalian CLC proteins and that is located between the predicted helices K and M. Three asparagine residues (N410, N422 and N432) have been defined by mutagenesis as acceptor sites for N-glycosylation, but only two of the three sites seem to be simultaneously N-glycosylated.
17534424	3	84	dep	K	912:912	arg1	N432					963:966	N432	963:966	N432	963:966	PRINCIPAL FINDINGS: Using a polyclonal affinity-purified antibody directed against a unique epitope in the ClC-6 COOH-terminal tail, we show that human ClC-6, when transfected in COS-1 cells, is N-glycosylated in a region that is evolutionary poorly conserved between mammalian CLC proteins and that is located between the predicted helices K and M. Three asparagine residues (N410, N422 and N432) have been defined by mutagenesis as acceptor sites for N-glycosylation, but only two of the three sites seem to be simultaneously N-glycosylated.
17534424	3	84	dep	K	912:912	arg1	N422					954:957	N422	954:957	N422	954:957	PRINCIPAL FINDINGS: Using a polyclonal affinity-purified antibody directed against a unique epitope in the ClC-6 COOH-terminal tail, we show that human ClC-6, when transfected in COS-1 cells, is N-glycosylated in a region that is evolutionary poorly conserved between mammalian CLC proteins and that is located between the predicted helices K and M. Three asparagine residues (N410, N422 and N432) have been defined by mutagenesis as acceptor sites for N-glycosylation, but only two of the three sites seem to be simultaneously N-glycosylated.
17534424	3	84	dep	K	912:912	arg1	N410					948:951	N410	948:951	N410	948:951	PRINCIPAL FINDINGS: Using a polyclonal affinity-purified antibody directed against a unique epitope in the ClC-6 COOH-terminal tail, we show that human ClC-6, when transfected in COS-1 cells, is N-glycosylated in a region that is evolutionary poorly conserved between mammalian CLC proteins and that is located between the predicted helices K and M. Three asparagine residues (N410, N422 and N432) have been defined by mutagenesis as acceptor sites for N-glycosylation, but only two of the three sites seem to be simultaneously N-glycosylated.
17534424	3	84	dep	K	912:912	arg1	residues					938:945	Three asparagine residues	921:945	Three asparagine residues	921:945	PRINCIPAL FINDINGS: Using a polyclonal affinity-purified antibody directed against a unique epitope in the ClC-6 COOH-terminal tail, we show that human ClC-6, when transfected in COS-1 cells, is N-glycosylated in a region that is evolutionary poorly conserved between mammalian CLC proteins and that is located between the predicted helices K and M. Three asparagine residues (N410, N422 and N432) have been defined by mutagenesis as acceptor sites for N-glycosylation, but only two of the three sites seem to be simultaneously N-glycosylated.
17534424	6	85	theme	ClC-6	1616:1620	arg1	overexpression					1592:1605	overexpression	1592:1605	overexpression of human ClC-6 in SH-SY5Y cells	1592:1637	Analogously, overexpression of human ClC-6 in SH-SY5Y cells also leads to an early/recycling endosomal localization of the exogenously expressed ClC-6 protein.
17534424	8	86	theme	amino	1935:1939	arg1	acids					1941:1945	basic amino acids	1929:1945	basic amino acids (amino acids 71-75: KKGRR)	1929:1972	Mutating a juxtamembrane string of basic amino acids (amino acids 71-75: KKGRR) disturbs the association with detergent-resistant membrane fractions and also affects the segregation of ClC-6 and ClC-7 when cotransfected in COS-1 cells.
17534424	1	87	theme	broad	325:329	arg1	channels					248:255	plasma membrane chloride channels	223:255	plasma membrane chloride channels	223:255	BACKGROUND: The mammalian CLC protein family comprises nine members (ClC-1 to -7 and ClC-Ka, -Kb) that function either as plasma membrane chloride channels or as intracellular chloride/proton antiporters, and that sustain a broad spectrum of cellular processes, such as membrane excitability, transepithelial transport, endocytosis and lysosomal degradation.
17534424	1	87	theme	broad	325:329	arg1	spectrum					331:338	a broad spectrum	323:338	a broad spectrum of cellular processes, such as membrane excitability, transepithelial transport, endocytosis and lysosomal degradation	323:457	BACKGROUND: The mammalian CLC protein family comprises nine members (ClC-1 to -7 and ClC-Ka, -Kb) that function either as plasma membrane chloride channels or as intracellular chloride/proton antiporters, and that sustain a broad spectrum of cellular processes, such as membrane excitability, transepithelial transport, endocytosis and lysosomal degradation.
17534424	1	87	theme	broad	325:329	arg1	members					161:167	nine members	156:167	nine members (ClC-1 to -7 and ClC-Ka, -Kb) that function either as plasma membrane chloride channels or as intracellular chloride/proton antiporters, and that sustain a broad spectrum of cellular processes, such as membrane excitability, transepithelial transport, endocytosis and lysosomal degradation	156:457	BACKGROUND: The mammalian CLC protein family comprises nine members (ClC-1 to -7 and ClC-Ka, -Kb) that function either as plasma membrane chloride channels or as intracellular chloride/proton antiporters, and that sustain a broad spectrum of cellular processes, such as membrane excitability, transepithelial transport, endocytosis and lysosomal degradation.
17534424	7	88	theme	lipid	1881:1885	arg1	rafts					1887:1891	lipid rafts	1881:1891	lipid rafts	1881:1891	Finally, in transiently transfected COS-1 cells, ClC-6 copurifies with detergent-resistant membrane fractions, suggesting its partitioning in lipid rafts.
17534424	3	89	theme	CLC	849:851	arg1	proteins					853:860	mammalian CLC proteins	839:860	mammalian CLC proteins	839:860	PRINCIPAL FINDINGS: Using a polyclonal affinity-purified antibody directed against a unique epitope in the ClC-6 COOH-terminal tail, we show that human ClC-6, when transfected in COS-1 cells, is N-glycosylated in a region that is evolutionary poorly conserved between mammalian CLC proteins and that is located between the predicted helices K and M. Three asparagine residues (N410, N422 and N432) have been defined by mutagenesis as acceptor sites for N-glycosylation, but only two of the three sites seem to be simultaneously N-glycosylated.
17534424	4	90	theme	endogenous	1176:1185	arg1	ClC-6					1187:1191	endogenous ClC-6	1176:1191	endogenous ClC-6	1176:1191	In a differentiated human neuroblastoma cell line (SH-SY5Y), endogenous ClC-6 colocalizes with LAMP-1, a late endosomal/lysosomal marker, but not with early/recycling endosomal markers such as EEA-1 and transferrin receptor.
17534424	2	91	theme	human	486:490	arg1	ClC-6					492:496	human ClC-6	486:496	human ClC-6	486:496	In this study we focus on human ClC-6, which is structurally most related to the late endosomal/lysomal ClC-7.
17534424	6	92	theme	SH-SY5Y	1625:1631	arg1	cells					1633:1637	SH-SY5Y cells	1625:1637	SH-SY5Y cells	1625:1637	Analogously, overexpression of human ClC-6 in SH-SY5Y cells also leads to an early/recycling endosomal localization of the exogenously expressed ClC-6 protein.
17534424	4	93	theme	cell	1155:1158	arg1	line					1160:1163	human neuroblastoma cell line	1135:1163	a differentiated human neuroblastoma cell line (SH-SY5Y)	1118:1173	In a differentiated human neuroblastoma cell line (SH-SY5Y), endogenous ClC-6 colocalizes with LAMP-1, a late endosomal/lysosomal marker, but not with early/recycling endosomal markers such as EEA-1 and transferrin receptor.
17534424	4	93	theme	cell	1155:1158	arg1	SH-SY5Y					1166:1172	SH-SY5Y	1166:1172	SH-SY5Y	1166:1172	In a differentiated human neuroblastoma cell line (SH-SY5Y), endogenous ClC-6 colocalizes with LAMP-1, a late endosomal/lysosomal marker, but not with early/recycling endosomal markers such as EEA-1 and transferrin receptor.
17534424	1	94	theme	processes	352:360	arg1	channels					248:255	plasma membrane chloride channels	223:255	plasma membrane chloride channels	223:255	BACKGROUND: The mammalian CLC protein family comprises nine members (ClC-1 to -7 and ClC-Ka, -Kb) that function either as plasma membrane chloride channels or as intracellular chloride/proton antiporters, and that sustain a broad spectrum of cellular processes, such as membrane excitability, transepithelial transport, endocytosis and lysosomal degradation.
17534424	1	94	theme	processes	352:360	arg1	spectrum					331:338	a broad spectrum	323:338	a broad spectrum of cellular processes, such as membrane excitability, transepithelial transport, endocytosis and lysosomal degradation	323:457	BACKGROUND: The mammalian CLC protein family comprises nine members (ClC-1 to -7 and ClC-Ka, -Kb) that function either as plasma membrane chloride channels or as intracellular chloride/proton antiporters, and that sustain a broad spectrum of cellular processes, such as membrane excitability, transepithelial transport, endocytosis and lysosomal degradation.
17534424	1	94	theme	processes	352:360	arg1	members					161:167	nine members	156:167	nine members (ClC-1 to -7 and ClC-Ka, -Kb) that function either as plasma membrane chloride channels or as intracellular chloride/proton antiporters, and that sustain a broad spectrum of cellular processes, such as membrane excitability, transepithelial transport, endocytosis and lysosomal degradation	156:457	BACKGROUND: The mammalian CLC protein family comprises nine members (ClC-1 to -7 and ClC-Ka, -Kb) that function either as plasma membrane chloride channels or as intracellular chloride/proton antiporters, and that sustain a broad spectrum of cellular processes, such as membrane excitability, transepithelial transport, endocytosis and lysosomal degradation.
17534424	8	95	theme	membrane	2024:2031	arg1	fractions					2033:2041	detergent-resistant membrane fractions	2004:2041	detergent-resistant membrane fractions	2004:2041	Mutating a juxtamembrane string of basic amino acids (amino acids 71-75: KKGRR) disturbs the association with detergent-resistant membrane fractions and also affects the segregation of ClC-6 and ClC-7 when cotransfected in COS-1 cells.
17534424	6	96	from	overexpression	1592:1605	arg1	cells					1633:1637	SH-SY5Y cells	1625:1637	SH-SY5Y cells	1625:1637	Analogously, overexpression of human ClC-6 in SH-SY5Y cells also leads to an early/recycling endosomal localization of the exogenously expressed ClC-6 protein.
17534424	6	97	theme	protein	1730:1736	arg1	localization					1682:1693	an early/recycling endosomal localization	1653:1693	an early/recycling endosomal localization of the exogenously expressed ClC-6 protein	1653:1736	Analogously, overexpression of human ClC-6 in SH-SY5Y cells also leads to an early/recycling endosomal localization of the exogenously expressed ClC-6 protein.
17534424	5	98	theme	human	1404:1408	arg1	ClC-6					1410:1414	human ClC-6	1404:1414	human ClC-6	1404:1414	In contrast, when transiently expressed in COS-1 or HeLa cells, human ClC-6 mainly overlaps with markers for early/recycling endosomes (transferrin receptor, EEA-1, Rab5, Rab4) and not with late endosomal/lysosomal markers (LAMP-1, Rab7).
17534424	9	99	theme	resistant	2230:2238	arg1	domains					2246:2252	detergent resistant lipid domains	2220:2252	detergent resistant lipid domains	2220:2252	CONCLUSIONS: We conclude that human ClC-6 is an endosomal glycoprotein that partitions in detergent resistant lipid domains.
17534424	10	100	theme	ClC-6	2364:2368	arg1	reminiscent					2373:2383	reminiscent	2373:2383	reminiscent	2373:2383	The differential sorting of endogenous (late endosomal) versus overexpressed (early and recycling endosomal) ClC-6 is reminiscent of that of other late endosomal/lysosomal membrane proteins (e.g. LIMP II), and is consistent with a rate-limiting sorting step for ClC-6 between early endosomes and its final destination in late endosomes.
17534424	10	100	theme	ClC-6	2364:2368	arg1	consistent					2468:2477	consistent	2468:2477	consistent	2468:2477	The differential sorting of endogenous (late endosomal) versus overexpressed (early and recycling endosomal) ClC-6 is reminiscent of that of other late endosomal/lysosomal membrane proteins (e.g. LIMP II), and is consistent with a rate-limiting sorting step for ClC-6 between early endosomes and its final destination in late endosomes.
17534424	10	100	theme	ClC-6	2364:2368	arg1	sorting					2272:2278	The differential sorting	2255:2278	The differential sorting of endogenous (late endosomal) versus overexpressed (early and recycling endosomal) ClC-6	2255:2368	The differential sorting of endogenous (late endosomal) versus overexpressed (early and recycling endosomal) ClC-6 is reminiscent of that of other late endosomal/lysosomal membrane proteins (e.g. LIMP II), and is consistent with a rate-limiting sorting step for ClC-6 between early endosomes and its final destination in late endosomes.
17534424	6	101	theme	expressed	1714:1722	arg1	protein					1730:1736	the exogenously expressed ClC-6 protein	1698:1736	the exogenously expressed ClC-6 protein	1698:1736	Analogously, overexpression of human ClC-6 in SH-SY5Y cells also leads to an early/recycling endosomal localization of the exogenously expressed ClC-6 protein.
17534424	5	102	theme	transferrin	1476:1486	arg1	EEA-1					1498:1502	EEA-1	1498:1502	EEA-1	1498:1502	In contrast, when transiently expressed in COS-1 or HeLa cells, human ClC-6 mainly overlaps with markers for early/recycling endosomes (transferrin receptor, EEA-1, Rab5, Rab4) and not with late endosomal/lysosomal markers (LAMP-1, Rab7).
17534424	5	102	theme	transferrin	1476:1486	arg1	receptor					1488:1495	transferrin receptor	1476:1495	transferrin receptor	1476:1495	In contrast, when transiently expressed in COS-1 or HeLa cells, human ClC-6 mainly overlaps with markers for early/recycling endosomes (transferrin receptor, EEA-1, Rab5, Rab4) and not with late endosomal/lysosomal markers (LAMP-1, Rab7).
17534424	5	102	theme	transferrin	1476:1486	arg1	Rab4					1511:1514	Rab4	1511:1514	Rab4	1511:1514	In contrast, when transiently expressed in COS-1 or HeLa cells, human ClC-6 mainly overlaps with markers for early/recycling endosomes (transferrin receptor, EEA-1, Rab5, Rab4) and not with late endosomal/lysosomal markers (LAMP-1, Rab7).
17534424	10	103	theme	early	2531:2535	arg1	endosomes					2537:2545	early endosomes	2531:2545	early endosomes	2531:2545	The differential sorting of endogenous (late endosomal) versus overexpressed (early and recycling endosomal) ClC-6 is reminiscent of that of other late endosomal/lysosomal membrane proteins (e.g. LIMP II), and is consistent with a rate-limiting sorting step for ClC-6 between early endosomes and its final destination in late endosomes.
17534424	0	104	theme	endosomal	22:30	arg1	glycoprotein					32:43	a late endosomal glycoprotein	15:43	a late endosomal glycoprotein that associates with detergent-resistant lipid domains	15:98	Human ClC-6 is a late endosomal glycoprotein that associates with detergent-resistant lipid domains.
17534424	0	104	theme	endosomal	22:30	arg1	ClC-6					6:10	Human ClC-6	0:10	Human ClC-6	0:10	Human ClC-6 is a late endosomal glycoprotein that associates with detergent-resistant lipid domains.
17534424	1	105	theme	intracellular	263:275	arg1	antiporters					293:303	intracellular chloride/proton antiporters	263:303	intracellular chloride/proton antiporters	263:303	BACKGROUND: The mammalian CLC protein family comprises nine members (ClC-1 to -7 and ClC-Ka, -Kb) that function either as plasma membrane chloride channels or as intracellular chloride/proton antiporters, and that sustain a broad spectrum of cellular processes, such as membrane excitability, transepithelial transport, endocytosis and lysosomal degradation.
17534424	1	105	theme	intracellular	263:275	arg1	members					161:167	nine members	156:167	nine members (ClC-1 to -7 and ClC-Ka, -Kb) that function either as plasma membrane chloride channels or as intracellular chloride/proton antiporters, and that sustain a broad spectrum of cellular processes, such as membrane excitability, transepithelial transport, endocytosis and lysosomal degradation	156:457	BACKGROUND: The mammalian CLC protein family comprises nine members (ClC-1 to -7 and ClC-Ka, -Kb) that function either as plasma membrane chloride channels or as intracellular chloride/proton antiporters, and that sustain a broad spectrum of cellular processes, such as membrane excitability, transepithelial transport, endocytosis and lysosomal degradation.
17534424	7	106	theme	detergent-resistant	1810:1828	arg1	fractions					1839:1847	detergent-resistant membrane fractions	1810:1847	detergent-resistant membrane fractions	1810:1847	Finally, in transiently transfected COS-1 cells, ClC-6 copurifies with detergent-resistant membrane fractions, suggesting its partitioning in lipid rafts.
17534424	3	107	theme	predicted	894:902	arg1	helices					904:910	the predicted helices K and M. Three asparagine residues (N410, N422 and N432)	890:967	the predicted helices K and M. Three asparagine residues (N410, N422 and N432)	890:967	PRINCIPAL FINDINGS: Using a polyclonal affinity-purified antibody directed against a unique epitope in the ClC-6 COOH-terminal tail, we show that human ClC-6, when transfected in COS-1 cells, is N-glycosylated in a region that is evolutionary poorly conserved between mammalian CLC proteins and that is located between the predicted helices K and M. Three asparagine residues (N410, N422 and N432) have been defined by mutagenesis as acceptor sites for N-glycosylation, but only two of the three sites seem to be simultaneously N-glycosylated.
17534424	3	107	theme	predicted	894:902	arg1	M.					918:919	M.	918:919	M.	918:919	PRINCIPAL FINDINGS: Using a polyclonal affinity-purified antibody directed against a unique epitope in the ClC-6 COOH-terminal tail, we show that human ClC-6, when transfected in COS-1 cells, is N-glycosylated in a region that is evolutionary poorly conserved between mammalian CLC proteins and that is located between the predicted helices K and M. Three asparagine residues (N410, N422 and N432) have been defined by mutagenesis as acceptor sites for N-glycosylation, but only two of the three sites seem to be simultaneously N-glycosylated.
17534424	3	107	theme	predicted	894:902	arg1	K					912:912	K	912:912	K	912:912	PRINCIPAL FINDINGS: Using a polyclonal affinity-purified antibody directed against a unique epitope in the ClC-6 COOH-terminal tail, we show that human ClC-6, when transfected in COS-1 cells, is N-glycosylated in a region that is evolutionary poorly conserved between mammalian CLC proteins and that is located between the predicted helices K and M. Three asparagine residues (N410, N422 and N432) have been defined by mutagenesis as acceptor sites for N-glycosylation, but only two of the three sites seem to be simultaneously N-glycosylated.
17534424	10	108	theme	other	2396:2400	arg1	proteins					2436:2443	other late endosomal/lysosomal membrane proteins	2396:2443	other late endosomal/lysosomal membrane proteins (e.g. LIMP II)	2396:2458	The differential sorting of endogenous (late endosomal) versus overexpressed (early and recycling endosomal) ClC-6 is reminiscent of that of other late endosomal/lysosomal membrane proteins (e.g. LIMP II), and is consistent with a rate-limiting sorting step for ClC-6 between early endosomes and its final destination in late endosomes.
17534424	10	108	theme	other	2396:2400	arg1	LIMP					2451:2454	e.g. LIMP II	2446:2457	e.g. LIMP II	2446:2457	The differential sorting of endogenous (late endosomal) versus overexpressed (early and recycling endosomal) ClC-6 is reminiscent of that of other late endosomal/lysosomal membrane proteins (e.g. LIMP II), and is consistent with a rate-limiting sorting step for ClC-6 between early endosomes and its final destination in late endosomes.
17534424	4	109	theme	endosomal/lysosomal	1225:1243	arg1	marker					1245:1250	a late endosomal/lysosomal marker	1218:1250	a late endosomal/lysosomal marker	1218:1250	In a differentiated human neuroblastoma cell line (SH-SY5Y), endogenous ClC-6 colocalizes with LAMP-1, a late endosomal/lysosomal marker, but not with early/recycling endosomal markers such as EEA-1 and transferrin receptor.
17534424	4	109	theme	endosomal/lysosomal	1225:1243	arg1	LAMP-1					1210:1215	LAMP-1	1210:1215	LAMP-1	1210:1215	In a differentiated human neuroblastoma cell line (SH-SY5Y), endogenous ClC-6 colocalizes with LAMP-1, a late endosomal/lysosomal marker, but not with early/recycling endosomal markers such as EEA-1 and transferrin receptor.
17534424	3	110	theme	asparagine	927:936	arg1	residues					938:945	Three asparagine residues	921:945	Three asparagine residues	921:945	PRINCIPAL FINDINGS: Using a polyclonal affinity-purified antibody directed against a unique epitope in the ClC-6 COOH-terminal tail, we show that human ClC-6, when transfected in COS-1 cells, is N-glycosylated in a region that is evolutionary poorly conserved between mammalian CLC proteins and that is located between the predicted helices K and M. Three asparagine residues (N410, N422 and N432) have been defined by mutagenesis as acceptor sites for N-glycosylation, but only two of the three sites seem to be simultaneously N-glycosylated.
17534424	10	111	theme	differential	2259:2270	arg1	reminiscent					2373:2383	reminiscent	2373:2383	reminiscent	2373:2383	The differential sorting of endogenous (late endosomal) versus overexpressed (early and recycling endosomal) ClC-6 is reminiscent of that of other late endosomal/lysosomal membrane proteins (e.g. LIMP II), and is consistent with a rate-limiting sorting step for ClC-6 between early endosomes and its final destination in late endosomes.
17534424	10	111	theme	differential	2259:2270	arg1	consistent					2468:2477	consistent	2468:2477	consistent	2468:2477	The differential sorting of endogenous (late endosomal) versus overexpressed (early and recycling endosomal) ClC-6 is reminiscent of that of other late endosomal/lysosomal membrane proteins (e.g. LIMP II), and is consistent with a rate-limiting sorting step for ClC-6 between early endosomes and its final destination in late endosomes.
17534424	10	111	theme	differential	2259:2270	arg1	sorting					2272:2278	The differential sorting	2255:2278	The differential sorting of endogenous (late endosomal) versus overexpressed (early and recycling endosomal) ClC-6	2255:2368	The differential sorting of endogenous (late endosomal) versus overexpressed (early and recycling endosomal) ClC-6 is reminiscent of that of other late endosomal/lysosomal membrane proteins (e.g. LIMP II), and is consistent with a rate-limiting sorting step for ClC-6 between early endosomes and its final destination in late endosomes.
17534424	3	112	theme	COOH-terminal	684:696	arg1	tail					698:701	the ClC-6 COOH-terminal tail	674:701	the ClC-6 COOH-terminal tail	674:701	PRINCIPAL FINDINGS: Using a polyclonal affinity-purified antibody directed against a unique epitope in the ClC-6 COOH-terminal tail, we show that human ClC-6, when transfected in COS-1 cells, is N-glycosylated in a region that is evolutionary poorly conserved between mammalian CLC proteins and that is located between the predicted helices K and M. Three asparagine residues (N410, N422 and N432) have been defined by mutagenesis as acceptor sites for N-glycosylation, but only two of the three sites seem to be simultaneously N-glycosylated.
17534424	1	113	dep	ClC-1	170:174	arg1	to					176:177	to	176:177	to	176:177	BACKGROUND: The mammalian CLC protein family comprises nine members (ClC-1 to -7 and ClC-Ka, -Kb) that function either as plasma membrane chloride channels or as intracellular chloride/proton antiporters, and that sustain a broad spectrum of cellular processes, such as membrane excitability, transepithelial transport, endocytosis and lysosomal degradation.
17534424	1	113	dep	ClC-1	170:174	arg1	-Kb					194:196	-Kb	194:196	-Kb	194:196	BACKGROUND: The mammalian CLC protein family comprises nine members (ClC-1 to -7 and ClC-Ka, -Kb) that function either as plasma membrane chloride channels or as intracellular chloride/proton antiporters, and that sustain a broad spectrum of cellular processes, such as membrane excitability, transepithelial transport, endocytosis and lysosomal degradation.
17534424	7	114	theme	transfected	1763:1773	arg1	cells					1781:1785	transiently transfected COS-1 cells	1751:1785	transiently transfected COS-1 cells	1751:1785	Finally, in transiently transfected COS-1 cells, ClC-6 copurifies with detergent-resistant membrane fractions, suggesting its partitioning in lipid rafts.
17534424	8	115	theme	ClC-6	2079:2083	arg1	segregation					2064:2074	the segregation	2060:2074	the segregation of ClC-6 and ClC-7	2060:2093	Mutating a juxtamembrane string of basic amino acids (amino acids 71-75: KKGRR) disturbs the association with detergent-resistant membrane fractions and also affects the segregation of ClC-6 and ClC-7 when cotransfected in COS-1 cells.
17534424	0	116	gly	glycoprotein	32:43	arg1	glycoprotein					32:43	a late endosomal glycoprotein	15:43	a late endosomal glycoprotein that associates with detergent-resistant lipid domains	15:98	Human ClC-6 is a late endosomal glycoprotein that associates with detergent-resistant lipid domains.
17534424	0	116	gly	glycoprotein	32:43	arg1	ClC-6					6:10	Human ClC-6	0:10	Human ClC-6	0:10	Human ClC-6 is a late endosomal glycoprotein that associates with detergent-resistant lipid domains.
17534424	8	117	theme	ClC-7	2089:2093	arg1	segregation					2064:2074	the segregation	2060:2074	the segregation of ClC-6 and ClC-7	2060:2093	Mutating a juxtamembrane string of basic amino acids (amino acids 71-75: KKGRR) disturbs the association with detergent-resistant membrane fractions and also affects the segregation of ClC-6 and ClC-7 when cotransfected in COS-1 cells.
17534424	4	118	theme	early/recycling	1266:1280	arg1	EEA-1					1308:1312	EEA-1	1308:1312	EEA-1	1308:1312	In a differentiated human neuroblastoma cell line (SH-SY5Y), endogenous ClC-6 colocalizes with LAMP-1, a late endosomal/lysosomal marker, but not with early/recycling endosomal markers such as EEA-1 and transferrin receptor.
17534424	4	118	theme	early/recycling	1266:1280	arg1	receptor					1330:1337	transferrin receptor	1318:1337	transferrin receptor	1318:1337	In a differentiated human neuroblastoma cell line (SH-SY5Y), endogenous ClC-6 colocalizes with LAMP-1, a late endosomal/lysosomal marker, but not with early/recycling endosomal markers such as EEA-1 and transferrin receptor.
17534424	4	118	theme	early/recycling	1266:1280	arg1	markers					1292:1298	early/recycling endosomal markers	1266:1298	early/recycling endosomal markers such as EEA-1 and transferrin receptor	1266:1337	In a differentiated human neuroblastoma cell line (SH-SY5Y), endogenous ClC-6 colocalizes with LAMP-1, a late endosomal/lysosomal marker, but not with early/recycling endosomal markers such as EEA-1 and transferrin receptor.
22173220	9	0	theme	ligand	1088:1093	arg1	TLRs					1118:1121	other TLRs	1112:1121	other TLRs	1112:1121	Ligand binding in this region would be consistent with the ligand binding sites of other TLRs.
22173220	9	0	theme	ligand	1088:1093	arg1	sites					1103:1107	the ligand binding sites	1084:1107	the ligand binding sites of other TLRs	1084:1121	Ligand binding in this region would be consistent with the ligand binding sites of other TLRs.
22173220	5	1	theme	molecular	662:670	arg1	surface					672:678	the molecular surface	658:678	the molecular surface	658:678	All seven predicted N-linked glycosylation sites are exposed on the molecular surface, away from the dimer interface.
22173220	6	2	theme	first	733:737	arg1	sites					744:748	the first five sites	729:748	the first five sites	729:748	Glycosylation at the first five sites was confirmed by tandem mass spectrometry.
22173220	1	3	theme	single-particle	148:162	arg1	reconstruction					170:183	electron microscopy single-particle image reconstruction	128:183	electron microscopy single-particle image reconstruction	128:183	The structure of full-length human TLR5 determined by electron microscopy single-particle image reconstruction at 26Å resolution shows that TLR5 forms an asymmetric homodimer via ectodomain interactions.
22173220	1	4	theme	ectodomain	253:262	arg1	interactions					264:275	ectodomain interactions	253:275	ectodomain interactions	253:275	The structure of full-length human TLR5 determined by electron microscopy single-particle image reconstruction at 26Å resolution shows that TLR5 forms an asymmetric homodimer via ectodomain interactions.
22173220	0	5	theme	flagellin	63:71	arg1	absence					52:58	the absence	48:58	the absence of flagellin	48:71	Toll-like receptor 5 forms asymmetric dimers in the absence of flagellin.
22173220	5	6	theme	predicted	604:612	arg1	sites					637:641	All seven predicted N-linked glycosylation sites	594:641	All seven predicted N-linked glycosylation sites	594:641	All seven predicted N-linked glycosylation sites are exposed on the molecular surface, away from the dimer interface.
22173220	1	7	theme	image	164:168	arg1	reconstruction					170:183	electron microscopy single-particle image reconstruction	128:183	electron microscopy single-particle image reconstruction	128:183	The structure of full-length human TLR5 determined by electron microscopy single-particle image reconstruction at 26Å resolution shows that TLR5 forms an asymmetric homodimer via ectodomain interactions.
22173220	4	8	theme	homology	514:521	arg1	model					523:527	A TLR5 homology model	507:527	A TLR5 homology model	507:527	A TLR5 homology model was generated and fitted into the electron microscopy structure.
22173220	2	9	theme	ligand	347:352	arg1	absence					336:342	the absence	332:342	the absence of ligand	332:352	The structure shows that like TLR9, TLR5 dimerizes in the absence of ligand.
22173220	5	10	theme	N-linked	614:621	arg1	sites					637:641	All seven predicted N-linked glycosylation sites	594:641	All seven predicted N-linked glycosylation sites	594:641	All seven predicted N-linked glycosylation sites are exposed on the molecular surface, away from the dimer interface.
22173220	9	11	theme	other	1112:1116	arg1	TLRs					1118:1121	other TLRs	1112:1121	other TLRs	1112:1121	Ligand binding in this region would be consistent with the ligand binding sites of other TLRs.
22173220	5	12	theme	glycosylation	623:635	arg1	sites					637:641	All seven predicted N-linked glycosylation sites	594:641	All seven predicted N-linked glycosylation sites	594:641	All seven predicted N-linked glycosylation sites are exposed on the molecular surface, away from the dimer interface.
22173220	5	13	link	N-linked	614:621	arg1	sites					637:641	All seven predicted N-linked glycosylation sites	594:641	All seven predicted N-linked glycosylation sites	594:641	All seven predicted N-linked glycosylation sites are exposed on the molecular surface, away from the dimer interface.
22173220	8	14	from	unobstructed	1004:1015	arg1	contrast					928:935	contrast	928:935	contrast	928:935	In contrast, the central region of the ectodomains near the dimer interface is unobstructed by glycans.
22173220	9	15	from	binding	1036:1042	arg1	region					1052:1057	this region	1047:1057	this region	1047:1057	Ligand binding in this region would be consistent with the ligand binding sites of other TLRs.
22173220	8	16	from	contrast	928:935	arg1	region					950:955	the central region	938:955	the central region of the ectodomains near the dimer interface	938:999	In contrast, the central region of the ectodomains near the dimer interface is unobstructed by glycans.
22173220	8	16	from	contrast	928:935	arg1	unobstructed					1004:1015	unobstructed	1004:1015	unobstructed	1004:1015	In contrast, the central region of the ectodomains near the dimer interface is unobstructed by glycans.
22173220	3	17	theme	dimer	376:380	arg1	asymmetry					359:367	The asymmetry	355:367	The asymmetry of the dimer	355:380	The asymmetry of the dimer suggests that TLR5 may recognize two flagellin molecules cooperatively to establish an optimal flagellin response threshold.
22173220	8	18	theme	dimer	985:989	arg1	interface					991:999	the dimer interface	981:999	the dimer interface	981:999	In contrast, the central region of the ectodomains near the dimer interface is unobstructed by glycans.
22173220	1	19	theme	26Å	188:190	arg1	resolution					192:201	26Å resolution	188:201	26Å resolution	188:201	The structure of full-length human TLR5 determined by electron microscopy single-particle image reconstruction at 26Å resolution shows that TLR5 forms an asymmetric homodimer via ectodomain interactions.
22173220	0	20	theme	Toll-like	0:8	arg1	receptor					10:17	Toll-like receptor 5	0:19	Toll-like receptor 5	0:19	Toll-like receptor 5 forms asymmetric dimers in the absence of flagellin.
22173220	3	21	theme	flagellin	419:427	arg1	molecules					429:437	two flagellin molecules	415:437	two flagellin molecules	415:437	The asymmetry of the dimer suggests that TLR5 may recognize two flagellin molecules cooperatively to establish an optimal flagellin response threshold.
22173220	7	22	from	position	911:918	arg1	glycan					901:906	a glycan	899:906	a glycan at position 342	899:922	Two aspartate residues proposed to interact with flagellin (Asp294 and Asp366) are sterically occluded by a glycan at position 342.
22173220	8	23	theme	ectodomains	964:974	arg1	region					950:955	the central region	938:955	the central region of the ectodomains near the dimer interface	938:999	In contrast, the central region of the ectodomains near the dimer interface is unobstructed by glycans.
22173220	8	23	theme	ectodomains	964:974	arg1	unobstructed					1004:1015	unobstructed	1004:1015	unobstructed	1004:1015	In contrast, the central region of the ectodomains near the dimer interface is unobstructed by glycans.
22173220	4	24	theme	microscopy	572:581	arg1	structure					583:591	the electron microscopy structure	559:591	the electron microscopy structure	559:591	A TLR5 homology model was generated and fitted into the electron microscopy structure.
22173220	1	25	theme	full-length	91:101	arg1	TLR5					109:112	full-length human TLR5	91:112	full-length human TLR5	91:112	The structure of full-length human TLR5 determined by electron microscopy single-particle image reconstruction at 26Å resolution shows that TLR5 forms an asymmetric homodimer via ectodomain interactions.
22173220	9	26	theme	binding	1095:1101	arg1	TLRs					1118:1121	other TLRs	1112:1121	other TLRs	1112:1121	Ligand binding in this region would be consistent with the ligand binding sites of other TLRs.
22173220	9	26	theme	binding	1095:1101	arg1	sites					1103:1107	the ligand binding sites	1084:1107	the ligand binding sites of other TLRs	1084:1121	Ligand binding in this region would be consistent with the ligand binding sites of other TLRs.
22173220	3	27	theme	optimal	469:475	arg1	threshold					496:504	an optimal flagellin response threshold	466:504	an optimal flagellin response threshold	466:504	The asymmetry of the dimer suggests that TLR5 may recognize two flagellin molecules cooperatively to establish an optimal flagellin response threshold.
22173220	4	28	theme	electron	563:570	arg1	structure					583:591	the electron microscopy structure	559:591	the electron microscopy structure	559:591	A TLR5 homology model was generated and fitted into the electron microscopy structure.
22173220	0	29	theme	asymmetric	27:36	arg1	dimers					38:43	asymmetric dimers	27:43	asymmetric dimers	27:43	Toll-like receptor 5 forms asymmetric dimers in the absence of flagellin.
22173220	6	30	theme	mass	774:777	arg1	spectrometry					779:790	tandem mass spectrometry	767:790	tandem mass spectrometry	767:790	Glycosylation at the first five sites was confirmed by tandem mass spectrometry.
22173220	7	31	theme	aspartate	797:805	arg1	residues					807:814	Two aspartate residues	793:814	Two aspartate residues proposed to interact with flagellin (Asp294 and Asp366)	793:870	Two aspartate residues proposed to interact with flagellin (Asp294 and Asp366) are sterically occluded by a glycan at position 342.
22173220	6	32	theme	tandem	767:772	arg1	spectrometry					779:790	tandem mass spectrometry	767:790	tandem mass spectrometry	767:790	Glycosylation at the first five sites was confirmed by tandem mass spectrometry.
22173220	1	33	theme	human	103:107	arg1	TLR5					109:112	full-length human TLR5	91:112	full-length human TLR5	91:112	The structure of full-length human TLR5 determined by electron microscopy single-particle image reconstruction at 26Å resolution shows that TLR5 forms an asymmetric homodimer via ectodomain interactions.
22173220	9	34	with	consistent	1068:1077	arg1	TLRs					1118:1121	other TLRs	1112:1121	other TLRs	1112:1121	Ligand binding in this region would be consistent with the ligand binding sites of other TLRs.
22173220	9	34	with	consistent	1068:1077	arg1	sites					1103:1107	the ligand binding sites	1084:1107	the ligand binding sites of other TLRs	1084:1121	Ligand binding in this region would be consistent with the ligand binding sites of other TLRs.
22173220	9	35	theme	TLRs	1118:1121	arg1	TLRs					1118:1121	other TLRs	1112:1121	other TLRs	1112:1121	Ligand binding in this region would be consistent with the ligand binding sites of other TLRs.
22173220	9	35	theme	TLRs	1118:1121	arg1	sites					1103:1107	the ligand binding sites	1084:1107	the ligand binding sites of other TLRs	1084:1121	Ligand binding in this region would be consistent with the ligand binding sites of other TLRs.
22173220	1	36	theme	TLR5	109:112	arg1	structure					78:86	The structure	74:86	The structure of full-length human TLR5 determined by electron microscopy single-particle image reconstruction at 26Å resolution	74:201	The structure of full-length human TLR5 determined by electron microscopy single-particle image reconstruction at 26Å resolution shows that TLR5 forms an asymmetric homodimer via ectodomain interactions.
22173220	5	37	theme	dimer	695:699	arg1	interface					701:709	the dimer interface	691:709	the dimer interface	691:709	All seven predicted N-linked glycosylation sites are exposed on the molecular surface, away from the dimer interface.
22173220	3	38	theme	flagellin	477:485	arg1	threshold					496:504	an optimal flagellin response threshold	466:504	an optimal flagellin response threshold	466:504	The asymmetry of the dimer suggests that TLR5 may recognize two flagellin molecules cooperatively to establish an optimal flagellin response threshold.
22173220	6	39	from	sites	744:748	arg1	Glycosylation					712:724	Glycosylation	712:724	Glycosylation at the first five sites	712:748	Glycosylation at the first five sites was confirmed by tandem mass spectrometry.
22173220	8	40	theme	central	942:948	arg1	region					950:955	the central region	938:955	the central region of the ectodomains near the dimer interface	938:999	In contrast, the central region of the ectodomains near the dimer interface is unobstructed by glycans.
22173220	8	40	theme	central	942:948	arg1	unobstructed					1004:1015	unobstructed	1004:1015	unobstructed	1004:1015	In contrast, the central region of the ectodomains near the dimer interface is unobstructed by glycans.
22173220	3	41	theme	response	487:494	arg1	threshold					496:504	an optimal flagellin response threshold	466:504	an optimal flagellin response threshold	466:504	The asymmetry of the dimer suggests that TLR5 may recognize two flagellin molecules cooperatively to establish an optimal flagellin response threshold.
22173220	1	42	theme	asymmetric	228:237	arg1	homodimer					239:247	an asymmetric homodimer	225:247	an asymmetric homodimer	225:247	The structure of full-length human TLR5 determined by electron microscopy single-particle image reconstruction at 26Å resolution shows that TLR5 forms an asymmetric homodimer via ectodomain interactions.
22173220	6	43	gly	Glycosylation	712:724	arg2	sites					744:748	the first five sites	729:748	the first five sites	729:748	Glycosylation at the first five sites was confirmed by tandem mass spectrometry.
22173220	7	44	dep	flagellin	842:850	arg1	Asp366					864:869	Asp366	864:869	Asp366	864:869	Two aspartate residues proposed to interact with flagellin (Asp294 and Asp366) are sterically occluded by a glycan at position 342.
22173220	7	44	dep	flagellin	842:850	arg1	Asp294					853:858	Asp294	853:858	Asp294	853:858	Two aspartate residues proposed to interact with flagellin (Asp294 and Asp366) are sterically occluded by a glycan at position 342.
22173220	1	45	theme	electron	128:135	arg1	microscopy					137:146	electron microscopy	128:146	electron microscopy single-particle image reconstruction	128:183	The structure of full-length human TLR5 determined by electron microscopy single-particle image reconstruction at 26Å resolution shows that TLR5 forms an asymmetric homodimer via ectodomain interactions.
22173220	9	46	theme	Ligand	1029:1034	arg1	binding					1036:1042	Ligand binding	1029:1042	Ligand binding in this region	1029:1057	Ligand binding in this region would be consistent with the ligand binding sites of other TLRs.
22173220	4	47	theme	TLR5	509:512	arg1	model					523:527	A TLR5 homology model	507:527	A TLR5 homology model	507:527	A TLR5 homology model was generated and fitted into the electron microscopy structure.
22173220	1	48	theme	microscopy	137:146	arg1	reconstruction					170:183	electron microscopy single-particle image reconstruction	128:183	electron microscopy single-particle image reconstruction	128:183	The structure of full-length human TLR5 determined by electron microscopy single-particle image reconstruction at 26Å resolution shows that TLR5 forms an asymmetric homodimer via ectodomain interactions.
22173220	5	49	gly	glycosylation	623:635	arg2	sites					637:641	All seven predicted N-linked glycosylation sites	594:641	All seven predicted N-linked glycosylation sites	594:641	All seven predicted N-linked glycosylation sites are exposed on the molecular surface, away from the dimer interface.
22173220	5	49	gly	glycosylation	623:635	arg2	seven					598:602	seven	598:602	seven	598:602	All seven predicted N-linked glycosylation sites are exposed on the molecular surface, away from the dimer interface.
10486146	0	0	theme	extracellular	69:81	arg1	domains					83:89	extracellular domains	69:89	extracellular domains	69:89	Characterization of recombinant human CXCR4 in insect cells: role of extracellular domains and N-glycosylation in ligand binding.
10486146	7	1	theme	N-glycosylation	853:867	arg1	Asn-176					887:893	Asn-176	887:893	Asn-176	887:893	Two potential N-glycosylation sites (Asn-11 and Asn-176) were either singly or doubly mutated to a leucine residue.
10486146	7	1	theme	N-glycosylation	853:867	arg1	Asn-11					876:881	Asn-11	876:881	Asn-11	876:881	Two potential N-glycosylation sites (Asn-11 and Asn-176) were either singly or doubly mutated to a leucine residue.
10486146	7	1	theme	N-glycosylation	853:867	arg1	sites					869:873	Two potential N-glycosylation sites	839:873	Two potential N-glycosylation sites (Asn-11 and Asn-176)	839:894	Two potential N-glycosylation sites (Asn-11 and Asn-176) were either singly or doubly mutated to a leucine residue.
10486146	7	2	dep	sites	869:873	arg1	Asn-176					887:893	Asn-176	887:893	Asn-176	887:893	Two potential N-glycosylation sites (Asn-11 and Asn-176) were either singly or doubly mutated to a leucine residue.
10486146	7	2	dep	sites	869:873	arg1	Asn-11					876:881	Asn-11	876:881	Asn-11	876:881	Two potential N-glycosylation sites (Asn-11 and Asn-176) were either singly or doubly mutated to a leucine residue.
10486146	7	2	dep	sites	869:873	arg1	sites					869:873	Two potential N-glycosylation sites	839:873	Two potential N-glycosylation sites (Asn-11 and Asn-176)	839:894	Two potential N-glycosylation sites (Asn-11 and Asn-176) were either singly or doubly mutated to a leucine residue.
10486146	1	3	theme	human	146:150	arg1	CXCR4/fusin					152:162	the human CXCR4/fusin	142:162	the human CXCR4/fusin	142:162	The cDNA of the human CXCR4/fusin was isolated from a human HeLa cell cDNA library by PCR and functionally expressed in Sf9 insect cells.
10486146	0	4	from	Characterization	0:15	arg1	cells					54:58	insect cells	47:58	insect cells	47:58	Characterization of recombinant human CXCR4 in insect cells: role of extracellular domains and N-glycosylation in ligand binding.
10486146	8	5	theme	significant	996:1006	arg1	decrease					1008:1015	a significant decrease	994:1015	a significant decrease in ligand binding activity and affinity	994:1055	Both single mutant receptors exhibited a significant decrease in ligand binding activity and affinity.
10486146	3	6	theme	different	545:553	arg1	domains					555:561	the different domains	541:561	the different domains of the receptor and the ligand	541:592	Sequence-specific antibodies against each of the four extracellular domains were generated and used to investigate the interactions between the different domains of the receptor and the ligand.
10486146	3	6	theme	different	545:553	arg1	receptor					570:577	the receptor	566:577	the receptor	566:577	Sequence-specific antibodies against each of the four extracellular domains were generated and used to investigate the interactions between the different domains of the receptor and the ligand.
10486146	3	6	theme	different	545:553	arg1	ligand					587:592	the ligand	583:592	the ligand	583:592	Sequence-specific antibodies against each of the four extracellular domains were generated and used to investigate the interactions between the different domains of the receptor and the ligand.
10486146	8	7	from	decrease	1008:1015	arg1	affinity					1048:1055	affinity	1048:1055	affinity	1048:1055	Both single mutant receptors exhibited a significant decrease in ligand binding activity and affinity.
10486146	8	7	from	decrease	1008:1015	arg1	activity					1035:1042	ligand binding activity	1020:1042	ligand binding activity	1020:1042	Both single mutant receptors exhibited a significant decrease in ligand binding activity and affinity.
10486146	0	8	theme	domains	83:89	arg1	role					61:64	role	61:64	Characterization of recombinant human CXCR4 in insect cells: role of extracellular domains and N-glycosylation in ligand binding.	0:128	Characterization of recombinant human CXCR4 in insect cells: role of extracellular domains and N-glycosylation in ligand binding.
10486146	10	9	theme	extracellular	1150:1162	arg1	domains					1164:1170	the extracellular domains	1146:1170	the extracellular domains	1146:1170	Our data suggest that all of the extracellular domains are involved in ligand-receptor interactions and that N-glycosylation is required to maintain high-affinity ligand binding.
10486146	10	10	theme	ligand	1280:1285	arg1	binding					1287:1293	high-affinity ligand binding	1266:1293	high-affinity ligand binding	1266:1293	Our data suggest that all of the extracellular domains are involved in ligand-receptor interactions and that N-glycosylation is required to maintain high-affinity ligand binding.
10486146	6	11	from	role	713:716	arg1	binding					756:762	ligand binding	749:762	ligand binding	749:762	The role of N-glycosylation of CXCR4 in ligand binding was investigated in the insect cells overexpressed with recombinant CXCR4.
10486146	4	12	theme	ligand	655:660	arg1	binding					662:668	ligand binding	655:668	ligand binding	655:668	Each of the four antibodies was found to be able to inhibit ligand binding.
10486146	6	13	theme	ligand	749:754	arg1	binding					756:762	ligand binding	749:762	ligand binding	749:762	The role of N-glycosylation of CXCR4 in ligand binding was investigated in the insect cells overexpressed with recombinant CXCR4.
10486146	10	14	theme	high-affinity	1266:1278	arg1	binding					1287:1293	high-affinity ligand binding	1266:1293	high-affinity ligand binding	1266:1293	Our data suggest that all of the extracellular domains are involved in ligand-receptor interactions and that N-glycosylation is required to maintain high-affinity ligand binding.
10486146	1	15	theme	CXCR4/fusin	152:162	arg1	cDNA					134:137	The cDNA	130:137	The cDNA of the human CXCR4/fusin	130:162	The cDNA of the human CXCR4/fusin was isolated from a human HeLa cell cDNA library by PCR and functionally expressed in Sf9 insect cells.
10486146	0	16	theme	N-glycosylation	95:109	arg1	role					61:64	role	61:64	Characterization of recombinant human CXCR4 in insect cells: role of extracellular domains and N-glycosylation in ligand binding.	0:128	Characterization of recombinant human CXCR4 in insect cells: role of extracellular domains and N-glycosylation in ligand binding.
10486146	2	17	theme	comparable	358:367	arg1	affinity					349:356	an affinity	346:356	an affinity comparable to that of the native receptor	346:398	The recombinant receptor was found to bind its natural ligand SDF-1alpha with an affinity comparable to that of the native receptor.
10486146	8	18	theme	binding	1027:1033	arg1	activity					1035:1042	ligand binding activity	1020:1042	ligand binding activity	1020:1042	Both single mutant receptors exhibited a significant decrease in ligand binding activity and affinity.
10486146	6	19	theme	CXCR4	740:744	arg1	N-glycosylation					721:735	N-glycosylation	721:735	N-glycosylation of CXCR4	721:744	The role of N-glycosylation of CXCR4 in ligand binding was investigated in the insect cells overexpressed with recombinant CXCR4.
10486146	1	20	theme	Sf9	250:252	arg1	cells					261:265	Sf9 insect cells	250:265	Sf9 insect cells	250:265	The cDNA of the human CXCR4/fusin was isolated from a human HeLa cell cDNA library by PCR and functionally expressed in Sf9 insect cells.
10486146	8	21	theme	ligand	1020:1025	arg1	activity					1035:1042	ligand binding activity	1020:1042	ligand binding activity	1020:1042	Both single mutant receptors exhibited a significant decrease in ligand binding activity and affinity.
10486146	8	22	theme	mutant	967:972	arg1	receptors					974:982	Both single mutant receptors	955:982	Both single mutant receptors	955:982	Both single mutant receptors exhibited a significant decrease in ligand binding activity and affinity.
10486146	0	23	theme	human	32:36	arg1	CXCR4					38:42	recombinant human CXCR4	20:42	recombinant human CXCR4	20:42	Characterization of recombinant human CXCR4 in insect cells: role of extracellular domains and N-glycosylation in ligand binding.
10486146	1	24	theme	insect	254:259	arg1	cells					261:265	Sf9 insect cells	250:265	Sf9 insect cells	250:265	The cDNA of the human CXCR4/fusin was isolated from a human HeLa cell cDNA library by PCR and functionally expressed in Sf9 insect cells.
10486146	6	25	theme	N-glycosylation	721:735	arg1	role					713:716	The role	709:716	The role of N-glycosylation of CXCR4 in ligand binding	709:762	The role of N-glycosylation of CXCR4 in ligand binding was investigated in the insect cells overexpressed with recombinant CXCR4.
10486146	0	26	gly	N-glycosylation	95:109	arg1	ligand					114:119	ligand binding	114:127	ligand binding	114:127	Characterization of recombinant human CXCR4 in insect cells: role of extracellular domains and N-glycosylation in ligand binding.
10486146	9	27	theme	double	1062:1067	arg1	receptor					1076:1083	The double mutant receptor	1058:1083	The double mutant receptor	1058:1083	The double mutant receptor showed little binding activity.
10486146	2	28	theme	native	384:389	arg1	receptor					391:398	the native receptor	380:398	the native receptor	380:398	The recombinant receptor was found to bind its natural ligand SDF-1alpha with an affinity comparable to that of the native receptor.
10486146	0	29	theme	recombinant	20:30	arg1	CXCR4					38:42	recombinant human CXCR4	20:42	recombinant human CXCR4	20:42	Characterization of recombinant human CXCR4 in insect cells: role of extracellular domains and N-glycosylation in ligand binding.
10486146	6	30	gly	N-glycosylation	721:735	arg1	CXCR4					740:744	CXCR4	740:744	CXCR4	740:744	The role of N-glycosylation of CXCR4 in ligand binding was investigated in the insect cells overexpressed with recombinant CXCR4.
10486146	6	30	gly	N-glycosylation	721:735	arg1	ligand					749:754	ligand binding	749:762	ligand binding	749:762	The role of N-glycosylation of CXCR4 in ligand binding was investigated in the insect cells overexpressed with recombinant CXCR4.
10486146	0	31	theme	ligand	114:119	arg1	binding					121:127	ligand binding	114:127	ligand binding	114:127	Characterization of recombinant human CXCR4 in insect cells: role of extracellular domains and N-glycosylation in ligand binding.
10486146	7	32	gly	N-glycosylation	853:867	arg2	Asn-176					887:893	Asn-176	887:893	Asn-176	887:893	Two potential N-glycosylation sites (Asn-11 and Asn-176) were either singly or doubly mutated to a leucine residue.
10486146	7	32	gly	N-glycosylation	853:867	arg2	Asn-11					876:881	Asn-11	876:881	Asn-11	876:881	Two potential N-glycosylation sites (Asn-11 and Asn-176) were either singly or doubly mutated to a leucine residue.
10486146	7	32	gly	N-glycosylation	853:867	arg2	sites					869:873	Two potential N-glycosylation sites	839:873	Two potential N-glycosylation sites (Asn-11 and Asn-176)	839:894	Two potential N-glycosylation sites (Asn-11 and Asn-176) were either singly or doubly mutated to a leucine residue.
10486146	7	32	gly	N-glycosylation	853:867	arg2	Two					839:841	Two	839:841	Two	839:841	Two potential N-glycosylation sites (Asn-11 and Asn-176) were either singly or doubly mutated to a leucine residue.
10486146	2	33	theme	natural	315:321	arg1	ligand					323:328	its natural ligand	311:328	its natural ligand SDF-1alpha with an affinity comparable to that of the native receptor	311:398	The recombinant receptor was found to bind its natural ligand SDF-1alpha with an affinity comparable to that of the native receptor.
10486146	9	34	theme	mutant	1069:1074	arg1	receptor					1076:1083	The double mutant receptor	1058:1083	The double mutant receptor	1058:1083	The double mutant receptor showed little binding activity.
10486146	1	35	theme	human	184:188	arg1	library					205:211	a human HeLa cell cDNA library	182:211	a human HeLa cell cDNA library	182:211	The cDNA of the human CXCR4/fusin was isolated from a human HeLa cell cDNA library by PCR and functionally expressed in Sf9 insect cells.
10486146	6	36	theme	recombinant	820:830	arg1	CXCR4					832:836	recombinant CXCR4	820:836	recombinant CXCR4	820:836	The role of N-glycosylation of CXCR4 in ligand binding was investigated in the insect cells overexpressed with recombinant CXCR4.
10486146	1	37	theme	HeLa	190:193	arg1	library					205:211	a human HeLa cell cDNA library	182:211	a human HeLa cell cDNA library	182:211	The cDNA of the human CXCR4/fusin was isolated from a human HeLa cell cDNA library by PCR and functionally expressed in Sf9 insect cells.
10486146	0	38	theme	CXCR4	38:42	arg1	Characterization					0:15	Characterization	0:15	Characterization of recombinant human CXCR4 in insect cells: role of extracellular domains and N-glycosylation in ligand binding.	0:128	Characterization of recombinant human CXCR4 in insect cells: role of extracellular domains and N-glycosylation in ligand binding.
10486146	0	39	from	role	61:64	arg1	binding					121:127	ligand binding	114:127	ligand binding	114:127	Characterization of recombinant human CXCR4 in insect cells: role of extracellular domains and N-glycosylation in ligand binding.
10486146	8	40	theme	single	960:965	arg1	receptors					974:982	Both single mutant receptors	955:982	Both single mutant receptors	955:982	Both single mutant receptors exhibited a significant decrease in ligand binding activity and affinity.
10486146	5	41	gly	glycoprotein	695:706	arg1	CXCR4					671:675	CXCR4	671:675	CXCR4	671:675	CXCR4 was shown to be a glycoprotein.
10486146	5	41	gly	glycoprotein	695:706	arg1	glycoprotein					695:706	a glycoprotein	693:706	a glycoprotein	693:706	CXCR4 was shown to be a glycoprotein.
10486146	1	42	theme	cell	195:198	arg1	library					205:211	a human HeLa cell cDNA library	182:211	a human HeLa cell cDNA library	182:211	The cDNA of the human CXCR4/fusin was isolated from a human HeLa cell cDNA library by PCR and functionally expressed in Sf9 insect cells.
10486146	1	43	attach	isolated	168:175	arg2	cDNA					134:137	The cDNA	130:137	The cDNA of the human CXCR4/fusin	130:162	The cDNA of the human CXCR4/fusin was isolated from a human HeLa cell cDNA library by PCR and functionally expressed in Sf9 insect cells.
10486146	1	43	attach	isolated	168:175	arg1	library					205:211	a human HeLa cell cDNA library	182:211	a human HeLa cell cDNA library	182:211	The cDNA of the human CXCR4/fusin was isolated from a human HeLa cell cDNA library by PCR and functionally expressed in Sf9 insect cells.
10486146	9	44	theme	little	1092:1097	arg1	activity					1107:1114	little binding activity	1092:1114	little binding activity	1092:1114	The double mutant receptor showed little binding activity.
10486146	0	45	theme	insect	47:52	arg1	cells					54:58	insect cells	47:58	insect cells	47:58	Characterization of recombinant human CXCR4 in insect cells: role of extracellular domains and N-glycosylation in ligand binding.
10486146	3	46	theme	receptor	570:577	arg1	domains					555:561	the different domains	541:561	the different domains of the receptor and the ligand	541:592	Sequence-specific antibodies against each of the four extracellular domains were generated and used to investigate the interactions between the different domains of the receptor and the ligand.
10486146	3	46	theme	receptor	570:577	arg1	receptor					570:577	the receptor	566:577	the receptor	566:577	Sequence-specific antibodies against each of the four extracellular domains were generated and used to investigate the interactions between the different domains of the receptor and the ligand.
10486146	3	46	theme	receptor	570:577	arg1	ligand					587:592	the ligand	583:592	the ligand	583:592	Sequence-specific antibodies against each of the four extracellular domains were generated and used to investigate the interactions between the different domains of the receptor and the ligand.
10486146	9	47	theme	binding	1099:1105	arg1	activity					1107:1114	little binding activity	1092:1114	little binding activity	1092:1114	The double mutant receptor showed little binding activity.
10486146	3	48	theme	Sequence-specific	401:417	arg1	antibodies					419:428	Sequence-specific antibodies	401:428	Sequence-specific antibodies against each of the four extracellular domains	401:475	Sequence-specific antibodies against each of the four extracellular domains were generated and used to investigate the interactions between the different domains of the receptor and the ligand.
10486146	3	49	used	used	496:499	arg2	antibodies					419:428	Sequence-specific antibodies	401:428	Sequence-specific antibodies against each of the four extracellular domains	401:475	Sequence-specific antibodies against each of the four extracellular domains were generated and used to investigate the interactions between the different domains of the receptor and the ligand.
10486146	6	50	theme	insect	788:793	arg1	cells					795:799	the insect cells	784:799	the insect cells overexpressed with recombinant CXCR4	784:836	The role of N-glycosylation of CXCR4 in ligand binding was investigated in the insect cells overexpressed with recombinant CXCR4.
10486146	2	51	theme	recombinant	272:282	arg1	receptor					284:291	The recombinant receptor	268:291	The recombinant receptor	268:291	The recombinant receptor was found to bind its natural ligand SDF-1alpha with an affinity comparable to that of the native receptor.
10486146	1	52	theme	cDNA	200:203	arg1	library					205:211	a human HeLa cell cDNA library	182:211	a human HeLa cell cDNA library	182:211	The cDNA of the human CXCR4/fusin was isolated from a human HeLa cell cDNA library by PCR and functionally expressed in Sf9 insect cells.
10486146	7	53	theme	leucine	938:944	arg1	residue					946:952	a leucine residue	936:952	a leucine residue	936:952	Two potential N-glycosylation sites (Asn-11 and Asn-176) were either singly or doubly mutated to a leucine residue.
10486146	3	54	theme	extracellular	455:467	arg1	domains					469:475	the four extracellular domains	446:475	the four extracellular domains	446:475	Sequence-specific antibodies against each of the four extracellular domains were generated and used to investigate the interactions between the different domains of the receptor and the ligand.
10486146	10	55	theme	ligand-receptor	1188:1202	arg1	interactions					1204:1215	ligand-receptor interactions	1188:1215	ligand-receptor interactions	1188:1215	Our data suggest that all of the extracellular domains are involved in ligand-receptor interactions and that N-glycosylation is required to maintain high-affinity ligand binding.
10486146	2	56	with	SDF-1alpha	330:339	arg1	affinity					349:356	an affinity	346:356	an affinity comparable to that of the native receptor	346:398	The recombinant receptor was found to bind its natural ligand SDF-1alpha with an affinity comparable to that of the native receptor.
10486146	3	57	theme	ligand	587:592	arg1	domains					555:561	the different domains	541:561	the different domains of the receptor and the ligand	541:592	Sequence-specific antibodies against each of the four extracellular domains were generated and used to investigate the interactions between the different domains of the receptor and the ligand.
10486146	3	57	theme	ligand	587:592	arg1	receptor					570:577	the receptor	566:577	the receptor	566:577	Sequence-specific antibodies against each of the four extracellular domains were generated and used to investigate the interactions between the different domains of the receptor and the ligand.
10486146	3	57	theme	ligand	587:592	arg1	ligand					587:592	the ligand	583:592	the ligand	583:592	Sequence-specific antibodies against each of the four extracellular domains were generated and used to investigate the interactions between the different domains of the receptor and the ligand.
10486146	0	58	dep	Characterization	0:15	arg1	role					61:64	role	61:64	Characterization of recombinant human CXCR4 in insect cells: role of extracellular domains and N-glycosylation in ligand binding.	0:128	Characterization of recombinant human CXCR4 in insect cells: role of extracellular domains and N-glycosylation in ligand binding.
10486146	2	59	theme	SDF-1alpha	330:339	arg1	ligand					323:328	its natural ligand	311:328	its natural ligand SDF-1alpha with an affinity comparable to that of the native receptor	311:398	The recombinant receptor was found to bind its natural ligand SDF-1alpha with an affinity comparable to that of the native receptor.
10486146	7	60	theme	potential	843:851	arg1	Asn-176					887:893	Asn-176	887:893	Asn-176	887:893	Two potential N-glycosylation sites (Asn-11 and Asn-176) were either singly or doubly mutated to a leucine residue.
10486146	7	60	theme	potential	843:851	arg1	Asn-11					876:881	Asn-11	876:881	Asn-11	876:881	Two potential N-glycosylation sites (Asn-11 and Asn-176) were either singly or doubly mutated to a leucine residue.
10486146	7	60	theme	potential	843:851	arg1	sites					869:873	Two potential N-glycosylation sites	839:873	Two potential N-glycosylation sites (Asn-11 and Asn-176)	839:894	Two potential N-glycosylation sites (Asn-11 and Asn-176) were either singly or doubly mutated to a leucine residue.
9587408	6	0	theme	[3H	896:898	arg1	SQ29548					900:906	TXA2R antagonist [3H]SQ29548	879:906	TXA2R antagonist [3H]SQ29548	879:906	However, the mutant receptors possess lower binding affinity toward TXA2R antagonist [3H]SQ29548.
9587408	1	1	theme	insect	129:134	arg1	cells					141:145	insect Sf21 cells	129:145	insect Sf21 cells	129:145	Thromboxane A2 receptor (TXA2R) was expressed in insect Sf21 cells and demonstrated to interact with 8-iso-PGF2 alpha and 9 alpha, 11 beta-PGF2 alpha with a potency similar to that of TXA2 agonist U46619.
9587408	4	2	theme	Sf21	532:535	arg1	cells					537:541	Sf21 cells	532:541	Sf21 cells	532:541	Deletion of the carbohydrate moiety by adding tunicamycin during infection of Sf21 cells or mutation of both potential N-glycosylation sites (Asn-4 and Asn-16) abolished the ligand binding of TXA2R, suggesting that N-glycosylation is crucial for binding function.
9587408	0	3	theme	ligand	64:69	arg1	binding					71:77	ligand binding	64:77	ligand binding	64:77	The role of N-glycosylation of human thromboxane A2 receptor in ligand binding.
9587408	0	4	from	role	4:7	arg1	binding					71:77	ligand binding	64:77	ligand binding	64:77	The role of N-glycosylation of human thromboxane A2 receptor in ligand binding.
9587408	1	5	theme	Sf21	136:139	arg1	cells					141:145	insect Sf21 cells	129:145	insect Sf21 cells	129:145	Thromboxane A2 receptor (TXA2R) was expressed in insect Sf21 cells and demonstrated to interact with 8-iso-PGF2 alpha and 9 alpha, 11 beta-PGF2 alpha with a potency similar to that of TXA2 agonist U46619.
9587408	1	6	theme	beta-PGF2	214:222	arg1	alpha					224:228	9 alpha, 11 beta-PGF2 alpha	202:228	alpha	224:228	Thromboxane A2 receptor (TXA2R) was expressed in insect Sf21 cells and demonstrated to interact with 8-iso-PGF2 alpha and 9 alpha, 11 beta-PGF2 alpha with a potency similar to that of TXA2 agonist U46619.
9587408	6	7	theme	mutant	824:829	arg1	receptors					831:839	the mutant receptors	820:839	the mutant receptors	820:839	However, the mutant receptors possess lower binding affinity toward TXA2R antagonist [3H]SQ29548.
9587408	3	8	gly	N-glycosylation	335:349	arg1	ligand					363:368	ligand binding	363:376	ligand binding	363:376	The role of N-glycosylation of TXA2R in ligand binding was investigated in the insect cells over-expressed with recombinant TXA2R.
9587408	3	8	gly	N-glycosylation	335:349	arg1	TXA2R					354:358	TXA2R	354:358	TXA2R	354:358	The role of N-glycosylation of TXA2R in ligand binding was investigated in the insect cells over-expressed with recombinant TXA2R.
9587408	5	9	theme	Asn-4	737:741	arg1	Mutation					718:725	Mutation	718:725	Mutation of either Asn-4 or Asn-16 to a leucine	718:764	Mutation of either Asn-4 or Asn-16 to a leucine did not have much effect on maximal binding.
9587408	4	10	theme	binding	700:706	arg1	function					708:715	binding function	700:715	binding function	700:715	Deletion of the carbohydrate moiety by adding tunicamycin during infection of Sf21 cells or mutation of both potential N-glycosylation sites (Asn-4 and Asn-16) abolished the ligand binding of TXA2R, suggesting that N-glycosylation is crucial for binding function.
9587408	4	11	theme	cells	537:541	arg1	infection					519:527	infection	519:527	infection of Sf21 cells	519:541	Deletion of the carbohydrate moiety by adding tunicamycin during infection of Sf21 cells or mutation of both potential N-glycosylation sites (Asn-4 and Asn-16) abolished the ligand binding of TXA2R, suggesting that N-glycosylation is crucial for binding function.
9587408	4	12	gly	N-glycosylation	573:587	arg2	Asn-16					606:611	Asn-16	606:611	Asn-16	606:611	Deletion of the carbohydrate moiety by adding tunicamycin during infection of Sf21 cells or mutation of both potential N-glycosylation sites (Asn-4 and Asn-16) abolished the ligand binding of TXA2R, suggesting that N-glycosylation is crucial for binding function.
9587408	4	12	gly	N-glycosylation	573:587	arg2	Asn-4					596:600	Asn-4	596:600	Asn-4	596:600	Deletion of the carbohydrate moiety by adding tunicamycin during infection of Sf21 cells or mutation of both potential N-glycosylation sites (Asn-4 and Asn-16) abolished the ligand binding of TXA2R, suggesting that N-glycosylation is crucial for binding function.
9587408	4	12	gly	N-glycosylation	573:587	arg2	sites					589:593	both potential N-glycosylation sites	558:593	both potential N-glycosylation sites (Asn-4 and Asn-16)	558:612	Deletion of the carbohydrate moiety by adding tunicamycin during infection of Sf21 cells or mutation of both potential N-glycosylation sites (Asn-4 and Asn-16) abolished the ligand binding of TXA2R, suggesting that N-glycosylation is crucial for binding function.
9587408	4	13	theme	N-glycosylation	573:587	arg1	Asn-16					606:611	Asn-16	606:611	Asn-16	606:611	Deletion of the carbohydrate moiety by adding tunicamycin during infection of Sf21 cells or mutation of both potential N-glycosylation sites (Asn-4 and Asn-16) abolished the ligand binding of TXA2R, suggesting that N-glycosylation is crucial for binding function.
9587408	4	13	theme	N-glycosylation	573:587	arg1	Asn-4					596:600	Asn-4	596:600	Asn-4	596:600	Deletion of the carbohydrate moiety by adding tunicamycin during infection of Sf21 cells or mutation of both potential N-glycosylation sites (Asn-4 and Asn-16) abolished the ligand binding of TXA2R, suggesting that N-glycosylation is crucial for binding function.
9587408	4	13	theme	N-glycosylation	573:587	arg1	sites					589:593	both potential N-glycosylation sites	558:593	both potential N-glycosylation sites (Asn-4 and Asn-16)	558:612	Deletion of the carbohydrate moiety by adding tunicamycin during infection of Sf21 cells or mutation of both potential N-glycosylation sites (Asn-4 and Asn-16) abolished the ligand binding of TXA2R, suggesting that N-glycosylation is crucial for binding function.
9587408	6	14	contain	possess	841:847	arg1	receptors					831:839	the mutant receptors	820:839	the mutant receptors	820:839	However, the mutant receptors possess lower binding affinity toward TXA2R antagonist [3H]SQ29548.
9587408	6	14	contain	possess	841:847	arg2	affinity					863:870	lower binding affinity	849:870	lower binding affinity toward TXA2R antagonist [3H]SQ29548	849:906	However, the mutant receptors possess lower binding affinity toward TXA2R antagonist [3H]SQ29548.
9587408	0	15	theme	thromboxane	37:47	arg1	receptor					52:59	human thromboxane A2 receptor	31:59	human thromboxane A2 receptor	31:59	The role of N-glycosylation of human thromboxane A2 receptor in ligand binding.
9587408	9	16	theme	binding	1188:1194	arg1	affinity					1196:1203	binding affinity	1188:1203	binding affinity	1188:1203	However, glycosylation on both sites is required to maintain binding affinity and specificity.
9587408	5	17	theme	Asn-16	746:751	arg1	Mutation					718:725	Mutation	718:725	Mutation of either Asn-4 or Asn-16 to a leucine	718:764	Mutation of either Asn-4 or Asn-16 to a leucine did not have much effect on maximal binding.
9587408	3	18	from	role	327:330	arg1	binding					370:376	ligand binding	363:376	ligand binding	363:376	The role of N-glycosylation of TXA2R in ligand binding was investigated in the insect cells over-expressed with recombinant TXA2R.
9587408	2	19	gly	glycoprotein	309:320	arg1	TXA2R					285:289	TXA2R	285:289	TXA2R	285:289	TXA2R was shown to be a glycoprotein.
9587408	2	19	gly	glycoprotein	309:320	arg1	glycoprotein					309:320	a glycoprotein	307:320	a glycoprotein	307:320	TXA2R was shown to be a glycoprotein.
9587408	5	20	contain	have	774:777	arg2	effect					784:789	much effect	779:789	much effect	779:789	Mutation of either Asn-4 or Asn-16 to a leucine did not have much effect on maximal binding.
9587408	5	20	contain	have	774:777	arg1	Mutation					718:725	Mutation	718:725	Mutation of either Asn-4 or Asn-16 to a leucine	718:764	Mutation of either Asn-4 or Asn-16 to a leucine did not have much effect on maximal binding.
9587408	5	21	theme	maximal	794:800	arg1	binding					802:808	maximal binding	794:808	maximal binding	794:808	Mutation of either Asn-4 or Asn-16 to a leucine did not have much effect on maximal binding.
9587408	6	22	theme	binding	855:861	arg1	affinity					863:870	lower binding affinity	849:870	lower binding affinity toward TXA2R antagonist [3H]SQ29548	849:906	However, the mutant receptors possess lower binding affinity toward TXA2R antagonist [3H]SQ29548.
9587408	1	23	theme	Thromboxane	80:90	arg1	A2					92:93	Thromboxane A2	80:93	Thromboxane A2 receptor (TXA2R)	80:110	Thromboxane A2 receptor (TXA2R) was expressed in insect Sf21 cells and demonstrated to interact with 8-iso-PGF2 alpha and 9 alpha, 11 beta-PGF2 alpha with a potency similar to that of TXA2 agonist U46619.
9587408	3	24	theme	ligand	363:368	arg1	binding					370:376	ligand binding	363:376	ligand binding	363:376	The role of N-glycosylation of TXA2R in ligand binding was investigated in the insect cells over-expressed with recombinant TXA2R.
9587408	0	25	theme	N-glycosylation	12:26	arg1	role					4:7	The role	0:7	The role of N-glycosylation of human thromboxane A2 receptor in ligand binding.	0:78	The role of N-glycosylation of human thromboxane A2 receptor in ligand binding.
9587408	1	26	theme	A2	92:93	arg1	TXA2R					105:109	TXA2R	105:109	TXA2R	105:109	Thromboxane A2 receptor (TXA2R) was expressed in insect Sf21 cells and demonstrated to interact with 8-iso-PGF2 alpha and 9 alpha, 11 beta-PGF2 alpha with a potency similar to that of TXA2 agonist U46619.
9587408	1	26	theme	A2	92:93	arg1	receptor					95:102	Thromboxane A2 receptor	80:102	Thromboxane A2 receptor (TXA2R)	80:110	Thromboxane A2 receptor (TXA2R) was expressed in insect Sf21 cells and demonstrated to interact with 8-iso-PGF2 alpha and 9 alpha, 11 beta-PGF2 alpha with a potency similar to that of TXA2 agonist U46619.
9587408	4	27	theme	sites	589:593	arg1	Deletion					454:461	Deletion	454:461	Deletion of the carbohydrate moiety by adding tunicamycin during infection of Sf21 cells	454:541	Deletion of the carbohydrate moiety by adding tunicamycin during infection of Sf21 cells or mutation of both potential N-glycosylation sites (Asn-4 and Asn-16) abolished the ligand binding of TXA2R, suggesting that N-glycosylation is crucial for binding function.
9587408	4	27	theme	sites	589:593	arg1	mutation					546:553	mutation	546:553	mutation of both potential N-glycosylation sites (Asn-4 and Asn-16)	546:612	Deletion of the carbohydrate moiety by adding tunicamycin during infection of Sf21 cells or mutation of both potential N-glycosylation sites (Asn-4 and Asn-16) abolished the ligand binding of TXA2R, suggesting that N-glycosylation is crucial for binding function.
9587408	8	28	theme	ligand	1107:1112	arg1	recognition					1114:1124	ligand recognition	1107:1124	ligand recognition	1107:1124	Our data suggest that both Asn-4 and Asn-16 are glycosylated and glycosylation on either site is sufficient for ligand recognition.
9587408	1	29	theme	similar	245:251	arg1	potency					237:243	a potency	235:243	a potency similar to that of TXA2 agonist U46619	235:282	Thromboxane A2 receptor (TXA2R) was expressed in insect Sf21 cells and demonstrated to interact with 8-iso-PGF2 alpha and 9 alpha, 11 beta-PGF2 alpha with a potency similar to that of TXA2 agonist U46619.
9587408	8	30	from	glycosylation	1060:1072	arg1	site					1084:1087	either site	1077:1087	either site	1077:1087	Our data suggest that both Asn-4 and Asn-16 are glycosylated and glycosylation on either site is sufficient for ligand recognition.
9587408	3	31	theme	insect	402:407	arg1	cells					409:413	the insect cells	398:413	the insect cells over-expressed with recombinant TXA2R	398:451	The role of N-glycosylation of TXA2R in ligand binding was investigated in the insect cells over-expressed with recombinant TXA2R.
9587408	0	32	theme	human	31:35	arg1	receptor					52:59	human thromboxane A2 receptor	31:59	human thromboxane A2 receptor	31:59	The role of N-glycosylation of human thromboxane A2 receptor in ligand binding.
9587408	4	33	theme	TXA2R	646:650	arg1	binding					635:641	the ligand binding	624:641	the ligand binding of TXA2R	624:650	Deletion of the carbohydrate moiety by adding tunicamycin during infection of Sf21 cells or mutation of both potential N-glycosylation sites (Asn-4 and Asn-16) abolished the ligand binding of TXA2R, suggesting that N-glycosylation is crucial for binding function.
9587408	6	34	theme	antagonist	885:894	arg1	SQ29548					900:906	TXA2R antagonist [3H]SQ29548	879:906	TXA2R antagonist [3H]SQ29548	879:906	However, the mutant receptors possess lower binding affinity toward TXA2R antagonist [3H]SQ29548.
9587408	1	35	theme	8-iso-PGF2	181:190	arg1	alpha					192:196	8-iso-PGF2 alpha	181:196	8-iso-PGF2 alpha	181:196	Thromboxane A2 receptor (TXA2R) was expressed in insect Sf21 cells and demonstrated to interact with 8-iso-PGF2 alpha and 9 alpha, 11 beta-PGF2 alpha with a potency similar to that of TXA2 agonist U46619.
9587408	3	36	theme	TXA2R	354:358	arg1	N-glycosylation					335:349	N-glycosylation	335:349	N-glycosylation of TXA2R	335:358	The role of N-glycosylation of TXA2R in ligand binding was investigated in the insect cells over-expressed with recombinant TXA2R.
9587408	4	37	theme	carbohydrate	470:481	arg1	moiety					483:488	the carbohydrate moiety	466:488	the carbohydrate moiety by adding tunicamycin during infection of Sf21 cells	466:541	Deletion of the carbohydrate moiety by adding tunicamycin during infection of Sf21 cells or mutation of both potential N-glycosylation sites (Asn-4 and Asn-16) abolished the ligand binding of TXA2R, suggesting that N-glycosylation is crucial for binding function.
9587408	4	38	theme	potential	563:571	arg1	Asn-16					606:611	Asn-16	606:611	Asn-16	606:611	Deletion of the carbohydrate moiety by adding tunicamycin during infection of Sf21 cells or mutation of both potential N-glycosylation sites (Asn-4 and Asn-16) abolished the ligand binding of TXA2R, suggesting that N-glycosylation is crucial for binding function.
9587408	4	38	theme	potential	563:571	arg1	Asn-4					596:600	Asn-4	596:600	Asn-4	596:600	Deletion of the carbohydrate moiety by adding tunicamycin during infection of Sf21 cells or mutation of both potential N-glycosylation sites (Asn-4 and Asn-16) abolished the ligand binding of TXA2R, suggesting that N-glycosylation is crucial for binding function.
9587408	4	38	theme	potential	563:571	arg1	sites					589:593	both potential N-glycosylation sites	558:593	both potential N-glycosylation sites (Asn-4 and Asn-16)	558:612	Deletion of the carbohydrate moiety by adding tunicamycin during infection of Sf21 cells or mutation of both potential N-glycosylation sites (Asn-4 and Asn-16) abolished the ligand binding of TXA2R, suggesting that N-glycosylation is crucial for binding function.
9587408	4	39	theme	moiety	483:488	arg1	Deletion					454:461	Deletion	454:461	Deletion of the carbohydrate moiety by adding tunicamycin during infection of Sf21 cells	454:541	Deletion of the carbohydrate moiety by adding tunicamycin during infection of Sf21 cells or mutation of both potential N-glycosylation sites (Asn-4 and Asn-16) abolished the ligand binding of TXA2R, suggesting that N-glycosylation is crucial for binding function.
9587408	4	39	theme	moiety	483:488	arg1	mutation					546:553	mutation	546:553	mutation of both potential N-glycosylation sites (Asn-4 and Asn-16)	546:612	Deletion of the carbohydrate moiety by adding tunicamycin during infection of Sf21 cells or mutation of both potential N-glycosylation sites (Asn-4 and Asn-16) abolished the ligand binding of TXA2R, suggesting that N-glycosylation is crucial for binding function.
9587408	0	40	theme	A2	49:50	arg1	receptor					52:59	human thromboxane A2 receptor	31:59	human thromboxane A2 receptor	31:59	The role of N-glycosylation of human thromboxane A2 receptor in ligand binding.
9587408	6	41	theme	TXA2R	879:883	arg1	SQ29548					900:906	TXA2R antagonist [3H]SQ29548	879:906	TXA2R antagonist [3H]SQ29548	879:906	However, the mutant receptors possess lower binding affinity toward TXA2R antagonist [3H]SQ29548.
9587408	4	42	dep	sites	589:593	arg1	Asn-16					606:611	Asn-16	606:611	Asn-16	606:611	Deletion of the carbohydrate moiety by adding tunicamycin during infection of Sf21 cells or mutation of both potential N-glycosylation sites (Asn-4 and Asn-16) abolished the ligand binding of TXA2R, suggesting that N-glycosylation is crucial for binding function.
9587408	4	42	dep	sites	589:593	arg1	Asn-4					596:600	Asn-4	596:600	Asn-4	596:600	Deletion of the carbohydrate moiety by adding tunicamycin during infection of Sf21 cells or mutation of both potential N-glycosylation sites (Asn-4 and Asn-16) abolished the ligand binding of TXA2R, suggesting that N-glycosylation is crucial for binding function.
9587408	4	42	dep	sites	589:593	arg1	sites					589:593	both potential N-glycosylation sites	558:593	both potential N-glycosylation sites (Asn-4 and Asn-16)	558:612	Deletion of the carbohydrate moiety by adding tunicamycin during infection of Sf21 cells or mutation of both potential N-glycosylation sites (Asn-4 and Asn-16) abolished the ligand binding of TXA2R, suggesting that N-glycosylation is crucial for binding function.
9587408	8	43	gly	glycosylated	1043:1054	arg1	Asn-4					1022:1026	Asn-4	1022:1026	Asn-4	1022:1026	Our data suggest that both Asn-4 and Asn-16 are glycosylated and glycosylation on either site is sufficient for ligand recognition.
9587408	8	43	gly	glycosylated	1043:1054	arg1	Asn-16					1032:1037	Asn-16	1032:1037	Asn-16	1032:1037	Our data suggest that both Asn-4 and Asn-16 are glycosylated and glycosylation on either site is sufficient for ligand recognition.
9587408	3	44	theme	N-glycosylation	335:349	arg1	role					327:330	The role	323:330	The role of N-glycosylation of TXA2R in ligand binding	323:376	The role of N-glycosylation of TXA2R in ligand binding was investigated in the insect cells over-expressed with recombinant TXA2R.
9587408	1	45	theme	TXA2	264:267	arg1	U46619					277:282	TXA2 agonist U46619	264:282	TXA2 agonist U46619	264:282	Thromboxane A2 receptor (TXA2R) was expressed in insect Sf21 cells and demonstrated to interact with 8-iso-PGF2 alpha and 9 alpha, 11 beta-PGF2 alpha with a potency similar to that of TXA2 agonist U46619.
9587408	0	46	gly	N-glycosylation	12:26	arg1	ligand					64:69	ligand binding	64:77	ligand binding	64:77	The role of N-glycosylation of human thromboxane A2 receptor in ligand binding.
9587408	0	46	gly	N-glycosylation	12:26	arg1	receptor					52:59	human thromboxane A2 receptor	31:59	human thromboxane A2 receptor	31:59	The role of N-glycosylation of human thromboxane A2 receptor in ligand binding.
9587408	7	47	theme	binding	926:932	arg1	specificity					934:944	the binding specificity	922:944	the binding specificity of the mutant receptors	922:968	Furthermore, the binding specificity of the mutant receptors was shown to be altered.
9587408	3	48	theme	recombinant	435:445	arg1	TXA2R					447:451	recombinant TXA2R	435:451	recombinant TXA2R	435:451	The role of N-glycosylation of TXA2R in ligand binding was investigated in the insect cells over-expressed with recombinant TXA2R.
9587408	1	49	theme	agonist	269:275	arg1	U46619					277:282	TXA2 agonist U46619	264:282	TXA2 agonist U46619	264:282	Thromboxane A2 receptor (TXA2R) was expressed in insect Sf21 cells and demonstrated to interact with 8-iso-PGF2 alpha and 9 alpha, 11 beta-PGF2 alpha with a potency similar to that of TXA2 agonist U46619.
9587408	7	50	theme	mutant	953:958	arg1	receptors					960:968	the mutant receptors	949:968	the mutant receptors	949:968	Furthermore, the binding specificity of the mutant receptors was shown to be altered.
9587408	8	51	gly	glycosylation	1060:1072	arg1	site					1084:1087	either site	1077:1087	either site	1077:1087	Our data suggest that both Asn-4 and Asn-16 are glycosylated and glycosylation on either site is sufficient for ligand recognition.
9587408	7	52	theme	receptors	960:968	arg1	specificity					934:944	the binding specificity	922:944	the binding specificity of the mutant receptors	922:968	Furthermore, the binding specificity of the mutant receptors was shown to be altered.
9587408	5	53	theme	much	779:782	arg1	effect					784:789	much effect	779:789	much effect	779:789	Mutation of either Asn-4 or Asn-16 to a leucine did not have much effect on maximal binding.
9587408	9	54	gly	glycosylation	1136:1148	arg1	sites					1158:1162	both sites	1153:1162	both sites	1153:1162	However, glycosylation on both sites is required to maintain binding affinity and specificity.
9587408	4	55	theme	ligand	628:633	arg1	binding					635:641	the ligand binding	624:641	the ligand binding of TXA2R	624:650	Deletion of the carbohydrate moiety by adding tunicamycin during infection of Sf21 cells or mutation of both potential N-glycosylation sites (Asn-4 and Asn-16) abolished the ligand binding of TXA2R, suggesting that N-glycosylation is crucial for binding function.
9587408	1	56	theme	alpha	204:208	arg1	alpha					224:228	9 alpha, 11 beta-PGF2 alpha	202:228	alpha	224:228	Thromboxane A2 receptor (TXA2R) was expressed in insect Sf21 cells and demonstrated to interact with 8-iso-PGF2 alpha and 9 alpha, 11 beta-PGF2 alpha with a potency similar to that of TXA2 agonist U46619.
9587408	0	57	theme	receptor	52:59	arg1	N-glycosylation					12:26	N-glycosylation	12:26	N-glycosylation of human thromboxane A2 receptor	12:59	The role of N-glycosylation of human thromboxane A2 receptor in ligand binding.
9587408	6	58	theme	lower	849:853	arg1	affinity					863:870	lower binding affinity	849:870	lower binding affinity toward TXA2R antagonist [3H]SQ29548	849:906	However, the mutant receptors possess lower binding affinity toward TXA2R antagonist [3H]SQ29548.
9587408	9	59	from	glycosylation	1136:1148	arg1	sites					1158:1162	both sites	1153:1162	both sites	1153:1162	However, glycosylation on both sites is required to maintain binding affinity and specificity.
28327359	4	0	theme	lines	498:502	arg1	mutant					464:469	a C-mannosylation-defective mutant	436:469	a C-mannosylation-defective mutant of LPL-overexpressing cell lines	436:502	Furthermore, by using wild-type and a C-mannosylation-defective mutant of LPL-overexpressing cell lines, we revealed that both secretion efficiency and enzymatic activity of C-mannosylation-defective mutant LPL were lower than those of wild-type.
28327359	4	0	theme	lines	498:502	arg1	wild-type					422:430	wild-type	422:430	wild-type	422:430	Furthermore, by using wild-type and a C-mannosylation-defective mutant of LPL-overexpressing cell lines, we revealed that both secretion efficiency and enzymatic activity of C-mannosylation-defective mutant LPL were lower than those of wild-type.
28327359	4	1	theme	LPL-overexpressing	474:491	arg1	lines					498:502	LPL-overexpressing cell lines	474:502	LPL-overexpressing cell lines	474:502	Furthermore, by using wild-type and a C-mannosylation-defective mutant of LPL-overexpressing cell lines, we revealed that both secretion efficiency and enzymatic activity of C-mannosylation-defective mutant LPL were lower than those of wild-type.
28327359	1	2	theme	lipid	137:141	arg1	metabolism					143:152	lipid metabolism	137:152	lipid metabolism	137:152	Lipoprotein lipase (LPL) is a crucial enzyme in lipid metabolism and transport, and its enzymatic deficiency causes metabolic disorders, such as hypertriglyceridemia.
28327359	4	3	theme	mutant	600:605	arg1	LPL					607:609	C-mannosylation-defective mutant LPL	574:609	C-mannosylation-defective mutant LPL	574:609	Furthermore, by using wild-type and a C-mannosylation-defective mutant of LPL-overexpressing cell lines, we revealed that both secretion efficiency and enzymatic activity of C-mannosylation-defective mutant LPL were lower than those of wild-type.
28327359	4	4	theme	C-mannosylation-defective	574:598	arg1	LPL					607:609	C-mannosylation-defective mutant LPL	574:609	C-mannosylation-defective mutant LPL	574:609	Furthermore, by using wild-type and a C-mannosylation-defective mutant of LPL-overexpressing cell lines, we revealed that both secretion efficiency and enzymatic activity of C-mannosylation-defective mutant LPL were lower than those of wild-type.
28327359	2	5	theme	C-mannosylation	278:292	arg1	site					294:297	one predicted C-mannosylation site	264:297	one predicted C-mannosylation site	264:297	LPL has one predicted C-mannosylation site at Trp417.
28327359	2	6	gly	C-mannosylation	278:292	arg2	site					294:297	one predicted C-mannosylation site	264:297	one predicted C-mannosylation site	264:297	LPL has one predicted C-mannosylation site at Trp417.
28327359	1	7	from	enzyme	127:132	arg1	transport					158:166	transport	158:166	transport	158:166	Lipoprotein lipase (LPL) is a crucial enzyme in lipid metabolism and transport, and its enzymatic deficiency causes metabolic disorders, such as hypertriglyceridemia.
28327359	1	7	from	enzyme	127:132	arg1	metabolism					143:152	lipid metabolism	137:152	lipid metabolism	137:152	Lipoprotein lipase (LPL) is a crucial enzyme in lipid metabolism and transport, and its enzymatic deficiency causes metabolic disorders, such as hypertriglyceridemia.
28327359	2	8	theme	predicted	268:276	arg1	site					294:297	one predicted C-mannosylation site	264:297	one predicted C-mannosylation site	264:297	LPL has one predicted C-mannosylation site at Trp417.
28327359	4	9	theme	LPL	607:609	arg1	efficiency					537:546	secretion efficiency	527:546	secretion efficiency	527:546	Furthermore, by using wild-type and a C-mannosylation-defective mutant of LPL-overexpressing cell lines, we revealed that both secretion efficiency and enzymatic activity of C-mannosylation-defective mutant LPL were lower than those of wild-type.
28327359	4	9	theme	LPL	607:609	arg1	activity					562:569	enzymatic activity	552:569	enzymatic activity of C-mannosylation-defective mutant LPL	552:609	Furthermore, by using wild-type and a C-mannosylation-defective mutant of LPL-overexpressing cell lines, we revealed that both secretion efficiency and enzymatic activity of C-mannosylation-defective mutant LPL were lower than those of wild-type.
28327359	4	10	theme	cell	493:496	arg1	lines					498:502	LPL-overexpressing cell lines	474:502	LPL-overexpressing cell lines	474:502	Furthermore, by using wild-type and a C-mannosylation-defective mutant of LPL-overexpressing cell lines, we revealed that both secretion efficiency and enzymatic activity of C-mannosylation-defective mutant LPL were lower than those of wild-type.
28327359	3	11	from	Trp417	371:376	arg1	C-mannosylated					353:366	C-mannosylated	353:366	C-mannosylated	353:366	In this study, we demonstrated that LPL is C-mannosylated at Trp417 by mass spectrometry.
28327359	3	12	gly	C-mannosylated	353:366	arg2	Trp417					371:376	Trp417	371:376	Trp417	371:376	In this study, we demonstrated that LPL is C-mannosylated at Trp417 by mass spectrometry.
28327359	3	12	gly	C-mannosylated	353:366	arg1	LPL					346:348	LPL	346:348	LPL	346:348	In this study, we demonstrated that LPL is C-mannosylated at Trp417 by mass spectrometry.
28327359	4	13	theme	enzymatic	552:560	arg1	activity					562:569	enzymatic activity	552:569	enzymatic activity of C-mannosylation-defective mutant LPL	552:609	Furthermore, by using wild-type and a C-mannosylation-defective mutant of LPL-overexpressing cell lines, we revealed that both secretion efficiency and enzymatic activity of C-mannosylation-defective mutant LPL were lower than those of wild-type.
28327359	1	14	theme	Lipoprotein	89:99	arg1	lipase					101:106	Lipoprotein lipase	89:106	Lipoprotein lipase (LPL)	89:112	Lipoprotein lipase (LPL) is a crucial enzyme in lipid metabolism and transport, and its enzymatic deficiency causes metabolic disorders, such as hypertriglyceridemia.
28327359	1	14	theme	Lipoprotein	89:99	arg1	enzyme					127:132	a crucial enzyme	117:132	a crucial enzyme in lipid metabolism and transport	117:166	Lipoprotein lipase (LPL) is a crucial enzyme in lipid metabolism and transport, and its enzymatic deficiency causes metabolic disorders, such as hypertriglyceridemia.
28327359	1	14	theme	Lipoprotein	89:99	arg1	LPL					109:111	LPL	109:111	LPL	109:111	Lipoprotein lipase (LPL) is a crucial enzyme in lipid metabolism and transport, and its enzymatic deficiency causes metabolic disorders, such as hypertriglyceridemia.
28327359	2	15	contain	has	260:262	arg2	site					294:297	one predicted C-mannosylation site	264:297	one predicted C-mannosylation site	264:297	LPL has one predicted C-mannosylation site at Trp417.
28327359	2	15	contain	has	260:262	arg1	LPL					256:258	LPL	256:258	LPL	256:258	LPL has one predicted C-mannosylation site at Trp417.
28327359	0	16	theme	secretion	14:22	arg1	Regulation					0:9	Regulation	0:9	Regulation of secretion and enzymatic activity of lipoprotein lipase by C-mannosylation.	0:87	Regulation of secretion and enzymatic activity of lipoprotein lipase by C-mannosylation.
28327359	1	17	theme	enzymatic	177:185	arg1	deficiency					187:196	its enzymatic deficiency	173:196	its enzymatic deficiency	173:196	Lipoprotein lipase (LPL) is a crucial enzyme in lipid metabolism and transport, and its enzymatic deficiency causes metabolic disorders, such as hypertriglyceridemia.
28327359	0	18	theme	activity	38:45	arg1	Regulation					0:9	Regulation	0:9	Regulation of secretion and enzymatic activity of lipoprotein lipase by C-mannosylation.	0:87	Regulation of secretion and enzymatic activity of lipoprotein lipase by C-mannosylation.
28327359	0	19	theme	enzymatic	28:36	arg1	activity					38:45	enzymatic activity	28:45	enzymatic activity	28:45	Regulation of secretion and enzymatic activity of lipoprotein lipase by C-mannosylation.
28327359	4	20	theme	C-mannosylation-defective	438:462	arg1	mutant					464:469	a C-mannosylation-defective mutant	436:469	a C-mannosylation-defective mutant of LPL-overexpressing cell lines	436:502	Furthermore, by using wild-type and a C-mannosylation-defective mutant of LPL-overexpressing cell lines, we revealed that both secretion efficiency and enzymatic activity of C-mannosylation-defective mutant LPL were lower than those of wild-type.
28327359	0	21	theme	lipoprotein	50:60	arg1	lipase					62:67	lipoprotein lipase	50:67	lipoprotein lipase	50:67	Regulation of secretion and enzymatic activity of lipoprotein lipase by C-mannosylation.
28327359	5	22	theme	C-mannosylation	684:698	arg1	importance					670:679	the importance	666:679	the importance of C-mannosylation for LPL functions	666:716	These data suggest the importance of C-mannosylation for LPL functions.
28327359	3	23	theme	mass	381:384	arg1	spectrometry					386:397	mass spectrometry	381:397	mass spectrometry	381:397	In this study, we demonstrated that LPL is C-mannosylated at Trp417 by mass spectrometry.
28327359	4	24	theme	secretion	527:535	arg1	efficiency					537:546	secretion efficiency	527:546	secretion efficiency	527:546	Furthermore, by using wild-type and a C-mannosylation-defective mutant of LPL-overexpressing cell lines, we revealed that both secretion efficiency and enzymatic activity of C-mannosylation-defective mutant LPL were lower than those of wild-type.
28327359	5	25	theme	LPL	704:706	arg1	functions					708:716	LPL functions	704:716	LPL functions	704:716	These data suggest the importance of C-mannosylation for LPL functions.
28327359	1	26	theme	metabolic	205:213	arg1	hypertriglyceridemia					234:253	hypertriglyceridemia	234:253	hypertriglyceridemia	234:253	Lipoprotein lipase (LPL) is a crucial enzyme in lipid metabolism and transport, and its enzymatic deficiency causes metabolic disorders, such as hypertriglyceridemia.
28327359	1	26	theme	metabolic	205:213	arg1	disorders					215:223	metabolic disorders	205:223	metabolic disorders	205:223	Lipoprotein lipase (LPL) is a crucial enzyme in lipid metabolism and transport, and its enzymatic deficiency causes metabolic disorders, such as hypertriglyceridemia.
28327359	1	27	theme	crucial	119:125	arg1	lipase					101:106	Lipoprotein lipase	89:106	Lipoprotein lipase (LPL)	89:112	Lipoprotein lipase (LPL) is a crucial enzyme in lipid metabolism and transport, and its enzymatic deficiency causes metabolic disorders, such as hypertriglyceridemia.
28327359	1	27	theme	crucial	119:125	arg1	enzyme					127:132	a crucial enzyme	117:132	a crucial enzyme in lipid metabolism and transport	117:166	Lipoprotein lipase (LPL) is a crucial enzyme in lipid metabolism and transport, and its enzymatic deficiency causes metabolic disorders, such as hypertriglyceridemia.
28327359	0	28	theme	lipase	62:67	arg1	secretion					14:22	secretion	14:22	secretion	14:22	Regulation of secretion and enzymatic activity of lipoprotein lipase by C-mannosylation.
28327359	0	28	theme	lipase	62:67	arg1	activity					38:45	enzymatic activity	28:45	enzymatic activity	28:45	Regulation of secretion and enzymatic activity of lipoprotein lipase by C-mannosylation.
2514791	4	0	dep	cells	1253:1257	arg1	cell					1276:1279	(iv) fibroblast cell	1260:1279	melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines	1244:1583	Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
2514791	5	1	theme	common	1786:1791	arg1	polypeptide					1793:1803	a common polypeptide	1784:1803	a common polypeptide	1784:1803	These results indicate that the t-PA glycoprotein is secreted by each cell line as a set of glycoforms, each glycoform being unique with respect to the nature and disposition of oligosaccharides on a common polypeptide.
2514791	4	2	theme	following	810:818	arg1	Asn-184					1046:1052	the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184	806:1052	the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184	806:1052	Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
2514791	3	3	theme	digestion	526:534	arg1	combination					485:495	a combination	483:495	a combination of sequential exoglycosidase digestion, methylation analysis, and controlled acetolysis	483:583	In an effort to elucidate the factors controlling the expression of N-linked oligosaccharides on this polypeptide, we have used a combination of sequential exoglycosidase digestion, methylation analysis, and controlled acetolysis to determine the oligosaccharide structures at each of the N-glycosylation sites of type I and type II t-PA when isolated from a human colon fibroblast cell strain and from a Bowes melanoma cell line.
2514791	4	4	theme	cell	940:943	arg1	line					945:948	the same cell line	931:948	the same cell line	931:948	Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
2514791	4	5	from	Asn-448	1476:1482	arg1	located					1453:1459	located	1453:1459	located	1453:1459	Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
2514791	7	6	theme	oligosaccharide	1970:1984	arg1	processing					1986:1995	oligosaccharide processing	1970:1995	oligosaccharide processing in different cell lines	1970:2019	The implications of these results for both the control of oligosaccharide processing in different cell lines and the genetic engineering of mammalian glycoproteins are discussed.
2514791	5	7	gly	glycoprotein	1623:1634	arg1	glycoprotein					1623:1634	the t-PA glycoprotein	1614:1634	the t-PA glycoprotein	1614:1634	These results indicate that the t-PA glycoprotein is secreted by each cell line as a set of glycoforms, each glycoform being unique with respect to the nature and disposition of oligosaccharides on a common polypeptide.
2514791	5	7	gly	glycoprotein	1623:1634	arg1	glycoforms					1678:1687	glycoforms	1678:1687	glycoforms	1678:1687	These results indicate that the t-PA glycoprotein is secreted by each cell line as a set of glycoforms, each glycoform being unique with respect to the nature and disposition of oligosaccharides on a common polypeptide.
2514791	5	7	gly	glycoprotein	1623:1634	arg1	set					1671:1673	a set	1669:1673	a set of glycoforms	1669:1687	These results indicate that the t-PA glycoprotein is secreted by each cell line as a set of glycoforms, each glycoform being unique with respect to the nature and disposition of oligosaccharides on a common polypeptide.
2514791	3	8	theme	type	669:672	arg1	sites					660:664	the N-glycosylation sites	640:664	the N-glycosylation sites of type I and type II t-PA	640:691	In an effort to elucidate the factors controlling the expression of N-linked oligosaccharides on this polypeptide, we have used a combination of sequential exoglycosidase digestion, methylation analysis, and controlled acetolysis to determine the oligosaccharide structures at each of the N-glycosylation sites of type I and type II t-PA when isolated from a human colon fibroblast cell strain and from a Bowes melanoma cell line.
2514791	3	8	theme	type	669:672	arg1	type					669:672	type I	669:674	type I	669:674	In an effort to elucidate the factors controlling the expression of N-linked oligosaccharides on this polypeptide, we have used a combination of sequential exoglycosidase digestion, methylation analysis, and controlled acetolysis to determine the oligosaccharide structures at each of the N-glycosylation sites of type I and type II t-PA when isolated from a human colon fibroblast cell strain and from a Bowes melanoma cell line.
2514791	3	8	theme	type	669:672	arg1	type					680:683	type II	680:686	type II	680:686	In an effort to elucidate the factors controlling the expression of N-linked oligosaccharides on this polypeptide, we have used a combination of sequential exoglycosidase digestion, methylation analysis, and controlled acetolysis to determine the oligosaccharide structures at each of the N-glycosylation sites of type I and type II t-PA when isolated from a human colon fibroblast cell strain and from a Bowes melanoma cell line.
2514791	3	9	from	expression	409:418	arg1	polypeptide					457:467	this polypeptide	452:467	this polypeptide	452:467	In an effort to elucidate the factors controlling the expression of N-linked oligosaccharides on this polypeptide, we have used a combination of sequential exoglycosidase digestion, methylation analysis, and controlled acetolysis to determine the oligosaccharide structures at each of the N-glycosylation sites of type I and type II t-PA when isolated from a human colon fibroblast cell strain and from a Bowes melanoma cell line.
2514791	5	10	theme	cell	1656:1659	arg1	line					1661:1664	each cell line	1651:1664	each cell line	1651:1664	These results indicate that the t-PA glycoprotein is secreted by each cell line as a set of glycoforms, each glycoform being unique with respect to the nature and disposition of oligosaccharides on a common polypeptide.
2514791	4	11	from	structures	1015:1024	arg1	cases					1033:1037	all cases	1029:1037	all cases	1029:1037	Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
2514791	3	12	theme	exoglycosidase	511:524	arg1	digestion					526:534	sequential exoglycosidase digestion	500:534	sequential exoglycosidase digestion	500:534	In an effort to elucidate the factors controlling the expression of N-linked oligosaccharides on this polypeptide, we have used a combination of sequential exoglycosidase digestion, methylation analysis, and controlled acetolysis to determine the oligosaccharide structures at each of the N-glycosylation sites of type I and type II t-PA when isolated from a human colon fibroblast cell strain and from a Bowes melanoma cell line.
2514791	4	13	dep	occur	1532:1536	arg1	v					1502:1502	v	1502:1502	v	1502:1502	Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
2514791	4	14	theme	fibroblast	1265:1274	arg1	cell					1276:1279	(iv) fibroblast cell	1260:1279	melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines	1244:1583	Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
2514791	4	15	theme	complex-type	1508:1519	arg1	structures					1521:1530	no complex-type structures	1505:1530	no complex-type structures	1505:1530	Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
2514791	4	16	theme	type	836:839	arg1	t-PA					844:847	type II t-PA	836:847	type II t-PA	836:847	Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
2514791	4	17	attach	isolated	1137:1144	arg2	t-PA					1129:1132	t-PA	1129:1132	t-PA	1129:1132	Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
2514791	4	17	attach	isolated	1137:1144	arg1	cells					1162:1166	fibroblast cells	1151:1166	fibroblast cells	1151:1166	Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
2514791	4	18	theme	melanoma	1244:1251	arg1	cells					1253:1257	melanoma cells	1244:1257	melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines	1244:1583	Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
2514791	2	19	theme	N-glycosylation	230:244	arg1	sites					246:250	four potential N-glycosylation sites	215:250	four potential N-glycosylation sites of which three are occupied in type I (Asn-117, -184, and -448) and two in type II (Asn-117 and -448)	215:352	The t-PA polypeptide has four potential N-glycosylation sites of which three are occupied in type I (Asn-117, -184, and -448) and two in type II (Asn-117 and -448).
2514791	2	20	contain	has	211:213	arg2	sites					246:250	four potential N-glycosylation sites	215:250	four potential N-glycosylation sites of which three are occupied in type I (Asn-117, -184, and -448) and two in type II (Asn-117 and -448)	215:352	The t-PA polypeptide has four potential N-glycosylation sites of which three are occupied in type I (Asn-117, -184, and -448) and two in type II (Asn-117 and -448).
2514791	2	20	contain	has	211:213	arg1	polypeptide					199:209	The t-PA polypeptide	190:209	The t-PA polypeptide	190:209	The t-PA polypeptide has four potential N-glycosylation sites of which three are occupied in type I (Asn-117, -184, and -448) and two in type II (Asn-117 and -448).
2514791	4	21	located	located	1453:1459	arg1	Asn-448					1476:1482	Asn-448	1476:1482	Asn-448 of type II t-PA	1476:1498	Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
2514791	4	21	located	located	1453:1459	arg2	oligosaccharides					1425:1440	sulfated oligosaccharides	1416:1440	sulfated oligosaccharides	1416:1440	Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
2514791	3	22	link	N-linked	423:430	arg1	oligosaccharides					432:447	N-linked oligosaccharides	423:447	N-linked oligosaccharides	423:447	In an effort to elucidate the factors controlling the expression of N-linked oligosaccharides on this polypeptide, we have used a combination of sequential exoglycosidase digestion, methylation analysis, and controlled acetolysis to determine the oligosaccharide structures at each of the N-glycosylation sites of type I and type II t-PA when isolated from a human colon fibroblast cell strain and from a Bowes melanoma cell line.
2514791	4	23	theme	t-PA	1495:1498	arg1	Asn-448					1476:1482	Asn-448	1476:1482	Asn-448 of type II t-PA	1476:1498	Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
2514791	3	24	theme	acetolysis	574:583	arg1	combination					485:495	a combination	483:495	a combination of sequential exoglycosidase digestion, methylation analysis, and controlled acetolysis	483:583	In an effort to elucidate the factors controlling the expression of N-linked oligosaccharides on this polypeptide, we have used a combination of sequential exoglycosidase digestion, methylation analysis, and controlled acetolysis to determine the oligosaccharide structures at each of the N-glycosylation sites of type I and type II t-PA when isolated from a human colon fibroblast cell strain and from a Bowes melanoma cell line.
2514791	7	25	from	control	1959:1965	arg1	lines					2015:2019	different cell lines	2000:2019	different cell lines	2000:2019	The implications of these results for both the control of oligosaccharide processing in different cell lines and the genetic engineering of mammalian glycoproteins are discussed.
2514791	3	26	theme	cell	775:778	arg1	line					780:783	a Bowes melanoma cell line	758:783	a Bowes melanoma cell line	758:783	In an effort to elucidate the factors controlling the expression of N-linked oligosaccharides on this polypeptide, we have used a combination of sequential exoglycosidase digestion, methylation analysis, and controlled acetolysis to determine the oligosaccharide structures at each of the N-glycosylation sites of type I and type II t-PA when isolated from a human colon fibroblast cell strain and from a Bowes melanoma cell line.
2514791	5	27	dep	nature	1738:1743	arg1	the					1734:1736	the	1734:1736	the	1734:1736	These results indicate that the t-PA glycoprotein is secreted by each cell line as a set of glycoforms, each glycoform being unique with respect to the nature and disposition of oligosaccharides on a common polypeptide.
2514791	4	28	theme	neutral	1318:1324	arg1	oligosaccharides					1341:1356	both neutral and sialylated oligosaccharides	1313:1356	both neutral and sialylated oligosaccharides	1313:1356	Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
2514791	0	29	theme	type	67:70	arg1	N-glycosylation					37:51	Cell-type-specific and site-specific N-glycosylation	0:51	Cell-type-specific and site-specific N-glycosylation of type I and type II human tissue plasminogen activator	0:108	Cell-type-specific and site-specific N-glycosylation of type I and type II human tissue plasminogen activator.
2514791	6	30	from	glycoform	1845:1853	arg1	common					1858:1863	common	1858:1863	common	1858:1863	Further, the two cell lines express no glycoform in common, despite expressing the same t-PA polypeptide.
2514791	2	31	dep	I	288:288	arg1	-448					310:313	-448	310:313	-448	310:313	The t-PA polypeptide has four potential N-glycosylation sites of which three are occupied in type I (Asn-117, -184, and -448) and two in type II (Asn-117 and -448).
2514791	2	31	dep	I	288:288	arg1	Asn-117					291:297	Asn-117	291:297	Asn-117	291:297	The t-PA polypeptide has four potential N-glycosylation sites of which three are occupied in type I (Asn-117, -184, and -448) and two in type II (Asn-117 and -448).
2514791	2	31	dep	I	288:288	arg1	-184					300:303	-184	300:303	-184	300:303	The t-PA polypeptide has four potential N-glycosylation sites of which three are occupied in type I (Asn-117, -184, and -448) and two in type II (Asn-117 and -448).
2514791	3	32	theme	Bowes	760:764	arg1	line					780:783	a Bowes melanoma cell line	758:783	a Bowes melanoma cell line	758:783	In an effort to elucidate the factors controlling the expression of N-linked oligosaccharides on this polypeptide, we have used a combination of sequential exoglycosidase digestion, methylation analysis, and controlled acetolysis to determine the oligosaccharide structures at each of the N-glycosylation sites of type I and type II t-PA when isolated from a human colon fibroblast cell strain and from a Bowes melanoma cell line.
2514791	0	33	theme	human	75:79	arg1	activator					100:108	human tissue plasminogen activator	75:108	human tissue plasminogen activator	75:108	Cell-type-specific and site-specific N-glycosylation of type I and type II human tissue plasminogen activator.
2514791	1	34	theme	important	153:161	arg1	initiator					163:171	an important initiator	150:171	an important initiator of fibrinolysis	150:187	Tissue plasminogen activator (t-PA) is an important initiator of fibrinolysis.
2514791	1	34	theme	important	153:161	arg1	activator					130:138	Tissue plasminogen activator	111:138	Tissue plasminogen activator (t-PA)	111:145	Tissue plasminogen activator (t-PA) is an important initiator of fibrinolysis.
2514791	2	35	dep	two	320:322	arg1	Asn-117					336:342	Asn-117	336:342	Asn-117	336:342	The t-PA polypeptide has four potential N-glycosylation sites of which three are occupied in type I (Asn-117, -184, and -448) and two in type II (Asn-117 and -448).
2514791	2	35	dep	two	320:322	arg1	-448					348:351	-448	348:351	-448	348:351	The t-PA polypeptide has four potential N-glycosylation sites of which three are occupied in type I (Asn-117, -184, and -448) and two in type II (Asn-117 and -448).
2514791	1	36	theme	Tissue	111:116	arg1	initiator					163:171	an important initiator	150:171	an important initiator of fibrinolysis	150:187	Tissue plasminogen activator (t-PA) is an important initiator of fibrinolysis.
2514791	1	36	theme	Tissue	111:116	arg1	t-PA					141:144	t-PA	141:144	t-PA	141:144	Tissue plasminogen activator (t-PA) is an important initiator of fibrinolysis.
2514791	1	36	theme	Tissue	111:116	arg1	activator					130:138	Tissue plasminogen activator	111:138	Tissue plasminogen activator (t-PA)	111:145	Tissue plasminogen activator (t-PA) is an important initiator of fibrinolysis.
2514791	0	37	theme	plasminogen	88:98	arg1	activator					100:108	human tissue plasminogen activator	75:108	human tissue plasminogen activator	75:108	Cell-type-specific and site-specific N-glycosylation of type I and type II human tissue plasminogen activator.
2514791	6	38	theme	cell	1823:1826	arg1	lines					1828:1832	the two cell lines	1815:1832	the two cell lines	1815:1832	Further, the two cell lines express no glycoform in common, despite expressing the same t-PA polypeptide.
2514791	4	39	theme	melanoma	1365:1372	arg1	cell					1374:1377	melanoma cell	1365:1377	melanoma cell	1365:1377	Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
2514791	7	40	theme	glycoproteins	2062:2074	arg1	control					1959:1965	the control	1955:1965	the control of oligosaccharide processing in different cell lines	1955:2019	The implications of these results for both the control of oligosaccharide processing in different cell lines and the genetic engineering of mammalian glycoproteins are discussed.
2514791	7	40	theme	glycoproteins	2062:2074	arg1	engineering					2037:2047	the genetic engineering	2025:2047	the genetic engineering of mammalian glycoproteins	2025:2074	The implications of these results for both the control of oligosaccharide processing in different cell lines and the genetic engineering of mammalian glycoproteins are discussed.
2514791	0	41	theme	Cell-type-specific	0:17	arg1	N-glycosylation					37:51	Cell-type-specific and site-specific N-glycosylation	0:51	Cell-type-specific and site-specific N-glycosylation of type I and type II human tissue plasminogen activator	0:108	Cell-type-specific and site-specific N-glycosylation of type I and type II human tissue plasminogen activator.
2514791	6	42	theme	same	1889:1892	arg1	polypeptide					1899:1909	the same t-PA polypeptide	1885:1909	the same t-PA polypeptide	1885:1909	Further, the two cell lines express no glycoform in common, despite expressing the same t-PA polypeptide.
2514791	3	43	theme	oligosaccharide	602:616	arg1	structures					618:627	the oligosaccharide structures	598:627	the oligosaccharide structures at each of the N-glycosylation sites of type I and type II t-PA	598:691	In an effort to elucidate the factors controlling the expression of N-linked oligosaccharides on this polypeptide, we have used a combination of sequential exoglycosidase digestion, methylation analysis, and controlled acetolysis to determine the oligosaccharide structures at each of the N-glycosylation sites of type I and type II t-PA when isolated from a human colon fibroblast cell strain and from a Bowes melanoma cell line.
2514791	4	44	theme	sialylated	1330:1339	arg1	oligosaccharides					1341:1356	both neutral and sialylated oligosaccharides	1313:1356	both neutral and sialylated oligosaccharides	1313:1356	Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
2514791	0	45	theme	site-specific	23:35	arg1	N-glycosylation					37:51	Cell-type-specific and site-specific N-glycosylation	0:51	Cell-type-specific and site-specific N-glycosylation of type I and type II human tissue plasminogen activator	0:108	Cell-type-specific and site-specific N-glycosylation of type I and type II human tissue plasminogen activator.
2514791	4	46	gly	N-glycosylated	853:866	arg1	I					830:830	(i) type I	821:830	(i) type I	821:830	Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
2514791	4	46	gly	N-glycosylated	853:866	arg2	t-PA					844:847	type II t-PA	836:847	type II t-PA	836:847	Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
2514791	4	46	gly	N-glycosylated	853:866	arg2	I					830:830	(i) type I	821:830	(i) type I	821:830	Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
2514791	4	46	gly	N-glycosylated	853:866	arg1	Asn-184					1046:1052	the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184	806:1052	the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184	806:1052	Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
2514791	4	46	gly	N-glycosylated	853:866	arg2	Asn-117					891:897	Asn-117	891:897	Asn-117	891:897	Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
2514791	4	46	gly	N-glycosylated	853:866	arg1	way					884:886	an identical way	871:886	an identical way	871:886	Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
2514791	4	46	gly	N-glycosylated	853:866	arg2	Asn-448					903:909	Asn-448	903:909	Asn-448	903:909	Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
2514791	4	46	gly	N-glycosylated	853:866	arg1	t-PA					844:847	type II t-PA	836:847	type II t-PA	836:847	Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
2514791	4	47	theme	fibroblast	1151:1160	arg1	cells					1162:1166	fibroblast cells	1151:1166	fibroblast cells	1151:1166	Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
2514791	7	48	theme	genetic	2029:2035	arg1	engineering					2037:2047	the genetic engineering	2025:2047	the genetic engineering of mammalian glycoproteins	2025:2074	The implications of these results for both the control of oligosaccharide processing in different cell lines and the genetic engineering of mammalian glycoproteins are discussed.
2514791	3	49	dep	type	669:672	arg1	t-PA					688:691	t-PA	688:691	t-PA	688:691	In an effort to elucidate the factors controlling the expression of N-linked oligosaccharides on this polypeptide, we have used a combination of sequential exoglycosidase digestion, methylation analysis, and controlled acetolysis to determine the oligosaccharide structures at each of the N-glycosylation sites of type I and type II t-PA when isolated from a human colon fibroblast cell strain and from a Bowes melanoma cell line.
2514791	3	50	theme	fibroblast	726:735	arg1	strain					742:747	a human colon fibroblast cell strain	712:747	a human colon fibroblast cell strain	712:747	In an effort to elucidate the factors controlling the expression of N-linked oligosaccharides on this polypeptide, we have used a combination of sequential exoglycosidase digestion, methylation analysis, and controlled acetolysis to determine the oligosaccharide structures at each of the N-glycosylation sites of type I and type II t-PA when isolated from a human colon fibroblast cell strain and from a Bowes melanoma cell line.
2514791	4	51	from	Asn-448	903:909	arg1	N-glycosylated					853:866	N-glycosylated	853:866	N-glycosylated	853:866	Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
2514791	4	52	theme	cell	1574:1577	arg1	lines					1579:1583	the two cell lines	1566:1583	the two cell lines	1566:1583	Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
2514791	7	53	gly	glycoproteins	2062:2074	arg1	glycoproteins					2062:2074	mammalian glycoproteins	2052:2074	mammalian glycoproteins	2052:2074	The implications of these results for both the control of oligosaccharide processing in different cell lines and the genetic engineering of mammalian glycoproteins are discussed.
2514791	4	54	theme	sulfated	1416:1423	arg1	oligosaccharides					1425:1440	sulfated oligosaccharides	1416:1440	sulfated oligosaccharides	1416:1440	Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
2514791	4	55	from	Asn-117	891:897	arg1	N-glycosylated					853:866	N-glycosylated	853:866	N-glycosylated	853:866	Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
2514791	0	56	gly	N-glycosylation	37:51	arg1	type					56:59	type I	56:61	type I	56:61	Cell-type-specific and site-specific N-glycosylation of type I and type II human tissue plasminogen activator.
2514791	0	56	gly	N-glycosylation	37:51	arg1	type					67:70	type II	67:73	type II	67:73	Cell-type-specific and site-specific N-glycosylation of type I and type II human tissue plasminogen activator.
2514791	4	57	from	lines	1579:1583	arg1	t-PA					1556:1559	t-PA	1556:1559	t-PA from the two cell lines	1556:1583	Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
2514791	7	58	theme	cell	2010:2013	arg1	lines					2015:2019	different cell lines	2000:2019	different cell lines	2000:2019	The implications of these results for both the control of oligosaccharide processing in different cell lines and the genetic engineering of mammalian glycoproteins are discussed.
2514791	4	59	from	way	884:886	arg1	N-glycosylated					853:866	N-glycosylated	853:866	N-glycosylated	853:866	Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
2514791	4	60	theme	same	935:938	arg1	line					945:948	the same cell line	931:948	the same cell line	931:948	Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
2514791	3	61	from	each	632:635	arg1	structures					618:627	the oligosaccharide structures	598:627	the oligosaccharide structures at each of the N-glycosylation sites of type I and type II t-PA	598:691	In an effort to elucidate the factors controlling the expression of N-linked oligosaccharides on this polypeptide, we have used a combination of sequential exoglycosidase digestion, methylation analysis, and controlled acetolysis to determine the oligosaccharide structures at each of the N-glycosylation sites of type I and type II t-PA when isolated from a human colon fibroblast cell strain and from a Bowes melanoma cell line.
2514791	4	62	theme	oligomannose-type	1196:1212	arg1	structures					1214:1223	oligomannose-type structures	1196:1223	oligomannose-type structures	1196:1223	Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
2514791	4	63	from	N-glycosylated	853:866	arg1	way					884:886	an identical way	871:886	an identical way	871:886	Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
2514791	3	64	theme	N-glycosylation	644:658	arg1	sites					660:664	the N-glycosylation sites	640:664	the N-glycosylation sites of type I and type II t-PA	640:691	In an effort to elucidate the factors controlling the expression of N-linked oligosaccharides on this polypeptide, we have used a combination of sequential exoglycosidase digestion, methylation analysis, and controlled acetolysis to determine the oligosaccharide structures at each of the N-glycosylation sites of type I and type II t-PA when isolated from a human colon fibroblast cell strain and from a Bowes melanoma cell line.
2514791	3	64	theme	N-glycosylation	644:658	arg1	type					669:672	type I	669:674	type I	669:674	In an effort to elucidate the factors controlling the expression of N-linked oligosaccharides on this polypeptide, we have used a combination of sequential exoglycosidase digestion, methylation analysis, and controlled acetolysis to determine the oligosaccharide structures at each of the N-glycosylation sites of type I and type II t-PA when isolated from a human colon fibroblast cell strain and from a Bowes melanoma cell line.
2514791	3	64	theme	N-glycosylation	644:658	arg1	type					680:683	type II	680:686	type II	680:686	In an effort to elucidate the factors controlling the expression of N-linked oligosaccharides on this polypeptide, we have used a combination of sequential exoglycosidase digestion, methylation analysis, and controlled acetolysis to determine the oligosaccharide structures at each of the N-glycosylation sites of type I and type II t-PA when isolated from a human colon fibroblast cell strain and from a Bowes melanoma cell line.
2514791	5	65	from	nature	1738:1743	arg1	polypeptide					1793:1803	a common polypeptide	1784:1803	a common polypeptide	1784:1803	These results indicate that the t-PA glycoprotein is secreted by each cell line as a set of glycoforms, each glycoform being unique with respect to the nature and disposition of oligosaccharides on a common polypeptide.
2514791	4	66	theme	oligomannose-type	997:1013	arg1	structures					1015:1024	oligomannose-type structures	997:1024	oligomannose-type structures in all cases	997:1037	Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
2514791	3	67	theme	type	680:683	arg1	sites					660:664	the N-glycosylation sites	640:664	the N-glycosylation sites of type I and type II t-PA	640:691	In an effort to elucidate the factors controlling the expression of N-linked oligosaccharides on this polypeptide, we have used a combination of sequential exoglycosidase digestion, methylation analysis, and controlled acetolysis to determine the oligosaccharide structures at each of the N-glycosylation sites of type I and type II t-PA when isolated from a human colon fibroblast cell strain and from a Bowes melanoma cell line.
2514791	3	67	theme	type	680:683	arg1	type					669:672	type I	669:674	type I	669:674	In an effort to elucidate the factors controlling the expression of N-linked oligosaccharides on this polypeptide, we have used a combination of sequential exoglycosidase digestion, methylation analysis, and controlled acetolysis to determine the oligosaccharide structures at each of the N-glycosylation sites of type I and type II t-PA when isolated from a human colon fibroblast cell strain and from a Bowes melanoma cell line.
2514791	3	67	theme	type	680:683	arg1	type					680:683	type II	680:686	type II	680:686	In an effort to elucidate the factors controlling the expression of N-linked oligosaccharides on this polypeptide, we have used a combination of sequential exoglycosidase digestion, methylation analysis, and controlled acetolysis to determine the oligosaccharide structures at each of the N-glycosylation sites of type I and type II t-PA when isolated from a human colon fibroblast cell strain and from a Bowes melanoma cell line.
2514791	4	68	theme	type	1487:1490	arg1	t-PA					1495:1498	type II t-PA	1487:1498	type II t-PA	1487:1498	Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
2514791	2	69	from	two	320:322	arg1	type					327:330	type II	327:333	type II	327:333	The t-PA polypeptide has four potential N-glycosylation sites of which three are occupied in type I (Asn-117, -184, and -448) and two in type II (Asn-117 and -448).
2514791	7	70	theme	processing	1986:1995	arg1	control					1959:1965	the control	1955:1965	the control of oligosaccharide processing in different cell lines	1955:2019	The implications of these results for both the control of oligosaccharide processing in different cell lines and the genetic engineering of mammalian glycoproteins are discussed.
2514791	7	70	theme	processing	1986:1995	arg1	engineering					2037:2047	the genetic engineering	2025:2047	the genetic engineering of mammalian glycoproteins	2025:2074	The implications of these results for both the control of oligosaccharide processing in different cell lines and the genetic engineering of mammalian glycoproteins are discussed.
2514791	5	71	theme	oligosaccharides	1764:1779	arg1	disposition					1749:1759	disposition	1749:1759	disposition	1749:1759	These results indicate that the t-PA glycoprotein is secreted by each cell line as a set of glycoforms, each glycoform being unique with respect to the nature and disposition of oligosaccharides on a common polypeptide.
2514791	5	71	theme	oligosaccharides	1764:1779	arg1	nature					1738:1743	nature	1738:1743	nature	1738:1743	These results indicate that the t-PA glycoprotein is secreted by each cell line as a set of glycoforms, each glycoform being unique with respect to the nature and disposition of oligosaccharides on a common polypeptide.
2514791	3	72	theme	sequential	500:509	arg1	digestion					526:534	sequential exoglycosidase digestion	500:534	sequential exoglycosidase digestion	500:534	In an effort to elucidate the factors controlling the expression of N-linked oligosaccharides on this polypeptide, we have used a combination of sequential exoglycosidase digestion, methylation analysis, and controlled acetolysis to determine the oligosaccharide structures at each of the N-glycosylation sites of type I and type II t-PA when isolated from a human colon fibroblast cell strain and from a Bowes melanoma cell line.
2514791	7	73	from	lines	2015:2019	arg1	control					1959:1965	the control	1955:1965	the control of oligosaccharide processing in different cell lines	1955:2019	The implications of these results for both the control of oligosaccharide processing in different cell lines and the genetic engineering of mammalian glycoproteins are discussed.
2514791	7	73	from	lines	2015:2019	arg1	engineering					2037:2047	the genetic engineering	2025:2047	the genetic engineering of mammalian glycoproteins	2025:2074	The implications of these results for both the control of oligosaccharide processing in different cell lines and the genetic engineering of mammalian glycoproteins are discussed.
2514791	1	74	theme	fibrinolysis	176:187	arg1	initiator					163:171	an important initiator	150:171	an important initiator of fibrinolysis	150:187	Tissue plasminogen activator (t-PA) is an important initiator of fibrinolysis.
2514791	1	74	theme	fibrinolysis	176:187	arg1	activator					130:138	Tissue plasminogen activator	111:138	Tissue plasminogen activator (t-PA)	111:145	Tissue plasminogen activator (t-PA) is an important initiator of fibrinolysis.
2514791	5	75	from	oligosaccharides	1764:1779	arg1	polypeptide					1793:1803	a common polypeptide	1784:1803	a common polypeptide	1784:1803	These results indicate that the t-PA glycoprotein is secreted by each cell line as a set of glycoforms, each glycoform being unique with respect to the nature and disposition of oligosaccharides on a common polypeptide.
2514791	3	76	used	used	478:481	arg2	we					470:471	we	470:471	we	470:471	In an effort to elucidate the factors controlling the expression of N-linked oligosaccharides on this polypeptide, we have used a combination of sequential exoglycosidase digestion, methylation analysis, and controlled acetolysis to determine the oligosaccharide structures at each of the N-glycosylation sites of type I and type II t-PA when isolated from a human colon fibroblast cell strain and from a Bowes melanoma cell line.
2514791	4	77	dep	N-glycosylated	853:866	arg1	iii					1041:1043	iii	1041:1043	iii	1041:1043	Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
2514791	4	78	dep	Asn-184	1046:1052	arg1	N-glycosylated					853:866	N-glycosylated	853:866	N-glycosylated	853:866	Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
2514791	5	79	theme	t-PA	1618:1621	arg1	glycoprotein					1623:1634	the t-PA glycoprotein	1614:1634	the t-PA glycoprotein	1614:1634	These results indicate that the t-PA glycoprotein is secreted by each cell line as a set of glycoforms, each glycoform being unique with respect to the nature and disposition of oligosaccharides on a common polypeptide.
2514791	5	79	theme	t-PA	1618:1621	arg1	glycoforms					1678:1687	glycoforms	1678:1687	glycoforms	1678:1687	These results indicate that the t-PA glycoprotein is secreted by each cell line as a set of glycoforms, each glycoform being unique with respect to the nature and disposition of oligosaccharides on a common polypeptide.
2514791	5	79	theme	t-PA	1618:1621	arg1	set					1671:1673	a set	1669:1673	a set of glycoforms	1669:1687	These results indicate that the t-PA glycoprotein is secreted by each cell line as a set of glycoforms, each glycoform being unique with respect to the nature and disposition of oligosaccharides on a common polypeptide.
2514791	4	80	theme	type	825:828	arg1	I					830:830	(i) type I	821:830	(i) type I	821:830	Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
2514791	2	81	gly	N-glycosylation	230:244	arg2	four					215:218	four	215:218	four	215:218	The t-PA polypeptide has four potential N-glycosylation sites of which three are occupied in type I (Asn-117, -184, and -448) and two in type II (Asn-117 and -448).
2514791	2	81	gly	N-glycosylation	230:244	arg2	sites					246:250	four potential N-glycosylation sites	215:250	four potential N-glycosylation sites of which three are occupied in type I (Asn-117, -184, and -448) and two in type II (Asn-117 and -448)	215:352	The t-PA polypeptide has four potential N-glycosylation sites of which three are occupied in type I (Asn-117, -184, and -448) and two in type II (Asn-117 and -448).
2514791	3	82	theme	methylation	537:547	arg1	analysis					549:556	methylation analysis	537:556	methylation analysis	537:556	In an effort to elucidate the factors controlling the expression of N-linked oligosaccharides on this polypeptide, we have used a combination of sequential exoglycosidase digestion, methylation analysis, and controlled acetolysis to determine the oligosaccharide structures at each of the N-glycosylation sites of type I and type II t-PA when isolated from a human colon fibroblast cell strain and from a Bowes melanoma cell line.
2514791	7	83	from	engineering	2037:2047	arg1	lines					2015:2019	different cell lines	2000:2019	different cell lines	2000:2019	The implications of these results for both the control of oligosaccharide processing in different cell lines and the genetic engineering of mammalian glycoproteins are discussed.
2514791	5	84	from	polypeptide	1793:1803	arg1	disposition					1749:1759	disposition	1749:1759	disposition	1749:1759	These results indicate that the t-PA glycoprotein is secreted by each cell line as a set of glycoforms, each glycoform being unique with respect to the nature and disposition of oligosaccharides on a common polypeptide.
2514791	5	84	from	polypeptide	1793:1803	arg1	nature					1738:1743	nature	1738:1743	nature	1738:1743	These results indicate that the t-PA glycoprotein is secreted by each cell line as a set of glycoforms, each glycoform being unique with respect to the nature and disposition of oligosaccharides on a common polypeptide.
2514791	3	85	theme	colon	720:724	arg1	strain					742:747	a human colon fibroblast cell strain	712:747	a human colon fibroblast cell strain	712:747	In an effort to elucidate the factors controlling the expression of N-linked oligosaccharides on this polypeptide, we have used a combination of sequential exoglycosidase digestion, methylation analysis, and controlled acetolysis to determine the oligosaccharide structures at each of the N-glycosylation sites of type I and type II t-PA when isolated from a human colon fibroblast cell strain and from a Bowes melanoma cell line.
2514791	5	86	theme	glycoforms	1678:1687	arg1	glycoprotein					1623:1634	the t-PA glycoprotein	1614:1634	the t-PA glycoprotein	1614:1634	These results indicate that the t-PA glycoprotein is secreted by each cell line as a set of glycoforms, each glycoform being unique with respect to the nature and disposition of oligosaccharides on a common polypeptide.
2514791	5	86	theme	glycoforms	1678:1687	arg1	glycoforms					1678:1687	glycoforms	1678:1687	glycoforms	1678:1687	These results indicate that the t-PA glycoprotein is secreted by each cell line as a set of glycoforms, each glycoform being unique with respect to the nature and disposition of oligosaccharides on a common polypeptide.
2514791	5	86	theme	glycoforms	1678:1687	arg1	set					1671:1673	a set	1669:1673	a set of glycoforms	1669:1687	These results indicate that the t-PA glycoprotein is secreted by each cell line as a set of glycoforms, each glycoform being unique with respect to the nature and disposition of oligosaccharides on a common polypeptide.
2514791	2	87	theme	potential	220:228	arg1	sites					246:250	four potential N-glycosylation sites	215:250	four potential N-glycosylation sites of which three are occupied in type I (Asn-117, -184, and -448) and two in type II (Asn-117 and -448)	215:352	The t-PA polypeptide has four potential N-glycosylation sites of which three are occupied in type I (Asn-117, -184, and -448) and two in type II (Asn-117 and -448).
2514791	1	88	theme	plasminogen	118:128	arg1	initiator					163:171	an important initiator	150:171	an important initiator of fibrinolysis	150:187	Tissue plasminogen activator (t-PA) is an important initiator of fibrinolysis.
2514791	1	88	theme	plasminogen	118:128	arg1	t-PA					141:144	t-PA	141:144	t-PA	141:144	Tissue plasminogen activator (t-PA) is an important initiator of fibrinolysis.
2514791	1	88	theme	plasminogen	118:128	arg1	activator					130:138	Tissue plasminogen activator	111:138	Tissue plasminogen activator (t-PA)	111:145	Tissue plasminogen activator (t-PA) is an important initiator of fibrinolysis.
2514791	3	89	theme	controlled	563:572	arg1	acetolysis					574:583	controlled acetolysis	563:583	controlled acetolysis	563:583	In an effort to elucidate the factors controlling the expression of N-linked oligosaccharides on this polypeptide, we have used a combination of sequential exoglycosidase digestion, methylation analysis, and controlled acetolysis to determine the oligosaccharide structures at each of the N-glycosylation sites of type I and type II t-PA when isolated from a human colon fibroblast cell strain and from a Bowes melanoma cell line.
2514791	4	90	dep	Asn-117	956:962	arg1	ii					952:953	ii	952:953	ii	952:953	Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
2514791	5	91	from	disposition	1749:1759	arg1	polypeptide					1793:1803	a common polypeptide	1784:1803	a common polypeptide	1784:1803	These results indicate that the t-PA glycoprotein is secreted by each cell line as a set of glycoforms, each glycoform being unique with respect to the nature and disposition of oligosaccharides on a common polypeptide.
2514791	3	92	theme	cell	737:740	arg1	strain					742:747	a human colon fibroblast cell strain	712:747	a human colon fibroblast cell strain	712:747	In an effort to elucidate the factors controlling the expression of N-linked oligosaccharides on this polypeptide, we have used a combination of sequential exoglycosidase digestion, methylation analysis, and controlled acetolysis to determine the oligosaccharide structures at each of the N-glycosylation sites of type I and type II t-PA when isolated from a human colon fibroblast cell strain and from a Bowes melanoma cell line.
2514791	0	93	theme	tissue	81:86	arg1	activator					100:108	human tissue plasminogen activator	75:108	human tissue plasminogen activator	75:108	Cell-type-specific and site-specific N-glycosylation of type I and type II human tissue plasminogen activator.
2514791	7	94	from	processing	1986:1995	arg1	lines					2015:2019	different cell lines	2000:2019	different cell lines	2000:2019	The implications of these results for both the control of oligosaccharide processing in different cell lines and the genetic engineering of mammalian glycoproteins are discussed.
2514791	4	95	theme	identical	874:882	arg1	way					884:886	an identical way	871:886	an identical way	871:886	Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
2514791	4	96	theme	complex-type	1100:1111	arg1	structures					1113:1122	complex-type structures	1100:1122	complex-type structures when t-PA is isolated from fibroblast cells	1100:1166	Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
2514791	2	97	dep	type	283:286	arg1	two					320:322	two	320:322	two	320:322	The t-PA polypeptide has four potential N-glycosylation sites of which three are occupied in type I (Asn-117, -184, and -448) and two in type II (Asn-117 and -448).
2514791	2	97	dep	type	283:286	arg1	I					288:288	I	288:288	I	288:288	The t-PA polypeptide has four potential N-glycosylation sites of which three are occupied in type I (Asn-117, -184, and -448) and two in type II (Asn-117 and -448).
2514791	3	98	theme	melanoma	766:773	arg1	line					780:783	a Bowes melanoma cell line	758:783	a Bowes melanoma cell line	758:783	In an effort to elucidate the factors controlling the expression of N-linked oligosaccharides on this polypeptide, we have used a combination of sequential exoglycosidase digestion, methylation analysis, and controlled acetolysis to determine the oligosaccharide structures at each of the N-glycosylation sites of type I and type II t-PA when isolated from a human colon fibroblast cell strain and from a Bowes melanoma cell line.
2514791	6	99	gly	glycoform	1845:1853	arg2	common					1858:1863	common	1858:1863	common	1858:1863	Further, the two cell lines express no glycoform in common, despite expressing the same t-PA polypeptide.
2514791	4	100	dep	I	830:830	arg1	i					822:822	i	822:822	i	822:822	Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
2514791	4	101	gly	sialylated	1330:1339	arg1	oligosaccharides					1341:1356	both neutral and sialylated oligosaccharides	1313:1356	both neutral and sialylated oligosaccharides	1313:1356	Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
2514791	3	102	theme	N-linked	423:430	arg1	oligosaccharides					432:447	N-linked oligosaccharides	423:447	N-linked oligosaccharides	423:447	In an effort to elucidate the factors controlling the expression of N-linked oligosaccharides on this polypeptide, we have used a combination of sequential exoglycosidase digestion, methylation analysis, and controlled acetolysis to determine the oligosaccharide structures at each of the N-glycosylation sites of type I and type II t-PA when isolated from a human colon fibroblast cell strain and from a Bowes melanoma cell line.
2514791	6	103	theme	t-PA	1894:1897	arg1	polypeptide					1899:1909	the same t-PA polypeptide	1885:1909	the same t-PA polypeptide	1885:1909	Further, the two cell lines express no glycoform in common, despite expressing the same t-PA polypeptide.
2514791	7	104	theme	mammalian	2052:2060	arg1	glycoproteins					2062:2074	mammalian glycoproteins	2052:2074	mammalian glycoproteins	2052:2074	The implications of these results for both the control of oligosaccharide processing in different cell lines and the genetic engineering of mammalian glycoproteins are discussed.
2514791	0	105	theme	type	56:59	arg1	N-glycosylation					37:51	Cell-type-specific and site-specific N-glycosylation	0:51	Cell-type-specific and site-specific N-glycosylation of type I and type II human tissue plasminogen activator	0:108	Cell-type-specific and site-specific N-glycosylation of type I and type II human tissue plasminogen activator.
2514791	7	106	theme	results	1938:1944	arg1	implications					1916:1927	The implications	1912:1927	The implications of these results for both the control of oligosaccharide processing in different cell lines and the genetic engineering of mammalian glycoproteins	1912:2074	The implications of these results for both the control of oligosaccharide processing in different cell lines and the genetic engineering of mammalian glycoproteins are discussed.
2514791	4	107	dep	suggest	798:804	arg1	complex-					1183:1190	complex-	1183:1190	complex-	1183:1190	Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
2514791	4	107	dep	suggest	798:804	arg1	associated					1084:1093	associated	1084:1093	are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells	1066:1166	Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
2514791	3	108	theme	human	714:718	arg1	strain					742:747	a human colon fibroblast cell strain	712:747	a human colon fibroblast cell strain	712:747	In an effort to elucidate the factors controlling the expression of N-linked oligosaccharides on this polypeptide, we have used a combination of sequential exoglycosidase digestion, methylation analysis, and controlled acetolysis to determine the oligosaccharide structures at each of the N-glycosylation sites of type I and type II t-PA when isolated from a human colon fibroblast cell strain and from a Bowes melanoma cell line.
2514791	4	109	dep	cell	1276:1279	arg1	iv					1261:1262	iv	1261:1262	iv	1261:1262	Our results suggest the following: (i) type I and type II t-PA are N-glycosylated in an identical way at Asn-117 and Asn-448, when isolated from the same cell line; (ii) Asn-117 is predominantly associated with oligomannose-type structures in all cases; (iii) Asn-184 and Asn-448 are predominantly associated with complex-type structures when t-PA is isolated from fibroblast cells, but with both complex- and oligomannose-type structures when isolated from melanoma cells; (iv) fibroblast cell derived t-PA is associated with both neutral and sialylated oligosaccharides, while melanoma cell derived t-PA is also associated with sulfated oligosaccharides, which are located exclusively at Asn-448 of type II t-PA; (v) no complex-type structures occur in common between t-PA from the two cell lines.
2514791	0	110	dep	type	56:59	arg1	activator					100:108	human tissue plasminogen activator	75:108	human tissue plasminogen activator	75:108	Cell-type-specific and site-specific N-glycosylation of type I and type II human tissue plasminogen activator.
2514791	3	111	gly	N-glycosylation	644:658	arg2	type					680:683	type II	680:686	type II	680:686	In an effort to elucidate the factors controlling the expression of N-linked oligosaccharides on this polypeptide, we have used a combination of sequential exoglycosidase digestion, methylation analysis, and controlled acetolysis to determine the oligosaccharide structures at each of the N-glycosylation sites of type I and type II t-PA when isolated from a human colon fibroblast cell strain and from a Bowes melanoma cell line.
2514791	3	111	gly	N-glycosylation	644:658	arg1	type					680:683	type II	680:686	type II	680:686	In an effort to elucidate the factors controlling the expression of N-linked oligosaccharides on this polypeptide, we have used a combination of sequential exoglycosidase digestion, methylation analysis, and controlled acetolysis to determine the oligosaccharide structures at each of the N-glycosylation sites of type I and type II t-PA when isolated from a human colon fibroblast cell strain and from a Bowes melanoma cell line.
2514791	3	111	gly	N-glycosylation	644:658	arg2	type					669:672	type I	669:674	type I	669:674	In an effort to elucidate the factors controlling the expression of N-linked oligosaccharides on this polypeptide, we have used a combination of sequential exoglycosidase digestion, methylation analysis, and controlled acetolysis to determine the oligosaccharide structures at each of the N-glycosylation sites of type I and type II t-PA when isolated from a human colon fibroblast cell strain and from a Bowes melanoma cell line.
2514791	3	111	gly	N-glycosylation	644:658	arg1	type					669:672	type I	669:674	type I	669:674	In an effort to elucidate the factors controlling the expression of N-linked oligosaccharides on this polypeptide, we have used a combination of sequential exoglycosidase digestion, methylation analysis, and controlled acetolysis to determine the oligosaccharide structures at each of the N-glycosylation sites of type I and type II t-PA when isolated from a human colon fibroblast cell strain and from a Bowes melanoma cell line.
2514791	3	111	gly	N-glycosylation	644:658	arg2	sites					660:664	the N-glycosylation sites	640:664	the N-glycosylation sites of type I and type II t-PA	640:691	In an effort to elucidate the factors controlling the expression of N-linked oligosaccharides on this polypeptide, we have used a combination of sequential exoglycosidase digestion, methylation analysis, and controlled acetolysis to determine the oligosaccharide structures at each of the N-glycosylation sites of type I and type II t-PA when isolated from a human colon fibroblast cell strain and from a Bowes melanoma cell line.
2514791	3	112	theme	oligosaccharides	432:447	arg1	expression					409:418	the expression	405:418	the expression of N-linked oligosaccharides on this polypeptide	405:467	In an effort to elucidate the factors controlling the expression of N-linked oligosaccharides on this polypeptide, we have used a combination of sequential exoglycosidase digestion, methylation analysis, and controlled acetolysis to determine the oligosaccharide structures at each of the N-glycosylation sites of type I and type II t-PA when isolated from a human colon fibroblast cell strain and from a Bowes melanoma cell line.
2514791	3	113	theme	analysis	549:556	arg1	combination					485:495	a combination	483:495	a combination of sequential exoglycosidase digestion, methylation analysis, and controlled acetolysis	483:583	In an effort to elucidate the factors controlling the expression of N-linked oligosaccharides on this polypeptide, we have used a combination of sequential exoglycosidase digestion, methylation analysis, and controlled acetolysis to determine the oligosaccharide structures at each of the N-glycosylation sites of type I and type II t-PA when isolated from a human colon fibroblast cell strain and from a Bowes melanoma cell line.
2514791	5	114	dep	secreted	1639:1646	arg1	unique					1711:1716	unique	1711:1716	unique	1711:1716	These results indicate that the t-PA glycoprotein is secreted by each cell line as a set of glycoforms, each glycoform being unique with respect to the nature and disposition of oligosaccharides on a common polypeptide.
2514791	2	115	theme	t-PA	194:197	arg1	polypeptide					199:209	The t-PA polypeptide	190:209	The t-PA polypeptide	190:209	The t-PA polypeptide has four potential N-glycosylation sites of which three are occupied in type I (Asn-117, -184, and -448) and two in type II (Asn-117 and -448).
2514791	2	116	used	occupied	271:278	arg2	three					261:265	three	261:265	three	261:265	The t-PA polypeptide has four potential N-glycosylation sites of which three are occupied in type I (Asn-117, -184, and -448) and two in type II (Asn-117 and -448).
2514791	7	117	theme	different	2000:2008	arg1	lines					2015:2019	different cell lines	2000:2019	different cell lines	2000:2019	The implications of these results for both the control of oligosaccharide processing in different cell lines and the genetic engineering of mammalian glycoproteins are discussed.
21780104	2	0	theme	colon	336:340	arg1	progression					349:359	colon cancer progression	336:359	colon cancer progression	336:359	To elucidate relationships between glycosylation and colon cancer progression, we analyzed glycosylation status of β-haptoglobin (β-Hp) obtained from 46 cancer patients, 14 inflammatory bowel disease patients and 38 normal subjects.
21780104	7	1	theme	LC/MS	1114:1118	arg1	analysis					1120:1127	sequential LC/MS analysis	1103:1127	sequential LC/MS analysis	1103:1127	Moreover, site-specific glycan occupancy was determined by sequential LC/MS analysis.
21780104	3	2	theme	lectin	533:538	arg1	reactivity					540:549	Aleuria aurantia lectin reactivity	516:549	Aleuria aurantia lectin reactivity with cancer β-Hp	516:566	Aleuria aurantia lectin reactivity with cancer β-Hp was much higher than in the other two study groups.
21780104	9	3	theme	fucosylated	1393:1403	arg1	glycopeptides					1405:1417	fucosylated glycopeptides	1393:1417	fucosylated glycopeptides containing Asn 241	1393:1436	In particular, fucosylation at Asn 241 of β-Hp in sera of colon cancer patients was clearly higher than in the other groups, and the ratio of fucosylated glycopeptides containing Asn 241 decreased greatly after treatment with α1-3/4 fucosidase.
21780104	8	4	theme	β-Hp	1186:1189	arg1	fucosylation					1170:1181	fucosylation	1170:1181	fucosylation of β-Hp	1170:1189	Mass spectrometric analysis showed that fucosylation of β-Hp was higher in colon cancer patients than in other subjects.
21780104	10	5	from	useful	1581:1586	arg1	conclusion					1499:1508	conclusion	1499:1508	conclusion	1499:1508	In conclusion, the level of α1-3/4 fucosyl epitope at Asn 241 of β-Hp is potentially useful as a novel marker for colon cancer.
21780104	10	6	theme	epitope	1539:1545	arg1	level					1515:1519	the level	1511:1519	the level of α1-3/4 fucosyl epitope at Asn 241 of β-Hp	1511:1564	In conclusion, the level of α1-3/4 fucosyl epitope at Asn 241 of β-Hp is potentially useful as a novel marker for colon cancer.
21780104	10	6	theme	epitope	1539:1545	arg1	useful					1581:1586	useful	1581:1586	useful	1581:1586	In conclusion, the level of α1-3/4 fucosyl epitope at Asn 241 of β-Hp is potentially useful as a novel marker for colon cancer.
21780104	3	7	theme	Aleuria	516:522	arg1	lectin					533:538	Aleuria aurantia lectin	516:538	Aleuria aurantia lectin reactivity with cancer β-Hp	516:566	Aleuria aurantia lectin reactivity with cancer β-Hp was much higher than in the other two study groups.
21780104	1	8	theme	change	248:253	arg1	mechanism					221:229	the mechanism	217:229	the mechanism of glycosylation change	217:253	Aberrant glycosylation has been observed in many types of cancer, but the mechanism of glycosylation change is still poorly understood.
21780104	8	9	theme	colon	1205:1209	arg1	patients					1218:1225	colon cancer patients	1205:1225	colon cancer patients	1205:1225	Mass spectrometric analysis showed that fucosylation of β-Hp was higher in colon cancer patients than in other subjects.
21780104	7	10	theme	glycan	1068:1073	arg1	occupancy					1075:1083	site-specific glycan occupancy	1054:1083	site-specific glycan occupancy	1054:1083	Moreover, site-specific glycan occupancy was determined by sequential LC/MS analysis.
21780104	6	11	theme	enhanced	946:953	arg1	reactivity					962:971	enhanced lectin reactivity	946:971	enhanced lectin reactivity with the fucose moiety of colon cancer β-Hp	946:1015	Reactivity with fucosylated glycans was eliminated by treatment with α1-3/4 fucosidase but not α1-6 fucosidase, indicating that enhanced lectin reactivity with the fucose moiety of colon cancer β-Hp is due to Fucα1-3/4GlcNAc.
21780104	9	12	gly	glycopeptides	1405:1417	arg2	glycopeptides					1405:1417	fucosylated glycopeptides	1393:1417	fucosylated glycopeptides containing Asn 241	1393:1436	In particular, fucosylation at Asn 241 of β-Hp in sera of colon cancer patients was clearly higher than in the other groups, and the ratio of fucosylated glycopeptides containing Asn 241 decreased greatly after treatment with α1-3/4 fucosidase.
21780104	9	13	from	Asn	1282:1284	arg1	fucosylation					1266:1277	fucosylation	1266:1277	fucosylation at Asn 241 of β-Hp in sera of colon cancer patients	1266:1329	In particular, fucosylation at Asn 241 of β-Hp in sera of colon cancer patients was clearly higher than in the other groups, and the ratio of fucosylated glycopeptides containing Asn 241 decreased greatly after treatment with α1-3/4 fucosidase.
21780104	0	14	theme	biomarkers	135:144	arg1	development					113:123	development	113:123	development of glycan biomarkers	113:144	α1-3/4 fucosylation at Asn 241 of β-haptoglobin is a novel marker for colon cancer: a combinatorial approach for development of glycan biomarkers.
21780104	6	15	theme	colon	999:1003	arg1	cancer					1005:1010	colon cancer β-Hp	999:1015	colon cancer β-Hp	999:1015	Reactivity with fucosylated glycans was eliminated by treatment with α1-3/4 fucosidase but not α1-6 fucosidase, indicating that enhanced lectin reactivity with the fucose moiety of colon cancer β-Hp is due to Fucα1-3/4GlcNAc.
21780104	2	16	theme	bowel	469:473	arg1	disease					475:481	inflammatory bowel disease	456:481	14 inflammatory bowel disease patients	453:490	To elucidate relationships between glycosylation and colon cancer progression, we analyzed glycosylation status of β-haptoglobin (β-Hp) obtained from 46 cancer patients, 14 inflammatory bowel disease patients and 38 normal subjects.
21780104	4	17	theme	microarray	672:681	arg1	assay					683:687	microarray assay	672:687	microarray assay	672:687	These results were confirmed by lectin blotting and microarray assay using other lectins directed to fucosyl residues.
21780104	5	18	theme	such	749:752	arg1	glycans					754:760	such glycans	749:760	such glycans	749:760	Levels of such glycans were correlated with stage of colon cancer progression.
21780104	9	19	contain	containing	1419:1428	arg1	glycopeptides					1405:1417	fucosylated glycopeptides	1393:1417	fucosylated glycopeptides containing Asn 241	1393:1436	In particular, fucosylation at Asn 241 of β-Hp in sera of colon cancer patients was clearly higher than in the other groups, and the ratio of fucosylated glycopeptides containing Asn 241 decreased greatly after treatment with α1-3/4 fucosidase.
21780104	9	19	contain	containing	1419:1428	arg2	241					1434:1436	Asn 241	1430:1436	Asn 241	1430:1436	In particular, fucosylation at Asn 241 of β-Hp in sera of colon cancer patients was clearly higher than in the other groups, and the ratio of fucosylated glycopeptides containing Asn 241 decreased greatly after treatment with α1-3/4 fucosidase.
21780104	0	20	theme	colon	70:74	arg1	cancer					76:81	colon cancer	70:81	colon cancer	70:81	α1-3/4 fucosylation at Asn 241 of β-haptoglobin is a novel marker for colon cancer: a combinatorial approach for development of glycan biomarkers.
21780104	2	21	gly	glycosylation	374:386	arg1	β-haptoglobin					398:410	β-haptoglobin	398:410	β-haptoglobin (β-Hp) obtained from 46 cancer patients, 14 inflammatory bowel disease patients and 38 normal subjects	398:513	To elucidate relationships between glycosylation and colon cancer progression, we analyzed glycosylation status of β-haptoglobin (β-Hp) obtained from 46 cancer patients, 14 inflammatory bowel disease patients and 38 normal subjects.
21780104	2	21	gly	glycosylation	374:386	arg1	β-Hp					413:416	β-Hp	413:416	β-Hp	413:416	To elucidate relationships between glycosylation and colon cancer progression, we analyzed glycosylation status of β-haptoglobin (β-Hp) obtained from 46 cancer patients, 14 inflammatory bowel disease patients and 38 normal subjects.
21780104	1	22	theme	glycosylation	234:246	arg1	change					248:253	glycosylation change	234:253	glycosylation change	234:253	Aberrant glycosylation has been observed in many types of cancer, but the mechanism of glycosylation change is still poorly understood.
21780104	9	23	theme	cancer	1315:1320	arg1	patients					1322:1329	colon cancer patients	1309:1329	colon cancer patients	1309:1329	In particular, fucosylation at Asn 241 of β-Hp in sera of colon cancer patients was clearly higher than in the other groups, and the ratio of fucosylated glycopeptides containing Asn 241 decreased greatly after treatment with α1-3/4 fucosidase.
21780104	5	24	theme	cancer	798:803	arg1	progression					805:815	colon cancer progression	792:815	colon cancer progression	792:815	Levels of such glycans were correlated with stage of colon cancer progression.
21780104	2	25	theme	β-haptoglobin	398:410	arg1	status					388:393	glycosylation status	374:393	glycosylation status of β-haptoglobin (β-Hp) obtained from 46 cancer patients, 14 inflammatory bowel disease patients and 38 normal subjects	374:513	To elucidate relationships between glycosylation and colon cancer progression, we analyzed glycosylation status of β-haptoglobin (β-Hp) obtained from 46 cancer patients, 14 inflammatory bowel disease patients and 38 normal subjects.
21780104	9	26	theme	glycopeptides	1405:1417	arg1	ratio					1384:1388	the ratio	1380:1388	the ratio of fucosylated glycopeptides containing Asn 241	1380:1436	In particular, fucosylation at Asn 241 of β-Hp in sera of colon cancer patients was clearly higher than in the other groups, and the ratio of fucosylated glycopeptides containing Asn 241 decreased greatly after treatment with α1-3/4 fucosidase.
21780104	0	27	gly	fucosylation	7:18	arg1	Asn					23:25	Asn 241	23:29	Asn 241	23:29	α1-3/4 fucosylation at Asn 241 of β-haptoglobin is a novel marker for colon cancer: a combinatorial approach for development of glycan biomarkers.
21780104	0	27	gly	fucosylation	7:18	arg1	β-haptoglobin					34:46	β-haptoglobin	34:46	β-haptoglobin	34:46	α1-3/4 fucosylation at Asn 241 of β-haptoglobin is a novel marker for colon cancer: a combinatorial approach for development of glycan biomarkers.
21780104	6	28	with	Reactivity	818:827	arg1	glycans					846:852	fucosylated glycans	834:852	fucosylated glycans	834:852	Reactivity with fucosylated glycans was eliminated by treatment with α1-3/4 fucosidase but not α1-6 fucosidase, indicating that enhanced lectin reactivity with the fucose moiety of colon cancer β-Hp is due to Fucα1-3/4GlcNAc.
21780104	0	29	theme	β-haptoglobin	34:46	arg1	marker					59:64	a novel marker	51:64	a novel marker for colon cancer	51:81	α1-3/4 fucosylation at Asn 241 of β-haptoglobin is a novel marker for colon cancer: a combinatorial approach for development of glycan biomarkers.
21780104	0	29	theme	β-haptoglobin	34:46	arg1	fucosylation					7:18	α1-3/4 fucosylation	0:18	α1-3/4 fucosylation at Asn 241 of β-haptoglobin	0:46	α1-3/4 fucosylation at Asn 241 of β-haptoglobin is a novel marker for colon cancer: a combinatorial approach for development of glycan biomarkers.
21780104	9	30	theme	other	1362:1366	arg1	groups					1368:1373	the other groups	1358:1373	the other groups	1358:1373	In particular, fucosylation at Asn 241 of β-Hp in sera of colon cancer patients was clearly higher than in the other groups, and the ratio of fucosylated glycopeptides containing Asn 241 decreased greatly after treatment with α1-3/4 fucosidase.
21780104	10	31	theme	fucosyl	1531:1537	arg1	epitope					1539:1545	α1-3/4 fucosyl epitope	1524:1545	α1-3/4 fucosyl epitope	1524:1545	In conclusion, the level of α1-3/4 fucosyl epitope at Asn 241 of β-Hp is potentially useful as a novel marker for colon cancer.
21780104	9	32	gly	fucosylated	1393:1403	arg1	glycopeptides					1405:1417	fucosylated glycopeptides	1393:1417	fucosylated glycopeptides containing Asn 241	1393:1436	In particular, fucosylation at Asn 241 of β-Hp in sera of colon cancer patients was clearly higher than in the other groups, and the ratio of fucosylated glycopeptides containing Asn 241 decreased greatly after treatment with α1-3/4 fucosidase.
21780104	8	33	gly	fucosylation	1170:1181	arg1	β-Hp					1186:1189	β-Hp	1186:1189	β-Hp	1186:1189	Mass spectrometric analysis showed that fucosylation of β-Hp was higher in colon cancer patients than in other subjects.
21780104	8	34	theme	Mass	1130:1133	arg1	analysis					1149:1156	Mass spectrometric analysis	1130:1156	Mass spectrometric analysis	1130:1156	Mass spectrometric analysis showed that fucosylation of β-Hp was higher in colon cancer patients than in other subjects.
21780104	6	35	theme	α1-6	913:916	arg1	fucosidase					918:927	α1-6 fucosidase	913:927	α1-3/4 fucosidase but not α1-6 fucosidase	887:927	Reactivity with fucosylated glycans was eliminated by treatment with α1-3/4 fucosidase but not α1-6 fucosidase, indicating that enhanced lectin reactivity with the fucose moiety of colon cancer β-Hp is due to Fucα1-3/4GlcNAc.
21780104	1	36	gly	glycosylation	156:168	arg1	types					196:200	many types	191:200	many types of cancer	191:210	Aberrant glycosylation has been observed in many types of cancer, but the mechanism of glycosylation change is still poorly understood.
21780104	2	37	theme	cancer	342:347	arg1	progression					349:359	colon cancer progression	336:359	colon cancer progression	336:359	To elucidate relationships between glycosylation and colon cancer progression, we analyzed glycosylation status of β-haptoglobin (β-Hp) obtained from 46 cancer patients, 14 inflammatory bowel disease patients and 38 normal subjects.
21780104	7	38	theme	sequential	1103:1112	arg1	analysis					1120:1127	sequential LC/MS analysis	1103:1127	sequential LC/MS analysis	1103:1127	Moreover, site-specific glycan occupancy was determined by sequential LC/MS analysis.
21780104	3	39	theme	aurantia	524:531	arg1	lectin					533:538	Aleuria aurantia lectin	516:538	Aleuria aurantia lectin reactivity with cancer β-Hp	516:566	Aleuria aurantia lectin reactivity with cancer β-Hp was much higher than in the other two study groups.
21780104	1	40	theme	Aberrant	147:154	arg1	glycosylation					156:168	Aberrant glycosylation	147:168	Aberrant glycosylation	147:168	Aberrant glycosylation has been observed in many types of cancer, but the mechanism of glycosylation change is still poorly understood.
21780104	6	41	with	reactivity	962:971	arg1	moiety					989:994	the fucose moiety	978:994	the fucose moiety of colon cancer β-Hp	978:1015	Reactivity with fucosylated glycans was eliminated by treatment with α1-3/4 fucosidase but not α1-6 fucosidase, indicating that enhanced lectin reactivity with the fucose moiety of colon cancer β-Hp is due to Fucα1-3/4GlcNAc.
21780104	8	42	theme	other	1235:1239	arg1	subjects					1241:1248	other subjects	1235:1248	other subjects	1235:1248	Mass spectrometric analysis showed that fucosylation of β-Hp was higher in colon cancer patients than in other subjects.
21780104	3	43	theme	cancer	556:561	arg1	β-Hp					563:566	cancer β-Hp	556:566	cancer β-Hp	556:566	Aleuria aurantia lectin reactivity with cancer β-Hp was much higher than in the other two study groups.
21780104	9	44	theme	Asn	1430:1432	arg1	241					1434:1436	Asn 241	1430:1436	Asn 241	1430:1436	In particular, fucosylation at Asn 241 of β-Hp in sera of colon cancer patients was clearly higher than in the other groups, and the ratio of fucosylated glycopeptides containing Asn 241 decreased greatly after treatment with α1-3/4 fucosidase.
21780104	10	45	theme	β-Hp	1561:1564	arg1	Asn					1550:1552	Asn 241	1550:1556	Asn 241 of β-Hp	1550:1564	In conclusion, the level of α1-3/4 fucosyl epitope at Asn 241 of β-Hp is potentially useful as a novel marker for colon cancer.
21780104	7	46	theme	site-specific	1054:1066	arg1	occupancy					1075:1083	site-specific glycan occupancy	1054:1083	site-specific glycan occupancy	1054:1083	Moreover, site-specific glycan occupancy was determined by sequential LC/MS analysis.
21780104	5	47	theme	progression	805:815	arg1	stage					783:787	stage	783:787	stage of colon cancer progression	783:815	Levels of such glycans were correlated with stage of colon cancer progression.
21780104	9	48	from	sera	1301:1304	arg1	fucosylation					1266:1277	fucosylation	1266:1277	fucosylation at Asn 241 of β-Hp in sera of colon cancer patients	1266:1329	In particular, fucosylation at Asn 241 of β-Hp in sera of colon cancer patients was clearly higher than in the other groups, and the ratio of fucosylated glycopeptides containing Asn 241 decreased greatly after treatment with α1-3/4 fucosidase.
21780104	6	49	theme	lectin	955:960	arg1	reactivity					962:971	enhanced lectin reactivity	946:971	enhanced lectin reactivity with the fucose moiety of colon cancer β-Hp	946:1015	Reactivity with fucosylated glycans was eliminated by treatment with α1-3/4 fucosidase but not α1-6 fucosidase, indicating that enhanced lectin reactivity with the fucose moiety of colon cancer β-Hp is due to Fucα1-3/4GlcNAc.
21780104	10	50	theme	novel	1593:1597	arg1	marker					1599:1604	a novel marker	1591:1604	a novel marker for colon cancer	1591:1621	In conclusion, the level of α1-3/4 fucosyl epitope at Asn 241 of β-Hp is potentially useful as a novel marker for colon cancer.
21780104	1	51	theme	many	191:194	arg1	types					196:200	many types	191:200	many types of cancer	191:210	Aberrant glycosylation has been observed in many types of cancer, but the mechanism of glycosylation change is still poorly understood.
21780104	8	52	theme	cancer	1211:1216	arg1	patients					1218:1225	colon cancer patients	1205:1225	colon cancer patients	1205:1225	Mass spectrometric analysis showed that fucosylation of β-Hp was higher in colon cancer patients than in other subjects.
21780104	9	53	gly	fucosylation	1266:1277	arg1	Asn					1282:1284	Asn 241	1282:1288	Asn 241	1282:1288	In particular, fucosylation at Asn 241 of β-Hp in sera of colon cancer patients was clearly higher than in the other groups, and the ratio of fucosylated glycopeptides containing Asn 241 decreased greatly after treatment with α1-3/4 fucosidase.
21780104	9	53	gly	fucosylation	1266:1277	arg1	β-Hp					1293:1296	β-Hp	1293:1296	β-Hp in sera of colon cancer patients	1293:1329	In particular, fucosylation at Asn 241 of β-Hp in sera of colon cancer patients was clearly higher than in the other groups, and the ratio of fucosylated glycopeptides containing Asn 241 decreased greatly after treatment with α1-3/4 fucosidase.
21780104	0	54	theme	glycan	128:133	arg1	biomarkers					135:144	glycan biomarkers	128:144	glycan biomarkers	128:144	α1-3/4 fucosylation at Asn 241 of β-haptoglobin is a novel marker for colon cancer: a combinatorial approach for development of glycan biomarkers.
21780104	1	55	located	observed	179:186	arg2	glycosylation					156:168	Aberrant glycosylation	147:168	Aberrant glycosylation	147:168	Aberrant glycosylation has been observed in many types of cancer, but the mechanism of glycosylation change is still poorly understood.
21780104	1	55	located	observed	179:186	arg1	types					196:200	many types	191:200	many types of cancer	191:210	Aberrant glycosylation has been observed in many types of cancer, but the mechanism of glycosylation change is still poorly understood.
21780104	3	56	theme	other	596:600	arg1	groups					612:617	the other two study groups	592:617	the other two study groups	592:617	Aleuria aurantia lectin reactivity with cancer β-Hp was much higher than in the other two study groups.
21780104	4	57	theme	other	695:699	arg1	lectins					701:707	other lectins	695:707	other lectins directed to fucosyl residues	695:736	These results were confirmed by lectin blotting and microarray assay using other lectins directed to fucosyl residues.
21780104	0	58	theme	novel	53:57	arg1	marker					59:64	a novel marker	51:64	a novel marker for colon cancer	51:81	α1-3/4 fucosylation at Asn 241 of β-haptoglobin is a novel marker for colon cancer: a combinatorial approach for development of glycan biomarkers.
21780104	0	58	theme	novel	53:57	arg1	fucosylation					7:18	α1-3/4 fucosylation	0:18	α1-3/4 fucosylation at Asn 241 of β-haptoglobin	0:46	α1-3/4 fucosylation at Asn 241 of β-haptoglobin is a novel marker for colon cancer: a combinatorial approach for development of glycan biomarkers.
21780104	6	59	theme	cancer	1005:1010	arg1	moiety					989:994	the fucose moiety	978:994	the fucose moiety of colon cancer β-Hp	978:1015	Reactivity with fucosylated glycans was eliminated by treatment with α1-3/4 fucosidase but not α1-6 fucosidase, indicating that enhanced lectin reactivity with the fucose moiety of colon cancer β-Hp is due to Fucα1-3/4GlcNAc.
21780104	2	60	theme	disease	475:481	arg1	patients					443:450	46 cancer patients	433:450	46 cancer patients	433:450	To elucidate relationships between glycosylation and colon cancer progression, we analyzed glycosylation status of β-haptoglobin (β-Hp) obtained from 46 cancer patients, 14 inflammatory bowel disease patients and 38 normal subjects.
21780104	2	60	theme	disease	475:481	arg1	patients					483:490	14 inflammatory bowel disease patients	453:490	14 inflammatory bowel disease patients	453:490	To elucidate relationships between glycosylation and colon cancer progression, we analyzed glycosylation status of β-haptoglobin (β-Hp) obtained from 46 cancer patients, 14 inflammatory bowel disease patients and 38 normal subjects.
21780104	0	61	from	Asn	23:25	arg1	marker					59:64	a novel marker	51:64	a novel marker for colon cancer	51:81	α1-3/4 fucosylation at Asn 241 of β-haptoglobin is a novel marker for colon cancer: a combinatorial approach for development of glycan biomarkers.
21780104	0	61	from	Asn	23:25	arg1	fucosylation					7:18	α1-3/4 fucosylation	0:18	α1-3/4 fucosylation at Asn 241 of β-haptoglobin	0:46	α1-3/4 fucosylation at Asn 241 of β-haptoglobin is a novel marker for colon cancer: a combinatorial approach for development of glycan biomarkers.
21780104	4	62	theme	lectin	652:657	arg1	blotting					659:666	lectin blotting	652:666	lectin blotting	652:666	These results were confirmed by lectin blotting and microarray assay using other lectins directed to fucosyl residues.
21780104	10	63	from	conclusion	1499:1508	arg1	level					1515:1519	the level	1511:1519	the level of α1-3/4 fucosyl epitope at Asn 241 of β-Hp	1511:1564	In conclusion, the level of α1-3/4 fucosyl epitope at Asn 241 of β-Hp is potentially useful as a novel marker for colon cancer.
21780104	10	63	from	conclusion	1499:1508	arg1	useful					1581:1586	useful	1581:1586	useful	1581:1586	In conclusion, the level of α1-3/4 fucosyl epitope at Asn 241 of β-Hp is potentially useful as a novel marker for colon cancer.
21780104	2	64	theme	inflammatory	456:467	arg1	disease					475:481	inflammatory bowel disease	456:481	14 inflammatory bowel disease patients	453:490	To elucidate relationships between glycosylation and colon cancer progression, we analyzed glycosylation status of β-haptoglobin (β-Hp) obtained from 46 cancer patients, 14 inflammatory bowel disease patients and 38 normal subjects.
21780104	9	65	theme	β-Hp	1293:1296	arg1	fucosylation					1266:1277	fucosylation	1266:1277	fucosylation at Asn 241 of β-Hp in sera of colon cancer patients	1266:1329	In particular, fucosylation at Asn 241 of β-Hp in sera of colon cancer patients was clearly higher than in the other groups, and the ratio of fucosylated glycopeptides containing Asn 241 decreased greatly after treatment with α1-3/4 fucosidase.
21780104	6	66	theme	fucose	982:987	arg1	moiety					989:994	the fucose moiety	978:994	the fucose moiety of colon cancer β-Hp	978:1015	Reactivity with fucosylated glycans was eliminated by treatment with α1-3/4 fucosidase but not α1-6 fucosidase, indicating that enhanced lectin reactivity with the fucose moiety of colon cancer β-Hp is due to Fucα1-3/4GlcNAc.
21780104	2	67	theme	normal	499:504	arg1	patients					443:450	46 cancer patients	433:450	46 cancer patients	433:450	To elucidate relationships between glycosylation and colon cancer progression, we analyzed glycosylation status of β-haptoglobin (β-Hp) obtained from 46 cancer patients, 14 inflammatory bowel disease patients and 38 normal subjects.
21780104	2	67	theme	normal	499:504	arg1	subjects					506:513	38 normal subjects	496:513	38 normal subjects	496:513	To elucidate relationships between glycosylation and colon cancer progression, we analyzed glycosylation status of β-haptoglobin (β-Hp) obtained from 46 cancer patients, 14 inflammatory bowel disease patients and 38 normal subjects.
21780104	6	68	dep	cancer	1005:1010	arg1	β-Hp					1012:1015	β-Hp	1012:1015	colon cancer β-Hp	999:1015	Reactivity with fucosylated glycans was eliminated by treatment with α1-3/4 fucosidase but not α1-6 fucosidase, indicating that enhanced lectin reactivity with the fucose moiety of colon cancer β-Hp is due to Fucα1-3/4GlcNAc.
21780104	10	69	theme	colon	1610:1614	arg1	cancer					1616:1621	colon cancer	1610:1621	colon cancer	1610:1621	In conclusion, the level of α1-3/4 fucosyl epitope at Asn 241 of β-Hp is potentially useful as a novel marker for colon cancer.
21780104	3	70	with	reactivity	540:549	arg1	β-Hp					563:566	cancer β-Hp	556:566	cancer β-Hp	556:566	Aleuria aurantia lectin reactivity with cancer β-Hp was much higher than in the other two study groups.
21780104	9	71	theme	colon	1309:1313	arg1	patients					1322:1329	colon cancer patients	1309:1329	colon cancer patients	1309:1329	In particular, fucosylation at Asn 241 of β-Hp in sera of colon cancer patients was clearly higher than in the other groups, and the ratio of fucosylated glycopeptides containing Asn 241 decreased greatly after treatment with α1-3/4 fucosidase.
21780104	8	72	theme	spectrometric	1135:1147	arg1	analysis					1149:1156	Mass spectrometric analysis	1130:1156	Mass spectrometric analysis	1130:1156	Mass spectrometric analysis showed that fucosylation of β-Hp was higher in colon cancer patients than in other subjects.
21780104	5	73	theme	colon	792:796	arg1	progression					805:815	colon cancer progression	792:815	colon cancer progression	792:815	Levels of such glycans were correlated with stage of colon cancer progression.
21780104	9	74	theme	patients	1322:1329	arg1	sera					1301:1304	sera	1301:1304	sera of colon cancer patients	1301:1329	In particular, fucosylation at Asn 241 of β-Hp in sera of colon cancer patients was clearly higher than in the other groups, and the ratio of fucosylated glycopeptides containing Asn 241 decreased greatly after treatment with α1-3/4 fucosidase.
21780104	9	75	with	treatment	1462:1470	arg1	fucosidase					1484:1493	α1-3/4 fucosidase	1477:1493	α1-3/4 fucosidase	1477:1493	In particular, fucosylation at Asn 241 of β-Hp in sera of colon cancer patients was clearly higher than in the other groups, and the ratio of fucosylated glycopeptides containing Asn 241 decreased greatly after treatment with α1-3/4 fucosidase.
21780104	4	76	theme	fucosyl	721:727	arg1	residues					729:736	fucosyl residues	721:736	fucosyl residues	721:736	These results were confirmed by lectin blotting and microarray assay using other lectins directed to fucosyl residues.
21780104	6	77	gly	fucosylated	834:844	arg1	glycans					846:852	fucosylated glycans	834:852	fucosylated glycans	834:852	Reactivity with fucosylated glycans was eliminated by treatment with α1-3/4 fucosidase but not α1-6 fucosidase, indicating that enhanced lectin reactivity with the fucose moiety of colon cancer β-Hp is due to Fucα1-3/4GlcNAc.
21780104	6	78	with	treatment	872:880	arg1	fucosidase					918:927	α1-6 fucosidase	913:927	α1-3/4 fucosidase but not α1-6 fucosidase	887:927	Reactivity with fucosylated glycans was eliminated by treatment with α1-3/4 fucosidase but not α1-6 fucosidase, indicating that enhanced lectin reactivity with the fucose moiety of colon cancer β-Hp is due to Fucα1-3/4GlcNAc.
21780104	6	78	with	treatment	872:880	arg1	fucosidase					894:903	α1-3/4 fucosidase	887:903	α1-3/4 fucosidase but not α1-6 fucosidase	887:927	Reactivity with fucosylated glycans was eliminated by treatment with α1-3/4 fucosidase but not α1-6 fucosidase, indicating that enhanced lectin reactivity with the fucose moiety of colon cancer β-Hp is due to Fucα1-3/4GlcNAc.
21780104	5	79	theme	glycans	754:760	arg1	Levels					739:744	Levels	739:744	Levels of such glycans	739:760	Levels of such glycans were correlated with stage of colon cancer progression.
21780104	9	80	from	β-Hp	1293:1296	arg1	sera					1301:1304	sera	1301:1304	sera of colon cancer patients	1301:1329	In particular, fucosylation at Asn 241 of β-Hp in sera of colon cancer patients was clearly higher than in the other groups, and the ratio of fucosylated glycopeptides containing Asn 241 decreased greatly after treatment with α1-3/4 fucosidase.
21780104	3	81	theme	study	606:610	arg1	groups					612:617	the other two study groups	592:617	the other two study groups	592:617	Aleuria aurantia lectin reactivity with cancer β-Hp was much higher than in the other two study groups.
21780104	6	82	theme	fucosylated	834:844	arg1	glycans					846:852	fucosylated glycans	834:852	fucosylated glycans	834:852	Reactivity with fucosylated glycans was eliminated by treatment with α1-3/4 fucosidase but not α1-6 fucosidase, indicating that enhanced lectin reactivity with the fucose moiety of colon cancer β-Hp is due to Fucα1-3/4GlcNAc.
21780104	2	83	theme	cancer	436:441	arg1	patients					443:450	46 cancer patients	433:450	46 cancer patients	433:450	To elucidate relationships between glycosylation and colon cancer progression, we analyzed glycosylation status of β-haptoglobin (β-Hp) obtained from 46 cancer patients, 14 inflammatory bowel disease patients and 38 normal subjects.
21780104	2	83	theme	cancer	436:441	arg1	patients					483:490	14 inflammatory bowel disease patients	453:490	14 inflammatory bowel disease patients	453:490	To elucidate relationships between glycosylation and colon cancer progression, we analyzed glycosylation status of β-haptoglobin (β-Hp) obtained from 46 cancer patients, 14 inflammatory bowel disease patients and 38 normal subjects.
21780104	2	83	theme	cancer	436:441	arg1	subjects					506:513	38 normal subjects	496:513	38 normal subjects	496:513	To elucidate relationships between glycosylation and colon cancer progression, we analyzed glycosylation status of β-haptoglobin (β-Hp) obtained from 46 cancer patients, 14 inflammatory bowel disease patients and 38 normal subjects.
21780104	1	84	theme	cancer	205:210	arg1	types					196:200	many types	191:200	many types of cancer	191:210	Aberrant glycosylation has been observed in many types of cancer, but the mechanism of glycosylation change is still poorly understood.
21780104	9	85	from	fucosylation	1266:1277	arg1	sera					1301:1304	sera	1301:1304	sera of colon cancer patients	1301:1329	In particular, fucosylation at Asn 241 of β-Hp in sera of colon cancer patients was clearly higher than in the other groups, and the ratio of fucosylated glycopeptides containing Asn 241 decreased greatly after treatment with α1-3/4 fucosidase.
21780104	10	86	from	Asn	1550:1552	arg1	level					1515:1519	the level	1511:1519	the level of α1-3/4 fucosyl epitope at Asn 241 of β-Hp	1511:1564	In conclusion, the level of α1-3/4 fucosyl epitope at Asn 241 of β-Hp is potentially useful as a novel marker for colon cancer.
21780104	10	86	from	Asn	1550:1552	arg1	useful					1581:1586	useful	1581:1586	useful	1581:1586	In conclusion, the level of α1-3/4 fucosyl epitope at Asn 241 of β-Hp is potentially useful as a novel marker for colon cancer.
21780104	0	87	theme	combinatorial	86:98	arg1	approach					100:107	a combinatorial approach	84:107	a combinatorial approach for development of glycan biomarkers	84:144	α1-3/4 fucosylation at Asn 241 of β-haptoglobin is a novel marker for colon cancer: a combinatorial approach for development of glycan biomarkers.
21780104	2	88	theme	glycosylation	374:386	arg1	status					388:393	glycosylation status	374:393	glycosylation status of β-haptoglobin (β-Hp) obtained from 46 cancer patients, 14 inflammatory bowel disease patients and 38 normal subjects	374:513	To elucidate relationships between glycosylation and colon cancer progression, we analyzed glycosylation status of β-haptoglobin (β-Hp) obtained from 46 cancer patients, 14 inflammatory bowel disease patients and 38 normal subjects.
11356966	9	0	theme	retrovirus	994:1003	arg1	sites					1013:1017	retrovirus binding sites	994:1017	retrovirus binding sites	994:1017	Data were interpreted with respect to previous knowledge about retrovirus binding sites, to the existence of repeated homology domains, and to predictions made in family members.
11356966	10	1	theme	transmembrane	1140:1152	arg1	domains					1154:1160	12 transmembrane domains	1137:1160	12 transmembrane domains	1137:1160	A model in which PiT-2 has 12 transmembrane domains and extracellular N- and C-terminal extremities is proposed.
11356966	1	2	theme	phosphate	173:181	arg1	proteins					129:136	related multiple transmembrane proteins	98:136	related multiple transmembrane proteins which function as sodium-dependent phosphate transporters and as the cell receptors of several oncoretroviruses	98:248	PiT-1 and PiT-2 are related multiple transmembrane proteins which function as sodium-dependent phosphate transporters and as the cell receptors of several oncoretroviruses.
11356966	1	2	theme	phosphate	173:181	arg1	transporters					183:194	sodium-dependent phosphate transporters	156:194	sodium-dependent phosphate transporters	156:194	PiT-1 and PiT-2 are related multiple transmembrane proteins which function as sodium-dependent phosphate transporters and as the cell receptors of several oncoretroviruses.
11356966	8	3	theme	translation	832:842	arg1	assays					844:849	cell-free translation assays	822:849	cell-free translation assays	822:849	The orientation of C-terminal-truncation mutants expressed in cell-free translation assays and incorporated into microsomal membranes was examined by immunoprecipitation.
11356966	9	4	theme	binding	1005:1011	arg1	sites					1013:1017	retrovirus binding sites	994:1017	retrovirus binding sites	994:1017	Data were interpreted with respect to previous knowledge about retrovirus binding sites, to the existence of repeated homology domains, and to predictions made in family members.
11356966	8	5	theme	cell-free	822:830	arg1	assays					844:849	cell-free translation assays	822:849	cell-free translation assays	822:849	The orientation of C-terminal-truncation mutants expressed in cell-free translation assays and incorporated into microsomal membranes was examined by immunoprecipitation.
11356966	5	6	theme	human	608:612	arg1	PiT-2					614:618	human PiT-2	608:618	human PiT-2	608:618	We addressed this issue by a comprehensive study of human PiT-2.
11356966	1	7	theme	multiple	106:113	arg1	PiT-1					78:82	PiT-1	78:82	PiT-1	78:82	PiT-1 and PiT-2 are related multiple transmembrane proteins which function as sodium-dependent phosphate transporters and as the cell receptors of several oncoretroviruses.
11356966	1	7	theme	multiple	106:113	arg1	PiT-2					88:92	PiT-2	88:92	PiT-2	88:92	PiT-1 and PiT-2 are related multiple transmembrane proteins which function as sodium-dependent phosphate transporters and as the cell receptors of several oncoretroviruses.
11356966	1	7	theme	multiple	106:113	arg1	proteins					129:136	related multiple transmembrane proteins	98:136	related multiple transmembrane proteins which function as sodium-dependent phosphate transporters and as the cell receptors of several oncoretroviruses	98:248	PiT-1 and PiT-2 are related multiple transmembrane proteins which function as sodium-dependent phosphate transporters and as the cell receptors of several oncoretroviruses.
11356966	1	7	theme	multiple	106:113	arg1	receptors					212:220	the cell receptors	203:220	the cell receptors of several oncoretroviruses	203:248	PiT-1 and PiT-2 are related multiple transmembrane proteins which function as sodium-dependent phosphate transporters and as the cell receptors of several oncoretroviruses.
11356966	1	7	theme	multiple	106:113	arg1	transporters					183:194	sodium-dependent phosphate transporters	156:194	sodium-dependent phosphate transporters	156:194	PiT-1 and PiT-2 are related multiple transmembrane proteins which function as sodium-dependent phosphate transporters and as the cell receptors of several oncoretroviruses.
11356966	7	8	theme	C-terminal	718:727	arg1	extremities					729:739	C-terminal extremities	718:739	C-terminal extremities	718:739	Epitope tagging showed that the N- and C-terminal extremities are extracellular.
11356966	11	9	theme	further	1329:1335	arg1	investigations					1337:1350	further investigations	1329:1350	further investigations of PiT-2 interactions with other proteins	1329:1392	This model, which differs significantly from previous predictions about PiT-2 topology, may be useful for further investigations of PiT-2 interactions with other proteins and for the understanding of PiT-2 transporter and virus receptor functions.
11356966	5	10	theme	PiT-2	614:618	arg1	study					599:603	a comprehensive study	583:603	a comprehensive study of human PiT-2	583:618	We addressed this issue by a comprehensive study of human PiT-2.
11356966	1	11	theme	transmembrane	115:127	arg1	PiT-1					78:82	PiT-1	78:82	PiT-1	78:82	PiT-1 and PiT-2 are related multiple transmembrane proteins which function as sodium-dependent phosphate transporters and as the cell receptors of several oncoretroviruses.
11356966	1	11	theme	transmembrane	115:127	arg1	PiT-2					88:92	PiT-2	88:92	PiT-2	88:92	PiT-1 and PiT-2 are related multiple transmembrane proteins which function as sodium-dependent phosphate transporters and as the cell receptors of several oncoretroviruses.
11356966	1	11	theme	transmembrane	115:127	arg1	proteins					129:136	related multiple transmembrane proteins	98:136	related multiple transmembrane proteins which function as sodium-dependent phosphate transporters and as the cell receptors of several oncoretroviruses	98:248	PiT-1 and PiT-2 are related multiple transmembrane proteins which function as sodium-dependent phosphate transporters and as the cell receptors of several oncoretroviruses.
11356966	1	11	theme	transmembrane	115:127	arg1	receptors					212:220	the cell receptors	203:220	the cell receptors of several oncoretroviruses	203:248	PiT-1 and PiT-2 are related multiple transmembrane proteins which function as sodium-dependent phosphate transporters and as the cell receptors of several oncoretroviruses.
11356966	1	11	theme	transmembrane	115:127	arg1	transporters					183:194	sodium-dependent phosphate transporters	156:194	sodium-dependent phosphate transporters	156:194	PiT-1 and PiT-2 are related multiple transmembrane proteins which function as sodium-dependent phosphate transporters and as the cell receptors of several oncoretroviruses.
11356966	6	12	gly	glycosylation	647:659	arg1	asparagine					664:673	asparagine 81	664:676	asparagine 81	664:676	Evidence was obtained for glycosylation of asparagine 81.
11356966	11	13	theme	PiT-2	1423:1427	arg1	transporter					1429:1439	PiT-2 transporter	1423:1439	PiT-2 transporter	1423:1439	This model, which differs significantly from previous predictions about PiT-2 topology, may be useful for further investigations of PiT-2 interactions with other proteins and for the understanding of PiT-2 transporter and virus receptor functions.
11356966	0	14	theme	Transmembrane	0:12	arg1	receptor					68:75	a phosphate transporter-retrovirus receptor	33:75	a phosphate transporter-retrovirus receptor	33:75	Transmembrane topology of PiT-2, a phosphate transporter-retrovirus receptor.
11356966	0	14	theme	Transmembrane	0:12	arg1	topology					14:21	Transmembrane topology	0:21	Transmembrane topology of PiT-2	0:30	Transmembrane topology of PiT-2, a phosphate transporter-retrovirus receptor.
11356966	3	15	theme	current	395:401	arg1	model					421:425	A current membrane topology model	393:425	A current membrane topology model of PiT-1 and PiT-2	393:444	A current membrane topology model of PiT-1 and PiT-2 predicts 10 transmembrane domains.
11356966	11	16	theme	virus	1445:1449	arg1	functions					1460:1468	virus receptor functions	1445:1468	virus receptor functions	1445:1468	This model, which differs significantly from previous predictions about PiT-2 topology, may be useful for further investigations of PiT-2 interactions with other proteins and for the understanding of PiT-2 transporter and virus receptor functions.
11356966	11	17	theme	PiT-2	1355:1359	arg1	interactions					1361:1372	PiT-2 interactions	1355:1372	PiT-2 interactions with other proteins	1355:1392	This model, which differs significantly from previous predictions about PiT-2 topology, may be useful for further investigations of PiT-2 interactions with other proteins and for the understanding of PiT-2 transporter and virus receptor functions.
11356966	10	18	contain	has	1133:1135	arg1	PiT-2					1127:1131	PiT-2	1127:1131	PiT-2	1127:1131	A model in which PiT-2 has 12 transmembrane domains and extracellular N- and C-terminal extremities is proposed.
11356966	10	18	contain	has	1133:1135	arg2	domains					1154:1160	12 transmembrane domains	1137:1160	12 transmembrane domains	1137:1160	A model in which PiT-2 has 12 transmembrane domains and extracellular N- and C-terminal extremities is proposed.
11356966	10	18	contain	has	1133:1135	arg2	N-					1180:1181	extracellular N-	1166:1181	extracellular N-	1166:1181	A model in which PiT-2 has 12 transmembrane domains and extracellular N- and C-terminal extremities is proposed.
11356966	3	19	theme	membrane	403:410	arg1	model					421:425	A current membrane topology model	393:425	A current membrane topology model of PiT-1 and PiT-2	393:444	A current membrane topology model of PiT-1 and PiT-2 predicts 10 transmembrane domains.
11356966	10	20	theme	C-terminal	1187:1196	arg1	extremities					1198:1208	C-terminal extremities	1187:1208	C-terminal extremities	1187:1208	A model in which PiT-2 has 12 transmembrane domains and extracellular N- and C-terminal extremities is proposed.
11356966	11	21	theme	interactions	1361:1372	arg1	investigations					1337:1350	further investigations	1329:1350	further investigations of PiT-2 interactions with other proteins	1329:1392	This model, which differs significantly from previous predictions about PiT-2 topology, may be useful for further investigations of PiT-2 interactions with other proteins and for the understanding of PiT-2 transporter and virus receptor functions.
11356966	5	22	theme	comprehensive	585:597	arg1	study					599:603	a comprehensive study	583:603	a comprehensive study of human PiT-2	583:618	We addressed this issue by a comprehensive study of human PiT-2.
11356966	11	23	theme	previous	1268:1275	arg1	predictions					1277:1287	previous predictions	1268:1287	previous predictions about PiT-2 topology	1268:1308	This model, which differs significantly from previous predictions about PiT-2 topology, may be useful for further investigations of PiT-2 interactions with other proteins and for the understanding of PiT-2 transporter and virus receptor functions.
11356966	1	24	theme	cell	207:210	arg1	proteins					129:136	related multiple transmembrane proteins	98:136	related multiple transmembrane proteins which function as sodium-dependent phosphate transporters and as the cell receptors of several oncoretroviruses	98:248	PiT-1 and PiT-2 are related multiple transmembrane proteins which function as sodium-dependent phosphate transporters and as the cell receptors of several oncoretroviruses.
11356966	1	24	theme	cell	207:210	arg1	receptors					212:220	the cell receptors	203:220	the cell receptors of several oncoretroviruses	203:248	PiT-1 and PiT-2 are related multiple transmembrane proteins which function as sodium-dependent phosphate transporters and as the cell receptors of several oncoretroviruses.
11356966	0	25	theme	PiT-2	26:30	arg1	receptor					68:75	a phosphate transporter-retrovirus receptor	33:75	a phosphate transporter-retrovirus receptor	33:75	Transmembrane topology of PiT-2, a phosphate transporter-retrovirus receptor.
11356966	0	25	theme	PiT-2	26:30	arg1	topology					14:21	Transmembrane topology	0:21	Transmembrane topology of PiT-2	0:30	Transmembrane topology of PiT-2, a phosphate transporter-retrovirus receptor.
11356966	11	26	theme	PiT-2	1295:1299	arg1	topology					1301:1308	PiT-2 topology	1295:1308	PiT-2 topology	1295:1308	This model, which differs significantly from previous predictions about PiT-2 topology, may be useful for further investigations of PiT-2 interactions with other proteins and for the understanding of PiT-2 transporter and virus receptor functions.
11356966	1	27	theme	related	98:104	arg1	PiT-1					78:82	PiT-1	78:82	PiT-1	78:82	PiT-1 and PiT-2 are related multiple transmembrane proteins which function as sodium-dependent phosphate transporters and as the cell receptors of several oncoretroviruses.
11356966	1	27	theme	related	98:104	arg1	PiT-2					88:92	PiT-2	88:92	PiT-2	88:92	PiT-1 and PiT-2 are related multiple transmembrane proteins which function as sodium-dependent phosphate transporters and as the cell receptors of several oncoretroviruses.
11356966	1	27	theme	related	98:104	arg1	proteins					129:136	related multiple transmembrane proteins	98:136	related multiple transmembrane proteins which function as sodium-dependent phosphate transporters and as the cell receptors of several oncoretroviruses	98:248	PiT-1 and PiT-2 are related multiple transmembrane proteins which function as sodium-dependent phosphate transporters and as the cell receptors of several oncoretroviruses.
11356966	1	27	theme	related	98:104	arg1	receptors					212:220	the cell receptors	203:220	the cell receptors of several oncoretroviruses	203:248	PiT-1 and PiT-2 are related multiple transmembrane proteins which function as sodium-dependent phosphate transporters and as the cell receptors of several oncoretroviruses.
11356966	1	27	theme	related	98:104	arg1	transporters					183:194	sodium-dependent phosphate transporters	156:194	sodium-dependent phosphate transporters	156:194	PiT-1 and PiT-2 are related multiple transmembrane proteins which function as sodium-dependent phosphate transporters and as the cell receptors of several oncoretroviruses.
11356966	9	28	theme	homology	1049:1056	arg1	domains					1058:1064	repeated homology domains	1040:1064	repeated homology domains	1040:1064	Data were interpreted with respect to previous knowledge about retrovirus binding sites, to the existence of repeated homology domains, and to predictions made in family members.
11356966	2	29	theme	related	310:316	arg1	species					318:324	distantly related species	300:324	distantly related species	300:324	Two copies of a homology domain that is found in distantly related species assign these proteins to a large family of phosphate transporters.
11356966	9	30	theme	domains	1058:1064	arg1	existence					1027:1035	the existence	1023:1035	the existence of repeated homology domains	1023:1064	Data were interpreted with respect to previous knowledge about retrovirus binding sites, to the existence of repeated homology domains, and to predictions made in family members.
11356966	10	31	theme	extracellular	1166:1178	arg1	N-					1180:1181	extracellular N-	1166:1181	extracellular N-	1166:1181	A model in which PiT-2 has 12 transmembrane domains and extracellular N- and C-terminal extremities is proposed.
11356966	1	32	theme	several	225:231	arg1	oncoretroviruses					233:248	several oncoretroviruses	225:248	several oncoretroviruses	225:248	PiT-1 and PiT-2 are related multiple transmembrane proteins which function as sodium-dependent phosphate transporters and as the cell receptors of several oncoretroviruses.
11356966	3	33	theme	PiT-2	440:444	arg1	model					421:425	A current membrane topology model	393:425	A current membrane topology model of PiT-1 and PiT-2	393:444	A current membrane topology model of PiT-1 and PiT-2 predicts 10 transmembrane domains.
11356966	3	34	theme	transmembrane	458:470	arg1	domains					472:478	10 transmembrane domains	455:478	10 transmembrane domains	455:478	A current membrane topology model of PiT-1 and PiT-2 predicts 10 transmembrane domains.
11356966	3	35	theme	PiT-1	430:434	arg1	model					421:425	A current membrane topology model	393:425	A current membrane topology model of PiT-1 and PiT-2	393:444	A current membrane topology model of PiT-1 and PiT-2 predicts 10 transmembrane domains.
11356966	11	36	theme	transporter	1429:1439	arg1	understanding					1406:1418	the understanding	1402:1418	the understanding of PiT-2 transporter and virus receptor functions	1402:1468	This model, which differs significantly from previous predictions about PiT-2 topology, may be useful for further investigations of PiT-2 interactions with other proteins and for the understanding of PiT-2 transporter and virus receptor functions.
11356966	9	37	theme	repeated	1040:1047	arg1	domains					1058:1064	repeated homology domains	1040:1064	repeated homology domains	1040:1064	Data were interpreted with respect to previous knowledge about retrovirus binding sites, to the existence of repeated homology domains, and to predictions made in family members.
11356966	1	38	theme	oncoretroviruses	233:248	arg1	proteins					129:136	related multiple transmembrane proteins	98:136	related multiple transmembrane proteins which function as sodium-dependent phosphate transporters and as the cell receptors of several oncoretroviruses	98:248	PiT-1 and PiT-2 are related multiple transmembrane proteins which function as sodium-dependent phosphate transporters and as the cell receptors of several oncoretroviruses.
11356966	1	38	theme	oncoretroviruses	233:248	arg1	receptors					212:220	the cell receptors	203:220	the cell receptors of several oncoretroviruses	203:248	PiT-1 and PiT-2 are related multiple transmembrane proteins which function as sodium-dependent phosphate transporters and as the cell receptors of several oncoretroviruses.
11356966	0	39	theme	transporter-retrovirus	45:66	arg1	receptor					68:75	a phosphate transporter-retrovirus receptor	33:75	a phosphate transporter-retrovirus receptor	33:75	Transmembrane topology of PiT-2, a phosphate transporter-retrovirus receptor.
11356966	0	39	theme	transporter-retrovirus	45:66	arg1	topology					14:21	Transmembrane topology	0:21	Transmembrane topology of PiT-2	0:30	Transmembrane topology of PiT-2, a phosphate transporter-retrovirus receptor.
11356966	11	40	theme	functions	1460:1468	arg1	understanding					1406:1418	the understanding	1402:1418	the understanding of PiT-2 transporter and virus receptor functions	1402:1468	This model, which differs significantly from previous predictions about PiT-2 topology, may be useful for further investigations of PiT-2 interactions with other proteins and for the understanding of PiT-2 transporter and virus receptor functions.
11356966	8	41	dep	mutants	801:807	arg1	expressed					809:817	expressed	809:817	expressed in cell-free translation assays	809:849	The orientation of C-terminal-truncation mutants expressed in cell-free translation assays and incorporated into microsomal membranes was examined by immunoprecipitation.
11356966	8	41	dep	mutants	801:807	arg1	incorporated					855:866	incorporated	855:866	incorporated into microsomal membranes	855:892	The orientation of C-terminal-truncation mutants expressed in cell-free translation assays and incorporated into microsomal membranes was examined by immunoprecipitation.
11356966	2	42	theme	large	353:357	arg1	family					359:364	a large family	351:364	a large family of phosphate transporters	351:390	Two copies of a homology domain that is found in distantly related species assign these proteins to a large family of phosphate transporters.
11356966	0	43	theme	phosphate	35:43	arg1	receptor					68:75	a phosphate transporter-retrovirus receptor	33:75	a phosphate transporter-retrovirus receptor	33:75	Transmembrane topology of PiT-2, a phosphate transporter-retrovirus receptor.
11356966	0	43	theme	phosphate	35:43	arg1	topology					14:21	Transmembrane topology	0:21	Transmembrane topology of PiT-2	0:30	Transmembrane topology of PiT-2, a phosphate transporter-retrovirus receptor.
11356966	11	44	theme	other	1379:1383	arg1	proteins					1385:1392	other proteins	1379:1392	other proteins	1379:1392	This model, which differs significantly from previous predictions about PiT-2 topology, may be useful for further investigations of PiT-2 interactions with other proteins and for the understanding of PiT-2 transporter and virus receptor functions.
11356966	11	45	with	interactions	1361:1372	arg1	proteins					1385:1392	other proteins	1379:1392	other proteins	1379:1392	This model, which differs significantly from previous predictions about PiT-2 topology, may be useful for further investigations of PiT-2 interactions with other proteins and for the understanding of PiT-2 transporter and virus receptor functions.
11356966	2	46	located	found	291:295	arg1	species					318:324	distantly related species	300:324	distantly related species	300:324	Two copies of a homology domain that is found in distantly related species assign these proteins to a large family of phosphate transporters.
11356966	2	46	located	found	291:295	arg2	domain					276:281	a homology domain	265:281	a homology domain that is found in distantly related species	265:324	Two copies of a homology domain that is found in distantly related species assign these proteins to a large family of phosphate transporters.
11356966	6	47	theme	asparagine	664:673	arg1	glycosylation					647:659	glycosylation	647:659	glycosylation of asparagine 81	647:676	Evidence was obtained for glycosylation of asparagine 81.
11356966	8	48	theme	mutants	801:807	arg1	orientation					764:774	The orientation	760:774	The orientation of C-terminal-truncation mutants expressed in cell-free translation assays and incorporated into microsomal membranes	760:892	The orientation of C-terminal-truncation mutants expressed in cell-free translation assays and incorporated into microsomal membranes was examined by immunoprecipitation.
11356966	9	49	theme	previous	969:976	arg1	knowledge					978:986	previous knowledge	969:986	previous knowledge about retrovirus binding sites	969:1017	Data were interpreted with respect to previous knowledge about retrovirus binding sites, to the existence of repeated homology domains, and to predictions made in family members.
11356966	2	50	theme	domain	276:281	arg1	copies					255:260	Two copies	251:260	Two copies of a homology domain that is found in distantly related species	251:324	Two copies of a homology domain that is found in distantly related species assign these proteins to a large family of phosphate transporters.
11356966	1	51	theme	sodium-dependent	156:171	arg1	proteins					129:136	related multiple transmembrane proteins	98:136	related multiple transmembrane proteins which function as sodium-dependent phosphate transporters and as the cell receptors of several oncoretroviruses	98:248	PiT-1 and PiT-2 are related multiple transmembrane proteins which function as sodium-dependent phosphate transporters and as the cell receptors of several oncoretroviruses.
11356966	1	51	theme	sodium-dependent	156:171	arg1	transporters					183:194	sodium-dependent phosphate transporters	156:194	sodium-dependent phosphate transporters	156:194	PiT-1 and PiT-2 are related multiple transmembrane proteins which function as sodium-dependent phosphate transporters and as the cell receptors of several oncoretroviruses.
11356966	8	52	theme	C-terminal-truncation	779:799	arg1	mutants					801:807	C-terminal-truncation mutants	779:807	C-terminal-truncation mutants expressed in cell-free translation assays and incorporated into microsomal membranes	779:892	The orientation of C-terminal-truncation mutants expressed in cell-free translation assays and incorporated into microsomal membranes was examined by immunoprecipitation.
11356966	11	53	theme	receptor	1451:1458	arg1	functions					1460:1468	virus receptor functions	1445:1468	virus receptor functions	1445:1468	This model, which differs significantly from previous predictions about PiT-2 topology, may be useful for further investigations of PiT-2 interactions with other proteins and for the understanding of PiT-2 transporter and virus receptor functions.
11356966	7	54	theme	Epitope	679:685	arg1	tagging					687:693	Epitope tagging	679:693	Epitope tagging	679:693	Epitope tagging showed that the N- and C-terminal extremities are extracellular.
11356966	2	55	theme	homology	267:274	arg1	domain					276:281	a homology domain	265:281	a homology domain that is found in distantly related species	265:324	Two copies of a homology domain that is found in distantly related species assign these proteins to a large family of phosphate transporters.
11356966	2	56	theme	transporters	379:390	arg1	family					359:364	a large family	351:364	a large family of phosphate transporters	351:390	Two copies of a homology domain that is found in distantly related species assign these proteins to a large family of phosphate transporters.
11356966	8	57	theme	microsomal	873:882	arg1	membranes					884:892	microsomal membranes	873:892	microsomal membranes	873:892	The orientation of C-terminal-truncation mutants expressed in cell-free translation assays and incorporated into microsomal membranes was examined by immunoprecipitation.
11356966	3	58	theme	topology	412:419	arg1	model					421:425	A current membrane topology model	393:425	A current membrane topology model of PiT-1 and PiT-2	393:444	A current membrane topology model of PiT-1 and PiT-2 predicts 10 transmembrane domains.
11356966	4	59	theme	model	511:515	arg1	validity					494:501	the validity	490:501	the validity of this model	490:515	However, the validity of this model has not been addressed experimentally.
11356966	9	60	theme	family	1094:1099	arg1	members					1101:1107	family members	1094:1107	family members	1094:1107	Data were interpreted with respect to previous knowledge about retrovirus binding sites, to the existence of repeated homology domains, and to predictions made in family members.
11356966	2	61	theme	phosphate	369:377	arg1	transporters					379:390	phosphate transporters	369:390	phosphate transporters	369:390	Two copies of a homology domain that is found in distantly related species assign these proteins to a large family of phosphate transporters.
27114449	8	0	theme	metabolic	1196:1204	arg1	method					1215:1220	this metabolic labeling method	1191:1220	this metabolic labeling method	1191:1220	Other advantages of this metabolic labeling method include in vivo application, direct labeling of the O-GlcNAc sites and higher confidence for site identification.
27114449	6	1	theme	boronic	949:955	arg1	acid					957:960	boronic acid	949:960	boronic acid	949:960	The near stoichiometry reaction between the diol of GlcNAc and boronic acid dramatically improved the enrichment efficiency.
27114449	12	2	theme	protein	1858:1864	arg1	O-GlcNAcylation					1866:1880	protein O-GlcNAcylation	1858:1880	protein O-GlcNAcylation	1858:1880	We believe this methodology can be broadly applied to reveal turnovers/dynamics of protein O-GlcNAcylation from different biological states and will provide more information on the significance of O-GlcNAcylation, enabling us to study the temporal dynamics of this critical modification for the first time.
27114449	8	3	theme	method	1215:1220	arg1	advantages					1177:1186	Other advantages	1171:1186	Other advantages of this metabolic labeling method	1171:1220	Other advantages of this metabolic labeling method include in vivo application, direct labeling of the O-GlcNAc sites and higher confidence for site identification.
27114449	6	4	theme	GlcNAc	938:943	arg1	diol					930:933	the diol	926:933	the diol of GlcNAc and boronic acid	926:960	The near stoichiometry reaction between the diol of GlcNAc and boronic acid dramatically improved the enrichment efficiency.
27114449	7	5	theme	estimation	1159:1168	arg1	accuracy					1129:1136	the accuracy	1125:1136	the accuracy of the turnover rate estimation	1125:1168	Additionally, our kinetic model for turnover rates integrates both metabolomic and proteomic data, which increase the accuracy of the turnover rate estimation.
27114449	8	6	theme	in	1230:1231	arg1	application					1238:1248	in vivo application	1230:1248	in vivo application	1230:1248	Other advantages of this metabolic labeling method include in vivo application, direct labeling of the O-GlcNAc sites and higher confidence for site identification.
27114449	7	7	theme	turnover	1145:1152	arg1	estimation					1159:1168	the turnover rate estimation	1141:1168	the turnover rate estimation	1141:1168	Additionally, our kinetic model for turnover rates integrates both metabolomic and proteomic data, which increase the accuracy of the turnover rate estimation.
27114449	1	8	theme	fundamental	170:180	arg1	role					182:185	a fundamental role	168:185	a fundamental role	168:185	Over the past decades, protein O-GlcNAcylation has been found to play a fundamental role in cell cycle control, metabolism, transcriptional regulation, and cellular signaling.
27114449	12	9	theme	modification	2049:2060	arg1	dynamics					2023:2030	the temporal dynamics	2010:2030	the temporal dynamics of this critical modification for the first time	2010:2079	We believe this methodology can be broadly applied to reveal turnovers/dynamics of protein O-GlcNAcylation from different biological states and will provide more information on the significance of O-GlcNAcylation, enabling us to study the temporal dynamics of this critical modification for the first time.
27114449	9	10	theme	peptides	1507:1514	arg1	rates					1486:1490	turnover rates	1477:1490	turnover rates of 20 O-GlcNAc peptides from 14 proteins extracted from HeLa nuclei	1477:1558	Concentrating only on nuclear localized GlcNAc modified proteins, we are able to identify 105 O-GlcNAc peptides on 42 proteins and determine turnover rates of 20 O-GlcNAc peptides from 14 proteins extracted from HeLa nuclei.
27114449	8	11	theme	direct	1251:1256	arg1	labeling					1258:1265	direct labeling	1251:1265	direct labeling of the O-GlcNAc sites	1251:1287	Other advantages of this metabolic labeling method include in vivo application, direct labeling of the O-GlcNAc sites and higher confidence for site identification.
27114449	8	12	theme	site	1315:1318	arg1	identification					1320:1333	site identification	1315:1333	site identification	1315:1333	Other advantages of this metabolic labeling method include in vivo application, direct labeling of the O-GlcNAc sites and higher confidence for site identification.
27114449	5	13	theme	anhydrous	870:878	arg1	DMSO					880:883	anhydrous DMSO	870:883	anhydrous DMSO	870:883	First, an efficient enrichment method for O-GlcNAc peptides was developed with the use of phenylboronic acid solid-phase extraction and anhydrous DMSO.
27114449	1	14	theme	protein	121:127	arg1	O-GlcNAcylation					129:143	protein O-GlcNAcylation	121:143	protein O-GlcNAcylation	121:143	Over the past decades, protein O-GlcNAcylation has been found to play a fundamental role in cell cycle control, metabolism, transcriptional regulation, and cellular signaling.
27114449	4	15	theme	mass	646:649	arg1	proteomics					670:679	quantitative mass spectrometry-based proteomics	633:679	quantitative mass spectrometry-based proteomics	633:679	This metabolic labeling was combined with quantitative mass spectrometry-based proteomics to determine protein O-GlcNAcylation turnover rates.
27114449	5	16	theme	solid-phase	843:853	arg1	extraction					855:864	phenylboronic acid solid-phase extraction	824:864	phenylboronic acid solid-phase extraction	824:864	First, an efficient enrichment method for O-GlcNAc peptides was developed with the use of phenylboronic acid solid-phase extraction and anhydrous DMSO.
27114449	8	17	theme	O-GlcNAc	1274:1281	arg1	sites					1283:1287	the O-GlcNAc sites	1270:1287	the O-GlcNAc sites	1270:1287	Other advantages of this metabolic labeling method include in vivo application, direct labeling of the O-GlcNAc sites and higher confidence for site identification.
27114449	7	18	theme	metabolomic	1078:1088	arg1	data					1104:1107	both metabolomic and proteomic data	1073:1107	both metabolomic and proteomic data	1073:1107	Additionally, our kinetic model for turnover rates integrates both metabolomic and proteomic data, which increase the accuracy of the turnover rate estimation.
27114449	3	19	theme	biosynthetic	569:580	arg1	pathway					582:588	the hexosamine biosynthetic pathway	554:588	the hexosamine biosynthetic pathway	554:588	Here, we have developed an approach to isotopically label O-GlcNAc modifications on proteins by producing (13)C-labeled UDP-GlcNAc from (13)C6-glucose via the hexosamine biosynthetic pathway.
27114449	7	20	theme	turnover	1047:1054	arg1	rates					1056:1060	turnover rates	1047:1060	turnover rates	1047:1060	Additionally, our kinetic model for turnover rates integrates both metabolomic and proteomic data, which increase the accuracy of the turnover rate estimation.
27114449	9	21	theme	HeLa	1548:1551	arg1	nuclei					1553:1558	HeLa nuclei	1548:1558	HeLa nuclei	1548:1558	Concentrating only on nuclear localized GlcNAc modified proteins, we are able to identify 105 O-GlcNAc peptides on 42 proteins and determine turnover rates of 20 O-GlcNAc peptides from 14 proteins extracted from HeLa nuclei.
27114449	2	22	dep	in	325:326	arg1	vivo					328:331	vivo	328:331	vivo	328:331	Nevertheless, quantitative approaches to determine in vivo GlcNAc dynamics at a large-scale are still not readily available.
27114449	3	23	from	C6-glucose	539:548	arg1	UDP-GlcNAc					519:528	(13)C-labeled UDP-GlcNAc	505:528	(13)C-labeled UDP-GlcNAc from (13)C6-glucose	505:548	Here, we have developed an approach to isotopically label O-GlcNAc modifications on proteins by producing (13)C-labeled UDP-GlcNAc from (13)C6-glucose via the hexosamine biosynthetic pathway.
27114449	4	24	theme	O-GlcNAcylation	702:716	arg1	rates					727:731	protein O-GlcNAcylation turnover rates	694:731	protein O-GlcNAcylation turnover rates	694:731	This metabolic labeling was combined with quantitative mass spectrometry-based proteomics to determine protein O-GlcNAcylation turnover rates.
27114449	1	25	theme	cellular	254:261	arg1	signaling					263:271	cellular signaling	254:271	cellular signaling	254:271	Over the past decades, protein O-GlcNAcylation has been found to play a fundamental role in cell cycle control, metabolism, transcriptional regulation, and cellular signaling.
27114449	5	26	theme	extraction	855:864	arg1	use					817:819	the use	813:819	the use of phenylboronic acid solid-phase extraction and anhydrous DMSO	813:883	First, an efficient enrichment method for O-GlcNAc peptides was developed with the use of phenylboronic acid solid-phase extraction and anhydrous DMSO.
27114449	12	27	theme	first	2070:2074	arg1	time					2076:2079	the first time	2066:2079	the first time	2066:2079	We believe this methodology can be broadly applied to reveal turnovers/dynamics of protein O-GlcNAcylation from different biological states and will provide more information on the significance of O-GlcNAcylation, enabling us to study the temporal dynamics of this critical modification for the first time.
27114449	8	28	dep	in	1230:1231	arg1	vivo					1233:1236	vivo	1233:1236	vivo	1233:1236	Other advantages of this metabolic labeling method include in vivo application, direct labeling of the O-GlcNAc sites and higher confidence for site identification.
27114449	12	29	theme	more	1932:1935	arg1	information					1937:1947	more information	1932:1947	more information on the significance of O-GlcNAcylation	1932:1986	We believe this methodology can be broadly applied to reveal turnovers/dynamics of protein O-GlcNAcylation from different biological states and will provide more information on the significance of O-GlcNAcylation, enabling us to study the temporal dynamics of this critical modification for the first time.
27114449	5	30	theme	enrichment	754:763	arg1	method					765:770	an efficient enrichment method	741:770	an efficient enrichment method for O-GlcNAc peptides	741:792	First, an efficient enrichment method for O-GlcNAc peptides was developed with the use of phenylboronic acid solid-phase extraction and anhydrous DMSO.
27114449	9	31	theme	localized	1366:1374	arg1	proteins					1392:1399	nuclear localized GlcNAc modified proteins	1358:1399	nuclear localized GlcNAc modified proteins	1358:1399	Concentrating only on nuclear localized GlcNAc modified proteins, we are able to identify 105 O-GlcNAc peptides on 42 proteins and determine turnover rates of 20 O-GlcNAc peptides from 14 proteins extracted from HeLa nuclei.
27114449	9	32	theme	modified	1383:1390	arg1	proteins					1392:1399	nuclear localized GlcNAc modified proteins	1358:1399	nuclear localized GlcNAc modified proteins	1358:1399	Concentrating only on nuclear localized GlcNAc modified proteins, we are able to identify 105 O-GlcNAc peptides on 42 proteins and determine turnover rates of 20 O-GlcNAc peptides from 14 proteins extracted from HeLa nuclei.
27114449	0	33	theme	O-GlcNAcylation	72:86	arg1	Dynamics					88:95	Protein O-GlcNAcylation Dynamics	64:95	Protein O-GlcNAcylation Dynamics	64:95	A Novel Quantitative Mass Spectrometry Platform for Determining Protein O-GlcNAcylation Dynamics.
27114449	5	34	theme	acid	838:841	arg1	extraction					855:864	phenylboronic acid solid-phase extraction	824:864	phenylboronic acid solid-phase extraction	824:864	First, an efficient enrichment method for O-GlcNAc peptides was developed with the use of phenylboronic acid solid-phase extraction and anhydrous DMSO.
27114449	3	35	theme	O-GlcNAc	457:464	arg1	modifications					466:478	O-GlcNAc modifications	457:478	O-GlcNAc modifications on proteins	457:490	Here, we have developed an approach to isotopically label O-GlcNAc modifications on proteins by producing (13)C-labeled UDP-GlcNAc from (13)C6-glucose via the hexosamine biosynthetic pathway.
27114449	0	36	theme	Quantitative	8:19	arg1	Platform					39:46	A Novel Quantitative Mass Spectrometry Platform	0:46	A Novel Quantitative Mass Spectrometry Platform for Determining Protein O-GlcNAcylation Dynamics.	0:96	A Novel Quantitative Mass Spectrometry Platform for Determining Protein O-GlcNAcylation Dynamics.
27114449	9	37	from	rates	1486:1490	arg1	proteins					1524:1531	14 proteins	1521:1531	14 proteins extracted from HeLa nuclei	1521:1558	Concentrating only on nuclear localized GlcNAc modified proteins, we are able to identify 105 O-GlcNAc peptides on 42 proteins and determine turnover rates of 20 O-GlcNAc peptides from 14 proteins extracted from HeLa nuclei.
27114449	0	38	theme	Spectrometry	26:37	arg1	Platform					39:46	A Novel Quantitative Mass Spectrometry Platform	0:46	A Novel Quantitative Mass Spectrometry Platform for Determining Protein O-GlcNAcylation Dynamics.	0:96	A Novel Quantitative Mass Spectrometry Platform for Determining Protein O-GlcNAcylation Dynamics.
27114449	6	39	theme	near	890:893	arg1	reaction					909:916	The near stoichiometry reaction	886:916	The near stoichiometry reaction between the diol of GlcNAc and boronic acid	886:960	The near stoichiometry reaction between the diol of GlcNAc and boronic acid dramatically improved the enrichment efficiency.
27114449	9	40	from	proteins	1524:1531	arg1	peptides					1507:1514	20 O-GlcNAc peptides	1495:1514	20 O-GlcNAc peptides from 14 proteins extracted from HeLa nuclei	1495:1558	Concentrating only on nuclear localized GlcNAc modified proteins, we are able to identify 105 O-GlcNAc peptides on 42 proteins and determine turnover rates of 20 O-GlcNAc peptides from 14 proteins extracted from HeLa nuclei.
27114449	9	40	from	proteins	1524:1531	arg1	rates					1486:1490	turnover rates	1477:1490	turnover rates of 20 O-GlcNAc peptides from 14 proteins extracted from HeLa nuclei	1477:1558	Concentrating only on nuclear localized GlcNAc modified proteins, we are able to identify 105 O-GlcNAc peptides on 42 proteins and determine turnover rates of 20 O-GlcNAc peptides from 14 proteins extracted from HeLa nuclei.
27114449	0	41	theme	Protein	64:70	arg1	Dynamics					88:95	Protein O-GlcNAcylation Dynamics	64:95	Protein O-GlcNAcylation Dynamics	64:95	A Novel Quantitative Mass Spectrometry Platform for Determining Protein O-GlcNAcylation Dynamics.
27114449	3	42	from	modifications	466:478	arg1	proteins					483:490	proteins	483:490	proteins	483:490	Here, we have developed an approach to isotopically label O-GlcNAc modifications on proteins by producing (13)C-labeled UDP-GlcNAc from (13)C6-glucose via the hexosamine biosynthetic pathway.
27114449	2	43	theme	GlcNAc	333:338	arg1	dynamics					340:347	in vivo GlcNAc dynamics	325:347	in vivo GlcNAc dynamics	325:347	Nevertheless, quantitative approaches to determine in vivo GlcNAc dynamics at a large-scale are still not readily available.
27114449	12	44	theme	different	1887:1895	arg1	states					1908:1913	different biological states	1887:1913	different biological states	1887:1913	We believe this methodology can be broadly applied to reveal turnovers/dynamics of protein O-GlcNAcylation from different biological states and will provide more information on the significance of O-GlcNAcylation, enabling us to study the temporal dynamics of this critical modification for the first time.
27114449	4	45	theme	spectrometry-based	651:668	arg1	proteomics					670:679	quantitative mass spectrometry-based proteomics	633:679	quantitative mass spectrometry-based proteomics	633:679	This metabolic labeling was combined with quantitative mass spectrometry-based proteomics to determine protein O-GlcNAcylation turnover rates.
27114449	1	46	theme	transcriptional	222:236	arg1	regulation					238:247	transcriptional regulation	222:247	transcriptional regulation	222:247	Over the past decades, protein O-GlcNAcylation has been found to play a fundamental role in cell cycle control, metabolism, transcriptional regulation, and cellular signaling.
27114449	6	47	theme	acid	957:960	arg1	diol					930:933	the diol	926:933	the diol of GlcNAc and boronic acid	926:960	The near stoichiometry reaction between the diol of GlcNAc and boronic acid dramatically improved the enrichment efficiency.
27114449	12	48	theme	O-GlcNAcylation	1866:1880	arg1	turnovers/dynamics					1836:1853	turnovers/dynamics	1836:1853	turnovers/dynamics of protein O-GlcNAcylation from different biological states	1836:1913	We believe this methodology can be broadly applied to reveal turnovers/dynamics of protein O-GlcNAcylation from different biological states and will provide more information on the significance of O-GlcNAcylation, enabling us to study the temporal dynamics of this critical modification for the first time.
27114449	10	49	theme	O-GlcNAcylation	1582:1596	arg1	rates					1607:1611	O-GlcNAcylation turnover rates	1582:1611	O-GlcNAcylation turnover rates are slower than those published for phosphorylation or acetylation	1582:1678	In general, we found O-GlcNAcylation turnover rates are slower than those published for phosphorylation or acetylation.
27114449	7	50	theme	rate	1154:1157	arg1	estimation					1159:1168	the turnover rate estimation	1141:1168	the turnover rate estimation	1141:1168	Additionally, our kinetic model for turnover rates integrates both metabolomic and proteomic data, which increase the accuracy of the turnover rate estimation.
27114449	2	51	theme	quantitative	288:299	arg1	approaches					301:310	quantitative approaches	288:310	quantitative approaches to determine in vivo GlcNAc dynamics at a large-scale	288:364	Nevertheless, quantitative approaches to determine in vivo GlcNAc dynamics at a large-scale are still not readily available.
27114449	9	52	theme	turnover	1477:1484	arg1	rates					1486:1490	turnover rates	1477:1490	turnover rates of 20 O-GlcNAc peptides from 14 proteins extracted from HeLa nuclei	1477:1558	Concentrating only on nuclear localized GlcNAc modified proteins, we are able to identify 105 O-GlcNAc peptides on 42 proteins and determine turnover rates of 20 O-GlcNAc peptides from 14 proteins extracted from HeLa nuclei.
27114449	8	53	theme	labeling	1206:1213	arg1	method					1215:1220	this metabolic labeling method	1191:1220	this metabolic labeling method	1191:1220	Other advantages of this metabolic labeling method include in vivo application, direct labeling of the O-GlcNAc sites and higher confidence for site identification.
27114449	8	54	theme	sites	1283:1287	arg1	confidence					1300:1309	higher confidence	1293:1309	higher confidence for site identification	1293:1333	Other advantages of this metabolic labeling method include in vivo application, direct labeling of the O-GlcNAc sites and higher confidence for site identification.
27114449	8	54	theme	sites	1283:1287	arg1	application					1238:1248	in vivo application	1230:1248	in vivo application	1230:1248	Other advantages of this metabolic labeling method include in vivo application, direct labeling of the O-GlcNAc sites and higher confidence for site identification.
27114449	8	54	theme	sites	1283:1287	arg1	labeling					1258:1265	direct labeling	1251:1265	direct labeling of the O-GlcNAc sites	1251:1287	Other advantages of this metabolic labeling method include in vivo application, direct labeling of the O-GlcNAc sites and higher confidence for site identification.
27114449	2	55	theme	in	325:326	arg1	dynamics					340:347	in vivo GlcNAc dynamics	325:347	in vivo GlcNAc dynamics	325:347	Nevertheless, quantitative approaches to determine in vivo GlcNAc dynamics at a large-scale are still not readily available.
27114449	9	56	theme	O-GlcNAc	1498:1505	arg1	peptides					1507:1514	20 O-GlcNAc peptides	1495:1514	20 O-GlcNAc peptides from 14 proteins extracted from HeLa nuclei	1495:1558	Concentrating only on nuclear localized GlcNAc modified proteins, we are able to identify 105 O-GlcNAc peptides on 42 proteins and determine turnover rates of 20 O-GlcNAc peptides from 14 proteins extracted from HeLa nuclei.
27114449	12	57	theme	critical	2040:2047	arg1	modification					2049:2060	this critical modification	2035:2060	this critical modification	2035:2060	We believe this methodology can be broadly applied to reveal turnovers/dynamics of protein O-GlcNAcylation from different biological states and will provide more information on the significance of O-GlcNAcylation, enabling us to study the temporal dynamics of this critical modification for the first time.
27114449	8	58	theme	higher	1293:1298	arg1	confidence					1300:1309	higher confidence	1293:1309	higher confidence for site identification	1293:1333	Other advantages of this metabolic labeling method include in vivo application, direct labeling of the O-GlcNAc sites and higher confidence for site identification.
27114449	1	59	theme	cell	190:193	arg1	control					201:207	cell cycle control	190:207	cell cycle control	190:207	Over the past decades, protein O-GlcNAcylation has been found to play a fundamental role in cell cycle control, metabolism, transcriptional regulation, and cellular signaling.
27114449	5	60	theme	DMSO	880:883	arg1	use					817:819	the use	813:819	the use of phenylboronic acid solid-phase extraction and anhydrous DMSO	813:883	First, an efficient enrichment method for O-GlcNAc peptides was developed with the use of phenylboronic acid solid-phase extraction and anhydrous DMSO.
27114449	12	61	theme	temporal	2014:2021	arg1	dynamics					2023:2030	the temporal dynamics	2010:2030	the temporal dynamics of this critical modification for the first time	2010:2079	We believe this methodology can be broadly applied to reveal turnovers/dynamics of protein O-GlcNAcylation from different biological states and will provide more information on the significance of O-GlcNAcylation, enabling us to study the temporal dynamics of this critical modification for the first time.
27114449	6	62	theme	enrichment	988:997	arg1	efficiency					999:1008	the enrichment efficiency	984:1008	the enrichment efficiency	984:1008	The near stoichiometry reaction between the diol of GlcNAc and boronic acid dramatically improved the enrichment efficiency.
27114449	4	63	theme	quantitative	633:644	arg1	proteomics					670:679	quantitative mass spectrometry-based proteomics	633:679	quantitative mass spectrometry-based proteomics	633:679	This metabolic labeling was combined with quantitative mass spectrometry-based proteomics to determine protein O-GlcNAcylation turnover rates.
27114449	7	64	theme	proteomic	1094:1102	arg1	data					1104:1107	both metabolomic and proteomic data	1073:1107	both metabolomic and proteomic data	1073:1107	Additionally, our kinetic model for turnover rates integrates both metabolomic and proteomic data, which increase the accuracy of the turnover rate estimation.
27114449	3	65	theme	hexosamine	558:567	arg1	pathway					582:588	the hexosamine biosynthetic pathway	554:588	the hexosamine biosynthetic pathway	554:588	Here, we have developed an approach to isotopically label O-GlcNAc modifications on proteins by producing (13)C-labeled UDP-GlcNAc from (13)C6-glucose via the hexosamine biosynthetic pathway.
27114449	8	66	theme	Other	1171:1175	arg1	advantages					1177:1186	Other advantages	1171:1186	Other advantages of this metabolic labeling method	1171:1220	Other advantages of this metabolic labeling method include in vivo application, direct labeling of the O-GlcNAc sites and higher confidence for site identification.
27114449	2	67	dep	approaches	301:310	arg1	determine					315:323	determine	315:323	to determine in vivo GlcNAc dynamics at a large-scale	312:364	Nevertheless, quantitative approaches to determine in vivo GlcNAc dynamics at a large-scale are still not readily available.
27114449	10	68	dep	rates	1607:1611	arg1	slower					1617:1622	slower	1617:1622	slower	1617:1622	In general, we found O-GlcNAcylation turnover rates are slower than those published for phosphorylation or acetylation.
27114449	5	69	theme	O-GlcNAc	776:783	arg1	peptides					785:792	O-GlcNAc peptides	776:792	O-GlcNAc peptides	776:792	First, an efficient enrichment method for O-GlcNAc peptides was developed with the use of phenylboronic acid solid-phase extraction and anhydrous DMSO.
27114449	4	70	theme	protein	694:700	arg1	rates					727:731	protein O-GlcNAcylation turnover rates	694:731	protein O-GlcNAcylation turnover rates	694:731	This metabolic labeling was combined with quantitative mass spectrometry-based proteomics to determine protein O-GlcNAcylation turnover rates.
27114449	7	71	theme	kinetic	1029:1035	arg1	model					1037:1041	our kinetic model	1025:1041	our kinetic model for turnover rates	1025:1060	Additionally, our kinetic model for turnover rates integrates both metabolomic and proteomic data, which increase the accuracy of the turnover rate estimation.
27114449	4	72	theme	turnover	718:725	arg1	rates					727:731	protein O-GlcNAcylation turnover rates	694:731	protein O-GlcNAcylation turnover rates	694:731	This metabolic labeling was combined with quantitative mass spectrometry-based proteomics to determine protein O-GlcNAcylation turnover rates.
27114449	5	73	theme	efficient	744:752	arg1	method					765:770	an efficient enrichment method	741:770	an efficient enrichment method for O-GlcNAc peptides	741:792	First, an efficient enrichment method for O-GlcNAc peptides was developed with the use of phenylboronic acid solid-phase extraction and anhydrous DMSO.
27114449	9	74	theme	nuclear	1358:1364	arg1	proteins					1392:1399	nuclear localized GlcNAc modified proteins	1358:1399	nuclear localized GlcNAc modified proteins	1358:1399	Concentrating only on nuclear localized GlcNAc modified proteins, we are able to identify 105 O-GlcNAc peptides on 42 proteins and determine turnover rates of 20 O-GlcNAc peptides from 14 proteins extracted from HeLa nuclei.
27114449	9	75	theme	GlcNAc	1376:1381	arg1	proteins					1392:1399	nuclear localized GlcNAc modified proteins	1358:1399	nuclear localized GlcNAc modified proteins	1358:1399	Concentrating only on nuclear localized GlcNAc modified proteins, we are able to identify 105 O-GlcNAc peptides on 42 proteins and determine turnover rates of 20 O-GlcNAc peptides from 14 proteins extracted from HeLa nuclei.
27114449	12	76	theme	O-GlcNAcylation	1972:1986	arg1	significance					1956:1967	the significance	1952:1967	the significance of O-GlcNAcylation	1952:1986	We believe this methodology can be broadly applied to reveal turnovers/dynamics of protein O-GlcNAcylation from different biological states and will provide more information on the significance of O-GlcNAcylation, enabling us to study the temporal dynamics of this critical modification for the first time.
27114449	1	77	theme	cycle	195:199	arg1	control					201:207	cell cycle control	190:207	cell cycle control	190:207	Over the past decades, protein O-GlcNAcylation has been found to play a fundamental role in cell cycle control, metabolism, transcriptional regulation, and cellular signaling.
27114449	5	78	theme	phenylboronic	824:836	arg1	extraction					855:864	phenylboronic acid solid-phase extraction	824:864	phenylboronic acid solid-phase extraction	824:864	First, an efficient enrichment method for O-GlcNAc peptides was developed with the use of phenylboronic acid solid-phase extraction and anhydrous DMSO.
27114449	12	79	from	information	1937:1947	arg1	significance					1956:1967	the significance	1952:1967	the significance of O-GlcNAcylation	1952:1986	We believe this methodology can be broadly applied to reveal turnovers/dynamics of protein O-GlcNAcylation from different biological states and will provide more information on the significance of O-GlcNAcylation, enabling us to study the temporal dynamics of this critical modification for the first time.
27114449	0	80	theme	Mass	21:24	arg1	Platform					39:46	A Novel Quantitative Mass Spectrometry Platform	0:46	A Novel Quantitative Mass Spectrometry Platform for Determining Protein O-GlcNAcylation Dynamics.	0:96	A Novel Quantitative Mass Spectrometry Platform for Determining Protein O-GlcNAcylation Dynamics.
27114449	1	81	theme	past	107:110	arg1	decades					112:118	the past decades	103:118	the past decades	103:118	Over the past decades, protein O-GlcNAcylation has been found to play a fundamental role in cell cycle control, metabolism, transcriptional regulation, and cellular signaling.
27114449	6	82	theme	stoichiometry	895:907	arg1	reaction					909:916	The near stoichiometry reaction	886:916	The near stoichiometry reaction between the diol of GlcNAc and boronic acid	886:960	The near stoichiometry reaction between the diol of GlcNAc and boronic acid dramatically improved the enrichment efficiency.
27114449	12	83	from	states	1908:1913	arg1	turnovers/dynamics					1836:1853	turnovers/dynamics	1836:1853	turnovers/dynamics of protein O-GlcNAcylation from different biological states	1836:1913	We believe this methodology can be broadly applied to reveal turnovers/dynamics of protein O-GlcNAcylation from different biological states and will provide more information on the significance of O-GlcNAcylation, enabling us to study the temporal dynamics of this critical modification for the first time.
27114449	9	84	theme	O-GlcNAc	1430:1437	arg1	peptides					1439:1446	105 O-GlcNAc peptides	1426:1446	105 O-GlcNAc peptides on 42 proteins	1426:1461	Concentrating only on nuclear localized GlcNAc modified proteins, we are able to identify 105 O-GlcNAc peptides on 42 proteins and determine turnover rates of 20 O-GlcNAc peptides from 14 proteins extracted from HeLa nuclei.
27114449	9	85	from	peptides	1439:1446	arg1	proteins					1454:1461	42 proteins	1451:1461	42 proteins	1451:1461	Concentrating only on nuclear localized GlcNAc modified proteins, we are able to identify 105 O-GlcNAc peptides on 42 proteins and determine turnover rates of 20 O-GlcNAc peptides from 14 proteins extracted from HeLa nuclei.
27114449	12	86	theme	biological	1897:1906	arg1	states					1908:1913	different biological states	1887:1913	different biological states	1887:1913	We believe this methodology can be broadly applied to reveal turnovers/dynamics of protein O-GlcNAcylation from different biological states and will provide more information on the significance of O-GlcNAcylation, enabling us to study the temporal dynamics of this critical modification for the first time.
27114449	4	87	theme	metabolic	596:604	arg1	labeling					606:613	This metabolic labeling	591:613	This metabolic labeling	591:613	This metabolic labeling was combined with quantitative mass spectrometry-based proteomics to determine protein O-GlcNAcylation turnover rates.
27114449	3	88	theme	C-labeled	509:517	arg1	UDP-GlcNAc					519:528	(13)C-labeled UDP-GlcNAc	505:528	(13)C-labeled UDP-GlcNAc from (13)C6-glucose	505:548	Here, we have developed an approach to isotopically label O-GlcNAc modifications on proteins by producing (13)C-labeled UDP-GlcNAc from (13)C6-glucose via the hexosamine biosynthetic pathway.
27114449	10	89	theme	turnover	1598:1605	arg1	rates					1607:1611	O-GlcNAcylation turnover rates	1582:1611	O-GlcNAcylation turnover rates are slower than those published for phosphorylation or acetylation	1582:1678	In general, we found O-GlcNAcylation turnover rates are slower than those published for phosphorylation or acetylation.
27114449	0	90	theme	Novel	2:6	arg1	Platform					39:46	A Novel Quantitative Mass Spectrometry Platform	0:46	A Novel Quantitative Mass Spectrometry Platform for Determining Protein O-GlcNAcylation Dynamics.	0:96	A Novel Quantitative Mass Spectrometry Platform for Determining Protein O-GlcNAcylation Dynamics.
10471296	4	0	theme	B	723:723	arg1	construct					741:749	a B domain deletion construct	721:749	a B domain deletion construct (rHFV des B)	721:762	To confirm the structural basis for factor Va(1) and factor Va(2), we mutated Asn-2181 to glutamine (N2181Q) and expressed this mutant using a B domain deletion construct (rHFV des B) in COS cells.
10471296	4	0	theme	B	723:723	arg1	B					761:761	rHFV des B	752:761	rHFV des B	752:761	To confirm the structural basis for factor Va(1) and factor Va(2), we mutated Asn-2181 to glutamine (N2181Q) and expressed this mutant using a B domain deletion construct (rHFV des B) in COS cells.
10471296	6	1	theme	functional	896:905	arg1	properties					907:916	The functional properties	892:916	The functional properties of purified N2181Q	892:935	The functional properties of purified N2181Q were similar to those of factor Va(2) in prothrombinase assays carried out in the presence of limiting concentrations of phosphatidylserine.
10471296	6	1	theme	functional	896:905	arg1	similar					942:948	similar	942:948	similar	942:948	The functional properties of purified N2181Q were similar to those of factor Va(2) in prothrombinase assays carried out in the presence of limiting concentrations of phosphatidylserine.
10471296	5	2	with	chain	825:829	arg1	mobility					836:843	mobility	836:843	mobility identical to that of factor Va(2) on SDS-PAGE	836:889	Thrombin activation of N2181Q released a light chain with mobility identical to that of factor Va(2) on SDS-PAGE.
10471296	3	3	theme	factor	438:443	arg1	domain					450:455	the factor V C2 domain	434:455	the factor V C2 domain	434:455	However, we found that the factor V C2 domain, which contains a single potential glycosylation site at Asn-2181, was partially glycosylated when expressed in COS cells.
10471296	9	4	gly	glycosylation	1430:1442	arg1	V					1454:1454	factor V	1447:1454	factor V	1447:1454	These results indicate that partial glycosylation of factor V at asparagine-2181 is the structural basis of the light chain doublet and that the presence of this oligosaccharide reduces the affinity of factor Va for biological membranes.
10471296	9	4	gly	glycosylation	1430:1442	arg2	asparagine-2181					1459:1473	asparagine-2181	1459:1473	asparagine-2181	1459:1473	These results indicate that partial glycosylation of factor V at asparagine-2181 is the structural basis of the light chain doublet and that the presence of this oligosaccharide reduces the affinity of factor Va for biological membranes.
10471296	9	4	gly	glycosylation	1430:1442	arg1	asparagine-2181					1459:1473	asparagine-2181	1459:1473	asparagine-2181	1459:1473	These results indicate that partial glycosylation of factor V at asparagine-2181 is the structural basis of the light chain doublet and that the presence of this oligosaccharide reduces the affinity of factor Va for biological membranes.
10471296	7	5	theme	heavy	1257:1261	arg1	chain					1263:1267	a fluorescein-labeled heavy chain	1235:1267	a fluorescein-labeled heavy chain	1235:1267	The binding of human factor Va(1) and factor Va(2) to 75:25 POPC/POPS vesicles was also investigated in equilibrium binding assays using proteins containing a fluorescein-labeled heavy chain.
10471296	4	6	theme	deletion	732:739	arg1	construct					741:749	a B domain deletion construct	721:749	a B domain deletion construct (rHFV des B)	721:762	To confirm the structural basis for factor Va(1) and factor Va(2), we mutated Asn-2181 to glutamine (N2181Q) and expressed this mutant using a B domain deletion construct (rHFV des B) in COS cells.
10471296	4	6	theme	deletion	732:739	arg1	B					761:761	rHFV des B	752:761	rHFV des B	752:761	To confirm the structural basis for factor Va(1) and factor Va(2), we mutated Asn-2181 to glutamine (N2181Q) and expressed this mutant using a B domain deletion construct (rHFV des B) in COS cells.
10471296	7	7	theme	binding	1194:1200	arg1	assays					1202:1207	equilibrium binding assays	1182:1207	equilibrium binding assays using proteins containing a fluorescein-labeled heavy chain	1182:1267	The binding of human factor Va(1) and factor Va(2) to 75:25 POPC/POPS vesicles was also investigated in equilibrium binding assays using proteins containing a fluorescein-labeled heavy chain.
10471296	6	8	theme	phosphatidylserine	1058:1075	arg1	concentrations					1040:1053	limiting concentrations	1031:1053	limiting concentrations of phosphatidylserine	1031:1075	The functional properties of purified N2181Q were similar to those of factor Va(2) in prothrombinase assays carried out in the presence of limiting concentrations of phosphatidylserine.
10471296	9	9	theme	partial	1422:1428	arg1	basis					1493:1497	the structural basis	1478:1497	the structural basis of the light chain doublet	1478:1524	These results indicate that partial glycosylation of factor V at asparagine-2181 is the structural basis of the light chain doublet and that the presence of this oligosaccharide reduces the affinity of factor Va for biological membranes.
10471296	9	9	theme	partial	1422:1428	arg1	glycosylation					1430:1442	partial glycosylation	1422:1442	partial glycosylation of factor V at asparagine-2181	1422:1473	These results indicate that partial glycosylation of factor V at asparagine-2181 is the structural basis of the light chain doublet and that the presence of this oligosaccharide reduces the affinity of factor Va for biological membranes.
10471296	6	10	theme	factor	962:967	arg1	2					972:972	2	972:972	2	972:972	The functional properties of purified N2181Q were similar to those of factor Va(2) in prothrombinase assays carried out in the presence of limiting concentrations of phosphatidylserine.
10471296	6	10	theme	factor	962:967	arg1	Va					969:970	factor Va	962:970	factor Va(2)	962:973	The functional properties of purified N2181Q were similar to those of factor Va(2) in prothrombinase assays carried out in the presence of limiting concentrations of phosphatidylserine.
10471296	3	11	theme	glycosylation	492:504	arg1	site					506:509	a single potential glycosylation site	473:509	a single potential glycosylation site at Asn-2181	473:521	However, we found that the factor V C2 domain, which contains a single potential glycosylation site at Asn-2181, was partially glycosylated when expressed in COS cells.
10471296	3	12	theme	single	475:480	arg1	site					506:509	a single potential glycosylation site	473:509	a single potential glycosylation site at Asn-2181	473:521	However, we found that the factor V C2 domain, which contains a single potential glycosylation site at Asn-2181, was partially glycosylated when expressed in COS cells.
10471296	4	13	theme	COS	767:769	arg1	cells					771:775	COS cells	767:775	COS cells	767:775	To confirm the structural basis for factor Va(1) and factor Va(2), we mutated Asn-2181 to glutamine (N2181Q) and expressed this mutant using a B domain deletion construct (rHFV des B) in COS cells.
10471296	7	14	theme	75:25	1132:1136	arg1	vesicles					1148:1155	75:25 POPC/POPS vesicles	1132:1155	75:25 POPC/POPS vesicles	1132:1155	The binding of human factor Va(1) and factor Va(2) to 75:25 POPC/POPS vesicles was also investigated in equilibrium binding assays using proteins containing a fluorescein-labeled heavy chain.
10471296	0	15	theme	complex	128:134	arg1	assembly					97:104	assembly	97:104	assembly of the prothrombinase complex	97:134	Partial glycosylation at asparagine-2181 of the second C-type domain of human factor V modulates assembly of the prothrombinase complex.
10471296	3	16	gly	glycosylation	492:504	arg2	site					506:509	a single potential glycosylation site	473:509	a single potential glycosylation site at Asn-2181	473:521	However, we found that the factor V C2 domain, which contains a single potential glycosylation site at Asn-2181, was partially glycosylated when expressed in COS cells.
10471296	3	16	gly	glycosylation	492:504	arg2	Asn-2181					514:521	Asn-2181	514:521	Asn-2181	514:521	However, we found that the factor V C2 domain, which contains a single potential glycosylation site at Asn-2181, was partially glycosylated when expressed in COS cells.
10471296	5	17	theme	factor	866:871	arg1	2					876:876	2	876:876	2	876:876	Thrombin activation of N2181Q released a light chain with mobility identical to that of factor Va(2) on SDS-PAGE.
10471296	5	17	theme	factor	866:871	arg1	Va					873:874	factor Va	866:874	factor Va(2) on SDS-PAGE	866:889	Thrombin activation of N2181Q released a light chain with mobility identical to that of factor Va(2) on SDS-PAGE.
10471296	4	18	theme	des	757:759	arg1	construct					741:749	a B domain deletion construct	721:749	a B domain deletion construct (rHFV des B)	721:762	To confirm the structural basis for factor Va(1) and factor Va(2), we mutated Asn-2181 to glutamine (N2181Q) and expressed this mutant using a B domain deletion construct (rHFV des B) in COS cells.
10471296	4	18	theme	des	757:759	arg1	B					761:761	rHFV des B	752:761	rHFV des B	752:761	To confirm the structural basis for factor Va(1) and factor Va(2), we mutated Asn-2181 to glutamine (N2181Q) and expressed this mutant using a B domain deletion construct (rHFV des B) in COS cells.
10471296	7	19	contain	containing	1224:1233	arg2	chain					1263:1267	a fluorescein-labeled heavy chain	1235:1267	a fluorescein-labeled heavy chain	1235:1267	The binding of human factor Va(1) and factor Va(2) to 75:25 POPC/POPS vesicles was also investigated in equilibrium binding assays using proteins containing a fluorescein-labeled heavy chain.
10471296	7	19	contain	containing	1224:1233	arg1	proteins					1215:1222	proteins	1215:1222	proteins containing a fluorescein-labeled heavy chain	1215:1267	The binding of human factor Va(1) and factor Va(2) to 75:25 POPC/POPS vesicles was also investigated in equilibrium binding assays using proteins containing a fluorescein-labeled heavy chain.
10471296	7	20	theme	factor	1116:1121	arg1	2					1126:1126	2	1126:1126	2	1126:1126	The binding of human factor Va(1) and factor Va(2) to 75:25 POPC/POPS vesicles was also investigated in equilibrium binding assays using proteins containing a fluorescein-labeled heavy chain.
10471296	7	20	theme	factor	1116:1121	arg1	Va					1123:1124	factor Va	1116:1124	factor Va(2)	1116:1127	The binding of human factor Va(1) and factor Va(2) to 75:25 POPC/POPS vesicles was also investigated in equilibrium binding assays using proteins containing a fluorescein-labeled heavy chain.
10471296	0	21	theme	domain	62:67	arg1	asparagine-2181					25:39	asparagine-2181	25:39	asparagine-2181 of the second C-type domain of human factor V	25:85	Partial glycosylation at asparagine-2181 of the second C-type domain of human factor V modulates assembly of the prothrombinase complex.
10471296	1	22	theme	chains	261:266	arg1	affinity					278:285	their affinity	272:285	their affinity for biological membranes	272:310	Thrombin-activated factor Va exists as two isoforms, factor Va(1) and factor Va(2), which differ in the size of their light chains and their affinity for biological membranes.
10471296	1	22	theme	chains	261:266	arg1	size					241:244	the size	237:244	the size of their light chains	237:266	Thrombin-activated factor Va exists as two isoforms, factor Va(1) and factor Va(2), which differ in the size of their light chains and their affinity for biological membranes.
10471296	1	23	theme	factor	156:161	arg1	Va					163:164	Thrombin-activated factor Va	137:164	Thrombin-activated factor Va	137:164	Thrombin-activated factor Va exists as two isoforms, factor Va(1) and factor Va(2), which differ in the size of their light chains and their affinity for biological membranes.
10471296	9	24	theme	structural	1482:1491	arg1	basis					1493:1497	the structural basis	1478:1497	the structural basis of the light chain doublet	1478:1524	These results indicate that partial glycosylation of factor V at asparagine-2181 is the structural basis of the light chain doublet and that the presence of this oligosaccharide reduces the affinity of factor Va for biological membranes.
10471296	9	24	theme	structural	1482:1491	arg1	glycosylation					1430:1442	partial glycosylation	1422:1442	partial glycosylation of factor V at asparagine-2181	1422:1473	These results indicate that partial glycosylation of factor V at asparagine-2181 is the structural basis of the light chain doublet and that the presence of this oligosaccharide reduces the affinity of factor Va for biological membranes.
10471296	4	25	theme	factor	616:621	arg1	1					626:626	1	626:626	1	626:626	To confirm the structural basis for factor Va(1) and factor Va(2), we mutated Asn-2181 to glutamine (N2181Q) and expressed this mutant using a B domain deletion construct (rHFV des B) in COS cells.
10471296	4	25	theme	factor	616:621	arg1	Va					623:624	factor Va	616:624	factor Va(1)	616:627	To confirm the structural basis for factor Va(1) and factor Va(2), we mutated Asn-2181 to glutamine (N2181Q) and expressed this mutant using a B domain deletion construct (rHFV des B) in COS cells.
10471296	0	26	theme	human	72:76	arg1	V					85:85	human factor V	72:85	human factor V	72:85	Partial glycosylation at asparagine-2181 of the second C-type domain of human factor V modulates assembly of the prothrombinase complex.
10471296	9	27	theme	chain	1512:1516	arg1	doublet					1518:1524	the light chain doublet	1502:1524	the light chain doublet	1502:1524	These results indicate that partial glycosylation of factor V at asparagine-2181 is the structural basis of the light chain doublet and that the presence of this oligosaccharide reduces the affinity of factor Va for biological membranes.
10471296	6	28	from	assays	993:998	arg1	properties					907:916	The functional properties	892:916	The functional properties of purified N2181Q	892:935	The functional properties of purified N2181Q were similar to those of factor Va(2) in prothrombinase assays carried out in the presence of limiting concentrations of phosphatidylserine.
10471296	6	28	from	assays	993:998	arg1	similar					942:948	similar	942:948	similar	942:948	The functional properties of purified N2181Q were similar to those of factor Va(2) in prothrombinase assays carried out in the presence of limiting concentrations of phosphatidylserine.
10471296	0	29	theme	V	85:85	arg1	domain					62:67	the second C-type domain	44:67	the second C-type domain of human factor V	44:85	Partial glycosylation at asparagine-2181 of the second C-type domain of human factor V modulates assembly of the prothrombinase complex.
10471296	0	29	theme	V	85:85	arg1	V					85:85	human factor V	72:85	human factor V	72:85	Partial glycosylation at asparagine-2181 of the second C-type domain of human factor V modulates assembly of the prothrombinase complex.
10471296	5	30	theme	N2181Q	801:806	arg1	activation					787:796	Thrombin activation	778:796	Thrombin activation of N2181Q	778:806	Thrombin activation of N2181Q released a light chain with mobility identical to that of factor Va(2) on SDS-PAGE.
10471296	8	31	theme	factor	1292:1297	arg1	Va					1299:1300	human factor Va	1286:1300	human factor Va(2)	1286:1303	The affinity of human factor Va(2) binding to POPC/POPS vesicles was approximately 3-fold higher than that of factor Va(1).
10471296	8	31	theme	factor	1292:1297	arg1	2					1302:1302	2	1302:1302	2	1302:1302	The affinity of human factor Va(2) binding to POPC/POPS vesicles was approximately 3-fold higher than that of factor Va(1).
10471296	2	32	theme	Va	390:391	arg1	incubation					369:378	incubation	369:378	incubation of factor Va with N-glycanase	369:408	The heterogeneity of the light chain remained following incubation of factor Va with N-glycanase.
10471296	4	33	theme	factor	633:638	arg1	Va					640:641	factor Va	633:641	factor Va(2)	633:644	To confirm the structural basis for factor Va(1) and factor Va(2), we mutated Asn-2181 to glutamine (N2181Q) and expressed this mutant using a B domain deletion construct (rHFV des B) in COS cells.
10471296	4	33	theme	factor	633:638	arg1	2					643:643	2	643:643	2	643:643	To confirm the structural basis for factor Va(1) and factor Va(2), we mutated Asn-2181 to glutamine (N2181Q) and expressed this mutant using a B domain deletion construct (rHFV des B) in COS cells.
10471296	0	34	theme	Partial	0:6	arg1	glycosylation					8:20	Partial glycosylation	0:20	Partial glycosylation at asparagine-2181 of the second C-type domain of human factor V	0:85	Partial glycosylation at asparagine-2181 of the second C-type domain of human factor V modulates assembly of the prothrombinase complex.
10471296	6	35	theme	prothrombinase	978:991	arg1	assays					993:998	prothrombinase assays	978:998	prothrombinase assays carried out in the presence of limiting concentrations of phosphatidylserine	978:1075	The functional properties of purified N2181Q were similar to those of factor Va(2) in prothrombinase assays carried out in the presence of limiting concentrations of phosphatidylserine.
10471296	7	36	theme	Va	1106:1107	arg1	binding					1082:1088	The binding	1078:1088	The binding of human factor Va(1) and factor Va(2) to 75:25 POPC/POPS vesicles	1078:1155	The binding of human factor Va(1) and factor Va(2) to 75:25 POPC/POPS vesicles was also investigated in equilibrium binding assays using proteins containing a fluorescein-labeled heavy chain.
10471296	9	37	theme	oligosaccharide	1556:1570	arg1	presence					1539:1546	the presence	1535:1546	the presence of this oligosaccharide	1535:1570	These results indicate that partial glycosylation of factor V at asparagine-2181 is the structural basis of the light chain doublet and that the presence of this oligosaccharide reduces the affinity of factor Va for biological membranes.
10471296	2	38	theme	chain	344:348	arg1	heterogeneity					317:329	The heterogeneity	313:329	The heterogeneity of the light chain	313:348	The heterogeneity of the light chain remained following incubation of factor Va with N-glycanase.
10471296	0	39	gly	glycosylation	8:20	arg1	asparagine-2181					25:39	asparagine-2181	25:39	asparagine-2181 of the second C-type domain of human factor V	25:85	Partial glycosylation at asparagine-2181 of the second C-type domain of human factor V modulates assembly of the prothrombinase complex.
10471296	0	39	gly	glycosylation	8:20	arg2	asparagine-2181					25:39	asparagine-2181	25:39	asparagine-2181 of the second C-type domain of human factor V	25:85	Partial glycosylation at asparagine-2181 of the second C-type domain of human factor V modulates assembly of the prothrombinase complex.
10471296	7	40	theme	human	1093:1097	arg1	1					1109:1109	1	1109:1109	1	1109:1109	The binding of human factor Va(1) and factor Va(2) to 75:25 POPC/POPS vesicles was also investigated in equilibrium binding assays using proteins containing a fluorescein-labeled heavy chain.
10471296	7	40	theme	human	1093:1097	arg1	Va					1106:1107	human factor Va	1093:1107	human factor Va(1)	1093:1110	The binding of human factor Va(1) and factor Va(2) to 75:25 POPC/POPS vesicles was also investigated in equilibrium binding assays using proteins containing a fluorescein-labeled heavy chain.
10471296	0	41	theme	second	48:53	arg1	domain					62:67	the second C-type domain	44:67	the second C-type domain of human factor V	44:85	Partial glycosylation at asparagine-2181 of the second C-type domain of human factor V modulates assembly of the prothrombinase complex.
10471296	0	41	theme	second	48:53	arg1	V					85:85	human factor V	72:85	human factor V	72:85	Partial glycosylation at asparagine-2181 of the second C-type domain of human factor V modulates assembly of the prothrombinase complex.
10471296	6	42	theme	purified	921:928	arg1	N2181Q					930:935	purified N2181Q	921:935	purified N2181Q	921:935	The functional properties of purified N2181Q were similar to those of factor Va(2) in prothrombinase assays carried out in the presence of limiting concentrations of phosphatidylserine.
10471296	9	43	theme	Va	1603:1604	arg1	affinity					1584:1591	the affinity	1580:1591	the affinity of factor Va for biological membranes	1580:1629	These results indicate that partial glycosylation of factor V at asparagine-2181 is the structural basis of the light chain doublet and that the presence of this oligosaccharide reduces the affinity of factor Va for biological membranes.
10471296	3	44	theme	V	445:445	arg1	domain					450:455	the factor V C2 domain	434:455	the factor V C2 domain	434:455	However, we found that the factor V C2 domain, which contains a single potential glycosylation site at Asn-2181, was partially glycosylated when expressed in COS cells.
10471296	1	45	theme	factor	207:212	arg1	isoforms					180:187	two isoforms	176:187	two isoforms	176:187	Thrombin-activated factor Va exists as two isoforms, factor Va(1) and factor Va(2), which differ in the size of their light chains and their affinity for biological membranes.
10471296	1	45	theme	factor	207:212	arg1	2					217:217	2	217:217	2	217:217	Thrombin-activated factor Va exists as two isoforms, factor Va(1) and factor Va(2), which differ in the size of their light chains and their affinity for biological membranes.
10471296	1	45	theme	factor	207:212	arg1	Va					214:215	factor Va	207:215	factor Va(2)	207:218	Thrombin-activated factor Va exists as two isoforms, factor Va(1) and factor Va(2), which differ in the size of their light chains and their affinity for biological membranes.
10471296	9	46	theme	biological	1610:1619	arg1	membranes					1621:1629	biological membranes	1610:1629	biological membranes	1610:1629	These results indicate that partial glycosylation of factor V at asparagine-2181 is the structural basis of the light chain doublet and that the presence of this oligosaccharide reduces the affinity of factor Va for biological membranes.
10471296	6	47	dep	concentrations	1040:1053	arg1	the					1015:1017	the	1015:1017	the	1015:1017	The functional properties of purified N2181Q were similar to those of factor Va(2) in prothrombinase assays carried out in the presence of limiting concentrations of phosphatidylserine.
10471296	6	47	dep	concentrations	1040:1053	arg1	presence					1019:1026	presence	1019:1026	presence	1019:1026	The functional properties of purified N2181Q were similar to those of factor Va(2) in prothrombinase assays carried out in the presence of limiting concentrations of phosphatidylserine.
10471296	7	48	theme	fluorescein-labeled	1237:1255	arg1	chain					1263:1267	a fluorescein-labeled heavy chain	1235:1267	a fluorescein-labeled heavy chain	1235:1267	The binding of human factor Va(1) and factor Va(2) to 75:25 POPC/POPS vesicles was also investigated in equilibrium binding assays using proteins containing a fluorescein-labeled heavy chain.
10471296	8	49	theme	factor	1380:1385	arg1	Va					1387:1388	factor Va	1380:1388	factor Va	1380:1388	The affinity of human factor Va(2) binding to POPC/POPS vesicles was approximately 3-fold higher than that of factor Va(1).
10471296	4	50	theme	domain	725:730	arg1	construct					741:749	a B domain deletion construct	721:749	a B domain deletion construct (rHFV des B)	721:762	To confirm the structural basis for factor Va(1) and factor Va(2), we mutated Asn-2181 to glutamine (N2181Q) and expressed this mutant using a B domain deletion construct (rHFV des B) in COS cells.
10471296	4	50	theme	domain	725:730	arg1	B					761:761	rHFV des B	752:761	rHFV des B	752:761	To confirm the structural basis for factor Va(1) and factor Va(2), we mutated Asn-2181 to glutamine (N2181Q) and expressed this mutant using a B domain deletion construct (rHFV des B) in COS cells.
10471296	9	51	theme	V	1454:1454	arg1	basis					1493:1497	the structural basis	1478:1497	the structural basis of the light chain doublet	1478:1524	These results indicate that partial glycosylation of factor V at asparagine-2181 is the structural basis of the light chain doublet and that the presence of this oligosaccharide reduces the affinity of factor Va for biological membranes.
10471296	9	51	theme	V	1454:1454	arg1	glycosylation					1430:1442	partial glycosylation	1422:1442	partial glycosylation of factor V at asparagine-2181	1422:1473	These results indicate that partial glycosylation of factor V at asparagine-2181 is the structural basis of the light chain doublet and that the presence of this oligosaccharide reduces the affinity of factor Va for biological membranes.
10471296	7	52	theme	equilibrium	1182:1192	arg1	assays					1202:1207	equilibrium binding assays	1182:1207	equilibrium binding assays using proteins containing a fluorescein-labeled heavy chain	1182:1267	The binding of human factor Va(1) and factor Va(2) to 75:25 POPC/POPS vesicles was also investigated in equilibrium binding assays using proteins containing a fluorescein-labeled heavy chain.
10471296	3	53	gly	glycosylated	538:549	arg1	domain					450:455	the factor V C2 domain	434:455	the factor V C2 domain	434:455	However, we found that the factor V C2 domain, which contains a single potential glycosylation site at Asn-2181, was partially glycosylated when expressed in COS cells.
10471296	5	54	from	Va	873:874	arg1	SDS-PAGE					882:889	SDS-PAGE	882:889	SDS-PAGE	882:889	Thrombin activation of N2181Q released a light chain with mobility identical to that of factor Va(2) on SDS-PAGE.
10471296	6	55	theme	limiting	1031:1038	arg1	concentrations					1040:1053	limiting concentrations	1031:1053	limiting concentrations of phosphatidylserine	1031:1075	The functional properties of purified N2181Q were similar to those of factor Va(2) in prothrombinase assays carried out in the presence of limiting concentrations of phosphatidylserine.
10471296	3	56	theme	potential	482:490	arg1	site					506:509	a single potential glycosylation site	473:509	a single potential glycosylation site at Asn-2181	473:521	However, we found that the factor V C2 domain, which contains a single potential glycosylation site at Asn-2181, was partially glycosylated when expressed in COS cells.
10471296	0	57	theme	prothrombinase	113:126	arg1	complex					128:134	the prothrombinase complex	109:134	the prothrombinase complex	109:134	Partial glycosylation at asparagine-2181 of the second C-type domain of human factor V modulates assembly of the prothrombinase complex.
10471296	1	58	theme	factor	190:195	arg1	isoforms					180:187	two isoforms	176:187	two isoforms	176:187	Thrombin-activated factor Va exists as two isoforms, factor Va(1) and factor Va(2), which differ in the size of their light chains and their affinity for biological membranes.
10471296	1	58	theme	factor	190:195	arg1	Va					197:198	factor Va(1)	190:201	factor Va(1)	190:201	Thrombin-activated factor Va exists as two isoforms, factor Va(1) and factor Va(2), which differ in the size of their light chains and their affinity for biological membranes.
10471296	9	59	theme	factor	1447:1452	arg1	V					1454:1454	factor V	1447:1454	factor V	1447:1454	These results indicate that partial glycosylation of factor V at asparagine-2181 is the structural basis of the light chain doublet and that the presence of this oligosaccharide reduces the affinity of factor Va for biological membranes.
10471296	7	60	theme	POPC/POPS	1138:1146	arg1	vesicles					1148:1155	75:25 POPC/POPS vesicles	1132:1155	75:25 POPC/POPS vesicles	1132:1155	The binding of human factor Va(1) and factor Va(2) to 75:25 POPC/POPS vesicles was also investigated in equilibrium binding assays using proteins containing a fluorescein-labeled heavy chain.
10471296	2	61	with	incubation	369:378	arg1	N-glycanase					398:408	N-glycanase	398:408	N-glycanase	398:408	The heterogeneity of the light chain remained following incubation of factor Va with N-glycanase.
10471296	4	62	theme	rHFV	752:755	arg1	construct					741:749	a B domain deletion construct	721:749	a B domain deletion construct (rHFV des B)	721:762	To confirm the structural basis for factor Va(1) and factor Va(2), we mutated Asn-2181 to glutamine (N2181Q) and expressed this mutant using a B domain deletion construct (rHFV des B) in COS cells.
10471296	4	62	theme	rHFV	752:755	arg1	B					761:761	rHFV des B	752:761	rHFV des B	752:761	To confirm the structural basis for factor Va(1) and factor Va(2), we mutated Asn-2181 to glutamine (N2181Q) and expressed this mutant using a B domain deletion construct (rHFV des B) in COS cells.
10471296	1	63	theme	Thrombin-activated	137:154	arg1	Va					163:164	Thrombin-activated factor Va	137:164	Thrombin-activated factor Va	137:164	Thrombin-activated factor Va exists as two isoforms, factor Va(1) and factor Va(2), which differ in the size of their light chains and their affinity for biological membranes.
10471296	9	64	from	asparagine-2181	1459:1473	arg1	basis					1493:1497	the structural basis	1478:1497	the structural basis of the light chain doublet	1478:1524	These results indicate that partial glycosylation of factor V at asparagine-2181 is the structural basis of the light chain doublet and that the presence of this oligosaccharide reduces the affinity of factor Va for biological membranes.
10471296	9	64	from	asparagine-2181	1459:1473	arg1	glycosylation					1430:1442	partial glycosylation	1422:1442	partial glycosylation of factor V at asparagine-2181	1422:1473	These results indicate that partial glycosylation of factor V at asparagine-2181 is the structural basis of the light chain doublet and that the presence of this oligosaccharide reduces the affinity of factor Va for biological membranes.
10471296	0	65	from	asparagine-2181	25:39	arg1	glycosylation					8:20	Partial glycosylation	0:20	Partial glycosylation at asparagine-2181 of the second C-type domain of human factor V	0:85	Partial glycosylation at asparagine-2181 of the second C-type domain of human factor V modulates assembly of the prothrombinase complex.
10471296	7	66	theme	Va	1123:1124	arg1	binding					1082:1088	The binding	1078:1088	The binding of human factor Va(1) and factor Va(2) to 75:25 POPC/POPS vesicles	1078:1155	The binding of human factor Va(1) and factor Va(2) to 75:25 POPC/POPS vesicles was also investigated in equilibrium binding assays using proteins containing a fluorescein-labeled heavy chain.
10471296	4	67	theme	structural	595:604	arg1	basis					606:610	the structural basis	591:610	the structural basis for factor Va(1) and factor Va(2)	591:644	To confirm the structural basis for factor Va(1) and factor Va(2), we mutated Asn-2181 to glutamine (N2181Q) and expressed this mutant using a B domain deletion construct (rHFV des B) in COS cells.
10471296	0	68	theme	factor	78:83	arg1	V					85:85	human factor V	72:85	human factor V	72:85	Partial glycosylation at asparagine-2181 of the second C-type domain of human factor V modulates assembly of the prothrombinase complex.
10471296	9	69	theme	light	1506:1510	arg1	chain					1512:1516	the light chain	1502:1516	the light chain doublet	1502:1524	These results indicate that partial glycosylation of factor V at asparagine-2181 is the structural basis of the light chain doublet and that the presence of this oligosaccharide reduces the affinity of factor Va for biological membranes.
10471296	8	70	theme	human	1286:1290	arg1	Va					1299:1300	human factor Va	1286:1300	human factor Va(2)	1286:1303	The affinity of human factor Va(2) binding to POPC/POPS vesicles was approximately 3-fold higher than that of factor Va(1).
10471296	8	70	theme	human	1286:1290	arg1	2					1302:1302	2	1302:1302	2	1302:1302	The affinity of human factor Va(2) binding to POPC/POPS vesicles was approximately 3-fold higher than that of factor Va(1).
10471296	9	71	theme	doublet	1518:1524	arg1	basis					1493:1497	the structural basis	1478:1497	the structural basis of the light chain doublet	1478:1524	These results indicate that partial glycosylation of factor V at asparagine-2181 is the structural basis of the light chain doublet and that the presence of this oligosaccharide reduces the affinity of factor Va for biological membranes.
10471296	9	71	theme	doublet	1518:1524	arg1	glycosylation					1430:1442	partial glycosylation	1422:1442	partial glycosylation of factor V at asparagine-2181	1422:1473	These results indicate that partial glycosylation of factor V at asparagine-2181 is the structural basis of the light chain doublet and that the presence of this oligosaccharide reduces the affinity of factor Va for biological membranes.
10471296	8	72	theme	Va	1299:1300	arg1	higher					1360:1365	higher	1360:1365	higher	1360:1365	The affinity of human factor Va(2) binding to POPC/POPS vesicles was approximately 3-fold higher than that of factor Va(1).
10471296	8	72	theme	Va	1299:1300	arg1	affinity					1274:1281	The affinity	1270:1281	The affinity of human factor Va(2) binding to POPC/POPS vesicles	1270:1333	The affinity of human factor Va(2) binding to POPC/POPS vesicles was approximately 3-fold higher than that of factor Va(1).
10471296	1	73	theme	biological	291:300	arg1	membranes					302:310	biological membranes	291:310	biological membranes	291:310	Thrombin-activated factor Va exists as two isoforms, factor Va(1) and factor Va(2), which differ in the size of their light chains and their affinity for biological membranes.
10471296	8	74	dep	higher	1360:1365	arg1	1					1390:1390	1	1390:1390	1	1390:1390	The affinity of human factor Va(2) binding to POPC/POPS vesicles was approximately 3-fold higher than that of factor Va(1).
10471296	2	75	theme	factor	383:388	arg1	Va					390:391	factor Va	383:391	factor Va	383:391	The heterogeneity of the light chain remained following incubation of factor Va with N-glycanase.
10471296	2	76	gly	heterogeneity	317:329	arg1	chain					344:348	the light chain	334:348	the light chain	334:348	The heterogeneity of the light chain remained following incubation of factor Va with N-glycanase.
10471296	5	77	theme	Thrombin	778:785	arg1	activation					787:796	Thrombin activation	778:796	Thrombin activation of N2181Q	778:806	Thrombin activation of N2181Q released a light chain with mobility identical to that of factor Va(2) on SDS-PAGE.
10471296	7	78	theme	factor	1099:1104	arg1	1					1109:1109	1	1109:1109	1	1109:1109	The binding of human factor Va(1) and factor Va(2) to 75:25 POPC/POPS vesicles was also investigated in equilibrium binding assays using proteins containing a fluorescein-labeled heavy chain.
10471296	7	78	theme	factor	1099:1104	arg1	Va					1106:1107	human factor Va	1093:1107	human factor Va(1)	1093:1110	The binding of human factor Va(1) and factor Va(2) to 75:25 POPC/POPS vesicles was also investigated in equilibrium binding assays using proteins containing a fluorescein-labeled heavy chain.
10471296	8	79	theme	POPC/POPS	1316:1324	arg1	vesicles					1326:1333	POPC/POPS vesicles	1316:1333	POPC/POPS vesicles	1316:1333	The affinity of human factor Va(2) binding to POPC/POPS vesicles was approximately 3-fold higher than that of factor Va(1).
10471296	3	80	theme	COS	569:571	arg1	cells					573:577	COS cells	569:577	COS cells	569:577	However, we found that the factor V C2 domain, which contains a single potential glycosylation site at Asn-2181, was partially glycosylated when expressed in COS cells.
10471296	3	81	from	Asn-2181	514:521	arg1	site					506:509	a single potential glycosylation site	473:509	a single potential glycosylation site at Asn-2181	473:521	However, we found that the factor V C2 domain, which contains a single potential glycosylation site at Asn-2181, was partially glycosylated when expressed in COS cells.
10471296	5	82	theme	identical	845:853	arg1	mobility					836:843	mobility	836:843	mobility identical to that of factor Va(2) on SDS-PAGE	836:889	Thrombin activation of N2181Q released a light chain with mobility identical to that of factor Va(2) on SDS-PAGE.
10471296	2	83	theme	light	338:342	arg1	chain					344:348	the light chain	334:348	the light chain	334:348	The heterogeneity of the light chain remained following incubation of factor Va with N-glycanase.
10471296	0	84	theme	C-type	55:60	arg1	domain					62:67	the second C-type domain	44:67	the second C-type domain of human factor V	44:85	Partial glycosylation at asparagine-2181 of the second C-type domain of human factor V modulates assembly of the prothrombinase complex.
10471296	0	84	theme	C-type	55:60	arg1	V					85:85	human factor V	72:85	human factor V	72:85	Partial glycosylation at asparagine-2181 of the second C-type domain of human factor V modulates assembly of the prothrombinase complex.
10471296	3	85	contain	contains	464:471	arg2	site					506:509	a single potential glycosylation site	473:509	a single potential glycosylation site at Asn-2181	473:521	However, we found that the factor V C2 domain, which contains a single potential glycosylation site at Asn-2181, was partially glycosylated when expressed in COS cells.
10471296	3	85	contain	contains	464:471	arg1	domain					450:455	the factor V C2 domain	434:455	the factor V C2 domain	434:455	However, we found that the factor V C2 domain, which contains a single potential glycosylation site at Asn-2181, was partially glycosylated when expressed in COS cells.
10471296	6	86	from	similar	942:948	arg1	assays					993:998	prothrombinase assays	978:998	prothrombinase assays carried out in the presence of limiting concentrations of phosphatidylserine	978:1075	The functional properties of purified N2181Q were similar to those of factor Va(2) in prothrombinase assays carried out in the presence of limiting concentrations of phosphatidylserine.
10471296	1	87	theme	light	255:259	arg1	chains					261:266	their light chains	249:266	their light chains	249:266	Thrombin-activated factor Va exists as two isoforms, factor Va(1) and factor Va(2), which differ in the size of their light chains and their affinity for biological membranes.
10471296	5	88	theme	light	819:823	arg1	chain					825:829	a light chain	817:829	a light chain with mobility identical to that of factor Va(2) on SDS-PAGE	817:889	Thrombin activation of N2181Q released a light chain with mobility identical to that of factor Va(2) on SDS-PAGE.
10471296	6	89	theme	N2181Q	930:935	arg1	properties					907:916	The functional properties	892:916	The functional properties of purified N2181Q	892:935	The functional properties of purified N2181Q were similar to those of factor Va(2) in prothrombinase assays carried out in the presence of limiting concentrations of phosphatidylserine.
10471296	6	89	theme	N2181Q	930:935	arg1	similar					942:948	similar	942:948	similar	942:948	The functional properties of purified N2181Q were similar to those of factor Va(2) in prothrombinase assays carried out in the presence of limiting concentrations of phosphatidylserine.
10471296	9	90	theme	factor	1596:1601	arg1	Va					1603:1604	factor Va	1596:1604	factor Va	1596:1604	These results indicate that partial glycosylation of factor V at asparagine-2181 is the structural basis of the light chain doublet and that the presence of this oligosaccharide reduces the affinity of factor Va for biological membranes.
10471296	3	91	theme	C2	447:448	arg1	domain					450:455	the factor V C2 domain	434:455	the factor V C2 domain	434:455	However, we found that the factor V C2 domain, which contains a single potential glycosylation site at Asn-2181, was partially glycosylated when expressed in COS cells.
9295302	6	0	theme	PNGase	948:953	arg1	F					955:955	PNGase F	948:955	PNGase F	948:955	Limited proteolysis of MRP-enriched membranes and deglycosylation of intact MRP and its tryptic fragments with PNGase F was carried out followed by immunoblotting with antibodies known to react with specific regions of MRP.
9295302	6	1	theme	Limited	837:843	arg1	proteolysis					845:855	Limited proteolysis	837:855	Limited proteolysis of MRP-enriched membranes and deglycosylation of intact MRP	837:915	Limited proteolysis of MRP-enriched membranes and deglycosylation of intact MRP and its tryptic fragments with PNGase F was carried out followed by immunoblotting with antibodies known to react with specific regions of MRP.
9295302	2	2	theme	chemotherapeutic	352:367	arg1	agents					369:374	multiple chemotherapeutic agents	343:374	multiple chemotherapeutic agents	343:374	Multidrug resistance protein, MRP, is a 190-kDa integral membrane phosphoglycoprotein that belongs to the ATP-binding cassette superfamily of transport proteins and is capable of conferring resistance to multiple chemotherapeutic agents.
9295302	4	3	theme	sequence	622:629	arg1	alignments					631:640	multiple sequence alignments	613:640	multiple sequence alignments	613:640	Computer-assisted hydropathy analyses and multiple sequence alignments suggest several topological models for MRP.
9295302	2	4	theme	resistance	149:158	arg1	MRP					169:171	MRP	169:171	MRP	169:171	Multidrug resistance protein, MRP, is a 190-kDa integral membrane phosphoglycoprotein that belongs to the ATP-binding cassette superfamily of transport proteins and is capable of conferring resistance to multiple chemotherapeutic agents.
9295302	2	4	theme	resistance	149:158	arg1	protein					160:166	Multidrug resistance protein	139:166	Multidrug resistance protein	139:166	Multidrug resistance protein, MRP, is a 190-kDa integral membrane phosphoglycoprotein that belongs to the ATP-binding cassette superfamily of transport proteins and is capable of conferring resistance to multiple chemotherapeutic agents.
9295302	2	4	theme	resistance	149:158	arg1	capable					307:313	capable	307:313	capable	307:313	Multidrug resistance protein, MRP, is a 190-kDa integral membrane phosphoglycoprotein that belongs to the ATP-binding cassette superfamily of transport proteins and is capable of conferring resistance to multiple chemotherapeutic agents.
9295302	2	4	theme	resistance	149:158	arg1	phosphoglycoprotein					205:223	a 190-kDa integral membrane phosphoglycoprotein	177:223	a 190-kDa integral membrane phosphoglycoprotein that belongs to the ATP-binding cassette superfamily of transport proteins and is capable of conferring resistance to multiple chemotherapeutic agents	177:374	Multidrug resistance protein, MRP, is a 190-kDa integral membrane phosphoglycoprotein that belongs to the ATP-binding cassette superfamily of transport proteins and is capable of conferring resistance to multiple chemotherapeutic agents.
9295302	3	5	theme	NH2-terminal	553:564	arg1	MSD					566:568	an additional extremely hydrophobic NH2-terminal MSD	517:568	an additional extremely hydrophobic NH2-terminal MSD	517:568	Previous studies have indicated that MRP consists of two membrane spanning domains (MSD) each followed by a nucleotide binding domain, plus an additional extremely hydrophobic NH2-terminal MSD.
9295302	9	6	theme	first	1467:1471	arg1	evidence					1493:1500	the first direct experimental evidence that MRP has an extracytosolic NH2 terminus	1463:1544	the first direct experimental evidence that MRP has an extracytosolic NH2 terminus	1463:1544	N-Glycosylation of Asn19 and Asn23 provides the first direct experimental evidence that MRP has an extracytosolic NH2 terminus.
9295302	8	7	from	Asn19	1266:1270	arg1	MSD					1339:1341	the COOH-terminal MSD	1321:1341	the COOH-terminal MSD	1321:1341	Subsequent site-directed mutagenesis studies established that Asn19 and Asn23 in the NH2-terminal MSD and Asn1006 in the COOH-terminal MSD are the only sites in MRP that are modified with N-linked oligosaccharides.
9295302	8	7	from	Asn19	1266:1270	arg1	MSD					1302:1304	the NH2-terminal MSD	1285:1304	the NH2-terminal MSD	1285:1304	Subsequent site-directed mutagenesis studies established that Asn19 and Asn23 in the NH2-terminal MSD and Asn1006 in the COOH-terminal MSD are the only sites in MRP that are modified with N-linked oligosaccharides.
9295302	10	8	theme	MRP	1649:1651	arg1	MSD					1642:1644	the NH2-terminal MSD	1625:1644	the NH2-terminal MSD of MRP	1625:1651	This finding, together with those of previous studies, strongly suggests that the NH2-terminal MSD of MRP contains an odd number of transmembrane helices.
9295302	9	9	theme	experimental	1480:1491	arg1	evidence					1493:1500	the first direct experimental evidence that MRP has an extracytosolic NH2 terminus	1463:1544	the first direct experimental evidence that MRP has an extracytosolic NH2 terminus	1463:1544	N-Glycosylation of Asn19 and Asn23 provides the first direct experimental evidence that MRP has an extracytosolic NH2 terminus.
9295302	8	10	theme	site-directed	1215:1227	arg1	studies					1241:1247	Subsequent site-directed mutagenesis studies	1204:1247	Subsequent site-directed mutagenesis studies	1204:1247	Subsequent site-directed mutagenesis studies established that Asn19 and Asn23 in the NH2-terminal MSD and Asn1006 in the COOH-terminal MSD are the only sites in MRP that are modified with N-linked oligosaccharides.
9295302	6	11	theme	MRP	913:915	arg1	deglycosylation					887:901	deglycosylation	887:901	deglycosylation of intact MRP	887:915	Limited proteolysis of MRP-enriched membranes and deglycosylation of intact MRP and its tryptic fragments with PNGase F was carried out followed by immunoblotting with antibodies known to react with specific regions of MRP.
9295302	6	11	theme	MRP	913:915	arg1	membranes					873:881	MRP-enriched membranes	860:881	MRP-enriched membranes	860:881	Limited proteolysis of MRP-enriched membranes and deglycosylation of intact MRP and its tryptic fragments with PNGase F was carried out followed by immunoblotting with antibodies known to react with specific regions of MRP.
9295302	8	12	theme	NH2-terminal	1289:1300	arg1	MSD					1302:1304	the NH2-terminal MSD	1285:1304	the NH2-terminal MSD	1285:1304	Subsequent site-directed mutagenesis studies established that Asn19 and Asn23 in the NH2-terminal MSD and Asn1006 in the COOH-terminal MSD are the only sites in MRP that are modified with N-linked oligosaccharides.
9295302	9	13	theme	extracytosolic	1518:1531	arg1	terminus					1537:1544	an extracytosolic NH2 terminus	1515:1544	an extracytosolic NH2 terminus	1515:1544	N-Glycosylation of Asn19 and Asn23 provides the first direct experimental evidence that MRP has an extracytosolic NH2 terminus.
9295302	8	14	theme	COOH-terminal	1325:1337	arg1	MSD					1339:1341	the COOH-terminal MSD	1321:1341	the COOH-terminal MSD	1321:1341	Subsequent site-directed mutagenesis studies established that Asn19 and Asn23 in the NH2-terminal MSD and Asn1006 in the COOH-terminal MSD are the only sites in MRP that are modified with N-linked oligosaccharides.
9295302	2	15	gly	phosphoglycoprotein	205:223	arg1	protein					160:166	Multidrug resistance protein	139:166	Multidrug resistance protein	139:166	Multidrug resistance protein, MRP, is a 190-kDa integral membrane phosphoglycoprotein that belongs to the ATP-binding cassette superfamily of transport proteins and is capable of conferring resistance to multiple chemotherapeutic agents.
9295302	2	15	gly	phosphoglycoprotein	205:223	arg1	capable					307:313	capable	307:313	capable	307:313	Multidrug resistance protein, MRP, is a 190-kDa integral membrane phosphoglycoprotein that belongs to the ATP-binding cassette superfamily of transport proteins and is capable of conferring resistance to multiple chemotherapeutic agents.
9295302	2	15	gly	phosphoglycoprotein	205:223	arg1	phosphoglycoprotein					205:223	a 190-kDa integral membrane phosphoglycoprotein	177:223	a 190-kDa integral membrane phosphoglycoprotein that belongs to the ATP-binding cassette superfamily of transport proteins and is capable of conferring resistance to multiple chemotherapeutic agents	177:374	Multidrug resistance protein, MRP, is a 190-kDa integral membrane phosphoglycoprotein that belongs to the ATP-binding cassette superfamily of transport proteins and is capable of conferring resistance to multiple chemotherapeutic agents.
9295302	2	16	theme	membrane	196:203	arg1	protein					160:166	Multidrug resistance protein	139:166	Multidrug resistance protein	139:166	Multidrug resistance protein, MRP, is a 190-kDa integral membrane phosphoglycoprotein that belongs to the ATP-binding cassette superfamily of transport proteins and is capable of conferring resistance to multiple chemotherapeutic agents.
9295302	2	16	theme	membrane	196:203	arg1	capable					307:313	capable	307:313	capable	307:313	Multidrug resistance protein, MRP, is a 190-kDa integral membrane phosphoglycoprotein that belongs to the ATP-binding cassette superfamily of transport proteins and is capable of conferring resistance to multiple chemotherapeutic agents.
9295302	2	16	theme	membrane	196:203	arg1	phosphoglycoprotein					205:223	a 190-kDa integral membrane phosphoglycoprotein	177:223	a 190-kDa integral membrane phosphoglycoprotein that belongs to the ATP-binding cassette superfamily of transport proteins and is capable of conferring resistance to multiple chemotherapeutic agents	177:374	Multidrug resistance protein, MRP, is a 190-kDa integral membrane phosphoglycoprotein that belongs to the ATP-binding cassette superfamily of transport proteins and is capable of conferring resistance to multiple chemotherapeutic agents.
9295302	5	17	theme	likely	726:731	arg1	topology					712:719	the topology	708:719	the topology most likely to be correct	708:745	To aid in determining the topology most likely to be correct, we have identified which of the 14 N-glycosylation sequons in this protein are utilized.
9295302	2	18	theme	ATP-binding	245:255	arg1	superfamily					266:276	the ATP-binding cassette superfamily	241:276	the ATP-binding cassette superfamily of transport proteins	241:298	Multidrug resistance protein, MRP, is a 190-kDa integral membrane phosphoglycoprotein that belongs to the ATP-binding cassette superfamily of transport proteins and is capable of conferring resistance to multiple chemotherapeutic agents.
9295302	1	19	theme	NH2	125:127	arg1	terminus					129:136	an extracytosolic NH2 terminus	107:136	an extracytosolic NH2 terminus	107:136	A study of glycosylation-site mutants reveals an extracytosolic NH2 terminus.
9295302	8	20	theme	only	1351:1354	arg1	Asn1006					1310:1316	Asn1006	1310:1316	Asn1006 in the COOH-terminal MSD	1310:1341	Subsequent site-directed mutagenesis studies established that Asn19 and Asn23 in the NH2-terminal MSD and Asn1006 in the COOH-terminal MSD are the only sites in MRP that are modified with N-linked oligosaccharides.
9295302	8	20	theme	only	1351:1354	arg1	Asn19					1266:1270	Asn19	1266:1270	Asn19	1266:1270	Subsequent site-directed mutagenesis studies established that Asn19 and Asn23 in the NH2-terminal MSD and Asn1006 in the COOH-terminal MSD are the only sites in MRP that are modified with N-linked oligosaccharides.
9295302	8	20	theme	only	1351:1354	arg1	Asn23					1276:1280	Asn23	1276:1280	Asn23	1276:1280	Subsequent site-directed mutagenesis studies established that Asn19 and Asn23 in the NH2-terminal MSD and Asn1006 in the COOH-terminal MSD are the only sites in MRP that are modified with N-linked oligosaccharides.
9295302	8	20	theme	only	1351:1354	arg1	sites					1356:1360	the only sites	1347:1360	the only sites in MRP that are modified with N-linked oligosaccharides	1347:1416	Subsequent site-directed mutagenesis studies established that Asn19 and Asn23 in the NH2-terminal MSD and Asn1006 in the COOH-terminal MSD are the only sites in MRP that are modified with N-linked oligosaccharides.
9295302	3	21	theme	hydrophobic	541:551	arg1	MSD					566:568	an additional extremely hydrophobic NH2-terminal MSD	517:568	an additional extremely hydrophobic NH2-terminal MSD	517:568	Previous studies have indicated that MRP consists of two membrane spanning domains (MSD) each followed by a nucleotide binding domain, plus an additional extremely hydrophobic NH2-terminal MSD.
9295302	6	22	theme	specific	1036:1043	arg1	regions					1045:1051	specific regions	1036:1051	specific regions of MRP	1036:1058	Limited proteolysis of MRP-enriched membranes and deglycosylation of intact MRP and its tryptic fragments with PNGase F was carried out followed by immunoblotting with antibodies known to react with specific regions of MRP.
9295302	5	23	theme	N-glycosylation	783:797	arg1	sequons					799:805	the 14 N-glycosylation sequons	776:805	the 14 N-glycosylation sequons in this protein	776:821	To aid in determining the topology most likely to be correct, we have identified which of the 14 N-glycosylation sequons in this protein are utilized.
9295302	5	24	from	sequons	799:805	arg1	protein					815:821	this protein	810:821	this protein	810:821	To aid in determining the topology most likely to be correct, we have identified which of the 14 N-glycosylation sequons in this protein are utilized.
9295302	2	25	theme	transport	281:289	arg1	proteins					291:298	transport proteins	281:298	transport proteins	281:298	Multidrug resistance protein, MRP, is a 190-kDa integral membrane phosphoglycoprotein that belongs to the ATP-binding cassette superfamily of transport proteins and is capable of conferring resistance to multiple chemotherapeutic agents.
9295302	5	26	gly	N-glycosylation	783:797	arg2	sequons					799:805	the 14 N-glycosylation sequons	776:805	the 14 N-glycosylation sequons in this protein	776:821	To aid in determining the topology most likely to be correct, we have identified which of the 14 N-glycosylation sequons in this protein are utilized.
9295302	10	27	theme	helices	1693:1699	arg1	number					1669:1674	an odd number	1662:1674	an odd number of transmembrane helices	1662:1699	This finding, together with those of previous studies, strongly suggests that the NH2-terminal MSD of MRP contains an odd number of transmembrane helices.
9295302	7	28	from	sequon	1101:1106	arg1	MSD					1132:1134	the middle MSD	1121:1134	the middle MSD	1121:1134	The results obtained indicated that the sequon at Asn354 in the middle MSD is not utilized and suggested approximate sites of N-glycosylation.
9295302	9	29	contain	has	1511:1513	arg2	terminus					1537:1544	an extracytosolic NH2 terminus	1515:1544	an extracytosolic NH2 terminus	1515:1544	N-Glycosylation of Asn19 and Asn23 provides the first direct experimental evidence that MRP has an extracytosolic NH2 terminus.
9295302	9	29	contain	has	1511:1513	arg1	MRP					1507:1509	MRP	1507:1509	MRP	1507:1509	N-Glycosylation of Asn19 and Asn23 provides the first direct experimental evidence that MRP has an extracytosolic NH2 terminus.
9295302	8	30	theme	N-linked	1392:1399	arg1	oligosaccharides					1401:1416	N-linked oligosaccharides	1392:1416	N-linked oligosaccharides	1392:1416	Subsequent site-directed mutagenesis studies established that Asn19 and Asn23 in the NH2-terminal MSD and Asn1006 in the COOH-terminal MSD are the only sites in MRP that are modified with N-linked oligosaccharides.
9295302	3	31	theme	membrane	434:441	arg1	domains					452:458	two membrane spanning domains	430:458	two membrane spanning domains (MSD) each followed by a nucleotide binding domain, plus an additional extremely hydrophobic NH2-terminal MSD	430:568	Previous studies have indicated that MRP consists of two membrane spanning domains (MSD) each followed by a nucleotide binding domain, plus an additional extremely hydrophobic NH2-terminal MSD.
9295302	3	31	theme	membrane	434:441	arg1	MSD					461:463	MSD	461:463	MSD	461:463	Previous studies have indicated that MRP consists of two membrane spanning domains (MSD) each followed by a nucleotide binding domain, plus an additional extremely hydrophobic NH2-terminal MSD.
9295302	0	32	theme	Membrane	0:7	arg1	topology					9:16	Membrane topology	0:16	Membrane topology of the multidrug resistance protein (MRP).	0:59	Membrane topology of the multidrug resistance protein (MRP).
9295302	7	33	from	Asn354	1111:1116	arg1	sequon					1101:1106	the sequon	1097:1106	the sequon at Asn354 in the middle MSD	1097:1134	The results obtained indicated that the sequon at Asn354 in the middle MSD is not utilized and suggested approximate sites of N-glycosylation.
9295302	11	34	with	interaction	1785:1795	arg1	MRP					1811:1813	MRP	1811:1813	MRP	1811:1813	These results may have important implications for the further understanding of the interaction of drugs with MRP.
9295302	6	35	theme	intact	906:911	arg1	MRP					913:915	intact MRP	906:915	intact MRP	906:915	Limited proteolysis of MRP-enriched membranes and deglycosylation of intact MRP and its tryptic fragments with PNGase F was carried out followed by immunoblotting with antibodies known to react with specific regions of MRP.
9295302	1	36	theme	mutants	91:97	arg1	study					63:67	A study	61:67	A study of glycosylation-site mutants	61:97	A study of glycosylation-site mutants reveals an extracytosolic NH2 terminus.
9295302	6	37	with	proteolysis	845:855	arg1	F					955:955	PNGase F	948:955	PNGase F	948:955	Limited proteolysis of MRP-enriched membranes and deglycosylation of intact MRP and its tryptic fragments with PNGase F was carried out followed by immunoblotting with antibodies known to react with specific regions of MRP.
9295302	4	38	theme	Computer-assisted	571:587	arg1	analyses					600:607	Computer-assisted hydropathy analyses	571:607	Computer-assisted hydropathy analyses	571:607	Computer-assisted hydropathy analyses and multiple sequence alignments suggest several topological models for MRP.
9295302	6	39	gly	deglycosylation	887:901	arg1	MRP					913:915	intact MRP	906:915	intact MRP	906:915	Limited proteolysis of MRP-enriched membranes and deglycosylation of intact MRP and its tryptic fragments with PNGase F was carried out followed by immunoblotting with antibodies known to react with specific regions of MRP.
9295302	0	40	theme	multidrug	25:33	arg1	MRP					55:57	MRP	55:57	MRP	55:57	Membrane topology of the multidrug resistance protein (MRP).
9295302	0	40	theme	multidrug	25:33	arg1	protein					46:52	multidrug resistance protein	25:52	the multidrug resistance protein (MRP)	21:58	Membrane topology of the multidrug resistance protein (MRP).
9295302	7	41	theme	approximate	1166:1176	arg1	N-glycosylation					1187:1201	N-glycosylation	1187:1201	N-glycosylation	1187:1201	The results obtained indicated that the sequon at Asn354 in the middle MSD is not utilized and suggested approximate sites of N-glycosylation.
9295302	7	41	theme	approximate	1166:1176	arg1	sites					1178:1182	approximate sites	1166:1182	approximate sites of N-glycosylation	1166:1201	The results obtained indicated that the sequon at Asn354 in the middle MSD is not utilized and suggested approximate sites of N-glycosylation.
9295302	6	42	theme	deglycosylation	887:901	arg1	proteolysis					845:855	Limited proteolysis	837:855	Limited proteolysis of MRP-enriched membranes and deglycosylation of intact MRP	837:915	Limited proteolysis of MRP-enriched membranes and deglycosylation of intact MRP and its tryptic fragments with PNGase F was carried out followed by immunoblotting with antibodies known to react with specific regions of MRP.
9295302	6	42	theme	deglycosylation	887:901	arg1	fragments					933:941	its tryptic fragments	921:941	its tryptic fragments with PNGase F	921:955	Limited proteolysis of MRP-enriched membranes and deglycosylation of intact MRP and its tryptic fragments with PNGase F was carried out followed by immunoblotting with antibodies known to react with specific regions of MRP.
9295302	11	43	theme	important	1725:1733	arg1	implications					1735:1746	important implications	1725:1746	important implications for the further understanding of the interaction of drugs with MRP	1725:1813	These results may have important implications for the further understanding of the interaction of drugs with MRP.
9295302	2	44	theme	multiple	343:350	arg1	agents					369:374	multiple chemotherapeutic agents	343:374	multiple chemotherapeutic agents	343:374	Multidrug resistance protein, MRP, is a 190-kDa integral membrane phosphoglycoprotein that belongs to the ATP-binding cassette superfamily of transport proteins and is capable of conferring resistance to multiple chemotherapeutic agents.
9295302	3	45	theme	nucleotide	485:494	arg1	domain					504:509	a nucleotide binding domain	483:509	a nucleotide binding domain	483:509	Previous studies have indicated that MRP consists of two membrane spanning domains (MSD) each followed by a nucleotide binding domain, plus an additional extremely hydrophobic NH2-terminal MSD.
9295302	0	46	theme	protein	46:52	arg1	topology					9:16	Membrane topology	0:16	Membrane topology of the multidrug resistance protein (MRP).	0:59	Membrane topology of the multidrug resistance protein (MRP).
9295302	7	47	used	utilized	1143:1150	arg2	sequon					1101:1106	the sequon	1097:1106	the sequon at Asn354 in the middle MSD	1097:1134	The results obtained indicated that the sequon at Asn354 in the middle MSD is not utilized and suggested approximate sites of N-glycosylation.
9295302	7	47	used	utilized	1143:1150	arg2	Asn354					1111:1116	Asn354	1111:1116	Asn354	1111:1116	The results obtained indicated that the sequon at Asn354 in the middle MSD is not utilized and suggested approximate sites of N-glycosylation.
9295302	6	48	theme	membranes	873:881	arg1	proteolysis					845:855	Limited proteolysis	837:855	Limited proteolysis of MRP-enriched membranes and deglycosylation of intact MRP	837:915	Limited proteolysis of MRP-enriched membranes and deglycosylation of intact MRP and its tryptic fragments with PNGase F was carried out followed by immunoblotting with antibodies known to react with specific regions of MRP.
9295302	6	48	theme	membranes	873:881	arg1	fragments					933:941	its tryptic fragments	921:941	its tryptic fragments with PNGase F	921:955	Limited proteolysis of MRP-enriched membranes and deglycosylation of intact MRP and its tryptic fragments with PNGase F was carried out followed by immunoblotting with antibodies known to react with specific regions of MRP.
9295302	6	49	with	fragments	933:941	arg1	F					955:955	PNGase F	948:955	PNGase F	948:955	Limited proteolysis of MRP-enriched membranes and deglycosylation of intact MRP and its tryptic fragments with PNGase F was carried out followed by immunoblotting with antibodies known to react with specific regions of MRP.
9295302	2	50	theme	190-kDa	179:185	arg1	protein					160:166	Multidrug resistance protein	139:166	Multidrug resistance protein	139:166	Multidrug resistance protein, MRP, is a 190-kDa integral membrane phosphoglycoprotein that belongs to the ATP-binding cassette superfamily of transport proteins and is capable of conferring resistance to multiple chemotherapeutic agents.
9295302	2	50	theme	190-kDa	179:185	arg1	capable					307:313	capable	307:313	capable	307:313	Multidrug resistance protein, MRP, is a 190-kDa integral membrane phosphoglycoprotein that belongs to the ATP-binding cassette superfamily of transport proteins and is capable of conferring resistance to multiple chemotherapeutic agents.
9295302	2	50	theme	190-kDa	179:185	arg1	phosphoglycoprotein					205:223	a 190-kDa integral membrane phosphoglycoprotein	177:223	a 190-kDa integral membrane phosphoglycoprotein that belongs to the ATP-binding cassette superfamily of transport proteins and is capable of conferring resistance to multiple chemotherapeutic agents	177:374	Multidrug resistance protein, MRP, is a 190-kDa integral membrane phosphoglycoprotein that belongs to the ATP-binding cassette superfamily of transport proteins and is capable of conferring resistance to multiple chemotherapeutic agents.
9295302	10	51	contain	contains	1653:1660	arg1	MSD					1642:1644	the NH2-terminal MSD	1625:1644	the NH2-terminal MSD of MRP	1625:1651	This finding, together with those of previous studies, strongly suggests that the NH2-terminal MSD of MRP contains an odd number of transmembrane helices.
9295302	10	51	contain	contains	1653:1660	arg2	number					1669:1674	an odd number	1662:1674	an odd number of transmembrane helices	1662:1699	This finding, together with those of previous studies, strongly suggests that the NH2-terminal MSD of MRP contains an odd number of transmembrane helices.
9295302	11	52	theme	further	1756:1762	arg1	understanding					1764:1776	the further understanding	1752:1776	the further understanding of the interaction of drugs with MRP	1752:1813	These results may have important implications for the further understanding of the interaction of drugs with MRP.
9295302	9	53	theme	Asn19	1438:1442	arg1	N-Glycosylation					1419:1433	N-Glycosylation	1419:1433	N-Glycosylation of Asn19 and Asn23	1419:1452	N-Glycosylation of Asn19 and Asn23 provides the first direct experimental evidence that MRP has an extracytosolic NH2 terminus.
9295302	4	54	theme	several	650:656	arg1	models					670:675	several topological models	650:675	several topological models for MRP	650:683	Computer-assisted hydropathy analyses and multiple sequence alignments suggest several topological models for MRP.
9295302	9	55	theme	Asn23	1448:1452	arg1	N-Glycosylation					1419:1433	N-Glycosylation	1419:1433	N-Glycosylation of Asn19 and Asn23	1419:1452	N-Glycosylation of Asn19 and Asn23 provides the first direct experimental evidence that MRP has an extracytosolic NH2 terminus.
9295302	7	56	theme	middle	1125:1130	arg1	MSD					1132:1134	the middle MSD	1121:1134	the middle MSD	1121:1134	The results obtained indicated that the sequon at Asn354 in the middle MSD is not utilized and suggested approximate sites of N-glycosylation.
9295302	2	57	theme	proteins	291:298	arg1	superfamily					266:276	the ATP-binding cassette superfamily	241:276	the ATP-binding cassette superfamily of transport proteins	241:298	Multidrug resistance protein, MRP, is a 190-kDa integral membrane phosphoglycoprotein that belongs to the ATP-binding cassette superfamily of transport proteins and is capable of conferring resistance to multiple chemotherapeutic agents.
9295302	6	58	theme	tryptic	925:931	arg1	fragments					933:941	its tryptic fragments	921:941	its tryptic fragments with PNGase F	921:955	Limited proteolysis of MRP-enriched membranes and deglycosylation of intact MRP and its tryptic fragments with PNGase F was carried out followed by immunoblotting with antibodies known to react with specific regions of MRP.
9295302	4	59	theme	multiple	613:620	arg1	alignments					631:640	multiple sequence alignments	613:640	multiple sequence alignments	613:640	Computer-assisted hydropathy analyses and multiple sequence alignments suggest several topological models for MRP.
9295302	2	60	theme	Multidrug	139:147	arg1	MRP					169:171	MRP	169:171	MRP	169:171	Multidrug resistance protein, MRP, is a 190-kDa integral membrane phosphoglycoprotein that belongs to the ATP-binding cassette superfamily of transport proteins and is capable of conferring resistance to multiple chemotherapeutic agents.
9295302	2	60	theme	Multidrug	139:147	arg1	protein					160:166	Multidrug resistance protein	139:166	Multidrug resistance protein	139:166	Multidrug resistance protein, MRP, is a 190-kDa integral membrane phosphoglycoprotein that belongs to the ATP-binding cassette superfamily of transport proteins and is capable of conferring resistance to multiple chemotherapeutic agents.
9295302	2	60	theme	Multidrug	139:147	arg1	capable					307:313	capable	307:313	capable	307:313	Multidrug resistance protein, MRP, is a 190-kDa integral membrane phosphoglycoprotein that belongs to the ATP-binding cassette superfamily of transport proteins and is capable of conferring resistance to multiple chemotherapeutic agents.
9295302	2	60	theme	Multidrug	139:147	arg1	phosphoglycoprotein					205:223	a 190-kDa integral membrane phosphoglycoprotein	177:223	a 190-kDa integral membrane phosphoglycoprotein that belongs to the ATP-binding cassette superfamily of transport proteins and is capable of conferring resistance to multiple chemotherapeutic agents	177:374	Multidrug resistance protein, MRP, is a 190-kDa integral membrane phosphoglycoprotein that belongs to the ATP-binding cassette superfamily of transport proteins and is capable of conferring resistance to multiple chemotherapeutic agents.
9295302	3	61	theme	additional	520:529	arg1	MSD					566:568	an additional extremely hydrophobic NH2-terminal MSD	517:568	an additional extremely hydrophobic NH2-terminal MSD	517:568	Previous studies have indicated that MRP consists of two membrane spanning domains (MSD) each followed by a nucleotide binding domain, plus an additional extremely hydrophobic NH2-terminal MSD.
9295302	9	62	theme	direct	1473:1478	arg1	evidence					1493:1500	the first direct experimental evidence that MRP has an extracytosolic NH2 terminus	1463:1544	the first direct experimental evidence that MRP has an extracytosolic NH2 terminus	1463:1544	N-Glycosylation of Asn19 and Asn23 provides the first direct experimental evidence that MRP has an extracytosolic NH2 terminus.
9295302	8	63	theme	Subsequent	1204:1213	arg1	studies					1241:1247	Subsequent site-directed mutagenesis studies	1204:1247	Subsequent site-directed mutagenesis studies	1204:1247	Subsequent site-directed mutagenesis studies established that Asn19 and Asn23 in the NH2-terminal MSD and Asn1006 in the COOH-terminal MSD are the only sites in MRP that are modified with N-linked oligosaccharides.
9295302	10	64	theme	NH2-terminal	1629:1640	arg1	MSD					1642:1644	the NH2-terminal MSD	1625:1644	the NH2-terminal MSD of MRP	1625:1651	This finding, together with those of previous studies, strongly suggests that the NH2-terminal MSD of MRP contains an odd number of transmembrane helices.
9295302	8	65	theme	mutagenesis	1229:1239	arg1	studies					1241:1247	Subsequent site-directed mutagenesis studies	1204:1247	Subsequent site-directed mutagenesis studies	1204:1247	Subsequent site-directed mutagenesis studies established that Asn19 and Asn23 in the NH2-terminal MSD and Asn1006 in the COOH-terminal MSD are the only sites in MRP that are modified with N-linked oligosaccharides.
9295302	6	66	dep	carried	961:967	arg1	followed					973:980	followed	973:980	followed by immunoblotting with antibodies known to react with specific regions of MRP	973:1058	Limited proteolysis of MRP-enriched membranes and deglycosylation of intact MRP and its tryptic fragments with PNGase F was carried out followed by immunoblotting with antibodies known to react with specific regions of MRP.
9295302	10	67	theme	odd	1665:1667	arg1	number					1669:1674	an odd number	1662:1674	an odd number of transmembrane helices	1662:1699	This finding, together with those of previous studies, strongly suggests that the NH2-terminal MSD of MRP contains an odd number of transmembrane helices.
9295302	9	68	theme	NH2	1533:1535	arg1	terminus					1537:1544	an extracytosolic NH2 terminus	1515:1544	an extracytosolic NH2 terminus	1515:1544	N-Glycosylation of Asn19 and Asn23 provides the first direct experimental evidence that MRP has an extracytosolic NH2 terminus.
9295302	8	69	link	N-linked	1392:1399	arg1	oligosaccharides					1401:1416	N-linked oligosaccharides	1392:1416	N-linked oligosaccharides	1392:1416	Subsequent site-directed mutagenesis studies established that Asn19 and Asn23 in the NH2-terminal MSD and Asn1006 in the COOH-terminal MSD are the only sites in MRP that are modified with N-linked oligosaccharides.
9295302	2	70	theme	cassette	257:264	arg1	superfamily					266:276	the ATP-binding cassette superfamily	241:276	the ATP-binding cassette superfamily of transport proteins	241:298	Multidrug resistance protein, MRP, is a 190-kDa integral membrane phosphoglycoprotein that belongs to the ATP-binding cassette superfamily of transport proteins and is capable of conferring resistance to multiple chemotherapeutic agents.
9295302	8	71	from	Asn23	1276:1280	arg1	MSD					1339:1341	the COOH-terminal MSD	1321:1341	the COOH-terminal MSD	1321:1341	Subsequent site-directed mutagenesis studies established that Asn19 and Asn23 in the NH2-terminal MSD and Asn1006 in the COOH-terminal MSD are the only sites in MRP that are modified with N-linked oligosaccharides.
9295302	8	71	from	Asn23	1276:1280	arg1	MSD					1302:1304	the NH2-terminal MSD	1285:1304	the NH2-terminal MSD	1285:1304	Subsequent site-directed mutagenesis studies established that Asn19 and Asn23 in the NH2-terminal MSD and Asn1006 in the COOH-terminal MSD are the only sites in MRP that are modified with N-linked oligosaccharides.
9295302	1	72	theme	extracytosolic	110:123	arg1	terminus					129:136	an extracytosolic NH2 terminus	107:136	an extracytosolic NH2 terminus	107:136	A study of glycosylation-site mutants reveals an extracytosolic NH2 terminus.
9295302	6	73	theme	MRP	1056:1058	arg1	regions					1045:1051	specific regions	1036:1051	specific regions of MRP	1036:1058	Limited proteolysis of MRP-enriched membranes and deglycosylation of intact MRP and its tryptic fragments with PNGase F was carried out followed by immunoblotting with antibodies known to react with specific regions of MRP.
9295302	8	74	mod	modified	1378:1385	arg1	Asn1006					1310:1316	Asn1006	1310:1316	Asn1006 in the COOH-terminal MSD	1310:1341	Subsequent site-directed mutagenesis studies established that Asn19 and Asn23 in the NH2-terminal MSD and Asn1006 in the COOH-terminal MSD are the only sites in MRP that are modified with N-linked oligosaccharides.
9295302	8	74	mod	modified	1378:1385	arg1	Asn19					1266:1270	Asn19	1266:1270	Asn19	1266:1270	Subsequent site-directed mutagenesis studies established that Asn19 and Asn23 in the NH2-terminal MSD and Asn1006 in the COOH-terminal MSD are the only sites in MRP that are modified with N-linked oligosaccharides.
9295302	8	74	mod	modified	1378:1385	arg1	Asn23					1276:1280	Asn23	1276:1280	Asn23	1276:1280	Subsequent site-directed mutagenesis studies established that Asn19 and Asn23 in the NH2-terminal MSD and Asn1006 in the COOH-terminal MSD are the only sites in MRP that are modified with N-linked oligosaccharides.
9295302	8	74	mod	modified	1378:1385	arg1	sites					1356:1360	the only sites	1347:1360	the only sites in MRP that are modified with N-linked oligosaccharides	1347:1416	Subsequent site-directed mutagenesis studies established that Asn19 and Asn23 in the NH2-terminal MSD and Asn1006 in the COOH-terminal MSD are the only sites in MRP that are modified with N-linked oligosaccharides.
9295302	8	74	mod	modified	1378:1385	arg3	oligosaccharides					1401:1416	N-linked oligosaccharides	1392:1416	N-linked oligosaccharides	1392:1416	Subsequent site-directed mutagenesis studies established that Asn19 and Asn23 in the NH2-terminal MSD and Asn1006 in the COOH-terminal MSD are the only sites in MRP that are modified with N-linked oligosaccharides.
9295302	11	75	theme	drugs	1800:1804	arg1	interaction					1785:1795	the interaction	1781:1795	the interaction of drugs with MRP	1781:1813	These results may have important implications for the further understanding of the interaction of drugs with MRP.
9295302	8	76	from	Asn1006	1310:1316	arg1	MSD					1339:1341	the COOH-terminal MSD	1321:1341	the COOH-terminal MSD	1321:1341	Subsequent site-directed mutagenesis studies established that Asn19 and Asn23 in the NH2-terminal MSD and Asn1006 in the COOH-terminal MSD are the only sites in MRP that are modified with N-linked oligosaccharides.
9295302	8	76	from	Asn1006	1310:1316	arg1	MSD					1302:1304	the NH2-terminal MSD	1285:1304	the NH2-terminal MSD	1285:1304	Subsequent site-directed mutagenesis studies established that Asn19 and Asn23 in the NH2-terminal MSD and Asn1006 in the COOH-terminal MSD are the only sites in MRP that are modified with N-linked oligosaccharides.
9295302	11	77	theme	interaction	1785:1795	arg1	understanding					1764:1776	the further understanding	1752:1776	the further understanding of the interaction of drugs with MRP	1752:1813	These results may have important implications for the further understanding of the interaction of drugs with MRP.
9295302	11	78	contain	have	1720:1723	arg1	results					1708:1714	These results	1702:1714	These results	1702:1714	These results may have important implications for the further understanding of the interaction of drugs with MRP.
9295302	11	78	contain	have	1720:1723	arg2	implications					1735:1746	important implications	1725:1746	important implications for the further understanding of the interaction of drugs with MRP	1725:1813	These results may have important implications for the further understanding of the interaction of drugs with MRP.
9295302	3	79	theme	Previous	377:384	arg1	studies					386:392	Previous studies	377:392	Previous studies	377:392	Previous studies have indicated that MRP consists of two membrane spanning domains (MSD) each followed by a nucleotide binding domain, plus an additional extremely hydrophobic NH2-terminal MSD.
9295302	10	80	theme	transmembrane	1679:1691	arg1	helices					1693:1699	transmembrane helices	1679:1699	transmembrane helices	1679:1699	This finding, together with those of previous studies, strongly suggests that the NH2-terminal MSD of MRP contains an odd number of transmembrane helices.
9295302	7	81	theme	N-glycosylation	1187:1201	arg1	N-glycosylation					1187:1201	N-glycosylation	1187:1201	N-glycosylation	1187:1201	The results obtained indicated that the sequon at Asn354 in the middle MSD is not utilized and suggested approximate sites of N-glycosylation.
9295302	7	81	theme	N-glycosylation	1187:1201	arg1	sites					1178:1182	approximate sites	1166:1182	approximate sites of N-glycosylation	1166:1201	The results obtained indicated that the sequon at Asn354 in the middle MSD is not utilized and suggested approximate sites of N-glycosylation.
9295302	8	82	from	sites	1356:1360	arg1	MRP					1365:1367	MRP	1365:1367	MRP	1365:1367	Subsequent site-directed mutagenesis studies established that Asn19 and Asn23 in the NH2-terminal MSD and Asn1006 in the COOH-terminal MSD are the only sites in MRP that are modified with N-linked oligosaccharides.
9295302	3	83	theme	spanning	443:450	arg1	domains					452:458	two membrane spanning domains	430:458	two membrane spanning domains (MSD) each followed by a nucleotide binding domain, plus an additional extremely hydrophobic NH2-terminal MSD	430:568	Previous studies have indicated that MRP consists of two membrane spanning domains (MSD) each followed by a nucleotide binding domain, plus an additional extremely hydrophobic NH2-terminal MSD.
9295302	3	83	theme	spanning	443:450	arg1	MSD					461:463	MSD	461:463	MSD	461:463	Previous studies have indicated that MRP consists of two membrane spanning domains (MSD) each followed by a nucleotide binding domain, plus an additional extremely hydrophobic NH2-terminal MSD.
9295302	1	84	theme	glycosylation-site	72:89	arg1	mutants					91:97	glycosylation-site mutants	72:97	glycosylation-site mutants	72:97	A study of glycosylation-site mutants reveals an extracytosolic NH2 terminus.
9295302	4	85	theme	hydropathy	589:598	arg1	analyses					600:607	Computer-assisted hydropathy analyses	571:607	Computer-assisted hydropathy analyses	571:607	Computer-assisted hydropathy analyses and multiple sequence alignments suggest several topological models for MRP.
9295302	0	86	theme	resistance	35:44	arg1	MRP					55:57	MRP	55:57	MRP	55:57	Membrane topology of the multidrug resistance protein (MRP).
9295302	0	86	theme	resistance	35:44	arg1	protein					46:52	multidrug resistance protein	25:52	the multidrug resistance protein (MRP)	21:58	Membrane topology of the multidrug resistance protein (MRP).
9295302	9	87	gly	N-Glycosylation	1419:1433	arg1	Asn19					1438:1442	Asn19	1438:1442	Asn19	1438:1442	N-Glycosylation of Asn19 and Asn23 provides the first direct experimental evidence that MRP has an extracytosolic NH2 terminus.
9295302	9	87	gly	N-Glycosylation	1419:1433	arg1	Asn23					1448:1452	Asn23	1448:1452	Asn23	1448:1452	N-Glycosylation of Asn19 and Asn23 provides the first direct experimental evidence that MRP has an extracytosolic NH2 terminus.
9295302	3	88	dep	domains	452:458	arg1	each					466:469	each	466:469	each	466:469	Previous studies have indicated that MRP consists of two membrane spanning domains (MSD) each followed by a nucleotide binding domain, plus an additional extremely hydrophobic NH2-terminal MSD.
9295302	2	89	theme	integral	187:194	arg1	protein					160:166	Multidrug resistance protein	139:166	Multidrug resistance protein	139:166	Multidrug resistance protein, MRP, is a 190-kDa integral membrane phosphoglycoprotein that belongs to the ATP-binding cassette superfamily of transport proteins and is capable of conferring resistance to multiple chemotherapeutic agents.
9295302	2	89	theme	integral	187:194	arg1	capable					307:313	capable	307:313	capable	307:313	Multidrug resistance protein, MRP, is a 190-kDa integral membrane phosphoglycoprotein that belongs to the ATP-binding cassette superfamily of transport proteins and is capable of conferring resistance to multiple chemotherapeutic agents.
9295302	2	89	theme	integral	187:194	arg1	phosphoglycoprotein					205:223	a 190-kDa integral membrane phosphoglycoprotein	177:223	a 190-kDa integral membrane phosphoglycoprotein that belongs to the ATP-binding cassette superfamily of transport proteins and is capable of conferring resistance to multiple chemotherapeutic agents	177:374	Multidrug resistance protein, MRP, is a 190-kDa integral membrane phosphoglycoprotein that belongs to the ATP-binding cassette superfamily of transport proteins and is capable of conferring resistance to multiple chemotherapeutic agents.
9295302	3	90	theme	binding	496:502	arg1	domain					504:509	a nucleotide binding domain	483:509	a nucleotide binding domain	483:509	Previous studies have indicated that MRP consists of two membrane spanning domains (MSD) each followed by a nucleotide binding domain, plus an additional extremely hydrophobic NH2-terminal MSD.
9295302	5	91	used	utilized	827:834	arg2	which					767:771	which	767:771	which	767:771	To aid in determining the topology most likely to be correct, we have identified which of the 14 N-glycosylation sequons in this protein are utilized.
9295302	6	92	theme	MRP-enriched	860:871	arg1	membranes					873:881	MRP-enriched membranes	860:881	MRP-enriched membranes	860:881	Limited proteolysis of MRP-enriched membranes and deglycosylation of intact MRP and its tryptic fragments with PNGase F was carried out followed by immunoblotting with antibodies known to react with specific regions of MRP.
9295302	7	93	gly	N-glycosylation	1187:1201	arg2	N-glycosylation					1187:1201	N-glycosylation	1187:1201	N-glycosylation	1187:1201	The results obtained indicated that the sequon at Asn354 in the middle MSD is not utilized and suggested approximate sites of N-glycosylation.
9295302	7	93	gly	N-glycosylation	1187:1201	arg2	sites					1178:1182	approximate sites	1166:1182	approximate sites of N-glycosylation	1166:1201	The results obtained indicated that the sequon at Asn354 in the middle MSD is not utilized and suggested approximate sites of N-glycosylation.
9295302	4	94	theme	topological	658:668	arg1	models					670:675	several topological models	650:675	several topological models for MRP	650:683	Computer-assisted hydropathy analyses and multiple sequence alignments suggest several topological models for MRP.
9295302	10	95	theme	previous	1584:1591	arg1	studies					1593:1599	previous studies	1584:1599	previous studies	1584:1599	This finding, together with those of previous studies, strongly suggests that the NH2-terminal MSD of MRP contains an odd number of transmembrane helices.
19038967	6	0	theme	151-residue	1093:1103	arg1	prodomain					1114:1122	A large 151-residue C-shaped prodomain	1085:1122	A large 151-residue C-shaped prodomain	1085:1122	A large 151-residue C-shaped prodomain makes extensive contacts as it wraps around the surface of the catalytic domain with the two domains connected by a 24-residue flexible linker that passes through the substrate-binding groove.
19038967	2	1	theme	known	358:362	arg1	group					422:426	a group	420:426	a group characterized by a subtilisin-like fold, a Ser-Glu-Asp catalytic triad, and an acidic pH optimum	420:523	TPP1 represents the only known mammalian member of the S53 family of serine proteases, a group characterized by a subtilisin-like fold, a Ser-Glu-Asp catalytic triad, and an acidic pH optimum.
19038967	2	1	theme	known	358:362	arg1	member					374:379	the only known mammalian member	349:379	the only known mammalian member of the S53 family of serine proteases	349:417	TPP1 represents the only known mammalian member of the S53 family of serine proteases, a group characterized by a subtilisin-like fold, a Ser-Glu-Asp catalytic triad, and an acidic pH optimum.
19038967	7	2	theme	protease	1517:1524	arg1	activation					1499:1508	premature activation	1489:1508	premature activation of the protease	1489:1524	The proenzyme structure reveals suboptimal catalytic triad geometry with its propiece linker partially blocking the substrate-binding site, which together serve to prevent premature activation of the protease.
19038967	6	3	theme	catalytic	1187:1195	arg1	domain					1197:1202	the catalytic domain	1183:1202	the catalytic domain	1183:1202	A large 151-residue C-shaped prodomain makes extensive contacts as it wraps around the surface of the catalytic domain with the two domains connected by a 24-residue flexible linker that passes through the substrate-binding groove.
19038967	0	4	from	lipofuscinosis	147:160	arg1	deficient					112:120	deficient	112:120	deficient	112:120	Crystal structure and autoactivation pathway of the precursor form of human tripeptidyl-peptidase 1, the enzyme deficient in late infantile ceroid lipofuscinosis.
19038967	4	5	theme	Asn-linked	803:812	arg1	N-acetylglucosamines					814:833	four Asn-linked N-acetylglucosamines	798:833	four Asn-linked N-acetylglucosamines	798:833	In this study, we describe an endoglycosidase H-deglycosylated form of TPP1 containing four Asn-linked N-acetylglucosamines that is indistinguishable from fully glycosylated TPP1 in terms of autocatalytic processing of the proform and enzymatic properties of the mature protease.
19038967	1	6	theme	neuronal	178:185	arg1	lipofuscinosis					194:207	Late infantile neuronal ceroid lipofuscinosis	163:207	Late infantile neuronal ceroid lipofuscinosis	163:207	Late infantile neuronal ceroid lipofuscinosis is a fatal childhood neurological disorder caused by a deficiency in the lysosomal protease tripeptidyl-peptidase 1 (TPP1).
19038967	1	6	theme	neuronal	178:185	arg1	disorder					243:250	a fatal childhood neurological disorder	212:250	a fatal childhood neurological disorder caused by a deficiency in the lysosomal protease tripeptidyl-peptidase 1 (TPP1)	212:330	Late infantile neuronal ceroid lipofuscinosis is a fatal childhood neurological disorder caused by a deficiency in the lysosomal protease tripeptidyl-peptidase 1 (TPP1).
19038967	7	7	theme	premature	1489:1497	arg1	activation					1499:1508	premature activation	1489:1508	premature activation of the protease	1489:1524	The proenzyme structure reveals suboptimal catalytic triad geometry with its propiece linker partially blocking the substrate-binding site, which together serve to prevent premature activation of the protease.
19038967	9	8	theme	improved	1778:1785	arg1	variants					1792:1799	improved TPP1 variants	1778:1799	improved TPP1 variants	1778:1799	These data provide new insights into TPP1 function and represent a valuable resource for constructing improved TPP1 variants for treatment of late infantile neuronal ceroid lipofuscinosis.
19038967	6	9	theme	24-residue	1240:1249	arg1	linker					1260:1265	a 24-residue flexible linker	1238:1265	a 24-residue flexible linker that passes through the substrate-binding groove	1238:1314	A large 151-residue C-shaped prodomain makes extensive contacts as it wraps around the surface of the catalytic domain with the two domains connected by a 24-residue flexible linker that passes through the substrate-binding groove.
19038967	3	10	theme	inactive	552:559	arg1	pro-TPP1					572:579	pro-TPP1	572:579	pro-TPP1	572:579	TPP1 is synthesized as an inactive proenzyme (pro-TPP1) that is proteolytically processed into the active enzyme after exposure to low pH in vitro or targeting to the lysosome in vivo.
19038967	3	10	theme	inactive	552:559	arg1	TPP1					526:529	TPP1	526:529	TPP1	526:529	TPP1 is synthesized as an inactive proenzyme (pro-TPP1) that is proteolytically processed into the active enzyme after exposure to low pH in vitro or targeting to the lysosome in vivo.
19038967	3	10	theme	inactive	552:559	arg1	proenzyme					561:569	an inactive proenzyme	549:569	an inactive proenzyme (pro-TPP1) that is proteolytically processed into the active enzyme after exposure to low pH in vitro or targeting to the lysosome in vivo	549:708	TPP1 is synthesized as an inactive proenzyme (pro-TPP1) that is proteolytically processed into the active enzyme after exposure to low pH in vitro or targeting to the lysosome in vivo.
19038967	4	11	theme	autocatalytic	902:914	arg1	processing					916:925	autocatalytic processing	902:925	autocatalytic processing of the proform	902:940	In this study, we describe an endoglycosidase H-deglycosylated form of TPP1 containing four Asn-linked N-acetylglucosamines that is indistinguishable from fully glycosylated TPP1 in terms of autocatalytic processing of the proform and enzymatic properties of the mature protease.
19038967	0	12	theme	deficient	112:120	arg1	human					70:74	human tripeptidyl-peptidase 1	70:98	human tripeptidyl-peptidase 1	70:98	Crystal structure and autoactivation pathway of the precursor form of human tripeptidyl-peptidase 1, the enzyme deficient in late infantile ceroid lipofuscinosis.
19038967	0	12	theme	deficient	112:120	arg1	enzyme					105:110	the enzyme	101:110	the enzyme deficient in late infantile ceroid lipofuscinosis	101:160	Crystal structure and autoactivation pathway of the precursor form of human tripeptidyl-peptidase 1, the enzyme deficient in late infantile ceroid lipofuscinosis.
19038967	5	13	theme	angstroms	1063:1071	arg1	resolution					1073:1082	1.85 angstroms resolution	1058:1082	1.85 angstroms resolution	1058:1082	The crystal structure of deglycosylated pro-TPP1 was determined at 1.85 angstroms resolution.
19038967	0	14	theme	late	125:128	arg1	lipofuscinosis					147:160	late infantile ceroid lipofuscinosis	125:160	late infantile ceroid lipofuscinosis	125:160	Crystal structure and autoactivation pathway of the precursor form of human tripeptidyl-peptidase 1, the enzyme deficient in late infantile ceroid lipofuscinosis.
19038967	1	15	theme	childhood	220:228	arg1	lipofuscinosis					194:207	Late infantile neuronal ceroid lipofuscinosis	163:207	Late infantile neuronal ceroid lipofuscinosis	163:207	Late infantile neuronal ceroid lipofuscinosis is a fatal childhood neurological disorder caused by a deficiency in the lysosomal protease tripeptidyl-peptidase 1 (TPP1).
19038967	1	15	theme	childhood	220:228	arg1	disorder					243:250	a fatal childhood neurological disorder	212:250	a fatal childhood neurological disorder caused by a deficiency in the lysosomal protease tripeptidyl-peptidase 1 (TPP1)	212:330	Late infantile neuronal ceroid lipofuscinosis is a fatal childhood neurological disorder caused by a deficiency in the lysosomal protease tripeptidyl-peptidase 1 (TPP1).
19038967	7	16	theme	propiece	1394:1401	arg1	linker					1403:1408	its propiece linker	1390:1408	its propiece linker	1390:1408	The proenzyme structure reveals suboptimal catalytic triad geometry with its propiece linker partially blocking the substrate-binding site, which together serve to prevent premature activation of the protease.
19038967	0	17	theme	ceroid	140:145	arg1	lipofuscinosis					147:160	late infantile ceroid lipofuscinosis	125:160	late infantile ceroid lipofuscinosis	125:160	Crystal structure and autoactivation pathway of the precursor form of human tripeptidyl-peptidase 1, the enzyme deficient in late infantile ceroid lipofuscinosis.
19038967	9	18	theme	TPP1	1787:1790	arg1	variants					1792:1799	improved TPP1 variants	1778:1799	improved TPP1 variants	1778:1799	These data provide new insights into TPP1 function and represent a valuable resource for constructing improved TPP1 variants for treatment of late infantile neuronal ceroid lipofuscinosis.
19038967	4	19	from	TPP1	885:888	arg1	indistinguishable					843:859	indistinguishable	843:859	indistinguishable	843:859	In this study, we describe an endoglycosidase H-deglycosylated form of TPP1 containing four Asn-linked N-acetylglucosamines that is indistinguishable from fully glycosylated TPP1 in terms of autocatalytic processing of the proform and enzymatic properties of the mature protease.
19038967	4	19	from	TPP1	885:888	arg1	terms					893:897	terms	893:897	terms of autocatalytic processing of the proform	893:940	In this study, we describe an endoglycosidase H-deglycosylated form of TPP1 containing four Asn-linked N-acetylglucosamines that is indistinguishable from fully glycosylated TPP1 in terms of autocatalytic processing of the proform and enzymatic properties of the mature protease.
19038967	4	19	from	TPP1	885:888	arg1	form					774:777	an endoglycosidase H-deglycosylated form	738:777	an endoglycosidase H-deglycosylated form of TPP1 containing four Asn-linked N-acetylglucosamines that is indistinguishable from fully glycosylated TPP1 in terms of autocatalytic processing of the proform and enzymatic properties of the mature protease	738:988	In this study, we describe an endoglycosidase H-deglycosylated form of TPP1 containing four Asn-linked N-acetylglucosamines that is indistinguishable from fully glycosylated TPP1 in terms of autocatalytic processing of the proform and enzymatic properties of the mature protease.
19038967	7	20	theme	triad	1370:1374	arg1	geometry					1376:1383	suboptimal catalytic triad geometry	1349:1383	suboptimal catalytic triad geometry	1349:1383	The proenzyme structure reveals suboptimal catalytic triad geometry with its propiece linker partially blocking the substrate-binding site, which together serve to prevent premature activation of the protease.
19038967	0	21	theme	form	62:65	arg1	structure					8:16	Crystal structure	0:16	Crystal structure	0:16	Crystal structure and autoactivation pathway of the precursor form of human tripeptidyl-peptidase 1, the enzyme deficient in late infantile ceroid lipofuscinosis.
19038967	0	21	theme	form	62:65	arg1	pathway					37:43	autoactivation pathway	22:43	autoactivation pathway	22:43	Crystal structure and autoactivation pathway of the precursor form of human tripeptidyl-peptidase 1, the enzyme deficient in late infantile ceroid lipofuscinosis.
19038967	2	22	theme	catalytic	483:491	arg1	triad					493:497	a Ser-Glu-Asp catalytic triad	469:497	a Ser-Glu-Asp catalytic triad	469:497	TPP1 represents the only known mammalian member of the S53 family of serine proteases, a group characterized by a subtilisin-like fold, a Ser-Glu-Asp catalytic triad, and an acidic pH optimum.
19038967	0	23	theme	human	70:74	arg1	form					62:65	the precursor form	48:65	the precursor form of human tripeptidyl-peptidase 1, the enzyme deficient in late infantile ceroid lipofuscinosis	48:160	Crystal structure and autoactivation pathway of the precursor form of human tripeptidyl-peptidase 1, the enzyme deficient in late infantile ceroid lipofuscinosis.
19038967	1	24	theme	Late	163:166	arg1	lipofuscinosis					194:207	Late infantile neuronal ceroid lipofuscinosis	163:207	Late infantile neuronal ceroid lipofuscinosis	163:207	Late infantile neuronal ceroid lipofuscinosis is a fatal childhood neurological disorder caused by a deficiency in the lysosomal protease tripeptidyl-peptidase 1 (TPP1).
19038967	1	24	theme	Late	163:166	arg1	disorder					243:250	a fatal childhood neurological disorder	212:250	a fatal childhood neurological disorder caused by a deficiency in the lysosomal protease tripeptidyl-peptidase 1 (TPP1)	212:330	Late infantile neuronal ceroid lipofuscinosis is a fatal childhood neurological disorder caused by a deficiency in the lysosomal protease tripeptidyl-peptidase 1 (TPP1).
19038967	2	25	theme	pH	514:515	arg1	optimum					517:523	an acidic pH optimum	504:523	an acidic pH optimum	504:523	TPP1 represents the only known mammalian member of the S53 family of serine proteases, a group characterized by a subtilisin-like fold, a Ser-Glu-Asp catalytic triad, and an acidic pH optimum.
19038967	4	26	theme	enzymatic	946:954	arg1	properties					956:965	enzymatic properties	946:965	enzymatic properties of the mature protease	946:988	In this study, we describe an endoglycosidase H-deglycosylated form of TPP1 containing four Asn-linked N-acetylglucosamines that is indistinguishable from fully glycosylated TPP1 in terms of autocatalytic processing of the proform and enzymatic properties of the mature protease.
19038967	8	27	theme	numerous	1555:1562	arg1	intermediates					1575:1587	numerous processing intermediates	1555:1587	numerous processing intermediates	1555:1587	Finally, we have identified numerous processing intermediates and propose a structural model that explains the pathway for TPP1 activation in vitro.
19038967	7	28	theme	catalytic	1360:1368	arg1	geometry					1376:1383	suboptimal catalytic triad geometry	1349:1383	suboptimal catalytic triad geometry	1349:1383	The proenzyme structure reveals suboptimal catalytic triad geometry with its propiece linker partially blocking the substrate-binding site, which together serve to prevent premature activation of the protease.
19038967	2	29	theme	S53	388:390	arg1	family					392:397	the S53 family	384:397	the S53 family of serine proteases	384:417	TPP1 represents the only known mammalian member of the S53 family of serine proteases, a group characterized by a subtilisin-like fold, a Ser-Glu-Asp catalytic triad, and an acidic pH optimum.
19038967	0	30	theme	Crystal	0:6	arg1	structure					8:16	Crystal structure	0:16	Crystal structure	0:16	Crystal structure and autoactivation pathway of the precursor form of human tripeptidyl-peptidase 1, the enzyme deficient in late infantile ceroid lipofuscinosis.
19038967	1	31	theme	lysosomal	282:290	arg1	TPP1					326:329	TPP1	326:329	TPP1	326:329	Late infantile neuronal ceroid lipofuscinosis is a fatal childhood neurological disorder caused by a deficiency in the lysosomal protease tripeptidyl-peptidase 1 (TPP1).
19038967	1	31	theme	lysosomal	282:290	arg1	protease					292:299	the lysosomal protease tripeptidyl-peptidase 1	278:323	the lysosomal protease tripeptidyl-peptidase 1 (TPP1)	278:330	Late infantile neuronal ceroid lipofuscinosis is a fatal childhood neurological disorder caused by a deficiency in the lysosomal protease tripeptidyl-peptidase 1 (TPP1).
19038967	9	32	theme	TPP1	1713:1716	arg1	function					1718:1725	TPP1 function	1713:1725	TPP1 function	1713:1725	These data provide new insights into TPP1 function and represent a valuable resource for constructing improved TPP1 variants for treatment of late infantile neuronal ceroid lipofuscinosis.
19038967	1	33	theme	tripeptidyl-peptidase	301:321	arg1	TPP1					326:329	TPP1	326:329	TPP1	326:329	Late infantile neuronal ceroid lipofuscinosis is a fatal childhood neurological disorder caused by a deficiency in the lysosomal protease tripeptidyl-peptidase 1 (TPP1).
19038967	1	33	theme	tripeptidyl-peptidase	301:321	arg1	protease					292:299	the lysosomal protease tripeptidyl-peptidase 1	278:323	the lysosomal protease tripeptidyl-peptidase 1 (TPP1)	278:330	Late infantile neuronal ceroid lipofuscinosis is a fatal childhood neurological disorder caused by a deficiency in the lysosomal protease tripeptidyl-peptidase 1 (TPP1).
19038967	7	34	theme	proenzyme	1321:1329	arg1	structure					1331:1339	The proenzyme structure	1317:1339	The proenzyme structure	1317:1339	The proenzyme structure reveals suboptimal catalytic triad geometry with its propiece linker partially blocking the substrate-binding site, which together serve to prevent premature activation of the protease.
19038967	8	35	theme	structural	1603:1612	arg1	model					1614:1618	a structural model	1601:1618	a structural model that explains the pathway for TPP1 activation in vitro	1601:1673	Finally, we have identified numerous processing intermediates and propose a structural model that explains the pathway for TPP1 activation in vitro.
19038967	2	36	theme	proteases	409:417	arg1	family					392:397	the S53 family	384:397	the S53 family of serine proteases	384:417	TPP1 represents the only known mammalian member of the S53 family of serine proteases, a group characterized by a subtilisin-like fold, a Ser-Glu-Asp catalytic triad, and an acidic pH optimum.
19038967	4	37	gly	H-deglycosylated	757:772	arg1	indistinguishable					843:859	indistinguishable	843:859	indistinguishable	843:859	In this study, we describe an endoglycosidase H-deglycosylated form of TPP1 containing four Asn-linked N-acetylglucosamines that is indistinguishable from fully glycosylated TPP1 in terms of autocatalytic processing of the proform and enzymatic properties of the mature protease.
19038967	4	37	gly	H-deglycosylated	757:772	arg1	TPP1					782:785	TPP1	782:785	TPP1 containing four Asn-linked N-acetylglucosamines	782:833	In this study, we describe an endoglycosidase H-deglycosylated form of TPP1 containing four Asn-linked N-acetylglucosamines that is indistinguishable from fully glycosylated TPP1 in terms of autocatalytic processing of the proform and enzymatic properties of the mature protease.
19038967	4	37	gly	H-deglycosylated	757:772	arg1	form					774:777	an endoglycosidase H-deglycosylated form	738:777	an endoglycosidase H-deglycosylated form of TPP1 containing four Asn-linked N-acetylglucosamines that is indistinguishable from fully glycosylated TPP1 in terms of autocatalytic processing of the proform and enzymatic properties of the mature protease	738:988	In this study, we describe an endoglycosidase H-deglycosylated form of TPP1 containing four Asn-linked N-acetylglucosamines that is indistinguishable from fully glycosylated TPP1 in terms of autocatalytic processing of the proform and enzymatic properties of the mature protease.
19038967	5	38	theme	pro-TPP1	1031:1038	arg1	structure					1003:1011	The crystal structure	991:1011	The crystal structure of deglycosylated pro-TPP1	991:1038	The crystal structure of deglycosylated pro-TPP1 was determined at 1.85 angstroms resolution.
19038967	3	39	theme	low	657:659	arg1	pH					661:662	low pH	657:662	low pH	657:662	TPP1 is synthesized as an inactive proenzyme (pro-TPP1) that is proteolytically processed into the active enzyme after exposure to low pH in vitro or targeting to the lysosome in vivo.
19038967	1	40	theme	neurological	230:241	arg1	lipofuscinosis					194:207	Late infantile neuronal ceroid lipofuscinosis	163:207	Late infantile neuronal ceroid lipofuscinosis	163:207	Late infantile neuronal ceroid lipofuscinosis is a fatal childhood neurological disorder caused by a deficiency in the lysosomal protease tripeptidyl-peptidase 1 (TPP1).
19038967	1	40	theme	neurological	230:241	arg1	disorder					243:250	a fatal childhood neurological disorder	212:250	a fatal childhood neurological disorder caused by a deficiency in the lysosomal protease tripeptidyl-peptidase 1 (TPP1)	212:330	Late infantile neuronal ceroid lipofuscinosis is a fatal childhood neurological disorder caused by a deficiency in the lysosomal protease tripeptidyl-peptidase 1 (TPP1).
19038967	4	41	theme	H-deglycosylated	757:772	arg1	indistinguishable					843:859	indistinguishable	843:859	indistinguishable	843:859	In this study, we describe an endoglycosidase H-deglycosylated form of TPP1 containing four Asn-linked N-acetylglucosamines that is indistinguishable from fully glycosylated TPP1 in terms of autocatalytic processing of the proform and enzymatic properties of the mature protease.
19038967	4	41	theme	H-deglycosylated	757:772	arg1	form					774:777	an endoglycosidase H-deglycosylated form	738:777	an endoglycosidase H-deglycosylated form of TPP1 containing four Asn-linked N-acetylglucosamines that is indistinguishable from fully glycosylated TPP1 in terms of autocatalytic processing of the proform and enzymatic properties of the mature protease	738:988	In this study, we describe an endoglycosidase H-deglycosylated form of TPP1 containing four Asn-linked N-acetylglucosamines that is indistinguishable from fully glycosylated TPP1 in terms of autocatalytic processing of the proform and enzymatic properties of the mature protease.
19038967	5	42	theme	crystal	995:1001	arg1	structure					1003:1011	The crystal structure	991:1011	The crystal structure of deglycosylated pro-TPP1	991:1038	The crystal structure of deglycosylated pro-TPP1 was determined at 1.85 angstroms resolution.
19038967	6	43	theme	C-shaped	1105:1112	arg1	prodomain					1114:1122	A large 151-residue C-shaped prodomain	1085:1122	A large 151-residue C-shaped prodomain	1085:1122	A large 151-residue C-shaped prodomain makes extensive contacts as it wraps around the surface of the catalytic domain with the two domains connected by a 24-residue flexible linker that passes through the substrate-binding groove.
19038967	0	44	from	deficient	112:120	arg1	lipofuscinosis					147:160	late infantile ceroid lipofuscinosis	125:160	late infantile ceroid lipofuscinosis	125:160	Crystal structure and autoactivation pathway of the precursor form of human tripeptidyl-peptidase 1, the enzyme deficient in late infantile ceroid lipofuscinosis.
19038967	4	45	theme	mature	974:979	arg1	protease					981:988	the mature protease	970:988	the mature protease	970:988	In this study, we describe an endoglycosidase H-deglycosylated form of TPP1 containing four Asn-linked N-acetylglucosamines that is indistinguishable from fully glycosylated TPP1 in terms of autocatalytic processing of the proform and enzymatic properties of the mature protease.
19038967	6	46	theme	substrate-binding	1291:1307	arg1	groove					1309:1314	the substrate-binding groove	1287:1314	the substrate-binding groove	1287:1314	A large 151-residue C-shaped prodomain makes extensive contacts as it wraps around the surface of the catalytic domain with the two domains connected by a 24-residue flexible linker that passes through the substrate-binding groove.
19038967	2	47	theme	mammalian	364:372	arg1	group					422:426	a group	420:426	a group characterized by a subtilisin-like fold, a Ser-Glu-Asp catalytic triad, and an acidic pH optimum	420:523	TPP1 represents the only known mammalian member of the S53 family of serine proteases, a group characterized by a subtilisin-like fold, a Ser-Glu-Asp catalytic triad, and an acidic pH optimum.
19038967	2	47	theme	mammalian	364:372	arg1	member					374:379	the only known mammalian member	349:379	the only known mammalian member of the S53 family of serine proteases	349:417	TPP1 represents the only known mammalian member of the S53 family of serine proteases, a group characterized by a subtilisin-like fold, a Ser-Glu-Asp catalytic triad, and an acidic pH optimum.
19038967	9	48	theme	new	1695:1697	arg1	insights					1699:1706	new insights	1695:1706	new insights into TPP1 function	1695:1725	These data provide new insights into TPP1 function and represent a valuable resource for constructing improved TPP1 variants for treatment of late infantile neuronal ceroid lipofuscinosis.
19038967	6	49	theme	large	1087:1091	arg1	prodomain					1114:1122	A large 151-residue C-shaped prodomain	1085:1122	A large 151-residue C-shaped prodomain	1085:1122	A large 151-residue C-shaped prodomain makes extensive contacts as it wraps around the surface of the catalytic domain with the two domains connected by a 24-residue flexible linker that passes through the substrate-binding groove.
19038967	1	50	theme	infantile	168:176	arg1	lipofuscinosis					194:207	Late infantile neuronal ceroid lipofuscinosis	163:207	Late infantile neuronal ceroid lipofuscinosis	163:207	Late infantile neuronal ceroid lipofuscinosis is a fatal childhood neurological disorder caused by a deficiency in the lysosomal protease tripeptidyl-peptidase 1 (TPP1).
19038967	1	50	theme	infantile	168:176	arg1	disorder					243:250	a fatal childhood neurological disorder	212:250	a fatal childhood neurological disorder caused by a deficiency in the lysosomal protease tripeptidyl-peptidase 1 (TPP1)	212:330	Late infantile neuronal ceroid lipofuscinosis is a fatal childhood neurological disorder caused by a deficiency in the lysosomal protease tripeptidyl-peptidase 1 (TPP1).
19038967	1	51	from	deficiency	264:273	arg1	TPP1					326:329	TPP1	326:329	TPP1	326:329	Late infantile neuronal ceroid lipofuscinosis is a fatal childhood neurological disorder caused by a deficiency in the lysosomal protease tripeptidyl-peptidase 1 (TPP1).
19038967	1	51	from	deficiency	264:273	arg1	protease					292:299	the lysosomal protease tripeptidyl-peptidase 1	278:323	the lysosomal protease tripeptidyl-peptidase 1 (TPP1)	278:330	Late infantile neuronal ceroid lipofuscinosis is a fatal childhood neurological disorder caused by a deficiency in the lysosomal protease tripeptidyl-peptidase 1 (TPP1).
19038967	2	52	theme	Ser-Glu-Asp	471:481	arg1	triad					493:497	a Ser-Glu-Asp catalytic triad	469:497	a Ser-Glu-Asp catalytic triad	469:497	TPP1 represents the only known mammalian member of the S53 family of serine proteases, a group characterized by a subtilisin-like fold, a Ser-Glu-Asp catalytic triad, and an acidic pH optimum.
19038967	6	53	theme	flexible	1251:1258	arg1	linker					1260:1265	a 24-residue flexible linker	1238:1265	a 24-residue flexible linker that passes through the substrate-binding groove	1238:1314	A large 151-residue C-shaped prodomain makes extensive contacts as it wraps around the surface of the catalytic domain with the two domains connected by a 24-residue flexible linker that passes through the substrate-binding groove.
19038967	1	54	theme	ceroid	187:192	arg1	lipofuscinosis					194:207	Late infantile neuronal ceroid lipofuscinosis	163:207	Late infantile neuronal ceroid lipofuscinosis	163:207	Late infantile neuronal ceroid lipofuscinosis is a fatal childhood neurological disorder caused by a deficiency in the lysosomal protease tripeptidyl-peptidase 1 (TPP1).
19038967	1	54	theme	ceroid	187:192	arg1	disorder					243:250	a fatal childhood neurological disorder	212:250	a fatal childhood neurological disorder caused by a deficiency in the lysosomal protease tripeptidyl-peptidase 1 (TPP1)	212:330	Late infantile neuronal ceroid lipofuscinosis is a fatal childhood neurological disorder caused by a deficiency in the lysosomal protease tripeptidyl-peptidase 1 (TPP1).
19038967	9	55	theme	valuable	1743:1750	arg1	resource					1752:1759	a valuable resource	1741:1759	a valuable resource for constructing improved TPP1 variants for treatment of late infantile neuronal ceroid lipofuscinosis	1741:1862	These data provide new insights into TPP1 function and represent a valuable resource for constructing improved TPP1 variants for treatment of late infantile neuronal ceroid lipofuscinosis.
19038967	7	56	theme	substrate-binding	1433:1449	arg1	site					1451:1454	the substrate-binding site	1429:1454	the substrate-binding site	1429:1454	The proenzyme structure reveals suboptimal catalytic triad geometry with its propiece linker partially blocking the substrate-binding site, which together serve to prevent premature activation of the protease.
19038967	0	57	theme	infantile	130:138	arg1	lipofuscinosis					147:160	late infantile ceroid lipofuscinosis	125:160	late infantile ceroid lipofuscinosis	125:160	Crystal structure and autoactivation pathway of the precursor form of human tripeptidyl-peptidase 1, the enzyme deficient in late infantile ceroid lipofuscinosis.
19038967	1	58	theme	fatal	214:218	arg1	lipofuscinosis					194:207	Late infantile neuronal ceroid lipofuscinosis	163:207	Late infantile neuronal ceroid lipofuscinosis	163:207	Late infantile neuronal ceroid lipofuscinosis is a fatal childhood neurological disorder caused by a deficiency in the lysosomal protease tripeptidyl-peptidase 1 (TPP1).
19038967	1	58	theme	fatal	214:218	arg1	disorder					243:250	a fatal childhood neurological disorder	212:250	a fatal childhood neurological disorder caused by a deficiency in the lysosomal protease tripeptidyl-peptidase 1 (TPP1)	212:330	Late infantile neuronal ceroid lipofuscinosis is a fatal childhood neurological disorder caused by a deficiency in the lysosomal protease tripeptidyl-peptidase 1 (TPP1).
19038967	4	59	theme	processing	916:925	arg1	terms					893:897	terms	893:897	terms of autocatalytic processing of the proform	893:940	In this study, we describe an endoglycosidase H-deglycosylated form of TPP1 containing four Asn-linked N-acetylglucosamines that is indistinguishable from fully glycosylated TPP1 in terms of autocatalytic processing of the proform and enzymatic properties of the mature protease.
19038967	4	60	link	Asn-linked	803:812	arg1	N-acetylglucosamines					814:833	four Asn-linked N-acetylglucosamines	798:833	four Asn-linked N-acetylglucosamines	798:833	In this study, we describe an endoglycosidase H-deglycosylated form of TPP1 containing four Asn-linked N-acetylglucosamines that is indistinguishable from fully glycosylated TPP1 in terms of autocatalytic processing of the proform and enzymatic properties of the mature protease.
19038967	9	61	theme	infantile	1823:1831	arg1	lipofuscinosis					1849:1862	late infantile neuronal ceroid lipofuscinosis	1818:1862	late infantile neuronal ceroid lipofuscinosis	1818:1862	These data provide new insights into TPP1 function and represent a valuable resource for constructing improved TPP1 variants for treatment of late infantile neuronal ceroid lipofuscinosis.
19038967	4	62	theme	glycosylated	872:883	arg1	TPP1					885:888	fully glycosylated TPP1	866:888	fully glycosylated TPP1 in terms of autocatalytic processing of the proform	866:940	In this study, we describe an endoglycosidase H-deglycosylated form of TPP1 containing four Asn-linked N-acetylglucosamines that is indistinguishable from fully glycosylated TPP1 in terms of autocatalytic processing of the proform and enzymatic properties of the mature protease.
19038967	4	63	gly	glycosylated	872:883	arg1	TPP1					885:888	fully glycosylated TPP1	866:888	fully glycosylated TPP1 in terms of autocatalytic processing of the proform	866:940	In this study, we describe an endoglycosidase H-deglycosylated form of TPP1 containing four Asn-linked N-acetylglucosamines that is indistinguishable from fully glycosylated TPP1 in terms of autocatalytic processing of the proform and enzymatic properties of the mature protease.
19038967	6	64	theme	domain	1197:1202	arg1	surface					1172:1178	the surface	1168:1178	the surface of the catalytic domain	1168:1202	A large 151-residue C-shaped prodomain makes extensive contacts as it wraps around the surface of the catalytic domain with the two domains connected by a 24-residue flexible linker that passes through the substrate-binding groove.
19038967	9	65	theme	neuronal	1833:1840	arg1	lipofuscinosis					1849:1862	late infantile neuronal ceroid lipofuscinosis	1818:1862	late infantile neuronal ceroid lipofuscinosis	1818:1862	These data provide new insights into TPP1 function and represent a valuable resource for constructing improved TPP1 variants for treatment of late infantile neuronal ceroid lipofuscinosis.
19038967	0	66	theme	tripeptidyl-peptidase	76:96	arg1	human					70:74	human tripeptidyl-peptidase 1	70:98	human tripeptidyl-peptidase 1	70:98	Crystal structure and autoactivation pathway of the precursor form of human tripeptidyl-peptidase 1, the enzyme deficient in late infantile ceroid lipofuscinosis.
19038967	0	66	theme	tripeptidyl-peptidase	76:96	arg1	enzyme					105:110	the enzyme	101:110	the enzyme deficient in late infantile ceroid lipofuscinosis	101:160	Crystal structure and autoactivation pathway of the precursor form of human tripeptidyl-peptidase 1, the enzyme deficient in late infantile ceroid lipofuscinosis.
19038967	9	67	theme	late	1818:1821	arg1	lipofuscinosis					1849:1862	late infantile neuronal ceroid lipofuscinosis	1818:1862	late infantile neuronal ceroid lipofuscinosis	1818:1862	These data provide new insights into TPP1 function and represent a valuable resource for constructing improved TPP1 variants for treatment of late infantile neuronal ceroid lipofuscinosis.
19038967	4	68	contain	containing	787:796	arg1	TPP1					782:785	TPP1	782:785	TPP1 containing four Asn-linked N-acetylglucosamines	782:833	In this study, we describe an endoglycosidase H-deglycosylated form of TPP1 containing four Asn-linked N-acetylglucosamines that is indistinguishable from fully glycosylated TPP1 in terms of autocatalytic processing of the proform and enzymatic properties of the mature protease.
19038967	4	68	contain	containing	787:796	arg2	N-acetylglucosamines					814:833	four Asn-linked N-acetylglucosamines	798:833	four Asn-linked N-acetylglucosamines	798:833	In this study, we describe an endoglycosidase H-deglycosylated form of TPP1 containing four Asn-linked N-acetylglucosamines that is indistinguishable from fully glycosylated TPP1 in terms of autocatalytic processing of the proform and enzymatic properties of the mature protease.
19038967	2	69	theme	acidic	507:512	arg1	optimum					517:523	an acidic pH optimum	504:523	an acidic pH optimum	504:523	TPP1 represents the only known mammalian member of the S53 family of serine proteases, a group characterized by a subtilisin-like fold, a Ser-Glu-Asp catalytic triad, and an acidic pH optimum.
19038967	8	70	theme	processing	1564:1573	arg1	intermediates					1575:1587	numerous processing intermediates	1555:1587	numerous processing intermediates	1555:1587	Finally, we have identified numerous processing intermediates and propose a structural model that explains the pathway for TPP1 activation in vitro.
19038967	7	71	theme	suboptimal	1349:1358	arg1	geometry					1376:1383	suboptimal catalytic triad geometry	1349:1383	suboptimal catalytic triad geometry	1349:1383	The proenzyme structure reveals suboptimal catalytic triad geometry with its propiece linker partially blocking the substrate-binding site, which together serve to prevent premature activation of the protease.
19038967	9	72	theme	lipofuscinosis	1849:1862	arg1	treatment					1805:1813	treatment	1805:1813	treatment of late infantile neuronal ceroid lipofuscinosis	1805:1862	These data provide new insights into TPP1 function and represent a valuable resource for constructing improved TPP1 variants for treatment of late infantile neuronal ceroid lipofuscinosis.
19038967	9	73	theme	ceroid	1842:1847	arg1	lipofuscinosis					1849:1862	late infantile neuronal ceroid lipofuscinosis	1818:1862	late infantile neuronal ceroid lipofuscinosis	1818:1862	These data provide new insights into TPP1 function and represent a valuable resource for constructing improved TPP1 variants for treatment of late infantile neuronal ceroid lipofuscinosis.
19038967	4	74	theme	proform	934:940	arg1	processing					916:925	autocatalytic processing	902:925	autocatalytic processing of the proform	902:940	In this study, we describe an endoglycosidase H-deglycosylated form of TPP1 containing four Asn-linked N-acetylglucosamines that is indistinguishable from fully glycosylated TPP1 in terms of autocatalytic processing of the proform and enzymatic properties of the mature protease.
19038967	0	75	theme	autoactivation	22:35	arg1	pathway					37:43	autoactivation pathway	22:43	autoactivation pathway	22:43	Crystal structure and autoactivation pathway of the precursor form of human tripeptidyl-peptidase 1, the enzyme deficient in late infantile ceroid lipofuscinosis.
19038967	5	76	gly	deglycosylated	1016:1029	arg1	pro-TPP1					1031:1038	deglycosylated pro-TPP1	1016:1038	deglycosylated pro-TPP1	1016:1038	The crystal structure of deglycosylated pro-TPP1 was determined at 1.85 angstroms resolution.
19038967	3	77	theme	active	625:630	arg1	enzyme					632:637	the active enzyme	621:637	the active enzyme	621:637	TPP1 is synthesized as an inactive proenzyme (pro-TPP1) that is proteolytically processed into the active enzyme after exposure to low pH in vitro or targeting to the lysosome in vivo.
19038967	4	78	theme	protease	981:988	arg1	TPP1					885:888	fully glycosylated TPP1	866:888	fully glycosylated TPP1 in terms of autocatalytic processing of the proform	866:940	In this study, we describe an endoglycosidase H-deglycosylated form of TPP1 containing four Asn-linked N-acetylglucosamines that is indistinguishable from fully glycosylated TPP1 in terms of autocatalytic processing of the proform and enzymatic properties of the mature protease.
19038967	4	78	theme	protease	981:988	arg1	properties					956:965	enzymatic properties	946:965	enzymatic properties of the mature protease	946:988	In this study, we describe an endoglycosidase H-deglycosylated form of TPP1 containing four Asn-linked N-acetylglucosamines that is indistinguishable from fully glycosylated TPP1 in terms of autocatalytic processing of the proform and enzymatic properties of the mature protease.
19038967	2	79	theme	serine	402:407	arg1	proteases					409:417	serine proteases	402:417	serine proteases	402:417	TPP1 represents the only known mammalian member of the S53 family of serine proteases, a group characterized by a subtilisin-like fold, a Ser-Glu-Asp catalytic triad, and an acidic pH optimum.
19038967	0	80	theme	precursor	52:60	arg1	form					62:65	the precursor form	48:65	the precursor form of human tripeptidyl-peptidase 1, the enzyme deficient in late infantile ceroid lipofuscinosis	48:160	Crystal structure and autoactivation pathway of the precursor form of human tripeptidyl-peptidase 1, the enzyme deficient in late infantile ceroid lipofuscinosis.
19038967	5	81	theme	deglycosylated	1016:1029	arg1	pro-TPP1					1031:1038	deglycosylated pro-TPP1	1016:1038	deglycosylated pro-TPP1	1016:1038	The crystal structure of deglycosylated pro-TPP1 was determined at 1.85 angstroms resolution.
19038967	2	82	theme	subtilisin-like	447:461	arg1	fold					463:466	a subtilisin-like fold	445:466	a subtilisin-like fold	445:466	TPP1 represents the only known mammalian member of the S53 family of serine proteases, a group characterized by a subtilisin-like fold, a Ser-Glu-Asp catalytic triad, and an acidic pH optimum.
19038967	4	83	theme	TPP1	782:785	arg1	indistinguishable					843:859	indistinguishable	843:859	indistinguishable	843:859	In this study, we describe an endoglycosidase H-deglycosylated form of TPP1 containing four Asn-linked N-acetylglucosamines that is indistinguishable from fully glycosylated TPP1 in terms of autocatalytic processing of the proform and enzymatic properties of the mature protease.
19038967	4	83	theme	TPP1	782:785	arg1	form					774:777	an endoglycosidase H-deglycosylated form	738:777	an endoglycosidase H-deglycosylated form of TPP1 containing four Asn-linked N-acetylglucosamines that is indistinguishable from fully glycosylated TPP1 in terms of autocatalytic processing of the proform and enzymatic properties of the mature protease	738:988	In this study, we describe an endoglycosidase H-deglycosylated form of TPP1 containing four Asn-linked N-acetylglucosamines that is indistinguishable from fully glycosylated TPP1 in terms of autocatalytic processing of the proform and enzymatic properties of the mature protease.
19038967	6	84	theme	extensive	1130:1138	arg1	contacts					1140:1147	extensive contacts	1130:1147	extensive contacts	1130:1147	A large 151-residue C-shaped prodomain makes extensive contacts as it wraps around the surface of the catalytic domain with the two domains connected by a 24-residue flexible linker that passes through the substrate-binding groove.
19038967	8	85	theme	TPP1	1650:1653	arg1	activation					1655:1664	TPP1 activation	1650:1664	TPP1 activation	1650:1664	Finally, we have identified numerous processing intermediates and propose a structural model that explains the pathway for TPP1 activation in vitro.
19038967	2	86	theme	family	392:397	arg1	group					422:426	a group	420:426	a group characterized by a subtilisin-like fold, a Ser-Glu-Asp catalytic triad, and an acidic pH optimum	420:523	TPP1 represents the only known mammalian member of the S53 family of serine proteases, a group characterized by a subtilisin-like fold, a Ser-Glu-Asp catalytic triad, and an acidic pH optimum.
19038967	2	86	theme	family	392:397	arg1	member					374:379	the only known mammalian member	349:379	the only known mammalian member of the S53 family of serine proteases	349:417	TPP1 represents the only known mammalian member of the S53 family of serine proteases, a group characterized by a subtilisin-like fold, a Ser-Glu-Asp catalytic triad, and an acidic pH optimum.
19038967	4	87	theme	endoglycosidase	741:755	arg1	indistinguishable					843:859	indistinguishable	843:859	indistinguishable	843:859	In this study, we describe an endoglycosidase H-deglycosylated form of TPP1 containing four Asn-linked N-acetylglucosamines that is indistinguishable from fully glycosylated TPP1 in terms of autocatalytic processing of the proform and enzymatic properties of the mature protease.
19038967	4	87	theme	endoglycosidase	741:755	arg1	form					774:777	an endoglycosidase H-deglycosylated form	738:777	an endoglycosidase H-deglycosylated form of TPP1 containing four Asn-linked N-acetylglucosamines that is indistinguishable from fully glycosylated TPP1 in terms of autocatalytic processing of the proform and enzymatic properties of the mature protease	738:988	In this study, we describe an endoglycosidase H-deglycosylated form of TPP1 containing four Asn-linked N-acetylglucosamines that is indistinguishable from fully glycosylated TPP1 in terms of autocatalytic processing of the proform and enzymatic properties of the mature protease.
19038967	4	88	from	properties	956:965	arg1	indistinguishable					843:859	indistinguishable	843:859	indistinguishable	843:859	In this study, we describe an endoglycosidase H-deglycosylated form of TPP1 containing four Asn-linked N-acetylglucosamines that is indistinguishable from fully glycosylated TPP1 in terms of autocatalytic processing of the proform and enzymatic properties of the mature protease.
19038967	4	88	from	properties	956:965	arg1	terms					893:897	terms	893:897	terms of autocatalytic processing of the proform	893:940	In this study, we describe an endoglycosidase H-deglycosylated form of TPP1 containing four Asn-linked N-acetylglucosamines that is indistinguishable from fully glycosylated TPP1 in terms of autocatalytic processing of the proform and enzymatic properties of the mature protease.
19038967	4	88	from	properties	956:965	arg1	form					774:777	an endoglycosidase H-deglycosylated form	738:777	an endoglycosidase H-deglycosylated form of TPP1 containing four Asn-linked N-acetylglucosamines that is indistinguishable from fully glycosylated TPP1 in terms of autocatalytic processing of the proform and enzymatic properties of the mature protease	738:988	In this study, we describe an endoglycosidase H-deglycosylated form of TPP1 containing four Asn-linked N-acetylglucosamines that is indistinguishable from fully glycosylated TPP1 in terms of autocatalytic processing of the proform and enzymatic properties of the mature protease.
9126611	7	0	from	decrease	1282:1289	arg1	heterogeneity					1294:1306	heterogeneity	1294:1306	heterogeneity	1294:1306	Expression of a double N-glycosylation site mutant in Sf9 cells, N580Q/N592Q, resulted in a decrease in glycosylation but no clear decrease in heterogeneity, indicating that the high degree of N-glycosylation heterogeneity observed with the BV-Sf9 system is not due to partial glycosylation of both Asn580 and Asn592.
9126611	6	1	theme	heterogeneity	1055:1067	arg1	levels					1029:1034	High levels	1024:1034	High levels of N-glycosylation heterogeneity	1024:1067	High levels of N-glycosylation heterogeneity are observed in hCox-2 expressed using recombinant baculovirus (BV) in Sf9 cells.
9126611	8	2	theme	high	1576:1579	arg1	GlcNAc					1609:1614	(Man)n (GlcNAc)2	1601:1616	(Man)n (GlcNAc)2	1601:1616	N-linked oligosaccharide profiling of purified VV and BV WT and S582A mutant hCox-2 showed the presence of high mannose structures, (Man)n (GlcNAc)2, n = 9, 8, 7, 6.
9126611	8	2	theme	high	1576:1579	arg1	structures					1589:1598	high mannose structures	1576:1598	high mannose structures	1576:1598	N-linked oligosaccharide profiling of purified VV and BV WT and S582A mutant hCox-2 showed the presence of high mannose structures, (Man)n (GlcNAc)2, n = 9, 8, 7, 6.
9126611	3	3	theme	single	516:521	arg1	glycoform					523:531	a single glycoform	514:531	a single glycoform	514:531	Removal of the N-glycosylation consensus sequence at Asn580 (N580Q and S582A mutants) resulted in the expression of protein comprising a single glycoform, consistent with the partial N-glycosylation at this site in the wild-type (WT) enzyme.
9126611	1	4	theme	drugs	275:279	arg1	target					234:239	the target	230:239	the target of nonsteroidal anti-inflammatory drugs	230:279	Human cyclooxygenase-2 (hCox-2) is a key enzyme in the biosynthesis of prostaglandins and the target of nonsteroidal anti-inflammatory drugs.
9126611	1	4	theme	drugs	275:279	arg1	biosynthesis					195:206	the biosynthesis	191:206	the biosynthesis of prostaglandins	191:224	Human cyclooxygenase-2 (hCox-2) is a key enzyme in the biosynthesis of prostaglandins and the target of nonsteroidal anti-inflammatory drugs.
9126611	7	5	theme	BV-Sf9	1392:1397	arg1	system					1399:1404	the BV-Sf9 system	1388:1404	the BV-Sf9 system	1388:1404	Expression of a double N-glycosylation site mutant in Sf9 cells, N580Q/N592Q, resulted in a decrease in glycosylation but no clear decrease in heterogeneity, indicating that the high degree of N-glycosylation heterogeneity observed with the BV-Sf9 system is not due to partial glycosylation of both Asn580 and Asn592.
9126611	8	6	theme	structures	1589:1598	arg1	presence					1564:1571	the presence	1560:1571	the presence of high mannose structures, (Man)n (GlcNAc)2, n = 9, 8, 7, 6	1560:1632	N-linked oligosaccharide profiling of purified VV and BV WT and S582A mutant hCox-2 showed the presence of high mannose structures, (Man)n (GlcNAc)2, n = 9, 8, 7, 6.
9126611	10	7	theme	purified	1767:1774	arg1	hCox-2					1799:1804	purified VV WT and S582A mutant hCox-2	1767:1804	purified VV WT and S582A mutant hCox-2	1767:1804	Analysis of purified VV WT and S582A mutant hCox-2 by liquid chromatography-electrospray ionization-mass spectrometry showed an envelope of peaks separated by approximately 160 Da, corresponding to differences of a single monosaccharide.
9126611	3	8	theme	partial	554:560	arg1	N-glycosylation					562:576	the partial N-glycosylation	550:576	the partial N-glycosylation at this site in the wild-type (WT) enzyme	550:618	Removal of the N-glycosylation consensus sequence at Asn580 (N580Q and S582A mutants) resulted in the expression of protein comprising a single glycoform, consistent with the partial N-glycosylation at this site in the wild-type (WT) enzyme.
9126611	11	9	theme	wild-type	2110:2118	arg1	enzyme					2120:2125	the wild-type enzyme	2106:2125	the wild-type enzyme containing an additional high mannose oligosaccharide	2106:2179	The difference between the highest mass peaks of the two envelopes, of approximately 1500 Da, is consistent with the wild-type enzyme containing an additional high mannose oligosaccharide.
9126611	11	10	theme	mass	2028:2031	arg1	peaks					2033:2037	the highest mass peaks	2016:2037	the highest mass peaks of the two envelopes	2016:2058	The difference between the highest mass peaks of the two envelopes, of approximately 1500 Da, is consistent with the wild-type enzyme containing an additional high mannose oligosaccharide.
9126611	7	11	theme	heterogeneity	1360:1372	arg1	due					1413:1415	due	1413:1415	due	1413:1415	Expression of a double N-glycosylation site mutant in Sf9 cells, N580Q/N592Q, resulted in a decrease in glycosylation but no clear decrease in heterogeneity, indicating that the high degree of N-glycosylation heterogeneity observed with the BV-Sf9 system is not due to partial glycosylation of both Asn580 and Asn592.
9126611	7	11	theme	heterogeneity	1360:1372	arg1	degree					1334:1339	the high degree	1325:1339	the high degree of N-glycosylation heterogeneity observed with the BV-Sf9 system	1325:1404	Expression of a double N-glycosylation site mutant in Sf9 cells, N580Q/N592Q, resulted in a decrease in glycosylation but no clear decrease in heterogeneity, indicating that the high degree of N-glycosylation heterogeneity observed with the BV-Sf9 system is not due to partial glycosylation of both Asn580 and Asn592.
9126611	9	12	theme	present	1746:1752	arg1	oligosaccharides					1729:1744	oligosaccharides	1729:1744	oligosaccharides present	1729:1752	The S582A mutant was the most homogeneous with (Man)9(GlcNAc)2 comprising greater than 50% of oligosaccharides present.
9126611	4	13	theme	WT	676:677	arg1	mutant					689:694	the purified WT and N580Q mutant	663:694	the purified WT and N580Q mutant	663:694	The specific cyclooxygenase activities of the purified WT and N580Q mutant were equivalent (40 +/- 3 mumol O2/min/mg) and titrations with diclofenac showed no difference in inhibitor sensitivities of WT and both mutants.
9126611	5	14	theme	expression	857:866	arg1	Results					842:848	Results	842:848	Results of the expression of WT and N580Q hCox-2 in a Drosophila S2 cell system	842:920	Results of the expression of WT and N580Q hCox-2 in a Drosophila S2 cell system were also consistent with the N-glycosylation at this site, but low levels of activity were obtained.
9126611	11	15	theme	additional	2141:2150	arg1	oligosaccharide					2165:2179	an additional high mannose oligosaccharide	2138:2179	an additional high mannose oligosaccharide	2138:2179	The difference between the highest mass peaks of the two envelopes, of approximately 1500 Da, is consistent with the wild-type enzyme containing an additional high mannose oligosaccharide.
9126611	4	16	theme	specific	625:632	arg1	O2/min/mg					728:736	40 +/- 3 mumol O2/min/mg	713:736	40 +/- 3 mumol O2/min/mg	713:736	The specific cyclooxygenase activities of the purified WT and N580Q mutant were equivalent (40 +/- 3 mumol O2/min/mg) and titrations with diclofenac showed no difference in inhibitor sensitivities of WT and both mutants.
9126611	4	16	theme	specific	625:632	arg1	activities					649:658	The specific cyclooxygenase activities	621:658	The specific cyclooxygenase activities of the purified WT and N580Q mutant	621:694	The specific cyclooxygenase activities of the purified WT and N580Q mutant were equivalent (40 +/- 3 mumol O2/min/mg) and titrations with diclofenac showed no difference in inhibitor sensitivities of WT and both mutants.
9126611	4	16	theme	specific	625:632	arg1	equivalent					701:710	equivalent	701:710	equivalent	701:710	The specific cyclooxygenase activities of the purified WT and N580Q mutant were equivalent (40 +/- 3 mumol O2/min/mg) and titrations with diclofenac showed no difference in inhibitor sensitivities of WT and both mutants.
9126611	4	17	with	titrations	743:752	arg1	diclofenac					759:768	diclofenac	759:768	diclofenac	759:768	The specific cyclooxygenase activities of the purified WT and N580Q mutant were equivalent (40 +/- 3 mumol O2/min/mg) and titrations with diclofenac showed no difference in inhibitor sensitivities of WT and both mutants.
9126611	6	18	theme	N-glycosylation	1039:1053	arg1	heterogeneity					1055:1067	N-glycosylation heterogeneity	1039:1067	N-glycosylation heterogeneity	1039:1067	High levels of N-glycosylation heterogeneity are observed in hCox-2 expressed using recombinant baculovirus (BV) in Sf9 cells.
9126611	6	19	located	observed	1073:1080	arg1	hCox-2					1085:1090	hCox-2	1085:1090	hCox-2 expressed using recombinant baculovirus (BV) in Sf9 cells	1085:1148	High levels of N-glycosylation heterogeneity are observed in hCox-2 expressed using recombinant baculovirus (BV) in Sf9 cells.
9126611	6	19	located	observed	1073:1080	arg2	levels					1029:1034	High levels	1024:1034	High levels of N-glycosylation heterogeneity	1024:1067	High levels of N-glycosylation heterogeneity are observed in hCox-2 expressed using recombinant baculovirus (BV) in Sf9 cells.
9126611	7	20	theme	high	1329:1332	arg1	due					1413:1415	due	1413:1415	due	1413:1415	Expression of a double N-glycosylation site mutant in Sf9 cells, N580Q/N592Q, resulted in a decrease in glycosylation but no clear decrease in heterogeneity, indicating that the high degree of N-glycosylation heterogeneity observed with the BV-Sf9 system is not due to partial glycosylation of both Asn580 and Asn592.
9126611	7	20	theme	high	1329:1332	arg1	degree					1334:1339	the high degree	1325:1339	the high degree of N-glycosylation heterogeneity observed with the BV-Sf9 system	1325:1404	Expression of a double N-glycosylation site mutant in Sf9 cells, N580Q/N592Q, resulted in a decrease in glycosylation but no clear decrease in heterogeneity, indicating that the high degree of N-glycosylation heterogeneity observed with the BV-Sf9 system is not due to partial glycosylation of both Asn580 and Asn592.
9126611	10	21	theme	monosaccharide	1977:1990	arg1	differences					1953:1963	differences	1953:1963	differences of a single monosaccharide	1953:1990	Analysis of purified VV WT and S582A mutant hCox-2 by liquid chromatography-electrospray ionization-mass spectrometry showed an envelope of peaks separated by approximately 160 Da, corresponding to differences of a single monosaccharide.
9126611	10	22	theme	liquid	1809:1814	arg1	spectrometry					1860:1871	liquid chromatography-electrospray ionization-mass spectrometry	1809:1871	liquid chromatography-electrospray ionization-mass spectrometry	1809:1871	Analysis of purified VV WT and S582A mutant hCox-2 by liquid chromatography-electrospray ionization-mass spectrometry showed an envelope of peaks separated by approximately 160 Da, corresponding to differences of a single monosaccharide.
9126611	0	23	from	expression	80:89	arg1	systems					131:137	insect and mammalian cell expression systems	94:137	insect and mammalian cell expression systems	94:137	Investigation of human cyclooxygenase-2 glycosylation heterogeneity and protein expression in insect and mammalian cell expression systems.
9126611	8	24	dep	GlcNAc	1609:1614	arg1	=					1621:1621	=	1621:1621	=	1621:1621	N-linked oligosaccharide profiling of purified VV and BV WT and S582A mutant hCox-2 showed the presence of high mannose structures, (Man)n (GlcNAc)2, n = 9, 8, 7, 6.
9126611	5	25	with	consistent	932:941	arg1	N-glycosylation					952:966	the N-glycosylation	948:966	the N-glycosylation at this site	948:979	Results of the expression of WT and N580Q hCox-2 in a Drosophila S2 cell system were also consistent with the N-glycosylation at this site, but low levels of activity were obtained.
9126611	10	26	theme	hCox-2	1799:1804	arg1	Analysis					1755:1762	Analysis	1755:1762	Analysis of purified VV WT and S582A mutant hCox-2 by liquid chromatography-electrospray ionization-mass spectrometry	1755:1871	Analysis of purified VV WT and S582A mutant hCox-2 by liquid chromatography-electrospray ionization-mass spectrometry showed an envelope of peaks separated by approximately 160 Da, corresponding to differences of a single monosaccharide.
9126611	1	27	theme	Human	140:144	arg1	cyclooxygenase-2					146:161	Human cyclooxygenase-2	140:161	Human cyclooxygenase-2 (hCox-2)	140:170	Human cyclooxygenase-2 (hCox-2) is a key enzyme in the biosynthesis of prostaglandins and the target of nonsteroidal anti-inflammatory drugs.
9126611	1	27	theme	Human	140:144	arg1	enzyme					181:186	a key enzyme	175:186	a key enzyme in the biosynthesis of prostaglandins and the target of nonsteroidal anti-inflammatory drugs	175:279	Human cyclooxygenase-2 (hCox-2) is a key enzyme in the biosynthesis of prostaglandins and the target of nonsteroidal anti-inflammatory drugs.
9126611	1	27	theme	Human	140:144	arg1	hCox-2					164:169	hCox-2	164:169	hCox-2	164:169	Human cyclooxygenase-2 (hCox-2) is a key enzyme in the biosynthesis of prostaglandins and the target of nonsteroidal anti-inflammatory drugs.
9126611	5	28	theme	Drosophila	896:905	arg1	system					915:920	a Drosophila S2 cell system	894:920	a Drosophila S2 cell system	894:920	Results of the expression of WT and N580Q hCox-2 in a Drosophila S2 cell system were also consistent with the N-glycosylation at this site, but low levels of activity were obtained.
9126611	7	29	from	mutant	1195:1200	arg1	cells					1209:1213	Sf9 cells	1205:1213	Sf9 cells	1205:1213	Expression of a double N-glycosylation site mutant in Sf9 cells, N580Q/N592Q, resulted in a decrease in glycosylation but no clear decrease in heterogeneity, indicating that the high degree of N-glycosylation heterogeneity observed with the BV-Sf9 system is not due to partial glycosylation of both Asn580 and Asn592.
9126611	4	30	theme	N580Q	683:687	arg1	mutant					689:694	the purified WT and N580Q mutant	663:694	the purified WT and N580Q mutant	663:694	The specific cyclooxygenase activities of the purified WT and N580Q mutant were equivalent (40 +/- 3 mumol O2/min/mg) and titrations with diclofenac showed no difference in inhibitor sensitivities of WT and both mutants.
9126611	3	31	from	site	586:589	arg1	enzyme					613:618	the wild-type (WT) enzyme	594:618	the wild-type (WT) enzyme	594:618	Removal of the N-glycosylation consensus sequence at Asn580 (N580Q and S582A mutants) resulted in the expression of protein comprising a single glycoform, consistent with the partial N-glycosylation at this site in the wild-type (WT) enzyme.
9126611	3	31	from	site	586:589	arg1	N-glycosylation					562:576	the partial N-glycosylation	550:576	the partial N-glycosylation at this site in the wild-type (WT) enzyme	550:618	Removal of the N-glycosylation consensus sequence at Asn580 (N580Q and S582A mutants) resulted in the expression of protein comprising a single glycoform, consistent with the partial N-glycosylation at this site in the wild-type (WT) enzyme.
9126611	10	32	theme	ionization-mass	1844:1858	arg1	spectrometry					1860:1871	liquid chromatography-electrospray ionization-mass spectrometry	1809:1871	liquid chromatography-electrospray ionization-mass spectrometry	1809:1871	Analysis of purified VV WT and S582A mutant hCox-2 by liquid chromatography-electrospray ionization-mass spectrometry showed an envelope of peaks separated by approximately 160 Da, corresponding to differences of a single monosaccharide.
9126611	7	33	theme	mutant	1195:1200	arg1	Expression					1151:1160	Expression	1151:1160	Expression of a double N-glycosylation site mutant in Sf9 cells, N580Q/N592Q,	1151:1227	Expression of a double N-glycosylation site mutant in Sf9 cells, N580Q/N592Q, resulted in a decrease in glycosylation but no clear decrease in heterogeneity, indicating that the high degree of N-glycosylation heterogeneity observed with the BV-Sf9 system is not due to partial glycosylation of both Asn580 and Asn592.
9126611	5	34	from	Results	842:848	arg1	system					915:920	a Drosophila S2 cell system	894:920	a Drosophila S2 cell system	894:920	Results of the expression of WT and N580Q hCox-2 in a Drosophila S2 cell system were also consistent with the N-glycosylation at this site, but low levels of activity were obtained.
9126611	5	35	theme	WT	871:872	arg1	expression					857:866	the expression	853:866	the expression of WT and N580Q hCox-2 in a Drosophila S2 cell system	853:920	Results of the expression of WT and N580Q hCox-2 in a Drosophila S2 cell system were also consistent with the N-glycosylation at this site, but low levels of activity were obtained.
9126611	11	36	theme	envelopes	2050:2058	arg1	peaks					2033:2037	the highest mass peaks	2016:2037	the highest mass peaks of the two envelopes	2016:2058	The difference between the highest mass peaks of the two envelopes, of approximately 1500 Da, is consistent with the wild-type enzyme containing an additional high mannose oligosaccharide.
9126611	10	37	theme	peaks	1895:1899	arg1	envelope					1883:1890	an envelope	1880:1890	an envelope of peaks separated by approximately 160 Da	1880:1933	Analysis of purified VV WT and S582A mutant hCox-2 by liquid chromatography-electrospray ionization-mass spectrometry showed an envelope of peaks separated by approximately 160 Da, corresponding to differences of a single monosaccharide.
9126611	0	38	theme	insect	94:99	arg1	systems					131:137	insect and mammalian cell expression systems	94:137	insect and mammalian cell expression systems	94:137	Investigation of human cyclooxygenase-2 glycosylation heterogeneity and protein expression in insect and mammalian cell expression systems.
9126611	3	39	from	Asn580	432:437	arg1	sequence					420:427	the N-glycosylation consensus sequence	390:427	the N-glycosylation consensus sequence at Asn580 (N580Q and S582A mutants)	390:463	Removal of the N-glycosylation consensus sequence at Asn580 (N580Q and S582A mutants) resulted in the expression of protein comprising a single glycoform, consistent with the partial N-glycosylation at this site in the wild-type (WT) enzyme.
9126611	3	39	from	Asn580	432:437	arg1	Removal					379:385	Removal	379:385	Removal of the N-glycosylation consensus sequence at Asn580 (N580Q and S582A mutants)	379:463	Removal of the N-glycosylation consensus sequence at Asn580 (N580Q and S582A mutants) resulted in the expression of protein comprising a single glycoform, consistent with the partial N-glycosylation at this site in the wild-type (WT) enzyme.
9126611	5	40	theme	N580Q	878:882	arg1	hCox-2					884:889	N580Q hCox-2	878:889	N580Q hCox-2	878:889	Results of the expression of WT and N580Q hCox-2 in a Drosophila S2 cell system were also consistent with the N-glycosylation at this site, but low levels of activity were obtained.
9126611	0	41	from	Investigation	0:12	arg1	systems					131:137	insect and mammalian cell expression systems	94:137	insect and mammalian cell expression systems	94:137	Investigation of human cyclooxygenase-2 glycosylation heterogeneity and protein expression in insect and mammalian cell expression systems.
9126611	0	42	theme	mammalian	105:113	arg1	systems					131:137	insect and mammalian cell expression systems	94:137	insect and mammalian cell expression systems	94:137	Investigation of human cyclooxygenase-2 glycosylation heterogeneity and protein expression in insect and mammalian cell expression systems.
9126611	8	43	theme	N-linked	1469:1476	arg1	profiling					1494:1502	N-linked oligosaccharide profiling	1469:1502	N-linked oligosaccharide profiling of purified VV and BV WT and S582A mutant hCox-2	1469:1551	N-linked oligosaccharide profiling of purified VV and BV WT and S582A mutant hCox-2 showed the presence of high mannose structures, (Man)n (GlcNAc)2, n = 9, 8, 7, 6.
9126611	0	44	theme	expression	120:129	arg1	systems					131:137	insect and mammalian cell expression systems	94:137	insect and mammalian cell expression systems	94:137	Investigation of human cyclooxygenase-2 glycosylation heterogeneity and protein expression in insect and mammalian cell expression systems.
9126611	0	45	theme	heterogeneity	54:66	arg1	Investigation					0:12	Investigation	0:12	Investigation of human cyclooxygenase-2 glycosylation heterogeneity	0:66	Investigation of human cyclooxygenase-2 glycosylation heterogeneity and protein expression in insect and mammalian cell expression systems.
9126611	0	45	theme	heterogeneity	54:66	arg1	expression					80:89	protein expression	72:89	protein expression in insect and mammalian cell expression systems	72:137	Investigation of human cyclooxygenase-2 glycosylation heterogeneity and protein expression in insect and mammalian cell expression systems.
9126611	3	46	theme	N-glycosylation	394:408	arg1	sequence					420:427	the N-glycosylation consensus sequence	390:427	the N-glycosylation consensus sequence at Asn580 (N580Q and S582A mutants)	390:463	Removal of the N-glycosylation consensus sequence at Asn580 (N580Q and S582A mutants) resulted in the expression of protein comprising a single glycoform, consistent with the partial N-glycosylation at this site in the wild-type (WT) enzyme.
9126611	3	47	dep	Asn580	432:437	arg1	S582A					450:454	S582A	450:454	S582A	450:454	Removal of the N-glycosylation consensus sequence at Asn580 (N580Q and S582A mutants) resulted in the expression of protein comprising a single glycoform, consistent with the partial N-glycosylation at this site in the wild-type (WT) enzyme.
9126611	3	47	dep	Asn580	432:437	arg1	N580Q					440:444	N580Q	440:444	N580Q	440:444	Removal of the N-glycosylation consensus sequence at Asn580 (N580Q and S582A mutants) resulted in the expression of protein comprising a single glycoform, consistent with the partial N-glycosylation at this site in the wild-type (WT) enzyme.
9126611	4	48	theme	mumol	722:726	arg1	O2/min/mg					728:736	40 +/- 3 mumol O2/min/mg	713:736	40 +/- 3 mumol O2/min/mg	713:736	The specific cyclooxygenase activities of the purified WT and N580Q mutant were equivalent (40 +/- 3 mumol O2/min/mg) and titrations with diclofenac showed no difference in inhibitor sensitivities of WT and both mutants.
9126611	4	48	theme	mumol	722:726	arg1	activities					649:658	The specific cyclooxygenase activities	621:658	The specific cyclooxygenase activities of the purified WT and N580Q mutant	621:694	The specific cyclooxygenase activities of the purified WT and N580Q mutant were equivalent (40 +/- 3 mumol O2/min/mg) and titrations with diclofenac showed no difference in inhibitor sensitivities of WT and both mutants.
9126611	4	48	theme	mumol	722:726	arg1	equivalent					701:710	equivalent	701:710	equivalent	701:710	The specific cyclooxygenase activities of the purified WT and N580Q mutant were equivalent (40 +/- 3 mumol O2/min/mg) and titrations with diclofenac showed no difference in inhibitor sensitivities of WT and both mutants.
9126611	5	49	theme	cell	910:913	arg1	system					915:920	a Drosophila S2 cell system	894:920	a Drosophila S2 cell system	894:920	Results of the expression of WT and N580Q hCox-2 in a Drosophila S2 cell system were also consistent with the N-glycosylation at this site, but low levels of activity were obtained.
9126611	8	50	theme	purified	1507:1514	arg1	VV					1516:1517	purified VV and BV WT and S582A mutant hCox-2	1507:1551	VV	1516:1517	N-linked oligosaccharide profiling of purified VV and BV WT and S582A mutant hCox-2 showed the presence of high mannose structures, (Man)n (GlcNAc)2, n = 9, 8, 7, 6.
9126611	7	51	gly	N-glycosylation	1174:1188	arg2	mutant					1195:1200	a double N-glycosylation site mutant	1165:1200	a double N-glycosylation site mutant in Sf9 cells	1165:1213	Expression of a double N-glycosylation site mutant in Sf9 cells, N580Q/N592Q, resulted in a decrease in glycosylation but no clear decrease in heterogeneity, indicating that the high degree of N-glycosylation heterogeneity observed with the BV-Sf9 system is not due to partial glycosylation of both Asn580 and Asn592.
9126611	7	51	gly	N-glycosylation	1174:1188	arg2	site					1190:1193	a double N-glycosylation site mutant	1165:1200	a double N-glycosylation site mutant in Sf9 cells	1165:1213	Expression of a double N-glycosylation site mutant in Sf9 cells, N580Q/N592Q, resulted in a decrease in glycosylation but no clear decrease in heterogeneity, indicating that the high degree of N-glycosylation heterogeneity observed with the BV-Sf9 system is not due to partial glycosylation of both Asn580 and Asn592.
9126611	7	51	gly	N-glycosylation	1174:1188	arg2	N580Q/N592Q					1216:1226	N580Q/N592Q	1216:1226	N580Q/N592Q	1216:1226	Expression of a double N-glycosylation site mutant in Sf9 cells, N580Q/N592Q, resulted in a decrease in glycosylation but no clear decrease in heterogeneity, indicating that the high degree of N-glycosylation heterogeneity observed with the BV-Sf9 system is not due to partial glycosylation of both Asn580 and Asn592.
9126611	0	52	theme	human	17:21	arg1	heterogeneity					54:66	human cyclooxygenase-2 glycosylation heterogeneity	17:66	human cyclooxygenase-2 glycosylation heterogeneity	17:66	Investigation of human cyclooxygenase-2 glycosylation heterogeneity and protein expression in insect and mammalian cell expression systems.
9126611	4	53	dep	equivalent	701:710	arg1	O2/min/mg					728:736	40 +/- 3 mumol O2/min/mg	713:736	40 +/- 3 mumol O2/min/mg	713:736	The specific cyclooxygenase activities of the purified WT and N580Q mutant were equivalent (40 +/- 3 mumol O2/min/mg) and titrations with diclofenac showed no difference in inhibitor sensitivities of WT and both mutants.
9126611	4	53	dep	equivalent	701:710	arg1	activities					649:658	The specific cyclooxygenase activities	621:658	The specific cyclooxygenase activities of the purified WT and N580Q mutant	621:694	The specific cyclooxygenase activities of the purified WT and N580Q mutant were equivalent (40 +/- 3 mumol O2/min/mg) and titrations with diclofenac showed no difference in inhibitor sensitivities of WT and both mutants.
9126611	4	53	dep	equivalent	701:710	arg1	equivalent					701:710	equivalent	701:710	equivalent	701:710	The specific cyclooxygenase activities of the purified WT and N580Q mutant were equivalent (40 +/- 3 mumol O2/min/mg) and titrations with diclofenac showed no difference in inhibitor sensitivities of WT and both mutants.
9126611	7	54	gly	glycosylation	1428:1440	arg1	Asn592					1461:1466	Asn592	1461:1466	Asn592	1461:1466	Expression of a double N-glycosylation site mutant in Sf9 cells, N580Q/N592Q, resulted in a decrease in glycosylation but no clear decrease in heterogeneity, indicating that the high degree of N-glycosylation heterogeneity observed with the BV-Sf9 system is not due to partial glycosylation of both Asn580 and Asn592.
9126611	7	54	gly	glycosylation	1428:1440	arg1	Asn580					1450:1455	Asn580	1450:1455	Asn580	1450:1455	Expression of a double N-glycosylation site mutant in Sf9 cells, N580Q/N592Q, resulted in a decrease in glycosylation but no clear decrease in heterogeneity, indicating that the high degree of N-glycosylation heterogeneity observed with the BV-Sf9 system is not due to partial glycosylation of both Asn580 and Asn592.
9126611	0	55	theme	glycosylation	40:52	arg1	heterogeneity					54:66	human cyclooxygenase-2 glycosylation heterogeneity	17:66	human cyclooxygenase-2 glycosylation heterogeneity	17:66	Investigation of human cyclooxygenase-2 glycosylation heterogeneity and protein expression in insect and mammalian cell expression systems.
9126611	9	56	theme	Man	1683:1685	arg1	GlcNAc					1689:1694	(Man)9(GlcNAc)2	1682:1696	(Man)9(GlcNAc)2 comprising greater than 50% of oligosaccharides present	1682:1752	The S582A mutant was the most homogeneous with (Man)9(GlcNAc)2 comprising greater than 50% of oligosaccharides present.
9126611	3	57	theme	sequence	420:427	arg1	Removal					379:385	Removal	379:385	Removal of the N-glycosylation consensus sequence at Asn580 (N580Q and S582A mutants)	379:463	Removal of the N-glycosylation consensus sequence at Asn580 (N580Q and S582A mutants) resulted in the expression of protein comprising a single glycoform, consistent with the partial N-glycosylation at this site in the wild-type (WT) enzyme.
9126611	8	58	theme	WT	1526:1527	arg1	profiling					1494:1502	N-linked oligosaccharide profiling	1469:1502	N-linked oligosaccharide profiling of purified VV and BV WT and S582A mutant hCox-2	1469:1551	N-linked oligosaccharide profiling of purified VV and BV WT and S582A mutant hCox-2 showed the presence of high mannose structures, (Man)n (GlcNAc)2, n = 9, 8, 7, 6.
9126611	4	59	theme	WT	821:822	arg1	sensitivities					804:816	inhibitor sensitivities	794:816	inhibitor sensitivities of WT and both mutants	794:839	The specific cyclooxygenase activities of the purified WT and N580Q mutant were equivalent (40 +/- 3 mumol O2/min/mg) and titrations with diclofenac showed no difference in inhibitor sensitivities of WT and both mutants.
9126611	3	60	theme	protein	495:501	arg1	expression					481:490	the expression	477:490	the expression of protein comprising a single glycoform	477:531	Removal of the N-glycosylation consensus sequence at Asn580 (N580Q and S582A mutants) resulted in the expression of protein comprising a single glycoform, consistent with the partial N-glycosylation at this site in the wild-type (WT) enzyme.
9126611	7	61	theme	Asn592	1461:1466	arg1	glycosylation					1428:1440	partial glycosylation	1420:1440	partial glycosylation of both Asn580 and Asn592	1420:1466	Expression of a double N-glycosylation site mutant in Sf9 cells, N580Q/N592Q, resulted in a decrease in glycosylation but no clear decrease in heterogeneity, indicating that the high degree of N-glycosylation heterogeneity observed with the BV-Sf9 system is not due to partial glycosylation of both Asn580 and Asn592.
9126611	8	62	theme	S582A	1533:1537	arg1	hCox-2					1546:1551	purified VV and BV WT and S582A mutant hCox-2	1507:1551	hCox-2	1546:1551	N-linked oligosaccharide profiling of purified VV and BV WT and S582A mutant hCox-2 showed the presence of high mannose structures, (Man)n (GlcNAc)2, n = 9, 8, 7, 6.
9126611	2	63	theme	-COS-7	339:344	arg1	system					346:351	a vaccinia virus (VV)-COS-7 system	318:351	a vaccinia virus (VV)-COS-7 system	318:351	Recombinant hCox-2 overexpressed in a vaccinia virus (VV)-COS-7 system comprises two glycoforms.
9126611	7	64	theme	Asn580	1450:1455	arg1	glycosylation					1428:1440	partial glycosylation	1420:1440	partial glycosylation of both Asn580 and Asn592	1420:1466	Expression of a double N-glycosylation site mutant in Sf9 cells, N580Q/N592Q, resulted in a decrease in glycosylation but no clear decrease in heterogeneity, indicating that the high degree of N-glycosylation heterogeneity observed with the BV-Sf9 system is not due to partial glycosylation of both Asn580 and Asn592.
9126611	11	65	theme	high	2152:2155	arg1	oligosaccharide					2165:2179	an additional high mannose oligosaccharide	2138:2179	an additional high mannose oligosaccharide	2138:2179	The difference between the highest mass peaks of the two envelopes, of approximately 1500 Da, is consistent with the wild-type enzyme containing an additional high mannose oligosaccharide.
9126611	8	66	theme	hCox-2	1546:1551	arg1	profiling					1494:1502	N-linked oligosaccharide profiling	1469:1502	N-linked oligosaccharide profiling of purified VV and BV WT and S582A mutant hCox-2	1469:1551	N-linked oligosaccharide profiling of purified VV and BV WT and S582A mutant hCox-2 showed the presence of high mannose structures, (Man)n (GlcNAc)2, n = 9, 8, 7, 6.
9126611	8	67	theme	Man	1602:1604	arg1	GlcNAc					1609:1614	(Man)n (GlcNAc)2	1601:1616	(Man)n (GlcNAc)2	1601:1616	N-linked oligosaccharide profiling of purified VV and BV WT and S582A mutant hCox-2 showed the presence of high mannose structures, (Man)n (GlcNAc)2, n = 9, 8, 7, 6.
9126611	8	67	theme	Man	1602:1604	arg1	structures					1589:1598	high mannose structures	1576:1598	high mannose structures	1576:1598	N-linked oligosaccharide profiling of purified VV and BV WT and S582A mutant hCox-2 showed the presence of high mannose structures, (Man)n (GlcNAc)2, n = 9, 8, 7, 6.
9126611	6	68	theme	recombinant	1108:1118	arg1	BV					1133:1134	BV	1133:1134	BV	1133:1134	High levels of N-glycosylation heterogeneity are observed in hCox-2 expressed using recombinant baculovirus (BV) in Sf9 cells.
9126611	6	68	theme	recombinant	1108:1118	arg1	baculovirus					1120:1130	recombinant baculovirus	1108:1130	recombinant baculovirus (BV) in Sf9 cells	1108:1148	High levels of N-glycosylation heterogeneity are observed in hCox-2 expressed using recombinant baculovirus (BV) in Sf9 cells.
9126611	8	69	theme	n	1606:1606	arg1	GlcNAc					1609:1614	(Man)n (GlcNAc)2	1601:1616	(Man)n (GlcNAc)2	1601:1616	N-linked oligosaccharide profiling of purified VV and BV WT and S582A mutant hCox-2 showed the presence of high mannose structures, (Man)n (GlcNAc)2, n = 9, 8, 7, 6.
9126611	8	69	theme	n	1606:1606	arg1	structures					1589:1598	high mannose structures	1576:1598	high mannose structures	1576:1598	N-linked oligosaccharide profiling of purified VV and BV WT and S582A mutant hCox-2 showed the presence of high mannose structures, (Man)n (GlcNAc)2, n = 9, 8, 7, 6.
9126611	1	70	theme	anti-inflammatory	257:273	arg1	drugs					275:279	nonsteroidal anti-inflammatory drugs	244:279	nonsteroidal anti-inflammatory drugs	244:279	Human cyclooxygenase-2 (hCox-2) is a key enzyme in the biosynthesis of prostaglandins and the target of nonsteroidal anti-inflammatory drugs.
9126611	7	71	theme	partial	1420:1426	arg1	glycosylation					1428:1440	partial glycosylation	1420:1440	partial glycosylation of both Asn580 and Asn592	1420:1466	Expression of a double N-glycosylation site mutant in Sf9 cells, N580Q/N592Q, resulted in a decrease in glycosylation but no clear decrease in heterogeneity, indicating that the high degree of N-glycosylation heterogeneity observed with the BV-Sf9 system is not due to partial glycosylation of both Asn580 and Asn592.
9126611	7	72	theme	Sf9	1205:1207	arg1	cells					1209:1213	Sf9 cells	1205:1213	Sf9 cells	1205:1213	Expression of a double N-glycosylation site mutant in Sf9 cells, N580Q/N592Q, resulted in a decrease in glycosylation but no clear decrease in heterogeneity, indicating that the high degree of N-glycosylation heterogeneity observed with the BV-Sf9 system is not due to partial glycosylation of both Asn580 and Asn592.
9126611	7	73	from	cells	1209:1213	arg1	Expression					1151:1160	Expression	1151:1160	Expression of a double N-glycosylation site mutant in Sf9 cells, N580Q/N592Q,	1151:1227	Expression of a double N-glycosylation site mutant in Sf9 cells, N580Q/N592Q, resulted in a decrease in glycosylation but no clear decrease in heterogeneity, indicating that the high degree of N-glycosylation heterogeneity observed with the BV-Sf9 system is not due to partial glycosylation of both Asn580 and Asn592.
9126611	6	74	theme	Sf9	1140:1142	arg1	cells					1144:1148	Sf9 cells	1140:1148	Sf9 cells	1140:1148	High levels of N-glycosylation heterogeneity are observed in hCox-2 expressed using recombinant baculovirus (BV) in Sf9 cells.
9126611	10	75	theme	single	1970:1975	arg1	monosaccharide					1977:1990	a single monosaccharide	1968:1990	a single monosaccharide	1968:1990	Analysis of purified VV WT and S582A mutant hCox-2 by liquid chromatography-electrospray ionization-mass spectrometry showed an envelope of peaks separated by approximately 160 Da, corresponding to differences of a single monosaccharide.
9126611	8	76	theme	mannose	1581:1587	arg1	GlcNAc					1609:1614	(Man)n (GlcNAc)2	1601:1616	(Man)n (GlcNAc)2	1601:1616	N-linked oligosaccharide profiling of purified VV and BV WT and S582A mutant hCox-2 showed the presence of high mannose structures, (Man)n (GlcNAc)2, n = 9, 8, 7, 6.
9126611	8	76	theme	mannose	1581:1587	arg1	structures					1589:1598	high mannose structures	1576:1598	high mannose structures	1576:1598	N-linked oligosaccharide profiling of purified VV and BV WT and S582A mutant hCox-2 showed the presence of high mannose structures, (Man)n (GlcNAc)2, n = 9, 8, 7, 6.
9126611	5	77	from	site	976:979	arg1	N-glycosylation					952:966	the N-glycosylation	948:966	the N-glycosylation at this site	948:979	Results of the expression of WT and N580Q hCox-2 in a Drosophila S2 cell system were also consistent with the N-glycosylation at this site, but low levels of activity were obtained.
9126611	1	78	theme	key	177:179	arg1	cyclooxygenase-2					146:161	Human cyclooxygenase-2	140:161	Human cyclooxygenase-2 (hCox-2)	140:170	Human cyclooxygenase-2 (hCox-2) is a key enzyme in the biosynthesis of prostaglandins and the target of nonsteroidal anti-inflammatory drugs.
9126611	1	78	theme	key	177:179	arg1	enzyme					181:186	a key enzyme	175:186	a key enzyme in the biosynthesis of prostaglandins and the target of nonsteroidal anti-inflammatory drugs	175:279	Human cyclooxygenase-2 (hCox-2) is a key enzyme in the biosynthesis of prostaglandins and the target of nonsteroidal anti-inflammatory drugs.
9126611	9	79	theme	oligosaccharides	1729:1744	arg1	oligosaccharides					1729:1744	oligosaccharides	1729:1744	oligosaccharides present	1729:1752	The S582A mutant was the most homogeneous with (Man)9(GlcNAc)2 comprising greater than 50% of oligosaccharides present.
9126611	9	79	theme	oligosaccharides	1729:1744	arg1	%					1724:1724	greater than 50%	1709:1724	greater than 50% of oligosaccharides present	1709:1752	The S582A mutant was the most homogeneous with (Man)9(GlcNAc)2 comprising greater than 50% of oligosaccharides present.
9126611	7	80	theme	N-glycosylation	1174:1188	arg1	N580Q/N592Q					1216:1226	N580Q/N592Q	1216:1226	N580Q/N592Q	1216:1226	Expression of a double N-glycosylation site mutant in Sf9 cells, N580Q/N592Q, resulted in a decrease in glycosylation but no clear decrease in heterogeneity, indicating that the high degree of N-glycosylation heterogeneity observed with the BV-Sf9 system is not due to partial glycosylation of both Asn580 and Asn592.
9126611	7	80	theme	N-glycosylation	1174:1188	arg1	mutant					1195:1200	a double N-glycosylation site mutant	1165:1200	a double N-glycosylation site mutant in Sf9 cells	1165:1213	Expression of a double N-glycosylation site mutant in Sf9 cells, N580Q/N592Q, resulted in a decrease in glycosylation but no clear decrease in heterogeneity, indicating that the high degree of N-glycosylation heterogeneity observed with the BV-Sf9 system is not due to partial glycosylation of both Asn580 and Asn592.
9126611	9	81	with	homogeneous	1665:1675	arg1	GlcNAc					1689:1694	(Man)9(GlcNAc)2	1682:1696	(Man)9(GlcNAc)2 comprising greater than 50% of oligosaccharides present	1682:1752	The S582A mutant was the most homogeneous with (Man)9(GlcNAc)2 comprising greater than 50% of oligosaccharides present.
9126611	3	82	dep	wild-type	598:606	arg1	WT					609:610	WT	609:610	WT	609:610	Removal of the N-glycosylation consensus sequence at Asn580 (N580Q and S582A mutants) resulted in the expression of protein comprising a single glycoform, consistent with the partial N-glycosylation at this site in the wild-type (WT) enzyme.
9126611	4	83	theme	mutants	833:839	arg1	sensitivities					804:816	inhibitor sensitivities	794:816	inhibitor sensitivities of WT and both mutants	794:839	The specific cyclooxygenase activities of the purified WT and N580Q mutant were equivalent (40 +/- 3 mumol O2/min/mg) and titrations with diclofenac showed no difference in inhibitor sensitivities of WT and both mutants.
9126611	11	84	with	consistent	2090:2099	arg1	enzyme					2120:2125	the wild-type enzyme	2106:2125	the wild-type enzyme containing an additional high mannose oligosaccharide	2106:2179	The difference between the highest mass peaks of the two envelopes, of approximately 1500 Da, is consistent with the wild-type enzyme containing an additional high mannose oligosaccharide.
9126611	4	85	theme	purified	667:674	arg1	mutant					689:694	the purified WT and N580Q mutant	663:694	the purified WT and N580Q mutant	663:694	The specific cyclooxygenase activities of the purified WT and N580Q mutant were equivalent (40 +/- 3 mumol O2/min/mg) and titrations with diclofenac showed no difference in inhibitor sensitivities of WT and both mutants.
9126611	2	86	theme	virus	329:333	arg1	system					346:351	a vaccinia virus (VV)-COS-7 system	318:351	a vaccinia virus (VV)-COS-7 system	318:351	Recombinant hCox-2 overexpressed in a vaccinia virus (VV)-COS-7 system comprises two glycoforms.
9126611	7	87	theme	N-glycosylation	1344:1358	arg1	heterogeneity					1360:1372	N-glycosylation heterogeneity	1344:1372	N-glycosylation heterogeneity observed with the BV-Sf9 system	1344:1404	Expression of a double N-glycosylation site mutant in Sf9 cells, N580Q/N592Q, resulted in a decrease in glycosylation but no clear decrease in heterogeneity, indicating that the high degree of N-glycosylation heterogeneity observed with the BV-Sf9 system is not due to partial glycosylation of both Asn580 and Asn592.
9126611	10	88	theme	VV	1776:1777	arg1	hCox-2					1799:1804	purified VV WT and S582A mutant hCox-2	1767:1804	purified VV WT and S582A mutant hCox-2	1767:1804	Analysis of purified VV WT and S582A mutant hCox-2 by liquid chromatography-electrospray ionization-mass spectrometry showed an envelope of peaks separated by approximately 160 Da, corresponding to differences of a single monosaccharide.
9126611	3	89	theme	wild-type	598:606	arg1	enzyme					613:618	the wild-type (WT) enzyme	594:618	the wild-type (WT) enzyme	594:618	Removal of the N-glycosylation consensus sequence at Asn580 (N580Q and S582A mutants) resulted in the expression of protein comprising a single glycoform, consistent with the partial N-glycosylation at this site in the wild-type (WT) enzyme.
9126611	1	90	theme	prostaglandins	211:224	arg1	target					234:239	the target	230:239	the target of nonsteroidal anti-inflammatory drugs	230:279	Human cyclooxygenase-2 (hCox-2) is a key enzyme in the biosynthesis of prostaglandins and the target of nonsteroidal anti-inflammatory drugs.
9126611	1	90	theme	prostaglandins	211:224	arg1	biosynthesis					195:206	the biosynthesis	191:206	the biosynthesis of prostaglandins	191:224	Human cyclooxygenase-2 (hCox-2) is a key enzyme in the biosynthesis of prostaglandins and the target of nonsteroidal anti-inflammatory drugs.
9126611	4	91	theme	cyclooxygenase	634:647	arg1	O2/min/mg					728:736	40 +/- 3 mumol O2/min/mg	713:736	40 +/- 3 mumol O2/min/mg	713:736	The specific cyclooxygenase activities of the purified WT and N580Q mutant were equivalent (40 +/- 3 mumol O2/min/mg) and titrations with diclofenac showed no difference in inhibitor sensitivities of WT and both mutants.
9126611	4	91	theme	cyclooxygenase	634:647	arg1	activities					649:658	The specific cyclooxygenase activities	621:658	The specific cyclooxygenase activities of the purified WT and N580Q mutant	621:694	The specific cyclooxygenase activities of the purified WT and N580Q mutant were equivalent (40 +/- 3 mumol O2/min/mg) and titrations with diclofenac showed no difference in inhibitor sensitivities of WT and both mutants.
9126611	4	91	theme	cyclooxygenase	634:647	arg1	equivalent					701:710	equivalent	701:710	equivalent	701:710	The specific cyclooxygenase activities of the purified WT and N580Q mutant were equivalent (40 +/- 3 mumol O2/min/mg) and titrations with diclofenac showed no difference in inhibitor sensitivities of WT and both mutants.
9126611	3	92	from	Removal	379:385	arg1	Asn580					432:437	Asn580	432:437	Asn580 (N580Q and S582A mutants)	432:463	Removal of the N-glycosylation consensus sequence at Asn580 (N580Q and S582A mutants) resulted in the expression of protein comprising a single glycoform, consistent with the partial N-glycosylation at this site in the wild-type (WT) enzyme.
9126611	5	93	theme	hCox-2	884:889	arg1	expression					857:866	the expression	853:866	the expression of WT and N580Q hCox-2 in a Drosophila S2 cell system	853:920	Results of the expression of WT and N580Q hCox-2 in a Drosophila S2 cell system were also consistent with the N-glycosylation at this site, but low levels of activity were obtained.
9126611	10	94	theme	mutant	1792:1797	arg1	hCox-2					1799:1804	purified VV WT and S582A mutant hCox-2	1767:1804	purified VV WT and S582A mutant hCox-2	1767:1804	Analysis of purified VV WT and S582A mutant hCox-2 by liquid chromatography-electrospray ionization-mass spectrometry showed an envelope of peaks separated by approximately 160 Da, corresponding to differences of a single monosaccharide.
9126611	5	95	theme	activity	1000:1007	arg1	levels					990:995	low levels	986:995	low levels of activity	986:1007	Results of the expression of WT and N580Q hCox-2 in a Drosophila S2 cell system were also consistent with the N-glycosylation at this site, but low levels of activity were obtained.
9126611	2	96	theme	Recombinant	282:292	arg1	hCox-2					294:299	Recombinant hCox-2	282:299	Recombinant hCox-2 overexpressed in a vaccinia virus (VV)-COS-7 system	282:351	Recombinant hCox-2 overexpressed in a vaccinia virus (VV)-COS-7 system comprises two glycoforms.
9126611	8	97	link	N-linked	1469:1476	arg1	profiling					1494:1502	N-linked oligosaccharide profiling	1469:1502	N-linked oligosaccharide profiling of purified VV and BV WT and S582A mutant hCox-2	1469:1551	N-linked oligosaccharide profiling of purified VV and BV WT and S582A mutant hCox-2 showed the presence of high mannose structures, (Man)n (GlcNAc)2, n = 9, 8, 7, 6.
9126611	3	98	gly	N-glycosylation	562:576	arg2	site					586:589	this site	581:589	this site in the wild-type (WT) enzyme	581:618	Removal of the N-glycosylation consensus sequence at Asn580 (N580Q and S582A mutants) resulted in the expression of protein comprising a single glycoform, consistent with the partial N-glycosylation at this site in the wild-type (WT) enzyme.
9126611	3	98	gly	N-glycosylation	562:576	arg1	site					586:589	this site	581:589	this site in the wild-type (WT) enzyme	581:618	Removal of the N-glycosylation consensus sequence at Asn580 (N580Q and S582A mutants) resulted in the expression of protein comprising a single glycoform, consistent with the partial N-glycosylation at this site in the wild-type (WT) enzyme.
9126611	7	99	theme	site	1190:1193	arg1	N580Q/N592Q					1216:1226	N580Q/N592Q	1216:1226	N580Q/N592Q	1216:1226	Expression of a double N-glycosylation site mutant in Sf9 cells, N580Q/N592Q, resulted in a decrease in glycosylation but no clear decrease in heterogeneity, indicating that the high degree of N-glycosylation heterogeneity observed with the BV-Sf9 system is not due to partial glycosylation of both Asn580 and Asn592.
9126611	7	99	theme	site	1190:1193	arg1	mutant					1195:1200	a double N-glycosylation site mutant	1165:1200	a double N-glycosylation site mutant in Sf9 cells	1165:1213	Expression of a double N-glycosylation site mutant in Sf9 cells, N580Q/N592Q, resulted in a decrease in glycosylation but no clear decrease in heterogeneity, indicating that the high degree of N-glycosylation heterogeneity observed with the BV-Sf9 system is not due to partial glycosylation of both Asn580 and Asn592.
9126611	5	100	from	expression	857:866	arg1	system					915:920	a Drosophila S2 cell system	894:920	a Drosophila S2 cell system	894:920	Results of the expression of WT and N580Q hCox-2 in a Drosophila S2 cell system were also consistent with the N-glycosylation at this site, but low levels of activity were obtained.
9126611	11	101	contain	containing	2127:2136	arg1	enzyme					2120:2125	the wild-type enzyme	2106:2125	the wild-type enzyme containing an additional high mannose oligosaccharide	2106:2179	The difference between the highest mass peaks of the two envelopes, of approximately 1500 Da, is consistent with the wild-type enzyme containing an additional high mannose oligosaccharide.
9126611	11	101	contain	containing	2127:2136	arg2	oligosaccharide					2165:2179	an additional high mannose oligosaccharide	2138:2179	an additional high mannose oligosaccharide	2138:2179	The difference between the highest mass peaks of the two envelopes, of approximately 1500 Da, is consistent with the wild-type enzyme containing an additional high mannose oligosaccharide.
9126611	10	102	theme	chromatography-electrospray	1816:1842	arg1	spectrometry					1860:1871	liquid chromatography-electrospray ionization-mass spectrometry	1809:1871	liquid chromatography-electrospray ionization-mass spectrometry	1809:1871	Analysis of purified VV WT and S582A mutant hCox-2 by liquid chromatography-electrospray ionization-mass spectrometry showed an envelope of peaks separated by approximately 160 Da, corresponding to differences of a single monosaccharide.
9126611	7	103	theme	double	1167:1172	arg1	N580Q/N592Q					1216:1226	N580Q/N592Q	1216:1226	N580Q/N592Q	1216:1226	Expression of a double N-glycosylation site mutant in Sf9 cells, N580Q/N592Q, resulted in a decrease in glycosylation but no clear decrease in heterogeneity, indicating that the high degree of N-glycosylation heterogeneity observed with the BV-Sf9 system is not due to partial glycosylation of both Asn580 and Asn592.
9126611	7	103	theme	double	1167:1172	arg1	mutant					1195:1200	a double N-glycosylation site mutant	1165:1200	a double N-glycosylation site mutant in Sf9 cells	1165:1213	Expression of a double N-glycosylation site mutant in Sf9 cells, N580Q/N592Q, resulted in a decrease in glycosylation but no clear decrease in heterogeneity, indicating that the high degree of N-glycosylation heterogeneity observed with the BV-Sf9 system is not due to partial glycosylation of both Asn580 and Asn592.
9126611	10	104	theme	WT	1779:1780	arg1	hCox-2					1799:1804	purified VV WT and S582A mutant hCox-2	1767:1804	purified VV WT and S582A mutant hCox-2	1767:1804	Analysis of purified VV WT and S582A mutant hCox-2 by liquid chromatography-electrospray ionization-mass spectrometry showed an envelope of peaks separated by approximately 160 Da, corresponding to differences of a single monosaccharide.
9126611	1	105	from	enzyme	181:186	arg1	target					234:239	the target	230:239	the target of nonsteroidal anti-inflammatory drugs	230:279	Human cyclooxygenase-2 (hCox-2) is a key enzyme in the biosynthesis of prostaglandins and the target of nonsteroidal anti-inflammatory drugs.
9126611	1	105	from	enzyme	181:186	arg1	biosynthesis					195:206	the biosynthesis	191:206	the biosynthesis of prostaglandins	191:224	Human cyclooxygenase-2 (hCox-2) is a key enzyme in the biosynthesis of prostaglandins and the target of nonsteroidal anti-inflammatory drugs.
9126611	4	106	theme	mutant	689:694	arg1	O2/min/mg					728:736	40 +/- 3 mumol O2/min/mg	713:736	40 +/- 3 mumol O2/min/mg	713:736	The specific cyclooxygenase activities of the purified WT and N580Q mutant were equivalent (40 +/- 3 mumol O2/min/mg) and titrations with diclofenac showed no difference in inhibitor sensitivities of WT and both mutants.
9126611	4	106	theme	mutant	689:694	arg1	activities					649:658	The specific cyclooxygenase activities	621:658	The specific cyclooxygenase activities of the purified WT and N580Q mutant	621:694	The specific cyclooxygenase activities of the purified WT and N580Q mutant were equivalent (40 +/- 3 mumol O2/min/mg) and titrations with diclofenac showed no difference in inhibitor sensitivities of WT and both mutants.
9126611	4	106	theme	mutant	689:694	arg1	equivalent					701:710	equivalent	701:710	equivalent	701:710	The specific cyclooxygenase activities of the purified WT and N580Q mutant were equivalent (40 +/- 3 mumol O2/min/mg) and titrations with diclofenac showed no difference in inhibitor sensitivities of WT and both mutants.
9126611	0	107	theme	cell	115:118	arg1	systems					131:137	insect and mammalian cell expression systems	94:137	insect and mammalian cell expression systems	94:137	Investigation of human cyclooxygenase-2 glycosylation heterogeneity and protein expression in insect and mammalian cell expression systems.
9126611	2	108	theme	vaccinia	320:327	arg1	virus					329:333	vaccinia virus	320:333	a vaccinia virus (VV)-COS-7 system	318:351	Recombinant hCox-2 overexpressed in a vaccinia virus (VV)-COS-7 system comprises two glycoforms.
9126611	2	108	theme	vaccinia	320:327	arg1	VV					336:337	VV	336:337	VV	336:337	Recombinant hCox-2 overexpressed in a vaccinia virus (VV)-COS-7 system comprises two glycoforms.
9126611	9	109	theme	S582A	1639:1643	arg1	homogeneous					1665:1675	homogeneous	1665:1675	homogeneous	1665:1675	The S582A mutant was the most homogeneous with (Man)9(GlcNAc)2 comprising greater than 50% of oligosaccharides present.
9126611	9	109	theme	S582A	1639:1643	arg1	mutant					1645:1650	The S582A mutant	1635:1650	The S582A mutant	1635:1650	The S582A mutant was the most homogeneous with (Man)9(GlcNAc)2 comprising greater than 50% of oligosaccharides present.
9126611	8	110	theme	oligosaccharide	1478:1492	arg1	profiling					1494:1502	N-linked oligosaccharide profiling	1469:1502	N-linked oligosaccharide profiling of purified VV and BV WT and S582A mutant hCox-2	1469:1551	N-linked oligosaccharide profiling of purified VV and BV WT and S582A mutant hCox-2 showed the presence of high mannose structures, (Man)n (GlcNAc)2, n = 9, 8, 7, 6.
9126611	7	111	theme	clear	1276:1280	arg1	decrease					1282:1289	no clear decrease	1273:1289	no clear decrease in heterogeneity	1273:1306	Expression of a double N-glycosylation site mutant in Sf9 cells, N580Q/N592Q, resulted in a decrease in glycosylation but no clear decrease in heterogeneity, indicating that the high degree of N-glycosylation heterogeneity observed with the BV-Sf9 system is not due to partial glycosylation of both Asn580 and Asn592.
9126611	11	112	theme	Da	2083:2084	arg1	consistent					2090:2099	consistent	2090:2099	consistent	2090:2099	The difference between the highest mass peaks of the two envelopes, of approximately 1500 Da, is consistent with the wild-type enzyme containing an additional high mannose oligosaccharide.
9126611	11	112	theme	Da	2083:2084	arg1	difference					1997:2006	The difference	1993:2006	The difference	1993:2006	The difference between the highest mass peaks of the two envelopes, of approximately 1500 Da, is consistent with the wild-type enzyme containing an additional high mannose oligosaccharide.
9126611	5	113	theme	S2	907:908	arg1	system					915:920	a Drosophila S2 cell system	894:920	a Drosophila S2 cell system	894:920	Results of the expression of WT and N580Q hCox-2 in a Drosophila S2 cell system were also consistent with the N-glycosylation at this site, but low levels of activity were obtained.
9126611	6	114	theme	High	1024:1027	arg1	levels					1029:1034	High levels	1024:1034	High levels of N-glycosylation heterogeneity	1024:1067	High levels of N-glycosylation heterogeneity are observed in hCox-2 expressed using recombinant baculovirus (BV) in Sf9 cells.
9126611	3	115	theme	consensus	410:418	arg1	sequence					420:427	the N-glycosylation consensus sequence	390:427	the N-glycosylation consensus sequence at Asn580 (N580Q and S582A mutants)	390:463	Removal of the N-glycosylation consensus sequence at Asn580 (N580Q and S582A mutants) resulted in the expression of protein comprising a single glycoform, consistent with the partial N-glycosylation at this site in the wild-type (WT) enzyme.
9126611	8	116	theme	VV	1516:1517	arg1	profiling					1494:1502	N-linked oligosaccharide profiling	1469:1502	N-linked oligosaccharide profiling of purified VV and BV WT and S582A mutant hCox-2	1469:1551	N-linked oligosaccharide profiling of purified VV and BV WT and S582A mutant hCox-2 showed the presence of high mannose structures, (Man)n (GlcNAc)2, n = 9, 8, 7, 6.
9126611	6	117	from	baculovirus	1120:1130	arg1	cells					1144:1148	Sf9 cells	1140:1148	Sf9 cells	1140:1148	High levels of N-glycosylation heterogeneity are observed in hCox-2 expressed using recombinant baculovirus (BV) in Sf9 cells.
9126611	7	118	from	Expression	1151:1160	arg1	cells					1209:1213	Sf9 cells	1205:1213	Sf9 cells	1205:1213	Expression of a double N-glycosylation site mutant in Sf9 cells, N580Q/N592Q, resulted in a decrease in glycosylation but no clear decrease in heterogeneity, indicating that the high degree of N-glycosylation heterogeneity observed with the BV-Sf9 system is not due to partial glycosylation of both Asn580 and Asn592.
9126611	0	119	theme	cyclooxygenase-2	23:38	arg1	heterogeneity					54:66	human cyclooxygenase-2 glycosylation heterogeneity	17:66	human cyclooxygenase-2 glycosylation heterogeneity	17:66	Investigation of human cyclooxygenase-2 glycosylation heterogeneity and protein expression in insect and mammalian cell expression systems.
9126611	8	120	theme	BV	1523:1524	arg1	WT					1526:1527	purified VV and BV WT and S582A mutant hCox-2	1507:1551	WT	1526:1527	N-linked oligosaccharide profiling of purified VV and BV WT and S582A mutant hCox-2 showed the presence of high mannose structures, (Man)n (GlcNAc)2, n = 9, 8, 7, 6.
9126611	3	121	with	consistent	534:543	arg1	N-glycosylation					562:576	the partial N-glycosylation	550:576	the partial N-glycosylation at this site in the wild-type (WT) enzyme	550:618	Removal of the N-glycosylation consensus sequence at Asn580 (N580Q and S582A mutants) resulted in the expression of protein comprising a single glycoform, consistent with the partial N-glycosylation at this site in the wild-type (WT) enzyme.
9126611	3	122	dep	N580Q	440:444	arg1	mutants					456:462	mutants	456:462	mutants	456:462	Removal of the N-glycosylation consensus sequence at Asn580 (N580Q and S582A mutants) resulted in the expression of protein comprising a single glycoform, consistent with the partial N-glycosylation at this site in the wild-type (WT) enzyme.
9126611	5	123	gly	N-glycosylation	952:966	arg1	site					976:979	this site	971:979	this site	971:979	Results of the expression of WT and N580Q hCox-2 in a Drosophila S2 cell system were also consistent with the N-glycosylation at this site, but low levels of activity were obtained.
9126611	5	123	gly	N-glycosylation	952:966	arg2	site					976:979	this site	971:979	this site	971:979	Results of the expression of WT and N580Q hCox-2 in a Drosophila S2 cell system were also consistent with the N-glycosylation at this site, but low levels of activity were obtained.
9126611	4	124	theme	inhibitor	794:802	arg1	sensitivities					804:816	inhibitor sensitivities	794:816	inhibitor sensitivities of WT and both mutants	794:839	The specific cyclooxygenase activities of the purified WT and N580Q mutant were equivalent (40 +/- 3 mumol O2/min/mg) and titrations with diclofenac showed no difference in inhibitor sensitivities of WT and both mutants.
9126611	0	125	theme	protein	72:78	arg1	expression					80:89	protein expression	72:89	protein expression in insect and mammalian cell expression systems	72:137	Investigation of human cyclooxygenase-2 glycosylation heterogeneity and protein expression in insect and mammalian cell expression systems.
9126611	5	126	theme	low	986:988	arg1	levels					990:995	low levels	986:995	low levels of activity	986:1007	Results of the expression of WT and N580Q hCox-2 in a Drosophila S2 cell system were also consistent with the N-glycosylation at this site, but low levels of activity were obtained.
9126611	7	127	from	decrease	1243:1250	arg1	glycosylation					1255:1267	glycosylation	1255:1267	glycosylation	1255:1267	Expression of a double N-glycosylation site mutant in Sf9 cells, N580Q/N592Q, resulted in a decrease in glycosylation but no clear decrease in heterogeneity, indicating that the high degree of N-glycosylation heterogeneity observed with the BV-Sf9 system is not due to partial glycosylation of both Asn580 and Asn592.
9126611	8	128	theme	mutant	1539:1544	arg1	hCox-2					1546:1551	purified VV and BV WT and S582A mutant hCox-2	1507:1551	hCox-2	1546:1551	N-linked oligosaccharide profiling of purified VV and BV WT and S582A mutant hCox-2 showed the presence of high mannose structures, (Man)n (GlcNAc)2, n = 9, 8, 7, 6.
9126611	5	129	from	system	915:920	arg1	Results					842:848	Results	842:848	Results of the expression of WT and N580Q hCox-2 in a Drosophila S2 cell system	842:920	Results of the expression of WT and N580Q hCox-2 in a Drosophila S2 cell system were also consistent with the N-glycosylation at this site, but low levels of activity were obtained.
9126611	11	130	theme	mannose	2157:2163	arg1	oligosaccharide					2165:2179	an additional high mannose oligosaccharide	2138:2179	an additional high mannose oligosaccharide	2138:2179	The difference between the highest mass peaks of the two envelopes, of approximately 1500 Da, is consistent with the wild-type enzyme containing an additional high mannose oligosaccharide.
9126611	11	131	theme	highest	2020:2026	arg1	peaks					2033:2037	the highest mass peaks	2016:2037	the highest mass peaks of the two envelopes	2016:2058	The difference between the highest mass peaks of the two envelopes, of approximately 1500 Da, is consistent with the wild-type enzyme containing an additional high mannose oligosaccharide.
9126611	1	132	theme	nonsteroidal	244:255	arg1	drugs					275:279	nonsteroidal anti-inflammatory drugs	244:279	nonsteroidal anti-inflammatory drugs	244:279	Human cyclooxygenase-2 (hCox-2) is a key enzyme in the biosynthesis of prostaglandins and the target of nonsteroidal anti-inflammatory drugs.
18780401	3	0	theme	glycoproteins	613:625	arg1	classes					593:599	restricted classes	582:599	restricted classes of N-linked glycoproteins	582:625	A number of approaches to describe the complexity of human milk proteome have provided only a partial characterization of restricted classes of N-linked glycoproteins.
18780401	6	1	theme	PNGase	933:938	arg1	F					930:930	peptide N-glycosidase F	908:930	peptide N-glycosidase F (PNGase F) treatment	908:951	Oligosaccharide-free peptides obtained by peptide N-glycosidase F (PNGase F) treatment were characterized by a shotgun MS-based approach, allowing the identification of N-glycosylated sites localized on proteins.
18780401	6	1	theme	PNGase	933:938	arg1	F					940:940	PNGase F	933:940	PNGase F	933:940	Oligosaccharide-free peptides obtained by peptide N-glycosidase F (PNGase F) treatment were characterized by a shotgun MS-based approach, allowing the identification of N-glycosylated sites localized on proteins.
18780401	3	2	theme	proteome	524:531	arg1	complexity					499:508	the complexity	495:508	the complexity of human milk proteome	495:531	A number of approaches to describe the complexity of human milk proteome have provided only a partial characterization of restricted classes of N-linked glycoproteins.
18780401	5	3	theme	samples	857:863	arg1	digest					836:841	the protein tryptic digest	816:841	the protein tryptic digest of human milk samples	816:863	Glycopeptides were selectively enriched from the protein tryptic digest of human milk samples.
18780401	0	4	theme	liquid	82:87	arg1	chromatography					89:102	hydrophilic interaction liquid chromatography	58:102	hydrophilic interaction liquid chromatography	58:102	Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry.
18780401	5	5	theme	protein	820:826	arg1	digest					836:841	the protein tryptic digest	816:841	the protein tryptic digest of human milk samples	816:863	Glycopeptides were selectively enriched from the protein tryptic digest of human milk samples.
18780401	2	6	gly	glycoproteins	445:457	arg1	glycoproteins					445:457	glycoproteins	445:457	glycoproteins	445:457	An important mechanism responsible for the antibacterial and antiviral effects of breast milk is the prevention of pathogen adhesion to host cell membranes mediated by a number of glycoconjugates, also including glycoproteins.
18780401	1	7	theme	critical	174:181	arg1	factor					183:188	a critical factor	172:188	a critical factor in protecting newborns against infections	172:230	Breastfeeding is now generally recognized as a critical factor in protecting newborns against infections.
18780401	1	7	theme	critical	174:181	arg1	Breastfeeding					127:139	Breastfeeding	127:139	Breastfeeding	127:139	Breastfeeding is now generally recognized as a critical factor in protecting newborns against infections.
18780401	0	8	theme	mass	108:111	arg1	spectrometry					113:124	mass spectrometry	108:124	mass spectrometry	108:124	Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry.
18780401	0	9	from	Identification	0:13	arg1	milk					50:53	human milk	44:53	human milk	44:53	Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry.
18780401	8	10	theme	fat	1263:1265	arg1	proteins					1286:1293	membrane fat globule-associated proteins	1254:1293	membrane fat globule-associated proteins	1254:1293	The glycoproteins include immunocompetent factors, membrane fat globule-associated proteins, enzymes involved in lipid degradation and cell differentiation, specific receptors, and other gene products with still unknown functions.
18780401	0	11	link	N-linked	18:25	arg1	glycoproteins					27:39	N-linked glycoproteins	18:39	N-linked glycoproteins in human milk	18:53	Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry.
18780401	2	12	theme	milk	322:325	arg1	effects					304:310	the antibacterial and antiviral effects	272:310	the antibacterial and antiviral effects of breast milk	272:325	An important mechanism responsible for the antibacterial and antiviral effects of breast milk is the prevention of pathogen adhesion to host cell membranes mediated by a number of glycoconjugates, also including glycoproteins.
18780401	3	13	theme	classes	593:599	arg1	characterization					562:577	only a partial characterization	547:577	only a partial characterization of restricted classes of N-linked glycoproteins	547:625	A number of approaches to describe the complexity of human milk proteome have provided only a partial characterization of restricted classes of N-linked glycoproteins.
18780401	6	14	theme	sites	1050:1054	arg1	identification					1017:1030	the identification	1013:1030	the identification of N-glycosylated sites localized on proteins	1013:1076	Oligosaccharide-free peptides obtained by peptide N-glycosidase F (PNGase F) treatment were characterized by a shotgun MS-based approach, allowing the identification of N-glycosylated sites localized on proteins.
18780401	8	15	theme	immunocompetent	1229:1243	arg1	factors					1245:1251	immunocompetent factors	1229:1251	immunocompetent factors	1229:1251	The glycoproteins include immunocompetent factors, membrane fat globule-associated proteins, enzymes involved in lipid degradation and cell differentiation, specific receptors, and other gene products with still unknown functions.
18780401	2	16	theme	breast	315:320	arg1	milk					322:325	breast milk	315:325	breast milk	315:325	An important mechanism responsible for the antibacterial and antiviral effects of breast milk is the prevention of pathogen adhesion to host cell membranes mediated by a number of glycoconjugates, also including glycoproteins.
18780401	6	17	theme	N-glycosylated	1035:1048	arg1	sites					1050:1054	N-glycosylated sites	1035:1054	N-glycosylated sites localized on proteins	1035:1076	Oligosaccharide-free peptides obtained by peptide N-glycosidase F (PNGase F) treatment were characterized by a shotgun MS-based approach, allowing the identification of N-glycosylated sites localized on proteins.
18780401	8	18	theme	membrane	1254:1261	arg1	proteins					1286:1293	membrane fat globule-associated proteins	1254:1293	membrane fat globule-associated proteins	1254:1293	The glycoproteins include immunocompetent factors, membrane fat globule-associated proteins, enzymes involved in lipid degradation and cell differentiation, specific receptors, and other gene products with still unknown functions.
18780401	0	19	from	milk	50:53	arg1	Identification					0:13	Identification	0:13	Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry.	0:125	Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry.
18780401	2	20	theme	glycoconjugates	413:427	arg1	number					403:408	a number	401:408	a number	401:408	An important mechanism responsible for the antibacterial and antiviral effects of breast milk is the prevention of pathogen adhesion to host cell membranes mediated by a number of glycoconjugates, also including glycoproteins.
18780401	4	21	gly	glycoproteins	674:686	arg1	glycoproteins					674:686	profiling N-linked glycoproteins	655:686	profiling N-linked glycoproteins of human milk	655:700	To achieve this objective, profiling N-linked glycoproteins of human milk was performed by Hydrophilic Interaction LC (HILIC) and MS analysis.
18780401	8	22	theme	other	1384:1388	arg1	products					1395:1402	other gene products	1384:1402	other gene products	1384:1402	The glycoproteins include immunocompetent factors, membrane fat globule-associated proteins, enzymes involved in lipid degradation and cell differentiation, specific receptors, and other gene products with still unknown functions.
18780401	3	23	theme	partial	554:560	arg1	characterization					562:577	only a partial characterization	547:577	only a partial characterization of restricted classes of N-linked glycoproteins	547:625	A number of approaches to describe the complexity of human milk proteome have provided only a partial characterization of restricted classes of N-linked glycoproteins.
18780401	3	24	theme	human	513:517	arg1	proteome					524:531	human milk proteome	513:531	human milk proteome	513:531	A number of approaches to describe the complexity of human milk proteome have provided only a partial characterization of restricted classes of N-linked glycoproteins.
18780401	4	25	theme	milk	697:700	arg1	glycoproteins					674:686	profiling N-linked glycoproteins	655:686	profiling N-linked glycoproteins of human milk	655:700	To achieve this objective, profiling N-linked glycoproteins of human milk was performed by Hydrophilic Interaction LC (HILIC) and MS analysis.
18780401	5	26	theme	human	846:850	arg1	samples					857:863	human milk samples	846:863	human milk samples	846:863	Glycopeptides were selectively enriched from the protein tryptic digest of human milk samples.
18780401	3	27	link	N-linked	604:611	arg1	glycoproteins					613:625	N-linked glycoproteins	604:625	N-linked glycoproteins	604:625	A number of approaches to describe the complexity of human milk proteome have provided only a partial characterization of restricted classes of N-linked glycoproteins.
18780401	8	28	with	receptors	1369:1377	arg1	functions					1423:1431	still unknown functions	1409:1431	still unknown functions	1409:1431	The glycoproteins include immunocompetent factors, membrane fat globule-associated proteins, enzymes involved in lipid degradation and cell differentiation, specific receptors, and other gene products with still unknown functions.
18780401	7	29	gly	N-glycosylated	1150:1163	arg1	sites					1165:1169	63 N-glycosylated sites	1147:1169	63 N-glycosylated sites encrypted in them	1147:1187	Using this strategy, 32 different glycoproteins were identified and 63 N-glycosylated sites encrypted in them were located.
18780401	5	30	theme	milk	852:855	arg1	samples					857:863	human milk samples	846:863	human milk samples	846:863	Glycopeptides were selectively enriched from the protein tryptic digest of human milk samples.
18780401	7	31	theme	N-glycosylated	1150:1163	arg1	sites					1165:1169	63 N-glycosylated sites	1147:1169	63 N-glycosylated sites encrypted in them	1147:1187	Using this strategy, 32 different glycoproteins were identified and 63 N-glycosylated sites encrypted in them were located.
18780401	8	32	with	factors	1245:1251	arg1	functions					1423:1431	still unknown functions	1409:1431	still unknown functions	1409:1431	The glycoproteins include immunocompetent factors, membrane fat globule-associated proteins, enzymes involved in lipid degradation and cell differentiation, specific receptors, and other gene products with still unknown functions.
18780401	3	33	theme	N-linked	604:611	arg1	glycoproteins					613:625	N-linked glycoproteins	604:625	N-linked glycoproteins	604:625	A number of approaches to describe the complexity of human milk proteome have provided only a partial characterization of restricted classes of N-linked glycoproteins.
18780401	6	34	theme	F	930:930	arg1	treatment					943:951	peptide N-glycosidase F (PNGase F) treatment	908:951	peptide N-glycosidase F (PNGase F) treatment	908:951	Oligosaccharide-free peptides obtained by peptide N-glycosidase F (PNGase F) treatment were characterized by a shotgun MS-based approach, allowing the identification of N-glycosylated sites localized on proteins.
18780401	0	35	theme	glycoproteins	27:39	arg1	Identification					0:13	Identification	0:13	Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry.	0:125	Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry.
18780401	8	36	theme	gene	1390:1393	arg1	products					1395:1402	other gene products	1384:1402	other gene products	1384:1402	The glycoproteins include immunocompetent factors, membrane fat globule-associated proteins, enzymes involved in lipid degradation and cell differentiation, specific receptors, and other gene products with still unknown functions.
18780401	0	37	gly	glycoproteins	27:39	arg1	glycoproteins					27:39	N-linked glycoproteins	18:39	N-linked glycoproteins in human milk	18:53	Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry.
18780401	3	38	theme	restricted	582:591	arg1	classes					593:599	restricted classes	582:599	restricted classes of N-linked glycoproteins	582:625	A number of approaches to describe the complexity of human milk proteome have provided only a partial characterization of restricted classes of N-linked glycoproteins.
18780401	8	39	theme	specific	1360:1367	arg1	receptors					1369:1377	specific receptors	1360:1377	specific receptors	1360:1377	The glycoproteins include immunocompetent factors, membrane fat globule-associated proteins, enzymes involved in lipid degradation and cell differentiation, specific receptors, and other gene products with still unknown functions.
18780401	0	40	theme	N-linked	18:25	arg1	glycoproteins					27:39	N-linked glycoproteins	18:39	N-linked glycoproteins in human milk	18:53	Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry.
18780401	8	41	gly	glycoproteins	1207:1219	arg1	glycoproteins					1207:1219	The glycoproteins	1203:1219	The glycoproteins	1203:1219	The glycoproteins include immunocompetent factors, membrane fat globule-associated proteins, enzymes involved in lipid degradation and cell differentiation, specific receptors, and other gene products with still unknown functions.
18780401	8	42	with	products	1395:1402	arg1	functions					1423:1431	still unknown functions	1409:1431	still unknown functions	1409:1431	The glycoproteins include immunocompetent factors, membrane fat globule-associated proteins, enzymes involved in lipid degradation and cell differentiation, specific receptors, and other gene products with still unknown functions.
18780401	2	43	theme	cell	374:377	arg1	membranes					379:387	host cell membranes	369:387	host cell membranes mediated by a number of glycoconjugates, also including glycoproteins	369:457	An important mechanism responsible for the antibacterial and antiviral effects of breast milk is the prevention of pathogen adhesion to host cell membranes mediated by a number of glycoconjugates, also including glycoproteins.
18780401	8	44	with	enzymes	1296:1302	arg1	functions					1423:1431	still unknown functions	1409:1431	still unknown functions	1409:1431	The glycoproteins include immunocompetent factors, membrane fat globule-associated proteins, enzymes involved in lipid degradation and cell differentiation, specific receptors, and other gene products with still unknown functions.
18780401	4	45	theme	N-linked	665:672	arg1	glycoproteins					674:686	profiling N-linked glycoproteins	655:686	profiling N-linked glycoproteins of human milk	655:700	To achieve this objective, profiling N-linked glycoproteins of human milk was performed by Hydrophilic Interaction LC (HILIC) and MS analysis.
18780401	0	46	theme	human	44:48	arg1	milk					50:53	human milk	44:53	human milk	44:53	Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry.
18780401	8	47	theme	unknown	1415:1421	arg1	functions					1423:1431	still unknown functions	1409:1431	still unknown functions	1409:1431	The glycoproteins include immunocompetent factors, membrane fat globule-associated proteins, enzymes involved in lipid degradation and cell differentiation, specific receptors, and other gene products with still unknown functions.
18780401	4	48	theme	human	691:695	arg1	milk					697:700	human milk	691:700	human milk	691:700	To achieve this objective, profiling N-linked glycoproteins of human milk was performed by Hydrophilic Interaction LC (HILIC) and MS analysis.
18780401	8	49	theme	globule-associated	1267:1284	arg1	proteins					1286:1293	membrane fat globule-associated proteins	1254:1293	membrane fat globule-associated proteins	1254:1293	The glycoproteins include immunocompetent factors, membrane fat globule-associated proteins, enzymes involved in lipid degradation and cell differentiation, specific receptors, and other gene products with still unknown functions.
18780401	8	50	theme	cell	1338:1341	arg1	differentiation					1343:1357	cell differentiation	1338:1357	cell differentiation	1338:1357	The glycoproteins include immunocompetent factors, membrane fat globule-associated proteins, enzymes involved in lipid degradation and cell differentiation, specific receptors, and other gene products with still unknown functions.
18780401	3	51	theme	approaches	472:481	arg1	number					462:467	A number	460:467	A number of approaches to describe the complexity of human milk proteome	460:531	A number of approaches to describe the complexity of human milk proteome have provided only a partial characterization of restricted classes of N-linked glycoproteins.
18780401	5	52	theme	tryptic	828:834	arg1	digest					836:841	the protein tryptic digest	816:841	the protein tryptic digest of human milk samples	816:863	Glycopeptides were selectively enriched from the protein tryptic digest of human milk samples.
18780401	6	53	theme	N-glycosidase	916:928	arg1	F					930:930	peptide N-glycosidase F	908:930	peptide N-glycosidase F (PNGase F) treatment	908:951	Oligosaccharide-free peptides obtained by peptide N-glycosidase F (PNGase F) treatment were characterized by a shotgun MS-based approach, allowing the identification of N-glycosylated sites localized on proteins.
18780401	6	53	theme	N-glycosidase	916:928	arg1	F					940:940	PNGase F	933:940	PNGase F	933:940	Oligosaccharide-free peptides obtained by peptide N-glycosidase F (PNGase F) treatment were characterized by a shotgun MS-based approach, allowing the identification of N-glycosylated sites localized on proteins.
18780401	2	54	theme	responsible	256:266	arg1	prevention					334:343	the prevention	330:343	the prevention of pathogen adhesion to host cell membranes mediated by a number of glycoconjugates, also including glycoproteins	330:457	An important mechanism responsible for the antibacterial and antiviral effects of breast milk is the prevention of pathogen adhesion to host cell membranes mediated by a number of glycoconjugates, also including glycoproteins.
18780401	2	54	theme	responsible	256:266	arg1	mechanism					246:254	An important mechanism	233:254	An important mechanism responsible for the antibacterial and antiviral effects of breast milk	233:325	An important mechanism responsible for the antibacterial and antiviral effects of breast milk is the prevention of pathogen adhesion to host cell membranes mediated by a number of glycoconjugates, also including glycoproteins.
18780401	3	55	gly	glycoproteins	613:625	arg1	glycoproteins					613:625	N-linked glycoproteins	604:625	N-linked glycoproteins	604:625	A number of approaches to describe the complexity of human milk proteome have provided only a partial characterization of restricted classes of N-linked glycoproteins.
18780401	8	56	theme	lipid	1316:1320	arg1	degradation					1322:1332	lipid degradation	1316:1332	lipid degradation	1316:1332	The glycoproteins include immunocompetent factors, membrane fat globule-associated proteins, enzymes involved in lipid degradation and cell differentiation, specific receptors, and other gene products with still unknown functions.
18780401	6	57	theme	peptide	908:914	arg1	F					930:930	peptide N-glycosidase F	908:930	peptide N-glycosidase F (PNGase F) treatment	908:951	Oligosaccharide-free peptides obtained by peptide N-glycosidase F (PNGase F) treatment were characterized by a shotgun MS-based approach, allowing the identification of N-glycosylated sites localized on proteins.
18780401	6	57	theme	peptide	908:914	arg1	F					940:940	PNGase F	933:940	PNGase F	933:940	Oligosaccharide-free peptides obtained by peptide N-glycosidase F (PNGase F) treatment were characterized by a shotgun MS-based approach, allowing the identification of N-glycosylated sites localized on proteins.
18780401	2	58	dep	glycoproteins	445:457	arg1	including					435:443	including	435:443	including	435:443	An important mechanism responsible for the antibacterial and antiviral effects of breast milk is the prevention of pathogen adhesion to host cell membranes mediated by a number of glycoconjugates, also including glycoproteins.
18780401	8	59	with	proteins	1286:1293	arg1	functions					1423:1431	still unknown functions	1409:1431	still unknown functions	1409:1431	The glycoproteins include immunocompetent factors, membrane fat globule-associated proteins, enzymes involved in lipid degradation and cell differentiation, specific receptors, and other gene products with still unknown functions.
18780401	2	60	theme	host	369:372	arg1	membranes					379:387	host cell membranes	369:387	host cell membranes mediated by a number of glycoconjugates, also including glycoproteins	369:457	An important mechanism responsible for the antibacterial and antiviral effects of breast milk is the prevention of pathogen adhesion to host cell membranes mediated by a number of glycoconjugates, also including glycoproteins.
18780401	7	61	gly	glycoproteins	1113:1125	arg1	glycoproteins					1113:1125	32 different glycoproteins	1100:1125	32 different glycoproteins	1100:1125	Using this strategy, 32 different glycoproteins were identified and 63 N-glycosylated sites encrypted in them were located.
18780401	6	62	theme	MS-based	985:992	arg1	approach					994:1001	a shotgun MS-based approach	975:1001	a shotgun MS-based approach	975:1001	Oligosaccharide-free peptides obtained by peptide N-glycosidase F (PNGase F) treatment were characterized by a shotgun MS-based approach, allowing the identification of N-glycosylated sites localized on proteins.
18780401	7	63	theme	different	1103:1111	arg1	glycoproteins					1113:1125	32 different glycoproteins	1100:1125	32 different glycoproteins	1100:1125	Using this strategy, 32 different glycoproteins were identified and 63 N-glycosylated sites encrypted in them were located.
18780401	2	64	theme	important	236:244	arg1	prevention					334:343	the prevention	330:343	the prevention of pathogen adhesion to host cell membranes mediated by a number of glycoconjugates, also including glycoproteins	330:457	An important mechanism responsible for the antibacterial and antiviral effects of breast milk is the prevention of pathogen adhesion to host cell membranes mediated by a number of glycoconjugates, also including glycoproteins.
18780401	2	64	theme	important	236:244	arg1	mechanism					246:254	An important mechanism	233:254	An important mechanism responsible for the antibacterial and antiviral effects of breast milk	233:325	An important mechanism responsible for the antibacterial and antiviral effects of breast milk is the prevention of pathogen adhesion to host cell membranes mediated by a number of glycoconjugates, also including glycoproteins.
18780401	6	65	gly	N-glycosylated	1035:1048	arg1	sites					1050:1054	N-glycosylated sites	1035:1054	N-glycosylated sites localized on proteins	1035:1076	Oligosaccharide-free peptides obtained by peptide N-glycosidase F (PNGase F) treatment were characterized by a shotgun MS-based approach, allowing the identification of N-glycosylated sites localized on proteins.
18780401	3	66	theme	milk	519:522	arg1	proteome					524:531	human milk proteome	513:531	human milk proteome	513:531	A number of approaches to describe the complexity of human milk proteome have provided only a partial characterization of restricted classes of N-linked glycoproteins.
18780401	6	67	theme	shotgun	977:983	arg1	approach					994:1001	a shotgun MS-based approach	975:1001	a shotgun MS-based approach	975:1001	Oligosaccharide-free peptides obtained by peptide N-glycosidase F (PNGase F) treatment were characterized by a shotgun MS-based approach, allowing the identification of N-glycosylated sites localized on proteins.
18780401	3	68	dep	number	462:467	arg1	describe					486:493	describe	486:493	to describe the complexity of human milk proteome	483:531	A number of approaches to describe the complexity of human milk proteome have provided only a partial characterization of restricted classes of N-linked glycoproteins.
18780401	2	69	theme	antiviral	294:302	arg1	effects					304:310	the antibacterial and antiviral effects	272:310	the antibacterial and antiviral effects of breast milk	272:325	An important mechanism responsible for the antibacterial and antiviral effects of breast milk is the prevention of pathogen adhesion to host cell membranes mediated by a number of glycoconjugates, also including glycoproteins.
18780401	2	70	theme	adhesion	357:364	arg1	prevention					334:343	the prevention	330:343	the prevention of pathogen adhesion to host cell membranes mediated by a number of glycoconjugates, also including glycoproteins	330:457	An important mechanism responsible for the antibacterial and antiviral effects of breast milk is the prevention of pathogen adhesion to host cell membranes mediated by a number of glycoconjugates, also including glycoproteins.
18780401	2	70	theme	adhesion	357:364	arg1	mechanism					246:254	An important mechanism	233:254	An important mechanism responsible for the antibacterial and antiviral effects of breast milk	233:325	An important mechanism responsible for the antibacterial and antiviral effects of breast milk is the prevention of pathogen adhesion to host cell membranes mediated by a number of glycoconjugates, also including glycoproteins.
18780401	6	71	located	localized	1056:1064	arg2	sites					1050:1054	N-glycosylated sites	1035:1054	N-glycosylated sites localized on proteins	1035:1076	Oligosaccharide-free peptides obtained by peptide N-glycosidase F (PNGase F) treatment were characterized by a shotgun MS-based approach, allowing the identification of N-glycosylated sites localized on proteins.
18780401	6	71	located	localized	1056:1064	arg1	proteins					1069:1076	proteins	1069:1076	proteins	1069:1076	Oligosaccharide-free peptides obtained by peptide N-glycosidase F (PNGase F) treatment were characterized by a shotgun MS-based approach, allowing the identification of N-glycosylated sites localized on proteins.
18780401	2	72	theme	pathogen	348:355	arg1	adhesion					357:364	pathogen adhesion	348:364	pathogen adhesion to host cell membranes mediated by a number of glycoconjugates, also including glycoproteins	348:457	An important mechanism responsible for the antibacterial and antiviral effects of breast milk is the prevention of pathogen adhesion to host cell membranes mediated by a number of glycoconjugates, also including glycoproteins.
18780401	4	73	theme	MS	758:759	arg1	analysis					761:768	MS analysis	758:768	MS analysis	758:768	To achieve this objective, profiling N-linked glycoproteins of human milk was performed by Hydrophilic Interaction LC (HILIC) and MS analysis.
18780401	0	74	theme	interaction	70:80	arg1	chromatography					89:102	hydrophilic interaction liquid chromatography	58:102	hydrophilic interaction liquid chromatography	58:102	Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry.
18780401	6	75	theme	Oligosaccharide-free	866:885	arg1	peptides					887:894	Oligosaccharide-free peptides	866:894	Oligosaccharide-free peptides obtained by peptide N-glycosidase F (PNGase F) treatment	866:951	Oligosaccharide-free peptides obtained by peptide N-glycosidase F (PNGase F) treatment were characterized by a shotgun MS-based approach, allowing the identification of N-glycosylated sites localized on proteins.
18780401	2	76	theme	antibacterial	276:288	arg1	effects					304:310	the antibacterial and antiviral effects	272:310	the antibacterial and antiviral effects of breast milk	272:325	An important mechanism responsible for the antibacterial and antiviral effects of breast milk is the prevention of pathogen adhesion to host cell membranes mediated by a number of glycoconjugates, also including glycoproteins.
18780401	4	77	theme	Interaction	731:741	arg1	LC					743:744	Hydrophilic Interaction LC	719:744	Hydrophilic Interaction LC (HILIC)	719:752	To achieve this objective, profiling N-linked glycoproteins of human milk was performed by Hydrophilic Interaction LC (HILIC) and MS analysis.
18780401	4	77	theme	Interaction	731:741	arg1	HILIC					747:751	HILIC	747:751	HILIC	747:751	To achieve this objective, profiling N-linked glycoproteins of human milk was performed by Hydrophilic Interaction LC (HILIC) and MS analysis.
18780401	4	78	theme	profiling	655:663	arg1	glycoproteins					674:686	profiling N-linked glycoproteins	655:686	profiling N-linked glycoproteins of human milk	655:700	To achieve this objective, profiling N-linked glycoproteins of human milk was performed by Hydrophilic Interaction LC (HILIC) and MS analysis.
18780401	0	79	theme	hydrophilic	58:68	arg1	chromatography					89:102	hydrophilic interaction liquid chromatography	58:102	hydrophilic interaction liquid chromatography	58:102	Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry.
18780401	0	80	from	glycoproteins	27:39	arg1	milk					50:53	human milk	44:53	human milk	44:53	Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry.
18780401	4	81	link	N-linked	665:672	arg1	glycoproteins					674:686	profiling N-linked glycoproteins	655:686	profiling N-linked glycoproteins of human milk	655:700	To achieve this objective, profiling N-linked glycoproteins of human milk was performed by Hydrophilic Interaction LC (HILIC) and MS analysis.
18780401	4	82	theme	Hydrophilic	719:729	arg1	LC					743:744	Hydrophilic Interaction LC	719:744	Hydrophilic Interaction LC (HILIC)	719:752	To achieve this objective, profiling N-linked glycoproteins of human milk was performed by Hydrophilic Interaction LC (HILIC) and MS analysis.
18780401	4	82	theme	Hydrophilic	719:729	arg1	HILIC					747:751	HILIC	747:751	HILIC	747:751	To achieve this objective, profiling N-linked glycoproteins of human milk was performed by Hydrophilic Interaction LC (HILIC) and MS analysis.
12218058	1	0	theme	precursor	317:325	arg1	proteins					327:334	other precursor proteins	311:334	other precursor proteins	311:334	Bone morphogenetic protein (BMP)-1 is a glycosylated metalloproteinase that is fundamental to the synthesis of a normal extracellular matrix because it cleaves type I procollagen, as well as other precursor proteins.
12218058	1	1	gly	glycosylated	160:171	arg1	metalloproteinase					173:189	a glycosylated metalloproteinase	158:189	a glycosylated metalloproteinase that is fundamental to the synthesis of a normal extracellular matrix because it cleaves type I procollagen, as well as other precursor proteins	158:334	Bone morphogenetic protein (BMP)-1 is a glycosylated metalloproteinase that is fundamental to the synthesis of a normal extracellular matrix because it cleaves type I procollagen, as well as other precursor proteins.
12218058	1	1	gly	glycosylated	160:171	arg1	fundamental					199:209	fundamental	199:209	fundamental	199:209	Bone morphogenetic protein (BMP)-1 is a glycosylated metalloproteinase that is fundamental to the synthesis of a normal extracellular matrix because it cleaves type I procollagen, as well as other precursor proteins.
12218058	1	1	gly	glycosylated	160:171	arg1	BMP					148:150	Bone morphogenetic protein (BMP)-1	120:153	Bone morphogenetic protein (BMP)-1	120:153	Bone morphogenetic protein (BMP)-1 is a glycosylated metalloproteinase that is fundamental to the synthesis of a normal extracellular matrix because it cleaves type I procollagen, as well as other precursor proteins.
12218058	3	2	theme	threonine	809:817	arg1	C-terminal					795:804	C-terminal	795:804	C-terminal	795:804	In this study we showed that all these sites are N-glycosylated with complex-type oligosaccharides containing sialic acid, except Asn(726) presumably because proline occurs immediately C-terminal of threonine in the consensus sequence.
12218058	4	3	theme	glycosylation	886:898	arg1	sites					900:904	all glycosylation sites	882:904	all glycosylation sites	882:904	Recombinant BMP-1 molecules lacking all glycosylation sites or the three CUB-specific sites were not secreted.
12218058	1	4	theme	extracellular	240:252	arg1	matrix					254:259	a normal extracellular matrix	231:259	a normal extracellular matrix	231:259	Bone morphogenetic protein (BMP)-1 is a glycosylated metalloproteinase that is fundamental to the synthesis of a normal extracellular matrix because it cleaves type I procollagen, as well as other precursor proteins.
12218058	5	5	theme	CUB	971:973	arg1	glycosylation					975:987	CUB glycosylation	971:987	CUB glycosylation	971:987	BMP-1 lacking CUB glycosylation was translocated to the proteasome for degradation.
12218058	8	6	theme	CUB	1398:1400	arg1	BMP-1					1413:1417	BMP-1	1413:1417	BMP-1	1413:1417	The study showed that the glycosylation sites in the CUB domains of BMP-1 are important for secretion and stability of the molecule.
12218058	8	6	theme	CUB	1398:1400	arg1	domains					1402:1408	the CUB domains	1394:1408	the CUB domains of BMP-1	1394:1417	The study showed that the glycosylation sites in the CUB domains of BMP-1 are important for secretion and stability of the molecule.
12218058	6	7	theme	full	1136:1139	arg1	activity					1166:1173	full procollagen C-proteinase activity	1136:1173	full procollagen C-proteinase activity	1136:1173	BMP-1 molecules lacking individual glycosylation sites were efficiently secreted and exhibited full procollagen C-proteinase activity, but N332Q and N599Q exhibited a slower rate of cleavage.
12218058	2	8	theme	Sequence	337:344	arg1	analysis					346:353	Sequence analysis	337:353	Sequence analysis	337:353	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	1	9	theme	matrix	254:259	arg1	synthesis					218:226	the synthesis	214:226	the synthesis of a normal extracellular matrix	214:259	Bone morphogenetic protein (BMP)-1 is a glycosylated metalloproteinase that is fundamental to the synthesis of a normal extracellular matrix because it cleaves type I procollagen, as well as other precursor proteins.
12218058	6	10	theme	BMP-1	1041:1045	arg1	molecules					1047:1055	BMP-1 molecules	1041:1055	BMP-1 molecules lacking individual glycosylation sites	1041:1094	BMP-1 molecules lacking individual glycosylation sites were efficiently secreted and exhibited full procollagen C-proteinase activity, but N332Q and N599Q exhibited a slower rate of cleavage.
12218058	2	11	gly	glycosylation	402:414	arg2	Asn					443:445	Asn(91)	443:449	Asn(91) (prodomain)	443:461	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	11	gly	glycosylation	402:414	arg2	sites					416:420	six potential N-linked glycosylation sites	379:420	six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726)	379:573	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	11	gly	glycosylation	402:414	arg2	Asn					538:540	Asn(599)	538:545	Asn(599) (CUB3 domain)	538:559	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	11	gly	glycosylation	402:414	arg2	Asn					464:466	Asn(142)	464:471	Asn(142) (metalloproteinase domain)	464:498	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	11	gly	glycosylation	402:414	arg2	NXS/T					428:432	i.e. NXS/T	423:432	i.e. NXS/T	423:432	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	11	gly	glycosylation	402:414	arg2	six					379:381	six	379:381	six	379:381	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	11	gly	glycosylation	402:414	arg2	Asn					501:503	Asn(332)	501:508	Asn(332)	501:508	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	3	12	theme	consensus	826:834	arg1	sequence					836:843	the consensus sequence	822:843	the consensus sequence	822:843	In this study we showed that all these sites are N-glycosylated with complex-type oligosaccharides containing sialic acid, except Asn(726) presumably because proline occurs immediately C-terminal of threonine in the consensus sequence.
12218058	7	13	theme	thermal	1323:1329	arg1	denaturation					1331:1342	thermal denaturation	1323:1342	thermal denaturation	1323:1342	BMP-1 molecules lacking any one of the CUB-specific glycosylation sites were sensitive to thermal denaturation.
12218058	3	14	with	N-glycosylated	659:672	arg1	oligosaccharides					692:707	complex-type oligosaccharides	679:707	complex-type oligosaccharides containing sialic acid	679:730	In this study we showed that all these sites are N-glycosylated with complex-type oligosaccharides containing sialic acid, except Asn(726) presumably because proline occurs immediately C-terminal of threonine in the consensus sequence.
12218058	6	15	theme	procollagen	1141:1151	arg1	activity					1166:1173	full procollagen C-proteinase activity	1136:1173	full procollagen C-proteinase activity	1136:1173	BMP-1 molecules lacking individual glycosylation sites were efficiently secreted and exhibited full procollagen C-proteinase activity, but N332Q and N599Q exhibited a slower rate of cleavage.
12218058	2	16	theme	CUB1	524:527	arg1	Asn					443:445	Asn(91)	443:449	Asn(91) (prodomain)	443:461	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	16	theme	CUB1	524:527	arg1	domain					529:534	CUB1 domain	524:534	CUB1 domain	524:534	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	3	17	dep	occurs	776:781	arg1	Asn					740:742	Asn	740:742	Asn(726)	740:747	In this study we showed that all these sites are N-glycosylated with complex-type oligosaccharides containing sialic acid, except Asn(726) presumably because proline occurs immediately C-terminal of threonine in the consensus sequence.
12218058	3	17	dep	occurs	776:781	arg1	except					733:738	except	733:738	except	733:738	In this study we showed that all these sites are N-glycosylated with complex-type oligosaccharides containing sialic acid, except Asn(726) presumably because proline occurs immediately C-terminal of threonine in the consensus sequence.
12218058	3	17	dep	occurs	776:781	arg1	726					744:746	726	744:746	726	744:746	In this study we showed that all these sites are N-glycosylated with complex-type oligosaccharides containing sialic acid, except Asn(726) presumably because proline occurs immediately C-terminal of threonine in the consensus sequence.
12218058	2	18	theme	potential	383:391	arg1	Asn					464:466	Asn(142)	464:471	Asn(142) (metalloproteinase domain)	464:498	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	18	theme	potential	383:391	arg1	NXS/T					428:432	i.e. NXS/T	423:432	i.e. NXS/T	423:432	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	18	theme	potential	383:391	arg1	Asn					501:503	Asn(332)	501:508	Asn(332)	501:508	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	18	theme	potential	383:391	arg1	sites					416:420	six potential N-linked glycosylation sites	379:420	six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726)	379:573	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	18	theme	potential	383:391	arg1	Asn					538:540	Asn(599)	538:545	Asn(599) (CUB3 domain)	538:559	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	18	theme	potential	383:391	arg1	Asn					443:445	Asn(91)	443:449	Asn(91) (prodomain)	443:461	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	0	19	theme	protein	111:117	arg1	stability					94:102	stability	94:102	stability	94:102	Post-translational modification of bone morphogenetic protein-1 is required for secretion and stability of the protein.
12218058	0	19	theme	protein	111:117	arg1	secretion					80:88	secretion	80:88	secretion	80:88	Post-translational modification of bone morphogenetic protein-1 is required for secretion and stability of the protein.
12218058	6	20	theme	cleavage	1223:1230	arg1	rate					1215:1218	a slower rate	1206:1218	a slower rate of cleavage	1206:1230	BMP-1 molecules lacking individual glycosylation sites were efficiently secreted and exhibited full procollagen C-proteinase activity, but N332Q and N599Q exhibited a slower rate of cleavage.
12218058	4	21	theme	BMP-1	858:862	arg1	molecules					864:872	Recombinant BMP-1 molecules	846:872	Recombinant BMP-1 molecules lacking all glycosylation sites or the three CUB-specific sites	846:936	Recombinant BMP-1 molecules lacking all glycosylation sites or the three CUB-specific sites were not secreted.
12218058	1	22	theme	glycosylated	160:171	arg1	metalloproteinase					173:189	a glycosylated metalloproteinase	158:189	a glycosylated metalloproteinase that is fundamental to the synthesis of a normal extracellular matrix because it cleaves type I procollagen, as well as other precursor proteins	158:334	Bone morphogenetic protein (BMP)-1 is a glycosylated metalloproteinase that is fundamental to the synthesis of a normal extracellular matrix because it cleaves type I procollagen, as well as other precursor proteins.
12218058	1	22	theme	glycosylated	160:171	arg1	fundamental					199:209	fundamental	199:209	fundamental	199:209	Bone morphogenetic protein (BMP)-1 is a glycosylated metalloproteinase that is fundamental to the synthesis of a normal extracellular matrix because it cleaves type I procollagen, as well as other precursor proteins.
12218058	1	22	theme	glycosylated	160:171	arg1	BMP					148:150	Bone morphogenetic protein (BMP)-1	120:153	Bone morphogenetic protein (BMP)-1	120:153	Bone morphogenetic protein (BMP)-1 is a glycosylated metalloproteinase that is fundamental to the synthesis of a normal extracellular matrix because it cleaves type I procollagen, as well as other precursor proteins.
12218058	8	23	theme	BMP-1	1413:1417	arg1	BMP-1					1413:1417	BMP-1	1413:1417	BMP-1	1413:1417	The study showed that the glycosylation sites in the CUB domains of BMP-1 are important for secretion and stability of the molecule.
12218058	8	23	theme	BMP-1	1413:1417	arg1	domains					1402:1408	the CUB domains	1394:1408	the CUB domains of BMP-1	1394:1417	The study showed that the glycosylation sites in the CUB domains of BMP-1 are important for secretion and stability of the molecule.
12218058	8	24	theme	molecule	1468:1475	arg1	secretion					1437:1445	secretion	1437:1445	secretion	1437:1445	The study showed that the glycosylation sites in the CUB domains of BMP-1 are important for secretion and stability of the molecule.
12218058	8	24	theme	molecule	1468:1475	arg1	stability					1451:1459	stability	1451:1459	stability	1451:1459	The study showed that the glycosylation sites in the CUB domains of BMP-1 are important for secretion and stability of the molecule.
12218058	7	25	theme	glycosylation	1285:1297	arg1	sites					1299:1303	the CUB-specific glycosylation sites	1268:1303	the CUB-specific glycosylation sites	1268:1303	BMP-1 molecules lacking any one of the CUB-specific glycosylation sites were sensitive to thermal denaturation.
12218058	0	26	theme	Post-translational	0:17	arg1	modification					19:30	Post-translational modification	0:30	Post-translational modification of bone morphogenetic protein-1	0:62	Post-translational modification of bone morphogenetic protein-1 is required for secretion and stability of the protein.
12218058	2	27	theme	Asn	514:516	arg1	prodomain					452:460	prodomain	452:460	prodomain	452:460	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	27	theme	Asn	514:516	arg1	Asn					443:445	Asn(91)	443:449	Asn(91) (prodomain)	443:461	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	27	theme	Asn	514:516	arg1	sites					416:420	six potential N-linked glycosylation sites	379:420	six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726)	379:573	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	27	theme	Asn	514:516	arg1	domain					529:534	CUB1 domain	524:534	CUB1 domain	524:534	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	3	28	gly	N-glycosylated	659:672	arg1	sites					649:653	all these sites	639:653	all these sites	639:653	In this study we showed that all these sites are N-glycosylated with complex-type oligosaccharides containing sialic acid, except Asn(726) presumably because proline occurs immediately C-terminal of threonine in the consensus sequence.
12218058	7	29	theme	BMP-1	1233:1237	arg1	molecules					1239:1247	BMP-1 molecules	1233:1247	BMP-1 molecules lacking any one of the CUB-specific glycosylation sites	1233:1303	BMP-1 molecules lacking any one of the CUB-specific glycosylation sites were sensitive to thermal denaturation.
12218058	0	30	theme	bone	35:38	arg1	protein-1					54:62	bone morphogenetic protein-1	35:62	bone morphogenetic protein-1	35:62	Post-translational modification of bone morphogenetic protein-1 is required for secretion and stability of the protein.
12218058	1	31	theme	type	280:283	arg1	procollagen					287:297	type I procollagen	280:297	type I procollagen	280:297	Bone morphogenetic protein (BMP)-1 is a glycosylated metalloproteinase that is fundamental to the synthesis of a normal extracellular matrix because it cleaves type I procollagen, as well as other precursor proteins.
12218058	2	32	theme	i.e.	423:426	arg1	sites					416:420	six potential N-linked glycosylation sites	379:420	six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726)	379:573	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	32	theme	i.e.	423:426	arg1	NXS/T					428:432	i.e. NXS/T	423:432	i.e. NXS/T	423:432	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	1	33	theme	I	285:285	arg1	procollagen					287:297	type I procollagen	280:297	type I procollagen	280:297	Bone morphogenetic protein (BMP)-1 is a glycosylated metalloproteinase that is fundamental to the synthesis of a normal extracellular matrix because it cleaves type I procollagen, as well as other precursor proteins.
12218058	2	34	theme	metalloproteinase	474:490	arg1	Asn					464:466	Asn(142)	464:471	Asn(142) (metalloproteinase domain)	464:498	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	34	theme	metalloproteinase	474:490	arg1	domain					492:497	metalloproteinase domain	474:497	metalloproteinase domain	474:497	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	7	35	theme	CUB-specific	1272:1283	arg1	sites					1299:1303	the CUB-specific glycosylation sites	1268:1303	the CUB-specific glycosylation sites	1268:1303	BMP-1 molecules lacking any one of the CUB-specific glycosylation sites were sensitive to thermal denaturation.
12218058	0	36	theme	protein-1	54:62	arg1	modification					19:30	Post-translational modification	0:30	Post-translational modification of bone morphogenetic protein-1	0:62	Post-translational modification of bone morphogenetic protein-1 is required for secretion and stability of the protein.
12218058	6	37	theme	slower	1208:1213	arg1	rate					1215:1218	a slower rate	1206:1218	a slower rate of cleavage	1206:1230	BMP-1 molecules lacking individual glycosylation sites were efficiently secreted and exhibited full procollagen C-proteinase activity, but N332Q and N599Q exhibited a slower rate of cleavage.
12218058	2	38	contain	has	375:377	arg2	Asn					443:445	Asn(91)	443:449	Asn(91) (prodomain)	443:461	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	38	contain	has	375:377	arg2	sites					416:420	six potential N-linked glycosylation sites	379:420	six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726)	379:573	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	38	contain	has	375:377	arg2	Asn					538:540	Asn(599)	538:545	Asn(599) (CUB3 domain)	538:559	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	38	contain	has	375:377	arg2	Asn					464:466	Asn(142)	464:471	Asn(142) (metalloproteinase domain)	464:498	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	38	contain	has	375:377	arg2	NXS/T					428:432	i.e. NXS/T	423:432	i.e. NXS/T	423:432	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	38	contain	has	375:377	arg1	BMP-1					369:373	BMP-1	369:373	BMP-1	369:373	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	38	contain	has	375:377	arg2	Asn					501:503	Asn(332)	501:508	Asn(332)	501:508	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	39	theme	C-terminal-specific	582:600	arg1	domain					602:607	the C-terminal-specific domain	578:607	the C-terminal-specific domain	578:607	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	40	theme	glycosylation	402:414	arg1	Asn					464:466	Asn(142)	464:471	Asn(142) (metalloproteinase domain)	464:498	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	40	theme	glycosylation	402:414	arg1	NXS/T					428:432	i.e. NXS/T	423:432	i.e. NXS/T	423:432	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	40	theme	glycosylation	402:414	arg1	Asn					501:503	Asn(332)	501:508	Asn(332)	501:508	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	40	theme	glycosylation	402:414	arg1	sites					416:420	six potential N-linked glycosylation sites	379:420	six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726)	379:573	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	40	theme	glycosylation	402:414	arg1	Asn					538:540	Asn(599)	538:545	Asn(599) (CUB3 domain)	538:559	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	40	theme	glycosylation	402:414	arg1	Asn					443:445	Asn(91)	443:449	Asn(91) (prodomain)	443:461	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	0	41	theme	morphogenetic	40:52	arg1	protein-1					54:62	bone morphogenetic protein-1	35:62	bone morphogenetic protein-1	35:62	Post-translational modification of bone morphogenetic protein-1 is required for secretion and stability of the protein.
12218058	2	42	theme	N-linked	393:400	arg1	Asn					464:466	Asn(142)	464:471	Asn(142) (metalloproteinase domain)	464:498	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	42	theme	N-linked	393:400	arg1	NXS/T					428:432	i.e. NXS/T	423:432	i.e. NXS/T	423:432	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	42	theme	N-linked	393:400	arg1	Asn					501:503	Asn(332)	501:508	Asn(332)	501:508	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	42	theme	N-linked	393:400	arg1	sites					416:420	six potential N-linked glycosylation sites	379:420	six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726)	379:573	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	42	theme	N-linked	393:400	arg1	Asn					538:540	Asn(599)	538:545	Asn(599) (CUB3 domain)	538:559	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	42	theme	N-linked	393:400	arg1	Asn					443:445	Asn(91)	443:449	Asn(91) (prodomain)	443:461	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	4	43	theme	Recombinant	846:856	arg1	molecules					864:872	Recombinant BMP-1 molecules	846:872	Recombinant BMP-1 molecules lacking all glycosylation sites or the three CUB-specific sites	846:936	Recombinant BMP-1 molecules lacking all glycosylation sites or the three CUB-specific sites were not secreted.
12218058	7	44	gly	glycosylation	1285:1297	arg2	sites					1299:1303	the CUB-specific glycosylation sites	1268:1303	the CUB-specific glycosylation sites	1268:1303	BMP-1 molecules lacking any one of the CUB-specific glycosylation sites were sensitive to thermal denaturation.
12218058	1	45	theme	Bone	120:123	arg1	metalloproteinase					173:189	a glycosylated metalloproteinase	158:189	a glycosylated metalloproteinase that is fundamental to the synthesis of a normal extracellular matrix because it cleaves type I procollagen, as well as other precursor proteins	158:334	Bone morphogenetic protein (BMP)-1 is a glycosylated metalloproteinase that is fundamental to the synthesis of a normal extracellular matrix because it cleaves type I procollagen, as well as other precursor proteins.
12218058	1	45	theme	Bone	120:123	arg1	fundamental					199:209	fundamental	199:209	fundamental	199:209	Bone morphogenetic protein (BMP)-1 is a glycosylated metalloproteinase that is fundamental to the synthesis of a normal extracellular matrix because it cleaves type I procollagen, as well as other precursor proteins.
12218058	1	45	theme	Bone	120:123	arg1	BMP					148:150	Bone morphogenetic protein (BMP)-1	120:153	Bone morphogenetic protein (BMP)-1	120:153	Bone morphogenetic protein (BMP)-1 is a glycosylated metalloproteinase that is fundamental to the synthesis of a normal extracellular matrix because it cleaves type I procollagen, as well as other precursor proteins.
12218058	6	46	theme	C-proteinase	1153:1164	arg1	activity					1166:1173	full procollagen C-proteinase activity	1136:1173	full procollagen C-proteinase activity	1136:1173	BMP-1 molecules lacking individual glycosylation sites were efficiently secreted and exhibited full procollagen C-proteinase activity, but N332Q and N599Q exhibited a slower rate of cleavage.
12218058	4	47	gly	glycosylation	886:898	arg2	sites					900:904	all glycosylation sites	882:904	all glycosylation sites	882:904	Recombinant BMP-1 molecules lacking all glycosylation sites or the three CUB-specific sites were not secreted.
12218058	2	48	dep	sites	416:420	arg1	prodomain					452:460	prodomain	452:460	prodomain	452:460	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	48	dep	sites	416:420	arg1	domain					529:534	CUB1 domain	524:534	CUB1 domain	524:534	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	48	dep	sites	416:420	arg1	Asn					464:466	Asn(142)	464:471	Asn(142) (metalloproteinase domain)	464:498	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	48	dep	sites	416:420	arg1	Asn					501:503	Asn(332)	501:508	Asn(332)	501:508	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	48	dep	sites	416:420	arg1	domain					553:558	CUB3 domain	548:558	CUB3 domain	548:558	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	48	dep	sites	416:420	arg1	sites					416:420	six potential N-linked glycosylation sites	379:420	six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726)	379:573	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	48	dep	sites	416:420	arg1	Asn					538:540	Asn(599)	538:545	Asn(599) (CUB3 domain)	538:559	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	48	dep	sites	416:420	arg1	Asn					443:445	Asn(91)	443:449	Asn(91) (prodomain)	443:461	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	48	dep	sites	416:420	arg1	domain					492:497	metalloproteinase domain	474:497	metalloproteinase domain	474:497	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	49	theme	CUB3	548:551	arg1	domain					553:558	CUB3 domain	548:558	CUB3 domain	548:558	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	49	theme	CUB3	548:551	arg1	Asn					538:540	Asn(599)	538:545	Asn(599) (CUB3 domain)	538:559	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	1	50	theme	morphogenetic	125:137	arg1	metalloproteinase					173:189	a glycosylated metalloproteinase	158:189	a glycosylated metalloproteinase that is fundamental to the synthesis of a normal extracellular matrix because it cleaves type I procollagen, as well as other precursor proteins	158:334	Bone morphogenetic protein (BMP)-1 is a glycosylated metalloproteinase that is fundamental to the synthesis of a normal extracellular matrix because it cleaves type I procollagen, as well as other precursor proteins.
12218058	1	50	theme	morphogenetic	125:137	arg1	fundamental					199:209	fundamental	199:209	fundamental	199:209	Bone morphogenetic protein (BMP)-1 is a glycosylated metalloproteinase that is fundamental to the synthesis of a normal extracellular matrix because it cleaves type I procollagen, as well as other precursor proteins.
12218058	1	50	theme	morphogenetic	125:137	arg1	BMP					148:150	Bone morphogenetic protein (BMP)-1	120:153	Bone morphogenetic protein (BMP)-1	120:153	Bone morphogenetic protein (BMP)-1 is a glycosylated metalloproteinase that is fundamental to the synthesis of a normal extracellular matrix because it cleaves type I procollagen, as well as other precursor proteins.
12218058	4	51	theme	CUB-specific	919:930	arg1	sites					932:936	the three CUB-specific sites	909:936	the three CUB-specific sites	909:936	Recombinant BMP-1 molecules lacking all glycosylation sites or the three CUB-specific sites were not secreted.
12218058	2	52	link	N-linked	393:400	arg1	Asn					464:466	Asn(142)	464:471	Asn(142) (metalloproteinase domain)	464:498	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	52	link	N-linked	393:400	arg1	NXS/T					428:432	i.e. NXS/T	423:432	i.e. NXS/T	423:432	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	52	link	N-linked	393:400	arg1	Asn					501:503	Asn(332)	501:508	Asn(332)	501:508	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	52	link	N-linked	393:400	arg1	sites					416:420	six potential N-linked glycosylation sites	379:420	six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726)	379:573	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	52	link	N-linked	393:400	arg1	Asn					538:540	Asn(599)	538:545	Asn(599) (CUB3 domain)	538:559	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	52	link	N-linked	393:400	arg1	Asn					443:445	Asn(91)	443:449	Asn(91) (prodomain)	443:461	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	6	53	theme	glycosylation	1076:1088	arg1	sites					1090:1094	individual glycosylation sites	1065:1094	individual glycosylation sites	1065:1094	BMP-1 molecules lacking individual glycosylation sites were efficiently secreted and exhibited full procollagen C-proteinase activity, but N332Q and N599Q exhibited a slower rate of cleavage.
12218058	1	54	theme	protein	139:145	arg1	metalloproteinase					173:189	a glycosylated metalloproteinase	158:189	a glycosylated metalloproteinase that is fundamental to the synthesis of a normal extracellular matrix because it cleaves type I procollagen, as well as other precursor proteins	158:334	Bone morphogenetic protein (BMP)-1 is a glycosylated metalloproteinase that is fundamental to the synthesis of a normal extracellular matrix because it cleaves type I procollagen, as well as other precursor proteins.
12218058	1	54	theme	protein	139:145	arg1	fundamental					199:209	fundamental	199:209	fundamental	199:209	Bone morphogenetic protein (BMP)-1 is a glycosylated metalloproteinase that is fundamental to the synthesis of a normal extracellular matrix because it cleaves type I procollagen, as well as other precursor proteins.
12218058	1	54	theme	protein	139:145	arg1	BMP					148:150	Bone morphogenetic protein (BMP)-1	120:153	Bone morphogenetic protein (BMP)-1	120:153	Bone morphogenetic protein (BMP)-1 is a glycosylated metalloproteinase that is fundamental to the synthesis of a normal extracellular matrix because it cleaves type I procollagen, as well as other precursor proteins.
12218058	3	55	theme	complex-type	679:690	arg1	oligosaccharides					692:707	complex-type oligosaccharides	679:707	complex-type oligosaccharides containing sialic acid	679:730	In this study we showed that all these sites are N-glycosylated with complex-type oligosaccharides containing sialic acid, except Asn(726) presumably because proline occurs immediately C-terminal of threonine in the consensus sequence.
12218058	7	56	theme	sites	1299:1303	arg1	sites					1299:1303	the CUB-specific glycosylation sites	1268:1303	the CUB-specific glycosylation sites	1268:1303	BMP-1 molecules lacking any one of the CUB-specific glycosylation sites were sensitive to thermal denaturation.
12218058	7	56	theme	sites	1299:1303	arg1	one					1261:1263	one	1261:1263	one	1261:1263	BMP-1 molecules lacking any one of the CUB-specific glycosylation sites were sensitive to thermal denaturation.
12218058	8	57	theme	glycosylation	1371:1383	arg1	sites					1385:1389	the glycosylation sites	1367:1389	the glycosylation sites in the CUB domains of BMP-1	1367:1417	The study showed that the glycosylation sites in the CUB domains of BMP-1 are important for secretion and stability of the molecule.
12218058	8	57	theme	glycosylation	1371:1383	arg1	important					1423:1431	important	1423:1431	important	1423:1431	The study showed that the glycosylation sites in the CUB domains of BMP-1 are important for secretion and stability of the molecule.
12218058	6	58	theme	individual	1065:1074	arg1	sites					1090:1094	individual glycosylation sites	1065:1094	individual glycosylation sites	1065:1094	BMP-1 molecules lacking individual glycosylation sites were efficiently secreted and exhibited full procollagen C-proteinase activity, but N332Q and N599Q exhibited a slower rate of cleavage.
12218058	3	59	contain	containing	709:718	arg2	acid					727:730	sialic acid	720:730	sialic acid	720:730	In this study we showed that all these sites are N-glycosylated with complex-type oligosaccharides containing sialic acid, except Asn(726) presumably because proline occurs immediately C-terminal of threonine in the consensus sequence.
12218058	3	59	contain	containing	709:718	arg1	oligosaccharides					692:707	complex-type oligosaccharides	679:707	complex-type oligosaccharides containing sialic acid	679:730	In this study we showed that all these sites are N-glycosylated with complex-type oligosaccharides containing sialic acid, except Asn(726) presumably because proline occurs immediately C-terminal of threonine in the consensus sequence.
12218058	8	60	gly	glycosylation	1371:1383	arg2	sites					1385:1389	the glycosylation sites	1367:1389	the glycosylation sites in the CUB domains of BMP-1	1367:1417	The study showed that the glycosylation sites in the CUB domains of BMP-1 are important for secretion and stability of the molecule.
12218058	8	60	gly	glycosylation	1371:1383	arg2	important					1423:1431	important	1423:1431	important	1423:1431	The study showed that the glycosylation sites in the CUB domains of BMP-1 are important for secretion and stability of the molecule.
12218058	2	61	theme	Asn	566:568	arg1	prodomain					452:460	prodomain	452:460	prodomain	452:460	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	61	theme	Asn	566:568	arg1	Asn					443:445	Asn(91)	443:449	Asn(91) (prodomain)	443:461	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	61	theme	Asn	566:568	arg1	sites					416:420	six potential N-linked glycosylation sites	379:420	six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726)	379:573	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	2	61	theme	Asn	566:568	arg1	domain					529:534	CUB1 domain	524:534	CUB1 domain	524:534	Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain.
12218058	6	62	gly	glycosylation	1076:1088	arg2	sites					1090:1094	individual glycosylation sites	1065:1094	individual glycosylation sites	1065:1094	BMP-1 molecules lacking individual glycosylation sites were efficiently secreted and exhibited full procollagen C-proteinase activity, but N332Q and N599Q exhibited a slower rate of cleavage.
12218058	1	63	theme	other	311:315	arg1	proteins					327:334	other precursor proteins	311:334	other precursor proteins	311:334	Bone morphogenetic protein (BMP)-1 is a glycosylated metalloproteinase that is fundamental to the synthesis of a normal extracellular matrix because it cleaves type I procollagen, as well as other precursor proteins.
12218058	8	64	from	sites	1385:1389	arg1	BMP-1					1413:1417	BMP-1	1413:1417	BMP-1	1413:1417	The study showed that the glycosylation sites in the CUB domains of BMP-1 are important for secretion and stability of the molecule.
12218058	8	64	from	sites	1385:1389	arg1	domains					1402:1408	the CUB domains	1394:1408	the CUB domains of BMP-1	1394:1417	The study showed that the glycosylation sites in the CUB domains of BMP-1 are important for secretion and stability of the molecule.
12218058	3	65	theme	sialic	720:725	arg1	acid					727:730	sialic acid	720:730	sialic acid	720:730	In this study we showed that all these sites are N-glycosylated with complex-type oligosaccharides containing sialic acid, except Asn(726) presumably because proline occurs immediately C-terminal of threonine in the consensus sequence.
12218058	1	66	theme	normal	233:238	arg1	matrix					254:259	a normal extracellular matrix	231:259	a normal extracellular matrix	231:259	Bone morphogenetic protein (BMP)-1 is a glycosylated metalloproteinase that is fundamental to the synthesis of a normal extracellular matrix because it cleaves type I procollagen, as well as other precursor proteins.
1820200	2	0	theme	amino	540:544	arg1	sequencing					551:560	amino acid sequencing	540:560	amino acid sequencing	540:560	Following purification by reverse-phase HPLC and identification by amino acid sequencing, the glycopeptides were analysed by one- and two-dimensional 1H NMR spectroscopy.
1820200	1	1	gly	glycoprotein	231:242	arg1	glycoprotein					231:242	the heterodimeric glycoprotein hormone	213:250	the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG)	213:286	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	2	2	theme	NMR	626:628	arg1	spectroscopy					630:641	one- and two-dimensional 1H NMR spectroscopy	598:641	one- and two-dimensional 1H NMR spectroscopy	598:641	Following purification by reverse-phase HPLC and identification by amino acid sequencing, the glycopeptides were analysed by one- and two-dimensional 1H NMR spectroscopy.
1820200	0	3	theme	one-	104:107	arg1	spectroscopy					136:147	one- and two-dimensional 1H NMR spectroscopy	104:147	one- and two-dimensional 1H NMR spectroscopy	104:147	Site-specific N-glycosylation of human chorionic gonadotrophin--structural analysis of glycopeptides by one- and two-dimensional 1H NMR spectroscopy.
1820200	1	4	theme	N-glycosylated	378:391	arg1	beta					372:375	hCG beta	368:375	hCG beta (N-glycosylated at Asn-13 and Asn-30)	368:413	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	1	4	theme	N-glycosylated	378:391	arg1	subunits					307:314	subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30)	307:413	subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30)	307:413	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	1	5	theme	hCG	316:318	arg1	alpha					320:324	hCG alpha	316:324	hCG alpha (N-glycosylated at Asn-52 and Asn-78)	316:362	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	1	5	theme	hCG	316:318	arg1	subunits					307:314	subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30)	307:413	subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30)	307:413	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	0	6	theme	1H	129:130	arg1	spectroscopy					136:147	one- and two-dimensional 1H NMR spectroscopy	104:147	one- and two-dimensional 1H NMR spectroscopy	104:147	Site-specific N-glycosylation of human chorionic gonadotrophin--structural analysis of glycopeptides by one- and two-dimensional 1H NMR spectroscopy.
1820200	3	7	theme	oligosaccharide	1772:1786	arg1	structures					1788:1797	the oligosaccharide structures	1768:1797	the oligosaccharide structures	1768:1797	The distinct site-specific distribution of the oligosaccharide structures among individual N-glycosylation sites of hCG appears to reflect primarily the influence of the surrounding protein structure on the substrate accessibility of the Golgi processing enzymes alpha-mannosidase II, GlcNAc transferase II and alpha 1,6-fucosyltransferase.
1820200	1	8	from	Asn-78	356:361	arg1	N-glycosylated					327:340	N-glycosylated	327:340	N-glycosylated	327:340	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	0	9	gly	glycopeptides	87:99	arg2	glycopeptides					87:99	glycopeptides	87:99	glycopeptides	87:99	Site-specific N-glycosylation of human chorionic gonadotrophin--structural analysis of glycopeptides by one- and two-dimensional 1H NMR spectroscopy.
1820200	0	10	theme	two-dimensional	113:127	arg1	spectroscopy					136:147	one- and two-dimensional 1H NMR spectroscopy	104:147	one- and two-dimensional 1H NMR spectroscopy	104:147	Site-specific N-glycosylation of human chorionic gonadotrophin--structural analysis of glycopeptides by one- and two-dimensional 1H NMR spectroscopy.
1820200	3	11	theme	surrounding	1895:1905	arg1	structure					1915:1923	the surrounding protein structure	1891:1923	the surrounding protein structure	1891:1923	The distinct site-specific distribution of the oligosaccharide structures among individual N-glycosylation sites of hCG appears to reflect primarily the influence of the surrounding protein structure on the substrate accessibility of the Golgi processing enzymes alpha-mannosidase II, GlcNAc transferase II and alpha 1,6-fucosyltransferase.
1820200	1	12	from	Asn-52	345:350	arg1	N-glycosylated					327:340	N-glycosylated	327:340	N-glycosylated	327:340	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	1	13	theme	heterodimeric	217:229	arg1	hormone					244:250	the heterodimeric glycoprotein hormone	213:250	the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG)	213:286	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	0	14	theme	NMR	132:134	arg1	spectroscopy					136:147	one- and two-dimensional 1H NMR spectroscopy	104:147	one- and two-dimensional 1H NMR spectroscopy	104:147	Site-specific N-glycosylation of human chorionic gonadotrophin--structural analysis of glycopeptides by one- and two-dimensional 1H NMR spectroscopy.
1820200	3	15	gly	N-glycosylation	1816:1830	arg2	hCG					1841:1843	hCG	1841:1843	hCG	1841:1843	The distinct site-specific distribution of the oligosaccharide structures among individual N-glycosylation sites of hCG appears to reflect primarily the influence of the surrounding protein structure on the substrate accessibility of the Golgi processing enzymes alpha-mannosidase II, GlcNAc transferase II and alpha 1,6-fucosyltransferase.
1820200	3	15	gly	N-glycosylation	1816:1830	arg1	hCG					1841:1843	hCG	1841:1843	hCG	1841:1843	The distinct site-specific distribution of the oligosaccharide structures among individual N-glycosylation sites of hCG appears to reflect primarily the influence of the surrounding protein structure on the substrate accessibility of the Golgi processing enzymes alpha-mannosidase II, GlcNAc transferase II and alpha 1,6-fucosyltransferase.
1820200	3	15	gly	N-glycosylation	1816:1830	arg2	sites					1832:1836	individual N-glycosylation sites	1805:1836	individual N-glycosylation sites of hCG	1805:1843	The distinct site-specific distribution of the oligosaccharide structures among individual N-glycosylation sites of hCG appears to reflect primarily the influence of the surrounding protein structure on the substrate accessibility of the Golgi processing enzymes alpha-mannosidase II, GlcNAc transferase II and alpha 1,6-fucosyltransferase.
1820200	1	16	theme	glycoprotein	231:242	arg1	hormone					244:250	the heterodimeric glycoprotein hormone	213:250	the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG)	213:286	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	1	17	from	Asn-30	407:412	arg1	N-glycosylated					378:391	N-glycosylated	378:391	N-glycosylated	378:391	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	1	18	gly	N-glycosylated	378:391	arg1	beta					372:375	hCG beta	368:375	hCG beta (N-glycosylated at Asn-13 and Asn-30)	368:413	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	1	18	gly	N-glycosylated	378:391	arg2	Asn-30					407:412	Asn-30	407:412	Asn-30	407:412	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	1	18	gly	N-glycosylated	378:391	arg2	Asn-13					396:401	Asn-13	396:401	Asn-13	396:401	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	1	18	gly	N-glycosylated	378:391	arg1	subunits					307:314	subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30)	307:413	subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30)	307:413	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	1	19	theme	hormone	244:250	arg1	gonadotrophin					268:280	the heterodimeric glycoprotein hormone human chorionic gonadotrophin	213:280	the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG)	213:286	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	1	19	theme	hormone	244:250	arg1	hCG					283:285	hCG	283:285	hCG	283:285	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	0	20	theme	Site-specific	0:12	arg1	N-glycosylation					14:28	Site-specific N-glycosylation	0:28	Site-specific N-glycosylation of human chorionic gonadotrophin--structural analysis of glycopeptides by one- and two-dimensional 1H NMR spectroscopy.	0:148	Site-specific N-glycosylation of human chorionic gonadotrophin--structural analysis of glycopeptides by one- and two-dimensional 1H NMR spectroscopy.
1820200	1	21	from	Asn-13	396:401	arg1	N-glycosylated					378:391	N-glycosylated	378:391	N-glycosylated	378:391	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	3	22	theme	hCG	1841:1843	arg1	hCG					1841:1843	hCG	1841:1843	hCG	1841:1843	The distinct site-specific distribution of the oligosaccharide structures among individual N-glycosylation sites of hCG appears to reflect primarily the influence of the surrounding protein structure on the substrate accessibility of the Golgi processing enzymes alpha-mannosidase II, GlcNAc transferase II and alpha 1,6-fucosyltransferase.
1820200	3	22	theme	hCG	1841:1843	arg1	sites					1832:1836	individual N-glycosylation sites	1805:1836	individual N-glycosylation sites of hCG	1805:1843	The distinct site-specific distribution of the oligosaccharide structures among individual N-glycosylation sites of hCG appears to reflect primarily the influence of the surrounding protein structure on the substrate accessibility of the Golgi processing enzymes alpha-mannosidase II, GlcNAc transferase II and alpha 1,6-fucosyltransferase.
1820200	1	23	theme	human	252:256	arg1	gonadotrophin					268:280	the heterodimeric glycoprotein hormone human chorionic gonadotrophin	213:280	the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG)	213:286	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	1	23	theme	human	252:256	arg1	hCG					283:285	hCG	283:285	hCG	283:285	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	0	24	theme	human	33:37	arg1	analysis					75:82	human chorionic gonadotrophin--structural analysis	33:82	human chorionic gonadotrophin--structural analysis of glycopeptides	33:99	Site-specific N-glycosylation of human chorionic gonadotrophin--structural analysis of glycopeptides by one- and two-dimensional 1H NMR spectroscopy.
1820200	1	25	theme	chorionic	258:266	arg1	gonadotrophin					268:280	the heterodimeric glycoprotein hormone human chorionic gonadotrophin	213:280	the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG)	213:286	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	1	25	theme	chorionic	258:266	arg1	hCG					283:285	hCG	283:285	hCG	283:285	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	3	26	theme	protein	1907:1913	arg1	structure					1915:1923	the surrounding protein structure	1891:1923	the surrounding protein structure	1891:1923	The distinct site-specific distribution of the oligosaccharide structures among individual N-glycosylation sites of hCG appears to reflect primarily the influence of the surrounding protein structure on the substrate accessibility of the Golgi processing enzymes alpha-mannosidase II, GlcNAc transferase II and alpha 1,6-fucosyltransferase.
1820200	2	27	theme	one-	598:601	arg1	spectroscopy					630:641	one- and two-dimensional 1H NMR spectroscopy	598:641	one- and two-dimensional 1H NMR spectroscopy	598:641	Following purification by reverse-phase HPLC and identification by amino acid sequencing, the glycopeptides were analysed by one- and two-dimensional 1H NMR spectroscopy.
1820200	3	28	theme	individual	1805:1814	arg1	hCG					1841:1843	hCG	1841:1843	hCG	1841:1843	The distinct site-specific distribution of the oligosaccharide structures among individual N-glycosylation sites of hCG appears to reflect primarily the influence of the surrounding protein structure on the substrate accessibility of the Golgi processing enzymes alpha-mannosidase II, GlcNAc transferase II and alpha 1,6-fucosyltransferase.
1820200	3	28	theme	individual	1805:1814	arg1	sites					1832:1836	individual N-glycosylation sites	1805:1836	individual N-glycosylation sites of hCG	1805:1843	The distinct site-specific distribution of the oligosaccharide structures among individual N-glycosylation sites of hCG appears to reflect primarily the influence of the surrounding protein structure on the substrate accessibility of the Golgi processing enzymes alpha-mannosidase II, GlcNAc transferase II and alpha 1,6-fucosyltransferase.
1820200	1	29	theme	gonadotrophin	268:280	arg1	sites					204:208	individual N-glycosylation sites	177:208	individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG)	177:286	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	1	29	theme	gonadotrophin	268:280	arg1	gonadotrophin					268:280	the heterodimeric glycoprotein hormone human chorionic gonadotrophin	213:280	the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG)	213:286	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	0	30	theme	gonadotrophin--structural	49:73	arg1	analysis					75:82	human chorionic gonadotrophin--structural analysis	33:82	human chorionic gonadotrophin--structural analysis of glycopeptides	33:99	Site-specific N-glycosylation of human chorionic gonadotrophin--structural analysis of glycopeptides by one- and two-dimensional 1H NMR spectroscopy.
1820200	3	31	theme	structure	1915:1923	arg1	influence					1878:1886	the influence	1874:1886	the influence of the surrounding protein structure on the substrate accessibility of the Golgi processing enzymes alpha-mannosidase II, GlcNAc transferase II and alpha 1,6-fucosyltransferase	1874:2063	The distinct site-specific distribution of the oligosaccharide structures among individual N-glycosylation sites of hCG appears to reflect primarily the influence of the surrounding protein structure on the substrate accessibility of the Golgi processing enzymes alpha-mannosidase II, GlcNAc transferase II and alpha 1,6-fucosyltransferase.
1820200	3	32	theme	N-glycosylation	1816:1830	arg1	hCG					1841:1843	hCG	1841:1843	hCG	1841:1843	The distinct site-specific distribution of the oligosaccharide structures among individual N-glycosylation sites of hCG appears to reflect primarily the influence of the surrounding protein structure on the substrate accessibility of the Golgi processing enzymes alpha-mannosidase II, GlcNAc transferase II and alpha 1,6-fucosyltransferase.
1820200	3	32	theme	N-glycosylation	1816:1830	arg1	sites					1832:1836	individual N-glycosylation sites	1805:1836	individual N-glycosylation sites of hCG	1805:1843	The distinct site-specific distribution of the oligosaccharide structures among individual N-glycosylation sites of hCG appears to reflect primarily the influence of the surrounding protein structure on the substrate accessibility of the Golgi processing enzymes alpha-mannosidase II, GlcNAc transferase II and alpha 1,6-fucosyltransferase.
1820200	3	33	theme	distinct	1729:1736	arg1	distribution					1752:1763	The distinct site-specific distribution	1725:1763	The distinct site-specific distribution of the oligosaccharide structures among individual N-glycosylation sites of hCG	1725:1843	The distinct site-specific distribution of the oligosaccharide structures among individual N-glycosylation sites of hCG appears to reflect primarily the influence of the surrounding protein structure on the substrate accessibility of the Golgi processing enzymes alpha-mannosidase II, GlcNAc transferase II and alpha 1,6-fucosyltransferase.
1820200	1	34	with	digestion	418:426	arg1	chymotrypsin					445:456	chymotrypsin	445:456	chymotrypsin	445:456	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	1	34	with	digestion	418:426	arg1	trypsin					433:439	trypsin	433:439	trypsin	433:439	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	0	35	theme	chorionic	39:47	arg1	analysis					75:82	human chorionic gonadotrophin--structural analysis	33:82	human chorionic gonadotrophin--structural analysis of glycopeptides	33:99	Site-specific N-glycosylation of human chorionic gonadotrophin--structural analysis of glycopeptides by one- and two-dimensional 1H NMR spectroscopy.
1820200	3	36	theme	structures	1788:1797	arg1	distribution					1752:1763	The distinct site-specific distribution	1725:1763	The distinct site-specific distribution of the oligosaccharide structures among individual N-glycosylation sites of hCG	1725:1843	The distinct site-specific distribution of the oligosaccharide structures among individual N-glycosylation sites of hCG appears to reflect primarily the influence of the surrounding protein structure on the substrate accessibility of the Golgi processing enzymes alpha-mannosidase II, GlcNAc transferase II and alpha 1,6-fucosyltransferase.
1820200	0	37	gly	N-glycosylation	14:28	arg1	analysis					75:82	human chorionic gonadotrophin--structural analysis	33:82	human chorionic gonadotrophin--structural analysis of glycopeptides	33:99	Site-specific N-glycosylation of human chorionic gonadotrophin--structural analysis of glycopeptides by one- and two-dimensional 1H NMR spectroscopy.
1820200	2	38	theme	acid	546:549	arg1	sequencing					551:560	amino acid sequencing	540:560	amino acid sequencing	540:560	Following purification by reverse-phase HPLC and identification by amino acid sequencing, the glycopeptides were analysed by one- and two-dimensional 1H NMR spectroscopy.
1820200	1	39	gly	N-glycosylated	327:340	arg1	alpha					320:324	hCG alpha	316:324	hCG alpha (N-glycosylated at Asn-52 and Asn-78)	316:362	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	1	39	gly	N-glycosylated	327:340	arg2	Asn-78					356:361	Asn-78	356:361	Asn-78	356:361	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	1	39	gly	N-glycosylated	327:340	arg1	subunits					307:314	subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30)	307:413	subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30)	307:413	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	1	39	gly	N-glycosylated	327:340	arg2	Asn-52					345:350	Asn-52	345:350	Asn-52	345:350	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	0	40	theme	analysis	75:82	arg1	N-glycosylation					14:28	Site-specific N-glycosylation	0:28	Site-specific N-glycosylation of human chorionic gonadotrophin--structural analysis of glycopeptides by one- and two-dimensional 1H NMR spectroscopy.	0:148	Site-specific N-glycosylation of human chorionic gonadotrophin--structural analysis of glycopeptides by one- and two-dimensional 1H NMR spectroscopy.
1820200	3	41	theme	substrate	1932:1940	arg1	accessibility					1942:1954	the substrate accessibility	1928:1954	the substrate accessibility of the Golgi processing enzymes alpha-mannosidase II, GlcNAc transferase II and alpha 1,6-fucosyltransferase	1928:2063	The distinct site-specific distribution of the oligosaccharide structures among individual N-glycosylation sites of hCG appears to reflect primarily the influence of the surrounding protein structure on the substrate accessibility of the Golgi processing enzymes alpha-mannosidase II, GlcNAc transferase II and alpha 1,6-fucosyltransferase.
1820200	1	42	gly	N-glycosylation	188:202	arg1	gonadotrophin					268:280	the heterodimeric glycoprotein hormone human chorionic gonadotrophin	213:280	the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG)	213:286	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	1	42	gly	N-glycosylation	188:202	arg2	sites					204:208	individual N-glycosylation sites	177:208	individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG)	177:286	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	1	42	gly	N-glycosylation	188:202	arg2	gonadotrophin					268:280	the heterodimeric glycoprotein hormone human chorionic gonadotrophin	213:280	the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG)	213:286	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	1	42	gly	N-glycosylation	188:202	arg1	hCG					283:285	hCG	283:285	hCG	283:285	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	1	43	dep	alpha	320:324	arg1	N-glycosylated					327:340	N-glycosylated	327:340	N-glycosylated	327:340	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	3	44	dep	enzymes	1980:1986	arg1	alpha-mannosidase					1988:2004	alpha-mannosidase II	1988:2007	the Golgi processing enzymes alpha-mannosidase II	1959:2007	The distinct site-specific distribution of the oligosaccharide structures among individual N-glycosylation sites of hCG appears to reflect primarily the influence of the surrounding protein structure on the substrate accessibility of the Golgi processing enzymes alpha-mannosidase II, GlcNAc transferase II and alpha 1,6-fucosyltransferase.
1820200	3	45	theme	alpha	2036:2040	arg1	enzymes					1980:1986	Golgi processing enzymes	1963:1986	the Golgi processing enzymes alpha-mannosidase II	1959:2007	The distinct site-specific distribution of the oligosaccharide structures among individual N-glycosylation sites of hCG appears to reflect primarily the influence of the surrounding protein structure on the substrate accessibility of the Golgi processing enzymes alpha-mannosidase II, GlcNAc transferase II and alpha 1,6-fucosyltransferase.
1820200	3	45	theme	alpha	2036:2040	arg1	1,6-fucosyltransferase					2042:2063	alpha 1,6-fucosyltransferase	2036:2063	alpha 1,6-fucosyltransferase	2036:2063	The distinct site-specific distribution of the oligosaccharide structures among individual N-glycosylation sites of hCG appears to reflect primarily the influence of the surrounding protein structure on the substrate accessibility of the Golgi processing enzymes alpha-mannosidase II, GlcNAc transferase II and alpha 1,6-fucosyltransferase.
1820200	1	46	theme	hCG	368:370	arg1	beta					372:375	hCG beta	368:375	hCG beta (N-glycosylated at Asn-13 and Asn-30)	368:413	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	1	46	theme	hCG	368:370	arg1	subunits					307:314	subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30)	307:413	subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30)	307:413	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	2	47	theme	1H	623:624	arg1	spectroscopy					630:641	one- and two-dimensional 1H NMR spectroscopy	598:641	one- and two-dimensional 1H NMR spectroscopy	598:641	Following purification by reverse-phase HPLC and identification by amino acid sequencing, the glycopeptides were analysed by one- and two-dimensional 1H NMR spectroscopy.
1820200	3	48	theme	site-specific	1738:1750	arg1	distribution					1752:1763	The distinct site-specific distribution	1725:1763	The distinct site-specific distribution of the oligosaccharide structures among individual N-glycosylation sites of hCG	1725:1843	The distinct site-specific distribution of the oligosaccharide structures among individual N-glycosylation sites of hCG appears to reflect primarily the influence of the surrounding protein structure on the substrate accessibility of the Golgi processing enzymes alpha-mannosidase II, GlcNAc transferase II and alpha 1,6-fucosyltransferase.
1820200	3	49	theme	enzymes	1980:1986	arg1	accessibility					1942:1954	the substrate accessibility	1928:1954	the substrate accessibility of the Golgi processing enzymes alpha-mannosidase II, GlcNAc transferase II and alpha 1,6-fucosyltransferase	1928:2063	The distinct site-specific distribution of the oligosaccharide structures among individual N-glycosylation sites of hCG appears to reflect primarily the influence of the surrounding protein structure on the substrate accessibility of the Golgi processing enzymes alpha-mannosidase II, GlcNAc transferase II and alpha 1,6-fucosyltransferase.
1820200	2	50	theme	two-dimensional	607:621	arg1	spectroscopy					630:641	one- and two-dimensional 1H NMR spectroscopy	598:641	one- and two-dimensional 1H NMR spectroscopy	598:641	Following purification by reverse-phase HPLC and identification by amino acid sequencing, the glycopeptides were analysed by one- and two-dimensional 1H NMR spectroscopy.
1820200	1	51	dep	subunits	307:314	arg1	beta					372:375	hCG beta	368:375	hCG beta (N-glycosylated at Asn-13 and Asn-30)	368:413	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	1	51	dep	subunits	307:314	arg1	alpha					320:324	hCG alpha	316:324	hCG alpha (N-glycosylated at Asn-52 and Asn-78)	316:362	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	1	51	dep	subunits	307:314	arg1	subunits					307:314	subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30)	307:413	subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30)	307:413	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	2	52	gly	glycopeptides	567:579	arg2	glycopeptides					567:579	the glycopeptides	563:579	the glycopeptides	563:579	Following purification by reverse-phase HPLC and identification by amino acid sequencing, the glycopeptides were analysed by one- and two-dimensional 1H NMR spectroscopy.
1820200	3	53	theme	GlcNAc	2010:2015	arg1	enzymes					1980:1986	Golgi processing enzymes	1963:1986	the Golgi processing enzymes alpha-mannosidase II	1959:2007	The distinct site-specific distribution of the oligosaccharide structures among individual N-glycosylation sites of hCG appears to reflect primarily the influence of the surrounding protein structure on the substrate accessibility of the Golgi processing enzymes alpha-mannosidase II, GlcNAc transferase II and alpha 1,6-fucosyltransferase.
1820200	3	53	theme	GlcNAc	2010:2015	arg1	transferase					2017:2027	GlcNAc transferase II	2010:2030	GlcNAc transferase II	2010:2030	The distinct site-specific distribution of the oligosaccharide structures among individual N-glycosylation sites of hCG appears to reflect primarily the influence of the surrounding protein structure on the substrate accessibility of the Golgi processing enzymes alpha-mannosidase II, GlcNAc transferase II and alpha 1,6-fucosyltransferase.
1820200	1	54	theme	individual	177:186	arg1	sites					204:208	individual N-glycosylation sites	177:208	individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG)	177:286	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	1	54	theme	individual	177:186	arg1	gonadotrophin					268:280	the heterodimeric glycoprotein hormone human chorionic gonadotrophin	213:280	the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG)	213:286	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	2	55	theme	reverse-phase	499:511	arg1	HPLC					513:516	reverse-phase HPLC	499:516	reverse-phase HPLC	499:516	Following purification by reverse-phase HPLC and identification by amino acid sequencing, the glycopeptides were analysed by one- and two-dimensional 1H NMR spectroscopy.
1820200	1	56	theme	N-glycosylation	188:202	arg1	sites					204:208	individual N-glycosylation sites	177:208	individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG)	177:286	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	1	56	theme	N-glycosylation	188:202	arg1	gonadotrophin					268:280	the heterodimeric glycoprotein hormone human chorionic gonadotrophin	213:280	the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG)	213:286	Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained from subunits hCG alpha (N-glycosylated at Asn-52 and Asn-78) and hCG beta (N-glycosylated at Asn-13 and Asn-30) by digestion with trypsin and chymotrypsin, respectively.
1820200	3	57	theme	Golgi	1963:1967	arg1	enzymes					1980:1986	Golgi processing enzymes	1963:1986	the Golgi processing enzymes alpha-mannosidase II	1959:2007	The distinct site-specific distribution of the oligosaccharide structures among individual N-glycosylation sites of hCG appears to reflect primarily the influence of the surrounding protein structure on the substrate accessibility of the Golgi processing enzymes alpha-mannosidase II, GlcNAc transferase II and alpha 1,6-fucosyltransferase.
1820200	3	57	theme	Golgi	1963:1967	arg1	1,6-fucosyltransferase					2042:2063	alpha 1,6-fucosyltransferase	2036:2063	alpha 1,6-fucosyltransferase	2036:2063	The distinct site-specific distribution of the oligosaccharide structures among individual N-glycosylation sites of hCG appears to reflect primarily the influence of the surrounding protein structure on the substrate accessibility of the Golgi processing enzymes alpha-mannosidase II, GlcNAc transferase II and alpha 1,6-fucosyltransferase.
1820200	3	57	theme	Golgi	1963:1967	arg1	transferase					2017:2027	GlcNAc transferase II	2010:2030	GlcNAc transferase II	2010:2030	The distinct site-specific distribution of the oligosaccharide structures among individual N-glycosylation sites of hCG appears to reflect primarily the influence of the surrounding protein structure on the substrate accessibility of the Golgi processing enzymes alpha-mannosidase II, GlcNAc transferase II and alpha 1,6-fucosyltransferase.
1820200	0	58	theme	glycopeptides	87:99	arg1	analysis					75:82	human chorionic gonadotrophin--structural analysis	33:82	human chorionic gonadotrophin--structural analysis of glycopeptides	33:99	Site-specific N-glycosylation of human chorionic gonadotrophin--structural analysis of glycopeptides by one- and two-dimensional 1H NMR spectroscopy.
1820200	3	59	from	influence	1878:1886	arg1	accessibility					1942:1954	the substrate accessibility	1928:1954	the substrate accessibility of the Golgi processing enzymes alpha-mannosidase II, GlcNAc transferase II and alpha 1,6-fucosyltransferase	1928:2063	The distinct site-specific distribution of the oligosaccharide structures among individual N-glycosylation sites of hCG appears to reflect primarily the influence of the surrounding protein structure on the substrate accessibility of the Golgi processing enzymes alpha-mannosidase II, GlcNAc transferase II and alpha 1,6-fucosyltransferase.
1820200	3	60	theme	processing	1969:1978	arg1	enzymes					1980:1986	Golgi processing enzymes	1963:1986	the Golgi processing enzymes alpha-mannosidase II	1959:2007	The distinct site-specific distribution of the oligosaccharide structures among individual N-glycosylation sites of hCG appears to reflect primarily the influence of the surrounding protein structure on the substrate accessibility of the Golgi processing enzymes alpha-mannosidase II, GlcNAc transferase II and alpha 1,6-fucosyltransferase.
1820200	3	60	theme	processing	1969:1978	arg1	1,6-fucosyltransferase					2042:2063	alpha 1,6-fucosyltransferase	2036:2063	alpha 1,6-fucosyltransferase	2036:2063	The distinct site-specific distribution of the oligosaccharide structures among individual N-glycosylation sites of hCG appears to reflect primarily the influence of the surrounding protein structure on the substrate accessibility of the Golgi processing enzymes alpha-mannosidase II, GlcNAc transferase II and alpha 1,6-fucosyltransferase.
1820200	3	60	theme	processing	1969:1978	arg1	transferase					2017:2027	GlcNAc transferase II	2010:2030	GlcNAc transferase II	2010:2030	The distinct site-specific distribution of the oligosaccharide structures among individual N-glycosylation sites of hCG appears to reflect primarily the influence of the surrounding protein structure on the substrate accessibility of the Golgi processing enzymes alpha-mannosidase II, GlcNAc transferase II and alpha 1,6-fucosyltransferase.
7620335	2	0	theme	endoproteinase	576:589	arg1	Asp-N					591:595	endoproteinase Asp-N	576:595	endoproteinase Asp-N followed by reversed-phase HPLC	576:627	We determined the structure of oligosaccharides in the XAP region of human factor X. Four glycopeptides each containing a glycosylation site were isolated by digestion of XAP with endoproteinase Asp-N followed by reversed-phase HPLC.
7620335	0	1	from	structures	38:47	arg1	site					120:123	each glycosylation site	101:123	each glycosylation site	101:123	Identification of the oligosaccharide structures of human coagulation factor X activation peptide at each glycosylation site.
7620335	7	2	theme	monosialyl	1153:1162	arg1	oligosaccharides					1164:1179	Six neutral and twelve monosialyl oligosaccharides	1130:1179	Six neutral and twelve monosialyl oligosaccharides isolated from both N-linked glycosylation sites	1130:1227	Six neutral and twelve monosialyl oligosaccharides isolated from both N-linked glycosylation sites showed similar elution profiles composed of bi-, tri- and tetra-antennary complex type oligosaccharides.
7620335	2	3	with	digestion	554:562	arg1	Asp-N					591:595	endoproteinase Asp-N	576:595	endoproteinase Asp-N followed by reversed-phase HPLC	576:627	We determined the structure of oligosaccharides in the XAP region of human factor X. Four glycopeptides each containing a glycosylation site were isolated by digestion of XAP with endoproteinase Asp-N followed by reversed-phase HPLC.
7620335	2	4	theme	XAP	567:569	arg1	digestion					554:562	digestion	554:562	digestion of XAP with endoproteinase Asp-N followed by reversed-phase HPLC	554:627	We determined the structure of oligosaccharides in the XAP region of human factor X. Four glycopeptides each containing a glycosylation site were isolated by digestion of XAP with endoproteinase Asp-N followed by reversed-phase HPLC.
7620335	10	5	theme	Gal	1663:1665	arg1	3GalNAc					1672:1678	disialylated Gal beta 3GalNAc	1650:1678	disialylated Gal beta 3GalNAc sequences	1650:1688	In addition, the structures of O-linked oligosaccharides at Thr17 and Thr29 residues were suggested to be disialylated Gal beta 3GalNAc sequences by their component analyses.
7620335	9	6	theme	Neu5Ac	1516:1521	arg1	residue					1535:1541	a Neu5Ac alpha 2-->6 residue	1514:1541	a Neu5Ac alpha 2-->6 residue	1514:1541	Two major monosialyl oligosaccharides were also biantennary without fucose and with a Neu5Ac alpha 2-->6 residue.
7620335	4	7	theme	anion-exchange	862:875	arg1	column					877:882	an anion-exchange column	859:882	an anion-exchange column	859:882	Pyridylamino(PA)-oligosaccharides were separated by HPLC into neutral and sialyl oligosaccharides using an anion-exchange column.
7620335	9	8	theme	2-->6	1529:1533	arg1	residue					1535:1541	a Neu5Ac alpha 2-->6 residue	1514:1541	a Neu5Ac alpha 2-->6 residue	1514:1541	Two major monosialyl oligosaccharides were also biantennary without fucose and with a Neu5Ac alpha 2-->6 residue.
7620335	9	9	theme	alpha	1523:1527	arg1	residue					1535:1541	a Neu5Ac alpha 2-->6 residue	1514:1541	a Neu5Ac alpha 2-->6 residue	1514:1541	Two major monosialyl oligosaccharides were also biantennary without fucose and with a Neu5Ac alpha 2-->6 residue.
7620335	10	10	theme	3GalNAc	1672:1678	arg1	structures					1561:1570	the structures	1557:1570	the structures of O-linked oligosaccharides at Thr17 and Thr29 residues	1557:1627	In addition, the structures of O-linked oligosaccharides at Thr17 and Thr29 residues were suggested to be disialylated Gal beta 3GalNAc sequences by their component analyses.
7620335	10	10	theme	3GalNAc	1672:1678	arg1	sequences					1680:1688	disialylated Gal beta 3GalNAc sequences	1650:1688	disialylated Gal beta 3GalNAc sequences	1650:1688	In addition, the structures of O-linked oligosaccharides at Thr17 and Thr29 residues were suggested to be disialylated Gal beta 3GalNAc sequences by their component analyses.
7620335	1	11	from	residues	274:281	arg1	oligosaccharides					238:253	two O-linked oligosaccharides	225:253	two O-linked oligosaccharides at Thr17 and Thr29 residues	225:281	Human blood coagulation factor X has two N-linked oligosaccharides at Asn39 and Asn49 residues and two O-linked oligosaccharides at Thr17 and Thr29 residues in the region of the factor X activation peptide (XAP) which is cleaved off during its activation by factor IXa.
7620335	1	11	from	residues	274:281	arg1	oligosaccharides					176:191	two N-linked oligosaccharides	163:191	two N-linked oligosaccharides at Asn39 and Asn49 residues	163:219	Human blood coagulation factor X has two N-linked oligosaccharides at Asn39 and Asn49 residues and two O-linked oligosaccharides at Thr17 and Thr29 residues in the region of the factor X activation peptide (XAP) which is cleaved off during its activation by factor IXa.
7620335	8	12	theme	predominant	1338:1348	arg1	biantennary					1392:1402	biantennary	1392:1402	biantennary	1392:1402	The predominant component in neutral oligosaccharides was biantennary without a fucose residue.
7620335	8	12	theme	predominant	1338:1348	arg1	component					1350:1358	The predominant component	1334:1358	The predominant component in neutral oligosaccharides	1334:1386	The predominant component in neutral oligosaccharides was biantennary without a fucose residue.
7620335	7	13	theme	N-linked	1200:1207	arg1	sites					1223:1227	both N-linked glycosylation sites	1195:1227	both N-linked glycosylation sites	1195:1227	Six neutral and twelve monosialyl oligosaccharides isolated from both N-linked glycosylation sites showed similar elution profiles composed of bi-, tri- and tetra-antennary complex type oligosaccharides.
7620335	1	14	from	residues	212:219	arg1	oligosaccharides					238:253	two O-linked oligosaccharides	225:253	two O-linked oligosaccharides at Thr17 and Thr29 residues	225:281	Human blood coagulation factor X has two N-linked oligosaccharides at Asn39 and Asn49 residues and two O-linked oligosaccharides at Thr17 and Thr29 residues in the region of the factor X activation peptide (XAP) which is cleaved off during its activation by factor IXa.
7620335	1	14	from	residues	212:219	arg1	oligosaccharides					176:191	two N-linked oligosaccharides	163:191	two N-linked oligosaccharides at Asn39 and Asn49 residues	163:219	Human blood coagulation factor X has two N-linked oligosaccharides at Asn39 and Asn49 residues and two O-linked oligosaccharides at Thr17 and Thr29 residues in the region of the factor X activation peptide (XAP) which is cleaved off during its activation by factor IXa.
7620335	10	15	theme	component	1699:1707	arg1	analyses					1709:1716	their component analyses	1693:1716	their component analyses	1693:1716	In addition, the structures of O-linked oligosaccharides at Thr17 and Thr29 residues were suggested to be disialylated Gal beta 3GalNAc sequences by their component analyses.
7620335	1	16	theme	factor	384:389	arg1	IXa					391:393	factor IXa	384:393	factor IXa	384:393	Human blood coagulation factor X has two N-linked oligosaccharides at Asn39 and Asn49 residues and two O-linked oligosaccharides at Thr17 and Thr29 residues in the region of the factor X activation peptide (XAP) which is cleaved off during its activation by factor IXa.
7620335	1	17	theme	Human	126:130	arg1	X					157:157	Human blood coagulation factor X	126:157	Human blood coagulation factor X	126:157	Human blood coagulation factor X has two N-linked oligosaccharides at Asn39 and Asn49 residues and two O-linked oligosaccharides at Thr17 and Thr29 residues in the region of the factor X activation peptide (XAP) which is cleaved off during its activation by factor IXa.
7620335	10	18	gly	disialylated	1650:1661	arg1	3GalNAc					1672:1678	disialylated Gal beta 3GalNAc	1650:1678	disialylated Gal beta 3GalNAc sequences	1650:1688	In addition, the structures of O-linked oligosaccharides at Thr17 and Thr29 residues were suggested to be disialylated Gal beta 3GalNAc sequences by their component analyses.
7620335	5	19	theme	two-dimensional	983:997	arg1	method					1013:1018	a two-dimensional sugar mapping method	981:1018	a two-dimensional sugar mapping method	981:1018	Structures of oligosaccharides and their contents at each glycosylation site were determined by a two-dimensional sugar mapping method.
7620335	1	20	theme	coagulation	138:148	arg1	X					157:157	Human blood coagulation factor X	126:157	Human blood coagulation factor X	126:157	Human blood coagulation factor X has two N-linked oligosaccharides at Asn39 and Asn49 residues and two O-linked oligosaccharides at Thr17 and Thr29 residues in the region of the factor X activation peptide (XAP) which is cleaved off during its activation by factor IXa.
7620335	2	21	theme	factor	471:476	arg1	region					455:460	the XAP region	447:460	the XAP region of human factor X. Four glycopeptides each containing a glycosylation site were isolated by digestion of XAP with endoproteinase Asp-N followed by reversed-phase HPLC	447:627	We determined the structure of oligosaccharides in the XAP region of human factor X. Four glycopeptides each containing a glycosylation site were isolated by digestion of XAP with endoproteinase Asp-N followed by reversed-phase HPLC.
7620335	0	22	theme	factor	70:75	arg1	peptide					90:96	human coagulation factor X activation peptide	52:96	human coagulation factor X activation peptide at each glycosylation site	52:123	Identification of the oligosaccharide structures of human coagulation factor X activation peptide at each glycosylation site.
7620335	1	23	theme	peptide	324:330	arg1	region					290:295	the region	286:295	the region of the factor X activation peptide (XAP) which is cleaved off during its activation by factor IXa	286:393	Human blood coagulation factor X has two N-linked oligosaccharides at Asn39 and Asn49 residues and two O-linked oligosaccharides at Thr17 and Thr29 residues in the region of the factor X activation peptide (XAP) which is cleaved off during its activation by factor IXa.
7620335	5	24	theme	contents	926:933	arg1	Structures					885:894	Structures	885:894	Structures of oligosaccharides and their contents at each glycosylation site	885:960	Structures of oligosaccharides and their contents at each glycosylation site were determined by a two-dimensional sugar mapping method.
7620335	6	25	theme	oligosaccharides	1049:1064	arg1	contents					1025:1032	The contents	1021:1032	The contents of the neutral oligosaccharides at Asn39 and Asn49 residues	1021:1092	The contents of the neutral oligosaccharides at Asn39 and Asn49 residues were 32.5% and 30.0%, respectively.
7620335	6	25	theme	oligosaccharides	1049:1064	arg1	%					1103:1103	32.5%	1099:1103	32.5%	1099:1103	The contents of the neutral oligosaccharides at Asn39 and Asn49 residues were 32.5% and 30.0%, respectively.
7620335	0	26	theme	activation	79:88	arg1	peptide					90:96	human coagulation factor X activation peptide	52:96	human coagulation factor X activation peptide at each glycosylation site	52:123	Identification of the oligosaccharide structures of human coagulation factor X activation peptide at each glycosylation site.
7620335	7	27	theme	elution	1244:1250	arg1	profiles					1252:1259	similar elution profiles	1236:1259	similar elution profiles composed of bi-, tri- and tetra-antennary complex type oligosaccharides	1236:1331	Six neutral and twelve monosialyl oligosaccharides isolated from both N-linked glycosylation sites showed similar elution profiles composed of bi-, tri- and tetra-antennary complex type oligosaccharides.
7620335	6	28	dep	Asn39	1069:1073	arg1	residues					1085:1092	residues	1085:1092	residues	1085:1092	The contents of the neutral oligosaccharides at Asn39 and Asn49 residues were 32.5% and 30.0%, respectively.
7620335	1	29	link	N-linked	167:174	arg1	oligosaccharides					176:191	two N-linked oligosaccharides	163:191	two N-linked oligosaccharides at Asn39 and Asn49 residues	163:219	Human blood coagulation factor X has two N-linked oligosaccharides at Asn39 and Asn49 residues and two O-linked oligosaccharides at Thr17 and Thr29 residues in the region of the factor X activation peptide (XAP) which is cleaved off during its activation by factor IXa.
7620335	4	30	theme	Pyridylamino	755:766	arg1	-oligosaccharides					771:787	Pyridylamino(PA)-oligosaccharides	755:787	Pyridylamino(PA)-oligosaccharides	755:787	Pyridylamino(PA)-oligosaccharides were separated by HPLC into neutral and sialyl oligosaccharides using an anion-exchange column.
7620335	10	31	link	O-linked	1575:1582	arg1	oligosaccharides					1584:1599	O-linked oligosaccharides	1575:1599	O-linked oligosaccharides	1575:1599	In addition, the structures of O-linked oligosaccharides at Thr17 and Thr29 residues were suggested to be disialylated Gal beta 3GalNAc sequences by their component analyses.
7620335	2	32	theme	reversed-phase	609:622	arg1	HPLC					624:627	reversed-phase HPLC	609:627	reversed-phase HPLC	609:627	We determined the structure of oligosaccharides in the XAP region of human factor X. Four glycopeptides each containing a glycosylation site were isolated by digestion of XAP with endoproteinase Asp-N followed by reversed-phase HPLC.
7620335	10	33	theme	oligosaccharides	1584:1599	arg1	structures					1561:1570	the structures	1557:1570	the structures of O-linked oligosaccharides at Thr17 and Thr29 residues	1557:1627	In addition, the structures of O-linked oligosaccharides at Thr17 and Thr29 residues were suggested to be disialylated Gal beta 3GalNAc sequences by their component analyses.
7620335	10	33	theme	oligosaccharides	1584:1599	arg1	sequences					1680:1688	disialylated Gal beta 3GalNAc sequences	1650:1688	disialylated Gal beta 3GalNAc sequences	1650:1688	In addition, the structures of O-linked oligosaccharides at Thr17 and Thr29 residues were suggested to be disialylated Gal beta 3GalNAc sequences by their component analyses.
7620335	7	34	theme	glycosylation	1209:1221	arg1	sites					1223:1227	both N-linked glycosylation sites	1195:1227	both N-linked glycosylation sites	1195:1227	Six neutral and twelve monosialyl oligosaccharides isolated from both N-linked glycosylation sites showed similar elution profiles composed of bi-, tri- and tetra-antennary complex type oligosaccharides.
7620335	5	35	theme	sugar	999:1003	arg1	method					1013:1018	a two-dimensional sugar mapping method	981:1018	a two-dimensional sugar mapping method	981:1018	Structures of oligosaccharides and their contents at each glycosylation site were determined by a two-dimensional sugar mapping method.
7620335	1	36	theme	factor	150:155	arg1	X					157:157	Human blood coagulation factor X	126:157	Human blood coagulation factor X	126:157	Human blood coagulation factor X has two N-linked oligosaccharides at Asn39 and Asn49 residues and two O-linked oligosaccharides at Thr17 and Thr29 residues in the region of the factor X activation peptide (XAP) which is cleaved off during its activation by factor IXa.
7620335	2	37	theme	XAP	451:453	arg1	region					455:460	the XAP region	447:460	the XAP region of human factor X. Four glycopeptides each containing a glycosylation site were isolated by digestion of XAP with endoproteinase Asp-N followed by reversed-phase HPLC	447:627	We determined the structure of oligosaccharides in the XAP region of human factor X. Four glycopeptides each containing a glycosylation site were isolated by digestion of XAP with endoproteinase Asp-N followed by reversed-phase HPLC.
7620335	4	38	theme	sialyl	829:834	arg1	oligosaccharides					836:851	sialyl oligosaccharides	829:851	sialyl oligosaccharides	829:851	Pyridylamino(PA)-oligosaccharides were separated by HPLC into neutral and sialyl oligosaccharides using an anion-exchange column.
7620335	0	39	theme	structures	38:47	arg1	Identification					0:13	Identification	0:13	Identification of the oligosaccharide structures of human coagulation factor X activation peptide at each glycosylation site.	0:124	Identification of the oligosaccharide structures of human coagulation factor X activation peptide at each glycosylation site.
7620335	9	40	theme	major	1434:1438	arg1	oligosaccharides					1451:1466	Two major monosialyl oligosaccharides	1430:1466	Two major monosialyl oligosaccharides	1430:1466	Two major monosialyl oligosaccharides were also biantennary without fucose and with a Neu5Ac alpha 2-->6 residue.
7620335	2	41	dep	glycopeptides	486:498	arg1	each					500:503	each	500:503	each	500:503	We determined the structure of oligosaccharides in the XAP region of human factor X. Four glycopeptides each containing a glycosylation site were isolated by digestion of XAP with endoproteinase Asp-N followed by reversed-phase HPLC.
7620335	10	42	theme	Thr29	1614:1618	arg1	residues					1620:1627	Thr17 and Thr29 residues	1604:1627	residues	1620:1627	In addition, the structures of O-linked oligosaccharides at Thr17 and Thr29 residues were suggested to be disialylated Gal beta 3GalNAc sequences by their component analyses.
7620335	0	43	theme	human	52:56	arg1	peptide					90:96	human coagulation factor X activation peptide	52:96	human coagulation factor X activation peptide at each glycosylation site	52:123	Identification of the oligosaccharide structures of human coagulation factor X activation peptide at each glycosylation site.
7620335	1	44	theme	X	311:311	arg1	XAP					333:335	XAP	333:335	XAP	333:335	Human blood coagulation factor X has two N-linked oligosaccharides at Asn39 and Asn49 residues and two O-linked oligosaccharides at Thr17 and Thr29 residues in the region of the factor X activation peptide (XAP) which is cleaved off during its activation by factor IXa.
7620335	1	44	theme	X	311:311	arg1	peptide					324:330	the factor X activation peptide	300:330	the factor X activation peptide (XAP) which is cleaved off during its activation by factor IXa	300:393	Human blood coagulation factor X has two N-linked oligosaccharides at Asn39 and Asn49 residues and two O-linked oligosaccharides at Thr17 and Thr29 residues in the region of the factor X activation peptide (XAP) which is cleaved off during its activation by factor IXa.
7620335	2	45	dep	region	455:460	arg1	isolated					542:549	isolated	542:549	were isolated by digestion of XAP with endoproteinase Asp-N followed by reversed-phase HPLC	537:627	We determined the structure of oligosaccharides in the XAP region of human factor X. Four glycopeptides each containing a glycosylation site were isolated by digestion of XAP with endoproteinase Asp-N followed by reversed-phase HPLC.
7620335	10	46	theme	Thr17	1604:1608	arg1	residues					1620:1627	Thr17 and Thr29 residues	1604:1627	residues	1620:1627	In addition, the structures of O-linked oligosaccharides at Thr17 and Thr29 residues were suggested to be disialylated Gal beta 3GalNAc sequences by their component analyses.
7620335	7	47	gly	glycosylation	1209:1221	arg2	sites					1223:1227	both N-linked glycosylation sites	1195:1227	both N-linked glycosylation sites	1195:1227	Six neutral and twelve monosialyl oligosaccharides isolated from both N-linked glycosylation sites showed similar elution profiles composed of bi-, tri- and tetra-antennary complex type oligosaccharides.
7620335	7	48	theme	type	1311:1314	arg1	oligosaccharides					1316:1331	tetra-antennary complex type oligosaccharides	1287:1331	tetra-antennary complex type oligosaccharides	1287:1331	Six neutral and twelve monosialyl oligosaccharides isolated from both N-linked glycosylation sites showed similar elution profiles composed of bi-, tri- and tetra-antennary complex type oligosaccharides.
7620335	9	49	theme	monosialyl	1440:1449	arg1	oligosaccharides					1451:1466	Two major monosialyl oligosaccharides	1430:1466	Two major monosialyl oligosaccharides	1430:1466	Two major monosialyl oligosaccharides were also biantennary without fucose and with a Neu5Ac alpha 2-->6 residue.
7620335	9	50	with	biantennary	1478:1488	arg1	residue					1535:1541	a Neu5Ac alpha 2-->6 residue	1514:1541	a Neu5Ac alpha 2-->6 residue	1514:1541	Two major monosialyl oligosaccharides were also biantennary without fucose and with a Neu5Ac alpha 2-->6 residue.
7620335	1	51	theme	Thr17	258:262	arg1	residues					274:281	Thr17 and Thr29 residues	258:281	residues	274:281	Human blood coagulation factor X has two N-linked oligosaccharides at Asn39 and Asn49 residues and two O-linked oligosaccharides at Thr17 and Thr29 residues in the region of the factor X activation peptide (XAP) which is cleaved off during its activation by factor IXa.
7620335	7	52	theme	tetra-antennary	1287:1301	arg1	oligosaccharides					1316:1331	tetra-antennary complex type oligosaccharides	1287:1331	tetra-antennary complex type oligosaccharides	1287:1331	Six neutral and twelve monosialyl oligosaccharides isolated from both N-linked glycosylation sites showed similar elution profiles composed of bi-, tri- and tetra-antennary complex type oligosaccharides.
7620335	3	53	link	N-linked	630:637	arg1	oligosaccharides					639:654	N-linked oligosaccharides	630:654	N-linked oligosaccharides released from the glycopeptides by glycoamidase A digestion	630:714	N-linked oligosaccharides released from the glycopeptides by glycoamidase A digestion were derivatized with 2-aminopyridine.
7620335	10	54	theme	beta	1667:1670	arg1	3GalNAc					1672:1678	disialylated Gal beta 3GalNAc	1650:1678	disialylated Gal beta 3GalNAc sequences	1650:1688	In addition, the structures of O-linked oligosaccharides at Thr17 and Thr29 residues were suggested to be disialylated Gal beta 3GalNAc sequences by their component analyses.
7620335	3	55	theme	glycoamidase	691:702	arg1	digestion					706:714	glycoamidase A digestion	691:714	glycoamidase A digestion	691:714	N-linked oligosaccharides released from the glycopeptides by glycoamidase A digestion were derivatized with 2-aminopyridine.
7620335	7	56	theme	neutral	1134:1140	arg1	oligosaccharides					1164:1179	Six neutral and twelve monosialyl oligosaccharides	1130:1179	Six neutral and twelve monosialyl oligosaccharides isolated from both N-linked glycosylation sites	1130:1227	Six neutral and twelve monosialyl oligosaccharides isolated from both N-linked glycosylation sites showed similar elution profiles composed of bi-, tri- and tetra-antennary complex type oligosaccharides.
7620335	1	57	theme	Thr29	268:272	arg1	residues					274:281	Thr17 and Thr29 residues	258:281	residues	274:281	Human blood coagulation factor X has two N-linked oligosaccharides at Asn39 and Asn49 residues and two O-linked oligosaccharides at Thr17 and Thr29 residues in the region of the factor X activation peptide (XAP) which is cleaved off during its activation by factor IXa.
7620335	10	58	theme	disialylated	1650:1661	arg1	3GalNAc					1672:1678	disialylated Gal beta 3GalNAc	1650:1678	disialylated Gal beta 3GalNAc sequences	1650:1688	In addition, the structures of O-linked oligosaccharides at Thr17 and Thr29 residues were suggested to be disialylated Gal beta 3GalNAc sequences by their component analyses.
7620335	1	59	contain	has	159:161	arg1	X					157:157	Human blood coagulation factor X	126:157	Human blood coagulation factor X	126:157	Human blood coagulation factor X has two N-linked oligosaccharides at Asn39 and Asn49 residues and two O-linked oligosaccharides at Thr17 and Thr29 residues in the region of the factor X activation peptide (XAP) which is cleaved off during its activation by factor IXa.
7620335	1	59	contain	has	159:161	arg2	oligosaccharides					176:191	two N-linked oligosaccharides	163:191	two N-linked oligosaccharides at Asn39 and Asn49 residues	163:219	Human blood coagulation factor X has two N-linked oligosaccharides at Asn39 and Asn49 residues and two O-linked oligosaccharides at Thr17 and Thr29 residues in the region of the factor X activation peptide (XAP) which is cleaved off during its activation by factor IXa.
7620335	1	59	contain	has	159:161	arg2	oligosaccharides					238:253	two O-linked oligosaccharides	225:253	two O-linked oligosaccharides at Thr17 and Thr29 residues	225:281	Human blood coagulation factor X has two N-linked oligosaccharides at Asn39 and Asn49 residues and two O-linked oligosaccharides at Thr17 and Thr29 residues in the region of the factor X activation peptide (XAP) which is cleaved off during its activation by factor IXa.
7620335	1	60	theme	N-linked	167:174	arg1	oligosaccharides					176:191	two N-linked oligosaccharides	163:191	two N-linked oligosaccharides at Asn39 and Asn49 residues	163:219	Human blood coagulation factor X has two N-linked oligosaccharides at Asn39 and Asn49 residues and two O-linked oligosaccharides at Thr17 and Thr29 residues in the region of the factor X activation peptide (XAP) which is cleaved off during its activation by factor IXa.
7620335	6	61	from	Asn49	1079:1083	arg1	contents					1025:1032	The contents	1021:1032	The contents of the neutral oligosaccharides at Asn39 and Asn49 residues	1021:1092	The contents of the neutral oligosaccharides at Asn39 and Asn49 residues were 32.5% and 30.0%, respectively.
7620335	6	61	from	Asn49	1079:1083	arg1	%					1103:1103	32.5%	1099:1103	32.5%	1099:1103	The contents of the neutral oligosaccharides at Asn39 and Asn49 residues were 32.5% and 30.0%, respectively.
7620335	6	61	from	Asn49	1079:1083	arg1	oligosaccharides					1049:1064	the neutral oligosaccharides	1037:1064	the neutral oligosaccharides at Asn39 and Asn49 residues	1037:1092	The contents of the neutral oligosaccharides at Asn39 and Asn49 residues were 32.5% and 30.0%, respectively.
7620335	5	62	theme	oligosaccharides	899:914	arg1	Structures					885:894	Structures	885:894	Structures of oligosaccharides and their contents at each glycosylation site	885:960	Structures of oligosaccharides and their contents at each glycosylation site were determined by a two-dimensional sugar mapping method.
7620335	1	63	link	O-linked	229:236	arg1	oligosaccharides					238:253	two O-linked oligosaccharides	225:253	two O-linked oligosaccharides at Thr17 and Thr29 residues	225:281	Human blood coagulation factor X has two N-linked oligosaccharides at Asn39 and Asn49 residues and two O-linked oligosaccharides at Thr17 and Thr29 residues in the region of the factor X activation peptide (XAP) which is cleaved off during its activation by factor IXa.
7620335	3	64	attach	released	656:663	arg2	oligosaccharides					639:654	N-linked oligosaccharides	630:654	N-linked oligosaccharides released from the glycopeptides by glycoamidase A digestion	630:714	N-linked oligosaccharides released from the glycopeptides by glycoamidase A digestion were derivatized with 2-aminopyridine.
7620335	3	64	attach	released	656:663	arg1	glycopeptides					674:686	the glycopeptides	670:686	the glycopeptides	670:686	N-linked oligosaccharides released from the glycopeptides by glycoamidase A digestion were derivatized with 2-aminopyridine.
7620335	2	65	theme	glycosylation	518:530	arg1	site					532:535	a glycosylation site	516:535	a glycosylation site	516:535	We determined the structure of oligosaccharides in the XAP region of human factor X. Four glycopeptides each containing a glycosylation site were isolated by digestion of XAP with endoproteinase Asp-N followed by reversed-phase HPLC.
7620335	5	66	theme	glycosylation	943:955	arg1	site					957:960	each glycosylation site	938:960	each glycosylation site	938:960	Structures of oligosaccharides and their contents at each glycosylation site were determined by a two-dimensional sugar mapping method.
7620335	0	67	from	site	120:123	arg1	peptide					90:96	human coagulation factor X activation peptide	52:96	human coagulation factor X activation peptide at each glycosylation site	52:123	Identification of the oligosaccharide structures of human coagulation factor X activation peptide at each glycosylation site.
7620335	0	67	from	site	120:123	arg1	structures					38:47	the oligosaccharide structures	18:47	the oligosaccharide structures of human coagulation factor X activation peptide at each glycosylation site	18:123	Identification of the oligosaccharide structures of human coagulation factor X activation peptide at each glycosylation site.
7620335	7	68	link	N-linked	1200:1207	arg1	sites					1223:1227	both N-linked glycosylation sites	1195:1227	both N-linked glycosylation sites	1195:1227	Six neutral and twelve monosialyl oligosaccharides isolated from both N-linked glycosylation sites showed similar elution profiles composed of bi-, tri- and tetra-antennary complex type oligosaccharides.
7620335	1	69	theme	blood	132:136	arg1	X					157:157	Human blood coagulation factor X	126:157	Human blood coagulation factor X	126:157	Human blood coagulation factor X has two N-linked oligosaccharides at Asn39 and Asn49 residues and two O-linked oligosaccharides at Thr17 and Thr29 residues in the region of the factor X activation peptide (XAP) which is cleaved off during its activation by factor IXa.
7620335	5	70	theme	mapping	1005:1011	arg1	method					1013:1018	a two-dimensional sugar mapping method	981:1018	a two-dimensional sugar mapping method	981:1018	Structures of oligosaccharides and their contents at each glycosylation site were determined by a two-dimensional sugar mapping method.
7620335	8	71	theme	neutral	1363:1369	arg1	oligosaccharides					1371:1386	neutral oligosaccharides	1363:1386	neutral oligosaccharides	1363:1386	The predominant component in neutral oligosaccharides was biantennary without a fucose residue.
7620335	0	72	theme	X	77:77	arg1	peptide					90:96	human coagulation factor X activation peptide	52:96	human coagulation factor X activation peptide at each glycosylation site	52:123	Identification of the oligosaccharide structures of human coagulation factor X activation peptide at each glycosylation site.
7620335	2	73	gly	glycosylation	518:530	arg2	site					532:535	a glycosylation site	516:535	a glycosylation site	516:535	We determined the structure of oligosaccharides in the XAP region of human factor X. Four glycopeptides each containing a glycosylation site were isolated by digestion of XAP with endoproteinase Asp-N followed by reversed-phase HPLC.
7620335	2	74	theme	human	465:469	arg1	factor					471:476	human factor	465:476	human factor	465:476	We determined the structure of oligosaccharides in the XAP region of human factor X. Four glycopeptides each containing a glycosylation site were isolated by digestion of XAP with endoproteinase Asp-N followed by reversed-phase HPLC.
7620335	0	75	theme	peptide	90:96	arg1	structures					38:47	the oligosaccharide structures	18:47	the oligosaccharide structures of human coagulation factor X activation peptide at each glycosylation site	18:123	Identification of the oligosaccharide structures of human coagulation factor X activation peptide at each glycosylation site.
7620335	6	76	theme	neutral	1041:1047	arg1	oligosaccharides					1049:1064	the neutral oligosaccharides	1037:1064	the neutral oligosaccharides at Asn39 and Asn49 residues	1037:1092	The contents of the neutral oligosaccharides at Asn39 and Asn49 residues were 32.5% and 30.0%, respectively.
7620335	5	77	gly	glycosylation	943:955	arg2	site					957:960	each glycosylation site	938:960	each glycosylation site	938:960	Structures of oligosaccharides and their contents at each glycosylation site were determined by a two-dimensional sugar mapping method.
7620335	2	78	gly	glycopeptides	486:498	arg2	glycopeptides					486:498	X. Four glycopeptides	478:498	X. Four glycopeptides each containing a glycosylation site	478:535	We determined the structure of oligosaccharides in the XAP region of human factor X. Four glycopeptides each containing a glycosylation site were isolated by digestion of XAP with endoproteinase Asp-N followed by reversed-phase HPLC.
7620335	6	79	from	Asn39	1069:1073	arg1	contents					1025:1032	The contents	1021:1032	The contents of the neutral oligosaccharides at Asn39 and Asn49 residues	1021:1092	The contents of the neutral oligosaccharides at Asn39 and Asn49 residues were 32.5% and 30.0%, respectively.
7620335	6	79	from	Asn39	1069:1073	arg1	%					1103:1103	32.5%	1099:1103	32.5%	1099:1103	The contents of the neutral oligosaccharides at Asn39 and Asn49 residues were 32.5% and 30.0%, respectively.
7620335	6	79	from	Asn39	1069:1073	arg1	oligosaccharides					1049:1064	the neutral oligosaccharides	1037:1064	the neutral oligosaccharides at Asn39 and Asn49 residues	1037:1092	The contents of the neutral oligosaccharides at Asn39 and Asn49 residues were 32.5% and 30.0%, respectively.
7620335	7	80	attach	isolated	1181:1188	arg2	oligosaccharides					1164:1179	Six neutral and twelve monosialyl oligosaccharides	1130:1179	Six neutral and twelve monosialyl oligosaccharides isolated from both N-linked glycosylation sites	1130:1227	Six neutral and twelve monosialyl oligosaccharides isolated from both N-linked glycosylation sites showed similar elution profiles composed of bi-, tri- and tetra-antennary complex type oligosaccharides.
7620335	7	80	attach	isolated	1181:1188	arg1	sites					1223:1227	both N-linked glycosylation sites	1195:1227	both N-linked glycosylation sites	1195:1227	Six neutral and twelve monosialyl oligosaccharides isolated from both N-linked glycosylation sites showed similar elution profiles composed of bi-, tri- and tetra-antennary complex type oligosaccharides.
7620335	8	81	theme	fucose	1414:1419	arg1	residue					1421:1427	a fucose residue	1412:1427	a fucose residue	1412:1427	The predominant component in neutral oligosaccharides was biantennary without a fucose residue.
7620335	2	82	contain	containing	505:514	arg2	site					532:535	a glycosylation site	516:535	a glycosylation site	516:535	We determined the structure of oligosaccharides in the XAP region of human factor X. Four glycopeptides each containing a glycosylation site were isolated by digestion of XAP with endoproteinase Asp-N followed by reversed-phase HPLC.
7620335	2	82	contain	containing	505:514	arg1	each					500:503	each	500:503	each	500:503	We determined the structure of oligosaccharides in the XAP region of human factor X. Four glycopeptides each containing a glycosylation site were isolated by digestion of XAP with endoproteinase Asp-N followed by reversed-phase HPLC.
7620335	7	83	theme	similar	1236:1242	arg1	profiles					1252:1259	similar elution profiles	1236:1259	similar elution profiles composed of bi-, tri- and tetra-antennary complex type oligosaccharides	1236:1331	Six neutral and twelve monosialyl oligosaccharides isolated from both N-linked glycosylation sites showed similar elution profiles composed of bi-, tri- and tetra-antennary complex type oligosaccharides.
7620335	8	84	from	component	1350:1358	arg1	oligosaccharides					1371:1386	neutral oligosaccharides	1363:1386	neutral oligosaccharides	1363:1386	The predominant component in neutral oligosaccharides was biantennary without a fucose residue.
7620335	2	85	theme	X.	478:479	arg1	glycopeptides					486:498	X. Four glycopeptides	478:498	X. Four glycopeptides each containing a glycosylation site	478:535	We determined the structure of oligosaccharides in the XAP region of human factor X. Four glycopeptides each containing a glycosylation site were isolated by digestion of XAP with endoproteinase Asp-N followed by reversed-phase HPLC.
7620335	6	86	from	contents	1025:1032	arg1	Asn49					1079:1083	Asn49	1079:1083	Asn49	1079:1083	The contents of the neutral oligosaccharides at Asn39 and Asn49 residues were 32.5% and 30.0%, respectively.
7620335	6	86	from	contents	1025:1032	arg1	Asn39					1069:1073	Asn39	1069:1073	Asn39	1069:1073	The contents of the neutral oligosaccharides at Asn39 and Asn49 residues were 32.5% and 30.0%, respectively.
7620335	0	87	theme	oligosaccharide	22:36	arg1	structures					38:47	the oligosaccharide structures	18:47	the oligosaccharide structures of human coagulation factor X activation peptide at each glycosylation site	18:123	Identification of the oligosaccharide structures of human coagulation factor X activation peptide at each glycosylation site.
7620335	5	88	from	site	957:960	arg1	Structures					885:894	Structures	885:894	Structures of oligosaccharides and their contents at each glycosylation site	885:960	Structures of oligosaccharides and their contents at each glycosylation site were determined by a two-dimensional sugar mapping method.
7620335	0	89	gly	glycosylation	106:118	arg2	site					120:123	each glycosylation site	101:123	each glycosylation site	101:123	Identification of the oligosaccharide structures of human coagulation factor X activation peptide at each glycosylation site.
7620335	10	90	theme	O-linked	1575:1582	arg1	oligosaccharides					1584:1599	O-linked oligosaccharides	1575:1599	O-linked oligosaccharides	1575:1599	In addition, the structures of O-linked oligosaccharides at Thr17 and Thr29 residues were suggested to be disialylated Gal beta 3GalNAc sequences by their component analyses.
7620335	3	91	theme	N-linked	630:637	arg1	oligosaccharides					639:654	N-linked oligosaccharides	630:654	N-linked oligosaccharides released from the glycopeptides by glycoamidase A digestion	630:714	N-linked oligosaccharides released from the glycopeptides by glycoamidase A digestion were derivatized with 2-aminopyridine.
7620335	10	92	from	residues	1620:1627	arg1	structures					1561:1570	the structures	1557:1570	the structures of O-linked oligosaccharides at Thr17 and Thr29 residues	1557:1627	In addition, the structures of O-linked oligosaccharides at Thr17 and Thr29 residues were suggested to be disialylated Gal beta 3GalNAc sequences by their component analyses.
7620335	10	92	from	residues	1620:1627	arg1	sequences					1680:1688	disialylated Gal beta 3GalNAc sequences	1650:1688	disialylated Gal beta 3GalNAc sequences	1650:1688	In addition, the structures of O-linked oligosaccharides at Thr17 and Thr29 residues were suggested to be disialylated Gal beta 3GalNAc sequences by their component analyses.
7620335	0	93	theme	glycosylation	106:118	arg1	site					120:123	each glycosylation site	101:123	each glycosylation site	101:123	Identification of the oligosaccharide structures of human coagulation factor X activation peptide at each glycosylation site.
7620335	0	94	theme	coagulation	58:68	arg1	peptide					90:96	human coagulation factor X activation peptide	52:96	human coagulation factor X activation peptide at each glycosylation site	52:123	Identification of the oligosaccharide structures of human coagulation factor X activation peptide at each glycosylation site.
7620335	1	95	theme	factor	304:309	arg1	XAP					333:335	XAP	333:335	XAP	333:335	Human blood coagulation factor X has two N-linked oligosaccharides at Asn39 and Asn49 residues and two O-linked oligosaccharides at Thr17 and Thr29 residues in the region of the factor X activation peptide (XAP) which is cleaved off during its activation by factor IXa.
7620335	1	95	theme	factor	304:309	arg1	peptide					324:330	the factor X activation peptide	300:330	the factor X activation peptide (XAP) which is cleaved off during its activation by factor IXa	300:393	Human blood coagulation factor X has two N-linked oligosaccharides at Asn39 and Asn49 residues and two O-linked oligosaccharides at Thr17 and Thr29 residues in the region of the factor X activation peptide (XAP) which is cleaved off during its activation by factor IXa.
7620335	2	96	theme	oligosaccharides	427:442	arg1	structure					414:422	the structure	410:422	the structure of oligosaccharides	410:442	We determined the structure of oligosaccharides in the XAP region of human factor X. Four glycopeptides each containing a glycosylation site were isolated by digestion of XAP with endoproteinase Asp-N followed by reversed-phase HPLC.
7620335	1	97	theme	activation	313:322	arg1	XAP					333:335	XAP	333:335	XAP	333:335	Human blood coagulation factor X has two N-linked oligosaccharides at Asn39 and Asn49 residues and two O-linked oligosaccharides at Thr17 and Thr29 residues in the region of the factor X activation peptide (XAP) which is cleaved off during its activation by factor IXa.
7620335	1	97	theme	activation	313:322	arg1	peptide					324:330	the factor X activation peptide	300:330	the factor X activation peptide (XAP) which is cleaved off during its activation by factor IXa	300:393	Human blood coagulation factor X has two N-linked oligosaccharides at Asn39 and Asn49 residues and two O-linked oligosaccharides at Thr17 and Thr29 residues in the region of the factor X activation peptide (XAP) which is cleaved off during its activation by factor IXa.
7620335	3	98	gly	glycopeptides	674:686	arg2	glycopeptides					674:686	the glycopeptides	670:686	the glycopeptides	670:686	N-linked oligosaccharides released from the glycopeptides by glycoamidase A digestion were derivatized with 2-aminopyridine.
7620335	1	99	theme	O-linked	229:236	arg1	oligosaccharides					238:253	two O-linked oligosaccharides	225:253	two O-linked oligosaccharides at Thr17 and Thr29 residues	225:281	Human blood coagulation factor X has two N-linked oligosaccharides at Asn39 and Asn49 residues and two O-linked oligosaccharides at Thr17 and Thr29 residues in the region of the factor X activation peptide (XAP) which is cleaved off during its activation by factor IXa.
7620335	7	100	theme	complex	1303:1309	arg1	oligosaccharides					1316:1331	tetra-antennary complex type oligosaccharides	1287:1331	tetra-antennary complex type oligosaccharides	1287:1331	Six neutral and twelve monosialyl oligosaccharides isolated from both N-linked glycosylation sites showed similar elution profiles composed of bi-, tri- and tetra-antennary complex type oligosaccharides.
7620335	3	101	theme	A	704:704	arg1	digestion					706:714	glycoamidase A digestion	691:714	glycoamidase A digestion	691:714	N-linked oligosaccharides released from the glycopeptides by glycoamidase A digestion were derivatized with 2-aminopyridine.
12458951	0	0	with	chromatography	92:105	arg1	spectrometry					124:135	tandem mass spectrometry	112:135	tandem mass spectrometry	112:135	Structural analysis of a glycoprotein by liquid chromatography-mass spectrometry and liquid chromatography with tandem mass spectrometry.
12458951	3	1	theme	N-linked	505:512	arg1	glycans					514:520	both the O- and N-linked glycans	489:520	glycans	514:520	First, we analyzed the structure of both the O- and N-linked glycans in rhTM by oligosaccharide mapping using LC-MS equipped with a graphitized carbon column (GCC-LC-MS).
12458951	8	2	theme	mass	1234:1237	arg1	spectrum					1239:1246	its mass spectrum	1230:1246	its mass spectrum	1230:1246	O-Glycosylation could be estimated on the basis of its mass spectrum.
12458951	10	3	theme	LC-MS	1458:1462	arg1	useful					1486:1491	useful	1486:1491	useful	1486:1491	We demonstrated that a sequential analysis of LC-MS and LC-MS-MS are very useful for the structural analysis of O- and N-linked glycans, polypeptides, and post-translational modifications and their heterogeneities, including site-specific glycosylation in a glycoprotein.
12458951	10	3	theme	LC-MS	1458:1462	arg1	analysis					1446:1453	a sequential analysis	1433:1453	a sequential analysis of LC-MS and LC-MS-MS	1433:1475	We demonstrated that a sequential analysis of LC-MS and LC-MS-MS are very useful for the structural analysis of O- and N-linked glycans, polypeptides, and post-translational modifications and their heterogeneities, including site-specific glycosylation in a glycoprotein.
12458951	9	4	from	beta-hydroxylation	1282:1299	arg1	Asn439					1315:1320	Asn439	1315:1320	Asn439	1315:1320	We were able to identify partial beta-hydroxylation on Asn324 and Asn439, and O-linked glucose on Ser287 from the peptide/glycopeptide map and their mass spectra.
12458951	9	4	from	beta-hydroxylation	1282:1299	arg1	Ser287					1347:1352	Ser287	1347:1352	Ser287 from the peptide/glycopeptide map	1347:1386	We were able to identify partial beta-hydroxylation on Asn324 and Asn439, and O-linked glucose on Ser287 from the peptide/glycopeptide map and their mass spectra.
12458951	9	4	from	beta-hydroxylation	1282:1299	arg1	Asn324					1304:1309	Asn324	1304:1309	Asn324	1304:1309	We were able to identify partial beta-hydroxylation on Asn324 and Asn439, and O-linked glucose on Ser287 from the peptide/glycopeptide map and their mass spectra.
12458951	9	4	from	beta-hydroxylation	1282:1299	arg1	spectra					1403:1409	their mass spectra	1392:1409	their mass spectra	1392:1409	We were able to identify partial beta-hydroxylation on Asn324 and Asn439, and O-linked glucose on Ser287 from the peptide/glycopeptide map and their mass spectra.
12458951	5	5	dep	modifications	782:794	arg1	the					759:761	the	759:761	the	759:761	Next, the post-translational modifications and their heterogeneities, including the site-specific glycosylation, were analyzed by mass spectrometric peptide/glycopeptide mapping of trypsin-digested rhTM and precursor-ion scanning.
12458951	7	6	theme	mass	1165:1168	arg1	spectra					1170:1176	their mass spectra	1159:1176	their mass spectra	1159:1176	Four N-glycosylation sites and their site-specific carbohydrate heterogeneity were determined by their mass spectra.
12458951	5	7	theme	mass	883:886	arg1	mapping					923:929	mass spectrometric peptide/glycopeptide mapping	883:929	mass spectrometric peptide/glycopeptide mapping of trypsin-digested rhTM and precursor-ion scanning	883:981	Next, the post-translational modifications and their heterogeneities, including the site-specific glycosylation, were analyzed by mass spectrometric peptide/glycopeptide mapping of trypsin-digested rhTM and precursor-ion scanning.
12458951	9	8	from	map	1384:1386	arg1	Ser287					1347:1352	Ser287	1347:1352	Ser287 from the peptide/glycopeptide map	1347:1386	We were able to identify partial beta-hydroxylation on Asn324 and Asn439, and O-linked glucose on Ser287 from the peptide/glycopeptide map and their mass spectra.
12458951	9	8	from	map	1384:1386	arg1	spectra					1403:1409	their mass spectra	1392:1409	their mass spectra	1392:1409	We were able to identify partial beta-hydroxylation on Asn324 and Asn439, and O-linked glucose on Ser287 from the peptide/glycopeptide map and their mass spectra.
12458951	2	9	theme	Chinese	246:252	arg1	cells					274:278	Chinese hamster ovary (CHO) cells	246:278	Chinese hamster ovary (CHO) cells	246:278	Using recombinant human thrombomodulin (rhTM) expressed in Chinese hamster ovary (CHO) cells, we studied the structural analysis of a glycoprotein by liquid chromatography-mass spectrometry (LC-MS) and liquid chromatography with tandem mass spectrometry (LC-MS-MS).
12458951	10	10	theme	LC-MS-MS	1468:1475	arg1	useful					1486:1491	useful	1486:1491	useful	1486:1491	We demonstrated that a sequential analysis of LC-MS and LC-MS-MS are very useful for the structural analysis of O- and N-linked glycans, polypeptides, and post-translational modifications and their heterogeneities, including site-specific glycosylation in a glycoprotein.
12458951	10	10	theme	LC-MS-MS	1468:1475	arg1	analysis					1446:1453	a sequential analysis	1433:1453	a sequential analysis of LC-MS and LC-MS-MS	1433:1475	We demonstrated that a sequential analysis of LC-MS and LC-MS-MS are very useful for the structural analysis of O- and N-linked glycans, polypeptides, and post-translational modifications and their heterogeneities, including site-specific glycosylation in a glycoprotein.
12458951	5	11	theme	site-specific	837:849	arg1	glycosylation					851:863	the site-specific glycosylation	833:863	the site-specific glycosylation	833:863	Next, the post-translational modifications and their heterogeneities, including the site-specific glycosylation, were analyzed by mass spectrometric peptide/glycopeptide mapping of trypsin-digested rhTM and precursor-ion scanning.
12458951	4	12	theme	N-linked	637:644	arg1	glycans					646:652	Major O- and N-linked glycans	624:652	glycans	646:652	Major O- and N-linked glycans were determined to be core 1 structure and fucosyl biantennary containing NeuAc(0-2) respectively.
12458951	2	13	theme	ovary	262:266	arg1	cells					274:278	Chinese hamster ovary (CHO) cells	246:278	Chinese hamster ovary (CHO) cells	246:278	Using recombinant human thrombomodulin (rhTM) expressed in Chinese hamster ovary (CHO) cells, we studied the structural analysis of a glycoprotein by liquid chromatography-mass spectrometry (LC-MS) and liquid chromatography with tandem mass spectrometry (LC-MS-MS).
12458951	7	14	theme	N-glycosylation	1067:1081	arg1	sites					1083:1087	Four N-glycosylation sites	1062:1087	Four N-glycosylation sites	1062:1087	Four N-glycosylation sites and their site-specific carbohydrate heterogeneity were determined by their mass spectra.
12458951	6	15	theme	Precursor-ion	984:996	arg1	scanning					998:1005	Precursor-ion scanning	984:1005	Precursor-ion scanning	984:1005	Precursor-ion scanning was successful in the detection of five glycopeptides.
12458951	5	16	gly	peptide/glycopeptide	902:921	arg2	peptide/glycopeptide					902:921	mass spectrometric peptide/glycopeptide mapping	883:929	mass spectrometric peptide/glycopeptide mapping of trypsin-digested rhTM and precursor-ion scanning	883:981	Next, the post-translational modifications and their heterogeneities, including the site-specific glycosylation, were analyzed by mass spectrometric peptide/glycopeptide mapping of trypsin-digested rhTM and precursor-ion scanning.
12458951	10	17	gly	glycoprotein	1670:1681	arg1	glycoprotein					1670:1681	a glycoprotein	1668:1681	a glycoprotein	1668:1681	We demonstrated that a sequential analysis of LC-MS and LC-MS-MS are very useful for the structural analysis of O- and N-linked glycans, polypeptides, and post-translational modifications and their heterogeneities, including site-specific glycosylation in a glycoprotein.
12458951	4	18	theme	fucosyl	697:703	arg1	0-2					734:736	0-2	734:736	0-2	734:736	Major O- and N-linked glycans were determined to be core 1 structure and fucosyl biantennary containing NeuAc(0-2) respectively.
12458951	4	18	theme	fucosyl	697:703	arg1	NeuAc					728:732	fucosyl biantennary containing NeuAc	697:732	fucosyl biantennary containing NeuAc(0-2)	697:737	Major O- and N-linked glycans were determined to be core 1 structure and fucosyl biantennary containing NeuAc(0-2) respectively.
12458951	7	19	theme	carbohydrate	1113:1124	arg1	heterogeneity					1126:1138	their site-specific carbohydrate heterogeneity	1093:1138	their site-specific carbohydrate heterogeneity	1093:1138	Four N-glycosylation sites and their site-specific carbohydrate heterogeneity were determined by their mass spectra.
12458951	3	20	theme	graphitized	585:595	arg1	GCC-LC-MS					612:620	GCC-LC-MS	612:620	GCC-LC-MS	612:620	First, we analyzed the structure of both the O- and N-linked glycans in rhTM by oligosaccharide mapping using LC-MS equipped with a graphitized carbon column (GCC-LC-MS).
12458951	3	20	theme	graphitized	585:595	arg1	column					604:609	a graphitized carbon column	583:609	a graphitized carbon column (GCC-LC-MS)	583:621	First, we analyzed the structure of both the O- and N-linked glycans in rhTM by oligosaccharide mapping using LC-MS equipped with a graphitized carbon column (GCC-LC-MS).
12458951	5	21	theme	rhTM	951:954	arg1	mapping					923:929	mass spectrometric peptide/glycopeptide mapping	883:929	mass spectrometric peptide/glycopeptide mapping of trypsin-digested rhTM and precursor-ion scanning	883:981	Next, the post-translational modifications and their heterogeneities, including the site-specific glycosylation, were analyzed by mass spectrometric peptide/glycopeptide mapping of trypsin-digested rhTM and precursor-ion scanning.
12458951	4	22	link	N-linked	637:644	arg1	glycans					646:652	Major O- and N-linked glycans	624:652	glycans	646:652	Major O- and N-linked glycans were determined to be core 1 structure and fucosyl biantennary containing NeuAc(0-2) respectively.
12458951	9	23	gly	peptide/glycopeptide	1363:1382	arg2	peptide/glycopeptide					1363:1382	the peptide/glycopeptide map	1359:1386	the peptide/glycopeptide map	1359:1386	We were able to identify partial beta-hydroxylation on Asn324 and Asn439, and O-linked glucose on Ser287 from the peptide/glycopeptide map and their mass spectra.
12458951	3	24	theme	oligosaccharide	533:547	arg1	mapping					549:555	oligosaccharide mapping	533:555	oligosaccharide mapping using LC-MS equipped with a graphitized carbon column (GCC-LC-MS)	533:621	First, we analyzed the structure of both the O- and N-linked glycans in rhTM by oligosaccharide mapping using LC-MS equipped with a graphitized carbon column (GCC-LC-MS).
12458951	5	25	theme	precursor-ion	960:972	arg1	scanning					974:981	precursor-ion scanning	960:981	precursor-ion scanning	960:981	Next, the post-translational modifications and their heterogeneities, including the site-specific glycosylation, were analyzed by mass spectrometric peptide/glycopeptide mapping of trypsin-digested rhTM and precursor-ion scanning.
12458951	4	26	theme	containing	717:726	arg1	0-2					734:736	0-2	734:736	0-2	734:736	Major O- and N-linked glycans were determined to be core 1 structure and fucosyl biantennary containing NeuAc(0-2) respectively.
12458951	4	26	theme	containing	717:726	arg1	NeuAc					728:732	fucosyl biantennary containing NeuAc	697:732	fucosyl biantennary containing NeuAc(0-2)	697:737	Major O- and N-linked glycans were determined to be core 1 structure and fucosyl biantennary containing NeuAc(0-2) respectively.
12458951	4	27	theme	core	676:679	arg1	structure					683:691	core 1 structure	676:691	core 1 structure	676:691	Major O- and N-linked glycans were determined to be core 1 structure and fucosyl biantennary containing NeuAc(0-2) respectively.
12458951	2	28	theme	CHO	269:271	arg1	cells					274:278	Chinese hamster ovary (CHO) cells	246:278	Chinese hamster ovary (CHO) cells	246:278	Using recombinant human thrombomodulin (rhTM) expressed in Chinese hamster ovary (CHO) cells, we studied the structural analysis of a glycoprotein by liquid chromatography-mass spectrometry (LC-MS) and liquid chromatography with tandem mass spectrometry (LC-MS-MS).
12458951	5	29	theme	peptide/glycopeptide	902:921	arg1	mapping					923:929	mass spectrometric peptide/glycopeptide mapping	883:929	mass spectrometric peptide/glycopeptide mapping of trypsin-digested rhTM and precursor-ion scanning	883:981	Next, the post-translational modifications and their heterogeneities, including the site-specific glycosylation, were analyzed by mass spectrometric peptide/glycopeptide mapping of trypsin-digested rhTM and precursor-ion scanning.
12458951	0	30	theme	liquid	85:90	arg1	chromatography					92:105	liquid chromatography	85:105	liquid chromatography	85:105	Structural analysis of a glycoprotein by liquid chromatography-mass spectrometry and liquid chromatography with tandem mass spectrometry.
12458951	10	31	theme	structural	1501:1510	arg1	analysis					1512:1519	the structural analysis	1497:1519	the structural analysis of O- and N-linked glycans, polypeptides, and post-translational modifications	1497:1598	We demonstrated that a sequential analysis of LC-MS and LC-MS-MS are very useful for the structural analysis of O- and N-linked glycans, polypeptides, and post-translational modifications and their heterogeneities, including site-specific glycosylation in a glycoprotein.
12458951	10	32	link	N-linked	1531:1538	arg1	glycans					1540:1546	O- and N-linked glycans	1524:1546	glycans	1540:1546	We demonstrated that a sequential analysis of LC-MS and LC-MS-MS are very useful for the structural analysis of O- and N-linked glycans, polypeptides, and post-translational modifications and their heterogeneities, including site-specific glycosylation in a glycoprotein.
12458951	1	33	theme	recombinant	153:163	arg1	thrombomodulin					171:184	recombinant human thrombomodulin	153:184	recombinant human thrombomodulin	153:184	Application to recombinant human thrombomodulin.
12458951	10	34	theme	glycans	1540:1546	arg1	analysis					1512:1519	the structural analysis	1497:1519	the structural analysis of O- and N-linked glycans, polypeptides, and post-translational modifications	1497:1598	We demonstrated that a sequential analysis of LC-MS and LC-MS-MS are very useful for the structural analysis of O- and N-linked glycans, polypeptides, and post-translational modifications and their heterogeneities, including site-specific glycosylation in a glycoprotein.
12458951	10	34	theme	glycans	1540:1546	arg1	heterogeneities					1610:1624	their heterogeneities	1604:1624	their heterogeneities	1604:1624	We demonstrated that a sequential analysis of LC-MS and LC-MS-MS are very useful for the structural analysis of O- and N-linked glycans, polypeptides, and post-translational modifications and their heterogeneities, including site-specific glycosylation in a glycoprotein.
12458951	10	34	theme	glycans	1540:1546	arg1	glycosylation					1651:1663	site-specific glycosylation	1637:1663	site-specific glycosylation in a glycoprotein	1637:1681	We demonstrated that a sequential analysis of LC-MS and LC-MS-MS are very useful for the structural analysis of O- and N-linked glycans, polypeptides, and post-translational modifications and their heterogeneities, including site-specific glycosylation in a glycoprotein.
12458951	2	35	theme	tandem	416:421	arg1	spectrometry					428:439	tandem mass spectrometry	416:439	tandem mass spectrometry (LC-MS-MS)	416:450	Using recombinant human thrombomodulin (rhTM) expressed in Chinese hamster ovary (CHO) cells, we studied the structural analysis of a glycoprotein by liquid chromatography-mass spectrometry (LC-MS) and liquid chromatography with tandem mass spectrometry (LC-MS-MS).
12458951	2	35	theme	tandem	416:421	arg1	LC-MS-MS					442:449	LC-MS-MS	442:449	LC-MS-MS	442:449	Using recombinant human thrombomodulin (rhTM) expressed in Chinese hamster ovary (CHO) cells, we studied the structural analysis of a glycoprotein by liquid chromatography-mass spectrometry (LC-MS) and liquid chromatography with tandem mass spectrometry (LC-MS-MS).
12458951	0	36	theme	mass	119:122	arg1	spectrometry					124:135	tandem mass spectrometry	112:135	tandem mass spectrometry	112:135	Structural analysis of a glycoprotein by liquid chromatography-mass spectrometry and liquid chromatography with tandem mass spectrometry.
12458951	0	37	theme	Structural	0:9	arg1	analysis					11:18	Structural analysis	0:18	Structural analysis of a glycoprotein by liquid chromatography-mass spectrometry and liquid chromatography with tandem mass spectrometry.	0:136	Structural analysis of a glycoprotein by liquid chromatography-mass spectrometry and liquid chromatography with tandem mass spectrometry.
12458951	6	38	from	successful	1011:1020	arg1	detection					1029:1037	the detection	1025:1037	the detection of five glycopeptides	1025:1059	Precursor-ion scanning was successful in the detection of five glycopeptides.
12458951	1	39	theme	human	165:169	arg1	thrombomodulin					171:184	recombinant human thrombomodulin	153:184	recombinant human thrombomodulin	153:184	Application to recombinant human thrombomodulin.
12458951	11	40	from	glycoprotein	1715:1726	arg1	samples					1742:1748	biological samples	1731:1748	biological samples	1731:1748	Our method can be applied to a glycoprotein in biological samples.
12458951	10	41	theme	polypeptides	1549:1560	arg1	analysis					1512:1519	the structural analysis	1497:1519	the structural analysis of O- and N-linked glycans, polypeptides, and post-translational modifications	1497:1598	We demonstrated that a sequential analysis of LC-MS and LC-MS-MS are very useful for the structural analysis of O- and N-linked glycans, polypeptides, and post-translational modifications and their heterogeneities, including site-specific glycosylation in a glycoprotein.
12458951	10	41	theme	polypeptides	1549:1560	arg1	heterogeneities					1610:1624	their heterogeneities	1604:1624	their heterogeneities	1604:1624	We demonstrated that a sequential analysis of LC-MS and LC-MS-MS are very useful for the structural analysis of O- and N-linked glycans, polypeptides, and post-translational modifications and their heterogeneities, including site-specific glycosylation in a glycoprotein.
12458951	10	41	theme	polypeptides	1549:1560	arg1	glycosylation					1651:1663	site-specific glycosylation	1637:1663	site-specific glycosylation in a glycoprotein	1637:1681	We demonstrated that a sequential analysis of LC-MS and LC-MS-MS are very useful for the structural analysis of O- and N-linked glycans, polypeptides, and post-translational modifications and their heterogeneities, including site-specific glycosylation in a glycoprotein.
12458951	0	42	theme	glycoprotein	25:36	arg1	analysis					11:18	Structural analysis	0:18	Structural analysis of a glycoprotein by liquid chromatography-mass spectrometry and liquid chromatography with tandem mass spectrometry.	0:136	Structural analysis of a glycoprotein by liquid chromatography-mass spectrometry and liquid chromatography with tandem mass spectrometry.
12458951	5	43	theme	post-translational	763:780	arg1	modifications					782:794	post-translational modifications	763:794	post-translational modifications	763:794	Next, the post-translational modifications and their heterogeneities, including the site-specific glycosylation, were analyzed by mass spectrometric peptide/glycopeptide mapping of trypsin-digested rhTM and precursor-ion scanning.
12458951	5	43	theme	post-translational	763:780	arg1	glycosylation					851:863	the site-specific glycosylation	833:863	the site-specific glycosylation	833:863	Next, the post-translational modifications and their heterogeneities, including the site-specific glycosylation, were analyzed by mass spectrometric peptide/glycopeptide mapping of trypsin-digested rhTM and precursor-ion scanning.
12458951	7	44	gly	N-glycosylation	1067:1081	arg2	sites					1083:1087	Four N-glycosylation sites	1062:1087	Four N-glycosylation sites	1062:1087	Four N-glycosylation sites and their site-specific carbohydrate heterogeneity were determined by their mass spectra.
12458951	7	44	gly	N-glycosylation	1067:1081	arg2	Four					1062:1065	Four	1062:1065	Four	1062:1065	Four N-glycosylation sites and their site-specific carbohydrate heterogeneity were determined by their mass spectra.
12458951	2	45	theme	recombinant	193:203	arg1	thrombomodulin					211:224	recombinant human thrombomodulin	193:224	recombinant human thrombomodulin (rhTM) expressed in Chinese hamster ovary (CHO) cells	193:278	Using recombinant human thrombomodulin (rhTM) expressed in Chinese hamster ovary (CHO) cells, we studied the structural analysis of a glycoprotein by liquid chromatography-mass spectrometry (LC-MS) and liquid chromatography with tandem mass spectrometry (LC-MS-MS).
12458951	2	45	theme	recombinant	193:203	arg1	rhTM					227:230	rhTM	227:230	rhTM	227:230	Using recombinant human thrombomodulin (rhTM) expressed in Chinese hamster ovary (CHO) cells, we studied the structural analysis of a glycoprotein by liquid chromatography-mass spectrometry (LC-MS) and liquid chromatography with tandem mass spectrometry (LC-MS-MS).
12458951	6	46	gly	glycopeptides	1047:1059	arg2	glycopeptides					1047:1059	five glycopeptides	1042:1059	five glycopeptides	1042:1059	Precursor-ion scanning was successful in the detection of five glycopeptides.
12458951	0	47	theme	liquid	41:46	arg1	spectrometry					68:79	liquid chromatography-mass spectrometry	41:79	liquid chromatography-mass spectrometry	41:79	Structural analysis of a glycoprotein by liquid chromatography-mass spectrometry and liquid chromatography with tandem mass spectrometry.
12458951	10	48	theme	modifications	1586:1598	arg1	analysis					1512:1519	the structural analysis	1497:1519	the structural analysis of O- and N-linked glycans, polypeptides, and post-translational modifications	1497:1598	We demonstrated that a sequential analysis of LC-MS and LC-MS-MS are very useful for the structural analysis of O- and N-linked glycans, polypeptides, and post-translational modifications and their heterogeneities, including site-specific glycosylation in a glycoprotein.
12458951	10	48	theme	modifications	1586:1598	arg1	heterogeneities					1610:1624	their heterogeneities	1604:1624	their heterogeneities	1604:1624	We demonstrated that a sequential analysis of LC-MS and LC-MS-MS are very useful for the structural analysis of O- and N-linked glycans, polypeptides, and post-translational modifications and their heterogeneities, including site-specific glycosylation in a glycoprotein.
12458951	10	48	theme	modifications	1586:1598	arg1	glycosylation					1651:1663	site-specific glycosylation	1637:1663	site-specific glycosylation in a glycoprotein	1637:1681	We demonstrated that a sequential analysis of LC-MS and LC-MS-MS are very useful for the structural analysis of O- and N-linked glycans, polypeptides, and post-translational modifications and their heterogeneities, including site-specific glycosylation in a glycoprotein.
12458951	3	49	from	structure	476:484	arg1	rhTM					525:528	rhTM	525:528	rhTM	525:528	First, we analyzed the structure of both the O- and N-linked glycans in rhTM by oligosaccharide mapping using LC-MS equipped with a graphitized carbon column (GCC-LC-MS).
12458951	2	50	theme	liquid	337:342	arg1	LC-MS					378:382	LC-MS	378:382	LC-MS	378:382	Using recombinant human thrombomodulin (rhTM) expressed in Chinese hamster ovary (CHO) cells, we studied the structural analysis of a glycoprotein by liquid chromatography-mass spectrometry (LC-MS) and liquid chromatography with tandem mass spectrometry (LC-MS-MS).
12458951	2	50	theme	liquid	337:342	arg1	spectrometry					364:375	liquid chromatography-mass spectrometry	337:375	liquid chromatography-mass spectrometry (LC-MS)	337:383	Using recombinant human thrombomodulin (rhTM) expressed in Chinese hamster ovary (CHO) cells, we studied the structural analysis of a glycoprotein by liquid chromatography-mass spectrometry (LC-MS) and liquid chromatography with tandem mass spectrometry (LC-MS-MS).
12458951	10	51	theme	site-specific	1637:1649	arg1	glycosylation					1651:1663	site-specific glycosylation	1637:1663	site-specific glycosylation in a glycoprotein	1637:1681	We demonstrated that a sequential analysis of LC-MS and LC-MS-MS are very useful for the structural analysis of O- and N-linked glycans, polypeptides, and post-translational modifications and their heterogeneities, including site-specific glycosylation in a glycoprotein.
12458951	10	52	theme	sequential	1435:1444	arg1	useful					1486:1491	useful	1486:1491	useful	1486:1491	We demonstrated that a sequential analysis of LC-MS and LC-MS-MS are very useful for the structural analysis of O- and N-linked glycans, polypeptides, and post-translational modifications and their heterogeneities, including site-specific glycosylation in a glycoprotein.
12458951	10	52	theme	sequential	1435:1444	arg1	analysis					1446:1453	a sequential analysis	1433:1453	a sequential analysis of LC-MS and LC-MS-MS	1433:1475	We demonstrated that a sequential analysis of LC-MS and LC-MS-MS are very useful for the structural analysis of O- and N-linked glycans, polypeptides, and post-translational modifications and their heterogeneities, including site-specific glycosylation in a glycoprotein.
12458951	3	53	theme	glycans	514:520	arg1	structure					476:484	the structure	472:484	the structure of both the O- and N-linked glycans in rhTM	472:528	First, we analyzed the structure of both the O- and N-linked glycans in rhTM by oligosaccharide mapping using LC-MS equipped with a graphitized carbon column (GCC-LC-MS).
12458951	2	54	theme	structural	296:305	arg1	analysis					307:314	the structural analysis	292:314	the structural analysis of a glycoprotein	292:332	Using recombinant human thrombomodulin (rhTM) expressed in Chinese hamster ovary (CHO) cells, we studied the structural analysis of a glycoprotein by liquid chromatography-mass spectrometry (LC-MS) and liquid chromatography with tandem mass spectrometry (LC-MS-MS).
12458951	0	55	with	spectrometry	68:79	arg1	spectrometry					124:135	tandem mass spectrometry	112:135	tandem mass spectrometry	112:135	Structural analysis of a glycoprotein by liquid chromatography-mass spectrometry and liquid chromatography with tandem mass spectrometry.
12458951	8	56	theme	spectrum	1239:1246	arg1	basis					1221:1225	the basis	1217:1225	the basis of its mass spectrum	1217:1246	O-Glycosylation could be estimated on the basis of its mass spectrum.
12458951	9	57	theme	partial	1274:1280	arg1	beta-hydroxylation					1282:1299	partial beta-hydroxylation	1274:1299	partial beta-hydroxylation on Asn324 and Asn439	1274:1320	We were able to identify partial beta-hydroxylation on Asn324 and Asn439, and O-linked glucose on Ser287 from the peptide/glycopeptide map and their mass spectra.
12458951	2	58	theme	glycoprotein	321:332	arg1	analysis					307:314	the structural analysis	292:314	the structural analysis of a glycoprotein	292:332	Using recombinant human thrombomodulin (rhTM) expressed in Chinese hamster ovary (CHO) cells, we studied the structural analysis of a glycoprotein by liquid chromatography-mass spectrometry (LC-MS) and liquid chromatography with tandem mass spectrometry (LC-MS-MS).
12458951	3	59	link	N-linked	505:512	arg1	glycans					514:520	both the O- and N-linked glycans	489:520	glycans	514:520	First, we analyzed the structure of both the O- and N-linked glycans in rhTM by oligosaccharide mapping using LC-MS equipped with a graphitized carbon column (GCC-LC-MS).
12458951	4	60	theme	Major	624:628	arg1	O-					630:631	Major O- and N-linked glycans	624:652	O-	630:631	Major O- and N-linked glycans were determined to be core 1 structure and fucosyl biantennary containing NeuAc(0-2) respectively.
12458951	2	61	theme	chromatography-mass	344:362	arg1	LC-MS					378:382	LC-MS	378:382	LC-MS	378:382	Using recombinant human thrombomodulin (rhTM) expressed in Chinese hamster ovary (CHO) cells, we studied the structural analysis of a glycoprotein by liquid chromatography-mass spectrometry (LC-MS) and liquid chromatography with tandem mass spectrometry (LC-MS-MS).
12458951	2	61	theme	chromatography-mass	344:362	arg1	spectrometry					364:375	liquid chromatography-mass spectrometry	337:375	liquid chromatography-mass spectrometry (LC-MS)	337:383	Using recombinant human thrombomodulin (rhTM) expressed in Chinese hamster ovary (CHO) cells, we studied the structural analysis of a glycoprotein by liquid chromatography-mass spectrometry (LC-MS) and liquid chromatography with tandem mass spectrometry (LC-MS-MS).
12458951	3	62	theme	carbon	597:602	arg1	GCC-LC-MS					612:620	GCC-LC-MS	612:620	GCC-LC-MS	612:620	First, we analyzed the structure of both the O- and N-linked glycans in rhTM by oligosaccharide mapping using LC-MS equipped with a graphitized carbon column (GCC-LC-MS).
12458951	3	62	theme	carbon	597:602	arg1	column					604:609	a graphitized carbon column	583:609	a graphitized carbon column (GCC-LC-MS)	583:621	First, we analyzed the structure of both the O- and N-linked glycans in rhTM by oligosaccharide mapping using LC-MS equipped with a graphitized carbon column (GCC-LC-MS).
12458951	11	63	gly	glycoprotein	1715:1726	arg1	glycoprotein					1715:1726	a glycoprotein	1713:1726	a glycoprotein in biological samples	1713:1748	Our method can be applied to a glycoprotein in biological samples.
12458951	7	64	theme	site-specific	1099:1111	arg1	heterogeneity					1126:1138	their site-specific carbohydrate heterogeneity	1093:1138	their site-specific carbohydrate heterogeneity	1093:1138	Four N-glycosylation sites and their site-specific carbohydrate heterogeneity were determined by their mass spectra.
12458951	2	65	theme	hamster	254:260	arg1	cells					274:278	Chinese hamster ovary (CHO) cells	246:278	Chinese hamster ovary (CHO) cells	246:278	Using recombinant human thrombomodulin (rhTM) expressed in Chinese hamster ovary (CHO) cells, we studied the structural analysis of a glycoprotein by liquid chromatography-mass spectrometry (LC-MS) and liquid chromatography with tandem mass spectrometry (LC-MS-MS).
12458951	5	66	theme	trypsin-digested	934:949	arg1	rhTM					951:954	trypsin-digested rhTM	934:954	trypsin-digested rhTM	934:954	Next, the post-translational modifications and their heterogeneities, including the site-specific glycosylation, were analyzed by mass spectrometric peptide/glycopeptide mapping of trypsin-digested rhTM and precursor-ion scanning.
12458951	10	67	gly	glycosylation	1651:1663	arg1	glycoprotein					1670:1681	a glycoprotein	1668:1681	a glycoprotein	1668:1681	We demonstrated that a sequential analysis of LC-MS and LC-MS-MS are very useful for the structural analysis of O- and N-linked glycans, polypeptides, and post-translational modifications and their heterogeneities, including site-specific glycosylation in a glycoprotein.
12458951	9	68	theme	O-linked	1327:1334	arg1	glucose					1336:1342	O-linked glucose	1327:1342	O-linked glucose on Ser287 from the peptide/glycopeptide map and their mass spectra	1327:1409	We were able to identify partial beta-hydroxylation on Asn324 and Asn439, and O-linked glucose on Ser287 from the peptide/glycopeptide map and their mass spectra.
12458951	4	69	theme	biantennary	705:715	arg1	0-2					734:736	0-2	734:736	0-2	734:736	Major O- and N-linked glycans were determined to be core 1 structure and fucosyl biantennary containing NeuAc(0-2) respectively.
12458951	4	69	theme	biantennary	705:715	arg1	NeuAc					728:732	fucosyl biantennary containing NeuAc	697:732	fucosyl biantennary containing NeuAc(0-2)	697:737	Major O- and N-linked glycans were determined to be core 1 structure and fucosyl biantennary containing NeuAc(0-2) respectively.
12458951	5	70	theme	spectrometric	888:900	arg1	mapping					923:929	mass spectrometric peptide/glycopeptide mapping	883:929	mass spectrometric peptide/glycopeptide mapping of trypsin-digested rhTM and precursor-ion scanning	883:981	Next, the post-translational modifications and their heterogeneities, including the site-specific glycosylation, were analyzed by mass spectrometric peptide/glycopeptide mapping of trypsin-digested rhTM and precursor-ion scanning.
12458951	9	71	link	O-linked	1327:1334	arg1	glucose					1336:1342	O-linked glucose	1327:1342	O-linked glucose on Ser287 from the peptide/glycopeptide map and their mass spectra	1327:1409	We were able to identify partial beta-hydroxylation on Asn324 and Asn439, and O-linked glucose on Ser287 from the peptide/glycopeptide map and their mass spectra.
12458951	6	72	theme	glycopeptides	1047:1059	arg1	detection					1029:1037	the detection	1025:1037	the detection of five glycopeptides	1025:1059	Precursor-ion scanning was successful in the detection of five glycopeptides.
12458951	0	73	theme	tandem	112:117	arg1	spectrometry					124:135	tandem mass spectrometry	112:135	tandem mass spectrometry	112:135	Structural analysis of a glycoprotein by liquid chromatography-mass spectrometry and liquid chromatography with tandem mass spectrometry.
12458951	9	74	theme	peptide/glycopeptide	1363:1382	arg1	map					1384:1386	the peptide/glycopeptide map	1359:1386	the peptide/glycopeptide map	1359:1386	We were able to identify partial beta-hydroxylation on Asn324 and Asn439, and O-linked glucose on Ser287 from the peptide/glycopeptide map and their mass spectra.
12458951	6	75	from	detection	1029:1037	arg1	successful					1011:1020	successful	1011:1020	successful	1011:1020	Precursor-ion scanning was successful in the detection of five glycopeptides.
12458951	1	76	dep	Application	138:148	arg1	thrombomodulin					171:184	recombinant human thrombomodulin	153:184	recombinant human thrombomodulin	153:184	Application to recombinant human thrombomodulin.
12458951	9	77	theme	mass	1398:1401	arg1	spectra					1403:1409	their mass spectra	1392:1409	their mass spectra	1392:1409	We were able to identify partial beta-hydroxylation on Asn324 and Asn439, and O-linked glucose on Ser287 from the peptide/glycopeptide map and their mass spectra.
12458951	5	78	theme	scanning	974:981	arg1	mapping					923:929	mass spectrometric peptide/glycopeptide mapping	883:929	mass spectrometric peptide/glycopeptide mapping of trypsin-digested rhTM and precursor-ion scanning	883:981	Next, the post-translational modifications and their heterogeneities, including the site-specific glycosylation, were analyzed by mass spectrometric peptide/glycopeptide mapping of trypsin-digested rhTM and precursor-ion scanning.
12458951	10	79	theme	O-	1524:1525	arg1	glycans					1540:1546	O- and N-linked glycans	1524:1546	glycans	1540:1546	We demonstrated that a sequential analysis of LC-MS and LC-MS-MS are very useful for the structural analysis of O- and N-linked glycans, polypeptides, and post-translational modifications and their heterogeneities, including site-specific glycosylation in a glycoprotein.
12458951	8	80	gly	O-Glycosylation	1179:1193	arg1	basis					1221:1225	the basis	1217:1225	the basis of its mass spectrum	1217:1246	O-Glycosylation could be estimated on the basis of its mass spectrum.
12458951	2	81	theme	liquid	389:394	arg1	chromatography					396:409	liquid chromatography	389:409	liquid chromatography	389:409	Using recombinant human thrombomodulin (rhTM) expressed in Chinese hamster ovary (CHO) cells, we studied the structural analysis of a glycoprotein by liquid chromatography-mass spectrometry (LC-MS) and liquid chromatography with tandem mass spectrometry (LC-MS-MS).
12458951	2	82	theme	human	205:209	arg1	thrombomodulin					211:224	recombinant human thrombomodulin	193:224	recombinant human thrombomodulin (rhTM) expressed in Chinese hamster ovary (CHO) cells	193:278	Using recombinant human thrombomodulin (rhTM) expressed in Chinese hamster ovary (CHO) cells, we studied the structural analysis of a glycoprotein by liquid chromatography-mass spectrometry (LC-MS) and liquid chromatography with tandem mass spectrometry (LC-MS-MS).
12458951	2	82	theme	human	205:209	arg1	rhTM					227:230	rhTM	227:230	rhTM	227:230	Using recombinant human thrombomodulin (rhTM) expressed in Chinese hamster ovary (CHO) cells, we studied the structural analysis of a glycoprotein by liquid chromatography-mass spectrometry (LC-MS) and liquid chromatography with tandem mass spectrometry (LC-MS-MS).
12458951	2	83	theme	mass	423:426	arg1	spectrometry					428:439	tandem mass spectrometry	416:439	tandem mass spectrometry (LC-MS-MS)	416:450	Using recombinant human thrombomodulin (rhTM) expressed in Chinese hamster ovary (CHO) cells, we studied the structural analysis of a glycoprotein by liquid chromatography-mass spectrometry (LC-MS) and liquid chromatography with tandem mass spectrometry (LC-MS-MS).
12458951	2	83	theme	mass	423:426	arg1	LC-MS-MS					442:449	LC-MS-MS	442:449	LC-MS-MS	442:449	Using recombinant human thrombomodulin (rhTM) expressed in Chinese hamster ovary (CHO) cells, we studied the structural analysis of a glycoprotein by liquid chromatography-mass spectrometry (LC-MS) and liquid chromatography with tandem mass spectrometry (LC-MS-MS).
12458951	0	84	theme	chromatography-mass	48:66	arg1	spectrometry					68:79	liquid chromatography-mass spectrometry	41:79	liquid chromatography-mass spectrometry	41:79	Structural analysis of a glycoprotein by liquid chromatography-mass spectrometry and liquid chromatography with tandem mass spectrometry.
12458951	10	85	theme	N-linked	1531:1538	arg1	glycans					1540:1546	O- and N-linked glycans	1524:1546	glycans	1540:1546	We demonstrated that a sequential analysis of LC-MS and LC-MS-MS are very useful for the structural analysis of O- and N-linked glycans, polypeptides, and post-translational modifications and their heterogeneities, including site-specific glycosylation in a glycoprotein.
12458951	3	86	theme	O-	498:499	arg1	structure					476:484	the structure	472:484	the structure of both the O- and N-linked glycans in rhTM	472:528	First, we analyzed the structure of both the O- and N-linked glycans in rhTM by oligosaccharide mapping using LC-MS equipped with a graphitized carbon column (GCC-LC-MS).
12458951	10	87	from	glycosylation	1651:1663	arg1	glycoprotein					1670:1681	a glycoprotein	1668:1681	a glycoprotein	1668:1681	We demonstrated that a sequential analysis of LC-MS and LC-MS-MS are very useful for the structural analysis of O- and N-linked glycans, polypeptides, and post-translational modifications and their heterogeneities, including site-specific glycosylation in a glycoprotein.
12458951	0	88	gly	glycoprotein	25:36	arg1	glycoprotein					25:36	a glycoprotein	23:36	a glycoprotein	23:36	Structural analysis of a glycoprotein by liquid chromatography-mass spectrometry and liquid chromatography with tandem mass spectrometry.
12458951	10	89	theme	post-translational	1567:1584	arg1	modifications					1586:1598	post-translational modifications	1567:1598	post-translational modifications	1567:1598	We demonstrated that a sequential analysis of LC-MS and LC-MS-MS are very useful for the structural analysis of O- and N-linked glycans, polypeptides, and post-translational modifications and their heterogeneities, including site-specific glycosylation in a glycoprotein.
12458951	9	90	from	glucose	1336:1342	arg1	Asn439					1315:1320	Asn439	1315:1320	Asn439	1315:1320	We were able to identify partial beta-hydroxylation on Asn324 and Asn439, and O-linked glucose on Ser287 from the peptide/glycopeptide map and their mass spectra.
12458951	9	90	from	glucose	1336:1342	arg1	Ser287					1347:1352	Ser287	1347:1352	Ser287 from the peptide/glycopeptide map	1347:1386	We were able to identify partial beta-hydroxylation on Asn324 and Asn439, and O-linked glucose on Ser287 from the peptide/glycopeptide map and their mass spectra.
12458951	9	90	from	glucose	1336:1342	arg1	Asn324					1304:1309	Asn324	1304:1309	Asn324	1304:1309	We were able to identify partial beta-hydroxylation on Asn324 and Asn439, and O-linked glucose on Ser287 from the peptide/glycopeptide map and their mass spectra.
12458951	9	90	from	glucose	1336:1342	arg1	spectra					1403:1409	their mass spectra	1392:1409	their mass spectra	1392:1409	We were able to identify partial beta-hydroxylation on Asn324 and Asn439, and O-linked glucose on Ser287 from the peptide/glycopeptide map and their mass spectra.
12458951	2	91	gly	glycoprotein	321:332	arg1	glycoprotein					321:332	a glycoprotein	319:332	a glycoprotein	319:332	Using recombinant human thrombomodulin (rhTM) expressed in Chinese hamster ovary (CHO) cells, we studied the structural analysis of a glycoprotein by liquid chromatography-mass spectrometry (LC-MS) and liquid chromatography with tandem mass spectrometry (LC-MS-MS).
12458951	11	92	theme	biological	1731:1740	arg1	samples					1742:1748	biological samples	1731:1748	biological samples	1731:1748	Our method can be applied to a glycoprotein in biological samples.
19864504	4	0	from	importance	521:530	arg1	ERT					575:577	ERT	575:577	ERT	575:577	Because of the importance of N-linked oligosaccharide side chains in ERT, we examined the composition of the three N-linked glycans of four different recombinant ASAs in a site-specific manner.
19864504	2	1	theme	other	332:336	arg1	disorders					348:356	other lysosomal disorders	332:356	other lysosomal disorders	332:356	Enzyme replacement therapy (ERT) is a therapeutic option for MLD and other lysosomal disorders.
19864504	12	2	theme	oligosaccharide	1635:1649	arg1	structures					1651:1660	the oligosaccharide structures	1631:1660	the oligosaccharide structures	1631:1660	Our data show that the oligosaccharide structures were very different in these trials making it difficult to draw common conclusions from the various investigations.
19864504	12	2	theme	oligosaccharide	1635:1649	arg1	different					1672:1680	different	1672:1680	different	1672:1680	Our data show that the oligosaccharide structures were very different in these trials making it difficult to draw common conclusions from the various investigations.
19864504	10	3	theme	glycosylation	1478:1490	arg1	sites					1492:1496	the three glycosylation sites	1468:1496	the three glycosylation sites	1468:1496	Notably, roughly one-third of the N-glycans released from the three glycosylation sites were fucosylated.
19864504	0	4	link	N-linked	26:33	arg1	oligosaccharides					35:50	N-linked oligosaccharides	26:50	N-linked oligosaccharides of recombinant lysosomal arylsulfatase A	26:91	Site-specific analysis of N-linked oligosaccharides of recombinant lysosomal arylsulfatase A produced in different cell lines.
19864504	1	5	theme	lysosomal	167:175	arg1	disease					185:191	a lysosomal storage disease	165:191	a lysosomal storage disease caused by a deficiency of the lysosomal enzyme arylsulfatase A (ASA)	165:260	Metachromatic leukodystrophy (MLD) is a lysosomal storage disease caused by a deficiency of the lysosomal enzyme arylsulfatase A (ASA).
19864504	1	5	theme	lysosomal	167:175	arg1	leukodystrophy					141:154	Metachromatic leukodystrophy	127:154	Metachromatic leukodystrophy (MLD)	127:160	Metachromatic leukodystrophy (MLD) is a lysosomal storage disease caused by a deficiency of the lysosomal enzyme arylsulfatase A (ASA).
19864504	11	6	theme	numerous	1535:1542	arg1	enzymes					1566:1572	numerous recombinant lysosomal enzymes	1535:1572	numerous recombinant lysosomal enzymes	1535:1572	In the last years, numerous recombinant lysosomal enzymes were used for preclinical ERT trials.
19864504	5	7	gly	glycosylation	864:876	arg2	sites					878:882	all glycosylation sites	860:882	all glycosylation sites	860:882	Depending on the culture conditions and the cell line expressing the enzyme, we detected a high variability of the high-mannose-type N-glycans which prevail at all glycosylation sites.
19864504	0	8	theme	cell	115:118	arg1	lines					120:124	different cell lines	105:124	different cell lines	105:124	Site-specific analysis of N-linked oligosaccharides of recombinant lysosomal arylsulfatase A produced in different cell lines.
19864504	11	9	theme	preclinical	1588:1598	arg1	trials					1604:1609	preclinical ERT trials	1588:1609	preclinical ERT trials	1588:1609	In the last years, numerous recombinant lysosomal enzymes were used for preclinical ERT trials.
19864504	4	10	theme	ASAs	668:671	arg1	composition					596:606	the composition	592:606	the composition of the three N-linked glycans of four different recombinant ASAs	592:671	Because of the importance of N-linked oligosaccharide side chains in ERT, we examined the composition of the three N-linked glycans of four different recombinant ASAs in a site-specific manner.
19864504	0	11	theme	different	105:113	arg1	lines					120:124	different cell lines	105:124	different cell lines	105:124	Site-specific analysis of N-linked oligosaccharides of recombinant lysosomal arylsulfatase A produced in different cell lines.
19864504	9	12	theme	highest	1320:1326	arg1	content					1348:1354	the highest mannose-6-phosphate content	1316:1354	the highest mannose-6-phosphate content	1316:1354	CHO cells cultured under bioreactor conditions yielded recombinant ASA with the most preserved N-glycan structures, the highest mannose-6-phosphate content and the highest similarity to non-recombinant enzyme.
19864504	3	13	theme	patient	491:497	arg1	cells					499:503	patient cells	491:503	patient cells	491:503	This therapy depends on N-linked oligosaccharide-mediated delivery of intravenously injected recombinant enzyme to the lysosomes of patient cells.
19864504	5	14	theme	cell	744:747	arg1	line					749:752	the cell line	740:752	the cell line expressing the enzyme	740:774	Depending on the culture conditions and the cell line expressing the enzyme, we detected a high variability of the high-mannose-type N-glycans which prevail at all glycosylation sites.
19864504	3	15	theme	cells	499:503	arg1	lysosomes					478:486	the lysosomes	474:486	the lysosomes of patient cells	474:503	This therapy depends on N-linked oligosaccharide-mediated delivery of intravenously injected recombinant enzyme to the lysosomes of patient cells.
19864504	9	16	theme	CHO	1200:1202	arg1	cells					1204:1208	CHO cells	1200:1208	CHO cells cultured under bioreactor conditions	1200:1245	CHO cells cultured under bioreactor conditions yielded recombinant ASA with the most preserved N-glycan structures, the highest mannose-6-phosphate content and the highest similarity to non-recombinant enzyme.
19864504	2	17	theme	replacement	270:280	arg1	therapy					282:288	Enzyme replacement therapy	263:288	Enzyme replacement therapy (ERT)	263:294	Enzyme replacement therapy (ERT) is a therapeutic option for MLD and other lysosomal disorders.
19864504	2	17	theme	replacement	270:280	arg1	option					313:318	a therapeutic option	299:318	a therapeutic option for MLD and other lysosomal disorders	299:356	Enzyme replacement therapy (ERT) is a therapeutic option for MLD and other lysosomal disorders.
19864504	2	17	theme	replacement	270:280	arg1	ERT					291:293	ERT	291:293	ERT	291:293	Enzyme replacement therapy (ERT) is a therapeutic option for MLD and other lysosomal disorders.
19864504	1	18	theme	storage	177:183	arg1	disease					185:191	a lysosomal storage disease	165:191	a lysosomal storage disease caused by a deficiency of the lysosomal enzyme arylsulfatase A (ASA)	165:260	Metachromatic leukodystrophy (MLD) is a lysosomal storage disease caused by a deficiency of the lysosomal enzyme arylsulfatase A (ASA).
19864504	1	18	theme	storage	177:183	arg1	leukodystrophy					141:154	Metachromatic leukodystrophy	127:154	Metachromatic leukodystrophy (MLD)	127:160	Metachromatic leukodystrophy (MLD) is a lysosomal storage disease caused by a deficiency of the lysosomal enzyme arylsulfatase A (ASA).
19864504	3	19	theme	N-linked	383:390	arg1	delivery					417:424	N-linked oligosaccharide-mediated delivery	383:424	N-linked oligosaccharide-mediated delivery of intravenously injected recombinant enzyme to the lysosomes of patient cells	383:503	This therapy depends on N-linked oligosaccharide-mediated delivery of intravenously injected recombinant enzyme to the lysosomes of patient cells.
19864504	4	20	link	N-linked	535:542	arg1	chains					565:570	N-linked oligosaccharide side chains	535:570	N-linked oligosaccharide side chains	535:570	Because of the importance of N-linked oligosaccharide side chains in ERT, we examined the composition of the three N-linked glycans of four different recombinant ASAs in a site-specific manner.
19864504	11	21	theme	lysosomal	1556:1564	arg1	enzymes					1566:1572	numerous recombinant lysosomal enzymes	1535:1572	numerous recombinant lysosomal enzymes	1535:1572	In the last years, numerous recombinant lysosomal enzymes were used for preclinical ERT trials.
19864504	2	22	theme	Enzyme	263:268	arg1	therapy					282:288	Enzyme replacement therapy	263:288	Enzyme replacement therapy (ERT)	263:294	Enzyme replacement therapy (ERT) is a therapeutic option for MLD and other lysosomal disorders.
19864504	2	22	theme	Enzyme	263:268	arg1	option					313:318	a therapeutic option	299:318	a therapeutic option for MLD and other lysosomal disorders	299:356	Enzyme replacement therapy (ERT) is a therapeutic option for MLD and other lysosomal disorders.
19864504	2	22	theme	Enzyme	263:268	arg1	ERT					291:293	ERT	291:293	ERT	291:293	Enzyme replacement therapy (ERT) is a therapeutic option for MLD and other lysosomal disorders.
19864504	3	23	theme	recombinant	452:462	arg1	enzyme					464:469	intravenously injected recombinant enzyme	429:469	intravenously injected recombinant enzyme	429:469	This therapy depends on N-linked oligosaccharide-mediated delivery of intravenously injected recombinant enzyme to the lysosomes of patient cells.
19864504	12	24	from	trials	1691:1696	arg1	structures					1651:1660	the oligosaccharide structures	1631:1660	the oligosaccharide structures	1631:1660	Our data show that the oligosaccharide structures were very different in these trials making it difficult to draw common conclusions from the various investigations.
19864504	12	24	from	trials	1691:1696	arg1	different					1672:1680	different	1672:1680	different	1672:1680	Our data show that the oligosaccharide structures were very different in these trials making it difficult to draw common conclusions from the various investigations.
19864504	9	25	theme	mannose-6-phosphate	1328:1346	arg1	content					1348:1354	the highest mannose-6-phosphate content	1316:1354	the highest mannose-6-phosphate content	1316:1354	CHO cells cultured under bioreactor conditions yielded recombinant ASA with the most preserved N-glycan structures, the highest mannose-6-phosphate content and the highest similarity to non-recombinant enzyme.
19864504	0	26	theme	Site-specific	0:12	arg1	analysis					14:21	Site-specific analysis	0:21	Site-specific analysis of N-linked oligosaccharides of recombinant lysosomal arylsulfatase A	0:91	Site-specific analysis of N-linked oligosaccharides of recombinant lysosomal arylsulfatase A produced in different cell lines.
19864504	7	27	from	sites	1086:1090	arg1	glycans					1049:1055	the glycans	1045:1055	the glycans at the three N-glycosylation sites	1045:1090	The susceptibility for trimming is different for the glycans at the three N-glycosylation sites.
19864504	10	28	theme	N-glycans	1444:1452	arg1	one-third					1427:1435	one-third	1427:1435	one-third	1427:1435	Notably, roughly one-third of the N-glycans released from the three glycosylation sites were fucosylated.
19864504	10	28	theme	N-glycans	1444:1452	arg1	N-glycans					1444:1452	the N-glycans	1440:1452	the N-glycans released from the three glycosylation sites	1440:1496	Notably, roughly one-third of the N-glycans released from the three glycosylation sites were fucosylated.
19864504	5	29	theme	glycosylation	864:876	arg1	sites					878:882	all glycosylation sites	860:882	all glycosylation sites	860:882	Depending on the culture conditions and the cell line expressing the enzyme, we detected a high variability of the high-mannose-type N-glycans which prevail at all glycosylation sites.
19864504	11	30	used	used	1579:1582	arg2	enzymes					1566:1572	numerous recombinant lysosomal enzymes	1535:1572	numerous recombinant lysosomal enzymes	1535:1572	In the last years, numerous recombinant lysosomal enzymes were used for preclinical ERT trials.
19864504	0	31	theme	N-linked	26:33	arg1	oligosaccharides					35:50	N-linked oligosaccharides	26:50	N-linked oligosaccharides of recombinant lysosomal arylsulfatase A	26:91	Site-specific analysis of N-linked oligosaccharides of recombinant lysosomal arylsulfatase A produced in different cell lines.
19864504	4	32	theme	chains	565:570	arg1	importance					521:530	the importance	517:530	the importance of N-linked oligosaccharide side chains in ERT	517:577	Because of the importance of N-linked oligosaccharide side chains in ERT, we examined the composition of the three N-linked glycans of four different recombinant ASAs in a site-specific manner.
19864504	9	33	theme	bioreactor	1225:1234	arg1	conditions					1236:1245	bioreactor conditions	1225:1245	bioreactor conditions	1225:1245	CHO cells cultured under bioreactor conditions yielded recombinant ASA with the most preserved N-glycan structures, the highest mannose-6-phosphate content and the highest similarity to non-recombinant enzyme.
19864504	10	34	attach	released	1454:1461	arg2	N-glycans					1444:1452	the N-glycans	1440:1452	the N-glycans released from the three glycosylation sites	1440:1496	Notably, roughly one-third of the N-glycans released from the three glycosylation sites were fucosylated.
19864504	10	34	attach	released	1454:1461	arg1	sites					1492:1496	the three glycosylation sites	1468:1496	the three glycosylation sites	1468:1496	Notably, roughly one-third of the N-glycans released from the three glycosylation sites were fucosylated.
19864504	9	35	with	ASA	1267:1269	arg1	similarity					1372:1381	the highest similarity	1360:1381	the highest similarity to non-recombinant enzyme	1360:1407	CHO cells cultured under bioreactor conditions yielded recombinant ASA with the most preserved N-glycan structures, the highest mannose-6-phosphate content and the highest similarity to non-recombinant enzyme.
19864504	9	35	with	ASA	1267:1269	arg1	content					1348:1354	the highest mannose-6-phosphate content	1316:1354	the highest mannose-6-phosphate content	1316:1354	CHO cells cultured under bioreactor conditions yielded recombinant ASA with the most preserved N-glycan structures, the highest mannose-6-phosphate content and the highest similarity to non-recombinant enzyme.
19864504	9	35	with	ASA	1267:1269	arg1	structures					1304:1313	the most preserved N-glycan structures	1276:1313	the most preserved N-glycan structures	1276:1313	CHO cells cultured under bioreactor conditions yielded recombinant ASA with the most preserved N-glycan structures, the highest mannose-6-phosphate content and the highest similarity to non-recombinant enzyme.
19864504	5	36	theme	N-glycans	833:841	arg1	variability					796:806	a high variability	789:806	a high variability of the high-mannose-type N-glycans which prevail at all glycosylation sites	789:882	Depending on the culture conditions and the cell line expressing the enzyme, we detected a high variability of the high-mannose-type N-glycans which prevail at all glycosylation sites.
19864504	5	37	theme	high-mannose-type	815:831	arg1	N-glycans					833:841	the high-mannose-type N-glycans	811:841	the high-mannose-type N-glycans which prevail at all glycosylation sites	811:882	Depending on the culture conditions and the cell line expressing the enzyme, we detected a high variability of the high-mannose-type N-glycans which prevail at all glycosylation sites.
19864504	6	38	theme	substantial	960:970	arg1	trimming					972:979	substantial trimming	960:979	substantial trimming in the medium	960:993	Our data show that the composition of the glycans is largely determined by substantial trimming in the medium.
19864504	7	39	theme	N-glycosylation	1070:1084	arg1	sites					1086:1090	the three N-glycosylation sites	1060:1090	the three N-glycosylation sites	1060:1090	The susceptibility for trimming is different for the glycans at the three N-glycosylation sites.
19864504	4	40	link	N-linked	621:628	arg1	glycans					630:636	the three N-linked glycans	611:636	the three N-linked glycans	611:636	Because of the importance of N-linked oligosaccharide side chains in ERT, we examined the composition of the three N-linked glycans of four different recombinant ASAs in a site-specific manner.
19864504	12	41	from	different	1672:1680	arg1	trials					1691:1696	these trials	1685:1696	these trials	1685:1696	Our data show that the oligosaccharide structures were very different in these trials making it difficult to draw common conclusions from the various investigations.
19864504	4	42	theme	glycans	630:636	arg1	composition					596:606	the composition	592:606	the composition of the three N-linked glycans of four different recombinant ASAs	592:671	Because of the importance of N-linked oligosaccharide side chains in ERT, we examined the composition of the three N-linked glycans of four different recombinant ASAs in a site-specific manner.
19864504	3	43	theme	oligosaccharide-mediated	392:415	arg1	delivery					417:424	N-linked oligosaccharide-mediated delivery	383:424	N-linked oligosaccharide-mediated delivery of intravenously injected recombinant enzyme to the lysosomes of patient cells	383:503	This therapy depends on N-linked oligosaccharide-mediated delivery of intravenously injected recombinant enzyme to the lysosomes of patient cells.
19864504	5	44	theme	culture	717:723	arg1	conditions					725:734	the culture conditions	713:734	the culture conditions	713:734	Depending on the culture conditions and the cell line expressing the enzyme, we detected a high variability of the high-mannose-type N-glycans which prevail at all glycosylation sites.
19864504	4	45	theme	different	646:654	arg1	ASAs					668:671	four different recombinant ASAs	641:671	four different recombinant ASAs	641:671	Because of the importance of N-linked oligosaccharide side chains in ERT, we examined the composition of the three N-linked glycans of four different recombinant ASAs in a site-specific manner.
19864504	12	46	theme	common	1726:1731	arg1	conclusions					1733:1743	common conclusions	1726:1743	common conclusions	1726:1743	Our data show that the oligosaccharide structures were very different in these trials making it difficult to draw common conclusions from the various investigations.
19864504	10	47	gly	fucosylated	1503:1513	arg1	one-third					1427:1435	one-third	1427:1435	one-third	1427:1435	Notably, roughly one-third of the N-glycans released from the three glycosylation sites were fucosylated.
19864504	10	47	gly	fucosylated	1503:1513	arg1	N-glycans					1444:1452	the N-glycans	1440:1452	the N-glycans released from the three glycosylation sites	1440:1496	Notably, roughly one-third of the N-glycans released from the three glycosylation sites were fucosylated.
19864504	3	48	theme	enzyme	464:469	arg1	delivery					417:424	N-linked oligosaccharide-mediated delivery	383:424	N-linked oligosaccharide-mediated delivery of intravenously injected recombinant enzyme to the lysosomes of patient cells	383:503	This therapy depends on N-linked oligosaccharide-mediated delivery of intravenously injected recombinant enzyme to the lysosomes of patient cells.
19864504	0	49	theme	oligosaccharides	35:50	arg1	analysis					14:21	Site-specific analysis	0:21	Site-specific analysis of N-linked oligosaccharides of recombinant lysosomal arylsulfatase A	0:91	Site-specific analysis of N-linked oligosaccharides of recombinant lysosomal arylsulfatase A produced in different cell lines.
19864504	4	50	theme	N-linked	535:542	arg1	chains					565:570	N-linked oligosaccharide side chains	535:570	N-linked oligosaccharide side chains	535:570	Because of the importance of N-linked oligosaccharide side chains in ERT, we examined the composition of the three N-linked glycans of four different recombinant ASAs in a site-specific manner.
19864504	6	51	from	trimming	972:979	arg1	medium					988:993	the medium	984:993	the medium	984:993	Our data show that the composition of the glycans is largely determined by substantial trimming in the medium.
19864504	9	52	theme	recombinant	1255:1265	arg1	ASA					1267:1269	recombinant ASA	1255:1269	recombinant ASA with the most preserved N-glycan structures, the highest mannose-6-phosphate content and the highest similarity to non-recombinant enzyme	1255:1407	CHO cells cultured under bioreactor conditions yielded recombinant ASA with the most preserved N-glycan structures, the highest mannose-6-phosphate content and the highest similarity to non-recombinant enzyme.
19864504	3	53	link	N-linked	383:390	arg1	delivery					417:424	N-linked oligosaccharide-mediated delivery	383:424	N-linked oligosaccharide-mediated delivery of intravenously injected recombinant enzyme to the lysosomes of patient cells	383:503	This therapy depends on N-linked oligosaccharide-mediated delivery of intravenously injected recombinant enzyme to the lysosomes of patient cells.
19864504	6	54	theme	glycans	927:933	arg1	composition					908:918	the composition	904:918	the composition of the glycans	904:933	Our data show that the composition of the glycans is largely determined by substantial trimming in the medium.
19864504	0	55	theme	lysosomal	67:75	arg1	A					91:91	recombinant lysosomal arylsulfatase A	55:91	recombinant lysosomal arylsulfatase A	55:91	Site-specific analysis of N-linked oligosaccharides of recombinant lysosomal arylsulfatase A produced in different cell lines.
19864504	9	56	theme	non-recombinant	1386:1400	arg1	enzyme					1402:1407	non-recombinant enzyme	1386:1407	non-recombinant enzyme	1386:1407	CHO cells cultured under bioreactor conditions yielded recombinant ASA with the most preserved N-glycan structures, the highest mannose-6-phosphate content and the highest similarity to non-recombinant enzyme.
19864504	5	57	theme	high	791:794	arg1	variability					796:806	a high variability	789:806	a high variability of the high-mannose-type N-glycans which prevail at all glycosylation sites	789:882	Depending on the culture conditions and the cell line expressing the enzyme, we detected a high variability of the high-mannose-type N-glycans which prevail at all glycosylation sites.
19864504	3	58	theme	injected	443:450	arg1	enzyme					464:469	intravenously injected recombinant enzyme	429:469	intravenously injected recombinant enzyme	429:469	This therapy depends on N-linked oligosaccharide-mediated delivery of intravenously injected recombinant enzyme to the lysosomes of patient cells.
19864504	1	59	theme	Metachromatic	127:139	arg1	MLD					157:159	MLD	157:159	MLD	157:159	Metachromatic leukodystrophy (MLD) is a lysosomal storage disease caused by a deficiency of the lysosomal enzyme arylsulfatase A (ASA).
19864504	1	59	theme	Metachromatic	127:139	arg1	leukodystrophy					141:154	Metachromatic leukodystrophy	127:154	Metachromatic leukodystrophy (MLD)	127:160	Metachromatic leukodystrophy (MLD) is a lysosomal storage disease caused by a deficiency of the lysosomal enzyme arylsulfatase A (ASA).
19864504	1	59	theme	Metachromatic	127:139	arg1	disease					185:191	a lysosomal storage disease	165:191	a lysosomal storage disease caused by a deficiency of the lysosomal enzyme arylsulfatase A (ASA)	165:260	Metachromatic leukodystrophy (MLD) is a lysosomal storage disease caused by a deficiency of the lysosomal enzyme arylsulfatase A (ASA).
19864504	0	60	theme	recombinant	55:65	arg1	A					91:91	recombinant lysosomal arylsulfatase A	55:91	recombinant lysosomal arylsulfatase A	55:91	Site-specific analysis of N-linked oligosaccharides of recombinant lysosomal arylsulfatase A produced in different cell lines.
19864504	4	61	theme	side	560:563	arg1	chains					565:570	N-linked oligosaccharide side chains	535:570	N-linked oligosaccharide side chains	535:570	Because of the importance of N-linked oligosaccharide side chains in ERT, we examined the composition of the three N-linked glycans of four different recombinant ASAs in a site-specific manner.
19864504	11	62	theme	last	1523:1526	arg1	years					1528:1532	the last years	1519:1532	the last years	1519:1532	In the last years, numerous recombinant lysosomal enzymes were used for preclinical ERT trials.
19864504	12	63	theme	various	1754:1760	arg1	investigations					1762:1775	the various investigations	1750:1775	the various investigations	1750:1775	Our data show that the oligosaccharide structures were very different in these trials making it difficult to draw common conclusions from the various investigations.
19864504	4	64	theme	oligosaccharide	544:558	arg1	chains					565:570	N-linked oligosaccharide side chains	535:570	N-linked oligosaccharide side chains	535:570	Because of the importance of N-linked oligosaccharide side chains in ERT, we examined the composition of the three N-linked glycans of four different recombinant ASAs in a site-specific manner.
19864504	11	65	theme	ERT	1600:1602	arg1	trials					1604:1609	preclinical ERT trials	1588:1609	preclinical ERT trials	1588:1609	In the last years, numerous recombinant lysosomal enzymes were used for preclinical ERT trials.
19864504	4	66	theme	site-specific	678:690	arg1	manner					692:697	a site-specific manner	676:697	a site-specific manner	676:697	Because of the importance of N-linked oligosaccharide side chains in ERT, we examined the composition of the three N-linked glycans of four different recombinant ASAs in a site-specific manner.
19864504	1	67	theme	lysosomal	223:231	arg1	ASA					257:259	ASA	257:259	ASA	257:259	Metachromatic leukodystrophy (MLD) is a lysosomal storage disease caused by a deficiency of the lysosomal enzyme arylsulfatase A (ASA).
19864504	1	67	theme	lysosomal	223:231	arg1	A					254:254	the lysosomal enzyme arylsulfatase A	219:254	the lysosomal enzyme arylsulfatase A (ASA)	219:260	Metachromatic leukodystrophy (MLD) is a lysosomal storage disease caused by a deficiency of the lysosomal enzyme arylsulfatase A (ASA).
19864504	9	68	theme	most	1280:1283	arg1	structures					1304:1313	the most preserved N-glycan structures	1276:1313	the most preserved N-glycan structures	1276:1313	CHO cells cultured under bioreactor conditions yielded recombinant ASA with the most preserved N-glycan structures, the highest mannose-6-phosphate content and the highest similarity to non-recombinant enzyme.
19864504	8	69	theme	production	1177:1186	arg1	conditions					1188:1197	production conditions	1177:1197	production conditions	1177:1197	Interestingly, which of the glycans is most susceptible to trimming also depends on production conditions.
19864504	9	70	theme	highest	1364:1370	arg1	similarity					1372:1381	the highest similarity	1360:1381	the highest similarity to non-recombinant enzyme	1360:1407	CHO cells cultured under bioreactor conditions yielded recombinant ASA with the most preserved N-glycan structures, the highest mannose-6-phosphate content and the highest similarity to non-recombinant enzyme.
19864504	2	71	theme	therapeutic	301:311	arg1	therapy					282:288	Enzyme replacement therapy	263:288	Enzyme replacement therapy (ERT)	263:294	Enzyme replacement therapy (ERT) is a therapeutic option for MLD and other lysosomal disorders.
19864504	2	71	theme	therapeutic	301:311	arg1	option					313:318	a therapeutic option	299:318	a therapeutic option for MLD and other lysosomal disorders	299:356	Enzyme replacement therapy (ERT) is a therapeutic option for MLD and other lysosomal disorders.
19864504	1	72	theme	enzyme	233:238	arg1	ASA					257:259	ASA	257:259	ASA	257:259	Metachromatic leukodystrophy (MLD) is a lysosomal storage disease caused by a deficiency of the lysosomal enzyme arylsulfatase A (ASA).
19864504	1	72	theme	enzyme	233:238	arg1	A					254:254	the lysosomal enzyme arylsulfatase A	219:254	the lysosomal enzyme arylsulfatase A (ASA)	219:260	Metachromatic leukodystrophy (MLD) is a lysosomal storage disease caused by a deficiency of the lysosomal enzyme arylsulfatase A (ASA).
19864504	0	73	theme	A	91:91	arg1	oligosaccharides					35:50	N-linked oligosaccharides	26:50	N-linked oligosaccharides of recombinant lysosomal arylsulfatase A	26:91	Site-specific analysis of N-linked oligosaccharides of recombinant lysosomal arylsulfatase A produced in different cell lines.
19864504	9	74	theme	preserved	1285:1293	arg1	structures					1304:1313	the most preserved N-glycan structures	1276:1313	the most preserved N-glycan structures	1276:1313	CHO cells cultured under bioreactor conditions yielded recombinant ASA with the most preserved N-glycan structures, the highest mannose-6-phosphate content and the highest similarity to non-recombinant enzyme.
19864504	11	75	theme	recombinant	1544:1554	arg1	enzymes					1566:1572	numerous recombinant lysosomal enzymes	1535:1572	numerous recombinant lysosomal enzymes	1535:1572	In the last years, numerous recombinant lysosomal enzymes were used for preclinical ERT trials.
19864504	4	76	theme	N-linked	621:628	arg1	glycans					630:636	the three N-linked glycans	611:636	the three N-linked glycans	611:636	Because of the importance of N-linked oligosaccharide side chains in ERT, we examined the composition of the three N-linked glycans of four different recombinant ASAs in a site-specific manner.
19864504	7	77	gly	N-glycosylation	1070:1084	arg2	sites					1086:1090	the three N-glycosylation sites	1060:1090	the three N-glycosylation sites	1060:1090	The susceptibility for trimming is different for the glycans at the three N-glycosylation sites.
19864504	7	77	gly	N-glycosylation	1070:1084	arg2	three					1064:1068	three	1064:1068	three	1064:1068	The susceptibility for trimming is different for the glycans at the three N-glycosylation sites.
19864504	4	78	theme	recombinant	656:666	arg1	ASAs					668:671	four different recombinant ASAs	641:671	four different recombinant ASAs	641:671	Because of the importance of N-linked oligosaccharide side chains in ERT, we examined the composition of the three N-linked glycans of four different recombinant ASAs in a site-specific manner.
19864504	1	79	theme	arylsulfatase	240:252	arg1	ASA					257:259	ASA	257:259	ASA	257:259	Metachromatic leukodystrophy (MLD) is a lysosomal storage disease caused by a deficiency of the lysosomal enzyme arylsulfatase A (ASA).
19864504	1	79	theme	arylsulfatase	240:252	arg1	A					254:254	the lysosomal enzyme arylsulfatase A	219:254	the lysosomal enzyme arylsulfatase A (ASA)	219:260	Metachromatic leukodystrophy (MLD) is a lysosomal storage disease caused by a deficiency of the lysosomal enzyme arylsulfatase A (ASA).
19864504	0	80	theme	arylsulfatase	77:89	arg1	A					91:91	recombinant lysosomal arylsulfatase A	55:91	recombinant lysosomal arylsulfatase A	55:91	Site-specific analysis of N-linked oligosaccharides of recombinant lysosomal arylsulfatase A produced in different cell lines.
19864504	9	81	theme	N-glycan	1295:1302	arg1	structures					1304:1313	the most preserved N-glycan structures	1276:1313	the most preserved N-glycan structures	1276:1313	CHO cells cultured under bioreactor conditions yielded recombinant ASA with the most preserved N-glycan structures, the highest mannose-6-phosphate content and the highest similarity to non-recombinant enzyme.
19864504	2	82	theme	lysosomal	338:346	arg1	disorders					348:356	other lysosomal disorders	332:356	other lysosomal disorders	332:356	Enzyme replacement therapy (ERT) is a therapeutic option for MLD and other lysosomal disorders.
19864504	10	83	gly	glycosylation	1478:1490	arg2	sites					1492:1496	the three glycosylation sites	1468:1496	the three glycosylation sites	1468:1496	Notably, roughly one-third of the N-glycans released from the three glycosylation sites were fucosylated.
19864504	10	83	gly	glycosylation	1478:1490	arg2	three					1472:1476	three	1472:1476	three	1472:1476	Notably, roughly one-third of the N-glycans released from the three glycosylation sites were fucosylated.
19864504	1	84	theme	A	254:254	arg1	deficiency					205:214	a deficiency	203:214	a deficiency of the lysosomal enzyme arylsulfatase A (ASA)	203:260	Metachromatic leukodystrophy (MLD) is a lysosomal storage disease caused by a deficiency of the lysosomal enzyme arylsulfatase A (ASA).
7727388	7	0	theme	amino	1424:1428	arg1	loop					1435:1438	the second 49 amino acid loop	1410:1438	the second 49 amino acid loop in common with NPR-C	1410:1459	These data describe the intra- and intermolecular linkages in NPR-C, providing a model for the homologous guanylyl cyclase receptors, NPR-A and NPR-B; both of the cyclase receptors likely contain the first amino-terminal 29 amino acid loop, but only NPR-A possesses the second 49 amino acid loop in common with NPR-C.
7727388	3	1	theme	extracellular	492:504	arg1	domain					506:511	the extracellular domain	488:511	the extracellular domain	488:511	Two sources and types of ANP affinity-purified human NPR-C were used to map disulfide linkages and glycosylation sites of this receptor by mass spectrometry: the extracellular domain obtained by papain cleavage of a receptor-IgG fusion protein expressed in Chinese hamster ovary cells, and a baculovirus/Sf9-expressed cytoplasmic truncation mutant in which 34 of 37 cytoplasmic domain amino acids were deleted.
7727388	7	2	theme	second	1414:1419	arg1	loop					1435:1438	the second 49 amino acid loop	1410:1438	the second 49 amino acid loop in common with NPR-C	1410:1459	These data describe the intra- and intermolecular linkages in NPR-C, providing a model for the homologous guanylyl cyclase receptors, NPR-A and NPR-B; both of the cyclase receptors likely contain the first amino-terminal 29 amino acid loop, but only NPR-A possesses the second 49 amino acid loop in common with NPR-C.
7727388	7	3	theme	amino	1368:1372	arg1	acid					1374:1377	29 amino acid	1365:1377	the first amino-terminal 29 amino acid loop	1340:1382	These data describe the intra- and intermolecular linkages in NPR-C, providing a model for the homologous guanylyl cyclase receptors, NPR-A and NPR-B; both of the cyclase receptors likely contain the first amino-terminal 29 amino acid loop, but only NPR-A possesses the second 49 amino acid loop in common with NPR-C.
7727388	3	4	theme	amino	715:719	arg1	acids					721:725	37 cytoplasmic domain amino acids	693:725	37 cytoplasmic domain amino acids	693:725	Two sources and types of ANP affinity-purified human NPR-C were used to map disulfide linkages and glycosylation sites of this receptor by mass spectrometry: the extracellular domain obtained by papain cleavage of a receptor-IgG fusion protein expressed in Chinese hamster ovary cells, and a baculovirus/Sf9-expressed cytoplasmic truncation mutant in which 34 of 37 cytoplasmic domain amino acids were deleted.
7727388	3	5	theme	papain	525:530	arg1	cleavage					532:539	papain cleavage	525:539	papain cleavage of a receptor-IgG fusion protein expressed in Chinese hamster ovary cells, and a baculovirus/Sf9-expressed cytoplasmic truncation mutant in which 34 of 37 cytoplasmic domain amino acids were deleted	525:738	Two sources and types of ANP affinity-purified human NPR-C were used to map disulfide linkages and glycosylation sites of this receptor by mass spectrometry: the extracellular domain obtained by papain cleavage of a receptor-IgG fusion protein expressed in Chinese hamster ovary cells, and a baculovirus/Sf9-expressed cytoplasmic truncation mutant in which 34 of 37 cytoplasmic domain amino acids were deleted.
7727388	7	6	theme	amino-terminal	1350:1363	arg1	loop					1379:1382	the first amino-terminal 29 amino acid loop	1340:1382	the first amino-terminal 29 amino acid loop	1340:1382	These data describe the intra- and intermolecular linkages in NPR-C, providing a model for the homologous guanylyl cyclase receptors, NPR-A and NPR-B; both of the cyclase receptors likely contain the first amino-terminal 29 amino acid loop, but only NPR-A possesses the second 49 amino acid loop in common with NPR-C.
7727388	2	7	link	disulfide-linked	260:275	arg1	homodimer					277:285	a disulfide-linked homodimer	258:285	a disulfide-linked homodimer with a subunit molecular weight of 68,000	258:327	This cell surface glycoprotein is a disulfide-linked homodimer with a subunit molecular weight of 68,000.
7727388	2	7	link	disulfide-linked	260:275	arg1	glycoprotein					242:253	This cell surface glycoprotein	224:253	This cell surface glycoprotein	224:253	This cell surface glycoprotein is a disulfide-linked homodimer with a subunit molecular weight of 68,000.
7727388	2	8	theme	molecular	302:310	arg1	weight					312:317	a subunit molecular weight	292:317	a subunit molecular weight of 68,000	292:327	This cell surface glycoprotein is a disulfide-linked homodimer with a subunit molecular weight of 68,000.
7727388	3	9	theme	receptor-IgG	546:557	arg1	protein					566:572	a receptor-IgG fusion protein	544:572	a receptor-IgG fusion protein expressed in Chinese hamster ovary cells, and a baculovirus/Sf9-expressed cytoplasmic truncation mutant in which 34 of 37 cytoplasmic domain amino acids were deleted	544:738	Two sources and types of ANP affinity-purified human NPR-C were used to map disulfide linkages and glycosylation sites of this receptor by mass spectrometry: the extracellular domain obtained by papain cleavage of a receptor-IgG fusion protein expressed in Chinese hamster ovary cells, and a baculovirus/Sf9-expressed cytoplasmic truncation mutant in which 34 of 37 cytoplasmic domain amino acids were deleted.
7727388	1	10	theme	peptide	193:199	arg1	sites					209:213	the natriuretic peptide binding sites	177:213	the natriuretic peptide binding sites in vivo	177:221	The natriuretic peptide receptor-C (NPR-C) constitutes greater than 95% of the natriuretic peptide binding sites in vivo.
7727388	3	11	theme	hamster	595:601	arg1	cells					609:613	Chinese hamster ovary cells	587:613	Chinese hamster ovary cells	587:613	Two sources and types of ANP affinity-purified human NPR-C were used to map disulfide linkages and glycosylation sites of this receptor by mass spectrometry: the extracellular domain obtained by papain cleavage of a receptor-IgG fusion protein expressed in Chinese hamster ovary cells, and a baculovirus/Sf9-expressed cytoplasmic truncation mutant in which 34 of 37 cytoplasmic domain amino acids were deleted.
7727388	1	12	theme	sites	209:213	arg1	%					172:172	greater than 95%	157:172	greater than 95% of the natriuretic peptide binding sites in vivo	157:221	The natriuretic peptide receptor-C (NPR-C) constitutes greater than 95% of the natriuretic peptide binding sites in vivo.
7727388	1	12	theme	sites	209:213	arg1	sites					209:213	the natriuretic peptide binding sites	177:213	the natriuretic peptide binding sites in vivo	177:221	The natriuretic peptide receptor-C (NPR-C) constitutes greater than 95% of the natriuretic peptide binding sites in vivo.
7727388	7	13	theme	cyclase	1307:1313	arg1	receptors					1315:1323	the cyclase receptors	1303:1323	the cyclase receptors	1303:1323	These data describe the intra- and intermolecular linkages in NPR-C, providing a model for the homologous guanylyl cyclase receptors, NPR-A and NPR-B; both of the cyclase receptors likely contain the first amino-terminal 29 amino acid loop, but only NPR-A possesses the second 49 amino acid loop in common with NPR-C.
7727388	1	14	theme	receptor-C	126:135	arg1	peptide					118:124	The natriuretic peptide receptor-C	102:135	The natriuretic peptide receptor-C (NPR-C)	102:143	The natriuretic peptide receptor-C (NPR-C) constitutes greater than 95% of the natriuretic peptide binding sites in vivo.
7727388	1	14	theme	receptor-C	126:135	arg1	NPR-C					138:142	NPR-C	138:142	NPR-C	138:142	The natriuretic peptide receptor-C (NPR-C) constitutes greater than 95% of the natriuretic peptide binding sites in vivo.
7727388	6	15	theme	Asn-linked	1024:1033	arg1	sites					1049:1053	the four potential Asn-linked glycosylation sites	1005:1053	the four potential Asn-linked glycosylation sites	1005:1053	Three of the four potential Asn-linked glycosylation sites are occupied: N41 (complex), N248 (high mannose), and N349 (complex; partial occupancy).
7727388	7	16	from	linkages	1194:1201	arg1	NPR-C					1206:1210	NPR-C	1206:1210	NPR-C	1206:1210	These data describe the intra- and intermolecular linkages in NPR-C, providing a model for the homologous guanylyl cyclase receptors, NPR-A and NPR-B; both of the cyclase receptors likely contain the first amino-terminal 29 amino acid loop, but only NPR-A possesses the second 49 amino acid loop in common with NPR-C.
7727388	0	17	theme	human	54:58	arg1	homodimer					91:99	the human natriuretic peptide receptor-C homodimer	50:99	the human natriuretic peptide receptor-C homodimer	50:99	The disulfide linkages and glycosylation sites of the human natriuretic peptide receptor-C homodimer.
7727388	2	18	theme	cell	229:232	arg1	homodimer					277:285	a disulfide-linked homodimer	258:285	a disulfide-linked homodimer with a subunit molecular weight of 68,000	258:327	This cell surface glycoprotein is a disulfide-linked homodimer with a subunit molecular weight of 68,000.
7727388	2	18	theme	cell	229:232	arg1	glycoprotein					242:253	This cell surface glycoprotein	224:253	This cell surface glycoprotein	224:253	This cell surface glycoprotein is a disulfide-linked homodimer with a subunit molecular weight of 68,000.
7727388	2	19	with	homodimer	277:285	arg1	weight					312:317	a subunit molecular weight	292:317	a subunit molecular weight of 68,000	292:327	This cell surface glycoprotein is a disulfide-linked homodimer with a subunit molecular weight of 68,000.
7727388	0	20	theme	peptide	72:78	arg1	homodimer					91:99	the human natriuretic peptide receptor-C homodimer	50:99	the human natriuretic peptide receptor-C homodimer	50:99	The disulfide linkages and glycosylation sites of the human natriuretic peptide receptor-C homodimer.
7727388	7	21	theme	intra-	1168:1173	arg1	linkages					1194:1201	the intra- and intermolecular linkages	1164:1201	the intra- and intermolecular linkages in NPR-C	1164:1210	These data describe the intra- and intermolecular linkages in NPR-C, providing a model for the homologous guanylyl cyclase receptors, NPR-A and NPR-B; both of the cyclase receptors likely contain the first amino-terminal 29 amino acid loop, but only NPR-A possesses the second 49 amino acid loop in common with NPR-C.
7727388	5	22	theme	site-directed	950:962	arg1	mutagenesis					964:974	site-directed mutagenesis	950:974	site-directed mutagenesis of full-length NPR	950:993	The juxtamembrane residues C428 and C431 are involved in homodimer formation, confirmed by site-directed mutagenesis of full-length NPR.
7727388	0	23	theme	homodimer	91:99	arg1	linkages					14:21	disulfide linkages	4:21	disulfide linkages	4:21	The disulfide linkages and glycosylation sites of the human natriuretic peptide receptor-C homodimer.
7727388	0	23	theme	homodimer	91:99	arg1	sites					41:45	glycosylation sites	27:45	glycosylation sites	27:45	The disulfide linkages and glycosylation sites of the human natriuretic peptide receptor-C homodimer.
7727388	0	23	theme	homodimer	91:99	arg1	homodimer					91:99	the human natriuretic peptide receptor-C homodimer	50:99	the human natriuretic peptide receptor-C homodimer	50:99	The disulfide linkages and glycosylation sites of the human natriuretic peptide receptor-C homodimer.
7727388	6	24	used	occupied	1059:1066	arg2	sites					1049:1053	the four potential Asn-linked glycosylation sites	1005:1053	the four potential Asn-linked glycosylation sites	1005:1053	Three of the four potential Asn-linked glycosylation sites are occupied: N41 (complex), N248 (high mannose), and N349 (complex; partial occupancy).
7727388	6	24	used	occupied	1059:1066	arg2	Three					996:1000	Three	996:1000	Three	996:1000	Three of the four potential Asn-linked glycosylation sites are occupied: N41 (complex), N248 (high mannose), and N349 (complex; partial occupancy).
7727388	5	25	theme	NPR	991:993	arg1	mutagenesis					964:974	site-directed mutagenesis	950:974	site-directed mutagenesis of full-length NPR	950:993	The juxtamembrane residues C428 and C431 are involved in homodimer formation, confirmed by site-directed mutagenesis of full-length NPR.
7727388	3	26	theme	human	377:381	arg1	NPR-C					383:387	ANP affinity-purified human NPR-C	355:387	ANP affinity-purified human NPR-C	355:387	Two sources and types of ANP affinity-purified human NPR-C were used to map disulfide linkages and glycosylation sites of this receptor by mass spectrometry: the extracellular domain obtained by papain cleavage of a receptor-IgG fusion protein expressed in Chinese hamster ovary cells, and a baculovirus/Sf9-expressed cytoplasmic truncation mutant in which 34 of 37 cytoplasmic domain amino acids were deleted.
7727388	7	27	theme	intermolecular	1179:1192	arg1	linkages					1194:1201	the intra- and intermolecular linkages	1164:1201	the intra- and intermolecular linkages in NPR-C	1164:1210	These data describe the intra- and intermolecular linkages in NPR-C, providing a model for the homologous guanylyl cyclase receptors, NPR-A and NPR-B; both of the cyclase receptors likely contain the first amino-terminal 29 amino acid loop, but only NPR-A possesses the second 49 amino acid loop in common with NPR-C.
7727388	3	28	theme	disulfide	406:414	arg1	linkages					416:423	disulfide linkages	406:423	disulfide linkages	406:423	Two sources and types of ANP affinity-purified human NPR-C were used to map disulfide linkages and glycosylation sites of this receptor by mass spectrometry: the extracellular domain obtained by papain cleavage of a receptor-IgG fusion protein expressed in Chinese hamster ovary cells, and a baculovirus/Sf9-expressed cytoplasmic truncation mutant in which 34 of 37 cytoplasmic domain amino acids were deleted.
7727388	3	29	theme	ANP	355:357	arg1	NPR-C					383:387	ANP affinity-purified human NPR-C	355:387	ANP affinity-purified human NPR-C	355:387	Two sources and types of ANP affinity-purified human NPR-C were used to map disulfide linkages and glycosylation sites of this receptor by mass spectrometry: the extracellular domain obtained by papain cleavage of a receptor-IgG fusion protein expressed in Chinese hamster ovary cells, and a baculovirus/Sf9-expressed cytoplasmic truncation mutant in which 34 of 37 cytoplasmic domain amino acids were deleted.
7727388	2	30	theme	surface	234:240	arg1	homodimer					277:285	a disulfide-linked homodimer	258:285	a disulfide-linked homodimer with a subunit molecular weight of 68,000	258:327	This cell surface glycoprotein is a disulfide-linked homodimer with a subunit molecular weight of 68,000.
7727388	2	30	theme	surface	234:240	arg1	glycoprotein					242:253	This cell surface glycoprotein	224:253	This cell surface glycoprotein	224:253	This cell surface glycoprotein is a disulfide-linked homodimer with a subunit molecular weight of 68,000.
7727388	4	31	theme	disulfide	760:768	arg1	loops					777:781	Two intramolecular disulfide bonded loops	741:781	Two intramolecular disulfide bonded loops	741:781	Two intramolecular disulfide bonded loops were found in the 435 amino acid extracellular domain (C63-C91, C168-C216).
7727388	1	32	theme	natriuretic	106:116	arg1	peptide					118:124	The natriuretic peptide receptor-C	102:135	The natriuretic peptide receptor-C (NPR-C)	102:143	The natriuretic peptide receptor-C (NPR-C) constitutes greater than 95% of the natriuretic peptide binding sites in vivo.
7727388	1	32	theme	natriuretic	106:116	arg1	NPR-C					138:142	NPR-C	138:142	NPR-C	138:142	The natriuretic peptide receptor-C (NPR-C) constitutes greater than 95% of the natriuretic peptide binding sites in vivo.
7727388	4	33	located	found	788:792	arg2	loops					777:781	Two intramolecular disulfide bonded loops	741:781	Two intramolecular disulfide bonded loops	741:781	Two intramolecular disulfide bonded loops were found in the 435 amino acid extracellular domain (C63-C91, C168-C216).
7727388	4	33	located	found	788:792	arg1	domain					830:835	the 435 amino acid extracellular domain	797:835	the 435 amino acid extracellular domain (C63-C91, C168-C216)	797:856	Two intramolecular disulfide bonded loops were found in the 435 amino acid extracellular domain (C63-C91, C168-C216).
7727388	3	34	theme	truncation	660:669	arg1	mutant					671:676	a baculovirus/Sf9-expressed cytoplasmic truncation mutant	620:676	a baculovirus/Sf9-expressed cytoplasmic truncation mutant in which 34 of 37 cytoplasmic domain amino acids were deleted	620:738	Two sources and types of ANP affinity-purified human NPR-C were used to map disulfide linkages and glycosylation sites of this receptor by mass spectrometry: the extracellular domain obtained by papain cleavage of a receptor-IgG fusion protein expressed in Chinese hamster ovary cells, and a baculovirus/Sf9-expressed cytoplasmic truncation mutant in which 34 of 37 cytoplasmic domain amino acids were deleted.
7727388	4	35	theme	extracellular	816:828	arg1	domain					830:835	the 435 amino acid extracellular domain	797:835	the 435 amino acid extracellular domain (C63-C91, C168-C216)	797:856	Two intramolecular disulfide bonded loops were found in the 435 amino acid extracellular domain (C63-C91, C168-C216).
7727388	0	36	theme	glycosylation	27:39	arg1	sites					41:45	glycosylation sites	27:45	glycosylation sites	27:45	The disulfide linkages and glycosylation sites of the human natriuretic peptide receptor-C homodimer.
7727388	0	36	theme	glycosylation	27:39	arg1	homodimer					91:99	the human natriuretic peptide receptor-C homodimer	50:99	the human natriuretic peptide receptor-C homodimer	50:99	The disulfide linkages and glycosylation sites of the human natriuretic peptide receptor-C homodimer.
7727388	7	37	theme	guanylyl	1250:1257	arg1	cyclase					1259:1265	homologous guanylyl cyclase	1239:1265	the homologous guanylyl cyclase receptors	1235:1275	These data describe the intra- and intermolecular linkages in NPR-C, providing a model for the homologous guanylyl cyclase receptors, NPR-A and NPR-B; both of the cyclase receptors likely contain the first amino-terminal 29 amino acid loop, but only NPR-A possesses the second 49 amino acid loop in common with NPR-C.
7727388	3	38	theme	baculovirus/Sf9-expressed	622:646	arg1	mutant					671:676	a baculovirus/Sf9-expressed cytoplasmic truncation mutant	620:676	a baculovirus/Sf9-expressed cytoplasmic truncation mutant in which 34 of 37 cytoplasmic domain amino acids were deleted	620:738	Two sources and types of ANP affinity-purified human NPR-C were used to map disulfide linkages and glycosylation sites of this receptor by mass spectrometry: the extracellular domain obtained by papain cleavage of a receptor-IgG fusion protein expressed in Chinese hamster ovary cells, and a baculovirus/Sf9-expressed cytoplasmic truncation mutant in which 34 of 37 cytoplasmic domain amino acids were deleted.
7727388	3	39	gly	glycosylation	429:441	arg2	receptor					457:464	this receptor	452:464	this receptor	452:464	Two sources and types of ANP affinity-purified human NPR-C were used to map disulfide linkages and glycosylation sites of this receptor by mass spectrometry: the extracellular domain obtained by papain cleavage of a receptor-IgG fusion protein expressed in Chinese hamster ovary cells, and a baculovirus/Sf9-expressed cytoplasmic truncation mutant in which 34 of 37 cytoplasmic domain amino acids were deleted.
7727388	3	39	gly	glycosylation	429:441	arg2	sites					443:447	glycosylation sites	429:447	glycosylation sites	429:447	Two sources and types of ANP affinity-purified human NPR-C were used to map disulfide linkages and glycosylation sites of this receptor by mass spectrometry: the extracellular domain obtained by papain cleavage of a receptor-IgG fusion protein expressed in Chinese hamster ovary cells, and a baculovirus/Sf9-expressed cytoplasmic truncation mutant in which 34 of 37 cytoplasmic domain amino acids were deleted.
7727388	3	39	gly	glycosylation	429:441	arg1	receptor					457:464	this receptor	452:464	this receptor	452:464	Two sources and types of ANP affinity-purified human NPR-C were used to map disulfide linkages and glycosylation sites of this receptor by mass spectrometry: the extracellular domain obtained by papain cleavage of a receptor-IgG fusion protein expressed in Chinese hamster ovary cells, and a baculovirus/Sf9-expressed cytoplasmic truncation mutant in which 34 of 37 cytoplasmic domain amino acids were deleted.
7727388	4	40	theme	acid	811:814	arg1	domain					830:835	the 435 amino acid extracellular domain	797:835	the 435 amino acid extracellular domain (C63-C91, C168-C216)	797:856	Two intramolecular disulfide bonded loops were found in the 435 amino acid extracellular domain (C63-C91, C168-C216).
7727388	2	41	theme	68,000	322:327	arg1	weight					312:317	a subunit molecular weight	292:317	a subunit molecular weight of 68,000	292:327	This cell surface glycoprotein is a disulfide-linked homodimer with a subunit molecular weight of 68,000.
7727388	1	42	theme	in	215:216	arg1	sites					209:213	the natriuretic peptide binding sites	177:213	the natriuretic peptide binding sites in vivo	177:221	The natriuretic peptide receptor-C (NPR-C) constitutes greater than 95% of the natriuretic peptide binding sites in vivo.
7727388	6	43	link	Asn-linked	1024:1033	arg1	sites					1049:1053	the four potential Asn-linked glycosylation sites	1005:1053	the four potential Asn-linked glycosylation sites	1005:1053	Three of the four potential Asn-linked glycosylation sites are occupied: N41 (complex), N248 (high mannose), and N349 (complex; partial occupancy).
7727388	7	44	theme	acid	1430:1433	arg1	loop					1435:1438	the second 49 amino acid loop	1410:1438	the second 49 amino acid loop in common with NPR-C	1410:1459	These data describe the intra- and intermolecular linkages in NPR-C, providing a model for the homologous guanylyl cyclase receptors, NPR-A and NPR-B; both of the cyclase receptors likely contain the first amino-terminal 29 amino acid loop, but only NPR-A possesses the second 49 amino acid loop in common with NPR-C.
7727388	0	45	dep	linkages	14:21	arg1	The					0:2	The	0:2	The	0:2	The disulfide linkages and glycosylation sites of the human natriuretic peptide receptor-C homodimer.
7727388	6	46	theme	sites	1049:1053	arg1	sites					1049:1053	the four potential Asn-linked glycosylation sites	1005:1053	the four potential Asn-linked glycosylation sites	1005:1053	Three of the four potential Asn-linked glycosylation sites are occupied: N41 (complex), N248 (high mannose), and N349 (complex; partial occupancy).
7727388	6	46	theme	sites	1049:1053	arg1	Three					996:1000	Three	996:1000	Three	996:1000	Three of the four potential Asn-linked glycosylation sites are occupied: N41 (complex), N248 (high mannose), and N349 (complex; partial occupancy).
7727388	4	47	theme	amino	805:809	arg1	domain					830:835	the 435 amino acid extracellular domain	797:835	the 435 amino acid extracellular domain (C63-C91, C168-C216)	797:856	Two intramolecular disulfide bonded loops were found in the 435 amino acid extracellular domain (C63-C91, C168-C216).
7727388	6	48	gly	glycosylation	1035:1047	arg2	sites					1049:1053	the four potential Asn-linked glycosylation sites	1005:1053	the four potential Asn-linked glycosylation sites	1005:1053	Three of the four potential Asn-linked glycosylation sites are occupied: N41 (complex), N248 (high mannose), and N349 (complex; partial occupancy).
7727388	6	48	gly	glycosylation	1035:1047	arg2	four					1009:1012	four	1009:1012	four	1009:1012	Three of the four potential Asn-linked glycosylation sites are occupied: N41 (complex), N248 (high mannose), and N349 (complex; partial occupancy).
7727388	7	49	from	loop	1435:1438	arg1	common					1443:1448	common	1443:1448	common	1443:1448	These data describe the intra- and intermolecular linkages in NPR-C, providing a model for the homologous guanylyl cyclase receptors, NPR-A and NPR-B; both of the cyclase receptors likely contain the first amino-terminal 29 amino acid loop, but only NPR-A possesses the second 49 amino acid loop in common with NPR-C.
7727388	3	50	theme	domain	708:713	arg1	acids					721:725	37 cytoplasmic domain amino acids	693:725	37 cytoplasmic domain amino acids	693:725	Two sources and types of ANP affinity-purified human NPR-C were used to map disulfide linkages and glycosylation sites of this receptor by mass spectrometry: the extracellular domain obtained by papain cleavage of a receptor-IgG fusion protein expressed in Chinese hamster ovary cells, and a baculovirus/Sf9-expressed cytoplasmic truncation mutant in which 34 of 37 cytoplasmic domain amino acids were deleted.
7727388	7	51	contain	contain	1332:1338	arg1	receptors					1315:1323	the cyclase receptors	1303:1323	the cyclase receptors	1303:1323	These data describe the intra- and intermolecular linkages in NPR-C, providing a model for the homologous guanylyl cyclase receptors, NPR-A and NPR-B; both of the cyclase receptors likely contain the first amino-terminal 29 amino acid loop, but only NPR-A possesses the second 49 amino acid loop in common with NPR-C.
7727388	7	51	contain	contain	1332:1338	arg2	loop					1379:1382	the first amino-terminal 29 amino acid loop	1340:1382	the first amino-terminal 29 amino acid loop	1340:1382	These data describe the intra- and intermolecular linkages in NPR-C, providing a model for the homologous guanylyl cyclase receptors, NPR-A and NPR-B; both of the cyclase receptors likely contain the first amino-terminal 29 amino acid loop, but only NPR-A possesses the second 49 amino acid loop in common with NPR-C.
7727388	7	51	contain	contain	1332:1338	arg1	both					1295:1298	both	1295:1298	both	1295:1298	These data describe the intra- and intermolecular linkages in NPR-C, providing a model for the homologous guanylyl cyclase receptors, NPR-A and NPR-B; both of the cyclase receptors likely contain the first amino-terminal 29 amino acid loop, but only NPR-A possesses the second 49 amino acid loop in common with NPR-C.
7727388	7	52	theme	acid	1374:1377	arg1	loop					1379:1382	the first amino-terminal 29 amino acid loop	1340:1382	the first amino-terminal 29 amino acid loop	1340:1382	These data describe the intra- and intermolecular linkages in NPR-C, providing a model for the homologous guanylyl cyclase receptors, NPR-A and NPR-B; both of the cyclase receptors likely contain the first amino-terminal 29 amino acid loop, but only NPR-A possesses the second 49 amino acid loop in common with NPR-C.
7727388	2	53	theme	disulfide-linked	260:275	arg1	homodimer					277:285	a disulfide-linked homodimer	258:285	a disulfide-linked homodimer with a subunit molecular weight of 68,000	258:327	This cell surface glycoprotein is a disulfide-linked homodimer with a subunit molecular weight of 68,000.
7727388	2	53	theme	disulfide-linked	260:275	arg1	glycoprotein					242:253	This cell surface glycoprotein	224:253	This cell surface glycoprotein	224:253	This cell surface glycoprotein is a disulfide-linked homodimer with a subunit molecular weight of 68,000.
7727388	6	54	theme	partial	1124:1130	arg1	occupancy					1132:1140	partial occupancy	1124:1140	complex; partial occupancy	1115:1140	Three of the four potential Asn-linked glycosylation sites are occupied: N41 (complex), N248 (high mannose), and N349 (complex; partial occupancy).
7727388	6	55	dep	N349	1109:1112	arg1	complex					1115:1121	complex	1115:1121	complex; partial occupancy	1115:1140	Three of the four potential Asn-linked glycosylation sites are occupied: N41 (complex), N248 (high mannose), and N349 (complex; partial occupancy).
7727388	2	56	gly	glycoprotein	242:253	arg1	homodimer					277:285	a disulfide-linked homodimer	258:285	a disulfide-linked homodimer with a subunit molecular weight of 68,000	258:327	This cell surface glycoprotein is a disulfide-linked homodimer with a subunit molecular weight of 68,000.
7727388	2	56	gly	glycoprotein	242:253	arg1	glycoprotein					242:253	This cell surface glycoprotein	224:253	This cell surface glycoprotein	224:253	This cell surface glycoprotein is a disulfide-linked homodimer with a subunit molecular weight of 68,000.
7727388	3	57	theme	acids	721:725	arg1	34					687:688	34	687:688	34 of 37 cytoplasmic domain amino acids	687:725	Two sources and types of ANP affinity-purified human NPR-C were used to map disulfide linkages and glycosylation sites of this receptor by mass spectrometry: the extracellular domain obtained by papain cleavage of a receptor-IgG fusion protein expressed in Chinese hamster ovary cells, and a baculovirus/Sf9-expressed cytoplasmic truncation mutant in which 34 of 37 cytoplasmic domain amino acids were deleted.
7727388	3	58	theme	fusion	559:564	arg1	protein					566:572	a receptor-IgG fusion protein	544:572	a receptor-IgG fusion protein expressed in Chinese hamster ovary cells, and a baculovirus/Sf9-expressed cytoplasmic truncation mutant in which 34 of 37 cytoplasmic domain amino acids were deleted	544:738	Two sources and types of ANP affinity-purified human NPR-C were used to map disulfide linkages and glycosylation sites of this receptor by mass spectrometry: the extracellular domain obtained by papain cleavage of a receptor-IgG fusion protein expressed in Chinese hamster ovary cells, and a baculovirus/Sf9-expressed cytoplasmic truncation mutant in which 34 of 37 cytoplasmic domain amino acids were deleted.
7727388	7	59	with	common	1443:1448	arg1	NPR-C					1455:1459	NPR-C	1455:1459	NPR-C	1455:1459	These data describe the intra- and intermolecular linkages in NPR-C, providing a model for the homologous guanylyl cyclase receptors, NPR-A and NPR-B; both of the cyclase receptors likely contain the first amino-terminal 29 amino acid loop, but only NPR-A possesses the second 49 amino acid loop in common with NPR-C.
7727388	5	60	theme	juxtamembrane	863:875	arg1	C431					895:898	C431	895:898	C431	895:898	The juxtamembrane residues C428 and C431 are involved in homodimer formation, confirmed by site-directed mutagenesis of full-length NPR.
7727388	5	60	theme	juxtamembrane	863:875	arg1	C428					886:889	C428	886:889	C428	886:889	The juxtamembrane residues C428 and C431 are involved in homodimer formation, confirmed by site-directed mutagenesis of full-length NPR.
7727388	5	60	theme	juxtamembrane	863:875	arg1	residues					877:884	The juxtamembrane residues C428 and C431	859:898	The juxtamembrane residues C428 and C431	859:898	The juxtamembrane residues C428 and C431 are involved in homodimer formation, confirmed by site-directed mutagenesis of full-length NPR.
7727388	6	61	dep	complex	1115:1121	arg1	occupancy					1132:1140	partial occupancy	1124:1140	complex; partial occupancy	1115:1140	Three of the four potential Asn-linked glycosylation sites are occupied: N41 (complex), N248 (high mannose), and N349 (complex; partial occupancy).
7727388	2	62	theme	subunit	294:300	arg1	weight					312:317	a subunit molecular weight	292:317	a subunit molecular weight of 68,000	292:327	This cell surface glycoprotein is a disulfide-linked homodimer with a subunit molecular weight of 68,000.
7727388	1	63	theme	natriuretic	181:191	arg1	sites					209:213	the natriuretic peptide binding sites	177:213	the natriuretic peptide binding sites in vivo	177:221	The natriuretic peptide receptor-C (NPR-C) constitutes greater than 95% of the natriuretic peptide binding sites in vivo.
7727388	3	64	theme	protein	566:572	arg1	cleavage					532:539	papain cleavage	525:539	papain cleavage of a receptor-IgG fusion protein expressed in Chinese hamster ovary cells, and a baculovirus/Sf9-expressed cytoplasmic truncation mutant in which 34 of 37 cytoplasmic domain amino acids were deleted	525:738	Two sources and types of ANP affinity-purified human NPR-C were used to map disulfide linkages and glycosylation sites of this receptor by mass spectrometry: the extracellular domain obtained by papain cleavage of a receptor-IgG fusion protein expressed in Chinese hamster ovary cells, and a baculovirus/Sf9-expressed cytoplasmic truncation mutant in which 34 of 37 cytoplasmic domain amino acids were deleted.
7727388	7	65	theme	first	1344:1348	arg1	loop					1379:1382	the first amino-terminal 29 amino acid loop	1340:1382	the first amino-terminal 29 amino acid loop	1340:1382	These data describe the intra- and intermolecular linkages in NPR-C, providing a model for the homologous guanylyl cyclase receptors, NPR-A and NPR-B; both of the cyclase receptors likely contain the first amino-terminal 29 amino acid loop, but only NPR-A possesses the second 49 amino acid loop in common with NPR-C.
7727388	3	66	theme	Chinese	587:593	arg1	cells					609:613	Chinese hamster ovary cells	587:613	Chinese hamster ovary cells	587:613	Two sources and types of ANP affinity-purified human NPR-C were used to map disulfide linkages and glycosylation sites of this receptor by mass spectrometry: the extracellular domain obtained by papain cleavage of a receptor-IgG fusion protein expressed in Chinese hamster ovary cells, and a baculovirus/Sf9-expressed cytoplasmic truncation mutant in which 34 of 37 cytoplasmic domain amino acids were deleted.
7727388	1	67	theme	binding	201:207	arg1	sites					209:213	the natriuretic peptide binding sites	177:213	the natriuretic peptide binding sites in vivo	177:221	The natriuretic peptide receptor-C (NPR-C) constitutes greater than 95% of the natriuretic peptide binding sites in vivo.
7727388	1	68	dep	in	215:216	arg1	vivo					218:221	vivo	218:221	vivo	218:221	The natriuretic peptide receptor-C (NPR-C) constitutes greater than 95% of the natriuretic peptide binding sites in vivo.
7727388	7	69	contain	possesses	1400:1408	arg1	NPR-A					1394:1398	only NPR-A	1389:1398	only NPR-A	1389:1398	These data describe the intra- and intermolecular linkages in NPR-C, providing a model for the homologous guanylyl cyclase receptors, NPR-A and NPR-B; both of the cyclase receptors likely contain the first amino-terminal 29 amino acid loop, but only NPR-A possesses the second 49 amino acid loop in common with NPR-C.
7727388	7	69	contain	possesses	1400:1408	arg2	loop					1435:1438	the second 49 amino acid loop	1410:1438	the second 49 amino acid loop in common with NPR-C	1410:1459	These data describe the intra- and intermolecular linkages in NPR-C, providing a model for the homologous guanylyl cyclase receptors, NPR-A and NPR-B; both of the cyclase receptors likely contain the first amino-terminal 29 amino acid loop, but only NPR-A possesses the second 49 amino acid loop in common with NPR-C.
7727388	6	70	theme	glycosylation	1035:1047	arg1	sites					1049:1053	the four potential Asn-linked glycosylation sites	1005:1053	the four potential Asn-linked glycosylation sites	1005:1053	Three of the four potential Asn-linked glycosylation sites are occupied: N41 (complex), N248 (high mannose), and N349 (complex; partial occupancy).
7727388	0	71	theme	natriuretic	60:70	arg1	homodimer					91:99	the human natriuretic peptide receptor-C homodimer	50:99	the human natriuretic peptide receptor-C homodimer	50:99	The disulfide linkages and glycosylation sites of the human natriuretic peptide receptor-C homodimer.
7727388	3	72	theme	ovary	603:607	arg1	cells					609:613	Chinese hamster ovary cells	587:613	Chinese hamster ovary cells	587:613	Two sources and types of ANP affinity-purified human NPR-C were used to map disulfide linkages and glycosylation sites of this receptor by mass spectrometry: the extracellular domain obtained by papain cleavage of a receptor-IgG fusion protein expressed in Chinese hamster ovary cells, and a baculovirus/Sf9-expressed cytoplasmic truncation mutant in which 34 of 37 cytoplasmic domain amino acids were deleted.
7727388	6	73	theme	potential	1014:1022	arg1	sites					1049:1053	the four potential Asn-linked glycosylation sites	1005:1053	the four potential Asn-linked glycosylation sites	1005:1053	Three of the four potential Asn-linked glycosylation sites are occupied: N41 (complex), N248 (high mannose), and N349 (complex; partial occupancy).
7727388	0	74	theme	receptor-C	80:89	arg1	homodimer					91:99	the human natriuretic peptide receptor-C homodimer	50:99	the human natriuretic peptide receptor-C homodimer	50:99	The disulfide linkages and glycosylation sites of the human natriuretic peptide receptor-C homodimer.
7727388	4	75	theme	bonded	770:775	arg1	loops					777:781	Two intramolecular disulfide bonded loops	741:781	Two intramolecular disulfide bonded loops	741:781	Two intramolecular disulfide bonded loops were found in the 435 amino acid extracellular domain (C63-C91, C168-C216).
7727388	4	76	dep	domain	830:835	arg1	C168-C216					847:855	C168-C216	847:855	C168-C216	847:855	Two intramolecular disulfide bonded loops were found in the 435 amino acid extracellular domain (C63-C91, C168-C216).
7727388	4	76	dep	domain	830:835	arg1	C63-C91					838:844	C63-C91	838:844	C63-C91	838:844	Two intramolecular disulfide bonded loops were found in the 435 amino acid extracellular domain (C63-C91, C168-C216).
7727388	5	77	theme	full-length	979:989	arg1	NPR					991:993	full-length NPR	979:993	full-length NPR	979:993	The juxtamembrane residues C428 and C431 are involved in homodimer formation, confirmed by site-directed mutagenesis of full-length NPR.
7727388	5	78	theme	homodimer	916:924	arg1	formation					926:934	homodimer formation	916:934	homodimer formation	916:934	The juxtamembrane residues C428 and C431 are involved in homodimer formation, confirmed by site-directed mutagenesis of full-length NPR.
7727388	6	79	dep	occupied	1059:1066	arg1	mannose					1095:1101	high mannose	1090:1101	high mannose	1090:1101	Three of the four potential Asn-linked glycosylation sites are occupied: N41 (complex), N248 (high mannose), and N349 (complex; partial occupancy).
7727388	6	79	dep	occupied	1059:1066	arg1	N349					1109:1112	N349	1109:1112	N349	1109:1112	Three of the four potential Asn-linked glycosylation sites are occupied: N41 (complex), N248 (high mannose), and N349 (complex; partial occupancy).
7727388	6	79	dep	occupied	1059:1066	arg1	complex					1074:1080	complex	1074:1080	complex	1074:1080	Three of the four potential Asn-linked glycosylation sites are occupied: N41 (complex), N248 (high mannose), and N349 (complex; partial occupancy).
7727388	6	79	dep	occupied	1059:1066	arg1	N248					1084:1087	N248	1084:1087	N248	1084:1087	Three of the four potential Asn-linked glycosylation sites are occupied: N41 (complex), N248 (high mannose), and N349 (complex; partial occupancy).
7727388	6	79	dep	occupied	1059:1066	arg1	N41					1069:1071	N41	1069:1071	N41	1069:1071	Three of the four potential Asn-linked glycosylation sites are occupied: N41 (complex), N248 (high mannose), and N349 (complex; partial occupancy).
7727388	3	80	theme	glycosylation	429:441	arg1	sites					443:447	glycosylation sites	429:447	glycosylation sites	429:447	Two sources and types of ANP affinity-purified human NPR-C were used to map disulfide linkages and glycosylation sites of this receptor by mass spectrometry: the extracellular domain obtained by papain cleavage of a receptor-IgG fusion protein expressed in Chinese hamster ovary cells, and a baculovirus/Sf9-expressed cytoplasmic truncation mutant in which 34 of 37 cytoplasmic domain amino acids were deleted.
7727388	3	80	theme	glycosylation	429:441	arg1	receptor					457:464	this receptor	452:464	this receptor	452:464	Two sources and types of ANP affinity-purified human NPR-C were used to map disulfide linkages and glycosylation sites of this receptor by mass spectrometry: the extracellular domain obtained by papain cleavage of a receptor-IgG fusion protein expressed in Chinese hamster ovary cells, and a baculovirus/Sf9-expressed cytoplasmic truncation mutant in which 34 of 37 cytoplasmic domain amino acids were deleted.
7727388	0	81	theme	disulfide	4:12	arg1	linkages					14:21	disulfide linkages	4:21	disulfide linkages	4:21	The disulfide linkages and glycosylation sites of the human natriuretic peptide receptor-C homodimer.
7727388	3	82	theme	NPR-C	383:387	arg1	types					346:350	types	346:350	types	346:350	Two sources and types of ANP affinity-purified human NPR-C were used to map disulfide linkages and glycosylation sites of this receptor by mass spectrometry: the extracellular domain obtained by papain cleavage of a receptor-IgG fusion protein expressed in Chinese hamster ovary cells, and a baculovirus/Sf9-expressed cytoplasmic truncation mutant in which 34 of 37 cytoplasmic domain amino acids were deleted.
7727388	3	82	theme	NPR-C	383:387	arg1	sources					334:340	Two sources	330:340	Two sources	330:340	Two sources and types of ANP affinity-purified human NPR-C were used to map disulfide linkages and glycosylation sites of this receptor by mass spectrometry: the extracellular domain obtained by papain cleavage of a receptor-IgG fusion protein expressed in Chinese hamster ovary cells, and a baculovirus/Sf9-expressed cytoplasmic truncation mutant in which 34 of 37 cytoplasmic domain amino acids were deleted.
7727388	7	83	theme	cyclase	1259:1265	arg1	NPR-A					1278:1282	NPR-A	1278:1282	NPR-A	1278:1282	These data describe the intra- and intermolecular linkages in NPR-C, providing a model for the homologous guanylyl cyclase receptors, NPR-A and NPR-B; both of the cyclase receptors likely contain the first amino-terminal 29 amino acid loop, but only NPR-A possesses the second 49 amino acid loop in common with NPR-C.
7727388	7	83	theme	cyclase	1259:1265	arg1	receptors					1267:1275	the homologous guanylyl cyclase receptors	1235:1275	the homologous guanylyl cyclase receptors	1235:1275	These data describe the intra- and intermolecular linkages in NPR-C, providing a model for the homologous guanylyl cyclase receptors, NPR-A and NPR-B; both of the cyclase receptors likely contain the first amino-terminal 29 amino acid loop, but only NPR-A possesses the second 49 amino acid loop in common with NPR-C.
7727388	7	83	theme	cyclase	1259:1265	arg1	NPR-B					1288:1292	NPR-B	1288:1292	NPR-B	1288:1292	These data describe the intra- and intermolecular linkages in NPR-C, providing a model for the homologous guanylyl cyclase receptors, NPR-A and NPR-B; both of the cyclase receptors likely contain the first amino-terminal 29 amino acid loop, but only NPR-A possesses the second 49 amino acid loop in common with NPR-C.
7727388	3	84	theme	affinity-purified	359:375	arg1	NPR-C					383:387	ANP affinity-purified human NPR-C	355:387	ANP affinity-purified human NPR-C	355:387	Two sources and types of ANP affinity-purified human NPR-C were used to map disulfide linkages and glycosylation sites of this receptor by mass spectrometry: the extracellular domain obtained by papain cleavage of a receptor-IgG fusion protein expressed in Chinese hamster ovary cells, and a baculovirus/Sf9-expressed cytoplasmic truncation mutant in which 34 of 37 cytoplasmic domain amino acids were deleted.
7727388	3	85	theme	cytoplasmic	648:658	arg1	mutant					671:676	a baculovirus/Sf9-expressed cytoplasmic truncation mutant	620:676	a baculovirus/Sf9-expressed cytoplasmic truncation mutant in which 34 of 37 cytoplasmic domain amino acids were deleted	620:738	Two sources and types of ANP affinity-purified human NPR-C were used to map disulfide linkages and glycosylation sites of this receptor by mass spectrometry: the extracellular domain obtained by papain cleavage of a receptor-IgG fusion protein expressed in Chinese hamster ovary cells, and a baculovirus/Sf9-expressed cytoplasmic truncation mutant in which 34 of 37 cytoplasmic domain amino acids were deleted.
7727388	4	86	theme	intramolecular	745:758	arg1	loops					777:781	Two intramolecular disulfide bonded loops	741:781	Two intramolecular disulfide bonded loops	741:781	Two intramolecular disulfide bonded loops were found in the 435 amino acid extracellular domain (C63-C91, C168-C216).
7727388	3	87	theme	receptor	457:464	arg1	linkages					416:423	disulfide linkages	406:423	disulfide linkages	406:423	Two sources and types of ANP affinity-purified human NPR-C were used to map disulfide linkages and glycosylation sites of this receptor by mass spectrometry: the extracellular domain obtained by papain cleavage of a receptor-IgG fusion protein expressed in Chinese hamster ovary cells, and a baculovirus/Sf9-expressed cytoplasmic truncation mutant in which 34 of 37 cytoplasmic domain amino acids were deleted.
7727388	3	87	theme	receptor	457:464	arg1	sites					443:447	glycosylation sites	429:447	glycosylation sites	429:447	Two sources and types of ANP affinity-purified human NPR-C were used to map disulfide linkages and glycosylation sites of this receptor by mass spectrometry: the extracellular domain obtained by papain cleavage of a receptor-IgG fusion protein expressed in Chinese hamster ovary cells, and a baculovirus/Sf9-expressed cytoplasmic truncation mutant in which 34 of 37 cytoplasmic domain amino acids were deleted.
7727388	3	87	theme	receptor	457:464	arg1	receptor					457:464	this receptor	452:464	this receptor	452:464	Two sources and types of ANP affinity-purified human NPR-C were used to map disulfide linkages and glycosylation sites of this receptor by mass spectrometry: the extracellular domain obtained by papain cleavage of a receptor-IgG fusion protein expressed in Chinese hamster ovary cells, and a baculovirus/Sf9-expressed cytoplasmic truncation mutant in which 34 of 37 cytoplasmic domain amino acids were deleted.
7727388	7	88	theme	homologous	1239:1248	arg1	cyclase					1259:1265	homologous guanylyl cyclase	1239:1265	the homologous guanylyl cyclase receptors	1235:1275	These data describe the intra- and intermolecular linkages in NPR-C, providing a model for the homologous guanylyl cyclase receptors, NPR-A and NPR-B; both of the cyclase receptors likely contain the first amino-terminal 29 amino acid loop, but only NPR-A possesses the second 49 amino acid loop in common with NPR-C.
7727388	5	89	dep	residues	877:884	arg1	C431					895:898	C431	895:898	C431	895:898	The juxtamembrane residues C428 and C431 are involved in homodimer formation, confirmed by site-directed mutagenesis of full-length NPR.
7727388	5	89	dep	residues	877:884	arg1	C428					886:889	C428	886:889	C428	886:889	The juxtamembrane residues C428 and C431 are involved in homodimer formation, confirmed by site-directed mutagenesis of full-length NPR.
7727388	5	89	dep	residues	877:884	arg1	residues					877:884	The juxtamembrane residues C428 and C431	859:898	The juxtamembrane residues C428 and C431	859:898	The juxtamembrane residues C428 and C431 are involved in homodimer formation, confirmed by site-directed mutagenesis of full-length NPR.
7727388	3	90	used	used	394:397	arg2	types					346:350	types	346:350	types	346:350	Two sources and types of ANP affinity-purified human NPR-C were used to map disulfide linkages and glycosylation sites of this receptor by mass spectrometry: the extracellular domain obtained by papain cleavage of a receptor-IgG fusion protein expressed in Chinese hamster ovary cells, and a baculovirus/Sf9-expressed cytoplasmic truncation mutant in which 34 of 37 cytoplasmic domain amino acids were deleted.
7727388	3	90	used	used	394:397	arg2	sources					334:340	Two sources	330:340	Two sources	330:340	Two sources and types of ANP affinity-purified human NPR-C were used to map disulfide linkages and glycosylation sites of this receptor by mass spectrometry: the extracellular domain obtained by papain cleavage of a receptor-IgG fusion protein expressed in Chinese hamster ovary cells, and a baculovirus/Sf9-expressed cytoplasmic truncation mutant in which 34 of 37 cytoplasmic domain amino acids were deleted.
7727388	0	91	gly	glycosylation	27:39	arg2	sites					41:45	glycosylation sites	27:45	glycosylation sites	27:45	The disulfide linkages and glycosylation sites of the human natriuretic peptide receptor-C homodimer.
7727388	0	91	gly	glycosylation	27:39	arg2	homodimer					91:99	the human natriuretic peptide receptor-C homodimer	50:99	the human natriuretic peptide receptor-C homodimer	50:99	The disulfide linkages and glycosylation sites of the human natriuretic peptide receptor-C homodimer.
7727388	0	91	gly	glycosylation	27:39	arg1	homodimer					91:99	the human natriuretic peptide receptor-C homodimer	50:99	the human natriuretic peptide receptor-C homodimer	50:99	The disulfide linkages and glycosylation sites of the human natriuretic peptide receptor-C homodimer.
7727388	3	92	theme	mass	469:472	arg1	spectrometry					474:485	mass spectrometry	469:485	mass spectrometry	469:485	Two sources and types of ANP affinity-purified human NPR-C were used to map disulfide linkages and glycosylation sites of this receptor by mass spectrometry: the extracellular domain obtained by papain cleavage of a receptor-IgG fusion protein expressed in Chinese hamster ovary cells, and a baculovirus/Sf9-expressed cytoplasmic truncation mutant in which 34 of 37 cytoplasmic domain amino acids were deleted.
7727388	6	93	theme	high	1090:1093	arg1	N248					1084:1087	N248	1084:1087	N248	1084:1087	Three of the four potential Asn-linked glycosylation sites are occupied: N41 (complex), N248 (high mannose), and N349 (complex; partial occupancy).
7727388	6	93	theme	high	1090:1093	arg1	mannose					1095:1101	high mannose	1090:1101	high mannose	1090:1101	Three of the four potential Asn-linked glycosylation sites are occupied: N41 (complex), N248 (high mannose), and N349 (complex; partial occupancy).
7727388	3	94	theme	cytoplasmic	696:706	arg1	acids					721:725	37 cytoplasmic domain amino acids	693:725	37 cytoplasmic domain amino acids	693:725	Two sources and types of ANP affinity-purified human NPR-C were used to map disulfide linkages and glycosylation sites of this receptor by mass spectrometry: the extracellular domain obtained by papain cleavage of a receptor-IgG fusion protein expressed in Chinese hamster ovary cells, and a baculovirus/Sf9-expressed cytoplasmic truncation mutant in which 34 of 37 cytoplasmic domain amino acids were deleted.
8068684	6	0	theme	N-glycosylation	1129:1143	arg1	site					1145:1148	only the first N-glycosylation site	1114:1148	only the first N-glycosylation site (Asn 75)	1114:1157	Immunoblot analysis of the expressed proteins with and without N-glycosidase F treatment showed that only the first N-glycosylation site (Asn 75) is utilized.
8068684	6	0	theme	N-glycosylation	1129:1143	arg1	Asn					1151:1153	Asn 75	1151:1156	Asn 75	1151:1156	Immunoblot analysis of the expressed proteins with and without N-glycosidase F treatment showed that only the first N-glycosylation site (Asn 75) is utilized.
8068684	1	1	theme	ubiquitously-expressed	128:149	arg1	exchanger					163:171	The ubiquitously-expressed human Na+H+ exchanger	124:171	The ubiquitously-expressed human Na+H+ exchanger (NHE-1)	124:179	The ubiquitously-expressed human Na+H+ exchanger (NHE-1) contains three consensus sites (Asn-X-Ser/Thr) for N-linked glycosylation at asparagines 75, 370, and 410.
8068684	1	1	theme	ubiquitously-expressed	128:149	arg1	NHE-1					174:178	NHE-1	174:178	NHE-1	174:178	The ubiquitously-expressed human Na+H+ exchanger (NHE-1) contains three consensus sites (Asn-X-Ser/Thr) for N-linked glycosylation at asparagines 75, 370, and 410.
8068684	0	2	contain	possesses	27:35	arg2	glycosylation					53:65	N- and O-linked glycosylation	37:65	N- and O-linked glycosylation restricted to the first N-terminal extracellular domain	37:121	The Na+/H+ exchanger NHE-1 possesses N- and O-linked glycosylation restricted to the first N-terminal extracellular domain.
8068684	0	2	contain	possesses	27:35	arg1	NHE-1					21:25	The Na+/H+ exchanger NHE-1	0:25	The Na+/H+ exchanger NHE-1	0:25	The Na+/H+ exchanger NHE-1 possesses N- and O-linked glycosylation restricted to the first N-terminal extracellular domain.
8068684	3	3	theme	individual	548:557	arg1	Asp					599:601	Asn to Asp	592:601	Asn to Asp	592:601	In order to determine unambiguously the sites of glycosylation and their role in biosynthesis and cation transport, site-directed mutagenesis at the individual potential N-glycosylation sites (Asn to Asp) was performed and all possible double and triple mutants were constructed.
8068684	3	3	theme	individual	548:557	arg1	sites					585:589	the individual potential N-glycosylation sites	544:589	the individual potential N-glycosylation sites (Asn to Asp)	544:602	In order to determine unambiguously the sites of glycosylation and their role in biosynthesis and cation transport, site-directed mutagenesis at the individual potential N-glycosylation sites (Asn to Asp) was performed and all possible double and triple mutants were constructed.
8068684	6	4	used	utilized	1162:1169	arg2	Asn					1151:1153	Asn 75	1151:1156	Asn 75	1151:1156	Immunoblot analysis of the expressed proteins with and without N-glycosidase F treatment showed that only the first N-glycosylation site (Asn 75) is utilized.
8068684	6	4	used	utilized	1162:1169	arg2	site					1145:1148	only the first N-glycosylation site	1114:1148	only the first N-glycosylation site (Asn 75)	1114:1157	Immunoblot analysis of the expressed proteins with and without N-glycosidase F treatment showed that only the first N-glycosylation site (Asn 75) is utilized.
8068684	4	5	theme	intracellular	844:856	arg1	acidification					858:870	acute intracellular acidification	838:870	acute intracellular acidification	838:870	The mutated DNAs were expressed in PS120 hamster fibroblasts lacking endogenous exchanger, and the transfected cells were selected by their ability to survive acute intracellular acidification.
8068684	8	6	with	forms	1309:1313	arg1	mass					1382:1385	a molecular mass	1370:1385	a molecular mass of 110,000 Da which contains N-linked and O-linked oligosaccharide and is expressed at the cell surface	1370:1489	Two forms of NHE-1 was consistently observed, a mature form with a molecular mass of 110,000 Da which contains N-linked and O-linked oligosaccharide and is expressed at the cell surface, and a lower molecular mass form (85,000 Da) present in the endoplasmic reticulum which only contains N-linked high-mannose oligosaccharide.
8068684	3	7	from	role	472:475	arg1	biosynthesis					480:491	biosynthesis	480:491	biosynthesis	480:491	In order to determine unambiguously the sites of glycosylation and their role in biosynthesis and cation transport, site-directed mutagenesis at the individual potential N-glycosylation sites (Asn to Asp) was performed and all possible double and triple mutants were constructed.
8068684	3	7	from	role	472:475	arg1	transport					504:512	cation transport	497:512	cation transport	497:512	In order to determine unambiguously the sites of glycosylation and their role in biosynthesis and cation transport, site-directed mutagenesis at the individual potential N-glycosylation sites (Asn to Asp) was performed and all possible double and triple mutants were constructed.
8068684	9	8	theme	N-linked	1711:1718	arg1	site					1743:1746	the N75 N-linked putative glycosylation site	1703:1746	the N75 N-linked putative glycosylation site	1703:1746	NHE-3, an apically-expressed epithelial isoform which does not possess the N75 N-linked putative glycosylation site and any extracellular loops enriched in serine and threonine residues, does not exhibit any detectable glycosylation.
8068684	3	9	from	biosynthesis	480:491	arg1	glycosylation					448:460	glycosylation	448:460	glycosylation	448:460	In order to determine unambiguously the sites of glycosylation and their role in biosynthesis and cation transport, site-directed mutagenesis at the individual potential N-glycosylation sites (Asn to Asp) was performed and all possible double and triple mutants were constructed.
8068684	3	9	from	biosynthesis	480:491	arg1	role					472:475	their role	466:475	their role in biosynthesis and cation transport	466:512	In order to determine unambiguously the sites of glycosylation and their role in biosynthesis and cation transport, site-directed mutagenesis at the individual potential N-glycosylation sites (Asn to Asp) was performed and all possible double and triple mutants were constructed.
8068684	3	9	from	biosynthesis	480:491	arg1	sites					439:443	the sites	435:443	the sites of glycosylation and their role in biosynthesis and cation transport	435:512	In order to determine unambiguously the sites of glycosylation and their role in biosynthesis and cation transport, site-directed mutagenesis at the individual potential N-glycosylation sites (Asn to Asp) was performed and all possible double and triple mutants were constructed.
8068684	2	10	theme	extracellular	298:310	arg1	rich					320:323	rich	320:323	rich	320:323	The first extracellular loop is rich in serine and threonine residues which may contain O-linked carbohydrate.
8068684	2	10	theme	extracellular	298:310	arg1	loop					312:315	The first extracellular loop	288:315	The first extracellular loop	288:315	The first extracellular loop is rich in serine and threonine residues which may contain O-linked carbohydrate.
8068684	1	11	theme	consensus	196:204	arg1	sites					206:210	three consensus sites	190:210	three consensus sites (Asn-X-Ser/Thr) for N-linked glycosylation at asparagines 75, 370, and 410	190:285	The ubiquitously-expressed human Na+H+ exchanger (NHE-1) contains three consensus sites (Asn-X-Ser/Thr) for N-linked glycosylation at asparagines 75, 370, and 410.
8068684	9	12	theme	glycosylation	1729:1741	arg1	site					1743:1746	the N75 N-linked putative glycosylation site	1703:1746	the N75 N-linked putative glycosylation site	1703:1746	NHE-3, an apically-expressed epithelial isoform which does not possess the N75 N-linked putative glycosylation site and any extracellular loops enriched in serine and threonine residues, does not exhibit any detectable glycosylation.
8068684	3	13	theme	N-glycosylation	569:583	arg1	Asp					599:601	Asn to Asp	592:601	Asn to Asp	592:601	In order to determine unambiguously the sites of glycosylation and their role in biosynthesis and cation transport, site-directed mutagenesis at the individual potential N-glycosylation sites (Asn to Asp) was performed and all possible double and triple mutants were constructed.
8068684	3	13	theme	N-glycosylation	569:583	arg1	sites					585:589	the individual potential N-glycosylation sites	544:589	the individual potential N-glycosylation sites (Asn to Asp)	544:602	In order to determine unambiguously the sites of glycosylation and their role in biosynthesis and cation transport, site-directed mutagenesis at the individual potential N-glycosylation sites (Asn to Asp) was performed and all possible double and triple mutants were constructed.
8068684	8	14	attach	present	1536:1542	arg1	reticulum					1563:1571	the endoplasmic reticulum	1547:1571	the endoplasmic reticulum which only contains N-linked high-mannose oligosaccharide	1547:1629	Two forms of NHE-1 was consistently observed, a mature form with a molecular mass of 110,000 Da which contains N-linked and O-linked oligosaccharide and is expressed at the cell surface, and a lower molecular mass form (85,000 Da) present in the endoplasmic reticulum which only contains N-linked high-mannose oligosaccharide.
8068684	8	14	attach	present	1536:1542	arg2	forms					1309:1313	Two forms	1305:1313	Two forms of NHE-1 was consistently observed	1305:1348	Two forms of NHE-1 was consistently observed, a mature form with a molecular mass of 110,000 Da which contains N-linked and O-linked oligosaccharide and is expressed at the cell surface, and a lower molecular mass form (85,000 Da) present in the endoplasmic reticulum which only contains N-linked high-mannose oligosaccharide.
8068684	8	14	attach	present	1536:1542	arg2	form					1360:1363	a mature form	1351:1363	a mature form with a molecular mass of 110,000 Da which contains N-linked and O-linked oligosaccharide and is expressed at the cell surface	1351:1489	Two forms of NHE-1 was consistently observed, a mature form with a molecular mass of 110,000 Da which contains N-linked and O-linked oligosaccharide and is expressed at the cell surface, and a lower molecular mass form (85,000 Da) present in the endoplasmic reticulum which only contains N-linked high-mannose oligosaccharide.
8068684	8	14	attach	present	1536:1542	arg2	Da					1532:1533	85,000 Da	1525:1533	85,000 Da	1525:1533	Two forms of NHE-1 was consistently observed, a mature form with a molecular mass of 110,000 Da which contains N-linked and O-linked oligosaccharide and is expressed at the cell surface, and a lower molecular mass form (85,000 Da) present in the endoplasmic reticulum which only contains N-linked high-mannose oligosaccharide.
8068684	8	14	attach	present	1536:1542	arg2	form					1519:1522	a lower molecular mass form	1496:1522	a lower molecular mass form (85,000 Da)	1496:1534	Two forms of NHE-1 was consistently observed, a mature form with a molecular mass of 110,000 Da which contains N-linked and O-linked oligosaccharide and is expressed at the cell surface, and a lower molecular mass form (85,000 Da) present in the endoplasmic reticulum which only contains N-linked high-mannose oligosaccharide.
8068684	9	15	theme	extracellular	1756:1768	arg1	loops					1770:1774	any extracellular loops	1752:1774	any extracellular loops enriched in serine and threonine residues	1752:1816	NHE-3, an apically-expressed epithelial isoform which does not possess the N75 N-linked putative glycosylation site and any extracellular loops enriched in serine and threonine residues, does not exhibit any detectable glycosylation.
8068684	8	16	contain	contains	1584:1591	arg1	reticulum					1563:1571	the endoplasmic reticulum	1547:1571	the endoplasmic reticulum which only contains N-linked high-mannose oligosaccharide	1547:1629	Two forms of NHE-1 was consistently observed, a mature form with a molecular mass of 110,000 Da which contains N-linked and O-linked oligosaccharide and is expressed at the cell surface, and a lower molecular mass form (85,000 Da) present in the endoplasmic reticulum which only contains N-linked high-mannose oligosaccharide.
8068684	8	16	contain	contains	1584:1591	arg2	oligosaccharide					1615:1629	N-linked high-mannose oligosaccharide	1593:1629	N-linked high-mannose oligosaccharide	1593:1629	Two forms of NHE-1 was consistently observed, a mature form with a molecular mass of 110,000 Da which contains N-linked and O-linked oligosaccharide and is expressed at the cell surface, and a lower molecular mass form (85,000 Da) present in the endoplasmic reticulum which only contains N-linked high-mannose oligosaccharide.
8068684	3	17	gly	N-glycosylation	569:583	arg2	sites					585:589	the individual potential N-glycosylation sites	544:589	the individual potential N-glycosylation sites (Asn to Asp)	544:602	In order to determine unambiguously the sites of glycosylation and their role in biosynthesis and cation transport, site-directed mutagenesis at the individual potential N-glycosylation sites (Asn to Asp) was performed and all possible double and triple mutants were constructed.
8068684	3	17	gly	N-glycosylation	569:583	arg2	Asp					599:601	Asn to Asp	592:601	Asn to Asp	592:601	In order to determine unambiguously the sites of glycosylation and their role in biosynthesis and cation transport, site-directed mutagenesis at the individual potential N-glycosylation sites (Asn to Asp) was performed and all possible double and triple mutants were constructed.
8068684	1	18	theme	human	151:155	arg1	exchanger					163:171	The ubiquitously-expressed human Na+H+ exchanger	124:171	The ubiquitously-expressed human Na+H+ exchanger (NHE-1)	124:179	The ubiquitously-expressed human Na+H+ exchanger (NHE-1) contains three consensus sites (Asn-X-Ser/Thr) for N-linked glycosylation at asparagines 75, 370, and 410.
8068684	1	18	theme	human	151:155	arg1	NHE-1					174:178	NHE-1	174:178	NHE-1	174:178	The ubiquitously-expressed human Na+H+ exchanger (NHE-1) contains three consensus sites (Asn-X-Ser/Thr) for N-linked glycosylation at asparagines 75, 370, and 410.
8068684	8	19	link	O-linked	1429:1436	arg1	oligosaccharide					1438:1452	N-linked and O-linked oligosaccharide	1416:1452	N-linked and O-linked oligosaccharide	1416:1452	Two forms of NHE-1 was consistently observed, a mature form with a molecular mass of 110,000 Da which contains N-linked and O-linked oligosaccharide and is expressed at the cell surface, and a lower molecular mass form (85,000 Da) present in the endoplasmic reticulum which only contains N-linked high-mannose oligosaccharide.
8068684	8	20	theme	lower	1498:1502	arg1	mass					1514:1517	lower molecular mass	1498:1517	a lower molecular mass form (85,000 Da)	1496:1534	Two forms of NHE-1 was consistently observed, a mature form with a molecular mass of 110,000 Da which contains N-linked and O-linked oligosaccharide and is expressed at the cell surface, and a lower molecular mass form (85,000 Da) present in the endoplasmic reticulum which only contains N-linked high-mannose oligosaccharide.
8068684	5	21	contain	had	924:926	arg2	profiles					964:971	pharmacological profiles	948:971	pharmacological profiles that were similar to that of wild-type	948:1010	All constructs produced functional exchangers that had transport rates and pharmacological profiles that were similar to that of wild-type.
8068684	5	21	contain	had	924:926	arg1	exchangers					908:917	functional exchangers	897:917	functional exchangers that had transport rates and pharmacological profiles that were similar to that of wild-type	897:1010	All constructs produced functional exchangers that had transport rates and pharmacological profiles that were similar to that of wild-type.
8068684	5	21	contain	had	924:926	arg2	rates					938:942	transport rates	928:942	transport rates	928:942	All constructs produced functional exchangers that had transport rates and pharmacological profiles that were similar to that of wild-type.
8068684	4	22	theme	mutated	683:689	arg1	DNAs					691:694	The mutated DNAs	679:694	The mutated DNAs	679:694	The mutated DNAs were expressed in PS120 hamster fibroblasts lacking endogenous exchanger, and the transfected cells were selected by their ability to survive acute intracellular acidification.
8068684	8	23	link	N-linked	1416:1423	arg1	oligosaccharide					1438:1452	N-linked and O-linked oligosaccharide	1416:1452	N-linked and O-linked oligosaccharide	1416:1452	Two forms of NHE-1 was consistently observed, a mature form with a molecular mass of 110,000 Da which contains N-linked and O-linked oligosaccharide and is expressed at the cell surface, and a lower molecular mass form (85,000 Da) present in the endoplasmic reticulum which only contains N-linked high-mannose oligosaccharide.
8068684	8	24	theme	mass	1514:1517	arg1	form					1519:1522	a lower molecular mass form	1496:1522	a lower molecular mass form (85,000 Da)	1496:1534	Two forms of NHE-1 was consistently observed, a mature form with a molecular mass of 110,000 Da which contains N-linked and O-linked oligosaccharide and is expressed at the cell surface, and a lower molecular mass form (85,000 Da) present in the endoplasmic reticulum which only contains N-linked high-mannose oligosaccharide.
8068684	8	24	theme	mass	1514:1517	arg1	Da					1532:1533	85,000 Da	1525:1533	85,000 Da	1525:1533	Two forms of NHE-1 was consistently observed, a mature form with a molecular mass of 110,000 Da which contains N-linked and O-linked oligosaccharide and is expressed at the cell surface, and a lower molecular mass form (85,000 Da) present in the endoplasmic reticulum which only contains N-linked high-mannose oligosaccharide.
8068684	5	25	theme	transport	928:936	arg1	rates					938:942	transport rates	928:942	transport rates	928:942	All constructs produced functional exchangers that had transport rates and pharmacological profiles that were similar to that of wild-type.
8068684	8	26	theme	molecular	1372:1380	arg1	mass					1382:1385	a molecular mass	1370:1385	a molecular mass of 110,000 Da which contains N-linked and O-linked oligosaccharide and is expressed at the cell surface	1370:1489	Two forms of NHE-1 was consistently observed, a mature form with a molecular mass of 110,000 Da which contains N-linked and O-linked oligosaccharide and is expressed at the cell surface, and a lower molecular mass form (85,000 Da) present in the endoplasmic reticulum which only contains N-linked high-mannose oligosaccharide.
8068684	0	27	theme	first	85:89	arg1	domain					116:121	the first N-terminal extracellular domain	81:121	the first N-terminal extracellular domain	81:121	The Na+/H+ exchanger NHE-1 possesses N- and O-linked glycosylation restricted to the first N-terminal extracellular domain.
8068684	7	28	theme	O-linked	1279:1286	arg1	oligosaccharide					1288:1302	O-linked oligosaccharide	1279:1302	O-linked oligosaccharide	1279:1302	In addition, treatment of NHE-1 with neuraminidase and O-glycosidase demonstrated that NHE-1 also contains O-linked oligosaccharide.
8068684	4	29	theme	hamster	720:726	arg1	fibroblasts					728:738	PS120 hamster fibroblasts	714:738	PS120 hamster fibroblasts lacking endogenous exchanger	714:767	The mutated DNAs were expressed in PS120 hamster fibroblasts lacking endogenous exchanger, and the transfected cells were selected by their ability to survive acute intracellular acidification.
8068684	6	30	theme	Immunoblot	1013:1022	arg1	analysis					1024:1031	Immunoblot analysis	1013:1031	Immunoblot analysis of the expressed proteins with and without N-glycosidase F treatment	1013:1100	Immunoblot analysis of the expressed proteins with and without N-glycosidase F treatment showed that only the first N-glycosylation site (Asn 75) is utilized.
8068684	2	31	link	O-linked	376:383	arg1	carbohydrate					385:396	O-linked carbohydrate	376:396	O-linked carbohydrate	376:396	The first extracellular loop is rich in serine and threonine residues which may contain O-linked carbohydrate.
8068684	4	32	theme	transfected	778:788	arg1	cells					790:794	the transfected cells	774:794	the transfected cells	774:794	The mutated DNAs were expressed in PS120 hamster fibroblasts lacking endogenous exchanger, and the transfected cells were selected by their ability to survive acute intracellular acidification.
8068684	9	33	contain	possess	1695:1701	arg1	NHE-3					1632:1636	NHE-3	1632:1636	NHE-3	1632:1636	NHE-3, an apically-expressed epithelial isoform which does not possess the N75 N-linked putative glycosylation site and any extracellular loops enriched in serine and threonine residues, does not exhibit any detectable glycosylation.
8068684	9	33	contain	possess	1695:1701	arg2	loops					1770:1774	any extracellular loops	1752:1774	any extracellular loops enriched in serine and threonine residues	1752:1816	NHE-3, an apically-expressed epithelial isoform which does not possess the N75 N-linked putative glycosylation site and any extracellular loops enriched in serine and threonine residues, does not exhibit any detectable glycosylation.
8068684	9	33	contain	possess	1695:1701	arg2	site					1743:1746	the N75 N-linked putative glycosylation site	1703:1746	the N75 N-linked putative glycosylation site	1703:1746	NHE-3, an apically-expressed epithelial isoform which does not possess the N75 N-linked putative glycosylation site and any extracellular loops enriched in serine and threonine residues, does not exhibit any detectable glycosylation.
8068684	9	33	contain	possess	1695:1701	arg1	isoform					1672:1678	an apically-expressed epithelial isoform	1639:1678	an apically-expressed epithelial isoform which does not possess the N75 N-linked putative glycosylation site and any extracellular loops enriched in serine and threonine residues	1639:1816	NHE-3, an apically-expressed epithelial isoform which does not possess the N75 N-linked putative glycosylation site and any extracellular loops enriched in serine and threonine residues, does not exhibit any detectable glycosylation.
8068684	0	34	theme	extracellular	102:114	arg1	domain					116:121	the first N-terminal extracellular domain	81:121	the first N-terminal extracellular domain	81:121	The Na+/H+ exchanger NHE-1 possesses N- and O-linked glycosylation restricted to the first N-terminal extracellular domain.
8068684	8	35	theme	Da	1398:1399	arg1	mass					1382:1385	a molecular mass	1370:1385	a molecular mass of 110,000 Da which contains N-linked and O-linked oligosaccharide and is expressed at the cell surface	1370:1489	Two forms of NHE-1 was consistently observed, a mature form with a molecular mass of 110,000 Da which contains N-linked and O-linked oligosaccharide and is expressed at the cell surface, and a lower molecular mass form (85,000 Da) present in the endoplasmic reticulum which only contains N-linked high-mannose oligosaccharide.
8068684	8	36	with	form	1519:1522	arg1	mass					1382:1385	a molecular mass	1370:1385	a molecular mass of 110,000 Da which contains N-linked and O-linked oligosaccharide and is expressed at the cell surface	1370:1489	Two forms of NHE-1 was consistently observed, a mature form with a molecular mass of 110,000 Da which contains N-linked and O-linked oligosaccharide and is expressed at the cell surface, and a lower molecular mass form (85,000 Da) present in the endoplasmic reticulum which only contains N-linked high-mannose oligosaccharide.
8068684	7	37	theme	NHE-1	1198:1202	arg1	treatment					1185:1193	treatment	1185:1193	treatment of NHE-1 with neuraminidase and O-glycosidase	1185:1239	In addition, treatment of NHE-1 with neuraminidase and O-glycosidase demonstrated that NHE-1 also contains O-linked oligosaccharide.
8068684	2	38	dep	serine	328:333	arg1	residues					349:356	residues	349:356	residues	349:356	The first extracellular loop is rich in serine and threonine residues which may contain O-linked carbohydrate.
8068684	0	39	theme	exchanger	11:19	arg1	NHE-1					21:25	The Na+/H+ exchanger NHE-1	0:25	The Na+/H+ exchanger NHE-1	0:25	The Na+/H+ exchanger NHE-1 possesses N- and O-linked glycosylation restricted to the first N-terminal extracellular domain.
8068684	6	40	theme	F	1090:1090	arg1	treatment					1092:1100	N-glycosidase F treatment	1076:1100	N-glycosidase F treatment	1076:1100	Immunoblot analysis of the expressed proteins with and without N-glycosidase F treatment showed that only the first N-glycosylation site (Asn 75) is utilized.
8068684	3	41	theme	triple	646:651	arg1	mutants					653:659	all possible double and triple mutants	622:659	all possible double and triple mutants	622:659	In order to determine unambiguously the sites of glycosylation and their role in biosynthesis and cation transport, site-directed mutagenesis at the individual potential N-glycosylation sites (Asn to Asp) was performed and all possible double and triple mutants were constructed.
8068684	3	42	theme	double	635:640	arg1	mutants					653:659	all possible double and triple mutants	622:659	all possible double and triple mutants	622:659	In order to determine unambiguously the sites of glycosylation and their role in biosynthesis and cation transport, site-directed mutagenesis at the individual potential N-glycosylation sites (Asn to Asp) was performed and all possible double and triple mutants were constructed.
8068684	3	43	gly	glycosylation	448:460	arg1	biosynthesis					480:491	biosynthesis	480:491	biosynthesis	480:491	In order to determine unambiguously the sites of glycosylation and their role in biosynthesis and cation transport, site-directed mutagenesis at the individual potential N-glycosylation sites (Asn to Asp) was performed and all possible double and triple mutants were constructed.
8068684	3	43	gly	glycosylation	448:460	arg1	transport					504:512	cation transport	497:512	cation transport	497:512	In order to determine unambiguously the sites of glycosylation and their role in biosynthesis and cation transport, site-directed mutagenesis at the individual potential N-glycosylation sites (Asn to Asp) was performed and all possible double and triple mutants were constructed.
8068684	3	43	gly	glycosylation	448:460	arg2	glycosylation					448:460	glycosylation	448:460	glycosylation	448:460	In order to determine unambiguously the sites of glycosylation and their role in biosynthesis and cation transport, site-directed mutagenesis at the individual potential N-glycosylation sites (Asn to Asp) was performed and all possible double and triple mutants were constructed.
8068684	3	43	gly	glycosylation	448:460	arg2	sites					439:443	the sites	435:443	the sites of glycosylation and their role in biosynthesis and cation transport	435:512	In order to determine unambiguously the sites of glycosylation and their role in biosynthesis and cation transport, site-directed mutagenesis at the individual potential N-glycosylation sites (Asn to Asp) was performed and all possible double and triple mutants were constructed.
8068684	3	43	gly	glycosylation	448:460	arg2	role					472:475	their role	466:475	their role in biosynthesis and cation transport	466:512	In order to determine unambiguously the sites of glycosylation and their role in biosynthesis and cation transport, site-directed mutagenesis at the individual potential N-glycosylation sites (Asn to Asp) was performed and all possible double and triple mutants were constructed.
8068684	3	44	from	glycosylation	448:460	arg1	biosynthesis					480:491	biosynthesis	480:491	biosynthesis	480:491	In order to determine unambiguously the sites of glycosylation and their role in biosynthesis and cation transport, site-directed mutagenesis at the individual potential N-glycosylation sites (Asn to Asp) was performed and all possible double and triple mutants were constructed.
8068684	3	44	from	glycosylation	448:460	arg1	transport					504:512	cation transport	497:512	cation transport	497:512	In order to determine unambiguously the sites of glycosylation and their role in biosynthesis and cation transport, site-directed mutagenesis at the individual potential N-glycosylation sites (Asn to Asp) was performed and all possible double and triple mutants were constructed.
8068684	9	45	theme	N75	1707:1709	arg1	site					1743:1746	the N75 N-linked putative glycosylation site	1703:1746	the N75 N-linked putative glycosylation site	1703:1746	NHE-3, an apically-expressed epithelial isoform which does not possess the N75 N-linked putative glycosylation site and any extracellular loops enriched in serine and threonine residues, does not exhibit any detectable glycosylation.
8068684	3	46	theme	possible	626:633	arg1	mutants					653:659	all possible double and triple mutants	622:659	all possible double and triple mutants	622:659	In order to determine unambiguously the sites of glycosylation and their role in biosynthesis and cation transport, site-directed mutagenesis at the individual potential N-glycosylation sites (Asn to Asp) was performed and all possible double and triple mutants were constructed.
8068684	8	47	theme	N-linked	1593:1600	arg1	oligosaccharide					1615:1629	N-linked high-mannose oligosaccharide	1593:1629	N-linked high-mannose oligosaccharide	1593:1629	Two forms of NHE-1 was consistently observed, a mature form with a molecular mass of 110,000 Da which contains N-linked and O-linked oligosaccharide and is expressed at the cell surface, and a lower molecular mass form (85,000 Da) present in the endoplasmic reticulum which only contains N-linked high-mannose oligosaccharide.
8068684	2	48	from	threonine	339:347	arg1	rich					320:323	rich	320:323	rich	320:323	The first extracellular loop is rich in serine and threonine residues which may contain O-linked carbohydrate.
8068684	2	48	from	threonine	339:347	arg1	loop					312:315	The first extracellular loop	288:315	The first extracellular loop	288:315	The first extracellular loop is rich in serine and threonine residues which may contain O-linked carbohydrate.
8068684	3	49	theme	role	472:475	arg1	glycosylation					448:460	glycosylation	448:460	glycosylation	448:460	In order to determine unambiguously the sites of glycosylation and their role in biosynthesis and cation transport, site-directed mutagenesis at the individual potential N-glycosylation sites (Asn to Asp) was performed and all possible double and triple mutants were constructed.
8068684	3	49	theme	role	472:475	arg1	role					472:475	their role	466:475	their role in biosynthesis and cation transport	466:512	In order to determine unambiguously the sites of glycosylation and their role in biosynthesis and cation transport, site-directed mutagenesis at the individual potential N-glycosylation sites (Asn to Asp) was performed and all possible double and triple mutants were constructed.
8068684	3	49	theme	role	472:475	arg1	sites					439:443	the sites	435:443	the sites of glycosylation and their role in biosynthesis and cation transport	435:512	In order to determine unambiguously the sites of glycosylation and their role in biosynthesis and cation transport, site-directed mutagenesis at the individual potential N-glycosylation sites (Asn to Asp) was performed and all possible double and triple mutants were constructed.
8068684	8	50	theme	mature	1353:1358	arg1	form					1360:1363	a mature form	1351:1363	a mature form with a molecular mass of 110,000 Da which contains N-linked and O-linked oligosaccharide and is expressed at the cell surface	1351:1489	Two forms of NHE-1 was consistently observed, a mature form with a molecular mass of 110,000 Da which contains N-linked and O-linked oligosaccharide and is expressed at the cell surface, and a lower molecular mass form (85,000 Da) present in the endoplasmic reticulum which only contains N-linked high-mannose oligosaccharide.
8068684	1	51	dep	sites	206:210	arg1	Asn-X-Ser/Thr					213:225	Asn-X-Ser/Thr	213:225	Asn-X-Ser/Thr	213:225	The ubiquitously-expressed human Na+H+ exchanger (NHE-1) contains three consensus sites (Asn-X-Ser/Thr) for N-linked glycosylation at asparagines 75, 370, and 410.
8068684	6	52	theme	expressed	1040:1048	arg1	proteins					1050:1057	the expressed proteins	1036:1057	the expressed proteins	1036:1057	Immunoblot analysis of the expressed proteins with and without N-glycosidase F treatment showed that only the first N-glycosylation site (Asn 75) is utilized.
8068684	3	53	from	sites	439:443	arg1	biosynthesis					480:491	biosynthesis	480:491	biosynthesis	480:491	In order to determine unambiguously the sites of glycosylation and their role in biosynthesis and cation transport, site-directed mutagenesis at the individual potential N-glycosylation sites (Asn to Asp) was performed and all possible double and triple mutants were constructed.
8068684	3	53	from	sites	439:443	arg1	transport					504:512	cation transport	497:512	cation transport	497:512	In order to determine unambiguously the sites of glycosylation and their role in biosynthesis and cation transport, site-directed mutagenesis at the individual potential N-glycosylation sites (Asn to Asp) was performed and all possible double and triple mutants were constructed.
8068684	3	54	theme	cation	497:502	arg1	transport					504:512	cation transport	497:512	cation transport	497:512	In order to determine unambiguously the sites of glycosylation and their role in biosynthesis and cation transport, site-directed mutagenesis at the individual potential N-glycosylation sites (Asn to Asp) was performed and all possible double and triple mutants were constructed.
8068684	2	55	from	rich	320:323	arg1	threonine					339:347	threonine	339:347	threonine	339:347	The first extracellular loop is rich in serine and threonine residues which may contain O-linked carbohydrate.
8068684	2	55	from	rich	320:323	arg1	serine					328:333	serine	328:333	serine	328:333	The first extracellular loop is rich in serine and threonine residues which may contain O-linked carbohydrate.
8068684	6	56	theme	first	1123:1127	arg1	site					1145:1148	only the first N-glycosylation site	1114:1148	only the first N-glycosylation site (Asn 75)	1114:1157	Immunoblot analysis of the expressed proteins with and without N-glycosidase F treatment showed that only the first N-glycosylation site (Asn 75) is utilized.
8068684	6	56	theme	first	1123:1127	arg1	Asn					1151:1153	Asn 75	1151:1156	Asn 75	1151:1156	Immunoblot analysis of the expressed proteins with and without N-glycosidase F treatment showed that only the first N-glycosylation site (Asn 75) is utilized.
8068684	3	57	from	transport	504:512	arg1	glycosylation					448:460	glycosylation	448:460	glycosylation	448:460	In order to determine unambiguously the sites of glycosylation and their role in biosynthesis and cation transport, site-directed mutagenesis at the individual potential N-glycosylation sites (Asn to Asp) was performed and all possible double and triple mutants were constructed.
8068684	3	57	from	transport	504:512	arg1	role					472:475	their role	466:475	their role in biosynthesis and cation transport	466:512	In order to determine unambiguously the sites of glycosylation and their role in biosynthesis and cation transport, site-directed mutagenesis at the individual potential N-glycosylation sites (Asn to Asp) was performed and all possible double and triple mutants were constructed.
8068684	3	57	from	transport	504:512	arg1	sites					439:443	the sites	435:443	the sites of glycosylation and their role in biosynthesis and cation transport	435:512	In order to determine unambiguously the sites of glycosylation and their role in biosynthesis and cation transport, site-directed mutagenesis at the individual potential N-glycosylation sites (Asn to Asp) was performed and all possible double and triple mutants were constructed.
8068684	2	58	from	serine	328:333	arg1	rich					320:323	rich	320:323	rich	320:323	The first extracellular loop is rich in serine and threonine residues which may contain O-linked carbohydrate.
8068684	2	58	from	serine	328:333	arg1	loop					312:315	The first extracellular loop	288:315	The first extracellular loop	288:315	The first extracellular loop is rich in serine and threonine residues which may contain O-linked carbohydrate.
8068684	9	59	gly	glycosylation	1729:1741	arg2	site					1743:1746	the N75 N-linked putative glycosylation site	1703:1746	the N75 N-linked putative glycosylation site	1703:1746	NHE-3, an apically-expressed epithelial isoform which does not possess the N75 N-linked putative glycosylation site and any extracellular loops enriched in serine and threonine residues, does not exhibit any detectable glycosylation.
8068684	4	60	theme	acute	838:842	arg1	acidification					858:870	acute intracellular acidification	838:870	acute intracellular acidification	838:870	The mutated DNAs were expressed in PS120 hamster fibroblasts lacking endogenous exchanger, and the transfected cells were selected by their ability to survive acute intracellular acidification.
8068684	0	61	link	O-linked	44:51	arg1	glycosylation					53:65	N- and O-linked glycosylation	37:65	N- and O-linked glycosylation restricted to the first N-terminal extracellular domain	37:121	The Na+/H+ exchanger NHE-1 possesses N- and O-linked glycosylation restricted to the first N-terminal extracellular domain.
8068684	3	62	dep	Asp	599:601	arg1	to					596:597	to	596:597	to	596:597	In order to determine unambiguously the sites of glycosylation and their role in biosynthesis and cation transport, site-directed mutagenesis at the individual potential N-glycosylation sites (Asn to Asp) was performed and all possible double and triple mutants were constructed.
8068684	9	63	theme	putative	1720:1727	arg1	site					1743:1746	the N75 N-linked putative glycosylation site	1703:1746	the N75 N-linked putative glycosylation site	1703:1746	NHE-3, an apically-expressed epithelial isoform which does not possess the N75 N-linked putative glycosylation site and any extracellular loops enriched in serine and threonine residues, does not exhibit any detectable glycosylation.
8068684	8	64	link	N-linked	1593:1600	arg1	oligosaccharide					1615:1629	N-linked high-mannose oligosaccharide	1593:1629	N-linked high-mannose oligosaccharide	1593:1629	Two forms of NHE-1 was consistently observed, a mature form with a molecular mass of 110,000 Da which contains N-linked and O-linked oligosaccharide and is expressed at the cell surface, and a lower molecular mass form (85,000 Da) present in the endoplasmic reticulum which only contains N-linked high-mannose oligosaccharide.
8068684	1	65	link	N-linked	232:239	arg1	glycosylation					241:253	N-linked glycosylation	232:253	N-linked glycosylation at asparagines 75, 370, and 410	232:285	The ubiquitously-expressed human Na+H+ exchanger (NHE-1) contains three consensus sites (Asn-X-Ser/Thr) for N-linked glycosylation at asparagines 75, 370, and 410.
8068684	3	66	theme	potential	559:567	arg1	Asp					599:601	Asn to Asp	592:601	Asn to Asp	592:601	In order to determine unambiguously the sites of glycosylation and their role in biosynthesis and cation transport, site-directed mutagenesis at the individual potential N-glycosylation sites (Asn to Asp) was performed and all possible double and triple mutants were constructed.
8068684	3	66	theme	potential	559:567	arg1	sites					585:589	the individual potential N-glycosylation sites	544:589	the individual potential N-glycosylation sites (Asn to Asp)	544:602	In order to determine unambiguously the sites of glycosylation and their role in biosynthesis and cation transport, site-directed mutagenesis at the individual potential N-glycosylation sites (Asn to Asp) was performed and all possible double and triple mutants were constructed.
8068684	7	67	with	treatment	1185:1193	arg1	O-glycosidase					1227:1239	O-glycosidase	1227:1239	O-glycosidase	1227:1239	In addition, treatment of NHE-1 with neuraminidase and O-glycosidase demonstrated that NHE-1 also contains O-linked oligosaccharide.
8068684	7	67	with	treatment	1185:1193	arg1	neuraminidase					1209:1221	neuraminidase	1209:1221	neuraminidase	1209:1221	In addition, treatment of NHE-1 with neuraminidase and O-glycosidase demonstrated that NHE-1 also contains O-linked oligosaccharide.
8068684	7	68	link	O-linked	1279:1286	arg1	oligosaccharide					1288:1302	O-linked oligosaccharide	1279:1302	O-linked oligosaccharide	1279:1302	In addition, treatment of NHE-1 with neuraminidase and O-glycosidase demonstrated that NHE-1 also contains O-linked oligosaccharide.
8068684	8	69	theme	cell	1478:1481	arg1	surface					1483:1489	the cell surface	1474:1489	the cell surface	1474:1489	Two forms of NHE-1 was consistently observed, a mature form with a molecular mass of 110,000 Da which contains N-linked and O-linked oligosaccharide and is expressed at the cell surface, and a lower molecular mass form (85,000 Da) present in the endoplasmic reticulum which only contains N-linked high-mannose oligosaccharide.
8068684	1	70	from	asparagines	258:268	arg1	glycosylation					241:253	N-linked glycosylation	232:253	N-linked glycosylation at asparagines 75, 370, and 410	232:285	The ubiquitously-expressed human Na+H+ exchanger (NHE-1) contains three consensus sites (Asn-X-Ser/Thr) for N-linked glycosylation at asparagines 75, 370, and 410.
8068684	2	71	contain	contain	368:374	arg2	carbohydrate					385:396	O-linked carbohydrate	376:396	O-linked carbohydrate	376:396	The first extracellular loop is rich in serine and threonine residues which may contain O-linked carbohydrate.
8068684	2	71	contain	contain	368:374	arg1	which					358:362	which	358:362	which	358:362	The first extracellular loop is rich in serine and threonine residues which may contain O-linked carbohydrate.
8068684	5	72	theme	functional	897:906	arg1	exchangers					908:917	functional exchangers	897:917	functional exchangers that had transport rates and pharmacological profiles that were similar to that of wild-type	897:1010	All constructs produced functional exchangers that had transport rates and pharmacological profiles that were similar to that of wild-type.
8068684	3	73	theme	Asn	592:594	arg1	Asp					599:601	Asn to Asp	592:601	Asn to Asp	592:601	In order to determine unambiguously the sites of glycosylation and their role in biosynthesis and cation transport, site-directed mutagenesis at the individual potential N-glycosylation sites (Asn to Asp) was performed and all possible double and triple mutants were constructed.
8068684	3	73	theme	Asn	592:594	arg1	sites					585:589	the individual potential N-glycosylation sites	544:589	the individual potential N-glycosylation sites (Asn to Asp)	544:602	In order to determine unambiguously the sites of glycosylation and their role in biosynthesis and cation transport, site-directed mutagenesis at the individual potential N-glycosylation sites (Asn to Asp) was performed and all possible double and triple mutants were constructed.
8068684	8	74	with	form	1360:1363	arg1	mass					1382:1385	a molecular mass	1370:1385	a molecular mass of 110,000 Da which contains N-linked and O-linked oligosaccharide and is expressed at the cell surface	1370:1489	Two forms of NHE-1 was consistently observed, a mature form with a molecular mass of 110,000 Da which contains N-linked and O-linked oligosaccharide and is expressed at the cell surface, and a lower molecular mass form (85,000 Da) present in the endoplasmic reticulum which only contains N-linked high-mannose oligosaccharide.
8068684	5	75	theme	pharmacological	948:962	arg1	profiles					964:971	pharmacological profiles	948:971	pharmacological profiles that were similar to that of wild-type	948:1010	All constructs produced functional exchangers that had transport rates and pharmacological profiles that were similar to that of wild-type.
8068684	2	76	theme	first	292:296	arg1	rich					320:323	rich	320:323	rich	320:323	The first extracellular loop is rich in serine and threonine residues which may contain O-linked carbohydrate.
8068684	2	76	theme	first	292:296	arg1	loop					312:315	The first extracellular loop	288:315	The first extracellular loop	288:315	The first extracellular loop is rich in serine and threonine residues which may contain O-linked carbohydrate.
8068684	8	77	theme	molecular	1504:1512	arg1	mass					1514:1517	lower molecular mass	1498:1517	a lower molecular mass form (85,000 Da)	1496:1534	Two forms of NHE-1 was consistently observed, a mature form with a molecular mass of 110,000 Da which contains N-linked and O-linked oligosaccharide and is expressed at the cell surface, and a lower molecular mass form (85,000 Da) present in the endoplasmic reticulum which only contains N-linked high-mannose oligosaccharide.
8068684	4	78	theme	PS120	714:718	arg1	fibroblasts					728:738	PS120 hamster fibroblasts	714:738	PS120 hamster fibroblasts lacking endogenous exchanger	714:767	The mutated DNAs were expressed in PS120 hamster fibroblasts lacking endogenous exchanger, and the transfected cells were selected by their ability to survive acute intracellular acidification.
8068684	3	79	from	sites	585:589	arg1	mutagenesis					529:539	site-directed mutagenesis	515:539	site-directed mutagenesis at the individual potential N-glycosylation sites (Asn to Asp)	515:602	In order to determine unambiguously the sites of glycosylation and their role in biosynthesis and cation transport, site-directed mutagenesis at the individual potential N-glycosylation sites (Asn to Asp) was performed and all possible double and triple mutants were constructed.
8068684	0	80	theme	restricted	67:76	arg1	glycosylation					53:65	N- and O-linked glycosylation	37:65	N- and O-linked glycosylation restricted to the first N-terminal extracellular domain	37:121	The Na+/H+ exchanger NHE-1 possesses N- and O-linked glycosylation restricted to the first N-terminal extracellular domain.
8068684	1	81	theme	Na+H+	157:161	arg1	exchanger					163:171	The ubiquitously-expressed human Na+H+ exchanger	124:171	The ubiquitously-expressed human Na+H+ exchanger (NHE-1)	124:179	The ubiquitously-expressed human Na+H+ exchanger (NHE-1) contains three consensus sites (Asn-X-Ser/Thr) for N-linked glycosylation at asparagines 75, 370, and 410.
8068684	1	81	theme	Na+H+	157:161	arg1	NHE-1					174:178	NHE-1	174:178	NHE-1	174:178	The ubiquitously-expressed human Na+H+ exchanger (NHE-1) contains three consensus sites (Asn-X-Ser/Thr) for N-linked glycosylation at asparagines 75, 370, and 410.
8068684	6	82	theme	proteins	1050:1057	arg1	analysis					1024:1031	Immunoblot analysis	1013:1031	Immunoblot analysis of the expressed proteins with and without N-glycosidase F treatment	1013:1100	Immunoblot analysis of the expressed proteins with and without N-glycosidase F treatment showed that only the first N-glycosylation site (Asn 75) is utilized.
8068684	8	83	contain	contains	1407:1414	arg1	Da					1398:1399	110,000 Da	1390:1399	110,000 Da which contains N-linked and O-linked oligosaccharide and is expressed at the cell surface	1390:1489	Two forms of NHE-1 was consistently observed, a mature form with a molecular mass of 110,000 Da which contains N-linked and O-linked oligosaccharide and is expressed at the cell surface, and a lower molecular mass form (85,000 Da) present in the endoplasmic reticulum which only contains N-linked high-mannose oligosaccharide.
8068684	8	83	contain	contains	1407:1414	arg2	oligosaccharide					1438:1452	N-linked and O-linked oligosaccharide	1416:1452	N-linked and O-linked oligosaccharide	1416:1452	Two forms of NHE-1 was consistently observed, a mature form with a molecular mass of 110,000 Da which contains N-linked and O-linked oligosaccharide and is expressed at the cell surface, and a lower molecular mass form (85,000 Da) present in the endoplasmic reticulum which only contains N-linked high-mannose oligosaccharide.
8068684	7	84	contain	contains	1270:1277	arg1	NHE-1					1259:1263	NHE-1	1259:1263	NHE-1	1259:1263	In addition, treatment of NHE-1 with neuraminidase and O-glycosidase demonstrated that NHE-1 also contains O-linked oligosaccharide.
8068684	7	84	contain	contains	1270:1277	arg2	oligosaccharide					1288:1302	O-linked oligosaccharide	1279:1302	O-linked oligosaccharide	1279:1302	In addition, treatment of NHE-1 with neuraminidase and O-glycosidase demonstrated that NHE-1 also contains O-linked oligosaccharide.
8068684	0	85	theme	N-terminal	91:100	arg1	domain					116:121	the first N-terminal extracellular domain	81:121	the first N-terminal extracellular domain	81:121	The Na+/H+ exchanger NHE-1 possesses N- and O-linked glycosylation restricted to the first N-terminal extracellular domain.
8068684	9	86	theme	apically-expressed	1642:1659	arg1	NHE-3					1632:1636	NHE-3	1632:1636	NHE-3	1632:1636	NHE-3, an apically-expressed epithelial isoform which does not possess the N75 N-linked putative glycosylation site and any extracellular loops enriched in serine and threonine residues, does not exhibit any detectable glycosylation.
8068684	9	86	theme	apically-expressed	1642:1659	arg1	isoform					1672:1678	an apically-expressed epithelial isoform	1639:1678	an apically-expressed epithelial isoform which does not possess the N75 N-linked putative glycosylation site and any extracellular loops enriched in serine and threonine residues	1639:1816	NHE-3, an apically-expressed epithelial isoform which does not possess the N75 N-linked putative glycosylation site and any extracellular loops enriched in serine and threonine residues, does not exhibit any detectable glycosylation.
8068684	6	87	gly	N-glycosylation	1129:1143	arg2	Asn					1151:1153	Asn 75	1151:1156	Asn 75	1151:1156	Immunoblot analysis of the expressed proteins with and without N-glycosidase F treatment showed that only the first N-glycosylation site (Asn 75) is utilized.
8068684	6	87	gly	N-glycosylation	1129:1143	arg2	site					1145:1148	only the first N-glycosylation site	1114:1148	only the first N-glycosylation site (Asn 75)	1114:1157	Immunoblot analysis of the expressed proteins with and without N-glycosidase F treatment showed that only the first N-glycosylation site (Asn 75) is utilized.
8068684	1	88	gly	glycosylation	241:253	arg2	asparagines					258:268	asparagines 75, 370, and 410	258:285	asparagines 75, 370, and 410	258:285	The ubiquitously-expressed human Na+H+ exchanger (NHE-1) contains three consensus sites (Asn-X-Ser/Thr) for N-linked glycosylation at asparagines 75, 370, and 410.
8068684	1	88	gly	glycosylation	241:253	arg1	asparagines					258:268	asparagines 75, 370, and 410	258:285	asparagines 75, 370, and 410	258:285	The ubiquitously-expressed human Na+H+ exchanger (NHE-1) contains three consensus sites (Asn-X-Ser/Thr) for N-linked glycosylation at asparagines 75, 370, and 410.
8068684	8	89	dep	forms	1309:1313	arg1	observed					1341:1348	observed	1341:1348	was consistently observed	1324:1348	Two forms of NHE-1 was consistently observed, a mature form with a molecular mass of 110,000 Da which contains N-linked and O-linked oligosaccharide and is expressed at the cell surface, and a lower molecular mass form (85,000 Da) present in the endoplasmic reticulum which only contains N-linked high-mannose oligosaccharide.
8068684	9	90	link	N-linked	1711:1718	arg1	site					1743:1746	the N75 N-linked putative glycosylation site	1703:1746	the N75 N-linked putative glycosylation site	1703:1746	NHE-3, an apically-expressed epithelial isoform which does not possess the N75 N-linked putative glycosylation site and any extracellular loops enriched in serine and threonine residues, does not exhibit any detectable glycosylation.
8068684	2	91	theme	O-linked	376:383	arg1	carbohydrate					385:396	O-linked carbohydrate	376:396	O-linked carbohydrate	376:396	The first extracellular loop is rich in serine and threonine residues which may contain O-linked carbohydrate.
8068684	0	92	theme	Na+/H+	4:9	arg1	exchanger					11:19	The Na+/H+ exchanger	0:19	The Na+/H+ exchanger NHE-1	0:25	The Na+/H+ exchanger NHE-1 possesses N- and O-linked glycosylation restricted to the first N-terminal extracellular domain.
8068684	9	93	theme	detectable	1840:1849	arg1	glycosylation					1851:1863	any detectable glycosylation	1836:1863	any detectable glycosylation	1836:1863	NHE-3, an apically-expressed epithelial isoform which does not possess the N75 N-linked putative glycosylation site and any extracellular loops enriched in serine and threonine residues, does not exhibit any detectable glycosylation.
8068684	8	94	theme	endoplasmic	1551:1561	arg1	reticulum					1563:1571	the endoplasmic reticulum	1547:1571	the endoplasmic reticulum which only contains N-linked high-mannose oligosaccharide	1547:1629	Two forms of NHE-1 was consistently observed, a mature form with a molecular mass of 110,000 Da which contains N-linked and O-linked oligosaccharide and is expressed at the cell surface, and a lower molecular mass form (85,000 Da) present in the endoplasmic reticulum which only contains N-linked high-mannose oligosaccharide.
8068684	8	95	theme	110,000	1390:1396	arg1	Da					1398:1399	110,000 Da	1390:1399	110,000 Da which contains N-linked and O-linked oligosaccharide and is expressed at the cell surface	1390:1489	Two forms of NHE-1 was consistently observed, a mature form with a molecular mass of 110,000 Da which contains N-linked and O-linked oligosaccharide and is expressed at the cell surface, and a lower molecular mass form (85,000 Da) present in the endoplasmic reticulum which only contains N-linked high-mannose oligosaccharide.
8068684	4	96	theme	endogenous	748:757	arg1	exchanger					759:767	endogenous exchanger	748:767	endogenous exchanger	748:767	The mutated DNAs were expressed in PS120 hamster fibroblasts lacking endogenous exchanger, and the transfected cells were selected by their ability to survive acute intracellular acidification.
8068684	0	97	theme	N-	37:38	arg1	glycosylation					53:65	N- and O-linked glycosylation	37:65	N- and O-linked glycosylation restricted to the first N-terminal extracellular domain	37:121	The Na+/H+ exchanger NHE-1 possesses N- and O-linked glycosylation restricted to the first N-terminal extracellular domain.
8068684	6	98	theme	N-glycosidase	1076:1088	arg1	treatment					1092:1100	N-glycosidase F treatment	1076:1100	N-glycosidase F treatment	1076:1100	Immunoblot analysis of the expressed proteins with and without N-glycosidase F treatment showed that only the first N-glycosylation site (Asn 75) is utilized.
8068684	1	99	contain	contains	181:188	arg1	exchanger					163:171	The ubiquitously-expressed human Na+H+ exchanger	124:171	The ubiquitously-expressed human Na+H+ exchanger (NHE-1)	124:179	The ubiquitously-expressed human Na+H+ exchanger (NHE-1) contains three consensus sites (Asn-X-Ser/Thr) for N-linked glycosylation at asparagines 75, 370, and 410.
8068684	1	99	contain	contains	181:188	arg2	sites					206:210	three consensus sites	190:210	three consensus sites (Asn-X-Ser/Thr) for N-linked glycosylation at asparagines 75, 370, and 410	190:285	The ubiquitously-expressed human Na+H+ exchanger (NHE-1) contains three consensus sites (Asn-X-Ser/Thr) for N-linked glycosylation at asparagines 75, 370, and 410.
8068684	1	99	contain	contains	181:188	arg1	NHE-1					174:178	NHE-1	174:178	NHE-1	174:178	The ubiquitously-expressed human Na+H+ exchanger (NHE-1) contains three consensus sites (Asn-X-Ser/Thr) for N-linked glycosylation at asparagines 75, 370, and 410.
8068684	8	100	theme	N-linked	1416:1423	arg1	oligosaccharide					1438:1452	N-linked and O-linked oligosaccharide	1416:1452	N-linked and O-linked oligosaccharide	1416:1452	Two forms of NHE-1 was consistently observed, a mature form with a molecular mass of 110,000 Da which contains N-linked and O-linked oligosaccharide and is expressed at the cell surface, and a lower molecular mass form (85,000 Da) present in the endoplasmic reticulum which only contains N-linked high-mannose oligosaccharide.
8068684	3	101	theme	glycosylation	448:460	arg1	glycosylation					448:460	glycosylation	448:460	glycosylation	448:460	In order to determine unambiguously the sites of glycosylation and their role in biosynthesis and cation transport, site-directed mutagenesis at the individual potential N-glycosylation sites (Asn to Asp) was performed and all possible double and triple mutants were constructed.
8068684	3	101	theme	glycosylation	448:460	arg1	role					472:475	their role	466:475	their role in biosynthesis and cation transport	466:512	In order to determine unambiguously the sites of glycosylation and their role in biosynthesis and cation transport, site-directed mutagenesis at the individual potential N-glycosylation sites (Asn to Asp) was performed and all possible double and triple mutants were constructed.
8068684	3	101	theme	glycosylation	448:460	arg1	sites					439:443	the sites	435:443	the sites of glycosylation and their role in biosynthesis and cation transport	435:512	In order to determine unambiguously the sites of glycosylation and their role in biosynthesis and cation transport, site-directed mutagenesis at the individual potential N-glycosylation sites (Asn to Asp) was performed and all possible double and triple mutants were constructed.
8068684	0	102	theme	O-linked	44:51	arg1	glycosylation					53:65	N- and O-linked glycosylation	37:65	N- and O-linked glycosylation restricted to the first N-terminal extracellular domain	37:121	The Na+/H+ exchanger NHE-1 possesses N- and O-linked glycosylation restricted to the first N-terminal extracellular domain.
8068684	8	103	theme	high-mannose	1602:1613	arg1	oligosaccharide					1615:1629	N-linked high-mannose oligosaccharide	1593:1629	N-linked high-mannose oligosaccharide	1593:1629	Two forms of NHE-1 was consistently observed, a mature form with a molecular mass of 110,000 Da which contains N-linked and O-linked oligosaccharide and is expressed at the cell surface, and a lower molecular mass form (85,000 Da) present in the endoplasmic reticulum which only contains N-linked high-mannose oligosaccharide.
8068684	8	104	theme	O-linked	1429:1436	arg1	oligosaccharide					1438:1452	N-linked and O-linked oligosaccharide	1416:1452	N-linked and O-linked oligosaccharide	1416:1452	Two forms of NHE-1 was consistently observed, a mature form with a molecular mass of 110,000 Da which contains N-linked and O-linked oligosaccharide and is expressed at the cell surface, and a lower molecular mass form (85,000 Da) present in the endoplasmic reticulum which only contains N-linked high-mannose oligosaccharide.
8068684	9	105	dep	serine	1788:1793	arg1	residues					1809:1816	residues	1809:1816	residues	1809:1816	NHE-3, an apically-expressed epithelial isoform which does not possess the N75 N-linked putative glycosylation site and any extracellular loops enriched in serine and threonine residues, does not exhibit any detectable glycosylation.
8068684	1	106	theme	N-linked	232:239	arg1	glycosylation					241:253	N-linked glycosylation	232:253	N-linked glycosylation at asparagines 75, 370, and 410	232:285	The ubiquitously-expressed human Na+H+ exchanger (NHE-1) contains three consensus sites (Asn-X-Ser/Thr) for N-linked glycosylation at asparagines 75, 370, and 410.
8068684	9	107	theme	epithelial	1661:1670	arg1	NHE-3					1632:1636	NHE-3	1632:1636	NHE-3	1632:1636	NHE-3, an apically-expressed epithelial isoform which does not possess the N75 N-linked putative glycosylation site and any extracellular loops enriched in serine and threonine residues, does not exhibit any detectable glycosylation.
8068684	9	107	theme	epithelial	1661:1670	arg1	isoform					1672:1678	an apically-expressed epithelial isoform	1639:1678	an apically-expressed epithelial isoform which does not possess the N75 N-linked putative glycosylation site and any extracellular loops enriched in serine and threonine residues	1639:1816	NHE-3, an apically-expressed epithelial isoform which does not possess the N75 N-linked putative glycosylation site and any extracellular loops enriched in serine and threonine residues, does not exhibit any detectable glycosylation.
8068684	3	108	theme	site-directed	515:527	arg1	mutagenesis					529:539	site-directed mutagenesis	515:539	site-directed mutagenesis at the individual potential N-glycosylation sites (Asn to Asp)	515:602	In order to determine unambiguously the sites of glycosylation and their role in biosynthesis and cation transport, site-directed mutagenesis at the individual potential N-glycosylation sites (Asn to Asp) was performed and all possible double and triple mutants were constructed.
22365600	3	0	theme	homolog	347:353	arg1	interaction					308:318	the interaction	304:318	the interaction of a bacterial O-GlcNAcase homolog with three different synthetic glycopeptides derived from characterized O-GlcNAc sites in the human proteome	304:462	We report the molecular details of the interaction of a bacterial O-GlcNAcase homolog with three different synthetic glycopeptides derived from characterized O-GlcNAc sites in the human proteome.
22365600	3	1	attach	derived	400:406	arg1	sites					436:440	characterized O-GlcNAc sites	413:440	characterized O-GlcNAc sites in the human proteome	413:462	We report the molecular details of the interaction of a bacterial O-GlcNAcase homolog with three different synthetic glycopeptides derived from characterized O-GlcNAc sites in the human proteome.
22365600	3	1	attach	derived	400:406	arg2	glycopeptides					386:398	three different synthetic glycopeptides	360:398	three different synthetic glycopeptides derived from characterized O-GlcNAc sites in the human proteome	360:462	We report the molecular details of the interaction of a bacterial O-GlcNAcase homolog with three different synthetic glycopeptides derived from characterized O-GlcNAc sites in the human proteome.
22365600	5	2	theme	hydrogen	733:740	arg1	bonds					742:746	intramolecular hydrogen bonds	718:746	intramolecular hydrogen bonds	718:746	In addition to extensive contacts with the sugar, O-GlcNAcase recognizes the peptide backbone through hydrophobic interactions and intramolecular hydrogen bonds, while avoiding interactions with the glycopeptide side chains.
22365600	4	3	theme	similar	549:555	arg1	orientation					557:567	similar orientation	549:567	similar orientation	549:567	Strikingly, the peptides bind a conserved O-GlcNAcase substrate binding groove with similar orientation and conformation.
22365600	7	4	theme	peptide	1064:1070	arg1	site					1080:1083	the peptide binding site	1060:1083	the peptide binding site	1060:1083	In addition, this work will aid development of O-GlcNAcase inhibitors that target the peptide binding site.
22365600	6	5	theme	complete	950:957	arg1	proteome					968:975	the complete O-GlcNAc proteome	946:975	the complete O-GlcNAc proteome	946:975	These findings elucidate the molecular basis of O-GlcNAcase substrate specificity, explaining how a single enzyme achieves cycling of the complete O-GlcNAc proteome.
22365600	6	6	theme	O-GlcNAc	959:966	arg1	proteome					968:975	the complete O-GlcNAc proteome	946:975	the complete O-GlcNAc proteome	946:975	These findings elucidate the molecular basis of O-GlcNAcase substrate specificity, explaining how a single enzyme achieves cycling of the complete O-GlcNAc proteome.
22365600	0	7	from	Synergy	0:6	arg1	recognition					54:64	O-GlcNAcase substrate recognition	32:64	O-GlcNAcase substrate recognition	32:64	Synergy of peptide and sugar in O-GlcNAcase substrate recognition.
22365600	7	8	theme	binding	1072:1078	arg1	site					1080:1083	the peptide binding site	1060:1083	the peptide binding site	1060:1083	In addition, this work will aid development of O-GlcNAcase inhibitors that target the peptide binding site.
22365600	5	9	theme	peptide	664:670	arg1	backbone					672:679	the peptide backbone	660:679	the peptide backbone	660:679	In addition to extensive contacts with the sugar, O-GlcNAcase recognizes the peptide backbone through hydrophobic interactions and intramolecular hydrogen bonds, while avoiding interactions with the glycopeptide side chains.
22365600	4	10	theme	binding	529:535	arg1	groove					537:542	a conserved O-GlcNAcase substrate binding groove	495:542	a conserved O-GlcNAcase substrate binding groove with similar orientation and conformation	495:584	Strikingly, the peptides bind a conserved O-GlcNAcase substrate binding groove with similar orientation and conformation.
22365600	5	11	with	contacts	612:619	arg1	sugar					630:634	the sugar	626:634	the sugar	626:634	In addition to extensive contacts with the sugar, O-GlcNAcase recognizes the peptide backbone through hydrophobic interactions and intramolecular hydrogen bonds, while avoiding interactions with the glycopeptide side chains.
22365600	3	12	theme	synthetic	376:384	arg1	glycopeptides					386:398	three different synthetic glycopeptides	360:398	three different synthetic glycopeptides derived from characterized O-GlcNAc sites in the human proteome	360:462	We report the molecular details of the interaction of a bacterial O-GlcNAcase homolog with three different synthetic glycopeptides derived from characterized O-GlcNAc sites in the human proteome.
22365600	2	13	theme	O-GlcNAc	171:178	arg1	addition					180:187	O-GlcNAc addition	171:187	O-GlcNAc addition	171:187	O-GlcNAc addition and removal is catalyzed by O-GlcNAc transferase and O-GlcNAcase, respectively.
22365600	5	14	theme	hydrophobic	689:699	arg1	interactions					701:712	hydrophobic interactions	689:712	hydrophobic interactions	689:712	In addition to extensive contacts with the sugar, O-GlcNAcase recognizes the peptide backbone through hydrophobic interactions and intramolecular hydrogen bonds, while avoiding interactions with the glycopeptide side chains.
22365600	1	15	theme	Protein	67:73	arg1	O-GlcNAcylation					75:89	Protein O-GlcNAcylation	67:89	Protein O-GlcNAcylation	67:89	Protein O-GlcNAcylation is an essential reversible posttranslational modification in higher eukaryotes.
22365600	1	15	theme	Protein	67:73	arg1	modification					136:147	an essential reversible posttranslational modification	94:147	an essential reversible posttranslational modification in higher eukaryotes	94:168	Protein O-GlcNAcylation is an essential reversible posttranslational modification in higher eukaryotes.
22365600	5	16	theme	side	799:802	arg1	chains					804:809	the glycopeptide side chains	782:809	the glycopeptide side chains	782:809	In addition to extensive contacts with the sugar, O-GlcNAcase recognizes the peptide backbone through hydrophobic interactions and intramolecular hydrogen bonds, while avoiding interactions with the glycopeptide side chains.
22365600	3	17	theme	human	449:453	arg1	proteome					455:462	the human proteome	445:462	the human proteome	445:462	We report the molecular details of the interaction of a bacterial O-GlcNAcase homolog with three different synthetic glycopeptides derived from characterized O-GlcNAc sites in the human proteome.
22365600	3	18	from	sites	436:440	arg1	proteome					455:462	the human proteome	445:462	the human proteome	445:462	We report the molecular details of the interaction of a bacterial O-GlcNAcase homolog with three different synthetic glycopeptides derived from characterized O-GlcNAc sites in the human proteome.
22365600	3	19	theme	molecular	283:291	arg1	details					293:299	the molecular details	279:299	the molecular details of the interaction of a bacterial O-GlcNAcase homolog with three different synthetic glycopeptides derived from characterized O-GlcNAc sites in the human proteome	279:462	We report the molecular details of the interaction of a bacterial O-GlcNAcase homolog with three different synthetic glycopeptides derived from characterized O-GlcNAc sites in the human proteome.
22365600	7	20	theme	inhibitors	1037:1046	arg1	development					1010:1020	development	1010:1020	development of O-GlcNAcase inhibitors that target the peptide binding site	1010:1083	In addition, this work will aid development of O-GlcNAcase inhibitors that target the peptide binding site.
22365600	7	21	theme	O-GlcNAcase	1025:1035	arg1	inhibitors					1037:1046	O-GlcNAcase inhibitors	1025:1046	O-GlcNAcase inhibitors that target the peptide binding site	1025:1083	In addition, this work will aid development of O-GlcNAcase inhibitors that target the peptide binding site.
22365600	4	22	theme	substrate	519:527	arg1	groove					537:542	a conserved O-GlcNAcase substrate binding groove	495:542	a conserved O-GlcNAcase substrate binding groove with similar orientation and conformation	495:584	Strikingly, the peptides bind a conserved O-GlcNAcase substrate binding groove with similar orientation and conformation.
22365600	5	23	theme	intramolecular	718:731	arg1	bonds					742:746	intramolecular hydrogen bonds	718:746	intramolecular hydrogen bonds	718:746	In addition to extensive contacts with the sugar, O-GlcNAcase recognizes the peptide backbone through hydrophobic interactions and intramolecular hydrogen bonds, while avoiding interactions with the glycopeptide side chains.
22365600	6	24	theme	specificity	882:892	arg1	basis					851:855	the molecular basis	837:855	the molecular basis of O-GlcNAcase substrate specificity	837:892	These findings elucidate the molecular basis of O-GlcNAcase substrate specificity, explaining how a single enzyme achieves cycling of the complete O-GlcNAc proteome.
22365600	5	25	with	interactions	764:775	arg1	chains					804:809	the glycopeptide side chains	782:809	the glycopeptide side chains	782:809	In addition to extensive contacts with the sugar, O-GlcNAcase recognizes the peptide backbone through hydrophobic interactions and intramolecular hydrogen bonds, while avoiding interactions with the glycopeptide side chains.
22365600	3	26	theme	characterized	413:425	arg1	sites					436:440	characterized O-GlcNAc sites	413:440	characterized O-GlcNAc sites in the human proteome	413:462	We report the molecular details of the interaction of a bacterial O-GlcNAcase homolog with three different synthetic glycopeptides derived from characterized O-GlcNAc sites in the human proteome.
22365600	5	27	theme	glycopeptide	786:797	arg1	chains					804:809	the glycopeptide side chains	782:809	the glycopeptide side chains	782:809	In addition to extensive contacts with the sugar, O-GlcNAcase recognizes the peptide backbone through hydrophobic interactions and intramolecular hydrogen bonds, while avoiding interactions with the glycopeptide side chains.
22365600	1	28	from	modification	136:147	arg1	eukaryotes					159:168	higher eukaryotes	152:168	higher eukaryotes	152:168	Protein O-GlcNAcylation is an essential reversible posttranslational modification in higher eukaryotes.
22365600	1	29	theme	essential	97:105	arg1	O-GlcNAcylation					75:89	Protein O-GlcNAcylation	67:89	Protein O-GlcNAcylation	67:89	Protein O-GlcNAcylation is an essential reversible posttranslational modification in higher eukaryotes.
22365600	1	29	theme	essential	97:105	arg1	modification					136:147	an essential reversible posttranslational modification	94:147	an essential reversible posttranslational modification in higher eukaryotes	94:168	Protein O-GlcNAcylation is an essential reversible posttranslational modification in higher eukaryotes.
22365600	3	30	theme	O-GlcNAc	427:434	arg1	sites					436:440	characterized O-GlcNAc sites	413:440	characterized O-GlcNAc sites in the human proteome	413:462	We report the molecular details of the interaction of a bacterial O-GlcNAcase homolog with three different synthetic glycopeptides derived from characterized O-GlcNAc sites in the human proteome.
22365600	3	31	theme	interaction	308:318	arg1	details					293:299	the molecular details	279:299	the molecular details of the interaction of a bacterial O-GlcNAcase homolog with three different synthetic glycopeptides derived from characterized O-GlcNAc sites in the human proteome	279:462	We report the molecular details of the interaction of a bacterial O-GlcNAcase homolog with three different synthetic glycopeptides derived from characterized O-GlcNAc sites in the human proteome.
22365600	1	32	theme	reversible	107:116	arg1	O-GlcNAcylation					75:89	Protein O-GlcNAcylation	67:89	Protein O-GlcNAcylation	67:89	Protein O-GlcNAcylation is an essential reversible posttranslational modification in higher eukaryotes.
22365600	1	32	theme	reversible	107:116	arg1	modification					136:147	an essential reversible posttranslational modification	94:147	an essential reversible posttranslational modification in higher eukaryotes	94:168	Protein O-GlcNAcylation is an essential reversible posttranslational modification in higher eukaryotes.
22365600	3	33	gly	glycopeptides	386:398	arg2	glycopeptides					386:398	three different synthetic glycopeptides	360:398	three different synthetic glycopeptides derived from characterized O-GlcNAc sites in the human proteome	360:462	We report the molecular details of the interaction of a bacterial O-GlcNAcase homolog with three different synthetic glycopeptides derived from characterized O-GlcNAc sites in the human proteome.
22365600	6	34	theme	proteome	968:975	arg1	cycling					935:941	cycling	935:941	cycling of the complete O-GlcNAc proteome	935:975	These findings elucidate the molecular basis of O-GlcNAcase substrate specificity, explaining how a single enzyme achieves cycling of the complete O-GlcNAc proteome.
22365600	0	35	theme	sugar	23:27	arg1	Synergy					0:6	Synergy	0:6	Synergy of peptide and sugar in O-GlcNAcase substrate recognition	0:64	Synergy of peptide and sugar in O-GlcNAcase substrate recognition.
22365600	4	36	theme	O-GlcNAcase	507:517	arg1	groove					537:542	a conserved O-GlcNAcase substrate binding groove	495:542	a conserved O-GlcNAcase substrate binding groove with similar orientation and conformation	495:584	Strikingly, the peptides bind a conserved O-GlcNAcase substrate binding groove with similar orientation and conformation.
22365600	5	37	theme	extensive	602:610	arg1	contacts					612:619	extensive contacts	602:619	extensive contacts with the sugar	602:634	In addition to extensive contacts with the sugar, O-GlcNAcase recognizes the peptide backbone through hydrophobic interactions and intramolecular hydrogen bonds, while avoiding interactions with the glycopeptide side chains.
22365600	3	38	with	interaction	308:318	arg1	glycopeptides					386:398	three different synthetic glycopeptides	360:398	three different synthetic glycopeptides derived from characterized O-GlcNAc sites in the human proteome	360:462	We report the molecular details of the interaction of a bacterial O-GlcNAcase homolog with three different synthetic glycopeptides derived from characterized O-GlcNAc sites in the human proteome.
22365600	0	39	theme	substrate	44:52	arg1	recognition					54:64	O-GlcNAcase substrate recognition	32:64	O-GlcNAcase substrate recognition	32:64	Synergy of peptide and sugar in O-GlcNAcase substrate recognition.
22365600	3	40	theme	bacterial	325:333	arg1	homolog					347:353	a bacterial O-GlcNAcase homolog	323:353	a bacterial O-GlcNAcase homolog	323:353	We report the molecular details of the interaction of a bacterial O-GlcNAcase homolog with three different synthetic glycopeptides derived from characterized O-GlcNAc sites in the human proteome.
22365600	4	41	theme	conserved	497:505	arg1	groove					537:542	a conserved O-GlcNAcase substrate binding groove	495:542	a conserved O-GlcNAcase substrate binding groove with similar orientation and conformation	495:584	Strikingly, the peptides bind a conserved O-GlcNAcase substrate binding groove with similar orientation and conformation.
22365600	1	42	theme	posttranslational	118:134	arg1	O-GlcNAcylation					75:89	Protein O-GlcNAcylation	67:89	Protein O-GlcNAcylation	67:89	Protein O-GlcNAcylation is an essential reversible posttranslational modification in higher eukaryotes.
22365600	1	42	theme	posttranslational	118:134	arg1	modification					136:147	an essential reversible posttranslational modification	94:147	an essential reversible posttranslational modification in higher eukaryotes	94:168	Protein O-GlcNAcylation is an essential reversible posttranslational modification in higher eukaryotes.
22365600	0	43	theme	O-GlcNAcase	32:42	arg1	recognition					54:64	O-GlcNAcase substrate recognition	32:64	O-GlcNAcase substrate recognition	32:64	Synergy of peptide and sugar in O-GlcNAcase substrate recognition.
22365600	3	44	theme	O-GlcNAcase	335:345	arg1	homolog					347:353	a bacterial O-GlcNAcase homolog	323:353	a bacterial O-GlcNAcase homolog	323:353	We report the molecular details of the interaction of a bacterial O-GlcNAcase homolog with three different synthetic glycopeptides derived from characterized O-GlcNAc sites in the human proteome.
22365600	5	45	gly	glycopeptide	786:797	arg2	glycopeptide					786:797	glycopeptide	786:797	glycopeptide	786:797	In addition to extensive contacts with the sugar, O-GlcNAcase recognizes the peptide backbone through hydrophobic interactions and intramolecular hydrogen bonds, while avoiding interactions with the glycopeptide side chains.
22365600	6	46	theme	substrate	872:880	arg1	specificity					882:892	O-GlcNAcase substrate specificity	860:892	O-GlcNAcase substrate specificity	860:892	These findings elucidate the molecular basis of O-GlcNAcase substrate specificity, explaining how a single enzyme achieves cycling of the complete O-GlcNAc proteome.
22365600	6	47	theme	single	912:917	arg1	enzyme					919:924	a single enzyme	910:924	a single enzyme	910:924	These findings elucidate the molecular basis of O-GlcNAcase substrate specificity, explaining how a single enzyme achieves cycling of the complete O-GlcNAc proteome.
22365600	6	48	theme	molecular	841:849	arg1	basis					851:855	the molecular basis	837:855	the molecular basis of O-GlcNAcase substrate specificity	837:892	These findings elucidate the molecular basis of O-GlcNAcase substrate specificity, explaining how a single enzyme achieves cycling of the complete O-GlcNAc proteome.
22365600	2	49	theme	O-GlcNAc	217:224	arg1	transferase					226:236	O-GlcNAc transferase	217:236	O-GlcNAc transferase	217:236	O-GlcNAc addition and removal is catalyzed by O-GlcNAc transferase and O-GlcNAcase, respectively.
22365600	6	50	theme	O-GlcNAcase	860:870	arg1	specificity					882:892	O-GlcNAcase substrate specificity	860:892	O-GlcNAcase substrate specificity	860:892	These findings elucidate the molecular basis of O-GlcNAcase substrate specificity, explaining how a single enzyme achieves cycling of the complete O-GlcNAc proteome.
22365600	1	51	theme	higher	152:157	arg1	eukaryotes					159:168	higher eukaryotes	152:168	higher eukaryotes	152:168	Protein O-GlcNAcylation is an essential reversible posttranslational modification in higher eukaryotes.
22365600	3	52	theme	different	366:374	arg1	glycopeptides					386:398	three different synthetic glycopeptides	360:398	three different synthetic glycopeptides derived from characterized O-GlcNAc sites in the human proteome	360:462	We report the molecular details of the interaction of a bacterial O-GlcNAcase homolog with three different synthetic glycopeptides derived from characterized O-GlcNAc sites in the human proteome.
22365600	0	53	theme	peptide	11:17	arg1	Synergy					0:6	Synergy	0:6	Synergy of peptide and sugar in O-GlcNAcase substrate recognition	0:64	Synergy of peptide and sugar in O-GlcNAcase substrate recognition.
22365600	4	54	with	groove	537:542	arg1	orientation					557:567	similar orientation	549:567	similar orientation	549:567	Strikingly, the peptides bind a conserved O-GlcNAcase substrate binding groove with similar orientation and conformation.
22365600	4	54	with	groove	537:542	arg1	conformation					573:584	conformation	573:584	conformation	573:584	Strikingly, the peptides bind a conserved O-GlcNAcase substrate binding groove with similar orientation and conformation.
28625484	0	0	theme	O-GlcNAc	81:88	arg1	transferase					90:100	O-GlcNAc transferase	81:100	O-GlcNAc transferase	81:100	Nuclear factor-erythroid-2 related transcription factor-1 (Nrf1) is regulated by O-GlcNAc transferase.
28625484	5	1	theme	O-GlcNAc	679:686	arg1	Addition					667:674	Addition	667:674	Addition of O-GlcNAc	667:686	Addition of O-GlcNAc decreases ubiquitination and degradation of Nrf1a.
28625484	7	2	theme	Nrf1a	901:905	arg1	regulator					888:896	a regulator	886:896	a regulator of Nrf1a	886:905	Together, these data suggest that OGT can act as a regulator of Nrf1a.
28625484	7	2	theme	Nrf1a	901:905	arg1	OGT					871:873	OGT	871:873	OGT	871:873	Together, these data suggest that OGT can act as a regulator of Nrf1a.
28625484	1	3	theme	transcription	149:161	arg1	factor					163:168	transcription factor	149:168	The Nrf1 (Nuclear factor E2-related factor 1) transcription factor	103:168	The Nrf1 (Nuclear factor E2-related factor 1) transcription factor performs a critical role in regulating cellular homeostasis.
28625484	2	4	theme	Cell	278:281	arg1	transferase					346:356	O-GlcNAc transferase	337:356	O-GlcNAc transferase (OGT)	337:362	Using a proteomic approach, we identified Host Cell Factor-1 (HCF1), a co-regulator of transcription, and O-GlcNAc transferase (OGT), the enzyme that mediates protein O-GlcNAcylation, as cellular partners of Nrf1a, an isoform of Nrf1.
28625484	2	4	theme	Cell	278:281	arg1	partners					427:434	cellular partners	418:434	cellular partners of Nrf1a, an isoform of Nrf1	418:463	Using a proteomic approach, we identified Host Cell Factor-1 (HCF1), a co-regulator of transcription, and O-GlcNAc transferase (OGT), the enzyme that mediates protein O-GlcNAcylation, as cellular partners of Nrf1a, an isoform of Nrf1.
28625484	2	4	theme	Cell	278:281	arg1	Factor-1					283:290	Host Cell Factor-1	273:290	Host Cell Factor-1 (HCF1)	273:297	Using a proteomic approach, we identified Host Cell Factor-1 (HCF1), a co-regulator of transcription, and O-GlcNAc transferase (OGT), the enzyme that mediates protein O-GlcNAcylation, as cellular partners of Nrf1a, an isoform of Nrf1.
28625484	2	4	theme	Cell	278:281	arg1	co-regulator					302:313	a co-regulator	300:313	a co-regulator of transcription	300:330	Using a proteomic approach, we identified Host Cell Factor-1 (HCF1), a co-regulator of transcription, and O-GlcNAc transferase (OGT), the enzyme that mediates protein O-GlcNAcylation, as cellular partners of Nrf1a, an isoform of Nrf1.
28625484	2	4	theme	Cell	278:281	arg1	HCF1					293:296	HCF1	293:296	HCF1	293:296	Using a proteomic approach, we identified Host Cell Factor-1 (HCF1), a co-regulator of transcription, and O-GlcNAc transferase (OGT), the enzyme that mediates protein O-GlcNAcylation, as cellular partners of Nrf1a, an isoform of Nrf1.
28625484	4	5	theme	protein	648:654	arg1	stability					656:664	increased Nrf1a protein stability	632:664	increased Nrf1a protein stability	632:664	Overexpression of HCF1 and OGT leads to increased Nrf1a protein stability.
28625484	4	6	theme	Nrf1a	642:646	arg1	stability					656:664	increased Nrf1a protein stability	632:664	increased Nrf1a protein stability	632:664	Overexpression of HCF1 and OGT leads to increased Nrf1a protein stability.
28625484	2	7	theme	Host	273:276	arg1	transferase					346:356	O-GlcNAc transferase	337:356	O-GlcNAc transferase (OGT)	337:362	Using a proteomic approach, we identified Host Cell Factor-1 (HCF1), a co-regulator of transcription, and O-GlcNAc transferase (OGT), the enzyme that mediates protein O-GlcNAcylation, as cellular partners of Nrf1a, an isoform of Nrf1.
28625484	2	7	theme	Host	273:276	arg1	partners					427:434	cellular partners	418:434	cellular partners of Nrf1a, an isoform of Nrf1	418:463	Using a proteomic approach, we identified Host Cell Factor-1 (HCF1), a co-regulator of transcription, and O-GlcNAc transferase (OGT), the enzyme that mediates protein O-GlcNAcylation, as cellular partners of Nrf1a, an isoform of Nrf1.
28625484	2	7	theme	Host	273:276	arg1	Factor-1					283:290	Host Cell Factor-1	273:290	Host Cell Factor-1 (HCF1)	273:297	Using a proteomic approach, we identified Host Cell Factor-1 (HCF1), a co-regulator of transcription, and O-GlcNAc transferase (OGT), the enzyme that mediates protein O-GlcNAcylation, as cellular partners of Nrf1a, an isoform of Nrf1.
28625484	2	7	theme	Host	273:276	arg1	co-regulator					302:313	a co-regulator	300:313	a co-regulator of transcription	300:330	Using a proteomic approach, we identified Host Cell Factor-1 (HCF1), a co-regulator of transcription, and O-GlcNAc transferase (OGT), the enzyme that mediates protein O-GlcNAcylation, as cellular partners of Nrf1a, an isoform of Nrf1.
28625484	2	7	theme	Host	273:276	arg1	HCF1					293:296	HCF1	293:296	HCF1	293:296	Using a proteomic approach, we identified Host Cell Factor-1 (HCF1), a co-regulator of transcription, and O-GlcNAc transferase (OGT), the enzyme that mediates protein O-GlcNAcylation, as cellular partners of Nrf1a, an isoform of Nrf1.
28625484	6	8	with	treatment	814:822	arg1	PUGNAc					829:834	PUGNAc	829:834	PUGNAc	829:834	Transcriptional activation by Nrf1a is increased by OGT overexpression and treatment with PUGNAc.
28625484	2	9	theme	Nrf1	460:463	arg1	isoform					449:455	an isoform	446:455	an isoform of Nrf1	446:463	Using a proteomic approach, we identified Host Cell Factor-1 (HCF1), a co-regulator of transcription, and O-GlcNAc transferase (OGT), the enzyme that mediates protein O-GlcNAcylation, as cellular partners of Nrf1a, an isoform of Nrf1.
28625484	2	9	theme	Nrf1	460:463	arg1	Nrf1a					439:443	Nrf1a	439:443	Nrf1a	439:443	Using a proteomic approach, we identified Host Cell Factor-1 (HCF1), a co-regulator of transcription, and O-GlcNAc transferase (OGT), the enzyme that mediates protein O-GlcNAcylation, as cellular partners of Nrf1a, an isoform of Nrf1.
28625484	6	10	theme	Transcriptional	739:753	arg1	activation					755:764	Transcriptional activation	739:764	Transcriptional activation by Nrf1a	739:773	Transcriptional activation by Nrf1a is increased by OGT overexpression and treatment with PUGNAc.
28625484	0	11	theme	factor-erythroid-2	8:25	arg1	Nrf1					59:62	Nrf1	59:62	Nrf1	59:62	Nuclear factor-erythroid-2 related transcription factor-1 (Nrf1) is regulated by O-GlcNAc transferase.
28625484	0	11	theme	factor-erythroid-2	8:25	arg1	factor-1					49:56	Nuclear factor-erythroid-2 related transcription factor-1	0:56	Nuclear factor-erythroid-2 related transcription factor-1 (Nrf1)	0:63	Nuclear factor-erythroid-2 related transcription factor-1 (Nrf1) is regulated by O-GlcNAc transferase.
28625484	3	12	theme	binding	518:524	arg1	HBM					533:535	HBM	533:535	HBM	533:535	Nrf1a directly interacts with HCF1 through the HCF1 binding motif (HBM), while interaction with OGT is mediated through HCF1.
28625484	3	12	theme	binding	518:524	arg1	motif					526:530	the HCF1 binding motif	509:530	the HCF1 binding motif (HBM)	509:536	Nrf1a directly interacts with HCF1 through the HCF1 binding motif (HBM), while interaction with OGT is mediated through HCF1.
28625484	4	13	theme	HCF1	610:613	arg1	Overexpression					592:605	Overexpression	592:605	Overexpression of HCF1 and OGT	592:621	Overexpression of HCF1 and OGT leads to increased Nrf1a protein stability.
28625484	0	14	theme	Nuclear	0:6	arg1	Nrf1					59:62	Nrf1	59:62	Nrf1	59:62	Nuclear factor-erythroid-2 related transcription factor-1 (Nrf1) is regulated by O-GlcNAc transferase.
28625484	0	14	theme	Nuclear	0:6	arg1	factor-1					49:56	Nuclear factor-erythroid-2 related transcription factor-1	0:56	Nuclear factor-erythroid-2 related transcription factor-1 (Nrf1)	0:63	Nuclear factor-erythroid-2 related transcription factor-1 (Nrf1) is regulated by O-GlcNAc transferase.
28625484	1	15	theme	critical	181:188	arg1	role					190:193	a critical role	179:193	a critical role	179:193	The Nrf1 (Nuclear factor E2-related factor 1) transcription factor performs a critical role in regulating cellular homeostasis.
28625484	0	16	theme	transcription	35:47	arg1	Nrf1					59:62	Nrf1	59:62	Nrf1	59:62	Nuclear factor-erythroid-2 related transcription factor-1 (Nrf1) is regulated by O-GlcNAc transferase.
28625484	0	16	theme	transcription	35:47	arg1	factor-1					49:56	Nuclear factor-erythroid-2 related transcription factor-1	0:56	Nuclear factor-erythroid-2 related transcription factor-1 (Nrf1)	0:63	Nuclear factor-erythroid-2 related transcription factor-1 (Nrf1) is regulated by O-GlcNAc transferase.
28625484	2	17	theme	protein	390:396	arg1	O-GlcNAcylation					398:412	protein O-GlcNAcylation	390:412	protein O-GlcNAcylation	390:412	Using a proteomic approach, we identified Host Cell Factor-1 (HCF1), a co-regulator of transcription, and O-GlcNAc transferase (OGT), the enzyme that mediates protein O-GlcNAcylation, as cellular partners of Nrf1a, an isoform of Nrf1.
28625484	3	18	theme	HCF1	513:516	arg1	HBM					533:535	HBM	533:535	HBM	533:535	Nrf1a directly interacts with HCF1 through the HCF1 binding motif (HBM), while interaction with OGT is mediated through HCF1.
28625484	3	18	theme	HCF1	513:516	arg1	motif					526:530	the HCF1 binding motif	509:530	the HCF1 binding motif (HBM)	509:536	Nrf1a directly interacts with HCF1 through the HCF1 binding motif (HBM), while interaction with OGT is mediated through HCF1.
28625484	2	19	theme	Nrf1a	439:443	arg1	partners					427:434	cellular partners	418:434	cellular partners of Nrf1a, an isoform of Nrf1	418:463	Using a proteomic approach, we identified Host Cell Factor-1 (HCF1), a co-regulator of transcription, and O-GlcNAc transferase (OGT), the enzyme that mediates protein O-GlcNAcylation, as cellular partners of Nrf1a, an isoform of Nrf1.
28625484	2	19	theme	Nrf1a	439:443	arg1	Factor-1					283:290	Host Cell Factor-1	273:290	Host Cell Factor-1 (HCF1)	273:297	Using a proteomic approach, we identified Host Cell Factor-1 (HCF1), a co-regulator of transcription, and O-GlcNAc transferase (OGT), the enzyme that mediates protein O-GlcNAcylation, as cellular partners of Nrf1a, an isoform of Nrf1.
28625484	2	19	theme	Nrf1a	439:443	arg1	co-regulator					302:313	a co-regulator	300:313	a co-regulator of transcription	300:330	Using a proteomic approach, we identified Host Cell Factor-1 (HCF1), a co-regulator of transcription, and O-GlcNAc transferase (OGT), the enzyme that mediates protein O-GlcNAcylation, as cellular partners of Nrf1a, an isoform of Nrf1.
28625484	2	19	theme	Nrf1a	439:443	arg1	transferase					346:356	O-GlcNAc transferase	337:356	O-GlcNAc transferase (OGT)	337:362	Using a proteomic approach, we identified Host Cell Factor-1 (HCF1), a co-regulator of transcription, and O-GlcNAc transferase (OGT), the enzyme that mediates protein O-GlcNAcylation, as cellular partners of Nrf1a, an isoform of Nrf1.
28625484	4	20	theme	increased	632:640	arg1	stability					656:664	increased Nrf1a protein stability	632:664	increased Nrf1a protein stability	632:664	Overexpression of HCF1 and OGT leads to increased Nrf1a protein stability.
28625484	6	21	with	overexpression	795:808	arg1	PUGNAc					829:834	PUGNAc	829:834	PUGNAc	829:834	Transcriptional activation by Nrf1a is increased by OGT overexpression and treatment with PUGNAc.
28625484	0	22	theme	related	27:33	arg1	Nrf1					59:62	Nrf1	59:62	Nrf1	59:62	Nuclear factor-erythroid-2 related transcription factor-1 (Nrf1) is regulated by O-GlcNAc transferase.
28625484	0	22	theme	related	27:33	arg1	factor-1					49:56	Nuclear factor-erythroid-2 related transcription factor-1	0:56	Nuclear factor-erythroid-2 related transcription factor-1 (Nrf1)	0:63	Nuclear factor-erythroid-2 related transcription factor-1 (Nrf1) is regulated by O-GlcNAc transferase.
28625484	5	23	theme	Nrf1a	732:736	arg1	ubiquitination					698:711	ubiquitination	698:711	ubiquitination	698:711	Addition of O-GlcNAc decreases ubiquitination and degradation of Nrf1a.
28625484	5	23	theme	Nrf1a	732:736	arg1	degradation					717:727	degradation	717:727	degradation	717:727	Addition of O-GlcNAc decreases ubiquitination and degradation of Nrf1a.
28625484	1	24	theme	cellular	209:216	arg1	homeostasis					218:228	cellular homeostasis	209:228	cellular homeostasis	209:228	The Nrf1 (Nuclear factor E2-related factor 1) transcription factor performs a critical role in regulating cellular homeostasis.
28625484	1	25	dep	Nrf1	107:110	arg1	factor					163:168	transcription factor	149:168	The Nrf1 (Nuclear factor E2-related factor 1) transcription factor	103:168	The Nrf1 (Nuclear factor E2-related factor 1) transcription factor performs a critical role in regulating cellular homeostasis.
28625484	1	25	dep	Nrf1	107:110	arg1	factor					139:144	Nuclear factor E2-related factor 1	113:146	The Nrf1 (Nuclear factor E2-related factor 1) transcription factor	103:168	The Nrf1 (Nuclear factor E2-related factor 1) transcription factor performs a critical role in regulating cellular homeostasis.
28625484	2	26	theme	transcription	318:330	arg1	HCF1					293:296	HCF1	293:296	HCF1	293:296	Using a proteomic approach, we identified Host Cell Factor-1 (HCF1), a co-regulator of transcription, and O-GlcNAc transferase (OGT), the enzyme that mediates protein O-GlcNAcylation, as cellular partners of Nrf1a, an isoform of Nrf1.
28625484	2	26	theme	transcription	318:330	arg1	transferase					346:356	O-GlcNAc transferase	337:356	O-GlcNAc transferase (OGT)	337:362	Using a proteomic approach, we identified Host Cell Factor-1 (HCF1), a co-regulator of transcription, and O-GlcNAc transferase (OGT), the enzyme that mediates protein O-GlcNAcylation, as cellular partners of Nrf1a, an isoform of Nrf1.
28625484	2	26	theme	transcription	318:330	arg1	enzyme					369:374	the enzyme	365:374	the enzyme that mediates protein O-GlcNAcylation	365:412	Using a proteomic approach, we identified Host Cell Factor-1 (HCF1), a co-regulator of transcription, and O-GlcNAc transferase (OGT), the enzyme that mediates protein O-GlcNAcylation, as cellular partners of Nrf1a, an isoform of Nrf1.
28625484	2	26	theme	transcription	318:330	arg1	Factor-1					283:290	Host Cell Factor-1	273:290	Host Cell Factor-1 (HCF1)	273:297	Using a proteomic approach, we identified Host Cell Factor-1 (HCF1), a co-regulator of transcription, and O-GlcNAc transferase (OGT), the enzyme that mediates protein O-GlcNAcylation, as cellular partners of Nrf1a, an isoform of Nrf1.
28625484	2	26	theme	transcription	318:330	arg1	co-regulator					302:313	a co-regulator	300:313	a co-regulator of transcription	300:330	Using a proteomic approach, we identified Host Cell Factor-1 (HCF1), a co-regulator of transcription, and O-GlcNAc transferase (OGT), the enzyme that mediates protein O-GlcNAcylation, as cellular partners of Nrf1a, an isoform of Nrf1.
28625484	2	26	theme	transcription	318:330	arg1	partners					427:434	cellular partners	418:434	cellular partners of Nrf1a, an isoform of Nrf1	418:463	Using a proteomic approach, we identified Host Cell Factor-1 (HCF1), a co-regulator of transcription, and O-GlcNAc transferase (OGT), the enzyme that mediates protein O-GlcNAcylation, as cellular partners of Nrf1a, an isoform of Nrf1.
28625484	2	26	theme	transcription	318:330	arg1	OGT					359:361	OGT	359:361	OGT	359:361	Using a proteomic approach, we identified Host Cell Factor-1 (HCF1), a co-regulator of transcription, and O-GlcNAc transferase (OGT), the enzyme that mediates protein O-GlcNAcylation, as cellular partners of Nrf1a, an isoform of Nrf1.
28625484	2	27	theme	cellular	418:425	arg1	partners					427:434	cellular partners	418:434	cellular partners of Nrf1a, an isoform of Nrf1	418:463	Using a proteomic approach, we identified Host Cell Factor-1 (HCF1), a co-regulator of transcription, and O-GlcNAc transferase (OGT), the enzyme that mediates protein O-GlcNAcylation, as cellular partners of Nrf1a, an isoform of Nrf1.
28625484	2	27	theme	cellular	418:425	arg1	Factor-1					283:290	Host Cell Factor-1	273:290	Host Cell Factor-1 (HCF1)	273:297	Using a proteomic approach, we identified Host Cell Factor-1 (HCF1), a co-regulator of transcription, and O-GlcNAc transferase (OGT), the enzyme that mediates protein O-GlcNAcylation, as cellular partners of Nrf1a, an isoform of Nrf1.
28625484	2	27	theme	cellular	418:425	arg1	co-regulator					302:313	a co-regulator	300:313	a co-regulator of transcription	300:330	Using a proteomic approach, we identified Host Cell Factor-1 (HCF1), a co-regulator of transcription, and O-GlcNAc transferase (OGT), the enzyme that mediates protein O-GlcNAcylation, as cellular partners of Nrf1a, an isoform of Nrf1.
28625484	2	27	theme	cellular	418:425	arg1	transferase					346:356	O-GlcNAc transferase	337:356	O-GlcNAc transferase (OGT)	337:362	Using a proteomic approach, we identified Host Cell Factor-1 (HCF1), a co-regulator of transcription, and O-GlcNAc transferase (OGT), the enzyme that mediates protein O-GlcNAcylation, as cellular partners of Nrf1a, an isoform of Nrf1.
28625484	1	28	theme	Nuclear	113:119	arg1	factor					139:144	Nuclear factor E2-related factor 1	113:146	The Nrf1 (Nuclear factor E2-related factor 1) transcription factor	103:168	The Nrf1 (Nuclear factor E2-related factor 1) transcription factor performs a critical role in regulating cellular homeostasis.
28625484	6	29	theme	OGT	791:793	arg1	overexpression					795:808	OGT overexpression	791:808	OGT overexpression	791:808	Transcriptional activation by Nrf1a is increased by OGT overexpression and treatment with PUGNAc.
28625484	1	30	theme	factor	121:126	arg1	factor					139:144	Nuclear factor E2-related factor 1	113:146	The Nrf1 (Nuclear factor E2-related factor 1) transcription factor	103:168	The Nrf1 (Nuclear factor E2-related factor 1) transcription factor performs a critical role in regulating cellular homeostasis.
28625484	1	31	theme	E2-related	128:137	arg1	factor					139:144	Nuclear factor E2-related factor 1	113:146	The Nrf1 (Nuclear factor E2-related factor 1) transcription factor	103:168	The Nrf1 (Nuclear factor E2-related factor 1) transcription factor performs a critical role in regulating cellular homeostasis.
28625484	4	32	theme	OGT	619:621	arg1	Overexpression					592:605	Overexpression	592:605	Overexpression of HCF1 and OGT	592:621	Overexpression of HCF1 and OGT leads to increased Nrf1a protein stability.
28625484	3	33	with	interaction	545:555	arg1	OGT					562:564	OGT	562:564	OGT	562:564	Nrf1a directly interacts with HCF1 through the HCF1 binding motif (HBM), while interaction with OGT is mediated through HCF1.
28625484	2	34	theme	proteomic	239:247	arg1	approach					249:256	a proteomic approach	237:256	a proteomic approach	237:256	Using a proteomic approach, we identified Host Cell Factor-1 (HCF1), a co-regulator of transcription, and O-GlcNAc transferase (OGT), the enzyme that mediates protein O-GlcNAcylation, as cellular partners of Nrf1a, an isoform of Nrf1.
28625484	2	35	theme	O-GlcNAc	337:344	arg1	transferase					346:356	O-GlcNAc transferase	337:356	O-GlcNAc transferase (OGT)	337:362	Using a proteomic approach, we identified Host Cell Factor-1 (HCF1), a co-regulator of transcription, and O-GlcNAc transferase (OGT), the enzyme that mediates protein O-GlcNAcylation, as cellular partners of Nrf1a, an isoform of Nrf1.
28625484	2	35	theme	O-GlcNAc	337:344	arg1	enzyme					369:374	the enzyme	365:374	the enzyme that mediates protein O-GlcNAcylation	365:412	Using a proteomic approach, we identified Host Cell Factor-1 (HCF1), a co-regulator of transcription, and O-GlcNAc transferase (OGT), the enzyme that mediates protein O-GlcNAcylation, as cellular partners of Nrf1a, an isoform of Nrf1.
28625484	2	35	theme	O-GlcNAc	337:344	arg1	Factor-1					283:290	Host Cell Factor-1	273:290	Host Cell Factor-1 (HCF1)	273:297	Using a proteomic approach, we identified Host Cell Factor-1 (HCF1), a co-regulator of transcription, and O-GlcNAc transferase (OGT), the enzyme that mediates protein O-GlcNAcylation, as cellular partners of Nrf1a, an isoform of Nrf1.
28625484	2	35	theme	O-GlcNAc	337:344	arg1	co-regulator					302:313	a co-regulator	300:313	a co-regulator of transcription	300:330	Using a proteomic approach, we identified Host Cell Factor-1 (HCF1), a co-regulator of transcription, and O-GlcNAc transferase (OGT), the enzyme that mediates protein O-GlcNAcylation, as cellular partners of Nrf1a, an isoform of Nrf1.
28625484	2	35	theme	O-GlcNAc	337:344	arg1	partners					427:434	cellular partners	418:434	cellular partners of Nrf1a, an isoform of Nrf1	418:463	Using a proteomic approach, we identified Host Cell Factor-1 (HCF1), a co-regulator of transcription, and O-GlcNAc transferase (OGT), the enzyme that mediates protein O-GlcNAcylation, as cellular partners of Nrf1a, an isoform of Nrf1.
28625484	2	35	theme	O-GlcNAc	337:344	arg1	OGT					359:361	OGT	359:361	OGT	359:361	Using a proteomic approach, we identified Host Cell Factor-1 (HCF1), a co-regulator of transcription, and O-GlcNAc transferase (OGT), the enzyme that mediates protein O-GlcNAcylation, as cellular partners of Nrf1a, an isoform of Nrf1.
28797110	5	0	theme	GNB2L1	755:760	arg1	function					743:750	the function	739:750	the function of GNB2L1 and its O-GlcNAcylation on gastric cancer metastasis during chemoresistance	739:836	Next, we investigate the function of GNB2L1 and its O-GlcNAcylation on gastric cancer metastasis during chemoresistance, and confirmed Ser124 as the major O-GlcNAcylation site on GNB2L1 that regulated its function on metastasis.
28797110	7	1	theme	gastric	1269:1275	arg1	cancer					1277:1282	gastric cancer	1269:1282	gastric cancer	1269:1282	In summary, this study indicated that GNB2L1 and its O-GlcNAcylation regulated metastasis via modulating the translation of EMT-related proteins in the chemoresistance of gastric cancer.
28797110	3	2	theme	mRNA	501:504	arg1	levels					506:511	mRNA levels	501:511	the decrease of GNB2L1 in protein levels instead of mRNA levels	449:511	In the present study, we found that GNB2L1 was downregulated in chemoresistant patients of gastric cancer, and observed the decrease of GNB2L1 in protein levels instead of mRNA levels in different chemoresistant gastric cancer cell lines.
28797110	7	3	theme	EMT-related	1222:1232	arg1	proteins					1234:1241	EMT-related proteins	1222:1241	EMT-related proteins	1222:1241	In summary, this study indicated that GNB2L1 and its O-GlcNAcylation regulated metastasis via modulating the translation of EMT-related proteins in the chemoresistance of gastric cancer.
28797110	5	4	from	O-GlcNAcylation	770:784	arg1	metastasis					804:813	gastric cancer metastasis	789:813	gastric cancer metastasis	789:813	Next, we investigate the function of GNB2L1 and its O-GlcNAcylation on gastric cancer metastasis during chemoresistance, and confirmed Ser124 as the major O-GlcNAcylation site on GNB2L1 that regulated its function on metastasis.
28797110	3	5	theme	gastric	541:547	arg1	lines					561:565	different chemoresistant gastric cancer cell lines	516:565	different chemoresistant gastric cancer cell lines	516:565	In the present study, we found that GNB2L1 was downregulated in chemoresistant patients of gastric cancer, and observed the decrease of GNB2L1 in protein levels instead of mRNA levels in different chemoresistant gastric cancer cell lines.
28797110	7	6	theme	proteins	1234:1241	arg1	translation					1207:1217	the translation	1203:1217	the translation of EMT-related proteins in the chemoresistance of gastric cancer	1203:1282	In summary, this study indicated that GNB2L1 and its O-GlcNAcylation regulated metastasis via modulating the translation of EMT-related proteins in the chemoresistance of gastric cancer.
28797110	2	7	theme	cancer	295:300	arg1	chemoresistance					268:282	chemoresistance	268:282	chemoresistance of gastric cancer	268:300	However, the roles of GNB2L1 in chemoresistance of gastric cancer has never been determined.
28797110	5	8	from	site	889:892	arg1	GNB2L1					897:902	GNB2L1	897:902	GNB2L1 that regulated its function on metastasis	897:944	Next, we investigate the function of GNB2L1 and its O-GlcNAcylation on gastric cancer metastasis during chemoresistance, and confirmed Ser124 as the major O-GlcNAcylation site on GNB2L1 that regulated its function on metastasis.
28797110	3	9	theme	cancer	549:554	arg1	lines					561:565	different chemoresistant gastric cancer cell lines	516:565	different chemoresistant gastric cancer cell lines	516:565	In the present study, we found that GNB2L1 was downregulated in chemoresistant patients of gastric cancer, and observed the decrease of GNB2L1 in protein levels instead of mRNA levels in different chemoresistant gastric cancer cell lines.
28797110	4	10	from	OGT	681:683	arg1	patients					708:715	patients	708:715	patients	708:715	Further we proved that this downregulation of GNB2L1 was resulted from its elevated O-GlcNAcylation catalyzed by OGT in both cell lines and patients.
28797110	4	10	from	OGT	681:683	arg1	lines					698:702	cell lines	693:702	cell lines	693:702	Further we proved that this downregulation of GNB2L1 was resulted from its elevated O-GlcNAcylation catalyzed by OGT in both cell lines and patients.
28797110	0	11	theme	cancer	135:140	arg1	chemoresistance					108:122	the chemoresistance	104:122	the chemoresistance of gastric cancer	104:140	GNB2L1 and its O-GlcNAcylation regulates metastasis via modulating epithelial-mesenchymal transition in the chemoresistance of gastric cancer.
28797110	3	12	theme	GNB2L1	465:470	arg1	decrease					453:460	the decrease	449:460	the decrease of GNB2L1 in protein levels instead of mRNA levels	449:511	In the present study, we found that GNB2L1 was downregulated in chemoresistant patients of gastric cancer, and observed the decrease of GNB2L1 in protein levels instead of mRNA levels in different chemoresistant gastric cancer cell lines.
28797110	2	13	theme	gastric	287:293	arg1	cancer					295:300	gastric cancer	287:300	gastric cancer	287:300	However, the roles of GNB2L1 in chemoresistance of gastric cancer has never been determined.
28797110	5	14	theme	major	867:871	arg1	site					889:892	the major O-GlcNAcylation site	863:892	the major O-GlcNAcylation site on GNB2L1 that regulated its function on metastasis	863:944	Next, we investigate the function of GNB2L1 and its O-GlcNAcylation on gastric cancer metastasis during chemoresistance, and confirmed Ser124 as the major O-GlcNAcylation site on GNB2L1 that regulated its function on metastasis.
28797110	5	14	theme	major	867:871	arg1	Ser124					853:858	Ser124	853:858	Ser124	853:858	Next, we investigate the function of GNB2L1 and its O-GlcNAcylation on gastric cancer metastasis during chemoresistance, and confirmed Ser124 as the major O-GlcNAcylation site on GNB2L1 that regulated its function on metastasis.
28797110	0	15	theme	gastric	127:133	arg1	cancer					135:140	gastric cancer	127:140	gastric cancer	127:140	GNB2L1 and its O-GlcNAcylation regulates metastasis via modulating epithelial-mesenchymal transition in the chemoresistance of gastric cancer.
28797110	5	16	from	function	923:930	arg1	metastasis					935:944	metastasis	935:944	metastasis	935:944	Next, we investigate the function of GNB2L1 and its O-GlcNAcylation on gastric cancer metastasis during chemoresistance, and confirmed Ser124 as the major O-GlcNAcylation site on GNB2L1 that regulated its function on metastasis.
28797110	3	17	theme	chemoresistant	526:539	arg1	lines					561:565	different chemoresistant gastric cancer cell lines	516:565	different chemoresistant gastric cancer cell lines	516:565	In the present study, we found that GNB2L1 was downregulated in chemoresistant patients of gastric cancer, and observed the decrease of GNB2L1 in protein levels instead of mRNA levels in different chemoresistant gastric cancer cell lines.
28797110	2	18	from	roles	249:253	arg1	chemoresistance					268:282	chemoresistance	268:282	chemoresistance of gastric cancer	268:300	However, the roles of GNB2L1 in chemoresistance of gastric cancer has never been determined.
28797110	6	19	theme	chemoresistance	1081:1095	arg1	process					1070:1076	the process	1066:1076	the process of chemoresistance	1066:1095	Furthermore, our data demonstrated that GNB2L1 modulated EMT via regulating the translation of EMT-related proteins in the process of chemoresistance.
28797110	5	20	theme	cancer	797:802	arg1	metastasis					804:813	gastric cancer metastasis	789:813	gastric cancer metastasis	789:813	Next, we investigate the function of GNB2L1 and its O-GlcNAcylation on gastric cancer metastasis during chemoresistance, and confirmed Ser124 as the major O-GlcNAcylation site on GNB2L1 that regulated its function on metastasis.
28797110	5	21	from	metastasis	804:813	arg1	function					743:750	the function	739:750	the function of GNB2L1 and its O-GlcNAcylation on gastric cancer metastasis during chemoresistance	739:836	Next, we investigate the function of GNB2L1 and its O-GlcNAcylation on gastric cancer metastasis during chemoresistance, and confirmed Ser124 as the major O-GlcNAcylation site on GNB2L1 that regulated its function on metastasis.
28797110	3	22	theme	cancer	428:433	arg1	patients					408:415	chemoresistant patients	393:415	chemoresistant patients of gastric cancer	393:433	In the present study, we found that GNB2L1 was downregulated in chemoresistant patients of gastric cancer, and observed the decrease of GNB2L1 in protein levels instead of mRNA levels in different chemoresistant gastric cancer cell lines.
28797110	5	23	theme	O-GlcNAcylation	873:887	arg1	site					889:892	the major O-GlcNAcylation site	863:892	the major O-GlcNAcylation site on GNB2L1 that regulated its function on metastasis	863:944	Next, we investigate the function of GNB2L1 and its O-GlcNAcylation on gastric cancer metastasis during chemoresistance, and confirmed Ser124 as the major O-GlcNAcylation site on GNB2L1 that regulated its function on metastasis.
28797110	5	23	theme	O-GlcNAcylation	873:887	arg1	Ser124					853:858	Ser124	853:858	Ser124	853:858	Next, we investigate the function of GNB2L1 and its O-GlcNAcylation on gastric cancer metastasis during chemoresistance, and confirmed Ser124 as the major O-GlcNAcylation site on GNB2L1 that regulated its function on metastasis.
28797110	3	24	theme	cell	556:559	arg1	lines					561:565	different chemoresistant gastric cancer cell lines	516:565	different chemoresistant gastric cancer cell lines	516:565	In the present study, we found that GNB2L1 was downregulated in chemoresistant patients of gastric cancer, and observed the decrease of GNB2L1 in protein levels instead of mRNA levels in different chemoresistant gastric cancer cell lines.
28797110	1	25	theme	gastric	209:215	arg1	metastasis					224:233	gastric cancer metastasis	209:233	gastric cancer metastasis	209:233	GNB2L1 and its O-GlcNAcylation has been reported to play roles in gastric cancer metastasis.
28797110	3	26	theme	different	516:524	arg1	lines					561:565	different chemoresistant gastric cancer cell lines	516:565	different chemoresistant gastric cancer cell lines	516:565	In the present study, we found that GNB2L1 was downregulated in chemoresistant patients of gastric cancer, and observed the decrease of GNB2L1 in protein levels instead of mRNA levels in different chemoresistant gastric cancer cell lines.
28797110	7	27	from	translation	1207:1217	arg1	chemoresistance					1250:1264	the chemoresistance	1246:1264	the chemoresistance of gastric cancer	1246:1282	In summary, this study indicated that GNB2L1 and its O-GlcNAcylation regulated metastasis via modulating the translation of EMT-related proteins in the chemoresistance of gastric cancer.
28797110	4	28	theme	cell	693:696	arg1	lines					698:702	cell lines	693:702	cell lines	693:702	Further we proved that this downregulation of GNB2L1 was resulted from its elevated O-GlcNAcylation catalyzed by OGT in both cell lines and patients.
28797110	1	29	theme	cancer	217:222	arg1	metastasis					224:233	gastric cancer metastasis	209:233	gastric cancer metastasis	209:233	GNB2L1 and its O-GlcNAcylation has been reported to play roles in gastric cancer metastasis.
28797110	6	30	from	translation	1027:1037	arg1	process					1070:1076	the process	1066:1076	the process of chemoresistance	1066:1095	Furthermore, our data demonstrated that GNB2L1 modulated EMT via regulating the translation of EMT-related proteins in the process of chemoresistance.
28797110	6	31	theme	proteins	1054:1061	arg1	translation					1027:1037	the translation	1023:1037	the translation of EMT-related proteins in the process of chemoresistance	1023:1095	Furthermore, our data demonstrated that GNB2L1 modulated EMT via regulating the translation of EMT-related proteins in the process of chemoresistance.
28797110	4	32	theme	elevated	643:650	arg1	O-GlcNAcylation					652:666	its elevated O-GlcNAcylation	639:666	its elevated O-GlcNAcylation catalyzed by OGT in both cell lines and patients	639:715	Further we proved that this downregulation of GNB2L1 was resulted from its elevated O-GlcNAcylation catalyzed by OGT in both cell lines and patients.
28797110	3	33	theme	gastric	420:426	arg1	cancer					428:433	gastric cancer	420:433	gastric cancer	420:433	In the present study, we found that GNB2L1 was downregulated in chemoresistant patients of gastric cancer, and observed the decrease of GNB2L1 in protein levels instead of mRNA levels in different chemoresistant gastric cancer cell lines.
28797110	5	34	theme	O-GlcNAcylation	770:784	arg1	function					743:750	the function	739:750	the function of GNB2L1 and its O-GlcNAcylation on gastric cancer metastasis during chemoresistance	739:836	Next, we investigate the function of GNB2L1 and its O-GlcNAcylation on gastric cancer metastasis during chemoresistance, and confirmed Ser124 as the major O-GlcNAcylation site on GNB2L1 that regulated its function on metastasis.
28797110	6	35	theme	EMT-related	1042:1052	arg1	proteins					1054:1061	EMT-related proteins	1042:1061	EMT-related proteins	1042:1061	Furthermore, our data demonstrated that GNB2L1 modulated EMT via regulating the translation of EMT-related proteins in the process of chemoresistance.
28797110	3	36	theme	chemoresistant	393:406	arg1	patients					408:415	chemoresistant patients	393:415	chemoresistant patients of gastric cancer	393:433	In the present study, we found that GNB2L1 was downregulated in chemoresistant patients of gastric cancer, and observed the decrease of GNB2L1 in protein levels instead of mRNA levels in different chemoresistant gastric cancer cell lines.
28797110	7	37	theme	cancer	1277:1282	arg1	chemoresistance					1250:1264	the chemoresistance	1246:1264	the chemoresistance of gastric cancer	1246:1282	In summary, this study indicated that GNB2L1 and its O-GlcNAcylation regulated metastasis via modulating the translation of EMT-related proteins in the chemoresistance of gastric cancer.
28797110	3	38	from	decrease	453:460	arg1	levels					483:488	protein levels	475:488	protein levels	475:488	In the present study, we found that GNB2L1 was downregulated in chemoresistant patients of gastric cancer, and observed the decrease of GNB2L1 in protein levels instead of mRNA levels in different chemoresistant gastric cancer cell lines.
28797110	5	39	theme	gastric	789:795	arg1	metastasis					804:813	gastric cancer metastasis	789:813	gastric cancer metastasis	789:813	Next, we investigate the function of GNB2L1 and its O-GlcNAcylation on gastric cancer metastasis during chemoresistance, and confirmed Ser124 as the major O-GlcNAcylation site on GNB2L1 that regulated its function on metastasis.
28797110	5	40	from	GNB2L1	755:760	arg1	metastasis					804:813	gastric cancer metastasis	789:813	gastric cancer metastasis	789:813	Next, we investigate the function of GNB2L1 and its O-GlcNAcylation on gastric cancer metastasis during chemoresistance, and confirmed Ser124 as the major O-GlcNAcylation site on GNB2L1 that regulated its function on metastasis.
28797110	5	41	from	function	743:750	arg1	metastasis					804:813	gastric cancer metastasis	789:813	gastric cancer metastasis	789:813	Next, we investigate the function of GNB2L1 and its O-GlcNAcylation on gastric cancer metastasis during chemoresistance, and confirmed Ser124 as the major O-GlcNAcylation site on GNB2L1 that regulated its function on metastasis.
28797110	3	42	theme	protein	475:481	arg1	levels					483:488	protein levels	475:488	protein levels	475:488	In the present study, we found that GNB2L1 was downregulated in chemoresistant patients of gastric cancer, and observed the decrease of GNB2L1 in protein levels instead of mRNA levels in different chemoresistant gastric cancer cell lines.
28797110	3	43	theme	present	336:342	arg1	study					344:348	the present study	332:348	the present study	332:348	In the present study, we found that GNB2L1 was downregulated in chemoresistant patients of gastric cancer, and observed the decrease of GNB2L1 in protein levels instead of mRNA levels in different chemoresistant gastric cancer cell lines.
28797110	2	44	theme	GNB2L1	258:263	arg1	roles					249:253	the roles	245:253	the roles of GNB2L1 in chemoresistance of gastric cancer	245:300	However, the roles of GNB2L1 in chemoresistance of gastric cancer has never been determined.
28797110	0	45	theme	epithelial-mesenchymal	67:88	arg1	transition					90:99	epithelial-mesenchymal transition	67:99	epithelial-mesenchymal transition	67:99	GNB2L1 and its O-GlcNAcylation regulates metastasis via modulating epithelial-mesenchymal transition in the chemoresistance of gastric cancer.
28797110	4	46	theme	GNB2L1	614:619	arg1	downregulation					596:609	this downregulation	591:609	this downregulation of GNB2L1	591:619	Further we proved that this downregulation of GNB2L1 was resulted from its elevated O-GlcNAcylation catalyzed by OGT in both cell lines and patients.
1457969	6	0	theme	4-O-sulphated	1150:1162	arg1	GalNAc					1164:1169	4-O-sulphated GalNAc	1150:1169	4-O-sulphated GalNAc	1150:1169	The Man alpha 1-6 branch displayed structural heterogeneity in the terminal sequence, with chiefly alpha 2-3-sialylated Gal and/or 4-O-sulphated GalNAc.
1457969	8	1	from	presence	1787:1794	arg1	cells					1872:1876	thyrotroph cells	1861:1876	thyrotroph cells	1861:1876	Some interesting structural features, not previously reported for the N-glycans of hTSH, included 3-O-sulphated galactose (SO4-3Gal) and peripheral fucose (Fuc alpha 1-3GlcNAc) in the Man alpha 1-6 branch of some diantennary structures; the former suggests the presence of a hitherto uncharacterized galactose-3-O-sulphotransferase in thyrotroph cells of the human anterior pituitary gland.
1457969	7	2	theme	relative	1176:1183	arg1	oligosaccharides					1231:1246	the two major complete diantennary oligosaccharides	1196:1246	the two major complete diantennary oligosaccharides	1196:1246	The relative amounts of the two major complete diantennary oligosaccharides and their core fucosylation differed according to glycosylation site; the sulphated/sialylated diantennary oligosaccharide was most abundant at the two sites on the alpha-subunit, whereas the disulphated, core-fucosylated oligosaccharide was more plentiful on the beta-subunit.
1457969	7	2	theme	relative	1176:1183	arg1	amounts					1185:1191	The relative amounts	1172:1191	The relative amounts of the two major complete diantennary oligosaccharides and their core fucosylation	1172:1274	The relative amounts of the two major complete diantennary oligosaccharides and their core fucosylation differed according to glycosylation site; the sulphated/sialylated diantennary oligosaccharide was most abundant at the two sites on the alpha-subunit, whereas the disulphated, core-fucosylated oligosaccharide was more plentiful on the beta-subunit.
1457969	7	2	theme	relative	1176:1183	arg1	fucosylation					1263:1274	their core fucosylation	1252:1274	their core fucosylation	1252:1274	The relative amounts of the two major complete diantennary oligosaccharides and their core fucosylation differed according to glycosylation site; the sulphated/sialylated diantennary oligosaccharide was most abundant at the two sites on the alpha-subunit, whereas the disulphated, core-fucosylated oligosaccharide was more plentiful on the beta-subunit.
1457969	4	3	theme	alpha	668:672	arg1	glycopeptides					674:686	hTSH alpha glycopeptides	663:686	hTSH alpha glycopeptides	663:686	The oligosaccharides were liberated from hTSH alpha glycopeptides and from intact hTSH beta by hydrazinolysis, and were fractionated as alditols by anion-exchange and ion-suppression amine-adsorption HPLC preparatory to structural analysis.
1457969	8	4	theme	uncharacterized	1810:1824	arg1	galactose-3-O-sulphotransferase					1826:1856	a hitherto uncharacterized galactose-3-O-sulphotransferase	1799:1856	a hitherto uncharacterized galactose-3-O-sulphotransferase in thyrotroph cells of the human anterior pituitary gland	1799:1914	Some interesting structural features, not previously reported for the N-glycans of hTSH, included 3-O-sulphated galactose (SO4-3Gal) and peripheral fucose (Fuc alpha 1-3GlcNAc) in the Man alpha 1-6 branch of some diantennary structures; the former suggests the presence of a hitherto uncharacterized galactose-3-O-sulphotransferase in thyrotroph cells of the human anterior pituitary gland.
1457969	5	5	theme	complex-type	917:928	arg1	structures					930:939	diantennary complex-type structures	905:939	diantennary complex-type structures	905:939	The N-glycans present on hTSH were mainly diantennary complex-type structures with a common Man alpha 1-3 branch that terminated with 4-O-sulphated GalNAc.
1457969	5	5	theme	complex-type	917:928	arg1	N-glycans					867:875	The N-glycans	863:875	The N-glycans present on hTSH	863:891	The N-glycans present on hTSH were mainly diantennary complex-type structures with a common Man alpha 1-3 branch that terminated with 4-O-sulphated GalNAc.
1457969	3	6	theme	reverse-phase	555:567	arg1	HPLC					569:572	reverse-phase HPLC	555:572	reverse-phase HPLC	555:572	The alpha-subunit was further treated with trypsin which gave two glycopeptides that were subsequently separated by reverse-phase HPLC and identified by amino acid sequence analysis.
1457969	5	7	theme	present	877:883	arg1	N-glycans					867:875	The N-glycans	863:875	The N-glycans present on hTSH	863:891	The N-glycans present on hTSH were mainly diantennary complex-type structures with a common Man alpha 1-3 branch that terminated with 4-O-sulphated GalNAc.
1457969	5	7	theme	present	877:883	arg1	structures					930:939	diantennary complex-type structures	905:939	diantennary complex-type structures	905:939	The N-glycans present on hTSH were mainly diantennary complex-type structures with a common Man alpha 1-3 branch that terminated with 4-O-sulphated GalNAc.
1457969	2	8	theme	purified	262:269	arg1	hTSH					312:315	hTSH	312:315	hTSH	312:315	Highly purified, biologically active human thyrotrophin (hTSH) was dissociated into its subunits hTSH alpha (glycosylated at Asn 52 and Asn 78) and hTSH beta (glycosylated at Asn 23).
1457969	2	8	theme	purified	262:269	arg1	thyrotrophin					298:309	human thyrotrophin	292:309	Highly purified, biologically active human thyrotrophin (hTSH)	255:316	Highly purified, biologically active human thyrotrophin (hTSH) was dissociated into its subunits hTSH alpha (glycosylated at Asn 52 and Asn 78) and hTSH beta (glycosylated at Asn 23).
1457969	1	9	gly	glycosylation	163:175	arg2	thyrotrophin					192:203	human thyrotrophin	186:203	human thyrotrophin	186:203	The asparagine-linked carbohydrate structures at each of the three glycosylation sites of human thyrotrophin were investigated by 400 MHz 1H-NMR spectroscopy.
1457969	1	9	gly	glycosylation	163:175	arg2	sites					177:181	the three glycosylation sites	153:181	the three glycosylation sites of human thyrotrophin	153:203	The asparagine-linked carbohydrate structures at each of the three glycosylation sites of human thyrotrophin were investigated by 400 MHz 1H-NMR spectroscopy.
1457969	1	9	gly	glycosylation	163:175	arg2	three					157:161	three	157:161	three	157:161	The asparagine-linked carbohydrate structures at each of the three glycosylation sites of human thyrotrophin were investigated by 400 MHz 1H-NMR spectroscopy.
1457969	1	9	gly	glycosylation	163:175	arg1	thyrotrophin					192:203	human thyrotrophin	186:203	human thyrotrophin	186:203	The asparagine-linked carbohydrate structures at each of the three glycosylation sites of human thyrotrophin were investigated by 400 MHz 1H-NMR spectroscopy.
1457969	8	10	theme	anterior	1891:1898	arg1	gland					1910:1914	the human anterior pituitary gland	1881:1914	the human anterior pituitary gland	1881:1914	Some interesting structural features, not previously reported for the N-glycans of hTSH, included 3-O-sulphated galactose (SO4-3Gal) and peripheral fucose (Fuc alpha 1-3GlcNAc) in the Man alpha 1-6 branch of some diantennary structures; the former suggests the presence of a hitherto uncharacterized galactose-3-O-sulphotransferase in thyrotroph cells of the human anterior pituitary gland.
1457969	5	11	theme	alpha	959:963	arg1	branch					969:974	a common Man alpha 1-3 branch	946:974	a common Man alpha 1-3 branch that terminated with 4-O-sulphated GalNAc	946:1016	The N-glycans present on hTSH were mainly diantennary complex-type structures with a common Man alpha 1-3 branch that terminated with 4-O-sulphated GalNAc.
1457969	2	12	dep	subunits	343:350	arg1	beta					408:411	hTSH beta	403:411	hTSH beta (glycosylated at Asn 23)	403:436	Highly purified, biologically active human thyrotrophin (hTSH) was dissociated into its subunits hTSH alpha (glycosylated at Asn 52 and Asn 78) and hTSH beta (glycosylated at Asn 23).
1457969	2	12	dep	subunits	343:350	arg1	alpha					357:361	hTSH alpha	352:361	hTSH alpha (glycosylated at Asn 52 and Asn 78)	352:397	Highly purified, biologically active human thyrotrophin (hTSH) was dissociated into its subunits hTSH alpha (glycosylated at Asn 52 and Asn 78) and hTSH beta (glycosylated at Asn 23).
1457969	2	12	dep	subunits	343:350	arg1	subunits					343:350	its subunits	339:350	its subunits hTSH alpha (glycosylated at Asn 52 and Asn 78) and hTSH beta (glycosylated at Asn 23)	339:436	Highly purified, biologically active human thyrotrophin (hTSH) was dissociated into its subunits hTSH alpha (glycosylated at Asn 52 and Asn 78) and hTSH beta (glycosylated at Asn 23).
1457969	2	13	theme	human	292:296	arg1	hTSH					312:315	hTSH	312:315	hTSH	312:315	Highly purified, biologically active human thyrotrophin (hTSH) was dissociated into its subunits hTSH alpha (glycosylated at Asn 52 and Asn 78) and hTSH beta (glycosylated at Asn 23).
1457969	2	13	theme	human	292:296	arg1	thyrotrophin					298:309	human thyrotrophin	292:309	Highly purified, biologically active human thyrotrophin (hTSH)	255:316	Highly purified, biologically active human thyrotrophin (hTSH) was dissociated into its subunits hTSH alpha (glycosylated at Asn 52 and Asn 78) and hTSH beta (glycosylated at Asn 23).
1457969	8	14	theme	gland	1910:1914	arg1	galactose-3-O-sulphotransferase					1826:1856	a hitherto uncharacterized galactose-3-O-sulphotransferase	1799:1856	a hitherto uncharacterized galactose-3-O-sulphotransferase in thyrotroph cells of the human anterior pituitary gland	1799:1914	Some interesting structural features, not previously reported for the N-glycans of hTSH, included 3-O-sulphated galactose (SO4-3Gal) and peripheral fucose (Fuc alpha 1-3GlcNAc) in the Man alpha 1-6 branch of some diantennary structures; the former suggests the presence of a hitherto uncharacterized galactose-3-O-sulphotransferase in thyrotroph cells of the human anterior pituitary gland.
1457969	4	15	theme	intact	697:702	arg1	beta					709:712	intact hTSH beta	697:712	intact hTSH beta	697:712	The oligosaccharides were liberated from hTSH alpha glycopeptides and from intact hTSH beta by hydrazinolysis, and were fractionated as alditols by anion-exchange and ion-suppression amine-adsorption HPLC preparatory to structural analysis.
1457969	0	16	theme	human	76:80	arg1	thyrotrophin					82:93	human thyrotrophin	76:93	human thyrotrophin	76:93	The asparagine-linked oligosaccharides at individual glycosylation sites in human thyrotrophin.
1457969	6	17	theme	structural	1054:1063	arg1	heterogeneity					1065:1077	structural heterogeneity	1054:1077	structural heterogeneity in the terminal sequence	1054:1102	The Man alpha 1-6 branch displayed structural heterogeneity in the terminal sequence, with chiefly alpha 2-3-sialylated Gal and/or 4-O-sulphated GalNAc.
1457969	8	18	theme	hTSH	1609:1612	arg1	N-glycans					1596:1604	the N-glycans	1592:1604	the N-glycans of hTSH	1592:1612	Some interesting structural features, not previously reported for the N-glycans of hTSH, included 3-O-sulphated galactose (SO4-3Gal) and peripheral fucose (Fuc alpha 1-3GlcNAc) in the Man alpha 1-6 branch of some diantennary structures; the former suggests the presence of a hitherto uncharacterized galactose-3-O-sulphotransferase in thyrotroph cells of the human anterior pituitary gland.
1457969	6	19	from	heterogeneity	1065:1077	arg1	sequence					1095:1102	the terminal sequence	1082:1102	the terminal sequence	1082:1102	The Man alpha 1-6 branch displayed structural heterogeneity in the terminal sequence, with chiefly alpha 2-3-sialylated Gal and/or 4-O-sulphated GalNAc.
1457969	7	20	theme	glycosylation	1298:1310	arg1	site					1312:1315	glycosylation site	1298:1315	glycosylation site	1298:1315	The relative amounts of the two major complete diantennary oligosaccharides and their core fucosylation differed according to glycosylation site; the sulphated/sialylated diantennary oligosaccharide was most abundant at the two sites on the alpha-subunit, whereas the disulphated, core-fucosylated oligosaccharide was more plentiful on the beta-subunit.
1457969	1	21	theme	human	186:190	arg1	thyrotrophin					192:203	human thyrotrophin	186:203	human thyrotrophin	186:203	The asparagine-linked carbohydrate structures at each of the three glycosylation sites of human thyrotrophin were investigated by 400 MHz 1H-NMR spectroscopy.
1457969	5	22	with	structures	930:939	arg1	branch					969:974	a common Man alpha 1-3 branch	946:974	a common Man alpha 1-3 branch that terminated with 4-O-sulphated GalNAc	946:1016	The N-glycans present on hTSH were mainly diantennary complex-type structures with a common Man alpha 1-3 branch that terminated with 4-O-sulphated GalNAc.
1457969	3	23	gly	glycopeptides	505:517	arg2	glycopeptides					505:517	two glycopeptides	501:517	two glycopeptides that were subsequently separated by reverse-phase HPLC and identified by amino acid sequence analysis	501:619	The alpha-subunit was further treated with trypsin which gave two glycopeptides that were subsequently separated by reverse-phase HPLC and identified by amino acid sequence analysis.
1457969	6	24	theme	alpha	1027:1031	arg1	branch					1037:1042	The Man alpha 1-6 branch	1019:1042	The Man alpha 1-6 branch	1019:1042	The Man alpha 1-6 branch displayed structural heterogeneity in the terminal sequence, with chiefly alpha 2-3-sialylated Gal and/or 4-O-sulphated GalNAc.
1457969	0	25	from	sites	67:71	arg1	thyrotrophin					82:93	human thyrotrophin	76:93	human thyrotrophin	76:93	The asparagine-linked oligosaccharides at individual glycosylation sites in human thyrotrophin.
1457969	4	26	theme	ion-suppression	789:803	arg1	HPLC					822:825	anion-exchange and ion-suppression amine-adsorption HPLC	770:825	HPLC	822:825	The oligosaccharides were liberated from hTSH alpha glycopeptides and from intact hTSH beta by hydrazinolysis, and were fractionated as alditols by anion-exchange and ion-suppression amine-adsorption HPLC preparatory to structural analysis.
1457969	7	27	theme	fucosylation	1263:1274	arg1	oligosaccharides					1231:1246	the two major complete diantennary oligosaccharides	1196:1246	the two major complete diantennary oligosaccharides	1196:1246	The relative amounts of the two major complete diantennary oligosaccharides and their core fucosylation differed according to glycosylation site; the sulphated/sialylated diantennary oligosaccharide was most abundant at the two sites on the alpha-subunit, whereas the disulphated, core-fucosylated oligosaccharide was more plentiful on the beta-subunit.
1457969	7	27	theme	fucosylation	1263:1274	arg1	amounts					1185:1191	The relative amounts	1172:1191	The relative amounts of the two major complete diantennary oligosaccharides and their core fucosylation	1172:1274	The relative amounts of the two major complete diantennary oligosaccharides and their core fucosylation differed according to glycosylation site; the sulphated/sialylated diantennary oligosaccharide was most abundant at the two sites on the alpha-subunit, whereas the disulphated, core-fucosylated oligosaccharide was more plentiful on the beta-subunit.
1457969	7	27	theme	fucosylation	1263:1274	arg1	fucosylation					1263:1274	their core fucosylation	1252:1274	their core fucosylation	1252:1274	The relative amounts of the two major complete diantennary oligosaccharides and their core fucosylation differed according to glycosylation site; the sulphated/sialylated diantennary oligosaccharide was most abundant at the two sites on the alpha-subunit, whereas the disulphated, core-fucosylated oligosaccharide was more plentiful on the beta-subunit.
1457969	0	28	theme	glycosylation	53:65	arg1	sites					67:71	individual glycosylation sites	42:71	individual glycosylation sites in human thyrotrophin	42:93	The asparagine-linked oligosaccharides at individual glycosylation sites in human thyrotrophin.
1457969	6	29	theme	2-3-sialylated	1124:1137	arg1	Gal					1139:1141	chiefly alpha 2-3-sialylated Gal	1110:1141	chiefly alpha 2-3-sialylated Gal	1110:1141	The Man alpha 1-6 branch displayed structural heterogeneity in the terminal sequence, with chiefly alpha 2-3-sialylated Gal and/or 4-O-sulphated GalNAc.
1457969	2	30	dep	alpha	357:361	arg1	glycosylated					364:375	glycosylated	364:375	glycosylated at Asn 52 and Asn 78	364:396	Highly purified, biologically active human thyrotrophin (hTSH) was dissociated into its subunits hTSH alpha (glycosylated at Asn 52 and Asn 78) and hTSH beta (glycosylated at Asn 23).
1457969	1	31	from	each	145:148	arg1	structures					131:140	The asparagine-linked carbohydrate structures	96:140	The asparagine-linked carbohydrate structures at each of the three glycosylation sites of human thyrotrophin	96:203	The asparagine-linked carbohydrate structures at each of the three glycosylation sites of human thyrotrophin were investigated by 400 MHz 1H-NMR spectroscopy.
1457969	1	32	theme	carbohydrate	118:129	arg1	structures					131:140	The asparagine-linked carbohydrate structures	96:140	The asparagine-linked carbohydrate structures at each of the three glycosylation sites of human thyrotrophin	96:203	The asparagine-linked carbohydrate structures at each of the three glycosylation sites of human thyrotrophin were investigated by 400 MHz 1H-NMR spectroscopy.
1457969	6	33	theme	chiefly	1110:1116	arg1	Gal					1139:1141	chiefly alpha 2-3-sialylated Gal	1110:1141	chiefly alpha 2-3-sialylated Gal	1110:1141	The Man alpha 1-6 branch displayed structural heterogeneity in the terminal sequence, with chiefly alpha 2-3-sialylated Gal and/or 4-O-sulphated GalNAc.
1457969	7	34	gly	glycosylation	1298:1310	arg2	site					1312:1315	glycosylation site	1298:1315	glycosylation site	1298:1315	The relative amounts of the two major complete diantennary oligosaccharides and their core fucosylation differed according to glycosylation site; the sulphated/sialylated diantennary oligosaccharide was most abundant at the two sites on the alpha-subunit, whereas the disulphated, core-fucosylated oligosaccharide was more plentiful on the beta-subunit.
1457969	7	35	theme	oligosaccharides	1231:1246	arg1	oligosaccharides					1231:1246	the two major complete diantennary oligosaccharides	1196:1246	the two major complete diantennary oligosaccharides	1196:1246	The relative amounts of the two major complete diantennary oligosaccharides and their core fucosylation differed according to glycosylation site; the sulphated/sialylated diantennary oligosaccharide was most abundant at the two sites on the alpha-subunit, whereas the disulphated, core-fucosylated oligosaccharide was more plentiful on the beta-subunit.
1457969	7	35	theme	oligosaccharides	1231:1246	arg1	amounts					1185:1191	The relative amounts	1172:1191	The relative amounts of the two major complete diantennary oligosaccharides and their core fucosylation	1172:1274	The relative amounts of the two major complete diantennary oligosaccharides and their core fucosylation differed according to glycosylation site; the sulphated/sialylated diantennary oligosaccharide was most abundant at the two sites on the alpha-subunit, whereas the disulphated, core-fucosylated oligosaccharide was more plentiful on the beta-subunit.
1457969	7	35	theme	oligosaccharides	1231:1246	arg1	fucosylation					1263:1274	their core fucosylation	1252:1274	their core fucosylation	1252:1274	The relative amounts of the two major complete diantennary oligosaccharides and their core fucosylation differed according to glycosylation site; the sulphated/sialylated diantennary oligosaccharide was most abundant at the two sites on the alpha-subunit, whereas the disulphated, core-fucosylated oligosaccharide was more plentiful on the beta-subunit.
1457969	5	36	theme	4-O-sulphated	997:1009	arg1	GalNAc					1011:1016	4-O-sulphated GalNAc	997:1016	4-O-sulphated GalNAc	997:1016	The N-glycans present on hTSH were mainly diantennary complex-type structures with a common Man alpha 1-3 branch that terminated with 4-O-sulphated GalNAc.
1457969	2	37	dep	beta	408:411	arg1	glycosylated					414:425	glycosylated	414:425	glycosylated at Asn 23	414:435	Highly purified, biologically active human thyrotrophin (hTSH) was dissociated into its subunits hTSH alpha (glycosylated at Asn 52 and Asn 78) and hTSH beta (glycosylated at Asn 23).
1457969	0	38	theme	individual	42:51	arg1	sites					67:71	individual glycosylation sites	42:71	individual glycosylation sites in human thyrotrophin	42:93	The asparagine-linked oligosaccharides at individual glycosylation sites in human thyrotrophin.
1457969	7	39	theme	complete	1210:1217	arg1	oligosaccharides					1231:1246	the two major complete diantennary oligosaccharides	1196:1246	the two major complete diantennary oligosaccharides	1196:1246	The relative amounts of the two major complete diantennary oligosaccharides and their core fucosylation differed according to glycosylation site; the sulphated/sialylated diantennary oligosaccharide was most abundant at the two sites on the alpha-subunit, whereas the disulphated, core-fucosylated oligosaccharide was more plentiful on the beta-subunit.
1457969	6	40	theme	terminal	1086:1093	arg1	sequence					1095:1102	the terminal sequence	1082:1102	the terminal sequence	1082:1102	The Man alpha 1-6 branch displayed structural heterogeneity in the terminal sequence, with chiefly alpha 2-3-sialylated Gal and/or 4-O-sulphated GalNAc.
1457969	8	41	theme	Fuc	1682:1684	arg1	fucose					1674:1679	peripheral fucose	1663:1679	peripheral fucose (Fuc alpha 1-3GlcNAc)	1663:1701	Some interesting structural features, not previously reported for the N-glycans of hTSH, included 3-O-sulphated galactose (SO4-3Gal) and peripheral fucose (Fuc alpha 1-3GlcNAc) in the Man alpha 1-6 branch of some diantennary structures; the former suggests the presence of a hitherto uncharacterized galactose-3-O-sulphotransferase in thyrotroph cells of the human anterior pituitary gland.
1457969	8	41	theme	Fuc	1682:1684	arg1	1-3GlcNAc					1692:1700	Fuc alpha 1-3GlcNAc	1682:1700	Fuc alpha 1-3GlcNAc	1682:1700	Some interesting structural features, not previously reported for the N-glycans of hTSH, included 3-O-sulphated galactose (SO4-3Gal) and peripheral fucose (Fuc alpha 1-3GlcNAc) in the Man alpha 1-6 branch of some diantennary structures; the former suggests the presence of a hitherto uncharacterized galactose-3-O-sulphotransferase in thyrotroph cells of the human anterior pituitary gland.
1457969	6	42	gly	2-3-sialylated	1124:1137	arg1	Gal					1139:1141	chiefly alpha 2-3-sialylated Gal	1110:1141	chiefly alpha 2-3-sialylated Gal	1110:1141	The Man alpha 1-6 branch displayed structural heterogeneity in the terminal sequence, with chiefly alpha 2-3-sialylated Gal and/or 4-O-sulphated GalNAc.
1457969	5	43	attach	present	877:883	arg2	N-glycans					867:875	The N-glycans	863:875	The N-glycans present on hTSH	863:891	The N-glycans present on hTSH were mainly diantennary complex-type structures with a common Man alpha 1-3 branch that terminated with 4-O-sulphated GalNAc.
1457969	5	43	attach	present	877:883	arg1	hTSH					888:891	hTSH	888:891	hTSH	888:891	The N-glycans present on hTSH were mainly diantennary complex-type structures with a common Man alpha 1-3 branch that terminated with 4-O-sulphated GalNAc.
1457969	5	43	attach	present	877:883	arg2	structures					930:939	diantennary complex-type structures	905:939	diantennary complex-type structures	905:939	The N-glycans present on hTSH were mainly diantennary complex-type structures with a common Man alpha 1-3 branch that terminated with 4-O-sulphated GalNAc.
1457969	7	44	from	sites	1400:1404	arg1	alpha-subunit					1413:1425	the alpha-subunit	1409:1425	the alpha-subunit	1409:1425	The relative amounts of the two major complete diantennary oligosaccharides and their core fucosylation differed according to glycosylation site; the sulphated/sialylated diantennary oligosaccharide was most abundant at the two sites on the alpha-subunit, whereas the disulphated, core-fucosylated oligosaccharide was more plentiful on the beta-subunit.
1457969	7	44	from	sites	1400:1404	arg1	oligosaccharide					1355:1369	the sulphated/sialylated diantennary oligosaccharide	1318:1369	the sulphated/sialylated diantennary oligosaccharide	1318:1369	The relative amounts of the two major complete diantennary oligosaccharides and their core fucosylation differed according to glycosylation site; the sulphated/sialylated diantennary oligosaccharide was most abundant at the two sites on the alpha-subunit, whereas the disulphated, core-fucosylated oligosaccharide was more plentiful on the beta-subunit.
1457969	7	44	from	sites	1400:1404	arg1	abundant					1380:1387	abundant	1380:1387	abundant	1380:1387	The relative amounts of the two major complete diantennary oligosaccharides and their core fucosylation differed according to glycosylation site; the sulphated/sialylated diantennary oligosaccharide was most abundant at the two sites on the alpha-subunit, whereas the disulphated, core-fucosylated oligosaccharide was more plentiful on the beta-subunit.
1457969	8	45	theme	interesting	1531:1541	arg1	features					1554:1561	Some interesting structural features	1526:1561	Some interesting structural features	1526:1561	Some interesting structural features, not previously reported for the N-glycans of hTSH, included 3-O-sulphated galactose (SO4-3Gal) and peripheral fucose (Fuc alpha 1-3GlcNAc) in the Man alpha 1-6 branch of some diantennary structures; the former suggests the presence of a hitherto uncharacterized galactose-3-O-sulphotransferase in thyrotroph cells of the human anterior pituitary gland.
1457969	8	46	theme	diantennary	1739:1749	arg1	structures					1751:1760	some diantennary structures	1734:1760	some diantennary structures	1734:1760	Some interesting structural features, not previously reported for the N-glycans of hTSH, included 3-O-sulphated galactose (SO4-3Gal) and peripheral fucose (Fuc alpha 1-3GlcNAc) in the Man alpha 1-6 branch of some diantennary structures; the former suggests the presence of a hitherto uncharacterized galactose-3-O-sulphotransferase in thyrotroph cells of the human anterior pituitary gland.
1457969	0	47	gly	glycosylation	53:65	arg2	sites					67:71	individual glycosylation sites	42:71	individual glycosylation sites in human thyrotrophin	42:93	The asparagine-linked oligosaccharides at individual glycosylation sites in human thyrotrophin.
1457969	8	48	theme	Man	1710:1712	arg1	branch					1724:1729	the Man alpha 1-6 branch	1706:1729	the Man alpha 1-6 branch of some diantennary structures	1706:1760	Some interesting structural features, not previously reported for the N-glycans of hTSH, included 3-O-sulphated galactose (SO4-3Gal) and peripheral fucose (Fuc alpha 1-3GlcNAc) in the Man alpha 1-6 branch of some diantennary structures; the former suggests the presence of a hitherto uncharacterized galactose-3-O-sulphotransferase in thyrotroph cells of the human anterior pituitary gland.
1457969	1	49	link	asparagine-linked	100:116	arg1	structures					131:140	The asparagine-linked carbohydrate structures	96:140	The asparagine-linked carbohydrate structures at each of the three glycosylation sites of human thyrotrophin	96:203	The asparagine-linked carbohydrate structures at each of the three glycosylation sites of human thyrotrophin were investigated by 400 MHz 1H-NMR spectroscopy.
1457969	7	50	theme	sulphated/sialylated	1322:1341	arg1	oligosaccharide					1355:1369	the sulphated/sialylated diantennary oligosaccharide	1318:1369	the sulphated/sialylated diantennary oligosaccharide	1318:1369	The relative amounts of the two major complete diantennary oligosaccharides and their core fucosylation differed according to glycosylation site; the sulphated/sialylated diantennary oligosaccharide was most abundant at the two sites on the alpha-subunit, whereas the disulphated, core-fucosylated oligosaccharide was more plentiful on the beta-subunit.
1457969	7	50	theme	sulphated/sialylated	1322:1341	arg1	abundant					1380:1387	abundant	1380:1387	abundant	1380:1387	The relative amounts of the two major complete diantennary oligosaccharides and their core fucosylation differed according to glycosylation site; the sulphated/sialylated diantennary oligosaccharide was most abundant at the two sites on the alpha-subunit, whereas the disulphated, core-fucosylated oligosaccharide was more plentiful on the beta-subunit.
1457969	4	51	gly	glycopeptides	674:686	arg2	glycopeptides					674:686	hTSH alpha glycopeptides	663:686	hTSH alpha glycopeptides	663:686	The oligosaccharides were liberated from hTSH alpha glycopeptides and from intact hTSH beta by hydrazinolysis, and were fractionated as alditols by anion-exchange and ion-suppression amine-adsorption HPLC preparatory to structural analysis.
1457969	1	52	theme	thyrotrophin	192:203	arg1	sites					177:181	the three glycosylation sites	153:181	the three glycosylation sites of human thyrotrophin	153:203	The asparagine-linked carbohydrate structures at each of the three glycosylation sites of human thyrotrophin were investigated by 400 MHz 1H-NMR spectroscopy.
1457969	1	52	theme	thyrotrophin	192:203	arg1	thyrotrophin					192:203	human thyrotrophin	186:203	human thyrotrophin	186:203	The asparagine-linked carbohydrate structures at each of the three glycosylation sites of human thyrotrophin were investigated by 400 MHz 1H-NMR spectroscopy.
1457969	4	53	theme	hTSH	663:666	arg1	glycopeptides					674:686	hTSH alpha glycopeptides	663:686	hTSH alpha glycopeptides	663:686	The oligosaccharides were liberated from hTSH alpha glycopeptides and from intact hTSH beta by hydrazinolysis, and were fractionated as alditols by anion-exchange and ion-suppression amine-adsorption HPLC preparatory to structural analysis.
1457969	8	54	from	galactose-3-O-sulphotransferase	1826:1856	arg1	cells					1872:1876	thyrotroph cells	1861:1876	thyrotroph cells	1861:1876	Some interesting structural features, not previously reported for the N-glycans of hTSH, included 3-O-sulphated galactose (SO4-3Gal) and peripheral fucose (Fuc alpha 1-3GlcNAc) in the Man alpha 1-6 branch of some diantennary structures; the former suggests the presence of a hitherto uncharacterized galactose-3-O-sulphotransferase in thyrotroph cells of the human anterior pituitary gland.
1457969	6	55	theme	Man	1023:1025	arg1	branch					1037:1042	The Man alpha 1-6 branch	1019:1042	The Man alpha 1-6 branch	1019:1042	The Man alpha 1-6 branch displayed structural heterogeneity in the terminal sequence, with chiefly alpha 2-3-sialylated Gal and/or 4-O-sulphated GalNAc.
1457969	7	56	dep	disulphated	1440:1450	arg1	core-fucosylated					1453:1468	core-fucosylated	1453:1468	core-fucosylated	1453:1468	The relative amounts of the two major complete diantennary oligosaccharides and their core fucosylation differed according to glycosylation site; the sulphated/sialylated diantennary oligosaccharide was most abundant at the two sites on the alpha-subunit, whereas the disulphated, core-fucosylated oligosaccharide was more plentiful on the beta-subunit.
1457969	8	57	theme	galactose-3-O-sulphotransferase	1826:1856	arg1	presence					1787:1794	the presence	1783:1794	the presence of a hitherto uncharacterized galactose-3-O-sulphotransferase in thyrotroph cells of the human anterior pituitary gland	1783:1914	Some interesting structural features, not previously reported for the N-glycans of hTSH, included 3-O-sulphated galactose (SO4-3Gal) and peripheral fucose (Fuc alpha 1-3GlcNAc) in the Man alpha 1-6 branch of some diantennary structures; the former suggests the presence of a hitherto uncharacterized galactose-3-O-sulphotransferase in thyrotroph cells of the human anterior pituitary gland.
1457969	5	58	theme	common	948:953	arg1	branch					969:974	a common Man alpha 1-3 branch	946:974	a common Man alpha 1-3 branch that terminated with 4-O-sulphated GalNAc	946:1016	The N-glycans present on hTSH were mainly diantennary complex-type structures with a common Man alpha 1-3 branch that terminated with 4-O-sulphated GalNAc.
1457969	3	59	theme	amino	592:596	arg1	analysis					612:619	amino acid sequence analysis	592:619	amino acid sequence analysis	592:619	The alpha-subunit was further treated with trypsin which gave two glycopeptides that were subsequently separated by reverse-phase HPLC and identified by amino acid sequence analysis.
1457969	8	60	theme	thyrotroph	1861:1870	arg1	cells					1872:1876	thyrotroph cells	1861:1876	thyrotroph cells	1861:1876	Some interesting structural features, not previously reported for the N-glycans of hTSH, included 3-O-sulphated galactose (SO4-3Gal) and peripheral fucose (Fuc alpha 1-3GlcNAc) in the Man alpha 1-6 branch of some diantennary structures; the former suggests the presence of a hitherto uncharacterized galactose-3-O-sulphotransferase in thyrotroph cells of the human anterior pituitary gland.
1457969	1	61	theme	1H-NMR	234:239	arg1	spectroscopy					241:252	400 MHz 1H-NMR spectroscopy	226:252	400 MHz 1H-NMR spectroscopy	226:252	The asparagine-linked carbohydrate structures at each of the three glycosylation sites of human thyrotrophin were investigated by 400 MHz 1H-NMR spectroscopy.
1457969	2	62	dep	purified	262:269	arg1	active					285:290	active	285:290	active	285:290	Highly purified, biologically active human thyrotrophin (hTSH) was dissociated into its subunits hTSH alpha (glycosylated at Asn 52 and Asn 78) and hTSH beta (glycosylated at Asn 23).
1457969	5	63	theme	Man	955:957	arg1	branch					969:974	a common Man alpha 1-3 branch	946:974	a common Man alpha 1-3 branch that terminated with 4-O-sulphated GalNAc	946:1016	The N-glycans present on hTSH were mainly diantennary complex-type structures with a common Man alpha 1-3 branch that terminated with 4-O-sulphated GalNAc.
1457969	8	64	from	cells	1872:1876	arg1	presence					1787:1794	the presence	1783:1794	the presence of a hitherto uncharacterized galactose-3-O-sulphotransferase in thyrotroph cells of the human anterior pituitary gland	1783:1914	Some interesting structural features, not previously reported for the N-glycans of hTSH, included 3-O-sulphated galactose (SO4-3Gal) and peripheral fucose (Fuc alpha 1-3GlcNAc) in the Man alpha 1-6 branch of some diantennary structures; the former suggests the presence of a hitherto uncharacterized galactose-3-O-sulphotransferase in thyrotroph cells of the human anterior pituitary gland.
1457969	8	65	theme	human	1885:1889	arg1	gland					1910:1914	the human anterior pituitary gland	1881:1914	the human anterior pituitary gland	1881:1914	Some interesting structural features, not previously reported for the N-glycans of hTSH, included 3-O-sulphated galactose (SO4-3Gal) and peripheral fucose (Fuc alpha 1-3GlcNAc) in the Man alpha 1-6 branch of some diantennary structures; the former suggests the presence of a hitherto uncharacterized galactose-3-O-sulphotransferase in thyrotroph cells of the human anterior pituitary gland.
1457969	4	66	theme	anion-exchange	770:783	arg1	HPLC					822:825	anion-exchange and ion-suppression amine-adsorption HPLC	770:825	HPLC	822:825	The oligosaccharides were liberated from hTSH alpha glycopeptides and from intact hTSH beta by hydrazinolysis, and were fractionated as alditols by anion-exchange and ion-suppression amine-adsorption HPLC preparatory to structural analysis.
1457969	3	67	theme	sequence	603:610	arg1	analysis					612:619	amino acid sequence analysis	592:619	amino acid sequence analysis	592:619	The alpha-subunit was further treated with trypsin which gave two glycopeptides that were subsequently separated by reverse-phase HPLC and identified by amino acid sequence analysis.
1457969	8	68	theme	pituitary	1900:1908	arg1	gland					1910:1914	the human anterior pituitary gland	1881:1914	the human anterior pituitary gland	1881:1914	Some interesting structural features, not previously reported for the N-glycans of hTSH, included 3-O-sulphated galactose (SO4-3Gal) and peripheral fucose (Fuc alpha 1-3GlcNAc) in the Man alpha 1-6 branch of some diantennary structures; the former suggests the presence of a hitherto uncharacterized galactose-3-O-sulphotransferase in thyrotroph cells of the human anterior pituitary gland.
1457969	1	69	theme	glycosylation	163:175	arg1	sites					177:181	the three glycosylation sites	153:181	the three glycosylation sites of human thyrotrophin	153:203	The asparagine-linked carbohydrate structures at each of the three glycosylation sites of human thyrotrophin were investigated by 400 MHz 1H-NMR spectroscopy.
1457969	1	69	theme	glycosylation	163:175	arg1	thyrotrophin					192:203	human thyrotrophin	186:203	human thyrotrophin	186:203	The asparagine-linked carbohydrate structures at each of the three glycosylation sites of human thyrotrophin were investigated by 400 MHz 1H-NMR spectroscopy.
1457969	7	70	theme	disulphated	1440:1450	arg1	oligosaccharide					1470:1484	the disulphated, core-fucosylated oligosaccharide	1436:1484	the disulphated, core-fucosylated oligosaccharide	1436:1484	The relative amounts of the two major complete diantennary oligosaccharides and their core fucosylation differed according to glycosylation site; the sulphated/sialylated diantennary oligosaccharide was most abundant at the two sites on the alpha-subunit, whereas the disulphated, core-fucosylated oligosaccharide was more plentiful on the beta-subunit.
1457969	7	70	theme	disulphated	1440:1450	arg1	plentiful					1495:1503	plentiful	1495:1503	plentiful	1495:1503	The relative amounts of the two major complete diantennary oligosaccharides and their core fucosylation differed according to glycosylation site; the sulphated/sialylated diantennary oligosaccharide was most abundant at the two sites on the alpha-subunit, whereas the disulphated, core-fucosylated oligosaccharide was more plentiful on the beta-subunit.
1457969	8	71	theme	3-O-sulphated	1624:1636	arg1	SO4-3Gal					1649:1656	SO4-3Gal	1649:1656	SO4-3Gal	1649:1656	Some interesting structural features, not previously reported for the N-glycans of hTSH, included 3-O-sulphated galactose (SO4-3Gal) and peripheral fucose (Fuc alpha 1-3GlcNAc) in the Man alpha 1-6 branch of some diantennary structures; the former suggests the presence of a hitherto uncharacterized galactose-3-O-sulphotransferase in thyrotroph cells of the human anterior pituitary gland.
1457969	8	71	theme	3-O-sulphated	1624:1636	arg1	galactose					1638:1646	3-O-sulphated galactose	1624:1646	3-O-sulphated galactose (SO4-3Gal)	1624:1657	Some interesting structural features, not previously reported for the N-glycans of hTSH, included 3-O-sulphated galactose (SO4-3Gal) and peripheral fucose (Fuc alpha 1-3GlcNAc) in the Man alpha 1-6 branch of some diantennary structures; the former suggests the presence of a hitherto uncharacterized galactose-3-O-sulphotransferase in thyrotroph cells of the human anterior pituitary gland.
1457969	2	72	gly	glycosylated	414:425	arg1	beta					408:411	hTSH beta	403:411	hTSH beta (glycosylated at Asn 23)	403:436	Highly purified, biologically active human thyrotrophin (hTSH) was dissociated into its subunits hTSH alpha (glycosylated at Asn 52 and Asn 78) and hTSH beta (glycosylated at Asn 23).
1457969	2	72	gly	glycosylated	414:425	arg2	Asn					430:432	Asn 23	430:435	Asn 23	430:435	Highly purified, biologically active human thyrotrophin (hTSH) was dissociated into its subunits hTSH alpha (glycosylated at Asn 52 and Asn 78) and hTSH beta (glycosylated at Asn 23).
1457969	2	72	gly	glycosylated	414:425	arg1	subunits					343:350	its subunits	339:350	its subunits hTSH alpha (glycosylated at Asn 52 and Asn 78) and hTSH beta (glycosylated at Asn 23)	339:436	Highly purified, biologically active human thyrotrophin (hTSH) was dissociated into its subunits hTSH alpha (glycosylated at Asn 52 and Asn 78) and hTSH beta (glycosylated at Asn 23).
1457969	4	73	theme	hTSH	704:707	arg1	beta					709:712	intact hTSH beta	697:712	intact hTSH beta	697:712	The oligosaccharides were liberated from hTSH alpha glycopeptides and from intact hTSH beta by hydrazinolysis, and were fractionated as alditols by anion-exchange and ion-suppression amine-adsorption HPLC preparatory to structural analysis.
1457969	7	74	theme	core	1258:1261	arg1	fucosylation					1263:1274	their core fucosylation	1252:1274	their core fucosylation	1252:1274	The relative amounts of the two major complete diantennary oligosaccharides and their core fucosylation differed according to glycosylation site; the sulphated/sialylated diantennary oligosaccharide was most abundant at the two sites on the alpha-subunit, whereas the disulphated, core-fucosylated oligosaccharide was more plentiful on the beta-subunit.
1457969	1	75	theme	MHz	230:232	arg1	spectroscopy					241:252	400 MHz 1H-NMR spectroscopy	226:252	400 MHz 1H-NMR spectroscopy	226:252	The asparagine-linked carbohydrate structures at each of the three glycosylation sites of human thyrotrophin were investigated by 400 MHz 1H-NMR spectroscopy.
1457969	1	76	theme	asparagine-linked	100:116	arg1	structures					131:140	The asparagine-linked carbohydrate structures	96:140	The asparagine-linked carbohydrate structures at each of the three glycosylation sites of human thyrotrophin	96:203	The asparagine-linked carbohydrate structures at each of the three glycosylation sites of human thyrotrophin were investigated by 400 MHz 1H-NMR spectroscopy.
1457969	6	77	theme	alpha	1118:1122	arg1	Gal					1139:1141	chiefly alpha 2-3-sialylated Gal	1110:1141	chiefly alpha 2-3-sialylated Gal	1110:1141	The Man alpha 1-6 branch displayed structural heterogeneity in the terminal sequence, with chiefly alpha 2-3-sialylated Gal and/or 4-O-sulphated GalNAc.
1457969	8	78	theme	peripheral	1663:1672	arg1	fucose					1674:1679	peripheral fucose	1663:1679	peripheral fucose (Fuc alpha 1-3GlcNAc)	1663:1701	Some interesting structural features, not previously reported for the N-glycans of hTSH, included 3-O-sulphated galactose (SO4-3Gal) and peripheral fucose (Fuc alpha 1-3GlcNAc) in the Man alpha 1-6 branch of some diantennary structures; the former suggests the presence of a hitherto uncharacterized galactose-3-O-sulphotransferase in thyrotroph cells of the human anterior pituitary gland.
1457969	8	78	theme	peripheral	1663:1672	arg1	1-3GlcNAc					1692:1700	Fuc alpha 1-3GlcNAc	1682:1700	Fuc alpha 1-3GlcNAc	1682:1700	Some interesting structural features, not previously reported for the N-glycans of hTSH, included 3-O-sulphated galactose (SO4-3Gal) and peripheral fucose (Fuc alpha 1-3GlcNAc) in the Man alpha 1-6 branch of some diantennary structures; the former suggests the presence of a hitherto uncharacterized galactose-3-O-sulphotransferase in thyrotroph cells of the human anterior pituitary gland.
1457969	7	79	theme	diantennary	1219:1229	arg1	oligosaccharides					1231:1246	the two major complete diantennary oligosaccharides	1196:1246	the two major complete diantennary oligosaccharides	1196:1246	The relative amounts of the two major complete diantennary oligosaccharides and their core fucosylation differed according to glycosylation site; the sulphated/sialylated diantennary oligosaccharide was most abundant at the two sites on the alpha-subunit, whereas the disulphated, core-fucosylated oligosaccharide was more plentiful on the beta-subunit.
1457969	7	80	theme	major	1204:1208	arg1	oligosaccharides					1231:1246	the two major complete diantennary oligosaccharides	1196:1246	the two major complete diantennary oligosaccharides	1196:1246	The relative amounts of the two major complete diantennary oligosaccharides and their core fucosylation differed according to glycosylation site; the sulphated/sialylated diantennary oligosaccharide was most abundant at the two sites on the alpha-subunit, whereas the disulphated, core-fucosylated oligosaccharide was more plentiful on the beta-subunit.
1457969	7	81	gly	sulphated/sialylated	1322:1341	arg1	oligosaccharide					1355:1369	the sulphated/sialylated diantennary oligosaccharide	1318:1369	the sulphated/sialylated diantennary oligosaccharide	1318:1369	The relative amounts of the two major complete diantennary oligosaccharides and their core fucosylation differed according to glycosylation site; the sulphated/sialylated diantennary oligosaccharide was most abundant at the two sites on the alpha-subunit, whereas the disulphated, core-fucosylated oligosaccharide was more plentiful on the beta-subunit.
1457969	7	81	gly	sulphated/sialylated	1322:1341	arg1	abundant					1380:1387	abundant	1380:1387	abundant	1380:1387	The relative amounts of the two major complete diantennary oligosaccharides and their core fucosylation differed according to glycosylation site; the sulphated/sialylated diantennary oligosaccharide was most abundant at the two sites on the alpha-subunit, whereas the disulphated, core-fucosylated oligosaccharide was more plentiful on the beta-subunit.
1457969	8	82	theme	alpha	1686:1690	arg1	fucose					1674:1679	peripheral fucose	1663:1679	peripheral fucose (Fuc alpha 1-3GlcNAc)	1663:1701	Some interesting structural features, not previously reported for the N-glycans of hTSH, included 3-O-sulphated galactose (SO4-3Gal) and peripheral fucose (Fuc alpha 1-3GlcNAc) in the Man alpha 1-6 branch of some diantennary structures; the former suggests the presence of a hitherto uncharacterized galactose-3-O-sulphotransferase in thyrotroph cells of the human anterior pituitary gland.
1457969	8	82	theme	alpha	1686:1690	arg1	1-3GlcNAc					1692:1700	Fuc alpha 1-3GlcNAc	1682:1700	Fuc alpha 1-3GlcNAc	1682:1700	Some interesting structural features, not previously reported for the N-glycans of hTSH, included 3-O-sulphated galactose (SO4-3Gal) and peripheral fucose (Fuc alpha 1-3GlcNAc) in the Man alpha 1-6 branch of some diantennary structures; the former suggests the presence of a hitherto uncharacterized galactose-3-O-sulphotransferase in thyrotroph cells of the human anterior pituitary gland.
1457969	4	83	theme	structural	842:851	arg1	analysis					853:860	structural analysis	842:860	structural analysis	842:860	The oligosaccharides were liberated from hTSH alpha glycopeptides and from intact hTSH beta by hydrazinolysis, and were fractionated as alditols by anion-exchange and ion-suppression amine-adsorption HPLC preparatory to structural analysis.
1457969	2	84	theme	hTSH	403:406	arg1	beta					408:411	hTSH beta	403:411	hTSH beta (glycosylated at Asn 23)	403:436	Highly purified, biologically active human thyrotrophin (hTSH) was dissociated into its subunits hTSH alpha (glycosylated at Asn 52 and Asn 78) and hTSH beta (glycosylated at Asn 23).
1457969	2	84	theme	hTSH	403:406	arg1	subunits					343:350	its subunits	339:350	its subunits hTSH alpha (glycosylated at Asn 52 and Asn 78) and hTSH beta (glycosylated at Asn 23)	339:436	Highly purified, biologically active human thyrotrophin (hTSH) was dissociated into its subunits hTSH alpha (glycosylated at Asn 52 and Asn 78) and hTSH beta (glycosylated at Asn 23).
1457969	2	85	gly	glycosylated	364:375	arg2	Asn					391:393	Asn 78	391:396	Asn 78	391:396	Highly purified, biologically active human thyrotrophin (hTSH) was dissociated into its subunits hTSH alpha (glycosylated at Asn 52 and Asn 78) and hTSH beta (glycosylated at Asn 23).
1457969	2	85	gly	glycosylated	364:375	arg2	Asn					380:382	Asn 52	380:385	Asn 52	380:385	Highly purified, biologically active human thyrotrophin (hTSH) was dissociated into its subunits hTSH alpha (glycosylated at Asn 52 and Asn 78) and hTSH beta (glycosylated at Asn 23).
1457969	2	85	gly	glycosylated	364:375	arg1	alpha					357:361	hTSH alpha	352:361	hTSH alpha (glycosylated at Asn 52 and Asn 78)	352:397	Highly purified, biologically active human thyrotrophin (hTSH) was dissociated into its subunits hTSH alpha (glycosylated at Asn 52 and Asn 78) and hTSH beta (glycosylated at Asn 23).
1457969	2	85	gly	glycosylated	364:375	arg1	subunits					343:350	its subunits	339:350	its subunits hTSH alpha (glycosylated at Asn 52 and Asn 78) and hTSH beta (glycosylated at Asn 23)	339:436	Highly purified, biologically active human thyrotrophin (hTSH) was dissociated into its subunits hTSH alpha (glycosylated at Asn 52 and Asn 78) and hTSH beta (glycosylated at Asn 23).
1457969	8	86	theme	structures	1751:1760	arg1	branch					1724:1729	the Man alpha 1-6 branch	1706:1729	the Man alpha 1-6 branch of some diantennary structures	1706:1760	Some interesting structural features, not previously reported for the N-glycans of hTSH, included 3-O-sulphated galactose (SO4-3Gal) and peripheral fucose (Fuc alpha 1-3GlcNAc) in the Man alpha 1-6 branch of some diantennary structures; the former suggests the presence of a hitherto uncharacterized galactose-3-O-sulphotransferase in thyrotroph cells of the human anterior pituitary gland.
1457969	8	87	theme	structural	1543:1552	arg1	features					1554:1561	Some interesting structural features	1526:1561	Some interesting structural features	1526:1561	Some interesting structural features, not previously reported for the N-glycans of hTSH, included 3-O-sulphated galactose (SO4-3Gal) and peripheral fucose (Fuc alpha 1-3GlcNAc) in the Man alpha 1-6 branch of some diantennary structures; the former suggests the presence of a hitherto uncharacterized galactose-3-O-sulphotransferase in thyrotroph cells of the human anterior pituitary gland.
1457969	3	88	theme	acid	598:601	arg1	analysis					612:619	amino acid sequence analysis	592:619	amino acid sequence analysis	592:619	The alpha-subunit was further treated with trypsin which gave two glycopeptides that were subsequently separated by reverse-phase HPLC and identified by amino acid sequence analysis.
1457969	4	89	attach	liberated	648:656	arg2	alditols					758:765	alditols	758:765	alditols	758:765	The oligosaccharides were liberated from hTSH alpha glycopeptides and from intact hTSH beta by hydrazinolysis, and were fractionated as alditols by anion-exchange and ion-suppression amine-adsorption HPLC preparatory to structural analysis.
1457969	4	89	attach	liberated	648:656	arg2	oligosaccharides					626:641	The oligosaccharides	622:641	The oligosaccharides	622:641	The oligosaccharides were liberated from hTSH alpha glycopeptides and from intact hTSH beta by hydrazinolysis, and were fractionated as alditols by anion-exchange and ion-suppression amine-adsorption HPLC preparatory to structural analysis.
1457969	4	89	attach	liberated	648:656	arg1	beta					709:712	intact hTSH beta	697:712	intact hTSH beta	697:712	The oligosaccharides were liberated from hTSH alpha glycopeptides and from intact hTSH beta by hydrazinolysis, and were fractionated as alditols by anion-exchange and ion-suppression amine-adsorption HPLC preparatory to structural analysis.
1457969	4	89	attach	liberated	648:656	arg1	glycopeptides					674:686	hTSH alpha glycopeptides	663:686	hTSH alpha glycopeptides	663:686	The oligosaccharides were liberated from hTSH alpha glycopeptides and from intact hTSH beta by hydrazinolysis, and were fractionated as alditols by anion-exchange and ion-suppression amine-adsorption HPLC preparatory to structural analysis.
1457969	4	90	theme	amine-adsorption	805:820	arg1	HPLC					822:825	anion-exchange and ion-suppression amine-adsorption HPLC	770:825	HPLC	822:825	The oligosaccharides were liberated from hTSH alpha glycopeptides and from intact hTSH beta by hydrazinolysis, and were fractionated as alditols by anion-exchange and ion-suppression amine-adsorption HPLC preparatory to structural analysis.
1457969	2	91	theme	hTSH	352:355	arg1	alpha					357:361	hTSH alpha	352:361	hTSH alpha (glycosylated at Asn 52 and Asn 78)	352:397	Highly purified, biologically active human thyrotrophin (hTSH) was dissociated into its subunits hTSH alpha (glycosylated at Asn 52 and Asn 78) and hTSH beta (glycosylated at Asn 23).
1457969	2	91	theme	hTSH	352:355	arg1	subunits					343:350	its subunits	339:350	its subunits hTSH alpha (glycosylated at Asn 52 and Asn 78) and hTSH beta (glycosylated at Asn 23)	339:436	Highly purified, biologically active human thyrotrophin (hTSH) was dissociated into its subunits hTSH alpha (glycosylated at Asn 52 and Asn 78) and hTSH beta (glycosylated at Asn 23).
1457969	7	92	theme	diantennary	1343:1353	arg1	oligosaccharide					1355:1369	the sulphated/sialylated diantennary oligosaccharide	1318:1369	the sulphated/sialylated diantennary oligosaccharide	1318:1369	The relative amounts of the two major complete diantennary oligosaccharides and their core fucosylation differed according to glycosylation site; the sulphated/sialylated diantennary oligosaccharide was most abundant at the two sites on the alpha-subunit, whereas the disulphated, core-fucosylated oligosaccharide was more plentiful on the beta-subunit.
1457969	7	92	theme	diantennary	1343:1353	arg1	abundant					1380:1387	abundant	1380:1387	abundant	1380:1387	The relative amounts of the two major complete diantennary oligosaccharides and their core fucosylation differed according to glycosylation site; the sulphated/sialylated diantennary oligosaccharide was most abundant at the two sites on the alpha-subunit, whereas the disulphated, core-fucosylated oligosaccharide was more plentiful on the beta-subunit.
1457969	8	93	theme	alpha	1714:1718	arg1	branch					1724:1729	the Man alpha 1-6 branch	1706:1729	the Man alpha 1-6 branch of some diantennary structures	1706:1760	Some interesting structural features, not previously reported for the N-glycans of hTSH, included 3-O-sulphated galactose (SO4-3Gal) and peripheral fucose (Fuc alpha 1-3GlcNAc) in the Man alpha 1-6 branch of some diantennary structures; the former suggests the presence of a hitherto uncharacterized galactose-3-O-sulphotransferase in thyrotroph cells of the human anterior pituitary gland.
1457969	4	94	theme	preparatory	827:837	arg1	HPLC					822:825	anion-exchange and ion-suppression amine-adsorption HPLC	770:825	HPLC	822:825	The oligosaccharides were liberated from hTSH alpha glycopeptides and from intact hTSH beta by hydrazinolysis, and were fractionated as alditols by anion-exchange and ion-suppression amine-adsorption HPLC preparatory to structural analysis.
17293352	8	0	theme	enhancement	1138:1148	arg1	spectroscopy					1150:1161	600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy	1050:1161	600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H	1050:1167	The structures of the components were analyzed by 500 MHz one-dimensional and 600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H nuclear magnetic resonance spectroscopy, combined with two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy, matrix-assisted laser desorption ionization time-of-flight mass spectrometry, and high-performance liquid chromatography (HPLC)-profiling of 2-aminobenzamide-labeled glycans combined with exoglycosidase digestions.
17293352	6	1	theme	asparagine	770:779	arg1	F					789:789	(N-acetyl-beta-glucosaminyl)asparagine amidase F	742:789	(N-acetyl-beta-glucosaminyl)asparagine amidase F	742:789	The N-linked glycans of recombinant human GAA (rhAGLU), isolated from the rabbit milk, were released by peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase F.
17293352	8	2	theme	2-aminobenzamide-labeled	1426:1449	arg1	glycans					1451:1457	2-aminobenzamide-labeled glycans	1426:1457	2-aminobenzamide-labeled glycans combined with exoglycosidase digestions	1426:1497	The structures of the components were analyzed by 500 MHz one-dimensional and 600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H nuclear magnetic resonance spectroscopy, combined with two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy, matrix-assisted laser desorption ionization time-of-flight mass spectrometry, and high-performance liquid chromatography (HPLC)-profiling of 2-aminobenzamide-labeled glycans combined with exoglycosidase digestions.
17293352	11	3	dep	glycans	1775:1781	arg1	partially					1784:1792	partially	1784:1792	partially	1784:1792	For the complex-type glycans (partially) (alpha2-6)-sialylated (nearly only N-acetylneuraminic acid) diantennary structures were found; part of the structures were (alpha1-6)-core-fucosylated or (alpha1-3)-fucosylated in the upper antenna (Lewis x).
17293352	6	4	theme	N-acetyl-beta-glucosaminyl	743:768	arg1	F					789:789	(N-acetyl-beta-glucosaminyl)asparagine amidase F	742:789	(N-acetyl-beta-glucosaminyl)asparagine amidase F	742:789	The N-linked glycans of recombinant human GAA (rhAGLU), isolated from the rabbit milk, were released by peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase F.
17293352	12	5	theme	glycopeptides	2036:2048	arg1	spectrometry					2020:2031	HPLC-mass spectrometry	2010:2031	HPLC-mass spectrometry of glycopeptides	2010:2048	Using HPLC-mass spectrometry of glycopeptides, information was generated with respect to the site-specific location of the various glycans.
17293352	8	6	theme	two-dimensional	1224:1238	arg1	HPLC					1407:1410	HPLC	1407:1410	HPLC	1407:1410	The structures of the components were analyzed by 500 MHz one-dimensional and 600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H nuclear magnetic resonance spectroscopy, combined with two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy, matrix-assisted laser desorption ionization time-of-flight mass spectrometry, and high-performance liquid chromatography (HPLC)-profiling of 2-aminobenzamide-labeled glycans combined with exoglycosidase digestions.
17293352	8	6	theme	two-dimensional	1224:1238	arg1	spectroscopy					1271:1282	two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy	1224:1282	two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy	1224:1282	The structures of the components were analyzed by 500 MHz one-dimensional and 600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H nuclear magnetic resonance spectroscopy, combined with two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy, matrix-assisted laser desorption ionization time-of-flight mass spectrometry, and high-performance liquid chromatography (HPLC)-profiling of 2-aminobenzamide-labeled glycans combined with exoglycosidase digestions.
17293352	5	7	theme	rabbits	616:622	arg1	gland					596:600	the mammary gland	584:600	the mammary gland of transgenic rabbits	584:622	Here, human GAA was expressed in the mammary gland of transgenic rabbits.
17293352	7	8	theme	N-glycan	796:803	arg1	pool					805:808	The N-glycan pool	792:808	The N-glycan pool	792:808	The N-glycan pool was fractionated and purified into individual components by a combination of anion-exchange, normal-phase, and Sambucus nigra agglutinin-affinity chromatography.
17293352	1	9	theme	alpha-glucosidase	176:192	arg1	deficiency					200:209	acid alpha-glucosidase (GAA) deficiency	171:209	acid alpha-glucosidase (GAA) deficiency	171:209	Pompe disease is a lysosomal glycogen storage disorder characterized by acid alpha-glucosidase (GAA) deficiency.
17293352	8	10	theme	H	1167:1167	arg1	spectroscopy					1196:1207	500 MHz one-dimensional and 600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H nuclear magnetic resonance spectroscopy	1022:1207	500 MHz one-dimensional and 600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H nuclear magnetic resonance spectroscopy	1022:1207	The structures of the components were analyzed by 500 MHz one-dimensional and 600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H nuclear magnetic resonance spectroscopy, combined with two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy, matrix-assisted laser desorption ionization time-of-flight mass spectrometry, and high-performance liquid chromatography (HPLC)-profiling of 2-aminobenzamide-labeled glycans combined with exoglycosidase digestions.
17293352	8	11	theme	magnetic	1177:1184	arg1	spectroscopy					1196:1207	500 MHz one-dimensional and 600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H nuclear magnetic resonance spectroscopy	1022:1207	500 MHz one-dimensional and 600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H nuclear magnetic resonance spectroscopy	1022:1207	The structures of the components were analyzed by 500 MHz one-dimensional and 600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H nuclear magnetic resonance spectroscopy, combined with two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy, matrix-assisted laser desorption ionization time-of-flight mass spectrometry, and high-performance liquid chromatography (HPLC)-profiling of 2-aminobenzamide-labeled glycans combined with exoglycosidase digestions.
17293352	11	12	from	antenna	1985:1991	arg1	-core-fucosylated					1928:1944	-core-fucosylated	1928:1944	-core-fucosylated	1928:1944	For the complex-type glycans (partially) (alpha2-6)-sialylated (nearly only N-acetylneuraminic acid) diantennary structures were found; part of the structures were (alpha1-6)-core-fucosylated or (alpha1-3)-fucosylated in the upper antenna (Lewis x).
17293352	8	13	theme	P-filtered	1244:1253	arg1	HPLC					1407:1410	HPLC	1407:1410	HPLC	1407:1410	The structures of the components were analyzed by 500 MHz one-dimensional and 600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H nuclear magnetic resonance spectroscopy, combined with two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy, matrix-assisted laser desorption ionization time-of-flight mass spectrometry, and high-performance liquid chromatography (HPLC)-profiling of 2-aminobenzamide-labeled glycans combined with exoglycosidase digestions.
17293352	8	13	theme	P-filtered	1244:1253	arg1	spectroscopy					1271:1282	two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy	1224:1282	two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy	1224:1282	The structures of the components were analyzed by 500 MHz one-dimensional and 600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H nuclear magnetic resonance spectroscopy, combined with two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy, matrix-assisted laser desorption ionization time-of-flight mass spectrometry, and high-performance liquid chromatography (HPLC)-profiling of 2-aminobenzamide-labeled glycans combined with exoglycosidase digestions.
17293352	11	14	theme	N-acetylneuraminic	1830:1847	arg1	acid					1849:1852	nearly only N-acetylneuraminic acid	1818:1852	nearly only N-acetylneuraminic acid	1818:1852	For the complex-type glycans (partially) (alpha2-6)-sialylated (nearly only N-acetylneuraminic acid) diantennary structures were found; part of the structures were (alpha1-6)-core-fucosylated or (alpha1-3)-fucosylated in the upper antenna (Lewis x).
17293352	8	15	theme	one-dimensional	1030:1044	arg1	spectroscopy					1196:1207	500 MHz one-dimensional and 600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H nuclear magnetic resonance spectroscopy	1022:1207	500 MHz one-dimensional and 600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H nuclear magnetic resonance spectroscopy	1022:1207	The structures of the components were analyzed by 500 MHz one-dimensional and 600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H nuclear magnetic resonance spectroscopy, combined with two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy, matrix-assisted laser desorption ionization time-of-flight mass spectrometry, and high-performance liquid chromatography (HPLC)-profiling of 2-aminobenzamide-labeled glycans combined with exoglycosidase digestions.
17293352	8	16	theme	-profiling	1412:1421	arg1	HPLC					1407:1410	HPLC	1407:1410	HPLC	1407:1410	The structures of the components were analyzed by 500 MHz one-dimensional and 600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H nuclear magnetic resonance spectroscopy, combined with two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy, matrix-assisted laser desorption ionization time-of-flight mass spectrometry, and high-performance liquid chromatography (HPLC)-profiling of 2-aminobenzamide-labeled glycans combined with exoglycosidase digestions.
17293352	8	16	theme	-profiling	1412:1421	arg1	spectroscopy					1271:1282	two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy	1224:1282	two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy	1224:1282	The structures of the components were analyzed by 500 MHz one-dimensional and 600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H nuclear magnetic resonance spectroscopy, combined with two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy, matrix-assisted laser desorption ionization time-of-flight mass spectrometry, and high-performance liquid chromatography (HPLC)-profiling of 2-aminobenzamide-labeled glycans combined with exoglycosidase digestions.
17293352	2	17	theme	different	226:234	arg1	mutations					247:255	More than 110 different pathogenic mutations	212:255	More than 110 different pathogenic mutations in the gene encoding GAA	212:280	More than 110 different pathogenic mutations in the gene encoding GAA have been observed.
17293352	4	18	theme	enzyme	458:463	arg1	paid					505:508	paid	505:508	paid	505:508	Focusing on recombinant approaches to produce the enzyme means that specific attention has to be paid to the generated glycosylation patterns.
17293352	4	18	theme	enzyme	458:463	arg1	means					465:469	the enzyme means	454:469	the enzyme means that specific attention has to be paid to the generated glycosylation patterns	454:548	Focusing on recombinant approaches to produce the enzyme means that specific attention has to be paid to the generated glycosylation patterns.
17293352	8	19	theme	H-	1258:1259	arg1	HPLC					1407:1410	HPLC	1407:1410	HPLC	1407:1410	The structures of the components were analyzed by 500 MHz one-dimensional and 600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H nuclear magnetic resonance spectroscopy, combined with two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy, matrix-assisted laser desorption ionization time-of-flight mass spectrometry, and high-performance liquid chromatography (HPLC)-profiling of 2-aminobenzamide-labeled glycans combined with exoglycosidase digestions.
17293352	8	19	theme	H-	1258:1259	arg1	spectroscopy					1271:1282	two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy	1224:1282	two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy	1224:1282	The structures of the components were analyzed by 500 MHz one-dimensional and 600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H nuclear magnetic resonance spectroscopy, combined with two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy, matrix-assisted laser desorption ionization time-of-flight mass spectrometry, and high-performance liquid chromatography (HPLC)-profiling of 2-aminobenzamide-labeled glycans combined with exoglycosidase digestions.
17293352	11	20	dep	-sialylated	1805:1815	arg1	acid					1849:1852	nearly only N-acetylneuraminic acid	1818:1852	nearly only N-acetylneuraminic acid	1818:1852	For the complex-type glycans (partially) (alpha2-6)-sialylated (nearly only N-acetylneuraminic acid) diantennary structures were found; part of the structures were (alpha1-6)-core-fucosylated or (alpha1-3)-fucosylated in the upper antenna (Lewis x).
17293352	9	21	theme	oligomannose-	1595:1607	arg1	structures					1636:1645	oligomannose-, hybrid-, and complex-type structures	1595:1645	oligomannose-, hybrid-, and complex-type structures	1595:1645	The recombinant rabbit glycoprotein contained a broad array of different N-glycans, comprising oligomannose-, hybrid-, and complex-type structures.
17293352	1	22	theme	glycogen	128:135	arg1	disorder					145:152	a lysosomal glycogen storage disorder	116:152	a lysosomal glycogen storage disorder characterized by acid alpha-glucosidase (GAA) deficiency	116:209	Pompe disease is a lysosomal glycogen storage disorder characterized by acid alpha-glucosidase (GAA) deficiency.
17293352	1	22	theme	glycogen	128:135	arg1	disease					105:111	Pompe disease	99:111	Pompe disease	99:111	Pompe disease is a lysosomal glycogen storage disorder characterized by acid alpha-glucosidase (GAA) deficiency.
17293352	9	23	theme	recombinant	1504:1514	arg1	glycoprotein					1523:1534	The recombinant rabbit glycoprotein	1500:1534	The recombinant rabbit glycoprotein	1500:1534	The recombinant rabbit glycoprotein contained a broad array of different N-glycans, comprising oligomannose-, hybrid-, and complex-type structures.
17293352	8	24	theme	exoglycosidase	1473:1486	arg1	digestions					1488:1497	exoglycosidase digestions	1473:1497	exoglycosidase digestions	1473:1497	The structures of the components were analyzed by 500 MHz one-dimensional and 600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H nuclear magnetic resonance spectroscopy, combined with two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy, matrix-assisted laser desorption ionization time-of-flight mass spectrometry, and high-performance liquid chromatography (HPLC)-profiling of 2-aminobenzamide-labeled glycans combined with exoglycosidase digestions.
17293352	8	25	theme	H	1263:1263	arg1	HPLC					1407:1410	HPLC	1407:1410	HPLC	1407:1410	The structures of the components were analyzed by 500 MHz one-dimensional and 600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H nuclear magnetic resonance spectroscopy, combined with two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy, matrix-assisted laser desorption ionization time-of-flight mass spectrometry, and high-performance liquid chromatography (HPLC)-profiling of 2-aminobenzamide-labeled glycans combined with exoglycosidase digestions.
17293352	8	25	theme	H	1263:1263	arg1	spectroscopy					1271:1282	two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy	1224:1282	two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy	1224:1282	The structures of the components were analyzed by 500 MHz one-dimensional and 600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H nuclear magnetic resonance spectroscopy, combined with two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy, matrix-assisted laser desorption ionization time-of-flight mass spectrometry, and high-performance liquid chromatography (HPLC)-profiling of 2-aminobenzamide-labeled glycans combined with exoglycosidase digestions.
17293352	6	26	theme	N-linked	629:636	arg1	glycans					638:644	The N-linked glycans	625:644	The N-linked glycans	625:644	The N-linked glycans of recombinant human GAA (rhAGLU), isolated from the rabbit milk, were released by peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase F.
17293352	7	27	theme	agglutinin-affinity	936:954	arg1	chromatography					956:969	Sambucus nigra agglutinin-affinity chromatography	921:969	Sambucus nigra agglutinin-affinity chromatography	921:969	The N-glycan pool was fractionated and purified into individual components by a combination of anion-exchange, normal-phase, and Sambucus nigra agglutinin-affinity chromatography.
17293352	12	28	theme	HPLC-mass	2010:2018	arg1	spectrometry					2020:2031	HPLC-mass spectrometry	2010:2031	HPLC-mass spectrometry of glycopeptides	2010:2048	Using HPLC-mass spectrometry of glycopeptides, information was generated with respect to the site-specific location of the various glycans.
17293352	8	29	theme	MHz	1054:1056	arg1	spectroscopy					1150:1161	600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy	1050:1161	600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H	1050:1167	The structures of the components were analyzed by 500 MHz one-dimensional and 600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H nuclear magnetic resonance spectroscopy, combined with two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy, matrix-assisted laser desorption ionization time-of-flight mass spectrometry, and high-performance liquid chromatography (HPLC)-profiling of 2-aminobenzamide-labeled glycans combined with exoglycosidase digestions.
17293352	7	30	theme	Sambucus	921:928	arg1	chromatography					956:969	Sambucus nigra agglutinin-affinity chromatography	921:969	Sambucus nigra agglutinin-affinity chromatography	921:969	The N-glycan pool was fractionated and purified into individual components by a combination of anion-exchange, normal-phase, and Sambucus nigra agglutinin-affinity chromatography.
17293352	9	31	theme	broad	1548:1552	arg1	array					1554:1558	a broad array	1546:1558	a broad array	1546:1558	The recombinant rabbit glycoprotein contained a broad array of different N-glycans, comprising oligomannose-, hybrid-, and complex-type structures.
17293352	3	32	theme	intravenous	350:360	arg1	injection					362:370	intravenous injection	350:370	intravenous injection of recombinant forms of the enzyme	350:405	Patients with this disease are being treated by intravenous injection of recombinant forms of the enzyme.
17293352	8	33	theme	matrix-assisted	1285:1299	arg1	spectrometry					1349:1360	matrix-assisted laser desorption ionization time-of-flight mass spectrometry	1285:1360	matrix-assisted laser desorption ionization time-of-flight mass spectrometry	1285:1360	The structures of the components were analyzed by 500 MHz one-dimensional and 600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H nuclear magnetic resonance spectroscopy, combined with two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy, matrix-assisted laser desorption ionization time-of-flight mass spectrometry, and high-performance liquid chromatography (HPLC)-profiling of 2-aminobenzamide-labeled glycans combined with exoglycosidase digestions.
17293352	11	34	theme	-sialylated	1805:1815	arg1	structures					1867:1876	(alpha2-6)-sialylated (nearly only N-acetylneuraminic acid) diantennary structures	1795:1876	(alpha2-6)-sialylated (nearly only N-acetylneuraminic acid) diantennary structures	1795:1876	For the complex-type glycans (partially) (alpha2-6)-sialylated (nearly only N-acetylneuraminic acid) diantennary structures were found; part of the structures were (alpha1-6)-core-fucosylated or (alpha1-3)-fucosylated in the upper antenna (Lewis x).
17293352	0	35	theme	rabbits	90:96	arg1	milk					71:74	the milk	67:74	the milk of transgenic rabbits	67:96	N-glycans of recombinant human acid alpha-glucosidase expressed in the milk of transgenic rabbits.
17293352	9	36	theme	rabbit	1516:1521	arg1	glycoprotein					1523:1534	The recombinant rabbit glycoprotein	1500:1534	The recombinant rabbit glycoprotein	1500:1534	The recombinant rabbit glycoprotein contained a broad array of different N-glycans, comprising oligomannose-, hybrid-, and complex-type structures.
17293352	9	37	gly	glycoprotein	1523:1534	arg1	glycoprotein					1523:1534	The recombinant rabbit glycoprotein	1500:1534	The recombinant rabbit glycoprotein	1500:1534	The recombinant rabbit glycoprotein contained a broad array of different N-glycans, comprising oligomannose-, hybrid-, and complex-type structures.
17293352	8	38	theme	desorption	1307:1316	arg1	spectrometry					1349:1360	matrix-assisted laser desorption ionization time-of-flight mass spectrometry	1285:1360	matrix-assisted laser desorption ionization time-of-flight mass spectrometry	1285:1360	The structures of the components were analyzed by 500 MHz one-dimensional and 600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H nuclear magnetic resonance spectroscopy, combined with two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy, matrix-assisted laser desorption ionization time-of-flight mass spectrometry, and high-performance liquid chromatography (HPLC)-profiling of 2-aminobenzamide-labeled glycans combined with exoglycosidase digestions.
17293352	8	39	theme	MHz	1026:1028	arg1	one-dimensional					1030:1044	500 MHz one-dimensional	1022:1044	500 MHz one-dimensional	1022:1044	The structures of the components were analyzed by 500 MHz one-dimensional and 600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H nuclear magnetic resonance spectroscopy, combined with two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy, matrix-assisted laser desorption ionization time-of-flight mass spectrometry, and high-performance liquid chromatography (HPLC)-profiling of 2-aminobenzamide-labeled glycans combined with exoglycosidase digestions.
17293352	9	40	theme	N-glycans	1573:1581	arg1	array					1554:1558	a broad array	1546:1558	a broad array	1546:1558	The recombinant rabbit glycoprotein contained a broad array of different N-glycans, comprising oligomannose-, hybrid-, and complex-type structures.
17293352	3	41	theme	forms	387:391	arg1	injection					362:370	intravenous injection	350:370	intravenous injection of recombinant forms of the enzyme	350:405	Patients with this disease are being treated by intravenous injection of recombinant forms of the enzyme.
17293352	11	42	gly	-core-fucosylated	1928:1944	arg1	part					1890:1893	part	1890:1893	part of the structures	1890:1911	For the complex-type glycans (partially) (alpha2-6)-sialylated (nearly only N-acetylneuraminic acid) diantennary structures were found; part of the structures were (alpha1-6)-core-fucosylated or (alpha1-3)-fucosylated in the upper antenna (Lewis x).
17293352	8	43	theme	time-of-flight	1329:1342	arg1	spectrometry					1349:1360	matrix-assisted laser desorption ionization time-of-flight mass spectrometry	1285:1360	matrix-assisted laser desorption ionization time-of-flight mass spectrometry	1285:1360	The structures of the components were analyzed by 500 MHz one-dimensional and 600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H nuclear magnetic resonance spectroscopy, combined with two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy, matrix-assisted laser desorption ionization time-of-flight mass spectrometry, and high-performance liquid chromatography (HPLC)-profiling of 2-aminobenzamide-labeled glycans combined with exoglycosidase digestions.
17293352	10	44	theme	oligomannose-type	1660:1676	arg1	glycans					1678:1684	the oligomannose-type glycans	1656:1684	the oligomannose-type glycans	1656:1684	Part of the oligomannose-type glycans showed the presence of phospho-diester-bridged N-acetylglucosamine.
17293352	9	45	theme	hybrid-	1610:1616	arg1	structures					1636:1645	oligomannose-, hybrid-, and complex-type structures	1595:1645	oligomannose-, hybrid-, and complex-type structures	1595:1645	The recombinant rabbit glycoprotein contained a broad array of different N-glycans, comprising oligomannose-, hybrid-, and complex-type structures.
17293352	10	46	theme	phospho-diester-bridged	1709:1731	arg1	N-acetylglucosamine					1733:1751	phospho-diester-bridged N-acetylglucosamine	1709:1751	phospho-diester-bridged N-acetylglucosamine	1709:1751	Part of the oligomannose-type glycans showed the presence of phospho-diester-bridged N-acetylglucosamine.
17293352	0	47	theme	recombinant	13:23	arg1	alpha-glucosidase					36:52	recombinant human acid alpha-glucosidase	13:52	recombinant human acid alpha-glucosidase	13:52	N-glycans of recombinant human acid alpha-glucosidase expressed in the milk of transgenic rabbits.
17293352	6	48	link	N-linked	629:636	arg1	glycans					638:644	The N-linked glycans	625:644	The N-linked glycans	625:644	The N-linked glycans of recombinant human GAA (rhAGLU), isolated from the rabbit milk, were released by peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase F.
17293352	6	49	theme	human	661:665	arg1	rhAGLU					672:677	rhAGLU	672:677	rhAGLU	672:677	The N-linked glycans of recombinant human GAA (rhAGLU), isolated from the rabbit milk, were released by peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase F.
17293352	6	49	theme	human	661:665	arg1	GAA					667:669	recombinant human GAA	649:669	recombinant human GAA (rhAGLU)	649:678	The N-linked glycans of recombinant human GAA (rhAGLU), isolated from the rabbit milk, were released by peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase F.
17293352	0	50	theme	acid	31:34	arg1	alpha-glucosidase					36:52	recombinant human acid alpha-glucosidase	13:52	recombinant human acid alpha-glucosidase	13:52	N-glycans of recombinant human acid alpha-glucosidase expressed in the milk of transgenic rabbits.
17293352	8	51	theme	two-dimensional	1063:1077	arg1	spectroscopy					1150:1161	600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy	1050:1161	600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H	1050:1167	The structures of the components were analyzed by 500 MHz one-dimensional and 600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H nuclear magnetic resonance spectroscopy, combined with two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy, matrix-assisted laser desorption ionization time-of-flight mass spectrometry, and high-performance liquid chromatography (HPLC)-profiling of 2-aminobenzamide-labeled glycans combined with exoglycosidase digestions.
17293352	8	52	theme	liquid	1384:1389	arg1	chromatography					1391:1404	high-performance liquid chromatography	1367:1404	high-performance liquid chromatography	1367:1404	The structures of the components were analyzed by 500 MHz one-dimensional and 600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H nuclear magnetic resonance spectroscopy, combined with two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy, matrix-assisted laser desorption ionization time-of-flight mass spectrometry, and high-performance liquid chromatography (HPLC)-profiling of 2-aminobenzamide-labeled glycans combined with exoglycosidase digestions.
17293352	8	53	theme	total	1080:1084	arg1	spectroscopy					1098:1109	total correlation spectroscopy	1080:1109	600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H	1050:1167	The structures of the components were analyzed by 500 MHz one-dimensional and 600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H nuclear magnetic resonance spectroscopy, combined with two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy, matrix-assisted laser desorption ionization time-of-flight mass spectrometry, and high-performance liquid chromatography (HPLC)-profiling of 2-aminobenzamide-labeled glycans combined with exoglycosidase digestions.
17293352	9	54	theme	complex-type	1623:1634	arg1	structures					1636:1645	oligomannose-, hybrid-, and complex-type structures	1595:1645	oligomannose-, hybrid-, and complex-type structures	1595:1645	The recombinant rabbit glycoprotein contained a broad array of different N-glycans, comprising oligomannose-, hybrid-, and complex-type structures.
17293352	4	55	theme	glycosylation	527:539	arg1	patterns					541:548	the generated glycosylation patterns	513:548	the generated glycosylation patterns	513:548	Focusing on recombinant approaches to produce the enzyme means that specific attention has to be paid to the generated glycosylation patterns.
17293352	8	56	dep	H	1167:1167	arg1	1					1165:1165	1	1165:1165	1	1165:1165	The structures of the components were analyzed by 500 MHz one-dimensional and 600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H nuclear magnetic resonance spectroscopy, combined with two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy, matrix-assisted laser desorption ionization time-of-flight mass spectrometry, and high-performance liquid chromatography (HPLC)-profiling of 2-aminobenzamide-labeled glycans combined with exoglycosidase digestions.
17293352	8	57	theme	spectroscopy	1098:1109	arg1	[TOCSY					1111:1116	total correlation spectroscopy [TOCSY	1080:1116	600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H	1050:1167	The structures of the components were analyzed by 500 MHz one-dimensional and 600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H nuclear magnetic resonance spectroscopy, combined with two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy, matrix-assisted laser desorption ionization time-of-flight mass spectrometry, and high-performance liquid chromatography (HPLC)-profiling of 2-aminobenzamide-labeled glycans combined with exoglycosidase digestions.
17293352	12	58	gly	glycopeptides	2036:2048	arg2	glycopeptides					2036:2048	glycopeptides	2036:2048	glycopeptides	2036:2048	Using HPLC-mass spectrometry of glycopeptides, information was generated with respect to the site-specific location of the various glycans.
17293352	7	59	theme	individual	845:854	arg1	components					856:865	individual components	845:865	individual components	845:865	The N-glycan pool was fractionated and purified into individual components by a combination of anion-exchange, normal-phase, and Sambucus nigra agglutinin-affinity chromatography.
17293352	8	60	theme	Overhauser	1127:1136	arg1	spectroscopy					1150:1161	600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy	1050:1161	600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H	1050:1167	The structures of the components were analyzed by 500 MHz one-dimensional and 600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H nuclear magnetic resonance spectroscopy, combined with two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy, matrix-assisted laser desorption ionization time-of-flight mass spectrometry, and high-performance liquid chromatography (HPLC)-profiling of 2-aminobenzamide-labeled glycans combined with exoglycosidase digestions.
17293352	8	61	theme	spectroscopy	1150:1161	arg1	H					1167:1167	600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H	1050:1167	600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H	1050:1167	The structures of the components were analyzed by 500 MHz one-dimensional and 600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H nuclear magnetic resonance spectroscopy, combined with two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy, matrix-assisted laser desorption ionization time-of-flight mass spectrometry, and high-performance liquid chromatography (HPLC)-profiling of 2-aminobenzamide-labeled glycans combined with exoglycosidase digestions.
17293352	5	62	theme	transgenic	605:614	arg1	rabbits					616:622	transgenic rabbits	605:622	transgenic rabbits	605:622	Here, human GAA was expressed in the mammary gland of transgenic rabbits.
17293352	1	63	theme	acid	171:174	arg1	GAA					195:197	GAA	195:197	GAA	195:197	Pompe disease is a lysosomal glycogen storage disorder characterized by acid alpha-glucosidase (GAA) deficiency.
17293352	1	63	theme	acid	171:174	arg1	alpha-glucosidase					176:192	acid alpha-glucosidase	171:192	acid alpha-glucosidase (GAA) deficiency	171:209	Pompe disease is a lysosomal glycogen storage disorder characterized by acid alpha-glucosidase (GAA) deficiency.
17293352	11	64	dep	-core-fucosylated	1928:1944	arg1	alpha1-6					1919:1926	alpha1-6	1919:1926	alpha1-6	1919:1926	For the complex-type glycans (partially) (alpha2-6)-sialylated (nearly only N-acetylneuraminic acid) diantennary structures were found; part of the structures were (alpha1-6)-core-fucosylated or (alpha1-3)-fucosylated in the upper antenna (Lewis x).
17293352	11	64	dep	-core-fucosylated	1928:1944	arg1	x					2000:2000	Lewis x	1994:2000	Lewis x	1994:2000	For the complex-type glycans (partially) (alpha2-6)-sialylated (nearly only N-acetylneuraminic acid) diantennary structures were found; part of the structures were (alpha1-6)-core-fucosylated or (alpha1-3)-fucosylated in the upper antenna (Lewis x).
17293352	8	65	theme	components	994:1003	arg1	structures					976:985	The structures	972:985	The structures of the components	972:1003	The structures of the components were analyzed by 500 MHz one-dimensional and 600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H nuclear magnetic resonance spectroscopy, combined with two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy, matrix-assisted laser desorption ionization time-of-flight mass spectrometry, and high-performance liquid chromatography (HPLC)-profiling of 2-aminobenzamide-labeled glycans combined with exoglycosidase digestions.
17293352	11	66	theme	diantennary	1855:1865	arg1	structures					1867:1876	(alpha2-6)-sialylated (nearly only N-acetylneuraminic acid) diantennary structures	1795:1876	(alpha2-6)-sialylated (nearly only N-acetylneuraminic acid) diantennary structures	1795:1876	For the complex-type glycans (partially) (alpha2-6)-sialylated (nearly only N-acetylneuraminic acid) diantennary structures were found; part of the structures were (alpha1-6)-core-fucosylated or (alpha1-3)-fucosylated in the upper antenna (Lewis x).
17293352	8	67	theme	nuclear	1169:1175	arg1	spectroscopy					1196:1207	500 MHz one-dimensional and 600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H nuclear magnetic resonance spectroscopy	1022:1207	500 MHz one-dimensional and 600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H nuclear magnetic resonance spectroscopy	1022:1207	The structures of the components were analyzed by 500 MHz one-dimensional and 600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H nuclear magnetic resonance spectroscopy, combined with two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy, matrix-assisted laser desorption ionization time-of-flight mass spectrometry, and high-performance liquid chromatography (HPLC)-profiling of 2-aminobenzamide-labeled glycans combined with exoglycosidase digestions.
17293352	12	68	theme	various	2127:2133	arg1	glycans					2135:2141	the various glycans	2123:2141	the various glycans	2123:2141	Using HPLC-mass spectrometry of glycopeptides, information was generated with respect to the site-specific location of the various glycans.
17293352	11	69	theme	structures	1902:1911	arg1	part					1890:1893	part	1890:1893	part of the structures	1890:1911	For the complex-type glycans (partially) (alpha2-6)-sialylated (nearly only N-acetylneuraminic acid) diantennary structures were found; part of the structures were (alpha1-6)-core-fucosylated or (alpha1-3)-fucosylated in the upper antenna (Lewis x).
17293352	2	70	theme	pathogenic	236:245	arg1	mutations					247:255	More than 110 different pathogenic mutations	212:255	More than 110 different pathogenic mutations in the gene encoding GAA	212:280	More than 110 different pathogenic mutations in the gene encoding GAA have been observed.
17293352	8	71	theme	resonance	1186:1194	arg1	spectroscopy					1196:1207	500 MHz one-dimensional and 600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H nuclear magnetic resonance spectroscopy	1022:1207	500 MHz one-dimensional and 600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H nuclear magnetic resonance spectroscopy	1022:1207	The structures of the components were analyzed by 500 MHz one-dimensional and 600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H nuclear magnetic resonance spectroscopy, combined with two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy, matrix-assisted laser desorption ionization time-of-flight mass spectrometry, and high-performance liquid chromatography (HPLC)-profiling of 2-aminobenzamide-labeled glycans combined with exoglycosidase digestions.
17293352	8	72	theme	glycans	1451:1457	arg1	-profiling					1412:1421	-profiling	1412:1421	-profiling	1412:1421	The structures of the components were analyzed by 500 MHz one-dimensional and 600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H nuclear magnetic resonance spectroscopy, combined with two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy, matrix-assisted laser desorption ionization time-of-flight mass spectrometry, and high-performance liquid chromatography (HPLC)-profiling of 2-aminobenzamide-labeled glycans combined with exoglycosidase digestions.
17293352	11	73	theme	upper	1979:1983	arg1	antenna					1985:1991	the upper antenna	1975:1991	the upper antenna	1975:1991	For the complex-type glycans (partially) (alpha2-6)-sialylated (nearly only N-acetylneuraminic acid) diantennary structures were found; part of the structures were (alpha1-6)-core-fucosylated or (alpha1-3)-fucosylated in the upper antenna (Lewis x).
17293352	9	74	contain	contained	1536:1544	arg2	array					1554:1558	a broad array	1546:1558	a broad array	1546:1558	The recombinant rabbit glycoprotein contained a broad array of different N-glycans, comprising oligomannose-, hybrid-, and complex-type structures.
17293352	9	74	contain	contained	1536:1544	arg1	glycoprotein					1523:1534	The recombinant rabbit glycoprotein	1500:1534	The recombinant rabbit glycoprotein	1500:1534	The recombinant rabbit glycoprotein contained a broad array of different N-glycans, comprising oligomannose-, hybrid-, and complex-type structures.
17293352	4	75	theme	recombinant	420:430	arg1	approaches					432:441	recombinant approaches	420:441	recombinant approaches	420:441	Focusing on recombinant approaches to produce the enzyme means that specific attention has to be paid to the generated glycosylation patterns.
17293352	12	76	theme	site-specific	2097:2109	arg1	location					2111:2118	the site-specific location	2093:2118	the site-specific location of the various glycans	2093:2141	Using HPLC-mass spectrometry of glycopeptides, information was generated with respect to the site-specific location of the various glycans.
17293352	6	77	theme	recombinant	649:659	arg1	rhAGLU					672:677	rhAGLU	672:677	rhAGLU	672:677	The N-linked glycans of recombinant human GAA (rhAGLU), isolated from the rabbit milk, were released by peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase F.
17293352	6	77	theme	recombinant	649:659	arg1	GAA					667:669	recombinant human GAA	649:669	recombinant human GAA (rhAGLU)	649:678	The N-linked glycans of recombinant human GAA (rhAGLU), isolated from the rabbit milk, were released by peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase F.
17293352	5	78	theme	human	557:561	arg1	GAA					563:565	human GAA	557:565	human GAA	557:565	Here, human GAA was expressed in the mammary gland of transgenic rabbits.
17293352	1	79	theme	lysosomal	118:126	arg1	disorder					145:152	a lysosomal glycogen storage disorder	116:152	a lysosomal glycogen storage disorder characterized by acid alpha-glucosidase (GAA) deficiency	116:209	Pompe disease is a lysosomal glycogen storage disorder characterized by acid alpha-glucosidase (GAA) deficiency.
17293352	1	79	theme	lysosomal	118:126	arg1	disease					105:111	Pompe disease	99:111	Pompe disease	99:111	Pompe disease is a lysosomal glycogen storage disorder characterized by acid alpha-glucosidase (GAA) deficiency.
17293352	11	80	from	-core-fucosylated	1928:1944	arg1	antenna					1985:1991	the upper antenna	1975:1991	the upper antenna	1975:1991	For the complex-type glycans (partially) (alpha2-6)-sialylated (nearly only N-acetylneuraminic acid) diantennary structures were found; part of the structures were (alpha1-6)-core-fucosylated or (alpha1-3)-fucosylated in the upper antenna (Lewis x).
17293352	7	81	dep	Sambucus	921:928	arg1	nigra					930:934	nigra	930:934	nigra	930:934	The N-glycan pool was fractionated and purified into individual components by a combination of anion-exchange, normal-phase, and Sambucus nigra agglutinin-affinity chromatography.
17293352	12	82	theme	glycans	2135:2141	arg1	location					2111:2118	the site-specific location	2093:2118	the site-specific location of the various glycans	2093:2141	Using HPLC-mass spectrometry of glycopeptides, information was generated with respect to the site-specific location of the various glycans.
17293352	1	83	theme	storage	137:143	arg1	disorder					145:152	a lysosomal glycogen storage disorder	116:152	a lysosomal glycogen storage disorder characterized by acid alpha-glucosidase (GAA) deficiency	116:209	Pompe disease is a lysosomal glycogen storage disorder characterized by acid alpha-glucosidase (GAA) deficiency.
17293352	1	83	theme	storage	137:143	arg1	disease					105:111	Pompe disease	99:111	Pompe disease	99:111	Pompe disease is a lysosomal glycogen storage disorder characterized by acid alpha-glucosidase (GAA) deficiency.
17293352	0	84	theme	transgenic	79:88	arg1	rabbits					90:96	transgenic rabbits	79:96	transgenic rabbits	79:96	N-glycans of recombinant human acid alpha-glucosidase expressed in the milk of transgenic rabbits.
17293352	7	85	theme	chromatography	956:969	arg1	combination					872:882	a combination	870:882	a combination of anion-exchange, normal-phase, and Sambucus nigra agglutinin-affinity chromatography	870:969	The N-glycan pool was fractionated and purified into individual components by a combination of anion-exchange, normal-phase, and Sambucus nigra agglutinin-affinity chromatography.
17293352	8	86	theme	TOCSY	1265:1269	arg1	HPLC					1407:1410	HPLC	1407:1410	HPLC	1407:1410	The structures of the components were analyzed by 500 MHz one-dimensional and 600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H nuclear magnetic resonance spectroscopy, combined with two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy, matrix-assisted laser desorption ionization time-of-flight mass spectrometry, and high-performance liquid chromatography (HPLC)-profiling of 2-aminobenzamide-labeled glycans combined with exoglycosidase digestions.
17293352	8	86	theme	TOCSY	1265:1269	arg1	spectroscopy					1271:1282	two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy	1224:1282	two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy	1224:1282	The structures of the components were analyzed by 500 MHz one-dimensional and 600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H nuclear magnetic resonance spectroscopy, combined with two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy, matrix-assisted laser desorption ionization time-of-flight mass spectrometry, and high-performance liquid chromatography (HPLC)-profiling of 2-aminobenzamide-labeled glycans combined with exoglycosidase digestions.
17293352	5	87	theme	mammary	588:594	arg1	gland					596:600	the mammary gland	584:600	the mammary gland of transgenic rabbits	584:622	Here, human GAA was expressed in the mammary gland of transgenic rabbits.
17293352	4	88	theme	specific	476:483	arg1	attention					485:493	specific attention	476:493	specific attention	476:493	Focusing on recombinant approaches to produce the enzyme means that specific attention has to be paid to the generated glycosylation patterns.
17293352	6	89	attach	isolated	681:688	arg1	milk					706:709	the rabbit milk	695:709	the rabbit milk	695:709	The N-linked glycans of recombinant human GAA (rhAGLU), isolated from the rabbit milk, were released by peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase F.
17293352	6	89	attach	isolated	681:688	arg2	glycans					638:644	The N-linked glycans	625:644	The N-linked glycans	625:644	The N-linked glycans of recombinant human GAA (rhAGLU), isolated from the rabbit milk, were released by peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase F.
17293352	9	90	theme	different	1563:1571	arg1	N-glycans					1573:1581	different N-glycans	1563:1581	different N-glycans	1563:1581	The recombinant rabbit glycoprotein contained a broad array of different N-glycans, comprising oligomannose-, hybrid-, and complex-type structures.
17293352	8	91	theme	laser	1301:1305	arg1	spectrometry					1349:1360	matrix-assisted laser desorption ionization time-of-flight mass spectrometry	1285:1360	matrix-assisted laser desorption ionization time-of-flight mass spectrometry	1285:1360	The structures of the components were analyzed by 500 MHz one-dimensional and 600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H nuclear magnetic resonance spectroscopy, combined with two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy, matrix-assisted laser desorption ionization time-of-flight mass spectrometry, and high-performance liquid chromatography (HPLC)-profiling of 2-aminobenzamide-labeled glycans combined with exoglycosidase digestions.
17293352	10	92	theme	glycans	1678:1684	arg1	Part					1648:1651	Part	1648:1651	Part of the oligomannose-type glycans	1648:1684	Part of the oligomannose-type glycans showed the presence of phospho-diester-bridged N-acetylglucosamine.
17293352	8	93	theme	600	1050:1052	arg1	MHz					1054:1056	MHz	1054:1056	MHz	1054:1056	The structures of the components were analyzed by 500 MHz one-dimensional and 600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H nuclear magnetic resonance spectroscopy, combined with two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy, matrix-assisted laser desorption ionization time-of-flight mass spectrometry, and high-performance liquid chromatography (HPLC)-profiling of 2-aminobenzamide-labeled glycans combined with exoglycosidase digestions.
17293352	7	94	theme	normal-phase	903:914	arg1	combination					872:882	a combination	870:882	a combination of anion-exchange, normal-phase, and Sambucus nigra agglutinin-affinity chromatography	870:969	The N-glycan pool was fractionated and purified into individual components by a combination of anion-exchange, normal-phase, and Sambucus nigra agglutinin-affinity chromatography.
17293352	3	95	with	Patients	302:309	arg1	disease					321:327	this disease	316:327	this disease	316:327	Patients with this disease are being treated by intravenous injection of recombinant forms of the enzyme.
17293352	8	96	theme	ionization	1318:1327	arg1	spectrometry					1349:1360	matrix-assisted laser desorption ionization time-of-flight mass spectrometry	1285:1360	matrix-assisted laser desorption ionization time-of-flight mass spectrometry	1285:1360	The structures of the components were analyzed by 500 MHz one-dimensional and 600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H nuclear magnetic resonance spectroscopy, combined with two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy, matrix-assisted laser desorption ionization time-of-flight mass spectrometry, and high-performance liquid chromatography (HPLC)-profiling of 2-aminobenzamide-labeled glycans combined with exoglycosidase digestions.
17293352	0	97	theme	human	25:29	arg1	alpha-glucosidase					36:52	recombinant human acid alpha-glucosidase	13:52	recombinant human acid alpha-glucosidase	13:52	N-glycans of recombinant human acid alpha-glucosidase expressed in the milk of transgenic rabbits.
17293352	8	98	theme	cryo	1058:1061	arg1	spectroscopy					1150:1161	600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy	1050:1161	600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H	1050:1167	The structures of the components were analyzed by 500 MHz one-dimensional and 600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H nuclear magnetic resonance spectroscopy, combined with two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy, matrix-assisted laser desorption ionization time-of-flight mass spectrometry, and high-performance liquid chromatography (HPLC)-profiling of 2-aminobenzamide-labeled glycans combined with exoglycosidase digestions.
17293352	7	99	theme	anion-exchange	887:900	arg1	combination					872:882	a combination	870:882	a combination of anion-exchange, normal-phase, and Sambucus nigra agglutinin-affinity chromatography	870:969	The N-glycan pool was fractionated and purified into individual components by a combination of anion-exchange, normal-phase, and Sambucus nigra agglutinin-affinity chromatography.
17293352	1	100	theme	Pompe	99:103	arg1	disorder					145:152	a lysosomal glycogen storage disorder	116:152	a lysosomal glycogen storage disorder characterized by acid alpha-glucosidase (GAA) deficiency	116:209	Pompe disease is a lysosomal glycogen storage disorder characterized by acid alpha-glucosidase (GAA) deficiency.
17293352	1	100	theme	Pompe	99:103	arg1	disease					105:111	Pompe disease	99:111	Pompe disease	99:111	Pompe disease is a lysosomal glycogen storage disorder characterized by acid alpha-glucosidase (GAA) deficiency.
17293352	2	101	from	mutations	247:255	arg1	gene					264:267	the gene	260:267	the gene encoding GAA	260:280	More than 110 different pathogenic mutations in the gene encoding GAA have been observed.
17293352	3	102	theme	recombinant	375:385	arg1	forms					387:391	recombinant forms	375:391	recombinant forms of the enzyme	375:405	Patients with this disease are being treated by intravenous injection of recombinant forms of the enzyme.
17293352	8	103	theme	mass	1344:1347	arg1	spectrometry					1349:1360	matrix-assisted laser desorption ionization time-of-flight mass spectrometry	1285:1360	matrix-assisted laser desorption ionization time-of-flight mass spectrometry	1285:1360	The structures of the components were analyzed by 500 MHz one-dimensional and 600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H nuclear magnetic resonance spectroscopy, combined with two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy, matrix-assisted laser desorption ionization time-of-flight mass spectrometry, and high-performance liquid chromatography (HPLC)-profiling of 2-aminobenzamide-labeled glycans combined with exoglycosidase digestions.
17293352	6	104	theme	GAA	667:669	arg1	glycans					638:644	The N-linked glycans	625:644	The N-linked glycans	625:644	The N-linked glycans of recombinant human GAA (rhAGLU), isolated from the rabbit milk, were released by peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase F.
17293352	0	105	theme	alpha-glucosidase	36:52	arg1	N-glycans					0:8	N-glycans	0:8	N-glycans of recombinant human acid alpha-glucosidase	0:52	N-glycans of recombinant human acid alpha-glucosidase expressed in the milk of transgenic rabbits.
17293352	8	106	dep	spectroscopy	1271:1282	arg1	1					1261:1261	1	1261:1261	1	1261:1261	The structures of the components were analyzed by 500 MHz one-dimensional and 600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H nuclear magnetic resonance spectroscopy, combined with two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy, matrix-assisted laser desorption ionization time-of-flight mass spectrometry, and high-performance liquid chromatography (HPLC)-profiling of 2-aminobenzamide-labeled glycans combined with exoglycosidase digestions.
17293352	8	106	dep	spectroscopy	1271:1282	arg1	1					1256:1256	1	1256:1256	1	1256:1256	The structures of the components were analyzed by 500 MHz one-dimensional and 600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H nuclear magnetic resonance spectroscopy, combined with two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy, matrix-assisted laser desorption ionization time-of-flight mass spectrometry, and high-performance liquid chromatography (HPLC)-profiling of 2-aminobenzamide-labeled glycans combined with exoglycosidase digestions.
17293352	4	107	theme	generated	517:525	arg1	patterns					541:548	the generated glycosylation patterns	513:548	the generated glycosylation patterns	513:548	Focusing on recombinant approaches to produce the enzyme means that specific attention has to be paid to the generated glycosylation patterns.
17293352	8	108	theme	correlation	1086:1096	arg1	spectroscopy					1098:1109	total correlation spectroscopy	1080:1109	600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H	1050:1167	The structures of the components were analyzed by 500 MHz one-dimensional and 600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H nuclear magnetic resonance spectroscopy, combined with two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy, matrix-assisted laser desorption ionization time-of-flight mass spectrometry, and high-performance liquid chromatography (HPLC)-profiling of 2-aminobenzamide-labeled glycans combined with exoglycosidase digestions.
17293352	3	109	theme	enzyme	400:405	arg1	forms					387:391	recombinant forms	375:391	recombinant forms of the enzyme	375:405	Patients with this disease are being treated by intravenous injection of recombinant forms of the enzyme.
17293352	8	110	theme	high-performance	1367:1382	arg1	chromatography					1391:1404	high-performance liquid chromatography	1367:1404	high-performance liquid chromatography	1367:1404	The structures of the components were analyzed by 500 MHz one-dimensional and 600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H nuclear magnetic resonance spectroscopy, combined with two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy, matrix-assisted laser desorption ionization time-of-flight mass spectrometry, and high-performance liquid chromatography (HPLC)-profiling of 2-aminobenzamide-labeled glycans combined with exoglycosidase digestions.
17293352	4	111	contain	has	495:497	arg1	attention					485:493	specific attention	476:493	specific attention	476:493	Focusing on recombinant approaches to produce the enzyme means that specific attention has to be paid to the generated glycosylation patterns.
17293352	4	111	contain	has	495:497	arg2	means					465:469	the enzyme means	454:469	the enzyme means that specific attention has to be paid to the generated glycosylation patterns	454:548	Focusing on recombinant approaches to produce the enzyme means that specific attention has to be paid to the generated glycosylation patterns.
17293352	4	111	contain	has	495:497	arg2	paid					505:508	paid	505:508	paid	505:508	Focusing on recombinant approaches to produce the enzyme means that specific attention has to be paid to the generated glycosylation patterns.
17293352	8	112	theme	[TOCSY	1111:1116	arg1	spectroscopy					1150:1161	600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy	1050:1161	600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H	1050:1167	The structures of the components were analyzed by 500 MHz one-dimensional and 600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H nuclear magnetic resonance spectroscopy, combined with two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy, matrix-assisted laser desorption ionization time-of-flight mass spectrometry, and high-performance liquid chromatography (HPLC)-profiling of 2-aminobenzamide-labeled glycans combined with exoglycosidase digestions.
17293352	11	113	theme	Lewis	1994:1998	arg1	x					2000:2000	Lewis x	1994:2000	Lewis x	1994:2000	For the complex-type glycans (partially) (alpha2-6)-sialylated (nearly only N-acetylneuraminic acid) diantennary structures were found; part of the structures were (alpha1-6)-core-fucosylated or (alpha1-3)-fucosylated in the upper antenna (Lewis x).
17293352	11	114	gly	-sialylated	1805:1815	arg1	structures					1867:1876	(alpha2-6)-sialylated (nearly only N-acetylneuraminic acid) diantennary structures	1795:1876	(alpha2-6)-sialylated (nearly only N-acetylneuraminic acid) diantennary structures	1795:1876	For the complex-type glycans (partially) (alpha2-6)-sialylated (nearly only N-acetylneuraminic acid) diantennary structures were found; part of the structures were (alpha1-6)-core-fucosylated or (alpha1-3)-fucosylated in the upper antenna (Lewis x).
17293352	11	115	theme	complex-type	1762:1773	arg1	glycans					1775:1781	the complex-type glycans	1758:1781	the complex-type glycans (partially)	1758:1793	For the complex-type glycans (partially) (alpha2-6)-sialylated (nearly only N-acetylneuraminic acid) diantennary structures were found; part of the structures were (alpha1-6)-core-fucosylated or (alpha1-3)-fucosylated in the upper antenna (Lewis x).
17293352	10	116	theme	N-acetylglucosamine	1733:1751	arg1	presence					1697:1704	the presence	1693:1704	the presence of phospho-diester-bridged N-acetylglucosamine	1693:1751	Part of the oligomannose-type glycans showed the presence of phospho-diester-bridged N-acetylglucosamine.
17293352	8	117	theme	nuclear	1119:1125	arg1	spectroscopy					1150:1161	600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy	1050:1161	600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H	1050:1167	The structures of the components were analyzed by 500 MHz one-dimensional and 600 MHz cryo two-dimensional (total correlation spectroscopy [TOCSY] nuclear Overhauser enhancement spectroscopy) (1)H nuclear magnetic resonance spectroscopy, combined with two-dimensional (31)P-filtered (1)H-(1)H TOCSY spectroscopy, matrix-assisted laser desorption ionization time-of-flight mass spectrometry, and high-performance liquid chromatography (HPLC)-profiling of 2-aminobenzamide-labeled glycans combined with exoglycosidase digestions.
17293352	6	118	theme	amidase	781:787	arg1	F					789:789	(N-acetyl-beta-glucosaminyl)asparagine amidase F	742:789	(N-acetyl-beta-glucosaminyl)asparagine amidase F	742:789	The N-linked glycans of recombinant human GAA (rhAGLU), isolated from the rabbit milk, were released by peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase F.
17293352	6	119	theme	rabbit	699:704	arg1	milk					706:709	the rabbit milk	695:709	the rabbit milk	695:709	The N-linked glycans of recombinant human GAA (rhAGLU), isolated from the rabbit milk, were released by peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase F.
8615697	4	0	theme	gel	576:578	arg1	chromatography					591:604	gel permeation chromatography	576:604	gel permeation chromatography followed by several steps of HPLC	576:638	Glycopeptides were purified using gel permeation chromatography followed by several steps of HPLC.
8615697	5	1	theme	tryptic	654:660	arg1	glycopeptides					662:674	The purified tryptic glycopeptides	641:674	The purified tryptic glycopeptides	641:674	The purified tryptic glycopeptides were characterized by gas phase sequencing and carbohydrate analysis and located within the amino acid sequence of thyroglobulin.
8615697	2	2	gly	glycopeptides	293:305	arg2	glycopeptides					293:305	the glycopeptides	289:305	the glycopeptides contained in a tryptic digest of hTG	289:342	We have characterized the glycopeptides contained in a tryptic digest of hTG in order to determine which sites are actually linked to carbohydrate.
8615697	6	3	theme	recovered	818:826	arg1	glycopeptides					828:840	the recovered glycopeptides	814:840	the recovered glycopeptides	814:840	Each of the recovered glycopeptides contained a consensus sequence for N-linked glycosylation.
8615697	9	4	theme	high	1362:1365	arg1	units					1380:1384	high mannose type units	1362:1384	high mannose type units	1362:1384	Five sites (at positions 1200, 1329, 1993, 2275, and 2562) contain high mannose type units and two sites (at positions 179 and 1345) are linked to oligosaccharide units containing galactose in addition to mannose and glucosamine but no fucose and may be either hybrid or complex structures.
8615697	8	5	theme	oligosaccharide	1201:1215	arg1	units					1217:1221	complex-type oligosaccharide units	1188:1221	complex-type oligosaccharide units containing fucose and galactose in addition to mannose and glucosamine	1188:1292	Eight of these confirmed glycosylation sites (at positions 57, 465, 510, 729, 797, 1696, 1754, and 2230) appear to be linked to complex-type oligosaccharide units containing fucose and galactose in addition to mannose and glucosamine.
8615697	9	6	theme	type	1375:1378	arg1	units					1380:1384	high mannose type units	1362:1384	high mannose type units	1362:1384	Five sites (at positions 1200, 1329, 1993, 2275, and 2562) contain high mannose type units and two sites (at positions 179 and 1345) are linked to oligosaccharide units containing galactose in addition to mannose and glucosamine but no fucose and may be either hybrid or complex structures.
8615697	10	7	theme	oligosaccharide	1687:1701	arg1	types					1715:1719	very different oligosaccharide composition types	1672:1719	very different oligosaccharide composition types	1672:1719	In addition, position 928 was found to be degenerate in oligosaccharide structure and very different oligosaccharide composition types were found associated with peptides containing the same amino acid sequence.
8615697	13	8	theme	purified	2342:2349	arg1	population					2364:2373	the purified glycopeptide population	2338:2373	the purified glycopeptide population	2338:2373	Only four of the 20 putative sites the sequence of hTG, at asparagine residues 91, 477, 1849, and 2102 were not represented in the purified glycopeptide population and are presumed to escape significant glycosylation.
8615697	11	9	theme	asparagine	1869:1878	arg1	residue					1880:1886	the glycosylated asparagine residue	1852:1886	the glycosylated asparagine residue	1852:1886	A high probability of a beta turn which would include the glycosylated asparagine residue was predicted for the amino acid sequence found at 13 of the 16 sites.
8615697	4	10	theme	HPLC	635:638	arg1	steps					626:630	several steps	618:630	several steps of HPLC	618:638	Glycopeptides were purified using gel permeation chromatography followed by several steps of HPLC.
8615697	7	11	from	sites	943:947	arg1	chain					988:992	the human thyroglobulin polypeptide chain	952:992	the human thyroglobulin polypeptide chain	952:992	Of the 20 putative N-linked glycosylation sites in the human thyroglobulin polypeptide chain, 16 were shown to be actually glycosylated in the mature protein.
8615697	11	12	theme	sites	1952:1956	arg1	sites					1952:1956	the 16 sites	1945:1956	the 16 sites	1945:1956	A high probability of a beta turn which would include the glycosylated asparagine residue was predicted for the amino acid sequence found at 13 of the 16 sites.
8615697	11	12	theme	sites	1952:1956	arg1	13					1939:1940	13	1939:1940	13	1939:1940	A high probability of a beta turn which would include the glycosylated asparagine residue was predicted for the amino acid sequence found at 13 of the 16 sites.
8615697	12	13	theme	N-terminal	2184:2193	arg1	portion					2195:2201	the N-terminal portion	2180:2201	the N-terminal portion of hTG	2180:2208	The glycosylation pattern in hTG was also compared with the data recently reported for bovine thyroglobulin (bTG) (27) and as has been recently reported for bTG, no oligosaccharides of the high mannose type were found in the N-terminal portion of hTG.
8615697	11	14	located	found	1930:1934	arg1	sites					1952:1956	the 16 sites	1945:1956	the 16 sites	1945:1956	A high probability of a beta turn which would include the glycosylated asparagine residue was predicted for the amino acid sequence found at 13 of the 16 sites.
8615697	11	14	located	found	1930:1934	arg2	sequence					1921:1928	the amino acid sequence	1906:1928	the amino acid sequence found at 13 of the 16 sites	1906:1956	A high probability of a beta turn which would include the glycosylated asparagine residue was predicted for the amino acid sequence found at 13 of the 16 sites.
8615697	11	14	located	found	1930:1934	arg1	13					1939:1940	13	1939:1940	13	1939:1940	A high probability of a beta turn which would include the glycosylated asparagine residue was predicted for the amino acid sequence found at 13 of the 16 sites.
8615697	7	15	theme	mature	1044:1049	arg1	protein					1051:1057	the mature protein	1040:1057	the mature protein	1040:1057	Of the 20 putative N-linked glycosylation sites in the human thyroglobulin polypeptide chain, 16 were shown to be actually glycosylated in the mature protein.
8615697	1	16	contain	contains	216:223	arg2	sites					260:264	20 putative N-linked glycosylation sites	225:264	20 putative N-linked glycosylation sites	225:264	The amino acid sequence established for human thyroglobulin (hTG) from its cDNA sequence contains 20 putative N-linked glycosylation sites.
8615697	1	16	contain	contains	216:223	arg1	sequence					142:149	The amino acid sequence	127:149	The amino acid sequence established for human thyroglobulin (hTG) from its cDNA sequence	127:214	The amino acid sequence established for human thyroglobulin (hTG) from its cDNA sequence contains 20 putative N-linked glycosylation sites.
8615697	5	17	theme	phase	702:706	arg1	sequencing					708:717	gas phase sequencing	698:717	gas phase sequencing	698:717	The purified tryptic glycopeptides were characterized by gas phase sequencing and carbohydrate analysis and located within the amino acid sequence of thyroglobulin.
8615697	11	18	theme	amino	1910:1914	arg1	sequence					1921:1928	the amino acid sequence	1906:1928	the amino acid sequence found at 13 of the 16 sites	1906:1956	A high probability of a beta turn which would include the glycosylated asparagine residue was predicted for the amino acid sequence found at 13 of the 16 sites.
8615697	1	19	theme	acid	137:140	arg1	sequence					142:149	The amino acid sequence	127:149	The amino acid sequence established for human thyroglobulin (hTG) from its cDNA sequence	127:214	The amino acid sequence established for human thyroglobulin (hTG) from its cDNA sequence contains 20 putative N-linked glycosylation sites.
8615697	7	20	gly	glycosylation	929:941	arg2	sites					943:947	the 20 putative N-linked glycosylation sites	904:947	the 20 putative N-linked glycosylation sites in the human thyroglobulin polypeptide chain	904:992	Of the 20 putative N-linked glycosylation sites in the human thyroglobulin polypeptide chain, 16 were shown to be actually glycosylated in the mature protein.
8615697	7	20	gly	glycosylation	929:941	arg2	20					908:909	20	908:909	20	908:909	Of the 20 putative N-linked glycosylation sites in the human thyroglobulin polypeptide chain, 16 were shown to be actually glycosylated in the mature protein.
8615697	8	21	attach	linked	1178:1183	arg1	units					1217:1221	complex-type oligosaccharide units	1188:1221	complex-type oligosaccharide units containing fucose and galactose in addition to mannose and glucosamine	1188:1292	Eight of these confirmed glycosylation sites (at positions 57, 465, 510, 729, 797, 1696, 1754, and 2230) appear to be linked to complex-type oligosaccharide units containing fucose and galactose in addition to mannose and glucosamine.
8615697	8	21	attach	linked	1178:1183	arg2	sites					1099:1103	these confirmed glycosylation sites	1069:1103	these confirmed glycosylation sites	1069:1103	Eight of these confirmed glycosylation sites (at positions 57, 465, 510, 729, 797, 1696, 1754, and 2230) appear to be linked to complex-type oligosaccharide units containing fucose and galactose in addition to mannose and glucosamine.
8615697	8	21	attach	linked	1178:1183	arg2	Eight					1060:1064	Eight	1060:1064	Eight	1060:1064	Eight of these confirmed glycosylation sites (at positions 57, 465, 510, 729, 797, 1696, 1754, and 2230) appear to be linked to complex-type oligosaccharide units containing fucose and galactose in addition to mannose and glucosamine.
8615697	5	22	theme	acid	774:777	arg1	sequence					779:786	the amino acid sequence	764:786	the amino acid sequence of thyroglobulin	764:803	The purified tryptic glycopeptides were characterized by gas phase sequencing and carbohydrate analysis and located within the amino acid sequence of thyroglobulin.
8615697	12	23	theme	glycosylation	1963:1975	arg1	pattern					1977:1983	The glycosylation pattern	1959:1983	The glycosylation pattern in hTG	1959:1990	The glycosylation pattern in hTG was also compared with the data recently reported for bovine thyroglobulin (bTG) (27) and as has been recently reported for bTG, no oligosaccharides of the high mannose type were found in the N-terminal portion of hTG.
8615697	8	24	gly	glycosylation	1085:1097	arg2	sites					1099:1103	these confirmed glycosylation sites	1069:1103	these confirmed glycosylation sites	1069:1103	Eight of these confirmed glycosylation sites (at positions 57, 465, 510, 729, 797, 1696, 1754, and 2230) appear to be linked to complex-type oligosaccharide units containing fucose and galactose in addition to mannose and glucosamine.
8615697	0	25	theme	units	79:83	arg1	location					38:45	location	38:45	location of the N-linked oligosaccharide units	38:83	Glycosylation in human thyroglobulin: location of the N-linked oligosaccharide units and comparison with bovine thyroglobulin.
8615697	0	25	theme	units	79:83	arg1	comparison					89:98	comparison	89:98	comparison with bovine thyroglobulin	89:124	Glycosylation in human thyroglobulin: location of the N-linked oligosaccharide units and comparison with bovine thyroglobulin.
8615697	1	26	theme	human	167:171	arg1	hTG					188:190	hTG	188:190	hTG	188:190	The amino acid sequence established for human thyroglobulin (hTG) from its cDNA sequence contains 20 putative N-linked glycosylation sites.
8615697	1	26	theme	human	167:171	arg1	thyroglobulin					173:185	human thyroglobulin	167:185	human thyroglobulin (hTG)	167:191	The amino acid sequence established for human thyroglobulin (hTG) from its cDNA sequence contains 20 putative N-linked glycosylation sites.
8615697	0	27	from	Glycosylation	0:12	arg1	thyroglobulin					23:35	human thyroglobulin	17:35	human thyroglobulin	17:35	Glycosylation in human thyroglobulin: location of the N-linked oligosaccharide units and comparison with bovine thyroglobulin.
8615697	11	28	theme	beta	1822:1825	arg1	turn					1827:1830	a beta turn	1820:1830	a beta turn which would include the glycosylated asparagine residue	1820:1886	A high probability of a beta turn which would include the glycosylated asparagine residue was predicted for the amino acid sequence found at 13 of the 16 sites.
8615697	0	29	theme	bovine	105:110	arg1	thyroglobulin					112:124	bovine thyroglobulin	105:124	bovine thyroglobulin	105:124	Glycosylation in human thyroglobulin: location of the N-linked oligosaccharide units and comparison with bovine thyroglobulin.
8615697	8	30	theme	confirmed	1075:1083	arg1	sites					1099:1103	these confirmed glycosylation sites	1069:1103	these confirmed glycosylation sites	1069:1103	Eight of these confirmed glycosylation sites (at positions 57, 465, 510, 729, 797, 1696, 1754, and 2230) appear to be linked to complex-type oligosaccharide units containing fucose and galactose in addition to mannose and glucosamine.
8615697	7	31	theme	polypeptide	976:986	arg1	chain					988:992	the human thyroglobulin polypeptide chain	952:992	the human thyroglobulin polypeptide chain	952:992	Of the 20 putative N-linked glycosylation sites in the human thyroglobulin polypeptide chain, 16 were shown to be actually glycosylated in the mature protein.
8615697	0	32	theme	oligosaccharide	63:77	arg1	units					79:83	the N-linked oligosaccharide units	50:83	the N-linked oligosaccharide units	50:83	Glycosylation in human thyroglobulin: location of the N-linked oligosaccharide units and comparison with bovine thyroglobulin.
8615697	13	33	theme	significant	2402:2412	arg1	glycosylation					2414:2426	significant glycosylation	2402:2426	significant glycosylation	2402:2426	Only four of the 20 putative sites the sequence of hTG, at asparagine residues 91, 477, 1849, and 2102 were not represented in the purified glycopeptide population and are presumed to escape significant glycosylation.
8615697	8	34	theme	sites	1099:1103	arg1	sites					1099:1103	these confirmed glycosylation sites	1069:1103	these confirmed glycosylation sites	1069:1103	Eight of these confirmed glycosylation sites (at positions 57, 465, 510, 729, 797, 1696, 1754, and 2230) appear to be linked to complex-type oligosaccharide units containing fucose and galactose in addition to mannose and glucosamine.
8615697	8	34	theme	sites	1099:1103	arg1	Eight					1060:1064	Eight	1060:1064	Eight	1060:1064	Eight of these confirmed glycosylation sites (at positions 57, 465, 510, 729, 797, 1696, 1754, and 2230) appear to be linked to complex-type oligosaccharide units containing fucose and galactose in addition to mannose and glucosamine.
8615697	7	35	theme	human	956:960	arg1	chain					988:992	the human thyroglobulin polypeptide chain	952:992	the human thyroglobulin polypeptide chain	952:992	Of the 20 putative N-linked glycosylation sites in the human thyroglobulin polypeptide chain, 16 were shown to be actually glycosylated in the mature protein.
8615697	3	36	theme	type	464:467	arg1	s					469:469	oligosaccharide type(s)	448:470	oligosaccharide type(s)	448:470	In addition, the distribution of oligosaccharide type(s) at these confirmed sites of N-linked glycosylation has been examined.
8615697	0	37	theme	human	17:21	arg1	thyroglobulin					23:35	human thyroglobulin	17:35	human thyroglobulin	17:35	Glycosylation in human thyroglobulin: location of the N-linked oligosaccharide units and comparison with bovine thyroglobulin.
8615697	10	38	theme	oligosaccharide	1642:1656	arg1	structure					1658:1666	oligosaccharide structure	1642:1666	oligosaccharide structure	1642:1666	In addition, position 928 was found to be degenerate in oligosaccharide structure and very different oligosaccharide composition types were found associated with peptides containing the same amino acid sequence.
8615697	13	39	theme	hTG	2262:2264	arg1	four					2216:2219	four	2216:2219	four	2216:2219	Only four of the 20 putative sites the sequence of hTG, at asparagine residues 91, 477, 1849, and 2102 were not represented in the purified glycopeptide population and are presumed to escape significant glycosylation.
8615697	13	39	theme	hTG	2262:2264	arg1	hTG					2262:2264	hTG	2262:2264	hTG	2262:2264	Only four of the 20 putative sites the sequence of hTG, at asparagine residues 91, 477, 1849, and 2102 were not represented in the purified glycopeptide population and are presumed to escape significant glycosylation.
8615697	13	39	theme	hTG	2262:2264	arg1	sites					2240:2244	the 20 putative sites	2224:2244	the 20 putative sites	2224:2244	Only four of the 20 putative sites the sequence of hTG, at asparagine residues 91, 477, 1849, and 2102 were not represented in the purified glycopeptide population and are presumed to escape significant glycosylation.
8615697	0	40	theme	N-linked	54:61	arg1	units					79:83	the N-linked oligosaccharide units	50:83	the N-linked oligosaccharide units	50:83	Glycosylation in human thyroglobulin: location of the N-linked oligosaccharide units and comparison with bovine thyroglobulin.
8615697	10	41	theme	acid	1783:1786	arg1	sequence					1788:1795	the same amino acid sequence	1768:1795	the same amino acid sequence	1768:1795	In addition, position 928 was found to be degenerate in oligosaccharide structure and very different oligosaccharide composition types were found associated with peptides containing the same amino acid sequence.
8615697	10	42	contain	containing	1757:1766	arg1	peptides					1748:1755	peptides	1748:1755	peptides containing the same amino acid sequence	1748:1795	In addition, position 928 was found to be degenerate in oligosaccharide structure and very different oligosaccharide composition types were found associated with peptides containing the same amino acid sequence.
8615697	10	42	contain	containing	1757:1766	arg2	sequence					1788:1795	the same amino acid sequence	1768:1795	the same amino acid sequence	1768:1795	In addition, position 928 was found to be degenerate in oligosaccharide structure and very different oligosaccharide composition types were found associated with peptides containing the same amino acid sequence.
8615697	7	43	link	N-linked	920:927	arg1	sites					943:947	the 20 putative N-linked glycosylation sites	904:947	the 20 putative N-linked glycosylation sites in the human thyroglobulin polypeptide chain	904:992	Of the 20 putative N-linked glycosylation sites in the human thyroglobulin polypeptide chain, 16 were shown to be actually glycosylated in the mature protein.
8615697	13	44	theme	sites	2240:2244	arg1	four					2216:2219	four	2216:2219	four	2216:2219	Only four of the 20 putative sites the sequence of hTG, at asparagine residues 91, 477, 1849, and 2102 were not represented in the purified glycopeptide population and are presumed to escape significant glycosylation.
8615697	13	44	theme	sites	2240:2244	arg1	hTG					2262:2264	hTG	2262:2264	hTG	2262:2264	Only four of the 20 putative sites the sequence of hTG, at asparagine residues 91, 477, 1849, and 2102 were not represented in the purified glycopeptide population and are presumed to escape significant glycosylation.
8615697	13	44	theme	sites	2240:2244	arg1	sites					2240:2244	the 20 putative sites	2224:2244	the 20 putative sites	2224:2244	Only four of the 20 putative sites the sequence of hTG, at asparagine residues 91, 477, 1849, and 2102 were not represented in the purified glycopeptide population and are presumed to escape significant glycosylation.
8615697	11	45	gly	glycosylated	1856:1867	arg1	residue					1880:1886	the glycosylated asparagine residue	1852:1886	the glycosylated asparagine residue	1852:1886	A high probability of a beta turn which would include the glycosylated asparagine residue was predicted for the amino acid sequence found at 13 of the 16 sites.
8615697	3	46	theme	s	469:469	arg1	distribution					432:443	the distribution	428:443	the distribution of oligosaccharide type(s) at these confirmed sites of N-linked glycosylation	428:521	In addition, the distribution of oligosaccharide type(s) at these confirmed sites of N-linked glycosylation has been examined.
8615697	6	47	theme	consensus	854:862	arg1	sequence					864:871	a consensus sequence	852:871	a consensus sequence for N-linked glycosylation	852:898	Each of the recovered glycopeptides contained a consensus sequence for N-linked glycosylation.
8615697	11	48	theme	high	1800:1803	arg1	probability					1805:1815	A high probability	1798:1815	A high probability of a beta turn which would include the glycosylated asparagine residue	1798:1886	A high probability of a beta turn which would include the glycosylated asparagine residue was predicted for the amino acid sequence found at 13 of the 16 sites.
8615697	1	49	theme	putative	228:235	arg1	sites					260:264	20 putative N-linked glycosylation sites	225:264	20 putative N-linked glycosylation sites	225:264	The amino acid sequence established for human thyroglobulin (hTG) from its cDNA sequence contains 20 putative N-linked glycosylation sites.
8615697	0	50	dep	Glycosylation	0:12	arg1	location					38:45	location	38:45	location of the N-linked oligosaccharide units	38:83	Glycosylation in human thyroglobulin: location of the N-linked oligosaccharide units and comparison with bovine thyroglobulin.
8615697	0	50	dep	Glycosylation	0:12	arg1	comparison					89:98	comparison	89:98	comparison with bovine thyroglobulin	89:124	Glycosylation in human thyroglobulin: location of the N-linked oligosaccharide units and comparison with bovine thyroglobulin.
8615697	4	51	theme	several	618:624	arg1	steps					626:630	several steps	618:630	several steps of HPLC	618:638	Glycopeptides were purified using gel permeation chromatography followed by several steps of HPLC.
8615697	5	52	theme	purified	645:652	arg1	glycopeptides					662:674	The purified tryptic glycopeptides	641:674	The purified tryptic glycopeptides	641:674	The purified tryptic glycopeptides were characterized by gas phase sequencing and carbohydrate analysis and located within the amino acid sequence of thyroglobulin.
8615697	3	53	theme	confirmed	481:489	arg1	sites					491:495	these confirmed sites	475:495	these confirmed sites of N-linked glycosylation	475:521	In addition, the distribution of oligosaccharide type(s) at these confirmed sites of N-linked glycosylation has been examined.
8615697	3	53	theme	confirmed	481:489	arg1	glycosylation					509:521	N-linked glycosylation	500:521	N-linked glycosylation	500:521	In addition, the distribution of oligosaccharide type(s) at these confirmed sites of N-linked glycosylation has been examined.
8615697	7	54	theme	N-linked	920:927	arg1	sites					943:947	the 20 putative N-linked glycosylation sites	904:947	the 20 putative N-linked glycosylation sites in the human thyroglobulin polypeptide chain	904:992	Of the 20 putative N-linked glycosylation sites in the human thyroglobulin polypeptide chain, 16 were shown to be actually glycosylated in the mature protein.
8615697	1	55	theme	glycosylation	246:258	arg1	sites					260:264	20 putative N-linked glycosylation sites	225:264	20 putative N-linked glycosylation sites	225:264	The amino acid sequence established for human thyroglobulin (hTG) from its cDNA sequence contains 20 putative N-linked glycosylation sites.
8615697	9	56	theme	hybrid	1556:1561	arg1	structures					1574:1583	either hybrid or complex structures	1549:1583	structures	1574:1583	Five sites (at positions 1200, 1329, 1993, 2275, and 2562) contain high mannose type units and two sites (at positions 179 and 1345) are linked to oligosaccharide units containing galactose in addition to mannose and glucosamine but no fucose and may be either hybrid or complex structures.
8615697	10	57	theme	same	1772:1775	arg1	sequence					1788:1795	the same amino acid sequence	1768:1795	the same amino acid sequence	1768:1795	In addition, position 928 was found to be degenerate in oligosaccharide structure and very different oligosaccharide composition types were found associated with peptides containing the same amino acid sequence.
8615697	1	58	link	N-linked	237:244	arg1	sites					260:264	20 putative N-linked glycosylation sites	225:264	20 putative N-linked glycosylation sites	225:264	The amino acid sequence established for human thyroglobulin (hTG) from its cDNA sequence contains 20 putative N-linked glycosylation sites.
8615697	13	59	theme	glycopeptide	2351:2362	arg1	population					2364:2373	the purified glycopeptide population	2338:2373	the purified glycopeptide population	2338:2373	Only four of the 20 putative sites the sequence of hTG, at asparagine residues 91, 477, 1849, and 2102 were not represented in the purified glycopeptide population and are presumed to escape significant glycosylation.
8615697	3	60	from	sites	491:495	arg1	distribution					432:443	the distribution	428:443	the distribution of oligosaccharide type(s) at these confirmed sites of N-linked glycosylation	428:521	In addition, the distribution of oligosaccharide type(s) at these confirmed sites of N-linked glycosylation has been examined.
8615697	10	61	theme	composition	1703:1713	arg1	types					1715:1719	very different oligosaccharide composition types	1672:1719	very different oligosaccharide composition types	1672:1719	In addition, position 928 was found to be degenerate in oligosaccharide structure and very different oligosaccharide composition types were found associated with peptides containing the same amino acid sequence.
8615697	9	62	theme	complex	1566:1572	arg1	structures					1574:1583	either hybrid or complex structures	1549:1583	structures	1574:1583	Five sites (at positions 1200, 1329, 1993, 2275, and 2562) contain high mannose type units and two sites (at positions 179 and 1345) are linked to oligosaccharide units containing galactose in addition to mannose and glucosamine but no fucose and may be either hybrid or complex structures.
8615697	4	63	theme	permeation	580:589	arg1	chromatography					591:604	gel permeation chromatography	576:604	gel permeation chromatography followed by several steps of HPLC	576:638	Glycopeptides were purified using gel permeation chromatography followed by several steps of HPLC.
8615697	13	64	from	residues	2281:2288	arg1	four					2216:2219	four	2216:2219	four	2216:2219	Only four of the 20 putative sites the sequence of hTG, at asparagine residues 91, 477, 1849, and 2102 were not represented in the purified glycopeptide population and are presumed to escape significant glycosylation.
8615697	13	64	from	residues	2281:2288	arg1	hTG					2262:2264	hTG	2262:2264	hTG	2262:2264	Only four of the 20 putative sites the sequence of hTG, at asparagine residues 91, 477, 1849, and 2102 were not represented in the purified glycopeptide population and are presumed to escape significant glycosylation.
8615697	13	64	from	residues	2281:2288	arg1	sites					2240:2244	the 20 putative sites	2224:2244	the 20 putative sites	2224:2244	Only four of the 20 putative sites the sequence of hTG, at asparagine residues 91, 477, 1849, and 2102 were not represented in the purified glycopeptide population and are presumed to escape significant glycosylation.
8615697	3	65	theme	glycosylation	509:521	arg1	sites					491:495	these confirmed sites	475:495	these confirmed sites of N-linked glycosylation	475:521	In addition, the distribution of oligosaccharide type(s) at these confirmed sites of N-linked glycosylation has been examined.
8615697	3	65	theme	glycosylation	509:521	arg1	glycosylation					509:521	N-linked glycosylation	500:521	N-linked glycosylation	500:521	In addition, the distribution of oligosaccharide type(s) at these confirmed sites of N-linked glycosylation has been examined.
8615697	9	66	theme	mannose	1367:1373	arg1	units					1380:1384	high mannose type units	1362:1384	high mannose type units	1362:1384	Five sites (at positions 1200, 1329, 1993, 2275, and 2562) contain high mannose type units and two sites (at positions 179 and 1345) are linked to oligosaccharide units containing galactose in addition to mannose and glucosamine but no fucose and may be either hybrid or complex structures.
8615697	8	67	contain	containing	1223:1232	arg1	units					1217:1221	complex-type oligosaccharide units	1188:1221	complex-type oligosaccharide units containing fucose and galactose in addition to mannose and glucosamine	1188:1292	Eight of these confirmed glycosylation sites (at positions 57, 465, 510, 729, 797, 1696, 1754, and 2230) appear to be linked to complex-type oligosaccharide units containing fucose and galactose in addition to mannose and glucosamine.
8615697	8	67	contain	containing	1223:1232	arg2	galactose					1245:1253	galactose	1245:1253	galactose	1245:1253	Eight of these confirmed glycosylation sites (at positions 57, 465, 510, 729, 797, 1696, 1754, and 2230) appear to be linked to complex-type oligosaccharide units containing fucose and galactose in addition to mannose and glucosamine.
8615697	8	67	contain	containing	1223:1232	arg2	fucose					1234:1239	fucose	1234:1239	fucose	1234:1239	Eight of these confirmed glycosylation sites (at positions 57, 465, 510, 729, 797, 1696, 1754, and 2230) appear to be linked to complex-type oligosaccharide units containing fucose and galactose in addition to mannose and glucosamine.
8615697	8	68	theme	complex-type	1188:1199	arg1	units					1217:1221	complex-type oligosaccharide units	1188:1221	complex-type oligosaccharide units containing fucose and galactose in addition to mannose and glucosamine	1188:1292	Eight of these confirmed glycosylation sites (at positions 57, 465, 510, 729, 797, 1696, 1754, and 2230) appear to be linked to complex-type oligosaccharide units containing fucose and galactose in addition to mannose and glucosamine.
8615697	9	69	contain	contain	1354:1360	arg2	units					1380:1384	high mannose type units	1362:1384	high mannose type units	1362:1384	Five sites (at positions 1200, 1329, 1993, 2275, and 2562) contain high mannose type units and two sites (at positions 179 and 1345) are linked to oligosaccharide units containing galactose in addition to mannose and glucosamine but no fucose and may be either hybrid or complex structures.
8615697	9	69	contain	contain	1354:1360	arg1	sites					1300:1304	Five sites	1295:1304	Five sites (at positions 1200, 1329, 1993, 2275, and 2562)	1295:1352	Five sites (at positions 1200, 1329, 1993, 2275, and 2562) contain high mannose type units and two sites (at positions 179 and 1345) are linked to oligosaccharide units containing galactose in addition to mannose and glucosamine but no fucose and may be either hybrid or complex structures.
8615697	2	70	theme	tryptic	322:328	arg1	digest					330:335	a tryptic digest	320:335	a tryptic digest of hTG	320:342	We have characterized the glycopeptides contained in a tryptic digest of hTG in order to determine which sites are actually linked to carbohydrate.
8615697	9	71	from	positions	1404:1412	arg1	sites					1394:1398	two sites	1390:1398	two sites (at positions 179 and 1345)	1390:1426	Five sites (at positions 1200, 1329, 1993, 2275, and 2562) contain high mannose type units and two sites (at positions 179 and 1345) are linked to oligosaccharide units containing galactose in addition to mannose and glucosamine but no fucose and may be either hybrid or complex structures.
8615697	5	72	gly	glycopeptides	662:674	arg2	glycopeptides					662:674	The purified tryptic glycopeptides	641:674	The purified tryptic glycopeptides	641:674	The purified tryptic glycopeptides were characterized by gas phase sequencing and carbohydrate analysis and located within the amino acid sequence of thyroglobulin.
8615697	11	73	theme	acid	1916:1919	arg1	sequence					1921:1928	the amino acid sequence	1906:1928	the amino acid sequence found at 13 of the 16 sites	1906:1956	A high probability of a beta turn which would include the glycosylated asparagine residue was predicted for the amino acid sequence found at 13 of the 16 sites.
8615697	10	74	from	degenerate	1628:1637	arg1	structure					1658:1666	oligosaccharide structure	1642:1666	oligosaccharide structure	1642:1666	In addition, position 928 was found to be degenerate in oligosaccharide structure and very different oligosaccharide composition types were found associated with peptides containing the same amino acid sequence.
8615697	0	75	with	comparison	89:98	arg1	thyroglobulin					112:124	bovine thyroglobulin	105:124	bovine thyroglobulin	105:124	Glycosylation in human thyroglobulin: location of the N-linked oligosaccharide units and comparison with bovine thyroglobulin.
8615697	10	76	theme	different	1677:1685	arg1	types					1715:1719	very different oligosaccharide composition types	1672:1719	very different oligosaccharide composition types	1672:1719	In addition, position 928 was found to be degenerate in oligosaccharide structure and very different oligosaccharide composition types were found associated with peptides containing the same amino acid sequence.
8615697	2	77	theme	hTG	340:342	arg1	digest					330:335	a tryptic digest	320:335	a tryptic digest of hTG	320:342	We have characterized the glycopeptides contained in a tryptic digest of hTG in order to determine which sites are actually linked to carbohydrate.
8615697	10	78	located	found	1616:1620	arg2	position					1599:1606	position 928	1599:1610	position 928	1599:1610	In addition, position 928 was found to be degenerate in oligosaccharide structure and very different oligosaccharide composition types were found associated with peptides containing the same amino acid sequence.
8615697	10	78	located	found	1616:1620	arg1	addition					1589:1596	addition	1589:1596	addition	1589:1596	In addition, position 928 was found to be degenerate in oligosaccharide structure and very different oligosaccharide composition types were found associated with peptides containing the same amino acid sequence.
8615697	1	79	theme	cDNA	202:205	arg1	sequence					207:214	its cDNA sequence	198:214	its cDNA sequence	198:214	The amino acid sequence established for human thyroglobulin (hTG) from its cDNA sequence contains 20 putative N-linked glycosylation sites.
8615697	6	80	gly	glycopeptides	828:840	arg2	glycopeptides					828:840	the recovered glycopeptides	814:840	the recovered glycopeptides	814:840	Each of the recovered glycopeptides contained a consensus sequence for N-linked glycosylation.
8615697	3	81	link	N-linked	500:507	arg1	glycosylation					509:521	N-linked glycosylation	500:521	N-linked glycosylation	500:521	In addition, the distribution of oligosaccharide type(s) at these confirmed sites of N-linked glycosylation has been examined.
8615697	12	82	theme	hTG	2206:2208	arg1	portion					2195:2201	the N-terminal portion	2180:2201	the N-terminal portion of hTG	2180:2208	The glycosylation pattern in hTG was also compared with the data recently reported for bovine thyroglobulin (bTG) (27) and as has been recently reported for bTG, no oligosaccharides of the high mannose type were found in the N-terminal portion of hTG.
8615697	10	83	dep	found	1726:1730	arg1	associated					1732:1741	associated	1732:1741	associated with peptides containing the same amino acid sequence	1732:1795	In addition, position 928 was found to be degenerate in oligosaccharide structure and very different oligosaccharide composition types were found associated with peptides containing the same amino acid sequence.
8615697	11	84	theme	glycosylated	1856:1867	arg1	residue					1880:1886	the glycosylated asparagine residue	1852:1886	the glycosylated asparagine residue	1852:1886	A high probability of a beta turn which would include the glycosylated asparagine residue was predicted for the amino acid sequence found at 13 of the 16 sites.
8615697	12	85	theme	mannose	2153:2159	arg1	type					2161:2164	the high mannose type	2144:2164	the high mannose type	2144:2164	The glycosylation pattern in hTG was also compared with the data recently reported for bovine thyroglobulin (bTG) (27) and as has been recently reported for bTG, no oligosaccharides of the high mannose type were found in the N-terminal portion of hTG.
8615697	5	86	theme	gas	698:700	arg1	sequencing					708:717	gas phase sequencing	698:717	gas phase sequencing	698:717	The purified tryptic glycopeptides were characterized by gas phase sequencing and carbohydrate analysis and located within the amino acid sequence of thyroglobulin.
8615697	12	87	from	pattern	1977:1983	arg1	hTG					1988:1990	hTG	1988:1990	hTG	1988:1990	The glycosylation pattern in hTG was also compared with the data recently reported for bovine thyroglobulin (bTG) (27) and as has been recently reported for bTG, no oligosaccharides of the high mannose type were found in the N-terminal portion of hTG.
8615697	1	88	theme	amino	131:135	arg1	sequence					142:149	The amino acid sequence	127:149	The amino acid sequence established for human thyroglobulin (hTG) from its cDNA sequence	127:214	The amino acid sequence established for human thyroglobulin (hTG) from its cDNA sequence contains 20 putative N-linked glycosylation sites.
8615697	5	89	theme	amino	768:772	arg1	sequence					779:786	the amino acid sequence	764:786	the amino acid sequence of thyroglobulin	764:803	The purified tryptic glycopeptides were characterized by gas phase sequencing and carbohydrate analysis and located within the amino acid sequence of thyroglobulin.
8615697	13	90	dep	four	2216:2219	arg1	sequence					2250:2257	the sequence	2246:2257	Only four of the 20 putative sites the sequence	2211:2257	Only four of the 20 putative sites the sequence of hTG, at asparagine residues 91, 477, 1849, and 2102 were not represented in the purified glycopeptide population and are presumed to escape significant glycosylation.
8615697	10	91	from	structure	1658:1666	arg1	degenerate					1628:1637	degenerate	1628:1637	degenerate	1628:1637	In addition, position 928 was found to be degenerate in oligosaccharide structure and very different oligosaccharide composition types were found associated with peptides containing the same amino acid sequence.
8615697	8	92	from	positions	1109:1117	arg1	sites					1099:1103	these confirmed glycosylation sites	1069:1103	these confirmed glycosylation sites	1069:1103	Eight of these confirmed glycosylation sites (at positions 57, 465, 510, 729, 797, 1696, 1754, and 2230) appear to be linked to complex-type oligosaccharide units containing fucose and galactose in addition to mannose and glucosamine.
8615697	8	92	from	positions	1109:1117	arg1	Eight					1060:1064	Eight	1060:1064	Eight	1060:1064	Eight of these confirmed glycosylation sites (at positions 57, 465, 510, 729, 797, 1696, 1754, and 2230) appear to be linked to complex-type oligosaccharide units containing fucose and galactose in addition to mannose and glucosamine.
8615697	12	93	theme	high	2148:2151	arg1	type					2161:2164	the high mannose type	2144:2164	the high mannose type	2144:2164	The glycosylation pattern in hTG was also compared with the data recently reported for bovine thyroglobulin (bTG) (27) and as has been recently reported for bTG, no oligosaccharides of the high mannose type were found in the N-terminal portion of hTG.
8615697	12	94	located	found	2171:2175	arg1	portion					2195:2201	the N-terminal portion	2180:2201	the N-terminal portion of hTG	2180:2208	The glycosylation pattern in hTG was also compared with the data recently reported for bovine thyroglobulin (bTG) (27) and as has been recently reported for bTG, no oligosaccharides of the high mannose type were found in the N-terminal portion of hTG.
8615697	12	94	located	found	2171:2175	arg2	oligosaccharides					2124:2139	no oligosaccharides	2121:2139	no oligosaccharides of the high mannose type	2121:2164	The glycosylation pattern in hTG was also compared with the data recently reported for bovine thyroglobulin (bTG) (27) and as has been recently reported for bTG, no oligosaccharides of the high mannose type were found in the N-terminal portion of hTG.
8615697	6	95	contain	contained	842:850	arg1	Each					806:809	Each	806:809	Each	806:809	Each of the recovered glycopeptides contained a consensus sequence for N-linked glycosylation.
8615697	6	95	contain	contained	842:850	arg1	glycopeptides					828:840	the recovered glycopeptides	814:840	the recovered glycopeptides	814:840	Each of the recovered glycopeptides contained a consensus sequence for N-linked glycosylation.
8615697	6	95	contain	contained	842:850	arg2	sequence					864:871	a consensus sequence	852:871	a consensus sequence for N-linked glycosylation	852:898	Each of the recovered glycopeptides contained a consensus sequence for N-linked glycosylation.
8615697	12	96	theme	type	2161:2164	arg1	oligosaccharides					2124:2139	no oligosaccharides	2121:2139	no oligosaccharides of the high mannose type	2121:2164	The glycosylation pattern in hTG was also compared with the data recently reported for bovine thyroglobulin (bTG) (27) and as has been recently reported for bTG, no oligosaccharides of the high mannose type were found in the N-terminal portion of hTG.
8615697	3	97	gly	glycosylation	509:521	arg2	glycosylation					509:521	N-linked glycosylation	500:521	N-linked glycosylation	500:521	In addition, the distribution of oligosaccharide type(s) at these confirmed sites of N-linked glycosylation has been examined.
8615697	3	97	gly	glycosylation	509:521	arg2	sites					491:495	these confirmed sites	475:495	these confirmed sites of N-linked glycosylation	475:521	In addition, the distribution of oligosaccharide type(s) at these confirmed sites of N-linked glycosylation has been examined.
8615697	9	98	theme	oligosaccharide	1442:1456	arg1	units					1458:1462	oligosaccharide units	1442:1462	oligosaccharide units containing galactose in addition to mannose and glucosamine but no fucose	1442:1536	Five sites (at positions 1200, 1329, 1993, 2275, and 2562) contain high mannose type units and two sites (at positions 179 and 1345) are linked to oligosaccharide units containing galactose in addition to mannose and glucosamine but no fucose and may be either hybrid or complex structures.
8615697	8	99	theme	glycosylation	1085:1097	arg1	sites					1099:1103	these confirmed glycosylation sites	1069:1103	these confirmed glycosylation sites	1069:1103	Eight of these confirmed glycosylation sites (at positions 57, 465, 510, 729, 797, 1696, 1754, and 2230) appear to be linked to complex-type oligosaccharide units containing fucose and galactose in addition to mannose and glucosamine.
8615697	13	100	theme	asparagine	2270:2279	arg1	residues					2281:2288	asparagine residues 91, 477, 1849, and 2102	2270:2312	asparagine residues 91, 477, 1849, and 2102	2270:2312	Only four of the 20 putative sites the sequence of hTG, at asparagine residues 91, 477, 1849, and 2102 were not represented in the purified glycopeptide population and are presumed to escape significant glycosylation.
8615697	11	101	theme	turn	1827:1830	arg1	probability					1805:1815	A high probability	1798:1815	A high probability of a beta turn which would include the glycosylated asparagine residue	1798:1886	A high probability of a beta turn which would include the glycosylated asparagine residue was predicted for the amino acid sequence found at 13 of the 16 sites.
8615697	1	102	gly	glycosylation	246:258	arg2	sites					260:264	20 putative N-linked glycosylation sites	225:264	20 putative N-linked glycosylation sites	225:264	The amino acid sequence established for human thyroglobulin (hTG) from its cDNA sequence contains 20 putative N-linked glycosylation sites.
8615697	1	102	gly	glycosylation	246:258	arg2	20					225:226	20	225:226	20	225:226	The amino acid sequence established for human thyroglobulin (hTG) from its cDNA sequence contains 20 putative N-linked glycosylation sites.
8615697	5	103	theme	carbohydrate	723:734	arg1	analysis					736:743	carbohydrate analysis	723:743	carbohydrate analysis	723:743	The purified tryptic glycopeptides were characterized by gas phase sequencing and carbohydrate analysis and located within the amino acid sequence of thyroglobulin.
8615697	7	104	gly	glycosylated	1024:1035	arg1	16					995:996	16	995:996	16	995:996	Of the 20 putative N-linked glycosylation sites in the human thyroglobulin polypeptide chain, 16 were shown to be actually glycosylated in the mature protein.
8615697	7	104	gly	glycosylated	1024:1035	arg2	16					995:996	16	995:996	16	995:996	Of the 20 putative N-linked glycosylation sites in the human thyroglobulin polypeptide chain, 16 were shown to be actually glycosylated in the mature protein.
8615697	7	104	gly	glycosylated	1024:1035	arg1	protein					1051:1057	the mature protein	1040:1057	the mature protein	1040:1057	Of the 20 putative N-linked glycosylation sites in the human thyroglobulin polypeptide chain, 16 were shown to be actually glycosylated in the mature protein.
8615697	9	105	from	positions	1310:1318	arg1	sites					1300:1304	Five sites	1295:1304	Five sites (at positions 1200, 1329, 1993, 2275, and 2562)	1295:1352	Five sites (at positions 1200, 1329, 1993, 2275, and 2562) contain high mannose type units and two sites (at positions 179 and 1345) are linked to oligosaccharide units containing galactose in addition to mannose and glucosamine but no fucose and may be either hybrid or complex structures.
8615697	7	106	theme	thyroglobulin	962:974	arg1	chain					988:992	the human thyroglobulin polypeptide chain	952:992	the human thyroglobulin polypeptide chain	952:992	Of the 20 putative N-linked glycosylation sites in the human thyroglobulin polypeptide chain, 16 were shown to be actually glycosylated in the mature protein.
8615697	5	107	theme	thyroglobulin	791:803	arg1	sequence					779:786	the amino acid sequence	764:786	the amino acid sequence of thyroglobulin	764:803	The purified tryptic glycopeptides were characterized by gas phase sequencing and carbohydrate analysis and located within the amino acid sequence of thyroglobulin.
8615697	10	108	theme	amino	1777:1781	arg1	sequence					1788:1795	the same amino acid sequence	1768:1795	the same amino acid sequence	1768:1795	In addition, position 928 was found to be degenerate in oligosaccharide structure and very different oligosaccharide composition types were found associated with peptides containing the same amino acid sequence.
8615697	3	109	theme	oligosaccharide	448:462	arg1	s					469:469	oligosaccharide type(s)	448:470	oligosaccharide type(s)	448:470	In addition, the distribution of oligosaccharide type(s) at these confirmed sites of N-linked glycosylation has been examined.
8615697	6	110	theme	N-linked	877:884	arg1	glycosylation					886:898	N-linked glycosylation	877:898	N-linked glycosylation	877:898	Each of the recovered glycopeptides contained a consensus sequence for N-linked glycosylation.
8615697	13	111	theme	putative	2231:2238	arg1	sites					2240:2244	the 20 putative sites	2224:2244	the 20 putative sites	2224:2244	Only four of the 20 putative sites the sequence of hTG, at asparagine residues 91, 477, 1849, and 2102 were not represented in the purified glycopeptide population and are presumed to escape significant glycosylation.
8615697	6	112	link	N-linked	877:884	arg1	glycosylation					886:898	N-linked glycosylation	877:898	N-linked glycosylation	877:898	Each of the recovered glycopeptides contained a consensus sequence for N-linked glycosylation.
8615697	2	113	attach	linked	391:396	arg2	sites					372:376	sites	372:376	sites	372:376	We have characterized the glycopeptides contained in a tryptic digest of hTG in order to determine which sites are actually linked to carbohydrate.
8615697	2	113	attach	linked	391:396	arg1	carbohydrate					401:412	carbohydrate	401:412	carbohydrate	401:412	We have characterized the glycopeptides contained in a tryptic digest of hTG in order to determine which sites are actually linked to carbohydrate.
8615697	0	114	link	N-linked	54:61	arg1	units					79:83	the N-linked oligosaccharide units	50:83	the N-linked oligosaccharide units	50:83	Glycosylation in human thyroglobulin: location of the N-linked oligosaccharide units and comparison with bovine thyroglobulin.
8615697	9	115	attach	linked	1432:1437	arg2	sites					1394:1398	two sites	1390:1398	two sites (at positions 179 and 1345)	1390:1426	Five sites (at positions 1200, 1329, 1993, 2275, and 2562) contain high mannose type units and two sites (at positions 179 and 1345) are linked to oligosaccharide units containing galactose in addition to mannose and glucosamine but no fucose and may be either hybrid or complex structures.
8615697	9	115	attach	linked	1432:1437	arg1	units					1458:1462	oligosaccharide units	1442:1462	oligosaccharide units containing galactose in addition to mannose and glucosamine but no fucose	1442:1536	Five sites (at positions 1200, 1329, 1993, 2275, and 2562) contain high mannose type units and two sites (at positions 179 and 1345) are linked to oligosaccharide units containing galactose in addition to mannose and glucosamine but no fucose and may be either hybrid or complex structures.
8615697	12	116	theme	bovine	2046:2051	arg1	bTG					2068:2070	bTG	2068:2070	bTG	2068:2070	The glycosylation pattern in hTG was also compared with the data recently reported for bovine thyroglobulin (bTG) (27) and as has been recently reported for bTG, no oligosaccharides of the high mannose type were found in the N-terminal portion of hTG.
8615697	12	116	theme	bovine	2046:2051	arg1	27					2074:2075	27	2074:2075	27	2074:2075	The glycosylation pattern in hTG was also compared with the data recently reported for bovine thyroglobulin (bTG) (27) and as has been recently reported for bTG, no oligosaccharides of the high mannose type were found in the N-terminal portion of hTG.
8615697	12	116	theme	bovine	2046:2051	arg1	thyroglobulin					2053:2065	bovine thyroglobulin	2046:2065	bovine thyroglobulin (bTG) (27)	2046:2076	The glycosylation pattern in hTG was also compared with the data recently reported for bovine thyroglobulin (bTG) (27) and as has been recently reported for bTG, no oligosaccharides of the high mannose type were found in the N-terminal portion of hTG.
8615697	7	117	theme	glycosylation	929:941	arg1	sites					943:947	the 20 putative N-linked glycosylation sites	904:947	the 20 putative N-linked glycosylation sites in the human thyroglobulin polypeptide chain	904:992	Of the 20 putative N-linked glycosylation sites in the human thyroglobulin polypeptide chain, 16 were shown to be actually glycosylated in the mature protein.
8615697	13	118	gly	glycopeptide	2351:2362	arg2	glycopeptide					2351:2362	the purified glycopeptide population	2338:2373	the purified glycopeptide population	2338:2373	Only four of the 20 putative sites the sequence of hTG, at asparagine residues 91, 477, 1849, and 2102 were not represented in the purified glycopeptide population and are presumed to escape significant glycosylation.
8615697	9	119	contain	containing	1464:1473	arg2	galactose					1475:1483	galactose	1475:1483	galactose	1475:1483	Five sites (at positions 1200, 1329, 1993, 2275, and 2562) contain high mannose type units and two sites (at positions 179 and 1345) are linked to oligosaccharide units containing galactose in addition to mannose and glucosamine but no fucose and may be either hybrid or complex structures.
8615697	9	119	contain	containing	1464:1473	arg1	units					1458:1462	oligosaccharide units	1442:1462	oligosaccharide units containing galactose in addition to mannose and glucosamine but no fucose	1442:1536	Five sites (at positions 1200, 1329, 1993, 2275, and 2562) contain high mannose type units and two sites (at positions 179 and 1345) are linked to oligosaccharide units containing galactose in addition to mannose and glucosamine but no fucose and may be either hybrid or complex structures.
8615697	0	120	with	location	38:45	arg1	thyroglobulin					112:124	bovine thyroglobulin	105:124	bovine thyroglobulin	105:124	Glycosylation in human thyroglobulin: location of the N-linked oligosaccharide units and comparison with bovine thyroglobulin.
8615697	3	121	theme	N-linked	500:507	arg1	glycosylation					509:521	N-linked glycosylation	500:521	N-linked glycosylation	500:521	In addition, the distribution of oligosaccharide type(s) at these confirmed sites of N-linked glycosylation has been examined.
8615697	7	122	theme	putative	911:918	arg1	sites					943:947	the 20 putative N-linked glycosylation sites	904:947	the 20 putative N-linked glycosylation sites in the human thyroglobulin polypeptide chain	904:992	Of the 20 putative N-linked glycosylation sites in the human thyroglobulin polypeptide chain, 16 were shown to be actually glycosylated in the mature protein.
8615697	1	123	theme	N-linked	237:244	arg1	sites					260:264	20 putative N-linked glycosylation sites	225:264	20 putative N-linked glycosylation sites	225:264	The amino acid sequence established for human thyroglobulin (hTG) from its cDNA sequence contains 20 putative N-linked glycosylation sites.
1421757	1	0	gly	glycosylation	177:189	arg2	three					145:149	three	145:149	three	145:149	The human transferrin receptor is a glycoprotein containing three N-linked and one O-linked glycosylation sites.
1421757	1	0	gly	glycosylation	177:189	arg2	sites					191:195	three N-linked and one O-linked glycosylation sites	145:195	three N-linked and one O-linked glycosylation sites	145:195	The human transferrin receptor is a glycoprotein containing three N-linked and one O-linked glycosylation sites.
1421757	0	1	theme	receptor	75:82	arg1	receptor					75:82	the human transferrin receptor	53:82	the human transferrin receptor	53:82	Identification of the O-linked glycosylation site of the human transferrin receptor.
1421757	0	1	theme	receptor	75:82	arg1	site					45:48	the O-linked glycosylation site	18:48	the O-linked glycosylation site of the human transferrin receptor	18:82	Identification of the O-linked glycosylation site of the human transferrin receptor.
1421757	0	2	link	O-linked	22:29	arg1	receptor					75:82	the human transferrin receptor	53:82	the human transferrin receptor	53:82	Identification of the O-linked glycosylation site of the human transferrin receptor.
1421757	0	2	link	O-linked	22:29	arg1	site					45:48	the O-linked glycosylation site	18:48	the O-linked glycosylation site of the human transferrin receptor	18:82	Identification of the O-linked glycosylation site of the human transferrin receptor.
1421757	4	3	theme	Mass	454:457	arg1	analysis					468:475	Mass spectral analysis	454:475	Mass spectral analysis	454:475	Mass spectral analysis is consistent with the presence of a Gal-GalNAc core with predominantly two sialic acid residues.
1421757	3	4	gly	O-glycosylation	426:440	arg2	site					418:421	the site	414:421	the site of O-glycosylation	414:440	Amino acid sequence analysis reveals that the site of O-glycosylation is Thr-104.
1421757	3	4	gly	O-glycosylation	426:440	arg2	Thr-104					445:451	Thr-104	445:451	Thr-104	445:451	Amino acid sequence analysis reveals that the site of O-glycosylation is Thr-104.
1421757	3	4	gly	O-glycosylation	426:440	arg2	O-glycosylation					426:440	O-glycosylation	426:440	O-glycosylation	426:440	Amino acid sequence analysis reveals that the site of O-glycosylation is Thr-104.
1421757	2	5	contain	containing	342:351	arg2	site					366:369	the O-linked site	353:369	the O-linked site	353:369	Tryptic digestion of the receptor, followed by chromatography on BioGel P-2 and reverse-phase HPLC, yields a glycopeptide (amino acids 101-120) containing the O-linked site.
1421757	2	5	contain	containing	342:351	arg1	glycopeptide					307:318	a glycopeptide	305:318	a glycopeptide (amino acids 101-120) containing the O-linked site	305:369	Tryptic digestion of the receptor, followed by chromatography on BioGel P-2 and reverse-phase HPLC, yields a glycopeptide (amino acids 101-120) containing the O-linked site.
1421757	2	5	contain	containing	342:351	arg1	acids					327:331	amino acids 101-120	321:339	amino acids 101-120	321:339	Tryptic digestion of the receptor, followed by chromatography on BioGel P-2 and reverse-phase HPLC, yields a glycopeptide (amino acids 101-120) containing the O-linked site.
1421757	2	6	theme	reverse-phase	278:290	arg1	HPLC					292:295	reverse-phase HPLC	278:295	reverse-phase HPLC	278:295	Tryptic digestion of the receptor, followed by chromatography on BioGel P-2 and reverse-phase HPLC, yields a glycopeptide (amino acids 101-120) containing the O-linked site.
1421757	1	7	theme	O-linked	168:175	arg1	sites					191:195	three N-linked and one O-linked glycosylation sites	145:195	three N-linked and one O-linked glycosylation sites	145:195	The human transferrin receptor is a glycoprotein containing three N-linked and one O-linked glycosylation sites.
1421757	1	8	theme	glycosylation	177:189	arg1	sites					191:195	three N-linked and one O-linked glycosylation sites	145:195	three N-linked and one O-linked glycosylation sites	145:195	The human transferrin receptor is a glycoprotein containing three N-linked and one O-linked glycosylation sites.
1421757	3	9	theme	acid	378:381	arg1	analysis					392:399	Amino acid sequence analysis	372:399	Amino acid sequence analysis	372:399	Amino acid sequence analysis reveals that the site of O-glycosylation is Thr-104.
1421757	2	10	link	O-linked	357:364	arg1	site					366:369	the O-linked site	353:369	the O-linked site	353:369	Tryptic digestion of the receptor, followed by chromatography on BioGel P-2 and reverse-phase HPLC, yields a glycopeptide (amino acids 101-120) containing the O-linked site.
1421757	1	11	link	O-linked	168:175	arg1	sites					191:195	three N-linked and one O-linked glycosylation sites	145:195	three N-linked and one O-linked glycosylation sites	145:195	The human transferrin receptor is a glycoprotein containing three N-linked and one O-linked glycosylation sites.
1421757	2	12	gly	glycopeptide	307:318	arg2	glycopeptide					307:318	a glycopeptide	305:318	a glycopeptide (amino acids 101-120) containing the O-linked site	305:369	Tryptic digestion of the receptor, followed by chromatography on BioGel P-2 and reverse-phase HPLC, yields a glycopeptide (amino acids 101-120) containing the O-linked site.
1421757	2	12	gly	glycopeptide	307:318	arg2	acids					327:331	amino acids 101-120	321:339	amino acids 101-120	321:339	Tryptic digestion of the receptor, followed by chromatography on BioGel P-2 and reverse-phase HPLC, yields a glycopeptide (amino acids 101-120) containing the O-linked site.
1421757	3	13	theme	sequence	383:390	arg1	analysis					392:399	Amino acid sequence analysis	372:399	Amino acid sequence analysis	372:399	Amino acid sequence analysis reveals that the site of O-glycosylation is Thr-104.
1421757	4	14	theme	sialic	553:558	arg1	residues					565:572	predominantly two sialic acid residues	535:572	predominantly two sialic acid residues	535:572	Mass spectral analysis is consistent with the presence of a Gal-GalNAc core with predominantly two sialic acid residues.
1421757	1	15	theme	human	89:93	arg1	glycoprotein					121:132	a glycoprotein	119:132	a glycoprotein containing three N-linked and one O-linked glycosylation sites	119:195	The human transferrin receptor is a glycoprotein containing three N-linked and one O-linked glycosylation sites.
1421757	1	15	theme	human	89:93	arg1	receptor					107:114	The human transferrin receptor	85:114	The human transferrin receptor	85:114	The human transferrin receptor is a glycoprotein containing three N-linked and one O-linked glycosylation sites.
1421757	0	16	theme	O-linked	22:29	arg1	receptor					75:82	the human transferrin receptor	53:82	the human transferrin receptor	53:82	Identification of the O-linked glycosylation site of the human transferrin receptor.
1421757	0	16	theme	O-linked	22:29	arg1	site					45:48	the O-linked glycosylation site	18:48	the O-linked glycosylation site of the human transferrin receptor	18:82	Identification of the O-linked glycosylation site of the human transferrin receptor.
1421757	2	17	theme	O-linked	357:364	arg1	site					366:369	the O-linked site	353:369	the O-linked site	353:369	Tryptic digestion of the receptor, followed by chromatography on BioGel P-2 and reverse-phase HPLC, yields a glycopeptide (amino acids 101-120) containing the O-linked site.
1421757	4	18	with	consistent	480:489	arg1	presence					500:507	the presence	496:507	the presence of a Gal-GalNAc core with predominantly two sialic acid residues	496:572	Mass spectral analysis is consistent with the presence of a Gal-GalNAc core with predominantly two sialic acid residues.
1421757	1	19	theme	transferrin	95:105	arg1	glycoprotein					121:132	a glycoprotein	119:132	a glycoprotein containing three N-linked and one O-linked glycosylation sites	119:195	The human transferrin receptor is a glycoprotein containing three N-linked and one O-linked glycosylation sites.
1421757	1	19	theme	transferrin	95:105	arg1	receptor					107:114	The human transferrin receptor	85:114	The human transferrin receptor	85:114	The human transferrin receptor is a glycoprotein containing three N-linked and one O-linked glycosylation sites.
1421757	2	20	from	chromatography	245:258	arg1	P-2					270:272	BioGel P-2	263:272	BioGel P-2	263:272	Tryptic digestion of the receptor, followed by chromatography on BioGel P-2 and reverse-phase HPLC, yields a glycopeptide (amino acids 101-120) containing the O-linked site.
1421757	3	21	theme	Amino	372:376	arg1	analysis					392:399	Amino acid sequence analysis	372:399	Amino acid sequence analysis	372:399	Amino acid sequence analysis reveals that the site of O-glycosylation is Thr-104.
1421757	0	22	theme	site	45:48	arg1	Identification					0:13	Identification	0:13	Identification of the O-linked glycosylation site of the human transferrin receptor.	0:83	Identification of the O-linked glycosylation site of the human transferrin receptor.
1421757	4	23	theme	acid	560:563	arg1	residues					565:572	predominantly two sialic acid residues	535:572	predominantly two sialic acid residues	535:572	Mass spectral analysis is consistent with the presence of a Gal-GalNAc core with predominantly two sialic acid residues.
1421757	0	24	theme	glycosylation	31:43	arg1	receptor					75:82	the human transferrin receptor	53:82	the human transferrin receptor	53:82	Identification of the O-linked glycosylation site of the human transferrin receptor.
1421757	0	24	theme	glycosylation	31:43	arg1	site					45:48	the O-linked glycosylation site	18:48	the O-linked glycosylation site of the human transferrin receptor	18:82	Identification of the O-linked glycosylation site of the human transferrin receptor.
1421757	4	25	theme	core	525:528	arg1	presence					500:507	the presence	496:507	the presence of a Gal-GalNAc core with predominantly two sialic acid residues	496:572	Mass spectral analysis is consistent with the presence of a Gal-GalNAc core with predominantly two sialic acid residues.
1421757	1	26	link	N-linked	151:158	arg1	sites					191:195	three N-linked and one O-linked glycosylation sites	145:195	three N-linked and one O-linked glycosylation sites	145:195	The human transferrin receptor is a glycoprotein containing three N-linked and one O-linked glycosylation sites.
1421757	4	27	theme	spectral	459:466	arg1	analysis					468:475	Mass spectral analysis	454:475	Mass spectral analysis	454:475	Mass spectral analysis is consistent with the presence of a Gal-GalNAc core with predominantly two sialic acid residues.
1421757	4	28	theme	Gal-GalNAc	514:523	arg1	core					525:528	a Gal-GalNAc core	512:528	a Gal-GalNAc core with predominantly two sialic acid residues	512:572	Mass spectral analysis is consistent with the presence of a Gal-GalNAc core with predominantly two sialic acid residues.
1421757	3	29	theme	O-glycosylation	426:440	arg1	O-glycosylation					426:440	O-glycosylation	426:440	O-glycosylation	426:440	Amino acid sequence analysis reveals that the site of O-glycosylation is Thr-104.
1421757	3	29	theme	O-glycosylation	426:440	arg1	site					418:421	the site	414:421	the site of O-glycosylation	414:440	Amino acid sequence analysis reveals that the site of O-glycosylation is Thr-104.
1421757	3	29	theme	O-glycosylation	426:440	arg1	Thr-104					445:451	Thr-104	445:451	Thr-104	445:451	Amino acid sequence analysis reveals that the site of O-glycosylation is Thr-104.
1421757	1	30	gly	glycoprotein	121:132	arg1	glycoprotein					121:132	a glycoprotein	119:132	a glycoprotein containing three N-linked and one O-linked glycosylation sites	119:195	The human transferrin receptor is a glycoprotein containing three N-linked and one O-linked glycosylation sites.
1421757	1	30	gly	glycoprotein	121:132	arg1	receptor					107:114	The human transferrin receptor	85:114	The human transferrin receptor	85:114	The human transferrin receptor is a glycoprotein containing three N-linked and one O-linked glycosylation sites.
1421757	2	31	theme	receptor	223:230	arg1	digestion					206:214	Tryptic digestion	198:214	Tryptic digestion	198:214	Tryptic digestion of the receptor, followed by chromatography on BioGel P-2 and reverse-phase HPLC, yields a glycopeptide (amino acids 101-120) containing the O-linked site.
1421757	0	32	gly	glycosylation	31:43	arg1	receptor					75:82	the human transferrin receptor	53:82	the human transferrin receptor	53:82	Identification of the O-linked glycosylation site of the human transferrin receptor.
1421757	0	32	gly	glycosylation	31:43	arg2	site					45:48	the O-linked glycosylation site	18:48	the O-linked glycosylation site of the human transferrin receptor	18:82	Identification of the O-linked glycosylation site of the human transferrin receptor.
1421757	0	32	gly	glycosylation	31:43	arg2	receptor					75:82	the human transferrin receptor	53:82	the human transferrin receptor	53:82	Identification of the O-linked glycosylation site of the human transferrin receptor.
1421757	4	33	with	core	525:528	arg1	residues					565:572	predominantly two sialic acid residues	535:572	predominantly two sialic acid residues	535:572	Mass spectral analysis is consistent with the presence of a Gal-GalNAc core with predominantly two sialic acid residues.
1421757	2	34	theme	BioGel	263:268	arg1	P-2					270:272	BioGel P-2	263:272	BioGel P-2	263:272	Tryptic digestion of the receptor, followed by chromatography on BioGel P-2 and reverse-phase HPLC, yields a glycopeptide (amino acids 101-120) containing the O-linked site.
1421757	2	35	theme	amino	321:325	arg1	glycopeptide					307:318	a glycopeptide	305:318	a glycopeptide (amino acids 101-120) containing the O-linked site	305:369	Tryptic digestion of the receptor, followed by chromatography on BioGel P-2 and reverse-phase HPLC, yields a glycopeptide (amino acids 101-120) containing the O-linked site.
1421757	2	35	theme	amino	321:325	arg1	acids					327:331	amino acids 101-120	321:339	amino acids 101-120	321:339	Tryptic digestion of the receptor, followed by chromatography on BioGel P-2 and reverse-phase HPLC, yields a glycopeptide (amino acids 101-120) containing the O-linked site.
1421757	0	36	theme	transferrin	63:73	arg1	receptor					75:82	the human transferrin receptor	53:82	the human transferrin receptor	53:82	Identification of the O-linked glycosylation site of the human transferrin receptor.
1421757	2	37	theme	Tryptic	198:204	arg1	digestion					206:214	Tryptic digestion	198:214	Tryptic digestion	198:214	Tryptic digestion of the receptor, followed by chromatography on BioGel P-2 and reverse-phase HPLC, yields a glycopeptide (amino acids 101-120) containing the O-linked site.
1421757	2	38	from	HPLC	292:295	arg1	P-2					270:272	BioGel P-2	263:272	BioGel P-2	263:272	Tryptic digestion of the receptor, followed by chromatography on BioGel P-2 and reverse-phase HPLC, yields a glycopeptide (amino acids 101-120) containing the O-linked site.
1421757	0	39	theme	human	57:61	arg1	receptor					75:82	the human transferrin receptor	53:82	the human transferrin receptor	53:82	Identification of the O-linked glycosylation site of the human transferrin receptor.
1421757	1	40	contain	containing	134:143	arg1	glycoprotein					121:132	a glycoprotein	119:132	a glycoprotein containing three N-linked and one O-linked glycosylation sites	119:195	The human transferrin receptor is a glycoprotein containing three N-linked and one O-linked glycosylation sites.
1421757	1	40	contain	containing	134:143	arg1	receptor					107:114	The human transferrin receptor	85:114	The human transferrin receptor	85:114	The human transferrin receptor is a glycoprotein containing three N-linked and one O-linked glycosylation sites.
1421757	1	40	contain	containing	134:143	arg2	sites					191:195	three N-linked and one O-linked glycosylation sites	145:195	three N-linked and one O-linked glycosylation sites	145:195	The human transferrin receptor is a glycoprotein containing three N-linked and one O-linked glycosylation sites.
1421757	1	41	theme	N-linked	151:158	arg1	sites					191:195	three N-linked and one O-linked glycosylation sites	145:195	three N-linked and one O-linked glycosylation sites	145:195	The human transferrin receptor is a glycoprotein containing three N-linked and one O-linked glycosylation sites.
29427759	11	0	theme	protein	2409:2415	arg1	N-glycopeptides					2381:2395	different N-glycopeptides	2371:2395	different N-glycopeptides of the same protein	2371:2415	Moreover, increased and decreased fucosylation was observed on different N-glycopeptides of the same protein.
29427759	12	1	theme	core	2426:2429	arg1	assay					2505:2509	an alternative serologic assay	2480:2509	an alternative serologic assay for the evaluation of fibrotic liver disease	2480:2554	Altered core fucosylation of N-glycopeptides might be used as an alternative serologic assay for the evaluation of fibrotic liver disease.
29427759	12	1	theme	core	2426:2429	arg1	fucosylation					2431:2442	Altered core fucosylation	2418:2442	Altered core fucosylation of N-glycopeptides	2418:2461	Altered core fucosylation of N-glycopeptides might be used as an alternative serologic assay for the evaluation of fibrotic liver disease.
29427759	9	2	theme	comparison	2027:2036	arg1	groups					2038:2043	three comparison groups	2021:2043	three comparison groups (healthy control, fibrosis and cirrhosis patients)	2021:2094	BIOLOGICAL SIGNIFICANCE: We have quantified the difference in core fucosylation among three comparison groups (healthy control, fibrosis and cirrhosis patients) using a sensitive and selective LC-MS-MRM method.
29427759	4	3	from	abundance	695:703	arg1	cohort					733:738	a cohort	731:738	a cohort of 45 participants (15 disease-free control, 15 fibrosis and 15 cirrhosis patients)	731:822	Specifically, we quantified core fucosylation of 22 N-glycopeptides derived from 17 proteins together with protein abundance of these glycoproteins in a cohort of 45 participants (15 disease-free control, 15 fibrosis and 15 cirrhosis patients) using a multiplex nanoUPLC-MS-MRM workflow.
29427759	2	4	gly	N-glycopeptides	267:281	arg1	proteins					292:299	serum proteins	286:299	serum proteins partially deglycosylated by a combination of endoglycosidases (endoF1, endoF2, and endoF3)	286:390	In this study, we carried out multiple reaction monitoring (MRM) quantification of core fucosylated N-glycopeptides of serum proteins partially deglycosylated by a combination of endoglycosidases (endoF1, endoF2, and endoF3).
29427759	2	4	gly	N-glycopeptides	267:281	arg2	N-glycopeptides					267:281	core fucosylated N-glycopeptides	250:281	core fucosylated N-glycopeptides of serum proteins partially deglycosylated by a combination of endoglycosidases (endoF1, endoF2, and endoF3)	250:390	In this study, we carried out multiple reaction monitoring (MRM) quantification of core fucosylated N-glycopeptides of serum proteins partially deglycosylated by a combination of endoglycosidases (endoF1, endoF2, and endoF3).
29427759	1	5	attach	linked	141:146	arg2	fucosylation					107:118	Aberrant core fucosylation	93:118	Aberrant core fucosylation of proteins	93:130	Aberrant core fucosylation of proteins has been linked to liver diseases.
29427759	1	5	attach	linked	141:146	arg1	diseases					157:164	liver diseases	151:164	liver diseases	151:164	Aberrant core fucosylation of proteins has been linked to liver diseases.
29427759	5	6	theme	glycopeptides	1340:1352	arg1	fucosylation					1321:1332	core fucosylation	1316:1332	core fucosylation of 10 glycopeptides	1316:1352	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	3	7	theme	serum	539:543	arg1	fractionation					522:534	fractionation	522:534	fractionation of serum besides the nanoRP chromatography	522:577	To minimize variability associated with the preparatory steps, the analysis was performed without enrichment of glycopeptides or fractionation of serum besides the nanoRP chromatography.
29427759	3	7	theme	serum	539:543	arg1	glycopeptides					505:517	glycopeptides	505:517	glycopeptides	505:517	To minimize variability associated with the preparatory steps, the analysis was performed without enrichment of glycopeptides or fractionation of serum besides the nanoRP chromatography.
29427759	4	8	theme	multiplex	832:840	arg1	workflow					858:865	a multiplex nanoUPLC-MS-MRM workflow	830:865	a multiplex nanoUPLC-MS-MRM workflow	830:865	Specifically, we quantified core fucosylation of 22 N-glycopeptides derived from 17 proteins together with protein abundance of these glycoproteins in a cohort of 45 participants (15 disease-free control, 15 fibrosis and 15 cirrhosis patients) using a multiplex nanoUPLC-MS-MRM workflow.
29427759	7	9	theme	liver	1684:1688	arg1	disease					1690:1696	fibrotic liver disease	1675:1696	fibrotic liver disease	1675:1696	Our results demonstrate that the changes in core fucosylation are protein and site specific during the progression of fibrotic liver disease and independent of the changes in the quantity of N-glycoproteins.
29427759	4	10	gly	N-glycopeptides	632:646	arg2	N-glycopeptides					632:646	22 N-glycopeptides	629:646	22 N-glycopeptides derived from 17 proteins together with protein abundance of these glycoproteins in a cohort of 45 participants (15 disease-free control, 15 fibrosis and 15 cirrhosis patients)	629:822	Specifically, we quantified core fucosylation of 22 N-glycopeptides derived from 17 proteins together with protein abundance of these glycoproteins in a cohort of 45 participants (15 disease-free control, 15 fibrosis and 15 cirrhosis patients) using a multiplex nanoUPLC-MS-MRM workflow.
29427759	3	11	theme	fractionation	522:534	arg1	enrichment					491:500	enrichment	491:500	enrichment of glycopeptides or fractionation of serum besides the nanoRP chromatography	491:577	To minimize variability associated with the preparatory steps, the analysis was performed without enrichment of glycopeptides or fractionation of serum besides the nanoRP chromatography.
29427759	10	12	theme	many	2198:2201	arg1	fucosylation					2182:2193	core fucosylation	2177:2193	core fucosylation of many of the glycoproteins that we examined	2177:2239	Despite an overall increase in core fucosylation of many of the glycoproteins that we examined, core fucosylation changed in a protein- and site-specific manner.
29427759	9	13	theme	fibrosis	2063:2070	arg1	patients					2086:2093	fibrosis and cirrhosis patients	2063:2093	fibrosis and cirrhosis patients	2063:2093	BIOLOGICAL SIGNIFICANCE: We have quantified the difference in core fucosylation among three comparison groups (healthy control, fibrosis and cirrhosis patients) using a sensitive and selective LC-MS-MRM method.
29427759	9	13	theme	fibrosis	2063:2070	arg1	control					2054:2060	control	2054:2060	control	2054:2060	BIOLOGICAL SIGNIFICANCE: We have quantified the difference in core fucosylation among three comparison groups (healthy control, fibrosis and cirrhosis patients) using a sensitive and selective LC-MS-MRM method.
29427759	12	14	gly	N-glycopeptides	2447:2461	arg2	N-glycopeptides					2447:2461	N-glycopeptides	2447:2461	N-glycopeptides	2447:2461	Altered core fucosylation of N-glycopeptides might be used as an alternative serologic assay for the evaluation of fibrotic liver disease.
29427759	5	15	theme	core	1316:1319	arg1	fucosylation					1321:1332	core fucosylation	1316:1332	core fucosylation of 10 glycopeptides	1316:1352	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	2	16	theme	proteins	292:299	arg1	N-glycopeptides					267:281	core fucosylated N-glycopeptides	250:281	core fucosylated N-glycopeptides of serum proteins partially deglycosylated by a combination of endoglycosidases (endoF1, endoF2, and endoF3)	250:390	In this study, we carried out multiple reaction monitoring (MRM) quantification of core fucosylated N-glycopeptides of serum proteins partially deglycosylated by a combination of endoglycosidases (endoF1, endoF2, and endoF3).
29427759	5	17	theme	increased	876:884	arg1	fucosylation					891:902	increased core fucosylation	876:902	increased core fucosylation of 5 glycopeptides	876:921	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	9	18	dep	groups	2038:2043	arg1	patients					2086:2093	fibrosis and cirrhosis patients	2063:2093	fibrosis and cirrhosis patients	2063:2093	BIOLOGICAL SIGNIFICANCE: We have quantified the difference in core fucosylation among three comparison groups (healthy control, fibrosis and cirrhosis patients) using a sensitive and selective LC-MS-MRM method.
29427759	9	18	dep	groups	2038:2043	arg1	control					2054:2060	control	2054:2060	control	2054:2060	BIOLOGICAL SIGNIFICANCE: We have quantified the difference in core fucosylation among three comparison groups (healthy control, fibrosis and cirrhosis patients) using a sensitive and selective LC-MS-MRM method.
29427759	4	19	theme	N-glycopeptides	632:646	arg1	fucosylation					613:624	core fucosylation	608:624	core fucosylation of 22 N-glycopeptides derived from 17 proteins together with protein abundance of these glycoproteins in a cohort of 45 participants (15 disease-free control, 15 fibrosis and 15 cirrhosis patients)	608:822	Specifically, we quantified core fucosylation of 22 N-glycopeptides derived from 17 proteins together with protein abundance of these glycoproteins in a cohort of 45 participants (15 disease-free control, 15 fibrosis and 15 cirrhosis patients) using a multiplex nanoUPLC-MS-MRM workflow.
29427759	9	20	theme	cirrhosis	2076:2084	arg1	patients					2086:2093	fibrosis and cirrhosis patients	2063:2093	fibrosis and cirrhosis patients	2063:2093	BIOLOGICAL SIGNIFICANCE: We have quantified the difference in core fucosylation among three comparison groups (healthy control, fibrosis and cirrhosis patients) using a sensitive and selective LC-MS-MRM method.
29427759	9	20	theme	cirrhosis	2076:2084	arg1	control					2054:2060	control	2054:2060	control	2054:2060	BIOLOGICAL SIGNIFICANCE: We have quantified the difference in core fucosylation among three comparison groups (healthy control, fibrosis and cirrhosis patients) using a sensitive and selective LC-MS-MRM method.
29427759	1	21	gly	fucosylation	107:118	arg1	proteins					123:130	proteins	123:130	proteins	123:130	Aberrant core fucosylation of proteins has been linked to liver diseases.
29427759	0	22	from	diseases	70:77	arg1	analysis					13:20	Quantitative analysis	0:20	Quantitative analysis of core fucosylation of serum proteins in liver diseases by LC-MS-MRM.	0:91	Quantitative analysis of core fucosylation of serum proteins in liver diseases by LC-MS-MRM.
29427759	8	23	gly	glycopeptides	1851:1863	arg2	glycopeptides					1851:1863	core fucosylated glycopeptides	1834:1863	core fucosylated glycopeptides	1834:1863	It is expected that the fully optimized multiplex LC-MS-MRM assay of core fucosylated glycopeptides will be useful for the serologic assessment of the fibrosis of liver.
29427759	8	24	theme	LC-MS-MRM	1815:1823	arg1	useful					1873:1878	useful	1873:1878	useful	1873:1878	It is expected that the fully optimized multiplex LC-MS-MRM assay of core fucosylated glycopeptides will be useful for the serologic assessment of the fibrosis of liver.
29427759	8	24	theme	LC-MS-MRM	1815:1823	arg1	assay					1825:1829	the fully optimized multiplex LC-MS-MRM assay	1785:1829	the fully optimized multiplex LC-MS-MRM assay of core fucosylated glycopeptides	1785:1863	It is expected that the fully optimized multiplex LC-MS-MRM assay of core fucosylated glycopeptides will be useful for the serologic assessment of the fibrosis of liver.
29427759	2	25	theme	reaction	206:213	arg1	MRM					227:229	MRM	227:229	MRM	227:229	In this study, we carried out multiple reaction monitoring (MRM) quantification of core fucosylated N-glycopeptides of serum proteins partially deglycosylated by a combination of endoglycosidases (endoF1, endoF2, and endoF3).
29427759	2	25	theme	reaction	206:213	arg1	monitoring					215:224	multiple reaction monitoring	197:224	multiple reaction monitoring (MRM) quantification of core fucosylated N-glycopeptides of serum proteins partially deglycosylated by a combination of endoglycosidases (endoF1, endoF2, and endoF3)	197:390	In this study, we carried out multiple reaction monitoring (MRM) quantification of core fucosylated N-glycopeptides of serum proteins partially deglycosylated by a combination of endoglycosidases (endoF1, endoF2, and endoF3).
29427759	5	26	gly	fucosylation	891:902	arg1	glycopeptides					909:921	5 glycopeptides	907:921	5 glycopeptides	907:921	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	11	27	theme	decreased	2332:2340	arg1	fucosylation					2342:2353	increased and decreased fucosylation	2318:2353	increased and decreased fucosylation	2318:2353	Moreover, increased and decreased fucosylation was observed on different N-glycopeptides of the same protein.
29427759	5	28	dep	N630	961:964	arg1	i.e.					955:958	i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin	955:1097	i.e.	955:958	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	5	29	theme	plasma	1023:1028	arg1	inhibitor					1042:1050	plasma protease C1 inhibitor	1023:1050	plasma protease C1 inhibitor	1023:1050	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	4	30	dep	participants	746:757	arg1	patients					814:821	15 disease-free control, 15 fibrosis and 15 cirrhosis patients	760:821	patients	814:821	Specifically, we quantified core fucosylation of 22 N-glycopeptides derived from 17 proteins together with protein abundance of these glycoproteins in a cohort of 45 participants (15 disease-free control, 15 fibrosis and 15 cirrhosis patients) using a multiplex nanoUPLC-MS-MRM workflow.
29427759	4	30	dep	participants	746:757	arg1	fibrosis					788:795	15 disease-free control, 15 fibrosis and 15 cirrhosis patients	760:821	fibrosis	788:795	Specifically, we quantified core fucosylation of 22 N-glycopeptides derived from 17 proteins together with protein abundance of these glycoproteins in a cohort of 45 participants (15 disease-free control, 15 fibrosis and 15 cirrhosis patients) using a multiplex nanoUPLC-MS-MRM workflow.
29427759	10	31	theme	core	2242:2245	arg1	fucosylation					2247:2258	core fucosylation	2242:2258	core fucosylation	2242:2258	Despite an overall increase in core fucosylation of many of the glycoproteins that we examined, core fucosylation changed in a protein- and site-specific manner.
29427759	11	32	theme	increased	2318:2326	arg1	fucosylation					2342:2353	increased and decreased fucosylation	2318:2353	increased and decreased fucosylation	2318:2353	Moreover, increased and decreased fucosylation was observed on different N-glycopeptides of the same protein.
29427759	5	33	theme	fibrosis	945:952	arg1	increase					1101:1108	increase	1101:1108	increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican)	1101:1293	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	5	33	theme	fibrosis	945:952	arg1	stage					930:934	the stage	926:934	the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin)	926:1098	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	8	34	theme	fucosylated	1839:1849	arg1	glycopeptides					1851:1863	core fucosylated glycopeptides	1834:1863	core fucosylated glycopeptides	1834:1863	It is expected that the fully optimized multiplex LC-MS-MRM assay of core fucosylated glycopeptides will be useful for the serologic assessment of the fibrosis of liver.
29427759	5	35	theme	C1	1039:1040	arg1	inhibitor					1042:1050	plasma protease C1 inhibitor	1023:1050	plasma protease C1 inhibitor	1023:1050	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	6	36	theme	liver	1467:1471	arg1	fibrosis					1473:1480	liver fibrosis	1467:1480	liver fibrosis	1467:1480	Interestingly, although we observe an increase in the core fucosylation at N86 of vitronectin in liver fibrosis, core fucosylation decreases on the N169 glycopeptide of the same protein.
29427759	6	37	theme	protein	1548:1554	arg1	glycopeptide					1523:1534	the N169 glycopeptide	1514:1534	the N169 glycopeptide of the same protein	1514:1554	Interestingly, although we observe an increase in the core fucosylation at N86 of vitronectin in liver fibrosis, core fucosylation decreases on the N169 glycopeptide of the same protein.
29427759	12	38	theme	fibrotic	2533:2540	arg1	disease					2548:2554	fibrotic liver disease	2533:2554	fibrotic liver disease	2533:2554	Altered core fucosylation of N-glycopeptides might be used as an alternative serologic assay for the evaluation of fibrotic liver disease.
29427759	9	39	theme	LC-MS-MRM	2128:2136	arg1	method					2138:2143	a sensitive and selective LC-MS-MRM method	2102:2143	a sensitive and selective LC-MS-MRM method	2102:2143	BIOLOGICAL SIGNIFICANCE: We have quantified the difference in core fucosylation among three comparison groups (healthy control, fibrosis and cirrhosis patients) using a sensitive and selective LC-MS-MRM method.
29427759	5	40	theme	serotransferrin	969:983	arg1	serotransferrin					969:983	serotransferrin	969:983	serotransferrin	969:983	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	5	40	theme	serotransferrin	969:983	arg1	N630					961:964	N630	961:964	N630	961:964	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	5	41	theme	vitronectin	1087:1097	arg1	N86					1080:1082	N86	1080:1082	N86	1080:1082	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	5	41	theme	vitronectin	1087:1097	arg1	vitronectin					1087:1097	vitronectin	1087:1097	vitronectin	1087:1097	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	6	42	theme	vitronectin	1452:1462	arg1	N86					1445:1447	N86	1445:1447	N86 of vitronectin in liver fibrosis	1445:1480	Interestingly, although we observe an increase in the core fucosylation at N86 of vitronectin in liver fibrosis, core fucosylation decreases on the N169 glycopeptide of the same protein.
29427759	12	43	theme	disease	2548:2554	arg1	evaluation					2519:2528	the evaluation	2515:2528	the evaluation of fibrotic liver disease	2515:2554	Altered core fucosylation of N-glycopeptides might be used as an alternative serologic assay for the evaluation of fibrotic liver disease.
29427759	10	44	gly	fucosylation	2182:2193	arg1	many					2198:2201	many	2198:2201	many	2198:2201	Despite an overall increase in core fucosylation of many of the glycoproteins that we examined, core fucosylation changed in a protein- and site-specific manner.
29427759	10	44	gly	fucosylation	2182:2193	arg1	glycoproteins					2210:2222	the glycoproteins	2206:2222	the glycoproteins that we examined	2206:2239	Despite an overall increase in core fucosylation of many of the glycoproteins that we examined, core fucosylation changed in a protein- and site-specific manner.
29427759	6	45	theme	same	1543:1546	arg1	protein					1548:1554	the same protein	1539:1554	the same protein	1539:1554	Interestingly, although we observe an increase in the core fucosylation at N86 of vitronectin in liver fibrosis, core fucosylation decreases on the N169 glycopeptide of the same protein.
29427759	1	46	theme	liver	151:155	arg1	diseases					157:164	liver diseases	151:164	liver diseases	151:164	Aberrant core fucosylation of proteins has been linked to liver diseases.
29427759	3	47	gly	glycopeptides	505:517	arg2	glycopeptides					505:517	glycopeptides	505:517	glycopeptides	505:517	To minimize variability associated with the preparatory steps, the analysis was performed without enrichment of glycopeptides or fractionation of serum besides the nanoRP chromatography.
29427759	3	47	gly	glycopeptides	505:517	arg1	serum					539:543	serum	539:543	serum besides the nanoRP chromatography	539:577	To minimize variability associated with the preparatory steps, the analysis was performed without enrichment of glycopeptides or fractionation of serum besides the nanoRP chromatography.
29427759	5	48	gly	fucosylation	1321:1332	arg1	glycopeptides					1340:1352	10 glycopeptides	1337:1352	10 glycopeptides	1337:1352	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	2	49	theme	fucosylated	255:265	arg1	N-glycopeptides					267:281	core fucosylated N-glycopeptides	250:281	core fucosylated N-glycopeptides of serum proteins partially deglycosylated by a combination of endoglycosidases (endoF1, endoF2, and endoF3)	250:390	In this study, we carried out multiple reaction monitoring (MRM) quantification of core fucosylated N-glycopeptides of serum proteins partially deglycosylated by a combination of endoglycosidases (endoF1, endoF2, and endoF3).
29427759	4	50	gly	fucosylation	613:624	arg1	N-glycopeptides					632:646	22 N-glycopeptides	629:646	22 N-glycopeptides derived from 17 proteins together with protein abundance of these glycoproteins in a cohort of 45 participants (15 disease-free control, 15 fibrosis and 15 cirrhosis patients)	629:822	Specifically, we quantified core fucosylation of 22 N-glycopeptides derived from 17 proteins together with protein abundance of these glycoproteins in a cohort of 45 participants (15 disease-free control, 15 fibrosis and 15 cirrhosis patients) using a multiplex nanoUPLC-MS-MRM workflow.
29427759	7	51	dep	specific	1640:1647	arg1	specific					1640:1647	specific	1640:1647	specific	1640:1647	Our results demonstrate that the changes in core fucosylation are protein and site specific during the progression of fibrotic liver disease and independent of the changes in the quantity of N-glycoproteins.
29427759	7	51	dep	specific	1640:1647	arg1	protein					1623:1629	protein	1623:1629	protein	1623:1629	Our results demonstrate that the changes in core fucosylation are protein and site specific during the progression of fibrotic liver disease and independent of the changes in the quantity of N-glycoproteins.
29427759	7	51	dep	specific	1640:1647	arg1	changes					1590:1596	the changes	1586:1596	the changes in core fucosylation	1586:1617	Our results demonstrate that the changes in core fucosylation are protein and site specific during the progression of fibrotic liver disease and independent of the changes in the quantity of N-glycoproteins.
29427759	5	52	theme	J	1265:1265	arg1	chain					1267:1271	immunoglobulin J chain	1250:1271	immunoglobulin J chain	1250:1271	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	8	53	theme	liver	1928:1932	arg1	fibrosis					1916:1923	the fibrosis	1912:1923	the fibrosis of liver	1912:1932	It is expected that the fully optimized multiplex LC-MS-MRM assay of core fucosylated glycopeptides will be useful for the serologic assessment of the fibrosis of liver.
29427759	6	54	theme	N169	1518:1521	arg1	glycopeptide					1523:1534	the N169 glycopeptide	1514:1534	the N169 glycopeptide of the same protein	1514:1554	Interestingly, although we observe an increase in the core fucosylation at N86 of vitronectin in liver fibrosis, core fucosylation decreases on the N169 glycopeptide of the same protein.
29427759	0	55	from	fucosylation	30:41	arg1	diseases					70:77	liver diseases	64:77	liver diseases	64:77	Quantitative analysis of core fucosylation of serum proteins in liver diseases by LC-MS-MRM.
29427759	9	56	theme	BIOLOGICAL	1935:1944	arg1	SIGNIFICANCE					1946:1957	BIOLOGICAL SIGNIFICANCE	1935:1957	BIOLOGICAL SIGNIFICANCE: We have quantified the difference in core fucosylation among three comparison groups (healthy control, fibrosis and cirrhosis patients) using a sensitive and selective LC-MS-MRM method.	1935:2144	BIOLOGICAL SIGNIFICANCE: We have quantified the difference in core fucosylation among three comparison groups (healthy control, fibrosis and cirrhosis patients) using a sensitive and selective LC-MS-MRM method.
29427759	0	57	theme	Quantitative	0:11	arg1	analysis					13:20	Quantitative analysis	0:20	Quantitative analysis of core fucosylation of serum proteins in liver diseases by LC-MS-MRM.	0:91	Quantitative analysis of core fucosylation of serum proteins in liver diseases by LC-MS-MRM.
29427759	5	58	theme	liver	939:943	arg1	fibrosis					945:952	liver fibrosis	939:952	liver fibrosis	939:952	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	7	59	from	changes	1721:1727	arg1	quantity					1736:1743	the quantity	1732:1743	the quantity of N-glycoproteins	1732:1762	Our results demonstrate that the changes in core fucosylation are protein and site specific during the progression of fibrotic liver disease and independent of the changes in the quantity of N-glycoproteins.
29427759	10	60	from	increase	2165:2172	arg1	fucosylation					2182:2193	core fucosylation	2177:2193	core fucosylation of many of the glycoproteins that we examined	2177:2239	Despite an overall increase in core fucosylation of many of the glycoproteins that we examined, core fucosylation changed in a protein- and site-specific manner.
29427759	12	61	theme	serologic	2495:2503	arg1	assay					2505:2509	an alternative serologic assay	2480:2509	an alternative serologic assay for the evaluation of fibrotic liver disease	2480:2554	Altered core fucosylation of N-glycopeptides might be used as an alternative serologic assay for the evaluation of fibrotic liver disease.
29427759	12	61	theme	serologic	2495:2503	arg1	fucosylation					2431:2442	Altered core fucosylation	2418:2442	Altered core fucosylation of N-glycopeptides	2418:2461	Altered core fucosylation of N-glycopeptides might be used as an alternative serologic assay for the evaluation of fibrotic liver disease.
29427759	1	62	theme	core	102:105	arg1	fucosylation					107:118	Aberrant core fucosylation	93:118	Aberrant core fucosylation of proteins	93:130	Aberrant core fucosylation of proteins has been linked to liver diseases.
29427759	11	63	gly	N-glycopeptides	2381:2395	arg1	protein					2409:2415	the same protein	2400:2415	the same protein	2400:2415	Moreover, increased and decreased fucosylation was observed on different N-glycopeptides of the same protein.
29427759	11	63	gly	N-glycopeptides	2381:2395	arg2	N-glycopeptides					2381:2395	different N-glycopeptides	2371:2395	different N-glycopeptides of the same protein	2371:2415	Moreover, increased and decreased fucosylation was observed on different N-glycopeptides of the same protein.
29427759	0	64	theme	fucosylation	30:41	arg1	analysis					13:20	Quantitative analysis	0:20	Quantitative analysis of core fucosylation of serum proteins in liver diseases by LC-MS-MRM.	0:91	Quantitative analysis of core fucosylation of serum proteins in liver diseases by LC-MS-MRM.
29427759	5	65	from	increase	1101:1108	arg1	stage					1147:1151	the stage	1143:1151	the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican)	1143:1293	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	0	66	theme	serum	46:50	arg1	proteins					52:59	serum proteins	46:59	serum proteins	46:59	Quantitative analysis of core fucosylation of serum proteins in liver diseases by LC-MS-MRM.
29427759	6	67	gly	glycopeptide	1523:1534	arg1	protein					1548:1554	the same protein	1539:1554	the same protein	1539:1554	Interestingly, although we observe an increase in the core fucosylation at N86 of vitronectin in liver fibrosis, core fucosylation decreases on the N169 glycopeptide of the same protein.
29427759	6	67	gly	glycopeptide	1523:1534	arg2	glycopeptide					1523:1534	the N169 glycopeptide	1514:1534	the N169 glycopeptide of the same protein	1514:1554	Interestingly, although we observe an increase in the core fucosylation at N86 of vitronectin in liver fibrosis, core fucosylation decreases on the N169 glycopeptide of the same protein.
29427759	12	68	gly	fucosylation	2431:2442	arg1	N-glycopeptides					2447:2461	N-glycopeptides	2447:2461	N-glycopeptides	2447:2461	Altered core fucosylation of N-glycopeptides might be used as an alternative serologic assay for the evaluation of fibrotic liver disease.
29427759	2	69	gly	deglycosylated	311:324	arg1	proteins					292:299	serum proteins	286:299	serum proteins partially deglycosylated by a combination of endoglycosidases (endoF1, endoF2, and endoF3)	286:390	In this study, we carried out multiple reaction monitoring (MRM) quantification of core fucosylated N-glycopeptides of serum proteins partially deglycosylated by a combination of endoglycosidases (endoF1, endoF2, and endoF3).
29427759	7	70	gly	N-glycoproteins	1748:1762	arg1	N-glycoproteins					1748:1762	N-glycoproteins	1748:1762	N-glycoproteins	1748:1762	Our results demonstrate that the changes in core fucosylation are protein and site specific during the progression of fibrotic liver disease and independent of the changes in the quantity of N-glycoproteins.
29427759	5	71	theme	lumican	1286:1292	arg1	lumican					1286:1292	lumican	1286:1292	lumican	1286:1292	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	5	71	theme	lumican	1286:1292	arg1	N127					1278:1281	N127	1278:1281	N127	1278:1281	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	2	72	theme	endoglycosidases	346:361	arg1	combination					331:341	a combination	329:341	a combination of endoglycosidases (endoF1, endoF2, and endoF3)	329:390	In this study, we carried out multiple reaction monitoring (MRM) quantification of core fucosylated N-glycopeptides of serum proteins partially deglycosylated by a combination of endoglycosidases (endoF1, endoF2, and endoF3).
29427759	5	73	theme	cirrhosis	1156:1164	arg1	stage					1147:1151	the stage	1143:1151	the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican)	1143:1293	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	10	74	theme	core	2177:2180	arg1	fucosylation					2182:2193	core fucosylation	2177:2193	core fucosylation of many of the glycoproteins that we examined	2177:2239	Despite an overall increase in core fucosylation of many of the glycoproteins that we examined, core fucosylation changed in a protein- and site-specific manner.
29427759	7	75	theme	disease	1690:1696	arg1	progression					1660:1670	the progression	1656:1670	the progression of fibrotic liver disease	1656:1696	Our results demonstrate that the changes in core fucosylation are protein and site specific during the progression of fibrotic liver disease and independent of the changes in the quantity of N-glycoproteins.
29427759	12	76	theme	N-glycopeptides	2447:2461	arg1	assay					2505:2509	an alternative serologic assay	2480:2509	an alternative serologic assay for the evaluation of fibrotic liver disease	2480:2554	Altered core fucosylation of N-glycopeptides might be used as an alternative serologic assay for the evaluation of fibrotic liver disease.
29427759	12	76	theme	N-glycopeptides	2447:2461	arg1	fucosylation					2431:2442	Altered core fucosylation	2418:2442	Altered core fucosylation of N-glycopeptides	2418:2461	Altered core fucosylation of N-glycopeptides might be used as an alternative serologic assay for the evaluation of fibrotic liver disease.
29427759	2	77	gly	fucosylated	255:265	arg1	N-glycopeptides					267:281	core fucosylated N-glycopeptides	250:281	core fucosylated N-glycopeptides of serum proteins partially deglycosylated by a combination of endoglycosidases (endoF1, endoF2, and endoF3)	250:390	In this study, we carried out multiple reaction monitoring (MRM) quantification of core fucosylated N-glycopeptides of serum proteins partially deglycosylated by a combination of endoglycosidases (endoF1, endoF2, and endoF3).
29427759	2	78	theme	N-glycopeptides	267:281	arg1	quantification					232:245	multiple reaction monitoring (MRM) quantification	197:245	multiple reaction monitoring (MRM) quantification of core fucosylated N-glycopeptides of serum proteins partially deglycosylated by a combination of endoglycosidases (endoF1, endoF2, and endoF3)	197:390	In this study, we carried out multiple reaction monitoring (MRM) quantification of core fucosylated N-glycopeptides of serum proteins partially deglycosylated by a combination of endoglycosidases (endoF1, endoF2, and endoF3).
29427759	5	79	gly	find	871:874	arg1	increase					1101:1108	increase	1101:1108	increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican)	1101:1293	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	5	79	gly	find	871:874	arg1	stage					930:934	the stage	926:934	the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin)	926:1098	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	7	80	theme	fibrotic	1675:1682	arg1	disease					1690:1696	fibrotic liver disease	1675:1696	fibrotic liver disease	1675:1696	Our results demonstrate that the changes in core fucosylation are protein and site specific during the progression of fibrotic liver disease and independent of the changes in the quantity of N-glycoproteins.
29427759	5	81	from	stage	1147:1151	arg1	glycopeptides					1126:1138	additional 6 glycopeptides	1113:1138	additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican)	1113:1293	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	5	81	from	stage	1147:1151	arg1	stage					930:934	the stage	926:934	the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin)	926:1098	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	5	81	from	stage	1147:1151	arg1	increase					1101:1108	increase	1101:1108	increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican)	1101:1293	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	2	82	theme	core	250:253	arg1	N-glycopeptides					267:281	core fucosylated N-glycopeptides	250:281	core fucosylated N-glycopeptides of serum proteins partially deglycosylated by a combination of endoglycosidases (endoF1, endoF2, and endoF3)	250:390	In this study, we carried out multiple reaction monitoring (MRM) quantification of core fucosylated N-glycopeptides of serum proteins partially deglycosylated by a combination of endoglycosidases (endoF1, endoF2, and endoF3).
29427759	12	83	theme	Altered	2418:2424	arg1	assay					2505:2509	an alternative serologic assay	2480:2509	an alternative serologic assay for the evaluation of fibrotic liver disease	2480:2554	Altered core fucosylation of N-glycopeptides might be used as an alternative serologic assay for the evaluation of fibrotic liver disease.
29427759	12	83	theme	Altered	2418:2424	arg1	fucosylation					2431:2442	Altered core fucosylation	2418:2442	Altered core fucosylation of N-glycopeptides	2418:2461	Altered core fucosylation of N-glycopeptides might be used as an alternative serologic assay for the evaluation of fibrotic liver disease.
29427759	3	84	theme	nanoRP	557:562	arg1	chromatography					564:577	the nanoRP chromatography	553:577	the nanoRP chromatography	553:577	To minimize variability associated with the preparatory steps, the analysis was performed without enrichment of glycopeptides or fractionation of serum besides the nanoRP chromatography.
29427759	6	85	theme	core	1424:1427	arg1	fucosylation					1429:1440	the core fucosylation	1420:1440	the core fucosylation	1420:1440	Interestingly, although we observe an increase in the core fucosylation at N86 of vitronectin in liver fibrosis, core fucosylation decreases on the N169 glycopeptide of the same protein.
29427759	11	86	theme	different	2371:2379	arg1	N-glycopeptides					2381:2395	different N-glycopeptides	2371:2395	different N-glycopeptides of the same protein	2371:2415	Moreover, increased and decreased fucosylation was observed on different N-glycopeptides of the same protein.
29427759	4	87	theme	nanoUPLC-MS-MRM	842:856	arg1	workflow					858:865	a multiplex nanoUPLC-MS-MRM workflow	830:865	a multiplex nanoUPLC-MS-MRM workflow	830:865	Specifically, we quantified core fucosylation of 22 N-glycopeptides derived from 17 proteins together with protein abundance of these glycoproteins in a cohort of 45 participants (15 disease-free control, 15 fibrosis and 15 cirrhosis patients) using a multiplex nanoUPLC-MS-MRM workflow.
29427759	4	88	gly	glycoproteins	714:726	arg1	glycoproteins					714:726	these glycoproteins	708:726	these glycoproteins	708:726	Specifically, we quantified core fucosylation of 22 N-glycopeptides derived from 17 proteins together with protein abundance of these glycoproteins in a cohort of 45 participants (15 disease-free control, 15 fibrosis and 15 cirrhosis patients) using a multiplex nanoUPLC-MS-MRM workflow.
29427759	5	89	theme	fucosylation	1321:1332	arg1	degree					1306:1311	the degree	1302:1311	the degree of core fucosylation of 10 glycopeptides	1302:1352	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	2	90	theme	serum	286:290	arg1	proteins					292:299	serum proteins	286:299	serum proteins partially deglycosylated by a combination of endoglycosidases (endoF1, endoF2, and endoF3)	286:390	In this study, we carried out multiple reaction monitoring (MRM) quantification of core fucosylated N-glycopeptides of serum proteins partially deglycosylated by a combination of endoglycosidases (endoF1, endoF2, and endoF3).
29427759	11	91	gly	fucosylation	2342:2353	arg1	N-glycopeptides					2381:2395	different N-glycopeptides	2371:2395	different N-glycopeptides of the same protein	2371:2415	Moreover, increased and decreased fucosylation was observed on different N-glycopeptides of the same protein.
29427759	5	92	gly	glycopeptides	909:921	arg2	glycopeptides					909:921	5 glycopeptides	907:921	5 glycopeptides	907:921	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	8	93	gly	fucosylated	1839:1849	arg1	glycopeptides					1851:1863	core fucosylated glycopeptides	1834:1863	core fucosylated glycopeptides	1834:1863	It is expected that the fully optimized multiplex LC-MS-MRM assay of core fucosylated glycopeptides will be useful for the serologic assessment of the fibrosis of liver.
29427759	2	94	theme	monitoring	215:224	arg1	quantification					232:245	multiple reaction monitoring (MRM) quantification	197:245	multiple reaction monitoring (MRM) quantification of core fucosylated N-glycopeptides of serum proteins partially deglycosylated by a combination of endoglycosidases (endoF1, endoF2, and endoF3)	197:390	In this study, we carried out multiple reaction monitoring (MRM) quantification of core fucosylated N-glycopeptides of serum proteins partially deglycosylated by a combination of endoglycosidases (endoF1, endoF2, and endoF3).
29427759	10	95	theme	glycoproteins	2210:2222	arg1	many					2198:2201	many	2198:2201	many	2198:2201	Despite an overall increase in core fucosylation of many of the glycoproteins that we examined, core fucosylation changed in a protein- and site-specific manner.
29427759	10	95	theme	glycoproteins	2210:2222	arg1	glycoproteins					2210:2222	the glycoproteins	2206:2222	the glycoproteins that we examined	2206:2239	Despite an overall increase in core fucosylation of many of the glycoproteins that we examined, core fucosylation changed in a protein- and site-specific manner.
29427759	5	96	dep	N138	1173:1176	arg1	i.e.					1167:1170	i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican	1167:1292	i.e.	1167:1170	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	8	97	theme	core	1834:1837	arg1	glycopeptides					1851:1863	core fucosylated glycopeptides	1834:1863	core fucosylated glycopeptides	1834:1863	It is expected that the fully optimized multiplex LC-MS-MRM assay of core fucosylated glycopeptides will be useful for the serologic assessment of the fibrosis of liver.
29427759	5	98	theme	ceruloplasmin	1061:1073	arg1	N397					1053:1056	N397	1053:1056	N397	1053:1056	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	5	98	theme	ceruloplasmin	1061:1073	arg1	ceruloplasmin					1061:1073	ceruloplasmin	1061:1073	ceruloplasmin	1061:1073	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	2	99	theme	multiple	197:204	arg1	MRM					227:229	MRM	227:229	MRM	227:229	In this study, we carried out multiple reaction monitoring (MRM) quantification of core fucosylated N-glycopeptides of serum proteins partially deglycosylated by a combination of endoglycosidases (endoF1, endoF2, and endoF3).
29427759	2	99	theme	multiple	197:204	arg1	monitoring					215:224	multiple reaction monitoring	197:224	multiple reaction monitoring (MRM) quantification of core fucosylated N-glycopeptides of serum proteins partially deglycosylated by a combination of endoglycosidases (endoF1, endoF2, and endoF3)	197:390	In this study, we carried out multiple reaction monitoring (MRM) quantification of core fucosylated N-glycopeptides of serum proteins partially deglycosylated by a combination of endoglycosidases (endoF1, endoF2, and endoF3).
29427759	6	100	theme	core	1483:1486	arg1	fucosylation					1488:1499	core fucosylation	1483:1499	core fucosylation	1483:1499	Interestingly, although we observe an increase in the core fucosylation at N86 of vitronectin in liver fibrosis, core fucosylation decreases on the N169 glycopeptide of the same protein.
29427759	5	101	theme	glycopeptides	909:921	arg1	fucosylation					891:902	increased core fucosylation	876:902	increased core fucosylation of 5 glycopeptides	876:921	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	8	102	theme	multiplex	1805:1813	arg1	useful					1873:1878	useful	1873:1878	useful	1873:1878	It is expected that the fully optimized multiplex LC-MS-MRM assay of core fucosylated glycopeptides will be useful for the serologic assessment of the fibrosis of liver.
29427759	8	102	theme	multiplex	1805:1813	arg1	assay					1825:1829	the fully optimized multiplex LC-MS-MRM assay	1785:1829	the fully optimized multiplex LC-MS-MRM assay of core fucosylated glycopeptides	1785:1863	It is expected that the fully optimized multiplex LC-MS-MRM assay of core fucosylated glycopeptides will be useful for the serologic assessment of the fibrosis of liver.
29427759	4	103	theme	glycoproteins	714:726	arg1	abundance					695:703	protein abundance	687:703	protein abundance of these glycoproteins in a cohort of 45 participants (15 disease-free control, 15 fibrosis and 15 cirrhosis patients)	687:822	Specifically, we quantified core fucosylation of 22 N-glycopeptides derived from 17 proteins together with protein abundance of these glycoproteins in a cohort of 45 participants (15 disease-free control, 15 fibrosis and 15 cirrhosis patients) using a multiplex nanoUPLC-MS-MRM workflow.
29427759	5	104	theme	clusterin	1213:1221	arg1	N354					1205:1208	N354	1205:1208	N354	1205:1208	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	5	104	theme	clusterin	1213:1221	arg1	clusterin					1213:1221	clusterin	1213:1221	clusterin	1213:1221	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	9	105	theme	sensitive	2104:2112	arg1	method					2138:2143	a sensitive and selective LC-MS-MRM method	2102:2143	a sensitive and selective LC-MS-MRM method	2102:2143	BIOLOGICAL SIGNIFICANCE: We have quantified the difference in core fucosylation among three comparison groups (healthy control, fibrosis and cirrhosis patients) using a sensitive and selective LC-MS-MRM method.
29427759	8	106	theme	glycopeptides	1851:1863	arg1	useful					1873:1878	useful	1873:1878	useful	1873:1878	It is expected that the fully optimized multiplex LC-MS-MRM assay of core fucosylated glycopeptides will be useful for the serologic assessment of the fibrosis of liver.
29427759	8	106	theme	glycopeptides	1851:1863	arg1	assay					1825:1829	the fully optimized multiplex LC-MS-MRM assay	1785:1829	the fully optimized multiplex LC-MS-MRM assay of core fucosylated glycopeptides	1785:1863	It is expected that the fully optimized multiplex LC-MS-MRM assay of core fucosylated glycopeptides will be useful for the serologic assessment of the fibrosis of liver.
29427759	5	107	theme	protease	1030:1037	arg1	inhibitor					1042:1050	plasma protease C1 inhibitor	1023:1050	plasma protease C1 inhibitor	1023:1050	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	1	108	theme	proteins	123:130	arg1	fucosylation					107:118	Aberrant core fucosylation	93:118	Aberrant core fucosylation of proteins	93:130	Aberrant core fucosylation of proteins has been linked to liver diseases.
29427759	5	109	dep	cirrhosis	1156:1164	arg1	ceruloplasmin					1190:1202	ceruloplasmin	1190:1202	ceruloplasmin	1190:1202	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	5	109	dep	cirrhosis	1156:1164	arg1	chain					1267:1271	immunoglobulin J chain	1250:1271	immunoglobulin J chain	1250:1271	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	5	109	dep	cirrhosis	1156:1164	arg1	N354					1205:1208	N354	1205:1208	N354	1205:1208	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	5	109	dep	cirrhosis	1156:1164	arg1	hemopexin					1232:1240	hemopexin	1232:1240	hemopexin	1232:1240	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	5	109	dep	cirrhosis	1156:1164	arg1	N138					1173:1176	N138	1173:1176	N138	1173:1176	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	5	109	dep	cirrhosis	1156:1164	arg1	N71					1243:1245	N71	1243:1245	N71	1243:1245	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	5	109	dep	cirrhosis	1156:1164	arg1	N762					1182:1185	N762	1182:1185	N762	1182:1185	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	5	109	dep	cirrhosis	1156:1164	arg1	N127					1278:1281	N127	1278:1281	N127	1278:1281	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	5	109	dep	cirrhosis	1156:1164	arg1	clusterin					1213:1221	clusterin	1213:1221	clusterin	1213:1221	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	5	109	dep	cirrhosis	1156:1164	arg1	lumican					1286:1292	lumican	1286:1292	lumican	1286:1292	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	5	109	dep	cirrhosis	1156:1164	arg1	N187					1224:1227	N187	1224:1227	N187	1224:1227	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	4	110	theme	disease-free	763:774	arg1	fibrosis					788:795	15 disease-free control, 15 fibrosis and 15 cirrhosis patients	760:821	fibrosis	788:795	Specifically, we quantified core fucosylation of 22 N-glycopeptides derived from 17 proteins together with protein abundance of these glycoproteins in a cohort of 45 participants (15 disease-free control, 15 fibrosis and 15 cirrhosis patients) using a multiplex nanoUPLC-MS-MRM workflow.
29427759	12	111	theme	liver	2542:2546	arg1	disease					2548:2554	fibrotic liver disease	2533:2554	fibrotic liver disease	2533:2554	Altered core fucosylation of N-glycopeptides might be used as an alternative serologic assay for the evaluation of fibrotic liver disease.
29427759	9	112	theme	selective	2118:2126	arg1	method					2138:2143	a sensitive and selective LC-MS-MRM method	2102:2143	a sensitive and selective LC-MS-MRM method	2102:2143	BIOLOGICAL SIGNIFICANCE: We have quantified the difference in core fucosylation among three comparison groups (healthy control, fibrosis and cirrhosis patients) using a sensitive and selective LC-MS-MRM method.
29427759	0	113	theme	liver	64:68	arg1	diseases					70:77	liver diseases	64:77	liver diseases	64:77	Quantitative analysis of core fucosylation of serum proteins in liver diseases by LC-MS-MRM.
29427759	5	114	theme	inhibitor	1042:1050	arg1	inhibitor					1042:1050	plasma protease C1 inhibitor	1023:1050	plasma protease C1 inhibitor	1023:1050	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	5	114	theme	inhibitor	1042:1050	arg1	N253					1015:1018	N253	1015:1018	N253	1015:1018	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	5	115	theme	core	886:889	arg1	fucosylation					891:902	increased core fucosylation	876:902	increased core fucosylation of 5 glycopeptides	876:921	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	10	116	theme	protein-	2273:2280	arg1	manner					2300:2305	a protein- and site-specific manner	2271:2305	a protein- and site-specific manner	2271:2305	Despite an overall increase in core fucosylation of many of the glycoproteins that we examined, core fucosylation changed in a protein- and site-specific manner.
29427759	7	117	from	changes	1590:1596	arg1	fucosylation					1606:1617	core fucosylation	1601:1617	core fucosylation	1601:1617	Our results demonstrate that the changes in core fucosylation are protein and site specific during the progression of fibrotic liver disease and independent of the changes in the quantity of N-glycoproteins.
29427759	5	118	gly	glycopeptides	1126:1138	arg2	glycopeptides					1126:1138	additional 6 glycopeptides	1113:1138	additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican)	1113:1293	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	4	119	theme	protein	687:693	arg1	abundance					695:703	protein abundance	687:703	protein abundance of these glycoproteins in a cohort of 45 participants (15 disease-free control, 15 fibrosis and 15 cirrhosis patients)	687:822	Specifically, we quantified core fucosylation of 22 N-glycopeptides derived from 17 proteins together with protein abundance of these glycoproteins in a cohort of 45 participants (15 disease-free control, 15 fibrosis and 15 cirrhosis patients) using a multiplex nanoUPLC-MS-MRM workflow.
29427759	5	120	theme	ceruloplasmin	1190:1202	arg1	ceruloplasmin					1190:1202	ceruloplasmin	1190:1202	ceruloplasmin	1190:1202	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	5	120	theme	ceruloplasmin	1190:1202	arg1	N138					1173:1176	N138	1173:1176	N138	1173:1176	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	5	121	gly	glycopeptides	1340:1352	arg2	glycopeptides					1340:1352	10 glycopeptides	1337:1352	10 glycopeptides	1337:1352	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	9	122	from	difference	1983:1992	arg1	fucosylation					2002:2013	core fucosylation	1997:2013	core fucosylation	1997:2013	BIOLOGICAL SIGNIFICANCE: We have quantified the difference in core fucosylation among three comparison groups (healthy control, fibrosis and cirrhosis patients) using a sensitive and selective LC-MS-MRM method.
29427759	8	123	theme	optimized	1795:1803	arg1	useful					1873:1878	useful	1873:1878	useful	1873:1878	It is expected that the fully optimized multiplex LC-MS-MRM assay of core fucosylated glycopeptides will be useful for the serologic assessment of the fibrosis of liver.
29427759	8	123	theme	optimized	1795:1803	arg1	assay					1825:1829	the fully optimized multiplex LC-MS-MRM assay	1785:1829	the fully optimized multiplex LC-MS-MRM assay of core fucosylated glycopeptides	1785:1863	It is expected that the fully optimized multiplex LC-MS-MRM assay of core fucosylated glycopeptides will be useful for the serologic assessment of the fibrosis of liver.
29427759	0	124	from	analysis	13:20	arg1	diseases					70:77	liver diseases	64:77	liver diseases	64:77	Quantitative analysis of core fucosylation of serum proteins in liver diseases by LC-MS-MRM.
29427759	9	125	theme	core	1997:2000	arg1	fucosylation					2002:2013	core fucosylation	1997:2013	core fucosylation	1997:2013	BIOLOGICAL SIGNIFICANCE: We have quantified the difference in core fucosylation among three comparison groups (healthy control, fibrosis and cirrhosis patients) using a sensitive and selective LC-MS-MRM method.
29427759	8	126	theme	serologic	1888:1896	arg1	assessment					1898:1907	the serologic assessment	1884:1907	the serologic assessment of the fibrosis of liver	1884:1932	It is expected that the fully optimized multiplex LC-MS-MRM assay of core fucosylated glycopeptides will be useful for the serologic assessment of the fibrosis of liver.
29427759	7	127	theme	core	1601:1604	arg1	fucosylation					1606:1617	core fucosylation	1601:1617	core fucosylation	1601:1617	Our results demonstrate that the changes in core fucosylation are protein and site specific during the progression of fibrotic liver disease and independent of the changes in the quantity of N-glycoproteins.
29427759	5	128	dep	stage	930:934	arg1	N107					986:989	N107	986:989	N107	986:989	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	5	128	dep	stage	930:934	arg1	inhibitor					1042:1050	plasma protease C1 inhibitor	1023:1050	plasma protease C1 inhibitor	1023:1050	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	5	128	dep	stage	930:934	arg1	N630					961:964	N630	961:964	N630	961:964	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	5	128	dep	stage	930:934	arg1	alpha-1-antitrypsin					994:1012	alpha-1-antitrypsin	994:1012	alpha-1-antitrypsin	994:1012	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	5	128	dep	stage	930:934	arg1	N86					1080:1082	N86	1080:1082	N86	1080:1082	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	5	128	dep	stage	930:934	arg1	N253					1015:1018	N253	1015:1018	N253	1015:1018	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	5	128	dep	stage	930:934	arg1	N397					1053:1056	N397	1053:1056	N397	1053:1056	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	5	128	dep	stage	930:934	arg1	serotransferrin					969:983	serotransferrin	969:983	serotransferrin	969:983	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	5	128	dep	stage	930:934	arg1	vitronectin					1087:1097	vitronectin	1087:1097	vitronectin	1087:1097	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	5	128	dep	stage	930:934	arg1	ceruloplasmin					1061:1073	ceruloplasmin	1061:1073	ceruloplasmin	1061:1073	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	5	129	theme	immunoglobulin	1250:1263	arg1	chain					1267:1271	immunoglobulin J chain	1250:1271	immunoglobulin J chain	1250:1271	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	6	130	from	N86	1445:1447	arg1	fibrosis					1473:1480	liver fibrosis	1467:1480	liver fibrosis	1467:1480	Interestingly, although we observe an increase in the core fucosylation at N86 of vitronectin in liver fibrosis, core fucosylation decreases on the N169 glycopeptide of the same protein.
29427759	10	131	theme	site-specific	2286:2298	arg1	manner					2300:2305	a protein- and site-specific manner	2271:2305	a protein- and site-specific manner	2271:2305	Despite an overall increase in core fucosylation of many of the glycoproteins that we examined, core fucosylation changed in a protein- and site-specific manner.
29427759	11	132	theme	same	2404:2407	arg1	protein					2409:2415	the same protein	2400:2415	the same protein	2400:2415	Moreover, increased and decreased fucosylation was observed on different N-glycopeptides of the same protein.
29427759	10	133	theme	overall	2157:2163	arg1	increase					2165:2172	an overall increase	2154:2172	an overall increase in core fucosylation of many of the glycoproteins that we examined	2154:2239	Despite an overall increase in core fucosylation of many of the glycoproteins that we examined, core fucosylation changed in a protein- and site-specific manner.
29427759	4	134	theme	control	776:782	arg1	fibrosis					788:795	15 disease-free control, 15 fibrosis and 15 cirrhosis patients	760:821	fibrosis	788:795	Specifically, we quantified core fucosylation of 22 N-glycopeptides derived from 17 proteins together with protein abundance of these glycoproteins in a cohort of 45 participants (15 disease-free control, 15 fibrosis and 15 cirrhosis patients) using a multiplex nanoUPLC-MS-MRM workflow.
29427759	5	135	theme	chain	1267:1271	arg1	N71					1243:1245	N71	1243:1245	N71	1243:1245	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	5	135	theme	chain	1267:1271	arg1	chain					1267:1271	immunoglobulin J chain	1250:1271	immunoglobulin J chain	1250:1271	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	8	136	theme	fibrosis	1916:1923	arg1	assessment					1898:1907	the serologic assessment	1884:1907	the serologic assessment of the fibrosis of liver	1884:1932	It is expected that the fully optimized multiplex LC-MS-MRM assay of core fucosylated glycopeptides will be useful for the serologic assessment of the fibrosis of liver.
29427759	6	137	from	increase	1408:1415	arg1	fucosylation					1429:1440	the core fucosylation	1420:1440	the core fucosylation	1420:1440	Interestingly, although we observe an increase in the core fucosylation at N86 of vitronectin in liver fibrosis, core fucosylation decreases on the N169 glycopeptide of the same protein.
29427759	5	138	theme	hemopexin	1232:1240	arg1	hemopexin					1232:1240	hemopexin	1232:1240	hemopexin	1232:1240	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	5	138	theme	hemopexin	1232:1240	arg1	N187					1224:1227	N187	1224:1227	N187	1224:1227	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	0	139	theme	core	25:28	arg1	fucosylation					30:41	core fucosylation	25:41	core fucosylation of serum proteins in liver diseases	25:77	Quantitative analysis of core fucosylation of serum proteins in liver diseases by LC-MS-MRM.
29427759	1	140	theme	Aberrant	93:100	arg1	fucosylation					107:118	Aberrant core fucosylation	93:118	Aberrant core fucosylation of proteins	93:130	Aberrant core fucosylation of proteins has been linked to liver diseases.
29427759	4	141	theme	participants	746:757	arg1	cohort					733:738	a cohort	731:738	a cohort of 45 participants (15 disease-free control, 15 fibrosis and 15 cirrhosis patients)	731:822	Specifically, we quantified core fucosylation of 22 N-glycopeptides derived from 17 proteins together with protein abundance of these glycoproteins in a cohort of 45 participants (15 disease-free control, 15 fibrosis and 15 cirrhosis patients) using a multiplex nanoUPLC-MS-MRM workflow.
29427759	10	142	gly	glycoproteins	2210:2222	arg1	glycoproteins					2210:2222	the glycoproteins	2206:2222	the glycoproteins that we examined	2206:2239	Despite an overall increase in core fucosylation of many of the glycoproteins that we examined, core fucosylation changed in a protein- and site-specific manner.
29427759	2	143	dep	endoglycosidases	346:361	arg1	endoglycosidases					346:361	endoglycosidases	346:361	endoglycosidases (endoF1, endoF2, and endoF3)	346:390	In this study, we carried out multiple reaction monitoring (MRM) quantification of core fucosylated N-glycopeptides of serum proteins partially deglycosylated by a combination of endoglycosidases (endoF1, endoF2, and endoF3).
29427759	2	143	dep	endoglycosidases	346:361	arg1	endoF2					372:377	endoF2	372:377	endoF2	372:377	In this study, we carried out multiple reaction monitoring (MRM) quantification of core fucosylated N-glycopeptides of serum proteins partially deglycosylated by a combination of endoglycosidases (endoF1, endoF2, and endoF3).
29427759	2	143	dep	endoglycosidases	346:361	arg1	endoF3					384:389	endoF3	384:389	endoF3	384:389	In this study, we carried out multiple reaction monitoring (MRM) quantification of core fucosylated N-glycopeptides of serum proteins partially deglycosylated by a combination of endoglycosidases (endoF1, endoF2, and endoF3).
29427759	2	143	dep	endoglycosidases	346:361	arg1	endoF1					364:369	endoF1	364:369	endoF1	364:369	In this study, we carried out multiple reaction monitoring (MRM) quantification of core fucosylated N-glycopeptides of serum proteins partially deglycosylated by a combination of endoglycosidases (endoF1, endoF2, and endoF3).
29427759	5	144	theme	alpha-1-antitrypsin	994:1012	arg1	N107					986:989	N107	986:989	N107	986:989	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	5	144	theme	alpha-1-antitrypsin	994:1012	arg1	alpha-1-antitrypsin					994:1012	alpha-1-antitrypsin	994:1012	alpha-1-antitrypsin	994:1012	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	4	145	theme	cirrhosis	804:812	arg1	patients					814:821	15 disease-free control, 15 fibrosis and 15 cirrhosis patients	760:821	patients	814:821	Specifically, we quantified core fucosylation of 22 N-glycopeptides derived from 17 proteins together with protein abundance of these glycoproteins in a cohort of 45 participants (15 disease-free control, 15 fibrosis and 15 cirrhosis patients) using a multiplex nanoUPLC-MS-MRM workflow.
29427759	12	146	used	used	2472:2475	arg2	assay					2505:2509	an alternative serologic assay	2480:2509	an alternative serologic assay for the evaluation of fibrotic liver disease	2480:2554	Altered core fucosylation of N-glycopeptides might be used as an alternative serologic assay for the evaluation of fibrotic liver disease.
29427759	12	146	used	used	2472:2475	arg2	fucosylation					2431:2442	Altered core fucosylation	2418:2442	Altered core fucosylation of N-glycopeptides	2418:2461	Altered core fucosylation of N-glycopeptides might be used as an alternative serologic assay for the evaluation of fibrotic liver disease.
29427759	3	147	theme	preparatory	437:447	arg1	steps					449:453	the preparatory steps	433:453	the preparatory steps	433:453	To minimize variability associated with the preparatory steps, the analysis was performed without enrichment of glycopeptides or fractionation of serum besides the nanoRP chromatography.
29427759	0	148	theme	proteins	52:59	arg1	fucosylation					30:41	core fucosylation	25:41	core fucosylation of serum proteins in liver diseases	25:77	Quantitative analysis of core fucosylation of serum proteins in liver diseases by LC-MS-MRM.
29427759	5	149	theme	additional	1113:1122	arg1	glycopeptides					1126:1138	additional 6 glycopeptides	1113:1138	additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican)	1113:1293	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	5	150	theme	glycopeptides	1126:1138	arg1	stage					930:934	the stage	926:934	the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin)	926:1098	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	5	150	theme	glycopeptides	1126:1138	arg1	increase					1101:1108	increase	1101:1108	increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican)	1101:1293	We find increased core fucosylation of 5 glycopeptides at the stage of liver fibrosis (i.e., N630 of serotransferrin, N107 of alpha-1-antitrypsin, N253 of plasma protease C1 inhibitor, N397 of ceruloplasmin, and N86 of vitronectin), increase of additional 6 glycopeptides at the stage of cirrhosis (i.e., N138 and N762 of ceruloplasmin, N354 of clusterin, N187 of hemopexin, N71 of immunoglobulin J chain, and N127 of lumican), while the degree of core fucosylation of 10 glycopeptides did not change.
29427759	7	151	theme	N-glycoproteins	1748:1762	arg1	quantity					1736:1743	the quantity	1732:1743	the quantity of N-glycoproteins	1732:1762	Our results demonstrate that the changes in core fucosylation are protein and site specific during the progression of fibrotic liver disease and independent of the changes in the quantity of N-glycoproteins.
29427759	12	152	theme	alternative	2483:2493	arg1	assay					2505:2509	an alternative serologic assay	2480:2509	an alternative serologic assay for the evaluation of fibrotic liver disease	2480:2554	Altered core fucosylation of N-glycopeptides might be used as an alternative serologic assay for the evaluation of fibrotic liver disease.
29427759	12	152	theme	alternative	2483:2493	arg1	fucosylation					2431:2442	Altered core fucosylation	2418:2442	Altered core fucosylation of N-glycopeptides	2418:2461	Altered core fucosylation of N-glycopeptides might be used as an alternative serologic assay for the evaluation of fibrotic liver disease.
29427759	0	153	gly	fucosylation	30:41	arg1	diseases					70:77	liver diseases	64:77	liver diseases	64:77	Quantitative analysis of core fucosylation of serum proteins in liver diseases by LC-MS-MRM.
29427759	0	153	gly	fucosylation	30:41	arg1	proteins					52:59	serum proteins	46:59	serum proteins	46:59	Quantitative analysis of core fucosylation of serum proteins in liver diseases by LC-MS-MRM.
29427759	4	154	theme	core	608:611	arg1	fucosylation					613:624	core fucosylation	608:624	core fucosylation of 22 N-glycopeptides derived from 17 proteins together with protein abundance of these glycoproteins in a cohort of 45 participants (15 disease-free control, 15 fibrosis and 15 cirrhosis patients)	608:822	Specifically, we quantified core fucosylation of 22 N-glycopeptides derived from 17 proteins together with protein abundance of these glycoproteins in a cohort of 45 participants (15 disease-free control, 15 fibrosis and 15 cirrhosis patients) using a multiplex nanoUPLC-MS-MRM workflow.
29427759	4	155	attach	derived	648:654	arg1	proteins					664:671	17 proteins	661:671	17 proteins together with protein abundance of these glycoproteins in a cohort of 45 participants (15 disease-free control, 15 fibrosis and 15 cirrhosis patients)	661:822	Specifically, we quantified core fucosylation of 22 N-glycopeptides derived from 17 proteins together with protein abundance of these glycoproteins in a cohort of 45 participants (15 disease-free control, 15 fibrosis and 15 cirrhosis patients) using a multiplex nanoUPLC-MS-MRM workflow.
29427759	4	155	attach	derived	648:654	arg2	N-glycopeptides					632:646	22 N-glycopeptides	629:646	22 N-glycopeptides derived from 17 proteins together with protein abundance of these glycoproteins in a cohort of 45 participants (15 disease-free control, 15 fibrosis and 15 cirrhosis patients)	629:822	Specifically, we quantified core fucosylation of 22 N-glycopeptides derived from 17 proteins together with protein abundance of these glycoproteins in a cohort of 45 participants (15 disease-free control, 15 fibrosis and 15 cirrhosis patients) using a multiplex nanoUPLC-MS-MRM workflow.
29427759	11	156	located	observed	2359:2366	arg1	N-glycopeptides					2381:2395	different N-glycopeptides	2371:2395	different N-glycopeptides of the same protein	2371:2415	Moreover, increased and decreased fucosylation was observed on different N-glycopeptides of the same protein.
29427759	11	156	located	observed	2359:2366	arg2	fucosylation					2342:2353	increased and decreased fucosylation	2318:2353	increased and decreased fucosylation	2318:2353	Moreover, increased and decreased fucosylation was observed on different N-glycopeptides of the same protein.
29427759	7	157	theme	changes	1721:1727	arg1	independent					1702:1712	independent	1702:1712	independent	1702:1712	Our results demonstrate that the changes in core fucosylation are protein and site specific during the progression of fibrotic liver disease and independent of the changes in the quantity of N-glycoproteins.
29427759	3	158	theme	glycopeptides	505:517	arg1	enrichment					491:500	enrichment	491:500	enrichment of glycopeptides or fractionation of serum besides the nanoRP chromatography	491:577	To minimize variability associated with the preparatory steps, the analysis was performed without enrichment of glycopeptides or fractionation of serum besides the nanoRP chromatography.
29427759	9	159	dep	SIGNIFICANCE	1946:1957	arg1	quantified					1968:1977	quantified	1968:1977	have quantified the difference in core fucosylation among three comparison groups (healthy control, fibrosis and cirrhosis patients) using a sensitive and selective LC-MS-MRM method	1963:2143	BIOLOGICAL SIGNIFICANCE: We have quantified the difference in core fucosylation among three comparison groups (healthy control, fibrosis and cirrhosis patients) using a sensitive and selective LC-MS-MRM method.
19193796	2	0	theme	factors	326:332	arg1	binding					292:298	The binding	288:298	The binding of cellular transcription factors to specific regulatory sites in the 5' LTR	288:375	The binding of cellular transcription factors to specific regulatory sites in the 5' LTR is a key event in the replication cycle of HIV-1.
19193796	2	0	theme	factors	326:332	arg1	event					386:390	a key event	380:390	a key event in the replication cycle of HIV-1	380:424	The binding of cellular transcription factors to specific regulatory sites in the 5' LTR is a key event in the replication cycle of HIV-1.
19193796	1	1	theme	proviral	248:255	arg1	repeat					274:279	long terminal repeat	260:279	the proviral 5' long terminal repeat (LTR)	244:285	Human immunodeficiency virus type 1 (HIV-1) gene expression and replication are regulated by the promoter/enhancer located in the U3 region of the proviral 5' long terminal repeat (LTR).
19193796	1	1	theme	proviral	248:255	arg1	LTR					282:284	LTR	282:284	LTR	282:284	Human immunodeficiency virus type 1 (HIV-1) gene expression and replication are regulated by the promoter/enhancer located in the U3 region of the proviral 5' long terminal repeat (LTR).
19193796	3	2	theme	transcription	512:524	arg1	factors					526:532	transcription factors	512:532	transcription factors	512:532	Since transcriptional activity is regulated by the posttranslational modification of transcription factors with the monosaccharide O-linked N-acetyl-D-glucosamine (O-GlcNAc), we evaluated whether increased O-GlcNAcylation affects HIV-1 transcription.
19193796	5	3	theme	known	932:936	arg1	enzyme					938:943	the sole known enzyme	923:943	the sole known enzyme catalyzing the addition of O-GlcNAc to proteins	923:991	Overexpression of O-GlcNAc transferase (OGT), the sole known enzyme catalyzing the addition of O-GlcNAc to proteins, specifically inhibited the activity of the HIV-1 LTR promoter in different T-cell lines and in primary CD4(+) T lymphocytes.
19193796	5	3	theme	known	932:936	arg1	transferase					904:914	O-GlcNAc transferase	895:914	O-GlcNAc transferase (OGT)	895:920	Overexpression of O-GlcNAc transferase (OGT), the sole known enzyme catalyzing the addition of O-GlcNAc to proteins, specifically inhibited the activity of the HIV-1 LTR promoter in different T-cell lines and in primary CD4(+) T lymphocytes.
19193796	9	4	theme	viral	1625:1629	arg1	replication					1631:1641	viral replication	1625:1641	viral replication	1625:1641	Modulation of Sp1 O-GlcNAcylation may play a role in the regulation of HIV-1 latency and activation and links viral replication to the glucose metabolism of the host cell.
19193796	0	5	link	O-linked	0:7	arg1	N-acetylglucosaminylation					9:33	O-linked N-acetylglucosaminylation	0:33	O-linked N-acetylglucosaminylation of Sp1	0:40	O-linked N-acetylglucosaminylation of Sp1 inhibits the human immunodeficiency virus type 1 promoter.
19193796	7	6	theme	inhibitory	1390:1399	arg1	effect					1401:1406	this inhibitory effect	1385:1406	this inhibitory effect	1385:1406	O-GlcNAcylation of the transcription factor Sp1 and the presence of Sp1-binding sites in the LTR were found to be crucial for this inhibitory effect.
19193796	5	7	theme	transferase	904:914	arg1	Overexpression					877:890	Overexpression	877:890	Overexpression of O-GlcNAc transferase (OGT), the sole known enzyme catalyzing the addition of O-GlcNAc to proteins,	877:992	Overexpression of O-GlcNAc transferase (OGT), the sole known enzyme catalyzing the addition of O-GlcNAc to proteins, specifically inhibited the activity of the HIV-1 LTR promoter in different T-cell lines and in primary CD4(+) T lymphocytes.
19193796	6	8	theme	infected	1155:1162	arg1	cells					1166:1170	infected T cells	1155:1170	infected T cells	1155:1170	Inhibition of HIV-1 LTR activity in infected T cells was most efficient (>95%) when OGT was recombinantly overexpressed prior to infection.
19193796	3	9	theme	monosaccharide	543:556	arg1	O-GlcNAc					591:598	O-GlcNAc	591:598	O-GlcNAc	591:598	Since transcriptional activity is regulated by the posttranslational modification of transcription factors with the monosaccharide O-linked N-acetyl-D-glucosamine (O-GlcNAc), we evaluated whether increased O-GlcNAcylation affects HIV-1 transcription.
19193796	3	9	theme	monosaccharide	543:556	arg1	N-acetyl-D-glucosamine					567:588	the monosaccharide O-linked N-acetyl-D-glucosamine	539:588	the monosaccharide O-linked N-acetyl-D-glucosamine (O-GlcNAc)	539:599	Since transcriptional activity is regulated by the posttranslational modification of transcription factors with the monosaccharide O-linked N-acetyl-D-glucosamine (O-GlcNAc), we evaluated whether increased O-GlcNAcylation affects HIV-1 transcription.
19193796	9	10	theme	glucose	1650:1656	arg1	metabolism					1658:1667	the glucose metabolism	1646:1667	the glucose metabolism of the host cell	1646:1684	Modulation of Sp1 O-GlcNAcylation may play a role in the regulation of HIV-1 latency and activation and links viral replication to the glucose metabolism of the host cell.
19193796	6	11	theme	activity	1143:1150	arg1	Inhibition					1119:1128	Inhibition	1119:1128	Inhibition of HIV-1 LTR activity in infected T cells	1119:1170	Inhibition of HIV-1 LTR activity in infected T cells was most efficient (>95%) when OGT was recombinantly overexpressed prior to infection.
19193796	9	12	theme	O-GlcNAcylation	1533:1547	arg1	Modulation					1515:1524	Modulation	1515:1524	Modulation of Sp1 O-GlcNAcylation	1515:1547	Modulation of Sp1 O-GlcNAcylation may play a role in the regulation of HIV-1 latency and activation and links viral replication to the glucose metabolism of the host cell.
19193796	5	13	theme	CD4	1097:1099	arg1	lymphocytes					1106:1116	primary CD4(+) T lymphocytes	1089:1116	primary CD4(+) T lymphocytes	1089:1116	Overexpression of O-GlcNAc transferase (OGT), the sole known enzyme catalyzing the addition of O-GlcNAc to proteins, specifically inhibited the activity of the HIV-1 LTR promoter in different T-cell lines and in primary CD4(+) T lymphocytes.
19193796	1	14	from	located	216:222	arg1	region					234:239	the U3 region	227:239	the U3 region of the proviral 5' long terminal repeat (LTR)	227:285	Human immunodeficiency virus type 1 (HIV-1) gene expression and replication are regulated by the promoter/enhancer located in the U3 region of the proviral 5' long terminal repeat (LTR).
19193796	9	15	theme	host	1676:1679	arg1	cell					1681:1684	the host cell	1672:1684	the host cell	1672:1684	Modulation of Sp1 O-GlcNAcylation may play a role in the regulation of HIV-1 latency and activation and links viral replication to the glucose metabolism of the host cell.
19193796	5	16	theme	different	1059:1067	arg1	lines					1076:1080	different T-cell lines	1059:1080	different T-cell lines	1059:1080	Overexpression of O-GlcNAc transferase (OGT), the sole known enzyme catalyzing the addition of O-GlcNAc to proteins, specifically inhibited the activity of the HIV-1 LTR promoter in different T-cell lines and in primary CD4(+) T lymphocytes.
19193796	5	17	theme	O-GlcNAc	972:979	arg1	addition					960:967	the addition	956:967	the addition of O-GlcNAc to proteins	956:991	Overexpression of O-GlcNAc transferase (OGT), the sole known enzyme catalyzing the addition of O-GlcNAc to proteins, specifically inhibited the activity of the HIV-1 LTR promoter in different T-cell lines and in primary CD4(+) T lymphocytes.
19193796	7	18	theme	Sp1-binding	1327:1337	arg1	sites					1339:1343	Sp1-binding sites	1327:1343	Sp1-binding sites	1327:1343	O-GlcNAcylation of the transcription factor Sp1 and the presence of Sp1-binding sites in the LTR were found to be crucial for this inhibitory effect.
19193796	4	19	theme	present	685:691	arg1	study					693:697	the present study	681:697	the present study	681:697	In the present study we demonstrate that treatment of HIV-1-infected lymphocytes with the O-GlcNAcylation-enhancing agent glucosamine (GlcN) repressed viral transcription in a dose-dependent manner.
19193796	0	20	theme	virus	78:82	arg1	type					84:87	human immunodeficiency virus type 1	55:89	the human immunodeficiency virus type 1 promoter	51:98	O-linked N-acetylglucosaminylation of Sp1 inhibits the human immunodeficiency virus type 1 promoter.
19193796	10	21	theme	antiretroviral	1772:1785	arg1	therapies					1787:1795	antiretroviral therapies	1772:1795	antiretroviral therapies against AIDS	1772:1808	Hence, the establishment of a metabolic treatment might supplement the repertoire of antiretroviral therapies against AIDS.
19193796	1	22	theme	gene	145:148	arg1	expression					150:159	Human immunodeficiency virus type 1 (HIV-1) gene expression	101:159	Human immunodeficiency virus type 1 (HIV-1) gene expression	101:159	Human immunodeficiency virus type 1 (HIV-1) gene expression and replication are regulated by the promoter/enhancer located in the U3 region of the proviral 5' long terminal repeat (LTR).
19193796	8	23	theme	Sp1	1462:1464	arg1	O-GlcNAcylation					1443:1457	O-GlcNAcylation	1443:1457	O-GlcNAcylation of Sp1	1443:1464	From this study, we conclude that O-GlcNAcylation of Sp1 inhibits the activity of the HIV-1 LTR promoter.
19193796	5	24	theme	sole	927:930	arg1	enzyme					938:943	the sole known enzyme	923:943	the sole known enzyme catalyzing the addition of O-GlcNAc to proteins	923:991	Overexpression of O-GlcNAc transferase (OGT), the sole known enzyme catalyzing the addition of O-GlcNAc to proteins, specifically inhibited the activity of the HIV-1 LTR promoter in different T-cell lines and in primary CD4(+) T lymphocytes.
19193796	5	24	theme	sole	927:930	arg1	transferase					904:914	O-GlcNAc transferase	895:914	O-GlcNAc transferase (OGT)	895:920	Overexpression of O-GlcNAc transferase (OGT), the sole known enzyme catalyzing the addition of O-GlcNAc to proteins, specifically inhibited the activity of the HIV-1 LTR promoter in different T-cell lines and in primary CD4(+) T lymphocytes.
19193796	4	25	theme	agent	794:798	arg1	GlcN					813:816	GlcN	813:816	GlcN	813:816	In the present study we demonstrate that treatment of HIV-1-infected lymphocytes with the O-GlcNAcylation-enhancing agent glucosamine (GlcN) repressed viral transcription in a dose-dependent manner.
19193796	4	25	theme	agent	794:798	arg1	glucosamine					800:810	the O-GlcNAcylation-enhancing agent glucosamine	764:810	the O-GlcNAcylation-enhancing agent glucosamine (GlcN)	764:817	In the present study we demonstrate that treatment of HIV-1-infected lymphocytes with the O-GlcNAcylation-enhancing agent glucosamine (GlcN) repressed viral transcription in a dose-dependent manner.
19193796	5	26	theme	T	1104:1104	arg1	lymphocytes					1106:1116	primary CD4(+) T lymphocytes	1089:1116	primary CD4(+) T lymphocytes	1089:1116	Overexpression of O-GlcNAc transferase (OGT), the sole known enzyme catalyzing the addition of O-GlcNAc to proteins, specifically inhibited the activity of the HIV-1 LTR promoter in different T-cell lines and in primary CD4(+) T lymphocytes.
19193796	2	27	theme	HIV-1	420:424	arg1	cycle					411:415	the replication cycle	395:415	the replication cycle of HIV-1	395:424	The binding of cellular transcription factors to specific regulatory sites in the 5' LTR is a key event in the replication cycle of HIV-1.
19193796	8	28	theme	HIV-1	1495:1499	arg1	promoter					1505:1512	the HIV-1 LTR promoter	1491:1512	the HIV-1 LTR promoter	1491:1512	From this study, we conclude that O-GlcNAcylation of Sp1 inhibits the activity of the HIV-1 LTR promoter.
19193796	4	29	theme	lymphocytes	747:757	arg1	treatment					719:727	treatment	719:727	treatment of HIV-1-infected lymphocytes with the O-GlcNAcylation-enhancing agent glucosamine (GlcN)	719:817	In the present study we demonstrate that treatment of HIV-1-infected lymphocytes with the O-GlcNAcylation-enhancing agent glucosamine (GlcN) repressed viral transcription in a dose-dependent manner.
19193796	9	30	attach	links	1619:1623	arg1	metabolism					1658:1667	the glucose metabolism	1646:1667	the glucose metabolism of the host cell	1646:1684	Modulation of Sp1 O-GlcNAcylation may play a role in the regulation of HIV-1 latency and activation and links viral replication to the glucose metabolism of the host cell.
19193796	9	30	attach	links	1619:1623	arg2	Modulation					1515:1524	Modulation	1515:1524	Modulation of Sp1 O-GlcNAcylation	1515:1547	Modulation of Sp1 O-GlcNAcylation may play a role in the regulation of HIV-1 latency and activation and links viral replication to the glucose metabolism of the host cell.
19193796	0	31	theme	O-linked	0:7	arg1	N-acetylglucosaminylation					9:33	O-linked N-acetylglucosaminylation	0:33	O-linked N-acetylglucosaminylation of Sp1	0:40	O-linked N-acetylglucosaminylation of Sp1 inhibits the human immunodeficiency virus type 1 promoter.
19193796	1	32	theme	long	260:263	arg1	repeat					274:279	long terminal repeat	260:279	the proviral 5' long terminal repeat (LTR)	244:285	Human immunodeficiency virus type 1 (HIV-1) gene expression and replication are regulated by the promoter/enhancer located in the U3 region of the proviral 5' long terminal repeat (LTR).
19193796	1	32	theme	long	260:263	arg1	LTR					282:284	LTR	282:284	LTR	282:284	Human immunodeficiency virus type 1 (HIV-1) gene expression and replication are regulated by the promoter/enhancer located in the U3 region of the proviral 5' long terminal repeat (LTR).
19193796	1	33	theme	Human	101:105	arg1	type					130:133	Human immunodeficiency virus type 1	101:135	Human immunodeficiency virus type 1 (HIV-1) gene expression	101:159	Human immunodeficiency virus type 1 (HIV-1) gene expression and replication are regulated by the promoter/enhancer located in the U3 region of the proviral 5' long terminal repeat (LTR).
19193796	1	33	theme	Human	101:105	arg1	HIV-1					138:142	HIV-1	138:142	HIV-1	138:142	Human immunodeficiency virus type 1 (HIV-1) gene expression and replication are regulated by the promoter/enhancer located in the U3 region of the proviral 5' long terminal repeat (LTR).
19193796	7	34	from	LTR	1352:1354	arg1	O-GlcNAcylation					1259:1273	O-GlcNAcylation	1259:1273	O-GlcNAcylation of the transcription factor Sp1 and the presence of Sp1-binding sites in the LTR	1259:1354	O-GlcNAcylation of the transcription factor Sp1 and the presence of Sp1-binding sites in the LTR were found to be crucial for this inhibitory effect.
19193796	8	35	theme	promoter	1505:1512	arg1	activity					1479:1486	the activity	1475:1486	the activity of the HIV-1 LTR promoter	1475:1512	From this study, we conclude that O-GlcNAcylation of Sp1 inhibits the activity of the HIV-1 LTR promoter.
19193796	1	36	theme	repeat	274:279	arg1	region					234:239	the U3 region	227:239	the U3 region of the proviral 5' long terminal repeat (LTR)	227:285	Human immunodeficiency virus type 1 (HIV-1) gene expression and replication are regulated by the promoter/enhancer located in the U3 region of the proviral 5' long terminal repeat (LTR).
19193796	1	37	theme	virus	124:128	arg1	type					130:133	Human immunodeficiency virus type 1	101:135	Human immunodeficiency virus type 1 (HIV-1) gene expression	101:159	Human immunodeficiency virus type 1 (HIV-1) gene expression and replication are regulated by the promoter/enhancer located in the U3 region of the proviral 5' long terminal repeat (LTR).
19193796	1	37	theme	virus	124:128	arg1	HIV-1					138:142	HIV-1	138:142	HIV-1	138:142	Human immunodeficiency virus type 1 (HIV-1) gene expression and replication are regulated by the promoter/enhancer located in the U3 region of the proviral 5' long terminal repeat (LTR).
19193796	7	38	theme	Sp1	1303:1305	arg1	O-GlcNAcylation					1259:1273	O-GlcNAcylation	1259:1273	O-GlcNAcylation of the transcription factor Sp1 and the presence of Sp1-binding sites in the LTR	1259:1354	O-GlcNAcylation of the transcription factor Sp1 and the presence of Sp1-binding sites in the LTR were found to be crucial for this inhibitory effect.
19193796	3	39	link	O-linked	558:565	arg1	O-GlcNAc					591:598	O-GlcNAc	591:598	O-GlcNAc	591:598	Since transcriptional activity is regulated by the posttranslational modification of transcription factors with the monosaccharide O-linked N-acetyl-D-glucosamine (O-GlcNAc), we evaluated whether increased O-GlcNAcylation affects HIV-1 transcription.
19193796	3	39	link	O-linked	558:565	arg1	N-acetyl-D-glucosamine					567:588	the monosaccharide O-linked N-acetyl-D-glucosamine	539:588	the monosaccharide O-linked N-acetyl-D-glucosamine (O-GlcNAc)	539:599	Since transcriptional activity is regulated by the posttranslational modification of transcription factors with the monosaccharide O-linked N-acetyl-D-glucosamine (O-GlcNAc), we evaluated whether increased O-GlcNAcylation affects HIV-1 transcription.
19193796	3	40	with	modification	496:507	arg1	O-GlcNAc					591:598	O-GlcNAc	591:598	O-GlcNAc	591:598	Since transcriptional activity is regulated by the posttranslational modification of transcription factors with the monosaccharide O-linked N-acetyl-D-glucosamine (O-GlcNAc), we evaluated whether increased O-GlcNAcylation affects HIV-1 transcription.
19193796	3	40	with	modification	496:507	arg1	N-acetyl-D-glucosamine					567:588	the monosaccharide O-linked N-acetyl-D-glucosamine	539:588	the monosaccharide O-linked N-acetyl-D-glucosamine (O-GlcNAc)	539:599	Since transcriptional activity is regulated by the posttranslational modification of transcription factors with the monosaccharide O-linked N-acetyl-D-glucosamine (O-GlcNAc), we evaluated whether increased O-GlcNAcylation affects HIV-1 transcription.
19193796	5	41	theme	LTR	1043:1045	arg1	promoter					1047:1054	the HIV-1 LTR promoter	1033:1054	the HIV-1 LTR promoter	1033:1054	Overexpression of O-GlcNAc transferase (OGT), the sole known enzyme catalyzing the addition of O-GlcNAc to proteins, specifically inhibited the activity of the HIV-1 LTR promoter in different T-cell lines and in primary CD4(+) T lymphocytes.
19193796	7	42	theme	transcription	1282:1294	arg1	Sp1					1303:1305	the transcription factor Sp1	1278:1305	the transcription factor Sp1	1278:1305	O-GlcNAcylation of the transcription factor Sp1 and the presence of Sp1-binding sites in the LTR were found to be crucial for this inhibitory effect.
19193796	3	43	theme	increased	623:631	arg1	O-GlcNAcylation					633:647	increased O-GlcNAcylation	623:647	increased O-GlcNAcylation	623:647	Since transcriptional activity is regulated by the posttranslational modification of transcription factors with the monosaccharide O-linked N-acetyl-D-glucosamine (O-GlcNAc), we evaluated whether increased O-GlcNAcylation affects HIV-1 transcription.
19193796	4	44	theme	dose-dependent	854:867	arg1	manner					869:874	a dose-dependent manner	852:874	a dose-dependent manner	852:874	In the present study we demonstrate that treatment of HIV-1-infected lymphocytes with the O-GlcNAcylation-enhancing agent glucosamine (GlcN) repressed viral transcription in a dose-dependent manner.
19193796	3	45	theme	transcriptional	433:447	arg1	activity					449:456	transcriptional activity	433:456	transcriptional activity	433:456	Since transcriptional activity is regulated by the posttranslational modification of transcription factors with the monosaccharide O-linked N-acetyl-D-glucosamine (O-GlcNAc), we evaluated whether increased O-GlcNAcylation affects HIV-1 transcription.
19193796	0	46	theme	human	55:59	arg1	type					84:87	human immunodeficiency virus type 1	55:89	the human immunodeficiency virus type 1 promoter	51:98	O-linked N-acetylglucosaminylation of Sp1 inhibits the human immunodeficiency virus type 1 promoter.
19193796	7	47	attach	presence	1315:1322	arg1	LTR					1352:1354	the LTR	1348:1354	the LTR	1348:1354	O-GlcNAcylation of the transcription factor Sp1 and the presence of Sp1-binding sites in the LTR were found to be crucial for this inhibitory effect.
19193796	7	47	attach	presence	1315:1322	arg2	sites					1339:1343	Sp1-binding sites	1327:1343	Sp1-binding sites	1327:1343	O-GlcNAcylation of the transcription factor Sp1 and the presence of Sp1-binding sites in the LTR were found to be crucial for this inhibitory effect.
19193796	4	48	theme	viral	829:833	arg1	transcription					835:847	viral transcription	829:847	viral transcription	829:847	In the present study we demonstrate that treatment of HIV-1-infected lymphocytes with the O-GlcNAcylation-enhancing agent glucosamine (GlcN) repressed viral transcription in a dose-dependent manner.
19193796	2	49	theme	regulatory	346:355	arg1	sites					357:361	specific regulatory sites	337:361	specific regulatory sites in the 5' LTR	337:375	The binding of cellular transcription factors to specific regulatory sites in the 5' LTR is a key event in the replication cycle of HIV-1.
19193796	9	50	theme	latency	1592:1598	arg1	regulation					1572:1581	the regulation	1568:1581	the regulation of HIV-1 latency and activation	1568:1613	Modulation of Sp1 O-GlcNAcylation may play a role in the regulation of HIV-1 latency and activation and links viral replication to the glucose metabolism of the host cell.
19193796	7	51	from	presence	1315:1322	arg1	LTR					1352:1354	the LTR	1348:1354	the LTR	1348:1354	O-GlcNAcylation of the transcription factor Sp1 and the presence of Sp1-binding sites in the LTR were found to be crucial for this inhibitory effect.
19193796	4	52	with	treatment	719:727	arg1	GlcN					813:816	GlcN	813:816	GlcN	813:816	In the present study we demonstrate that treatment of HIV-1-infected lymphocytes with the O-GlcNAcylation-enhancing agent glucosamine (GlcN) repressed viral transcription in a dose-dependent manner.
19193796	4	52	with	treatment	719:727	arg1	glucosamine					800:810	the O-GlcNAcylation-enhancing agent glucosamine	764:810	the O-GlcNAcylation-enhancing agent glucosamine (GlcN)	764:817	In the present study we demonstrate that treatment of HIV-1-infected lymphocytes with the O-GlcNAcylation-enhancing agent glucosamine (GlcN) repressed viral transcription in a dose-dependent manner.
19193796	9	53	theme	activation	1604:1613	arg1	regulation					1572:1581	the regulation	1568:1581	the regulation of HIV-1 latency and activation	1568:1613	Modulation of Sp1 O-GlcNAcylation may play a role in the regulation of HIV-1 latency and activation and links viral replication to the glucose metabolism of the host cell.
19193796	2	54	theme	transcription	312:324	arg1	factors					326:332	cellular transcription factors	303:332	cellular transcription factors	303:332	The binding of cellular transcription factors to specific regulatory sites in the 5' LTR is a key event in the replication cycle of HIV-1.
19193796	3	55	theme	posttranslational	478:494	arg1	modification					496:507	the posttranslational modification	474:507	the posttranslational modification of transcription factors with the monosaccharide O-linked N-acetyl-D-glucosamine (O-GlcNAc)	474:599	Since transcriptional activity is regulated by the posttranslational modification of transcription factors with the monosaccharide O-linked N-acetyl-D-glucosamine (O-GlcNAc), we evaluated whether increased O-GlcNAcylation affects HIV-1 transcription.
19193796	5	56	theme	O-GlcNAc	895:902	arg1	transferase					904:914	O-GlcNAc transferase	895:914	O-GlcNAc transferase (OGT)	895:920	Overexpression of O-GlcNAc transferase (OGT), the sole known enzyme catalyzing the addition of O-GlcNAc to proteins, specifically inhibited the activity of the HIV-1 LTR promoter in different T-cell lines and in primary CD4(+) T lymphocytes.
19193796	5	56	theme	O-GlcNAc	895:902	arg1	enzyme					938:943	the sole known enzyme	923:943	the sole known enzyme catalyzing the addition of O-GlcNAc to proteins	923:991	Overexpression of O-GlcNAc transferase (OGT), the sole known enzyme catalyzing the addition of O-GlcNAc to proteins, specifically inhibited the activity of the HIV-1 LTR promoter in different T-cell lines and in primary CD4(+) T lymphocytes.
19193796	5	56	theme	O-GlcNAc	895:902	arg1	OGT					917:919	OGT	917:919	OGT	917:919	Overexpression of O-GlcNAc transferase (OGT), the sole known enzyme catalyzing the addition of O-GlcNAc to proteins, specifically inhibited the activity of the HIV-1 LTR promoter in different T-cell lines and in primary CD4(+) T lymphocytes.
19193796	6	57	theme	T	1164:1164	arg1	cells					1166:1170	infected T cells	1155:1170	infected T cells	1155:1170	Inhibition of HIV-1 LTR activity in infected T cells was most efficient (>95%) when OGT was recombinantly overexpressed prior to infection.
19193796	5	58	from	activity	1021:1028	arg1	lines					1076:1080	different T-cell lines	1059:1080	different T-cell lines	1059:1080	Overexpression of O-GlcNAc transferase (OGT), the sole known enzyme catalyzing the addition of O-GlcNAc to proteins, specifically inhibited the activity of the HIV-1 LTR promoter in different T-cell lines and in primary CD4(+) T lymphocytes.
19193796	5	58	from	activity	1021:1028	arg1	lymphocytes					1106:1116	primary CD4(+) T lymphocytes	1089:1116	primary CD4(+) T lymphocytes	1089:1116	Overexpression of O-GlcNAc transferase (OGT), the sole known enzyme catalyzing the addition of O-GlcNAc to proteins, specifically inhibited the activity of the HIV-1 LTR promoter in different T-cell lines and in primary CD4(+) T lymphocytes.
19193796	7	59	from	O-GlcNAcylation	1259:1273	arg1	LTR					1352:1354	the LTR	1348:1354	the LTR	1348:1354	O-GlcNAcylation of the transcription factor Sp1 and the presence of Sp1-binding sites in the LTR were found to be crucial for this inhibitory effect.
19193796	3	60	theme	factors	526:532	arg1	modification					496:507	the posttranslational modification	474:507	the posttranslational modification of transcription factors with the monosaccharide O-linked N-acetyl-D-glucosamine (O-GlcNAc)	474:599	Since transcriptional activity is regulated by the posttranslational modification of transcription factors with the monosaccharide O-linked N-acetyl-D-glucosamine (O-GlcNAc), we evaluated whether increased O-GlcNAcylation affects HIV-1 transcription.
19193796	10	61	theme	treatment	1727:1735	arg1	establishment					1698:1710	the establishment	1694:1710	the establishment of a metabolic treatment	1694:1735	Hence, the establishment of a metabolic treatment might supplement the repertoire of antiretroviral therapies against AIDS.
19193796	6	62	theme	LTR	1139:1141	arg1	activity					1143:1150	HIV-1 LTR activity	1133:1150	HIV-1 LTR activity	1133:1150	Inhibition of HIV-1 LTR activity in infected T cells was most efficient (>95%) when OGT was recombinantly overexpressed prior to infection.
19193796	5	63	theme	primary	1089:1095	arg1	CD4					1097:1099	primary CD4	1089:1099	primary CD4	1089:1099	Overexpression of O-GlcNAc transferase (OGT), the sole known enzyme catalyzing the addition of O-GlcNAc to proteins, specifically inhibited the activity of the HIV-1 LTR promoter in different T-cell lines and in primary CD4(+) T lymphocytes.
19193796	1	64	theme	located	216:222	arg1	promoter/enhancer					198:214	the promoter/enhancer	194:214	the promoter/enhancer located in the U3 region of the proviral 5' long terminal repeat (LTR)	194:285	Human immunodeficiency virus type 1 (HIV-1) gene expression and replication are regulated by the promoter/enhancer located in the U3 region of the proviral 5' long terminal repeat (LTR).
19193796	1	65	from	region	234:239	arg1	located					216:222	located	216:222	located	216:222	Human immunodeficiency virus type 1 (HIV-1) gene expression and replication are regulated by the promoter/enhancer located in the U3 region of the proviral 5' long terminal repeat (LTR).
19193796	3	66	theme	O-linked	558:565	arg1	O-GlcNAc					591:598	O-GlcNAc	591:598	O-GlcNAc	591:598	Since transcriptional activity is regulated by the posttranslational modification of transcription factors with the monosaccharide O-linked N-acetyl-D-glucosamine (O-GlcNAc), we evaluated whether increased O-GlcNAcylation affects HIV-1 transcription.
19193796	3	66	theme	O-linked	558:565	arg1	N-acetyl-D-glucosamine					567:588	the monosaccharide O-linked N-acetyl-D-glucosamine	539:588	the monosaccharide O-linked N-acetyl-D-glucosamine (O-GlcNAc)	539:599	Since transcriptional activity is regulated by the posttranslational modification of transcription factors with the monosaccharide O-linked N-acetyl-D-glucosamine (O-GlcNAc), we evaluated whether increased O-GlcNAcylation affects HIV-1 transcription.
19193796	1	67	theme	type	130:133	arg1	expression					150:159	Human immunodeficiency virus type 1 (HIV-1) gene expression	101:159	Human immunodeficiency virus type 1 (HIV-1) gene expression	101:159	Human immunodeficiency virus type 1 (HIV-1) gene expression and replication are regulated by the promoter/enhancer located in the U3 region of the proviral 5' long terminal repeat (LTR).
19193796	9	68	theme	cell	1681:1684	arg1	metabolism					1658:1667	the glucose metabolism	1646:1667	the glucose metabolism of the host cell	1646:1684	Modulation of Sp1 O-GlcNAcylation may play a role in the regulation of HIV-1 latency and activation and links viral replication to the glucose metabolism of the host cell.
19193796	6	69	dep	efficient	1181:1189	arg1	%					1195:1195	>95%	1192:1195	>95%	1192:1195	Inhibition of HIV-1 LTR activity in infected T cells was most efficient (>95%) when OGT was recombinantly overexpressed prior to infection.
19193796	5	70	theme	T-cell	1069:1074	arg1	lines					1076:1080	different T-cell lines	1059:1080	different T-cell lines	1059:1080	Overexpression of O-GlcNAc transferase (OGT), the sole known enzyme catalyzing the addition of O-GlcNAc to proteins, specifically inhibited the activity of the HIV-1 LTR promoter in different T-cell lines and in primary CD4(+) T lymphocytes.
19193796	10	71	theme	metabolic	1717:1725	arg1	treatment					1727:1735	a metabolic treatment	1715:1735	a metabolic treatment	1715:1735	Hence, the establishment of a metabolic treatment might supplement the repertoire of antiretroviral therapies against AIDS.
19193796	0	72	theme	type	84:87	arg1	promoter					91:98	the human immunodeficiency virus type 1 promoter	51:98	the human immunodeficiency virus type 1 promoter	51:98	O-linked N-acetylglucosaminylation of Sp1 inhibits the human immunodeficiency virus type 1 promoter.
19193796	10	73	theme	therapies	1787:1795	arg1	repertoire					1758:1767	the repertoire	1754:1767	the repertoire of antiretroviral therapies against AIDS	1754:1808	Hence, the establishment of a metabolic treatment might supplement the repertoire of antiretroviral therapies against AIDS.
19193796	10	73	theme	therapies	1787:1795	arg1	therapies					1787:1795	antiretroviral therapies	1772:1795	antiretroviral therapies against AIDS	1772:1808	Hence, the establishment of a metabolic treatment might supplement the repertoire of antiretroviral therapies against AIDS.
19193796	2	74	from	event	386:390	arg1	cycle					411:415	the replication cycle	395:415	the replication cycle of HIV-1	395:424	The binding of cellular transcription factors to specific regulatory sites in the 5' LTR is a key event in the replication cycle of HIV-1.
19193796	7	75	theme	sites	1339:1343	arg1	Sp1					1303:1305	the transcription factor Sp1	1278:1305	the transcription factor Sp1	1278:1305	O-GlcNAcylation of the transcription factor Sp1 and the presence of Sp1-binding sites in the LTR were found to be crucial for this inhibitory effect.
19193796	7	75	theme	sites	1339:1343	arg1	presence					1315:1322	the presence	1311:1322	the presence of Sp1-binding sites in the LTR	1311:1354	O-GlcNAcylation of the transcription factor Sp1 and the presence of Sp1-binding sites in the LTR were found to be crucial for this inhibitory effect.
19193796	4	76	theme	O-GlcNAcylation-enhancing	768:792	arg1	GlcN					813:816	GlcN	813:816	GlcN	813:816	In the present study we demonstrate that treatment of HIV-1-infected lymphocytes with the O-GlcNAcylation-enhancing agent glucosamine (GlcN) repressed viral transcription in a dose-dependent manner.
19193796	4	76	theme	O-GlcNAcylation-enhancing	768:792	arg1	glucosamine					800:810	the O-GlcNAcylation-enhancing agent glucosamine	764:810	the O-GlcNAcylation-enhancing agent glucosamine (GlcN)	764:817	In the present study we demonstrate that treatment of HIV-1-infected lymphocytes with the O-GlcNAcylation-enhancing agent glucosamine (GlcN) repressed viral transcription in a dose-dependent manner.
19193796	7	77	theme	presence	1315:1322	arg1	O-GlcNAcylation					1259:1273	O-GlcNAcylation	1259:1273	O-GlcNAcylation of the transcription factor Sp1 and the presence of Sp1-binding sites in the LTR	1259:1354	O-GlcNAcylation of the transcription factor Sp1 and the presence of Sp1-binding sites in the LTR were found to be crucial for this inhibitory effect.
19193796	8	78	theme	LTR	1501:1503	arg1	promoter					1505:1512	the HIV-1 LTR promoter	1491:1512	the HIV-1 LTR promoter	1491:1512	From this study, we conclude that O-GlcNAcylation of Sp1 inhibits the activity of the HIV-1 LTR promoter.
19193796	9	79	theme	Sp1	1529:1531	arg1	O-GlcNAcylation					1533:1547	Sp1 O-GlcNAcylation	1529:1547	Sp1 O-GlcNAcylation	1529:1547	Modulation of Sp1 O-GlcNAcylation may play a role in the regulation of HIV-1 latency and activation and links viral replication to the glucose metabolism of the host cell.
19193796	4	80	theme	HIV-1-infected	732:745	arg1	lymphocytes					747:757	HIV-1-infected lymphocytes	732:757	HIV-1-infected lymphocytes	732:757	In the present study we demonstrate that treatment of HIV-1-infected lymphocytes with the O-GlcNAcylation-enhancing agent glucosamine (GlcN) repressed viral transcription in a dose-dependent manner.
19193796	0	81	theme	Sp1	38:40	arg1	N-acetylglucosaminylation					9:33	O-linked N-acetylglucosaminylation	0:33	O-linked N-acetylglucosaminylation of Sp1	0:40	O-linked N-acetylglucosaminylation of Sp1 inhibits the human immunodeficiency virus type 1 promoter.
19193796	1	82	theme	terminal	265:272	arg1	repeat					274:279	long terminal repeat	260:279	the proviral 5' long terminal repeat (LTR)	244:285	Human immunodeficiency virus type 1 (HIV-1) gene expression and replication are regulated by the promoter/enhancer located in the U3 region of the proviral 5' long terminal repeat (LTR).
19193796	1	82	theme	terminal	265:272	arg1	LTR					282:284	LTR	282:284	LTR	282:284	Human immunodeficiency virus type 1 (HIV-1) gene expression and replication are regulated by the promoter/enhancer located in the U3 region of the proviral 5' long terminal repeat (LTR).
19193796	1	83	theme	immunodeficiency	107:122	arg1	type					130:133	Human immunodeficiency virus type 1	101:135	Human immunodeficiency virus type 1 (HIV-1) gene expression	101:159	Human immunodeficiency virus type 1 (HIV-1) gene expression and replication are regulated by the promoter/enhancer located in the U3 region of the proviral 5' long terminal repeat (LTR).
19193796	1	83	theme	immunodeficiency	107:122	arg1	HIV-1					138:142	HIV-1	138:142	HIV-1	138:142	Human immunodeficiency virus type 1 (HIV-1) gene expression and replication are regulated by the promoter/enhancer located in the U3 region of the proviral 5' long terminal repeat (LTR).
19193796	7	84	theme	factor	1296:1301	arg1	Sp1					1303:1305	the transcription factor Sp1	1278:1305	the transcription factor Sp1	1278:1305	O-GlcNAcylation of the transcription factor Sp1 and the presence of Sp1-binding sites in the LTR were found to be crucial for this inhibitory effect.
19193796	2	85	theme	key	382:384	arg1	binding					292:298	The binding	288:298	The binding of cellular transcription factors to specific regulatory sites in the 5' LTR	288:375	The binding of cellular transcription factors to specific regulatory sites in the 5' LTR is a key event in the replication cycle of HIV-1.
19193796	2	85	theme	key	382:384	arg1	event					386:390	a key event	380:390	a key event in the replication cycle of HIV-1	380:424	The binding of cellular transcription factors to specific regulatory sites in the 5' LTR is a key event in the replication cycle of HIV-1.
19193796	5	86	theme	HIV-1	1037:1041	arg1	promoter					1047:1054	the HIV-1 LTR promoter	1033:1054	the HIV-1 LTR promoter	1033:1054	Overexpression of O-GlcNAc transferase (OGT), the sole known enzyme catalyzing the addition of O-GlcNAc to proteins, specifically inhibited the activity of the HIV-1 LTR promoter in different T-cell lines and in primary CD4(+) T lymphocytes.
19193796	6	87	from	Inhibition	1119:1128	arg1	cells					1166:1170	infected T cells	1155:1170	infected T cells	1155:1170	Inhibition of HIV-1 LTR activity in infected T cells was most efficient (>95%) when OGT was recombinantly overexpressed prior to infection.
19193796	0	88	theme	immunodeficiency	61:76	arg1	type					84:87	human immunodeficiency virus type 1	55:89	the human immunodeficiency virus type 1 promoter	51:98	O-linked N-acetylglucosaminylation of Sp1 inhibits the human immunodeficiency virus type 1 promoter.
19193796	5	89	theme	promoter	1047:1054	arg1	activity					1021:1028	the activity	1017:1028	the activity of the HIV-1 LTR promoter in different T-cell lines and in primary CD4(+) T lymphocytes	1017:1116	Overexpression of O-GlcNAc transferase (OGT), the sole known enzyme catalyzing the addition of O-GlcNAc to proteins, specifically inhibited the activity of the HIV-1 LTR promoter in different T-cell lines and in primary CD4(+) T lymphocytes.
19193796	2	90	from	sites	357:361	arg1	LTR					373:375	the 5' LTR	366:375	the 5' LTR	366:375	The binding of cellular transcription factors to specific regulatory sites in the 5' LTR is a key event in the replication cycle of HIV-1.
19193796	6	91	theme	HIV-1	1133:1137	arg1	LTR					1139:1141	HIV-1 LTR	1133:1141	HIV-1 LTR activity	1133:1150	Inhibition of HIV-1 LTR activity in infected T cells was most efficient (>95%) when OGT was recombinantly overexpressed prior to infection.
19193796	2	92	theme	replication	399:409	arg1	cycle					411:415	the replication cycle	395:415	the replication cycle of HIV-1	395:424	The binding of cellular transcription factors to specific regulatory sites in the 5' LTR is a key event in the replication cycle of HIV-1.
19193796	2	93	theme	cellular	303:310	arg1	factors					326:332	cellular transcription factors	303:332	cellular transcription factors	303:332	The binding of cellular transcription factors to specific regulatory sites in the 5' LTR is a key event in the replication cycle of HIV-1.
19193796	7	94	from	Sp1	1303:1305	arg1	LTR					1352:1354	the LTR	1348:1354	the LTR	1348:1354	O-GlcNAcylation of the transcription factor Sp1 and the presence of Sp1-binding sites in the LTR were found to be crucial for this inhibitory effect.
19193796	3	95	theme	HIV-1	657:661	arg1	transcription					663:675	HIV-1 transcription	657:675	HIV-1 transcription	657:675	Since transcriptional activity is regulated by the posttranslational modification of transcription factors with the monosaccharide O-linked N-acetyl-D-glucosamine (O-GlcNAc), we evaluated whether increased O-GlcNAcylation affects HIV-1 transcription.
19193796	1	96	theme	U3	231:232	arg1	region					234:239	the U3 region	227:239	the U3 region of the proviral 5' long terminal repeat (LTR)	227:285	Human immunodeficiency virus type 1 (HIV-1) gene expression and replication are regulated by the promoter/enhancer located in the U3 region of the proviral 5' long terminal repeat (LTR).
19193796	9	97	theme	HIV-1	1586:1590	arg1	latency					1592:1598	HIV-1 latency	1586:1598	HIV-1 latency	1586:1598	Modulation of Sp1 O-GlcNAcylation may play a role in the regulation of HIV-1 latency and activation and links viral replication to the glucose metabolism of the host cell.
19193796	2	98	theme	specific	337:344	arg1	sites					357:361	specific regulatory sites	337:361	specific regulatory sites in the 5' LTR	337:375	The binding of cellular transcription factors to specific regulatory sites in the 5' LTR is a key event in the replication cycle of HIV-1.
26846330	2	0	theme	crystal	336:342	arg1	structure					344:352	the crystal structure	332:352	the crystal structure of glycosylated NPC1 luminal domain C	332:390	We have determined the crystal structure of glycosylated NPC1 luminal domain C and find all seven possible sites are glycosylated.
26846330	1	1	theme	domain	238:243	arg1	receptor					273:280	an essential endosomal receptor	250:280	an essential endosomal receptor for Ebola and Marburg viruses	250:310	Niemann-pick type C1 (NPC1) is an endo/lysosomal membrane protein involved in intracellular cholesterol trafficking, and its luminal domain C is an essential endosomal receptor for Ebola and Marburg viruses.
26846330	1	1	theme	domain	238:243	arg1	C					245:245	its luminal domain C	226:245	its luminal domain C	226:245	Niemann-pick type C1 (NPC1) is an endo/lysosomal membrane protein involved in intracellular cholesterol trafficking, and its luminal domain C is an essential endosomal receptor for Ebola and Marburg viruses.
26846330	0	2	theme	NPC2	70:73	arg1	interactions					91:102	NPC2 and Ebola virus interactions	70:102	NPC2 and Ebola virus interactions	70:102	Structure of glycosylated NPC1 luminal domain C reveals insights into NPC2 and Ebola virus interactions.
26846330	0	3	theme	virus	85:89	arg1	interactions					91:102	NPC2 and Ebola virus interactions	70:102	NPC2 and Ebola virus interactions	70:102	Structure of glycosylated NPC1 luminal domain C reveals insights into NPC2 and Ebola virus interactions.
26846330	0	4	gly	glycosylated	13:24	arg1	C					46:46	glycosylated NPC1 luminal domain C	13:46	glycosylated NPC1 luminal domain C	13:46	Structure of glycosylated NPC1 luminal domain C reveals insights into NPC2 and Ebola virus interactions.
26846330	4	5	theme	refractory	662:671	arg1	species					673:679	filovirus susceptible and refractory species	636:679	filovirus susceptible and refractory species	636:679	Knowledge-based docking of NPC1 onto Ebola viral glycoprotein and sequence analysis of filovirus susceptible and refractory species reveals four critical residues, H418, Q421, F502 and F504, some or all of which are likely responsible for the species-specific susceptibility to the virus infection.
26846330	4	6	theme	Ebola	586:590	arg1	glycoprotein					598:609	Ebola viral glycoprotein	586:609	Ebola viral glycoprotein	586:609	Knowledge-based docking of NPC1 onto Ebola viral glycoprotein and sequence analysis of filovirus susceptible and refractory species reveals four critical residues, H418, Q421, F502 and F504, some or all of which are likely responsible for the species-specific susceptibility to the virus infection.
26846330	0	7	theme	Ebola	79:83	arg1	virus					85:89	Ebola virus	79:89	Ebola virus	79:89	Structure of glycosylated NPC1 luminal domain C reveals insights into NPC2 and Ebola virus interactions.
26846330	3	8	theme	glycosylated	483:494	arg1	structure					496:504	the glycosylated structure	479:504	the glycosylated structure	479:504	Mapping the disease mutations onto the glycosylated structure reveals a potential binding face for NPC2.
26846330	3	9	theme	potential	516:524	arg1	face					534:537	a potential binding face	514:537	a potential binding face for NPC2	514:546	Mapping the disease mutations onto the glycosylated structure reveals a potential binding face for NPC2.
26846330	1	10	theme	endo/lysosomal	139:152	arg1	protein					163:169	an endo/lysosomal membrane protein	136:169	an endo/lysosomal membrane protein involved in intracellular cholesterol trafficking	136:219	Niemann-pick type C1 (NPC1) is an endo/lysosomal membrane protein involved in intracellular cholesterol trafficking, and its luminal domain C is an essential endosomal receptor for Ebola and Marburg viruses.
26846330	1	10	theme	endo/lysosomal	139:152	arg1	C1					123:124	Niemann-pick type C1	105:124	Niemann-pick type C1 (NPC1)	105:131	Niemann-pick type C1 (NPC1) is an endo/lysosomal membrane protein involved in intracellular cholesterol trafficking, and its luminal domain C is an essential endosomal receptor for Ebola and Marburg viruses.
26846330	1	11	dep	Ebola	286:290	arg1	viruses					304:310	viruses	304:310	viruses	304:310	Niemann-pick type C1 (NPC1) is an endo/lysosomal membrane protein involved in intracellular cholesterol trafficking, and its luminal domain C is an essential endosomal receptor for Ebola and Marburg viruses.
26846330	4	12	theme	NPC1	576:579	arg1	docking					565:571	Knowledge-based docking	549:571	Knowledge-based docking of NPC1 onto Ebola viral glycoprotein and sequence analysis of filovirus susceptible and refractory species	549:679	Knowledge-based docking of NPC1 onto Ebola viral glycoprotein and sequence analysis of filovirus susceptible and refractory species reveals four critical residues, H418, Q421, F502 and F504, some or all of which are likely responsible for the species-specific susceptibility to the virus infection.
26846330	3	13	gly	glycosylated	483:494	arg1	structure					496:504	the glycosylated structure	479:504	the glycosylated structure	479:504	Mapping the disease mutations onto the glycosylated structure reveals a potential binding face for NPC2.
26846330	1	14	theme	membrane	154:161	arg1	protein					163:169	an endo/lysosomal membrane protein	136:169	an endo/lysosomal membrane protein involved in intracellular cholesterol trafficking	136:219	Niemann-pick type C1 (NPC1) is an endo/lysosomal membrane protein involved in intracellular cholesterol trafficking, and its luminal domain C is an essential endosomal receptor for Ebola and Marburg viruses.
26846330	1	14	theme	membrane	154:161	arg1	C1					123:124	Niemann-pick type C1	105:124	Niemann-pick type C1 (NPC1)	105:131	Niemann-pick type C1 (NPC1) is an endo/lysosomal membrane protein involved in intracellular cholesterol trafficking, and its luminal domain C is an essential endosomal receptor for Ebola and Marburg viruses.
26846330	2	15	gly	glycosylated	357:368	arg1	C					390:390	glycosylated NPC1 luminal domain C	357:390	glycosylated NPC1 luminal domain C	357:390	We have determined the crystal structure of glycosylated NPC1 luminal domain C and find all seven possible sites are glycosylated.
26846330	2	16	theme	NPC1	370:373	arg1	C					390:390	glycosylated NPC1 luminal domain C	357:390	glycosylated NPC1 luminal domain C	357:390	We have determined the crystal structure of glycosylated NPC1 luminal domain C and find all seven possible sites are glycosylated.
26846330	1	17	theme	essential	253:261	arg1	receptor					273:280	an essential endosomal receptor	250:280	an essential endosomal receptor for Ebola and Marburg viruses	250:310	Niemann-pick type C1 (NPC1) is an endo/lysosomal membrane protein involved in intracellular cholesterol trafficking, and its luminal domain C is an essential endosomal receptor for Ebola and Marburg viruses.
26846330	1	17	theme	essential	253:261	arg1	C					245:245	its luminal domain C	226:245	its luminal domain C	226:245	Niemann-pick type C1 (NPC1) is an endo/lysosomal membrane protein involved in intracellular cholesterol trafficking, and its luminal domain C is an essential endosomal receptor for Ebola and Marburg viruses.
26846330	4	18	theme	virus	831:835	arg1	infection					837:845	the virus infection	827:845	the virus infection	827:845	Knowledge-based docking of NPC1 onto Ebola viral glycoprotein and sequence analysis of filovirus susceptible and refractory species reveals four critical residues, H418, Q421, F502 and F504, some or all of which are likely responsible for the species-specific susceptibility to the virus infection.
26846330	2	19	theme	glycosylated	357:368	arg1	C					390:390	glycosylated NPC1 luminal domain C	357:390	glycosylated NPC1 luminal domain C	357:390	We have determined the crystal structure of glycosylated NPC1 luminal domain C and find all seven possible sites are glycosylated.
26846330	0	20	theme	NPC1	26:29	arg1	C					46:46	glycosylated NPC1 luminal domain C	13:46	glycosylated NPC1 luminal domain C	13:46	Structure of glycosylated NPC1 luminal domain C reveals insights into NPC2 and Ebola virus interactions.
26846330	1	21	theme	endosomal	263:271	arg1	receptor					273:280	an essential endosomal receptor	250:280	an essential endosomal receptor for Ebola and Marburg viruses	250:310	Niemann-pick type C1 (NPC1) is an endo/lysosomal membrane protein involved in intracellular cholesterol trafficking, and its luminal domain C is an essential endosomal receptor for Ebola and Marburg viruses.
26846330	1	21	theme	endosomal	263:271	arg1	C					245:245	its luminal domain C	226:245	its luminal domain C	226:245	Niemann-pick type C1 (NPC1) is an endo/lysosomal membrane protein involved in intracellular cholesterol trafficking, and its luminal domain C is an essential endosomal receptor for Ebola and Marburg viruses.
26846330	0	22	theme	glycosylated	13:24	arg1	C					46:46	glycosylated NPC1 luminal domain C	13:46	glycosylated NPC1 luminal domain C	13:46	Structure of glycosylated NPC1 luminal domain C reveals insights into NPC2 and Ebola virus interactions.
26846330	1	23	theme	intracellular	183:195	arg1	trafficking					209:219	intracellular cholesterol trafficking	183:219	intracellular cholesterol trafficking	183:219	Niemann-pick type C1 (NPC1) is an endo/lysosomal membrane protein involved in intracellular cholesterol trafficking, and its luminal domain C is an essential endosomal receptor for Ebola and Marburg viruses.
26846330	0	24	theme	domain	39:44	arg1	C					46:46	glycosylated NPC1 luminal domain C	13:46	glycosylated NPC1 luminal domain C	13:46	Structure of glycosylated NPC1 luminal domain C reveals insights into NPC2 and Ebola virus interactions.
26846330	4	25	theme	Knowledge-based	549:563	arg1	docking					565:571	Knowledge-based docking	549:571	Knowledge-based docking of NPC1 onto Ebola viral glycoprotein and sequence analysis of filovirus susceptible and refractory species	549:679	Knowledge-based docking of NPC1 onto Ebola viral glycoprotein and sequence analysis of filovirus susceptible and refractory species reveals four critical residues, H418, Q421, F502 and F504, some or all of which are likely responsible for the species-specific susceptibility to the virus infection.
26846330	4	26	theme	susceptible	646:656	arg1	species					673:679	filovirus susceptible and refractory species	636:679	filovirus susceptible and refractory species	636:679	Knowledge-based docking of NPC1 onto Ebola viral glycoprotein and sequence analysis of filovirus susceptible and refractory species reveals four critical residues, H418, Q421, F502 and F504, some or all of which are likely responsible for the species-specific susceptibility to the virus infection.
26846330	4	27	theme	species	673:679	arg1	glycoprotein					598:609	Ebola viral glycoprotein	586:609	Ebola viral glycoprotein	586:609	Knowledge-based docking of NPC1 onto Ebola viral glycoprotein and sequence analysis of filovirus susceptible and refractory species reveals four critical residues, H418, Q421, F502 and F504, some or all of which are likely responsible for the species-specific susceptibility to the virus infection.
26846330	4	27	theme	species	673:679	arg1	analysis					624:631	sequence analysis	615:631	sequence analysis	615:631	Knowledge-based docking of NPC1 onto Ebola viral glycoprotein and sequence analysis of filovirus susceptible and refractory species reveals four critical residues, H418, Q421, F502 and F504, some or all of which are likely responsible for the species-specific susceptibility to the virus infection.
26846330	1	28	theme	cholesterol	197:207	arg1	trafficking					209:219	intracellular cholesterol trafficking	183:219	intracellular cholesterol trafficking	183:219	Niemann-pick type C1 (NPC1) is an endo/lysosomal membrane protein involved in intracellular cholesterol trafficking, and its luminal domain C is an essential endosomal receptor for Ebola and Marburg viruses.
26846330	0	29	theme	luminal	31:37	arg1	C					46:46	glycosylated NPC1 luminal domain C	13:46	glycosylated NPC1 luminal domain C	13:46	Structure of glycosylated NPC1 luminal domain C reveals insights into NPC2 and Ebola virus interactions.
26846330	2	30	theme	possible	411:418	arg1	sites					420:424	all seven possible sites	401:424	all seven possible sites	401:424	We have determined the crystal structure of glycosylated NPC1 luminal domain C and find all seven possible sites are glycosylated.
26846330	2	31	theme	C	390:390	arg1	structure					344:352	the crystal structure	332:352	the crystal structure of glycosylated NPC1 luminal domain C	332:390	We have determined the crystal structure of glycosylated NPC1 luminal domain C and find all seven possible sites are glycosylated.
26846330	2	32	gly	glycosylated	430:441	arg1	sites					420:424	all seven possible sites	401:424	all seven possible sites	401:424	We have determined the crystal structure of glycosylated NPC1 luminal domain C and find all seven possible sites are glycosylated.
26846330	1	33	theme	Niemann-pick	105:116	arg1	C1					123:124	Niemann-pick type C1	105:124	Niemann-pick type C1 (NPC1)	105:131	Niemann-pick type C1 (NPC1) is an endo/lysosomal membrane protein involved in intracellular cholesterol trafficking, and its luminal domain C is an essential endosomal receptor for Ebola and Marburg viruses.
26846330	1	33	theme	Niemann-pick	105:116	arg1	protein					163:169	an endo/lysosomal membrane protein	136:169	an endo/lysosomal membrane protein involved in intracellular cholesterol trafficking	136:219	Niemann-pick type C1 (NPC1) is an endo/lysosomal membrane protein involved in intracellular cholesterol trafficking, and its luminal domain C is an essential endosomal receptor for Ebola and Marburg viruses.
26846330	1	33	theme	Niemann-pick	105:116	arg1	NPC1					127:130	NPC1	127:130	NPC1	127:130	Niemann-pick type C1 (NPC1) is an endo/lysosomal membrane protein involved in intracellular cholesterol trafficking, and its luminal domain C is an essential endosomal receptor for Ebola and Marburg viruses.
26846330	0	34	theme	C	46:46	arg1	Structure					0:8	Structure	0:8	Structure of glycosylated NPC1 luminal domain C	0:46	Structure of glycosylated NPC1 luminal domain C reveals insights into NPC2 and Ebola virus interactions.
26846330	2	35	theme	domain	383:388	arg1	C					390:390	glycosylated NPC1 luminal domain C	357:390	glycosylated NPC1 luminal domain C	357:390	We have determined the crystal structure of glycosylated NPC1 luminal domain C and find all seven possible sites are glycosylated.
26846330	4	36	theme	species-specific	792:807	arg1	susceptibility					809:822	the species-specific susceptibility	788:822	the species-specific susceptibility to the virus infection	788:845	Knowledge-based docking of NPC1 onto Ebola viral glycoprotein and sequence analysis of filovirus susceptible and refractory species reveals four critical residues, H418, Q421, F502 and F504, some or all of which are likely responsible for the species-specific susceptibility to the virus infection.
26846330	1	37	theme	type	118:121	arg1	C1					123:124	Niemann-pick type C1	105:124	Niemann-pick type C1 (NPC1)	105:131	Niemann-pick type C1 (NPC1) is an endo/lysosomal membrane protein involved in intracellular cholesterol trafficking, and its luminal domain C is an essential endosomal receptor for Ebola and Marburg viruses.
26846330	1	37	theme	type	118:121	arg1	protein					163:169	an endo/lysosomal membrane protein	136:169	an endo/lysosomal membrane protein involved in intracellular cholesterol trafficking	136:219	Niemann-pick type C1 (NPC1) is an endo/lysosomal membrane protein involved in intracellular cholesterol trafficking, and its luminal domain C is an essential endosomal receptor for Ebola and Marburg viruses.
26846330	1	37	theme	type	118:121	arg1	NPC1					127:130	NPC1	127:130	NPC1	127:130	Niemann-pick type C1 (NPC1) is an endo/lysosomal membrane protein involved in intracellular cholesterol trafficking, and its luminal domain C is an essential endosomal receptor for Ebola and Marburg viruses.
26846330	4	38	gly	glycoprotein	598:609	arg1	glycoprotein					598:609	Ebola viral glycoprotein	586:609	Ebola viral glycoprotein	586:609	Knowledge-based docking of NPC1 onto Ebola viral glycoprotein and sequence analysis of filovirus susceptible and refractory species reveals four critical residues, H418, Q421, F502 and F504, some or all of which are likely responsible for the species-specific susceptibility to the virus infection.
26846330	3	39	theme	disease	456:462	arg1	mutations					464:472	the disease mutations	452:472	the disease mutations onto the glycosylated structure	452:504	Mapping the disease mutations onto the glycosylated structure reveals a potential binding face for NPC2.
26846330	3	40	theme	binding	526:532	arg1	face					534:537	a potential binding face	514:537	a potential binding face for NPC2	514:546	Mapping the disease mutations onto the glycosylated structure reveals a potential binding face for NPC2.
26846330	4	41	theme	viral	592:596	arg1	glycoprotein					598:609	Ebola viral glycoprotein	586:609	Ebola viral glycoprotein	586:609	Knowledge-based docking of NPC1 onto Ebola viral glycoprotein and sequence analysis of filovirus susceptible and refractory species reveals four critical residues, H418, Q421, F502 and F504, some or all of which are likely responsible for the species-specific susceptibility to the virus infection.
26846330	4	42	theme	filovirus	636:644	arg1	species					673:679	filovirus susceptible and refractory species	636:679	filovirus susceptible and refractory species	636:679	Knowledge-based docking of NPC1 onto Ebola viral glycoprotein and sequence analysis of filovirus susceptible and refractory species reveals four critical residues, H418, Q421, F502 and F504, some or all of which are likely responsible for the species-specific susceptibility to the virus infection.
26846330	4	43	theme	critical	694:701	arg1	residues					703:710	four critical residues	689:710	four critical residues	689:710	Knowledge-based docking of NPC1 onto Ebola viral glycoprotein and sequence analysis of filovirus susceptible and refractory species reveals four critical residues, H418, Q421, F502 and F504, some or all of which are likely responsible for the species-specific susceptibility to the virus infection.
26846330	4	43	theme	critical	694:701	arg1	F504					734:737	F504	734:737	F504	734:737	Knowledge-based docking of NPC1 onto Ebola viral glycoprotein and sequence analysis of filovirus susceptible and refractory species reveals four critical residues, H418, Q421, F502 and F504, some or all of which are likely responsible for the species-specific susceptibility to the virus infection.
26846330	4	43	theme	critical	694:701	arg1	F502					725:728	F502	725:728	F502	725:728	Knowledge-based docking of NPC1 onto Ebola viral glycoprotein and sequence analysis of filovirus susceptible and refractory species reveals four critical residues, H418, Q421, F502 and F504, some or all of which are likely responsible for the species-specific susceptibility to the virus infection.
26846330	4	43	theme	critical	694:701	arg1	Q421					719:722	Q421	719:722	Q421	719:722	Knowledge-based docking of NPC1 onto Ebola viral glycoprotein and sequence analysis of filovirus susceptible and refractory species reveals four critical residues, H418, Q421, F502 and F504, some or all of which are likely responsible for the species-specific susceptibility to the virus infection.
26846330	2	44	theme	luminal	375:381	arg1	C					390:390	glycosylated NPC1 luminal domain C	357:390	glycosylated NPC1 luminal domain C	357:390	We have determined the crystal structure of glycosylated NPC1 luminal domain C and find all seven possible sites are glycosylated.
26846330	4	45	theme	sequence	615:622	arg1	analysis					624:631	sequence analysis	615:631	sequence analysis	615:631	Knowledge-based docking of NPC1 onto Ebola viral glycoprotein and sequence analysis of filovirus susceptible and refractory species reveals four critical residues, H418, Q421, F502 and F504, some or all of which are likely responsible for the species-specific susceptibility to the virus infection.
26846330	1	46	theme	luminal	230:236	arg1	receptor					273:280	an essential endosomal receptor	250:280	an essential endosomal receptor for Ebola and Marburg viruses	250:310	Niemann-pick type C1 (NPC1) is an endo/lysosomal membrane protein involved in intracellular cholesterol trafficking, and its luminal domain C is an essential endosomal receptor for Ebola and Marburg viruses.
26846330	1	46	theme	luminal	230:236	arg1	C					245:245	its luminal domain C	226:245	its luminal domain C	226:245	Niemann-pick type C1 (NPC1) is an endo/lysosomal membrane protein involved in intracellular cholesterol trafficking, and its luminal domain C is an essential endosomal receptor for Ebola and Marburg viruses.
16212439	5	0	theme	global	1036:1041	arg1	maps					1059:1062	global phosphorylation maps	1036:1062	global phosphorylation maps	1036:1062	Extension of these methods to other substrates should facilitate generation of global phosphorylation maps and protein-protein interactions for any protein of interest.
16212439	2	1	theme	mass	603:606	arg1	spectrometry					608:619	LTQ-FT or LTQ-ETD mass spectrometry	585:619	spectrometry	608:619	The strategy includes (1) lower-level, transient transfection of FLAG-GFP-Paxillin into HEK293 cells, (2) incubation of cells with phosphatase inhibitors prior to lysis, (3) purification of paxillin by anti-FLAG immunoprecipitation, (4) analysis of peptides generated from on-beads digestion using LTQ-FT or LTQ-ETD mass spectrometry, and (5) enrichment of phosphopeptide methyl esters with IMAC.
16212439	4	2	attach	present	920:926	arg2	proteins					901:908	10 co-purifying proteins	885:908	10 co-purifying proteins which are present in focal adhesion complexes	885:954	Furthermore, with this method, we simultaneously detect 10 co-purifying proteins which are present in focal adhesion complexes.
16212439	4	2	attach	present	920:926	arg1	complexes					946:954	focal adhesion complexes	931:954	focal adhesion complexes	931:954	Furthermore, with this method, we simultaneously detect 10 co-purifying proteins which are present in focal adhesion complexes.
16212439	1	3	theme	proteins	177:184	arg1	identification					147:160	the simultaneous identification	130:160	the simultaneous identification of interacting proteins and post-translational modifications of the focal adhesion adapter protein, paxillin,	130:270	Methods for the simultaneous identification of interacting proteins and post-translational modifications of the focal adhesion adapter protein, paxillin, are presented.
16212439	3	4	theme	novel	793:797	arg1	site					813:816	a novel glycosylation site	791:816	a novel glycosylation site on Ser 74	791:826	Using the above strategies, we identify 29 phosphorylation sites (19 novel and 10 previously reported) and a novel glycosylation site on Ser 74.
16212439	0	5	theme	proteins	87:94	arg1	detection					16:24	the detection	12:24	the detection of paxillin post-translational modifications and interacting proteins by mass spectrometry	12:115	Methods for the detection of paxillin post-translational modifications and interacting proteins by mass spectrometry.
16212439	5	6	theme	interest	1116:1123	arg1	protein					1105:1111	any protein	1101:1111	any protein of interest	1101:1123	Extension of these methods to other substrates should facilitate generation of global phosphorylation maps and protein-protein interactions for any protein of interest.
16212439	2	7	theme	LTQ-ETD	595:601	arg1	spectrometry					608:619	LTQ-FT or LTQ-ETD mass spectrometry	585:619	spectrometry	608:619	The strategy includes (1) lower-level, transient transfection of FLAG-GFP-Paxillin into HEK293 cells, (2) incubation of cells with phosphatase inhibitors prior to lysis, (3) purification of paxillin by anti-FLAG immunoprecipitation, (4) analysis of peptides generated from on-beads digestion using LTQ-FT or LTQ-ETD mass spectrometry, and (5) enrichment of phosphopeptide methyl esters with IMAC.
16212439	2	8	dep	purification	461:472	arg1	3					458:458	3	458:458	3	458:458	The strategy includes (1) lower-level, transient transfection of FLAG-GFP-Paxillin into HEK293 cells, (2) incubation of cells with phosphatase inhibitors prior to lysis, (3) purification of paxillin by anti-FLAG immunoprecipitation, (4) analysis of peptides generated from on-beads digestion using LTQ-FT or LTQ-ETD mass spectrometry, and (5) enrichment of phosphopeptide methyl esters with IMAC.
16212439	3	9	theme	glycosylation	799:811	arg1	site					813:816	a novel glycosylation site	791:816	a novel glycosylation site on Ser 74	791:826	Using the above strategies, we identify 29 phosphorylation sites (19 novel and 10 previously reported) and a novel glycosylation site on Ser 74.
16212439	3	10	dep	sites	743:747	arg1	10					763:764	10	763:764	10	763:764	Using the above strategies, we identify 29 phosphorylation sites (19 novel and 10 previously reported) and a novel glycosylation site on Ser 74.
16212439	3	10	dep	sites	743:747	arg1	novel					753:757	novel	753:757	novel	753:757	Using the above strategies, we identify 29 phosphorylation sites (19 novel and 10 previously reported) and a novel glycosylation site on Ser 74.
16212439	4	11	located	present	920:926	arg2	proteins					901:908	10 co-purifying proteins	885:908	10 co-purifying proteins which are present in focal adhesion complexes	885:954	Furthermore, with this method, we simultaneously detect 10 co-purifying proteins which are present in focal adhesion complexes.
16212439	4	11	located	present	920:926	arg1	complexes					946:954	focal adhesion complexes	931:954	focal adhesion complexes	931:954	Furthermore, with this method, we simultaneously detect 10 co-purifying proteins which are present in focal adhesion complexes.
16212439	4	12	theme	adhesion	937:944	arg1	complexes					946:954	focal adhesion complexes	931:954	focal adhesion complexes	931:954	Furthermore, with this method, we simultaneously detect 10 co-purifying proteins which are present in focal adhesion complexes.
16212439	0	13	theme	mass	99:102	arg1	spectrometry					104:115	mass spectrometry	99:115	mass spectrometry	99:115	Methods for the detection of paxillin post-translational modifications and interacting proteins by mass spectrometry.
16212439	5	14	theme	protein-protein	1068:1082	arg1	interactions					1084:1095	protein-protein interactions	1068:1095	protein-protein interactions	1068:1095	Extension of these methods to other substrates should facilitate generation of global phosphorylation maps and protein-protein interactions for any protein of interest.
16212439	2	15	theme	LTQ-FT	585:590	arg1	spectrometry					608:619	LTQ-FT or LTQ-ETD mass spectrometry	585:619	spectrometry	608:619	The strategy includes (1) lower-level, transient transfection of FLAG-GFP-Paxillin into HEK293 cells, (2) incubation of cells with phosphatase inhibitors prior to lysis, (3) purification of paxillin by anti-FLAG immunoprecipitation, (4) analysis of peptides generated from on-beads digestion using LTQ-FT or LTQ-ETD mass spectrometry, and (5) enrichment of phosphopeptide methyl esters with IMAC.
16212439	4	16	theme	focal	931:935	arg1	complexes					946:954	focal adhesion complexes	931:954	focal adhesion complexes	931:954	Furthermore, with this method, we simultaneously detect 10 co-purifying proteins which are present in focal adhesion complexes.
16212439	5	17	theme	interactions	1084:1095	arg1	generation					1022:1031	generation	1022:1031	generation of global phosphorylation maps and protein-protein interactions for any protein of interest	1022:1123	Extension of these methods to other substrates should facilitate generation of global phosphorylation maps and protein-protein interactions for any protein of interest.
16212439	1	18	theme	post-translational	190:207	arg1	modifications					209:221	post-translational modifications	190:221	post-translational modifications of the focal adhesion adapter protein, paxillin,	190:270	Methods for the simultaneous identification of interacting proteins and post-translational modifications of the focal adhesion adapter protein, paxillin, are presented.
16212439	2	19	with	esters	666:671	arg1	IMAC					678:681	IMAC	678:681	IMAC	678:681	The strategy includes (1) lower-level, transient transfection of FLAG-GFP-Paxillin into HEK293 cells, (2) incubation of cells with phosphatase inhibitors prior to lysis, (3) purification of paxillin by anti-FLAG immunoprecipitation, (4) analysis of peptides generated from on-beads digestion using LTQ-FT or LTQ-ETD mass spectrometry, and (5) enrichment of phosphopeptide methyl esters with IMAC.
16212439	3	20	theme	above	694:698	arg1	strategies					700:709	the above strategies	690:709	the above strategies	690:709	Using the above strategies, we identify 29 phosphorylation sites (19 novel and 10 previously reported) and a novel glycosylation site on Ser 74.
16212439	4	21	from	present	920:926	arg1	complexes					946:954	focal adhesion complexes	931:954	focal adhesion complexes	931:954	Furthermore, with this method, we simultaneously detect 10 co-purifying proteins which are present in focal adhesion complexes.
16212439	1	22	theme	modifications	209:221	arg1	identification					147:160	the simultaneous identification	130:160	the simultaneous identification of interacting proteins and post-translational modifications of the focal adhesion adapter protein, paxillin,	130:270	Methods for the simultaneous identification of interacting proteins and post-translational modifications of the focal adhesion adapter protein, paxillin, are presented.
16212439	2	23	theme	paxillin	477:484	arg1	purification					461:472	(3) purification	457:472	(3) purification of paxillin by anti-FLAG immunoprecipitation	457:517	The strategy includes (1) lower-level, transient transfection of FLAG-GFP-Paxillin into HEK293 cells, (2) incubation of cells with phosphatase inhibitors prior to lysis, (3) purification of paxillin by anti-FLAG immunoprecipitation, (4) analysis of peptides generated from on-beads digestion using LTQ-FT or LTQ-ETD mass spectrometry, and (5) enrichment of phosphopeptide methyl esters with IMAC.
16212439	2	23	theme	paxillin	477:484	arg1	transfection					336:347	(1) lower-level, transient transfection	309:347	transfection	336:347	The strategy includes (1) lower-level, transient transfection of FLAG-GFP-Paxillin into HEK293 cells, (2) incubation of cells with phosphatase inhibitors prior to lysis, (3) purification of paxillin by anti-FLAG immunoprecipitation, (4) analysis of peptides generated from on-beads digestion using LTQ-FT or LTQ-ETD mass spectrometry, and (5) enrichment of phosphopeptide methyl esters with IMAC.
16212439	2	24	theme	esters	666:671	arg1	enrichment					630:639	(5) enrichment	626:639	(5) enrichment of phosphopeptide methyl esters with IMAC	626:681	The strategy includes (1) lower-level, transient transfection of FLAG-GFP-Paxillin into HEK293 cells, (2) incubation of cells with phosphatase inhibitors prior to lysis, (3) purification of paxillin by anti-FLAG immunoprecipitation, (4) analysis of peptides generated from on-beads digestion using LTQ-FT or LTQ-ETD mass spectrometry, and (5) enrichment of phosphopeptide methyl esters with IMAC.
16212439	2	24	theme	esters	666:671	arg1	spectrometry					608:619	LTQ-FT or LTQ-ETD mass spectrometry	585:619	spectrometry	608:619	The strategy includes (1) lower-level, transient transfection of FLAG-GFP-Paxillin into HEK293 cells, (2) incubation of cells with phosphatase inhibitors prior to lysis, (3) purification of paxillin by anti-FLAG immunoprecipitation, (4) analysis of peptides generated from on-beads digestion using LTQ-FT or LTQ-ETD mass spectrometry, and (5) enrichment of phosphopeptide methyl esters with IMAC.
16212439	3	25	from	site	813:816	arg1	Ser					821:823	Ser 74	821:826	Ser 74	821:826	Using the above strategies, we identify 29 phosphorylation sites (19 novel and 10 previously reported) and a novel glycosylation site on Ser 74.
16212439	3	26	theme	phosphorylation	727:741	arg1	sites					743:747	29 phosphorylation sites	724:747	29 phosphorylation sites (19 novel and 10 previously reported)	724:785	Using the above strategies, we identify 29 phosphorylation sites (19 novel and 10 previously reported) and a novel glycosylation site on Ser 74.
16212439	3	27	from	sites	743:747	arg1	Ser					821:823	Ser 74	821:826	Ser 74	821:826	Using the above strategies, we identify 29 phosphorylation sites (19 novel and 10 previously reported) and a novel glycosylation site on Ser 74.
16212439	2	28	theme	methyl	659:664	arg1	esters					666:671	phosphopeptide methyl esters	644:671	phosphopeptide methyl esters with IMAC	644:681	The strategy includes (1) lower-level, transient transfection of FLAG-GFP-Paxillin into HEK293 cells, (2) incubation of cells with phosphatase inhibitors prior to lysis, (3) purification of paxillin by anti-FLAG immunoprecipitation, (4) analysis of peptides generated from on-beads digestion using LTQ-FT or LTQ-ETD mass spectrometry, and (5) enrichment of phosphopeptide methyl esters with IMAC.
16212439	2	29	theme	transient	326:334	arg1	analysis					524:531	(4) analysis	520:531	(4) analysis of peptides generated from on-beads digestion using LTQ-FT or LTQ-ETD mass spectrometry, and (5) enrichment of phosphopeptide methyl esters with IMAC	520:681	The strategy includes (1) lower-level, transient transfection of FLAG-GFP-Paxillin into HEK293 cells, (2) incubation of cells with phosphatase inhibitors prior to lysis, (3) purification of paxillin by anti-FLAG immunoprecipitation, (4) analysis of peptides generated from on-beads digestion using LTQ-FT or LTQ-ETD mass spectrometry, and (5) enrichment of phosphopeptide methyl esters with IMAC.
16212439	2	29	theme	transient	326:334	arg1	purification					461:472	(3) purification	457:472	(3) purification of paxillin by anti-FLAG immunoprecipitation	457:517	The strategy includes (1) lower-level, transient transfection of FLAG-GFP-Paxillin into HEK293 cells, (2) incubation of cells with phosphatase inhibitors prior to lysis, (3) purification of paxillin by anti-FLAG immunoprecipitation, (4) analysis of peptides generated from on-beads digestion using LTQ-FT or LTQ-ETD mass spectrometry, and (5) enrichment of phosphopeptide methyl esters with IMAC.
16212439	2	29	theme	transient	326:334	arg1	incubation					393:402	(2) incubation	389:402	(2) incubation of cells with phosphatase inhibitors prior to lysis	389:454	The strategy includes (1) lower-level, transient transfection of FLAG-GFP-Paxillin into HEK293 cells, (2) incubation of cells with phosphatase inhibitors prior to lysis, (3) purification of paxillin by anti-FLAG immunoprecipitation, (4) analysis of peptides generated from on-beads digestion using LTQ-FT or LTQ-ETD mass spectrometry, and (5) enrichment of phosphopeptide methyl esters with IMAC.
16212439	2	29	theme	transient	326:334	arg1	transfection					336:347	(1) lower-level, transient transfection	309:347	transfection	336:347	The strategy includes (1) lower-level, transient transfection of FLAG-GFP-Paxillin into HEK293 cells, (2) incubation of cells with phosphatase inhibitors prior to lysis, (3) purification of paxillin by anti-FLAG immunoprecipitation, (4) analysis of peptides generated from on-beads digestion using LTQ-FT or LTQ-ETD mass spectrometry, and (5) enrichment of phosphopeptide methyl esters with IMAC.
16212439	5	30	theme	phosphorylation	1043:1057	arg1	maps					1059:1062	global phosphorylation maps	1036:1062	global phosphorylation maps	1036:1062	Extension of these methods to other substrates should facilitate generation of global phosphorylation maps and protein-protein interactions for any protein of interest.
16212439	2	31	theme	phosphopeptide	644:657	arg1	esters					666:671	phosphopeptide methyl esters	644:671	phosphopeptide methyl esters with IMAC	644:681	The strategy includes (1) lower-level, transient transfection of FLAG-GFP-Paxillin into HEK293 cells, (2) incubation of cells with phosphatase inhibitors prior to lysis, (3) purification of paxillin by anti-FLAG immunoprecipitation, (4) analysis of peptides generated from on-beads digestion using LTQ-FT or LTQ-ETD mass spectrometry, and (5) enrichment of phosphopeptide methyl esters with IMAC.
16212439	2	32	dep	transfection	336:347	arg1	1					310:310	1	310:310	1	310:310	The strategy includes (1) lower-level, transient transfection of FLAG-GFP-Paxillin into HEK293 cells, (2) incubation of cells with phosphatase inhibitors prior to lysis, (3) purification of paxillin by anti-FLAG immunoprecipitation, (4) analysis of peptides generated from on-beads digestion using LTQ-FT or LTQ-ETD mass spectrometry, and (5) enrichment of phosphopeptide methyl esters with IMAC.
16212439	1	33	theme	focal	230:234	arg1	paxillin					262:269	paxillin	262:269	paxillin	262:269	Methods for the simultaneous identification of interacting proteins and post-translational modifications of the focal adhesion adapter protein, paxillin, are presented.
16212439	1	33	theme	focal	230:234	arg1	protein					253:259	the focal adhesion adapter protein	226:259	the focal adhesion adapter protein	226:259	Methods for the simultaneous identification of interacting proteins and post-translational modifications of the focal adhesion adapter protein, paxillin, are presented.
16212439	2	34	theme	peptides	536:543	arg1	analysis					524:531	(4) analysis	520:531	(4) analysis of peptides generated from on-beads digestion using LTQ-FT or LTQ-ETD mass spectrometry, and (5) enrichment of phosphopeptide methyl esters with IMAC	520:681	The strategy includes (1) lower-level, transient transfection of FLAG-GFP-Paxillin into HEK293 cells, (2) incubation of cells with phosphatase inhibitors prior to lysis, (3) purification of paxillin by anti-FLAG immunoprecipitation, (4) analysis of peptides generated from on-beads digestion using LTQ-FT or LTQ-ETD mass spectrometry, and (5) enrichment of phosphopeptide methyl esters with IMAC.
16212439	2	34	theme	peptides	536:543	arg1	transfection					336:347	(1) lower-level, transient transfection	309:347	transfection	336:347	The strategy includes (1) lower-level, transient transfection of FLAG-GFP-Paxillin into HEK293 cells, (2) incubation of cells with phosphatase inhibitors prior to lysis, (3) purification of paxillin by anti-FLAG immunoprecipitation, (4) analysis of peptides generated from on-beads digestion using LTQ-FT or LTQ-ETD mass spectrometry, and (5) enrichment of phosphopeptide methyl esters with IMAC.
16212439	3	35	gly	glycosylation	799:811	arg2	site					813:816	a novel glycosylation site	791:816	a novel glycosylation site on Ser 74	791:826	Using the above strategies, we identify 29 phosphorylation sites (19 novel and 10 previously reported) and a novel glycosylation site on Ser 74.
16212439	2	36	theme	lower-level	313:323	arg1	analysis					524:531	(4) analysis	520:531	(4) analysis of peptides generated from on-beads digestion using LTQ-FT or LTQ-ETD mass spectrometry, and (5) enrichment of phosphopeptide methyl esters with IMAC	520:681	The strategy includes (1) lower-level, transient transfection of FLAG-GFP-Paxillin into HEK293 cells, (2) incubation of cells with phosphatase inhibitors prior to lysis, (3) purification of paxillin by anti-FLAG immunoprecipitation, (4) analysis of peptides generated from on-beads digestion using LTQ-FT or LTQ-ETD mass spectrometry, and (5) enrichment of phosphopeptide methyl esters with IMAC.
16212439	2	36	theme	lower-level	313:323	arg1	purification					461:472	(3) purification	457:472	(3) purification of paxillin by anti-FLAG immunoprecipitation	457:517	The strategy includes (1) lower-level, transient transfection of FLAG-GFP-Paxillin into HEK293 cells, (2) incubation of cells with phosphatase inhibitors prior to lysis, (3) purification of paxillin by anti-FLAG immunoprecipitation, (4) analysis of peptides generated from on-beads digestion using LTQ-FT or LTQ-ETD mass spectrometry, and (5) enrichment of phosphopeptide methyl esters with IMAC.
16212439	2	36	theme	lower-level	313:323	arg1	incubation					393:402	(2) incubation	389:402	(2) incubation of cells with phosphatase inhibitors prior to lysis	389:454	The strategy includes (1) lower-level, transient transfection of FLAG-GFP-Paxillin into HEK293 cells, (2) incubation of cells with phosphatase inhibitors prior to lysis, (3) purification of paxillin by anti-FLAG immunoprecipitation, (4) analysis of peptides generated from on-beads digestion using LTQ-FT or LTQ-ETD mass spectrometry, and (5) enrichment of phosphopeptide methyl esters with IMAC.
16212439	2	36	theme	lower-level	313:323	arg1	transfection					336:347	(1) lower-level, transient transfection	309:347	transfection	336:347	The strategy includes (1) lower-level, transient transfection of FLAG-GFP-Paxillin into HEK293 cells, (2) incubation of cells with phosphatase inhibitors prior to lysis, (3) purification of paxillin by anti-FLAG immunoprecipitation, (4) analysis of peptides generated from on-beads digestion using LTQ-FT or LTQ-ETD mass spectrometry, and (5) enrichment of phosphopeptide methyl esters with IMAC.
16212439	1	37	theme	adhesion	236:243	arg1	paxillin					262:269	paxillin	262:269	paxillin	262:269	Methods for the simultaneous identification of interacting proteins and post-translational modifications of the focal adhesion adapter protein, paxillin, are presented.
16212439	1	37	theme	adhesion	236:243	arg1	protein					253:259	the focal adhesion adapter protein	226:259	the focal adhesion adapter protein	226:259	Methods for the simultaneous identification of interacting proteins and post-translational modifications of the focal adhesion adapter protein, paxillin, are presented.
16212439	0	38	theme	paxillin	29:36	arg1	modifications					57:69	paxillin post-translational modifications	29:69	paxillin post-translational modifications	29:69	Methods for the detection of paxillin post-translational modifications and interacting proteins by mass spectrometry.
16212439	4	39	theme	co-purifying	888:899	arg1	proteins					901:908	10 co-purifying proteins	885:908	10 co-purifying proteins which are present in focal adhesion complexes	885:954	Furthermore, with this method, we simultaneously detect 10 co-purifying proteins which are present in focal adhesion complexes.
16212439	2	40	theme	phosphatase	418:428	arg1	inhibitors					430:439	phosphatase inhibitors	418:439	phosphatase inhibitors prior to lysis	418:454	The strategy includes (1) lower-level, transient transfection of FLAG-GFP-Paxillin into HEK293 cells, (2) incubation of cells with phosphatase inhibitors prior to lysis, (3) purification of paxillin by anti-FLAG immunoprecipitation, (4) analysis of peptides generated from on-beads digestion using LTQ-FT or LTQ-ETD mass spectrometry, and (5) enrichment of phosphopeptide methyl esters with IMAC.
16212439	5	41	theme	methods	976:982	arg1	Extension					957:965	Extension	957:965	Extension of these methods to other substrates	957:1002	Extension of these methods to other substrates should facilitate generation of global phosphorylation maps and protein-protein interactions for any protein of interest.
16212439	1	42	theme	adapter	245:251	arg1	paxillin					262:269	paxillin	262:269	paxillin	262:269	Methods for the simultaneous identification of interacting proteins and post-translational modifications of the focal adhesion adapter protein, paxillin, are presented.
16212439	1	42	theme	adapter	245:251	arg1	protein					253:259	the focal adhesion adapter protein	226:259	the focal adhesion adapter protein	226:259	Methods for the simultaneous identification of interacting proteins and post-translational modifications of the focal adhesion adapter protein, paxillin, are presented.
16212439	2	43	theme	cells	407:411	arg1	incubation					393:402	(2) incubation	389:402	(2) incubation of cells with phosphatase inhibitors prior to lysis	389:454	The strategy includes (1) lower-level, transient transfection of FLAG-GFP-Paxillin into HEK293 cells, (2) incubation of cells with phosphatase inhibitors prior to lysis, (3) purification of paxillin by anti-FLAG immunoprecipitation, (4) analysis of peptides generated from on-beads digestion using LTQ-FT or LTQ-ETD mass spectrometry, and (5) enrichment of phosphopeptide methyl esters with IMAC.
16212439	2	43	theme	cells	407:411	arg1	transfection					336:347	(1) lower-level, transient transfection	309:347	transfection	336:347	The strategy includes (1) lower-level, transient transfection of FLAG-GFP-Paxillin into HEK293 cells, (2) incubation of cells with phosphatase inhibitors prior to lysis, (3) purification of paxillin by anti-FLAG immunoprecipitation, (4) analysis of peptides generated from on-beads digestion using LTQ-FT or LTQ-ETD mass spectrometry, and (5) enrichment of phosphopeptide methyl esters with IMAC.
16212439	5	44	theme	maps	1059:1062	arg1	generation					1022:1031	generation	1022:1031	generation of global phosphorylation maps and protein-protein interactions for any protein of interest	1022:1123	Extension of these methods to other substrates should facilitate generation of global phosphorylation maps and protein-protein interactions for any protein of interest.
16212439	1	45	theme	protein	253:259	arg1	proteins					177:184	interacting proteins	165:184	interacting proteins	165:184	Methods for the simultaneous identification of interacting proteins and post-translational modifications of the focal adhesion adapter protein, paxillin, are presented.
16212439	1	45	theme	protein	253:259	arg1	modifications					209:221	post-translational modifications	190:221	post-translational modifications of the focal adhesion adapter protein, paxillin,	190:270	Methods for the simultaneous identification of interacting proteins and post-translational modifications of the focal adhesion adapter protein, paxillin, are presented.
16212439	0	46	theme	modifications	57:69	arg1	detection					16:24	the detection	12:24	the detection of paxillin post-translational modifications and interacting proteins by mass spectrometry	12:115	Methods for the detection of paxillin post-translational modifications and interacting proteins by mass spectrometry.
16212439	5	47	theme	other	987:991	arg1	substrates					993:1002	other substrates	987:1002	other substrates	987:1002	Extension of these methods to other substrates should facilitate generation of global phosphorylation maps and protein-protein interactions for any protein of interest.
16212439	2	48	theme	HEK293	375:380	arg1	cells					382:386	HEK293 cells	375:386	HEK293 cells	375:386	The strategy includes (1) lower-level, transient transfection of FLAG-GFP-Paxillin into HEK293 cells, (2) incubation of cells with phosphatase inhibitors prior to lysis, (3) purification of paxillin by anti-FLAG immunoprecipitation, (4) analysis of peptides generated from on-beads digestion using LTQ-FT or LTQ-ETD mass spectrometry, and (5) enrichment of phosphopeptide methyl esters with IMAC.
16212439	0	49	theme	post-translational	38:55	arg1	modifications					57:69	paxillin post-translational modifications	29:69	paxillin post-translational modifications	29:69	Methods for the detection of paxillin post-translational modifications and interacting proteins by mass spectrometry.
16212439	2	50	theme	on-beads	560:567	arg1	digestion					569:577	on-beads digestion	560:577	on-beads digestion using LTQ-FT or LTQ-ETD mass spectrometry, and (5) enrichment of phosphopeptide methyl esters with IMAC	560:681	The strategy includes (1) lower-level, transient transfection of FLAG-GFP-Paxillin into HEK293 cells, (2) incubation of cells with phosphatase inhibitors prior to lysis, (3) purification of paxillin by anti-FLAG immunoprecipitation, (4) analysis of peptides generated from on-beads digestion using LTQ-FT or LTQ-ETD mass spectrometry, and (5) enrichment of phosphopeptide methyl esters with IMAC.
16212439	2	51	dep	incubation	393:402	arg1	2					390:390	2	390:390	2	390:390	The strategy includes (1) lower-level, transient transfection of FLAG-GFP-Paxillin into HEK293 cells, (2) incubation of cells with phosphatase inhibitors prior to lysis, (3) purification of paxillin by anti-FLAG immunoprecipitation, (4) analysis of peptides generated from on-beads digestion using LTQ-FT or LTQ-ETD mass spectrometry, and (5) enrichment of phosphopeptide methyl esters with IMAC.
16212439	1	52	theme	simultaneous	134:145	arg1	identification					147:160	the simultaneous identification	130:160	the simultaneous identification of interacting proteins and post-translational modifications of the focal adhesion adapter protein, paxillin,	130:270	Methods for the simultaneous identification of interacting proteins and post-translational modifications of the focal adhesion adapter protein, paxillin, are presented.
16212439	4	53	from	complexes	946:954	arg1	present					920:926	present	920:926	present	920:926	Furthermore, with this method, we simultaneously detect 10 co-purifying proteins which are present in focal adhesion complexes.
16212439	2	54	theme	FLAG-GFP-Paxillin	352:368	arg1	analysis					524:531	(4) analysis	520:531	(4) analysis of peptides generated from on-beads digestion using LTQ-FT or LTQ-ETD mass spectrometry, and (5) enrichment of phosphopeptide methyl esters with IMAC	520:681	The strategy includes (1) lower-level, transient transfection of FLAG-GFP-Paxillin into HEK293 cells, (2) incubation of cells with phosphatase inhibitors prior to lysis, (3) purification of paxillin by anti-FLAG immunoprecipitation, (4) analysis of peptides generated from on-beads digestion using LTQ-FT or LTQ-ETD mass spectrometry, and (5) enrichment of phosphopeptide methyl esters with IMAC.
16212439	2	54	theme	FLAG-GFP-Paxillin	352:368	arg1	purification					461:472	(3) purification	457:472	(3) purification of paxillin by anti-FLAG immunoprecipitation	457:517	The strategy includes (1) lower-level, transient transfection of FLAG-GFP-Paxillin into HEK293 cells, (2) incubation of cells with phosphatase inhibitors prior to lysis, (3) purification of paxillin by anti-FLAG immunoprecipitation, (4) analysis of peptides generated from on-beads digestion using LTQ-FT or LTQ-ETD mass spectrometry, and (5) enrichment of phosphopeptide methyl esters with IMAC.
16212439	2	54	theme	FLAG-GFP-Paxillin	352:368	arg1	incubation					393:402	(2) incubation	389:402	(2) incubation of cells with phosphatase inhibitors prior to lysis	389:454	The strategy includes (1) lower-level, transient transfection of FLAG-GFP-Paxillin into HEK293 cells, (2) incubation of cells with phosphatase inhibitors prior to lysis, (3) purification of paxillin by anti-FLAG immunoprecipitation, (4) analysis of peptides generated from on-beads digestion using LTQ-FT or LTQ-ETD mass spectrometry, and (5) enrichment of phosphopeptide methyl esters with IMAC.
16212439	2	54	theme	FLAG-GFP-Paxillin	352:368	arg1	transfection					336:347	(1) lower-level, transient transfection	309:347	transfection	336:347	The strategy includes (1) lower-level, transient transfection of FLAG-GFP-Paxillin into HEK293 cells, (2) incubation of cells with phosphatase inhibitors prior to lysis, (3) purification of paxillin by anti-FLAG immunoprecipitation, (4) analysis of peptides generated from on-beads digestion using LTQ-FT or LTQ-ETD mass spectrometry, and (5) enrichment of phosphopeptide methyl esters with IMAC.
16212439	0	55	theme	interacting	75:85	arg1	proteins					87:94	interacting proteins	75:94	interacting proteins	75:94	Methods for the detection of paxillin post-translational modifications and interacting proteins by mass spectrometry.
16212439	2	56	theme	prior	441:445	arg1	inhibitors					430:439	phosphatase inhibitors	418:439	phosphatase inhibitors prior to lysis	418:454	The strategy includes (1) lower-level, transient transfection of FLAG-GFP-Paxillin into HEK293 cells, (2) incubation of cells with phosphatase inhibitors prior to lysis, (3) purification of paxillin by anti-FLAG immunoprecipitation, (4) analysis of peptides generated from on-beads digestion using LTQ-FT or LTQ-ETD mass spectrometry, and (5) enrichment of phosphopeptide methyl esters with IMAC.
16212439	2	57	theme	anti-FLAG	489:497	arg1	immunoprecipitation					499:517	anti-FLAG immunoprecipitation	489:517	anti-FLAG immunoprecipitation	489:517	The strategy includes (1) lower-level, transient transfection of FLAG-GFP-Paxillin into HEK293 cells, (2) incubation of cells with phosphatase inhibitors prior to lysis, (3) purification of paxillin by anti-FLAG immunoprecipitation, (4) analysis of peptides generated from on-beads digestion using LTQ-FT or LTQ-ETD mass spectrometry, and (5) enrichment of phosphopeptide methyl esters with IMAC.
16212439	2	58	with	incubation	393:402	arg1	inhibitors					430:439	phosphatase inhibitors	418:439	phosphatase inhibitors prior to lysis	418:454	The strategy includes (1) lower-level, transient transfection of FLAG-GFP-Paxillin into HEK293 cells, (2) incubation of cells with phosphatase inhibitors prior to lysis, (3) purification of paxillin by anti-FLAG immunoprecipitation, (4) analysis of peptides generated from on-beads digestion using LTQ-FT or LTQ-ETD mass spectrometry, and (5) enrichment of phosphopeptide methyl esters with IMAC.
16212439	1	59	theme	interacting	165:175	arg1	proteins					177:184	interacting proteins	165:184	interacting proteins	165:184	Methods for the simultaneous identification of interacting proteins and post-translational modifications of the focal adhesion adapter protein, paxillin, are presented.
16212439	2	60	dep	analysis	524:531	arg1	4					521:521	4	521:521	4	521:521	The strategy includes (1) lower-level, transient transfection of FLAG-GFP-Paxillin into HEK293 cells, (2) incubation of cells with phosphatase inhibitors prior to lysis, (3) purification of paxillin by anti-FLAG immunoprecipitation, (4) analysis of peptides generated from on-beads digestion using LTQ-FT or LTQ-ETD mass spectrometry, and (5) enrichment of phosphopeptide methyl esters with IMAC.
29913562	0	0	theme	secretory	103:111	arg1	pathway					113:119	conventional secretory pathway	90:119	conventional secretory pathway	90:119	O-GlcNAcylation regulates endoplasmic reticulum exit sites through Sec31A modification in conventional secretory pathway.
29913562	6	1	theme	specific	779:786	arg1	complex					801:807	a specific coat-protein complex	777:807	a specific coat-protein complex for anterograde trafficking in the ER-Golgi network	777:859	We report that Sec31A on COPII vesicles, a specific coat-protein complex for anterograde trafficking in the ER-Golgi network, is O-GlcNAcylated on S964, which accelerates COPII vesicle formation through control of its binding affinity to apoptosis-linked gene 2, a calcium-binding protein.
29913562	6	1	theme	specific	779:786	arg1	Sec31A					751:756	Sec31A	751:756	Sec31A on COPII vesicles	751:774	We report that Sec31A on COPII vesicles, a specific coat-protein complex for anterograde trafficking in the ER-Golgi network, is O-GlcNAcylated on S964, which accelerates COPII vesicle formation through control of its binding affinity to apoptosis-linked gene 2, a calcium-binding protein.
29913562	7	2	from	O-GlcNAc	1036:1043	arg1	Sec31A					1048:1053	Sec31A	1048:1053	Sec31A	1048:1053	Together, O-GlcNAc on Sec31A regulates conventional secretory vesicle trafficking in the ER-Golgi network.
29913562	0	3	theme	conventional	90:101	arg1	pathway					113:119	conventional secretory pathway	90:119	conventional secretory pathway	90:119	O-GlcNAcylation regulates endoplasmic reticulum exit sites through Sec31A modification in conventional secretory pathway.
29913562	8	4	theme	vesicle	1170:1176	arg1	formation					1178:1186	COPII vesicle formation	1164:1186	COPII vesicle formation	1164:1186	These modifications accelerate COPII vesicle formation and accelerated anterograde transport of vesicles within the ER-Golgi networks.-Cho, H. J., Mook-Jung, I. O-GlcNAcylation regulates endoplasmic reticulum exit sites through Sec31A modification in conventional secretory pathway.
29913562	8	5	theme	exit	1342:1345	arg1	sites					1347:1351	endoplasmic reticulum exit sites	1320:1351	endoplasmic reticulum exit sites	1320:1351	These modifications accelerate COPII vesicle formation and accelerated anterograde transport of vesicles within the ER-Golgi networks.-Cho, H. J., Mook-Jung, I. O-GlcNAcylation regulates endoplasmic reticulum exit sites through Sec31A modification in conventional secretory pathway.
29913562	4	6	theme	nuclear	581:587	arg1	proteins					605:612	nuclear and cytoplasmic proteins	581:612	nuclear and cytoplasmic proteins	581:612	O-GlcNAcylation ( O-GlcNAc) is a unique protein glycosylation signature, whose dynamic regulation by O-GlcNAc transferase and O-GlcNAcase occurs exclusively for nuclear and cytoplasmic proteins.
29913562	5	7	theme	O-GlcNAc	669:676	arg1	unknown					727:733	unknown	727:733	unknown	727:733	Because of this locally limited property, the role of O-GlcNAc in the conventional protein secretory pathway is unknown.
29913562	5	7	theme	O-GlcNAc	669:676	arg1	role					661:664	the role	657:664	the role of O-GlcNAc in the conventional protein secretory pathway	657:722	Because of this locally limited property, the role of O-GlcNAc in the conventional protein secretory pathway is unknown.
29913562	2	8	theme	appropriate	332:342	arg1	destination					344:354	their appropriate destination	326:354	their appropriate destination	326:354	Newly synthesized membrane and secretory proteins are released from the endoplasmic reticulum (ER) through ER-derived vesicles to their appropriate destination.
29913562	4	9	theme	protein	460:466	arg1	O-GlcNAcylation					420:434	O-GlcNAcylation	420:434	O-GlcNAcylation ( O-GlcNAc)	420:446	O-GlcNAcylation ( O-GlcNAc) is a unique protein glycosylation signature, whose dynamic regulation by O-GlcNAc transferase and O-GlcNAcase occurs exclusively for nuclear and cytoplasmic proteins.
29913562	4	9	theme	protein	460:466	arg1	signature					482:490	a unique protein glycosylation signature	451:490	a unique protein glycosylation signature	451:490	O-GlcNAcylation ( O-GlcNAc) is a unique protein glycosylation signature, whose dynamic regulation by O-GlcNAc transferase and O-GlcNAcase occurs exclusively for nuclear and cytoplasmic proteins.
29913562	3	10	theme	steady	392:397	arg1	trafficking					407:417	steady protein trafficking	392:417	steady protein trafficking	392:417	Vesicle formation is important for steady protein trafficking.
29913562	6	11	theme	affinity	962:969	arg1	control					939:945	control	939:945	control of its binding affinity to apoptosis-linked gene 2, a calcium-binding protein	939:1023	We report that Sec31A on COPII vesicles, a specific coat-protein complex for anterograde trafficking in the ER-Golgi network, is O-GlcNAcylated on S964, which accelerates COPII vesicle formation through control of its binding affinity to apoptosis-linked gene 2, a calcium-binding protein.
29913562	5	12	theme	conventional	685:696	arg1	pathway					716:722	the conventional protein secretory pathway	681:722	the conventional protein secretory pathway	681:722	Because of this locally limited property, the role of O-GlcNAc in the conventional protein secretory pathway is unknown.
29913562	4	13	theme	unique	453:458	arg1	O-GlcNAcylation					420:434	O-GlcNAcylation	420:434	O-GlcNAcylation ( O-GlcNAc)	420:446	O-GlcNAcylation ( O-GlcNAc) is a unique protein glycosylation signature, whose dynamic regulation by O-GlcNAc transferase and O-GlcNAcase occurs exclusively for nuclear and cytoplasmic proteins.
29913562	4	13	theme	unique	453:458	arg1	signature					482:490	a unique protein glycosylation signature	451:490	a unique protein glycosylation signature	451:490	O-GlcNAcylation ( O-GlcNAc) is a unique protein glycosylation signature, whose dynamic regulation by O-GlcNAc transferase and O-GlcNAcase occurs exclusively for nuclear and cytoplasmic proteins.
29913562	8	14	theme	Sec31A	1361:1366	arg1	modification					1368:1379	Sec31A modification	1361:1379	Sec31A modification in conventional secretory pathway	1361:1413	These modifications accelerate COPII vesicle formation and accelerated anterograde transport of vesicles within the ER-Golgi networks.-Cho, H. J., Mook-Jung, I. O-GlcNAcylation regulates endoplasmic reticulum exit sites through Sec31A modification in conventional secretory pathway.
29913562	3	15	theme	protein	399:405	arg1	trafficking					407:417	steady protein trafficking	392:417	steady protein trafficking	392:417	Vesicle formation is important for steady protein trafficking.
29913562	6	16	theme	binding	954:960	arg1	affinity					962:969	its binding affinity	950:969	its binding affinity to apoptosis-linked gene 2, a calcium-binding protein	950:1023	We report that Sec31A on COPII vesicles, a specific coat-protein complex for anterograde trafficking in the ER-Golgi network, is O-GlcNAcylated on S964, which accelerates COPII vesicle formation through control of its binding affinity to apoptosis-linked gene 2, a calcium-binding protein.
29913562	5	17	theme	protein	698:704	arg1	pathway					716:722	the conventional protein secretory pathway	681:722	the conventional protein secretory pathway	681:722	Because of this locally limited property, the role of O-GlcNAc in the conventional protein secretory pathway is unknown.
29913562	5	18	theme	property	647:654	arg1	unknown					727:733	unknown	727:733	unknown	727:733	Because of this locally limited property, the role of O-GlcNAc in the conventional protein secretory pathway is unknown.
29913562	5	18	theme	property	647:654	arg1	role					661:664	the role	657:664	the role of O-GlcNAc in the conventional protein secretory pathway	657:722	Because of this locally limited property, the role of O-GlcNAc in the conventional protein secretory pathway is unknown.
29913562	2	19	theme	ER-derived	303:312	arg1	vesicles					314:321	ER-derived vesicles	303:321	ER-derived vesicles	303:321	Newly synthesized membrane and secretory proteins are released from the endoplasmic reticulum (ER) through ER-derived vesicles to their appropriate destination.
29913562	2	20	attach	released	250:257	arg1	ER					291:292	ER	291:292	ER	291:292	Newly synthesized membrane and secretory proteins are released from the endoplasmic reticulum (ER) through ER-derived vesicles to their appropriate destination.
29913562	2	20	attach	released	250:257	arg2	proteins					237:244	Newly synthesized membrane and secretory proteins	196:244	proteins	237:244	Newly synthesized membrane and secretory proteins are released from the endoplasmic reticulum (ER) through ER-derived vesicles to their appropriate destination.
29913562	2	20	attach	released	250:257	arg1	reticulum					280:288	the endoplasmic reticulum	264:288	the endoplasmic reticulum (ER) through ER-derived vesicles to their appropriate destination	264:354	Newly synthesized membrane and secretory proteins are released from the endoplasmic reticulum (ER) through ER-derived vesicles to their appropriate destination.
29913562	2	20	attach	released	250:257	arg2	membrane					214:221	Newly synthesized membrane and secretory proteins	196:244	membrane	214:221	Newly synthesized membrane and secretory proteins are released from the endoplasmic reticulum (ER) through ER-derived vesicles to their appropriate destination.
29913562	8	21	theme	I.	1291:1292	arg1	O-GlcNAcylation					1294:1308	H. J., Mook-Jung, I. O-GlcNAcylation	1273:1308	H. J., Mook-Jung, I. O-GlcNAcylation	1273:1308	These modifications accelerate COPII vesicle formation and accelerated anterograde transport of vesicles within the ER-Golgi networks.-Cho, H. J., Mook-Jung, I. O-GlcNAcylation regulates endoplasmic reticulum exit sites through Sec31A modification in conventional secretory pathway.
29913562	5	22	theme	secretory	706:714	arg1	pathway					716:722	the conventional protein secretory pathway	681:722	the conventional protein secretory pathway	681:722	Because of this locally limited property, the role of O-GlcNAc in the conventional protein secretory pathway is unknown.
29913562	6	23	theme	COPII	761:765	arg1	vesicles					767:774	COPII vesicles	761:774	COPII vesicles	761:774	We report that Sec31A on COPII vesicles, a specific coat-protein complex for anterograde trafficking in the ER-Golgi network, is O-GlcNAcylated on S964, which accelerates COPII vesicle formation through control of its binding affinity to apoptosis-linked gene 2, a calcium-binding protein.
29913562	6	24	from	trafficking	825:835	arg1	network					853:859	the ER-Golgi network	840:859	the ER-Golgi network	840:859	We report that Sec31A on COPII vesicles, a specific coat-protein complex for anterograde trafficking in the ER-Golgi network, is O-GlcNAcylated on S964, which accelerates COPII vesicle formation through control of its binding affinity to apoptosis-linked gene 2, a calcium-binding protein.
29913562	8	25	theme	accelerated	1192:1202	arg1	transport					1216:1224	accelerated anterograde transport	1192:1224	accelerated anterograde transport	1192:1224	These modifications accelerate COPII vesicle formation and accelerated anterograde transport of vesicles within the ER-Golgi networks.-Cho, H. J., Mook-Jung, I. O-GlcNAcylation regulates endoplasmic reticulum exit sites through Sec31A modification in conventional secretory pathway.
29913562	8	26	theme	COPII	1164:1168	arg1	formation					1178:1186	COPII vesicle formation	1164:1186	COPII vesicle formation	1164:1186	These modifications accelerate COPII vesicle formation and accelerated anterograde transport of vesicles within the ER-Golgi networks.-Cho, H. J., Mook-Jung, I. O-GlcNAcylation regulates endoplasmic reticulum exit sites through Sec31A modification in conventional secretory pathway.
29913562	0	27	theme	reticulum	38:46	arg1	sites					53:57	endoplasmic reticulum exit sites	26:57	endoplasmic reticulum exit sites	26:57	O-GlcNAcylation regulates endoplasmic reticulum exit sites through Sec31A modification in conventional secretory pathway.
29913562	2	28	link	ER-derived	303:312	arg1	vesicles					314:321	ER-derived vesicles	303:321	ER-derived vesicles	303:321	Newly synthesized membrane and secretory proteins are released from the endoplasmic reticulum (ER) through ER-derived vesicles to their appropriate destination.
29913562	6	29	from	Sec31A	751:756	arg1	vesicles					767:774	COPII vesicles	761:774	COPII vesicles	761:774	We report that Sec31A on COPII vesicles, a specific coat-protein complex for anterograde trafficking in the ER-Golgi network, is O-GlcNAcylated on S964, which accelerates COPII vesicle formation through control of its binding affinity to apoptosis-linked gene 2, a calcium-binding protein.
29913562	6	30	theme	ER-Golgi	844:851	arg1	network					853:859	the ER-Golgi network	840:859	the ER-Golgi network	840:859	We report that Sec31A on COPII vesicles, a specific coat-protein complex for anterograde trafficking in the ER-Golgi network, is O-GlcNAcylated on S964, which accelerates COPII vesicle formation through control of its binding affinity to apoptosis-linked gene 2, a calcium-binding protein.
29913562	8	31	theme	secretory	1397:1405	arg1	pathway					1407:1413	conventional secretory pathway	1384:1413	conventional secretory pathway	1384:1413	These modifications accelerate COPII vesicle formation and accelerated anterograde transport of vesicles within the ER-Golgi networks.-Cho, H. J., Mook-Jung, I. O-GlcNAcylation regulates endoplasmic reticulum exit sites through Sec31A modification in conventional secretory pathway.
29913562	0	32	theme	endoplasmic	26:36	arg1	reticulum					38:46	endoplasmic reticulum	26:46	endoplasmic reticulum exit sites	26:57	O-GlcNAcylation regulates endoplasmic reticulum exit sites through Sec31A modification in conventional secretory pathway.
29913562	1	33	theme	conventional	126:137	arg1	indispensable					160:172	indispensable	160:172	indispensable	160:172	The conventional secretory pathway is indispensable for eukaryotic cells.
29913562	1	33	theme	conventional	126:137	arg1	pathway					149:155	The conventional secretory pathway	122:155	The conventional secretory pathway	122:155	The conventional secretory pathway is indispensable for eukaryotic cells.
29913562	8	34	theme	conventional	1384:1395	arg1	pathway					1407:1413	conventional secretory pathway	1384:1413	conventional secretory pathway	1384:1413	These modifications accelerate COPII vesicle formation and accelerated anterograde transport of vesicles within the ER-Golgi networks.-Cho, H. J., Mook-Jung, I. O-GlcNAcylation regulates endoplasmic reticulum exit sites through Sec31A modification in conventional secretory pathway.
29913562	8	35	theme	reticulum	1332:1340	arg1	sites					1347:1351	endoplasmic reticulum exit sites	1320:1351	endoplasmic reticulum exit sites	1320:1351	These modifications accelerate COPII vesicle formation and accelerated anterograde transport of vesicles within the ER-Golgi networks.-Cho, H. J., Mook-Jung, I. O-GlcNAcylation regulates endoplasmic reticulum exit sites through Sec31A modification in conventional secretory pathway.
29913562	5	36	from	role	661:664	arg1	pathway					716:722	the conventional protein secretory pathway	681:722	the conventional protein secretory pathway	681:722	Because of this locally limited property, the role of O-GlcNAc in the conventional protein secretory pathway is unknown.
29913562	8	37	theme	anterograde	1204:1214	arg1	transport					1216:1224	accelerated anterograde transport	1192:1224	accelerated anterograde transport	1192:1224	These modifications accelerate COPII vesicle formation and accelerated anterograde transport of vesicles within the ER-Golgi networks.-Cho, H. J., Mook-Jung, I. O-GlcNAcylation regulates endoplasmic reticulum exit sites through Sec31A modification in conventional secretory pathway.
29913562	4	38	theme	dynamic	499:505	arg1	regulation					507:516	regulation	507:516	regulation	507:516	O-GlcNAcylation ( O-GlcNAc) is a unique protein glycosylation signature, whose dynamic regulation by O-GlcNAc transferase and O-GlcNAcase occurs exclusively for nuclear and cytoplasmic proteins.
29913562	0	39	theme	exit	48:51	arg1	sites					53:57	endoplasmic reticulum exit sites	26:57	endoplasmic reticulum exit sites	26:57	O-GlcNAcylation regulates endoplasmic reticulum exit sites through Sec31A modification in conventional secretory pathway.
29913562	8	40	theme	endoplasmic	1320:1330	arg1	reticulum					1332:1340	endoplasmic reticulum	1320:1340	endoplasmic reticulum exit sites	1320:1351	These modifications accelerate COPII vesicle formation and accelerated anterograde transport of vesicles within the ER-Golgi networks.-Cho, H. J., Mook-Jung, I. O-GlcNAcylation regulates endoplasmic reticulum exit sites through Sec31A modification in conventional secretory pathway.
29913562	2	41	theme	synthesized	202:212	arg1	membrane					214:221	Newly synthesized membrane and secretory proteins	196:244	membrane	214:221	Newly synthesized membrane and secretory proteins are released from the endoplasmic reticulum (ER) through ER-derived vesicles to their appropriate destination.
29913562	2	42	theme	endoplasmic	268:278	arg1	ER					291:292	ER	291:292	ER	291:292	Newly synthesized membrane and secretory proteins are released from the endoplasmic reticulum (ER) through ER-derived vesicles to their appropriate destination.
29913562	2	42	theme	endoplasmic	268:278	arg1	reticulum					280:288	the endoplasmic reticulum	264:288	the endoplasmic reticulum (ER) through ER-derived vesicles to their appropriate destination	264:354	Newly synthesized membrane and secretory proteins are released from the endoplasmic reticulum (ER) through ER-derived vesicles to their appropriate destination.
29913562	0	43	theme	Sec31A	67:72	arg1	modification					74:85	Sec31A modification	67:85	Sec31A modification in conventional secretory pathway	67:119	O-GlcNAcylation regulates endoplasmic reticulum exit sites through Sec31A modification in conventional secretory pathway.
29913562	4	44	theme	cytoplasmic	593:603	arg1	proteins					605:612	nuclear and cytoplasmic proteins	581:612	nuclear and cytoplasmic proteins	581:612	O-GlcNAcylation ( O-GlcNAc) is a unique protein glycosylation signature, whose dynamic regulation by O-GlcNAc transferase and O-GlcNAcase occurs exclusively for nuclear and cytoplasmic proteins.
29913562	0	45	from	modification	74:85	arg1	pathway					113:119	conventional secretory pathway	90:119	conventional secretory pathway	90:119	O-GlcNAcylation regulates endoplasmic reticulum exit sites through Sec31A modification in conventional secretory pathway.
29913562	8	46	from	modification	1368:1379	arg1	pathway					1407:1413	conventional secretory pathway	1384:1413	conventional secretory pathway	1384:1413	These modifications accelerate COPII vesicle formation and accelerated anterograde transport of vesicles within the ER-Golgi networks.-Cho, H. J., Mook-Jung, I. O-GlcNAcylation regulates endoplasmic reticulum exit sites through Sec31A modification in conventional secretory pathway.
29913562	1	47	theme	secretory	139:147	arg1	indispensable					160:172	indispensable	160:172	indispensable	160:172	The conventional secretory pathway is indispensable for eukaryotic cells.
29913562	1	47	theme	secretory	139:147	arg1	pathway					149:155	The conventional secretory pathway	122:155	The conventional secretory pathway	122:155	The conventional secretory pathway is indispensable for eukaryotic cells.
29913562	6	48	theme	apoptosis-linked	974:989	arg1	protein					1017:1023	a calcium-binding protein	999:1023	a calcium-binding protein	999:1023	We report that Sec31A on COPII vesicles, a specific coat-protein complex for anterograde trafficking in the ER-Golgi network, is O-GlcNAcylated on S964, which accelerates COPII vesicle formation through control of its binding affinity to apoptosis-linked gene 2, a calcium-binding protein.
29913562	6	48	theme	apoptosis-linked	974:989	arg1	gene					991:994	apoptosis-linked gene 2	974:996	apoptosis-linked gene 2	974:996	We report that Sec31A on COPII vesicles, a specific coat-protein complex for anterograde trafficking in the ER-Golgi network, is O-GlcNAcylated on S964, which accelerates COPII vesicle formation through control of its binding affinity to apoptosis-linked gene 2, a calcium-binding protein.
29913562	6	49	theme	calcium-binding	1001:1015	arg1	protein					1017:1023	a calcium-binding protein	999:1023	a calcium-binding protein	999:1023	We report that Sec31A on COPII vesicles, a specific coat-protein complex for anterograde trafficking in the ER-Golgi network, is O-GlcNAcylated on S964, which accelerates COPII vesicle formation through control of its binding affinity to apoptosis-linked gene 2, a calcium-binding protein.
29913562	6	49	theme	calcium-binding	1001:1015	arg1	gene					991:994	apoptosis-linked gene 2	974:996	apoptosis-linked gene 2	974:996	We report that Sec31A on COPII vesicles, a specific coat-protein complex for anterograde trafficking in the ER-Golgi network, is O-GlcNAcylated on S964, which accelerates COPII vesicle formation through control of its binding affinity to apoptosis-linked gene 2, a calcium-binding protein.
29913562	3	50	theme	Vesicle	357:363	arg1	formation					365:373	Vesicle formation	357:373	Vesicle formation	357:373	Vesicle formation is important for steady protein trafficking.
29913562	6	51	theme	vesicle	913:919	arg1	formation					921:929	COPII vesicle formation	907:929	COPII vesicle formation	907:929	We report that Sec31A on COPII vesicles, a specific coat-protein complex for anterograde trafficking in the ER-Golgi network, is O-GlcNAcylated on S964, which accelerates COPII vesicle formation through control of its binding affinity to apoptosis-linked gene 2, a calcium-binding protein.
29913562	6	52	theme	COPII	907:911	arg1	formation					921:929	COPII vesicle formation	907:929	COPII vesicle formation	907:929	We report that Sec31A on COPII vesicles, a specific coat-protein complex for anterograde trafficking in the ER-Golgi network, is O-GlcNAcylated on S964, which accelerates COPII vesicle formation through control of its binding affinity to apoptosis-linked gene 2, a calcium-binding protein.
29913562	7	53	theme	vesicle	1088:1094	arg1	trafficking					1096:1106	conventional secretory vesicle trafficking	1065:1106	conventional secretory vesicle trafficking	1065:1106	Together, O-GlcNAc on Sec31A regulates conventional secretory vesicle trafficking in the ER-Golgi network.
29913562	4	54	theme	O-GlcNAc	521:528	arg1	transferase					530:540	O-GlcNAc transferase	521:540	O-GlcNAc transferase	521:540	O-GlcNAcylation ( O-GlcNAc) is a unique protein glycosylation signature, whose dynamic regulation by O-GlcNAc transferase and O-GlcNAcase occurs exclusively for nuclear and cytoplasmic proteins.
29913562	7	55	theme	ER-Golgi	1115:1122	arg1	network					1124:1130	the ER-Golgi network	1111:1130	the ER-Golgi network	1111:1130	Together, O-GlcNAc on Sec31A regulates conventional secretory vesicle trafficking in the ER-Golgi network.
29913562	4	56	theme	glycosylation	468:480	arg1	O-GlcNAcylation					420:434	O-GlcNAcylation	420:434	O-GlcNAcylation ( O-GlcNAc)	420:446	O-GlcNAcylation ( O-GlcNAc) is a unique protein glycosylation signature, whose dynamic regulation by O-GlcNAc transferase and O-GlcNAcase occurs exclusively for nuclear and cytoplasmic proteins.
29913562	4	56	theme	glycosylation	468:480	arg1	signature					482:490	a unique protein glycosylation signature	451:490	a unique protein glycosylation signature	451:490	O-GlcNAcylation ( O-GlcNAc) is a unique protein glycosylation signature, whose dynamic regulation by O-GlcNAc transferase and O-GlcNAcase occurs exclusively for nuclear and cytoplasmic proteins.
29913562	5	57	theme	limited	639:645	arg1	property					647:654	this locally limited property	626:654	this locally limited property	626:654	Because of this locally limited property, the role of O-GlcNAc in the conventional protein secretory pathway is unknown.
29913562	6	58	theme	anterograde	813:823	arg1	trafficking					825:835	anterograde trafficking	813:835	anterograde trafficking in the ER-Golgi network	813:859	We report that Sec31A on COPII vesicles, a specific coat-protein complex for anterograde trafficking in the ER-Golgi network, is O-GlcNAcylated on S964, which accelerates COPII vesicle formation through control of its binding affinity to apoptosis-linked gene 2, a calcium-binding protein.
29913562	7	59	theme	conventional	1065:1076	arg1	trafficking					1096:1106	conventional secretory vesicle trafficking	1065:1106	conventional secretory vesicle trafficking	1065:1106	Together, O-GlcNAc on Sec31A regulates conventional secretory vesicle trafficking in the ER-Golgi network.
29913562	8	60	theme	ER-Golgi	1249:1256	arg1	networks.-Cho					1258:1270	the ER-Golgi networks.-Cho	1245:1270	the ER-Golgi networks.-Cho	1245:1270	These modifications accelerate COPII vesicle formation and accelerated anterograde transport of vesicles within the ER-Golgi networks.-Cho, H. J., Mook-Jung, I. O-GlcNAcylation regulates endoplasmic reticulum exit sites through Sec31A modification in conventional secretory pathway.
29913562	2	61	theme	secretory	227:235	arg1	proteins					237:244	Newly synthesized membrane and secretory proteins	196:244	proteins	237:244	Newly synthesized membrane and secretory proteins are released from the endoplasmic reticulum (ER) through ER-derived vesicles to their appropriate destination.
29913562	7	62	theme	secretory	1078:1086	arg1	trafficking					1096:1106	conventional secretory vesicle trafficking	1065:1106	conventional secretory vesicle trafficking	1065:1106	Together, O-GlcNAc on Sec31A regulates conventional secretory vesicle trafficking in the ER-Golgi network.
29913562	6	63	link	apoptosis-linked	974:989	arg1	protein					1017:1023	a calcium-binding protein	999:1023	a calcium-binding protein	999:1023	We report that Sec31A on COPII vesicles, a specific coat-protein complex for anterograde trafficking in the ER-Golgi network, is O-GlcNAcylated on S964, which accelerates COPII vesicle formation through control of its binding affinity to apoptosis-linked gene 2, a calcium-binding protein.
29913562	6	63	link	apoptosis-linked	974:989	arg1	gene					991:994	apoptosis-linked gene 2	974:996	apoptosis-linked gene 2	974:996	We report that Sec31A on COPII vesicles, a specific coat-protein complex for anterograde trafficking in the ER-Golgi network, is O-GlcNAcylated on S964, which accelerates COPII vesicle formation through control of its binding affinity to apoptosis-linked gene 2, a calcium-binding protein.
29913562	6	64	theme	coat-protein	788:799	arg1	complex					801:807	a specific coat-protein complex	777:807	a specific coat-protein complex for anterograde trafficking in the ER-Golgi network	777:859	We report that Sec31A on COPII vesicles, a specific coat-protein complex for anterograde trafficking in the ER-Golgi network, is O-GlcNAcylated on S964, which accelerates COPII vesicle formation through control of its binding affinity to apoptosis-linked gene 2, a calcium-binding protein.
29913562	6	64	theme	coat-protein	788:799	arg1	Sec31A					751:756	Sec31A	751:756	Sec31A on COPII vesicles	751:774	We report that Sec31A on COPII vesicles, a specific coat-protein complex for anterograde trafficking in the ER-Golgi network, is O-GlcNAcylated on S964, which accelerates COPII vesicle formation through control of its binding affinity to apoptosis-linked gene 2, a calcium-binding protein.
29913562	1	65	theme	eukaryotic	178:187	arg1	cells					189:193	eukaryotic cells	178:193	eukaryotic cells	178:193	The conventional secretory pathway is indispensable for eukaryotic cells.
29913562	8	66	theme	vesicles	1229:1236	arg1	formation					1178:1186	COPII vesicle formation	1164:1186	COPII vesicle formation	1164:1186	These modifications accelerate COPII vesicle formation and accelerated anterograde transport of vesicles within the ER-Golgi networks.-Cho, H. J., Mook-Jung, I. O-GlcNAcylation regulates endoplasmic reticulum exit sites through Sec31A modification in conventional secretory pathway.
29913562	8	66	theme	vesicles	1229:1236	arg1	transport					1216:1224	accelerated anterograde transport	1192:1224	accelerated anterograde transport	1192:1224	These modifications accelerate COPII vesicle formation and accelerated anterograde transport of vesicles within the ER-Golgi networks.-Cho, H. J., Mook-Jung, I. O-GlcNAcylation regulates endoplasmic reticulum exit sites through Sec31A modification in conventional secretory pathway.
23222540	3	0	theme	protein	333:339	arg1	purification					350:361	protein affinity purification	333:361	protein affinity purification	333:361	Using protein affinity purification, here we search for functional partners of TET proteins, and find that TET2 and TET3 associate with O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT), an enzyme that by itself catalyses the addition of O-GlcNAc onto serine and threonine residues (O-GlcNAcylation) in vivo.
23222540	7	1	dep	GlcNAc	1013:1018	arg1	marks					1020:1024	marks	1020:1024	marks in vivo	1020:1032	Downregulation of TET2 reduces the amount of histone 2B Ser 112 GlcNAc marks in vivo, which are associated with gene transcription regulation.
23222540	2	2	theme	gene	291:294	arg1	transcription					296:308	gene transcription	291:308	gene transcription	291:308	However, the molecular mechanism by which TET family enzymes regulate gene transcription remains elusive.
23222540	4	3	theme	chromatin	707:715	arg1	association					717:727	the chromatin association	703:727	the chromatin association of OGT in vivo	703:742	TET2 directly interacts with OGT, which is important for the chromatin association of OGT in vivo.
23222540	9	4	theme	gene	1295:1298	arg1	transcription					1300:1312	gene transcription	1295:1312	gene transcription	1295:1312	The double epigenetic modifications on both DNA and histones by TET2 and OGT coordinate together for the regulation of gene transcription.
23222540	3	5	link	O-linked	463:470	arg1	enzyme					527:532	an enzyme	524:532	an enzyme that by itself catalyses the addition of O-GlcNAc onto serine and threonine residues (O-GlcNAcylation) in vivo	524:643	Using protein affinity purification, here we search for functional partners of TET proteins, and find that TET2 and TET3 associate with O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT), an enzyme that by itself catalyses the addition of O-GlcNAc onto serine and threonine residues (O-GlcNAcylation) in vivo.
23222540	3	5	link	O-linked	463:470	arg1	OGT					518:520	OGT	518:520	OGT	518:520	Using protein affinity purification, here we search for functional partners of TET proteins, and find that TET2 and TET3 associate with O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT), an enzyme that by itself catalyses the addition of O-GlcNAc onto serine and threonine residues (O-GlcNAcylation) in vivo.
23222540	3	5	link	O-linked	463:470	arg1	transferase					505:515	O-linked β-N-acetylglucosamine (O-GlcNAc) transferase	463:515	O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT)	463:521	Using protein affinity purification, here we search for functional partners of TET proteins, and find that TET2 and TET3 associate with O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT), an enzyme that by itself catalyses the addition of O-GlcNAc onto serine and threonine residues (O-GlcNAcylation) in vivo.
23222540	9	6	theme	double	1180:1185	arg1	modifications					1198:1210	The double epigenetic modifications	1176:1210	The double epigenetic modifications on both DNA and histones by TET2 and OGT	1176:1251	The double epigenetic modifications on both DNA and histones by TET2 and OGT coordinate together for the regulation of gene transcription.
23222540	4	7	theme	OGT	732:734	arg1	association					717:727	the chromatin association	703:727	the chromatin association of OGT in vivo	703:742	TET2 directly interacts with OGT, which is important for the chromatin association of OGT in vivo.
23222540	8	8	theme	chromatin	1165:1173	arg1	O-GlcNAcylation					1146:1160	a TET2-dependent O-GlcNAcylation	1129:1160	a TET2-dependent O-GlcNAcylation of chromatin	1129:1173	Taken together, these results reveal a TET2-dependent O-GlcNAcylation of chromatin.
23222540	9	9	theme	transcription	1300:1312	arg1	regulation					1281:1290	the regulation	1277:1290	the regulation of gene transcription	1277:1312	The double epigenetic modifications on both DNA and histones by TET2 and OGT coordinate together for the regulation of gene transcription.
23222540	7	10	theme	transcription	1066:1078	arg1	regulation					1080:1089	gene transcription regulation	1061:1089	gene transcription regulation	1061:1089	Downregulation of TET2 reduces the amount of histone 2B Ser 112 GlcNAc marks in vivo, which are associated with gene transcription regulation.
23222540	3	11	theme	O-linked	463:470	arg1	enzyme					527:532	an enzyme	524:532	an enzyme that by itself catalyses the addition of O-GlcNAc onto serine and threonine residues (O-GlcNAcylation) in vivo	524:643	Using protein affinity purification, here we search for functional partners of TET proteins, and find that TET2 and TET3 associate with O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT), an enzyme that by itself catalyses the addition of O-GlcNAc onto serine and threonine residues (O-GlcNAcylation) in vivo.
23222540	3	11	theme	O-linked	463:470	arg1	OGT					518:520	OGT	518:520	OGT	518:520	Using protein affinity purification, here we search for functional partners of TET proteins, and find that TET2 and TET3 associate with O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT), an enzyme that by itself catalyses the addition of O-GlcNAc onto serine and threonine residues (O-GlcNAcylation) in vivo.
23222540	3	11	theme	O-linked	463:470	arg1	transferase					505:515	O-linked β-N-acetylglucosamine (O-GlcNAc) transferase	463:515	O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT)	463:521	Using protein affinity purification, here we search for functional partners of TET proteins, and find that TET2 and TET3 associate with O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT), an enzyme that by itself catalyses the addition of O-GlcNAc onto serine and threonine residues (O-GlcNAcylation) in vivo.
23222540	1	12	theme	translocation	76:88	arg1	TET3					130:133	TET3	130:133	TET3	130:133	Ten eleven translocation (TET) enzymes, including TET1, TET2 and TET3, convert 5-methylcytosine to 5-hydroxymethylcytosine and regulate gene transcription.
23222540	1	12	theme	translocation	76:88	arg1	TET2					121:124	TET2	121:124	TET2	121:124	Ten eleven translocation (TET) enzymes, including TET1, TET2 and TET3, convert 5-methylcytosine to 5-hydroxymethylcytosine and regulate gene transcription.
23222540	1	12	theme	translocation	76:88	arg1	enzymes					96:102	Ten eleven translocation (TET) enzymes	65:102	Ten eleven translocation (TET) enzymes	65:102	Ten eleven translocation (TET) enzymes, including TET1, TET2 and TET3, convert 5-methylcytosine to 5-hydroxymethylcytosine and regulate gene transcription.
23222540	1	12	theme	translocation	76:88	arg1	TET1					115:118	TET1	115:118	TET1	115:118	Ten eleven translocation (TET) enzymes, including TET1, TET2 and TET3, convert 5-methylcytosine to 5-hydroxymethylcytosine and regulate gene transcription.
23222540	2	13	theme	family	267:272	arg1	enzymes					274:280	TET family enzymes	263:280	TET family enzymes	263:280	However, the molecular mechanism by which TET family enzymes regulate gene transcription remains elusive.
23222540	1	14	theme	TET	91:93	arg1	TET3					130:133	TET3	130:133	TET3	130:133	Ten eleven translocation (TET) enzymes, including TET1, TET2 and TET3, convert 5-methylcytosine to 5-hydroxymethylcytosine and regulate gene transcription.
23222540	1	14	theme	TET	91:93	arg1	TET2					121:124	TET2	121:124	TET2	121:124	Ten eleven translocation (TET) enzymes, including TET1, TET2 and TET3, convert 5-methylcytosine to 5-hydroxymethylcytosine and regulate gene transcription.
23222540	1	14	theme	TET	91:93	arg1	enzymes					96:102	Ten eleven translocation (TET) enzymes	65:102	Ten eleven translocation (TET) enzymes	65:102	Ten eleven translocation (TET) enzymes, including TET1, TET2 and TET3, convert 5-methylcytosine to 5-hydroxymethylcytosine and regulate gene transcription.
23222540	1	14	theme	TET	91:93	arg1	TET1					115:118	TET1	115:118	TET1	115:118	Ten eleven translocation (TET) enzymes, including TET1, TET2 and TET3, convert 5-methylcytosine to 5-hydroxymethylcytosine and regulate gene transcription.
23222540	7	15	theme	gene	1061:1064	arg1	regulation					1080:1089	gene transcription regulation	1061:1089	gene transcription regulation	1061:1089	Downregulation of TET2 reduces the amount of histone 2B Ser 112 GlcNAc marks in vivo, which are associated with gene transcription regulation.
23222540	5	16	theme	OGT-dependent	845:857	arg1	O-GlcNAcylation					867:881	OGT-dependent histone O-GlcNAcylation	845:881	OGT-dependent histone O-GlcNAcylation	845:881	Although this specific interaction does not regulate the enzymatic activity of TET2, it facilitates OGT-dependent histone O-GlcNAcylation.
23222540	9	17	theme	epigenetic	1187:1196	arg1	modifications					1198:1210	The double epigenetic modifications	1176:1210	The double epigenetic modifications on both DNA and histones by TET2 and OGT	1176:1251	The double epigenetic modifications on both DNA and histones by TET2 and OGT coordinate together for the regulation of gene transcription.
23222540	3	18	theme	O-GlcNAc	575:582	arg1	addition					563:570	the addition	559:570	the addition of O-GlcNAc onto serine and threonine residues (O-GlcNAcylation)	559:635	Using protein affinity purification, here we search for functional partners of TET proteins, and find that TET2 and TET3 associate with O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT), an enzyme that by itself catalyses the addition of O-GlcNAc onto serine and threonine residues (O-GlcNAcylation) in vivo.
23222540	3	19	dep	serine	589:594	arg1	residues					610:617	residues	610:617	residues	610:617	Using protein affinity purification, here we search for functional partners of TET proteins, and find that TET2 and TET3 associate with O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT), an enzyme that by itself catalyses the addition of O-GlcNAc onto serine and threonine residues (O-GlcNAcylation) in vivo.
23222540	3	20	theme	functional	383:392	arg1	partners					394:401	functional partners	383:401	functional partners of TET proteins	383:417	Using protein affinity purification, here we search for functional partners of TET proteins, and find that TET2 and TET3 associate with O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT), an enzyme that by itself catalyses the addition of O-GlcNAc onto serine and threonine residues (O-GlcNAcylation) in vivo.
23222540	1	21	theme	gene	201:204	arg1	transcription					206:218	gene transcription	201:218	gene transcription	201:218	Ten eleven translocation (TET) enzymes, including TET1, TET2 and TET3, convert 5-methylcytosine to 5-hydroxymethylcytosine and regulate gene transcription.
23222540	0	22	theme	gene	45:48	arg1	transcription					50:62	gene transcription	45:62	gene transcription	45:62	TET2 promotes histone O-GlcNAcylation during gene transcription.
23222540	2	23	theme	molecular	234:242	arg1	mechanism					244:252	the molecular mechanism	230:252	the molecular mechanism by which TET family enzymes regulate gene transcription	230:308	However, the molecular mechanism by which TET family enzymes regulate gene transcription remains elusive.
23222540	6	24	theme	start	936:940	arg1	sites					942:946	transcription start sites	922:946	transcription start sites	922:946	Moreover, OGT associates with TET2 at transcription start sites.
23222540	7	25	theme	2B	1002:1003	arg1	GlcNAc					1013:1018	histone 2B Ser 112 GlcNAc	994:1018	histone 2B Ser 112 GlcNAc	994:1018	Downregulation of TET2 reduces the amount of histone 2B Ser 112 GlcNAc marks in vivo, which are associated with gene transcription regulation.
23222540	5	26	theme	TET2	824:827	arg1	activity					812:819	the enzymatic activity	798:819	the enzymatic activity of TET2	798:827	Although this specific interaction does not regulate the enzymatic activity of TET2, it facilitates OGT-dependent histone O-GlcNAcylation.
23222540	3	27	theme	TET	406:408	arg1	proteins					410:417	TET proteins	406:417	TET proteins	406:417	Using protein affinity purification, here we search for functional partners of TET proteins, and find that TET2 and TET3 associate with O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT), an enzyme that by itself catalyses the addition of O-GlcNAc onto serine and threonine residues (O-GlcNAcylation) in vivo.
23222540	6	28	theme	transcription	922:934	arg1	sites					942:946	transcription start sites	922:946	transcription start sites	922:946	Moreover, OGT associates with TET2 at transcription start sites.
23222540	3	29	theme	O-GlcNAc	495:502	arg1	enzyme					527:532	an enzyme	524:532	an enzyme that by itself catalyses the addition of O-GlcNAc onto serine and threonine residues (O-GlcNAcylation) in vivo	524:643	Using protein affinity purification, here we search for functional partners of TET proteins, and find that TET2 and TET3 associate with O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT), an enzyme that by itself catalyses the addition of O-GlcNAc onto serine and threonine residues (O-GlcNAcylation) in vivo.
23222540	3	29	theme	O-GlcNAc	495:502	arg1	OGT					518:520	OGT	518:520	OGT	518:520	Using protein affinity purification, here we search for functional partners of TET proteins, and find that TET2 and TET3 associate with O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT), an enzyme that by itself catalyses the addition of O-GlcNAc onto serine and threonine residues (O-GlcNAcylation) in vivo.
23222540	3	29	theme	O-GlcNAc	495:502	arg1	transferase					505:515	O-linked β-N-acetylglucosamine (O-GlcNAc) transferase	463:515	O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT)	463:521	Using protein affinity purification, here we search for functional partners of TET proteins, and find that TET2 and TET3 associate with O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT), an enzyme that by itself catalyses the addition of O-GlcNAc onto serine and threonine residues (O-GlcNAcylation) in vivo.
23222540	3	30	theme	proteins	410:417	arg1	partners					394:401	functional partners	383:401	functional partners of TET proteins	383:417	Using protein affinity purification, here we search for functional partners of TET proteins, and find that TET2 and TET3 associate with O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT), an enzyme that by itself catalyses the addition of O-GlcNAc onto serine and threonine residues (O-GlcNAcylation) in vivo.
23222540	7	31	theme	GlcNAc	1013:1018	arg1	GlcNAc					1013:1018	histone 2B Ser 112 GlcNAc	994:1018	histone 2B Ser 112 GlcNAc	994:1018	Downregulation of TET2 reduces the amount of histone 2B Ser 112 GlcNAc marks in vivo, which are associated with gene transcription regulation.
23222540	7	31	theme	GlcNAc	1013:1018	arg1	amount					984:989	the amount	980:989	the amount of histone 2B Ser 112 GlcNAc marks in vivo, which are associated with gene transcription regulation	980:1089	Downregulation of TET2 reduces the amount of histone 2B Ser 112 GlcNAc marks in vivo, which are associated with gene transcription regulation.
23222540	2	32	theme	TET	263:265	arg1	enzymes					274:280	TET family enzymes	263:280	TET family enzymes	263:280	However, the molecular mechanism by which TET family enzymes regulate gene transcription remains elusive.
23222540	7	33	theme	histone	994:1000	arg1	2B					1002:1003	histone 2B Ser 112	994:1011	histone 2B Ser 112 GlcNAc	994:1018	Downregulation of TET2 reduces the amount of histone 2B Ser 112 GlcNAc marks in vivo, which are associated with gene transcription regulation.
23222540	3	34	theme	β-N-acetylglucosamine	472:492	arg1	enzyme					527:532	an enzyme	524:532	an enzyme that by itself catalyses the addition of O-GlcNAc onto serine and threonine residues (O-GlcNAcylation) in vivo	524:643	Using protein affinity purification, here we search for functional partners of TET proteins, and find that TET2 and TET3 associate with O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT), an enzyme that by itself catalyses the addition of O-GlcNAc onto serine and threonine residues (O-GlcNAcylation) in vivo.
23222540	3	34	theme	β-N-acetylglucosamine	472:492	arg1	OGT					518:520	OGT	518:520	OGT	518:520	Using protein affinity purification, here we search for functional partners of TET proteins, and find that TET2 and TET3 associate with O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT), an enzyme that by itself catalyses the addition of O-GlcNAc onto serine and threonine residues (O-GlcNAcylation) in vivo.
23222540	3	34	theme	β-N-acetylglucosamine	472:492	arg1	transferase					505:515	O-linked β-N-acetylglucosamine (O-GlcNAc) transferase	463:515	O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT)	463:521	Using protein affinity purification, here we search for functional partners of TET proteins, and find that TET2 and TET3 associate with O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT), an enzyme that by itself catalyses the addition of O-GlcNAc onto serine and threonine residues (O-GlcNAcylation) in vivo.
23222540	9	35	from	modifications	1198:1210	arg1	histones					1228:1235	histones	1228:1235	histones	1228:1235	The double epigenetic modifications on both DNA and histones by TET2 and OGT coordinate together for the regulation of gene transcription.
23222540	9	35	from	modifications	1198:1210	arg1	DNA					1220:1222	DNA	1220:1222	DNA	1220:1222	The double epigenetic modifications on both DNA and histones by TET2 and OGT coordinate together for the regulation of gene transcription.
23222540	3	36	theme	affinity	341:348	arg1	purification					350:361	protein affinity purification	333:361	protein affinity purification	333:361	Using protein affinity purification, here we search for functional partners of TET proteins, and find that TET2 and TET3 associate with O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT), an enzyme that by itself catalyses the addition of O-GlcNAc onto serine and threonine residues (O-GlcNAcylation) in vivo.
23222540	5	37	theme	enzymatic	802:810	arg1	activity					812:819	the enzymatic activity	798:819	the enzymatic activity of TET2	798:827	Although this specific interaction does not regulate the enzymatic activity of TET2, it facilitates OGT-dependent histone O-GlcNAcylation.
23222540	5	38	theme	histone	859:865	arg1	O-GlcNAcylation					867:881	OGT-dependent histone O-GlcNAcylation	845:881	OGT-dependent histone O-GlcNAcylation	845:881	Although this specific interaction does not regulate the enzymatic activity of TET2, it facilitates OGT-dependent histone O-GlcNAcylation.
23222540	5	39	theme	specific	759:766	arg1	interaction					768:778	this specific interaction	754:778	this specific interaction	754:778	Although this specific interaction does not regulate the enzymatic activity of TET2, it facilitates OGT-dependent histone O-GlcNAcylation.
23222540	0	40	theme	histone	14:20	arg1	O-GlcNAcylation					22:36	histone O-GlcNAcylation	14:36	histone O-GlcNAcylation	14:36	TET2 promotes histone O-GlcNAcylation during gene transcription.
23222540	7	41	theme	TET2	967:970	arg1	Downregulation					949:962	Downregulation	949:962	Downregulation of TET2	949:970	Downregulation of TET2 reduces the amount of histone 2B Ser 112 GlcNAc marks in vivo, which are associated with gene transcription regulation.
23222540	8	42	theme	TET2-dependent	1131:1144	arg1	O-GlcNAcylation					1146:1160	a TET2-dependent O-GlcNAcylation	1129:1160	a TET2-dependent O-GlcNAcylation of chromatin	1129:1173	Taken together, these results reveal a TET2-dependent O-GlcNAcylation of chromatin.
12956774	5	0	theme	C195	1041:1044	arg1	Mutations					1003:1011	Mutations	1003:1011	Mutations of C51 (ECD1), C129 (ECD2), C195 (ECD3) and C276 (ECD4	1003:1066	Mutations of C51 (ECD1), C129 (ECD2), C195 (ECD3) and C276 (ECD4 severely reduced anti-Fy3 and CXC-chemokine ligand 8 (CXCL-8) binding.
12956774	1	1	theme	Duffy	165:169	arg1	receptor					332:339	a widely expressed promiscuous chemokine receptor	291:339	a widely expressed promiscuous chemokine receptor	291:339	The Duffy antigen/receptor for chemokines (DARC), a seven-transmembrane glycoprotein carrying the Duffy (Fy) blood group, acts as a widely expressed promiscuous chemokine receptor.
12956774	1	1	theme	Duffy	165:169	arg1	antigen/receptor					171:186	The Duffy antigen/receptor	161:186	The Duffy antigen/receptor for chemokines (DARC), a seven-transmembrane glycoprotein carrying the Duffy (Fy) blood group,	161:281	The Duffy antigen/receptor for chemokines (DARC), a seven-transmembrane glycoprotein carrying the Duffy (Fy) blood group, acts as a widely expressed promiscuous chemokine receptor.
12956774	6	2	theme	D283	1225:1228	arg1	mutations					1176:1184	mutations	1176:1184	mutations of F22-E23, P50 (ECD1) and D263, R267, D283 (ECD4)	1176:1235	CXCL-8 binding was also abrogated by mutations of F22-E23, P50 (ECD1) and D263, R267, D283 (ECD4).
12956774	7	3	dep	ECDs	1429:1432	arg1	1-4					1434:1436	1-4	1434:1436	1-4	1434:1436	These results defined the Fya epitope and suggested that (1) two disulphide bridges are involved in the creation of an active chemokine binding pocket; (2) a limited number of amino acids in ECDs 1-4 participate in CXCL-8 binding; and (3) Fy3 is a conformation-dependent epitope involving all ECDs.
12956774	7	4	from	number	1404:1409	arg1	ECDs					1429:1432	ECDs 1-4	1429:1436	ECDs 1-4	1429:1436	These results defined the Fya epitope and suggested that (1) two disulphide bridges are involved in the creation of an active chemokine binding pocket; (2) a limited number of amino acids in ECDs 1-4 participate in CXCL-8 binding; and (3) Fy3 is a conformation-dependent epitope involving all ECDs.
12956774	5	5	theme	ECD4	1063:1066	arg1	Mutations					1003:1011	Mutations	1003:1011	Mutations of C51 (ECD1), C129 (ECD2), C195 (ECD3) and C276 (ECD4	1003:1066	Mutations of C51 (ECD1), C129 (ECD2), C195 (ECD3) and C276 (ECD4 severely reduced anti-Fy3 and CXC-chemokine ligand 8 (CXCL-8) binding.
12956774	1	6	theme	Fy	266:267	arg1	group					276:280	the Duffy (Fy) blood group	255:280	the Duffy (Fy) blood group	255:280	The Duffy antigen/receptor for chemokines (DARC), a seven-transmembrane glycoprotein carrying the Duffy (Fy) blood group, acts as a widely expressed promiscuous chemokine receptor.
12956774	2	7	theme	alanine	506:512	arg1	substitutions					514:526	alanine substitutions	506:526	alanine substitutions spread out on the four extracellular domains (ECDs)	506:578	In a structure-function study, we analysed the binding of chemokines and anti-Fy monoclonal antibodies (mAbs) to K562 cells expressing 39 mutant forms of DARC with alanine substitutions spread out on the four extracellular domains (ECDs).
12956774	1	8	gly	glycoprotein	233:244	arg1	glycoprotein					233:244	a seven-transmembrane glycoprotein	211:244	a seven-transmembrane glycoprotein carrying the Duffy (Fy) blood group	211:280	The Duffy antigen/receptor for chemokines (DARC), a seven-transmembrane glycoprotein carrying the Duffy (Fy) blood group, acts as a widely expressed promiscuous chemokine receptor.
12956774	1	8	gly	glycoprotein	233:244	arg1	chemokines					192:201	chemokines	192:201	chemokines (DARC)	192:208	The Duffy antigen/receptor for chemokines (DARC), a seven-transmembrane glycoprotein carrying the Duffy (Fy) blood group, acts as a widely expressed promiscuous chemokine receptor.
12956774	0	9	dep	antibody	123:130	arg1	sites					154:158	binding sites	146:158	binding sites	146:158	Structure-function analysis of the extracellular domains of the Duffy antigen/receptor for chemokines: characterization of antibody and chemokine binding sites.
12956774	7	10	theme	amino	1414:1418	arg1	acids					1420:1424	amino acids	1414:1424	amino acids in ECDs 1-4	1414:1436	These results defined the Fya epitope and suggested that (1) two disulphide bridges are involved in the creation of an active chemokine binding pocket; (2) a limited number of amino acids in ECDs 1-4 participate in CXCL-8 binding; and (3) Fy3 is a conformation-dependent epitope involving all ECDs.
12956774	3	11	theme	Fya	685:687	arg1	41-YGANLE-46					720:731	the linear sequence 41-YGANLE-46	700:731	the linear sequence 41-YGANLE-46	700:731	Using synthetic peptides, we defined previously the Fy6 epitope (22-FEDVW-26), and we characterized the Fya epitope as the linear sequence 41-YGANLE-46.
12956774	3	11	theme	Fya	685:687	arg1	epitope					689:695	the Fya epitope	681:695	the Fya epitope	681:695	Using synthetic peptides, we defined previously the Fy6 epitope (22-FEDVW-26), and we characterized the Fya epitope as the linear sequence 41-YGANLE-46.
12956774	2	12	theme	structure-function	347:364	arg1	study					366:370	a structure-function study	345:370	a structure-function study	345:370	In a structure-function study, we analysed the binding of chemokines and anti-Fy monoclonal antibodies (mAbs) to K562 cells expressing 39 mutant forms of DARC with alanine substitutions spread out on the four extracellular domains (ECDs).
12956774	4	13	theme	Anti-Fy3	904:911	arg1	binding					913:919	Anti-Fy3 binding	904:919	Anti-Fy3 binding	904:919	In agreement with these results, mutations of F22-E23, V25 and Y41, G42, N44, L45 on ECD1 abolished the binding of anti-Fy6 and anti-Fya mAbs to K562 cells respectively, Anti-Fy3 binding was abolished by D58-D59 (ECD1), R124 (ECD2), D263 and D283 (ECD4) substitutions.
12956774	1	14	theme	blood	270:274	arg1	group					276:280	the Duffy (Fy) blood group	255:280	the Duffy (Fy) blood group	255:280	The Duffy antigen/receptor for chemokines (DARC), a seven-transmembrane glycoprotein carrying the Duffy (Fy) blood group, acts as a widely expressed promiscuous chemokine receptor.
12956774	0	15	theme	antibody	123:130	arg1	characterization					103:118	characterization	103:118	Structure-function analysis of the extracellular domains of the Duffy antigen/receptor for chemokines: characterization of antibody and chemokine binding sites.	0:159	Structure-function analysis of the extracellular domains of the Duffy antigen/receptor for chemokines: characterization of antibody and chemokine binding sites.
12956774	7	16	theme	limited	1396:1402	arg1	number					1404:1409	a limited number	1394:1409	a limited number of amino acids in ECDs 1-4	1394:1436	These results defined the Fya epitope and suggested that (1) two disulphide bridges are involved in the creation of an active chemokine binding pocket; (2) a limited number of amino acids in ECDs 1-4 participate in CXCL-8 binding; and (3) Fy3 is a conformation-dependent epitope involving all ECDs.
12956774	7	17	from	acids	1420:1424	arg1	ECDs					1429:1432	ECDs 1-4	1429:1436	ECDs 1-4	1429:1436	These results defined the Fya epitope and suggested that (1) two disulphide bridges are involved in the creation of an active chemokine binding pocket; (2) a limited number of amino acids in ECDs 1-4 participate in CXCL-8 binding; and (3) Fy3 is a conformation-dependent epitope involving all ECDs.
12956774	4	18	theme	mAbs	871:874	arg1	binding					838:844	the binding	834:844	the binding of anti-Fy6 and anti-Fya mAbs to K562 cells	834:888	In agreement with these results, mutations of F22-E23, V25 and Y41, G42, N44, L45 on ECD1 abolished the binding of anti-Fy6 and anti-Fya mAbs to K562 cells respectively, Anti-Fy3 binding was abolished by D58-D59 (ECD1), R124 (ECD2), D263 and D283 (ECD4) substitutions.
12956774	6	19	theme	CXCL-8	1139:1144	arg1	binding					1146:1152	CXCL-8 binding	1139:1152	CXCL-8 binding	1139:1152	CXCL-8 binding was also abrogated by mutations of F22-E23, P50 (ECD1) and D263, R267, D283 (ECD4).
12956774	2	20	theme	DARC	496:499	arg1	forms					487:491	39 mutant forms	477:491	39 mutant forms of DARC	477:499	In a structure-function study, we analysed the binding of chemokines and anti-Fy monoclonal antibodies (mAbs) to K562 cells expressing 39 mutant forms of DARC with alanine substitutions spread out on the four extracellular domains (ECDs).
12956774	5	21	theme	C51	1016:1018	arg1	Mutations					1003:1011	Mutations	1003:1011	Mutations of C51 (ECD1), C129 (ECD2), C195 (ECD3) and C276 (ECD4	1003:1066	Mutations of C51 (ECD1), C129 (ECD2), C195 (ECD3) and C276 (ECD4 severely reduced anti-Fy3 and CXC-chemokine ligand 8 (CXCL-8) binding.
12956774	4	22	with	agreement	737:745	arg1	results					758:764	these results	752:764	these results	752:764	In agreement with these results, mutations of F22-E23, V25 and Y41, G42, N44, L45 on ECD1 abolished the binding of anti-Fy6 and anti-Fya mAbs to K562 cells respectively, Anti-Fy3 binding was abolished by D58-D59 (ECD1), R124 (ECD2), D263 and D283 (ECD4) substitutions.
12956774	7	23	from	ECDs	1429:1432	arg1	number					1404:1409	a limited number	1394:1409	a limited number of amino acids in ECDs 1-4	1394:1436	These results defined the Fya epitope and suggested that (1) two disulphide bridges are involved in the creation of an active chemokine binding pocket; (2) a limited number of amino acids in ECDs 1-4 participate in CXCL-8 binding; and (3) Fy3 is a conformation-dependent epitope involving all ECDs.
12956774	4	24	dep	ECD2	960:963	arg1	substitutions					988:1000	substitutions	988:1000	substitutions	988:1000	In agreement with these results, mutations of F22-E23, V25 and Y41, G42, N44, L45 on ECD1 abolished the binding of anti-Fy6 and anti-Fya mAbs to K562 cells respectively, Anti-Fy3 binding was abolished by D58-D59 (ECD1), R124 (ECD2), D263 and D283 (ECD4) substitutions.
12956774	0	25	theme	Structure-function	0:17	arg1	analysis					19:26	Structure-function analysis	0:26	Structure-function analysis of the extracellular domains of the Duffy antigen/receptor for chemokines: characterization of antibody and chemokine binding sites.	0:159	Structure-function analysis of the extracellular domains of the Duffy antigen/receptor for chemokines: characterization of antibody and chemokine binding sites.
12956774	3	26	theme	linear	704:709	arg1	41-YGANLE-46					720:731	the linear sequence 41-YGANLE-46	700:731	the linear sequence 41-YGANLE-46	700:731	Using synthetic peptides, we defined previously the Fy6 epitope (22-FEDVW-26), and we characterized the Fya epitope as the linear sequence 41-YGANLE-46.
12956774	3	26	theme	linear	704:709	arg1	epitope					689:695	the Fya epitope	681:695	the Fya epitope	681:695	Using synthetic peptides, we defined previously the Fy6 epitope (22-FEDVW-26), and we characterized the Fya epitope as the linear sequence 41-YGANLE-46.
12956774	8	27	theme	DARC	1576:1579	arg1	N-glycosylation					1557:1571	N-glycosylation	1557:1571	N-glycosylation of DARC	1557:1579	We also showed that N-glycosylation of DARC occurred on N16SS and did not influence antibody and chemokine binding.
12956774	7	28	theme	CXCL-8	1453:1458	arg1	binding					1460:1466	CXCL-8 binding	1453:1466	CXCL-8 binding	1453:1466	These results defined the Fya epitope and suggested that (1) two disulphide bridges are involved in the creation of an active chemokine binding pocket; (2) a limited number of amino acids in ECDs 1-4 participate in CXCL-8 binding; and (3) Fy3 is a conformation-dependent epitope involving all ECDs.
12956774	5	29	theme	ligand	1112:1117	arg1	binding					1130:1136	CXC-chemokine ligand 8 (CXCL-8) binding	1098:1136	CXC-chemokine ligand 8 (CXCL-8) binding	1098:1136	Mutations of C51 (ECD1), C129 (ECD2), C195 (ECD3) and C276 (ECD4 severely reduced anti-Fy3 and CXC-chemokine ligand 8 (CXCL-8) binding.
12956774	8	30	theme	chemokine	1634:1642	arg1	binding					1644:1650	chemokine binding	1634:1650	chemokine binding	1634:1650	We also showed that N-glycosylation of DARC occurred on N16SS and did not influence antibody and chemokine binding.
12956774	2	31	theme	antibodies	434:443	arg1	binding					389:395	the binding	385:395	the binding of chemokines and anti-Fy monoclonal antibodies (mAbs) to K562 cells expressing 39 mutant forms of DARC with alanine substitutions spread out on the four extracellular domains (ECDs)	385:578	In a structure-function study, we analysed the binding of chemokines and anti-Fy monoclonal antibodies (mAbs) to K562 cells expressing 39 mutant forms of DARC with alanine substitutions spread out on the four extracellular domains (ECDs).
12956774	3	32	theme	sequence	711:718	arg1	41-YGANLE-46					720:731	the linear sequence 41-YGANLE-46	700:731	the linear sequence 41-YGANLE-46	700:731	Using synthetic peptides, we defined previously the Fy6 epitope (22-FEDVW-26), and we characterized the Fya epitope as the linear sequence 41-YGANLE-46.
12956774	3	32	theme	sequence	711:718	arg1	epitope					689:695	the Fya epitope	681:695	the Fya epitope	681:695	Using synthetic peptides, we defined previously the Fy6 epitope (22-FEDVW-26), and we characterized the Fya epitope as the linear sequence 41-YGANLE-46.
12956774	0	33	theme	chemokine	136:144	arg1	characterization					103:118	characterization	103:118	Structure-function analysis of the extracellular domains of the Duffy antigen/receptor for chemokines: characterization of antibody and chemokine binding sites.	0:159	Structure-function analysis of the extracellular domains of the Duffy antigen/receptor for chemokines: characterization of antibody and chemokine binding sites.
12956774	4	34	theme	F22-E23	780:786	arg1	mutations					767:775	mutations	767:775	mutations of F22-E23, V25 and Y41, G42, N44, L45 on ECD1	767:822	In agreement with these results, mutations of F22-E23, V25 and Y41, G42, N44, L45 on ECD1 abolished the binding of anti-Fy6 and anti-Fya mAbs to K562 cells respectively, Anti-Fy3 binding was abolished by D58-D59 (ECD1), R124 (ECD2), D263 and D283 (ECD4) substitutions.
12956774	2	35	theme	anti-Fy	415:421	arg1	mAbs					446:449	mAbs	446:449	mAbs	446:449	In a structure-function study, we analysed the binding of chemokines and anti-Fy monoclonal antibodies (mAbs) to K562 cells expressing 39 mutant forms of DARC with alanine substitutions spread out on the four extracellular domains (ECDs).
12956774	2	35	theme	anti-Fy	415:421	arg1	antibodies					434:443	anti-Fy monoclonal antibodies	415:443	anti-Fy monoclonal antibodies (mAbs)	415:450	In a structure-function study, we analysed the binding of chemokines and anti-Fy monoclonal antibodies (mAbs) to K562 cells expressing 39 mutant forms of DARC with alanine substitutions spread out on the four extracellular domains (ECDs).
12956774	2	36	theme	monoclonal	423:432	arg1	mAbs					446:449	mAbs	446:449	mAbs	446:449	In a structure-function study, we analysed the binding of chemokines and anti-Fy monoclonal antibodies (mAbs) to K562 cells expressing 39 mutant forms of DARC with alanine substitutions spread out on the four extracellular domains (ECDs).
12956774	2	36	theme	monoclonal	423:432	arg1	antibodies					434:443	anti-Fy monoclonal antibodies	415:443	anti-Fy monoclonal antibodies (mAbs)	415:450	In a structure-function study, we analysed the binding of chemokines and anti-Fy monoclonal antibodies (mAbs) to K562 cells expressing 39 mutant forms of DARC with alanine substitutions spread out on the four extracellular domains (ECDs).
12956774	5	37	theme	C129	1028:1031	arg1	Mutations					1003:1011	Mutations	1003:1011	Mutations of C51 (ECD1), C129 (ECD2), C195 (ECD3) and C276 (ECD4	1003:1066	Mutations of C51 (ECD1), C129 (ECD2), C195 (ECD3) and C276 (ECD4 severely reduced anti-Fy3 and CXC-chemokine ligand 8 (CXCL-8) binding.
12956774	7	38	theme	pocket	1382:1387	arg1	creation					1342:1349	the creation	1338:1349	the creation of an active chemokine binding pocket	1338:1387	These results defined the Fya epitope and suggested that (1) two disulphide bridges are involved in the creation of an active chemokine binding pocket; (2) a limited number of amino acids in ECDs 1-4 participate in CXCL-8 binding; and (3) Fy3 is a conformation-dependent epitope involving all ECDs.
12956774	0	39	theme	domains	49:55	arg1	analysis					19:26	Structure-function analysis	0:26	Structure-function analysis of the extracellular domains of the Duffy antigen/receptor for chemokines: characterization of antibody and chemokine binding sites.	0:159	Structure-function analysis of the extracellular domains of the Duffy antigen/receptor for chemokines: characterization of antibody and chemokine binding sites.
12956774	7	40	theme	active	1357:1362	arg1	pocket					1382:1387	an active chemokine binding pocket	1354:1387	an active chemokine binding pocket	1354:1387	These results defined the Fya epitope and suggested that (1) two disulphide bridges are involved in the creation of an active chemokine binding pocket; (2) a limited number of amino acids in ECDs 1-4 participate in CXCL-8 binding; and (3) Fy3 is a conformation-dependent epitope involving all ECDs.
12956774	4	41	theme	anti-Fy6	849:856	arg1	mAbs					871:874	anti-Fy6 and anti-Fya mAbs	849:874	anti-Fy6 and anti-Fya mAbs	849:874	In agreement with these results, mutations of F22-E23, V25 and Y41, G42, N44, L45 on ECD1 abolished the binding of anti-Fy6 and anti-Fya mAbs to K562 cells respectively, Anti-Fy3 binding was abolished by D58-D59 (ECD1), R124 (ECD2), D263 and D283 (ECD4) substitutions.
12956774	7	42	dep	Fy3	1477:1479	arg1	3					1474:1474	3	1474:1474	3	1474:1474	These results defined the Fya epitope and suggested that (1) two disulphide bridges are involved in the creation of an active chemokine binding pocket; (2) a limited number of amino acids in ECDs 1-4 participate in CXCL-8 binding; and (3) Fy3 is a conformation-dependent epitope involving all ECDs.
12956774	2	43	theme	chemokines	400:409	arg1	binding					389:395	the binding	385:395	the binding of chemokines and anti-Fy monoclonal antibodies (mAbs) to K562 cells expressing 39 mutant forms of DARC with alanine substitutions spread out on the four extracellular domains (ECDs)	385:578	In a structure-function study, we analysed the binding of chemokines and anti-Fy monoclonal antibodies (mAbs) to K562 cells expressing 39 mutant forms of DARC with alanine substitutions spread out on the four extracellular domains (ECDs).
12956774	2	44	theme	K562	455:458	arg1	cells					460:464	K562 cells	455:464	K562 cells expressing 39 mutant forms of DARC with alanine substitutions spread out on the four extracellular domains (ECDs)	455:578	In a structure-function study, we analysed the binding of chemokines and anti-Fy monoclonal antibodies (mAbs) to K562 cells expressing 39 mutant forms of DARC with alanine substitutions spread out on the four extracellular domains (ECDs).
12956774	0	45	theme	extracellular	35:47	arg1	domains					49:55	the extracellular domains	31:55	the extracellular domains of the Duffy antigen/receptor for chemokines	31:100	Structure-function analysis of the extracellular domains of the Duffy antigen/receptor for chemokines: characterization of antibody and chemokine binding sites.
12956774	0	45	theme	extracellular	35:47	arg1	antigen/receptor					70:85	the Duffy antigen/receptor	60:85	the Duffy antigen/receptor for chemokines	60:100	Structure-function analysis of the extracellular domains of the Duffy antigen/receptor for chemokines: characterization of antibody and chemokine binding sites.
12956774	7	46	theme	binding	1374:1380	arg1	pocket					1382:1387	an active chemokine binding pocket	1354:1387	an active chemokine binding pocket	1354:1387	These results defined the Fya epitope and suggested that (1) two disulphide bridges are involved in the creation of an active chemokine binding pocket; (2) a limited number of amino acids in ECDs 1-4 participate in CXCL-8 binding; and (3) Fy3 is a conformation-dependent epitope involving all ECDs.
12956774	1	47	theme	seven-transmembrane	213:231	arg1	glycoprotein					233:244	a seven-transmembrane glycoprotein	211:244	a seven-transmembrane glycoprotein carrying the Duffy (Fy) blood group	211:280	The Duffy antigen/receptor for chemokines (DARC), a seven-transmembrane glycoprotein carrying the Duffy (Fy) blood group, acts as a widely expressed promiscuous chemokine receptor.
12956774	1	47	theme	seven-transmembrane	213:231	arg1	chemokines					192:201	chemokines	192:201	chemokines (DARC)	192:208	The Duffy antigen/receptor for chemokines (DARC), a seven-transmembrane glycoprotein carrying the Duffy (Fy) blood group, acts as a widely expressed promiscuous chemokine receptor.
12956774	6	48	theme	P50	1198:1200	arg1	mutations					1176:1184	mutations	1176:1184	mutations of F22-E23, P50 (ECD1) and D263, R267, D283 (ECD4)	1176:1235	CXCL-8 binding was also abrogated by mutations of F22-E23, P50 (ECD1) and D263, R267, D283 (ECD4).
12956774	4	49	theme	anti-Fya	862:869	arg1	mAbs					871:874	anti-Fy6 and anti-Fya mAbs	849:874	anti-Fy6 and anti-Fya mAbs	849:874	In agreement with these results, mutations of F22-E23, V25 and Y41, G42, N44, L45 on ECD1 abolished the binding of anti-Fy6 and anti-Fya mAbs to K562 cells respectively, Anti-Fy3 binding was abolished by D58-D59 (ECD1), R124 (ECD2), D263 and D283 (ECD4) substitutions.
12956774	2	50	theme	mutant	480:485	arg1	forms					487:491	39 mutant forms	477:491	39 mutant forms of DARC	477:499	In a structure-function study, we analysed the binding of chemokines and anti-Fy monoclonal antibodies (mAbs) to K562 cells expressing 39 mutant forms of DARC with alanine substitutions spread out on the four extracellular domains (ECDs).
12956774	1	51	contain	carrying	246:253	arg2	group					276:280	the Duffy (Fy) blood group	255:280	the Duffy (Fy) blood group	255:280	The Duffy antigen/receptor for chemokines (DARC), a seven-transmembrane glycoprotein carrying the Duffy (Fy) blood group, acts as a widely expressed promiscuous chemokine receptor.
12956774	1	51	contain	carrying	246:253	arg1	glycoprotein					233:244	a seven-transmembrane glycoprotein	211:244	a seven-transmembrane glycoprotein carrying the Duffy (Fy) blood group	211:280	The Duffy antigen/receptor for chemokines (DARC), a seven-transmembrane glycoprotein carrying the Duffy (Fy) blood group, acts as a widely expressed promiscuous chemokine receptor.
12956774	1	51	contain	carrying	246:253	arg1	chemokines					192:201	chemokines	192:201	chemokines (DARC)	192:208	The Duffy antigen/receptor for chemokines (DARC), a seven-transmembrane glycoprotein carrying the Duffy (Fy) blood group, acts as a widely expressed promiscuous chemokine receptor.
12956774	0	52	theme	binding	146:152	arg1	sites					154:158	binding sites	146:158	binding sites	146:158	Structure-function analysis of the extracellular domains of the Duffy antigen/receptor for chemokines: characterization of antibody and chemokine binding sites.
12956774	1	53	theme	expressed	300:308	arg1	receptor					332:339	a widely expressed promiscuous chemokine receptor	291:339	a widely expressed promiscuous chemokine receptor	291:339	The Duffy antigen/receptor for chemokines (DARC), a seven-transmembrane glycoprotein carrying the Duffy (Fy) blood group, acts as a widely expressed promiscuous chemokine receptor.
12956774	1	53	theme	expressed	300:308	arg1	antigen/receptor					171:186	The Duffy antigen/receptor	161:186	The Duffy antigen/receptor for chemokines (DARC), a seven-transmembrane glycoprotein carrying the Duffy (Fy) blood group,	161:281	The Duffy antigen/receptor for chemokines (DARC), a seven-transmembrane glycoprotein carrying the Duffy (Fy) blood group, acts as a widely expressed promiscuous chemokine receptor.
12956774	2	54	theme	extracellular	551:563	arg1	ECDs					574:577	ECDs	574:577	ECDs	574:577	In a structure-function study, we analysed the binding of chemokines and anti-Fy monoclonal antibodies (mAbs) to K562 cells expressing 39 mutant forms of DARC with alanine substitutions spread out on the four extracellular domains (ECDs).
12956774	2	54	theme	extracellular	551:563	arg1	domains					565:571	the four extracellular domains	542:571	the four extracellular domains (ECDs)	542:578	In a structure-function study, we analysed the binding of chemokines and anti-Fy monoclonal antibodies (mAbs) to K562 cells expressing 39 mutant forms of DARC with alanine substitutions spread out on the four extracellular domains (ECDs).
12956774	4	55	theme	K562	879:882	arg1	cells					884:888	K562 cells	879:888	K562 cells	879:888	In agreement with these results, mutations of F22-E23, V25 and Y41, G42, N44, L45 on ECD1 abolished the binding of anti-Fy6 and anti-Fya mAbs to K562 cells respectively, Anti-Fy3 binding was abolished by D58-D59 (ECD1), R124 (ECD2), D263 and D283 (ECD4) substitutions.
12956774	1	56	theme	promiscuous	310:320	arg1	receptor					332:339	a widely expressed promiscuous chemokine receptor	291:339	a widely expressed promiscuous chemokine receptor	291:339	The Duffy antigen/receptor for chemokines (DARC), a seven-transmembrane glycoprotein carrying the Duffy (Fy) blood group, acts as a widely expressed promiscuous chemokine receptor.
12956774	1	56	theme	promiscuous	310:320	arg1	antigen/receptor					171:186	The Duffy antigen/receptor	161:186	The Duffy antigen/receptor for chemokines (DARC), a seven-transmembrane glycoprotein carrying the Duffy (Fy) blood group,	161:281	The Duffy antigen/receptor for chemokines (DARC), a seven-transmembrane glycoprotein carrying the Duffy (Fy) blood group, acts as a widely expressed promiscuous chemokine receptor.
12956774	7	57	theme	Fya	1264:1266	arg1	epitope					1268:1274	the Fya epitope	1260:1274	the Fya epitope	1260:1274	These results defined the Fya epitope and suggested that (1) two disulphide bridges are involved in the creation of an active chemokine binding pocket; (2) a limited number of amino acids in ECDs 1-4 participate in CXCL-8 binding; and (3) Fy3 is a conformation-dependent epitope involving all ECDs.
12956774	4	58	from	mutations	767:775	arg1	ECD1					819:822	ECD1	819:822	ECD1	819:822	In agreement with these results, mutations of F22-E23, V25 and Y41, G42, N44, L45 on ECD1 abolished the binding of anti-Fy6 and anti-Fya mAbs to K562 cells respectively, Anti-Fy3 binding was abolished by D58-D59 (ECD1), R124 (ECD2), D263 and D283 (ECD4) substitutions.
12956774	7	59	dep	involved	1326:1333	arg1	2					1391:1391	2	1391:1391	2	1391:1391	These results defined the Fya epitope and suggested that (1) two disulphide bridges are involved in the creation of an active chemokine binding pocket; (2) a limited number of amino acids in ECDs 1-4 participate in CXCL-8 binding; and (3) Fy3 is a conformation-dependent epitope involving all ECDs.
12956774	7	59	dep	involved	1326:1333	arg1	participate					1438:1448	participate	1438:1448	participate in CXCL-8 binding	1438:1466	These results defined the Fya epitope and suggested that (1) two disulphide bridges are involved in the creation of an active chemokine binding pocket; (2) a limited number of amino acids in ECDs 1-4 participate in CXCL-8 binding; and (3) Fy3 is a conformation-dependent epitope involving all ECDs.
12956774	7	60	theme	chemokine	1364:1372	arg1	pocket					1382:1387	an active chemokine binding pocket	1354:1387	an active chemokine binding pocket	1354:1387	These results defined the Fya epitope and suggested that (1) two disulphide bridges are involved in the creation of an active chemokine binding pocket; (2) a limited number of amino acids in ECDs 1-4 participate in CXCL-8 binding; and (3) Fy3 is a conformation-dependent epitope involving all ECDs.
12956774	3	61	theme	Fy6	633:635	arg1	epitope					637:643	the Fy6 epitope	629:643	the Fy6 epitope (22-FEDVW-26)	629:657	Using synthetic peptides, we defined previously the Fy6 epitope (22-FEDVW-26), and we characterized the Fya epitope as the linear sequence 41-YGANLE-46.
12956774	3	61	theme	Fy6	633:635	arg1	22-FEDVW-26					646:656	22-FEDVW-26	646:656	22-FEDVW-26	646:656	Using synthetic peptides, we defined previously the Fy6 epitope (22-FEDVW-26), and we characterized the Fya epitope as the linear sequence 41-YGANLE-46.
12956774	6	62	theme	F22-E23	1189:1195	arg1	mutations					1176:1184	mutations	1176:1184	mutations of F22-E23, P50 (ECD1) and D263, R267, D283 (ECD4)	1176:1235	CXCL-8 binding was also abrogated by mutations of F22-E23, P50 (ECD1) and D263, R267, D283 (ECD4).
12956774	7	63	theme	conformation-dependent	1486:1507	arg1	epitope					1509:1515	a conformation-dependent epitope	1484:1515	a conformation-dependent epitope involving all ECDs	1484:1534	These results defined the Fya epitope and suggested that (1) two disulphide bridges are involved in the creation of an active chemokine binding pocket; (2) a limited number of amino acids in ECDs 1-4 participate in CXCL-8 binding; and (3) Fy3 is a conformation-dependent epitope involving all ECDs.
12956774	7	63	theme	conformation-dependent	1486:1507	arg1	Fy3					1477:1479	(3) Fy3	1473:1479	(3) Fy3	1473:1479	These results defined the Fya epitope and suggested that (1) two disulphide bridges are involved in the creation of an active chemokine binding pocket; (2) a limited number of amino acids in ECDs 1-4 participate in CXCL-8 binding; and (3) Fy3 is a conformation-dependent epitope involving all ECDs.
12956774	8	64	gly	N-glycosylation	1557:1571	arg1	DARC					1576:1579	DARC	1576:1579	DARC	1576:1579	We also showed that N-glycosylation of DARC occurred on N16SS and did not influence antibody and chemokine binding.
12956774	8	64	gly	N-glycosylation	1557:1571	arg2	N16SS					1593:1597	N16SS	1593:1597	N16SS	1593:1597	We also showed that N-glycosylation of DARC occurred on N16SS and did not influence antibody and chemokine binding.
12956774	0	65	theme	antigen/receptor	70:85	arg1	domains					49:55	the extracellular domains	31:55	the extracellular domains of the Duffy antigen/receptor for chemokines	31:100	Structure-function analysis of the extracellular domains of the Duffy antigen/receptor for chemokines: characterization of antibody and chemokine binding sites.
12956774	0	65	theme	antigen/receptor	70:85	arg1	antigen/receptor					70:85	the Duffy antigen/receptor	60:85	the Duffy antigen/receptor for chemokines	60:100	Structure-function analysis of the extracellular domains of the Duffy antigen/receptor for chemokines: characterization of antibody and chemokine binding sites.
12956774	0	66	dep	analysis	19:26	arg1	characterization					103:118	characterization	103:118	Structure-function analysis of the extracellular domains of the Duffy antigen/receptor for chemokines: characterization of antibody and chemokine binding sites.	0:159	Structure-function analysis of the extracellular domains of the Duffy antigen/receptor for chemokines: characterization of antibody and chemokine binding sites.
12956774	7	67	theme	acids	1420:1424	arg1	number					1404:1409	a limited number	1394:1409	a limited number of amino acids in ECDs 1-4	1394:1436	These results defined the Fya epitope and suggested that (1) two disulphide bridges are involved in the creation of an active chemokine binding pocket; (2) a limited number of amino acids in ECDs 1-4 participate in CXCL-8 binding; and (3) Fy3 is a conformation-dependent epitope involving all ECDs.
12956774	5	68	theme	CXC-chemokine	1098:1110	arg1	binding					1130:1136	CXC-chemokine ligand 8 (CXCL-8) binding	1098:1136	CXC-chemokine ligand 8 (CXCL-8) binding	1098:1136	Mutations of C51 (ECD1), C129 (ECD2), C195 (ECD3) and C276 (ECD4 severely reduced anti-Fy3 and CXC-chemokine ligand 8 (CXCL-8) binding.
12956774	7	69	theme	disulphide	1303:1312	arg1	bridges					1314:1320	(1) two disulphide bridges	1295:1320	(1) two disulphide bridges	1295:1320	These results defined the Fya epitope and suggested that (1) two disulphide bridges are involved in the creation of an active chemokine binding pocket; (2) a limited number of amino acids in ECDs 1-4 participate in CXCL-8 binding; and (3) Fy3 is a conformation-dependent epitope involving all ECDs.
12956774	0	70	theme	Duffy	64:68	arg1	antigen/receptor					70:85	the Duffy antigen/receptor	60:85	the Duffy antigen/receptor for chemokines	60:100	Structure-function analysis of the extracellular domains of the Duffy antigen/receptor for chemokines: characterization of antibody and chemokine binding sites.
12956774	1	71	theme	chemokine	322:330	arg1	receptor					332:339	a widely expressed promiscuous chemokine receptor	291:339	a widely expressed promiscuous chemokine receptor	291:339	The Duffy antigen/receptor for chemokines (DARC), a seven-transmembrane glycoprotein carrying the Duffy (Fy) blood group, acts as a widely expressed promiscuous chemokine receptor.
12956774	1	71	theme	chemokine	322:330	arg1	antigen/receptor					171:186	The Duffy antigen/receptor	161:186	The Duffy antigen/receptor for chemokines (DARC), a seven-transmembrane glycoprotein carrying the Duffy (Fy) blood group,	161:281	The Duffy antigen/receptor for chemokines (DARC), a seven-transmembrane glycoprotein carrying the Duffy (Fy) blood group, acts as a widely expressed promiscuous chemokine receptor.
12956774	3	72	theme	synthetic	587:595	arg1	peptides					597:604	synthetic peptides	587:604	synthetic peptides	587:604	Using synthetic peptides, we defined previously the Fy6 epitope (22-FEDVW-26), and we characterized the Fya epitope as the linear sequence 41-YGANLE-46.
12956774	5	73	theme	C276	1057:1060	arg1	ECD4					1063:1066	C276 (ECD4	1057:1066	C276 (ECD4	1057:1066	Mutations of C51 (ECD1), C129 (ECD2), C195 (ECD3) and C276 (ECD4 severely reduced anti-Fy3 and CXC-chemokine ligand 8 (CXCL-8) binding.
12956774	1	74	theme	Duffy	259:263	arg1	group					276:280	the Duffy (Fy) blood group	255:280	the Duffy (Fy) blood group	255:280	The Duffy antigen/receptor for chemokines (DARC), a seven-transmembrane glycoprotein carrying the Duffy (Fy) blood group, acts as a widely expressed promiscuous chemokine receptor.
21692080	7	0	theme	Hp	1195:1196	arg1	N241					1187:1190	N241	1187:1190	N241 of Hp	1187:1196	In addition, N241 of Hp was partially glycosylated, even though this site is unaffected by steric consideration.
21692080	6	1	theme	steric	1047:1052	arg1	hindrance					1054:1062	steric hindrance	1047:1062	steric hindrance	1047:1062	A molecular model of the glycosylated Hp multimer was constructed, suggesting that the effect of steric hindrance on multimeric formation is critical for the enlargement of the glycan moieties on either side of the monomer.
21692080	6	2	theme	Hp	988:989	arg1	multimer					991:998	the glycosylated Hp multimer	971:998	the glycosylated Hp multimer	971:998	A molecular model of the glycosylated Hp multimer was constructed, suggesting that the effect of steric hindrance on multimeric formation is critical for the enlargement of the glycan moieties on either side of the monomer.
21692080	8	3	theme	present	1297:1303	arg1	study					1305:1309	the present study	1293:1309	the present study	1293:1309	Thus, the present study provides evidence for the alteration of glycan structures on different multimeric conformations of Hp, improving our knowledge of conformation-dependent function of this glycoprotein.
21692080	3	4	theme	isoform	343:349	arg1	distributions					351:363	The isoform distributions	339:363	The isoform distributions of different multimers	339:386	The isoform distributions of different multimers were examined by an alternative approach, i.e. 3-D-(Native/IEF/SDS)-PAGE, which revealed differences in N-glycosylation among individual multimers of the same Hp sample.
21692080	6	5	from	effect	1037:1042	arg1	formation					1078:1086	multimeric formation	1067:1086	multimeric formation	1067:1086	A molecular model of the glycosylated Hp multimer was constructed, suggesting that the effect of steric hindrance on multimeric formation is critical for the enlargement of the glycan moieties on either side of the monomer.
21692080	8	6	theme	glycan	1351:1356	arg1	structures					1358:1367	glycan structures	1351:1367	glycan structures	1351:1367	Thus, the present study provides evidence for the alteration of glycan structures on different multimeric conformations of Hp, improving our knowledge of conformation-dependent function of this glycoprotein.
21692080	4	7	theme	N-glycan	592:599	arg1	mapping					567:573	Glycomic mapping	558:573	Glycomic mapping of permethylated N-glycan	558:599	Glycomic mapping of permethylated N-glycan indicated that the assembled monomer and multimeric conformation modulate the degree of glycosylation, especially the reduction in terminal sialic acid residues on the bi-antennary glycan.
21692080	7	8	gly	glycosylated	1212:1223	arg1	N241					1187:1190	N241	1187:1190	N241 of Hp	1187:1196	In addition, N241 of Hp was partially glycosylated, even though this site is unaffected by steric consideration.
21692080	7	8	gly	glycosylated	1212:1223	arg1	addition					1177:1184	addition	1177:1184	addition	1177:1184	In addition, N241 of Hp was partially glycosylated, even though this site is unaffected by steric consideration.
21692080	7	8	gly	glycosylated	1212:1223	arg2	N241					1187:1190	N241	1187:1190	N241 of Hp	1187:1196	In addition, N241 of Hp was partially glycosylated, even though this site is unaffected by steric consideration.
21692080	3	9	theme	same	542:545	arg1	sample					550:555	the same Hp sample	538:555	the same Hp sample	538:555	The isoform distributions of different multimers were examined by an alternative approach, i.e. 3-D-(Native/IEF/SDS)-PAGE, which revealed differences in N-glycosylation among individual multimers of the same Hp sample.
21692080	4	10	from	glycan	782:787	arg1	reduction					719:727	the reduction	715:727	the reduction in terminal sialic acid residues on the bi-antennary glycan	715:787	Glycomic mapping of permethylated N-glycan indicated that the assembled monomer and multimeric conformation modulate the degree of glycosylation, especially the reduction in terminal sialic acid residues on the bi-antennary glycan.
21692080	1	11	theme	Extra-thiol	73:83	arg1	groups					85:90	Extra-thiol groups	73:90	Extra-thiol groups on the α-subunit	73:107	Extra-thiol groups on the α-subunit allow haptoglobin (Hp) to form a variety of native multimers which influence the biophysical and biological properties of Hp.
21692080	4	12	theme	terminal	732:739	arg1	residues					753:760	terminal sialic acid residues	732:760	terminal sialic acid residues on the bi-antennary glycan	732:787	Glycomic mapping of permethylated N-glycan indicated that the assembled monomer and multimeric conformation modulate the degree of glycosylation, especially the reduction in terminal sialic acid residues on the bi-antennary glycan.
21692080	6	13	theme	moieties	1134:1141	arg1	enlargement					1108:1118	the enlargement	1104:1118	the enlargement of the glycan moieties on either side of the monomer	1104:1171	A molecular model of the glycosylated Hp multimer was constructed, suggesting that the effect of steric hindrance on multimeric formation is critical for the enlargement of the glycan moieties on either side of the monomer.
21692080	5	14	theme	acid	818:821	arg1	Loss					790:793	Loss	790:793	Loss of the terminal sialic acid in the higher order multimers	790:851	Loss of the terminal sialic acid in the higher order multimers increases the number of terminal galactose residues, which may contribute to conformation of Hp.
21692080	6	15	theme	monomer	1165:1171	arg1	side					1153:1156	either side	1146:1156	either side of the monomer	1146:1171	A molecular model of the glycosylated Hp multimer was constructed, suggesting that the effect of steric hindrance on multimeric formation is critical for the enlargement of the glycan moieties on either side of the monomer.
21692080	6	16	theme	multimeric	1067:1076	arg1	formation					1078:1086	multimeric formation	1067:1086	multimeric formation	1067:1086	A molecular model of the glycosylated Hp multimer was constructed, suggesting that the effect of steric hindrance on multimeric formation is critical for the enlargement of the glycan moieties on either side of the monomer.
21692080	1	17	theme	native	153:158	arg1	multimers					160:168	native multimers	153:168	native multimers which influence the biophysical and biological properties of Hp	153:232	Extra-thiol groups on the α-subunit allow haptoglobin (Hp) to form a variety of native multimers which influence the biophysical and biological properties of Hp.
21692080	4	18	theme	permethylated	578:590	arg1	N-glycan					592:599	permethylated N-glycan	578:599	permethylated N-glycan	578:599	Glycomic mapping of permethylated N-glycan indicated that the assembled monomer and multimeric conformation modulate the degree of glycosylation, especially the reduction in terminal sialic acid residues on the bi-antennary glycan.
21692080	1	19	theme	multimers	160:168	arg1	variety					142:148	a variety	140:148	a variety of native multimers which influence the biophysical and biological properties of Hp	140:232	Extra-thiol groups on the α-subunit allow haptoglobin (Hp) to form a variety of native multimers which influence the biophysical and biological properties of Hp.
21692080	1	19	theme	multimers	160:168	arg1	multimers					160:168	native multimers	153:168	native multimers which influence the biophysical and biological properties of Hp	153:232	Extra-thiol groups on the α-subunit allow haptoglobin (Hp) to form a variety of native multimers which influence the biophysical and biological properties of Hp.
21692080	3	20	theme	multimers	378:386	arg1	distributions					351:363	The isoform distributions	339:363	The isoform distributions of different multimers	339:386	The isoform distributions of different multimers were examined by an alternative approach, i.e. 3-D-(Native/IEF/SDS)-PAGE, which revealed differences in N-glycosylation among individual multimers of the same Hp sample.
21692080	6	21	gly	glycosylated	975:986	arg1	multimer					991:998	the glycosylated Hp multimer	971:998	the glycosylated Hp multimer	971:998	A molecular model of the glycosylated Hp multimer was constructed, suggesting that the effect of steric hindrance on multimeric formation is critical for the enlargement of the glycan moieties on either side of the monomer.
21692080	5	22	theme	Hp	946:947	arg1	conformation					930:941	conformation	930:941	conformation of Hp	930:947	Loss of the terminal sialic acid in the higher order multimers increases the number of terminal galactose residues, which may contribute to conformation of Hp.
21692080	5	23	theme	terminal	877:884	arg1	residues					896:903	terminal galactose residues	877:903	terminal galactose residues	877:903	Loss of the terminal sialic acid in the higher order multimers increases the number of terminal galactose residues, which may contribute to conformation of Hp.
21692080	0	24	theme	Glycoproteomic	0:13	arg1	analysis					15:22	Glycoproteomic analysis	0:22	Glycoproteomic analysis	0:22	Glycoproteomic analysis and molecular modeling of haptoglobin multimers.
21692080	6	25	theme	glycosylated	975:986	arg1	multimer					991:998	the glycosylated Hp multimer	971:998	the glycosylated Hp multimer	971:998	A molecular model of the glycosylated Hp multimer was constructed, suggesting that the effect of steric hindrance on multimeric formation is critical for the enlargement of the glycan moieties on either side of the monomer.
21692080	4	26	from	residues	753:760	arg1	glycan					782:787	the bi-antennary glycan	765:787	the bi-antennary glycan	765:787	Glycomic mapping of permethylated N-glycan indicated that the assembled monomer and multimeric conformation modulate the degree of glycosylation, especially the reduction in terminal sialic acid residues on the bi-antennary glycan.
21692080	2	27	theme	conformation	295:306	arg1	differences					269:279	differences	269:279	differences of multimeric conformation	269:306	In this work, we demonstrated how differences of multimeric conformation alter the glycosylation of Hp.
21692080	5	28	theme	galactose	886:894	arg1	residues					896:903	terminal galactose residues	877:903	terminal galactose residues	877:903	Loss of the terminal sialic acid in the higher order multimers increases the number of terminal galactose residues, which may contribute to conformation of Hp.
21692080	0	29	theme	molecular	28:36	arg1	modeling					38:45	molecular modeling	28:45	molecular modeling	28:45	Glycoproteomic analysis and molecular modeling of haptoglobin multimers.
21692080	4	30	theme	acid	748:751	arg1	residues					753:760	terminal sialic acid residues	732:760	terminal sialic acid residues on the bi-antennary glycan	732:787	Glycomic mapping of permethylated N-glycan indicated that the assembled monomer and multimeric conformation modulate the degree of glycosylation, especially the reduction in terminal sialic acid residues on the bi-antennary glycan.
21692080	3	31	from	differences	477:487	arg1	N-glycosylation					492:506	N-glycosylation	492:506	N-glycosylation	492:506	The isoform distributions of different multimers were examined by an alternative approach, i.e. 3-D-(Native/IEF/SDS)-PAGE, which revealed differences in N-glycosylation among individual multimers of the same Hp sample.
21692080	3	32	theme	Hp	547:548	arg1	sample					550:555	the same Hp sample	538:555	the same Hp sample	538:555	The isoform distributions of different multimers were examined by an alternative approach, i.e. 3-D-(Native/IEF/SDS)-PAGE, which revealed differences in N-glycosylation among individual multimers of the same Hp sample.
21692080	5	33	theme	order	837:841	arg1	multimers					843:851	the higher order multimers	826:851	the higher order multimers	826:851	Loss of the terminal sialic acid in the higher order multimers increases the number of terminal galactose residues, which may contribute to conformation of Hp.
21692080	3	34	theme	different	368:376	arg1	multimers					378:386	different multimers	368:386	different multimers	368:386	The isoform distributions of different multimers were examined by an alternative approach, i.e. 3-D-(Native/IEF/SDS)-PAGE, which revealed differences in N-glycosylation among individual multimers of the same Hp sample.
21692080	4	35	theme	Glycomic	558:565	arg1	mapping					567:573	Glycomic mapping	558:573	Glycomic mapping of permethylated N-glycan	558:599	Glycomic mapping of permethylated N-glycan indicated that the assembled monomer and multimeric conformation modulate the degree of glycosylation, especially the reduction in terminal sialic acid residues on the bi-antennary glycan.
21692080	8	36	theme	conformation-dependent	1441:1462	arg1	function					1464:1471	conformation-dependent function	1441:1471	conformation-dependent function of this glycoprotein	1441:1492	Thus, the present study provides evidence for the alteration of glycan structures on different multimeric conformations of Hp, improving our knowledge of conformation-dependent function of this glycoprotein.
21692080	3	37	theme	sample	550:555	arg1	multimers					525:533	individual multimers	514:533	individual multimers of the same Hp sample	514:555	The isoform distributions of different multimers were examined by an alternative approach, i.e. 3-D-(Native/IEF/SDS)-PAGE, which revealed differences in N-glycosylation among individual multimers of the same Hp sample.
21692080	1	38	theme	biophysical	190:200	arg1	properties					217:226	the biophysical and biological properties	186:226	the biophysical and biological properties of Hp	186:232	Extra-thiol groups on the α-subunit allow haptoglobin (Hp) to form a variety of native multimers which influence the biophysical and biological properties of Hp.
21692080	8	39	from	alteration	1337:1346	arg1	conformations					1393:1405	different multimeric conformations	1372:1405	different multimeric conformations of Hp	1372:1411	Thus, the present study provides evidence for the alteration of glycan structures on different multimeric conformations of Hp, improving our knowledge of conformation-dependent function of this glycoprotein.
21692080	8	40	theme	different	1372:1380	arg1	conformations					1393:1405	different multimeric conformations	1372:1405	different multimeric conformations of Hp	1372:1411	Thus, the present study provides evidence for the alteration of glycan structures on different multimeric conformations of Hp, improving our knowledge of conformation-dependent function of this glycoprotein.
21692080	6	41	from	side	1153:1156	arg1	enlargement					1108:1118	the enlargement	1104:1118	the enlargement of the glycan moieties on either side of the monomer	1104:1171	A molecular model of the glycosylated Hp multimer was constructed, suggesting that the effect of steric hindrance on multimeric formation is critical for the enlargement of the glycan moieties on either side of the monomer.
21692080	7	42	theme	steric	1265:1270	arg1	consideration					1272:1284	steric consideration	1265:1284	steric consideration	1265:1284	In addition, N241 of Hp was partially glycosylated, even though this site is unaffected by steric consideration.
21692080	3	43	theme	alternative	408:418	arg1	approach					420:427	an alternative approach	405:427	an alternative approach	405:427	The isoform distributions of different multimers were examined by an alternative approach, i.e. 3-D-(Native/IEF/SDS)-PAGE, which revealed differences in N-glycosylation among individual multimers of the same Hp sample.
21692080	6	44	theme	molecular	952:960	arg1	model					962:966	A molecular model	950:966	A molecular model of the glycosylated Hp multimer	950:998	A molecular model of the glycosylated Hp multimer was constructed, suggesting that the effect of steric hindrance on multimeric formation is critical for the enlargement of the glycan moieties on either side of the monomer.
21692080	4	45	theme	bi-antennary	769:780	arg1	glycan					782:787	the bi-antennary glycan	765:787	the bi-antennary glycan	765:787	Glycomic mapping of permethylated N-glycan indicated that the assembled monomer and multimeric conformation modulate the degree of glycosylation, especially the reduction in terminal sialic acid residues on the bi-antennary glycan.
21692080	4	46	theme	assembled	620:628	arg1	monomer					630:636	the assembled monomer	616:636	the assembled monomer	616:636	Glycomic mapping of permethylated N-glycan indicated that the assembled monomer and multimeric conformation modulate the degree of glycosylation, especially the reduction in terminal sialic acid residues on the bi-antennary glycan.
21692080	1	47	theme	biological	206:215	arg1	properties					217:226	the biophysical and biological properties	186:226	the biophysical and biological properties of Hp	186:232	Extra-thiol groups on the α-subunit allow haptoglobin (Hp) to form a variety of native multimers which influence the biophysical and biological properties of Hp.
21692080	0	48	theme	multimers	62:70	arg1	analysis					15:22	Glycoproteomic analysis	0:22	Glycoproteomic analysis	0:22	Glycoproteomic analysis and molecular modeling of haptoglobin multimers.
21692080	0	48	theme	multimers	62:70	arg1	modeling					38:45	molecular modeling	28:45	molecular modeling	28:45	Glycoproteomic analysis and molecular modeling of haptoglobin multimers.
21692080	5	49	theme	sialic	811:816	arg1	acid					818:821	the terminal sialic acid	798:821	the terminal sialic acid	798:821	Loss of the terminal sialic acid in the higher order multimers increases the number of terminal galactose residues, which may contribute to conformation of Hp.
21692080	2	50	theme	Hp	335:336	arg1	glycosylation					318:330	the glycosylation	314:330	the glycosylation of Hp	314:336	In this work, we demonstrated how differences of multimeric conformation alter the glycosylation of Hp.
21692080	0	51	theme	haptoglobin	50:60	arg1	multimers					62:70	haptoglobin multimers	50:70	haptoglobin multimers	50:70	Glycoproteomic analysis and molecular modeling of haptoglobin multimers.
21692080	8	52	gly	glycoprotein	1481:1492	arg1	glycoprotein					1481:1492	this glycoprotein	1476:1492	this glycoprotein	1476:1492	Thus, the present study provides evidence for the alteration of glycan structures on different multimeric conformations of Hp, improving our knowledge of conformation-dependent function of this glycoprotein.
21692080	8	53	theme	function	1464:1471	arg1	knowledge					1428:1436	our knowledge	1424:1436	our knowledge of conformation-dependent function of this glycoprotein	1424:1492	Thus, the present study provides evidence for the alteration of glycan structures on different multimeric conformations of Hp, improving our knowledge of conformation-dependent function of this glycoprotein.
21692080	6	54	from	moieties	1134:1141	arg1	side					1153:1156	either side	1146:1156	either side of the monomer	1146:1171	A molecular model of the glycosylated Hp multimer was constructed, suggesting that the effect of steric hindrance on multimeric formation is critical for the enlargement of the glycan moieties on either side of the monomer.
21692080	6	55	theme	glycan	1127:1132	arg1	moieties					1134:1141	the glycan moieties	1123:1141	the glycan moieties on either side of the monomer	1123:1171	A molecular model of the glycosylated Hp multimer was constructed, suggesting that the effect of steric hindrance on multimeric formation is critical for the enlargement of the glycan moieties on either side of the monomer.
21692080	5	56	from	Loss	790:793	arg1	multimers					843:851	the higher order multimers	826:851	the higher order multimers	826:851	Loss of the terminal sialic acid in the higher order multimers increases the number of terminal galactose residues, which may contribute to conformation of Hp.
21692080	8	57	theme	Hp	1410:1411	arg1	conformations					1393:1405	different multimeric conformations	1372:1405	different multimeric conformations of Hp	1372:1411	Thus, the present study provides evidence for the alteration of glycan structures on different multimeric conformations of Hp, improving our knowledge of conformation-dependent function of this glycoprotein.
21692080	4	58	theme	sialic	741:746	arg1	residues					753:760	terminal sialic acid residues	732:760	terminal sialic acid residues on the bi-antennary glycan	732:787	Glycomic mapping of permethylated N-glycan indicated that the assembled monomer and multimeric conformation modulate the degree of glycosylation, especially the reduction in terminal sialic acid residues on the bi-antennary glycan.
21692080	2	59	theme	multimeric	284:293	arg1	conformation					295:306	multimeric conformation	284:306	multimeric conformation	284:306	In this work, we demonstrated how differences of multimeric conformation alter the glycosylation of Hp.
21692080	6	60	theme	multimer	991:998	arg1	model					962:966	A molecular model	950:966	A molecular model of the glycosylated Hp multimer	950:998	A molecular model of the glycosylated Hp multimer was constructed, suggesting that the effect of steric hindrance on multimeric formation is critical for the enlargement of the glycan moieties on either side of the monomer.
21692080	2	61	gly	glycosylation	318:330	arg1	Hp					335:336	Hp	335:336	Hp	335:336	In this work, we demonstrated how differences of multimeric conformation alter the glycosylation of Hp.
21692080	8	62	theme	glycoprotein	1481:1492	arg1	function					1464:1471	conformation-dependent function	1441:1471	conformation-dependent function of this glycoprotein	1441:1492	Thus, the present study provides evidence for the alteration of glycan structures on different multimeric conformations of Hp, improving our knowledge of conformation-dependent function of this glycoprotein.
21692080	5	63	theme	higher	830:835	arg1	multimers					843:851	the higher order multimers	826:851	the higher order multimers	826:851	Loss of the terminal sialic acid in the higher order multimers increases the number of terminal galactose residues, which may contribute to conformation of Hp.
21692080	4	64	theme	glycosylation	689:701	arg1	degree					679:684	the degree	675:684	the degree of glycosylation	675:701	Glycomic mapping of permethylated N-glycan indicated that the assembled monomer and multimeric conformation modulate the degree of glycosylation, especially the reduction in terminal sialic acid residues on the bi-antennary glycan.
21692080	8	65	theme	multimeric	1382:1391	arg1	conformations					1393:1405	different multimeric conformations	1372:1405	different multimeric conformations of Hp	1372:1411	Thus, the present study provides evidence for the alteration of glycan structures on different multimeric conformations of Hp, improving our knowledge of conformation-dependent function of this glycoprotein.
21692080	4	66	theme	multimeric	642:651	arg1	conformation					653:664	multimeric conformation	642:664	multimeric conformation	642:664	Glycomic mapping of permethylated N-glycan indicated that the assembled monomer and multimeric conformation modulate the degree of glycosylation, especially the reduction in terminal sialic acid residues on the bi-antennary glycan.
21692080	8	67	theme	structures	1358:1367	arg1	alteration					1337:1346	the alteration	1333:1346	the alteration of glycan structures on different multimeric conformations of Hp	1333:1411	Thus, the present study provides evidence for the alteration of glycan structures on different multimeric conformations of Hp, improving our knowledge of conformation-dependent function of this glycoprotein.
21692080	6	68	theme	hindrance	1054:1062	arg1	effect					1037:1042	the effect	1033:1042	the effect of steric hindrance on multimeric formation	1033:1086	A molecular model of the glycosylated Hp multimer was constructed, suggesting that the effect of steric hindrance on multimeric formation is critical for the enlargement of the glycan moieties on either side of the monomer.
21692080	6	68	theme	hindrance	1054:1062	arg1	critical					1091:1098	critical	1091:1098	critical	1091:1098	A molecular model of the glycosylated Hp multimer was constructed, suggesting that the effect of steric hindrance on multimeric formation is critical for the enlargement of the glycan moieties on either side of the monomer.
21692080	5	69	theme	residues	896:903	arg1	number					867:872	the number	863:872	the number	863:872	Loss of the terminal sialic acid in the higher order multimers increases the number of terminal galactose residues, which may contribute to conformation of Hp.
21692080	4	70	from	reduction	719:727	arg1	glycan					782:787	the bi-antennary glycan	765:787	the bi-antennary glycan	765:787	Glycomic mapping of permethylated N-glycan indicated that the assembled monomer and multimeric conformation modulate the degree of glycosylation, especially the reduction in terminal sialic acid residues on the bi-antennary glycan.
21692080	4	70	from	reduction	719:727	arg1	residues					753:760	terminal sialic acid residues	732:760	terminal sialic acid residues on the bi-antennary glycan	732:787	Glycomic mapping of permethylated N-glycan indicated that the assembled monomer and multimeric conformation modulate the degree of glycosylation, especially the reduction in terminal sialic acid residues on the bi-antennary glycan.
21692080	1	71	theme	Hp	231:232	arg1	properties					217:226	the biophysical and biological properties	186:226	the biophysical and biological properties of Hp	186:232	Extra-thiol groups on the α-subunit allow haptoglobin (Hp) to form a variety of native multimers which influence the biophysical and biological properties of Hp.
21692080	5	72	theme	terminal	802:809	arg1	acid					818:821	the terminal sialic acid	798:821	the terminal sialic acid	798:821	Loss of the terminal sialic acid in the higher order multimers increases the number of terminal galactose residues, which may contribute to conformation of Hp.
21692080	3	73	dep	-PAGE	455:459	arg1	i.e.					430:433	i.e.	430:433	i.e.	430:433	The isoform distributions of different multimers were examined by an alternative approach, i.e. 3-D-(Native/IEF/SDS)-PAGE, which revealed differences in N-glycosylation among individual multimers of the same Hp sample.
21692080	6	74	from	enlargement	1108:1118	arg1	side					1153:1156	either side	1146:1156	either side of the monomer	1146:1171	A molecular model of the glycosylated Hp multimer was constructed, suggesting that the effect of steric hindrance on multimeric formation is critical for the enlargement of the glycan moieties on either side of the monomer.
21692080	3	75	theme	individual	514:523	arg1	multimers					525:533	individual multimers	514:533	individual multimers of the same Hp sample	514:555	The isoform distributions of different multimers were examined by an alternative approach, i.e. 3-D-(Native/IEF/SDS)-PAGE, which revealed differences in N-glycosylation among individual multimers of the same Hp sample.
21692080	1	76	from	groups	85:90	arg1	α-subunit					99:107	the α-subunit	95:107	the α-subunit	95:107	Extra-thiol groups on the α-subunit allow haptoglobin (Hp) to form a variety of native multimers which influence the biophysical and biological properties of Hp.
18214858	6	0	with	patients	1119:1126	arg1	CP					1133:1134	CP	1133:1134	CP	1133:1134	While fucosylated N-glycans derived from serum haptoglobin of patients with CP slightly increased, di-fucosylated tetra-antennary N-glycans were observed only at this site in PC patients, and were absent in the haptoglobin of normal controls and individuals with CP.
18214858	4	1	theme	tri-	851:854	arg1	concentrations					810:823	concentrations	810:823	concentrations of total fucosylated di-, tri- and tetra-branched glycans of haptoglobin	810:896	Mass spectrometry analyses demonstrated that concentrations of total fucosylated di-, tri- and tetra-branched glycans of haptoglobin increased in the sera of PC patients.
18214858	6	2	theme	serum	1098:1102	arg1	haptoglobin					1104:1114	serum haptoglobin	1098:1114	serum haptoglobin of patients with CP	1098:1134	While fucosylated N-glycans derived from serum haptoglobin of patients with CP slightly increased, di-fucosylated tetra-antennary N-glycans were observed only at this site in PC patients, and were absent in the haptoglobin of normal controls and individuals with CP.
18214858	6	3	located	observed	1202:1209	arg1	site					1224:1227	this site	1219:1227	this site	1219:1227	While fucosylated N-glycans derived from serum haptoglobin of patients with CP slightly increased, di-fucosylated tetra-antennary N-glycans were observed only at this site in PC patients, and were absent in the haptoglobin of normal controls and individuals with CP.
18214858	6	3	located	observed	1202:1209	arg1	patients					1235:1242	PC patients	1232:1242	PC patients	1232:1242	While fucosylated N-glycans derived from serum haptoglobin of patients with CP slightly increased, di-fucosylated tetra-antennary N-glycans were observed only at this site in PC patients, and were absent in the haptoglobin of normal controls and individuals with CP.
18214858	6	3	located	observed	1202:1209	arg2	N-glycans					1187:1195	di-fucosylated tetra-antennary N-glycans	1156:1195	di-fucosylated tetra-antennary N-glycans	1156:1195	While fucosylated N-glycans derived from serum haptoglobin of patients with CP slightly increased, di-fucosylated tetra-antennary N-glycans were observed only at this site in PC patients, and were absent in the haptoglobin of normal controls and individuals with CP.
18214858	6	4	theme	normal	1283:1288	arg1	controls					1290:1297	normal controls	1283:1297	normal controls	1283:1297	While fucosylated N-glycans derived from serum haptoglobin of patients with CP slightly increased, di-fucosylated tetra-antennary N-glycans were observed only at this site in PC patients, and were absent in the haptoglobin of normal controls and individuals with CP.
18214858	1	5	located	found	157:161	arg2	It					150:151	It	150:151	It	150:151	It was found in our previous studies that the concentration of fucosylated haptoglobin had increased in the sera of patients with pancreatic cancer (PC) compared to those of other types of cancer and normal controls.
18214858	1	5	located	found	157:161	arg1	studies					179:185	our previous studies	166:185	our previous studies that the concentration of fucosylated haptoglobin had increased in the sera of patients with pancreatic cancer (PC) compared to those of other types of cancer and normal controls	166:364	It was found in our previous studies that the concentration of fucosylated haptoglobin had increased in the sera of patients with pancreatic cancer (PC) compared to those of other types of cancer and normal controls.
18214858	4	6	theme	tetra-branched	860:873	arg1	glycans					875:881	tetra-branched glycans	860:881	tetra-branched glycans	860:881	Mass spectrometry analyses demonstrated that concentrations of total fucosylated di-, tri- and tetra-branched glycans of haptoglobin increased in the sera of PC patients.
18214858	7	7	theme	tumor	1430:1434	arg1	markers					1436:1442	novel tumor markers	1424:1442	novel tumor markers for PC	1424:1449	Thus, the present study provides evidence that site-specific analyses of N-glycans may be useful as novel tumor markers for PC.
18214858	3	8	from	structures	586:595	arg1	sera					615:618	sera	615:618	sera obtained from patients with PC or chronic pancreatitis (CP)	615:678	In the present study, site-specific N-glycan structures of haptoglobin in sera obtained from patients with PC or chronic pancreatitis (CP) were analyzed using liquid chromatography-electrospray ionization mass spectrometry.
18214858	0	9	with	patients	62:69	arg1	cancer					87:92	pancreatic cancer	76:92	pancreatic cancer	76:92	Site-specific analysis of N-glycans on haptoglobin in sera of patients with pancreatic cancer: a novel approach for the development of tumor markers.
18214858	4	10	theme	total	828:832	arg1	di-					846:848	total fucosylated di-	828:848	total fucosylated di-	828:848	Mass spectrometry analyses demonstrated that concentrations of total fucosylated di-, tri- and tetra-branched glycans of haptoglobin increased in the sera of PC patients.
18214858	3	11	theme	chronic	654:660	arg1	pancreatitis					662:673	chronic pancreatitis	654:673	chronic pancreatitis (CP)	654:678	In the present study, site-specific N-glycan structures of haptoglobin in sera obtained from patients with PC or chronic pancreatitis (CP) were analyzed using liquid chromatography-electrospray ionization mass spectrometry.
18214858	3	11	theme	chronic	654:660	arg1	CP					676:677	CP	676:677	CP	676:677	In the present study, site-specific N-glycan structures of haptoglobin in sera obtained from patients with PC or chronic pancreatitis (CP) were analyzed using liquid chromatography-electrospray ionization mass spectrometry.
18214858	6	12	from	absent	1254:1259	arg1	haptoglobin					1268:1278	the haptoglobin	1264:1278	the haptoglobin of normal controls and individuals with CP	1264:1321	While fucosylated N-glycans derived from serum haptoglobin of patients with CP slightly increased, di-fucosylated tetra-antennary N-glycans were observed only at this site in PC patients, and were absent in the haptoglobin of normal controls and individuals with CP.
18214858	4	13	theme	di-	846:848	arg1	concentrations					810:823	concentrations	810:823	concentrations of total fucosylated di-, tri- and tetra-branched glycans of haptoglobin	810:896	Mass spectrometry analyses demonstrated that concentrations of total fucosylated di-, tri- and tetra-branched glycans of haptoglobin increased in the sera of PC patients.
18214858	1	14	with	patients	266:273	arg1	PC					299:300	PC	299:300	PC	299:300	It was found in our previous studies that the concentration of fucosylated haptoglobin had increased in the sera of patients with pancreatic cancer (PC) compared to those of other types of cancer and normal controls.
18214858	1	14	with	patients	266:273	arg1	cancer					291:296	pancreatic cancer	280:296	pancreatic cancer (PC)	280:301	It was found in our previous studies that the concentration of fucosylated haptoglobin had increased in the sera of patients with pancreatic cancer (PC) compared to those of other types of cancer and normal controls.
18214858	6	15	theme	tetra-antennary	1171:1185	arg1	N-glycans					1187:1195	di-fucosylated tetra-antennary N-glycans	1156:1195	di-fucosylated tetra-antennary N-glycans	1156:1195	While fucosylated N-glycans derived from serum haptoglobin of patients with CP slightly increased, di-fucosylated tetra-antennary N-glycans were observed only at this site in PC patients, and were absent in the haptoglobin of normal controls and individuals with CP.
18214858	6	16	with	individuals	1303:1313	arg1	CP					1320:1321	CP	1320:1321	CP	1320:1321	While fucosylated N-glycans derived from serum haptoglobin of patients with CP slightly increased, di-fucosylated tetra-antennary N-glycans were observed only at this site in PC patients, and were absent in the haptoglobin of normal controls and individuals with CP.
18214858	6	17	theme	PC	1232:1233	arg1	patients					1235:1242	PC patients	1232:1242	PC patients	1232:1242	While fucosylated N-glycans derived from serum haptoglobin of patients with CP slightly increased, di-fucosylated tetra-antennary N-glycans were observed only at this site in PC patients, and were absent in the haptoglobin of normal controls and individuals with CP.
18214858	7	18	theme	N-glycans	1397:1405	arg1	analyses					1385:1392	site-specific analyses	1371:1392	site-specific analyses of N-glycans	1371:1405	Thus, the present study provides evidence that site-specific analyses of N-glycans may be useful as novel tumor markers for PC.
18214858	1	19	theme	previous	170:177	arg1	studies					179:185	our previous studies	166:185	our previous studies that the concentration of fucosylated haptoglobin had increased in the sera of patients with pancreatic cancer (PC) compared to those of other types of cancer and normal controls	166:364	It was found in our previous studies that the concentration of fucosylated haptoglobin had increased in the sera of patients with pancreatic cancer (PC) compared to those of other types of cancer and normal controls.
18214858	3	20	theme	ionization	735:744	arg1	spectrometry					751:762	liquid chromatography-electrospray ionization mass spectrometry	700:762	liquid chromatography-electrospray ionization mass spectrometry	700:762	In the present study, site-specific N-glycan structures of haptoglobin in sera obtained from patients with PC or chronic pancreatitis (CP) were analyzed using liquid chromatography-electrospray ionization mass spectrometry.
18214858	2	21	theme	fucosylated	518:528	arg1	N-glycans					530:538	fucosylated N-glycans	518:538	fucosylated N-glycans	518:538	Haptoglobin, an acute phase protein, has four potential N-glycosylation sites, although it remains unknown which site is responsible for the change in fucosylated N-glycans.
18214858	3	22	theme	liquid	700:705	arg1	spectrometry					751:762	liquid chromatography-electrospray ionization mass spectrometry	700:762	liquid chromatography-electrospray ionization mass spectrometry	700:762	In the present study, site-specific N-glycan structures of haptoglobin in sera obtained from patients with PC or chronic pancreatitis (CP) were analyzed using liquid chromatography-electrospray ionization mass spectrometry.
18214858	1	23	theme	controls	357:364	arg1	types					330:334	other types	324:334	other types of cancer and normal controls	324:364	It was found in our previous studies that the concentration of fucosylated haptoglobin had increased in the sera of patients with pancreatic cancer (PC) compared to those of other types of cancer and normal controls.
18214858	2	24	gly	fucosylated	518:528	arg1	N-glycans					530:538	fucosylated N-glycans	518:538	fucosylated N-glycans	518:538	Haptoglobin, an acute phase protein, has four potential N-glycosylation sites, although it remains unknown which site is responsible for the change in fucosylated N-glycans.
18214858	0	25	theme	markers	141:147	arg1	development					120:130	the development	116:130	the development of tumor markers	116:147	Site-specific analysis of N-glycans on haptoglobin in sera of patients with pancreatic cancer: a novel approach for the development of tumor markers.
18214858	5	26	theme	N-glycans	1046:1054	arg1	N-glycans					1046:1054	haptoglobin N-glycans	1034:1054	haptoglobin N-glycans	1034:1054	Tri-antennary N-glycans containing a Lewis X-type fucose markedly increased at the Asn211 site of haptoglobin N-glycans.
18214858	5	26	theme	N-glycans	1046:1054	arg1	site					1026:1029	the Asn211 site	1015:1029	the Asn211 site of haptoglobin N-glycans	1015:1054	Tri-antennary N-glycans containing a Lewis X-type fucose markedly increased at the Asn211 site of haptoglobin N-glycans.
18214858	3	27	theme	site-specific	563:575	arg1	structures					586:595	site-specific N-glycan structures	563:595	site-specific N-glycan structures of haptoglobin in sera obtained from patients with PC or chronic pancreatitis (CP)	563:678	In the present study, site-specific N-glycan structures of haptoglobin in sera obtained from patients with PC or chronic pancreatitis (CP) were analyzed using liquid chromatography-electrospray ionization mass spectrometry.
18214858	7	28	theme	present	1334:1340	arg1	study					1342:1346	the present study	1330:1346	the present study	1330:1346	Thus, the present study provides evidence that site-specific analyses of N-glycans may be useful as novel tumor markers for PC.
18214858	4	29	theme	patients	926:933	arg1	sera					915:918	the sera	911:918	the sera of PC patients	911:933	Mass spectrometry analyses demonstrated that concentrations of total fucosylated di-, tri- and tetra-branched glycans of haptoglobin increased in the sera of PC patients.
18214858	1	30	gly	fucosylated	213:223	arg1	haptoglobin					225:235	fucosylated haptoglobin	213:235	fucosylated haptoglobin	213:235	It was found in our previous studies that the concentration of fucosylated haptoglobin had increased in the sera of patients with pancreatic cancer (PC) compared to those of other types of cancer and normal controls.
18214858	1	31	theme	other	324:328	arg1	types					330:334	other types	324:334	other types of cancer and normal controls	324:364	It was found in our previous studies that the concentration of fucosylated haptoglobin had increased in the sera of patients with pancreatic cancer (PC) compared to those of other types of cancer and normal controls.
18214858	5	32	theme	Lewis	973:977	arg1	fucose					986:991	a Lewis X-type fucose	971:991	a Lewis X-type fucose	971:991	Tri-antennary N-glycans containing a Lewis X-type fucose markedly increased at the Asn211 site of haptoglobin N-glycans.
18214858	0	33	theme	Site-specific	0:12	arg1	analysis					14:21	Site-specific analysis	0:21	Site-specific analysis of N-glycans on haptoglobin in sera of patients with pancreatic cancer: a novel approach for the development of tumor markers.	0:148	Site-specific analysis of N-glycans on haptoglobin in sera of patients with pancreatic cancer: a novel approach for the development of tumor markers.
18214858	2	34	theme	acute	383:387	arg1	protein					395:401	an acute phase protein	380:401	an acute phase protein	380:401	Haptoglobin, an acute phase protein, has four potential N-glycosylation sites, although it remains unknown which site is responsible for the change in fucosylated N-glycans.
18214858	2	34	theme	acute	383:387	arg1	Haptoglobin					367:377	Haptoglobin	367:377	Haptoglobin	367:377	Haptoglobin, an acute phase protein, has four potential N-glycosylation sites, although it remains unknown which site is responsible for the change in fucosylated N-glycans.
18214858	5	35	theme	Tri-antennary	936:948	arg1	N-glycans					950:958	Tri-antennary N-glycans	936:958	Tri-antennary N-glycans containing a Lewis X-type fucose	936:991	Tri-antennary N-glycans containing a Lewis X-type fucose markedly increased at the Asn211 site of haptoglobin N-glycans.
18214858	2	36	theme	potential	413:421	arg1	sites					439:443	four potential N-glycosylation sites	408:443	four potential N-glycosylation sites	408:443	Haptoglobin, an acute phase protein, has four potential N-glycosylation sites, although it remains unknown which site is responsible for the change in fucosylated N-glycans.
18214858	3	37	theme	haptoglobin	600:610	arg1	structures					586:595	site-specific N-glycan structures	563:595	site-specific N-glycan structures of haptoglobin in sera obtained from patients with PC or chronic pancreatitis (CP)	563:678	In the present study, site-specific N-glycan structures of haptoglobin in sera obtained from patients with PC or chronic pancreatitis (CP) were analyzed using liquid chromatography-electrospray ionization mass spectrometry.
18214858	6	38	theme	patients	1119:1126	arg1	haptoglobin					1104:1114	serum haptoglobin	1098:1114	serum haptoglobin of patients with CP	1098:1134	While fucosylated N-glycans derived from serum haptoglobin of patients with CP slightly increased, di-fucosylated tetra-antennary N-glycans were observed only at this site in PC patients, and were absent in the haptoglobin of normal controls and individuals with CP.
18214858	4	39	theme	spectrometry	770:781	arg1	analyses					783:790	Mass spectrometry analyses	765:790	Mass spectrometry analyses	765:790	Mass spectrometry analyses demonstrated that concentrations of total fucosylated di-, tri- and tetra-branched glycans of haptoglobin increased in the sera of PC patients.
18214858	6	40	theme	controls	1290:1297	arg1	haptoglobin					1268:1278	the haptoglobin	1264:1278	the haptoglobin of normal controls and individuals with CP	1264:1321	While fucosylated N-glycans derived from serum haptoglobin of patients with CP slightly increased, di-fucosylated tetra-antennary N-glycans were observed only at this site in PC patients, and were absent in the haptoglobin of normal controls and individuals with CP.
18214858	1	41	theme	haptoglobin	225:235	arg1	concentration					196:208	the concentration	192:208	the concentration of fucosylated haptoglobin	192:235	It was found in our previous studies that the concentration of fucosylated haptoglobin had increased in the sera of patients with pancreatic cancer (PC) compared to those of other types of cancer and normal controls.
18214858	6	42	attach	derived	1085:1091	arg1	haptoglobin					1104:1114	serum haptoglobin	1098:1114	serum haptoglobin of patients with CP	1098:1134	While fucosylated N-glycans derived from serum haptoglobin of patients with CP slightly increased, di-fucosylated tetra-antennary N-glycans were observed only at this site in PC patients, and were absent in the haptoglobin of normal controls and individuals with CP.
18214858	6	42	attach	derived	1085:1091	arg2	N-glycans					1075:1083	fucosylated N-glycans	1063:1083	fucosylated N-glycans derived from serum haptoglobin of patients with CP	1063:1134	While fucosylated N-glycans derived from serum haptoglobin of patients with CP slightly increased, di-fucosylated tetra-antennary N-glycans were observed only at this site in PC patients, and were absent in the haptoglobin of normal controls and individuals with CP.
18214858	7	43	theme	novel	1424:1428	arg1	markers					1436:1442	novel tumor markers	1424:1442	novel tumor markers for PC	1424:1449	Thus, the present study provides evidence that site-specific analyses of N-glycans may be useful as novel tumor markers for PC.
18214858	5	44	contain	containing	960:969	arg2	fucose					986:991	a Lewis X-type fucose	971:991	a Lewis X-type fucose	971:991	Tri-antennary N-glycans containing a Lewis X-type fucose markedly increased at the Asn211 site of haptoglobin N-glycans.
18214858	5	44	contain	containing	960:969	arg1	N-glycans					950:958	Tri-antennary N-glycans	936:958	Tri-antennary N-glycans containing a Lewis X-type fucose	936:991	Tri-antennary N-glycans containing a Lewis X-type fucose markedly increased at the Asn211 site of haptoglobin N-glycans.
18214858	6	45	gly	di-fucosylated	1156:1169	arg1	N-glycans					1187:1195	di-fucosylated tetra-antennary N-glycans	1156:1195	di-fucosylated tetra-antennary N-glycans	1156:1195	While fucosylated N-glycans derived from serum haptoglobin of patients with CP slightly increased, di-fucosylated tetra-antennary N-glycans were observed only at this site in PC patients, and were absent in the haptoglobin of normal controls and individuals with CP.
18214858	2	46	contain	has	404:406	arg1	protein					395:401	an acute phase protein	380:401	an acute phase protein	380:401	Haptoglobin, an acute phase protein, has four potential N-glycosylation sites, although it remains unknown which site is responsible for the change in fucosylated N-glycans.
18214858	2	46	contain	has	404:406	arg1	Haptoglobin					367:377	Haptoglobin	367:377	Haptoglobin	367:377	Haptoglobin, an acute phase protein, has four potential N-glycosylation sites, although it remains unknown which site is responsible for the change in fucosylated N-glycans.
18214858	2	46	contain	has	404:406	arg2	sites					439:443	four potential N-glycosylation sites	408:443	four potential N-glycosylation sites	408:443	Haptoglobin, an acute phase protein, has four potential N-glycosylation sites, although it remains unknown which site is responsible for the change in fucosylated N-glycans.
18214858	4	47	theme	fucosylated	834:844	arg1	di-					846:848	total fucosylated di-	828:848	total fucosylated di-	828:848	Mass spectrometry analyses demonstrated that concentrations of total fucosylated di-, tri- and tetra-branched glycans of haptoglobin increased in the sera of PC patients.
18214858	6	48	theme	di-fucosylated	1156:1169	arg1	N-glycans					1187:1195	di-fucosylated tetra-antennary N-glycans	1156:1195	di-fucosylated tetra-antennary N-glycans	1156:1195	While fucosylated N-glycans derived from serum haptoglobin of patients with CP slightly increased, di-fucosylated tetra-antennary N-glycans were observed only at this site in PC patients, and were absent in the haptoglobin of normal controls and individuals with CP.
18214858	1	49	theme	cancer	339:344	arg1	types					330:334	other types	324:334	other types of cancer and normal controls	324:364	It was found in our previous studies that the concentration of fucosylated haptoglobin had increased in the sera of patients with pancreatic cancer (PC) compared to those of other types of cancer and normal controls.
18214858	4	50	gly	fucosylated	834:844	arg1	di-					846:848	total fucosylated di-	828:848	total fucosylated di-	828:848	Mass spectrometry analyses demonstrated that concentrations of total fucosylated di-, tri- and tetra-branched glycans of haptoglobin increased in the sera of PC patients.
18214858	3	51	theme	mass	746:749	arg1	spectrometry					751:762	liquid chromatography-electrospray ionization mass spectrometry	700:762	liquid chromatography-electrospray ionization mass spectrometry	700:762	In the present study, site-specific N-glycan structures of haptoglobin in sera obtained from patients with PC or chronic pancreatitis (CP) were analyzed using liquid chromatography-electrospray ionization mass spectrometry.
18214858	0	52	theme	tumor	135:139	arg1	markers					141:147	tumor markers	135:147	tumor markers	135:147	Site-specific analysis of N-glycans on haptoglobin in sera of patients with pancreatic cancer: a novel approach for the development of tumor markers.
18214858	1	53	theme	normal	350:355	arg1	controls					357:364	normal controls	350:364	normal controls	350:364	It was found in our previous studies that the concentration of fucosylated haptoglobin had increased in the sera of patients with pancreatic cancer (PC) compared to those of other types of cancer and normal controls.
18214858	4	54	theme	glycans	875:881	arg1	concentrations					810:823	concentrations	810:823	concentrations of total fucosylated di-, tri- and tetra-branched glycans of haptoglobin	810:896	Mass spectrometry analyses demonstrated that concentrations of total fucosylated di-, tri- and tetra-branched glycans of haptoglobin increased in the sera of PC patients.
18214858	1	55	dep	increased	241:249	arg1	compared					303:310	compared	303:310	compared to those of other types of cancer and normal controls	303:364	It was found in our previous studies that the concentration of fucosylated haptoglobin had increased in the sera of patients with pancreatic cancer (PC) compared to those of other types of cancer and normal controls.
18214858	7	56	theme	site-specific	1371:1383	arg1	analyses					1385:1392	site-specific analyses	1371:1392	site-specific analyses of N-glycans	1371:1405	Thus, the present study provides evidence that site-specific analyses of N-glycans may be useful as novel tumor markers for PC.
18214858	3	57	theme	chromatography-electrospray	707:733	arg1	spectrometry					751:762	liquid chromatography-electrospray ionization mass spectrometry	700:762	liquid chromatography-electrospray ionization mass spectrometry	700:762	In the present study, site-specific N-glycan structures of haptoglobin in sera obtained from patients with PC or chronic pancreatitis (CP) were analyzed using liquid chromatography-electrospray ionization mass spectrometry.
18214858	6	58	theme	individuals	1303:1313	arg1	haptoglobin					1268:1278	the haptoglobin	1264:1278	the haptoglobin of normal controls and individuals with CP	1264:1321	While fucosylated N-glycans derived from serum haptoglobin of patients with CP slightly increased, di-fucosylated tetra-antennary N-glycans were observed only at this site in PC patients, and were absent in the haptoglobin of normal controls and individuals with CP.
18214858	5	59	theme	haptoglobin	1034:1044	arg1	N-glycans					1046:1054	haptoglobin N-glycans	1034:1054	haptoglobin N-glycans	1034:1054	Tri-antennary N-glycans containing a Lewis X-type fucose markedly increased at the Asn211 site of haptoglobin N-glycans.
18214858	4	60	theme	haptoglobin	886:896	arg1	tri-					851:854	tri-	851:854	tri-	851:854	Mass spectrometry analyses demonstrated that concentrations of total fucosylated di-, tri- and tetra-branched glycans of haptoglobin increased in the sera of PC patients.
18214858	4	60	theme	haptoglobin	886:896	arg1	glycans					875:881	tetra-branched glycans	860:881	tetra-branched glycans	860:881	Mass spectrometry analyses demonstrated that concentrations of total fucosylated di-, tri- and tetra-branched glycans of haptoglobin increased in the sera of PC patients.
18214858	4	60	theme	haptoglobin	886:896	arg1	di-					846:848	total fucosylated di-	828:848	total fucosylated di-	828:848	Mass spectrometry analyses demonstrated that concentrations of total fucosylated di-, tri- and tetra-branched glycans of haptoglobin increased in the sera of PC patients.
18214858	0	61	theme	patients	62:69	arg1	sera					54:57	sera	54:57	sera of patients with pancreatic cancer	54:92	Site-specific analysis of N-glycans on haptoglobin in sera of patients with pancreatic cancer: a novel approach for the development of tumor markers.
18214858	3	62	theme	present	548:554	arg1	study					556:560	the present study	544:560	the present study	544:560	In the present study, site-specific N-glycan structures of haptoglobin in sera obtained from patients with PC or chronic pancreatitis (CP) were analyzed using liquid chromatography-electrospray ionization mass spectrometry.
18214858	0	63	theme	pancreatic	76:85	arg1	cancer					87:92	pancreatic cancer	76:92	pancreatic cancer	76:92	Site-specific analysis of N-glycans on haptoglobin in sera of patients with pancreatic cancer: a novel approach for the development of tumor markers.
18214858	2	64	theme	N-glycosylation	423:437	arg1	sites					439:443	four potential N-glycosylation sites	408:443	four potential N-glycosylation sites	408:443	Haptoglobin, an acute phase protein, has four potential N-glycosylation sites, although it remains unknown which site is responsible for the change in fucosylated N-glycans.
18214858	0	65	from	analysis	14:21	arg1	haptoglobin					39:49	haptoglobin	39:49	haptoglobin in sera of patients with pancreatic cancer	39:92	Site-specific analysis of N-glycans on haptoglobin in sera of patients with pancreatic cancer: a novel approach for the development of tumor markers.
18214858	4	66	theme	PC	923:924	arg1	patients					926:933	PC patients	923:933	PC patients	923:933	Mass spectrometry analyses demonstrated that concentrations of total fucosylated di-, tri- and tetra-branched glycans of haptoglobin increased in the sera of PC patients.
18214858	0	67	theme	novel	97:101	arg1	approach					103:110	a novel approach	95:110	Site-specific analysis of N-glycans on haptoglobin in sera of patients with pancreatic cancer: a novel approach for the development of tumor markers.	0:148	Site-specific analysis of N-glycans on haptoglobin in sera of patients with pancreatic cancer: a novel approach for the development of tumor markers.
18214858	0	68	from	haptoglobin	39:49	arg1	sera					54:57	sera	54:57	sera of patients with pancreatic cancer	54:92	Site-specific analysis of N-glycans on haptoglobin in sera of patients with pancreatic cancer: a novel approach for the development of tumor markers.
18214858	6	69	theme	fucosylated	1063:1073	arg1	N-glycans					1075:1083	fucosylated N-glycans	1063:1083	fucosylated N-glycans derived from serum haptoglobin of patients with CP	1063:1134	While fucosylated N-glycans derived from serum haptoglobin of patients with CP slightly increased, di-fucosylated tetra-antennary N-glycans were observed only at this site in PC patients, and were absent in the haptoglobin of normal controls and individuals with CP.
18214858	2	70	theme	phase	389:393	arg1	protein					395:401	an acute phase protein	380:401	an acute phase protein	380:401	Haptoglobin, an acute phase protein, has four potential N-glycosylation sites, although it remains unknown which site is responsible for the change in fucosylated N-glycans.
18214858	2	70	theme	phase	389:393	arg1	Haptoglobin					367:377	Haptoglobin	367:377	Haptoglobin	367:377	Haptoglobin, an acute phase protein, has four potential N-glycosylation sites, although it remains unknown which site is responsible for the change in fucosylated N-glycans.
18214858	0	71	theme	N-glycans	26:34	arg1	analysis					14:21	Site-specific analysis	0:21	Site-specific analysis of N-glycans on haptoglobin in sera of patients with pancreatic cancer: a novel approach for the development of tumor markers.	0:148	Site-specific analysis of N-glycans on haptoglobin in sera of patients with pancreatic cancer: a novel approach for the development of tumor markers.
18214858	2	72	gly	N-glycosylation	423:437	arg2	four					408:411	four	408:411	four	408:411	Haptoglobin, an acute phase protein, has four potential N-glycosylation sites, although it remains unknown which site is responsible for the change in fucosylated N-glycans.
18214858	2	72	gly	N-glycosylation	423:437	arg2	sites					439:443	four potential N-glycosylation sites	408:443	four potential N-glycosylation sites	408:443	Haptoglobin, an acute phase protein, has four potential N-glycosylation sites, although it remains unknown which site is responsible for the change in fucosylated N-glycans.
18214858	1	73	theme	patients	266:273	arg1	sera					258:261	the sera	254:261	the sera of patients with pancreatic cancer (PC)	254:301	It was found in our previous studies that the concentration of fucosylated haptoglobin had increased in the sera of patients with pancreatic cancer (PC) compared to those of other types of cancer and normal controls.
18214858	2	74	from	change	508:513	arg1	N-glycans					530:538	fucosylated N-glycans	518:538	fucosylated N-glycans	518:538	Haptoglobin, an acute phase protein, has four potential N-glycosylation sites, although it remains unknown which site is responsible for the change in fucosylated N-glycans.
18214858	3	75	theme	N-glycan	577:584	arg1	structures					586:595	site-specific N-glycan structures	563:595	site-specific N-glycan structures of haptoglobin in sera obtained from patients with PC or chronic pancreatitis (CP)	563:678	In the present study, site-specific N-glycan structures of haptoglobin in sera obtained from patients with PC or chronic pancreatitis (CP) were analyzed using liquid chromatography-electrospray ionization mass spectrometry.
18214858	1	76	theme	pancreatic	280:289	arg1	PC					299:300	PC	299:300	PC	299:300	It was found in our previous studies that the concentration of fucosylated haptoglobin had increased in the sera of patients with pancreatic cancer (PC) compared to those of other types of cancer and normal controls.
18214858	1	76	theme	pancreatic	280:289	arg1	cancer					291:296	pancreatic cancer	280:296	pancreatic cancer (PC)	280:301	It was found in our previous studies that the concentration of fucosylated haptoglobin had increased in the sera of patients with pancreatic cancer (PC) compared to those of other types of cancer and normal controls.
18214858	5	77	theme	Asn211	1019:1024	arg1	N-glycans					1046:1054	haptoglobin N-glycans	1034:1054	haptoglobin N-glycans	1034:1054	Tri-antennary N-glycans containing a Lewis X-type fucose markedly increased at the Asn211 site of haptoglobin N-glycans.
18214858	5	77	theme	Asn211	1019:1024	arg1	site					1026:1029	the Asn211 site	1015:1029	the Asn211 site of haptoglobin N-glycans	1015:1054	Tri-antennary N-glycans containing a Lewis X-type fucose markedly increased at the Asn211 site of haptoglobin N-glycans.
18214858	5	78	theme	X-type	979:984	arg1	fucose					986:991	a Lewis X-type fucose	971:991	a Lewis X-type fucose	971:991	Tri-antennary N-glycans containing a Lewis X-type fucose markedly increased at the Asn211 site of haptoglobin N-glycans.
18214858	6	79	gly	fucosylated	1063:1073	arg1	N-glycans					1075:1083	fucosylated N-glycans	1063:1083	fucosylated N-glycans derived from serum haptoglobin of patients with CP	1063:1134	While fucosylated N-glycans derived from serum haptoglobin of patients with CP slightly increased, di-fucosylated tetra-antennary N-glycans were observed only at this site in PC patients, and were absent in the haptoglobin of normal controls and individuals with CP.
18214858	6	80	with	controls	1290:1297	arg1	CP					1320:1321	CP	1320:1321	CP	1320:1321	While fucosylated N-glycans derived from serum haptoglobin of patients with CP slightly increased, di-fucosylated tetra-antennary N-glycans were observed only at this site in PC patients, and were absent in the haptoglobin of normal controls and individuals with CP.
18214858	6	81	from	haptoglobin	1268:1278	arg1	absent					1254:1259	absent	1254:1259	absent	1254:1259	While fucosylated N-glycans derived from serum haptoglobin of patients with CP slightly increased, di-fucosylated tetra-antennary N-glycans were observed only at this site in PC patients, and were absent in the haptoglobin of normal controls and individuals with CP.
18214858	0	82	dep	analysis	14:21	arg1	approach					103:110	a novel approach	95:110	Site-specific analysis of N-glycans on haptoglobin in sera of patients with pancreatic cancer: a novel approach for the development of tumor markers.	0:148	Site-specific analysis of N-glycans on haptoglobin in sera of patients with pancreatic cancer: a novel approach for the development of tumor markers.
18214858	4	83	theme	Mass	765:768	arg1	analyses					783:790	Mass spectrometry analyses	765:790	Mass spectrometry analyses	765:790	Mass spectrometry analyses demonstrated that concentrations of total fucosylated di-, tri- and tetra-branched glycans of haptoglobin increased in the sera of PC patients.
18214858	3	84	with	patients	634:641	arg1	PC					648:649	PC	648:649	PC	648:649	In the present study, site-specific N-glycan structures of haptoglobin in sera obtained from patients with PC or chronic pancreatitis (CP) were analyzed using liquid chromatography-electrospray ionization mass spectrometry.
18214858	3	84	with	patients	634:641	arg1	pancreatitis					662:673	chronic pancreatitis	654:673	chronic pancreatitis (CP)	654:678	In the present study, site-specific N-glycan structures of haptoglobin in sera obtained from patients with PC or chronic pancreatitis (CP) were analyzed using liquid chromatography-electrospray ionization mass spectrometry.
18214858	3	84	with	patients	634:641	arg1	CP					676:677	CP	676:677	CP	676:677	In the present study, site-specific N-glycan structures of haptoglobin in sera obtained from patients with PC or chronic pancreatitis (CP) were analyzed using liquid chromatography-electrospray ionization mass spectrometry.
18214858	1	85	theme	fucosylated	213:223	arg1	haptoglobin					225:235	fucosylated haptoglobin	213:235	fucosylated haptoglobin	213:235	It was found in our previous studies that the concentration of fucosylated haptoglobin had increased in the sera of patients with pancreatic cancer (PC) compared to those of other types of cancer and normal controls.
15926890	3	0	theme	PSGL-1	997:1002	arg1	synthesis					973:981	the synthesis	969:981	the synthesis of functional PSGL-1	969:1002	We found that (i) both enzymes have their two N-glycosylation sites occupied, (ii) for C2GnT-I, the N-glycan chain linked to Asn-95 significantly contributes to the synthesis of functional PSGL-1 and is required to localize the enzyme to the cis/medial-Golgi compartment, (iii) all N-glycosylation-deficient proteins of FucT-VII displayr a dramatic impairment of their in vitro enzymatic activities, but retain their ability to fucosylate the core2-modified PSGL-I and to generate P- and L-selectin binding, and (iv) the glycomutants of FucT-VII fail to synthesize sialyl-Lewis x or to generate E-selectin binding unless core2-modified PSGL-1 is present.
15926890	0	1	from	effects	223:229	arg1	E-selectin					245:254	E-selectin	245:254	E-selectin	245:254	N-glycans of core2 beta(1,6)-N-acetylglucosaminyltransferase-I (C2GnT-I) but not those of alpha(1,3)-fucosyltransferase-VII (FucT-VII) are required for the synthesis of functional P-selectin glycoprotein ligand-1 (PSGL-1): effects on P-, L- and E-selectin binding.
15926890	0	1	from	effects	223:229	arg1	L-					238:239	L-	238:239	L-	238:239	N-glycans of core2 beta(1,6)-N-acetylglucosaminyltransferase-I (C2GnT-I) but not those of alpha(1,3)-fucosyltransferase-VII (FucT-VII) are required for the synthesis of functional P-selectin glycoprotein ligand-1 (PSGL-1): effects on P-, L- and E-selectin binding.
15926890	0	1	from	effects	223:229	arg1	P-					234:235	P-	234:235	P-	234:235	N-glycans of core2 beta(1,6)-N-acetylglucosaminyltransferase-I (C2GnT-I) but not those of alpha(1,3)-fucosyltransferase-VII (FucT-VII) are required for the synthesis of functional P-selectin glycoprotein ligand-1 (PSGL-1): effects on P-, L- and E-selectin binding.
15926890	4	2	gly	fucosylate	1648:1657	arg1	PSGL-1					1659:1664	PSGL-1	1659:1664	PSGL-1	1659:1664	All combined, our results show a differential functional impact of N-glycosylation on C2GnT-1 and FucT-VII and disclose that a strongly reduced FucT-VII activity retains the ability to fucosylate PSGL-1 on the core2-based binding site(s) for the three selectins.
15926890	4	3	theme	binding	1685:1691	arg1	site					1693:1696	the core2-based binding site	1669:1696	the core2-based binding site(s) for the three selectins	1669:1723	All combined, our results show a differential functional impact of N-glycosylation on C2GnT-1 and FucT-VII and disclose that a strongly reduced FucT-VII activity retains the ability to fucosylate PSGL-1 on the core2-based binding site(s) for the three selectins.
15926890	4	3	theme	binding	1685:1691	arg1	s					1698:1698	s	1698:1698	s	1698:1698	All combined, our results show a differential functional impact of N-glycosylation on C2GnT-1 and FucT-VII and disclose that a strongly reduced FucT-VII activity retains the ability to fucosylate PSGL-1 on the core2-based binding site(s) for the three selectins.
15926890	1	4	theme	1,6	285:287	arg1	-fucosyltransferase-VII					348:370	FucT-VII [alpha(1,3)-fucosyltransferase-VII	328:370	FucT-VII [alpha(1,3)-fucosyltransferase-VII	328:370	C2GnT-I [core2 beta(1,6)-N-acetyglucosaminyltransferase-I] and FucT-VII [alpha(1,3)-fucosyltransferase-VII] are the key enzymes for the biosynthesis of sialyl-Lewis x determinants on selectin ligands and therefore they represent good drug targets for the treatment of inflammatory disorders and other pathologies involving selectins.
15926890	1	4	theme	1,6	285:287	arg1	enzymes					385:391	the key enzymes	377:391	the key enzymes for the biosynthesis of sialyl-Lewis x determinants on selectin ligands	377:463	C2GnT-I [core2 beta(1,6)-N-acetyglucosaminyltransferase-I] and FucT-VII [alpha(1,3)-fucosyltransferase-VII] are the key enzymes for the biosynthesis of sialyl-Lewis x determinants on selectin ligands and therefore they represent good drug targets for the treatment of inflammatory disorders and other pathologies involving selectins.
15926890	1	4	theme	1,6	285:287	arg1	-N-acetyglucosaminyltransferase-I					289:321	C2GnT-I [core2 beta(1,6)-N-acetyglucosaminyltransferase-I	265:321	C2GnT-I [core2 beta(1,6)-N-acetyglucosaminyltransferase-I	265:321	C2GnT-I [core2 beta(1,6)-N-acetyglucosaminyltransferase-I] and FucT-VII [alpha(1,3)-fucosyltransferase-VII] are the key enzymes for the biosynthesis of sialyl-Lewis x determinants on selectin ligands and therefore they represent good drug targets for the treatment of inflammatory disorders and other pathologies involving selectins.
15926890	1	5	theme	key	381:383	arg1	-fucosyltransferase-VII					348:370	FucT-VII [alpha(1,3)-fucosyltransferase-VII	328:370	FucT-VII [alpha(1,3)-fucosyltransferase-VII	328:370	C2GnT-I [core2 beta(1,6)-N-acetyglucosaminyltransferase-I] and FucT-VII [alpha(1,3)-fucosyltransferase-VII] are the key enzymes for the biosynthesis of sialyl-Lewis x determinants on selectin ligands and therefore they represent good drug targets for the treatment of inflammatory disorders and other pathologies involving selectins.
15926890	1	5	theme	key	381:383	arg1	enzymes					385:391	the key enzymes	377:391	the key enzymes for the biosynthesis of sialyl-Lewis x determinants on selectin ligands	377:463	C2GnT-I [core2 beta(1,6)-N-acetyglucosaminyltransferase-I] and FucT-VII [alpha(1,3)-fucosyltransferase-VII] are the key enzymes for the biosynthesis of sialyl-Lewis x determinants on selectin ligands and therefore they represent good drug targets for the treatment of inflammatory disorders and other pathologies involving selectins.
15926890	1	5	theme	key	381:383	arg1	-N-acetyglucosaminyltransferase-I					289:321	C2GnT-I [core2 beta(1,6)-N-acetyglucosaminyltransferase-I	265:321	C2GnT-I [core2 beta(1,6)-N-acetyglucosaminyltransferase-I	265:321	C2GnT-I [core2 beta(1,6)-N-acetyglucosaminyltransferase-I] and FucT-VII [alpha(1,3)-fucosyltransferase-VII] are the key enzymes for the biosynthesis of sialyl-Lewis x determinants on selectin ligands and therefore they represent good drug targets for the treatment of inflammatory disorders and other pathologies involving selectins.
15926890	0	6	theme	those	81:85	arg1	N-glycans					0:8	N-glycans	0:8	N-glycans of core2 beta(1,6)-N-acetylglucosaminyltransferase-I (C2GnT-I) but not those of alpha(1,3)-fucosyltransferase-VII (FucT-VII)	0:133	N-glycans of core2 beta(1,6)-N-acetylglucosaminyltransferase-I (C2GnT-I) but not those of alpha(1,3)-fucosyltransferase-VII (FucT-VII) are required for the synthesis of functional P-selectin glycoprotein ligand-1 (PSGL-1): effects on P-, L- and E-selectin binding.
15926890	3	7	dep	ability	1225:1231	arg1	generate					1280:1287	generate	1280:1287	to generate P- and L-selectin binding	1277:1313	We found that (i) both enzymes have their two N-glycosylation sites occupied, (ii) for C2GnT-I, the N-glycan chain linked to Asn-95 significantly contributes to the synthesis of functional PSGL-1 and is required to localize the enzyme to the cis/medial-Golgi compartment, (iii) all N-glycosylation-deficient proteins of FucT-VII displayr a dramatic impairment of their in vitro enzymatic activities, but retain their ability to fucosylate the core2-modified PSGL-I and to generate P- and L-selectin binding, and (iv) the glycomutants of FucT-VII fail to synthesize sialyl-Lewis x or to generate E-selectin binding unless core2-modified PSGL-1 is present.
15926890	3	7	dep	ability	1225:1231	arg1	fucosylate					1236:1245	fucosylate	1236:1245	to fucosylate the core2-modified PSGL-I	1233:1271	We found that (i) both enzymes have their two N-glycosylation sites occupied, (ii) for C2GnT-I, the N-glycan chain linked to Asn-95 significantly contributes to the synthesis of functional PSGL-1 and is required to localize the enzyme to the cis/medial-Golgi compartment, (iii) all N-glycosylation-deficient proteins of FucT-VII displayr a dramatic impairment of their in vitro enzymatic activities, but retain their ability to fucosylate the core2-modified PSGL-I and to generate P- and L-selectin binding, and (iv) the glycomutants of FucT-VII fail to synthesize sialyl-Lewis x or to generate E-selectin binding unless core2-modified PSGL-1 is present.
15926890	0	8	theme	ligand-1	204:211	arg1	synthesis					156:164	the synthesis	152:164	the synthesis of functional P-selectin glycoprotein ligand-1 (PSGL-1)	152:220	N-glycans of core2 beta(1,6)-N-acetylglucosaminyltransferase-I (C2GnT-I) but not those of alpha(1,3)-fucosyltransferase-VII (FucT-VII) are required for the synthesis of functional P-selectin glycoprotein ligand-1 (PSGL-1): effects on P-, L- and E-selectin binding.
15926890	2	9	theme	glycoprotein	784:795	arg1	ligand-1					797:804	P-selectin glycoprotein ligand-1	773:804	P-selectin glycoprotein ligand-1	773:804	In the present study, we examined the importance of N-glycosylation for the ability of C2GnT-I and FucT-VII to generate functional selectin ligands, particularly the PSGL-1 (P-selectin glycoprotein ligand-1).
15926890	2	9	theme	glycoprotein	784:795	arg1	PSGL-1					765:770	the PSGL-1	761:770	the PSGL-1 (P-selectin glycoprotein ligand-1)	761:805	In the present study, we examined the importance of N-glycosylation for the ability of C2GnT-I and FucT-VII to generate functional selectin ligands, particularly the PSGL-1 (P-selectin glycoprotein ligand-1).
15926890	3	10	theme	N-glycan	908:915	arg1	chain					917:921	the N-glycan chain	904:921	the N-glycan chain linked to Asn-95	904:938	We found that (i) both enzymes have their two N-glycosylation sites occupied, (ii) for C2GnT-I, the N-glycan chain linked to Asn-95 significantly contributes to the synthesis of functional PSGL-1 and is required to localize the enzyme to the cis/medial-Golgi compartment, (iii) all N-glycosylation-deficient proteins of FucT-VII displayr a dramatic impairment of their in vitro enzymatic activities, but retain their ability to fucosylate the core2-modified PSGL-I and to generate P- and L-selectin binding, and (iv) the glycomutants of FucT-VII fail to synthesize sialyl-Lewis x or to generate E-selectin binding unless core2-modified PSGL-1 is present.
15926890	4	11	theme	differential	1496:1507	arg1	impact					1520:1525	a differential functional impact	1494:1525	a differential functional impact of N-glycosylation on C2GnT-1 and FucT-VII	1494:1568	All combined, our results show a differential functional impact of N-glycosylation on C2GnT-1 and FucT-VII and disclose that a strongly reduced FucT-VII activity retains the ability to fucosylate PSGL-1 on the core2-based binding site(s) for the three selectins.
15926890	3	12	theme	functional	986:995	arg1	PSGL-1					997:1002	functional PSGL-1	986:1002	functional PSGL-1	986:1002	We found that (i) both enzymes have their two N-glycosylation sites occupied, (ii) for C2GnT-I, the N-glycan chain linked to Asn-95 significantly contributes to the synthesis of functional PSGL-1 and is required to localize the enzyme to the cis/medial-Golgi compartment, (iii) all N-glycosylation-deficient proteins of FucT-VII displayr a dramatic impairment of their in vitro enzymatic activities, but retain their ability to fucosylate the core2-modified PSGL-I and to generate P- and L-selectin binding, and (iv) the glycomutants of FucT-VII fail to synthesize sialyl-Lewis x or to generate E-selectin binding unless core2-modified PSGL-1 is present.
15926890	2	13	theme	present	606:612	arg1	study					614:618	the present study	602:618	the present study	602:618	In the present study, we examined the importance of N-glycosylation for the ability of C2GnT-I and FucT-VII to generate functional selectin ligands, particularly the PSGL-1 (P-selectin glycoprotein ligand-1).
15926890	1	14	theme	good	494:497	arg1	targets					504:510	good drug targets	494:510	good drug targets for the treatment of inflammatory disorders and other pathologies involving selectins	494:596	C2GnT-I [core2 beta(1,6)-N-acetyglucosaminyltransferase-I] and FucT-VII [alpha(1,3)-fucosyltransferase-VII] are the key enzymes for the biosynthesis of sialyl-Lewis x determinants on selectin ligands and therefore they represent good drug targets for the treatment of inflammatory disorders and other pathologies involving selectins.
15926890	0	15	theme	alpha	90:94	arg1	FucT-VII					125:132	FucT-VII	125:132	FucT-VII	125:132	N-glycans of core2 beta(1,6)-N-acetylglucosaminyltransferase-I (C2GnT-I) but not those of alpha(1,3)-fucosyltransferase-VII (FucT-VII) are required for the synthesis of functional P-selectin glycoprotein ligand-1 (PSGL-1): effects on P-, L- and E-selectin binding.
15926890	0	15	theme	alpha	90:94	arg1	-fucosyltransferase-VII					100:122	alpha(1,3)-fucosyltransferase-VII	90:122	alpha(1,3)-fucosyltransferase-VII (FucT-VII)	90:133	N-glycans of core2 beta(1,6)-N-acetylglucosaminyltransferase-I (C2GnT-I) but not those of alpha(1,3)-fucosyltransferase-VII (FucT-VII) are required for the synthesis of functional P-selectin glycoprotein ligand-1 (PSGL-1): effects on P-, L- and E-selectin binding.
15926890	2	16	theme	functional	719:728	arg1	ligands					739:745	functional selectin ligands	719:745	functional selectin ligands	719:745	In the present study, we examined the importance of N-glycosylation for the ability of C2GnT-I and FucT-VII to generate functional selectin ligands, particularly the PSGL-1 (P-selectin glycoprotein ligand-1).
15926890	2	16	theme	functional	719:728	arg1	PSGL-1					765:770	the PSGL-1	761:770	the PSGL-1 (P-selectin glycoprotein ligand-1)	761:805	In the present study, we examined the importance of N-glycosylation for the ability of C2GnT-I and FucT-VII to generate functional selectin ligands, particularly the PSGL-1 (P-selectin glycoprotein ligand-1).
15926890	0	17	theme	functional	169:178	arg1	PSGL-1					214:219	PSGL-1	214:219	PSGL-1	214:219	N-glycans of core2 beta(1,6)-N-acetylglucosaminyltransferase-I (C2GnT-I) but not those of alpha(1,3)-fucosyltransferase-VII (FucT-VII) are required for the synthesis of functional P-selectin glycoprotein ligand-1 (PSGL-1): effects on P-, L- and E-selectin binding.
15926890	0	17	theme	functional	169:178	arg1	ligand-1					204:211	functional P-selectin glycoprotein ligand-1	169:211	functional P-selectin glycoprotein ligand-1 (PSGL-1)	169:220	N-glycans of core2 beta(1,6)-N-acetylglucosaminyltransferase-I (C2GnT-I) but not those of alpha(1,3)-fucosyltransferase-VII (FucT-VII) are required for the synthesis of functional P-selectin glycoprotein ligand-1 (PSGL-1): effects on P-, L- and E-selectin binding.
15926890	4	18	from	impact	1520:1525	arg1	FucT-VII					1561:1568	FucT-VII	1561:1568	FucT-VII	1561:1568	All combined, our results show a differential functional impact of N-glycosylation on C2GnT-1 and FucT-VII and disclose that a strongly reduced FucT-VII activity retains the ability to fucosylate PSGL-1 on the core2-based binding site(s) for the three selectins.
15926890	4	18	from	impact	1520:1525	arg1	C2GnT-1					1549:1555	C2GnT-1	1549:1555	C2GnT-1	1549:1555	All combined, our results show a differential functional impact of N-glycosylation on C2GnT-1 and FucT-VII and disclose that a strongly reduced FucT-VII activity retains the ability to fucosylate PSGL-1 on the core2-based binding site(s) for the three selectins.
15926890	3	19	theme	L-selectin	1296:1305	arg1	binding					1307:1313	L-selectin binding	1296:1313	L-selectin binding	1296:1313	We found that (i) both enzymes have their two N-glycosylation sites occupied, (ii) for C2GnT-I, the N-glycan chain linked to Asn-95 significantly contributes to the synthesis of functional PSGL-1 and is required to localize the enzyme to the cis/medial-Golgi compartment, (iii) all N-glycosylation-deficient proteins of FucT-VII displayr a dramatic impairment of their in vitro enzymatic activities, but retain their ability to fucosylate the core2-modified PSGL-I and to generate P- and L-selectin binding, and (iv) the glycomutants of FucT-VII fail to synthesize sialyl-Lewis x or to generate E-selectin binding unless core2-modified PSGL-1 is present.
15926890	1	20	theme	drug	499:502	arg1	targets					504:510	good drug targets	494:510	good drug targets for the treatment of inflammatory disorders and other pathologies involving selectins	494:596	C2GnT-I [core2 beta(1,6)-N-acetyglucosaminyltransferase-I] and FucT-VII [alpha(1,3)-fucosyltransferase-VII] are the key enzymes for the biosynthesis of sialyl-Lewis x determinants on selectin ligands and therefore they represent good drug targets for the treatment of inflammatory disorders and other pathologies involving selectins.
15926890	3	21	dep	sites	870:874	arg1	occupied					876:883	occupied	876:883	occupied	876:883	We found that (i) both enzymes have their two N-glycosylation sites occupied, (ii) for C2GnT-I, the N-glycan chain linked to Asn-95 significantly contributes to the synthesis of functional PSGL-1 and is required to localize the enzyme to the cis/medial-Golgi compartment, (iii) all N-glycosylation-deficient proteins of FucT-VII displayr a dramatic impairment of their in vitro enzymatic activities, but retain their ability to fucosylate the core2-modified PSGL-I and to generate P- and L-selectin binding, and (iv) the glycomutants of FucT-VII fail to synthesize sialyl-Lewis x or to generate E-selectin binding unless core2-modified PSGL-1 is present.
15926890	3	22	dep	in	1177:1178	arg1	vitro					1180:1184	vitro	1180:1184	vitro	1180:1184	We found that (i) both enzymes have their two N-glycosylation sites occupied, (ii) for C2GnT-I, the N-glycan chain linked to Asn-95 significantly contributes to the synthesis of functional PSGL-1 and is required to localize the enzyme to the cis/medial-Golgi compartment, (iii) all N-glycosylation-deficient proteins of FucT-VII displayr a dramatic impairment of their in vitro enzymatic activities, but retain their ability to fucosylate the core2-modified PSGL-I and to generate P- and L-selectin binding, and (iv) the glycomutants of FucT-VII fail to synthesize sialyl-Lewis x or to generate E-selectin binding unless core2-modified PSGL-1 is present.
15926890	3	23	dep	compartment	1067:1077	arg1	impairment					1157:1166	a dramatic impairment	1146:1166	a dramatic impairment of their in vitro enzymatic activities	1146:1205	We found that (i) both enzymes have their two N-glycosylation sites occupied, (ii) for C2GnT-I, the N-glycan chain linked to Asn-95 significantly contributes to the synthesis of functional PSGL-1 and is required to localize the enzyme to the cis/medial-Golgi compartment, (iii) all N-glycosylation-deficient proteins of FucT-VII displayr a dramatic impairment of their in vitro enzymatic activities, but retain their ability to fucosylate the core2-modified PSGL-I and to generate P- and L-selectin binding, and (iv) the glycomutants of FucT-VII fail to synthesize sialyl-Lewis x or to generate E-selectin binding unless core2-modified PSGL-1 is present.
15926890	4	24	theme	N-glycosylation	1530:1544	arg1	impact					1520:1525	a differential functional impact	1494:1525	a differential functional impact of N-glycosylation on C2GnT-1 and FucT-VII	1494:1568	All combined, our results show a differential functional impact of N-glycosylation on C2GnT-1 and FucT-VII and disclose that a strongly reduced FucT-VII activity retains the ability to fucosylate PSGL-1 on the core2-based binding site(s) for the three selectins.
15926890	1	25	theme	FucT-VII	328:335	arg1	-N-acetyglucosaminyltransferase-I					289:321	C2GnT-I [core2 beta(1,6)-N-acetyglucosaminyltransferase-I	265:321	C2GnT-I [core2 beta(1,6)-N-acetyglucosaminyltransferase-I	265:321	C2GnT-I [core2 beta(1,6)-N-acetyglucosaminyltransferase-I] and FucT-VII [alpha(1,3)-fucosyltransferase-VII] are the key enzymes for the biosynthesis of sialyl-Lewis x determinants on selectin ligands and therefore they represent good drug targets for the treatment of inflammatory disorders and other pathologies involving selectins.
15926890	1	25	theme	FucT-VII	328:335	arg1	enzymes					385:391	the key enzymes	377:391	the key enzymes for the biosynthesis of sialyl-Lewis x determinants on selectin ligands	377:463	C2GnT-I [core2 beta(1,6)-N-acetyglucosaminyltransferase-I] and FucT-VII [alpha(1,3)-fucosyltransferase-VII] are the key enzymes for the biosynthesis of sialyl-Lewis x determinants on selectin ligands and therefore they represent good drug targets for the treatment of inflammatory disorders and other pathologies involving selectins.
15926890	1	25	theme	FucT-VII	328:335	arg1	-fucosyltransferase-VII					348:370	FucT-VII [alpha(1,3)-fucosyltransferase-VII	328:370	FucT-VII [alpha(1,3)-fucosyltransferase-VII	328:370	C2GnT-I [core2 beta(1,6)-N-acetyglucosaminyltransferase-I] and FucT-VII [alpha(1,3)-fucosyltransferase-VII] are the key enzymes for the biosynthesis of sialyl-Lewis x determinants on selectin ligands and therefore they represent good drug targets for the treatment of inflammatory disorders and other pathologies involving selectins.
15926890	0	26	theme	glycoprotein	191:202	arg1	PSGL-1					214:219	PSGL-1	214:219	PSGL-1	214:219	N-glycans of core2 beta(1,6)-N-acetylglucosaminyltransferase-I (C2GnT-I) but not those of alpha(1,3)-fucosyltransferase-VII (FucT-VII) are required for the synthesis of functional P-selectin glycoprotein ligand-1 (PSGL-1): effects on P-, L- and E-selectin binding.
15926890	0	26	theme	glycoprotein	191:202	arg1	ligand-1					204:211	functional P-selectin glycoprotein ligand-1	169:211	functional P-selectin glycoprotein ligand-1 (PSGL-1)	169:220	N-glycans of core2 beta(1,6)-N-acetylglucosaminyltransferase-I (C2GnT-I) but not those of alpha(1,3)-fucosyltransferase-VII (FucT-VII) are required for the synthesis of functional P-selectin glycoprotein ligand-1 (PSGL-1): effects on P-, L- and E-selectin binding.
15926890	2	27	theme	FucT-VII	698:705	arg1	ability					675:681	the ability	671:681	the ability of C2GnT-I and FucT-VII to generate functional selectin ligands, particularly the PSGL-1 (P-selectin glycoprotein ligand-1)	671:805	In the present study, we examined the importance of N-glycosylation for the ability of C2GnT-I and FucT-VII to generate functional selectin ligands, particularly the PSGL-1 (P-selectin glycoprotein ligand-1).
15926890	3	28	theme	activities	1196:1205	arg1	impairment					1157:1166	a dramatic impairment	1146:1166	a dramatic impairment of their in vitro enzymatic activities	1146:1205	We found that (i) both enzymes have their two N-glycosylation sites occupied, (ii) for C2GnT-I, the N-glycan chain linked to Asn-95 significantly contributes to the synthesis of functional PSGL-1 and is required to localize the enzyme to the cis/medial-Golgi compartment, (iii) all N-glycosylation-deficient proteins of FucT-VII displayr a dramatic impairment of their in vitro enzymatic activities, but retain their ability to fucosylate the core2-modified PSGL-I and to generate P- and L-selectin binding, and (iv) the glycomutants of FucT-VII fail to synthesize sialyl-Lewis x or to generate E-selectin binding unless core2-modified PSGL-1 is present.
15926890	0	29	theme	P-selectin	180:189	arg1	PSGL-1					214:219	PSGL-1	214:219	PSGL-1	214:219	N-glycans of core2 beta(1,6)-N-acetylglucosaminyltransferase-I (C2GnT-I) but not those of alpha(1,3)-fucosyltransferase-VII (FucT-VII) are required for the synthesis of functional P-selectin glycoprotein ligand-1 (PSGL-1): effects on P-, L- and E-selectin binding.
15926890	0	29	theme	P-selectin	180:189	arg1	ligand-1					204:211	functional P-selectin glycoprotein ligand-1	169:211	functional P-selectin glycoprotein ligand-1 (PSGL-1)	169:220	N-glycans of core2 beta(1,6)-N-acetylglucosaminyltransferase-I (C2GnT-I) but not those of alpha(1,3)-fucosyltransferase-VII (FucT-VII) are required for the synthesis of functional P-selectin glycoprotein ligand-1 (PSGL-1): effects on P-, L- and E-selectin binding.
15926890	1	30	theme	sialyl-Lewis	417:428	arg1	determinants					432:443	sialyl-Lewis x determinants	417:443	sialyl-Lewis x determinants on selectin ligands	417:463	C2GnT-I [core2 beta(1,6)-N-acetyglucosaminyltransferase-I] and FucT-VII [alpha(1,3)-fucosyltransferase-VII] are the key enzymes for the biosynthesis of sialyl-Lewis x determinants on selectin ligands and therefore they represent good drug targets for the treatment of inflammatory disorders and other pathologies involving selectins.
15926890	4	31	theme	FucT-VII	1607:1614	arg1	activity					1616:1623	a strongly reduced FucT-VII activity	1588:1623	a strongly reduced FucT-VII activity	1588:1623	All combined, our results show a differential functional impact of N-glycosylation on C2GnT-1 and FucT-VII and disclose that a strongly reduced FucT-VII activity retains the ability to fucosylate PSGL-1 on the core2-based binding site(s) for the three selectins.
15926890	3	32	dep	fail	1354:1357	arg1	iv					1321:1322	iv	1321:1322	iv	1321:1322	We found that (i) both enzymes have their two N-glycosylation sites occupied, (ii) for C2GnT-I, the N-glycan chain linked to Asn-95 significantly contributes to the synthesis of functional PSGL-1 and is required to localize the enzyme to the cis/medial-Golgi compartment, (iii) all N-glycosylation-deficient proteins of FucT-VII displayr a dramatic impairment of their in vitro enzymatic activities, but retain their ability to fucosylate the core2-modified PSGL-I and to generate P- and L-selectin binding, and (iv) the glycomutants of FucT-VII fail to synthesize sialyl-Lewis x or to generate E-selectin binding unless core2-modified PSGL-1 is present.
15926890	0	33	theme	beta	19:22	arg1	C2GnT-I					64:70	C2GnT-I	64:70	C2GnT-I	64:70	N-glycans of core2 beta(1,6)-N-acetylglucosaminyltransferase-I (C2GnT-I) but not those of alpha(1,3)-fucosyltransferase-VII (FucT-VII) are required for the synthesis of functional P-selectin glycoprotein ligand-1 (PSGL-1): effects on P-, L- and E-selectin binding.
15926890	0	33	theme	beta	19:22	arg1	-N-acetylglucosaminyltransferase-I					28:61	core2 beta(1,6)-N-acetylglucosaminyltransferase-I	13:61	core2 beta(1,6)-N-acetylglucosaminyltransferase-I (C2GnT-I) but not those of alpha(1,3)-fucosyltransferase-VII (FucT-VII)	13:133	N-glycans of core2 beta(1,6)-N-acetylglucosaminyltransferase-I (C2GnT-I) but not those of alpha(1,3)-fucosyltransferase-VII (FucT-VII) are required for the synthesis of functional P-selectin glycoprotein ligand-1 (PSGL-1): effects on P-, L- and E-selectin binding.
15926890	1	34	theme	x	430:430	arg1	determinants					432:443	sialyl-Lewis x determinants	417:443	sialyl-Lewis x determinants on selectin ligands	417:463	C2GnT-I [core2 beta(1,6)-N-acetyglucosaminyltransferase-I] and FucT-VII [alpha(1,3)-fucosyltransferase-VII] are the key enzymes for the biosynthesis of sialyl-Lewis x determinants on selectin ligands and therefore they represent good drug targets for the treatment of inflammatory disorders and other pathologies involving selectins.
15926890	4	35	theme	functional	1509:1518	arg1	impact					1520:1525	a differential functional impact	1494:1525	a differential functional impact of N-glycosylation on C2GnT-1 and FucT-VII	1494:1568	All combined, our results show a differential functional impact of N-glycosylation on C2GnT-1 and FucT-VII and disclose that a strongly reduced FucT-VII activity retains the ability to fucosylate PSGL-1 on the core2-based binding site(s) for the three selectins.
15926890	3	36	theme	FucT-VII	1345:1352	arg1	glycomutants					1329:1340	the glycomutants	1325:1340	the glycomutants of FucT-VII	1325:1352	We found that (i) both enzymes have their two N-glycosylation sites occupied, (ii) for C2GnT-I, the N-glycan chain linked to Asn-95 significantly contributes to the synthesis of functional PSGL-1 and is required to localize the enzyme to the cis/medial-Golgi compartment, (iii) all N-glycosylation-deficient proteins of FucT-VII displayr a dramatic impairment of their in vitro enzymatic activities, but retain their ability to fucosylate the core2-modified PSGL-I and to generate P- and L-selectin binding, and (iv) the glycomutants of FucT-VII fail to synthesize sialyl-Lewis x or to generate E-selectin binding unless core2-modified PSGL-1 is present.
15926890	0	37	theme	core2	13:17	arg1	1,6					24:26	1,6	24:26	1,6	24:26	N-glycans of core2 beta(1,6)-N-acetylglucosaminyltransferase-I (C2GnT-I) but not those of alpha(1,3)-fucosyltransferase-VII (FucT-VII) are required for the synthesis of functional P-selectin glycoprotein ligand-1 (PSGL-1): effects on P-, L- and E-selectin binding.
15926890	0	37	theme	core2	13:17	arg1	beta					19:22	core2 beta	13:22	core2 beta(1,6)-N-acetylglucosaminyltransferase-I (C2GnT-I) but not those of alpha(1,3)-fucosyltransferase-VII (FucT-VII)	13:133	N-glycans of core2 beta(1,6)-N-acetylglucosaminyltransferase-I (C2GnT-I) but not those of alpha(1,3)-fucosyltransferase-VII (FucT-VII) are required for the synthesis of functional P-selectin glycoprotein ligand-1 (PSGL-1): effects on P-, L- and E-selectin binding.
15926890	2	38	theme	N-glycosylation	651:665	arg1	importance					637:646	the importance	633:646	the importance of N-glycosylation for the ability of C2GnT-I and FucT-VII to generate functional selectin ligands, particularly the PSGL-1 (P-selectin glycoprotein ligand-1)	633:805	In the present study, we examined the importance of N-glycosylation for the ability of C2GnT-I and FucT-VII to generate functional selectin ligands, particularly the PSGL-1 (P-selectin glycoprotein ligand-1).
15926890	1	39	theme	[alpha	337:342	arg1	-N-acetyglucosaminyltransferase-I					289:321	C2GnT-I [core2 beta(1,6)-N-acetyglucosaminyltransferase-I	265:321	C2GnT-I [core2 beta(1,6)-N-acetyglucosaminyltransferase-I	265:321	C2GnT-I [core2 beta(1,6)-N-acetyglucosaminyltransferase-I] and FucT-VII [alpha(1,3)-fucosyltransferase-VII] are the key enzymes for the biosynthesis of sialyl-Lewis x determinants on selectin ligands and therefore they represent good drug targets for the treatment of inflammatory disorders and other pathologies involving selectins.
15926890	1	39	theme	[alpha	337:342	arg1	enzymes					385:391	the key enzymes	377:391	the key enzymes for the biosynthesis of sialyl-Lewis x determinants on selectin ligands	377:463	C2GnT-I [core2 beta(1,6)-N-acetyglucosaminyltransferase-I] and FucT-VII [alpha(1,3)-fucosyltransferase-VII] are the key enzymes for the biosynthesis of sialyl-Lewis x determinants on selectin ligands and therefore they represent good drug targets for the treatment of inflammatory disorders and other pathologies involving selectins.
15926890	1	39	theme	[alpha	337:342	arg1	-fucosyltransferase-VII					348:370	FucT-VII [alpha(1,3)-fucosyltransferase-VII	328:370	FucT-VII [alpha(1,3)-fucosyltransferase-VII	328:370	C2GnT-I [core2 beta(1,6)-N-acetyglucosaminyltransferase-I] and FucT-VII [alpha(1,3)-fucosyltransferase-VII] are the key enzymes for the biosynthesis of sialyl-Lewis x determinants on selectin ligands and therefore they represent good drug targets for the treatment of inflammatory disorders and other pathologies involving selectins.
15926890	2	40	theme	selectin	730:737	arg1	ligands					739:745	functional selectin ligands	719:745	functional selectin ligands	719:745	In the present study, we examined the importance of N-glycosylation for the ability of C2GnT-I and FucT-VII to generate functional selectin ligands, particularly the PSGL-1 (P-selectin glycoprotein ligand-1).
15926890	2	40	theme	selectin	730:737	arg1	PSGL-1					765:770	the PSGL-1	761:770	the PSGL-1 (P-selectin glycoprotein ligand-1)	761:805	In the present study, we examined the importance of N-glycosylation for the ability of C2GnT-I and FucT-VII to generate functional selectin ligands, particularly the PSGL-1 (P-selectin glycoprotein ligand-1).
15926890	1	41	from	ligands	457:463	arg1	biosynthesis					401:412	the biosynthesis	397:412	the biosynthesis of sialyl-Lewis x determinants on selectin ligands	397:463	C2GnT-I [core2 beta(1,6)-N-acetyglucosaminyltransferase-I] and FucT-VII [alpha(1,3)-fucosyltransferase-VII] are the key enzymes for the biosynthesis of sialyl-Lewis x determinants on selectin ligands and therefore they represent good drug targets for the treatment of inflammatory disorders and other pathologies involving selectins.
15926890	3	42	theme	N-glycosylation	854:868	arg1	sites					870:874	two N-glycosylation sites	850:874	their two N-glycosylation sites occupied, (ii) for C2GnT-I, the N-glycan chain linked to Asn-95 significantly contributes to the synthesis of functional PSGL-1 and is required to localize the enzyme to the cis/medial-Golgi compartment, (iii) all N-glycosylation-deficient proteins of FucT-VII displayr a dramatic impairment of their in vitro enzymatic activities, but retain their ability to fucosylate the core2-modified PSGL-I and to generate P- and L-selectin binding, and (iv) the glycomutants of FucT-VII fail to synthesize sialyl-Lewis x or to generate E-selectin binding unless core2-modified PSGL-1 is present	844:1460	We found that (i) both enzymes have their two N-glycosylation sites occupied, (ii) for C2GnT-I, the N-glycan chain linked to Asn-95 significantly contributes to the synthesis of functional PSGL-1 and is required to localize the enzyme to the cis/medial-Golgi compartment, (iii) all N-glycosylation-deficient proteins of FucT-VII displayr a dramatic impairment of their in vitro enzymatic activities, but retain their ability to fucosylate the core2-modified PSGL-I and to generate P- and L-selectin binding, and (iv) the glycomutants of FucT-VII fail to synthesize sialyl-Lewis x or to generate E-selectin binding unless core2-modified PSGL-1 is present.
15926890	3	43	theme	E-selectin	1403:1412	arg1	binding					1414:1420	E-selectin binding	1403:1420	E-selectin binding	1403:1420	We found that (i) both enzymes have their two N-glycosylation sites occupied, (ii) for C2GnT-I, the N-glycan chain linked to Asn-95 significantly contributes to the synthesis of functional PSGL-1 and is required to localize the enzyme to the cis/medial-Golgi compartment, (iii) all N-glycosylation-deficient proteins of FucT-VII displayr a dramatic impairment of their in vitro enzymatic activities, but retain their ability to fucosylate the core2-modified PSGL-I and to generate P- and L-selectin binding, and (iv) the glycomutants of FucT-VII fail to synthesize sialyl-Lewis x or to generate E-selectin binding unless core2-modified PSGL-1 is present.
15926890	3	44	gly	fucosylate	1236:1245	arg1	PSGL-I					1266:1271	the core2-modified PSGL-I	1247:1271	the core2-modified PSGL-I	1247:1271	We found that (i) both enzymes have their two N-glycosylation sites occupied, (ii) for C2GnT-I, the N-glycan chain linked to Asn-95 significantly contributes to the synthesis of functional PSGL-1 and is required to localize the enzyme to the cis/medial-Golgi compartment, (iii) all N-glycosylation-deficient proteins of FucT-VII displayr a dramatic impairment of their in vitro enzymatic activities, but retain their ability to fucosylate the core2-modified PSGL-I and to generate P- and L-selectin binding, and (iv) the glycomutants of FucT-VII fail to synthesize sialyl-Lewis x or to generate E-selectin binding unless core2-modified PSGL-1 is present.
15926890	1	45	theme	inflammatory	533:544	arg1	disorders					546:554	inflammatory disorders	533:554	inflammatory disorders	533:554	C2GnT-I [core2 beta(1,6)-N-acetyglucosaminyltransferase-I] and FucT-VII [alpha(1,3)-fucosyltransferase-VII] are the key enzymes for the biosynthesis of sialyl-Lewis x determinants on selectin ligands and therefore they represent good drug targets for the treatment of inflammatory disorders and other pathologies involving selectins.
15926890	1	46	from	determinants	432:443	arg1	ligands					457:463	selectin ligands	448:463	selectin ligands	448:463	C2GnT-I [core2 beta(1,6)-N-acetyglucosaminyltransferase-I] and FucT-VII [alpha(1,3)-fucosyltransferase-VII] are the key enzymes for the biosynthesis of sialyl-Lewis x determinants on selectin ligands and therefore they represent good drug targets for the treatment of inflammatory disorders and other pathologies involving selectins.
15926890	2	47	theme	P-selectin	773:782	arg1	ligand-1					797:804	P-selectin glycoprotein ligand-1	773:804	P-selectin glycoprotein ligand-1	773:804	In the present study, we examined the importance of N-glycosylation for the ability of C2GnT-I and FucT-VII to generate functional selectin ligands, particularly the PSGL-1 (P-selectin glycoprotein ligand-1).
15926890	2	47	theme	P-selectin	773:782	arg1	PSGL-1					765:770	the PSGL-1	761:770	the PSGL-1 (P-selectin glycoprotein ligand-1)	761:805	In the present study, we examined the importance of N-glycosylation for the ability of C2GnT-I and FucT-VII to generate functional selectin ligands, particularly the PSGL-1 (P-selectin glycoprotein ligand-1).
15926890	3	48	theme	enzymatic	1186:1194	arg1	activities					1196:1205	their in vitro enzymatic activities	1171:1205	their in vitro enzymatic activities	1171:1205	We found that (i) both enzymes have their two N-glycosylation sites occupied, (ii) for C2GnT-I, the N-glycan chain linked to Asn-95 significantly contributes to the synthesis of functional PSGL-1 and is required to localize the enzyme to the cis/medial-Golgi compartment, (iii) all N-glycosylation-deficient proteins of FucT-VII displayr a dramatic impairment of their in vitro enzymatic activities, but retain their ability to fucosylate the core2-modified PSGL-I and to generate P- and L-selectin binding, and (iv) the glycomutants of FucT-VII fail to synthesize sialyl-Lewis x or to generate E-selectin binding unless core2-modified PSGL-1 is present.
15926890	1	49	theme	1,3	344:346	arg1	-N-acetyglucosaminyltransferase-I					289:321	C2GnT-I [core2 beta(1,6)-N-acetyglucosaminyltransferase-I	265:321	C2GnT-I [core2 beta(1,6)-N-acetyglucosaminyltransferase-I	265:321	C2GnT-I [core2 beta(1,6)-N-acetyglucosaminyltransferase-I] and FucT-VII [alpha(1,3)-fucosyltransferase-VII] are the key enzymes for the biosynthesis of sialyl-Lewis x determinants on selectin ligands and therefore they represent good drug targets for the treatment of inflammatory disorders and other pathologies involving selectins.
15926890	1	49	theme	1,3	344:346	arg1	enzymes					385:391	the key enzymes	377:391	the key enzymes for the biosynthesis of sialyl-Lewis x determinants on selectin ligands	377:463	C2GnT-I [core2 beta(1,6)-N-acetyglucosaminyltransferase-I] and FucT-VII [alpha(1,3)-fucosyltransferase-VII] are the key enzymes for the biosynthesis of sialyl-Lewis x determinants on selectin ligands and therefore they represent good drug targets for the treatment of inflammatory disorders and other pathologies involving selectins.
15926890	1	49	theme	1,3	344:346	arg1	-fucosyltransferase-VII					348:370	FucT-VII [alpha(1,3)-fucosyltransferase-VII	328:370	FucT-VII [alpha(1,3)-fucosyltransferase-VII	328:370	C2GnT-I [core2 beta(1,6)-N-acetyglucosaminyltransferase-I] and FucT-VII [alpha(1,3)-fucosyltransferase-VII] are the key enzymes for the biosynthesis of sialyl-Lewis x determinants on selectin ligands and therefore they represent good drug targets for the treatment of inflammatory disorders and other pathologies involving selectins.
15926890	1	50	theme	determinants	432:443	arg1	biosynthesis					401:412	the biosynthesis	397:412	the biosynthesis of sialyl-Lewis x determinants on selectin ligands	397:463	C2GnT-I [core2 beta(1,6)-N-acetyglucosaminyltransferase-I] and FucT-VII [alpha(1,3)-fucosyltransferase-VII] are the key enzymes for the biosynthesis of sialyl-Lewis x determinants on selectin ligands and therefore they represent good drug targets for the treatment of inflammatory disorders and other pathologies involving selectins.
15926890	0	51	gly	glycoprotein	191:202	arg1	glycoprotein					191:202	functional P-selectin glycoprotein ligand-1	169:211	functional P-selectin glycoprotein ligand-1 (PSGL-1)	169:220	N-glycans of core2 beta(1,6)-N-acetylglucosaminyltransferase-I (C2GnT-I) but not those of alpha(1,3)-fucosyltransferase-VII (FucT-VII) are required for the synthesis of functional P-selectin glycoprotein ligand-1 (PSGL-1): effects on P-, L- and E-selectin binding.
15926890	0	52	theme	-N-acetylglucosaminyltransferase-I	28:61	arg1	N-glycans					0:8	N-glycans	0:8	N-glycans of core2 beta(1,6)-N-acetylglucosaminyltransferase-I (C2GnT-I) but not those of alpha(1,3)-fucosyltransferase-VII (FucT-VII)	0:133	N-glycans of core2 beta(1,6)-N-acetylglucosaminyltransferase-I (C2GnT-I) but not those of alpha(1,3)-fucosyltransferase-VII (FucT-VII) are required for the synthesis of functional P-selectin glycoprotein ligand-1 (PSGL-1): effects on P-, L- and E-selectin binding.
15926890	3	53	theme	FucT-VII	1128:1135	arg1	displayr					1137:1144	FucT-VII displayr	1128:1144	FucT-VII displayr	1128:1144	We found that (i) both enzymes have their two N-glycosylation sites occupied, (ii) for C2GnT-I, the N-glycan chain linked to Asn-95 significantly contributes to the synthesis of functional PSGL-1 and is required to localize the enzyme to the cis/medial-Golgi compartment, (iii) all N-glycosylation-deficient proteins of FucT-VII displayr a dramatic impairment of their in vitro enzymatic activities, but retain their ability to fucosylate the core2-modified PSGL-I and to generate P- and L-selectin binding, and (iv) the glycomutants of FucT-VII fail to synthesize sialyl-Lewis x or to generate E-selectin binding unless core2-modified PSGL-1 is present.
15926890	3	54	dep	proteins	1116:1123	arg1	iii					1081:1083	iii	1081:1083	iii	1081:1083	We found that (i) both enzymes have their two N-glycosylation sites occupied, (ii) for C2GnT-I, the N-glycan chain linked to Asn-95 significantly contributes to the synthesis of functional PSGL-1 and is required to localize the enzyme to the cis/medial-Golgi compartment, (iii) all N-glycosylation-deficient proteins of FucT-VII displayr a dramatic impairment of their in vitro enzymatic activities, but retain their ability to fucosylate the core2-modified PSGL-I and to generate P- and L-selectin binding, and (iv) the glycomutants of FucT-VII fail to synthesize sialyl-Lewis x or to generate E-selectin binding unless core2-modified PSGL-1 is present.
15926890	4	55	theme	core2-based	1673:1683	arg1	site					1693:1696	the core2-based binding site	1669:1696	the core2-based binding site(s) for the three selectins	1669:1723	All combined, our results show a differential functional impact of N-glycosylation on C2GnT-1 and FucT-VII and disclose that a strongly reduced FucT-VII activity retains the ability to fucosylate PSGL-1 on the core2-based binding site(s) for the three selectins.
15926890	4	55	theme	core2-based	1673:1683	arg1	s					1698:1698	s	1698:1698	s	1698:1698	All combined, our results show a differential functional impact of N-glycosylation on C2GnT-1 and FucT-VII and disclose that a strongly reduced FucT-VII activity retains the ability to fucosylate PSGL-1 on the core2-based binding site(s) for the three selectins.
15926890	3	56	theme	in	1177:1178	arg1	activities					1196:1205	their in vitro enzymatic activities	1171:1205	their in vitro enzymatic activities	1171:1205	We found that (i) both enzymes have their two N-glycosylation sites occupied, (ii) for C2GnT-I, the N-glycan chain linked to Asn-95 significantly contributes to the synthesis of functional PSGL-1 and is required to localize the enzyme to the cis/medial-Golgi compartment, (iii) all N-glycosylation-deficient proteins of FucT-VII displayr a dramatic impairment of their in vitro enzymatic activities, but retain their ability to fucosylate the core2-modified PSGL-I and to generate P- and L-selectin binding, and (iv) the glycomutants of FucT-VII fail to synthesize sialyl-Lewis x or to generate E-selectin binding unless core2-modified PSGL-1 is present.
15926890	1	57	theme	C2GnT-I	265:271	arg1	-fucosyltransferase-VII					348:370	FucT-VII [alpha(1,3)-fucosyltransferase-VII	328:370	FucT-VII [alpha(1,3)-fucosyltransferase-VII	328:370	C2GnT-I [core2 beta(1,6)-N-acetyglucosaminyltransferase-I] and FucT-VII [alpha(1,3)-fucosyltransferase-VII] are the key enzymes for the biosynthesis of sialyl-Lewis x determinants on selectin ligands and therefore they represent good drug targets for the treatment of inflammatory disorders and other pathologies involving selectins.
15926890	1	57	theme	C2GnT-I	265:271	arg1	enzymes					385:391	the key enzymes	377:391	the key enzymes for the biosynthesis of sialyl-Lewis x determinants on selectin ligands	377:463	C2GnT-I [core2 beta(1,6)-N-acetyglucosaminyltransferase-I] and FucT-VII [alpha(1,3)-fucosyltransferase-VII] are the key enzymes for the biosynthesis of sialyl-Lewis x determinants on selectin ligands and therefore they represent good drug targets for the treatment of inflammatory disorders and other pathologies involving selectins.
15926890	1	57	theme	C2GnT-I	265:271	arg1	-N-acetyglucosaminyltransferase-I					289:321	C2GnT-I [core2 beta(1,6)-N-acetyglucosaminyltransferase-I	265:321	C2GnT-I [core2 beta(1,6)-N-acetyglucosaminyltransferase-I	265:321	C2GnT-I [core2 beta(1,6)-N-acetyglucosaminyltransferase-I] and FucT-VII [alpha(1,3)-fucosyltransferase-VII] are the key enzymes for the biosynthesis of sialyl-Lewis x determinants on selectin ligands and therefore they represent good drug targets for the treatment of inflammatory disorders and other pathologies involving selectins.
15926890	3	58	theme	core2-modified	1429:1442	arg1	PSGL-1					1444:1449	core2-modified PSGL-1	1429:1449	core2-modified PSGL-1	1429:1449	We found that (i) both enzymes have their two N-glycosylation sites occupied, (ii) for C2GnT-I, the N-glycan chain linked to Asn-95 significantly contributes to the synthesis of functional PSGL-1 and is required to localize the enzyme to the cis/medial-Golgi compartment, (iii) all N-glycosylation-deficient proteins of FucT-VII displayr a dramatic impairment of their in vitro enzymatic activities, but retain their ability to fucosylate the core2-modified PSGL-I and to generate P- and L-selectin binding, and (iv) the glycomutants of FucT-VII fail to synthesize sialyl-Lewis x or to generate E-selectin binding unless core2-modified PSGL-1 is present.
15926890	4	59	theme	reduced	1599:1605	arg1	activity					1616:1623	a strongly reduced FucT-VII activity	1588:1623	a strongly reduced FucT-VII activity	1588:1623	All combined, our results show a differential functional impact of N-glycosylation on C2GnT-1 and FucT-VII and disclose that a strongly reduced FucT-VII activity retains the ability to fucosylate PSGL-1 on the core2-based binding site(s) for the three selectins.
15926890	1	60	theme	selectin	448:455	arg1	ligands					457:463	selectin ligands	448:463	selectin ligands	448:463	C2GnT-I [core2 beta(1,6)-N-acetyglucosaminyltransferase-I] and FucT-VII [alpha(1,3)-fucosyltransferase-VII] are the key enzymes for the biosynthesis of sialyl-Lewis x determinants on selectin ligands and therefore they represent good drug targets for the treatment of inflammatory disorders and other pathologies involving selectins.
15926890	2	61	gly	glycoprotein	784:795	arg1	glycoprotein					784:795	P-selectin glycoprotein ligand-1	773:804	P-selectin glycoprotein ligand-1	773:804	In the present study, we examined the importance of N-glycosylation for the ability of C2GnT-I and FucT-VII to generate functional selectin ligands, particularly the PSGL-1 (P-selectin glycoprotein ligand-1).
15926890	1	62	theme	disorders	546:554	arg1	treatment					520:528	the treatment	516:528	the treatment of inflammatory disorders and other pathologies involving selectins	516:596	C2GnT-I [core2 beta(1,6)-N-acetyglucosaminyltransferase-I] and FucT-VII [alpha(1,3)-fucosyltransferase-VII] are the key enzymes for the biosynthesis of sialyl-Lewis x determinants on selectin ligands and therefore they represent good drug targets for the treatment of inflammatory disorders and other pathologies involving selectins.
15926890	1	63	theme	[core2	273:278	arg1	-fucosyltransferase-VII					348:370	FucT-VII [alpha(1,3)-fucosyltransferase-VII	328:370	FucT-VII [alpha(1,3)-fucosyltransferase-VII	328:370	C2GnT-I [core2 beta(1,6)-N-acetyglucosaminyltransferase-I] and FucT-VII [alpha(1,3)-fucosyltransferase-VII] are the key enzymes for the biosynthesis of sialyl-Lewis x determinants on selectin ligands and therefore they represent good drug targets for the treatment of inflammatory disorders and other pathologies involving selectins.
15926890	1	63	theme	[core2	273:278	arg1	enzymes					385:391	the key enzymes	377:391	the key enzymes for the biosynthesis of sialyl-Lewis x determinants on selectin ligands	377:463	C2GnT-I [core2 beta(1,6)-N-acetyglucosaminyltransferase-I] and FucT-VII [alpha(1,3)-fucosyltransferase-VII] are the key enzymes for the biosynthesis of sialyl-Lewis x determinants on selectin ligands and therefore they represent good drug targets for the treatment of inflammatory disorders and other pathologies involving selectins.
15926890	1	63	theme	[core2	273:278	arg1	-N-acetyglucosaminyltransferase-I					289:321	C2GnT-I [core2 beta(1,6)-N-acetyglucosaminyltransferase-I	265:321	C2GnT-I [core2 beta(1,6)-N-acetyglucosaminyltransferase-I	265:321	C2GnT-I [core2 beta(1,6)-N-acetyglucosaminyltransferase-I] and FucT-VII [alpha(1,3)-fucosyltransferase-VII] are the key enzymes for the biosynthesis of sialyl-Lewis x determinants on selectin ligands and therefore they represent good drug targets for the treatment of inflammatory disorders and other pathologies involving selectins.
15926890	3	64	theme	cis/medial-Golgi	1050:1065	arg1	compartment					1067:1077	the cis/medial-Golgi compartment	1046:1077	the cis/medial-Golgi compartment	1046:1077	We found that (i) both enzymes have their two N-glycosylation sites occupied, (ii) for C2GnT-I, the N-glycan chain linked to Asn-95 significantly contributes to the synthesis of functional PSGL-1 and is required to localize the enzyme to the cis/medial-Golgi compartment, (iii) all N-glycosylation-deficient proteins of FucT-VII displayr a dramatic impairment of their in vitro enzymatic activities, but retain their ability to fucosylate the core2-modified PSGL-I and to generate P- and L-selectin binding, and (iv) the glycomutants of FucT-VII fail to synthesize sialyl-Lewis x or to generate E-selectin binding unless core2-modified PSGL-1 is present.
15926890	3	64	theme	cis/medial-Golgi	1050:1065	arg1	proteins					1116:1123	all N-glycosylation-deficient proteins	1086:1123	(iii) all N-glycosylation-deficient proteins of FucT-VII displayr	1080:1144	We found that (i) both enzymes have their two N-glycosylation sites occupied, (ii) for C2GnT-I, the N-glycan chain linked to Asn-95 significantly contributes to the synthesis of functional PSGL-1 and is required to localize the enzyme to the cis/medial-Golgi compartment, (iii) all N-glycosylation-deficient proteins of FucT-VII displayr a dramatic impairment of their in vitro enzymatic activities, but retain their ability to fucosylate the core2-modified PSGL-I and to generate P- and L-selectin binding, and (iv) the glycomutants of FucT-VII fail to synthesize sialyl-Lewis x or to generate E-selectin binding unless core2-modified PSGL-1 is present.
15926890	3	65	theme	sialyl-Lewis	1373:1384	arg1	x					1386:1386	sialyl-Lewis x	1373:1386	sialyl-Lewis x	1373:1386	We found that (i) both enzymes have their two N-glycosylation sites occupied, (ii) for C2GnT-I, the N-glycan chain linked to Asn-95 significantly contributes to the synthesis of functional PSGL-1 and is required to localize the enzyme to the cis/medial-Golgi compartment, (iii) all N-glycosylation-deficient proteins of FucT-VII displayr a dramatic impairment of their in vitro enzymatic activities, but retain their ability to fucosylate the core2-modified PSGL-I and to generate P- and L-selectin binding, and (iv) the glycomutants of FucT-VII fail to synthesize sialyl-Lewis x or to generate E-selectin binding unless core2-modified PSGL-1 is present.
15926890	1	66	from	biosynthesis	401:412	arg1	ligands					457:463	selectin ligands	448:463	selectin ligands	448:463	C2GnT-I [core2 beta(1,6)-N-acetyglucosaminyltransferase-I] and FucT-VII [alpha(1,3)-fucosyltransferase-VII] are the key enzymes for the biosynthesis of sialyl-Lewis x determinants on selectin ligands and therefore they represent good drug targets for the treatment of inflammatory disorders and other pathologies involving selectins.
15926890	0	67	dep	P-	234:235	arg1	binding					256:262	binding	256:262	binding	256:262	N-glycans of core2 beta(1,6)-N-acetylglucosaminyltransferase-I (C2GnT-I) but not those of alpha(1,3)-fucosyltransferase-VII (FucT-VII) are required for the synthesis of functional P-selectin glycoprotein ligand-1 (PSGL-1): effects on P-, L- and E-selectin binding.
15926890	3	68	dep	have	839:842	arg1	both					826:829	both	826:829	both	826:829	We found that (i) both enzymes have their two N-glycosylation sites occupied, (ii) for C2GnT-I, the N-glycan chain linked to Asn-95 significantly contributes to the synthesis of functional PSGL-1 and is required to localize the enzyme to the cis/medial-Golgi compartment, (iii) all N-glycosylation-deficient proteins of FucT-VII displayr a dramatic impairment of their in vitro enzymatic activities, but retain their ability to fucosylate the core2-modified PSGL-I and to generate P- and L-selectin binding, and (iv) the glycomutants of FucT-VII fail to synthesize sialyl-Lewis x or to generate E-selectin binding unless core2-modified PSGL-1 is present.
15926890	3	68	dep	have	839:842	arg1	i					823:823	i	823:823	i	823:823	We found that (i) both enzymes have their two N-glycosylation sites occupied, (ii) for C2GnT-I, the N-glycan chain linked to Asn-95 significantly contributes to the synthesis of functional PSGL-1 and is required to localize the enzyme to the cis/medial-Golgi compartment, (iii) all N-glycosylation-deficient proteins of FucT-VII displayr a dramatic impairment of their in vitro enzymatic activities, but retain their ability to fucosylate the core2-modified PSGL-I and to generate P- and L-selectin binding, and (iv) the glycomutants of FucT-VII fail to synthesize sialyl-Lewis x or to generate E-selectin binding unless core2-modified PSGL-1 is present.
15926890	3	69	gly	N-glycosylation	854:868	arg2	sites					870:874	two N-glycosylation sites	850:874	their two N-glycosylation sites occupied, (ii) for C2GnT-I, the N-glycan chain linked to Asn-95 significantly contributes to the synthesis of functional PSGL-1 and is required to localize the enzyme to the cis/medial-Golgi compartment, (iii) all N-glycosylation-deficient proteins of FucT-VII displayr a dramatic impairment of their in vitro enzymatic activities, but retain their ability to fucosylate the core2-modified PSGL-I and to generate P- and L-selectin binding, and (iv) the glycomutants of FucT-VII fail to synthesize sialyl-Lewis x or to generate E-selectin binding unless core2-modified PSGL-1 is present	844:1460	We found that (i) both enzymes have their two N-glycosylation sites occupied, (ii) for C2GnT-I, the N-glycan chain linked to Asn-95 significantly contributes to the synthesis of functional PSGL-1 and is required to localize the enzyme to the cis/medial-Golgi compartment, (iii) all N-glycosylation-deficient proteins of FucT-VII displayr a dramatic impairment of their in vitro enzymatic activities, but retain their ability to fucosylate the core2-modified PSGL-I and to generate P- and L-selectin binding, and (iv) the glycomutants of FucT-VII fail to synthesize sialyl-Lewis x or to generate E-selectin binding unless core2-modified PSGL-1 is present.
15926890	3	69	gly	N-glycosylation	854:868	arg2	two					850:852	two	850:852	two	850:852	We found that (i) both enzymes have their two N-glycosylation sites occupied, (ii) for C2GnT-I, the N-glycan chain linked to Asn-95 significantly contributes to the synthesis of functional PSGL-1 and is required to localize the enzyme to the cis/medial-Golgi compartment, (iii) all N-glycosylation-deficient proteins of FucT-VII displayr a dramatic impairment of their in vitro enzymatic activities, but retain their ability to fucosylate the core2-modified PSGL-I and to generate P- and L-selectin binding, and (iv) the glycomutants of FucT-VII fail to synthesize sialyl-Lewis x or to generate E-selectin binding unless core2-modified PSGL-1 is present.
15926890	3	70	theme	core2-modified	1251:1264	arg1	PSGL-I					1266:1271	the core2-modified PSGL-I	1247:1271	the core2-modified PSGL-I	1247:1271	We found that (i) both enzymes have their two N-glycosylation sites occupied, (ii) for C2GnT-I, the N-glycan chain linked to Asn-95 significantly contributes to the synthesis of functional PSGL-1 and is required to localize the enzyme to the cis/medial-Golgi compartment, (iii) all N-glycosylation-deficient proteins of FucT-VII displayr a dramatic impairment of their in vitro enzymatic activities, but retain their ability to fucosylate the core2-modified PSGL-I and to generate P- and L-selectin binding, and (iv) the glycomutants of FucT-VII fail to synthesize sialyl-Lewis x or to generate E-selectin binding unless core2-modified PSGL-1 is present.
15926890	1	71	theme	other	560:564	arg1	pathologies					566:576	other pathologies	560:576	other pathologies	560:576	C2GnT-I [core2 beta(1,6)-N-acetyglucosaminyltransferase-I] and FucT-VII [alpha(1,3)-fucosyltransferase-VII] are the key enzymes for the biosynthesis of sialyl-Lewis x determinants on selectin ligands and therefore they represent good drug targets for the treatment of inflammatory disorders and other pathologies involving selectins.
15926890	3	72	attach	linked	923:928	arg2	chain					917:921	the N-glycan chain	904:921	the N-glycan chain linked to Asn-95	904:938	We found that (i) both enzymes have their two N-glycosylation sites occupied, (ii) for C2GnT-I, the N-glycan chain linked to Asn-95 significantly contributes to the synthesis of functional PSGL-1 and is required to localize the enzyme to the cis/medial-Golgi compartment, (iii) all N-glycosylation-deficient proteins of FucT-VII displayr a dramatic impairment of their in vitro enzymatic activities, but retain their ability to fucosylate the core2-modified PSGL-I and to generate P- and L-selectin binding, and (iv) the glycomutants of FucT-VII fail to synthesize sialyl-Lewis x or to generate E-selectin binding unless core2-modified PSGL-1 is present.
15926890	3	72	attach	linked	923:928	arg1	Asn-95					933:938	Asn-95	933:938	Asn-95	933:938	We found that (i) both enzymes have their two N-glycosylation sites occupied, (ii) for C2GnT-I, the N-glycan chain linked to Asn-95 significantly contributes to the synthesis of functional PSGL-1 and is required to localize the enzyme to the cis/medial-Golgi compartment, (iii) all N-glycosylation-deficient proteins of FucT-VII displayr a dramatic impairment of their in vitro enzymatic activities, but retain their ability to fucosylate the core2-modified PSGL-I and to generate P- and L-selectin binding, and (iv) the glycomutants of FucT-VII fail to synthesize sialyl-Lewis x or to generate E-selectin binding unless core2-modified PSGL-1 is present.
15926890	2	73	theme	C2GnT-I	686:692	arg1	ability					675:681	the ability	671:681	the ability of C2GnT-I and FucT-VII to generate functional selectin ligands, particularly the PSGL-1 (P-selectin glycoprotein ligand-1)	671:805	In the present study, we examined the importance of N-glycosylation for the ability of C2GnT-I and FucT-VII to generate functional selectin ligands, particularly the PSGL-1 (P-selectin glycoprotein ligand-1).
15926890	1	74	theme	pathologies	566:576	arg1	treatment					520:528	the treatment	516:528	the treatment of inflammatory disorders and other pathologies involving selectins	516:596	C2GnT-I [core2 beta(1,6)-N-acetyglucosaminyltransferase-I] and FucT-VII [alpha(1,3)-fucosyltransferase-VII] are the key enzymes for the biosynthesis of sialyl-Lewis x determinants on selectin ligands and therefore they represent good drug targets for the treatment of inflammatory disorders and other pathologies involving selectins.
15926890	3	75	theme	N-glycosylation-deficient	1090:1114	arg1	compartment					1067:1077	the cis/medial-Golgi compartment	1046:1077	the cis/medial-Golgi compartment	1046:1077	We found that (i) both enzymes have their two N-glycosylation sites occupied, (ii) for C2GnT-I, the N-glycan chain linked to Asn-95 significantly contributes to the synthesis of functional PSGL-1 and is required to localize the enzyme to the cis/medial-Golgi compartment, (iii) all N-glycosylation-deficient proteins of FucT-VII displayr a dramatic impairment of their in vitro enzymatic activities, but retain their ability to fucosylate the core2-modified PSGL-I and to generate P- and L-selectin binding, and (iv) the glycomutants of FucT-VII fail to synthesize sialyl-Lewis x or to generate E-selectin binding unless core2-modified PSGL-1 is present.
15926890	3	75	theme	N-glycosylation-deficient	1090:1114	arg1	proteins					1116:1123	all N-glycosylation-deficient proteins	1086:1123	(iii) all N-glycosylation-deficient proteins of FucT-VII displayr	1080:1144	We found that (i) both enzymes have their two N-glycosylation sites occupied, (ii) for C2GnT-I, the N-glycan chain linked to Asn-95 significantly contributes to the synthesis of functional PSGL-1 and is required to localize the enzyme to the cis/medial-Golgi compartment, (iii) all N-glycosylation-deficient proteins of FucT-VII displayr a dramatic impairment of their in vitro enzymatic activities, but retain their ability to fucosylate the core2-modified PSGL-I and to generate P- and L-selectin binding, and (iv) the glycomutants of FucT-VII fail to synthesize sialyl-Lewis x or to generate E-selectin binding unless core2-modified PSGL-1 is present.
15926890	1	76	theme	beta	280:283	arg1	-fucosyltransferase-VII					348:370	FucT-VII [alpha(1,3)-fucosyltransferase-VII	328:370	FucT-VII [alpha(1,3)-fucosyltransferase-VII	328:370	C2GnT-I [core2 beta(1,6)-N-acetyglucosaminyltransferase-I] and FucT-VII [alpha(1,3)-fucosyltransferase-VII] are the key enzymes for the biosynthesis of sialyl-Lewis x determinants on selectin ligands and therefore they represent good drug targets for the treatment of inflammatory disorders and other pathologies involving selectins.
15926890	1	76	theme	beta	280:283	arg1	enzymes					385:391	the key enzymes	377:391	the key enzymes for the biosynthesis of sialyl-Lewis x determinants on selectin ligands	377:463	C2GnT-I [core2 beta(1,6)-N-acetyglucosaminyltransferase-I] and FucT-VII [alpha(1,3)-fucosyltransferase-VII] are the key enzymes for the biosynthesis of sialyl-Lewis x determinants on selectin ligands and therefore they represent good drug targets for the treatment of inflammatory disorders and other pathologies involving selectins.
15926890	1	76	theme	beta	280:283	arg1	-N-acetyglucosaminyltransferase-I					289:321	C2GnT-I [core2 beta(1,6)-N-acetyglucosaminyltransferase-I	265:321	C2GnT-I [core2 beta(1,6)-N-acetyglucosaminyltransferase-I	265:321	C2GnT-I [core2 beta(1,6)-N-acetyglucosaminyltransferase-I] and FucT-VII [alpha(1,3)-fucosyltransferase-VII] are the key enzymes for the biosynthesis of sialyl-Lewis x determinants on selectin ligands and therefore they represent good drug targets for the treatment of inflammatory disorders and other pathologies involving selectins.
15926890	3	77	theme	dramatic	1148:1155	arg1	impairment					1157:1166	a dramatic impairment	1146:1166	a dramatic impairment of their in vitro enzymatic activities	1146:1205	We found that (i) both enzymes have their two N-glycosylation sites occupied, (ii) for C2GnT-I, the N-glycan chain linked to Asn-95 significantly contributes to the synthesis of functional PSGL-1 and is required to localize the enzyme to the cis/medial-Golgi compartment, (iii) all N-glycosylation-deficient proteins of FucT-VII displayr a dramatic impairment of their in vitro enzymatic activities, but retain their ability to fucosylate the core2-modified PSGL-I and to generate P- and L-selectin binding, and (iv) the glycomutants of FucT-VII fail to synthesize sialyl-Lewis x or to generate E-selectin binding unless core2-modified PSGL-1 is present.
15926890	3	78	dep	contributes	954:964	arg1	ii					887:888	ii	887:888	ii	887:888	We found that (i) both enzymes have their two N-glycosylation sites occupied, (ii) for C2GnT-I, the N-glycan chain linked to Asn-95 significantly contributes to the synthesis of functional PSGL-1 and is required to localize the enzyme to the cis/medial-Golgi compartment, (iii) all N-glycosylation-deficient proteins of FucT-VII displayr a dramatic impairment of their in vitro enzymatic activities, but retain their ability to fucosylate the core2-modified PSGL-I and to generate P- and L-selectin binding, and (iv) the glycomutants of FucT-VII fail to synthesize sialyl-Lewis x or to generate E-selectin binding unless core2-modified PSGL-1 is present.
15926890	3	79	theme	displayr	1137:1144	arg1	compartment					1067:1077	the cis/medial-Golgi compartment	1046:1077	the cis/medial-Golgi compartment	1046:1077	We found that (i) both enzymes have their two N-glycosylation sites occupied, (ii) for C2GnT-I, the N-glycan chain linked to Asn-95 significantly contributes to the synthesis of functional PSGL-1 and is required to localize the enzyme to the cis/medial-Golgi compartment, (iii) all N-glycosylation-deficient proteins of FucT-VII displayr a dramatic impairment of their in vitro enzymatic activities, but retain their ability to fucosylate the core2-modified PSGL-I and to generate P- and L-selectin binding, and (iv) the glycomutants of FucT-VII fail to synthesize sialyl-Lewis x or to generate E-selectin binding unless core2-modified PSGL-1 is present.
15926890	3	79	theme	displayr	1137:1144	arg1	proteins					1116:1123	all N-glycosylation-deficient proteins	1086:1123	(iii) all N-glycosylation-deficient proteins of FucT-VII displayr	1080:1144	We found that (i) both enzymes have their two N-glycosylation sites occupied, (ii) for C2GnT-I, the N-glycan chain linked to Asn-95 significantly contributes to the synthesis of functional PSGL-1 and is required to localize the enzyme to the cis/medial-Golgi compartment, (iii) all N-glycosylation-deficient proteins of FucT-VII displayr a dramatic impairment of their in vitro enzymatic activities, but retain their ability to fucosylate the core2-modified PSGL-I and to generate P- and L-selectin binding, and (iv) the glycomutants of FucT-VII fail to synthesize sialyl-Lewis x or to generate E-selectin binding unless core2-modified PSGL-1 is present.
29779877	0	0	theme	Corpus	114:119	arg1	Axons					130:134	Corpus Callosum Axons	114:134	Corpus Callosum Axons	114:134	Developmental Upregulation of Ephrin-B1 Silences Sema3C/Neuropilin-1 Signaling during Post-crossing Navigation of Corpus Callosum Axons.
29779877	6	1	gly	a N-glycosylation	1126:1142	arg2	N-139					1150:1154	N-139	1150:1154	N-139	1150:1154	This silencing activity is independent of Eph receptors and involves a N-glycosylation site (N-139) in the extracellular domain of Ephrin-B1.
29779877	6	1	gly	a N-glycosylation	1126:1142	arg2	site					1144:1147	a N-glycosylation site	1126:1147	a N-glycosylation site (N-139)	1126:1155	This silencing activity is independent of Eph receptors and involves a N-glycosylation site (N-139) in the extracellular domain of Ephrin-B1.
29779877	1	2	theme	cerebral	277:284	arg1	cortex					286:291	the cerebral cortex	273:291	the cerebral cortex	273:291	The corpus callosum is the largest commissure in the brain, whose main function is to ensure communication between homotopic regions of the cerebral cortex.
29779877	0	3	theme	Axons	130:134	arg1	Navigation					100:109	Post-crossing Navigation	86:109	Post-crossing Navigation of Corpus Callosum Axons	86:134	Developmental Upregulation of Ephrin-B1 Silences Sema3C/Neuropilin-1 Signaling during Post-crossing Navigation of Corpus Callosum Axons.
29779877	3	4	theme	key	507:509	arg1	question					525:532	a key developmental question	505:532	a key developmental question	505:532	A particular feature of this circuit, which raises a key developmental question, is that the outgoing trajectory of post-crossing CCAs is mirror-symmetric with the incoming trajectory of pre-crossing axons.
29779877	5	5	theme	surface	928:934	arg1	Ephrin-B1					944:952	the surface protein Ephrin-B1	924:952	the surface protein Ephrin-B1	924:952	This change is concomitant with an upregulation of the surface protein Ephrin-B1, which acts in CCAs to inhibit Sema3C signaling via interaction with the Neuropilin-1 (Nrp1) receptor.
29779877	3	6	theme	outgoing	547:554	arg1	mirror-symmetric					592:607	mirror-symmetric	592:607	mirror-symmetric	592:607	A particular feature of this circuit, which raises a key developmental question, is that the outgoing trajectory of post-crossing CCAs is mirror-symmetric with the incoming trajectory of pre-crossing axons.
29779877	3	6	theme	outgoing	547:554	arg1	trajectory					556:565	the outgoing trajectory	543:565	the outgoing trajectory of post-crossing CCAs	543:587	A particular feature of this circuit, which raises a key developmental question, is that the outgoing trajectory of post-crossing CCAs is mirror-symmetric with the incoming trajectory of pre-crossing axons.
29779877	1	7	theme	cortex	286:291	arg1	regions					262:268	homotopic regions	252:268	homotopic regions of the cerebral cortex	252:291	The corpus callosum is the largest commissure in the brain, whose main function is to ensure communication between homotopic regions of the cerebral cortex.
29779877	4	8	theme	guidance	733:740	arg1	cues					742:745	axon guidance cues	728:745	axon guidance cues	728:745	Here, we show that post-crossing CCAs switch off their response to axon guidance cues, among which the secreted Semaphorin-3C (Sema3C), that act as attractants for pre-crossing axons on their way to the midline.
29779877	5	9	theme	protein	936:942	arg1	Ephrin-B1					944:952	the surface protein Ephrin-B1	924:952	the surface protein Ephrin-B1	924:952	This change is concomitant with an upregulation of the surface protein Ephrin-B1, which acts in CCAs to inhibit Sema3C signaling via interaction with the Neuropilin-1 (Nrp1) receptor.
29779877	7	10	theme	molecular	1230:1238	arg1	mechanism					1240:1248	a molecular mechanism	1228:1248	a molecular mechanism	1228:1248	Together, our results reveal a molecular mechanism, involving interaction between the two unrelated guidance receptors Ephrin-B1 and Nrp1, that is used to control the navigation of post-crossing axons in the corpus callosum.
29779877	5	11	with	concomitant	888:898	arg1	upregulation					908:919	an upregulation	905:919	an upregulation	905:919	This change is concomitant with an upregulation of the surface protein Ephrin-B1, which acts in CCAs to inhibit Sema3C signaling via interaction with the Neuropilin-1 (Nrp1) receptor.
29779877	1	12	from	commissure	172:181	arg1	the brain					186:194	the brain	186:194	the brain	186:194	The corpus callosum is the largest commissure in the brain, whose main function is to ensure communication between homotopic regions of the cerebral cortex.
29779877	2	13	theme	fetal	301:305	arg1	development					307:317	fetal development	301:317	fetal development	301:317	During fetal development, corpus callosum axons (CCAs) grow toward and across the brain midline and then away on the contralateral hemisphere to their targets.
29779877	7	14	theme	unrelated	1289:1297	arg1	receptors					1308:1316	the two unrelated guidance receptors	1281:1316	the two unrelated guidance receptors Ephrin-B1 and Nrp1	1281:1335	Together, our results reveal a molecular mechanism, involving interaction between the two unrelated guidance receptors Ephrin-B1 and Nrp1, that is used to control the navigation of post-crossing axons in the corpus callosum.
29779877	7	14	theme	unrelated	1289:1297	arg1	Nrp1					1332:1335	Nrp1	1332:1335	Nrp1	1332:1335	Together, our results reveal a molecular mechanism, involving interaction between the two unrelated guidance receptors Ephrin-B1 and Nrp1, that is used to control the navigation of post-crossing axons in the corpus callosum.
29779877	7	14	theme	unrelated	1289:1297	arg1	Ephrin-B1					1318:1326	Ephrin-B1	1318:1326	Ephrin-B1	1318:1326	Together, our results reveal a molecular mechanism, involving interaction between the two unrelated guidance receptors Ephrin-B1 and Nrp1, that is used to control the navigation of post-crossing axons in the corpus callosum.
29779877	3	15	with	mirror-symmetric	592:607	arg1	trajectory					627:636	the incoming trajectory	614:636	the incoming trajectory of pre-crossing axons	614:658	A particular feature of this circuit, which raises a key developmental question, is that the outgoing trajectory of post-crossing CCAs is mirror-symmetric with the incoming trajectory of pre-crossing axons.
29779877	6	16	theme	a N-glycosylation	1126:1142	arg1	site					1144:1147	a N-glycosylation site	1126:1147	a N-glycosylation site (N-139)	1126:1155	This silencing activity is independent of Eph receptors and involves a N-glycosylation site (N-139) in the extracellular domain of Ephrin-B1.
29779877	6	16	theme	a N-glycosylation	1126:1142	arg1	N-139					1150:1154	N-139	1150:1154	N-139	1150:1154	This silencing activity is independent of Eph receptors and involves a N-glycosylation site (N-139) in the extracellular domain of Ephrin-B1.
29779877	7	17	theme	guidance	1299:1306	arg1	receptors					1308:1316	the two unrelated guidance receptors	1281:1316	the two unrelated guidance receptors Ephrin-B1 and Nrp1	1281:1335	Together, our results reveal a molecular mechanism, involving interaction between the two unrelated guidance receptors Ephrin-B1 and Nrp1, that is used to control the navigation of post-crossing axons in the corpus callosum.
29779877	7	17	theme	guidance	1299:1306	arg1	Nrp1					1332:1335	Nrp1	1332:1335	Nrp1	1332:1335	Together, our results reveal a molecular mechanism, involving interaction between the two unrelated guidance receptors Ephrin-B1 and Nrp1, that is used to control the navigation of post-crossing axons in the corpus callosum.
29779877	7	17	theme	guidance	1299:1306	arg1	Ephrin-B1					1318:1326	Ephrin-B1	1318:1326	Ephrin-B1	1318:1326	Together, our results reveal a molecular mechanism, involving interaction between the two unrelated guidance receptors Ephrin-B1 and Nrp1, that is used to control the navigation of post-crossing axons in the corpus callosum.
29779877	7	18	theme	corpus	1407:1412	arg1	callosum					1414:1421	the corpus callosum	1403:1421	the corpus callosum	1403:1421	Together, our results reveal a molecular mechanism, involving interaction between the two unrelated guidance receptors Ephrin-B1 and Nrp1, that is used to control the navigation of post-crossing axons in the corpus callosum.
29779877	0	19	dep	Corpus	114:119	arg1	Callosum					121:128	Callosum	121:128	Callosum	121:128	Developmental Upregulation of Ephrin-B1 Silences Sema3C/Neuropilin-1 Signaling during Post-crossing Navigation of Corpus Callosum Axons.
29779877	5	20	with	interaction	1006:1016	arg1	receptor					1047:1054	the Neuropilin-1 (Nrp1) receptor	1023:1054	the Neuropilin-1 (Nrp1) receptor	1023:1054	This change is concomitant with an upregulation of the surface protein Ephrin-B1, which acts in CCAs to inhibit Sema3C signaling via interaction with the Neuropilin-1 (Nrp1) receptor.
29779877	1	21	theme	main	203:206	arg1	function					208:215	function	208:215	function	208:215	The corpus callosum is the largest commissure in the brain, whose main function is to ensure communication between homotopic regions of the cerebral cortex.
29779877	0	22	theme	Developmental	0:12	arg1	Upregulation					14:25	Developmental Upregulation	0:25	Developmental Upregulation of Ephrin-B1	0:38	Developmental Upregulation of Ephrin-B1 Silences Sema3C/Neuropilin-1 Signaling during Post-crossing Navigation of Corpus Callosum Axons.
29779877	4	23	theme	pre-crossing	825:836	arg1	axons					838:842	pre-crossing axons	825:842	pre-crossing axons	825:842	Here, we show that post-crossing CCAs switch off their response to axon guidance cues, among which the secreted Semaphorin-3C (Sema3C), that act as attractants for pre-crossing axons on their way to the midline.
29779877	4	24	theme	axon	728:731	arg1	cues					742:745	axon guidance cues	728:745	axon guidance cues	728:745	Here, we show that post-crossing CCAs switch off their response to axon guidance cues, among which the secreted Semaphorin-3C (Sema3C), that act as attractants for pre-crossing axons on their way to the midline.
29779877	0	25	theme	Ephrin-B1	30:38	arg1	Upregulation					14:25	Developmental Upregulation	0:25	Developmental Upregulation of Ephrin-B1	0:38	Developmental Upregulation of Ephrin-B1 Silences Sema3C/Neuropilin-1 Signaling during Post-crossing Navigation of Corpus Callosum Axons.
29779877	6	26	theme	receptors	1103:1111	arg1	independent					1084:1094	independent	1084:1094	independent	1084:1094	This silencing activity is independent of Eph receptors and involves a N-glycosylation site (N-139) in the extracellular domain of Ephrin-B1.
29779877	7	27	dep	receptors	1308:1316	arg1	receptors					1308:1316	the two unrelated guidance receptors	1281:1316	the two unrelated guidance receptors Ephrin-B1 and Nrp1	1281:1335	Together, our results reveal a molecular mechanism, involving interaction between the two unrelated guidance receptors Ephrin-B1 and Nrp1, that is used to control the navigation of post-crossing axons in the corpus callosum.
29779877	7	27	dep	receptors	1308:1316	arg1	Nrp1					1332:1335	Nrp1	1332:1335	Nrp1	1332:1335	Together, our results reveal a molecular mechanism, involving interaction between the two unrelated guidance receptors Ephrin-B1 and Nrp1, that is used to control the navigation of post-crossing axons in the corpus callosum.
29779877	7	27	dep	receptors	1308:1316	arg1	Ephrin-B1					1318:1326	Ephrin-B1	1318:1326	Ephrin-B1	1318:1326	Together, our results reveal a molecular mechanism, involving interaction between the two unrelated guidance receptors Ephrin-B1 and Nrp1, that is used to control the navigation of post-crossing axons in the corpus callosum.
29779877	4	28	theme	secreted	764:771	arg1	Sema3C					788:793	Sema3C	788:793	Sema3C	788:793	Here, we show that post-crossing CCAs switch off their response to axon guidance cues, among which the secreted Semaphorin-3C (Sema3C), that act as attractants for pre-crossing axons on their way to the midline.
29779877	4	28	theme	secreted	764:771	arg1	Semaphorin-3C					773:785	the secreted Semaphorin-3C	760:785	the secreted Semaphorin-3C (Sema3C)	760:794	Here, we show that post-crossing CCAs switch off their response to axon guidance cues, among which the secreted Semaphorin-3C (Sema3C), that act as attractants for pre-crossing axons on their way to the midline.
29779877	3	29	theme	axons	654:658	arg1	trajectory					627:636	the incoming trajectory	614:636	the incoming trajectory of pre-crossing axons	614:658	A particular feature of this circuit, which raises a key developmental question, is that the outgoing trajectory of post-crossing CCAs is mirror-symmetric with the incoming trajectory of pre-crossing axons.
29779877	2	30	theme	corpus	320:325	arg1	CCAs					343:346	CCAs	343:346	CCAs	343:346	During fetal development, corpus callosum axons (CCAs) grow toward and across the brain midline and then away on the contralateral hemisphere to their targets.
29779877	2	30	theme	corpus	320:325	arg1	axons					336:340	corpus callosum axons	320:340	corpus callosum axons (CCAs)	320:347	During fetal development, corpus callosum axons (CCAs) grow toward and across the brain midline and then away on the contralateral hemisphere to their targets.
29779877	5	31	theme	Sema3C	985:990	arg1	signaling					992:1000	Sema3C signaling	985:1000	Sema3C signaling	985:1000	This change is concomitant with an upregulation of the surface protein Ephrin-B1, which acts in CCAs to inhibit Sema3C signaling via interaction with the Neuropilin-1 (Nrp1) receptor.
29779877	2	32	theme	contralateral	411:423	arg1	hemisphere					425:434	the contralateral hemisphere	407:434	the contralateral hemisphere to their targets	407:451	During fetal development, corpus callosum axons (CCAs) grow toward and across the brain midline and then away on the contralateral hemisphere to their targets.
29779877	0	33	theme	Sema3C/Neuropilin-1	49:67	arg1	Signaling					69:77	Sema3C/Neuropilin-1 Signaling	49:77	Sema3C/Neuropilin-1 Signaling	49:77	Developmental Upregulation of Ephrin-B1 Silences Sema3C/Neuropilin-1 Signaling during Post-crossing Navigation of Corpus Callosum Axons.
29779877	4	34	theme	post-crossing	680:692	arg1	CCAs					694:697	post-crossing CCAs	680:697	post-crossing CCAs	680:697	Here, we show that post-crossing CCAs switch off their response to axon guidance cues, among which the secreted Semaphorin-3C (Sema3C), that act as attractants for pre-crossing axons on their way to the midline.
29779877	5	35	theme	Nrp1	1041:1044	arg1	receptor					1047:1054	the Neuropilin-1 (Nrp1) receptor	1023:1054	the Neuropilin-1 (Nrp1) receptor	1023:1054	This change is concomitant with an upregulation of the surface protein Ephrin-B1, which acts in CCAs to inhibit Sema3C signaling via interaction with the Neuropilin-1 (Nrp1) receptor.
29779877	6	36	theme	Ephrin-B1	1188:1196	arg1	Ephrin-B1					1188:1196	Ephrin-B1	1188:1196	Ephrin-B1	1188:1196	This silencing activity is independent of Eph receptors and involves a N-glycosylation site (N-139) in the extracellular domain of Ephrin-B1.
29779877	6	36	theme	Ephrin-B1	1188:1196	arg1	domain					1178:1183	the extracellular domain	1160:1183	the extracellular domain of Ephrin-B1	1160:1196	This silencing activity is independent of Eph receptors and involves a N-glycosylation site (N-139) in the extracellular domain of Ephrin-B1.
29779877	3	37	theme	particular	456:465	arg1	feature					467:473	A particular feature	454:473	A particular feature	454:473	A particular feature of this circuit, which raises a key developmental question, is that the outgoing trajectory of post-crossing CCAs is mirror-symmetric with the incoming trajectory of pre-crossing axons.
29779877	5	38	theme	Neuropilin-1	1027:1038	arg1	receptor					1047:1054	the Neuropilin-1 (Nrp1) receptor	1023:1054	the Neuropilin-1 (Nrp1) receptor	1023:1054	This change is concomitant with an upregulation of the surface protein Ephrin-B1, which acts in CCAs to inhibit Sema3C signaling via interaction with the Neuropilin-1 (Nrp1) receptor.
29779877	3	39	theme	pre-crossing	641:652	arg1	axons					654:658	pre-crossing axons	641:658	pre-crossing axons	641:658	A particular feature of this circuit, which raises a key developmental question, is that the outgoing trajectory of post-crossing CCAs is mirror-symmetric with the incoming trajectory of pre-crossing axons.
29779877	3	40	theme	post-crossing	570:582	arg1	CCAs					584:587	post-crossing CCAs	570:587	post-crossing CCAs	570:587	A particular feature of this circuit, which raises a key developmental question, is that the outgoing trajectory of post-crossing CCAs is mirror-symmetric with the incoming trajectory of pre-crossing axons.
29779877	6	41	theme	silencing	1062:1070	arg1	activity					1072:1079	This silencing activity	1057:1079	This silencing activity	1057:1079	This silencing activity is independent of Eph receptors and involves a N-glycosylation site (N-139) in the extracellular domain of Ephrin-B1.
29779877	1	42	theme	corpus	141:146	arg1	commissure					172:181	the largest commissure	160:181	the largest commissure	160:181	The corpus callosum is the largest commissure in the brain, whose main function is to ensure communication between homotopic regions of the cerebral cortex.
29779877	1	42	theme	corpus	141:146	arg1	callosum					148:155	The corpus callosum	137:155	The corpus callosum	137:155	The corpus callosum is the largest commissure in the brain, whose main function is to ensure communication between homotopic regions of the cerebral cortex.
29779877	3	43	theme	CCAs	584:587	arg1	mirror-symmetric					592:607	mirror-symmetric	592:607	mirror-symmetric	592:607	A particular feature of this circuit, which raises a key developmental question, is that the outgoing trajectory of post-crossing CCAs is mirror-symmetric with the incoming trajectory of pre-crossing axons.
29779877	3	43	theme	CCAs	584:587	arg1	trajectory					556:565	the outgoing trajectory	543:565	the outgoing trajectory of post-crossing CCAs	543:587	A particular feature of this circuit, which raises a key developmental question, is that the outgoing trajectory of post-crossing CCAs is mirror-symmetric with the incoming trajectory of pre-crossing axons.
29779877	2	44	dep	corpus	320:325	arg1	callosum					327:334	callosum	327:334	callosum	327:334	During fetal development, corpus callosum axons (CCAs) grow toward and across the brain midline and then away on the contralateral hemisphere to their targets.
29779877	1	45	theme	largest	164:170	arg1	commissure					172:181	the largest commissure	160:181	the largest commissure	160:181	The corpus callosum is the largest commissure in the brain, whose main function is to ensure communication between homotopic regions of the cerebral cortex.
29779877	1	45	theme	largest	164:170	arg1	callosum					148:155	The corpus callosum	137:155	The corpus callosum	137:155	The corpus callosum is the largest commissure in the brain, whose main function is to ensure communication between homotopic regions of the cerebral cortex.
29779877	3	46	theme	incoming	618:625	arg1	trajectory					627:636	the incoming trajectory	614:636	the incoming trajectory of pre-crossing axons	614:658	A particular feature of this circuit, which raises a key developmental question, is that the outgoing trajectory of post-crossing CCAs is mirror-symmetric with the incoming trajectory of pre-crossing axons.
29779877	7	47	used	used	1346:1349	arg2	mechanism					1240:1248	a molecular mechanism	1228:1248	a molecular mechanism	1228:1248	Together, our results reveal a molecular mechanism, involving interaction between the two unrelated guidance receptors Ephrin-B1 and Nrp1, that is used to control the navigation of post-crossing axons in the corpus callosum.
29779877	7	48	theme	post-crossing	1380:1392	arg1	axons					1394:1398	post-crossing axons	1380:1398	post-crossing axons	1380:1398	Together, our results reveal a molecular mechanism, involving interaction between the two unrelated guidance receptors Ephrin-B1 and Nrp1, that is used to control the navigation of post-crossing axons in the corpus callosum.
29779877	6	49	theme	extracellular	1164:1176	arg1	Ephrin-B1					1188:1196	Ephrin-B1	1188:1196	Ephrin-B1	1188:1196	This silencing activity is independent of Eph receptors and involves a N-glycosylation site (N-139) in the extracellular domain of Ephrin-B1.
29779877	6	49	theme	extracellular	1164:1176	arg1	domain					1178:1183	the extracellular domain	1160:1183	the extracellular domain of Ephrin-B1	1160:1196	This silencing activity is independent of Eph receptors and involves a N-glycosylation site (N-139) in the extracellular domain of Ephrin-B1.
29779877	7	50	theme	axons	1394:1398	arg1	navigation					1366:1375	the navigation	1362:1375	the navigation of post-crossing axons in the corpus callosum	1362:1421	Together, our results reveal a molecular mechanism, involving interaction between the two unrelated guidance receptors Ephrin-B1 and Nrp1, that is used to control the navigation of post-crossing axons in the corpus callosum.
29779877	3	51	theme	circuit	483:489	arg1	feature					467:473	A particular feature	454:473	A particular feature	454:473	A particular feature of this circuit, which raises a key developmental question, is that the outgoing trajectory of post-crossing CCAs is mirror-symmetric with the incoming trajectory of pre-crossing axons.
29779877	1	52	theme	homotopic	252:260	arg1	regions					262:268	homotopic regions	252:268	homotopic regions of the cerebral cortex	252:291	The corpus callosum is the largest commissure in the brain, whose main function is to ensure communication between homotopic regions of the cerebral cortex.
29779877	5	53	theme	Ephrin-B1	944:952	arg1	upregulation					908:919	an upregulation	905:919	an upregulation	905:919	This change is concomitant with an upregulation of the surface protein Ephrin-B1, which acts in CCAs to inhibit Sema3C signaling via interaction with the Neuropilin-1 (Nrp1) receptor.
29779877	2	54	theme	brain	376:380	arg1	midline					382:388	the brain midline	372:388	the brain midline	372:388	During fetal development, corpus callosum axons (CCAs) grow toward and across the brain midline and then away on the contralateral hemisphere to their targets.
29779877	7	55	from	navigation	1366:1375	arg1	callosum					1414:1421	the corpus callosum	1403:1421	the corpus callosum	1403:1421	Together, our results reveal a molecular mechanism, involving interaction between the two unrelated guidance receptors Ephrin-B1 and Nrp1, that is used to control the navigation of post-crossing axons in the corpus callosum.
29779877	0	56	theme	Post-crossing	86:98	arg1	Navigation					100:109	Post-crossing Navigation	86:109	Post-crossing Navigation of Corpus Callosum Axons	86:134	Developmental Upregulation of Ephrin-B1 Silences Sema3C/Neuropilin-1 Signaling during Post-crossing Navigation of Corpus Callosum Axons.
29779877	6	57	theme	Eph	1099:1101	arg1	receptors					1103:1111	Eph receptors	1099:1111	Eph receptors	1099:1111	This silencing activity is independent of Eph receptors and involves a N-glycosylation site (N-139) in the extracellular domain of Ephrin-B1.
29779877	3	58	theme	developmental	511:523	arg1	question					525:532	a key developmental question	505:532	a key developmental question	505:532	A particular feature of this circuit, which raises a key developmental question, is that the outgoing trajectory of post-crossing CCAs is mirror-symmetric with the incoming trajectory of pre-crossing axons.
22375065	7	0	theme	β-N-acetylglucosamine	734:754	arg1	modification					767:778	O-linked β-N-acetylglucosamine (O-GlcNAc) modification	725:778	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of the cytoplasmic domain	725:804	First, O-linked β-N-acetylglucosamine (O-GlcNAc) modification of the cytoplasmic domain retains E-cadherin in the endoplasmic reticulum.
22375065	11	1	theme	E-cadherin	1358:1367	arg1	trafficking					1369:1379	E-cadherin trafficking	1358:1379	E-cadherin trafficking to the plasma membrane	1358:1402	Consequently, E-cadherin trafficking to the plasma membrane was inhibited.
22375065	8	2	theme	secretory	952:960	arg1	pathway					962:968	the secretory pathway	948:968	the secretory pathway	948:968	Second, incomplete processing by proprotein convertases arrests E-cadherin transport late in the secretory pathway.
22375065	14	3	theme	proprotein	1743:1752	arg1	convertases					1754:1764	proprotein convertases	1743:1764	proprotein convertases	1743:1764	Furthermore, cell-stress-induced inactivation of proprotein convertases, inhibited E-cadherin maturation, further exacerbating apoptosis.
22375065	7	4	mod	modification	767:778	arg3	β-N-acetylglucosamine					734:754	O-linked β-N-acetylglucosamine (O-GlcNAc) modification	725:778	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of the cytoplasmic domain	725:804	First, O-linked β-N-acetylglucosamine (O-GlcNAc) modification of the cytoplasmic domain retains E-cadherin in the endoplasmic reticulum.
22375065	7	4	mod	modification	767:778	arg3	O-GlcNAc					757:764	O-linked β-N-acetylglucosamine (O-GlcNAc) modification	725:778	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of the cytoplasmic domain	725:804	First, O-linked β-N-acetylglucosamine (O-GlcNAc) modification of the cytoplasmic domain retains E-cadherin in the endoplasmic reticulum.
22375065	7	4	mod	modification	767:778	arg1	domain					799:804	the cytoplasmic domain	783:804	the cytoplasmic domain	783:804	First, O-linked β-N-acetylglucosamine (O-GlcNAc) modification of the cytoplasmic domain retains E-cadherin in the endoplasmic reticulum.
22375065	6	5	theme	surface	699:705	arg1	transport					707:715	its cell surface transport	690:715	its cell surface transport	690:715	After treatment of breast cancer cells with drugs, we found that two independent modifications of E-cadherin inhibit its cell surface transport.
22375065	8	6	theme	proprotein	888:897	arg1	convertases					899:909	proprotein convertases	888:909	proprotein convertases	888:909	Second, incomplete processing by proprotein convertases arrests E-cadherin transport late in the secretory pathway.
22375065	10	7	theme	phosphatidylinositol	1171:1190	arg1	kinase					1202:1207	Type I gamma phosphatidylinositol phosphate kinase	1158:1207	Type I gamma phosphatidylinositol phosphate kinase (PIPKIγ)	1158:1216	However, binding of E-cadherin to Type I gamma phosphatidylinositol phosphate kinase (PIPKIγ), a protein required for recruitment of E-cadherin to adhesion sites, was blocked by O-GlcNAc glycosylation (O-GlcNAcylation).
22375065	10	7	theme	phosphatidylinositol	1171:1190	arg1	protein					1221:1227	a protein	1219:1227	a protein required for recruitment of E-cadherin to adhesion sites	1219:1284	However, binding of E-cadherin to Type I gamma phosphatidylinositol phosphate kinase (PIPKIγ), a protein required for recruitment of E-cadherin to adhesion sites, was blocked by O-GlcNAc glycosylation (O-GlcNAcylation).
22375065	10	7	theme	phosphatidylinositol	1171:1190	arg1	PIPKIγ					1210:1215	PIPKIγ	1210:1215	PIPKIγ	1210:1215	However, binding of E-cadherin to Type I gamma phosphatidylinositol phosphate kinase (PIPKIγ), a protein required for recruitment of E-cadherin to adhesion sites, was blocked by O-GlcNAc glycosylation (O-GlcNAcylation).
22375065	5	8	theme	E-cadherin	490:499	arg1	loss					482:485	acute loss	476:485	acute loss of E-cadherin	476:499	Conversely, acute loss of E-cadherin sensitizes cells to apoptosis by unknown post-translational mechanisms.
22375065	8	9	theme	E-cadherin	919:928	arg1	transport					930:938	E-cadherin transport	919:938	E-cadherin transport	919:938	Second, incomplete processing by proprotein convertases arrests E-cadherin transport late in the secretory pathway.
22375065	6	10	theme	cells	606:610	arg1	treatment					579:587	treatment	579:587	treatment of breast cancer cells with drugs	579:621	After treatment of breast cancer cells with drugs, we found that two independent modifications of E-cadherin inhibit its cell surface transport.
22375065	11	11	theme	plasma	1388:1393	arg1	membrane					1395:1402	the plasma membrane	1384:1402	the plasma membrane	1384:1402	Consequently, E-cadherin trafficking to the plasma membrane was inhibited.
22375065	7	12	link	O-linked	725:732	arg1	modification					767:778	O-linked β-N-acetylglucosamine (O-GlcNAc) modification	725:778	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of the cytoplasmic domain	725:804	First, O-linked β-N-acetylglucosamine (O-GlcNAc) modification of the cytoplasmic domain retains E-cadherin in the endoplasmic reticulum.
22375065	10	13	theme	phosphate	1192:1200	arg1	kinase					1202:1207	Type I gamma phosphatidylinositol phosphate kinase	1158:1207	Type I gamma phosphatidylinositol phosphate kinase (PIPKIγ)	1158:1216	However, binding of E-cadherin to Type I gamma phosphatidylinositol phosphate kinase (PIPKIγ), a protein required for recruitment of E-cadherin to adhesion sites, was blocked by O-GlcNAc glycosylation (O-GlcNAcylation).
22375065	10	13	theme	phosphate	1192:1200	arg1	protein					1221:1227	a protein	1219:1227	a protein required for recruitment of E-cadherin to adhesion sites	1219:1284	However, binding of E-cadherin to Type I gamma phosphatidylinositol phosphate kinase (PIPKIγ), a protein required for recruitment of E-cadherin to adhesion sites, was blocked by O-GlcNAc glycosylation (O-GlcNAcylation).
22375065	10	13	theme	phosphate	1192:1200	arg1	PIPKIγ					1210:1215	PIPKIγ	1210:1215	PIPKIγ	1210:1215	However, binding of E-cadherin to Type I gamma phosphatidylinositol phosphate kinase (PIPKIγ), a protein required for recruitment of E-cadherin to adhesion sites, was blocked by O-GlcNAc glycosylation (O-GlcNAcylation).
22375065	7	14	theme	O-GlcNAc	757:764	arg1	modification					767:778	O-linked β-N-acetylglucosamine (O-GlcNAc) modification	725:778	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of the cytoplasmic domain	725:804	First, O-linked β-N-acetylglucosamine (O-GlcNAc) modification of the cytoplasmic domain retains E-cadherin in the endoplasmic reticulum.
22375065	6	15	theme	cancer	599:604	arg1	cells					606:610	breast cancer cells	592:610	breast cancer cells	592:610	After treatment of breast cancer cells with drugs, we found that two independent modifications of E-cadherin inhibit its cell surface transport.
22375065	15	16	theme	novel	1927:1931	arg1	mechanisms					1933:1942	novel mechanisms	1927:1942	novel mechanisms for rapid regulation of cell surface transport of E-cadherin in response to intoxication	1927:2031	The modifications of E-cadherin by O-GlcNAcylation and lack of pro-region processing represent novel mechanisms for rapid regulation of cell surface transport of E-cadherin in response to intoxication.
22375065	6	17	theme	breast	592:597	arg1	cells					606:610	breast cancer cells	592:610	breast cancer cells	592:610	After treatment of breast cancer cells with drugs, we found that two independent modifications of E-cadherin inhibit its cell surface transport.
22375065	3	18	theme	detachment-induced	289:306	arg1	apoptosis					308:316	detachment-induced apoptosis	289:316	detachment-induced apoptosis	289:316	Loss of cell adhesion causes detachment-induced apoptosis, which is called anoikis.
22375065	10	19	theme	O-GlcNAc	1302:1309	arg1	O-GlcNAcylation					1326:1340	O-GlcNAcylation	1326:1340	O-GlcNAcylation	1326:1340	However, binding of E-cadherin to Type I gamma phosphatidylinositol phosphate kinase (PIPKIγ), a protein required for recruitment of E-cadherin to adhesion sites, was blocked by O-GlcNAc glycosylation (O-GlcNAcylation).
22375065	10	19	theme	O-GlcNAc	1302:1309	arg1	glycosylation					1311:1323	O-GlcNAc glycosylation	1302:1323	O-GlcNAc glycosylation (O-GlcNAcylation)	1302:1341	However, binding of E-cadherin to Type I gamma phosphatidylinositol phosphate kinase (PIPKIγ), a protein required for recruitment of E-cadherin to adhesion sites, was blocked by O-GlcNAc glycosylation (O-GlcNAcylation).
22375065	12	20	theme	cell	1519:1522	arg1	surface					1524:1530	the cell surface	1515:1530	the cell surface	1515:1530	However, deletion mutants that cannot be O-GlcNAcylated continued to bind PIPKIγ, trafficked to the cell surface and delayed apoptosis, confirming the biological significance of the modifications and PIPKIγ binding.
22375065	10	21	theme	E-cadherin	1257:1266	arg1	recruitment					1242:1252	recruitment	1242:1252	recruitment of E-cadherin to adhesion sites	1242:1284	However, binding of E-cadherin to Type I gamma phosphatidylinositol phosphate kinase (PIPKIγ), a protein required for recruitment of E-cadherin to adhesion sites, was blocked by O-GlcNAc glycosylation (O-GlcNAcylation).
22375065	0	22	theme	post-translational	9:26	arg1	modifications					28:40	Multiple post-translational modifications	0:40	Multiple post-translational modifications	0:40	Multiple post-translational modifications regulate E-cadherin transport during apoptosis.
22375065	14	23	theme	E-cadherin	1777:1786	arg1	maturation					1788:1797	E-cadherin maturation	1777:1797	E-cadherin maturation	1777:1797	Furthermore, cell-stress-induced inactivation of proprotein convertases, inhibited E-cadherin maturation, further exacerbating apoptosis.
22375065	3	24	theme	cell	268:271	arg1	adhesion					273:280	cell adhesion	268:280	cell adhesion	268:280	Loss of cell adhesion causes detachment-induced apoptosis, which is called anoikis.
22375065	15	25	theme	E-cadherin	1994:2003	arg1	transport					1981:1989	cell surface transport	1968:1989	cell surface transport of E-cadherin in response to intoxication	1968:2031	The modifications of E-cadherin by O-GlcNAcylation and lack of pro-region processing represent novel mechanisms for rapid regulation of cell surface transport of E-cadherin in response to intoxication.
22375065	6	26	with	treatment	579:587	arg1	drugs					617:621	drugs	617:621	drugs	617:621	After treatment of breast cancer cells with drugs, we found that two independent modifications of E-cadherin inhibit its cell surface transport.
22375065	0	27	theme	Multiple	0:7	arg1	modifications					28:40	Multiple post-translational modifications	0:40	Multiple post-translational modifications	0:40	Multiple post-translational modifications regulate E-cadherin transport during apoptosis.
22375065	3	28	theme	adhesion	273:280	arg1	Loss					260:263	Loss	260:263	Loss of cell adhesion	260:280	Loss of cell adhesion causes detachment-induced apoptosis, which is called anoikis.
22375065	4	29	theme	cell-cell	444:452	arg1	adhesion					454:461	E-cadherin-mediated cell-cell adhesion	424:461	E-cadherin-mediated cell-cell adhesion	424:461	Anoikis can be inhibited despite loss of cell-matrix interactions by preserving E-cadherin-mediated cell-cell adhesion.
22375065	10	30	theme	gamma	1165:1169	arg1	kinase					1202:1207	Type I gamma phosphatidylinositol phosphate kinase	1158:1207	Type I gamma phosphatidylinositol phosphate kinase (PIPKIγ)	1158:1216	However, binding of E-cadherin to Type I gamma phosphatidylinositol phosphate kinase (PIPKIγ), a protein required for recruitment of E-cadherin to adhesion sites, was blocked by O-GlcNAc glycosylation (O-GlcNAcylation).
22375065	10	30	theme	gamma	1165:1169	arg1	protein					1221:1227	a protein	1219:1227	a protein required for recruitment of E-cadherin to adhesion sites	1219:1284	However, binding of E-cadherin to Type I gamma phosphatidylinositol phosphate kinase (PIPKIγ), a protein required for recruitment of E-cadherin to adhesion sites, was blocked by O-GlcNAc glycosylation (O-GlcNAcylation).
22375065	10	30	theme	gamma	1165:1169	arg1	PIPKIγ					1210:1215	PIPKIγ	1210:1215	PIPKIγ	1210:1215	However, binding of E-cadherin to Type I gamma phosphatidylinositol phosphate kinase (PIPKIγ), a protein required for recruitment of E-cadherin to adhesion sites, was blocked by O-GlcNAc glycosylation (O-GlcNAcylation).
22375065	15	31	theme	surface	1973:1979	arg1	transport					1981:1989	cell surface transport	1968:1989	cell surface transport of E-cadherin in response to intoxication	1968:2031	The modifications of E-cadherin by O-GlcNAcylation and lack of pro-region processing represent novel mechanisms for rapid regulation of cell surface transport of E-cadherin in response to intoxication.
22375065	6	32	theme	E-cadherin	671:680	arg1	modifications					654:666	two independent modifications	638:666	two independent modifications of E-cadherin	638:680	After treatment of breast cancer cells with drugs, we found that two independent modifications of E-cadherin inhibit its cell surface transport.
22375065	4	33	theme	E-cadherin-mediated	424:442	arg1	adhesion					454:461	E-cadherin-mediated cell-cell adhesion	424:461	E-cadherin-mediated cell-cell adhesion	424:461	Anoikis can be inhibited despite loss of cell-matrix interactions by preserving E-cadherin-mediated cell-cell adhesion.
22375065	5	34	theme	unknown	534:540	arg1	mechanisms					561:570	unknown post-translational mechanisms	534:570	unknown post-translational mechanisms	534:570	Conversely, acute loss of E-cadherin sensitizes cells to apoptosis by unknown post-translational mechanisms.
22375065	15	35	theme	pro-region	1895:1904	arg1	processing					1906:1915	pro-region processing	1895:1915	pro-region processing	1895:1915	The modifications of E-cadherin by O-GlcNAcylation and lack of pro-region processing represent novel mechanisms for rapid regulation of cell surface transport of E-cadherin in response to intoxication.
22375065	7	36	from	E-cadherin	814:823	arg1	reticulum					844:852	the endoplasmic reticulum	828:852	the endoplasmic reticulum	828:852	First, O-linked β-N-acetylglucosamine (O-GlcNAc) modification of the cytoplasmic domain retains E-cadherin in the endoplasmic reticulum.
22375065	7	37	theme	cytoplasmic	787:797	arg1	domain					799:804	the cytoplasmic domain	783:804	the cytoplasmic domain	783:804	First, O-linked β-N-acetylglucosamine (O-GlcNAc) modification of the cytoplasmic domain retains E-cadherin in the endoplasmic reticulum.
22375065	15	38	from	regulation	1954:1963	arg1	response					2008:2015	response	2008:2015	response to intoxication	2008:2031	The modifications of E-cadherin by O-GlcNAcylation and lack of pro-region processing represent novel mechanisms for rapid regulation of cell surface transport of E-cadherin in response to intoxication.
22375065	5	39	theme	post-translational	542:559	arg1	mechanisms					561:570	unknown post-translational mechanisms	534:570	unknown post-translational mechanisms	534:570	Conversely, acute loss of E-cadherin sensitizes cells to apoptosis by unknown post-translational mechanisms.
22375065	9	40	theme	E-cadherin	993:1002	arg1	modifications					1004:1016	these E-cadherin modifications	987:1016	these E-cadherin modifications (detected by specific lectins and antibodies)	987:1062	We demonstrated these E-cadherin modifications (detected by specific lectins and antibodies) do not affect binding to α-catenin, β-catenin or γ-catenin.
22375065	7	41	theme	domain	799:804	arg1	modification					767:778	O-linked β-N-acetylglucosamine (O-GlcNAc) modification	725:778	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of the cytoplasmic domain	725:804	First, O-linked β-N-acetylglucosamine (O-GlcNAc) modification of the cytoplasmic domain retains E-cadherin in the endoplasmic reticulum.
22375065	15	42	theme	cell	1968:1971	arg1	transport					1981:1989	cell surface transport	1968:1989	cell surface transport of E-cadherin in response to intoxication	1968:2031	The modifications of E-cadherin by O-GlcNAcylation and lack of pro-region processing represent novel mechanisms for rapid regulation of cell surface transport of E-cadherin in response to intoxication.
22375065	0	43	theme	E-cadherin	51:60	arg1	transport					62:70	E-cadherin transport	51:70	E-cadherin transport	51:70	Multiple post-translational modifications regulate E-cadherin transport during apoptosis.
22375065	10	44	theme	adhesion	1271:1278	arg1	sites					1280:1284	adhesion sites	1271:1284	adhesion sites	1271:1284	However, binding of E-cadherin to Type I gamma phosphatidylinositol phosphate kinase (PIPKIγ), a protein required for recruitment of E-cadherin to adhesion sites, was blocked by O-GlcNAc glycosylation (O-GlcNAcylation).
22375065	6	45	theme	independent	642:652	arg1	modifications					654:666	two independent modifications	638:666	two independent modifications of E-cadherin	638:680	After treatment of breast cancer cells with drugs, we found that two independent modifications of E-cadherin inhibit its cell surface transport.
22375065	15	46	theme	processing	1906:1915	arg1	lack					1887:1890	lack	1887:1890	lack of pro-region processing	1887:1915	The modifications of E-cadherin by O-GlcNAcylation and lack of pro-region processing represent novel mechanisms for rapid regulation of cell surface transport of E-cadherin in response to intoxication.
22375065	15	46	theme	processing	1906:1915	arg1	O-GlcNAcylation					1867:1881	O-GlcNAcylation	1867:1881	O-GlcNAcylation	1867:1881	The modifications of E-cadherin by O-GlcNAcylation and lack of pro-region processing represent novel mechanisms for rapid regulation of cell surface transport of E-cadherin in response to intoxication.
22375065	10	47	theme	E-cadherin	1144:1153	arg1	binding					1133:1139	binding	1133:1139	binding of E-cadherin to Type I gamma phosphatidylinositol phosphate kinase (PIPKIγ), a protein required for recruitment of E-cadherin to adhesion sites,	1133:1285	However, binding of E-cadherin to Type I gamma phosphatidylinositol phosphate kinase (PIPKIγ), a protein required for recruitment of E-cadherin to adhesion sites, was blocked by O-GlcNAc glycosylation (O-GlcNAcylation).
22375065	12	48	theme	biological	1570:1579	arg1	significance					1581:1592	the biological significance	1566:1592	the biological significance of the modifications	1566:1613	However, deletion mutants that cannot be O-GlcNAcylated continued to bind PIPKIγ, trafficked to the cell surface and delayed apoptosis, confirming the biological significance of the modifications and PIPKIγ binding.
22375065	8	49	theme	Second	855:860	arg1	processing					874:883	Second, incomplete processing	855:883	Second, incomplete processing by proprotein convertases	855:909	Second, incomplete processing by proprotein convertases arrests E-cadherin transport late in the secretory pathway.
22375065	2	50	theme	cell	245:248	arg1	adhesion					250:257	cell adhesion	245:257	cell adhesion	245:257	This processing is essential for E-cadherin maturation and cell adhesion.
22375065	15	51	from	transport	1981:1989	arg1	response					2008:2015	response	2008:2015	response to intoxication	2008:2031	The modifications of E-cadherin by O-GlcNAcylation and lack of pro-region processing represent novel mechanisms for rapid regulation of cell surface transport of E-cadherin in response to intoxication.
22375065	4	52	theme	interactions	397:408	arg1	loss					377:380	loss	377:380	loss of cell-matrix interactions	377:408	Anoikis can be inhibited despite loss of cell-matrix interactions by preserving E-cadherin-mediated cell-cell adhesion.
22375065	14	53	theme	convertases	1754:1764	arg1	inactivation					1727:1738	cell-stress-induced inactivation	1707:1738	cell-stress-induced inactivation of proprotein convertases	1707:1764	Furthermore, cell-stress-induced inactivation of proprotein convertases, inhibited E-cadherin maturation, further exacerbating apoptosis.
22375065	15	54	theme	rapid	1948:1952	arg1	regulation					1954:1963	rapid regulation	1948:1963	rapid regulation of cell surface transport of E-cadherin in response to intoxication	1948:2031	The modifications of E-cadherin by O-GlcNAcylation and lack of pro-region processing represent novel mechanisms for rapid regulation of cell surface transport of E-cadherin in response to intoxication.
22375065	15	55	from	response	2008:2015	arg1	regulation					1954:1963	rapid regulation	1948:1963	rapid regulation of cell surface transport of E-cadherin in response to intoxication	1948:2031	The modifications of E-cadherin by O-GlcNAcylation and lack of pro-region processing represent novel mechanisms for rapid regulation of cell surface transport of E-cadherin in response to intoxication.
22375065	6	56	theme	cell	694:697	arg1	transport					707:715	its cell surface transport	690:715	its cell surface transport	690:715	After treatment of breast cancer cells with drugs, we found that two independent modifications of E-cadherin inhibit its cell surface transport.
22375065	15	57	theme	E-cadherin	1853:1862	arg1	modifications					1836:1848	The modifications	1832:1848	The modifications of E-cadherin by O-GlcNAcylation and lack of pro-region processing	1832:1915	The modifications of E-cadherin by O-GlcNAcylation and lack of pro-region processing represent novel mechanisms for rapid regulation of cell surface transport of E-cadherin in response to intoxication.
22375065	4	58	theme	cell-matrix	385:395	arg1	interactions					397:408	cell-matrix interactions	385:408	cell-matrix interactions	385:408	Anoikis can be inhibited despite loss of cell-matrix interactions by preserving E-cadherin-mediated cell-cell adhesion.
22375065	8	59	dep	Second	855:860	arg1	incomplete					863:872	incomplete	863:872	incomplete	863:872	Second, incomplete processing by proprotein convertases arrests E-cadherin transport late in the secretory pathway.
22375065	9	60	theme	specific	1031:1038	arg1	lectins					1040:1046	specific lectins	1031:1046	specific lectins	1031:1046	We demonstrated these E-cadherin modifications (detected by specific lectins and antibodies) do not affect binding to α-catenin, β-catenin or γ-catenin.
22375065	10	61	theme	Type	1158:1161	arg1	kinase					1202:1207	Type I gamma phosphatidylinositol phosphate kinase	1158:1207	Type I gamma phosphatidylinositol phosphate kinase (PIPKIγ)	1158:1216	However, binding of E-cadherin to Type I gamma phosphatidylinositol phosphate kinase (PIPKIγ), a protein required for recruitment of E-cadherin to adhesion sites, was blocked by O-GlcNAc glycosylation (O-GlcNAcylation).
22375065	10	61	theme	Type	1158:1161	arg1	protein					1221:1227	a protein	1219:1227	a protein required for recruitment of E-cadherin to adhesion sites	1219:1284	However, binding of E-cadherin to Type I gamma phosphatidylinositol phosphate kinase (PIPKIγ), a protein required for recruitment of E-cadherin to adhesion sites, was blocked by O-GlcNAc glycosylation (O-GlcNAcylation).
22375065	10	61	theme	Type	1158:1161	arg1	PIPKIγ					1210:1215	PIPKIγ	1210:1215	PIPKIγ	1210:1215	However, binding of E-cadherin to Type I gamma phosphatidylinositol phosphate kinase (PIPKIγ), a protein required for recruitment of E-cadherin to adhesion sites, was blocked by O-GlcNAc glycosylation (O-GlcNAcylation).
22375065	12	62	theme	deletion	1428:1435	arg1	mutants					1437:1443	deletion mutants	1428:1443	deletion mutants that cannot be O-GlcNAcylated	1428:1473	However, deletion mutants that cannot be O-GlcNAcylated continued to bind PIPKIγ, trafficked to the cell surface and delayed apoptosis, confirming the biological significance of the modifications and PIPKIγ binding.
22375065	15	63	theme	transport	1981:1989	arg1	regulation					1954:1963	rapid regulation	1948:1963	rapid regulation of cell surface transport of E-cadherin in response to intoxication	1948:2031	The modifications of E-cadherin by O-GlcNAcylation and lack of pro-region processing represent novel mechanisms for rapid regulation of cell surface transport of E-cadherin in response to intoxication.
22375065	2	64	theme	E-cadherin	219:228	arg1	maturation					230:239	E-cadherin maturation	219:239	E-cadherin maturation	219:239	This processing is essential for E-cadherin maturation and cell adhesion.
22375065	1	65	theme	proprotein	162:171	arg1	convertases					173:183	proprotein convertases	162:183	proprotein convertases	162:183	E-cadherin is synthesized as a precursor and then undergoes cleavage by proprotein convertases.
22375065	7	66	theme	endoplasmic	832:842	arg1	reticulum					844:852	the endoplasmic reticulum	828:852	the endoplasmic reticulum	828:852	First, O-linked β-N-acetylglucosamine (O-GlcNAc) modification of the cytoplasmic domain retains E-cadherin in the endoplasmic reticulum.
22375065	9	67	dep	modifications	1004:1016	arg1	detected					1019:1026	detected	1019:1026	detected by specific lectins and antibodies	1019:1061	We demonstrated these E-cadherin modifications (detected by specific lectins and antibodies) do not affect binding to α-catenin, β-catenin or γ-catenin.
22375065	7	68	theme	O-linked	725:732	arg1	modification					767:778	O-linked β-N-acetylglucosamine (O-GlcNAc) modification	725:778	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of the cytoplasmic domain	725:804	First, O-linked β-N-acetylglucosamine (O-GlcNAc) modification of the cytoplasmic domain retains E-cadherin in the endoplasmic reticulum.
22375065	13	69	theme	E-cadherin	1660:1669	arg1	O-GlyNAcylation					1641:1655	O-GlyNAcylation	1641:1655	O-GlyNAcylation of E-cadherin	1641:1669	Thus, O-GlyNAcylation of E-cadherin accelerates apoptosis.
22375065	14	70	theme	cell-stress-induced	1707:1725	arg1	inactivation					1727:1738	cell-stress-induced inactivation	1707:1738	cell-stress-induced inactivation of proprotein convertases	1707:1764	Furthermore, cell-stress-induced inactivation of proprotein convertases, inhibited E-cadherin maturation, further exacerbating apoptosis.
22375065	5	71	theme	acute	476:480	arg1	loss					482:485	acute loss	476:485	acute loss of E-cadherin	476:499	Conversely, acute loss of E-cadherin sensitizes cells to apoptosis by unknown post-translational mechanisms.
22375065	12	72	theme	modifications	1601:1613	arg1	significance					1581:1592	the biological significance	1566:1592	the biological significance of the modifications	1566:1613	However, deletion mutants that cannot be O-GlcNAcylated continued to bind PIPKIγ, trafficked to the cell surface and delayed apoptosis, confirming the biological significance of the modifications and PIPKIγ binding.
16601115	0	0	theme	important	86:94	arg1	basis					11:15	Structural basis	0:15	Structural basis of reduction-dependent activation of human cystatin F. Cystatins	0:80	Structural basis of reduction-dependent activation of human cystatin F. Cystatins are important natural cysteine protease inhibitors targeting primarily papain-like cysteine proteases, including cathepsins and parasitic proteases like cruzipain, but also mammalian asparaginyl endopeptidase.
16601115	0	0	theme	important	86:94	arg1	inhibitors					122:131	important natural cysteine protease inhibitors	86:131	important natural cysteine protease inhibitors targeting primarily papain-like cysteine proteases, including cathepsins and parasitic proteases like cruzipain, but also mammalian asparaginyl endopeptidase	86:289	Structural basis of reduction-dependent activation of human cystatin F. Cystatins are important natural cysteine protease inhibitors targeting primarily papain-like cysteine proteases, including cathepsins and parasitic proteases like cruzipain, but also mammalian asparaginyl endopeptidase.
16601115	2	1	theme	superfamily	536:546	arg1	member					548:553	an unusual cystatin superfamily member	516:553	an unusual cystatin superfamily member with a redox-regulated activation mechanism and a restricted specificity profile	516:634	It is an unusual cystatin superfamily member with a redox-regulated activation mechanism and a restricted specificity profile.
16601115	2	1	theme	superfamily	536:546	arg1	It					510:511	It	510:511	It	510:511	It is an unusual cystatin superfamily member with a redox-regulated activation mechanism and a restricted specificity profile.
16601115	0	2	theme	parasitic	210:218	arg1	proteases					220:228	parasitic proteases	210:228	parasitic proteases	210:228	Structural basis of reduction-dependent activation of human cystatin F. Cystatins are important natural cysteine protease inhibitors targeting primarily papain-like cysteine proteases, including cathepsins and parasitic proteases like cruzipain, but also mammalian asparaginyl endopeptidase.
16601115	1	3	theme	Mammalian	292:300	arg1	F					311:311	Mammalian cystatin F	292:311	Mammalian cystatin F	292:311	Mammalian cystatin F, which is expressed almost exclusively in hematopoietic cells and accumulates in lysosome-like organelles, has been implicated in the regulation of antigen presentation and other immune processes.
16601115	2	4	theme	cystatin	527:534	arg1	member					548:553	an unusual cystatin superfamily member	516:553	an unusual cystatin superfamily member with a redox-regulated activation mechanism and a restricted specificity profile	516:634	It is an unusual cystatin superfamily member with a redox-regulated activation mechanism and a restricted specificity profile.
16601115	2	4	theme	cystatin	527:534	arg1	It					510:511	It	510:511	It	510:511	It is an unusual cystatin superfamily member with a redox-regulated activation mechanism and a restricted specificity profile.
16601115	4	5	theme	unusual	853:859	arg1	bridge					886:891	an unusual intermolecular disulfide bridge	850:891	an unusual intermolecular disulfide bridge	850:891	The two monomers interact in a fashion not seen before for cystatins or cystatin-like proteins that is crucially dependent on an unusual intermolecular disulfide bridge, suggesting how reduction leads to monomer formation and activation.
16601115	0	6	theme	asparaginyl	265:275	arg1	endopeptidase					277:289	mammalian asparaginyl endopeptidase	255:289	mammalian asparaginyl endopeptidase	255:289	Structural basis of reduction-dependent activation of human cystatin F. Cystatins are important natural cysteine protease inhibitors targeting primarily papain-like cysteine proteases, including cathepsins and parasitic proteases like cruzipain, but also mammalian asparaginyl endopeptidase.
16601115	1	7	theme	cystatin	302:309	arg1	F					311:311	Mammalian cystatin F	292:311	Mammalian cystatin F	292:311	Mammalian cystatin F, which is expressed almost exclusively in hematopoietic cells and accumulates in lysosome-like organelles, has been implicated in the regulation of antigen presentation and other immune processes.
16601115	0	8	theme	cysteine	104:111	arg1	basis					11:15	Structural basis	0:15	Structural basis of reduction-dependent activation of human cystatin F. Cystatins	0:80	Structural basis of reduction-dependent activation of human cystatin F. Cystatins are important natural cysteine protease inhibitors targeting primarily papain-like cysteine proteases, including cathepsins and parasitic proteases like cruzipain, but also mammalian asparaginyl endopeptidase.
16601115	0	8	theme	cysteine	104:111	arg1	inhibitors					122:131	important natural cysteine protease inhibitors	86:131	important natural cysteine protease inhibitors targeting primarily papain-like cysteine proteases, including cathepsins and parasitic proteases like cruzipain, but also mammalian asparaginyl endopeptidase	86:289	Structural basis of reduction-dependent activation of human cystatin F. Cystatins are important natural cysteine protease inhibitors targeting primarily papain-like cysteine proteases, including cathepsins and parasitic proteases like cruzipain, but also mammalian asparaginyl endopeptidase.
16601115	1	9	theme	lysosome-like	394:406	arg1	organelles					408:417	lysosome-like organelles	394:417	lysosome-like organelles	394:417	Mammalian cystatin F, which is expressed almost exclusively in hematopoietic cells and accumulates in lysosome-like organelles, has been implicated in the regulation of antigen presentation and other immune processes.
16601115	4	10	theme	monomer	928:934	arg1	formation					936:944	monomer formation	928:944	monomer formation	928:944	The two monomers interact in a fashion not seen before for cystatins or cystatin-like proteins that is crucially dependent on an unusual intermolecular disulfide bridge, suggesting how reduction leads to monomer formation and activation.
16601115	0	11	theme	mammalian	255:263	arg1	endopeptidase					277:289	mammalian asparaginyl endopeptidase	255:289	mammalian asparaginyl endopeptidase	255:289	Structural basis of reduction-dependent activation of human cystatin F. Cystatins are important natural cysteine protease inhibitors targeting primarily papain-like cysteine proteases, including cathepsins and parasitic proteases like cruzipain, but also mammalian asparaginyl endopeptidase.
16601115	4	12	theme	cystatin-like	796:808	arg1	proteins					810:817	cystatin-like proteins	796:817	cystatin-like proteins that is crucially dependent on an unusual intermolecular disulfide bridge, suggesting how reduction leads to monomer formation and activation	796:959	The two monomers interact in a fashion not seen before for cystatins or cystatin-like proteins that is crucially dependent on an unusual intermolecular disulfide bridge, suggesting how reduction leads to monomer formation and activation.
16601115	5	13	theme	cystatin	1037:1044	arg1	F					1046:1046	cystatin F	1037:1046	cystatin F	1037:1046	Strikingly, core sugars for one of the two N-linked glycosylation sites of cystatin F are well ordered, and their conformation and interactions with the protein indicate that this unique feature of cystatin F may modulate its inhibitory properties, in particular its reduced affinity toward asparaginyl endopeptidase compared with other cystatins.
16601115	0	14	theme	natural	96:102	arg1	basis					11:15	Structural basis	0:15	Structural basis of reduction-dependent activation of human cystatin F. Cystatins	0:80	Structural basis of reduction-dependent activation of human cystatin F. Cystatins are important natural cysteine protease inhibitors targeting primarily papain-like cysteine proteases, including cathepsins and parasitic proteases like cruzipain, but also mammalian asparaginyl endopeptidase.
16601115	0	14	theme	natural	96:102	arg1	inhibitors					122:131	important natural cysteine protease inhibitors	86:131	important natural cysteine protease inhibitors targeting primarily papain-like cysteine proteases, including cathepsins and parasitic proteases like cruzipain, but also mammalian asparaginyl endopeptidase	86:289	Structural basis of reduction-dependent activation of human cystatin F. Cystatins are important natural cysteine protease inhibitors targeting primarily papain-like cysteine proteases, including cathepsins and parasitic proteases like cruzipain, but also mammalian asparaginyl endopeptidase.
16601115	5	15	theme	other	1293:1297	arg1	cystatins					1299:1307	other cystatins	1293:1307	other cystatins	1293:1307	Strikingly, core sugars for one of the two N-linked glycosylation sites of cystatin F are well ordered, and their conformation and interactions with the protein indicate that this unique feature of cystatin F may modulate its inhibitory properties, in particular its reduced affinity toward asparaginyl endopeptidase compared with other cystatins.
16601115	1	16	theme	processes	499:507	arg1	regulation					447:456	the regulation	443:456	the regulation of antigen presentation and other immune processes	443:507	Mammalian cystatin F, which is expressed almost exclusively in hematopoietic cells and accumulates in lysosome-like organelles, has been implicated in the regulation of antigen presentation and other immune processes.
16601115	5	17	theme	N-linked	1005:1012	arg1	F					1046:1046	cystatin F	1037:1046	cystatin F	1037:1046	Strikingly, core sugars for one of the two N-linked glycosylation sites of cystatin F are well ordered, and their conformation and interactions with the protein indicate that this unique feature of cystatin F may modulate its inhibitory properties, in particular its reduced affinity toward asparaginyl endopeptidase compared with other cystatins.
16601115	5	17	theme	N-linked	1005:1012	arg1	sites					1028:1032	the two N-linked glycosylation sites	997:1032	the two N-linked glycosylation sites of cystatin F	997:1046	Strikingly, core sugars for one of the two N-linked glycosylation sites of cystatin F are well ordered, and their conformation and interactions with the protein indicate that this unique feature of cystatin F may modulate its inhibitory properties, in particular its reduced affinity toward asparaginyl endopeptidase compared with other cystatins.
16601115	5	18	theme	asparaginyl	1253:1263	arg1	endopeptidase					1265:1277	asparaginyl endopeptidase	1253:1277	asparaginyl endopeptidase compared with other cystatins	1253:1307	Strikingly, core sugars for one of the two N-linked glycosylation sites of cystatin F are well ordered, and their conformation and interactions with the protein indicate that this unique feature of cystatin F may modulate its inhibitory properties, in particular its reduced affinity toward asparaginyl endopeptidase compared with other cystatins.
16601115	2	19	theme	redox-regulated	562:576	arg1	mechanism					589:597	a redox-regulated activation mechanism	560:597	a redox-regulated activation mechanism	560:597	It is an unusual cystatin superfamily member with a redox-regulated activation mechanism and a restricted specificity profile.
16601115	2	20	with	member	548:553	arg1	profile					628:634	a restricted specificity profile	603:634	a restricted specificity profile	603:634	It is an unusual cystatin superfamily member with a redox-regulated activation mechanism and a restricted specificity profile.
16601115	2	20	with	member	548:553	arg1	mechanism					589:597	a redox-regulated activation mechanism	560:597	a redox-regulated activation mechanism	560:597	It is an unusual cystatin superfamily member with a redox-regulated activation mechanism and a restricted specificity profile.
16601115	5	21	theme	glycosylation	1014:1026	arg1	F					1046:1046	cystatin F	1037:1046	cystatin F	1037:1046	Strikingly, core sugars for one of the two N-linked glycosylation sites of cystatin F are well ordered, and their conformation and interactions with the protein indicate that this unique feature of cystatin F may modulate its inhibitory properties, in particular its reduced affinity toward asparaginyl endopeptidase compared with other cystatins.
16601115	5	21	theme	glycosylation	1014:1026	arg1	sites					1028:1032	the two N-linked glycosylation sites	997:1032	the two N-linked glycosylation sites of cystatin F	997:1046	Strikingly, core sugars for one of the two N-linked glycosylation sites of cystatin F are well ordered, and their conformation and interactions with the protein indicate that this unique feature of cystatin F may modulate its inhibitory properties, in particular its reduced affinity toward asparaginyl endopeptidase compared with other cystatins.
16601115	5	22	with	interactions	1093:1104	arg1	protein					1115:1121	the protein	1111:1121	the protein	1111:1121	Strikingly, core sugars for one of the two N-linked glycosylation sites of cystatin F are well ordered, and their conformation and interactions with the protein indicate that this unique feature of cystatin F may modulate its inhibitory properties, in particular its reduced affinity toward asparaginyl endopeptidase compared with other cystatins.
16601115	0	23	theme	protease	113:120	arg1	basis					11:15	Structural basis	0:15	Structural basis of reduction-dependent activation of human cystatin F. Cystatins	0:80	Structural basis of reduction-dependent activation of human cystatin F. Cystatins are important natural cysteine protease inhibitors targeting primarily papain-like cysteine proteases, including cathepsins and parasitic proteases like cruzipain, but also mammalian asparaginyl endopeptidase.
16601115	0	23	theme	protease	113:120	arg1	inhibitors					122:131	important natural cysteine protease inhibitors	86:131	important natural cysteine protease inhibitors targeting primarily papain-like cysteine proteases, including cathepsins and parasitic proteases like cruzipain, but also mammalian asparaginyl endopeptidase	86:289	Structural basis of reduction-dependent activation of human cystatin F. Cystatins are important natural cysteine protease inhibitors targeting primarily papain-like cysteine proteases, including cathepsins and parasitic proteases like cruzipain, but also mammalian asparaginyl endopeptidase.
16601115	5	24	theme	unique	1142:1147	arg1	feature					1149:1155	this unique feature	1137:1155	this unique feature of cystatin F	1137:1169	Strikingly, core sugars for one of the two N-linked glycosylation sites of cystatin F are well ordered, and their conformation and interactions with the protein indicate that this unique feature of cystatin F may modulate its inhibitory properties, in particular its reduced affinity toward asparaginyl endopeptidase compared with other cystatins.
16601115	5	25	theme	cystatin	1160:1167	arg1	F					1169:1169	cystatin F	1160:1169	cystatin F	1160:1169	Strikingly, core sugars for one of the two N-linked glycosylation sites of cystatin F are well ordered, and their conformation and interactions with the protein indicate that this unique feature of cystatin F may modulate its inhibitory properties, in particular its reduced affinity toward asparaginyl endopeptidase compared with other cystatins.
16601115	5	26	theme	sites	1028:1032	arg1	F					1046:1046	cystatin F	1037:1046	cystatin F	1037:1046	Strikingly, core sugars for one of the two N-linked glycosylation sites of cystatin F are well ordered, and their conformation and interactions with the protein indicate that this unique feature of cystatin F may modulate its inhibitory properties, in particular its reduced affinity toward asparaginyl endopeptidase compared with other cystatins.
16601115	5	26	theme	sites	1028:1032	arg1	one					990:992	one	990:992	one	990:992	Strikingly, core sugars for one of the two N-linked glycosylation sites of cystatin F are well ordered, and their conformation and interactions with the protein indicate that this unique feature of cystatin F may modulate its inhibitory properties, in particular its reduced affinity toward asparaginyl endopeptidase compared with other cystatins.
16601115	5	26	theme	sites	1028:1032	arg1	sites					1028:1032	the two N-linked glycosylation sites	997:1032	the two N-linked glycosylation sites of cystatin F	997:1046	Strikingly, core sugars for one of the two N-linked glycosylation sites of cystatin F are well ordered, and their conformation and interactions with the protein indicate that this unique feature of cystatin F may modulate its inhibitory properties, in particular its reduced affinity toward asparaginyl endopeptidase compared with other cystatins.
16601115	5	27	theme	inhibitory	1188:1197	arg1	properties					1199:1208	its inhibitory properties	1184:1208	its inhibitory properties	1184:1208	Strikingly, core sugars for one of the two N-linked glycosylation sites of cystatin F are well ordered, and their conformation and interactions with the protein indicate that this unique feature of cystatin F may modulate its inhibitory properties, in particular its reduced affinity toward asparaginyl endopeptidase compared with other cystatins.
16601115	5	28	gly	glycosylation	1014:1026	arg2	sites					1028:1032	the two N-linked glycosylation sites	997:1032	the two N-linked glycosylation sites of cystatin F	997:1046	Strikingly, core sugars for one of the two N-linked glycosylation sites of cystatin F are well ordered, and their conformation and interactions with the protein indicate that this unique feature of cystatin F may modulate its inhibitory properties, in particular its reduced affinity toward asparaginyl endopeptidase compared with other cystatins.
16601115	5	28	gly	glycosylation	1014:1026	arg1	F					1046:1046	cystatin F	1037:1046	cystatin F	1037:1046	Strikingly, core sugars for one of the two N-linked glycosylation sites of cystatin F are well ordered, and their conformation and interactions with the protein indicate that this unique feature of cystatin F may modulate its inhibitory properties, in particular its reduced affinity toward asparaginyl endopeptidase compared with other cystatins.
16601115	5	28	gly	glycosylation	1014:1026	arg2	two					1001:1003	two	1001:1003	two	1001:1003	Strikingly, core sugars for one of the two N-linked glycosylation sites of cystatin F are well ordered, and their conformation and interactions with the protein indicate that this unique feature of cystatin F may modulate its inhibitory properties, in particular its reduced affinity toward asparaginyl endopeptidase compared with other cystatins.
16601115	5	28	gly	glycosylation	1014:1026	arg2	F					1046:1046	cystatin F	1037:1046	cystatin F	1037:1046	Strikingly, core sugars for one of the two N-linked glycosylation sites of cystatin F are well ordered, and their conformation and interactions with the protein indicate that this unique feature of cystatin F may modulate its inhibitory properties, in particular its reduced affinity toward asparaginyl endopeptidase compared with other cystatins.
16601115	5	29	theme	particular	1214:1223	arg1	affinity					1237:1244	particular its reduced affinity	1214:1244	particular its reduced affinity toward asparaginyl endopeptidase compared with other cystatins	1214:1307	Strikingly, core sugars for one of the two N-linked glycosylation sites of cystatin F are well ordered, and their conformation and interactions with the protein indicate that this unique feature of cystatin F may modulate its inhibitory properties, in particular its reduced affinity toward asparaginyl endopeptidase compared with other cystatins.
16601115	5	30	with	conformation	1076:1087	arg1	protein					1115:1121	the protein	1111:1121	the protein	1111:1121	Strikingly, core sugars for one of the two N-linked glycosylation sites of cystatin F are well ordered, and their conformation and interactions with the protein indicate that this unique feature of cystatin F may modulate its inhibitory properties, in particular its reduced affinity toward asparaginyl endopeptidase compared with other cystatins.
16601115	0	31	theme	Structural	0:9	arg1	basis					11:15	Structural basis	0:15	Structural basis of reduction-dependent activation of human cystatin F. Cystatins	0:80	Structural basis of reduction-dependent activation of human cystatin F. Cystatins are important natural cysteine protease inhibitors targeting primarily papain-like cysteine proteases, including cathepsins and parasitic proteases like cruzipain, but also mammalian asparaginyl endopeptidase.
16601115	0	31	theme	Structural	0:9	arg1	inhibitors					122:131	important natural cysteine protease inhibitors	86:131	important natural cysteine protease inhibitors targeting primarily papain-like cysteine proteases, including cathepsins and parasitic proteases like cruzipain, but also mammalian asparaginyl endopeptidase	86:289	Structural basis of reduction-dependent activation of human cystatin F. Cystatins are important natural cysteine protease inhibitors targeting primarily papain-like cysteine proteases, including cathepsins and parasitic proteases like cruzipain, but also mammalian asparaginyl endopeptidase.
16601115	5	32	theme	reduced	1229:1235	arg1	affinity					1237:1244	particular its reduced affinity	1214:1244	particular its reduced affinity toward asparaginyl endopeptidase compared with other cystatins	1214:1307	Strikingly, core sugars for one of the two N-linked glycosylation sites of cystatin F are well ordered, and their conformation and interactions with the protein indicate that this unique feature of cystatin F may modulate its inhibitory properties, in particular its reduced affinity toward asparaginyl endopeptidase compared with other cystatins.
16601115	0	33	theme	reduction-dependent	20:38	arg1	activation					40:49	reduction-dependent activation	20:49	reduction-dependent activation of human cystatin F. Cystatins	20:80	Structural basis of reduction-dependent activation of human cystatin F. Cystatins are important natural cysteine protease inhibitors targeting primarily papain-like cysteine proteases, including cathepsins and parasitic proteases like cruzipain, but also mammalian asparaginyl endopeptidase.
16601115	2	34	theme	specificity	616:626	arg1	profile					628:634	a restricted specificity profile	603:634	a restricted specificity profile	603:634	It is an unusual cystatin superfamily member with a redox-regulated activation mechanism and a restricted specificity profile.
16601115	4	35	theme	intermolecular	861:874	arg1	bridge					886:891	an unusual intermolecular disulfide bridge	850:891	an unusual intermolecular disulfide bridge	850:891	The two monomers interact in a fashion not seen before for cystatins or cystatin-like proteins that is crucially dependent on an unusual intermolecular disulfide bridge, suggesting how reduction leads to monomer formation and activation.
16601115	1	36	theme	other	486:490	arg1	processes					499:507	other immune processes	486:507	other immune processes	486:507	Mammalian cystatin F, which is expressed almost exclusively in hematopoietic cells and accumulates in lysosome-like organelles, has been implicated in the regulation of antigen presentation and other immune processes.
16601115	3	37	dep	"	715:715	arg1	off					712:714	off	712:714	off	712:714	We describe the 2.1A crystal structure of human cystatin F in its dimeric "off" state.
16601115	2	38	theme	restricted	605:614	arg1	profile					628:634	a restricted specificity profile	603:634	a restricted specificity profile	603:634	It is an unusual cystatin superfamily member with a redox-regulated activation mechanism and a restricted specificity profile.
16601115	3	39	theme	dimeric	703:709	arg1	state					717:721	its dimeric "off" state	699:721	its dimeric "off" state	699:721	We describe the 2.1A crystal structure of human cystatin F in its dimeric "off" state.
16601115	2	40	theme	unusual	519:525	arg1	member					548:553	an unusual cystatin superfamily member	516:553	an unusual cystatin superfamily member with a redox-regulated activation mechanism and a restricted specificity profile	516:634	It is an unusual cystatin superfamily member with a redox-regulated activation mechanism and a restricted specificity profile.
16601115	2	40	theme	unusual	519:525	arg1	It					510:511	It	510:511	It	510:511	It is an unusual cystatin superfamily member with a redox-regulated activation mechanism and a restricted specificity profile.
16601115	0	41	theme	cysteine	165:172	arg1	proteases					220:228	parasitic proteases	210:228	parasitic proteases	210:228	Structural basis of reduction-dependent activation of human cystatin F. Cystatins are important natural cysteine protease inhibitors targeting primarily papain-like cysteine proteases, including cathepsins and parasitic proteases like cruzipain, but also mammalian asparaginyl endopeptidase.
16601115	0	41	theme	cysteine	165:172	arg1	proteases					174:182	papain-like cysteine proteases	153:182	papain-like cysteine proteases	153:182	Structural basis of reduction-dependent activation of human cystatin F. Cystatins are important natural cysteine protease inhibitors targeting primarily papain-like cysteine proteases, including cathepsins and parasitic proteases like cruzipain, but also mammalian asparaginyl endopeptidase.
16601115	0	41	theme	cysteine	165:172	arg1	cathepsins					195:204	cathepsins	195:204	cathepsins	195:204	Structural basis of reduction-dependent activation of human cystatin F. Cystatins are important natural cysteine protease inhibitors targeting primarily papain-like cysteine proteases, including cathepsins and parasitic proteases like cruzipain, but also mammalian asparaginyl endopeptidase.
16601115	3	42	theme	crystal	658:664	arg1	structure					666:674	the 2.1A crystal structure	649:674	the 2.1A crystal structure of human cystatin F in its dimeric "off" state	649:721	We describe the 2.1A crystal structure of human cystatin F in its dimeric "off" state.
16601115	3	43	from	structure	666:674	arg1	state					717:721	its dimeric "off" state	699:721	its dimeric "off" state	699:721	We describe the 2.1A crystal structure of human cystatin F in its dimeric "off" state.
16601115	0	44	theme	activation	40:49	arg1	basis					11:15	Structural basis	0:15	Structural basis of reduction-dependent activation of human cystatin F. Cystatins	0:80	Structural basis of reduction-dependent activation of human cystatin F. Cystatins are important natural cysteine protease inhibitors targeting primarily papain-like cysteine proteases, including cathepsins and parasitic proteases like cruzipain, but also mammalian asparaginyl endopeptidase.
16601115	0	44	theme	activation	40:49	arg1	inhibitors					122:131	important natural cysteine protease inhibitors	86:131	important natural cysteine protease inhibitors targeting primarily papain-like cysteine proteases, including cathepsins and parasitic proteases like cruzipain, but also mammalian asparaginyl endopeptidase	86:289	Structural basis of reduction-dependent activation of human cystatin F. Cystatins are important natural cysteine protease inhibitors targeting primarily papain-like cysteine proteases, including cathepsins and parasitic proteases like cruzipain, but also mammalian asparaginyl endopeptidase.
16601115	0	45	theme	papain-like	153:163	arg1	proteases					220:228	parasitic proteases	210:228	parasitic proteases	210:228	Structural basis of reduction-dependent activation of human cystatin F. Cystatins are important natural cysteine protease inhibitors targeting primarily papain-like cysteine proteases, including cathepsins and parasitic proteases like cruzipain, but also mammalian asparaginyl endopeptidase.
16601115	0	45	theme	papain-like	153:163	arg1	proteases					174:182	papain-like cysteine proteases	153:182	papain-like cysteine proteases	153:182	Structural basis of reduction-dependent activation of human cystatin F. Cystatins are important natural cysteine protease inhibitors targeting primarily papain-like cysteine proteases, including cathepsins and parasitic proteases like cruzipain, but also mammalian asparaginyl endopeptidase.
16601115	0	45	theme	papain-like	153:163	arg1	cathepsins					195:204	cathepsins	195:204	cathepsins	195:204	Structural basis of reduction-dependent activation of human cystatin F. Cystatins are important natural cysteine protease inhibitors targeting primarily papain-like cysteine proteases, including cathepsins and parasitic proteases like cruzipain, but also mammalian asparaginyl endopeptidase.
16601115	5	46	link	N-linked	1005:1012	arg1	F					1046:1046	cystatin F	1037:1046	cystatin F	1037:1046	Strikingly, core sugars for one of the two N-linked glycosylation sites of cystatin F are well ordered, and their conformation and interactions with the protein indicate that this unique feature of cystatin F may modulate its inhibitory properties, in particular its reduced affinity toward asparaginyl endopeptidase compared with other cystatins.
16601115	5	46	link	N-linked	1005:1012	arg1	sites					1028:1032	the two N-linked glycosylation sites	997:1032	the two N-linked glycosylation sites of cystatin F	997:1046	Strikingly, core sugars for one of the two N-linked glycosylation sites of cystatin F are well ordered, and their conformation and interactions with the protein indicate that this unique feature of cystatin F may modulate its inhibitory properties, in particular its reduced affinity toward asparaginyl endopeptidase compared with other cystatins.
16601115	0	47	theme	cystatin	60:67	arg1	Cystatins					72:80	human cystatin F. Cystatins	54:80	human cystatin F. Cystatins	54:80	Structural basis of reduction-dependent activation of human cystatin F. Cystatins are important natural cysteine protease inhibitors targeting primarily papain-like cysteine proteases, including cathepsins and parasitic proteases like cruzipain, but also mammalian asparaginyl endopeptidase.
16601115	4	48	theme	disulfide	876:884	arg1	bridge					886:891	an unusual intermolecular disulfide bridge	850:891	an unusual intermolecular disulfide bridge	850:891	The two monomers interact in a fashion not seen before for cystatins or cystatin-like proteins that is crucially dependent on an unusual intermolecular disulfide bridge, suggesting how reduction leads to monomer formation and activation.
16601115	5	49	theme	F	1169:1169	arg1	feature					1149:1155	this unique feature	1137:1155	this unique feature of cystatin F	1137:1169	Strikingly, core sugars for one of the two N-linked glycosylation sites of cystatin F are well ordered, and their conformation and interactions with the protein indicate that this unique feature of cystatin F may modulate its inhibitory properties, in particular its reduced affinity toward asparaginyl endopeptidase compared with other cystatins.
16601115	0	50	theme	human	54:58	arg1	Cystatins					72:80	human cystatin F. Cystatins	54:80	human cystatin F. Cystatins	54:80	Structural basis of reduction-dependent activation of human cystatin F. Cystatins are important natural cysteine protease inhibitors targeting primarily papain-like cysteine proteases, including cathepsins and parasitic proteases like cruzipain, but also mammalian asparaginyl endopeptidase.
16601115	1	51	theme	hematopoietic	355:367	arg1	cells					369:373	hematopoietic cells	355:373	hematopoietic cells	355:373	Mammalian cystatin F, which is expressed almost exclusively in hematopoietic cells and accumulates in lysosome-like organelles, has been implicated in the regulation of antigen presentation and other immune processes.
16601115	3	52	theme	2.1A	653:656	arg1	structure					666:674	the 2.1A crystal structure	649:674	the 2.1A crystal structure of human cystatin F in its dimeric "off" state	649:721	We describe the 2.1A crystal structure of human cystatin F in its dimeric "off" state.
16601115	1	53	theme	antigen	461:467	arg1	presentation					469:480	antigen presentation	461:480	antigen presentation	461:480	Mammalian cystatin F, which is expressed almost exclusively in hematopoietic cells and accumulates in lysosome-like organelles, has been implicated in the regulation of antigen presentation and other immune processes.
16601115	3	54	theme	cystatin	685:692	arg1	F					694:694	human cystatin F	679:694	human cystatin F	679:694	We describe the 2.1A crystal structure of human cystatin F in its dimeric "off" state.
16601115	1	55	theme	immune	492:497	arg1	processes					499:507	other immune processes	486:507	other immune processes	486:507	Mammalian cystatin F, which is expressed almost exclusively in hematopoietic cells and accumulates in lysosome-like organelles, has been implicated in the regulation of antigen presentation and other immune processes.
16601115	5	56	theme	core	974:977	arg1	sugars					979:984	core sugars	974:984	core sugars for one of the two N-linked glycosylation sites of cystatin F	974:1046	Strikingly, core sugars for one of the two N-linked glycosylation sites of cystatin F are well ordered, and their conformation and interactions with the protein indicate that this unique feature of cystatin F may modulate its inhibitory properties, in particular its reduced affinity toward asparaginyl endopeptidase compared with other cystatins.
16601115	1	57	theme	presentation	469:480	arg1	regulation					447:456	the regulation	443:456	the regulation of antigen presentation and other immune processes	443:507	Mammalian cystatin F, which is expressed almost exclusively in hematopoietic cells and accumulates in lysosome-like organelles, has been implicated in the regulation of antigen presentation and other immune processes.
16601115	3	58	theme	F	694:694	arg1	structure					666:674	the 2.1A crystal structure	649:674	the 2.1A crystal structure of human cystatin F in its dimeric "off" state	649:721	We describe the 2.1A crystal structure of human cystatin F in its dimeric "off" state.
16601115	0	59	theme	Cystatins	72:80	arg1	activation					40:49	reduction-dependent activation	20:49	reduction-dependent activation of human cystatin F. Cystatins	20:80	Structural basis of reduction-dependent activation of human cystatin F. Cystatins are important natural cysteine protease inhibitors targeting primarily papain-like cysteine proteases, including cathepsins and parasitic proteases like cruzipain, but also mammalian asparaginyl endopeptidase.
16601115	5	60	theme	F	1046:1046	arg1	F					1046:1046	cystatin F	1037:1046	cystatin F	1037:1046	Strikingly, core sugars for one of the two N-linked glycosylation sites of cystatin F are well ordered, and their conformation and interactions with the protein indicate that this unique feature of cystatin F may modulate its inhibitory properties, in particular its reduced affinity toward asparaginyl endopeptidase compared with other cystatins.
16601115	5	60	theme	F	1046:1046	arg1	sites					1028:1032	the two N-linked glycosylation sites	997:1032	the two N-linked glycosylation sites of cystatin F	997:1046	Strikingly, core sugars for one of the two N-linked glycosylation sites of cystatin F are well ordered, and their conformation and interactions with the protein indicate that this unique feature of cystatin F may modulate its inhibitory properties, in particular its reduced affinity toward asparaginyl endopeptidase compared with other cystatins.
16601115	0	61	theme	F.	69:70	arg1	Cystatins					72:80	human cystatin F. Cystatins	54:80	human cystatin F. Cystatins	54:80	Structural basis of reduction-dependent activation of human cystatin F. Cystatins are important natural cysteine protease inhibitors targeting primarily papain-like cysteine proteases, including cathepsins and parasitic proteases like cruzipain, but also mammalian asparaginyl endopeptidase.
16601115	3	62	theme	human	679:683	arg1	F					694:694	human cystatin F	679:694	human cystatin F	679:694	We describe the 2.1A crystal structure of human cystatin F in its dimeric "off" state.
16601115	2	63	theme	activation	578:587	arg1	mechanism					589:597	a redox-regulated activation mechanism	560:597	a redox-regulated activation mechanism	560:597	It is an unusual cystatin superfamily member with a redox-regulated activation mechanism and a restricted specificity profile.
19022411	6	0	from	present	1008:1014	arg1	cytoplasm					1023:1031	cytoplasm	1023:1031	cytoplasm	1023:1031	Transient transfection assays demonstrated that the T227A mutation induced the cytoplasmic accumulation of GAPDH, whereas the wild type was present in the cytoplasm and nuclei.
19022411	6	0	from	present	1008:1014	arg1	nuclei					1037:1042	nuclei	1037:1042	nuclei	1037:1042	Transient transfection assays demonstrated that the T227A mutation induced the cytoplasmic accumulation of GAPDH, whereas the wild type was present in the cytoplasm and nuclei.
19022411	7	1	theme	tetrameric	1295:1304	arg1	state					1306:1310	its tetrameric state	1291:1310	its tetrameric state	1291:1310	Structural modeling, mutagenesis of Thr227 to Lys and Arg, and gel filtration chromatography of mutated and wild type GAPDH, together suggested that O-GlcNAcylation at Thr227 interrupts the hydrophobic interfaces formed between GAPDH monomers in its tetrameric state.
19022411	4	2	theme	derivatization	764:777	arg1	significance					743:754	the biological significance	728:754	the biological significance of this derivatization	728:777	To elucidate the effect of O-GlcNAcylation on GAPDH, we determined the location of the O-GlcNAcylation site by tandem mass spectrometry, and subsequently examined the biological significance of this derivatization.
19022411	6	3	located	present	1008:1014	arg1	cytoplasm					1023:1031	cytoplasm	1023:1031	cytoplasm	1023:1031	Transient transfection assays demonstrated that the T227A mutation induced the cytoplasmic accumulation of GAPDH, whereas the wild type was present in the cytoplasm and nuclei.
19022411	6	3	located	present	1008:1014	arg2	present					1008:1014	present	1008:1014	present	1008:1014	Transient transfection assays demonstrated that the T227A mutation induced the cytoplasmic accumulation of GAPDH, whereas the wild type was present in the cytoplasm and nuclei.
19022411	6	3	located	present	1008:1014	arg2	type					999:1002	the wild type	990:1002	the wild type	990:1002	Transient transfection assays demonstrated that the T227A mutation induced the cytoplasmic accumulation of GAPDH, whereas the wild type was present in the cytoplasm and nuclei.
19022411	6	3	located	present	1008:1014	arg1	nuclei					1037:1042	nuclei	1037:1042	nuclei	1037:1042	Transient transfection assays demonstrated that the T227A mutation induced the cytoplasmic accumulation of GAPDH, whereas the wild type was present in the cytoplasm and nuclei.
19022411	7	4	from	Thr227	1213:1218	arg1	O-GlcNAcylation					1194:1208	O-GlcNAcylation	1194:1208	O-GlcNAcylation at Thr227	1194:1218	Structural modeling, mutagenesis of Thr227 to Lys and Arg, and gel filtration chromatography of mutated and wild type GAPDH, together suggested that O-GlcNAcylation at Thr227 interrupts the hydrophobic interfaces formed between GAPDH monomers in its tetrameric state.
19022411	7	5	theme	type	1158:1161	arg1	GAPDH					1163:1167	wild type GAPDH	1153:1167	wild type GAPDH	1153:1167	Structural modeling, mutagenesis of Thr227 to Lys and Arg, and gel filtration chromatography of mutated and wild type GAPDH, together suggested that O-GlcNAcylation at Thr227 interrupts the hydrophobic interfaces formed between GAPDH monomers in its tetrameric state.
19022411	3	6	theme	protein	400:406	arg1	O-GlcNAcylation					451:465	O-GlcNAcylation	451:465	O-GlcNAcylation	451:465	Generally, protein O-linked N-acetylglucosamine modification (O-GlcNAcylation) is considered, among other effects, to mediate the nuclear transportation of cytosolic proteins.
19022411	3	6	theme	protein	400:406	arg1	modification					437:448	protein O-linked N-acetylglucosamine modification	400:448	protein O-linked N-acetylglucosamine modification (O-GlcNAcylation)	400:466	Generally, protein O-linked N-acetylglucosamine modification (O-GlcNAcylation) is considered, among other effects, to mediate the nuclear transportation of cytosolic proteins.
19022411	6	7	theme	wild	994:997	arg1	type					999:1002	the wild type	990:1002	the wild type	990:1002	Transient transfection assays demonstrated that the T227A mutation induced the cytoplasmic accumulation of GAPDH, whereas the wild type was present in the cytoplasm and nuclei.
19022411	6	7	theme	wild	994:997	arg1	present					1008:1014	present	1008:1014	present	1008:1014	Transient transfection assays demonstrated that the T227A mutation induced the cytoplasmic accumulation of GAPDH, whereas the wild type was present in the cytoplasm and nuclei.
19022411	2	8	theme	functions	328:336	arg1	number					307:312	a number	305:312	a number of biological functions which are related to its subcellular localization	305:386	In addition to its glycolytic function, GAPDH has a number of biological functions which are related to its subcellular localization.
19022411	2	9	contain	has	301:303	arg1	GAPDH					295:299	GAPDH	295:299	GAPDH	295:299	In addition to its glycolytic function, GAPDH has a number of biological functions which are related to its subcellular localization.
19022411	2	9	contain	has	301:303	arg2	number					307:312	a number	305:312	a number of biological functions which are related to its subcellular localization	305:386	In addition to its glycolytic function, GAPDH has a number of biological functions which are related to its subcellular localization.
19022411	3	10	theme	O-linked	408:415	arg1	O-GlcNAcylation					451:465	O-GlcNAcylation	451:465	O-GlcNAcylation	451:465	Generally, protein O-linked N-acetylglucosamine modification (O-GlcNAcylation) is considered, among other effects, to mediate the nuclear transportation of cytosolic proteins.
19022411	3	10	theme	O-linked	408:415	arg1	modification					437:448	protein O-linked N-acetylglucosamine modification	400:448	protein O-linked N-acetylglucosamine modification (O-GlcNAcylation)	400:466	Generally, protein O-linked N-acetylglucosamine modification (O-GlcNAcylation) is considered, among other effects, to mediate the nuclear transportation of cytosolic proteins.
19022411	2	11	theme	biological	317:326	arg1	functions					328:336	biological functions	317:336	biological functions which are related to its subcellular localization	317:386	In addition to its glycolytic function, GAPDH has a number of biological functions which are related to its subcellular localization.
19022411	7	12	theme	GAPDH	1273:1277	arg1	monomers					1279:1286	GAPDH monomers	1273:1286	GAPDH monomers in its tetrameric state	1273:1310	Structural modeling, mutagenesis of Thr227 to Lys and Arg, and gel filtration chromatography of mutated and wild type GAPDH, together suggested that O-GlcNAcylation at Thr227 interrupts the hydrophobic interfaces formed between GAPDH monomers in its tetrameric state.
19022411	7	13	theme	GAPDH	1163:1167	arg1	mutagenesis					1066:1076	mutagenesis	1066:1076	mutagenesis of Thr227 to Lys and Arg	1066:1101	Structural modeling, mutagenesis of Thr227 to Lys and Arg, and gel filtration chromatography of mutated and wild type GAPDH, together suggested that O-GlcNAcylation at Thr227 interrupts the hydrophobic interfaces formed between GAPDH monomers in its tetrameric state.
19022411	7	13	theme	GAPDH	1163:1167	arg1	chromatography					1123:1136	gel filtration chromatography	1108:1136	gel filtration chromatography of mutated and wild type GAPDH	1108:1167	Structural modeling, mutagenesis of Thr227 to Lys and Arg, and gel filtration chromatography of mutated and wild type GAPDH, together suggested that O-GlcNAcylation at Thr227 interrupts the hydrophobic interfaces formed between GAPDH monomers in its tetrameric state.
19022411	7	13	theme	GAPDH	1163:1167	arg1	modeling					1056:1063	Structural modeling	1045:1063	Structural modeling	1045:1063	Structural modeling, mutagenesis of Thr227 to Lys and Arg, and gel filtration chromatography of mutated and wild type GAPDH, together suggested that O-GlcNAcylation at Thr227 interrupts the hydrophobic interfaces formed between GAPDH monomers in its tetrameric state.
19022411	4	14	theme	mass	683:686	arg1	spectrometry					688:699	tandem mass spectrometry	676:699	tandem mass spectrometry	676:699	To elucidate the effect of O-GlcNAcylation on GAPDH, we determined the location of the O-GlcNAcylation site by tandem mass spectrometry, and subsequently examined the biological significance of this derivatization.
19022411	4	15	theme	biological	732:741	arg1	significance					743:754	the biological significance	728:754	the biological significance of this derivatization	728:777	To elucidate the effect of O-GlcNAcylation on GAPDH, we determined the location of the O-GlcNAcylation site by tandem mass spectrometry, and subsequently examined the biological significance of this derivatization.
19022411	8	16	theme	nuclear	1441:1447	arg1	translocation					1449:1461	the nuclear translocation	1437:1461	the nuclear translocation of GAPDH	1437:1470	The present study identified Thr227 as the major GAPDH O-GlcNAcylation site, which suggests that this modification mediates the nuclear translocation of GAPDH, presumably by disrupting the conformation of tetrameric GAPDH.
19022411	6	17	theme	Transient	868:876	arg1	assays					891:896	Transient transfection assays	868:896	Transient transfection assays	868:896	Transient transfection assays demonstrated that the T227A mutation induced the cytoplasmic accumulation of GAPDH, whereas the wild type was present in the cytoplasm and nuclei.
19022411	3	18	link	O-linked	408:415	arg1	O-GlcNAcylation					451:465	O-GlcNAcylation	451:465	O-GlcNAcylation	451:465	Generally, protein O-linked N-acetylglucosamine modification (O-GlcNAcylation) is considered, among other effects, to mediate the nuclear transportation of cytosolic proteins.
19022411	3	18	link	O-linked	408:415	arg1	modification					437:448	protein O-linked N-acetylglucosamine modification	400:448	protein O-linked N-acetylglucosamine modification (O-GlcNAcylation)	400:466	Generally, protein O-linked N-acetylglucosamine modification (O-GlcNAcylation) is considered, among other effects, to mediate the nuclear transportation of cytosolic proteins.
19022411	1	19	theme	identical	228:236	arg1	subunits					245:252	four identical 37 kDa subunits	223:252	four identical 37 kDa subunits	223:252	Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a typical glycolytic enzyme comprised of four identical 37 kDa subunits.
19022411	6	20	theme	GAPDH	975:979	arg1	accumulation					959:970	the cytoplasmic accumulation	943:970	the cytoplasmic accumulation of GAPDH	943:979	Transient transfection assays demonstrated that the T227A mutation induced the cytoplasmic accumulation of GAPDH, whereas the wild type was present in the cytoplasm and nuclei.
19022411	7	21	theme	wild	1153:1156	arg1	GAPDH					1163:1167	wild type GAPDH	1153:1167	wild type GAPDH	1153:1167	Structural modeling, mutagenesis of Thr227 to Lys and Arg, and gel filtration chromatography of mutated and wild type GAPDH, together suggested that O-GlcNAcylation at Thr227 interrupts the hydrophobic interfaces formed between GAPDH monomers in its tetrameric state.
19022411	1	22	theme	Glyceraldehyde-3-phosphate	130:155	arg1	dehydrogenase					157:169	Glyceraldehyde-3-phosphate dehydrogenase	130:169	Glyceraldehyde-3-phosphate dehydrogenase (GAPDH)	130:177	Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a typical glycolytic enzyme comprised of four identical 37 kDa subunits.
19022411	1	22	theme	Glyceraldehyde-3-phosphate	130:155	arg1	enzyme					203:208	a typical glycolytic enzyme	182:208	a typical glycolytic enzyme comprised of four identical 37 kDa subunits	182:252	Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a typical glycolytic enzyme comprised of four identical 37 kDa subunits.
19022411	1	22	theme	Glyceraldehyde-3-phosphate	130:155	arg1	GAPDH					172:176	GAPDH	172:176	GAPDH	172:176	Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a typical glycolytic enzyme comprised of four identical 37 kDa subunits.
19022411	1	23	theme	37	238:239	arg1	kDa					241:243	kDa	241:243	kDa	241:243	Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a typical glycolytic enzyme comprised of four identical 37 kDa subunits.
19022411	0	24	theme	dehydrogenase	52:64	arg1	formation					80:88	glyceraldehyde-3-phosphate dehydrogenase homo-tetramer formation	25:88	glyceraldehyde-3-phosphate dehydrogenase homo-tetramer formation	25:88	O-GlcNAcylation disrupts glyceraldehyde-3-phosphate dehydrogenase homo-tetramer formation and mediates its nuclear translocation.
19022411	3	25	theme	other	489:493	arg1	effects					495:501	other effects	489:501	other effects	489:501	Generally, protein O-linked N-acetylglucosamine modification (O-GlcNAcylation) is considered, among other effects, to mediate the nuclear transportation of cytosolic proteins.
19022411	3	26	theme	N-acetylglucosamine	417:435	arg1	O-GlcNAcylation					451:465	O-GlcNAcylation	451:465	O-GlcNAcylation	451:465	Generally, protein O-linked N-acetylglucosamine modification (O-GlcNAcylation) is considered, among other effects, to mediate the nuclear transportation of cytosolic proteins.
19022411	3	26	theme	N-acetylglucosamine	417:435	arg1	modification					437:448	protein O-linked N-acetylglucosamine modification	400:448	protein O-linked N-acetylglucosamine modification (O-GlcNAcylation)	400:466	Generally, protein O-linked N-acetylglucosamine modification (O-GlcNAcylation) is considered, among other effects, to mediate the nuclear transportation of cytosolic proteins.
19022411	7	27	theme	mutated	1141:1147	arg1	mutagenesis					1066:1076	mutagenesis	1066:1076	mutagenesis of Thr227 to Lys and Arg	1066:1101	Structural modeling, mutagenesis of Thr227 to Lys and Arg, and gel filtration chromatography of mutated and wild type GAPDH, together suggested that O-GlcNAcylation at Thr227 interrupts the hydrophobic interfaces formed between GAPDH monomers in its tetrameric state.
19022411	7	27	theme	mutated	1141:1147	arg1	chromatography					1123:1136	gel filtration chromatography	1108:1136	gel filtration chromatography of mutated and wild type GAPDH	1108:1167	Structural modeling, mutagenesis of Thr227 to Lys and Arg, and gel filtration chromatography of mutated and wild type GAPDH, together suggested that O-GlcNAcylation at Thr227 interrupts the hydrophobic interfaces formed between GAPDH monomers in its tetrameric state.
19022411	7	27	theme	mutated	1141:1147	arg1	modeling					1056:1063	Structural modeling	1045:1063	Structural modeling	1045:1063	Structural modeling, mutagenesis of Thr227 to Lys and Arg, and gel filtration chromatography of mutated and wild type GAPDH, together suggested that O-GlcNAcylation at Thr227 interrupts the hydrophobic interfaces formed between GAPDH monomers in its tetrameric state.
19022411	6	28	theme	transfection	878:889	arg1	assays					891:896	Transient transfection assays	868:896	Transient transfection assays	868:896	Transient transfection assays demonstrated that the T227A mutation induced the cytoplasmic accumulation of GAPDH, whereas the wild type was present in the cytoplasm and nuclei.
19022411	7	29	theme	Structural	1045:1054	arg1	modeling					1056:1063	Structural modeling	1045:1063	Structural modeling	1045:1063	Structural modeling, mutagenesis of Thr227 to Lys and Arg, and gel filtration chromatography of mutated and wild type GAPDH, together suggested that O-GlcNAcylation at Thr227 interrupts the hydrophobic interfaces formed between GAPDH monomers in its tetrameric state.
19022411	0	30	theme	glyceraldehyde-3-phosphate	25:50	arg1	dehydrogenase					52:64	glyceraldehyde-3-phosphate dehydrogenase	25:64	glyceraldehyde-3-phosphate dehydrogenase homo-tetramer formation	25:88	O-GlcNAcylation disrupts glyceraldehyde-3-phosphate dehydrogenase homo-tetramer formation and mediates its nuclear translocation.
19022411	6	31	from	nuclei	1037:1042	arg1	type					999:1002	the wild type	990:1002	the wild type	990:1002	Transient transfection assays demonstrated that the T227A mutation induced the cytoplasmic accumulation of GAPDH, whereas the wild type was present in the cytoplasm and nuclei.
19022411	6	31	from	nuclei	1037:1042	arg1	present					1008:1014	present	1008:1014	present	1008:1014	Transient transfection assays demonstrated that the T227A mutation induced the cytoplasmic accumulation of GAPDH, whereas the wild type was present in the cytoplasm and nuclei.
19022411	8	32	theme	GAPDH	1466:1470	arg1	translocation					1449:1461	the nuclear translocation	1437:1461	the nuclear translocation of GAPDH	1437:1470	The present study identified Thr227 as the major GAPDH O-GlcNAcylation site, which suggests that this modification mediates the nuclear translocation of GAPDH, presumably by disrupting the conformation of tetrameric GAPDH.
19022411	3	33	theme	nuclear	519:525	arg1	transportation					527:540	the nuclear transportation	515:540	the nuclear transportation of cytosolic proteins	515:562	Generally, protein O-linked N-acetylglucosamine modification (O-GlcNAcylation) is considered, among other effects, to mediate the nuclear transportation of cytosolic proteins.
19022411	5	34	theme	Michael	850:856	arg1	addition					858:865	Michael addition	850:865	Michael addition	850:865	The site involved was identified to be Thr227 by beta-elimination and Michael addition.
19022411	8	35	theme	O-GlcNAcylation	1368:1382	arg1	Thr227					1342:1347	Thr227	1342:1347	Thr227	1342:1347	The present study identified Thr227 as the major GAPDH O-GlcNAcylation site, which suggests that this modification mediates the nuclear translocation of GAPDH, presumably by disrupting the conformation of tetrameric GAPDH.
19022411	8	35	theme	O-GlcNAcylation	1368:1382	arg1	site					1384:1387	the major GAPDH O-GlcNAcylation site	1352:1387	the major GAPDH O-GlcNAcylation site	1352:1387	The present study identified Thr227 as the major GAPDH O-GlcNAcylation site, which suggests that this modification mediates the nuclear translocation of GAPDH, presumably by disrupting the conformation of tetrameric GAPDH.
19022411	7	36	from	monomers	1279:1286	arg1	state					1306:1310	its tetrameric state	1291:1310	its tetrameric state	1291:1310	Structural modeling, mutagenesis of Thr227 to Lys and Arg, and gel filtration chromatography of mutated and wild type GAPDH, together suggested that O-GlcNAcylation at Thr227 interrupts the hydrophobic interfaces formed between GAPDH monomers in its tetrameric state.
19022411	1	37	theme	kDa	241:243	arg1	subunits					245:252	four identical 37 kDa subunits	223:252	four identical 37 kDa subunits	223:252	Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a typical glycolytic enzyme comprised of four identical 37 kDa subunits.
19022411	2	38	dep	function	285:292	arg1	addition					258:265	addition	258:265	addition	258:265	In addition to its glycolytic function, GAPDH has a number of biological functions which are related to its subcellular localization.
19022411	0	39	theme	homo-tetramer	66:78	arg1	formation					80:88	glyceraldehyde-3-phosphate dehydrogenase homo-tetramer formation	25:88	glyceraldehyde-3-phosphate dehydrogenase homo-tetramer formation	25:88	O-GlcNAcylation disrupts glyceraldehyde-3-phosphate dehydrogenase homo-tetramer formation and mediates its nuclear translocation.
19022411	6	40	theme	cytoplasmic	947:957	arg1	accumulation					959:970	the cytoplasmic accumulation	943:970	the cytoplasmic accumulation of GAPDH	943:979	Transient transfection assays demonstrated that the T227A mutation induced the cytoplasmic accumulation of GAPDH, whereas the wild type was present in the cytoplasm and nuclei.
19022411	2	41	theme	glycolytic	274:283	arg1	function					285:292	its glycolytic function	270:292	its glycolytic function	270:292	In addition to its glycolytic function, GAPDH has a number of biological functions which are related to its subcellular localization.
19022411	7	42	theme	hydrophobic	1235:1245	arg1	interfaces					1247:1256	the hydrophobic interfaces	1231:1256	the hydrophobic interfaces formed between GAPDH monomers in its tetrameric state	1231:1310	Structural modeling, mutagenesis of Thr227 to Lys and Arg, and gel filtration chromatography of mutated and wild type GAPDH, together suggested that O-GlcNAcylation at Thr227 interrupts the hydrophobic interfaces formed between GAPDH monomers in its tetrameric state.
19022411	7	43	theme	gel	1108:1110	arg1	chromatography					1123:1136	gel filtration chromatography	1108:1136	gel filtration chromatography of mutated and wild type GAPDH	1108:1167	Structural modeling, mutagenesis of Thr227 to Lys and Arg, and gel filtration chromatography of mutated and wild type GAPDH, together suggested that O-GlcNAcylation at Thr227 interrupts the hydrophobic interfaces formed between GAPDH monomers in its tetrameric state.
19022411	3	44	theme	cytosolic	545:553	arg1	proteins					555:562	cytosolic proteins	545:562	cytosolic proteins	545:562	Generally, protein O-linked N-acetylglucosamine modification (O-GlcNAcylation) is considered, among other effects, to mediate the nuclear transportation of cytosolic proteins.
19022411	4	45	from	effect	582:587	arg1	GAPDH					611:615	GAPDH	611:615	GAPDH	611:615	To elucidate the effect of O-GlcNAcylation on GAPDH, we determined the location of the O-GlcNAcylation site by tandem mass spectrometry, and subsequently examined the biological significance of this derivatization.
19022411	7	46	theme	filtration	1112:1121	arg1	chromatography					1123:1136	gel filtration chromatography	1108:1136	gel filtration chromatography of mutated and wild type GAPDH	1108:1167	Structural modeling, mutagenesis of Thr227 to Lys and Arg, and gel filtration chromatography of mutated and wild type GAPDH, together suggested that O-GlcNAcylation at Thr227 interrupts the hydrophobic interfaces formed between GAPDH monomers in its tetrameric state.
19022411	3	47	theme	proteins	555:562	arg1	transportation					527:540	the nuclear transportation	515:540	the nuclear transportation of cytosolic proteins	515:562	Generally, protein O-linked N-acetylglucosamine modification (O-GlcNAcylation) is considered, among other effects, to mediate the nuclear transportation of cytosolic proteins.
19022411	4	48	theme	O-GlcNAcylation	592:606	arg1	effect					582:587	the effect	578:587	the effect of O-GlcNAcylation on GAPDH	578:615	To elucidate the effect of O-GlcNAcylation on GAPDH, we determined the location of the O-GlcNAcylation site by tandem mass spectrometry, and subsequently examined the biological significance of this derivatization.
19022411	8	49	theme	GAPDH	1362:1366	arg1	Thr227					1342:1347	Thr227	1342:1347	Thr227	1342:1347	The present study identified Thr227 as the major GAPDH O-GlcNAcylation site, which suggests that this modification mediates the nuclear translocation of GAPDH, presumably by disrupting the conformation of tetrameric GAPDH.
19022411	8	49	theme	GAPDH	1362:1366	arg1	site					1384:1387	the major GAPDH O-GlcNAcylation site	1352:1387	the major GAPDH O-GlcNAcylation site	1352:1387	The present study identified Thr227 as the major GAPDH O-GlcNAcylation site, which suggests that this modification mediates the nuclear translocation of GAPDH, presumably by disrupting the conformation of tetrameric GAPDH.
19022411	8	50	theme	tetrameric	1518:1527	arg1	GAPDH					1529:1533	tetrameric GAPDH	1518:1533	tetrameric GAPDH	1518:1533	The present study identified Thr227 as the major GAPDH O-GlcNAcylation site, which suggests that this modification mediates the nuclear translocation of GAPDH, presumably by disrupting the conformation of tetrameric GAPDH.
19022411	2	51	theme	subcellular	363:373	arg1	localization					375:386	its subcellular localization	359:386	its subcellular localization	359:386	In addition to its glycolytic function, GAPDH has a number of biological functions which are related to its subcellular localization.
19022411	4	52	theme	site	668:671	arg1	location					636:643	the location	632:643	the location of the O-GlcNAcylation site	632:671	To elucidate the effect of O-GlcNAcylation on GAPDH, we determined the location of the O-GlcNAcylation site by tandem mass spectrometry, and subsequently examined the biological significance of this derivatization.
19022411	6	53	from	cytoplasm	1023:1031	arg1	type					999:1002	the wild type	990:1002	the wild type	990:1002	Transient transfection assays demonstrated that the T227A mutation induced the cytoplasmic accumulation of GAPDH, whereas the wild type was present in the cytoplasm and nuclei.
19022411	6	53	from	cytoplasm	1023:1031	arg1	present					1008:1014	present	1008:1014	present	1008:1014	Transient transfection assays demonstrated that the T227A mutation induced the cytoplasmic accumulation of GAPDH, whereas the wild type was present in the cytoplasm and nuclei.
19022411	6	54	theme	T227A	920:924	arg1	mutation					926:933	the T227A mutation	916:933	the T227A mutation	916:933	Transient transfection assays demonstrated that the T227A mutation induced the cytoplasmic accumulation of GAPDH, whereas the wild type was present in the cytoplasm and nuclei.
19022411	1	55	theme	typical	184:190	arg1	enzyme					203:208	a typical glycolytic enzyme	182:208	a typical glycolytic enzyme comprised of four identical 37 kDa subunits	182:252	Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a typical glycolytic enzyme comprised of four identical 37 kDa subunits.
19022411	1	55	theme	typical	184:190	arg1	dehydrogenase					157:169	Glyceraldehyde-3-phosphate dehydrogenase	130:169	Glyceraldehyde-3-phosphate dehydrogenase (GAPDH)	130:177	Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a typical glycolytic enzyme comprised of four identical 37 kDa subunits.
19022411	4	56	theme	O-GlcNAcylation	652:666	arg1	site					668:671	the O-GlcNAcylation site	648:671	the O-GlcNAcylation site	648:671	To elucidate the effect of O-GlcNAcylation on GAPDH, we determined the location of the O-GlcNAcylation site by tandem mass spectrometry, and subsequently examined the biological significance of this derivatization.
19022411	0	57	theme	nuclear	107:113	arg1	translocation					115:127	its nuclear translocation	103:127	its nuclear translocation	103:127	O-GlcNAcylation disrupts glyceraldehyde-3-phosphate dehydrogenase homo-tetramer formation and mediates its nuclear translocation.
19022411	8	58	theme	major	1356:1360	arg1	Thr227					1342:1347	Thr227	1342:1347	Thr227	1342:1347	The present study identified Thr227 as the major GAPDH O-GlcNAcylation site, which suggests that this modification mediates the nuclear translocation of GAPDH, presumably by disrupting the conformation of tetrameric GAPDH.
19022411	8	58	theme	major	1356:1360	arg1	site					1384:1387	the major GAPDH O-GlcNAcylation site	1352:1387	the major GAPDH O-GlcNAcylation site	1352:1387	The present study identified Thr227 as the major GAPDH O-GlcNAcylation site, which suggests that this modification mediates the nuclear translocation of GAPDH, presumably by disrupting the conformation of tetrameric GAPDH.
19022411	7	59	theme	Thr227	1081:1086	arg1	mutagenesis					1066:1076	mutagenesis	1066:1076	mutagenesis of Thr227 to Lys and Arg	1066:1101	Structural modeling, mutagenesis of Thr227 to Lys and Arg, and gel filtration chromatography of mutated and wild type GAPDH, together suggested that O-GlcNAcylation at Thr227 interrupts the hydrophobic interfaces formed between GAPDH monomers in its tetrameric state.
19022411	7	59	theme	Thr227	1081:1086	arg1	chromatography					1123:1136	gel filtration chromatography	1108:1136	gel filtration chromatography of mutated and wild type GAPDH	1108:1167	Structural modeling, mutagenesis of Thr227 to Lys and Arg, and gel filtration chromatography of mutated and wild type GAPDH, together suggested that O-GlcNAcylation at Thr227 interrupts the hydrophobic interfaces formed between GAPDH monomers in its tetrameric state.
19022411	7	59	theme	Thr227	1081:1086	arg1	modeling					1056:1063	Structural modeling	1045:1063	Structural modeling	1045:1063	Structural modeling, mutagenesis of Thr227 to Lys and Arg, and gel filtration chromatography of mutated and wild type GAPDH, together suggested that O-GlcNAcylation at Thr227 interrupts the hydrophobic interfaces formed between GAPDH monomers in its tetrameric state.
19022411	1	60	theme	glycolytic	192:201	arg1	enzyme					203:208	a typical glycolytic enzyme	182:208	a typical glycolytic enzyme comprised of four identical 37 kDa subunits	182:252	Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a typical glycolytic enzyme comprised of four identical 37 kDa subunits.
19022411	1	60	theme	glycolytic	192:201	arg1	dehydrogenase					157:169	Glyceraldehyde-3-phosphate dehydrogenase	130:169	Glyceraldehyde-3-phosphate dehydrogenase (GAPDH)	130:177	Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a typical glycolytic enzyme comprised of four identical 37 kDa subunits.
19022411	8	61	theme	present	1317:1323	arg1	study					1325:1329	The present study	1313:1329	The present study	1313:1329	The present study identified Thr227 as the major GAPDH O-GlcNAcylation site, which suggests that this modification mediates the nuclear translocation of GAPDH, presumably by disrupting the conformation of tetrameric GAPDH.
19022411	4	62	theme	tandem	676:681	arg1	spectrometry					688:699	tandem mass spectrometry	676:699	tandem mass spectrometry	676:699	To elucidate the effect of O-GlcNAcylation on GAPDH, we determined the location of the O-GlcNAcylation site by tandem mass spectrometry, and subsequently examined the biological significance of this derivatization.
19022411	6	63	attach	present	1008:1014	arg1	cytoplasm					1023:1031	cytoplasm	1023:1031	cytoplasm	1023:1031	Transient transfection assays demonstrated that the T227A mutation induced the cytoplasmic accumulation of GAPDH, whereas the wild type was present in the cytoplasm and nuclei.
19022411	6	63	attach	present	1008:1014	arg2	present					1008:1014	present	1008:1014	present	1008:1014	Transient transfection assays demonstrated that the T227A mutation induced the cytoplasmic accumulation of GAPDH, whereas the wild type was present in the cytoplasm and nuclei.
19022411	6	63	attach	present	1008:1014	arg2	type					999:1002	the wild type	990:1002	the wild type	990:1002	Transient transfection assays demonstrated that the T227A mutation induced the cytoplasmic accumulation of GAPDH, whereas the wild type was present in the cytoplasm and nuclei.
19022411	6	63	attach	present	1008:1014	arg1	nuclei					1037:1042	nuclei	1037:1042	nuclei	1037:1042	Transient transfection assays demonstrated that the T227A mutation induced the cytoplasmic accumulation of GAPDH, whereas the wild type was present in the cytoplasm and nuclei.
19022411	8	64	theme	GAPDH	1529:1533	arg1	conformation					1502:1513	the conformation	1498:1513	the conformation of tetrameric GAPDH	1498:1533	The present study identified Thr227 as the major GAPDH O-GlcNAcylation site, which suggests that this modification mediates the nuclear translocation of GAPDH, presumably by disrupting the conformation of tetrameric GAPDH.
21896475	0	0	theme	multiple	75:82	arg1	H3					112:113	histone H3	104:113	histone H3 serine 10	104:123	Modification of histones by sugar β-N-acetylglucosamine (GlcNAc) occurs on multiple residues, including histone H3 serine 10, and is cell cycle-regulated.
21896475	0	0	theme	multiple	75:82	arg1	residues					84:91	multiple residues	75:91	multiple residues	75:91	Modification of histones by sugar β-N-acetylglucosamine (GlcNAc) occurs on multiple residues, including histone H3 serine 10, and is cell cycle-regulated.
21896475	1	1	theme	β-N-acetylglucosamine	298:318	arg1	residue					331:337	an O-linked β-N-acetylglucosamine (O-GlcNAc) residue	286:337	an O-linked β-N-acetylglucosamine (O-GlcNAc) residue	286:337	The monosaccharide, β-N-acetylglucosamine (GlcNAc), can be added to the hydroxyl group of either serines or threonines to generate an O-linked β-N-acetylglucosamine (O-GlcNAc) residue (Love, D. C., and Hanover, J. A. (2005) Sci.
21896475	7	2	theme	H3S10ph	1292:1298	arg1	immunoprecipitates					1300:1317	H3S10ph immunoprecipitates	1292:1317	H3S10ph immunoprecipitates	1292:1317	Moreover, O-GlcNAcylated histones were lost from H3S10ph immunoprecipitates, whereas immunoprecipitation of either H3K4me3 or H3K9me3 (active or inactive histone marks, respectively) resulted in co-immunoprecipitation of O-GlcNAcylated histones.
21896475	6	3	theme	O-GlcNAcylation	1215:1229	arg1	H3S10					1185:1189	H3S10	1185:1189	H3S10	1185:1189	Expression of recombinant H3.3 harboring an S10A mutation abrogated histone H3 O-GlcNAcylation relative to its wild-type version, consistent with H3S10 being a site of histone O-GlcNAcylation (H3S10glc).
21896475	6	3	theme	O-GlcNAcylation	1215:1229	arg1	site					1199:1202	a site	1197:1202	a site of histone O-GlcNAcylation (H3S10glc)	1197:1240	Expression of recombinant H3.3 harboring an S10A mutation abrogated histone H3 O-GlcNAcylation relative to its wild-type version, consistent with H3S10 being a site of histone O-GlcNAcylation (H3S10glc).
21896475	6	3	theme	O-GlcNAcylation	1215:1229	arg1	O-GlcNAcylation					1215:1229	histone O-GlcNAcylation	1207:1229	histone O-GlcNAcylation (H3S10glc)	1207:1240	Expression of recombinant H3.3 harboring an S10A mutation abrogated histone H3 O-GlcNAcylation relative to its wild-type version, consistent with H3S10 being a site of histone O-GlcNAcylation (H3S10glc).
21896475	4	4	theme	human	682:686	arg1	cells					688:692	human cells	682:692	human cells	682:692	Here, we present evidence that in human cells all four core histones of the nucleosome are substrates for this glycosylation in the relative abundance H3, H4/H2B, and H2A.
21896475	0	5	dep	H3	112:113	arg1	serine					115:120	serine 10	115:123	histone H3 serine 10	104:123	Modification of histones by sugar β-N-acetylglucosamine (GlcNAc) occurs on multiple residues, including histone H3 serine 10, and is cell cycle-regulated.
21896475	7	6	dep	histone	1397:1403	arg1	marks					1405:1409	marks	1405:1409	marks	1405:1409	Moreover, O-GlcNAcylated histones were lost from H3S10ph immunoprecipitates, whereas immunoprecipitation of either H3K4me3 or H3K9me3 (active or inactive histone marks, respectively) resulted in co-immunoprecipitation of O-GlcNAcylated histones.
21896475	9	7	theme	S	1632:1632	arg1	phase					1634:1638	the S phase	1628:1638	the S phase	1628:1638	Histone O-GlcNAcylation is high in G(1) cells, declines throughout the S phase, increases again during late S/early G(2), and persists through late G(2) and mitosis.
21896475	1	8	theme	O-GlcNAc	321:328	arg1	residue					331:337	an O-linked β-N-acetylglucosamine (O-GlcNAc) residue	286:337	an O-linked β-N-acetylglucosamine (O-GlcNAc) residue	286:337	The monosaccharide, β-N-acetylglucosamine (GlcNAc), can be added to the hydroxyl group of either serines or threonines to generate an O-linked β-N-acetylglucosamine (O-GlcNAc) residue (Love, D. C., and Hanover, J. A. (2005) Sci.
21896475	2	9	dep	STKE	384:387	arg1	C					447:447	C	447:447	C	447:447	STKE 2005 312, 1-14; Hart, G. W., Housley, M. P., and Slawson, C. (2007) Nature 446, 1017-1022).
21896475	2	9	dep	STKE	384:387	arg1	M.					427:428	M.	427:428	M.	427:428	STKE 2005 312, 1-14; Hart, G. W., Housley, M. P., and Slawson, C. (2007) Nature 446, 1017-1022).
21896475	2	9	dep	STKE	384:387	arg1	G.					411:412	G.	411:412	G.	411:412	STKE 2005 312, 1-14; Hart, G. W., Housley, M. P., and Slawson, C. (2007) Nature 446, 1017-1022).
21896475	2	9	dep	STKE	384:387	arg1	P.					430:431	P.	430:431	P.	430:431	STKE 2005 312, 1-14; Hart, G. W., Housley, M. P., and Slawson, C. (2007) Nature 446, 1017-1022).
21896475	2	9	dep	STKE	384:387	arg1	312					394:396	312	394:396	312	394:396	STKE 2005 312, 1-14; Hart, G. W., Housley, M. P., and Slawson, C. (2007) Nature 446, 1017-1022).
21896475	2	9	dep	STKE	384:387	arg1	2007					451:454	2007	451:454	2007	451:454	STKE 2005 312, 1-14; Hart, G. W., Housley, M. P., and Slawson, C. (2007) Nature 446, 1017-1022).
21896475	2	9	dep	STKE	384:387	arg1	W.					414:415	W.	414:415	W.	414:415	STKE 2005 312, 1-14; Hart, G. W., Housley, M. P., and Slawson, C. (2007) Nature 446, 1017-1022).
21896475	2	9	dep	STKE	384:387	arg1	Slawson					438:444	Slawson	438:444	Slawson	438:444	STKE 2005 312, 1-14; Hart, G. W., Housley, M. P., and Slawson, C. (2007) Nature 446, 1017-1022).
21896475	1	10	theme	hydroxyl	227:234	arg1	serines					252:258	serines	252:258	serines	252:258	The monosaccharide, β-N-acetylglucosamine (GlcNAc), can be added to the hydroxyl group of either serines or threonines to generate an O-linked β-N-acetylglucosamine (O-GlcNAc) residue (Love, D. C., and Hanover, J. A. (2005) Sci.
21896475	1	10	theme	hydroxyl	227:234	arg1	threonines					263:272	threonines	263:272	threonines	263:272	The monosaccharide, β-N-acetylglucosamine (GlcNAc), can be added to the hydroxyl group of either serines or threonines to generate an O-linked β-N-acetylglucosamine (O-GlcNAc) residue (Love, D. C., and Hanover, J. A. (2005) Sci.
21896475	1	10	theme	hydroxyl	227:234	arg1	group					236:240	the hydroxyl group	223:240	the hydroxyl group of either serines or threonines	223:272	The monosaccharide, β-N-acetylglucosamine (GlcNAc), can be added to the hydroxyl group of either serines or threonines to generate an O-linked β-N-acetylglucosamine (O-GlcNAc) residue (Love, D. C., and Hanover, J. A. (2005) Sci.
21896475	2	11	dep	W.	414:415	arg1	1017-1022					469:477	1017-1022	469:477	1017-1022	469:477	STKE 2005 312, 1-14; Hart, G. W., Housley, M. P., and Slawson, C. (2007) Nature 446, 1017-1022).
21896475	2	11	dep	W.	414:415	arg1	Nature					457:462	Nature	457:462	Nature	457:462	STKE 2005 312, 1-14; Hart, G. W., Housley, M. P., and Slawson, C. (2007) Nature 446, 1017-1022).
21896475	1	12	dep	generate	277:284	arg1	C.					349:350	C.	349:350	C.	349:350	The monosaccharide, β-N-acetylglucosamine (GlcNAc), can be added to the hydroxyl group of either serines or threonines to generate an O-linked β-N-acetylglucosamine (O-GlcNAc) residue (Love, D. C., and Hanover, J. A. (2005) Sci.
21896475	1	12	dep	generate	277:284	arg1	A					369:369	A	369:369	A	369:369	The monosaccharide, β-N-acetylglucosamine (GlcNAc), can be added to the hydroxyl group of either serines or threonines to generate an O-linked β-N-acetylglucosamine (O-GlcNAc) residue (Love, D. C., and Hanover, J. A. (2005) Sci.
21896475	1	12	dep	generate	277:284	arg1	2005					373:376	2005	373:376	2005	373:376	The monosaccharide, β-N-acetylglucosamine (GlcNAc), can be added to the hydroxyl group of either serines or threonines to generate an O-linked β-N-acetylglucosamine (O-GlcNAc) residue (Love, D. C., and Hanover, J. A. (2005) Sci.
21896475	1	12	dep	generate	277:284	arg1	D.					346:347	D.	346:347	D.	346:347	The monosaccharide, β-N-acetylglucosamine (GlcNAc), can be added to the hydroxyl group of either serines or threonines to generate an O-linked β-N-acetylglucosamine (O-GlcNAc) residue (Love, D. C., and Hanover, J. A. (2005) Sci.
21896475	1	12	dep	generate	277:284	arg1	J.					366:367	J.	366:367	J.	366:367	The monosaccharide, β-N-acetylglucosamine (GlcNAc), can be added to the hydroxyl group of either serines or threonines to generate an O-linked β-N-acetylglucosamine (O-GlcNAc) residue (Love, D. C., and Hanover, J. A. (2005) Sci.
21896475	10	13	theme	novel	1754:1758	arg1	O-GlcNAcylation					1733:1747	O-GlcNAcylation	1733:1747	O-GlcNAcylation	1733:1747	Thus, O-GlcNAcylation is a novel histone post-translational modification regulating chromatin conformation during transcription and cell cycle progression.
21896475	10	13	theme	novel	1754:1758	arg1	modification					1787:1798	a novel histone post-translational modification	1752:1798	a novel histone post-translational modification regulating chromatin conformation during transcription and cell cycle progression	1752:1880	Thus, O-GlcNAcylation is a novel histone post-translational modification regulating chromatin conformation during transcription and cell cycle progression.
21896475	7	14	dep	H3K9me3	1369:1375	arg1	histone					1397:1403	active or inactive histone	1378:1403	active or inactive histone marks	1378:1409	Moreover, O-GlcNAcylated histones were lost from H3S10ph immunoprecipitates, whereas immunoprecipitation of either H3K4me3 or H3K9me3 (active or inactive histone marks, respectively) resulted in co-immunoprecipitation of O-GlcNAcylated histones.
21896475	0	15	theme	histone	104:110	arg1	H3					112:113	histone H3	104:113	histone H3 serine 10	104:123	Modification of histones by sugar β-N-acetylglucosamine (GlcNAc) occurs on multiple residues, including histone H3 serine 10, and is cell cycle-regulated.
21896475	6	16	theme	S10A	1083:1086	arg1	mutation					1088:1095	an S10A mutation	1080:1095	an S10A mutation	1080:1095	Expression of recombinant H3.3 harboring an S10A mutation abrogated histone H3 O-GlcNAcylation relative to its wild-type version, consistent with H3S10 being a site of histone O-GlcNAcylation (H3S10glc).
21896475	6	17	theme	histone	1207:1213	arg1	H3S10glc					1232:1239	H3S10glc	1232:1239	H3S10glc	1232:1239	Expression of recombinant H3.3 harboring an S10A mutation abrogated histone H3 O-GlcNAcylation relative to its wild-type version, consistent with H3S10 being a site of histone O-GlcNAcylation (H3S10glc).
21896475	6	17	theme	histone	1207:1213	arg1	O-GlcNAcylation					1215:1229	histone O-GlcNAcylation	1207:1229	histone O-GlcNAcylation (H3S10glc)	1207:1240	Expression of recombinant H3.3 harboring an S10A mutation abrogated histone H3 O-GlcNAcylation relative to its wild-type version, consistent with H3S10 being a site of histone O-GlcNAcylation (H3S10glc).
21896475	9	18	from	high	1588:1591	arg1	cells					1601:1605	G(1) cells	1596:1605	G(1) cells	1596:1605	Histone O-GlcNAcylation is high in G(1) cells, declines throughout the S phase, increases again during late S/early G(2), and persists through late G(2) and mitosis.
21896475	5	19	dep	suppressed	974:983	arg1	H3S10ph					1029:1035	H3S10ph	1029:1035	H3S10ph	1029:1035	Increasing the intracellular level of UDP-GlcNAc, the nucleotide sugar donor substrate for O-GlcNAcylation enhanced histone O-GlcNAcylation and partially suppressed phosphorylation of histone H3 at serine 10 (H3S10ph).
21896475	5	20	theme	histone	936:942	arg1	O-GlcNAcylation					944:958	histone O-GlcNAcylation	936:958	histone O-GlcNAcylation	936:958	Increasing the intracellular level of UDP-GlcNAc, the nucleotide sugar donor substrate for O-GlcNAcylation enhanced histone O-GlcNAcylation and partially suppressed phosphorylation of histone H3 at serine 10 (H3S10ph).
21896475	7	21	theme	O-GlcNAcylated	1253:1266	arg1	histones					1268:1275	O-GlcNAcylated histones	1253:1275	O-GlcNAcylated histones	1253:1275	Moreover, O-GlcNAcylated histones were lost from H3S10ph immunoprecipitates, whereas immunoprecipitation of either H3K4me3 or H3K9me3 (active or inactive histone marks, respectively) resulted in co-immunoprecipitation of O-GlcNAcylated histones.
21896475	9	22	theme	Histone	1561:1567	arg1	O-GlcNAcylation					1569:1583	Histone O-GlcNAcylation	1561:1583	Histone O-GlcNAcylation	1561:1583	Histone O-GlcNAcylation is high in G(1) cells, declines throughout the S phase, increases again during late S/early G(2), and persists through late G(2) and mitosis.
21896475	10	23	theme	post-translational	1768:1785	arg1	O-GlcNAcylation					1733:1747	O-GlcNAcylation	1733:1747	O-GlcNAcylation	1733:1747	Thus, O-GlcNAcylation is a novel histone post-translational modification regulating chromatin conformation during transcription and cell cycle progression.
21896475	10	23	theme	post-translational	1768:1785	arg1	modification					1787:1798	a novel histone post-translational modification	1752:1798	a novel histone post-translational modification regulating chromatin conformation during transcription and cell cycle progression	1752:1880	Thus, O-GlcNAcylation is a novel histone post-translational modification regulating chromatin conformation during transcription and cell cycle progression.
21896475	5	24	theme	H3	1012:1013	arg1	phosphorylation					985:999	phosphorylation	985:999	phosphorylation of histone H3	985:1013	Increasing the intracellular level of UDP-GlcNAc, the nucleotide sugar donor substrate for O-GlcNAcylation enhanced histone O-GlcNAcylation and partially suppressed phosphorylation of histone H3 at serine 10 (H3S10ph).
21896475	4	25	gly	glycosylation	759:771	arg1	abundance					789:797	the relative abundance H3, H4/H2B, and H2A	776:817	the relative abundance H3, H4/H2B, and H2A	776:817	Here, we present evidence that in human cells all four core histones of the nucleosome are substrates for this glycosylation in the relative abundance H3, H4/H2B, and H2A.
21896475	10	26	theme	chromatin	1811:1819	arg1	conformation					1821:1832	chromatin conformation	1811:1832	chromatin conformation	1811:1832	Thus, O-GlcNAcylation is a novel histone post-translational modification regulating chromatin conformation during transcription and cell cycle progression.
21896475	5	27	theme	nucleotide	874:883	arg1	UDP-GlcNAc					858:867	UDP-GlcNAc	858:867	UDP-GlcNAc	858:867	Increasing the intracellular level of UDP-GlcNAc, the nucleotide sugar donor substrate for O-GlcNAcylation enhanced histone O-GlcNAcylation and partially suppressed phosphorylation of histone H3 at serine 10 (H3S10ph).
21896475	5	27	theme	nucleotide	874:883	arg1	substrate					897:905	the nucleotide sugar donor substrate	870:905	the nucleotide sugar donor substrate for O-GlcNAcylation	870:925	Increasing the intracellular level of UDP-GlcNAc, the nucleotide sugar donor substrate for O-GlcNAcylation enhanced histone O-GlcNAcylation and partially suppressed phosphorylation of histone H3 at serine 10 (H3S10ph).
21896475	9	28	theme	late	1664:1667	arg1	2					1679:1679	2	1679:1679	2	1679:1679	Histone O-GlcNAcylation is high in G(1) cells, declines throughout the S phase, increases again during late S/early G(2), and persists through late G(2) and mitosis.
21896475	9	28	theme	late	1664:1667	arg1	G					1677:1677	late S/early G	1664:1677	late S/early G(2)	1664:1680	Histone O-GlcNAcylation is high in G(1) cells, declines throughout the S phase, increases again during late S/early G(2), and persists through late G(2) and mitosis.
21896475	10	29	theme	histone	1760:1766	arg1	O-GlcNAcylation					1733:1747	O-GlcNAcylation	1733:1747	O-GlcNAcylation	1733:1747	Thus, O-GlcNAcylation is a novel histone post-translational modification regulating chromatin conformation during transcription and cell cycle progression.
21896475	10	29	theme	histone	1760:1766	arg1	modification					1787:1798	a novel histone post-translational modification	1752:1798	a novel histone post-translational modification regulating chromatin conformation during transcription and cell cycle progression	1752:1880	Thus, O-GlcNAcylation is a novel histone post-translational modification regulating chromatin conformation during transcription and cell cycle progression.
21896475	6	30	theme	H3	1115:1116	arg1	O-GlcNAcylation					1118:1132	histone H3 O-GlcNAcylation	1107:1132	histone H3 O-GlcNAcylation relative to its wild-type version	1107:1166	Expression of recombinant H3.3 harboring an S10A mutation abrogated histone H3 O-GlcNAcylation relative to its wild-type version, consistent with H3S10 being a site of histone O-GlcNAcylation (H3S10glc).
21896475	0	31	theme	histones	16:23	arg1	Modification					0:11	Modification	0:11	Modification of histones by sugar β-N-acetylglucosamine (GlcNAc)	0:63	Modification of histones by sugar β-N-acetylglucosamine (GlcNAc) occurs on multiple residues, including histone H3 serine 10, and is cell cycle-regulated.
21896475	1	32	theme	serines	252:258	arg1	serines					252:258	serines	252:258	serines	252:258	The monosaccharide, β-N-acetylglucosamine (GlcNAc), can be added to the hydroxyl group of either serines or threonines to generate an O-linked β-N-acetylglucosamine (O-GlcNAc) residue (Love, D. C., and Hanover, J. A. (2005) Sci.
21896475	1	32	theme	serines	252:258	arg1	threonines					263:272	threonines	263:272	threonines	263:272	The monosaccharide, β-N-acetylglucosamine (GlcNAc), can be added to the hydroxyl group of either serines or threonines to generate an O-linked β-N-acetylglucosamine (O-GlcNAc) residue (Love, D. C., and Hanover, J. A. (2005) Sci.
21896475	1	32	theme	serines	252:258	arg1	group					236:240	the hydroxyl group	223:240	the hydroxyl group of either serines or threonines	223:272	The monosaccharide, β-N-acetylglucosamine (GlcNAc), can be added to the hydroxyl group of either serines or threonines to generate an O-linked β-N-acetylglucosamine (O-GlcNAc) residue (Love, D. C., and Hanover, J. A. (2005) Sci.
21896475	4	33	theme	nucleosome	724:733	arg1	substrates					739:748	substrates	739:748	substrates for this glycosylation in the relative abundance H3, H4/H2B, and H2A	739:817	Here, we present evidence that in human cells all four core histones of the nucleosome are substrates for this glycosylation in the relative abundance H3, H4/H2B, and H2A.
21896475	4	33	theme	nucleosome	724:733	arg1	histones					708:715	all four core histones	694:715	all four core histones of the nucleosome	694:733	Here, we present evidence that in human cells all four core histones of the nucleosome are substrates for this glycosylation in the relative abundance H3, H4/H2B, and H2A.
21896475	1	34	link	O-linked	289:296	arg1	residue					331:337	an O-linked β-N-acetylglucosamine (O-GlcNAc) residue	286:337	an O-linked β-N-acetylglucosamine (O-GlcNAc) residue	286:337	The monosaccharide, β-N-acetylglucosamine (GlcNAc), can be added to the hydroxyl group of either serines or threonines to generate an O-linked β-N-acetylglucosamine (O-GlcNAc) residue (Love, D. C., and Hanover, J. A. (2005) Sci.
21896475	10	35	theme	cycle	1864:1868	arg1	progression					1870:1880	cell cycle progression	1859:1880	cell cycle progression	1859:1880	Thus, O-GlcNAcylation is a novel histone post-translational modification regulating chromatin conformation during transcription and cell cycle progression.
21896475	4	36	from	substrates	739:748	arg1	cells					688:692	human cells	682:692	human cells	682:692	Here, we present evidence that in human cells all four core histones of the nucleosome are substrates for this glycosylation in the relative abundance H3, H4/H2B, and H2A.
21896475	6	37	theme	H3.3	1065:1068	arg1	Expression					1039:1048	Expression	1039:1048	Expression of recombinant H3.3 harboring an S10A mutation	1039:1095	Expression of recombinant H3.3 harboring an S10A mutation abrogated histone H3 O-GlcNAcylation relative to its wild-type version, consistent with H3S10 being a site of histone O-GlcNAcylation (H3S10glc).
21896475	7	38	theme	H3K9me3	1369:1375	arg1	immunoprecipitation					1328:1346	immunoprecipitation	1328:1346	immunoprecipitation of either H3K4me3 or H3K9me3 (active or inactive histone marks, respectively)	1328:1424	Moreover, O-GlcNAcylated histones were lost from H3S10ph immunoprecipitates, whereas immunoprecipitation of either H3K4me3 or H3K9me3 (active or inactive histone marks, respectively) resulted in co-immunoprecipitation of O-GlcNAcylated histones.
21896475	7	39	theme	active	1378:1383	arg1	histone					1397:1403	active or inactive histone	1378:1403	active or inactive histone marks	1378:1409	Moreover, O-GlcNAcylated histones were lost from H3S10ph immunoprecipitates, whereas immunoprecipitation of either H3K4me3 or H3K9me3 (active or inactive histone marks, respectively) resulted in co-immunoprecipitation of O-GlcNAcylated histones.
21896475	0	40	theme	sugar	28:32	arg1	β-N-acetylglucosamine					34:54	sugar β-N-acetylglucosamine	28:54	sugar β-N-acetylglucosamine (GlcNAc)	28:63	Modification of histones by sugar β-N-acetylglucosamine (GlcNAc) occurs on multiple residues, including histone H3 serine 10, and is cell cycle-regulated.
21896475	0	40	theme	sugar	28:32	arg1	GlcNAc					57:62	GlcNAc	57:62	GlcNAc	57:62	Modification of histones by sugar β-N-acetylglucosamine (GlcNAc) occurs on multiple residues, including histone H3 serine 10, and is cell cycle-regulated.
21896475	1	41	theme	threonines	263:272	arg1	serines					252:258	serines	252:258	serines	252:258	The monosaccharide, β-N-acetylglucosamine (GlcNAc), can be added to the hydroxyl group of either serines or threonines to generate an O-linked β-N-acetylglucosamine (O-GlcNAc) residue (Love, D. C., and Hanover, J. A. (2005) Sci.
21896475	1	41	theme	threonines	263:272	arg1	threonines					263:272	threonines	263:272	threonines	263:272	The monosaccharide, β-N-acetylglucosamine (GlcNAc), can be added to the hydroxyl group of either serines or threonines to generate an O-linked β-N-acetylglucosamine (O-GlcNAc) residue (Love, D. C., and Hanover, J. A. (2005) Sci.
21896475	1	41	theme	threonines	263:272	arg1	group					236:240	the hydroxyl group	223:240	the hydroxyl group of either serines or threonines	223:272	The monosaccharide, β-N-acetylglucosamine (GlcNAc), can be added to the hydroxyl group of either serines or threonines to generate an O-linked β-N-acetylglucosamine (O-GlcNAc) residue (Love, D. C., and Hanover, J. A. (2005) Sci.
21896475	9	42	theme	G	1596:1596	arg1	cells					1601:1605	G(1) cells	1596:1605	G(1) cells	1596:1605	Histone O-GlcNAcylation is high in G(1) cells, declines throughout the S phase, increases again during late S/early G(2), and persists through late G(2) and mitosis.
21896475	5	43	theme	sugar	885:889	arg1	UDP-GlcNAc					858:867	UDP-GlcNAc	858:867	UDP-GlcNAc	858:867	Increasing the intracellular level of UDP-GlcNAc, the nucleotide sugar donor substrate for O-GlcNAcylation enhanced histone O-GlcNAcylation and partially suppressed phosphorylation of histone H3 at serine 10 (H3S10ph).
21896475	5	43	theme	sugar	885:889	arg1	substrate					897:905	the nucleotide sugar donor substrate	870:905	the nucleotide sugar donor substrate for O-GlcNAcylation	870:925	Increasing the intracellular level of UDP-GlcNAc, the nucleotide sugar donor substrate for O-GlcNAcylation enhanced histone O-GlcNAcylation and partially suppressed phosphorylation of histone H3 at serine 10 (H3S10ph).
21896475	6	44	theme	recombinant	1053:1063	arg1	H3.3					1065:1068	recombinant H3.3	1053:1068	recombinant H3.3 harboring an S10A mutation	1053:1095	Expression of recombinant H3.3 harboring an S10A mutation abrogated histone H3 O-GlcNAcylation relative to its wild-type version, consistent with H3S10 being a site of histone O-GlcNAcylation (H3S10glc).
21896475	7	45	theme	O-GlcNAcylated	1464:1477	arg1	histones					1479:1486	O-GlcNAcylated histones	1464:1486	O-GlcNAcylated histones	1464:1486	Moreover, O-GlcNAcylated histones were lost from H3S10ph immunoprecipitates, whereas immunoprecipitation of either H3K4me3 or H3K9me3 (active or inactive histone marks, respectively) resulted in co-immunoprecipitation of O-GlcNAcylated histones.
21896475	7	46	theme	histones	1479:1486	arg1	co-immunoprecipitation					1438:1459	co-immunoprecipitation	1438:1459	co-immunoprecipitation of O-GlcNAcylated histones	1438:1486	Moreover, O-GlcNAcylated histones were lost from H3S10ph immunoprecipitates, whereas immunoprecipitation of either H3K4me3 or H3K9me3 (active or inactive histone marks, respectively) resulted in co-immunoprecipitation of O-GlcNAcylated histones.
21896475	6	47	theme	wild-type	1150:1158	arg1	version					1160:1166	its wild-type version	1146:1166	its wild-type version	1146:1166	Expression of recombinant H3.3 harboring an S10A mutation abrogated histone H3 O-GlcNAcylation relative to its wild-type version, consistent with H3S10 being a site of histone O-GlcNAcylation (H3S10glc).
21896475	5	48	theme	donor	891:895	arg1	UDP-GlcNAc					858:867	UDP-GlcNAc	858:867	UDP-GlcNAc	858:867	Increasing the intracellular level of UDP-GlcNAc, the nucleotide sugar donor substrate for O-GlcNAcylation enhanced histone O-GlcNAcylation and partially suppressed phosphorylation of histone H3 at serine 10 (H3S10ph).
21896475	5	48	theme	donor	891:895	arg1	substrate					897:905	the nucleotide sugar donor substrate	870:905	the nucleotide sugar donor substrate for O-GlcNAcylation	870:925	Increasing the intracellular level of UDP-GlcNAc, the nucleotide sugar donor substrate for O-GlcNAcylation enhanced histone O-GlcNAcylation and partially suppressed phosphorylation of histone H3 at serine 10 (H3S10ph).
21896475	4	49	theme	core	703:706	arg1	substrates					739:748	substrates	739:748	substrates for this glycosylation in the relative abundance H3, H4/H2B, and H2A	739:817	Here, we present evidence that in human cells all four core histones of the nucleosome are substrates for this glycosylation in the relative abundance H3, H4/H2B, and H2A.
21896475	4	49	theme	core	703:706	arg1	histones					708:715	all four core histones	694:715	all four core histones of the nucleosome	694:733	Here, we present evidence that in human cells all four core histones of the nucleosome are substrates for this glycosylation in the relative abundance H3, H4/H2B, and H2A.
21896475	3	50	theme	post-translational	486:503	arg1	modification					513:524	This post-translational protein modification	481:524	This post-translational protein modification	481:524	This post-translational protein modification, termed O-GlcNAcylation, is reversible, analogous to phosphorylation, and has been implicated in many cellular processes.
21896475	5	51	theme	intracellular	835:847	arg1	level					849:853	the intracellular level	831:853	the intracellular level of UDP-GlcNAc, the nucleotide sugar donor substrate for O-GlcNAcylation	831:925	Increasing the intracellular level of UDP-GlcNAc, the nucleotide sugar donor substrate for O-GlcNAcylation enhanced histone O-GlcNAcylation and partially suppressed phosphorylation of histone H3 at serine 10 (H3S10ph).
21896475	6	52	theme	histone	1107:1113	arg1	O-GlcNAcylation					1118:1132	histone H3 O-GlcNAcylation	1107:1132	histone H3 O-GlcNAcylation relative to its wild-type version	1107:1166	Expression of recombinant H3.3 harboring an S10A mutation abrogated histone H3 O-GlcNAcylation relative to its wild-type version, consistent with H3S10 being a site of histone O-GlcNAcylation (H3S10glc).
21896475	7	53	theme	inactive	1388:1395	arg1	histone					1397:1403	active or inactive histone	1378:1403	active or inactive histone marks	1378:1409	Moreover, O-GlcNAcylated histones were lost from H3S10ph immunoprecipitates, whereas immunoprecipitation of either H3K4me3 or H3K9me3 (active or inactive histone marks, respectively) resulted in co-immunoprecipitation of O-GlcNAcylated histones.
21896475	5	54	theme	histone	1004:1010	arg1	H3					1012:1013	histone H3	1004:1013	histone H3	1004:1013	Increasing the intracellular level of UDP-GlcNAc, the nucleotide sugar donor substrate for O-GlcNAcylation enhanced histone O-GlcNAcylation and partially suppressed phosphorylation of histone H3 at serine 10 (H3S10ph).
21896475	4	55	dep	abundance	789:797	arg1	H4/H2B					803:808	H4/H2B	803:808	H4/H2B	803:808	Here, we present evidence that in human cells all four core histones of the nucleosome are substrates for this glycosylation in the relative abundance H3, H4/H2B, and H2A.
21896475	4	55	dep	abundance	789:797	arg1	H2A					815:817	H2A	815:817	H2A	815:817	Here, we present evidence that in human cells all four core histones of the nucleosome are substrates for this glycosylation in the relative abundance H3, H4/H2B, and H2A.
21896475	4	55	dep	abundance	789:797	arg1	H3					799:800	H3	799:800	H3	799:800	Here, we present evidence that in human cells all four core histones of the nucleosome are substrates for this glycosylation in the relative abundance H3, H4/H2B, and H2A.
21896475	3	56	theme	protein	505:511	arg1	modification					513:524	This post-translational protein modification	481:524	This post-translational protein modification	481:524	This post-translational protein modification, termed O-GlcNAcylation, is reversible, analogous to phosphorylation, and has been implicated in many cellular processes.
21896475	4	57	from	glycosylation	759:771	arg1	abundance					789:797	the relative abundance H3, H4/H2B, and H2A	776:817	the relative abundance H3, H4/H2B, and H2A	776:817	Here, we present evidence that in human cells all four core histones of the nucleosome are substrates for this glycosylation in the relative abundance H3, H4/H2B, and H2A.
21896475	1	58	dep	C.	349:350	arg1	Sci					379:381	Sci	379:381	Sci	379:381	The monosaccharide, β-N-acetylglucosamine (GlcNAc), can be added to the hydroxyl group of either serines or threonines to generate an O-linked β-N-acetylglucosamine (O-GlcNAc) residue (Love, D. C., and Hanover, J. A. (2005) Sci.
21896475	6	59	theme	relative	1134:1141	arg1	O-GlcNAcylation					1118:1132	histone H3 O-GlcNAcylation	1107:1132	histone H3 O-GlcNAcylation relative to its wild-type version	1107:1166	Expression of recombinant H3.3 harboring an S10A mutation abrogated histone H3 O-GlcNAcylation relative to its wild-type version, consistent with H3S10 being a site of histone O-GlcNAcylation (H3S10glc).
21896475	5	60	theme	UDP-GlcNAc	858:867	arg1	level					849:853	the intracellular level	831:853	the intracellular level of UDP-GlcNAc, the nucleotide sugar donor substrate for O-GlcNAcylation	831:925	Increasing the intracellular level of UDP-GlcNAc, the nucleotide sugar donor substrate for O-GlcNAcylation enhanced histone O-GlcNAcylation and partially suppressed phosphorylation of histone H3 at serine 10 (H3S10ph).
21896475	8	61	theme	cycle	1542:1546	arg1	progression					1548:1558	cell cycle progression	1537:1558	cell cycle progression	1537:1558	We also examined histone O-GlcNAcylation during cell cycle progression.
21896475	9	62	from	cells	1601:1605	arg1	high					1588:1591	high	1588:1591	high	1588:1591	Histone O-GlcNAcylation is high in G(1) cells, declines throughout the S phase, increases again during late S/early G(2), and persists through late G(2) and mitosis.
21896475	7	63	theme	H3K4me3	1358:1364	arg1	immunoprecipitation					1328:1346	immunoprecipitation	1328:1346	immunoprecipitation of either H3K4me3 or H3K9me3 (active or inactive histone marks, respectively)	1328:1424	Moreover, O-GlcNAcylated histones were lost from H3S10ph immunoprecipitates, whereas immunoprecipitation of either H3K4me3 or H3K9me3 (active or inactive histone marks, respectively) resulted in co-immunoprecipitation of O-GlcNAcylated histones.
21896475	10	64	theme	cell	1859:1862	arg1	progression					1870:1880	cell cycle progression	1859:1880	cell cycle progression	1859:1880	Thus, O-GlcNAcylation is a novel histone post-translational modification regulating chromatin conformation during transcription and cell cycle progression.
21896475	9	65	theme	late	1704:1707	arg1	G					1709:1709	late G	1704:1709	late G(2)	1704:1712	Histone O-GlcNAcylation is high in G(1) cells, declines throughout the S phase, increases again during late S/early G(2), and persists through late G(2) and mitosis.
21896475	9	65	theme	late	1704:1707	arg1	2					1711:1711	2	1711:1711	2	1711:1711	Histone O-GlcNAcylation is high in G(1) cells, declines throughout the S phase, increases again during late S/early G(2), and persists through late G(2) and mitosis.
21896475	8	66	theme	cell	1537:1540	arg1	progression					1548:1558	cell cycle progression	1537:1558	cell cycle progression	1537:1558	We also examined histone O-GlcNAcylation during cell cycle progression.
21896475	4	67	theme	relative	780:787	arg1	abundance					789:797	the relative abundance H3, H4/H2B, and H2A	776:817	the relative abundance H3, H4/H2B, and H2A	776:817	Here, we present evidence that in human cells all four core histones of the nucleosome are substrates for this glycosylation in the relative abundance H3, H4/H2B, and H2A.
21896475	1	68	theme	O-linked	289:296	arg1	residue					331:337	an O-linked β-N-acetylglucosamine (O-GlcNAc) residue	286:337	an O-linked β-N-acetylglucosamine (O-GlcNAc) residue	286:337	The monosaccharide, β-N-acetylglucosamine (GlcNAc), can be added to the hydroxyl group of either serines or threonines to generate an O-linked β-N-acetylglucosamine (O-GlcNAc) residue (Love, D. C., and Hanover, J. A. (2005) Sci.
21896475	9	69	theme	S/early	1669:1675	arg1	2					1679:1679	2	1679:1679	2	1679:1679	Histone O-GlcNAcylation is high in G(1) cells, declines throughout the S phase, increases again during late S/early G(2), and persists through late G(2) and mitosis.
21896475	9	69	theme	S/early	1669:1675	arg1	G					1677:1677	late S/early G	1664:1677	late S/early G(2)	1664:1680	Histone O-GlcNAcylation is high in G(1) cells, declines throughout the S phase, increases again during late S/early G(2), and persists through late G(2) and mitosis.
21896475	3	70	theme	cellular	628:635	arg1	processes					637:645	many cellular processes	623:645	many cellular processes	623:645	This post-translational protein modification, termed O-GlcNAcylation, is reversible, analogous to phosphorylation, and has been implicated in many cellular processes.
21896475	8	71	theme	histone	1506:1512	arg1	O-GlcNAcylation					1514:1528	histone O-GlcNAcylation	1506:1528	histone O-GlcNAcylation	1506:1528	We also examined histone O-GlcNAcylation during cell cycle progression.
21896475	3	72	theme	many	623:626	arg1	processes					637:645	many cellular processes	623:645	many cellular processes	623:645	This post-translational protein modification, termed O-GlcNAcylation, is reversible, analogous to phosphorylation, and has been implicated in many cellular processes.
7688323	0	0	theme	platelet	74:81	arg1	GPIIb/IIIa					92:101	the human platelet integrin GPIIb/IIIa	64:101	the human platelet integrin GPIIb/IIIa	64:101	Localization of an O-glycosylation site in the alpha-subunit of the human platelet integrin GPIIb/IIIa involved in Baka (HPA-3a) alloantigen expression.
7688323	3	1	theme	antibodies	690:699	arg1	loss					668:671	the loss	664:671	the loss of its anti-Baka antibodies binding ability	664:715	Here we show that the GPIIb fragment 704-856 contains the whole Baka epitope, and that chemical cleavage of a single O-linked oligosaccharide chain within this GPIIb domain correlates with the loss of its anti-Baka antibodies binding ability.
7688323	1	2	theme	glycoprotein	247:258	arg1	IIb					260:262	platelet glycoprotein IIb	238:262	platelet glycoprotein IIb	238:262	The human alloantigen system Baka/b is associated with a Ile843-->Ser replacement on platelet glycoprotein IIb, the alpha-subunit of the integrin receptor for fibrinogen (GPIIb/IIIa).
7688323	1	2	theme	glycoprotein	247:258	arg1	alpha-subunit					269:281	the alpha-subunit	265:281	the alpha-subunit of the integrin receptor for fibrinogen (GPIIb/IIIa)	265:334	The human alloantigen system Baka/b is associated with a Ile843-->Ser replacement on platelet glycoprotein IIb, the alpha-subunit of the integrin receptor for fibrinogen (GPIIb/IIIa).
7688323	0	3	theme	human	68:72	arg1	GPIIb/IIIa					92:101	the human platelet integrin GPIIb/IIIa	64:101	the human platelet integrin GPIIb/IIIa	64:101	Localization of an O-glycosylation site in the alpha-subunit of the human platelet integrin GPIIb/IIIa involved in Baka (HPA-3a) alloantigen expression.
7688323	2	4	theme	immunological	344:356	arg1	studies					358:364	Recent immunological studies	337:364	Recent immunological studies	337:364	Recent immunological studies indicate that sialylated oligosaccharide chain(s) are also implicated in expression of the Baka determinant.
7688323	0	5	theme	GPIIb/IIIa	92:101	arg1	alpha-subunit					47:59	the alpha-subunit	43:59	the alpha-subunit of the human platelet integrin GPIIb/IIIa	43:101	Localization of an O-glycosylation site in the alpha-subunit of the human platelet integrin GPIIb/IIIa involved in Baka (HPA-3a) alloantigen expression.
7688323	0	6	from	Localization	0:11	arg1	alpha-subunit					47:59	the alpha-subunit	43:59	the alpha-subunit of the human platelet integrin GPIIb/IIIa	43:101	Localization of an O-glycosylation site in the alpha-subunit of the human platelet integrin GPIIb/IIIa involved in Baka (HPA-3a) alloantigen expression.
7688323	3	7	theme	whole	533:537	arg1	epitope					544:550	the whole Baka epitope	529:550	the whole Baka epitope	529:550	Here we show that the GPIIb fragment 704-856 contains the whole Baka epitope, and that chemical cleavage of a single O-linked oligosaccharide chain within this GPIIb domain correlates with the loss of its anti-Baka antibodies binding ability.
7688323	0	8	theme	integrin	83:90	arg1	GPIIb/IIIa					92:101	the human platelet integrin GPIIb/IIIa	64:101	the human platelet integrin GPIIb/IIIa	64:101	Localization of an O-glycosylation site in the alpha-subunit of the human platelet integrin GPIIb/IIIa involved in Baka (HPA-3a) alloantigen expression.
7688323	4	9	theme	O-glycosylation	747:761	arg1	site					763:766	the O-glycosylation site	743:766	the O-glycosylation site	743:766	Ser847 was identified as the O-glycosylation site.
7688323	4	9	theme	O-glycosylation	747:761	arg1	Ser847					718:723	Ser847	718:723	Ser847	718:723	Ser847 was identified as the O-glycosylation site.
7688323	3	10	theme	Baka	539:542	arg1	epitope					544:550	the whole Baka epitope	529:550	the whole Baka epitope	529:550	Here we show that the GPIIb fragment 704-856 contains the whole Baka epitope, and that chemical cleavage of a single O-linked oligosaccharide chain within this GPIIb domain correlates with the loss of its anti-Baka antibodies binding ability.
7688323	5	11	theme	immunologic	962:972	arg1	observations					974:985	the immunologic observations	958:985	the immunologic observations	958:985	Therefore, our results show that the Ser847 modification is responsible for the expression of the GPIIb-specific Baka alloantigen, and provide thus a link between the molecular biology and the immunologic observations.
7688323	2	12	theme	oligosaccharide	391:405	arg1	s					413:413	sialylated oligosaccharide chain(s)	380:414	sialylated oligosaccharide chain(s)	380:414	Recent immunological studies indicate that sialylated oligosaccharide chain(s) are also implicated in expression of the Baka determinant.
7688323	1	13	theme	human	157:161	arg1	system					175:180	The human alloantigen system	153:180	The human alloantigen system Baka/b	153:187	The human alloantigen system Baka/b is associated with a Ile843-->Ser replacement on platelet glycoprotein IIb, the alpha-subunit of the integrin receptor for fibrinogen (GPIIb/IIIa).
7688323	1	14	theme	alloantigen	163:173	arg1	system					175:180	The human alloantigen system	153:180	The human alloantigen system Baka/b	153:187	The human alloantigen system Baka/b is associated with a Ile843-->Ser replacement on platelet glycoprotein IIb, the alpha-subunit of the integrin receptor for fibrinogen (GPIIb/IIIa).
7688323	2	15	theme	determinant	462:472	arg1	expression					439:448	expression	439:448	expression of the Baka determinant	439:472	Recent immunological studies indicate that sialylated oligosaccharide chain(s) are also implicated in expression of the Baka determinant.
7688323	2	16	gly	sialylated	380:389	arg1	s					413:413	sialylated oligosaccharide chain(s)	380:414	sialylated oligosaccharide chain(s)	380:414	Recent immunological studies indicate that sialylated oligosaccharide chain(s) are also implicated in expression of the Baka determinant.
7688323	1	17	gly	glycoprotein	247:258	arg1	glycoprotein					247:258	platelet glycoprotein IIb	238:262	platelet glycoprotein IIb	238:262	The human alloantigen system Baka/b is associated with a Ile843-->Ser replacement on platelet glycoprotein IIb, the alpha-subunit of the integrin receptor for fibrinogen (GPIIb/IIIa).
7688323	1	18	theme	system	175:180	arg1	Baka/b					182:187	The human alloantigen system Baka/b	153:187	The human alloantigen system Baka/b	153:187	The human alloantigen system Baka/b is associated with a Ile843-->Ser replacement on platelet glycoprotein IIb, the alpha-subunit of the integrin receptor for fibrinogen (GPIIb/IIIa).
7688323	3	19	link	O-linked	592:599	arg1	chain					617:621	a single O-linked oligosaccharide chain	583:621	a single O-linked oligosaccharide chain	583:621	Here we show that the GPIIb fragment 704-856 contains the whole Baka epitope, and that chemical cleavage of a single O-linked oligosaccharide chain within this GPIIb domain correlates with the loss of its anti-Baka antibodies binding ability.
7688323	2	20	theme	sialylated	380:389	arg1	s					413:413	sialylated oligosaccharide chain(s)	380:414	sialylated oligosaccharide chain(s)	380:414	Recent immunological studies indicate that sialylated oligosaccharide chain(s) are also implicated in expression of the Baka determinant.
7688323	0	21	theme	O-glycosylation	19:33	arg1	site					35:38	an O-glycosylation site	16:38	an O-glycosylation site	16:38	Localization of an O-glycosylation site in the alpha-subunit of the human platelet integrin GPIIb/IIIa involved in Baka (HPA-3a) alloantigen expression.
7688323	5	22	theme	molecular	936:944	arg1	biology					946:952	the molecular biology	932:952	the molecular biology	932:952	Therefore, our results show that the Ser847 modification is responsible for the expression of the GPIIb-specific Baka alloantigen, and provide thus a link between the molecular biology and the immunologic observations.
7688323	0	23	theme	Baka	115:118	arg1	expression					141:150	Baka (HPA-3a) alloantigen expression	115:150	Baka (HPA-3a) alloantigen expression	115:150	Localization of an O-glycosylation site in the alpha-subunit of the human platelet integrin GPIIb/IIIa involved in Baka (HPA-3a) alloantigen expression.
7688323	3	24	theme	GPIIb	635:639	arg1	domain					641:646	this GPIIb domain	630:646	this GPIIb domain	630:646	Here we show that the GPIIb fragment 704-856 contains the whole Baka epitope, and that chemical cleavage of a single O-linked oligosaccharide chain within this GPIIb domain correlates with the loss of its anti-Baka antibodies binding ability.
7688323	3	25	theme	GPIIb	497:501	arg1	fragment					503:510	the GPIIb fragment 704-856	493:518	the GPIIb fragment 704-856	493:518	Here we show that the GPIIb fragment 704-856 contains the whole Baka epitope, and that chemical cleavage of a single O-linked oligosaccharide chain within this GPIIb domain correlates with the loss of its anti-Baka antibodies binding ability.
7688323	1	26	theme	integrin	290:297	arg1	receptor					299:306	the integrin receptor	286:306	the integrin receptor for fibrinogen (GPIIb/IIIa)	286:334	The human alloantigen system Baka/b is associated with a Ile843-->Ser replacement on platelet glycoprotein IIb, the alpha-subunit of the integrin receptor for fibrinogen (GPIIb/IIIa).
7688323	5	27	theme	GPIIb-specific	867:880	arg1	alloantigen					887:897	the GPIIb-specific Baka alloantigen	863:897	the GPIIb-specific Baka alloantigen	863:897	Therefore, our results show that the Ser847 modification is responsible for the expression of the GPIIb-specific Baka alloantigen, and provide thus a link between the molecular biology and the immunologic observations.
7688323	0	28	theme	site	35:38	arg1	Localization					0:11	Localization	0:11	Localization of an O-glycosylation site in the alpha-subunit of the human platelet integrin GPIIb/IIIa	0:101	Localization of an O-glycosylation site in the alpha-subunit of the human platelet integrin GPIIb/IIIa involved in Baka (HPA-3a) alloantigen expression.
7688323	1	29	theme	receptor	299:306	arg1	IIb					260:262	platelet glycoprotein IIb	238:262	platelet glycoprotein IIb	238:262	The human alloantigen system Baka/b is associated with a Ile843-->Ser replacement on platelet glycoprotein IIb, the alpha-subunit of the integrin receptor for fibrinogen (GPIIb/IIIa).
7688323	1	29	theme	receptor	299:306	arg1	alpha-subunit					269:281	the alpha-subunit	265:281	the alpha-subunit of the integrin receptor for fibrinogen (GPIIb/IIIa)	265:334	The human alloantigen system Baka/b is associated with a Ile843-->Ser replacement on platelet glycoprotein IIb, the alpha-subunit of the integrin receptor for fibrinogen (GPIIb/IIIa).
7688323	0	30	theme	HPA-3a	121:126	arg1	expression					141:150	Baka (HPA-3a) alloantigen expression	115:150	Baka (HPA-3a) alloantigen expression	115:150	Localization of an O-glycosylation site in the alpha-subunit of the human platelet integrin GPIIb/IIIa involved in Baka (HPA-3a) alloantigen expression.
7688323	5	31	theme	Ser847	806:811	arg1	responsible					829:839	responsible	829:839	responsible	829:839	Therefore, our results show that the Ser847 modification is responsible for the expression of the GPIIb-specific Baka alloantigen, and provide thus a link between the molecular biology and the immunologic observations.
7688323	5	31	theme	Ser847	806:811	arg1	modification					813:824	the Ser847 modification	802:824	the Ser847 modification	802:824	Therefore, our results show that the Ser847 modification is responsible for the expression of the GPIIb-specific Baka alloantigen, and provide thus a link between the molecular biology and the immunologic observations.
7688323	2	32	theme	Baka	457:460	arg1	determinant					462:472	the Baka determinant	453:472	the Baka determinant	453:472	Recent immunological studies indicate that sialylated oligosaccharide chain(s) are also implicated in expression of the Baka determinant.
7688323	3	33	contain	contains	520:527	arg1	fragment					503:510	the GPIIb fragment 704-856	493:518	the GPIIb fragment 704-856	493:518	Here we show that the GPIIb fragment 704-856 contains the whole Baka epitope, and that chemical cleavage of a single O-linked oligosaccharide chain within this GPIIb domain correlates with the loss of its anti-Baka antibodies binding ability.
7688323	3	33	contain	contains	520:527	arg2	epitope					544:550	the whole Baka epitope	529:550	the whole Baka epitope	529:550	Here we show that the GPIIb fragment 704-856 contains the whole Baka epitope, and that chemical cleavage of a single O-linked oligosaccharide chain within this GPIIb domain correlates with the loss of its anti-Baka antibodies binding ability.
7688323	3	34	theme	chemical	562:569	arg1	cleavage					571:578	chemical cleavage	562:578	chemical cleavage of a single O-linked oligosaccharide chain within this GPIIb domain	562:646	Here we show that the GPIIb fragment 704-856 contains the whole Baka epitope, and that chemical cleavage of a single O-linked oligosaccharide chain within this GPIIb domain correlates with the loss of its anti-Baka antibodies binding ability.
7688323	2	35	theme	Recent	337:342	arg1	studies					358:364	Recent immunological studies	337:364	Recent immunological studies	337:364	Recent immunological studies indicate that sialylated oligosaccharide chain(s) are also implicated in expression of the Baka determinant.
7688323	0	36	theme	alloantigen	129:139	arg1	expression					141:150	Baka (HPA-3a) alloantigen expression	115:150	Baka (HPA-3a) alloantigen expression	115:150	Localization of an O-glycosylation site in the alpha-subunit of the human platelet integrin GPIIb/IIIa involved in Baka (HPA-3a) alloantigen expression.
7688323	0	37	gly	O-glycosylation	19:33	arg2	site					35:38	an O-glycosylation site	16:38	an O-glycosylation site	16:38	Localization of an O-glycosylation site in the alpha-subunit of the human platelet integrin GPIIb/IIIa involved in Baka (HPA-3a) alloantigen expression.
7688323	3	38	theme	oligosaccharide	601:615	arg1	chain					617:621	a single O-linked oligosaccharide chain	583:621	a single O-linked oligosaccharide chain	583:621	Here we show that the GPIIb fragment 704-856 contains the whole Baka epitope, and that chemical cleavage of a single O-linked oligosaccharide chain within this GPIIb domain correlates with the loss of its anti-Baka antibodies binding ability.
7688323	1	39	theme	Ile843-->Ser	210:221	arg1	replacement					223:233	a Ile843-->Ser replacement	208:233	a Ile843-->Ser replacement on platelet glycoprotein IIb, the alpha-subunit of the integrin receptor for fibrinogen (GPIIb/IIIa)	208:334	The human alloantigen system Baka/b is associated with a Ile843-->Ser replacement on platelet glycoprotein IIb, the alpha-subunit of the integrin receptor for fibrinogen (GPIIb/IIIa).
7688323	1	40	from	replacement	223:233	arg1	IIb					260:262	platelet glycoprotein IIb	238:262	platelet glycoprotein IIb	238:262	The human alloantigen system Baka/b is associated with a Ile843-->Ser replacement on platelet glycoprotein IIb, the alpha-subunit of the integrin receptor for fibrinogen (GPIIb/IIIa).
7688323	1	40	from	replacement	223:233	arg1	alpha-subunit					269:281	the alpha-subunit	265:281	the alpha-subunit of the integrin receptor for fibrinogen (GPIIb/IIIa)	265:334	The human alloantigen system Baka/b is associated with a Ile843-->Ser replacement on platelet glycoprotein IIb, the alpha-subunit of the integrin receptor for fibrinogen (GPIIb/IIIa).
7688323	3	41	theme	chain	617:621	arg1	cleavage					571:578	chemical cleavage	562:578	chemical cleavage of a single O-linked oligosaccharide chain within this GPIIb domain	562:646	Here we show that the GPIIb fragment 704-856 contains the whole Baka epitope, and that chemical cleavage of a single O-linked oligosaccharide chain within this GPIIb domain correlates with the loss of its anti-Baka antibodies binding ability.
7688323	4	42	gly	O-glycosylation	747:761	arg2	Ser847					718:723	Ser847	718:723	Ser847	718:723	Ser847 was identified as the O-glycosylation site.
7688323	4	42	gly	O-glycosylation	747:761	arg2	site					763:766	the O-glycosylation site	743:766	the O-glycosylation site	743:766	Ser847 was identified as the O-glycosylation site.
7688323	3	43	theme	single	585:590	arg1	chain					617:621	a single O-linked oligosaccharide chain	583:621	a single O-linked oligosaccharide chain	583:621	Here we show that the GPIIb fragment 704-856 contains the whole Baka epitope, and that chemical cleavage of a single O-linked oligosaccharide chain within this GPIIb domain correlates with the loss of its anti-Baka antibodies binding ability.
7688323	5	44	theme	Baka	882:885	arg1	alloantigen					887:897	the GPIIb-specific Baka alloantigen	863:897	the GPIIb-specific Baka alloantigen	863:897	Therefore, our results show that the Ser847 modification is responsible for the expression of the GPIIb-specific Baka alloantigen, and provide thus a link between the molecular biology and the immunologic observations.
7688323	2	45	theme	chain	407:411	arg1	s					413:413	sialylated oligosaccharide chain(s)	380:414	sialylated oligosaccharide chain(s)	380:414	Recent immunological studies indicate that sialylated oligosaccharide chain(s) are also implicated in expression of the Baka determinant.
7688323	3	46	theme	anti-Baka	680:688	arg1	antibodies					690:699	its anti-Baka antibodies	676:699	its anti-Baka antibodies binding ability	676:715	Here we show that the GPIIb fragment 704-856 contains the whole Baka epitope, and that chemical cleavage of a single O-linked oligosaccharide chain within this GPIIb domain correlates with the loss of its anti-Baka antibodies binding ability.
7688323	3	47	theme	O-linked	592:599	arg1	chain					617:621	a single O-linked oligosaccharide chain	583:621	a single O-linked oligosaccharide chain	583:621	Here we show that the GPIIb fragment 704-856 contains the whole Baka epitope, and that chemical cleavage of a single O-linked oligosaccharide chain within this GPIIb domain correlates with the loss of its anti-Baka antibodies binding ability.
7688323	5	48	theme	alloantigen	887:897	arg1	expression					849:858	the expression	845:858	the expression of the GPIIb-specific Baka alloantigen	845:897	Therefore, our results show that the Ser847 modification is responsible for the expression of the GPIIb-specific Baka alloantigen, and provide thus a link between the molecular biology and the immunologic observations.
7688323	1	49	theme	platelet	238:245	arg1	IIb					260:262	platelet glycoprotein IIb	238:262	platelet glycoprotein IIb	238:262	The human alloantigen system Baka/b is associated with a Ile843-->Ser replacement on platelet glycoprotein IIb, the alpha-subunit of the integrin receptor for fibrinogen (GPIIb/IIIa).
7688323	1	49	theme	platelet	238:245	arg1	alpha-subunit					269:281	the alpha-subunit	265:281	the alpha-subunit of the integrin receptor for fibrinogen (GPIIb/IIIa)	265:334	The human alloantigen system Baka/b is associated with a Ile843-->Ser replacement on platelet glycoprotein IIb, the alpha-subunit of the integrin receptor for fibrinogen (GPIIb/IIIa).
17307740	3	0	theme	catalytic	530:538	arg1	activities					565:574	the catalytic and motility-stimulating activities	526:574	the catalytic and motility-stimulating activities of NPP2	526:582	Mutagenesis and deglycosylation experiments revealed that only the glycosylation of Asn-524 is essential for the expression of the catalytic and motility-stimulating activities of NPP2.
17307740	0	1	theme	autotaxin	69:77	arg1	autotaxin					69:77	autotaxin	69:77	autotaxin	69:77	An essential oligomannosidic glycan chain in the catalytic domain of autotaxin, a secreted lysophospholipase-D.
17307740	0	1	theme	autotaxin	69:77	arg1	domain					59:64	the catalytic domain	45:64	the catalytic domain of autotaxin	45:77	An essential oligomannosidic glycan chain in the catalytic domain of autotaxin, a secreted lysophospholipase-D.
17307740	5	2	theme	Additional	702:711	arg1	studies					713:719	Additional studies	702:719	Additional studies	702:719	Additional studies show that this Asn-524-linked glycan is not accessible to alpha-1,2-mannosidase, suggesting that its non-reducing termini are buried inside the folded protein.
17307740	1	3	theme	cell	169:172	arg1	proliferation					174:186	cell proliferation	169:186	cell proliferation	169:186	Autotaxin/NPP2, a secreted lysophospholipase-D, promotes cell proliferation, survival, and motility by generating the signaling molecule lysophosphatidic acid.
17307740	6	4	theme	Native	1063:1068	arg1	PAGE					1070:1073	Blue Native PAGE	1058:1073	Blue Native PAGE	1058:1073	Consistent with a structural role for the Asn-524-linked glycan, only the mutation of Asn-524 augmented the sensitivity of NPP2 to proteolysis and increased its mobility during Blue Native PAGE.
17307740	0	5	theme	secreted	82:89	arg1	lysophospholipase-D					91:109	a secreted lysophospholipase-D	80:109	a secreted lysophospholipase-D	80:109	An essential oligomannosidic glycan chain in the catalytic domain of autotaxin, a secreted lysophospholipase-D.
17307740	0	5	theme	secreted	82:89	arg1	chain					36:40	An essential oligomannosidic glycan chain	0:40	An essential oligomannosidic glycan chain in the catalytic domain of autotaxin	0:77	An essential oligomannosidic glycan chain in the catalytic domain of autotaxin, a secreted lysophospholipase-D.
17307740	6	6	theme	Asn-524	967:973	arg1	mutation					955:962	only the mutation	946:962	only the mutation of Asn-524	946:973	Consistent with a structural role for the Asn-524-linked glycan, only the mutation of Asn-524 augmented the sensitivity of NPP2 to proteolysis and increased its mobility during Blue Native PAGE.
17307740	7	7	theme	structural	1162:1171	arg1	model					1173:1177	a structural model	1160:1177	a structural model of this domain	1160:1192	Asn-524 is phylogenetically conserved and maps to the catalytic domain of NPP2, but a structural model of this domain suggests that Asn-524 is remote from the catalytic site.
17307740	2	8	theme	pyrophosphatase/phosphodiesterase	305:337	arg1	NPP2					342:345	ectonucleotide pyrophosphatase/phosphodiesterase 2 (NPP2)	290:346	ectonucleotide pyrophosphatase/phosphodiesterase 2 (NPP2)	290:346	Here we show that ectonucleotide pyrophosphatase/phosphodiesterase 2 (NPP2) is N-glycosylated on Asn-53, Asn-410, and Asn-524.
17307740	6	9	theme	Blue	1058:1061	arg1	PAGE					1070:1073	Blue Native PAGE	1058:1073	Blue Native PAGE	1058:1073	Consistent with a structural role for the Asn-524-linked glycan, only the mutation of Asn-524 augmented the sensitivity of NPP2 to proteolysis and increased its mobility during Blue Native PAGE.
17307740	2	10	theme	ectonucleotide	290:303	arg1	NPP2					342:345	ectonucleotide pyrophosphatase/phosphodiesterase 2 (NPP2)	290:346	ectonucleotide pyrophosphatase/phosphodiesterase 2 (NPP2)	290:346	Here we show that ectonucleotide pyrophosphatase/phosphodiesterase 2 (NPP2) is N-glycosylated on Asn-53, Asn-410, and Asn-524.
17307740	7	11	theme	catalytic	1235:1243	arg1	site					1245:1248	the catalytic site	1231:1248	the catalytic site	1231:1248	Asn-524 is phylogenetically conserved and maps to the catalytic domain of NPP2, but a structural model of this domain suggests that Asn-524 is remote from the catalytic site.
17307740	6	12	link	Asn-524-linked	923:936	arg1	glycan					938:943	the Asn-524-linked glycan	919:943	the Asn-524-linked glycan	919:943	Consistent with a structural role for the Asn-524-linked glycan, only the mutation of Asn-524 augmented the sensitivity of NPP2 to proteolysis and increased its mobility during Blue Native PAGE.
17307740	7	13	theme	domain	1187:1192	arg1	model					1173:1177	a structural model	1160:1177	a structural model of this domain	1160:1192	Asn-524 is phylogenetically conserved and maps to the catalytic domain of NPP2, but a structural model of this domain suggests that Asn-524 is remote from the catalytic site.
17307740	3	14	theme	NPP2	579:582	arg1	activities					565:574	the catalytic and motility-stimulating activities	526:574	the catalytic and motility-stimulating activities of NPP2	526:582	Mutagenesis and deglycosylation experiments revealed that only the glycosylation of Asn-524 is essential for the expression of the catalytic and motility-stimulating activities of NPP2.
17307740	0	15	theme	essential	3:11	arg1	lysophospholipase-D					91:109	a secreted lysophospholipase-D	80:109	a secreted lysophospholipase-D	80:109	An essential oligomannosidic glycan chain in the catalytic domain of autotaxin, a secreted lysophospholipase-D.
17307740	0	15	theme	essential	3:11	arg1	chain					36:40	An essential oligomannosidic glycan chain	0:40	An essential oligomannosidic glycan chain in the catalytic domain of autotaxin	0:77	An essential oligomannosidic glycan chain in the catalytic domain of autotaxin, a secreted lysophospholipase-D.
17307740	0	16	from	chain	36:40	arg1	autotaxin					69:77	autotaxin	69:77	autotaxin	69:77	An essential oligomannosidic glycan chain in the catalytic domain of autotaxin, a secreted lysophospholipase-D.
17307740	0	16	from	chain	36:40	arg1	domain					59:64	the catalytic domain	45:64	the catalytic domain of autotaxin	45:77	An essential oligomannosidic glycan chain in the catalytic domain of autotaxin, a secreted lysophospholipase-D.
17307740	7	17	theme	NPP2	1150:1153	arg1	NPP2					1150:1153	NPP2	1150:1153	NPP2	1150:1153	Asn-524 is phylogenetically conserved and maps to the catalytic domain of NPP2, but a structural model of this domain suggests that Asn-524 is remote from the catalytic site.
17307740	7	17	theme	NPP2	1150:1153	arg1	domain					1140:1145	the catalytic domain	1126:1145	the catalytic domain of NPP2	1126:1153	Asn-524 is phylogenetically conserved and maps to the catalytic domain of NPP2, but a structural model of this domain suggests that Asn-524 is remote from the catalytic site.
17307740	8	18	theme	Asn-524-linked	1295:1308	arg1	chain					1317:1321	the Asn-524-linked glycan chain	1291:1321	the Asn-524-linked glycan chain of NPP2	1291:1329	Our study defines an essential role for the Asn-524-linked glycan chain of NPP2.
17307740	4	19	gly	glycoproteins	687:699	arg1	glycoproteins					687:699	mature eukaryotic glycoproteins	669:699	mature eukaryotic glycoproteins	669:699	The N-glycan on Asn-524 was identified as Man8/9GlcNAc2, which is rarely present on mature eukaryotic glycoproteins.
17307740	0	20	theme	glycan	29:34	arg1	lysophospholipase-D					91:109	a secreted lysophospholipase-D	80:109	a secreted lysophospholipase-D	80:109	An essential oligomannosidic glycan chain in the catalytic domain of autotaxin, a secreted lysophospholipase-D.
17307740	0	20	theme	glycan	29:34	arg1	chain					36:40	An essential oligomannosidic glycan chain	0:40	An essential oligomannosidic glycan chain in the catalytic domain of autotaxin	0:77	An essential oligomannosidic glycan chain in the catalytic domain of autotaxin, a secreted lysophospholipase-D.
17307740	4	21	located	present	658:664	arg1	glycoproteins					687:699	mature eukaryotic glycoproteins	669:699	mature eukaryotic glycoproteins	669:699	The N-glycan on Asn-524 was identified as Man8/9GlcNAc2, which is rarely present on mature eukaryotic glycoproteins.
17307740	4	21	located	present	658:664	arg2	N-glycan					589:596	The N-glycan	585:596	The N-glycan on Asn-524	585:607	The N-glycan on Asn-524 was identified as Man8/9GlcNAc2, which is rarely present on mature eukaryotic glycoproteins.
17307740	4	21	located	present	658:664	arg2	Man8/9GlcNAc2					627:639	Man8/9GlcNAc2	627:639	Man8/9GlcNAc2	627:639	The N-glycan on Asn-524 was identified as Man8/9GlcNAc2, which is rarely present on mature eukaryotic glycoproteins.
17307740	4	22	theme	mature	669:674	arg1	glycoproteins					687:699	mature eukaryotic glycoproteins	669:699	mature eukaryotic glycoproteins	669:699	The N-glycan on Asn-524 was identified as Man8/9GlcNAc2, which is rarely present on mature eukaryotic glycoproteins.
17307740	0	23	theme	oligomannosidic	13:27	arg1	lysophospholipase-D					91:109	a secreted lysophospholipase-D	80:109	a secreted lysophospholipase-D	80:109	An essential oligomannosidic glycan chain in the catalytic domain of autotaxin, a secreted lysophospholipase-D.
17307740	0	23	theme	oligomannosidic	13:27	arg1	chain					36:40	An essential oligomannosidic glycan chain	0:40	An essential oligomannosidic glycan chain in the catalytic domain of autotaxin	0:77	An essential oligomannosidic glycan chain in the catalytic domain of autotaxin, a secreted lysophospholipase-D.
17307740	8	24	link	Asn-524-linked	1295:1308	arg1	chain					1317:1321	the Asn-524-linked glycan chain	1291:1321	the Asn-524-linked glycan chain of NPP2	1291:1329	Our study defines an essential role for the Asn-524-linked glycan chain of NPP2.
17307740	6	25	with	Consistent	881:890	arg1	role					910:913	a structural role	897:913	a structural role for the Asn-524-linked glycan	897:943	Consistent with a structural role for the Asn-524-linked glycan, only the mutation of Asn-524 augmented the sensitivity of NPP2 to proteolysis and increased its mobility during Blue Native PAGE.
17307740	8	26	theme	glycan	1310:1315	arg1	chain					1317:1321	the Asn-524-linked glycan chain	1291:1321	the Asn-524-linked glycan chain of NPP2	1291:1329	Our study defines an essential role for the Asn-524-linked glycan chain of NPP2.
17307740	7	27	from	site	1245:1248	arg1	remote					1219:1224	remote	1219:1224	remote	1219:1224	Asn-524 is phylogenetically conserved and maps to the catalytic domain of NPP2, but a structural model of this domain suggests that Asn-524 is remote from the catalytic site.
17307740	3	28	theme	Asn-524	483:489	arg1	glycosylation					466:478	only the glycosylation	457:478	only the glycosylation of Asn-524	457:489	Mutagenesis and deglycosylation experiments revealed that only the glycosylation of Asn-524 is essential for the expression of the catalytic and motility-stimulating activities of NPP2.
17307740	3	28	theme	Asn-524	483:489	arg1	essential					494:502	essential	494:502	essential	494:502	Mutagenesis and deglycosylation experiments revealed that only the glycosylation of Asn-524 is essential for the expression of the catalytic and motility-stimulating activities of NPP2.
17307740	8	29	theme	NPP2	1326:1329	arg1	chain					1317:1321	the Asn-524-linked glycan chain	1291:1321	the Asn-524-linked glycan chain of NPP2	1291:1329	Our study defines an essential role for the Asn-524-linked glycan chain of NPP2.
17307740	7	30	theme	catalytic	1130:1138	arg1	NPP2					1150:1153	NPP2	1150:1153	NPP2	1150:1153	Asn-524 is phylogenetically conserved and maps to the catalytic domain of NPP2, but a structural model of this domain suggests that Asn-524 is remote from the catalytic site.
17307740	7	30	theme	catalytic	1130:1138	arg1	domain					1140:1145	the catalytic domain	1126:1145	the catalytic domain of NPP2	1126:1153	Asn-524 is phylogenetically conserved and maps to the catalytic domain of NPP2, but a structural model of this domain suggests that Asn-524 is remote from the catalytic site.
17307740	6	31	theme	Asn-524-linked	923:936	arg1	glycan					938:943	the Asn-524-linked glycan	919:943	the Asn-524-linked glycan	919:943	Consistent with a structural role for the Asn-524-linked glycan, only the mutation of Asn-524 augmented the sensitivity of NPP2 to proteolysis and increased its mobility during Blue Native PAGE.
17307740	4	32	theme	eukaryotic	676:685	arg1	glycoproteins					687:699	mature eukaryotic glycoproteins	669:699	mature eukaryotic glycoproteins	669:699	The N-glycan on Asn-524 was identified as Man8/9GlcNAc2, which is rarely present on mature eukaryotic glycoproteins.
17307740	3	33	theme	deglycosylation	415:429	arg1	experiments					431:441	deglycosylation experiments	415:441	deglycosylation experiments	415:441	Mutagenesis and deglycosylation experiments revealed that only the glycosylation of Asn-524 is essential for the expression of the catalytic and motility-stimulating activities of NPP2.
17307740	5	34	theme	non-reducing	822:833	arg1	termini					835:841	its non-reducing termini	818:841	its non-reducing termini	818:841	Additional studies show that this Asn-524-linked glycan is not accessible to alpha-1,2-mannosidase, suggesting that its non-reducing termini are buried inside the folded protein.
17307740	5	35	link	Asn-524-linked	736:749	arg1	glycan					751:756	this Asn-524-linked glycan	731:756	this Asn-524-linked glycan	731:756	Additional studies show that this Asn-524-linked glycan is not accessible to alpha-1,2-mannosidase, suggesting that its non-reducing termini are buried inside the folded protein.
17307740	5	36	theme	folded	865:870	arg1	protein					872:878	the folded protein	861:878	the folded protein	861:878	Additional studies show that this Asn-524-linked glycan is not accessible to alpha-1,2-mannosidase, suggesting that its non-reducing termini are buried inside the folded protein.
17307740	6	37	theme	NPP2	1004:1007	arg1	sensitivity					989:999	the sensitivity	985:999	the sensitivity of NPP2 to proteolysis	985:1022	Consistent with a structural role for the Asn-524-linked glycan, only the mutation of Asn-524 augmented the sensitivity of NPP2 to proteolysis and increased its mobility during Blue Native PAGE.
17307740	4	38	attach	present	658:664	arg1	glycoproteins					687:699	mature eukaryotic glycoproteins	669:699	mature eukaryotic glycoproteins	669:699	The N-glycan on Asn-524 was identified as Man8/9GlcNAc2, which is rarely present on mature eukaryotic glycoproteins.
17307740	4	38	attach	present	658:664	arg2	N-glycan					589:596	The N-glycan	585:596	The N-glycan on Asn-524	585:607	The N-glycan on Asn-524 was identified as Man8/9GlcNAc2, which is rarely present on mature eukaryotic glycoproteins.
17307740	4	38	attach	present	658:664	arg2	Man8/9GlcNAc2					627:639	Man8/9GlcNAc2	627:639	Man8/9GlcNAc2	627:639	The N-glycan on Asn-524 was identified as Man8/9GlcNAc2, which is rarely present on mature eukaryotic glycoproteins.
17307740	5	39	theme	Asn-524-linked	736:749	arg1	glycan					751:756	this Asn-524-linked glycan	731:756	this Asn-524-linked glycan	731:756	Additional studies show that this Asn-524-linked glycan is not accessible to alpha-1,2-mannosidase, suggesting that its non-reducing termini are buried inside the folded protein.
17307740	2	40	gly	N-glycosylated	351:364	arg1	NPP2					342:345	ectonucleotide pyrophosphatase/phosphodiesterase 2 (NPP2)	290:346	ectonucleotide pyrophosphatase/phosphodiesterase 2 (NPP2)	290:346	Here we show that ectonucleotide pyrophosphatase/phosphodiesterase 2 (NPP2) is N-glycosylated on Asn-53, Asn-410, and Asn-524.
17307740	2	40	gly	N-glycosylated	351:364	arg1	Asn-410					377:383	Asn-410	377:383	Asn-410	377:383	Here we show that ectonucleotide pyrophosphatase/phosphodiesterase 2 (NPP2) is N-glycosylated on Asn-53, Asn-410, and Asn-524.
17307740	2	40	gly	N-glycosylated	351:364	arg2	Asn-53					369:374	Asn-53	369:374	Asn-53	369:374	Here we show that ectonucleotide pyrophosphatase/phosphodiesterase 2 (NPP2) is N-glycosylated on Asn-53, Asn-410, and Asn-524.
17307740	2	40	gly	N-glycosylated	351:364	arg2	Asn-524					390:396	Asn-524	390:396	Asn-524	390:396	Here we show that ectonucleotide pyrophosphatase/phosphodiesterase 2 (NPP2) is N-glycosylated on Asn-53, Asn-410, and Asn-524.
17307740	2	40	gly	N-glycosylated	351:364	arg2	Asn-410					377:383	Asn-410	377:383	Asn-410	377:383	Here we show that ectonucleotide pyrophosphatase/phosphodiesterase 2 (NPP2) is N-glycosylated on Asn-53, Asn-410, and Asn-524.
17307740	2	40	gly	N-glycosylated	351:364	arg2	NPP2					342:345	ectonucleotide pyrophosphatase/phosphodiesterase 2 (NPP2)	290:346	ectonucleotide pyrophosphatase/phosphodiesterase 2 (NPP2)	290:346	Here we show that ectonucleotide pyrophosphatase/phosphodiesterase 2 (NPP2) is N-glycosylated on Asn-53, Asn-410, and Asn-524.
17307740	2	40	gly	N-glycosylated	351:364	arg1	Asn-524					390:396	Asn-524	390:396	Asn-524	390:396	Here we show that ectonucleotide pyrophosphatase/phosphodiesterase 2 (NPP2) is N-glycosylated on Asn-53, Asn-410, and Asn-524.
17307740	2	40	gly	N-glycosylated	351:364	arg1	Asn-53					369:374	Asn-53	369:374	Asn-53	369:374	Here we show that ectonucleotide pyrophosphatase/phosphodiesterase 2 (NPP2) is N-glycosylated on Asn-53, Asn-410, and Asn-524.
17307740	6	41	theme	structural	899:908	arg1	role					910:913	a structural role	897:913	a structural role for the Asn-524-linked glycan	897:943	Consistent with a structural role for the Asn-524-linked glycan, only the mutation of Asn-524 augmented the sensitivity of NPP2 to proteolysis and increased its mobility during Blue Native PAGE.
17307740	3	42	gly	glycosylation	466:478	arg1	Asn-524					483:489	Asn-524	483:489	Asn-524	483:489	Mutagenesis and deglycosylation experiments revealed that only the glycosylation of Asn-524 is essential for the expression of the catalytic and motility-stimulating activities of NPP2.
17307740	3	42	gly	glycosylation	466:478	arg1	activities					565:574	the catalytic and motility-stimulating activities	526:574	the catalytic and motility-stimulating activities of NPP2	526:582	Mutagenesis and deglycosylation experiments revealed that only the glycosylation of Asn-524 is essential for the expression of the catalytic and motility-stimulating activities of NPP2.
17307740	1	43	theme	secreted	130:137	arg1	Autotaxin/NPP2					112:125	Autotaxin/NPP2	112:125	Autotaxin/NPP2	112:125	Autotaxin/NPP2, a secreted lysophospholipase-D, promotes cell proliferation, survival, and motility by generating the signaling molecule lysophosphatidic acid.
17307740	1	43	theme	secreted	130:137	arg1	lysophospholipase-D					139:157	a secreted lysophospholipase-D	128:157	a secreted lysophospholipase-D	128:157	Autotaxin/NPP2, a secreted lysophospholipase-D, promotes cell proliferation, survival, and motility by generating the signaling molecule lysophosphatidic acid.
17307740	8	44	theme	essential	1272:1280	arg1	role					1282:1285	an essential role	1269:1285	an essential role for the Asn-524-linked glycan chain of NPP2	1269:1329	Our study defines an essential role for the Asn-524-linked glycan chain of NPP2.
17307740	1	45	theme	signaling	230:238	arg1	acid					266:269	the signaling molecule lysophosphatidic acid	226:269	the signaling molecule lysophosphatidic acid	226:269	Autotaxin/NPP2, a secreted lysophospholipase-D, promotes cell proliferation, survival, and motility by generating the signaling molecule lysophosphatidic acid.
17307740	3	46	theme	motility-stimulating	544:563	arg1	activities					565:574	the catalytic and motility-stimulating activities	526:574	the catalytic and motility-stimulating activities of NPP2	526:582	Mutagenesis and deglycosylation experiments revealed that only the glycosylation of Asn-524 is essential for the expression of the catalytic and motility-stimulating activities of NPP2.
17307740	1	47	theme	molecule	240:247	arg1	acid					266:269	the signaling molecule lysophosphatidic acid	226:269	the signaling molecule lysophosphatidic acid	226:269	Autotaxin/NPP2, a secreted lysophospholipase-D, promotes cell proliferation, survival, and motility by generating the signaling molecule lysophosphatidic acid.
17307740	0	48	theme	catalytic	49:57	arg1	autotaxin					69:77	autotaxin	69:77	autotaxin	69:77	An essential oligomannosidic glycan chain in the catalytic domain of autotaxin, a secreted lysophospholipase-D.
17307740	0	48	theme	catalytic	49:57	arg1	domain					59:64	the catalytic domain	45:64	the catalytic domain of autotaxin	45:77	An essential oligomannosidic glycan chain in the catalytic domain of autotaxin, a secreted lysophospholipase-D.
17307740	4	49	from	N-glycan	589:596	arg1	Asn-524					601:607	Asn-524	601:607	Asn-524	601:607	The N-glycan on Asn-524 was identified as Man8/9GlcNAc2, which is rarely present on mature eukaryotic glycoproteins.
17307740	3	50	theme	activities	565:574	arg1	expression					512:521	the expression	508:521	the expression of the catalytic and motility-stimulating activities of NPP2	508:582	Mutagenesis and deglycosylation experiments revealed that only the glycosylation of Asn-524 is essential for the expression of the catalytic and motility-stimulating activities of NPP2.
17307740	1	51	theme	lysophosphatidic	249:264	arg1	acid					266:269	the signaling molecule lysophosphatidic acid	226:269	the signaling molecule lysophosphatidic acid	226:269	Autotaxin/NPP2, a secreted lysophospholipase-D, promotes cell proliferation, survival, and motility by generating the signaling molecule lysophosphatidic acid.
24211831	3	0	theme	galectin-3-induced	503:520	arg1	apoptosis					522:530	galectin-3-induced apoptosis	503:530	galectin-3-induced apoptosis	503:530	In this study, no apoptosis induced by galectin-3 was detected in CD45RO-transfected cells, whereas apoptosis of CD45RABC-transfected cells was observed, implying that O-glycans on CD45 might play roles in galectin-3-induced apoptosis.
24211831	4	1	theme	O-glycans	595:603	arg1	role					587:590	the role	583:590	the role of O-glycans on CD45	583:611	O-Glycosylation inhibition assay further suggests the role of O-glycans on CD45 in regulation of galectin-3-induced apoptosis.
24211831	5	2	from	N109	818:821	arg1	deglycosylation					792:806	deglycosylation	792:806	deglycosylation at N36 or N109 of CD45RO	792:831	We also found that deglycosylation at N327 of CD45RO resulted in increased binding to galectin-3 without affecting apoptosis, while deglycosylation at N36 or N109 of CD45RO enhanced galectin-3-induced apoptosis.
24211831	5	3	gly	deglycosylation	792:806	arg2	N36					811:813	N36	811:813	N36	811:813	We also found that deglycosylation at N327 of CD45RO resulted in increased binding to galectin-3 without affecting apoptosis, while deglycosylation at N36 or N109 of CD45RO enhanced galectin-3-induced apoptosis.
24211831	5	3	gly	deglycosylation	792:806	arg1	N109					818:821	N109	818:821	N109	818:821	We also found that deglycosylation at N327 of CD45RO resulted in increased binding to galectin-3 without affecting apoptosis, while deglycosylation at N36 or N109 of CD45RO enhanced galectin-3-induced apoptosis.
24211831	5	3	gly	deglycosylation	792:806	arg2	N109					818:821	N109	818:821	N109	818:821	We also found that deglycosylation at N327 of CD45RO resulted in increased binding to galectin-3 without affecting apoptosis, while deglycosylation at N36 or N109 of CD45RO enhanced galectin-3-induced apoptosis.
24211831	5	3	gly	deglycosylation	792:806	arg1	N36					811:813	N36	811:813	N36	811:813	We also found that deglycosylation at N327 of CD45RO resulted in increased binding to galectin-3 without affecting apoptosis, while deglycosylation at N36 or N109 of CD45RO enhanced galectin-3-induced apoptosis.
24211831	2	4	gly	N-glycosylated	281:294	arg1	CD45RO					266:271	CD45RO	266:271	CD45RO	266:271	CD45RABC is heavily O-glycosylated and N-glycosylated, while CD45RO is only N-glycosylated.
24211831	5	5	from	N327	698:701	arg1	deglycosylation					679:693	deglycosylation	679:693	deglycosylation at N327 of CD45RO	679:711	We also found that deglycosylation at N327 of CD45RO resulted in increased binding to galectin-3 without affecting apoptosis, while deglycosylation at N36 or N109 of CD45RO enhanced galectin-3-induced apoptosis.
24211831	1	6	theme	cells	159:163	arg1	apoptosis					139:147	apoptosis	139:147	apoptosis of Jurkat cells	139:163	Galectin-3 has been reported to induce apoptosis of Jurkat cells through binding receptors such as CD45.
24211831	5	7	gly	deglycosylation	679:693	arg2	N327					698:701	N327	698:701	N327 of CD45RO	698:711	We also found that deglycosylation at N327 of CD45RO resulted in increased binding to galectin-3 without affecting apoptosis, while deglycosylation at N36 or N109 of CD45RO enhanced galectin-3-induced apoptosis.
24211831	5	7	gly	deglycosylation	679:693	arg1	N327					698:701	N327	698:701	N327 of CD45RO	698:711	We also found that deglycosylation at N327 of CD45RO resulted in increased binding to galectin-3 without affecting apoptosis, while deglycosylation at N36 or N109 of CD45RO enhanced galectin-3-induced apoptosis.
24211831	5	8	theme	galectin-3-induced	842:859	arg1	apoptosis					861:869	galectin-3-induced apoptosis	842:869	galectin-3-induced apoptosis	842:869	We also found that deglycosylation at N327 of CD45RO resulted in increased binding to galectin-3 without affecting apoptosis, while deglycosylation at N36 or N109 of CD45RO enhanced galectin-3-induced apoptosis.
24211831	6	9	theme	cells	939:943	arg1	apoptosis					919:927	galectin-3-induced apoptosis	900:927	galectin-3-induced apoptosis of Jurkat cells	900:943	These data demonstrate that galectin-3-induced apoptosis of Jurkat cells is regulated by both O-glycans and N-glycans on CD45.
24211831	3	10	theme	cells	431:435	arg1	apoptosis					397:405	apoptosis	397:405	apoptosis of CD45RABC-transfected cells	397:435	In this study, no apoptosis induced by galectin-3 was detected in CD45RO-transfected cells, whereas apoptosis of CD45RABC-transfected cells was observed, implying that O-glycans on CD45 might play roles in galectin-3-induced apoptosis.
24211831	4	11	from	role	587:590	arg1	CD45					608:611	CD45	608:611	CD45	608:611	O-Glycosylation inhibition assay further suggests the role of O-glycans on CD45 in regulation of galectin-3-induced apoptosis.
24211831	0	12	theme	apoptosis	33:41	arg1	Regulation					0:9	Regulation	0:9	Regulation of galectin-3-induced apoptosis of Jurkat cells by both O-glycans and N-glycans on CD45.	0:98	Regulation of galectin-3-induced apoptosis of Jurkat cells by both O-glycans and N-glycans on CD45.
24211831	5	13	theme	increased	725:733	arg1	binding					735:741	increased binding	725:741	increased binding to galectin-3	725:755	We also found that deglycosylation at N327 of CD45RO resulted in increased binding to galectin-3 without affecting apoptosis, while deglycosylation at N36 or N109 of CD45RO enhanced galectin-3-induced apoptosis.
24211831	3	14	theme	CD45RO-transfected	363:380	arg1	cells					382:386	CD45RO-transfected cells	363:386	CD45RO-transfected cells	363:386	In this study, no apoptosis induced by galectin-3 was detected in CD45RO-transfected cells, whereas apoptosis of CD45RABC-transfected cells was observed, implying that O-glycans on CD45 might play roles in galectin-3-induced apoptosis.
24211831	0	15	from	N-glycans	81:89	arg1	CD45					94:97	CD45	94:97	CD45	94:97	Regulation of galectin-3-induced apoptosis of Jurkat cells by both O-glycans and N-glycans on CD45.
24211831	1	16	theme	Jurkat	152:157	arg1	cells					159:163	Jurkat cells	152:163	Jurkat cells	152:163	Galectin-3 has been reported to induce apoptosis of Jurkat cells through binding receptors such as CD45.
24211831	0	17	theme	Jurkat	46:51	arg1	cells					53:57	Jurkat cells	46:57	Jurkat cells	46:57	Regulation of galectin-3-induced apoptosis of Jurkat cells by both O-glycans and N-glycans on CD45.
24211831	2	18	gly	O-glycosylated	225:238	arg1	CD45RABC					205:212	CD45RABC	205:212	CD45RABC	205:212	CD45RABC is heavily O-glycosylated and N-glycosylated, while CD45RO is only N-glycosylated.
24211831	4	19	theme	inhibition	549:558	arg1	assay					560:564	O-Glycosylation inhibition assay	533:564	O-Glycosylation inhibition assay	533:564	O-Glycosylation inhibition assay further suggests the role of O-glycans on CD45 in regulation of galectin-3-induced apoptosis.
24211831	3	20	theme	CD45RABC-transfected	410:429	arg1	cells					431:435	CD45RABC-transfected cells	410:435	CD45RABC-transfected cells	410:435	In this study, no apoptosis induced by galectin-3 was detected in CD45RO-transfected cells, whereas apoptosis of CD45RABC-transfected cells was observed, implying that O-glycans on CD45 might play roles in galectin-3-induced apoptosis.
24211831	0	21	from	O-glycans	67:75	arg1	CD45					94:97	CD45	94:97	CD45	94:97	Regulation of galectin-3-induced apoptosis of Jurkat cells by both O-glycans and N-glycans on CD45.
24211831	4	22	theme	O-Glycosylation	533:547	arg1	assay					560:564	O-Glycosylation inhibition assay	533:564	O-Glycosylation inhibition assay	533:564	O-Glycosylation inhibition assay further suggests the role of O-glycans on CD45 in regulation of galectin-3-induced apoptosis.
24211831	5	23	theme	CD45RO	826:831	arg1	N109					818:821	N109	818:821	N109	818:821	We also found that deglycosylation at N327 of CD45RO resulted in increased binding to galectin-3 without affecting apoptosis, while deglycosylation at N36 or N109 of CD45RO enhanced galectin-3-induced apoptosis.
24211831	5	23	theme	CD45RO	826:831	arg1	N36					811:813	N36	811:813	N36	811:813	We also found that deglycosylation at N327 of CD45RO resulted in increased binding to galectin-3 without affecting apoptosis, while deglycosylation at N36 or N109 of CD45RO enhanced galectin-3-induced apoptosis.
24211831	6	24	theme	galectin-3-induced	900:917	arg1	apoptosis					919:927	galectin-3-induced apoptosis	900:927	galectin-3-induced apoptosis of Jurkat cells	900:943	These data demonstrate that galectin-3-induced apoptosis of Jurkat cells is regulated by both O-glycans and N-glycans on CD45.
24211831	6	25	theme	Jurkat	932:937	arg1	cells					939:943	Jurkat cells	932:943	Jurkat cells	932:943	These data demonstrate that galectin-3-induced apoptosis of Jurkat cells is regulated by both O-glycans and N-glycans on CD45.
24211831	0	26	theme	cells	53:57	arg1	apoptosis					33:41	galectin-3-induced apoptosis	14:41	galectin-3-induced apoptosis of Jurkat cells	14:57	Regulation of galectin-3-induced apoptosis of Jurkat cells by both O-glycans and N-glycans on CD45.
24211831	5	27	theme	CD45RO	706:711	arg1	N327					698:701	N327	698:701	N327 of CD45RO	698:711	We also found that deglycosylation at N327 of CD45RO resulted in increased binding to galectin-3 without affecting apoptosis, while deglycosylation at N36 or N109 of CD45RO enhanced galectin-3-induced apoptosis.
24211831	3	28	from	O-glycans	465:473	arg1	CD45					478:481	CD45	478:481	CD45	478:481	In this study, no apoptosis induced by galectin-3 was detected in CD45RO-transfected cells, whereas apoptosis of CD45RABC-transfected cells was observed, implying that O-glycans on CD45 might play roles in galectin-3-induced apoptosis.
24211831	5	29	from	N36	811:813	arg1	deglycosylation					792:806	deglycosylation	792:806	deglycosylation at N36 or N109 of CD45RO	792:831	We also found that deglycosylation at N327 of CD45RO resulted in increased binding to galectin-3 without affecting apoptosis, while deglycosylation at N36 or N109 of CD45RO enhanced galectin-3-induced apoptosis.
24211831	4	30	theme	apoptosis	649:657	arg1	regulation					616:625	regulation	616:625	regulation of galectin-3-induced apoptosis	616:657	O-Glycosylation inhibition assay further suggests the role of O-glycans on CD45 in regulation of galectin-3-induced apoptosis.
24211831	3	31	located	detected	351:358	arg1	cells					382:386	CD45RO-transfected cells	363:386	CD45RO-transfected cells	363:386	In this study, no apoptosis induced by galectin-3 was detected in CD45RO-transfected cells, whereas apoptosis of CD45RABC-transfected cells was observed, implying that O-glycans on CD45 might play roles in galectin-3-induced apoptosis.
24211831	3	31	located	detected	351:358	arg2	apoptosis					315:323	no apoptosis	312:323	no apoptosis induced by galectin-3	312:345	In this study, no apoptosis induced by galectin-3 was detected in CD45RO-transfected cells, whereas apoptosis of CD45RABC-transfected cells was observed, implying that O-glycans on CD45 might play roles in galectin-3-induced apoptosis.
24211831	3	31	located	detected	351:358	arg1	study					305:309	this study	300:309	this study	300:309	In this study, no apoptosis induced by galectin-3 was detected in CD45RO-transfected cells, whereas apoptosis of CD45RABC-transfected cells was observed, implying that O-glycans on CD45 might play roles in galectin-3-induced apoptosis.
24211831	0	32	theme	galectin-3-induced	14:31	arg1	apoptosis					33:41	galectin-3-induced apoptosis	14:41	galectin-3-induced apoptosis of Jurkat cells	14:57	Regulation of galectin-3-induced apoptosis of Jurkat cells by both O-glycans and N-glycans on CD45.
24211831	4	33	theme	galectin-3-induced	630:647	arg1	apoptosis					649:657	galectin-3-induced apoptosis	630:657	galectin-3-induced apoptosis	630:657	O-Glycosylation inhibition assay further suggests the role of O-glycans on CD45 in regulation of galectin-3-induced apoptosis.
14760718	7	0	theme	digest	928:933	arg1	mixture					935:941	the digest mixture	924:941	the digest mixture	924:941	Glycosylated peptides are then selected from the digest mixture by a second lectin chromatography step.
14760718	4	1	from	information	540:550	arg1	N-glycosylation					555:569	N-glycosylation	555:569	N-glycosylation	555:569	However, information on N-glycosylation can be gained at an intermediary level.
14760718	1	2	theme	choice	147:152	arg1	method					137:142	the method	133:142	the method of choice for characterization of post-translationally modified proteins	133:215	In the last few years mass spectrometry has become the method of choice for characterization of post-translationally modified proteins.
14760718	7	3	theme	lectin	955:960	arg1	step					977:980	a second lectin chromatography step	946:980	a second lectin chromatography step	946:980	Glycosylated peptides are then selected from the digest mixture by a second lectin chromatography step.
14760718	9	4	theme	wheat	1208:1212	arg1	lectins					1180:1186	two different lectins	1166:1186	two different lectins	1166:1186	Using two different lectins, concanavalin A and wheat germ agglutinin, this procedure was applied to human serum and a total of 86 N-glycosylation sites in 77 proteins were identified.
14760718	9	4	theme	wheat	1208:1212	arg1	agglutinin					1219:1228	wheat germ agglutinin	1208:1228	wheat germ agglutinin	1208:1228	Using two different lectins, concanavalin A and wheat germ agglutinin, this procedure was applied to human serum and a total of 86 N-glycosylation sites in 77 proteins were identified.
14760718	8	5	theme	on-line	1096:1102	arg1	chromatography					1126:1139	on-line reversed-phase liquid chromatography	1096:1139	on-line reversed-phase liquid chromatography mass spectrometry	1096:1157	The glycan components are removed with N-glycosidase F and the peptides digested with trypsin before analysis by on-line reversed-phase liquid chromatography mass spectrometry.
14760718	9	6	theme	human	1261:1265	arg1	serum					1267:1271	human serum	1261:1271	human serum	1261:1271	Using two different lectins, concanavalin A and wheat germ agglutinin, this procedure was applied to human serum and a total of 86 N-glycosylation sites in 77 proteins were identified.
14760718	2	7	theme	many	347:350	arg1	oligosaccharides					362:377	many different oligosaccharides	347:377	many different oligosaccharides	347:377	Whereas most protein chemical modifications are binary in the sense that only one change can be associated with a given residue, many different oligosaccharides can be attached to a glycosylation site residue.
14760718	5	8	theme	complex	680:686	arg1	mixtures					688:695	complex mixtures	680:695	complex mixtures	680:695	Here we demonstrate a procedure for mapping N-glycosylation sites in complex mixtures by reducing sample complexity and enriching glycoprotein content.
14760718	2	9	gly	glycosylation	400:412	arg2	site					414:417	a glycosylation site residue	398:425	a glycosylation site residue	398:425	Whereas most protein chemical modifications are binary in the sense that only one change can be associated with a given residue, many different oligosaccharides can be attached to a glycosylation site residue.
14760718	2	9	gly	glycosylation	400:412	arg2	residue					419:425	a glycosylation site residue	398:425	a glycosylation site residue	398:425	Whereas most protein chemical modifications are binary in the sense that only one change can be associated with a given residue, many different oligosaccharides can be attached to a glycosylation site residue.
14760718	0	10	gly	N-glycosylated	14:27	arg1	proteins					29:36	N-glycosylated proteins	14:36	N-glycosylated proteins	14:36	Screening for N-glycosylated proteins by liquid chromatography mass spectrometry.
14760718	8	11	theme	chromatography	1126:1139	arg1	spectrometry					1146:1157	on-line reversed-phase liquid chromatography mass spectrometry	1096:1157	on-line reversed-phase liquid chromatography mass spectrometry	1096:1157	The glycan components are removed with N-glycosidase F and the peptides digested with trypsin before analysis by on-line reversed-phase liquid chromatography mass spectrometry.
14760718	9	12	from	proteins	1319:1326	arg1	total					1279:1283	a total	1277:1283	a total of 86 N-glycosylation sites in 77 proteins	1277:1326	Using two different lectins, concanavalin A and wheat germ agglutinin, this procedure was applied to human serum and a total of 86 N-glycosylation sites in 77 proteins were identified.
14760718	8	13	theme	liquid	1119:1124	arg1	chromatography					1126:1139	on-line reversed-phase liquid chromatography	1096:1139	on-line reversed-phase liquid chromatography mass spectrometry	1096:1157	The glycan components are removed with N-glycosidase F and the peptides digested with trypsin before analysis by on-line reversed-phase liquid chromatography mass spectrometry.
14760718	2	14	theme	different	352:360	arg1	oligosaccharides					362:377	many different oligosaccharides	347:377	many different oligosaccharides	347:377	Whereas most protein chemical modifications are binary in the sense that only one change can be associated with a given residue, many different oligosaccharides can be attached to a glycosylation site residue.
14760718	5	15	gly	N-glycosylation	655:669	arg2	sites					671:675	N-glycosylation sites	655:675	N-glycosylation sites in complex mixtures	655:695	Here we demonstrate a procedure for mapping N-glycosylation sites in complex mixtures by reducing sample complexity and enriching glycoprotein content.
14760718	9	16	from	sites	1307:1311	arg1	proteins					1319:1326	77 proteins	1316:1326	77 proteins	1316:1326	Using two different lectins, concanavalin A and wheat germ agglutinin, this procedure was applied to human serum and a total of 86 N-glycosylation sites in 77 proteins were identified.
14760718	6	17	theme	Glycosylated	763:774	arg1	proteins					776:783	Glycosylated proteins	763:783	Glycosylated proteins	763:783	Glycosylated proteins are selected by an initial lectin chromatography step and digested with endoproteinase Lys-C.
14760718	6	18	theme	endoproteinase	857:870	arg1	Lys-C					872:876	endoproteinase Lys-C	857:876	endoproteinase Lys-C	857:876	Glycosylated proteins are selected by an initial lectin chromatography step and digested with endoproteinase Lys-C.
14760718	9	19	theme	different	1170:1178	arg1	lectins					1180:1186	two different lectins	1166:1186	two different lectins	1166:1186	Using two different lectins, concanavalin A and wheat germ agglutinin, this procedure was applied to human serum and a total of 86 N-glycosylation sites in 77 proteins were identified.
14760718	9	19	theme	different	1170:1178	arg1	A					1202:1202	concanavalin A	1189:1202	concanavalin A	1189:1202	Using two different lectins, concanavalin A and wheat germ agglutinin, this procedure was applied to human serum and a total of 86 N-glycosylation sites in 77 proteins were identified.
14760718	9	19	theme	different	1170:1178	arg1	agglutinin					1219:1228	wheat germ agglutinin	1208:1228	wheat germ agglutinin	1208:1228	Using two different lectins, concanavalin A and wheat germ agglutinin, this procedure was applied to human serum and a total of 86 N-glycosylation sites in 77 proteins were identified.
14760718	5	20	theme	N-glycosylation	655:669	arg1	sites					671:675	N-glycosylation sites	655:675	N-glycosylation sites in complex mixtures	655:695	Here we demonstrate a procedure for mapping N-glycosylation sites in complex mixtures by reducing sample complexity and enriching glycoprotein content.
14760718	1	21	theme	last	89:92	arg1	years					98:102	the last few years	85:102	the last few years	85:102	In the last few years mass spectrometry has become the method of choice for characterization of post-translationally modified proteins.
14760718	5	22	from	sites	671:675	arg1	mixtures					688:695	complex mixtures	680:695	complex mixtures	680:695	Here we demonstrate a procedure for mapping N-glycosylation sites in complex mixtures by reducing sample complexity and enriching glycoprotein content.
14760718	1	23	theme	few	94:96	arg1	years					98:102	the last few years	85:102	the last few years	85:102	In the last few years mass spectrometry has become the method of choice for characterization of post-translationally modified proteins.
14760718	9	24	theme	concanavalin	1189:1200	arg1	lectins					1180:1186	two different lectins	1166:1186	two different lectins	1166:1186	Using two different lectins, concanavalin A and wheat germ agglutinin, this procedure was applied to human serum and a total of 86 N-glycosylation sites in 77 proteins were identified.
14760718	9	24	theme	concanavalin	1189:1200	arg1	A					1202:1202	concanavalin A	1189:1202	concanavalin A	1189:1202	Using two different lectins, concanavalin A and wheat germ agglutinin, this procedure was applied to human serum and a total of 86 N-glycosylation sites in 77 proteins were identified.
14760718	1	25	theme	modified	199:206	arg1	proteins					208:215	post-translationally modified proteins	178:215	post-translationally modified proteins	178:215	In the last few years mass spectrometry has become the method of choice for characterization of post-translationally modified proteins.
14760718	7	26	theme	Glycosylated	879:890	arg1	peptides					892:899	Glycosylated peptides	879:899	Glycosylated peptides	879:899	Glycosylated peptides are then selected from the digest mixture by a second lectin chromatography step.
14760718	5	27	theme	glycoprotein	741:752	arg1	content					754:760	glycoprotein content	741:760	glycoprotein content	741:760	Here we demonstrate a procedure for mapping N-glycosylation sites in complex mixtures by reducing sample complexity and enriching glycoprotein content.
14760718	3	28	gly	glycoproteins	461:473	arg1	glycoproteins					461:473	glycoproteins	461:473	glycoproteins	461:473	The detailed characterization of glycoproteins in complex biological samples is extremely challenging.
14760718	2	29	from	binary	266:271	arg1	sense					280:284	the sense that only one change can be associated with a given residue, many different oligosaccharides can be attached to a glycosylation site residue	276:425	the sense that only one change can be associated with a given residue, many different oligosaccharides can be attached to a glycosylation site residue	276:425	Whereas most protein chemical modifications are binary in the sense that only one change can be associated with a given residue, many different oligosaccharides can be attached to a glycosylation site residue.
14760718	1	30	theme	proteins	208:215	arg1	characterization					158:173	characterization	158:173	characterization of post-translationally modified proteins	158:215	In the last few years mass spectrometry has become the method of choice for characterization of post-translationally modified proteins.
14760718	0	31	theme	N-glycosylated	14:27	arg1	proteins					29:36	N-glycosylated proteins	14:36	N-glycosylated proteins	14:36	Screening for N-glycosylated proteins by liquid chromatography mass spectrometry.
14760718	4	32	theme	intermediary	591:602	arg1	level					604:608	an intermediary level	588:608	an intermediary level	588:608	However, information on N-glycosylation can be gained at an intermediary level.
14760718	9	33	theme	sites	1307:1311	arg1	total					1279:1283	a total	1277:1283	a total of 86 N-glycosylation sites in 77 proteins	1277:1326	Using two different lectins, concanavalin A and wheat germ agglutinin, this procedure was applied to human serum and a total of 86 N-glycosylation sites in 77 proteins were identified.
14760718	1	34	theme	mass	104:107	arg1	spectrometry					109:120	mass spectrometry	104:120	mass spectrometry	104:120	In the last few years mass spectrometry has become the method of choice for characterization of post-translationally modified proteins.
14760718	2	35	from	sense	280:284	arg1	binary					266:271	binary	266:271	binary	266:271	Whereas most protein chemical modifications are binary in the sense that only one change can be associated with a given residue, many different oligosaccharides can be attached to a glycosylation site residue.
14760718	3	36	theme	biological	486:495	arg1	samples					497:503	complex biological samples	478:503	complex biological samples	478:503	The detailed characterization of glycoproteins in complex biological samples is extremely challenging.
14760718	0	37	theme	liquid	41:46	arg1	spectrometry					68:79	liquid chromatography mass spectrometry	41:79	liquid chromatography mass spectrometry	41:79	Screening for N-glycosylated proteins by liquid chromatography mass spectrometry.
14760718	3	38	theme	glycoproteins	461:473	arg1	characterization					441:456	The detailed characterization	428:456	The detailed characterization of glycoproteins in complex biological samples	428:503	The detailed characterization of glycoproteins in complex biological samples is extremely challenging.
14760718	3	39	theme	detailed	432:439	arg1	characterization					441:456	The detailed characterization	428:456	The detailed characterization of glycoproteins in complex biological samples	428:503	The detailed characterization of glycoproteins in complex biological samples is extremely challenging.
14760718	2	40	theme	site	414:417	arg1	residue					419:425	a glycosylation site residue	398:425	a glycosylation site residue	398:425	Whereas most protein chemical modifications are binary in the sense that only one change can be associated with a given residue, many different oligosaccharides can be attached to a glycosylation site residue.
14760718	9	41	theme	77	1316:1317	arg1	proteins					1319:1326	77 proteins	1316:1326	77 proteins	1316:1326	Using two different lectins, concanavalin A and wheat germ agglutinin, this procedure was applied to human serum and a total of 86 N-glycosylation sites in 77 proteins were identified.
14760718	6	42	theme	chromatography	819:832	arg1	step					834:837	an initial lectin chromatography step	801:837	an initial lectin chromatography step	801:837	Glycosylated proteins are selected by an initial lectin chromatography step and digested with endoproteinase Lys-C.
14760718	2	43	theme	glycosylation	400:412	arg1	residue					419:425	a glycosylation site residue	398:425	a glycosylation site residue	398:425	Whereas most protein chemical modifications are binary in the sense that only one change can be associated with a given residue, many different oligosaccharides can be attached to a glycosylation site residue.
14760718	0	44	theme	mass	63:66	arg1	spectrometry					68:79	liquid chromatography mass spectrometry	41:79	liquid chromatography mass spectrometry	41:79	Screening for N-glycosylated proteins by liquid chromatography mass spectrometry.
14760718	5	45	theme	sample	709:714	arg1	complexity					716:725	sample complexity	709:725	sample complexity	709:725	Here we demonstrate a procedure for mapping N-glycosylation sites in complex mixtures by reducing sample complexity and enriching glycoprotein content.
14760718	2	46	theme	chemical	239:246	arg1	modifications					248:260	Whereas most protein chemical modifications	218:260	Whereas most protein chemical modifications	218:260	Whereas most protein chemical modifications are binary in the sense that only one change can be associated with a given residue, many different oligosaccharides can be attached to a glycosylation site residue.
14760718	6	47	theme	lectin	812:817	arg1	step					834:837	an initial lectin chromatography step	801:837	an initial lectin chromatography step	801:837	Glycosylated proteins are selected by an initial lectin chromatography step and digested with endoproteinase Lys-C.
14760718	0	48	theme	chromatography	48:61	arg1	spectrometry					68:79	liquid chromatography mass spectrometry	41:79	liquid chromatography mass spectrometry	41:79	Screening for N-glycosylated proteins by liquid chromatography mass spectrometry.
14760718	2	49	theme	most	226:229	arg1	modifications					248:260	Whereas most protein chemical modifications	218:260	Whereas most protein chemical modifications	218:260	Whereas most protein chemical modifications are binary in the sense that only one change can be associated with a given residue, many different oligosaccharides can be attached to a glycosylation site residue.
14760718	2	50	theme	protein	231:237	arg1	modifications					248:260	Whereas most protein chemical modifications	218:260	Whereas most protein chemical modifications	218:260	Whereas most protein chemical modifications are binary in the sense that only one change can be associated with a given residue, many different oligosaccharides can be attached to a glycosylation site residue.
14760718	6	51	theme	initial	804:810	arg1	step					834:837	an initial lectin chromatography step	801:837	an initial lectin chromatography step	801:837	Glycosylated proteins are selected by an initial lectin chromatography step and digested with endoproteinase Lys-C.
14760718	5	52	gly	glycoprotein	741:752	arg1	glycoprotein					741:752	glycoprotein content	741:760	glycoprotein content	741:760	Here we demonstrate a procedure for mapping N-glycosylation sites in complex mixtures by reducing sample complexity and enriching glycoprotein content.
14760718	8	53	theme	glycan	987:992	arg1	components					994:1003	The glycan components	983:1003	The glycan components	983:1003	The glycan components are removed with N-glycosidase F and the peptides digested with trypsin before analysis by on-line reversed-phase liquid chromatography mass spectrometry.
14760718	9	54	theme	N-glycosylation	1291:1305	arg1	sites					1307:1311	86 N-glycosylation sites	1288:1311	86 N-glycosylation sites in 77 proteins	1288:1326	Using two different lectins, concanavalin A and wheat germ agglutinin, this procedure was applied to human serum and a total of 86 N-glycosylation sites in 77 proteins were identified.
14760718	2	55	theme	Whereas	218:224	arg1	modifications					248:260	Whereas most protein chemical modifications	218:260	Whereas most protein chemical modifications	218:260	Whereas most protein chemical modifications are binary in the sense that only one change can be associated with a given residue, many different oligosaccharides can be attached to a glycosylation site residue.
14760718	2	56	theme	given	332:336	arg1	residue					338:344	a given residue	330:344	a given residue	330:344	Whereas most protein chemical modifications are binary in the sense that only one change can be associated with a given residue, many different oligosaccharides can be attached to a glycosylation site residue.
14760718	9	57	theme	germ	1214:1217	arg1	lectins					1180:1186	two different lectins	1166:1186	two different lectins	1166:1186	Using two different lectins, concanavalin A and wheat germ agglutinin, this procedure was applied to human serum and a total of 86 N-glycosylation sites in 77 proteins were identified.
14760718	9	57	theme	germ	1214:1217	arg1	agglutinin					1219:1228	wheat germ agglutinin	1208:1228	wheat germ agglutinin	1208:1228	Using two different lectins, concanavalin A and wheat germ agglutinin, this procedure was applied to human serum and a total of 86 N-glycosylation sites in 77 proteins were identified.
14760718	8	58	theme	N-glycosidase	1022:1034	arg1	F					1036:1036	N-glycosidase F	1022:1036	N-glycosidase F	1022:1036	The glycan components are removed with N-glycosidase F and the peptides digested with trypsin before analysis by on-line reversed-phase liquid chromatography mass spectrometry.
14760718	7	59	theme	chromatography	962:975	arg1	step					977:980	a second lectin chromatography step	946:980	a second lectin chromatography step	946:980	Glycosylated peptides are then selected from the digest mixture by a second lectin chromatography step.
14760718	9	60	from	total	1279:1283	arg1	proteins					1319:1326	77 proteins	1316:1326	77 proteins	1316:1326	Using two different lectins, concanavalin A and wheat germ agglutinin, this procedure was applied to human serum and a total of 86 N-glycosylation sites in 77 proteins were identified.
14760718	8	61	theme	mass	1141:1144	arg1	spectrometry					1146:1157	on-line reversed-phase liquid chromatography mass spectrometry	1096:1157	on-line reversed-phase liquid chromatography mass spectrometry	1096:1157	The glycan components are removed with N-glycosidase F and the peptides digested with trypsin before analysis by on-line reversed-phase liquid chromatography mass spectrometry.
14760718	2	62	attach	attached	386:393	arg2	oligosaccharides					362:377	many different oligosaccharides	347:377	many different oligosaccharides	347:377	Whereas most protein chemical modifications are binary in the sense that only one change can be associated with a given residue, many different oligosaccharides can be attached to a glycosylation site residue.
14760718	2	62	attach	attached	386:393	arg1	residue					419:425	a glycosylation site residue	398:425	a glycosylation site residue	398:425	Whereas most protein chemical modifications are binary in the sense that only one change can be associated with a given residue, many different oligosaccharides can be attached to a glycosylation site residue.
14760718	3	63	theme	complex	478:484	arg1	samples					497:503	complex biological samples	478:503	complex biological samples	478:503	The detailed characterization of glycoproteins in complex biological samples is extremely challenging.
14760718	9	64	gly	N-glycosylation	1291:1305	arg2	sites					1307:1311	86 N-glycosylation sites	1288:1311	86 N-glycosylation sites in 77 proteins	1288:1326	Using two different lectins, concanavalin A and wheat germ agglutinin, this procedure was applied to human serum and a total of 86 N-glycosylation sites in 77 proteins were identified.
14760718	9	64	gly	N-glycosylation	1291:1305	arg2	86					1288:1289	86	1288:1289	86	1288:1289	Using two different lectins, concanavalin A and wheat germ agglutinin, this procedure was applied to human serum and a total of 86 N-glycosylation sites in 77 proteins were identified.
14760718	8	65	theme	reversed-phase	1104:1117	arg1	chromatography					1126:1139	on-line reversed-phase liquid chromatography	1096:1139	on-line reversed-phase liquid chromatography mass spectrometry	1096:1157	The glycan components are removed with N-glycosidase F and the peptides digested with trypsin before analysis by on-line reversed-phase liquid chromatography mass spectrometry.
14760718	3	66	from	characterization	441:456	arg1	samples					497:503	complex biological samples	478:503	complex biological samples	478:503	The detailed characterization of glycoproteins in complex biological samples is extremely challenging.
14760718	7	67	theme	second	948:953	arg1	step					977:980	a second lectin chromatography step	946:980	a second lectin chromatography step	946:980	Glycosylated peptides are then selected from the digest mixture by a second lectin chromatography step.
16740002	0	0	theme	mass	85:88	arg1	spectrometry					90:101	mass spectrometry	85:101	mass spectrometry	85:101	Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry.
16740002	5	1	dep	focusing	813:820	arg1	isoelectric					801:811	isoelectric	801:811	isoelectric	801:811	Employing this method, coupled with in-solution isoelectric focusing separation as an additional means for pre-fractionation, we identified 84 formerly N-glycosylated peptides from 45 unique N-glycoproteins.
16740002	2	2	from	processes	430:438	arg1	body					447:450	the body	443:450	the body	443:450	Because changes in the physiological state of a person are reflected as changes in the glycoproteome composition, mapping the salivary glycoproteome will provide insights into various processes in the body.
16740002	5	3	theme	N-glycosylated	905:918	arg1	peptides					920:927	84 formerly N-glycosylated peptides	893:927	84 formerly N-glycosylated peptides from 45 unique N-glycoproteins	893:958	Employing this method, coupled with in-solution isoelectric focusing separation as an additional means for pre-fractionation, we identified 84 formerly N-glycosylated peptides from 45 unique N-glycoproteins.
16740002	1	4	theme	oral	233:236	arg1	cavity					238:243	the oral cavity	229:243	the oral cavity	229:243	Glycoproteins make up a major and important part of the salivary proteome and play a vital role in maintaining the health of the oral cavity.
16740002	7	5	from	sites	1067:1071	arg1	proteins					1106:1113	the proteins	1102:1113	the proteins	1102:1113	In addition, we identified 44 new sites of N-linked glycosylation on the proteins.
16740002	0	6	from	Identification	0:13	arg1	saliva					50:55	human saliva	44:55	human saliva	44:55	Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry.
16740002	0	7	link	N-linked	18:25	arg1	glycoproteins					27:39	N-linked glycoproteins	18:39	N-linked glycoproteins in human saliva	18:55	Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry.
16740002	0	8	gly	glycoprotein	60:71	arg1	glycoprotein					60:71	glycoprotein capture	60:79	glycoprotein capture	60:79	Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry.
16740002	1	9	theme	cavity	238:243	arg1	health					219:224	the health	215:224	the health of the oral cavity	215:243	Glycoproteins make up a major and important part of the salivary proteome and play a vital role in maintaining the health of the oral cavity.
16740002	5	10	gly	N-glycoproteins	944:958	arg1	N-glycoproteins					944:958	45 unique N-glycoproteins	934:958	45 unique N-glycoproteins	934:958	Employing this method, coupled with in-solution isoelectric focusing separation as an additional means for pre-fractionation, we identified 84 formerly N-glycosylated peptides from 45 unique N-glycoproteins.
16740002	4	11	gly	N-glycosylated	652:665	arg1	peptides					667:674	formerly N-glycosylated peptides	643:674	formerly N-glycosylated peptides	643:674	In this approach, glycoproteins were coupled onto a hydrazide resin, the proteins were then digested and formerly N-glycosylated peptides were selectively released with the enzyme PNGase F and analyzed by LC-MS/MS.
16740002	4	12	theme	PNGase	718:723	arg1	F					725:725	the enzyme PNGase F	707:725	the enzyme PNGase F	707:725	In this approach, glycoproteins were coupled onto a hydrazide resin, the proteins were then digested and formerly N-glycosylated peptides were selectively released with the enzyme PNGase F and analyzed by LC-MS/MS.
16740002	4	13	theme	enzyme	711:716	arg1	F					725:725	the enzyme PNGase F	707:725	the enzyme PNGase F	707:725	In this approach, glycoproteins were coupled onto a hydrazide resin, the proteins were then digested and formerly N-glycosylated peptides were selectively released with the enzyme PNGase F and analyzed by LC-MS/MS.
16740002	0	14	from	saliva	50:55	arg1	Identification					0:13	Identification	0:13	Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry.	0:102	Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry.
16740002	7	15	gly	glycosylation	1085:1097	arg2	sites					1067:1071	44 new sites	1060:1071	44 new sites of N-linked glycosylation on the proteins	1060:1113	In addition, we identified 44 new sites of N-linked glycosylation on the proteins.
16740002	7	15	gly	glycosylation	1085:1097	arg2	glycosylation					1085:1097	N-linked glycosylation	1076:1097	N-linked glycosylation	1076:1097	In addition, we identified 44 new sites of N-linked glycosylation on the proteins.
16740002	1	16	theme	salivary	160:167	arg1	proteome					169:176	the salivary proteome	156:176	the salivary proteome	156:176	Glycoproteins make up a major and important part of the salivary proteome and play a vital role in maintaining the health of the oral cavity.
16740002	4	17	gly	glycoproteins	556:568	arg1	glycoproteins					556:568	glycoproteins	556:568	glycoproteins	556:568	In this approach, glycoproteins were coupled onto a hydrazide resin, the proteins were then digested and formerly N-glycosylated peptides were selectively released with the enzyme PNGase F and analyzed by LC-MS/MS.
16740002	3	18	theme	release	522:528	arg1	method					530:535	the hydrazide coupling and release method	495:535	method	530:535	Salivary glycoproteins were identified by the hydrazide coupling and release method.
16740002	1	19	theme	proteome	169:176	arg1	part					148:151	a major and important part	126:151	a major and important part of the salivary proteome	126:176	Glycoproteins make up a major and important part of the salivary proteome and play a vital role in maintaining the health of the oral cavity.
16740002	5	20	theme	in-solution	789:799	arg1	separation					822:831	in-solution isoelectric focusing separation	789:831	in-solution isoelectric focusing separation	789:831	Employing this method, coupled with in-solution isoelectric focusing separation as an additional means for pre-fractionation, we identified 84 formerly N-glycosylated peptides from 45 unique N-glycoproteins.
16740002	7	21	theme	N-linked	1076:1083	arg1	glycosylation					1085:1097	N-linked glycosylation	1076:1097	N-linked glycosylation	1076:1097	In addition, we identified 44 new sites of N-linked glycosylation on the proteins.
16740002	2	22	from	changes	318:324	arg1	composition					347:357	the glycoproteome composition	329:357	the glycoproteome composition	329:357	Because changes in the physiological state of a person are reflected as changes in the glycoproteome composition, mapping the salivary glycoproteome will provide insights into various processes in the body.
16740002	3	23	theme	hydrazide	499:507	arg1	coupling					509:516	the hydrazide coupling and release method	495:535	coupling	509:516	Salivary glycoproteins were identified by the hydrazide coupling and release method.
16740002	4	24	theme	N-glycosylated	652:665	arg1	peptides					667:674	formerly N-glycosylated peptides	643:674	formerly N-glycosylated peptides	643:674	In this approach, glycoproteins were coupled onto a hydrazide resin, the proteins were then digested and formerly N-glycosylated peptides were selectively released with the enzyme PNGase F and analyzed by LC-MS/MS.
16740002	2	25	theme	various	422:428	arg1	processes					430:438	various processes	422:438	various processes in the body	422:450	Because changes in the physiological state of a person are reflected as changes in the glycoproteome composition, mapping the salivary glycoproteome will provide insights into various processes in the body.
16740002	7	26	theme	glycosylation	1085:1097	arg1	sites					1067:1071	44 new sites	1060:1071	44 new sites of N-linked glycosylation on the proteins	1060:1113	In addition, we identified 44 new sites of N-linked glycosylation on the proteins.
16740002	7	26	theme	glycosylation	1085:1097	arg1	glycosylation					1085:1097	N-linked glycosylation	1076:1097	N-linked glycosylation	1076:1097	In addition, we identified 44 new sites of N-linked glycosylation on the proteins.
16740002	0	27	theme	glycoproteins	27:39	arg1	Identification					0:13	Identification	0:13	Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry.	0:102	Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry.
16740002	5	28	theme	unique	937:942	arg1	N-glycoproteins					944:958	45 unique N-glycoproteins	934:958	45 unique N-glycoproteins	934:958	Employing this method, coupled with in-solution isoelectric focusing separation as an additional means for pre-fractionation, we identified 84 formerly N-glycosylated peptides from 45 unique N-glycoproteins.
16740002	3	29	gly	glycoproteins	462:474	arg1	glycoproteins					462:474	Salivary glycoproteins	453:474	Salivary glycoproteins	453:474	Salivary glycoproteins were identified by the hydrazide coupling and release method.
16740002	0	30	theme	N-linked	18:25	arg1	glycoproteins					27:39	N-linked glycoproteins	18:39	N-linked glycoproteins in human saliva	18:55	Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry.
16740002	2	31	theme	glycoproteome	333:345	arg1	composition					347:357	the glycoproteome composition	329:357	the glycoproteome composition	329:357	Because changes in the physiological state of a person are reflected as changes in the glycoproteome composition, mapping the salivary glycoproteome will provide insights into various processes in the body.
16740002	2	32	theme	physiological	269:281	arg1	state					283:287	the physiological state	265:287	the physiological state of a person	265:299	Because changes in the physiological state of a person are reflected as changes in the glycoproteome composition, mapping the salivary glycoproteome will provide insights into various processes in the body.
16740002	1	33	theme	vital	189:193	arg1	role					195:198	a vital role	187:198	a vital role	187:198	Glycoproteins make up a major and important part of the salivary proteome and play a vital role in maintaining the health of the oral cavity.
16740002	0	34	theme	human	44:48	arg1	saliva					50:55	human saliva	44:55	human saliva	44:55	Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry.
16740002	5	35	theme	additional	839:848	arg1	method					768:773	this method	763:773	this method	763:773	Employing this method, coupled with in-solution isoelectric focusing separation as an additional means for pre-fractionation, we identified 84 formerly N-glycosylated peptides from 45 unique N-glycoproteins.
16740002	5	35	theme	additional	839:848	arg1	means					850:854	an additional means	836:854	an additional means for pre-fractionation	836:876	Employing this method, coupled with in-solution isoelectric focusing separation as an additional means for pre-fractionation, we identified 84 formerly N-glycosylated peptides from 45 unique N-glycoproteins.
16740002	7	36	link	N-linked	1076:1083	arg1	glycosylation					1085:1097	N-linked glycosylation	1076:1097	N-linked glycosylation	1076:1097	In addition, we identified 44 new sites of N-linked glycosylation on the proteins.
16740002	7	37	theme	new	1063:1065	arg1	sites					1067:1071	44 new sites	1060:1071	44 new sites of N-linked glycosylation on the proteins	1060:1113	In addition, we identified 44 new sites of N-linked glycosylation on the proteins.
16740002	7	37	theme	new	1063:1065	arg1	glycosylation					1085:1097	N-linked glycosylation	1076:1097	N-linked glycosylation	1076:1097	In addition, we identified 44 new sites of N-linked glycosylation on the proteins.
16740002	5	38	theme	focusing	813:820	arg1	separation					822:831	in-solution isoelectric focusing separation	789:831	in-solution isoelectric focusing separation	789:831	Employing this method, coupled with in-solution isoelectric focusing separation as an additional means for pre-fractionation, we identified 84 formerly N-glycosylated peptides from 45 unique N-glycoproteins.
16740002	2	39	theme	salivary	372:379	arg1	glycoproteome					381:393	the salivary glycoproteome	368:393	mapping the salivary glycoproteome	360:393	Because changes in the physiological state of a person are reflected as changes in the glycoproteome composition, mapping the salivary glycoproteome will provide insights into various processes in the body.
16740002	0	40	gly	glycoproteins	27:39	arg1	glycoproteins					27:39	N-linked glycoproteins	18:39	N-linked glycoproteins in human saliva	18:55	Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry.
16740002	2	41	from	changes	254:260	arg1	state					283:287	the physiological state	265:287	the physiological state of a person	265:299	Because changes in the physiological state of a person are reflected as changes in the glycoproteome composition, mapping the salivary glycoproteome will provide insights into various processes in the body.
16740002	5	42	gly	N-glycosylated	905:918	arg1	peptides					920:927	84 formerly N-glycosylated peptides	893:927	84 formerly N-glycosylated peptides from 45 unique N-glycoproteins	893:958	Employing this method, coupled with in-solution isoelectric focusing separation as an additional means for pre-fractionation, we identified 84 formerly N-glycosylated peptides from 45 unique N-glycoproteins.
16740002	6	43	gly	glycoproteins	974:986	arg1	glycoproteins					974:986	16 glycoproteins	971:986	16 glycoproteins	971:986	Of these, 16 glycoproteins have not been reported previously in saliva.
16740002	1	44	theme	major	128:132	arg1	part					148:151	a major and important part	126:151	a major and important part of the salivary proteome	126:176	Glycoproteins make up a major and important part of the salivary proteome and play a vital role in maintaining the health of the oral cavity.
16740002	4	45	theme	hydrazide	590:598	arg1	resin					600:604	a hydrazide resin	588:604	a hydrazide resin	588:604	In this approach, glycoproteins were coupled onto a hydrazide resin, the proteins were then digested and formerly N-glycosylated peptides were selectively released with the enzyme PNGase F and analyzed by LC-MS/MS.
16740002	2	46	theme	person	294:299	arg1	state					283:287	the physiological state	265:287	the physiological state of a person	265:299	Because changes in the physiological state of a person are reflected as changes in the glycoproteome composition, mapping the salivary glycoproteome will provide insights into various processes in the body.
16740002	5	47	from	N-glycoproteins	944:958	arg1	peptides					920:927	84 formerly N-glycosylated peptides	893:927	84 formerly N-glycosylated peptides from 45 unique N-glycoproteins	893:958	Employing this method, coupled with in-solution isoelectric focusing separation as an additional means for pre-fractionation, we identified 84 formerly N-glycosylated peptides from 45 unique N-glycoproteins.
16740002	3	48	theme	Salivary	453:460	arg1	glycoproteins					462:474	Salivary glycoproteins	453:474	Salivary glycoproteins	453:474	Salivary glycoproteins were identified by the hydrazide coupling and release method.
16740002	1	49	theme	important	138:146	arg1	part					148:151	a major and important part	126:151	a major and important part of the salivary proteome	126:176	Glycoproteins make up a major and important part of the salivary proteome and play a vital role in maintaining the health of the oral cavity.
16740002	2	50	theme	mapping	360:366	arg1	glycoproteome					381:393	the salivary glycoproteome	368:393	mapping the salivary glycoproteome	360:393	Because changes in the physiological state of a person are reflected as changes in the glycoproteome composition, mapping the salivary glycoproteome will provide insights into various processes in the body.
16740002	0	51	theme	glycoprotein	60:71	arg1	capture					73:79	glycoprotein capture	60:79	glycoprotein capture	60:79	Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry.
16740002	0	52	from	glycoproteins	27:39	arg1	saliva					50:55	human saliva	44:55	human saliva	44:55	Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry.
24014025	2	0	theme	recombinant	475:485	arg1	LOXL2					487:491	recombinant LOXL2	475:491	recombinant LOXL2 differing in their subcellular localizations and catalytic competencies	475:563	In this study, we selected MCF-7 cells that stably express forms of recombinant LOXL2 differing in their subcellular localizations and catalytic competencies.
24014025	7	1	theme	factor	1248:1253	arg1	stabilization					1210:1222	the stabilization	1206:1222	the stabilization of Snail1 transcription factor at the protein level	1206:1274	The results indicate that nuclear associated LOXL2 contributes to the stabilization of Snail1 transcription factor at the protein level to induce EMT and promote invasion in vitro, through repression of E-cadherin, occludin, and estrogen receptor-α, and up-regulation of vimentin, fibronectin, and MT1-MMP.
24014025	6	2	theme	secreted	1115:1122	arg1	LOXL2					1124:1128	secreted LOXL2	1115:1128	secreted LOXL2	1115:1128	However, we found that expression of intracellular LOXL2 is more strongly associated with EMT and invasiveness than secreted LOXL2 in vitro.
24014025	4	3	from	Asn-644	807:813	arg1	N-glycosylated					777:790	N-glycosylated	777:790	N-glycosylated	777:790	We discovered that secreted LOXL2 (~100-kDa) is N-glycosylated at Asn-455 and Asn-644, whereas intracellular LOXL2 (~75-kDa) is nonglycosylated and N-terminally processed, and is primarily associated with the nucleus.
24014025	7	4	from	stabilization	1210:1222	arg1	level					1270:1274	the protein level	1258:1274	the protein level	1258:1274	The results indicate that nuclear associated LOXL2 contributes to the stabilization of Snail1 transcription factor at the protein level to induce EMT and promote invasion in vitro, through repression of E-cadherin, occludin, and estrogen receptor-α, and up-regulation of vimentin, fibronectin, and MT1-MMP.
24014025	0	5	theme	epithelial-to-mesenchymal	82:106	arg1	EMT					120:122	EMT	120:122	EMT	120:122	MCF-7 cells expressing nuclear associated lysyl oxidase-like 2 (LOXL2) exhibit an epithelial-to-mesenchymal transition (EMT) phenotype and are highly invasive in vitro.
24014025	0	5	theme	epithelial-to-mesenchymal	82:106	arg1	transition					108:117	epithelial-to-mesenchymal transition	82:117	an epithelial-to-mesenchymal transition (EMT) phenotype	79:133	MCF-7 cells expressing nuclear associated lysyl oxidase-like 2 (LOXL2) exhibit an epithelial-to-mesenchymal transition (EMT) phenotype and are highly invasive in vitro.
24014025	7	6	theme	receptor-α	1378:1387	arg1	repression					1329:1338	repression	1329:1338	repression of E-cadherin, occludin, and estrogen receptor-α, and up-regulation of vimentin, fibronectin, and MT1-MMP	1329:1444	The results indicate that nuclear associated LOXL2 contributes to the stabilization of Snail1 transcription factor at the protein level to induce EMT and promote invasion in vitro, through repression of E-cadherin, occludin, and estrogen receptor-α, and up-regulation of vimentin, fibronectin, and MT1-MMP.
24014025	2	7	theme	subcellular	512:522	arg1	localizations					524:536	their subcellular localizations	506:536	their subcellular localizations	506:536	In this study, we selected MCF-7 cells that stably express forms of recombinant LOXL2 differing in their subcellular localizations and catalytic competencies.
24014025	4	8	from	Asn-455	795:801	arg1	N-glycosylated					777:790	N-glycosylated	777:790	N-glycosylated	777:790	We discovered that secreted LOXL2 (~100-kDa) is N-glycosylated at Asn-455 and Asn-644, whereas intracellular LOXL2 (~75-kDa) is nonglycosylated and N-terminally processed, and is primarily associated with the nucleus.
24014025	7	9	theme	fibronectin	1421:1431	arg1	E-cadherin					1343:1352	E-cadherin	1343:1352	E-cadherin	1343:1352	The results indicate that nuclear associated LOXL2 contributes to the stabilization of Snail1 transcription factor at the protein level to induce EMT and promote invasion in vitro, through repression of E-cadherin, occludin, and estrogen receptor-α, and up-regulation of vimentin, fibronectin, and MT1-MMP.
24014025	7	9	theme	fibronectin	1421:1431	arg1	receptor-α					1378:1387	estrogen receptor-α	1369:1387	estrogen receptor-α	1369:1387	The results indicate that nuclear associated LOXL2 contributes to the stabilization of Snail1 transcription factor at the protein level to induce EMT and promote invasion in vitro, through repression of E-cadherin, occludin, and estrogen receptor-α, and up-regulation of vimentin, fibronectin, and MT1-MMP.
24014025	7	9	theme	fibronectin	1421:1431	arg1	up-regulation					1394:1406	up-regulation	1394:1406	up-regulation of vimentin, fibronectin, and MT1-MMP	1394:1444	The results indicate that nuclear associated LOXL2 contributes to the stabilization of Snail1 transcription factor at the protein level to induce EMT and promote invasion in vitro, through repression of E-cadherin, occludin, and estrogen receptor-α, and up-regulation of vimentin, fibronectin, and MT1-MMP.
24014025	7	9	theme	fibronectin	1421:1431	arg1	occludin					1355:1362	occludin	1355:1362	occludin	1355:1362	The results indicate that nuclear associated LOXL2 contributes to the stabilization of Snail1 transcription factor at the protein level to induce EMT and promote invasion in vitro, through repression of E-cadherin, occludin, and estrogen receptor-α, and up-regulation of vimentin, fibronectin, and MT1-MMP.
24014025	4	10	dep	N-glycosylated	777:790	arg1	whereas					816:822	whereas	816:822	whereas	816:822	We discovered that secreted LOXL2 (~100-kDa) is N-glycosylated at Asn-455 and Asn-644, whereas intracellular LOXL2 (~75-kDa) is nonglycosylated and N-terminally processed, and is primarily associated with the nucleus.
24014025	0	11	theme	transition	108:117	arg1	phenotype					125:133	an epithelial-to-mesenchymal transition (EMT) phenotype	79:133	an epithelial-to-mesenchymal transition (EMT) phenotype	79:133	MCF-7 cells expressing nuclear associated lysyl oxidase-like 2 (LOXL2) exhibit an epithelial-to-mesenchymal transition (EMT) phenotype and are highly invasive in vitro.
24014025	0	12	theme	MCF-7	0:4	arg1	cells					6:10	MCF-7 cells	0:10	MCF-7 cells expressing nuclear associated lysyl oxidase-like 2 (LOXL2)	0:69	MCF-7 cells expressing nuclear associated lysyl oxidase-like 2 (LOXL2) exhibit an epithelial-to-mesenchymal transition (EMT) phenotype and are highly invasive in vitro.
24014025	7	13	theme	occludin	1355:1362	arg1	repression					1329:1338	repression	1329:1338	repression of E-cadherin, occludin, and estrogen receptor-α, and up-regulation of vimentin, fibronectin, and MT1-MMP	1329:1444	The results indicate that nuclear associated LOXL2 contributes to the stabilization of Snail1 transcription factor at the protein level to induce EMT and promote invasion in vitro, through repression of E-cadherin, occludin, and estrogen receptor-α, and up-regulation of vimentin, fibronectin, and MT1-MMP.
24014025	7	14	from	level	1270:1274	arg1	stabilization					1210:1222	the stabilization	1206:1222	the stabilization of Snail1 transcription factor at the protein level	1206:1274	The results indicate that nuclear associated LOXL2 contributes to the stabilization of Snail1 transcription factor at the protein level to induce EMT and promote invasion in vitro, through repression of E-cadherin, occludin, and estrogen receptor-α, and up-regulation of vimentin, fibronectin, and MT1-MMP.
24014025	7	14	from	level	1270:1274	arg1	factor					1248:1253	Snail1 transcription factor	1227:1253	Snail1 transcription factor at the protein level	1227:1274	The results indicate that nuclear associated LOXL2 contributes to the stabilization of Snail1 transcription factor at the protein level to induce EMT and promote invasion in vitro, through repression of E-cadherin, occludin, and estrogen receptor-α, and up-regulation of vimentin, fibronectin, and MT1-MMP.
24014025	5	15	theme	LOXL2	961:965	arg1	forms					952:956	Both forms	947:956	Both forms of LOXL2	947:965	Both forms of LOXL2 can oxidize lysine in solution.
24014025	2	16	theme	MCF-7	434:438	arg1	cells					440:444	MCF-7 cells	434:444	MCF-7 cells that stably express forms of recombinant LOXL2 differing in their subcellular localizations and catalytic competencies	434:563	In this study, we selected MCF-7 cells that stably express forms of recombinant LOXL2 differing in their subcellular localizations and catalytic competencies.
24014025	7	17	theme	E-cadherin	1343:1352	arg1	repression					1329:1338	repression	1329:1338	repression of E-cadherin, occludin, and estrogen receptor-α, and up-regulation of vimentin, fibronectin, and MT1-MMP	1329:1444	The results indicate that nuclear associated LOXL2 contributes to the stabilization of Snail1 transcription factor at the protein level to induce EMT and promote invasion in vitro, through repression of E-cadherin, occludin, and estrogen receptor-α, and up-regulation of vimentin, fibronectin, and MT1-MMP.
24014025	0	18	theme	nuclear	23:29	arg1	lysyl					42:46	nuclear associated lysyl oxidase-like 2	23:61	nuclear associated lysyl oxidase-like 2 (LOXL2)	23:69	MCF-7 cells expressing nuclear associated lysyl oxidase-like 2 (LOXL2) exhibit an epithelial-to-mesenchymal transition (EMT) phenotype and are highly invasive in vitro.
24014025	0	18	theme	nuclear	23:29	arg1	LOXL2					64:68	LOXL2	64:68	LOXL2	64:68	MCF-7 cells expressing nuclear associated lysyl oxidase-like 2 (LOXL2) exhibit an epithelial-to-mesenchymal transition (EMT) phenotype and are highly invasive in vitro.
24014025	7	19	theme	vimentin	1411:1418	arg1	E-cadherin					1343:1352	E-cadherin	1343:1352	E-cadherin	1343:1352	The results indicate that nuclear associated LOXL2 contributes to the stabilization of Snail1 transcription factor at the protein level to induce EMT and promote invasion in vitro, through repression of E-cadherin, occludin, and estrogen receptor-α, and up-regulation of vimentin, fibronectin, and MT1-MMP.
24014025	7	19	theme	vimentin	1411:1418	arg1	receptor-α					1378:1387	estrogen receptor-α	1369:1387	estrogen receptor-α	1369:1387	The results indicate that nuclear associated LOXL2 contributes to the stabilization of Snail1 transcription factor at the protein level to induce EMT and promote invasion in vitro, through repression of E-cadherin, occludin, and estrogen receptor-α, and up-regulation of vimentin, fibronectin, and MT1-MMP.
24014025	7	19	theme	vimentin	1411:1418	arg1	up-regulation					1394:1406	up-regulation	1394:1406	up-regulation of vimentin, fibronectin, and MT1-MMP	1394:1444	The results indicate that nuclear associated LOXL2 contributes to the stabilization of Snail1 transcription factor at the protein level to induce EMT and promote invasion in vitro, through repression of E-cadherin, occludin, and estrogen receptor-α, and up-regulation of vimentin, fibronectin, and MT1-MMP.
24014025	7	19	theme	vimentin	1411:1418	arg1	occludin					1355:1362	occludin	1355:1362	occludin	1355:1362	The results indicate that nuclear associated LOXL2 contributes to the stabilization of Snail1 transcription factor at the protein level to induce EMT and promote invasion in vitro, through repression of E-cadherin, occludin, and estrogen receptor-α, and up-regulation of vimentin, fibronectin, and MT1-MMP.
24014025	7	20	theme	up-regulation	1394:1406	arg1	repression					1329:1338	repression	1329:1338	repression of E-cadherin, occludin, and estrogen receptor-α, and up-regulation of vimentin, fibronectin, and MT1-MMP	1329:1444	The results indicate that nuclear associated LOXL2 contributes to the stabilization of Snail1 transcription factor at the protein level to induce EMT and promote invasion in vitro, through repression of E-cadherin, occludin, and estrogen receptor-α, and up-regulation of vimentin, fibronectin, and MT1-MMP.
24014025	4	21	theme	intracellular	824:836	arg1	~75-kDa					845:851	~75-kDa	845:851	~75-kDa	845:851	We discovered that secreted LOXL2 (~100-kDa) is N-glycosylated at Asn-455 and Asn-644, whereas intracellular LOXL2 (~75-kDa) is nonglycosylated and N-terminally processed, and is primarily associated with the nucleus.
24014025	4	21	theme	intracellular	824:836	arg1	LOXL2					838:842	intracellular LOXL2	824:842	intracellular LOXL2 (~75-kDa)	824:852	We discovered that secreted LOXL2 (~100-kDa) is N-glycosylated at Asn-455 and Asn-644, whereas intracellular LOXL2 (~75-kDa) is nonglycosylated and N-terminally processed, and is primarily associated with the nucleus.
24014025	1	22	theme	breast	386:391	arg1	cells					400:404	breast cancer cells	386:404	breast cancer cells	386:404	LOXL2 is a copper- and lysine tyrosylquinone-dependent amine oxidase that has been proposed to function both extracellularly and intracellularly to activate oncogenic signaling pathways leading to EMT and invasion of breast cancer cells.
24014025	1	23	theme	copper-	180:186	arg1	oxidase					230:236	a copper- and lysine tyrosylquinone-dependent amine oxidase	178:236	a copper- and lysine tyrosylquinone-dependent amine oxidase that has been proposed to function both extracellularly and intracellularly to activate oncogenic signaling pathways leading to EMT and invasion of breast cancer cells	178:404	LOXL2 is a copper- and lysine tyrosylquinone-dependent amine oxidase that has been proposed to function both extracellularly and intracellularly to activate oncogenic signaling pathways leading to EMT and invasion of breast cancer cells.
24014025	1	23	theme	copper-	180:186	arg1	LOXL2					169:173	LOXL2	169:173	LOXL2	169:173	LOXL2 is a copper- and lysine tyrosylquinone-dependent amine oxidase that has been proposed to function both extracellularly and intracellularly to activate oncogenic signaling pathways leading to EMT and invasion of breast cancer cells.
24014025	7	24	theme	nuclear	1166:1172	arg1	LOXL2					1185:1189	nuclear associated LOXL2	1166:1189	nuclear associated LOXL2	1166:1189	The results indicate that nuclear associated LOXL2 contributes to the stabilization of Snail1 transcription factor at the protein level to induce EMT and promote invasion in vitro, through repression of E-cadherin, occludin, and estrogen receptor-α, and up-regulation of vimentin, fibronectin, and MT1-MMP.
24014025	2	25	theme	catalytic	542:550	arg1	competencies					552:563	catalytic competencies	542:563	catalytic competencies	542:563	In this study, we selected MCF-7 cells that stably express forms of recombinant LOXL2 differing in their subcellular localizations and catalytic competencies.
24014025	1	26	theme	cancer	393:398	arg1	cells					400:404	breast cancer cells	386:404	breast cancer cells	386:404	LOXL2 is a copper- and lysine tyrosylquinone-dependent amine oxidase that has been proposed to function both extracellularly and intracellularly to activate oncogenic signaling pathways leading to EMT and invasion of breast cancer cells.
24014025	3	27	theme	molecular	597:605	arg1	functions					607:615	the molecular functions	593:615	the molecular functions of intracellular and extracellular LOXL2s	593:657	This enabled us to dissect the molecular functions of intracellular and extracellular LOXL2s and examine their contributions to breast cancer metastasis/invasion.
24014025	0	28	theme	associated	31:40	arg1	lysyl					42:46	nuclear associated lysyl oxidase-like 2	23:61	nuclear associated lysyl oxidase-like 2 (LOXL2)	23:69	MCF-7 cells expressing nuclear associated lysyl oxidase-like 2 (LOXL2) exhibit an epithelial-to-mesenchymal transition (EMT) phenotype and are highly invasive in vitro.
24014025	0	28	theme	associated	31:40	arg1	LOXL2					64:68	LOXL2	64:68	LOXL2	64:68	MCF-7 cells expressing nuclear associated lysyl oxidase-like 2 (LOXL2) exhibit an epithelial-to-mesenchymal transition (EMT) phenotype and are highly invasive in vitro.
24014025	7	29	theme	associated	1174:1183	arg1	LOXL2					1185:1189	nuclear associated LOXL2	1166:1189	nuclear associated LOXL2	1166:1189	The results indicate that nuclear associated LOXL2 contributes to the stabilization of Snail1 transcription factor at the protein level to induce EMT and promote invasion in vitro, through repression of E-cadherin, occludin, and estrogen receptor-α, and up-regulation of vimentin, fibronectin, and MT1-MMP.
24014025	3	30	theme	LOXL2s	652:657	arg1	functions					607:615	the molecular functions	593:615	the molecular functions of intracellular and extracellular LOXL2s	593:657	This enabled us to dissect the molecular functions of intracellular and extracellular LOXL2s and examine their contributions to breast cancer metastasis/invasion.
24014025	4	31	gly	N-glycosylated	777:790	arg2	Asn-644					807:813	Asn-644	807:813	Asn-644	807:813	We discovered that secreted LOXL2 (~100-kDa) is N-glycosylated at Asn-455 and Asn-644, whereas intracellular LOXL2 (~75-kDa) is nonglycosylated and N-terminally processed, and is primarily associated with the nucleus.
24014025	4	31	gly	N-glycosylated	777:790	arg2	Asn-455					795:801	Asn-455	795:801	Asn-455	795:801	We discovered that secreted LOXL2 (~100-kDa) is N-glycosylated at Asn-455 and Asn-644, whereas intracellular LOXL2 (~75-kDa) is nonglycosylated and N-terminally processed, and is primarily associated with the nucleus.
24014025	4	31	gly	N-glycosylated	777:790	arg1	LOXL2					757:761	secreted LOXL2	748:761	secreted LOXL2 (~100-kDa)	748:772	We discovered that secreted LOXL2 (~100-kDa) is N-glycosylated at Asn-455 and Asn-644, whereas intracellular LOXL2 (~75-kDa) is nonglycosylated and N-terminally processed, and is primarily associated with the nucleus.
24014025	4	31	gly	N-glycosylated	777:790	arg1	~100-kDa					764:771	~100-kDa	764:771	~100-kDa	764:771	We discovered that secreted LOXL2 (~100-kDa) is N-glycosylated at Asn-455 and Asn-644, whereas intracellular LOXL2 (~75-kDa) is nonglycosylated and N-terminally processed, and is primarily associated with the nucleus.
24014025	7	32	theme	Snail1	1227:1232	arg1	factor					1248:1253	Snail1 transcription factor	1227:1253	Snail1 transcription factor at the protein level	1227:1274	The results indicate that nuclear associated LOXL2 contributes to the stabilization of Snail1 transcription factor at the protein level to induce EMT and promote invasion in vitro, through repression of E-cadherin, occludin, and estrogen receptor-α, and up-regulation of vimentin, fibronectin, and MT1-MMP.
24014025	7	33	theme	protein	1262:1268	arg1	level					1270:1274	the protein level	1258:1274	the protein level	1258:1274	The results indicate that nuclear associated LOXL2 contributes to the stabilization of Snail1 transcription factor at the protein level to induce EMT and promote invasion in vitro, through repression of E-cadherin, occludin, and estrogen receptor-α, and up-regulation of vimentin, fibronectin, and MT1-MMP.
24014025	4	34	theme	secreted	748:755	arg1	~100-kDa					764:771	~100-kDa	764:771	~100-kDa	764:771	We discovered that secreted LOXL2 (~100-kDa) is N-glycosylated at Asn-455 and Asn-644, whereas intracellular LOXL2 (~75-kDa) is nonglycosylated and N-terminally processed, and is primarily associated with the nucleus.
24014025	4	34	theme	secreted	748:755	arg1	LOXL2					757:761	secreted LOXL2	748:761	secreted LOXL2 (~100-kDa)	748:772	We discovered that secreted LOXL2 (~100-kDa) is N-glycosylated at Asn-455 and Asn-644, whereas intracellular LOXL2 (~75-kDa) is nonglycosylated and N-terminally processed, and is primarily associated with the nucleus.
24014025	0	35	theme	oxidase-like	48:59	arg1	lysyl					42:46	nuclear associated lysyl oxidase-like 2	23:61	nuclear associated lysyl oxidase-like 2 (LOXL2)	23:69	MCF-7 cells expressing nuclear associated lysyl oxidase-like 2 (LOXL2) exhibit an epithelial-to-mesenchymal transition (EMT) phenotype and are highly invasive in vitro.
24014025	0	35	theme	oxidase-like	48:59	arg1	LOXL2					64:68	LOXL2	64:68	LOXL2	64:68	MCF-7 cells expressing nuclear associated lysyl oxidase-like 2 (LOXL2) exhibit an epithelial-to-mesenchymal transition (EMT) phenotype and are highly invasive in vitro.
24014025	3	36	theme	breast	694:699	arg1	metastasis/invasion					708:726	breast cancer metastasis/invasion	694:726	breast cancer metastasis/invasion	694:726	This enabled us to dissect the molecular functions of intracellular and extracellular LOXL2s and examine their contributions to breast cancer metastasis/invasion.
24014025	1	37	theme	cells	400:404	arg1	invasion					374:381	invasion	374:381	invasion	374:381	LOXL2 is a copper- and lysine tyrosylquinone-dependent amine oxidase that has been proposed to function both extracellularly and intracellularly to activate oncogenic signaling pathways leading to EMT and invasion of breast cancer cells.
24014025	1	37	theme	cells	400:404	arg1	EMT					366:368	EMT	366:368	EMT	366:368	LOXL2 is a copper- and lysine tyrosylquinone-dependent amine oxidase that has been proposed to function both extracellularly and intracellularly to activate oncogenic signaling pathways leading to EMT and invasion of breast cancer cells.
24014025	1	38	theme	oncogenic	326:334	arg1	pathways					346:353	oncogenic signaling pathways	326:353	oncogenic signaling pathways leading to EMT and invasion of breast cancer cells	326:404	LOXL2 is a copper- and lysine tyrosylquinone-dependent amine oxidase that has been proposed to function both extracellularly and intracellularly to activate oncogenic signaling pathways leading to EMT and invasion of breast cancer cells.
24014025	3	39	theme	cancer	701:706	arg1	metastasis/invasion					708:726	breast cancer metastasis/invasion	694:726	breast cancer metastasis/invasion	694:726	This enabled us to dissect the molecular functions of intracellular and extracellular LOXL2s and examine their contributions to breast cancer metastasis/invasion.
24014025	7	40	theme	estrogen	1369:1376	arg1	receptor-α					1378:1387	estrogen receptor-α	1369:1387	estrogen receptor-α	1369:1387	The results indicate that nuclear associated LOXL2 contributes to the stabilization of Snail1 transcription factor at the protein level to induce EMT and promote invasion in vitro, through repression of E-cadherin, occludin, and estrogen receptor-α, and up-regulation of vimentin, fibronectin, and MT1-MMP.
24014025	6	41	theme	intracellular	1036:1048	arg1	LOXL2					1050:1054	intracellular LOXL2	1036:1054	intracellular LOXL2	1036:1054	However, we found that expression of intracellular LOXL2 is more strongly associated with EMT and invasiveness than secreted LOXL2 in vitro.
24014025	1	42	theme	tyrosylquinone-dependent	199:222	arg1	oxidase					230:236	a copper- and lysine tyrosylquinone-dependent amine oxidase	178:236	a copper- and lysine tyrosylquinone-dependent amine oxidase that has been proposed to function both extracellularly and intracellularly to activate oncogenic signaling pathways leading to EMT and invasion of breast cancer cells	178:404	LOXL2 is a copper- and lysine tyrosylquinone-dependent amine oxidase that has been proposed to function both extracellularly and intracellularly to activate oncogenic signaling pathways leading to EMT and invasion of breast cancer cells.
24014025	1	42	theme	tyrosylquinone-dependent	199:222	arg1	LOXL2					169:173	LOXL2	169:173	LOXL2	169:173	LOXL2 is a copper- and lysine tyrosylquinone-dependent amine oxidase that has been proposed to function both extracellularly and intracellularly to activate oncogenic signaling pathways leading to EMT and invasion of breast cancer cells.
24014025	7	43	theme	MT1-MMP	1438:1444	arg1	E-cadherin					1343:1352	E-cadherin	1343:1352	E-cadherin	1343:1352	The results indicate that nuclear associated LOXL2 contributes to the stabilization of Snail1 transcription factor at the protein level to induce EMT and promote invasion in vitro, through repression of E-cadherin, occludin, and estrogen receptor-α, and up-regulation of vimentin, fibronectin, and MT1-MMP.
24014025	7	43	theme	MT1-MMP	1438:1444	arg1	receptor-α					1378:1387	estrogen receptor-α	1369:1387	estrogen receptor-α	1369:1387	The results indicate that nuclear associated LOXL2 contributes to the stabilization of Snail1 transcription factor at the protein level to induce EMT and promote invasion in vitro, through repression of E-cadherin, occludin, and estrogen receptor-α, and up-regulation of vimentin, fibronectin, and MT1-MMP.
24014025	7	43	theme	MT1-MMP	1438:1444	arg1	up-regulation					1394:1406	up-regulation	1394:1406	up-regulation of vimentin, fibronectin, and MT1-MMP	1394:1444	The results indicate that nuclear associated LOXL2 contributes to the stabilization of Snail1 transcription factor at the protein level to induce EMT and promote invasion in vitro, through repression of E-cadherin, occludin, and estrogen receptor-α, and up-regulation of vimentin, fibronectin, and MT1-MMP.
24014025	7	43	theme	MT1-MMP	1438:1444	arg1	occludin					1355:1362	occludin	1355:1362	occludin	1355:1362	The results indicate that nuclear associated LOXL2 contributes to the stabilization of Snail1 transcription factor at the protein level to induce EMT and promote invasion in vitro, through repression of E-cadherin, occludin, and estrogen receptor-α, and up-regulation of vimentin, fibronectin, and MT1-MMP.
24014025	3	44	theme	extracellular	638:650	arg1	LOXL2s					652:657	intracellular and extracellular LOXL2s	620:657	intracellular and extracellular LOXL2s	620:657	This enabled us to dissect the molecular functions of intracellular and extracellular LOXL2s and examine their contributions to breast cancer metastasis/invasion.
24014025	1	45	theme	amine	224:228	arg1	oxidase					230:236	a copper- and lysine tyrosylquinone-dependent amine oxidase	178:236	a copper- and lysine tyrosylquinone-dependent amine oxidase that has been proposed to function both extracellularly and intracellularly to activate oncogenic signaling pathways leading to EMT and invasion of breast cancer cells	178:404	LOXL2 is a copper- and lysine tyrosylquinone-dependent amine oxidase that has been proposed to function both extracellularly and intracellularly to activate oncogenic signaling pathways leading to EMT and invasion of breast cancer cells.
24014025	1	45	theme	amine	224:228	arg1	LOXL2					169:173	LOXL2	169:173	LOXL2	169:173	LOXL2 is a copper- and lysine tyrosylquinone-dependent amine oxidase that has been proposed to function both extracellularly and intracellularly to activate oncogenic signaling pathways leading to EMT and invasion of breast cancer cells.
24014025	2	46	theme	LOXL2	487:491	arg1	forms					466:470	forms	466:470	forms of recombinant LOXL2 differing in their subcellular localizations and catalytic competencies	466:563	In this study, we selected MCF-7 cells that stably express forms of recombinant LOXL2 differing in their subcellular localizations and catalytic competencies.
24014025	1	47	theme	signaling	336:344	arg1	pathways					346:353	oncogenic signaling pathways	326:353	oncogenic signaling pathways leading to EMT and invasion of breast cancer cells	326:404	LOXL2 is a copper- and lysine tyrosylquinone-dependent amine oxidase that has been proposed to function both extracellularly and intracellularly to activate oncogenic signaling pathways leading to EMT and invasion of breast cancer cells.
24014025	3	48	theme	intracellular	620:632	arg1	LOXL2s					652:657	intracellular and extracellular LOXL2s	620:657	intracellular and extracellular LOXL2s	620:657	This enabled us to dissect the molecular functions of intracellular and extracellular LOXL2s and examine their contributions to breast cancer metastasis/invasion.
24014025	6	49	theme	LOXL2	1050:1054	arg1	expression					1022:1031	expression	1022:1031	expression of intracellular LOXL2	1022:1054	However, we found that expression of intracellular LOXL2 is more strongly associated with EMT and invasiveness than secreted LOXL2 in vitro.
24014025	7	50	theme	transcription	1234:1246	arg1	factor					1248:1253	Snail1 transcription factor	1227:1253	Snail1 transcription factor at the protein level	1227:1274	The results indicate that nuclear associated LOXL2 contributes to the stabilization of Snail1 transcription factor at the protein level to induce EMT and promote invasion in vitro, through repression of E-cadherin, occludin, and estrogen receptor-α, and up-regulation of vimentin, fibronectin, and MT1-MMP.
23677006	7	0	theme	mammalian	1108:1116	arg1	cells					1118:1122	mammalian cells	1108:1122	mammalian cells	1108:1122	To test this hypothesis, we expressed both wild-type FX and FX containing this mutation in mammalian cells and following the purification of the zymogens to homogeneity characterized their properties in both purified and plasma-based assay systems.
23677006	8	1	theme	substrate	1452:1460	arg1	concentration					1431:1443	physiological concentration	1417:1443	physiological concentration of the substrate	1417:1460	Analysis of the results suggests that Thr211 to Pro substitution renders the FX mutant a poor substrate for both physiological activators, however, at physiological concentration of the substrate, the clotting defect manifest itself only in the intrinsic pathway, thus explaining the bleeding phenotype for the patient carrying this mutation.
23677006	1	2	theme	Factor	138:143	arg1	zymogen					189:195	a vitamin K-dependent coagulation zymogen	155:195	a vitamin K-dependent coagulation zymogen	155:195	Factor X (FX) is a vitamin K-dependent coagulation zymogen, which upon activation to factor Xa assembles into the prothrombinase complex to activate prothrombin to thrombin.
23677006	1	2	theme	Factor	138:143	arg1	FX					148:149	FX	148:149	FX	148:149	Factor X (FX) is a vitamin K-dependent coagulation zymogen, which upon activation to factor Xa assembles into the prothrombinase complex to activate prothrombin to thrombin.
23677006	1	2	theme	Factor	138:143	arg1	X					145:145	Factor X	138:145	Factor X (FX)	138:150	Factor X (FX) is a vitamin K-dependent coagulation zymogen, which upon activation to factor Xa assembles into the prothrombinase complex to activate prothrombin to thrombin.
23677006	5	3	from	site	767:770	arg1	peptide					819:825	the activation peptide	804:825	the activation peptide of FX	804:831	Thr211 is the site of an O-linked glycosylation in the activation peptide of FX.
23677006	7	4	theme	zymogens	1162:1169	arg1	purification					1142:1153	the purification	1138:1153	the purification of the zymogens to homogeneity	1138:1184	To test this hypothesis, we expressed both wild-type FX and FX containing this mutation in mammalian cells and following the purification of the zymogens to homogeneity characterized their properties in both purified and plasma-based assay systems.
23677006	7	5	theme	wild-type	1060:1068	arg1	FX					1070:1071	wild-type FX	1060:1071	wild-type FX	1060:1071	To test this hypothesis, we expressed both wild-type FX and FX containing this mutation in mammalian cells and following the purification of the zymogens to homogeneity characterized their properties in both purified and plasma-based assay systems.
23677006	7	6	contain	containing	1080:1089	arg1	FX					1077:1078	FX	1077:1078	FX containing this mutation	1077:1103	To test this hypothesis, we expressed both wild-type FX and FX containing this mutation in mammalian cells and following the purification of the zymogens to homogeneity characterized their properties in both purified and plasma-based assay systems.
23677006	7	6	contain	containing	1080:1089	arg2	mutation					1096:1103	this mutation	1091:1103	this mutation	1091:1103	To test this hypothesis, we expressed both wild-type FX and FX containing this mutation in mammalian cells and following the purification of the zymogens to homogeneity characterized their properties in both purified and plasma-based assay systems.
23677006	4	7	theme	missense	654:661	arg1	mutation					663:670	a novel homozygous missense mutation	635:670	a novel homozygous missense mutation that results in substitution of Thr211 with Pro in the activation peptide of FX	635:750	Exome sequencing revealed that the patient carries a novel homozygous missense mutation that results in substitution of Thr211 with Pro in the activation peptide of FX.
23677006	6	8	theme	intrinsic	947:955	arg1	Xase					957:960	intrinsic Xase	947:960	intrinsic Xase	947:960	We postulated that the lack of this post-translational modification specifically impacts the activation of FX by intrinsic Xase, thereby impairing thrombin generation in the subject.
23677006	0	9	theme	patient	81:87	arg1	peptide					59:65	the factor X activation peptide	35:65	the factor X activation peptide of a bleeding patient	35:87	The missense Thr211Pro mutation in the factor X activation peptide of a bleeding patient causes molecular defect in the clotting cascade.
23677006	8	10	dep	defect	1476:1481	arg1	manifest					1483:1490	manifest	1483:1490	manifest	1483:1490	Analysis of the results suggests that Thr211 to Pro substitution renders the FX mutant a poor substrate for both physiological activators, however, at physiological concentration of the substrate, the clotting defect manifest itself only in the intrinsic pathway, thus explaining the bleeding phenotype for the patient carrying this mutation.
23677006	3	11	theme	moderate	499:506	arg1	deficiency					511:520	moderate FX deficiency	499:520	moderate FX deficiency	499:520	In this study, we identified a bleeding patient with moderate FX deficiency who exhibits a clotting defect only in the intrinsic pathway.
23677006	1	12	theme	factor	223:228	arg1	Xa					230:231	factor Xa	223:231	factor Xa	223:231	Factor X (FX) is a vitamin K-dependent coagulation zymogen, which upon activation to factor Xa assembles into the prothrombinase complex to activate prothrombin to thrombin.
23677006	0	13	theme	bleeding	72:79	arg1	patient					81:87	a bleeding patient	70:87	a bleeding patient	70:87	The missense Thr211Pro mutation in the factor X activation peptide of a bleeding patient causes molecular defect in the clotting cascade.
23677006	4	14	theme	Exome	584:588	arg1	sequencing					590:599	Exome sequencing	584:599	Exome sequencing	584:599	Exome sequencing revealed that the patient carries a novel homozygous missense mutation that results in substitution of Thr211 with Pro in the activation peptide of FX.
23677006	5	15	link	O-linked	778:785	arg1	glycosylation					787:799	an O-linked glycosylation	775:799	an O-linked glycosylation	775:799	Thr211 is the site of an O-linked glycosylation in the activation peptide of FX.
23677006	3	16	theme	FX	508:509	arg1	deficiency					511:520	moderate FX deficiency	499:520	moderate FX deficiency	499:520	In this study, we identified a bleeding patient with moderate FX deficiency who exhibits a clotting defect only in the intrinsic pathway.
23677006	5	17	theme	glycosylation	787:799	arg1	glycosylation					787:799	an O-linked glycosylation	775:799	an O-linked glycosylation	775:799	Thr211 is the site of an O-linked glycosylation in the activation peptide of FX.
23677006	5	17	theme	glycosylation	787:799	arg1	Thr211					753:758	Thr211	753:758	Thr211	753:758	Thr211 is the site of an O-linked glycosylation in the activation peptide of FX.
23677006	5	17	theme	glycosylation	787:799	arg1	site					767:770	the site	763:770	the site of an O-linked glycosylation in the activation peptide of FX	763:831	Thr211 is the site of an O-linked glycosylation in the activation peptide of FX.
23677006	0	18	theme	molecular	96:104	arg1	defect					106:111	molecular defect	96:111	molecular defect	96:111	The missense Thr211Pro mutation in the factor X activation peptide of a bleeding patient causes molecular defect in the clotting cascade.
23677006	5	19	theme	O-linked	778:785	arg1	glycosylation					787:799	an O-linked glycosylation	775:799	an O-linked glycosylation	775:799	Thr211 is the site of an O-linked glycosylation in the activation peptide of FX.
23677006	2	20	theme	IXa-factor	378:387	arg1	VIIIa					389:393	either factor VIIa-tissue factor or factor IXa-factor VIIIa	335:393	VIIIa	389:393	FX can be activated by either factor VIIa-tissue factor or factor IXa-factor VIIIa in extrinsic and intrinsic pathways, respectively.
23677006	8	21	theme	Pro	1314:1316	arg1	substitution					1318:1329	Thr211 to Pro substitution	1304:1329	Thr211 to Pro substitution	1304:1329	Analysis of the results suggests that Thr211 to Pro substitution renders the FX mutant a poor substrate for both physiological activators, however, at physiological concentration of the substrate, the clotting defect manifest itself only in the intrinsic pathway, thus explaining the bleeding phenotype for the patient carrying this mutation.
23677006	6	22	theme	FX	941:942	arg1	activation					927:936	the activation	923:936	the activation of FX by intrinsic Xase	923:960	We postulated that the lack of this post-translational modification specifically impacts the activation of FX by intrinsic Xase, thereby impairing thrombin generation in the subject.
23677006	4	23	theme	activation	727:736	arg1	peptide					738:744	the activation peptide	723:744	the activation peptide of FX	723:750	Exome sequencing revealed that the patient carries a novel homozygous missense mutation that results in substitution of Thr211 with Pro in the activation peptide of FX.
23677006	2	24	theme	VIIa-tissue	349:359	arg1	factor					361:366	either factor VIIa-tissue factor or factor IXa-factor VIIIa	335:393	factor	361:366	FX can be activated by either factor VIIa-tissue factor or factor IXa-factor VIIIa in extrinsic and intrinsic pathways, respectively.
23677006	0	25	theme	missense	4:11	arg1	mutation					23:30	The missense Thr211Pro mutation	0:30	The missense Thr211Pro mutation in the factor X activation peptide of a bleeding patient	0:87	The missense Thr211Pro mutation in the factor X activation peptide of a bleeding patient causes molecular defect in the clotting cascade.
23677006	8	26	theme	intrinsic	1511:1519	arg1	pathway					1521:1527	the intrinsic pathway	1507:1527	the intrinsic pathway	1507:1527	Analysis of the results suggests that Thr211 to Pro substitution renders the FX mutant a poor substrate for both physiological activators, however, at physiological concentration of the substrate, the clotting defect manifest itself only in the intrinsic pathway, thus explaining the bleeding phenotype for the patient carrying this mutation.
23677006	7	27	theme	assay	1251:1255	arg1	systems					1257:1263	both purified and plasma-based assay systems	1220:1263	both purified and plasma-based assay systems	1220:1263	To test this hypothesis, we expressed both wild-type FX and FX containing this mutation in mammalian cells and following the purification of the zymogens to homogeneity characterized their properties in both purified and plasma-based assay systems.
23677006	4	28	theme	Thr211	704:709	arg1	substitution					688:699	substitution	688:699	substitution of Thr211 with Pro in the activation peptide of FX	688:750	Exome sequencing revealed that the patient carries a novel homozygous missense mutation that results in substitution of Thr211 with Pro in the activation peptide of FX.
23677006	7	29	theme	purified	1225:1232	arg1	systems					1257:1263	both purified and plasma-based assay systems	1220:1263	both purified and plasma-based assay systems	1220:1263	To test this hypothesis, we expressed both wild-type FX and FX containing this mutation in mammalian cells and following the purification of the zymogens to homogeneity characterized their properties in both purified and plasma-based assay systems.
23677006	2	30	theme	factor	342:347	arg1	factor					361:366	either factor VIIa-tissue factor or factor IXa-factor VIIIa	335:393	factor	361:366	FX can be activated by either factor VIIa-tissue factor or factor IXa-factor VIIIa in extrinsic and intrinsic pathways, respectively.
23677006	8	31	theme	clotting	1467:1474	arg1	defect					1476:1481	the clotting defect	1463:1481	the clotting defect manifest itself only in the intrinsic pathway, thus explaining the bleeding phenotype for the patient carrying this mutation	1463:1606	Analysis of the results suggests that Thr211 to Pro substitution renders the FX mutant a poor substrate for both physiological activators, however, at physiological concentration of the substrate, the clotting defect manifest itself only in the intrinsic pathway, thus explaining the bleeding phenotype for the patient carrying this mutation.
23677006	5	32	gly	glycosylation	787:799	arg2	Thr211					753:758	Thr211	753:758	Thr211	753:758	Thr211 is the site of an O-linked glycosylation in the activation peptide of FX.
23677006	5	32	gly	glycosylation	787:799	arg2	site					767:770	the site	763:770	the site of an O-linked glycosylation in the activation peptide of FX	763:831	Thr211 is the site of an O-linked glycosylation in the activation peptide of FX.
23677006	5	32	gly	glycosylation	787:799	arg1	peptide					819:825	the activation peptide	804:825	the activation peptide of FX	804:831	Thr211 is the site of an O-linked glycosylation in the activation peptide of FX.
23677006	5	32	gly	glycosylation	787:799	arg2	glycosylation					787:799	an O-linked glycosylation	775:799	an O-linked glycosylation	775:799	Thr211 is the site of an O-linked glycosylation in the activation peptide of FX.
23677006	8	33	dep	substitution	1318:1329	arg1	to					1311:1312	to	1311:1312	to	1311:1312	Analysis of the results suggests that Thr211 to Pro substitution renders the FX mutant a poor substrate for both physiological activators, however, at physiological concentration of the substrate, the clotting defect manifest itself only in the intrinsic pathway, thus explaining the bleeding phenotype for the patient carrying this mutation.
23677006	2	34	theme	extrinsic	398:406	arg1	pathways					422:429	extrinsic and intrinsic pathways	398:429	extrinsic and intrinsic pathways	398:429	FX can be activated by either factor VIIa-tissue factor or factor IXa-factor VIIIa in extrinsic and intrinsic pathways, respectively.
23677006	8	35	contain	carrying	1585:1592	arg2	mutation					1599:1606	this mutation	1594:1606	this mutation	1594:1606	Analysis of the results suggests that Thr211 to Pro substitution renders the FX mutant a poor substrate for both physiological activators, however, at physiological concentration of the substrate, the clotting defect manifest itself only in the intrinsic pathway, thus explaining the bleeding phenotype for the patient carrying this mutation.
23677006	8	35	contain	carrying	1585:1592	arg1	patient					1577:1583	the patient	1573:1583	the patient carrying this mutation	1573:1606	Analysis of the results suggests that Thr211 to Pro substitution renders the FX mutant a poor substrate for both physiological activators, however, at physiological concentration of the substrate, the clotting defect manifest itself only in the intrinsic pathway, thus explaining the bleeding phenotype for the patient carrying this mutation.
23677006	8	36	theme	FX	1343:1344	arg1	mutant					1346:1351	the FX mutant	1339:1351	the FX mutant	1339:1351	Analysis of the results suggests that Thr211 to Pro substitution renders the FX mutant a poor substrate for both physiological activators, however, at physiological concentration of the substrate, the clotting defect manifest itself only in the intrinsic pathway, thus explaining the bleeding phenotype for the patient carrying this mutation.
23677006	0	37	theme	Thr211Pro	13:21	arg1	mutation					23:30	The missense Thr211Pro mutation	0:30	The missense Thr211Pro mutation in the factor X activation peptide of a bleeding patient	0:87	The missense Thr211Pro mutation in the factor X activation peptide of a bleeding patient causes molecular defect in the clotting cascade.
23677006	7	38	dep	expressed	1045:1053	arg1	characterized					1186:1198	characterized	1186:1198	characterized their properties in both purified and plasma-based assay systems	1186:1263	To test this hypothesis, we expressed both wild-type FX and FX containing this mutation in mammalian cells and following the purification of the zymogens to homogeneity characterized their properties in both purified and plasma-based assay systems.
23677006	8	39	theme	results	1282:1288	arg1	Analysis					1266:1273	Analysis	1266:1273	Analysis of the results	1266:1288	Analysis of the results suggests that Thr211 to Pro substitution renders the FX mutant a poor substrate for both physiological activators, however, at physiological concentration of the substrate, the clotting defect manifest itself only in the intrinsic pathway, thus explaining the bleeding phenotype for the patient carrying this mutation.
23677006	1	40	theme	vitamin	157:163	arg1	zymogen					189:195	a vitamin K-dependent coagulation zymogen	155:195	a vitamin K-dependent coagulation zymogen	155:195	Factor X (FX) is a vitamin K-dependent coagulation zymogen, which upon activation to factor Xa assembles into the prothrombinase complex to activate prothrombin to thrombin.
23677006	1	40	theme	vitamin	157:163	arg1	X					145:145	Factor X	138:145	Factor X (FX)	138:150	Factor X (FX) is a vitamin K-dependent coagulation zymogen, which upon activation to factor Xa assembles into the prothrombinase complex to activate prothrombin to thrombin.
23677006	3	41	with	patient	486:492	arg1	deficiency					511:520	moderate FX deficiency	499:520	moderate FX deficiency	499:520	In this study, we identified a bleeding patient with moderate FX deficiency who exhibits a clotting defect only in the intrinsic pathway.
23677006	1	42	theme	prothrombinase	252:265	arg1	complex					267:273	the prothrombinase complex	248:273	the prothrombinase complex	248:273	Factor X (FX) is a vitamin K-dependent coagulation zymogen, which upon activation to factor Xa assembles into the prothrombinase complex to activate prothrombin to thrombin.
23677006	0	43	theme	clotting	120:127	arg1	cascade					129:135	the clotting cascade	116:135	the clotting cascade	116:135	The missense Thr211Pro mutation in the factor X activation peptide of a bleeding patient causes molecular defect in the clotting cascade.
23677006	1	44	theme	K-dependent	165:175	arg1	zymogen					189:195	a vitamin K-dependent coagulation zymogen	155:195	a vitamin K-dependent coagulation zymogen	155:195	Factor X (FX) is a vitamin K-dependent coagulation zymogen, which upon activation to factor Xa assembles into the prothrombinase complex to activate prothrombin to thrombin.
23677006	1	44	theme	K-dependent	165:175	arg1	X					145:145	Factor X	138:145	Factor X (FX)	138:150	Factor X (FX) is a vitamin K-dependent coagulation zymogen, which upon activation to factor Xa assembles into the prothrombinase complex to activate prothrombin to thrombin.
23677006	2	45	theme	factor	371:376	arg1	VIIIa					389:393	either factor VIIa-tissue factor or factor IXa-factor VIIIa	335:393	VIIIa	389:393	FX can be activated by either factor VIIa-tissue factor or factor IXa-factor VIIIa in extrinsic and intrinsic pathways, respectively.
23677006	1	46	theme	coagulation	177:187	arg1	zymogen					189:195	a vitamin K-dependent coagulation zymogen	155:195	a vitamin K-dependent coagulation zymogen	155:195	Factor X (FX) is a vitamin K-dependent coagulation zymogen, which upon activation to factor Xa assembles into the prothrombinase complex to activate prothrombin to thrombin.
23677006	1	46	theme	coagulation	177:187	arg1	X					145:145	Factor X	138:145	Factor X (FX)	138:150	Factor X (FX) is a vitamin K-dependent coagulation zymogen, which upon activation to factor Xa assembles into the prothrombinase complex to activate prothrombin to thrombin.
23677006	0	47	theme	X	46:46	arg1	peptide					59:65	the factor X activation peptide	35:65	the factor X activation peptide of a bleeding patient	35:87	The missense Thr211Pro mutation in the factor X activation peptide of a bleeding patient causes molecular defect in the clotting cascade.
23677006	5	48	theme	FX	830:831	arg1	peptide					819:825	the activation peptide	804:825	the activation peptide of FX	804:831	Thr211 is the site of an O-linked glycosylation in the activation peptide of FX.
23677006	3	49	theme	clotting	537:544	arg1	defect					546:551	a clotting defect	535:551	a clotting defect	535:551	In this study, we identified a bleeding patient with moderate FX deficiency who exhibits a clotting defect only in the intrinsic pathway.
23677006	0	50	theme	factor	39:44	arg1	peptide					59:65	the factor X activation peptide	35:65	the factor X activation peptide of a bleeding patient	35:87	The missense Thr211Pro mutation in the factor X activation peptide of a bleeding patient causes molecular defect in the clotting cascade.
23677006	6	51	theme	post-translational	870:887	arg1	modification					889:900	this post-translational modification	865:900	this post-translational modification	865:900	We postulated that the lack of this post-translational modification specifically impacts the activation of FX by intrinsic Xase, thereby impairing thrombin generation in the subject.
23677006	4	52	with	substitution	688:699	arg1	Pro					716:718	Pro	716:718	Pro	716:718	Exome sequencing revealed that the patient carries a novel homozygous missense mutation that results in substitution of Thr211 with Pro in the activation peptide of FX.
23677006	4	53	contain	carries	627:633	arg1	patient					619:625	the patient	615:625	the patient	615:625	Exome sequencing revealed that the patient carries a novel homozygous missense mutation that results in substitution of Thr211 with Pro in the activation peptide of FX.
23677006	4	53	contain	carries	627:633	arg2	mutation					663:670	a novel homozygous missense mutation	635:670	a novel homozygous missense mutation that results in substitution of Thr211 with Pro in the activation peptide of FX	635:750	Exome sequencing revealed that the patient carries a novel homozygous missense mutation that results in substitution of Thr211 with Pro in the activation peptide of FX.
23677006	8	54	theme	poor	1355:1358	arg1	substrate					1360:1368	a poor substrate	1353:1368	a poor substrate for both physiological activators	1353:1402	Analysis of the results suggests that Thr211 to Pro substitution renders the FX mutant a poor substrate for both physiological activators, however, at physiological concentration of the substrate, the clotting defect manifest itself only in the intrinsic pathway, thus explaining the bleeding phenotype for the patient carrying this mutation.
23677006	7	55	theme	plasma-based	1238:1249	arg1	systems					1257:1263	both purified and plasma-based assay systems	1220:1263	both purified and plasma-based assay systems	1220:1263	To test this hypothesis, we expressed both wild-type FX and FX containing this mutation in mammalian cells and following the purification of the zymogens to homogeneity characterized their properties in both purified and plasma-based assay systems.
23677006	4	56	from	substitution	688:699	arg1	peptide					738:744	the activation peptide	723:744	the activation peptide of FX	723:750	Exome sequencing revealed that the patient carries a novel homozygous missense mutation that results in substitution of Thr211 with Pro in the activation peptide of FX.
23677006	8	57	theme	physiological	1379:1391	arg1	activators					1393:1402	both physiological activators	1374:1402	both physiological activators	1374:1402	Analysis of the results suggests that Thr211 to Pro substitution renders the FX mutant a poor substrate for both physiological activators, however, at physiological concentration of the substrate, the clotting defect manifest itself only in the intrinsic pathway, thus explaining the bleeding phenotype for the patient carrying this mutation.
23677006	8	58	theme	physiological	1417:1429	arg1	concentration					1431:1443	physiological concentration	1417:1443	physiological concentration of the substrate	1417:1460	Analysis of the results suggests that Thr211 to Pro substitution renders the FX mutant a poor substrate for both physiological activators, however, at physiological concentration of the substrate, the clotting defect manifest itself only in the intrinsic pathway, thus explaining the bleeding phenotype for the patient carrying this mutation.
23677006	4	59	theme	FX	749:750	arg1	peptide					738:744	the activation peptide	723:744	the activation peptide of FX	723:750	Exome sequencing revealed that the patient carries a novel homozygous missense mutation that results in substitution of Thr211 with Pro in the activation peptide of FX.
23677006	4	60	theme	novel	637:641	arg1	mutation					663:670	a novel homozygous missense mutation	635:670	a novel homozygous missense mutation that results in substitution of Thr211 with Pro in the activation peptide of FX	635:750	Exome sequencing revealed that the patient carries a novel homozygous missense mutation that results in substitution of Thr211 with Pro in the activation peptide of FX.
23677006	6	61	theme	thrombin	981:988	arg1	generation					990:999	thrombin generation	981:999	thrombin generation	981:999	We postulated that the lack of this post-translational modification specifically impacts the activation of FX by intrinsic Xase, thereby impairing thrombin generation in the subject.
23677006	8	62	theme	Thr211	1304:1309	arg1	substitution					1318:1329	Thr211 to Pro substitution	1304:1329	Thr211 to Pro substitution	1304:1329	Analysis of the results suggests that Thr211 to Pro substitution renders the FX mutant a poor substrate for both physiological activators, however, at physiological concentration of the substrate, the clotting defect manifest itself only in the intrinsic pathway, thus explaining the bleeding phenotype for the patient carrying this mutation.
23677006	3	63	theme	bleeding	477:484	arg1	patient					486:492	a bleeding patient	475:492	a bleeding patient with moderate FX deficiency who exhibits a clotting defect only in the intrinsic pathway	475:581	In this study, we identified a bleeding patient with moderate FX deficiency who exhibits a clotting defect only in the intrinsic pathway.
23677006	8	64	theme	bleeding	1550:1557	arg1	phenotype					1559:1567	the bleeding phenotype	1546:1567	the bleeding phenotype for the patient carrying this mutation	1546:1606	Analysis of the results suggests that Thr211 to Pro substitution renders the FX mutant a poor substrate for both physiological activators, however, at physiological concentration of the substrate, the clotting defect manifest itself only in the intrinsic pathway, thus explaining the bleeding phenotype for the patient carrying this mutation.
23677006	4	65	theme	homozygous	643:652	arg1	mutation					663:670	a novel homozygous missense mutation	635:670	a novel homozygous missense mutation that results in substitution of Thr211 with Pro in the activation peptide of FX	635:750	Exome sequencing revealed that the patient carries a novel homozygous missense mutation that results in substitution of Thr211 with Pro in the activation peptide of FX.
23677006	5	66	theme	activation	808:817	arg1	peptide					819:825	the activation peptide	804:825	the activation peptide of FX	804:831	Thr211 is the site of an O-linked glycosylation in the activation peptide of FX.
23677006	0	67	theme	activation	48:57	arg1	peptide					59:65	the factor X activation peptide	35:65	the factor X activation peptide of a bleeding patient	35:87	The missense Thr211Pro mutation in the factor X activation peptide of a bleeding patient causes molecular defect in the clotting cascade.
23677006	0	68	from	mutation	23:30	arg1	peptide					59:65	the factor X activation peptide	35:65	the factor X activation peptide of a bleeding patient	35:87	The missense Thr211Pro mutation in the factor X activation peptide of a bleeding patient causes molecular defect in the clotting cascade.
23677006	3	69	theme	intrinsic	565:573	arg1	pathway					575:581	the intrinsic pathway	561:581	the intrinsic pathway	561:581	In this study, we identified a bleeding patient with moderate FX deficiency who exhibits a clotting defect only in the intrinsic pathway.
23677006	2	70	theme	intrinsic	412:420	arg1	pathways					422:429	extrinsic and intrinsic pathways	398:429	extrinsic and intrinsic pathways	398:429	FX can be activated by either factor VIIa-tissue factor or factor IXa-factor VIIIa in extrinsic and intrinsic pathways, respectively.
23677006	6	71	theme	modification	889:900	arg1	lack					857:860	the lack	853:860	the lack of this post-translational modification	853:900	We postulated that the lack of this post-translational modification specifically impacts the activation of FX by intrinsic Xase, thereby impairing thrombin generation in the subject.
19671700	10	0	from	TSR1	1635:1638	arg1	Replacement					1591:1601	Replacement	1591:1601	Replacement of mannosylated Trp residues in TSR1 with either Ala or Phe	1591:1661	Replacement of mannosylated Trp residues in TSR1 with either Ala or Phe affected punctin secretion efficiency.
19671700	9	1	from	Quantitation	1470:1481	arg1	cells					1537:1541	CHO-K1 cells	1530:1541	CHO-K1 cells	1530:1541	Quantitation of punctin-1 secretion in Lec35.1 cells versus CHO-K1 cells suggested decreased secretion in Lec35.1 cells.
19671700	9	1	from	Quantitation	1470:1481	arg1	cells					1517:1521	Lec35.1 cells	1509:1521	Lec35.1 cells	1509:1521	Quantitation of punctin-1 secretion in Lec35.1 cells versus CHO-K1 cells suggested decreased secretion in Lec35.1 cells.
19671700	0	2	from	1/punctin-1	80:90	arg1	modification					19:30	Post-translational modification	0:30	Post-translational modification of thrombospondin type-1 repeats in ADAMTS-like 1/punctin-1 by C-mannosylation of tryptophan.	0:124	Post-translational modification of thrombospondin type-1 repeats in ADAMTS-like 1/punctin-1 by C-mannosylation of tryptophan.
19671700	4	3	theme	mass	640:643	arg1	spectrometry					645:656	mass spectrometry	640:656	mass spectrometry	640:656	We investigated the presence and functional significance of C-mannosylation of ADAMTS-like 1/punctin-1, which contains four TSRs (two with predicted C-mannosylation sites), using mass spectrometry, metabolic labeling, site-directed mutagenesis, and expression in C-mannosylation-defective Chinese hamster ovary cell variants.
19671700	10	4	theme	residues	1623:1630	arg1	Replacement					1591:1601	Replacement	1591:1601	Replacement of mannosylated Trp residues in TSR1 with either Ala or Phe	1591:1661	Replacement of mannosylated Trp residues in TSR1 with either Ala or Phe affected punctin secretion efficiency.
19671700	8	5	from	cells	1441:1445	arg1	incorporation					1370:1382	incorporation	1370:1382	incorporation of d-[2,6-(3)H]mannose in secreted punctin-1 from CHO-K1 cells but not Lec35.1 cells	1370:1467	Metabolic labeling of CHO-K1 cells or Lec35.1 cells demonstrated incorporation of d-[2,6-(3)H]mannose in secreted punctin-1 from CHO-K1 cells but not Lec35.1 cells.
19671700	8	5	from	cells	1441:1445	arg1	punctin-1					1419:1427	secreted punctin-1	1410:1427	secreted punctin-1 from CHO-K1 cells but not Lec35.1 cells	1410:1467	Metabolic labeling of CHO-K1 cells or Lec35.1 cells demonstrated incorporation of d-[2,6-(3)H]mannose in secreted punctin-1 from CHO-K1 cells but not Lec35.1 cells.
19671700	4	6	dep	presence	481:488	arg1	the					477:479	the	477:479	the	477:479	We investigated the presence and functional significance of C-mannosylation of ADAMTS-like 1/punctin-1, which contains four TSRs (two with predicted C-mannosylation sites), using mass spectrometry, metabolic labeling, site-directed mutagenesis, and expression in C-mannosylation-defective Chinese hamster ovary cell variants.
19671700	9	7	from	secretion	1563:1571	arg1	cells					1584:1588	Lec35.1 cells	1576:1588	Lec35.1 cells	1576:1588	Quantitation of punctin-1 secretion in Lec35.1 cells versus CHO-K1 cells suggested decreased secretion in Lec35.1 cells.
19671700	10	8	theme	mannosylated	1606:1617	arg1	residues					1623:1630	mannosylated Trp residues	1606:1630	mannosylated Trp residues in TSR1	1606:1638	Replacement of mannosylated Trp residues in TSR1 with either Ala or Phe affected punctin secretion efficiency.
19671700	4	9	from	expression	710:719	arg1	variants					777:784	C-mannosylation-defective Chinese hamster ovary cell variants	724:784	C-mannosylation-defective Chinese hamster ovary cell variants	724:784	We investigated the presence and functional significance of C-mannosylation of ADAMTS-like 1/punctin-1, which contains four TSRs (two with predicted C-mannosylation sites), using mass spectrometry, metabolic labeling, site-directed mutagenesis, and expression in C-mannosylation-defective Chinese hamster ovary cell variants.
19671700	1	10	theme	C-C	211:213	arg1	linkage					215:221	a C-C linkage	209:221	a C-C linkage	209:221	Protein C-mannosylation is the attachment of alpha-mannopyranose to tryptophan via a C-C linkage.
19671700	4	11	theme	C-mannosylation-defective	724:748	arg1	ovary					766:770	C-mannosylation-defective Chinese hamster ovary	724:770	C-mannosylation-defective Chinese hamster ovary cell variants	724:784	We investigated the presence and functional significance of C-mannosylation of ADAMTS-like 1/punctin-1, which contains four TSRs (two with predicted C-mannosylation sites), using mass spectrometry, metabolic labeling, site-directed mutagenesis, and expression in C-mannosylation-defective Chinese hamster ovary cell variants.
19671700	8	12	from	cells	1463:1467	arg1	incorporation					1370:1382	incorporation	1370:1382	incorporation of d-[2,6-(3)H]mannose in secreted punctin-1 from CHO-K1 cells but not Lec35.1 cells	1370:1467	Metabolic labeling of CHO-K1 cells or Lec35.1 cells demonstrated incorporation of d-[2,6-(3)H]mannose in secreted punctin-1 from CHO-K1 cells but not Lec35.1 cells.
19671700	8	12	from	cells	1463:1467	arg1	punctin-1					1419:1427	secreted punctin-1	1410:1427	secreted punctin-1 from CHO-K1 cells but not Lec35.1 cells	1410:1467	Metabolic labeling of CHO-K1 cells or Lec35.1 cells demonstrated incorporation of d-[2,6-(3)H]mannose in secreted punctin-1 from CHO-K1 cells but not Lec35.1 cells.
19671700	9	13	theme	punctin-1	1486:1494	arg1	secretion					1496:1504	punctin-1 secretion	1486:1504	punctin-1 secretion	1486:1504	Quantitation of punctin-1 secretion in Lec35.1 cells versus CHO-K1 cells suggested decreased secretion in Lec35.1 cells.
19671700	4	14	theme	site-directed	679:691	arg1	mutagenesis					693:703	site-directed mutagenesis	679:703	site-directed mutagenesis	679:703	We investigated the presence and functional significance of C-mannosylation of ADAMTS-like 1/punctin-1, which contains four TSRs (two with predicted C-mannosylation sites), using mass spectrometry, metabolic labeling, site-directed mutagenesis, and expression in C-mannosylation-defective Chinese hamster ovary cell variants.
19671700	2	15	theme	thrombospondin	341:354	arg1	TSRs					372:375	TSRs	372:375	TSRs	372:375	This post-translational modification typically occurs within the sequence motif WXXW, which is frequently present in thrombospondin type-1 repeats (TSRs).
19671700	2	15	theme	thrombospondin	341:354	arg1	repeats					363:369	thrombospondin type-1 repeats	341:369	thrombospondin type-1 repeats (TSRs)	341:376	This post-translational modification typically occurs within the sequence motif WXXW, which is frequently present in thrombospondin type-1 repeats (TSRs).
19671700	8	16	theme	CHO-K1	1327:1332	arg1	cells					1334:1338	CHO-K1 cells	1327:1338	CHO-K1 cells	1327:1338	Metabolic labeling of CHO-K1 cells or Lec35.1 cells demonstrated incorporation of d-[2,6-(3)H]mannose in secreted punctin-1 from CHO-K1 cells but not Lec35.1 cells.
19671700	3	17	from	numerous	399:406	arg1	feature					426:432	and a defining feature	411:432	feature	426:432	TSRs are especially numerous in and a defining feature of the ADAMTS superfamily.
19671700	4	18	theme	functional	494:503	arg1	significance					505:516	functional significance	494:516	functional significance	494:516	We investigated the presence and functional significance of C-mannosylation of ADAMTS-like 1/punctin-1, which contains four TSRs (two with predicted C-mannosylation sites), using mass spectrometry, metabolic labeling, site-directed mutagenesis, and expression in C-mannosylation-defective Chinese hamster ovary cell variants.
19671700	4	19	gly	C-mannosylation	610:624	arg2	sites					626:630	predicted C-mannosylation sites	600:630	predicted C-mannosylation sites	600:630	We investigated the presence and functional significance of C-mannosylation of ADAMTS-like 1/punctin-1, which contains four TSRs (two with predicted C-mannosylation sites), using mass spectrometry, metabolic labeling, site-directed mutagenesis, and expression in C-mannosylation-defective Chinese hamster ovary cell variants.
19671700	9	20	theme	CHO-K1	1530:1535	arg1	cells					1537:1541	CHO-K1 cells	1530:1541	CHO-K1 cells	1530:1541	Quantitation of punctin-1 secretion in Lec35.1 cells versus CHO-K1 cells suggested decreased secretion in Lec35.1 cells.
19671700	8	21	theme	cells	1351:1355	arg1	labeling					1315:1322	Metabolic labeling	1305:1322	Metabolic labeling of CHO-K1 cells or Lec35.1 cells	1305:1355	Metabolic labeling of CHO-K1 cells or Lec35.1 cells demonstrated incorporation of d-[2,6-(3)H]mannose in secreted punctin-1 from CHO-K1 cells but not Lec35.1 cells.
19671700	1	22	theme	Protein	126:132	arg1	attachment					157:166	the attachment	153:166	the attachment of alpha-mannopyranose to tryptophan	153:203	Protein C-mannosylation is the attachment of alpha-mannopyranose to tryptophan via a C-C linkage.
19671700	1	22	theme	Protein	126:132	arg1	C-mannosylation					134:148	Protein C-mannosylation	126:148	Protein C-mannosylation	126:148	Protein C-mannosylation is the attachment of alpha-mannopyranose to tryptophan via a C-C linkage.
19671700	4	23	theme	hamster	758:764	arg1	ovary					766:770	C-mannosylation-defective Chinese hamster ovary	724:770	C-mannosylation-defective Chinese hamster ovary cell variants	724:784	We investigated the presence and functional significance of C-mannosylation of ADAMTS-like 1/punctin-1, which contains four TSRs (two with predicted C-mannosylation sites), using mass spectrometry, metabolic labeling, site-directed mutagenesis, and expression in C-mannosylation-defective Chinese hamster ovary cell variants.
19671700	11	24	theme	O-linked	1796:1803	arg1	fucose					1805:1810	O-linked fucose	1796:1810	O-linked fucose	1796:1810	These data demonstrate that TSR1 from punctin-1 carries C-mannosylation in close proximity to O-linked fucose.
19671700	7	25	theme	ADAMTS5	1276:1282	arg1	TSR1					1247:1250	TSR1	1247:1250	TSR1 of the related protease ADAMTS5	1247:1282	C-Mannosylation of TSR1 of the related protease ADAMTS5 was also identified.
19671700	2	26	theme	motif	298:302	arg1	present					330:336	present	330:336	present	330:336	This post-translational modification typically occurs within the sequence motif WXXW, which is frequently present in thrombospondin type-1 repeats (TSRs).
19671700	2	26	theme	motif	298:302	arg1	WXXW					304:307	the sequence motif WXXW	285:307	the sequence motif WXXW	285:307	This post-translational modification typically occurs within the sequence motif WXXW, which is frequently present in thrombospondin type-1 repeats (TSRs).
19671700	4	27	theme	1/punctin-1	552:562	arg1	presence					481:488	presence	481:488	presence	481:488	We investigated the presence and functional significance of C-mannosylation of ADAMTS-like 1/punctin-1, which contains four TSRs (two with predicted C-mannosylation sites), using mass spectrometry, metabolic labeling, site-directed mutagenesis, and expression in C-mannosylation-defective Chinese hamster ovary cell variants.
19671700	4	27	theme	1/punctin-1	552:562	arg1	significance					505:516	functional significance	494:516	functional significance	494:516	We investigated the presence and functional significance of C-mannosylation of ADAMTS-like 1/punctin-1, which contains four TSRs (two with predicted C-mannosylation sites), using mass spectrometry, metabolic labeling, site-directed mutagenesis, and expression in C-mannosylation-defective Chinese hamster ovary cell variants.
19671700	4	28	theme	cell	772:775	arg1	variants					777:784	C-mannosylation-defective Chinese hamster ovary cell variants	724:784	C-mannosylation-defective Chinese hamster ovary cell variants	724:784	We investigated the presence and functional significance of C-mannosylation of ADAMTS-like 1/punctin-1, which contains four TSRs (two with predicted C-mannosylation sites), using mass spectrometry, metabolic labeling, site-directed mutagenesis, and expression in C-mannosylation-defective Chinese hamster ovary cell variants.
19671700	4	29	from	spectrometry	645:656	arg1	variants					777:784	C-mannosylation-defective Chinese hamster ovary cell variants	724:784	C-mannosylation-defective Chinese hamster ovary cell variants	724:784	We investigated the presence and functional significance of C-mannosylation of ADAMTS-like 1/punctin-1, which contains four TSRs (two with predicted C-mannosylation sites), using mass spectrometry, metabolic labeling, site-directed mutagenesis, and expression in C-mannosylation-defective Chinese hamster ovary cell variants.
19671700	4	30	dep	TSRs	585:588	arg1	two					591:593	two	591:593	two	591:593	We investigated the presence and functional significance of C-mannosylation of ADAMTS-like 1/punctin-1, which contains four TSRs (two with predicted C-mannosylation sites), using mass spectrometry, metabolic labeling, site-directed mutagenesis, and expression in C-mannosylation-defective Chinese hamster ovary cell variants.
19671700	9	31	theme	Lec35.1	1576:1582	arg1	cells					1584:1588	Lec35.1 cells	1576:1588	Lec35.1 cells	1576:1588	Quantitation of punctin-1 secretion in Lec35.1 cells versus CHO-K1 cells suggested decreased secretion in Lec35.1 cells.
19671700	0	32	theme	tryptophan	114:123	arg1	C-mannosylation					95:109	C-mannosylation	95:109	C-mannosylation of tryptophan	95:123	Post-translational modification of thrombospondin type-1 repeats in ADAMTS-like 1/punctin-1 by C-mannosylation of tryptophan.
19671700	6	33	theme	Tandem	1047:1052	arg1	spectrometry					1059:1070	Tandem mass spectrometry	1047:1070	Tandem mass spectrometry (MS/MS)	1047:1078	Tandem mass spectrometry (MS/MS) and MS/MS/MS analysis demonstrated the characteristic cross-ring cleavage of C-mannose and identified the modified residues as Trp(39) and Trp(42).
19671700	6	33	theme	Tandem	1047:1052	arg1	MS/MS					1073:1077	MS/MS	1073:1077	MS/MS	1073:1077	Tandem mass spectrometry (MS/MS) and MS/MS/MS analysis demonstrated the characteristic cross-ring cleavage of C-mannose and identified the modified residues as Trp(39) and Trp(42).
19671700	5	34	theme	recombinant	820:830	arg1	punctin-1					838:846	recombinant human punctin-1	820:846	recombinant human punctin-1	820:846	Analysis of tryptic fragments of recombinant human punctin-1 by mass spectrometry identified a peptide derived from TSR1 containing the (36)WDAWGPWSECSRTC(49) sequence of interest modified with two mannose residues and a Glc-Fuc disaccharide (O-fucosylation).
19671700	3	35	theme	defining	417:424	arg1	feature					426:432	and a defining feature	411:432	feature	426:432	TSRs are especially numerous in and a defining feature of the ADAMTS superfamily.
19671700	7	36	theme	protease	1267:1274	arg1	ADAMTS5					1276:1282	the related protease ADAMTS5	1255:1282	the related protease ADAMTS5	1255:1282	C-Mannosylation of TSR1 of the related protease ADAMTS5 was also identified.
19671700	8	37	theme	mannose	1399:1405	arg1	incorporation					1370:1382	incorporation	1370:1382	incorporation of d-[2,6-(3)H]mannose in secreted punctin-1 from CHO-K1 cells but not Lec35.1 cells	1370:1467	Metabolic labeling of CHO-K1 cells or Lec35.1 cells demonstrated incorporation of d-[2,6-(3)H]mannose in secreted punctin-1 from CHO-K1 cells but not Lec35.1 cells.
19671700	0	38	theme	Post-translational	0:17	arg1	modification					19:30	Post-translational modification	0:30	Post-translational modification of thrombospondin type-1 repeats in ADAMTS-like 1/punctin-1 by C-mannosylation of tryptophan.	0:124	Post-translational modification of thrombospondin type-1 repeats in ADAMTS-like 1/punctin-1 by C-mannosylation of tryptophan.
19671700	8	39	from	incorporation	1370:1382	arg1	punctin-1					1419:1427	secreted punctin-1	1410:1427	secreted punctin-1 from CHO-K1 cells but not Lec35.1 cells	1410:1467	Metabolic labeling of CHO-K1 cells or Lec35.1 cells demonstrated incorporation of d-[2,6-(3)H]mannose in secreted punctin-1 from CHO-K1 cells but not Lec35.1 cells.
19671700	8	39	from	incorporation	1370:1382	arg1	cells					1441:1445	CHO-K1 cells	1434:1445	CHO-K1 cells but not Lec35.1 cells	1434:1467	Metabolic labeling of CHO-K1 cells or Lec35.1 cells demonstrated incorporation of d-[2,6-(3)H]mannose in secreted punctin-1 from CHO-K1 cells but not Lec35.1 cells.
19671700	8	39	from	incorporation	1370:1382	arg1	cells					1463:1467	Lec35.1 cells	1455:1467	CHO-K1 cells but not Lec35.1 cells	1434:1467	Metabolic labeling of CHO-K1 cells or Lec35.1 cells demonstrated incorporation of d-[2,6-(3)H]mannose in secreted punctin-1 from CHO-K1 cells but not Lec35.1 cells.
19671700	6	40	theme	cross-ring	1134:1143	arg1	cleavage					1145:1152	the characteristic cross-ring cleavage	1115:1152	the characteristic cross-ring cleavage of C-mannose	1115:1165	Tandem mass spectrometry (MS/MS) and MS/MS/MS analysis demonstrated the characteristic cross-ring cleavage of C-mannose and identified the modified residues as Trp(39) and Trp(42).
19671700	10	41	with	Replacement	1591:1601	arg1	Phe					1659:1661	Phe	1659:1661	Phe	1659:1661	Replacement of mannosylated Trp residues in TSR1 with either Ala or Phe affected punctin secretion efficiency.
19671700	10	41	with	Replacement	1591:1601	arg1	Ala					1652:1654	Ala	1652:1654	Ala	1652:1654	Replacement of mannosylated Trp residues in TSR1 with either Ala or Phe affected punctin secretion efficiency.
19671700	8	42	theme	secreted	1410:1417	arg1	punctin-1					1419:1427	secreted punctin-1	1410:1427	secreted punctin-1 from CHO-K1 cells but not Lec35.1 cells	1410:1467	Metabolic labeling of CHO-K1 cells or Lec35.1 cells demonstrated incorporation of d-[2,6-(3)H]mannose in secreted punctin-1 from CHO-K1 cells but not Lec35.1 cells.
19671700	9	43	theme	decreased	1553:1561	arg1	secretion					1563:1571	decreased secretion	1553:1571	decreased secretion in Lec35.1 cells	1553:1588	Quantitation of punctin-1 secretion in Lec35.1 cells versus CHO-K1 cells suggested decreased secretion in Lec35.1 cells.
19671700	3	44	theme	ADAMTS	441:446	arg1	superfamily					448:458	the ADAMTS superfamily	437:458	the ADAMTS superfamily	437:458	TSRs are especially numerous in and a defining feature of the ADAMTS superfamily.
19671700	4	45	theme	C-mannosylation	610:624	arg1	sites					626:630	predicted C-mannosylation sites	600:630	predicted C-mannosylation sites	600:630	We investigated the presence and functional significance of C-mannosylation of ADAMTS-like 1/punctin-1, which contains four TSRs (two with predicted C-mannosylation sites), using mass spectrometry, metabolic labeling, site-directed mutagenesis, and expression in C-mannosylation-defective Chinese hamster ovary cell variants.
19671700	0	46	theme	type-1	50:55	arg1	repeats					57:63	thrombospondin type-1 repeats	35:63	thrombospondin type-1 repeats in ADAMTS-like 1/punctin-1	35:90	Post-translational modification of thrombospondin type-1 repeats in ADAMTS-like 1/punctin-1 by C-mannosylation of tryptophan.
19671700	5	47	theme	punctin-1	838:846	arg1	fragments					807:815	tryptic fragments	799:815	tryptic fragments of recombinant human punctin-1	799:846	Analysis of tryptic fragments of recombinant human punctin-1 by mass spectrometry identified a peptide derived from TSR1 containing the (36)WDAWGPWSECSRTC(49) sequence of interest modified with two mannose residues and a Glc-Fuc disaccharide (O-fucosylation).
19671700	12	48	theme	punctin-1	1893:1901	arg1	secretion					1903:1911	punctin-1 secretion	1893:1911	punctin-1 secretion	1893:1911	Together, these modifications appear to provide a quality control mechanism for punctin-1 secretion.
19671700	11	49	gly	carries	1750:1756	arg1	proximity					1783:1791	close proximity	1777:1791	close proximity to O-linked fucose	1777:1810	These data demonstrate that TSR1 from punctin-1 carries C-mannosylation in close proximity to O-linked fucose.
19671700	11	50	theme	close	1777:1781	arg1	proximity					1783:1791	close proximity	1777:1791	close proximity to O-linked fucose	1777:1810	These data demonstrate that TSR1 from punctin-1 carries C-mannosylation in close proximity to O-linked fucose.
19671700	12	51	theme	quality	1863:1869	arg1	mechanism					1879:1887	a quality control mechanism	1861:1887	a quality control mechanism for punctin-1 secretion	1861:1911	Together, these modifications appear to provide a quality control mechanism for punctin-1 secretion.
19671700	4	52	theme	metabolic	659:667	arg1	labeling					669:676	metabolic labeling	659:676	metabolic labeling	659:676	We investigated the presence and functional significance of C-mannosylation of ADAMTS-like 1/punctin-1, which contains four TSRs (two with predicted C-mannosylation sites), using mass spectrometry, metabolic labeling, site-directed mutagenesis, and expression in C-mannosylation-defective Chinese hamster ovary cell variants.
19671700	1	53	attach	attachment	157:166	arg1	tryptophan					194:203	tryptophan	194:203	tryptophan	194:203	Protein C-mannosylation is the attachment of alpha-mannopyranose to tryptophan via a C-C linkage.
19671700	1	53	attach	attachment	157:166	arg2	alpha-mannopyranose					171:189	alpha-mannopyranose	171:189	alpha-mannopyranose	171:189	Protein C-mannosylation is the attachment of alpha-mannopyranose to tryptophan via a C-C linkage.
19671700	5	54	attach	derived	890:896	arg1	TSR1					903:906	TSR1	903:906	TSR1 containing the (36)WDAWGPWSECSRTC(49) sequence of interest modified with two mannose residues and a Glc-Fuc disaccharide (O-fucosylation)	903:1044	Analysis of tryptic fragments of recombinant human punctin-1 by mass spectrometry identified a peptide derived from TSR1 containing the (36)WDAWGPWSECSRTC(49) sequence of interest modified with two mannose residues and a Glc-Fuc disaccharide (O-fucosylation).
19671700	5	54	attach	derived	890:896	arg2	peptide					882:888	a peptide	880:888	a peptide derived from TSR1 containing the (36)WDAWGPWSECSRTC(49) sequence of interest modified with two mannose residues and a Glc-Fuc disaccharide (O-fucosylation)	880:1044	Analysis of tryptic fragments of recombinant human punctin-1 by mass spectrometry identified a peptide derived from TSR1 containing the (36)WDAWGPWSECSRTC(49) sequence of interest modified with two mannose residues and a Glc-Fuc disaccharide (O-fucosylation).
19671700	12	55	theme	control	1871:1877	arg1	mechanism					1879:1887	a quality control mechanism	1861:1887	a quality control mechanism for punctin-1 secretion	1861:1911	Together, these modifications appear to provide a quality control mechanism for punctin-1 secretion.
19671700	8	56	theme	d-[2,6-	1387:1393	arg1	mannose					1399:1405	d-[2,6-(3)H]mannose	1387:1405	d-[2,6-(3)H]mannose	1387:1405	Metabolic labeling of CHO-K1 cells or Lec35.1 cells demonstrated incorporation of d-[2,6-(3)H]mannose in secreted punctin-1 from CHO-K1 cells but not Lec35.1 cells.
19671700	8	56	theme	d-[2,6-	1387:1393	arg1	H					1397:1397	3)H	1395:1397	3)H	1395:1397	Metabolic labeling of CHO-K1 cells or Lec35.1 cells demonstrated incorporation of d-[2,6-(3)H]mannose in secreted punctin-1 from CHO-K1 cells but not Lec35.1 cells.
19671700	10	57	theme	Trp	1619:1621	arg1	residues					1623:1630	mannosylated Trp residues	1606:1630	mannosylated Trp residues in TSR1	1606:1638	Replacement of mannosylated Trp residues in TSR1 with either Ala or Phe affected punctin secretion efficiency.
19671700	5	58	theme	WDAWGPWSECSRTC	927:940	arg1	sequence					946:953	the (36)WDAWGPWSECSRTC(49) sequence	919:953	the (36)WDAWGPWSECSRTC(49) sequence of interest modified with two mannose residues	919:1000	Analysis of tryptic fragments of recombinant human punctin-1 by mass spectrometry identified a peptide derived from TSR1 containing the (36)WDAWGPWSECSRTC(49) sequence of interest modified with two mannose residues and a Glc-Fuc disaccharide (O-fucosylation).
19671700	5	59	theme	mass	851:854	arg1	spectrometry					856:867	mass spectrometry	851:867	mass spectrometry	851:867	Analysis of tryptic fragments of recombinant human punctin-1 by mass spectrometry identified a peptide derived from TSR1 containing the (36)WDAWGPWSECSRTC(49) sequence of interest modified with two mannose residues and a Glc-Fuc disaccharide (O-fucosylation).
19671700	7	60	theme	related	1259:1265	arg1	ADAMTS5					1276:1282	the related protease ADAMTS5	1255:1282	the related protease ADAMTS5	1255:1282	C-Mannosylation of TSR1 of the related protease ADAMTS5 was also identified.
19671700	2	61	theme	type-1	356:361	arg1	TSRs					372:375	TSRs	372:375	TSRs	372:375	This post-translational modification typically occurs within the sequence motif WXXW, which is frequently present in thrombospondin type-1 repeats (TSRs).
19671700	2	61	theme	type-1	356:361	arg1	repeats					363:369	thrombospondin type-1 repeats	341:369	thrombospondin type-1 repeats (TSRs)	341:376	This post-translational modification typically occurs within the sequence motif WXXW, which is frequently present in thrombospondin type-1 repeats (TSRs).
19671700	4	62	from	mutagenesis	693:703	arg1	variants					777:784	C-mannosylation-defective Chinese hamster ovary cell variants	724:784	C-mannosylation-defective Chinese hamster ovary cell variants	724:784	We investigated the presence and functional significance of C-mannosylation of ADAMTS-like 1/punctin-1, which contains four TSRs (two with predicted C-mannosylation sites), using mass spectrometry, metabolic labeling, site-directed mutagenesis, and expression in C-mannosylation-defective Chinese hamster ovary cell variants.
19671700	8	63	dep	H	1397:1397	arg1	3					1395:1395	3	1395:1395	3	1395:1395	Metabolic labeling of CHO-K1 cells or Lec35.1 cells demonstrated incorporation of d-[2,6-(3)H]mannose in secreted punctin-1 from CHO-K1 cells but not Lec35.1 cells.
19671700	5	64	contain	containing	908:917	arg2	disaccharide					1016:1027	a Glc-Fuc disaccharide	1006:1027	a Glc-Fuc disaccharide (O-fucosylation)	1006:1044	Analysis of tryptic fragments of recombinant human punctin-1 by mass spectrometry identified a peptide derived from TSR1 containing the (36)WDAWGPWSECSRTC(49) sequence of interest modified with two mannose residues and a Glc-Fuc disaccharide (O-fucosylation).
19671700	5	64	contain	containing	908:917	arg2	O-fucosylation					1030:1043	O-fucosylation	1030:1043	O-fucosylation	1030:1043	Analysis of tryptic fragments of recombinant human punctin-1 by mass spectrometry identified a peptide derived from TSR1 containing the (36)WDAWGPWSECSRTC(49) sequence of interest modified with two mannose residues and a Glc-Fuc disaccharide (O-fucosylation).
19671700	5	64	contain	containing	908:917	arg1	TSR1					903:906	TSR1	903:906	TSR1 containing the (36)WDAWGPWSECSRTC(49) sequence of interest modified with two mannose residues and a Glc-Fuc disaccharide (O-fucosylation)	903:1044	Analysis of tryptic fragments of recombinant human punctin-1 by mass spectrometry identified a peptide derived from TSR1 containing the (36)WDAWGPWSECSRTC(49) sequence of interest modified with two mannose residues and a Glc-Fuc disaccharide (O-fucosylation).
19671700	5	64	contain	containing	908:917	arg2	sequence					946:953	the (36)WDAWGPWSECSRTC(49) sequence	919:953	the (36)WDAWGPWSECSRTC(49) sequence of interest modified with two mannose residues	919:1000	Analysis of tryptic fragments of recombinant human punctin-1 by mass spectrometry identified a peptide derived from TSR1 containing the (36)WDAWGPWSECSRTC(49) sequence of interest modified with two mannose residues and a Glc-Fuc disaccharide (O-fucosylation).
19671700	8	65	theme	Metabolic	1305:1313	arg1	labeling					1315:1322	Metabolic labeling	1305:1322	Metabolic labeling of CHO-K1 cells or Lec35.1 cells	1305:1355	Metabolic labeling of CHO-K1 cells or Lec35.1 cells demonstrated incorporation of d-[2,6-(3)H]mannose in secreted punctin-1 from CHO-K1 cells but not Lec35.1 cells.
19671700	10	66	theme	punctin	1672:1678	arg1	efficiency					1690:1699	punctin secretion efficiency	1672:1699	punctin secretion efficiency	1672:1699	Replacement of mannosylated Trp residues in TSR1 with either Ala or Phe affected punctin secretion efficiency.
19671700	2	67	theme	sequence	289:296	arg1	present					330:336	present	330:336	present	330:336	This post-translational modification typically occurs within the sequence motif WXXW, which is frequently present in thrombospondin type-1 repeats (TSRs).
19671700	2	67	theme	sequence	289:296	arg1	WXXW					304:307	the sequence motif WXXW	285:307	the sequence motif WXXW	285:307	This post-translational modification typically occurs within the sequence motif WXXW, which is frequently present in thrombospondin type-1 repeats (TSRs).
19671700	9	68	theme	Lec35.1	1509:1515	arg1	cells					1517:1521	Lec35.1 cells	1509:1521	Lec35.1 cells	1509:1521	Quantitation of punctin-1 secretion in Lec35.1 cells versus CHO-K1 cells suggested decreased secretion in Lec35.1 cells.
19671700	4	69	from	labeling	669:676	arg1	variants					777:784	C-mannosylation-defective Chinese hamster ovary cell variants	724:784	C-mannosylation-defective Chinese hamster ovary cell variants	724:784	We investigated the presence and functional significance of C-mannosylation of ADAMTS-like 1/punctin-1, which contains four TSRs (two with predicted C-mannosylation sites), using mass spectrometry, metabolic labeling, site-directed mutagenesis, and expression in C-mannosylation-defective Chinese hamster ovary cell variants.
19671700	2	70	attach	present	330:336	arg2	WXXW					304:307	the sequence motif WXXW	285:307	the sequence motif WXXW	285:307	This post-translational modification typically occurs within the sequence motif WXXW, which is frequently present in thrombospondin type-1 repeats (TSRs).
19671700	2	70	attach	present	330:336	arg1	repeats					363:369	thrombospondin type-1 repeats	341:369	thrombospondin type-1 repeats (TSRs)	341:376	This post-translational modification typically occurs within the sequence motif WXXW, which is frequently present in thrombospondin type-1 repeats (TSRs).
19671700	2	70	attach	present	330:336	arg1	TSRs					372:375	TSRs	372:375	TSRs	372:375	This post-translational modification typically occurs within the sequence motif WXXW, which is frequently present in thrombospondin type-1 repeats (TSRs).
19671700	2	70	attach	present	330:336	arg2	present					330:336	present	330:336	present	330:336	This post-translational modification typically occurs within the sequence motif WXXW, which is frequently present in thrombospondin type-1 repeats (TSRs).
19671700	7	71	theme	TSR1	1247:1250	arg1	C-Mannosylation					1228:1242	C-Mannosylation	1228:1242	C-Mannosylation of TSR1 of the related protease ADAMTS5	1228:1282	C-Mannosylation of TSR1 of the related protease ADAMTS5 was also identified.
19671700	10	72	gly	mannosylated	1606:1617	arg1	residues					1623:1630	mannosylated Trp residues	1606:1630	mannosylated Trp residues in TSR1	1606:1638	Replacement of mannosylated Trp residues in TSR1 with either Ala or Phe affected punctin secretion efficiency.
19671700	8	73	theme	cells	1334:1338	arg1	labeling					1315:1322	Metabolic labeling	1305:1322	Metabolic labeling of CHO-K1 cells or Lec35.1 cells	1305:1355	Metabolic labeling of CHO-K1 cells or Lec35.1 cells demonstrated incorporation of d-[2,6-(3)H]mannose in secreted punctin-1 from CHO-K1 cells but not Lec35.1 cells.
19671700	5	74	theme	mannose	985:991	arg1	residues					993:1000	two mannose residues	981:1000	two mannose residues	981:1000	Analysis of tryptic fragments of recombinant human punctin-1 by mass spectrometry identified a peptide derived from TSR1 containing the (36)WDAWGPWSECSRTC(49) sequence of interest modified with two mannose residues and a Glc-Fuc disaccharide (O-fucosylation).
19671700	6	75	theme	MS/MS/MS	1084:1091	arg1	analysis					1093:1100	MS/MS/MS analysis	1084:1100	MS/MS/MS analysis	1084:1100	Tandem mass spectrometry (MS/MS) and MS/MS/MS analysis demonstrated the characteristic cross-ring cleavage of C-mannose and identified the modified residues as Trp(39) and Trp(42).
19671700	8	76	theme	Lec35.1	1343:1349	arg1	cells					1351:1355	Lec35.1 cells	1343:1355	Lec35.1 cells	1343:1355	Metabolic labeling of CHO-K1 cells or Lec35.1 cells demonstrated incorporation of d-[2,6-(3)H]mannose in secreted punctin-1 from CHO-K1 cells but not Lec35.1 cells.
19671700	5	77	theme	human	832:836	arg1	punctin-1					838:846	recombinant human punctin-1	820:846	recombinant human punctin-1	820:846	Analysis of tryptic fragments of recombinant human punctin-1 by mass spectrometry identified a peptide derived from TSR1 containing the (36)WDAWGPWSECSRTC(49) sequence of interest modified with two mannose residues and a Glc-Fuc disaccharide (O-fucosylation).
19671700	11	78	contain	carries	1750:1756	arg2	C-mannosylation					1758:1772	C-mannosylation	1758:1772	C-mannosylation	1758:1772	These data demonstrate that TSR1 from punctin-1 carries C-mannosylation in close proximity to O-linked fucose.
19671700	11	78	contain	carries	1750:1756	arg3	proximity					1783:1791	close proximity	1777:1791	close proximity to O-linked fucose	1777:1810	These data demonstrate that TSR1 from punctin-1 carries C-mannosylation in close proximity to O-linked fucose.
19671700	11	78	contain	carries	1750:1756	arg1	TSR1					1730:1733	TSR1	1730:1733	TSR1 from punctin-1	1730:1748	These data demonstrate that TSR1 from punctin-1 carries C-mannosylation in close proximity to O-linked fucose.
19671700	9	79	theme	secretion	1496:1504	arg1	Quantitation					1470:1481	Quantitation	1470:1481	Quantitation of punctin-1 secretion in Lec35.1 cells versus CHO-K1 cells	1470:1541	Quantitation of punctin-1 secretion in Lec35.1 cells versus CHO-K1 cells suggested decreased secretion in Lec35.1 cells.
19671700	1	80	theme	alpha-mannopyranose	171:189	arg1	attachment					157:166	the attachment	153:166	the attachment of alpha-mannopyranose to tryptophan	153:203	Protein C-mannosylation is the attachment of alpha-mannopyranose to tryptophan via a C-C linkage.
19671700	1	80	theme	alpha-mannopyranose	171:189	arg1	C-mannosylation					134:148	Protein C-mannosylation	126:148	Protein C-mannosylation	126:148	Protein C-mannosylation is the attachment of alpha-mannopyranose to tryptophan via a C-C linkage.
19671700	2	81	from	present	330:336	arg1	TSRs					372:375	TSRs	372:375	TSRs	372:375	This post-translational modification typically occurs within the sequence motif WXXW, which is frequently present in thrombospondin type-1 repeats (TSRs).
19671700	2	81	from	present	330:336	arg1	repeats					363:369	thrombospondin type-1 repeats	341:369	thrombospondin type-1 repeats (TSRs)	341:376	This post-translational modification typically occurs within the sequence motif WXXW, which is frequently present in thrombospondin type-1 repeats (TSRs).
19671700	4	82	theme	Chinese	750:756	arg1	ovary					766:770	C-mannosylation-defective Chinese hamster ovary	724:770	C-mannosylation-defective Chinese hamster ovary cell variants	724:784	We investigated the presence and functional significance of C-mannosylation of ADAMTS-like 1/punctin-1, which contains four TSRs (two with predicted C-mannosylation sites), using mass spectrometry, metabolic labeling, site-directed mutagenesis, and expression in C-mannosylation-defective Chinese hamster ovary cell variants.
19671700	5	83	theme	fragments	807:815	arg1	Analysis					787:794	Analysis	787:794	Analysis of tryptic fragments of recombinant human punctin-1 by mass spectrometry	787:867	Analysis of tryptic fragments of recombinant human punctin-1 by mass spectrometry identified a peptide derived from TSR1 containing the (36)WDAWGPWSECSRTC(49) sequence of interest modified with two mannose residues and a Glc-Fuc disaccharide (O-fucosylation).
19671700	5	84	theme	interest	958:965	arg1	O-fucosylation					1030:1043	O-fucosylation	1030:1043	O-fucosylation	1030:1043	Analysis of tryptic fragments of recombinant human punctin-1 by mass spectrometry identified a peptide derived from TSR1 containing the (36)WDAWGPWSECSRTC(49) sequence of interest modified with two mannose residues and a Glc-Fuc disaccharide (O-fucosylation).
19671700	5	84	theme	interest	958:965	arg1	sequence					946:953	the (36)WDAWGPWSECSRTC(49) sequence	919:953	the (36)WDAWGPWSECSRTC(49) sequence of interest modified with two mannose residues	919:1000	Analysis of tryptic fragments of recombinant human punctin-1 by mass spectrometry identified a peptide derived from TSR1 containing the (36)WDAWGPWSECSRTC(49) sequence of interest modified with two mannose residues and a Glc-Fuc disaccharide (O-fucosylation).
19671700	5	84	theme	interest	958:965	arg1	disaccharide					1016:1027	a Glc-Fuc disaccharide	1006:1027	a Glc-Fuc disaccharide (O-fucosylation)	1006:1044	Analysis of tryptic fragments of recombinant human punctin-1 by mass spectrometry identified a peptide derived from TSR1 containing the (36)WDAWGPWSECSRTC(49) sequence of interest modified with two mannose residues and a Glc-Fuc disaccharide (O-fucosylation).
19671700	0	85	from	modification	19:30	arg1	1/punctin-1					80:90	ADAMTS-like 1/punctin-1	68:90	ADAMTS-like 1/punctin-1	68:90	Post-translational modification of thrombospondin type-1 repeats in ADAMTS-like 1/punctin-1 by C-mannosylation of tryptophan.
19671700	4	86	theme	ovary	766:770	arg1	variants					777:784	C-mannosylation-defective Chinese hamster ovary cell variants	724:784	C-mannosylation-defective Chinese hamster ovary cell variants	724:784	We investigated the presence and functional significance of C-mannosylation of ADAMTS-like 1/punctin-1, which contains four TSRs (two with predicted C-mannosylation sites), using mass spectrometry, metabolic labeling, site-directed mutagenesis, and expression in C-mannosylation-defective Chinese hamster ovary cell variants.
19671700	5	87	theme	tryptic	799:805	arg1	fragments					807:815	tryptic fragments	799:815	tryptic fragments of recombinant human punctin-1	799:846	Analysis of tryptic fragments of recombinant human punctin-1 by mass spectrometry identified a peptide derived from TSR1 containing the (36)WDAWGPWSECSRTC(49) sequence of interest modified with two mannose residues and a Glc-Fuc disaccharide (O-fucosylation).
19671700	2	88	from	repeats	363:369	arg1	present					330:336	present	330:336	present	330:336	This post-translational modification typically occurs within the sequence motif WXXW, which is frequently present in thrombospondin type-1 repeats (TSRs).
19671700	2	88	from	repeats	363:369	arg1	WXXW					304:307	the sequence motif WXXW	285:307	the sequence motif WXXW	285:307	This post-translational modification typically occurs within the sequence motif WXXW, which is frequently present in thrombospondin type-1 repeats (TSRs).
19671700	6	89	theme	mass	1054:1057	arg1	spectrometry					1059:1070	Tandem mass spectrometry	1047:1070	Tandem mass spectrometry (MS/MS)	1047:1078	Tandem mass spectrometry (MS/MS) and MS/MS/MS analysis demonstrated the characteristic cross-ring cleavage of C-mannose and identified the modified residues as Trp(39) and Trp(42).
19671700	6	89	theme	mass	1054:1057	arg1	MS/MS					1073:1077	MS/MS	1073:1077	MS/MS	1073:1077	Tandem mass spectrometry (MS/MS) and MS/MS/MS analysis demonstrated the characteristic cross-ring cleavage of C-mannose and identified the modified residues as Trp(39) and Trp(42).
19671700	11	90	from	punctin-1	1740:1748	arg1	TSR1					1730:1733	TSR1	1730:1733	TSR1 from punctin-1	1730:1748	These data demonstrate that TSR1 from punctin-1 carries C-mannosylation in close proximity to O-linked fucose.
19671700	4	91	theme	C-mannosylation	521:535	arg1	presence					481:488	presence	481:488	presence	481:488	We investigated the presence and functional significance of C-mannosylation of ADAMTS-like 1/punctin-1, which contains four TSRs (two with predicted C-mannosylation sites), using mass spectrometry, metabolic labeling, site-directed mutagenesis, and expression in C-mannosylation-defective Chinese hamster ovary cell variants.
19671700	4	91	theme	C-mannosylation	521:535	arg1	significance					505:516	functional significance	494:516	functional significance	494:516	We investigated the presence and functional significance of C-mannosylation of ADAMTS-like 1/punctin-1, which contains four TSRs (two with predicted C-mannosylation sites), using mass spectrometry, metabolic labeling, site-directed mutagenesis, and expression in C-mannosylation-defective Chinese hamster ovary cell variants.
19671700	0	92	gly	C-mannosylation	95:109	arg1	tryptophan					114:123	tryptophan	114:123	tryptophan	114:123	Post-translational modification of thrombospondin type-1 repeats in ADAMTS-like 1/punctin-1 by C-mannosylation of tryptophan.
19671700	6	93	theme	C-mannose	1157:1165	arg1	cleavage					1145:1152	the characteristic cross-ring cleavage	1115:1152	the characteristic cross-ring cleavage of C-mannose	1115:1165	Tandem mass spectrometry (MS/MS) and MS/MS/MS analysis demonstrated the characteristic cross-ring cleavage of C-mannose and identified the modified residues as Trp(39) and Trp(42).
19671700	0	94	from	repeats	57:63	arg1	1/punctin-1					80:90	ADAMTS-like 1/punctin-1	68:90	ADAMTS-like 1/punctin-1	68:90	Post-translational modification of thrombospondin type-1 repeats in ADAMTS-like 1/punctin-1 by C-mannosylation of tryptophan.
19671700	11	95	link	O-linked	1796:1803	arg1	fucose					1805:1810	O-linked fucose	1796:1810	O-linked fucose	1796:1810	These data demonstrate that TSR1 from punctin-1 carries C-mannosylation in close proximity to O-linked fucose.
19671700	3	96	from	feature	426:432	arg1	numerous					399:406	numerous	399:406	numerous	399:406	TSRs are especially numerous in and a defining feature of the ADAMTS superfamily.
19671700	4	97	theme	predicted	600:608	arg1	sites					626:630	predicted C-mannosylation sites	600:630	predicted C-mannosylation sites	600:630	We investigated the presence and functional significance of C-mannosylation of ADAMTS-like 1/punctin-1, which contains four TSRs (two with predicted C-mannosylation sites), using mass spectrometry, metabolic labeling, site-directed mutagenesis, and expression in C-mannosylation-defective Chinese hamster ovary cell variants.
19671700	10	98	theme	secretion	1680:1688	arg1	efficiency					1690:1699	punctin secretion efficiency	1672:1699	punctin secretion efficiency	1672:1699	Replacement of mannosylated Trp residues in TSR1 with either Ala or Phe affected punctin secretion efficiency.
19671700	0	99	theme	thrombospondin	35:48	arg1	repeats					57:63	thrombospondin type-1 repeats	35:63	thrombospondin type-1 repeats in ADAMTS-like 1/punctin-1	35:90	Post-translational modification of thrombospondin type-1 repeats in ADAMTS-like 1/punctin-1 by C-mannosylation of tryptophan.
19671700	5	100	theme	Glc-Fuc	1008:1014	arg1	O-fucosylation					1030:1043	O-fucosylation	1030:1043	O-fucosylation	1030:1043	Analysis of tryptic fragments of recombinant human punctin-1 by mass spectrometry identified a peptide derived from TSR1 containing the (36)WDAWGPWSECSRTC(49) sequence of interest modified with two mannose residues and a Glc-Fuc disaccharide (O-fucosylation).
19671700	5	100	theme	Glc-Fuc	1008:1014	arg1	disaccharide					1016:1027	a Glc-Fuc disaccharide	1006:1027	a Glc-Fuc disaccharide (O-fucosylation)	1006:1044	Analysis of tryptic fragments of recombinant human punctin-1 by mass spectrometry identified a peptide derived from TSR1 containing the (36)WDAWGPWSECSRTC(49) sequence of interest modified with two mannose residues and a Glc-Fuc disaccharide (O-fucosylation).
19671700	6	101	theme	characteristic	1119:1132	arg1	cleavage					1145:1152	the characteristic cross-ring cleavage	1115:1152	the characteristic cross-ring cleavage of C-mannose	1115:1165	Tandem mass spectrometry (MS/MS) and MS/MS/MS analysis demonstrated the characteristic cross-ring cleavage of C-mannose and identified the modified residues as Trp(39) and Trp(42).
19671700	0	102	theme	repeats	57:63	arg1	modification					19:30	Post-translational modification	0:30	Post-translational modification of thrombospondin type-1 repeats in ADAMTS-like 1/punctin-1 by C-mannosylation of tryptophan.	0:124	Post-translational modification of thrombospondin type-1 repeats in ADAMTS-like 1/punctin-1 by C-mannosylation of tryptophan.
19671700	3	103	theme	superfamily	448:458	arg1	feature					426:432	and a defining feature	411:432	feature	426:432	TSRs are especially numerous in and a defining feature of the ADAMTS superfamily.
19671700	2	104	located	present	330:336	arg2	WXXW					304:307	the sequence motif WXXW	285:307	the sequence motif WXXW	285:307	This post-translational modification typically occurs within the sequence motif WXXW, which is frequently present in thrombospondin type-1 repeats (TSRs).
19671700	2	104	located	present	330:336	arg1	repeats					363:369	thrombospondin type-1 repeats	341:369	thrombospondin type-1 repeats (TSRs)	341:376	This post-translational modification typically occurs within the sequence motif WXXW, which is frequently present in thrombospondin type-1 repeats (TSRs).
19671700	2	104	located	present	330:336	arg1	TSRs					372:375	TSRs	372:375	TSRs	372:375	This post-translational modification typically occurs within the sequence motif WXXW, which is frequently present in thrombospondin type-1 repeats (TSRs).
19671700	2	104	located	present	330:336	arg2	present					330:336	present	330:336	present	330:336	This post-translational modification typically occurs within the sequence motif WXXW, which is frequently present in thrombospondin type-1 repeats (TSRs).
19671700	0	105	theme	ADAMTS-like	68:78	arg1	1/punctin-1					80:90	ADAMTS-like 1/punctin-1	68:90	ADAMTS-like 1/punctin-1	68:90	Post-translational modification of thrombospondin type-1 repeats in ADAMTS-like 1/punctin-1 by C-mannosylation of tryptophan.
19671700	10	106	from	Replacement	1591:1601	arg1	TSR1					1635:1638	TSR1	1635:1638	TSR1	1635:1638	Replacement of mannosylated Trp residues in TSR1 with either Ala or Phe affected punctin secretion efficiency.
19671700	4	107	theme	ADAMTS-like	540:550	arg1	1/punctin-1					552:562	ADAMTS-like 1/punctin-1	540:562	ADAMTS-like 1/punctin-1	540:562	We investigated the presence and functional significance of C-mannosylation of ADAMTS-like 1/punctin-1, which contains four TSRs (two with predicted C-mannosylation sites), using mass spectrometry, metabolic labeling, site-directed mutagenesis, and expression in C-mannosylation-defective Chinese hamster ovary cell variants.
19671700	8	108	theme	CHO-K1	1434:1439	arg1	cells					1441:1445	CHO-K1 cells	1434:1445	CHO-K1 cells but not Lec35.1 cells	1434:1467	Metabolic labeling of CHO-K1 cells or Lec35.1 cells demonstrated incorporation of d-[2,6-(3)H]mannose in secreted punctin-1 from CHO-K1 cells but not Lec35.1 cells.
19671700	2	109	theme	post-translational	229:246	arg1	modification					248:259	This post-translational modification	224:259	This post-translational modification	224:259	This post-translational modification typically occurs within the sequence motif WXXW, which is frequently present in thrombospondin type-1 repeats (TSRs).
19671700	10	110	from	residues	1623:1630	arg1	TSR1					1635:1638	TSR1	1635:1638	TSR1	1635:1638	Replacement of mannosylated Trp residues in TSR1 with either Ala or Phe affected punctin secretion efficiency.
19671700	6	111	theme	modified	1186:1193	arg1	residues					1195:1202	the modified residues	1182:1202	the modified residues	1182:1202	Tandem mass spectrometry (MS/MS) and MS/MS/MS analysis demonstrated the characteristic cross-ring cleavage of C-mannose and identified the modified residues as Trp(39) and Trp(42).
19671700	8	112	theme	Lec35.1	1455:1461	arg1	cells					1463:1467	Lec35.1 cells	1455:1467	CHO-K1 cells but not Lec35.1 cells	1434:1467	Metabolic labeling of CHO-K1 cells or Lec35.1 cells demonstrated incorporation of d-[2,6-(3)H]mannose in secreted punctin-1 from CHO-K1 cells but not Lec35.1 cells.
19671700	4	113	contain	contains	571:578	arg2	TSRs					585:588	four TSRs	580:588	four TSRs (two with predicted C-mannosylation sites)	580:631	We investigated the presence and functional significance of C-mannosylation of ADAMTS-like 1/punctin-1, which contains four TSRs (two with predicted C-mannosylation sites), using mass spectrometry, metabolic labeling, site-directed mutagenesis, and expression in C-mannosylation-defective Chinese hamster ovary cell variants.
19671700	4	113	contain	contains	571:578	arg1	1/punctin-1					552:562	ADAMTS-like 1/punctin-1	540:562	ADAMTS-like 1/punctin-1	540:562	We investigated the presence and functional significance of C-mannosylation of ADAMTS-like 1/punctin-1, which contains four TSRs (two with predicted C-mannosylation sites), using mass spectrometry, metabolic labeling, site-directed mutagenesis, and expression in C-mannosylation-defective Chinese hamster ovary cell variants.
26165356	5	0	theme	PTM-deficient	799:811	arg1	mutants					830:836	PTM-deficient or PTM-mimicking mutants	799:836	PTM-deficient or PTM-mimicking mutants	799:836	By using a series of PTM-deficient or PTM-mimicking mutants, we further find that tubulin phosphorylation and acetylation play important roles in the control of microtubule assembly and stability.
26165356	6	1	theme	adenoviruses	1060:1071	arg1	transport					1047:1055	the retrograde transport	1032:1055	the retrograde transport of adenoviruses along microtubules	1032:1090	In addition, these tubulin PTMs have distinct effects on the retrograde transport of adenoviruses along microtubules.
26165356	5	2	theme	microtubule	939:949	arg1	assembly					951:958	microtubule assembly	939:958	microtubule assembly	939:958	By using a series of PTM-deficient or PTM-mimicking mutants, we further find that tubulin phosphorylation and acetylation play important roles in the control of microtubule assembly and stability.
26165356	2	3	from	PTMs	322:325	arg1	regulation					361:370	the regulation	357:370	the regulation of microtubule properties and functions	357:410	However, more conventional PTMs of tubulin and their roles in the regulation of microtubule properties and functions remain poorly defined.
26165356	0	4	theme	Tubulin	100:106	arg1	Modifications					83:95	Multiple Post-Translational Modifications	55:95	Multiple Post-Translational Modifications of Tubulin	55:106	Proteomic Profiling and Functional Characterization of Multiple Post-Translational Modifications of Tubulin.
26165356	2	5	from	roles	348:352	arg1	regulation					361:370	the regulation	357:370	the regulation of microtubule properties and functions	357:410	However, more conventional PTMs of tubulin and their roles in the regulation of microtubule properties and functions remain poorly defined.
26165356	5	6	theme	assembly	951:958	arg1	control					928:934	the control	924:934	the control of microtubule assembly and stability	924:972	By using a series of PTM-deficient or PTM-mimicking mutants, we further find that tubulin phosphorylation and acetylation play important roles in the control of microtubule assembly and stability.
26165356	4	7	theme	tubulin-targeted	601:616	arg1	analysis					618:625	Our tubulin-targeted analysis	597:625	Our tubulin-targeted analysis	597:625	Our tubulin-targeted analysis has identified 80 residues bearing single or multiple conventional PTMs including 24 novel PTM sites not covered in previous global proteomic surveys.
26165356	7	8	theme	functions	1261:1269	arg1	regulation					1213:1222	the regulation	1209:1222	the regulation of microtubule dynamics and cellular functions	1209:1269	These findings thus enlarge the repertoire of tubulin PTMs and foster our understanding of their versatile roles in the regulation of microtubule dynamics and cellular functions.
26165356	2	9	theme	conventional	309:320	arg1	PTMs					322:325	more conventional PTMs	304:325	more conventional PTMs of tubulin	304:336	However, more conventional PTMs of tubulin and their roles in the regulation of microtubule properties and functions remain poorly defined.
26165356	7	10	theme	cellular	1252:1259	arg1	functions					1261:1269	cellular functions	1252:1269	cellular functions	1252:1269	These findings thus enlarge the repertoire of tubulin PTMs and foster our understanding of their versatile roles in the regulation of microtubule dynamics and cellular functions.
26165356	7	11	from	regulation	1213:1222	arg1	understanding					1167:1179	our understanding	1163:1179	our understanding of their versatile roles in the regulation of microtubule dynamics and cellular functions	1163:1269	These findings thus enlarge the repertoire of tubulin PTMs and foster our understanding of their versatile roles in the regulation of microtubule dynamics and cellular functions.
26165356	4	12	theme	proteomic	759:767	arg1	surveys					769:775	previous global proteomic surveys	743:775	previous global proteomic surveys	743:775	Our tubulin-targeted analysis has identified 80 residues bearing single or multiple conventional PTMs including 24 novel PTM sites not covered in previous global proteomic surveys.
26165356	3	13	theme	phosphorylation	490:504	arg1	profiling					469:477	the comprehensive profiling	451:477	the comprehensive profiling of tubulin phosphorylation, acetylation, ubiquitylation, and O-GlcNAcylation in HeLa cells with a proteomic approach	451:594	Here, we report the comprehensive profiling of tubulin phosphorylation, acetylation, ubiquitylation, and O-GlcNAcylation in HeLa cells with a proteomic approach.
26165356	3	14	theme	HeLa	559:562	arg1	cells					564:568	HeLa cells	559:568	HeLa cells with a proteomic approach	559:594	Here, we report the comprehensive profiling of tubulin phosphorylation, acetylation, ubiquitylation, and O-GlcNAcylation in HeLa cells with a proteomic approach.
26165356	4	15	theme	PTM	718:720	arg1	sites					722:726	24 novel PTM sites	709:726	24 novel PTM sites not covered in previous global proteomic surveys	709:775	Our tubulin-targeted analysis has identified 80 residues bearing single or multiple conventional PTMs including 24 novel PTM sites not covered in previous global proteomic surveys.
26165356	5	16	theme	important	905:913	arg1	roles					915:919	important roles	905:919	important roles	905:919	By using a series of PTM-deficient or PTM-mimicking mutants, we further find that tubulin phosphorylation and acetylation play important roles in the control of microtubule assembly and stability.
26165356	7	17	theme	roles	1200:1204	arg1	understanding					1167:1179	our understanding	1163:1179	our understanding of their versatile roles in the regulation of microtubule dynamics and cellular functions	1163:1269	These findings thus enlarge the repertoire of tubulin PTMs and foster our understanding of their versatile roles in the regulation of microtubule dynamics and cellular functions.
26165356	7	18	theme	dynamics	1239:1246	arg1	regulation					1213:1222	the regulation	1209:1222	the regulation of microtubule dynamics and cellular functions	1209:1269	These findings thus enlarge the repertoire of tubulin PTMs and foster our understanding of their versatile roles in the regulation of microtubule dynamics and cellular functions.
26165356	3	19	theme	comprehensive	455:467	arg1	profiling					469:477	the comprehensive profiling	451:477	the comprehensive profiling of tubulin phosphorylation, acetylation, ubiquitylation, and O-GlcNAcylation in HeLa cells with a proteomic approach	451:594	Here, we report the comprehensive profiling of tubulin phosphorylation, acetylation, ubiquitylation, and O-GlcNAcylation in HeLa cells with a proteomic approach.
26165356	7	20	theme	microtubule	1227:1237	arg1	dynamics					1239:1246	microtubule dynamics	1227:1246	microtubule dynamics	1227:1246	These findings thus enlarge the repertoire of tubulin PTMs and foster our understanding of their versatile roles in the regulation of microtubule dynamics and cellular functions.
26165356	7	21	theme	tubulin	1139:1145	arg1	PTMs					1147:1150	tubulin PTMs	1139:1150	tubulin PTMs	1139:1150	These findings thus enlarge the repertoire of tubulin PTMs and foster our understanding of their versatile roles in the regulation of microtubule dynamics and cellular functions.
26165356	1	22	from	modifications	163:175	arg1	CTTs					288:291	CTTs	288:291	CTTs	288:291	Tubulin is known to undergo unique post-translational modifications (PTMs), such as detyrosination and polyglutamylation, particularly in the unstructured carboxy-terminal tails (CTTs).
26165356	1	22	from	modifications	163:175	arg1	tails					281:285	the unstructured carboxy-terminal tails	247:285	the unstructured carboxy-terminal tails (CTTs)	247:292	Tubulin is known to undergo unique post-translational modifications (PTMs), such as detyrosination and polyglutamylation, particularly in the unstructured carboxy-terminal tails (CTTs).
26165356	2	23	theme	functions	402:410	arg1	regulation					361:370	the regulation	357:370	the regulation of microtubule properties and functions	357:410	However, more conventional PTMs of tubulin and their roles in the regulation of microtubule properties and functions remain poorly defined.
26165356	0	24	theme	Proteomic	0:8	arg1	Profiling					10:18	Proteomic Profiling	0:18	Proteomic Profiling	0:18	Proteomic Profiling and Functional Characterization of Multiple Post-Translational Modifications of Tubulin.
26165356	7	25	from	roles	1200:1204	arg1	regulation					1213:1222	the regulation	1209:1222	the regulation of microtubule dynamics and cellular functions	1209:1269	These findings thus enlarge the repertoire of tubulin PTMs and foster our understanding of their versatile roles in the regulation of microtubule dynamics and cellular functions.
26165356	7	26	theme	PTMs	1147:1150	arg1	repertoire					1125:1134	the repertoire	1121:1134	the repertoire of tubulin PTMs	1121:1150	These findings thus enlarge the repertoire of tubulin PTMs and foster our understanding of their versatile roles in the regulation of microtubule dynamics and cellular functions.
26165356	7	26	theme	PTMs	1147:1150	arg1	PTMs					1147:1150	tubulin PTMs	1139:1150	tubulin PTMs	1139:1150	These findings thus enlarge the repertoire of tubulin PTMs and foster our understanding of their versatile roles in the regulation of microtubule dynamics and cellular functions.
26165356	2	27	theme	tubulin	330:336	arg1	roles					348:352	their roles	342:352	their roles in the regulation of microtubule properties and functions	342:410	However, more conventional PTMs of tubulin and their roles in the regulation of microtubule properties and functions remain poorly defined.
26165356	2	27	theme	tubulin	330:336	arg1	PTMs					322:325	more conventional PTMs	304:325	more conventional PTMs of tubulin	304:336	However, more conventional PTMs of tubulin and their roles in the regulation of microtubule properties and functions remain poorly defined.
26165356	4	28	theme	novel	712:716	arg1	sites					722:726	24 novel PTM sites	709:726	24 novel PTM sites not covered in previous global proteomic surveys	709:775	Our tubulin-targeted analysis has identified 80 residues bearing single or multiple conventional PTMs including 24 novel PTM sites not covered in previous global proteomic surveys.
26165356	0	29	theme	Functional	24:33	arg1	Characterization					35:50	Functional Characterization	24:50	Functional Characterization	24:50	Proteomic Profiling and Functional Characterization of Multiple Post-Translational Modifications of Tubulin.
26165356	6	30	theme	distinct	1012:1019	arg1	effects					1021:1027	distinct effects	1012:1027	distinct effects	1012:1027	In addition, these tubulin PTMs have distinct effects on the retrograde transport of adenoviruses along microtubules.
26165356	3	31	theme	proteomic	577:585	arg1	approach					587:594	a proteomic approach	575:594	a proteomic approach	575:594	Here, we report the comprehensive profiling of tubulin phosphorylation, acetylation, ubiquitylation, and O-GlcNAcylation in HeLa cells with a proteomic approach.
26165356	3	32	theme	tubulin	482:488	arg1	phosphorylation					490:504	tubulin phosphorylation	482:504	tubulin phosphorylation	482:504	Here, we report the comprehensive profiling of tubulin phosphorylation, acetylation, ubiquitylation, and O-GlcNAcylation in HeLa cells with a proteomic approach.
26165356	5	33	theme	tubulin	860:866	arg1	phosphorylation					868:882	tubulin phosphorylation	860:882	tubulin phosphorylation	860:882	By using a series of PTM-deficient or PTM-mimicking mutants, we further find that tubulin phosphorylation and acetylation play important roles in the control of microtubule assembly and stability.
26165356	2	34	theme	properties	387:396	arg1	regulation					361:370	the regulation	357:370	the regulation of microtubule properties and functions	357:410	However, more conventional PTMs of tubulin and their roles in the regulation of microtubule properties and functions remain poorly defined.
26165356	5	35	theme	PTM-mimicking	816:828	arg1	mutants					830:836	PTM-deficient or PTM-mimicking mutants	799:836	PTM-deficient or PTM-mimicking mutants	799:836	By using a series of PTM-deficient or PTM-mimicking mutants, we further find that tubulin phosphorylation and acetylation play important roles in the control of microtubule assembly and stability.
26165356	3	36	theme	ubiquitylation	520:533	arg1	profiling					469:477	the comprehensive profiling	451:477	the comprehensive profiling of tubulin phosphorylation, acetylation, ubiquitylation, and O-GlcNAcylation in HeLa cells with a proteomic approach	451:594	Here, we report the comprehensive profiling of tubulin phosphorylation, acetylation, ubiquitylation, and O-GlcNAcylation in HeLa cells with a proteomic approach.
26165356	7	37	theme	versatile	1190:1198	arg1	roles					1200:1204	their versatile roles	1184:1204	their versatile roles in the regulation of microtubule dynamics and cellular functions	1184:1269	These findings thus enlarge the repertoire of tubulin PTMs and foster our understanding of their versatile roles in the regulation of microtubule dynamics and cellular functions.
26165356	3	38	with	cells	564:568	arg1	approach					587:594	a proteomic approach	575:594	a proteomic approach	575:594	Here, we report the comprehensive profiling of tubulin phosphorylation, acetylation, ubiquitylation, and O-GlcNAcylation in HeLa cells with a proteomic approach.
26165356	6	39	theme	tubulin	994:1000	arg1	PTMs					1002:1005	these tubulin PTMs	988:1005	these tubulin PTMs	988:1005	In addition, these tubulin PTMs have distinct effects on the retrograde transport of adenoviruses along microtubules.
26165356	5	40	theme	mutants	830:836	arg1	series					789:794	a series	787:794	a series of PTM-deficient or PTM-mimicking mutants	787:836	By using a series of PTM-deficient or PTM-mimicking mutants, we further find that tubulin phosphorylation and acetylation play important roles in the control of microtubule assembly and stability.
26165356	6	41	theme	retrograde	1036:1045	arg1	transport					1047:1055	the retrograde transport	1032:1055	the retrograde transport of adenoviruses along microtubules	1032:1090	In addition, these tubulin PTMs have distinct effects on the retrograde transport of adenoviruses along microtubules.
26165356	4	42	theme	single	662:667	arg1	sites					722:726	24 novel PTM sites	709:726	24 novel PTM sites not covered in previous global proteomic surveys	709:775	Our tubulin-targeted analysis has identified 80 residues bearing single or multiple conventional PTMs including 24 novel PTM sites not covered in previous global proteomic surveys.
26165356	4	42	theme	single	662:667	arg1	PTMs					694:697	single or multiple conventional PTMs	662:697	single or multiple conventional PTMs including 24 novel PTM sites not covered in previous global proteomic surveys	662:775	Our tubulin-targeted analysis has identified 80 residues bearing single or multiple conventional PTMs including 24 novel PTM sites not covered in previous global proteomic surveys.
26165356	3	43	from	profiling	469:477	arg1	cells					564:568	HeLa cells	559:568	HeLa cells with a proteomic approach	559:594	Here, we report the comprehensive profiling of tubulin phosphorylation, acetylation, ubiquitylation, and O-GlcNAcylation in HeLa cells with a proteomic approach.
26165356	4	44	theme	conventional	681:692	arg1	sites					722:726	24 novel PTM sites	709:726	24 novel PTM sites not covered in previous global proteomic surveys	709:775	Our tubulin-targeted analysis has identified 80 residues bearing single or multiple conventional PTMs including 24 novel PTM sites not covered in previous global proteomic surveys.
26165356	4	44	theme	conventional	681:692	arg1	PTMs					694:697	single or multiple conventional PTMs	662:697	single or multiple conventional PTMs including 24 novel PTM sites not covered in previous global proteomic surveys	662:775	Our tubulin-targeted analysis has identified 80 residues bearing single or multiple conventional PTMs including 24 novel PTM sites not covered in previous global proteomic surveys.
26165356	0	45	theme	Post-Translational	64:81	arg1	Modifications					83:95	Multiple Post-Translational Modifications	55:95	Multiple Post-Translational Modifications of Tubulin	55:106	Proteomic Profiling and Functional Characterization of Multiple Post-Translational Modifications of Tubulin.
26165356	7	46	from	understanding	1167:1179	arg1	regulation					1213:1222	the regulation	1209:1222	the regulation of microtubule dynamics and cellular functions	1209:1269	These findings thus enlarge the repertoire of tubulin PTMs and foster our understanding of their versatile roles in the regulation of microtubule dynamics and cellular functions.
26165356	4	47	theme	global	752:757	arg1	surveys					769:775	previous global proteomic surveys	743:775	previous global proteomic surveys	743:775	Our tubulin-targeted analysis has identified 80 residues bearing single or multiple conventional PTMs including 24 novel PTM sites not covered in previous global proteomic surveys.
26165356	0	48	theme	Multiple	55:62	arg1	Modifications					83:95	Multiple Post-Translational Modifications	55:95	Multiple Post-Translational Modifications of Tubulin	55:106	Proteomic Profiling and Functional Characterization of Multiple Post-Translational Modifications of Tubulin.
26165356	1	49	theme	unique	137:142	arg1	detyrosination					193:206	detyrosination	193:206	detyrosination	193:206	Tubulin is known to undergo unique post-translational modifications (PTMs), such as detyrosination and polyglutamylation, particularly in the unstructured carboxy-terminal tails (CTTs).
26165356	1	49	theme	unique	137:142	arg1	PTMs					178:181	PTMs	178:181	PTMs	178:181	Tubulin is known to undergo unique post-translational modifications (PTMs), such as detyrosination and polyglutamylation, particularly in the unstructured carboxy-terminal tails (CTTs).
26165356	1	49	theme	unique	137:142	arg1	modifications					163:175	unique post-translational modifications	137:175	unique post-translational modifications (PTMs)	137:182	Tubulin is known to undergo unique post-translational modifications (PTMs), such as detyrosination and polyglutamylation, particularly in the unstructured carboxy-terminal tails (CTTs).
26165356	1	49	theme	unique	137:142	arg1	polyglutamylation					212:228	polyglutamylation	212:228	polyglutamylation	212:228	Tubulin is known to undergo unique post-translational modifications (PTMs), such as detyrosination and polyglutamylation, particularly in the unstructured carboxy-terminal tails (CTTs).
26165356	5	50	theme	stability	964:972	arg1	control					928:934	the control	924:934	the control of microtubule assembly and stability	924:972	By using a series of PTM-deficient or PTM-mimicking mutants, we further find that tubulin phosphorylation and acetylation play important roles in the control of microtubule assembly and stability.
26165356	6	51	contain	have	1007:1010	arg2	effects					1021:1027	distinct effects	1012:1027	distinct effects	1012:1027	In addition, these tubulin PTMs have distinct effects on the retrograde transport of adenoviruses along microtubules.
26165356	6	51	contain	have	1007:1010	arg1	PTMs					1002:1005	these tubulin PTMs	988:1005	these tubulin PTMs	988:1005	In addition, these tubulin PTMs have distinct effects on the retrograde transport of adenoviruses along microtubules.
26165356	1	52	theme	post-translational	144:161	arg1	detyrosination					193:206	detyrosination	193:206	detyrosination	193:206	Tubulin is known to undergo unique post-translational modifications (PTMs), such as detyrosination and polyglutamylation, particularly in the unstructured carboxy-terminal tails (CTTs).
26165356	1	52	theme	post-translational	144:161	arg1	PTMs					178:181	PTMs	178:181	PTMs	178:181	Tubulin is known to undergo unique post-translational modifications (PTMs), such as detyrosination and polyglutamylation, particularly in the unstructured carboxy-terminal tails (CTTs).
26165356	1	52	theme	post-translational	144:161	arg1	modifications					163:175	unique post-translational modifications	137:175	unique post-translational modifications (PTMs)	137:182	Tubulin is known to undergo unique post-translational modifications (PTMs), such as detyrosination and polyglutamylation, particularly in the unstructured carboxy-terminal tails (CTTs).
26165356	1	52	theme	post-translational	144:161	arg1	polyglutamylation					212:228	polyglutamylation	212:228	polyglutamylation	212:228	Tubulin is known to undergo unique post-translational modifications (PTMs), such as detyrosination and polyglutamylation, particularly in the unstructured carboxy-terminal tails (CTTs).
26165356	3	53	theme	acetylation	507:517	arg1	profiling					469:477	the comprehensive profiling	451:477	the comprehensive profiling of tubulin phosphorylation, acetylation, ubiquitylation, and O-GlcNAcylation in HeLa cells with a proteomic approach	451:594	Here, we report the comprehensive profiling of tubulin phosphorylation, acetylation, ubiquitylation, and O-GlcNAcylation in HeLa cells with a proteomic approach.
26165356	1	54	theme	unstructured	251:262	arg1	CTTs					288:291	CTTs	288:291	CTTs	288:291	Tubulin is known to undergo unique post-translational modifications (PTMs), such as detyrosination and polyglutamylation, particularly in the unstructured carboxy-terminal tails (CTTs).
26165356	1	54	theme	unstructured	251:262	arg1	tails					281:285	the unstructured carboxy-terminal tails	247:285	the unstructured carboxy-terminal tails (CTTs)	247:292	Tubulin is known to undergo unique post-translational modifications (PTMs), such as detyrosination and polyglutamylation, particularly in the unstructured carboxy-terminal tails (CTTs).
26165356	4	55	theme	multiple	672:679	arg1	sites					722:726	24 novel PTM sites	709:726	24 novel PTM sites not covered in previous global proteomic surveys	709:775	Our tubulin-targeted analysis has identified 80 residues bearing single or multiple conventional PTMs including 24 novel PTM sites not covered in previous global proteomic surveys.
26165356	4	55	theme	multiple	672:679	arg1	PTMs					694:697	single or multiple conventional PTMs	662:697	single or multiple conventional PTMs including 24 novel PTM sites not covered in previous global proteomic surveys	662:775	Our tubulin-targeted analysis has identified 80 residues bearing single or multiple conventional PTMs including 24 novel PTM sites not covered in previous global proteomic surveys.
26165356	3	56	theme	O-GlcNAcylation	540:554	arg1	profiling					469:477	the comprehensive profiling	451:477	the comprehensive profiling of tubulin phosphorylation, acetylation, ubiquitylation, and O-GlcNAcylation in HeLa cells with a proteomic approach	451:594	Here, we report the comprehensive profiling of tubulin phosphorylation, acetylation, ubiquitylation, and O-GlcNAcylation in HeLa cells with a proteomic approach.
26165356	1	57	theme	carboxy-terminal	264:279	arg1	CTTs					288:291	CTTs	288:291	CTTs	288:291	Tubulin is known to undergo unique post-translational modifications (PTMs), such as detyrosination and polyglutamylation, particularly in the unstructured carboxy-terminal tails (CTTs).
26165356	1	57	theme	carboxy-terminal	264:279	arg1	tails					281:285	the unstructured carboxy-terminal tails	247:285	the unstructured carboxy-terminal tails (CTTs)	247:292	Tubulin is known to undergo unique post-translational modifications (PTMs), such as detyrosination and polyglutamylation, particularly in the unstructured carboxy-terminal tails (CTTs).
26165356	0	58	theme	Modifications	83:95	arg1	Profiling					10:18	Proteomic Profiling	0:18	Proteomic Profiling	0:18	Proteomic Profiling and Functional Characterization of Multiple Post-Translational Modifications of Tubulin.
26165356	0	58	theme	Modifications	83:95	arg1	Characterization					35:50	Functional Characterization	24:50	Functional Characterization	24:50	Proteomic Profiling and Functional Characterization of Multiple Post-Translational Modifications of Tubulin.
26165356	2	59	theme	microtubule	375:385	arg1	properties					387:396	microtubule properties	375:396	microtubule properties	375:396	However, more conventional PTMs of tubulin and their roles in the regulation of microtubule properties and functions remain poorly defined.
26165356	4	60	theme	previous	743:750	arg1	surveys					769:775	previous global proteomic surveys	743:775	previous global proteomic surveys	743:775	Our tubulin-targeted analysis has identified 80 residues bearing single or multiple conventional PTMs including 24 novel PTM sites not covered in previous global proteomic surveys.
15476821	2	0	theme	X-ray	468:472	arg1	structure					482:490	the X-ray crystal structure	464:490	the X-ray crystal structure of the extracellular domain of human DPPX determined at 3.0A resolution	464:562	Here we report the X-ray crystal structure of the extracellular domain of human DPPX determined at 3.0A resolution.
15476821	6	1	theme	protein	955:961	arg1	DPP-IV					963:968	the related protein DPP-IV	943:968	the related protein DPP-IV	943:968	The dimeric structure of DPPX is highly homologous to the related protein DPP-IV.
15476821	7	2	theme	serine	1100:1105	arg1	presence					1074:1081	the presence	1070:1081	the presence of an additional serine	1070:1105	Comparison of the active sites of DPPX and DPP-IV reveals loss of the catalytic serine residue but the presence of an additional serine near the "active" site.
15476821	6	3	theme	dimeric	893:899	arg1	homologous					929:938	homologous	929:938	homologous	929:938	The dimeric structure of DPPX is highly homologous to the related protein DPP-IV.
15476821	6	3	theme	dimeric	893:899	arg1	structure					901:909	The dimeric structure	889:909	The dimeric structure of DPPX	889:917	The dimeric structure of DPPX is highly homologous to the related protein DPP-IV.
15476821	1	4	theme	channel	235:241	arg1	Kv4					243:245	the voltage-gated potassium channel Kv4	207:245	the voltage-gated potassium channel Kv4	207:245	It has recently been reported that dipeptidyl aminopeptidase X (DPPX) interacts with the voltage-gated potassium channel Kv4 and that co-expression of DPPX together with Kv4 pore forming alpha-subunits, and potassium channel interacting proteins (KChIPs), reconstitutes properties of native A-type potassium channels in vitro.
15476821	2	5	theme	DPPX	529:532	arg1	DPPX					529:532	human DPPX	523:532	human DPPX	523:532	Here we report the X-ray crystal structure of the extracellular domain of human DPPX determined at 3.0A resolution.
15476821	2	5	theme	DPPX	529:532	arg1	domain					513:518	the extracellular domain	495:518	the extracellular domain of human DPPX determined at 3.0A resolution	495:562	Here we report the X-ray crystal structure of the extracellular domain of human DPPX determined at 3.0A resolution.
15476821	3	6	theme	histidine	671:679	arg1	state					662:666	the protonation state	646:666	the protonation state of histidine	646:679	This structure reveals the potential for a surface electrostatic change based on the protonation state of histidine.
15476821	1	7	theme	potassium	420:428	arg1	channels					430:437	native A-type potassium channels	406:437	native A-type potassium channels	406:437	It has recently been reported that dipeptidyl aminopeptidase X (DPPX) interacts with the voltage-gated potassium channel Kv4 and that co-expression of DPPX together with Kv4 pore forming alpha-subunits, and potassium channel interacting proteins (KChIPs), reconstitutes properties of native A-type potassium channels in vitro.
15476821	4	8	theme	Subtle	682:687	arg1	changes					689:695	Subtle changes	682:695	Subtle changes in extracellular pH	682:715	Subtle changes in extracellular pH might modulate the interaction of DPPX with Kv4.2 and possibly with other proteins.
15476821	2	9	theme	domain	513:518	arg1	structure					482:490	the X-ray crystal structure	464:490	the X-ray crystal structure of the extracellular domain of human DPPX determined at 3.0A resolution	464:562	Here we report the X-ray crystal structure of the extracellular domain of human DPPX determined at 3.0A resolution.
15476821	1	10	theme	potassium	329:337	arg1	KChIPs					369:374	KChIPs	369:374	KChIPs	369:374	It has recently been reported that dipeptidyl aminopeptidase X (DPPX) interacts with the voltage-gated potassium channel Kv4 and that co-expression of DPPX together with Kv4 pore forming alpha-subunits, and potassium channel interacting proteins (KChIPs), reconstitutes properties of native A-type potassium channels in vitro.
15476821	1	10	theme	potassium	329:337	arg1	proteins					359:366	potassium channel interacting proteins	329:366	potassium channel interacting proteins (KChIPs)	329:375	It has recently been reported that dipeptidyl aminopeptidase X (DPPX) interacts with the voltage-gated potassium channel Kv4 and that co-expression of DPPX together with Kv4 pore forming alpha-subunits, and potassium channel interacting proteins (KChIPs), reconstitutes properties of native A-type potassium channels in vitro.
15476821	1	11	theme	channels	430:437	arg1	properties					392:401	properties	392:401	properties of native A-type potassium channels	392:437	It has recently been reported that dipeptidyl aminopeptidase X (DPPX) interacts with the voltage-gated potassium channel Kv4 and that co-expression of DPPX together with Kv4 pore forming alpha-subunits, and potassium channel interacting proteins (KChIPs), reconstitutes properties of native A-type potassium channels in vitro.
15476821	2	12	theme	extracellular	499:511	arg1	DPPX					529:532	human DPPX	523:532	human DPPX	523:532	Here we report the X-ray crystal structure of the extracellular domain of human DPPX determined at 3.0A resolution.
15476821	2	12	theme	extracellular	499:511	arg1	domain					513:518	the extracellular domain	495:518	the extracellular domain of human DPPX determined at 3.0A resolution	495:562	Here we report the X-ray crystal structure of the extracellular domain of human DPPX determined at 3.0A resolution.
15476821	1	13	theme	channel	339:345	arg1	KChIPs					369:374	KChIPs	369:374	KChIPs	369:374	It has recently been reported that dipeptidyl aminopeptidase X (DPPX) interacts with the voltage-gated potassium channel Kv4 and that co-expression of DPPX together with Kv4 pore forming alpha-subunits, and potassium channel interacting proteins (KChIPs), reconstitutes properties of native A-type potassium channels in vitro.
15476821	1	13	theme	channel	339:345	arg1	proteins					359:366	potassium channel interacting proteins	329:366	potassium channel interacting proteins (KChIPs)	329:375	It has recently been reported that dipeptidyl aminopeptidase X (DPPX) interacts with the voltage-gated potassium channel Kv4 and that co-expression of DPPX together with Kv4 pore forming alpha-subunits, and potassium channel interacting proteins (KChIPs), reconstitutes properties of native A-type potassium channels in vitro.
15476821	7	14	theme	additional	1089:1098	arg1	serine					1100:1105	an additional serine	1086:1105	an additional serine	1086:1105	Comparison of the active sites of DPPX and DPP-IV reveals loss of the catalytic serine residue but the presence of an additional serine near the "active" site.
15476821	4	15	theme	DPPX	751:754	arg1	interaction					736:746	the interaction	732:746	the interaction of DPPX with Kv4.2 and possibly with other proteins	732:798	Subtle changes in extracellular pH might modulate the interaction of DPPX with Kv4.2 and possibly with other proteins.
15476821	0	16	theme	dipeptidyl	88:97	arg1	family					114:119	the dipeptidyl aminopeptidase family	84:119	the dipeptidyl aminopeptidase family	84:119	Structure of a human A-type potassium channel interacting protein DPPX, a member of the dipeptidyl aminopeptidase family.
15476821	1	17	theme	interacting	347:357	arg1	KChIPs					369:374	KChIPs	369:374	KChIPs	369:374	It has recently been reported that dipeptidyl aminopeptidase X (DPPX) interacts with the voltage-gated potassium channel Kv4 and that co-expression of DPPX together with Kv4 pore forming alpha-subunits, and potassium channel interacting proteins (KChIPs), reconstitutes properties of native A-type potassium channels in vitro.
15476821	1	17	theme	interacting	347:357	arg1	proteins					359:366	potassium channel interacting proteins	329:366	potassium channel interacting proteins (KChIPs)	329:375	It has recently been reported that dipeptidyl aminopeptidase X (DPPX) interacts with the voltage-gated potassium channel Kv4 and that co-expression of DPPX together with Kv4 pore forming alpha-subunits, and potassium channel interacting proteins (KChIPs), reconstitutes properties of native A-type potassium channels in vitro.
15476821	5	18	theme	potassium	862:870	arg1	channel					872:878	the voltage-gated potassium channel	844:878	the voltage-gated potassium channel complex	844:886	We propose models of DPPX interaction with the voltage-gated potassium channel complex.
15476821	8	19	theme	canonical	1197:1205	arg1	proteases					1214:1222	canonical serine proteases	1197:1222	canonical serine proteases	1197:1222	However, the arrangement of residues is inconsistent with that of canonical serine proteases and DPPX is unlikely to function as a protease (dipeptidyl aminopeptidase).
15476821	7	20	theme	active	1117:1122	arg1	site					1125:1128	the "active" site	1112:1128	the "active" site	1112:1128	Comparison of the active sites of DPPX and DPP-IV reveals loss of the catalytic serine residue but the presence of an additional serine near the "active" site.
15476821	7	21	theme	residue	1058:1064	arg1	loss					1029:1032	loss	1029:1032	loss of the catalytic serine residue	1029:1064	Comparison of the active sites of DPPX and DPP-IV reveals loss of the catalytic serine residue but the presence of an additional serine near the "active" site.
15476821	1	22	theme	dipeptidyl	157:166	arg1	DPPX					186:189	DPPX	186:189	DPPX	186:189	It has recently been reported that dipeptidyl aminopeptidase X (DPPX) interacts with the voltage-gated potassium channel Kv4 and that co-expression of DPPX together with Kv4 pore forming alpha-subunits, and potassium channel interacting proteins (KChIPs), reconstitutes properties of native A-type potassium channels in vitro.
15476821	1	22	theme	dipeptidyl	157:166	arg1	X					183:183	dipeptidyl aminopeptidase X	157:183	dipeptidyl aminopeptidase X (DPPX)	157:190	It has recently been reported that dipeptidyl aminopeptidase X (DPPX) interacts with the voltage-gated potassium channel Kv4 and that co-expression of DPPX together with Kv4 pore forming alpha-subunits, and potassium channel interacting proteins (KChIPs), reconstitutes properties of native A-type potassium channels in vitro.
15476821	1	23	theme	aminopeptidase	168:181	arg1	DPPX					186:189	DPPX	186:189	DPPX	186:189	It has recently been reported that dipeptidyl aminopeptidase X (DPPX) interacts with the voltage-gated potassium channel Kv4 and that co-expression of DPPX together with Kv4 pore forming alpha-subunits, and potassium channel interacting proteins (KChIPs), reconstitutes properties of native A-type potassium channels in vitro.
15476821	1	23	theme	aminopeptidase	168:181	arg1	X					183:183	dipeptidyl aminopeptidase X	157:183	dipeptidyl aminopeptidase X (DPPX)	157:190	It has recently been reported that dipeptidyl aminopeptidase X (DPPX) interacts with the voltage-gated potassium channel Kv4 and that co-expression of DPPX together with Kv4 pore forming alpha-subunits, and potassium channel interacting proteins (KChIPs), reconstitutes properties of native A-type potassium channels in vitro.
15476821	3	24	theme	protonation	650:660	arg1	state					662:666	the protonation state	646:666	the protonation state of histidine	646:679	This structure reveals the potential for a surface electrostatic change based on the protonation state of histidine.
15476821	7	25	theme	catalytic	1041:1049	arg1	residue					1058:1064	the catalytic serine residue	1037:1064	the catalytic serine residue	1037:1064	Comparison of the active sites of DPPX and DPP-IV reveals loss of the catalytic serine residue but the presence of an additional serine near the "active" site.
15476821	7	26	theme	serine	1051:1056	arg1	residue					1058:1064	the catalytic serine residue	1037:1064	the catalytic serine residue	1037:1064	Comparison of the active sites of DPPX and DPP-IV reveals loss of the catalytic serine residue but the presence of an additional serine near the "active" site.
15476821	5	27	theme	channel	872:878	arg1	complex					880:886	the voltage-gated potassium channel complex	844:886	the voltage-gated potassium channel complex	844:886	We propose models of DPPX interaction with the voltage-gated potassium channel complex.
15476821	0	28	theme	human	15:19	arg1	channel					38:44	a human A-type potassium channel	13:44	a human A-type potassium channel	13:44	Structure of a human A-type potassium channel interacting protein DPPX, a member of the dipeptidyl aminopeptidase family.
15476821	0	29	theme	family	114:119	arg1	DPPX					66:69	protein DPPX	58:69	protein DPPX	58:69	Structure of a human A-type potassium channel interacting protein DPPX, a member of the dipeptidyl aminopeptidase family.
15476821	0	29	theme	family	114:119	arg1	member					74:79	a member	72:79	a member of the dipeptidyl aminopeptidase family	72:119	Structure of a human A-type potassium channel interacting protein DPPX, a member of the dipeptidyl aminopeptidase family.
15476821	8	30	theme	residues	1159:1166	arg1	inconsistent					1171:1182	inconsistent	1171:1182	inconsistent	1171:1182	However, the arrangement of residues is inconsistent with that of canonical serine proteases and DPPX is unlikely to function as a protease (dipeptidyl aminopeptidase).
15476821	8	30	theme	residues	1159:1166	arg1	arrangement					1144:1154	the arrangement	1140:1154	the arrangement of residues	1140:1166	However, the arrangement of residues is inconsistent with that of canonical serine proteases and DPPX is unlikely to function as a protease (dipeptidyl aminopeptidase).
15476821	1	31	theme	DPPX	273:276	arg1	co-expression					256:268	co-expression	256:268	co-expression of DPPX together with Kv4 pore forming alpha-subunits, and potassium channel interacting proteins (KChIPs),	256:376	It has recently been reported that dipeptidyl aminopeptidase X (DPPX) interacts with the voltage-gated potassium channel Kv4 and that co-expression of DPPX together with Kv4 pore forming alpha-subunits, and potassium channel interacting proteins (KChIPs), reconstitutes properties of native A-type potassium channels in vitro.
15476821	0	32	theme	aminopeptidase	99:112	arg1	family					114:119	the dipeptidyl aminopeptidase family	84:119	the dipeptidyl aminopeptidase family	84:119	Structure of a human A-type potassium channel interacting protein DPPX, a member of the dipeptidyl aminopeptidase family.
15476821	8	33	theme	dipeptidyl	1272:1281	arg1	protease					1262:1269	a protease	1260:1269	a protease (dipeptidyl aminopeptidase)	1260:1297	However, the arrangement of residues is inconsistent with that of canonical serine proteases and DPPX is unlikely to function as a protease (dipeptidyl aminopeptidase).
15476821	8	33	theme	dipeptidyl	1272:1281	arg1	aminopeptidase					1283:1296	dipeptidyl aminopeptidase	1272:1296	dipeptidyl aminopeptidase	1272:1296	However, the arrangement of residues is inconsistent with that of canonical serine proteases and DPPX is unlikely to function as a protease (dipeptidyl aminopeptidase).
15476821	6	34	theme	DPPX	914:917	arg1	homologous					929:938	homologous	929:938	homologous	929:938	The dimeric structure of DPPX is highly homologous to the related protein DPP-IV.
15476821	6	34	theme	DPPX	914:917	arg1	structure					901:909	The dimeric structure	889:909	The dimeric structure of DPPX	889:917	The dimeric structure of DPPX is highly homologous to the related protein DPP-IV.
15476821	5	35	theme	DPPX	822:825	arg1	interaction					827:837	DPPX interaction	822:837	DPPX interaction with the voltage-gated potassium channel complex	822:886	We propose models of DPPX interaction with the voltage-gated potassium channel complex.
15476821	0	36	theme	potassium	28:36	arg1	channel					38:44	a human A-type potassium channel	13:44	a human A-type potassium channel	13:44	Structure of a human A-type potassium channel interacting protein DPPX, a member of the dipeptidyl aminopeptidase family.
15476821	6	37	theme	related	947:953	arg1	DPP-IV					963:968	the related protein DPP-IV	943:968	the related protein DPP-IV	943:968	The dimeric structure of DPPX is highly homologous to the related protein DPP-IV.
15476821	2	38	theme	human	523:527	arg1	DPPX					529:532	human DPPX	523:532	human DPPX	523:532	Here we report the X-ray crystal structure of the extracellular domain of human DPPX determined at 3.0A resolution.
15476821	8	39	theme	serine	1207:1212	arg1	proteases					1214:1222	canonical serine proteases	1197:1222	canonical serine proteases	1197:1222	However, the arrangement of residues is inconsistent with that of canonical serine proteases and DPPX is unlikely to function as a protease (dipeptidyl aminopeptidase).
15476821	5	40	theme	interaction	827:837	arg1	models					812:817	models	812:817	models of DPPX interaction with the voltage-gated potassium channel complex	812:886	We propose models of DPPX interaction with the voltage-gated potassium channel complex.
15476821	0	41	theme	A-type	21:26	arg1	channel					38:44	a human A-type potassium channel	13:44	a human A-type potassium channel	13:44	Structure of a human A-type potassium channel interacting protein DPPX, a member of the dipeptidyl aminopeptidase family.
15476821	7	42	theme	"	1123:1123	arg1	site					1125:1128	the "active" site	1112:1128	the "active" site	1112:1128	Comparison of the active sites of DPPX and DPP-IV reveals loss of the catalytic serine residue but the presence of an additional serine near the "active" site.
15476821	3	43	theme	electrostatic	616:628	arg1	change					630:635	a surface electrostatic change	606:635	a surface electrostatic change based on the protonation state of histidine	606:679	This structure reveals the potential for a surface electrostatic change based on the protonation state of histidine.
15476821	4	44	with	interaction	736:746	arg1	proteins					791:798	other proteins	785:798	other proteins	785:798	Subtle changes in extracellular pH might modulate the interaction of DPPX with Kv4.2 and possibly with other proteins.
15476821	4	44	with	interaction	736:746	arg1	Kv4.2					761:765	Kv4.2	761:765	Kv4.2	761:765	Subtle changes in extracellular pH might modulate the interaction of DPPX with Kv4.2 and possibly with other proteins.
15476821	7	45	theme	DPPX	1005:1008	arg1	DPP-IV					1014:1019	DPP-IV	1014:1019	DPP-IV	1014:1019	Comparison of the active sites of DPPX and DPP-IV reveals loss of the catalytic serine residue but the presence of an additional serine near the "active" site.
15476821	7	45	theme	DPPX	1005:1008	arg1	DPPX					1005:1008	DPPX	1005:1008	DPPX	1005:1008	Comparison of the active sites of DPPX and DPP-IV reveals loss of the catalytic serine residue but the presence of an additional serine near the "active" site.
15476821	7	45	theme	DPPX	1005:1008	arg1	sites					996:1000	the active sites	985:1000	the active sites of DPPX and DPP-IV	985:1019	Comparison of the active sites of DPPX and DPP-IV reveals loss of the catalytic serine residue but the presence of an additional serine near the "active" site.
15476821	1	46	theme	Kv4	292:294	arg1	alpha-subunits					309:322	Kv4 pore forming alpha-subunits	292:322	Kv4 pore forming alpha-subunits	292:322	It has recently been reported that dipeptidyl aminopeptidase X (DPPX) interacts with the voltage-gated potassium channel Kv4 and that co-expression of DPPX together with Kv4 pore forming alpha-subunits, and potassium channel interacting proteins (KChIPs), reconstitutes properties of native A-type potassium channels in vitro.
15476821	2	47	theme	crystal	474:480	arg1	structure					482:490	the X-ray crystal structure	464:490	the X-ray crystal structure of the extracellular domain of human DPPX determined at 3.0A resolution	464:562	Here we report the X-ray crystal structure of the extracellular domain of human DPPX determined at 3.0A resolution.
15476821	7	48	theme	DPP-IV	1014:1019	arg1	DPP-IV					1014:1019	DPP-IV	1014:1019	DPP-IV	1014:1019	Comparison of the active sites of DPPX and DPP-IV reveals loss of the catalytic serine residue but the presence of an additional serine near the "active" site.
15476821	7	48	theme	DPP-IV	1014:1019	arg1	DPPX					1005:1008	DPPX	1005:1008	DPPX	1005:1008	Comparison of the active sites of DPPX and DPP-IV reveals loss of the catalytic serine residue but the presence of an additional serine near the "active" site.
15476821	7	48	theme	DPP-IV	1014:1019	arg1	sites					996:1000	the active sites	985:1000	the active sites of DPPX and DPP-IV	985:1019	Comparison of the active sites of DPPX and DPP-IV reveals loss of the catalytic serine residue but the presence of an additional serine near the "active" site.
15476821	4	49	theme	extracellular	700:712	arg1	pH					714:715	extracellular pH	700:715	extracellular pH	700:715	Subtle changes in extracellular pH might modulate the interaction of DPPX with Kv4.2 and possibly with other proteins.
15476821	0	50	theme	channel	38:44	arg1	Structure					0:8	Structure	0:8	Structure of a human A-type potassium channel	0:44	Structure of a human A-type potassium channel interacting protein DPPX, a member of the dipeptidyl aminopeptidase family.
15476821	1	51	theme	pore	296:299	arg1	alpha-subunits					309:322	Kv4 pore forming alpha-subunits	292:322	Kv4 pore forming alpha-subunits	292:322	It has recently been reported that dipeptidyl aminopeptidase X (DPPX) interacts with the voltage-gated potassium channel Kv4 and that co-expression of DPPX together with Kv4 pore forming alpha-subunits, and potassium channel interacting proteins (KChIPs), reconstitutes properties of native A-type potassium channels in vitro.
15476821	5	52	with	interaction	827:837	arg1	complex					880:886	the voltage-gated potassium channel complex	844:886	the voltage-gated potassium channel complex	844:886	We propose models of DPPX interaction with the voltage-gated potassium channel complex.
15476821	7	53	theme	sites	996:1000	arg1	Comparison					971:980	Comparison	971:980	Comparison of the active sites of DPPX and DPP-IV	971:1019	Comparison of the active sites of DPPX and DPP-IV reveals loss of the catalytic serine residue but the presence of an additional serine near the "active" site.
15476821	1	54	theme	forming	301:307	arg1	alpha-subunits					309:322	Kv4 pore forming alpha-subunits	292:322	Kv4 pore forming alpha-subunits	292:322	It has recently been reported that dipeptidyl aminopeptidase X (DPPX) interacts with the voltage-gated potassium channel Kv4 and that co-expression of DPPX together with Kv4 pore forming alpha-subunits, and potassium channel interacting proteins (KChIPs), reconstitutes properties of native A-type potassium channels in vitro.
15476821	2	55	theme	3.0A	548:551	arg1	resolution					553:562	3.0A resolution	548:562	3.0A resolution	548:562	Here we report the X-ray crystal structure of the extracellular domain of human DPPX determined at 3.0A resolution.
15476821	1	56	theme	native	406:411	arg1	channels					430:437	native A-type potassium channels	406:437	native A-type potassium channels	406:437	It has recently been reported that dipeptidyl aminopeptidase X (DPPX) interacts with the voltage-gated potassium channel Kv4 and that co-expression of DPPX together with Kv4 pore forming alpha-subunits, and potassium channel interacting proteins (KChIPs), reconstitutes properties of native A-type potassium channels in vitro.
15476821	3	57	theme	surface	608:614	arg1	change					630:635	a surface electrostatic change	606:635	a surface electrostatic change based on the protonation state of histidine	606:679	This structure reveals the potential for a surface electrostatic change based on the protonation state of histidine.
15476821	1	58	theme	A-type	413:418	arg1	channels					430:437	native A-type potassium channels	406:437	native A-type potassium channels	406:437	It has recently been reported that dipeptidyl aminopeptidase X (DPPX) interacts with the voltage-gated potassium channel Kv4 and that co-expression of DPPX together with Kv4 pore forming alpha-subunits, and potassium channel interacting proteins (KChIPs), reconstitutes properties of native A-type potassium channels in vitro.
15476821	7	59	theme	active	989:994	arg1	DPP-IV					1014:1019	DPP-IV	1014:1019	DPP-IV	1014:1019	Comparison of the active sites of DPPX and DPP-IV reveals loss of the catalytic serine residue but the presence of an additional serine near the "active" site.
15476821	7	59	theme	active	989:994	arg1	DPPX					1005:1008	DPPX	1005:1008	DPPX	1005:1008	Comparison of the active sites of DPPX and DPP-IV reveals loss of the catalytic serine residue but the presence of an additional serine near the "active" site.
15476821	7	59	theme	active	989:994	arg1	sites					996:1000	the active sites	985:1000	the active sites of DPPX and DPP-IV	985:1019	Comparison of the active sites of DPPX and DPP-IV reveals loss of the catalytic serine residue but the presence of an additional serine near the "active" site.
15476821	5	60	theme	voltage-gated	848:860	arg1	channel					872:878	the voltage-gated potassium channel	844:878	the voltage-gated potassium channel complex	844:886	We propose models of DPPX interaction with the voltage-gated potassium channel complex.
15476821	1	61	theme	voltage-gated	211:223	arg1	channel					235:241	the voltage-gated potassium channel	207:241	the voltage-gated potassium channel Kv4	207:245	It has recently been reported that dipeptidyl aminopeptidase X (DPPX) interacts with the voltage-gated potassium channel Kv4 and that co-expression of DPPX together with Kv4 pore forming alpha-subunits, and potassium channel interacting proteins (KChIPs), reconstitutes properties of native A-type potassium channels in vitro.
15476821	0	62	theme	protein	58:64	arg1	DPPX					66:69	protein DPPX	58:69	protein DPPX	58:69	Structure of a human A-type potassium channel interacting protein DPPX, a member of the dipeptidyl aminopeptidase family.
15476821	0	62	theme	protein	58:64	arg1	member					74:79	a member	72:79	a member of the dipeptidyl aminopeptidase family	72:119	Structure of a human A-type potassium channel interacting protein DPPX, a member of the dipeptidyl aminopeptidase family.
15476821	4	63	theme	other	785:789	arg1	proteins					791:798	other proteins	785:798	other proteins	785:798	Subtle changes in extracellular pH might modulate the interaction of DPPX with Kv4.2 and possibly with other proteins.
15476821	8	64	with	inconsistent	1171:1182	arg1	that					1189:1192	that	1189:1192	that	1189:1192	However, the arrangement of residues is inconsistent with that of canonical serine proteases and DPPX is unlikely to function as a protease (dipeptidyl aminopeptidase).
15476821	4	65	from	changes	689:695	arg1	pH					714:715	extracellular pH	700:715	extracellular pH	700:715	Subtle changes in extracellular pH might modulate the interaction of DPPX with Kv4.2 and possibly with other proteins.
15476821	1	66	theme	potassium	225:233	arg1	channel					235:241	the voltage-gated potassium channel	207:241	the voltage-gated potassium channel Kv4	207:245	It has recently been reported that dipeptidyl aminopeptidase X (DPPX) interacts with the voltage-gated potassium channel Kv4 and that co-expression of DPPX together with Kv4 pore forming alpha-subunits, and potassium channel interacting proteins (KChIPs), reconstitutes properties of native A-type potassium channels in vitro.
20068230	2	0	theme	cycle	501:505	arg1	functions					507:515	its cell cycle functions	492:515	its cell cycle functions	492:515	Overexpression of the enzyme that adds O-GlcNAc to target proteins, O-GlcNAc transferase (OGT), perturbs cytokinesis and promotes polyploidy, but the molecular targets of OGT that are important for its cell cycle functions are unknown.
20068230	6	1	theme	inhibitory	947:956	arg1	phosphorylation					958:972	the inhibitory phosphorylation	943:972	the inhibitory phosphorylation of cyclin-dependent kinase 1 (CDK1)	943:1008	Forced overexpression of OGT increased the inhibitory phosphorylation of cyclin-dependent kinase 1 (CDK1) and reduced the phosphorylation of CDK1 target proteins.
20068230	1	2	theme	ubiquitous	182:191	arg1	addition					113:120	the addition	109:120	the addition of O-linked beta-N-acetylglucosamine (O-GlcNAcylation)	109:175	Like phosphorylation, the addition of O-linked beta-N-acetylglucosamine (O-GlcNAcylation) is a ubiquitous, reversible process that modifies serine and threonine residues on nuclear and cytoplasmic proteins.
20068230	1	2	theme	ubiquitous	182:191	arg1	process					205:211	a ubiquitous, reversible process	180:211	a ubiquitous, reversible process that modifies serine and threonine residues on nuclear and cytoplasmic proteins	180:291	Like phosphorylation, the addition of O-linked beta-N-acetylglucosamine (O-GlcNAcylation) is a ubiquitous, reversible process that modifies serine and threonine residues on nuclear and cytoplasmic proteins.
20068230	2	3	theme	cell	496:499	arg1	functions					507:515	its cell cycle functions	492:515	its cell cycle functions	492:515	Overexpression of the enzyme that adds O-GlcNAc to target proteins, O-GlcNAc transferase (OGT), perturbs cytokinesis and promotes polyploidy, but the molecular targets of OGT that are important for its cell cycle functions are unknown.
20068230	4	4	theme	known	709:713	arg1	sites					731:735	known phosphorylation sites	709:735	known phosphorylation sites	709:735	Many of these O-GlcNAcylation sites are either identical to known phosphorylation sites or in close proximity to them.
20068230	9	5	theme	proteins	1509:1516	arg1	phosphorylation					1490:1504	phosphorylation	1490:1504	phosphorylation	1490:1504	The data not only illustrate the crosstalk between O-GlcNAcylation and phosphorylation of proteins that are regulators of crucial signaling pathways but also uncover a mechanism for the role of O-GlcNAcylation in regulation of cell division.
20068230	9	5	theme	proteins	1509:1516	arg1	O-GlcNAcylation					1470:1484	O-GlcNAcylation	1470:1484	O-GlcNAcylation	1470:1484	The data not only illustrate the crosstalk between O-GlcNAcylation and phosphorylation of proteins that are regulators of crucial signaling pathways but also uncover a mechanism for the role of O-GlcNAcylation in regulation of cell division.
20068230	7	6	theme	upstream	1149:1156	arg1	kinase					1158:1163	its upstream kinase	1145:1163	its upstream kinase	1145:1163	The increased phosphorylation of CDK1 is explained by increased activation of its upstream kinase, MYT1, and by a concomitant reduction in the transcript for the CDK1 phosphatase, CDC25C.
20068230	7	6	theme	upstream	1149:1156	arg1	MYT1					1166:1169	MYT1	1166:1169	MYT1	1166:1169	The increased phosphorylation of CDK1 is explained by increased activation of its upstream kinase, MYT1, and by a concomitant reduction in the transcript for the CDK1 phosphatase, CDC25C.
20068230	3	7	theme	O-GlcNAc	571:578	arg1	sites					580:584	141 previously unknown O-GlcNAc sites	548:584	141 previously unknown O-GlcNAc sites on proteins that function in spindle assembly and cytokinesis	548:646	Here, we identify 141 previously unknown O-GlcNAc sites on proteins that function in spindle assembly and cytokinesis.
20068230	7	8	theme	CDK1	1229:1232	arg1	CDC25C					1247:1252	CDC25C	1247:1252	CDC25C	1247:1252	The increased phosphorylation of CDK1 is explained by increased activation of its upstream kinase, MYT1, and by a concomitant reduction in the transcript for the CDK1 phosphatase, CDC25C.
20068230	7	8	theme	CDK1	1229:1232	arg1	phosphatase					1234:1244	the CDK1 phosphatase	1225:1244	the CDK1 phosphatase	1225:1244	The increased phosphorylation of CDK1 is explained by increased activation of its upstream kinase, MYT1, and by a concomitant reduction in the transcript for the CDK1 phosphatase, CDC25C.
20068230	6	9	theme	OGT	929:931	arg1	overexpression					911:924	Forced overexpression	904:924	Forced overexpression of OGT	904:931	Forced overexpression of OGT increased the inhibitory phosphorylation of cyclin-dependent kinase 1 (CDK1) and reduced the phosphorylation of CDK1 target proteins.
20068230	7	10	theme	kinase	1158:1163	arg1	activation					1131:1140	increased activation	1121:1140	increased activation of its upstream kinase, MYT1	1121:1169	The increased phosphorylation of CDK1 is explained by increased activation of its upstream kinase, MYT1, and by a concomitant reduction in the transcript for the CDK1 phosphatase, CDC25C.
20068230	8	11	theme	kinase	1366:1371	arg1	expression					1320:1329	messenger RNA expression	1306:1329	messenger RNA expression	1306:1329	OGT overexpression also caused a reduction in both messenger RNA expression and protein abundance of Polo-like kinase 1, which is upstream of both MYT1 and CDC25C.
20068230	8	11	theme	kinase	1366:1371	arg1	abundance					1343:1351	protein abundance	1335:1351	protein abundance	1335:1351	OGT overexpression also caused a reduction in both messenger RNA expression and protein abundance of Polo-like kinase 1, which is upstream of both MYT1 and CDC25C.
20068230	4	12	theme	phosphorylation	715:729	arg1	sites					731:735	known phosphorylation sites	709:735	known phosphorylation sites	709:735	Many of these O-GlcNAcylation sites are either identical to known phosphorylation sites or in close proximity to them.
20068230	8	13	theme	Polo-like	1356:1364	arg1	kinase					1366:1371	Polo-like kinase 1	1356:1373	Polo-like kinase 1	1356:1373	OGT overexpression also caused a reduction in both messenger RNA expression and protein abundance of Polo-like kinase 1, which is upstream of both MYT1 and CDC25C.
20068230	7	14	from	reduction	1193:1201	arg1	transcript					1210:1219	the transcript	1206:1219	the transcript for the CDK1 phosphatase, CDC25C	1206:1252	The increased phosphorylation of CDK1 is explained by increased activation of its upstream kinase, MYT1, and by a concomitant reduction in the transcript for the CDK1 phosphatase, CDC25C.
20068230	2	15	theme	enzyme	316:321	arg1	Overexpression					294:307	Overexpression	294:307	Overexpression of the enzyme that adds O-GlcNAc to target proteins, O-GlcNAc transferase (OGT),	294:388	Overexpression of the enzyme that adds O-GlcNAc to target proteins, O-GlcNAc transferase (OGT), perturbs cytokinesis and promotes polyploidy, but the molecular targets of OGT that are important for its cell cycle functions are unknown.
20068230	4	16	theme	sites	679:683	arg1	sites					679:683	these O-GlcNAcylation sites	657:683	these O-GlcNAcylation sites	657:683	Many of these O-GlcNAcylation sites are either identical to known phosphorylation sites or in close proximity to them.
20068230	4	16	theme	sites	679:683	arg1	Many					649:652	Many	649:652	Many	649:652	Many of these O-GlcNAcylation sites are either identical to known phosphorylation sites or in close proximity to them.
20068230	0	17	theme	Extensive	0:8	arg1	crosstalk					10:18	Extensive crosstalk	0:18	Extensive crosstalk between O-GlcNAcylation and phosphorylation	0:62	Extensive crosstalk between O-GlcNAcylation and phosphorylation regulates cytokinesis.
20068230	4	18	theme	O-GlcNAcylation	663:677	arg1	sites					679:683	these O-GlcNAcylation sites	657:683	these O-GlcNAcylation sites	657:683	Many of these O-GlcNAcylation sites are either identical to known phosphorylation sites or in close proximity to them.
20068230	9	19	theme	signaling	1549:1557	arg1	pathways					1559:1566	crucial signaling pathways	1541:1566	crucial signaling pathways	1541:1566	The data not only illustrate the crosstalk between O-GlcNAcylation and phosphorylation of proteins that are regulators of crucial signaling pathways but also uncover a mechanism for the role of O-GlcNAcylation in regulation of cell division.
20068230	6	20	theme	Forced	904:909	arg1	overexpression					911:924	Forced overexpression	904:924	Forced overexpression of OGT	904:931	Forced overexpression of OGT increased the inhibitory phosphorylation of cyclin-dependent kinase 1 (CDK1) and reduced the phosphorylation of CDK1 target proteins.
20068230	7	21	theme	increased	1121:1129	arg1	activation					1131:1140	increased activation	1121:1140	increased activation of its upstream kinase, MYT1	1121:1169	The increased phosphorylation of CDK1 is explained by increased activation of its upstream kinase, MYT1, and by a concomitant reduction in the transcript for the CDK1 phosphatase, CDC25C.
20068230	1	22	dep	ubiquitous	182:191	arg1	reversible					194:203	reversible	194:203	reversible	194:203	Like phosphorylation, the addition of O-linked beta-N-acetylglucosamine (O-GlcNAcylation) is a ubiquitous, reversible process that modifies serine and threonine residues on nuclear and cytoplasmic proteins.
20068230	2	23	theme	OGT	465:467	arg1	important					478:486	important	478:486	important	478:486	Overexpression of the enzyme that adds O-GlcNAc to target proteins, O-GlcNAc transferase (OGT), perturbs cytokinesis and promotes polyploidy, but the molecular targets of OGT that are important for its cell cycle functions are unknown.
20068230	2	23	theme	OGT	465:467	arg1	targets					454:460	the molecular targets	440:460	the molecular targets of OGT that are important for its cell cycle functions	440:515	Overexpression of the enzyme that adds O-GlcNAc to target proteins, O-GlcNAc transferase (OGT), perturbs cytokinesis and promotes polyploidy, but the molecular targets of OGT that are important for its cell cycle functions are unknown.
20068230	2	23	theme	OGT	465:467	arg1	unknown					521:527	unknown	521:527	unknown	521:527	Overexpression of the enzyme that adds O-GlcNAc to target proteins, O-GlcNAc transferase (OGT), perturbs cytokinesis and promotes polyploidy, but the molecular targets of OGT that are important for its cell cycle functions are unknown.
20068230	2	24	theme	target	345:350	arg1	proteins					352:359	target proteins	345:359	target proteins	345:359	Overexpression of the enzyme that adds O-GlcNAc to target proteins, O-GlcNAc transferase (OGT), perturbs cytokinesis and promotes polyploidy, but the molecular targets of OGT that are important for its cell cycle functions are unknown.
20068230	5	25	theme	key	842:844	arg1	proteins					846:853	key proteins	842:853	key proteins associated with the mitotic spindle and midbody	842:901	Furthermore, we found that O-GlcNAcylation altered the phosphorylation of key proteins associated with the mitotic spindle and midbody.
20068230	1	26	dep	serine	227:232	arg1	residues					248:255	residues	248:255	residues	248:255	Like phosphorylation, the addition of O-linked beta-N-acetylglucosamine (O-GlcNAcylation) is a ubiquitous, reversible process that modifies serine and threonine residues on nuclear and cytoplasmic proteins.
20068230	3	27	theme	unknown	563:569	arg1	sites					580:584	141 previously unknown O-GlcNAc sites	548:584	141 previously unknown O-GlcNAc sites on proteins that function in spindle assembly and cytokinesis	548:646	Here, we identify 141 previously unknown O-GlcNAc sites on proteins that function in spindle assembly and cytokinesis.
20068230	2	28	theme	molecular	444:452	arg1	important					478:486	important	478:486	important	478:486	Overexpression of the enzyme that adds O-GlcNAc to target proteins, O-GlcNAc transferase (OGT), perturbs cytokinesis and promotes polyploidy, but the molecular targets of OGT that are important for its cell cycle functions are unknown.
20068230	2	28	theme	molecular	444:452	arg1	targets					454:460	the molecular targets	440:460	the molecular targets of OGT that are important for its cell cycle functions	440:515	Overexpression of the enzyme that adds O-GlcNAc to target proteins, O-GlcNAc transferase (OGT), perturbs cytokinesis and promotes polyploidy, but the molecular targets of OGT that are important for its cell cycle functions are unknown.
20068230	2	28	theme	molecular	444:452	arg1	unknown					521:527	unknown	521:527	unknown	521:527	Overexpression of the enzyme that adds O-GlcNAc to target proteins, O-GlcNAc transferase (OGT), perturbs cytokinesis and promotes polyploidy, but the molecular targets of OGT that are important for its cell cycle functions are unknown.
20068230	5	29	theme	proteins	846:853	arg1	phosphorylation					823:837	the phosphorylation	819:837	the phosphorylation of key proteins associated with the mitotic spindle and midbody	819:901	Furthermore, we found that O-GlcNAcylation altered the phosphorylation of key proteins associated with the mitotic spindle and midbody.
20068230	8	30	theme	MYT1	1402:1405	arg1	upstream					1385:1392	upstream	1385:1392	upstream	1385:1392	OGT overexpression also caused a reduction in both messenger RNA expression and protein abundance of Polo-like kinase 1, which is upstream of both MYT1 and CDC25C.
20068230	8	30	theme	MYT1	1402:1405	arg1	reduction					1288:1296	a reduction	1286:1296	a reduction	1286:1296	OGT overexpression also caused a reduction in both messenger RNA expression and protein abundance of Polo-like kinase 1, which is upstream of both MYT1 and CDC25C.
20068230	1	31	theme	O-linked	125:132	arg1	O-GlcNAcylation					160:174	O-GlcNAcylation	160:174	O-GlcNAcylation	160:174	Like phosphorylation, the addition of O-linked beta-N-acetylglucosamine (O-GlcNAcylation) is a ubiquitous, reversible process that modifies serine and threonine residues on nuclear and cytoplasmic proteins.
20068230	1	31	theme	O-linked	125:132	arg1	beta-N-acetylglucosamine					134:157	O-linked beta-N-acetylglucosamine	125:157	O-linked beta-N-acetylglucosamine (O-GlcNAcylation)	125:175	Like phosphorylation, the addition of O-linked beta-N-acetylglucosamine (O-GlcNAcylation) is a ubiquitous, reversible process that modifies serine and threonine residues on nuclear and cytoplasmic proteins.
20068230	9	32	theme	pathways	1559:1566	arg1	proteins					1509:1516	proteins	1509:1516	proteins that are regulators of crucial signaling pathways	1509:1566	The data not only illustrate the crosstalk between O-GlcNAcylation and phosphorylation of proteins that are regulators of crucial signaling pathways but also uncover a mechanism for the role of O-GlcNAcylation in regulation of cell division.
20068230	9	32	theme	pathways	1559:1566	arg1	regulators					1527:1536	regulators	1527:1536	regulators of crucial signaling pathways	1527:1566	The data not only illustrate the crosstalk between O-GlcNAcylation and phosphorylation of proteins that are regulators of crucial signaling pathways but also uncover a mechanism for the role of O-GlcNAcylation in regulation of cell division.
20068230	8	33	theme	messenger	1306:1314	arg1	RNA					1316:1318	messenger RNA	1306:1318	messenger RNA expression	1306:1329	OGT overexpression also caused a reduction in both messenger RNA expression and protein abundance of Polo-like kinase 1, which is upstream of both MYT1 and CDC25C.
20068230	7	34	theme	CDK1	1100:1103	arg1	phosphorylation					1081:1095	The increased phosphorylation	1067:1095	The increased phosphorylation of CDK1	1067:1103	The increased phosphorylation of CDK1 is explained by increased activation of its upstream kinase, MYT1, and by a concomitant reduction in the transcript for the CDK1 phosphatase, CDC25C.
20068230	9	35	theme	O-GlcNAcylation	1613:1627	arg1	role					1605:1608	the role	1601:1608	the role of O-GlcNAcylation in regulation of cell division	1601:1658	The data not only illustrate the crosstalk between O-GlcNAcylation and phosphorylation of proteins that are regulators of crucial signaling pathways but also uncover a mechanism for the role of O-GlcNAcylation in regulation of cell division.
20068230	9	36	theme	division	1651:1658	arg1	regulation					1632:1641	regulation	1632:1641	regulation of cell division	1632:1658	The data not only illustrate the crosstalk between O-GlcNAcylation and phosphorylation of proteins that are regulators of crucial signaling pathways but also uncover a mechanism for the role of O-GlcNAcylation in regulation of cell division.
20068230	7	37	theme	concomitant	1181:1191	arg1	reduction					1193:1201	a concomitant reduction	1179:1201	a concomitant reduction in the transcript for the CDK1 phosphatase, CDC25C	1179:1252	The increased phosphorylation of CDK1 is explained by increased activation of its upstream kinase, MYT1, and by a concomitant reduction in the transcript for the CDK1 phosphatase, CDC25C.
20068230	1	38	from	threonine	238:246	arg1	proteins					284:291	nuclear and cytoplasmic proteins	260:291	nuclear and cytoplasmic proteins	260:291	Like phosphorylation, the addition of O-linked beta-N-acetylglucosamine (O-GlcNAcylation) is a ubiquitous, reversible process that modifies serine and threonine residues on nuclear and cytoplasmic proteins.
20068230	5	39	theme	mitotic	875:881	arg1	spindle					883:889	the mitotic spindle	871:889	the mitotic spindle	871:889	Furthermore, we found that O-GlcNAcylation altered the phosphorylation of key proteins associated with the mitotic spindle and midbody.
20068230	8	40	theme	RNA	1316:1318	arg1	expression					1320:1329	messenger RNA expression	1306:1329	messenger RNA expression	1306:1329	OGT overexpression also caused a reduction in both messenger RNA expression and protein abundance of Polo-like kinase 1, which is upstream of both MYT1 and CDC25C.
20068230	6	41	theme	kinase	994:999	arg1	phosphorylation					958:972	the inhibitory phosphorylation	943:972	the inhibitory phosphorylation of cyclin-dependent kinase 1 (CDK1)	943:1008	Forced overexpression of OGT increased the inhibitory phosphorylation of cyclin-dependent kinase 1 (CDK1) and reduced the phosphorylation of CDK1 target proteins.
20068230	1	42	theme	beta-N-acetylglucosamine	134:157	arg1	addition					113:120	the addition	109:120	the addition of O-linked beta-N-acetylglucosamine (O-GlcNAcylation)	109:175	Like phosphorylation, the addition of O-linked beta-N-acetylglucosamine (O-GlcNAcylation) is a ubiquitous, reversible process that modifies serine and threonine residues on nuclear and cytoplasmic proteins.
20068230	1	42	theme	beta-N-acetylglucosamine	134:157	arg1	process					205:211	a ubiquitous, reversible process	180:211	a ubiquitous, reversible process that modifies serine and threonine residues on nuclear and cytoplasmic proteins	180:291	Like phosphorylation, the addition of O-linked beta-N-acetylglucosamine (O-GlcNAcylation) is a ubiquitous, reversible process that modifies serine and threonine residues on nuclear and cytoplasmic proteins.
20068230	6	43	theme	cyclin-dependent	977:992	arg1	kinase					994:999	cyclin-dependent kinase 1	977:1001	cyclin-dependent kinase 1 (CDK1)	977:1008	Forced overexpression of OGT increased the inhibitory phosphorylation of cyclin-dependent kinase 1 (CDK1) and reduced the phosphorylation of CDK1 target proteins.
20068230	6	43	theme	cyclin-dependent	977:992	arg1	CDK1					1004:1007	CDK1	1004:1007	CDK1	1004:1007	Forced overexpression of OGT increased the inhibitory phosphorylation of cyclin-dependent kinase 1 (CDK1) and reduced the phosphorylation of CDK1 target proteins.
20068230	8	44	theme	CDC25C	1411:1416	arg1	upstream					1385:1392	upstream	1385:1392	upstream	1385:1392	OGT overexpression also caused a reduction in both messenger RNA expression and protein abundance of Polo-like kinase 1, which is upstream of both MYT1 and CDC25C.
20068230	8	44	theme	CDC25C	1411:1416	arg1	reduction					1288:1296	a reduction	1286:1296	a reduction	1286:1296	OGT overexpression also caused a reduction in both messenger RNA expression and protein abundance of Polo-like kinase 1, which is upstream of both MYT1 and CDC25C.
20068230	1	45	from	serine	227:232	arg1	proteins					284:291	nuclear and cytoplasmic proteins	260:291	nuclear and cytoplasmic proteins	260:291	Like phosphorylation, the addition of O-linked beta-N-acetylglucosamine (O-GlcNAcylation) is a ubiquitous, reversible process that modifies serine and threonine residues on nuclear and cytoplasmic proteins.
20068230	4	46	theme	close	743:747	arg1	proximity					749:757	close proximity	743:757	close proximity to them	743:765	Many of these O-GlcNAcylation sites are either identical to known phosphorylation sites or in close proximity to them.
20068230	4	47	dep	either	689:694	arg1	identical					696:704	identical	696:704	identical	696:704	Many of these O-GlcNAcylation sites are either identical to known phosphorylation sites or in close proximity to them.
20068230	6	48	theme	proteins	1057:1064	arg1	phosphorylation					1026:1040	the phosphorylation	1022:1040	the phosphorylation of CDK1 target proteins	1022:1064	Forced overexpression of OGT increased the inhibitory phosphorylation of cyclin-dependent kinase 1 (CDK1) and reduced the phosphorylation of CDK1 target proteins.
20068230	2	49	theme	O-GlcNAc	362:369	arg1	transferase					371:381	O-GlcNAc transferase	362:381	O-GlcNAc transferase (OGT)	362:387	Overexpression of the enzyme that adds O-GlcNAc to target proteins, O-GlcNAc transferase (OGT), perturbs cytokinesis and promotes polyploidy, but the molecular targets of OGT that are important for its cell cycle functions are unknown.
20068230	2	49	theme	O-GlcNAc	362:369	arg1	enzyme					316:321	the enzyme	312:321	the enzyme that adds O-GlcNAc to target proteins	312:359	Overexpression of the enzyme that adds O-GlcNAc to target proteins, O-GlcNAc transferase (OGT), perturbs cytokinesis and promotes polyploidy, but the molecular targets of OGT that are important for its cell cycle functions are unknown.
20068230	2	49	theme	O-GlcNAc	362:369	arg1	OGT					384:386	OGT	384:386	OGT	384:386	Overexpression of the enzyme that adds O-GlcNAc to target proteins, O-GlcNAc transferase (OGT), perturbs cytokinesis and promotes polyploidy, but the molecular targets of OGT that are important for its cell cycle functions are unknown.
20068230	9	50	from	role	1605:1608	arg1	regulation					1632:1641	regulation	1632:1641	regulation of cell division	1632:1658	The data not only illustrate the crosstalk between O-GlcNAcylation and phosphorylation of proteins that are regulators of crucial signaling pathways but also uncover a mechanism for the role of O-GlcNAcylation in regulation of cell division.
20068230	7	51	theme	increased	1071:1079	arg1	phosphorylation					1081:1095	The increased phosphorylation	1067:1095	The increased phosphorylation of CDK1	1067:1103	The increased phosphorylation of CDK1 is explained by increased activation of its upstream kinase, MYT1, and by a concomitant reduction in the transcript for the CDK1 phosphatase, CDC25C.
20068230	9	52	theme	cell	1646:1649	arg1	division					1651:1658	cell division	1646:1658	cell division	1646:1658	The data not only illustrate the crosstalk between O-GlcNAcylation and phosphorylation of proteins that are regulators of crucial signaling pathways but also uncover a mechanism for the role of O-GlcNAcylation in regulation of cell division.
20068230	9	53	theme	crucial	1541:1547	arg1	pathways					1559:1566	crucial signaling pathways	1541:1566	crucial signaling pathways	1541:1566	The data not only illustrate the crosstalk between O-GlcNAcylation and phosphorylation of proteins that are regulators of crucial signaling pathways but also uncover a mechanism for the role of O-GlcNAcylation in regulation of cell division.
20068230	3	54	from	sites	580:584	arg1	proteins					589:596	proteins	589:596	proteins that function in spindle assembly and cytokinesis	589:646	Here, we identify 141 previously unknown O-GlcNAc sites on proteins that function in spindle assembly and cytokinesis.
20068230	1	55	theme	nuclear	260:266	arg1	proteins					284:291	nuclear and cytoplasmic proteins	260:291	nuclear and cytoplasmic proteins	260:291	Like phosphorylation, the addition of O-linked beta-N-acetylglucosamine (O-GlcNAcylation) is a ubiquitous, reversible process that modifies serine and threonine residues on nuclear and cytoplasmic proteins.
20068230	3	56	theme	spindle	615:621	arg1	assembly					623:630	spindle assembly	615:630	spindle assembly	615:630	Here, we identify 141 previously unknown O-GlcNAc sites on proteins that function in spindle assembly and cytokinesis.
20068230	8	57	theme	OGT	1255:1257	arg1	overexpression					1259:1272	OGT overexpression	1255:1272	OGT overexpression	1255:1272	OGT overexpression also caused a reduction in both messenger RNA expression and protein abundance of Polo-like kinase 1, which is upstream of both MYT1 and CDC25C.
20068230	6	58	theme	target	1050:1055	arg1	proteins					1057:1064	CDK1 target proteins	1045:1064	CDK1 target proteins	1045:1064	Forced overexpression of OGT increased the inhibitory phosphorylation of cyclin-dependent kinase 1 (CDK1) and reduced the phosphorylation of CDK1 target proteins.
20068230	1	59	link	O-linked	125:132	arg1	O-GlcNAcylation					160:174	O-GlcNAcylation	160:174	O-GlcNAcylation	160:174	Like phosphorylation, the addition of O-linked beta-N-acetylglucosamine (O-GlcNAcylation) is a ubiquitous, reversible process that modifies serine and threonine residues on nuclear and cytoplasmic proteins.
20068230	1	59	link	O-linked	125:132	arg1	beta-N-acetylglucosamine					134:157	O-linked beta-N-acetylglucosamine	125:157	O-linked beta-N-acetylglucosamine (O-GlcNAcylation)	125:175	Like phosphorylation, the addition of O-linked beta-N-acetylglucosamine (O-GlcNAcylation) is a ubiquitous, reversible process that modifies serine and threonine residues on nuclear and cytoplasmic proteins.
20068230	6	60	theme	CDK1	1045:1048	arg1	proteins					1057:1064	CDK1 target proteins	1045:1064	CDK1 target proteins	1045:1064	Forced overexpression of OGT increased the inhibitory phosphorylation of cyclin-dependent kinase 1 (CDK1) and reduced the phosphorylation of CDK1 target proteins.
20068230	8	61	from	reduction	1288:1296	arg1	expression					1320:1329	messenger RNA expression	1306:1329	messenger RNA expression	1306:1329	OGT overexpression also caused a reduction in both messenger RNA expression and protein abundance of Polo-like kinase 1, which is upstream of both MYT1 and CDC25C.
20068230	8	61	from	reduction	1288:1296	arg1	abundance					1343:1351	protein abundance	1335:1351	protein abundance	1335:1351	OGT overexpression also caused a reduction in both messenger RNA expression and protein abundance of Polo-like kinase 1, which is upstream of both MYT1 and CDC25C.
20068230	8	62	theme	protein	1335:1341	arg1	abundance					1343:1351	protein abundance	1335:1351	protein abundance	1335:1351	OGT overexpression also caused a reduction in both messenger RNA expression and protein abundance of Polo-like kinase 1, which is upstream of both MYT1 and CDC25C.
20068230	1	63	theme	cytoplasmic	272:282	arg1	proteins					284:291	nuclear and cytoplasmic proteins	260:291	nuclear and cytoplasmic proteins	260:291	Like phosphorylation, the addition of O-linked beta-N-acetylglucosamine (O-GlcNAcylation) is a ubiquitous, reversible process that modifies serine and threonine residues on nuclear and cytoplasmic proteins.
22371497	9	0	from	threonine	1387:1395	arg1	phosphorylation					1342:1356	mitosis-specific phosphorylation	1325:1356	mitosis-specific phosphorylation at serine 10, serine 28, and threonine 32	1325:1398	Furthermore, increased O-GlcNAcylation was observed to reduce mitosis-specific phosphorylation at serine 10, serine 28, and threonine 32.
22371497	4	1	dep	histones	758:765	arg1	histones					758:765	all four core nucleosomal histones	732:765	all four core nucleosomal histones (H2A, H2B, H3, and H4)	732:788	A recent study also found that all four core nucleosomal histones (H2A, H2B, H3, and H4) are modified with O-GlcNAc, although no specific sites on H3 were reported.
22371497	4	1	dep	histones	758:765	arg1	H3					778:779	H3	778:779	H3	778:779	A recent study also found that all four core nucleosomal histones (H2A, H2B, H3, and H4) are modified with O-GlcNAc, although no specific sites on H3 were reported.
22371497	4	1	dep	histones	758:765	arg1	H4					786:787	H4	786:787	H4	786:787	A recent study also found that all four core nucleosomal histones (H2A, H2B, H3, and H4) are modified with O-GlcNAc, although no specific sites on H3 were reported.
22371497	4	1	dep	histones	758:765	arg1	H2B					773:775	H2B	773:775	H2B	773:775	A recent study also found that all four core nucleosomal histones (H2A, H2B, H3, and H4) are modified with O-GlcNAc, although no specific sites on H3 were reported.
22371497	4	1	dep	histones	758:765	arg1	H2A					768:770	H2A	768:770	H2A	768:770	A recent study also found that all four core nucleosomal histones (H2A, H2B, H3, and H4) are modified with O-GlcNAc, although no specific sites on H3 were reported.
22371497	2	2	with	relationship	323:334	arg1	phosphorylation					341:355	phosphorylation	341:355	phosphorylation	341:355	The O-GlcNAc modification shares a complex relationship with phosphorylation, as both modifications are capable of mutually inhibiting the occupation of each other on the same or nearby amino acid residue.
22371497	0	3	theme	phosphorylations	74:89	arg1	β-N-Acetylglucosamine					0:20	β-N-Acetylglucosamine	0:20	β-N-Acetylglucosamine (O-GlcNAc)	0:31	β-N-Acetylglucosamine (O-GlcNAc) is a novel regulator of mitosis-specific phosphorylations on histone H3.
22371497	0	3	theme	phosphorylations	74:89	arg1	regulator					44:52	a novel regulator	36:52	a novel regulator of mitosis-specific phosphorylations on histone H3	36:103	β-N-Acetylglucosamine (O-GlcNAc) is a novel regulator of mitosis-specific phosphorylations on histone H3.
22371497	1	4	theme	dynamic	156:162	arg1	β-N-acetylglucosamine					115:135	O-Linked β-N-acetylglucosamine	106:135	O-Linked β-N-acetylglucosamine	106:135	O-Linked β-N-acetylglucosamine, or O-GlcNAc, is a dynamic post-translational modification that cycles on and off serine and threonine residues of nucleocytoplasmic proteins.
22371497	1	4	theme	dynamic	156:162	arg1	O-GlcNAc					141:148	O-GlcNAc	141:148	O-GlcNAc	141:148	O-Linked β-N-acetylglucosamine, or O-GlcNAc, is a dynamic post-translational modification that cycles on and off serine and threonine residues of nucleocytoplasmic proteins.
22371497	1	4	theme	dynamic	156:162	arg1	modification					183:194	a dynamic post-translational modification	154:194	a dynamic post-translational modification that cycles on and off serine and threonine residues of nucleocytoplasmic proteins	154:277	O-Linked β-N-acetylglucosamine, or O-GlcNAc, is a dynamic post-translational modification that cycles on and off serine and threonine residues of nucleocytoplasmic proteins.
22371497	1	5	theme	proteins	270:277	arg1	threonine					230:238	threonine	230:238	threonine	230:238	O-Linked β-N-acetylglucosamine, or O-GlcNAc, is a dynamic post-translational modification that cycles on and off serine and threonine residues of nucleocytoplasmic proteins.
22371497	1	5	theme	proteins	270:277	arg1	serine					219:224	serine	219:224	serine	219:224	O-Linked β-N-acetylglucosamine, or O-GlcNAc, is a dynamic post-translational modification that cycles on and off serine and threonine residues of nucleocytoplasmic proteins.
22371497	4	6	mod	modified	794:801	arg1	H3					778:779	H3	778:779	H3	778:779	A recent study also found that all four core nucleosomal histones (H2A, H2B, H3, and H4) are modified with O-GlcNAc, although no specific sites on H3 were reported.
22371497	4	6	mod	modified	794:801	arg1	histones					758:765	all four core nucleosomal histones	732:765	all four core nucleosomal histones (H2A, H2B, H3, and H4)	732:788	A recent study also found that all four core nucleosomal histones (H2A, H2B, H3, and H4) are modified with O-GlcNAc, although no specific sites on H3 were reported.
22371497	4	6	mod	modified	794:801	arg3	O-GlcNAc					808:815	O-GlcNAc	808:815	O-GlcNAc	808:815	A recent study also found that all four core nucleosomal histones (H2A, H2B, H3, and H4) are modified with O-GlcNAc, although no specific sites on H3 were reported.
22371497	4	6	mod	modified	794:801	arg1	H2A					768:770	H2A	768:770	H2A	768:770	A recent study also found that all four core nucleosomal histones (H2A, H2B, H3, and H4) are modified with O-GlcNAc, although no specific sites on H3 were reported.
22371497	4	6	mod	modified	794:801	arg1	H4					786:787	H4	786:787	H4	786:787	A recent study also found that all four core nucleosomal histones (H2A, H2B, H3, and H4) are modified with O-GlcNAc, although no specific sites on H3 were reported.
22371497	4	6	mod	modified	794:801	arg1	H2B					773:775	H2B	773:775	H2B	773:775	A recent study also found that all four core nucleosomal histones (H2A, H2B, H3, and H4) are modified with O-GlcNAc, although no specific sites on H3 were reported.
22371497	4	7	theme	specific	830:837	arg1	sites					839:843	no specific sites	827:843	no specific sites on H3	827:849	A recent study also found that all four core nucleosomal histones (H2A, H2B, H3, and H4) are modified with O-GlcNAc, although no specific sites on H3 were reported.
22371497	2	8	theme	complex	315:321	arg1	relationship					323:334	a complex relationship	313:334	a complex relationship with phosphorylation	313:355	The O-GlcNAc modification shares a complex relationship with phosphorylation, as both modifications are capable of mutually inhibiting the occupation of each other on the same or nearby amino acid residue.
22371497	0	9	theme	histone	94:100	arg1	H3					102:103	histone H3	94:103	histone H3	94:103	β-N-Acetylglucosamine (O-GlcNAc) is a novel regulator of mitosis-specific phosphorylations on histone H3.
22371497	0	10	from	regulator	44:52	arg1	H3					102:103	histone H3	94:103	histone H3	94:103	β-N-Acetylglucosamine (O-GlcNAc) is a novel regulator of mitosis-specific phosphorylations on histone H3.
22371497	4	11	theme	nucleosomal	746:756	arg1	histones					758:765	all four core nucleosomal histones	732:765	all four core nucleosomal histones (H2A, H2B, H3, and H4)	732:788	A recent study also found that all four core nucleosomal histones (H2A, H2B, H3, and H4) are modified with O-GlcNAc, although no specific sites on H3 were reported.
22371497	4	11	theme	nucleosomal	746:756	arg1	H3					778:779	H3	778:779	H3	778:779	A recent study also found that all four core nucleosomal histones (H2A, H2B, H3, and H4) are modified with O-GlcNAc, although no specific sites on H3 were reported.
22371497	4	11	theme	nucleosomal	746:756	arg1	H4					786:787	H4	786:787	H4	786:787	A recent study also found that all four core nucleosomal histones (H2A, H2B, H3, and H4) are modified with O-GlcNAc, although no specific sites on H3 were reported.
22371497	4	11	theme	nucleosomal	746:756	arg1	H2B					773:775	H2B	773:775	H2B	773:775	A recent study also found that all four core nucleosomal histones (H2A, H2B, H3, and H4) are modified with O-GlcNAc, although no specific sites on H3 were reported.
22371497	4	11	theme	nucleosomal	746:756	arg1	H2A					768:770	H2A	768:770	H2A	768:770	A recent study also found that all four core nucleosomal histones (H2A, H2B, H3, and H4) are modified with O-GlcNAc, although no specific sites on H3 were reported.
22371497	6	12	mod	modified	1036:1043	arg1	H3					1030:1031	H3	1030:1031	H3	1030:1031	Several biochemical assays were used to validate that H3 is modified with O-GlcNAc.
22371497	6	12	mod	modified	1036:1043	arg3	O-GlcNAc					1050:1057	O-GlcNAc	1050:1057	O-GlcNAc	1050:1057	Several biochemical assays were used to validate that H3 is modified with O-GlcNAc.
22371497	7	13	theme	novel	1116:1120	arg1	site					1131:1134	a novel O-GlcNAc site	1114:1134	a novel O-GlcNAc site	1114:1134	Mass spectrometry analysis identified threonine 32 as a novel O-GlcNAc site.
22371497	7	13	theme	novel	1116:1120	arg1	threonine					1098:1106	threonine 32	1098:1109	threonine 32	1098:1109	Mass spectrometry analysis identified threonine 32 as a novel O-GlcNAc site.
22371497	1	14	theme	post-translational	164:181	arg1	β-N-acetylglucosamine					115:135	O-Linked β-N-acetylglucosamine	106:135	O-Linked β-N-acetylglucosamine	106:135	O-Linked β-N-acetylglucosamine, or O-GlcNAc, is a dynamic post-translational modification that cycles on and off serine and threonine residues of nucleocytoplasmic proteins.
22371497	1	14	theme	post-translational	164:181	arg1	O-GlcNAc					141:148	O-GlcNAc	141:148	O-GlcNAc	141:148	O-Linked β-N-acetylglucosamine, or O-GlcNAc, is a dynamic post-translational modification that cycles on and off serine and threonine residues of nucleocytoplasmic proteins.
22371497	1	14	theme	post-translational	164:181	arg1	modification					183:194	a dynamic post-translational modification	154:194	a dynamic post-translational modification that cycles on and off serine and threonine residues of nucleocytoplasmic proteins	154:277	O-Linked β-N-acetylglucosamine, or O-GlcNAc, is a dynamic post-translational modification that cycles on and off serine and threonine residues of nucleocytoplasmic proteins.
22371497	2	15	theme	acid	472:475	arg1	residue					477:483	the same or nearby amino acid residue	447:483	the same or nearby amino acid residue	447:483	The O-GlcNAc modification shares a complex relationship with phosphorylation, as both modifications are capable of mutually inhibiting the occupation of each other on the same or nearby amino acid residue.
22371497	11	16	theme	mitosis-specific	1686:1701	arg1	phosphorylations					1703:1718	mitosis-specific phosphorylations	1686:1718	mitosis-specific phosphorylations on H3	1686:1724	Taken together, these data indicate that O-GlcNAcylation regulates mitosis-specific phosphorylations on H3, providing a mechanistic switch that orchestrates the G2-M transition of the cell cycle.
22371497	1	17	theme	nucleocytoplasmic	252:268	arg1	proteins					270:277	nucleocytoplasmic proteins	252:277	nucleocytoplasmic proteins	252:277	O-Linked β-N-acetylglucosamine, or O-GlcNAc, is a dynamic post-translational modification that cycles on and off serine and threonine residues of nucleocytoplasmic proteins.
22371497	2	18	theme	O-GlcNAc	284:291	arg1	modification					293:304	The O-GlcNAc modification	280:304	The O-GlcNAc modification	280:304	The O-GlcNAc modification shares a complex relationship with phosphorylation, as both modifications are capable of mutually inhibiting the occupation of each other on the same or nearby amino acid residue.
22371497	8	19	theme	higher	1162:1167	arg1	levels					1169:1174	higher levels	1162:1174	higher levels on H3	1162:1180	O-GlcNAc was detected at higher levels on H3 during interphase than mitosis, which inversely correlated with phosphorylation.
22371497	2	20	theme	amino	466:470	arg1	residue					477:483	the same or nearby amino acid residue	447:483	the same or nearby amino acid residue	447:483	The O-GlcNAc modification shares a complex relationship with phosphorylation, as both modifications are capable of mutually inhibiting the occupation of each other on the same or nearby amino acid residue.
22371497	10	21	from	phosphorylation	1596:1610	arg1	H3					1615:1616	H3	1615:1616	H3	1615:1616	Finally, inhibiting OGA, the enzyme responsible for removing O-GlcNAc, hindered the transition from G2 to M phase of the cell cycle, displaying a phenotype similar to preventing mitosis-specific phosphorylation on H3.
22371497	10	22	theme	cell	1522:1525	arg1	cycle					1527:1531	the cell cycle	1518:1531	the cell cycle	1518:1531	Finally, inhibiting OGA, the enzyme responsible for removing O-GlcNAc, hindered the transition from G2 to M phase of the cell cycle, displaying a phenotype similar to preventing mitosis-specific phosphorylation on H3.
22371497	2	23	theme	nearby	459:464	arg1	residue					477:483	the same or nearby amino acid residue	447:483	the same or nearby amino acid residue	447:483	The O-GlcNAc modification shares a complex relationship with phosphorylation, as both modifications are capable of mutually inhibiting the occupation of each other on the same or nearby amino acid residue.
22371497	6	24	used	used	1008:1011	arg2	assays					996:1001	Several biochemical assays	976:1001	Several biochemical assays	976:1001	Several biochemical assays were used to validate that H3 is modified with O-GlcNAc.
22371497	3	25	theme	significant	578:588	arg1	role					590:593	a significant role	576:593	a significant role	576:593	In addition to diabetes, cancer, and neurodegenerative diseases, O-GlcNAc appears to play a significant role in cell growth and cell cycle progression, although the precise mechanisms are still not well understood.
22371497	10	26	theme	similar	1557:1563	arg1	phenotype					1547:1555	a phenotype	1545:1555	a phenotype similar to preventing mitosis-specific phosphorylation on H3	1545:1616	Finally, inhibiting OGA, the enzyme responsible for removing O-GlcNAc, hindered the transition from G2 to M phase of the cell cycle, displaying a phenotype similar to preventing mitosis-specific phosphorylation on H3.
22371497	9	27	theme	increased	1276:1284	arg1	O-GlcNAcylation					1286:1300	increased O-GlcNAcylation	1276:1300	increased O-GlcNAcylation	1276:1300	Furthermore, increased O-GlcNAcylation was observed to reduce mitosis-specific phosphorylation at serine 10, serine 28, and threonine 32.
22371497	10	28	theme	cycle	1527:1531	arg1	phase					1509:1513	M phase	1507:1513	M phase of the cell cycle	1507:1531	Finally, inhibiting OGA, the enzyme responsible for removing O-GlcNAc, hindered the transition from G2 to M phase of the cell cycle, displaying a phenotype similar to preventing mitosis-specific phosphorylation on H3.
22371497	4	29	theme	core	741:744	arg1	histones					758:765	all four core nucleosomal histones	732:765	all four core nucleosomal histones (H2A, H2B, H3, and H4)	732:788	A recent study also found that all four core nucleosomal histones (H2A, H2B, H3, and H4) are modified with O-GlcNAc, although no specific sites on H3 were reported.
22371497	4	29	theme	core	741:744	arg1	H3					778:779	H3	778:779	H3	778:779	A recent study also found that all four core nucleosomal histones (H2A, H2B, H3, and H4) are modified with O-GlcNAc, although no specific sites on H3 were reported.
22371497	4	29	theme	core	741:744	arg1	H4					786:787	H4	786:787	H4	786:787	A recent study also found that all four core nucleosomal histones (H2A, H2B, H3, and H4) are modified with O-GlcNAc, although no specific sites on H3 were reported.
22371497	4	29	theme	core	741:744	arg1	H2B					773:775	H2B	773:775	H2B	773:775	A recent study also found that all four core nucleosomal histones (H2A, H2B, H3, and H4) are modified with O-GlcNAc, although no specific sites on H3 were reported.
22371497	4	29	theme	core	741:744	arg1	H2A					768:770	H2A	768:770	H2A	768:770	A recent study also found that all four core nucleosomal histones (H2A, H2B, H3, and H4) are modified with O-GlcNAc, although no specific sites on H3 were reported.
22371497	6	30	theme	biochemical	984:994	arg1	assays					996:1001	Several biochemical assays	976:1001	Several biochemical assays	976:1001	Several biochemical assays were used to validate that H3 is modified with O-GlcNAc.
22371497	2	31	theme	same	451:454	arg1	residue					477:483	the same or nearby amino acid residue	447:483	the same or nearby amino acid residue	447:483	The O-GlcNAc modification shares a complex relationship with phosphorylation, as both modifications are capable of mutually inhibiting the occupation of each other on the same or nearby amino acid residue.
22371497	11	32	theme	mechanistic	1739:1749	arg1	switch					1751:1756	a mechanistic switch	1737:1756	a mechanistic switch that orchestrates the G2-M transition of the cell cycle	1737:1812	Taken together, these data indicate that O-GlcNAcylation regulates mitosis-specific phosphorylations on H3, providing a mechanistic switch that orchestrates the G2-M transition of the cell cycle.
22371497	1	33	theme	O-Linked	106:113	arg1	β-N-acetylglucosamine					115:135	O-Linked β-N-acetylglucosamine	106:135	O-Linked β-N-acetylglucosamine	106:135	O-Linked β-N-acetylglucosamine, or O-GlcNAc, is a dynamic post-translational modification that cycles on and off serine and threonine residues of nucleocytoplasmic proteins.
22371497	1	33	theme	O-Linked	106:113	arg1	O-GlcNAc					141:148	O-GlcNAc	141:148	O-GlcNAc	141:148	O-Linked β-N-acetylglucosamine, or O-GlcNAc, is a dynamic post-translational modification that cycles on and off serine and threonine residues of nucleocytoplasmic proteins.
22371497	1	33	theme	O-Linked	106:113	arg1	modification					183:194	a dynamic post-translational modification	154:194	a dynamic post-translational modification that cycles on and off serine and threonine residues of nucleocytoplasmic proteins	154:277	O-Linked β-N-acetylglucosamine, or O-GlcNAc, is a dynamic post-translational modification that cycles on and off serine and threonine residues of nucleocytoplasmic proteins.
22371497	6	34	theme	Several	976:982	arg1	assays					996:1001	Several biochemical assays	976:1001	Several biochemical assays	976:1001	Several biochemical assays were used to validate that H3 is modified with O-GlcNAc.
22371497	3	35	theme	precise	651:657	arg1	mechanisms					659:668	the precise mechanisms	647:668	the precise mechanisms	647:668	In addition to diabetes, cancer, and neurodegenerative diseases, O-GlcNAc appears to play a significant role in cell growth and cell cycle progression, although the precise mechanisms are still not well understood.
22371497	3	36	theme	cell	598:601	arg1	growth					603:608	cell growth	598:608	cell growth	598:608	In addition to diabetes, cancer, and neurodegenerative diseases, O-GlcNAc appears to play a significant role in cell growth and cell cycle progression, although the precise mechanisms are still not well understood.
22371497	2	37	theme	other	438:442	arg1	occupation					419:428	the occupation	415:428	the occupation of each other on the same or nearby amino acid residue	415:483	The O-GlcNAc modification shares a complex relationship with phosphorylation, as both modifications are capable of mutually inhibiting the occupation of each other on the same or nearby amino acid residue.
22371497	10	38	theme	mitosis-specific	1579:1594	arg1	phosphorylation					1596:1610	mitosis-specific phosphorylation	1579:1610	mitosis-specific phosphorylation on H3	1579:1616	Finally, inhibiting OGA, the enzyme responsible for removing O-GlcNAc, hindered the transition from G2 to M phase of the cell cycle, displaying a phenotype similar to preventing mitosis-specific phosphorylation on H3.
22371497	9	39	from	serine	1372:1377	arg1	phosphorylation					1342:1356	mitosis-specific phosphorylation	1325:1356	mitosis-specific phosphorylation at serine 10, serine 28, and threonine 32	1325:1398	Furthermore, increased O-GlcNAcylation was observed to reduce mitosis-specific phosphorylation at serine 10, serine 28, and threonine 32.
22371497	5	40	mod	modified	952:959	arg3	O-GlcNAc					966:973	O-GlcNAc	966:973	O-GlcNAc	966:973	Here, we describe that histone H3, a protein highly phosphorylated during mitosis, is modified with O-GlcNAc.
22371497	5	40	mod	modified	952:959	arg1	H3					897:898	histone H3	889:898	histone H3	889:898	Here, we describe that histone H3, a protein highly phosphorylated during mitosis, is modified with O-GlcNAc.
22371497	5	40	mod	modified	952:959	arg1	protein					903:909	a protein	901:909	a protein highly phosphorylated during mitosis	901:946	Here, we describe that histone H3, a protein highly phosphorylated during mitosis, is modified with O-GlcNAc.
22371497	7	41	theme	O-GlcNAc	1122:1129	arg1	site					1131:1134	a novel O-GlcNAc site	1114:1134	a novel O-GlcNAc site	1114:1134	Mass spectrometry analysis identified threonine 32 as a novel O-GlcNAc site.
22371497	7	41	theme	O-GlcNAc	1122:1129	arg1	threonine					1098:1106	threonine 32	1098:1109	threonine 32	1098:1109	Mass spectrometry analysis identified threonine 32 as a novel O-GlcNAc site.
22371497	7	42	theme	Mass	1060:1063	arg1	analysis					1078:1085	Mass spectrometry analysis	1060:1085	Mass spectrometry analysis	1060:1085	Mass spectrometry analysis identified threonine 32 as a novel O-GlcNAc site.
22371497	9	43	from	serine	1361:1366	arg1	phosphorylation					1342:1356	mitosis-specific phosphorylation	1325:1356	mitosis-specific phosphorylation at serine 10, serine 28, and threonine 32	1325:1398	Furthermore, increased O-GlcNAcylation was observed to reduce mitosis-specific phosphorylation at serine 10, serine 28, and threonine 32.
22371497	11	44	from	phosphorylations	1703:1718	arg1	H3					1723:1724	H3	1723:1724	H3	1723:1724	Taken together, these data indicate that O-GlcNAcylation regulates mitosis-specific phosphorylations on H3, providing a mechanistic switch that orchestrates the G2-M transition of the cell cycle.
22371497	11	45	theme	cycle	1808:1812	arg1	transition					1785:1794	the G2-M transition	1776:1794	the G2-M transition of the cell cycle	1776:1812	Taken together, these data indicate that O-GlcNAcylation regulates mitosis-specific phosphorylations on H3, providing a mechanistic switch that orchestrates the G2-M transition of the cell cycle.
22371497	0	46	theme	novel	38:42	arg1	β-N-Acetylglucosamine					0:20	β-N-Acetylglucosamine	0:20	β-N-Acetylglucosamine (O-GlcNAc)	0:31	β-N-Acetylglucosamine (O-GlcNAc) is a novel regulator of mitosis-specific phosphorylations on histone H3.
22371497	0	46	theme	novel	38:42	arg1	regulator					44:52	a novel regulator	36:52	a novel regulator of mitosis-specific phosphorylations on histone H3	36:103	β-N-Acetylglucosamine (O-GlcNAc) is a novel regulator of mitosis-specific phosphorylations on histone H3.
22371497	10	47	theme	responsible	1437:1447	arg1	enzyme					1430:1435	the enzyme	1426:1435	the enzyme responsible for removing O-GlcNAc	1426:1469	Finally, inhibiting OGA, the enzyme responsible for removing O-GlcNAc, hindered the transition from G2 to M phase of the cell cycle, displaying a phenotype similar to preventing mitosis-specific phosphorylation on H3.
22371497	10	47	theme	responsible	1437:1447	arg1	OGA					1421:1423	inhibiting OGA	1410:1423	inhibiting OGA	1410:1423	Finally, inhibiting OGA, the enzyme responsible for removing O-GlcNAc, hindered the transition from G2 to M phase of the cell cycle, displaying a phenotype similar to preventing mitosis-specific phosphorylation on H3.
22371497	10	48	theme	inhibiting	1410:1419	arg1	enzyme					1430:1435	the enzyme	1426:1435	the enzyme responsible for removing O-GlcNAc	1426:1469	Finally, inhibiting OGA, the enzyme responsible for removing O-GlcNAc, hindered the transition from G2 to M phase of the cell cycle, displaying a phenotype similar to preventing mitosis-specific phosphorylation on H3.
22371497	10	48	theme	inhibiting	1410:1419	arg1	OGA					1421:1423	inhibiting OGA	1410:1423	inhibiting OGA	1410:1423	Finally, inhibiting OGA, the enzyme responsible for removing O-GlcNAc, hindered the transition from G2 to M phase of the cell cycle, displaying a phenotype similar to preventing mitosis-specific phosphorylation on H3.
22371497	8	49	from	levels	1169:1174	arg1	H3					1179:1180	H3	1179:1180	H3	1179:1180	O-GlcNAc was detected at higher levels on H3 during interphase than mitosis, which inversely correlated with phosphorylation.
22371497	4	50	theme	recent	703:708	arg1	study					710:714	A recent study	701:714	A recent study	701:714	A recent study also found that all four core nucleosomal histones (H2A, H2B, H3, and H4) are modified with O-GlcNAc, although no specific sites on H3 were reported.
22371497	9	51	theme	mitosis-specific	1325:1340	arg1	phosphorylation					1342:1356	mitosis-specific phosphorylation	1325:1356	mitosis-specific phosphorylation at serine 10, serine 28, and threonine 32	1325:1398	Furthermore, increased O-GlcNAcylation was observed to reduce mitosis-specific phosphorylation at serine 10, serine 28, and threonine 32.
22371497	7	52	theme	spectrometry	1065:1076	arg1	analysis					1078:1085	Mass spectrometry analysis	1060:1085	Mass spectrometry analysis	1060:1085	Mass spectrometry analysis identified threonine 32 as a novel O-GlcNAc site.
22371497	10	53	from	G2	1501:1502	arg1	transition					1485:1494	the transition	1481:1494	the transition from G2 to M phase of the cell cycle	1481:1531	Finally, inhibiting OGA, the enzyme responsible for removing O-GlcNAc, hindered the transition from G2 to M phase of the cell cycle, displaying a phenotype similar to preventing mitosis-specific phosphorylation on H3.
22371497	3	54	theme	cycle	619:623	arg1	progression					625:635	cell cycle progression	614:635	cell cycle progression	614:635	In addition to diabetes, cancer, and neurodegenerative diseases, O-GlcNAc appears to play a significant role in cell growth and cell cycle progression, although the precise mechanisms are still not well understood.
22371497	2	55	from	occupation	419:428	arg1	residue					477:483	the same or nearby amino acid residue	447:483	the same or nearby amino acid residue	447:483	The O-GlcNAc modification shares a complex relationship with phosphorylation, as both modifications are capable of mutually inhibiting the occupation of each other on the same or nearby amino acid residue.
22371497	1	56	dep	serine	219:224	arg1	residues					240:247	residues	240:247	residues	240:247	O-Linked β-N-acetylglucosamine, or O-GlcNAc, is a dynamic post-translational modification that cycles on and off serine and threonine residues of nucleocytoplasmic proteins.
22371497	1	56	dep	serine	219:224	arg1	off					215:217	off	215:217	off	215:217	O-Linked β-N-acetylglucosamine, or O-GlcNAc, is a dynamic post-translational modification that cycles on and off serine and threonine residues of nucleocytoplasmic proteins.
22371497	11	57	theme	cell	1803:1806	arg1	cycle					1808:1812	the cell cycle	1799:1812	the cell cycle	1799:1812	Taken together, these data indicate that O-GlcNAcylation regulates mitosis-specific phosphorylations on H3, providing a mechanistic switch that orchestrates the G2-M transition of the cell cycle.
22371497	0	58	theme	mitosis-specific	57:72	arg1	phosphorylations					74:89	mitosis-specific phosphorylations	57:89	mitosis-specific phosphorylations	57:89	β-N-Acetylglucosamine (O-GlcNAc) is a novel regulator of mitosis-specific phosphorylations on histone H3.
22371497	4	59	from	sites	839:843	arg1	H3					848:849	H3	848:849	H3	848:849	A recent study also found that all four core nucleosomal histones (H2A, H2B, H3, and H4) are modified with O-GlcNAc, although no specific sites on H3 were reported.
22371497	8	60	located	detected	1150:1157	arg1	levels					1169:1174	higher levels	1162:1174	higher levels on H3	1162:1180	O-GlcNAc was detected at higher levels on H3 during interphase than mitosis, which inversely correlated with phosphorylation.
22371497	8	60	located	detected	1150:1157	arg2	O-GlcNAc					1137:1144	O-GlcNAc	1137:1144	O-GlcNAc	1137:1144	O-GlcNAc was detected at higher levels on H3 during interphase than mitosis, which inversely correlated with phosphorylation.
22371497	1	61	from	cycles	201:206	arg1	and					211:213	and	211:213	and	211:213	O-Linked β-N-acetylglucosamine, or O-GlcNAc, is a dynamic post-translational modification that cycles on and off serine and threonine residues of nucleocytoplasmic proteins.
22371497	5	62	theme	histone	889:895	arg1	H3					897:898	histone H3	889:898	histone H3	889:898	Here, we describe that histone H3, a protein highly phosphorylated during mitosis, is modified with O-GlcNAc.
22371497	5	62	theme	histone	889:895	arg1	protein					903:909	a protein	901:909	a protein highly phosphorylated during mitosis	901:946	Here, we describe that histone H3, a protein highly phosphorylated during mitosis, is modified with O-GlcNAc.
22371497	11	63	theme	G2-M	1780:1783	arg1	transition					1785:1794	the G2-M transition	1776:1794	the G2-M transition of the cell cycle	1776:1812	Taken together, these data indicate that O-GlcNAcylation regulates mitosis-specific phosphorylations on H3, providing a mechanistic switch that orchestrates the G2-M transition of the cell cycle.
22371497	3	64	theme	cell	614:617	arg1	progression					625:635	cell cycle progression	614:635	cell cycle progression	614:635	In addition to diabetes, cancer, and neurodegenerative diseases, O-GlcNAc appears to play a significant role in cell growth and cell cycle progression, although the precise mechanisms are still not well understood.
22371497	3	65	theme	neurodegenerative	523:539	arg1	diseases					541:548	neurodegenerative diseases	523:548	neurodegenerative diseases	523:548	In addition to diabetes, cancer, and neurodegenerative diseases, O-GlcNAc appears to play a significant role in cell growth and cell cycle progression, although the precise mechanisms are still not well understood.
22371497	10	66	theme	M	1507:1507	arg1	phase					1509:1513	M phase	1507:1513	M phase of the cell cycle	1507:1531	Finally, inhibiting OGA, the enzyme responsible for removing O-GlcNAc, hindered the transition from G2 to M phase of the cell cycle, displaying a phenotype similar to preventing mitosis-specific phosphorylation on H3.
21548981	9	0	with	assembly	1701:1708	arg1	IGF-II					1715:1720	IGF-II	1715:1720	IGF-II	1715:1720	This information may be used for developing new therapies by regulating IGFBP-6 assembly with IGF-II to minimize the risk of viral associated hepatocellular carcinoma.
21548981	2	1	theme	IGF-II	383:388	arg1	levels					390:395	Elevated IGF-II levels	374:395	Elevated IGF-II levels	374:395	Elevated IGF-II levels are indicator of increased risk for cholangiocellular and hepatocellular carcinomas through over saturation of IGF-II binding capacities with IGF receptors leading to cellular dedifferentiation.
21548981	2	1	theme	IGF-II	383:388	arg1	indicator					401:409	indicator	401:409	indicator of increased risk for cholangiocellular and hepatocellular carcinomas	401:479	Elevated IGF-II levels are indicator of increased risk for cholangiocellular and hepatocellular carcinomas through over saturation of IGF-II binding capacities with IGF receptors leading to cellular dedifferentiation.
21548981	1	2	theme	IGF-II	274:279	arg1	gene					281:284	cell growth stimulator IGF-II gene	251:284	cell growth stimulator IGF-II gene	251:284	Hepatocellular carcinoma is mainly associated with viral hepatitis B and C. Activation of cell growth stimulator IGF-II gene is observed in tumor formation especially in viral associated hepatocellular carcinoma.
21548981	6	3	theme	higher	1244:1249	arg1	affinity					1251:1258	a 10-fold higher affinity	1234:1258	a 10-fold higher affinity for IGF-II	1234:1269	Phosphorylation of IGFBPs inhibits IGFs action on target cells while O-glycosylation prevents binding of IGFBP-6 to glycosaminoglycans and cell membranes and resulting in a 10-fold higher affinity for IGF-II.
21548981	3	4	theme	transcriptional	777:791	arg1	level					793:797	transcriptional level	777:797	transcriptional level	777:797	In HCV, core protein is believed to trans-activate host IGF-II receptor through PKC pathway and the inhibition of tumor cell growth can be achieved by blocking IGF-II pathway either at transcriptional level or increasing its binding with IGFBPs (Insulin like growth factor proteins) at C-terminal, so that it is not available in free form.
21548981	11	5	theme	IGF-II	2095:2100	arg1	actions					2102:2108	the IGF-II actions	2091:2108	the IGF-II actions during viral infection to minimize the risk of hepatocellular carcinoma	2091:2180	Furthermore, this site can be used for developing new therapies to control the IGF-II actions during viral infection to minimize the risk of hepatocellular carcinoma.
21548981	9	6	theme	associated	1752:1761	arg1	carcinoma					1778:1786	viral associated hepatocellular carcinoma	1746:1786	viral associated hepatocellular carcinoma	1746:1786	This information may be used for developing new therapies by regulating IGFBP-6 assembly with IGF-II to minimize the risk of viral associated hepatocellular carcinoma.
21548981	5	7	with	Affinity	983:990	arg1	IGFs					1007:1010	IGFs	1007:1010	IGFs	1007:1010	Affinity of IGFBPs with IGFs is controlled by post-translational modifications.
21548981	6	8	from	action	1103:1108	arg1	cells					1120:1124	target cells	1113:1124	target cells	1113:1124	Phosphorylation of IGFBPs inhibits IGFs action on target cells while O-glycosylation prevents binding of IGFBP-6 to glycosaminoglycans and cell membranes and resulting in a 10-fold higher affinity for IGF-II.
21548981	1	9	theme	viral	212:216	arg1	B					228:228	viral hepatitis B	212:228	viral hepatitis B	212:228	Hepatocellular carcinoma is mainly associated with viral hepatitis B and C. Activation of cell growth stimulator IGF-II gene is observed in tumor formation especially in viral associated hepatocellular carcinoma.
21548981	4	10	theme	specific	945:952	arg1	IGFBP-6					932:938	IGFBP-6	932:938	IGFBP-6	932:938	IGFBP-6 is a specific inhibitor of IGF-II actions.
21548981	4	10	theme	specific	945:952	arg1	inhibitor					954:962	a specific inhibitor	943:962	a specific inhibitor of IGF-II actions	943:980	IGFBP-6 is a specific inhibitor of IGF-II actions.
21548981	0	11	theme	viral	120:124	arg1	carcinoma					150:158	viral mediated hepatocellular carcinoma	120:158	viral mediated hepatocellular carcinoma	120:158	Serine 204 phosphorylation and O-β-GlcNAC interplay of IGFBP-6 as therapeutic indicator to regulate IGF-II functions in viral mediated hepatocellular carcinoma.
21548981	10	12	theme	IGFBP-6	1850:1856	arg1	O-β-GlcNAc					1836:1845	O-β-GlcNAc	1836:1845	O-β-GlcNAc of IGFBP-6 at Ser 204	1836:1867	We can conclude that during HCV/HBV infection, O-β-GlcNAc of IGFBP-6 at Ser 204 diminish their binding with IGF-II, increase IGF-II cellular expression and promote cancer progression which can lead to hepatocellular carcinoma.
21548981	10	13	with	binding	1884:1890	arg1	IGF-II					1897:1902	IGF-II	1897:1902	IGF-II	1897:1902	We can conclude that during HCV/HBV infection, O-β-GlcNAc of IGFBP-6 at Ser 204 diminish their binding with IGF-II, increase IGF-II cellular expression and promote cancer progression which can lead to hepatocellular carcinoma.
21548981	0	14	theme	hepatocellular	135:148	arg1	carcinoma					150:158	viral mediated hepatocellular carcinoma	120:158	viral mediated hepatocellular carcinoma	120:158	Serine 204 phosphorylation and O-β-GlcNAC interplay of IGFBP-6 as therapeutic indicator to regulate IGF-II functions in viral mediated hepatocellular carcinoma.
21548981	1	15	theme	C.	234:235	arg1	Activation					237:246	C. Activation	234:246	C. Activation of cell growth stimulator IGF-II gene	234:284	Hepatocellular carcinoma is mainly associated with viral hepatitis B and C. Activation of cell growth stimulator IGF-II gene is observed in tumor formation especially in viral associated hepatocellular carcinoma.
21548981	11	16	theme	carcinoma	2172:2180	arg1	risk					2149:2152	the risk	2145:2152	the risk of hepatocellular carcinoma	2145:2180	Furthermore, this site can be used for developing new therapies to control the IGF-II actions during viral infection to minimize the risk of hepatocellular carcinoma.
21548981	8	17	theme	O-β-GlcNAc	1522:1531	arg1	modification					1533:1544	alternate O-β-GlcNAc modification	1512:1544	alternate O-β-GlcNAc modification	1512:1544	By using neural network based prediction methods, we propose that alternate O-β-GlcNAc modification and phosphorylation on Ser 204 control the binding of IGFBP-6 with IGF-II.
21548981	3	18	theme	IGF-II	648:653	arg1	receptor					655:662	host IGF-II receptor	643:662	host IGF-II receptor through PKC pathway and the inhibition of tumor cell growth can be achieved by blocking IGF-II pathway either at transcriptional level or increasing its binding with IGFBPs (Insulin like growth factor proteins) at C-terminal, so that it is not available in free form	643:929	In HCV, core protein is believed to trans-activate host IGF-II receptor through PKC pathway and the inhibition of tumor cell growth can be achieved by blocking IGF-II pathway either at transcriptional level or increasing its binding with IGFBPs (Insulin like growth factor proteins) at C-terminal, so that it is not available in free form.
21548981	11	19	theme	new	2066:2068	arg1	therapies					2070:2078	new therapies	2066:2078	new therapies	2066:2078	Furthermore, this site can be used for developing new therapies to control the IGF-II actions during viral infection to minimize the risk of hepatocellular carcinoma.
21548981	3	20	from	form	926:929	arg1	available					908:916	available	908:916	available	908:916	In HCV, core protein is believed to trans-activate host IGF-II receptor through PKC pathway and the inhibition of tumor cell growth can be achieved by blocking IGF-II pathway either at transcriptional level or increasing its binding with IGFBPs (Insulin like growth factor proteins) at C-terminal, so that it is not available in free form.
21548981	3	21	theme	factor	858:863	arg1	proteins					865:872	growth factor proteins	851:872	growth factor proteins	851:872	In HCV, core protein is believed to trans-activate host IGF-II receptor through PKC pathway and the inhibition of tumor cell growth can be achieved by blocking IGF-II pathway either at transcriptional level or increasing its binding with IGFBPs (Insulin like growth factor proteins) at C-terminal, so that it is not available in free form.
21548981	1	22	theme	hepatocellular	348:361	arg1	carcinoma					363:371	viral associated hepatocellular carcinoma	331:371	viral associated hepatocellular carcinoma	331:371	Hepatocellular carcinoma is mainly associated with viral hepatitis B and C. Activation of cell growth stimulator IGF-II gene is observed in tumor formation especially in viral associated hepatocellular carcinoma.
21548981	1	23	theme	Hepatocellular	161:174	arg1	carcinoma					176:184	Hepatocellular carcinoma	161:184	Hepatocellular carcinoma	161:184	Hepatocellular carcinoma is mainly associated with viral hepatitis B and C. Activation of cell growth stimulator IGF-II gene is observed in tumor formation especially in viral associated hepatocellular carcinoma.
21548981	4	24	theme	actions	974:980	arg1	IGFBP-6					932:938	IGFBP-6	932:938	IGFBP-6	932:938	IGFBP-6 is a specific inhibitor of IGF-II actions.
21548981	4	24	theme	actions	974:980	arg1	inhibitor					954:962	a specific inhibitor	943:962	a specific inhibitor of IGF-II actions	943:980	IGFBP-6 is a specific inhibitor of IGF-II actions.
21548981	1	25	located	observed	289:296	arg2	Activation					237:246	C. Activation	234:246	C. Activation of cell growth stimulator IGF-II gene	234:284	Hepatocellular carcinoma is mainly associated with viral hepatitis B and C. Activation of cell growth stimulator IGF-II gene is observed in tumor formation especially in viral associated hepatocellular carcinoma.
21548981	1	25	located	observed	289:296	arg1	formation					307:315	tumor formation	301:315	tumor formation	301:315	Hepatocellular carcinoma is mainly associated with viral hepatitis B and C. Activation of cell growth stimulator IGF-II gene is observed in tumor formation especially in viral associated hepatocellular carcinoma.
21548981	1	25	located	observed	289:296	arg1	carcinoma					363:371	viral associated hepatocellular carcinoma	331:371	viral associated hepatocellular carcinoma	331:371	Hepatocellular carcinoma is mainly associated with viral hepatitis B and C. Activation of cell growth stimulator IGF-II gene is observed in tumor formation especially in viral associated hepatocellular carcinoma.
21548981	8	26	with	binding	1589:1595	arg1	IGF-II					1613:1618	IGF-II	1613:1618	IGF-II	1613:1618	By using neural network based prediction methods, we propose that alternate O-β-GlcNAc modification and phosphorylation on Ser 204 control the binding of IGFBP-6 with IGF-II.
21548981	11	27	used	used	2046:2049	arg2	site					2034:2037	this site	2029:2037	this site	2029:2037	Furthermore, this site can be used for developing new therapies to control the IGF-II actions during viral infection to minimize the risk of hepatocellular carcinoma.
21548981	0	28	theme	therapeutic	66:76	arg1	indicator					78:86	therapeutic indicator	66:86	therapeutic indicator	66:86	Serine 204 phosphorylation and O-β-GlcNAC interplay of IGFBP-6 as therapeutic indicator to regulate IGF-II functions in viral mediated hepatocellular carcinoma.
21548981	2	29	theme	increased	414:422	arg1	risk					424:427	increased risk	414:427	increased risk for cholangiocellular and hepatocellular carcinomas	414:479	Elevated IGF-II levels are indicator of increased risk for cholangiocellular and hepatocellular carcinomas through over saturation of IGF-II binding capacities with IGF receptors leading to cellular dedifferentiation.
21548981	0	30	theme	Serine	0:5	arg1	phosphorylation					11:25	Serine 204 phosphorylation	0:25	Serine 204 phosphorylation	0:25	Serine 204 phosphorylation and O-β-GlcNAC interplay of IGFBP-6 as therapeutic indicator to regulate IGF-II functions in viral mediated hepatocellular carcinoma.
21548981	7	31	theme	protein	1394:1400	arg1	expression					1402:1411	the protein expression	1390:1411	the protein expression	1390:1411	O-glycosylation and phosphorylation operate the functional expression of cellular proteins, this switching on and off the protein expression is difficult to monitor in vivo.
21548981	1	32	theme	tumor	301:305	arg1	formation					307:315	tumor formation	301:315	tumor formation	301:315	Hepatocellular carcinoma is mainly associated with viral hepatitis B and C. Activation of cell growth stimulator IGF-II gene is observed in tumor formation especially in viral associated hepatocellular carcinoma.
21548981	6	33	theme	IGFs	1098:1101	arg1	action					1103:1108	IGFs action	1098:1108	IGFs action on target cells	1098:1124	Phosphorylation of IGFBPs inhibits IGFs action on target cells while O-glycosylation prevents binding of IGFBP-6 to glycosaminoglycans and cell membranes and resulting in a 10-fold higher affinity for IGF-II.
21548981	3	34	from	C-terminal	878:887	arg1	binding					817:823	its binding	813:823	its binding with IGFBPs (Insulin like growth factor proteins)	813:873	In HCV, core protein is believed to trans-activate host IGF-II receptor through PKC pathway and the inhibition of tumor cell growth can be achieved by blocking IGF-II pathway either at transcriptional level or increasing its binding with IGFBPs (Insulin like growth factor proteins) at C-terminal, so that it is not available in free form.
21548981	3	35	theme	cell	712:715	arg1	growth					717:722	tumor cell growth	706:722	tumor cell growth	706:722	In HCV, core protein is believed to trans-activate host IGF-II receptor through PKC pathway and the inhibition of tumor cell growth can be achieved by blocking IGF-II pathway either at transcriptional level or increasing its binding with IGFBPs (Insulin like growth factor proteins) at C-terminal, so that it is not available in free form.
21548981	8	36	theme	network	1462:1468	arg1	methods					1487:1493	neural network based prediction methods	1455:1493	neural network based prediction methods	1455:1493	By using neural network based prediction methods, we propose that alternate O-β-GlcNAc modification and phosphorylation on Ser 204 control the binding of IGFBP-6 with IGF-II.
21548981	0	37	theme	O-β-GlcNAC	31:40	arg1	interplay					42:50	O-β-GlcNAC interplay	31:50	O-β-GlcNAC interplay	31:50	Serine 204 phosphorylation and O-β-GlcNAC interplay of IGFBP-6 as therapeutic indicator to regulate IGF-II functions in viral mediated hepatocellular carcinoma.
21548981	7	38	from	switching	1369:1377	arg1	and					1382:1384	and	1382:1384	and	1382:1384	O-glycosylation and phosphorylation operate the functional expression of cellular proteins, this switching on and off the protein expression is difficult to monitor in vivo.
21548981	6	39	theme	IGFBPs	1082:1087	arg1	Phosphorylation					1063:1077	Phosphorylation	1063:1077	Phosphorylation of IGFBPs	1063:1087	Phosphorylation of IGFBPs inhibits IGFs action on target cells while O-glycosylation prevents binding of IGFBP-6 to glycosaminoglycans and cell membranes and resulting in a 10-fold higher affinity for IGF-II.
21548981	2	40	theme	binding	515:521	arg1	capacities					523:532	IGF-II binding capacities	508:532	IGF-II binding capacities with IGF receptors leading to cellular dedifferentiation	508:589	Elevated IGF-II levels are indicator of increased risk for cholangiocellular and hepatocellular carcinomas through over saturation of IGF-II binding capacities with IGF receptors leading to cellular dedifferentiation.
21548981	10	41	theme	cellular	1921:1928	arg1	expression					1930:1939	IGF-II cellular expression	1914:1939	IGF-II cellular expression	1914:1939	We can conclude that during HCV/HBV infection, O-β-GlcNAc of IGFBP-6 at Ser 204 diminish their binding with IGF-II, increase IGF-II cellular expression and promote cancer progression which can lead to hepatocellular carcinoma.
21548981	8	42	theme	prediction	1476:1485	arg1	methods					1487:1493	neural network based prediction methods	1455:1493	neural network based prediction methods	1455:1493	By using neural network based prediction methods, we propose that alternate O-β-GlcNAc modification and phosphorylation on Ser 204 control the binding of IGFBP-6 with IGF-II.
21548981	2	43	theme	Elevated	374:381	arg1	levels					390:395	Elevated IGF-II levels	374:395	Elevated IGF-II levels	374:395	Elevated IGF-II levels are indicator of increased risk for cholangiocellular and hepatocellular carcinomas through over saturation of IGF-II binding capacities with IGF receptors leading to cellular dedifferentiation.
21548981	2	43	theme	Elevated	374:381	arg1	indicator					401:409	indicator	401:409	indicator of increased risk for cholangiocellular and hepatocellular carcinomas	401:479	Elevated IGF-II levels are indicator of increased risk for cholangiocellular and hepatocellular carcinomas through over saturation of IGF-II binding capacities with IGF receptors leading to cellular dedifferentiation.
21548981	1	44	theme	viral	331:335	arg1	carcinoma					363:371	viral associated hepatocellular carcinoma	331:371	viral associated hepatocellular carcinoma	331:371	Hepatocellular carcinoma is mainly associated with viral hepatitis B and C. Activation of cell growth stimulator IGF-II gene is observed in tumor formation especially in viral associated hepatocellular carcinoma.
21548981	7	45	theme	proteins	1354:1361	arg1	expression					1331:1340	the functional expression	1316:1340	the functional expression of cellular proteins	1316:1361	O-glycosylation and phosphorylation operate the functional expression of cellular proteins, this switching on and off the protein expression is difficult to monitor in vivo.
21548981	10	46	theme	cancer	1953:1958	arg1	progression					1960:1970	cancer progression	1953:1970	cancer progression which can lead to hepatocellular carcinoma	1953:2013	We can conclude that during HCV/HBV infection, O-β-GlcNAc of IGFBP-6 at Ser 204 diminish their binding with IGF-II, increase IGF-II cellular expression and promote cancer progression which can lead to hepatocellular carcinoma.
21548981	10	47	theme	HCV/HBV	1817:1823	arg1	infection					1825:1833	HCV/HBV infection	1817:1833	HCV/HBV infection	1817:1833	We can conclude that during HCV/HBV infection, O-β-GlcNAc of IGFBP-6 at Ser 204 diminish their binding with IGF-II, increase IGF-II cellular expression and promote cancer progression which can lead to hepatocellular carcinoma.
21548981	1	48	theme	cell	251:254	arg1	gene					281:284	cell growth stimulator IGF-II gene	251:284	cell growth stimulator IGF-II gene	251:284	Hepatocellular carcinoma is mainly associated with viral hepatitis B and C. Activation of cell growth stimulator IGF-II gene is observed in tumor formation especially in viral associated hepatocellular carcinoma.
21548981	5	49	theme	post-translational	1029:1046	arg1	modifications					1048:1060	post-translational modifications	1029:1060	post-translational modifications	1029:1060	Affinity of IGFBPs with IGFs is controlled by post-translational modifications.
21548981	10	50	theme	hepatocellular	1990:2003	arg1	carcinoma					2005:2013	hepatocellular carcinoma	1990:2013	hepatocellular carcinoma	1990:2013	We can conclude that during HCV/HBV infection, O-β-GlcNAc of IGFBP-6 at Ser 204 diminish their binding with IGF-II, increase IGF-II cellular expression and promote cancer progression which can lead to hepatocellular carcinoma.
21548981	1	51	theme	stimulator	263:272	arg1	gene					281:284	cell growth stimulator IGF-II gene	251:284	cell growth stimulator IGF-II gene	251:284	Hepatocellular carcinoma is mainly associated with viral hepatitis B and C. Activation of cell growth stimulator IGF-II gene is observed in tumor formation especially in viral associated hepatocellular carcinoma.
21548981	7	52	theme	functional	1320:1329	arg1	expression					1331:1340	the functional expression	1316:1340	the functional expression of cellular proteins	1316:1361	O-glycosylation and phosphorylation operate the functional expression of cellular proteins, this switching on and off the protein expression is difficult to monitor in vivo.
21548981	3	53	theme	core	600:603	arg1	protein					605:611	core protein	600:611	core protein	600:611	In HCV, core protein is believed to trans-activate host IGF-II receptor through PKC pathway and the inhibition of tumor cell growth can be achieved by blocking IGF-II pathway either at transcriptional level or increasing its binding with IGFBPs (Insulin like growth factor proteins) at C-terminal, so that it is not available in free form.
21548981	1	54	theme	gene	281:284	arg1	Activation					237:246	C. Activation	234:246	C. Activation of cell growth stimulator IGF-II gene	234:284	Hepatocellular carcinoma is mainly associated with viral hepatitis B and C. Activation of cell growth stimulator IGF-II gene is observed in tumor formation especially in viral associated hepatocellular carcinoma.
21548981	9	55	used	used	1645:1648	arg2	information					1626:1636	This information	1621:1636	This information	1621:1636	This information may be used for developing new therapies by regulating IGFBP-6 assembly with IGF-II to minimize the risk of viral associated hepatocellular carcinoma.
21548981	3	56	from	available	908:916	arg1	form					926:929	free form	921:929	free form	921:929	In HCV, core protein is believed to trans-activate host IGF-II receptor through PKC pathway and the inhibition of tumor cell growth can be achieved by blocking IGF-II pathway either at transcriptional level or increasing its binding with IGFBPs (Insulin like growth factor proteins) at C-terminal, so that it is not available in free form.
21548981	9	57	theme	viral	1746:1750	arg1	carcinoma					1778:1786	viral associated hepatocellular carcinoma	1746:1786	viral associated hepatocellular carcinoma	1746:1786	This information may be used for developing new therapies by regulating IGFBP-6 assembly with IGF-II to minimize the risk of viral associated hepatocellular carcinoma.
21548981	11	58	theme	viral	2117:2121	arg1	infection					2123:2131	viral infection	2117:2131	viral infection	2117:2131	Furthermore, this site can be used for developing new therapies to control the IGF-II actions during viral infection to minimize the risk of hepatocellular carcinoma.
21548981	3	59	dep	receptor	655:662	arg1	achieved					731:738	achieved	731:738	can be achieved by blocking IGF-II pathway either at transcriptional level or increasing its binding with IGFBPs (Insulin like growth factor proteins) at C-terminal, so that it is not available in free form	724:929	In HCV, core protein is believed to trans-activate host IGF-II receptor through PKC pathway and the inhibition of tumor cell growth can be achieved by blocking IGF-II pathway either at transcriptional level or increasing its binding with IGFBPs (Insulin like growth factor proteins) at C-terminal, so that it is not available in free form.
21548981	9	60	theme	hepatocellular	1763:1776	arg1	carcinoma					1778:1786	viral associated hepatocellular carcinoma	1746:1786	viral associated hepatocellular carcinoma	1746:1786	This information may be used for developing new therapies by regulating IGFBP-6 assembly with IGF-II to minimize the risk of viral associated hepatocellular carcinoma.
21548981	0	61	theme	mediated	126:133	arg1	carcinoma					150:158	viral mediated hepatocellular carcinoma	120:158	viral mediated hepatocellular carcinoma	120:158	Serine 204 phosphorylation and O-β-GlcNAC interplay of IGFBP-6 as therapeutic indicator to regulate IGF-II functions in viral mediated hepatocellular carcinoma.
21548981	1	62	theme	hepatitis	218:226	arg1	B					228:228	viral hepatitis B	212:228	viral hepatitis B	212:228	Hepatocellular carcinoma is mainly associated with viral hepatitis B and C. Activation of cell growth stimulator IGF-II gene is observed in tumor formation especially in viral associated hepatocellular carcinoma.
21548981	8	63	theme	alternate	1512:1520	arg1	modification					1533:1544	alternate O-β-GlcNAc modification	1512:1544	alternate O-β-GlcNAc modification	1512:1544	By using neural network based prediction methods, we propose that alternate O-β-GlcNAc modification and phosphorylation on Ser 204 control the binding of IGFBP-6 with IGF-II.
21548981	6	64	theme	cell	1202:1205	arg1	membranes					1207:1215	cell membranes	1202:1215	cell membranes	1202:1215	Phosphorylation of IGFBPs inhibits IGFs action on target cells while O-glycosylation prevents binding of IGFBP-6 to glycosaminoglycans and cell membranes and resulting in a 10-fold higher affinity for IGF-II.
21548981	3	65	theme	host	643:646	arg1	receptor					655:662	host IGF-II receptor	643:662	host IGF-II receptor through PKC pathway and the inhibition of tumor cell growth can be achieved by blocking IGF-II pathway either at transcriptional level or increasing its binding with IGFBPs (Insulin like growth factor proteins) at C-terminal, so that it is not available in free form	643:929	In HCV, core protein is believed to trans-activate host IGF-II receptor through PKC pathway and the inhibition of tumor cell growth can be achieved by blocking IGF-II pathway either at transcriptional level or increasing its binding with IGFBPs (Insulin like growth factor proteins) at C-terminal, so that it is not available in free form.
21548981	9	66	theme	carcinoma	1778:1786	arg1	risk					1738:1741	the risk	1734:1741	the risk of viral associated hepatocellular carcinoma	1734:1786	This information may be used for developing new therapies by regulating IGFBP-6 assembly with IGF-II to minimize the risk of viral associated hepatocellular carcinoma.
21548981	10	67	theme	IGF-II	1914:1919	arg1	expression					1930:1939	IGF-II cellular expression	1914:1939	IGF-II cellular expression	1914:1939	We can conclude that during HCV/HBV infection, O-β-GlcNAc of IGFBP-6 at Ser 204 diminish their binding with IGF-II, increase IGF-II cellular expression and promote cancer progression which can lead to hepatocellular carcinoma.
21548981	11	68	theme	hepatocellular	2157:2170	arg1	carcinoma					2172:2180	hepatocellular carcinoma	2157:2180	hepatocellular carcinoma	2157:2180	Furthermore, this site can be used for developing new therapies to control the IGF-II actions during viral infection to minimize the risk of hepatocellular carcinoma.
21548981	8	69	from	modification	1533:1544	arg1	Ser					1569:1571	Ser 204	1569:1575	Ser 204	1569:1575	By using neural network based prediction methods, we propose that alternate O-β-GlcNAc modification and phosphorylation on Ser 204 control the binding of IGFBP-6 with IGF-II.
21548981	3	70	theme	PKC	672:674	arg1	pathway					676:682	PKC pathway	672:682	PKC pathway	672:682	In HCV, core protein is believed to trans-activate host IGF-II receptor through PKC pathway and the inhibition of tumor cell growth can be achieved by blocking IGF-II pathway either at transcriptional level or increasing its binding with IGFBPs (Insulin like growth factor proteins) at C-terminal, so that it is not available in free form.
21548981	3	71	theme	growth	851:856	arg1	proteins					865:872	growth factor proteins	851:872	growth factor proteins	851:872	In HCV, core protein is believed to trans-activate host IGF-II receptor through PKC pathway and the inhibition of tumor cell growth can be achieved by blocking IGF-II pathway either at transcriptional level or increasing its binding with IGFBPs (Insulin like growth factor proteins) at C-terminal, so that it is not available in free form.
21548981	2	72	with	capacities	523:532	arg1	receptors					543:551	IGF receptors	539:551	IGF receptors leading to cellular dedifferentiation	539:589	Elevated IGF-II levels are indicator of increased risk for cholangiocellular and hepatocellular carcinomas through over saturation of IGF-II binding capacities with IGF receptors leading to cellular dedifferentiation.
21548981	3	73	theme	free	921:924	arg1	form					926:929	free form	921:929	free form	921:929	In HCV, core protein is believed to trans-activate host IGF-II receptor through PKC pathway and the inhibition of tumor cell growth can be achieved by blocking IGF-II pathway either at transcriptional level or increasing its binding with IGFBPs (Insulin like growth factor proteins) at C-terminal, so that it is not available in free form.
21548981	2	74	theme	IGF	539:541	arg1	receptors					543:551	IGF receptors	539:551	IGF receptors leading to cellular dedifferentiation	539:589	Elevated IGF-II levels are indicator of increased risk for cholangiocellular and hepatocellular carcinomas through over saturation of IGF-II binding capacities with IGF receptors leading to cellular dedifferentiation.
21548981	0	75	theme	IGF-II	100:105	arg1	functions					107:115	IGF-II functions	100:115	IGF-II functions	100:115	Serine 204 phosphorylation and O-β-GlcNAC interplay of IGFBP-6 as therapeutic indicator to regulate IGF-II functions in viral mediated hepatocellular carcinoma.
21548981	10	76	from	Ser	1861:1863	arg1	O-β-GlcNAc					1836:1845	O-β-GlcNAc	1836:1845	O-β-GlcNAc of IGFBP-6 at Ser 204	1836:1867	We can conclude that during HCV/HBV infection, O-β-GlcNAc of IGFBP-6 at Ser 204 diminish their binding with IGF-II, increase IGF-II cellular expression and promote cancer progression which can lead to hepatocellular carcinoma.
21548981	4	77	theme	IGF-II	967:972	arg1	actions					974:980	IGF-II actions	967:980	IGF-II actions	967:980	IGFBP-6 is a specific inhibitor of IGF-II actions.
21548981	8	78	theme	IGFBP-6	1600:1606	arg1	binding					1589:1595	the binding	1585:1595	the binding of IGFBP-6 with IGF-II	1585:1618	By using neural network based prediction methods, we propose that alternate O-β-GlcNAc modification and phosphorylation on Ser 204 control the binding of IGFBP-6 with IGF-II.
21548981	5	79	theme	IGFBPs	995:1000	arg1	Affinity					983:990	Affinity	983:990	Affinity of IGFBPs with IGFs	983:1010	Affinity of IGFBPs with IGFs is controlled by post-translational modifications.
21548981	6	80	theme	IGFBP-6	1168:1174	arg1	binding					1157:1163	binding	1157:1163	binding of IGFBP-6 to glycosaminoglycans and cell membranes	1157:1215	Phosphorylation of IGFBPs inhibits IGFs action on target cells while O-glycosylation prevents binding of IGFBP-6 to glycosaminoglycans and cell membranes and resulting in a 10-fold higher affinity for IGF-II.
21548981	8	81	from	phosphorylation	1550:1564	arg1	Ser					1569:1571	Ser 204	1569:1575	Ser 204	1569:1575	By using neural network based prediction methods, we propose that alternate O-β-GlcNAc modification and phosphorylation on Ser 204 control the binding of IGFBP-6 with IGF-II.
21548981	3	82	dep	IGFBPs	830:835	arg1	Insulin					838:844	Insulin	838:844	Insulin like growth factor proteins	838:872	In HCV, core protein is believed to trans-activate host IGF-II receptor through PKC pathway and the inhibition of tumor cell growth can be achieved by blocking IGF-II pathway either at transcriptional level or increasing its binding with IGFBPs (Insulin like growth factor proteins) at C-terminal, so that it is not available in free form.
21548981	2	83	theme	cellular	564:571	arg1	dedifferentiation					573:589	cellular dedifferentiation	564:589	cellular dedifferentiation	564:589	Elevated IGF-II levels are indicator of increased risk for cholangiocellular and hepatocellular carcinomas through over saturation of IGF-II binding capacities with IGF receptors leading to cellular dedifferentiation.
21548981	2	84	theme	risk	424:427	arg1	levels					390:395	Elevated IGF-II levels	374:395	Elevated IGF-II levels	374:395	Elevated IGF-II levels are indicator of increased risk for cholangiocellular and hepatocellular carcinomas through over saturation of IGF-II binding capacities with IGF receptors leading to cellular dedifferentiation.
21548981	2	84	theme	risk	424:427	arg1	indicator					401:409	indicator	401:409	indicator of increased risk for cholangiocellular and hepatocellular carcinomas	401:479	Elevated IGF-II levels are indicator of increased risk for cholangiocellular and hepatocellular carcinomas through over saturation of IGF-II binding capacities with IGF receptors leading to cellular dedifferentiation.
21548981	0	85	theme	204	7:9	arg1	phosphorylation					11:25	Serine 204 phosphorylation	0:25	Serine 204 phosphorylation	0:25	Serine 204 phosphorylation and O-β-GlcNAC interplay of IGFBP-6 as therapeutic indicator to regulate IGF-II functions in viral mediated hepatocellular carcinoma.
21548981	6	86	theme	target	1113:1118	arg1	cells					1120:1124	target cells	1113:1124	target cells	1113:1124	Phosphorylation of IGFBPs inhibits IGFs action on target cells while O-glycosylation prevents binding of IGFBP-6 to glycosaminoglycans and cell membranes and resulting in a 10-fold higher affinity for IGF-II.
21548981	3	87	with	binding	817:823	arg1	IGFBPs					830:835	IGFBPs	830:835	IGFBPs (Insulin like growth factor proteins)	830:873	In HCV, core protein is believed to trans-activate host IGF-II receptor through PKC pathway and the inhibition of tumor cell growth can be achieved by blocking IGF-II pathway either at transcriptional level or increasing its binding with IGFBPs (Insulin like growth factor proteins) at C-terminal, so that it is not available in free form.
21548981	3	88	theme	tumor	706:710	arg1	growth					717:722	tumor cell growth	706:722	tumor cell growth	706:722	In HCV, core protein is believed to trans-activate host IGF-II receptor through PKC pathway and the inhibition of tumor cell growth can be achieved by blocking IGF-II pathway either at transcriptional level or increasing its binding with IGFBPs (Insulin like growth factor proteins) at C-terminal, so that it is not available in free form.
21548981	2	89	theme	hepatocellular	455:468	arg1	carcinomas					470:479	cholangiocellular and hepatocellular carcinomas	433:479	cholangiocellular and hepatocellular carcinomas	433:479	Elevated IGF-II levels are indicator of increased risk for cholangiocellular and hepatocellular carcinomas through over saturation of IGF-II binding capacities with IGF receptors leading to cellular dedifferentiation.
21548981	9	90	theme	new	1665:1667	arg1	therapies					1669:1677	new therapies	1665:1677	new therapies	1665:1677	This information may be used for developing new therapies by regulating IGFBP-6 assembly with IGF-II to minimize the risk of viral associated hepatocellular carcinoma.
21548981	2	91	theme	capacities	523:532	arg1	saturation					494:503	saturation	494:503	saturation of IGF-II binding capacities with IGF receptors leading to cellular dedifferentiation	494:589	Elevated IGF-II levels are indicator of increased risk for cholangiocellular and hepatocellular carcinomas through over saturation of IGF-II binding capacities with IGF receptors leading to cellular dedifferentiation.
21548981	7	92	dep	operate	1308:1314	arg1	difficult					1416:1424	difficult	1416:1424	difficult	1416:1424	O-glycosylation and phosphorylation operate the functional expression of cellular proteins, this switching on and off the protein expression is difficult to monitor in vivo.
21548981	8	93	theme	neural	1455:1460	arg1	methods					1487:1493	neural network based prediction methods	1455:1493	neural network based prediction methods	1455:1493	By using neural network based prediction methods, we propose that alternate O-β-GlcNAc modification and phosphorylation on Ser 204 control the binding of IGFBP-6 with IGF-II.
21548981	2	94	theme	cholangiocellular	433:449	arg1	carcinomas					470:479	cholangiocellular and hepatocellular carcinomas	433:479	cholangiocellular and hepatocellular carcinomas	433:479	Elevated IGF-II levels are indicator of increased risk for cholangiocellular and hepatocellular carcinomas through over saturation of IGF-II binding capacities with IGF receptors leading to cellular dedifferentiation.
21548981	0	95	theme	IGFBP-6	55:61	arg1	phosphorylation					11:25	Serine 204 phosphorylation	0:25	Serine 204 phosphorylation	0:25	Serine 204 phosphorylation and O-β-GlcNAC interplay of IGFBP-6 as therapeutic indicator to regulate IGF-II functions in viral mediated hepatocellular carcinoma.
21548981	0	95	theme	IGFBP-6	55:61	arg1	interplay					42:50	O-β-GlcNAC interplay	31:50	O-β-GlcNAC interplay	31:50	Serine 204 phosphorylation and O-β-GlcNAC interplay of IGFBP-6 as therapeutic indicator to regulate IGF-II functions in viral mediated hepatocellular carcinoma.
21548981	7	96	dep	expression	1402:1411	arg1	off					1386:1388	off	1386:1388	off	1386:1388	O-glycosylation and phosphorylation operate the functional expression of cellular proteins, this switching on and off the protein expression is difficult to monitor in vivo.
21548981	2	97	theme	IGF-II	508:513	arg1	capacities					523:532	IGF-II binding capacities	508:532	IGF-II binding capacities with IGF receptors leading to cellular dedifferentiation	508:589	Elevated IGF-II levels are indicator of increased risk for cholangiocellular and hepatocellular carcinomas through over saturation of IGF-II binding capacities with IGF receptors leading to cellular dedifferentiation.
21548981	8	98	theme	based	1470:1474	arg1	methods					1487:1493	neural network based prediction methods	1455:1493	neural network based prediction methods	1455:1493	By using neural network based prediction methods, we propose that alternate O-β-GlcNAc modification and phosphorylation on Ser 204 control the binding of IGFBP-6 with IGF-II.
21548981	1	99	theme	associated	337:346	arg1	carcinoma					363:371	viral associated hepatocellular carcinoma	331:371	viral associated hepatocellular carcinoma	331:371	Hepatocellular carcinoma is mainly associated with viral hepatitis B and C. Activation of cell growth stimulator IGF-II gene is observed in tumor formation especially in viral associated hepatocellular carcinoma.
21548981	9	100	theme	IGFBP-6	1693:1699	arg1	assembly					1701:1708	IGFBP-6 assembly	1693:1708	IGFBP-6 assembly with IGF-II to minimize the risk of viral associated hepatocellular carcinoma	1693:1786	This information may be used for developing new therapies by regulating IGFBP-6 assembly with IGF-II to minimize the risk of viral associated hepatocellular carcinoma.
21548981	7	101	theme	cellular	1345:1352	arg1	proteins					1354:1361	cellular proteins	1345:1361	cellular proteins	1345:1361	O-glycosylation and phosphorylation operate the functional expression of cellular proteins, this switching on and off the protein expression is difficult to monitor in vivo.
21548981	3	102	theme	growth	717:722	arg1	pathway					676:682	PKC pathway	672:682	PKC pathway	672:682	In HCV, core protein is believed to trans-activate host IGF-II receptor through PKC pathway and the inhibition of tumor cell growth can be achieved by blocking IGF-II pathway either at transcriptional level or increasing its binding with IGFBPs (Insulin like growth factor proteins) at C-terminal, so that it is not available in free form.
21548981	3	102	theme	growth	717:722	arg1	inhibition					692:701	the inhibition	688:701	the inhibition of tumor cell growth	688:722	In HCV, core protein is believed to trans-activate host IGF-II receptor through PKC pathway and the inhibition of tumor cell growth can be achieved by blocking IGF-II pathway either at transcriptional level or increasing its binding with IGFBPs (Insulin like growth factor proteins) at C-terminal, so that it is not available in free form.
21548981	3	103	theme	IGF-II	752:757	arg1	pathway					759:765	IGF-II pathway	752:765	IGF-II pathway	752:765	In HCV, core protein is believed to trans-activate host IGF-II receptor through PKC pathway and the inhibition of tumor cell growth can be achieved by blocking IGF-II pathway either at transcriptional level or increasing its binding with IGFBPs (Insulin like growth factor proteins) at C-terminal, so that it is not available in free form.
21548981	1	104	theme	growth	256:261	arg1	gene					281:284	cell growth stimulator IGF-II gene	251:284	cell growth stimulator IGF-II gene	251:284	Hepatocellular carcinoma is mainly associated with viral hepatitis B and C. Activation of cell growth stimulator IGF-II gene is observed in tumor formation especially in viral associated hepatocellular carcinoma.
1991473	2	0	gly	N-glycosylated	268:281	arg2	Asn30					286:290	Asn30	286:290	Asn30	286:290	hLH alpha (N-glycosylated at Asn52 and Asn78) and hLH beta (N-glycosylated at Asn30).
1991473	2	0	gly	N-glycosylated	268:281	arg1	beta					262:265	hLH beta	258:265	hLH beta (N-glycosylated at Asn30)	258:291	hLH alpha (N-glycosylated at Asn52 and Asn78) and hLH beta (N-glycosylated at Asn30).
1991473	7	1	link	1-6-linked	1098:1107	arg1	residue					1084:1090	a fucose residue	1075:1090	a fucose residue alpha 1-6-linked	1075:1107	However, virtually all N-glycans on the beta subunit bear a fucose residue alpha 1-6-linked to the proximal GlcNAc, whereas those at Asn52 (and Asn78) of the alpha subunit are predominantly non-fucosylated.
1991473	2	2	theme	hLH	258:260	arg1	beta					262:265	hLH beta	258:265	hLH beta (N-glycosylated at Asn30)	258:291	hLH alpha (N-glycosylated at Asn52 and Asn78) and hLH beta (N-glycosylated at Asn30).
1991473	6	3	theme	4-sulphated	892:902	arg1	GalNAc					941:946	GalNAc	941:946	GalNAc	941:946	The oligosaccharides attached to Asn52 (hLH alpha) and Asn30 (hLH beta) show a remarkably similar pattern, with mainly chain-terminating 4-sulphated 2-deoxy-2-N-acetylamino-D-galactose (GalNAc) and a sulphated/sialylated structure as the major single component.
1991473	6	3	theme	4-sulphated	892:902	arg1	2-deoxy-2-N-acetylamino-D-galactose					904:938	mainly chain-terminating 4-sulphated 2-deoxy-2-N-acetylamino-D-galactose	867:938	mainly chain-terminating 4-sulphated 2-deoxy-2-N-acetylamino-D-galactose (GalNAc)	867:947	The oligosaccharides attached to Asn52 (hLH alpha) and Asn30 (hLH beta) show a remarkably similar pattern, with mainly chain-terminating 4-sulphated 2-deoxy-2-N-acetylamino-D-galactose (GalNAc) and a sulphated/sialylated structure as the major single component.
1991473	7	4	theme	alpha	1175:1179	arg1	subunit					1181:1187	the alpha subunit	1171:1187	the alpha subunit	1171:1187	However, virtually all N-glycans on the beta subunit bear a fucose residue alpha 1-6-linked to the proximal GlcNAc, whereas those at Asn52 (and Asn78) of the alpha subunit are predominantly non-fucosylated.
1991473	6	5	theme	single	999:1004	arg1	component					1006:1014	the major single component	989:1014	the major single component	989:1014	The oligosaccharides attached to Asn52 (hLH alpha) and Asn30 (hLH beta) show a remarkably similar pattern, with mainly chain-terminating 4-sulphated 2-deoxy-2-N-acetylamino-D-galactose (GalNAc) and a sulphated/sialylated structure as the major single component.
1991473	0	6	link	N-linked	26:33	arg1	oligosaccharides					35:50	the N-linked oligosaccharides	22:50	the N-linked oligosaccharides	22:50	NMR investigations of the N-linked oligosaccharides at individual glycosylation sites of human lutropin.
1991473	2	7	dep	alpha	212:216	arg1	N-glycosylated					219:232	N-glycosylated	219:232	N-glycosylated	219:232	hLH alpha (N-glycosylated at Asn52 and Asn78) and hLH beta (N-glycosylated at Asn30).
1991473	7	8	theme	1-6-linked	1098:1107	arg1	residue					1084:1090	a fucose residue	1075:1090	a fucose residue alpha 1-6-linked	1075:1107	However, virtually all N-glycans on the beta subunit bear a fucose residue alpha 1-6-linked to the proximal GlcNAc, whereas those at Asn52 (and Asn78) of the alpha subunit are predominantly non-fucosylated.
1991473	3	9	dep	two-dimensional	595:609	arg1	2D					612:613	2D	612:613	2D	612:613	The sugar chains were liberated by hydrazinolysis from intact hLH beta and from glycopeptides obtained after tryptic digestion of hLH alpha, subsequently reduced and fractionated as alditols by anion-exchange and ion-suppression amine-adsorption HPLC and identified mainly by one-dimensional (1D) and two-dimensional (2D) 1H-NMR spectroscopy.
1991473	8	10	theme	mono-	1423:1427	arg1	compounds					1446:1454	mono- and disialylated compounds	1423:1454	mono- and disialylated compounds	1423:1454	The oligosaccharides at Asn78 (hLH alpha) are sialylated rather than sulphated and contain the unique sequence NeuAc alpha 2-6 GalNAc beta 1-4GlcNAc beta 1-2 Man alpha 1-3 as part of the majority of mono- and disialylated compounds.
1991473	2	11	gly	N-glycosylated	219:232	arg2	Asn78					247:251	Asn78	247:251	Asn78	247:251	hLH alpha (N-glycosylated at Asn52 and Asn78) and hLH beta (N-glycosylated at Asn30).
1991473	2	11	gly	N-glycosylated	219:232	arg2	Asn52					237:241	Asn52	237:241	Asn52	237:241	hLH alpha (N-glycosylated at Asn52 and Asn78) and hLH beta (N-glycosylated at Asn30).
1991473	2	11	gly	N-glycosylated	219:232	arg1	alpha					212:216	hLH alpha	208:216	hLH alpha (N-glycosylated at Asn52 and Asn78)	208:252	hLH alpha (N-glycosylated at Asn52 and Asn78) and hLH beta (N-glycosylated at Asn30).
1991473	5	12	theme	glycosylation	734:746	arg1	sites					748:752	all three glycosylation sites	724:752	all three glycosylation sites	724:752	N-acetyllactosamine-type structures at all three glycosylation sites.
1991473	5	13	from	sites	748:752	arg1	structures					710:719	N-acetyllactosamine-type structures	685:719	N-acetyllactosamine-type structures at all three glycosylation sites	685:752	N-acetyllactosamine-type structures at all three glycosylation sites.
1991473	9	14	theme	single	1467:1472	arg1	constituent					1474:1484	The major single constituent	1457:1484	The major single constituent at Asn78	1457:1493	The major single constituent at Asn78 has the following structure: [formula, see text]
1991473	6	15	attach	attached	776:783	arg1	Asn52					788:792	Asn52	788:792	Asn52 (hLH alpha)	788:804	The oligosaccharides attached to Asn52 (hLH alpha) and Asn30 (hLH beta) show a remarkably similar pattern, with mainly chain-terminating 4-sulphated 2-deoxy-2-N-acetylamino-D-galactose (GalNAc) and a sulphated/sialylated structure as the major single component.
1991473	6	15	attach	attached	776:783	arg2	oligosaccharides					759:774	The oligosaccharides	755:774	The oligosaccharides attached to Asn52 (hLH alpha) and Asn30 (hLH beta)	755:825	The oligosaccharides attached to Asn52 (hLH alpha) and Asn30 (hLH beta) show a remarkably similar pattern, with mainly chain-terminating 4-sulphated 2-deoxy-2-N-acetylamino-D-galactose (GalNAc) and a sulphated/sialylated structure as the major single component.
1991473	6	15	attach	attached	776:783	arg1	alpha					799:803	hLH alpha	795:803	hLH alpha	795:803	The oligosaccharides attached to Asn52 (hLH alpha) and Asn30 (hLH beta) show a remarkably similar pattern, with mainly chain-terminating 4-sulphated 2-deoxy-2-N-acetylamino-D-galactose (GalNAc) and a sulphated/sialylated structure as the major single component.
1991473	6	15	attach	attached	776:783	arg1	Asn30					810:814	Asn30	810:814	Asn30 (hLH beta)	810:825	The oligosaccharides attached to Asn52 (hLH alpha) and Asn30 (hLH beta) show a remarkably similar pattern, with mainly chain-terminating 4-sulphated 2-deoxy-2-N-acetylamino-D-galactose (GalNAc) and a sulphated/sialylated structure as the major single component.
1991473	6	15	attach	attached	776:783	arg1	beta					821:824	hLH beta	817:824	hLH beta	817:824	The oligosaccharides attached to Asn52 (hLH alpha) and Asn30 (hLH beta) show a remarkably similar pattern, with mainly chain-terminating 4-sulphated 2-deoxy-2-N-acetylamino-D-galactose (GalNAc) and a sulphated/sialylated structure as the major single component.
1991473	8	16	theme	disialylated	1433:1444	arg1	compounds					1446:1454	mono- and disialylated compounds	1423:1454	mono- and disialylated compounds	1423:1454	The oligosaccharides at Asn78 (hLH alpha) are sialylated rather than sulphated and contain the unique sequence NeuAc alpha 2-6 GalNAc beta 1-4GlcNAc beta 1-2 Man alpha 1-3 as part of the majority of mono- and disialylated compounds.
1991473	5	17	theme	N-acetyllactosamine-type	685:708	arg1	structures					710:719	N-acetyllactosamine-type structures	685:719	N-acetyllactosamine-type structures at all three glycosylation sites	685:752	N-acetyllactosamine-type structures at all three glycosylation sites.
1991473	2	18	theme	hLH	208:210	arg1	alpha					212:216	hLH alpha	208:216	hLH alpha (N-glycosylated at Asn52 and Asn78)	208:252	hLH alpha (N-glycosylated at Asn52 and Asn78) and hLH beta (N-glycosylated at Asn30).
1991473	1	19	theme	luteinizing	123:133	arg1	hormone					135:141	luteinizing hormone	123:141	luteinizing hormone	123:141	Human lutropin or luteinizing hormone (hLH) is a heterodimeric glycoprotein, composed of two subunits.
1991473	1	19	theme	luteinizing	123:133	arg1	glycoprotein					168:179	a heterodimeric glycoprotein	152:179	a heterodimeric glycoprotein	152:179	Human lutropin or luteinizing hormone (hLH) is a heterodimeric glycoprotein, composed of two subunits.
1991473	1	19	theme	luteinizing	123:133	arg1	lutropin					111:118	Human lutropin	105:118	Human lutropin	105:118	Human lutropin or luteinizing hormone (hLH) is a heterodimeric glycoprotein, composed of two subunits.
1991473	5	20	gly	glycosylation	734:746	arg2	sites					748:752	all three glycosylation sites	724:752	all three glycosylation sites	724:752	N-acetyllactosamine-type structures at all three glycosylation sites.
1991473	5	20	gly	glycosylation	734:746	arg2	three					728:732	three	728:732	three	728:732	N-acetyllactosamine-type structures at all three glycosylation sites.
1991473	8	21	gly	sialylated	1270:1279	arg1	oligosaccharides					1228:1243	The oligosaccharides	1224:1243	The oligosaccharides at Asn78 (hLH alpha)	1224:1264	The oligosaccharides at Asn78 (hLH alpha) are sialylated rather than sulphated and contain the unique sequence NeuAc alpha 2-6 GalNAc beta 1-4GlcNAc beta 1-2 Man alpha 1-3 as part of the majority of mono- and disialylated compounds.
1991473	9	22	dep	[formula	1524:1531	arg1	see					1534:1536	see	1534:1536	see text	1534:1541	The major single constituent at Asn78 has the following structure: [formula, see text]
1991473	8	23	theme	unique	1319:1324	arg1	beta					1373:1376	the unique sequence NeuAc alpha 2-6 GalNAc beta 1-4GlcNAc beta	1315:1376	the unique sequence NeuAc alpha 2-6 GalNAc beta 1-4GlcNAc beta 1-2 Man alpha 1-3	1315:1394	The oligosaccharides at Asn78 (hLH alpha) are sialylated rather than sulphated and contain the unique sequence NeuAc alpha 2-6 GalNAc beta 1-4GlcNAc beta 1-2 Man alpha 1-3 as part of the majority of mono- and disialylated compounds.
1991473	0	24	theme	glycosylation	66:78	arg1	sites					80:84	individual glycosylation sites	55:84	individual glycosylation sites of human lutropin	55:102	NMR investigations of the N-linked oligosaccharides at individual glycosylation sites of human lutropin.
1991473	0	24	theme	glycosylation	66:78	arg1	lutropin					95:102	human lutropin	89:102	human lutropin	89:102	NMR investigations of the N-linked oligosaccharides at individual glycosylation sites of human lutropin.
1991473	3	25	theme	two-dimensional	595:609	arg1	spectroscopy					623:634	one-dimensional (1D) and two-dimensional (2D) 1H-NMR spectroscopy	570:634	one-dimensional (1D) and two-dimensional (2D) 1H-NMR spectroscopy	570:634	The sugar chains were liberated by hydrazinolysis from intact hLH beta and from glycopeptides obtained after tryptic digestion of hLH alpha, subsequently reduced and fractionated as alditols by anion-exchange and ion-suppression amine-adsorption HPLC and identified mainly by one-dimensional (1D) and two-dimensional (2D) 1H-NMR spectroscopy.
1991473	9	26	theme	following	1503:1511	arg1	structure					1513:1521	the following structure	1499:1521	the following structure	1499:1521	The major single constituent at Asn78 has the following structure: [formula, see text]
1991473	3	27	attach	liberated	316:324	arg2	chains					304:309	The sugar chains	294:309	The sugar chains	294:309	The sugar chains were liberated by hydrazinolysis from intact hLH beta and from glycopeptides obtained after tryptic digestion of hLH alpha, subsequently reduced and fractionated as alditols by anion-exchange and ion-suppression amine-adsorption HPLC and identified mainly by one-dimensional (1D) and two-dimensional (2D) 1H-NMR spectroscopy.
1991473	3	27	attach	liberated	316:324	arg1	beta					360:363	intact hLH beta	349:363	intact hLH beta	349:363	The sugar chains were liberated by hydrazinolysis from intact hLH beta and from glycopeptides obtained after tryptic digestion of hLH alpha, subsequently reduced and fractionated as alditols by anion-exchange and ion-suppression amine-adsorption HPLC and identified mainly by one-dimensional (1D) and two-dimensional (2D) 1H-NMR spectroscopy.
1991473	3	27	attach	liberated	316:324	arg1	glycopeptides					374:386	glycopeptides	374:386	glycopeptides obtained after tryptic digestion of hLH alpha	374:432	The sugar chains were liberated by hydrazinolysis from intact hLH beta and from glycopeptides obtained after tryptic digestion of hLH alpha, subsequently reduced and fractionated as alditols by anion-exchange and ion-suppression amine-adsorption HPLC and identified mainly by one-dimensional (1D) and two-dimensional (2D) 1H-NMR spectroscopy.
1991473	2	28	dep	beta	262:265	arg1	N-glycosylated					268:281	N-glycosylated	268:281	N-glycosylated	268:281	hLH alpha (N-glycosylated at Asn52 and Asn78) and hLH beta (N-glycosylated at Asn30).
1991473	2	29	from	Asn30	286:290	arg1	N-glycosylated					268:281	N-glycosylated	268:281	N-glycosylated	268:281	hLH alpha (N-glycosylated at Asn52 and Asn78) and hLH beta (N-glycosylated at Asn30).
1991473	7	30	gly	non-fucosylated	1207:1221	arg1	those					1141:1145	those	1141:1145	those	1141:1145	However, virtually all N-glycans on the beta subunit bear a fucose residue alpha 1-6-linked to the proximal GlcNAc, whereas those at Asn52 (and Asn78) of the alpha subunit are predominantly non-fucosylated.
1991473	0	31	theme	lutropin	95:102	arg1	sites					80:84	individual glycosylation sites	55:84	individual glycosylation sites of human lutropin	55:102	NMR investigations of the N-linked oligosaccharides at individual glycosylation sites of human lutropin.
1991473	0	31	theme	lutropin	95:102	arg1	lutropin					95:102	human lutropin	89:102	human lutropin	89:102	NMR investigations of the N-linked oligosaccharides at individual glycosylation sites of human lutropin.
1991473	8	32	theme	beta	1358:1361	arg1	beta					1373:1376	the unique sequence NeuAc alpha 2-6 GalNAc beta 1-4GlcNAc beta	1315:1376	the unique sequence NeuAc alpha 2-6 GalNAc beta 1-4GlcNAc beta 1-2 Man alpha 1-3	1315:1394	The oligosaccharides at Asn78 (hLH alpha) are sialylated rather than sulphated and contain the unique sequence NeuAc alpha 2-6 GalNAc beta 1-4GlcNAc beta 1-2 Man alpha 1-3 as part of the majority of mono- and disialylated compounds.
1991473	3	33	theme	tryptic	403:409	arg1	digestion					411:419	tryptic digestion	403:419	tryptic digestion of hLH alpha	403:432	The sugar chains were liberated by hydrazinolysis from intact hLH beta and from glycopeptides obtained after tryptic digestion of hLH alpha, subsequently reduced and fractionated as alditols by anion-exchange and ion-suppression amine-adsorption HPLC and identified mainly by one-dimensional (1D) and two-dimensional (2D) 1H-NMR spectroscopy.
1991473	3	34	theme	intact	349:354	arg1	beta					360:363	intact hLH beta	349:363	intact hLH beta	349:363	The sugar chains were liberated by hydrazinolysis from intact hLH beta and from glycopeptides obtained after tryptic digestion of hLH alpha, subsequently reduced and fractionated as alditols by anion-exchange and ion-suppression amine-adsorption HPLC and identified mainly by one-dimensional (1D) and two-dimensional (2D) 1H-NMR spectroscopy.
1991473	7	35	contain	bear	1070:1073	arg1	N-glycans					1040:1048	virtually all N-glycans	1026:1048	virtually all N-glycans on the beta subunit	1026:1068	However, virtually all N-glycans on the beta subunit bear a fucose residue alpha 1-6-linked to the proximal GlcNAc, whereas those at Asn52 (and Asn78) of the alpha subunit are predominantly non-fucosylated.
1991473	7	35	contain	bear	1070:1073	arg2	residue					1084:1090	a fucose residue	1075:1090	a fucose residue alpha 1-6-linked	1075:1107	However, virtually all N-glycans on the beta subunit bear a fucose residue alpha 1-6-linked to the proximal GlcNAc, whereas those at Asn52 (and Asn78) of the alpha subunit are predominantly non-fucosylated.
1991473	0	36	theme	NMR	0:2	arg1	investigations					4:17	NMR investigations	0:17	NMR investigations of the N-linked oligosaccharides at individual glycosylation sites of human lutropin	0:102	NMR investigations of the N-linked oligosaccharides at individual glycosylation sites of human lutropin.
1991473	2	37	from	Asn52	237:241	arg1	N-glycosylated					219:232	N-glycosylated	219:232	N-glycosylated	219:232	hLH alpha (N-glycosylated at Asn52 and Asn78) and hLH beta (N-glycosylated at Asn30).
1991473	9	38	contain	has	1495:1497	arg1	constituent					1474:1484	The major single constituent	1457:1484	The major single constituent at Asn78	1457:1493	The major single constituent at Asn78 has the following structure: [formula, see text]
1991473	9	38	contain	has	1495:1497	arg2	structure					1513:1521	the following structure	1499:1521	the following structure	1499:1521	The major single constituent at Asn78 has the following structure: [formula, see text]
1991473	8	39	theme	Man	1382:1384	arg1	alpha					1386:1390	1-2 Man alpha 1-3	1378:1394	the unique sequence NeuAc alpha 2-6 GalNAc beta 1-4GlcNAc beta 1-2 Man alpha 1-3	1315:1394	The oligosaccharides at Asn78 (hLH alpha) are sialylated rather than sulphated and contain the unique sequence NeuAc alpha 2-6 GalNAc beta 1-4GlcNAc beta 1-2 Man alpha 1-3 as part of the majority of mono- and disialylated compounds.
1991473	3	40	theme	alpha	428:432	arg1	digestion					411:419	tryptic digestion	403:419	tryptic digestion of hLH alpha	403:432	The sugar chains were liberated by hydrazinolysis from intact hLH beta and from glycopeptides obtained after tryptic digestion of hLH alpha, subsequently reduced and fractionated as alditols by anion-exchange and ion-suppression amine-adsorption HPLC and identified mainly by one-dimensional (1D) and two-dimensional (2D) 1H-NMR spectroscopy.
1991473	2	41	from	Asn78	247:251	arg1	N-glycosylated					219:232	N-glycosylated	219:232	N-glycosylated	219:232	hLH alpha (N-glycosylated at Asn52 and Asn78) and hLH beta (N-glycosylated at Asn30).
1991473	1	42	theme	heterodimeric	154:166	arg1	hormone					135:141	luteinizing hormone	123:141	luteinizing hormone	123:141	Human lutropin or luteinizing hormone (hLH) is a heterodimeric glycoprotein, composed of two subunits.
1991473	1	42	theme	heterodimeric	154:166	arg1	glycoprotein					168:179	a heterodimeric glycoprotein	152:179	a heterodimeric glycoprotein	152:179	Human lutropin or luteinizing hormone (hLH) is a heterodimeric glycoprotein, composed of two subunits.
1991473	1	42	theme	heterodimeric	154:166	arg1	lutropin					111:118	Human lutropin	105:118	Human lutropin	105:118	Human lutropin or luteinizing hormone (hLH) is a heterodimeric glycoprotein, composed of two subunits.
1991473	0	43	theme	N-linked	26:33	arg1	oligosaccharides					35:50	the N-linked oligosaccharides	22:50	the N-linked oligosaccharides	22:50	NMR investigations of the N-linked oligosaccharides at individual glycosylation sites of human lutropin.
1991473	3	44	theme	1H-NMR	616:621	arg1	spectroscopy					623:634	one-dimensional (1D) and two-dimensional (2D) 1H-NMR spectroscopy	570:634	one-dimensional (1D) and two-dimensional (2D) 1H-NMR spectroscopy	570:634	The sugar chains were liberated by hydrazinolysis from intact hLH beta and from glycopeptides obtained after tryptic digestion of hLH alpha, subsequently reduced and fractionated as alditols by anion-exchange and ion-suppression amine-adsorption HPLC and identified mainly by one-dimensional (1D) and two-dimensional (2D) 1H-NMR spectroscopy.
1991473	3	45	dep	liberated	316:324	arg1	fractionated					460:471	fractionated	460:471	fractionated as alditols by anion-exchange and ion-suppression amine-adsorption HPLC	460:543	The sugar chains were liberated by hydrazinolysis from intact hLH beta and from glycopeptides obtained after tryptic digestion of hLH alpha, subsequently reduced and fractionated as alditols by anion-exchange and ion-suppression amine-adsorption HPLC and identified mainly by one-dimensional (1D) and two-dimensional (2D) 1H-NMR spectroscopy.
1991473	3	45	dep	liberated	316:324	arg1	reduced					448:454	reduced	448:454	reduced	448:454	The sugar chains were liberated by hydrazinolysis from intact hLH beta and from glycopeptides obtained after tryptic digestion of hLH alpha, subsequently reduced and fractionated as alditols by anion-exchange and ion-suppression amine-adsorption HPLC and identified mainly by one-dimensional (1D) and two-dimensional (2D) 1H-NMR spectroscopy.
1991473	3	46	theme	ion-suppression	507:521	arg1	HPLC					540:543	anion-exchange and ion-suppression amine-adsorption HPLC	488:543	HPLC	540:543	The sugar chains were liberated by hydrazinolysis from intact hLH beta and from glycopeptides obtained after tryptic digestion of hLH alpha, subsequently reduced and fractionated as alditols by anion-exchange and ion-suppression amine-adsorption HPLC and identified mainly by one-dimensional (1D) and two-dimensional (2D) 1H-NMR spectroscopy.
1991473	1	47	gly	glycoprotein	168:179	arg1	hormone					135:141	luteinizing hormone	123:141	luteinizing hormone	123:141	Human lutropin or luteinizing hormone (hLH) is a heterodimeric glycoprotein, composed of two subunits.
1991473	1	47	gly	glycoprotein	168:179	arg1	glycoprotein					168:179	a heterodimeric glycoprotein	152:179	a heterodimeric glycoprotein	152:179	Human lutropin or luteinizing hormone (hLH) is a heterodimeric glycoprotein, composed of two subunits.
1991473	1	47	gly	glycoprotein	168:179	arg1	lutropin					111:118	Human lutropin	105:118	Human lutropin	105:118	Human lutropin or luteinizing hormone (hLH) is a heterodimeric glycoprotein, composed of two subunits.
1991473	6	48	theme	hLH	817:819	arg1	Asn30					810:814	Asn30	810:814	Asn30 (hLH beta)	810:825	The oligosaccharides attached to Asn52 (hLH alpha) and Asn30 (hLH beta) show a remarkably similar pattern, with mainly chain-terminating 4-sulphated 2-deoxy-2-N-acetylamino-D-galactose (GalNAc) and a sulphated/sialylated structure as the major single component.
1991473	6	48	theme	hLH	817:819	arg1	beta					821:824	hLH beta	817:824	hLH beta	817:824	The oligosaccharides attached to Asn52 (hLH alpha) and Asn30 (hLH beta) show a remarkably similar pattern, with mainly chain-terminating 4-sulphated 2-deoxy-2-N-acetylamino-D-galactose (GalNAc) and a sulphated/sialylated structure as the major single component.
1991473	3	49	theme	amine-adsorption	523:538	arg1	HPLC					540:543	anion-exchange and ion-suppression amine-adsorption HPLC	488:543	HPLC	540:543	The sugar chains were liberated by hydrazinolysis from intact hLH beta and from glycopeptides obtained after tryptic digestion of hLH alpha, subsequently reduced and fractionated as alditols by anion-exchange and ion-suppression amine-adsorption HPLC and identified mainly by one-dimensional (1D) and two-dimensional (2D) 1H-NMR spectroscopy.
1991473	8	50	theme	NeuAc	1335:1339	arg1	beta					1373:1376	the unique sequence NeuAc alpha 2-6 GalNAc beta 1-4GlcNAc beta	1315:1376	the unique sequence NeuAc alpha 2-6 GalNAc beta 1-4GlcNAc beta 1-2 Man alpha 1-3	1315:1394	The oligosaccharides at Asn78 (hLH alpha) are sialylated rather than sulphated and contain the unique sequence NeuAc alpha 2-6 GalNAc beta 1-4GlcNAc beta 1-2 Man alpha 1-3 as part of the majority of mono- and disialylated compounds.
1991473	7	51	dep	bear	1070:1073	arg1	whereas					1133:1139	whereas	1133:1139	whereas	1133:1139	However, virtually all N-glycans on the beta subunit bear a fucose residue alpha 1-6-linked to the proximal GlcNAc, whereas those at Asn52 (and Asn78) of the alpha subunit are predominantly non-fucosylated.
1991473	7	52	theme	proximal	1116:1123	arg1	GlcNAc					1125:1130	the proximal GlcNAc	1112:1130	the proximal GlcNAc	1112:1130	However, virtually all N-glycans on the beta subunit bear a fucose residue alpha 1-6-linked to the proximal GlcNAc, whereas those at Asn52 (and Asn78) of the alpha subunit are predominantly non-fucosylated.
1991473	6	53	gly	sulphated/sialylated	955:974	arg1	structure					976:984	a sulphated/sialylated structure	953:984	a sulphated/sialylated structure as the major single component	953:1014	The oligosaccharides attached to Asn52 (hLH alpha) and Asn30 (hLH beta) show a remarkably similar pattern, with mainly chain-terminating 4-sulphated 2-deoxy-2-N-acetylamino-D-galactose (GalNAc) and a sulphated/sialylated structure as the major single component.
1991473	8	54	dep	beta	1373:1376	arg1	alpha					1386:1390	1-2 Man alpha 1-3	1378:1394	the unique sequence NeuAc alpha 2-6 GalNAc beta 1-4GlcNAc beta 1-2 Man alpha 1-3	1315:1394	The oligosaccharides at Asn78 (hLH alpha) are sialylated rather than sulphated and contain the unique sequence NeuAc alpha 2-6 GalNAc beta 1-4GlcNAc beta 1-2 Man alpha 1-3 as part of the majority of mono- and disialylated compounds.
1991473	3	55	dep	one-dimensional	570:584	arg1	1D					587:588	1D	587:588	1D	587:588	The sugar chains were liberated by hydrazinolysis from intact hLH beta and from glycopeptides obtained after tryptic digestion of hLH alpha, subsequently reduced and fractionated as alditols by anion-exchange and ion-suppression amine-adsorption HPLC and identified mainly by one-dimensional (1D) and two-dimensional (2D) 1H-NMR spectroscopy.
1991473	6	56	theme	chain-terminating	874:890	arg1	GalNAc					941:946	GalNAc	941:946	GalNAc	941:946	The oligosaccharides attached to Asn52 (hLH alpha) and Asn30 (hLH beta) show a remarkably similar pattern, with mainly chain-terminating 4-sulphated 2-deoxy-2-N-acetylamino-D-galactose (GalNAc) and a sulphated/sialylated structure as the major single component.
1991473	6	56	theme	chain-terminating	874:890	arg1	2-deoxy-2-N-acetylamino-D-galactose					904:938	mainly chain-terminating 4-sulphated 2-deoxy-2-N-acetylamino-D-galactose	867:938	mainly chain-terminating 4-sulphated 2-deoxy-2-N-acetylamino-D-galactose (GalNAc)	867:947	The oligosaccharides attached to Asn52 (hLH alpha) and Asn30 (hLH beta) show a remarkably similar pattern, with mainly chain-terminating 4-sulphated 2-deoxy-2-N-acetylamino-D-galactose (GalNAc) and a sulphated/sialylated structure as the major single component.
1991473	9	57	from	Asn78	1489:1493	arg1	constituent					1474:1484	The major single constituent	1457:1484	The major single constituent at Asn78	1457:1493	The major single constituent at Asn78 has the following structure: [formula, see text]
1991473	8	58	gly	disialylated	1433:1444	arg1	compounds					1446:1454	mono- and disialylated compounds	1423:1454	mono- and disialylated compounds	1423:1454	The oligosaccharides at Asn78 (hLH alpha) are sialylated rather than sulphated and contain the unique sequence NeuAc alpha 2-6 GalNAc beta 1-4GlcNAc beta 1-2 Man alpha 1-3 as part of the majority of mono- and disialylated compounds.
1991473	8	59	theme	hLH	1255:1257	arg1	Asn78					1248:1252	Asn78	1248:1252	Asn78 (hLH alpha)	1248:1264	The oligosaccharides at Asn78 (hLH alpha) are sialylated rather than sulphated and contain the unique sequence NeuAc alpha 2-6 GalNAc beta 1-4GlcNAc beta 1-2 Man alpha 1-3 as part of the majority of mono- and disialylated compounds.
1991473	8	59	theme	hLH	1255:1257	arg1	alpha					1259:1263	hLH alpha	1255:1263	hLH alpha	1255:1263	The oligosaccharides at Asn78 (hLH alpha) are sialylated rather than sulphated and contain the unique sequence NeuAc alpha 2-6 GalNAc beta 1-4GlcNAc beta 1-2 Man alpha 1-3 as part of the majority of mono- and disialylated compounds.
1991473	6	60	theme	hLH	795:797	arg1	Asn52					788:792	Asn52	788:792	Asn52 (hLH alpha)	788:804	The oligosaccharides attached to Asn52 (hLH alpha) and Asn30 (hLH beta) show a remarkably similar pattern, with mainly chain-terminating 4-sulphated 2-deoxy-2-N-acetylamino-D-galactose (GalNAc) and a sulphated/sialylated structure as the major single component.
1991473	6	60	theme	hLH	795:797	arg1	alpha					799:803	hLH alpha	795:803	hLH alpha	795:803	The oligosaccharides attached to Asn52 (hLH alpha) and Asn30 (hLH beta) show a remarkably similar pattern, with mainly chain-terminating 4-sulphated 2-deoxy-2-N-acetylamino-D-galactose (GalNAc) and a sulphated/sialylated structure as the major single component.
1991473	6	61	theme	major	993:997	arg1	component					1006:1014	the major single component	989:1014	the major single component	989:1014	The oligosaccharides attached to Asn52 (hLH alpha) and Asn30 (hLH beta) show a remarkably similar pattern, with mainly chain-terminating 4-sulphated 2-deoxy-2-N-acetylamino-D-galactose (GalNAc) and a sulphated/sialylated structure as the major single component.
1991473	7	62	from	N-glycans	1040:1048	arg1	subunit					1062:1068	the beta subunit	1053:1068	the beta subunit	1053:1068	However, virtually all N-glycans on the beta subunit bear a fucose residue alpha 1-6-linked to the proximal GlcNAc, whereas those at Asn52 (and Asn78) of the alpha subunit are predominantly non-fucosylated.
1991473	7	63	theme	fucose	1077:1082	arg1	residue					1084:1090	a fucose residue	1075:1090	a fucose residue alpha 1-6-linked	1075:1107	However, virtually all N-glycans on the beta subunit bear a fucose residue alpha 1-6-linked to the proximal GlcNAc, whereas those at Asn52 (and Asn78) of the alpha subunit are predominantly non-fucosylated.
1991473	9	64	theme	major	1461:1465	arg1	constituent					1474:1484	The major single constituent	1457:1484	The major single constituent at Asn78	1457:1493	The major single constituent at Asn78 has the following structure: [formula, see text]
1991473	0	65	from	sites	80:84	arg1	investigations					4:17	NMR investigations	0:17	NMR investigations of the N-linked oligosaccharides at individual glycosylation sites of human lutropin	0:102	NMR investigations of the N-linked oligosaccharides at individual glycosylation sites of human lutropin.
1991473	3	66	theme	one-dimensional	570:584	arg1	spectroscopy					623:634	one-dimensional (1D) and two-dimensional (2D) 1H-NMR spectroscopy	570:634	one-dimensional (1D) and two-dimensional (2D) 1H-NMR spectroscopy	570:634	The sugar chains were liberated by hydrazinolysis from intact hLH beta and from glycopeptides obtained after tryptic digestion of hLH alpha, subsequently reduced and fractionated as alditols by anion-exchange and ion-suppression amine-adsorption HPLC and identified mainly by one-dimensional (1D) and two-dimensional (2D) 1H-NMR spectroscopy.
1991473	6	67	theme	sulphated/sialylated	955:974	arg1	structure					976:984	a sulphated/sialylated structure	953:984	a sulphated/sialylated structure as the major single component	953:1014	The oligosaccharides attached to Asn52 (hLH alpha) and Asn30 (hLH beta) show a remarkably similar pattern, with mainly chain-terminating 4-sulphated 2-deoxy-2-N-acetylamino-D-galactose (GalNAc) and a sulphated/sialylated structure as the major single component.
1991473	8	68	contain	contain	1307:1313	arg2	beta					1373:1376	the unique sequence NeuAc alpha 2-6 GalNAc beta 1-4GlcNAc beta	1315:1376	the unique sequence NeuAc alpha 2-6 GalNAc beta 1-4GlcNAc beta 1-2 Man alpha 1-3	1315:1394	The oligosaccharides at Asn78 (hLH alpha) are sialylated rather than sulphated and contain the unique sequence NeuAc alpha 2-6 GalNAc beta 1-4GlcNAc beta 1-2 Man alpha 1-3 as part of the majority of mono- and disialylated compounds.
1991473	8	68	contain	contain	1307:1313	arg1	oligosaccharides					1228:1243	The oligosaccharides	1224:1243	The oligosaccharides at Asn78 (hLH alpha)	1224:1264	The oligosaccharides at Asn78 (hLH alpha) are sialylated rather than sulphated and contain the unique sequence NeuAc alpha 2-6 GalNAc beta 1-4GlcNAc beta 1-2 Man alpha 1-3 as part of the majority of mono- and disialylated compounds.
1991473	7	69	theme	beta	1057:1060	arg1	subunit					1062:1068	the beta subunit	1053:1068	the beta subunit	1053:1068	However, virtually all N-glycans on the beta subunit bear a fucose residue alpha 1-6-linked to the proximal GlcNAc, whereas those at Asn52 (and Asn78) of the alpha subunit are predominantly non-fucosylated.
1991473	8	70	from	Asn78	1248:1252	arg1	oligosaccharides					1228:1243	The oligosaccharides	1224:1243	The oligosaccharides at Asn78 (hLH alpha)	1224:1264	The oligosaccharides at Asn78 (hLH alpha) are sialylated rather than sulphated and contain the unique sequence NeuAc alpha 2-6 GalNAc beta 1-4GlcNAc beta 1-2 Man alpha 1-3 as part of the majority of mono- and disialylated compounds.
1991473	3	71	theme	sugar	298:302	arg1	chains					304:309	The sugar chains	294:309	The sugar chains	294:309	The sugar chains were liberated by hydrazinolysis from intact hLH beta and from glycopeptides obtained after tryptic digestion of hLH alpha, subsequently reduced and fractionated as alditols by anion-exchange and ion-suppression amine-adsorption HPLC and identified mainly by one-dimensional (1D) and two-dimensional (2D) 1H-NMR spectroscopy.
1991473	1	72	dep	lutropin	111:118	arg1	hLH					144:146	hLH	144:146	hLH	144:146	Human lutropin or luteinizing hormone (hLH) is a heterodimeric glycoprotein, composed of two subunits.
1991473	0	73	theme	human	89:93	arg1	lutropin					95:102	human lutropin	89:102	human lutropin	89:102	NMR investigations of the N-linked oligosaccharides at individual glycosylation sites of human lutropin.
1991473	3	74	gly	glycopeptides	374:386	arg2	glycopeptides					374:386	glycopeptides	374:386	glycopeptides obtained after tryptic digestion of hLH alpha	374:432	The sugar chains were liberated by hydrazinolysis from intact hLH beta and from glycopeptides obtained after tryptic digestion of hLH alpha, subsequently reduced and fractionated as alditols by anion-exchange and ion-suppression amine-adsorption HPLC and identified mainly by one-dimensional (1D) and two-dimensional (2D) 1H-NMR spectroscopy.
1991473	8	75	theme	sequence	1326:1333	arg1	beta					1373:1376	the unique sequence NeuAc alpha 2-6 GalNAc beta 1-4GlcNAc beta	1315:1376	the unique sequence NeuAc alpha 2-6 GalNAc beta 1-4GlcNAc beta 1-2 Man alpha 1-3	1315:1394	The oligosaccharides at Asn78 (hLH alpha) are sialylated rather than sulphated and contain the unique sequence NeuAc alpha 2-6 GalNAc beta 1-4GlcNAc beta 1-2 Man alpha 1-3 as part of the majority of mono- and disialylated compounds.
1991473	0	76	gly	glycosylation	66:78	arg1	lutropin					95:102	human lutropin	89:102	human lutropin	89:102	NMR investigations of the N-linked oligosaccharides at individual glycosylation sites of human lutropin.
1991473	0	76	gly	glycosylation	66:78	arg2	sites					80:84	individual glycosylation sites	55:84	individual glycosylation sites of human lutropin	55:102	NMR investigations of the N-linked oligosaccharides at individual glycosylation sites of human lutropin.
1991473	0	76	gly	glycosylation	66:78	arg2	lutropin					95:102	human lutropin	89:102	human lutropin	89:102	NMR investigations of the N-linked oligosaccharides at individual glycosylation sites of human lutropin.
1991473	9	77	dep	has	1495:1497	arg1	[formula					1524:1531	[formula	1524:1531	[formula, see text]	1524:1542	The major single constituent at Asn78 has the following structure: [formula, see text]
1991473	8	78	theme	alpha	1341:1345	arg1	beta					1373:1376	the unique sequence NeuAc alpha 2-6 GalNAc beta 1-4GlcNAc beta	1315:1376	the unique sequence NeuAc alpha 2-6 GalNAc beta 1-4GlcNAc beta 1-2 Man alpha 1-3	1315:1394	The oligosaccharides at Asn78 (hLH alpha) are sialylated rather than sulphated and contain the unique sequence NeuAc alpha 2-6 GalNAc beta 1-4GlcNAc beta 1-2 Man alpha 1-3 as part of the majority of mono- and disialylated compounds.
1991473	7	79	theme	subunit	1181:1187	arg1	Asn52					1150:1154	Asn52	1150:1154	Asn52 (and Asn78) of the alpha subunit	1150:1187	However, virtually all N-glycans on the beta subunit bear a fucose residue alpha 1-6-linked to the proximal GlcNAc, whereas those at Asn52 (and Asn78) of the alpha subunit are predominantly non-fucosylated.
1991473	7	79	theme	subunit	1181:1187	arg1	Asn78					1161:1165	Asn78	1161:1165	Asn78	1161:1165	However, virtually all N-glycans on the beta subunit bear a fucose residue alpha 1-6-linked to the proximal GlcNAc, whereas those at Asn52 (and Asn78) of the alpha subunit are predominantly non-fucosylated.
1991473	8	80	theme	GalNAc	1351:1356	arg1	beta					1373:1376	the unique sequence NeuAc alpha 2-6 GalNAc beta 1-4GlcNAc beta	1315:1376	the unique sequence NeuAc alpha 2-6 GalNAc beta 1-4GlcNAc beta 1-2 Man alpha 1-3	1315:1394	The oligosaccharides at Asn78 (hLH alpha) are sialylated rather than sulphated and contain the unique sequence NeuAc alpha 2-6 GalNAc beta 1-4GlcNAc beta 1-2 Man alpha 1-3 as part of the majority of mono- and disialylated compounds.
1991473	3	81	theme	hLH	356:358	arg1	beta					360:363	intact hLH beta	349:363	intact hLH beta	349:363	The sugar chains were liberated by hydrazinolysis from intact hLH beta and from glycopeptides obtained after tryptic digestion of hLH alpha, subsequently reduced and fractionated as alditols by anion-exchange and ion-suppression amine-adsorption HPLC and identified mainly by one-dimensional (1D) and two-dimensional (2D) 1H-NMR spectroscopy.
1991473	8	82	theme	1-4GlcNAc	1363:1371	arg1	beta					1373:1376	the unique sequence NeuAc alpha 2-6 GalNAc beta 1-4GlcNAc beta	1315:1376	the unique sequence NeuAc alpha 2-6 GalNAc beta 1-4GlcNAc beta 1-2 Man alpha 1-3	1315:1394	The oligosaccharides at Asn78 (hLH alpha) are sialylated rather than sulphated and contain the unique sequence NeuAc alpha 2-6 GalNAc beta 1-4GlcNAc beta 1-2 Man alpha 1-3 as part of the majority of mono- and disialylated compounds.
1991473	1	83	theme	Human	105:109	arg1	hormone					135:141	luteinizing hormone	123:141	luteinizing hormone	123:141	Human lutropin or luteinizing hormone (hLH) is a heterodimeric glycoprotein, composed of two subunits.
1991473	1	83	theme	Human	105:109	arg1	glycoprotein					168:179	a heterodimeric glycoprotein	152:179	a heterodimeric glycoprotein	152:179	Human lutropin or luteinizing hormone (hLH) is a heterodimeric glycoprotein, composed of two subunits.
1991473	1	83	theme	Human	105:109	arg1	lutropin					111:118	Human lutropin	105:118	Human lutropin	105:118	Human lutropin or luteinizing hormone (hLH) is a heterodimeric glycoprotein, composed of two subunits.
1991473	0	84	theme	oligosaccharides	35:50	arg1	investigations					4:17	NMR investigations	0:17	NMR investigations of the N-linked oligosaccharides at individual glycosylation sites of human lutropin	0:102	NMR investigations of the N-linked oligosaccharides at individual glycosylation sites of human lutropin.
1991473	3	85	theme	hLH	424:426	arg1	alpha					428:432	hLH alpha	424:432	hLH alpha	424:432	The sugar chains were liberated by hydrazinolysis from intact hLH beta and from glycopeptides obtained after tryptic digestion of hLH alpha, subsequently reduced and fractionated as alditols by anion-exchange and ion-suppression amine-adsorption HPLC and identified mainly by one-dimensional (1D) and two-dimensional (2D) 1H-NMR spectroscopy.
1991473	0	86	theme	individual	55:64	arg1	sites					80:84	individual glycosylation sites	55:84	individual glycosylation sites of human lutropin	55:102	NMR investigations of the N-linked oligosaccharides at individual glycosylation sites of human lutropin.
1991473	0	86	theme	individual	55:64	arg1	lutropin					95:102	human lutropin	89:102	human lutropin	89:102	NMR investigations of the N-linked oligosaccharides at individual glycosylation sites of human lutropin.
1991473	6	87	theme	similar	845:851	arg1	pattern					853:859	a remarkably similar pattern	832:859	a remarkably similar pattern	832:859	The oligosaccharides attached to Asn52 (hLH alpha) and Asn30 (hLH beta) show a remarkably similar pattern, with mainly chain-terminating 4-sulphated 2-deoxy-2-N-acetylamino-D-galactose (GalNAc) and a sulphated/sialylated structure as the major single component.
1991473	8	88	theme	compounds	1446:1454	arg1	majority					1411:1418	the majority	1407:1418	the majority of mono- and disialylated compounds	1407:1454	The oligosaccharides at Asn78 (hLH alpha) are sialylated rather than sulphated and contain the unique sequence NeuAc alpha 2-6 GalNAc beta 1-4GlcNAc beta 1-2 Man alpha 1-3 as part of the majority of mono- and disialylated compounds.
1991473	8	89	theme	majority	1411:1418	arg1	part					1399:1402	part	1399:1402	part of the majority of mono- and disialylated compounds	1399:1454	The oligosaccharides at Asn78 (hLH alpha) are sialylated rather than sulphated and contain the unique sequence NeuAc alpha 2-6 GalNAc beta 1-4GlcNAc beta 1-2 Man alpha 1-3 as part of the majority of mono- and disialylated compounds.
1991473	3	90	theme	anion-exchange	488:501	arg1	HPLC					540:543	anion-exchange and ion-suppression amine-adsorption HPLC	488:543	HPLC	540:543	The sugar chains were liberated by hydrazinolysis from intact hLH beta and from glycopeptides obtained after tryptic digestion of hLH alpha, subsequently reduced and fractionated as alditols by anion-exchange and ion-suppression amine-adsorption HPLC and identified mainly by one-dimensional (1D) and two-dimensional (2D) 1H-NMR spectroscopy.
17569869	5	0	theme	antiseptic	722:731	arg1	development					738:748	antiseptic drug development	722:748	antiseptic drug development	722:748	These structures suggest that MD-2 plays a principal role in endotoxin recognition and provide a basis for antiseptic drug development.
17569869	4	1	theme	phosphorylated	536:549	arg1	located					576:582	located	576:582	located	576:582	The phosphorylated glucosamine moieties are located at the entrance to the cavity.
17569869	4	1	theme	phosphorylated	536:549	arg1	moieties					563:570	The phosphorylated glucosamine moieties	532:570	The phosphorylated glucosamine moieties	532:570	The phosphorylated glucosamine moieties are located at the entrance to the cavity.
17569869	0	2	theme	lipid	68:72	arg1	IVa					74:76	antiendotoxic lipid IVa	54:76	antiendotoxic lipid IVa	54:76	Crystal structures of human MD-2 and its complex with antiendotoxic lipid IVa.
17569869	3	3	theme	ligand	505:510	arg1	chains					491:496	four acyl chains	481:496	four acyl chains of the ligand	481:510	MD-2 shows a deep hydrophobic cavity sandwiched by two beta sheets, in which four acyl chains of the ligand are fully confined.
17569869	2	4	theme	A	318:318	arg1	core					320:323	the antiendotoxic tetra-acylated lipid A core	279:323	the antiendotoxic tetra-acylated lipid A core of LPS	279:330	Crystal structures of human MD-2 and its complex with the antiendotoxic tetra-acylated lipid A core of LPS have been determined at 2.0 and 2.2 angstrom resolutions, respectively.
17569869	2	5	theme	angstrom	368:375	arg1	resolutions					377:387	2.0 and 2.2 angstrom resolutions	356:387	2.0 and 2.2 angstrom resolutions	356:387	Crystal structures of human MD-2 and its complex with the antiendotoxic tetra-acylated lipid A core of LPS have been determined at 2.0 and 2.2 angstrom resolutions, respectively.
17569869	4	6	theme	glucosamine	551:561	arg1	located					576:582	located	576:582	located	576:582	The phosphorylated glucosamine moieties are located at the entrance to the cavity.
17569869	4	6	theme	glucosamine	551:561	arg1	moieties					563:570	The phosphorylated glucosamine moieties	532:570	The phosphorylated glucosamine moieties	532:570	The phosphorylated glucosamine moieties are located at the entrance to the cavity.
17569869	3	7	theme	deep	417:420	arg1	cavity					434:439	a deep hydrophobic cavity	415:439	a deep hydrophobic cavity sandwiched by two beta sheets, in which four acyl chains of the ligand are fully confined	415:529	MD-2 shows a deep hydrophobic cavity sandwiched by two beta sheets, in which four acyl chains of the ligand are fully confined.
17569869	1	8	with	lipopolysaccharide	89:106	arg1	activity					144:151	potent immunostimulatory activity	119:151	potent immunostimulatory activity	119:151	Endotoxic lipopolysaccharide (LPS) with potent immunostimulatory activity is recognized by the receptor complex of MD-2 and Toll-like receptor 4.
17569869	5	9	theme	drug	733:736	arg1	development					738:748	antiseptic drug development	722:748	antiseptic drug development	722:748	These structures suggest that MD-2 plays a principal role in endotoxin recognition and provide a basis for antiseptic drug development.
17569869	2	10	theme	lipid	312:316	arg1	A					318:318	the antiendotoxic tetra-acylated lipid A	279:318	the antiendotoxic tetra-acylated lipid A core of LPS	279:330	Crystal structures of human MD-2 and its complex with the antiendotoxic tetra-acylated lipid A core of LPS have been determined at 2.0 and 2.2 angstrom resolutions, respectively.
17569869	1	11	theme	receptor	174:181	arg1	complex					183:189	the receptor complex	170:189	the receptor complex of MD-2 and Toll-like receptor 4	170:222	Endotoxic lipopolysaccharide (LPS) with potent immunostimulatory activity is recognized by the receptor complex of MD-2 and Toll-like receptor 4.
17569869	0	12	theme	Crystal	0:6	arg1	structures					8:17	Crystal structures	0:17	Crystal structures of human MD-2	0:31	Crystal structures of human MD-2 and its complex with antiendotoxic lipid IVa.
17569869	1	13	theme	Endotoxic	79:87	arg1	LPS					109:111	LPS	109:111	LPS	109:111	Endotoxic lipopolysaccharide (LPS) with potent immunostimulatory activity is recognized by the receptor complex of MD-2 and Toll-like receptor 4.
17569869	1	13	theme	Endotoxic	79:87	arg1	lipopolysaccharide					89:106	Endotoxic lipopolysaccharide	79:106	Endotoxic lipopolysaccharide (LPS) with potent immunostimulatory activity	79:151	Endotoxic lipopolysaccharide (LPS) with potent immunostimulatory activity is recognized by the receptor complex of MD-2 and Toll-like receptor 4.
17569869	0	14	theme	human	22:26	arg1	MD-2					28:31	human MD-2	22:31	human MD-2	22:31	Crystal structures of human MD-2 and its complex with antiendotoxic lipid IVa.
17569869	5	15	theme	principal	658:666	arg1	role					668:671	a principal role	656:671	a principal role	656:671	These structures suggest that MD-2 plays a principal role in endotoxin recognition and provide a basis for antiseptic drug development.
17569869	2	16	theme	antiendotoxic	283:295	arg1	A					318:318	the antiendotoxic tetra-acylated lipid A	279:318	the antiendotoxic tetra-acylated lipid A core of LPS	279:330	Crystal structures of human MD-2 and its complex with the antiendotoxic tetra-acylated lipid A core of LPS have been determined at 2.0 and 2.2 angstrom resolutions, respectively.
17569869	3	17	theme	sandwiched	441:450	arg1	cavity					434:439	a deep hydrophobic cavity	415:439	a deep hydrophobic cavity sandwiched by two beta sheets, in which four acyl chains of the ligand are fully confined	415:529	MD-2 shows a deep hydrophobic cavity sandwiched by two beta sheets, in which four acyl chains of the ligand are fully confined.
17569869	2	18	theme	tetra-acylated	297:310	arg1	A					318:318	the antiendotoxic tetra-acylated lipid A	279:318	the antiendotoxic tetra-acylated lipid A core of LPS	279:330	Crystal structures of human MD-2 and its complex with the antiendotoxic tetra-acylated lipid A core of LPS have been determined at 2.0 and 2.2 angstrom resolutions, respectively.
17569869	1	19	theme	MD-2	194:197	arg1	complex					183:189	the receptor complex	170:189	the receptor complex of MD-2 and Toll-like receptor 4	170:222	Endotoxic lipopolysaccharide (LPS) with potent immunostimulatory activity is recognized by the receptor complex of MD-2 and Toll-like receptor 4.
17569869	2	20	theme	Crystal	225:231	arg1	structures					233:242	Crystal structures	225:242	Crystal structures of human MD-2	225:256	Crystal structures of human MD-2 and its complex with the antiendotoxic tetra-acylated lipid A core of LPS have been determined at 2.0 and 2.2 angstrom resolutions, respectively.
17569869	4	21	from	entrance	591:598	arg1	located					576:582	located	576:582	located	576:582	The phosphorylated glucosamine moieties are located at the entrance to the cavity.
17569869	4	21	from	entrance	591:598	arg1	moieties					563:570	The phosphorylated glucosamine moieties	532:570	The phosphorylated glucosamine moieties	532:570	The phosphorylated glucosamine moieties are located at the entrance to the cavity.
17569869	3	22	theme	hydrophobic	422:432	arg1	cavity					434:439	a deep hydrophobic cavity	415:439	a deep hydrophobic cavity sandwiched by two beta sheets, in which four acyl chains of the ligand are fully confined	415:529	MD-2 shows a deep hydrophobic cavity sandwiched by two beta sheets, in which four acyl chains of the ligand are fully confined.
17569869	0	23	theme	MD-2	28:31	arg1	structures					8:17	Crystal structures	0:17	Crystal structures of human MD-2	0:31	Crystal structures of human MD-2 and its complex with antiendotoxic lipid IVa.
17569869	0	23	theme	MD-2	28:31	arg1	complex					41:47	its complex	37:47	its complex with antiendotoxic lipid IVa	37:76	Crystal structures of human MD-2 and its complex with antiendotoxic lipid IVa.
17569869	5	24	theme	endotoxin	676:684	arg1	recognition					686:696	endotoxin recognition	676:696	endotoxin recognition	676:696	These structures suggest that MD-2 plays a principal role in endotoxin recognition and provide a basis for antiseptic drug development.
17569869	4	25	located	located	576:582	arg1	entrance					591:598	the entrance	587:598	the entrance to the cavity	587:612	The phosphorylated glucosamine moieties are located at the entrance to the cavity.
17569869	4	25	located	located	576:582	arg2	moieties					563:570	The phosphorylated glucosamine moieties	532:570	The phosphorylated glucosamine moieties	532:570	The phosphorylated glucosamine moieties are located at the entrance to the cavity.
17569869	4	25	located	located	576:582	arg2	located					576:582	located	576:582	located	576:582	The phosphorylated glucosamine moieties are located at the entrance to the cavity.
17569869	1	26	theme	Toll-like	203:211	arg1	receptor					213:220	Toll-like receptor 4	203:222	Toll-like receptor 4	203:222	Endotoxic lipopolysaccharide (LPS) with potent immunostimulatory activity is recognized by the receptor complex of MD-2 and Toll-like receptor 4.
17569869	2	27	with	structures	233:242	arg1	core					320:323	the antiendotoxic tetra-acylated lipid A core	279:323	the antiendotoxic tetra-acylated lipid A core of LPS	279:330	Crystal structures of human MD-2 and its complex with the antiendotoxic tetra-acylated lipid A core of LPS have been determined at 2.0 and 2.2 angstrom resolutions, respectively.
17569869	2	28	theme	LPS	328:330	arg1	core					320:323	the antiendotoxic tetra-acylated lipid A core	279:323	the antiendotoxic tetra-acylated lipid A core of LPS	279:330	Crystal structures of human MD-2 and its complex with the antiendotoxic tetra-acylated lipid A core of LPS have been determined at 2.0 and 2.2 angstrom resolutions, respectively.
17569869	0	29	with	structures	8:17	arg1	IVa					74:76	antiendotoxic lipid IVa	54:76	antiendotoxic lipid IVa	54:76	Crystal structures of human MD-2 and its complex with antiendotoxic lipid IVa.
17569869	2	30	theme	MD-2	253:256	arg1	complex					266:272	its complex	262:272	its complex with the antiendotoxic tetra-acylated lipid A core of LPS	262:330	Crystal structures of human MD-2 and its complex with the antiendotoxic tetra-acylated lipid A core of LPS have been determined at 2.0 and 2.2 angstrom resolutions, respectively.
17569869	2	30	theme	MD-2	253:256	arg1	structures					233:242	Crystal structures	225:242	Crystal structures of human MD-2	225:256	Crystal structures of human MD-2 and its complex with the antiendotoxic tetra-acylated lipid A core of LPS have been determined at 2.0 and 2.2 angstrom resolutions, respectively.
17569869	1	31	theme	receptor	213:220	arg1	complex					183:189	the receptor complex	170:189	the receptor complex of MD-2 and Toll-like receptor 4	170:222	Endotoxic lipopolysaccharide (LPS) with potent immunostimulatory activity is recognized by the receptor complex of MD-2 and Toll-like receptor 4.
17569869	2	32	theme	human	247:251	arg1	MD-2					253:256	human MD-2	247:256	human MD-2	247:256	Crystal structures of human MD-2 and its complex with the antiendotoxic tetra-acylated lipid A core of LPS have been determined at 2.0 and 2.2 angstrom resolutions, respectively.
17569869	0	33	with	complex	41:47	arg1	IVa					74:76	antiendotoxic lipid IVa	54:76	antiendotoxic lipid IVa	54:76	Crystal structures of human MD-2 and its complex with antiendotoxic lipid IVa.
17569869	1	34	theme	potent	119:124	arg1	activity					144:151	potent immunostimulatory activity	119:151	potent immunostimulatory activity	119:151	Endotoxic lipopolysaccharide (LPS) with potent immunostimulatory activity is recognized by the receptor complex of MD-2 and Toll-like receptor 4.
17569869	0	35	theme	antiendotoxic	54:66	arg1	IVa					74:76	antiendotoxic lipid IVa	54:76	antiendotoxic lipid IVa	54:76	Crystal structures of human MD-2 and its complex with antiendotoxic lipid IVa.
17569869	1	36	theme	immunostimulatory	126:142	arg1	activity					144:151	potent immunostimulatory activity	119:151	potent immunostimulatory activity	119:151	Endotoxic lipopolysaccharide (LPS) with potent immunostimulatory activity is recognized by the receptor complex of MD-2 and Toll-like receptor 4.
17569869	3	37	theme	beta	459:462	arg1	sheets					464:469	two beta sheets	455:469	two beta sheets	455:469	MD-2 shows a deep hydrophobic cavity sandwiched by two beta sheets, in which four acyl chains of the ligand are fully confined.
17569869	3	38	theme	acyl	486:489	arg1	chains					491:496	four acyl chains	481:496	four acyl chains of the ligand	481:510	MD-2 shows a deep hydrophobic cavity sandwiched by two beta sheets, in which four acyl chains of the ligand are fully confined.
17569869	2	39	with	complex	266:272	arg1	core					320:323	the antiendotoxic tetra-acylated lipid A core	279:323	the antiendotoxic tetra-acylated lipid A core of LPS	279:330	Crystal structures of human MD-2 and its complex with the antiendotoxic tetra-acylated lipid A core of LPS have been determined at 2.0 and 2.2 angstrom resolutions, respectively.
9721187	5	0	theme	p62-like	655:662	arg1	protein					664:670	a p62-like protein	653:670	a p62-like protein isolated from mouse neuroblastoma cells	653:710	Recently, a p62-like protein isolated from mouse neuroblastoma cells was reported to be modified by both GlcNAc and sialic acid.
9721187	7	1	theme	p62	989:991	arg1	sialation					993:1001	p62 sialation	989:1001	p62 sialation	989:1001	To assess the biological importance of p62 sialation, GlcNAc and sialic acid-specific lectins were used to examine the state of p62 glycosylation in cells commonly used to study nuclear transport: frog eggs and normal rat kidney and HeLa fibroblasts.
9721187	5	2	theme	mouse	686:690	arg1	cells					706:710	mouse neuroblastoma cells	686:710	mouse neuroblastoma cells	686:710	Recently, a p62-like protein isolated from mouse neuroblastoma cells was reported to be modified by both GlcNAc and sialic acid.
9721187	9	3	theme	significant	1393:1403	arg1	sialation					1405:1413	no significant sialation	1390:1413	no significant sialation	1390:1413	The glycosylation of p62 in these cells appears to involve only single O-linked GlcNAc moieties; no significant sialation was detected.
9721187	7	4	theme	biological	964:973	arg1	importance					975:984	the biological importance	960:984	the biological importance of p62 sialation, GlcNAc and sialic acid-specific lectins	960:1042	To assess the biological importance of p62 sialation, GlcNAc and sialic acid-specific lectins were used to examine the state of p62 glycosylation in cells commonly used to study nuclear transport: frog eggs and normal rat kidney and HeLa fibroblasts.
9721187	9	5	gly	glycosylation	1297:1309	arg1	p62					1314:1316	p62	1314:1316	p62	1314:1316	The glycosylation of p62 in these cells appears to involve only single O-linked GlcNAc moieties; no significant sialation was detected.
9721187	9	5	gly	glycosylation	1297:1309	arg1	cells					1327:1331	these cells	1321:1331	these cells	1321:1331	The glycosylation of p62 in these cells appears to involve only single O-linked GlcNAc moieties; no significant sialation was detected.
9721187	6	6	theme	nuclear	863:869	arg1	sialated					887:894	sialated	887:894	sialated	887:894	As there is little precedent for nucleoplasmic sialation, the finding that a characterized nuclear pore protein is sialated is significant because it may regulate pore function.
9721187	6	6	theme	nuclear	863:869	arg1	protein					876:882	a characterized nuclear pore protein	847:882	a characterized nuclear pore protein	847:882	As there is little precedent for nucleoplasmic sialation, the finding that a characterized nuclear pore protein is sialated is significant because it may regulate pore function.
9721187	7	7	theme	HeLa	1183:1186	arg1	fibroblasts					1188:1198	normal rat kidney and HeLa fibroblasts	1161:1198	normal rat kidney and HeLa fibroblasts	1161:1198	To assess the biological importance of p62 sialation, GlcNAc and sialic acid-specific lectins were used to examine the state of p62 glycosylation in cells commonly used to study nuclear transport: frog eggs and normal rat kidney and HeLa fibroblasts.
9721187	7	8	from	state	1069:1073	arg1	cells					1099:1103	cells	1099:1103	cells commonly used to study nuclear transport	1099:1144	To assess the biological importance of p62 sialation, GlcNAc and sialic acid-specific lectins were used to examine the state of p62 glycosylation in cells commonly used to study nuclear transport: frog eggs and normal rat kidney and HeLa fibroblasts.
9721187	6	9	theme	nucleoplasmic	805:817	arg1	sialation					819:827	nucleoplasmic sialation	805:827	nucleoplasmic sialation	805:827	As there is little precedent for nucleoplasmic sialation, the finding that a characterized nuclear pore protein is sialated is significant because it may regulate pore function.
9721187	1	10	theme	Many	51:54	arg1	proteins					78:85	Many nuclear and cytosolic proteins	51:85	Many nuclear and cytosolic proteins	51:85	Many nuclear and cytosolic proteins are modified by single residues of O-linked N-acetyl-D-glucosamine.
9721187	4	11	theme	protein-protein	594:608	arg1	interactions					610:621	protein-protein interactions	594:621	protein-protein interactions of the p62 complex	594:640	Although p62 sugar residues are not essential for nuclear transport, they appear to oppose protein phosphorylation occurring at sites predicted to destabilize protein-protein interactions of the p62 complex.
9721187	7	12	theme	kidney	1172:1177	arg1	fibroblasts					1188:1198	normal rat kidney and HeLa fibroblasts	1161:1198	normal rat kidney and HeLa fibroblasts	1161:1198	To assess the biological importance of p62 sialation, GlcNAc and sialic acid-specific lectins were used to examine the state of p62 glycosylation in cells commonly used to study nuclear transport: frog eggs and normal rat kidney and HeLa fibroblasts.
9721187	1	13	theme	nuclear	56:62	arg1	proteins					78:85	Many nuclear and cytosolic proteins	51:85	Many nuclear and cytosolic proteins	51:85	Many nuclear and cytosolic proteins are modified by single residues of O-linked N-acetyl-D-glucosamine.
9721187	8	14	theme	cell	1239:1242	arg1	lines					1244:1248	four mouse neuroblastoma cell lines	1214:1248	four mouse neuroblastoma cell lines derived from the same tumor	1214:1276	In addition, four mouse neuroblastoma cell lines derived from the same tumor were examined.
9721187	8	15	theme	mouse	1219:1223	arg1	lines					1244:1248	four mouse neuroblastoma cell lines	1214:1248	four mouse neuroblastoma cell lines derived from the same tumor	1214:1276	In addition, four mouse neuroblastoma cell lines derived from the same tumor were examined.
9721187	0	16	theme	nucleoporin	34:44	arg1	p62					46:48	the nucleoporin p62	30:48	the nucleoporin p62	30:48	An evaluation of sialation of the nucleoporin p62.
9721187	4	17	theme	nuclear	485:491	arg1	transport					493:501	nuclear transport	485:501	nuclear transport	485:501	Although p62 sugar residues are not essential for nuclear transport, they appear to oppose protein phosphorylation occurring at sites predicted to destabilize protein-protein interactions of the p62 complex.
9721187	8	18	attach	derived	1250:1256	arg2	lines					1244:1248	four mouse neuroblastoma cell lines	1214:1248	four mouse neuroblastoma cell lines derived from the same tumor	1214:1276	In addition, four mouse neuroblastoma cell lines derived from the same tumor were examined.
9721187	8	18	attach	derived	1250:1256	arg1	tumor					1272:1276	the same tumor	1263:1276	the same tumor	1263:1276	In addition, four mouse neuroblastoma cell lines derived from the same tumor were examined.
9721187	7	19	dep	used	1049:1052	arg1	fibroblasts					1188:1198	normal rat kidney and HeLa fibroblasts	1161:1198	normal rat kidney and HeLa fibroblasts	1161:1198	To assess the biological importance of p62 sialation, GlcNAc and sialic acid-specific lectins were used to examine the state of p62 glycosylation in cells commonly used to study nuclear transport: frog eggs and normal rat kidney and HeLa fibroblasts.
9721187	7	19	dep	used	1049:1052	arg1	eggs					1152:1155	frog eggs	1147:1155	frog eggs	1147:1155	To assess the biological importance of p62 sialation, GlcNAc and sialic acid-specific lectins were used to examine the state of p62 glycosylation in cells commonly used to study nuclear transport: frog eggs and normal rat kidney and HeLa fibroblasts.
9721187	7	20	theme	normal	1161:1166	arg1	fibroblasts					1188:1198	normal rat kidney and HeLa fibroblasts	1161:1198	normal rat kidney and HeLa fibroblasts	1161:1198	To assess the biological importance of p62 sialation, GlcNAc and sialic acid-specific lectins were used to examine the state of p62 glycosylation in cells commonly used to study nuclear transport: frog eggs and normal rat kidney and HeLa fibroblasts.
9721187	7	21	theme	p62	1078:1080	arg1	glycosylation					1082:1094	p62 glycosylation	1078:1094	p62 glycosylation	1078:1094	To assess the biological importance of p62 sialation, GlcNAc and sialic acid-specific lectins were used to examine the state of p62 glycosylation in cells commonly used to study nuclear transport: frog eggs and normal rat kidney and HeLa fibroblasts.
9721187	6	22	theme	little	784:789	arg1	precedent					791:799	little precedent	784:799	little precedent for nucleoplasmic sialation	784:827	As there is little precedent for nucleoplasmic sialation, the finding that a characterized nuclear pore protein is sialated is significant because it may regulate pore function.
9721187	1	23	theme	cytosolic	68:76	arg1	proteins					78:85	Many nuclear and cytosolic proteins	51:85	Many nuclear and cytosolic proteins	51:85	Many nuclear and cytosolic proteins are modified by single residues of O-linked N-acetyl-D-glucosamine.
9721187	5	24	theme	neuroblastoma	692:704	arg1	cells					706:710	mouse neuroblastoma cells	686:710	mouse neuroblastoma cells	686:710	Recently, a p62-like protein isolated from mouse neuroblastoma cells was reported to be modified by both GlcNAc and sialic acid.
9721187	3	25	theme	nuclear	416:422	arg1	transport					424:432	nuclear transport	416:432	nuclear transport	416:432	The best characterized pore glycoprotein, p62, mediates its function as one component of a protein complex essential for nuclear transport.
9721187	7	26	theme	rat	1168:1170	arg1	kidney					1172:1177	rat kidney	1168:1177	rat kidney	1168:1177	To assess the biological importance of p62 sialation, GlcNAc and sialic acid-specific lectins were used to examine the state of p62 glycosylation in cells commonly used to study nuclear transport: frog eggs and normal rat kidney and HeLa fibroblasts.
9721187	9	27	theme	p62	1314:1316	arg1	glycosylation					1297:1309	The glycosylation	1293:1309	The glycosylation of p62 in these cells	1293:1331	The glycosylation of p62 in these cells appears to involve only single O-linked GlcNAc moieties; no significant sialation was detected.
9721187	7	28	theme	glycosylation	1082:1094	arg1	state					1069:1073	the state	1065:1073	the state of p62 glycosylation in cells commonly used to study nuclear transport	1065:1144	To assess the biological importance of p62 sialation, GlcNAc and sialic acid-specific lectins were used to examine the state of p62 glycosylation in cells commonly used to study nuclear transport: frog eggs and normal rat kidney and HeLa fibroblasts.
9721187	6	29	theme	pore	871:874	arg1	sialated					887:894	sialated	887:894	sialated	887:894	As there is little precedent for nucleoplasmic sialation, the finding that a characterized nuclear pore protein is sialated is significant because it may regulate pore function.
9721187	6	29	theme	pore	871:874	arg1	protein					876:882	a characterized nuclear pore protein	847:882	a characterized nuclear pore protein	847:882	As there is little precedent for nucleoplasmic sialation, the finding that a characterized nuclear pore protein is sialated is significant because it may regulate pore function.
9721187	0	30	theme	sialation	17:25	arg1	evaluation					3:12	An evaluation	0:12	An evaluation of sialation of the nucleoporin p62	0:48	An evaluation of sialation of the nucleoporin p62.
9721187	5	31	mod	modified	731:738	arg1	protein					664:670	a p62-like protein	653:670	a p62-like protein isolated from mouse neuroblastoma cells	653:710	Recently, a p62-like protein isolated from mouse neuroblastoma cells was reported to be modified by both GlcNAc and sialic acid.
9721187	5	31	mod	modified	731:738	arg3	GlcNAc					748:753	GlcNAc	748:753	GlcNAc	748:753	Recently, a p62-like protein isolated from mouse neuroblastoma cells was reported to be modified by both GlcNAc and sialic acid.
9721187	5	31	mod	modified	731:738	arg3	acid					766:769	sialic acid	759:769	sialic acid	759:769	Recently, a p62-like protein isolated from mouse neuroblastoma cells was reported to be modified by both GlcNAc and sialic acid.
9721187	9	32	link	O-linked	1364:1371	arg1	moieties					1380:1387	only single O-linked GlcNAc moieties	1352:1387	only single O-linked GlcNAc moieties	1352:1387	The glycosylation of p62 in these cells appears to involve only single O-linked GlcNAc moieties; no significant sialation was detected.
9721187	4	33	theme	sugar	448:452	arg1	residues					454:461	p62 sugar residues	444:461	p62 sugar residues	444:461	Although p62 sugar residues are not essential for nuclear transport, they appear to oppose protein phosphorylation occurring at sites predicted to destabilize protein-protein interactions of the p62 complex.
9721187	2	34	located	found	183:187	arg2	proteins					174:181	many proteins	169:181	many proteins found in nuclear pore complexes required for transport of macromolecules between the nucleus and the cytoplasm	169:292	These include many proteins found in nuclear pore complexes required for transport of macromolecules between the nucleus and the cytoplasm.
9721187	2	34	located	found	183:187	arg1	complexes					205:213	nuclear pore complexes	192:213	nuclear pore complexes required for transport of macromolecules between the nucleus and the cytoplasm	192:292	These include many proteins found in nuclear pore complexes required for transport of macromolecules between the nucleus and the cytoplasm.
9721187	3	35	theme	essential	402:410	arg1	complex					394:400	a protein complex	384:400	a protein complex essential for nuclear transport	384:432	The best characterized pore glycoprotein, p62, mediates its function as one component of a protein complex essential for nuclear transport.
9721187	8	36	theme	same	1267:1270	arg1	tumor					1272:1276	the same tumor	1263:1276	the same tumor	1263:1276	In addition, four mouse neuroblastoma cell lines derived from the same tumor were examined.
9721187	1	37	link	O-linked	122:129	arg1	N-acetyl-D-glucosamine					131:152	O-linked N-acetyl-D-glucosamine	122:152	O-linked N-acetyl-D-glucosamine	122:152	Many nuclear and cytosolic proteins are modified by single residues of O-linked N-acetyl-D-glucosamine.
9721187	4	38	theme	p62	444:446	arg1	residues					454:461	p62 sugar residues	444:461	p62 sugar residues	444:461	Although p62 sugar residues are not essential for nuclear transport, they appear to oppose protein phosphorylation occurring at sites predicted to destabilize protein-protein interactions of the p62 complex.
9721187	8	39	theme	neuroblastoma	1225:1237	arg1	lines					1244:1248	four mouse neuroblastoma cell lines	1214:1248	four mouse neuroblastoma cell lines derived from the same tumor	1214:1276	In addition, four mouse neuroblastoma cell lines derived from the same tumor were examined.
9721187	7	40	theme	nuclear	1128:1134	arg1	transport					1136:1144	nuclear transport	1128:1144	nuclear transport	1128:1144	To assess the biological importance of p62 sialation, GlcNAc and sialic acid-specific lectins were used to examine the state of p62 glycosylation in cells commonly used to study nuclear transport: frog eggs and normal rat kidney and HeLa fibroblasts.
9721187	7	41	theme	frog	1147:1150	arg1	eggs					1152:1155	frog eggs	1147:1155	frog eggs	1147:1155	To assess the biological importance of p62 sialation, GlcNAc and sialic acid-specific lectins were used to examine the state of p62 glycosylation in cells commonly used to study nuclear transport: frog eggs and normal rat kidney and HeLa fibroblasts.
9721187	2	42	theme	many	169:172	arg1	proteins					174:181	many proteins	169:181	many proteins found in nuclear pore complexes required for transport of macromolecules between the nucleus and the cytoplasm	169:292	These include many proteins found in nuclear pore complexes required for transport of macromolecules between the nucleus and the cytoplasm.
9721187	9	43	theme	GlcNAc	1373:1378	arg1	moieties					1380:1387	only single O-linked GlcNAc moieties	1352:1387	only single O-linked GlcNAc moieties	1352:1387	The glycosylation of p62 in these cells appears to involve only single O-linked GlcNAc moieties; no significant sialation was detected.
9721187	7	44	theme	sialic	1015:1020	arg1	lectins					1036:1042	sialic acid-specific lectins	1015:1042	sialic acid-specific lectins	1015:1042	To assess the biological importance of p62 sialation, GlcNAc and sialic acid-specific lectins were used to examine the state of p62 glycosylation in cells commonly used to study nuclear transport: frog eggs and normal rat kidney and HeLa fibroblasts.
9721187	6	45	theme	pore	935:938	arg1	function					940:947	pore function	935:947	pore function	935:947	As there is little precedent for nucleoplasmic sialation, the finding that a characterized nuclear pore protein is sialated is significant because it may regulate pore function.
9721187	3	46	theme	protein	386:392	arg1	complex					394:400	a protein complex	384:400	a protein complex essential for nuclear transport	384:432	The best characterized pore glycoprotein, p62, mediates its function as one component of a protein complex essential for nuclear transport.
9721187	3	47	theme	characterized	304:316	arg1	p62					337:339	p62	337:339	p62	337:339	The best characterized pore glycoprotein, p62, mediates its function as one component of a protein complex essential for nuclear transport.
9721187	3	47	theme	characterized	304:316	arg1	glycoprotein					323:334	The best characterized pore glycoprotein	295:334	The best characterized pore glycoprotein	295:334	The best characterized pore glycoprotein, p62, mediates its function as one component of a protein complex essential for nuclear transport.
9721187	6	48	theme	characterized	849:861	arg1	sialated					887:894	sialated	887:894	sialated	887:894	As there is little precedent for nucleoplasmic sialation, the finding that a characterized nuclear pore protein is sialated is significant because it may regulate pore function.
9721187	6	48	theme	characterized	849:861	arg1	protein					876:882	a characterized nuclear pore protein	847:882	a characterized nuclear pore protein	847:882	As there is little precedent for nucleoplasmic sialation, the finding that a characterized nuclear pore protein is sialated is significant because it may regulate pore function.
9721187	7	49	theme	acid-specific	1022:1034	arg1	lectins					1036:1042	sialic acid-specific lectins	1015:1042	sialic acid-specific lectins	1015:1042	To assess the biological importance of p62 sialation, GlcNAc and sialic acid-specific lectins were used to examine the state of p62 glycosylation in cells commonly used to study nuclear transport: frog eggs and normal rat kidney and HeLa fibroblasts.
9721187	3	50	theme	complex	394:400	arg1	component					371:379	one component	367:379	one component of a protein complex essential for nuclear transport	367:432	The best characterized pore glycoprotein, p62, mediates its function as one component of a protein complex essential for nuclear transport.
9721187	3	51	theme	pore	318:321	arg1	p62					337:339	p62	337:339	p62	337:339	The best characterized pore glycoprotein, p62, mediates its function as one component of a protein complex essential for nuclear transport.
9721187	3	51	theme	pore	318:321	arg1	glycoprotein					323:334	The best characterized pore glycoprotein	295:334	The best characterized pore glycoprotein	295:334	The best characterized pore glycoprotein, p62, mediates its function as one component of a protein complex essential for nuclear transport.
9721187	7	52	theme	GlcNAc	1004:1009	arg1	importance					975:984	the biological importance	960:984	the biological importance of p62 sialation, GlcNAc and sialic acid-specific lectins	960:1042	To assess the biological importance of p62 sialation, GlcNAc and sialic acid-specific lectins were used to examine the state of p62 glycosylation in cells commonly used to study nuclear transport: frog eggs and normal rat kidney and HeLa fibroblasts.
9721187	1	53	theme	single	103:108	arg1	residues					110:117	single residues	103:117	single residues of O-linked N-acetyl-D-glucosamine	103:152	Many nuclear and cytosolic proteins are modified by single residues of O-linked N-acetyl-D-glucosamine.
9721187	1	53	theme	single	103:108	arg1	N-acetyl-D-glucosamine					131:152	O-linked N-acetyl-D-glucosamine	122:152	O-linked N-acetyl-D-glucosamine	122:152	Many nuclear and cytosolic proteins are modified by single residues of O-linked N-acetyl-D-glucosamine.
9721187	4	54	theme	protein	526:532	arg1	phosphorylation					534:548	protein phosphorylation	526:548	protein phosphorylation occurring at sites predicted to destabilize protein-protein interactions of the p62 complex	526:640	Although p62 sugar residues are not essential for nuclear transport, they appear to oppose protein phosphorylation occurring at sites predicted to destabilize protein-protein interactions of the p62 complex.
9721187	7	55	theme	lectins	1036:1042	arg1	importance					975:984	the biological importance	960:984	the biological importance of p62 sialation, GlcNAc and sialic acid-specific lectins	960:1042	To assess the biological importance of p62 sialation, GlcNAc and sialic acid-specific lectins were used to examine the state of p62 glycosylation in cells commonly used to study nuclear transport: frog eggs and normal rat kidney and HeLa fibroblasts.
9721187	2	56	theme	pore	200:203	arg1	complexes					205:213	nuclear pore complexes	192:213	nuclear pore complexes required for transport of macromolecules between the nucleus and the cytoplasm	192:292	These include many proteins found in nuclear pore complexes required for transport of macromolecules between the nucleus and the cytoplasm.
9721187	1	57	mod	modified	91:98	arg1	proteins					78:85	Many nuclear and cytosolic proteins	51:85	Many nuclear and cytosolic proteins	51:85	Many nuclear and cytosolic proteins are modified by single residues of O-linked N-acetyl-D-glucosamine.
9721187	1	57	mod	modified	91:98	arg3	residues					110:117	single residues	103:117	single residues of O-linked N-acetyl-D-glucosamine	103:152	Many nuclear and cytosolic proteins are modified by single residues of O-linked N-acetyl-D-glucosamine.
9721187	1	57	mod	modified	91:98	arg3	N-acetyl-D-glucosamine					131:152	O-linked N-acetyl-D-glucosamine	122:152	O-linked N-acetyl-D-glucosamine	122:152	Many nuclear and cytosolic proteins are modified by single residues of O-linked N-acetyl-D-glucosamine.
9721187	9	58	theme	single	1357:1362	arg1	moieties					1380:1387	only single O-linked GlcNAc moieties	1352:1387	only single O-linked GlcNAc moieties	1352:1387	The glycosylation of p62 in these cells appears to involve only single O-linked GlcNAc moieties; no significant sialation was detected.
9721187	3	59	gly	glycoprotein	323:334	arg1	p62					337:339	p62	337:339	p62	337:339	The best characterized pore glycoprotein, p62, mediates its function as one component of a protein complex essential for nuclear transport.
9721187	3	59	gly	glycoprotein	323:334	arg1	glycoprotein					323:334	The best characterized pore glycoprotein	295:334	The best characterized pore glycoprotein	295:334	The best characterized pore glycoprotein, p62, mediates its function as one component of a protein complex essential for nuclear transport.
9721187	2	60	theme	nuclear	192:198	arg1	complexes					205:213	nuclear pore complexes	192:213	nuclear pore complexes required for transport of macromolecules between the nucleus and the cytoplasm	192:292	These include many proteins found in nuclear pore complexes required for transport of macromolecules between the nucleus and the cytoplasm.
9721187	7	61	theme	sialation	993:1001	arg1	importance					975:984	the biological importance	960:984	the biological importance of p62 sialation, GlcNAc and sialic acid-specific lectins	960:1042	To assess the biological importance of p62 sialation, GlcNAc and sialic acid-specific lectins were used to examine the state of p62 glycosylation in cells commonly used to study nuclear transport: frog eggs and normal rat kidney and HeLa fibroblasts.
9721187	9	62	theme	O-linked	1364:1371	arg1	moieties					1380:1387	only single O-linked GlcNAc moieties	1352:1387	only single O-linked GlcNAc moieties	1352:1387	The glycosylation of p62 in these cells appears to involve only single O-linked GlcNAc moieties; no significant sialation was detected.
9721187	5	63	theme	sialic	759:764	arg1	acid					766:769	sialic acid	759:769	sialic acid	759:769	Recently, a p62-like protein isolated from mouse neuroblastoma cells was reported to be modified by both GlcNAc and sialic acid.
9721187	1	64	theme	O-linked	122:129	arg1	N-acetyl-D-glucosamine					131:152	O-linked N-acetyl-D-glucosamine	122:152	O-linked N-acetyl-D-glucosamine	122:152	Many nuclear and cytosolic proteins are modified by single residues of O-linked N-acetyl-D-glucosamine.
9721187	5	65	attach	isolated	672:679	arg1	cells					706:710	mouse neuroblastoma cells	686:710	mouse neuroblastoma cells	686:710	Recently, a p62-like protein isolated from mouse neuroblastoma cells was reported to be modified by both GlcNAc and sialic acid.
9721187	5	65	attach	isolated	672:679	arg2	protein					664:670	a p62-like protein	653:670	a p62-like protein isolated from mouse neuroblastoma cells	653:710	Recently, a p62-like protein isolated from mouse neuroblastoma cells was reported to be modified by both GlcNAc and sialic acid.
9721187	4	66	theme	complex	634:640	arg1	interactions					610:621	protein-protein interactions	594:621	protein-protein interactions of the p62 complex	594:640	Although p62 sugar residues are not essential for nuclear transport, they appear to oppose protein phosphorylation occurring at sites predicted to destabilize protein-protein interactions of the p62 complex.
9721187	0	67	theme	p62	46:48	arg1	sialation					17:25	sialation	17:25	sialation of the nucleoporin p62	17:48	An evaluation of sialation of the nucleoporin p62.
9721187	2	68	theme	macromolecules	241:254	arg1	transport					228:236	transport	228:236	transport of macromolecules between the nucleus and the cytoplasm	228:292	These include many proteins found in nuclear pore complexes required for transport of macromolecules between the nucleus and the cytoplasm.
9721187	1	69	theme	N-acetyl-D-glucosamine	131:152	arg1	residues					110:117	single residues	103:117	single residues of O-linked N-acetyl-D-glucosamine	103:152	Many nuclear and cytosolic proteins are modified by single residues of O-linked N-acetyl-D-glucosamine.
9721187	1	69	theme	N-acetyl-D-glucosamine	131:152	arg1	N-acetyl-D-glucosamine					131:152	O-linked N-acetyl-D-glucosamine	122:152	O-linked N-acetyl-D-glucosamine	122:152	Many nuclear and cytosolic proteins are modified by single residues of O-linked N-acetyl-D-glucosamine.
9721187	9	70	from	glycosylation	1297:1309	arg1	cells					1327:1331	these cells	1321:1331	these cells	1321:1331	The glycosylation of p62 in these cells appears to involve only single O-linked GlcNAc moieties; no significant sialation was detected.
9721187	4	71	theme	p62	630:632	arg1	complex					634:640	the p62 complex	626:640	the p62 complex	626:640	Although p62 sugar residues are not essential for nuclear transport, they appear to oppose protein phosphorylation occurring at sites predicted to destabilize protein-protein interactions of the p62 complex.
8344946	5	0	theme	glycopeptides	975:987	arg1	purification					955:966	purification	955:966	purification of the glycopeptides	955:987	The predominant sites of O-GlcNAc attachment on NF-L and NF-M are identified using proteolysis, purification of the glycopeptides, and subsequent analysis by automated gas-phase sequencing, manual Edman degradation, and laser desorption mass spectrometry.
8344946	5	0	theme	glycopeptides	975:987	arg1	proteolysis					942:952	proteolysis	942:952	proteolysis	942:952	The predominant sites of O-GlcNAc attachment on NF-L and NF-M are identified using proteolysis, purification of the glycopeptides, and subsequent analysis by automated gas-phase sequencing, manual Edman degradation, and laser desorption mass spectrometry.
8344946	5	0	theme	glycopeptides	975:987	arg1	analysis					1005:1012	subsequent analysis	994:1012	subsequent analysis by automated gas-phase sequencing, manual Edman degradation, and laser desorption mass spectrometry	994:1112	The predominant sites of O-GlcNAc attachment on NF-L and NF-M are identified using proteolysis, purification of the glycopeptides, and subsequent analysis by automated gas-phase sequencing, manual Edman degradation, and laser desorption mass spectrometry.
8344946	6	1	theme	NH2-terminal	1196:1207	arg1	domain					1214:1219	the NH2-terminal head domain	1192:1219	the NH2-terminal head domain	1192:1219	For NF-L, both major sites of glycosylation (Thr21 and Ser27) are located at the NH2-terminal head domain.
8344946	4	2	theme	neurofilament	703:715	arg1	proteins					717:724	purified neurofilament proteins	694:724	purified neurofilament proteins	694:724	In purified neurofilament proteins, the O-GlcNAc modifications occur at a stoichiometry of approximately 0.1 and 0.15 mol of GlcNAc/mol of NF-L and NF-M, respectively.
8344946	3	3	theme	glycosylation	553:565	arg1	type					523:526	an abundant type	511:526	an abundant type of intracellular protein glycosylation in which single N-acetylglucosamine monosaccharides are O-glycosidically (O-GlcNAc) linked to serine or threonine residues	511:688	Here, we demonstrate by several criteria that neurofilament polypeptides are also modified by an abundant type of intracellular protein glycosylation in which single N-acetylglucosamine monosaccharides are O-glycosidically (O-GlcNAc) linked to serine or threonine residues.
8344946	1	4	theme	important	209:217	arg1	role					219:222	an important role	206:222	an important role	206:222	Localization of multiple O-linked N-acetylglucosamine moieties on neurofilament polypeptides L and M. Neurofilaments are neuronal intermediate filaments that play an important role in the growth and maintenance of large myelinated axons.
8344946	9	5	theme	detailed	1662:1669	arg1	analysis					1681:1688	more detailed mutagenic analysis	1657:1688	more detailed mutagenic analysis of O-GlcNAc functions on neurofilaments	1657:1728	Specific identification of these O-GlcNAc attachment sites has set the stage for more detailed mutagenic analysis of O-GlcNAc functions on neurofilaments.
8344946	3	6	theme	N-acetylglucosamine	583:601	arg1	monosaccharides					603:617	single N-acetylglucosamine monosaccharides	576:617	single N-acetylglucosamine monosaccharides	576:617	Here, we demonstrate by several criteria that neurofilament polypeptides are also modified by an abundant type of intracellular protein glycosylation in which single N-acetylglucosamine monosaccharides are O-glycosidically (O-GlcNAc) linked to serine or threonine residues.
8344946	9	7	theme	O-GlcNAc	1693:1700	arg1	functions					1702:1710	O-GlcNAc functions	1693:1710	O-GlcNAc functions on neurofilaments	1693:1728	Specific identification of these O-GlcNAc attachment sites has set the stage for more detailed mutagenic analysis of O-GlcNAc functions on neurofilaments.
8344946	5	8	theme	attachment	893:902	arg1	sites					875:879	The predominant sites	859:879	The predominant sites of O-GlcNAc attachment on NF-L and NF-M	859:919	The predominant sites of O-GlcNAc attachment on NF-L and NF-M are identified using proteolysis, purification of the glycopeptides, and subsequent analysis by automated gas-phase sequencing, manual Edman degradation, and laser desorption mass spectrometry.
8344946	5	8	theme	attachment	893:902	arg1	attachment					893:902	O-GlcNAc attachment	884:902	O-GlcNAc attachment	884:902	The predominant sites of O-GlcNAc attachment on NF-L and NF-M are identified using proteolysis, purification of the glycopeptides, and subsequent analysis by automated gas-phase sequencing, manual Edman degradation, and laser desorption mass spectrometry.
8344946	8	9	theme	detrimental	1436:1446	arg1	effect					1448:1453	a dominant detrimental effect	1425:1453	a dominant detrimental effect	1425:1453	Deletions encompassing these sites have been shown previously to have a dominant detrimental effect upon neurofilament assembly, raising questions about the specific function(s) of the saccharide moieties at these sites.
8344946	5	10	theme	desorption	1085:1094	arg1	spectrometry					1101:1112	laser desorption mass spectrometry	1079:1112	laser desorption mass spectrometry	1079:1112	The predominant sites of O-GlcNAc attachment on NF-L and NF-M are identified using proteolysis, purification of the glycopeptides, and subsequent analysis by automated gas-phase sequencing, manual Edman degradation, and laser desorption mass spectrometry.
8344946	5	11	from	sites	875:879	arg1	NF-L					907:910	NF-L	907:910	NF-L	907:910	The predominant sites of O-GlcNAc attachment on NF-L and NF-M are identified using proteolysis, purification of the glycopeptides, and subsequent analysis by automated gas-phase sequencing, manual Edman degradation, and laser desorption mass spectrometry.
8344946	5	11	from	sites	875:879	arg1	NF-M					916:919	NF-M	916:919	NF-M	916:919	The predominant sites of O-GlcNAc attachment on NF-L and NF-M are identified using proteolysis, purification of the glycopeptides, and subsequent analysis by automated gas-phase sequencing, manual Edman degradation, and laser desorption mass spectrometry.
8344946	1	12	theme	neuronal	164:171	arg1	filaments					186:194	neuronal intermediate filaments	164:194	neuronal intermediate filaments that play an important role in the growth and maintenance of large myelinated axons	164:278	Localization of multiple O-linked N-acetylglucosamine moieties on neurofilament polypeptides L and M. Neurofilaments are neuronal intermediate filaments that play an important role in the growth and maintenance of large myelinated axons.
8344946	1	12	theme	neuronal	164:171	arg1	Localization					43:54	Localization	43:54	Localization of multiple O-linked N-acetylglucosamine moieties on neurofilament polypeptides L and M. Neurofilaments	43:158	Localization of multiple O-linked N-acetylglucosamine moieties on neurofilament polypeptides L and M. Neurofilaments are neuronal intermediate filaments that play an important role in the growth and maintenance of large myelinated axons.
8344946	4	13	theme	O-GlcNAc	731:738	arg1	modifications					740:752	the O-GlcNAc modifications	727:752	the O-GlcNAc modifications	727:752	In purified neurofilament proteins, the O-GlcNAc modifications occur at a stoichiometry of approximately 0.1 and 0.15 mol of GlcNAc/mol of NF-L and NF-M, respectively.
8344946	5	14	theme	predominant	863:873	arg1	sites					875:879	The predominant sites	859:879	The predominant sites of O-GlcNAc attachment on NF-L and NF-M	859:919	The predominant sites of O-GlcNAc attachment on NF-L and NF-M are identified using proteolysis, purification of the glycopeptides, and subsequent analysis by automated gas-phase sequencing, manual Edman degradation, and laser desorption mass spectrometry.
8344946	5	14	theme	predominant	863:873	arg1	attachment					893:902	O-GlcNAc attachment	884:902	O-GlcNAc attachment	884:902	The predominant sites of O-GlcNAc attachment on NF-L and NF-M are identified using proteolysis, purification of the glycopeptides, and subsequent analysis by automated gas-phase sequencing, manual Edman degradation, and laser desorption mass spectrometry.
8344946	9	15	from	neurofilaments	1715:1728	arg1	analysis					1681:1688	more detailed mutagenic analysis	1657:1688	more detailed mutagenic analysis of O-GlcNAc functions on neurofilaments	1657:1728	Specific identification of these O-GlcNAc attachment sites has set the stage for more detailed mutagenic analysis of O-GlcNAc functions on neurofilaments.
8344946	7	16	theme	major	1236:1240	arg1	Thr48					1248:1252	Thr48	1248:1252	Thr48	1248:1252	For NF-M, one major site (Thr48) lies within the NH2-terminal head domain, whereas the other (Thr431) is located at the tail domain.
8344946	7	16	theme	major	1236:1240	arg1	site					1242:1245	one major site	1232:1245	one major site (Thr48)	1232:1253	For NF-M, one major site (Thr48) lies within the NH2-terminal head domain, whereas the other (Thr431) is located at the tail domain.
8344946	9	17	from	functions	1702:1710	arg1	neurofilaments					1715:1728	neurofilaments	1715:1728	neurofilaments	1715:1728	Specific identification of these O-GlcNAc attachment sites has set the stage for more detailed mutagenic analysis of O-GlcNAc functions on neurofilaments.
8344946	1	18	theme	N-acetylglucosamine	77:95	arg1	moieties					97:104	multiple O-linked N-acetylglucosamine moieties	59:104	multiple O-linked N-acetylglucosamine moieties on neurofilament polypeptides L and M. Neurofilaments	59:158	Localization of multiple O-linked N-acetylglucosamine moieties on neurofilament polypeptides L and M. Neurofilaments are neuronal intermediate filaments that play an important role in the growth and maintenance of large myelinated axons.
8344946	8	19	theme	specific	1512:1519	arg1	s					1530:1530	the specific function(s)	1508:1531	the specific function(s) of the saccharide moieties	1508:1558	Deletions encompassing these sites have been shown previously to have a dominant detrimental effect upon neurofilament assembly, raising questions about the specific function(s) of the saccharide moieties at these sites.
8344946	3	20	theme	several	441:447	arg1	criteria					449:456	several criteria	441:456	several criteria	441:456	Here, we demonstrate by several criteria that neurofilament polypeptides are also modified by an abundant type of intracellular protein glycosylation in which single N-acetylglucosamine monosaccharides are O-glycosidically (O-GlcNAc) linked to serine or threonine residues.
8344946	5	21	theme	gas-phase	1027:1035	arg1	sequencing					1037:1046	automated gas-phase sequencing	1017:1046	automated gas-phase sequencing	1017:1046	The predominant sites of O-GlcNAc attachment on NF-L and NF-M are identified using proteolysis, purification of the glycopeptides, and subsequent analysis by automated gas-phase sequencing, manual Edman degradation, and laser desorption mass spectrometry.
8344946	7	22	from	domain	1347:1352	arg1	located					1327:1333	located	1327:1333	located	1327:1333	For NF-M, one major site (Thr48) lies within the NH2-terminal head domain, whereas the other (Thr431) is located at the tail domain.
8344946	7	22	from	domain	1347:1352	arg1	other					1309:1313	other	1309:1313	other	1309:1313	For NF-M, one major site (Thr48) lies within the NH2-terminal head domain, whereas the other (Thr431) is located at the tail domain.
8344946	1	23	theme	multiple	59:66	arg1	moieties					97:104	multiple O-linked N-acetylglucosamine moieties	59:104	multiple O-linked N-acetylglucosamine moieties on neurofilament polypeptides L and M. Neurofilaments	59:158	Localization of multiple O-linked N-acetylglucosamine moieties on neurofilament polypeptides L and M. Neurofilaments are neuronal intermediate filaments that play an important role in the growth and maintenance of large myelinated axons.
8344946	0	24	theme	mammalian	17:25	arg1	neurofilaments					27:40	mammalian neurofilaments	17:40	mammalian neurofilaments	17:40	Glycosylation of mammalian neurofilaments.
8344946	5	25	theme	subsequent	994:1003	arg1	analysis					1005:1012	subsequent analysis	994:1012	subsequent analysis by automated gas-phase sequencing, manual Edman degradation, and laser desorption mass spectrometry	994:1112	The predominant sites of O-GlcNAc attachment on NF-L and NF-M are identified using proteolysis, purification of the glycopeptides, and subsequent analysis by automated gas-phase sequencing, manual Edman degradation, and laser desorption mass spectrometry.
8344946	9	26	theme	Specific	1576:1583	arg1	identification					1585:1598	Specific identification	1576:1598	Specific identification of these O-GlcNAc attachment sites	1576:1633	Specific identification of these O-GlcNAc attachment sites has set the stage for more detailed mutagenic analysis of O-GlcNAc functions on neurofilaments.
8344946	8	27	theme	moieties	1551:1558	arg1	s					1530:1530	the specific function(s)	1508:1531	the specific function(s) of the saccharide moieties	1508:1558	Deletions encompassing these sites have been shown previously to have a dominant detrimental effect upon neurofilament assembly, raising questions about the specific function(s) of the saccharide moieties at these sites.
8344946	6	28	dep	glycosylation	1145:1157	arg1	Thr21					1160:1164	Thr21	1160:1164	Thr21	1160:1164	For NF-L, both major sites of glycosylation (Thr21 and Ser27) are located at the NH2-terminal head domain.
8344946	6	28	dep	glycosylation	1145:1157	arg1	Ser27					1170:1174	Ser27	1170:1174	Ser27	1170:1174	For NF-L, both major sites of glycosylation (Thr21 and Ser27) are located at the NH2-terminal head domain.
8344946	5	29	theme	laser	1079:1083	arg1	spectrometry					1101:1112	laser desorption mass spectrometry	1079:1112	laser desorption mass spectrometry	1079:1112	The predominant sites of O-GlcNAc attachment on NF-L and NF-M are identified using proteolysis, purification of the glycopeptides, and subsequent analysis by automated gas-phase sequencing, manual Edman degradation, and laser desorption mass spectrometry.
8344946	9	30	theme	O-GlcNAc	1609:1616	arg1	sites					1629:1633	these O-GlcNAc attachment sites	1603:1633	these O-GlcNAc attachment sites	1603:1633	Specific identification of these O-GlcNAc attachment sites has set the stage for more detailed mutagenic analysis of O-GlcNAc functions on neurofilaments.
8344946	7	31	theme	NH2-terminal	1271:1282	arg1	domain					1289:1294	the NH2-terminal head domain	1267:1294	the NH2-terminal head domain	1267:1294	For NF-M, one major site (Thr48) lies within the NH2-terminal head domain, whereas the other (Thr431) is located at the tail domain.
8344946	1	32	from	polypeptides	123:134	arg1	Localization					43:54	Localization	43:54	Localization of multiple O-linked N-acetylglucosamine moieties on neurofilament polypeptides L and M. Neurofilaments	43:158	Localization of multiple O-linked N-acetylglucosamine moieties on neurofilament polypeptides L and M. Neurofilaments are neuronal intermediate filaments that play an important role in the growth and maintenance of large myelinated axons.
8344946	1	32	from	polypeptides	123:134	arg1	filaments					186:194	neuronal intermediate filaments	164:194	neuronal intermediate filaments that play an important role in the growth and maintenance of large myelinated axons	164:278	Localization of multiple O-linked N-acetylglucosamine moieties on neurofilament polypeptides L and M. Neurofilaments are neuronal intermediate filaments that play an important role in the growth and maintenance of large myelinated axons.
8344946	1	33	theme	myelinated	263:272	arg1	axons					274:278	large myelinated axons	257:278	large myelinated axons	257:278	Localization of multiple O-linked N-acetylglucosamine moieties on neurofilament polypeptides L and M. Neurofilaments are neuronal intermediate filaments that play an important role in the growth and maintenance of large myelinated axons.
8344946	5	34	theme	Edman	1056:1060	arg1	degradation					1062:1072	manual Edman degradation	1049:1072	manual Edman degradation	1049:1072	The predominant sites of O-GlcNAc attachment on NF-L and NF-M are identified using proteolysis, purification of the glycopeptides, and subsequent analysis by automated gas-phase sequencing, manual Edman degradation, and laser desorption mass spectrometry.
8344946	3	35	theme	abundant	514:521	arg1	type					523:526	an abundant type	511:526	an abundant type of intracellular protein glycosylation in which single N-acetylglucosamine monosaccharides are O-glycosidically (O-GlcNAc) linked to serine or threonine residues	511:688	Here, we demonstrate by several criteria that neurofilament polypeptides are also modified by an abundant type of intracellular protein glycosylation in which single N-acetylglucosamine monosaccharides are O-glycosidically (O-GlcNAc) linked to serine or threonine residues.
8344946	1	36	theme	axons	274:278	arg1	growth					231:236	growth	231:236	growth	231:236	Localization of multiple O-linked N-acetylglucosamine moieties on neurofilament polypeptides L and M. Neurofilaments are neuronal intermediate filaments that play an important role in the growth and maintenance of large myelinated axons.
8344946	1	36	theme	axons	274:278	arg1	maintenance					242:252	maintenance	242:252	maintenance	242:252	Localization of multiple O-linked N-acetylglucosamine moieties on neurofilament polypeptides L and M. Neurofilaments are neuronal intermediate filaments that play an important role in the growth and maintenance of large myelinated axons.
8344946	6	37	theme	major	1130:1134	arg1	glycosylation					1145:1157	glycosylation	1145:1157	glycosylation (Thr21 and Ser27)	1145:1175	For NF-L, both major sites of glycosylation (Thr21 and Ser27) are located at the NH2-terminal head domain.
8344946	6	37	theme	major	1130:1134	arg1	sites					1136:1140	both major sites	1125:1140	both major sites of glycosylation (Thr21 and Ser27)	1125:1175	For NF-L, both major sites of glycosylation (Thr21 and Ser27) are located at the NH2-terminal head domain.
8344946	2	38	theme	polypeptide	328:338	arg1	subunits					340:347	three polypeptide subunits	322:347	three polypeptide subunits	322:347	Mammalian neurofilaments are composed of three polypeptide subunits, designed as NF-L, NF-M, and NF-H, all of which are phosphorylated.
8344946	6	39	theme	head	1209:1212	arg1	domain					1214:1219	the NH2-terminal head domain	1192:1219	the NH2-terminal head domain	1192:1219	For NF-L, both major sites of glycosylation (Thr21 and Ser27) are located at the NH2-terminal head domain.
8344946	1	40	link	O-linked	68:75	arg1	moieties					97:104	multiple O-linked N-acetylglucosamine moieties	59:104	multiple O-linked N-acetylglucosamine moieties on neurofilament polypeptides L and M. Neurofilaments	59:158	Localization of multiple O-linked N-acetylglucosamine moieties on neurofilament polypeptides L and M. Neurofilaments are neuronal intermediate filaments that play an important role in the growth and maintenance of large myelinated axons.
8344946	3	41	theme	protein	545:551	arg1	glycosylation					553:565	intracellular protein glycosylation	531:565	intracellular protein glycosylation in which single N-acetylglucosamine monosaccharides are O-glycosidically (O-GlcNAc) linked to serine or threonine residues	531:688	Here, we demonstrate by several criteria that neurofilament polypeptides are also modified by an abundant type of intracellular protein glycosylation in which single N-acetylglucosamine monosaccharides are O-glycosidically (O-GlcNAc) linked to serine or threonine residues.
8344946	3	42	dep	O-glycosidically	623:638	arg1	O-GlcNAc					641:648	O-GlcNAc	641:648	O-GlcNAc	641:648	Here, we demonstrate by several criteria that neurofilament polypeptides are also modified by an abundant type of intracellular protein glycosylation in which single N-acetylglucosamine monosaccharides are O-glycosidically (O-GlcNAc) linked to serine or threonine residues.
8344946	4	43	theme	purified	694:701	arg1	proteins					717:724	purified neurofilament proteins	694:724	purified neurofilament proteins	694:724	In purified neurofilament proteins, the O-GlcNAc modifications occur at a stoichiometry of approximately 0.1 and 0.15 mol of GlcNAc/mol of NF-L and NF-M, respectively.
8344946	1	44	from	Localization	43:54	arg1	polypeptides					123:134	neurofilament polypeptides L and M. Neurofilaments	109:158	neurofilament polypeptides L and M. Neurofilaments	109:158	Localization of multiple O-linked N-acetylglucosamine moieties on neurofilament polypeptides L and M. Neurofilaments are neuronal intermediate filaments that play an important role in the growth and maintenance of large myelinated axons.
8344946	9	45	theme	mutagenic	1671:1679	arg1	analysis					1681:1688	more detailed mutagenic analysis	1657:1688	more detailed mutagenic analysis of O-GlcNAc functions on neurofilaments	1657:1728	Specific identification of these O-GlcNAc attachment sites has set the stage for more detailed mutagenic analysis of O-GlcNAc functions on neurofilaments.
8344946	3	46	theme	single	576:581	arg1	monosaccharides					603:617	single N-acetylglucosamine monosaccharides	576:617	single N-acetylglucosamine monosaccharides	576:617	Here, we demonstrate by several criteria that neurofilament polypeptides are also modified by an abundant type of intracellular protein glycosylation in which single N-acetylglucosamine monosaccharides are O-glycosidically (O-GlcNAc) linked to serine or threonine residues.
8344946	3	47	mod	modified	499:506	arg1	polypeptides					477:488	neurofilament polypeptides	463:488	neurofilament polypeptides	463:488	Here, we demonstrate by several criteria that neurofilament polypeptides are also modified by an abundant type of intracellular protein glycosylation in which single N-acetylglucosamine monosaccharides are O-glycosidically (O-GlcNAc) linked to serine or threonine residues.
8344946	3	47	mod	modified	499:506	arg3	type					523:526	an abundant type	511:526	an abundant type of intracellular protein glycosylation in which single N-acetylglucosamine monosaccharides are O-glycosidically (O-GlcNAc) linked to serine or threonine residues	511:688	Here, we demonstrate by several criteria that neurofilament polypeptides are also modified by an abundant type of intracellular protein glycosylation in which single N-acetylglucosamine monosaccharides are O-glycosidically (O-GlcNAc) linked to serine or threonine residues.
8344946	8	48	theme	dominant	1427:1434	arg1	effect					1448:1453	a dominant detrimental effect	1425:1453	a dominant detrimental effect	1425:1453	Deletions encompassing these sites have been shown previously to have a dominant detrimental effect upon neurofilament assembly, raising questions about the specific function(s) of the saccharide moieties at these sites.
8344946	5	49	theme	O-GlcNAc	884:891	arg1	attachment					893:902	O-GlcNAc attachment	884:902	O-GlcNAc attachment	884:902	The predominant sites of O-GlcNAc attachment on NF-L and NF-M are identified using proteolysis, purification of the glycopeptides, and subsequent analysis by automated gas-phase sequencing, manual Edman degradation, and laser desorption mass spectrometry.
8344946	9	50	theme	functions	1702:1710	arg1	analysis					1681:1688	more detailed mutagenic analysis	1657:1688	more detailed mutagenic analysis of O-GlcNAc functions on neurofilaments	1657:1728	Specific identification of these O-GlcNAc attachment sites has set the stage for more detailed mutagenic analysis of O-GlcNAc functions on neurofilaments.
8344946	1	51	theme	M.	142:143	arg1	Neurofilaments					145:158	M. Neurofilaments	142:158	M. Neurofilaments	142:158	Localization of multiple O-linked N-acetylglucosamine moieties on neurofilament polypeptides L and M. Neurofilaments are neuronal intermediate filaments that play an important role in the growth and maintenance of large myelinated axons.
8344946	8	52	theme	neurofilament	1460:1472	arg1	assembly					1474:1481	neurofilament assembly	1460:1481	neurofilament assembly	1460:1481	Deletions encompassing these sites have been shown previously to have a dominant detrimental effect upon neurofilament assembly, raising questions about the specific function(s) of the saccharide moieties at these sites.
8344946	5	53	theme	mass	1096:1099	arg1	spectrometry					1101:1112	laser desorption mass spectrometry	1079:1112	laser desorption mass spectrometry	1079:1112	The predominant sites of O-GlcNAc attachment on NF-L and NF-M are identified using proteolysis, purification of the glycopeptides, and subsequent analysis by automated gas-phase sequencing, manual Edman degradation, and laser desorption mass spectrometry.
8344946	7	54	theme	tail	1342:1345	arg1	domain					1347:1352	the tail domain	1338:1352	the tail domain	1338:1352	For NF-M, one major site (Thr48) lies within the NH2-terminal head domain, whereas the other (Thr431) is located at the tail domain.
8344946	2	55	theme	Mammalian	281:289	arg1	neurofilaments					291:304	Mammalian neurofilaments	281:304	Mammalian neurofilaments	281:304	Mammalian neurofilaments are composed of three polypeptide subunits, designed as NF-L, NF-M, and NF-H, all of which are phosphorylated.
8344946	1	56	theme	intermediate	173:184	arg1	filaments					186:194	neuronal intermediate filaments	164:194	neuronal intermediate filaments that play an important role in the growth and maintenance of large myelinated axons	164:278	Localization of multiple O-linked N-acetylglucosamine moieties on neurofilament polypeptides L and M. Neurofilaments are neuronal intermediate filaments that play an important role in the growth and maintenance of large myelinated axons.
8344946	1	56	theme	intermediate	173:184	arg1	Localization					43:54	Localization	43:54	Localization of multiple O-linked N-acetylglucosamine moieties on neurofilament polypeptides L and M. Neurofilaments	43:158	Localization of multiple O-linked N-acetylglucosamine moieties on neurofilament polypeptides L and M. Neurofilaments are neuronal intermediate filaments that play an important role in the growth and maintenance of large myelinated axons.
8344946	3	57	attach	linked	651:656	arg1	threonine					671:679	threonine	671:679	threonine	671:679	Here, we demonstrate by several criteria that neurofilament polypeptides are also modified by an abundant type of intracellular protein glycosylation in which single N-acetylglucosamine monosaccharides are O-glycosidically (O-GlcNAc) linked to serine or threonine residues.
8344946	3	57	attach	linked	651:656	arg2	monosaccharides					603:617	single N-acetylglucosamine monosaccharides	576:617	single N-acetylglucosamine monosaccharides	576:617	Here, we demonstrate by several criteria that neurofilament polypeptides are also modified by an abundant type of intracellular protein glycosylation in which single N-acetylglucosamine monosaccharides are O-glycosidically (O-GlcNAc) linked to serine or threonine residues.
8344946	3	57	attach	linked	651:656	arg1	serine					661:666	serine	661:666	serine	661:666	Here, we demonstrate by several criteria that neurofilament polypeptides are also modified by an abundant type of intracellular protein glycosylation in which single N-acetylglucosamine monosaccharides are O-glycosidically (O-GlcNAc) linked to serine or threonine residues.
8344946	3	57	attach	linked	651:656	arg3	glycosylation					553:565	intracellular protein glycosylation	531:565	intracellular protein glycosylation in which single N-acetylglucosamine monosaccharides are O-glycosidically (O-GlcNAc) linked to serine or threonine residues	531:688	Here, we demonstrate by several criteria that neurofilament polypeptides are also modified by an abundant type of intracellular protein glycosylation in which single N-acetylglucosamine monosaccharides are O-glycosidically (O-GlcNAc) linked to serine or threonine residues.
8344946	6	58	gly	glycosylation	1145:1157	arg2	glycosylation					1145:1157	glycosylation	1145:1157	glycosylation (Thr21 and Ser27)	1145:1175	For NF-L, both major sites of glycosylation (Thr21 and Ser27) are located at the NH2-terminal head domain.
8344946	6	58	gly	glycosylation	1145:1157	arg2	sites					1136:1140	both major sites	1125:1140	both major sites of glycosylation (Thr21 and Ser27)	1125:1175	For NF-L, both major sites of glycosylation (Thr21 and Ser27) are located at the NH2-terminal head domain.
8344946	1	59	dep	polypeptides	123:134	arg1	L					136:136	L	136:136	L	136:136	Localization of multiple O-linked N-acetylglucosamine moieties on neurofilament polypeptides L and M. Neurofilaments are neuronal intermediate filaments that play an important role in the growth and maintenance of large myelinated axons.
8344946	1	59	dep	polypeptides	123:134	arg1	Neurofilaments					145:158	M. Neurofilaments	142:158	M. Neurofilaments	142:158	Localization of multiple O-linked N-acetylglucosamine moieties on neurofilament polypeptides L and M. Neurofilaments are neuronal intermediate filaments that play an important role in the growth and maintenance of large myelinated axons.
8344946	1	60	theme	O-linked	68:75	arg1	moieties					97:104	multiple O-linked N-acetylglucosamine moieties	59:104	multiple O-linked N-acetylglucosamine moieties on neurofilament polypeptides L and M. Neurofilaments	59:158	Localization of multiple O-linked N-acetylglucosamine moieties on neurofilament polypeptides L and M. Neurofilaments are neuronal intermediate filaments that play an important role in the growth and maintenance of large myelinated axons.
8344946	9	61	from	analysis	1681:1688	arg1	neurofilaments					1715:1728	neurofilaments	1715:1728	neurofilaments	1715:1728	Specific identification of these O-GlcNAc attachment sites has set the stage for more detailed mutagenic analysis of O-GlcNAc functions on neurofilaments.
8344946	5	62	gly	glycopeptides	975:987	arg2	glycopeptides					975:987	the glycopeptides	971:987	the glycopeptides	971:987	The predominant sites of O-GlcNAc attachment on NF-L and NF-M are identified using proteolysis, purification of the glycopeptides, and subsequent analysis by automated gas-phase sequencing, manual Edman degradation, and laser desorption mass spectrometry.
8344946	8	63	theme	function	1521:1528	arg1	s					1530:1530	the specific function(s)	1508:1531	the specific function(s) of the saccharide moieties	1508:1558	Deletions encompassing these sites have been shown previously to have a dominant detrimental effect upon neurofilament assembly, raising questions about the specific function(s) of the saccharide moieties at these sites.
8344946	4	64	theme	mol	809:811	arg1	stoichiometry					765:777	a stoichiometry	763:777	a stoichiometry of approximately 0.1 and 0.15 mol of GlcNAc/mol of NF-L and NF-M, respectively	763:856	In purified neurofilament proteins, the O-GlcNAc modifications occur at a stoichiometry of approximately 0.1 and 0.15 mol of GlcNAc/mol of NF-L and NF-M, respectively.
8344946	1	65	theme	moieties	97:104	arg1	Localization					43:54	Localization	43:54	Localization of multiple O-linked N-acetylglucosamine moieties on neurofilament polypeptides L and M. Neurofilaments	43:158	Localization of multiple O-linked N-acetylglucosamine moieties on neurofilament polypeptides L and M. Neurofilaments are neuronal intermediate filaments that play an important role in the growth and maintenance of large myelinated axons.
8344946	1	65	theme	moieties	97:104	arg1	filaments					186:194	neuronal intermediate filaments	164:194	neuronal intermediate filaments that play an important role in the growth and maintenance of large myelinated axons	164:278	Localization of multiple O-linked N-acetylglucosamine moieties on neurofilament polypeptides L and M. Neurofilaments are neuronal intermediate filaments that play an important role in the growth and maintenance of large myelinated axons.
8344946	4	66	theme	GlcNAc/mol	816:825	arg1	mol					809:811	approximately 0.1 and 0.15 mol	782:811	approximately 0.1 and 0.15 mol of GlcNAc/mol of NF-L and NF-M, respectively	782:856	In purified neurofilament proteins, the O-GlcNAc modifications occur at a stoichiometry of approximately 0.1 and 0.15 mol of GlcNAc/mol of NF-L and NF-M, respectively.
8344946	6	67	from	domain	1214:1219	arg1	located					1181:1187	located	1181:1187	located	1181:1187	For NF-L, both major sites of glycosylation (Thr21 and Ser27) are located at the NH2-terminal head domain.
8344946	1	68	theme	neurofilament	109:121	arg1	polypeptides					123:134	neurofilament polypeptides L and M. Neurofilaments	109:158	neurofilament polypeptides L and M. Neurofilaments	109:158	Localization of multiple O-linked N-acetylglucosamine moieties on neurofilament polypeptides L and M. Neurofilaments are neuronal intermediate filaments that play an important role in the growth and maintenance of large myelinated axons.
8344946	8	69	contain	have	1420:1423	arg2	effect					1448:1453	a dominant detrimental effect	1425:1453	a dominant detrimental effect	1425:1453	Deletions encompassing these sites have been shown previously to have a dominant detrimental effect upon neurofilament assembly, raising questions about the specific function(s) of the saccharide moieties at these sites.
8344946	8	69	contain	have	1420:1423	arg1	Deletions					1355:1363	Deletions	1355:1363	Deletions encompassing these sites	1355:1388	Deletions encompassing these sites have been shown previously to have a dominant detrimental effect upon neurofilament assembly, raising questions about the specific function(s) of the saccharide moieties at these sites.
8344946	0	70	theme	neurofilaments	27:40	arg1	Glycosylation					0:12	Glycosylation	0:12	Glycosylation of mammalian neurofilaments.	0:41	Glycosylation of mammalian neurofilaments.
8344946	5	71	theme	manual	1049:1054	arg1	degradation					1062:1072	manual Edman degradation	1049:1072	manual Edman degradation	1049:1072	The predominant sites of O-GlcNAc attachment on NF-L and NF-M are identified using proteolysis, purification of the glycopeptides, and subsequent analysis by automated gas-phase sequencing, manual Edman degradation, and laser desorption mass spectrometry.
8344946	8	72	theme	saccharide	1540:1549	arg1	moieties					1551:1558	the saccharide moieties	1536:1558	the saccharide moieties	1536:1558	Deletions encompassing these sites have been shown previously to have a dominant detrimental effect upon neurofilament assembly, raising questions about the specific function(s) of the saccharide moieties at these sites.
8344946	5	73	theme	automated	1017:1025	arg1	sequencing					1037:1046	automated gas-phase sequencing	1017:1046	automated gas-phase sequencing	1017:1046	The predominant sites of O-GlcNAc attachment on NF-L and NF-M are identified using proteolysis, purification of the glycopeptides, and subsequent analysis by automated gas-phase sequencing, manual Edman degradation, and laser desorption mass spectrometry.
8344946	3	74	dep	serine	661:666	arg1	residues					681:688	residues	681:688	residues	681:688	Here, we demonstrate by several criteria that neurofilament polypeptides are also modified by an abundant type of intracellular protein glycosylation in which single N-acetylglucosamine monosaccharides are O-glycosidically (O-GlcNAc) linked to serine or threonine residues.
8344946	0	75	gly	Glycosylation	0:12	arg1	neurofilaments					27:40	mammalian neurofilaments	17:40	mammalian neurofilaments	17:40	Glycosylation of mammalian neurofilaments.
8344946	3	76	theme	neurofilament	463:475	arg1	polypeptides					477:488	neurofilament polypeptides	463:488	neurofilament polypeptides	463:488	Here, we demonstrate by several criteria that neurofilament polypeptides are also modified by an abundant type of intracellular protein glycosylation in which single N-acetylglucosamine monosaccharides are O-glycosidically (O-GlcNAc) linked to serine or threonine residues.
8344946	7	77	theme	head	1284:1287	arg1	domain					1289:1294	the NH2-terminal head domain	1267:1294	the NH2-terminal head domain	1267:1294	For NF-M, one major site (Thr48) lies within the NH2-terminal head domain, whereas the other (Thr431) is located at the tail domain.
8344946	9	78	theme	sites	1629:1633	arg1	identification					1585:1598	Specific identification	1576:1598	Specific identification of these O-GlcNAc attachment sites	1576:1633	Specific identification of these O-GlcNAc attachment sites has set the stage for more detailed mutagenic analysis of O-GlcNAc functions on neurofilaments.
8344946	6	79	located	located	1181:1187	arg2	glycosylation					1145:1157	glycosylation	1145:1157	glycosylation (Thr21 and Ser27)	1145:1175	For NF-L, both major sites of glycosylation (Thr21 and Ser27) are located at the NH2-terminal head domain.
8344946	6	79	located	located	1181:1187	arg2	sites					1136:1140	both major sites	1125:1140	both major sites of glycosylation (Thr21 and Ser27)	1125:1175	For NF-L, both major sites of glycosylation (Thr21 and Ser27) are located at the NH2-terminal head domain.
8344946	6	79	located	located	1181:1187	arg1	domain					1214:1219	the NH2-terminal head domain	1192:1219	the NH2-terminal head domain	1192:1219	For NF-L, both major sites of glycosylation (Thr21 and Ser27) are located at the NH2-terminal head domain.
8344946	4	80	theme	NF-L	830:833	arg1	GlcNAc/mol					816:825	GlcNAc/mol	816:825	GlcNAc/mol of NF-L and NF-M, respectively	816:856	In purified neurofilament proteins, the O-GlcNAc modifications occur at a stoichiometry of approximately 0.1 and 0.15 mol of GlcNAc/mol of NF-L and NF-M, respectively.
8344946	1	81	theme	large	257:261	arg1	axons					274:278	large myelinated axons	257:278	large myelinated axons	257:278	Localization of multiple O-linked N-acetylglucosamine moieties on neurofilament polypeptides L and M. Neurofilaments are neuronal intermediate filaments that play an important role in the growth and maintenance of large myelinated axons.
8344946	9	82	theme	attachment	1618:1627	arg1	sites					1629:1633	these O-GlcNAc attachment sites	1603:1633	these O-GlcNAc attachment sites	1603:1633	Specific identification of these O-GlcNAc attachment sites has set the stage for more detailed mutagenic analysis of O-GlcNAc functions on neurofilaments.
8344946	6	83	theme	glycosylation	1145:1157	arg1	glycosylation					1145:1157	glycosylation	1145:1157	glycosylation (Thr21 and Ser27)	1145:1175	For NF-L, both major sites of glycosylation (Thr21 and Ser27) are located at the NH2-terminal head domain.
8344946	6	83	theme	glycosylation	1145:1157	arg1	sites					1136:1140	both major sites	1125:1140	both major sites of glycosylation (Thr21 and Ser27)	1125:1175	For NF-L, both major sites of glycosylation (Thr21 and Ser27) are located at the NH2-terminal head domain.
8344946	4	84	theme	NF-M	839:842	arg1	GlcNAc/mol					816:825	GlcNAc/mol	816:825	GlcNAc/mol of NF-L and NF-M, respectively	816:856	In purified neurofilament proteins, the O-GlcNAc modifications occur at a stoichiometry of approximately 0.1 and 0.15 mol of GlcNAc/mol of NF-L and NF-M, respectively.
8344946	3	85	theme	intracellular	531:543	arg1	glycosylation					553:565	intracellular protein glycosylation	531:565	intracellular protein glycosylation in which single N-acetylglucosamine monosaccharides are O-glycosidically (O-GlcNAc) linked to serine or threonine residues	531:688	Here, we demonstrate by several criteria that neurofilament polypeptides are also modified by an abundant type of intracellular protein glycosylation in which single N-acetylglucosamine monosaccharides are O-glycosidically (O-GlcNAc) linked to serine or threonine residues.
8344946	1	86	from	moieties	97:104	arg1	polypeptides					123:134	neurofilament polypeptides L and M. Neurofilaments	109:158	neurofilament polypeptides L and M. Neurofilaments	109:158	Localization of multiple O-linked N-acetylglucosamine moieties on neurofilament polypeptides L and M. Neurofilaments are neuronal intermediate filaments that play an important role in the growth and maintenance of large myelinated axons.
8344946	7	87	located	located	1327:1333	arg2	located					1327:1333	located	1327:1333	located	1327:1333	For NF-M, one major site (Thr48) lies within the NH2-terminal head domain, whereas the other (Thr431) is located at the tail domain.
8344946	7	87	located	located	1327:1333	arg2	Thr431					1316:1321	Thr431	1316:1321	Thr431	1316:1321	For NF-M, one major site (Thr48) lies within the NH2-terminal head domain, whereas the other (Thr431) is located at the tail domain.
8344946	7	87	located	located	1327:1333	arg2	other					1309:1313	other	1309:1313	other	1309:1313	For NF-M, one major site (Thr48) lies within the NH2-terminal head domain, whereas the other (Thr431) is located at the tail domain.
8344946	7	87	located	located	1327:1333	arg1	domain					1347:1352	the tail domain	1338:1352	the tail domain	1338:1352	For NF-M, one major site (Thr48) lies within the NH2-terminal head domain, whereas the other (Thr431) is located at the tail domain.
11544325	7	0	theme	LPS	1320:1322	arg1	transduction					1304:1315	TLR4-mediated signal transduction	1283:1315	TLR4-mediated signal transduction of LPS	1283:1322	These observations demonstrate that hMD-2 undergoes N-linked glycosylation at Asn(26) and Asn(114), and that these glycosylations are crucial for TLR4-mediated signal transduction of LPS.
11544325	5	1	theme	MD-2	984:987	arg1	ability					973:979	the ability	969:979	the ability of MD-2 to complement TLR4-mediated activation of NF-kappaB by LPS	969:1046	Although these mutants were expressed on the cell surface and maintained its ability to associate with human TLR4, these mutations or tunicamycin treatment substantially impaired the ability of MD-2 to complement TLR4-mediated activation of NF-kappaB by LPS.
11544325	5	2	theme	tunicamycin	924:934	arg1	treatment					936:944	tunicamycin treatment	924:944	tunicamycin treatment	924:944	Although these mutants were expressed on the cell surface and maintained its ability to associate with human TLR4, these mutations or tunicamycin treatment substantially impaired the ability of MD-2 to complement TLR4-mediated activation of NF-kappaB by LPS.
11544325	0	3	theme	human	51:55	arg1	MD-2					57:60	human MD-2	51:60	human MD-2	51:60	N-linked glycosylations at Asn(26) and Asn(114) of human MD-2 are required for toll-like receptor 4-mediated activation of NF-kappaB by lipopolysaccharide.
11544325	4	4	theme	potential	572:580	arg1	sites					596:600	two potential glycosylation sites	568:600	two potential glycosylation sites (Asn(26) and Asn(114)) of MD-2	568:631	Mutation of either one of two potential glycosylation sites (Asn(26) and Asn(114)) of MD-2 resulted in the disappearance of the slowest mobility form, and only the fastest form was detected in hMD-2 carrying mutations at both Asn(26) and Asn(114).
11544325	4	4	theme	potential	572:580	arg1	Asn					615:617	Asn(114)	615:622	Asn(114)	615:622	Mutation of either one of two potential glycosylation sites (Asn(26) and Asn(114)) of MD-2 resulted in the disappearance of the slowest mobility form, and only the fastest form was detected in hMD-2 carrying mutations at both Asn(26) and Asn(114).
11544325	4	4	theme	potential	572:580	arg1	Asn					603:605	Asn(26)	603:609	Asn(26)	603:609	Mutation of either one of two potential glycosylation sites (Asn(26) and Asn(114)) of MD-2 resulted in the disappearance of the slowest mobility form, and only the fastest form was detected in hMD-2 carrying mutations at both Asn(26) and Asn(114).
11544325	4	4	theme	potential	572:580	arg1	MD-2					628:631	MD-2	628:631	MD-2	628:631	Mutation of either one of two potential glycosylation sites (Asn(26) and Asn(114)) of MD-2 resulted in the disappearance of the slowest mobility form, and only the fastest form was detected in hMD-2 carrying mutations at both Asn(26) and Asn(114).
11544325	7	5	theme	TLR4-mediated	1283:1295	arg1	transduction					1304:1315	TLR4-mediated signal transduction	1283:1315	TLR4-mediated signal transduction of LPS	1283:1322	These observations demonstrate that hMD-2 undergoes N-linked glycosylation at Asn(26) and Asn(114), and that these glycosylations are crucial for TLR4-mediated signal transduction of LPS.
11544325	0	6	link	N-linked	0:7	arg1	glycosylations					9:22	N-linked glycosylations	0:22	N-linked glycosylations at Asn(26) and Asn(114) of human MD-2	0:60	N-linked glycosylations at Asn(26) and Asn(114) of human MD-2 are required for toll-like receptor 4-mediated activation of NF-kappaB by lipopolysaccharide.
11544325	4	7	theme	mobility	678:685	arg1	form					687:690	the slowest mobility form	666:690	the slowest mobility form	666:690	Mutation of either one of two potential glycosylation sites (Asn(26) and Asn(114)) of MD-2 resulted in the disappearance of the slowest mobility form, and only the fastest form was detected in hMD-2 carrying mutations at both Asn(26) and Asn(114).
11544325	0	8	theme	MD-2	57:60	arg1	glycosylations					9:22	N-linked glycosylations	0:22	N-linked glycosylations at Asn(26) and Asn(114) of human MD-2	0:60	N-linked glycosylations at Asn(26) and Asn(114) of human MD-2 are required for toll-like receptor 4-mediated activation of NF-kappaB by lipopolysaccharide.
11544325	4	9	gly	glycosylation	582:594	arg2	two					568:570	two	568:570	two	568:570	Mutation of either one of two potential glycosylation sites (Asn(26) and Asn(114)) of MD-2 resulted in the disappearance of the slowest mobility form, and only the fastest form was detected in hMD-2 carrying mutations at both Asn(26) and Asn(114).
11544325	4	9	gly	glycosylation	582:594	arg2	Asn					603:605	Asn(26)	603:609	Asn(26)	603:609	Mutation of either one of two potential glycosylation sites (Asn(26) and Asn(114)) of MD-2 resulted in the disappearance of the slowest mobility form, and only the fastest form was detected in hMD-2 carrying mutations at both Asn(26) and Asn(114).
11544325	4	9	gly	glycosylation	582:594	arg1	MD-2					628:631	MD-2	628:631	MD-2	628:631	Mutation of either one of two potential glycosylation sites (Asn(26) and Asn(114)) of MD-2 resulted in the disappearance of the slowest mobility form, and only the fastest form was detected in hMD-2 carrying mutations at both Asn(26) and Asn(114).
11544325	4	9	gly	glycosylation	582:594	arg2	MD-2					628:631	MD-2	628:631	MD-2	628:631	Mutation of either one of two potential glycosylation sites (Asn(26) and Asn(114)) of MD-2 resulted in the disappearance of the slowest mobility form, and only the fastest form was detected in hMD-2 carrying mutations at both Asn(26) and Asn(114).
11544325	4	9	gly	glycosylation	582:594	arg2	Asn					615:617	Asn(114)	615:622	Asn(114)	615:622	Mutation of either one of two potential glycosylation sites (Asn(26) and Asn(114)) of MD-2 resulted in the disappearance of the slowest mobility form, and only the fastest form was detected in hMD-2 carrying mutations at both Asn(26) and Asn(114).
11544325	4	9	gly	glycosylation	582:594	arg2	sites					596:600	two potential glycosylation sites	568:600	two potential glycosylation sites (Asn(26) and Asn(114)) of MD-2	568:631	Mutation of either one of two potential glycosylation sites (Asn(26) and Asn(114)) of MD-2 resulted in the disappearance of the slowest mobility form, and only the fastest form was detected in hMD-2 carrying mutations at both Asn(26) and Asn(114).
11544325	3	10	theme	single	490:495	arg1	form					497:500	only a single form	483:500	only a single form with the fastest mobility	483:526	After N-glycosidase treatment of the cellular extract prepared from cells expressing hMD-2, only a single form with the fastest mobility was detected.
11544325	3	11	theme	N-glycosidase	397:409	arg1	treatment					411:419	N-glycosidase treatment	397:419	N-glycosidase treatment of the cellular extract prepared from cells expressing hMD-2	397:480	After N-glycosidase treatment of the cellular extract prepared from cells expressing hMD-2, only a single form with the fastest mobility was detected.
11544325	2	12	theme	blotting	276:283	arg1	analysis					285:292	Western blotting analysis	268:292	Western blotting analysis	268:292	Western blotting analysis revealed the presence of three forms of human (h)MD-2 with different electrophoretic mobilities.
11544325	0	13	theme	N-linked	0:7	arg1	glycosylations					9:22	N-linked glycosylations	0:22	N-linked glycosylations at Asn(26) and Asn(114) of human MD-2	0:60	N-linked glycosylations at Asn(26) and Asn(114) of human MD-2 are required for toll-like receptor 4-mediated activation of NF-kappaB by lipopolysaccharide.
11544325	5	14	theme	NF-kappaB	1031:1039	arg1	activation					1017:1026	TLR4-mediated activation	1003:1026	TLR4-mediated activation of NF-kappaB by LPS	1003:1046	Although these mutants were expressed on the cell surface and maintained its ability to associate with human TLR4, these mutations or tunicamycin treatment substantially impaired the ability of MD-2 to complement TLR4-mediated activation of NF-kappaB by LPS.
11544325	7	15	link	N-linked	1189:1196	arg1	glycosylation					1198:1210	N-linked glycosylation	1189:1210	N-linked glycosylation	1189:1210	These observations demonstrate that hMD-2 undergoes N-linked glycosylation at Asn(26) and Asn(114), and that these glycosylations are crucial for TLR4-mediated signal transduction of LPS.
11544325	2	16	theme	Western	268:274	arg1	analysis					285:292	Western blotting analysis	268:292	Western blotting analysis	268:292	Western blotting analysis revealed the presence of three forms of human (h)MD-2 with different electrophoretic mobilities.
11544325	2	17	theme	human	334:338	arg1	h					341:341	h	341:341	h	341:341	Western blotting analysis revealed the presence of three forms of human (h)MD-2 with different electrophoretic mobilities.
11544325	2	17	theme	human	334:338	arg1	MD-2					343:346	human (h)MD-2	334:346	human (h)MD-2	334:346	Western blotting analysis revealed the presence of three forms of human (h)MD-2 with different electrophoretic mobilities.
11544325	2	18	theme	electrophoretic	363:377	arg1	mobilities					379:388	different electrophoretic mobilities	353:388	different electrophoretic mobilities	353:388	Western blotting analysis revealed the presence of three forms of human (h)MD-2 with different electrophoretic mobilities.
11544325	7	19	gly	glycosylation	1198:1210	arg1	Asn					1215:1217	Asn	1215:1217	Asn(26)	1215:1221	These observations demonstrate that hMD-2 undergoes N-linked glycosylation at Asn(26) and Asn(114), and that these glycosylations are crucial for TLR4-mediated signal transduction of LPS.
11544325	7	19	gly	glycosylation	1198:1210	arg1	hMD-2					1173:1177	hMD-2	1173:1177	hMD-2	1173:1177	These observations demonstrate that hMD-2 undergoes N-linked glycosylation at Asn(26) and Asn(114), and that these glycosylations are crucial for TLR4-mediated signal transduction of LPS.
11544325	7	19	gly	glycosylation	1198:1210	arg1	114					1231:1233	114	1231:1233	114	1231:1233	These observations demonstrate that hMD-2 undergoes N-linked glycosylation at Asn(26) and Asn(114), and that these glycosylations are crucial for TLR4-mediated signal transduction of LPS.
11544325	7	19	gly	glycosylation	1198:1210	arg1	26					1219:1220	26	1219:1220	26	1219:1220	These observations demonstrate that hMD-2 undergoes N-linked glycosylation at Asn(26) and Asn(114), and that these glycosylations are crucial for TLR4-mediated signal transduction of LPS.
11544325	7	19	gly	glycosylation	1198:1210	arg1	Asn					1227:1229	Asn	1227:1229	Asn(114)	1227:1234	These observations demonstrate that hMD-2 undergoes N-linked glycosylation at Asn(26) and Asn(114), and that these glycosylations are crucial for TLR4-mediated signal transduction of LPS.
11544325	1	20	theme	TLR4-mediated	239:251	arg1	signaling					257:265	TLR4-mediated LPS signaling	239:265	TLR4-mediated LPS signaling	239:265	MD-2 is physically associated with Toll-like receptor 4 (TLR4) and is required for TLR4-mediated LPS signaling.
11544325	4	21	theme	one	561:563	arg1	Mutation					542:549	Mutation	542:549	Mutation of either one of two potential glycosylation sites (Asn(26) and Asn(114)) of MD-2	542:631	Mutation of either one of two potential glycosylation sites (Asn(26) and Asn(114)) of MD-2 resulted in the disappearance of the slowest mobility form, and only the fastest form was detected in hMD-2 carrying mutations at both Asn(26) and Asn(114).
11544325	3	22	theme	fastest	511:517	arg1	mobility					519:526	the fastest mobility	507:526	the fastest mobility	507:526	After N-glycosidase treatment of the cellular extract prepared from cells expressing hMD-2, only a single form with the fastest mobility was detected.
11544325	2	23	theme	different	353:361	arg1	mobilities					379:388	different electrophoretic mobilities	353:388	different electrophoretic mobilities	353:388	Western blotting analysis revealed the presence of three forms of human (h)MD-2 with different electrophoretic mobilities.
11544325	1	24	theme	LPS	253:255	arg1	signaling					257:265	TLR4-mediated LPS signaling	239:265	TLR4-mediated LPS signaling	239:265	MD-2 is physically associated with Toll-like receptor 4 (TLR4) and is required for TLR4-mediated LPS signaling.
11544325	0	25	theme	receptor	89:96	arg1	activation					109:118	toll-like receptor 4-mediated activation	79:118	toll-like receptor 4-mediated activation of NF-kappaB by lipopolysaccharide	79:153	N-linked glycosylations at Asn(26) and Asn(114) of human MD-2 are required for toll-like receptor 4-mediated activation of NF-kappaB by lipopolysaccharide.
11544325	4	26	theme	fastest	706:712	arg1	form					714:717	only the fastest form	697:717	only the fastest form	697:717	Mutation of either one of two potential glycosylation sites (Asn(26) and Asn(114)) of MD-2 resulted in the disappearance of the slowest mobility form, and only the fastest form was detected in hMD-2 carrying mutations at both Asn(26) and Asn(114).
11544325	7	27	theme	signal	1297:1302	arg1	transduction					1304:1315	TLR4-mediated signal transduction	1283:1315	TLR4-mediated signal transduction of LPS	1283:1322	These observations demonstrate that hMD-2 undergoes N-linked glycosylation at Asn(26) and Asn(114), and that these glycosylations are crucial for TLR4-mediated signal transduction of LPS.
11544325	0	28	theme	toll-like	79:87	arg1	activation					109:118	toll-like receptor 4-mediated activation	79:118	toll-like receptor 4-mediated activation of NF-kappaB by lipopolysaccharide	79:153	N-linked glycosylations at Asn(26) and Asn(114) of human MD-2 are required for toll-like receptor 4-mediated activation of NF-kappaB by lipopolysaccharide.
11544325	2	29	with	presence	307:314	arg1	mobilities					379:388	different electrophoretic mobilities	353:388	different electrophoretic mobilities	353:388	Western blotting analysis revealed the presence of three forms of human (h)MD-2 with different electrophoretic mobilities.
11544325	0	30	gly	glycosylations	9:22	arg2	Asn					27:29	Asn	27:29	Asn(26)	27:33	N-linked glycosylations at Asn(26) and Asn(114) of human MD-2 are required for toll-like receptor 4-mediated activation of NF-kappaB by lipopolysaccharide.
11544325	0	30	gly	glycosylations	9:22	arg2	26					31:32	26	31:32	26	31:32	N-linked glycosylations at Asn(26) and Asn(114) of human MD-2 are required for toll-like receptor 4-mediated activation of NF-kappaB by lipopolysaccharide.
11544325	0	30	gly	glycosylations	9:22	arg2	114					43:45	114	43:45	114	43:45	N-linked glycosylations at Asn(26) and Asn(114) of human MD-2 are required for toll-like receptor 4-mediated activation of NF-kappaB by lipopolysaccharide.
11544325	0	30	gly	glycosylations	9:22	arg1	MD-2					57:60	human MD-2	51:60	human MD-2	51:60	N-linked glycosylations at Asn(26) and Asn(114) of human MD-2 are required for toll-like receptor 4-mediated activation of NF-kappaB by lipopolysaccharide.
11544325	0	30	gly	glycosylations	9:22	arg2	Asn					39:41	Asn	39:41	Asn(114)	39:46	N-linked glycosylations at Asn(26) and Asn(114) of human MD-2 are required for toll-like receptor 4-mediated activation of NF-kappaB by lipopolysaccharide.
11544325	2	31	theme	MD-2	343:346	arg1	forms					325:329	three forms	319:329	three forms of human (h)MD-2	319:346	Western blotting analysis revealed the presence of three forms of human (h)MD-2 with different electrophoretic mobilities.
11544325	3	32	with	form	497:500	arg1	mobility					519:526	the fastest mobility	507:526	the fastest mobility	507:526	After N-glycosidase treatment of the cellular extract prepared from cells expressing hMD-2, only a single form with the fastest mobility was detected.
11544325	5	33	theme	TLR4-mediated	1003:1015	arg1	activation					1017:1026	TLR4-mediated activation	1003:1026	TLR4-mediated activation of NF-kappaB by LPS	1003:1046	Although these mutants were expressed on the cell surface and maintained its ability to associate with human TLR4, these mutations or tunicamycin treatment substantially impaired the ability of MD-2 to complement TLR4-mediated activation of NF-kappaB by LPS.
11544325	0	34	from	Asn	39:41	arg1	glycosylations					9:22	N-linked glycosylations	0:22	N-linked glycosylations at Asn(26) and Asn(114) of human MD-2	0:60	N-linked glycosylations at Asn(26) and Asn(114) of human MD-2 are required for toll-like receptor 4-mediated activation of NF-kappaB by lipopolysaccharide.
11544325	3	35	theme	cellular	428:435	arg1	extract					437:443	the cellular extract	424:443	the cellular extract prepared from cells expressing hMD-2	424:480	After N-glycosidase treatment of the cellular extract prepared from cells expressing hMD-2, only a single form with the fastest mobility was detected.
11544325	0	36	theme	4-mediated	98:107	arg1	activation					109:118	toll-like receptor 4-mediated activation	79:118	toll-like receptor 4-mediated activation of NF-kappaB by lipopolysaccharide	79:153	N-linked glycosylations at Asn(26) and Asn(114) of human MD-2 are required for toll-like receptor 4-mediated activation of NF-kappaB by lipopolysaccharide.
11544325	0	37	theme	NF-kappaB	123:131	arg1	activation					109:118	toll-like receptor 4-mediated activation	79:118	toll-like receptor 4-mediated activation of NF-kappaB by lipopolysaccharide	79:153	N-linked glycosylations at Asn(26) and Asn(114) of human MD-2 are required for toll-like receptor 4-mediated activation of NF-kappaB by lipopolysaccharide.
11544325	5	38	theme	human	893:897	arg1	TLR4					899:902	human TLR4	893:902	human TLR4	893:902	Although these mutants were expressed on the cell surface and maintained its ability to associate with human TLR4, these mutations or tunicamycin treatment substantially impaired the ability of MD-2 to complement TLR4-mediated activation of NF-kappaB by LPS.
11544325	5	39	theme	cell	835:838	arg1	surface					840:846	the cell surface	831:846	the cell surface	831:846	Although these mutants were expressed on the cell surface and maintained its ability to associate with human TLR4, these mutations or tunicamycin treatment substantially impaired the ability of MD-2 to complement TLR4-mediated activation of NF-kappaB by LPS.
11544325	4	40	dep	sites	596:600	arg1	sites					596:600	two potential glycosylation sites	568:600	two potential glycosylation sites (Asn(26) and Asn(114)) of MD-2	568:631	Mutation of either one of two potential glycosylation sites (Asn(26) and Asn(114)) of MD-2 resulted in the disappearance of the slowest mobility form, and only the fastest form was detected in hMD-2 carrying mutations at both Asn(26) and Asn(114).
11544325	4	40	dep	sites	596:600	arg1	Asn					615:617	Asn(114)	615:622	Asn(114)	615:622	Mutation of either one of two potential glycosylation sites (Asn(26) and Asn(114)) of MD-2 resulted in the disappearance of the slowest mobility form, and only the fastest form was detected in hMD-2 carrying mutations at both Asn(26) and Asn(114).
11544325	4	40	dep	sites	596:600	arg1	Asn					603:605	Asn(26)	603:609	Asn(26)	603:609	Mutation of either one of two potential glycosylation sites (Asn(26) and Asn(114)) of MD-2 resulted in the disappearance of the slowest mobility form, and only the fastest form was detected in hMD-2 carrying mutations at both Asn(26) and Asn(114).
11544325	4	40	dep	sites	596:600	arg1	MD-2					628:631	MD-2	628:631	MD-2	628:631	Mutation of either one of two potential glycosylation sites (Asn(26) and Asn(114)) of MD-2 resulted in the disappearance of the slowest mobility form, and only the fastest form was detected in hMD-2 carrying mutations at both Asn(26) and Asn(114).
11544325	3	41	theme	extract	437:443	arg1	treatment					411:419	N-glycosidase treatment	397:419	N-glycosidase treatment of the cellular extract prepared from cells expressing hMD-2	397:480	After N-glycosidase treatment of the cellular extract prepared from cells expressing hMD-2, only a single form with the fastest mobility was detected.
11544325	4	42	contain	carrying	741:748	arg1	hMD-2					735:739	hMD-2	735:739	hMD-2 carrying mutations at both Asn(26) and Asn(114)	735:787	Mutation of either one of two potential glycosylation sites (Asn(26) and Asn(114)) of MD-2 resulted in the disappearance of the slowest mobility form, and only the fastest form was detected in hMD-2 carrying mutations at both Asn(26) and Asn(114).
11544325	4	42	contain	carrying	741:748	arg2	mutations					750:758	mutations	750:758	mutations	750:758	Mutation of either one of two potential glycosylation sites (Asn(26) and Asn(114)) of MD-2 resulted in the disappearance of the slowest mobility form, and only the fastest form was detected in hMD-2 carrying mutations at both Asn(26) and Asn(114).
11544325	1	43	theme	Toll-like	191:199	arg1	receptor					201:208	Toll-like receptor 4	191:210	Toll-like receptor 4 (TLR4)	191:217	MD-2 is physically associated with Toll-like receptor 4 (TLR4) and is required for TLR4-mediated LPS signaling.
11544325	1	43	theme	Toll-like	191:199	arg1	TLR4					213:216	TLR4	213:216	TLR4	213:216	MD-2 is physically associated with Toll-like receptor 4 (TLR4) and is required for TLR4-mediated LPS signaling.
11544325	4	44	theme	slowest	670:676	arg1	form					687:690	the slowest mobility form	666:690	the slowest mobility form	666:690	Mutation of either one of two potential glycosylation sites (Asn(26) and Asn(114)) of MD-2 resulted in the disappearance of the slowest mobility form, and only the fastest form was detected in hMD-2 carrying mutations at both Asn(26) and Asn(114).
11544325	4	45	dep	one	561:563	arg1	either					554:559	either	554:559	either	554:559	Mutation of either one of two potential glycosylation sites (Asn(26) and Asn(114)) of MD-2 resulted in the disappearance of the slowest mobility form, and only the fastest form was detected in hMD-2 carrying mutations at both Asn(26) and Asn(114).
11544325	4	46	theme	form	687:690	arg1	disappearance					649:661	the disappearance	645:661	the disappearance of the slowest mobility form	645:690	Mutation of either one of two potential glycosylation sites (Asn(26) and Asn(114)) of MD-2 resulted in the disappearance of the slowest mobility form, and only the fastest form was detected in hMD-2 carrying mutations at both Asn(26) and Asn(114).
11544325	4	47	theme	MD-2	628:631	arg1	sites					596:600	two potential glycosylation sites	568:600	two potential glycosylation sites (Asn(26) and Asn(114)) of MD-2	568:631	Mutation of either one of two potential glycosylation sites (Asn(26) and Asn(114)) of MD-2 resulted in the disappearance of the slowest mobility form, and only the fastest form was detected in hMD-2 carrying mutations at both Asn(26) and Asn(114).
11544325	4	47	theme	MD-2	628:631	arg1	Asn					615:617	Asn(114)	615:622	Asn(114)	615:622	Mutation of either one of two potential glycosylation sites (Asn(26) and Asn(114)) of MD-2 resulted in the disappearance of the slowest mobility form, and only the fastest form was detected in hMD-2 carrying mutations at both Asn(26) and Asn(114).
11544325	4	47	theme	MD-2	628:631	arg1	Asn					603:605	Asn(26)	603:609	Asn(26)	603:609	Mutation of either one of two potential glycosylation sites (Asn(26) and Asn(114)) of MD-2 resulted in the disappearance of the slowest mobility form, and only the fastest form was detected in hMD-2 carrying mutations at both Asn(26) and Asn(114).
11544325	4	47	theme	MD-2	628:631	arg1	MD-2					628:631	MD-2	628:631	MD-2	628:631	Mutation of either one of two potential glycosylation sites (Asn(26) and Asn(114)) of MD-2 resulted in the disappearance of the slowest mobility form, and only the fastest form was detected in hMD-2 carrying mutations at both Asn(26) and Asn(114).
11544325	4	48	theme	sites	596:600	arg1	sites					596:600	two potential glycosylation sites	568:600	two potential glycosylation sites (Asn(26) and Asn(114)) of MD-2	568:631	Mutation of either one of two potential glycosylation sites (Asn(26) and Asn(114)) of MD-2 resulted in the disappearance of the slowest mobility form, and only the fastest form was detected in hMD-2 carrying mutations at both Asn(26) and Asn(114).
11544325	4	48	theme	sites	596:600	arg1	one					561:563	one	561:563	one	561:563	Mutation of either one of two potential glycosylation sites (Asn(26) and Asn(114)) of MD-2 resulted in the disappearance of the slowest mobility form, and only the fastest form was detected in hMD-2 carrying mutations at both Asn(26) and Asn(114).
11544325	4	48	theme	sites	596:600	arg1	Asn					615:617	Asn(114)	615:622	Asn(114)	615:622	Mutation of either one of two potential glycosylation sites (Asn(26) and Asn(114)) of MD-2 resulted in the disappearance of the slowest mobility form, and only the fastest form was detected in hMD-2 carrying mutations at both Asn(26) and Asn(114).
11544325	4	48	theme	sites	596:600	arg1	Asn					603:605	Asn(26)	603:609	Asn(26)	603:609	Mutation of either one of two potential glycosylation sites (Asn(26) and Asn(114)) of MD-2 resulted in the disappearance of the slowest mobility form, and only the fastest form was detected in hMD-2 carrying mutations at both Asn(26) and Asn(114).
11544325	4	48	theme	sites	596:600	arg1	MD-2					628:631	MD-2	628:631	MD-2	628:631	Mutation of either one of two potential glycosylation sites (Asn(26) and Asn(114)) of MD-2 resulted in the disappearance of the slowest mobility form, and only the fastest form was detected in hMD-2 carrying mutations at both Asn(26) and Asn(114).
11544325	4	49	theme	glycosylation	582:594	arg1	sites					596:600	two potential glycosylation sites	568:600	two potential glycosylation sites (Asn(26) and Asn(114)) of MD-2	568:631	Mutation of either one of two potential glycosylation sites (Asn(26) and Asn(114)) of MD-2 resulted in the disappearance of the slowest mobility form, and only the fastest form was detected in hMD-2 carrying mutations at both Asn(26) and Asn(114).
11544325	4	49	theme	glycosylation	582:594	arg1	Asn					615:617	Asn(114)	615:622	Asn(114)	615:622	Mutation of either one of two potential glycosylation sites (Asn(26) and Asn(114)) of MD-2 resulted in the disappearance of the slowest mobility form, and only the fastest form was detected in hMD-2 carrying mutations at both Asn(26) and Asn(114).
11544325	4	49	theme	glycosylation	582:594	arg1	Asn					603:605	Asn(26)	603:609	Asn(26)	603:609	Mutation of either one of two potential glycosylation sites (Asn(26) and Asn(114)) of MD-2 resulted in the disappearance of the slowest mobility form, and only the fastest form was detected in hMD-2 carrying mutations at both Asn(26) and Asn(114).
11544325	4	49	theme	glycosylation	582:594	arg1	MD-2					628:631	MD-2	628:631	MD-2	628:631	Mutation of either one of two potential glycosylation sites (Asn(26) and Asn(114)) of MD-2 resulted in the disappearance of the slowest mobility form, and only the fastest form was detected in hMD-2 carrying mutations at both Asn(26) and Asn(114).
11544325	7	50	theme	N-linked	1189:1196	arg1	glycosylation					1198:1210	N-linked glycosylation	1189:1210	N-linked glycosylation	1189:1210	These observations demonstrate that hMD-2 undergoes N-linked glycosylation at Asn(26) and Asn(114), and that these glycosylations are crucial for TLR4-mediated signal transduction of LPS.
11544325	0	51	from	Asn	27:29	arg1	glycosylations					9:22	N-linked glycosylations	0:22	N-linked glycosylations at Asn(26) and Asn(114) of human MD-2	0:60	N-linked glycosylations at Asn(26) and Asn(114) of human MD-2 are required for toll-like receptor 4-mediated activation of NF-kappaB by lipopolysaccharide.
11544325	6	52	theme	LPS	1049:1051	arg1	binding					1053:1059	LPS binding	1049:1059	LPS binding to cells expressing CD14, TLR4, and MD-2	1049:1100	LPS binding to cells expressing CD14, TLR4, and MD-2 was unaffected by these mutations.
11544325	2	53	theme	forms	325:329	arg1	presence					307:314	the presence	303:314	the presence of three forms of human (h)MD-2 with different electrophoretic mobilities	303:388	Western blotting analysis revealed the presence of three forms of human (h)MD-2 with different electrophoretic mobilities.
11544325	4	54	located	detected	723:730	arg1	hMD-2					735:739	hMD-2	735:739	hMD-2 carrying mutations at both Asn(26) and Asn(114)	735:787	Mutation of either one of two potential glycosylation sites (Asn(26) and Asn(114)) of MD-2 resulted in the disappearance of the slowest mobility form, and only the fastest form was detected in hMD-2 carrying mutations at both Asn(26) and Asn(114).
11544325	4	54	located	detected	723:730	arg2	form					714:717	only the fastest form	697:717	only the fastest form	697:717	Mutation of either one of two potential glycosylation sites (Asn(26) and Asn(114)) of MD-2 resulted in the disappearance of the slowest mobility form, and only the fastest form was detected in hMD-2 carrying mutations at both Asn(26) and Asn(114).
24841998	6	0	theme	N-glycopeptides	988:1002	arg1	analysis					969:976	in silico analysis	959:976	in silico analysis of intact N-glycopeptides	959:1002	Identification was performed on the web-based tool GlycopeptideID, developed for in silico analysis of intact N-glycopeptides.
24841998	0	1	theme	levels	40:45	arg1	Comparison					0:9	Comparison	0:9	Comparison of sialylated N-glycopeptide levels in serum of pancreatic cancer patients, acute pancreatitis patients, and healthy controls.	0:136	Comparison of sialylated N-glycopeptide levels in serum of pancreatic cancer patients, acute pancreatitis patients, and healthy controls.
24841998	9	2	dep	tenfold	1341:1347	arg1	to					1338:1339	to	1338:1339	to	1338:1339	In pancreatitis, up to tenfold changes were found in some glycoforms, and in pancreatic cancer, threefold.
24841998	11	3	theme	sialylated	1686:1695	arg1	N-glycopeptides					1697:1711	intact sialylated N-glycopeptides	1679:1711	intact sialylated N-glycopeptides derived from acute-phase proteins, and immunoglobulins	1679:1766	In conclusion, the analysis shows that pancreatic cancer, and acute pancreatitis are associated with changes in concentrations of intact sialylated N-glycopeptides derived from acute-phase proteins, and immunoglobulins, and that changes are site specific.
24841998	11	4	theme	pancreatic	1588:1597	arg1	cancer					1599:1604	pancreatic cancer	1588:1604	pancreatic cancer	1588:1604	In conclusion, the analysis shows that pancreatic cancer, and acute pancreatitis are associated with changes in concentrations of intact sialylated N-glycopeptides derived from acute-phase proteins, and immunoglobulins, and that changes are site specific.
24841998	11	5	theme	acute-phase	1726:1736	arg1	proteins					1738:1745	acute-phase proteins	1726:1745	acute-phase proteins	1726:1745	In conclusion, the analysis shows that pancreatic cancer, and acute pancreatitis are associated with changes in concentrations of intact sialylated N-glycopeptides derived from acute-phase proteins, and immunoglobulins, and that changes are site specific.
24841998	11	6	theme	acute	1611:1615	arg1	pancreatitis					1617:1628	acute pancreatitis	1611:1628	acute pancreatitis	1611:1628	In conclusion, the analysis shows that pancreatic cancer, and acute pancreatitis are associated with changes in concentrations of intact sialylated N-glycopeptides derived from acute-phase proteins, and immunoglobulins, and that changes are site specific.
24841998	8	7	theme	statistical	1281:1291	arg1	significance					1293:1304	statistical significance	1281:1304	statistical significance (p < 0.05)	1281:1315	Pancreatitis patient sera contained 38, and pancreatic cancer patients sera contained 13 glycoform changes with statistical significance (p < 0.05).
24841998	8	7	theme	statistical	1281:1291	arg1	<					1309:1309	p < 0.05	1307:1314	p < 0.05	1307:1314	Pancreatitis patient sera contained 38, and pancreatic cancer patients sera contained 13 glycoform changes with statistical significance (p < 0.05).
24841998	4	8	theme	individuals	718:728	arg1	sera					641:644	albumin-depleted sera	624:644	albumin-depleted sera of pancreatic cancer patients, acute pancreatitis patients, and healthy individuals	624:728	We used Sambucus nigra lectin affinity chromatography to enrich α-2,6 sialylated tryptic N-glycopeptides from albumin-depleted sera of pancreatic cancer patients, acute pancreatitis patients, and healthy individuals, and compared their relative abundance using ultra performance LC-MS.
24841998	4	9	theme	acute	677:681	arg1	pancreatitis					683:694	acute pancreatitis	677:694	acute pancreatitis patients	677:703	We used Sambucus nigra lectin affinity chromatography to enrich α-2,6 sialylated tryptic N-glycopeptides from albumin-depleted sera of pancreatic cancer patients, acute pancreatitis patients, and healthy individuals, and compared their relative abundance using ultra performance LC-MS.
24841998	2	10	theme	early	308:312	arg1	diagnosis					314:322	early diagnosis	308:322	early diagnosis	308:322	Pancreatic cancer patients would benefit from early diagnosis, as the disease is often detected in an advanced stage and has poor prognosis.
24841998	1	11	theme	pathological	193:204	arg1	conditions					206:215	pathological conditions	193:215	pathological conditions	193:215	Serum protein glycosylation is known to be affected by pathological conditions, including cancer and inflammatory diseases.
24841998	1	11	theme	pathological	193:204	arg1	cancer					228:233	cancer	228:233	cancer	228:233	Serum protein glycosylation is known to be affected by pathological conditions, including cancer and inflammatory diseases.
24841998	1	11	theme	pathological	193:204	arg1	diseases					252:259	inflammatory diseases	239:259	inflammatory diseases	239:259	Serum protein glycosylation is known to be affected by pathological conditions, including cancer and inflammatory diseases.
24841998	7	12	with	proteins	1036:1043	arg1	sites					1126:1130	total 27 N-glycosylation sites	1101:1130	total 27 N-glycosylation sites	1101:1130	Seventeen high-abundance serum proteins, mainly acute-phase proteins, and immunoglobulins, with total 27 N-glycosylation sites, and 62 glycoforms, were identified.
24841998	10	13	gly	glycoprotein	1535:1546	arg1	glycoprotein					1535:1546	a specific glycoprotein	1524:1546	a specific glycoprotein	1524:1546	Analysis showed that the changes often concerned one or two, but not all, N-glycosylation sites in a specific glycoprotein.
24841998	4	14	theme	patients	696:703	arg1	sera					641:644	albumin-depleted sera	624:644	albumin-depleted sera of pancreatic cancer patients, acute pancreatitis patients, and healthy individuals	624:728	We used Sambucus nigra lectin affinity chromatography to enrich α-2,6 sialylated tryptic N-glycopeptides from albumin-depleted sera of pancreatic cancer patients, acute pancreatitis patients, and healthy individuals, and compared their relative abundance using ultra performance LC-MS.
24841998	0	15	theme	controls	128:135	arg1	serum					50:54	serum	50:54	serum of pancreatic cancer patients, acute pancreatitis patients, and healthy controls	50:135	Comparison of sialylated N-glycopeptide levels in serum of pancreatic cancer patients, acute pancreatitis patients, and healthy controls.
24841998	2	16	contain	has	383:385	arg1	disease					332:338	the disease	328:338	the disease	328:338	Pancreatic cancer patients would benefit from early diagnosis, as the disease is often detected in an advanced stage and has poor prognosis.
24841998	2	16	contain	has	383:385	arg2	prognosis					392:400	poor prognosis	387:400	poor prognosis	387:400	Pancreatic cancer patients would benefit from early diagnosis, as the disease is often detected in an advanced stage and has poor prognosis.
24841998	11	17	from	changes	1650:1656	arg1	concentrations					1661:1674	concentrations	1661:1674	concentrations of intact sialylated N-glycopeptides derived from acute-phase proteins, and immunoglobulins	1661:1766	In conclusion, the analysis shows that pancreatic cancer, and acute pancreatitis are associated with changes in concentrations of intact sialylated N-glycopeptides derived from acute-phase proteins, and immunoglobulins, and that changes are site specific.
24841998	4	18	gly	sialylated	584:593	arg1	N-glycopeptides					603:617	α-2,6 sialylated tryptic N-glycopeptides	578:617	α-2,6 sialylated tryptic N-glycopeptides from albumin-depleted sera of pancreatic cancer patients, acute pancreatitis patients, and healthy individuals	578:728	We used Sambucus nigra lectin affinity chromatography to enrich α-2,6 sialylated tryptic N-glycopeptides from albumin-depleted sera of pancreatic cancer patients, acute pancreatitis patients, and healthy individuals, and compared their relative abundance using ultra performance LC-MS.
24841998	7	19	with	proteins	1065:1072	arg1	sites					1126:1130	total 27 N-glycosylation sites	1101:1130	total 27 N-glycosylation sites	1101:1130	Seventeen high-abundance serum proteins, mainly acute-phase proteins, and immunoglobulins, with total 27 N-glycosylation sites, and 62 glycoforms, were identified.
24841998	4	20	theme	ultra	775:779	arg1	LC-MS					793:797	ultra performance LC-MS	775:797	ultra performance LC-MS	775:797	We used Sambucus nigra lectin affinity chromatography to enrich α-2,6 sialylated tryptic N-glycopeptides from albumin-depleted sera of pancreatic cancer patients, acute pancreatitis patients, and healthy individuals, and compared their relative abundance using ultra performance LC-MS.
24841998	9	21	theme	tenfold	1341:1347	arg1	changes					1349:1355	up to tenfold changes	1335:1355	up to tenfold changes	1335:1355	In pancreatitis, up to tenfold changes were found in some glycoforms, and in pancreatic cancer, threefold.
24841998	2	22	theme	Pancreatic	262:271	arg1	patients					280:287	Pancreatic cancer patients	262:287	Pancreatic cancer patients	262:287	Pancreatic cancer patients would benefit from early diagnosis, as the disease is often detected in an advanced stage and has poor prognosis.
24841998	0	23	theme	pancreatic	59:68	arg1	patients					77:84	pancreatic cancer patients	59:84	pancreatic cancer patients	59:84	Comparison of sialylated N-glycopeptide levels in serum of pancreatic cancer patients, acute pancreatitis patients, and healthy controls.
24841998	4	24	used	used	517:520	arg2	We					514:515	We	514:515	We	514:515	We used Sambucus nigra lectin affinity chromatography to enrich α-2,6 sialylated tryptic N-glycopeptides from albumin-depleted sera of pancreatic cancer patients, acute pancreatitis patients, and healthy individuals, and compared their relative abundance using ultra performance LC-MS.
24841998	1	25	theme	protein	144:150	arg1	glycosylation					152:164	Serum protein glycosylation	138:164	Serum protein glycosylation	138:164	Serum protein glycosylation is known to be affected by pathological conditions, including cancer and inflammatory diseases.
24841998	0	26	theme	patients	77:84	arg1	serum					50:54	serum	50:54	serum of pancreatic cancer patients, acute pancreatitis patients, and healthy controls	50:135	Comparison of sialylated N-glycopeptide levels in serum of pancreatic cancer patients, acute pancreatitis patients, and healthy controls.
24841998	7	27	theme	acute-phase	1053:1063	arg1	proteins					1065:1072	acute-phase proteins	1053:1072	acute-phase proteins	1053:1072	Seventeen high-abundance serum proteins, mainly acute-phase proteins, and immunoglobulins, with total 27 N-glycosylation sites, and 62 glycoforms, were identified.
24841998	0	28	from	Comparison	0:9	arg1	serum					50:54	serum	50:54	serum of pancreatic cancer patients, acute pancreatitis patients, and healthy controls	50:135	Comparison of sialylated N-glycopeptide levels in serum of pancreatic cancer patients, acute pancreatitis patients, and healthy controls.
24841998	0	29	theme	acute	87:91	arg1	patients					106:113	acute pancreatitis patients	87:113	acute pancreatitis patients	87:113	Comparison of sialylated N-glycopeptide levels in serum of pancreatic cancer patients, acute pancreatitis patients, and healthy controls.
24841998	0	30	from	serum	50:54	arg1	Comparison					0:9	Comparison	0:9	Comparison of sialylated N-glycopeptide levels in serum of pancreatic cancer patients, acute pancreatitis patients, and healthy controls.	0:136	Comparison of sialylated N-glycopeptide levels in serum of pancreatic cancer patients, acute pancreatitis patients, and healthy controls.
24841998	2	31	theme	poor	387:390	arg1	prognosis					392:400	poor prognosis	387:400	poor prognosis	387:400	Pancreatic cancer patients would benefit from early diagnosis, as the disease is often detected in an advanced stage and has poor prognosis.
24841998	5	32	theme	Relative	800:807	arg1	quantitation					809:820	Relative quantitation	800:820	Relative quantitation	800:820	Relative quantitation was done using the spectrum processing software MZmine.
24841998	4	33	gly	N-glycopeptides	603:617	arg2	N-glycopeptides					603:617	α-2,6 sialylated tryptic N-glycopeptides	578:617	α-2,6 sialylated tryptic N-glycopeptides from albumin-depleted sera of pancreatic cancer patients, acute pancreatitis patients, and healthy individuals	578:728	We used Sambucus nigra lectin affinity chromatography to enrich α-2,6 sialylated tryptic N-glycopeptides from albumin-depleted sera of pancreatic cancer patients, acute pancreatitis patients, and healthy individuals, and compared their relative abundance using ultra performance LC-MS.
24841998	4	33	gly	N-glycopeptides	603:617	arg1	sera					641:644	albumin-depleted sera	624:644	albumin-depleted sera of pancreatic cancer patients, acute pancreatitis patients, and healthy individuals	624:728	We used Sambucus nigra lectin affinity chromatography to enrich α-2,6 sialylated tryptic N-glycopeptides from albumin-depleted sera of pancreatic cancer patients, acute pancreatitis patients, and healthy individuals, and compared their relative abundance using ultra performance LC-MS.
24841998	0	34	from	levels	40:45	arg1	serum					50:54	serum	50:54	serum of pancreatic cancer patients, acute pancreatitis patients, and healthy controls	50:135	Comparison of sialylated N-glycopeptide levels in serum of pancreatic cancer patients, acute pancreatitis patients, and healthy controls.
24841998	9	35	theme	pancreatic	1395:1404	arg1	cancer					1406:1411	pancreatic cancer	1395:1411	pancreatic cancer	1395:1411	In pancreatitis, up to tenfold changes were found in some glycoforms, and in pancreatic cancer, threefold.
24841998	3	36	gly	glycoprotein	489:500	arg1	glycoprotein					489:500	novel glycoprotein biomarkers	483:511	novel glycoprotein biomarkers	483:511	Searching for changes in serum protein site-specific glycosylation could reveal novel glycoprotein biomarkers.
24841998	0	37	theme	sialylated	14:23	arg1	levels					40:45	sialylated N-glycopeptide levels	14:45	sialylated N-glycopeptide levels in serum of pancreatic cancer patients, acute pancreatitis patients, and healthy controls	14:135	Comparison of sialylated N-glycopeptide levels in serum of pancreatic cancer patients, acute pancreatitis patients, and healthy controls.
24841998	4	38	theme	sialylated	584:593	arg1	N-glycopeptides					603:617	α-2,6 sialylated tryptic N-glycopeptides	578:617	α-2,6 sialylated tryptic N-glycopeptides from albumin-depleted sera of pancreatic cancer patients, acute pancreatitis patients, and healthy individuals	578:728	We used Sambucus nigra lectin affinity chromatography to enrich α-2,6 sialylated tryptic N-glycopeptides from albumin-depleted sera of pancreatic cancer patients, acute pancreatitis patients, and healthy individuals, and compared their relative abundance using ultra performance LC-MS.
24841998	3	39	theme	site-specific	442:454	arg1	glycosylation					456:468	serum protein site-specific glycosylation	428:468	serum protein site-specific glycosylation	428:468	Searching for changes in serum protein site-specific glycosylation could reveal novel glycoprotein biomarkers.
24841998	5	40	theme	spectrum	841:848	arg1	MZmine					870:875	the spectrum processing software MZmine	837:875	the spectrum processing software MZmine	837:875	Relative quantitation was done using the spectrum processing software MZmine.
24841998	8	41	theme	patient	1182:1188	arg1	sera					1190:1193	Pancreatitis patient sera	1169:1193	Pancreatitis patient sera	1169:1193	Pancreatitis patient sera contained 38, and pancreatic cancer patients sera contained 13 glycoform changes with statistical significance (p < 0.05).
24841998	4	42	theme	affinity	544:551	arg1	chromatography					553:566	Sambucus nigra lectin affinity chromatography	522:566	Sambucus nigra lectin affinity chromatography	522:566	We used Sambucus nigra lectin affinity chromatography to enrich α-2,6 sialylated tryptic N-glycopeptides from albumin-depleted sera of pancreatic cancer patients, acute pancreatitis patients, and healthy individuals, and compared their relative abundance using ultra performance LC-MS.
24841998	5	43	theme	software	861:868	arg1	MZmine					870:875	the spectrum processing software MZmine	837:875	the spectrum processing software MZmine	837:875	Relative quantitation was done using the spectrum processing software MZmine.
24841998	6	44	theme	web-based	914:922	arg1	GlycopeptideID					929:942	the web-based tool GlycopeptideID	910:942	the web-based tool GlycopeptideID	910:942	Identification was performed on the web-based tool GlycopeptideID, developed for in silico analysis of intact N-glycopeptides.
24841998	0	45	gly	N-glycopeptide	25:38	arg2	N-glycopeptide					25:38	sialylated N-glycopeptide levels	14:45	sialylated N-glycopeptide levels in serum of pancreatic cancer patients, acute pancreatitis patients, and healthy controls	14:135	Comparison of sialylated N-glycopeptide levels in serum of pancreatic cancer patients, acute pancreatitis patients, and healthy controls.
24841998	8	46	contain	contained	1195:1203	arg2	38					1205:1206	38	1205:1206	38	1205:1206	Pancreatitis patient sera contained 38, and pancreatic cancer patients sera contained 13 glycoform changes with statistical significance (p < 0.05).
24841998	8	46	contain	contained	1195:1203	arg1	sera					1190:1193	Pancreatitis patient sera	1169:1193	Pancreatitis patient sera	1169:1193	Pancreatitis patient sera contained 38, and pancreatic cancer patients sera contained 13 glycoform changes with statistical significance (p < 0.05).
24841998	10	47	dep	one	1474:1476	arg1	sites					1515:1519	N-glycosylation sites	1499:1519	N-glycosylation sites	1499:1519	Analysis showed that the changes often concerned one or two, but not all, N-glycosylation sites in a specific glycoprotein.
24841998	10	48	gly	N-glycosylation	1499:1513	arg2	sites					1515:1519	N-glycosylation sites	1499:1519	N-glycosylation sites	1499:1519	Analysis showed that the changes often concerned one or two, but not all, N-glycosylation sites in a specific glycoprotein.
24841998	11	49	theme	intact	1679:1684	arg1	N-glycopeptides					1697:1711	intact sialylated N-glycopeptides	1679:1711	intact sialylated N-glycopeptides derived from acute-phase proteins, and immunoglobulins	1679:1766	In conclusion, the analysis shows that pancreatic cancer, and acute pancreatitis are associated with changes in concentrations of intact sialylated N-glycopeptides derived from acute-phase proteins, and immunoglobulins, and that changes are site specific.
24841998	2	50	theme	advanced	364:371	arg1	stage					373:377	an advanced stage	361:377	an advanced stage	361:377	Pancreatic cancer patients would benefit from early diagnosis, as the disease is often detected in an advanced stage and has poor prognosis.
24841998	8	51	theme	pancreatic	1213:1222	arg1	sera					1240:1243	pancreatic cancer patients sera	1213:1243	pancreatic cancer patients sera	1213:1243	Pancreatitis patient sera contained 38, and pancreatic cancer patients sera contained 13 glycoform changes with statistical significance (p < 0.05).
24841998	4	52	theme	lectin	537:542	arg1	chromatography					553:566	Sambucus nigra lectin affinity chromatography	522:566	Sambucus nigra lectin affinity chromatography	522:566	We used Sambucus nigra lectin affinity chromatography to enrich α-2,6 sialylated tryptic N-glycopeptides from albumin-depleted sera of pancreatic cancer patients, acute pancreatitis patients, and healthy individuals, and compared their relative abundance using ultra performance LC-MS.
24841998	11	53	attach	derived	1713:1719	arg1	proteins					1738:1745	acute-phase proteins	1726:1745	acute-phase proteins	1726:1745	In conclusion, the analysis shows that pancreatic cancer, and acute pancreatitis are associated with changes in concentrations of intact sialylated N-glycopeptides derived from acute-phase proteins, and immunoglobulins, and that changes are site specific.
24841998	11	53	attach	derived	1713:1719	arg1	immunoglobulins					1752:1766	immunoglobulins	1752:1766	immunoglobulins	1752:1766	In conclusion, the analysis shows that pancreatic cancer, and acute pancreatitis are associated with changes in concentrations of intact sialylated N-glycopeptides derived from acute-phase proteins, and immunoglobulins, and that changes are site specific.
24841998	11	53	attach	derived	1713:1719	arg2	N-glycopeptides					1697:1711	intact sialylated N-glycopeptides	1679:1711	intact sialylated N-glycopeptides derived from acute-phase proteins, and immunoglobulins	1679:1766	In conclusion, the analysis shows that pancreatic cancer, and acute pancreatitis are associated with changes in concentrations of intact sialylated N-glycopeptides derived from acute-phase proteins, and immunoglobulins, and that changes are site specific.
24841998	8	54	theme	patients	1231:1238	arg1	sera					1240:1243	pancreatic cancer patients sera	1213:1243	pancreatic cancer patients sera	1213:1243	Pancreatitis patient sera contained 38, and pancreatic cancer patients sera contained 13 glycoform changes with statistical significance (p < 0.05).
24841998	6	55	theme	intact	981:986	arg1	N-glycopeptides					988:1002	intact N-glycopeptides	981:1002	intact N-glycopeptides	981:1002	Identification was performed on the web-based tool GlycopeptideID, developed for in silico analysis of intact N-glycopeptides.
24841998	11	56	theme	N-glycopeptides	1697:1711	arg1	concentrations					1661:1674	concentrations	1661:1674	concentrations of intact sialylated N-glycopeptides derived from acute-phase proteins, and immunoglobulins	1661:1766	In conclusion, the analysis shows that pancreatic cancer, and acute pancreatitis are associated with changes in concentrations of intact sialylated N-glycopeptides derived from acute-phase proteins, and immunoglobulins, and that changes are site specific.
24841998	9	57	located	found	1362:1366	arg1	pancreatitis					1321:1332	pancreatitis	1321:1332	pancreatitis	1321:1332	In pancreatitis, up to tenfold changes were found in some glycoforms, and in pancreatic cancer, threefold.
24841998	9	57	located	found	1362:1366	arg2	changes					1349:1355	up to tenfold changes	1335:1355	up to tenfold changes	1335:1355	In pancreatitis, up to tenfold changes were found in some glycoforms, and in pancreatic cancer, threefold.
24841998	9	57	located	found	1362:1366	arg1	glycoforms					1376:1385	some glycoforms	1371:1385	some glycoforms	1371:1385	In pancreatitis, up to tenfold changes were found in some glycoforms, and in pancreatic cancer, threefold.
24841998	4	58	theme	albumin-depleted	624:639	arg1	sera					641:644	albumin-depleted sera	624:644	albumin-depleted sera of pancreatic cancer patients, acute pancreatitis patients, and healthy individuals	624:728	We used Sambucus nigra lectin affinity chromatography to enrich α-2,6 sialylated tryptic N-glycopeptides from albumin-depleted sera of pancreatic cancer patients, acute pancreatitis patients, and healthy individuals, and compared their relative abundance using ultra performance LC-MS.
24841998	8	59	contain	contained	1245:1253	arg2	changes					1268:1274	13 glycoform changes	1255:1274	13 glycoform changes	1255:1274	Pancreatitis patient sera contained 38, and pancreatic cancer patients sera contained 13 glycoform changes with statistical significance (p < 0.05).
24841998	8	59	contain	contained	1245:1253	arg1	sera					1240:1243	pancreatic cancer patients sera	1213:1243	pancreatic cancer patients sera	1213:1243	Pancreatitis patient sera contained 38, and pancreatic cancer patients sera contained 13 glycoform changes with statistical significance (p < 0.05).
24841998	8	60	theme	glycoform	1258:1266	arg1	changes					1268:1274	13 glycoform changes	1255:1274	13 glycoform changes	1255:1274	Pancreatitis patient sera contained 38, and pancreatic cancer patients sera contained 13 glycoform changes with statistical significance (p < 0.05).
24841998	6	61	theme	in	959:960	arg1	analysis					969:976	in silico analysis	959:976	in silico analysis of intact N-glycopeptides	959:1002	Identification was performed on the web-based tool GlycopeptideID, developed for in silico analysis of intact N-glycopeptides.
24841998	4	62	theme	healthy	710:716	arg1	individuals					718:728	healthy individuals	710:728	healthy individuals	710:728	We used Sambucus nigra lectin affinity chromatography to enrich α-2,6 sialylated tryptic N-glycopeptides from albumin-depleted sera of pancreatic cancer patients, acute pancreatitis patients, and healthy individuals, and compared their relative abundance using ultra performance LC-MS.
24841998	0	63	theme	healthy	120:126	arg1	controls					128:135	healthy controls	120:135	healthy controls	120:135	Comparison of sialylated N-glycopeptide levels in serum of pancreatic cancer patients, acute pancreatitis patients, and healthy controls.
24841998	8	64	theme	p	1307:1307	arg1	significance					1293:1304	statistical significance	1281:1304	statistical significance (p < 0.05)	1281:1315	Pancreatitis patient sera contained 38, and pancreatic cancer patients sera contained 13 glycoform changes with statistical significance (p < 0.05).
24841998	8	64	theme	p	1307:1307	arg1	<					1309:1309	p < 0.05	1307:1314	p < 0.05	1307:1314	Pancreatitis patient sera contained 38, and pancreatic cancer patients sera contained 13 glycoform changes with statistical significance (p < 0.05).
24841998	4	65	theme	pancreatitis	683:694	arg1	patients					696:703	acute pancreatitis patients	677:703	acute pancreatitis patients	677:703	We used Sambucus nigra lectin affinity chromatography to enrich α-2,6 sialylated tryptic N-glycopeptides from albumin-depleted sera of pancreatic cancer patients, acute pancreatitis patients, and healthy individuals, and compared their relative abundance using ultra performance LC-MS.
24841998	4	66	from	sera	641:644	arg1	N-glycopeptides					603:617	α-2,6 sialylated tryptic N-glycopeptides	578:617	α-2,6 sialylated tryptic N-glycopeptides from albumin-depleted sera of pancreatic cancer patients, acute pancreatitis patients, and healthy individuals	578:728	We used Sambucus nigra lectin affinity chromatography to enrich α-2,6 sialylated tryptic N-glycopeptides from albumin-depleted sera of pancreatic cancer patients, acute pancreatitis patients, and healthy individuals, and compared their relative abundance using ultra performance LC-MS.
24841998	7	67	theme	N-glycosylation	1110:1124	arg1	sites					1126:1130	total 27 N-glycosylation sites	1101:1130	total 27 N-glycosylation sites	1101:1130	Seventeen high-abundance serum proteins, mainly acute-phase proteins, and immunoglobulins, with total 27 N-glycosylation sites, and 62 glycoforms, were identified.
24841998	4	68	theme	Sambucus	522:529	arg1	chromatography					553:566	Sambucus nigra lectin affinity chromatography	522:566	Sambucus nigra lectin affinity chromatography	522:566	We used Sambucus nigra lectin affinity chromatography to enrich α-2,6 sialylated tryptic N-glycopeptides from albumin-depleted sera of pancreatic cancer patients, acute pancreatitis patients, and healthy individuals, and compared their relative abundance using ultra performance LC-MS.
24841998	4	69	theme	relative	750:757	arg1	abundance					759:767	their relative abundance	744:767	their relative abundance	744:767	We used Sambucus nigra lectin affinity chromatography to enrich α-2,6 sialylated tryptic N-glycopeptides from albumin-depleted sera of pancreatic cancer patients, acute pancreatitis patients, and healthy individuals, and compared their relative abundance using ultra performance LC-MS.
24841998	2	70	theme	cancer	273:278	arg1	patients					280:287	Pancreatic cancer patients	262:287	Pancreatic cancer patients	262:287	Pancreatic cancer patients would benefit from early diagnosis, as the disease is often detected in an advanced stage and has poor prognosis.
24841998	7	71	theme	total	1101:1105	arg1	sites					1126:1130	total 27 N-glycosylation sites	1101:1130	total 27 N-glycosylation sites	1101:1130	Seventeen high-abundance serum proteins, mainly acute-phase proteins, and immunoglobulins, with total 27 N-glycosylation sites, and 62 glycoforms, were identified.
24841998	3	72	theme	novel	483:487	arg1	biomarkers					502:511	novel glycoprotein biomarkers	483:511	novel glycoprotein biomarkers	483:511	Searching for changes in serum protein site-specific glycosylation could reveal novel glycoprotein biomarkers.
24841998	0	73	theme	cancer	70:75	arg1	patients					77:84	pancreatic cancer patients	59:84	pancreatic cancer patients	59:84	Comparison of sialylated N-glycopeptide levels in serum of pancreatic cancer patients, acute pancreatitis patients, and healthy controls.
24841998	1	74	theme	Serum	138:142	arg1	glycosylation					152:164	Serum protein glycosylation	138:164	Serum protein glycosylation	138:164	Serum protein glycosylation is known to be affected by pathological conditions, including cancer and inflammatory diseases.
24841998	7	75	with	immunoglobulins	1079:1093	arg1	sites					1126:1130	total 27 N-glycosylation sites	1101:1130	total 27 N-glycosylation sites	1101:1130	Seventeen high-abundance serum proteins, mainly acute-phase proteins, and immunoglobulins, with total 27 N-glycosylation sites, and 62 glycoforms, were identified.
24841998	4	76	theme	pancreatic	649:658	arg1	patients					667:674	pancreatic cancer patients	649:674	pancreatic cancer patients	649:674	We used Sambucus nigra lectin affinity chromatography to enrich α-2,6 sialylated tryptic N-glycopeptides from albumin-depleted sera of pancreatic cancer patients, acute pancreatitis patients, and healthy individuals, and compared their relative abundance using ultra performance LC-MS.
24841998	6	77	gly	N-glycopeptides	988:1002	arg2	N-glycopeptides					988:1002	intact N-glycopeptides	981:1002	intact N-glycopeptides	981:1002	Identification was performed on the web-based tool GlycopeptideID, developed for in silico analysis of intact N-glycopeptides.
24841998	2	78	located	detected	349:356	arg1	stage					373:377	an advanced stage	361:377	an advanced stage	361:377	Pancreatic cancer patients would benefit from early diagnosis, as the disease is often detected in an advanced stage and has poor prognosis.
24841998	2	78	located	detected	349:356	arg2	disease					332:338	the disease	328:338	the disease	328:338	Pancreatic cancer patients would benefit from early diagnosis, as the disease is often detected in an advanced stage and has poor prognosis.
24841998	0	79	theme	pancreatitis	93:104	arg1	patients					106:113	acute pancreatitis patients	87:113	acute pancreatitis patients	87:113	Comparison of sialylated N-glycopeptide levels in serum of pancreatic cancer patients, acute pancreatitis patients, and healthy controls.
24841998	3	80	theme	protein	434:440	arg1	glycosylation					456:468	serum protein site-specific glycosylation	428:468	serum protein site-specific glycosylation	428:468	Searching for changes in serum protein site-specific glycosylation could reveal novel glycoprotein biomarkers.
24841998	10	81	theme	N-glycosylation	1499:1513	arg1	sites					1515:1519	N-glycosylation sites	1499:1519	N-glycosylation sites	1499:1519	Analysis showed that the changes often concerned one or two, but not all, N-glycosylation sites in a specific glycoprotein.
24841998	4	82	theme	performance	781:791	arg1	LC-MS					793:797	ultra performance LC-MS	775:797	ultra performance LC-MS	775:797	We used Sambucus nigra lectin affinity chromatography to enrich α-2,6 sialylated tryptic N-glycopeptides from albumin-depleted sera of pancreatic cancer patients, acute pancreatitis patients, and healthy individuals, and compared their relative abundance using ultra performance LC-MS.
24841998	0	83	theme	N-glycopeptide	25:38	arg1	levels					40:45	sialylated N-glycopeptide levels	14:45	sialylated N-glycopeptide levels in serum of pancreatic cancer patients, acute pancreatitis patients, and healthy controls	14:135	Comparison of sialylated N-glycopeptide levels in serum of pancreatic cancer patients, acute pancreatitis patients, and healthy controls.
24841998	8	84	theme	Pancreatitis	1169:1180	arg1	sera					1190:1193	Pancreatitis patient sera	1169:1193	Pancreatitis patient sera	1169:1193	Pancreatitis patient sera contained 38, and pancreatic cancer patients sera contained 13 glycoform changes with statistical significance (p < 0.05).
24841998	7	85	theme	high-abundance	1015:1028	arg1	proteins					1036:1043	Seventeen high-abundance serum proteins	1005:1043	Seventeen high-abundance serum proteins	1005:1043	Seventeen high-abundance serum proteins, mainly acute-phase proteins, and immunoglobulins, with total 27 N-glycosylation sites, and 62 glycoforms, were identified.
24841998	7	86	with	glycoforms	1140:1149	arg1	sites					1126:1130	total 27 N-glycosylation sites	1101:1130	total 27 N-glycosylation sites	1101:1130	Seventeen high-abundance serum proteins, mainly acute-phase proteins, and immunoglobulins, with total 27 N-glycosylation sites, and 62 glycoforms, were identified.
24841998	4	87	theme	tryptic	595:601	arg1	N-glycopeptides					603:617	α-2,6 sialylated tryptic N-glycopeptides	578:617	α-2,6 sialylated tryptic N-glycopeptides from albumin-depleted sera of pancreatic cancer patients, acute pancreatitis patients, and healthy individuals	578:728	We used Sambucus nigra lectin affinity chromatography to enrich α-2,6 sialylated tryptic N-glycopeptides from albumin-depleted sera of pancreatic cancer patients, acute pancreatitis patients, and healthy individuals, and compared their relative abundance using ultra performance LC-MS.
24841998	11	88	gly	N-glycopeptides	1697:1711	arg2	N-glycopeptides					1697:1711	intact sialylated N-glycopeptides	1679:1711	intact sialylated N-glycopeptides derived from acute-phase proteins, and immunoglobulins	1679:1766	In conclusion, the analysis shows that pancreatic cancer, and acute pancreatitis are associated with changes in concentrations of intact sialylated N-glycopeptides derived from acute-phase proteins, and immunoglobulins, and that changes are site specific.
24841998	3	89	theme	serum	428:432	arg1	glycosylation					456:468	serum protein site-specific glycosylation	428:468	serum protein site-specific glycosylation	428:468	Searching for changes in serum protein site-specific glycosylation could reveal novel glycoprotein biomarkers.
24841998	7	90	gly	N-glycosylation	1110:1124	arg2	sites					1126:1130	total 27 N-glycosylation sites	1101:1130	total 27 N-glycosylation sites	1101:1130	Seventeen high-abundance serum proteins, mainly acute-phase proteins, and immunoglobulins, with total 27 N-glycosylation sites, and 62 glycoforms, were identified.
24841998	7	90	gly	N-glycosylation	1110:1124	arg2	27					1107:1108	27	1107:1108	27	1107:1108	Seventeen high-abundance serum proteins, mainly acute-phase proteins, and immunoglobulins, with total 27 N-glycosylation sites, and 62 glycoforms, were identified.
24841998	10	91	theme	specific	1526:1533	arg1	glycoprotein					1535:1546	a specific glycoprotein	1524:1546	a specific glycoprotein	1524:1546	Analysis showed that the changes often concerned one or two, but not all, N-glycosylation sites in a specific glycoprotein.
24841998	0	92	theme	patients	106:113	arg1	serum					50:54	serum	50:54	serum of pancreatic cancer patients, acute pancreatitis patients, and healthy controls	50:135	Comparison of sialylated N-glycopeptide levels in serum of pancreatic cancer patients, acute pancreatitis patients, and healthy controls.
24841998	5	93	theme	processing	850:859	arg1	MZmine					870:875	the spectrum processing software MZmine	837:875	the spectrum processing software MZmine	837:875	Relative quantitation was done using the spectrum processing software MZmine.
24841998	4	94	dep	Sambucus	522:529	arg1	nigra					531:535	nigra	531:535	nigra	531:535	We used Sambucus nigra lectin affinity chromatography to enrich α-2,6 sialylated tryptic N-glycopeptides from albumin-depleted sera of pancreatic cancer patients, acute pancreatitis patients, and healthy individuals, and compared their relative abundance using ultra performance LC-MS.
24841998	6	95	theme	tool	924:927	arg1	GlycopeptideID					929:942	the web-based tool GlycopeptideID	910:942	the web-based tool GlycopeptideID	910:942	Identification was performed on the web-based tool GlycopeptideID, developed for in silico analysis of intact N-glycopeptides.
24841998	0	96	gly	sialylated	14:23	arg1	levels					40:45	sialylated N-glycopeptide levels	14:45	sialylated N-glycopeptide levels in serum of pancreatic cancer patients, acute pancreatitis patients, and healthy controls	14:135	Comparison of sialylated N-glycopeptide levels in serum of pancreatic cancer patients, acute pancreatitis patients, and healthy controls.
24841998	7	97	theme	serum	1030:1034	arg1	proteins					1036:1043	Seventeen high-abundance serum proteins	1005:1043	Seventeen high-abundance serum proteins	1005:1043	Seventeen high-abundance serum proteins, mainly acute-phase proteins, and immunoglobulins, with total 27 N-glycosylation sites, and 62 glycoforms, were identified.
24841998	6	98	dep	in	959:960	arg1	silico					962:967	silico	962:967	silico	962:967	Identification was performed on the web-based tool GlycopeptideID, developed for in silico analysis of intact N-glycopeptides.
24841998	3	99	from	changes	417:423	arg1	glycosylation					456:468	serum protein site-specific glycosylation	428:468	serum protein site-specific glycosylation	428:468	Searching for changes in serum protein site-specific glycosylation could reveal novel glycoprotein biomarkers.
24841998	3	100	theme	glycoprotein	489:500	arg1	biomarkers					502:511	novel glycoprotein biomarkers	483:511	novel glycoprotein biomarkers	483:511	Searching for changes in serum protein site-specific glycosylation could reveal novel glycoprotein biomarkers.
24841998	8	101	theme	cancer	1224:1229	arg1	sera					1240:1243	pancreatic cancer patients sera	1213:1243	pancreatic cancer patients sera	1213:1243	Pancreatitis patient sera contained 38, and pancreatic cancer patients sera contained 13 glycoform changes with statistical significance (p < 0.05).
24841998	11	102	gly	sialylated	1686:1695	arg1	N-glycopeptides					1697:1711	intact sialylated N-glycopeptides	1679:1711	intact sialylated N-glycopeptides derived from acute-phase proteins, and immunoglobulins	1679:1766	In conclusion, the analysis shows that pancreatic cancer, and acute pancreatitis are associated with changes in concentrations of intact sialylated N-glycopeptides derived from acute-phase proteins, and immunoglobulins, and that changes are site specific.
24841998	4	103	theme	patients	667:674	arg1	sera					641:644	albumin-depleted sera	624:644	albumin-depleted sera of pancreatic cancer patients, acute pancreatitis patients, and healthy individuals	624:728	We used Sambucus nigra lectin affinity chromatography to enrich α-2,6 sialylated tryptic N-glycopeptides from albumin-depleted sera of pancreatic cancer patients, acute pancreatitis patients, and healthy individuals, and compared their relative abundance using ultra performance LC-MS.
24841998	4	104	theme	cancer	660:665	arg1	patients					667:674	pancreatic cancer patients	649:674	pancreatic cancer patients	649:674	We used Sambucus nigra lectin affinity chromatography to enrich α-2,6 sialylated tryptic N-glycopeptides from albumin-depleted sera of pancreatic cancer patients, acute pancreatitis patients, and healthy individuals, and compared their relative abundance using ultra performance LC-MS.
24841998	1	105	theme	inflammatory	239:250	arg1	diseases					252:259	inflammatory diseases	239:259	inflammatory diseases	239:259	Serum protein glycosylation is known to be affected by pathological conditions, including cancer and inflammatory diseases.
20954982	9	0	from	sites	1283:1287	arg1	glycosylation					1250:1262	Possible glycosylation	1241:1262	Possible glycosylation at Asn51 and Asn78 sites of the prostaglandin H2 d-isomerase	1241:1323	Possible glycosylation at Asn51 and Asn78 sites of the prostaglandin H2 d-isomerase was detected.
20954982	9	1	theme	d-isomerase	1313:1323	arg1	d-isomerase					1313:1323	the prostaglandin H2 d-isomerase	1292:1323	the prostaglandin H2 d-isomerase	1292:1323	Possible glycosylation at Asn51 and Asn78 sites of the prostaglandin H2 d-isomerase was detected.
20954982	9	1	theme	d-isomerase	1313:1323	arg1	sites					1283:1287	Asn51 and Asn78 sites	1267:1287	Asn51 and Asn78 sites of the prostaglandin H2 d-isomerase	1267:1323	Possible glycosylation at Asn51 and Asn78 sites of the prostaglandin H2 d-isomerase was detected.
20954982	5	2	theme	matrix-assisted	650:664	arg1	spectrometry					714:725	matrix-assisted laser desorption/ionization time-of-flight mass spectrometry	650:725	matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS)	650:740	The proteins were then visualized by silver staining and characterized by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS).
20954982	5	2	theme	matrix-assisted	650:664	arg1	MS					738:739	MALDI-TOF MS	728:739	MALDI-TOF MS	728:739	The proteins were then visualized by silver staining and characterized by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS).
20954982	5	3	theme	MALDI-TOF	728:736	arg1	spectrometry					714:725	matrix-assisted laser desorption/ionization time-of-flight mass spectrometry	650:725	matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS)	650:740	The proteins were then visualized by silver staining and characterized by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS).
20954982	5	3	theme	MALDI-TOF	728:736	arg1	MS					738:739	MALDI-TOF MS	728:739	MALDI-TOF MS	728:739	The proteins were then visualized by silver staining and characterized by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS).
20954982	1	4	theme	α-galactosidase	142:156	arg1	activity					160:167	deficient α-galactosidase A activity	132:167	deficient α-galactosidase A activity	132:167	BACKGROUND: Anderson-Fabry disease (AFD) is an X-linked genetic disorder with deficient α-galactosidase A activity.
20954982	11	5	gly	glycosylation	1584:1596	arg1	subjects					1605:1612	AFD subjects	1601:1612	AFD subjects	1601:1612	We postulate that the observed difference in the amount of prostaglandin H2 d-isomerase and its position on two-dimensional gels might be related to different glycosylation in AFD subjects.
20954982	3	6	dep	MATERIAL	366:373	arg1	studied					391:397	studied	391:397	studied 2D electrophoresis images of urine samples collected from AFD patients and healthy subjects	391:489	MATERIAL AND METHODS: We studied 2D electrophoresis images of urine samples collected from AFD patients and healthy subjects.
20954982	6	7	theme	identical	832:840	arg1	proteins					842:849	identical proteins	832:849	identical proteins with molecular weight around 20-40 kDa	832:888	RESULTS: We found out that the urinary spectra of all the Fabry disease samples included identical proteins with molecular weight around 20-40 kDa.
20954982	1	8	theme	A	158:158	arg1	activity					160:167	deficient α-galactosidase A activity	132:167	deficient α-galactosidase A activity	132:167	BACKGROUND: Anderson-Fabry disease (AFD) is an X-linked genetic disorder with deficient α-galactosidase A activity.
20954982	8	9	theme	factor-related	1191:1204	arg1	alpha-1-antitrypsin					1087:1105	alpha-1-antitrypsin	1087:1105	alpha-1-antitrypsin	1087:1105	The abundant proteins were identified by MALDI-TOF MS and included the following: alpha-1-antitrypsin, alpha-1-microglobulin, prostaglandin H2 d-isomerase, complement-c1q tumor necrosis factor-related protein, and Ig kappa chain V-III.
20954982	8	9	theme	factor-related	1191:1204	arg1	protein					1206:1212	complement-c1q tumor necrosis factor-related protein	1161:1212	complement-c1q tumor necrosis factor-related protein	1161:1212	The abundant proteins were identified by MALDI-TOF MS and included the following: alpha-1-antitrypsin, alpha-1-microglobulin, prostaglandin H2 d-isomerase, complement-c1q tumor necrosis factor-related protein, and Ig kappa chain V-III.
20954982	0	10	from	Study	0:4	arg1	disease					45:51	Anderson-Fabry disease	30:51	Anderson-Fabry disease	30:51	Study of urinary proteomes in Anderson-Fabry disease.
20954982	5	11	theme	desorption/ionization	672:692	arg1	spectrometry					714:725	matrix-assisted laser desorption/ionization time-of-flight mass spectrometry	650:725	matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS)	650:740	The proteins were then visualized by silver staining and characterized by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS).
20954982	5	11	theme	desorption/ionization	672:692	arg1	MS					738:739	MALDI-TOF MS	728:739	MALDI-TOF MS	728:739	The proteins were then visualized by silver staining and characterized by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS).
20954982	11	12	theme	AFD	1601:1603	arg1	subjects					1605:1612	AFD subjects	1601:1612	AFD subjects	1601:1612	We postulate that the observed difference in the amount of prostaglandin H2 d-isomerase and its position on two-dimensional gels might be related to different glycosylation in AFD subjects.
20954982	8	13	theme	MALDI-TOF	1046:1054	arg1	MS					1056:1057	MALDI-TOF MS	1046:1057	MALDI-TOF MS	1046:1057	The abundant proteins were identified by MALDI-TOF MS and included the following: alpha-1-antitrypsin, alpha-1-microglobulin, prostaglandin H2 d-isomerase, complement-c1q tumor necrosis factor-related protein, and Ig kappa chain V-III.
20954982	2	14	theme	AFD	283:285	arg1	patients					287:294	AFD patients	283:294	AFD patients	283:294	The main aim of this work was to investigate possible differences in urine proteins between healthy controls and AFD patients and to identify abnormal proteins as potential biomarkers of disease.
20954982	11	15	from	gels	1549:1552	arg1	d-isomerase					1501:1511	prostaglandin H2 d-isomerase	1484:1511	prostaglandin H2 d-isomerase	1484:1511	We postulate that the observed difference in the amount of prostaglandin H2 d-isomerase and its position on two-dimensional gels might be related to different glycosylation in AFD subjects.
20954982	11	15	from	gels	1549:1552	arg1	position					1521:1528	its position	1517:1528	its position on two-dimensional gels	1517:1552	We postulate that the observed difference in the amount of prostaglandin H2 d-isomerase and its position on two-dimensional gels might be related to different glycosylation in AFD subjects.
20954982	11	15	from	gels	1549:1552	arg1	amount					1474:1479	the amount	1470:1479	the amount of prostaglandin H2 d-isomerase and its position on two-dimensional gels	1470:1552	We postulate that the observed difference in the amount of prostaglandin H2 d-isomerase and its position on two-dimensional gels might be related to different glycosylation in AFD subjects.
20954982	5	16	theme	time-of-flight	694:707	arg1	spectrometry					714:725	matrix-assisted laser desorption/ionization time-of-flight mass spectrometry	650:725	matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS)	650:740	The proteins were then visualized by silver staining and characterized by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS).
20954982	5	16	theme	time-of-flight	694:707	arg1	MS					738:739	MALDI-TOF MS	728:739	MALDI-TOF MS	728:739	The proteins were then visualized by silver staining and characterized by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS).
20954982	6	17	theme	samples	815:821	arg1	spectra					782:788	the urinary spectra	770:788	the urinary spectra of all the Fabry disease samples	770:821	RESULTS: We found out that the urinary spectra of all the Fabry disease samples included identical proteins with molecular weight around 20-40 kDa.
20954982	11	18	theme	H2	1498:1499	arg1	d-isomerase					1501:1511	prostaglandin H2 d-isomerase	1484:1511	prostaglandin H2 d-isomerase	1484:1511	We postulate that the observed difference in the amount of prostaglandin H2 d-isomerase and its position on two-dimensional gels might be related to different glycosylation in AFD subjects.
20954982	8	19	dep	identified	1032:1041	arg1	alpha-1-antitrypsin					1087:1105	alpha-1-antitrypsin	1087:1105	alpha-1-antitrypsin	1087:1105	The abundant proteins were identified by MALDI-TOF MS and included the following: alpha-1-antitrypsin, alpha-1-microglobulin, prostaglandin H2 d-isomerase, complement-c1q tumor necrosis factor-related protein, and Ig kappa chain V-III.
20954982	8	19	dep	identified	1032:1041	arg1	d-isomerase					1148:1158	prostaglandin H2 d-isomerase	1131:1158	prostaglandin H2 d-isomerase	1131:1158	The abundant proteins were identified by MALDI-TOF MS and included the following: alpha-1-antitrypsin, alpha-1-microglobulin, prostaglandin H2 d-isomerase, complement-c1q tumor necrosis factor-related protein, and Ig kappa chain V-III.
20954982	8	19	dep	identified	1032:1041	arg1	chain					1228:1232	Ig kappa chain V-III	1219:1238	Ig kappa chain V-III	1219:1238	The abundant proteins were identified by MALDI-TOF MS and included the following: alpha-1-antitrypsin, alpha-1-microglobulin, prostaglandin H2 d-isomerase, complement-c1q tumor necrosis factor-related protein, and Ig kappa chain V-III.
20954982	8	19	dep	identified	1032:1041	arg1	protein					1206:1212	complement-c1q tumor necrosis factor-related protein	1161:1212	complement-c1q tumor necrosis factor-related protein	1161:1212	The abundant proteins were identified by MALDI-TOF MS and included the following: alpha-1-antitrypsin, alpha-1-microglobulin, prostaglandin H2 d-isomerase, complement-c1q tumor necrosis factor-related protein, and Ig kappa chain V-III.
20954982	8	19	dep	identified	1032:1041	arg1	alpha-1-microglobulin					1108:1128	alpha-1-microglobulin	1108:1128	alpha-1-microglobulin	1108:1128	The abundant proteins were identified by MALDI-TOF MS and included the following: alpha-1-antitrypsin, alpha-1-microglobulin, prostaglandin H2 d-isomerase, complement-c1q tumor necrosis factor-related protein, and Ig kappa chain V-III.
20954982	6	20	with	proteins	842:849	arg1	weight					866:871	molecular weight	856:871	molecular weight around 20-40 kDa	856:888	RESULTS: We found out that the urinary spectra of all the Fabry disease samples included identical proteins with molecular weight around 20-40 kDa.
20954982	5	21	theme	silver	613:618	arg1	staining					620:627	silver staining	613:627	silver staining	613:627	The proteins were then visualized by silver staining and characterized by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS).
20954982	1	22	theme	Anderson-Fabry	66:79	arg1	AFD					90:92	AFD	90:92	AFD	90:92	BACKGROUND: Anderson-Fabry disease (AFD) is an X-linked genetic disorder with deficient α-galactosidase A activity.
20954982	1	22	theme	Anderson-Fabry	66:79	arg1	BACKGROUND					54:63	BACKGROUND	54:63	BACKGROUND: Anderson-Fabry disease (AFD) is an X-linked genetic disorder with deficient α-galactosidase A activity.	54:168	BACKGROUND: Anderson-Fabry disease (AFD) is an X-linked genetic disorder with deficient α-galactosidase A activity.
20954982	1	22	theme	Anderson-Fabry	66:79	arg1	disease					81:87	Anderson-Fabry disease	66:87	Anderson-Fabry disease (AFD)	66:93	BACKGROUND: Anderson-Fabry disease (AFD) is an X-linked genetic disorder with deficient α-galactosidase A activity.
20954982	1	22	theme	Anderson-Fabry	66:79	arg1	disorder					118:125	an X-linked genetic disorder	98:125	an X-linked genetic disorder with deficient α-galactosidase A activity	98:167	BACKGROUND: Anderson-Fabry disease (AFD) is an X-linked genetic disorder with deficient α-galactosidase A activity.
20954982	11	23	theme	prostaglandin	1484:1496	arg1	d-isomerase					1501:1511	prostaglandin H2 d-isomerase	1484:1511	prostaglandin H2 d-isomerase	1484:1511	We postulate that the observed difference in the amount of prostaglandin H2 d-isomerase and its position on two-dimensional gels might be related to different glycosylation in AFD subjects.
20954982	11	24	theme	observed	1447:1454	arg1	related					1563:1569	related	1563:1569	related	1563:1569	We postulate that the observed difference in the amount of prostaglandin H2 d-isomerase and its position on two-dimensional gels might be related to different glycosylation in AFD subjects.
20954982	11	24	theme	observed	1447:1454	arg1	difference					1456:1465	the observed difference	1443:1465	the observed difference in the amount of prostaglandin H2 d-isomerase and its position on two-dimensional gels	1443:1552	We postulate that the observed difference in the amount of prostaglandin H2 d-isomerase and its position on two-dimensional gels might be related to different glycosylation in AFD subjects.
20954982	1	25	with	disorder	118:125	arg1	activity					160:167	deficient α-galactosidase A activity	132:167	deficient α-galactosidase A activity	132:167	BACKGROUND: Anderson-Fabry disease (AFD) is an X-linked genetic disorder with deficient α-galactosidase A activity.
20954982	6	26	theme	Fabry	801:805	arg1	samples					815:821	all the Fabry disease samples	793:821	all the Fabry disease samples	793:821	RESULTS: We found out that the urinary spectra of all the Fabry disease samples included identical proteins with molecular weight around 20-40 kDa.
20954982	11	27	from	d-isomerase	1501:1511	arg1	gels					1549:1552	two-dimensional gels	1533:1552	two-dimensional gels	1533:1552	We postulate that the observed difference in the amount of prostaglandin H2 d-isomerase and its position on two-dimensional gels might be related to different glycosylation in AFD subjects.
20954982	3	28	theme	urine	428:432	arg1	samples					434:440	urine samples	428:440	urine samples collected from AFD patients and healthy subjects	428:489	MATERIAL AND METHODS: We studied 2D electrophoresis images of urine samples collected from AFD patients and healthy subjects.
20954982	8	29	theme	Ig	1219:1220	arg1	alpha-1-antitrypsin					1087:1105	alpha-1-antitrypsin	1087:1105	alpha-1-antitrypsin	1087:1105	The abundant proteins were identified by MALDI-TOF MS and included the following: alpha-1-antitrypsin, alpha-1-microglobulin, prostaglandin H2 d-isomerase, complement-c1q tumor necrosis factor-related protein, and Ig kappa chain V-III.
20954982	8	29	theme	Ig	1219:1220	arg1	chain					1228:1232	Ig kappa chain V-III	1219:1238	Ig kappa chain V-III	1219:1238	The abundant proteins were identified by MALDI-TOF MS and included the following: alpha-1-antitrypsin, alpha-1-microglobulin, prostaglandin H2 d-isomerase, complement-c1q tumor necrosis factor-related protein, and Ig kappa chain V-III.
20954982	11	30	from	position	1521:1528	arg1	gels					1549:1552	two-dimensional gels	1533:1552	two-dimensional gels	1533:1552	We postulate that the observed difference in the amount of prostaglandin H2 d-isomerase and its position on two-dimensional gels might be related to different glycosylation in AFD subjects.
20954982	3	31	theme	electrophoresis	402:416	arg1	images					418:423	2D electrophoresis images	399:423	2D electrophoresis images of urine samples collected from AFD patients and healthy subjects	399:489	MATERIAL AND METHODS: We studied 2D electrophoresis images of urine samples collected from AFD patients and healthy subjects.
20954982	9	32	theme	Possible	1241:1248	arg1	glycosylation					1250:1262	Possible glycosylation	1241:1262	Possible glycosylation at Asn51 and Asn78 sites of the prostaglandin H2 d-isomerase	1241:1323	Possible glycosylation at Asn51 and Asn78 sites of the prostaglandin H2 d-isomerase was detected.
20954982	10	33	theme	AFD	1352:1354	arg1	proteomics					1364:1373	AFD urinary proteomics	1352:1373	AFD urinary proteomics	1352:1373	CONCLUSIONS: AFD urinary proteomics revealed increased secretion of several proteins.
20954982	5	34	theme	laser	666:670	arg1	spectrometry					714:725	matrix-assisted laser desorption/ionization time-of-flight mass spectrometry	650:725	matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS)	650:740	The proteins were then visualized by silver staining and characterized by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS).
20954982	5	34	theme	laser	666:670	arg1	MS					738:739	MALDI-TOF MS	728:739	MALDI-TOF MS	728:739	The proteins were then visualized by silver staining and characterized by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS).
20954982	0	35	theme	proteomes	17:25	arg1	Study					0:4	Study	0:4	Study of urinary proteomes in Anderson-Fabry disease	0:51	Study of urinary proteomes in Anderson-Fabry disease.
20954982	6	36	theme	disease	807:813	arg1	samples					815:821	all the Fabry disease samples	793:821	all the Fabry disease samples	793:821	RESULTS: We found out that the urinary spectra of all the Fabry disease samples included identical proteins with molecular weight around 20-40 kDa.
20954982	11	37	from	amount	1474:1479	arg1	gels					1549:1552	two-dimensional gels	1533:1552	two-dimensional gels	1533:1552	We postulate that the observed difference in the amount of prostaglandin H2 d-isomerase and its position on two-dimensional gels might be related to different glycosylation in AFD subjects.
20954982	2	38	from	differences	224:234	arg1	proteins					245:252	urine proteins	239:252	urine proteins	239:252	The main aim of this work was to investigate possible differences in urine proteins between healthy controls and AFD patients and to identify abnormal proteins as potential biomarkers of disease.
20954982	0	39	theme	urinary	9:15	arg1	proteomes					17:25	urinary proteomes	9:25	urinary proteomes	9:25	Study of urinary proteomes in Anderson-Fabry disease.
20954982	2	40	theme	healthy	262:268	arg1	controls					270:277	healthy controls	262:277	healthy controls	262:277	The main aim of this work was to investigate possible differences in urine proteins between healthy controls and AFD patients and to identify abnormal proteins as potential biomarkers of disease.
20954982	2	41	theme	main	174:177	arg1	aim					179:181	The main aim	170:181	The main aim of this work	170:194	The main aim of this work was to investigate possible differences in urine proteins between healthy controls and AFD patients and to identify abnormal proteins as potential biomarkers of disease.
20954982	2	42	theme	potential	333:341	arg1	biomarkers					343:352	potential biomarkers	333:352	potential biomarkers of disease	333:363	The main aim of this work was to investigate possible differences in urine proteins between healthy controls and AFD patients and to identify abnormal proteins as potential biomarkers of disease.
20954982	7	43	theme	AFD	966:968	arg1	samples					970:976	the AFD samples	962:976	the AFD samples	962:976	The concentration of some proteins was more than three times higher in the AFD samples, compared to the controls.
20954982	3	44	theme	AFD	457:459	arg1	patients					461:468	AFD patients	457:468	AFD patients	457:468	MATERIAL AND METHODS: We studied 2D electrophoresis images of urine samples collected from AFD patients and healthy subjects.
20954982	0	45	theme	Anderson-Fabry	30:43	arg1	disease					45:51	Anderson-Fabry disease	30:51	Anderson-Fabry disease	30:51	Study of urinary proteomes in Anderson-Fabry disease.
20954982	9	46	theme	Asn51	1267:1271	arg1	d-isomerase					1313:1323	the prostaglandin H2 d-isomerase	1292:1323	the prostaglandin H2 d-isomerase	1292:1323	Possible glycosylation at Asn51 and Asn78 sites of the prostaglandin H2 d-isomerase was detected.
20954982	9	46	theme	Asn51	1267:1271	arg1	sites					1283:1287	Asn51 and Asn78 sites	1267:1287	Asn51 and Asn78 sites of the prostaglandin H2 d-isomerase	1267:1323	Possible glycosylation at Asn51 and Asn78 sites of the prostaglandin H2 d-isomerase was detected.
20954982	2	47	theme	possible	215:222	arg1	differences					224:234	possible differences	215:234	possible differences in urine proteins between healthy controls and AFD patients	215:294	The main aim of this work was to investigate possible differences in urine proteins between healthy controls and AFD patients and to identify abnormal proteins as potential biomarkers of disease.
20954982	11	48	theme	d-isomerase	1501:1511	arg1	d-isomerase					1501:1511	prostaglandin H2 d-isomerase	1484:1511	prostaglandin H2 d-isomerase	1484:1511	We postulate that the observed difference in the amount of prostaglandin H2 d-isomerase and its position on two-dimensional gels might be related to different glycosylation in AFD subjects.
20954982	11	48	theme	d-isomerase	1501:1511	arg1	position					1521:1528	its position	1517:1528	its position on two-dimensional gels	1517:1552	We postulate that the observed difference in the amount of prostaglandin H2 d-isomerase and its position on two-dimensional gels might be related to different glycosylation in AFD subjects.
20954982	11	48	theme	d-isomerase	1501:1511	arg1	amount					1474:1479	the amount	1470:1479	the amount of prostaglandin H2 d-isomerase and its position on two-dimensional gels	1470:1552	We postulate that the observed difference in the amount of prostaglandin H2 d-isomerase and its position on two-dimensional gels might be related to different glycosylation in AFD subjects.
20954982	3	49	theme	samples	434:440	arg1	images					418:423	2D electrophoresis images	399:423	2D electrophoresis images of urine samples collected from AFD patients and healthy subjects	399:489	MATERIAL AND METHODS: We studied 2D electrophoresis images of urine samples collected from AFD patients and healthy subjects.
20954982	3	50	theme	2D	399:400	arg1	images					418:423	2D electrophoresis images	399:423	2D electrophoresis images of urine samples collected from AFD patients and healthy subjects	399:489	MATERIAL AND METHODS: We studied 2D electrophoresis images of urine samples collected from AFD patients and healthy subjects.
20954982	11	51	theme	position	1521:1528	arg1	d-isomerase					1501:1511	prostaglandin H2 d-isomerase	1484:1511	prostaglandin H2 d-isomerase	1484:1511	We postulate that the observed difference in the amount of prostaglandin H2 d-isomerase and its position on two-dimensional gels might be related to different glycosylation in AFD subjects.
20954982	11	51	theme	position	1521:1528	arg1	position					1521:1528	its position	1517:1528	its position on two-dimensional gels	1517:1552	We postulate that the observed difference in the amount of prostaglandin H2 d-isomerase and its position on two-dimensional gels might be related to different glycosylation in AFD subjects.
20954982	11	51	theme	position	1521:1528	arg1	amount					1474:1479	the amount	1470:1479	the amount of prostaglandin H2 d-isomerase and its position on two-dimensional gels	1470:1552	We postulate that the observed difference in the amount of prostaglandin H2 d-isomerase and its position on two-dimensional gels might be related to different glycosylation in AFD subjects.
20954982	8	52	theme	abundant	1009:1016	arg1	proteins					1018:1025	The abundant proteins	1005:1025	The abundant proteins	1005:1025	The abundant proteins were identified by MALDI-TOF MS and included the following: alpha-1-antitrypsin, alpha-1-microglobulin, prostaglandin H2 d-isomerase, complement-c1q tumor necrosis factor-related protein, and Ig kappa chain V-III.
20954982	10	53	theme	increased	1384:1392	arg1	secretion					1394:1402	increased secretion	1384:1402	increased secretion of several proteins	1384:1422	CONCLUSIONS: AFD urinary proteomics revealed increased secretion of several proteins.
20954982	9	54	gly	glycosylation	1250:1262	arg2	d-isomerase					1313:1323	the prostaglandin H2 d-isomerase	1292:1323	the prostaglandin H2 d-isomerase	1292:1323	Possible glycosylation at Asn51 and Asn78 sites of the prostaglandin H2 d-isomerase was detected.
20954982	9	54	gly	glycosylation	1250:1262	arg2	sites					1283:1287	Asn51 and Asn78 sites	1267:1287	Asn51 and Asn78 sites of the prostaglandin H2 d-isomerase	1267:1323	Possible glycosylation at Asn51 and Asn78 sites of the prostaglandin H2 d-isomerase was detected.
20954982	9	54	gly	glycosylation	1250:1262	arg1	sites					1283:1287	Asn51 and Asn78 sites	1267:1287	Asn51 and Asn78 sites of the prostaglandin H2 d-isomerase	1267:1323	Possible glycosylation at Asn51 and Asn78 sites of the prostaglandin H2 d-isomerase was detected.
20954982	9	54	gly	glycosylation	1250:1262	arg1	d-isomerase					1313:1323	the prostaglandin H2 d-isomerase	1292:1323	the prostaglandin H2 d-isomerase	1292:1323	Possible glycosylation at Asn51 and Asn78 sites of the prostaglandin H2 d-isomerase was detected.
20954982	5	55	theme	mass	709:712	arg1	spectrometry					714:725	matrix-assisted laser desorption/ionization time-of-flight mass spectrometry	650:725	matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS)	650:740	The proteins were then visualized by silver staining and characterized by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS).
20954982	5	55	theme	mass	709:712	arg1	MS					738:739	MALDI-TOF MS	728:739	MALDI-TOF MS	728:739	The proteins were then visualized by silver staining and characterized by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS).
20954982	9	56	theme	Asn78	1277:1281	arg1	d-isomerase					1313:1323	the prostaglandin H2 d-isomerase	1292:1323	the prostaglandin H2 d-isomerase	1292:1323	Possible glycosylation at Asn51 and Asn78 sites of the prostaglandin H2 d-isomerase was detected.
20954982	9	56	theme	Asn78	1277:1281	arg1	sites					1283:1287	Asn51 and Asn78 sites	1267:1287	Asn51 and Asn78 sites of the prostaglandin H2 d-isomerase	1267:1323	Possible glycosylation at Asn51 and Asn78 sites of the prostaglandin H2 d-isomerase was detected.
20954982	6	57	theme	urinary	774:780	arg1	spectra					782:788	the urinary spectra	770:788	the urinary spectra of all the Fabry disease samples	770:821	RESULTS: We found out that the urinary spectra of all the Fabry disease samples included identical proteins with molecular weight around 20-40 kDa.
20954982	3	58	theme	healthy	474:480	arg1	subjects					482:489	healthy subjects	474:489	healthy subjects	474:489	MATERIAL AND METHODS: We studied 2D electrophoresis images of urine samples collected from AFD patients and healthy subjects.
20954982	10	59	theme	urinary	1356:1362	arg1	proteomics					1364:1373	AFD urinary proteomics	1352:1373	AFD urinary proteomics	1352:1373	CONCLUSIONS: AFD urinary proteomics revealed increased secretion of several proteins.
20954982	4	60	theme	focusing	538:545	arg1	method					547:552	isoelectric focusing method	526:552	isoelectric focusing method followed by SDS-PAGE	526:573	The proteins were separated using isoelectric focusing method followed by SDS-PAGE.
20954982	2	61	theme	work	191:194	arg1	aim					179:181	The main aim	170:181	The main aim of this work	170:194	The main aim of this work was to investigate possible differences in urine proteins between healthy controls and AFD patients and to identify abnormal proteins as potential biomarkers of disease.
20954982	1	62	theme	X-linked	101:108	arg1	BACKGROUND					54:63	BACKGROUND	54:63	BACKGROUND: Anderson-Fabry disease (AFD) is an X-linked genetic disorder with deficient α-galactosidase A activity.	54:168	BACKGROUND: Anderson-Fabry disease (AFD) is an X-linked genetic disorder with deficient α-galactosidase A activity.
20954982	1	62	theme	X-linked	101:108	arg1	disorder					118:125	an X-linked genetic disorder	98:125	an X-linked genetic disorder with deficient α-galactosidase A activity	98:167	BACKGROUND: Anderson-Fabry disease (AFD) is an X-linked genetic disorder with deficient α-galactosidase A activity.
20954982	1	62	theme	X-linked	101:108	arg1	disease					81:87	Anderson-Fabry disease	66:87	Anderson-Fabry disease (AFD)	66:93	BACKGROUND: Anderson-Fabry disease (AFD) is an X-linked genetic disorder with deficient α-galactosidase A activity.
20954982	11	63	theme	two-dimensional	1533:1547	arg1	gels					1549:1552	two-dimensional gels	1533:1552	two-dimensional gels	1533:1552	We postulate that the observed difference in the amount of prostaglandin H2 d-isomerase and its position on two-dimensional gels might be related to different glycosylation in AFD subjects.
20954982	4	64	theme	isoelectric	526:536	arg1	method					547:552	isoelectric focusing method	526:552	isoelectric focusing method followed by SDS-PAGE	526:573	The proteins were separated using isoelectric focusing method followed by SDS-PAGE.
20954982	8	65	theme	H2	1145:1146	arg1	alpha-1-antitrypsin					1087:1105	alpha-1-antitrypsin	1087:1105	alpha-1-antitrypsin	1087:1105	The abundant proteins were identified by MALDI-TOF MS and included the following: alpha-1-antitrypsin, alpha-1-microglobulin, prostaglandin H2 d-isomerase, complement-c1q tumor necrosis factor-related protein, and Ig kappa chain V-III.
20954982	8	65	theme	H2	1145:1146	arg1	d-isomerase					1148:1158	prostaglandin H2 d-isomerase	1131:1158	prostaglandin H2 d-isomerase	1131:1158	The abundant proteins were identified by MALDI-TOF MS and included the following: alpha-1-antitrypsin, alpha-1-microglobulin, prostaglandin H2 d-isomerase, complement-c1q tumor necrosis factor-related protein, and Ig kappa chain V-III.
20954982	6	66	theme	molecular	856:864	arg1	weight					866:871	molecular weight	856:871	molecular weight around 20-40 kDa	856:888	RESULTS: We found out that the urinary spectra of all the Fabry disease samples included identical proteins with molecular weight around 20-40 kDa.
20954982	11	67	theme	different	1574:1582	arg1	glycosylation					1584:1596	different glycosylation	1574:1596	different glycosylation in AFD subjects	1574:1612	We postulate that the observed difference in the amount of prostaglandin H2 d-isomerase and its position on two-dimensional gels might be related to different glycosylation in AFD subjects.
20954982	8	68	theme	prostaglandin	1131:1143	arg1	alpha-1-antitrypsin					1087:1105	alpha-1-antitrypsin	1087:1105	alpha-1-antitrypsin	1087:1105	The abundant proteins were identified by MALDI-TOF MS and included the following: alpha-1-antitrypsin, alpha-1-microglobulin, prostaglandin H2 d-isomerase, complement-c1q tumor necrosis factor-related protein, and Ig kappa chain V-III.
20954982	8	68	theme	prostaglandin	1131:1143	arg1	d-isomerase					1148:1158	prostaglandin H2 d-isomerase	1131:1158	prostaglandin H2 d-isomerase	1131:1158	The abundant proteins were identified by MALDI-TOF MS and included the following: alpha-1-antitrypsin, alpha-1-microglobulin, prostaglandin H2 d-isomerase, complement-c1q tumor necrosis factor-related protein, and Ig kappa chain V-III.
20954982	1	69	theme	genetic	110:116	arg1	BACKGROUND					54:63	BACKGROUND	54:63	BACKGROUND: Anderson-Fabry disease (AFD) is an X-linked genetic disorder with deficient α-galactosidase A activity.	54:168	BACKGROUND: Anderson-Fabry disease (AFD) is an X-linked genetic disorder with deficient α-galactosidase A activity.
20954982	1	69	theme	genetic	110:116	arg1	disorder					118:125	an X-linked genetic disorder	98:125	an X-linked genetic disorder with deficient α-galactosidase A activity	98:167	BACKGROUND: Anderson-Fabry disease (AFD) is an X-linked genetic disorder with deficient α-galactosidase A activity.
20954982	1	69	theme	genetic	110:116	arg1	disease					81:87	Anderson-Fabry disease	66:87	Anderson-Fabry disease (AFD)	66:93	BACKGROUND: Anderson-Fabry disease (AFD) is an X-linked genetic disorder with deficient α-galactosidase A activity.
20954982	1	70	link	X-linked	101:108	arg1	BACKGROUND					54:63	BACKGROUND	54:63	BACKGROUND: Anderson-Fabry disease (AFD) is an X-linked genetic disorder with deficient α-galactosidase A activity.	54:168	BACKGROUND: Anderson-Fabry disease (AFD) is an X-linked genetic disorder with deficient α-galactosidase A activity.
20954982	1	70	link	X-linked	101:108	arg1	disorder					118:125	an X-linked genetic disorder	98:125	an X-linked genetic disorder with deficient α-galactosidase A activity	98:167	BACKGROUND: Anderson-Fabry disease (AFD) is an X-linked genetic disorder with deficient α-galactosidase A activity.
20954982	1	70	link	X-linked	101:108	arg1	disease					81:87	Anderson-Fabry disease	66:87	Anderson-Fabry disease (AFD)	66:93	BACKGROUND: Anderson-Fabry disease (AFD) is an X-linked genetic disorder with deficient α-galactosidase A activity.
20954982	11	71	from	difference	1456:1465	arg1	d-isomerase					1501:1511	prostaglandin H2 d-isomerase	1484:1511	prostaglandin H2 d-isomerase	1484:1511	We postulate that the observed difference in the amount of prostaglandin H2 d-isomerase and its position on two-dimensional gels might be related to different glycosylation in AFD subjects.
20954982	11	71	from	difference	1456:1465	arg1	position					1521:1528	its position	1517:1528	its position on two-dimensional gels	1517:1552	We postulate that the observed difference in the amount of prostaglandin H2 d-isomerase and its position on two-dimensional gels might be related to different glycosylation in AFD subjects.
20954982	11	71	from	difference	1456:1465	arg1	amount					1474:1479	the amount	1470:1479	the amount of prostaglandin H2 d-isomerase and its position on two-dimensional gels	1470:1552	We postulate that the observed difference in the amount of prostaglandin H2 d-isomerase and its position on two-dimensional gels might be related to different glycosylation in AFD subjects.
20954982	2	72	theme	urine	239:243	arg1	proteins					245:252	urine proteins	239:252	urine proteins	239:252	The main aim of this work was to investigate possible differences in urine proteins between healthy controls and AFD patients and to identify abnormal proteins as potential biomarkers of disease.
20954982	10	73	theme	proteins	1415:1422	arg1	secretion					1394:1402	increased secretion	1384:1402	increased secretion of several proteins	1384:1422	CONCLUSIONS: AFD urinary proteomics revealed increased secretion of several proteins.
20954982	11	74	from	glycosylation	1584:1596	arg1	subjects					1605:1612	AFD subjects	1601:1612	AFD subjects	1601:1612	We postulate that the observed difference in the amount of prostaglandin H2 d-isomerase and its position on two-dimensional gels might be related to different glycosylation in AFD subjects.
20954982	7	75	theme	proteins	917:924	arg1	higher					952:957	higher	952:957	higher	952:957	The concentration of some proteins was more than three times higher in the AFD samples, compared to the controls.
20954982	7	75	theme	proteins	917:924	arg1	concentration					895:907	The concentration	891:907	The concentration of some proteins	891:924	The concentration of some proteins was more than three times higher in the AFD samples, compared to the controls.
20954982	2	76	theme	abnormal	312:319	arg1	proteins					321:328	abnormal proteins	312:328	abnormal proteins as potential biomarkers of disease	312:363	The main aim of this work was to investigate possible differences in urine proteins between healthy controls and AFD patients and to identify abnormal proteins as potential biomarkers of disease.
20954982	9	77	theme	prostaglandin	1296:1308	arg1	d-isomerase					1313:1323	the prostaglandin H2 d-isomerase	1292:1323	the prostaglandin H2 d-isomerase	1292:1323	Possible glycosylation at Asn51 and Asn78 sites of the prostaglandin H2 d-isomerase was detected.
20954982	10	78	theme	several	1407:1413	arg1	proteins					1415:1422	several proteins	1407:1422	several proteins	1407:1422	CONCLUSIONS: AFD urinary proteomics revealed increased secretion of several proteins.
20954982	2	79	theme	disease	357:363	arg1	biomarkers					343:352	potential biomarkers	333:352	potential biomarkers of disease	333:363	The main aim of this work was to investigate possible differences in urine proteins between healthy controls and AFD patients and to identify abnormal proteins as potential biomarkers of disease.
20954982	6	80	dep	found	755:759	arg1	out					761:763	out	761:763	out	761:763	RESULTS: We found out that the urinary spectra of all the Fabry disease samples included identical proteins with molecular weight around 20-40 kDa.
20954982	9	81	theme	H2	1310:1311	arg1	d-isomerase					1313:1323	the prostaglandin H2 d-isomerase	1292:1323	the prostaglandin H2 d-isomerase	1292:1323	Possible glycosylation at Asn51 and Asn78 sites of the prostaglandin H2 d-isomerase was detected.
20954982	8	82	theme	kappa	1222:1226	arg1	alpha-1-antitrypsin					1087:1105	alpha-1-antitrypsin	1087:1105	alpha-1-antitrypsin	1087:1105	The abundant proteins were identified by MALDI-TOF MS and included the following: alpha-1-antitrypsin, alpha-1-microglobulin, prostaglandin H2 d-isomerase, complement-c1q tumor necrosis factor-related protein, and Ig kappa chain V-III.
20954982	8	82	theme	kappa	1222:1226	arg1	chain					1228:1232	Ig kappa chain V-III	1219:1238	Ig kappa chain V-III	1219:1238	The abundant proteins were identified by MALDI-TOF MS and included the following: alpha-1-antitrypsin, alpha-1-microglobulin, prostaglandin H2 d-isomerase, complement-c1q tumor necrosis factor-related protein, and Ig kappa chain V-III.
20954982	1	83	theme	deficient	132:140	arg1	activity					160:167	deficient α-galactosidase A activity	132:167	deficient α-galactosidase A activity	132:167	BACKGROUND: Anderson-Fabry disease (AFD) is an X-linked genetic disorder with deficient α-galactosidase A activity.
14680951	0	0	theme	affinity	71:78	arg1	purification					80:91	dye affinity purification	67:91	dye affinity purification	67:91	Human pituitary glutaminyl cyclase: expression in insect cells and dye affinity purification.
14680951	1	1	theme	culture	335:341	arg1	media					343:347	the culture media	331:347	the culture media	331:347	Human pituitary glutaminyl cyclase (hQC) was expressed in Drosophila S2 cells under the control of an inducible metallothionene promoter and fused to the Drosophila immunoglobulin-binding protein signal sequence to enable secretion into the culture media.
14680951	3	2	theme	affinity	500:507	arg1	chromatography					509:522	affinity chromatography	500:522	affinity chromatography on Reactive Blue 4-agarose using a step pH elution	500:573	The enzyme was purified to homogeneity directly from culture media by affinity chromatography on Reactive Blue 4-agarose using a step pH elution.
14680951	0	3	theme	dye	67:69	arg1	purification					80:91	dye affinity purification	67:91	dye affinity purification	67:91	Human pituitary glutaminyl cyclase: expression in insect cells and dye affinity purification.
14680951	6	4	gly	deglycosylation	996:1010	arg1	enzyme					1029:1034	the expressed enzyme	1015:1034	the expressed enzyme	1015:1034	The two cysteines were disulfide bonded, and the lone predicted glycosylation site, asparagine 49, was shown by both enzymatic deglycosylation of the expressed enzyme and site-directed mutagenesis to be glycosylated.
14680951	6	5	theme	enzymatic	986:994	arg1	deglycosylation					996:1010	enzymatic deglycosylation	986:1010	enzymatic deglycosylation of the expressed enzyme	986:1034	The two cysteines were disulfide bonded, and the lone predicted glycosylation site, asparagine 49, was shown by both enzymatic deglycosylation of the expressed enzyme and site-directed mutagenesis to be glycosylated.
14680951	2	6	theme	Expression	350:359	arg1	levels					361:366	Expression levels	350:366	Expression levels	350:366	Expression levels reached 50 microg/mL culture media after 7 days of induction.
14680951	5	7	theme	37	725:726	arg1	kDa					728:730	kDa	728:730	kDa	728:730	Glutaminyl cyclase was expressed as a fully active 37 kDa enzyme with kcat/Km values of 14.3, 9.3, and 2.4 mM(-1)s(-1) for the substrates Gln-Gln, Gln-NH(2), and Gln-t-butyl ester, respectively.
14680951	3	8	from	chromatography	509:522	arg1	4-agarose					541:549	Reactive Blue 4-agarose	527:549	Reactive Blue 4-agarose using a step pH elution	527:573	The enzyme was purified to homogeneity directly from culture media by affinity chromatography on Reactive Blue 4-agarose using a step pH elution.
14680951	3	9	theme	pH	564:565	arg1	elution					567:573	a step pH elution	557:573	a step pH elution	557:573	The enzyme was purified to homogeneity directly from culture media by affinity chromatography on Reactive Blue 4-agarose using a step pH elution.
14680951	5	10	theme	kDa	728:730	arg1	enzyme					732:737	a fully active 37 kDa enzyme	710:737	a fully active 37 kDa enzyme with kcat/Km values of 14.3, 9.3, and 2.4 mM(-1)s(-1) for the substrates Gln-Gln, Gln-NH(2), and Gln-t-butyl ester, respectively	710:866	Glutaminyl cyclase was expressed as a fully active 37 kDa enzyme with kcat/Km values of 14.3, 9.3, and 2.4 mM(-1)s(-1) for the substrates Gln-Gln, Gln-NH(2), and Gln-t-butyl ester, respectively.
14680951	5	10	theme	kDa	728:730	arg1	cyclase					685:691	Glutaminyl cyclase	674:691	Glutaminyl cyclase	674:691	Glutaminyl cyclase was expressed as a fully active 37 kDa enzyme with kcat/Km values of 14.3, 9.3, and 2.4 mM(-1)s(-1) for the substrates Gln-Gln, Gln-NH(2), and Gln-t-butyl ester, respectively.
14680951	1	11	theme	Drosophila	248:257	arg1	sequence					297:304	the Drosophila immunoglobulin-binding protein signal sequence	244:304	the Drosophila immunoglobulin-binding protein signal sequence to enable secretion into the culture media	244:347	Human pituitary glutaminyl cyclase (hQC) was expressed in Drosophila S2 cells under the control of an inducible metallothionene promoter and fused to the Drosophila immunoglobulin-binding protein signal sequence to enable secretion into the culture media.
14680951	6	12	theme	enzyme	1029:1034	arg1	mutagenesis					1054:1064	site-directed mutagenesis	1040:1064	site-directed mutagenesis	1040:1064	The two cysteines were disulfide bonded, and the lone predicted glycosylation site, asparagine 49, was shown by both enzymatic deglycosylation of the expressed enzyme and site-directed mutagenesis to be glycosylated.
14680951	6	12	theme	enzyme	1029:1034	arg1	deglycosylation					996:1010	enzymatic deglycosylation	986:1010	enzymatic deglycosylation of the expressed enzyme	986:1034	The two cysteines were disulfide bonded, and the lone predicted glycosylation site, asparagine 49, was shown by both enzymatic deglycosylation of the expressed enzyme and site-directed mutagenesis to be glycosylated.
14680951	3	13	theme	Blue	536:539	arg1	4-agarose					541:549	Reactive Blue 4-agarose	527:549	Reactive Blue 4-agarose using a step pH elution	527:573	The enzyme was purified to homogeneity directly from culture media by affinity chromatography on Reactive Blue 4-agarose using a step pH elution.
14680951	1	14	theme	Drosophila	152:161	arg1	cells					166:170	Drosophila S2 cells	152:170	Drosophila S2 cells	152:170	Human pituitary glutaminyl cyclase (hQC) was expressed in Drosophila S2 cells under the control of an inducible metallothionene promoter and fused to the Drosophila immunoglobulin-binding protein signal sequence to enable secretion into the culture media.
14680951	6	15	theme	glycosylation	933:945	arg1	asparagine					953:962	asparagine 49	953:965	asparagine 49	953:965	The two cysteines were disulfide bonded, and the lone predicted glycosylation site, asparagine 49, was shown by both enzymatic deglycosylation of the expressed enzyme and site-directed mutagenesis to be glycosylated.
14680951	6	15	theme	glycosylation	933:945	arg1	site					947:950	the lone predicted glycosylation site	914:950	the lone predicted glycosylation site	914:950	The two cysteines were disulfide bonded, and the lone predicted glycosylation site, asparagine 49, was shown by both enzymatic deglycosylation of the expressed enzyme and site-directed mutagenesis to be glycosylated.
14680951	0	16	from	expression	36:45	arg1	cells					57:61	insect cells	50:61	insect cells	50:61	Human pituitary glutaminyl cyclase: expression in insect cells and dye affinity purification.
14680951	4	17	theme	expressed	596:604	arg1	protein					606:612	the expressed protein	592:612	the expressed protein	592:612	The identity of the expressed protein was confirmed by peptide mass mapping and Western blotting.
14680951	1	18	theme	S2	163:164	arg1	cells					166:170	Drosophila S2 cells	152:170	Drosophila S2 cells	152:170	Human pituitary glutaminyl cyclase (hQC) was expressed in Drosophila S2 cells under the control of an inducible metallothionene promoter and fused to the Drosophila immunoglobulin-binding protein signal sequence to enable secretion into the culture media.
14680951	0	19	theme	pituitary	6:14	arg1	cyclase					27:33	Human pituitary glutaminyl cyclase	0:33	Human pituitary glutaminyl cyclase: expression in insect cells and dye affinity purification.	0:92	Human pituitary glutaminyl cyclase: expression in insect cells and dye affinity purification.
14680951	5	20	theme	Gln-t-butyl	836:846	arg1	ester					848:852	Gln-t-butyl ester	836:852	Gln-t-butyl ester	836:852	Glutaminyl cyclase was expressed as a fully active 37 kDa enzyme with kcat/Km values of 14.3, 9.3, and 2.4 mM(-1)s(-1) for the substrates Gln-Gln, Gln-NH(2), and Gln-t-butyl ester, respectively.
14680951	5	20	theme	Gln-t-butyl	836:846	arg1	substrates					801:810	the substrates Gln-Gln, Gln-NH(2), and Gln-t-butyl ester	797:852	the substrates Gln-Gln, Gln-NH(2), and Gln-t-butyl ester	797:852	Glutaminyl cyclase was expressed as a fully active 37 kDa enzyme with kcat/Km values of 14.3, 9.3, and 2.4 mM(-1)s(-1) for the substrates Gln-Gln, Gln-NH(2), and Gln-t-butyl ester, respectively.
14680951	6	21	theme	predicted	923:931	arg1	asparagine					953:962	asparagine 49	953:965	asparagine 49	953:965	The two cysteines were disulfide bonded, and the lone predicted glycosylation site, asparagine 49, was shown by both enzymatic deglycosylation of the expressed enzyme and site-directed mutagenesis to be glycosylated.
14680951	6	21	theme	predicted	923:931	arg1	site					947:950	the lone predicted glycosylation site	914:950	the lone predicted glycosylation site	914:950	The two cysteines were disulfide bonded, and the lone predicted glycosylation site, asparagine 49, was shown by both enzymatic deglycosylation of the expressed enzyme and site-directed mutagenesis to be glycosylated.
14680951	2	22	theme	culture	389:395	arg1	media					397:401	50 microg/mL culture media	376:401	50 microg/mL culture media	376:401	Expression levels reached 50 microg/mL culture media after 7 days of induction.
14680951	0	23	theme	Human	0:4	arg1	cyclase					27:33	Human pituitary glutaminyl cyclase	0:33	Human pituitary glutaminyl cyclase: expression in insect cells and dye affinity purification.	0:92	Human pituitary glutaminyl cyclase: expression in insect cells and dye affinity purification.
14680951	1	24	theme	immunoglobulin-binding	259:280	arg1	sequence					297:304	the Drosophila immunoglobulin-binding protein signal sequence	244:304	the Drosophila immunoglobulin-binding protein signal sequence to enable secretion into the culture media	244:347	Human pituitary glutaminyl cyclase (hQC) was expressed in Drosophila S2 cells under the control of an inducible metallothionene promoter and fused to the Drosophila immunoglobulin-binding protein signal sequence to enable secretion into the culture media.
14680951	5	25	theme	mM	781:782	arg1	-1					789:790	-1	789:790	-1	789:790	Glutaminyl cyclase was expressed as a fully active 37 kDa enzyme with kcat/Km values of 14.3, 9.3, and 2.4 mM(-1)s(-1) for the substrates Gln-Gln, Gln-NH(2), and Gln-t-butyl ester, respectively.
14680951	5	25	theme	mM	781:782	arg1	s					787:787	14.3, 9.3, and 2.4 mM(-1)s	762:787	14.3, 9.3, and 2.4 mM(-1)s(-1) for the substrates Gln-Gln, Gln-NH(2), and Gln-t-butyl ester	762:852	Glutaminyl cyclase was expressed as a fully active 37 kDa enzyme with kcat/Km values of 14.3, 9.3, and 2.4 mM(-1)s(-1) for the substrates Gln-Gln, Gln-NH(2), and Gln-t-butyl ester, respectively.
14680951	2	26	theme	microg/mL	379:387	arg1	media					397:401	50 microg/mL culture media	376:401	50 microg/mL culture media	376:401	Expression levels reached 50 microg/mL culture media after 7 days of induction.
14680951	1	27	theme	protein	282:288	arg1	sequence					297:304	the Drosophila immunoglobulin-binding protein signal sequence	244:304	the Drosophila immunoglobulin-binding protein signal sequence to enable secretion into the culture media	244:347	Human pituitary glutaminyl cyclase (hQC) was expressed in Drosophila S2 cells under the control of an inducible metallothionene promoter and fused to the Drosophila immunoglobulin-binding protein signal sequence to enable secretion into the culture media.
14680951	1	28	theme	Human	94:98	arg1	hQC					130:132	hQC	130:132	hQC	130:132	Human pituitary glutaminyl cyclase (hQC) was expressed in Drosophila S2 cells under the control of an inducible metallothionene promoter and fused to the Drosophila immunoglobulin-binding protein signal sequence to enable secretion into the culture media.
14680951	1	28	theme	Human	94:98	arg1	cyclase					121:127	Human pituitary glutaminyl cyclase	94:127	Human pituitary glutaminyl cyclase (hQC)	94:133	Human pituitary glutaminyl cyclase (hQC) was expressed in Drosophila S2 cells under the control of an inducible metallothionene promoter and fused to the Drosophila immunoglobulin-binding protein signal sequence to enable secretion into the culture media.
14680951	2	29	theme	induction	419:427	arg1	days					411:414	7 days	409:414	7 days of induction	409:427	Expression levels reached 50 microg/mL culture media after 7 days of induction.
14680951	0	30	theme	glutaminyl	16:25	arg1	cyclase					27:33	Human pituitary glutaminyl cyclase	0:33	Human pituitary glutaminyl cyclase: expression in insect cells and dye affinity purification.	0:92	Human pituitary glutaminyl cyclase: expression in insect cells and dye affinity purification.
14680951	1	31	theme	signal	290:295	arg1	sequence					297:304	the Drosophila immunoglobulin-binding protein signal sequence	244:304	the Drosophila immunoglobulin-binding protein signal sequence to enable secretion into the culture media	244:347	Human pituitary glutaminyl cyclase (hQC) was expressed in Drosophila S2 cells under the control of an inducible metallothionene promoter and fused to the Drosophila immunoglobulin-binding protein signal sequence to enable secretion into the culture media.
14680951	4	32	theme	protein	606:612	arg1	identity					580:587	The identity	576:587	The identity of the expressed protein	576:612	The identity of the expressed protein was confirmed by peptide mass mapping and Western blotting.
14680951	1	33	theme	pituitary	100:108	arg1	hQC					130:132	hQC	130:132	hQC	130:132	Human pituitary glutaminyl cyclase (hQC) was expressed in Drosophila S2 cells under the control of an inducible metallothionene promoter and fused to the Drosophila immunoglobulin-binding protein signal sequence to enable secretion into the culture media.
14680951	1	33	theme	pituitary	100:108	arg1	cyclase					121:127	Human pituitary glutaminyl cyclase	94:127	Human pituitary glutaminyl cyclase (hQC)	94:133	Human pituitary glutaminyl cyclase (hQC) was expressed in Drosophila S2 cells under the control of an inducible metallothionene promoter and fused to the Drosophila immunoglobulin-binding protein signal sequence to enable secretion into the culture media.
14680951	5	34	theme	s	787:787	arg1	values					752:757	kcat/Km values	744:757	kcat/Km values	744:757	Glutaminyl cyclase was expressed as a fully active 37 kDa enzyme with kcat/Km values of 14.3, 9.3, and 2.4 mM(-1)s(-1) for the substrates Gln-Gln, Gln-NH(2), and Gln-t-butyl ester, respectively.
14680951	6	35	gly	glycosylation	933:945	arg2	asparagine					953:962	asparagine 49	953:965	asparagine 49	953:965	The two cysteines were disulfide bonded, and the lone predicted glycosylation site, asparagine 49, was shown by both enzymatic deglycosylation of the expressed enzyme and site-directed mutagenesis to be glycosylated.
14680951	6	35	gly	glycosylation	933:945	arg2	site					947:950	the lone predicted glycosylation site	914:950	the lone predicted glycosylation site	914:950	The two cysteines were disulfide bonded, and the lone predicted glycosylation site, asparagine 49, was shown by both enzymatic deglycosylation of the expressed enzyme and site-directed mutagenesis to be glycosylated.
14680951	5	36	with	enzyme	732:737	arg1	values					752:757	kcat/Km values	744:757	kcat/Km values	744:757	Glutaminyl cyclase was expressed as a fully active 37 kDa enzyme with kcat/Km values of 14.3, 9.3, and 2.4 mM(-1)s(-1) for the substrates Gln-Gln, Gln-NH(2), and Gln-t-butyl ester, respectively.
14680951	4	37	theme	Western	656:662	arg1	blotting					664:671	Western blotting	656:671	Western blotting	656:671	The identity of the expressed protein was confirmed by peptide mass mapping and Western blotting.
14680951	5	38	theme	active	718:723	arg1	enzyme					732:737	a fully active 37 kDa enzyme	710:737	a fully active 37 kDa enzyme with kcat/Km values of 14.3, 9.3, and 2.4 mM(-1)s(-1) for the substrates Gln-Gln, Gln-NH(2), and Gln-t-butyl ester, respectively	710:866	Glutaminyl cyclase was expressed as a fully active 37 kDa enzyme with kcat/Km values of 14.3, 9.3, and 2.4 mM(-1)s(-1) for the substrates Gln-Gln, Gln-NH(2), and Gln-t-butyl ester, respectively.
14680951	5	38	theme	active	718:723	arg1	cyclase					685:691	Glutaminyl cyclase	674:691	Glutaminyl cyclase	674:691	Glutaminyl cyclase was expressed as a fully active 37 kDa enzyme with kcat/Km values of 14.3, 9.3, and 2.4 mM(-1)s(-1) for the substrates Gln-Gln, Gln-NH(2), and Gln-t-butyl ester, respectively.
14680951	5	39	dep	substrates	801:810	arg1	Gln-NH					821:826	Gln-NH(2)	821:829	Gln-NH(2)	821:829	Glutaminyl cyclase was expressed as a fully active 37 kDa enzyme with kcat/Km values of 14.3, 9.3, and 2.4 mM(-1)s(-1) for the substrates Gln-Gln, Gln-NH(2), and Gln-t-butyl ester, respectively.
14680951	5	39	dep	substrates	801:810	arg1	Gln-Gln					812:818	Gln-Gln	812:818	Gln-Gln	812:818	Glutaminyl cyclase was expressed as a fully active 37 kDa enzyme with kcat/Km values of 14.3, 9.3, and 2.4 mM(-1)s(-1) for the substrates Gln-Gln, Gln-NH(2), and Gln-t-butyl ester, respectively.
14680951	5	39	dep	substrates	801:810	arg1	ester					848:852	Gln-t-butyl ester	836:852	Gln-t-butyl ester	836:852	Glutaminyl cyclase was expressed as a fully active 37 kDa enzyme with kcat/Km values of 14.3, 9.3, and 2.4 mM(-1)s(-1) for the substrates Gln-Gln, Gln-NH(2), and Gln-t-butyl ester, respectively.
14680951	5	39	dep	substrates	801:810	arg1	substrates					801:810	the substrates Gln-Gln, Gln-NH(2), and Gln-t-butyl ester	797:852	the substrates Gln-Gln, Gln-NH(2), and Gln-t-butyl ester	797:852	Glutaminyl cyclase was expressed as a fully active 37 kDa enzyme with kcat/Km values of 14.3, 9.3, and 2.4 mM(-1)s(-1) for the substrates Gln-Gln, Gln-NH(2), and Gln-t-butyl ester, respectively.
14680951	4	40	theme	mass	639:642	arg1	mapping					644:650	peptide mass mapping	631:650	peptide mass mapping	631:650	The identity of the expressed protein was confirmed by peptide mass mapping and Western blotting.
14680951	0	41	theme	insect	50:55	arg1	cells					57:61	insect cells	50:61	insect cells	50:61	Human pituitary glutaminyl cyclase: expression in insect cells and dye affinity purification.
14680951	5	42	theme	Glutaminyl	674:683	arg1	enzyme					732:737	a fully active 37 kDa enzyme	710:737	a fully active 37 kDa enzyme with kcat/Km values of 14.3, 9.3, and 2.4 mM(-1)s(-1) for the substrates Gln-Gln, Gln-NH(2), and Gln-t-butyl ester, respectively	710:866	Glutaminyl cyclase was expressed as a fully active 37 kDa enzyme with kcat/Km values of 14.3, 9.3, and 2.4 mM(-1)s(-1) for the substrates Gln-Gln, Gln-NH(2), and Gln-t-butyl ester, respectively.
14680951	5	42	theme	Glutaminyl	674:683	arg1	cyclase					685:691	Glutaminyl cyclase	674:691	Glutaminyl cyclase	674:691	Glutaminyl cyclase was expressed as a fully active 37 kDa enzyme with kcat/Km values of 14.3, 9.3, and 2.4 mM(-1)s(-1) for the substrates Gln-Gln, Gln-NH(2), and Gln-t-butyl ester, respectively.
14680951	1	43	theme	glutaminyl	110:119	arg1	hQC					130:132	hQC	130:132	hQC	130:132	Human pituitary glutaminyl cyclase (hQC) was expressed in Drosophila S2 cells under the control of an inducible metallothionene promoter and fused to the Drosophila immunoglobulin-binding protein signal sequence to enable secretion into the culture media.
14680951	1	43	theme	glutaminyl	110:119	arg1	cyclase					121:127	Human pituitary glutaminyl cyclase	94:127	Human pituitary glutaminyl cyclase (hQC)	94:133	Human pituitary glutaminyl cyclase (hQC) was expressed in Drosophila S2 cells under the control of an inducible metallothionene promoter and fused to the Drosophila immunoglobulin-binding protein signal sequence to enable secretion into the culture media.
14680951	6	44	gly	glycosylated	1072:1083	arg1	asparagine					953:962	asparagine 49	953:965	asparagine 49	953:965	The two cysteines were disulfide bonded, and the lone predicted glycosylation site, asparagine 49, was shown by both enzymatic deglycosylation of the expressed enzyme and site-directed mutagenesis to be glycosylated.
14680951	6	44	gly	glycosylated	1072:1083	arg1	site					947:950	the lone predicted glycosylation site	914:950	the lone predicted glycosylation site	914:950	The two cysteines were disulfide bonded, and the lone predicted glycosylation site, asparagine 49, was shown by both enzymatic deglycosylation of the expressed enzyme and site-directed mutagenesis to be glycosylated.
14680951	6	45	theme	site-directed	1040:1052	arg1	mutagenesis					1054:1064	site-directed mutagenesis	1040:1064	site-directed mutagenesis	1040:1064	The two cysteines were disulfide bonded, and the lone predicted glycosylation site, asparagine 49, was shown by both enzymatic deglycosylation of the expressed enzyme and site-directed mutagenesis to be glycosylated.
14680951	6	46	theme	expressed	1019:1027	arg1	enzyme					1029:1034	the expressed enzyme	1015:1034	the expressed enzyme	1015:1034	The two cysteines were disulfide bonded, and the lone predicted glycosylation site, asparagine 49, was shown by both enzymatic deglycosylation of the expressed enzyme and site-directed mutagenesis to be glycosylated.
14680951	0	47	dep	cyclase	27:33	arg1	expression					36:45	expression	36:45	expression in insect cells	36:61	Human pituitary glutaminyl cyclase: expression in insect cells and dye affinity purification.
14680951	0	47	dep	cyclase	27:33	arg1	purification					80:91	dye affinity purification	67:91	dye affinity purification	67:91	Human pituitary glutaminyl cyclase: expression in insect cells and dye affinity purification.
14680951	6	48	theme	lone	918:921	arg1	asparagine					953:962	asparagine 49	953:965	asparagine 49	953:965	The two cysteines were disulfide bonded, and the lone predicted glycosylation site, asparagine 49, was shown by both enzymatic deglycosylation of the expressed enzyme and site-directed mutagenesis to be glycosylated.
14680951	6	48	theme	lone	918:921	arg1	site					947:950	the lone predicted glycosylation site	914:950	the lone predicted glycosylation site	914:950	The two cysteines were disulfide bonded, and the lone predicted glycosylation site, asparagine 49, was shown by both enzymatic deglycosylation of the expressed enzyme and site-directed mutagenesis to be glycosylated.
14680951	3	49	theme	step	559:562	arg1	elution					567:573	a step pH elution	557:573	a step pH elution	557:573	The enzyme was purified to homogeneity directly from culture media by affinity chromatography on Reactive Blue 4-agarose using a step pH elution.
14680951	1	50	theme	inducible	196:204	arg1	promoter					222:229	an inducible metallothionene promoter	193:229	an inducible metallothionene promoter	193:229	Human pituitary glutaminyl cyclase (hQC) was expressed in Drosophila S2 cells under the control of an inducible metallothionene promoter and fused to the Drosophila immunoglobulin-binding protein signal sequence to enable secretion into the culture media.
14680951	3	51	theme	culture	483:489	arg1	media					491:495	culture media	483:495	culture media	483:495	The enzyme was purified to homogeneity directly from culture media by affinity chromatography on Reactive Blue 4-agarose using a step pH elution.
14680951	1	52	theme	metallothionene	206:220	arg1	promoter					222:229	an inducible metallothionene promoter	193:229	an inducible metallothionene promoter	193:229	Human pituitary glutaminyl cyclase (hQC) was expressed in Drosophila S2 cells under the control of an inducible metallothionene promoter and fused to the Drosophila immunoglobulin-binding protein signal sequence to enable secretion into the culture media.
14680951	5	53	theme	kcat/Km	744:750	arg1	values					752:757	kcat/Km values	744:757	kcat/Km values	744:757	Glutaminyl cyclase was expressed as a fully active 37 kDa enzyme with kcat/Km values of 14.3, 9.3, and 2.4 mM(-1)s(-1) for the substrates Gln-Gln, Gln-NH(2), and Gln-t-butyl ester, respectively.
14680951	0	54	from	purification	80:91	arg1	cells					57:61	insect cells	50:61	insect cells	50:61	Human pituitary glutaminyl cyclase: expression in insect cells and dye affinity purification.
14680951	4	55	theme	peptide	631:637	arg1	mapping					644:650	peptide mass mapping	631:650	peptide mass mapping	631:650	The identity of the expressed protein was confirmed by peptide mass mapping and Western blotting.
14680951	2	56	theme	50	376:377	arg1	microg/mL					379:387	microg/mL	379:387	microg/mL	379:387	Expression levels reached 50 microg/mL culture media after 7 days of induction.
14680951	1	57	theme	promoter	222:229	arg1	control					182:188	the control	178:188	the control of an inducible metallothionene promoter	178:229	Human pituitary glutaminyl cyclase (hQC) was expressed in Drosophila S2 cells under the control of an inducible metallothionene promoter and fused to the Drosophila immunoglobulin-binding protein signal sequence to enable secretion into the culture media.
14680951	3	58	theme	Reactive	527:534	arg1	4-agarose					541:549	Reactive Blue 4-agarose	527:549	Reactive Blue 4-agarose using a step pH elution	527:573	The enzyme was purified to homogeneity directly from culture media by affinity chromatography on Reactive Blue 4-agarose using a step pH elution.
25580119	0	0	theme	Impaired	86:93	arg1	Signaling					103:111	Impaired Insulin Signaling	86:111	Impaired Insulin Signaling in Alzheimer and Diabetes	86:137	Alternate Phosphorylation/O-GlcNAc Modification on Human Insulin IRSs: A Road towards Impaired Insulin Signaling in Alzheimer and Diabetes.
25580119	0	1	from	Modification	35:46	arg1	IRSs					65:68	Human Insulin IRSs	51:68	Human Insulin IRSs	51:68	Alternate Phosphorylation/O-GlcNAc Modification on Human Insulin IRSs: A Road towards Impaired Insulin Signaling in Alzheimer and Diabetes.
25580119	3	2	dep	substrates	551:560	arg1	2					568:568	2	568:568	2	568:568	Two important insulin receptor substrates 1 and 2 are widely expressed in human, and alternative phosphorylation on their serine (Ser) and threonine (Thr) residues has been known to block the Tyr phosphorylation of IRSs, thus inhibiting insulin signaling and promoting insulin resistance.
25580119	3	2	dep	substrates	551:560	arg1	1					562:562	1	562:562	1	562:562	Two important insulin receptor substrates 1 and 2 are widely expressed in human, and alternative phosphorylation on their serine (Ser) and threonine (Thr) residues has been known to block the Tyr phosphorylation of IRSs, thus inhibiting insulin signaling and promoting insulin resistance.
25580119	6	3	theme	possible	1241:1248	arg1	residues					1176:1183	more than 50 Ser/Thr residues	1155:1183	more than 50 Ser/Thr residues that have potential to be O-glycosylated and may act as possible sites as well	1155:1262	In this study, by using neuronal network based prediction methods, we found more than 50 Ser/Thr residues that have potential to be O-glycosylated and may act as possible sites as well.
25580119	6	3	theme	possible	1241:1248	arg1	sites					1250:1254	possible sites	1241:1254	possible sites	1241:1254	In this study, by using neuronal network based prediction methods, we found more than 50 Ser/Thr residues that have potential to be O-glycosylated and may act as possible sites as well.
25580119	7	4	theme	therapeutic	1381:1391	arg1	targets					1393:1399	possible therapeutic targets	1372:1399	possible therapeutic targets	1372:1399	Moreover, alternative phosphorylation and O-glycosylation on IRS-1 Ser-312, 984, 1037, and 1101 may act as possible therapeutic targets to minimize the risk of AD and T2DM.
25580119	7	4	theme	therapeutic	1381:1391	arg1	phosphorylation					1287:1301	alternative phosphorylation	1275:1301	alternative phosphorylation	1275:1301	Moreover, alternative phosphorylation and O-glycosylation on IRS-1 Ser-312, 984, 1037, and 1101 may act as possible therapeutic targets to minimize the risk of AD and T2DM.
25580119	7	4	theme	therapeutic	1381:1391	arg1	O-glycosylation					1307:1321	O-glycosylation	1307:1321	O-glycosylation	1307:1321	Moreover, alternative phosphorylation and O-glycosylation on IRS-1 Ser-312, 984, 1037, and 1101 may act as possible therapeutic targets to minimize the risk of AD and T2DM.
25580119	2	5	theme	several	479:485	arg1	residues					502:509	several tyrosine (TYR) residues	479:509	several tyrosine (TYR) residues on IRSs	479:517	Posttranslational modifications (PTMs) regulate functions and interaction of insulin with insulin receptors substrates (IRSs) and activate insulin signaling downstream pathways via autophosphorylation on several tyrosine (TYR) residues on IRSs.
25580119	4	6	theme	O-glycosylation	831:845	arg1	modification					847:858	O-glycosylation modification	831:858	O-glycosylation modification	831:858	Like phosphorylation, O-glycosylation modification is important PTM and inhibits phosphorylation on same or neighboring Ser/Thr residues, often called Yin Yang sites.
25580119	3	7	dep	serine	642:647	arg1	residues					675:682	residues	675:682	residues	675:682	Two important insulin receptor substrates 1 and 2 are widely expressed in human, and alternative phosphorylation on their serine (Ser) and threonine (Thr) residues has been known to block the Tyr phosphorylation of IRSs, thus inhibiting insulin signaling and promoting insulin resistance.
25580119	4	8	theme	neighboring	917:927	arg1	residues					937:944	same or neighboring Ser/Thr residues	909:944	same or neighboring Ser/Thr residues	909:944	Like phosphorylation, O-glycosylation modification is important PTM and inhibits phosphorylation on same or neighboring Ser/Thr residues, often called Yin Yang sites.
25580119	3	9	dep	block	702:706	arg1	inhibiting					746:755	inhibiting	746:755	inhibiting insulin signaling	746:773	Two important insulin receptor substrates 1 and 2 are widely expressed in human, and alternative phosphorylation on their serine (Ser) and threonine (Thr) residues has been known to block the Tyr phosphorylation of IRSs, thus inhibiting insulin signaling and promoting insulin resistance.
25580119	3	9	dep	block	702:706	arg1	promoting					779:787	promoting	779:787	promoting insulin resistance	779:806	Two important insulin receptor substrates 1 and 2 are widely expressed in human, and alternative phosphorylation on their serine (Ser) and threonine (Thr) residues has been known to block the Tyr phosphorylation of IRSs, thus inhibiting insulin signaling and promoting insulin resistance.
25580119	6	10	theme	prediction	1126:1135	arg1	methods					1137:1143	neuronal network based prediction methods	1103:1143	neuronal network based prediction methods	1103:1143	In this study, by using neuronal network based prediction methods, we found more than 50 Ser/Thr residues that have potential to be O-glycosylated and may act as possible sites as well.
25580119	1	11	theme	type	242:245	arg1	T2DM					268:271	T2DM	268:271	T2DM	268:271	Impaired insulin signaling has been thought of as important step in both Alzheimer's disease (AD) and type 2 diabetes mellitus (T2DM).
25580119	1	11	theme	type	242:245	arg1	mellitus					258:265	type 2 diabetes mellitus	242:265	type 2 diabetes mellitus (T2DM)	242:272	Impaired insulin signaling has been thought of as important step in both Alzheimer's disease (AD) and type 2 diabetes mellitus (T2DM).
25580119	0	12	theme	Insulin	95:101	arg1	Signaling					103:111	Impaired Insulin Signaling	86:111	Impaired Insulin Signaling in Alzheimer and Diabetes	86:137	Alternate Phosphorylation/O-GlcNAc Modification on Human Insulin IRSs: A Road towards Impaired Insulin Signaling in Alzheimer and Diabetes.
25580119	7	13	theme	T2DM	1432:1435	arg1	risk					1417:1420	the risk	1413:1420	the risk of AD and T2DM	1413:1435	Moreover, alternative phosphorylation and O-glycosylation on IRS-1 Ser-312, 984, 1037, and 1101 may act as possible therapeutic targets to minimize the risk of AD and T2DM.
25580119	3	14	theme	important	524:532	arg1	substrates					551:560	Two important insulin receptor substrates	520:560	Two important insulin receptor substrates 1 and 2	520:568	Two important insulin receptor substrates 1 and 2 are widely expressed in human, and alternative phosphorylation on their serine (Ser) and threonine (Thr) residues has been known to block the Tyr phosphorylation of IRSs, thus inhibiting insulin signaling and promoting insulin resistance.
25580119	2	15	dep	functions	323:331	arg1	IRSs					395:398	IRSs	395:398	IRSs	395:398	Posttranslational modifications (PTMs) regulate functions and interaction of insulin with insulin receptors substrates (IRSs) and activate insulin signaling downstream pathways via autophosphorylation on several tyrosine (TYR) residues on IRSs.
25580119	2	15	dep	functions	323:331	arg1	substrates					383:392	substrates	383:392	substrates (IRSs)	383:399	Posttranslational modifications (PTMs) regulate functions and interaction of insulin with insulin receptors substrates (IRSs) and activate insulin signaling downstream pathways via autophosphorylation on several tyrosine (TYR) residues on IRSs.
25580119	3	16	from	phosphorylation	617:631	arg1	threonine					659:667	threonine	659:667	threonine (Thr)	659:673	Two important insulin receptor substrates 1 and 2 are widely expressed in human, and alternative phosphorylation on their serine (Ser) and threonine (Thr) residues has been known to block the Tyr phosphorylation of IRSs, thus inhibiting insulin signaling and promoting insulin resistance.
25580119	3	16	from	phosphorylation	617:631	arg1	serine					642:647	their serine	636:647	their serine (Ser)	636:653	Two important insulin receptor substrates 1 and 2 are widely expressed in human, and alternative phosphorylation on their serine (Ser) and threonine (Thr) residues has been known to block the Tyr phosphorylation of IRSs, thus inhibiting insulin signaling and promoting insulin resistance.
25580119	3	16	from	phosphorylation	617:631	arg1	Thr					670:672	Thr	670:672	Thr	670:672	Two important insulin receptor substrates 1 and 2 are widely expressed in human, and alternative phosphorylation on their serine (Ser) and threonine (Thr) residues has been known to block the Tyr phosphorylation of IRSs, thus inhibiting insulin signaling and promoting insulin resistance.
25580119	3	16	from	phosphorylation	617:631	arg1	Ser					650:652	Ser	650:652	Ser	650:652	Two important insulin receptor substrates 1 and 2 are widely expressed in human, and alternative phosphorylation on their serine (Ser) and threonine (Thr) residues has been known to block the Tyr phosphorylation of IRSs, thus inhibiting insulin signaling and promoting insulin resistance.
25580119	7	17	theme	possible	1372:1379	arg1	targets					1393:1399	possible therapeutic targets	1372:1399	possible therapeutic targets	1372:1399	Moreover, alternative phosphorylation and O-glycosylation on IRS-1 Ser-312, 984, 1037, and 1101 may act as possible therapeutic targets to minimize the risk of AD and T2DM.
25580119	7	17	theme	possible	1372:1379	arg1	phosphorylation					1287:1301	alternative phosphorylation	1275:1301	alternative phosphorylation	1275:1301	Moreover, alternative phosphorylation and O-glycosylation on IRS-1 Ser-312, 984, 1037, and 1101 may act as possible therapeutic targets to minimize the risk of AD and T2DM.
25580119	7	17	theme	possible	1372:1379	arg1	O-glycosylation					1307:1321	O-glycosylation	1307:1321	O-glycosylation	1307:1321	Moreover, alternative phosphorylation and O-glycosylation on IRS-1 Ser-312, 984, 1037, and 1101 may act as possible therapeutic targets to minimize the risk of AD and T2DM.
25580119	6	18	theme	network	1112:1118	arg1	methods					1137:1143	neuronal network based prediction methods	1103:1143	neuronal network based prediction methods	1103:1143	In this study, by using neuronal network based prediction methods, we found more than 50 Ser/Thr residues that have potential to be O-glycosylated and may act as possible sites as well.
25580119	3	19	theme	insulin	757:763	arg1	signaling					765:773	insulin signaling	757:773	insulin signaling	757:773	Two important insulin receptor substrates 1 and 2 are widely expressed in human, and alternative phosphorylation on their serine (Ser) and threonine (Thr) residues has been known to block the Tyr phosphorylation of IRSs, thus inhibiting insulin signaling and promoting insulin resistance.
25580119	2	20	theme	TYR	497:499	arg1	residues					502:509	several tyrosine (TYR) residues	479:509	several tyrosine (TYR) residues on IRSs	479:517	Posttranslational modifications (PTMs) regulate functions and interaction of insulin with insulin receptors substrates (IRSs) and activate insulin signaling downstream pathways via autophosphorylation on several tyrosine (TYR) residues on IRSs.
25580119	2	21	from	autophosphorylation	456:474	arg1	residues					502:509	several tyrosine (TYR) residues	479:509	several tyrosine (TYR) residues on IRSs	479:517	Posttranslational modifications (PTMs) regulate functions and interaction of insulin with insulin receptors substrates (IRSs) and activate insulin signaling downstream pathways via autophosphorylation on several tyrosine (TYR) residues on IRSs.
25580119	0	22	theme	Alternate	0:8	arg1	Modification					35:46	Alternate Phosphorylation/O-GlcNAc Modification	0:46	Alternate Phosphorylation/O-GlcNAc Modification on Human Insulin IRSs: A Road towards Impaired Insulin Signaling in Alzheimer and Diabetes.	0:138	Alternate Phosphorylation/O-GlcNAc Modification on Human Insulin IRSs: A Road towards Impaired Insulin Signaling in Alzheimer and Diabetes.
25580119	2	23	theme	insulin	365:371	arg1	receptors					373:381	insulin receptors	365:381	insulin receptors	365:381	Posttranslational modifications (PTMs) regulate functions and interaction of insulin with insulin receptors substrates (IRSs) and activate insulin signaling downstream pathways via autophosphorylation on several tyrosine (TYR) residues on IRSs.
25580119	0	24	theme	Phosphorylation/O-GlcNAc	10:33	arg1	Modification					35:46	Alternate Phosphorylation/O-GlcNAc Modification	0:46	Alternate Phosphorylation/O-GlcNAc Modification on Human Insulin IRSs: A Road towards Impaired Insulin Signaling in Alzheimer and Diabetes.	0:138	Alternate Phosphorylation/O-GlcNAc Modification on Human Insulin IRSs: A Road towards Impaired Insulin Signaling in Alzheimer and Diabetes.
25580119	7	25	from	phosphorylation	1287:1301	arg1	984					1341:1343	984	1341:1343	984	1341:1343	Moreover, alternative phosphorylation and O-glycosylation on IRS-1 Ser-312, 984, 1037, and 1101 may act as possible therapeutic targets to minimize the risk of AD and T2DM.
25580119	7	25	from	phosphorylation	1287:1301	arg1	Ser-312					1332:1338	IRS-1 Ser-312	1326:1338	IRS-1 Ser-312	1326:1338	Moreover, alternative phosphorylation and O-glycosylation on IRS-1 Ser-312, 984, 1037, and 1101 may act as possible therapeutic targets to minimize the risk of AD and T2DM.
25580119	7	25	from	phosphorylation	1287:1301	arg1	1037					1346:1349	1037	1346:1349	1037	1346:1349	Moreover, alternative phosphorylation and O-glycosylation on IRS-1 Ser-312, 984, 1037, and 1101 may act as possible therapeutic targets to minimize the risk of AD and T2DM.
25580119	7	25	from	phosphorylation	1287:1301	arg1	1101					1356:1359	1101	1356:1359	1101	1356:1359	Moreover, alternative phosphorylation and O-glycosylation on IRS-1 Ser-312, 984, 1037, and 1101 may act as possible therapeutic targets to minimize the risk of AD and T2DM.
25580119	2	26	theme	insulin	414:420	arg1	pathways					443:450	insulin signaling downstream pathways	414:450	insulin signaling downstream pathways	414:450	Posttranslational modifications (PTMs) regulate functions and interaction of insulin with insulin receptors substrates (IRSs) and activate insulin signaling downstream pathways via autophosphorylation on several tyrosine (TYR) residues on IRSs.
25580119	1	27	theme	diabetes	249:256	arg1	T2DM					268:271	T2DM	268:271	T2DM	268:271	Impaired insulin signaling has been thought of as important step in both Alzheimer's disease (AD) and type 2 diabetes mellitus (T2DM).
25580119	1	27	theme	diabetes	249:256	arg1	mellitus					258:265	type 2 diabetes mellitus	242:265	type 2 diabetes mellitus (T2DM)	242:272	Impaired insulin signaling has been thought of as important step in both Alzheimer's disease (AD) and type 2 diabetes mellitus (T2DM).
25580119	2	28	with	interaction	337:347	arg1	receptors					373:381	insulin receptors	365:381	insulin receptors	365:381	Posttranslational modifications (PTMs) regulate functions and interaction of insulin with insulin receptors substrates (IRSs) and activate insulin signaling downstream pathways via autophosphorylation on several tyrosine (TYR) residues on IRSs.
25580119	2	29	theme	Posttranslational	275:291	arg1	PTMs					308:311	PTMs	308:311	PTMs	308:311	Posttranslational modifications (PTMs) regulate functions and interaction of insulin with insulin receptors substrates (IRSs) and activate insulin signaling downstream pathways via autophosphorylation on several tyrosine (TYR) residues on IRSs.
25580119	2	29	theme	Posttranslational	275:291	arg1	modifications					293:305	Posttranslational modifications	275:305	Posttranslational modifications (PTMs)	275:312	Posttranslational modifications (PTMs) regulate functions and interaction of insulin with insulin receptors substrates (IRSs) and activate insulin signaling downstream pathways via autophosphorylation on several tyrosine (TYR) residues on IRSs.
25580119	2	30	theme	insulin	352:358	arg1	interaction					337:347	interaction	337:347	interaction of insulin with insulin receptors	337:381	Posttranslational modifications (PTMs) regulate functions and interaction of insulin with insulin receptors substrates (IRSs) and activate insulin signaling downstream pathways via autophosphorylation on several tyrosine (TYR) residues on IRSs.
25580119	2	30	theme	insulin	352:358	arg1	functions					323:331	functions	323:331	functions	323:331	Posttranslational modifications (PTMs) regulate functions and interaction of insulin with insulin receptors substrates (IRSs) and activate insulin signaling downstream pathways via autophosphorylation on several tyrosine (TYR) residues on IRSs.
25580119	5	31	theme	exact	1043:1047	arg1	sites					1049:1053	exact sites	1043:1053	exact sites	1043:1053	Both IRS-1 and IRS-2 have been shown to be O-glycosylated; however exact sites are not determined yet.
25580119	3	32	theme	insulin	534:540	arg1	substrates					551:560	Two important insulin receptor substrates	520:560	Two important insulin receptor substrates 1 and 2	520:568	Two important insulin receptor substrates 1 and 2 are widely expressed in human, and alternative phosphorylation on their serine (Ser) and threonine (Thr) residues has been known to block the Tyr phosphorylation of IRSs, thus inhibiting insulin signaling and promoting insulin resistance.
25580119	7	33	from	O-glycosylation	1307:1321	arg1	984					1341:1343	984	1341:1343	984	1341:1343	Moreover, alternative phosphorylation and O-glycosylation on IRS-1 Ser-312, 984, 1037, and 1101 may act as possible therapeutic targets to minimize the risk of AD and T2DM.
25580119	7	33	from	O-glycosylation	1307:1321	arg1	Ser-312					1332:1338	IRS-1 Ser-312	1326:1338	IRS-1 Ser-312	1326:1338	Moreover, alternative phosphorylation and O-glycosylation on IRS-1 Ser-312, 984, 1037, and 1101 may act as possible therapeutic targets to minimize the risk of AD and T2DM.
25580119	7	33	from	O-glycosylation	1307:1321	arg1	1037					1346:1349	1037	1346:1349	1037	1346:1349	Moreover, alternative phosphorylation and O-glycosylation on IRS-1 Ser-312, 984, 1037, and 1101 may act as possible therapeutic targets to minimize the risk of AD and T2DM.
25580119	7	33	from	O-glycosylation	1307:1321	arg1	1101					1356:1359	1101	1356:1359	1101	1356:1359	Moreover, alternative phosphorylation and O-glycosylation on IRS-1 Ser-312, 984, 1037, and 1101 may act as possible therapeutic targets to minimize the risk of AD and T2DM.
25580119	3	34	theme	receptor	542:549	arg1	substrates					551:560	Two important insulin receptor substrates	520:560	Two important insulin receptor substrates 1 and 2	520:568	Two important insulin receptor substrates 1 and 2 are widely expressed in human, and alternative phosphorylation on their serine (Ser) and threonine (Thr) residues has been known to block the Tyr phosphorylation of IRSs, thus inhibiting insulin signaling and promoting insulin resistance.
25580119	0	35	theme	Insulin	57:63	arg1	IRSs					65:68	Human Insulin IRSs	51:68	Human Insulin IRSs	51:68	Alternate Phosphorylation/O-GlcNAc Modification on Human Insulin IRSs: A Road towards Impaired Insulin Signaling in Alzheimer and Diabetes.
25580119	4	36	theme	same	909:912	arg1	residues					937:944	same or neighboring Ser/Thr residues	909:944	same or neighboring Ser/Thr residues	909:944	Like phosphorylation, O-glycosylation modification is important PTM and inhibits phosphorylation on same or neighboring Ser/Thr residues, often called Yin Yang sites.
25580119	6	37	theme	Ser/Thr	1168:1174	arg1	residues					1176:1183	more than 50 Ser/Thr residues	1155:1183	more than 50 Ser/Thr residues that have potential to be O-glycosylated and may act as possible sites as well	1155:1262	In this study, by using neuronal network based prediction methods, we found more than 50 Ser/Thr residues that have potential to be O-glycosylated and may act as possible sites as well.
25580119	6	37	theme	Ser/Thr	1168:1174	arg1	sites					1250:1254	possible sites	1241:1254	possible sites	1241:1254	In this study, by using neuronal network based prediction methods, we found more than 50 Ser/Thr residues that have potential to be O-glycosylated and may act as possible sites as well.
25580119	1	38	theme	important	190:198	arg1	signaling					157:165	Impaired insulin signaling	140:165	Impaired insulin signaling	140:165	Impaired insulin signaling has been thought of as important step in both Alzheimer's disease (AD) and type 2 diabetes mellitus (T2DM).
25580119	1	38	theme	important	190:198	arg1	step					200:203	important step	190:203	important step in both Alzheimer's disease (AD) and type 2 diabetes mellitus (T2DM)	190:272	Impaired insulin signaling has been thought of as important step in both Alzheimer's disease (AD) and type 2 diabetes mellitus (T2DM).
25580119	0	39	theme	Human	51:55	arg1	IRSs					65:68	Human Insulin IRSs	51:68	Human Insulin IRSs	51:68	Alternate Phosphorylation/O-GlcNAc Modification on Human Insulin IRSs: A Road towards Impaired Insulin Signaling in Alzheimer and Diabetes.
25580119	4	40	theme	Yang	964:967	arg1	sites					969:973	Yin Yang sites	960:973	Yin Yang sites	960:973	Like phosphorylation, O-glycosylation modification is important PTM and inhibits phosphorylation on same or neighboring Ser/Thr residues, often called Yin Yang sites.
25580119	4	41	from	phosphorylation	890:904	arg1	residues					937:944	same or neighboring Ser/Thr residues	909:944	same or neighboring Ser/Thr residues	909:944	Like phosphorylation, O-glycosylation modification is important PTM and inhibits phosphorylation on same or neighboring Ser/Thr residues, often called Yin Yang sites.
25580119	7	42	theme	IRS-1	1326:1330	arg1	984					1341:1343	984	1341:1343	984	1341:1343	Moreover, alternative phosphorylation and O-glycosylation on IRS-1 Ser-312, 984, 1037, and 1101 may act as possible therapeutic targets to minimize the risk of AD and T2DM.
25580119	7	42	theme	IRS-1	1326:1330	arg1	Ser-312					1332:1338	IRS-1 Ser-312	1326:1338	IRS-1 Ser-312	1326:1338	Moreover, alternative phosphorylation and O-glycosylation on IRS-1 Ser-312, 984, 1037, and 1101 may act as possible therapeutic targets to minimize the risk of AD and T2DM.
25580119	7	42	theme	IRS-1	1326:1330	arg1	1037					1346:1349	1037	1346:1349	1037	1346:1349	Moreover, alternative phosphorylation and O-glycosylation on IRS-1 Ser-312, 984, 1037, and 1101 may act as possible therapeutic targets to minimize the risk of AD and T2DM.
25580119	7	42	theme	IRS-1	1326:1330	arg1	1101					1356:1359	1101	1356:1359	1101	1356:1359	Moreover, alternative phosphorylation and O-glycosylation on IRS-1 Ser-312, 984, 1037, and 1101 may act as possible therapeutic targets to minimize the risk of AD and T2DM.
25580119	4	43	theme	Ser/Thr	929:935	arg1	residues					937:944	same or neighboring Ser/Thr residues	909:944	same or neighboring Ser/Thr residues	909:944	Like phosphorylation, O-glycosylation modification is important PTM and inhibits phosphorylation on same or neighboring Ser/Thr residues, often called Yin Yang sites.
25580119	7	44	gly	O-glycosylation	1307:1321	arg1	984					1341:1343	984	1341:1343	984	1341:1343	Moreover, alternative phosphorylation and O-glycosylation on IRS-1 Ser-312, 984, 1037, and 1101 may act as possible therapeutic targets to minimize the risk of AD and T2DM.
25580119	7	44	gly	O-glycosylation	1307:1321	arg1	Ser-312					1332:1338	IRS-1 Ser-312	1326:1338	IRS-1 Ser-312	1326:1338	Moreover, alternative phosphorylation and O-glycosylation on IRS-1 Ser-312, 984, 1037, and 1101 may act as possible therapeutic targets to minimize the risk of AD and T2DM.
25580119	7	44	gly	O-glycosylation	1307:1321	arg1	1037					1346:1349	1037	1346:1349	1037	1346:1349	Moreover, alternative phosphorylation and O-glycosylation on IRS-1 Ser-312, 984, 1037, and 1101 may act as possible therapeutic targets to minimize the risk of AD and T2DM.
25580119	7	44	gly	O-glycosylation	1307:1321	arg1	1101					1356:1359	1101	1356:1359	1101	1356:1359	Moreover, alternative phosphorylation and O-glycosylation on IRS-1 Ser-312, 984, 1037, and 1101 may act as possible therapeutic targets to minimize the risk of AD and T2DM.
25580119	4	45	theme	important	863:871	arg1	PTM					873:875	important PTM	863:875	important PTM	863:875	Like phosphorylation, O-glycosylation modification is important PTM and inhibits phosphorylation on same or neighboring Ser/Thr residues, often called Yin Yang sites.
25580119	3	46	theme	alternative	605:615	arg1	phosphorylation					617:631	alternative phosphorylation	605:631	alternative phosphorylation on their serine (Ser) and threonine (Thr) residues	605:682	Two important insulin receptor substrates 1 and 2 are widely expressed in human, and alternative phosphorylation on their serine (Ser) and threonine (Thr) residues has been known to block the Tyr phosphorylation of IRSs, thus inhibiting insulin signaling and promoting insulin resistance.
25580119	2	47	theme	downstream	432:441	arg1	pathways					443:450	insulin signaling downstream pathways	414:450	insulin signaling downstream pathways	414:450	Posttranslational modifications (PTMs) regulate functions and interaction of insulin with insulin receptors substrates (IRSs) and activate insulin signaling downstream pathways via autophosphorylation on several tyrosine (TYR) residues on IRSs.
25580119	6	48	theme	based	1120:1124	arg1	methods					1137:1143	neuronal network based prediction methods	1103:1143	neuronal network based prediction methods	1103:1143	In this study, by using neuronal network based prediction methods, we found more than 50 Ser/Thr residues that have potential to be O-glycosylated and may act as possible sites as well.
25580119	7	49	theme	AD	1425:1426	arg1	risk					1417:1420	the risk	1413:1420	the risk of AD and T2DM	1413:1435	Moreover, alternative phosphorylation and O-glycosylation on IRS-1 Ser-312, 984, 1037, and 1101 may act as possible therapeutic targets to minimize the risk of AD and T2DM.
25580119	1	50	from	step	200:203	arg1	T2DM					268:271	T2DM	268:271	T2DM	268:271	Impaired insulin signaling has been thought of as important step in both Alzheimer's disease (AD) and type 2 diabetes mellitus (T2DM).
25580119	1	50	from	step	200:203	arg1	mellitus					258:265	type 2 diabetes mellitus	242:265	type 2 diabetes mellitus (T2DM)	242:272	Impaired insulin signaling has been thought of as important step in both Alzheimer's disease (AD) and type 2 diabetes mellitus (T2DM).
25580119	1	50	from	step	200:203	arg1	AD					234:235	AD	234:235	AD	234:235	Impaired insulin signaling has been thought of as important step in both Alzheimer's disease (AD) and type 2 diabetes mellitus (T2DM).
25580119	1	50	from	step	200:203	arg1	disease					225:231	Alzheimer's disease	213:231	Alzheimer's disease (AD)	213:236	Impaired insulin signaling has been thought of as important step in both Alzheimer's disease (AD) and type 2 diabetes mellitus (T2DM).
25580119	3	51	theme	Tyr	712:714	arg1	phosphorylation					716:730	the Tyr phosphorylation	708:730	the Tyr phosphorylation of IRSs	708:738	Two important insulin receptor substrates 1 and 2 are widely expressed in human, and alternative phosphorylation on their serine (Ser) and threonine (Thr) residues has been known to block the Tyr phosphorylation of IRSs, thus inhibiting insulin signaling and promoting insulin resistance.
25580119	2	52	with	functions	323:331	arg1	receptors					373:381	insulin receptors	365:381	insulin receptors	365:381	Posttranslational modifications (PTMs) regulate functions and interaction of insulin with insulin receptors substrates (IRSs) and activate insulin signaling downstream pathways via autophosphorylation on several tyrosine (TYR) residues on IRSs.
25580119	7	53	theme	alternative	1275:1285	arg1	targets					1393:1399	possible therapeutic targets	1372:1399	possible therapeutic targets	1372:1399	Moreover, alternative phosphorylation and O-glycosylation on IRS-1 Ser-312, 984, 1037, and 1101 may act as possible therapeutic targets to minimize the risk of AD and T2DM.
25580119	7	53	theme	alternative	1275:1285	arg1	phosphorylation					1287:1301	alternative phosphorylation	1275:1301	alternative phosphorylation	1275:1301	Moreover, alternative phosphorylation and O-glycosylation on IRS-1 Ser-312, 984, 1037, and 1101 may act as possible therapeutic targets to minimize the risk of AD and T2DM.
25580119	7	53	theme	alternative	1275:1285	arg1	O-glycosylation					1307:1321	O-glycosylation	1307:1321	O-glycosylation	1307:1321	Moreover, alternative phosphorylation and O-glycosylation on IRS-1 Ser-312, 984, 1037, and 1101 may act as possible therapeutic targets to minimize the risk of AD and T2DM.
25580119	5	54	gly	O-glycosylated	1019:1032	arg1	IRS-2					991:995	IRS-2	991:995	IRS-2	991:995	Both IRS-1 and IRS-2 have been shown to be O-glycosylated; however exact sites are not determined yet.
25580119	5	54	gly	O-glycosylated	1019:1032	arg1	IRS-1					981:985	IRS-1	981:985	IRS-1	981:985	Both IRS-1 and IRS-2 have been shown to be O-glycosylated; however exact sites are not determined yet.
25580119	6	55	theme	neuronal	1103:1110	arg1	methods					1137:1143	neuronal network based prediction methods	1103:1143	neuronal network based prediction methods	1103:1143	In this study, by using neuronal network based prediction methods, we found more than 50 Ser/Thr residues that have potential to be O-glycosylated and may act as possible sites as well.
25580119	0	56	from	Signaling	103:111	arg1	Diabetes					130:137	Diabetes	130:137	Diabetes	130:137	Alternate Phosphorylation/O-GlcNAc Modification on Human Insulin IRSs: A Road towards Impaired Insulin Signaling in Alzheimer and Diabetes.
25580119	0	56	from	Signaling	103:111	arg1	Alzheimer					116:124	Alzheimer	116:124	Alzheimer	116:124	Alternate Phosphorylation/O-GlcNAc Modification on Human Insulin IRSs: A Road towards Impaired Insulin Signaling in Alzheimer and Diabetes.
25580119	0	57	dep	Modification	35:46	arg1	Road					73:76	A Road	71:76	Alternate Phosphorylation/O-GlcNAc Modification on Human Insulin IRSs: A Road towards Impaired Insulin Signaling in Alzheimer and Diabetes.	0:138	Alternate Phosphorylation/O-GlcNAc Modification on Human Insulin IRSs: A Road towards Impaired Insulin Signaling in Alzheimer and Diabetes.
25580119	1	58	theme	Impaired	140:147	arg1	signaling					157:165	Impaired insulin signaling	140:165	Impaired insulin signaling	140:165	Impaired insulin signaling has been thought of as important step in both Alzheimer's disease (AD) and type 2 diabetes mellitus (T2DM).
25580119	1	58	theme	Impaired	140:147	arg1	step					200:203	important step	190:203	important step in both Alzheimer's disease (AD) and type 2 diabetes mellitus (T2DM)	190:272	Impaired insulin signaling has been thought of as important step in both Alzheimer's disease (AD) and type 2 diabetes mellitus (T2DM).
25580119	3	59	theme	insulin	789:795	arg1	resistance					797:806	insulin resistance	789:806	insulin resistance	789:806	Two important insulin receptor substrates 1 and 2 are widely expressed in human, and alternative phosphorylation on their serine (Ser) and threonine (Thr) residues has been known to block the Tyr phosphorylation of IRSs, thus inhibiting insulin signaling and promoting insulin resistance.
25580119	2	60	from	residues	502:509	arg1	IRSs					514:517	IRSs	514:517	IRSs	514:517	Posttranslational modifications (PTMs) regulate functions and interaction of insulin with insulin receptors substrates (IRSs) and activate insulin signaling downstream pathways via autophosphorylation on several tyrosine (TYR) residues on IRSs.
25580119	1	61	theme	insulin	149:155	arg1	signaling					157:165	Impaired insulin signaling	140:165	Impaired insulin signaling	140:165	Impaired insulin signaling has been thought of as important step in both Alzheimer's disease (AD) and type 2 diabetes mellitus (T2DM).
25580119	1	61	theme	insulin	149:155	arg1	step					200:203	important step	190:203	important step in both Alzheimer's disease (AD) and type 2 diabetes mellitus (T2DM)	190:272	Impaired insulin signaling has been thought of as important step in both Alzheimer's disease (AD) and type 2 diabetes mellitus (T2DM).
25580119	3	62	theme	IRSs	735:738	arg1	phosphorylation					716:730	the Tyr phosphorylation	708:730	the Tyr phosphorylation of IRSs	708:738	Two important insulin receptor substrates 1 and 2 are widely expressed in human, and alternative phosphorylation on their serine (Ser) and threonine (Thr) residues has been known to block the Tyr phosphorylation of IRSs, thus inhibiting insulin signaling and promoting insulin resistance.
25580119	2	63	theme	tyrosine	487:494	arg1	residues					502:509	several tyrosine (TYR) residues	479:509	several tyrosine (TYR) residues on IRSs	479:517	Posttranslational modifications (PTMs) regulate functions and interaction of insulin with insulin receptors substrates (IRSs) and activate insulin signaling downstream pathways via autophosphorylation on several tyrosine (TYR) residues on IRSs.
25580119	4	64	theme	Yin	960:962	arg1	Yang					964:967	Yin Yang	960:967	Yin Yang sites	960:973	Like phosphorylation, O-glycosylation modification is important PTM and inhibits phosphorylation on same or neighboring Ser/Thr residues, often called Yin Yang sites.
25580119	2	65	theme	signaling	422:430	arg1	pathways					443:450	insulin signaling downstream pathways	414:450	insulin signaling downstream pathways	414:450	Posttranslational modifications (PTMs) regulate functions and interaction of insulin with insulin receptors substrates (IRSs) and activate insulin signaling downstream pathways via autophosphorylation on several tyrosine (TYR) residues on IRSs.
9136890	11	0	theme	3T3	1336:1338	arg1	cells					1340:1344	mouse 3T3 cells	1330:1344	mouse 3T3 cells	1330:1344	The consensus sequences for each N-linked site were mutated in various combinations and the resultant TfRs expressed in mouse 3T3 cells.
9136890	10	1	theme	FACE	1126:1129	arg1	analysis					1131:1138	FACE analysis	1126:1138	FACE analysis	1126:1138	FACE analysis reveals predominantly a family of sialylated hybrid oligosaccharides.
9136890	13	2	from	Asn	1676:1678	arg1	oliosaccharide					1658:1671	the oliosaccharide	1654:1671	the oliosaccharide at Asn 727	1654:1682	Previous studies indicated that the oliosaccharide at Asn 727 was high-mannose type [Hayes, G. R., et al. (1995) Glycobiology 5, 227-232].
9136890	13	2	from	Asn	1676:1678	arg1	[Hayes					1706:1711	high-mannose type [Hayes	1688:1711	high-mannose type [Hayes	1688:1711	Previous studies indicated that the oliosaccharide at Asn 727 was high-mannose type [Hayes, G. R., et al. (1995) Glycobiology 5, 227-232].
9136890	12	3	theme	mutated	1382:1388	arg1	TfRs					1390:1393	the mutated TfRs	1378:1393	the mutated TfRs	1378:1393	Endoglycosidase H digestion of the mutated TfRs indicates that the pattern of oligosaccharides is consistent with the type of oligosaccharides found at each position in human tissue and the glycosylation of one site does not directly affect the glycosylation of other sites.
9136890	0	4	theme	processing	88:97	arg1	conservation					58:69	conservation	58:69	conservation of site-specific processing	58:97	Structure of human transferrin receptor oligosaccharides: conservation of site-specific processing.
9136890	11	5	link	N-linked	1243:1250	arg1	site					1252:1255	each N-linked site	1238:1255	each N-linked site	1238:1255	The consensus sequences for each N-linked site were mutated in various combinations and the resultant TfRs expressed in mouse 3T3 cells.
9136890	14	6	theme	oligosaccharide	1801:1815	arg1	type					1793:1796	the type	1789:1796	the type of oligosaccharide found at each site	1789:1834	These results indicate that the type of oligosaccharide found at each site is most dependent on the environment surrounding it.
9136890	14	6	theme	oligosaccharide	1801:1815	arg1	dependent					1844:1852	dependent	1844:1852	dependent	1844:1852	These results indicate that the type of oligosaccharide found at each site is most dependent on the environment surrounding it.
9136890	11	7	theme	N-linked	1243:1250	arg1	site					1252:1255	each N-linked site	1238:1255	each N-linked site	1238:1255	The consensus sequences for each N-linked site were mutated in various combinations and the resultant TfRs expressed in mouse 3T3 cells.
9136890	9	8	theme	limited	1087:1093	arg1	digestion					1103:1111	limited tryptic digestion	1087:1111	limited tryptic digestion	1087:1111	The glycopeptide containing the site at Asn 317 was obtained after limited tryptic digestion and RP-HPLC.
9136890	12	9	theme	site	1558:1561	arg1	glycosylation					1537:1549	the glycosylation	1533:1549	the glycosylation of one site	1533:1561	Endoglycosidase H digestion of the mutated TfRs indicates that the pattern of oligosaccharides is consistent with the type of oligosaccharides found at each position in human tissue and the glycosylation of one site does not directly affect the glycosylation of other sites.
9136890	12	10	theme	human	1516:1520	arg1	tissue					1522:1527	human tissue	1516:1527	human tissue	1516:1527	Endoglycosidase H digestion of the mutated TfRs indicates that the pattern of oligosaccharides is consistent with the type of oligosaccharides found at each position in human tissue and the glycosylation of one site does not directly affect the glycosylation of other sites.
9136890	0	11	dep	oligosaccharides	40:55	arg1	conservation					58:69	conservation	58:69	conservation of site-specific processing	58:97	Structure of human transferrin receptor oligosaccharides: conservation of site-specific processing.
9136890	2	12	theme	oligosaccharides	312:327	arg1	structures					285:294	the structures	281:294	the structures of the N-linked oligosaccharides	281:327	A combination of site-directed mutagenesis and carbohydrate and protein chemistry was used to characterize the structures of the N-linked oligosaccharides and to map their locations.
9136890	7	13	theme	complex	901:907	arg1	type					909:912	the complex type	897:912	the complex type	897:912	The oligosaccharides at Asn 251 are of the complex type.
9136890	13	14	theme	Previous	1622:1629	arg1	studies					1631:1637	Previous studies	1622:1637	Previous studies	1622:1637	Previous studies indicated that the oliosaccharide at Asn 727 was high-mannose type [Hayes, G. R., et al. (1995) Glycobiology 5, 227-232].
9136890	11	15	theme	various	1273:1279	arg1	combinations					1281:1292	various combinations	1273:1292	various combinations	1273:1292	The consensus sequences for each N-linked site were mutated in various combinations and the resultant TfRs expressed in mouse 3T3 cells.
9136890	11	16	theme	mouse	1330:1334	arg1	cells					1340:1344	mouse 3T3 cells	1330:1344	mouse 3T3 cells	1330:1344	The consensus sequences for each N-linked site were mutated in various combinations and the resultant TfRs expressed in mouse 3T3 cells.
9136890	6	17	theme	specific	836:843	arg1	residue					849:855	the specific Asn residue	832:855	the specific Asn residue	832:855	Peptides containing carbohydrate were subjected to amino acid sequencing to identify the specific Asn residue.
9136890	2	18	theme	N-linked	303:310	arg1	oligosaccharides					312:327	the N-linked oligosaccharides	299:327	the N-linked oligosaccharides	299:327	A combination of site-directed mutagenesis and carbohydrate and protein chemistry was used to characterize the structures of the N-linked oligosaccharides and to map their locations.
9136890	14	19	located	found	1817:1821	arg1	site					1831:1834	each site	1826:1834	each site	1826:1834	These results indicate that the type of oligosaccharide found at each site is most dependent on the environment surrounding it.
9136890	14	19	located	found	1817:1821	arg2	oligosaccharide					1801:1815	oligosaccharide	1801:1815	oligosaccharide found at each site	1801:1834	These results indicate that the type of oligosaccharide found at each site is most dependent on the environment surrounding it.
9136890	10	20	gly	sialylated	1174:1183	arg1	oligosaccharides					1192:1207	sialylated hybrid oligosaccharides	1174:1207	sialylated hybrid oligosaccharides	1174:1207	FACE analysis reveals predominantly a family of sialylated hybrid oligosaccharides.
9136890	12	21	theme	oligosaccharides	1473:1488	arg1	type					1465:1468	the type	1461:1468	the type of oligosaccharides found at each position in human tissue	1461:1527	Endoglycosidase H digestion of the mutated TfRs indicates that the pattern of oligosaccharides is consistent with the type of oligosaccharides found at each position in human tissue and the glycosylation of one site does not directly affect the glycosylation of other sites.
9136890	5	22	theme	individual	624:633	arg1	peptides					635:642	individual peptides	624:642	individual peptides	624:642	Following digestion of purified TfR with trypsin, individual peptides were obtained via RP-HPLC and were assayed for monosaccharides by strong acid hydrolysis and HPAE-PAD.
9136890	11	23	theme	consensus	1214:1222	arg1	sequences					1224:1232	The consensus sequences	1210:1232	The consensus sequences for each N-linked site	1210:1255	The consensus sequences for each N-linked site were mutated in various combinations and the resultant TfRs expressed in mouse 3T3 cells.
9136890	12	24	theme	TfRs	1390:1393	arg1	digestion					1365:1373	Endoglycosidase H digestion	1347:1373	Endoglycosidase H digestion of the mutated TfRs	1347:1393	Endoglycosidase H digestion of the mutated TfRs indicates that the pattern of oligosaccharides is consistent with the type of oligosaccharides found at each position in human tissue and the glycosylation of one site does not directly affect the glycosylation of other sites.
9136890	12	25	theme	Endoglycosidase	1347:1361	arg1	H					1363:1363	Endoglycosidase H	1347:1363	Endoglycosidase H digestion of the mutated TfRs	1347:1393	Endoglycosidase H digestion of the mutated TfRs indicates that the pattern of oligosaccharides is consistent with the type of oligosaccharides found at each position in human tissue and the glycosylation of one site does not directly affect the glycosylation of other sites.
9136890	8	26	with	triantennary	965:976	arg1	fucosylation					1006:1017	core fucosylation	1001:1017	core fucosylation	1001:1017	HPAE-PAD and FACE analysis suggests that they are triantennary and trisialylated with core fucosylation.
9136890	4	27	attach	isolated	462:469	arg2	TfR					458:460	Human TfR	452:460	Human TfR isolated from placentae	452:484	Human TfR isolated from placentae was used to characterize the structure of the oligosaccharides found in the native TfR.
9136890	4	27	attach	isolated	462:469	arg1	placentae					476:484	placentae	476:484	placentae	476:484	Human TfR isolated from placentae was used to characterize the structure of the oligosaccharides found in the native TfR.
9136890	3	28	from	position	406:413	arg1	unique					419:424	unique	419:424	unique	419:424	We find that the type of oligosaccharide at each position was unique for that particular site.
9136890	3	28	from	position	406:413	arg1	type					374:377	the type	370:377	the type of oligosaccharide at each position	370:413	We find that the type of oligosaccharide at each position was unique for that particular site.
9136890	9	29	gly	glycopeptide	1024:1035	arg2	glycopeptide					1024:1035	The glycopeptide	1020:1035	The glycopeptide containing the site at Asn 317	1020:1066	The glycopeptide containing the site at Asn 317 was obtained after limited tryptic digestion and RP-HPLC.
9136890	12	30	theme	oligosaccharides	1425:1440	arg1	consistent					1445:1454	consistent	1445:1454	consistent	1445:1454	Endoglycosidase H digestion of the mutated TfRs indicates that the pattern of oligosaccharides is consistent with the type of oligosaccharides found at each position in human tissue and the glycosylation of one site does not directly affect the glycosylation of other sites.
9136890	12	30	theme	oligosaccharides	1425:1440	arg1	pattern					1414:1420	the pattern	1410:1420	the pattern of oligosaccharides	1410:1440	Endoglycosidase H digestion of the mutated TfRs indicates that the pattern of oligosaccharides is consistent with the type of oligosaccharides found at each position in human tissue and the glycosylation of one site does not directly affect the glycosylation of other sites.
9136890	3	31	theme	particular	435:444	arg1	site					446:449	that particular site	430:449	that particular site	430:449	We find that the type of oligosaccharide at each position was unique for that particular site.
9136890	12	32	theme	sites	1615:1619	arg1	glycosylation					1592:1604	the glycosylation	1588:1604	the glycosylation of other sites	1588:1619	Endoglycosidase H digestion of the mutated TfRs indicates that the pattern of oligosaccharides is consistent with the type of oligosaccharides found at each position in human tissue and the glycosylation of one site does not directly affect the glycosylation of other sites.
9136890	10	33	theme	sialylated	1174:1183	arg1	oligosaccharides					1192:1207	sialylated hybrid oligosaccharides	1174:1207	sialylated hybrid oligosaccharides	1174:1207	FACE analysis reveals predominantly a family of sialylated hybrid oligosaccharides.
9136890	5	34	theme	purified	597:604	arg1	TfR					606:608	purified TfR	597:608	purified TfR	597:608	Following digestion of purified TfR with trypsin, individual peptides were obtained via RP-HPLC and were assayed for monosaccharides by strong acid hydrolysis and HPAE-PAD.
9136890	1	35	theme	human	104:108	arg1	TfR					132:134	TfR	132:134	TfR	132:134	The human transferrin receptor (TfR) has three N-linked oligosaccharides.
9136890	1	35	theme	human	104:108	arg1	receptor					122:129	The human transferrin receptor	100:129	The human transferrin receptor (TfR)	100:135	The human transferrin receptor (TfR) has three N-linked oligosaccharides.
9136890	12	36	theme	H	1363:1363	arg1	digestion					1365:1373	Endoglycosidase H digestion	1347:1373	Endoglycosidase H digestion of the mutated TfRs	1347:1393	Endoglycosidase H digestion of the mutated TfRs indicates that the pattern of oligosaccharides is consistent with the type of oligosaccharides found at each position in human tissue and the glycosylation of one site does not directly affect the glycosylation of other sites.
9136890	3	37	theme	oligosaccharide	382:396	arg1	unique					419:424	unique	419:424	unique	419:424	We find that the type of oligosaccharide at each position was unique for that particular site.
9136890	3	37	theme	oligosaccharide	382:396	arg1	type					374:377	the type	370:377	the type of oligosaccharide at each position	370:413	We find that the type of oligosaccharide at each position was unique for that particular site.
9136890	4	38	theme	native	562:567	arg1	TfR					569:571	the native TfR	558:571	the native TfR	558:571	Human TfR isolated from placentae was used to characterize the structure of the oligosaccharides found in the native TfR.
9136890	5	39	theme	acid	717:720	arg1	hydrolysis					722:731	strong acid hydrolysis	710:731	strong acid hydrolysis	710:731	Following digestion of purified TfR with trypsin, individual peptides were obtained via RP-HPLC and were assayed for monosaccharides by strong acid hydrolysis and HPAE-PAD.
9136890	5	40	theme	TfR	606:608	arg1	digestion					584:592	digestion	584:592	digestion of purified TfR with trypsin	584:621	Following digestion of purified TfR with trypsin, individual peptides were obtained via RP-HPLC and were assayed for monosaccharides by strong acid hydrolysis and HPAE-PAD.
9136890	1	41	theme	transferrin	110:120	arg1	TfR					132:134	TfR	132:134	TfR	132:134	The human transferrin receptor (TfR) has three N-linked oligosaccharides.
9136890	1	41	theme	transferrin	110:120	arg1	receptor					122:129	The human transferrin receptor	100:129	The human transferrin receptor (TfR)	100:135	The human transferrin receptor (TfR) has three N-linked oligosaccharides.
9136890	12	42	located	found	1490:1494	arg2	oligosaccharides					1473:1488	oligosaccharides	1473:1488	oligosaccharides found at each position in human tissue	1473:1527	Endoglycosidase H digestion of the mutated TfRs indicates that the pattern of oligosaccharides is consistent with the type of oligosaccharides found at each position in human tissue and the glycosylation of one site does not directly affect the glycosylation of other sites.
9136890	12	42	located	found	1490:1494	arg1	position					1504:1511	each position	1499:1511	each position in human tissue	1499:1527	Endoglycosidase H digestion of the mutated TfRs indicates that the pattern of oligosaccharides is consistent with the type of oligosaccharides found at each position in human tissue and the glycosylation of one site does not directly affect the glycosylation of other sites.
9136890	0	43	theme	human	13:17	arg1	receptor					31:38	human transferrin receptor	13:38	human transferrin receptor	13:38	Structure of human transferrin receptor oligosaccharides: conservation of site-specific processing.
9136890	5	44	with	digestion	584:592	arg1	trypsin					615:621	trypsin	615:621	trypsin	615:621	Following digestion of purified TfR with trypsin, individual peptides were obtained via RP-HPLC and were assayed for monosaccharides by strong acid hydrolysis and HPAE-PAD.
9136890	2	45	theme	site-directed	191:203	arg1	mutagenesis					205:215	site-directed mutagenesis	191:215	site-directed mutagenesis	191:215	A combination of site-directed mutagenesis and carbohydrate and protein chemistry was used to characterize the structures of the N-linked oligosaccharides and to map their locations.
9136890	8	46	theme	FACE	928:931	arg1	analysis					933:940	FACE analysis	928:940	FACE analysis	928:940	HPAE-PAD and FACE analysis suggests that they are triantennary and trisialylated with core fucosylation.
9136890	2	47	link	N-linked	303:310	arg1	oligosaccharides					312:327	the N-linked oligosaccharides	299:327	the N-linked oligosaccharides	299:327	A combination of site-directed mutagenesis and carbohydrate and protein chemistry was used to characterize the structures of the N-linked oligosaccharides and to map their locations.
9136890	2	48	used	used	260:263	arg2	combination					176:186	A combination	174:186	A combination of site-directed mutagenesis and carbohydrate and protein chemistry	174:254	A combination of site-directed mutagenesis and carbohydrate and protein chemistry was used to characterize the structures of the N-linked oligosaccharides and to map their locations.
9136890	12	49	gly	glycosylation	1537:1549	arg1	site					1558:1561	one site	1554:1561	one site	1554:1561	Endoglycosidase H digestion of the mutated TfRs indicates that the pattern of oligosaccharides is consistent with the type of oligosaccharides found at each position in human tissue and the glycosylation of one site does not directly affect the glycosylation of other sites.
9136890	12	49	gly	glycosylation	1537:1549	arg1	sites					1615:1619	other sites	1609:1619	other sites	1609:1619	Endoglycosidase H digestion of the mutated TfRs indicates that the pattern of oligosaccharides is consistent with the type of oligosaccharides found at each position in human tissue and the glycosylation of one site does not directly affect the glycosylation of other sites.
9136890	0	50	theme	receptor	31:38	arg1	Structure					0:8	Structure	0:8	Structure of human transferrin receptor	0:38	Structure of human transferrin receptor oligosaccharides: conservation of site-specific processing.
9136890	1	51	link	N-linked	147:154	arg1	oligosaccharides					156:171	three N-linked oligosaccharides	141:171	three N-linked oligosaccharides	141:171	The human transferrin receptor (TfR) has three N-linked oligosaccharides.
9136890	12	52	from	position	1504:1511	arg1	tissue					1522:1527	human tissue	1516:1527	human tissue	1516:1527	Endoglycosidase H digestion of the mutated TfRs indicates that the pattern of oligosaccharides is consistent with the type of oligosaccharides found at each position in human tissue and the glycosylation of one site does not directly affect the glycosylation of other sites.
9136890	0	53	theme	transferrin	19:29	arg1	receptor					31:38	human transferrin receptor	13:38	human transferrin receptor	13:38	Structure of human transferrin receptor oligosaccharides: conservation of site-specific processing.
9136890	6	54	theme	amino	798:802	arg1	sequencing					809:818	amino acid sequencing	798:818	amino acid sequencing	798:818	Peptides containing carbohydrate were subjected to amino acid sequencing to identify the specific Asn residue.
9136890	10	55	theme	hybrid	1185:1190	arg1	oligosaccharides					1192:1207	sialylated hybrid oligosaccharides	1174:1207	sialylated hybrid oligosaccharides	1174:1207	FACE analysis reveals predominantly a family of sialylated hybrid oligosaccharides.
9136890	6	56	contain	containing	756:765	arg2	carbohydrate					767:778	carbohydrate	767:778	carbohydrate	767:778	Peptides containing carbohydrate were subjected to amino acid sequencing to identify the specific Asn residue.
9136890	6	56	contain	containing	756:765	arg1	Peptides					747:754	Peptides	747:754	Peptides containing carbohydrate	747:778	Peptides containing carbohydrate were subjected to amino acid sequencing to identify the specific Asn residue.
9136890	4	57	theme	oligosaccharides	532:547	arg1	structure					515:523	the structure	511:523	the structure of the oligosaccharides found in the native TfR	511:571	Human TfR isolated from placentae was used to characterize the structure of the oligosaccharides found in the native TfR.
9136890	8	58	theme	core	1001:1004	arg1	fucosylation					1006:1017	core fucosylation	1001:1017	core fucosylation	1001:1017	HPAE-PAD and FACE analysis suggests that they are triantennary and trisialylated with core fucosylation.
9136890	2	59	theme	chemistry	246:254	arg1	combination					176:186	A combination	174:186	A combination of site-directed mutagenesis and carbohydrate and protein chemistry	174:254	A combination of site-directed mutagenesis and carbohydrate and protein chemistry was used to characterize the structures of the N-linked oligosaccharides and to map their locations.
9136890	13	60	theme	high-mannose	1688:1699	arg1	oliosaccharide					1658:1671	the oliosaccharide	1654:1671	the oliosaccharide at Asn 727	1654:1682	Previous studies indicated that the oliosaccharide at Asn 727 was high-mannose type [Hayes, G. R., et al. (1995) Glycobiology 5, 227-232].
9136890	13	60	theme	high-mannose	1688:1699	arg1	[Hayes					1706:1711	high-mannose type [Hayes	1688:1711	high-mannose type [Hayes	1688:1711	Previous studies indicated that the oliosaccharide at Asn 727 was high-mannose type [Hayes, G. R., et al. (1995) Glycobiology 5, 227-232].
9136890	13	60	theme	high-mannose	1688:1699	arg1	R.					1717:1718	R.	1717:1718	R.	1717:1718	Previous studies indicated that the oliosaccharide at Asn 727 was high-mannose type [Hayes, G. R., et al. (1995) Glycobiology 5, 227-232].
9136890	4	61	used	used	490:493	arg2	TfR					458:460	Human TfR	452:460	Human TfR isolated from placentae	452:484	Human TfR isolated from placentae was used to characterize the structure of the oligosaccharides found in the native TfR.
9136890	10	62	theme	oligosaccharides	1192:1207	arg1	family					1164:1169	a family	1162:1169	a family of sialylated hybrid oligosaccharides	1162:1207	FACE analysis reveals predominantly a family of sialylated hybrid oligosaccharides.
9136890	2	63	theme	protein	238:244	arg1	chemistry					246:254	carbohydrate and protein chemistry	221:254	carbohydrate and protein chemistry	221:254	A combination of site-directed mutagenesis and carbohydrate and protein chemistry was used to characterize the structures of the N-linked oligosaccharides and to map their locations.
9136890	6	64	theme	acid	804:807	arg1	sequencing					809:818	amino acid sequencing	798:818	amino acid sequencing	798:818	Peptides containing carbohydrate were subjected to amino acid sequencing to identify the specific Asn residue.
9136890	9	65	theme	tryptic	1095:1101	arg1	digestion					1103:1111	limited tryptic digestion	1087:1111	limited tryptic digestion	1087:1111	The glycopeptide containing the site at Asn 317 was obtained after limited tryptic digestion and RP-HPLC.
9136890	2	66	theme	carbohydrate	221:232	arg1	chemistry					246:254	carbohydrate and protein chemistry	221:254	carbohydrate and protein chemistry	221:254	A combination of site-directed mutagenesis and carbohydrate and protein chemistry was used to characterize the structures of the N-linked oligosaccharides and to map their locations.
9136890	7	67	from	Asn	882:884	arg1	oligosaccharides					862:877	The oligosaccharides	858:877	The oligosaccharides at Asn 251	858:888	The oligosaccharides at Asn 251 are of the complex type.
9136890	6	68	theme	Asn	845:847	arg1	residue					849:855	the specific Asn residue	832:855	the specific Asn residue	832:855	Peptides containing carbohydrate were subjected to amino acid sequencing to identify the specific Asn residue.
9136890	4	69	located	found	549:553	arg1	TfR					569:571	the native TfR	558:571	the native TfR	558:571	Human TfR isolated from placentae was used to characterize the structure of the oligosaccharides found in the native TfR.
9136890	4	69	located	found	549:553	arg2	oligosaccharides					532:547	the oligosaccharides	528:547	the oligosaccharides found in the native TfR	528:571	Human TfR isolated from placentae was used to characterize the structure of the oligosaccharides found in the native TfR.
9136890	12	70	theme	other	1609:1613	arg1	sites					1615:1619	other sites	1609:1619	other sites	1609:1619	Endoglycosidase H digestion of the mutated TfRs indicates that the pattern of oligosaccharides is consistent with the type of oligosaccharides found at each position in human tissue and the glycosylation of one site does not directly affect the glycosylation of other sites.
9136890	5	71	theme	strong	710:715	arg1	hydrolysis					722:731	strong acid hydrolysis	710:731	strong acid hydrolysis	710:731	Following digestion of purified TfR with trypsin, individual peptides were obtained via RP-HPLC and were assayed for monosaccharides by strong acid hydrolysis and HPAE-PAD.
9136890	4	72	theme	Human	452:456	arg1	TfR					458:460	Human TfR	452:460	Human TfR isolated from placentae	452:484	Human TfR isolated from placentae was used to characterize the structure of the oligosaccharides found in the native TfR.
9136890	0	73	theme	site-specific	74:86	arg1	processing					88:97	site-specific processing	74:97	site-specific processing	74:97	Structure of human transferrin receptor oligosaccharides: conservation of site-specific processing.
9136890	2	74	theme	mutagenesis	205:215	arg1	combination					176:186	A combination	174:186	A combination of site-directed mutagenesis and carbohydrate and protein chemistry	174:254	A combination of site-directed mutagenesis and carbohydrate and protein chemistry was used to characterize the structures of the N-linked oligosaccharides and to map their locations.
9136890	9	75	contain	containing	1037:1046	arg2	site					1052:1055	the site	1048:1055	the site	1048:1055	The glycopeptide containing the site at Asn 317 was obtained after limited tryptic digestion and RP-HPLC.
9136890	9	75	contain	containing	1037:1046	arg1	glycopeptide					1024:1035	The glycopeptide	1020:1035	The glycopeptide containing the site at Asn 317	1020:1066	The glycopeptide containing the site at Asn 317 was obtained after limited tryptic digestion and RP-HPLC.
9136890	13	76	theme	type	1701:1704	arg1	oliosaccharide					1658:1671	the oliosaccharide	1654:1671	the oliosaccharide at Asn 727	1654:1682	Previous studies indicated that the oliosaccharide at Asn 727 was high-mannose type [Hayes, G. R., et al. (1995) Glycobiology 5, 227-232].
9136890	13	76	theme	type	1701:1704	arg1	[Hayes					1706:1711	high-mannose type [Hayes	1688:1711	high-mannose type [Hayes	1688:1711	Previous studies indicated that the oliosaccharide at Asn 727 was high-mannose type [Hayes, G. R., et al. (1995) Glycobiology 5, 227-232].
9136890	13	76	theme	type	1701:1704	arg1	R.					1717:1718	R.	1717:1718	R.	1717:1718	Previous studies indicated that the oliosaccharide at Asn 727 was high-mannose type [Hayes, G. R., et al. (1995) Glycobiology 5, 227-232].
9136890	13	77	dep	R.	1717:1718	arg1	Glycobiology					1735:1746	Glycobiology	1735:1746	Glycobiology	1735:1746	Previous studies indicated that the oliosaccharide at Asn 727 was high-mannose type [Hayes, G. R., et al. (1995) Glycobiology 5, 227-232].
9136890	1	78	contain	has	137:139	arg2	oligosaccharides					156:171	three N-linked oligosaccharides	141:171	three N-linked oligosaccharides	141:171	The human transferrin receptor (TfR) has three N-linked oligosaccharides.
9136890	1	78	contain	has	137:139	arg1	TfR					132:134	TfR	132:134	TfR	132:134	The human transferrin receptor (TfR) has three N-linked oligosaccharides.
9136890	1	78	contain	has	137:139	arg1	receptor					122:129	The human transferrin receptor	100:129	The human transferrin receptor (TfR)	100:135	The human transferrin receptor (TfR) has three N-linked oligosaccharides.
9136890	12	79	gly	glycosylation	1592:1604	arg1	sites					1615:1619	other sites	1609:1619	other sites	1609:1619	Endoglycosidase H digestion of the mutated TfRs indicates that the pattern of oligosaccharides is consistent with the type of oligosaccharides found at each position in human tissue and the glycosylation of one site does not directly affect the glycosylation of other sites.
9136890	1	80	theme	N-linked	147:154	arg1	oligosaccharides					156:171	three N-linked oligosaccharides	141:171	three N-linked oligosaccharides	141:171	The human transferrin receptor (TfR) has three N-linked oligosaccharides.
9136890	12	81	with	consistent	1445:1454	arg1	type					1465:1468	the type	1461:1468	the type of oligosaccharides found at each position in human tissue	1461:1527	Endoglycosidase H digestion of the mutated TfRs indicates that the pattern of oligosaccharides is consistent with the type of oligosaccharides found at each position in human tissue and the glycosylation of one site does not directly affect the glycosylation of other sites.
9136890	11	82	theme	resultant	1302:1310	arg1	TfRs					1312:1315	the resultant TfRs	1298:1315	the resultant TfRs	1298:1315	The consensus sequences for each N-linked site were mutated in various combinations and the resultant TfRs expressed in mouse 3T3 cells.
12065289	10	0	theme	conserved	1595:1603	arg1	protein					1639:1645	the SLC19A2 protein	1627:1645	the SLC19A2 protein	1627:1645	Results also show conserved TM anionic residue of the SLC19A2 protein is critical for its function.
12065289	10	0	theme	conserved	1595:1603	arg1	residue					1616:1622	conserved TM anionic residue	1595:1622	conserved TM anionic residue of the SLC19A2 protein	1595:1645	Results also show conserved TM anionic residue of the SLC19A2 protein is critical for its function.
12065289	8	1	dep	fraction	1362:1369	arg1	cytoplasmic					1349:1359	cytoplasmic	1349:1359	cytoplasmic	1349:1359	Western blot analysis showed all proteins (except D93H) were expressed in the membrane (not the cytoplasmic) fraction of HeLa cells.
12065289	10	2	theme	SLC19A2	1631:1637	arg1	protein					1639:1645	the SLC19A2 protein	1627:1645	the SLC19A2 protein	1627:1645	Results also show conserved TM anionic residue of the SLC19A2 protein is critical for its function.
12065289	0	3	theme	Functional	0:9	arg1	role					11:14	Functional role	0:14	Functional role of specific amino acid residues in human thiamine transporter SLC19A2	0:84	Functional role of specific amino acid residues in human thiamine transporter SLC19A2: mutational analysis.
12065289	0	4	theme	thiamine	57:64	arg1	SLC19A2					78:84	human thiamine transporter SLC19A2	51:84	human thiamine transporter SLC19A2	51:84	Functional role of specific amino acid residues in human thiamine transporter SLC19A2: mutational analysis.
12065289	1	5	theme	human	177:181	arg1	tract					223:227	the gastrointestinal tract	202:227	the gastrointestinal tract	202:227	SLC19A2 is a membrane thiamine transporter expressed in a variety of human tissues, including the gastrointestinal tract.
12065289	1	5	theme	human	177:181	arg1	tissues					183:189	human tissues	177:189	human tissues	177:189	SLC19A2 is a membrane thiamine transporter expressed in a variety of human tissues, including the gastrointestinal tract.
12065289	4	6	theme	TM	626:627	arg1	domains					630:636	the transmembrane (TM) domains	607:636	the transmembrane (TM) domains of the SLC19A2	607:651	We also examined the effect of mutating the only conserved anionic residue (E138) in the transmembrane (TM) domains of the SLC19A2 and that of the putative glycosylation sites (N63, N314).
12065289	4	6	theme	TM	626:627	arg1	SLC19A2					645:651	the SLC19A2	641:651	the SLC19A2	641:651	We also examined the effect of mutating the only conserved anionic residue (E138) in the transmembrane (TM) domains of the SLC19A2 and that of the putative glycosylation sites (N63, N314).
12065289	3	7	from	mutations	348:356	arg1	SLC19A2					361:367	SLC19A2	361:367	SLC19A2 identical to those found in thiamine-responsive megaloblastic anemia syndrome (TRMA)	361:452	We examined the effect of introducing mutations in SLC19A2 identical to those found in thiamine-responsive megaloblastic anemia syndrome (TRMA), on functional activity and membrane expression of the transporter.
12065289	2	8	theme	SLC19A2	301:307	arg1	relationship					285:296	the structure/function relationship	262:296	the structure/function relationship of SLC19A2	262:307	Little is currently known about the structure/function relationship of SLC19A2.
12065289	5	9	theme	HeLa	789:792	arg1	cells					794:798	HeLa cells	789:798	HeLa cells transfected with wild-type or mutated SLC19A2	789:844	Northern blot analysis showed SLC19A2 mRNA was expressed at the same level in HeLa cells transfected with wild-type or mutated SLC19A2.
12065289	3	10	from	SLC19A2	361:367	arg1	effect					326:331	the effect	322:331	the effect	322:331	We examined the effect of introducing mutations in SLC19A2 identical to those found in thiamine-responsive megaloblastic anemia syndrome (TRMA), on functional activity and membrane expression of the transporter.
12065289	5	11	theme	same	775:778	arg1	level					780:784	the same level	771:784	the same level	771:784	Northern blot analysis showed SLC19A2 mRNA was expressed at the same level in HeLa cells transfected with wild-type or mutated SLC19A2.
12065289	7	12	theme	protein	1244:1250	arg1	weight					1234:1239	apparent molecular weight	1215:1239	apparent molecular weight of protein	1215:1250	Mutations of the two potential N-linked glycosylation sites (N63Q, N314Q) of SLC19A2 did not affect functional activity; they did, however, lead to a noticeable reduction in apparent molecular weight of protein.
12065289	11	13	theme	native	1690:1695	arg1	SLC19A2					1697:1703	native SLC19A2	1690:1703	native SLC19A2	1690:1703	Furthermore, native SLC19A2 is glycosylated, but this is not important for its function.
12065289	8	14	theme	membrane	1331:1338	arg1	fraction					1362:1369	the membrane (not the cytoplasmic) fraction	1327:1369	the membrane (not the cytoplasmic) fraction of HeLa cells	1327:1383	Western blot analysis showed all proteins (except D93H) were expressed in the membrane (not the cytoplasmic) fraction of HeLa cells.
12065289	10	15	dep	show	1590:1593	arg1	critical					1650:1657	critical	1650:1657	critical	1650:1657	Results also show conserved TM anionic residue of the SLC19A2 protein is critical for its function.
12065289	7	16	link	N-linked	1072:1079	arg1	N314Q					1108:1112	N314Q	1108:1112	N314Q	1108:1112	Mutations of the two potential N-linked glycosylation sites (N63Q, N314Q) of SLC19A2 did not affect functional activity; they did, however, lead to a noticeable reduction in apparent molecular weight of protein.
12065289	7	16	link	N-linked	1072:1079	arg1	SLC19A2					1118:1124	SLC19A2	1118:1124	SLC19A2	1118:1124	Mutations of the two potential N-linked glycosylation sites (N63Q, N314Q) of SLC19A2 did not affect functional activity; they did, however, lead to a noticeable reduction in apparent molecular weight of protein.
12065289	7	16	link	N-linked	1072:1079	arg1	sites					1095:1099	the two potential N-linked glycosylation sites	1054:1099	the two potential N-linked glycosylation sites (N63Q, N314Q) of SLC19A2	1054:1124	Mutations of the two potential N-linked glycosylation sites (N63Q, N314Q) of SLC19A2 did not affect functional activity; they did, however, lead to a noticeable reduction in apparent molecular weight of protein.
12065289	1	17	theme	membrane	121:128	arg1	transporter					139:149	a membrane thiamine transporter	119:149	a membrane thiamine transporter expressed in a variety of human tissues, including the gastrointestinal tract	119:227	SLC19A2 is a membrane thiamine transporter expressed in a variety of human tissues, including the gastrointestinal tract.
12065289	1	17	theme	membrane	121:128	arg1	SLC19A2					108:114	SLC19A2	108:114	SLC19A2	108:114	SLC19A2 is a membrane thiamine transporter expressed in a variety of human tissues, including the gastrointestinal tract.
12065289	7	18	theme	apparent	1215:1222	arg1	weight					1234:1239	apparent molecular weight	1215:1239	apparent molecular weight of protein	1215:1250	Mutations of the two potential N-linked glycosylation sites (N63Q, N314Q) of SLC19A2 did not affect functional activity; they did, however, lead to a noticeable reduction in apparent molecular weight of protein.
12065289	5	19	theme	blot	720:723	arg1	analysis					725:732	Northern blot analysis	711:732	Northern blot analysis	711:732	Northern blot analysis showed SLC19A2 mRNA was expressed at the same level in HeLa cells transfected with wild-type or mutated SLC19A2.
12065289	4	20	theme	putative	669:676	arg1	sites					692:696	the putative glycosylation sites	665:696	the putative glycosylation sites (N63, N314)	665:708	We also examined the effect of mutating the only conserved anionic residue (E138) in the transmembrane (TM) domains of the SLC19A2 and that of the putative glycosylation sites (N63, N314).
12065289	4	20	theme	putative	669:676	arg1	N314					704:707	N314	704:707	N314	704:707	We also examined the effect of mutating the only conserved anionic residue (E138) in the transmembrane (TM) domains of the SLC19A2 and that of the putative glycosylation sites (N63, N314).
12065289	0	21	theme	transporter	66:76	arg1	SLC19A2					78:84	human thiamine transporter SLC19A2	51:84	human thiamine transporter SLC19A2	51:84	Functional role of specific amino acid residues in human thiamine transporter SLC19A2: mutational analysis.
12065289	6	22	theme	conserved	933:941	arg1	E138A					960:964	E138A	960:964	E138A	960:964	Introducing the clinically relevant mutations (D93H, S143F, G172D) or mutation at the conserved anionic residue (E138A) of SLC19A2 led to a significant (P < 0.01) inhibition of thiamine uptake.
12065289	6	22	theme	conserved	933:941	arg1	SLC19A2					970:976	SLC19A2	970:976	SLC19A2	970:976	Introducing the clinically relevant mutations (D93H, S143F, G172D) or mutation at the conserved anionic residue (E138A) of SLC19A2 led to a significant (P < 0.01) inhibition of thiamine uptake.
12065289	6	22	theme	conserved	933:941	arg1	residue					951:957	the conserved anionic residue	929:957	the conserved anionic residue (E138A) of SLC19A2	929:976	Introducing the clinically relevant mutations (D93H, S143F, G172D) or mutation at the conserved anionic residue (E138A) of SLC19A2 led to a significant (P < 0.01) inhibition of thiamine uptake.
12065289	10	23	theme	TM	1605:1606	arg1	protein					1639:1645	the SLC19A2 protein	1627:1645	the SLC19A2 protein	1627:1645	Results also show conserved TM anionic residue of the SLC19A2 protein is critical for its function.
12065289	10	23	theme	TM	1605:1606	arg1	residue					1616:1622	conserved TM anionic residue	1595:1622	conserved TM anionic residue of the SLC19A2 protein	1595:1645	Results also show conserved TM anionic residue of the SLC19A2 protein is critical for its function.
12065289	0	24	dep	analysis	98:105	arg1	role					11:14	Functional role	0:14	Functional role of specific amino acid residues in human thiamine transporter SLC19A2	0:84	Functional role of specific amino acid residues in human thiamine transporter SLC19A2: mutational analysis.
12065289	3	25	theme	mutations	348:356	arg1	effect					326:331	the effect	322:331	the effect	322:331	We examined the effect of introducing mutations in SLC19A2 identical to those found in thiamine-responsive megaloblastic anemia syndrome (TRMA), on functional activity and membrane expression of the transporter.
12065289	8	26	theme	HeLa	1374:1377	arg1	cells					1379:1383	HeLa cells	1374:1383	HeLa cells	1374:1383	Western blot analysis showed all proteins (except D93H) were expressed in the membrane (not the cytoplasmic) fraction of HeLa cells.
12065289	5	27	theme	SLC19A2	741:747	arg1	mRNA					749:752	SLC19A2 mRNA	741:752	SLC19A2 mRNA	741:752	Northern blot analysis showed SLC19A2 mRNA was expressed at the same level in HeLa cells transfected with wild-type or mutated SLC19A2.
12065289	7	28	theme	SLC19A2	1118:1124	arg1	N314Q					1108:1112	N314Q	1108:1112	N314Q	1108:1112	Mutations of the two potential N-linked glycosylation sites (N63Q, N314Q) of SLC19A2 did not affect functional activity; they did, however, lead to a noticeable reduction in apparent molecular weight of protein.
12065289	7	28	theme	SLC19A2	1118:1124	arg1	SLC19A2					1118:1124	SLC19A2	1118:1124	SLC19A2	1118:1124	Mutations of the two potential N-linked glycosylation sites (N63Q, N314Q) of SLC19A2 did not affect functional activity; they did, however, lead to a noticeable reduction in apparent molecular weight of protein.
12065289	7	28	theme	SLC19A2	1118:1124	arg1	sites					1095:1099	the two potential N-linked glycosylation sites	1054:1099	the two potential N-linked glycosylation sites (N63Q, N314Q) of SLC19A2	1054:1124	Mutations of the two potential N-linked glycosylation sites (N63Q, N314Q) of SLC19A2 did not affect functional activity; they did, however, lead to a noticeable reduction in apparent molecular weight of protein.
12065289	6	29	dep	significant	987:997	arg1	<					1002:1002	P < 0.01	1000:1007	P < 0.01	1000:1007	Introducing the clinically relevant mutations (D93H, S143F, G172D) or mutation at the conserved anionic residue (E138A) of SLC19A2 led to a significant (P < 0.01) inhibition of thiamine uptake.
12065289	7	30	theme	sites	1095:1099	arg1	Mutations					1041:1049	Mutations	1041:1049	Mutations of the two potential N-linked glycosylation sites (N63Q, N314Q) of SLC19A2	1041:1124	Mutations of the two potential N-linked glycosylation sites (N63Q, N314Q) of SLC19A2 did not affect functional activity; they did, however, lead to a noticeable reduction in apparent molecular weight of protein.
12065289	7	31	theme	noticeable	1191:1200	arg1	reduction					1202:1210	a noticeable reduction	1189:1210	a noticeable reduction in apparent molecular weight of protein	1189:1250	Mutations of the two potential N-linked glycosylation sites (N63Q, N314Q) of SLC19A2 did not affect functional activity; they did, however, lead to a noticeable reduction in apparent molecular weight of protein.
12065289	8	32	theme	blot	1261:1264	arg1	analysis					1266:1273	Western blot analysis	1253:1273	Western blot analysis	1253:1273	Western blot analysis showed all proteins (except D93H) were expressed in the membrane (not the cytoplasmic) fraction of HeLa cells.
12065289	7	33	theme	N-linked	1072:1079	arg1	N314Q					1108:1112	N314Q	1108:1112	N314Q	1108:1112	Mutations of the two potential N-linked glycosylation sites (N63Q, N314Q) of SLC19A2 did not affect functional activity; they did, however, lead to a noticeable reduction in apparent molecular weight of protein.
12065289	7	33	theme	N-linked	1072:1079	arg1	SLC19A2					1118:1124	SLC19A2	1118:1124	SLC19A2	1118:1124	Mutations of the two potential N-linked glycosylation sites (N63Q, N314Q) of SLC19A2 did not affect functional activity; they did, however, lead to a noticeable reduction in apparent molecular weight of protein.
12065289	7	33	theme	N-linked	1072:1079	arg1	sites					1095:1099	the two potential N-linked glycosylation sites	1054:1099	the two potential N-linked glycosylation sites (N63Q, N314Q) of SLC19A2	1054:1124	Mutations of the two potential N-linked glycosylation sites (N63Q, N314Q) of SLC19A2 did not affect functional activity; they did, however, lead to a noticeable reduction in apparent molecular weight of protein.
12065289	3	34	theme	anemia	431:436	arg1	TRMA					448:451	TRMA	448:451	TRMA	448:451	We examined the effect of introducing mutations in SLC19A2 identical to those found in thiamine-responsive megaloblastic anemia syndrome (TRMA), on functional activity and membrane expression of the transporter.
12065289	3	34	theme	anemia	431:436	arg1	syndrome					438:445	thiamine-responsive megaloblastic anemia syndrome	397:445	thiamine-responsive megaloblastic anemia syndrome (TRMA)	397:452	We examined the effect of introducing mutations in SLC19A2 identical to those found in thiamine-responsive megaloblastic anemia syndrome (TRMA), on functional activity and membrane expression of the transporter.
12065289	11	35	gly	glycosylated	1708:1719	arg1	SLC19A2					1697:1703	native SLC19A2	1690:1703	native SLC19A2	1690:1703	Furthermore, native SLC19A2 is glycosylated, but this is not important for its function.
12065289	0	36	theme	amino	28:32	arg1	residues					39:46	specific amino acid residues	19:46	specific amino acid residues	19:46	Functional role of specific amino acid residues in human thiamine transporter SLC19A2: mutational analysis.
12065289	3	37	theme	thiamine-responsive	397:415	arg1	anemia					431:436	thiamine-responsive megaloblastic anemia	397:436	thiamine-responsive megaloblastic anemia syndrome (TRMA)	397:452	We examined the effect of introducing mutations in SLC19A2 identical to those found in thiamine-responsive megaloblastic anemia syndrome (TRMA), on functional activity and membrane expression of the transporter.
12065289	0	38	theme	human	51:55	arg1	SLC19A2					78:84	human thiamine transporter SLC19A2	51:84	human thiamine transporter SLC19A2	51:84	Functional role of specific amino acid residues in human thiamine transporter SLC19A2: mutational analysis.
12065289	0	39	theme	residues	39:46	arg1	role					11:14	Functional role	0:14	Functional role of specific amino acid residues in human thiamine transporter SLC19A2	0:84	Functional role of specific amino acid residues in human thiamine transporter SLC19A2: mutational analysis.
12065289	6	40	theme	uptake	1033:1038	arg1	inhibition					1010:1019	a significant (P < 0.01) inhibition	985:1019	a significant (P < 0.01) inhibition of thiamine uptake	985:1038	Introducing the clinically relevant mutations (D93H, S143F, G172D) or mutation at the conserved anionic residue (E138A) of SLC19A2 led to a significant (P < 0.01) inhibition of thiamine uptake.
12065289	3	41	theme	membrane	482:489	arg1	expression					491:500	membrane expression	482:500	membrane expression	482:500	We examined the effect of introducing mutations in SLC19A2 identical to those found in thiamine-responsive megaloblastic anemia syndrome (TRMA), on functional activity and membrane expression of the transporter.
12065289	1	42	theme	gastrointestinal	206:221	arg1	tract					223:227	the gastrointestinal tract	202:227	the gastrointestinal tract	202:227	SLC19A2 is a membrane thiamine transporter expressed in a variety of human tissues, including the gastrointestinal tract.
12065289	7	43	from	reduction	1202:1210	arg1	weight					1234:1239	apparent molecular weight	1215:1239	apparent molecular weight of protein	1215:1250	Mutations of the two potential N-linked glycosylation sites (N63Q, N314Q) of SLC19A2 did not affect functional activity; they did, however, lead to a noticeable reduction in apparent molecular weight of protein.
12065289	3	44	theme	transporter	509:519	arg1	activity					469:476	functional activity	458:476	functional activity	458:476	We examined the effect of introducing mutations in SLC19A2 identical to those found in thiamine-responsive megaloblastic anemia syndrome (TRMA), on functional activity and membrane expression of the transporter.
12065289	3	44	theme	transporter	509:519	arg1	expression					491:500	membrane expression	482:500	membrane expression	482:500	We examined the effect of introducing mutations in SLC19A2 identical to those found in thiamine-responsive megaloblastic anemia syndrome (TRMA), on functional activity and membrane expression of the transporter.
12065289	6	45	theme	relevant	874:881	arg1	mutations					883:891	the clinically relevant mutations	859:891	the clinically relevant mutations (D93H, S143F, G172D)	859:912	Introducing the clinically relevant mutations (D93H, S143F, G172D) or mutation at the conserved anionic residue (E138A) of SLC19A2 led to a significant (P < 0.01) inhibition of thiamine uptake.
12065289	6	45	theme	relevant	874:881	arg1	G172D					907:911	G172D	907:911	G172D	907:911	Introducing the clinically relevant mutations (D93H, S143F, G172D) or mutation at the conserved anionic residue (E138A) of SLC19A2 led to a significant (P < 0.01) inhibition of thiamine uptake.
12065289	9	46	theme	transporter	1519:1529	arg1	malfunctioning					1497:1510	malfunctioning	1497:1510	malfunctioning of the transporter	1497:1529	These results provide direct confirmation that clinically relevant mutations in SLC19A2 observed in TRMA cause malfunctioning of the transporter and/or a defect in its translation/stability.
12065289	4	47	theme	anionic	581:587	arg1	E138					598:601	E138	598:601	E138	598:601	We also examined the effect of mutating the only conserved anionic residue (E138) in the transmembrane (TM) domains of the SLC19A2 and that of the putative glycosylation sites (N63, N314).
12065289	4	47	theme	anionic	581:587	arg1	residue					589:595	the only conserved anionic residue	562:595	the only conserved anionic residue (E138) in the transmembrane (TM) domains of the SLC19A2	562:651	We also examined the effect of mutating the only conserved anionic residue (E138) in the transmembrane (TM) domains of the SLC19A2 and that of the putative glycosylation sites (N63, N314).
12065289	10	48	theme	protein	1639:1645	arg1	protein					1639:1645	the SLC19A2 protein	1627:1645	the SLC19A2 protein	1627:1645	Results also show conserved TM anionic residue of the SLC19A2 protein is critical for its function.
12065289	10	48	theme	protein	1639:1645	arg1	residue					1616:1622	conserved TM anionic residue	1595:1622	conserved TM anionic residue of the SLC19A2 protein	1595:1645	Results also show conserved TM anionic residue of the SLC19A2 protein is critical for its function.
12065289	2	49	theme	structure/function	266:283	arg1	relationship					285:296	the structure/function relationship	262:296	the structure/function relationship of SLC19A2	262:307	Little is currently known about the structure/function relationship of SLC19A2.
12065289	4	50	theme	SLC19A2	645:651	arg1	domains					630:636	the transmembrane (TM) domains	607:636	the transmembrane (TM) domains of the SLC19A2	607:651	We also examined the effect of mutating the only conserved anionic residue (E138) in the transmembrane (TM) domains of the SLC19A2 and that of the putative glycosylation sites (N63, N314).
12065289	4	50	theme	SLC19A2	645:651	arg1	SLC19A2					645:651	the SLC19A2	641:651	the SLC19A2	641:651	We also examined the effect of mutating the only conserved anionic residue (E138) in the transmembrane (TM) domains of the SLC19A2 and that of the putative glycosylation sites (N63, N314).
12065289	4	51	gly	glycosylation	678:690	arg2	sites					692:696	the putative glycosylation sites	665:696	the putative glycosylation sites (N63, N314)	665:708	We also examined the effect of mutating the only conserved anionic residue (E138) in the transmembrane (TM) domains of the SLC19A2 and that of the putative glycosylation sites (N63, N314).
12065289	4	51	gly	glycosylation	678:690	arg2	N314					704:707	N314	704:707	N314	704:707	We also examined the effect of mutating the only conserved anionic residue (E138) in the transmembrane (TM) domains of the SLC19A2 and that of the putative glycosylation sites (N63, N314).
12065289	1	52	theme	tissues	183:189	arg1	variety					166:172	a variety	164:172	a variety of human tissues, including the gastrointestinal tract	164:227	SLC19A2 is a membrane thiamine transporter expressed in a variety of human tissues, including the gastrointestinal tract.
12065289	1	52	theme	tissues	183:189	arg1	tissues					183:189	human tissues	177:189	human tissues	177:189	SLC19A2 is a membrane thiamine transporter expressed in a variety of human tissues, including the gastrointestinal tract.
12065289	1	52	theme	tissues	183:189	arg1	tract					223:227	the gastrointestinal tract	202:227	the gastrointestinal tract	202:227	SLC19A2 is a membrane thiamine transporter expressed in a variety of human tissues, including the gastrointestinal tract.
12065289	9	53	from	defect	1540:1545	arg1	translation/stability					1554:1574	its translation/stability	1550:1574	its translation/stability	1550:1574	These results provide direct confirmation that clinically relevant mutations in SLC19A2 observed in TRMA cause malfunctioning of the transporter and/or a defect in its translation/stability.
12065289	5	54	dep	showed	734:739	arg1	expressed					758:766	expressed	758:766	showed SLC19A2 mRNA was expressed at the same level in HeLa cells transfected with wild-type or mutated SLC19A2	734:844	Northern blot analysis showed SLC19A2 mRNA was expressed at the same level in HeLa cells transfected with wild-type or mutated SLC19A2.
12065289	5	55	theme	mutated	830:836	arg1	SLC19A2					838:844	mutated SLC19A2	830:844	mutated SLC19A2	830:844	Northern blot analysis showed SLC19A2 mRNA was expressed at the same level in HeLa cells transfected with wild-type or mutated SLC19A2.
12065289	4	56	theme	glycosylation	678:690	arg1	sites					692:696	the putative glycosylation sites	665:696	the putative glycosylation sites (N63, N314)	665:708	We also examined the effect of mutating the only conserved anionic residue (E138) in the transmembrane (TM) domains of the SLC19A2 and that of the putative glycosylation sites (N63, N314).
12065289	4	56	theme	glycosylation	678:690	arg1	N314					704:707	N314	704:707	N314	704:707	We also examined the effect of mutating the only conserved anionic residue (E138) in the transmembrane (TM) domains of the SLC19A2 and that of the putative glycosylation sites (N63, N314).
12065289	7	57	theme	potential	1062:1070	arg1	N314Q					1108:1112	N314Q	1108:1112	N314Q	1108:1112	Mutations of the two potential N-linked glycosylation sites (N63Q, N314Q) of SLC19A2 did not affect functional activity; they did, however, lead to a noticeable reduction in apparent molecular weight of protein.
12065289	7	57	theme	potential	1062:1070	arg1	SLC19A2					1118:1124	SLC19A2	1118:1124	SLC19A2	1118:1124	Mutations of the two potential N-linked glycosylation sites (N63Q, N314Q) of SLC19A2 did not affect functional activity; they did, however, lead to a noticeable reduction in apparent molecular weight of protein.
12065289	7	57	theme	potential	1062:1070	arg1	sites					1095:1099	the two potential N-linked glycosylation sites	1054:1099	the two potential N-linked glycosylation sites (N63Q, N314Q) of SLC19A2	1054:1124	Mutations of the two potential N-linked glycosylation sites (N63Q, N314Q) of SLC19A2 did not affect functional activity; they did, however, lead to a noticeable reduction in apparent molecular weight of protein.
12065289	3	58	from	effect	326:331	arg1	activity					469:476	functional activity	458:476	functional activity	458:476	We examined the effect of introducing mutations in SLC19A2 identical to those found in thiamine-responsive megaloblastic anemia syndrome (TRMA), on functional activity and membrane expression of the transporter.
12065289	3	58	from	effect	326:331	arg1	SLC19A2					361:367	SLC19A2	361:367	SLC19A2 identical to those found in thiamine-responsive megaloblastic anemia syndrome (TRMA)	361:452	We examined the effect of introducing mutations in SLC19A2 identical to those found in thiamine-responsive megaloblastic anemia syndrome (TRMA), on functional activity and membrane expression of the transporter.
12065289	3	58	from	effect	326:331	arg1	expression					491:500	membrane expression	482:500	membrane expression	482:500	We examined the effect of introducing mutations in SLC19A2 identical to those found in thiamine-responsive megaloblastic anemia syndrome (TRMA), on functional activity and membrane expression of the transporter.
12065289	9	59	from	mutations	1453:1461	arg1	SLC19A2					1466:1472	SLC19A2	1466:1472	SLC19A2 observed in TRMA	1466:1489	These results provide direct confirmation that clinically relevant mutations in SLC19A2 observed in TRMA cause malfunctioning of the transporter and/or a defect in its translation/stability.
12065289	5	60	theme	Northern	711:718	arg1	analysis					725:732	Northern blot analysis	711:732	Northern blot analysis	711:732	Northern blot analysis showed SLC19A2 mRNA was expressed at the same level in HeLa cells transfected with wild-type or mutated SLC19A2.
12065289	1	61	theme	thiamine	130:137	arg1	transporter					139:149	a membrane thiamine transporter	119:149	a membrane thiamine transporter expressed in a variety of human tissues, including the gastrointestinal tract	119:227	SLC19A2 is a membrane thiamine transporter expressed in a variety of human tissues, including the gastrointestinal tract.
12065289	1	61	theme	thiamine	130:137	arg1	SLC19A2					108:114	SLC19A2	108:114	SLC19A2	108:114	SLC19A2 is a membrane thiamine transporter expressed in a variety of human tissues, including the gastrointestinal tract.
12065289	3	62	theme	introducing	336:346	arg1	mutations					348:356	introducing mutations	336:356	introducing mutations in SLC19A2 identical to those found in thiamine-responsive megaloblastic anemia syndrome (TRMA)	336:452	We examined the effect of introducing mutations in SLC19A2 identical to those found in thiamine-responsive megaloblastic anemia syndrome (TRMA), on functional activity and membrane expression of the transporter.
12065289	7	63	theme	molecular	1224:1232	arg1	weight					1234:1239	apparent molecular weight	1215:1239	apparent molecular weight of protein	1215:1250	Mutations of the two potential N-linked glycosylation sites (N63Q, N314Q) of SLC19A2 did not affect functional activity; they did, however, lead to a noticeable reduction in apparent molecular weight of protein.
12065289	8	64	dep	showed	1275:1280	arg1	expressed					1314:1322	expressed	1314:1322	showed all proteins (except D93H) were expressed in the membrane (not the cytoplasmic) fraction of HeLa cells	1275:1383	Western blot analysis showed all proteins (except D93H) were expressed in the membrane (not the cytoplasmic) fraction of HeLa cells.
12065289	6	65	theme	anionic	943:949	arg1	E138A					960:964	E138A	960:964	E138A	960:964	Introducing the clinically relevant mutations (D93H, S143F, G172D) or mutation at the conserved anionic residue (E138A) of SLC19A2 led to a significant (P < 0.01) inhibition of thiamine uptake.
12065289	6	65	theme	anionic	943:949	arg1	SLC19A2					970:976	SLC19A2	970:976	SLC19A2	970:976	Introducing the clinically relevant mutations (D93H, S143F, G172D) or mutation at the conserved anionic residue (E138A) of SLC19A2 led to a significant (P < 0.01) inhibition of thiamine uptake.
12065289	6	65	theme	anionic	943:949	arg1	residue					951:957	the conserved anionic residue	929:957	the conserved anionic residue (E138A) of SLC19A2	929:976	Introducing the clinically relevant mutations (D93H, S143F, G172D) or mutation at the conserved anionic residue (E138A) of SLC19A2 led to a significant (P < 0.01) inhibition of thiamine uptake.
12065289	0	66	from	role	11:14	arg1	SLC19A2					78:84	human thiamine transporter SLC19A2	51:84	human thiamine transporter SLC19A2	51:84	Functional role of specific amino acid residues in human thiamine transporter SLC19A2: mutational analysis.
12065289	6	67	from	residue	951:957	arg1	mutations					883:891	the clinically relevant mutations	859:891	the clinically relevant mutations (D93H, S143F, G172D)	859:912	Introducing the clinically relevant mutations (D93H, S143F, G172D) or mutation at the conserved anionic residue (E138A) of SLC19A2 led to a significant (P < 0.01) inhibition of thiamine uptake.
12065289	6	67	from	residue	951:957	arg1	G172D					907:911	G172D	907:911	G172D	907:911	Introducing the clinically relevant mutations (D93H, S143F, G172D) or mutation at the conserved anionic residue (E138A) of SLC19A2 led to a significant (P < 0.01) inhibition of thiamine uptake.
12065289	6	67	from	residue	951:957	arg1	mutation					917:924	mutation	917:924	mutation at the conserved anionic residue (E138A) of SLC19A2	917:976	Introducing the clinically relevant mutations (D93H, S143F, G172D) or mutation at the conserved anionic residue (E138A) of SLC19A2 led to a significant (P < 0.01) inhibition of thiamine uptake.
12065289	0	68	theme	mutational	87:96	arg1	analysis					98:105	mutational analysis	87:105	mutational analysis	87:105	Functional role of specific amino acid residues in human thiamine transporter SLC19A2: mutational analysis.
12065289	3	69	theme	identical	369:377	arg1	SLC19A2					361:367	SLC19A2	361:367	SLC19A2 identical to those found in thiamine-responsive megaloblastic anemia syndrome (TRMA)	361:452	We examined the effect of introducing mutations in SLC19A2 identical to those found in thiamine-responsive megaloblastic anemia syndrome (TRMA), on functional activity and membrane expression of the transporter.
12065289	8	70	theme	cells	1379:1383	arg1	fraction					1362:1369	the membrane (not the cytoplasmic) fraction	1327:1369	the membrane (not the cytoplasmic) fraction of HeLa cells	1327:1383	Western blot analysis showed all proteins (except D93H) were expressed in the membrane (not the cytoplasmic) fraction of HeLa cells.
12065289	4	71	from	residue	589:595	arg1	domains					630:636	the transmembrane (TM) domains	607:636	the transmembrane (TM) domains of the SLC19A2	607:651	We also examined the effect of mutating the only conserved anionic residue (E138) in the transmembrane (TM) domains of the SLC19A2 and that of the putative glycosylation sites (N63, N314).
12065289	4	71	from	residue	589:595	arg1	SLC19A2					645:651	the SLC19A2	641:651	the SLC19A2	641:651	We also examined the effect of mutating the only conserved anionic residue (E138) in the transmembrane (TM) domains of the SLC19A2 and that of the putative glycosylation sites (N63, N314).
12065289	9	72	theme	direct	1408:1413	arg1	confirmation					1415:1426	direct confirmation that clinically relevant mutations in SLC19A2 observed in TRMA cause malfunctioning of the transporter and/or a defect in its translation/stability	1408:1574	direct confirmation that clinically relevant mutations in SLC19A2 observed in TRMA cause malfunctioning of the transporter and/or a defect in its translation/stability	1408:1574	These results provide direct confirmation that clinically relevant mutations in SLC19A2 observed in TRMA cause malfunctioning of the transporter and/or a defect in its translation/stability.
12065289	6	73	theme	P	1000:1000	arg1	<					1002:1002	P < 0.01	1000:1007	P < 0.01	1000:1007	Introducing the clinically relevant mutations (D93H, S143F, G172D) or mutation at the conserved anionic residue (E138A) of SLC19A2 led to a significant (P < 0.01) inhibition of thiamine uptake.
12065289	7	74	theme	glycosylation	1081:1093	arg1	N314Q					1108:1112	N314Q	1108:1112	N314Q	1108:1112	Mutations of the two potential N-linked glycosylation sites (N63Q, N314Q) of SLC19A2 did not affect functional activity; they did, however, lead to a noticeable reduction in apparent molecular weight of protein.
12065289	7	74	theme	glycosylation	1081:1093	arg1	SLC19A2					1118:1124	SLC19A2	1118:1124	SLC19A2	1118:1124	Mutations of the two potential N-linked glycosylation sites (N63Q, N314Q) of SLC19A2 did not affect functional activity; they did, however, lead to a noticeable reduction in apparent molecular weight of protein.
12065289	7	74	theme	glycosylation	1081:1093	arg1	sites					1095:1099	the two potential N-linked glycosylation sites	1054:1099	the two potential N-linked glycosylation sites (N63Q, N314Q) of SLC19A2	1054:1124	Mutations of the two potential N-linked glycosylation sites (N63Q, N314Q) of SLC19A2 did not affect functional activity; they did, however, lead to a noticeable reduction in apparent molecular weight of protein.
12065289	6	75	theme	significant	987:997	arg1	inhibition					1010:1019	a significant (P < 0.01) inhibition	985:1019	a significant (P < 0.01) inhibition of thiamine uptake	985:1038	Introducing the clinically relevant mutations (D93H, S143F, G172D) or mutation at the conserved anionic residue (E138A) of SLC19A2 led to a significant (P < 0.01) inhibition of thiamine uptake.
12065289	0	76	theme	specific	19:26	arg1	residues					39:46	specific amino acid residues	19:46	specific amino acid residues	19:46	Functional role of specific amino acid residues in human thiamine transporter SLC19A2: mutational analysis.
12065289	9	77	theme	relevant	1444:1451	arg1	mutations					1453:1461	clinically relevant mutations	1433:1461	clinically relevant mutations in SLC19A2 observed in TRMA	1433:1489	These results provide direct confirmation that clinically relevant mutations in SLC19A2 observed in TRMA cause malfunctioning of the transporter and/or a defect in its translation/stability.
12065289	9	78	located	observed	1474:1481	arg2	SLC19A2					1466:1472	SLC19A2	1466:1472	SLC19A2 observed in TRMA	1466:1489	These results provide direct confirmation that clinically relevant mutations in SLC19A2 observed in TRMA cause malfunctioning of the transporter and/or a defect in its translation/stability.
12065289	9	78	located	observed	1474:1481	arg1	TRMA					1486:1489	TRMA	1486:1489	TRMA	1486:1489	These results provide direct confirmation that clinically relevant mutations in SLC19A2 observed in TRMA cause malfunctioning of the transporter and/or a defect in its translation/stability.
12065289	4	79	theme	conserved	571:579	arg1	E138					598:601	E138	598:601	E138	598:601	We also examined the effect of mutating the only conserved anionic residue (E138) in the transmembrane (TM) domains of the SLC19A2 and that of the putative glycosylation sites (N63, N314).
12065289	4	79	theme	conserved	571:579	arg1	residue					589:595	the only conserved anionic residue	562:595	the only conserved anionic residue (E138) in the transmembrane (TM) domains of the SLC19A2	562:651	We also examined the effect of mutating the only conserved anionic residue (E138) in the transmembrane (TM) domains of the SLC19A2 and that of the putative glycosylation sites (N63, N314).
12065289	8	80	theme	Western	1253:1259	arg1	analysis					1266:1273	Western blot analysis	1253:1273	Western blot analysis	1253:1273	Western blot analysis showed all proteins (except D93H) were expressed in the membrane (not the cytoplasmic) fraction of HeLa cells.
12065289	0	81	theme	acid	34:37	arg1	residues					39:46	specific amino acid residues	19:46	specific amino acid residues	19:46	Functional role of specific amino acid residues in human thiamine transporter SLC19A2: mutational analysis.
12065289	6	82	theme	SLC19A2	970:976	arg1	E138A					960:964	E138A	960:964	E138A	960:964	Introducing the clinically relevant mutations (D93H, S143F, G172D) or mutation at the conserved anionic residue (E138A) of SLC19A2 led to a significant (P < 0.01) inhibition of thiamine uptake.
12065289	6	82	theme	SLC19A2	970:976	arg1	SLC19A2					970:976	SLC19A2	970:976	SLC19A2	970:976	Introducing the clinically relevant mutations (D93H, S143F, G172D) or mutation at the conserved anionic residue (E138A) of SLC19A2 led to a significant (P < 0.01) inhibition of thiamine uptake.
12065289	6	82	theme	SLC19A2	970:976	arg1	residue					951:957	the conserved anionic residue	929:957	the conserved anionic residue (E138A) of SLC19A2	929:976	Introducing the clinically relevant mutations (D93H, S143F, G172D) or mutation at the conserved anionic residue (E138A) of SLC19A2 led to a significant (P < 0.01) inhibition of thiamine uptake.
12065289	3	83	theme	functional	458:467	arg1	activity					469:476	functional activity	458:476	functional activity	458:476	We examined the effect of introducing mutations in SLC19A2 identical to those found in thiamine-responsive megaloblastic anemia syndrome (TRMA), on functional activity and membrane expression of the transporter.
12065289	3	84	theme	megaloblastic	417:429	arg1	anemia					431:436	thiamine-responsive megaloblastic anemia	397:436	thiamine-responsive megaloblastic anemia syndrome (TRMA)	397:452	We examined the effect of introducing mutations in SLC19A2 identical to those found in thiamine-responsive megaloblastic anemia syndrome (TRMA), on functional activity and membrane expression of the transporter.
12065289	3	85	located	found	388:392	arg1	TRMA					448:451	TRMA	448:451	TRMA	448:451	We examined the effect of introducing mutations in SLC19A2 identical to those found in thiamine-responsive megaloblastic anemia syndrome (TRMA), on functional activity and membrane expression of the transporter.
12065289	3	85	located	found	388:392	arg2	those					382:386	those	382:386	those	382:386	We examined the effect of introducing mutations in SLC19A2 identical to those found in thiamine-responsive megaloblastic anemia syndrome (TRMA), on functional activity and membrane expression of the transporter.
12065289	3	85	located	found	388:392	arg1	syndrome					438:445	thiamine-responsive megaloblastic anemia syndrome	397:445	thiamine-responsive megaloblastic anemia syndrome (TRMA)	397:452	We examined the effect of introducing mutations in SLC19A2 identical to those found in thiamine-responsive megaloblastic anemia syndrome (TRMA), on functional activity and membrane expression of the transporter.
12065289	6	86	theme	thiamine	1024:1031	arg1	uptake					1033:1038	thiamine uptake	1024:1038	thiamine uptake	1024:1038	Introducing the clinically relevant mutations (D93H, S143F, G172D) or mutation at the conserved anionic residue (E138A) of SLC19A2 led to a significant (P < 0.01) inhibition of thiamine uptake.
12065289	7	87	gly	glycosylation	1081:1093	arg2	sites					1095:1099	the two potential N-linked glycosylation sites	1054:1099	the two potential N-linked glycosylation sites (N63Q, N314Q) of SLC19A2	1054:1124	Mutations of the two potential N-linked glycosylation sites (N63Q, N314Q) of SLC19A2 did not affect functional activity; they did, however, lead to a noticeable reduction in apparent molecular weight of protein.
12065289	7	87	gly	glycosylation	1081:1093	arg2	two					1058:1060	two	1058:1060	two	1058:1060	Mutations of the two potential N-linked glycosylation sites (N63Q, N314Q) of SLC19A2 did not affect functional activity; they did, however, lead to a noticeable reduction in apparent molecular weight of protein.
12065289	7	87	gly	glycosylation	1081:1093	arg2	SLC19A2					1118:1124	SLC19A2	1118:1124	SLC19A2	1118:1124	Mutations of the two potential N-linked glycosylation sites (N63Q, N314Q) of SLC19A2 did not affect functional activity; they did, however, lead to a noticeable reduction in apparent molecular weight of protein.
12065289	7	87	gly	glycosylation	1081:1093	arg2	N314Q					1108:1112	N314Q	1108:1112	N314Q	1108:1112	Mutations of the two potential N-linked glycosylation sites (N63Q, N314Q) of SLC19A2 did not affect functional activity; they did, however, lead to a noticeable reduction in apparent molecular weight of protein.
12065289	7	87	gly	glycosylation	1081:1093	arg1	SLC19A2					1118:1124	SLC19A2	1118:1124	SLC19A2	1118:1124	Mutations of the two potential N-linked glycosylation sites (N63Q, N314Q) of SLC19A2 did not affect functional activity; they did, however, lead to a noticeable reduction in apparent molecular weight of protein.
12065289	7	88	theme	functional	1141:1150	arg1	activity					1152:1159	functional activity	1141:1159	functional activity	1141:1159	Mutations of the two potential N-linked glycosylation sites (N63Q, N314Q) of SLC19A2 did not affect functional activity; they did, however, lead to a noticeable reduction in apparent molecular weight of protein.
12065289	4	89	theme	transmembrane	611:623	arg1	domains					630:636	the transmembrane (TM) domains	607:636	the transmembrane (TM) domains of the SLC19A2	607:651	We also examined the effect of mutating the only conserved anionic residue (E138) in the transmembrane (TM) domains of the SLC19A2 and that of the putative glycosylation sites (N63, N314).
12065289	4	89	theme	transmembrane	611:623	arg1	SLC19A2					645:651	the SLC19A2	641:651	the SLC19A2	641:651	We also examined the effect of mutating the only conserved anionic residue (E138) in the transmembrane (TM) domains of the SLC19A2 and that of the putative glycosylation sites (N63, N314).
12065289	10	90	theme	anionic	1608:1614	arg1	protein					1639:1645	the SLC19A2 protein	1627:1645	the SLC19A2 protein	1627:1645	Results also show conserved TM anionic residue of the SLC19A2 protein is critical for its function.
12065289	10	90	theme	anionic	1608:1614	arg1	residue					1616:1622	conserved TM anionic residue	1595:1622	conserved TM anionic residue of the SLC19A2 protein	1595:1645	Results also show conserved TM anionic residue of the SLC19A2 protein is critical for its function.
18203274	8	0	theme	monosialylated	989:1002	arg1	N-glycans					1004:1012	monosialylated N-glycans	989:1012	monosialylated N-glycans	989:1012	On monosialylated N-glycans, sialic acid is exclusively located on the 3-arm and in alpha2,6 linkage, as verified by 2D-HPLC and exoglycosidase digests of 2-aminopyridine (PA)-labelled N-glycans.
18203274	9	1	theme	other	1333:1337	arg1	kind					1339:1342	any other kind	1329:1342	any other kind of PTMs	1329:1350	This first comprehensive glycoproteomic analysis of the important human plasma glycoprotein BChE did not give any indication of O-glycosylation or any other kind of PTMs as previously postulated.
18203274	6	2	theme	sites	766:770	arg1	analysis					719:726	Site-specific analysis	705:726	Site-specific analysis of all nine potential N-glycosylation sites	705:770	Site-specific analysis of all nine potential N-glycosylation sites revealed mainly mono- and disialylated N-glycans to be present on this glycoprotein.
18203274	8	3	located	located	1042:1048	arg1	N-glycans					1004:1012	monosialylated N-glycans	989:1012	monosialylated N-glycans	989:1012	On monosialylated N-glycans, sialic acid is exclusively located on the 3-arm and in alpha2,6 linkage, as verified by 2D-HPLC and exoglycosidase digests of 2-aminopyridine (PA)-labelled N-glycans.
18203274	8	3	located	located	1042:1048	arg2	acid					1022:1025	sialic acid	1015:1025	sialic acid	1015:1025	On monosialylated N-glycans, sialic acid is exclusively located on the 3-arm and in alpha2,6 linkage, as verified by 2D-HPLC and exoglycosidase digests of 2-aminopyridine (PA)-labelled N-glycans.
18203274	8	3	located	located	1042:1048	arg1	3-arm					1057:1061	the 3-arm	1053:1061	the 3-arm	1053:1061	On monosialylated N-glycans, sialic acid is exclusively located on the 3-arm and in alpha2,6 linkage, as verified by 2D-HPLC and exoglycosidase digests of 2-aminopyridine (PA)-labelled N-glycans.
18203274	8	4	theme	2D-HPLC	1103:1109	arg1	digests					1130:1136	2D-HPLC and exoglycosidase digests	1103:1136	digests	1130:1136	On monosialylated N-glycans, sialic acid is exclusively located on the 3-arm and in alpha2,6 linkage, as verified by 2D-HPLC and exoglycosidase digests of 2-aminopyridine (PA)-labelled N-glycans.
18203274	0	5	from	characterization	15:30	arg1	plasma					68:73	human plasma	62:73	human plasma	62:73	Glycoproteomic characterization of butyrylcholinesterase from human plasma.
18203274	8	6	from	located	1042:1048	arg1	linkage					1079:1085	alpha2,6 linkage	1070:1085	alpha2,6 linkage	1070:1085	On monosialylated N-glycans, sialic acid is exclusively located on the 3-arm and in alpha2,6 linkage, as verified by 2D-HPLC and exoglycosidase digests of 2-aminopyridine (PA)-labelled N-glycans.
18203274	1	7	attach	present	145:151	arg1	plasma					162:167	human plasma	156:167	human plasma	156:167	Human butyrylcholinesterase (hBChE) is a highly glycosylated protein present in human plasma.
18203274	1	7	attach	present	145:151	arg2	butyrylcholinesterase					82:102	Human butyrylcholinesterase	76:102	Human butyrylcholinesterase (hBChE)	76:110	Human butyrylcholinesterase (hBChE) is a highly glycosylated protein present in human plasma.
18203274	1	7	attach	present	145:151	arg2	protein					137:143	a highly glycosylated protein	115:143	a highly glycosylated protein present in human plasma	115:167	Human butyrylcholinesterase (hBChE) is a highly glycosylated protein present in human plasma.
18203274	8	8	theme	sialic	1015:1020	arg1	acid					1022:1025	sialic acid	1015:1025	sialic acid	1015:1025	On monosialylated N-glycans, sialic acid is exclusively located on the 3-arm and in alpha2,6 linkage, as verified by 2D-HPLC and exoglycosidase digests of 2-aminopyridine (PA)-labelled N-glycans.
18203274	1	9	theme	Human	76:80	arg1	hBChE					105:109	hBChE	105:109	hBChE	105:109	Human butyrylcholinesterase (hBChE) is a highly glycosylated protein present in human plasma.
18203274	1	9	theme	Human	76:80	arg1	butyrylcholinesterase					82:102	Human butyrylcholinesterase	76:102	Human butyrylcholinesterase (hBChE)	76:110	Human butyrylcholinesterase (hBChE) is a highly glycosylated protein present in human plasma.
18203274	1	9	theme	Human	76:80	arg1	protein					137:143	a highly glycosylated protein	115:143	a highly glycosylated protein present in human plasma	115:167	Human butyrylcholinesterase (hBChE) is a highly glycosylated protein present in human plasma.
18203274	9	10	theme	glycoproteomic	1207:1220	arg1	analysis					1222:1229	This first comprehensive glycoproteomic analysis	1182:1229	This first comprehensive glycoproteomic analysis of the important human plasma glycoprotein BChE	1182:1277	This first comprehensive glycoproteomic analysis of the important human plasma glycoprotein BChE did not give any indication of O-glycosylation or any other kind of PTMs as previously postulated.
18203274	8	11	gly	monosialylated	989:1002	arg1	N-glycans					1004:1012	monosialylated N-glycans	989:1012	monosialylated N-glycans	989:1012	On monosialylated N-glycans, sialic acid is exclusively located on the 3-arm and in alpha2,6 linkage, as verified by 2D-HPLC and exoglycosidase digests of 2-aminopyridine (PA)-labelled N-glycans.
18203274	9	12	theme	PTMs	1347:1350	arg1	kind					1339:1342	any other kind	1329:1342	any other kind of PTMs	1329:1350	This first comprehensive glycoproteomic analysis of the important human plasma glycoprotein BChE did not give any indication of O-glycosylation or any other kind of PTMs as previously postulated.
18203274	9	12	theme	PTMs	1347:1350	arg1	indication					1296:1305	any indication	1292:1305	any indication of O-glycosylation	1292:1324	This first comprehensive glycoproteomic analysis of the important human plasma glycoprotein BChE did not give any indication of O-glycosylation or any other kind of PTMs as previously postulated.
18203274	8	13	theme	alpha2,6	1070:1077	arg1	linkage					1079:1085	alpha2,6 linkage	1070:1085	alpha2,6 linkage	1070:1085	On monosialylated N-glycans, sialic acid is exclusively located on the 3-arm and in alpha2,6 linkage, as verified by 2D-HPLC and exoglycosidase digests of 2-aminopyridine (PA)-labelled N-glycans.
18203274	6	14	theme	N-glycosylation	750:764	arg1	sites					766:770	all nine potential N-glycosylation sites	731:770	all nine potential N-glycosylation sites	731:770	Site-specific analysis of all nine potential N-glycosylation sites revealed mainly mono- and disialylated N-glycans to be present on this glycoprotein.
18203274	6	15	gly	disialylated	798:809	arg1	N-glycans					811:819	mono- and disialylated N-glycans	788:819	mono- and disialylated N-glycans	788:819	Site-specific analysis of all nine potential N-glycosylation sites revealed mainly mono- and disialylated N-glycans to be present on this glycoprotein.
18203274	0	16	from	plasma	68:73	arg1	butyrylcholinesterase					35:55	butyrylcholinesterase	35:55	butyrylcholinesterase from human plasma	35:73	Glycoproteomic characterization of butyrylcholinesterase from human plasma.
18203274	0	16	from	plasma	68:73	arg1	characterization					15:30	Glycoproteomic characterization	0:30	Glycoproteomic characterization of butyrylcholinesterase from human plasma.	0:74	Glycoproteomic characterization of butyrylcholinesterase from human plasma.
18203274	7	17	contain	contained	943:951	arg1	linkage					977:983	alpha2,3 linkage	968:983	alpha2,3 linkage	968:983	Sialic acids (Neu5Ac) are mainly alpha2,6-linked, however a fraction of the N-glycans contained Neu5Ac also in alpha2,3 linkage.
18203274	7	17	contain	contained	943:951	arg2	Neu5Ac					953:958	Neu5Ac	953:958	Neu5Ac	953:958	Sialic acids (Neu5Ac) are mainly alpha2,6-linked, however a fraction of the N-glycans contained Neu5Ac also in alpha2,3 linkage.
18203274	7	17	contain	contained	943:951	arg1	fraction					917:924	a fraction	915:924	a fraction of the N-glycans	915:941	Sialic acids (Neu5Ac) are mainly alpha2,6-linked, however a fraction of the N-glycans contained Neu5Ac also in alpha2,3 linkage.
18203274	7	17	contain	contained	943:951	arg2	fraction					917:924	a fraction	915:924	a fraction of the N-glycans	915:941	Sialic acids (Neu5Ac) are mainly alpha2,6-linked, however a fraction of the N-glycans contained Neu5Ac also in alpha2,3 linkage.
18203274	1	18	from	plasma	162:167	arg1	present					145:151	present	145:151	present	145:151	Human butyrylcholinesterase (hBChE) is a highly glycosylated protein present in human plasma.
18203274	4	19	theme	hBChE	517:521	arg1	use					510:512	the therapeutic use	494:512	the therapeutic use of hBChE	494:521	A prerequisite for the therapeutic use of hBChE is a detailed characterization of this glycoprotein purified from human plasma.
18203274	6	20	theme	potential	740:748	arg1	sites					766:770	all nine potential N-glycosylation sites	731:770	all nine potential N-glycosylation sites	731:770	Site-specific analysis of all nine potential N-glycosylation sites revealed mainly mono- and disialylated N-glycans to be present on this glycoprotein.
18203274	4	21	theme	detailed	528:535	arg1	prerequisite					477:488	A prerequisite	475:488	A prerequisite for the therapeutic use of hBChE	475:521	A prerequisite for the therapeutic use of hBChE is a detailed characterization of this glycoprotein purified from human plasma.
18203274	4	21	theme	detailed	528:535	arg1	characterization					537:552	a detailed characterization	526:552	a detailed characterization of this glycoprotein purified from human plasma	526:600	A prerequisite for the therapeutic use of hBChE is a detailed characterization of this glycoprotein purified from human plasma.
18203274	9	22	theme	plasma	1254:1259	arg1	BChE					1274:1277	the important human plasma glycoprotein BChE	1234:1277	the important human plasma glycoprotein BChE	1234:1277	This first comprehensive glycoproteomic analysis of the important human plasma glycoprotein BChE did not give any indication of O-glycosylation or any other kind of PTMs as previously postulated.
18203274	1	23	from	present	145:151	arg1	plasma					162:167	human plasma	156:167	human plasma	156:167	Human butyrylcholinesterase (hBChE) is a highly glycosylated protein present in human plasma.
18203274	0	24	theme	Glycoproteomic	0:13	arg1	characterization					15:30	Glycoproteomic characterization	0:30	Glycoproteomic characterization of butyrylcholinesterase from human plasma.	0:74	Glycoproteomic characterization of butyrylcholinesterase from human plasma.
18203274	9	25	theme	human	1248:1252	arg1	BChE					1274:1277	the important human plasma glycoprotein BChE	1234:1277	the important human plasma glycoprotein BChE	1234:1277	This first comprehensive glycoproteomic analysis of the important human plasma glycoprotein BChE did not give any indication of O-glycosylation or any other kind of PTMs as previously postulated.
18203274	8	26	theme	N-glycans	1171:1179	arg1	digests					1130:1136	2D-HPLC and exoglycosidase digests	1103:1136	digests	1130:1136	On monosialylated N-glycans, sialic acid is exclusively located on the 3-arm and in alpha2,6 linkage, as verified by 2D-HPLC and exoglycosidase digests of 2-aminopyridine (PA)-labelled N-glycans.
18203274	7	27	theme	alpha2,3	968:975	arg1	linkage					977:983	alpha2,3 linkage	968:983	alpha2,3 linkage	968:983	Sialic acids (Neu5Ac) are mainly alpha2,6-linked, however a fraction of the N-glycans contained Neu5Ac also in alpha2,3 linkage.
18203274	4	28	gly	glycoprotein	562:573	arg1	glycoprotein					562:573	this glycoprotein	557:573	this glycoprotein purified from human plasma	557:600	A prerequisite for the therapeutic use of hBChE is a detailed characterization of this glycoprotein purified from human plasma.
18203274	3	29	theme	toxic	419:423	arg1	organophosphates					425:440	toxic organophosphates	419:440	toxic organophosphates	419:440	hBChE is primarily involved in neuronal transmission and is a potential bioscavenger of toxic organophosphates to protect acetylcholinesterase.
18203274	7	30	theme	Sialic	857:862	arg1	Neu5Ac					871:876	Neu5Ac	871:876	Neu5Ac	871:876	Sialic acids (Neu5Ac) are mainly alpha2,6-linked, however a fraction of the N-glycans contained Neu5Ac also in alpha2,3 linkage.
18203274	7	30	theme	Sialic	857:862	arg1	acids					864:868	Sialic acids	857:868	Sialic acids (Neu5Ac)	857:877	Sialic acids (Neu5Ac) are mainly alpha2,6-linked, however a fraction of the N-glycans contained Neu5Ac also in alpha2,3 linkage.
18203274	9	31	theme	glycoprotein	1261:1272	arg1	BChE					1274:1277	the important human plasma glycoprotein BChE	1234:1277	the important human plasma glycoprotein BChE	1234:1277	This first comprehensive glycoproteomic analysis of the important human plasma glycoprotein BChE did not give any indication of O-glycosylation or any other kind of PTMs as previously postulated.
18203274	3	32	theme	potential	393:401	arg1	bioscavenger					403:414	a potential bioscavenger	391:414	a potential bioscavenger of toxic organophosphates to protect acetylcholinesterase	391:472	hBChE is primarily involved in neuronal transmission and is a potential bioscavenger of toxic organophosphates to protect acetylcholinesterase.
18203274	5	33	theme	protein	650:656	arg1	backbone					658:665	the protein backbone	646:665	the protein backbone	646:665	In this study, MS/MS could confirm most of the protein backbone, including the N- and the C-terminus.
18203274	1	34	gly	glycosylated	124:135	arg1	protein					137:143	a highly glycosylated protein	115:143	a highly glycosylated protein present in human plasma	115:167	Human butyrylcholinesterase (hBChE) is a highly glycosylated protein present in human plasma.
18203274	1	34	gly	glycosylated	124:135	arg1	butyrylcholinesterase					82:102	Human butyrylcholinesterase	76:102	Human butyrylcholinesterase (hBChE)	76:110	Human butyrylcholinesterase (hBChE) is a highly glycosylated protein present in human plasma.
18203274	4	35	theme	therapeutic	498:508	arg1	use					510:512	the therapeutic use	494:512	the therapeutic use of hBChE	494:521	A prerequisite for the therapeutic use of hBChE is a detailed characterization of this glycoprotein purified from human plasma.
18203274	6	36	theme	Site-specific	705:717	arg1	analysis					719:726	Site-specific analysis	705:726	Site-specific analysis of all nine potential N-glycosylation sites	705:770	Site-specific analysis of all nine potential N-glycosylation sites revealed mainly mono- and disialylated N-glycans to be present on this glycoprotein.
18203274	0	37	theme	human	62:66	arg1	plasma					68:73	human plasma	62:73	human plasma	62:73	Glycoproteomic characterization of butyrylcholinesterase from human plasma.
18203274	2	38	theme	choline	192:198	arg1	esters					200:205	choline esters	192:205	choline esters	192:205	The enzyme hydrolyses choline esters, for example benzoylcholine, butyrylthiocholine and acetylthiocholine as well as noncholine esters like heroin and aspirin.
18203274	8	39	theme	exoglycosidase	1115:1128	arg1	digests					1130:1136	2D-HPLC and exoglycosidase digests	1103:1136	digests	1130:1136	On monosialylated N-glycans, sialic acid is exclusively located on the 3-arm and in alpha2,6 linkage, as verified by 2D-HPLC and exoglycosidase digests of 2-aminopyridine (PA)-labelled N-glycans.
18203274	0	40	theme	butyrylcholinesterase	35:55	arg1	characterization					15:30	Glycoproteomic characterization	0:30	Glycoproteomic characterization of butyrylcholinesterase from human plasma.	0:74	Glycoproteomic characterization of butyrylcholinesterase from human plasma.
18203274	4	41	theme	glycoprotein	562:573	arg1	prerequisite					477:488	A prerequisite	475:488	A prerequisite for the therapeutic use of hBChE	475:521	A prerequisite for the therapeutic use of hBChE is a detailed characterization of this glycoprotein purified from human plasma.
18203274	4	41	theme	glycoprotein	562:573	arg1	characterization					537:552	a detailed characterization	526:552	a detailed characterization of this glycoprotein purified from human plasma	526:600	A prerequisite for the therapeutic use of hBChE is a detailed characterization of this glycoprotein purified from human plasma.
18203274	9	42	theme	important	1238:1246	arg1	BChE					1274:1277	the important human plasma glycoprotein BChE	1234:1277	the important human plasma glycoprotein BChE	1234:1277	This first comprehensive glycoproteomic analysis of the important human plasma glycoprotein BChE did not give any indication of O-glycosylation or any other kind of PTMs as previously postulated.
18203274	3	43	theme	organophosphates	425:440	arg1	bioscavenger					403:414	a potential bioscavenger	391:414	a potential bioscavenger of toxic organophosphates to protect acetylcholinesterase	391:472	hBChE is primarily involved in neuronal transmission and is a potential bioscavenger of toxic organophosphates to protect acetylcholinesterase.
18203274	9	44	theme	BChE	1274:1277	arg1	analysis					1222:1229	This first comprehensive glycoproteomic analysis	1182:1229	This first comprehensive glycoproteomic analysis of the important human plasma glycoprotein BChE	1182:1277	This first comprehensive glycoproteomic analysis of the important human plasma glycoprotein BChE did not give any indication of O-glycosylation or any other kind of PTMs as previously postulated.
18203274	1	45	theme	glycosylated	124:135	arg1	protein					137:143	a highly glycosylated protein	115:143	a highly glycosylated protein present in human plasma	115:167	Human butyrylcholinesterase (hBChE) is a highly glycosylated protein present in human plasma.
18203274	1	45	theme	glycosylated	124:135	arg1	butyrylcholinesterase					82:102	Human butyrylcholinesterase	76:102	Human butyrylcholinesterase (hBChE)	76:110	Human butyrylcholinesterase (hBChE) is a highly glycosylated protein present in human plasma.
18203274	9	46	gly	glycoprotein	1261:1272	arg1	glycoprotein					1261:1272	the important human plasma glycoprotein BChE	1234:1277	the important human plasma glycoprotein BChE	1234:1277	This first comprehensive glycoproteomic analysis of the important human plasma glycoprotein BChE did not give any indication of O-glycosylation or any other kind of PTMs as previously postulated.
18203274	6	47	gly	glycoprotein	843:854	arg1	glycoprotein					843:854	this glycoprotein	838:854	this glycoprotein	838:854	Site-specific analysis of all nine potential N-glycosylation sites revealed mainly mono- and disialylated N-glycans to be present on this glycoprotein.
18203274	6	48	theme	disialylated	798:809	arg1	N-glycans					811:819	mono- and disialylated N-glycans	788:819	mono- and disialylated N-glycans	788:819	Site-specific analysis of all nine potential N-glycosylation sites revealed mainly mono- and disialylated N-glycans to be present on this glycoprotein.
18203274	4	49	theme	human	589:593	arg1	plasma					595:600	human plasma	589:600	human plasma	589:600	A prerequisite for the therapeutic use of hBChE is a detailed characterization of this glycoprotein purified from human plasma.
18203274	6	50	gly	N-glycosylation	750:764	arg2	sites					766:770	all nine potential N-glycosylation sites	731:770	all nine potential N-glycosylation sites	731:770	Site-specific analysis of all nine potential N-glycosylation sites revealed mainly mono- and disialylated N-glycans to be present on this glycoprotein.
18203274	6	50	gly	N-glycosylation	750:764	arg2	nine					735:738	nine	735:738	nine	735:738	Site-specific analysis of all nine potential N-glycosylation sites revealed mainly mono- and disialylated N-glycans to be present on this glycoprotein.
18203274	2	51	theme	noncholine	288:297	arg1	esters					299:304	noncholine esters	288:304	noncholine esters like heroin and aspirin	288:328	The enzyme hydrolyses choline esters, for example benzoylcholine, butyrylthiocholine and acetylthiocholine as well as noncholine esters like heroin and aspirin.
18203274	1	52	theme	present	145:151	arg1	protein					137:143	a highly glycosylated protein	115:143	a highly glycosylated protein present in human plasma	115:167	Human butyrylcholinesterase (hBChE) is a highly glycosylated protein present in human plasma.
18203274	1	52	theme	present	145:151	arg1	butyrylcholinesterase					82:102	Human butyrylcholinesterase	76:102	Human butyrylcholinesterase (hBChE)	76:110	Human butyrylcholinesterase (hBChE) is a highly glycosylated protein present in human plasma.
18203274	9	53	theme	O-glycosylation	1310:1324	arg1	kind					1339:1342	any other kind	1329:1342	any other kind of PTMs	1329:1350	This first comprehensive glycoproteomic analysis of the important human plasma glycoprotein BChE did not give any indication of O-glycosylation or any other kind of PTMs as previously postulated.
18203274	9	53	theme	O-glycosylation	1310:1324	arg1	indication					1296:1305	any indication	1292:1305	any indication of O-glycosylation	1292:1324	This first comprehensive glycoproteomic analysis of the important human plasma glycoprotein BChE did not give any indication of O-glycosylation or any other kind of PTMs as previously postulated.
18203274	6	54	theme	mono-	788:792	arg1	N-glycans					811:819	mono- and disialylated N-glycans	788:819	mono- and disialylated N-glycans	788:819	Site-specific analysis of all nine potential N-glycosylation sites revealed mainly mono- and disialylated N-glycans to be present on this glycoprotein.
18203274	7	55	theme	N-glycans	933:941	arg1	fraction					917:924	a fraction	915:924	a fraction of the N-glycans	915:941	Sialic acids (Neu5Ac) are mainly alpha2,6-linked, however a fraction of the N-glycans contained Neu5Ac also in alpha2,3 linkage.
18203274	8	56	theme	-labelled	1161:1169	arg1	N-glycans					1171:1179	2-aminopyridine (PA)-labelled N-glycans	1141:1179	2-aminopyridine (PA)-labelled N-glycans	1141:1179	On monosialylated N-glycans, sialic acid is exclusively located on the 3-arm and in alpha2,6 linkage, as verified by 2D-HPLC and exoglycosidase digests of 2-aminopyridine (PA)-labelled N-glycans.
18203274	9	57	theme	first	1187:1191	arg1	analysis					1222:1229	This first comprehensive glycoproteomic analysis	1182:1229	This first comprehensive glycoproteomic analysis of the important human plasma glycoprotein BChE	1182:1277	This first comprehensive glycoproteomic analysis of the important human plasma glycoprotein BChE did not give any indication of O-glycosylation or any other kind of PTMs as previously postulated.
18203274	1	58	theme	human	156:160	arg1	plasma					162:167	human plasma	156:167	human plasma	156:167	Human butyrylcholinesterase (hBChE) is a highly glycosylated protein present in human plasma.
18203274	3	59	theme	neuronal	362:369	arg1	transmission					371:382	neuronal transmission	362:382	neuronal transmission	362:382	hBChE is primarily involved in neuronal transmission and is a potential bioscavenger of toxic organophosphates to protect acetylcholinesterase.
18203274	8	60	from	linkage	1079:1085	arg1	located					1042:1048	located	1042:1048	located	1042:1048	On monosialylated N-glycans, sialic acid is exclusively located on the 3-arm and in alpha2,6 linkage, as verified by 2D-HPLC and exoglycosidase digests of 2-aminopyridine (PA)-labelled N-glycans.
18203274	9	61	theme	comprehensive	1193:1205	arg1	analysis					1222:1229	This first comprehensive glycoproteomic analysis	1182:1229	This first comprehensive glycoproteomic analysis of the important human plasma glycoprotein BChE	1182:1277	This first comprehensive glycoproteomic analysis of the important human plasma glycoprotein BChE did not give any indication of O-glycosylation or any other kind of PTMs as previously postulated.
18203274	2	62	dep	example	212:218	arg1	benzoylcholine					220:233	benzoylcholine	220:233	benzoylcholine	220:233	The enzyme hydrolyses choline esters, for example benzoylcholine, butyrylthiocholine and acetylthiocholine as well as noncholine esters like heroin and aspirin.
20729549	0	0	theme	keratins	83:90	arg1	solubility					31:40	solubility	31:40	solubility	31:40	O-GlcNAcylation determines the solubility, filament organization, and stability of keratins 8 and 18.
20729549	0	0	theme	keratins	83:90	arg1	organization					52:63	filament organization	43:63	filament organization	43:63	O-GlcNAcylation determines the solubility, filament organization, and stability of keratins 8 and 18.
20729549	0	0	theme	keratins	83:90	arg1	stability					70:78	stability	70:78	stability	70:78	O-GlcNAcylation determines the solubility, filament organization, and stability of keratins 8 and 18.
20729549	5	1	theme	Heat	734:737	arg1	stress					739:744	Heat stress	734:744	Heat stress	734:744	Heat stress, which increases K8/18 solubility, resulted in a simultaneous increase in O-GlcNAc on these proteins.
20729549	4	2	theme	positive	660:667	arg1	correlation					669:679	a positive correlation	658:679	a positive correlation with their solubility (Nonidet P-40 extractability)	658:731	Here, by comparing immortalized (Chang) and transformed hepatocyte (HepG2) cell lines, we have demonstrated that O-GlcNAcylation of K8/18 exhibits a positive correlation with their solubility (Nonidet P-40 extractability).
20729549	8	3	theme	reduced	1075:1081	arg1	half-life					1083:1091	the reduced half-life	1071:1091	the reduced half-life of K8 and K18	1071:1105	Unaltered levels of transcripts and the reduced half-life of K8 and K18 indicated their decreased stability on increasing O-GlcNAcylation.
20729549	8	4	theme	K18	1103:1105	arg1	levels					1045:1050	Unaltered levels	1035:1050	Unaltered levels of transcripts	1035:1065	Unaltered levels of transcripts and the reduced half-life of K8 and K18 indicated their decreased stability on increasing O-GlcNAcylation.
20729549	8	4	theme	K18	1103:1105	arg1	half-life					1083:1091	the reduced half-life	1071:1091	the reduced half-life of K8 and K18	1071:1105	Unaltered levels of transcripts and the reduced half-life of K8 and K18 indicated their decreased stability on increasing O-GlcNAcylation.
20729549	11	5	theme	keratins	1601:1608	arg1	functions					1582:1590	the functions	1578:1590	the functions of these keratins	1578:1608	These results strongly indicate the involvement of O-GlcNAc on K8/18 in regulating their solubility and stability, which may have a bearing on the functions of these keratins.
20729549	10	6	theme	filament	1412:1419	arg1	architecture					1421:1432	endogenous filament architecture	1401:1432	endogenous filament architecture	1401:1432	The K18-O-GlcNAc mutant accumulated as aggregates upon stable expression, which possibly altered endogenous filament architecture.
20729549	10	7	theme	stable	1359:1364	arg1	expression					1366:1375	stable expression	1359:1375	stable expression	1359:1375	The K18-O-GlcNAc mutant accumulated as aggregates upon stable expression, which possibly altered endogenous filament architecture.
20729549	2	8	theme	functions	345:353	arg1	determinant					315:325	an important determinant	302:325	an important determinant of their cellular functions	302:353	Dynamic equilibrium of these phosphoglycoproteins in the soluble and filament pool is an important determinant of their cellular functions, and it is known to be regulated by site-specific phosphorylation.
20729549	2	8	theme	functions	345:353	arg1	equilibrium					224:234	Dynamic equilibrium	216:234	Dynamic equilibrium of these phosphoglycoproteins in the soluble and filament pool	216:297	Dynamic equilibrium of these phosphoglycoproteins in the soluble and filament pool is an important determinant of their cellular functions, and it is known to be regulated by site-specific phosphorylation.
20729549	11	9	theme	O-GlcNAc	1486:1493	arg1	involvement					1471:1481	the involvement	1467:1481	the involvement of O-GlcNAc on K8/18 in regulating their solubility and stability, which may have a bearing on the functions of these keratins	1467:1608	These results strongly indicate the involvement of O-GlcNAc on K8/18 in regulating their solubility and stability, which may have a bearing on the functions of these keratins.
20729549	7	10	theme	notable	983:989	arg1	decrease					991:998	a notable decrease	981:998	a notable decrease in total cellular levels of K8/18	981:1032	This was also associated with a notable decrease in total cellular levels of K8/18.
20729549	8	11	theme	decreased	1123:1131	arg1	stability					1133:1141	their decreased stability	1117:1141	their decreased stability	1117:1141	Unaltered levels of transcripts and the reduced half-life of K8 and K18 indicated their decreased stability on increasing O-GlcNAcylation.
20729549	4	12	with	correlation	669:679	arg1	solubility					692:701	their solubility	686:701	their solubility (Nonidet P-40 extractability)	686:731	Here, by comparing immortalized (Chang) and transformed hepatocyte (HepG2) cell lines, we have demonstrated that O-GlcNAcylation of K8/18 exhibits a positive correlation with their solubility (Nonidet P-40 extractability).
20729549	10	13	theme	endogenous	1401:1410	arg1	architecture					1421:1432	endogenous filament architecture	1401:1432	endogenous filament architecture	1401:1432	The K18-O-GlcNAc mutant accumulated as aggregates upon stable expression, which possibly altered endogenous filament architecture.
20729549	2	14	theme	filament	285:292	arg1	pool					294:297	the soluble and filament pool	269:297	pool	294:297	Dynamic equilibrium of these phosphoglycoproteins in the soluble and filament pool is an important determinant of their cellular functions, and it is known to be regulated by site-specific phosphorylation.
20729549	4	15	theme	hepatocyte	567:576	arg1	lines					591:595	transformed hepatocyte (HepG2) cell lines	555:595	transformed hepatocyte (HepG2) cell lines	555:595	Here, by comparing immortalized (Chang) and transformed hepatocyte (HepG2) cell lines, we have demonstrated that O-GlcNAcylation of K8/18 exhibits a positive correlation with their solubility (Nonidet P-40 extractability).
20729549	4	16	theme	Nonidet	704:710	arg1	P-40					712:715	Nonidet P-40	704:715	Nonidet P-40 extractability	704:730	Here, by comparing immortalized (Chang) and transformed hepatocyte (HepG2) cell lines, we have demonstrated that O-GlcNAcylation of K8/18 exhibits a positive correlation with their solubility (Nonidet P-40 extractability).
20729549	6	17	theme	increasing	860:869	arg1	levels					880:885	increasing O-GlcNAc levels	860:885	increasing O-GlcNAc levels	860:885	Conversely, increasing O-GlcNAc levels were associated with a concurrent increase in their solubility.
20729549	4	18	theme	transformed	555:565	arg1	lines					591:595	transformed hepatocyte (HepG2) cell lines	555:595	transformed hepatocyte (HepG2) cell lines	555:595	Here, by comparing immortalized (Chang) and transformed hepatocyte (HepG2) cell lines, we have demonstrated that O-GlcNAcylation of K8/18 exhibits a positive correlation with their solubility (Nonidet P-40 extractability).
20729549	3	19	theme	dynamic	465:471	arg1	O-GlcNAcylation					473:487	dynamic O-GlcNAcylation	465:487	dynamic O-GlcNAcylation	465:487	However, little is known about the role of dynamic O-GlcNAcylation on this keratin pair.
20729549	5	20	theme	simultaneous	795:806	arg1	increase					808:815	a simultaneous increase	793:815	a simultaneous increase in O-GlcNAc on these proteins	793:845	Heat stress, which increases K8/18 solubility, resulted in a simultaneous increase in O-GlcNAc on these proteins.
20729549	1	21	dep	Keratins	102:109	arg1	K8/18					121:125	K8/18	121:125	K8/18	121:125	Keratins 8 and 18 (K8/18) are intermediate filament proteins expressed specifically in simple epithelial tissues.
20729549	1	21	dep	Keratins	102:109	arg1	18					117:118	18	117:118	18	117:118	Keratins 8 and 18 (K8/18) are intermediate filament proteins expressed specifically in simple epithelial tissues.
20729549	1	21	dep	Keratins	102:109	arg1	8					111:111	8	111:111	8	111:111	Keratins 8 and 18 (K8/18) are intermediate filament proteins expressed specifically in simple epithelial tissues.
20729549	1	22	theme	intermediate	132:143	arg1	proteins					154:161	intermediate filament proteins	132:161	intermediate filament proteins expressed specifically in simple epithelial tissues	132:213	Keratins 8 and 18 (K8/18) are intermediate filament proteins expressed specifically in simple epithelial tissues.
20729549	1	22	theme	intermediate	132:143	arg1	Keratins					102:109	Keratins 8 and 18 (K8/18)	102:126	Keratins 8 and 18 (K8/18)	102:126	Keratins 8 and 18 (K8/18) are intermediate filament proteins expressed specifically in simple epithelial tissues.
20729549	0	23	theme	18	98:99	arg1	solubility					31:40	solubility	31:40	solubility	31:40	O-GlcNAcylation determines the solubility, filament organization, and stability of keratins 8 and 18.
20729549	0	23	theme	18	98:99	arg1	organization					52:63	filament organization	43:63	filament organization	43:63	O-GlcNAcylation determines the solubility, filament organization, and stability of keratins 8 and 18.
20729549	0	23	theme	18	98:99	arg1	stability					70:78	stability	70:78	stability	70:78	O-GlcNAcylation determines the solubility, filament organization, and stability of keratins 8 and 18.
20729549	4	24	dep	immortalized	530:541	arg1	Chang					544:548	Chang	544:548	Chang	544:548	Here, by comparing immortalized (Chang) and transformed hepatocyte (HepG2) cell lines, we have demonstrated that O-GlcNAcylation of K8/18 exhibits a positive correlation with their solubility (Nonidet P-40 extractability).
20729549	3	25	from	role	457:460	arg1	pair					505:508	this keratin pair	492:508	this keratin pair	492:508	However, little is known about the role of dynamic O-GlcNAcylation on this keratin pair.
20729549	2	26	from	equilibrium	224:234	arg1	pool					294:297	the soluble and filament pool	269:297	pool	294:297	Dynamic equilibrium of these phosphoglycoproteins in the soluble and filament pool is an important determinant of their cellular functions, and it is known to be regulated by site-specific phosphorylation.
20729549	1	27	theme	filament	145:152	arg1	proteins					154:161	intermediate filament proteins	132:161	intermediate filament proteins expressed specifically in simple epithelial tissues	132:213	Keratins 8 and 18 (K8/18) are intermediate filament proteins expressed specifically in simple epithelial tissues.
20729549	1	27	theme	filament	145:152	arg1	Keratins					102:109	Keratins 8 and 18 (K8/18)	102:126	Keratins 8 and 18 (K8/18)	102:126	Keratins 8 and 18 (K8/18) are intermediate filament proteins expressed specifically in simple epithelial tissues.
20729549	2	28	gly	phosphoglycoproteins	245:264	arg1	phosphoglycoproteins					245:264	these phosphoglycoproteins	239:264	these phosphoglycoproteins	239:264	Dynamic equilibrium of these phosphoglycoproteins in the soluble and filament pool is an important determinant of their cellular functions, and it is known to be regulated by site-specific phosphorylation.
20729549	8	29	theme	Unaltered	1035:1043	arg1	levels					1045:1050	Unaltered levels	1035:1050	Unaltered levels of transcripts	1035:1065	Unaltered levels of transcripts and the reduced half-life of K8 and K18 indicated their decreased stability on increasing O-GlcNAcylation.
20729549	2	30	theme	important	305:313	arg1	determinant					315:325	an important determinant	302:325	an important determinant of their cellular functions	302:353	Dynamic equilibrium of these phosphoglycoproteins in the soluble and filament pool is an important determinant of their cellular functions, and it is known to be regulated by site-specific phosphorylation.
20729549	2	30	theme	important	305:313	arg1	equilibrium					224:234	Dynamic equilibrium	216:234	Dynamic equilibrium of these phosphoglycoproteins in the soluble and filament pool	216:297	Dynamic equilibrium of these phosphoglycoproteins in the soluble and filament pool is an important determinant of their cellular functions, and it is known to be regulated by site-specific phosphorylation.
20729549	9	31	theme	wild	1274:1277	arg1	K18					1284:1286	the wild type K18	1270:1286	the wild type K18 in Chang cells	1270:1301	On the contrary, the K18 glycosylation mutant (K18 S29A/S30A/S48A) was notably more stable than the wild type K18 in Chang cells.
20729549	9	32	from	K18	1284:1286	arg1	cells					1297:1301	Chang cells	1291:1301	Chang cells	1291:1301	On the contrary, the K18 glycosylation mutant (K18 S29A/S30A/S48A) was notably more stable than the wild type K18 in Chang cells.
20729549	9	33	theme	Chang	1291:1295	arg1	cells					1297:1301	Chang cells	1291:1301	Chang cells	1291:1301	On the contrary, the K18 glycosylation mutant (K18 S29A/S30A/S48A) was notably more stable than the wild type K18 in Chang cells.
20729549	11	34	from	involvement	1471:1481	arg1	K8/18					1498:1502	K8/18	1498:1502	K8/18	1498:1502	These results strongly indicate the involvement of O-GlcNAc on K8/18 in regulating their solubility and stability, which may have a bearing on the functions of these keratins.
20729549	6	35	theme	O-GlcNAc	871:878	arg1	levels					880:885	increasing O-GlcNAc levels	860:885	increasing O-GlcNAc levels	860:885	Conversely, increasing O-GlcNAc levels were associated with a concurrent increase in their solubility.
20729549	2	36	theme	soluble	273:279	arg1	pool					294:297	the soluble and filament pool	269:297	pool	294:297	Dynamic equilibrium of these phosphoglycoproteins in the soluble and filament pool is an important determinant of their cellular functions, and it is known to be regulated by site-specific phosphorylation.
20729549	9	37	theme	K18	1195:1197	arg1	mutant					1213:1218	the K18 glycosylation mutant	1191:1218	the K18 glycosylation mutant (K18 S29A/S30A/S48A)	1191:1239	On the contrary, the K18 glycosylation mutant (K18 S29A/S30A/S48A) was notably more stable than the wild type K18 in Chang cells.
20729549	9	37	theme	K18	1195:1197	arg1	S29A/S30A/S48A					1225:1238	K18 S29A/S30A/S48A	1221:1238	K18 S29A/S30A/S48A	1221:1238	On the contrary, the K18 glycosylation mutant (K18 S29A/S30A/S48A) was notably more stable than the wild type K18 in Chang cells.
20729549	9	37	theme	K18	1195:1197	arg1	stable					1258:1263	stable	1258:1263	stable	1258:1263	On the contrary, the K18 glycosylation mutant (K18 S29A/S30A/S48A) was notably more stable than the wild type K18 in Chang cells.
20729549	2	38	theme	site-specific	391:403	arg1	phosphorylation					405:419	site-specific phosphorylation	391:419	site-specific phosphorylation	391:419	Dynamic equilibrium of these phosphoglycoproteins in the soluble and filament pool is an important determinant of their cellular functions, and it is known to be regulated by site-specific phosphorylation.
20729549	0	39	theme	filament	43:50	arg1	organization					52:63	filament organization	43:63	filament organization	43:63	O-GlcNAcylation determines the solubility, filament organization, and stability of keratins 8 and 18.
20729549	4	40	dep	P-40	712:715	arg1	extractability					717:730	extractability	717:730	Nonidet P-40 extractability	704:730	Here, by comparing immortalized (Chang) and transformed hepatocyte (HepG2) cell lines, we have demonstrated that O-GlcNAcylation of K8/18 exhibits a positive correlation with their solubility (Nonidet P-40 extractability).
20729549	9	41	theme	glycosylation	1199:1211	arg1	mutant					1213:1218	the K18 glycosylation mutant	1191:1218	the K18 glycosylation mutant (K18 S29A/S30A/S48A)	1191:1239	On the contrary, the K18 glycosylation mutant (K18 S29A/S30A/S48A) was notably more stable than the wild type K18 in Chang cells.
20729549	9	41	theme	glycosylation	1199:1211	arg1	S29A/S30A/S48A					1225:1238	K18 S29A/S30A/S48A	1221:1238	K18 S29A/S30A/S48A	1221:1238	On the contrary, the K18 glycosylation mutant (K18 S29A/S30A/S48A) was notably more stable than the wild type K18 in Chang cells.
20729549	9	41	theme	glycosylation	1199:1211	arg1	stable					1258:1263	stable	1258:1263	stable	1258:1263	On the contrary, the K18 glycosylation mutant (K18 S29A/S30A/S48A) was notably more stable than the wild type K18 in Chang cells.
20729549	1	42	theme	simple	189:194	arg1	tissues					207:213	simple epithelial tissues	189:213	simple epithelial tissues	189:213	Keratins 8 and 18 (K8/18) are intermediate filament proteins expressed specifically in simple epithelial tissues.
20729549	7	43	theme	K8/18	1028:1032	arg1	levels					1018:1023	total cellular levels	1003:1023	total cellular levels of K8/18	1003:1032	This was also associated with a notable decrease in total cellular levels of K8/18.
20729549	2	44	theme	Dynamic	216:222	arg1	determinant					315:325	an important determinant	302:325	an important determinant of their cellular functions	302:353	Dynamic equilibrium of these phosphoglycoproteins in the soluble and filament pool is an important determinant of their cellular functions, and it is known to be regulated by site-specific phosphorylation.
20729549	2	44	theme	Dynamic	216:222	arg1	equilibrium					224:234	Dynamic equilibrium	216:234	Dynamic equilibrium of these phosphoglycoproteins in the soluble and filament pool	216:297	Dynamic equilibrium of these phosphoglycoproteins in the soluble and filament pool is an important determinant of their cellular functions, and it is known to be regulated by site-specific phosphorylation.
20729549	5	45	from	increase	808:815	arg1	O-GlcNAc					820:827	O-GlcNAc	820:827	O-GlcNAc	820:827	Heat stress, which increases K8/18 solubility, resulted in a simultaneous increase in O-GlcNAc on these proteins.
20729549	5	45	from	increase	808:815	arg1	proteins					838:845	these proteins	832:845	these proteins	832:845	Heat stress, which increases K8/18 solubility, resulted in a simultaneous increase in O-GlcNAc on these proteins.
20729549	1	46	theme	epithelial	196:205	arg1	tissues					207:213	simple epithelial tissues	189:213	simple epithelial tissues	189:213	Keratins 8 and 18 (K8/18) are intermediate filament proteins expressed specifically in simple epithelial tissues.
20729549	6	47	theme	concurrent	910:919	arg1	increase					921:928	a concurrent increase	908:928	a concurrent increase in their solubility	908:948	Conversely, increasing O-GlcNAc levels were associated with a concurrent increase in their solubility.
20729549	7	48	theme	cellular	1009:1016	arg1	levels					1018:1023	total cellular levels	1003:1023	total cellular levels of K8/18	1003:1032	This was also associated with a notable decrease in total cellular levels of K8/18.
20729549	9	49	theme	type	1279:1282	arg1	K18					1284:1286	the wild type K18	1270:1286	the wild type K18 in Chang cells	1270:1301	On the contrary, the K18 glycosylation mutant (K18 S29A/S30A/S48A) was notably more stable than the wild type K18 in Chang cells.
20729549	2	50	theme	cellular	336:343	arg1	functions					345:353	their cellular functions	330:353	their cellular functions	330:353	Dynamic equilibrium of these phosphoglycoproteins in the soluble and filament pool is an important determinant of their cellular functions, and it is known to be regulated by site-specific phosphorylation.
20729549	5	51	theme	K8/18	763:767	arg1	solubility					769:778	K8/18 solubility	763:778	K8/18 solubility	763:778	Heat stress, which increases K8/18 solubility, resulted in a simultaneous increase in O-GlcNAc on these proteins.
20729549	9	52	theme	K18	1221:1223	arg1	mutant					1213:1218	the K18 glycosylation mutant	1191:1218	the K18 glycosylation mutant (K18 S29A/S30A/S48A)	1191:1239	On the contrary, the K18 glycosylation mutant (K18 S29A/S30A/S48A) was notably more stable than the wild type K18 in Chang cells.
20729549	9	52	theme	K18	1221:1223	arg1	S29A/S30A/S48A					1225:1238	K18 S29A/S30A/S48A	1221:1238	K18 S29A/S30A/S48A	1221:1238	On the contrary, the K18 glycosylation mutant (K18 S29A/S30A/S48A) was notably more stable than the wild type K18 in Chang cells.
20729549	3	53	theme	O-GlcNAcylation	473:487	arg1	role					457:460	the role	453:460	the role of dynamic O-GlcNAcylation on this keratin pair	453:508	However, little is known about the role of dynamic O-GlcNAcylation on this keratin pair.
20729549	6	54	from	increase	921:928	arg1	solubility					939:948	their solubility	933:948	their solubility	933:948	Conversely, increasing O-GlcNAc levels were associated with a concurrent increase in their solubility.
20729549	0	55	dep	solubility	31:40	arg1	the					27:29	the	27:29	the	27:29	O-GlcNAcylation determines the solubility, filament organization, and stability of keratins 8 and 18.
20729549	4	56	dep	solubility	692:701	arg1	P-40					712:715	Nonidet P-40	704:715	Nonidet P-40 extractability	704:730	Here, by comparing immortalized (Chang) and transformed hepatocyte (HepG2) cell lines, we have demonstrated that O-GlcNAcylation of K8/18 exhibits a positive correlation with their solubility (Nonidet P-40 extractability).
20729549	4	57	theme	HepG2	579:583	arg1	lines					591:595	transformed hepatocyte (HepG2) cell lines	555:595	transformed hepatocyte (HepG2) cell lines	555:595	Here, by comparing immortalized (Chang) and transformed hepatocyte (HepG2) cell lines, we have demonstrated that O-GlcNAcylation of K8/18 exhibits a positive correlation with their solubility (Nonidet P-40 extractability).
20729549	7	58	theme	total	1003:1007	arg1	levels					1018:1023	total cellular levels	1003:1023	total cellular levels of K8/18	1003:1032	This was also associated with a notable decrease in total cellular levels of K8/18.
20729549	2	59	theme	phosphoglycoproteins	245:264	arg1	determinant					315:325	an important determinant	302:325	an important determinant of their cellular functions	302:353	Dynamic equilibrium of these phosphoglycoproteins in the soluble and filament pool is an important determinant of their cellular functions, and it is known to be regulated by site-specific phosphorylation.
20729549	2	59	theme	phosphoglycoproteins	245:264	arg1	equilibrium					224:234	Dynamic equilibrium	216:234	Dynamic equilibrium of these phosphoglycoproteins in the soluble and filament pool	216:297	Dynamic equilibrium of these phosphoglycoproteins in the soluble and filament pool is an important determinant of their cellular functions, and it is known to be regulated by site-specific phosphorylation.
20729549	7	60	from	decrease	991:998	arg1	levels					1018:1023	total cellular levels	1003:1023	total cellular levels of K8/18	1003:1032	This was also associated with a notable decrease in total cellular levels of K8/18.
20729549	3	61	theme	keratin	497:503	arg1	pair					505:508	this keratin pair	492:508	this keratin pair	492:508	However, little is known about the role of dynamic O-GlcNAcylation on this keratin pair.
20729549	4	62	theme	cell	586:589	arg1	lines					591:595	transformed hepatocyte (HepG2) cell lines	555:595	transformed hepatocyte (HepG2) cell lines	555:595	Here, by comparing immortalized (Chang) and transformed hepatocyte (HepG2) cell lines, we have demonstrated that O-GlcNAcylation of K8/18 exhibits a positive correlation with their solubility (Nonidet P-40 extractability).
20729549	8	63	theme	K8	1096:1097	arg1	levels					1045:1050	Unaltered levels	1035:1050	Unaltered levels of transcripts	1035:1065	Unaltered levels of transcripts and the reduced half-life of K8 and K18 indicated their decreased stability on increasing O-GlcNAcylation.
20729549	8	63	theme	K8	1096:1097	arg1	half-life					1083:1091	the reduced half-life	1071:1091	the reduced half-life of K8 and K18	1071:1105	Unaltered levels of transcripts and the reduced half-life of K8 and K18 indicated their decreased stability on increasing O-GlcNAcylation.
20729549	10	64	theme	K18-O-GlcNAc	1308:1319	arg1	mutant					1321:1326	The K18-O-GlcNAc mutant	1304:1326	The K18-O-GlcNAc mutant	1304:1326	The K18-O-GlcNAc mutant accumulated as aggregates upon stable expression, which possibly altered endogenous filament architecture.
20729549	4	65	theme	K8/18	643:647	arg1	O-GlcNAcylation					624:638	O-GlcNAcylation	624:638	O-GlcNAcylation of K8/18	624:647	Here, by comparing immortalized (Chang) and transformed hepatocyte (HepG2) cell lines, we have demonstrated that O-GlcNAcylation of K8/18 exhibits a positive correlation with their solubility (Nonidet P-40 extractability).
20729549	8	66	theme	transcripts	1055:1065	arg1	levels					1045:1050	Unaltered levels	1035:1050	Unaltered levels of transcripts	1035:1065	Unaltered levels of transcripts and the reduced half-life of K8 and K18 indicated their decreased stability on increasing O-GlcNAcylation.
20729549	8	66	theme	transcripts	1055:1065	arg1	half-life					1083:1091	the reduced half-life	1071:1091	the reduced half-life of K8 and K18	1071:1105	Unaltered levels of transcripts and the reduced half-life of K8 and K18 indicated their decreased stability on increasing O-GlcNAcylation.
20729549	11	67	contain	have	1560:1563	arg1	solubility					1524:1533	solubility	1524:1533	solubility	1524:1533	These results strongly indicate the involvement of O-GlcNAc on K8/18 in regulating their solubility and stability, which may have a bearing on the functions of these keratins.
20729549	11	67	contain	have	1560:1563	arg1	stability					1539:1547	stability	1539:1547	stability	1539:1547	These results strongly indicate the involvement of O-GlcNAc on K8/18 in regulating their solubility and stability, which may have a bearing on the functions of these keratins.
20729549	11	67	contain	have	1560:1563	arg2	bearing					1567:1573	a bearing	1565:1573	a bearing	1565:1573	These results strongly indicate the involvement of O-GlcNAc on K8/18 in regulating their solubility and stability, which may have a bearing on the functions of these keratins.
1371281	0	0	theme	18	83:84	arg1	glycosylation					42:54	O-linked glycosylation	33:54	O-linked glycosylation of human cytokeratin 8 and 18	33:84	Characterization and dynamics of O-linked glycosylation of human cytokeratin 8 and 18.
1371281	5	1	theme	disaccharide	604:615	arg1	N-acetyllactosaminitol					617:638	the disaccharide N-acetyllactosaminitol	600:638	the disaccharide N-acetyllactosaminitol	600:638	beta-Elimination of the [3H]galactose- labeled CK8/18 generated the disaccharide N-acetyllactosaminitol, indicating that cytokeratin 8 and 18 contain single O-linked N-acetylglucosamine residues.
1371281	8	2	theme	biosynthetic	1015:1026	arg1	rates					1044:1048	The biosynthetic and degradation rates	1011:1048	rates	1044:1048	The biosynthetic and degradation rates of the carbohydrate moiety were faster than the protein core as determined by metabolic radiolabeling or pulse-chase experiments, respectively.
1371281	8	2	theme	biosynthetic	1015:1026	arg1	faster					1082:1087	faster	1082:1087	faster	1082:1087	The biosynthetic and degradation rates of the carbohydrate moiety were faster than the protein core as determined by metabolic radiolabeling or pulse-chase experiments, respectively.
1371281	7	3	theme	multiple	958:965	arg1	peptides					967:974	multiple peptides	958:974	multiple peptides	958:974	Peptide maps of [3H]glucosamine-labeled CK8/18 showed that multiple peptides were labeled with the amino sugar.
1371281	1	4	theme	18	137:138	arg1	glycosylation					91:103	The glycosylation	87:103	The glycosylation of human cytokeratin (CK) 8 and 18	87:138	The glycosylation of human cytokeratin (CK) 8 and 18 was studied after metabolic labeling of HT29 colonic cells with [3H]glucosamine.
1371281	4	5	theme	18	532:533	arg1	labeling					502:509	the labeling	498:509	the labeling of cytokeratin 8 and 18	498:533	In the presence of UDP-[3H]galactose, galactosyltransferase catalyzed the labeling of cytokeratin 8 and 18.
1371281	3	6	theme	Acid	322:325	arg1	hydrolysis					327:336	Acid hydrolysis	322:336	Acid hydrolysis	322:336	Acid hydrolysis of CK8 and CK18, purified from [3H]glucosamine-labeled cells, generated free glucosamine.
1371281	4	7	theme	galactose	455:463	arg1	presence					435:442	the presence	431:442	the presence of UDP-[3H]galactose	431:463	In the presence of UDP-[3H]galactose, galactosyltransferase catalyzed the labeling of cytokeratin 8 and 18.
1371281	10	8	theme	functional	1385:1394	arg1	relevance					1396:1404	functional relevance	1385:1404	functional relevance	1385:1404	Furthermore, CK8/18 glycosylation is a dynamic process which is likely to have functional relevance.
1371281	8	9	theme	pulse-chase	1155:1165	arg1	experiments					1167:1177	pulse-chase experiments	1155:1177	pulse-chase experiments	1155:1177	The biosynthetic and degradation rates of the carbohydrate moiety were faster than the protein core as determined by metabolic radiolabeling or pulse-chase experiments, respectively.
1371281	8	10	theme	degradation	1032:1042	arg1	rates					1044:1048	The biosynthetic and degradation rates	1011:1048	rates	1044:1048	The biosynthetic and degradation rates of the carbohydrate moiety were faster than the protein core as determined by metabolic radiolabeling or pulse-chase experiments, respectively.
1371281	8	10	theme	degradation	1032:1042	arg1	faster					1082:1087	faster	1082:1087	faster	1082:1087	The biosynthetic and degradation rates of the carbohydrate moiety were faster than the protein core as determined by metabolic radiolabeling or pulse-chase experiments, respectively.
1371281	10	11	theme	CK8/18	1319:1324	arg1	process					1353:1359	a dynamic process	1343:1359	a dynamic process which is likely to have functional relevance	1343:1404	Furthermore, CK8/18 glycosylation is a dynamic process which is likely to have functional relevance.
1371281	10	11	theme	CK8/18	1319:1324	arg1	likely					1370:1375	likely	1370:1375	likely	1370:1375	Furthermore, CK8/18 glycosylation is a dynamic process which is likely to have functional relevance.
1371281	10	11	theme	CK8/18	1319:1324	arg1	glycosylation					1326:1338	CK8/18 glycosylation	1319:1338	CK8/18 glycosylation	1319:1338	Furthermore, CK8/18 glycosylation is a dynamic process which is likely to have functional relevance.
1371281	5	12	theme	labeled	575:581	arg1	CK8/18					583:588	the [3H]galactose- labeled CK8/18	556:588	the [3H]galactose- labeled CK8/18	556:588	beta-Elimination of the [3H]galactose- labeled CK8/18 generated the disaccharide N-acetyllactosaminitol, indicating that cytokeratin 8 and 18 contain single O-linked N-acetylglucosamine residues.
1371281	5	13	theme	galactose-	564:573	arg1	CK8/18					583:588	the [3H]galactose- labeled CK8/18	556:588	the [3H]galactose- labeled CK8/18	556:588	beta-Elimination of the [3H]galactose- labeled CK8/18 generated the disaccharide N-acetyllactosaminitol, indicating that cytokeratin 8 and 18 contain single O-linked N-acetylglucosamine residues.
1371281	9	14	gly	glycosylated	1231:1242	arg1	CK8					1216:1218	CK8	1216:1218	CK8	1216:1218	Our results show that CK8 and 18 are glycosylated at multiple sites with a single O-linked N-acetylglucosamine.
1371281	9	14	gly	glycosylated	1231:1242	arg2	sites					1256:1260	multiple sites	1247:1260	multiple sites with a single O-linked N-acetylglucosamine	1247:1303	Our results show that CK8 and 18 are glycosylated at multiple sites with a single O-linked N-acetylglucosamine.
1371281	9	14	gly	glycosylated	1231:1242	arg1	18					1224:1225	18	1224:1225	18	1224:1225	Our results show that CK8 and 18 are glycosylated at multiple sites with a single O-linked N-acetylglucosamine.
1371281	1	15	gly	glycosylation	91:103	arg1	CK					127:128	CK	127:128	CK	127:128	The glycosylation of human cytokeratin (CK) 8 and 18 was studied after metabolic labeling of HT29 colonic cells with [3H]glucosamine.
1371281	1	15	gly	glycosylation	91:103	arg1	cytokeratin					114:124	human cytokeratin	108:124	human cytokeratin (CK)	108:129	The glycosylation of human cytokeratin (CK) 8 and 18 was studied after metabolic labeling of HT29 colonic cells with [3H]glucosamine.
1371281	1	15	gly	glycosylation	91:103	arg1	18					137:138	18	137:138	18	137:138	The glycosylation of human cytokeratin (CK) 8 and 18 was studied after metabolic labeling of HT29 colonic cells with [3H]glucosamine.
1371281	6	16	theme	CK18	879:882	arg1	molecule					859:866	N-acetylglucosamine/protein molecule	831:866	N-acetylglucosamine/protein molecule of CK8 and CK18, respectively	831:896	Using chemical analysis, the stoichiometry of glycosylation was found to be 1.5 and 2 molecules of N-acetylglucosamine/protein molecule of CK8 and CK18, respectively.
1371281	5	17	theme	CK8/18	583:588	arg1	beta-Elimination					536:551	beta-Elimination	536:551	beta-Elimination of the [3H]galactose- labeled CK8/18	536:588	beta-Elimination of the [3H]galactose- labeled CK8/18 generated the disaccharide N-acetyllactosaminitol, indicating that cytokeratin 8 and 18 contain single O-linked N-acetylglucosamine residues.
1371281	7	18	theme	glucosamine-labeled	919:937	arg1	CK8/18					939:944	[3H]glucosamine-labeled CK8/18	915:944	[3H]glucosamine-labeled CK8/18	915:944	Peptide maps of [3H]glucosamine-labeled CK8/18 showed that multiple peptides were labeled with the amino sugar.
1371281	2	19	theme	CK8/18	233:238	arg1	Labeling					221:228	Labeling	221:228	Labeling of CK8/18	221:238	Labeling of CK8/18 was not inhibited by tunicamycin, suggesting that glycosylation was not N-linked.
1371281	9	20	with	sites	1256:1260	arg1	N-acetylglucosamine					1285:1303	a single O-linked N-acetylglucosamine	1267:1303	a single O-linked N-acetylglucosamine	1267:1303	Our results show that CK8 and 18 are glycosylated at multiple sites with a single O-linked N-acetylglucosamine.
1371281	9	21	theme	single	1269:1274	arg1	N-acetylglucosamine					1285:1303	a single O-linked N-acetylglucosamine	1267:1303	a single O-linked N-acetylglucosamine	1267:1303	Our results show that CK8 and 18 are glycosylated at multiple sites with a single O-linked N-acetylglucosamine.
1371281	8	22	theme	moiety	1070:1075	arg1	rates					1044:1048	The biosynthetic and degradation rates	1011:1048	rates	1044:1048	The biosynthetic and degradation rates of the carbohydrate moiety were faster than the protein core as determined by metabolic radiolabeling or pulse-chase experiments, respectively.
1371281	8	22	theme	moiety	1070:1075	arg1	faster					1082:1087	faster	1082:1087	faster	1082:1087	The biosynthetic and degradation rates of the carbohydrate moiety were faster than the protein core as determined by metabolic radiolabeling or pulse-chase experiments, respectively.
1371281	6	23	theme	glycosylation	778:790	arg1	molecules					818:826	1.5 and 2 molecules	808:826	1.5 and 2 molecules of N-acetylglucosamine/protein molecule of CK8 and CK18, respectively	808:896	Using chemical analysis, the stoichiometry of glycosylation was found to be 1.5 and 2 molecules of N-acetylglucosamine/protein molecule of CK8 and CK18, respectively.
1371281	6	23	theme	glycosylation	778:790	arg1	stoichiometry					761:773	the stoichiometry	757:773	the stoichiometry of glycosylation	757:790	Using chemical analysis, the stoichiometry of glycosylation was found to be 1.5 and 2 molecules of N-acetylglucosamine/protein molecule of CK8 and CK18, respectively.
1371281	5	24	theme	single	686:691	arg1	residues					722:729	single O-linked N-acetylglucosamine residues	686:729	single O-linked N-acetylglucosamine residues	686:729	beta-Elimination of the [3H]galactose- labeled CK8/18 generated the disaccharide N-acetyllactosaminitol, indicating that cytokeratin 8 and 18 contain single O-linked N-acetylglucosamine residues.
1371281	3	25	theme	CK18	349:352	arg1	hydrolysis					327:336	Acid hydrolysis	322:336	Acid hydrolysis	322:336	Acid hydrolysis of CK8 and CK18, purified from [3H]glucosamine-labeled cells, generated free glucosamine.
1371281	4	26	theme	cytokeratin	514:524	arg1	labeling					502:509	the labeling	498:509	the labeling of cytokeratin 8 and 18	498:533	In the presence of UDP-[3H]galactose, galactosyltransferase catalyzed the labeling of cytokeratin 8 and 18.
1371281	8	27	theme	carbohydrate	1057:1068	arg1	moiety					1070:1075	the carbohydrate moiety	1053:1075	the carbohydrate moiety	1053:1075	The biosynthetic and degradation rates of the carbohydrate moiety were faster than the protein core as determined by metabolic radiolabeling or pulse-chase experiments, respectively.
1371281	3	28	theme	glucosamine-labeled	373:391	arg1	cells					393:397	[3H]glucosamine-labeled cells	369:397	[3H]glucosamine-labeled cells	369:397	Acid hydrolysis of CK8 and CK18, purified from [3H]glucosamine-labeled cells, generated free glucosamine.
1371281	0	29	link	O-linked	33:40	arg1	glycosylation					42:54	O-linked glycosylation	33:54	O-linked glycosylation of human cytokeratin 8 and 18	33:84	Characterization and dynamics of O-linked glycosylation of human cytokeratin 8 and 18.
1371281	3	30	theme	CK8	341:343	arg1	hydrolysis					327:336	Acid hydrolysis	322:336	Acid hydrolysis	322:336	Acid hydrolysis of CK8 and CK18, purified from [3H]glucosamine-labeled cells, generated free glucosamine.
1371281	5	31	contain	contain	678:684	arg1	18					675:676	18	675:676	18	675:676	beta-Elimination of the [3H]galactose- labeled CK8/18 generated the disaccharide N-acetyllactosaminitol, indicating that cytokeratin 8 and 18 contain single O-linked N-acetylglucosamine residues.
1371281	5	31	contain	contain	678:684	arg1	cytokeratin					657:667	cytokeratin 8 and 18	657:676	cytokeratin	657:667	beta-Elimination of the [3H]galactose- labeled CK8/18 generated the disaccharide N-acetyllactosaminitol, indicating that cytokeratin 8 and 18 contain single O-linked N-acetylglucosamine residues.
1371281	5	31	contain	contain	678:684	arg2	residues					722:729	single O-linked N-acetylglucosamine residues	686:729	single O-linked N-acetylglucosamine residues	686:729	beta-Elimination of the [3H]galactose- labeled CK8/18 generated the disaccharide N-acetyllactosaminitol, indicating that cytokeratin 8 and 18 contain single O-linked N-acetylglucosamine residues.
1371281	10	32	theme	dynamic	1345:1351	arg1	process					1353:1359	a dynamic process	1343:1359	a dynamic process which is likely to have functional relevance	1343:1404	Furthermore, CK8/18 glycosylation is a dynamic process which is likely to have functional relevance.
1371281	10	32	theme	dynamic	1345:1351	arg1	likely					1370:1375	likely	1370:1375	likely	1370:1375	Furthermore, CK8/18 glycosylation is a dynamic process which is likely to have functional relevance.
1371281	10	32	theme	dynamic	1345:1351	arg1	glycosylation					1326:1338	CK8/18 glycosylation	1319:1338	CK8/18 glycosylation	1319:1338	Furthermore, CK8/18 glycosylation is a dynamic process which is likely to have functional relevance.
1371281	6	33	theme	CK8	871:873	arg1	molecule					859:866	N-acetylglucosamine/protein molecule	831:866	N-acetylglucosamine/protein molecule of CK8 and CK18, respectively	831:896	Using chemical analysis, the stoichiometry of glycosylation was found to be 1.5 and 2 molecules of N-acetylglucosamine/protein molecule of CK8 and CK18, respectively.
1371281	9	34	link	O-linked	1276:1283	arg1	N-acetylglucosamine					1285:1303	a single O-linked N-acetylglucosamine	1267:1303	a single O-linked N-acetylglucosamine	1267:1303	Our results show that CK8 and 18 are glycosylated at multiple sites with a single O-linked N-acetylglucosamine.
1371281	0	35	theme	glycosylation	42:54	arg1	dynamics					21:28	dynamics	21:28	dynamics	21:28	Characterization and dynamics of O-linked glycosylation of human cytokeratin 8 and 18.
1371281	0	35	theme	glycosylation	42:54	arg1	Characterization					0:15	Characterization	0:15	Characterization	0:15	Characterization and dynamics of O-linked glycosylation of human cytokeratin 8 and 18.
1371281	1	36	with	labeling	168:175	arg1	glucosamine					208:218	[3H]glucosamine	204:218	[3H]glucosamine	204:218	The glycosylation of human cytokeratin (CK) 8 and 18 was studied after metabolic labeling of HT29 colonic cells with [3H]glucosamine.
1371281	1	37	theme	metabolic	158:166	arg1	labeling					168:175	metabolic labeling	158:175	metabolic labeling of HT29 colonic cells with [3H]glucosamine	158:218	The glycosylation of human cytokeratin (CK) 8 and 18 was studied after metabolic labeling of HT29 colonic cells with [3H]glucosamine.
1371281	1	38	theme	HT29	180:183	arg1	cells					193:197	HT29 colonic cells	180:197	HT29 colonic cells	180:197	The glycosylation of human cytokeratin (CK) 8 and 18 was studied after metabolic labeling of HT29 colonic cells with [3H]glucosamine.
1371281	0	39	theme	O-linked	33:40	arg1	glycosylation					42:54	O-linked glycosylation	33:54	O-linked glycosylation of human cytokeratin 8 and 18	33:84	Characterization and dynamics of O-linked glycosylation of human cytokeratin 8 and 18.
1371281	5	40	theme	O-linked	693:700	arg1	residues					722:729	single O-linked N-acetylglucosamine residues	686:729	single O-linked N-acetylglucosamine residues	686:729	beta-Elimination of the [3H]galactose- labeled CK8/18 generated the disaccharide N-acetyllactosaminitol, indicating that cytokeratin 8 and 18 contain single O-linked N-acetylglucosamine residues.
1371281	6	41	theme	molecule	859:866	arg1	molecules					818:826	1.5 and 2 molecules	808:826	1.5 and 2 molecules of N-acetylglucosamine/protein molecule of CK8 and CK18, respectively	808:896	Using chemical analysis, the stoichiometry of glycosylation was found to be 1.5 and 2 molecules of N-acetylglucosamine/protein molecule of CK8 and CK18, respectively.
1371281	6	41	theme	molecule	859:866	arg1	stoichiometry					761:773	the stoichiometry	757:773	the stoichiometry of glycosylation	757:790	Using chemical analysis, the stoichiometry of glycosylation was found to be 1.5 and 2 molecules of N-acetylglucosamine/protein molecule of CK8 and CK18, respectively.
1371281	3	42	theme	free	410:413	arg1	glucosamine					415:425	free glucosamine	410:425	free glucosamine	410:425	Acid hydrolysis of CK8 and CK18, purified from [3H]glucosamine-labeled cells, generated free glucosamine.
1371281	0	43	theme	human	59:63	arg1	cytokeratin					65:75	human cytokeratin 8 and 18	59:84	cytokeratin	65:75	Characterization and dynamics of O-linked glycosylation of human cytokeratin 8 and 18.
1371281	5	44	theme	N-acetylglucosamine	702:720	arg1	residues					722:729	single O-linked N-acetylglucosamine residues	686:729	single O-linked N-acetylglucosamine residues	686:729	beta-Elimination of the [3H]galactose- labeled CK8/18 generated the disaccharide N-acetyllactosaminitol, indicating that cytokeratin 8 and 18 contain single O-linked N-acetylglucosamine residues.
1371281	6	45	theme	N-acetylglucosamine/protein	831:857	arg1	molecule					859:866	N-acetylglucosamine/protein molecule	831:866	N-acetylglucosamine/protein molecule of CK8 and CK18, respectively	831:896	Using chemical analysis, the stoichiometry of glycosylation was found to be 1.5 and 2 molecules of N-acetylglucosamine/protein molecule of CK8 and CK18, respectively.
1371281	1	46	theme	human	108:112	arg1	CK					127:128	CK	127:128	CK	127:128	The glycosylation of human cytokeratin (CK) 8 and 18 was studied after metabolic labeling of HT29 colonic cells with [3H]glucosamine.
1371281	1	46	theme	human	108:112	arg1	cytokeratin					114:124	human cytokeratin	108:124	human cytokeratin (CK)	108:129	The glycosylation of human cytokeratin (CK) 8 and 18 was studied after metabolic labeling of HT29 colonic cells with [3H]glucosamine.
1371281	8	47	theme	protein	1098:1104	arg1	core					1106:1109	the protein core	1094:1109	the protein core	1094:1109	The biosynthetic and degradation rates of the carbohydrate moiety were faster than the protein core as determined by metabolic radiolabeling or pulse-chase experiments, respectively.
1371281	9	48	theme	multiple	1247:1254	arg1	sites					1256:1260	multiple sites	1247:1260	multiple sites with a single O-linked N-acetylglucosamine	1247:1303	Our results show that CK8 and 18 are glycosylated at multiple sites with a single O-linked N-acetylglucosamine.
1371281	7	49	theme	amino	998:1002	arg1	sugar					1004:1008	the amino sugar	994:1008	the amino sugar	994:1008	Peptide maps of [3H]glucosamine-labeled CK8/18 showed that multiple peptides were labeled with the amino sugar.
1371281	1	50	theme	cytokeratin	114:124	arg1	glycosylation					91:103	The glycosylation	87:103	The glycosylation of human cytokeratin (CK) 8 and 18	87:138	The glycosylation of human cytokeratin (CK) 8 and 18 was studied after metabolic labeling of HT29 colonic cells with [3H]glucosamine.
1371281	10	51	contain	have	1380:1383	arg1	process					1353:1359	a dynamic process	1343:1359	a dynamic process which is likely to have functional relevance	1343:1404	Furthermore, CK8/18 glycosylation is a dynamic process which is likely to have functional relevance.
1371281	10	51	contain	have	1380:1383	arg1	likely					1370:1375	likely	1370:1375	likely	1370:1375	Furthermore, CK8/18 glycosylation is a dynamic process which is likely to have functional relevance.
1371281	10	51	contain	have	1380:1383	arg1	glycosylation					1326:1338	CK8/18 glycosylation	1319:1338	CK8/18 glycosylation	1319:1338	Furthermore, CK8/18 glycosylation is a dynamic process which is likely to have functional relevance.
1371281	10	51	contain	have	1380:1383	arg2	relevance					1396:1404	functional relevance	1385:1404	functional relevance	1385:1404	Furthermore, CK8/18 glycosylation is a dynamic process which is likely to have functional relevance.
1371281	6	52	theme	chemical	738:745	arg1	analysis					747:754	chemical analysis	738:754	chemical analysis	738:754	Using chemical analysis, the stoichiometry of glycosylation was found to be 1.5 and 2 molecules of N-acetylglucosamine/protein molecule of CK8 and CK18, respectively.
1371281	1	53	theme	cells	193:197	arg1	labeling					168:175	metabolic labeling	158:175	metabolic labeling of HT29 colonic cells with [3H]glucosamine	158:218	The glycosylation of human cytokeratin (CK) 8 and 18 was studied after metabolic labeling of HT29 colonic cells with [3H]glucosamine.
1371281	0	54	gly	glycosylation	42:54	arg1	cytokeratin					65:75	human cytokeratin 8 and 18	59:84	cytokeratin	65:75	Characterization and dynamics of O-linked glycosylation of human cytokeratin 8 and 18.
1371281	0	54	gly	glycosylation	42:54	arg1	18					83:84	18	83:84	18	83:84	Characterization and dynamics of O-linked glycosylation of human cytokeratin 8 and 18.
1371281	7	55	theme	CK8/18	939:944	arg1	maps					907:910	Peptide maps	899:910	Peptide maps of [3H]glucosamine-labeled CK8/18	899:944	Peptide maps of [3H]glucosamine-labeled CK8/18 showed that multiple peptides were labeled with the amino sugar.
1371281	8	56	theme	metabolic	1128:1136	arg1	radiolabeling					1138:1150	metabolic radiolabeling	1128:1150	metabolic radiolabeling	1128:1150	The biosynthetic and degradation rates of the carbohydrate moiety were faster than the protein core as determined by metabolic radiolabeling or pulse-chase experiments, respectively.
1371281	1	57	theme	colonic	185:191	arg1	cells					193:197	HT29 colonic cells	180:197	HT29 colonic cells	180:197	The glycosylation of human cytokeratin (CK) 8 and 18 was studied after metabolic labeling of HT29 colonic cells with [3H]glucosamine.
1371281	7	58	theme	Peptide	899:905	arg1	maps					907:910	Peptide maps	899:910	Peptide maps of [3H]glucosamine-labeled CK8/18	899:944	Peptide maps of [3H]glucosamine-labeled CK8/18 showed that multiple peptides were labeled with the amino sugar.
1371281	0	59	theme	cytokeratin	65:75	arg1	glycosylation					42:54	O-linked glycosylation	33:54	O-linked glycosylation of human cytokeratin 8 and 18	33:84	Characterization and dynamics of O-linked glycosylation of human cytokeratin 8 and 18.
1371281	9	60	theme	O-linked	1276:1283	arg1	N-acetylglucosamine					1285:1303	a single O-linked N-acetylglucosamine	1267:1303	a single O-linked N-acetylglucosamine	1267:1303	Our results show that CK8 and 18 are glycosylated at multiple sites with a single O-linked N-acetylglucosamine.
1371281	5	61	link	O-linked	693:700	arg1	residues					722:729	single O-linked N-acetylglucosamine residues	686:729	single O-linked N-acetylglucosamine residues	686:729	beta-Elimination of the [3H]galactose- labeled CK8/18 generated the disaccharide N-acetyllactosaminitol, indicating that cytokeratin 8 and 18 contain single O-linked N-acetylglucosamine residues.
11418126	1	0	from	present	172:178	arg1	lipoprotein					196:206	high-density lipoprotein	183:206	high-density lipoprotein	183:206	Apolipoprotein M (apoM) is a novel apolipoprotein that is predominantly present in high-density lipoprotein.
11418126	0	1	theme	site-directed	73:85	arg1	mutagenesis					87:97	site-directed mutagenesis	73:97	site-directed mutagenesis	73:97	Proposed lipocalin fold for apolipoprotein M based on bioinformatics and site-directed mutagenesis.
11418126	5	2	theme	strong	672:677	arg1	one					730:732	one	730:732	one	730:732	ApoM displays two strong acidic patches of potential functional importance, one around the N-terminus and the other next to the opening of the beta-barrel.
11418126	5	2	theme	strong	672:677	arg1	other					764:768	other	764:768	other	764:768	ApoM displays two strong acidic patches of potential functional importance, one around the N-terminus and the other next to the opening of the beta-barrel.
11418126	5	2	theme	strong	672:677	arg1	patches					686:692	two strong acidic patches	668:692	two strong acidic patches of potential functional importance	668:727	ApoM displays two strong acidic patches of potential functional importance, one around the N-terminus and the other next to the opening of the beta-barrel.
11418126	1	3	located	present	172:178	arg2	apolipoprotein					135:148	a novel apolipoprotein	127:148	a novel apolipoprotein that is predominantly present in high-density lipoprotein	127:206	Apolipoprotein M (apoM) is a novel apolipoprotein that is predominantly present in high-density lipoprotein.
11418126	1	3	located	present	172:178	arg2	M					115:115	Apolipoprotein M	100:115	Apolipoprotein M (apoM)	100:122	Apolipoprotein M (apoM) is a novel apolipoprotein that is predominantly present in high-density lipoprotein.
11418126	1	3	located	present	172:178	arg2	present					172:178	present	172:178	present	172:178	Apolipoprotein M (apoM) is a novel apolipoprotein that is predominantly present in high-density lipoprotein.
11418126	1	3	located	present	172:178	arg1	lipoprotein					196:206	high-density lipoprotein	183:206	high-density lipoprotein	183:206	Apolipoprotein M (apoM) is a novel apolipoprotein that is predominantly present in high-density lipoprotein.
11418126	3	4	theme	3D	370:371	arg1	model					373:377	a 3D model	368:377	a 3D model	368:377	In a 3D model, characterized by an eight-stranded anti-parallel beta-barrel, a segment including Asn135 could adopt a closed or open conformation.
11418126	5	5	theme	acidic	679:684	arg1	one					730:732	one	730:732	one	730:732	ApoM displays two strong acidic patches of potential functional importance, one around the N-terminus and the other next to the opening of the beta-barrel.
11418126	5	5	theme	acidic	679:684	arg1	other					764:768	other	764:768	other	764:768	ApoM displays two strong acidic patches of potential functional importance, one around the N-terminus and the other next to the opening of the beta-barrel.
11418126	5	5	theme	acidic	679:684	arg1	patches					686:692	two strong acidic patches	668:692	two strong acidic patches of potential functional importance	668:727	ApoM displays two strong acidic patches of potential functional importance, one around the N-terminus and the other next to the opening of the beta-barrel.
11418126	2	6	theme	lipocalin	339:347	arg1	family					357:362	the lipocalin protein family	335:362	the lipocalin protein family	335:362	Sensitive sequence searches, threading and comparative model building experiments revealed apoM to be structurally related to the lipocalin protein family.
11418126	4	7	gly	glycosylated	592:603	arg1	Asn135					561:566	Asn135	561:566	Asn135 in wild-type apoM to be glycosylated	561:603	Using site-directed mutagenesis, we demonstrated Asn135 in wild-type apoM to be glycosylated, suggesting that the segment is solvent exposed.
11418126	0	8	theme	lipocalin	9:17	arg1	fold					19:22	Proposed lipocalin fold	0:22	Proposed lipocalin fold for apolipoprotein M	0:43	Proposed lipocalin fold for apolipoprotein M based on bioinformatics and site-directed mutagenesis.
11418126	0	9	theme	Proposed	0:7	arg1	fold					19:22	Proposed lipocalin fold	0:22	Proposed lipocalin fold for apolipoprotein M	0:43	Proposed lipocalin fold for apolipoprotein M based on bioinformatics and site-directed mutagenesis.
11418126	1	10	theme	Apolipoprotein	100:113	arg1	apolipoprotein					135:148	a novel apolipoprotein	127:148	a novel apolipoprotein that is predominantly present in high-density lipoprotein	127:206	Apolipoprotein M (apoM) is a novel apolipoprotein that is predominantly present in high-density lipoprotein.
11418126	1	10	theme	Apolipoprotein	100:113	arg1	apoM					118:121	apoM	118:121	apoM	118:121	Apolipoprotein M (apoM) is a novel apolipoprotein that is predominantly present in high-density lipoprotein.
11418126	1	10	theme	Apolipoprotein	100:113	arg1	M					115:115	Apolipoprotein M	100:115	Apolipoprotein M (apoM)	100:122	Apolipoprotein M (apoM) is a novel apolipoprotein that is predominantly present in high-density lipoprotein.
11418126	1	10	theme	Apolipoprotein	100:113	arg1	present					172:178	present	172:178	present	172:178	Apolipoprotein M (apoM) is a novel apolipoprotein that is predominantly present in high-density lipoprotein.
11418126	1	11	theme	high-density	183:194	arg1	lipoprotein					196:206	high-density lipoprotein	183:206	high-density lipoprotein	183:206	Apolipoprotein M (apoM) is a novel apolipoprotein that is predominantly present in high-density lipoprotein.
11418126	4	12	theme	wild-type	571:579	arg1	apoM					581:584	wild-type apoM	571:584	wild-type apoM	571:584	Using site-directed mutagenesis, we demonstrated Asn135 in wild-type apoM to be glycosylated, suggesting that the segment is solvent exposed.
11418126	1	13	attach	present	172:178	arg2	apolipoprotein					135:148	a novel apolipoprotein	127:148	a novel apolipoprotein that is predominantly present in high-density lipoprotein	127:206	Apolipoprotein M (apoM) is a novel apolipoprotein that is predominantly present in high-density lipoprotein.
11418126	1	13	attach	present	172:178	arg2	M					115:115	Apolipoprotein M	100:115	Apolipoprotein M (apoM)	100:122	Apolipoprotein M (apoM) is a novel apolipoprotein that is predominantly present in high-density lipoprotein.
11418126	1	13	attach	present	172:178	arg2	present					172:178	present	172:178	present	172:178	Apolipoprotein M (apoM) is a novel apolipoprotein that is predominantly present in high-density lipoprotein.
11418126	1	13	attach	present	172:178	arg1	lipoprotein					196:206	high-density lipoprotein	183:206	high-density lipoprotein	183:206	Apolipoprotein M (apoM) is a novel apolipoprotein that is predominantly present in high-density lipoprotein.
11418126	3	14	theme	closed	483:488	arg1	conformation					498:509	a closed or open conformation	481:509	a closed or open conformation	481:509	In a 3D model, characterized by an eight-stranded anti-parallel beta-barrel, a segment including Asn135 could adopt a closed or open conformation.
11418126	0	15	theme	apolipoprotein	28:41	arg1	M					43:43	apolipoprotein M	28:43	apolipoprotein M	28:43	Proposed lipocalin fold for apolipoprotein M based on bioinformatics and site-directed mutagenesis.
11418126	4	16	from	Asn135	561:566	arg1	apoM					581:584	wild-type apoM	571:584	wild-type apoM	571:584	Using site-directed mutagenesis, we demonstrated Asn135 in wild-type apoM to be glycosylated, suggesting that the segment is solvent exposed.
11418126	2	17	theme	threading	238:246	arg1	building					270:277	threading and comparative model building	238:277	threading and comparative model building experiments	238:289	Sensitive sequence searches, threading and comparative model building experiments revealed apoM to be structurally related to the lipocalin protein family.
11418126	3	18	theme	eight-stranded	400:413	arg1	beta-barrel					429:439	an eight-stranded anti-parallel beta-barrel	397:439	an eight-stranded anti-parallel beta-barrel	397:439	In a 3D model, characterized by an eight-stranded anti-parallel beta-barrel, a segment including Asn135 could adopt a closed or open conformation.
11418126	3	19	theme	anti-parallel	415:427	arg1	beta-barrel					429:439	an eight-stranded anti-parallel beta-barrel	397:439	an eight-stranded anti-parallel beta-barrel	397:439	In a 3D model, characterized by an eight-stranded anti-parallel beta-barrel, a segment including Asn135 could adopt a closed or open conformation.
11418126	5	20	theme	potential	697:705	arg1	importance					718:727	potential functional importance	697:727	potential functional importance	697:727	ApoM displays two strong acidic patches of potential functional importance, one around the N-terminus and the other next to the opening of the beta-barrel.
11418126	2	21	theme	sequence	219:226	arg1	searches					228:235	Sensitive sequence searches	209:235	Sensitive sequence searches	209:235	Sensitive sequence searches, threading and comparative model building experiments revealed apoM to be structurally related to the lipocalin protein family.
11418126	2	21	theme	sequence	219:226	arg1	experiments					279:289	threading and comparative model building experiments	238:289	threading and comparative model building experiments	238:289	Sensitive sequence searches, threading and comparative model building experiments revealed apoM to be structurally related to the lipocalin protein family.
11418126	1	22	from	lipoprotein	196:206	arg1	apolipoprotein					135:148	a novel apolipoprotein	127:148	a novel apolipoprotein that is predominantly present in high-density lipoprotein	127:206	Apolipoprotein M (apoM) is a novel apolipoprotein that is predominantly present in high-density lipoprotein.
11418126	1	22	from	lipoprotein	196:206	arg1	M					115:115	Apolipoprotein M	100:115	Apolipoprotein M (apoM)	100:122	Apolipoprotein M (apoM) is a novel apolipoprotein that is predominantly present in high-density lipoprotein.
11418126	1	22	from	lipoprotein	196:206	arg1	present					172:178	present	172:178	present	172:178	Apolipoprotein M (apoM) is a novel apolipoprotein that is predominantly present in high-density lipoprotein.
11418126	5	23	theme	functional	707:716	arg1	importance					718:727	potential functional importance	697:727	potential functional importance	697:727	ApoM displays two strong acidic patches of potential functional importance, one around the N-terminus and the other next to the opening of the beta-barrel.
11418126	2	24	theme	Sensitive	209:217	arg1	searches					228:235	Sensitive sequence searches	209:235	Sensitive sequence searches	209:235	Sensitive sequence searches, threading and comparative model building experiments revealed apoM to be structurally related to the lipocalin protein family.
11418126	2	24	theme	Sensitive	209:217	arg1	experiments					279:289	threading and comparative model building experiments	238:289	threading and comparative model building experiments	238:289	Sensitive sequence searches, threading and comparative model building experiments revealed apoM to be structurally related to the lipocalin protein family.
11418126	2	25	theme	protein	349:355	arg1	family					357:362	the lipocalin protein family	335:362	the lipocalin protein family	335:362	Sensitive sequence searches, threading and comparative model building experiments revealed apoM to be structurally related to the lipocalin protein family.
11418126	5	26	theme	importance	718:727	arg1	one					730:732	one	730:732	one	730:732	ApoM displays two strong acidic patches of potential functional importance, one around the N-terminus and the other next to the opening of the beta-barrel.
11418126	5	26	theme	importance	718:727	arg1	other					764:768	other	764:768	other	764:768	ApoM displays two strong acidic patches of potential functional importance, one around the N-terminus and the other next to the opening of the beta-barrel.
11418126	5	26	theme	importance	718:727	arg1	patches					686:692	two strong acidic patches	668:692	two strong acidic patches of potential functional importance	668:727	ApoM displays two strong acidic patches of potential functional importance, one around the N-terminus and the other next to the opening of the beta-barrel.
11418126	2	27	theme	building	270:277	arg1	searches					228:235	Sensitive sequence searches	209:235	Sensitive sequence searches	209:235	Sensitive sequence searches, threading and comparative model building experiments revealed apoM to be structurally related to the lipocalin protein family.
11418126	2	27	theme	building	270:277	arg1	experiments					279:289	threading and comparative model building experiments	238:289	threading and comparative model building experiments	238:289	Sensitive sequence searches, threading and comparative model building experiments revealed apoM to be structurally related to the lipocalin protein family.
11418126	3	28	theme	open	493:496	arg1	conformation					498:509	a closed or open conformation	481:509	a closed or open conformation	481:509	In a 3D model, characterized by an eight-stranded anti-parallel beta-barrel, a segment including Asn135 could adopt a closed or open conformation.
11418126	2	29	theme	model	264:268	arg1	building					270:277	threading and comparative model building	238:277	threading and comparative model building experiments	238:289	Sensitive sequence searches, threading and comparative model building experiments revealed apoM to be structurally related to the lipocalin protein family.
11418126	1	30	theme	novel	129:133	arg1	apolipoprotein					135:148	a novel apolipoprotein	127:148	a novel apolipoprotein that is predominantly present in high-density lipoprotein	127:206	Apolipoprotein M (apoM) is a novel apolipoprotein that is predominantly present in high-density lipoprotein.
11418126	1	30	theme	novel	129:133	arg1	M					115:115	Apolipoprotein M	100:115	Apolipoprotein M (apoM)	100:122	Apolipoprotein M (apoM) is a novel apolipoprotein that is predominantly present in high-density lipoprotein.
11418126	1	30	theme	novel	129:133	arg1	present					172:178	present	172:178	present	172:178	Apolipoprotein M (apoM) is a novel apolipoprotein that is predominantly present in high-density lipoprotein.
11418126	5	31	theme	beta-barrel	797:807	arg1	opening					782:788	the opening	778:788	the opening of the beta-barrel	778:807	ApoM displays two strong acidic patches of potential functional importance, one around the N-terminus and the other next to the opening of the beta-barrel.
11418126	4	32	theme	site-directed	518:530	arg1	mutagenesis					532:542	site-directed mutagenesis	518:542	site-directed mutagenesis	518:542	Using site-directed mutagenesis, we demonstrated Asn135 in wild-type apoM to be glycosylated, suggesting that the segment is solvent exposed.
11418126	2	33	theme	comparative	252:262	arg1	building					270:277	threading and comparative model building	238:277	threading and comparative model building experiments	238:289	Sensitive sequence searches, threading and comparative model building experiments revealed apoM to be structurally related to the lipocalin protein family.
11418126	4	34	dep	solvent	637:643	arg1	segment					626:632	the segment	622:632	the segment	622:632	Using site-directed mutagenesis, we demonstrated Asn135 in wild-type apoM to be glycosylated, suggesting that the segment is solvent exposed.
11418126	4	34	dep	solvent	637:643	arg1	exposed					645:651	exposed	645:651	exposed	645:651	Using site-directed mutagenesis, we demonstrated Asn135 in wild-type apoM to be glycosylated, suggesting that the segment is solvent exposed.
11418126	4	34	dep	solvent	637:643	arg1	solvent					637:643	solvent	637:643	solvent	637:643	Using site-directed mutagenesis, we demonstrated Asn135 in wild-type apoM to be glycosylated, suggesting that the segment is solvent exposed.
21768352	3	0	theme	enzyme	325:330	arg1	fI					348:349	fI	348:349	fI	348:349	We have determined the crystal structure of the complement regulatory enzyme human factor I (fI).
21768352	3	0	theme	enzyme	325:330	arg1	I					345:345	the complement regulatory enzyme human factor I	299:345	the complement regulatory enzyme human factor I (fI)	299:350	We have determined the crystal structure of the complement regulatory enzyme human factor I (fI).
21768352	5	1	theme	functional	517:526	arg1	data					528:531	functional data	517:531	functional data from mutants of fI	517:550	Mapping of functional data from mutants of fI onto the structure suggests that this inactive form is maintained by the noncatalytic heavy-chain allosterically modulating activity of the light chain.
21768352	0	2	theme	sequence	76:83	arg1	polymorphisms					85:97	its disease-associated sequence polymorphisms	53:97	its disease-associated sequence polymorphisms	53:97	Structural basis for complement factor I control and its disease-associated sequence polymorphisms.
21768352	5	3	theme	noncatalytic	625:636	arg1	heavy-chain					638:648	the noncatalytic heavy-chain	621:648	the noncatalytic heavy-chain	621:648	Mapping of functional data from mutants of fI onto the structure suggests that this inactive form is maintained by the noncatalytic heavy-chain allosterically modulating activity of the light chain.
21768352	4	4	theme	inactive	380:387	arg1	form					389:392	a proteolytically inactive form	362:392	a proteolytically inactive form	362:392	FI is in a proteolytically inactive form, demonstrating that it circulates in a zymogen-like state despite being fully processed to the mature sequence.
21768352	1	5	theme	adaptive	155:162	arg1	responses					171:179	innate and adaptive immune responses	144:179	innate and adaptive immune responses	144:179	The complement system is a key component of innate and adaptive immune responses.
21768352	5	6	theme	light	692:696	arg1	chain					698:702	the light chain	688:702	the light chain	688:702	Mapping of functional data from mutants of fI onto the structure suggests that this inactive form is maintained by the noncatalytic heavy-chain allosterically modulating activity of the light chain.
21768352	4	7	theme	mature	489:494	arg1	sequence					496:503	the mature sequence	485:503	the mature sequence	485:503	FI is in a proteolytically inactive form, demonstrating that it circulates in a zymogen-like state despite being fully processed to the mature sequence.
21768352	7	8	from	cofactors	1018:1026	arg1	basis					962:966	the molecular basis	948:966	the molecular basis of disease-associated polymorphisms in fI and its cofactors	948:1026	In addition to explaining how circulating fI is limited to cleaving only C3b/C4b, our model explains the molecular basis of disease-associated polymorphisms in fI and its cofactors.
21768352	7	9	dep	explaining	862:871	arg1	addition					850:857	addition	850:857	addition	850:857	In addition to explaining how circulating fI is limited to cleaving only C3b/C4b, our model explains the molecular basis of disease-associated polymorphisms in fI and its cofactors.
21768352	5	10	theme	inactive	590:597	arg1	form					599:602	this inactive form	585:602	this inactive form	585:602	Mapping of functional data from mutants of fI onto the structure suggests that this inactive form is maintained by the noncatalytic heavy-chain allosterically modulating activity of the light chain.
21768352	1	11	theme	immune	164:169	arg1	responses					171:179	innate and adaptive immune responses	144:179	innate and adaptive immune responses	144:179	The complement system is a key component of innate and adaptive immune responses.
21768352	5	12	theme	fI	549:550	arg1	mutants					538:544	mutants	538:544	mutants of fI	538:550	Mapping of functional data from mutants of fI onto the structure suggests that this inactive form is maintained by the noncatalytic heavy-chain allosterically modulating activity of the light chain.
21768352	1	13	theme	responses	171:179	arg1	component					131:139	a key component	125:139	a key component of innate and adaptive immune responses	125:179	The complement system is a key component of innate and adaptive immune responses.
21768352	1	13	theme	responses	171:179	arg1	system					115:120	The complement system	100:120	The complement system	100:120	The complement system is a key component of innate and adaptive immune responses.
21768352	3	14	theme	human	332:336	arg1	fI					348:349	fI	348:349	fI	348:349	We have determined the crystal structure of the complement regulatory enzyme human factor I (fI).
21768352	3	14	theme	human	332:336	arg1	I					345:345	the complement regulatory enzyme human factor I	299:345	the complement regulatory enzyme human factor I (fI)	299:350	We have determined the crystal structure of the complement regulatory enzyme human factor I (fI).
21768352	0	15	theme	disease-associated	57:74	arg1	polymorphisms					85:97	its disease-associated sequence polymorphisms	53:97	its disease-associated sequence polymorphisms	53:97	Structural basis for complement factor I control and its disease-associated sequence polymorphisms.
21768352	0	16	theme	Structural	0:9	arg1	basis					11:15	Structural basis	0:15	Structural basis for complement factor I control and its disease-associated sequence polymorphisms.	0:98	Structural basis for complement factor I control and its disease-associated sequence polymorphisms.
21768352	7	17	theme	circulating	877:887	arg1	fI					889:890	circulating fI	877:890	circulating fI	877:890	In addition to explaining how circulating fI is limited to cleaving only C3b/C4b, our model explains the molecular basis of disease-associated polymorphisms in fI and its cofactors.
21768352	5	18	from	Mapping	506:512	arg1	mutants					538:544	mutants	538:544	mutants of fI	538:550	Mapping of functional data from mutants of fI onto the structure suggests that this inactive form is maintained by the noncatalytic heavy-chain allosterically modulating activity of the light chain.
21768352	0	19	theme	complement	21:30	arg1	control					41:47	complement factor I control	21:47	complement factor I control	21:47	Structural basis for complement factor I control and its disease-associated sequence polymorphisms.
21768352	3	20	theme	crystal	278:284	arg1	structure					286:294	the crystal structure	274:294	the crystal structure of the complement regulatory enzyme human factor I (fI)	274:350	We have determined the crystal structure of the complement regulatory enzyme human factor I (fI).
21768352	1	21	theme	complement	104:113	arg1	component					131:139	a key component	125:139	a key component of innate and adaptive immune responses	125:179	The complement system is a key component of innate and adaptive immune responses.
21768352	1	21	theme	complement	104:113	arg1	system					115:120	The complement system	100:120	The complement system	100:120	The complement system is a key component of innate and adaptive immune responses.
21768352	6	22	theme	allosteric	779:788	arg1	inhibition					790:799	the allosteric inhibition	775:799	the allosteric inhibition	775:799	Once the ternary complex of fI, a cofactor and a substrate is formed, the allosteric inhibition is released, and fI is oriented for cleavage.
21768352	5	23	from	mutants	538:544	arg1	Mapping					506:512	Mapping	506:512	Mapping of functional data from mutants of fI onto the structure	506:569	Mapping of functional data from mutants of fI onto the structure suggests that this inactive form is maintained by the noncatalytic heavy-chain allosterically modulating activity of the light chain.
21768352	5	23	from	mutants	538:544	arg1	data					528:531	functional data	517:531	functional data from mutants of fI	517:550	Mapping of functional data from mutants of fI onto the structure suggests that this inactive form is maintained by the noncatalytic heavy-chain allosterically modulating activity of the light chain.
21768352	5	24	theme	chain	698:702	arg1	activity					676:683	activity	676:683	activity of the light chain	676:702	Mapping of functional data from mutants of fI onto the structure suggests that this inactive form is maintained by the noncatalytic heavy-chain allosterically modulating activity of the light chain.
21768352	2	25	theme	Complement	182:191	arg1	regulation					193:202	Complement regulation	182:202	Complement regulation	182:202	Complement regulation is critical for prevention and control of disease.
21768352	0	26	theme	I	39:39	arg1	control					41:47	complement factor I control	21:47	complement factor I control	21:47	Structural basis for complement factor I control and its disease-associated sequence polymorphisms.
21768352	7	27	from	basis	962:966	arg1	fI					1007:1008	fI	1007:1008	fI	1007:1008	In addition to explaining how circulating fI is limited to cleaving only C3b/C4b, our model explains the molecular basis of disease-associated polymorphisms in fI and its cofactors.
21768352	7	27	from	basis	962:966	arg1	cofactors					1018:1026	its cofactors	1014:1026	its cofactors	1014:1026	In addition to explaining how circulating fI is limited to cleaving only C3b/C4b, our model explains the molecular basis of disease-associated polymorphisms in fI and its cofactors.
21768352	0	28	theme	factor	32:37	arg1	control					41:47	complement factor I control	21:47	complement factor I control	21:47	Structural basis for complement factor I control and its disease-associated sequence polymorphisms.
21768352	5	29	theme	data	528:531	arg1	Mapping					506:512	Mapping	506:512	Mapping of functional data from mutants of fI onto the structure	506:569	Mapping of functional data from mutants of fI onto the structure suggests that this inactive form is maintained by the noncatalytic heavy-chain allosterically modulating activity of the light chain.
21768352	3	30	theme	complement	303:312	arg1	fI					348:349	fI	348:349	fI	348:349	We have determined the crystal structure of the complement regulatory enzyme human factor I (fI).
21768352	3	30	theme	complement	303:312	arg1	I					345:345	the complement regulatory enzyme human factor I	299:345	the complement regulatory enzyme human factor I (fI)	299:350	We have determined the crystal structure of the complement regulatory enzyme human factor I (fI).
21768352	4	31	theme	zymogen-like	433:444	arg1	state					446:450	a zymogen-like state	431:450	a zymogen-like state	431:450	FI is in a proteolytically inactive form, demonstrating that it circulates in a zymogen-like state despite being fully processed to the mature sequence.
21768352	3	32	theme	regulatory	314:323	arg1	fI					348:349	fI	348:349	fI	348:349	We have determined the crystal structure of the complement regulatory enzyme human factor I (fI).
21768352	3	32	theme	regulatory	314:323	arg1	I					345:345	the complement regulatory enzyme human factor I	299:345	the complement regulatory enzyme human factor I (fI)	299:350	We have determined the crystal structure of the complement regulatory enzyme human factor I (fI).
21768352	7	33	theme	disease-associated	971:988	arg1	polymorphisms					990:1002	disease-associated polymorphisms	971:1002	disease-associated polymorphisms in fI and its cofactors	971:1026	In addition to explaining how circulating fI is limited to cleaving only C3b/C4b, our model explains the molecular basis of disease-associated polymorphisms in fI and its cofactors.
21768352	6	34	theme	fI	733:734	arg1	complex					722:728	the ternary complex	710:728	the ternary complex of fI, a cofactor and a substrate	710:762	Once the ternary complex of fI, a cofactor and a substrate is formed, the allosteric inhibition is released, and fI is oriented for cleavage.
21768352	1	35	theme	key	127:129	arg1	component					131:139	a key component	125:139	a key component of innate and adaptive immune responses	125:179	The complement system is a key component of innate and adaptive immune responses.
21768352	1	35	theme	key	127:129	arg1	system					115:120	The complement system	100:120	The complement system	100:120	The complement system is a key component of innate and adaptive immune responses.
21768352	7	36	theme	polymorphisms	990:1002	arg1	basis					962:966	the molecular basis	948:966	the molecular basis of disease-associated polymorphisms in fI and its cofactors	948:1026	In addition to explaining how circulating fI is limited to cleaving only C3b/C4b, our model explains the molecular basis of disease-associated polymorphisms in fI and its cofactors.
21768352	7	37	from	polymorphisms	990:1002	arg1	fI					1007:1008	fI	1007:1008	fI	1007:1008	In addition to explaining how circulating fI is limited to cleaving only C3b/C4b, our model explains the molecular basis of disease-associated polymorphisms in fI and its cofactors.
21768352	7	37	from	polymorphisms	990:1002	arg1	cofactors					1018:1026	its cofactors	1014:1026	its cofactors	1014:1026	In addition to explaining how circulating fI is limited to cleaving only C3b/C4b, our model explains the molecular basis of disease-associated polymorphisms in fI and its cofactors.
21768352	3	38	theme	factor	338:343	arg1	fI					348:349	fI	348:349	fI	348:349	We have determined the crystal structure of the complement regulatory enzyme human factor I (fI).
21768352	3	38	theme	factor	338:343	arg1	I					345:345	the complement regulatory enzyme human factor I	299:345	the complement regulatory enzyme human factor I (fI)	299:350	We have determined the crystal structure of the complement regulatory enzyme human factor I (fI).
21768352	7	39	theme	molecular	952:960	arg1	basis					962:966	the molecular basis	948:966	the molecular basis of disease-associated polymorphisms in fI and its cofactors	948:1026	In addition to explaining how circulating fI is limited to cleaving only C3b/C4b, our model explains the molecular basis of disease-associated polymorphisms in fI and its cofactors.
21768352	3	40	theme	I	345:345	arg1	structure					286:294	the crystal structure	274:294	the crystal structure of the complement regulatory enzyme human factor I (fI)	274:350	We have determined the crystal structure of the complement regulatory enzyme human factor I (fI).
21768352	2	41	theme	disease	246:252	arg1	control					235:241	control	235:241	control	235:241	Complement regulation is critical for prevention and control of disease.
21768352	2	41	theme	disease	246:252	arg1	prevention					220:229	prevention	220:229	prevention	220:229	Complement regulation is critical for prevention and control of disease.
21768352	6	42	theme	ternary	714:720	arg1	complex					722:728	the ternary complex	710:728	the ternary complex of fI, a cofactor and a substrate	710:762	Once the ternary complex of fI, a cofactor and a substrate is formed, the allosteric inhibition is released, and fI is oriented for cleavage.
21768352	1	43	theme	innate	144:149	arg1	responses					171:179	innate and adaptive immune responses	144:179	innate and adaptive immune responses	144:179	The complement system is a key component of innate and adaptive immune responses.
21768352	7	44	from	fI	1007:1008	arg1	basis					962:966	the molecular basis	948:966	the molecular basis of disease-associated polymorphisms in fI and its cofactors	948:1026	In addition to explaining how circulating fI is limited to cleaving only C3b/C4b, our model explains the molecular basis of disease-associated polymorphisms in fI and its cofactors.
7525874	12	0	theme	bisecting	1434:1442	arg1	N-acetylglucosamine					1444:1462	bisecting N-acetylglucosamine	1434:1462	bisecting N-acetylglucosamine	1434:1462	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	12	1	theme	fucosylation	1404:1415	arg1	amounts					1423:1429	high amounts	1418:1429	high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues,	1418:1527	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	12	1	theme	fucosylation	1404:1415	arg1	acid					1575:1578	N-acetylneuraminic acid	1556:1578	N-acetylneuraminic acid in alpha 2,3 linkage	1556:1599	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	12	1	theme	fucosylation	1404:1415	arg1	degree					1394:1399	a high degree	1387:1399	a high degree of fucosylation	1387:1415	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	12	1	theme	fucosylation	1404:1415	arg1	N-acetylglucosamine					1485:1503	terminal N-acetylglucosamine	1476:1503	terminal N-acetylglucosamine	1476:1503	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	12	1	theme	fucosylation	1404:1415	arg1	amounts					1545:1551	significant amounts	1533:1551	significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage	1533:1599	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	12	1	theme	fucosylation	1404:1415	arg1	N-acetylglucosamine					1444:1462	bisecting N-acetylglucosamine	1434:1462	bisecting N-acetylglucosamine	1434:1462	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	1	2	theme	cerebrospinal	182:194	arg1	fluid					196:200	human cerebrospinal fluid	176:200	human cerebrospinal fluid	176:200	The carbohydrate structures of beta-trace protein from human cerebrospinal fluid have been elucidated.
7525874	2	3	dep	sites	290:294	arg1	Asn56					307:311	Asn56	307:311	Asn56	307:311	This protein carries exclusively N-linked oligosaccharides at two sites (Asn29 and Asn56).
7525874	2	3	dep	sites	290:294	arg1	Asn29					297:301	Asn29	297:301	Asn29	297:301	This protein carries exclusively N-linked oligosaccharides at two sites (Asn29 and Asn56).
7525874	2	3	dep	sites	290:294	arg1	sites					290:294	two sites	286:294	two sites (Asn29 and Asn56)	286:312	This protein carries exclusively N-linked oligosaccharides at two sites (Asn29 and Asn56).
7525874	12	4	theme	2,3	1589:1591	arg1	linkage					1593:1599	alpha 2,3 linkage	1583:1599	alpha 2,3 linkage	1583:1599	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	0	5	from	fluid	71:75	arg1	structures					13:22	Carbohydrate structures	0:22	Carbohydrate structures of beta-trace protein from human cerebrospinal fluid: evidence for "brain-type" N-glycosylation.	0:119	Carbohydrate structures of beta-trace protein from human cerebrospinal fluid: evidence for "brain-type" N-glycosylation.
7525874	4	6	theme	acid	635:638	arg1	residues					640:647	N-acetylneuraminic acid residues	616:647	N-acetylneuraminic acid residues	616:647	All glycans were found to be of the complex type, and most (90%) of them were biantennary with no (40%), one (40%), or two (20%) N-acetylneuraminic acid residues.
7525874	12	7	dep	N-acetylglucosamine	1485:1503	arg1	residues					1519:1526	residues	1519:1526	residues	1519:1526	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	1	8	from	fluid	196:200	arg1	structures					138:147	The carbohydrate structures	121:147	The carbohydrate structures of beta-trace protein from human cerebrospinal fluid	121:200	The carbohydrate structures of beta-trace protein from human cerebrospinal fluid have been elucidated.
7525874	12	9	theme	N-acetylneuraminic	1556:1573	arg1	acid					1575:1578	N-acetylneuraminic acid	1556:1578	N-acetylneuraminic acid in alpha 2,3 linkage	1556:1599	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	5	10	with	chains	677:682	arg1	repeats					743:749	intact or truncated lactosamine repeats	711:749	intact or truncated lactosamine repeats	711:749	The rest were triantennary chains or biantennary chains with intact or truncated lactosamine repeats.
7525874	2	11	link	N-linked	257:264	arg1	oligosaccharides					266:281	exclusively N-linked oligosaccharides	245:281	exclusively N-linked oligosaccharides	245:281	This protein carries exclusively N-linked oligosaccharides at two sites (Asn29 and Asn56).
7525874	4	12	with	biantennary	565:575	arg1	no					582:583	no	582:583	no	582:583	All glycans were found to be of the complex type, and most (90%) of them were biantennary with no (40%), one (40%), or two (20%) N-acetylneuraminic acid residues.
7525874	1	13	theme	beta-trace	152:161	arg1	protein					163:169	beta-trace protein	152:169	beta-trace protein	152:169	The carbohydrate structures of beta-trace protein from human cerebrospinal fluid have been elucidated.
7525874	4	14	theme	complex	523:529	arg1	type					531:534	the complex type	519:534	the complex type	519:534	All glycans were found to be of the complex type, and most (90%) of them were biantennary with no (40%), one (40%), or two (20%) N-acetylneuraminic acid residues.
7525874	11	15	theme	glycosylation	1274:1286	arg1	patterns					1288:1295	the site-specific glycosylation patterns	1256:1295	the site-specific glycosylation patterns at Asn29 and Asn56	1256:1314	Analysis of the site-specific glycosylation patterns at Asn29 and Asn56 revealed only minor differences.
7525874	3	16	theme	methylation	382:392	arg1	analyses					394:401	compositional and methylation analyses	364:401	analyses	394:401	Enzymatically released N-glycans were studied by compositional and methylation analyses, high-pH anion-exchange chromatography, and liquid secondary ion mass spectrometry.
7525874	7	17	dep	%	887:887	arg1	20					885:886	20	885:886	20	885:886	Peripheral fucose (about 20% alpha 1,3-linked to N-acetylglucosamine) was also detected.
7525874	3	18	theme	compositional	364:376	arg1	analyses					394:401	compositional and methylation analyses	364:401	analyses	394:401	Enzymatically released N-glycans were studied by compositional and methylation analyses, high-pH anion-exchange chromatography, and liquid secondary ion mass spectrometry.
7525874	0	19	theme	"	102:102	arg1	N-glycosylation					104:118	"brain-type" N-glycosylation	91:118	"brain-type" N-glycosylation	91:118	Carbohydrate structures of beta-trace protein from human cerebrospinal fluid: evidence for "brain-type" N-glycosylation.
7525874	8	20	theme	bisecting	1001:1009	arg1	N-acetylglucosamine					1011:1029	a bisecting N-acetylglucosamine	999:1029	a bisecting N-acetylglucosamine	999:1029	Seventy percent of the oligosaccharides contained a bisecting N-acetylglucosamine.
7525874	3	21	theme	anion-exchange	412:425	arg1	chromatography					427:440	high-pH anion-exchange chromatography	404:440	high-pH anion-exchange chromatography	404:440	Enzymatically released N-glycans were studied by compositional and methylation analyses, high-pH anion-exchange chromatography, and liquid secondary ion mass spectrometry.
7525874	3	22	theme	ion	464:466	arg1	spectrometry					473:484	liquid secondary ion mass spectrometry	447:484	liquid secondary ion mass spectrometry	447:484	Enzymatically released N-glycans were studied by compositional and methylation analyses, high-pH anion-exchange chromatography, and liquid secondary ion mass spectrometry.
7525874	0	23	theme	Carbohydrate	0:11	arg1	structures					13:22	Carbohydrate structures	0:22	Carbohydrate structures of beta-trace protein from human cerebrospinal fluid: evidence for "brain-type" N-glycosylation.	0:119	Carbohydrate structures of beta-trace protein from human cerebrospinal fluid: evidence for "brain-type" N-glycosylation.
7525874	8	24	contain	contained	989:997	arg2	N-acetylglucosamine					1011:1029	a bisecting N-acetylglucosamine	999:1029	a bisecting N-acetylglucosamine	999:1029	Seventy percent of the oligosaccharides contained a bisecting N-acetylglucosamine.
7525874	8	24	contain	contained	989:997	arg1	percent					957:963	Seventy percent	949:963	Seventy percent of the oligosaccharides	949:987	Seventy percent of the oligosaccharides contained a bisecting N-acetylglucosamine.
7525874	12	25	theme	brain-type	1638:1647	arg1	protein					1608:1614	this protein	1603:1614	this protein	1603:1614	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	12	25	theme	brain-type	1638:1647	arg1	"					1648:1648	"brain-type"	1637:1648	"brain-type" glycosylated	1637:1661	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	3	26	theme	liquid	447:452	arg1	spectrometry					473:484	liquid secondary ion mass spectrometry	447:484	liquid secondary ion mass spectrometry	447:484	Enzymatically released N-glycans were studied by compositional and methylation analyses, high-pH anion-exchange chromatography, and liquid secondary ion mass spectrometry.
7525874	0	27	theme	protein	38:44	arg1	structures					13:22	Carbohydrate structures	0:22	Carbohydrate structures of beta-trace protein from human cerebrospinal fluid: evidence for "brain-type" N-glycosylation.	0:119	Carbohydrate structures of beta-trace protein from human cerebrospinal fluid: evidence for "brain-type" N-glycosylation.
7525874	5	28	theme	intact	711:716	arg1	repeats					743:749	intact or truncated lactosamine repeats	711:749	intact or truncated lactosamine repeats	711:749	The rest were triantennary chains or biantennary chains with intact or truncated lactosamine repeats.
7525874	9	29	theme	oligosaccharide	1090:1104	arg1	fractions					1106:1114	the monosialylated oligosaccharide fractions	1071:1114	the monosialylated oligosaccharide fractions	1071:1114	Especially in the neutral, but also in the monosialylated oligosaccharide fractions, many incomplete antennae consisting of N-acetylglucosamine only were present.
7525874	5	30	theme	truncated	721:729	arg1	repeats					743:749	intact or truncated lactosamine repeats	711:749	intact or truncated lactosamine repeats	711:749	The rest were triantennary chains or biantennary chains with intact or truncated lactosamine repeats.
7525874	4	31	dep	one	592:594	arg1	residues					640:647	N-acetylneuraminic acid residues	616:647	N-acetylneuraminic acid residues	616:647	All glycans were found to be of the complex type, and most (90%) of them were biantennary with no (40%), one (40%), or two (20%) N-acetylneuraminic acid residues.
7525874	12	32	dep	features	1377:1384	arg1	amounts					1423:1429	high amounts	1418:1429	high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues,	1418:1527	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	12	32	dep	features	1377:1384	arg1	acid					1575:1578	N-acetylneuraminic acid	1556:1578	N-acetylneuraminic acid in alpha 2,3 linkage	1556:1599	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	12	32	dep	features	1377:1384	arg1	degree					1394:1399	a high degree	1387:1399	a high degree of fucosylation	1387:1415	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	12	32	dep	features	1377:1384	arg1	N-acetylglucosamine					1485:1503	terminal N-acetylglucosamine	1476:1503	terminal N-acetylglucosamine	1476:1503	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	12	32	dep	features	1377:1384	arg1	amounts					1545:1551	significant amounts	1533:1551	significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage	1533:1599	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	12	32	dep	features	1377:1384	arg1	N-acetylglucosamine					1444:1462	bisecting N-acetylglucosamine	1434:1462	bisecting N-acetylglucosamine	1434:1462	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	12	33	theme	N-acetylglucosamine	1485:1503	arg1	amounts					1423:1429	high amounts	1418:1429	high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues,	1418:1527	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	12	33	theme	N-acetylglucosamine	1485:1503	arg1	acid					1575:1578	N-acetylneuraminic acid	1556:1578	N-acetylneuraminic acid in alpha 2,3 linkage	1556:1599	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	12	33	theme	N-acetylglucosamine	1485:1503	arg1	degree					1394:1399	a high degree	1387:1399	a high degree of fucosylation	1387:1415	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	12	33	theme	N-acetylglucosamine	1485:1503	arg1	N-acetylglucosamine					1485:1503	terminal N-acetylglucosamine	1476:1503	terminal N-acetylglucosamine	1476:1503	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	12	33	theme	N-acetylglucosamine	1485:1503	arg1	amounts					1545:1551	significant amounts	1533:1551	significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage	1533:1599	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	12	33	theme	N-acetylglucosamine	1485:1503	arg1	N-acetylglucosamine					1444:1462	bisecting N-acetylglucosamine	1434:1462	bisecting N-acetylglucosamine	1434:1462	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	9	34	theme	incomplete	1122:1131	arg1	antennae					1133:1140	many incomplete antennae	1117:1140	many incomplete antennae consisting of N-acetylglucosamine only	1117:1179	Especially in the neutral, but also in the monosialylated oligosaccharide fractions, many incomplete antennae consisting of N-acetylglucosamine only were present.
7525874	11	35	from	Analysis	1244:1251	arg1	Asn29					1300:1304	Asn29	1300:1304	Asn29	1300:1304	Analysis of the site-specific glycosylation patterns at Asn29 and Asn56 revealed only minor differences.
7525874	11	35	from	Analysis	1244:1251	arg1	Asn56					1310:1314	Asn56	1310:1314	Asn56	1310:1314	Analysis of the site-specific glycosylation patterns at Asn29 and Asn56 revealed only minor differences.
7525874	9	36	gly	monosialylated	1075:1088	arg1	fractions					1106:1114	the monosialylated oligosaccharide fractions	1071:1114	the monosialylated oligosaccharide fractions	1071:1114	Especially in the neutral, but also in the monosialylated oligosaccharide fractions, many incomplete antennae consisting of N-acetylglucosamine only were present.
7525874	12	37	theme	N-acetylglucosamine	1444:1462	arg1	amounts					1423:1429	high amounts	1418:1429	high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues,	1418:1527	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	12	37	theme	N-acetylglucosamine	1444:1462	arg1	acid					1575:1578	N-acetylneuraminic acid	1556:1578	N-acetylneuraminic acid in alpha 2,3 linkage	1556:1599	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	12	37	theme	N-acetylglucosamine	1444:1462	arg1	degree					1394:1399	a high degree	1387:1399	a high degree of fucosylation	1387:1415	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	12	37	theme	N-acetylglucosamine	1444:1462	arg1	N-acetylglucosamine					1485:1503	terminal N-acetylglucosamine	1476:1503	terminal N-acetylglucosamine	1476:1503	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	12	37	theme	N-acetylglucosamine	1444:1462	arg1	amounts					1545:1551	significant amounts	1533:1551	significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage	1533:1599	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	12	37	theme	N-acetylglucosamine	1444:1462	arg1	N-acetylglucosamine					1444:1462	bisecting N-acetylglucosamine	1434:1462	bisecting N-acetylglucosamine	1434:1462	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	12	38	from	amounts	1423:1429	arg1	linkage					1593:1599	alpha 2,3 linkage	1583:1599	alpha 2,3 linkage	1583:1599	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	12	39	theme	high	1418:1421	arg1	amounts					1423:1429	high amounts	1418:1429	high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues,	1418:1527	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	12	39	theme	high	1418:1421	arg1	N-acetylglucosamine					1444:1462	bisecting N-acetylglucosamine	1434:1462	bisecting N-acetylglucosamine	1434:1462	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	12	39	theme	high	1418:1421	arg1	N-acetylglucosamine					1485:1503	terminal N-acetylglucosamine	1476:1503	terminal N-acetylglucosamine	1476:1503	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	12	39	theme	high	1418:1421	arg1	degree					1394:1399	a high degree	1387:1399	a high degree of fucosylation	1387:1415	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	12	39	theme	high	1418:1421	arg1	acid					1575:1578	N-acetylneuraminic acid	1556:1578	N-acetylneuraminic acid in alpha 2,3 linkage	1556:1599	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	12	40	theme	high	1389:1392	arg1	amounts					1423:1429	high amounts	1418:1429	high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues,	1418:1527	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	12	40	theme	high	1389:1392	arg1	acid					1575:1578	N-acetylneuraminic acid	1556:1578	N-acetylneuraminic acid in alpha 2,3 linkage	1556:1599	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	12	40	theme	high	1389:1392	arg1	degree					1394:1399	a high degree	1387:1399	a high degree of fucosylation	1387:1415	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	12	40	theme	high	1389:1392	arg1	N-acetylglucosamine					1485:1503	terminal N-acetylglucosamine	1476:1503	terminal N-acetylglucosamine	1476:1503	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	12	40	theme	high	1389:1392	arg1	amounts					1545:1551	significant amounts	1533:1551	significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage	1533:1599	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	12	40	theme	high	1389:1392	arg1	N-acetylglucosamine					1444:1462	bisecting N-acetylglucosamine	1434:1462	bisecting N-acetylglucosamine	1434:1462	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	7	41	dep	fucose	871:876	arg1	alpha					889:893	about 20% alpha	879:893	about 20% alpha 1,3-linked to N-acetylglucosamine	879:927	Peripheral fucose (about 20% alpha 1,3-linked to N-acetylglucosamine) was also detected.
7525874	1	42	theme	human	176:180	arg1	fluid					196:200	human cerebrospinal fluid	176:200	human cerebrospinal fluid	176:200	The carbohydrate structures of beta-trace protein from human cerebrospinal fluid have been elucidated.
7525874	0	43	theme	human	51:55	arg1	fluid					71:75	human cerebrospinal fluid	51:75	human cerebrospinal fluid	51:75	Carbohydrate structures of beta-trace protein from human cerebrospinal fluid: evidence for "brain-type" N-glycosylation.
7525874	8	44	theme	Seventy	949:955	arg1	percent					957:963	Seventy percent	949:963	Seventy percent of the oligosaccharides	949:987	Seventy percent of the oligosaccharides contained a bisecting N-acetylglucosamine.
7525874	11	45	theme	minor	1330:1334	arg1	differences					1336:1346	only minor differences	1325:1346	only minor differences	1325:1346	Analysis of the site-specific glycosylation patterns at Asn29 and Asn56 revealed only minor differences.
7525874	12	46	theme	structural	1366:1375	arg1	features					1377:1384	the structural features	1362:1384	the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage)	1362:1600	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	11	47	gly	glycosylation	1274:1286	arg2	Asn56					1310:1314	Asn56	1310:1314	Asn56	1310:1314	Analysis of the site-specific glycosylation patterns at Asn29 and Asn56 revealed only minor differences.
7525874	11	47	gly	glycosylation	1274:1286	arg2	Asn29					1300:1304	Asn29	1300:1304	Asn29	1300:1304	Analysis of the site-specific glycosylation patterns at Asn29 and Asn56 revealed only minor differences.
7525874	2	48	theme	N-linked	257:264	arg1	oligosaccharides					266:281	exclusively N-linked oligosaccharides	245:281	exclusively N-linked oligosaccharides	245:281	This protein carries exclusively N-linked oligosaccharides at two sites (Asn29 and Asn56).
7525874	4	49	dep	biantennary	565:575	arg1	%					613:613	20%	611:613	20%	611:613	All glycans were found to be of the complex type, and most (90%) of them were biantennary with no (40%), one (40%), or two (20%) N-acetylneuraminic acid residues.
7525874	4	49	dep	biantennary	565:575	arg1	%					588:588	40%	586:588	40%	586:588	All glycans were found to be of the complex type, and most (90%) of them were biantennary with no (40%), one (40%), or two (20%) N-acetylneuraminic acid residues.
7525874	4	49	dep	biantennary	565:575	arg1	one					592:594	one	592:594	one	592:594	All glycans were found to be of the complex type, and most (90%) of them were biantennary with no (40%), one (40%), or two (20%) N-acetylneuraminic acid residues.
7525874	4	49	dep	biantennary	565:575	arg1	%					599:599	40%	597:599	40%	597:599	All glycans were found to be of the complex type, and most (90%) of them were biantennary with no (40%), one (40%), or two (20%) N-acetylneuraminic acid residues.
7525874	4	49	dep	biantennary	565:575	arg1	two					606:608	two	606:608	two	606:608	All glycans were found to be of the complex type, and most (90%) of them were biantennary with no (40%), one (40%), or two (20%) N-acetylneuraminic acid residues.
7525874	3	50	theme	released	329:336	arg1	N-glycans					338:346	Enzymatically released N-glycans	315:346	Enzymatically released N-glycans	315:346	Enzymatically released N-glycans were studied by compositional and methylation analyses, high-pH anion-exchange chromatography, and liquid secondary ion mass spectrometry.
7525874	4	51	theme	N-acetylneuraminic	616:633	arg1	residues					640:647	N-acetylneuraminic acid residues	616:647	N-acetylneuraminic acid residues	616:647	All glycans were found to be of the complex type, and most (90%) of them were biantennary with no (40%), one (40%), or two (20%) N-acetylneuraminic acid residues.
7525874	7	52	dep	alpha	889:893	arg1	%					887:887	%	887:887	%	887:887	Peripheral fucose (about 20% alpha 1,3-linked to N-acetylglucosamine) was also detected.
7525874	1	53	theme	carbohydrate	125:136	arg1	structures					138:147	The carbohydrate structures	121:147	The carbohydrate structures of beta-trace protein from human cerebrospinal fluid	121:200	The carbohydrate structures of beta-trace protein from human cerebrospinal fluid have been elucidated.
7525874	12	54	theme	acid	1575:1578	arg1	amounts					1423:1429	high amounts	1418:1429	high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues,	1418:1527	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	12	54	theme	acid	1575:1578	arg1	acid					1575:1578	N-acetylneuraminic acid	1556:1578	N-acetylneuraminic acid in alpha 2,3 linkage	1556:1599	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	12	54	theme	acid	1575:1578	arg1	degree					1394:1399	a high degree	1387:1399	a high degree of fucosylation	1387:1415	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	12	54	theme	acid	1575:1578	arg1	N-acetylglucosamine					1485:1503	terminal N-acetylglucosamine	1476:1503	terminal N-acetylglucosamine	1476:1503	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	12	54	theme	acid	1575:1578	arg1	amounts					1545:1551	significant amounts	1533:1551	significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage	1533:1599	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	12	54	theme	acid	1575:1578	arg1	N-acetylglucosamine					1444:1462	bisecting N-acetylglucosamine	1434:1462	bisecting N-acetylglucosamine	1434:1462	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	5	55	with	chains	699:704	arg1	repeats					743:749	intact or truncated lactosamine repeats	711:749	intact or truncated lactosamine repeats	711:749	The rest were triantennary chains or biantennary chains with intact or truncated lactosamine repeats.
7525874	10	56	theme	different	1207:1215	arg1	N-glycans					1217:1225	At least 20 different N-glycans	1195:1225	At least 20 different N-glycans	1195:1225	At least 20 different N-glycans were identified.
7525874	6	57	theme	N-acetylglucosamine	766:784	arg1	residues					786:793	The innermost N-acetylglucosamine residues	752:793	The innermost N-acetylglucosamine residues of nearly all structures	752:818	The innermost N-acetylglucosamine residues of nearly all structures were found to be alpha 1,6-fucosylated.
7525874	6	57	theme	N-acetylglucosamine	766:784	arg1	structures					809:818	nearly all structures	798:818	nearly all structures	798:818	The innermost N-acetylglucosamine residues of nearly all structures were found to be alpha 1,6-fucosylated.
7525874	6	57	theme	N-acetylglucosamine	766:784	arg1	1,6-fucosylated					843:857	1,6-fucosylated	843:857	1,6-fucosylated	843:857	The innermost N-acetylglucosamine residues of nearly all structures were found to be alpha 1,6-fucosylated.
7525874	12	58	theme	alpha	1583:1587	arg1	linkage					1593:1599	alpha 2,3 linkage	1583:1599	alpha 2,3 linkage	1583:1599	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	5	59	theme	biantennary	687:697	arg1	chains					699:704	biantennary chains	687:704	biantennary chains	687:704	The rest were triantennary chains or biantennary chains with intact or truncated lactosamine repeats.
7525874	8	60	theme	oligosaccharides	972:987	arg1	percent					957:963	Seventy percent	949:963	Seventy percent of the oligosaccharides	949:987	Seventy percent of the oligosaccharides contained a bisecting N-acetylglucosamine.
7525874	1	61	theme	protein	163:169	arg1	structures					138:147	The carbohydrate structures	121:147	The carbohydrate structures of beta-trace protein from human cerebrospinal fluid	121:200	The carbohydrate structures of beta-trace protein from human cerebrospinal fluid have been elucidated.
7525874	12	62	theme	significant	1533:1543	arg1	amounts					1545:1551	significant amounts	1533:1551	significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage	1533:1599	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	12	62	theme	significant	1533:1543	arg1	acid					1575:1578	N-acetylneuraminic acid	1556:1578	N-acetylneuraminic acid in alpha 2,3 linkage	1556:1599	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	12	62	theme	significant	1533:1543	arg1	N-acetylglucosamine					1485:1503	terminal N-acetylglucosamine	1476:1503	terminal N-acetylglucosamine	1476:1503	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	12	62	theme	significant	1533:1543	arg1	degree					1394:1399	a high degree	1387:1399	a high degree of fucosylation	1387:1415	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	12	62	theme	significant	1533:1543	arg1	N-acetylglucosamine					1444:1462	bisecting N-acetylglucosamine	1434:1462	bisecting N-acetylglucosamine	1434:1462	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	11	63	theme	patterns	1288:1295	arg1	Analysis					1244:1251	Analysis	1244:1251	Analysis of the site-specific glycosylation patterns at Asn29 and Asn56	1244:1314	Analysis of the site-specific glycosylation patterns at Asn29 and Asn56 revealed only minor differences.
7525874	6	64	gly	1,6-fucosylated	843:857	arg1	residues					786:793	The innermost N-acetylglucosamine residues	752:793	The innermost N-acetylglucosamine residues of nearly all structures	752:818	The innermost N-acetylglucosamine residues of nearly all structures were found to be alpha 1,6-fucosylated.
7525874	6	64	gly	1,6-fucosylated	843:857	arg1	structures					809:818	nearly all structures	798:818	nearly all structures	798:818	The innermost N-acetylglucosamine residues of nearly all structures were found to be alpha 1,6-fucosylated.
7525874	6	64	gly	1,6-fucosylated	843:857	arg1	1,6-fucosylated					843:857	1,6-fucosylated	843:857	1,6-fucosylated	843:857	The innermost N-acetylglucosamine residues of nearly all structures were found to be alpha 1,6-fucosylated.
7525874	7	65	link	1,3-linked	895:904	arg1	alpha					889:893	about 20% alpha	879:893	about 20% alpha 1,3-linked to N-acetylglucosamine	879:927	Peripheral fucose (about 20% alpha 1,3-linked to N-acetylglucosamine) was also detected.
7525874	0	66	theme	brain-type	92:101	arg1	N-glycosylation					104:118	"brain-type" N-glycosylation	91:118	"brain-type" N-glycosylation	91:118	Carbohydrate structures of beta-trace protein from human cerebrospinal fluid: evidence for "brain-type" N-glycosylation.
7525874	12	67	from	acid	1575:1578	arg1	linkage					1593:1599	alpha 2,3 linkage	1583:1599	alpha 2,3 linkage	1583:1599	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	11	68	theme	site-specific	1260:1272	arg1	patterns					1288:1295	the site-specific glycosylation patterns	1256:1295	the site-specific glycosylation patterns at Asn29 and Asn56	1256:1314	Analysis of the site-specific glycosylation patterns at Asn29 and Asn56 revealed only minor differences.
7525874	7	69	theme	1,3-linked	895:904	arg1	alpha					889:893	about 20% alpha	879:893	about 20% alpha 1,3-linked to N-acetylglucosamine	879:927	Peripheral fucose (about 20% alpha 1,3-linked to N-acetylglucosamine) was also detected.
7525874	5	70	theme	lactosamine	731:741	arg1	repeats					743:749	intact or truncated lactosamine repeats	711:749	intact or truncated lactosamine repeats	711:749	The rest were triantennary chains or biantennary chains with intact or truncated lactosamine repeats.
7525874	6	71	theme	innermost	756:764	arg1	residues					786:793	The innermost N-acetylglucosamine residues	752:793	The innermost N-acetylglucosamine residues of nearly all structures	752:818	The innermost N-acetylglucosamine residues of nearly all structures were found to be alpha 1,6-fucosylated.
7525874	6	71	theme	innermost	756:764	arg1	structures					809:818	nearly all structures	798:818	nearly all structures	798:818	The innermost N-acetylglucosamine residues of nearly all structures were found to be alpha 1,6-fucosylated.
7525874	6	71	theme	innermost	756:764	arg1	1,6-fucosylated					843:857	1,6-fucosylated	843:857	1,6-fucosylated	843:857	The innermost N-acetylglucosamine residues of nearly all structures were found to be alpha 1,6-fucosylated.
7525874	3	72	theme	mass	468:471	arg1	spectrometry					473:484	liquid secondary ion mass spectrometry	447:484	liquid secondary ion mass spectrometry	447:484	Enzymatically released N-glycans were studied by compositional and methylation analyses, high-pH anion-exchange chromatography, and liquid secondary ion mass spectrometry.
7525874	0	73	theme	beta-trace	27:36	arg1	protein					38:44	beta-trace protein	27:44	beta-trace protein	27:44	Carbohydrate structures of beta-trace protein from human cerebrospinal fluid: evidence for "brain-type" N-glycosylation.
7525874	11	74	from	Asn29	1300:1304	arg1	patterns					1288:1295	the site-specific glycosylation patterns	1256:1295	the site-specific glycosylation patterns at Asn29 and Asn56	1256:1314	Analysis of the site-specific glycosylation patterns at Asn29 and Asn56 revealed only minor differences.
7525874	11	74	from	Asn29	1300:1304	arg1	Analysis					1244:1251	Analysis	1244:1251	Analysis of the site-specific glycosylation patterns at Asn29 and Asn56	1244:1314	Analysis of the site-specific glycosylation patterns at Asn29 and Asn56 revealed only minor differences.
7525874	3	75	theme	high-pH	404:410	arg1	chromatography					427:440	high-pH anion-exchange chromatography	404:440	high-pH anion-exchange chromatography	404:440	Enzymatically released N-glycans were studied by compositional and methylation analyses, high-pH anion-exchange chromatography, and liquid secondary ion mass spectrometry.
7525874	12	76	gly	glycosylated	1650:1661	arg1	protein					1608:1614	this protein	1603:1614	this protein	1603:1614	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	12	76	gly	glycosylated	1650:1661	arg1	"					1648:1648	"brain-type"	1637:1648	"brain-type" glycosylated	1637:1661	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	11	77	from	Asn56	1310:1314	arg1	patterns					1288:1295	the site-specific glycosylation patterns	1256:1295	the site-specific glycosylation patterns at Asn29 and Asn56	1256:1314	Analysis of the site-specific glycosylation patterns at Asn29 and Asn56 revealed only minor differences.
7525874	11	77	from	Asn56	1310:1314	arg1	Analysis					1244:1251	Analysis	1244:1251	Analysis of the site-specific glycosylation patterns at Asn29 and Asn56	1244:1314	Analysis of the site-specific glycosylation patterns at Asn29 and Asn56 revealed only minor differences.
7525874	6	78	theme	structures	809:818	arg1	residues					786:793	The innermost N-acetylglucosamine residues	752:793	The innermost N-acetylglucosamine residues of nearly all structures	752:818	The innermost N-acetylglucosamine residues of nearly all structures were found to be alpha 1,6-fucosylated.
7525874	6	78	theme	structures	809:818	arg1	structures					809:818	nearly all structures	798:818	nearly all structures	798:818	The innermost N-acetylglucosamine residues of nearly all structures were found to be alpha 1,6-fucosylated.
7525874	6	78	theme	structures	809:818	arg1	1,6-fucosylated					843:857	1,6-fucosylated	843:857	1,6-fucosylated	843:857	The innermost N-acetylglucosamine residues of nearly all structures were found to be alpha 1,6-fucosylated.
7525874	3	79	theme	secondary	454:462	arg1	spectrometry					473:484	liquid secondary ion mass spectrometry	447:484	liquid secondary ion mass spectrometry	447:484	Enzymatically released N-glycans were studied by compositional and methylation analyses, high-pH anion-exchange chromatography, and liquid secondary ion mass spectrometry.
7525874	9	80	theme	monosialylated	1075:1088	arg1	fractions					1106:1114	the monosialylated oligosaccharide fractions	1071:1114	the monosialylated oligosaccharide fractions	1071:1114	Especially in the neutral, but also in the monosialylated oligosaccharide fractions, many incomplete antennae consisting of N-acetylglucosamine only were present.
7525874	5	81	theme	triantennary	664:675	arg1	rest					654:657	The rest	650:657	The rest	650:657	The rest were triantennary chains or biantennary chains with intact or truncated lactosamine repeats.
7525874	5	81	theme	triantennary	664:675	arg1	chains					677:682	triantennary chains	664:682	triantennary chains	664:682	The rest were triantennary chains or biantennary chains with intact or truncated lactosamine repeats.
7525874	0	82	theme	cerebrospinal	57:69	arg1	fluid					71:75	human cerebrospinal fluid	51:75	human cerebrospinal fluid	51:75	Carbohydrate structures of beta-trace protein from human cerebrospinal fluid: evidence for "brain-type" N-glycosylation.
7525874	12	83	from	amounts	1545:1551	arg1	linkage					1593:1599	alpha 2,3 linkage	1583:1599	alpha 2,3 linkage	1583:1599	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	7	84	theme	Peripheral	860:869	arg1	fucose					871:876	Peripheral fucose	860:876	Peripheral fucose (about 20% alpha 1,3-linked to N-acetylglucosamine)	860:928	Peripheral fucose (about 20% alpha 1,3-linked to N-acetylglucosamine) was also detected.
7525874	12	85	from	linkage	1593:1599	arg1	amounts					1423:1429	high amounts	1418:1429	high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues,	1418:1527	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	12	85	from	linkage	1593:1599	arg1	acid					1575:1578	N-acetylneuraminic acid	1556:1578	N-acetylneuraminic acid in alpha 2,3 linkage	1556:1599	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	12	85	from	linkage	1593:1599	arg1	degree					1394:1399	a high degree	1387:1399	a high degree of fucosylation	1387:1415	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	12	85	from	linkage	1593:1599	arg1	N-acetylglucosamine					1485:1503	terminal N-acetylglucosamine	1476:1503	terminal N-acetylglucosamine	1476:1503	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	12	85	from	linkage	1593:1599	arg1	amounts					1545:1551	significant amounts	1533:1551	significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage	1533:1599	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	12	85	from	linkage	1593:1599	arg1	N-acetylglucosamine					1444:1462	bisecting N-acetylglucosamine	1434:1462	bisecting N-acetylglucosamine	1434:1462	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	9	86	theme	many	1117:1120	arg1	antennae					1133:1140	many incomplete antennae	1117:1140	many incomplete antennae consisting of N-acetylglucosamine only	1117:1179	Especially in the neutral, but also in the monosialylated oligosaccharide fractions, many incomplete antennae consisting of N-acetylglucosamine only were present.
7525874	2	87	contain	carries	237:243	arg3	sites					290:294	two sites	286:294	two sites (Asn29 and Asn56)	286:312	This protein carries exclusively N-linked oligosaccharides at two sites (Asn29 and Asn56).
7525874	2	87	contain	carries	237:243	arg1	protein					229:235	This protein	224:235	This protein	224:235	This protein carries exclusively N-linked oligosaccharides at two sites (Asn29 and Asn56).
7525874	2	87	contain	carries	237:243	arg3	Asn29					297:301	Asn29	297:301	Asn29	297:301	This protein carries exclusively N-linked oligosaccharides at two sites (Asn29 and Asn56).
7525874	2	87	contain	carries	237:243	arg2	oligosaccharides					266:281	exclusively N-linked oligosaccharides	245:281	exclusively N-linked oligosaccharides	245:281	This protein carries exclusively N-linked oligosaccharides at two sites (Asn29 and Asn56).
7525874	2	87	contain	carries	237:243	arg3	Asn56					307:311	Asn56	307:311	Asn56	307:311	This protein carries exclusively N-linked oligosaccharides at two sites (Asn29 and Asn56).
7525874	12	88	theme	terminal	1476:1483	arg1	N-acetylglucosamine					1485:1503	terminal N-acetylglucosamine	1476:1503	terminal N-acetylglucosamine	1476:1503	According to the structural features (a high degree of fucosylation, high amounts of bisecting N-acetylglucosamine, as well as terminal N-acetylglucosamine and galactose residues, and significant amounts of N-acetylneuraminic acid in alpha 2,3 linkage), this protein can be classified as "brain-type" glycosylated.
7525874	0	89	dep	structures	13:22	arg1	evidence					78:85	evidence	78:85	Carbohydrate structures of beta-trace protein from human cerebrospinal fluid: evidence for "brain-type" N-glycosylation.	0:119	Carbohydrate structures of beta-trace protein from human cerebrospinal fluid: evidence for "brain-type" N-glycosylation.
7914890	8	0	theme	ordered	1095:1101	arg1	manner					1103:1108	an ordered manner	1092:1108	an ordered manner whereby phosphorylation of one site can affect the phosphorylation of another site	1092:1191	The lack of phosphorylation at Asn-184 in wild type arylsulfatase A therefore indicates that in vivo the presence of oligosaccharides can interfere with phosphorylation of other sites or that phosphorylation occurs in an ordered manner whereby phosphorylation of one site can affect the phosphorylation of another site.
7914890	3	1	from	site	550:553	arg1	oligosaccharides					494:509	oligosaccharides	494:509	oligosaccharides at the first and third N-glycosylation site (Asn-158 and Asn-350)	494:575	Phosphorylation of mannose residues is restricted to oligosaccharides at the first and third N-glycosylation site (Asn-158 and Asn-350).
7914890	5	2	theme	N-glycosylation	714:728	arg1	site					730:733	only the second N-glycosylation site	698:733	only the second N-glycosylation site	698:733	An earlier study had shown that a mutant arylsulfatase A containing only the second N-glycosylation site at Asn-184 folds correctly and is phosphorylated (Gieselmann, V., Schmidt, B., and von Figura, K. (1992) J. Biol.
7914890	8	3	theme	wild	916:919	arg1	A					940:940	wild type arylsulfatase A	916:940	wild type arylsulfatase A	916:940	The lack of phosphorylation at Asn-184 in wild type arylsulfatase A therefore indicates that in vivo the presence of oligosaccharides can interfere with phosphorylation of other sites or that phosphorylation occurs in an ordered manner whereby phosphorylation of one site can affect the phosphorylation of another site.
7914890	1	4	theme	metabolic	165:173	arg1	labeling					175:182	metabolic labeling	165:182	metabolic labeling	165:182	The glycosylation and phosphorylation of the lysosomal enzyme arylsulfatase A was analyzed by a combination of metabolic labeling, tryptic fragmentation, mass spectrometry, and radiosequencing.
7914890	2	5	gly	N-glycosylation	297:311	arg2	three					281:285	three	281:285	three	281:285	The results demonstrate that all three potential N-glycosylation sites at Asn residues 158, 184, and 350 are utilized in arylsufatase A and carry high mannose or hybride type oligosaccharides.
7914890	2	5	gly	N-glycosylation	297:311	arg2	residues					326:333	Asn residues 158, 184, and 350	322:351	Asn residues 158, 184, and 350	322:351	The results demonstrate that all three potential N-glycosylation sites at Asn residues 158, 184, and 350 are utilized in arylsufatase A and carry high mannose or hybride type oligosaccharides.
7914890	2	5	gly	N-glycosylation	297:311	arg2	sites					313:317	all three potential N-glycosylation sites	277:317	all three potential N-glycosylation sites at Asn residues 158, 184, and 350	277:351	The results demonstrate that all three potential N-glycosylation sites at Asn residues 158, 184, and 350 are utilized in arylsufatase A and carry high mannose or hybride type oligosaccharides.
7914890	5	6	theme	mutant	664:669	arg1	A					685:685	a mutant arylsulfatase A	662:685	a mutant arylsulfatase A containing only the second N-glycosylation site at Asn-184	662:744	An earlier study had shown that a mutant arylsulfatase A containing only the second N-glycosylation site at Asn-184 folds correctly and is phosphorylated (Gieselmann, V., Schmidt, B., and von Figura, K. (1992) J. Biol.
7914890	7	7	dep	267	855:857	arg1	13262-13266					860:870	13262-13266	860:870	13262-13266	860:870	267, 13262-13266).
7914890	2	8	from	residues	326:333	arg1	sites					313:317	all three potential N-glycosylation sites	277:317	all three potential N-glycosylation sites at Asn residues 158, 184, and 350	277:351	The results demonstrate that all three potential N-glycosylation sites at Asn residues 158, 184, and 350 are utilized in arylsufatase A and carry high mannose or hybride type oligosaccharides.
7914890	5	9	theme	arylsulfatase	671:683	arg1	A					685:685	a mutant arylsulfatase A	662:685	a mutant arylsulfatase A containing only the second N-glycosylation site at Asn-184	662:744	An earlier study had shown that a mutant arylsulfatase A containing only the second N-glycosylation site at Asn-184 folds correctly and is phosphorylated (Gieselmann, V., Schmidt, B., and von Figura, K. (1992) J. Biol.
7914890	2	10	used	utilized	357:364	arg2	residues					326:333	Asn residues 158, 184, and 350	322:351	Asn residues 158, 184, and 350	322:351	The results demonstrate that all three potential N-glycosylation sites at Asn residues 158, 184, and 350 are utilized in arylsufatase A and carry high mannose or hybride type oligosaccharides.
7914890	2	10	used	utilized	357:364	arg2	sites					313:317	all three potential N-glycosylation sites	277:317	all three potential N-glycosylation sites at Asn residues 158, 184, and 350	277:351	The results demonstrate that all three potential N-glycosylation sites at Asn residues 158, 184, and 350 are utilized in arylsufatase A and carry high mannose or hybride type oligosaccharides.
7914890	2	11	theme	N-glycosylation	297:311	arg1	sites					313:317	all three potential N-glycosylation sites	277:317	all three potential N-glycosylation sites at Asn residues 158, 184, and 350	277:351	The results demonstrate that all three potential N-glycosylation sites at Asn residues 158, 184, and 350 are utilized in arylsufatase A and carry high mannose or hybride type oligosaccharides.
7914890	5	12	gly	N-glycosylation	714:728	arg2	site					730:733	only the second N-glycosylation site	698:733	only the second N-glycosylation site	698:733	An earlier study had shown that a mutant arylsulfatase A containing only the second N-glycosylation site at Asn-184 folds correctly and is phosphorylated (Gieselmann, V., Schmidt, B., and von Figura, K. (1992) J. Biol.
7914890	5	13	theme	earlier	633:639	arg1	study					641:645	An earlier study	630:645	An earlier study	630:645	An earlier study had shown that a mutant arylsulfatase A containing only the second N-glycosylation site at Asn-184 folds correctly and is phosphorylated (Gieselmann, V., Schmidt, B., and von Figura, K. (1992) J. Biol.
7914890	8	14	theme	type	921:924	arg1	A					940:940	wild type arylsulfatase A	916:940	wild type arylsulfatase A	916:940	The lack of phosphorylation at Asn-184 in wild type arylsulfatase A therefore indicates that in vivo the presence of oligosaccharides can interfere with phosphorylation of other sites or that phosphorylation occurs in an ordered manner whereby phosphorylation of one site can affect the phosphorylation of another site.
7914890	2	15	theme	potential	287:295	arg1	sites					313:317	all three potential N-glycosylation sites	277:317	all three potential N-glycosylation sites at Asn residues 158, 184, and 350	277:351	The results demonstrate that all three potential N-glycosylation sites at Asn residues 158, 184, and 350 are utilized in arylsufatase A and carry high mannose or hybride type oligosaccharides.
7914890	1	16	theme	labeling	175:182	arg1	combination					150:160	a combination	148:160	a combination of metabolic labeling, tryptic fragmentation, mass spectrometry, and radiosequencing	148:245	The glycosylation and phosphorylation of the lysosomal enzyme arylsulfatase A was analyzed by a combination of metabolic labeling, tryptic fragmentation, mass spectrometry, and radiosequencing.
7914890	4	17	theme	comparable	607:616	arg1	efficiency					618:627	comparable efficiency	607:627	comparable efficiency	607:627	Both are phosphorylated with comparable efficiency.
7914890	8	18	theme	site	1188:1191	arg1	phosphorylation					1161:1175	the phosphorylation	1157:1175	the phosphorylation of another site	1157:1191	The lack of phosphorylation at Asn-184 in wild type arylsulfatase A therefore indicates that in vivo the presence of oligosaccharides can interfere with phosphorylation of other sites or that phosphorylation occurs in an ordered manner whereby phosphorylation of one site can affect the phosphorylation of another site.
7914890	8	19	theme	site	1141:1144	arg1	phosphorylation					1118:1132	phosphorylation	1118:1132	phosphorylation of one site	1118:1144	The lack of phosphorylation at Asn-184 in wild type arylsulfatase A therefore indicates that in vivo the presence of oligosaccharides can interfere with phosphorylation of other sites or that phosphorylation occurs in an ordered manner whereby phosphorylation of one site can affect the phosphorylation of another site.
7914890	1	20	theme	tryptic	185:191	arg1	fragmentation					193:205	tryptic fragmentation	185:205	tryptic fragmentation	185:205	The glycosylation and phosphorylation of the lysosomal enzyme arylsulfatase A was analyzed by a combination of metabolic labeling, tryptic fragmentation, mass spectrometry, and radiosequencing.
7914890	5	21	dep	V.	797:798	arg1	Biol					843:846	Biol	843:846	Biol	843:846	An earlier study had shown that a mutant arylsulfatase A containing only the second N-glycosylation site at Asn-184 folds correctly and is phosphorylated (Gieselmann, V., Schmidt, B., and von Figura, K. (1992) J. Biol.
7914890	1	22	theme	lysosomal	99:107	arg1	A					130:130	the lysosomal enzyme arylsulfatase A	95:130	the lysosomal enzyme arylsulfatase A	95:130	The glycosylation and phosphorylation of the lysosomal enzyme arylsulfatase A was analyzed by a combination of metabolic labeling, tryptic fragmentation, mass spectrometry, and radiosequencing.
7914890	1	23	theme	fragmentation	193:205	arg1	combination					150:160	a combination	148:160	a combination of metabolic labeling, tryptic fragmentation, mass spectrometry, and radiosequencing	148:245	The glycosylation and phosphorylation of the lysosomal enzyme arylsulfatase A was analyzed by a combination of metabolic labeling, tryptic fragmentation, mass spectrometry, and radiosequencing.
7914890	5	24	theme	second	707:712	arg1	site					730:733	only the second N-glycosylation site	698:733	only the second N-glycosylation site	698:733	An earlier study had shown that a mutant arylsulfatase A containing only the second N-glycosylation site at Asn-184 folds correctly and is phosphorylated (Gieselmann, V., Schmidt, B., and von Figura, K. (1992) J. Biol.
7914890	1	25	theme	enzyme	109:114	arg1	A					130:130	the lysosomal enzyme arylsulfatase A	95:130	the lysosomal enzyme arylsulfatase A	95:130	The glycosylation and phosphorylation of the lysosomal enzyme arylsulfatase A was analyzed by a combination of metabolic labeling, tryptic fragmentation, mass spectrometry, and radiosequencing.
7914890	2	26	theme	hybride	410:416	arg1	oligosaccharides					423:438	high mannose or hybride type oligosaccharides	394:438	oligosaccharides	423:438	The results demonstrate that all three potential N-glycosylation sites at Asn residues 158, 184, and 350 are utilized in arylsufatase A and carry high mannose or hybride type oligosaccharides.
7914890	2	27	theme	type	418:421	arg1	oligosaccharides					423:438	high mannose or hybride type oligosaccharides	394:438	oligosaccharides	423:438	The results demonstrate that all three potential N-glycosylation sites at Asn residues 158, 184, and 350 are utilized in arylsufatase A and carry high mannose or hybride type oligosaccharides.
7914890	3	28	theme	N-glycosylation	534:548	arg1	site					550:553	the first and third N-glycosylation site	514:553	the first and third N-glycosylation site (Asn-158 and Asn-350)	514:575	Phosphorylation of mannose residues is restricted to oligosaccharides at the first and third N-glycosylation site (Asn-158 and Asn-350).
7914890	1	29	theme	arylsulfatase	116:128	arg1	A					130:130	the lysosomal enzyme arylsulfatase A	95:130	the lysosomal enzyme arylsulfatase A	95:130	The glycosylation and phosphorylation of the lysosomal enzyme arylsulfatase A was analyzed by a combination of metabolic labeling, tryptic fragmentation, mass spectrometry, and radiosequencing.
7914890	1	30	theme	mass	208:211	arg1	spectrometry					213:224	mass spectrometry	208:224	mass spectrometry	208:224	The glycosylation and phosphorylation of the lysosomal enzyme arylsulfatase A was analyzed by a combination of metabolic labeling, tryptic fragmentation, mass spectrometry, and radiosequencing.
7914890	0	31	theme	A	51:51	arg1	phosphorylation					18:32	phosphorylation	18:32	phosphorylation	18:32	Glycosylation and phosphorylation of arylsulfatase A.
7914890	0	31	theme	A	51:51	arg1	Glycosylation					0:12	Glycosylation	0:12	Glycosylation	0:12	Glycosylation and phosphorylation of arylsulfatase A.
7914890	8	32	theme	other	1046:1050	arg1	sites					1052:1056	other sites	1046:1056	other sites	1046:1056	The lack of phosphorylation at Asn-184 in wild type arylsulfatase A therefore indicates that in vivo the presence of oligosaccharides can interfere with phosphorylation of other sites or that phosphorylation occurs in an ordered manner whereby phosphorylation of one site can affect the phosphorylation of another site.
7914890	8	33	from	lack	878:881	arg1	A					940:940	wild type arylsulfatase A	916:940	wild type arylsulfatase A	916:940	The lack of phosphorylation at Asn-184 in wild type arylsulfatase A therefore indicates that in vivo the presence of oligosaccharides can interfere with phosphorylation of other sites or that phosphorylation occurs in an ordered manner whereby phosphorylation of one site can affect the phosphorylation of another site.
7914890	8	33	from	lack	878:881	arg1	Asn-184					905:911	Asn-184	905:911	Asn-184	905:911	The lack of phosphorylation at Asn-184 in wild type arylsulfatase A therefore indicates that in vivo the presence of oligosaccharides can interfere with phosphorylation of other sites or that phosphorylation occurs in an ordered manner whereby phosphorylation of one site can affect the phosphorylation of another site.
7914890	0	34	gly	Glycosylation	0:12	arg1	A					51:51	arylsulfatase A	37:51	arylsulfatase A	37:51	Glycosylation and phosphorylation of arylsulfatase A.
7914890	2	35	theme	arylsufatase	369:380	arg1	A					382:382	arylsufatase A	369:382	arylsufatase A	369:382	The results demonstrate that all three potential N-glycosylation sites at Asn residues 158, 184, and 350 are utilized in arylsufatase A and carry high mannose or hybride type oligosaccharides.
7914890	1	36	theme	spectrometry	213:224	arg1	combination					150:160	a combination	148:160	a combination of metabolic labeling, tryptic fragmentation, mass spectrometry, and radiosequencing	148:245	The glycosylation and phosphorylation of the lysosomal enzyme arylsulfatase A was analyzed by a combination of metabolic labeling, tryptic fragmentation, mass spectrometry, and radiosequencing.
7914890	0	37	theme	arylsulfatase	37:49	arg1	A					51:51	arylsulfatase A	37:51	arylsulfatase A	37:51	Glycosylation and phosphorylation of arylsulfatase A.
7914890	8	38	theme	arylsulfatase	926:938	arg1	A					940:940	wild type arylsulfatase A	916:940	wild type arylsulfatase A	916:940	The lack of phosphorylation at Asn-184 in wild type arylsulfatase A therefore indicates that in vivo the presence of oligosaccharides can interfere with phosphorylation of other sites or that phosphorylation occurs in an ordered manner whereby phosphorylation of one site can affect the phosphorylation of another site.
7914890	5	39	dep	phosphorylated	769:782	arg1	B.					810:811	B.	810:811	B.	810:811	An earlier study had shown that a mutant arylsulfatase A containing only the second N-glycosylation site at Asn-184 folds correctly and is phosphorylated (Gieselmann, V., Schmidt, B., and von Figura, K. (1992) J. Biol.
7914890	5	39	dep	phosphorylated	769:782	arg1	K					830:830	K	830:830	K	830:830	An earlier study had shown that a mutant arylsulfatase A containing only the second N-glycosylation site at Asn-184 folds correctly and is phosphorylated (Gieselmann, V., Schmidt, B., and von Figura, K. (1992) J. Biol.
7914890	5	39	dep	phosphorylated	769:782	arg1	1992					834:837	1992	834:837	1992	834:837	An earlier study had shown that a mutant arylsulfatase A containing only the second N-glycosylation site at Asn-184 folds correctly and is phosphorylated (Gieselmann, V., Schmidt, B., and von Figura, K. (1992) J. Biol.
7914890	5	39	dep	phosphorylated	769:782	arg1	Figura					822:827	Figura	822:827	Figura	822:827	An earlier study had shown that a mutant arylsulfatase A containing only the second N-glycosylation site at Asn-184 folds correctly and is phosphorylated (Gieselmann, V., Schmidt, B., and von Figura, K. (1992) J. Biol.
7914890	5	39	dep	phosphorylated	769:782	arg1	V.					797:798	V.	797:798	V.	797:798	An earlier study had shown that a mutant arylsulfatase A containing only the second N-glycosylation site at Asn-184 folds correctly and is phosphorylated (Gieselmann, V., Schmidt, B., and von Figura, K. (1992) J. Biol.
7914890	2	40	theme	high	394:397	arg1	mannose					399:405	high mannose or hybride type oligosaccharides	394:438	mannose	399:405	The results demonstrate that all three potential N-glycosylation sites at Asn residues 158, 184, and 350 are utilized in arylsufatase A and carry high mannose or hybride type oligosaccharides.
7914890	2	41	contain	carry	388:392	arg2	mannose					399:405	high mannose or hybride type oligosaccharides	394:438	mannose	399:405	The results demonstrate that all three potential N-glycosylation sites at Asn residues 158, 184, and 350 are utilized in arylsufatase A and carry high mannose or hybride type oligosaccharides.
7914890	2	41	contain	carry	388:392	arg1	sites					313:317	all three potential N-glycosylation sites	277:317	all three potential N-glycosylation sites at Asn residues 158, 184, and 350	277:351	The results demonstrate that all three potential N-glycosylation sites at Asn residues 158, 184, and 350 are utilized in arylsufatase A and carry high mannose or hybride type oligosaccharides.
7914890	2	41	contain	carry	388:392	arg2	oligosaccharides					423:438	high mannose or hybride type oligosaccharides	394:438	oligosaccharides	423:438	The results demonstrate that all three potential N-glycosylation sites at Asn residues 158, 184, and 350 are utilized in arylsufatase A and carry high mannose or hybride type oligosaccharides.
7914890	1	42	theme	A	130:130	arg1	phosphorylation					76:90	phosphorylation	76:90	phosphorylation	76:90	The glycosylation and phosphorylation of the lysosomal enzyme arylsulfatase A was analyzed by a combination of metabolic labeling, tryptic fragmentation, mass spectrometry, and radiosequencing.
7914890	1	42	theme	A	130:130	arg1	glycosylation					58:70	glycosylation	58:70	glycosylation	58:70	The glycosylation and phosphorylation of the lysosomal enzyme arylsulfatase A was analyzed by a combination of metabolic labeling, tryptic fragmentation, mass spectrometry, and radiosequencing.
7914890	5	43	contain	containing	687:696	arg1	A					685:685	a mutant arylsulfatase A	662:685	a mutant arylsulfatase A containing only the second N-glycosylation site at Asn-184	662:744	An earlier study had shown that a mutant arylsulfatase A containing only the second N-glycosylation site at Asn-184 folds correctly and is phosphorylated (Gieselmann, V., Schmidt, B., and von Figura, K. (1992) J. Biol.
7914890	5	43	contain	containing	687:696	arg2	site					730:733	only the second N-glycosylation site	698:733	only the second N-glycosylation site	698:733	An earlier study had shown that a mutant arylsulfatase A containing only the second N-glycosylation site at Asn-184 folds correctly and is phosphorylated (Gieselmann, V., Schmidt, B., and von Figura, K. (1992) J. Biol.
7914890	8	44	theme	sites	1052:1056	arg1	phosphorylation					1027:1041	phosphorylation	1027:1041	phosphorylation of other sites	1027:1056	The lack of phosphorylation at Asn-184 in wild type arylsulfatase A therefore indicates that in vivo the presence of oligosaccharides can interfere with phosphorylation of other sites or that phosphorylation occurs in an ordered manner whereby phosphorylation of one site can affect the phosphorylation of another site.
7914890	3	45	theme	first	518:522	arg1	site					550:553	the first and third N-glycosylation site	514:553	the first and third N-glycosylation site (Asn-158 and Asn-350)	514:575	Phosphorylation of mannose residues is restricted to oligosaccharides at the first and third N-glycosylation site (Asn-158 and Asn-350).
7914890	3	46	dep	site	550:553	arg1	Asn-350					568:574	Asn-350	568:574	Asn-350	568:574	Phosphorylation of mannose residues is restricted to oligosaccharides at the first and third N-glycosylation site (Asn-158 and Asn-350).
7914890	3	46	dep	site	550:553	arg1	Asn-158					556:562	Asn-158	556:562	Asn-158	556:562	Phosphorylation of mannose residues is restricted to oligosaccharides at the first and third N-glycosylation site (Asn-158 and Asn-350).
7914890	8	47	theme	oligosaccharides	991:1006	arg1	presence					979:986	the presence	975:986	the presence of oligosaccharides	975:1006	The lack of phosphorylation at Asn-184 in wild type arylsulfatase A therefore indicates that in vivo the presence of oligosaccharides can interfere with phosphorylation of other sites or that phosphorylation occurs in an ordered manner whereby phosphorylation of one site can affect the phosphorylation of another site.
7914890	1	48	dep	glycosylation	58:70	arg1	The					54:56	The	54:56	The	54:56	The glycosylation and phosphorylation of the lysosomal enzyme arylsulfatase A was analyzed by a combination of metabolic labeling, tryptic fragmentation, mass spectrometry, and radiosequencing.
7914890	2	49	theme	Asn	322:324	arg1	residues					326:333	Asn residues 158, 184, and 350	322:351	Asn residues 158, 184, and 350	322:351	The results demonstrate that all three potential N-glycosylation sites at Asn residues 158, 184, and 350 are utilized in arylsufatase A and carry high mannose or hybride type oligosaccharides.
7914890	8	50	from	Asn-184	905:911	arg1	phosphorylation					886:900	phosphorylation	886:900	phosphorylation at Asn-184	886:911	The lack of phosphorylation at Asn-184 in wild type arylsulfatase A therefore indicates that in vivo the presence of oligosaccharides can interfere with phosphorylation of other sites or that phosphorylation occurs in an ordered manner whereby phosphorylation of one site can affect the phosphorylation of another site.
7914890	8	50	from	Asn-184	905:911	arg1	lack					878:881	The lack	874:881	The lack of phosphorylation at Asn-184 in wild type arylsulfatase A	874:940	The lack of phosphorylation at Asn-184 in wild type arylsulfatase A therefore indicates that in vivo the presence of oligosaccharides can interfere with phosphorylation of other sites or that phosphorylation occurs in an ordered manner whereby phosphorylation of one site can affect the phosphorylation of another site.
7914890	3	51	gly	N-glycosylation	534:548	arg2	site					550:553	the first and third N-glycosylation site	514:553	the first and third N-glycosylation site (Asn-158 and Asn-350)	514:575	Phosphorylation of mannose residues is restricted to oligosaccharides at the first and third N-glycosylation site (Asn-158 and Asn-350).
7914890	8	52	theme	phosphorylation	886:900	arg1	lack					878:881	The lack	874:881	The lack of phosphorylation at Asn-184 in wild type arylsulfatase A	874:940	The lack of phosphorylation at Asn-184 in wild type arylsulfatase A therefore indicates that in vivo the presence of oligosaccharides can interfere with phosphorylation of other sites or that phosphorylation occurs in an ordered manner whereby phosphorylation of one site can affect the phosphorylation of another site.
7914890	1	53	theme	radiosequencing	231:245	arg1	combination					150:160	a combination	148:160	a combination of metabolic labeling, tryptic fragmentation, mass spectrometry, and radiosequencing	148:245	The glycosylation and phosphorylation of the lysosomal enzyme arylsulfatase A was analyzed by a combination of metabolic labeling, tryptic fragmentation, mass spectrometry, and radiosequencing.
7914890	3	54	theme	mannose	460:466	arg1	residues					468:475	mannose residues	460:475	mannose residues	460:475	Phosphorylation of mannose residues is restricted to oligosaccharides at the first and third N-glycosylation site (Asn-158 and Asn-350).
7914890	3	55	theme	residues	468:475	arg1	Phosphorylation					441:455	Phosphorylation	441:455	Phosphorylation of mannose residues	441:475	Phosphorylation of mannose residues is restricted to oligosaccharides at the first and third N-glycosylation site (Asn-158 and Asn-350).
7914890	1	56	gly	glycosylation	58:70	arg1	A					130:130	the lysosomal enzyme arylsulfatase A	95:130	the lysosomal enzyme arylsulfatase A	95:130	The glycosylation and phosphorylation of the lysosomal enzyme arylsulfatase A was analyzed by a combination of metabolic labeling, tryptic fragmentation, mass spectrometry, and radiosequencing.
7914890	3	57	theme	third	528:532	arg1	site					550:553	the first and third N-glycosylation site	514:553	the first and third N-glycosylation site (Asn-158 and Asn-350)	514:575	Phosphorylation of mannose residues is restricted to oligosaccharides at the first and third N-glycosylation site (Asn-158 and Asn-350).
2017190	5	0	dep	decreased	781:789	arg1	Kd					792:793	Kd	792:793	Kd	792:793	In the receptor mutated at Asn113, the affinity of TSH binding was markedly decreased (Kd, 2.6 x 10(-8) 3.3 x 10(-10) M in the wild-type receptor).
2017190	6	1	theme	cAMP	963:966	arg1	generation					968:977	intracellular cAMP generation	949:977	intracellular cAMP generation	949:977	This affinity was too low to permit the transduction of a signal, as measured by an increase in intracellular cAMP generation.
2017190	8	2	theme	cell	1445:1448	arg1	surface					1450:1456	the cell surface	1441:1456	the cell surface	1441:1456	Therefore, either these four potential glycosylation sites are not glycolysated, or alternatively, oligosaccharide chains at these positions do not play a major role in the folding, intracellular trafficking, stability, or expression of a functional receptor on the cell surface.
2017190	9	3	gly	glycosylation	1502:1514	arg1	Asn113					1529:1534	Asn113	1529:1534	Asn113	1529:1534	Conversely, our data suggest that N-linked glycosylation of Asn77 and Asn113 does play a role in the expression of a biologically active TSH receptor on the cell surface.
2017190	9	3	gly	glycosylation	1502:1514	arg1	Asn77					1519:1523	Asn77	1519:1523	Asn77	1519:1523	Conversely, our data suggest that N-linked glycosylation of Asn77 and Asn113 does play a role in the expression of a biologically active TSH receptor on the cell surface.
2017190	8	4	from	stability	1388:1396	arg1	surface					1450:1456	the cell surface	1441:1456	the cell surface	1441:1456	Therefore, either these four potential glycosylation sites are not glycolysated, or alternatively, oligosaccharide chains at these positions do not play a major role in the folding, intracellular trafficking, stability, or expression of a functional receptor on the cell surface.
2017190	8	5	from	expression	1402:1411	arg1	surface					1450:1456	the cell surface	1441:1456	the cell surface	1441:1456	Therefore, either these four potential glycosylation sites are not glycolysated, or alternatively, oligosaccharide chains at these positions do not play a major role in the folding, intracellular trafficking, stability, or expression of a functional receptor on the cell surface.
2017190	1	6	theme	glycosylation	171:183	arg1	role					163:166	the role	159:166	the role of glycosylation in the expression of a functional human TSH receptor	159:236	We studied the role of glycosylation in the expression of a functional human TSH receptor.
2017190	9	7	theme	N-linked	1493:1500	arg1	glycosylation					1502:1514	N-linked glycosylation	1493:1514	N-linked glycosylation of Asn77 and Asn113	1493:1534	Conversely, our data suggest that N-linked glycosylation of Asn77 and Asn113 does play a role in the expression of a biologically active TSH receptor on the cell surface.
2017190	2	8	used	used	280:283	arg2	mutagenesis					264:274	Oligonucleotide-directed mutagenesis	239:274	Oligonucleotide-directed mutagenesis	239:274	Oligonucleotide-directed mutagenesis was used to replace, separately or together, the Asn codons with Gln in each of the six potential glycosylation sites in the receptor.
2017190	8	9	from	receptor	1429:1436	arg1	surface					1450:1456	the cell surface	1441:1456	the cell surface	1441:1456	Therefore, either these four potential glycosylation sites are not glycolysated, or alternatively, oligosaccharide chains at these positions do not play a major role in the folding, intracellular trafficking, stability, or expression of a functional receptor on the cell surface.
2017190	7	10	theme	TSH	1082:1084	arg1	receptor					1086:1093	the TSH receptor	1078:1093	the TSH receptor	1078:1093	Substitution of Asn at positions 99, 177, 198, and 302 did not appreciably affect the affinity of the TSH receptor for TSH binding or its ability to mediate an increase in intracellular cAMP levels.
2017190	0	11	theme	receptor	138:145	arg1	expression					111:120	the expression	107:120	the expression of a functional receptor	107:145	Site-directed mutagenesis of the human thyrotropin receptor: role of asparagine-linked oligosaccharides in the expression of a functional receptor.
2017190	1	12	theme	functional	208:217	arg1	receptor					229:236	a functional human TSH receptor	206:236	a functional human TSH receptor	206:236	We studied the role of glycosylation in the expression of a functional human TSH receptor.
2017190	0	13	from	role	61:64	arg1	expression					111:120	the expression	107:120	the expression of a functional receptor	107:145	Site-directed mutagenesis of the human thyrotropin receptor: role of asparagine-linked oligosaccharides in the expression of a functional receptor.
2017190	4	14	theme	glycosylation	684:696	arg1	sites					698:702	all six potential glycosylation sites	666:702	all six potential glycosylation sites	666:702	High affinity TSH binding and the cAMP response to TSH stimulation were abolished in the receptor mutated at Asn77 as well as in the receptor mutated at all six potential glycosylation sites.
2017190	8	15	from	surface	1450:1456	arg1	expression					1402:1411	expression	1402:1411	expression	1402:1411	Therefore, either these four potential glycosylation sites are not glycolysated, or alternatively, oligosaccharide chains at these positions do not play a major role in the folding, intracellular trafficking, stability, or expression of a functional receptor on the cell surface.
2017190	8	15	from	surface	1450:1456	arg1	stability					1388:1396	stability	1388:1396	stability	1388:1396	Therefore, either these four potential glycosylation sites are not glycolysated, or alternatively, oligosaccharide chains at these positions do not play a major role in the folding, intracellular trafficking, stability, or expression of a functional receptor on the cell surface.
2017190	8	15	from	surface	1450:1456	arg1	folding					1352:1358	folding	1352:1358	folding	1352:1358	Therefore, either these four potential glycosylation sites are not glycolysated, or alternatively, oligosaccharide chains at these positions do not play a major role in the folding, intracellular trafficking, stability, or expression of a functional receptor on the cell surface.
2017190	8	15	from	surface	1450:1456	arg1	trafficking					1375:1385	intracellular trafficking	1361:1385	intracellular trafficking	1361:1385	Therefore, either these four potential glycosylation sites are not glycolysated, or alternatively, oligosaccharide chains at these positions do not play a major role in the folding, intracellular trafficking, stability, or expression of a functional receptor on the cell surface.
2017190	5	16	from	Kd	792:793	arg1	receptor					842:849	the wild-type receptor	828:849	the wild-type receptor	828:849	In the receptor mutated at Asn113, the affinity of TSH binding was markedly decreased (Kd, 2.6 x 10(-8) 3.3 x 10(-10) M in the wild-type receptor).
2017190	5	17	dep	3.3	809:811	arg1	-10					818:820	-10	818:820	-10	818:820	In the receptor mutated at Asn113, the affinity of TSH binding was markedly decreased (Kd, 2.6 x 10(-8) 3.3 x 10(-10) M in the wild-type receptor).
2017190	2	18	theme	Oligonucleotide-directed	239:262	arg1	mutagenesis					264:274	Oligonucleotide-directed mutagenesis	239:274	Oligonucleotide-directed mutagenesis	239:274	Oligonucleotide-directed mutagenesis was used to replace, separately or together, the Asn codons with Gln in each of the six potential glycosylation sites in the receptor.
2017190	0	19	theme	asparagine-linked	69:85	arg1	oligosaccharides					87:102	asparagine-linked oligosaccharides	69:102	asparagine-linked oligosaccharides	69:102	Site-directed mutagenesis of the human thyrotropin receptor: role of asparagine-linked oligosaccharides in the expression of a functional receptor.
2017190	8	20	theme	major	1334:1338	arg1	role					1340:1343	a major role	1332:1343	a major role	1332:1343	Therefore, either these four potential glycosylation sites are not glycolysated, or alternatively, oligosaccharide chains at these positions do not play a major role in the folding, intracellular trafficking, stability, or expression of a functional receptor on the cell surface.
2017190	9	21	theme	active	1589:1594	arg1	receptor					1600:1607	a biologically active TSH receptor	1574:1607	a biologically active TSH receptor on the cell surface	1574:1627	Conversely, our data suggest that N-linked glycosylation of Asn77 and Asn113 does play a role in the expression of a biologically active TSH receptor on the cell surface.
2017190	2	22	gly	glycosylation	374:386	arg2	six					360:362	six	360:362	six	360:362	Oligonucleotide-directed mutagenesis was used to replace, separately or together, the Asn codons with Gln in each of the six potential glycosylation sites in the receptor.
2017190	2	22	gly	glycosylation	374:386	arg2	sites					388:392	the six potential glycosylation sites	356:392	the six potential glycosylation sites in the receptor	356:408	Oligonucleotide-directed mutagenesis was used to replace, separately or together, the Asn codons with Gln in each of the six potential glycosylation sites in the receptor.
2017190	7	23	theme	cAMP	1166:1169	arg1	levels					1171:1176	intracellular cAMP levels	1152:1176	intracellular cAMP levels	1152:1176	Substitution of Asn at positions 99, 177, 198, and 302 did not appreciably affect the affinity of the TSH receptor for TSH binding or its ability to mediate an increase in intracellular cAMP levels.
2017190	9	24	theme	receptor	1600:1607	arg1	expression					1560:1569	the expression	1556:1569	the expression of a biologically active TSH receptor on the cell surface	1556:1627	Conversely, our data suggest that N-linked glycosylation of Asn77 and Asn113 does play a role in the expression of a biologically active TSH receptor on the cell surface.
2017190	2	25	theme	potential	364:372	arg1	sites					388:392	the six potential glycosylation sites	356:392	the six potential glycosylation sites in the receptor	356:408	Oligonucleotide-directed mutagenesis was used to replace, separately or together, the Asn codons with Gln in each of the six potential glycosylation sites in the receptor.
2017190	0	26	theme	Site-directed	0:12	arg1	mutagenesis					14:24	Site-directed mutagenesis	0:24	Site-directed mutagenesis of the human thyrotropin receptor: role of asparagine-linked oligosaccharides in the expression of a functional receptor.	0:146	Site-directed mutagenesis of the human thyrotropin receptor: role of asparagine-linked oligosaccharides in the expression of a functional receptor.
2017190	5	27	theme	wild-type	832:840	arg1	receptor					842:849	the wild-type receptor	828:849	the wild-type receptor	828:849	In the receptor mutated at Asn113, the affinity of TSH binding was markedly decreased (Kd, 2.6 x 10(-8) 3.3 x 10(-10) M in the wild-type receptor).
2017190	8	28	theme	intracellular	1361:1373	arg1	trafficking					1375:1385	intracellular trafficking	1361:1385	intracellular trafficking	1361:1385	Therefore, either these four potential glycosylation sites are not glycolysated, or alternatively, oligosaccharide chains at these positions do not play a major role in the folding, intracellular trafficking, stability, or expression of a functional receptor on the cell surface.
2017190	8	29	theme	potential	1208:1216	arg1	sites					1232:1236	four potential glycosylation sites	1203:1236	four potential glycosylation sites	1203:1236	Therefore, either these four potential glycosylation sites are not glycolysated, or alternatively, oligosaccharide chains at these positions do not play a major role in the folding, intracellular trafficking, stability, or expression of a functional receptor on the cell surface.
2017190	2	30	with	codons	329:334	arg1	Gln					341:343	Gln	341:343	Gln	341:343	Oligonucleotide-directed mutagenesis was used to replace, separately or together, the Asn codons with Gln in each of the six potential glycosylation sites in the receptor.
2017190	3	31	theme	TSH	445:447	arg1	receptors					449:457	mutated TSH receptors	437:457	mutated TSH receptors	437:457	Recombinant wild-type and mutated TSH receptors were stably expressed in Chinese hamster ovary cells.
2017190	8	32	from	folding	1352:1358	arg1	surface					1450:1456	the cell surface	1441:1456	the cell surface	1441:1456	Therefore, either these four potential glycosylation sites are not glycolysated, or alternatively, oligosaccharide chains at these positions do not play a major role in the folding, intracellular trafficking, stability, or expression of a functional receptor on the cell surface.
2017190	0	33	theme	human	33:37	arg1	receptor					51:58	the human thyrotropin receptor	29:58	the human thyrotropin receptor	29:58	Site-directed mutagenesis of the human thyrotropin receptor: role of asparagine-linked oligosaccharides in the expression of a functional receptor.
2017190	6	34	theme	signal	911:916	arg1	transduction					893:904	the transduction	889:904	the transduction of a signal	889:916	This affinity was too low to permit the transduction of a signal, as measured by an increase in intracellular cAMP generation.
2017190	4	35	theme	affinity	518:525	arg1	binding					531:537	High affinity TSH binding	513:537	High affinity TSH binding	513:537	High affinity TSH binding and the cAMP response to TSH stimulation were abolished in the receptor mutated at Asn77 as well as in the receptor mutated at all six potential glycosylation sites.
2017190	3	36	theme	Chinese	484:490	arg1	cells					506:510	Chinese hamster ovary cells	484:510	Chinese hamster ovary cells	484:510	Recombinant wild-type and mutated TSH receptors were stably expressed in Chinese hamster ovary cells.
2017190	5	37	theme	binding	760:766	arg1	affinity					744:751	the affinity	740:751	the affinity of TSH binding	740:766	In the receptor mutated at Asn113, the affinity of TSH binding was markedly decreased (Kd, 2.6 x 10(-8) 3.3 x 10(-10) M in the wild-type receptor).
2017190	9	38	from	expression	1560:1569	arg1	surface					1621:1627	the cell surface	1612:1627	the cell surface	1612:1627	Conversely, our data suggest that N-linked glycosylation of Asn77 and Asn113 does play a role in the expression of a biologically active TSH receptor on the cell surface.
2017190	2	39	from	sites	388:392	arg1	receptor					401:408	the receptor	397:408	the receptor	397:408	Oligonucleotide-directed mutagenesis was used to replace, separately or together, the Asn codons with Gln in each of the six potential glycosylation sites in the receptor.
2017190	5	40	dep	2.6	796:798	arg1	-8					805:806	-8	805:806	-8	805:806	In the receptor mutated at Asn113, the affinity of TSH binding was markedly decreased (Kd, 2.6 x 10(-8) 3.3 x 10(-10) M in the wild-type receptor).
2017190	1	41	theme	human	219:223	arg1	receptor					229:236	a functional human TSH receptor	206:236	a functional human TSH receptor	206:236	We studied the role of glycosylation in the expression of a functional human TSH receptor.
2017190	7	42	from	increase	1140:1147	arg1	levels					1171:1176	intracellular cAMP levels	1152:1176	intracellular cAMP levels	1152:1176	Substitution of Asn at positions 99, 177, 198, and 302 did not appreciably affect the affinity of the TSH receptor for TSH binding or its ability to mediate an increase in intracellular cAMP levels.
2017190	5	43	dep	Kd	792:793	arg1	M					823:823	3.3 x 10(-10) M	809:823	3.3 x 10(-10) M	809:823	In the receptor mutated at Asn113, the affinity of TSH binding was markedly decreased (Kd, 2.6 x 10(-8) 3.3 x 10(-10) M in the wild-type receptor).
2017190	1	44	theme	receptor	229:236	arg1	expression					192:201	the expression	188:201	the expression of a functional human TSH receptor	188:236	We studied the role of glycosylation in the expression of a functional human TSH receptor.
2017190	8	45	theme	receptor	1429:1436	arg1	expression					1402:1411	expression	1402:1411	expression	1402:1411	Therefore, either these four potential glycosylation sites are not glycolysated, or alternatively, oligosaccharide chains at these positions do not play a major role in the folding, intracellular trafficking, stability, or expression of a functional receptor on the cell surface.
2017190	8	45	theme	receptor	1429:1436	arg1	stability					1388:1396	stability	1388:1396	stability	1388:1396	Therefore, either these four potential glycosylation sites are not glycolysated, or alternatively, oligosaccharide chains at these positions do not play a major role in the folding, intracellular trafficking, stability, or expression of a functional receptor on the cell surface.
2017190	8	45	theme	receptor	1429:1436	arg1	folding					1352:1358	folding	1352:1358	folding	1352:1358	Therefore, either these four potential glycosylation sites are not glycolysated, or alternatively, oligosaccharide chains at these positions do not play a major role in the folding, intracellular trafficking, stability, or expression of a functional receptor on the cell surface.
2017190	8	45	theme	receptor	1429:1436	arg1	trafficking					1375:1385	intracellular trafficking	1361:1385	intracellular trafficking	1361:1385	Therefore, either these four potential glycosylation sites are not glycolysated, or alternatively, oligosaccharide chains at these positions do not play a major role in the folding, intracellular trafficking, stability, or expression of a functional receptor on the cell surface.
2017190	1	46	gly	glycosylation	171:183	arg1	receptor					229:236	a functional human TSH receptor	206:236	a functional human TSH receptor	206:236	We studied the role of glycosylation in the expression of a functional human TSH receptor.
2017190	3	47	theme	ovary	500:504	arg1	cells					506:510	Chinese hamster ovary cells	484:510	Chinese hamster ovary cells	484:510	Recombinant wild-type and mutated TSH receptors were stably expressed in Chinese hamster ovary cells.
2017190	9	48	from	surface	1621:1627	arg1	expression					1560:1569	the expression	1556:1569	the expression of a biologically active TSH receptor on the cell surface	1556:1627	Conversely, our data suggest that N-linked glycosylation of Asn77 and Asn113 does play a role in the expression of a biologically active TSH receptor on the cell surface.
2017190	2	49	from	codons	329:334	arg1	each					348:351	each	348:351	each	348:351	Oligonucleotide-directed mutagenesis was used to replace, separately or together, the Asn codons with Gln in each of the six potential glycosylation sites in the receptor.
2017190	2	49	from	codons	329:334	arg1	sites					388:392	the six potential glycosylation sites	356:392	the six potential glycosylation sites in the receptor	356:408	Oligonucleotide-directed mutagenesis was used to replace, separately or together, the Asn codons with Gln in each of the six potential glycosylation sites in the receptor.
2017190	6	50	theme	intracellular	949:961	arg1	generation					968:977	intracellular cAMP generation	949:977	intracellular cAMP generation	949:977	This affinity was too low to permit the transduction of a signal, as measured by an increase in intracellular cAMP generation.
2017190	4	51	theme	TSH	564:566	arg1	stimulation					568:578	TSH stimulation	564:578	TSH stimulation	564:578	High affinity TSH binding and the cAMP response to TSH stimulation were abolished in the receptor mutated at Asn77 as well as in the receptor mutated at all six potential glycosylation sites.
2017190	8	52	from	trafficking	1375:1385	arg1	surface					1450:1456	the cell surface	1441:1456	the cell surface	1441:1456	Therefore, either these four potential glycosylation sites are not glycolysated, or alternatively, oligosaccharide chains at these positions do not play a major role in the folding, intracellular trafficking, stability, or expression of a functional receptor on the cell surface.
2017190	6	53	from	increase	937:944	arg1	generation					968:977	intracellular cAMP generation	949:977	intracellular cAMP generation	949:977	This affinity was too low to permit the transduction of a signal, as measured by an increase in intracellular cAMP generation.
2017190	0	54	theme	receptor	51:58	arg1	mutagenesis					14:24	Site-directed mutagenesis	0:24	Site-directed mutagenesis of the human thyrotropin receptor: role of asparagine-linked oligosaccharides in the expression of a functional receptor.	0:146	Site-directed mutagenesis of the human thyrotropin receptor: role of asparagine-linked oligosaccharides in the expression of a functional receptor.
2017190	9	55	from	receptor	1600:1607	arg1	surface					1621:1627	the cell surface	1612:1627	the cell surface	1612:1627	Conversely, our data suggest that N-linked glycosylation of Asn77 and Asn113 does play a role in the expression of a biologically active TSH receptor on the cell surface.
2017190	0	56	theme	functional	127:136	arg1	receptor					138:145	a functional receptor	125:145	a functional receptor	125:145	Site-directed mutagenesis of the human thyrotropin receptor: role of asparagine-linked oligosaccharides in the expression of a functional receptor.
2017190	9	57	theme	Asn77	1519:1523	arg1	glycosylation					1502:1514	N-linked glycosylation	1493:1514	N-linked glycosylation of Asn77 and Asn113	1493:1534	Conversely, our data suggest that N-linked glycosylation of Asn77 and Asn113 does play a role in the expression of a biologically active TSH receptor on the cell surface.
2017190	8	58	theme	oligosaccharide	1278:1292	arg1	chains					1294:1299	oligosaccharide chains	1278:1299	oligosaccharide chains at these positions	1278:1318	Therefore, either these four potential glycosylation sites are not glycolysated, or alternatively, oligosaccharide chains at these positions do not play a major role in the folding, intracellular trafficking, stability, or expression of a functional receptor on the cell surface.
2017190	9	59	theme	Asn113	1529:1534	arg1	glycosylation					1502:1514	N-linked glycosylation	1493:1514	N-linked glycosylation of Asn77 and Asn113	1493:1534	Conversely, our data suggest that N-linked glycosylation of Asn77 and Asn113 does play a role in the expression of a biologically active TSH receptor on the cell surface.
2017190	4	60	theme	potential	674:682	arg1	sites					698:702	all six potential glycosylation sites	666:702	all six potential glycosylation sites	666:702	High affinity TSH binding and the cAMP response to TSH stimulation were abolished in the receptor mutated at Asn77 as well as in the receptor mutated at all six potential glycosylation sites.
2017190	7	61	from	positions	1003:1011	arg1	Substitution					980:991	Substitution	980:991	Substitution of Asn at positions 99, 177, 198, and 302	980:1033	Substitution of Asn at positions 99, 177, 198, and 302 did not appreciably affect the affinity of the TSH receptor for TSH binding or its ability to mediate an increase in intracellular cAMP levels.
2017190	8	62	gly	glycosylation	1218:1230	arg2	four					1203:1206	four	1203:1206	four	1203:1206	Therefore, either these four potential glycosylation sites are not glycolysated, or alternatively, oligosaccharide chains at these positions do not play a major role in the folding, intracellular trafficking, stability, or expression of a functional receptor on the cell surface.
2017190	8	62	gly	glycosylation	1218:1230	arg2	sites					1232:1236	four potential glycosylation sites	1203:1236	four potential glycosylation sites	1203:1236	Therefore, either these four potential glycosylation sites are not glycolysated, or alternatively, oligosaccharide chains at these positions do not play a major role in the folding, intracellular trafficking, stability, or expression of a functional receptor on the cell surface.
2017190	0	63	theme	oligosaccharides	87:102	arg1	role					61:64	role	61:64	Site-directed mutagenesis of the human thyrotropin receptor: role of asparagine-linked oligosaccharides in the expression of a functional receptor.	0:146	Site-directed mutagenesis of the human thyrotropin receptor: role of asparagine-linked oligosaccharides in the expression of a functional receptor.
2017190	8	64	dep	sites	1232:1236	arg1	either					1190:1195	either	1190:1195	either	1190:1195	Therefore, either these four potential glycosylation sites are not glycolysated, or alternatively, oligosaccharide chains at these positions do not play a major role in the folding, intracellular trafficking, stability, or expression of a functional receptor on the cell surface.
2017190	4	65	gly	glycosylation	684:696	arg2	sites					698:702	all six potential glycosylation sites	666:702	all six potential glycosylation sites	666:702	High affinity TSH binding and the cAMP response to TSH stimulation were abolished in the receptor mutated at Asn77 as well as in the receptor mutated at all six potential glycosylation sites.
2017190	4	65	gly	glycosylation	684:696	arg2	six					670:672	six	670:672	six	670:672	High affinity TSH binding and the cAMP response to TSH stimulation were abolished in the receptor mutated at Asn77 as well as in the receptor mutated at all six potential glycosylation sites.
2017190	4	66	theme	High	513:516	arg1	binding					531:537	High affinity TSH binding	513:537	High affinity TSH binding	513:537	High affinity TSH binding and the cAMP response to TSH stimulation were abolished in the receptor mutated at Asn77 as well as in the receptor mutated at all six potential glycosylation sites.
2017190	1	67	from	role	163:166	arg1	expression					192:201	the expression	188:201	the expression of a functional human TSH receptor	188:236	We studied the role of glycosylation in the expression of a functional human TSH receptor.
2017190	8	68	from	positions	1310:1318	arg1	chains					1294:1299	oligosaccharide chains	1278:1299	oligosaccharide chains at these positions	1278:1318	Therefore, either these four potential glycosylation sites are not glycolysated, or alternatively, oligosaccharide chains at these positions do not play a major role in the folding, intracellular trafficking, stability, or expression of a functional receptor on the cell surface.
2017190	7	69	theme	intracellular	1152:1164	arg1	levels					1171:1176	intracellular cAMP levels	1152:1176	intracellular cAMP levels	1152:1176	Substitution of Asn at positions 99, 177, 198, and 302 did not appreciably affect the affinity of the TSH receptor for TSH binding or its ability to mediate an increase in intracellular cAMP levels.
2017190	9	70	theme	TSH	1596:1598	arg1	receptor					1600:1607	a biologically active TSH receptor	1574:1607	a biologically active TSH receptor on the cell surface	1574:1627	Conversely, our data suggest that N-linked glycosylation of Asn77 and Asn113 does play a role in the expression of a biologically active TSH receptor on the cell surface.
2017190	1	71	theme	TSH	225:227	arg1	receptor					229:236	a functional human TSH receptor	206:236	a functional human TSH receptor	206:236	We studied the role of glycosylation in the expression of a functional human TSH receptor.
2017190	2	72	theme	glycosylation	374:386	arg1	sites					388:392	the six potential glycosylation sites	356:392	the six potential glycosylation sites in the receptor	356:408	Oligonucleotide-directed mutagenesis was used to replace, separately or together, the Asn codons with Gln in each of the six potential glycosylation sites in the receptor.
2017190	4	73	theme	cAMP	547:550	arg1	response					552:559	the cAMP response	543:559	the cAMP response to TSH stimulation	543:578	High affinity TSH binding and the cAMP response to TSH stimulation were abolished in the receptor mutated at Asn77 as well as in the receptor mutated at all six potential glycosylation sites.
2017190	7	74	theme	Asn	996:998	arg1	Substitution					980:991	Substitution	980:991	Substitution of Asn at positions 99, 177, 198, and 302	980:1033	Substitution of Asn at positions 99, 177, 198, and 302 did not appreciably affect the affinity of the TSH receptor for TSH binding or its ability to mediate an increase in intracellular cAMP levels.
2017190	9	75	theme	cell	1616:1619	arg1	surface					1621:1627	the cell surface	1612:1627	the cell surface	1612:1627	Conversely, our data suggest that N-linked glycosylation of Asn77 and Asn113 does play a role in the expression of a biologically active TSH receptor on the cell surface.
2017190	0	76	theme	thyrotropin	39:49	arg1	receptor					51:58	the human thyrotropin receptor	29:58	the human thyrotropin receptor	29:58	Site-directed mutagenesis of the human thyrotropin receptor: role of asparagine-linked oligosaccharides in the expression of a functional receptor.
2017190	9	77	link	N-linked	1493:1500	arg1	glycosylation					1502:1514	N-linked glycosylation	1493:1514	N-linked glycosylation of Asn77 and Asn113	1493:1534	Conversely, our data suggest that N-linked glycosylation of Asn77 and Asn113 does play a role in the expression of a biologically active TSH receptor on the cell surface.
2017190	4	78	theme	TSH	527:529	arg1	binding					531:537	High affinity TSH binding	513:537	High affinity TSH binding	513:537	High affinity TSH binding and the cAMP response to TSH stimulation were abolished in the receptor mutated at Asn77 as well as in the receptor mutated at all six potential glycosylation sites.
2017190	8	79	theme	glycosylation	1218:1230	arg1	sites					1232:1236	four potential glycosylation sites	1203:1236	four potential glycosylation sites	1203:1236	Therefore, either these four potential glycosylation sites are not glycolysated, or alternatively, oligosaccharide chains at these positions do not play a major role in the folding, intracellular trafficking, stability, or expression of a functional receptor on the cell surface.
2017190	5	80	theme	TSH	756:758	arg1	binding					760:766	TSH binding	756:766	TSH binding	756:766	In the receptor mutated at Asn113, the affinity of TSH binding was markedly decreased (Kd, 2.6 x 10(-8) 3.3 x 10(-10) M in the wild-type receptor).
2017190	0	81	link	asparagine-linked	69:85	arg1	oligosaccharides					87:102	asparagine-linked oligosaccharides	69:102	asparagine-linked oligosaccharides	69:102	Site-directed mutagenesis of the human thyrotropin receptor: role of asparagine-linked oligosaccharides in the expression of a functional receptor.
2017190	3	82	theme	hamster	492:498	arg1	cells					506:510	Chinese hamster ovary cells	484:510	Chinese hamster ovary cells	484:510	Recombinant wild-type and mutated TSH receptors were stably expressed in Chinese hamster ovary cells.
2017190	7	83	theme	TSH	1099:1101	arg1	binding					1103:1109	TSH binding	1099:1109	TSH binding	1099:1109	Substitution of Asn at positions 99, 177, 198, and 302 did not appreciably affect the affinity of the TSH receptor for TSH binding or its ability to mediate an increase in intracellular cAMP levels.
2017190	8	84	theme	functional	1418:1427	arg1	receptor					1429:1436	a functional receptor	1416:1436	a functional receptor on the cell surface	1416:1456	Therefore, either these four potential glycosylation sites are not glycolysated, or alternatively, oligosaccharide chains at these positions do not play a major role in the folding, intracellular trafficking, stability, or expression of a functional receptor on the cell surface.
2017190	2	85	theme	Asn	325:327	arg1	codons					329:334	the Asn codons	321:334	the Asn codons with Gln in each of the six potential glycosylation sites in the receptor	321:408	Oligonucleotide-directed mutagenesis was used to replace, separately or together, the Asn codons with Gln in each of the six potential glycosylation sites in the receptor.
2017190	8	86	dep	folding	1352:1358	arg1	the					1348:1350	the	1348:1350	the	1348:1350	Therefore, either these four potential glycosylation sites are not glycolysated, or alternatively, oligosaccharide chains at these positions do not play a major role in the folding, intracellular trafficking, stability, or expression of a functional receptor on the cell surface.
2017190	0	87	dep	mutagenesis	14:24	arg1	role					61:64	role	61:64	Site-directed mutagenesis of the human thyrotropin receptor: role of asparagine-linked oligosaccharides in the expression of a functional receptor.	0:146	Site-directed mutagenesis of the human thyrotropin receptor: role of asparagine-linked oligosaccharides in the expression of a functional receptor.
2017190	7	88	theme	receptor	1086:1093	arg1	affinity					1066:1073	the affinity	1062:1073	the affinity of the TSH receptor for TSH binding or its ability to mediate an increase in intracellular cAMP levels	1062:1176	Substitution of Asn at positions 99, 177, 198, and 302 did not appreciably affect the affinity of the TSH receptor for TSH binding or its ability to mediate an increase in intracellular cAMP levels.
2017190	3	89	theme	mutated	437:443	arg1	receptors					449:457	mutated TSH receptors	437:457	mutated TSH receptors	437:457	Recombinant wild-type and mutated TSH receptors were stably expressed in Chinese hamster ovary cells.
22267120	2	0	from	β-N-acetyl-glucosamine	411:432	arg1	Ser347					448:453	Ser347	448:453	Ser347	448:453	Here we report that the CK2 catalytic subunit CK2α is modified by O-linked β-N-acetyl-glucosamine (O-GlcNAc) on Ser347, proximal to a cyclin-dependent kinase phosphorylation site (Thr344).
22267120	4	1	theme	substrate	993:1001	arg1	selectivity					1003:1013	the kinase substrate selectivity	982:1013	the kinase substrate selectivity of CK2	982:1020	By performing kinase assays with site-specifically phospho- and glyco-modified CK2α in combination with CK2β and Pin1 binding partners on human protein microarrays, we show that the kinase substrate selectivity of CK2 is modulated by these specific post-translational modifications.
22267120	5	2	theme	multiple	1160:1167	arg1	levels					1169:1174	multiple levels	1160:1174	multiple levels	1160:1174	This study suggests how a promiscuous protein kinase can be regulated at multiple levels to achieve particular biological outputs.
22267120	5	3	theme	promiscuous	1113:1123	arg1	kinase					1133:1138	a promiscuous protein kinase	1111:1138	a promiscuous protein kinase	1111:1138	This study suggests how a promiscuous protein kinase can be regulated at multiple levels to achieve particular biological outputs.
22267120	1	4	theme	hundreds	256:263	arg1	phosphorylation					237:251	its phosphorylation	233:251	its phosphorylation of hundreds of substrates	233:277	Protein serine-threonine kinase casein kinase II (CK2) is involved in a myriad of cellular processes including cell growth and proliferation through its phosphorylation of hundreds of substrates, yet how CK2 function is regulated is poorly understood.
22267120	4	5	theme	CK2β	908:911	arg1	partners					930:937	CK2β and Pin1 binding partners	908:937	CK2β and Pin1 binding partners on human protein microarrays	908:966	By performing kinase assays with site-specifically phospho- and glyco-modified CK2α in combination with CK2β and Pin1 binding partners on human protein microarrays, we show that the kinase substrate selectivity of CK2 is modulated by these specific post-translational modifications.
22267120	5	6	theme	protein	1125:1131	arg1	kinase					1133:1138	a promiscuous protein kinase	1111:1138	a promiscuous protein kinase	1111:1138	This study suggests how a promiscuous protein kinase can be regulated at multiple levels to achieve particular biological outputs.
22267120	1	7	theme	substrates	268:277	arg1	hundreds					256:263	hundreds	256:263	hundreds of substrates	256:277	Protein serine-threonine kinase casein kinase II (CK2) is involved in a myriad of cellular processes including cell growth and proliferation through its phosphorylation of hundreds of substrates, yet how CK2 function is regulated is poorly understood.
22267120	1	8	theme	cellular	166:173	arg1	proliferation					211:223	proliferation	211:223	proliferation	211:223	Protein serine-threonine kinase casein kinase II (CK2) is involved in a myriad of cellular processes including cell growth and proliferation through its phosphorylation of hundreds of substrates, yet how CK2 function is regulated is poorly understood.
22267120	1	8	theme	cellular	166:173	arg1	processes					175:183	cellular processes	166:183	cellular processes including cell growth and proliferation	166:223	Protein serine-threonine kinase casein kinase II (CK2) is involved in a myriad of cellular processes including cell growth and proliferation through its phosphorylation of hundreds of substrates, yet how CK2 function is regulated is poorly understood.
22267120	1	8	theme	cellular	166:173	arg1	growth					200:205	cell growth	195:205	cell growth	195:205	Protein serine-threonine kinase casein kinase II (CK2) is involved in a myriad of cellular processes including cell growth and proliferation through its phosphorylation of hundreds of substrates, yet how CK2 function is regulated is poorly understood.
22267120	2	9	theme	phosphorylation	494:508	arg1	site					510:513	a cyclin-dependent kinase phosphorylation site	468:513	a cyclin-dependent kinase phosphorylation site (Thr344)	468:522	Here we report that the CK2 catalytic subunit CK2α is modified by O-linked β-N-acetyl-glucosamine (O-GlcNAc) on Ser347, proximal to a cyclin-dependent kinase phosphorylation site (Thr344).
22267120	2	9	theme	phosphorylation	494:508	arg1	Thr344					516:521	Thr344	516:521	Thr344	516:521	Here we report that the CK2 catalytic subunit CK2α is modified by O-linked β-N-acetyl-glucosamine (O-GlcNAc) on Ser347, proximal to a cyclin-dependent kinase phosphorylation site (Thr344).
22267120	3	10	theme	Ser347	703:708	arg1	glycosylation					686:698	glycosylation	686:698	glycosylation of Ser347	686:708	We use protein semisynthesis to show that phosphorylation of Thr344 increases the cellular stability of CK2α by strengthening its interaction with Pin1, whereas glycosylation of Ser347 seems to be antagonistic to Thr344 phosphorylation and permissive to proteasomal degradation.
22267120	4	11	theme	CK2	1018:1020	arg1	selectivity					1003:1013	the kinase substrate selectivity	982:1013	the kinase substrate selectivity of CK2	982:1020	By performing kinase assays with site-specifically phospho- and glyco-modified CK2α in combination with CK2β and Pin1 binding partners on human protein microarrays, we show that the kinase substrate selectivity of CK2 is modulated by these specific post-translational modifications.
22267120	1	12	theme	Protein	84:90	arg1	CK2					134:136	CK2	134:136	CK2	134:136	Protein serine-threonine kinase casein kinase II (CK2) is involved in a myriad of cellular processes including cell growth and proliferation through its phosphorylation of hundreds of substrates, yet how CK2 function is regulated is poorly understood.
22267120	1	12	theme	Protein	84:90	arg1	kinase					123:128	Protein serine-threonine kinase casein kinase II	84:131	Protein serine-threonine kinase casein kinase II (CK2)	84:137	Protein serine-threonine kinase casein kinase II (CK2) is involved in a myriad of cellular processes including cell growth and proliferation through its phosphorylation of hundreds of substrates, yet how CK2 function is regulated is poorly understood.
22267120	4	13	theme	kinase	986:991	arg1	selectivity					1003:1013	the kinase substrate selectivity	982:1013	the kinase substrate selectivity of CK2	982:1020	By performing kinase assays with site-specifically phospho- and glyco-modified CK2α in combination with CK2β and Pin1 binding partners on human protein microarrays, we show that the kinase substrate selectivity of CK2 is modulated by these specific post-translational modifications.
22267120	1	14	theme	serine-threonine	92:107	arg1	CK2					134:136	CK2	134:136	CK2	134:136	Protein serine-threonine kinase casein kinase II (CK2) is involved in a myriad of cellular processes including cell growth and proliferation through its phosphorylation of hundreds of substrates, yet how CK2 function is regulated is poorly understood.
22267120	1	14	theme	serine-threonine	92:107	arg1	kinase					123:128	Protein serine-threonine kinase casein kinase II	84:131	Protein serine-threonine kinase casein kinase II (CK2)	84:137	Protein serine-threonine kinase casein kinase II (CK2) is involved in a myriad of cellular processes including cell growth and proliferation through its phosphorylation of hundreds of substrates, yet how CK2 function is regulated is poorly understood.
22267120	2	15	theme	catalytic	364:372	arg1	subunit					374:380	the CK2 catalytic subunit CK2α	356:385	the CK2 catalytic subunit CK2α	356:385	Here we report that the CK2 catalytic subunit CK2α is modified by O-linked β-N-acetyl-glucosamine (O-GlcNAc) on Ser347, proximal to a cyclin-dependent kinase phosphorylation site (Thr344).
22267120	3	16	theme	Thr344	738:743	arg1	phosphorylation					745:759	Thr344 phosphorylation	738:759	Thr344 phosphorylation	738:759	We use protein semisynthesis to show that phosphorylation of Thr344 increases the cellular stability of CK2α by strengthening its interaction with Pin1, whereas glycosylation of Ser347 seems to be antagonistic to Thr344 phosphorylation and permissive to proteasomal degradation.
22267120	4	17	theme	glyco-modified	868:881	arg1	CK2α					883:886	site-specifically phospho- and glyco-modified CK2α	837:886	site-specifically phospho- and glyco-modified CK2α	837:886	By performing kinase assays with site-specifically phospho- and glyco-modified CK2α in combination with CK2β and Pin1 binding partners on human protein microarrays, we show that the kinase substrate selectivity of CK2 is modulated by these specific post-translational modifications.
22267120	1	18	theme	kinase	109:114	arg1	CK2					134:136	CK2	134:136	CK2	134:136	Protein serine-threonine kinase casein kinase II (CK2) is involved in a myriad of cellular processes including cell growth and proliferation through its phosphorylation of hundreds of substrates, yet how CK2 function is regulated is poorly understood.
22267120	1	18	theme	kinase	109:114	arg1	kinase					123:128	Protein serine-threonine kinase casein kinase II	84:131	Protein serine-threonine kinase casein kinase II (CK2)	84:137	Protein serine-threonine kinase casein kinase II (CK2) is involved in a myriad of cellular processes including cell growth and proliferation through its phosphorylation of hundreds of substrates, yet how CK2 function is regulated is poorly understood.
22267120	2	19	theme	CK2	360:362	arg1	subunit					374:380	the CK2 catalytic subunit CK2α	356:385	the CK2 catalytic subunit CK2α	356:385	Here we report that the CK2 catalytic subunit CK2α is modified by O-linked β-N-acetyl-glucosamine (O-GlcNAc) on Ser347, proximal to a cyclin-dependent kinase phosphorylation site (Thr344).
22267120	4	20	theme	post-translational	1053:1070	arg1	modifications					1072:1084	these specific post-translational modifications	1038:1084	these specific post-translational modifications	1038:1084	By performing kinase assays with site-specifically phospho- and glyco-modified CK2α in combination with CK2β and Pin1 binding partners on human protein microarrays, we show that the kinase substrate selectivity of CK2 is modulated by these specific post-translational modifications.
22267120	4	21	theme	human	942:946	arg1	microarrays					956:966	human protein microarrays	942:966	human protein microarrays	942:966	By performing kinase assays with site-specifically phospho- and glyco-modified CK2α in combination with CK2β and Pin1 binding partners on human protein microarrays, we show that the kinase substrate selectivity of CK2 is modulated by these specific post-translational modifications.
22267120	1	22	theme	casein	116:121	arg1	CK2					134:136	CK2	134:136	CK2	134:136	Protein serine-threonine kinase casein kinase II (CK2) is involved in a myriad of cellular processes including cell growth and proliferation through its phosphorylation of hundreds of substrates, yet how CK2 function is regulated is poorly understood.
22267120	1	22	theme	casein	116:121	arg1	kinase					123:128	Protein serine-threonine kinase casein kinase II	84:131	Protein serine-threonine kinase casein kinase II (CK2)	84:137	Protein serine-threonine kinase casein kinase II (CK2) is involved in a myriad of cellular processes including cell growth and proliferation through its phosphorylation of hundreds of substrates, yet how CK2 function is regulated is poorly understood.
22267120	2	23	mod	modified	390:397	arg1	subunit					374:380	the CK2 catalytic subunit CK2α	356:385	the CK2 catalytic subunit CK2α	356:385	Here we report that the CK2 catalytic subunit CK2α is modified by O-linked β-N-acetyl-glucosamine (O-GlcNAc) on Ser347, proximal to a cyclin-dependent kinase phosphorylation site (Thr344).
22267120	2	23	mod	modified	390:397	arg3	β-N-acetyl-glucosamine					411:432	O-linked β-N-acetyl-glucosamine	402:432	O-linked β-N-acetyl-glucosamine (O-GlcNAc) on Ser347, proximal to a cyclin-dependent kinase phosphorylation site (Thr344)	402:522	Here we report that the CK2 catalytic subunit CK2α is modified by O-linked β-N-acetyl-glucosamine (O-GlcNAc) on Ser347, proximal to a cyclin-dependent kinase phosphorylation site (Thr344).
22267120	2	23	mod	modified	390:397	arg3	O-GlcNAc					435:442	O-GlcNAc	435:442	O-GlcNAc	435:442	Here we report that the CK2 catalytic subunit CK2α is modified by O-linked β-N-acetyl-glucosamine (O-GlcNAc) on Ser347, proximal to a cyclin-dependent kinase phosphorylation site (Thr344).
22267120	2	24	theme	O-linked	402:409	arg1	O-GlcNAc					435:442	O-GlcNAc	435:442	O-GlcNAc	435:442	Here we report that the CK2 catalytic subunit CK2α is modified by O-linked β-N-acetyl-glucosamine (O-GlcNAc) on Ser347, proximal to a cyclin-dependent kinase phosphorylation site (Thr344).
22267120	2	24	theme	O-linked	402:409	arg1	β-N-acetyl-glucosamine					411:432	O-linked β-N-acetyl-glucosamine	402:432	O-linked β-N-acetyl-glucosamine (O-GlcNAc) on Ser347, proximal to a cyclin-dependent kinase phosphorylation site (Thr344)	402:522	Here we report that the CK2 catalytic subunit CK2α is modified by O-linked β-N-acetyl-glucosamine (O-GlcNAc) on Ser347, proximal to a cyclin-dependent kinase phosphorylation site (Thr344).
22267120	0	25	theme	CK2	14:16	arg1	Regulation					0:9	Regulation	0:9	Regulation of CK2 by phosphorylation and O-GlcNAcylation	0:55	Regulation of CK2 by phosphorylation and O-GlcNAcylation revealed by semisynthesis.
22267120	1	26	dep	involved	142:149	arg1	regulated					304:312	regulated	304:312	is regulated is poorly understood	301:333	Protein serine-threonine kinase casein kinase II (CK2) is involved in a myriad of cellular processes including cell growth and proliferation through its phosphorylation of hundreds of substrates, yet how CK2 function is regulated is poorly understood.
22267120	1	27	theme	cell	195:198	arg1	growth					200:205	cell growth	195:205	cell growth	195:205	Protein serine-threonine kinase casein kinase II (CK2) is involved in a myriad of cellular processes including cell growth and proliferation through its phosphorylation of hundreds of substrates, yet how CK2 function is regulated is poorly understood.
22267120	2	28	theme	proximal	456:463	arg1	Ser347					448:453	Ser347	448:453	Ser347	448:453	Here we report that the CK2 catalytic subunit CK2α is modified by O-linked β-N-acetyl-glucosamine (O-GlcNAc) on Ser347, proximal to a cyclin-dependent kinase phosphorylation site (Thr344).
22267120	1	29	theme	CK2	288:290	arg1	function					292:299	CK2 function	288:299	CK2 function	288:299	Protein serine-threonine kinase casein kinase II (CK2) is involved in a myriad of cellular processes including cell growth and proliferation through its phosphorylation of hundreds of substrates, yet how CK2 function is regulated is poorly understood.
22267120	1	30	theme	processes	175:183	arg1	myriad					156:161	a myriad	154:161	a myriad of cellular processes including cell growth and proliferation	154:223	Protein serine-threonine kinase casein kinase II (CK2) is involved in a myriad of cellular processes including cell growth and proliferation through its phosphorylation of hundreds of substrates, yet how CK2 function is regulated is poorly understood.
22267120	4	31	theme	protein	948:954	arg1	microarrays					956:966	human protein microarrays	942:966	human protein microarrays	942:966	By performing kinase assays with site-specifically phospho- and glyco-modified CK2α in combination with CK2β and Pin1 binding partners on human protein microarrays, we show that the kinase substrate selectivity of CK2 is modulated by these specific post-translational modifications.
22267120	3	32	theme	Thr344	586:591	arg1	phosphorylation					567:581	phosphorylation	567:581	phosphorylation of Thr344	567:591	We use protein semisynthesis to show that phosphorylation of Thr344 increases the cellular stability of CK2α by strengthening its interaction with Pin1, whereas glycosylation of Ser347 seems to be antagonistic to Thr344 phosphorylation and permissive to proteasomal degradation.
22267120	3	33	gly	glycosylation	686:698	arg1	Ser347					703:708	Ser347	703:708	Ser347	703:708	We use protein semisynthesis to show that phosphorylation of Thr344 increases the cellular stability of CK2α by strengthening its interaction with Pin1, whereas glycosylation of Ser347 seems to be antagonistic to Thr344 phosphorylation and permissive to proteasomal degradation.
22267120	4	34	theme	Pin1	917:920	arg1	partners					930:937	CK2β and Pin1 binding partners	908:937	CK2β and Pin1 binding partners on human protein microarrays	908:966	By performing kinase assays with site-specifically phospho- and glyco-modified CK2α in combination with CK2β and Pin1 binding partners on human protein microarrays, we show that the kinase substrate selectivity of CK2 is modulated by these specific post-translational modifications.
22267120	3	35	theme	CK2α	629:632	arg1	stability					616:624	the cellular stability	603:624	the cellular stability of CK2α	603:632	We use protein semisynthesis to show that phosphorylation of Thr344 increases the cellular stability of CK2α by strengthening its interaction with Pin1, whereas glycosylation of Ser347 seems to be antagonistic to Thr344 phosphorylation and permissive to proteasomal degradation.
22267120	5	36	theme	particular	1187:1196	arg1	outputs					1209:1215	particular biological outputs	1187:1215	particular biological outputs	1187:1215	This study suggests how a promiscuous protein kinase can be regulated at multiple levels to achieve particular biological outputs.
22267120	4	37	from	partners	930:937	arg1	microarrays					956:966	human protein microarrays	942:966	human protein microarrays	942:966	By performing kinase assays with site-specifically phospho- and glyco-modified CK2α in combination with CK2β and Pin1 binding partners on human protein microarrays, we show that the kinase substrate selectivity of CK2 is modulated by these specific post-translational modifications.
22267120	4	38	theme	phospho-	855:862	arg1	CK2α					883:886	site-specifically phospho- and glyco-modified CK2α	837:886	site-specifically phospho- and glyco-modified CK2α	837:886	By performing kinase assays with site-specifically phospho- and glyco-modified CK2α in combination with CK2β and Pin1 binding partners on human protein microarrays, we show that the kinase substrate selectivity of CK2 is modulated by these specific post-translational modifications.
22267120	5	39	theme	biological	1198:1207	arg1	outputs					1209:1215	particular biological outputs	1187:1215	particular biological outputs	1187:1215	This study suggests how a promiscuous protein kinase can be regulated at multiple levels to achieve particular biological outputs.
22267120	3	40	theme	cellular	607:614	arg1	stability					616:624	the cellular stability	603:624	the cellular stability of CK2α	603:632	We use protein semisynthesis to show that phosphorylation of Thr344 increases the cellular stability of CK2α by strengthening its interaction with Pin1, whereas glycosylation of Ser347 seems to be antagonistic to Thr344 phosphorylation and permissive to proteasomal degradation.
22267120	4	41	theme	kinase	818:823	arg1	assays					825:830	kinase assays	818:830	kinase assays with site-specifically phospho- and glyco-modified CK2α	818:886	By performing kinase assays with site-specifically phospho- and glyco-modified CK2α in combination with CK2β and Pin1 binding partners on human protein microarrays, we show that the kinase substrate selectivity of CK2 is modulated by these specific post-translational modifications.
22267120	3	42	theme	protein	532:538	arg1	semisynthesis					540:552	protein semisynthesis	532:552	protein semisynthesis	532:552	We use protein semisynthesis to show that phosphorylation of Thr344 increases the cellular stability of CK2α by strengthening its interaction with Pin1, whereas glycosylation of Ser347 seems to be antagonistic to Thr344 phosphorylation and permissive to proteasomal degradation.
22267120	4	43	theme	binding	922:928	arg1	partners					930:937	CK2β and Pin1 binding partners	908:937	CK2β and Pin1 binding partners on human protein microarrays	908:966	By performing kinase assays with site-specifically phospho- and glyco-modified CK2α in combination with CK2β and Pin1 binding partners on human protein microarrays, we show that the kinase substrate selectivity of CK2 is modulated by these specific post-translational modifications.
22267120	2	44	link	O-linked	402:409	arg1	O-GlcNAc					435:442	O-GlcNAc	435:442	O-GlcNAc	435:442	Here we report that the CK2 catalytic subunit CK2α is modified by O-linked β-N-acetyl-glucosamine (O-GlcNAc) on Ser347, proximal to a cyclin-dependent kinase phosphorylation site (Thr344).
22267120	2	44	link	O-linked	402:409	arg1	β-N-acetyl-glucosamine					411:432	O-linked β-N-acetyl-glucosamine	402:432	O-linked β-N-acetyl-glucosamine (O-GlcNAc) on Ser347, proximal to a cyclin-dependent kinase phosphorylation site (Thr344)	402:522	Here we report that the CK2 catalytic subunit CK2α is modified by O-linked β-N-acetyl-glucosamine (O-GlcNAc) on Ser347, proximal to a cyclin-dependent kinase phosphorylation site (Thr344).
22267120	3	45	with	interaction	655:665	arg1	Pin1					672:675	Pin1	672:675	Pin1	672:675	We use protein semisynthesis to show that phosphorylation of Thr344 increases the cellular stability of CK2α by strengthening its interaction with Pin1, whereas glycosylation of Ser347 seems to be antagonistic to Thr344 phosphorylation and permissive to proteasomal degradation.
22267120	4	46	with	combination	891:901	arg1	partners					930:937	CK2β and Pin1 binding partners	908:937	CK2β and Pin1 binding partners on human protein microarrays	908:966	By performing kinase assays with site-specifically phospho- and glyco-modified CK2α in combination with CK2β and Pin1 binding partners on human protein microarrays, we show that the kinase substrate selectivity of CK2 is modulated by these specific post-translational modifications.
22267120	2	47	theme	kinase	487:492	arg1	site					510:513	a cyclin-dependent kinase phosphorylation site	468:513	a cyclin-dependent kinase phosphorylation site (Thr344)	468:522	Here we report that the CK2 catalytic subunit CK2α is modified by O-linked β-N-acetyl-glucosamine (O-GlcNAc) on Ser347, proximal to a cyclin-dependent kinase phosphorylation site (Thr344).
22267120	2	47	theme	kinase	487:492	arg1	Thr344					516:521	Thr344	516:521	Thr344	516:521	Here we report that the CK2 catalytic subunit CK2α is modified by O-linked β-N-acetyl-glucosamine (O-GlcNAc) on Ser347, proximal to a cyclin-dependent kinase phosphorylation site (Thr344).
22267120	4	48	with	assays	825:830	arg1	CK2α					883:886	site-specifically phospho- and glyco-modified CK2α	837:886	site-specifically phospho- and glyco-modified CK2α	837:886	By performing kinase assays with site-specifically phospho- and glyco-modified CK2α in combination with CK2β and Pin1 binding partners on human protein microarrays, we show that the kinase substrate selectivity of CK2 is modulated by these specific post-translational modifications.
22267120	2	49	theme	cyclin-dependent	470:485	arg1	site					510:513	a cyclin-dependent kinase phosphorylation site	468:513	a cyclin-dependent kinase phosphorylation site (Thr344)	468:522	Here we report that the CK2 catalytic subunit CK2α is modified by O-linked β-N-acetyl-glucosamine (O-GlcNAc) on Ser347, proximal to a cyclin-dependent kinase phosphorylation site (Thr344).
22267120	2	49	theme	cyclin-dependent	470:485	arg1	Thr344					516:521	Thr344	516:521	Thr344	516:521	Here we report that the CK2 catalytic subunit CK2α is modified by O-linked β-N-acetyl-glucosamine (O-GlcNAc) on Ser347, proximal to a cyclin-dependent kinase phosphorylation site (Thr344).
22267120	4	50	theme	specific	1044:1051	arg1	modifications					1072:1084	these specific post-translational modifications	1038:1084	these specific post-translational modifications	1038:1084	By performing kinase assays with site-specifically phospho- and glyco-modified CK2α in combination with CK2β and Pin1 binding partners on human protein microarrays, we show that the kinase substrate selectivity of CK2 is modulated by these specific post-translational modifications.
22267120	3	51	theme	proteasomal	779:789	arg1	degradation					791:801	proteasomal degradation	779:801	proteasomal degradation	779:801	We use protein semisynthesis to show that phosphorylation of Thr344 increases the cellular stability of CK2α by strengthening its interaction with Pin1, whereas glycosylation of Ser347 seems to be antagonistic to Thr344 phosphorylation and permissive to proteasomal degradation.
9343410	4	0	dep	mapping	867:873	arg1	the					863:865	the	863:865	the	863:865	When the model Sp1 peptide was overexpressed in primate cells, this 97-amino-acid domain of Sp1 was found to contain a dominant O-GlcNAc residue at high stoichiometry, which allowed the mapping and mutagenesis of this glycosylation site.
9343410	6	1	gly	glycosylation	1174:1186	arg2	site					1188:1191	the mapped glycosylation site	1163:1191	the mapped glycosylation site	1163:1191	In HeLa cells, the mutation at the mapped glycosylation site was permissive for transcriptional activation.
9343410	3	2	theme	Sp1	485:487	arg1	domain					475:480	the previously characterized glutamine-rich transactivation domain	415:480	the previously characterized glutamine-rich transactivation domain of Sp1 (B-c)	415:493	In this paper we describe the use of the previously characterized glutamine-rich transactivation domain of Sp1 (B-c) as a model to investigate the role of O-GlcNAc in Sp1's transcriptionally relevant protein-to-protein interactions with the TATA-binding-protein-associated factor (TAF110) and holo-Sp1.
9343410	3	2	theme	Sp1	485:487	arg1	Sp1					485:487	Sp1	485:487	Sp1 (B-c)	485:493	In this paper we describe the use of the previously characterized glutamine-rich transactivation domain of Sp1 (B-c) as a model to investigate the role of O-GlcNAc in Sp1's transcriptionally relevant protein-to-protein interactions with the TATA-binding-protein-associated factor (TAF110) and holo-Sp1.
9343410	1	3	link	O-linked	85:92	arg1	O-GlcNAc					115:122	O-GlcNAc	115:122	O-GlcNAc	115:122	The O-linked N-acetylglucosamine (O-GlcNAc) modification of proteins is dynamic and abundant in the nucleus and cytosol.
9343410	1	3	link	O-linked	85:92	arg1	N-acetylglucosamine					94:112	O-linked N-acetylglucosamine	85:112	The O-linked N-acetylglucosamine (O-GlcNAc) modification of proteins	81:148	The O-linked N-acetylglucosamine (O-GlcNAc) modification of proteins is dynamic and abundant in the nucleus and cytosol.
9343410	1	4	from	dynamic	153:159	arg1	cytosol					193:199	cytosol	193:199	cytosol	193:199	The O-linked N-acetylglucosamine (O-GlcNAc) modification of proteins is dynamic and abundant in the nucleus and cytosol.
9343410	1	4	from	dynamic	153:159	arg1	nucleus					181:187	nucleus	181:187	nucleus	181:187	The O-linked N-acetylglucosamine (O-GlcNAc) modification of proteins is dynamic and abundant in the nucleus and cytosol.
9343410	2	5	theme	O-GlcNAc	326:333	arg1	role					318:321	the functional role	303:321	the functional role of O-GlcNAc in these proteins	303:351	Several transcription factors, including Sp1, have been shown to contain this modification; however, the functional role of O-GlcNAc in these proteins has not been determined.
9343410	6	6	from	permissive	1197:1206	arg1	cells					1140:1144	HeLa cells	1135:1144	HeLa cells	1135:1144	In HeLa cells, the mutation at the mapped glycosylation site was permissive for transcriptional activation.
9343410	4	7	from	stoichiometry	834:846	arg1	residue					818:824	a dominant O-GlcNAc residue	798:824	a dominant O-GlcNAc residue	798:824	When the model Sp1 peptide was overexpressed in primate cells, this 97-amino-acid domain of Sp1 was found to contain a dominant O-GlcNAc residue at high stoichiometry, which allowed the mapping and mutagenesis of this glycosylation site.
9343410	4	8	gly	glycosylation	899:911	arg2	site					913:916	this glycosylation site	894:916	this glycosylation site	894:916	When the model Sp1 peptide was overexpressed in primate cells, this 97-amino-acid domain of Sp1 was found to contain a dominant O-GlcNAc residue at high stoichiometry, which allowed the mapping and mutagenesis of this glycosylation site.
9343410	6	9	theme	mapped	1167:1172	arg1	site					1188:1191	the mapped glycosylation site	1163:1191	the mapped glycosylation site	1163:1191	In HeLa cells, the mutation at the mapped glycosylation site was permissive for transcriptional activation.
9343410	5	10	theme	interaction	928:938	arg1	studies					940:946	In vitro interaction studies	919:946	In vitro interaction studies between this segment of Sp1 and Drosophila TAF110 or holo-Sp1	919:1008	In vitro interaction studies between this segment of Sp1 and Drosophila TAF110 or holo-Sp1 indicate that the O-GlcNAc modification functions to inhibit the largely hydrophobic interactions between these proteins.
9343410	6	11	theme	transcriptional	1212:1226	arg1	activation					1228:1237	transcriptional activation	1212:1237	transcriptional activation	1212:1237	In HeLa cells, the mutation at the mapped glycosylation site was permissive for transcriptional activation.
9343410	4	12	contain	contain	790:796	arg1	Sp1					773:775	Sp1	773:775	Sp1	773:775	When the model Sp1 peptide was overexpressed in primate cells, this 97-amino-acid domain of Sp1 was found to contain a dominant O-GlcNAc residue at high stoichiometry, which allowed the mapping and mutagenesis of this glycosylation site.
9343410	4	12	contain	contain	790:796	arg2	residue					818:824	a dominant O-GlcNAc residue	798:824	a dominant O-GlcNAc residue	798:824	When the model Sp1 peptide was overexpressed in primate cells, this 97-amino-acid domain of Sp1 was found to contain a dominant O-GlcNAc residue at high stoichiometry, which allowed the mapping and mutagenesis of this glycosylation site.
9343410	4	12	contain	contain	790:796	arg1	domain					763:768	this 97-amino-acid domain	744:768	this 97-amino-acid domain of Sp1	744:775	When the model Sp1 peptide was overexpressed in primate cells, this 97-amino-acid domain of Sp1 was found to contain a dominant O-GlcNAc residue at high stoichiometry, which allowed the mapping and mutagenesis of this glycosylation site.
9343410	4	13	theme	Sp1	696:698	arg1	peptide					700:706	the model Sp1 peptide	686:706	the model Sp1 peptide	686:706	When the model Sp1 peptide was overexpressed in primate cells, this 97-amino-acid domain of Sp1 was found to contain a dominant O-GlcNAc residue at high stoichiometry, which allowed the mapping and mutagenesis of this glycosylation site.
9343410	2	14	from	role	318:321	arg1	proteins					344:351	these proteins	338:351	these proteins	338:351	Several transcription factors, including Sp1, have been shown to contain this modification; however, the functional role of O-GlcNAc in these proteins has not been determined.
9343410	8	15	theme	ectopic	1405:1411	arg1	interactions					1413:1424	untimely and ectopic interactions	1392:1424	untimely and ectopic interactions	1392:1424	O-GlcNAc may thereby prevent untimely and ectopic interactions.
9343410	4	16	theme	O-GlcNAc	809:816	arg1	residue					818:824	a dominant O-GlcNAc residue	798:824	a dominant O-GlcNAc residue	798:824	When the model Sp1 peptide was overexpressed in primate cells, this 97-amino-acid domain of Sp1 was found to contain a dominant O-GlcNAc residue at high stoichiometry, which allowed the mapping and mutagenesis of this glycosylation site.
9343410	7	17	theme	interaction	1303:1313	arg1	domain					1315:1320	an interaction domain	1300:1320	an interaction domain	1300:1320	We propose the hypothesis that the removal of O-GlcNAc from an interaction domain can be a signal for protein association.
9343410	4	18	theme	97-amino-acid	749:761	arg1	Sp1					773:775	Sp1	773:775	Sp1	773:775	When the model Sp1 peptide was overexpressed in primate cells, this 97-amino-acid domain of Sp1 was found to contain a dominant O-GlcNAc residue at high stoichiometry, which allowed the mapping and mutagenesis of this glycosylation site.
9343410	4	18	theme	97-amino-acid	749:761	arg1	domain					763:768	this 97-amino-acid domain	744:768	this 97-amino-acid domain of Sp1	744:775	When the model Sp1 peptide was overexpressed in primate cells, this 97-amino-acid domain of Sp1 was found to contain a dominant O-GlcNAc residue at high stoichiometry, which allowed the mapping and mutagenesis of this glycosylation site.
9343410	8	19	theme	untimely	1392:1399	arg1	interactions					1413:1424	untimely and ectopic interactions	1392:1424	untimely and ectopic interactions	1392:1424	O-GlcNAc may thereby prevent untimely and ectopic interactions.
9343410	1	20	mod	modification	125:136	arg3	O-GlcNAc					115:122	O-GlcNAc	115:122	O-GlcNAc	115:122	The O-linked N-acetylglucosamine (O-GlcNAc) modification of proteins is dynamic and abundant in the nucleus and cytosol.
9343410	1	20	mod	modification	125:136	arg3	N-acetylglucosamine					94:112	O-linked N-acetylglucosamine	85:112	The O-linked N-acetylglucosamine (O-GlcNAc) modification of proteins	81:148	The O-linked N-acetylglucosamine (O-GlcNAc) modification of proteins is dynamic and abundant in the nucleus and cytosol.
9343410	1	20	mod	modification	125:136	arg1	proteins					141:148	proteins	141:148	proteins	141:148	The O-linked N-acetylglucosamine (O-GlcNAc) modification of proteins is dynamic and abundant in the nucleus and cytosol.
9343410	3	21	with	interactions	597:608	arg1	TAF110					659:664	TAF110	659:664	TAF110	659:664	In this paper we describe the use of the previously characterized glutamine-rich transactivation domain of Sp1 (B-c) as a model to investigate the role of O-GlcNAc in Sp1's transcriptionally relevant protein-to-protein interactions with the TATA-binding-protein-associated factor (TAF110) and holo-Sp1.
9343410	3	21	with	interactions	597:608	arg1	holo-Sp1					671:678	holo-Sp1	671:678	holo-Sp1	671:678	In this paper we describe the use of the previously characterized glutamine-rich transactivation domain of Sp1 (B-c) as a model to investigate the role of O-GlcNAc in Sp1's transcriptionally relevant protein-to-protein interactions with the TATA-binding-protein-associated factor (TAF110) and holo-Sp1.
9343410	3	21	with	interactions	597:608	arg1	factor					651:656	the TATA-binding-protein-associated factor	615:656	the TATA-binding-protein-associated factor (TAF110)	615:665	In this paper we describe the use of the previously characterized glutamine-rich transactivation domain of Sp1 (B-c) as a model to investigate the role of O-GlcNAc in Sp1's transcriptionally relevant protein-to-protein interactions with the TATA-binding-protein-associated factor (TAF110) and holo-Sp1.
9343410	4	22	theme	high	829:832	arg1	stoichiometry					834:846	high stoichiometry	829:846	high stoichiometry	829:846	When the model Sp1 peptide was overexpressed in primate cells, this 97-amino-acid domain of Sp1 was found to contain a dominant O-GlcNAc residue at high stoichiometry, which allowed the mapping and mutagenesis of this glycosylation site.
9343410	5	23	theme	hydrophobic	1083:1093	arg1	interactions					1095:1106	the largely hydrophobic interactions	1071:1106	the largely hydrophobic interactions between these proteins	1071:1129	In vitro interaction studies between this segment of Sp1 and Drosophila TAF110 or holo-Sp1 indicate that the O-GlcNAc modification functions to inhibit the largely hydrophobic interactions between these proteins.
9343410	0	24	theme	O	0:0	arg1	glycosylation					2:14	O glycosylation	0:14	O glycosylation of an Sp1-derived peptide	0:40	O glycosylation of an Sp1-derived peptide blocks known Sp1 protein interactions.
9343410	1	25	theme	O-linked	85:92	arg1	O-GlcNAc					115:122	O-GlcNAc	115:122	O-GlcNAc	115:122	The O-linked N-acetylglucosamine (O-GlcNAc) modification of proteins is dynamic and abundant in the nucleus and cytosol.
9343410	1	25	theme	O-linked	85:92	arg1	N-acetylglucosamine					94:112	O-linked N-acetylglucosamine	85:112	The O-linked N-acetylglucosamine (O-GlcNAc) modification of proteins	81:148	The O-linked N-acetylglucosamine (O-GlcNAc) modification of proteins is dynamic and abundant in the nucleus and cytosol.
9343410	6	26	from	cells	1140:1144	arg1	permissive					1197:1206	permissive	1197:1206	permissive	1197:1206	In HeLa cells, the mutation at the mapped glycosylation site was permissive for transcriptional activation.
9343410	6	26	from	cells	1140:1144	arg1	mutation					1151:1158	the mutation	1147:1158	the mutation at the mapped glycosylation site	1147:1191	In HeLa cells, the mutation at the mapped glycosylation site was permissive for transcriptional activation.
9343410	0	27	link	Sp1-derived	22:32	arg1	peptide					34:40	an Sp1-derived peptide	19:40	an Sp1-derived peptide	19:40	O glycosylation of an Sp1-derived peptide blocks known Sp1 protein interactions.
9343410	1	28	theme	N-acetylglucosamine	94:112	arg1	modification					125:136	The O-linked N-acetylglucosamine (O-GlcNAc) modification	81:136	The O-linked N-acetylglucosamine (O-GlcNAc) modification of proteins	81:148	The O-linked N-acetylglucosamine (O-GlcNAc) modification of proteins is dynamic and abundant in the nucleus and cytosol.
9343410	1	28	theme	N-acetylglucosamine	94:112	arg1	dynamic					153:159	dynamic	153:159	dynamic	153:159	The O-linked N-acetylglucosamine (O-GlcNAc) modification of proteins is dynamic and abundant in the nucleus and cytosol.
9343410	5	29	theme	TAF110	991:996	arg1	segment					961:967	this segment	956:967	this segment of Sp1 and Drosophila TAF110 or holo-Sp1	956:1008	In vitro interaction studies between this segment of Sp1 and Drosophila TAF110 or holo-Sp1 indicate that the O-GlcNAc modification functions to inhibit the largely hydrophobic interactions between these proteins.
9343410	5	30	theme	In	919:920	arg1	studies					940:946	In vitro interaction studies	919:946	In vitro interaction studies between this segment of Sp1 and Drosophila TAF110 or holo-Sp1	919:1008	In vitro interaction studies between this segment of Sp1 and Drosophila TAF110 or holo-Sp1 indicate that the O-GlcNAc modification functions to inhibit the largely hydrophobic interactions between these proteins.
9343410	2	31	contain	contain	267:273	arg1	factors					224:230	Several transcription factors	202:230	Several transcription factors	202:230	Several transcription factors, including Sp1, have been shown to contain this modification; however, the functional role of O-GlcNAc in these proteins has not been determined.
9343410	2	31	contain	contain	267:273	arg1	Sp1					243:245	Sp1	243:245	Sp1	243:245	Several transcription factors, including Sp1, have been shown to contain this modification; however, the functional role of O-GlcNAc in these proteins has not been determined.
9343410	2	31	contain	contain	267:273	arg2	modification					280:291	this modification	275:291	this modification	275:291	Several transcription factors, including Sp1, have been shown to contain this modification; however, the functional role of O-GlcNAc in these proteins has not been determined.
9343410	3	32	theme	TATA-binding-protein-associated	619:649	arg1	TAF110					659:664	TAF110	659:664	TAF110	659:664	In this paper we describe the use of the previously characterized glutamine-rich transactivation domain of Sp1 (B-c) as a model to investigate the role of O-GlcNAc in Sp1's transcriptionally relevant protein-to-protein interactions with the TATA-binding-protein-associated factor (TAF110) and holo-Sp1.
9343410	3	32	theme	TATA-binding-protein-associated	619:649	arg1	factor					651:656	the TATA-binding-protein-associated factor	615:656	the TATA-binding-protein-associated factor (TAF110)	615:665	In this paper we describe the use of the previously characterized glutamine-rich transactivation domain of Sp1 (B-c) as a model to investigate the role of O-GlcNAc in Sp1's transcriptionally relevant protein-to-protein interactions with the TATA-binding-protein-associated factor (TAF110) and holo-Sp1.
9343410	4	33	theme	primate	729:735	arg1	cells					737:741	primate cells	729:741	primate cells	729:741	When the model Sp1 peptide was overexpressed in primate cells, this 97-amino-acid domain of Sp1 was found to contain a dominant O-GlcNAc residue at high stoichiometry, which allowed the mapping and mutagenesis of this glycosylation site.
9343410	3	34	theme	characterized	430:442	arg1	domain					475:480	the previously characterized glutamine-rich transactivation domain	415:480	the previously characterized glutamine-rich transactivation domain of Sp1 (B-c)	415:493	In this paper we describe the use of the previously characterized glutamine-rich transactivation domain of Sp1 (B-c) as a model to investigate the role of O-GlcNAc in Sp1's transcriptionally relevant protein-to-protein interactions with the TATA-binding-protein-associated factor (TAF110) and holo-Sp1.
9343410	3	34	theme	characterized	430:442	arg1	Sp1					485:487	Sp1	485:487	Sp1 (B-c)	485:493	In this paper we describe the use of the previously characterized glutamine-rich transactivation domain of Sp1 (B-c) as a model to investigate the role of O-GlcNAc in Sp1's transcriptionally relevant protein-to-protein interactions with the TATA-binding-protein-associated factor (TAF110) and holo-Sp1.
9343410	0	35	theme	peptide	34:40	arg1	glycosylation					2:14	O glycosylation	0:14	O glycosylation of an Sp1-derived peptide	0:40	O glycosylation of an Sp1-derived peptide blocks known Sp1 protein interactions.
9343410	4	36	theme	site	913:916	arg1	mutagenesis					879:889	mutagenesis	879:889	mutagenesis	879:889	When the model Sp1 peptide was overexpressed in primate cells, this 97-amino-acid domain of Sp1 was found to contain a dominant O-GlcNAc residue at high stoichiometry, which allowed the mapping and mutagenesis of this glycosylation site.
9343410	4	36	theme	site	913:916	arg1	mapping					867:873	mapping	867:873	mapping	867:873	When the model Sp1 peptide was overexpressed in primate cells, this 97-amino-acid domain of Sp1 was found to contain a dominant O-GlcNAc residue at high stoichiometry, which allowed the mapping and mutagenesis of this glycosylation site.
9343410	0	37	gly	glycosylation	2:14	arg1	peptide					34:40	an Sp1-derived peptide	19:40	an Sp1-derived peptide	19:40	O glycosylation of an Sp1-derived peptide blocks known Sp1 protein interactions.
9343410	6	38	theme	glycosylation	1174:1186	arg1	site					1188:1191	the mapped glycosylation site	1163:1191	the mapped glycosylation site	1163:1191	In HeLa cells, the mutation at the mapped glycosylation site was permissive for transcriptional activation.
9343410	7	39	theme	O-GlcNAc	1286:1293	arg1	signal					1331:1336	a signal	1329:1336	a signal for protein association	1329:1360	We propose the hypothesis that the removal of O-GlcNAc from an interaction domain can be a signal for protein association.
9343410	7	39	theme	O-GlcNAc	1286:1293	arg1	removal					1275:1281	the removal	1271:1281	the removal of O-GlcNAc from an interaction domain	1271:1320	We propose the hypothesis that the removal of O-GlcNAc from an interaction domain can be a signal for protein association.
9343410	0	40	theme	Sp1-derived	22:32	arg1	peptide					34:40	an Sp1-derived peptide	19:40	an Sp1-derived peptide	19:40	O glycosylation of an Sp1-derived peptide blocks known Sp1 protein interactions.
9343410	4	41	theme	glycosylation	899:911	arg1	site					913:916	this glycosylation site	894:916	this glycosylation site	894:916	When the model Sp1 peptide was overexpressed in primate cells, this 97-amino-acid domain of Sp1 was found to contain a dominant O-GlcNAc residue at high stoichiometry, which allowed the mapping and mutagenesis of this glycosylation site.
9343410	1	42	dep	nucleus	181:187	arg1	the					177:179	the	177:179	the	177:179	The O-linked N-acetylglucosamine (O-GlcNAc) modification of proteins is dynamic and abundant in the nucleus and cytosol.
9343410	0	43	theme	known	49:53	arg1	interactions					67:78	known Sp1 protein interactions	49:78	known Sp1 protein interactions	49:78	O glycosylation of an Sp1-derived peptide blocks known Sp1 protein interactions.
9343410	7	44	theme	protein	1342:1348	arg1	association					1350:1360	protein association	1342:1360	protein association	1342:1360	We propose the hypothesis that the removal of O-GlcNAc from an interaction domain can be a signal for protein association.
9343410	3	45	theme	O-GlcNAc	533:540	arg1	role					525:528	the role	521:528	the role of O-GlcNAc in Sp1's transcriptionally relevant protein-to-protein interactions with the TATA-binding-protein-associated factor (TAF110) and holo-Sp1	521:678	In this paper we describe the use of the previously characterized glutamine-rich transactivation domain of Sp1 (B-c) as a model to investigate the role of O-GlcNAc in Sp1's transcriptionally relevant protein-to-protein interactions with the TATA-binding-protein-associated factor (TAF110) and holo-Sp1.
9343410	3	46	theme	domain	475:480	arg1	use					408:410	the use	404:410	the use of the previously characterized glutamine-rich transactivation domain of Sp1 (B-c) as a model to investigate the role of O-GlcNAc in Sp1's transcriptionally relevant protein-to-protein interactions with the TATA-binding-protein-associated factor (TAF110) and holo-Sp1	404:678	In this paper we describe the use of the previously characterized glutamine-rich transactivation domain of Sp1 (B-c) as a model to investigate the role of O-GlcNAc in Sp1's transcriptionally relevant protein-to-protein interactions with the TATA-binding-protein-associated factor (TAF110) and holo-Sp1.
9343410	5	47	dep	In	919:920	arg1	vitro					922:926	vitro	922:926	vitro	922:926	In vitro interaction studies between this segment of Sp1 and Drosophila TAF110 or holo-Sp1 indicate that the O-GlcNAc modification functions to inhibit the largely hydrophobic interactions between these proteins.
9343410	2	48	theme	Several	202:208	arg1	factors					224:230	Several transcription factors	202:230	Several transcription factors	202:230	Several transcription factors, including Sp1, have been shown to contain this modification; however, the functional role of O-GlcNAc in these proteins has not been determined.
9343410	2	48	theme	Several	202:208	arg1	Sp1					243:245	Sp1	243:245	Sp1	243:245	Several transcription factors, including Sp1, have been shown to contain this modification; however, the functional role of O-GlcNAc in these proteins has not been determined.
9343410	2	49	theme	transcription	210:222	arg1	factors					224:230	Several transcription factors	202:230	Several transcription factors	202:230	Several transcription factors, including Sp1, have been shown to contain this modification; however, the functional role of O-GlcNAc in these proteins has not been determined.
9343410	2	49	theme	transcription	210:222	arg1	Sp1					243:245	Sp1	243:245	Sp1	243:245	Several transcription factors, including Sp1, have been shown to contain this modification; however, the functional role of O-GlcNAc in these proteins has not been determined.
9343410	4	50	theme	model	690:694	arg1	peptide					700:706	the model Sp1 peptide	686:706	the model Sp1 peptide	686:706	When the model Sp1 peptide was overexpressed in primate cells, this 97-amino-acid domain of Sp1 was found to contain a dominant O-GlcNAc residue at high stoichiometry, which allowed the mapping and mutagenesis of this glycosylation site.
9343410	5	51	theme	Drosophila	980:989	arg1	TAF110					991:996	Drosophila TAF110	980:996	Drosophila TAF110	980:996	In vitro interaction studies between this segment of Sp1 and Drosophila TAF110 or holo-Sp1 indicate that the O-GlcNAc modification functions to inhibit the largely hydrophobic interactions between these proteins.
9343410	4	52	theme	Sp1	773:775	arg1	Sp1					773:775	Sp1	773:775	Sp1	773:775	When the model Sp1 peptide was overexpressed in primate cells, this 97-amino-acid domain of Sp1 was found to contain a dominant O-GlcNAc residue at high stoichiometry, which allowed the mapping and mutagenesis of this glycosylation site.
9343410	4	52	theme	Sp1	773:775	arg1	domain					763:768	this 97-amino-acid domain	744:768	this 97-amino-acid domain of Sp1	744:775	When the model Sp1 peptide was overexpressed in primate cells, this 97-amino-acid domain of Sp1 was found to contain a dominant O-GlcNAc residue at high stoichiometry, which allowed the mapping and mutagenesis of this glycosylation site.
9343410	3	53	theme	protein-to-protein	578:595	arg1	interactions					597:608	Sp1's transcriptionally relevant protein-to-protein interactions	545:608	Sp1's transcriptionally relevant protein-to-protein interactions with the TATA-binding-protein-associated factor (TAF110) and holo-Sp1	545:678	In this paper we describe the use of the previously characterized glutamine-rich transactivation domain of Sp1 (B-c) as a model to investigate the role of O-GlcNAc in Sp1's transcriptionally relevant protein-to-protein interactions with the TATA-binding-protein-associated factor (TAF110) and holo-Sp1.
9343410	1	54	from	cytosol	193:199	arg1	modification					125:136	The O-linked N-acetylglucosamine (O-GlcNAc) modification	81:136	The O-linked N-acetylglucosamine (O-GlcNAc) modification of proteins	81:148	The O-linked N-acetylglucosamine (O-GlcNAc) modification of proteins is dynamic and abundant in the nucleus and cytosol.
9343410	1	54	from	cytosol	193:199	arg1	dynamic					153:159	dynamic	153:159	dynamic	153:159	The O-linked N-acetylglucosamine (O-GlcNAc) modification of proteins is dynamic and abundant in the nucleus and cytosol.
9343410	2	55	theme	functional	307:316	arg1	role					318:321	the functional role	303:321	the functional role of O-GlcNAc in these proteins	303:351	Several transcription factors, including Sp1, have been shown to contain this modification; however, the functional role of O-GlcNAc in these proteins has not been determined.
9343410	5	56	theme	O-GlcNAc	1028:1035	arg1	modification					1037:1048	the O-GlcNAc modification	1024:1048	the O-GlcNAc modification	1024:1048	In vitro interaction studies between this segment of Sp1 and Drosophila TAF110 or holo-Sp1 indicate that the O-GlcNAc modification functions to inhibit the largely hydrophobic interactions between these proteins.
9343410	5	57	theme	Sp1	972:974	arg1	segment					961:967	this segment	956:967	this segment of Sp1 and Drosophila TAF110 or holo-Sp1	956:1008	In vitro interaction studies between this segment of Sp1 and Drosophila TAF110 or holo-Sp1 indicate that the O-GlcNAc modification functions to inhibit the largely hydrophobic interactions between these proteins.
9343410	7	58	from	domain	1315:1320	arg1	signal					1331:1336	a signal	1329:1336	a signal for protein association	1329:1360	We propose the hypothesis that the removal of O-GlcNAc from an interaction domain can be a signal for protein association.
9343410	7	58	from	domain	1315:1320	arg1	removal					1275:1281	the removal	1271:1281	the removal of O-GlcNAc from an interaction domain	1271:1320	We propose the hypothesis that the removal of O-GlcNAc from an interaction domain can be a signal for protein association.
9343410	3	59	theme	transactivation	459:473	arg1	domain					475:480	the previously characterized glutamine-rich transactivation domain	415:480	the previously characterized glutamine-rich transactivation domain of Sp1 (B-c)	415:493	In this paper we describe the use of the previously characterized glutamine-rich transactivation domain of Sp1 (B-c) as a model to investigate the role of O-GlcNAc in Sp1's transcriptionally relevant protein-to-protein interactions with the TATA-binding-protein-associated factor (TAF110) and holo-Sp1.
9343410	3	59	theme	transactivation	459:473	arg1	Sp1					485:487	Sp1	485:487	Sp1 (B-c)	485:493	In this paper we describe the use of the previously characterized glutamine-rich transactivation domain of Sp1 (B-c) as a model to investigate the role of O-GlcNAc in Sp1's transcriptionally relevant protein-to-protein interactions with the TATA-binding-protein-associated factor (TAF110) and holo-Sp1.
9343410	3	60	from	role	525:528	arg1	interactions					597:608	Sp1's transcriptionally relevant protein-to-protein interactions	545:608	Sp1's transcriptionally relevant protein-to-protein interactions with the TATA-binding-protein-associated factor (TAF110) and holo-Sp1	545:678	In this paper we describe the use of the previously characterized glutamine-rich transactivation domain of Sp1 (B-c) as a model to investigate the role of O-GlcNAc in Sp1's transcriptionally relevant protein-to-protein interactions with the TATA-binding-protein-associated factor (TAF110) and holo-Sp1.
9343410	3	61	theme	glutamine-rich	444:457	arg1	domain					475:480	the previously characterized glutamine-rich transactivation domain	415:480	the previously characterized glutamine-rich transactivation domain of Sp1 (B-c)	415:493	In this paper we describe the use of the previously characterized glutamine-rich transactivation domain of Sp1 (B-c) as a model to investigate the role of O-GlcNAc in Sp1's transcriptionally relevant protein-to-protein interactions with the TATA-binding-protein-associated factor (TAF110) and holo-Sp1.
9343410	3	61	theme	glutamine-rich	444:457	arg1	Sp1					485:487	Sp1	485:487	Sp1 (B-c)	485:493	In this paper we describe the use of the previously characterized glutamine-rich transactivation domain of Sp1 (B-c) as a model to investigate the role of O-GlcNAc in Sp1's transcriptionally relevant protein-to-protein interactions with the TATA-binding-protein-associated factor (TAF110) and holo-Sp1.
9343410	0	62	theme	protein	59:65	arg1	interactions					67:78	known Sp1 protein interactions	49:78	known Sp1 protein interactions	49:78	O glycosylation of an Sp1-derived peptide blocks known Sp1 protein interactions.
9343410	4	63	theme	dominant	800:807	arg1	residue					818:824	a dominant O-GlcNAc residue	798:824	a dominant O-GlcNAc residue	798:824	When the model Sp1 peptide was overexpressed in primate cells, this 97-amino-acid domain of Sp1 was found to contain a dominant O-GlcNAc residue at high stoichiometry, which allowed the mapping and mutagenesis of this glycosylation site.
9343410	1	64	from	nucleus	181:187	arg1	modification					125:136	The O-linked N-acetylglucosamine (O-GlcNAc) modification	81:136	The O-linked N-acetylglucosamine (O-GlcNAc) modification of proteins	81:148	The O-linked N-acetylglucosamine (O-GlcNAc) modification of proteins is dynamic and abundant in the nucleus and cytosol.
9343410	1	64	from	nucleus	181:187	arg1	dynamic					153:159	dynamic	153:159	dynamic	153:159	The O-linked N-acetylglucosamine (O-GlcNAc) modification of proteins is dynamic and abundant in the nucleus and cytosol.
9343410	1	65	theme	proteins	141:148	arg1	modification					125:136	The O-linked N-acetylglucosamine (O-GlcNAc) modification	81:136	The O-linked N-acetylglucosamine (O-GlcNAc) modification of proteins	81:148	The O-linked N-acetylglucosamine (O-GlcNAc) modification of proteins is dynamic and abundant in the nucleus and cytosol.
9343410	1	65	theme	proteins	141:148	arg1	dynamic					153:159	dynamic	153:159	dynamic	153:159	The O-linked N-acetylglucosamine (O-GlcNAc) modification of proteins is dynamic and abundant in the nucleus and cytosol.
9343410	0	66	theme	Sp1	55:57	arg1	interactions					67:78	known Sp1 protein interactions	49:78	known Sp1 protein interactions	49:78	O glycosylation of an Sp1-derived peptide blocks known Sp1 protein interactions.
9343410	6	67	theme	HeLa	1135:1138	arg1	cells					1140:1144	HeLa cells	1135:1144	HeLa cells	1135:1144	In HeLa cells, the mutation at the mapped glycosylation site was permissive for transcriptional activation.
9343410	3	68	theme	relevant	569:576	arg1	interactions					597:608	Sp1's transcriptionally relevant protein-to-protein interactions	545:608	Sp1's transcriptionally relevant protein-to-protein interactions with the TATA-binding-protein-associated factor (TAF110) and holo-Sp1	545:678	In this paper we describe the use of the previously characterized glutamine-rich transactivation domain of Sp1 (B-c) as a model to investigate the role of O-GlcNAc in Sp1's transcriptionally relevant protein-to-protein interactions with the TATA-binding-protein-associated factor (TAF110) and holo-Sp1.
9343410	6	69	from	site	1188:1191	arg1	permissive					1197:1206	permissive	1197:1206	permissive	1197:1206	In HeLa cells, the mutation at the mapped glycosylation site was permissive for transcriptional activation.
9343410	6	69	from	site	1188:1191	arg1	mutation					1151:1158	the mutation	1147:1158	the mutation at the mapped glycosylation site	1147:1191	In HeLa cells, the mutation at the mapped glycosylation site was permissive for transcriptional activation.
20147294	0	0	theme	ADA2	77:80	arg1	activity					39:46	the growth factor activity	21:46	the growth factor activity of human adenosine deaminase ADA2	21:80	Structural basis for the growth factor activity of human adenosine deaminase ADA2.
20147294	3	1	theme	isolated	293:300	arg1	ADA2					302:305	The recently isolated ADA2	280:305	The recently isolated ADA2	280:305	The recently isolated ADA2 belongs to the novel family of adenosine deaminase growth factors (ADGFs), which play an important role in tissue development.
20147294	7	2	theme	disulfide	952:960	arg1	bond					962:965	a conserved disulfide bond	940:965	a conserved disulfide bond	940:965	An extensive glycosylation and the presence of a conserved disulfide bond and a signal peptide in ADA2 strongly suggest that ADA2, in contrast to ADA1, is specifically designed to act in the extracellular environment.
20147294	5	3	dep	novel	710:714	arg1	folds					716:720	folds	716:720	folds	716:720	In addition to the catalytic domain, the structures discovered two ADGF/ADA2-specific domains of novel folds that mediate the protein dimerization and binding to the cell surface receptors.
20147294	0	4	theme	deaminase	67:75	arg1	ADA2					77:80	human adenosine deaminase ADA2	51:80	human adenosine deaminase ADA2	51:80	Structural basis for the growth factor activity of human adenosine deaminase ADA2.
20147294	4	5	theme	ADA2	469:472	arg1	structures					446:455	The crystal structures	434:455	The crystal structures of ADA2 and ADA2 bound to a transition state analogue presented here	434:524	The crystal structures of ADA2 and ADA2 bound to a transition state analogue presented here reveal the structural basis of the catalytic/signaling activity of ADGF/ADA2 proteins.
20147294	7	6	dep	ADA1	1039:1042	arg1	contrast					1027:1034	contrast	1027:1034	contrast	1027:1034	An extensive glycosylation and the presence of a conserved disulfide bond and a signal peptide in ADA2 strongly suggest that ADA2, in contrast to ADA1, is specifically designed to act in the extracellular environment.
20147294	6	7	theme	single	873:878	arg1	ADA1					887:890	monomeric single domain ADA1	863:890	monomeric single domain ADA1	863:890	This complex architecture is in sharp contrast with that of monomeric single domain ADA1.
20147294	2	8	theme	combined	253:260	arg1	immunodeficiency					262:277	severe combined immunodeficiency	246:277	severe combined immunodeficiency	246:277	ADA1 has an important role in lymphocyte function and inherited mutations in ADA1 result in severe combined immunodeficiency.
20147294	9	9	theme	ADA2-targeting	1394:1407	arg1	drugs					1409:1413	ADA2-targeting drugs	1394:1413	ADA2-targeting drugs	1394:1413	These structural differences explain the substrate and inhibitor specificity of adenosine deaminases and provide the basis for a rational design of ADA2-targeting drugs to modulate the immune system responses in pathophysiological conditions.
20147294	6	10	theme	monomeric	863:871	arg1	ADA1					887:890	monomeric single domain ADA1	863:890	monomeric single domain ADA1	863:890	This complex architecture is in sharp contrast with that of monomeric single domain ADA1.
20147294	8	11	theme	ADA2	1148:1151	arg1	ADA1					1157:1160	ADA1	1157:1160	ADA1	1157:1160	The comparison of catalytic sites of ADA2 and ADA1 demonstrates large differences in the arrangement of the substrate-binding pockets.
20147294	8	11	theme	ADA2	1148:1151	arg1	ADA2					1148:1151	ADA2	1148:1151	ADA2	1148:1151	The comparison of catalytic sites of ADA2 and ADA1 demonstrates large differences in the arrangement of the substrate-binding pockets.
20147294	8	11	theme	ADA2	1148:1151	arg1	sites					1139:1143	catalytic sites	1129:1143	catalytic sites of ADA2 and ADA1	1129:1160	The comparison of catalytic sites of ADA2 and ADA1 demonstrates large differences in the arrangement of the substrate-binding pockets.
20147294	2	12	theme	severe	246:251	arg1	immunodeficiency					262:277	severe combined immunodeficiency	246:277	severe combined immunodeficiency	246:277	ADA1 has an important role in lymphocyte function and inherited mutations in ADA1 result in severe combined immunodeficiency.
20147294	9	13	theme	system	1438:1443	arg1	responses					1445:1453	the immune system responses	1427:1453	the immune system responses	1427:1453	These structural differences explain the substrate and inhibitor specificity of adenosine deaminases and provide the basis for a rational design of ADA2-targeting drugs to modulate the immune system responses in pathophysiological conditions.
20147294	4	14	theme	structural	537:546	arg1	basis					548:552	the structural basis	533:552	the structural basis of the catalytic/signaling activity of ADGF/ADA2 proteins	533:610	The crystal structures of ADA2 and ADA2 bound to a transition state analogue presented here reveal the structural basis of the catalytic/signaling activity of ADGF/ADA2 proteins.
20147294	5	15	theme	protein	739:745	arg1	dimerization					747:758	the protein dimerization	735:758	the protein dimerization	735:758	In addition to the catalytic domain, the structures discovered two ADGF/ADA2-specific domains of novel folds that mediate the protein dimerization and binding to the cell surface receptors.
20147294	5	16	dep	domain	642:647	arg1	addition					616:623	addition	616:623	addition	616:623	In addition to the catalytic domain, the structures discovered two ADGF/ADA2-specific domains of novel folds that mediate the protein dimerization and binding to the cell surface receptors.
20147294	9	17	theme	drugs	1409:1413	arg1	design					1384:1389	a rational design	1373:1389	a rational design of ADA2-targeting drugs to modulate the immune system responses in pathophysiological conditions	1373:1486	These structural differences explain the substrate and inhibitor specificity of adenosine deaminases and provide the basis for a rational design of ADA2-targeting drugs to modulate the immune system responses in pathophysiological conditions.
20147294	3	18	theme	novel	322:326	arg1	family					328:333	the novel family	318:333	the novel family of adenosine deaminase growth factors (ADGFs), which play an important role in tissue development	318:431	The recently isolated ADA2 belongs to the novel family of adenosine deaminase growth factors (ADGFs), which play an important role in tissue development.
20147294	1	19	located	found	137:141	arg2	deaminases					106:115	Two distinct adenosine deaminases	83:115	Two distinct adenosine deaminases	83:115	Two distinct adenosine deaminases, ADA1 and ADA2, are found in humans.
20147294	1	19	located	found	137:141	arg1	humans					146:151	humans	146:151	humans	146:151	Two distinct adenosine deaminases, ADA1 and ADA2, are found in humans.
20147294	1	19	located	found	137:141	arg2	ADA2					127:130	ADA2	127:130	ADA2	127:130	Two distinct adenosine deaminases, ADA1 and ADA2, are found in humans.
20147294	1	19	located	found	137:141	arg2	ADA1					118:121	ADA1	118:121	ADA1	118:121	Two distinct adenosine deaminases, ADA1 and ADA2, are found in humans.
20147294	7	20	theme	extracellular	1084:1096	arg1	environment					1098:1108	the extracellular environment	1080:1108	the extracellular environment	1080:1108	An extensive glycosylation and the presence of a conserved disulfide bond and a signal peptide in ADA2 strongly suggest that ADA2, in contrast to ADA1, is specifically designed to act in the extracellular environment.
20147294	4	21	theme	ADGF/ADA2	593:601	arg1	proteins					603:610	ADGF/ADA2 proteins	593:610	ADGF/ADA2 proteins	593:610	The crystal structures of ADA2 and ADA2 bound to a transition state analogue presented here reveal the structural basis of the catalytic/signaling activity of ADGF/ADA2 proteins.
20147294	0	22	theme	Structural	0:9	arg1	basis					11:15	Structural basis	0:15	Structural basis for the growth factor activity of human adenosine deaminase ADA2.	0:81	Structural basis for the growth factor activity of human adenosine deaminase ADA2.
20147294	3	23	theme	important	396:404	arg1	role					406:409	an important role	393:409	an important role	393:409	The recently isolated ADA2 belongs to the novel family of adenosine deaminase growth factors (ADGFs), which play an important role in tissue development.
20147294	3	24	theme	growth	358:363	arg1	ADGFs					374:378	ADGFs	374:378	ADGFs	374:378	The recently isolated ADA2 belongs to the novel family of adenosine deaminase growth factors (ADGFs), which play an important role in tissue development.
20147294	3	24	theme	growth	358:363	arg1	factors					365:371	adenosine deaminase growth factors	338:371	adenosine deaminase growth factors (ADGFs)	338:379	The recently isolated ADA2 belongs to the novel family of adenosine deaminase growth factors (ADGFs), which play an important role in tissue development.
20147294	4	25	theme	crystal	438:444	arg1	structures					446:455	The crystal structures	434:455	The crystal structures of ADA2 and ADA2 bound to a transition state analogue presented here	434:524	The crystal structures of ADA2 and ADA2 bound to a transition state analogue presented here reveal the structural basis of the catalytic/signaling activity of ADGF/ADA2 proteins.
20147294	6	26	with	contrast	841:848	arg1	that					855:858	that	855:858	that	855:858	This complex architecture is in sharp contrast with that of monomeric single domain ADA1.
20147294	3	27	theme	factors	365:371	arg1	family					328:333	the novel family	318:333	the novel family of adenosine deaminase growth factors (ADGFs), which play an important role in tissue development	318:431	The recently isolated ADA2 belongs to the novel family of adenosine deaminase growth factors (ADGFs), which play an important role in tissue development.
20147294	9	28	theme	inhibitor	1301:1309	arg1	specificity					1311:1321	the substrate and inhibitor specificity	1283:1321	specificity	1311:1321	These structural differences explain the substrate and inhibitor specificity of adenosine deaminases and provide the basis for a rational design of ADA2-targeting drugs to modulate the immune system responses in pathophysiological conditions.
20147294	5	29	theme	cell	779:782	arg1	receptors					792:800	the cell surface receptors	775:800	the cell surface receptors	775:800	In addition to the catalytic domain, the structures discovered two ADGF/ADA2-specific domains of novel folds that mediate the protein dimerization and binding to the cell surface receptors.
20147294	2	30	from	mutations	218:226	arg1	ADA1					231:234	ADA1	231:234	ADA1	231:234	ADA1 has an important role in lymphocyte function and inherited mutations in ADA1 result in severe combined immunodeficiency.
20147294	9	31	theme	rational	1375:1382	arg1	design					1384:1389	a rational design	1373:1389	a rational design of ADA2-targeting drugs to modulate the immune system responses in pathophysiological conditions	1373:1486	These structural differences explain the substrate and inhibitor specificity of adenosine deaminases and provide the basis for a rational design of ADA2-targeting drugs to modulate the immune system responses in pathophysiological conditions.
20147294	3	32	theme	adenosine	338:346	arg1	deaminase					348:356	adenosine deaminase	338:356	adenosine deaminase growth factors (ADGFs)	338:379	The recently isolated ADA2 belongs to the novel family of adenosine deaminase growth factors (ADGFs), which play an important role in tissue development.
20147294	4	33	theme	state	496:500	arg1	analogue					502:509	a transition state analogue	483:509	a transition state analogue presented here	483:524	The crystal structures of ADA2 and ADA2 bound to a transition state analogue presented here reveal the structural basis of the catalytic/signaling activity of ADGF/ADA2 proteins.
20147294	7	34	theme	extensive	896:904	arg1	glycosylation					906:918	An extensive glycosylation	893:918	An extensive glycosylation	893:918	An extensive glycosylation and the presence of a conserved disulfide bond and a signal peptide in ADA2 strongly suggest that ADA2, in contrast to ADA1, is specifically designed to act in the extracellular environment.
20147294	1	35	theme	distinct	87:94	arg1	ADA1					118:121	ADA1	118:121	ADA1	118:121	Two distinct adenosine deaminases, ADA1 and ADA2, are found in humans.
20147294	1	35	theme	distinct	87:94	arg1	deaminases					106:115	Two distinct adenosine deaminases	83:115	Two distinct adenosine deaminases	83:115	Two distinct adenosine deaminases, ADA1 and ADA2, are found in humans.
20147294	1	35	theme	distinct	87:94	arg1	ADA2					127:130	ADA2	127:130	ADA2	127:130	Two distinct adenosine deaminases, ADA1 and ADA2, are found in humans.
20147294	3	36	theme	tissue	414:419	arg1	development					421:431	tissue development	414:431	tissue development	414:431	The recently isolated ADA2 belongs to the novel family of adenosine deaminase growth factors (ADGFs), which play an important role in tissue development.
20147294	3	37	theme	deaminase	348:356	arg1	ADGFs					374:378	ADGFs	374:378	ADGFs	374:378	The recently isolated ADA2 belongs to the novel family of adenosine deaminase growth factors (ADGFs), which play an important role in tissue development.
20147294	3	37	theme	deaminase	348:356	arg1	factors					365:371	adenosine deaminase growth factors	338:371	adenosine deaminase growth factors (ADGFs)	338:379	The recently isolated ADA2 belongs to the novel family of adenosine deaminase growth factors (ADGFs), which play an important role in tissue development.
20147294	1	38	theme	adenosine	96:104	arg1	ADA1					118:121	ADA1	118:121	ADA1	118:121	Two distinct adenosine deaminases, ADA1 and ADA2, are found in humans.
20147294	1	38	theme	adenosine	96:104	arg1	deaminases					106:115	Two distinct adenosine deaminases	83:115	Two distinct adenosine deaminases	83:115	Two distinct adenosine deaminases, ADA1 and ADA2, are found in humans.
20147294	1	38	theme	adenosine	96:104	arg1	ADA2					127:130	ADA2	127:130	ADA2	127:130	Two distinct adenosine deaminases, ADA1 and ADA2, are found in humans.
20147294	0	39	theme	factor	32:37	arg1	activity					39:46	the growth factor activity	21:46	the growth factor activity of human adenosine deaminase ADA2	21:80	Structural basis for the growth factor activity of human adenosine deaminase ADA2.
20147294	9	40	theme	adenosine	1326:1334	arg1	deaminases					1336:1345	adenosine deaminases	1326:1345	adenosine deaminases	1326:1345	These structural differences explain the substrate and inhibitor specificity of adenosine deaminases and provide the basis for a rational design of ADA2-targeting drugs to modulate the immune system responses in pathophysiological conditions.
20147294	6	41	theme	sharp	835:839	arg1	contrast					841:848	sharp contrast	835:848	sharp contrast with that of monomeric single domain ADA1	835:890	This complex architecture is in sharp contrast with that of monomeric single domain ADA1.
20147294	9	42	theme	immune	1431:1436	arg1	responses					1445:1453	the immune system responses	1427:1453	the immune system responses	1427:1453	These structural differences explain the substrate and inhibitor specificity of adenosine deaminases and provide the basis for a rational design of ADA2-targeting drugs to modulate the immune system responses in pathophysiological conditions.
20147294	8	43	theme	pockets	1237:1243	arg1	arrangement					1200:1210	the arrangement	1196:1210	the arrangement of the substrate-binding pockets	1196:1243	The comparison of catalytic sites of ADA2 and ADA1 demonstrates large differences in the arrangement of the substrate-binding pockets.
20147294	0	44	theme	growth	25:30	arg1	activity					39:46	the growth factor activity	21:46	the growth factor activity of human adenosine deaminase ADA2	21:80	Structural basis for the growth factor activity of human adenosine deaminase ADA2.
20147294	9	45	theme	deaminases	1336:1345	arg1	specificity					1311:1321	the substrate and inhibitor specificity	1283:1321	specificity	1311:1321	These structural differences explain the substrate and inhibitor specificity of adenosine deaminases and provide the basis for a rational design of ADA2-targeting drugs to modulate the immune system responses in pathophysiological conditions.
20147294	5	46	theme	ADGF/ADA2-specific	680:697	arg1	novel					710:714	novel	710:714	novel	710:714	In addition to the catalytic domain, the structures discovered two ADGF/ADA2-specific domains of novel folds that mediate the protein dimerization and binding to the cell surface receptors.
20147294	5	46	theme	ADGF/ADA2-specific	680:697	arg1	domains					699:705	two ADGF/ADA2-specific domains	676:705	two ADGF/ADA2-specific domains of novel folds that mediate the protein dimerization and binding to the cell surface receptors	676:800	In addition to the catalytic domain, the structures discovered two ADGF/ADA2-specific domains of novel folds that mediate the protein dimerization and binding to the cell surface receptors.
20147294	9	47	theme	pathophysiological	1458:1475	arg1	conditions					1477:1486	pathophysiological conditions	1458:1486	pathophysiological conditions	1458:1486	These structural differences explain the substrate and inhibitor specificity of adenosine deaminases and provide the basis for a rational design of ADA2-targeting drugs to modulate the immune system responses in pathophysiological conditions.
20147294	5	48	theme	surface	784:790	arg1	receptors					792:800	the cell surface receptors	775:800	the cell surface receptors	775:800	In addition to the catalytic domain, the structures discovered two ADGF/ADA2-specific domains of novel folds that mediate the protein dimerization and binding to the cell surface receptors.
20147294	7	49	theme	peptide	980:986	arg1	glycosylation					906:918	An extensive glycosylation	893:918	An extensive glycosylation	893:918	An extensive glycosylation and the presence of a conserved disulfide bond and a signal peptide in ADA2 strongly suggest that ADA2, in contrast to ADA1, is specifically designed to act in the extracellular environment.
20147294	7	49	theme	peptide	980:986	arg1	presence					928:935	the presence	924:935	the presence of a conserved disulfide bond and a signal peptide in ADA2	924:994	An extensive glycosylation and the presence of a conserved disulfide bond and a signal peptide in ADA2 strongly suggest that ADA2, in contrast to ADA1, is specifically designed to act in the extracellular environment.
20147294	4	50	theme	proteins	603:610	arg1	activity					581:588	the catalytic/signaling activity	557:588	the catalytic/signaling activity of ADGF/ADA2 proteins	557:610	The crystal structures of ADA2 and ADA2 bound to a transition state analogue presented here reveal the structural basis of the catalytic/signaling activity of ADGF/ADA2 proteins.
20147294	7	51	attach	presence	928:935	arg1	ADA2					991:994	ADA2	991:994	ADA2	991:994	An extensive glycosylation and the presence of a conserved disulfide bond and a signal peptide in ADA2 strongly suggest that ADA2, in contrast to ADA1, is specifically designed to act in the extracellular environment.
20147294	7	51	attach	presence	928:935	arg2	peptide					980:986	a signal peptide	971:986	a signal peptide	971:986	An extensive glycosylation and the presence of a conserved disulfide bond and a signal peptide in ADA2 strongly suggest that ADA2, in contrast to ADA1, is specifically designed to act in the extracellular environment.
20147294	7	51	attach	presence	928:935	arg2	bond					962:965	a conserved disulfide bond	940:965	a conserved disulfide bond	940:965	An extensive glycosylation and the presence of a conserved disulfide bond and a signal peptide in ADA2 strongly suggest that ADA2, in contrast to ADA1, is specifically designed to act in the extracellular environment.
20147294	5	52	theme	catalytic	632:640	arg1	domain					642:647	the catalytic domain	628:647	the catalytic domain	628:647	In addition to the catalytic domain, the structures discovered two ADGF/ADA2-specific domains of novel folds that mediate the protein dimerization and binding to the cell surface receptors.
20147294	2	53	theme	lymphocyte	184:193	arg1	function					195:202	lymphocyte function	184:202	lymphocyte function	184:202	ADA1 has an important role in lymphocyte function and inherited mutations in ADA1 result in severe combined immunodeficiency.
20147294	9	54	theme	substrate	1287:1295	arg1	specificity					1311:1321	the substrate and inhibitor specificity	1283:1321	specificity	1311:1321	These structural differences explain the substrate and inhibitor specificity of adenosine deaminases and provide the basis for a rational design of ADA2-targeting drugs to modulate the immune system responses in pathophysiological conditions.
20147294	9	55	theme	structural	1252:1261	arg1	differences					1263:1273	These structural differences	1246:1273	These structural differences	1246:1273	These structural differences explain the substrate and inhibitor specificity of adenosine deaminases and provide the basis for a rational design of ADA2-targeting drugs to modulate the immune system responses in pathophysiological conditions.
20147294	4	56	theme	transition	485:494	arg1	analogue					502:509	a transition state analogue	483:509	a transition state analogue presented here	483:524	The crystal structures of ADA2 and ADA2 bound to a transition state analogue presented here reveal the structural basis of the catalytic/signaling activity of ADGF/ADA2 proteins.
20147294	6	57	theme	domain	880:885	arg1	ADA1					887:890	monomeric single domain ADA1	863:890	monomeric single domain ADA1	863:890	This complex architecture is in sharp contrast with that of monomeric single domain ADA1.
20147294	6	58	theme	complex	808:814	arg1	architecture					816:827	This complex architecture	803:827	This complex architecture	803:827	This complex architecture is in sharp contrast with that of monomeric single domain ADA1.
20147294	8	59	theme	ADA1	1157:1160	arg1	ADA1					1157:1160	ADA1	1157:1160	ADA1	1157:1160	The comparison of catalytic sites of ADA2 and ADA1 demonstrates large differences in the arrangement of the substrate-binding pockets.
20147294	8	59	theme	ADA1	1157:1160	arg1	ADA2					1148:1151	ADA2	1148:1151	ADA2	1148:1151	The comparison of catalytic sites of ADA2 and ADA1 demonstrates large differences in the arrangement of the substrate-binding pockets.
20147294	8	59	theme	ADA1	1157:1160	arg1	sites					1139:1143	catalytic sites	1129:1143	catalytic sites of ADA2 and ADA1	1129:1160	The comparison of catalytic sites of ADA2 and ADA1 demonstrates large differences in the arrangement of the substrate-binding pockets.
20147294	8	60	theme	sites	1139:1143	arg1	comparison					1115:1124	The comparison	1111:1124	The comparison of catalytic sites of ADA2 and ADA1	1111:1160	The comparison of catalytic sites of ADA2 and ADA1 demonstrates large differences in the arrangement of the substrate-binding pockets.
20147294	2	61	theme	important	166:174	arg1	role					176:179	an important role	163:179	an important role	163:179	ADA1 has an important role in lymphocyte function and inherited mutations in ADA1 result in severe combined immunodeficiency.
20147294	7	62	theme	signal	973:978	arg1	peptide					980:986	a signal peptide	971:986	a signal peptide	971:986	An extensive glycosylation and the presence of a conserved disulfide bond and a signal peptide in ADA2 strongly suggest that ADA2, in contrast to ADA1, is specifically designed to act in the extracellular environment.
20147294	7	63	from	glycosylation	906:918	arg1	ADA2					991:994	ADA2	991:994	ADA2	991:994	An extensive glycosylation and the presence of a conserved disulfide bond and a signal peptide in ADA2 strongly suggest that ADA2, in contrast to ADA1, is specifically designed to act in the extracellular environment.
20147294	5	64	theme	novel	710:714	arg1	novel					710:714	novel	710:714	novel	710:714	In addition to the catalytic domain, the structures discovered two ADGF/ADA2-specific domains of novel folds that mediate the protein dimerization and binding to the cell surface receptors.
20147294	5	64	theme	novel	710:714	arg1	domains					699:705	two ADGF/ADA2-specific domains	676:705	two ADGF/ADA2-specific domains of novel folds that mediate the protein dimerization and binding to the cell surface receptors	676:800	In addition to the catalytic domain, the structures discovered two ADGF/ADA2-specific domains of novel folds that mediate the protein dimerization and binding to the cell surface receptors.
20147294	8	65	from	differences	1181:1191	arg1	arrangement					1200:1210	the arrangement	1196:1210	the arrangement of the substrate-binding pockets	1196:1243	The comparison of catalytic sites of ADA2 and ADA1 demonstrates large differences in the arrangement of the substrate-binding pockets.
20147294	8	66	theme	catalytic	1129:1137	arg1	ADA1					1157:1160	ADA1	1157:1160	ADA1	1157:1160	The comparison of catalytic sites of ADA2 and ADA1 demonstrates large differences in the arrangement of the substrate-binding pockets.
20147294	8	66	theme	catalytic	1129:1137	arg1	ADA2					1148:1151	ADA2	1148:1151	ADA2	1148:1151	The comparison of catalytic sites of ADA2 and ADA1 demonstrates large differences in the arrangement of the substrate-binding pockets.
20147294	8	66	theme	catalytic	1129:1137	arg1	sites					1139:1143	catalytic sites	1129:1143	catalytic sites of ADA2 and ADA1	1129:1160	The comparison of catalytic sites of ADA2 and ADA1 demonstrates large differences in the arrangement of the substrate-binding pockets.
20147294	7	67	theme	bond	962:965	arg1	glycosylation					906:918	An extensive glycosylation	893:918	An extensive glycosylation	893:918	An extensive glycosylation and the presence of a conserved disulfide bond and a signal peptide in ADA2 strongly suggest that ADA2, in contrast to ADA1, is specifically designed to act in the extracellular environment.
20147294	7	67	theme	bond	962:965	arg1	presence					928:935	the presence	924:935	the presence of a conserved disulfide bond and a signal peptide in ADA2	924:994	An extensive glycosylation and the presence of a conserved disulfide bond and a signal peptide in ADA2 strongly suggest that ADA2, in contrast to ADA1, is specifically designed to act in the extracellular environment.
20147294	8	68	theme	large	1175:1179	arg1	differences					1181:1191	large differences	1175:1191	large differences in the arrangement of the substrate-binding pockets	1175:1243	The comparison of catalytic sites of ADA2 and ADA1 demonstrates large differences in the arrangement of the substrate-binding pockets.
20147294	7	69	gly	glycosylation	906:918	arg1	bond					962:965	a conserved disulfide bond	940:965	a conserved disulfide bond	940:965	An extensive glycosylation and the presence of a conserved disulfide bond and a signal peptide in ADA2 strongly suggest that ADA2, in contrast to ADA1, is specifically designed to act in the extracellular environment.
20147294	7	69	gly	glycosylation	906:918	arg1	ADA2					991:994	ADA2	991:994	ADA2	991:994	An extensive glycosylation and the presence of a conserved disulfide bond and a signal peptide in ADA2 strongly suggest that ADA2, in contrast to ADA1, is specifically designed to act in the extracellular environment.
20147294	7	69	gly	glycosylation	906:918	arg1	peptide					980:986	a signal peptide	971:986	a signal peptide	971:986	An extensive glycosylation and the presence of a conserved disulfide bond and a signal peptide in ADA2 strongly suggest that ADA2, in contrast to ADA1, is specifically designed to act in the extracellular environment.
20147294	0	70	theme	adenosine	57:65	arg1	deaminase					67:75	human adenosine deaminase	51:75	human adenosine deaminase ADA2	51:80	Structural basis for the growth factor activity of human adenosine deaminase ADA2.
20147294	8	71	theme	substrate-binding	1219:1235	arg1	pockets					1237:1243	the substrate-binding pockets	1215:1243	the substrate-binding pockets	1215:1243	The comparison of catalytic sites of ADA2 and ADA1 demonstrates large differences in the arrangement of the substrate-binding pockets.
20147294	2	72	contain	has	159:161	arg2	role					176:179	an important role	163:179	an important role	163:179	ADA1 has an important role in lymphocyte function and inherited mutations in ADA1 result in severe combined immunodeficiency.
20147294	2	72	contain	has	159:161	arg1	ADA1					154:157	ADA1	154:157	ADA1	154:157	ADA1 has an important role in lymphocyte function and inherited mutations in ADA1 result in severe combined immunodeficiency.
20147294	4	73	theme	activity	581:588	arg1	basis					548:552	the structural basis	533:552	the structural basis of the catalytic/signaling activity of ADGF/ADA2 proteins	533:610	The crystal structures of ADA2 and ADA2 bound to a transition state analogue presented here reveal the structural basis of the catalytic/signaling activity of ADGF/ADA2 proteins.
20147294	0	74	theme	human	51:55	arg1	deaminase					67:75	human adenosine deaminase	51:75	human adenosine deaminase ADA2	51:80	Structural basis for the growth factor activity of human adenosine deaminase ADA2.
20147294	4	75	theme	ADA2	460:463	arg1	structures					446:455	The crystal structures	434:455	The crystal structures of ADA2 and ADA2 bound to a transition state analogue presented here	434:524	The crystal structures of ADA2 and ADA2 bound to a transition state analogue presented here reveal the structural basis of the catalytic/signaling activity of ADGF/ADA2 proteins.
20147294	2	76	theme	inherited	208:216	arg1	mutations					218:226	inherited mutations	208:226	inherited mutations in ADA1	208:234	ADA1 has an important role in lymphocyte function and inherited mutations in ADA1 result in severe combined immunodeficiency.
20147294	7	77	theme	conserved	942:950	arg1	bond					962:965	a conserved disulfide bond	940:965	a conserved disulfide bond	940:965	An extensive glycosylation and the presence of a conserved disulfide bond and a signal peptide in ADA2 strongly suggest that ADA2, in contrast to ADA1, is specifically designed to act in the extracellular environment.
20147294	7	78	from	presence	928:935	arg1	ADA2					991:994	ADA2	991:994	ADA2	991:994	An extensive glycosylation and the presence of a conserved disulfide bond and a signal peptide in ADA2 strongly suggest that ADA2, in contrast to ADA1, is specifically designed to act in the extracellular environment.
20147294	4	79	theme	catalytic/signaling	561:579	arg1	activity					581:588	the catalytic/signaling activity	557:588	the catalytic/signaling activity of ADGF/ADA2 proteins	557:610	The crystal structures of ADA2 and ADA2 bound to a transition state analogue presented here reveal the structural basis of the catalytic/signaling activity of ADGF/ADA2 proteins.
8885240	8	0	theme	precursor	1850:1858	arg1	cleavage					1819:1826	cleavage	1819:1826	cleavage of the 110K activin A precursor to the 24K form	1819:1874	In contrast, cleavage of the 110K activin A precursor to the 24K form would appear to be necessary for activity.
8885240	6	1	theme	inhibin	1419:1425	arg1	A					1427:1427	55K and 65K inhibin A	1407:1427	A	1427:1427	Since radioactively labeled 55K and 65K inhibin A and 110K activin A remained intact after incubation with rat pituitary cells for 72 h, there appears to be no conversion of these dimers to lower molecular weight forms by proteolytic cleavage at additional sites.
8885240	1	2	gly	glycosylation	543:555	arg1	sites					516:520	the proteolytic processing sites	489:520	the proteolytic processing sites	489:520	The present study verifies that the wide variation in the size of these products is due to incomplete cleavage of the proteolytic processing sites and the differential glycosylation of the N-linked glycosylation site at amino acid number 302 in the alpha C-subunit.
8885240	1	2	gly	glycosylation	543:555	arg1	site					587:590	the N-linked glycosylation site	560:590	the N-linked glycosylation site at amino acid number 302 in the alpha C-subunit	560:638	The present study verifies that the wide variation in the size of these products is due to incomplete cleavage of the proteolytic processing sites and the differential glycosylation of the N-linked glycosylation site at amino acid number 302 in the alpha C-subunit.
8885240	3	3	theme	microgram	1025:1033	arg1	quantities					1035:1044	microgram quantities	1025:1044	microgram quantities of noncleavable 55K and 65K inhibin dimers, and noncleavable 110K activin A dimers	1025:1127	Transient expression of processing site mutants of the alpha- and beta A-subunits in 293 cells was used to generate microgram quantities of noncleavable 55K and 65K inhibin dimers, and noncleavable 110K activin A dimers.
8885240	2	4	theme	products	820:827	arg1	analysis					795:802	the analysis	791:802	the analysis of transfection products	791:827	The identity of each of these products was established by mutagenesis of proteolytic processing sites and N-linked glycosylation sites, combined with the analysis of transfection products by immunoprecipitation and one- and two-dimensional SDS-PAGE (SDS/SDS-beta-ME).
8885240	0	5	theme	A-inhibin	184:192	arg1	subunit					194:200	beta A-inhibin subunit	179:200	beta A-inhibin subunit	179:200	Characterization and determination of the biological activities of noncleavable high molecular weight forms of inhibin A and activin A. Recombinant expression of human alpha- and beta A-inhibin subunit cDNAs in mammalian 293 cells results in the secretion of 20-53K free alpha-subunit-derived products, 30-105K alpha beta A-inhibin dimers, and 24-110K beta A-activin dimers.
8885240	3	6	used	used	1008:1011	arg2	expression					919:928	Transient expression	909:928	Transient expression of processing site mutants of the alpha- and beta A-subunits in 293 cells	909:1002	Transient expression of processing site mutants of the alpha- and beta A-subunits in 293 cells was used to generate microgram quantities of noncleavable 55K and 65K inhibin dimers, and noncleavable 110K activin A dimers.
8885240	0	7	theme	cDNAs	202:206	arg1	expression					148:157	Recombinant expression	136:157	Recombinant expression of human alpha- and beta A-inhibin subunit cDNAs in mammalian 293 cells	136:229	Characterization and determination of the biological activities of noncleavable high molecular weight forms of inhibin A and activin A. Recombinant expression of human alpha- and beta A-inhibin subunit cDNAs in mammalian 293 cells results in the secretion of 20-53K free alpha-subunit-derived products, 30-105K alpha beta A-inhibin dimers, and 24-110K beta A-activin dimers.
8885240	1	8	theme	products	447:454	arg1	size					433:436	the size	429:436	the size of these products	429:454	The present study verifies that the wide variation in the size of these products is due to incomplete cleavage of the proteolytic processing sites and the differential glycosylation of the N-linked glycosylation site at amino acid number 302 in the alpha C-subunit.
8885240	0	9	theme	beta	352:355	arg1	dimers					367:372	24-110K beta A-activin dimers	344:372	24-110K beta A-activin dimers	344:372	Characterization and determination of the biological activities of noncleavable high molecular weight forms of inhibin A and activin A. Recombinant expression of human alpha- and beta A-inhibin subunit cDNAs in mammalian 293 cells results in the secretion of 20-53K free alpha-subunit-derived products, 30-105K alpha beta A-inhibin dimers, and 24-110K beta A-activin dimers.
8885240	1	10	gly	glycosylation	573:585	arg2	site					587:590	the N-linked glycosylation site	560:590	the N-linked glycosylation site at amino acid number 302 in the alpha C-subunit	560:638	The present study verifies that the wide variation in the size of these products is due to incomplete cleavage of the proteolytic processing sites and the differential glycosylation of the N-linked glycosylation site at amino acid number 302 in the alpha C-subunit.
8885240	1	10	gly	glycosylation	573:585	arg2	number					606:611	amino acid number 302	595:615	amino acid number 302 in the alpha C-subunit	595:638	The present study verifies that the wide variation in the size of these products is due to incomplete cleavage of the proteolytic processing sites and the differential glycosylation of the N-linked glycosylation site at amino acid number 302 in the alpha C-subunit.
8885240	2	11	theme	sites	737:741	arg1	mutagenesis					699:709	mutagenesis	699:709	mutagenesis	699:709	The identity of each of these products was established by mutagenesis of proteolytic processing sites and N-linked glycosylation sites, combined with the analysis of transfection products by immunoprecipitation and one- and two-dimensional SDS-PAGE (SDS/SDS-beta-ME).
8885240	0	12	theme	mammalian	211:219	arg1	cells					225:229	mammalian 293 cells	211:229	mammalian 293 cells	211:229	Characterization and determination of the biological activities of noncleavable high molecular weight forms of inhibin A and activin A. Recombinant expression of human alpha- and beta A-inhibin subunit cDNAs in mammalian 293 cells results in the secretion of 20-53K free alpha-subunit-derived products, 30-105K alpha beta A-inhibin dimers, and 24-110K beta A-activin dimers.
8885240	0	13	theme	dimers	367:372	arg1	secretion					246:254	the secretion	242:254	the secretion of 20-53K free alpha-subunit-derived products, 30-105K alpha beta A-inhibin dimers, and 24-110K beta A-activin dimers	242:372	Characterization and determination of the biological activities of noncleavable high molecular weight forms of inhibin A and activin A. Recombinant expression of human alpha- and beta A-inhibin subunit cDNAs in mammalian 293 cells results in the secretion of 20-53K free alpha-subunit-derived products, 30-105K alpha beta A-inhibin dimers, and 24-110K beta A-activin dimers.
8885240	5	14	theme	molecular	1266:1274	arg1	HMW					1284:1286	HMW	1284:1286	HMW	1284:1286	The 110K high molecular weight (HMW) form of human activin A failed to show any FSH-releasing activity in the pituitary assay.
8885240	5	14	theme	molecular	1266:1274	arg1	weight					1276:1281	110K high molecular weight	1256:1281	The 110K high molecular weight (HMW) form of human activin A	1252:1311	The 110K high molecular weight (HMW) form of human activin A failed to show any FSH-releasing activity in the pituitary assay.
8885240	1	15	theme	present	379:385	arg1	study					387:391	The present study	375:391	The present study	375:391	The present study verifies that the wide variation in the size of these products is due to incomplete cleavage of the proteolytic processing sites and the differential glycosylation of the N-linked glycosylation site at amino acid number 302 in the alpha C-subunit.
8885240	2	16	theme	sites	770:774	arg1	mutagenesis					699:709	mutagenesis	699:709	mutagenesis	699:709	The identity of each of these products was established by mutagenesis of proteolytic processing sites and N-linked glycosylation sites, combined with the analysis of transfection products by immunoprecipitation and one- and two-dimensional SDS-PAGE (SDS/SDS-beta-ME).
8885240	0	17	theme	products	293:300	arg1	secretion					246:254	the secretion	242:254	the secretion of 20-53K free alpha-subunit-derived products, 30-105K alpha beta A-inhibin dimers, and 24-110K beta A-activin dimers	242:372	Characterization and determination of the biological activities of noncleavable high molecular weight forms of inhibin A and activin A. Recombinant expression of human alpha- and beta A-inhibin subunit cDNAs in mammalian 293 cells results in the secretion of 20-53K free alpha-subunit-derived products, 30-105K alpha beta A-inhibin dimers, and 24-110K beta A-activin dimers.
8885240	8	18	theme	activin	1840:1846	arg1	precursor					1850:1858	the 110K activin A precursor	1831:1858	the 110K activin A precursor	1831:1858	In contrast, cleavage of the 110K activin A precursor to the 24K form would appear to be necessary for activity.
8885240	6	19	theme	proteolytic	1601:1611	arg1	cleavage					1613:1620	proteolytic cleavage	1601:1620	proteolytic cleavage at additional sites	1601:1640	Since radioactively labeled 55K and 65K inhibin A and 110K activin A remained intact after incubation with rat pituitary cells for 72 h, there appears to be no conversion of these dimers to lower molecular weight forms by proteolytic cleavage at additional sites.
8885240	1	20	from	glycosylation	543:555	arg1	number					606:611	amino acid number 302	595:615	amino acid number 302 in the alpha C-subunit	595:638	The present study verifies that the wide variation in the size of these products is due to incomplete cleavage of the proteolytic processing sites and the differential glycosylation of the N-linked glycosylation site at amino acid number 302 in the alpha C-subunit.
8885240	1	21	theme	amino	595:599	arg1	number					606:611	amino acid number 302	595:615	amino acid number 302 in the alpha C-subunit	595:638	The present study verifies that the wide variation in the size of these products is due to incomplete cleavage of the proteolytic processing sites and the differential glycosylation of the N-linked glycosylation site at amino acid number 302 in the alpha C-subunit.
8885240	0	22	theme	human	162:166	arg1	alpha-					168:173	human alpha-	162:173	human alpha-	162:173	Characterization and determination of the biological activities of noncleavable high molecular weight forms of inhibin A and activin A. Recombinant expression of human alpha- and beta A-inhibin subunit cDNAs in mammalian 293 cells results in the secretion of 20-53K free alpha-subunit-derived products, 30-105K alpha beta A-inhibin dimers, and 24-110K beta A-activin dimers.
8885240	0	23	theme	beta	317:320	arg1	dimers					332:337	30-105K alpha beta A-inhibin dimers	303:337	30-105K alpha beta A-inhibin dimers	303:337	Characterization and determination of the biological activities of noncleavable high molecular weight forms of inhibin A and activin A. Recombinant expression of human alpha- and beta A-inhibin subunit cDNAs in mammalian 293 cells results in the secretion of 20-53K free alpha-subunit-derived products, 30-105K alpha beta A-inhibin dimers, and 24-110K beta A-activin dimers.
8885240	0	24	dep	expression	148:157	arg1	A.					133:134	A.	133:134	A.	133:134	Characterization and determination of the biological activities of noncleavable high molecular weight forms of inhibin A and activin A. Recombinant expression of human alpha- and beta A-inhibin subunit cDNAs in mammalian 293 cells results in the secretion of 20-53K free alpha-subunit-derived products, 30-105K alpha beta A-inhibin dimers, and 24-110K beta A-activin dimers.
8885240	7	25	dep	inhibit	1698:1704	arg1	active					1739:1744	active	1739:1744	active	1739:1744	These results show for the first time that 55K and 65K inhibit A are intrinsically biologically active and do not require cleavage to the 32K form for activation.
8885240	7	25	dep	inhibit	1698:1704	arg1	A					1706:1706	A	1706:1706	A	1706:1706	These results show for the first time that 55K and 65K inhibit A are intrinsically biologically active and do not require cleavage to the 32K form for activation.
8885240	2	26	theme	proteolytic	714:724	arg1	sites					737:741	proteolytic processing sites	714:741	proteolytic processing sites	714:741	The identity of each of these products was established by mutagenesis of proteolytic processing sites and N-linked glycosylation sites, combined with the analysis of transfection products by immunoprecipitation and one- and two-dimensional SDS-PAGE (SDS/SDS-beta-ME).
8885240	5	27	theme	weight	1276:1281	arg1	form					1289:1292	The 110K high molecular weight (HMW) form	1252:1292	The 110K high molecular weight (HMW) form of human activin A	1252:1311	The 110K high molecular weight (HMW) form of human activin A failed to show any FSH-releasing activity in the pituitary assay.
8885240	0	28	theme	noncleavable	67:78	arg1	forms					102:106	noncleavable high molecular weight forms	67:106	noncleavable high molecular weight forms of inhibin A and activin	67:131	Characterization and determination of the biological activities of noncleavable high molecular weight forms of inhibin A and activin A. Recombinant expression of human alpha- and beta A-inhibin subunit cDNAs in mammalian 293 cells results in the secretion of 20-53K free alpha-subunit-derived products, 30-105K alpha beta A-inhibin dimers, and 24-110K beta A-activin dimers.
8885240	0	29	theme	dimers	332:337	arg1	secretion					246:254	the secretion	242:254	the secretion of 20-53K free alpha-subunit-derived products, 30-105K alpha beta A-inhibin dimers, and 24-110K beta A-activin dimers	242:372	Characterization and determination of the biological activities of noncleavable high molecular weight forms of inhibin A and activin A. Recombinant expression of human alpha- and beta A-inhibin subunit cDNAs in mammalian 293 cells results in the secretion of 20-53K free alpha-subunit-derived products, 30-105K alpha beta A-inhibin dimers, and 24-110K beta A-activin dimers.
8885240	6	30	with	incubation	1470:1479	arg1	cells					1500:1504	rat pituitary cells	1486:1504	rat pituitary cells	1486:1504	Since radioactively labeled 55K and 65K inhibin A and 110K activin A remained intact after incubation with rat pituitary cells for 72 h, there appears to be no conversion of these dimers to lower molecular weight forms by proteolytic cleavage at additional sites.
8885240	0	31	theme	molecular	85:93	arg1	forms					102:106	noncleavable high molecular weight forms	67:106	noncleavable high molecular weight forms of inhibin A and activin	67:131	Characterization and determination of the biological activities of noncleavable high molecular weight forms of inhibin A and activin A. Recombinant expression of human alpha- and beta A-inhibin subunit cDNAs in mammalian 293 cells results in the secretion of 20-53K free alpha-subunit-derived products, 30-105K alpha beta A-inhibin dimers, and 24-110K beta A-activin dimers.
8885240	3	32	theme	dimers	1082:1087	arg1	quantities					1035:1044	microgram quantities	1025:1044	microgram quantities of noncleavable 55K and 65K inhibin dimers, and noncleavable 110K activin A dimers	1025:1127	Transient expression of processing site mutants of the alpha- and beta A-subunits in 293 cells was used to generate microgram quantities of noncleavable 55K and 65K inhibin dimers, and noncleavable 110K activin A dimers.
8885240	4	33	theme	A	1154:1154	arg1	forms					1156:1160	The 55K and 65K inhibin A forms	1130:1160	The 55K and 65K inhibin A forms	1130:1160	The 55K and 65K inhibin A forms were purified and found to be fully biologically active in a rat pituitary cell bioassay.
8885240	4	33	theme	A	1154:1154	arg1	active					1211:1216	active	1211:1216	active	1211:1216	The 55K and 65K inhibin A forms were purified and found to be fully biologically active in a rat pituitary cell bioassay.
8885240	1	34	theme	alpha	624:628	arg1	C-subunit					630:638	the alpha C-subunit	620:638	the alpha C-subunit	620:638	The present study verifies that the wide variation in the size of these products is due to incomplete cleavage of the proteolytic processing sites and the differential glycosylation of the N-linked glycosylation site at amino acid number 302 in the alpha C-subunit.
8885240	0	35	theme	forms	102:106	arg1	activities					53:62	the biological activities	38:62	the biological activities of noncleavable high molecular weight forms of inhibin A and activin A. Recombinant expression of human alpha- and beta A-inhibin subunit cDNAs in mammalian 293 cells	38:229	Characterization and determination of the biological activities of noncleavable high molecular weight forms of inhibin A and activin A. Recombinant expression of human alpha- and beta A-inhibin subunit cDNAs in mammalian 293 cells results in the secretion of 20-53K free alpha-subunit-derived products, 30-105K alpha beta A-inhibin dimers, and 24-110K beta A-activin dimers.
8885240	6	36	theme	pituitary	1490:1498	arg1	cells					1500:1504	rat pituitary cells	1486:1504	rat pituitary cells	1486:1504	Since radioactively labeled 55K and 65K inhibin A and 110K activin A remained intact after incubation with rat pituitary cells for 72 h, there appears to be no conversion of these dimers to lower molecular weight forms by proteolytic cleavage at additional sites.
8885240	6	37	theme	lower	1569:1573	arg1	forms					1592:1596	lower molecular weight forms	1569:1596	lower molecular weight forms	1569:1596	Since radioactively labeled 55K and 65K inhibin A and 110K activin A remained intact after incubation with rat pituitary cells for 72 h, there appears to be no conversion of these dimers to lower molecular weight forms by proteolytic cleavage at additional sites.
8885240	4	38	theme	55K	1134:1136	arg1	A					1154:1154	55K and 65K inhibin A	1134:1154	A	1154:1154	The 55K and 65K inhibin A forms were purified and found to be fully biologically active in a rat pituitary cell bioassay.
8885240	4	39	theme	rat	1223:1225	arg1	bioassay					1242:1249	a rat pituitary cell bioassay	1221:1249	a rat pituitary cell bioassay	1221:1249	The 55K and 65K inhibin A forms were purified and found to be fully biologically active in a rat pituitary cell bioassay.
8885240	1	40	theme	differential	530:541	arg1	glycosylation					543:555	the differential glycosylation	526:555	the differential glycosylation of the N-linked glycosylation site at amino acid number 302 in the alpha C-subunit	526:638	The present study verifies that the wide variation in the size of these products is due to incomplete cleavage of the proteolytic processing sites and the differential glycosylation of the N-linked glycosylation site at amino acid number 302 in the alpha C-subunit.
8885240	0	41	theme	inhibin	111:117	arg1	A					119:119	inhibin A	111:119	inhibin A	111:119	Characterization and determination of the biological activities of noncleavable high molecular weight forms of inhibin A and activin A. Recombinant expression of human alpha- and beta A-inhibin subunit cDNAs in mammalian 293 cells results in the secretion of 20-53K free alpha-subunit-derived products, 30-105K alpha beta A-inhibin dimers, and 24-110K beta A-activin dimers.
8885240	3	42	theme	110K	1107:1110	arg1	A					1120:1120	noncleavable 110K activin A	1094:1120	noncleavable 110K activin A dimers	1094:1127	Transient expression of processing site mutants of the alpha- and beta A-subunits in 293 cells was used to generate microgram quantities of noncleavable 55K and 65K inhibin dimers, and noncleavable 110K activin A dimers.
8885240	6	43	theme	dimers	1559:1564	arg1	conversion					1539:1548	no conversion	1536:1548	no conversion of these dimers to lower molecular weight forms	1536:1596	Since radioactively labeled 55K and 65K inhibin A and 110K activin A remained intact after incubation with rat pituitary cells for 72 h, there appears to be no conversion of these dimers to lower molecular weight forms by proteolytic cleavage at additional sites.
8885240	3	44	theme	Transient	909:917	arg1	expression					919:928	Transient expression	909:928	Transient expression of processing site mutants of the alpha- and beta A-subunits in 293 cells	909:1002	Transient expression of processing site mutants of the alpha- and beta A-subunits in 293 cells was used to generate microgram quantities of noncleavable 55K and 65K inhibin dimers, and noncleavable 110K activin A dimers.
8885240	0	45	theme	high	80:83	arg1	forms					102:106	noncleavable high molecular weight forms	67:106	noncleavable high molecular weight forms of inhibin A and activin	67:131	Characterization and determination of the biological activities of noncleavable high molecular weight forms of inhibin A and activin A. Recombinant expression of human alpha- and beta A-inhibin subunit cDNAs in mammalian 293 cells results in the secretion of 20-53K free alpha-subunit-derived products, 30-105K alpha beta A-inhibin dimers, and 24-110K beta A-activin dimers.
8885240	5	46	theme	A	1311:1311	arg1	form					1289:1292	The 110K high molecular weight (HMW) form	1252:1292	The 110K high molecular weight (HMW) form of human activin A	1252:1311	The 110K high molecular weight (HMW) form of human activin A failed to show any FSH-releasing activity in the pituitary assay.
8885240	6	47	theme	55K	1407:1409	arg1	A					1427:1427	55K and 65K inhibin A	1407:1427	A	1427:1427	Since radioactively labeled 55K and 65K inhibin A and 110K activin A remained intact after incubation with rat pituitary cells for 72 h, there appears to be no conversion of these dimers to lower molecular weight forms by proteolytic cleavage at additional sites.
8885240	0	48	theme	free	266:269	arg1	products					293:300	20-53K free alpha-subunit-derived products	259:300	20-53K free alpha-subunit-derived products	259:300	Characterization and determination of the biological activities of noncleavable high molecular weight forms of inhibin A and activin A. Recombinant expression of human alpha- and beta A-inhibin subunit cDNAs in mammalian 293 cells results in the secretion of 20-53K free alpha-subunit-derived products, 30-105K alpha beta A-inhibin dimers, and 24-110K beta A-activin dimers.
8885240	1	49	theme	N-linked	564:571	arg1	site					587:590	the N-linked glycosylation site	560:590	the N-linked glycosylation site at amino acid number 302 in the alpha C-subunit	560:638	The present study verifies that the wide variation in the size of these products is due to incomplete cleavage of the proteolytic processing sites and the differential glycosylation of the N-linked glycosylation site at amino acid number 302 in the alpha C-subunit.
8885240	4	50	theme	inhibin	1146:1152	arg1	A					1154:1154	55K and 65K inhibin A	1134:1154	A	1154:1154	The 55K and 65K inhibin A forms were purified and found to be fully biologically active in a rat pituitary cell bioassay.
8885240	3	51	theme	site	944:947	arg1	mutants					949:955	processing site mutants	933:955	processing site mutants of the alpha- and beta A-subunits in 293 cells	933:1002	Transient expression of processing site mutants of the alpha- and beta A-subunits in 293 cells was used to generate microgram quantities of noncleavable 55K and 65K inhibin dimers, and noncleavable 110K activin A dimers.
8885240	2	52	theme	N-linked	747:754	arg1	sites					770:774	N-linked glycosylation sites	747:774	N-linked glycosylation sites	747:774	The identity of each of these products was established by mutagenesis of proteolytic processing sites and N-linked glycosylation sites, combined with the analysis of transfection products by immunoprecipitation and one- and two-dimensional SDS-PAGE (SDS/SDS-beta-ME).
8885240	1	53	theme	site	587:590	arg1	glycosylation					543:555	the differential glycosylation	526:555	the differential glycosylation of the N-linked glycosylation site at amino acid number 302 in the alpha C-subunit	526:638	The present study verifies that the wide variation in the size of these products is due to incomplete cleavage of the proteolytic processing sites and the differential glycosylation of the N-linked glycosylation site at amino acid number 302 in the alpha C-subunit.
8885240	1	53	theme	site	587:590	arg1	cleavage					477:484	incomplete cleavage	466:484	incomplete cleavage of the proteolytic processing sites	466:520	The present study verifies that the wide variation in the size of these products is due to incomplete cleavage of the proteolytic processing sites and the differential glycosylation of the N-linked glycosylation site at amino acid number 302 in the alpha C-subunit.
8885240	3	54	theme	A	1120:1120	arg1	dimers					1122:1127	noncleavable 110K activin A dimers	1094:1127	noncleavable 110K activin A dimers	1094:1127	Transient expression of processing site mutants of the alpha- and beta A-subunits in 293 cells was used to generate microgram quantities of noncleavable 55K and 65K inhibin dimers, and noncleavable 110K activin A dimers.
8885240	3	55	theme	beta	975:978	arg1	A-subunits					980:989	the alpha- and beta A-subunits	960:989	the alpha- and beta A-subunits in 293 cells	960:1002	Transient expression of processing site mutants of the alpha- and beta A-subunits in 293 cells was used to generate microgram quantities of noncleavable 55K and 65K inhibin dimers, and noncleavable 110K activin A dimers.
8885240	1	56	from	cleavage	477:484	arg1	number					606:611	amino acid number 302	595:615	amino acid number 302 in the alpha C-subunit	595:638	The present study verifies that the wide variation in the size of these products is due to incomplete cleavage of the proteolytic processing sites and the differential glycosylation of the N-linked glycosylation site at amino acid number 302 in the alpha C-subunit.
8885240	0	57	theme	activities	53:62	arg1	determination					21:33	determination	21:33	determination	21:33	Characterization and determination of the biological activities of noncleavable high molecular weight forms of inhibin A and activin A. Recombinant expression of human alpha- and beta A-inhibin subunit cDNAs in mammalian 293 cells results in the secretion of 20-53K free alpha-subunit-derived products, 30-105K alpha beta A-inhibin dimers, and 24-110K beta A-activin dimers.
8885240	0	57	theme	activities	53:62	arg1	Characterization					0:15	Characterization	0:15	Characterization	0:15	Characterization and determination of the biological activities of noncleavable high molecular weight forms of inhibin A and activin A. Recombinant expression of human alpha- and beta A-inhibin subunit cDNAs in mammalian 293 cells results in the secretion of 20-53K free alpha-subunit-derived products, 30-105K alpha beta A-inhibin dimers, and 24-110K beta A-activin dimers.
8885240	3	58	theme	alpha-	964:969	arg1	A-subunits					980:989	the alpha- and beta A-subunits	960:989	the alpha- and beta A-subunits in 293 cells	960:1002	Transient expression of processing site mutants of the alpha- and beta A-subunits in 293 cells was used to generate microgram quantities of noncleavable 55K and 65K inhibin dimers, and noncleavable 110K activin A dimers.
8885240	2	59	theme	transfection	807:818	arg1	products					820:827	transfection products	807:827	transfection products	807:827	The identity of each of these products was established by mutagenesis of proteolytic processing sites and N-linked glycosylation sites, combined with the analysis of transfection products by immunoprecipitation and one- and two-dimensional SDS-PAGE (SDS/SDS-beta-ME).
8885240	4	60	from	bioassay	1242:1249	arg1	forms					1156:1160	The 55K and 65K inhibin A forms	1130:1160	The 55K and 65K inhibin A forms	1130:1160	The 55K and 65K inhibin A forms were purified and found to be fully biologically active in a rat pituitary cell bioassay.
8885240	4	60	from	bioassay	1242:1249	arg1	active					1211:1216	active	1211:1216	active	1211:1216	The 55K and 65K inhibin A forms were purified and found to be fully biologically active in a rat pituitary cell bioassay.
8885240	4	61	theme	cell	1237:1240	arg1	bioassay					1242:1249	a rat pituitary cell bioassay	1221:1249	a rat pituitary cell bioassay	1221:1249	The 55K and 65K inhibin A forms were purified and found to be fully biologically active in a rat pituitary cell bioassay.
8885240	5	62	theme	FSH-releasing	1332:1344	arg1	activity					1346:1353	any FSH-releasing activity	1328:1353	any FSH-releasing activity	1328:1353	The 110K high molecular weight (HMW) form of human activin A failed to show any FSH-releasing activity in the pituitary assay.
8885240	2	63	theme	two-dimensional	865:879	arg1	SDS/SDS-beta-ME					891:905	SDS/SDS-beta-ME	891:905	SDS/SDS-beta-ME	891:905	The identity of each of these products was established by mutagenesis of proteolytic processing sites and N-linked glycosylation sites, combined with the analysis of transfection products by immunoprecipitation and one- and two-dimensional SDS-PAGE (SDS/SDS-beta-ME).
8885240	2	63	theme	two-dimensional	865:879	arg1	SDS-PAGE					881:888	one- and two-dimensional SDS-PAGE	856:888	one- and two-dimensional SDS-PAGE (SDS/SDS-beta-ME)	856:906	The identity of each of these products was established by mutagenesis of proteolytic processing sites and N-linked glycosylation sites, combined with the analysis of transfection products by immunoprecipitation and one- and two-dimensional SDS-PAGE (SDS/SDS-beta-ME).
8885240	3	64	from	A-subunits	980:989	arg1	cells					998:1002	293 cells	994:1002	293 cells	994:1002	Transient expression of processing site mutants of the alpha- and beta A-subunits in 293 cells was used to generate microgram quantities of noncleavable 55K and 65K inhibin dimers, and noncleavable 110K activin A dimers.
8885240	1	65	theme	processing	505:514	arg1	sites					516:520	the proteolytic processing sites	489:520	the proteolytic processing sites	489:520	The present study verifies that the wide variation in the size of these products is due to incomplete cleavage of the proteolytic processing sites and the differential glycosylation of the N-linked glycosylation site at amino acid number 302 in the alpha C-subunit.
8885240	6	66	theme	110K	1433:1436	arg1	A					1446:1446	110K activin A	1433:1446	110K activin A	1433:1446	Since radioactively labeled 55K and 65K inhibin A and 110K activin A remained intact after incubation with rat pituitary cells for 72 h, there appears to be no conversion of these dimers to lower molecular weight forms by proteolytic cleavage at additional sites.
8885240	2	67	theme	one-	856:859	arg1	SDS/SDS-beta-ME					891:905	SDS/SDS-beta-ME	891:905	SDS/SDS-beta-ME	891:905	The identity of each of these products was established by mutagenesis of proteolytic processing sites and N-linked glycosylation sites, combined with the analysis of transfection products by immunoprecipitation and one- and two-dimensional SDS-PAGE (SDS/SDS-beta-ME).
8885240	2	67	theme	one-	856:859	arg1	SDS-PAGE					881:888	one- and two-dimensional SDS-PAGE	856:888	one- and two-dimensional SDS-PAGE (SDS/SDS-beta-ME)	856:906	The identity of each of these products was established by mutagenesis of proteolytic processing sites and N-linked glycosylation sites, combined with the analysis of transfection products by immunoprecipitation and one- and two-dimensional SDS-PAGE (SDS/SDS-beta-ME).
8885240	0	68	theme	beta	179:182	arg1	subunit					194:200	beta A-inhibin subunit	179:200	beta A-inhibin subunit	179:200	Characterization and determination of the biological activities of noncleavable high molecular weight forms of inhibin A and activin A. Recombinant expression of human alpha- and beta A-inhibin subunit cDNAs in mammalian 293 cells results in the secretion of 20-53K free alpha-subunit-derived products, 30-105K alpha beta A-inhibin dimers, and 24-110K beta A-activin dimers.
8885240	6	69	theme	weight	1585:1590	arg1	forms					1592:1596	lower molecular weight forms	1569:1596	lower molecular weight forms	1569:1596	Since radioactively labeled 55K and 65K inhibin A and 110K activin A remained intact after incubation with rat pituitary cells for 72 h, there appears to be no conversion of these dimers to lower molecular weight forms by proteolytic cleavage at additional sites.
8885240	0	70	link	alpha-subunit-derived	271:291	arg1	products					293:300	20-53K free alpha-subunit-derived products	259:300	20-53K free alpha-subunit-derived products	259:300	Characterization and determination of the biological activities of noncleavable high molecular weight forms of inhibin A and activin A. Recombinant expression of human alpha- and beta A-inhibin subunit cDNAs in mammalian 293 cells results in the secretion of 20-53K free alpha-subunit-derived products, 30-105K alpha beta A-inhibin dimers, and 24-110K beta A-activin dimers.
8885240	0	71	theme	subunit	194:200	arg1	cDNAs					202:206	human alpha- and beta A-inhibin subunit cDNAs	162:206	human alpha- and beta A-inhibin subunit cDNAs	162:206	Characterization and determination of the biological activities of noncleavable high molecular weight forms of inhibin A and activin A. Recombinant expression of human alpha- and beta A-inhibin subunit cDNAs in mammalian 293 cells results in the secretion of 20-53K free alpha-subunit-derived products, 30-105K alpha beta A-inhibin dimers, and 24-110K beta A-activin dimers.
8885240	6	72	theme	65K	1415:1417	arg1	A					1427:1427	55K and 65K inhibin A	1407:1427	A	1427:1427	Since radioactively labeled 55K and 65K inhibin A and 110K activin A remained intact after incubation with rat pituitary cells for 72 h, there appears to be no conversion of these dimers to lower molecular weight forms by proteolytic cleavage at additional sites.
8885240	2	73	theme	glycosylation	756:768	arg1	sites					770:774	N-linked glycosylation sites	747:774	N-linked glycosylation sites	747:774	The identity of each of these products was established by mutagenesis of proteolytic processing sites and N-linked glycosylation sites, combined with the analysis of transfection products by immunoprecipitation and one- and two-dimensional SDS-PAGE (SDS/SDS-beta-ME).
8885240	0	74	from	expression	148:157	arg1	cells					225:229	mammalian 293 cells	211:229	mammalian 293 cells	211:229	Characterization and determination of the biological activities of noncleavable high molecular weight forms of inhibin A and activin A. Recombinant expression of human alpha- and beta A-inhibin subunit cDNAs in mammalian 293 cells results in the secretion of 20-53K free alpha-subunit-derived products, 30-105K alpha beta A-inhibin dimers, and 24-110K beta A-activin dimers.
8885240	3	75	theme	noncleavable	1049:1060	arg1	dimers					1082:1087	55K and 65K inhibin dimers	1062:1087	55K and 65K inhibin dimers	1062:1087	Transient expression of processing site mutants of the alpha- and beta A-subunits in 293 cells was used to generate microgram quantities of noncleavable 55K and 65K inhibin dimers, and noncleavable 110K activin A dimers.
8885240	4	76	theme	65K	1142:1144	arg1	A					1154:1154	55K and 65K inhibin A	1134:1154	A	1154:1154	The 55K and 65K inhibin A forms were purified and found to be fully biologically active in a rat pituitary cell bioassay.
8885240	0	77	theme	24-110K	344:350	arg1	dimers					367:372	24-110K beta A-activin dimers	344:372	24-110K beta A-activin dimers	344:372	Characterization and determination of the biological activities of noncleavable high molecular weight forms of inhibin A and activin A. Recombinant expression of human alpha- and beta A-inhibin subunit cDNAs in mammalian 293 cells results in the secretion of 20-53K free alpha-subunit-derived products, 30-105K alpha beta A-inhibin dimers, and 24-110K beta A-activin dimers.
8885240	6	78	theme	rat	1486:1488	arg1	cells					1500:1504	rat pituitary cells	1486:1504	rat pituitary cells	1486:1504	Since radioactively labeled 55K and 65K inhibin A and 110K activin A remained intact after incubation with rat pituitary cells for 72 h, there appears to be no conversion of these dimers to lower molecular weight forms by proteolytic cleavage at additional sites.
8885240	1	79	from	number	606:611	arg1	glycosylation					543:555	the differential glycosylation	526:555	the differential glycosylation of the N-linked glycosylation site at amino acid number 302 in the alpha C-subunit	526:638	The present study verifies that the wide variation in the size of these products is due to incomplete cleavage of the proteolytic processing sites and the differential glycosylation of the N-linked glycosylation site at amino acid number 302 in the alpha C-subunit.
8885240	1	79	from	number	606:611	arg1	C-subunit					630:638	the alpha C-subunit	620:638	the alpha C-subunit	620:638	The present study verifies that the wide variation in the size of these products is due to incomplete cleavage of the proteolytic processing sites and the differential glycosylation of the N-linked glycosylation site at amino acid number 302 in the alpha C-subunit.
8885240	1	79	from	number	606:611	arg1	cleavage					477:484	incomplete cleavage	466:484	incomplete cleavage of the proteolytic processing sites	466:520	The present study verifies that the wide variation in the size of these products is due to incomplete cleavage of the proteolytic processing sites and the differential glycosylation of the N-linked glycosylation site at amino acid number 302 in the alpha C-subunit.
8885240	1	79	from	number	606:611	arg1	site					587:590	the N-linked glycosylation site	560:590	the N-linked glycosylation site at amino acid number 302 in the alpha C-subunit	560:638	The present study verifies that the wide variation in the size of these products is due to incomplete cleavage of the proteolytic processing sites and the differential glycosylation of the N-linked glycosylation site at amino acid number 302 in the alpha C-subunit.
8885240	0	80	theme	activin	125:131	arg1	forms					102:106	noncleavable high molecular weight forms	67:106	noncleavable high molecular weight forms of inhibin A and activin	67:131	Characterization and determination of the biological activities of noncleavable high molecular weight forms of inhibin A and activin A. Recombinant expression of human alpha- and beta A-inhibin subunit cDNAs in mammalian 293 cells results in the secretion of 20-53K free alpha-subunit-derived products, 30-105K alpha beta A-inhibin dimers, and 24-110K beta A-activin dimers.
8885240	8	81	theme	24K	1867:1869	arg1	form					1871:1874	the 24K form	1863:1874	the 24K form	1863:1874	In contrast, cleavage of the 110K activin A precursor to the 24K form would appear to be necessary for activity.
8885240	0	82	theme	A-activin	357:365	arg1	dimers					367:372	24-110K beta A-activin dimers	344:372	24-110K beta A-activin dimers	344:372	Characterization and determination of the biological activities of noncleavable high molecular weight forms of inhibin A and activin A. Recombinant expression of human alpha- and beta A-inhibin subunit cDNAs in mammalian 293 cells results in the secretion of 20-53K free alpha-subunit-derived products, 30-105K alpha beta A-inhibin dimers, and 24-110K beta A-activin dimers.
8885240	0	83	theme	Recombinant	136:146	arg1	expression					148:157	Recombinant expression	136:157	Recombinant expression of human alpha- and beta A-inhibin subunit cDNAs in mammalian 293 cells	136:229	Characterization and determination of the biological activities of noncleavable high molecular weight forms of inhibin A and activin A. Recombinant expression of human alpha- and beta A-inhibin subunit cDNAs in mammalian 293 cells results in the secretion of 20-53K free alpha-subunit-derived products, 30-105K alpha beta A-inhibin dimers, and 24-110K beta A-activin dimers.
8885240	2	84	link	N-linked	747:754	arg1	sites					770:774	N-linked glycosylation sites	747:774	N-linked glycosylation sites	747:774	The identity of each of these products was established by mutagenesis of proteolytic processing sites and N-linked glycosylation sites, combined with the analysis of transfection products by immunoprecipitation and one- and two-dimensional SDS-PAGE (SDS/SDS-beta-ME).
8885240	6	85	theme	additional	1625:1634	arg1	sites					1636:1640	additional sites	1625:1640	additional sites	1625:1640	Since radioactively labeled 55K and 65K inhibin A and 110K activin A remained intact after incubation with rat pituitary cells for 72 h, there appears to be no conversion of these dimers to lower molecular weight forms by proteolytic cleavage at additional sites.
8885240	3	86	from	mutants	949:955	arg1	cells					998:1002	293 cells	994:1002	293 cells	994:1002	Transient expression of processing site mutants of the alpha- and beta A-subunits in 293 cells was used to generate microgram quantities of noncleavable 55K and 65K inhibin dimers, and noncleavable 110K activin A dimers.
8885240	8	87	theme	A	1848:1848	arg1	precursor					1850:1858	the 110K activin A precursor	1831:1858	the 110K activin A precursor	1831:1858	In contrast, cleavage of the 110K activin A precursor to the 24K form would appear to be necessary for activity.
8885240	0	88	theme	alpha-subunit-derived	271:291	arg1	products					293:300	20-53K free alpha-subunit-derived products	259:300	20-53K free alpha-subunit-derived products	259:300	Characterization and determination of the biological activities of noncleavable high molecular weight forms of inhibin A and activin A. Recombinant expression of human alpha- and beta A-inhibin subunit cDNAs in mammalian 293 cells results in the secretion of 20-53K free alpha-subunit-derived products, 30-105K alpha beta A-inhibin dimers, and 24-110K beta A-activin dimers.
8885240	5	89	theme	110K	1256:1259	arg1	HMW					1284:1286	HMW	1284:1286	HMW	1284:1286	The 110K high molecular weight (HMW) form of human activin A failed to show any FSH-releasing activity in the pituitary assay.
8885240	5	89	theme	110K	1256:1259	arg1	weight					1276:1281	110K high molecular weight	1256:1281	The 110K high molecular weight (HMW) form of human activin A	1252:1311	The 110K high molecular weight (HMW) form of human activin A failed to show any FSH-releasing activity in the pituitary assay.
8885240	0	90	theme	alpha-	168:173	arg1	cDNAs					202:206	human alpha- and beta A-inhibin subunit cDNAs	162:206	human alpha- and beta A-inhibin subunit cDNAs	162:206	Characterization and determination of the biological activities of noncleavable high molecular weight forms of inhibin A and activin A. Recombinant expression of human alpha- and beta A-inhibin subunit cDNAs in mammalian 293 cells results in the secretion of 20-53K free alpha-subunit-derived products, 30-105K alpha beta A-inhibin dimers, and 24-110K beta A-activin dimers.
8885240	1	91	theme	wide	411:414	arg1	due					459:461	due	459:461	due	459:461	The present study verifies that the wide variation in the size of these products is due to incomplete cleavage of the proteolytic processing sites and the differential glycosylation of the N-linked glycosylation site at amino acid number 302 in the alpha C-subunit.
8885240	1	91	theme	wide	411:414	arg1	variation					416:424	the wide variation	407:424	the wide variation in the size of these products	407:454	The present study verifies that the wide variation in the size of these products is due to incomplete cleavage of the proteolytic processing sites and the differential glycosylation of the N-linked glycosylation site at amino acid number 302 in the alpha C-subunit.
8885240	2	92	theme	processing	726:735	arg1	sites					737:741	proteolytic processing sites	714:741	proteolytic processing sites	714:741	The identity of each of these products was established by mutagenesis of proteolytic processing sites and N-linked glycosylation sites, combined with the analysis of transfection products by immunoprecipitation and one- and two-dimensional SDS-PAGE (SDS/SDS-beta-ME).
8885240	1	93	theme	acid	601:604	arg1	number					606:611	amino acid number 302	595:615	amino acid number 302 in the alpha C-subunit	595:638	The present study verifies that the wide variation in the size of these products is due to incomplete cleavage of the proteolytic processing sites and the differential glycosylation of the N-linked glycosylation site at amino acid number 302 in the alpha C-subunit.
8885240	1	94	from	variation	416:424	arg1	size					433:436	the size	429:436	the size of these products	429:454	The present study verifies that the wide variation in the size of these products is due to incomplete cleavage of the proteolytic processing sites and the differential glycosylation of the N-linked glycosylation site at amino acid number 302 in the alpha C-subunit.
8885240	0	95	theme	alpha	311:315	arg1	dimers					332:337	30-105K alpha beta A-inhibin dimers	303:337	30-105K alpha beta A-inhibin dimers	303:337	Characterization and determination of the biological activities of noncleavable high molecular weight forms of inhibin A and activin A. Recombinant expression of human alpha- and beta A-inhibin subunit cDNAs in mammalian 293 cells results in the secretion of 20-53K free alpha-subunit-derived products, 30-105K alpha beta A-inhibin dimers, and 24-110K beta A-activin dimers.
8885240	7	96	theme	first	1670:1674	arg1	time					1676:1679	the first time	1666:1679	the first time	1666:1679	These results show for the first time that 55K and 65K inhibit A are intrinsically biologically active and do not require cleavage to the 32K form for activation.
8885240	0	97	theme	weight	95:100	arg1	forms					102:106	noncleavable high molecular weight forms	67:106	noncleavable high molecular weight forms of inhibin A and activin	67:131	Characterization and determination of the biological activities of noncleavable high molecular weight forms of inhibin A and activin A. Recombinant expression of human alpha- and beta A-inhibin subunit cDNAs in mammalian 293 cells results in the secretion of 20-53K free alpha-subunit-derived products, 30-105K alpha beta A-inhibin dimers, and 24-110K beta A-activin dimers.
8885240	3	98	theme	inhibin	1074:1080	arg1	dimers					1082:1087	55K and 65K inhibin dimers	1062:1087	55K and 65K inhibin dimers	1062:1087	Transient expression of processing site mutants of the alpha- and beta A-subunits in 293 cells was used to generate microgram quantities of noncleavable 55K and 65K inhibin dimers, and noncleavable 110K activin A dimers.
8885240	0	99	theme	A-inhibin	322:330	arg1	dimers					332:337	30-105K alpha beta A-inhibin dimers	303:337	30-105K alpha beta A-inhibin dimers	303:337	Characterization and determination of the biological activities of noncleavable high molecular weight forms of inhibin A and activin A. Recombinant expression of human alpha- and beta A-inhibin subunit cDNAs in mammalian 293 cells results in the secretion of 20-53K free alpha-subunit-derived products, 30-105K alpha beta A-inhibin dimers, and 24-110K beta A-activin dimers.
8885240	1	100	link	N-linked	564:571	arg1	site					587:590	the N-linked glycosylation site	560:590	the N-linked glycosylation site at amino acid number 302 in the alpha C-subunit	560:638	The present study verifies that the wide variation in the size of these products is due to incomplete cleavage of the proteolytic processing sites and the differential glycosylation of the N-linked glycosylation site at amino acid number 302 in the alpha C-subunit.
8885240	6	101	theme	molecular	1575:1583	arg1	forms					1592:1596	lower molecular weight forms	1569:1596	lower molecular weight forms	1569:1596	Since radioactively labeled 55K and 65K inhibin A and 110K activin A remained intact after incubation with rat pituitary cells for 72 h, there appears to be no conversion of these dimers to lower molecular weight forms by proteolytic cleavage at additional sites.
8885240	4	102	theme	pituitary	1227:1235	arg1	bioassay					1242:1249	a rat pituitary cell bioassay	1221:1249	a rat pituitary cell bioassay	1221:1249	The 55K and 65K inhibin A forms were purified and found to be fully biologically active in a rat pituitary cell bioassay.
8885240	0	103	theme	A	119:119	arg1	forms					102:106	noncleavable high molecular weight forms	67:106	noncleavable high molecular weight forms of inhibin A and activin	67:131	Characterization and determination of the biological activities of noncleavable high molecular weight forms of inhibin A and activin A. Recombinant expression of human alpha- and beta A-inhibin subunit cDNAs in mammalian 293 cells results in the secretion of 20-53K free alpha-subunit-derived products, 30-105K alpha beta A-inhibin dimers, and 24-110K beta A-activin dimers.
8885240	2	104	gly	glycosylation	756:768	arg2	sites					770:774	N-linked glycosylation sites	747:774	N-linked glycosylation sites	747:774	The identity of each of these products was established by mutagenesis of proteolytic processing sites and N-linked glycosylation sites, combined with the analysis of transfection products by immunoprecipitation and one- and two-dimensional SDS-PAGE (SDS/SDS-beta-ME).
8885240	3	105	theme	noncleavable	1094:1105	arg1	A					1120:1120	noncleavable 110K activin A	1094:1120	noncleavable 110K activin A dimers	1094:1127	Transient expression of processing site mutants of the alpha- and beta A-subunits in 293 cells was used to generate microgram quantities of noncleavable 55K and 65K inhibin dimers, and noncleavable 110K activin A dimers.
8885240	3	106	theme	processing	933:942	arg1	mutants					949:955	processing site mutants	933:955	processing site mutants of the alpha- and beta A-subunits in 293 cells	933:1002	Transient expression of processing site mutants of the alpha- and beta A-subunits in 293 cells was used to generate microgram quantities of noncleavable 55K and 65K inhibin dimers, and noncleavable 110K activin A dimers.
8885240	5	107	theme	high	1261:1264	arg1	HMW					1284:1286	HMW	1284:1286	HMW	1284:1286	The 110K high molecular weight (HMW) form of human activin A failed to show any FSH-releasing activity in the pituitary assay.
8885240	5	107	theme	high	1261:1264	arg1	weight					1276:1281	110K high molecular weight	1256:1281	The 110K high molecular weight (HMW) form of human activin A	1252:1311	The 110K high molecular weight (HMW) form of human activin A failed to show any FSH-releasing activity in the pituitary assay.
8885240	5	108	theme	activin	1303:1309	arg1	A					1311:1311	human activin A	1297:1311	human activin A	1297:1311	The 110K high molecular weight (HMW) form of human activin A failed to show any FSH-releasing activity in the pituitary assay.
8885240	4	109	from	active	1211:1216	arg1	bioassay					1242:1249	a rat pituitary cell bioassay	1221:1249	a rat pituitary cell bioassay	1221:1249	The 55K and 65K inhibin A forms were purified and found to be fully biologically active in a rat pituitary cell bioassay.
8885240	3	110	from	cells	998:1002	arg1	mutants					949:955	processing site mutants	933:955	processing site mutants of the alpha- and beta A-subunits in 293 cells	933:1002	Transient expression of processing site mutants of the alpha- and beta A-subunits in 293 cells was used to generate microgram quantities of noncleavable 55K and 65K inhibin dimers, and noncleavable 110K activin A dimers.
8885240	2	111	theme	each	657:660	arg1	identity					645:652	The identity	641:652	The identity of each of these products	641:678	The identity of each of these products was established by mutagenesis of proteolytic processing sites and N-linked glycosylation sites, combined with the analysis of transfection products by immunoprecipitation and one- and two-dimensional SDS-PAGE (SDS/SDS-beta-ME).
8885240	6	112	theme	labeled	1399:1405	arg1	A					1427:1427	55K and 65K inhibin A	1407:1427	A	1427:1427	Since radioactively labeled 55K and 65K inhibin A and 110K activin A remained intact after incubation with rat pituitary cells for 72 h, there appears to be no conversion of these dimers to lower molecular weight forms by proteolytic cleavage at additional sites.
8885240	3	113	theme	dimers	1122:1127	arg1	quantities					1035:1044	microgram quantities	1025:1044	microgram quantities of noncleavable 55K and 65K inhibin dimers, and noncleavable 110K activin A dimers	1025:1127	Transient expression of processing site mutants of the alpha- and beta A-subunits in 293 cells was used to generate microgram quantities of noncleavable 55K and 65K inhibin dimers, and noncleavable 110K activin A dimers.
8885240	0	114	theme	20-53K	259:264	arg1	products					293:300	20-53K free alpha-subunit-derived products	259:300	20-53K free alpha-subunit-derived products	259:300	Characterization and determination of the biological activities of noncleavable high molecular weight forms of inhibin A and activin A. Recombinant expression of human alpha- and beta A-inhibin subunit cDNAs in mammalian 293 cells results in the secretion of 20-53K free alpha-subunit-derived products, 30-105K alpha beta A-inhibin dimers, and 24-110K beta A-activin dimers.
8885240	6	115	from	sites	1636:1640	arg1	cleavage					1613:1620	proteolytic cleavage	1601:1620	proteolytic cleavage at additional sites	1601:1640	Since radioactively labeled 55K and 65K inhibin A and 110K activin A remained intact after incubation with rat pituitary cells for 72 h, there appears to be no conversion of these dimers to lower molecular weight forms by proteolytic cleavage at additional sites.
8885240	1	116	theme	glycosylation	573:585	arg1	site					587:590	the N-linked glycosylation site	560:590	the N-linked glycosylation site at amino acid number 302 in the alpha C-subunit	560:638	The present study verifies that the wide variation in the size of these products is due to incomplete cleavage of the proteolytic processing sites and the differential glycosylation of the N-linked glycosylation site at amino acid number 302 in the alpha C-subunit.
8885240	0	117	theme	biological	42:51	arg1	activities					53:62	the biological activities	38:62	the biological activities of noncleavable high molecular weight forms of inhibin A and activin A. Recombinant expression of human alpha- and beta A-inhibin subunit cDNAs in mammalian 293 cells	38:229	Characterization and determination of the biological activities of noncleavable high molecular weight forms of inhibin A and activin A. Recombinant expression of human alpha- and beta A-inhibin subunit cDNAs in mammalian 293 cells results in the secretion of 20-53K free alpha-subunit-derived products, 30-105K alpha beta A-inhibin dimers, and 24-110K beta A-activin dimers.
8885240	5	118	theme	human	1297:1301	arg1	A					1311:1311	human activin A	1297:1311	human activin A	1297:1311	The 110K high molecular weight (HMW) form of human activin A failed to show any FSH-releasing activity in the pituitary assay.
8885240	3	119	theme	activin	1112:1118	arg1	A					1120:1120	noncleavable 110K activin A	1094:1120	noncleavable 110K activin A dimers	1094:1127	Transient expression of processing site mutants of the alpha- and beta A-subunits in 293 cells was used to generate microgram quantities of noncleavable 55K and 65K inhibin dimers, and noncleavable 110K activin A dimers.
8885240	3	120	theme	mutants	949:955	arg1	expression					919:928	Transient expression	909:928	Transient expression of processing site mutants of the alpha- and beta A-subunits in 293 cells	909:1002	Transient expression of processing site mutants of the alpha- and beta A-subunits in 293 cells was used to generate microgram quantities of noncleavable 55K and 65K inhibin dimers, and noncleavable 110K activin A dimers.
8885240	1	121	theme	incomplete	466:475	arg1	cleavage					477:484	incomplete cleavage	466:484	incomplete cleavage of the proteolytic processing sites	466:520	The present study verifies that the wide variation in the size of these products is due to incomplete cleavage of the proteolytic processing sites and the differential glycosylation of the N-linked glycosylation site at amino acid number 302 in the alpha C-subunit.
8885240	3	122	theme	A-subunits	980:989	arg1	mutants					949:955	processing site mutants	933:955	processing site mutants of the alpha- and beta A-subunits in 293 cells	933:1002	Transient expression of processing site mutants of the alpha- and beta A-subunits in 293 cells was used to generate microgram quantities of noncleavable 55K and 65K inhibin dimers, and noncleavable 110K activin A dimers.
8885240	7	123	theme	32K	1781:1783	arg1	form					1785:1788	the 32K form	1777:1788	the 32K form	1777:1788	These results show for the first time that 55K and 65K inhibit A are intrinsically biologically active and do not require cleavage to the 32K form for activation.
8885240	5	124	theme	pituitary	1362:1370	arg1	assay					1372:1376	the pituitary assay	1358:1376	the pituitary assay	1358:1376	The 110K high molecular weight (HMW) form of human activin A failed to show any FSH-releasing activity in the pituitary assay.
8885240	1	125	theme	proteolytic	493:503	arg1	sites					516:520	the proteolytic processing sites	489:520	the proteolytic processing sites	489:520	The present study verifies that the wide variation in the size of these products is due to incomplete cleavage of the proteolytic processing sites and the differential glycosylation of the N-linked glycosylation site at amino acid number 302 in the alpha C-subunit.
8885240	6	126	theme	activin	1438:1444	arg1	A					1446:1446	110K activin A	1433:1446	110K activin A	1433:1446	Since radioactively labeled 55K and 65K inhibin A and 110K activin A remained intact after incubation with rat pituitary cells for 72 h, there appears to be no conversion of these dimers to lower molecular weight forms by proteolytic cleavage at additional sites.
8885240	1	127	theme	sites	516:520	arg1	glycosylation					543:555	the differential glycosylation	526:555	the differential glycosylation of the N-linked glycosylation site at amino acid number 302 in the alpha C-subunit	526:638	The present study verifies that the wide variation in the size of these products is due to incomplete cleavage of the proteolytic processing sites and the differential glycosylation of the N-linked glycosylation site at amino acid number 302 in the alpha C-subunit.
8885240	1	127	theme	sites	516:520	arg1	cleavage					477:484	incomplete cleavage	466:484	incomplete cleavage of the proteolytic processing sites	466:520	The present study verifies that the wide variation in the size of these products is due to incomplete cleavage of the proteolytic processing sites and the differential glycosylation of the N-linked glycosylation site at amino acid number 302 in the alpha C-subunit.
8638940	6	0	theme	glycosylasparaginase	1088:1107	arg1	folding					1063:1069	folding	1063:1069	folding	1063:1069	These glycosylation sequenons were mutagenized to determine the role of the oligosaccharide at each site in proper folding and transport of glycosylasparaginase.
8638940	6	0	theme	glycosylasparaginase	1088:1107	arg1	transport					1075:1083	transport	1075:1083	transport	1075:1083	These glycosylation sequenons were mutagenized to determine the role of the oligosaccharide at each site in proper folding and transport of glycosylasparaginase.
8638940	3	1	theme	initial	487:493	arg1	polypeptide					515:525	the initial single-chain 49-kDa polypeptide	483:525	the initial single-chain 49-kDa polypeptide	483:525	Mature enzyme is formed by two proteolytic cleavage steps subsequent to removal of its signal peptide: (1) an activation cleavage in the ER of the initial single-chain 49-kDa polypeptide into a 27-kDa alpha- and 19-kDa beta-subunit; (2) a cleavage in lysosomes which removes 10 amino acids from the C-terminus of the alpha-subunit without affecting enzyme activity.
8638940	8	2	gly	glycosylation	1454:1466	arg1	site					1488:1491	the beta-subunit site	1471:1491	the beta-subunit site	1471:1491	Deletion of the beta-subunit oligosaccharide oat N308 by an aspartic acid substitution resulted in very little protein or enzyme activity in the transfected cells, reemphasizing that glycosylation of the beta-subunit site is important for efficient folding and/or targeting.
8638940	3	3	theme	27-kDa	534:539	arg1	alpha-					541:546	a 27-kDa alpha-	532:546	a 27-kDa alpha-	532:546	Mature enzyme is formed by two proteolytic cleavage steps subsequent to removal of its signal peptide: (1) an activation cleavage in the ER of the initial single-chain 49-kDa polypeptide into a 27-kDa alpha- and 19-kDa beta-subunit; (2) a cleavage in lysosomes which removes 10 amino acids from the C-terminus of the alpha-subunit without affecting enzyme activity.
8638940	9	4	theme	same	1707:1710	arg1	substitution					1747:1758	the single beta-subunit substitution	1723:1758	the single beta-subunit substitution	1723:1758	A different mutation to eliminate the same N-glycosylation sequenon (T310A) yielded more protein and enzyme activity, and a double mutant N38D/T310A yielded the same results as the single beta-subunit substitution.
8638940	9	4	theme	same	1707:1710	arg1	results					1712:1718	the same results	1703:1718	the same results	1703:1718	A different mutation to eliminate the same N-glycosylation sequenon (T310A) yielded more protein and enzyme activity, and a double mutant N38D/T310A yielded the same results as the single beta-subunit substitution.
8638940	1	5	gly	glycoproteins	205:217	arg1	glycoproteins					205:217	N-linked glycoproteins	196:217	N-linked glycoproteins	196:217	Glycosylasparaginase (EC 3.5.1.26) is a lysosomal amidase which hydrolyzes the bond between asparagine and the sugar moiety in N-linked glycoproteins.
8638940	4	6	contain	contains	743:750	arg2	oligosaccharide					765:779	one N-linked oligosaccharide	752:779	one N-linked oligosaccharide	752:779	Each subunit of glycosylasparaginase contains one N-linked oligosaccharide (N38, alpha-subunit; N308, beta-subunit).
8638940	4	6	contain	contains	743:750	arg1	subunit					711:717	Each subunit	706:717	Each subunit of glycosylasparaginase	706:741	Each subunit of glycosylasparaginase contains one N-linked oligosaccharide (N38, alpha-subunit; N308, beta-subunit).
8638940	2	7	theme	glycoprotein	314:325	arg1	degradation					327:337	glycoprotein degradation	314:337	glycoprotein degradation	314:337	Deficiency of the enzyme results in aspartylglycosaminuria (AGU), the most common disorder of glycoprotein degradation.
8638940	1	8	theme	N-linked	196:203	arg1	glycoproteins					205:217	N-linked glycoproteins	196:217	N-linked glycoproteins	196:217	Glycosylasparaginase (EC 3.5.1.26) is a lysosomal amidase which hydrolyzes the bond between asparagine and the sugar moiety in N-linked glycoproteins.
8638940	9	9	theme	single	1727:1732	arg1	substitution					1747:1758	the single beta-subunit substitution	1723:1758	the single beta-subunit substitution	1723:1758	A different mutation to eliminate the same N-glycosylation sequenon (T310A) yielded more protein and enzyme activity, and a double mutant N38D/T310A yielded the same results as the single beta-subunit substitution.
8638940	9	9	theme	single	1727:1732	arg1	results					1712:1718	the same results	1703:1718	the same results	1703:1718	A different mutation to eliminate the same N-glycosylation sequenon (T310A) yielded more protein and enzyme activity, and a double mutant N38D/T310A yielded the same results as the single beta-subunit substitution.
8638940	8	10	theme	beta-subunit	1287:1298	arg1	N308					1320:1323	the beta-subunit oligosaccharide oat N308	1283:1323	the beta-subunit oligosaccharide oat N308	1283:1323	Deletion of the beta-subunit oligosaccharide oat N308 by an aspartic acid substitution resulted in very little protein or enzyme activity in the transfected cells, reemphasizing that glycosylation of the beta-subunit site is important for efficient folding and/or targeting.
8638940	3	11	dep	cleavage	579:586	arg1	2					574:574	2	574:574	2	574:574	Mature enzyme is formed by two proteolytic cleavage steps subsequent to removal of its signal peptide: (1) an activation cleavage in the ER of the initial single-chain 49-kDa polypeptide into a 27-kDa alpha- and 19-kDa beta-subunit; (2) a cleavage in lysosomes which removes 10 amino acids from the C-terminus of the alpha-subunit without affecting enzyme activity.
8638940	8	12	theme	beta-subunit	1475:1486	arg1	site					1488:1491	the beta-subunit site	1471:1491	the beta-subunit site	1471:1491	Deletion of the beta-subunit oligosaccharide oat N308 by an aspartic acid substitution resulted in very little protein or enzyme activity in the transfected cells, reemphasizing that glycosylation of the beta-subunit site is important for efficient folding and/or targeting.
8638940	8	13	theme	oat	1316:1318	arg1	N308					1320:1323	the beta-subunit oligosaccharide oat N308	1283:1323	the beta-subunit oligosaccharide oat N308	1283:1323	Deletion of the beta-subunit oligosaccharide oat N308 by an aspartic acid substitution resulted in very little protein or enzyme activity in the transfected cells, reemphasizing that glycosylation of the beta-subunit site is important for efficient folding and/or targeting.
8638940	11	14	theme	N308	1846:1849	arg1	important					1909:1917	important	1909:1917	important	1909:1917	The N308 glycosylation site of the beta-subunit appears to be more important in maintaining normal transport and stability of human glycosylasparaginase.
8638940	11	14	theme	N308	1846:1849	arg1	site					1865:1868	The N308 glycosylation site	1842:1868	The N308 glycosylation site of the beta-subunit	1842:1888	The N308 glycosylation site of the beta-subunit appears to be more important in maintaining normal transport and stability of human glycosylasparaginase.
8638940	11	14	theme	N308	1846:1849	arg1	beta-subunit					1877:1888	the beta-subunit	1873:1888	the beta-subunit	1873:1888	The N308 glycosylation site of the beta-subunit appears to be more important in maintaining normal transport and stability of human glycosylasparaginase.
8638940	10	15	theme	brefeldin	1829:1837	arg1	A					1839:1839	brefeldin A	1829:1839	brefeldin A	1829:1839	Yield of enzyme for all mutants was increased in cells treated with brefeldin A.
8638940	8	16	theme	aspartic	1331:1338	arg1	substitution					1345:1356	an aspartic acid substitution	1328:1356	an aspartic acid substitution	1328:1356	Deletion of the beta-subunit oligosaccharide oat N308 by an aspartic acid substitution resulted in very little protein or enzyme activity in the transfected cells, reemphasizing that glycosylation of the beta-subunit site is important for efficient folding and/or targeting.
8638940	4	17	theme	glycosylasparaginase	722:741	arg1	subunit					711:717	Each subunit	706:717	Each subunit of glycosylasparaginase	706:741	Each subunit of glycosylasparaginase contains one N-linked oligosaccharide (N38, alpha-subunit; N308, beta-subunit).
8638940	9	18	theme	different	1548:1556	arg1	mutation					1558:1565	A different mutation	1546:1565	A different mutation to eliminate the same N-glycosylation sequenon (T310A)	1546:1620	A different mutation to eliminate the same N-glycosylation sequenon (T310A) yielded more protein and enzyme activity, and a double mutant N38D/T310A yielded the same results as the single beta-subunit substitution.
8638940	3	19	theme	activation	450:459	arg1	cleavage					461:468	an activation cleavage	447:468	removal of its signal peptide: (1) an activation cleavage in the ER of the initial single-chain 49-kDa polypeptide into a 27-kDa alpha- and 19-kDa beta-subunit; (2) a cleavage in lysosomes which removes 10 amino acids from the C-terminus of the alpha-subunit without affecting enzyme activity	412:703	Mature enzyme is formed by two proteolytic cleavage steps subsequent to removal of its signal peptide: (1) an activation cleavage in the ER of the initial single-chain 49-kDa polypeptide into a 27-kDa alpha- and 19-kDa beta-subunit; (2) a cleavage in lysosomes which removes 10 amino acids from the C-terminus of the alpha-subunit without affecting enzyme activity.
8638940	5	20	theme	Endo-H	883:888	arg1	digestion					890:898	Endo-H digestion	883:898	Endo-H digestion	883:898	Both oligosaccharides were phosphorylated and releasable by Endo-H digestion, indicating they were of the high-mannose type.
8638940	7	21	theme	phosphorylated	1220:1233	arg1	oligosaccharide					1248:1262	the phosphorylated beta-subunit oligosaccharide	1216:1262	the phosphorylated beta-subunit oligosaccharide alone	1216:1268	An N38D mutant underwent the lysosomal processing step, indicating that targeting to lysosomes can be via the phosphorylated beta-subunit oligosaccharide alone.
8638940	4	22	dep	contains	743:750	arg1	N38					782:784	N38	782:784	N38	782:784	Each subunit of glycosylasparaginase contains one N-linked oligosaccharide (N38, alpha-subunit; N308, beta-subunit).
8638940	8	23	theme	little	1375:1380	arg1	protein					1382:1388	very little protein	1370:1388	very little protein	1370:1388	Deletion of the beta-subunit oligosaccharide oat N308 by an aspartic acid substitution resulted in very little protein or enzyme activity in the transfected cells, reemphasizing that glycosylation of the beta-subunit site is important for efficient folding and/or targeting.
8638940	9	24	theme	N-glycosylation	1589:1603	arg1	sequenon					1605:1612	the same N-glycosylation sequenon	1580:1612	the same N-glycosylation sequenon (T310A)	1580:1620	A different mutation to eliminate the same N-glycosylation sequenon (T310A) yielded more protein and enzyme activity, and a double mutant N38D/T310A yielded the same results as the single beta-subunit substitution.
8638940	9	24	theme	N-glycosylation	1589:1603	arg1	T310A					1615:1619	T310A	1615:1619	T310A	1615:1619	A different mutation to eliminate the same N-glycosylation sequenon (T310A) yielded more protein and enzyme activity, and a double mutant N38D/T310A yielded the same results as the single beta-subunit substitution.
8638940	3	25	dep	removal	412:418	arg1	cleavage					579:586	a cleavage	577:586	removal of its signal peptide: (1) an activation cleavage in the ER of the initial single-chain 49-kDa polypeptide into a 27-kDa alpha- and 19-kDa beta-subunit; (2) a cleavage in lysosomes which removes 10 amino acids from the C-terminus of the alpha-subunit without affecting enzyme activity	412:703	Mature enzyme is formed by two proteolytic cleavage steps subsequent to removal of its signal peptide: (1) an activation cleavage in the ER of the initial single-chain 49-kDa polypeptide into a 27-kDa alpha- and 19-kDa beta-subunit; (2) a cleavage in lysosomes which removes 10 amino acids from the C-terminus of the alpha-subunit without affecting enzyme activity.
8638940	3	25	dep	removal	412:418	arg1	cleavage					461:468	an activation cleavage	447:468	removal of its signal peptide: (1) an activation cleavage in the ER of the initial single-chain 49-kDa polypeptide into a 27-kDa alpha- and 19-kDa beta-subunit; (2) a cleavage in lysosomes which removes 10 amino acids from the C-terminus of the alpha-subunit without affecting enzyme activity	412:703	Mature enzyme is formed by two proteolytic cleavage steps subsequent to removal of its signal peptide: (1) an activation cleavage in the ER of the initial single-chain 49-kDa polypeptide into a 27-kDa alpha- and 19-kDa beta-subunit; (2) a cleavage in lysosomes which removes 10 amino acids from the C-terminus of the alpha-subunit without affecting enzyme activity.
8638940	3	26	from	cleavage	579:586	arg1	lysosomes					591:599	lysosomes	591:599	lysosomes which removes 10 amino acids from the C-terminus of the alpha-subunit without affecting enzyme activity	591:703	Mature enzyme is formed by two proteolytic cleavage steps subsequent to removal of its signal peptide: (1) an activation cleavage in the ER of the initial single-chain 49-kDa polypeptide into a 27-kDa alpha- and 19-kDa beta-subunit; (2) a cleavage in lysosomes which removes 10 amino acids from the C-terminus of the alpha-subunit without affecting enzyme activity.
8638940	3	27	theme	subsequent	398:407	arg1	steps					392:396	two proteolytic cleavage steps	367:396	two proteolytic cleavage steps subsequent to removal of its signal peptide: (1) an activation cleavage in the ER of the initial single-chain 49-kDa polypeptide into a 27-kDa alpha- and 19-kDa beta-subunit; (2) a cleavage in lysosomes which removes 10 amino acids from the C-terminus of the alpha-subunit without affecting enzyme activity	367:703	Mature enzyme is formed by two proteolytic cleavage steps subsequent to removal of its signal peptide: (1) an activation cleavage in the ER of the initial single-chain 49-kDa polypeptide into a 27-kDa alpha- and 19-kDa beta-subunit; (2) a cleavage in lysosomes which removes 10 amino acids from the C-terminus of the alpha-subunit without affecting enzyme activity.
8638940	3	28	theme	49-kDa	508:513	arg1	polypeptide					515:525	the initial single-chain 49-kDa polypeptide	483:525	the initial single-chain 49-kDa polypeptide	483:525	Mature enzyme is formed by two proteolytic cleavage steps subsequent to removal of its signal peptide: (1) an activation cleavage in the ER of the initial single-chain 49-kDa polypeptide into a 27-kDa alpha- and 19-kDa beta-subunit; (2) a cleavage in lysosomes which removes 10 amino acids from the C-terminus of the alpha-subunit without affecting enzyme activity.
8638940	3	29	theme	peptide	434:440	arg1	removal					412:418	removal	412:418	removal of its signal peptide: (1) an activation cleavage in the ER of the initial single-chain 49-kDa polypeptide into a 27-kDa alpha- and 19-kDa beta-subunit; (2) a cleavage in lysosomes which removes 10 amino acids from the C-terminus of the alpha-subunit without affecting enzyme activity	412:703	Mature enzyme is formed by two proteolytic cleavage steps subsequent to removal of its signal peptide: (1) an activation cleavage in the ER of the initial single-chain 49-kDa polypeptide into a 27-kDa alpha- and 19-kDa beta-subunit; (2) a cleavage in lysosomes which removes 10 amino acids from the C-terminus of the alpha-subunit without affecting enzyme activity.
8638940	5	30	theme	high-mannose	929:940	arg1	type					942:945	the high-mannose type	925:945	the high-mannose type	925:945	Both oligosaccharides were phosphorylated and releasable by Endo-H digestion, indicating they were of the high-mannose type.
8638940	6	31	theme	proper	1056:1061	arg1	folding					1063:1069	folding	1063:1069	folding	1063:1069	These glycosylation sequenons were mutagenized to determine the role of the oligosaccharide at each site in proper folding and transport of glycosylasparaginase.
8638940	3	32	theme	cleavage	383:390	arg1	steps					392:396	two proteolytic cleavage steps	367:396	two proteolytic cleavage steps subsequent to removal of its signal peptide: (1) an activation cleavage in the ER of the initial single-chain 49-kDa polypeptide into a 27-kDa alpha- and 19-kDa beta-subunit; (2) a cleavage in lysosomes which removes 10 amino acids from the C-terminus of the alpha-subunit without affecting enzyme activity	367:703	Mature enzyme is formed by two proteolytic cleavage steps subsequent to removal of its signal peptide: (1) an activation cleavage in the ER of the initial single-chain 49-kDa polypeptide into a 27-kDa alpha- and 19-kDa beta-subunit; (2) a cleavage in lysosomes which removes 10 amino acids from the C-terminus of the alpha-subunit without affecting enzyme activity.
8638940	9	33	dep	mutation	1558:1565	arg1	eliminate					1570:1578	eliminate	1570:1578	to eliminate the same N-glycosylation sequenon (T310A)	1567:1620	A different mutation to eliminate the same N-glycosylation sequenon (T310A) yielded more protein and enzyme activity, and a double mutant N38D/T310A yielded the same results as the single beta-subunit substitution.
8638940	11	34	theme	human	1968:1972	arg1	glycosylasparaginase					1974:1993	human glycosylasparaginase	1968:1993	human glycosylasparaginase	1968:1993	The N308 glycosylation site of the beta-subunit appears to be more important in maintaining normal transport and stability of human glycosylasparaginase.
8638940	3	35	theme	amino	618:622	arg1	acids					624:628	10 amino acids	615:628	10 amino acids	615:628	Mature enzyme is formed by two proteolytic cleavage steps subsequent to removal of its signal peptide: (1) an activation cleavage in the ER of the initial single-chain 49-kDa polypeptide into a 27-kDa alpha- and 19-kDa beta-subunit; (2) a cleavage in lysosomes which removes 10 amino acids from the C-terminus of the alpha-subunit without affecting enzyme activity.
8638940	0	36	theme	lysosomal	37:45	arg1	glycosylasparaginase					47:66	lysosomal glycosylasparaginase	37:66	lysosomal glycosylasparaginase	37:66	Glycosylation and phosphorylation of lysosomal glycosylasparaginase.
8638940	11	37	gly	glycosylation	1851:1863	arg2	important					1909:1917	important	1909:1917	important	1909:1917	The N308 glycosylation site of the beta-subunit appears to be more important in maintaining normal transport and stability of human glycosylasparaginase.
8638940	11	37	gly	glycosylation	1851:1863	arg2	site					1865:1868	The N308 glycosylation site	1842:1868	The N308 glycosylation site of the beta-subunit	1842:1888	The N308 glycosylation site of the beta-subunit appears to be more important in maintaining normal transport and stability of human glycosylasparaginase.
8638940	11	37	gly	glycosylation	1851:1863	arg1	beta-subunit					1877:1888	the beta-subunit	1873:1888	the beta-subunit	1873:1888	The N308 glycosylation site of the beta-subunit appears to be more important in maintaining normal transport and stability of human glycosylasparaginase.
8638940	11	37	gly	glycosylation	1851:1863	arg2	beta-subunit					1877:1888	the beta-subunit	1873:1888	the beta-subunit	1873:1888	The N308 glycosylation site of the beta-subunit appears to be more important in maintaining normal transport and stability of human glycosylasparaginase.
8638940	7	38	theme	processing	1149:1158	arg1	step					1160:1163	the lysosomal processing step	1135:1163	the lysosomal processing step	1135:1163	An N38D mutant underwent the lysosomal processing step, indicating that targeting to lysosomes can be via the phosphorylated beta-subunit oligosaccharide alone.
8638940	4	39	link	N-linked	756:763	arg1	oligosaccharide					765:779	one N-linked oligosaccharide	752:779	one N-linked oligosaccharide	752:779	Each subunit of glycosylasparaginase contains one N-linked oligosaccharide (N38, alpha-subunit; N308, beta-subunit).
8638940	3	40	from	cleavage	461:468	arg1	ER					477:478	the ER	473:478	the ER of the initial single-chain 49-kDa polypeptide	473:525	Mature enzyme is formed by two proteolytic cleavage steps subsequent to removal of its signal peptide: (1) an activation cleavage in the ER of the initial single-chain 49-kDa polypeptide into a 27-kDa alpha- and 19-kDa beta-subunit; (2) a cleavage in lysosomes which removes 10 amino acids from the C-terminus of the alpha-subunit without affecting enzyme activity.
8638940	2	41	gly	glycoprotein	314:325	arg1	glycoprotein					314:325	glycoprotein degradation	314:337	glycoprotein degradation	314:337	Deficiency of the enzyme results in aspartylglycosaminuria (AGU), the most common disorder of glycoprotein degradation.
8638940	3	42	theme	single-chain	495:506	arg1	polypeptide					515:525	the initial single-chain 49-kDa polypeptide	483:525	the initial single-chain 49-kDa polypeptide	483:525	Mature enzyme is formed by two proteolytic cleavage steps subsequent to removal of its signal peptide: (1) an activation cleavage in the ER of the initial single-chain 49-kDa polypeptide into a 27-kDa alpha- and 19-kDa beta-subunit; (2) a cleavage in lysosomes which removes 10 amino acids from the C-terminus of the alpha-subunit without affecting enzyme activity.
8638940	3	43	dep	cleavage	461:468	arg1	1					444:444	1	444:444	1	444:444	Mature enzyme is formed by two proteolytic cleavage steps subsequent to removal of its signal peptide: (1) an activation cleavage in the ER of the initial single-chain 49-kDa polypeptide into a 27-kDa alpha- and 19-kDa beta-subunit; (2) a cleavage in lysosomes which removes 10 amino acids from the C-terminus of the alpha-subunit without affecting enzyme activity.
8638940	7	44	theme	N38D	1113:1116	arg1	mutant					1118:1123	An N38D mutant	1110:1123	An N38D mutant	1110:1123	An N38D mutant underwent the lysosomal processing step, indicating that targeting to lysosomes can be via the phosphorylated beta-subunit oligosaccharide alone.
8638940	2	45	theme	common	295:300	arg1	aspartylglycosaminuria					256:277	aspartylglycosaminuria	256:277	aspartylglycosaminuria (AGU)	256:283	Deficiency of the enzyme results in aspartylglycosaminuria (AGU), the most common disorder of glycoprotein degradation.
8638940	2	45	theme	common	295:300	arg1	disorder					302:309	the most common disorder	286:309	the most common disorder of glycoprotein degradation	286:337	Deficiency of the enzyme results in aspartylglycosaminuria (AGU), the most common disorder of glycoprotein degradation.
8638940	3	46	theme	19-kDa	552:557	arg1	beta-subunit					559:570	19-kDa beta-subunit	552:570	19-kDa beta-subunit	552:570	Mature enzyme is formed by two proteolytic cleavage steps subsequent to removal of its signal peptide: (1) an activation cleavage in the ER of the initial single-chain 49-kDa polypeptide into a 27-kDa alpha- and 19-kDa beta-subunit; (2) a cleavage in lysosomes which removes 10 amino acids from the C-terminus of the alpha-subunit without affecting enzyme activity.
8638940	3	47	theme	polypeptide	515:525	arg1	ER					477:478	the ER	473:478	the ER of the initial single-chain 49-kDa polypeptide	473:525	Mature enzyme is formed by two proteolytic cleavage steps subsequent to removal of its signal peptide: (1) an activation cleavage in the ER of the initial single-chain 49-kDa polypeptide into a 27-kDa alpha- and 19-kDa beta-subunit; (2) a cleavage in lysosomes which removes 10 amino acids from the C-terminus of the alpha-subunit without affecting enzyme activity.
8638940	1	48	theme	sugar	180:184	arg1	moiety					186:191	the sugar moiety	176:191	the sugar moiety	176:191	Glycosylasparaginase (EC 3.5.1.26) is a lysosomal amidase which hydrolyzes the bond between asparagine and the sugar moiety in N-linked glycoproteins.
8638940	3	49	theme	enzyme	689:694	arg1	activity					696:703	enzyme activity	689:703	enzyme activity	689:703	Mature enzyme is formed by two proteolytic cleavage steps subsequent to removal of its signal peptide: (1) an activation cleavage in the ER of the initial single-chain 49-kDa polypeptide into a 27-kDa alpha- and 19-kDa beta-subunit; (2) a cleavage in lysosomes which removes 10 amino acids from the C-terminus of the alpha-subunit without affecting enzyme activity.
8638940	2	50	theme	degradation	327:337	arg1	aspartylglycosaminuria					256:277	aspartylglycosaminuria	256:277	aspartylglycosaminuria (AGU)	256:283	Deficiency of the enzyme results in aspartylglycosaminuria (AGU), the most common disorder of glycoprotein degradation.
8638940	2	50	theme	degradation	327:337	arg1	disorder					302:309	the most common disorder	286:309	the most common disorder of glycoprotein degradation	286:337	Deficiency of the enzyme results in aspartylglycosaminuria (AGU), the most common disorder of glycoprotein degradation.
8638940	4	51	dep	N38	782:784	arg1	alpha-subunit					787:799	alpha-subunit	787:799	alpha-subunit	787:799	Each subunit of glycosylasparaginase contains one N-linked oligosaccharide (N38, alpha-subunit; N308, beta-subunit).
8638940	4	51	dep	N38	782:784	arg1	beta-subunit					808:819	beta-subunit	808:819	beta-subunit	808:819	Each subunit of glycosylasparaginase contains one N-linked oligosaccharide (N38, alpha-subunit; N308, beta-subunit).
8638940	6	52	from	site	1048:1051	arg1	folding					1063:1069	folding	1063:1069	folding	1063:1069	These glycosylation sequenons were mutagenized to determine the role of the oligosaccharide at each site in proper folding and transport of glycosylasparaginase.
8638940	6	52	from	site	1048:1051	arg1	role					1012:1015	the role	1008:1015	the role of the oligosaccharide at each site in proper folding and transport of glycosylasparaginase	1008:1107	These glycosylation sequenons were mutagenized to determine the role of the oligosaccharide at each site in proper folding and transport of glycosylasparaginase.
8638940	6	52	from	site	1048:1051	arg1	transport					1075:1083	transport	1075:1083	transport	1075:1083	These glycosylation sequenons were mutagenized to determine the role of the oligosaccharide at each site in proper folding and transport of glycosylasparaginase.
8638940	6	53	theme	glycosylation	954:966	arg1	sequenons					968:976	These glycosylation sequenons	948:976	These glycosylation sequenons	948:976	These glycosylation sequenons were mutagenized to determine the role of the oligosaccharide at each site in proper folding and transport of glycosylasparaginase.
8638940	9	54	theme	beta-subunit	1734:1745	arg1	substitution					1747:1758	the single beta-subunit substitution	1723:1758	the single beta-subunit substitution	1723:1758	A different mutation to eliminate the same N-glycosylation sequenon (T310A) yielded more protein and enzyme activity, and a double mutant N38D/T310A yielded the same results as the single beta-subunit substitution.
8638940	9	54	theme	beta-subunit	1734:1745	arg1	results					1712:1718	the same results	1703:1718	the same results	1703:1718	A different mutation to eliminate the same N-glycosylation sequenon (T310A) yielded more protein and enzyme activity, and a double mutant N38D/T310A yielded the same results as the single beta-subunit substitution.
8638940	8	55	theme	site	1488:1491	arg1	glycosylation					1454:1466	glycosylation	1454:1466	glycosylation of the beta-subunit site	1454:1491	Deletion of the beta-subunit oligosaccharide oat N308 by an aspartic acid substitution resulted in very little protein or enzyme activity in the transfected cells, reemphasizing that glycosylation of the beta-subunit site is important for efficient folding and/or targeting.
8638940	8	56	theme	oligosaccharide	1300:1314	arg1	N308					1320:1323	the beta-subunit oligosaccharide oat N308	1283:1323	the beta-subunit oligosaccharide oat N308	1283:1323	Deletion of the beta-subunit oligosaccharide oat N308 by an aspartic acid substitution resulted in very little protein or enzyme activity in the transfected cells, reemphasizing that glycosylation of the beta-subunit site is important for efficient folding and/or targeting.
8638940	2	57	theme	enzyme	238:243	arg1	Deficiency					220:229	Deficiency	220:229	Deficiency of the enzyme	220:243	Deficiency of the enzyme results in aspartylglycosaminuria (AGU), the most common disorder of glycoprotein degradation.
8638940	8	58	theme	efficient	1510:1518	arg1	folding					1520:1526	efficient folding	1510:1526	efficient folding	1510:1526	Deletion of the beta-subunit oligosaccharide oat N308 by an aspartic acid substitution resulted in very little protein or enzyme activity in the transfected cells, reemphasizing that glycosylation of the beta-subunit site is important for efficient folding and/or targeting.
8638940	8	59	theme	N308	1320:1323	arg1	Deletion					1271:1278	Deletion	1271:1278	Deletion of the beta-subunit oligosaccharide oat N308 by an aspartic acid substitution	1271:1356	Deletion of the beta-subunit oligosaccharide oat N308 by an aspartic acid substitution resulted in very little protein or enzyme activity in the transfected cells, reemphasizing that glycosylation of the beta-subunit site is important for efficient folding and/or targeting.
8638940	11	60	theme	glycosylation	1851:1863	arg1	important					1909:1917	important	1909:1917	important	1909:1917	The N308 glycosylation site of the beta-subunit appears to be more important in maintaining normal transport and stability of human glycosylasparaginase.
8638940	11	60	theme	glycosylation	1851:1863	arg1	site					1865:1868	The N308 glycosylation site	1842:1868	The N308 glycosylation site of the beta-subunit	1842:1888	The N308 glycosylation site of the beta-subunit appears to be more important in maintaining normal transport and stability of human glycosylasparaginase.
8638940	11	60	theme	glycosylation	1851:1863	arg1	beta-subunit					1877:1888	the beta-subunit	1873:1888	the beta-subunit	1873:1888	The N308 glycosylation site of the beta-subunit appears to be more important in maintaining normal transport and stability of human glycosylasparaginase.
8638940	6	61	theme	oligosaccharide	1024:1038	arg1	role					1012:1015	the role	1008:1015	the role of the oligosaccharide at each site in proper folding and transport of glycosylasparaginase	1008:1107	These glycosylation sequenons were mutagenized to determine the role of the oligosaccharide at each site in proper folding and transport of glycosylasparaginase.
8638940	7	62	theme	beta-subunit	1235:1246	arg1	oligosaccharide					1248:1262	the phosphorylated beta-subunit oligosaccharide	1216:1262	the phosphorylated beta-subunit oligosaccharide alone	1216:1268	An N38D mutant underwent the lysosomal processing step, indicating that targeting to lysosomes can be via the phosphorylated beta-subunit oligosaccharide alone.
8638940	8	63	theme	acid	1340:1343	arg1	substitution					1345:1356	an aspartic acid substitution	1328:1356	an aspartic acid substitution	1328:1356	Deletion of the beta-subunit oligosaccharide oat N308 by an aspartic acid substitution resulted in very little protein or enzyme activity in the transfected cells, reemphasizing that glycosylation of the beta-subunit site is important for efficient folding and/or targeting.
8638940	3	64	theme	Mature	340:345	arg1	enzyme					347:352	Mature enzyme	340:352	Mature enzyme	340:352	Mature enzyme is formed by two proteolytic cleavage steps subsequent to removal of its signal peptide: (1) an activation cleavage in the ER of the initial single-chain 49-kDa polypeptide into a 27-kDa alpha- and 19-kDa beta-subunit; (2) a cleavage in lysosomes which removes 10 amino acids from the C-terminus of the alpha-subunit without affecting enzyme activity.
8638940	9	65	theme	same	1584:1587	arg1	sequenon					1605:1612	the same N-glycosylation sequenon	1580:1612	the same N-glycosylation sequenon (T310A)	1580:1620	A different mutation to eliminate the same N-glycosylation sequenon (T310A) yielded more protein and enzyme activity, and a double mutant N38D/T310A yielded the same results as the single beta-subunit substitution.
8638940	9	65	theme	same	1584:1587	arg1	T310A					1615:1619	T310A	1615:1619	T310A	1615:1619	A different mutation to eliminate the same N-glycosylation sequenon (T310A) yielded more protein and enzyme activity, and a double mutant N38D/T310A yielded the same results as the single beta-subunit substitution.
8638940	3	66	theme	proteolytic	371:381	arg1	steps					392:396	two proteolytic cleavage steps	367:396	two proteolytic cleavage steps subsequent to removal of its signal peptide: (1) an activation cleavage in the ER of the initial single-chain 49-kDa polypeptide into a 27-kDa alpha- and 19-kDa beta-subunit; (2) a cleavage in lysosomes which removes 10 amino acids from the C-terminus of the alpha-subunit without affecting enzyme activity	367:703	Mature enzyme is formed by two proteolytic cleavage steps subsequent to removal of its signal peptide: (1) an activation cleavage in the ER of the initial single-chain 49-kDa polypeptide into a 27-kDa alpha- and 19-kDa beta-subunit; (2) a cleavage in lysosomes which removes 10 amino acids from the C-terminus of the alpha-subunit without affecting enzyme activity.
8638940	1	67	link	N-linked	196:203	arg1	glycoproteins					205:217	N-linked glycoproteins	196:217	N-linked glycoproteins	196:217	Glycosylasparaginase (EC 3.5.1.26) is a lysosomal amidase which hydrolyzes the bond between asparagine and the sugar moiety in N-linked glycoproteins.
8638940	4	68	theme	N-linked	756:763	arg1	oligosaccharide					765:779	one N-linked oligosaccharide	752:779	one N-linked oligosaccharide	752:779	Each subunit of glycosylasparaginase contains one N-linked oligosaccharide (N38, alpha-subunit; N308, beta-subunit).
8638940	1	69	from	bond	148:151	arg1	glycoproteins					205:217	N-linked glycoproteins	196:217	N-linked glycoproteins	196:217	Glycosylasparaginase (EC 3.5.1.26) is a lysosomal amidase which hydrolyzes the bond between asparagine and the sugar moiety in N-linked glycoproteins.
8638940	8	70	theme	enzyme	1393:1398	arg1	activity					1400:1407	enzyme activity	1393:1407	enzyme activity	1393:1407	Deletion of the beta-subunit oligosaccharide oat N308 by an aspartic acid substitution resulted in very little protein or enzyme activity in the transfected cells, reemphasizing that glycosylation of the beta-subunit site is important for efficient folding and/or targeting.
8638940	11	71	theme	normal	1934:1939	arg1	transport					1941:1949	normal transport	1934:1949	normal transport	1934:1949	The N308 glycosylation site of the beta-subunit appears to be more important in maintaining normal transport and stability of human glycosylasparaginase.
8638940	9	72	dep	mutant	1677:1682	arg1	N38D/T310A					1684:1693	N38D/T310A	1684:1693	N38D/T310A	1684:1693	A different mutation to eliminate the same N-glycosylation sequenon (T310A) yielded more protein and enzyme activity, and a double mutant N38D/T310A yielded the same results as the single beta-subunit substitution.
8638940	1	73	theme	lysosomal	109:117	arg1	Glycosylasparaginase					69:88	Glycosylasparaginase	69:88	Glycosylasparaginase (EC 3.5.1.26)	69:102	Glycosylasparaginase (EC 3.5.1.26) is a lysosomal amidase which hydrolyzes the bond between asparagine and the sugar moiety in N-linked glycoproteins.
8638940	1	73	theme	lysosomal	109:117	arg1	amidase					119:125	a lysosomal amidase	107:125	a lysosomal amidase which hydrolyzes the bond between asparagine and the sugar moiety in N-linked glycoproteins	107:217	Glycosylasparaginase (EC 3.5.1.26) is a lysosomal amidase which hydrolyzes the bond between asparagine and the sugar moiety in N-linked glycoproteins.
8638940	11	74	theme	glycosylasparaginase	1974:1993	arg1	transport					1941:1949	normal transport	1934:1949	normal transport	1934:1949	The N308 glycosylation site of the beta-subunit appears to be more important in maintaining normal transport and stability of human glycosylasparaginase.
8638940	11	74	theme	glycosylasparaginase	1974:1993	arg1	stability					1955:1963	stability	1955:1963	stability	1955:1963	The N308 glycosylation site of the beta-subunit appears to be more important in maintaining normal transport and stability of human glycosylasparaginase.
8638940	0	75	theme	glycosylasparaginase	47:66	arg1	phosphorylation					18:32	phosphorylation	18:32	phosphorylation	18:32	Glycosylation and phosphorylation of lysosomal glycosylasparaginase.
8638940	0	75	theme	glycosylasparaginase	47:66	arg1	Glycosylation					0:12	Glycosylation	0:12	Glycosylation	0:12	Glycosylation and phosphorylation of lysosomal glycosylasparaginase.
8638940	0	76	gly	Glycosylation	0:12	arg1	glycosylasparaginase					47:66	lysosomal glycosylasparaginase	37:66	lysosomal glycosylasparaginase	37:66	Glycosylation and phosphorylation of lysosomal glycosylasparaginase.
8638940	3	77	theme	signal	427:432	arg1	peptide					434:440	its signal peptide	423:440	its signal peptide	423:440	Mature enzyme is formed by two proteolytic cleavage steps subsequent to removal of its signal peptide: (1) an activation cleavage in the ER of the initial single-chain 49-kDa polypeptide into a 27-kDa alpha- and 19-kDa beta-subunit; (2) a cleavage in lysosomes which removes 10 amino acids from the C-terminus of the alpha-subunit without affecting enzyme activity.
8638940	8	78	theme	transfected	1416:1426	arg1	cells					1428:1432	the transfected cells	1412:1432	the transfected cells	1412:1432	Deletion of the beta-subunit oligosaccharide oat N308 by an aspartic acid substitution resulted in very little protein or enzyme activity in the transfected cells, reemphasizing that glycosylation of the beta-subunit site is important for efficient folding and/or targeting.
8638940	7	79	theme	lysosomal	1139:1147	arg1	step					1160:1163	the lysosomal processing step	1135:1163	the lysosomal processing step	1135:1163	An N38D mutant underwent the lysosomal processing step, indicating that targeting to lysosomes can be via the phosphorylated beta-subunit oligosaccharide alone.
8638940	9	80	theme	enzyme	1647:1652	arg1	activity					1654:1661	enzyme activity	1647:1661	enzyme activity	1647:1661	A different mutation to eliminate the same N-glycosylation sequenon (T310A) yielded more protein and enzyme activity, and a double mutant N38D/T310A yielded the same results as the single beta-subunit substitution.
8638940	4	81	dep	alpha-subunit	787:799	arg1	N308					802:805	N308	802:805	N308	802:805	Each subunit of glycosylasparaginase contains one N-linked oligosaccharide (N38, alpha-subunit; N308, beta-subunit).
8638940	9	82	theme	double	1670:1675	arg1	mutant					1677:1682	a double mutant N38D/T310A	1668:1693	a double mutant N38D/T310A	1668:1693	A different mutation to eliminate the same N-glycosylation sequenon (T310A) yielded more protein and enzyme activity, and a double mutant N38D/T310A yielded the same results as the single beta-subunit substitution.
8638940	11	83	theme	beta-subunit	1877:1888	arg1	important					1909:1917	important	1909:1917	important	1909:1917	The N308 glycosylation site of the beta-subunit appears to be more important in maintaining normal transport and stability of human glycosylasparaginase.
8638940	11	83	theme	beta-subunit	1877:1888	arg1	site					1865:1868	The N308 glycosylation site	1842:1868	The N308 glycosylation site of the beta-subunit	1842:1888	The N308 glycosylation site of the beta-subunit appears to be more important in maintaining normal transport and stability of human glycosylasparaginase.
8638940	11	83	theme	beta-subunit	1877:1888	arg1	beta-subunit					1877:1888	the beta-subunit	1873:1888	the beta-subunit	1873:1888	The N308 glycosylation site of the beta-subunit appears to be more important in maintaining normal transport and stability of human glycosylasparaginase.
8638940	3	84	theme	alpha-subunit	657:669	arg1	C-terminus					639:648	the C-terminus	635:648	the C-terminus of the alpha-subunit	635:669	Mature enzyme is formed by two proteolytic cleavage steps subsequent to removal of its signal peptide: (1) an activation cleavage in the ER of the initial single-chain 49-kDa polypeptide into a 27-kDa alpha- and 19-kDa beta-subunit; (2) a cleavage in lysosomes which removes 10 amino acids from the C-terminus of the alpha-subunit without affecting enzyme activity.
8638940	10	85	theme	enzyme	1770:1775	arg1	Yield					1761:1765	Yield	1761:1765	Yield of enzyme for all mutants	1761:1791	Yield of enzyme for all mutants was increased in cells treated with brefeldin A.
8223648	5	0	theme	complex-type	508:519	arg1	oligosaccharides					521:536	complex-type oligosaccharides	508:536	complex-type oligosaccharides [Adolf	508:543	While natural IFN-omega 1 was shown to carry complex-type oligosaccharides [Adolf, G. R., Maurer-Fogy, I., Kalsner, I. & Cantell, K. (1990) J. Biol.
8223648	13	1	theme	biological	1481:1490	arg1	activity					1492:1499	the maximal biological activity	1469:1499	the maximal biological activity of human IFN-omega 1	1469:1520	This implies the importance of a complex-type glycosylation for the maximal biological activity of human IFN-omega 1.
8223648	12	2	theme	nonglycosylated	1376:1390	arg1	IFN-omega					1392:1400	glycosylated and nonglycosylated IFN-omega 1	1359:1402	glycosylated and nonglycosylated IFN-omega 1	1359:1402	Circular dichroism and fluorescence spectroscopy did not reveal any structural differences between glycosylated and nonglycosylated IFN-omega 1.
8223648	7	3	theme	core	763:766	arg1	oligosaccharide					768:782	only the core oligosaccharide	754:782	only the core oligosaccharide	754:782	265, 9290-9295], the insect cell produced protein which was demonstrated by lectin blot, mass spectroscopy and HPLC analysis to contain only the core oligosaccharide.
8223648	0	4	from	Expression	0:9	arg1	cells					46:50	Sf9 cells	42:50	Sf9 cells	42:50	Expression of human interferon omega 1 in Sf9 cells.
8223648	13	5	theme	glycosylation	1451:1463	arg1	importance					1422:1431	the importance	1418:1431	the importance of a complex-type glycosylation for the maximal biological activity of human IFN-omega 1	1418:1520	This implies the importance of a complex-type glycosylation for the maximal biological activity of human IFN-omega 1.
8223648	8	6	dep	Man	812:814	arg1	2[Fuc					850:854	2[Fuc	850:854	Man)2(GlcNAc)2[Fuc] and (Man)3(GlcNAc)2[Fuc	812:854	Two different structures, (Man)2(GlcNAc)2[Fuc] and (Man)3(GlcNAc)2[Fuc] were identified.
8223648	4	7	theme	rate	457:460	arg1	independent					427:437	independent	427:437	independent	427:437	The degree of glycosylation was independent of the expression rate.
8223648	4	7	theme	rate	457:460	arg1	degree					399:404	The degree	395:404	The degree of glycosylation	395:421	The degree of glycosylation was independent of the expression rate.
8223648	8	8	dep	structures	799:808	arg1	Man					837:839	(Man)3	836:841	(Man)3	836:841	Two different structures, (Man)2(GlcNAc)2[Fuc] and (Man)3(GlcNAc)2[Fuc] were identified.
8223648	8	8	dep	structures	799:808	arg1	structures					799:808	Two different structures	785:808	Two different structures, (Man)2(GlcNAc)2[Fuc] and (Man)3(GlcNAc)2[Fuc]	785:855	Two different structures, (Man)2(GlcNAc)2[Fuc] and (Man)3(GlcNAc)2[Fuc] were identified.
8223648	8	8	dep	structures	799:808	arg1	Man					812:814	Man)2	812:816	Man)2(GlcNAc)2[Fuc]	812:830	Two different structures, (Man)2(GlcNAc)2[Fuc] and (Man)3(GlcNAc)2[Fuc] were identified.
8223648	8	8	dep	structures	799:808	arg1	GlcNAc					843:848	GlcNAc	843:848	GlcNAc	843:848	Two different structures, (Man)2(GlcNAc)2[Fuc] and (Man)3(GlcNAc)2[Fuc] were identified.
8223648	8	8	dep	structures	799:808	arg1	GlcNAc					818:823	GlcNAc	818:823	GlcNAc	818:823	Two different structures, (Man)2(GlcNAc)2[Fuc] and (Man)3(GlcNAc)2[Fuc] were identified.
8223648	5	9	theme	natural	469:475	arg1	IFN-omega					477:485	natural IFN-omega 1	469:487	natural IFN-omega 1	469:487	While natural IFN-omega 1 was shown to carry complex-type oligosaccharides [Adolf, G. R., Maurer-Fogy, I., Kalsner, I. & Cantell, K. (1990) J. Biol.
8223648	11	10	theme	IFN-omega	1200:1208	arg1	activity					1188:1195	the activity	1184:1195	the activity of IFN-omega 1 produced by Sendai-virus-stimulated leukocytes	1184:1257	IFN-omega 1 expressed in S. frugiperda cells was shown to be partially truncated at the C-terminus by nine residues; its antiviral activity when glycosylated was significantly lower than the activity of IFN-omega 1 produced by Sendai-virus-stimulated leukocytes.
8223648	3	11	from	site	362:365	arg1	N-glycosylated					335:348	N-glycosylated	335:348	N-glycosylated	335:348	Half of the protein purified by immunoaffinity chromatography was shown to be N-glycosylated at the same site as the natural IFN-omega 1.
8223648	9	12	attach	-linked	923:929	arg1	saccharide					943:952	the core saccharide	934:952	the core saccharide	934:952	The fucosylation was identified to be (alpha 1-6)-linked to the core saccharide.
8223648	9	12	attach	-linked	923:929	arg2	-linked					923:929	-linked	923:929	-linked	923:929	The fucosylation was identified to be (alpha 1-6)-linked to the core saccharide.
8223648	9	12	attach	-linked	923:929	arg2	fucosylation					878:889	The fucosylation	874:889	The fucosylation	874:889	The fucosylation was identified to be (alpha 1-6)-linked to the core saccharide.
8223648	9	12	attach	-linked	923:929	arg2	alpha					913:917	alpha 1-6	913:921	alpha 1-6	913:921	The fucosylation was identified to be (alpha 1-6)-linked to the core saccharide.
8223648	13	13	theme	maximal	1473:1479	arg1	activity					1492:1499	the maximal biological activity	1469:1499	the maximal biological activity of human IFN-omega 1	1469:1520	This implies the importance of a complex-type glycosylation for the maximal biological activity of human IFN-omega 1.
8223648	11	14	theme	Sendai-virus-stimulated	1224:1246	arg1	leukocytes					1248:1257	Sendai-virus-stimulated leukocytes	1224:1257	Sendai-virus-stimulated leukocytes	1224:1257	IFN-omega 1 expressed in S. frugiperda cells was shown to be partially truncated at the C-terminus by nine residues; its antiviral activity when glycosylated was significantly lower than the activity of IFN-omega 1 produced by Sendai-virus-stimulated leukocytes.
8223648	2	15	theme	interferon	127:136	arg1	omega					138:142	Human interferon omega 1	121:144	Human interferon omega 1 (IFN-omega 1)	121:158	Human interferon omega 1 (IFN-omega 1) was expressed in Spodoptera frugiperda Sf9 insect cells using the baculovirus expression system.
8223648	2	15	theme	interferon	127:136	arg1	IFN-omega					147:155	IFN-omega 1	147:157	IFN-omega 1	147:157	Human interferon omega 1 (IFN-omega 1) was expressed in Spodoptera frugiperda Sf9 insect cells using the baculovirus expression system.
8223648	4	16	theme	expression	446:455	arg1	rate					457:460	the expression rate	442:460	the expression rate	442:460	The degree of glycosylation was independent of the expression rate.
8223648	7	17	dep	265	618:620	arg1	9290-9295					623:631	9290-9295	623:631	9290-9295	623:631	265, 9290-9295], the insect cell produced protein which was demonstrated by lectin blot, mass spectroscopy and HPLC analysis to contain only the core oligosaccharide.
8223648	1	18	theme	complex-type	69:80	arg1	glycosylation					91:103	complex-type N-linked glycosylation	69:103	complex-type N-linked glycosylation	69:103	No evidence for complex-type N-linked glycosylation or sialylation.
8223648	7	19	theme	HPLC	729:732	arg1	analysis					734:741	HPLC analysis	729:741	HPLC analysis	729:741	265, 9290-9295], the insect cell produced protein which was demonstrated by lectin blot, mass spectroscopy and HPLC analysis to contain only the core oligosaccharide.
8223648	12	20	gly	glycosylated	1359:1370	arg1	IFN-omega					1392:1400	glycosylated and nonglycosylated IFN-omega 1	1359:1402	glycosylated and nonglycosylated IFN-omega 1	1359:1402	Circular dichroism and fluorescence spectroscopy did not reveal any structural differences between glycosylated and nonglycosylated IFN-omega 1.
8223648	3	21	theme	same	357:360	arg1	site					362:365	the same site	353:365	the same site as the natural IFN-omega 1	353:392	Half of the protein purified by immunoaffinity chromatography was shown to be N-glycosylated at the same site as the natural IFN-omega 1.
8223648	7	22	theme	mass	707:710	arg1	spectroscopy					712:723	mass spectroscopy	707:723	mass spectroscopy	707:723	265, 9290-9295], the insect cell produced protein which was demonstrated by lectin blot, mass spectroscopy and HPLC analysis to contain only the core oligosaccharide.
8223648	13	23	theme	IFN-omega	1510:1518	arg1	activity					1492:1499	the maximal biological activity	1469:1499	the maximal biological activity of human IFN-omega 1	1469:1520	This implies the importance of a complex-type glycosylation for the maximal biological activity of human IFN-omega 1.
8223648	1	24	theme	N-linked	82:89	arg1	glycosylation					91:103	complex-type N-linked glycosylation	69:103	complex-type N-linked glycosylation	69:103	No evidence for complex-type N-linked glycosylation or sialylation.
8223648	8	25	theme	different	789:797	arg1	Man					837:839	(Man)3	836:841	(Man)3	836:841	Two different structures, (Man)2(GlcNAc)2[Fuc] and (Man)3(GlcNAc)2[Fuc] were identified.
8223648	8	25	theme	different	789:797	arg1	structures					799:808	Two different structures	785:808	Two different structures, (Man)2(GlcNAc)2[Fuc] and (Man)3(GlcNAc)2[Fuc]	785:855	Two different structures, (Man)2(GlcNAc)2[Fuc] and (Man)3(GlcNAc)2[Fuc] were identified.
8223648	8	25	theme	different	789:797	arg1	Man					812:814	Man)2	812:816	Man)2(GlcNAc)2[Fuc]	812:830	Two different structures, (Man)2(GlcNAc)2[Fuc] and (Man)3(GlcNAc)2[Fuc] were identified.
8223648	0	26	theme	human	14:18	arg1	omega					31:35	human interferon omega 1	14:37	human interferon omega 1	14:37	Expression of human interferon omega 1 in Sf9 cells.
8223648	7	27	theme	lectin	694:699	arg1	blot					701:704	lectin blot	694:704	lectin blot	694:704	265, 9290-9295], the insect cell produced protein which was demonstrated by lectin blot, mass spectroscopy and HPLC analysis to contain only the core oligosaccharide.
8223648	13	28	theme	complex-type	1438:1449	arg1	glycosylation					1451:1463	a complex-type glycosylation	1436:1463	a complex-type glycosylation	1436:1463	This implies the importance of a complex-type glycosylation for the maximal biological activity of human IFN-omega 1.
8223648	5	29	dep	shown	493:497	arg1	Biol					606:609	Biol	606:609	Biol	606:609	While natural IFN-omega 1 was shown to carry complex-type oligosaccharides [Adolf, G. R., Maurer-Fogy, I., Kalsner, I. & Cantell, K. (1990) J. Biol.
8223648	3	30	gly	N-glycosylated	335:348	arg1	Half					257:260	Half	257:260	Half of the protein purified by immunoaffinity chromatography	257:317	Half of the protein purified by immunoaffinity chromatography was shown to be N-glycosylated at the same site as the natural IFN-omega 1.
8223648	3	30	gly	N-glycosylated	335:348	arg2	site					362:365	the same site	353:365	the same site as the natural IFN-omega 1	353:392	Half of the protein purified by immunoaffinity chromatography was shown to be N-glycosylated at the same site as the natural IFN-omega 1.
8223648	12	31	theme	structural	1328:1337	arg1	differences					1339:1349	any structural differences	1324:1349	any structural differences between glycosylated and nonglycosylated IFN-omega 1	1324:1402	Circular dichroism and fluorescence spectroscopy did not reveal any structural differences between glycosylated and nonglycosylated IFN-omega 1.
8223648	0	32	theme	omega	31:35	arg1	Expression					0:9	Expression	0:9	Expression of human interferon omega 1 in Sf9 cells.	0:51	Expression of human interferon omega 1 in Sf9 cells.
8223648	11	33	theme	frugiperda	1025:1034	arg1	cells					1036:1040	S. frugiperda cells	1022:1040	S. frugiperda cells	1022:1040	IFN-omega 1 expressed in S. frugiperda cells was shown to be partially truncated at the C-terminus by nine residues; its antiviral activity when glycosylated was significantly lower than the activity of IFN-omega 1 produced by Sendai-virus-stimulated leukocytes.
8223648	12	34	theme	glycosylated	1359:1370	arg1	IFN-omega					1392:1400	glycosylated and nonglycosylated IFN-omega 1	1359:1402	glycosylated and nonglycosylated IFN-omega 1	1359:1402	Circular dichroism and fluorescence spectroscopy did not reveal any structural differences between glycosylated and nonglycosylated IFN-omega 1.
8223648	0	35	theme	interferon	20:29	arg1	omega					31:35	human interferon omega 1	14:37	human interferon omega 1	14:37	Expression of human interferon omega 1 in Sf9 cells.
8223648	12	36	theme	Circular	1260:1267	arg1	dichroism					1269:1277	Circular dichroism	1260:1277	Circular dichroism	1260:1277	Circular dichroism and fluorescence spectroscopy did not reveal any structural differences between glycosylated and nonglycosylated IFN-omega 1.
8223648	3	37	theme	natural	374:380	arg1	IFN-omega					382:390	the natural IFN-omega 1	370:392	the natural IFN-omega 1	370:392	Half of the protein purified by immunoaffinity chromatography was shown to be N-glycosylated at the same site as the natural IFN-omega 1.
8223648	10	38	theme	acid	962:965	arg1	residues					967:974	Sialic acid residues	955:974	Sialic acid residues	955:974	Sialic acid residues were clearly absent.
8223648	7	39	contain	contain	746:752	arg2	oligosaccharide					768:782	only the core oligosaccharide	754:782	only the core oligosaccharide	754:782	265, 9290-9295], the insect cell produced protein which was demonstrated by lectin blot, mass spectroscopy and HPLC analysis to contain only the core oligosaccharide.
8223648	7	39	contain	contain	746:752	arg1	protein					660:666	protein	660:666	protein which was demonstrated by lectin blot, mass spectroscopy and HPLC analysis to contain only the core oligosaccharide	660:782	265, 9290-9295], the insect cell produced protein which was demonstrated by lectin blot, mass spectroscopy and HPLC analysis to contain only the core oligosaccharide.
8223648	2	40	theme	insect	203:208	arg1	cells					210:214	Spodoptera frugiperda Sf9 insect cells	177:214	Spodoptera frugiperda Sf9 insect cells using the baculovirus expression system	177:254	Human interferon omega 1 (IFN-omega 1) was expressed in Spodoptera frugiperda Sf9 insect cells using the baculovirus expression system.
8223648	5	41	theme	[Adolf	538:543	arg1	oligosaccharides					521:536	complex-type oligosaccharides	508:536	complex-type oligosaccharides [Adolf	508:543	While natural IFN-omega 1 was shown to carry complex-type oligosaccharides [Adolf, G. R., Maurer-Fogy, I., Kalsner, I. & Cantell, K. (1990) J. Biol.
8223648	12	42	theme	fluorescence	1283:1294	arg1	spectroscopy					1296:1307	fluorescence spectroscopy	1283:1307	fluorescence spectroscopy	1283:1307	Circular dichroism and fluorescence spectroscopy did not reveal any structural differences between glycosylated and nonglycosylated IFN-omega 1.
8223648	10	43	theme	Sialic	955:960	arg1	residues					967:974	Sialic acid residues	955:974	Sialic acid residues	955:974	Sialic acid residues were clearly absent.
8223648	3	44	theme	immunoaffinity	289:302	arg1	chromatography					304:317	immunoaffinity chromatography	289:317	immunoaffinity chromatography	289:317	Half of the protein purified by immunoaffinity chromatography was shown to be N-glycosylated at the same site as the natural IFN-omega 1.
8223648	2	45	theme	frugiperda	188:197	arg1	cells					210:214	Spodoptera frugiperda Sf9 insect cells	177:214	Spodoptera frugiperda Sf9 insect cells using the baculovirus expression system	177:254	Human interferon omega 1 (IFN-omega 1) was expressed in Spodoptera frugiperda Sf9 insect cells using the baculovirus expression system.
8223648	2	46	theme	Sf9	199:201	arg1	cells					210:214	Spodoptera frugiperda Sf9 insect cells	177:214	Spodoptera frugiperda Sf9 insect cells using the baculovirus expression system	177:254	Human interferon omega 1 (IFN-omega 1) was expressed in Spodoptera frugiperda Sf9 insect cells using the baculovirus expression system.
8223648	9	47	theme	core	938:941	arg1	saccharide					943:952	the core saccharide	934:952	the core saccharide	934:952	The fucosylation was identified to be (alpha 1-6)-linked to the core saccharide.
8223648	3	48	theme	protein	269:275	arg1	Half					257:260	Half	257:260	Half of the protein purified by immunoaffinity chromatography	257:317	Half of the protein purified by immunoaffinity chromatography was shown to be N-glycosylated at the same site as the natural IFN-omega 1.
8223648	2	49	theme	Spodoptera	177:186	arg1	frugiperda					188:197	Spodoptera frugiperda	177:197	Spodoptera frugiperda Sf9 insect cells using the baculovirus expression system	177:254	Human interferon omega 1 (IFN-omega 1) was expressed in Spodoptera frugiperda Sf9 insect cells using the baculovirus expression system.
8223648	13	50	theme	human	1504:1508	arg1	IFN-omega					1510:1518	human IFN-omega 1	1504:1520	human IFN-omega 1	1504:1520	This implies the importance of a complex-type glycosylation for the maximal biological activity of human IFN-omega 1.
8223648	4	51	theme	glycosylation	409:421	arg1	independent					427:437	independent	427:437	independent	427:437	The degree of glycosylation was independent of the expression rate.
8223648	4	51	theme	glycosylation	409:421	arg1	degree					399:404	The degree	395:404	The degree of glycosylation	395:421	The degree of glycosylation was independent of the expression rate.
8223648	2	52	theme	expression	238:247	arg1	system					249:254	the baculovirus expression system	222:254	the baculovirus expression system	222:254	Human interferon omega 1 (IFN-omega 1) was expressed in Spodoptera frugiperda Sf9 insect cells using the baculovirus expression system.
8223648	1	53	link	N-linked	82:89	arg1	glycosylation					91:103	complex-type N-linked glycosylation	69:103	complex-type N-linked glycosylation	69:103	No evidence for complex-type N-linked glycosylation or sialylation.
8223648	2	54	theme	baculovirus	226:236	arg1	system					249:254	the baculovirus expression system	222:254	the baculovirus expression system	222:254	Human interferon omega 1 (IFN-omega 1) was expressed in Spodoptera frugiperda Sf9 insect cells using the baculovirus expression system.
8223648	9	55	dep	-linked	923:929	arg1	fucosylation					878:889	The fucosylation	874:889	The fucosylation	874:889	The fucosylation was identified to be (alpha 1-6)-linked to the core saccharide.
8223648	9	55	dep	-linked	923:929	arg1	alpha					913:917	alpha 1-6	913:921	alpha 1-6	913:921	The fucosylation was identified to be (alpha 1-6)-linked to the core saccharide.
8223648	9	55	dep	-linked	923:929	arg1	-linked					923:929	-linked	923:929	-linked	923:929	The fucosylation was identified to be (alpha 1-6)-linked to the core saccharide.
8223648	8	56	dep	GlcNAc	818:823	arg1	2[Fuc					825:829	2[Fuc	825:829	2[Fuc	825:829	Two different structures, (Man)2(GlcNAc)2[Fuc] and (Man)3(GlcNAc)2[Fuc] were identified.
8223648	7	57	theme	insect	639:644	arg1	cell					646:649	the insect cell	635:649	the insect cell	635:649	265, 9290-9295], the insect cell produced protein which was demonstrated by lectin blot, mass spectroscopy and HPLC analysis to contain only the core oligosaccharide.
8223648	7	57	theme	insect	639:644	arg1	265					618:620	265	618:620	265	618:620	265, 9290-9295], the insect cell produced protein which was demonstrated by lectin blot, mass spectroscopy and HPLC analysis to contain only the core oligosaccharide.
8223648	0	58	theme	Sf9	42:44	arg1	cells					46:50	Sf9 cells	42:50	Sf9 cells	42:50	Expression of human interferon omega 1 in Sf9 cells.
8223648	2	59	theme	Human	121:125	arg1	omega					138:142	Human interferon omega 1	121:144	Human interferon omega 1 (IFN-omega 1)	121:158	Human interferon omega 1 (IFN-omega 1) was expressed in Spodoptera frugiperda Sf9 insect cells using the baculovirus expression system.
8223648	2	59	theme	Human	121:125	arg1	IFN-omega					147:155	IFN-omega 1	147:157	IFN-omega 1	147:157	Human interferon omega 1 (IFN-omega 1) was expressed in Spodoptera frugiperda Sf9 insect cells using the baculovirus expression system.
8223648	11	60	theme	antiviral	1118:1126	arg1	activity					1128:1135	its antiviral activity	1114:1135	its antiviral activity when glycosylated	1114:1153	IFN-omega 1 expressed in S. frugiperda cells was shown to be partially truncated at the C-terminus by nine residues; its antiviral activity when glycosylated was significantly lower than the activity of IFN-omega 1 produced by Sendai-virus-stimulated leukocytes.
8223648	11	61	theme	S.	1022:1023	arg1	cells					1036:1040	S. frugiperda cells	1022:1040	S. frugiperda cells	1022:1040	IFN-omega 1 expressed in S. frugiperda cells was shown to be partially truncated at the C-terminus by nine residues; its antiviral activity when glycosylated was significantly lower than the activity of IFN-omega 1 produced by Sendai-virus-stimulated leukocytes.
8223648	5	62	contain	carry	502:506	arg1	IFN-omega					477:485	natural IFN-omega 1	469:487	natural IFN-omega 1	469:487	While natural IFN-omega 1 was shown to carry complex-type oligosaccharides [Adolf, G. R., Maurer-Fogy, I., Kalsner, I. & Cantell, K. (1990) J. Biol.
8223648	5	62	contain	carry	502:506	arg2	oligosaccharides					521:536	complex-type oligosaccharides	508:536	complex-type oligosaccharides [Adolf	508:543	While natural IFN-omega 1 was shown to carry complex-type oligosaccharides [Adolf, G. R., Maurer-Fogy, I., Kalsner, I. & Cantell, K. (1990) J. Biol.
8223648	12	63	gly	nonglycosylated	1376:1390	arg1	IFN-omega					1392:1400	glycosylated and nonglycosylated IFN-omega 1	1359:1402	glycosylated and nonglycosylated IFN-omega 1	1359:1402	Circular dichroism and fluorescence spectroscopy did not reveal any structural differences between glycosylated and nonglycosylated IFN-omega 1.
17395588	6	0	theme	spectral	1043:1050	arg1	analysis					1052:1059	mass spectral analysis	1038:1059	mass spectral analysis	1038:1059	Although mass spectral analysis did not unambiguously identify the relevant peptide from TSR1, metabolic labeling of cells expressing TSR1 and the cysteine-rich module led to incorporation of [(3)H]fucose into this construct.
17395588	8	1	theme	exogenous	1612:1620	arg1	l-fucose					1622:1629	exogenous l-fucose	1612:1629	exogenous l-fucose	1612:1629	Similarly, expression of punctin-1 in Lec-13 cells that are deficient in conversion of GDP-mannose to GDP-fucose substantially decreased the levels of secreted protein, which were restored upon culture in the presence of exogenous l-fucose.
17395588	10	2	from	role	1796:1799	arg1	biosynthesis					1847:1858	the biosynthesis	1843:1858	the biosynthesis of punctin-1	1843:1871	Taken together, the data define a critical role for N-glycosylation and O-fucosylation in the biosynthesis of punctin-1.
17395588	11	3	theme	regulatory	2042:2051	arg1	consequences					2053:2064	possible regulatory consequences	2033:2064	possible regulatory consequences	2033:2064	From a broad perspective, these data suggest that O-fucosylation may be a widespread post-translational modification in members of the ADAMTS superfamily with possible regulatory consequences.
17395588	6	4	theme	cysteine-rich	1176:1188	arg1	module					1190:1195	the cysteine-rich module	1172:1195	the cysteine-rich module	1172:1195	Although mass spectral analysis did not unambiguously identify the relevant peptide from TSR1, metabolic labeling of cells expressing TSR1 and the cysteine-rich module led to incorporation of [(3)H]fucose into this construct.
17395588	7	5	theme	punctin-1	1380:1388	arg1	levels					1361:1366	significantly decreased levels	1337:1366	significantly decreased levels of secreted punctin-1	1337:1388	Mutation of the putative modified Ser/Thr residues in TSR2, TSR3, and TSR4 led to significantly decreased levels of secreted punctin-1.
17395588	6	6	theme	metabolic	1124:1132	arg1	labeling					1134:1141	metabolic labeling	1124:1141	metabolic labeling of cells expressing TSR1 and the cysteine-rich module	1124:1195	Although mass spectral analysis did not unambiguously identify the relevant peptide from TSR1, metabolic labeling of cells expressing TSR1 and the cysteine-rich module led to incorporation of [(3)H]fucose into this construct.
17395588	5	7	dep	disaccharide	996:1007	arg1	TSR3					1016:1019	TSR3	1016:1019	TSR3	1016:1019	On mass spectrometric analysis of tryptic peptides from recombinant secreted human punctin-1, the appropriate peptides from TSR2, TSR3, and TSR4 were found to bear either a fucose monosaccharide (TSR3, TSR4) or a fucose-glucose disaccharide (TSR2, TSR3, TSR4).
17395588	5	7	dep	disaccharide	996:1007	arg1	TSR2					1010:1013	TSR2	1010:1013	TSR2	1010:1013	On mass spectrometric analysis of tryptic peptides from recombinant secreted human punctin-1, the appropriate peptides from TSR2, TSR3, and TSR4 were found to bear either a fucose monosaccharide (TSR3, TSR4) or a fucose-glucose disaccharide (TSR2, TSR3, TSR4).
17395588	5	7	dep	disaccharide	996:1007	arg1	TSR4					1022:1025	TSR4	1022:1025	TSR4	1022:1025	On mass spectrometric analysis of tryptic peptides from recombinant secreted human punctin-1, the appropriate peptides from TSR2, TSR3, and TSR4 were found to bear either a fucose monosaccharide (TSR3, TSR4) or a fucose-glucose disaccharide (TSR2, TSR3, TSR4).
17395588	5	8	theme	appropriate	866:876	arg1	peptides					878:885	the appropriate peptides	862:885	the appropriate peptides from TSR2, TSR3, and TSR4	862:911	On mass spectrometric analysis of tryptic peptides from recombinant secreted human punctin-1, the appropriate peptides from TSR2, TSR3, and TSR4 were found to bear either a fucose monosaccharide (TSR3, TSR4) or a fucose-glucose disaccharide (TSR2, TSR3, TSR4).
17395588	6	9	dep	fucose	1227:1232	arg1	3					1223:1223	3	1223:1223	3	1223:1223	Although mass spectral analysis did not unambiguously identify the relevant peptide from TSR1, metabolic labeling of cells expressing TSR1 and the cysteine-rich module led to incorporation of [(3)H]fucose into this construct.
17395588	4	10	theme	Cys-Xaa	677:683	arg1	-Xaa					687:690	sequence Cys-Xaa(1)-Xaa(2)-	668:694	the sequence Cys-Xaa(1)-Xaa(2)-(Ser/Thr)-Cys-Xaa-Xaa-Gly (where the fucosylated residue is underlined)	664:765	Previously, O-fucosylation on Ser or Thr mediated by the endoplasmic reticulum-localized enzyme protein-O-fucosyltransferase 2 (POFUT2) was described for TSRs of thrombospondin-1, properdin, and F-spondin within the sequence Cys-Xaa(1)-Xaa(2)-(Ser/Thr)-Cys-Xaa-Xaa-Gly (where the fucosylated residue is underlined).
17395588	4	10	theme	Cys-Xaa	677:683	arg1	Ser/Thr					696:702	Ser/Thr	696:702	Ser/Thr	696:702	Previously, O-fucosylation on Ser or Thr mediated by the endoplasmic reticulum-localized enzyme protein-O-fucosyltransferase 2 (POFUT2) was described for TSRs of thrombospondin-1, properdin, and F-spondin within the sequence Cys-Xaa(1)-Xaa(2)-(Ser/Thr)-Cys-Xaa-Xaa-Gly (where the fucosylated residue is underlined).
17395588	11	11	theme	widespread	1948:1957	arg1	O-fucosylation					1924:1937	O-fucosylation	1924:1937	O-fucosylation	1924:1937	From a broad perspective, these data suggest that O-fucosylation may be a widespread post-translational modification in members of the ADAMTS superfamily with possible regulatory consequences.
17395588	11	11	theme	widespread	1948:1957	arg1	modification					1978:1989	a widespread post-translational modification	1946:1989	a widespread post-translational modification in members of the ADAMTS superfamily with possible regulatory consequences	1946:2064	From a broad perspective, these data suggest that O-fucosylation may be a widespread post-translational modification in members of the ADAMTS superfamily with possible regulatory consequences.
17395588	5	12	theme	human	845:849	arg1	punctin-1					851:859	recombinant secreted human punctin-1	824:859	recombinant secreted human punctin-1	824:859	On mass spectrometric analysis of tryptic peptides from recombinant secreted human punctin-1, the appropriate peptides from TSR2, TSR3, and TSR4 were found to bear either a fucose monosaccharide (TSR3, TSR4) or a fucose-glucose disaccharide (TSR2, TSR3, TSR4).
17395588	8	13	theme	protein	1551:1557	arg1	levels					1532:1537	the levels	1528:1537	the levels of secreted protein, which were restored upon culture in the presence of exogenous l-fucose	1528:1629	Similarly, expression of punctin-1 in Lec-13 cells that are deficient in conversion of GDP-mannose to GDP-fucose substantially decreased the levels of secreted protein, which were restored upon culture in the presence of exogenous l-fucose.
17395588	5	14	from	punctin-1	851:859	arg1	analysis					790:797	mass spectrometric analysis	771:797	mass spectrometric analysis of tryptic peptides from recombinant secreted human punctin-1	771:859	On mass spectrometric analysis of tryptic peptides from recombinant secreted human punctin-1, the appropriate peptides from TSR2, TSR3, and TSR4 were found to bear either a fucose monosaccharide (TSR3, TSR4) or a fucose-glucose disaccharide (TSR2, TSR3, TSR4).
17395588	5	14	from	punctin-1	851:859	arg1	peptides					810:817	tryptic peptides	802:817	tryptic peptides from recombinant secreted human punctin-1	802:859	On mass spectrometric analysis of tryptic peptides from recombinant secreted human punctin-1, the appropriate peptides from TSR2, TSR3, and TSR4 were found to bear either a fucose monosaccharide (TSR3, TSR4) or a fucose-glucose disaccharide (TSR2, TSR3, TSR4).
17395588	7	15	theme	residues	1297:1304	arg1	Mutation					1255:1262	Mutation	1255:1262	Mutation of the putative modified Ser/Thr residues in TSR2, TSR3, and TSR4	1255:1328	Mutation of the putative modified Ser/Thr residues in TSR2, TSR3, and TSR4 led to significantly decreased levels of secreted punctin-1.
17395588	7	16	from	TSR3	1315:1318	arg1	Mutation					1255:1262	Mutation	1255:1262	Mutation of the putative modified Ser/Thr residues in TSR2, TSR3, and TSR4	1255:1328	Mutation of the putative modified Ser/Thr residues in TSR2, TSR3, and TSR4 led to significantly decreased levels of secreted punctin-1.
17395588	11	17	theme	ADAMTS	2009:2014	arg1	superfamily					2016:2026	the ADAMTS superfamily	2005:2026	the ADAMTS superfamily	2005:2026	From a broad perspective, these data suggest that O-fucosylation may be a widespread post-translational modification in members of the ADAMTS superfamily with possible regulatory consequences.
17395588	7	18	theme	modified	1280:1287	arg1	residues					1297:1304	the putative modified Ser/Thr residues	1267:1304	the putative modified Ser/Thr residues in TSR2, TSR3, and TSR4	1267:1328	Mutation of the putative modified Ser/Thr residues in TSR2, TSR3, and TSR4 led to significantly decreased levels of secreted punctin-1.
17395588	2	19	theme	common	284:289	arg1	presence					306:313	the presence	302:313	the presence of one or more thrombospondin type-1 repeats (TSRs) within a characteristic modular organization	302:410	Their common feature is the presence of one or more thrombospondin type-1 repeats (TSRs) within a characteristic modular organization.
17395588	2	19	theme	common	284:289	arg1	feature					291:297	Their common feature	278:297	Their common feature	278:297	Their common feature is the presence of one or more thrombospondin type-1 repeats (TSRs) within a characteristic modular organization.
17395588	9	20	theme	single	1661:1666	arg1	oligosaccharide					1677:1691	the single N-linked oligosaccharide	1657:1691	the single N-linked oligosaccharide	1657:1691	In addition, mutation of the single N-linked oligosaccharide in punctin-1 led to decreased levels of secreted punctin-1.
17395588	5	21	from	analysis	790:797	arg1	punctin-1					851:859	recombinant secreted human punctin-1	824:859	recombinant secreted human punctin-1	824:859	On mass spectrometric analysis of tryptic peptides from recombinant secreted human punctin-1, the appropriate peptides from TSR2, TSR3, and TSR4 were found to bear either a fucose monosaccharide (TSR3, TSR4) or a fucose-glucose disaccharide (TSR2, TSR3, TSR4).
17395588	5	22	theme	recombinant	824:834	arg1	punctin-1					851:859	recombinant secreted human punctin-1	824:859	recombinant secreted human punctin-1	824:859	On mass spectrometric analysis of tryptic peptides from recombinant secreted human punctin-1, the appropriate peptides from TSR2, TSR3, and TSR4 were found to bear either a fucose monosaccharide (TSR3, TSR4) or a fucose-glucose disaccharide (TSR2, TSR3, TSR4).
17395588	1	23	theme	several	169:175	arg1	metalloproteases					177:192	several metalloproteases	169:192	several metalloproteases (ADAMTS proteases) as well as ADAMTS-like molecules that lack proteolytic activity	169:275	The ADAMTS superfamily contains several metalloproteases (ADAMTS proteases) as well as ADAMTS-like molecules that lack proteolytic activity.
17395588	1	23	theme	several	169:175	arg1	proteases					202:210	ADAMTS proteases	195:210	ADAMTS proteases	195:210	The ADAMTS superfamily contains several metalloproteases (ADAMTS proteases) as well as ADAMTS-like molecules that lack proteolytic activity.
17395588	9	24	from	mutation	1645:1652	arg1	punctin-1					1696:1704	punctin-1	1696:1704	punctin-1	1696:1704	In addition, mutation of the single N-linked oligosaccharide in punctin-1 led to decreased levels of secreted punctin-1.
17395588	9	25	theme	oligosaccharide	1677:1691	arg1	mutation					1645:1652	mutation	1645:1652	mutation of the single N-linked oligosaccharide in punctin-1	1645:1704	In addition, mutation of the single N-linked oligosaccharide in punctin-1 led to decreased levels of secreted punctin-1.
17395588	4	26	theme	reticulum-localized	521:539	arg1	POFUT2					580:585	the endoplasmic reticulum-localized enzyme protein-O-fucosyltransferase 2 (POFUT2)	505:586	the endoplasmic reticulum-localized enzyme protein-O-fucosyltransferase 2 (POFUT2)	505:586	Previously, O-fucosylation on Ser or Thr mediated by the endoplasmic reticulum-localized enzyme protein-O-fucosyltransferase 2 (POFUT2) was described for TSRs of thrombospondin-1, properdin, and F-spondin within the sequence Cys-Xaa(1)-Xaa(2)-(Ser/Thr)-Cys-Xaa-Xaa-Gly (where the fucosylated residue is underlined).
17395588	5	27	located	found	918:922	arg1	analysis					790:797	mass spectrometric analysis	771:797	mass spectrometric analysis of tryptic peptides from recombinant secreted human punctin-1	771:859	On mass spectrometric analysis of tryptic peptides from recombinant secreted human punctin-1, the appropriate peptides from TSR2, TSR3, and TSR4 were found to bear either a fucose monosaccharide (TSR3, TSR4) or a fucose-glucose disaccharide (TSR2, TSR3, TSR4).
17395588	5	27	located	found	918:922	arg2	peptides					878:885	the appropriate peptides	862:885	the appropriate peptides from TSR2, TSR3, and TSR4	862:911	On mass spectrometric analysis of tryptic peptides from recombinant secreted human punctin-1, the appropriate peptides from TSR2, TSR3, and TSR4 were found to bear either a fucose monosaccharide (TSR3, TSR4) or a fucose-glucose disaccharide (TSR2, TSR3, TSR4).
17395588	5	28	from	TSR3	898:901	arg1	peptides					878:885	the appropriate peptides	862:885	the appropriate peptides from TSR2, TSR3, and TSR4	862:911	On mass spectrometric analysis of tryptic peptides from recombinant secreted human punctin-1, the appropriate peptides from TSR2, TSR3, and TSR4 were found to bear either a fucose monosaccharide (TSR3, TSR4) or a fucose-glucose disaccharide (TSR2, TSR3, TSR4).
17395588	0	29	from	O-fucosylation	0:13	arg1	ADAMTS-like-1/punctin-1					51:73	ADAMTS-like-1/punctin-1	51:73	ADAMTS-like-1/punctin-1	51:73	O-fucosylation of thrombospondin type 1 repeats in ADAMTS-like-1/punctin-1 regulates secretion: implications for the ADAMTS superfamily.
17395588	4	30	gly	fucosylated	732:742	arg1	residue					744:750	the fucosylated residue	728:750	the fucosylated residue	728:750	Previously, O-fucosylation on Ser or Thr mediated by the endoplasmic reticulum-localized enzyme protein-O-fucosyltransferase 2 (POFUT2) was described for TSRs of thrombospondin-1, properdin, and F-spondin within the sequence Cys-Xaa(1)-Xaa(2)-(Ser/Thr)-Cys-Xaa-Xaa-Gly (where the fucosylated residue is underlined).
17395588	5	31	from	TSR2	892:895	arg1	peptides					878:885	the appropriate peptides	862:885	the appropriate peptides from TSR2, TSR3, and TSR4	862:911	On mass spectrometric analysis of tryptic peptides from recombinant secreted human punctin-1, the appropriate peptides from TSR2, TSR3, and TSR4 were found to bear either a fucose monosaccharide (TSR3, TSR4) or a fucose-glucose disaccharide (TSR2, TSR3, TSR4).
17395588	0	32	theme	ADAMTS	117:122	arg1	superfamily					124:134	the ADAMTS superfamily	113:134	the ADAMTS superfamily	113:134	O-fucosylation of thrombospondin type 1 repeats in ADAMTS-like-1/punctin-1 regulates secretion: implications for the ADAMTS superfamily.
17395588	0	33	theme	repeats	40:46	arg1	O-fucosylation					0:13	O-fucosylation	0:13	O-fucosylation of thrombospondin type 1 repeats in ADAMTS-like-1/punctin-1	0:73	O-fucosylation of thrombospondin type 1 repeats in ADAMTS-like-1/punctin-1 regulates secretion: implications for the ADAMTS superfamily.
17395588	8	34	from	deficient	1451:1459	arg1	conversion					1464:1473	conversion	1464:1473	conversion of GDP-mannose to GDP-fucose	1464:1502	Similarly, expression of punctin-1 in Lec-13 cells that are deficient in conversion of GDP-mannose to GDP-fucose substantially decreased the levels of secreted protein, which were restored upon culture in the presence of exogenous l-fucose.
17395588	4	35	theme	fucosylated	732:742	arg1	residue					744:750	the fucosylated residue	728:750	the fucosylated residue	728:750	Previously, O-fucosylation on Ser or Thr mediated by the endoplasmic reticulum-localized enzyme protein-O-fucosyltransferase 2 (POFUT2) was described for TSRs of thrombospondin-1, properdin, and F-spondin within the sequence Cys-Xaa(1)-Xaa(2)-(Ser/Thr)-Cys-Xaa-Xaa-Gly (where the fucosylated residue is underlined).
17395588	5	36	theme	peptides	810:817	arg1	analysis					790:797	mass spectrometric analysis	771:797	mass spectrometric analysis of tryptic peptides from recombinant secreted human punctin-1	771:859	On mass spectrometric analysis of tryptic peptides from recombinant secreted human punctin-1, the appropriate peptides from TSR2, TSR3, and TSR4 were found to bear either a fucose monosaccharide (TSR3, TSR4) or a fucose-glucose disaccharide (TSR2, TSR3, TSR4).
17395588	7	37	from	residues	1297:1304	arg1	TSR3					1315:1318	TSR3	1315:1318	TSR3	1315:1318	Mutation of the putative modified Ser/Thr residues in TSR2, TSR3, and TSR4 led to significantly decreased levels of secreted punctin-1.
17395588	7	37	from	residues	1297:1304	arg1	TSR4					1325:1328	TSR4	1325:1328	TSR4	1325:1328	Mutation of the putative modified Ser/Thr residues in TSR2, TSR3, and TSR4 led to significantly decreased levels of secreted punctin-1.
17395588	7	37	from	residues	1297:1304	arg1	TSR2					1309:1312	TSR2	1309:1312	TSR2	1309:1312	Mutation of the putative modified Ser/Thr residues in TSR2, TSR3, and TSR4 led to significantly decreased levels of secreted punctin-1.
17395588	9	38	theme	secreted	1733:1740	arg1	punctin-1					1742:1750	secreted punctin-1	1733:1750	secreted punctin-1	1733:1750	In addition, mutation of the single N-linked oligosaccharide in punctin-1 led to decreased levels of secreted punctin-1.
17395588	0	39	theme	thrombospondin	18:31	arg1	repeats					40:46	thrombospondin type 1 repeats	18:46	thrombospondin type 1 repeats	18:46	O-fucosylation of thrombospondin type 1 repeats in ADAMTS-like-1/punctin-1 regulates secretion: implications for the ADAMTS superfamily.
17395588	7	40	from	TSR2	1309:1312	arg1	Mutation					1255:1262	Mutation	1255:1262	Mutation of the putative modified Ser/Thr residues in TSR2, TSR3, and TSR4	1255:1328	Mutation of the putative modified Ser/Thr residues in TSR2, TSR3, and TSR4 led to significantly decreased levels of secreted punctin-1.
17395588	4	41	theme	-Xaa	687:690	arg1	-Cys-Xaa-Xaa-Gly					704:719	the sequence Cys-Xaa(1)-Xaa(2)-(Ser/Thr)-Cys-Xaa-Xaa-Gly	664:719	the sequence Cys-Xaa(1)-Xaa(2)-(Ser/Thr)-Cys-Xaa-Xaa-Gly (where the fucosylated residue is underlined)	664:765	Previously, O-fucosylation on Ser or Thr mediated by the endoplasmic reticulum-localized enzyme protein-O-fucosyltransferase 2 (POFUT2) was described for TSRs of thrombospondin-1, properdin, and F-spondin within the sequence Cys-Xaa(1)-Xaa(2)-(Ser/Thr)-Cys-Xaa-Xaa-Gly (where the fucosylated residue is underlined).
17395588	5	42	theme	spectrometric	776:788	arg1	analysis					790:797	mass spectrometric analysis	771:797	mass spectrometric analysis of tryptic peptides from recombinant secreted human punctin-1	771:859	On mass spectrometric analysis of tryptic peptides from recombinant secreted human punctin-1, the appropriate peptides from TSR2, TSR3, and TSR4 were found to bear either a fucose monosaccharide (TSR3, TSR4) or a fucose-glucose disaccharide (TSR2, TSR3, TSR4).
17395588	5	43	theme	fucose-glucose	981:994	arg1	disaccharide					996:1007	a fucose-glucose disaccharide	979:1007	a fucose-glucose disaccharide (TSR2, TSR3, TSR4)	979:1026	On mass spectrometric analysis of tryptic peptides from recombinant secreted human punctin-1, the appropriate peptides from TSR2, TSR3, and TSR4 were found to bear either a fucose monosaccharide (TSR3, TSR4) or a fucose-glucose disaccharide (TSR2, TSR3, TSR4).
17395588	4	44	theme	enzyme	541:546	arg1	POFUT2					580:585	the endoplasmic reticulum-localized enzyme protein-O-fucosyltransferase 2 (POFUT2)	505:586	the endoplasmic reticulum-localized enzyme protein-O-fucosyltransferase 2 (POFUT2)	505:586	Previously, O-fucosylation on Ser or Thr mediated by the endoplasmic reticulum-localized enzyme protein-O-fucosyltransferase 2 (POFUT2) was described for TSRs of thrombospondin-1, properdin, and F-spondin within the sequence Cys-Xaa(1)-Xaa(2)-(Ser/Thr)-Cys-Xaa-Xaa-Gly (where the fucosylated residue is underlined).
17395588	7	45	theme	putative	1271:1278	arg1	residues					1297:1304	the putative modified Ser/Thr residues	1267:1304	the putative modified Ser/Thr residues in TSR2, TSR3, and TSR4	1267:1328	Mutation of the putative modified Ser/Thr residues in TSR2, TSR3, and TSR4 led to significantly decreased levels of secreted punctin-1.
17395588	2	46	theme	repeats	352:358	arg1	presence					306:313	the presence	302:313	the presence of one or more thrombospondin type-1 repeats (TSRs) within a characteristic modular organization	302:410	Their common feature is the presence of one or more thrombospondin type-1 repeats (TSRs) within a characteristic modular organization.
17395588	2	46	theme	repeats	352:358	arg1	feature					291:297	Their common feature	278:297	Their common feature	278:297	Their common feature is the presence of one or more thrombospondin type-1 repeats (TSRs) within a characteristic modular organization.
17395588	10	47	theme	critical	1787:1794	arg1	role					1796:1799	a critical role	1785:1799	a critical role for N-glycosylation and O-fucosylation in the biosynthesis of punctin-1	1785:1871	Taken together, the data define a critical role for N-glycosylation and O-fucosylation in the biosynthesis of punctin-1.
17395588	2	48	theme	characteristic	376:389	arg1	organization					399:410	a characteristic modular organization	374:410	a characteristic modular organization	374:410	Their common feature is the presence of one or more thrombospondin type-1 repeats (TSRs) within a characteristic modular organization.
17395588	1	49	theme	proteolytic	256:266	arg1	activity					268:275	proteolytic activity	256:275	proteolytic activity	256:275	The ADAMTS superfamily contains several metalloproteases (ADAMTS proteases) as well as ADAMTS-like molecules that lack proteolytic activity.
17395588	7	50	from	Mutation	1255:1262	arg1	TSR3					1315:1318	TSR3	1315:1318	TSR3	1315:1318	Mutation of the putative modified Ser/Thr residues in TSR2, TSR3, and TSR4 led to significantly decreased levels of secreted punctin-1.
17395588	7	50	from	Mutation	1255:1262	arg1	TSR4					1325:1328	TSR4	1325:1328	TSR4	1325:1328	Mutation of the putative modified Ser/Thr residues in TSR2, TSR3, and TSR4 led to significantly decreased levels of secreted punctin-1.
17395588	7	50	from	Mutation	1255:1262	arg1	TSR2					1309:1312	TSR2	1309:1312	TSR2	1309:1312	Mutation of the putative modified Ser/Thr residues in TSR2, TSR3, and TSR4 led to significantly decreased levels of secreted punctin-1.
17395588	6	51	theme	H	1225:1225	arg1	fucose					1227:1232	[(3)H]fucose	1221:1232	[(3)H]fucose	1221:1232	Although mass spectral analysis did not unambiguously identify the relevant peptide from TSR1, metabolic labeling of cells expressing TSR1 and the cysteine-rich module led to incorporation of [(3)H]fucose into this construct.
17395588	3	52	contain	has	437:439	arg2	TSRs					446:449	four TSRs	441:449	four TSRs	441:449	ADAMTS like-1/punctin-1 has four TSRs.
17395588	3	52	contain	has	437:439	arg1	like-1/punctin-1					420:435	ADAMTS like-1/punctin-1	413:435	ADAMTS like-1/punctin-1	413:435	ADAMTS like-1/punctin-1 has four TSRs.
17395588	6	53	theme	mass	1038:1041	arg1	analysis					1052:1059	mass spectral analysis	1038:1059	mass spectral analysis	1038:1059	Although mass spectral analysis did not unambiguously identify the relevant peptide from TSR1, metabolic labeling of cells expressing TSR1 and the cysteine-rich module led to incorporation of [(3)H]fucose into this construct.
17395588	4	54	theme	thrombospondin-1	614:629	arg1	TSRs					606:609	TSRs	606:609	TSRs of thrombospondin-1, properdin, and F-spondin within the sequence Cys-Xaa(1)-Xaa(2)-(Ser/Thr)-Cys-Xaa-Xaa-Gly (where the fucosylated residue is underlined)	606:765	Previously, O-fucosylation on Ser or Thr mediated by the endoplasmic reticulum-localized enzyme protein-O-fucosyltransferase 2 (POFUT2) was described for TSRs of thrombospondin-1, properdin, and F-spondin within the sequence Cys-Xaa(1)-Xaa(2)-(Ser/Thr)-Cys-Xaa-Xaa-Gly (where the fucosylated residue is underlined).
17395588	8	55	from	conversion	1464:1473	arg1	deficient					1451:1459	deficient	1451:1459	deficient	1451:1459	Similarly, expression of punctin-1 in Lec-13 cells that are deficient in conversion of GDP-mannose to GDP-fucose substantially decreased the levels of secreted protein, which were restored upon culture in the presence of exogenous l-fucose.
17395588	4	56	gly	O-fucosylation	464:477	arg1	Ser					482:484	Ser	482:484	Ser	482:484	Previously, O-fucosylation on Ser or Thr mediated by the endoplasmic reticulum-localized enzyme protein-O-fucosyltransferase 2 (POFUT2) was described for TSRs of thrombospondin-1, properdin, and F-spondin within the sequence Cys-Xaa(1)-Xaa(2)-(Ser/Thr)-Cys-Xaa-Xaa-Gly (where the fucosylated residue is underlined).
17395588	4	56	gly	O-fucosylation	464:477	arg1	Thr					489:491	Thr	489:491	Thr	489:491	Previously, O-fucosylation on Ser or Thr mediated by the endoplasmic reticulum-localized enzyme protein-O-fucosyltransferase 2 (POFUT2) was described for TSRs of thrombospondin-1, properdin, and F-spondin within the sequence Cys-Xaa(1)-Xaa(2)-(Ser/Thr)-Cys-Xaa-Xaa-Gly (where the fucosylated residue is underlined).
17395588	11	57	theme	post-translational	1959:1976	arg1	O-fucosylation					1924:1937	O-fucosylation	1924:1937	O-fucosylation	1924:1937	From a broad perspective, these data suggest that O-fucosylation may be a widespread post-translational modification in members of the ADAMTS superfamily with possible regulatory consequences.
17395588	11	57	theme	post-translational	1959:1976	arg1	modification					1978:1989	a widespread post-translational modification	1946:1989	a widespread post-translational modification in members of the ADAMTS superfamily with possible regulatory consequences	1946:2064	From a broad perspective, these data suggest that O-fucosylation may be a widespread post-translational modification in members of the ADAMTS superfamily with possible regulatory consequences.
17395588	7	58	theme	secreted	1371:1378	arg1	punctin-1					1380:1388	secreted punctin-1	1371:1388	secreted punctin-1	1371:1388	Mutation of the putative modified Ser/Thr residues in TSR2, TSR3, and TSR4 led to significantly decreased levels of secreted punctin-1.
17395588	7	59	theme	decreased	1351:1359	arg1	levels					1361:1366	significantly decreased levels	1337:1366	significantly decreased levels of secreted punctin-1	1337:1388	Mutation of the putative modified Ser/Thr residues in TSR2, TSR3, and TSR4 led to significantly decreased levels of secreted punctin-1.
17395588	4	60	theme	properdin	632:640	arg1	TSRs					606:609	TSRs	606:609	TSRs of thrombospondin-1, properdin, and F-spondin within the sequence Cys-Xaa(1)-Xaa(2)-(Ser/Thr)-Cys-Xaa-Xaa-Gly (where the fucosylated residue is underlined)	606:765	Previously, O-fucosylation on Ser or Thr mediated by the endoplasmic reticulum-localized enzyme protein-O-fucosyltransferase 2 (POFUT2) was described for TSRs of thrombospondin-1, properdin, and F-spondin within the sequence Cys-Xaa(1)-Xaa(2)-(Ser/Thr)-Cys-Xaa-Xaa-Gly (where the fucosylated residue is underlined).
17395588	10	61	theme	punctin-1	1863:1871	arg1	biosynthesis					1847:1858	the biosynthesis	1843:1858	the biosynthesis of punctin-1	1843:1871	Taken together, the data define a critical role for N-glycosylation and O-fucosylation in the biosynthesis of punctin-1.
17395588	8	62	theme	l-fucose	1622:1629	arg1	presence					1600:1607	the presence	1596:1607	the presence of exogenous l-fucose	1596:1629	Similarly, expression of punctin-1 in Lec-13 cells that are deficient in conversion of GDP-mannose to GDP-fucose substantially decreased the levels of secreted protein, which were restored upon culture in the presence of exogenous l-fucose.
17395588	1	63	theme	ADAMTS	195:200	arg1	metalloproteases					177:192	several metalloproteases	169:192	several metalloproteases (ADAMTS proteases) as well as ADAMTS-like molecules that lack proteolytic activity	169:275	The ADAMTS superfamily contains several metalloproteases (ADAMTS proteases) as well as ADAMTS-like molecules that lack proteolytic activity.
17395588	1	63	theme	ADAMTS	195:200	arg1	proteases					202:210	ADAMTS proteases	195:210	ADAMTS proteases	195:210	The ADAMTS superfamily contains several metalloproteases (ADAMTS proteases) as well as ADAMTS-like molecules that lack proteolytic activity.
17395588	1	64	contain	contains	160:167	arg2	molecules					236:244	ADAMTS-like molecules	224:244	several metalloproteases (ADAMTS proteases) as well as ADAMTS-like molecules that lack proteolytic activity	169:275	The ADAMTS superfamily contains several metalloproteases (ADAMTS proteases) as well as ADAMTS-like molecules that lack proteolytic activity.
17395588	1	64	contain	contains	160:167	arg2	metalloproteases					177:192	several metalloproteases	169:192	several metalloproteases (ADAMTS proteases) as well as ADAMTS-like molecules that lack proteolytic activity	169:275	The ADAMTS superfamily contains several metalloproteases (ADAMTS proteases) as well as ADAMTS-like molecules that lack proteolytic activity.
17395588	1	64	contain	contains	160:167	arg1	superfamily					148:158	The ADAMTS superfamily	137:158	The ADAMTS superfamily	137:158	The ADAMTS superfamily contains several metalloproteases (ADAMTS proteases) as well as ADAMTS-like molecules that lack proteolytic activity.
17395588	1	64	contain	contains	160:167	arg2	proteases					202:210	ADAMTS proteases	195:210	ADAMTS proteases	195:210	The ADAMTS superfamily contains several metalloproteases (ADAMTS proteases) as well as ADAMTS-like molecules that lack proteolytic activity.
17395588	2	65	theme	thrombospondin	330:343	arg1	TSRs					361:364	TSRs	361:364	TSRs	361:364	Their common feature is the presence of one or more thrombospondin type-1 repeats (TSRs) within a characteristic modular organization.
17395588	2	65	theme	thrombospondin	330:343	arg1	repeats					352:358	one or more thrombospondin type-1 repeats	318:358	one or more thrombospondin type-1 repeats (TSRs)	318:365	Their common feature is the presence of one or more thrombospondin type-1 repeats (TSRs) within a characteristic modular organization.
17395588	5	66	theme	secreted	836:843	arg1	punctin-1					851:859	recombinant secreted human punctin-1	824:859	recombinant secreted human punctin-1	824:859	On mass spectrometric analysis of tryptic peptides from recombinant secreted human punctin-1, the appropriate peptides from TSR2, TSR3, and TSR4 were found to bear either a fucose monosaccharide (TSR3, TSR4) or a fucose-glucose disaccharide (TSR2, TSR3, TSR4).
17395588	6	67	theme	relevant	1096:1103	arg1	peptide					1105:1111	the relevant peptide	1092:1111	the relevant peptide from TSR1	1092:1121	Although mass spectral analysis did not unambiguously identify the relevant peptide from TSR1, metabolic labeling of cells expressing TSR1 and the cysteine-rich module led to incorporation of [(3)H]fucose into this construct.
17395588	5	68	contain	bear	927:930	arg2	monosaccharide					948:961	a fucose monosaccharide	939:961	a fucose monosaccharide (TSR3, TSR4)	939:974	On mass spectrometric analysis of tryptic peptides from recombinant secreted human punctin-1, the appropriate peptides from TSR2, TSR3, and TSR4 were found to bear either a fucose monosaccharide (TSR3, TSR4) or a fucose-glucose disaccharide (TSR2, TSR3, TSR4).
17395588	5	68	contain	bear	927:930	arg2	disaccharide					996:1007	a fucose-glucose disaccharide	979:1007	a fucose-glucose disaccharide (TSR2, TSR3, TSR4)	979:1026	On mass spectrometric analysis of tryptic peptides from recombinant secreted human punctin-1, the appropriate peptides from TSR2, TSR3, and TSR4 were found to bear either a fucose monosaccharide (TSR3, TSR4) or a fucose-glucose disaccharide (TSR2, TSR3, TSR4).
17395588	5	68	contain	bear	927:930	arg1	peptides					878:885	the appropriate peptides	862:885	the appropriate peptides from TSR2, TSR3, and TSR4	862:911	On mass spectrometric analysis of tryptic peptides from recombinant secreted human punctin-1, the appropriate peptides from TSR2, TSR3, and TSR4 were found to bear either a fucose monosaccharide (TSR3, TSR4) or a fucose-glucose disaccharide (TSR2, TSR3, TSR4).
17395588	4	69	theme	sequence	668:675	arg1	-Xaa					687:690	sequence Cys-Xaa(1)-Xaa(2)-	668:694	the sequence Cys-Xaa(1)-Xaa(2)-(Ser/Thr)-Cys-Xaa-Xaa-Gly (where the fucosylated residue is underlined)	664:765	Previously, O-fucosylation on Ser or Thr mediated by the endoplasmic reticulum-localized enzyme protein-O-fucosyltransferase 2 (POFUT2) was described for TSRs of thrombospondin-1, properdin, and F-spondin within the sequence Cys-Xaa(1)-Xaa(2)-(Ser/Thr)-Cys-Xaa-Xaa-Gly (where the fucosylated residue is underlined).
17395588	4	69	theme	sequence	668:675	arg1	Ser/Thr					696:702	Ser/Thr	696:702	Ser/Thr	696:702	Previously, O-fucosylation on Ser or Thr mediated by the endoplasmic reticulum-localized enzyme protein-O-fucosyltransferase 2 (POFUT2) was described for TSRs of thrombospondin-1, properdin, and F-spondin within the sequence Cys-Xaa(1)-Xaa(2)-(Ser/Thr)-Cys-Xaa-Xaa-Gly (where the fucosylated residue is underlined).
17395588	11	70	theme	broad	1881:1885	arg1	perspective					1887:1897	a broad perspective	1879:1897	a broad perspective	1879:1897	From a broad perspective, these data suggest that O-fucosylation may be a widespread post-translational modification in members of the ADAMTS superfamily with possible regulatory consequences.
17395588	1	71	theme	ADAMTS-like	224:234	arg1	molecules					236:244	ADAMTS-like molecules	224:244	several metalloproteases (ADAMTS proteases) as well as ADAMTS-like molecules that lack proteolytic activity	169:275	The ADAMTS superfamily contains several metalloproteases (ADAMTS proteases) as well as ADAMTS-like molecules that lack proteolytic activity.
17395588	4	72	from	O-fucosylation	464:477	arg1	Ser					482:484	Ser	482:484	Ser	482:484	Previously, O-fucosylation on Ser or Thr mediated by the endoplasmic reticulum-localized enzyme protein-O-fucosyltransferase 2 (POFUT2) was described for TSRs of thrombospondin-1, properdin, and F-spondin within the sequence Cys-Xaa(1)-Xaa(2)-(Ser/Thr)-Cys-Xaa-Xaa-Gly (where the fucosylated residue is underlined).
17395588	4	72	from	O-fucosylation	464:477	arg1	Thr					489:491	Thr	489:491	Thr	489:491	Previously, O-fucosylation on Ser or Thr mediated by the endoplasmic reticulum-localized enzyme protein-O-fucosyltransferase 2 (POFUT2) was described for TSRs of thrombospondin-1, properdin, and F-spondin within the sequence Cys-Xaa(1)-Xaa(2)-(Ser/Thr)-Cys-Xaa-Xaa-Gly (where the fucosylated residue is underlined).
17395588	4	73	theme	protein-O-fucosyltransferase	548:575	arg1	POFUT2					580:585	the endoplasmic reticulum-localized enzyme protein-O-fucosyltransferase 2 (POFUT2)	505:586	the endoplasmic reticulum-localized enzyme protein-O-fucosyltransferase 2 (POFUT2)	505:586	Previously, O-fucosylation on Ser or Thr mediated by the endoplasmic reticulum-localized enzyme protein-O-fucosyltransferase 2 (POFUT2) was described for TSRs of thrombospondin-1, properdin, and F-spondin within the sequence Cys-Xaa(1)-Xaa(2)-(Ser/Thr)-Cys-Xaa-Xaa-Gly (where the fucosylated residue is underlined).
17395588	11	74	theme	possible	2033:2040	arg1	consequences					2053:2064	possible regulatory consequences	2033:2064	possible regulatory consequences	2033:2064	From a broad perspective, these data suggest that O-fucosylation may be a widespread post-translational modification in members of the ADAMTS superfamily with possible regulatory consequences.
17395588	6	75	theme	fucose	1227:1232	arg1	incorporation					1204:1216	incorporation	1204:1216	incorporation of [(3)H]fucose into this construct	1204:1252	Although mass spectral analysis did not unambiguously identify the relevant peptide from TSR1, metabolic labeling of cells expressing TSR1 and the cysteine-rich module led to incorporation of [(3)H]fucose into this construct.
17395588	1	76	theme	ADAMTS	141:146	arg1	superfamily					148:158	The ADAMTS superfamily	137:158	The ADAMTS superfamily	137:158	The ADAMTS superfamily contains several metalloproteases (ADAMTS proteases) as well as ADAMTS-like molecules that lack proteolytic activity.
17395588	11	77	theme	superfamily	2016:2026	arg1	members					1994:2000	members	1994:2000	members of the ADAMTS superfamily	1994:2026	From a broad perspective, these data suggest that O-fucosylation may be a widespread post-translational modification in members of the ADAMTS superfamily with possible regulatory consequences.
17395588	7	78	theme	Ser/Thr	1289:1295	arg1	residues					1297:1304	the putative modified Ser/Thr residues	1267:1304	the putative modified Ser/Thr residues in TSR2, TSR3, and TSR4	1267:1328	Mutation of the putative modified Ser/Thr residues in TSR2, TSR3, and TSR4 led to significantly decreased levels of secreted punctin-1.
17395588	5	79	dep	monosaccharide	948:961	arg1	TSR4					970:973	TSR4	970:973	TSR4	970:973	On mass spectrometric analysis of tryptic peptides from recombinant secreted human punctin-1, the appropriate peptides from TSR2, TSR3, and TSR4 were found to bear either a fucose monosaccharide (TSR3, TSR4) or a fucose-glucose disaccharide (TSR2, TSR3, TSR4).
17395588	5	79	dep	monosaccharide	948:961	arg1	TSR3					964:967	TSR3	964:967	TSR3	964:967	On mass spectrometric analysis of tryptic peptides from recombinant secreted human punctin-1, the appropriate peptides from TSR2, TSR3, and TSR4 were found to bear either a fucose monosaccharide (TSR3, TSR4) or a fucose-glucose disaccharide (TSR2, TSR3, TSR4).
17395588	7	80	from	TSR4	1325:1328	arg1	Mutation					1255:1262	Mutation	1255:1262	Mutation of the putative modified Ser/Thr residues in TSR2, TSR3, and TSR4	1255:1328	Mutation of the putative modified Ser/Thr residues in TSR2, TSR3, and TSR4 led to significantly decreased levels of secreted punctin-1.
17395588	9	81	theme	N-linked	1668:1675	arg1	oligosaccharide					1677:1691	the single N-linked oligosaccharide	1657:1691	the single N-linked oligosaccharide	1657:1691	In addition, mutation of the single N-linked oligosaccharide in punctin-1 led to decreased levels of secreted punctin-1.
17395588	8	82	theme	punctin-1	1416:1424	arg1	expression					1402:1411	expression	1402:1411	expression of punctin-1 in Lec-13 cells that are deficient in conversion of GDP-mannose to GDP-fucose	1402:1502	Similarly, expression of punctin-1 in Lec-13 cells that are deficient in conversion of GDP-mannose to GDP-fucose substantially decreased the levels of secreted protein, which were restored upon culture in the presence of exogenous l-fucose.
17395588	6	83	theme	cells	1146:1150	arg1	labeling					1134:1141	metabolic labeling	1124:1141	metabolic labeling of cells expressing TSR1 and the cysteine-rich module	1124:1195	Although mass spectral analysis did not unambiguously identify the relevant peptide from TSR1, metabolic labeling of cells expressing TSR1 and the cysteine-rich module led to incorporation of [(3)H]fucose into this construct.
17395588	8	84	theme	Lec-13	1429:1434	arg1	cells					1436:1440	Lec-13 cells	1429:1440	Lec-13 cells that are deficient in conversion of GDP-mannose to GDP-fucose	1429:1502	Similarly, expression of punctin-1 in Lec-13 cells that are deficient in conversion of GDP-mannose to GDP-fucose substantially decreased the levels of secreted protein, which were restored upon culture in the presence of exogenous l-fucose.
17395588	8	85	from	expression	1402:1411	arg1	cells					1436:1440	Lec-13 cells	1429:1440	Lec-13 cells that are deficient in conversion of GDP-mannose to GDP-fucose	1429:1502	Similarly, expression of punctin-1 in Lec-13 cells that are deficient in conversion of GDP-mannose to GDP-fucose substantially decreased the levels of secreted protein, which were restored upon culture in the presence of exogenous l-fucose.
17395588	5	86	theme	fucose	941:946	arg1	monosaccharide					948:961	a fucose monosaccharide	939:961	a fucose monosaccharide (TSR3, TSR4)	939:974	On mass spectrometric analysis of tryptic peptides from recombinant secreted human punctin-1, the appropriate peptides from TSR2, TSR3, and TSR4 were found to bear either a fucose monosaccharide (TSR3, TSR4) or a fucose-glucose disaccharide (TSR2, TSR3, TSR4).
17395588	9	87	link	N-linked	1668:1675	arg1	oligosaccharide					1677:1691	the single N-linked oligosaccharide	1657:1691	the single N-linked oligosaccharide	1657:1691	In addition, mutation of the single N-linked oligosaccharide in punctin-1 led to decreased levels of secreted punctin-1.
17395588	11	88	with	modification	1978:1989	arg1	consequences					2053:2064	possible regulatory consequences	2033:2064	possible regulatory consequences	2033:2064	From a broad perspective, these data suggest that O-fucosylation may be a widespread post-translational modification in members of the ADAMTS superfamily with possible regulatory consequences.
17395588	9	89	theme	decreased	1713:1721	arg1	levels					1723:1728	decreased levels	1713:1728	decreased levels of secreted punctin-1	1713:1750	In addition, mutation of the single N-linked oligosaccharide in punctin-1 led to decreased levels of secreted punctin-1.
17395588	4	90	theme	endoplasmic	509:519	arg1	POFUT2					580:585	the endoplasmic reticulum-localized enzyme protein-O-fucosyltransferase 2 (POFUT2)	505:586	the endoplasmic reticulum-localized enzyme protein-O-fucosyltransferase 2 (POFUT2)	505:586	Previously, O-fucosylation on Ser or Thr mediated by the endoplasmic reticulum-localized enzyme protein-O-fucosyltransferase 2 (POFUT2) was described for TSRs of thrombospondin-1, properdin, and F-spondin within the sequence Cys-Xaa(1)-Xaa(2)-(Ser/Thr)-Cys-Xaa-Xaa-Gly (where the fucosylated residue is underlined).
17395588	5	91	theme	tryptic	802:808	arg1	peptides					810:817	tryptic peptides	802:817	tryptic peptides from recombinant secreted human punctin-1	802:859	On mass spectrometric analysis of tryptic peptides from recombinant secreted human punctin-1, the appropriate peptides from TSR2, TSR3, and TSR4 were found to bear either a fucose monosaccharide (TSR3, TSR4) or a fucose-glucose disaccharide (TSR2, TSR3, TSR4).
17395588	3	92	theme	ADAMTS	413:418	arg1	like-1/punctin-1					420:435	ADAMTS like-1/punctin-1	413:435	ADAMTS like-1/punctin-1	413:435	ADAMTS like-1/punctin-1 has four TSRs.
17395588	2	93	theme	modular	391:397	arg1	organization					399:410	a characteristic modular organization	374:410	a characteristic modular organization	374:410	Their common feature is the presence of one or more thrombospondin type-1 repeats (TSRs) within a characteristic modular organization.
17395588	0	94	theme	type	33:36	arg1	repeats					40:46	thrombospondin type 1 repeats	18:46	thrombospondin type 1 repeats	18:46	O-fucosylation of thrombospondin type 1 repeats in ADAMTS-like-1/punctin-1 regulates secretion: implications for the ADAMTS superfamily.
17395588	5	95	from	TSR4	908:911	arg1	peptides					878:885	the appropriate peptides	862:885	the appropriate peptides from TSR2, TSR3, and TSR4	862:911	On mass spectrometric analysis of tryptic peptides from recombinant secreted human punctin-1, the appropriate peptides from TSR2, TSR3, and TSR4 were found to bear either a fucose monosaccharide (TSR3, TSR4) or a fucose-glucose disaccharide (TSR2, TSR3, TSR4).
17395588	0	96	dep	secretion	85:93	arg1	implications					96:107	implications	96:107	secretion: implications for the ADAMTS superfamily	85:134	O-fucosylation of thrombospondin type 1 repeats in ADAMTS-like-1/punctin-1 regulates secretion: implications for the ADAMTS superfamily.
17395588	9	97	theme	punctin-1	1742:1750	arg1	levels					1723:1728	decreased levels	1713:1728	decreased levels of secreted punctin-1	1713:1750	In addition, mutation of the single N-linked oligosaccharide in punctin-1 led to decreased levels of secreted punctin-1.
17395588	8	98	theme	GDP-mannose	1478:1488	arg1	conversion					1464:1473	conversion	1464:1473	conversion of GDP-mannose to GDP-fucose	1464:1502	Similarly, expression of punctin-1 in Lec-13 cells that are deficient in conversion of GDP-mannose to GDP-fucose substantially decreased the levels of secreted protein, which were restored upon culture in the presence of exogenous l-fucose.
17395588	6	99	from	TSR1	1118:1121	arg1	peptide					1105:1111	the relevant peptide	1092:1111	the relevant peptide from TSR1	1092:1121	Although mass spectral analysis did not unambiguously identify the relevant peptide from TSR1, metabolic labeling of cells expressing TSR1 and the cysteine-rich module led to incorporation of [(3)H]fucose into this construct.
17395588	5	100	theme	mass	771:774	arg1	analysis					790:797	mass spectrometric analysis	771:797	mass spectrometric analysis of tryptic peptides from recombinant secreted human punctin-1	771:859	On mass spectrometric analysis of tryptic peptides from recombinant secreted human punctin-1, the appropriate peptides from TSR2, TSR3, and TSR4 were found to bear either a fucose monosaccharide (TSR3, TSR4) or a fucose-glucose disaccharide (TSR2, TSR3, TSR4).
17395588	0	101	gly	O-fucosylation	0:13	arg1	repeats					40:46	thrombospondin type 1 repeats	18:46	thrombospondin type 1 repeats	18:46	O-fucosylation of thrombospondin type 1 repeats in ADAMTS-like-1/punctin-1 regulates secretion: implications for the ADAMTS superfamily.
17395588	0	101	gly	O-fucosylation	0:13	arg1	ADAMTS-like-1/punctin-1					51:73	ADAMTS-like-1/punctin-1	51:73	ADAMTS-like-1/punctin-1	51:73	O-fucosylation of thrombospondin type 1 repeats in ADAMTS-like-1/punctin-1 regulates secretion: implications for the ADAMTS superfamily.
17395588	4	102	theme	F-spondin	647:655	arg1	TSRs					606:609	TSRs	606:609	TSRs of thrombospondin-1, properdin, and F-spondin within the sequence Cys-Xaa(1)-Xaa(2)-(Ser/Thr)-Cys-Xaa-Xaa-Gly (where the fucosylated residue is underlined)	606:765	Previously, O-fucosylation on Ser or Thr mediated by the endoplasmic reticulum-localized enzyme protein-O-fucosyltransferase 2 (POFUT2) was described for TSRs of thrombospondin-1, properdin, and F-spondin within the sequence Cys-Xaa(1)-Xaa(2)-(Ser/Thr)-Cys-Xaa-Xaa-Gly (where the fucosylated residue is underlined).
17395588	2	103	theme	type-1	345:350	arg1	TSRs					361:364	TSRs	361:364	TSRs	361:364	Their common feature is the presence of one or more thrombospondin type-1 repeats (TSRs) within a characteristic modular organization.
17395588	2	103	theme	type-1	345:350	arg1	repeats					352:358	one or more thrombospondin type-1 repeats	318:358	one or more thrombospondin type-1 repeats (TSRs)	318:365	Their common feature is the presence of one or more thrombospondin type-1 repeats (TSRs) within a characteristic modular organization.
17395588	4	104	dep	-Xaa	687:690	arg1	1					685:685	1	685:685	1	685:685	Previously, O-fucosylation on Ser or Thr mediated by the endoplasmic reticulum-localized enzyme protein-O-fucosyltransferase 2 (POFUT2) was described for TSRs of thrombospondin-1, properdin, and F-spondin within the sequence Cys-Xaa(1)-Xaa(2)-(Ser/Thr)-Cys-Xaa-Xaa-Gly (where the fucosylated residue is underlined).
17395588	11	105	from	modification	1978:1989	arg1	members					1994:2000	members	1994:2000	members of the ADAMTS superfamily	1994:2026	From a broad perspective, these data suggest that O-fucosylation may be a widespread post-translational modification in members of the ADAMTS superfamily with possible regulatory consequences.
17395588	8	106	theme	secreted	1542:1549	arg1	protein					1551:1557	secreted protein	1542:1557	secreted protein	1542:1557	Similarly, expression of punctin-1 in Lec-13 cells that are deficient in conversion of GDP-mannose to GDP-fucose substantially decreased the levels of secreted protein, which were restored upon culture in the presence of exogenous l-fucose.
12093813	4	0	theme	cell	943:946	arg1	vesicles					957:964	inside-out and right-side-out red cell membrane vesicles	909:964	vesicles	957:964	Moreover, immunoadsorption studies, using inside-out and right-side-out red cell membrane vesicles as competing antigen, demonstrated that the C- and N-terminal ends of hUT-B1 are oriented intracellularly.
12093813	9	1	theme	urea	2026:2029	arg1	family					2043:2048	the urea transporter family	2022:2048	the urea transporter family	2022:2048	Altogether, these antigenic, topologic, and functional properties might have implications into the physiology of hUT-B1 and other members of the urea transporter family.
12093813	6	2	theme	C-terminal	1333:1342	arg1	deletion					1344:1351	C-terminal deletion	1333:1351	C-terminal deletion (residues 360-389)	1333:1370	Conversely, the transport function was not affected by the JK*A/JK*B polymorphism, C-terminal deletion (residues 360-389), or mutation of the extracellular N-glycosylation consensus site and remains poorly para-chloromercuribenzene sulfonate (pCMBS)-sensitive.
12093813	6	2	theme	C-terminal	1333:1342	arg1	residues					1354:1361	residues 360-389	1354:1369	residues 360-389	1354:1369	Conversely, the transport function was not affected by the JK*A/JK*B polymorphism, C-terminal deletion (residues 360-389), or mutation of the extracellular N-glycosylation consensus site and remains poorly para-chloromercuribenzene sulfonate (pCMBS)-sensitive.
12093813	1	3	theme	other	206:210	arg1	tissues					212:218	other tissues	206:218	other tissues	206:218	The Kidd (JK) blood group locus encodes the urea transporter hUT-B1, which is expressed on human red blood cells and other tissues.
12093813	2	4	theme	stable	521:526	arg1	clones					528:533	stable clones	521:533	stable clones that expressed the Jk(a) or Jk(b) antigens, respectively, thus providing the first direct demonstration that the hUT-B1 gene encodes the Kidd blood group antigens	521:696	The common JK*A/JK*B blood group polymorphism is caused by a single nucleotide transition G838A changing Asp-280 to Asn-280 on the polypeptide, and transfection of erythroleukemic K562 cells with hUT-B1 cDNAs carrying either the G838 or the A838 nucleotide substitutions resulted in the isolation of stable clones that expressed the Jk(a) or Jk(b) antigens, respectively, thus providing the first direct demonstration that the hUT-B1 gene encodes the Kidd blood group antigens.
12093813	9	5	theme	family	2043:2048	arg1	hUT-B1					1994:1999	hUT-B1	1994:1999	hUT-B1	1994:1999	Altogether, these antigenic, topologic, and functional properties might have implications into the physiology of hUT-B1 and other members of the urea transporter family.
12093813	9	5	theme	family	2043:2048	arg1	members					2011:2017	other members	2005:2017	other members of the urea transporter family	2005:2048	Altogether, these antigenic, topologic, and functional properties might have implications into the physiology of hUT-B1 and other members of the urea transporter family.
12093813	2	6	theme	JK	232:233	arg1	polymorphism					254:265	The common JK*A/JK*B blood group polymorphism	221:265	The common JK*A/JK*B blood group polymorphism	221:265	The common JK*A/JK*B blood group polymorphism is caused by a single nucleotide transition G838A changing Asp-280 to Asn-280 on the polypeptide, and transfection of erythroleukemic K562 cells with hUT-B1 cDNAs carrying either the G838 or the A838 nucleotide substitutions resulted in the isolation of stable clones that expressed the Jk(a) or Jk(b) antigens, respectively, thus providing the first direct demonstration that the hUT-B1 gene encodes the Kidd blood group antigens.
12093813	6	7	theme	site	1432:1435	arg1	deletion					1344:1351	C-terminal deletion	1333:1351	C-terminal deletion (residues 360-389)	1333:1370	Conversely, the transport function was not affected by the JK*A/JK*B polymorphism, C-terminal deletion (residues 360-389), or mutation of the extracellular N-glycosylation consensus site and remains poorly para-chloromercuribenzene sulfonate (pCMBS)-sensitive.
12093813	6	7	theme	site	1432:1435	arg1	mutation					1376:1383	mutation	1376:1383	mutation of the extracellular N-glycosylation consensus site	1376:1435	Conversely, the transport function was not affected by the JK*A/JK*B polymorphism, C-terminal deletion (residues 360-389), or mutation of the extracellular N-glycosylation consensus site and remains poorly para-chloromercuribenzene sulfonate (pCMBS)-sensitive.
12093813	6	7	theme	site	1432:1435	arg1	residues					1354:1361	residues 360-389	1354:1369	residues 360-389	1354:1369	Conversely, the transport function was not affected by the JK*A/JK*B polymorphism, C-terminal deletion (residues 360-389), or mutation of the extracellular N-glycosylation consensus site and remains poorly para-chloromercuribenzene sulfonate (pCMBS)-sensitive.
12093813	6	7	theme	site	1432:1435	arg1	polymorphism					1319:1330	the JK*A/JK*B polymorphism	1305:1330	the JK*A/JK*B polymorphism	1305:1330	Conversely, the transport function was not affected by the JK*A/JK*B polymorphism, C-terminal deletion (residues 360-389), or mutation of the extracellular N-glycosylation consensus site and remains poorly para-chloromercuribenzene sulfonate (pCMBS)-sensitive.
12093813	5	8	theme	Xenopus	1125:1131	arg1	oocytes					1133:1139	Xenopus oocytes	1125:1139	Xenopus oocytes	1125:1139	Mutagenesis and functional studies by expression in Xenopus oocytes revealed that both cysteines Cys-25 and Cys-30 (but not alone) are essential for plasma membrane addressing.
12093813	4	9	theme	N-terminal	1017:1026	arg1	ends					1028:1031	N-terminal ends	1017:1031	N-terminal ends	1017:1031	Moreover, immunoadsorption studies, using inside-out and right-side-out red cell membrane vesicles as competing antigen, demonstrated that the C- and N-terminal ends of hUT-B1 are oriented intracellularly.
12093813	3	10	attach	attached	811:818	arg1	chain					849:853	the single N-linked sugar chain	823:853	the single N-linked sugar chain	823:853	In addition, immunochemical analysis of red blood cells demonstrated that hUT-B1 also exhibits ABO determinants attached to the single N-linked sugar chain at Asn-211.
12093813	3	10	attach	attached	811:818	arg3	Asn-211					858:864	Asn-211	858:864	Asn-211	858:864	In addition, immunochemical analysis of red blood cells demonstrated that hUT-B1 also exhibits ABO determinants attached to the single N-linked sugar chain at Asn-211.
12093813	3	10	attach	attached	811:818	arg2	determinants					798:809	ABO determinants	794:809	ABO determinants attached to the single N-linked sugar chain at Asn-211	794:864	In addition, immunochemical analysis of red blood cells demonstrated that hUT-B1 also exhibits ABO determinants attached to the single N-linked sugar chain at Asn-211.
12093813	6	11	theme	N-glycosylation	1406:1420	arg1	site					1432:1435	the extracellular N-glycosylation consensus site	1388:1435	the extracellular N-glycosylation consensus site	1388:1435	Conversely, the transport function was not affected by the JK*A/JK*B polymorphism, C-terminal deletion (residues 360-389), or mutation of the extracellular N-glycosylation consensus site and remains poorly para-chloromercuribenzene sulfonate (pCMBS)-sensitive.
12093813	1	12	theme	transporter	138:148	arg1	hUT-B1					150:155	the urea transporter hUT-B1	129:155	the urea transporter hUT-B1	129:155	The Kidd (JK) blood group locus encodes the urea transporter hUT-B1, which is expressed on human red blood cells and other tissues.
12093813	1	12	theme	transporter	138:148	arg1	locus					115:119	The Kidd (JK) blood group locus	89:119	The Kidd (JK) blood group locus	89:119	The Kidd (JK) blood group locus encodes the urea transporter hUT-B1, which is expressed on human red blood cells and other tissues.
12093813	2	13	theme	B	240:240	arg1	polymorphism					254:265	The common JK*A/JK*B blood group polymorphism	221:265	The common JK*A/JK*B blood group polymorphism	221:265	The common JK*A/JK*B blood group polymorphism is caused by a single nucleotide transition G838A changing Asp-280 to Asn-280 on the polypeptide, and transfection of erythroleukemic K562 cells with hUT-B1 cDNAs carrying either the G838 or the A838 nucleotide substitutions resulted in the isolation of stable clones that expressed the Jk(a) or Jk(b) antigens, respectively, thus providing the first direct demonstration that the hUT-B1 gene encodes the Kidd blood group antigens.
12093813	7	14	theme	stopped	1541:1547	arg1	scattering					1560:1569	stopped flow light scattering	1541:1569	stopped flow light scattering using Jk-K562 transfectants	1541:1597	However, transport studies by stopped flow light scattering using Jk-K562 transfectants demonstrated that the hUT-B1-mediated urea transport is pCMBS-sensitive in an erythroid context, as reported previously for the transporter of human red blood cells.
12093813	5	15	dep	Cys-25	1170:1175	arg1	alone					1197:1201	alone	1197:1201	alone	1197:1201	Mutagenesis and functional studies by expression in Xenopus oocytes revealed that both cysteines Cys-25 and Cys-30 (but not alone) are essential for plasma membrane addressing.
12093813	3	16	theme	N-linked	834:841	arg1	chain					849:853	the single N-linked sugar chain	823:853	the single N-linked sugar chain	823:853	In addition, immunochemical analysis of red blood cells demonstrated that hUT-B1 also exhibits ABO determinants attached to the single N-linked sugar chain at Asn-211.
12093813	2	17	theme	A/JK	235:238	arg1	polymorphism					254:265	The common JK*A/JK*B blood group polymorphism	221:265	The common JK*A/JK*B blood group polymorphism	221:265	The common JK*A/JK*B blood group polymorphism is caused by a single nucleotide transition G838A changing Asp-280 to Asn-280 on the polypeptide, and transfection of erythroleukemic K562 cells with hUT-B1 cDNAs carrying either the G838 or the A838 nucleotide substitutions resulted in the isolation of stable clones that expressed the Jk(a) or Jk(b) antigens, respectively, thus providing the first direct demonstration that the hUT-B1 gene encodes the Kidd blood group antigens.
12093813	5	18	from	expression	1111:1120	arg1	oocytes					1133:1139	Xenopus oocytes	1125:1139	Xenopus oocytes	1125:1139	Mutagenesis and functional studies by expression in Xenopus oocytes revealed that both cysteines Cys-25 and Cys-30 (but not alone) are essential for plasma membrane addressing.
12093813	6	19	theme	B	1317:1317	arg1	polymorphism					1319:1330	the JK*A/JK*B polymorphism	1305:1330	the JK*A/JK*B polymorphism	1305:1330	Conversely, the transport function was not affected by the JK*A/JK*B polymorphism, C-terminal deletion (residues 360-389), or mutation of the extracellular N-glycosylation consensus site and remains poorly para-chloromercuribenzene sulfonate (pCMBS)-sensitive.
12093813	2	20	with	transfection	369:380	arg1	cDNAs					424:428	hUT-B1 cDNAs	417:428	hUT-B1 cDNAs carrying either the G838 or the A838 nucleotide substitutions	417:490	The common JK*A/JK*B blood group polymorphism is caused by a single nucleotide transition G838A changing Asp-280 to Asn-280 on the polypeptide, and transfection of erythroleukemic K562 cells with hUT-B1 cDNAs carrying either the G838 or the A838 nucleotide substitutions resulted in the isolation of stable clones that expressed the Jk(a) or Jk(b) antigens, respectively, thus providing the first direct demonstration that the hUT-B1 gene encodes the Kidd blood group antigens.
12093813	1	21	theme	JK	99:100	arg1	hUT-B1					150:155	the urea transporter hUT-B1	129:155	the urea transporter hUT-B1	129:155	The Kidd (JK) blood group locus encodes the urea transporter hUT-B1, which is expressed on human red blood cells and other tissues.
12093813	1	21	theme	JK	99:100	arg1	locus					115:119	The Kidd (JK) blood group locus	89:119	The Kidd (JK) blood group locus	89:119	The Kidd (JK) blood group locus encodes the urea transporter hUT-B1, which is expressed on human red blood cells and other tissues.
12093813	3	22	theme	red	739:741	arg1	cells					749:753	red blood cells	739:753	red blood cells	739:753	In addition, immunochemical analysis of red blood cells demonstrated that hUT-B1 also exhibits ABO determinants attached to the single N-linked sugar chain at Asn-211.
12093813	6	23	theme	para-chloromercuribenzene	1456:1480	arg1	pCMBS					1493:1497	pCMBS	1493:1497	pCMBS	1493:1497	Conversely, the transport function was not affected by the JK*A/JK*B polymorphism, C-terminal deletion (residues 360-389), or mutation of the extracellular N-glycosylation consensus site and remains poorly para-chloromercuribenzene sulfonate (pCMBS)-sensitive.
12093813	6	23	theme	para-chloromercuribenzene	1456:1480	arg1	sulfonate					1482:1490	para-chloromercuribenzene sulfonate	1456:1490	para-chloromercuribenzene sulfonate (pCMBS)	1456:1498	Conversely, the transport function was not affected by the JK*A/JK*B polymorphism, C-terminal deletion (residues 360-389), or mutation of the extracellular N-glycosylation consensus site and remains poorly para-chloromercuribenzene sulfonate (pCMBS)-sensitive.
12093813	1	24	theme	blood	103:107	arg1	hUT-B1					150:155	the urea transporter hUT-B1	129:155	the urea transporter hUT-B1	129:155	The Kidd (JK) blood group locus encodes the urea transporter hUT-B1, which is expressed on human red blood cells and other tissues.
12093813	1	24	theme	blood	103:107	arg1	locus					115:119	The Kidd (JK) blood group locus	89:119	The Kidd (JK) blood group locus	89:119	The Kidd (JK) blood group locus encodes the urea transporter hUT-B1, which is expressed on human red blood cells and other tissues.
12093813	2	25	theme	first	612:616	arg1	demonstration					625:637	the first direct demonstration that the hUT-B1 gene encodes the Kidd blood group antigens	608:696	the first direct demonstration that the hUT-B1 gene encodes the Kidd blood group antigens	608:696	The common JK*A/JK*B blood group polymorphism is caused by a single nucleotide transition G838A changing Asp-280 to Asn-280 on the polypeptide, and transfection of erythroleukemic K562 cells with hUT-B1 cDNAs carrying either the G838 or the A838 nucleotide substitutions resulted in the isolation of stable clones that expressed the Jk(a) or Jk(b) antigens, respectively, thus providing the first direct demonstration that the hUT-B1 gene encodes the Kidd blood group antigens.
12093813	0	26	theme	blood	53:57	arg1	cell					59:62	the human red blood cell	39:62	the human red blood cell	39:62	Antigenic and functional properties of the human red blood cell urea transporter hUT-B1.
12093813	6	27	theme	A/JK	1312:1315	arg1	polymorphism					1319:1330	the JK*A/JK*B polymorphism	1305:1330	the JK*A/JK*B polymorphism	1305:1330	Conversely, the transport function was not affected by the JK*A/JK*B polymorphism, C-terminal deletion (residues 360-389), or mutation of the extracellular N-glycosylation consensus site and remains poorly para-chloromercuribenzene sulfonate (pCMBS)-sensitive.
12093813	7	28	theme	urea	1637:1640	arg1	pCMBS-sensitive					1655:1669	pCMBS-sensitive	1655:1669	pCMBS-sensitive	1655:1669	However, transport studies by stopped flow light scattering using Jk-K562 transfectants demonstrated that the hUT-B1-mediated urea transport is pCMBS-sensitive in an erythroid context, as reported previously for the transporter of human red blood cells.
12093813	7	28	theme	urea	1637:1640	arg1	transport					1642:1650	the hUT-B1-mediated urea transport	1617:1650	the hUT-B1-mediated urea transport	1617:1650	However, transport studies by stopped flow light scattering using Jk-K562 transfectants demonstrated that the hUT-B1-mediated urea transport is pCMBS-sensitive in an erythroid context, as reported previously for the transporter of human red blood cells.
12093813	2	29	theme	hUT-B1	417:422	arg1	cDNAs					424:428	hUT-B1 cDNAs	417:428	hUT-B1 cDNAs carrying either the G838 or the A838 nucleotide substitutions	417:490	The common JK*A/JK*B blood group polymorphism is caused by a single nucleotide transition G838A changing Asp-280 to Asn-280 on the polypeptide, and transfection of erythroleukemic K562 cells with hUT-B1 cDNAs carrying either the G838 or the A838 nucleotide substitutions resulted in the isolation of stable clones that expressed the Jk(a) or Jk(b) antigens, respectively, thus providing the first direct demonstration that the hUT-B1 gene encodes the Kidd blood group antigens.
12093813	7	30	theme	red	1748:1750	arg1	cells					1758:1762	human red blood cells	1742:1762	human red blood cells	1742:1762	However, transport studies by stopped flow light scattering using Jk-K562 transfectants demonstrated that the hUT-B1-mediated urea transport is pCMBS-sensitive in an erythroid context, as reported previously for the transporter of human red blood cells.
12093813	3	31	theme	cells	749:753	arg1	analysis					727:734	immunochemical analysis	712:734	immunochemical analysis of red blood cells	712:753	In addition, immunochemical analysis of red blood cells demonstrated that hUT-B1 also exhibits ABO determinants attached to the single N-linked sugar chain at Asn-211.
12093813	3	32	theme	ABO	794:796	arg1	determinants					798:809	ABO determinants	794:809	ABO determinants attached to the single N-linked sugar chain at Asn-211	794:864	In addition, immunochemical analysis of red blood cells demonstrated that hUT-B1 also exhibits ABO determinants attached to the single N-linked sugar chain at Asn-211.
12093813	9	33	theme	functional	1925:1934	arg1	properties					1936:1945	these antigenic, topologic, and functional properties	1893:1945	these antigenic, topologic, and functional properties	1893:1945	Altogether, these antigenic, topologic, and functional properties might have implications into the physiology of hUT-B1 and other members of the urea transporter family.
12093813	5	34	theme	membrane	1229:1236	arg1	addressing					1238:1247	plasma membrane addressing	1222:1247	plasma membrane addressing	1222:1247	Mutagenesis and functional studies by expression in Xenopus oocytes revealed that both cysteines Cys-25 and Cys-30 (but not alone) are essential for plasma membrane addressing.
12093813	7	35	theme	Jk-K562	1577:1583	arg1	transfectants					1585:1597	Jk-K562 transfectants	1577:1597	Jk-K562 transfectants	1577:1597	However, transport studies by stopped flow light scattering using Jk-K562 transfectants demonstrated that the hUT-B1-mediated urea transport is pCMBS-sensitive in an erythroid context, as reported previously for the transporter of human red blood cells.
12093813	0	36	theme	Antigenic	0:8	arg1	properties					25:34	Antigenic and functional properties	0:34	Antigenic and functional properties of the human red blood cell	0:62	Antigenic and functional properties of the human red blood cell urea transporter hUT-B1.
12093813	8	37	theme	Mutagenesis	1765:1775	arg1	analysis					1777:1784	Mutagenesis analysis	1765:1784	Mutagenesis analysis	1765:1784	Mutagenesis analysis also indicated that Cys-151 and Cys-236, at least alone, are not involved in pCMBS inhibition.
12093813	4	38	theme	red	939:941	arg1	vesicles					957:964	inside-out and right-side-out red cell membrane vesicles	909:964	vesicles	957:964	Moreover, immunoadsorption studies, using inside-out and right-side-out red cell membrane vesicles as competing antigen, demonstrated that the C- and N-terminal ends of hUT-B1 are oriented intracellularly.
12093813	0	39	theme	functional	14:23	arg1	properties					25:34	Antigenic and functional properties	0:34	Antigenic and functional properties of the human red blood cell	0:62	Antigenic and functional properties of the human red blood cell urea transporter hUT-B1.
12093813	5	40	theme	functional	1089:1098	arg1	studies					1100:1106	functional studies	1089:1106	functional studies by expression in Xenopus oocytes	1089:1139	Mutagenesis and functional studies by expression in Xenopus oocytes revealed that both cysteines Cys-25 and Cys-30 (but not alone) are essential for plasma membrane addressing.
12093813	7	41	theme	flow	1549:1552	arg1	scattering					1560:1569	stopped flow light scattering	1541:1569	stopped flow light scattering using Jk-K562 transfectants	1541:1597	However, transport studies by stopped flow light scattering using Jk-K562 transfectants demonstrated that the hUT-B1-mediated urea transport is pCMBS-sensitive in an erythroid context, as reported previously for the transporter of human red blood cells.
12093813	2	42	theme	cells	406:410	arg1	transfection					369:380	transfection	369:380	transfection of erythroleukemic K562 cells with hUT-B1 cDNAs carrying either the G838 or the A838 nucleotide substitutions	369:490	The common JK*A/JK*B blood group polymorphism is caused by a single nucleotide transition G838A changing Asp-280 to Asn-280 on the polypeptide, and transfection of erythroleukemic K562 cells with hUT-B1 cDNAs carrying either the G838 or the A838 nucleotide substitutions resulted in the isolation of stable clones that expressed the Jk(a) or Jk(b) antigens, respectively, thus providing the first direct demonstration that the hUT-B1 gene encodes the Kidd blood group antigens.
12093813	2	43	dep	Asn-280	337:343	arg1	to					334:335	to	334:335	to	334:335	The common JK*A/JK*B blood group polymorphism is caused by a single nucleotide transition G838A changing Asp-280 to Asn-280 on the polypeptide, and transfection of erythroleukemic K562 cells with hUT-B1 cDNAs carrying either the G838 or the A838 nucleotide substitutions resulted in the isolation of stable clones that expressed the Jk(a) or Jk(b) antigens, respectively, thus providing the first direct demonstration that the hUT-B1 gene encodes the Kidd blood group antigens.
12093813	6	44	theme	JK	1309:1310	arg1	polymorphism					1319:1330	the JK*A/JK*B polymorphism	1305:1330	the JK*A/JK*B polymorphism	1305:1330	Conversely, the transport function was not affected by the JK*A/JK*B polymorphism, C-terminal deletion (residues 360-389), or mutation of the extracellular N-glycosylation consensus site and remains poorly para-chloromercuribenzene sulfonate (pCMBS)-sensitive.
12093813	4	45	theme	immunoadsorption	877:892	arg1	studies					894:900	immunoadsorption studies	877:900	immunoadsorption studies	877:900	Moreover, immunoadsorption studies, using inside-out and right-side-out red cell membrane vesicles as competing antigen, demonstrated that the C- and N-terminal ends of hUT-B1 are oriented intracellularly.
12093813	2	46	theme	erythroleukemic	385:399	arg1	cells					406:410	erythroleukemic K562 cells	385:410	erythroleukemic K562 cells	385:410	The common JK*A/JK*B blood group polymorphism is caused by a single nucleotide transition G838A changing Asp-280 to Asn-280 on the polypeptide, and transfection of erythroleukemic K562 cells with hUT-B1 cDNAs carrying either the G838 or the A838 nucleotide substitutions resulted in the isolation of stable clones that expressed the Jk(a) or Jk(b) antigens, respectively, thus providing the first direct demonstration that the hUT-B1 gene encodes the Kidd blood group antigens.
12093813	8	47	theme	pCMBS	1863:1867	arg1	inhibition					1869:1878	pCMBS inhibition	1863:1878	pCMBS inhibition	1863:1878	Mutagenesis analysis also indicated that Cys-151 and Cys-236, at least alone, are not involved in pCMBS inhibition.
12093813	0	48	theme	human	43:47	arg1	cell					59:62	the human red blood cell	39:62	the human red blood cell	39:62	Antigenic and functional properties of the human red blood cell urea transporter hUT-B1.
12093813	7	49	theme	blood	1752:1756	arg1	cells					1758:1762	human red blood cells	1742:1762	human red blood cells	1742:1762	However, transport studies by stopped flow light scattering using Jk-K562 transfectants demonstrated that the hUT-B1-mediated urea transport is pCMBS-sensitive in an erythroid context, as reported previously for the transporter of human red blood cells.
12093813	7	50	from	context	1687:1693	arg1	pCMBS-sensitive					1655:1669	pCMBS-sensitive	1655:1669	pCMBS-sensitive	1655:1669	However, transport studies by stopped flow light scattering using Jk-K562 transfectants demonstrated that the hUT-B1-mediated urea transport is pCMBS-sensitive in an erythroid context, as reported previously for the transporter of human red blood cells.
12093813	7	50	from	context	1687:1693	arg1	transport					1642:1650	the hUT-B1-mediated urea transport	1617:1650	the hUT-B1-mediated urea transport	1617:1650	However, transport studies by stopped flow light scattering using Jk-K562 transfectants demonstrated that the hUT-B1-mediated urea transport is pCMBS-sensitive in an erythroid context, as reported previously for the transporter of human red blood cells.
12093813	2	51	contain	carrying	430:437	arg1	cDNAs					424:428	hUT-B1 cDNAs	417:428	hUT-B1 cDNAs carrying either the G838 or the A838 nucleotide substitutions	417:490	The common JK*A/JK*B blood group polymorphism is caused by a single nucleotide transition G838A changing Asp-280 to Asn-280 on the polypeptide, and transfection of erythroleukemic K562 cells with hUT-B1 cDNAs carrying either the G838 or the A838 nucleotide substitutions resulted in the isolation of stable clones that expressed the Jk(a) or Jk(b) antigens, respectively, thus providing the first direct demonstration that the hUT-B1 gene encodes the Kidd blood group antigens.
12093813	2	51	contain	carrying	430:437	arg2	G838					450:453	the G838	446:453	the G838	446:453	The common JK*A/JK*B blood group polymorphism is caused by a single nucleotide transition G838A changing Asp-280 to Asn-280 on the polypeptide, and transfection of erythroleukemic K562 cells with hUT-B1 cDNAs carrying either the G838 or the A838 nucleotide substitutions resulted in the isolation of stable clones that expressed the Jk(a) or Jk(b) antigens, respectively, thus providing the first direct demonstration that the hUT-B1 gene encodes the Kidd blood group antigens.
12093813	2	51	contain	carrying	430:437	arg2	substitutions					478:490	the A838 nucleotide substitutions	458:490	the A838 nucleotide substitutions	458:490	The common JK*A/JK*B blood group polymorphism is caused by a single nucleotide transition G838A changing Asp-280 to Asn-280 on the polypeptide, and transfection of erythroleukemic K562 cells with hUT-B1 cDNAs carrying either the G838 or the A838 nucleotide substitutions resulted in the isolation of stable clones that expressed the Jk(a) or Jk(b) antigens, respectively, thus providing the first direct demonstration that the hUT-B1 gene encodes the Kidd blood group antigens.
12093813	1	52	theme	human	180:184	arg1	cells					196:200	human red blood cells	180:200	human red blood cells	180:200	The Kidd (JK) blood group locus encodes the urea transporter hUT-B1, which is expressed on human red blood cells and other tissues.
12093813	7	53	theme	human	1742:1746	arg1	cells					1758:1762	human red blood cells	1742:1762	human red blood cells	1742:1762	However, transport studies by stopped flow light scattering using Jk-K562 transfectants demonstrated that the hUT-B1-mediated urea transport is pCMBS-sensitive in an erythroid context, as reported previously for the transporter of human red blood cells.
12093813	2	54	theme	group	683:687	arg1	antigens					689:696	the Kidd blood group antigens	668:696	the Kidd blood group antigens	668:696	The common JK*A/JK*B blood group polymorphism is caused by a single nucleotide transition G838A changing Asp-280 to Asn-280 on the polypeptide, and transfection of erythroleukemic K562 cells with hUT-B1 cDNAs carrying either the G838 or the A838 nucleotide substitutions resulted in the isolation of stable clones that expressed the Jk(a) or Jk(b) antigens, respectively, thus providing the first direct demonstration that the hUT-B1 gene encodes the Kidd blood group antigens.
12093813	2	54	theme	group	683:687	arg1	gene					655:658	the hUT-B1 gene	644:658	the hUT-B1 gene	644:658	The common JK*A/JK*B blood group polymorphism is caused by a single nucleotide transition G838A changing Asp-280 to Asn-280 on the polypeptide, and transfection of erythroleukemic K562 cells with hUT-B1 cDNAs carrying either the G838 or the A838 nucleotide substitutions resulted in the isolation of stable clones that expressed the Jk(a) or Jk(b) antigens, respectively, thus providing the first direct demonstration that the hUT-B1 gene encodes the Kidd blood group antigens.
12093813	9	55	theme	members	2011:2017	arg1	physiology					1980:1989	the physiology	1976:1989	the physiology of hUT-B1 and other members of the urea transporter family	1976:2048	Altogether, these antigenic, topologic, and functional properties might have implications into the physiology of hUT-B1 and other members of the urea transporter family.
12093813	2	56	theme	nucleotide	289:298	arg1	transition					300:309	a single nucleotide transition	280:309	a single nucleotide transition G838A changing Asp-280 to Asn-280 on the polypeptide	280:362	The common JK*A/JK*B blood group polymorphism is caused by a single nucleotide transition G838A changing Asp-280 to Asn-280 on the polypeptide, and transfection of erythroleukemic K562 cells with hUT-B1 cDNAs carrying either the G838 or the A838 nucleotide substitutions resulted in the isolation of stable clones that expressed the Jk(a) or Jk(b) antigens, respectively, thus providing the first direct demonstration that the hUT-B1 gene encodes the Kidd blood group antigens.
12093813	1	57	theme	blood	190:194	arg1	cells					196:200	human red blood cells	180:200	human red blood cells	180:200	The Kidd (JK) blood group locus encodes the urea transporter hUT-B1, which is expressed on human red blood cells and other tissues.
12093813	4	58	theme	membrane	948:955	arg1	vesicles					957:964	inside-out and right-side-out red cell membrane vesicles	909:964	vesicles	957:964	Moreover, immunoadsorption studies, using inside-out and right-side-out red cell membrane vesicles as competing antigen, demonstrated that the C- and N-terminal ends of hUT-B1 are oriented intracellularly.
12093813	2	59	theme	clones	528:533	arg1	isolation					508:516	the isolation	504:516	the isolation of stable clones that expressed the Jk(a) or Jk(b) antigens, respectively, thus providing the first direct demonstration that the hUT-B1 gene encodes the Kidd blood group antigens	504:696	The common JK*A/JK*B blood group polymorphism is caused by a single nucleotide transition G838A changing Asp-280 to Asn-280 on the polypeptide, and transfection of erythroleukemic K562 cells with hUT-B1 cDNAs carrying either the G838 or the A838 nucleotide substitutions resulted in the isolation of stable clones that expressed the Jk(a) or Jk(b) antigens, respectively, thus providing the first direct demonstration that the hUT-B1 gene encodes the Kidd blood group antigens.
12093813	9	60	theme	transporter	2031:2041	arg1	family					2043:2048	the urea transporter family	2022:2048	the urea transporter family	2022:2048	Altogether, these antigenic, topologic, and functional properties might have implications into the physiology of hUT-B1 and other members of the urea transporter family.
12093813	2	61	theme	*	234:234	arg1	polymorphism					254:265	The common JK*A/JK*B blood group polymorphism	221:265	The common JK*A/JK*B blood group polymorphism	221:265	The common JK*A/JK*B blood group polymorphism is caused by a single nucleotide transition G838A changing Asp-280 to Asn-280 on the polypeptide, and transfection of erythroleukemic K562 cells with hUT-B1 cDNAs carrying either the G838 or the A838 nucleotide substitutions resulted in the isolation of stable clones that expressed the Jk(a) or Jk(b) antigens, respectively, thus providing the first direct demonstration that the hUT-B1 gene encodes the Kidd blood group antigens.
12093813	2	62	theme	hUT-B1	648:653	arg1	antigens					689:696	the Kidd blood group antigens	668:696	the Kidd blood group antigens	668:696	The common JK*A/JK*B blood group polymorphism is caused by a single nucleotide transition G838A changing Asp-280 to Asn-280 on the polypeptide, and transfection of erythroleukemic K562 cells with hUT-B1 cDNAs carrying either the G838 or the A838 nucleotide substitutions resulted in the isolation of stable clones that expressed the Jk(a) or Jk(b) antigens, respectively, thus providing the first direct demonstration that the hUT-B1 gene encodes the Kidd blood group antigens.
12093813	2	62	theme	hUT-B1	648:653	arg1	gene					655:658	the hUT-B1 gene	644:658	the hUT-B1 gene	644:658	The common JK*A/JK*B blood group polymorphism is caused by a single nucleotide transition G838A changing Asp-280 to Asn-280 on the polypeptide, and transfection of erythroleukemic K562 cells with hUT-B1 cDNAs carrying either the G838 or the A838 nucleotide substitutions resulted in the isolation of stable clones that expressed the Jk(a) or Jk(b) antigens, respectively, thus providing the first direct demonstration that the hUT-B1 gene encodes the Kidd blood group antigens.
12093813	2	63	theme	common	225:230	arg1	polymorphism					254:265	The common JK*A/JK*B blood group polymorphism	221:265	The common JK*A/JK*B blood group polymorphism	221:265	The common JK*A/JK*B blood group polymorphism is caused by a single nucleotide transition G838A changing Asp-280 to Asn-280 on the polypeptide, and transfection of erythroleukemic K562 cells with hUT-B1 cDNAs carrying either the G838 or the A838 nucleotide substitutions resulted in the isolation of stable clones that expressed the Jk(a) or Jk(b) antigens, respectively, thus providing the first direct demonstration that the hUT-B1 gene encodes the Kidd blood group antigens.
12093813	6	64	theme	consensus	1422:1430	arg1	site					1432:1435	the extracellular N-glycosylation consensus site	1388:1435	the extracellular N-glycosylation consensus site	1388:1435	Conversely, the transport function was not affected by the JK*A/JK*B polymorphism, C-terminal deletion (residues 360-389), or mutation of the extracellular N-glycosylation consensus site and remains poorly para-chloromercuribenzene sulfonate (pCMBS)-sensitive.
12093813	1	65	theme	urea	133:136	arg1	hUT-B1					150:155	the urea transporter hUT-B1	129:155	the urea transporter hUT-B1	129:155	The Kidd (JK) blood group locus encodes the urea transporter hUT-B1, which is expressed on human red blood cells and other tissues.
12093813	1	65	theme	urea	133:136	arg1	locus					115:119	The Kidd (JK) blood group locus	89:119	The Kidd (JK) blood group locus	89:119	The Kidd (JK) blood group locus encodes the urea transporter hUT-B1, which is expressed on human red blood cells and other tissues.
12093813	4	66	theme	hUT-B1	1036:1041	arg1	C-					1010:1011	C-	1010:1011	C-	1010:1011	Moreover, immunoadsorption studies, using inside-out and right-side-out red cell membrane vesicles as competing antigen, demonstrated that the C- and N-terminal ends of hUT-B1 are oriented intracellularly.
12093813	4	66	theme	hUT-B1	1036:1041	arg1	ends					1028:1031	N-terminal ends	1017:1031	N-terminal ends	1017:1031	Moreover, immunoadsorption studies, using inside-out and right-side-out red cell membrane vesicles as competing antigen, demonstrated that the C- and N-terminal ends of hUT-B1 are oriented intracellularly.
12093813	2	67	theme	blood	242:246	arg1	polymorphism					254:265	The common JK*A/JK*B blood group polymorphism	221:265	The common JK*A/JK*B blood group polymorphism	221:265	The common JK*A/JK*B blood group polymorphism is caused by a single nucleotide transition G838A changing Asp-280 to Asn-280 on the polypeptide, and transfection of erythroleukemic K562 cells with hUT-B1 cDNAs carrying either the G838 or the A838 nucleotide substitutions resulted in the isolation of stable clones that expressed the Jk(a) or Jk(b) antigens, respectively, thus providing the first direct demonstration that the hUT-B1 gene encodes the Kidd blood group antigens.
12093813	6	68	theme	extracellular	1392:1404	arg1	site					1432:1435	the extracellular N-glycosylation consensus site	1388:1435	the extracellular N-glycosylation consensus site	1388:1435	Conversely, the transport function was not affected by the JK*A/JK*B polymorphism, C-terminal deletion (residues 360-389), or mutation of the extracellular N-glycosylation consensus site and remains poorly para-chloromercuribenzene sulfonate (pCMBS)-sensitive.
12093813	5	69	dep	cysteines	1160:1168	arg1	cysteines					1160:1168	both cysteines Cys-25 and Cys-30 (but not alone)	1155:1202	both cysteines Cys-25 and Cys-30 (but not alone)	1155:1202	Mutagenesis and functional studies by expression in Xenopus oocytes revealed that both cysteines Cys-25 and Cys-30 (but not alone) are essential for plasma membrane addressing.
12093813	5	69	dep	cysteines	1160:1168	arg1	Cys-30					1181:1186	Cys-30	1181:1186	Cys-30	1181:1186	Mutagenesis and functional studies by expression in Xenopus oocytes revealed that both cysteines Cys-25 and Cys-30 (but not alone) are essential for plasma membrane addressing.
12093813	5	69	dep	cysteines	1160:1168	arg1	Cys-25					1170:1175	Cys-25	1170:1175	Cys-25	1170:1175	Mutagenesis and functional studies by expression in Xenopus oocytes revealed that both cysteines Cys-25 and Cys-30 (but not alone) are essential for plasma membrane addressing.
12093813	7	70	from	pCMBS-sensitive	1655:1669	arg1	context					1687:1693	an erythroid context	1674:1693	an erythroid context	1674:1693	However, transport studies by stopped flow light scattering using Jk-K562 transfectants demonstrated that the hUT-B1-mediated urea transport is pCMBS-sensitive in an erythroid context, as reported previously for the transporter of human red blood cells.
12093813	2	71	theme	Kidd	672:675	arg1	antigens					689:696	the Kidd blood group antigens	668:696	the Kidd blood group antigens	668:696	The common JK*A/JK*B blood group polymorphism is caused by a single nucleotide transition G838A changing Asp-280 to Asn-280 on the polypeptide, and transfection of erythroleukemic K562 cells with hUT-B1 cDNAs carrying either the G838 or the A838 nucleotide substitutions resulted in the isolation of stable clones that expressed the Jk(a) or Jk(b) antigens, respectively, thus providing the first direct demonstration that the hUT-B1 gene encodes the Kidd blood group antigens.
12093813	2	71	theme	Kidd	672:675	arg1	gene					655:658	the hUT-B1 gene	644:658	the hUT-B1 gene	644:658	The common JK*A/JK*B blood group polymorphism is caused by a single nucleotide transition G838A changing Asp-280 to Asn-280 on the polypeptide, and transfection of erythroleukemic K562 cells with hUT-B1 cDNAs carrying either the G838 or the A838 nucleotide substitutions resulted in the isolation of stable clones that expressed the Jk(a) or Jk(b) antigens, respectively, thus providing the first direct demonstration that the hUT-B1 gene encodes the Kidd blood group antigens.
12093813	7	72	theme	erythroid	1677:1685	arg1	context					1687:1693	an erythroid context	1674:1693	an erythroid context	1674:1693	However, transport studies by stopped flow light scattering using Jk-K562 transfectants demonstrated that the hUT-B1-mediated urea transport is pCMBS-sensitive in an erythroid context, as reported previously for the transporter of human red blood cells.
12093813	2	73	theme	*	239:239	arg1	polymorphism					254:265	The common JK*A/JK*B blood group polymorphism	221:265	The common JK*A/JK*B blood group polymorphism	221:265	The common JK*A/JK*B blood group polymorphism is caused by a single nucleotide transition G838A changing Asp-280 to Asn-280 on the polypeptide, and transfection of erythroleukemic K562 cells with hUT-B1 cDNAs carrying either the G838 or the A838 nucleotide substitutions resulted in the isolation of stable clones that expressed the Jk(a) or Jk(b) antigens, respectively, thus providing the first direct demonstration that the hUT-B1 gene encodes the Kidd blood group antigens.
12093813	9	74	theme	topologic	1910:1918	arg1	properties					1936:1945	these antigenic, topologic, and functional properties	1893:1945	these antigenic, topologic, and functional properties	1893:1945	Altogether, these antigenic, topologic, and functional properties might have implications into the physiology of hUT-B1 and other members of the urea transporter family.
12093813	7	75	theme	transport	1520:1528	arg1	studies					1530:1536	transport studies	1520:1536	transport studies by stopped flow light scattering using Jk-K562 transfectants	1520:1597	However, transport studies by stopped flow light scattering using Jk-K562 transfectants demonstrated that the hUT-B1-mediated urea transport is pCMBS-sensitive in an erythroid context, as reported previously for the transporter of human red blood cells.
12093813	2	76	theme	nucleotide	467:476	arg1	substitutions					478:490	the A838 nucleotide substitutions	458:490	the A838 nucleotide substitutions	458:490	The common JK*A/JK*B blood group polymorphism is caused by a single nucleotide transition G838A changing Asp-280 to Asn-280 on the polypeptide, and transfection of erythroleukemic K562 cells with hUT-B1 cDNAs carrying either the G838 or the A838 nucleotide substitutions resulted in the isolation of stable clones that expressed the Jk(a) or Jk(b) antigens, respectively, thus providing the first direct demonstration that the hUT-B1 gene encodes the Kidd blood group antigens.
12093813	9	77	contain	have	1953:1956	arg2	implications					1958:1969	implications	1958:1969	implications	1958:1969	Altogether, these antigenic, topologic, and functional properties might have implications into the physiology of hUT-B1 and other members of the urea transporter family.
12093813	9	77	contain	have	1953:1956	arg1	properties					1936:1945	these antigenic, topologic, and functional properties	1893:1945	these antigenic, topologic, and functional properties	1893:1945	Altogether, these antigenic, topologic, and functional properties might have implications into the physiology of hUT-B1 and other members of the urea transporter family.
12093813	4	78	dep	C-	1010:1011	arg1	the					1006:1008	the	1006:1008	the	1006:1008	Moreover, immunoadsorption studies, using inside-out and right-side-out red cell membrane vesicles as competing antigen, demonstrated that the C- and N-terminal ends of hUT-B1 are oriented intracellularly.
12093813	3	79	theme	blood	743:747	arg1	cells					749:753	red blood cells	739:753	red blood cells	739:753	In addition, immunochemical analysis of red blood cells demonstrated that hUT-B1 also exhibits ABO determinants attached to the single N-linked sugar chain at Asn-211.
12093813	7	80	theme	cells	1758:1762	arg1	transporter					1727:1737	the transporter	1723:1737	the transporter of human red blood cells	1723:1762	However, transport studies by stopped flow light scattering using Jk-K562 transfectants demonstrated that the hUT-B1-mediated urea transport is pCMBS-sensitive in an erythroid context, as reported previously for the transporter of human red blood cells.
12093813	2	81	theme	direct	618:623	arg1	demonstration					625:637	the first direct demonstration that the hUT-B1 gene encodes the Kidd blood group antigens	608:696	the first direct demonstration that the hUT-B1 gene encodes the Kidd blood group antigens	608:696	The common JK*A/JK*B blood group polymorphism is caused by a single nucleotide transition G838A changing Asp-280 to Asn-280 on the polypeptide, and transfection of erythroleukemic K562 cells with hUT-B1 cDNAs carrying either the G838 or the A838 nucleotide substitutions resulted in the isolation of stable clones that expressed the Jk(a) or Jk(b) antigens, respectively, thus providing the first direct demonstration that the hUT-B1 gene encodes the Kidd blood group antigens.
12093813	0	82	theme	cell	59:62	arg1	properties					25:34	Antigenic and functional properties	0:34	Antigenic and functional properties of the human red blood cell	0:62	Antigenic and functional properties of the human red blood cell urea transporter hUT-B1.
12093813	6	83	gly	N-glycosylation	1406:1420	arg2	site					1432:1435	the extracellular N-glycosylation consensus site	1388:1435	the extracellular N-glycosylation consensus site	1388:1435	Conversely, the transport function was not affected by the JK*A/JK*B polymorphism, C-terminal deletion (residues 360-389), or mutation of the extracellular N-glycosylation consensus site and remains poorly para-chloromercuribenzene sulfonate (pCMBS)-sensitive.
12093813	1	84	theme	group	109:113	arg1	hUT-B1					150:155	the urea transporter hUT-B1	129:155	the urea transporter hUT-B1	129:155	The Kidd (JK) blood group locus encodes the urea transporter hUT-B1, which is expressed on human red blood cells and other tissues.
12093813	1	84	theme	group	109:113	arg1	locus					115:119	The Kidd (JK) blood group locus	89:119	The Kidd (JK) blood group locus	89:119	The Kidd (JK) blood group locus encodes the urea transporter hUT-B1, which is expressed on human red blood cells and other tissues.
12093813	9	85	theme	antigenic	1899:1907	arg1	properties					1936:1945	these antigenic, topologic, and functional properties	1893:1945	these antigenic, topologic, and functional properties	1893:1945	Altogether, these antigenic, topologic, and functional properties might have implications into the physiology of hUT-B1 and other members of the urea transporter family.
12093813	0	86	theme	transporter	69:79	arg1	hUT-B1					81:86	transporter hUT-B1	69:86	transporter hUT-B1	69:86	Antigenic and functional properties of the human red blood cell urea transporter hUT-B1.
12093813	8	87	dep	Cys-151	1806:1812	arg1	alone					1836:1840	alone	1836:1840	alone	1836:1840	Mutagenesis analysis also indicated that Cys-151 and Cys-236, at least alone, are not involved in pCMBS inhibition.
12093813	2	88	theme	Jk	563:564	arg1	antigens					569:576	Jk(b) antigens	563:576	Jk(b) antigens	563:576	The common JK*A/JK*B blood group polymorphism is caused by a single nucleotide transition G838A changing Asp-280 to Asn-280 on the polypeptide, and transfection of erythroleukemic K562 cells with hUT-B1 cDNAs carrying either the G838 or the A838 nucleotide substitutions resulted in the isolation of stable clones that expressed the Jk(a) or Jk(b) antigens, respectively, thus providing the first direct demonstration that the hUT-B1 gene encodes the Kidd blood group antigens.
12093813	3	89	theme	immunochemical	712:725	arg1	analysis					727:734	immunochemical analysis	712:734	immunochemical analysis of red blood cells	712:753	In addition, immunochemical analysis of red blood cells demonstrated that hUT-B1 also exhibits ABO determinants attached to the single N-linked sugar chain at Asn-211.
12093813	6	90	theme	transport	1266:1274	arg1	function					1276:1283	the transport function	1262:1283	the transport function	1262:1283	Conversely, the transport function was not affected by the JK*A/JK*B polymorphism, C-terminal deletion (residues 360-389), or mutation of the extracellular N-glycosylation consensus site and remains poorly para-chloromercuribenzene sulfonate (pCMBS)-sensitive.
12093813	7	91	theme	hUT-B1-mediated	1621:1635	arg1	pCMBS-sensitive					1655:1669	pCMBS-sensitive	1655:1669	pCMBS-sensitive	1655:1669	However, transport studies by stopped flow light scattering using Jk-K562 transfectants demonstrated that the hUT-B1-mediated urea transport is pCMBS-sensitive in an erythroid context, as reported previously for the transporter of human red blood cells.
12093813	7	91	theme	hUT-B1-mediated	1621:1635	arg1	transport					1642:1650	the hUT-B1-mediated urea transport	1617:1650	the hUT-B1-mediated urea transport	1617:1650	However, transport studies by stopped flow light scattering using Jk-K562 transfectants demonstrated that the hUT-B1-mediated urea transport is pCMBS-sensitive in an erythroid context, as reported previously for the transporter of human red blood cells.
12093813	5	92	theme	plasma	1222:1227	arg1	addressing					1238:1247	plasma membrane addressing	1222:1247	plasma membrane addressing	1222:1247	Mutagenesis and functional studies by expression in Xenopus oocytes revealed that both cysteines Cys-25 and Cys-30 (but not alone) are essential for plasma membrane addressing.
12093813	4	93	theme	inside-out	909:918	arg1	vesicles					957:964	inside-out and right-side-out red cell membrane vesicles	909:964	vesicles	957:964	Moreover, immunoadsorption studies, using inside-out and right-side-out red cell membrane vesicles as competing antigen, demonstrated that the C- and N-terminal ends of hUT-B1 are oriented intracellularly.
12093813	2	94	theme	b	566:566	arg1	antigens					569:576	Jk(b) antigens	563:576	Jk(b) antigens	563:576	The common JK*A/JK*B blood group polymorphism is caused by a single nucleotide transition G838A changing Asp-280 to Asn-280 on the polypeptide, and transfection of erythroleukemic K562 cells with hUT-B1 cDNAs carrying either the G838 or the A838 nucleotide substitutions resulted in the isolation of stable clones that expressed the Jk(a) or Jk(b) antigens, respectively, thus providing the first direct demonstration that the hUT-B1 gene encodes the Kidd blood group antigens.
12093813	2	95	theme	transition	300:309	arg1	G838A					311:315	a single nucleotide transition G838A	280:315	a single nucleotide transition G838A changing Asp-280 to Asn-280 on the polypeptide	280:362	The common JK*A/JK*B blood group polymorphism is caused by a single nucleotide transition G838A changing Asp-280 to Asn-280 on the polypeptide, and transfection of erythroleukemic K562 cells with hUT-B1 cDNAs carrying either the G838 or the A838 nucleotide substitutions resulted in the isolation of stable clones that expressed the Jk(a) or Jk(b) antigens, respectively, thus providing the first direct demonstration that the hUT-B1 gene encodes the Kidd blood group antigens.
12093813	6	96	theme	*	1316:1316	arg1	polymorphism					1319:1330	the JK*A/JK*B polymorphism	1305:1330	the JK*A/JK*B polymorphism	1305:1330	Conversely, the transport function was not affected by the JK*A/JK*B polymorphism, C-terminal deletion (residues 360-389), or mutation of the extracellular N-glycosylation consensus site and remains poorly para-chloromercuribenzene sulfonate (pCMBS)-sensitive.
12093813	3	97	theme	single	827:832	arg1	chain					849:853	the single N-linked sugar chain	823:853	the single N-linked sugar chain	823:853	In addition, immunochemical analysis of red blood cells demonstrated that hUT-B1 also exhibits ABO determinants attached to the single N-linked sugar chain at Asn-211.
12093813	4	98	theme	right-side-out	924:937	arg1	vesicles					957:964	inside-out and right-side-out red cell membrane vesicles	909:964	vesicles	957:964	Moreover, immunoadsorption studies, using inside-out and right-side-out red cell membrane vesicles as competing antigen, demonstrated that the C- and N-terminal ends of hUT-B1 are oriented intracellularly.
12093813	6	99	theme	*	1311:1311	arg1	polymorphism					1319:1330	the JK*A/JK*B polymorphism	1305:1330	the JK*A/JK*B polymorphism	1305:1330	Conversely, the transport function was not affected by the JK*A/JK*B polymorphism, C-terminal deletion (residues 360-389), or mutation of the extracellular N-glycosylation consensus site and remains poorly para-chloromercuribenzene sulfonate (pCMBS)-sensitive.
12093813	7	100	theme	light	1554:1558	arg1	scattering					1560:1569	stopped flow light scattering	1541:1569	stopped flow light scattering using Jk-K562 transfectants	1541:1597	However, transport studies by stopped flow light scattering using Jk-K562 transfectants demonstrated that the hUT-B1-mediated urea transport is pCMBS-sensitive in an erythroid context, as reported previously for the transporter of human red blood cells.
12093813	2	101	theme	K562	401:404	arg1	cells					406:410	erythroleukemic K562 cells	385:410	erythroleukemic K562 cells	385:410	The common JK*A/JK*B blood group polymorphism is caused by a single nucleotide transition G838A changing Asp-280 to Asn-280 on the polypeptide, and transfection of erythroleukemic K562 cells with hUT-B1 cDNAs carrying either the G838 or the A838 nucleotide substitutions resulted in the isolation of stable clones that expressed the Jk(a) or Jk(b) antigens, respectively, thus providing the first direct demonstration that the hUT-B1 gene encodes the Kidd blood group antigens.
12093813	3	102	link	N-linked	834:841	arg1	chain					849:853	the single N-linked sugar chain	823:853	the single N-linked sugar chain	823:853	In addition, immunochemical analysis of red blood cells demonstrated that hUT-B1 also exhibits ABO determinants attached to the single N-linked sugar chain at Asn-211.
12093813	0	103	theme	red	49:51	arg1	cell					59:62	the human red blood cell	39:62	the human red blood cell	39:62	Antigenic and functional properties of the human red blood cell urea transporter hUT-B1.
12093813	9	104	theme	hUT-B1	1994:1999	arg1	physiology					1980:1989	the physiology	1976:1989	the physiology of hUT-B1 and other members of the urea transporter family	1976:2048	Altogether, these antigenic, topologic, and functional properties might have implications into the physiology of hUT-B1 and other members of the urea transporter family.
12093813	3	105	theme	sugar	843:847	arg1	chain					849:853	the single N-linked sugar chain	823:853	the single N-linked sugar chain	823:853	In addition, immunochemical analysis of red blood cells demonstrated that hUT-B1 also exhibits ABO determinants attached to the single N-linked sugar chain at Asn-211.
12093813	9	106	theme	other	2005:2009	arg1	members					2011:2017	other members	2005:2017	other members of the urea transporter family	2005:2048	Altogether, these antigenic, topologic, and functional properties might have implications into the physiology of hUT-B1 and other members of the urea transporter family.
12093813	2	107	theme	group	248:252	arg1	polymorphism					254:265	The common JK*A/JK*B blood group polymorphism	221:265	The common JK*A/JK*B blood group polymorphism	221:265	The common JK*A/JK*B blood group polymorphism is caused by a single nucleotide transition G838A changing Asp-280 to Asn-280 on the polypeptide, and transfection of erythroleukemic K562 cells with hUT-B1 cDNAs carrying either the G838 or the A838 nucleotide substitutions resulted in the isolation of stable clones that expressed the Jk(a) or Jk(b) antigens, respectively, thus providing the first direct demonstration that the hUT-B1 gene encodes the Kidd blood group antigens.
12093813	1	108	theme	red	186:188	arg1	cells					196:200	human red blood cells	180:200	human red blood cells	180:200	The Kidd (JK) blood group locus encodes the urea transporter hUT-B1, which is expressed on human red blood cells and other tissues.
12093813	6	109	dep	residues	1354:1361	arg1	360-389					1363:1369	360-389	1363:1369	360-389	1363:1369	Conversely, the transport function was not affected by the JK*A/JK*B polymorphism, C-terminal deletion (residues 360-389), or mutation of the extracellular N-glycosylation consensus site and remains poorly para-chloromercuribenzene sulfonate (pCMBS)-sensitive.
12093813	2	110	theme	blood	677:681	arg1	antigens					689:696	the Kidd blood group antigens	668:696	the Kidd blood group antigens	668:696	The common JK*A/JK*B blood group polymorphism is caused by a single nucleotide transition G838A changing Asp-280 to Asn-280 on the polypeptide, and transfection of erythroleukemic K562 cells with hUT-B1 cDNAs carrying either the G838 or the A838 nucleotide substitutions resulted in the isolation of stable clones that expressed the Jk(a) or Jk(b) antigens, respectively, thus providing the first direct demonstration that the hUT-B1 gene encodes the Kidd blood group antigens.
12093813	2	110	theme	blood	677:681	arg1	gene					655:658	the hUT-B1 gene	644:658	the hUT-B1 gene	644:658	The common JK*A/JK*B blood group polymorphism is caused by a single nucleotide transition G838A changing Asp-280 to Asn-280 on the polypeptide, and transfection of erythroleukemic K562 cells with hUT-B1 cDNAs carrying either the G838 or the A838 nucleotide substitutions resulted in the isolation of stable clones that expressed the Jk(a) or Jk(b) antigens, respectively, thus providing the first direct demonstration that the hUT-B1 gene encodes the Kidd blood group antigens.
12093813	2	111	theme	single	282:287	arg1	transition					300:309	a single nucleotide transition	280:309	a single nucleotide transition G838A changing Asp-280 to Asn-280 on the polypeptide	280:362	The common JK*A/JK*B blood group polymorphism is caused by a single nucleotide transition G838A changing Asp-280 to Asn-280 on the polypeptide, and transfection of erythroleukemic K562 cells with hUT-B1 cDNAs carrying either the G838 or the A838 nucleotide substitutions resulted in the isolation of stable clones that expressed the Jk(a) or Jk(b) antigens, respectively, thus providing the first direct demonstration that the hUT-B1 gene encodes the Kidd blood group antigens.
7753821	6	0	theme	transcription	1413:1425	arg1	domain					1463:1468	the N-terminal transcription activation/malignant transformation domain	1398:1468	the N-terminal transcription activation/malignant transformation domain	1398:1468	Analyses of serial deletion mutants of c-Myc further suggest that the O-GlcNAc site(s) are located within or near the N-terminal transcription activation/malignant transformation domain, a region where mutations of c-Myc that are frequently found in Burkitt and AIDS-related lymphomas cluster.
7753821	6	0	theme	transcription	1413:1425	arg1	region					1473:1478	a region	1471:1478	a region where mutations of c-Myc that are frequently found in Burkitt and AIDS-related lymphomas cluster	1471:1575	Analyses of serial deletion mutants of c-Myc further suggest that the O-GlcNAc site(s) are located within or near the N-terminal transcription activation/malignant transformation domain, a region where mutations of c-Myc that are frequently found in Burkitt and AIDS-related lymphomas cluster.
7753821	1	1	dep	serine	306:311	arg1	residues					326:333	residues	326:333	residues	326:333	O-linked N-acetylglucosamine (O-GlcNAc) is an abundant and dynamic posttranslational modification composed of a single monosaccharide, GlcNAc, glycosidically composed of a single monosaccharide, GlcNAc, glycosidically linked to the side-chain hydroxyl of serine or threonine residues.
7753821	5	2	from	protein	1207:1213	arg1	characterization					1144:1159	(iii) direct characterization	1131:1159	(iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells	1131:1281	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	5	2	from	protein	1207:1213	arg1	methods					868:874	three different methods	852:874	three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells	852:1281	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	5	2	from	protein	1207:1213	arg1	demonstration					881:893	(i) demonstration	877:893	(i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay	877:999	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	5	2	from	protein	1207:1213	arg1	glycosidase					1007:1017	(ii) glycosidase	1002:1017	(ii) glycosidase	1002:1017	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	5	2	from	protein	1207:1213	arg1	treatment					1042:1050	glycosyltransferase treatment	1022:1050	glycosyltransferase treatment	1022:1050	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	1	3	theme	single	163:168	arg1	GlcNAc					186:191	GlcNAc	186:191	GlcNAc	186:191	O-linked N-acetylglucosamine (O-GlcNAc) is an abundant and dynamic posttranslational modification composed of a single monosaccharide, GlcNAc, glycosidically composed of a single monosaccharide, GlcNAc, glycosidically linked to the side-chain hydroxyl of serine or threonine residues.
7753821	1	3	theme	single	163:168	arg1	monosaccharide					170:183	a single monosaccharide	161:183	a single monosaccharide	161:183	O-linked N-acetylglucosamine (O-GlcNAc) is an abundant and dynamic posttranslational modification composed of a single monosaccharide, GlcNAc, glycosidically composed of a single monosaccharide, GlcNAc, glycosidically linked to the side-chain hydroxyl of serine or threonine residues.
7753821	5	4	theme	sugar	1168:1172	arg1	moieties					1174:1181	the sugar moieties	1164:1181	the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells	1164:1281	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	5	5	theme	moieties	1174:1181	arg1	characterization					1144:1159	(iii) direct characterization	1131:1159	(iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells	1131:1281	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	5	5	theme	moieties	1174:1181	arg1	methods					868:874	three different methods	852:874	three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells	852:1281	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	5	5	theme	moieties	1174:1181	arg1	demonstration					881:893	(i) demonstration	877:893	(i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay	877:999	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	5	5	theme	moieties	1174:1181	arg1	glycosidase					1007:1017	(ii) glycosidase	1002:1017	(ii) glycosidase	1002:1017	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	5	5	theme	moieties	1174:1181	arg1	treatment					1042:1050	glycosyltransferase treatment	1022:1050	glycosyltransferase treatment	1022:1050	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	4	6	theme	O-GlcNAc	592:599	arg1	glycosylation					601:613	O-GlcNAc glycosylation	592:613	O-GlcNAc glycosylation of the oncoprotein c-Myc, a helix-loop-helix/leucine zipper phosphoprotein that heterodimerizes with Max and participates in the regulation of gene transcription in normal and neoplastic cells	592:806	Here we present evidence for O-GlcNAc glycosylation of the oncoprotein c-Myc, a helix-loop-helix/leucine zipper phosphoprotein that heterodimerizes with Max and participates in the regulation of gene transcription in normal and neoplastic cells.
7753821	5	7	theme	hamster	1263:1269	arg1	cells					1277:1281	Chinese hamster ovary cells	1255:1281	Chinese hamster ovary cells	1255:1281	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	6	8	theme	c-Myc	1323:1327	arg1	mutants					1312:1318	serial deletion mutants	1296:1318	serial deletion mutants of c-Myc	1296:1327	Analyses of serial deletion mutants of c-Myc further suggest that the O-GlcNAc site(s) are located within or near the N-terminal transcription activation/malignant transformation domain, a region where mutations of c-Myc that are frequently found in Burkitt and AIDS-related lymphomas cluster.
7753821	5	9	theme	translated	925:934	arg1	protein					936:942	in vitro translated protein	916:942	in vitro translated protein using a protein-protein interaction mobility-shift assay	916:999	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	5	10	theme	interaction	968:978	arg1	assay					995:999	a protein-protein interaction mobility-shift assay	950:999	a protein-protein interaction mobility-shift assay	950:999	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	4	11	theme	gene	758:761	arg1	transcription					763:775	gene transcription	758:775	gene transcription	758:775	Here we present evidence for O-GlcNAc glycosylation of the oncoprotein c-Myc, a helix-loop-helix/leucine zipper phosphoprotein that heterodimerizes with Max and participates in the regulation of gene transcription in normal and neoplastic cells.
7753821	5	12	from	glycosidase	1007:1017	arg1	protein					1207:1213	purified recombinant protein	1186:1213	purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells	1186:1281	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	3	13	theme	multimeric	541:550	arg1	complexes					552:560	reversible multimeric complexes	530:560	reversible multimeric complexes	530:560	These O-GlcNAc-bearing proteins are also modified by phosphorylation and form reversible multimeric complexes.
7753821	5	14	theme	binding	905:911	arg1	characterization					1144:1159	(iii) direct characterization	1131:1159	(iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells	1131:1281	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	5	14	theme	binding	905:911	arg1	methods					868:874	three different methods	852:874	three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells	852:1281	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	5	14	theme	binding	905:911	arg1	demonstration					881:893	(i) demonstration	877:893	(i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay	877:999	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	5	14	theme	binding	905:911	arg1	glycosidase					1007:1017	(ii) glycosidase	1002:1017	(ii) glycosidase	1002:1017	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	5	14	theme	binding	905:911	arg1	treatment					1042:1050	glycosyltransferase treatment	1022:1050	glycosyltransferase treatment	1022:1050	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	5	15	theme	ovary	1271:1275	arg1	cells					1277:1281	Chinese hamster ovary cells	1255:1281	Chinese hamster ovary cells	1255:1281	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	5	16	theme	c-Myc	834:838	arg1	modification					818:829	O-GlcNAc modification	809:829	O-GlcNAc modification of c-Myc	809:838	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	5	17	theme	different	858:866	arg1	characterization					1144:1159	(iii) direct characterization	1131:1159	(iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells	1131:1281	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	5	17	theme	different	858:866	arg1	glycosidase					1007:1017	(ii) glycosidase	1002:1017	(ii) glycosidase	1002:1017	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	5	17	theme	different	858:866	arg1	demonstration					881:893	(i) demonstration	877:893	(i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay	877:999	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	5	17	theme	different	858:866	arg1	methods					868:874	three different methods	852:874	three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells	852:1281	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	5	17	theme	different	858:866	arg1	treatment					1042:1050	glycosyltransferase treatment	1022:1050	glycosyltransferase treatment	1022:1050	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	5	18	from	moieties	1174:1181	arg1	protein					1207:1213	purified recombinant protein	1186:1213	purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells	1186:1281	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	2	19	theme	proteins	400:407	arg1	myriad					366:371	a myriad	364:371	a myriad of nuclear and cytoplasmic proteins	364:407	Although O-GlcNAc occurs on a myriad of nuclear and cytoplasmic proteins, only a few have thus far been identified.
7753821	5	20	from	characterization	1144:1159	arg1	protein					1207:1213	purified recombinant protein	1186:1213	purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells	1186:1281	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	5	21	from	treatment	1042:1050	arg1	protein					1207:1213	purified recombinant protein	1186:1213	purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells	1186:1281	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	6	22	theme	deletion	1303:1310	arg1	mutants					1312:1318	serial deletion mutants	1296:1318	serial deletion mutants of c-Myc	1296:1327	Analyses of serial deletion mutants of c-Myc further suggest that the O-GlcNAc site(s) are located within or near the N-terminal transcription activation/malignant transformation domain, a region where mutations of c-Myc that are frequently found in Burkitt and AIDS-related lymphomas cluster.
7753821	4	23	gly	glycosylation	601:613	arg1	phosphoprotein					675:688	a helix-loop-helix/leucine zipper phosphoprotein	641:688	a helix-loop-helix/leucine zipper phosphoprotein that heterodimerizes with Max and participates in the regulation of gene transcription in normal and neoplastic cells	641:806	Here we present evidence for O-GlcNAc glycosylation of the oncoprotein c-Myc, a helix-loop-helix/leucine zipper phosphoprotein that heterodimerizes with Max and participates in the regulation of gene transcription in normal and neoplastic cells.
7753821	4	23	gly	glycosylation	601:613	arg1	c-Myc					634:638	the oncoprotein c-Myc	618:638	the oncoprotein c-Myc	618:638	Here we present evidence for O-GlcNAc glycosylation of the oncoprotein c-Myc, a helix-loop-helix/leucine zipper phosphoprotein that heterodimerizes with Max and participates in the regulation of gene transcription in normal and neoplastic cells.
7753821	5	24	theme	mobility-shift	980:993	arg1	assay					995:999	a protein-protein interaction mobility-shift assay	950:999	a protein-protein interaction mobility-shift assay	950:999	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	5	25	theme	direct	1137:1142	arg1	characterization					1144:1159	(iii) direct characterization	1131:1159	(iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells	1131:1281	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	5	25	theme	direct	1137:1142	arg1	methods					868:874	three different methods	852:874	three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells	852:1281	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	2	26	theme	cytoplasmic	388:398	arg1	proteins					400:407	nuclear and cytoplasmic proteins	376:407	nuclear and cytoplasmic proteins	376:407	Although O-GlcNAc occurs on a myriad of nuclear and cytoplasmic proteins, only a few have thus far been identified.
7753821	1	27	link	O-linked	51:58	arg1	O-GlcNAc					81:88	O-GlcNAc	81:88	O-GlcNAc	81:88	O-linked N-acetylglucosamine (O-GlcNAc) is an abundant and dynamic posttranslational modification composed of a single monosaccharide, GlcNAc, glycosidically composed of a single monosaccharide, GlcNAc, glycosidically linked to the side-chain hydroxyl of serine or threonine residues.
7753821	1	27	link	O-linked	51:58	arg1	modification					136:147	an abundant and dynamic posttranslational modification	94:147	an abundant and dynamic posttranslational modification composed of a single monosaccharide, GlcNAc, glycosidically composed of a single monosaccharide, GlcNAc, glycosidically linked to the side-chain hydroxyl of serine or threonine residues	94:333	O-linked N-acetylglucosamine (O-GlcNAc) is an abundant and dynamic posttranslational modification composed of a single monosaccharide, GlcNAc, glycosidically composed of a single monosaccharide, GlcNAc, glycosidically linked to the side-chain hydroxyl of serine or threonine residues.
7753821	1	27	link	O-linked	51:58	arg1	N-acetylglucosamine					60:78	O-linked N-acetylglucosamine	51:78	O-linked N-acetylglucosamine (O-GlcNAc)	51:89	O-linked N-acetylglucosamine (O-GlcNAc) is an abundant and dynamic posttranslational modification composed of a single monosaccharide, GlcNAc, glycosidically composed of a single monosaccharide, GlcNAc, glycosidically linked to the side-chain hydroxyl of serine or threonine residues.
7753821	1	28	theme	side-chain	283:292	arg1	hydroxyl					294:301	the side-chain hydroxyl	279:301	the side-chain hydroxyl of serine or threonine residues	279:333	O-linked N-acetylglucosamine (O-GlcNAc) is an abundant and dynamic posttranslational modification composed of a single monosaccharide, GlcNAc, glycosidically composed of a single monosaccharide, GlcNAc, glycosidically linked to the side-chain hydroxyl of serine or threonine residues.
7753821	6	29	theme	serial	1296:1301	arg1	mutants					1312:1318	serial deletion mutants	1296:1318	serial deletion mutants of c-Myc	1296:1327	Analyses of serial deletion mutants of c-Myc further suggest that the O-GlcNAc site(s) are located within or near the N-terminal transcription activation/malignant transformation domain, a region where mutations of c-Myc that are frequently found in Burkitt and AIDS-related lymphomas cluster.
7753821	4	30	theme	normal	780:785	arg1	cells					802:806	normal and neoplastic cells	780:806	normal and neoplastic cells	780:806	Here we present evidence for O-GlcNAc glycosylation of the oncoprotein c-Myc, a helix-loop-helix/leucine zipper phosphoprotein that heterodimerizes with Max and participates in the regulation of gene transcription in normal and neoplastic cells.
7753821	0	31	theme	c-Myc	21:25	arg1	domain					43:48	the c-Myc transactivation domain	17:48	the c-Myc transactivation domain	17:48	Glycosylation of the c-Myc transactivation domain.
7753821	1	32	theme	abundant	97:104	arg1	modification					136:147	an abundant and dynamic posttranslational modification	94:147	an abundant and dynamic posttranslational modification composed of a single monosaccharide, GlcNAc, glycosidically composed of a single monosaccharide, GlcNAc, glycosidically linked to the side-chain hydroxyl of serine or threonine residues	94:333	O-linked N-acetylglucosamine (O-GlcNAc) is an abundant and dynamic posttranslational modification composed of a single monosaccharide, GlcNAc, glycosidically composed of a single monosaccharide, GlcNAc, glycosidically linked to the side-chain hydroxyl of serine or threonine residues.
7753821	1	32	theme	abundant	97:104	arg1	N-acetylglucosamine					60:78	O-linked N-acetylglucosamine	51:78	O-linked N-acetylglucosamine (O-GlcNAc)	51:89	O-linked N-acetylglucosamine (O-GlcNAc) is an abundant and dynamic posttranslational modification composed of a single monosaccharide, GlcNAc, glycosidically composed of a single monosaccharide, GlcNAc, glycosidically linked to the side-chain hydroxyl of serine or threonine residues.
7753821	3	33	theme	O-GlcNAc-bearing	458:473	arg1	proteins					475:482	These O-GlcNAc-bearing proteins	452:482	These O-GlcNAc-bearing proteins	452:482	These O-GlcNAc-bearing proteins are also modified by phosphorylation and form reversible multimeric complexes.
7753821	6	34	theme	c-Myc	1499:1503	arg1	mutations					1486:1494	mutations	1486:1494	mutations of c-Myc that are frequently found in Burkitt and AIDS-related lymphomas	1486:1567	Analyses of serial deletion mutants of c-Myc further suggest that the O-GlcNAc site(s) are located within or near the N-terminal transcription activation/malignant transformation domain, a region where mutations of c-Myc that are frequently found in Burkitt and AIDS-related lymphomas cluster.
7753821	5	35	theme	insect	1239:1244	arg1	cells					1246:1250	insect cells	1239:1250	insect cells	1239:1250	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	6	36	located	found	1525:1529	arg2	domain					1463:1468	the N-terminal transcription activation/malignant transformation domain	1398:1468	the N-terminal transcription activation/malignant transformation domain	1398:1468	Analyses of serial deletion mutants of c-Myc further suggest that the O-GlcNAc site(s) are located within or near the N-terminal transcription activation/malignant transformation domain, a region where mutations of c-Myc that are frequently found in Burkitt and AIDS-related lymphomas cluster.
7753821	6	36	located	found	1525:1529	arg1	lymphomas					1559:1567	Burkitt and AIDS-related lymphomas	1534:1567	lymphomas	1559:1567	Analyses of serial deletion mutants of c-Myc further suggest that the O-GlcNAc site(s) are located within or near the N-terminal transcription activation/malignant transformation domain, a region where mutations of c-Myc that are frequently found in Burkitt and AIDS-related lymphomas cluster.
7753821	6	36	located	found	1525:1529	arg2	region					1473:1478	a region	1471:1478	a region where mutations of c-Myc that are frequently found in Burkitt and AIDS-related lymphomas cluster	1471:1575	Analyses of serial deletion mutants of c-Myc further suggest that the O-GlcNAc site(s) are located within or near the N-terminal transcription activation/malignant transformation domain, a region where mutations of c-Myc that are frequently found in Burkitt and AIDS-related lymphomas cluster.
7753821	6	36	located	found	1525:1529	arg2	mutations					1486:1494	mutations	1486:1494	mutations of c-Myc that are frequently found in Burkitt and AIDS-related lymphomas	1486:1567	Analyses of serial deletion mutants of c-Myc further suggest that the O-GlcNAc site(s) are located within or near the N-terminal transcription activation/malignant transformation domain, a region where mutations of c-Myc that are frequently found in Burkitt and AIDS-related lymphomas cluster.
7753821	5	37	dep	methods	868:874	arg1	characterization					1144:1159	(iii) direct characterization	1131:1159	(iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells	1131:1281	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	5	37	dep	methods	868:874	arg1	methods					868:874	three different methods	852:874	three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells	852:1281	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	5	37	dep	methods	868:874	arg1	demonstration					881:893	(i) demonstration	877:893	(i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay	877:999	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	5	37	dep	methods	868:874	arg1	glycosidase					1007:1017	(ii) glycosidase	1002:1017	(ii) glycosidase	1002:1017	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	4	38	theme	neoplastic	791:800	arg1	cells					802:806	normal and neoplastic cells	780:806	normal and neoplastic cells	780:806	Here we present evidence for O-GlcNAc glycosylation of the oncoprotein c-Myc, a helix-loop-helix/leucine zipper phosphoprotein that heterodimerizes with Max and participates in the regulation of gene transcription in normal and neoplastic cells.
7753821	4	39	theme	helix-loop-helix/leucine	643:666	arg1	phosphoprotein					675:688	a helix-loop-helix/leucine zipper phosphoprotein	641:688	a helix-loop-helix/leucine zipper phosphoprotein that heterodimerizes with Max and participates in the regulation of gene transcription in normal and neoplastic cells	641:806	Here we present evidence for O-GlcNAc glycosylation of the oncoprotein c-Myc, a helix-loop-helix/leucine zipper phosphoprotein that heterodimerizes with Max and participates in the regulation of gene transcription in normal and neoplastic cells.
7753821	4	39	theme	helix-loop-helix/leucine	643:666	arg1	c-Myc					634:638	the oncoprotein c-Myc	618:638	the oncoprotein c-Myc	618:638	Here we present evidence for O-GlcNAc glycosylation of the oncoprotein c-Myc, a helix-loop-helix/leucine zipper phosphoprotein that heterodimerizes with Max and participates in the regulation of gene transcription in normal and neoplastic cells.
7753821	0	40	theme	domain	43:48	arg1	Glycosylation					0:12	Glycosylation	0:12	Glycosylation of the c-Myc transactivation domain	0:48	Glycosylation of the c-Myc transactivation domain.
7753821	1	41	theme	serine	306:311	arg1	hydroxyl					294:301	the side-chain hydroxyl	279:301	the side-chain hydroxyl of serine or threonine residues	279:333	O-linked N-acetylglucosamine (O-GlcNAc) is an abundant and dynamic posttranslational modification composed of a single monosaccharide, GlcNAc, glycosidically composed of a single monosaccharide, GlcNAc, glycosidically linked to the side-chain hydroxyl of serine or threonine residues.
7753821	0	42	gly	Glycosylation	0:12	arg1	domain					43:48	the c-Myc transactivation domain	17:48	the c-Myc transactivation domain	17:48	Glycosylation of the c-Myc transactivation domain.
7753821	0	43	theme	transactivation	27:41	arg1	domain					43:48	the c-Myc transactivation domain	17:48	the c-Myc transactivation domain	17:48	Glycosylation of the c-Myc transactivation domain.
7753821	5	44	theme	purified	1186:1193	arg1	protein					1207:1213	purified recombinant protein	1186:1213	purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells	1186:1281	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	5	45	theme	Chinese	1255:1261	arg1	cells					1277:1281	Chinese hamster ovary cells	1255:1281	Chinese hamster ovary cells	1255:1281	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	5	46	theme	translated	1064:1073	arg1	protein					1075:1081	in vitro translated protein	1055:1081	in vitro translated protein analyzed by lectin affinity chromatography	1055:1124	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	1	47	theme	single	223:228	arg1	GlcNAc					246:251	GlcNAc	246:251	GlcNAc	246:251	O-linked N-acetylglucosamine (O-GlcNAc) is an abundant and dynamic posttranslational modification composed of a single monosaccharide, GlcNAc, glycosidically composed of a single monosaccharide, GlcNAc, glycosidically linked to the side-chain hydroxyl of serine or threonine residues.
7753821	1	47	theme	single	223:228	arg1	monosaccharide					230:243	a single monosaccharide	221:243	a single monosaccharide	221:243	O-linked N-acetylglucosamine (O-GlcNAc) is an abundant and dynamic posttranslational modification composed of a single monosaccharide, GlcNAc, glycosidically composed of a single monosaccharide, GlcNAc, glycosidically linked to the side-chain hydroxyl of serine or threonine residues.
7753821	1	48	theme	threonine	316:324	arg1	hydroxyl					294:301	the side-chain hydroxyl	279:301	the side-chain hydroxyl of serine or threonine residues	279:333	O-linked N-acetylglucosamine (O-GlcNAc) is an abundant and dynamic posttranslational modification composed of a single monosaccharide, GlcNAc, glycosidically composed of a single monosaccharide, GlcNAc, glycosidically linked to the side-chain hydroxyl of serine or threonine residues.
7753821	5	49	theme	O-GlcNAc	809:816	arg1	modification					818:829	O-GlcNAc modification	809:829	O-GlcNAc modification of c-Myc	809:838	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	5	50	theme	protein	1075:1081	arg1	characterization					1144:1159	(iii) direct characterization	1131:1159	(iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells	1131:1281	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	5	50	theme	protein	1075:1081	arg1	methods					868:874	three different methods	852:874	three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells	852:1281	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	5	50	theme	protein	1075:1081	arg1	demonstration					881:893	(i) demonstration	877:893	(i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay	877:999	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	5	50	theme	protein	1075:1081	arg1	glycosidase					1007:1017	(ii) glycosidase	1002:1017	(ii) glycosidase	1002:1017	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	5	50	theme	protein	1075:1081	arg1	treatment					1042:1050	glycosyltransferase treatment	1022:1050	glycosyltransferase treatment	1022:1050	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	5	51	from	demonstration	881:893	arg1	protein					1207:1213	purified recombinant protein	1186:1213	purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells	1186:1281	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	1	52	theme	dynamic	110:116	arg1	modification					136:147	an abundant and dynamic posttranslational modification	94:147	an abundant and dynamic posttranslational modification composed of a single monosaccharide, GlcNAc, glycosidically composed of a single monosaccharide, GlcNAc, glycosidically linked to the side-chain hydroxyl of serine or threonine residues	94:333	O-linked N-acetylglucosamine (O-GlcNAc) is an abundant and dynamic posttranslational modification composed of a single monosaccharide, GlcNAc, glycosidically composed of a single monosaccharide, GlcNAc, glycosidically linked to the side-chain hydroxyl of serine or threonine residues.
7753821	1	52	theme	dynamic	110:116	arg1	N-acetylglucosamine					60:78	O-linked N-acetylglucosamine	51:78	O-linked N-acetylglucosamine (O-GlcNAc)	51:89	O-linked N-acetylglucosamine (O-GlcNAc) is an abundant and dynamic posttranslational modification composed of a single monosaccharide, GlcNAc, glycosidically composed of a single monosaccharide, GlcNAc, glycosidically linked to the side-chain hydroxyl of serine or threonine residues.
7753821	6	53	theme	site	1363:1366	arg1	s					1368:1368	the O-GlcNAc site(s)	1350:1369	the O-GlcNAc site(s)	1350:1369	Analyses of serial deletion mutants of c-Myc further suggest that the O-GlcNAc site(s) are located within or near the N-terminal transcription activation/malignant transformation domain, a region where mutations of c-Myc that are frequently found in Burkitt and AIDS-related lymphomas cluster.
7753821	6	53	theme	site	1363:1366	arg1	located					1375:1381	located	1375:1381	located	1375:1381	Analyses of serial deletion mutants of c-Myc further suggest that the O-GlcNAc site(s) are located within or near the N-terminal transcription activation/malignant transformation domain, a region where mutations of c-Myc that are frequently found in Burkitt and AIDS-related lymphomas cluster.
7753821	6	54	theme	mutants	1312:1318	arg1	Analyses					1284:1291	Analyses	1284:1291	Analyses of serial deletion mutants of c-Myc	1284:1327	Analyses of serial deletion mutants of c-Myc further suggest that the O-GlcNAc site(s) are located within or near the N-terminal transcription activation/malignant transformation domain, a region where mutations of c-Myc that are frequently found in Burkitt and AIDS-related lymphomas cluster.
7753821	5	55	dep	glycosidase	1007:1017	arg1	ii					1003:1004	ii	1003:1004	ii	1003:1004	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	1	56	theme	posttranslational	118:134	arg1	modification					136:147	an abundant and dynamic posttranslational modification	94:147	an abundant and dynamic posttranslational modification composed of a single monosaccharide, GlcNAc, glycosidically composed of a single monosaccharide, GlcNAc, glycosidically linked to the side-chain hydroxyl of serine or threonine residues	94:333	O-linked N-acetylglucosamine (O-GlcNAc) is an abundant and dynamic posttranslational modification composed of a single monosaccharide, GlcNAc, glycosidically composed of a single monosaccharide, GlcNAc, glycosidically linked to the side-chain hydroxyl of serine or threonine residues.
7753821	1	56	theme	posttranslational	118:134	arg1	N-acetylglucosamine					60:78	O-linked N-acetylglucosamine	51:78	O-linked N-acetylglucosamine (O-GlcNAc)	51:89	O-linked N-acetylglucosamine (O-GlcNAc) is an abundant and dynamic posttranslational modification composed of a single monosaccharide, GlcNAc, glycosidically composed of a single monosaccharide, GlcNAc, glycosidically linked to the side-chain hydroxyl of serine or threonine residues.
7753821	6	57	theme	AIDS-related	1546:1557	arg1	lymphomas					1559:1567	Burkitt and AIDS-related lymphomas	1534:1567	lymphomas	1559:1567	Analyses of serial deletion mutants of c-Myc further suggest that the O-GlcNAc site(s) are located within or near the N-terminal transcription activation/malignant transformation domain, a region where mutations of c-Myc that are frequently found in Burkitt and AIDS-related lymphomas cluster.
7753821	6	58	theme	O-GlcNAc	1354:1361	arg1	s					1368:1368	the O-GlcNAc site(s)	1350:1369	the O-GlcNAc site(s)	1350:1369	Analyses of serial deletion mutants of c-Myc further suggest that the O-GlcNAc site(s) are located within or near the N-terminal transcription activation/malignant transformation domain, a region where mutations of c-Myc that are frequently found in Burkitt and AIDS-related lymphomas cluster.
7753821	6	58	theme	O-GlcNAc	1354:1361	arg1	located					1375:1381	located	1375:1381	located	1375:1381	Analyses of serial deletion mutants of c-Myc further suggest that the O-GlcNAc site(s) are located within or near the N-terminal transcription activation/malignant transformation domain, a region where mutations of c-Myc that are frequently found in Burkitt and AIDS-related lymphomas cluster.
7753821	5	59	theme	lectin	1095:1100	arg1	chromatography					1111:1124	lectin affinity chromatography	1095:1124	lectin affinity chromatography	1095:1124	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	1	60	attach	linked	269:274	arg2	monosaccharide					230:243	a single monosaccharide	221:243	a single monosaccharide	221:243	O-linked N-acetylglucosamine (O-GlcNAc) is an abundant and dynamic posttranslational modification composed of a single monosaccharide, GlcNAc, glycosidically composed of a single monosaccharide, GlcNAc, glycosidically linked to the side-chain hydroxyl of serine or threonine residues.
7753821	1	60	attach	linked	269:274	arg1	hydroxyl					294:301	the side-chain hydroxyl	279:301	the side-chain hydroxyl of serine or threonine residues	279:333	O-linked N-acetylglucosamine (O-GlcNAc) is an abundant and dynamic posttranslational modification composed of a single monosaccharide, GlcNAc, glycosidically composed of a single monosaccharide, GlcNAc, glycosidically linked to the side-chain hydroxyl of serine or threonine residues.
7753821	1	60	attach	linked	269:274	arg2	GlcNAc					246:251	GlcNAc	246:251	GlcNAc	246:251	O-linked N-acetylglucosamine (O-GlcNAc) is an abundant and dynamic posttranslational modification composed of a single monosaccharide, GlcNAc, glycosidically composed of a single monosaccharide, GlcNAc, glycosidically linked to the side-chain hydroxyl of serine or threonine residues.
7753821	5	61	theme	protein-protein	952:966	arg1	assay					995:999	a protein-protein interaction mobility-shift assay	950:999	a protein-protein interaction mobility-shift assay	950:999	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	4	62	theme	c-Myc	634:638	arg1	glycosylation					601:613	O-GlcNAc glycosylation	592:613	O-GlcNAc glycosylation of the oncoprotein c-Myc, a helix-loop-helix/leucine zipper phosphoprotein that heterodimerizes with Max and participates in the regulation of gene transcription in normal and neoplastic cells	592:806	Here we present evidence for O-GlcNAc glycosylation of the oncoprotein c-Myc, a helix-loop-helix/leucine zipper phosphoprotein that heterodimerizes with Max and participates in the regulation of gene transcription in normal and neoplastic cells.
7753821	6	63	theme	N-terminal	1402:1411	arg1	domain					1463:1468	the N-terminal transcription activation/malignant transformation domain	1398:1468	the N-terminal transcription activation/malignant transformation domain	1398:1468	Analyses of serial deletion mutants of c-Myc further suggest that the O-GlcNAc site(s) are located within or near the N-terminal transcription activation/malignant transformation domain, a region where mutations of c-Myc that are frequently found in Burkitt and AIDS-related lymphomas cluster.
7753821	6	63	theme	N-terminal	1402:1411	arg1	region					1473:1478	a region	1471:1478	a region where mutations of c-Myc that are frequently found in Burkitt and AIDS-related lymphomas cluster	1471:1575	Analyses of serial deletion mutants of c-Myc further suggest that the O-GlcNAc site(s) are located within or near the N-terminal transcription activation/malignant transformation domain, a region where mutations of c-Myc that are frequently found in Burkitt and AIDS-related lymphomas cluster.
7753821	5	64	theme	affinity	1102:1109	arg1	chromatography					1111:1124	lectin affinity chromatography	1095:1124	lectin affinity chromatography	1095:1124	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	5	65	dep	demonstration	881:893	arg1	i					878:878	i	878:878	i	878:878	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	4	66	theme	transcription	763:775	arg1	regulation					744:753	the regulation	740:753	the regulation of gene transcription in normal and neoplastic cells	740:806	Here we present evidence for O-GlcNAc glycosylation of the oncoprotein c-Myc, a helix-loop-helix/leucine zipper phosphoprotein that heterodimerizes with Max and participates in the regulation of gene transcription in normal and neoplastic cells.
7753821	6	67	theme	Burkitt	1534:1540	arg1	lymphomas					1559:1567	Burkitt and AIDS-related lymphomas	1534:1567	lymphomas	1559:1567	Analyses of serial deletion mutants of c-Myc further suggest that the O-GlcNAc site(s) are located within or near the N-terminal transcription activation/malignant transformation domain, a region where mutations of c-Myc that are frequently found in Burkitt and AIDS-related lymphomas cluster.
7753821	4	68	theme	oncoprotein	622:632	arg1	phosphoprotein					675:688	a helix-loop-helix/leucine zipper phosphoprotein	641:688	a helix-loop-helix/leucine zipper phosphoprotein that heterodimerizes with Max and participates in the regulation of gene transcription in normal and neoplastic cells	641:806	Here we present evidence for O-GlcNAc glycosylation of the oncoprotein c-Myc, a helix-loop-helix/leucine zipper phosphoprotein that heterodimerizes with Max and participates in the regulation of gene transcription in normal and neoplastic cells.
7753821	4	68	theme	oncoprotein	622:632	arg1	c-Myc					634:638	the oncoprotein c-Myc	618:638	the oncoprotein c-Myc	618:638	Here we present evidence for O-GlcNAc glycosylation of the oncoprotein c-Myc, a helix-loop-helix/leucine zipper phosphoprotein that heterodimerizes with Max and participates in the regulation of gene transcription in normal and neoplastic cells.
7753821	6	69	theme	transformation	1448:1461	arg1	domain					1463:1468	the N-terminal transcription activation/malignant transformation domain	1398:1468	the N-terminal transcription activation/malignant transformation domain	1398:1468	Analyses of serial deletion mutants of c-Myc further suggest that the O-GlcNAc site(s) are located within or near the N-terminal transcription activation/malignant transformation domain, a region where mutations of c-Myc that are frequently found in Burkitt and AIDS-related lymphomas cluster.
7753821	6	69	theme	transformation	1448:1461	arg1	region					1473:1478	a region	1471:1478	a region where mutations of c-Myc that are frequently found in Burkitt and AIDS-related lymphomas cluster	1471:1575	Analyses of serial deletion mutants of c-Myc further suggest that the O-GlcNAc site(s) are located within or near the N-terminal transcription activation/malignant transformation domain, a region where mutations of c-Myc that are frequently found in Burkitt and AIDS-related lymphomas cluster.
7753821	3	70	mod	modified	493:500	arg3	phosphorylation					505:519	phosphorylation	505:519	phosphorylation	505:519	These O-GlcNAc-bearing proteins are also modified by phosphorylation and form reversible multimeric complexes.
7753821	3	70	mod	modified	493:500	arg1	proteins					475:482	These O-GlcNAc-bearing proteins	452:482	These O-GlcNAc-bearing proteins	452:482	These O-GlcNAc-bearing proteins are also modified by phosphorylation and form reversible multimeric complexes.
7753821	6	71	theme	activation/malignant	1427:1446	arg1	domain					1463:1468	the N-terminal transcription activation/malignant transformation domain	1398:1468	the N-terminal transcription activation/malignant transformation domain	1398:1468	Analyses of serial deletion mutants of c-Myc further suggest that the O-GlcNAc site(s) are located within or near the N-terminal transcription activation/malignant transformation domain, a region where mutations of c-Myc that are frequently found in Burkitt and AIDS-related lymphomas cluster.
7753821	6	71	theme	activation/malignant	1427:1446	arg1	region					1473:1478	a region	1471:1478	a region where mutations of c-Myc that are frequently found in Burkitt and AIDS-related lymphomas cluster	1471:1575	Analyses of serial deletion mutants of c-Myc further suggest that the O-GlcNAc site(s) are located within or near the N-terminal transcription activation/malignant transformation domain, a region where mutations of c-Myc that are frequently found in Burkitt and AIDS-related lymphomas cluster.
7753821	4	72	theme	zipper	668:673	arg1	phosphoprotein					675:688	a helix-loop-helix/leucine zipper phosphoprotein	641:688	a helix-loop-helix/leucine zipper phosphoprotein that heterodimerizes with Max and participates in the regulation of gene transcription in normal and neoplastic cells	641:806	Here we present evidence for O-GlcNAc glycosylation of the oncoprotein c-Myc, a helix-loop-helix/leucine zipper phosphoprotein that heterodimerizes with Max and participates in the regulation of gene transcription in normal and neoplastic cells.
7753821	4	72	theme	zipper	668:673	arg1	c-Myc					634:638	the oncoprotein c-Myc	618:638	the oncoprotein c-Myc	618:638	Here we present evidence for O-GlcNAc glycosylation of the oncoprotein c-Myc, a helix-loop-helix/leucine zipper phosphoprotein that heterodimerizes with Max and participates in the regulation of gene transcription in normal and neoplastic cells.
7753821	2	73	theme	nuclear	376:382	arg1	proteins					400:407	nuclear and cytoplasmic proteins	376:407	nuclear and cytoplasmic proteins	376:407	Although O-GlcNAc occurs on a myriad of nuclear and cytoplasmic proteins, only a few have thus far been identified.
7753821	5	74	theme	lectin	898:903	arg1	binding					905:911	lectin binding	898:911	lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay	898:999	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	5	75	dep	characterization	1144:1159	arg1	iii					1132:1134	iii	1132:1134	iii	1132:1134	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	5	76	theme	glycosyltransferase	1022:1040	arg1	methods					868:874	three different methods	852:874	three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells	852:1281	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	5	76	theme	glycosyltransferase	1022:1040	arg1	treatment					1042:1050	glycosyltransferase treatment	1022:1050	glycosyltransferase treatment	1022:1050	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
7753821	1	77	theme	O-linked	51:58	arg1	O-GlcNAc					81:88	O-GlcNAc	81:88	O-GlcNAc	81:88	O-linked N-acetylglucosamine (O-GlcNAc) is an abundant and dynamic posttranslational modification composed of a single monosaccharide, GlcNAc, glycosidically composed of a single monosaccharide, GlcNAc, glycosidically linked to the side-chain hydroxyl of serine or threonine residues.
7753821	1	77	theme	O-linked	51:58	arg1	modification					136:147	an abundant and dynamic posttranslational modification	94:147	an abundant and dynamic posttranslational modification composed of a single monosaccharide, GlcNAc, glycosidically composed of a single monosaccharide, GlcNAc, glycosidically linked to the side-chain hydroxyl of serine or threonine residues	94:333	O-linked N-acetylglucosamine (O-GlcNAc) is an abundant and dynamic posttranslational modification composed of a single monosaccharide, GlcNAc, glycosidically composed of a single monosaccharide, GlcNAc, glycosidically linked to the side-chain hydroxyl of serine or threonine residues.
7753821	1	77	theme	O-linked	51:58	arg1	N-acetylglucosamine					60:78	O-linked N-acetylglucosamine	51:78	O-linked N-acetylglucosamine (O-GlcNAc)	51:89	O-linked N-acetylglucosamine (O-GlcNAc) is an abundant and dynamic posttranslational modification composed of a single monosaccharide, GlcNAc, glycosidically composed of a single monosaccharide, GlcNAc, glycosidically linked to the side-chain hydroxyl of serine or threonine residues.
7753821	3	78	theme	reversible	530:539	arg1	complexes					552:560	reversible multimeric complexes	530:560	reversible multimeric complexes	530:560	These O-GlcNAc-bearing proteins are also modified by phosphorylation and form reversible multimeric complexes.
7753821	4	79	from	regulation	744:753	arg1	cells					802:806	normal and neoplastic cells	780:806	normal and neoplastic cells	780:806	Here we present evidence for O-GlcNAc glycosylation of the oncoprotein c-Myc, a helix-loop-helix/leucine zipper phosphoprotein that heterodimerizes with Max and participates in the regulation of gene transcription in normal and neoplastic cells.
7753821	5	80	theme	recombinant	1195:1205	arg1	protein					1207:1213	purified recombinant protein	1186:1213	purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells	1186:1281	O-GlcNAc modification of c-Myc is shown by three different methods: (i) demonstration of lectin binding to in vitro translated protein using a protein-protein interaction mobility-shift assay; (ii) glycosidase or glycosyltransferase treatment of in vitro translated protein analyzed by lectin affinity chromatography; and (iii) direct characterization of the sugar moieties on purified recombinant protein overexpressed in either insect cells or Chinese hamster ovary cells.
16750161	3	0	theme	O-linked	643:650	arg1	protein					574:580	The 108-amino acid CHO-expressed protein	541:580	The 108-amino acid CHO-expressed protein	541:580	The 108-amino acid CHO-expressed protein was examined by tryptic mapping and LC-MS and found to be an O-linked glycoprotein.
16750161	3	0	theme	O-linked	643:650	arg1	glycoprotein					652:663	an O-linked glycoprotein	640:663	an O-linked glycoprotein	640:663	The 108-amino acid CHO-expressed protein was examined by tryptic mapping and LC-MS and found to be an O-linked glycoprotein.
16750161	1	1	theme	B-type	138:143	arg1	BNP					166:168	BNP	166:168	BNP	166:168	Human pro-B-type natriuretic peptide (proBNP), the precursor for B-type natriuretic peptide (BNP), was expressed in Chinese hamster ovary cells (CHO) and compared by Western blot analysis to BNP cross-reacting material immunoprecipitated from the plasma of heart failure patients.
16750161	1	1	theme	B-type	138:143	arg1	peptide					157:163	B-type natriuretic peptide	138:163	B-type natriuretic peptide (BNP)	138:169	Human pro-B-type natriuretic peptide (proBNP), the precursor for B-type natriuretic peptide (BNP), was expressed in Chinese hamster ovary cells (CHO) and compared by Western blot analysis to BNP cross-reacting material immunoprecipitated from the plasma of heart failure patients.
16750161	5	2	theme	isoforms	1025:1032	arg1	observations					985:996	previous observations	976:996	previous observations of higher molecular weight isoforms of BNP	976:1039	This data is consistent with previous observations of higher molecular weight isoforms of BNP.
16750161	1	3	theme	natriuretic	145:155	arg1	BNP					166:168	BNP	166:168	BNP	166:168	Human pro-B-type natriuretic peptide (proBNP), the precursor for B-type natriuretic peptide (BNP), was expressed in Chinese hamster ovary cells (CHO) and compared by Western blot analysis to BNP cross-reacting material immunoprecipitated from the plasma of heart failure patients.
16750161	1	3	theme	natriuretic	145:155	arg1	peptide					157:163	B-type natriuretic peptide	138:163	B-type natriuretic peptide (BNP)	138:169	Human pro-B-type natriuretic peptide (proBNP), the precursor for B-type natriuretic peptide (BNP), was expressed in Chinese hamster ovary cells (CHO) and compared by Western blot analysis to BNP cross-reacting material immunoprecipitated from the plasma of heart failure patients.
16750161	3	4	theme	tryptic	598:604	arg1	mapping					606:612	tryptic mapping	598:612	tryptic mapping	598:612	The 108-amino acid CHO-expressed protein was examined by tryptic mapping and LC-MS and found to be an O-linked glycoprotein.
16750161	3	5	gly	glycoprotein	652:663	arg1	protein					574:580	The 108-amino acid CHO-expressed protein	541:580	The 108-amino acid CHO-expressed protein	541:580	The 108-amino acid CHO-expressed protein was examined by tryptic mapping and LC-MS and found to be an O-linked glycoprotein.
16750161	3	5	gly	glycoprotein	652:663	arg1	glycoprotein					652:663	an O-linked glycoprotein	640:663	an O-linked glycoprotein	640:663	The 108-amino acid CHO-expressed protein was examined by tryptic mapping and LC-MS and found to be an O-linked glycoprotein.
16750161	2	6	theme	kDa	466:468	arg1	species					470:476	a 12 kDa species	461:476	a 12 kDa species	461:476	Both recombinant and native forms co-migrated as a diffuse band centered around 25 kDa and were reduced to a 12 kDa species by treatment with a mixture of O-link deglycosylation enzymes.
16750161	5	7	theme	BNP	1037:1039	arg1	isoforms					1025:1032	higher molecular weight isoforms	1001:1032	higher molecular weight isoforms of BNP	1001:1039	This data is consistent with previous observations of higher molecular weight isoforms of BNP.
16750161	2	8	theme	enzymes	532:538	arg1	mixture					498:504	a mixture	496:504	a mixture of O-link deglycosylation enzymes	496:538	Both recombinant and native forms co-migrated as a diffuse band centered around 25 kDa and were reduced to a 12 kDa species by treatment with a mixture of O-link deglycosylation enzymes.
16750161	0	9	gly	glycoprotein	59:70	arg1	glycoprotein					59:70	an O-linked glycoprotein	47:70	an O-linked glycoprotein	47:70	The precursor to B-type natriuretic peptide is an O-linked glycoprotein.
16750161	0	9	gly	glycoprotein	59:70	arg1	precursor					4:12	The precursor	0:12	The precursor to B-type natriuretic peptide	0:42	The precursor to B-type natriuretic peptide is an O-linked glycoprotein.
16750161	2	10	theme	12	463:464	arg1	kDa					466:468	kDa	466:468	kDa	466:468	Both recombinant and native forms co-migrated as a diffuse band centered around 25 kDa and were reduced to a 12 kDa species by treatment with a mixture of O-link deglycosylation enzymes.
16750161	4	11	theme	sites	687:691	arg1	Determination					666:678	Determination	666:678	Determination of the sites of O-glycosyl addition by blank cycle sequencing of tryptic and Glu-C (Staphylococcus aureus V8 protease) peptides	666:806	Determination of the sites of O-glycosyl addition by blank cycle sequencing of tryptic and Glu-C (Staphylococcus aureus V8 protease) peptides showed that there are seven sites of glycosylation confined to a 36-amino acid residue stretch within the center of the propeptide region.
16750161	4	12	theme	cycle	725:729	arg1	sequencing					731:740	blank cycle sequencing	719:740	blank cycle sequencing of tryptic and Glu-C (Staphylococcus aureus V8 protease) peptides	719:806	Determination of the sites of O-glycosyl addition by blank cycle sequencing of tryptic and Glu-C (Staphylococcus aureus V8 protease) peptides showed that there are seven sites of glycosylation confined to a 36-amino acid residue stretch within the center of the propeptide region.
16750161	2	13	theme	recombinant	359:369	arg1	forms					382:386	Both recombinant and native forms	354:386	Both recombinant and native forms	354:386	Both recombinant and native forms co-migrated as a diffuse band centered around 25 kDa and were reduced to a 12 kDa species by treatment with a mixture of O-link deglycosylation enzymes.
16750161	1	14	theme	heart	330:334	arg1	failure					336:342	heart failure	330:342	heart failure patients	330:351	Human pro-B-type natriuretic peptide (proBNP), the precursor for B-type natriuretic peptide (BNP), was expressed in Chinese hamster ovary cells (CHO) and compared by Western blot analysis to BNP cross-reacting material immunoprecipitated from the plasma of heart failure patients.
16750161	4	15	theme	V8	786:787	arg1	tryptic					745:751	tryptic	745:751	tryptic	745:751	Determination of the sites of O-glycosyl addition by blank cycle sequencing of tryptic and Glu-C (Staphylococcus aureus V8 protease) peptides showed that there are seven sites of glycosylation confined to a 36-amino acid residue stretch within the center of the propeptide region.
16750161	4	15	theme	V8	786:787	arg1	protease					789:796	Staphylococcus aureus V8 protease	764:796	Staphylococcus aureus V8 protease	764:796	Determination of the sites of O-glycosyl addition by blank cycle sequencing of tryptic and Glu-C (Staphylococcus aureus V8 protease) peptides showed that there are seven sites of glycosylation confined to a 36-amino acid residue stretch within the center of the propeptide region.
16750161	1	16	theme	Human	73:77	arg1	proBNP					111:116	proBNP	111:116	proBNP	111:116	Human pro-B-type natriuretic peptide (proBNP), the precursor for B-type natriuretic peptide (BNP), was expressed in Chinese hamster ovary cells (CHO) and compared by Western blot analysis to BNP cross-reacting material immunoprecipitated from the plasma of heart failure patients.
16750161	1	16	theme	Human	73:77	arg1	peptide					102:108	Human pro-B-type natriuretic peptide	73:108	Human pro-B-type natriuretic peptide (proBNP)	73:117	Human pro-B-type natriuretic peptide (proBNP), the precursor for B-type natriuretic peptide (BNP), was expressed in Chinese hamster ovary cells (CHO) and compared by Western blot analysis to BNP cross-reacting material immunoprecipitated from the plasma of heart failure patients.
16750161	1	16	theme	Human	73:77	arg1	precursor					124:132	the precursor	120:132	the precursor for B-type natriuretic peptide (BNP)	120:169	Human pro-B-type natriuretic peptide (proBNP), the precursor for B-type natriuretic peptide (BNP), was expressed in Chinese hamster ovary cells (CHO) and compared by Western blot analysis to BNP cross-reacting material immunoprecipitated from the plasma of heart failure patients.
16750161	1	17	theme	failure	336:342	arg1	patients					344:351	heart failure patients	330:351	heart failure patients	330:351	Human pro-B-type natriuretic peptide (proBNP), the precursor for B-type natriuretic peptide (BNP), was expressed in Chinese hamster ovary cells (CHO) and compared by Western blot analysis to BNP cross-reacting material immunoprecipitated from the plasma of heart failure patients.
16750161	4	18	theme	peptides	799:806	arg1	sequencing					731:740	blank cycle sequencing	719:740	blank cycle sequencing of tryptic and Glu-C (Staphylococcus aureus V8 protease) peptides	719:806	Determination of the sites of O-glycosyl addition by blank cycle sequencing of tryptic and Glu-C (Staphylococcus aureus V8 protease) peptides showed that there are seven sites of glycosylation confined to a 36-amino acid residue stretch within the center of the propeptide region.
16750161	1	19	theme	pro-B-type	79:88	arg1	proBNP					111:116	proBNP	111:116	proBNP	111:116	Human pro-B-type natriuretic peptide (proBNP), the precursor for B-type natriuretic peptide (BNP), was expressed in Chinese hamster ovary cells (CHO) and compared by Western blot analysis to BNP cross-reacting material immunoprecipitated from the plasma of heart failure patients.
16750161	1	19	theme	pro-B-type	79:88	arg1	peptide					102:108	Human pro-B-type natriuretic peptide	73:108	Human pro-B-type natriuretic peptide (proBNP)	73:117	Human pro-B-type natriuretic peptide (proBNP), the precursor for B-type natriuretic peptide (BNP), was expressed in Chinese hamster ovary cells (CHO) and compared by Western blot analysis to BNP cross-reacting material immunoprecipitated from the plasma of heart failure patients.
16750161	1	19	theme	pro-B-type	79:88	arg1	precursor					124:132	the precursor	120:132	the precursor for B-type natriuretic peptide (BNP)	120:169	Human pro-B-type natriuretic peptide (proBNP), the precursor for B-type natriuretic peptide (BNP), was expressed in Chinese hamster ovary cells (CHO) and compared by Western blot analysis to BNP cross-reacting material immunoprecipitated from the plasma of heart failure patients.
16750161	2	20	theme	diffuse	405:411	arg1	band					413:416	a diffuse band	403:416	a diffuse band centered around 25 kDa	403:439	Both recombinant and native forms co-migrated as a diffuse band centered around 25 kDa and were reduced to a 12 kDa species by treatment with a mixture of O-link deglycosylation enzymes.
16750161	5	21	with	consistent	960:969	arg1	observations					985:996	previous observations	976:996	previous observations of higher molecular weight isoforms of BNP	976:1039	This data is consistent with previous observations of higher molecular weight isoforms of BNP.
16750161	1	22	theme	natriuretic	90:100	arg1	proBNP					111:116	proBNP	111:116	proBNP	111:116	Human pro-B-type natriuretic peptide (proBNP), the precursor for B-type natriuretic peptide (BNP), was expressed in Chinese hamster ovary cells (CHO) and compared by Western blot analysis to BNP cross-reacting material immunoprecipitated from the plasma of heart failure patients.
16750161	1	22	theme	natriuretic	90:100	arg1	peptide					102:108	Human pro-B-type natriuretic peptide	73:108	Human pro-B-type natriuretic peptide (proBNP)	73:117	Human pro-B-type natriuretic peptide (proBNP), the precursor for B-type natriuretic peptide (BNP), was expressed in Chinese hamster ovary cells (CHO) and compared by Western blot analysis to BNP cross-reacting material immunoprecipitated from the plasma of heart failure patients.
16750161	1	22	theme	natriuretic	90:100	arg1	precursor					124:132	the precursor	120:132	the precursor for B-type natriuretic peptide (BNP)	120:169	Human pro-B-type natriuretic peptide (proBNP), the precursor for B-type natriuretic peptide (BNP), was expressed in Chinese hamster ovary cells (CHO) and compared by Western blot analysis to BNP cross-reacting material immunoprecipitated from the plasma of heart failure patients.
16750161	0	23	theme	B-type	17:22	arg1	peptide					36:42	B-type natriuretic peptide	17:42	B-type natriuretic peptide	17:42	The precursor to B-type natriuretic peptide is an O-linked glycoprotein.
16750161	4	24	theme	O-glycosyl	696:705	arg1	addition					707:714	O-glycosyl addition	696:714	O-glycosyl addition	696:714	Determination of the sites of O-glycosyl addition by blank cycle sequencing of tryptic and Glu-C (Staphylococcus aureus V8 protease) peptides showed that there are seven sites of glycosylation confined to a 36-amino acid residue stretch within the center of the propeptide region.
16750161	1	25	theme	Western	239:245	arg1	analysis					252:259	Western blot analysis	239:259	Western blot analysis to BNP cross-reacting material immunoprecipitated from the plasma of heart failure patients	239:351	Human pro-B-type natriuretic peptide (proBNP), the precursor for B-type natriuretic peptide (BNP), was expressed in Chinese hamster ovary cells (CHO) and compared by Western blot analysis to BNP cross-reacting material immunoprecipitated from the plasma of heart failure patients.
16750161	1	26	theme	patients	344:351	arg1	plasma					320:325	the plasma	316:325	the plasma of heart failure patients	316:351	Human pro-B-type natriuretic peptide (proBNP), the precursor for B-type natriuretic peptide (BNP), was expressed in Chinese hamster ovary cells (CHO) and compared by Western blot analysis to BNP cross-reacting material immunoprecipitated from the plasma of heart failure patients.
16750161	4	27	gly	glycosylation	845:857	arg2	glycosylation					845:857	glycosylation	845:857	glycosylation confined to a 36-amino acid residue stretch within the center of the propeptide region	845:944	Determination of the sites of O-glycosyl addition by blank cycle sequencing of tryptic and Glu-C (Staphylococcus aureus V8 protease) peptides showed that there are seven sites of glycosylation confined to a 36-amino acid residue stretch within the center of the propeptide region.
16750161	4	27	gly	glycosylation	845:857	arg2	sites					836:840	seven sites	830:840	seven sites of glycosylation confined to a 36-amino acid residue stretch within the center of the propeptide region	830:944	Determination of the sites of O-glycosyl addition by blank cycle sequencing of tryptic and Glu-C (Staphylococcus aureus V8 protease) peptides showed that there are seven sites of glycosylation confined to a 36-amino acid residue stretch within the center of the propeptide region.
16750161	4	28	theme	region	939:944	arg1	center					914:919	the center	910:919	the center of the propeptide region	910:944	Determination of the sites of O-glycosyl addition by blank cycle sequencing of tryptic and Glu-C (Staphylococcus aureus V8 protease) peptides showed that there are seven sites of glycosylation confined to a 36-amino acid residue stretch within the center of the propeptide region.
16750161	1	29	theme	blot	247:250	arg1	analysis					252:259	Western blot analysis	239:259	Western blot analysis to BNP cross-reacting material immunoprecipitated from the plasma of heart failure patients	239:351	Human pro-B-type natriuretic peptide (proBNP), the precursor for B-type natriuretic peptide (BNP), was expressed in Chinese hamster ovary cells (CHO) and compared by Western blot analysis to BNP cross-reacting material immunoprecipitated from the plasma of heart failure patients.
16750161	4	30	theme	36-amino	873:880	arg1	stretch					895:901	a 36-amino acid residue stretch	871:901	a 36-amino acid residue stretch within the center of the propeptide region	871:944	Determination of the sites of O-glycosyl addition by blank cycle sequencing of tryptic and Glu-C (Staphylococcus aureus V8 protease) peptides showed that there are seven sites of glycosylation confined to a 36-amino acid residue stretch within the center of the propeptide region.
16750161	5	31	theme	weight	1018:1023	arg1	isoforms					1025:1032	higher molecular weight isoforms	1001:1032	higher molecular weight isoforms of BNP	1001:1039	This data is consistent with previous observations of higher molecular weight isoforms of BNP.
16750161	3	32	link	O-linked	643:650	arg1	protein					574:580	The 108-amino acid CHO-expressed protein	541:580	The 108-amino acid CHO-expressed protein	541:580	The 108-amino acid CHO-expressed protein was examined by tryptic mapping and LC-MS and found to be an O-linked glycoprotein.
16750161	3	32	link	O-linked	643:650	arg1	glycoprotein					652:663	an O-linked glycoprotein	640:663	an O-linked glycoprotein	640:663	The 108-amino acid CHO-expressed protein was examined by tryptic mapping and LC-MS and found to be an O-linked glycoprotein.
16750161	2	33	theme	native	375:380	arg1	forms					382:386	Both recombinant and native forms	354:386	Both recombinant and native forms	354:386	Both recombinant and native forms co-migrated as a diffuse band centered around 25 kDa and were reduced to a 12 kDa species by treatment with a mixture of O-link deglycosylation enzymes.
16750161	0	34	theme	natriuretic	24:34	arg1	peptide					36:42	B-type natriuretic peptide	17:42	B-type natriuretic peptide	17:42	The precursor to B-type natriuretic peptide is an O-linked glycoprotein.
16750161	4	35	theme	propeptide	928:937	arg1	region					939:944	the propeptide region	924:944	the propeptide region	924:944	Determination of the sites of O-glycosyl addition by blank cycle sequencing of tryptic and Glu-C (Staphylococcus aureus V8 protease) peptides showed that there are seven sites of glycosylation confined to a 36-amino acid residue stretch within the center of the propeptide region.
16750161	4	36	theme	addition	707:714	arg1	sites					687:691	the sites	683:691	the sites of O-glycosyl addition	683:714	Determination of the sites of O-glycosyl addition by blank cycle sequencing of tryptic and Glu-C (Staphylococcus aureus V8 protease) peptides showed that there are seven sites of glycosylation confined to a 36-amino acid residue stretch within the center of the propeptide region.
16750161	4	36	theme	addition	707:714	arg1	addition					707:714	O-glycosyl addition	696:714	O-glycosyl addition	696:714	Determination of the sites of O-glycosyl addition by blank cycle sequencing of tryptic and Glu-C (Staphylococcus aureus V8 protease) peptides showed that there are seven sites of glycosylation confined to a 36-amino acid residue stretch within the center of the propeptide region.
16750161	3	37	theme	108-amino	545:553	arg1	protein					574:580	The 108-amino acid CHO-expressed protein	541:580	The 108-amino acid CHO-expressed protein	541:580	The 108-amino acid CHO-expressed protein was examined by tryptic mapping and LC-MS and found to be an O-linked glycoprotein.
16750161	3	37	theme	108-amino	545:553	arg1	glycoprotein					652:663	an O-linked glycoprotein	640:663	an O-linked glycoprotein	640:663	The 108-amino acid CHO-expressed protein was examined by tryptic mapping and LC-MS and found to be an O-linked glycoprotein.
16750161	5	38	theme	molecular	1008:1016	arg1	isoforms					1025:1032	higher molecular weight isoforms	1001:1032	higher molecular weight isoforms of BNP	1001:1039	This data is consistent with previous observations of higher molecular weight isoforms of BNP.
16750161	4	39	theme	residue	887:893	arg1	stretch					895:901	a 36-amino acid residue stretch	871:901	a 36-amino acid residue stretch within the center of the propeptide region	871:944	Determination of the sites of O-glycosyl addition by blank cycle sequencing of tryptic and Glu-C (Staphylococcus aureus V8 protease) peptides showed that there are seven sites of glycosylation confined to a 36-amino acid residue stretch within the center of the propeptide region.
16750161	2	40	theme	deglycosylation	516:530	arg1	enzymes					532:538	O-link deglycosylation enzymes	509:538	O-link deglycosylation enzymes	509:538	Both recombinant and native forms co-migrated as a diffuse band centered around 25 kDa and were reduced to a 12 kDa species by treatment with a mixture of O-link deglycosylation enzymes.
16750161	4	41	theme	aureus	779:784	arg1	tryptic					745:751	tryptic	745:751	tryptic	745:751	Determination of the sites of O-glycosyl addition by blank cycle sequencing of tryptic and Glu-C (Staphylococcus aureus V8 protease) peptides showed that there are seven sites of glycosylation confined to a 36-amino acid residue stretch within the center of the propeptide region.
16750161	4	41	theme	aureus	779:784	arg1	protease					789:796	Staphylococcus aureus V8 protease	764:796	Staphylococcus aureus V8 protease	764:796	Determination of the sites of O-glycosyl addition by blank cycle sequencing of tryptic and Glu-C (Staphylococcus aureus V8 protease) peptides showed that there are seven sites of glycosylation confined to a 36-amino acid residue stretch within the center of the propeptide region.
16750161	2	42	theme	O-link	509:514	arg1	enzymes					532:538	O-link deglycosylation enzymes	509:538	O-link deglycosylation enzymes	509:538	Both recombinant and native forms co-migrated as a diffuse band centered around 25 kDa and were reduced to a 12 kDa species by treatment with a mixture of O-link deglycosylation enzymes.
16750161	5	43	theme	previous	976:983	arg1	observations					985:996	previous observations	976:996	previous observations of higher molecular weight isoforms of BNP	976:1039	This data is consistent with previous observations of higher molecular weight isoforms of BNP.
16750161	4	44	theme	Staphylococcus	764:777	arg1	tryptic					745:751	tryptic	745:751	tryptic	745:751	Determination of the sites of O-glycosyl addition by blank cycle sequencing of tryptic and Glu-C (Staphylococcus aureus V8 protease) peptides showed that there are seven sites of glycosylation confined to a 36-amino acid residue stretch within the center of the propeptide region.
16750161	4	44	theme	Staphylococcus	764:777	arg1	protease					789:796	Staphylococcus aureus V8 protease	764:796	Staphylococcus aureus V8 protease	764:796	Determination of the sites of O-glycosyl addition by blank cycle sequencing of tryptic and Glu-C (Staphylococcus aureus V8 protease) peptides showed that there are seven sites of glycosylation confined to a 36-amino acid residue stretch within the center of the propeptide region.
16750161	4	45	theme	Glu-C	757:761	arg1	peptides					799:806	tryptic and Glu-C (Staphylococcus aureus V8 protease) peptides	745:806	tryptic and Glu-C (Staphylococcus aureus V8 protease) peptides	745:806	Determination of the sites of O-glycosyl addition by blank cycle sequencing of tryptic and Glu-C (Staphylococcus aureus V8 protease) peptides showed that there are seven sites of glycosylation confined to a 36-amino acid residue stretch within the center of the propeptide region.
16750161	2	46	with	treatment	481:489	arg1	mixture					498:504	a mixture	496:504	a mixture of O-link deglycosylation enzymes	496:538	Both recombinant and native forms co-migrated as a diffuse band centered around 25 kDa and were reduced to a 12 kDa species by treatment with a mixture of O-link deglycosylation enzymes.
16750161	4	47	theme	tryptic	745:751	arg1	peptides					799:806	tryptic and Glu-C (Staphylococcus aureus V8 protease) peptides	745:806	tryptic and Glu-C (Staphylococcus aureus V8 protease) peptides	745:806	Determination of the sites of O-glycosyl addition by blank cycle sequencing of tryptic and Glu-C (Staphylococcus aureus V8 protease) peptides showed that there are seven sites of glycosylation confined to a 36-amino acid residue stretch within the center of the propeptide region.
16750161	4	48	theme	glycosylation	845:857	arg1	glycosylation					845:857	glycosylation	845:857	glycosylation confined to a 36-amino acid residue stretch within the center of the propeptide region	845:944	Determination of the sites of O-glycosyl addition by blank cycle sequencing of tryptic and Glu-C (Staphylococcus aureus V8 protease) peptides showed that there are seven sites of glycosylation confined to a 36-amino acid residue stretch within the center of the propeptide region.
16750161	4	48	theme	glycosylation	845:857	arg1	sites					836:840	seven sites	830:840	seven sites of glycosylation confined to a 36-amino acid residue stretch within the center of the propeptide region	830:944	Determination of the sites of O-glycosyl addition by blank cycle sequencing of tryptic and Glu-C (Staphylococcus aureus V8 protease) peptides showed that there are seven sites of glycosylation confined to a 36-amino acid residue stretch within the center of the propeptide region.
16750161	0	49	link	O-linked	50:57	arg1	glycoprotein					59:70	an O-linked glycoprotein	47:70	an O-linked glycoprotein	47:70	The precursor to B-type natriuretic peptide is an O-linked glycoprotein.
16750161	0	49	link	O-linked	50:57	arg1	precursor					4:12	The precursor	0:12	The precursor to B-type natriuretic peptide	0:42	The precursor to B-type natriuretic peptide is an O-linked glycoprotein.
16750161	1	50	theme	Chinese	189:195	arg1	CHO					218:220	CHO	218:220	CHO	218:220	Human pro-B-type natriuretic peptide (proBNP), the precursor for B-type natriuretic peptide (BNP), was expressed in Chinese hamster ovary cells (CHO) and compared by Western blot analysis to BNP cross-reacting material immunoprecipitated from the plasma of heart failure patients.
16750161	1	50	theme	Chinese	189:195	arg1	cells					211:215	Chinese hamster ovary cells	189:215	Chinese hamster ovary cells (CHO)	189:221	Human pro-B-type natriuretic peptide (proBNP), the precursor for B-type natriuretic peptide (BNP), was expressed in Chinese hamster ovary cells (CHO) and compared by Western blot analysis to BNP cross-reacting material immunoprecipitated from the plasma of heart failure patients.
16750161	4	51	theme	blank	719:723	arg1	sequencing					731:740	blank cycle sequencing	719:740	blank cycle sequencing of tryptic and Glu-C (Staphylococcus aureus V8 protease) peptides	719:806	Determination of the sites of O-glycosyl addition by blank cycle sequencing of tryptic and Glu-C (Staphylococcus aureus V8 protease) peptides showed that there are seven sites of glycosylation confined to a 36-amino acid residue stretch within the center of the propeptide region.
16750161	1	52	theme	hamster	197:203	arg1	CHO					218:220	CHO	218:220	CHO	218:220	Human pro-B-type natriuretic peptide (proBNP), the precursor for B-type natriuretic peptide (BNP), was expressed in Chinese hamster ovary cells (CHO) and compared by Western blot analysis to BNP cross-reacting material immunoprecipitated from the plasma of heart failure patients.
16750161	1	52	theme	hamster	197:203	arg1	cells					211:215	Chinese hamster ovary cells	189:215	Chinese hamster ovary cells (CHO)	189:221	Human pro-B-type natriuretic peptide (proBNP), the precursor for B-type natriuretic peptide (BNP), was expressed in Chinese hamster ovary cells (CHO) and compared by Western blot analysis to BNP cross-reacting material immunoprecipitated from the plasma of heart failure patients.
16750161	5	53	theme	higher	1001:1006	arg1	isoforms					1025:1032	higher molecular weight isoforms	1001:1032	higher molecular weight isoforms of BNP	1001:1039	This data is consistent with previous observations of higher molecular weight isoforms of BNP.
16750161	3	54	theme	acid	555:558	arg1	protein					574:580	The 108-amino acid CHO-expressed protein	541:580	The 108-amino acid CHO-expressed protein	541:580	The 108-amino acid CHO-expressed protein was examined by tryptic mapping and LC-MS and found to be an O-linked glycoprotein.
16750161	3	54	theme	acid	555:558	arg1	glycoprotein					652:663	an O-linked glycoprotein	640:663	an O-linked glycoprotein	640:663	The 108-amino acid CHO-expressed protein was examined by tryptic mapping and LC-MS and found to be an O-linked glycoprotein.
16750161	1	55	theme	ovary	205:209	arg1	CHO					218:220	CHO	218:220	CHO	218:220	Human pro-B-type natriuretic peptide (proBNP), the precursor for B-type natriuretic peptide (BNP), was expressed in Chinese hamster ovary cells (CHO) and compared by Western blot analysis to BNP cross-reacting material immunoprecipitated from the plasma of heart failure patients.
16750161	1	55	theme	ovary	205:209	arg1	cells					211:215	Chinese hamster ovary cells	189:215	Chinese hamster ovary cells (CHO)	189:221	Human pro-B-type natriuretic peptide (proBNP), the precursor for B-type natriuretic peptide (BNP), was expressed in Chinese hamster ovary cells (CHO) and compared by Western blot analysis to BNP cross-reacting material immunoprecipitated from the plasma of heart failure patients.
16750161	0	56	theme	O-linked	50:57	arg1	glycoprotein					59:70	an O-linked glycoprotein	47:70	an O-linked glycoprotein	47:70	The precursor to B-type natriuretic peptide is an O-linked glycoprotein.
16750161	0	56	theme	O-linked	50:57	arg1	precursor					4:12	The precursor	0:12	The precursor to B-type natriuretic peptide	0:42	The precursor to B-type natriuretic peptide is an O-linked glycoprotein.
16750161	3	57	theme	CHO-expressed	560:572	arg1	protein					574:580	The 108-amino acid CHO-expressed protein	541:580	The 108-amino acid CHO-expressed protein	541:580	The 108-amino acid CHO-expressed protein was examined by tryptic mapping and LC-MS and found to be an O-linked glycoprotein.
16750161	3	57	theme	CHO-expressed	560:572	arg1	glycoprotein					652:663	an O-linked glycoprotein	640:663	an O-linked glycoprotein	640:663	The 108-amino acid CHO-expressed protein was examined by tryptic mapping and LC-MS and found to be an O-linked glycoprotein.
16750161	4	58	theme	acid	882:885	arg1	stretch					895:901	a 36-amino acid residue stretch	871:901	a 36-amino acid residue stretch within the center of the propeptide region	871:944	Determination of the sites of O-glycosyl addition by blank cycle sequencing of tryptic and Glu-C (Staphylococcus aureus V8 protease) peptides showed that there are seven sites of glycosylation confined to a 36-amino acid residue stretch within the center of the propeptide region.
19038966	0	0	theme	late	82:85	arg1	lipofuscinosis					113:126	late infantile neuronal ceroid lipofuscinosis	82:126	late infantile neuronal ceroid lipofuscinosis	82:126	Structure of tripeptidyl-peptidase I provides insight into the molecular basis of late infantile neuronal ceroid lipofuscinosis.
19038966	4	1	theme	coordinated	766:776	arg1	site					791:794	an octahedrally coordinated Ca2+-binding site	750:794	an octahedrally coordinated Ca2+-binding site that are characteristic features of the S53 sedolisin family of peptidases	750:869	X-ray crystallographic analysis at 2.35 angstroms resolution reveals a globular structure with a subtilisin-like fold, a Ser475-Glu272-Asp360 catalytic triad, and an octahedrally coordinated Ca2+-binding site that are characteristic features of the S53 sedolisin family of peptidases.
19038966	4	1	theme	coordinated	766:776	arg1	features					820:827	characteristic features	805:827	characteristic features of the S53 sedolisin family of peptidases	805:869	X-ray crystallographic analysis at 2.35 angstroms resolution reveals a globular structure with a subtilisin-like fold, a Ser475-Glu272-Asp360 catalytic triad, and an octahedrally coordinated Ca2+-binding site that are characteristic features of the S53 sedolisin family of peptidases.
19038966	4	2	theme	family	850:855	arg1	site					791:794	an octahedrally coordinated Ca2+-binding site	750:794	an octahedrally coordinated Ca2+-binding site that are characteristic features of the S53 sedolisin family of peptidases	750:869	X-ray crystallographic analysis at 2.35 angstroms resolution reveals a globular structure with a subtilisin-like fold, a Ser475-Glu272-Asp360 catalytic triad, and an octahedrally coordinated Ca2+-binding site that are characteristic features of the S53 sedolisin family of peptidases.
19038966	4	2	theme	family	850:855	arg1	features					820:827	characteristic features	805:827	characteristic features of the S53 sedolisin family of peptidases	805:869	X-ray crystallographic analysis at 2.35 angstroms resolution reveals a globular structure with a subtilisin-like fold, a Ser475-Glu272-Asp360 catalytic triad, and an octahedrally coordinated Ca2+-binding site that are characteristic features of the S53 sedolisin family of peptidases.
19038966	1	3	theme	TPP1	254:257	arg1	gene					259:262	the TPP1 gene	250:262	the TPP1 gene that encodes tripeptidyl-peptidase I	250:299	Late infantile neuronal ceroid lipofuscinosis, a fatal neurodegenerative disease of childhood, is caused by mutations in the TPP1 gene that encodes tripeptidyl-peptidase I.
19038966	1	3	theme	TPP1	254:257	arg1	I					299:299	tripeptidyl-peptidase I	277:299	tripeptidyl-peptidase I	277:299	Late infantile neuronal ceroid lipofuscinosis, a fatal neurodegenerative disease of childhood, is caused by mutations in the TPP1 gene that encodes tripeptidyl-peptidase I.
19038966	5	4	theme	substrate	966:974	arg1	pocket					976:981	the P4 substrate pocket	959:981	the P4 substrate pocket explaining its preferential cleavage of tripeptides from the unsubstituted N terminus of proteins	959:1079	In contrast to other S53 peptidases, the TPP1 structure revealed steric constraints on the P4 substrate pocket explaining its preferential cleavage of tripeptides from the unsubstituted N terminus of proteins.
19038966	6	5	theme	TPP1	1181:1184	arg1	status					1171:1176	the activation status	1156:1176	the activation status of TPP1	1156:1184	Two alternative conformations of the catalytic Asp276 are associated with the activation status of TPP1.
19038966	4	6	theme	angstroms	627:635	arg1	resolution					637:646	2.35 angstroms resolution	622:646	2.35 angstroms resolution	622:646	X-ray crystallographic analysis at 2.35 angstroms resolution reveals a globular structure with a subtilisin-like fold, a Ser475-Glu272-Asp360 catalytic triad, and an octahedrally coordinated Ca2+-binding site that are characteristic features of the S53 sedolisin family of peptidases.
19038966	0	7	theme	neuronal	97:104	arg1	lipofuscinosis					113:126	late infantile neuronal ceroid lipofuscinosis	82:126	late infantile neuronal ceroid lipofuscinosis	82:126	Structure of tripeptidyl-peptidase I provides insight into the molecular basis of late infantile neuronal ceroid lipofuscinosis.
19038966	5	8	from	cleavage	1011:1018	arg1	terminus					1060:1067	the unsubstituted N terminus	1040:1067	the unsubstituted N terminus of proteins	1040:1079	In contrast to other S53 peptidases, the TPP1 structure revealed steric constraints on the P4 substrate pocket explaining its preferential cleavage of tripeptides from the unsubstituted N terminus of proteins.
19038966	7	9	theme	missense	1206:1213	arg1	mutations					1215:1223	28 disease-causing missense mutations	1187:1223	28 disease-causing missense mutations	1187:1223	28 disease-causing missense mutations are analyzed in the light of the TPP1 structure providing insight into the molecular basis of late infantile neuronal ceroid lipofuscinosis.
19038966	4	10	theme	sedolisin	840:848	arg1	family					850:855	the S53 sedolisin family	832:855	the S53 sedolisin family of peptidases	832:869	X-ray crystallographic analysis at 2.35 angstroms resolution reveals a globular structure with a subtilisin-like fold, a Ser475-Glu272-Asp360 catalytic triad, and an octahedrally coordinated Ca2+-binding site that are characteristic features of the S53 sedolisin family of peptidases.
19038966	4	11	theme	catalytic	729:737	arg1	triad					739:743	a Ser475-Glu272-Asp360 catalytic triad	706:743	a Ser475-Glu272-Asp360 catalytic triad	706:743	X-ray crystallographic analysis at 2.35 angstroms resolution reveals a globular structure with a subtilisin-like fold, a Ser475-Glu272-Asp360 catalytic triad, and an octahedrally coordinated Ca2+-binding site that are characteristic features of the S53 sedolisin family of peptidases.
19038966	4	11	theme	catalytic	729:737	arg1	fold					700:703	a subtilisin-like fold	682:703	a subtilisin-like fold	682:703	X-ray crystallographic analysis at 2.35 angstroms resolution reveals a globular structure with a subtilisin-like fold, a Ser475-Glu272-Asp360 catalytic triad, and an octahedrally coordinated Ca2+-binding site that are characteristic features of the S53 sedolisin family of peptidases.
19038966	5	12	theme	unsubstituted	1044:1056	arg1	terminus					1060:1067	the unsubstituted N terminus	1040:1067	the unsubstituted N terminus of proteins	1040:1079	In contrast to other S53 peptidases, the TPP1 structure revealed steric constraints on the P4 substrate pocket explaining its preferential cleavage of tripeptides from the unsubstituted N terminus of proteins.
19038966	0	13	theme	infantile	87:95	arg1	lipofuscinosis					113:126	late infantile neuronal ceroid lipofuscinosis	82:126	late infantile neuronal ceroid lipofuscinosis	82:126	Structure of tripeptidyl-peptidase I provides insight into the molecular basis of late infantile neuronal ceroid lipofuscinosis.
19038966	5	14	theme	N	1058:1058	arg1	terminus					1060:1067	the unsubstituted N terminus	1040:1067	the unsubstituted N terminus of proteins	1040:1079	In contrast to other S53 peptidases, the TPP1 structure revealed steric constraints on the P4 substrate pocket explaining its preferential cleavage of tripeptides from the unsubstituted N terminus of proteins.
19038966	4	15	theme	S53	836:838	arg1	family					850:855	the S53 sedolisin family	832:855	the S53 sedolisin family of peptidases	832:869	X-ray crystallographic analysis at 2.35 angstroms resolution reveals a globular structure with a subtilisin-like fold, a Ser475-Glu272-Asp360 catalytic triad, and an octahedrally coordinated Ca2+-binding site that are characteristic features of the S53 sedolisin family of peptidases.
19038966	3	16	theme	autocatalytic	515:527	arg1	cleavage					529:536	partial autocatalytic cleavage	507:536	partial autocatalytic cleavage between the prosegment and the catalytic domain	507:584	We crystallized the fully glycosylated TPP1 precursor under conditions that implied partial autocatalytic cleavage between the prosegment and the catalytic domain.
19038966	0	17	theme	lipofuscinosis	113:126	arg1	basis					73:77	the molecular basis	59:77	the molecular basis of late infantile neuronal ceroid lipofuscinosis	59:126	Structure of tripeptidyl-peptidase I provides insight into the molecular basis of late infantile neuronal ceroid lipofuscinosis.
19038966	4	18	theme	characteristic	805:818	arg1	site					791:794	an octahedrally coordinated Ca2+-binding site	750:794	an octahedrally coordinated Ca2+-binding site that are characteristic features of the S53 sedolisin family of peptidases	750:869	X-ray crystallographic analysis at 2.35 angstroms resolution reveals a globular structure with a subtilisin-like fold, a Ser475-Glu272-Asp360 catalytic triad, and an octahedrally coordinated Ca2+-binding site that are characteristic features of the S53 sedolisin family of peptidases.
19038966	4	18	theme	characteristic	805:818	arg1	features					820:827	characteristic features	805:827	characteristic features of the S53 sedolisin family of peptidases	805:869	X-ray crystallographic analysis at 2.35 angstroms resolution reveals a globular structure with a subtilisin-like fold, a Ser475-Glu272-Asp360 catalytic triad, and an octahedrally coordinated Ca2+-binding site that are characteristic features of the S53 sedolisin family of peptidases.
19038966	5	19	theme	steric	937:942	arg1	constraints					944:954	steric constraints	937:954	steric constraints on the P4 substrate pocket explaining its preferential cleavage of tripeptides from the unsubstituted N terminus of proteins	937:1079	In contrast to other S53 peptidases, the TPP1 structure revealed steric constraints on the P4 substrate pocket explaining its preferential cleavage of tripeptides from the unsubstituted N terminus of proteins.
19038966	3	20	theme	catalytic	569:577	arg1	domain					579:584	the catalytic domain	565:584	the catalytic domain	565:584	We crystallized the fully glycosylated TPP1 precursor under conditions that implied partial autocatalytic cleavage between the prosegment and the catalytic domain.
19038966	5	21	theme	preferential	998:1009	arg1	cleavage					1011:1018	its preferential cleavage	994:1018	its preferential cleavage of tripeptides from the unsubstituted N terminus of proteins	994:1079	In contrast to other S53 peptidases, the TPP1 structure revealed steric constraints on the P4 substrate pocket explaining its preferential cleavage of tripeptides from the unsubstituted N terminus of proteins.
19038966	1	22	theme	fatal	178:182	arg1	disease					202:208	a fatal neurodegenerative disease	176:208	a fatal neurodegenerative disease of childhood	176:221	Late infantile neuronal ceroid lipofuscinosis, a fatal neurodegenerative disease of childhood, is caused by mutations in the TPP1 gene that encodes tripeptidyl-peptidase I.
19038966	1	22	theme	fatal	178:182	arg1	lipofuscinosis					160:173	Late infantile neuronal ceroid lipofuscinosis	129:173	Late infantile neuronal ceroid lipofuscinosis	129:173	Late infantile neuronal ceroid lipofuscinosis, a fatal neurodegenerative disease of childhood, is caused by mutations in the TPP1 gene that encodes tripeptidyl-peptidase I.
19038966	0	23	theme	ceroid	106:111	arg1	lipofuscinosis					113:126	late infantile neuronal ceroid lipofuscinosis	82:126	late infantile neuronal ceroid lipofuscinosis	82:126	Structure of tripeptidyl-peptidase I provides insight into the molecular basis of late infantile neuronal ceroid lipofuscinosis.
19038966	6	24	theme	alternative	1086:1096	arg1	conformations					1098:1110	Two alternative conformations	1082:1110	Two alternative conformations of the catalytic Asp276	1082:1134	Two alternative conformations of the catalytic Asp276 are associated with the activation status of TPP1.
19038966	2	25	dep	in	373:374	arg1	vitro					376:380	vitro	376:380	vitro	376:380	We show that purified TPP1 requires at least partial glycosylation for in vitro autoprocessing and proteolytic activity.
19038966	1	26	theme	neurodegenerative	184:200	arg1	disease					202:208	a fatal neurodegenerative disease	176:208	a fatal neurodegenerative disease of childhood	176:221	Late infantile neuronal ceroid lipofuscinosis, a fatal neurodegenerative disease of childhood, is caused by mutations in the TPP1 gene that encodes tripeptidyl-peptidase I.
19038966	1	26	theme	neurodegenerative	184:200	arg1	lipofuscinosis					160:173	Late infantile neuronal ceroid lipofuscinosis	129:173	Late infantile neuronal ceroid lipofuscinosis	129:173	Late infantile neuronal ceroid lipofuscinosis, a fatal neurodegenerative disease of childhood, is caused by mutations in the TPP1 gene that encodes tripeptidyl-peptidase I.
19038966	7	27	theme	structure	1263:1271	arg1	light					1245:1249	the light	1241:1249	the light of the TPP1 structure providing insight into the molecular basis of late infantile neuronal ceroid lipofuscinosis	1241:1363	28 disease-causing missense mutations are analyzed in the light of the TPP1 structure providing insight into the molecular basis of late infantile neuronal ceroid lipofuscinosis.
19038966	4	28	theme	Ser475-Glu272-Asp360	708:727	arg1	triad					739:743	a Ser475-Glu272-Asp360 catalytic triad	706:743	a Ser475-Glu272-Asp360 catalytic triad	706:743	X-ray crystallographic analysis at 2.35 angstroms resolution reveals a globular structure with a subtilisin-like fold, a Ser475-Glu272-Asp360 catalytic triad, and an octahedrally coordinated Ca2+-binding site that are characteristic features of the S53 sedolisin family of peptidases.
19038966	4	28	theme	Ser475-Glu272-Asp360	708:727	arg1	fold					700:703	a subtilisin-like fold	682:703	a subtilisin-like fold	682:703	X-ray crystallographic analysis at 2.35 angstroms resolution reveals a globular structure with a subtilisin-like fold, a Ser475-Glu272-Asp360 catalytic triad, and an octahedrally coordinated Ca2+-binding site that are characteristic features of the S53 sedolisin family of peptidases.
19038966	6	29	theme	catalytic	1119:1127	arg1	Asp276					1129:1134	the catalytic Asp276	1115:1134	the catalytic Asp276	1115:1134	Two alternative conformations of the catalytic Asp276 are associated with the activation status of TPP1.
19038966	6	30	theme	activation	1160:1169	arg1	status					1171:1176	the activation status	1156:1176	the activation status of TPP1	1156:1184	Two alternative conformations of the catalytic Asp276 are associated with the activation status of TPP1.
19038966	5	31	theme	other	887:891	arg1	peptidases					897:906	other S53 peptidases	887:906	other S53 peptidases	887:906	In contrast to other S53 peptidases, the TPP1 structure revealed steric constraints on the P4 substrate pocket explaining its preferential cleavage of tripeptides from the unsubstituted N terminus of proteins.
19038966	1	32	theme	tripeptidyl-peptidase	277:297	arg1	gene					259:262	the TPP1 gene	250:262	the TPP1 gene that encodes tripeptidyl-peptidase I	250:299	Late infantile neuronal ceroid lipofuscinosis, a fatal neurodegenerative disease of childhood, is caused by mutations in the TPP1 gene that encodes tripeptidyl-peptidase I.
19038966	1	32	theme	tripeptidyl-peptidase	277:297	arg1	I					299:299	tripeptidyl-peptidase I	277:299	tripeptidyl-peptidase I	277:299	Late infantile neuronal ceroid lipofuscinosis, a fatal neurodegenerative disease of childhood, is caused by mutations in the TPP1 gene that encodes tripeptidyl-peptidase I.
19038966	2	33	theme	purified	315:322	arg1	TPP1					324:327	purified TPP1	315:327	purified TPP1	315:327	We show that purified TPP1 requires at least partial glycosylation for in vitro autoprocessing and proteolytic activity.
19038966	3	34	theme	glycosylated	449:460	arg1	precursor					467:475	the fully glycosylated TPP1 precursor	439:475	the fully glycosylated TPP1 precursor	439:475	We crystallized the fully glycosylated TPP1 precursor under conditions that implied partial autocatalytic cleavage between the prosegment and the catalytic domain.
19038966	0	35	theme	I	35:35	arg1	Structure					0:8	Structure	0:8	Structure of tripeptidyl-peptidase I	0:35	Structure of tripeptidyl-peptidase I provides insight into the molecular basis of late infantile neuronal ceroid lipofuscinosis.
19038966	4	36	theme	crystallographic	593:608	arg1	analysis					610:617	X-ray crystallographic analysis	587:617	X-ray crystallographic analysis at 2.35 angstroms resolution	587:646	X-ray crystallographic analysis at 2.35 angstroms resolution reveals a globular structure with a subtilisin-like fold, a Ser475-Glu272-Asp360 catalytic triad, and an octahedrally coordinated Ca2+-binding site that are characteristic features of the S53 sedolisin family of peptidases.
19038966	1	37	theme	childhood	213:221	arg1	disease					202:208	a fatal neurodegenerative disease	176:208	a fatal neurodegenerative disease of childhood	176:221	Late infantile neuronal ceroid lipofuscinosis, a fatal neurodegenerative disease of childhood, is caused by mutations in the TPP1 gene that encodes tripeptidyl-peptidase I.
19038966	1	37	theme	childhood	213:221	arg1	lipofuscinosis					160:173	Late infantile neuronal ceroid lipofuscinosis	129:173	Late infantile neuronal ceroid lipofuscinosis	129:173	Late infantile neuronal ceroid lipofuscinosis, a fatal neurodegenerative disease of childhood, is caused by mutations in the TPP1 gene that encodes tripeptidyl-peptidase I.
19038966	0	38	theme	tripeptidyl-peptidase	13:33	arg1	I					35:35	tripeptidyl-peptidase I	13:35	tripeptidyl-peptidase I	13:35	Structure of tripeptidyl-peptidase I provides insight into the molecular basis of late infantile neuronal ceroid lipofuscinosis.
19038966	5	39	theme	tripeptides	1023:1033	arg1	cleavage					1011:1018	its preferential cleavage	994:1018	its preferential cleavage of tripeptides from the unsubstituted N terminus of proteins	994:1079	In contrast to other S53 peptidases, the TPP1 structure revealed steric constraints on the P4 substrate pocket explaining its preferential cleavage of tripeptides from the unsubstituted N terminus of proteins.
19038966	7	40	theme	ceroid	1343:1348	arg1	lipofuscinosis					1350:1363	late infantile neuronal ceroid lipofuscinosis	1319:1363	late infantile neuronal ceroid lipofuscinosis	1319:1363	28 disease-causing missense mutations are analyzed in the light of the TPP1 structure providing insight into the molecular basis of late infantile neuronal ceroid lipofuscinosis.
19038966	4	41	theme	subtilisin-like	684:698	arg1	triad					739:743	a Ser475-Glu272-Asp360 catalytic triad	706:743	a Ser475-Glu272-Asp360 catalytic triad	706:743	X-ray crystallographic analysis at 2.35 angstroms resolution reveals a globular structure with a subtilisin-like fold, a Ser475-Glu272-Asp360 catalytic triad, and an octahedrally coordinated Ca2+-binding site that are characteristic features of the S53 sedolisin family of peptidases.
19038966	4	41	theme	subtilisin-like	684:698	arg1	fold					700:703	a subtilisin-like fold	682:703	a subtilisin-like fold	682:703	X-ray crystallographic analysis at 2.35 angstroms resolution reveals a globular structure with a subtilisin-like fold, a Ser475-Glu272-Asp360 catalytic triad, and an octahedrally coordinated Ca2+-binding site that are characteristic features of the S53 sedolisin family of peptidases.
19038966	4	42	theme	Ca2+-binding	778:789	arg1	site					791:794	an octahedrally coordinated Ca2+-binding site	750:794	an octahedrally coordinated Ca2+-binding site that are characteristic features of the S53 sedolisin family of peptidases	750:869	X-ray crystallographic analysis at 2.35 angstroms resolution reveals a globular structure with a subtilisin-like fold, a Ser475-Glu272-Asp360 catalytic triad, and an octahedrally coordinated Ca2+-binding site that are characteristic features of the S53 sedolisin family of peptidases.
19038966	4	42	theme	Ca2+-binding	778:789	arg1	features					820:827	characteristic features	805:827	characteristic features of the S53 sedolisin family of peptidases	805:869	X-ray crystallographic analysis at 2.35 angstroms resolution reveals a globular structure with a subtilisin-like fold, a Ser475-Glu272-Asp360 catalytic triad, and an octahedrally coordinated Ca2+-binding site that are characteristic features of the S53 sedolisin family of peptidases.
19038966	7	43	theme	lipofuscinosis	1350:1363	arg1	basis					1310:1314	the molecular basis	1296:1314	the molecular basis of late infantile neuronal ceroid lipofuscinosis	1296:1363	28 disease-causing missense mutations are analyzed in the light of the TPP1 structure providing insight into the molecular basis of late infantile neuronal ceroid lipofuscinosis.
19038966	5	44	theme	TPP1	913:916	arg1	structure					918:926	the TPP1 structure	909:926	the TPP1 structure	909:926	In contrast to other S53 peptidases, the TPP1 structure revealed steric constraints on the P4 substrate pocket explaining its preferential cleavage of tripeptides from the unsubstituted N terminus of proteins.
19038966	3	45	theme	TPP1	462:465	arg1	precursor					467:475	the fully glycosylated TPP1 precursor	439:475	the fully glycosylated TPP1 precursor	439:475	We crystallized the fully glycosylated TPP1 precursor under conditions that implied partial autocatalytic cleavage between the prosegment and the catalytic domain.
19038966	5	46	theme	S53	893:895	arg1	peptidases					897:906	other S53 peptidases	887:906	other S53 peptidases	887:906	In contrast to other S53 peptidases, the TPP1 structure revealed steric constraints on the P4 substrate pocket explaining its preferential cleavage of tripeptides from the unsubstituted N terminus of proteins.
19038966	6	47	theme	Asp276	1129:1134	arg1	conformations					1098:1110	Two alternative conformations	1082:1110	Two alternative conformations of the catalytic Asp276	1082:1134	Two alternative conformations of the catalytic Asp276 are associated with the activation status of TPP1.
19038966	7	48	theme	infantile	1324:1332	arg1	lipofuscinosis					1350:1363	late infantile neuronal ceroid lipofuscinosis	1319:1363	late infantile neuronal ceroid lipofuscinosis	1319:1363	28 disease-causing missense mutations are analyzed in the light of the TPP1 structure providing insight into the molecular basis of late infantile neuronal ceroid lipofuscinosis.
19038966	4	49	with	structure	667:675	arg1	site					791:794	an octahedrally coordinated Ca2+-binding site	750:794	an octahedrally coordinated Ca2+-binding site that are characteristic features of the S53 sedolisin family of peptidases	750:869	X-ray crystallographic analysis at 2.35 angstroms resolution reveals a globular structure with a subtilisin-like fold, a Ser475-Glu272-Asp360 catalytic triad, and an octahedrally coordinated Ca2+-binding site that are characteristic features of the S53 sedolisin family of peptidases.
19038966	4	49	with	structure	667:675	arg1	triad					739:743	a Ser475-Glu272-Asp360 catalytic triad	706:743	a Ser475-Glu272-Asp360 catalytic triad	706:743	X-ray crystallographic analysis at 2.35 angstroms resolution reveals a globular structure with a subtilisin-like fold, a Ser475-Glu272-Asp360 catalytic triad, and an octahedrally coordinated Ca2+-binding site that are characteristic features of the S53 sedolisin family of peptidases.
19038966	4	49	with	structure	667:675	arg1	fold					700:703	a subtilisin-like fold	682:703	a subtilisin-like fold	682:703	X-ray crystallographic analysis at 2.35 angstroms resolution reveals a globular structure with a subtilisin-like fold, a Ser475-Glu272-Asp360 catalytic triad, and an octahedrally coordinated Ca2+-binding site that are characteristic features of the S53 sedolisin family of peptidases.
19038966	4	49	with	structure	667:675	arg1	features					820:827	characteristic features	805:827	characteristic features of the S53 sedolisin family of peptidases	805:869	X-ray crystallographic analysis at 2.35 angstroms resolution reveals a globular structure with a subtilisin-like fold, a Ser475-Glu272-Asp360 catalytic triad, and an octahedrally coordinated Ca2+-binding site that are characteristic features of the S53 sedolisin family of peptidases.
19038966	2	50	theme	partial	347:353	arg1	glycosylation					355:367	partial glycosylation	347:367	partial glycosylation for in vitro autoprocessing and proteolytic activity	347:420	We show that purified TPP1 requires at least partial glycosylation for in vitro autoprocessing and proteolytic activity.
19038966	4	51	theme	globular	658:665	arg1	structure					667:675	a globular structure	656:675	a globular structure with a subtilisin-like fold, a Ser475-Glu272-Asp360 catalytic triad, and an octahedrally coordinated Ca2+-binding site that are characteristic features of the S53 sedolisin family of peptidases	656:869	X-ray crystallographic analysis at 2.35 angstroms resolution reveals a globular structure with a subtilisin-like fold, a Ser475-Glu272-Asp360 catalytic triad, and an octahedrally coordinated Ca2+-binding site that are characteristic features of the S53 sedolisin family of peptidases.
19038966	4	52	theme	X-ray	587:591	arg1	analysis					610:617	X-ray crystallographic analysis	587:617	X-ray crystallographic analysis at 2.35 angstroms resolution	587:646	X-ray crystallographic analysis at 2.35 angstroms resolution reveals a globular structure with a subtilisin-like fold, a Ser475-Glu272-Asp360 catalytic triad, and an octahedrally coordinated Ca2+-binding site that are characteristic features of the S53 sedolisin family of peptidases.
19038966	7	53	theme	disease-causing	1190:1204	arg1	mutations					1215:1223	28 disease-causing missense mutations	1187:1223	28 disease-causing missense mutations	1187:1223	28 disease-causing missense mutations are analyzed in the light of the TPP1 structure providing insight into the molecular basis of late infantile neuronal ceroid lipofuscinosis.
19038966	1	54	theme	Late	129:132	arg1	disease					202:208	a fatal neurodegenerative disease	176:208	a fatal neurodegenerative disease of childhood	176:221	Late infantile neuronal ceroid lipofuscinosis, a fatal neurodegenerative disease of childhood, is caused by mutations in the TPP1 gene that encodes tripeptidyl-peptidase I.
19038966	1	54	theme	Late	129:132	arg1	lipofuscinosis					160:173	Late infantile neuronal ceroid lipofuscinosis	129:173	Late infantile neuronal ceroid lipofuscinosis	129:173	Late infantile neuronal ceroid lipofuscinosis, a fatal neurodegenerative disease of childhood, is caused by mutations in the TPP1 gene that encodes tripeptidyl-peptidase I.
19038966	7	55	theme	neuronal	1334:1341	arg1	lipofuscinosis					1350:1363	late infantile neuronal ceroid lipofuscinosis	1319:1363	late infantile neuronal ceroid lipofuscinosis	1319:1363	28 disease-causing missense mutations are analyzed in the light of the TPP1 structure providing insight into the molecular basis of late infantile neuronal ceroid lipofuscinosis.
19038966	5	56	theme	proteins	1072:1079	arg1	terminus					1060:1067	the unsubstituted N terminus	1040:1067	the unsubstituted N terminus of proteins	1040:1079	In contrast to other S53 peptidases, the TPP1 structure revealed steric constraints on the P4 substrate pocket explaining its preferential cleavage of tripeptides from the unsubstituted N terminus of proteins.
19038966	1	57	theme	infantile	134:142	arg1	disease					202:208	a fatal neurodegenerative disease	176:208	a fatal neurodegenerative disease of childhood	176:221	Late infantile neuronal ceroid lipofuscinosis, a fatal neurodegenerative disease of childhood, is caused by mutations in the TPP1 gene that encodes tripeptidyl-peptidase I.
19038966	1	57	theme	infantile	134:142	arg1	lipofuscinosis					160:173	Late infantile neuronal ceroid lipofuscinosis	129:173	Late infantile neuronal ceroid lipofuscinosis	129:173	Late infantile neuronal ceroid lipofuscinosis, a fatal neurodegenerative disease of childhood, is caused by mutations in the TPP1 gene that encodes tripeptidyl-peptidase I.
19038966	4	58	from	resolution	637:646	arg1	analysis					610:617	X-ray crystallographic analysis	587:617	X-ray crystallographic analysis at 2.35 angstroms resolution	587:646	X-ray crystallographic analysis at 2.35 angstroms resolution reveals a globular structure with a subtilisin-like fold, a Ser475-Glu272-Asp360 catalytic triad, and an octahedrally coordinated Ca2+-binding site that are characteristic features of the S53 sedolisin family of peptidases.
19038966	1	59	from	mutations	237:245	arg1	gene					259:262	the TPP1 gene	250:262	the TPP1 gene that encodes tripeptidyl-peptidase I	250:299	Late infantile neuronal ceroid lipofuscinosis, a fatal neurodegenerative disease of childhood, is caused by mutations in the TPP1 gene that encodes tripeptidyl-peptidase I.
19038966	1	59	from	mutations	237:245	arg1	I					299:299	tripeptidyl-peptidase I	277:299	tripeptidyl-peptidase I	277:299	Late infantile neuronal ceroid lipofuscinosis, a fatal neurodegenerative disease of childhood, is caused by mutations in the TPP1 gene that encodes tripeptidyl-peptidase I.
19038966	4	60	theme	peptidases	860:869	arg1	family					850:855	the S53 sedolisin family	832:855	the S53 sedolisin family of peptidases	832:869	X-ray crystallographic analysis at 2.35 angstroms resolution reveals a globular structure with a subtilisin-like fold, a Ser475-Glu272-Asp360 catalytic triad, and an octahedrally coordinated Ca2+-binding site that are characteristic features of the S53 sedolisin family of peptidases.
19038966	5	61	from	constraints	944:954	arg1	pocket					976:981	the P4 substrate pocket	959:981	the P4 substrate pocket explaining its preferential cleavage of tripeptides from the unsubstituted N terminus of proteins	959:1079	In contrast to other S53 peptidases, the TPP1 structure revealed steric constraints on the P4 substrate pocket explaining its preferential cleavage of tripeptides from the unsubstituted N terminus of proteins.
19038966	1	62	theme	neuronal	144:151	arg1	disease					202:208	a fatal neurodegenerative disease	176:208	a fatal neurodegenerative disease of childhood	176:221	Late infantile neuronal ceroid lipofuscinosis, a fatal neurodegenerative disease of childhood, is caused by mutations in the TPP1 gene that encodes tripeptidyl-peptidase I.
19038966	1	62	theme	neuronal	144:151	arg1	lipofuscinosis					160:173	Late infantile neuronal ceroid lipofuscinosis	129:173	Late infantile neuronal ceroid lipofuscinosis	129:173	Late infantile neuronal ceroid lipofuscinosis, a fatal neurodegenerative disease of childhood, is caused by mutations in the TPP1 gene that encodes tripeptidyl-peptidase I.
19038966	3	63	theme	partial	507:513	arg1	cleavage					529:536	partial autocatalytic cleavage	507:536	partial autocatalytic cleavage between the prosegment and the catalytic domain	507:584	We crystallized the fully glycosylated TPP1 precursor under conditions that implied partial autocatalytic cleavage between the prosegment and the catalytic domain.
19038966	7	64	theme	late	1319:1322	arg1	lipofuscinosis					1350:1363	late infantile neuronal ceroid lipofuscinosis	1319:1363	late infantile neuronal ceroid lipofuscinosis	1319:1363	28 disease-causing missense mutations are analyzed in the light of the TPP1 structure providing insight into the molecular basis of late infantile neuronal ceroid lipofuscinosis.
19038966	5	65	theme	P4	963:964	arg1	pocket					976:981	the P4 substrate pocket	959:981	the P4 substrate pocket explaining its preferential cleavage of tripeptides from the unsubstituted N terminus of proteins	959:1079	In contrast to other S53 peptidases, the TPP1 structure revealed steric constraints on the P4 substrate pocket explaining its preferential cleavage of tripeptides from the unsubstituted N terminus of proteins.
19038966	3	66	gly	glycosylated	449:460	arg1	precursor					467:475	the fully glycosylated TPP1 precursor	439:475	the fully glycosylated TPP1 precursor	439:475	We crystallized the fully glycosylated TPP1 precursor under conditions that implied partial autocatalytic cleavage between the prosegment and the catalytic domain.
19038966	1	67	theme	ceroid	153:158	arg1	disease					202:208	a fatal neurodegenerative disease	176:208	a fatal neurodegenerative disease of childhood	176:221	Late infantile neuronal ceroid lipofuscinosis, a fatal neurodegenerative disease of childhood, is caused by mutations in the TPP1 gene that encodes tripeptidyl-peptidase I.
19038966	1	67	theme	ceroid	153:158	arg1	lipofuscinosis					160:173	Late infantile neuronal ceroid lipofuscinosis	129:173	Late infantile neuronal ceroid lipofuscinosis	129:173	Late infantile neuronal ceroid lipofuscinosis, a fatal neurodegenerative disease of childhood, is caused by mutations in the TPP1 gene that encodes tripeptidyl-peptidase I.
19038966	2	68	theme	proteolytic	401:411	arg1	activity					413:420	proteolytic activity	401:420	proteolytic activity	401:420	We show that purified TPP1 requires at least partial glycosylation for in vitro autoprocessing and proteolytic activity.
19038966	0	69	theme	molecular	63:71	arg1	basis					73:77	the molecular basis	59:77	the molecular basis of late infantile neuronal ceroid lipofuscinosis	59:126	Structure of tripeptidyl-peptidase I provides insight into the molecular basis of late infantile neuronal ceroid lipofuscinosis.
19038966	7	70	theme	TPP1	1258:1261	arg1	structure					1263:1271	the TPP1 structure	1254:1271	the TPP1 structure providing insight into the molecular basis of late infantile neuronal ceroid lipofuscinosis	1254:1363	28 disease-causing missense mutations are analyzed in the light of the TPP1 structure providing insight into the molecular basis of late infantile neuronal ceroid lipofuscinosis.
19038966	2	71	theme	in	373:374	arg1	autoprocessing					382:395	in vitro autoprocessing	373:395	in vitro autoprocessing	373:395	We show that purified TPP1 requires at least partial glycosylation for in vitro autoprocessing and proteolytic activity.
19038966	5	72	from	terminus	1060:1067	arg1	tripeptides					1023:1033	tripeptides	1023:1033	tripeptides from the unsubstituted N terminus of proteins	1023:1079	In contrast to other S53 peptidases, the TPP1 structure revealed steric constraints on the P4 substrate pocket explaining its preferential cleavage of tripeptides from the unsubstituted N terminus of proteins.
19038966	5	72	from	terminus	1060:1067	arg1	cleavage					1011:1018	its preferential cleavage	994:1018	its preferential cleavage of tripeptides from the unsubstituted N terminus of proteins	994:1079	In contrast to other S53 peptidases, the TPP1 structure revealed steric constraints on the P4 substrate pocket explaining its preferential cleavage of tripeptides from the unsubstituted N terminus of proteins.
19038966	7	73	theme	molecular	1300:1308	arg1	basis					1310:1314	the molecular basis	1296:1314	the molecular basis of late infantile neuronal ceroid lipofuscinosis	1296:1363	28 disease-causing missense mutations are analyzed in the light of the TPP1 structure providing insight into the molecular basis of late infantile neuronal ceroid lipofuscinosis.
1314561	8	0	theme	labelled	932:939	arg1	TMD1-105					941:948	labelled TMD1-105	932:948	labelled TMD1-105	932:948	Trypsin digestion of labelled TMD1-105 permitted isolation of two overlapping peptides that contained chondroitin sulphate, spanned the entire O-glycosylation domain and had O-glycosylation sites at Ser-492, Ser-498, Thr-500, Thr-504 and Thr-506.
1314561	2	1	dep	[TMD1-105	187:195	arg1	1990					262:265	1990	262:265	1990	262:265	Two glycoforms of a secretable human thrombomodulin mutant [TMD1-105 and TMD1-75; Parkinson, Grinnell, Moore, Hoskins, Vlahos & Bang (1990) J. Biol.
1314561	2	1	dep	[TMD1-105	187:195	arg1	Vlahos					247:252	Vlahos	247:252	Vlahos	247:252	Two glycoforms of a secretable human thrombomodulin mutant [TMD1-105 and TMD1-75; Parkinson, Grinnell, Moore, Hoskins, Vlahos & Bang (1990) J. Biol.
1314561	2	1	dep	[TMD1-105	187:195	arg1	Hoskins					238:244	Hoskins	238:244	Hoskins	238:244	Two glycoforms of a secretable human thrombomodulin mutant [TMD1-105 and TMD1-75; Parkinson, Grinnell, Moore, Hoskins, Vlahos & Bang (1990) J. Biol.
1314561	2	1	dep	[TMD1-105	187:195	arg1	Moore					231:235	Moore	231:235	Moore	231:235	Two glycoforms of a secretable human thrombomodulin mutant [TMD1-105 and TMD1-75; Parkinson, Grinnell, Moore, Hoskins, Vlahos & Bang (1990) J. Biol.
1314561	2	1	dep	[TMD1-105	187:195	arg1	Bang					256:259	Bang	256:259	Bang	256:259	Two glycoforms of a secretable human thrombomodulin mutant [TMD1-105 and TMD1-75; Parkinson, Grinnell, Moore, Hoskins, Vlahos & Bang (1990) J. Biol.
1314561	10	2	dep	fifth	1615:1619	arg1	Asn-409					1622:1628	Asn-409	1622:1628	Asn-409	1622:1628	Five peptides with N-linked carbohydrate were also isolated and contained glycosylation sites in the lectin-like domain (Asn-47, Asn-115, Asn-116) and in the fourth (Asn-382) and fifth (Asn-409) epidermal growth factor domains.
1314561	9	3	theme	chondroitin	1162:1172	arg1	site					1194:1197	The chondroitin sulphate-attachment site	1158:1197	The chondroitin sulphate-attachment site	1158:1197	The chondroitin sulphate-attachment site was assigned to Ser-492 as this residue is conserved in mouse and bovine thrombomodulin and lies within a sequence Ser-Gly-Ser-492-Gly-Glu-Pro, which has strong similarity to chondroitin sulphate attachment sites in other proteoglycans.
1314561	8	4	contain	had	1081:1083	arg1	peptides					989:996	two overlapping peptides	973:996	two overlapping peptides that contained chondroitin sulphate, spanned the entire O-glycosylation domain and had O-glycosylation sites at Ser-492, Ser-498, Thr-500, Thr-504 and Thr-506	973:1155	Trypsin digestion of labelled TMD1-105 permitted isolation of two overlapping peptides that contained chondroitin sulphate, spanned the entire O-glycosylation domain and had O-glycosylation sites at Ser-492, Ser-498, Thr-500, Thr-504 and Thr-506.
1314561	8	4	contain	had	1081:1083	arg2	sites					1101:1105	O-glycosylation sites	1085:1105	O-glycosylation sites	1085:1105	Trypsin digestion of labelled TMD1-105 permitted isolation of two overlapping peptides that contained chondroitin sulphate, spanned the entire O-glycosylation domain and had O-glycosylation sites at Ser-492, Ser-498, Thr-500, Thr-504 and Thr-506.
1314561	4	5	from	role	357:360	arg1	functions					386:394	the functions	382:394	the functions of this endothelial-cell thrombin receptor	382:437	265, 12602-12610] were expressed in human 293 cells and used to study the role of glycosylation in the functions of this endothelial-cell thrombin receptor.
1314561	11	6	link	O-linked	1696:1703	arg1	carbohydrates					1705:1717	N-linked and simple O-linked carbohydrates	1676:1717	N-linked and simple O-linked carbohydrates	1676:1717	The role of N-linked and simple O-linked carbohydrates in the functions of human thrombomodulin remain unclear.
1314561	2	7	theme	thrombomodulin	165:178	arg1	glycoforms					132:141	Two glycoforms	128:141	Two glycoforms of a secretable human thrombomodulin	128:178	Two glycoforms of a secretable human thrombomodulin mutant [TMD1-105 and TMD1-75; Parkinson, Grinnell, Moore, Hoskins, Vlahos & Bang (1990) J. Biol.
1314561	5	8	theme	content	453:459	arg1	analysis					461:468	Carbohydrate content analysis	440:468	Carbohydrate content analysis	440:468	Carbohydrate content analysis and intrinsic labelling with [3H]glucosamine and [35S]sulphate showed that TMD1-105 contained a chondroitin sulphate whereas TMD1-75 did not.
1314561	2	9	theme	secretable	148:157	arg1	thrombomodulin					165:178	a secretable human thrombomodulin	146:178	a secretable human thrombomodulin	146:178	Two glycoforms of a secretable human thrombomodulin mutant [TMD1-105 and TMD1-75; Parkinson, Grinnell, Moore, Hoskins, Vlahos & Bang (1990) J. Biol.
1314561	8	10	theme	overlapping	977:987	arg1	peptides					989:996	two overlapping peptides	973:996	two overlapping peptides that contained chondroitin sulphate, spanned the entire O-glycosylation domain and had O-glycosylation sites at Ser-492, Ser-498, Thr-500, Thr-504 and Thr-506	973:1155	Trypsin digestion of labelled TMD1-105 permitted isolation of two overlapping peptides that contained chondroitin sulphate, spanned the entire O-glycosylation domain and had O-glycosylation sites at Ser-492, Ser-498, Thr-500, Thr-504 and Thr-506.
1314561	2	11	dep	Bang	256:259	arg1	Biol					271:274	Biol	271:274	Biol	271:274	Two glycoforms of a secretable human thrombomodulin mutant [TMD1-105 and TMD1-75; Parkinson, Grinnell, Moore, Hoskins, Vlahos & Bang (1990) J. Biol.
1314561	2	11	dep	Bang	256:259	arg1	Grinnell					221:228	Grinnell	221:228	Grinnell	221:228	Two glycoforms of a secretable human thrombomodulin mutant [TMD1-105 and TMD1-75; Parkinson, Grinnell, Moore, Hoskins, Vlahos & Bang (1990) J. Biol.
1314561	6	12	theme	other	754:758	arg1	sites					782:786	other O-linked and N-linked sites	754:786	other O-linked and N-linked sites in the two glycoforms	754:808	Other than chondroitin sulphate, the carbohydrate contents of the two glycoforms were identical, indicating similar glycosylation patterns at other O-linked and N-linked sites in the two glycoforms.
1314561	6	13	theme	carbohydrate	649:660	arg1	identical					698:706	identical	698:706	identical	698:706	Other than chondroitin sulphate, the carbohydrate contents of the two glycoforms were identical, indicating similar glycosylation patterns at other O-linked and N-linked sites in the two glycoforms.
1314561	6	13	theme	carbohydrate	649:660	arg1	contents					662:669	the carbohydrate contents	645:669	the carbohydrate contents of the two glycoforms	645:691	Other than chondroitin sulphate, the carbohydrate contents of the two glycoforms were identical, indicating similar glycosylation patterns at other O-linked and N-linked sites in the two glycoforms.
1314561	12	14	theme	important	1952:1960	arg1	receptor					1985:1992	this important anticoagulant thrombin receptor	1947:1992	this important anticoagulant thrombin receptor	1947:1992	The present studies demonstrate, however, that the presence of chondroitin sulphate in human thrombomodulin has profound effects on all of the anticoagulant properties of this important anticoagulant thrombin receptor.
1314561	12	15	theme	thrombin	1976:1983	arg1	receptor					1985:1992	this important anticoagulant thrombin receptor	1947:1992	this important anticoagulant thrombin receptor	1947:1992	The present studies demonstrate, however, that the presence of chondroitin sulphate in human thrombomodulin has profound effects on all of the anticoagulant properties of this important anticoagulant thrombin receptor.
1314561	10	16	theme	fifth	1615:1619	arg1	domains					1655:1661	the fourth (Asn-382) and fifth (Asn-409) epidermal growth factor domains	1590:1661	the fourth (Asn-382) and fifth (Asn-409) epidermal growth factor domains	1590:1661	Five peptides with N-linked carbohydrate were also isolated and contained glycosylation sites in the lectin-like domain (Asn-47, Asn-115, Asn-116) and in the fourth (Asn-382) and fifth (Asn-409) epidermal growth factor domains.
1314561	5	17	theme	[35S	519:522	arg1	sulphate					524:531	[35S]sulphate	519:531	[35S]sulphate	519:531	Carbohydrate content analysis and intrinsic labelling with [3H]glucosamine and [35S]sulphate showed that TMD1-105 contained a chondroitin sulphate whereas TMD1-75 did not.
1314561	10	18	link	N-linked	1455:1462	arg1	carbohydrate					1464:1475	N-linked carbohydrate	1455:1475	N-linked carbohydrate	1455:1475	Five peptides with N-linked carbohydrate were also isolated and contained glycosylation sites in the lectin-like domain (Asn-47, Asn-115, Asn-116) and in the fourth (Asn-382) and fifth (Asn-409) epidermal growth factor domains.
1314561	11	19	theme	thrombomodulin	1745:1758	arg1	functions					1726:1734	the functions	1722:1734	the functions of human thrombomodulin	1722:1758	The role of N-linked and simple O-linked carbohydrates in the functions of human thrombomodulin remain unclear.
1314561	5	20	theme	[3H	499:501	arg1	glucosamine					503:513	[3H]glucosamine	499:513	[3H]glucosamine	499:513	Carbohydrate content analysis and intrinsic labelling with [3H]glucosamine and [35S]sulphate showed that TMD1-105 contained a chondroitin sulphate whereas TMD1-75 did not.
1314561	8	21	theme	chondroitin	1013:1023	arg1	sulphate					1025:1032	chondroitin sulphate	1013:1032	chondroitin sulphate	1013:1032	Trypsin digestion of labelled TMD1-105 permitted isolation of two overlapping peptides that contained chondroitin sulphate, spanned the entire O-glycosylation domain and had O-glycosylation sites at Ser-492, Ser-498, Thr-500, Thr-504 and Thr-506.
1314561	5	22	theme	chondroitin	566:576	arg1	sulphate					578:585	a chondroitin sulphate	564:585	a chondroitin sulphate	564:585	Carbohydrate content analysis and intrinsic labelling with [3H]glucosamine and [35S]sulphate showed that TMD1-105 contained a chondroitin sulphate whereas TMD1-75 did not.
1314561	1	23	theme	anticoagulant	70:82	arg1	function					84:91	anticoagulant function	70:91	anticoagulant function	70:91	Regulation of cofactor activity and anticoagulant function by a glycosaminoglycan side chain.
1314561	4	24	theme	thrombin	421:428	arg1	receptor					430:437	this endothelial-cell thrombin receptor	399:437	this endothelial-cell thrombin receptor	399:437	265, 12602-12610] were expressed in human 293 cells and used to study the role of glycosylation in the functions of this endothelial-cell thrombin receptor.
1314561	10	25	theme	glycosylation	1510:1522	arg1	sites					1524:1528	glycosylation sites	1510:1528	glycosylation sites	1510:1528	Five peptides with N-linked carbohydrate were also isolated and contained glycosylation sites in the lectin-like domain (Asn-47, Asn-115, Asn-116) and in the fourth (Asn-382) and fifth (Asn-409) epidermal growth factor domains.
1314561	4	26	dep	265	283:285	arg1	12602-12610					288:298	12602-12610	288:298	12602-12610	288:298	265, 12602-12610] were expressed in human 293 cells and used to study the role of glycosylation in the functions of this endothelial-cell thrombin receptor.
1314561	10	27	theme	growth	1641:1646	arg1	domains					1655:1661	the fourth (Asn-382) and fifth (Asn-409) epidermal growth factor domains	1590:1661	the fourth (Asn-382) and fifth (Asn-409) epidermal growth factor domains	1590:1661	Five peptides with N-linked carbohydrate were also isolated and contained glycosylation sites in the lectin-like domain (Asn-47, Asn-115, Asn-116) and in the fourth (Asn-382) and fifth (Asn-409) epidermal growth factor domains.
1314561	0	28	theme	Recombinant	0:10	arg1	thrombomodulin					18:31	Recombinant human thrombomodulin	0:31	Recombinant human thrombomodulin	0:31	Recombinant human thrombomodulin.
1314561	8	29	theme	O-glycosylation	1054:1068	arg1	domain					1070:1075	the entire O-glycosylation domain	1043:1075	the entire O-glycosylation domain	1043:1075	Trypsin digestion of labelled TMD1-105 permitted isolation of two overlapping peptides that contained chondroitin sulphate, spanned the entire O-glycosylation domain and had O-glycosylation sites at Ser-492, Ser-498, Thr-500, Thr-504 and Thr-506.
1314561	7	30	theme	lyase	894:898	arg1	digestion					900:908	chondroitin ABC lyase digestion	878:908	chondroitin ABC lyase digestion	878:908	The properties of TMD1-105 were converted into those of TMD1-75 by chondroitin ABC lyase digestion.
1314561	1	31	theme	glycosaminoglycan	98:114	arg1	chain					121:125	a glycosaminoglycan side chain	96:125	a glycosaminoglycan side chain	96:125	Regulation of cofactor activity and anticoagulant function by a glycosaminoglycan side chain.
1314561	11	32	from	role	1668:1671	arg1	functions					1726:1734	the functions	1722:1734	the functions of human thrombomodulin	1722:1758	The role of N-linked and simple O-linked carbohydrates in the functions of human thrombomodulin remain unclear.
1314561	10	33	theme	lectin-like	1537:1547	arg1	Asn-116					1574:1580	Asn-116	1574:1580	Asn-116	1574:1580	Five peptides with N-linked carbohydrate were also isolated and contained glycosylation sites in the lectin-like domain (Asn-47, Asn-115, Asn-116) and in the fourth (Asn-382) and fifth (Asn-409) epidermal growth factor domains.
1314561	10	33	theme	lectin-like	1537:1547	arg1	domain					1549:1554	the lectin-like domain	1533:1554	the lectin-like domain (Asn-47, Asn-115, Asn-116)	1533:1581	Five peptides with N-linked carbohydrate were also isolated and contained glycosylation sites in the lectin-like domain (Asn-47, Asn-115, Asn-116) and in the fourth (Asn-382) and fifth (Asn-409) epidermal growth factor domains.
1314561	9	34	theme	strong	1353:1358	arg1	similarity					1360:1369	strong similarity	1353:1369	strong similarity to chondroitin sulphate attachment sites in other proteoglycans	1353:1433	The chondroitin sulphate-attachment site was assigned to Ser-492 as this residue is conserved in mouse and bovine thrombomodulin and lies within a sequence Ser-Gly-Ser-492-Gly-Glu-Pro, which has strong similarity to chondroitin sulphate attachment sites in other proteoglycans.
1314561	12	35	theme	human	1863:1867	arg1	thrombomodulin					1869:1882	human thrombomodulin	1863:1882	human thrombomodulin	1863:1882	The present studies demonstrate, however, that the presence of chondroitin sulphate in human thrombomodulin has profound effects on all of the anticoagulant properties of this important anticoagulant thrombin receptor.
1314561	11	36	theme	O-linked	1696:1703	arg1	carbohydrates					1705:1717	N-linked and simple O-linked carbohydrates	1676:1717	N-linked and simple O-linked carbohydrates	1676:1717	The role of N-linked and simple O-linked carbohydrates in the functions of human thrombomodulin remain unclear.
1314561	8	37	theme	O-glycosylation	1085:1099	arg1	sites					1101:1105	O-glycosylation sites	1085:1105	O-glycosylation sites	1085:1105	Trypsin digestion of labelled TMD1-105 permitted isolation of two overlapping peptides that contained chondroitin sulphate, spanned the entire O-glycosylation domain and had O-glycosylation sites at Ser-492, Ser-498, Thr-500, Thr-504 and Thr-506.
1314561	10	38	with	peptides	1441:1448	arg1	carbohydrate					1464:1475	N-linked carbohydrate	1455:1475	N-linked carbohydrate	1455:1475	Five peptides with N-linked carbohydrate were also isolated and contained glycosylation sites in the lectin-like domain (Asn-47, Asn-115, Asn-116) and in the fourth (Asn-382) and fifth (Asn-409) epidermal growth factor domains.
1314561	6	39	theme	glycosylation	728:740	arg1	patterns					742:749	similar glycosylation patterns	720:749	similar glycosylation patterns	720:749	Other than chondroitin sulphate, the carbohydrate contents of the two glycoforms were identical, indicating similar glycosylation patterns at other O-linked and N-linked sites in the two glycoforms.
1314561	9	40	theme	sulphate	1386:1393	arg1	sites					1406:1410	chondroitin sulphate attachment sites	1374:1410	chondroitin sulphate attachment sites in other proteoglycans	1374:1433	The chondroitin sulphate-attachment site was assigned to Ser-492 as this residue is conserved in mouse and bovine thrombomodulin and lies within a sequence Ser-Gly-Ser-492-Gly-Glu-Pro, which has strong similarity to chondroitin sulphate attachment sites in other proteoglycans.
1314561	8	41	theme	Trypsin	911:917	arg1	digestion					919:927	Trypsin digestion	911:927	Trypsin digestion of labelled TMD1-105	911:948	Trypsin digestion of labelled TMD1-105 permitted isolation of two overlapping peptides that contained chondroitin sulphate, spanned the entire O-glycosylation domain and had O-glycosylation sites at Ser-492, Ser-498, Thr-500, Thr-504 and Thr-506.
1314561	7	42	theme	ABC	890:892	arg1	digestion					900:908	chondroitin ABC lyase digestion	878:908	chondroitin ABC lyase digestion	878:908	The properties of TMD1-105 were converted into those of TMD1-75 by chondroitin ABC lyase digestion.
1314561	12	43	theme	sulphate	1851:1858	arg1	presence					1827:1834	the presence	1823:1834	the presence of chondroitin sulphate in human thrombomodulin	1823:1882	The present studies demonstrate, however, that the presence of chondroitin sulphate in human thrombomodulin has profound effects on all of the anticoagulant properties of this important anticoagulant thrombin receptor.
1314561	9	44	contain	has	1349:1351	arg2	similarity					1360:1369	strong similarity	1353:1369	strong similarity to chondroitin sulphate attachment sites in other proteoglycans	1353:1433	The chondroitin sulphate-attachment site was assigned to Ser-492 as this residue is conserved in mouse and bovine thrombomodulin and lies within a sequence Ser-Gly-Ser-492-Gly-Glu-Pro, which has strong similarity to chondroitin sulphate attachment sites in other proteoglycans.
1314561	9	44	contain	has	1349:1351	arg1	Ser-Gly-Ser-492-Gly-Glu-Pro					1314:1340	a sequence Ser-Gly-Ser-492-Gly-Glu-Pro	1303:1340	a sequence Ser-Gly-Ser-492-Gly-Glu-Pro	1303:1340	The chondroitin sulphate-attachment site was assigned to Ser-492 as this residue is conserved in mouse and bovine thrombomodulin and lies within a sequence Ser-Gly-Ser-492-Gly-Glu-Pro, which has strong similarity to chondroitin sulphate attachment sites in other proteoglycans.
1314561	12	45	contain	has	1884:1886	arg2	effects					1897:1903	profound effects	1888:1903	profound effects	1888:1903	The present studies demonstrate, however, that the presence of chondroitin sulphate in human thrombomodulin has profound effects on all of the anticoagulant properties of this important anticoagulant thrombin receptor.
1314561	12	45	contain	has	1884:1886	arg1	presence					1827:1834	the presence	1823:1834	the presence of chondroitin sulphate in human thrombomodulin	1823:1882	The present studies demonstrate, however, that the presence of chondroitin sulphate in human thrombomodulin has profound effects on all of the anticoagulant properties of this important anticoagulant thrombin receptor.
1314561	9	46	theme	other	1415:1419	arg1	proteoglycans					1421:1433	other proteoglycans	1415:1433	other proteoglycans	1415:1433	The chondroitin sulphate-attachment site was assigned to Ser-492 as this residue is conserved in mouse and bovine thrombomodulin and lies within a sequence Ser-Gly-Ser-492-Gly-Glu-Pro, which has strong similarity to chondroitin sulphate attachment sites in other proteoglycans.
1314561	6	47	link	N-linked	773:780	arg1	sites					782:786	other O-linked and N-linked sites	754:786	other O-linked and N-linked sites in the two glycoforms	754:808	Other than chondroitin sulphate, the carbohydrate contents of the two glycoforms were identical, indicating similar glycosylation patterns at other O-linked and N-linked sites in the two glycoforms.
1314561	1	48	theme	activity	57:64	arg1	Regulation					34:43	Regulation	34:43	Regulation of cofactor activity and anticoagulant function by a glycosaminoglycan side chain.	34:126	Regulation of cofactor activity and anticoagulant function by a glycosaminoglycan side chain.
1314561	8	49	theme	TMD1-105	941:948	arg1	digestion					919:927	Trypsin digestion	911:927	Trypsin digestion of labelled TMD1-105	911:948	Trypsin digestion of labelled TMD1-105 permitted isolation of two overlapping peptides that contained chondroitin sulphate, spanned the entire O-glycosylation domain and had O-glycosylation sites at Ser-492, Ser-498, Thr-500, Thr-504 and Thr-506.
1314561	4	50	used	used	339:342	arg2	265					283:285	265	283:285	265	283:285	265, 12602-12610] were expressed in human 293 cells and used to study the role of glycosylation in the functions of this endothelial-cell thrombin receptor.
1314561	11	51	link	N-linked	1676:1683	arg1	carbohydrates					1705:1717	N-linked and simple O-linked carbohydrates	1676:1717	N-linked and simple O-linked carbohydrates	1676:1717	The role of N-linked and simple O-linked carbohydrates in the functions of human thrombomodulin remain unclear.
1314561	6	52	theme	glycoforms	682:691	arg1	identical					698:706	identical	698:706	identical	698:706	Other than chondroitin sulphate, the carbohydrate contents of the two glycoforms were identical, indicating similar glycosylation patterns at other O-linked and N-linked sites in the two glycoforms.
1314561	6	52	theme	glycoforms	682:691	arg1	contents					662:669	the carbohydrate contents	645:669	the carbohydrate contents of the two glycoforms	645:691	Other than chondroitin sulphate, the carbohydrate contents of the two glycoforms were identical, indicating similar glycosylation patterns at other O-linked and N-linked sites in the two glycoforms.
1314561	4	53	gly	glycosylation	365:377	arg1	receptor					430:437	this endothelial-cell thrombin receptor	399:437	this endothelial-cell thrombin receptor	399:437	265, 12602-12610] were expressed in human 293 cells and used to study the role of glycosylation in the functions of this endothelial-cell thrombin receptor.
1314561	10	54	theme	fourth	1594:1599	arg1	domains					1655:1661	the fourth (Asn-382) and fifth (Asn-409) epidermal growth factor domains	1590:1661	the fourth (Asn-382) and fifth (Asn-409) epidermal growth factor domains	1590:1661	Five peptides with N-linked carbohydrate were also isolated and contained glycosylation sites in the lectin-like domain (Asn-47, Asn-115, Asn-116) and in the fourth (Asn-382) and fifth (Asn-409) epidermal growth factor domains.
1314561	9	55	theme	sulphate-attachment	1174:1192	arg1	site					1194:1197	The chondroitin sulphate-attachment site	1158:1197	The chondroitin sulphate-attachment site	1158:1197	The chondroitin sulphate-attachment site was assigned to Ser-492 as this residue is conserved in mouse and bovine thrombomodulin and lies within a sequence Ser-Gly-Ser-492-Gly-Glu-Pro, which has strong similarity to chondroitin sulphate attachment sites in other proteoglycans.
1314561	12	56	theme	present	1780:1786	arg1	studies					1788:1794	The present studies	1776:1794	The present studies	1776:1794	The present studies demonstrate, however, that the presence of chondroitin sulphate in human thrombomodulin has profound effects on all of the anticoagulant properties of this important anticoagulant thrombin receptor.
1314561	2	57	theme	human	159:163	arg1	thrombomodulin					165:178	a secretable human thrombomodulin	146:178	a secretable human thrombomodulin	146:178	Two glycoforms of a secretable human thrombomodulin mutant [TMD1-105 and TMD1-75; Parkinson, Grinnell, Moore, Hoskins, Vlahos & Bang (1990) J. Biol.
1314561	6	58	theme	N-linked	773:780	arg1	sites					782:786	other O-linked and N-linked sites	754:786	other O-linked and N-linked sites in the two glycoforms	754:808	Other than chondroitin sulphate, the carbohydrate contents of the two glycoforms were identical, indicating similar glycosylation patterns at other O-linked and N-linked sites in the two glycoforms.
1314561	6	59	link	O-linked	760:767	arg1	sites					782:786	other O-linked and N-linked sites	754:786	other O-linked and N-linked sites in the two glycoforms	754:808	Other than chondroitin sulphate, the carbohydrate contents of the two glycoforms were identical, indicating similar glycosylation patterns at other O-linked and N-linked sites in the two glycoforms.
1314561	8	60	theme	peptides	989:996	arg1	isolation					960:968	isolation	960:968	isolation of two overlapping peptides that contained chondroitin sulphate, spanned the entire O-glycosylation domain and had O-glycosylation sites at Ser-492, Ser-498, Thr-500, Thr-504 and Thr-506	960:1155	Trypsin digestion of labelled TMD1-105 permitted isolation of two overlapping peptides that contained chondroitin sulphate, spanned the entire O-glycosylation domain and had O-glycosylation sites at Ser-492, Ser-498, Thr-500, Thr-504 and Thr-506.
1314561	6	61	theme	O-linked	760:767	arg1	sites					782:786	other O-linked and N-linked sites	754:786	other O-linked and N-linked sites in the two glycoforms	754:808	Other than chondroitin sulphate, the carbohydrate contents of the two glycoforms were identical, indicating similar glycosylation patterns at other O-linked and N-linked sites in the two glycoforms.
1314561	5	62	theme	intrinsic	474:482	arg1	labelling					484:492	intrinsic labelling	474:492	intrinsic labelling	474:492	Carbohydrate content analysis and intrinsic labelling with [3H]glucosamine and [35S]sulphate showed that TMD1-105 contained a chondroitin sulphate whereas TMD1-75 did not.
1314561	12	63	theme	receptor	1985:1992	arg1	properties					1933:1942	the anticoagulant properties	1915:1942	the anticoagulant properties of this important anticoagulant thrombin receptor	1915:1992	The present studies demonstrate, however, that the presence of chondroitin sulphate in human thrombomodulin has profound effects on all of the anticoagulant properties of this important anticoagulant thrombin receptor.
1314561	5	64	contain	contained	554:562	arg2	sulphate					578:585	a chondroitin sulphate	564:585	a chondroitin sulphate	564:585	Carbohydrate content analysis and intrinsic labelling with [3H]glucosamine and [35S]sulphate showed that TMD1-105 contained a chondroitin sulphate whereas TMD1-75 did not.
1314561	5	64	contain	contained	554:562	arg1	TMD1-105					545:552	TMD1-105	545:552	TMD1-105	545:552	Carbohydrate content analysis and intrinsic labelling with [3H]glucosamine and [35S]sulphate showed that TMD1-105 contained a chondroitin sulphate whereas TMD1-75 did not.
1314561	4	65	theme	human	319:323	arg1	cells					329:333	human 293 cells	319:333	human 293 cells	319:333	265, 12602-12610] were expressed in human 293 cells and used to study the role of glycosylation in the functions of this endothelial-cell thrombin receptor.
1314561	12	66	attach	presence	1827:1834	arg1	thrombomodulin					1869:1882	human thrombomodulin	1863:1882	human thrombomodulin	1863:1882	The present studies demonstrate, however, that the presence of chondroitin sulphate in human thrombomodulin has profound effects on all of the anticoagulant properties of this important anticoagulant thrombin receptor.
1314561	12	66	attach	presence	1827:1834	arg2	sulphate					1851:1858	chondroitin sulphate	1839:1858	chondroitin sulphate	1839:1858	The present studies demonstrate, however, that the presence of chondroitin sulphate in human thrombomodulin has profound effects on all of the anticoagulant properties of this important anticoagulant thrombin receptor.
1314561	10	67	dep	fourth	1594:1599	arg1	Asn-382					1602:1608	Asn-382	1602:1608	Asn-382	1602:1608	Five peptides with N-linked carbohydrate were also isolated and contained glycosylation sites in the lectin-like domain (Asn-47, Asn-115, Asn-116) and in the fourth (Asn-382) and fifth (Asn-409) epidermal growth factor domains.
1314561	5	68	theme	Carbohydrate	440:451	arg1	analysis					461:468	Carbohydrate content analysis	440:468	Carbohydrate content analysis	440:468	Carbohydrate content analysis and intrinsic labelling with [3H]glucosamine and [35S]sulphate showed that TMD1-105 contained a chondroitin sulphate whereas TMD1-75 did not.
1314561	4	69	theme	endothelial-cell	404:419	arg1	receptor					430:437	this endothelial-cell thrombin receptor	399:437	this endothelial-cell thrombin receptor	399:437	265, 12602-12610] were expressed in human 293 cells and used to study the role of glycosylation in the functions of this endothelial-cell thrombin receptor.
1314561	12	70	theme	anticoagulant	1962:1974	arg1	receptor					1985:1992	this important anticoagulant thrombin receptor	1947:1992	this important anticoagulant thrombin receptor	1947:1992	The present studies demonstrate, however, that the presence of chondroitin sulphate in human thrombomodulin has profound effects on all of the anticoagulant properties of this important anticoagulant thrombin receptor.
1314561	4	71	theme	glycosylation	365:377	arg1	role					357:360	the role	353:360	the role of glycosylation in the functions of this endothelial-cell thrombin receptor	353:437	265, 12602-12610] were expressed in human 293 cells and used to study the role of glycosylation in the functions of this endothelial-cell thrombin receptor.
1314561	6	72	theme	chondroitin	623:633	arg1	sulphate					635:642	chondroitin sulphate	623:642	chondroitin sulphate	623:642	Other than chondroitin sulphate, the carbohydrate contents of the two glycoforms were identical, indicating similar glycosylation patterns at other O-linked and N-linked sites in the two glycoforms.
1314561	8	73	contain	contained	1003:1011	arg1	peptides					989:996	two overlapping peptides	973:996	two overlapping peptides that contained chondroitin sulphate, spanned the entire O-glycosylation domain and had O-glycosylation sites at Ser-492, Ser-498, Thr-500, Thr-504 and Thr-506	973:1155	Trypsin digestion of labelled TMD1-105 permitted isolation of two overlapping peptides that contained chondroitin sulphate, spanned the entire O-glycosylation domain and had O-glycosylation sites at Ser-492, Ser-498, Thr-500, Thr-504 and Thr-506.
1314561	8	73	contain	contained	1003:1011	arg2	sulphate					1025:1032	chondroitin sulphate	1013:1032	chondroitin sulphate	1013:1032	Trypsin digestion of labelled TMD1-105 permitted isolation of two overlapping peptides that contained chondroitin sulphate, spanned the entire O-glycosylation domain and had O-glycosylation sites at Ser-492, Ser-498, Thr-500, Thr-504 and Thr-506.
1314561	9	74	theme	bovine	1265:1270	arg1	thrombomodulin					1272:1285	bovine thrombomodulin	1265:1285	bovine thrombomodulin	1265:1285	The chondroitin sulphate-attachment site was assigned to Ser-492 as this residue is conserved in mouse and bovine thrombomodulin and lies within a sequence Ser-Gly-Ser-492-Gly-Glu-Pro, which has strong similarity to chondroitin sulphate attachment sites in other proteoglycans.
1314561	5	75	with	labelling	484:492	arg1	sulphate					524:531	[35S]sulphate	519:531	[35S]sulphate	519:531	Carbohydrate content analysis and intrinsic labelling with [3H]glucosamine and [35S]sulphate showed that TMD1-105 contained a chondroitin sulphate whereas TMD1-75 did not.
1314561	5	75	with	labelling	484:492	arg1	glucosamine					503:513	[3H]glucosamine	499:513	[3H]glucosamine	499:513	Carbohydrate content analysis and intrinsic labelling with [3H]glucosamine and [35S]sulphate showed that TMD1-105 contained a chondroitin sulphate whereas TMD1-75 did not.
1314561	11	76	theme	human	1739:1743	arg1	thrombomodulin					1745:1758	human thrombomodulin	1739:1758	human thrombomodulin	1739:1758	The role of N-linked and simple O-linked carbohydrates in the functions of human thrombomodulin remain unclear.
1314561	12	77	theme	anticoagulant	1919:1931	arg1	properties					1933:1942	the anticoagulant properties	1915:1942	the anticoagulant properties of this important anticoagulant thrombin receptor	1915:1992	The present studies demonstrate, however, that the presence of chondroitin sulphate in human thrombomodulin has profound effects on all of the anticoagulant properties of this important anticoagulant thrombin receptor.
1314561	4	78	theme	receptor	430:437	arg1	functions					386:394	the functions	382:394	the functions of this endothelial-cell thrombin receptor	382:437	265, 12602-12610] were expressed in human 293 cells and used to study the role of glycosylation in the functions of this endothelial-cell thrombin receptor.
1314561	10	79	theme	N-linked	1455:1462	arg1	carbohydrate					1464:1475	N-linked carbohydrate	1455:1475	N-linked carbohydrate	1455:1475	Five peptides with N-linked carbohydrate were also isolated and contained glycosylation sites in the lectin-like domain (Asn-47, Asn-115, Asn-116) and in the fourth (Asn-382) and fifth (Asn-409) epidermal growth factor domains.
1314561	9	80	theme	sequence	1305:1312	arg1	Ser-Gly-Ser-492-Gly-Glu-Pro					1314:1340	a sequence Ser-Gly-Ser-492-Gly-Glu-Pro	1303:1340	a sequence Ser-Gly-Ser-492-Gly-Glu-Pro	1303:1340	The chondroitin sulphate-attachment site was assigned to Ser-492 as this residue is conserved in mouse and bovine thrombomodulin and lies within a sequence Ser-Gly-Ser-492-Gly-Glu-Pro, which has strong similarity to chondroitin sulphate attachment sites in other proteoglycans.
1314561	8	81	theme	entire	1047:1052	arg1	domain					1070:1075	the entire O-glycosylation domain	1043:1075	the entire O-glycosylation domain	1043:1075	Trypsin digestion of labelled TMD1-105 permitted isolation of two overlapping peptides that contained chondroitin sulphate, spanned the entire O-glycosylation domain and had O-glycosylation sites at Ser-492, Ser-498, Thr-500, Thr-504 and Thr-506.
1314561	1	82	theme	function	84:91	arg1	Regulation					34:43	Regulation	34:43	Regulation of cofactor activity and anticoagulant function by a glycosaminoglycan side chain.	34:126	Regulation of cofactor activity and anticoagulant function by a glycosaminoglycan side chain.
1314561	6	83	from	sites	782:786	arg1	glycoforms					799:808	the two glycoforms	791:808	the two glycoforms	791:808	Other than chondroitin sulphate, the carbohydrate contents of the two glycoforms were identical, indicating similar glycosylation patterns at other O-linked and N-linked sites in the two glycoforms.
1314561	8	84	gly	O-glycosylation	1085:1099	arg2	sites					1101:1105	O-glycosylation sites	1085:1105	O-glycosylation sites	1085:1105	Trypsin digestion of labelled TMD1-105 permitted isolation of two overlapping peptides that contained chondroitin sulphate, spanned the entire O-glycosylation domain and had O-glycosylation sites at Ser-492, Ser-498, Thr-500, Thr-504 and Thr-506.
1314561	10	85	theme	factor	1648:1653	arg1	domains					1655:1661	the fourth (Asn-382) and fifth (Asn-409) epidermal growth factor domains	1590:1661	the fourth (Asn-382) and fifth (Asn-409) epidermal growth factor domains	1590:1661	Five peptides with N-linked carbohydrate were also isolated and contained glycosylation sites in the lectin-like domain (Asn-47, Asn-115, Asn-116) and in the fourth (Asn-382) and fifth (Asn-409) epidermal growth factor domains.
1314561	0	86	theme	human	12:16	arg1	thrombomodulin					18:31	Recombinant human thrombomodulin	0:31	Recombinant human thrombomodulin	0:31	Recombinant human thrombomodulin.
1314561	2	87	gly	glycoforms	132:141	arg1	thrombomodulin					165:178	a secretable human thrombomodulin	146:178	a secretable human thrombomodulin	146:178	Two glycoforms of a secretable human thrombomodulin mutant [TMD1-105 and TMD1-75; Parkinson, Grinnell, Moore, Hoskins, Vlahos & Bang (1990) J. Biol.
1314561	10	88	theme	epidermal	1631:1639	arg1	domains					1655:1661	the fourth (Asn-382) and fifth (Asn-409) epidermal growth factor domains	1590:1661	the fourth (Asn-382) and fifth (Asn-409) epidermal growth factor domains	1590:1661	Five peptides with N-linked carbohydrate were also isolated and contained glycosylation sites in the lectin-like domain (Asn-47, Asn-115, Asn-116) and in the fourth (Asn-382) and fifth (Asn-409) epidermal growth factor domains.
1314561	1	89	theme	side	116:119	arg1	chain					121:125	a glycosaminoglycan side chain	96:125	a glycosaminoglycan side chain	96:125	Regulation of cofactor activity and anticoagulant function by a glycosaminoglycan side chain.
1314561	11	90	theme	simple	1689:1694	arg1	carbohydrates					1705:1717	N-linked and simple O-linked carbohydrates	1676:1717	N-linked and simple O-linked carbohydrates	1676:1717	The role of N-linked and simple O-linked carbohydrates in the functions of human thrombomodulin remain unclear.
1314561	12	91	theme	profound	1888:1895	arg1	effects					1897:1903	profound effects	1888:1903	profound effects	1888:1903	The present studies demonstrate, however, that the presence of chondroitin sulphate in human thrombomodulin has profound effects on all of the anticoagulant properties of this important anticoagulant thrombin receptor.
1314561	11	92	theme	N-linked	1676:1683	arg1	carbohydrates					1705:1717	N-linked and simple O-linked carbohydrates	1676:1717	N-linked and simple O-linked carbohydrates	1676:1717	The role of N-linked and simple O-linked carbohydrates in the functions of human thrombomodulin remain unclear.
1314561	7	93	theme	TMD1-105	829:836	arg1	properties					815:824	The properties	811:824	The properties of TMD1-105	811:836	The properties of TMD1-105 were converted into those of TMD1-75 by chondroitin ABC lyase digestion.
1314561	9	94	theme	chondroitin	1374:1384	arg1	sulphate					1386:1393	chondroitin sulphate	1374:1393	chondroitin sulphate attachment sites in other proteoglycans	1374:1433	The chondroitin sulphate-attachment site was assigned to Ser-492 as this residue is conserved in mouse and bovine thrombomodulin and lies within a sequence Ser-Gly-Ser-492-Gly-Glu-Pro, which has strong similarity to chondroitin sulphate attachment sites in other proteoglycans.
1314561	12	95	theme	chondroitin	1839:1849	arg1	sulphate					1851:1858	chondroitin sulphate	1839:1858	chondroitin sulphate	1839:1858	The present studies demonstrate, however, that the presence of chondroitin sulphate in human thrombomodulin has profound effects on all of the anticoagulant properties of this important anticoagulant thrombin receptor.
1314561	12	96	from	presence	1827:1834	arg1	thrombomodulin					1869:1882	human thrombomodulin	1863:1882	human thrombomodulin	1863:1882	The present studies demonstrate, however, that the presence of chondroitin sulphate in human thrombomodulin has profound effects on all of the anticoagulant properties of this important anticoagulant thrombin receptor.
1314561	6	97	theme	similar	720:726	arg1	patterns					742:749	similar glycosylation patterns	720:749	similar glycosylation patterns	720:749	Other than chondroitin sulphate, the carbohydrate contents of the two glycoforms were identical, indicating similar glycosylation patterns at other O-linked and N-linked sites in the two glycoforms.
1314561	7	98	theme	chondroitin	878:888	arg1	digestion					900:908	chondroitin ABC lyase digestion	878:908	chondroitin ABC lyase digestion	878:908	The properties of TMD1-105 were converted into those of TMD1-75 by chondroitin ABC lyase digestion.
1314561	9	99	theme	attachment	1395:1404	arg1	sites					1406:1410	chondroitin sulphate attachment sites	1374:1410	chondroitin sulphate attachment sites in other proteoglycans	1374:1433	The chondroitin sulphate-attachment site was assigned to Ser-492 as this residue is conserved in mouse and bovine thrombomodulin and lies within a sequence Ser-Gly-Ser-492-Gly-Glu-Pro, which has strong similarity to chondroitin sulphate attachment sites in other proteoglycans.
1314561	9	100	from	sites	1406:1410	arg1	proteoglycans					1421:1433	other proteoglycans	1415:1433	other proteoglycans	1415:1433	The chondroitin sulphate-attachment site was assigned to Ser-492 as this residue is conserved in mouse and bovine thrombomodulin and lies within a sequence Ser-Gly-Ser-492-Gly-Glu-Pro, which has strong similarity to chondroitin sulphate attachment sites in other proteoglycans.
1314561	10	101	gly	glycosylation	1510:1522	arg2	sites					1524:1528	glycosylation sites	1510:1528	glycosylation sites	1510:1528	Five peptides with N-linked carbohydrate were also isolated and contained glycosylation sites in the lectin-like domain (Asn-47, Asn-115, Asn-116) and in the fourth (Asn-382) and fifth (Asn-409) epidermal growth factor domains.
1314561	11	102	theme	carbohydrates	1705:1717	arg1	role					1668:1671	The role	1664:1671	The role of N-linked and simple O-linked carbohydrates in the functions of human thrombomodulin	1664:1758	The role of N-linked and simple O-linked carbohydrates in the functions of human thrombomodulin remain unclear.
1314561	5	103	with	analysis	461:468	arg1	sulphate					524:531	[35S]sulphate	519:531	[35S]sulphate	519:531	Carbohydrate content analysis and intrinsic labelling with [3H]glucosamine and [35S]sulphate showed that TMD1-105 contained a chondroitin sulphate whereas TMD1-75 did not.
1314561	5	103	with	analysis	461:468	arg1	glucosamine					503:513	[3H]glucosamine	499:513	[3H]glucosamine	499:513	Carbohydrate content analysis and intrinsic labelling with [3H]glucosamine and [35S]sulphate showed that TMD1-105 contained a chondroitin sulphate whereas TMD1-75 did not.
1314561	1	104	theme	cofactor	48:55	arg1	activity					57:64	cofactor activity	48:64	cofactor activity	48:64	Regulation of cofactor activity and anticoagulant function by a glycosaminoglycan side chain.
6427223	6	0	located	found	799:803	arg1	cases					761:765	both cases	756:765	both cases	756:765	In both cases six different COOH termini were found.
6427223	6	0	located	found	799:803	arg2	termini					786:792	six different COOH termini	767:792	six different COOH termini	767:792	In both cases six different COOH termini were found.
6427223	2	1	theme	blood	129:133	arg1	lymphocytes					135:145	Fresh human peripheral blood lymphocytes	106:145	Fresh human peripheral blood lymphocytes	106:145	Fresh human peripheral blood lymphocytes were induced with desacetylthymosin -alpha 1 and staphylococcal enterotoxin B.
6427223	9	2	theme	=	995:995	arg1	species					1004:1010	the Mr = 20,000 species	988:1010	the Mr = 20,000 species	988:1010	Both carry carbohydrates in the Mr = 25,000 species whereas in the Mr = 20,000 species only one site is glycosylated.
6427223	10	3	theme	apparent	1082:1089	arg1	weight					1101:1106	apparent molecular weight	1082:1106	apparent molecular weight	1082:1106	This likely explains the difference in apparent molecular weight between the two species and the expected molecular weight based upon the amino acid sequence.
6427223	2	4	theme	peripheral	118:127	arg1	lymphocytes					135:145	Fresh human peripheral blood lymphocytes	106:145	Fresh human peripheral blood lymphocytes	106:145	Fresh human peripheral blood lymphocytes were induced with desacetylthymosin -alpha 1 and staphylococcal enterotoxin B.
6427223	5	5	theme	identical	676:684	arg1	sequences					697:705	identical amino acid sequences	676:705	identical amino acid sequences	676:705	Both species were found to have identical amino acid sequences with a pyroglutamate residue as NH2-terminus.
6427223	5	6	theme	acid	692:695	arg1	sequences					697:705	identical amino acid sequences	676:705	identical amino acid sequences	676:705	Both species were found to have identical amino acid sequences with a pyroglutamate residue as NH2-terminus.
6427223	1	7	gly	glycosylation	91:103	arg2	glycosylation					91:103	glycosylation	91:103	glycosylation	91:103	Complete amino acid sequence and determination of sites of glycosylation.
6427223	1	7	gly	glycosylation	91:103	arg2	sites					82:86	sites	82:86	sites of glycosylation	82:103	Complete amino acid sequence and determination of sites of glycosylation.
6427223	2	8	theme	human	112:116	arg1	lymphocytes					135:145	Fresh human peripheral blood lymphocytes	106:145	Fresh human peripheral blood lymphocytes	106:145	Fresh human peripheral blood lymphocytes were induced with desacetylthymosin -alpha 1 and staphylococcal enterotoxin B.
6427223	3	9	theme	induced	230:236	arg1	interferon					244:253	The induced gamma interferon	226:253	The induced gamma interferon (or IFN-gamma, immune interferon, type II interferon)	226:307	The induced gamma interferon (or IFN-gamma, immune interferon, type II interferon) was purified to homogeneity utilizing controlled-pore glass, concanavalin A-Sepharose, Bio-Gel P100, or Sephacryl S-200, and reversed phase high performance liquid chromatography.
6427223	4	10	theme	sulfate-polyacrylamide	600:621	arg1	electrophoresis					627:641	sodium dodecyl sulfate-polyacrylamide gel electrophoresis	585:641	sodium dodecyl sulfate-polyacrylamide gel electrophoresis	585:641	This procedure resulted in two active species with apparent Mr = 20,000 and 25,000 as judged by sodium dodecyl sulfate-polyacrylamide gel electrophoresis.
6427223	2	11	theme	desacetylthymosin	165:181	arg1	-alpha					183:188	desacetylthymosin -alpha 1	165:190	desacetylthymosin -alpha 1	165:190	Fresh human peripheral blood lymphocytes were induced with desacetylthymosin -alpha 1 and staphylococcal enterotoxin B.
6427223	3	12	theme	gamma	238:242	arg1	interferon					244:253	The induced gamma interferon	226:253	The induced gamma interferon (or IFN-gamma, immune interferon, type II interferon)	226:307	The induced gamma interferon (or IFN-gamma, immune interferon, type II interferon) was purified to homogeneity utilizing controlled-pore glass, concanavalin A-Sepharose, Bio-Gel P100, or Sephacryl S-200, and reversed phase high performance liquid chromatography.
6427223	8	13	theme	possible	881:888	arg1	sites					918:922	two possible Asn-X-Ser/Thr glycosylation sites	877:922	two possible Asn-X-Ser/Thr glycosylation sites	877:922	There are two possible Asn-X-Ser/Thr glycosylation sites.
6427223	3	14	theme	phase	443:447	arg1	chromatography					473:486	reversed phase high performance liquid chromatography	434:486	reversed phase high performance liquid chromatography	434:486	The induced gamma interferon (or IFN-gamma, immune interferon, type II interferon) was purified to homogeneity utilizing controlled-pore glass, concanavalin A-Sepharose, Bio-Gel P100, or Sephacryl S-200, and reversed phase high performance liquid chromatography.
6427223	10	15	theme	acid	1187:1190	arg1	sequence					1192:1199	the amino acid sequence	1177:1199	the amino acid sequence	1177:1199	This likely explains the difference in apparent molecular weight between the two species and the expected molecular weight based upon the amino acid sequence.
6427223	3	16	theme	immune	270:275	arg1	IFN-gamma					259:267	IFN-gamma	259:267	IFN-gamma	259:267	The induced gamma interferon (or IFN-gamma, immune interferon, type II interferon) was purified to homogeneity utilizing controlled-pore glass, concanavalin A-Sepharose, Bio-Gel P100, or Sephacryl S-200, and reversed phase high performance liquid chromatography.
6427223	3	16	theme	immune	270:275	arg1	interferon					277:286	immune interferon	270:286	immune interferon	270:286	The induced gamma interferon (or IFN-gamma, immune interferon, type II interferon) was purified to homogeneity utilizing controlled-pore glass, concanavalin A-Sepharose, Bio-Gel P100, or Sephacryl S-200, and reversed phase high performance liquid chromatography.
6427223	1	17	theme	sites	82:86	arg1	determination					65:77	determination	65:77	determination of sites of glycosylation	65:103	Complete amino acid sequence and determination of sites of glycosylation.
6427223	1	17	theme	sites	82:86	arg1	sequence					52:59	Complete amino acid sequence	32:59	Complete amino acid sequence	32:59	Complete amino acid sequence and determination of sites of glycosylation.
6427223	7	18	dep	qualitatively	825:837	arg1	at					816:817	at	816:817	at	816:817	They are, at least qualitatively, identical in both species.
6427223	3	19	theme	high	449:452	arg1	chromatography					473:486	reversed phase high performance liquid chromatography	434:486	reversed phase high performance liquid chromatography	434:486	The induced gamma interferon (or IFN-gamma, immune interferon, type II interferon) was purified to homogeneity utilizing controlled-pore glass, concanavalin A-Sepharose, Bio-Gel P100, or Sephacryl S-200, and reversed phase high performance liquid chromatography.
6427223	0	20	theme	human	8:12	arg1	interferon-gamma					14:29	Natural human interferon-gamma	0:29	Natural human interferon-gamma.	0:30	Natural human interferon-gamma.
6427223	8	21	theme	glycosylation	904:916	arg1	sites					918:922	two possible Asn-X-Ser/Thr glycosylation sites	877:922	two possible Asn-X-Ser/Thr glycosylation sites	877:922	There are two possible Asn-X-Ser/Thr glycosylation sites.
6427223	8	22	theme	Asn-X-Ser/Thr	890:902	arg1	sites					918:922	two possible Asn-X-Ser/Thr glycosylation sites	877:922	two possible Asn-X-Ser/Thr glycosylation sites	877:922	There are two possible Asn-X-Ser/Thr glycosylation sites.
6427223	0	23	theme	Natural	0:6	arg1	interferon-gamma					14:29	Natural human interferon-gamma	0:29	Natural human interferon-gamma.	0:30	Natural human interferon-gamma.
6427223	10	24	theme	expected	1140:1147	arg1	weight					1159:1164	the expected molecular weight	1136:1164	the expected molecular weight based upon the amino acid sequence	1136:1199	This likely explains the difference in apparent molecular weight between the two species and the expected molecular weight based upon the amino acid sequence.
6427223	1	25	theme	glycosylation	91:103	arg1	glycosylation					91:103	glycosylation	91:103	glycosylation	91:103	Complete amino acid sequence and determination of sites of glycosylation.
6427223	1	25	theme	glycosylation	91:103	arg1	sites					82:86	sites	82:86	sites of glycosylation	82:103	Complete amino acid sequence and determination of sites of glycosylation.
6427223	3	26	theme	reversed	434:441	arg1	chromatography					473:486	reversed phase high performance liquid chromatography	434:486	reversed phase high performance liquid chromatography	434:486	The induced gamma interferon (or IFN-gamma, immune interferon, type II interferon) was purified to homogeneity utilizing controlled-pore glass, concanavalin A-Sepharose, Bio-Gel P100, or Sephacryl S-200, and reversed phase high performance liquid chromatography.
6427223	3	27	dep	interferon	244:253	arg1	IFN-gamma					259:267	IFN-gamma	259:267	IFN-gamma	259:267	The induced gamma interferon (or IFN-gamma, immune interferon, type II interferon) was purified to homogeneity utilizing controlled-pore glass, concanavalin A-Sepharose, Bio-Gel P100, or Sephacryl S-200, and reversed phase high performance liquid chromatography.
6427223	3	27	dep	interferon	244:253	arg1	interferon					277:286	immune interferon	270:286	immune interferon	270:286	The induced gamma interferon (or IFN-gamma, immune interferon, type II interferon) was purified to homogeneity utilizing controlled-pore glass, concanavalin A-Sepharose, Bio-Gel P100, or Sephacryl S-200, and reversed phase high performance liquid chromatography.
6427223	3	27	dep	interferon	244:253	arg1	interferon					297:306	type II interferon	289:306	type II interferon	289:306	The induced gamma interferon (or IFN-gamma, immune interferon, type II interferon) was purified to homogeneity utilizing controlled-pore glass, concanavalin A-Sepharose, Bio-Gel P100, or Sephacryl S-200, and reversed phase high performance liquid chromatography.
6427223	3	28	theme	type	289:292	arg1	IFN-gamma					259:267	IFN-gamma	259:267	IFN-gamma	259:267	The induced gamma interferon (or IFN-gamma, immune interferon, type II interferon) was purified to homogeneity utilizing controlled-pore glass, concanavalin A-Sepharose, Bio-Gel P100, or Sephacryl S-200, and reversed phase high performance liquid chromatography.
6427223	3	28	theme	type	289:292	arg1	interferon					297:306	type II interferon	289:306	type II interferon	289:306	The induced gamma interferon (or IFN-gamma, immune interferon, type II interferon) was purified to homogeneity utilizing controlled-pore glass, concanavalin A-Sepharose, Bio-Gel P100, or Sephacryl S-200, and reversed phase high performance liquid chromatography.
6427223	3	29	theme	Bio-Gel	396:402	arg1	P100					404:407	Bio-Gel P100	396:407	Bio-Gel P100	396:407	The induced gamma interferon (or IFN-gamma, immune interferon, type II interferon) was purified to homogeneity utilizing controlled-pore glass, concanavalin A-Sepharose, Bio-Gel P100, or Sephacryl S-200, and reversed phase high performance liquid chromatography.
6427223	2	30	theme	staphylococcal	196:209	arg1	B					223:223	staphylococcal enterotoxin B	196:223	staphylococcal enterotoxin B	196:223	Fresh human peripheral blood lymphocytes were induced with desacetylthymosin -alpha 1 and staphylococcal enterotoxin B.
6427223	9	31	theme	20,000	997:1002	arg1	species					1004:1010	the Mr = 20,000 species	988:1010	the Mr = 20,000 species	988:1010	Both carry carbohydrates in the Mr = 25,000 species whereas in the Mr = 20,000 species only one site is glycosylated.
6427223	3	32	theme	performance	454:464	arg1	chromatography					473:486	reversed phase high performance liquid chromatography	434:486	reversed phase high performance liquid chromatography	434:486	The induced gamma interferon (or IFN-gamma, immune interferon, type II interferon) was purified to homogeneity utilizing controlled-pore glass, concanavalin A-Sepharose, Bio-Gel P100, or Sephacryl S-200, and reversed phase high performance liquid chromatography.
6427223	2	33	theme	Fresh	106:110	arg1	lymphocytes					135:145	Fresh human peripheral blood lymphocytes	106:145	Fresh human peripheral blood lymphocytes	106:145	Fresh human peripheral blood lymphocytes were induced with desacetylthymosin -alpha 1 and staphylococcal enterotoxin B.
6427223	8	34	gly	glycosylation	904:916	arg2	two					877:879	two	877:879	two	877:879	There are two possible Asn-X-Ser/Thr glycosylation sites.
6427223	8	34	gly	glycosylation	904:916	arg2	sites					918:922	two possible Asn-X-Ser/Thr glycosylation sites	877:922	two possible Asn-X-Ser/Thr glycosylation sites	877:922	There are two possible Asn-X-Ser/Thr glycosylation sites.
6427223	7	35	from	identical	840:848	arg1	species					858:864	both species	853:864	both species	853:864	They are, at least qualitatively, identical in both species.
6427223	3	36	theme	liquid	466:471	arg1	chromatography					473:486	reversed phase high performance liquid chromatography	434:486	reversed phase high performance liquid chromatography	434:486	The induced gamma interferon (or IFN-gamma, immune interferon, type II interferon) was purified to homogeneity utilizing controlled-pore glass, concanavalin A-Sepharose, Bio-Gel P100, or Sephacryl S-200, and reversed phase high performance liquid chromatography.
6427223	3	37	theme	concanavalin	370:381	arg1	A-Sepharose					383:393	concanavalin A-Sepharose	370:393	concanavalin A-Sepharose	370:393	The induced gamma interferon (or IFN-gamma, immune interferon, type II interferon) was purified to homogeneity utilizing controlled-pore glass, concanavalin A-Sepharose, Bio-Gel P100, or Sephacryl S-200, and reversed phase high performance liquid chromatography.
6427223	3	38	theme	Sephacryl	413:421	arg1	S-200					423:427	Sephacryl S-200	413:427	Sephacryl S-200	413:427	The induced gamma interferon (or IFN-gamma, immune interferon, type II interferon) was purified to homogeneity utilizing controlled-pore glass, concanavalin A-Sepharose, Bio-Gel P100, or Sephacryl S-200, and reversed phase high performance liquid chromatography.
6427223	10	39	theme	molecular	1091:1099	arg1	weight					1101:1106	apparent molecular weight	1082:1106	apparent molecular weight	1082:1106	This likely explains the difference in apparent molecular weight between the two species and the expected molecular weight based upon the amino acid sequence.
6427223	5	40	theme	amino	686:690	arg1	sequences					697:705	identical amino acid sequences	676:705	identical amino acid sequences	676:705	Both species were found to have identical amino acid sequences with a pyroglutamate residue as NH2-terminus.
6427223	6	41	theme	COOH	781:784	arg1	termini					786:792	six different COOH termini	767:792	six different COOH termini	767:792	In both cases six different COOH termini were found.
6427223	4	42	with	species	527:533	arg1	Mr					549:550	apparent Mr	540:550	apparent Mr = 20,000 and 25,000	540:570	This procedure resulted in two active species with apparent Mr = 20,000 and 25,000 as judged by sodium dodecyl sulfate-polyacrylamide gel electrophoresis.
6427223	10	43	theme	molecular	1149:1157	arg1	weight					1159:1164	the expected molecular weight	1136:1164	the expected molecular weight based upon the amino acid sequence	1136:1199	This likely explains the difference in apparent molecular weight between the two species and the expected molecular weight based upon the amino acid sequence.
6427223	9	44	dep	=	960:960	arg1	species					969:975	25,000 species	962:975	25,000 species	962:975	Both carry carbohydrates in the Mr = 25,000 species whereas in the Mr = 20,000 species only one site is glycosylated.
6427223	7	45	from	species	858:864	arg1	identical					840:848	identical	840:848	identical	840:848	They are, at least qualitatively, identical in both species.
6427223	1	46	theme	Complete	32:39	arg1	sequence					52:59	Complete amino acid sequence	32:59	Complete amino acid sequence	32:59	Complete amino acid sequence and determination of sites of glycosylation.
6427223	6	47	theme	different	771:779	arg1	termini					786:792	six different COOH termini	767:792	six different COOH termini	767:792	In both cases six different COOH termini were found.
6427223	10	48	from	difference	1068:1077	arg1	weight					1101:1106	apparent molecular weight	1082:1106	apparent molecular weight	1082:1106	This likely explains the difference in apparent molecular weight between the two species and the expected molecular weight based upon the amino acid sequence.
6427223	5	49	theme	pyroglutamate	714:726	arg1	residue					728:734	a pyroglutamate residue	712:734	a pyroglutamate residue as NH2-terminus	712:750	Both species were found to have identical amino acid sequences with a pyroglutamate residue as NH2-terminus.
6427223	9	50	from	carbohydrates	936:948	arg1	Mr					957:958	the Mr	953:958	the Mr = 25,000 species	953:975	Both carry carbohydrates in the Mr = 25,000 species whereas in the Mr = 20,000 species only one site is glycosylated.
6427223	1	51	theme	amino	41:45	arg1	sequence					52:59	Complete amino acid sequence	32:59	Complete amino acid sequence	32:59	Complete amino acid sequence and determination of sites of glycosylation.
6427223	4	52	theme	gel	623:625	arg1	electrophoresis					627:641	sodium dodecyl sulfate-polyacrylamide gel electrophoresis	585:641	sodium dodecyl sulfate-polyacrylamide gel electrophoresis	585:641	This procedure resulted in two active species with apparent Mr = 20,000 and 25,000 as judged by sodium dodecyl sulfate-polyacrylamide gel electrophoresis.
6427223	9	53	theme	=	960:960	arg1	Mr					957:958	the Mr	953:958	the Mr = 25,000 species	953:975	Both carry carbohydrates in the Mr = 25,000 species whereas in the Mr = 20,000 species only one site is glycosylated.
6427223	2	54	theme	enterotoxin	211:221	arg1	B					223:223	staphylococcal enterotoxin B	196:223	staphylococcal enterotoxin B	196:223	Fresh human peripheral blood lymphocytes were induced with desacetylthymosin -alpha 1 and staphylococcal enterotoxin B.
6427223	1	55	theme	acid	47:50	arg1	sequence					52:59	Complete amino acid sequence	32:59	Complete amino acid sequence	32:59	Complete amino acid sequence and determination of sites of glycosylation.
6427223	9	56	contain	carry	930:934	arg2	carbohydrates					936:948	carbohydrates	936:948	carbohydrates in the Mr = 25,000 species	936:975	Both carry carbohydrates in the Mr = 25,000 species whereas in the Mr = 20,000 species only one site is glycosylated.
6427223	9	56	contain	carry	930:934	arg1	Both					925:928	Both	925:928	Both	925:928	Both carry carbohydrates in the Mr = 25,000 species whereas in the Mr = 20,000 species only one site is glycosylated.
6427223	10	57	theme	amino	1181:1185	arg1	sequence					1192:1199	the amino acid sequence	1177:1199	the amino acid sequence	1177:1199	This likely explains the difference in apparent molecular weight between the two species and the expected molecular weight based upon the amino acid sequence.
6427223	3	58	theme	controlled-pore	347:361	arg1	glass					363:367	controlled-pore glass	347:367	controlled-pore glass	347:367	The induced gamma interferon (or IFN-gamma, immune interferon, type II interferon) was purified to homogeneity utilizing controlled-pore glass, concanavalin A-Sepharose, Bio-Gel P100, or Sephacryl S-200, and reversed phase high performance liquid chromatography.
6427223	4	59	theme	active	520:525	arg1	species					527:533	two active species	516:533	two active species with apparent Mr = 20,000 and 25,000	516:570	This procedure resulted in two active species with apparent Mr = 20,000 and 25,000 as judged by sodium dodecyl sulfate-polyacrylamide gel electrophoresis.
6427223	5	60	contain	have	671:674	arg2	sequences					697:705	identical amino acid sequences	676:705	identical amino acid sequences	676:705	Both species were found to have identical amino acid sequences with a pyroglutamate residue as NH2-terminus.
6427223	5	60	contain	have	671:674	arg1	species					649:655	Both species	644:655	Both species	644:655	Both species were found to have identical amino acid sequences with a pyroglutamate residue as NH2-terminus.
6427223	9	61	gly	glycosylated	1029:1040	arg1	species					1004:1010	the Mr = 20,000 species	988:1010	the Mr = 20,000 species	988:1010	Both carry carbohydrates in the Mr = 25,000 species whereas in the Mr = 20,000 species only one site is glycosylated.
6427223	9	61	gly	glycosylated	1029:1040	arg1	site					1021:1024	only one site	1012:1024	only one site	1012:1024	Both carry carbohydrates in the Mr = 25,000 species whereas in the Mr = 20,000 species only one site is glycosylated.
6427223	9	61	gly	glycosylated	1029:1040	arg2	site					1021:1024	only one site	1012:1024	only one site	1012:1024	Both carry carbohydrates in the Mr = 25,000 species whereas in the Mr = 20,000 species only one site is glycosylated.
6427223	4	62	theme	apparent	540:547	arg1	Mr					549:550	apparent Mr	540:550	apparent Mr = 20,000 and 25,000	540:570	This procedure resulted in two active species with apparent Mr = 20,000 and 25,000 as judged by sodium dodecyl sulfate-polyacrylamide gel electrophoresis.
10731668	0	0	theme	recombinant	90:100	arg1	receptor					132:139	recombinant human epidermal growth factor receptor	90:139	recombinant human epidermal growth factor receptor	90:139	Characterization of the N-oligosaccharides attached to the atypical Asn-X-Cys sequence of recombinant human epidermal growth factor receptor.
10731668	4	1	theme	CHO	800:802	arg1	cells					804:808	CHO cells	800:808	CHO cells	800:808	Deletion of this atypical glycosylation site by replacement of Asn(32 ) with lysine changed neither the expression nor function of the full length EGFR in CHO cells.
10731668	1	2	theme	human	170:174	arg1	sEGFR					190:194	sEGFR	190:194	sEGFR	190:194	The extracellular domain of human EGF receptor (sEGFR) produced by CHO cells has been used in various biophysical studies to elucidate the molecular mechanism of EGF-induced receptor activation.
10731668	1	2	theme	human	170:174	arg1	receptor					180:187	human EGF receptor	170:187	human EGF receptor (sEGFR) produced by CHO cells	170:217	The extracellular domain of human EGF receptor (sEGFR) produced by CHO cells has been used in various biophysical studies to elucidate the molecular mechanism of EGF-induced receptor activation.
10731668	1	3	theme	various	236:242	arg1	studies					256:262	various biophysical studies	236:262	various biophysical studies	236:262	The extracellular domain of human EGF receptor (sEGFR) produced by CHO cells has been used in various biophysical studies to elucidate the molecular mechanism of EGF-induced receptor activation.
10731668	2	4	theme	-X	473:474	arg1	sequence					455:462	an atypical N-glycosylation consensus sequence	417:462	an atypical N-glycosylation consensus sequence	417:462	We have found that the CHO sEGFR contains one oligosaccharide chain attached to an atypical N-glycosylation consensus sequence, Asn(32 )-X( 33 )-Cys(34 ).
10731668	2	4	theme	-X	473:474	arg1	34					486:487	34	486:487	34	486:487	We have found that the CHO sEGFR contains one oligosaccharide chain attached to an atypical N-glycosylation consensus sequence, Asn(32 )-X( 33 )-Cys(34 ).
10731668	2	4	theme	-X	473:474	arg1	-Cys					481:484	Asn(32 )-X( 33 )-Cys	465:484	Asn(32 )-X( 33 )-Cys(34 )	465:489	We have found that the CHO sEGFR contains one oligosaccharide chain attached to an atypical N-glycosylation consensus sequence, Asn(32 )-X( 33 )-Cys(34 ).
10731668	3	5	theme	oligosaccharide	628:642	arg1	forms					575:579	the monosialo and asialo forms	550:579	the monosialo and asialo forms of a core fucosylated biantennary complex-type oligosaccharide	550:642	The oligosaccharide structure at Asn(32 ) is a mixture of the monosialo and asialo forms of a core fucosylated biantennary complex-type oligosaccharide.
10731668	1	6	theme	EGF	176:178	arg1	sEGFR					190:194	sEGFR	190:194	sEGFR	190:194	The extracellular domain of human EGF receptor (sEGFR) produced by CHO cells has been used in various biophysical studies to elucidate the molecular mechanism of EGF-induced receptor activation.
10731668	1	6	theme	EGF	176:178	arg1	receptor					180:187	human EGF receptor	170:187	human EGF receptor (sEGFR) produced by CHO cells	170:217	The extracellular domain of human EGF receptor (sEGFR) produced by CHO cells has been used in various biophysical studies to elucidate the molecular mechanism of EGF-induced receptor activation.
10731668	1	7	theme	biophysical	244:254	arg1	studies					256:262	various biophysical studies	236:262	various biophysical studies	236:262	The extracellular domain of human EGF receptor (sEGFR) produced by CHO cells has been used in various biophysical studies to elucidate the molecular mechanism of EGF-induced receptor activation.
10731668	0	8	theme	epidermal	108:116	arg1	receptor					132:139	recombinant human epidermal growth factor receptor	90:139	recombinant human epidermal growth factor receptor	90:139	Characterization of the N-oligosaccharides attached to the atypical Asn-X-Cys sequence of recombinant human epidermal growth factor receptor.
10731668	5	9	from	Asn	832:834	arg1	incomplete					858:867	incomplete	858:867	incomplete	858:867	The glycosylation at Asn(32 ) in CHO sEGFR was incomplete: 20% of Asn(32 ) remained unmodified.
10731668	5	9	from	Asn	832:834	arg1	glycosylation					815:827	The glycosylation	811:827	The glycosylation at Asn(32 ) in CHO sEGFR	811:852	The glycosylation at Asn(32 ) in CHO sEGFR was incomplete: 20% of Asn(32 ) remained unmodified.
10731668	3	10	theme	oligosaccharide	496:510	arg1	mixture					539:545	a mixture	537:545	a mixture of the monosialo and asialo forms of a core fucosylated biantennary complex-type oligosaccharide	537:642	The oligosaccharide structure at Asn(32 ) is a mixture of the monosialo and asialo forms of a core fucosylated biantennary complex-type oligosaccharide.
10731668	3	10	theme	oligosaccharide	496:510	arg1	structure					512:520	The oligosaccharide structure	492:520	The oligosaccharide structure at Asn(32 )	492:532	The oligosaccharide structure at Asn(32 ) is a mixture of the monosialo and asialo forms of a core fucosylated biantennary complex-type oligosaccharide.
10731668	0	11	theme	human	102:106	arg1	receptor					132:139	recombinant human epidermal growth factor receptor	90:139	recombinant human epidermal growth factor receptor	90:139	Characterization of the N-oligosaccharides attached to the atypical Asn-X-Cys sequence of recombinant human epidermal growth factor receptor.
10731668	6	12	theme	biophysical	1022:1032	arg1	studies					1034:1040	biophysical studies	1022:1040	biophysical studies	1022:1040	Thus, CHO sEGFR itself is heterogeneous with respect to the glycosylation at Asn(32 ), which may cause problems in biophysical studies.
10731668	5	13	theme	Asn	877:879	arg1	32					881:882	32	881:882	32	881:882	The glycosylation at Asn(32 ) in CHO sEGFR was incomplete: 20% of Asn(32 ) remained unmodified.
10731668	5	13	theme	Asn	877:879	arg1	Asn					877:879	Asn	877:879	Asn(32 )	877:884	The glycosylation at Asn(32 ) in CHO sEGFR was incomplete: 20% of Asn(32 ) remained unmodified.
10731668	5	13	theme	Asn	877:879	arg1	%					872:872	20%	870:872	20% of Asn(32 )	870:884	The glycosylation at Asn(32 ) in CHO sEGFR was incomplete: 20% of Asn(32 ) remained unmodified.
10731668	4	14	theme	glycosylation	671:683	arg1	site					685:688	this atypical glycosylation site	657:688	this atypical glycosylation site	657:688	Deletion of this atypical glycosylation site by replacement of Asn(32 ) with lysine changed neither the expression nor function of the full length EGFR in CHO cells.
10731668	0	15	theme	factor	125:130	arg1	receptor					132:139	recombinant human epidermal growth factor receptor	90:139	recombinant human epidermal growth factor receptor	90:139	Characterization of the N-oligosaccharides attached to the atypical Asn-X-Cys sequence of recombinant human epidermal growth factor receptor.
10731668	4	16	theme	full	780:783	arg1	EGFR					792:795	the full length EGFR	776:795	the full length EGFR	776:795	Deletion of this atypical glycosylation site by replacement of Asn(32 ) with lysine changed neither the expression nor function of the full length EGFR in CHO cells.
10731668	5	17	from	glycosylation	815:827	arg1	sEGFR					848:852	CHO sEGFR	844:852	CHO sEGFR	844:852	The glycosylation at Asn(32 ) in CHO sEGFR was incomplete: 20% of Asn(32 ) remained unmodified.
10731668	1	18	theme	receptor	180:187	arg1	receptor					180:187	human EGF receptor	170:187	human EGF receptor (sEGFR) produced by CHO cells	170:217	The extracellular domain of human EGF receptor (sEGFR) produced by CHO cells has been used in various biophysical studies to elucidate the molecular mechanism of EGF-induced receptor activation.
10731668	1	18	theme	receptor	180:187	arg1	domain					160:165	The extracellular domain	142:165	The extracellular domain of human EGF receptor (sEGFR) produced by CHO cells	142:217	The extracellular domain of human EGF receptor (sEGFR) produced by CHO cells has been used in various biophysical studies to elucidate the molecular mechanism of EGF-induced receptor activation.
10731668	0	19	theme	growth	118:123	arg1	receptor					132:139	recombinant human epidermal growth factor receptor	90:139	recombinant human epidermal growth factor receptor	90:139	Characterization of the N-oligosaccharides attached to the atypical Asn-X-Cys sequence of recombinant human epidermal growth factor receptor.
10731668	0	20	attach	attached	43:50	arg2	Characterization					0:15	Characterization	0:15	Characterization of the N-oligosaccharides	0:41	Characterization of the N-oligosaccharides attached to the atypical Asn-X-Cys sequence of recombinant human epidermal growth factor receptor.
10731668	0	20	attach	attached	43:50	arg1	sequence					78:85	the atypical Asn-X-Cys sequence	55:85	the atypical Asn-X-Cys sequence of recombinant human epidermal growth factor receptor	55:139	Characterization of the N-oligosaccharides attached to the atypical Asn-X-Cys sequence of recombinant human epidermal growth factor receptor.
10731668	2	21	theme	oligosaccharide	383:397	arg1	chain					399:403	one oligosaccharide chain	379:403	one oligosaccharide chain attached to an atypical N-glycosylation consensus sequence, Asn(32 )-X( 33 )-Cys(34 )	379:489	We have found that the CHO sEGFR contains one oligosaccharide chain attached to an atypical N-glycosylation consensus sequence, Asn(32 )-X( 33 )-Cys(34 ).
10731668	4	22	theme	EGFR	792:795	arg1	expression					749:758	expression	749:758	expression	749:758	Deletion of this atypical glycosylation site by replacement of Asn(32 ) with lysine changed neither the expression nor function of the full length EGFR in CHO cells.
10731668	5	23	theme	CHO	844:846	arg1	sEGFR					848:852	CHO sEGFR	844:852	CHO sEGFR	844:852	The glycosylation at Asn(32 ) in CHO sEGFR was incomplete: 20% of Asn(32 ) remained unmodified.
10731668	8	24	theme	Lys	1207:1209	arg1	mutation					1184:1191	the mutation	1180:1191	the mutation of Asn(32) -> Lys(32 )	1180:1214	Therefore, sEGFR with the mutation of Asn(32) -> Lys(32 )is useful for biophysical and biochemical studies, and, particularly, for X-ray crystallography.
10731668	4	25	theme	length	785:790	arg1	EGFR					792:795	the full length EGFR	776:795	the full length EGFR	776:795	Deletion of this atypical glycosylation site by replacement of Asn(32 ) with lysine changed neither the expression nor function of the full length EGFR in CHO cells.
10731668	0	26	theme	N-oligosaccharides	24:41	arg1	Characterization					0:15	Characterization	0:15	Characterization of the N-oligosaccharides	0:41	Characterization of the N-oligosaccharides attached to the atypical Asn-X-Cys sequence of recombinant human epidermal growth factor receptor.
10731668	4	27	theme	Asn	708:710	arg1	replacement					693:703	replacement	693:703	replacement of Asn(32 ) with lysine	693:727	Deletion of this atypical glycosylation site by replacement of Asn(32 ) with lysine changed neither the expression nor function of the full length EGFR in CHO cells.
10731668	2	28	theme	atypical	420:427	arg1	sequence					455:462	an atypical N-glycosylation consensus sequence	417:462	an atypical N-glycosylation consensus sequence	417:462	We have found that the CHO sEGFR contains one oligosaccharide chain attached to an atypical N-glycosylation consensus sequence, Asn(32 )-X( 33 )-Cys(34 ).
10731668	2	28	theme	atypical	420:427	arg1	-Cys					481:484	Asn(32 )-X( 33 )-Cys	465:484	Asn(32 )-X( 33 )-Cys(34 )	465:489	We have found that the CHO sEGFR contains one oligosaccharide chain attached to an atypical N-glycosylation consensus sequence, Asn(32 )-X( 33 )-Cys(34 ).
10731668	2	29	theme	N-glycosylation	429:443	arg1	sequence					455:462	an atypical N-glycosylation consensus sequence	417:462	an atypical N-glycosylation consensus sequence	417:462	We have found that the CHO sEGFR contains one oligosaccharide chain attached to an atypical N-glycosylation consensus sequence, Asn(32 )-X( 33 )-Cys(34 ).
10731668	2	29	theme	N-glycosylation	429:443	arg1	-Cys					481:484	Asn(32 )-X( 33 )-Cys	465:484	Asn(32 )-X( 33 )-Cys(34 )	465:489	We have found that the CHO sEGFR contains one oligosaccharide chain attached to an atypical N-glycosylation consensus sequence, Asn(32 )-X( 33 )-Cys(34 ).
10731668	1	30	theme	molecular	281:289	arg1	mechanism					291:299	the molecular mechanism	277:299	the molecular mechanism of EGF-induced receptor activation	277:334	The extracellular domain of human EGF receptor (sEGFR) produced by CHO cells has been used in various biophysical studies to elucidate the molecular mechanism of EGF-induced receptor activation.
10731668	0	31	theme	receptor	132:139	arg1	sequence					78:85	the atypical Asn-X-Cys sequence	55:85	the atypical Asn-X-Cys sequence of recombinant human epidermal growth factor receptor	55:139	Characterization of the N-oligosaccharides attached to the atypical Asn-X-Cys sequence of recombinant human epidermal growth factor receptor.
10731668	2	32	contain	contains	370:377	arg2	chain					399:403	one oligosaccharide chain	379:403	one oligosaccharide chain attached to an atypical N-glycosylation consensus sequence, Asn(32 )-X( 33 )-Cys(34 )	379:489	We have found that the CHO sEGFR contains one oligosaccharide chain attached to an atypical N-glycosylation consensus sequence, Asn(32 )-X( 33 )-Cys(34 ).
10731668	2	32	contain	contains	370:377	arg1	sEGFR					364:368	the CHO sEGFR	356:368	the CHO sEGFR	356:368	We have found that the CHO sEGFR contains one oligosaccharide chain attached to an atypical N-glycosylation consensus sequence, Asn(32 )-X( 33 )-Cys(34 ).
10731668	8	33	with	sEGFR	1169:1173	arg1	mutation					1184:1191	the mutation	1180:1191	the mutation of Asn(32) -> Lys(32 )	1180:1214	Therefore, sEGFR with the mutation of Asn(32) -> Lys(32 )is useful for biophysical and biochemical studies, and, particularly, for X-ray crystallography.
10731668	7	34	theme	nondenaturing	1132:1144	arg1	conditions					1146:1155	nondenaturing conditions	1132:1155	nondenaturing conditions	1132:1155	An attempt to remove the oligosaccharide at Asn(32 ) enzymatically did not succeed under nondenaturing conditions.
10731668	4	35	gly	glycosylation	671:683	arg2	site					685:688	this atypical glycosylation site	657:688	this atypical glycosylation site	657:688	Deletion of this atypical glycosylation site by replacement of Asn(32 ) with lysine changed neither the expression nor function of the full length EGFR in CHO cells.
10731668	6	36	theme	CHO	913:915	arg1	sEGFR					917:921	CHO sEGFR itself	913:928	CHO sEGFR itself	913:928	Thus, CHO sEGFR itself is heterogeneous with respect to the glycosylation at Asn(32 ), which may cause problems in biophysical studies.
10731668	1	37	theme	CHO	209:211	arg1	cells					213:217	CHO cells	209:217	CHO cells	209:217	The extracellular domain of human EGF receptor (sEGFR) produced by CHO cells has been used in various biophysical studies to elucidate the molecular mechanism of EGF-induced receptor activation.
10731668	2	38	attach	attached	405:412	arg1	sequence					455:462	an atypical N-glycosylation consensus sequence	417:462	an atypical N-glycosylation consensus sequence	417:462	We have found that the CHO sEGFR contains one oligosaccharide chain attached to an atypical N-glycosylation consensus sequence, Asn(32 )-X( 33 )-Cys(34 ).
10731668	2	38	attach	attached	405:412	arg2	chain					399:403	one oligosaccharide chain	379:403	one oligosaccharide chain attached to an atypical N-glycosylation consensus sequence, Asn(32 )-X( 33 )-Cys(34 )	379:489	We have found that the CHO sEGFR contains one oligosaccharide chain attached to an atypical N-glycosylation consensus sequence, Asn(32 )-X( 33 )-Cys(34 ).
10731668	2	38	attach	attached	405:412	arg1	-Cys					481:484	Asn(32 )-X( 33 )-Cys	465:484	Asn(32 )-X( 33 )-Cys(34 )	465:489	We have found that the CHO sEGFR contains one oligosaccharide chain attached to an atypical N-glycosylation consensus sequence, Asn(32 )-X( 33 )-Cys(34 ).
10731668	2	39	theme	consensus	445:453	arg1	sequence					455:462	an atypical N-glycosylation consensus sequence	417:462	an atypical N-glycosylation consensus sequence	417:462	We have found that the CHO sEGFR contains one oligosaccharide chain attached to an atypical N-glycosylation consensus sequence, Asn(32 )-X( 33 )-Cys(34 ).
10731668	2	39	theme	consensus	445:453	arg1	-Cys					481:484	Asn(32 )-X( 33 )-Cys	465:484	Asn(32 )-X( 33 )-Cys(34 )	465:489	We have found that the CHO sEGFR contains one oligosaccharide chain attached to an atypical N-glycosylation consensus sequence, Asn(32 )-X( 33 )-Cys(34 ).
10731668	8	40	theme	biochemical	1245:1255	arg1	studies					1257:1263	biophysical and biochemical studies	1229:1263	biophysical and biochemical studies	1229:1263	Therefore, sEGFR with the mutation of Asn(32) -> Lys(32 )is useful for biophysical and biochemical studies, and, particularly, for X-ray crystallography.
10731668	4	41	dep	expression	749:758	arg1	the					745:747	the	745:747	the	745:747	Deletion of this atypical glycosylation site by replacement of Asn(32 ) with lysine changed neither the expression nor function of the full length EGFR in CHO cells.
10731668	0	42	theme	atypical	59:66	arg1	sequence					78:85	the atypical Asn-X-Cys sequence	55:85	the atypical Asn-X-Cys sequence of recombinant human epidermal growth factor receptor	55:139	Characterization of the N-oligosaccharides attached to the atypical Asn-X-Cys sequence of recombinant human epidermal growth factor receptor.
10731668	1	43	theme	EGF-induced	304:314	arg1	activation					325:334	EGF-induced receptor activation	304:334	EGF-induced receptor activation	304:334	The extracellular domain of human EGF receptor (sEGFR) produced by CHO cells has been used in various biophysical studies to elucidate the molecular mechanism of EGF-induced receptor activation.
10731668	5	44	gly	glycosylation	815:827	arg1	32					836:837	32	836:837	32	836:837	The glycosylation at Asn(32 ) in CHO sEGFR was incomplete: 20% of Asn(32 ) remained unmodified.
10731668	5	44	gly	glycosylation	815:827	arg2	32					836:837	32	836:837	32	836:837	The glycosylation at Asn(32 ) in CHO sEGFR was incomplete: 20% of Asn(32 ) remained unmodified.
10731668	5	44	gly	glycosylation	815:827	arg1	Asn					832:834	Asn	832:834	Asn(32 )	832:839	The glycosylation at Asn(32 ) in CHO sEGFR was incomplete: 20% of Asn(32 ) remained unmodified.
10731668	5	44	gly	glycosylation	815:827	arg2	Asn					832:834	Asn	832:834	Asn(32 )	832:839	The glycosylation at Asn(32 ) in CHO sEGFR was incomplete: 20% of Asn(32 ) remained unmodified.
10731668	5	44	gly	glycosylation	815:827	arg1	sEGFR					848:852	CHO sEGFR	844:852	CHO sEGFR	844:852	The glycosylation at Asn(32 ) in CHO sEGFR was incomplete: 20% of Asn(32 ) remained unmodified.
10731668	3	45	theme	forms	575:579	arg1	structure					512:520	The oligosaccharide structure	492:520	The oligosaccharide structure at Asn(32 )	492:532	The oligosaccharide structure at Asn(32 ) is a mixture of the monosialo and asialo forms of a core fucosylated biantennary complex-type oligosaccharide.
10731668	3	45	theme	forms	575:579	arg1	mixture					539:545	a mixture	537:545	a mixture of the monosialo and asialo forms of a core fucosylated biantennary complex-type oligosaccharide	537:642	The oligosaccharide structure at Asn(32 ) is a mixture of the monosialo and asialo forms of a core fucosylated biantennary complex-type oligosaccharide.
10731668	6	46	from	Asn	984:986	arg1	glycosylation					967:979	the glycosylation	963:979	the glycosylation	963:979	Thus, CHO sEGFR itself is heterogeneous with respect to the glycosylation at Asn(32 ), which may cause problems in biophysical studies.
10731668	4	47	theme	atypical	662:669	arg1	site					685:688	this atypical glycosylation site	657:688	this atypical glycosylation site	657:688	Deletion of this atypical glycosylation site by replacement of Asn(32 ) with lysine changed neither the expression nor function of the full length EGFR in CHO cells.
10731668	2	48	theme	Asn	465:467	arg1	sequence					455:462	an atypical N-glycosylation consensus sequence	417:462	an atypical N-glycosylation consensus sequence	417:462	We have found that the CHO sEGFR contains one oligosaccharide chain attached to an atypical N-glycosylation consensus sequence, Asn(32 )-X( 33 )-Cys(34 ).
10731668	2	48	theme	Asn	465:467	arg1	34					486:487	34	486:487	34	486:487	We have found that the CHO sEGFR contains one oligosaccharide chain attached to an atypical N-glycosylation consensus sequence, Asn(32 )-X( 33 )-Cys(34 ).
10731668	2	48	theme	Asn	465:467	arg1	-Cys					481:484	Asn(32 )-X( 33 )-Cys	465:484	Asn(32 )-X( 33 )-Cys(34 )	465:489	We have found that the CHO sEGFR contains one oligosaccharide chain attached to an atypical N-glycosylation consensus sequence, Asn(32 )-X( 33 )-Cys(34 ).
10731668	1	49	theme	receptor	316:323	arg1	activation					325:334	EGF-induced receptor activation	304:334	EGF-induced receptor activation	304:334	The extracellular domain of human EGF receptor (sEGFR) produced by CHO cells has been used in various biophysical studies to elucidate the molecular mechanism of EGF-induced receptor activation.
10731668	3	50	theme	biantennary	603:613	arg1	oligosaccharide					628:642	a core fucosylated biantennary complex-type oligosaccharide	584:642	a core fucosylated biantennary complex-type oligosaccharide	584:642	The oligosaccharide structure at Asn(32 ) is a mixture of the monosialo and asialo forms of a core fucosylated biantennary complex-type oligosaccharide.
10731668	3	51	theme	complex-type	615:626	arg1	oligosaccharide					628:642	a core fucosylated biantennary complex-type oligosaccharide	584:642	a core fucosylated biantennary complex-type oligosaccharide	584:642	The oligosaccharide structure at Asn(32 ) is a mixture of the monosialo and asialo forms of a core fucosylated biantennary complex-type oligosaccharide.
10731668	4	52	with	replacement	693:703	arg1	lysine					722:727	lysine	722:727	lysine	722:727	Deletion of this atypical glycosylation site by replacement of Asn(32 ) with lysine changed neither the expression nor function of the full length EGFR in CHO cells.
10731668	3	53	theme	asialo	568:573	arg1	forms					575:579	the monosialo and asialo forms	550:579	the monosialo and asialo forms of a core fucosylated biantennary complex-type oligosaccharide	550:642	The oligosaccharide structure at Asn(32 ) is a mixture of the monosialo and asialo forms of a core fucosylated biantennary complex-type oligosaccharide.
10731668	1	54	theme	activation	325:334	arg1	mechanism					291:299	the molecular mechanism	277:299	the molecular mechanism of EGF-induced receptor activation	277:334	The extracellular domain of human EGF receptor (sEGFR) produced by CHO cells has been used in various biophysical studies to elucidate the molecular mechanism of EGF-induced receptor activation.
10731668	7	55	dep	attempt	1046:1052	arg1	remove					1057:1062	remove	1057:1062	to remove the oligosaccharide at Asn(32 ) enzymatically	1054:1108	An attempt to remove the oligosaccharide at Asn(32 ) enzymatically did not succeed under nondenaturing conditions.
10731668	1	56	used	used	228:231	arg2	receptor					180:187	human EGF receptor	170:187	human EGF receptor (sEGFR) produced by CHO cells	170:217	The extracellular domain of human EGF receptor (sEGFR) produced by CHO cells has been used in various biophysical studies to elucidate the molecular mechanism of EGF-induced receptor activation.
10731668	1	56	used	used	228:231	arg2	domain					160:165	The extracellular domain	142:165	The extracellular domain of human EGF receptor (sEGFR) produced by CHO cells	142:217	The extracellular domain of human EGF receptor (sEGFR) produced by CHO cells has been used in various biophysical studies to elucidate the molecular mechanism of EGF-induced receptor activation.
10731668	3	57	theme	monosialo	554:562	arg1	forms					575:579	the monosialo and asialo forms	550:579	the monosialo and asialo forms of a core fucosylated biantennary complex-type oligosaccharide	550:642	The oligosaccharide structure at Asn(32 ) is a mixture of the monosialo and asialo forms of a core fucosylated biantennary complex-type oligosaccharide.
10731668	4	58	from	expression	749:758	arg1	cells					804:808	CHO cells	800:808	CHO cells	800:808	Deletion of this atypical glycosylation site by replacement of Asn(32 ) with lysine changed neither the expression nor function of the full length EGFR in CHO cells.
10731668	4	59	theme	site	685:688	arg1	Deletion					645:652	Deletion	645:652	Deletion of this atypical glycosylation site by replacement of Asn(32 ) with lysine	645:727	Deletion of this atypical glycosylation site by replacement of Asn(32 ) with lysine changed neither the expression nor function of the full length EGFR in CHO cells.
10731668	3	60	from	Asn	525:527	arg1	mixture					539:545	a mixture	537:545	a mixture of the monosialo and asialo forms of a core fucosylated biantennary complex-type oligosaccharide	537:642	The oligosaccharide structure at Asn(32 ) is a mixture of the monosialo and asialo forms of a core fucosylated biantennary complex-type oligosaccharide.
10731668	3	60	from	Asn	525:527	arg1	structure					512:520	The oligosaccharide structure	492:520	The oligosaccharide structure at Asn(32 )	492:532	The oligosaccharide structure at Asn(32 ) is a mixture of the monosialo and asialo forms of a core fucosylated biantennary complex-type oligosaccharide.
10731668	3	61	theme	core	586:589	arg1	oligosaccharide					628:642	a core fucosylated biantennary complex-type oligosaccharide	584:642	a core fucosylated biantennary complex-type oligosaccharide	584:642	The oligosaccharide structure at Asn(32 ) is a mixture of the monosialo and asialo forms of a core fucosylated biantennary complex-type oligosaccharide.
10731668	1	62	theme	extracellular	146:158	arg1	receptor					180:187	human EGF receptor	170:187	human EGF receptor (sEGFR) produced by CHO cells	170:217	The extracellular domain of human EGF receptor (sEGFR) produced by CHO cells has been used in various biophysical studies to elucidate the molecular mechanism of EGF-induced receptor activation.
10731668	1	62	theme	extracellular	146:158	arg1	domain					160:165	The extracellular domain	142:165	The extracellular domain of human EGF receptor (sEGFR) produced by CHO cells	142:217	The extracellular domain of human EGF receptor (sEGFR) produced by CHO cells has been used in various biophysical studies to elucidate the molecular mechanism of EGF-induced receptor activation.
10731668	3	63	theme	fucosylated	591:601	arg1	oligosaccharide					628:642	a core fucosylated biantennary complex-type oligosaccharide	584:642	a core fucosylated biantennary complex-type oligosaccharide	584:642	The oligosaccharide structure at Asn(32 ) is a mixture of the monosialo and asialo forms of a core fucosylated biantennary complex-type oligosaccharide.
10731668	8	64	theme	biophysical	1229:1239	arg1	studies					1257:1263	biophysical and biochemical studies	1229:1263	biophysical and biochemical studies	1229:1263	Therefore, sEGFR with the mutation of Asn(32) -> Lys(32 )is useful for biophysical and biochemical studies, and, particularly, for X-ray crystallography.
10731668	6	65	gly	glycosylation	967:979	arg2	32					988:989	32	988:989	32	988:989	Thus, CHO sEGFR itself is heterogeneous with respect to the glycosylation at Asn(32 ), which may cause problems in biophysical studies.
10731668	6	65	gly	glycosylation	967:979	arg1	32					988:989	32	988:989	32	988:989	Thus, CHO sEGFR itself is heterogeneous with respect to the glycosylation at Asn(32 ), which may cause problems in biophysical studies.
10731668	6	65	gly	glycosylation	967:979	arg2	Asn					984:986	Asn	984:986	Asn(32 )	984:991	Thus, CHO sEGFR itself is heterogeneous with respect to the glycosylation at Asn(32 ), which may cause problems in biophysical studies.
10731668	6	65	gly	glycosylation	967:979	arg1	Asn					984:986	Asn	984:986	Asn(32 )	984:991	Thus, CHO sEGFR itself is heterogeneous with respect to the glycosylation at Asn(32 ), which may cause problems in biophysical studies.
10731668	3	66	gly	fucosylated	591:601	arg1	oligosaccharide					628:642	a core fucosylated biantennary complex-type oligosaccharide	584:642	a core fucosylated biantennary complex-type oligosaccharide	584:642	The oligosaccharide structure at Asn(32 ) is a mixture of the monosialo and asialo forms of a core fucosylated biantennary complex-type oligosaccharide.
10731668	0	67	theme	Asn-X-Cys	68:76	arg1	sequence					78:85	the atypical Asn-X-Cys sequence	55:85	the atypical Asn-X-Cys sequence of recombinant human epidermal growth factor receptor	55:139	Characterization of the N-oligosaccharides attached to the atypical Asn-X-Cys sequence of recombinant human epidermal growth factor receptor.
10731668	8	68	theme	X-ray	1289:1293	arg1	crystallography					1295:1309	X-ray crystallography	1289:1309	X-ray crystallography	1289:1309	Therefore, sEGFR with the mutation of Asn(32) -> Lys(32 )is useful for biophysical and biochemical studies, and, particularly, for X-ray crystallography.
10731668	2	69	theme	CHO	360:362	arg1	sEGFR					364:368	the CHO sEGFR	356:368	the CHO sEGFR	356:368	We have found that the CHO sEGFR contains one oligosaccharide chain attached to an atypical N-glycosylation consensus sequence, Asn(32 )-X( 33 )-Cys(34 ).
3934016	5	0	theme	rat	859:861	arg1	angiotensinogen					863:877	rat angiotensinogen	859:877	rat angiotensinogen	859:877	For rat angiotensinogen, only 2 of 3 potential sites of N-glycosylation were utilized; in contrast, all 4 potential sites of N-glycosylation of human angiotensinogen were utilized.
3934016	1	1	theme	microsomal	158:167	arg1	membranes					169:177	microsomal membranes	158:177	microsomal membranes	158:177	We have studied the processing of rat and human angiotensinogen precursors by microsomal membranes as a means of determining the number of asparagine-linked oligosaccharide units per angiotensinogen molecule, and thus the utilization of potential sites of N-glycosylation.
3934016	1	2	theme	angiotensinogen	263:277	arg1	molecule					279:286	angiotensinogen molecule	263:286	angiotensinogen molecule	263:286	We have studied the processing of rat and human angiotensinogen precursors by microsomal membranes as a means of determining the number of asparagine-linked oligosaccharide units per angiotensinogen molecule, and thus the utilization of potential sites of N-glycosylation.
3934016	3	3	theme	35S-methionine-labeled	589:610	arg1	forms					619:623	glycosylated and nonglycosylated 35S-methionine-labeled mature forms	556:623	glycosylated and nonglycosylated 35S-methionine-labeled mature forms of angiotensinogen secreted by hepatoma cells	556:669	35S-Methionine-labeled precursor and processed forms of angiotensinogen were compared with glycosylated and nonglycosylated 35S-methionine-labeled mature forms of angiotensinogen secreted by hepatoma cells, using immunoprecipitation, sodium dodecyl sulfate-polyacrylamide gel electrophoresis and autoradiography.
3934016	3	4	theme	angiotensinogen	628:642	arg1	forms					619:623	glycosylated and nonglycosylated 35S-methionine-labeled mature forms	556:623	glycosylated and nonglycosylated 35S-methionine-labeled mature forms of angiotensinogen secreted by hepatoma cells	556:669	35S-Methionine-labeled precursor and processed forms of angiotensinogen were compared with glycosylated and nonglycosylated 35S-methionine-labeled mature forms of angiotensinogen secreted by hepatoma cells, using immunoprecipitation, sodium dodecyl sulfate-polyacrylamide gel electrophoresis and autoradiography.
3934016	3	5	theme	hepatoma	656:663	arg1	cells					665:669	hepatoma cells	656:669	hepatoma cells	656:669	35S-Methionine-labeled precursor and processed forms of angiotensinogen were compared with glycosylated and nonglycosylated 35S-methionine-labeled mature forms of angiotensinogen secreted by hepatoma cells, using immunoprecipitation, sodium dodecyl sulfate-polyacrylamide gel electrophoresis and autoradiography.
3934016	5	6	theme	N-glycosylation	911:925	arg1	sites					902:906	only 2 of 3 potential sites	880:906	only 2 of 3 potential sites of N-glycosylation	880:925	For rat angiotensinogen, only 2 of 3 potential sites of N-glycosylation were utilized; in contrast, all 4 potential sites of N-glycosylation of human angiotensinogen were utilized.
3934016	5	6	theme	N-glycosylation	911:925	arg1	N-glycosylation					911:925	N-glycosylation	911:925	N-glycosylation	911:925	For rat angiotensinogen, only 2 of 3 potential sites of N-glycosylation were utilized; in contrast, all 4 potential sites of N-glycosylation of human angiotensinogen were utilized.
3934016	3	7	theme	angiotensinogen	521:535	arg1	precursor					488:496	35S-Methionine-labeled precursor	465:496	35S-Methionine-labeled precursor	465:496	35S-Methionine-labeled precursor and processed forms of angiotensinogen were compared with glycosylated and nonglycosylated 35S-methionine-labeled mature forms of angiotensinogen secreted by hepatoma cells, using immunoprecipitation, sodium dodecyl sulfate-polyacrylamide gel electrophoresis and autoradiography.
3934016	3	7	theme	angiotensinogen	521:535	arg1	forms					512:516	processed forms	502:516	processed forms of angiotensinogen	502:535	35S-Methionine-labeled precursor and processed forms of angiotensinogen were compared with glycosylated and nonglycosylated 35S-methionine-labeled mature forms of angiotensinogen secreted by hepatoma cells, using immunoprecipitation, sodium dodecyl sulfate-polyacrylamide gel electrophoresis and autoradiography.
3934016	3	8	gly	nonglycosylated	573:587	arg1	angiotensinogen					628:642	angiotensinogen	628:642	angiotensinogen secreted by hepatoma cells	628:669	35S-Methionine-labeled precursor and processed forms of angiotensinogen were compared with glycosylated and nonglycosylated 35S-methionine-labeled mature forms of angiotensinogen secreted by hepatoma cells, using immunoprecipitation, sodium dodecyl sulfate-polyacrylamide gel electrophoresis and autoradiography.
3934016	3	8	gly	nonglycosylated	573:587	arg1	forms					619:623	glycosylated and nonglycosylated 35S-methionine-labeled mature forms	556:623	glycosylated and nonglycosylated 35S-methionine-labeled mature forms of angiotensinogen secreted by hepatoma cells	556:669	35S-Methionine-labeled precursor and processed forms of angiotensinogen were compared with glycosylated and nonglycosylated 35S-methionine-labeled mature forms of angiotensinogen secreted by hepatoma cells, using immunoprecipitation, sodium dodecyl sulfate-polyacrylamide gel electrophoresis and autoradiography.
3934016	1	9	gly	N-glycosylation	336:350	arg2	N-glycosylation					336:350	N-glycosylation	336:350	N-glycosylation	336:350	We have studied the processing of rat and human angiotensinogen precursors by microsomal membranes as a means of determining the number of asparagine-linked oligosaccharide units per angiotensinogen molecule, and thus the utilization of potential sites of N-glycosylation.
3934016	1	9	gly	N-glycosylation	336:350	arg2	sites					327:331	potential sites	317:331	potential sites of N-glycosylation	317:350	We have studied the processing of rat and human angiotensinogen precursors by microsomal membranes as a means of determining the number of asparagine-linked oligosaccharide units per angiotensinogen molecule, and thus the utilization of potential sites of N-glycosylation.
3934016	4	10	theme	secreted	797:804	arg1	angiotensinogen					806:820	secreted angiotensinogen	797:820	secreted angiotensinogen	797:820	N-Glycosylation of secreted angiotensinogen was inhibited using tunicamycin.
3934016	5	11	theme	human	999:1003	arg1	angiotensinogen					1005:1019	human angiotensinogen	999:1019	human angiotensinogen	999:1019	For rat angiotensinogen, only 2 of 3 potential sites of N-glycosylation were utilized; in contrast, all 4 potential sites of N-glycosylation of human angiotensinogen were utilized.
3934016	3	12	theme	mature	612:617	arg1	forms					619:623	glycosylated and nonglycosylated 35S-methionine-labeled mature forms	556:623	glycosylated and nonglycosylated 35S-methionine-labeled mature forms of angiotensinogen secreted by hepatoma cells	556:669	35S-Methionine-labeled precursor and processed forms of angiotensinogen were compared with glycosylated and nonglycosylated 35S-methionine-labeled mature forms of angiotensinogen secreted by hepatoma cells, using immunoprecipitation, sodium dodecyl sulfate-polyacrylamide gel electrophoresis and autoradiography.
3934016	5	13	gly	N-glycosylation	980:994	arg2	N-glycosylation					980:994	N-glycosylation	980:994	N-glycosylation of human angiotensinogen	980:1019	For rat angiotensinogen, only 2 of 3 potential sites of N-glycosylation were utilized; in contrast, all 4 potential sites of N-glycosylation of human angiotensinogen were utilized.
3934016	5	13	gly	N-glycosylation	980:994	arg1	angiotensinogen					1005:1019	human angiotensinogen	999:1019	human angiotensinogen	999:1019	For rat angiotensinogen, only 2 of 3 potential sites of N-glycosylation were utilized; in contrast, all 4 potential sites of N-glycosylation of human angiotensinogen were utilized.
3934016	5	13	gly	N-glycosylation	980:994	arg2	sites					971:975	all 4 potential sites	955:975	all 4 potential sites of N-glycosylation of human angiotensinogen	955:1019	For rat angiotensinogen, only 2 of 3 potential sites of N-glycosylation were utilized; in contrast, all 4 potential sites of N-glycosylation of human angiotensinogen were utilized.
3934016	3	14	gly	glycosylated	556:567	arg1	angiotensinogen					628:642	angiotensinogen	628:642	angiotensinogen secreted by hepatoma cells	628:669	35S-Methionine-labeled precursor and processed forms of angiotensinogen were compared with glycosylated and nonglycosylated 35S-methionine-labeled mature forms of angiotensinogen secreted by hepatoma cells, using immunoprecipitation, sodium dodecyl sulfate-polyacrylamide gel electrophoresis and autoradiography.
3934016	3	14	gly	glycosylated	556:567	arg1	forms					619:623	glycosylated and nonglycosylated 35S-methionine-labeled mature forms	556:623	glycosylated and nonglycosylated 35S-methionine-labeled mature forms of angiotensinogen secreted by hepatoma cells	556:669	35S-Methionine-labeled precursor and processed forms of angiotensinogen were compared with glycosylated and nonglycosylated 35S-methionine-labeled mature forms of angiotensinogen secreted by hepatoma cells, using immunoprecipitation, sodium dodecyl sulfate-polyacrylamide gel electrophoresis and autoradiography.
3934016	5	15	theme	angiotensinogen	1005:1019	arg1	N-glycosylation					980:994	N-glycosylation	980:994	N-glycosylation of human angiotensinogen	980:1019	For rat angiotensinogen, only 2 of 3 potential sites of N-glycosylation were utilized; in contrast, all 4 potential sites of N-glycosylation of human angiotensinogen were utilized.
3934016	4	16	gly	N-Glycosylation	778:792	arg1	angiotensinogen					806:820	secreted angiotensinogen	797:820	secreted angiotensinogen	797:820	N-Glycosylation of secreted angiotensinogen was inhibited using tunicamycin.
3934016	3	17	theme	35S-Methionine-labeled	465:486	arg1	precursor					488:496	35S-Methionine-labeled precursor	465:496	35S-Methionine-labeled precursor	465:496	35S-Methionine-labeled precursor and processed forms of angiotensinogen were compared with glycosylated and nonglycosylated 35S-methionine-labeled mature forms of angiotensinogen secreted by hepatoma cells, using immunoprecipitation, sodium dodecyl sulfate-polyacrylamide gel electrophoresis and autoradiography.
3934016	1	18	link	asparagine-linked	219:235	arg1	units					253:257	asparagine-linked oligosaccharide units	219:257	asparagine-linked oligosaccharide units per angiotensinogen molecule, and thus the utilization of potential sites of N-glycosylation	219:350	We have studied the processing of rat and human angiotensinogen precursors by microsomal membranes as a means of determining the number of asparagine-linked oligosaccharide units per angiotensinogen molecule, and thus the utilization of potential sites of N-glycosylation.
3934016	5	19	theme	potential	961:969	arg1	N-glycosylation					980:994	N-glycosylation	980:994	N-glycosylation of human angiotensinogen	980:1019	For rat angiotensinogen, only 2 of 3 potential sites of N-glycosylation were utilized; in contrast, all 4 potential sites of N-glycosylation of human angiotensinogen were utilized.
3934016	5	19	theme	potential	961:969	arg1	sites					971:975	all 4 potential sites	955:975	all 4 potential sites of N-glycosylation of human angiotensinogen	955:1019	For rat angiotensinogen, only 2 of 3 potential sites of N-glycosylation were utilized; in contrast, all 4 potential sites of N-glycosylation of human angiotensinogen were utilized.
3934016	0	20	theme	rat	14:16	arg1	precursors					44:53	rat and human angiotensinogen precursors	14:53	rat and human angiotensinogen precursors	14:53	Processing of rat and human angiotensinogen precursors by microsomal membranes.
3934016	2	21	theme	angiotensinogen	386:400	arg1	forms					377:381	Glycosylated, processed forms	353:381	Glycosylated, processed forms of angiotensinogen	353:400	Glycosylated, processed forms of angiotensinogen were isolated by chromatography on lentil lectin-Sepharose 4B.
3934016	2	22	dep	Glycosylated	353:364	arg1	processed					367:375	processed	367:375	processed	367:375	Glycosylated, processed forms of angiotensinogen were isolated by chromatography on lentil lectin-Sepharose 4B.
3934016	2	23	theme	lectin-Sepharose	444:459	arg1	4B					461:462	lentil lectin-Sepharose 4B	437:462	lentil lectin-Sepharose 4B	437:462	Glycosylated, processed forms of angiotensinogen were isolated by chromatography on lentil lectin-Sepharose 4B.
3934016	0	24	theme	angiotensinogen	28:42	arg1	precursors					44:53	rat and human angiotensinogen precursors	14:53	rat and human angiotensinogen precursors	14:53	Processing of rat and human angiotensinogen precursors by microsomal membranes.
3934016	2	25	theme	Glycosylated	353:364	arg1	forms					377:381	Glycosylated, processed forms	353:381	Glycosylated, processed forms of angiotensinogen	353:400	Glycosylated, processed forms of angiotensinogen were isolated by chromatography on lentil lectin-Sepharose 4B.
3934016	5	26	used	utilized	932:939	arg2	N-glycosylation					911:925	N-glycosylation	911:925	N-glycosylation	911:925	For rat angiotensinogen, only 2 of 3 potential sites of N-glycosylation were utilized; in contrast, all 4 potential sites of N-glycosylation of human angiotensinogen were utilized.
3934016	5	26	used	utilized	932:939	arg2	sites					902:906	only 2 of 3 potential sites	880:906	only 2 of 3 potential sites of N-glycosylation	880:925	For rat angiotensinogen, only 2 of 3 potential sites of N-glycosylation were utilized; in contrast, all 4 potential sites of N-glycosylation of human angiotensinogen were utilized.
3934016	3	27	theme	processed	502:510	arg1	forms					512:516	processed forms	502:516	processed forms of angiotensinogen	502:535	35S-Methionine-labeled precursor and processed forms of angiotensinogen were compared with glycosylated and nonglycosylated 35S-methionine-labeled mature forms of angiotensinogen secreted by hepatoma cells, using immunoprecipitation, sodium dodecyl sulfate-polyacrylamide gel electrophoresis and autoradiography.
3934016	4	28	theme	angiotensinogen	806:820	arg1	N-Glycosylation					778:792	N-Glycosylation	778:792	N-Glycosylation of secreted angiotensinogen	778:820	N-Glycosylation of secreted angiotensinogen was inhibited using tunicamycin.
3934016	2	29	theme	lentil	437:442	arg1	4B					461:462	lentil lectin-Sepharose 4B	437:462	lentil lectin-Sepharose 4B	437:462	Glycosylated, processed forms of angiotensinogen were isolated by chromatography on lentil lectin-Sepharose 4B.
3934016	0	30	theme	human	22:26	arg1	precursors					44:53	rat and human angiotensinogen precursors	14:53	rat and human angiotensinogen precursors	14:53	Processing of rat and human angiotensinogen precursors by microsomal membranes.
3934016	6	31	dep	neither	1040:1046	arg1	rat					1048:1050	rat	1048:1050	rat	1048:1050	For neither rat or human angiotensinogen precursor was there any evidence for a prosequence.
3934016	5	32	theme	N-glycosylation	980:994	arg1	N-glycosylation					980:994	N-glycosylation	980:994	N-glycosylation of human angiotensinogen	980:1019	For rat angiotensinogen, only 2 of 3 potential sites of N-glycosylation were utilized; in contrast, all 4 potential sites of N-glycosylation of human angiotensinogen were utilized.
3934016	5	32	theme	N-glycosylation	980:994	arg1	sites					971:975	all 4 potential sites	955:975	all 4 potential sites of N-glycosylation of human angiotensinogen	955:1019	For rat angiotensinogen, only 2 of 3 potential sites of N-glycosylation were utilized; in contrast, all 4 potential sites of N-glycosylation of human angiotensinogen were utilized.
3934016	1	33	theme	potential	317:325	arg1	N-glycosylation					336:350	N-glycosylation	336:350	N-glycosylation	336:350	We have studied the processing of rat and human angiotensinogen precursors by microsomal membranes as a means of determining the number of asparagine-linked oligosaccharide units per angiotensinogen molecule, and thus the utilization of potential sites of N-glycosylation.
3934016	1	33	theme	potential	317:325	arg1	sites					327:331	potential sites	317:331	potential sites of N-glycosylation	317:350	We have studied the processing of rat and human angiotensinogen precursors by microsomal membranes as a means of determining the number of asparagine-linked oligosaccharide units per angiotensinogen molecule, and thus the utilization of potential sites of N-glycosylation.
3934016	6	34	dep	precursor	1077:1085	arg1	neither					1040:1046	neither	1040:1046	neither	1040:1046	For neither rat or human angiotensinogen precursor was there any evidence for a prosequence.
3934016	6	34	dep	precursor	1077:1085	arg1	human					1055:1059	human	1055:1059	human	1055:1059	For neither rat or human angiotensinogen precursor was there any evidence for a prosequence.
3934016	0	35	theme	precursors	44:53	arg1	Processing					0:9	Processing	0:9	Processing of rat and human angiotensinogen precursors by microsomal membranes.	0:78	Processing of rat and human angiotensinogen precursors by microsomal membranes.
3934016	1	36	theme	sites	327:331	arg1	utilization					302:312	the utilization	298:312	the utilization of potential sites of N-glycosylation	298:350	We have studied the processing of rat and human angiotensinogen precursors by microsomal membranes as a means of determining the number of asparagine-linked oligosaccharide units per angiotensinogen molecule, and thus the utilization of potential sites of N-glycosylation.
3934016	6	37	theme	angiotensinogen	1061:1075	arg1	precursor					1077:1085	neither rat or human angiotensinogen precursor	1040:1085	neither rat or human angiotensinogen precursor	1040:1085	For neither rat or human angiotensinogen precursor was there any evidence for a prosequence.
3934016	5	38	used	utilized	1026:1033	arg2	N-glycosylation					980:994	N-glycosylation	980:994	N-glycosylation of human angiotensinogen	980:1019	For rat angiotensinogen, only 2 of 3 potential sites of N-glycosylation were utilized; in contrast, all 4 potential sites of N-glycosylation of human angiotensinogen were utilized.
3934016	5	38	used	utilized	1026:1033	arg2	sites					971:975	all 4 potential sites	955:975	all 4 potential sites of N-glycosylation of human angiotensinogen	955:1019	For rat angiotensinogen, only 2 of 3 potential sites of N-glycosylation were utilized; in contrast, all 4 potential sites of N-glycosylation of human angiotensinogen were utilized.
3934016	2	39	from	chromatography	419:432	arg1	4B					461:462	lentil lectin-Sepharose 4B	437:462	lentil lectin-Sepharose 4B	437:462	Glycosylated, processed forms of angiotensinogen were isolated by chromatography on lentil lectin-Sepharose 4B.
3934016	1	40	theme	rat	114:116	arg1	precursors					144:153	rat and human angiotensinogen precursors	114:153	rat and human angiotensinogen precursors	114:153	We have studied the processing of rat and human angiotensinogen precursors by microsomal membranes as a means of determining the number of asparagine-linked oligosaccharide units per angiotensinogen molecule, and thus the utilization of potential sites of N-glycosylation.
3934016	3	41	theme	nonglycosylated	573:587	arg1	forms					619:623	glycosylated and nonglycosylated 35S-methionine-labeled mature forms	556:623	glycosylated and nonglycosylated 35S-methionine-labeled mature forms of angiotensinogen secreted by hepatoma cells	556:669	35S-Methionine-labeled precursor and processed forms of angiotensinogen were compared with glycosylated and nonglycosylated 35S-methionine-labeled mature forms of angiotensinogen secreted by hepatoma cells, using immunoprecipitation, sodium dodecyl sulfate-polyacrylamide gel electrophoresis and autoradiography.
3934016	3	42	theme	gel	737:739	arg1	immunoprecipitation					678:696	immunoprecipitation	678:696	immunoprecipitation	678:696	35S-Methionine-labeled precursor and processed forms of angiotensinogen were compared with glycosylated and nonglycosylated 35S-methionine-labeled mature forms of angiotensinogen secreted by hepatoma cells, using immunoprecipitation, sodium dodecyl sulfate-polyacrylamide gel electrophoresis and autoradiography.
3934016	3	42	theme	gel	737:739	arg1	electrophoresis					741:755	sodium dodecyl sulfate-polyacrylamide gel electrophoresis	699:755	sodium dodecyl sulfate-polyacrylamide gel electrophoresis	699:755	35S-Methionine-labeled precursor and processed forms of angiotensinogen were compared with glycosylated and nonglycosylated 35S-methionine-labeled mature forms of angiotensinogen secreted by hepatoma cells, using immunoprecipitation, sodium dodecyl sulfate-polyacrylamide gel electrophoresis and autoradiography.
3934016	5	43	gly	N-glycosylation	911:925	arg2	N-glycosylation					911:925	N-glycosylation	911:925	N-glycosylation	911:925	For rat angiotensinogen, only 2 of 3 potential sites of N-glycosylation were utilized; in contrast, all 4 potential sites of N-glycosylation of human angiotensinogen were utilized.
3934016	5	43	gly	N-glycosylation	911:925	arg2	sites					902:906	only 2 of 3 potential sites	880:906	only 2 of 3 potential sites of N-glycosylation	880:925	For rat angiotensinogen, only 2 of 3 potential sites of N-glycosylation were utilized; in contrast, all 4 potential sites of N-glycosylation of human angiotensinogen were utilized.
3934016	1	44	theme	human	122:126	arg1	precursors					144:153	rat and human angiotensinogen precursors	114:153	rat and human angiotensinogen precursors	114:153	We have studied the processing of rat and human angiotensinogen precursors by microsomal membranes as a means of determining the number of asparagine-linked oligosaccharide units per angiotensinogen molecule, and thus the utilization of potential sites of N-glycosylation.
3934016	1	45	theme	asparagine-linked	219:235	arg1	units					253:257	asparagine-linked oligosaccharide units	219:257	asparagine-linked oligosaccharide units per angiotensinogen molecule, and thus the utilization of potential sites of N-glycosylation	219:350	We have studied the processing of rat and human angiotensinogen precursors by microsomal membranes as a means of determining the number of asparagine-linked oligosaccharide units per angiotensinogen molecule, and thus the utilization of potential sites of N-glycosylation.
3934016	5	46	theme	potential	892:900	arg1	sites					902:906	only 2 of 3 potential sites	880:906	only 2 of 3 potential sites of N-glycosylation	880:925	For rat angiotensinogen, only 2 of 3 potential sites of N-glycosylation were utilized; in contrast, all 4 potential sites of N-glycosylation of human angiotensinogen were utilized.
3934016	5	46	theme	potential	892:900	arg1	N-glycosylation					911:925	N-glycosylation	911:925	N-glycosylation	911:925	For rat angiotensinogen, only 2 of 3 potential sites of N-glycosylation were utilized; in contrast, all 4 potential sites of N-glycosylation of human angiotensinogen were utilized.
3934016	1	47	theme	angiotensinogen	128:142	arg1	precursors					144:153	rat and human angiotensinogen precursors	114:153	rat and human angiotensinogen precursors	114:153	We have studied the processing of rat and human angiotensinogen precursors by microsomal membranes as a means of determining the number of asparagine-linked oligosaccharide units per angiotensinogen molecule, and thus the utilization of potential sites of N-glycosylation.
3934016	1	48	theme	oligosaccharide	237:251	arg1	units					253:257	asparagine-linked oligosaccharide units	219:257	asparagine-linked oligosaccharide units per angiotensinogen molecule, and thus the utilization of potential sites of N-glycosylation	219:350	We have studied the processing of rat and human angiotensinogen precursors by microsomal membranes as a means of determining the number of asparagine-linked oligosaccharide units per angiotensinogen molecule, and thus the utilization of potential sites of N-glycosylation.
3934016	0	49	theme	microsomal	58:67	arg1	membranes					69:77	microsomal membranes	58:77	microsomal membranes	58:77	Processing of rat and human angiotensinogen precursors by microsomal membranes.
3934016	1	50	theme	N-glycosylation	336:350	arg1	N-glycosylation					336:350	N-glycosylation	336:350	N-glycosylation	336:350	We have studied the processing of rat and human angiotensinogen precursors by microsomal membranes as a means of determining the number of asparagine-linked oligosaccharide units per angiotensinogen molecule, and thus the utilization of potential sites of N-glycosylation.
3934016	1	50	theme	N-glycosylation	336:350	arg1	sites					327:331	potential sites	317:331	potential sites of N-glycosylation	317:350	We have studied the processing of rat and human angiotensinogen precursors by microsomal membranes as a means of determining the number of asparagine-linked oligosaccharide units per angiotensinogen molecule, and thus the utilization of potential sites of N-glycosylation.
3934016	3	51	theme	sulfate-polyacrylamide	714:735	arg1	immunoprecipitation					678:696	immunoprecipitation	678:696	immunoprecipitation	678:696	35S-Methionine-labeled precursor and processed forms of angiotensinogen were compared with glycosylated and nonglycosylated 35S-methionine-labeled mature forms of angiotensinogen secreted by hepatoma cells, using immunoprecipitation, sodium dodecyl sulfate-polyacrylamide gel electrophoresis and autoradiography.
3934016	3	51	theme	sulfate-polyacrylamide	714:735	arg1	electrophoresis					741:755	sodium dodecyl sulfate-polyacrylamide gel electrophoresis	699:755	sodium dodecyl sulfate-polyacrylamide gel electrophoresis	699:755	35S-Methionine-labeled precursor and processed forms of angiotensinogen were compared with glycosylated and nonglycosylated 35S-methionine-labeled mature forms of angiotensinogen secreted by hepatoma cells, using immunoprecipitation, sodium dodecyl sulfate-polyacrylamide gel electrophoresis and autoradiography.
3934016	1	52	theme	precursors	144:153	arg1	means					184:188	a means	182:188	a means of determining the number of asparagine-linked oligosaccharide units per angiotensinogen molecule, and thus the utilization of potential sites of N-glycosylation	182:350	We have studied the processing of rat and human angiotensinogen precursors by microsomal membranes as a means of determining the number of asparagine-linked oligosaccharide units per angiotensinogen molecule, and thus the utilization of potential sites of N-glycosylation.
3934016	1	52	theme	precursors	144:153	arg1	processing					100:109	the processing	96:109	the processing of rat and human angiotensinogen precursors by microsomal membranes	96:177	We have studied the processing of rat and human angiotensinogen precursors by microsomal membranes as a means of determining the number of asparagine-linked oligosaccharide units per angiotensinogen molecule, and thus the utilization of potential sites of N-glycosylation.
3934016	3	53	theme	glycosylated	556:567	arg1	forms					619:623	glycosylated and nonglycosylated 35S-methionine-labeled mature forms	556:623	glycosylated and nonglycosylated 35S-methionine-labeled mature forms of angiotensinogen secreted by hepatoma cells	556:669	35S-Methionine-labeled precursor and processed forms of angiotensinogen were compared with glycosylated and nonglycosylated 35S-methionine-labeled mature forms of angiotensinogen secreted by hepatoma cells, using immunoprecipitation, sodium dodecyl sulfate-polyacrylamide gel electrophoresis and autoradiography.
3934016	1	54	theme	units	253:257	arg1	number					209:214	the number	205:214	the number of asparagine-linked oligosaccharide units per angiotensinogen molecule, and thus the utilization of potential sites of N-glycosylation	205:350	We have studied the processing of rat and human angiotensinogen precursors by microsomal membranes as a means of determining the number of asparagine-linked oligosaccharide units per angiotensinogen molecule, and thus the utilization of potential sites of N-glycosylation.
16239734	7	0	theme	integrin	914:921	arg1	binding					923:929	integrin binding	914:929	integrin binding	914:929	An RGD motif is displayed on the surface, where it could be involved in integrin binding and possibly play a role in the shedding of SSAO from the membrane.
16239734	1	1	theme	amine	183:187	arg1	CuAOs					199:203	CuAOs	199:203	CuAOs	199:203	Semicarbazide-sensitive amine oxidase (SSAO) belongs to a ubiquitous family of copper-containing amine oxidases (CuAOs).
16239734	1	1	theme	amine	183:187	arg1	oxidases					189:196	copper-containing amine oxidases	165:196	copper-containing amine oxidases (CuAOs)	165:204	Semicarbazide-sensitive amine oxidase (SSAO) belongs to a ubiquitous family of copper-containing amine oxidases (CuAOs).
16239734	5	2	located	present	614:620	arg2	present					614:620	present	614:620	present	614:620	The topaquinone (TPQ) cofactor and a copper ion characteristic of CuAOs are present in the active site, with the TPQ in the active ;off-copper' conformation.
16239734	5	2	located	present	614:620	arg2	TPQ					555:557	TPQ	555:557	TPQ	555:557	The topaquinone (TPQ) cofactor and a copper ion characteristic of CuAOs are present in the active site, with the TPQ in the active ;off-copper' conformation.
16239734	5	2	located	present	614:620	arg2	topaquinone					542:552	The topaquinone	538:552	The topaquinone (TPQ) cofactor	538:567	The topaquinone (TPQ) cofactor and a copper ion characteristic of CuAOs are present in the active site, with the TPQ in the active ;off-copper' conformation.
16239734	5	2	located	present	614:620	arg2	characteristic					586:599	a copper ion characteristic	573:599	a copper ion characteristic of CuAOs	573:608	The topaquinone (TPQ) cofactor and a copper ion characteristic of CuAOs are present in the active site, with the TPQ in the active ;off-copper' conformation.
16239734	5	2	located	present	614:620	arg1	site					636:639	the active site	625:639	the active site	625:639	The topaquinone (TPQ) cofactor and a copper ion characteristic of CuAOs are present in the active site, with the TPQ in the active ;off-copper' conformation.
16239734	2	3	theme	leukocyte-extravasation	338:360	arg1	process					362:368	the leukocyte-extravasation process	334:368	the leukocyte-extravasation process	334:368	SSAO is also known as vascular adhesion protein-1 (VAP-1) and has been identified as one of the adhesion molecules involved in the leukocyte-extravasation process.
16239734	4	4	theme	family	530:535	arg1	typical					510:516	typical	510:516	typical	510:516	As expected, SSAO is a homodimer with a fold typical of the CuAO family.
16239734	10	5	theme	A	1310:1310	arg1	resolution					1312:1321	2.9 A resolution	1306:1321	2.9 A resolution	1306:1321	The structure of an adduct of SSAO and the irreversible inhibitor 2-hydrazinopyridine has been solved and refined to 2.9 A resolution.
16239734	5	6	theme	CuAOs	604:608	arg1	TPQ					555:557	TPQ	555:557	TPQ	555:557	The topaquinone (TPQ) cofactor and a copper ion characteristic of CuAOs are present in the active site, with the TPQ in the active ;off-copper' conformation.
16239734	5	6	theme	CuAOs	604:608	arg1	present					614:620	present	614:620	present	614:620	The topaquinone (TPQ) cofactor and a copper ion characteristic of CuAOs are present in the active site, with the TPQ in the active ;off-copper' conformation.
16239734	5	6	theme	CuAOs	604:608	arg1	topaquinone					542:552	The topaquinone	538:552	The topaquinone (TPQ) cofactor	538:567	The topaquinone (TPQ) cofactor and a copper ion characteristic of CuAOs are present in the active site, with the TPQ in the active ;off-copper' conformation.
16239734	5	6	theme	CuAOs	604:608	arg1	characteristic					586:599	a copper ion characteristic	573:599	a copper ion characteristic of CuAOs	573:608	The topaquinone (TPQ) cofactor and a copper ion characteristic of CuAOs are present in the active site, with the TPQ in the active ;off-copper' conformation.
16239734	6	7	theme	leucine	725:731	arg1	gate					806:809	a gate	804:809	a gate controlling its accessibility	804:839	The structure reveals that a leucine residue (Leu469) located adjacent to the active site could function as a gate controlling its accessibility.
16239734	6	7	theme	leucine	725:731	arg1	residue					733:739	a leucine residue	723:739	a leucine residue (Leu469) located adjacent to the active site	723:784	The structure reveals that a leucine residue (Leu469) located adjacent to the active site could function as a gate controlling its accessibility.
16239734	4	8	with	homodimer	488:496	arg1	fold					505:508	a fold	503:508	a fold typical of the CuAO family	503:535	As expected, SSAO is a homodimer with a fold typical of the CuAO family.
16239734	5	9	from	site	636:639	arg1	present					614:620	present	614:620	present	614:620	The topaquinone (TPQ) cofactor and a copper ion characteristic of CuAOs are present in the active site, with the TPQ in the active ;off-copper' conformation.
16239734	5	9	from	site	636:639	arg1	topaquinone					542:552	The topaquinone	538:552	The topaquinone (TPQ) cofactor	538:567	The topaquinone (TPQ) cofactor and a copper ion characteristic of CuAOs are present in the active site, with the TPQ in the active ;off-copper' conformation.
16239734	5	9	from	site	636:639	arg1	characteristic					586:599	a copper ion characteristic	573:599	a copper ion characteristic of CuAOs	573:608	The topaquinone (TPQ) cofactor and a copper ion characteristic of CuAOs are present in the active site, with the TPQ in the active ;off-copper' conformation.
16239734	8	10	located	observed	1025:1032	arg1	sites					1075:1079	five of six potential N-glycosylation sites	1037:1079	five of six potential N-glycosylation sites	1037:1079	Carbohydrate moieties are observed at five of six potential N-glycosylation sites.
16239734	8	10	located	observed	1025:1032	arg2	moieties					1012:1019	Carbohydrate moieties	999:1019	Carbohydrate moieties	999:1019	Carbohydrate moieties are observed at five of six potential N-glycosylation sites.
16239734	8	11	gly	N-glycosylation	1059:1073	arg2	six					1045:1047	six	1045:1047	six	1045:1047	Carbohydrate moieties are observed at five of six potential N-glycosylation sites.
16239734	8	11	gly	N-glycosylation	1059:1073	arg2	sites					1075:1079	five of six potential N-glycosylation sites	1037:1079	five of six potential N-glycosylation sites	1037:1079	Carbohydrate moieties are observed at five of six potential N-glycosylation sites.
16239734	1	12	theme	Semicarbazide-sensitive	86:108	arg1	SSAO					125:128	SSAO	125:128	SSAO	125:128	Semicarbazide-sensitive amine oxidase (SSAO) belongs to a ubiquitous family of copper-containing amine oxidases (CuAOs).
16239734	1	12	theme	Semicarbazide-sensitive	86:108	arg1	oxidase					116:122	Semicarbazide-sensitive amine oxidase	86:122	Semicarbazide-sensitive amine oxidase (SSAO)	86:129	Semicarbazide-sensitive amine oxidase (SSAO) belongs to a ubiquitous family of copper-containing amine oxidases (CuAOs).
16239734	9	13	attach	attached	1096:1103	arg2	Carbohydrates					1082:1094	Carbohydrates	1082:1094	Carbohydrates attached to Asn232	1082:1113	Carbohydrates attached to Asn232 flank the active-site entrance and might influence substrate specificity.
16239734	9	13	attach	attached	1096:1103	arg1	Asn232					1108:1113	Asn232	1108:1113	Asn232	1108:1113	Carbohydrates attached to Asn232 flank the active-site entrance and might influence substrate specificity.
16239734	5	14	dep	topaquinone	542:552	arg1	cofactor					560:567	cofactor	560:567	The topaquinone (TPQ) cofactor	538:567	The topaquinone (TPQ) cofactor and a copper ion characteristic of CuAOs are present in the active site, with the TPQ in the active ;off-copper' conformation.
16239734	1	15	theme	amine	110:114	arg1	SSAO					125:128	SSAO	125:128	SSAO	125:128	Semicarbazide-sensitive amine oxidase (SSAO) belongs to a ubiquitous family of copper-containing amine oxidases (CuAOs).
16239734	1	15	theme	amine	110:114	arg1	oxidase					116:122	Semicarbazide-sensitive amine oxidase	86:122	Semicarbazide-sensitive amine oxidase (SSAO)	86:129	Semicarbazide-sensitive amine oxidase (SSAO) belongs to a ubiquitous family of copper-containing amine oxidases (CuAOs).
16239734	5	16	with	present	614:620	arg1	TPQ					651:653	the TPQ	647:653	the TPQ in the active ;off-copper' conformation	647:693	The topaquinone (TPQ) cofactor and a copper ion characteristic of CuAOs are present in the active site, with the TPQ in the active ;off-copper' conformation.
16239734	0	17	theme	adhesion	66:73	arg1	protein-1					75:83	human semicarbazide-sensitive amine oxidase/vascular adhesion protein-1	13:83	human semicarbazide-sensitive amine oxidase/vascular adhesion protein-1	13:83	Structure of human semicarbazide-sensitive amine oxidase/vascular adhesion protein-1.
16239734	6	18	theme	adjacent	758:765	arg1	gate					806:809	a gate	804:809	a gate controlling its accessibility	804:839	The structure reveals that a leucine residue (Leu469) located adjacent to the active site could function as a gate controlling its accessibility.
16239734	6	18	theme	adjacent	758:765	arg1	residue					733:739	a leucine residue	723:739	a leucine residue (Leu469) located adjacent to the active site	723:784	The structure reveals that a leucine residue (Leu469) located adjacent to the active site could function as a gate controlling its accessibility.
16239734	10	19	theme	irreversible	1232:1243	arg1	2-hydrazinopyridine					1255:1273	the irreversible inhibitor 2-hydrazinopyridine	1228:1273	the irreversible inhibitor 2-hydrazinopyridine	1228:1273	The structure of an adduct of SSAO and the irreversible inhibitor 2-hydrazinopyridine has been solved and refined to 2.9 A resolution.
16239734	8	20	theme	potential	1049:1057	arg1	sites					1075:1079	five of six potential N-glycosylation sites	1037:1079	five of six potential N-glycosylation sites	1037:1079	Carbohydrate moieties are observed at five of six potential N-glycosylation sites.
16239734	5	21	theme	copper	575:580	arg1	present					614:620	present	614:620	present	614:620	The topaquinone (TPQ) cofactor and a copper ion characteristic of CuAOs are present in the active site, with the TPQ in the active ;off-copper' conformation.
16239734	5	21	theme	copper	575:580	arg1	characteristic					586:599	a copper ion characteristic	573:599	a copper ion characteristic of CuAOs	573:608	The topaquinone (TPQ) cofactor and a copper ion characteristic of CuAOs are present in the active site, with the TPQ in the active ;off-copper' conformation.
16239734	7	22	theme	RGD	845:847	arg1	motif					849:853	An RGD motif	842:853	An RGD motif	842:853	An RGD motif is displayed on the surface, where it could be involved in integrin binding and possibly play a role in the shedding of SSAO from the membrane.
16239734	2	23	theme	adhesion	303:310	arg1	molecules					312:320	the adhesion molecules	299:320	the adhesion molecules involved in the leukocyte-extravasation process	299:368	SSAO is also known as vascular adhesion protein-1 (VAP-1) and has been identified as one of the adhesion molecules involved in the leukocyte-extravasation process.
16239734	3	24	theme	SSAO	422:425	arg1	form					408:411	a truncated soluble form	388:411	a truncated soluble form of human SSAO	388:425	The structure of a truncated soluble form of human SSAO has been solved and refined to 2.5 A.
16239734	3	25	theme	truncated	390:398	arg1	form					408:411	a truncated soluble form	388:411	a truncated soluble form of human SSAO	388:425	The structure of a truncated soluble form of human SSAO has been solved and refined to 2.5 A.
16239734	5	26	theme	ion	582:584	arg1	present					614:620	present	614:620	present	614:620	The topaquinone (TPQ) cofactor and a copper ion characteristic of CuAOs are present in the active site, with the TPQ in the active ;off-copper' conformation.
16239734	5	26	theme	ion	582:584	arg1	characteristic					586:599	a copper ion characteristic	573:599	a copper ion characteristic of CuAOs	573:608	The topaquinone (TPQ) cofactor and a copper ion characteristic of CuAOs are present in the active site, with the TPQ in the active ;off-copper' conformation.
16239734	11	27	theme	specific	1447:1454	arg1	inhibitors					1456:1465	specific inhibitors	1447:1465	specific inhibitors	1447:1465	Together, these structures will aid efforts to identify natural substrates, provide valuable information for the design of specific inhibitors and direct further studies.
16239734	10	28	theme	adduct	1209:1214	arg1	structure					1193:1201	The structure	1189:1201	The structure of an adduct of SSAO and the irreversible inhibitor 2-hydrazinopyridine	1189:1273	The structure of an adduct of SSAO and the irreversible inhibitor 2-hydrazinopyridine has been solved and refined to 2.9 A resolution.
16239734	0	29	theme	semicarbazide-sensitive	19:41	arg1	protein-1					75:83	human semicarbazide-sensitive amine oxidase/vascular adhesion protein-1	13:83	human semicarbazide-sensitive amine oxidase/vascular adhesion protein-1	13:83	Structure of human semicarbazide-sensitive amine oxidase/vascular adhesion protein-1.
16239734	4	30	theme	typical	510:516	arg1	fold					505:508	a fold	503:508	a fold typical of the CuAO family	503:535	As expected, SSAO is a homodimer with a fold typical of the CuAO family.
16239734	11	31	theme	inhibitors	1456:1465	arg1	design					1437:1442	the design	1433:1442	the design of specific inhibitors	1433:1465	Together, these structures will aid efforts to identify natural substrates, provide valuable information for the design of specific inhibitors and direct further studies.
16239734	5	32	attach	present	614:620	arg2	present					614:620	present	614:620	present	614:620	The topaquinone (TPQ) cofactor and a copper ion characteristic of CuAOs are present in the active site, with the TPQ in the active ;off-copper' conformation.
16239734	5	32	attach	present	614:620	arg2	TPQ					555:557	TPQ	555:557	TPQ	555:557	The topaquinone (TPQ) cofactor and a copper ion characteristic of CuAOs are present in the active site, with the TPQ in the active ;off-copper' conformation.
16239734	5	32	attach	present	614:620	arg2	topaquinone					542:552	The topaquinone	538:552	The topaquinone (TPQ) cofactor	538:567	The topaquinone (TPQ) cofactor and a copper ion characteristic of CuAOs are present in the active site, with the TPQ in the active ;off-copper' conformation.
16239734	5	32	attach	present	614:620	arg2	characteristic					586:599	a copper ion characteristic	573:599	a copper ion characteristic of CuAOs	573:608	The topaquinone (TPQ) cofactor and a copper ion characteristic of CuAOs are present in the active site, with the TPQ in the active ;off-copper' conformation.
16239734	5	32	attach	present	614:620	arg1	site					636:639	the active site	625:639	the active site	625:639	The topaquinone (TPQ) cofactor and a copper ion characteristic of CuAOs are present in the active site, with the TPQ in the active ;off-copper' conformation.
16239734	0	33	theme	human	13:17	arg1	protein-1					75:83	human semicarbazide-sensitive amine oxidase/vascular adhesion protein-1	13:83	human semicarbazide-sensitive amine oxidase/vascular adhesion protein-1	13:83	Structure of human semicarbazide-sensitive amine oxidase/vascular adhesion protein-1.
16239734	4	34	theme	CuAO	525:528	arg1	family					530:535	the CuAO family	521:535	the CuAO family	521:535	As expected, SSAO is a homodimer with a fold typical of the CuAO family.
16239734	11	35	theme	further	1478:1484	arg1	studies					1486:1492	further studies	1478:1492	further studies	1478:1492	Together, these structures will aid efforts to identify natural substrates, provide valuable information for the design of specific inhibitors and direct further studies.
16239734	6	36	theme	active	774:779	arg1	site					781:784	the active site	770:784	the active site	770:784	The structure reveals that a leucine residue (Leu469) located adjacent to the active site could function as a gate controlling its accessibility.
16239734	1	37	theme	oxidases	189:196	arg1	family					155:160	a ubiquitous family	142:160	a ubiquitous family of copper-containing amine oxidases (CuAOs)	142:204	Semicarbazide-sensitive amine oxidase (SSAO) belongs to a ubiquitous family of copper-containing amine oxidases (CuAOs).
16239734	0	38	theme	oxidase/vascular	49:64	arg1	protein-1					75:83	human semicarbazide-sensitive amine oxidase/vascular adhesion protein-1	13:83	human semicarbazide-sensitive amine oxidase/vascular adhesion protein-1	13:83	Structure of human semicarbazide-sensitive amine oxidase/vascular adhesion protein-1.
16239734	0	39	theme	amine	43:47	arg1	protein-1					75:83	human semicarbazide-sensitive amine oxidase/vascular adhesion protein-1	13:83	human semicarbazide-sensitive amine oxidase/vascular adhesion protein-1	13:83	Structure of human semicarbazide-sensitive amine oxidase/vascular adhesion protein-1.
16239734	3	40	theme	human	416:420	arg1	SSAO					422:425	human SSAO	416:425	human SSAO	416:425	The structure of a truncated soluble form of human SSAO has been solved and refined to 2.5 A.
16239734	5	41	from	TPQ	651:653	arg1	conformation					682:693	the active ;off-copper' conformation	658:693	the active ;off-copper' conformation	658:693	The topaquinone (TPQ) cofactor and a copper ion characteristic of CuAOs are present in the active site, with the TPQ in the active ;off-copper' conformation.
16239734	2	42	theme	adhesion	238:245	arg1	VAP-1					258:262	VAP-1	258:262	VAP-1	258:262	SSAO is also known as vascular adhesion protein-1 (VAP-1) and has been identified as one of the adhesion molecules involved in the leukocyte-extravasation process.
16239734	2	42	theme	adhesion	238:245	arg1	protein-1					247:255	vascular adhesion protein-1	229:255	vascular adhesion protein-1 (VAP-1)	229:263	SSAO is also known as vascular adhesion protein-1 (VAP-1) and has been identified as one of the adhesion molecules involved in the leukocyte-extravasation process.
16239734	2	42	theme	adhesion	238:245	arg1	SSAO					207:210	SSAO	207:210	SSAO	207:210	SSAO is also known as vascular adhesion protein-1 (VAP-1) and has been identified as one of the adhesion molecules involved in the leukocyte-extravasation process.
16239734	5	43	theme	active	662:667	arg1	conformation					682:693	the active ;off-copper' conformation	658:693	the active ;off-copper' conformation	658:693	The topaquinone (TPQ) cofactor and a copper ion characteristic of CuAOs are present in the active site, with the TPQ in the active ;off-copper' conformation.
16239734	3	44	theme	soluble	400:406	arg1	form					408:411	a truncated soluble form	388:411	a truncated soluble form of human SSAO	388:425	The structure of a truncated soluble form of human SSAO has been solved and refined to 2.5 A.
16239734	5	45	theme	off-copper	670:679	arg1	conformation					682:693	the active ;off-copper' conformation	658:693	the active ;off-copper' conformation	658:693	The topaquinone (TPQ) cofactor and a copper ion characteristic of CuAOs are present in the active site, with the TPQ in the active ;off-copper' conformation.
16239734	2	46	theme	vascular	229:236	arg1	VAP-1					258:262	VAP-1	258:262	VAP-1	258:262	SSAO is also known as vascular adhesion protein-1 (VAP-1) and has been identified as one of the adhesion molecules involved in the leukocyte-extravasation process.
16239734	2	46	theme	vascular	229:236	arg1	protein-1					247:255	vascular adhesion protein-1	229:255	vascular adhesion protein-1 (VAP-1)	229:263	SSAO is also known as vascular adhesion protein-1 (VAP-1) and has been identified as one of the adhesion molecules involved in the leukocyte-extravasation process.
16239734	2	46	theme	vascular	229:236	arg1	SSAO					207:210	SSAO	207:210	SSAO	207:210	SSAO is also known as vascular adhesion protein-1 (VAP-1) and has been identified as one of the adhesion molecules involved in the leukocyte-extravasation process.
16239734	3	47	theme	form	408:411	arg1	structure					375:383	The structure	371:383	The structure of a truncated soluble form of human SSAO	371:425	The structure of a truncated soluble form of human SSAO has been solved and refined to 2.5 A.
16239734	9	48	theme	active-site	1125:1135	arg1	entrance					1137:1144	the active-site entrance	1121:1144	the active-site entrance	1121:1144	Carbohydrates attached to Asn232 flank the active-site entrance and might influence substrate specificity.
16239734	10	49	theme	SSAO	1219:1222	arg1	adduct					1209:1214	an adduct	1206:1214	an adduct of SSAO and the irreversible inhibitor 2-hydrazinopyridine	1206:1273	The structure of an adduct of SSAO and the irreversible inhibitor 2-hydrazinopyridine has been solved and refined to 2.9 A resolution.
16239734	7	50	theme	SSAO	975:978	arg1	shedding					963:970	the shedding	959:970	the shedding of SSAO from the membrane	959:996	An RGD motif is displayed on the surface, where it could be involved in integrin binding and possibly play a role in the shedding of SSAO from the membrane.
16239734	11	51	theme	natural	1380:1386	arg1	substrates					1388:1397	natural substrates	1380:1397	natural substrates	1380:1397	Together, these structures will aid efforts to identify natural substrates, provide valuable information for the design of specific inhibitors and direct further studies.
16239734	7	52	from	membrane	989:996	arg1	shedding					963:970	the shedding	959:970	the shedding of SSAO from the membrane	959:996	An RGD motif is displayed on the surface, where it could be involved in integrin binding and possibly play a role in the shedding of SSAO from the membrane.
16239734	1	53	theme	ubiquitous	144:153	arg1	family					155:160	a ubiquitous family	142:160	a ubiquitous family of copper-containing amine oxidases (CuAOs)	142:204	Semicarbazide-sensitive amine oxidase (SSAO) belongs to a ubiquitous family of copper-containing amine oxidases (CuAOs).
16239734	5	54	theme	active	629:634	arg1	site					636:639	the active site	625:639	the active site	625:639	The topaquinone (TPQ) cofactor and a copper ion characteristic of CuAOs are present in the active site, with the TPQ in the active ;off-copper' conformation.
16239734	2	55	theme	molecules	312:320	arg1	molecules					312:320	the adhesion molecules	299:320	the adhesion molecules involved in the leukocyte-extravasation process	299:368	SSAO is also known as vascular adhesion protein-1 (VAP-1) and has been identified as one of the adhesion molecules involved in the leukocyte-extravasation process.
16239734	2	55	theme	molecules	312:320	arg1	SSAO					207:210	SSAO	207:210	SSAO	207:210	SSAO is also known as vascular adhesion protein-1 (VAP-1) and has been identified as one of the adhesion molecules involved in the leukocyte-extravasation process.
16239734	2	55	theme	molecules	312:320	arg1	one					292:294	one	292:294	one	292:294	SSAO is also known as vascular adhesion protein-1 (VAP-1) and has been identified as one of the adhesion molecules involved in the leukocyte-extravasation process.
16239734	8	56	theme	Carbohydrate	999:1010	arg1	moieties					1012:1019	Carbohydrate moieties	999:1019	Carbohydrate moieties	999:1019	Carbohydrate moieties are observed at five of six potential N-glycosylation sites.
16239734	10	57	theme	2-hydrazinopyridine	1255:1273	arg1	adduct					1209:1214	an adduct	1206:1214	an adduct of SSAO and the irreversible inhibitor 2-hydrazinopyridine	1206:1273	The structure of an adduct of SSAO and the irreversible inhibitor 2-hydrazinopyridine has been solved and refined to 2.9 A resolution.
16239734	5	58	from	present	614:620	arg1	site					636:639	the active site	625:639	the active site	625:639	The topaquinone (TPQ) cofactor and a copper ion characteristic of CuAOs are present in the active site, with the TPQ in the active ;off-copper' conformation.
16239734	0	59	theme	protein-1	75:83	arg1	Structure					0:8	Structure	0:8	Structure of human semicarbazide-sensitive amine oxidase/vascular adhesion protein-1	0:83	Structure of human semicarbazide-sensitive amine oxidase/vascular adhesion protein-1.
16239734	9	60	theme	substrate	1166:1174	arg1	specificity					1176:1186	substrate specificity	1166:1186	substrate specificity	1166:1186	Carbohydrates attached to Asn232 flank the active-site entrance and might influence substrate specificity.
16239734	8	61	theme	N-glycosylation	1059:1073	arg1	sites					1075:1079	five of six potential N-glycosylation sites	1037:1079	five of six potential N-glycosylation sites	1037:1079	Carbohydrate moieties are observed at five of six potential N-glycosylation sites.
16239734	10	62	theme	inhibitor	1245:1253	arg1	2-hydrazinopyridine					1255:1273	the irreversible inhibitor 2-hydrazinopyridine	1228:1273	the irreversible inhibitor 2-hydrazinopyridine	1228:1273	The structure of an adduct of SSAO and the irreversible inhibitor 2-hydrazinopyridine has been solved and refined to 2.9 A resolution.
16239734	1	63	theme	copper-containing	165:181	arg1	CuAOs					199:203	CuAOs	199:203	CuAOs	199:203	Semicarbazide-sensitive amine oxidase (SSAO) belongs to a ubiquitous family of copper-containing amine oxidases (CuAOs).
16239734	1	63	theme	copper-containing	165:181	arg1	oxidases					189:196	copper-containing amine oxidases	165:196	copper-containing amine oxidases (CuAOs)	165:204	Semicarbazide-sensitive amine oxidase (SSAO) belongs to a ubiquitous family of copper-containing amine oxidases (CuAOs).
16239734	11	64	theme	valuable	1408:1415	arg1	information					1417:1427	valuable information	1408:1427	valuable information for the design of specific inhibitors	1408:1465	Together, these structures will aid efforts to identify natural substrates, provide valuable information for the design of specific inhibitors and direct further studies.
23959878	6	0	theme	native	913:918	arg1	hIDUA					939:943	native and deglycosylated hIDUA	913:943	native and deglycosylated hIDUA	913:943	The kinetics of native and deglycosylated hIDUA suggested that the N-glycan is also involved in catalytic processes.
23959878	3	1	theme	sulfate	491:497	arg1	accumulation					458:469	accumulation	458:469	accumulation of dermatan/heparan sulfate	458:497	Here, we show that human α-l-iduronidase (hIDUA), of which a dysfunction causes accumulation of dermatan/heparan sulfate leading to mucopolysaccharidosis type I, uses its own N-glycan as a substrate binding and catalytic module.
23959878	0	2	theme	catalytic	71:79	arg1	N-glycan					35:42	its own N-glycan	27:42	its own N-glycan	27:42	Human α-L-iduronidase uses its own N-glycan as a substrate-binding and catalytic module.
23959878	0	2	theme	catalytic	71:79	arg1	module					81:86	a substrate-binding and catalytic module	47:86	a substrate-binding and catalytic module	47:86	Human α-L-iduronidase uses its own N-glycan as a substrate-binding and catalytic module.
23959878	1	3	theme	various	173:179	arg1	functions					181:189	various functions	173:189	various functions	173:189	N-glycosylation is a major posttranslational modification that endows proteins with various functions.
23959878	2	4	from	effects	314:320	arg1	activities					344:353	their activities	338:353	their activities	338:353	It is established that N-glycans are essential for the correct folding and stability of some enzymes; however, the actual effects of N-glycans on their activities are poorly understood.
23959878	6	5	theme	catalytic	993:1001	arg1	processes					1003:1011	catalytic processes	993:1011	catalytic processes	993:1011	The kinetics of native and deglycosylated hIDUA suggested that the N-glycan is also involved in catalytic processes.
23959878	3	6	theme	own	549:551	arg1	binding					577:583	a substrate binding	565:583	a substrate binding	565:583	Here, we show that human α-l-iduronidase (hIDUA), of which a dysfunction causes accumulation of dermatan/heparan sulfate leading to mucopolysaccharidosis type I, uses its own N-glycan as a substrate binding and catalytic module.
23959878	3	6	theme	own	549:551	arg1	N-glycan					553:560	its own N-glycan	545:560	its own N-glycan	545:560	Here, we show that human α-l-iduronidase (hIDUA), of which a dysfunction causes accumulation of dermatan/heparan sulfate leading to mucopolysaccharidosis type I, uses its own N-glycan as a substrate binding and catalytic module.
23959878	6	7	gly	deglycosylated	924:937	arg1	hIDUA					939:943	native and deglycosylated hIDUA	913:943	native and deglycosylated hIDUA	913:943	The kinetics of native and deglycosylated hIDUA suggested that the N-glycan is also involved in catalytic processes.
23959878	4	8	attach	attached	677:684	arg2	N-glycan					668:675	the N-glycan	664:675	the N-glycan attached to N372	664:692	Structural analysis revealed that the mannose residue of the N-glycan attached to N372 constituted a part of the substrate-binding pocket and interacted directly with a substrate.
23959878	4	8	attach	attached	677:684	arg1	N372					689:692	N372	689:692	N372	689:692	Structural analysis revealed that the mannose residue of the N-glycan attached to N372 constituted a part of the substrate-binding pocket and interacted directly with a substrate.
23959878	2	9	theme	enzymes	285:291	arg1	stability					267:275	stability	267:275	stability	267:275	It is established that N-glycans are essential for the correct folding and stability of some enzymes; however, the actual effects of N-glycans on their activities are poorly understood.
23959878	2	9	theme	enzymes	285:291	arg1	folding					255:261	folding	255:261	folding	255:261	It is established that N-glycans are essential for the correct folding and stability of some enzymes; however, the actual effects of N-glycans on their activities are poorly understood.
23959878	4	10	theme	mannose	645:651	arg1	residue					653:659	the mannose residue	641:659	the mannose residue of the N-glycan attached to N372	641:692	Structural analysis revealed that the mannose residue of the N-glycan attached to N372 constituted a part of the substrate-binding pocket and interacted directly with a substrate.
23959878	4	10	theme	mannose	645:651	arg1	N-glycan					668:675	the N-glycan	664:675	the N-glycan attached to N372	664:692	Structural analysis revealed that the mannose residue of the N-glycan attached to N372 constituted a part of the substrate-binding pocket and interacted directly with a substrate.
23959878	4	11	theme	substrate-binding	720:736	arg1	pocket					738:743	the substrate-binding pocket	716:743	the substrate-binding pocket	716:743	Structural analysis revealed that the mannose residue of the N-glycan attached to N372 constituted a part of the substrate-binding pocket and interacted directly with a substrate.
23959878	0	12	theme	Human	0:4	arg1	α-L-iduronidase					6:20	Human α-L-iduronidase	0:20	Human α-L-iduronidase	0:20	Human α-L-iduronidase uses its own N-glycan as a substrate-binding and catalytic module.
23959878	2	13	theme	actual	307:312	arg1	effects					314:320	the actual effects	303:320	the actual effects of N-glycans on their activities	303:353	It is established that N-glycans are essential for the correct folding and stability of some enzymes; however, the actual effects of N-glycans on their activities are poorly understood.
23959878	5	14	theme	enzyme	823:828	arg1	activity					830:837	enzyme activity	823:837	enzyme activity	823:837	A deglycosylation study showed that enzyme activity was highly correlated with the N-glycan attached to N372.
23959878	4	15	theme	pocket	738:743	arg1	part					708:711	a part	706:711	a part of the substrate-binding pocket	706:743	Structural analysis revealed that the mannose residue of the N-glycan attached to N372 constituted a part of the substrate-binding pocket and interacted directly with a substrate.
23959878	3	16	theme	human	397:401	arg1	hIDUA					420:424	hIDUA	420:424	hIDUA	420:424	Here, we show that human α-l-iduronidase (hIDUA), of which a dysfunction causes accumulation of dermatan/heparan sulfate leading to mucopolysaccharidosis type I, uses its own N-glycan as a substrate binding and catalytic module.
23959878	3	16	theme	human	397:401	arg1	α-l-iduronidase					403:417	human α-l-iduronidase	397:417	human α-l-iduronidase (hIDUA)	397:425	Here, we show that human α-l-iduronidase (hIDUA), of which a dysfunction causes accumulation of dermatan/heparan sulfate leading to mucopolysaccharidosis type I, uses its own N-glycan as a substrate binding and catalytic module.
23959878	3	17	theme	dermatan/heparan	474:489	arg1	sulfate					491:497	dermatan/heparan sulfate	474:497	dermatan/heparan sulfate	474:497	Here, we show that human α-l-iduronidase (hIDUA), of which a dysfunction causes accumulation of dermatan/heparan sulfate leading to mucopolysaccharidosis type I, uses its own N-glycan as a substrate binding and catalytic module.
23959878	2	18	theme	correct	247:253	arg1	folding					255:261	folding	255:261	folding	255:261	It is established that N-glycans are essential for the correct folding and stability of some enzymes; however, the actual effects of N-glycans on their activities are poorly understood.
23959878	0	19	theme	own	31:33	arg1	N-glycan					35:42	its own N-glycan	27:42	its own N-glycan	27:42	Human α-L-iduronidase uses its own N-glycan as a substrate-binding and catalytic module.
23959878	0	19	theme	own	31:33	arg1	module					81:86	a substrate-binding and catalytic module	47:86	a substrate-binding and catalytic module	47:86	Human α-L-iduronidase uses its own N-glycan as a substrate-binding and catalytic module.
23959878	7	20	theme	N-glycans	1075:1083	arg1	function					1063:1070	a previously unrecognized function	1037:1070	a previously unrecognized function of N-glycans	1037:1083	Our study demonstrates a previously unrecognized function of N-glycans.
23959878	5	21	attach	attached	879:886	arg2	N-glycan					870:877	the N-glycan	866:877	the N-glycan attached to N372	866:894	A deglycosylation study showed that enzyme activity was highly correlated with the N-glycan attached to N372.
23959878	5	21	attach	attached	879:886	arg1	N372					891:894	N372	891:894	N372	891:894	A deglycosylation study showed that enzyme activity was highly correlated with the N-glycan attached to N372.
23959878	7	22	theme	unrecognized	1050:1061	arg1	function					1063:1070	a previously unrecognized function	1037:1070	a previously unrecognized function of N-glycans	1037:1083	Our study demonstrates a previously unrecognized function of N-glycans.
23959878	1	23	theme	major	110:114	arg1	modification					134:145	a major posttranslational modification	108:145	a major posttranslational modification that endows proteins with various functions	108:189	N-glycosylation is a major posttranslational modification that endows proteins with various functions.
23959878	1	23	theme	major	110:114	arg1	N-glycosylation					89:103	N-glycosylation	89:103	N-glycosylation	89:103	N-glycosylation is a major posttranslational modification that endows proteins with various functions.
23959878	5	24	theme	deglycosylation	789:803	arg1	study					805:809	A deglycosylation study	787:809	A deglycosylation study	787:809	A deglycosylation study showed that enzyme activity was highly correlated with the N-glycan attached to N372.
23959878	6	25	theme	hIDUA	939:943	arg1	kinetics					901:908	The kinetics	897:908	The kinetics of native and deglycosylated hIDUA	897:943	The kinetics of native and deglycosylated hIDUA suggested that the N-glycan is also involved in catalytic processes.
23959878	3	26	theme	substrate	567:575	arg1	binding					577:583	a substrate binding	565:583	a substrate binding	565:583	Here, we show that human α-l-iduronidase (hIDUA), of which a dysfunction causes accumulation of dermatan/heparan sulfate leading to mucopolysaccharidosis type I, uses its own N-glycan as a substrate binding and catalytic module.
23959878	3	26	theme	substrate	567:575	arg1	N-glycan					553:560	its own N-glycan	545:560	its own N-glycan	545:560	Here, we show that human α-l-iduronidase (hIDUA), of which a dysfunction causes accumulation of dermatan/heparan sulfate leading to mucopolysaccharidosis type I, uses its own N-glycan as a substrate binding and catalytic module.
23959878	1	27	theme	posttranslational	116:132	arg1	modification					134:145	a major posttranslational modification	108:145	a major posttranslational modification that endows proteins with various functions	108:189	N-glycosylation is a major posttranslational modification that endows proteins with various functions.
23959878	1	27	theme	posttranslational	116:132	arg1	N-glycosylation					89:103	N-glycosylation	89:103	N-glycosylation	89:103	N-glycosylation is a major posttranslational modification that endows proteins with various functions.
23959878	6	28	theme	deglycosylated	924:937	arg1	hIDUA					939:943	native and deglycosylated hIDUA	913:943	native and deglycosylated hIDUA	913:943	The kinetics of native and deglycosylated hIDUA suggested that the N-glycan is also involved in catalytic processes.
23959878	2	29	theme	N-glycans	325:333	arg1	effects					314:320	the actual effects	303:320	the actual effects of N-glycans on their activities	303:353	It is established that N-glycans are essential for the correct folding and stability of some enzymes; however, the actual effects of N-glycans on their activities are poorly understood.
23959878	4	30	theme	N-glycan	668:675	arg1	residue					653:659	the mannose residue	641:659	the mannose residue of the N-glycan attached to N372	641:692	Structural analysis revealed that the mannose residue of the N-glycan attached to N372 constituted a part of the substrate-binding pocket and interacted directly with a substrate.
23959878	4	30	theme	N-glycan	668:675	arg1	N-glycan					668:675	the N-glycan	664:675	the N-glycan attached to N372	664:692	Structural analysis revealed that the mannose residue of the N-glycan attached to N372 constituted a part of the substrate-binding pocket and interacted directly with a substrate.
23959878	3	31	theme	catalytic	589:597	arg1	module					599:604	catalytic module	589:604	catalytic module	589:604	Here, we show that human α-l-iduronidase (hIDUA), of which a dysfunction causes accumulation of dermatan/heparan sulfate leading to mucopolysaccharidosis type I, uses its own N-glycan as a substrate binding and catalytic module.
23959878	4	32	theme	Structural	607:616	arg1	analysis					618:625	Structural analysis	607:625	Structural analysis	607:625	Structural analysis revealed that the mannose residue of the N-glycan attached to N372 constituted a part of the substrate-binding pocket and interacted directly with a substrate.
23959878	0	33	theme	substrate-binding	49:65	arg1	N-glycan					35:42	its own N-glycan	27:42	its own N-glycan	27:42	Human α-L-iduronidase uses its own N-glycan as a substrate-binding and catalytic module.
23959878	0	33	theme	substrate-binding	49:65	arg1	module					81:86	a substrate-binding and catalytic module	47:86	a substrate-binding and catalytic module	47:86	Human α-L-iduronidase uses its own N-glycan as a substrate-binding and catalytic module.
23959878	3	34	theme	mucopolysaccharidosis	510:530	arg1	type					532:535	mucopolysaccharidosis type I	510:537	mucopolysaccharidosis type I	510:537	Here, we show that human α-l-iduronidase (hIDUA), of which a dysfunction causes accumulation of dermatan/heparan sulfate leading to mucopolysaccharidosis type I, uses its own N-glycan as a substrate binding and catalytic module.
21045127	3	0	theme	interacting	662:672	arg1	subunits					674:681	myriad interacting subunits	655:681	myriad interacting subunits	655:681	Although cycling of O-GlcNAc is catalyzed by only two highly conserved enzymes, O-GlcNAc transferase (OGT), which adds the sugar, and β-N-acetylglucosaminidase (O-GlcNAcase), which hydrolyzes it, the targeting of these enzymes is highly specific and is controlled by myriad interacting subunits.
21045127	2	1	theme	wide	363:366	arg1	variety					368:374	a wide variety	361:374	a wide variety of stimuli	361:385	Like phosphorylation, O-GlcNAc cycles in response to a wide variety of stimuli.
21045127	2	1	theme	wide	363:366	arg1	stimuli					379:385	stimuli	379:385	stimuli	379:385	Like phosphorylation, O-GlcNAc cycles in response to a wide variety of stimuli.
21045127	7	2	theme	heat	1064:1067	arg1	shock					1069:1073	heat shock	1064:1073	heat shock	1064:1073	Finally, we show that histone O-GlcNAcylation changes during mitosis and with heat shock.
21045127	2	3	dep	variety	368:374	arg1	response					349:356	response	349:356	response	349:356	Like phosphorylation, O-GlcNAc cycles in response to a wide variety of stimuli.
21045127	1	4	theme	serine	107:112	arg1	modification					91:102	Dynamic posttranslational modification	65:102	Dynamic posttranslational modification of serine and threonine residues of nucleocytoplasmic proteins by β-N-acetylglucosamine (O-GlcNAc)	65:201	Dynamic posttranslational modification of serine and threonine residues of nucleocytoplasmic proteins by β-N-acetylglucosamine (O-GlcNAc) is a regulator of cellular processes such as transcription, signaling, and protein-protein interactions.
21045127	1	4	theme	serine	107:112	arg1	regulator					208:216	a regulator	206:216	a regulator of cellular processes such as transcription, signaling, and protein-protein interactions	206:305	Dynamic posttranslational modification of serine and threonine residues of nucleocytoplasmic proteins by β-N-acetylglucosamine (O-GlcNAc) is a regulator of cellular processes such as transcription, signaling, and protein-protein interactions.
21045127	4	5	theme	specific	717:724	arg1	approaches					754:763	multiple specific immunological and enzymatic approaches	708:763	multiple specific immunological and enzymatic approaches	708:763	Here, we demonstrate by multiple specific immunological and enzymatic approaches that histones, the proteins that package DNA within the nucleus, are O-GlcNAcylated in vivo.
21045127	4	6	theme	enzymatic	744:752	arg1	approaches					754:763	multiple specific immunological and enzymatic approaches	708:763	multiple specific immunological and enzymatic approaches	708:763	Here, we demonstrate by multiple specific immunological and enzymatic approaches that histones, the proteins that package DNA within the nucleus, are O-GlcNAcylated in vivo.
21045127	1	7	theme	Dynamic	65:71	arg1	modification					91:102	Dynamic posttranslational modification	65:102	Dynamic posttranslational modification of serine and threonine residues of nucleocytoplasmic proteins by β-N-acetylglucosamine (O-GlcNAc)	65:201	Dynamic posttranslational modification of serine and threonine residues of nucleocytoplasmic proteins by β-N-acetylglucosamine (O-GlcNAc) is a regulator of cellular processes such as transcription, signaling, and protein-protein interactions.
21045127	1	7	theme	Dynamic	65:71	arg1	regulator					208:216	a regulator	206:216	a regulator of cellular processes such as transcription, signaling, and protein-protein interactions	206:305	Dynamic posttranslational modification of serine and threonine residues of nucleocytoplasmic proteins by β-N-acetylglucosamine (O-GlcNAc) is a regulator of cellular processes such as transcription, signaling, and protein-protein interactions.
21045127	3	8	theme	conserved	449:457	arg1	β-N-acetylglucosaminidase					522:546	β-N-acetylglucosaminidase	522:546	β-N-acetylglucosaminidase (O-GlcNAcase)	522:560	Although cycling of O-GlcNAc is catalyzed by only two highly conserved enzymes, O-GlcNAc transferase (OGT), which adds the sugar, and β-N-acetylglucosaminidase (O-GlcNAcase), which hydrolyzes it, the targeting of these enzymes is highly specific and is controlled by myriad interacting subunits.
21045127	3	8	theme	conserved	449:457	arg1	enzymes					459:465	only two highly conserved enzymes	433:465	only two highly conserved enzymes	433:465	Although cycling of O-GlcNAc is catalyzed by only two highly conserved enzymes, O-GlcNAc transferase (OGT), which adds the sugar, and β-N-acetylglucosaminidase (O-GlcNAcase), which hydrolyzes it, the targeting of these enzymes is highly specific and is controlled by myriad interacting subunits.
21045127	3	8	theme	conserved	449:457	arg1	transferase					477:487	O-GlcNAc transferase	468:487	O-GlcNAc transferase (OGT)	468:493	Although cycling of O-GlcNAc is catalyzed by only two highly conserved enzymes, O-GlcNAc transferase (OGT), which adds the sugar, and β-N-acetylglucosaminidase (O-GlcNAcase), which hydrolyzes it, the targeting of these enzymes is highly specific and is controlled by myriad interacting subunits.
21045127	1	9	theme	posttranslational	73:89	arg1	modification					91:102	Dynamic posttranslational modification	65:102	Dynamic posttranslational modification of serine and threonine residues of nucleocytoplasmic proteins by β-N-acetylglucosamine (O-GlcNAc)	65:201	Dynamic posttranslational modification of serine and threonine residues of nucleocytoplasmic proteins by β-N-acetylglucosamine (O-GlcNAc) is a regulator of cellular processes such as transcription, signaling, and protein-protein interactions.
21045127	1	9	theme	posttranslational	73:89	arg1	regulator					208:216	a regulator	206:216	a regulator of cellular processes such as transcription, signaling, and protein-protein interactions	206:305	Dynamic posttranslational modification of serine and threonine residues of nucleocytoplasmic proteins by β-N-acetylglucosamine (O-GlcNAc) is a regulator of cellular processes such as transcription, signaling, and protein-protein interactions.
21045127	1	10	theme	protein-protein	278:292	arg1	interactions					294:305	protein-protein interactions	278:305	protein-protein interactions	278:305	Dynamic posttranslational modification of serine and threonine residues of nucleocytoplasmic proteins by β-N-acetylglucosamine (O-GlcNAc) is a regulator of cellular processes such as transcription, signaling, and protein-protein interactions.
21045127	4	11	theme	multiple	708:715	arg1	approaches					754:763	multiple specific immunological and enzymatic approaches	708:763	multiple specific immunological and enzymatic approaches	708:763	Here, we demonstrate by multiple specific immunological and enzymatic approaches that histones, the proteins that package DNA within the nucleus, are O-GlcNAcylated in vivo.
21045127	8	12	theme	histone	1187:1193	arg1	part					1175:1178	part	1175:1178	part of the histone code	1175:1198	Taken together, these data show that O-GlcNAc cycles dynamically on histones and can be considered part of the histone code.
21045127	3	13	theme	O-GlcNAc	468:475	arg1	OGT					490:492	OGT	490:492	OGT	490:492	Although cycling of O-GlcNAc is catalyzed by only two highly conserved enzymes, O-GlcNAc transferase (OGT), which adds the sugar, and β-N-acetylglucosaminidase (O-GlcNAcase), which hydrolyzes it, the targeting of these enzymes is highly specific and is controlled by myriad interacting subunits.
21045127	3	13	theme	O-GlcNAc	468:475	arg1	enzymes					459:465	only two highly conserved enzymes	433:465	only two highly conserved enzymes	433:465	Although cycling of O-GlcNAc is catalyzed by only two highly conserved enzymes, O-GlcNAc transferase (OGT), which adds the sugar, and β-N-acetylglucosaminidase (O-GlcNAcase), which hydrolyzes it, the targeting of these enzymes is highly specific and is controlled by myriad interacting subunits.
21045127	3	13	theme	O-GlcNAc	468:475	arg1	transferase					477:487	O-GlcNAc transferase	468:487	O-GlcNAc transferase (OGT)	468:493	Although cycling of O-GlcNAc is catalyzed by only two highly conserved enzymes, O-GlcNAc transferase (OGT), which adds the sugar, and β-N-acetylglucosaminidase (O-GlcNAcase), which hydrolyzes it, the targeting of these enzymes is highly specific and is controlled by myriad interacting subunits.
21045127	8	14	dep	histone	1187:1193	arg1	code					1195:1198	code	1195:1198	code	1195:1198	Taken together, these data show that O-GlcNAc cycles dynamically on histones and can be considered part of the histone code.
21045127	8	15	from	cycles	1122:1127	arg1	histones					1144:1151	histones	1144:1151	histones	1144:1151	Taken together, these data show that O-GlcNAc cycles dynamically on histones and can be considered part of the histone code.
21045127	0	16	dep	histone	51:57	arg1	code					59:62	code	59:62	code	59:62	Beta-N-acetylglucosamine (O-GlcNAc) is part of the histone code.
21045127	1	17	theme	nucleocytoplasmic	140:156	arg1	proteins					158:165	nucleocytoplasmic proteins	140:165	nucleocytoplasmic proteins	140:165	Dynamic posttranslational modification of serine and threonine residues of nucleocytoplasmic proteins by β-N-acetylglucosamine (O-GlcNAc) is a regulator of cellular processes such as transcription, signaling, and protein-protein interactions.
21045127	7	18	theme	histone	1008:1014	arg1	O-GlcNAcylation					1016:1030	histone O-GlcNAcylation	1008:1030	histone O-GlcNAcylation	1008:1030	Finally, we show that histone O-GlcNAcylation changes during mitosis and with heat shock.
21045127	1	19	theme	cellular	221:228	arg1	signaling					263:271	signaling	263:271	signaling	263:271	Dynamic posttranslational modification of serine and threonine residues of nucleocytoplasmic proteins by β-N-acetylglucosamine (O-GlcNAc) is a regulator of cellular processes such as transcription, signaling, and protein-protein interactions.
21045127	1	19	theme	cellular	221:228	arg1	processes					230:238	cellular processes	221:238	cellular processes such as transcription, signaling, and protein-protein interactions	221:305	Dynamic posttranslational modification of serine and threonine residues of nucleocytoplasmic proteins by β-N-acetylglucosamine (O-GlcNAc) is a regulator of cellular processes such as transcription, signaling, and protein-protein interactions.
21045127	1	19	theme	cellular	221:228	arg1	transcription					248:260	transcription	248:260	transcription	248:260	Dynamic posttranslational modification of serine and threonine residues of nucleocytoplasmic proteins by β-N-acetylglucosamine (O-GlcNAc) is a regulator of cellular processes such as transcription, signaling, and protein-protein interactions.
21045127	1	19	theme	cellular	221:228	arg1	interactions					294:305	protein-protein interactions	278:305	protein-protein interactions	278:305	Dynamic posttranslational modification of serine and threonine residues of nucleocytoplasmic proteins by β-N-acetylglucosamine (O-GlcNAc) is a regulator of cellular processes such as transcription, signaling, and protein-protein interactions.
21045127	3	20	theme	O-GlcNAc	408:415	arg1	cycling					397:403	cycling	397:403	cycling of O-GlcNAc	397:415	Although cycling of O-GlcNAc is catalyzed by only two highly conserved enzymes, O-GlcNAc transferase (OGT), which adds the sugar, and β-N-acetylglucosaminidase (O-GlcNAcase), which hydrolyzes it, the targeting of these enzymes is highly specific and is controlled by myriad interacting subunits.
21045127	6	21	theme	O-GlcNAc	917:924	arg1	sites					926:930	O-GlcNAc sites	917:930	O-GlcNAc sites on histones H2A, H2B, and H4 using mass spectrometry	917:983	We identify O-GlcNAc sites on histones H2A, H2B, and H4 using mass spectrometry.
21045127	6	22	dep	histones	935:942	arg1	histones					935:942	histones H2A, H2B, and H4	935:959	histones H2A, H2B, and H4 using mass spectrometry	935:983	We identify O-GlcNAc sites on histones H2A, H2B, and H4 using mass spectrometry.
21045127	6	22	dep	histones	935:942	arg1	H2B					949:951	H2B	949:951	H2B	949:951	We identify O-GlcNAc sites on histones H2A, H2B, and H4 using mass spectrometry.
21045127	6	22	dep	histones	935:942	arg1	H4					958:959	H4	958:959	H4	958:959	We identify O-GlcNAc sites on histones H2A, H2B, and H4 using mass spectrometry.
21045127	6	22	dep	histones	935:942	arg1	H2A					944:946	H2A	944:946	H2A	944:946	We identify O-GlcNAc sites on histones H2A, H2B, and H4 using mass spectrometry.
21045127	1	23	theme	threonine	118:126	arg1	modification					91:102	Dynamic posttranslational modification	65:102	Dynamic posttranslational modification of serine and threonine residues of nucleocytoplasmic proteins by β-N-acetylglucosamine (O-GlcNAc)	65:201	Dynamic posttranslational modification of serine and threonine residues of nucleocytoplasmic proteins by β-N-acetylglucosamine (O-GlcNAc) is a regulator of cellular processes such as transcription, signaling, and protein-protein interactions.
21045127	1	23	theme	threonine	118:126	arg1	regulator					208:216	a regulator	206:216	a regulator of cellular processes such as transcription, signaling, and protein-protein interactions	206:305	Dynamic posttranslational modification of serine and threonine residues of nucleocytoplasmic proteins by β-N-acetylglucosamine (O-GlcNAc) is a regulator of cellular processes such as transcription, signaling, and protein-protein interactions.
21045127	6	24	from	sites	926:930	arg1	histones					935:942	histones H2A, H2B, and H4	935:959	histones H2A, H2B, and H4 using mass spectrometry	935:983	We identify O-GlcNAc sites on histones H2A, H2B, and H4 using mass spectrometry.
21045127	6	24	from	sites	926:930	arg1	H2B					949:951	H2B	949:951	H2B	949:951	We identify O-GlcNAc sites on histones H2A, H2B, and H4 using mass spectrometry.
21045127	6	24	from	sites	926:930	arg1	H4					958:959	H4	958:959	H4	958:959	We identify O-GlcNAc sites on histones H2A, H2B, and H4 using mass spectrometry.
21045127	6	24	from	sites	926:930	arg1	H2A					944:946	H2A	944:946	H2A	944:946	We identify O-GlcNAc sites on histones H2A, H2B, and H4 using mass spectrometry.
21045127	3	25	theme	myriad	655:660	arg1	subunits					674:681	myriad interacting subunits	655:681	myriad interacting subunits	655:681	Although cycling of O-GlcNAc is catalyzed by only two highly conserved enzymes, O-GlcNAc transferase (OGT), which adds the sugar, and β-N-acetylglucosaminidase (O-GlcNAcase), which hydrolyzes it, the targeting of these enzymes is highly specific and is controlled by myriad interacting subunits.
21045127	1	26	theme	processes	230:238	arg1	regulator					208:216	a regulator	206:216	a regulator of cellular processes such as transcription, signaling, and protein-protein interactions	206:305	Dynamic posttranslational modification of serine and threonine residues of nucleocytoplasmic proteins by β-N-acetylglucosamine (O-GlcNAc) is a regulator of cellular processes such as transcription, signaling, and protein-protein interactions.
21045127	1	26	theme	processes	230:238	arg1	modification					91:102	Dynamic posttranslational modification	65:102	Dynamic posttranslational modification of serine and threonine residues of nucleocytoplasmic proteins by β-N-acetylglucosamine (O-GlcNAc)	65:201	Dynamic posttranslational modification of serine and threonine residues of nucleocytoplasmic proteins by β-N-acetylglucosamine (O-GlcNAc) is a regulator of cellular processes such as transcription, signaling, and protein-protein interactions.
21045127	3	27	theme	enzymes	607:613	arg1	specific					625:632	specific	625:632	specific	625:632	Although cycling of O-GlcNAc is catalyzed by only two highly conserved enzymes, O-GlcNAc transferase (OGT), which adds the sugar, and β-N-acetylglucosaminidase (O-GlcNAcase), which hydrolyzes it, the targeting of these enzymes is highly specific and is controlled by myriad interacting subunits.
21045127	3	27	theme	enzymes	607:613	arg1	targeting					588:596	the targeting	584:596	the targeting of these enzymes	584:613	Although cycling of O-GlcNAc is catalyzed by only two highly conserved enzymes, O-GlcNAc transferase (OGT), which adds the sugar, and β-N-acetylglucosaminidase (O-GlcNAcase), which hydrolyzes it, the targeting of these enzymes is highly specific and is controlled by myriad interacting subunits.
21045127	4	28	theme	immunological	726:738	arg1	approaches					754:763	multiple specific immunological and enzymatic approaches	708:763	multiple specific immunological and enzymatic approaches	708:763	Here, we demonstrate by multiple specific immunological and enzymatic approaches that histones, the proteins that package DNA within the nucleus, are O-GlcNAcylated in vivo.
21045127	1	29	theme	proteins	158:165	arg1	threonine					118:126	threonine	118:126	threonine	118:126	Dynamic posttranslational modification of serine and threonine residues of nucleocytoplasmic proteins by β-N-acetylglucosamine (O-GlcNAc) is a regulator of cellular processes such as transcription, signaling, and protein-protein interactions.
21045127	1	29	theme	proteins	158:165	arg1	serine					107:112	serine	107:112	serine	107:112	Dynamic posttranslational modification of serine and threonine residues of nucleocytoplasmic proteins by β-N-acetylglucosamine (O-GlcNAc) is a regulator of cellular processes such as transcription, signaling, and protein-protein interactions.
21045127	2	30	theme	stimuli	379:385	arg1	variety					368:374	a wide variety	361:374	a wide variety of stimuli	361:385	Like phosphorylation, O-GlcNAc cycles in response to a wide variety of stimuli.
21045127	2	30	theme	stimuli	379:385	arg1	stimuli					379:385	stimuli	379:385	stimuli	379:385	Like phosphorylation, O-GlcNAc cycles in response to a wide variety of stimuli.
21045127	6	31	theme	mass	967:970	arg1	spectrometry					972:983	mass spectrometry	967:983	mass spectrometry	967:983	We identify O-GlcNAc sites on histones H2A, H2B, and H4 using mass spectrometry.
21045127	0	32	theme	histone	51:57	arg1	part					39:42	part	39:42	part of the histone code	39:62	Beta-N-acetylglucosamine (O-GlcNAc) is part of the histone code.
21045127	1	33	dep	serine	107:112	arg1	residues					128:135	residues	128:135	residues	128:135	Dynamic posttranslational modification of serine and threonine residues of nucleocytoplasmic proteins by β-N-acetylglucosamine (O-GlcNAc) is a regulator of cellular processes such as transcription, signaling, and protein-protein interactions.
10861210	12	0	theme	human	1640:1644	arg1	AE1					1646:1648	human AE1	1640:1648	human AE1	1640:1648	The results show that the oligosaccharide attached to the endogenous site in extracellular loop 4 in human AE1 is not processed in HEK-293 or COS-7 cells, while the oligosaccharide attached to the preceding loop is converted into the complex form.
10861210	0	1	link	N-linked	14:21	arg1	oligosaccharide					23:37	N-linked oligosaccharide	14:37	N-linked oligosaccharide	14:37	Processing of N-linked oligosaccharide depends on its location in the anion exchanger, AE1, membrane glycoprotein.
10861210	1	2	dep	AE2	339:341	arg1	AE1					358:360	AE1	358:360	AE1	358:360	The human erythrocyte anion exchanger (AE)1 (Band 3) contains a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop.
10861210	12	3	theme	extracellular	1616:1628	arg1	loop					1630:1633	extracellular loop 4	1616:1635	extracellular loop 4	1616:1635	The results show that the oligosaccharide attached to the endogenous site in extracellular loop 4 in human AE1 is not processed in HEK-293 or COS-7 cells, while the oligosaccharide attached to the preceding loop is converted into the complex form.
10861210	10	4	theme	complex	1464:1470	arg1	form					1472:1475	the complex form	1460:1475	the complex form of the N555 mutant	1460:1494	The turnover of the complex form of the N555 mutant occurred with a half-life of approx.
10861210	1	5	from	Asn	239:241	arg1	loop					276:279	the fourth extracellular loop	251:279	the fourth extracellular loop of this polytopic membrane protein	251:314	The human erythrocyte anion exchanger (AE)1 (Band 3) contains a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop.
10861210	3	6	theme	biotinylation	650:662	arg1	assays					664:669	biotinylation assays	650:669	biotinylation assays	650:669	The lack of oligosaccharide processing was not due to retention of AE1 in the endoplasmic reticulum since biotinylation assays showed that approx.
10861210	12	7	theme	complex	1773:1779	arg1	form					1781:1784	the complex form	1769:1784	the complex form	1769:1784	The results show that the oligosaccharide attached to the endogenous site in extracellular loop 4 in human AE1 is not processed in HEK-293 or COS-7 cells, while the oligosaccharide attached to the preceding loop is converted into the complex form.
10861210	2	8	theme	embryonic	460:468	arg1	HEK					478:480	transfected human embryonic kidney (HEK)-293 or COS-7 cells	442:500	HEK	478:480	Human AE1 expressed in transfected human embryonic kidney (HEK)-293 or COS-7 cells contained a high-mannose oligosaccharide.
10861210	12	9	from	site	1608:1611	arg1	AE1					1646:1648	human AE1	1640:1648	human AE1	1640:1648	The results show that the oligosaccharide attached to the endogenous site in extracellular loop 4 in human AE1 is not processed in HEK-293 or COS-7 cells, while the oligosaccharide attached to the preceding loop is converted into the complex form.
10861210	12	9	from	site	1608:1611	arg1	loop					1630:1633	extracellular loop 4	1616:1635	extracellular loop 4	1616:1635	The results show that the oligosaccharide attached to the endogenous site in extracellular loop 4 in human AE1 is not processed in HEK-293 or COS-7 cells, while the oligosaccharide attached to the preceding loop is converted into the complex form.
10861210	5	10	dep	oligosaccharide	881:895	arg1	the					877:879	the	877:879	the	877:879	Moving the N-glycosylation site to the preceding extracellular loop in an AE1 glycosylation mutant (N555) resulted in processing of the oligosaccharide and production of a complex form of AE1.
10861210	10	11	theme	N555	1484:1487	arg1	mutant					1489:1494	the N555 mutant	1480:1494	the N555 mutant	1480:1494	The turnover of the complex form of the N555 mutant occurred with a half-life of approx.
10861210	7	12	theme	complex	1053:1059	arg1	form					1061:1064	The complex form	1049:1064	The complex form of the N555 mutant	1049:1083	The complex form of the N555 mutant could be biotinylated showing that this form of the glycoprotein was at the cell surface.
10861210	9	13	theme	time	1355:1358	arg1	course					1360:1365	the time course	1351:1365	the time course of trafficking of AE1 from the endoplasmic reticulum to the plasma membrane	1351:1441	4 h, which reflected the time course of trafficking of AE1 from the endoplasmic reticulum to the plasma membrane.
10861210	5	14	theme	AE1	933:935	arg1	form					925:928	a complex form	915:928	a complex form of AE1	915:935	Moving the N-glycosylation site to the preceding extracellular loop in an AE1 glycosylation mutant (N555) resulted in processing of the oligosaccharide and production of a complex form of AE1.
10861210	5	15	theme	AE1	819:821	arg1	N555					845:848	N555	845:848	N555	845:848	Moving the N-glycosylation site to the preceding extracellular loop in an AE1 glycosylation mutant (N555) resulted in processing of the oligosaccharide and production of a complex form of AE1.
10861210	5	15	theme	AE1	819:821	arg1	mutant					837:842	an AE1 glycosylation mutant	816:842	an AE1 glycosylation mutant (N555)	816:849	Moving the N-glycosylation site to the preceding extracellular loop in an AE1 glycosylation mutant (N555) resulted in processing of the oligosaccharide and production of a complex form of AE1.
10861210	6	16	contain	contained	982:990	arg1	mutant					963:968	A double N-glycosylation mutant	938:968	A double N-glycosylation mutant (N555/N642)	938:980	A double N-glycosylation mutant (N555/N642) contained both a high-mannose and a complex oligosaccharide chain.
10861210	6	16	contain	contained	982:990	arg2	high-mannose					999:1010	a high-mannose	997:1010	a high-mannose	997:1010	A double N-glycosylation mutant (N555/N642) contained both a high-mannose and a complex oligosaccharide chain.
10861210	6	16	contain	contained	982:990	arg2	chain					1042:1046	a complex oligosaccharide chain	1016:1046	a complex oligosaccharide chain	1016:1046	A double N-glycosylation mutant (N555/N642) contained both a high-mannose and a complex oligosaccharide chain.
10861210	6	16	contain	contained	982:990	arg1	N555/N642					971:979	N555/N642	971:979	N555/N642	971:979	A double N-glycosylation mutant (N555/N642) contained both a high-mannose and a complex oligosaccharide chain.
10861210	1	17	theme	human	119:123	arg1	exchanger					143:151	The human erythrocyte anion exchanger (AE)1	115:157	The human erythrocyte anion exchanger (AE)1 (Band 3)	115:166	The human erythrocyte anion exchanger (AE)1 (Band 3) contains a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop.
10861210	1	17	theme	human	119:123	arg1	Band					160:163	Band 3	160:165	Band 3	160:165	The human erythrocyte anion exchanger (AE)1 (Band 3) contains a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop.
10861210	5	18	theme	glycosylation	823:835	arg1	N555					845:848	N555	845:848	N555	845:848	Moving the N-glycosylation site to the preceding extracellular loop in an AE1 glycosylation mutant (N555) resulted in processing of the oligosaccharide and production of a complex form of AE1.
10861210	5	18	theme	glycosylation	823:835	arg1	mutant					837:842	an AE1 glycosylation mutant	816:842	an AE1 glycosylation mutant (N555)	816:849	Moving the N-glycosylation site to the preceding extracellular loop in an AE1 glycosylation mutant (N555) resulted in processing of the oligosaccharide and production of a complex form of AE1.
10861210	2	19	theme	Human	419:423	arg1	AE1					425:427	Human AE1	419:427	Human AE1 expressed in transfected human embryonic kidney (HEK)-293 or COS-7 cells	419:500	Human AE1 expressed in transfected human embryonic kidney (HEK)-293 or COS-7 cells contained a high-mannose oligosaccharide.
10861210	1	20	theme	extracellular	262:274	arg1	loop					276:279	the fourth extracellular loop	251:279	the fourth extracellular loop of this polytopic membrane protein	251:314	The human erythrocyte anion exchanger (AE)1 (Band 3) contains a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop.
10861210	5	21	theme	extracellular	794:806	arg1	loop					808:811	the preceding extracellular loop	780:811	the preceding extracellular loop in an AE1 glycosylation mutant (N555)	780:849	Moving the N-glycosylation site to the preceding extracellular loop in an AE1 glycosylation mutant (N555) resulted in processing of the oligosaccharide and production of a complex form of AE1.
10861210	8	22	theme	N555	1215:1218	arg1	mutant					1220:1225	the N555 mutant	1211:1225	the N555 mutant	1211:1225	Pulse-chase experiments showed that the N555 mutant was efficiently converted from a high-mannose to a complex oligosaccharide with a half-time of approx.
10861210	12	23	attach	attached	1581:1588	arg2	oligosaccharide					1565:1579	the oligosaccharide	1561:1579	the oligosaccharide attached to the endogenous site in extracellular loop 4 in human AE1	1561:1648	The results show that the oligosaccharide attached to the endogenous site in extracellular loop 4 in human AE1 is not processed in HEK-293 or COS-7 cells, while the oligosaccharide attached to the preceding loop is converted into the complex form.
10861210	12	23	attach	attached	1581:1588	arg1	site					1608:1611	the endogenous site	1593:1611	the endogenous site in extracellular loop 4 in human AE1	1593:1648	The results show that the oligosaccharide attached to the endogenous site in extracellular loop 4 in human AE1 is not processed in HEK-293 or COS-7 cells, while the oligosaccharide attached to the preceding loop is converted into the complex form.
10861210	0	24	theme	anion	70:74	arg1	AE1					87:89	AE1	87:89	AE1	87:89	Processing of N-linked oligosaccharide depends on its location in the anion exchanger, AE1, membrane glycoprotein.
10861210	0	24	theme	anion	70:74	arg1	glycoprotein					101:112	membrane glycoprotein	92:112	membrane glycoprotein	92:112	Processing of N-linked oligosaccharide depends on its location in the anion exchanger, AE1, membrane glycoprotein.
10861210	0	24	theme	anion	70:74	arg1	exchanger					76:84	the anion exchanger	66:84	the anion exchanger	66:84	Processing of N-linked oligosaccharide depends on its location in the anion exchanger, AE1, membrane glycoprotein.
10861210	3	25	dep	showed	671:676	arg1	approx					683:688	approx	683:688	approx	683:688	The lack of oligosaccharide processing was not due to retention of AE1 in the endoplasmic reticulum since biotinylation assays showed that approx.
10861210	5	26	from	loop	808:811	arg1	N555					845:848	N555	845:848	N555	845:848	Moving the N-glycosylation site to the preceding extracellular loop in an AE1 glycosylation mutant (N555) resulted in processing of the oligosaccharide and production of a complex form of AE1.
10861210	5	26	from	loop	808:811	arg1	mutant					837:842	an AE1 glycosylation mutant	816:842	an AE1 glycosylation mutant (N555)	816:849	Moving the N-glycosylation site to the preceding extracellular loop in an AE1 glycosylation mutant (N555) resulted in processing of the oligosaccharide and production of a complex form of AE1.
10861210	9	27	theme	endoplasmic	1398:1408	arg1	reticulum					1410:1418	the endoplasmic reticulum	1394:1418	the endoplasmic reticulum	1394:1418	4 h, which reflected the time course of trafficking of AE1 from the endoplasmic reticulum to the plasma membrane.
10861210	9	28	from	reticulum	1410:1418	arg1	trafficking					1370:1380	trafficking	1370:1380	trafficking of AE1 from the endoplasmic reticulum to the plasma membrane	1370:1441	4 h, which reflected the time course of trafficking of AE1 from the endoplasmic reticulum to the plasma membrane.
10861210	9	28	from	reticulum	1410:1418	arg1	course					1360:1365	the time course	1351:1365	the time course of trafficking of AE1 from the endoplasmic reticulum to the plasma membrane	1351:1441	4 h, which reflected the time course of trafficking of AE1 from the endoplasmic reticulum to the plasma membrane.
10861210	1	29	gly	N-glycosylated	367:380	arg1	isoforms					329:336	other isoforms	323:336	other isoforms (AE2, AE3 and trout AE1)	323:361	The human erythrocyte anion exchanger (AE)1 (Band 3) contains a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop.
10861210	1	29	gly	N-glycosylated	367:380	arg1	trout					352:356	trout	352:356	trout	352:356	The human erythrocyte anion exchanger (AE)1 (Band 3) contains a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop.
10861210	1	29	gly	N-glycosylated	367:380	arg2	AE3					344:346	AE3	344:346	AE3	344:346	The human erythrocyte anion exchanger (AE)1 (Band 3) contains a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop.
10861210	1	29	gly	N-glycosylated	367:380	arg1	loop					413:416	the preceding extracellular loop	385:416	the preceding extracellular loop	385:416	The human erythrocyte anion exchanger (AE)1 (Band 3) contains a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop.
10861210	1	29	gly	N-glycosylated	367:380	arg1	AE2					339:341	AE2	339:341	AE2	339:341	The human erythrocyte anion exchanger (AE)1 (Band 3) contains a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop.
10861210	1	29	gly	N-glycosylated	367:380	arg1	AE3					344:346	AE3	344:346	AE3	344:346	The human erythrocyte anion exchanger (AE)1 (Band 3) contains a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop.
10861210	1	29	gly	N-glycosylated	367:380	arg2	isoforms					329:336	other isoforms	323:336	other isoforms (AE2, AE3 and trout AE1)	323:361	The human erythrocyte anion exchanger (AE)1 (Band 3) contains a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop.
10861210	1	29	gly	N-glycosylated	367:380	arg2	trout					352:356	trout	352:356	trout	352:356	The human erythrocyte anion exchanger (AE)1 (Band 3) contains a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop.
10861210	1	29	gly	N-glycosylated	367:380	arg2	AE2					339:341	AE2	339:341	AE2	339:341	The human erythrocyte anion exchanger (AE)1 (Band 3) contains a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop.
10861210	1	29	gly	N-glycosylated	367:380	arg2	loop					413:416	the preceding extracellular loop	385:416	the preceding extracellular loop	385:416	The human erythrocyte anion exchanger (AE)1 (Band 3) contains a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop.
10861210	2	30	theme	transfected	442:452	arg1	HEK					478:480	transfected human embryonic kidney (HEK)-293 or COS-7 cells	442:500	HEK	478:480	Human AE1 expressed in transfected human embryonic kidney (HEK)-293 or COS-7 cells contained a high-mannose oligosaccharide.
10861210	1	31	theme	polytopic	289:297	arg1	protein					308:314	this polytopic membrane protein	284:314	this polytopic membrane protein	284:314	The human erythrocyte anion exchanger (AE)1 (Band 3) contains a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop.
10861210	7	32	theme	mutant	1078:1083	arg1	form					1061:1064	The complex form	1049:1064	The complex form of the N555 mutant	1049:1083	The complex form of the N555 mutant could be biotinylated showing that this form of the glycoprotein was at the cell surface.
10861210	1	33	theme	protein	308:314	arg1	loop					276:279	the fourth extracellular loop	251:279	the fourth extracellular loop of this polytopic membrane protein	251:314	The human erythrocyte anion exchanger (AE)1 (Band 3) contains a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop.
10861210	9	34	theme	plasma	1427:1432	arg1	membrane					1434:1441	the plasma membrane	1423:1441	the plasma membrane	1423:1441	4 h, which reflected the time course of trafficking of AE1 from the endoplasmic reticulum to the plasma membrane.
10861210	6	35	theme	N-glycosylation	947:961	arg1	mutant					963:968	A double N-glycosylation mutant	938:968	A double N-glycosylation mutant (N555/N642)	938:980	A double N-glycosylation mutant (N555/N642) contained both a high-mannose and a complex oligosaccharide chain.
10861210	6	35	theme	N-glycosylation	947:961	arg1	N555/N642					971:979	N555/N642	971:979	N555/N642	971:979	A double N-glycosylation mutant (N555/N642) contained both a high-mannose and a complex oligosaccharide chain.
10861210	12	36	attach	attached	1720:1727	arg2	oligosaccharide					1704:1718	the oligosaccharide	1700:1718	the oligosaccharide attached to the preceding loop	1700:1749	The results show that the oligosaccharide attached to the endogenous site in extracellular loop 4 in human AE1 is not processed in HEK-293 or COS-7 cells, while the oligosaccharide attached to the preceding loop is converted into the complex form.
10861210	12	36	attach	attached	1720:1727	arg1	loop					1746:1749	the preceding loop	1732:1749	the preceding loop	1732:1749	The results show that the oligosaccharide attached to the endogenous site in extracellular loop 4 in human AE1 is not processed in HEK-293 or COS-7 cells, while the oligosaccharide attached to the preceding loop is converted into the complex form.
10861210	0	37	theme	N-linked	14:21	arg1	oligosaccharide					23:37	N-linked oligosaccharide	14:37	N-linked oligosaccharide	14:37	Processing of N-linked oligosaccharide depends on its location in the anion exchanger, AE1, membrane glycoprotein.
10861210	9	38	theme	AE1	1385:1387	arg1	trafficking					1370:1380	trafficking	1370:1380	trafficking of AE1 from the endoplasmic reticulum to the plasma membrane	1370:1441	4 h, which reflected the time course of trafficking of AE1 from the endoplasmic reticulum to the plasma membrane.
10861210	3	39	theme	processing	572:581	arg1	lack					548:551	The lack	544:551	The lack of oligosaccharide processing	544:581	The lack of oligosaccharide processing was not due to retention of AE1 in the endoplasmic reticulum since biotinylation assays showed that approx.
10861210	3	39	theme	processing	572:581	arg1	due					591:593	due	591:593	due	591:593	The lack of oligosaccharide processing was not due to retention of AE1 in the endoplasmic reticulum since biotinylation assays showed that approx.
10861210	8	40	theme	complex	1278:1284	arg1	oligosaccharide					1286:1300	a complex oligosaccharide	1276:1300	a complex oligosaccharide with a half-time of approx	1276:1327	Pulse-chase experiments showed that the N555 mutant was efficiently converted from a high-mannose to a complex oligosaccharide with a half-time of approx.
10861210	10	41	theme	approx	1525:1530	arg1	half-life					1512:1520	a half-life	1510:1520	a half-life of approx	1510:1530	The turnover of the complex form of the N555 mutant occurred with a half-life of approx.
10861210	5	42	theme	complex	917:923	arg1	form					925:928	a complex form	915:928	a complex form of AE1	915:935	Moving the N-glycosylation site to the preceding extracellular loop in an AE1 glycosylation mutant (N555) resulted in processing of the oligosaccharide and production of a complex form of AE1.
10861210	4	43	theme	cell	731:734	arg1	surface					736:742	the cell surface	727:742	the cell surface	727:742	30% of the protein was expressed at the cell surface.
10861210	12	44	theme	HEK-293	1670:1676	arg1	cells					1687:1691	HEK-293 or COS-7 cells	1670:1691	cells	1687:1691	The results show that the oligosaccharide attached to the endogenous site in extracellular loop 4 in human AE1 is not processed in HEK-293 or COS-7 cells, while the oligosaccharide attached to the preceding loop is converted into the complex form.
10861210	7	45	theme	cell	1161:1164	arg1	surface					1166:1172	the cell surface	1157:1172	the cell surface	1157:1172	The complex form of the N555 mutant could be biotinylated showing that this form of the glycoprotein was at the cell surface.
10861210	12	46	theme	COS-7	1681:1685	arg1	cells					1687:1691	HEK-293 or COS-7 cells	1670:1691	cells	1687:1691	The results show that the oligosaccharide attached to the endogenous site in extracellular loop 4 in human AE1 is not processed in HEK-293 or COS-7 cells, while the oligosaccharide attached to the preceding loop is converted into the complex form.
10861210	1	47	theme	anion	137:141	arg1	exchanger					143:151	The human erythrocyte anion exchanger (AE)1	115:157	The human erythrocyte anion exchanger (AE)1 (Band 3)	115:166	The human erythrocyte anion exchanger (AE)1 (Band 3) contains a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop.
10861210	1	47	theme	anion	137:141	arg1	Band					160:163	Band 3	160:165	Band 3	160:165	The human erythrocyte anion exchanger (AE)1 (Band 3) contains a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop.
10861210	8	48	theme	approx	1322:1327	arg1	half-time					1309:1317	a half-time	1307:1317	a half-time of approx	1307:1327	Pulse-chase experiments showed that the N555 mutant was efficiently converted from a high-mannose to a complex oligosaccharide with a half-time of approx.
10861210	1	49	theme	complex	186:192	arg1	oligosaccharide					203:217	a single complex N-linked oligosaccharide	177:217	a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop	177:416	The human erythrocyte anion exchanger (AE)1 (Band 3) contains a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop.
10861210	7	50	theme	glycoprotein	1137:1148	arg1	form					1125:1128	this form	1120:1128	this form of the glycoprotein	1120:1148	The complex form of the N555 mutant could be biotinylated showing that this form of the glycoprotein was at the cell surface.
10861210	5	51	gly	N-glycosylation	756:770	arg2	site					772:775	the N-glycosylation site	752:775	the N-glycosylation site	752:775	Moving the N-glycosylation site to the preceding extracellular loop in an AE1 glycosylation mutant (N555) resulted in processing of the oligosaccharide and production of a complex form of AE1.
10861210	2	52	theme	COS-7	490:494	arg1	cells					496:500	transfected human embryonic kidney (HEK)-293 or COS-7 cells	442:500	cells	496:500	Human AE1 expressed in transfected human embryonic kidney (HEK)-293 or COS-7 cells contained a high-mannose oligosaccharide.
10861210	5	53	theme	N-glycosylation	756:770	arg1	site					772:775	the N-glycosylation site	752:775	the N-glycosylation site	752:775	Moving the N-glycosylation site to the preceding extracellular loop in an AE1 glycosylation mutant (N555) resulted in processing of the oligosaccharide and production of a complex form of AE1.
10861210	10	54	theme	form	1472:1475	arg1	turnover					1448:1455	The turnover	1444:1455	The turnover of the complex form of the N555 mutant	1444:1494	The turnover of the complex form of the N555 mutant occurred with a half-life of approx.
10861210	3	55	theme	endoplasmic	622:632	arg1	reticulum					634:642	the endoplasmic reticulum	618:642	the endoplasmic reticulum	618:642	The lack of oligosaccharide processing was not due to retention of AE1 in the endoplasmic reticulum since biotinylation assays showed that approx.
10861210	1	56	link	N-linked	194:201	arg1	oligosaccharide					203:217	a single complex N-linked oligosaccharide	177:217	a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop	177:416	The human erythrocyte anion exchanger (AE)1 (Band 3) contains a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop.
10861210	2	57	theme	high-mannose	514:525	arg1	oligosaccharide					527:541	a high-mannose oligosaccharide	512:541	a high-mannose oligosaccharide	512:541	Human AE1 expressed in transfected human embryonic kidney (HEK)-293 or COS-7 cells contained a high-mannose oligosaccharide.
10861210	9	58	from	course	1360:1365	arg1	reticulum					1410:1418	the endoplasmic reticulum	1394:1418	the endoplasmic reticulum	1394:1418	4 h, which reflected the time course of trafficking of AE1 from the endoplasmic reticulum to the plasma membrane.
10861210	8	59	with	oligosaccharide	1286:1300	arg1	half-time					1309:1317	a half-time	1307:1317	a half-time of approx	1307:1327	Pulse-chase experiments showed that the N555 mutant was efficiently converted from a high-mannose to a complex oligosaccharide with a half-time of approx.
10861210	1	60	theme	preceding	389:397	arg1	loop					413:416	the preceding extracellular loop	385:416	the preceding extracellular loop	385:416	The human erythrocyte anion exchanger (AE)1 (Band 3) contains a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop.
10861210	2	61	theme	kidney	470:475	arg1	HEK					478:480	transfected human embryonic kidney (HEK)-293 or COS-7 cells	442:500	HEK	478:480	Human AE1 expressed in transfected human embryonic kidney (HEK)-293 or COS-7 cells contained a high-mannose oligosaccharide.
10861210	6	62	theme	oligosaccharide	1026:1040	arg1	chain					1042:1046	a complex oligosaccharide chain	1016:1046	a complex oligosaccharide chain	1016:1046	A double N-glycosylation mutant (N555/N642) contained both a high-mannose and a complex oligosaccharide chain.
10861210	1	63	theme	erythrocyte	125:135	arg1	exchanger					143:151	The human erythrocyte anion exchanger (AE)1	115:157	The human erythrocyte anion exchanger (AE)1 (Band 3)	115:166	The human erythrocyte anion exchanger (AE)1 (Band 3) contains a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop.
10861210	1	63	theme	erythrocyte	125:135	arg1	Band					160:163	Band 3	160:165	Band 3	160:165	The human erythrocyte anion exchanger (AE)1 (Band 3) contains a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop.
10861210	10	64	theme	mutant	1489:1494	arg1	form					1472:1475	the complex form	1460:1475	the complex form of the N555 mutant	1460:1494	The turnover of the complex form of the N555 mutant occurred with a half-life of approx.
10861210	1	65	theme	other	323:327	arg1	isoforms					329:336	other isoforms	323:336	other isoforms (AE2, AE3 and trout AE1)	323:361	The human erythrocyte anion exchanger (AE)1 (Band 3) contains a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop.
10861210	1	65	theme	other	323:327	arg1	trout					352:356	trout	352:356	trout	352:356	The human erythrocyte anion exchanger (AE)1 (Band 3) contains a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop.
10861210	1	65	theme	other	323:327	arg1	AE3					344:346	AE3	344:346	AE3	344:346	The human erythrocyte anion exchanger (AE)1 (Band 3) contains a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop.
10861210	1	65	theme	other	323:327	arg1	AE2					339:341	AE2	339:341	AE2	339:341	The human erythrocyte anion exchanger (AE)1 (Band 3) contains a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop.
10861210	2	66	theme	human	454:458	arg1	HEK					478:480	transfected human embryonic kidney (HEK)-293 or COS-7 cells	442:500	HEK	478:480	Human AE1 expressed in transfected human embryonic kidney (HEK)-293 or COS-7 cells contained a high-mannose oligosaccharide.
10861210	0	67	gly	glycoprotein	101:112	arg1	glycoprotein					101:112	membrane glycoprotein	92:112	membrane glycoprotein	92:112	Processing of N-linked oligosaccharide depends on its location in the anion exchanger, AE1, membrane glycoprotein.
10861210	0	67	gly	glycoprotein	101:112	arg1	exchanger					76:84	the anion exchanger	66:84	the anion exchanger	66:84	Processing of N-linked oligosaccharide depends on its location in the anion exchanger, AE1, membrane glycoprotein.
10861210	9	68	theme	trafficking	1370:1380	arg1	course					1360:1365	the time course	1351:1365	the time course of trafficking of AE1 from the endoplasmic reticulum to the plasma membrane	1351:1441	4 h, which reflected the time course of trafficking of AE1 from the endoplasmic reticulum to the plasma membrane.
10861210	8	69	theme	Pulse-chase	1175:1185	arg1	experiments					1187:1197	Pulse-chase experiments	1175:1197	Pulse-chase experiments	1175:1197	Pulse-chase experiments showed that the N555 mutant was efficiently converted from a high-mannose to a complex oligosaccharide with a half-time of approx.
10861210	2	70	contain	contained	502:510	arg2	oligosaccharide					527:541	a high-mannose oligosaccharide	512:541	a high-mannose oligosaccharide	512:541	Human AE1 expressed in transfected human embryonic kidney (HEK)-293 or COS-7 cells contained a high-mannose oligosaccharide.
10861210	2	70	contain	contained	502:510	arg1	AE1					425:427	Human AE1	419:427	Human AE1 expressed in transfected human embryonic kidney (HEK)-293 or COS-7 cells	419:500	Human AE1 expressed in transfected human embryonic kidney (HEK)-293 or COS-7 cells contained a high-mannose oligosaccharide.
10861210	1	71	attach	attached	227:234	arg2	oligosaccharide					203:217	a single complex N-linked oligosaccharide	177:217	a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop	177:416	The human erythrocyte anion exchanger (AE)1 (Band 3) contains a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop.
10861210	1	71	attach	attached	227:234	arg1	Asn					239:241	Asn(642)	239:246	Asn(642) in the fourth extracellular loop of this polytopic membrane protein	239:314	The human erythrocyte anion exchanger (AE)1 (Band 3) contains a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop.
10861210	5	72	theme	preceding	784:792	arg1	loop					808:811	the preceding extracellular loop	780:811	the preceding extracellular loop in an AE1 glycosylation mutant (N555)	780:849	Moving the N-glycosylation site to the preceding extracellular loop in an AE1 glycosylation mutant (N555) resulted in processing of the oligosaccharide and production of a complex form of AE1.
10861210	12	73	theme	endogenous	1597:1606	arg1	site					1608:1611	the endogenous site	1593:1611	the endogenous site in extracellular loop 4 in human AE1	1593:1648	The results show that the oligosaccharide attached to the endogenous site in extracellular loop 4 in human AE1 is not processed in HEK-293 or COS-7 cells, while the oligosaccharide attached to the preceding loop is converted into the complex form.
10861210	0	74	from	location	54:61	arg1	AE1					87:89	AE1	87:89	AE1	87:89	Processing of N-linked oligosaccharide depends on its location in the anion exchanger, AE1, membrane glycoprotein.
10861210	0	74	from	location	54:61	arg1	glycoprotein					101:112	membrane glycoprotein	92:112	membrane glycoprotein	92:112	Processing of N-linked oligosaccharide depends on its location in the anion exchanger, AE1, membrane glycoprotein.
10861210	0	74	from	location	54:61	arg1	exchanger					76:84	the anion exchanger	66:84	the anion exchanger	66:84	Processing of N-linked oligosaccharide depends on its location in the anion exchanger, AE1, membrane glycoprotein.
10861210	0	75	theme	membrane	92:99	arg1	glycoprotein					101:112	membrane glycoprotein	92:112	membrane glycoprotein	92:112	Processing of N-linked oligosaccharide depends on its location in the anion exchanger, AE1, membrane glycoprotein.
10861210	0	75	theme	membrane	92:99	arg1	exchanger					76:84	the anion exchanger	66:84	the anion exchanger	66:84	Processing of N-linked oligosaccharide depends on its location in the anion exchanger, AE1, membrane glycoprotein.
10861210	1	76	theme	membrane	299:306	arg1	protein					308:314	this polytopic membrane protein	284:314	this polytopic membrane protein	284:314	The human erythrocyte anion exchanger (AE)1 (Band 3) contains a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop.
10861210	3	77	from	retention	598:606	arg1	reticulum					634:642	the endoplasmic reticulum	618:642	the endoplasmic reticulum	618:642	The lack of oligosaccharide processing was not due to retention of AE1 in the endoplasmic reticulum since biotinylation assays showed that approx.
10861210	7	78	theme	N555	1073:1076	arg1	mutant					1078:1083	the N555 mutant	1069:1083	the N555 mutant	1069:1083	The complex form of the N555 mutant could be biotinylated showing that this form of the glycoprotein was at the cell surface.
10861210	12	79	theme	preceding	1736:1744	arg1	loop					1746:1749	the preceding loop	1732:1749	the preceding loop	1732:1749	The results show that the oligosaccharide attached to the endogenous site in extracellular loop 4 in human AE1 is not processed in HEK-293 or COS-7 cells, while the oligosaccharide attached to the preceding loop is converted into the complex form.
10861210	0	80	theme	oligosaccharide	23:37	arg1	Processing					0:9	Processing	0:9	Processing of N-linked oligosaccharide	0:37	Processing of N-linked oligosaccharide depends on its location in the anion exchanger, AE1, membrane glycoprotein.
10861210	7	81	gly	glycoprotein	1137:1148	arg1	glycoprotein					1137:1148	the glycoprotein	1133:1148	the glycoprotein	1133:1148	The complex form of the N555 mutant could be biotinylated showing that this form of the glycoprotein was at the cell surface.
10861210	6	82	theme	double	940:945	arg1	mutant					963:968	A double N-glycosylation mutant	938:968	A double N-glycosylation mutant (N555/N642)	938:980	A double N-glycosylation mutant (N555/N642) contained both a high-mannose and a complex oligosaccharide chain.
10861210	6	82	theme	double	940:945	arg1	N555/N642					971:979	N555/N642	971:979	N555/N642	971:979	A double N-glycosylation mutant (N555/N642) contained both a high-mannose and a complex oligosaccharide chain.
10861210	3	83	theme	oligosaccharide	556:570	arg1	processing					572:581	oligosaccharide processing	556:581	oligosaccharide processing	556:581	The lack of oligosaccharide processing was not due to retention of AE1 in the endoplasmic reticulum since biotinylation assays showed that approx.
10861210	1	84	theme	extracellular	399:411	arg1	loop					413:416	the preceding extracellular loop	385:416	the preceding extracellular loop	385:416	The human erythrocyte anion exchanger (AE)1 (Band 3) contains a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop.
10861210	5	85	theme	form	925:928	arg1	production					901:910	production	901:910	production	901:910	Moving the N-glycosylation site to the preceding extracellular loop in an AE1 glycosylation mutant (N555) resulted in processing of the oligosaccharide and production of a complex form of AE1.
10861210	5	85	theme	form	925:928	arg1	oligosaccharide					881:895	oligosaccharide	881:895	oligosaccharide	881:895	Moving the N-glycosylation site to the preceding extracellular loop in an AE1 glycosylation mutant (N555) resulted in processing of the oligosaccharide and production of a complex form of AE1.
10861210	6	86	theme	complex	1018:1024	arg1	chain					1042:1046	a complex oligosaccharide chain	1016:1046	a complex oligosaccharide chain	1016:1046	A double N-glycosylation mutant (N555/N642) contained both a high-mannose and a complex oligosaccharide chain.
10861210	1	87	contain	contains	168:175	arg1	exchanger					143:151	The human erythrocyte anion exchanger (AE)1	115:157	The human erythrocyte anion exchanger (AE)1 (Band 3)	115:166	The human erythrocyte anion exchanger (AE)1 (Band 3) contains a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop.
10861210	1	87	contain	contains	168:175	arg2	oligosaccharide					203:217	a single complex N-linked oligosaccharide	177:217	a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop	177:416	The human erythrocyte anion exchanger (AE)1 (Band 3) contains a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop.
10861210	1	87	contain	contains	168:175	arg1	Band					160:163	Band 3	160:165	Band 3	160:165	The human erythrocyte anion exchanger (AE)1 (Band 3) contains a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop.
10861210	1	88	theme	fourth	255:260	arg1	loop					276:279	the fourth extracellular loop	251:279	the fourth extracellular loop of this polytopic membrane protein	251:314	The human erythrocyte anion exchanger (AE)1 (Band 3) contains a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop.
10861210	5	89	theme	oligosaccharide	881:895	arg1	processing					863:872	processing	863:872	processing of the oligosaccharide and production of a complex form of AE1	863:935	Moving the N-glycosylation site to the preceding extracellular loop in an AE1 glycosylation mutant (N555) resulted in processing of the oligosaccharide and production of a complex form of AE1.
10861210	1	90	dep	isoforms	329:336	arg1	isoforms					329:336	other isoforms	323:336	other isoforms (AE2, AE3 and trout AE1)	323:361	The human erythrocyte anion exchanger (AE)1 (Band 3) contains a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop.
10861210	1	90	dep	isoforms	329:336	arg1	trout					352:356	trout	352:356	trout	352:356	The human erythrocyte anion exchanger (AE)1 (Band 3) contains a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop.
10861210	1	90	dep	isoforms	329:336	arg1	AE3					344:346	AE3	344:346	AE3	344:346	The human erythrocyte anion exchanger (AE)1 (Band 3) contains a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop.
10861210	1	90	dep	isoforms	329:336	arg1	AE2					339:341	AE2	339:341	AE2	339:341	The human erythrocyte anion exchanger (AE)1 (Band 3) contains a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop.
10861210	1	91	theme	single	179:184	arg1	oligosaccharide					203:217	a single complex N-linked oligosaccharide	177:217	a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop	177:416	The human erythrocyte anion exchanger (AE)1 (Band 3) contains a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop.
10861210	5	92	theme	production	901:910	arg1	processing					863:872	processing	863:872	processing of the oligosaccharide and production of a complex form of AE1	863:935	Moving the N-glycosylation site to the preceding extracellular loop in an AE1 glycosylation mutant (N555) resulted in processing of the oligosaccharide and production of a complex form of AE1.
10861210	3	93	theme	AE1	611:613	arg1	retention					598:606	retention	598:606	retention of AE1 in the endoplasmic reticulum	598:642	The lack of oligosaccharide processing was not due to retention of AE1 in the endoplasmic reticulum since biotinylation assays showed that approx.
10861210	4	94	theme	protein	702:708	arg1	protein					702:708	the protein	698:708	the protein	698:708	30% of the protein was expressed at the cell surface.
10861210	4	94	theme	protein	702:708	arg1	%					693:693	30%	691:693	30% of the protein	691:708	30% of the protein was expressed at the cell surface.
10861210	1	95	theme	N-linked	194:201	arg1	oligosaccharide					203:217	a single complex N-linked oligosaccharide	177:217	a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop	177:416	The human erythrocyte anion exchanger (AE)1 (Band 3) contains a single complex N-linked oligosaccharide that is attached to Asn(642) in the fourth extracellular loop of this polytopic membrane protein, while other isoforms (AE2, AE3 and trout AE1) are N-glycosylated on the preceding extracellular loop.
15373830	6	0	theme	wheat	868:872	arg1	agglutinin					879:888	wheat germ agglutinin	868:888	wheat germ agglutinin affinity purification	868:910	Nonglycosylated and glycosylated forms of full-length HIC1 proteins separated by wheat germ agglutinin affinity purification, displayed the same specific DNA-binding activity in electrophoretic mobility shift assays proving that the O-GlcNAc modification is not directly implicated in the specific DNA recognition of HIC1.
15373830	6	1	theme	HIC1	841:844	arg1	proteins					846:853	full-length HIC1 proteins	829:853	full-length HIC1 proteins separated by wheat germ agglutinin affinity purification	829:910	Nonglycosylated and glycosylated forms of full-length HIC1 proteins separated by wheat germ agglutinin affinity purification, displayed the same specific DNA-binding activity in electrophoretic mobility shift assays proving that the O-GlcNAc modification is not directly implicated in the specific DNA recognition of HIC1.
15373830	6	2	theme	O-GlcNAc	1020:1027	arg1	modification					1029:1040	the O-GlcNAc modification	1016:1040	the O-GlcNAc modification	1016:1040	Nonglycosylated and glycosylated forms of full-length HIC1 proteins separated by wheat germ agglutinin affinity purification, displayed the same specific DNA-binding activity in electrophoretic mobility shift assays proving that the O-GlcNAc modification is not directly implicated in the specific DNA recognition of HIC1.
15373830	10	3	theme	DNA-binding	1935:1945	arg1	activity					1947:1954	its specific DNA-binding activity	1922:1954	its specific DNA-binding activity	1922:1954	Thus, the O-GlcNAc modification of HIC1 does not affect its specific DNA-binding activity and is highly sensitive to conformational effects, notably its dimerization through the BTB/POZ domain.
15373830	2	4	mod	modified	335:342	arg1	proteins					322:329	full-length HIC1 proteins	305:329	full-length HIC1 proteins	305:329	Here, we demonstrate that full-length HIC1 proteins are modified both in vivo and in vitro with O-linked N-acetylglucosamine (O-GlcNAc).
15373830	2	4	mod	modified	335:342	arg3	N-acetylglucosamine					384:402	O-linked N-acetylglucosamine	375:402	O-linked N-acetylglucosamine (O-GlcNAc)	375:413	Here, we demonstrate that full-length HIC1 proteins are modified both in vivo and in vitro with O-linked N-acetylglucosamine (O-GlcNAc).
15373830	2	4	mod	modified	335:342	arg3	O-GlcNAc					405:412	O-GlcNAc	405:412	O-GlcNAc	405:412	Here, we demonstrate that full-length HIC1 proteins are modified both in vivo and in vitro with O-linked N-acetylglucosamine (O-GlcNAc).
15373830	9	5	from	domain	1825:1830	arg1	modified					1745:1752	modified	1745:1752	modified	1745:1752	Interestingly, these truncated proteins are O-GlcNAc modified in their C-terminal tail (residues 670-711) and not in the DNA-binding domain, as for the full-length proteins.
15373830	3	6	theme	eukaryotes	514:523	arg1	cytosolic					472:480	cytosolic	472:480	cytosolic	472:480	This is a highly dynamic glycosylation found within the cytosolic and the nuclear compartments of eukaryotes.
15373830	1	7	theme	Krüppel-like	164:175	arg1	H					181:181	Krüppel-like C(2)H(2)	164:184	five Krüppel-like C(2)H(2) zinc fingers	159:197	HIC1 (hypermethylated in cancer 1) is a transcriptional repressor containing five Krüppel-like C(2)H(2) zinc fingers and an N-terminal dimerization and autonomous repression domain called BTB/POZ.
15373830	6	8	theme	same	927:930	arg1	activity					953:960	the same specific DNA-binding activity	923:960	the same specific DNA-binding activity	923:960	Nonglycosylated and glycosylated forms of full-length HIC1 proteins separated by wheat germ agglutinin affinity purification, displayed the same specific DNA-binding activity in electrophoretic mobility shift assays proving that the O-GlcNAc modification is not directly implicated in the specific DNA recognition of HIC1.
15373830	4	9	theme	Gal-labeled	544:554	arg1	peptides					564:571	[(3)H]Gal-labeled tryptic peptides	538:571	[(3)H]Gal-labeled tryptic peptides	538:571	Analysis of [(3)H]Gal-labeled tryptic peptides indicates that HIC1 has three major sites for O-GlcNAc glycosylation.
15373830	5	10	theme	DNA-binding	767:777	arg1	domain					779:784	the DNA-binding domain	763:784	the DNA-binding domain	763:784	Using C-terminal deletion mutants, we have shown that O-GlcNAc modification of HIC1 proteins occurred preferentially in the DNA-binding domain.
15373830	4	11	theme	peptides	564:571	arg1	Analysis					526:533	Analysis	526:533	Analysis of [(3)H]Gal-labeled tryptic peptides	526:571	Analysis of [(3)H]Gal-labeled tryptic peptides indicates that HIC1 has three major sites for O-GlcNAc glycosylation.
15373830	9	12	dep	residues	1780:1787	arg1	670-711					1789:1795	670-711	1789:1795	670-711	1789:1795	Interestingly, these truncated proteins are O-GlcNAc modified in their C-terminal tail (residues 670-711) and not in the DNA-binding domain, as for the full-length proteins.
15373830	8	13	theme	DNA-binding	1479:1489	arg1	domain					1491:1496	only the DNA-binding domain	1470:1496	only the DNA-binding domain	1470:1496	Electrophoretic mobility shift assays performed with separated pools of glycosylated and unglycosylated forms of a construct exhibiting only the DNA-binding domain and the C-terminal tail of HIC1 (residues 399-714) and supershift experiments with wheat germ agglutinin or RL-2, an antibody raised against O-GlcNAc residues, fully corroborated these results.
15373830	8	13	theme	DNA-binding	1479:1489	arg1	HIC1					1525:1528	HIC1	1525:1528	HIC1	1525:1528	Electrophoretic mobility shift assays performed with separated pools of glycosylated and unglycosylated forms of a construct exhibiting only the DNA-binding domain and the C-terminal tail of HIC1 (residues 399-714) and supershift experiments with wheat germ agglutinin or RL-2, an antibody raised against O-GlcNAc residues, fully corroborated these results.
15373830	4	14	dep	H	542:542	arg1	3					540:540	3	540:540	3	540:540	Analysis of [(3)H]Gal-labeled tryptic peptides indicates that HIC1 has three major sites for O-GlcNAc glycosylation.
15373830	8	15	with	experiments	1564:1574	arg1	RL-2					1606:1609	RL-2	1606:1609	RL-2	1606:1609	Electrophoretic mobility shift assays performed with separated pools of glycosylated and unglycosylated forms of a construct exhibiting only the DNA-binding domain and the C-terminal tail of HIC1 (residues 399-714) and supershift experiments with wheat germ agglutinin or RL-2, an antibody raised against O-GlcNAc residues, fully corroborated these results.
15373830	8	15	with	experiments	1564:1574	arg1	antibody					1615:1622	an antibody	1612:1622	an antibody raised against O-GlcNAc residues	1612:1655	Electrophoretic mobility shift assays performed with separated pools of glycosylated and unglycosylated forms of a construct exhibiting only the DNA-binding domain and the C-terminal tail of HIC1 (residues 399-714) and supershift experiments with wheat germ agglutinin or RL-2, an antibody raised against O-GlcNAc residues, fully corroborated these results.
15373830	8	15	with	experiments	1564:1574	arg1	agglutinin					1592:1601	wheat germ agglutinin	1581:1601	wheat germ agglutinin	1581:1601	Electrophoretic mobility shift assays performed with separated pools of glycosylated and unglycosylated forms of a construct exhibiting only the DNA-binding domain and the C-terminal tail of HIC1 (residues 399-714) and supershift experiments with wheat germ agglutinin or RL-2, an antibody raised against O-GlcNAc residues, fully corroborated these results.
15373830	6	16	theme	agglutinin	879:888	arg1	purification					899:910	wheat germ agglutinin affinity purification	868:910	wheat germ agglutinin affinity purification	868:910	Nonglycosylated and glycosylated forms of full-length HIC1 proteins separated by wheat germ agglutinin affinity purification, displayed the same specific DNA-binding activity in electrophoretic mobility shift assays proving that the O-GlcNAc modification is not directly implicated in the specific DNA recognition of HIC1.
15373830	9	17	theme	C-terminal	1763:1772	arg1	residues					1780:1787	residues 670-711	1780:1795	residues 670-711	1780:1795	Interestingly, these truncated proteins are O-GlcNAc modified in their C-terminal tail (residues 670-711) and not in the DNA-binding domain, as for the full-length proteins.
15373830	9	17	theme	C-terminal	1763:1772	arg1	tail					1774:1777	their C-terminal tail	1757:1777	their C-terminal tail (residues 670-711)	1757:1796	Interestingly, these truncated proteins are O-GlcNAc modified in their C-terminal tail (residues 670-711) and not in the DNA-binding domain, as for the full-length proteins.
15373830	9	18	from	tail	1774:1777	arg1	modified					1745:1752	modified	1745:1752	modified	1745:1752	Interestingly, these truncated proteins are O-GlcNAc modified in their C-terminal tail (residues 670-711) and not in the DNA-binding domain, as for the full-length proteins.
15373830	8	19	theme	C-terminal	1506:1515	arg1	residues					1531:1538	residues 399-714	1531:1546	residues 399-714	1531:1546	Electrophoretic mobility shift assays performed with separated pools of glycosylated and unglycosylated forms of a construct exhibiting only the DNA-binding domain and the C-terminal tail of HIC1 (residues 399-714) and supershift experiments with wheat germ agglutinin or RL-2, an antibody raised against O-GlcNAc residues, fully corroborated these results.
15373830	8	19	theme	C-terminal	1506:1515	arg1	tail					1517:1520	the C-terminal tail	1502:1520	the C-terminal tail of HIC1 (residues 399-714)	1502:1547	Electrophoretic mobility shift assays performed with separated pools of glycosylated and unglycosylated forms of a construct exhibiting only the DNA-binding domain and the C-terminal tail of HIC1 (residues 399-714) and supershift experiments with wheat germ agglutinin or RL-2, an antibody raised against O-GlcNAc residues, fully corroborated these results.
15373830	1	20	dep	HIC1	82:85	arg1	hypermethylated					88:102	hypermethylated	88:102	hypermethylated in cancer 1	88:114	HIC1 (hypermethylated in cancer 1) is a transcriptional repressor containing five Krüppel-like C(2)H(2) zinc fingers and an N-terminal dimerization and autonomous repression domain called BTB/POZ.
15373830	6	21	theme	mobility	981:988	arg1	assays					996:1001	electrophoretic mobility shift assays	965:1001	electrophoretic mobility shift assays proving that the O-GlcNAc modification is not directly implicated in the specific DNA recognition of HIC1	965:1107	Nonglycosylated and glycosylated forms of full-length HIC1 proteins separated by wheat germ agglutinin affinity purification, displayed the same specific DNA-binding activity in electrophoretic mobility shift assays proving that the O-GlcNAc modification is not directly implicated in the specific DNA recognition of HIC1.
15373830	8	22	theme	Electrophoretic	1334:1348	arg1	assays					1365:1370	Electrophoretic mobility shift assays	1334:1370	Electrophoretic mobility shift assays performed with separated pools of glycosylated and unglycosylated forms of a construct exhibiting only the DNA-binding domain and the C-terminal tail of HIC1 (residues 399-714)	1334:1547	Electrophoretic mobility shift assays performed with separated pools of glycosylated and unglycosylated forms of a construct exhibiting only the DNA-binding domain and the C-terminal tail of HIC1 (residues 399-714) and supershift experiments with wheat germ agglutinin or RL-2, an antibody raised against O-GlcNAc residues, fully corroborated these results.
15373830	1	23	theme	transcriptional	122:136	arg1	repressor					138:146	a transcriptional repressor	120:146	a transcriptional repressor containing five Krüppel-like C(2)H(2) zinc fingers and an N-terminal dimerization and autonomous repression domain called BTB/POZ	120:276	HIC1 (hypermethylated in cancer 1) is a transcriptional repressor containing five Krüppel-like C(2)H(2) zinc fingers and an N-terminal dimerization and autonomous repression domain called BTB/POZ.
15373830	1	23	theme	transcriptional	122:136	arg1	HIC1					82:85	HIC1	82:85	HIC1 (hypermethylated in cancer 1)	82:115	HIC1 (hypermethylated in cancer 1) is a transcriptional repressor containing five Krüppel-like C(2)H(2) zinc fingers and an N-terminal dimerization and autonomous repression domain called BTB/POZ.
15373830	9	24	from	modified	1745:1752	arg1	residues					1780:1787	residues 670-711	1780:1795	residues 670-711	1780:1795	Interestingly, these truncated proteins are O-GlcNAc modified in their C-terminal tail (residues 670-711) and not in the DNA-binding domain, as for the full-length proteins.
15373830	9	24	from	modified	1745:1752	arg1	domain					1825:1830	the DNA-binding domain	1809:1830	the DNA-binding domain	1809:1830	Interestingly, these truncated proteins are O-GlcNAc modified in their C-terminal tail (residues 670-711) and not in the DNA-binding domain, as for the full-length proteins.
15373830	9	24	from	modified	1745:1752	arg1	tail					1774:1777	their C-terminal tail	1757:1777	their C-terminal tail (residues 670-711)	1757:1796	Interestingly, these truncated proteins are O-GlcNAc modified in their C-terminal tail (residues 670-711) and not in the DNA-binding domain, as for the full-length proteins.
15373830	8	25	theme	shift	1359:1363	arg1	assays					1365:1370	Electrophoretic mobility shift assays	1334:1370	Electrophoretic mobility shift assays performed with separated pools of glycosylated and unglycosylated forms of a construct exhibiting only the DNA-binding domain and the C-terminal tail of HIC1 (residues 399-714)	1334:1547	Electrophoretic mobility shift assays performed with separated pools of glycosylated and unglycosylated forms of a construct exhibiting only the DNA-binding domain and the C-terminal tail of HIC1 (residues 399-714) and supershift experiments with wheat germ agglutinin or RL-2, an antibody raised against O-GlcNAc residues, fully corroborated these results.
15373830	5	26	theme	deletion	660:667	arg1	mutants					669:675	C-terminal deletion mutants	649:675	C-terminal deletion mutants	649:675	Using C-terminal deletion mutants, we have shown that O-GlcNAc modification of HIC1 proteins occurred preferentially in the DNA-binding domain.
15373830	6	27	theme	DNA-binding	941:951	arg1	activity					953:960	the same specific DNA-binding activity	923:960	the same specific DNA-binding activity	923:960	Nonglycosylated and glycosylated forms of full-length HIC1 proteins separated by wheat germ agglutinin affinity purification, displayed the same specific DNA-binding activity in electrophoretic mobility shift assays proving that the O-GlcNAc modification is not directly implicated in the specific DNA recognition of HIC1.
15373830	2	28	link	O-linked	375:382	arg1	O-GlcNAc					405:412	O-GlcNAc	405:412	O-GlcNAc	405:412	Here, we demonstrate that full-length HIC1 proteins are modified both in vivo and in vitro with O-linked N-acetylglucosamine (O-GlcNAc).
15373830	2	28	link	O-linked	375:382	arg1	N-acetylglucosamine					384:402	O-linked N-acetylglucosamine	375:402	O-linked N-acetylglucosamine (O-GlcNAc)	375:413	Here, we demonstrate that full-length HIC1 proteins are modified both in vivo and in vitro with O-linked N-acetylglucosamine (O-GlcNAc).
15373830	5	29	theme	O-GlcNAc	697:704	arg1	modification					706:717	O-GlcNAc modification	697:717	O-GlcNAc modification of HIC1 proteins	697:734	Using C-terminal deletion mutants, we have shown that O-GlcNAc modification of HIC1 proteins occurred preferentially in the DNA-binding domain.
15373830	0	30	dep	glycosylated	68:79	arg1	O-GlcNAc					59:66	O-GlcNAc	59:66	O-GlcNAc	59:66	The tumor suppressor HIC1 (hypermethylated in cancer 1) is O-GlcNAc glycosylated.
15373830	9	31	theme	DNA-binding	1813:1823	arg1	domain					1825:1830	the DNA-binding domain	1809:1830	the DNA-binding domain	1809:1830	Interestingly, these truncated proteins are O-GlcNAc modified in their C-terminal tail (residues 670-711) and not in the DNA-binding domain, as for the full-length proteins.
15373830	8	32	theme	separated	1387:1395	arg1	pools					1397:1401	separated pools	1387:1401	separated pools of glycosylated and unglycosylated forms of a construct exhibiting only the DNA-binding domain and the C-terminal tail of HIC1 (residues 399-714)	1387:1547	Electrophoretic mobility shift assays performed with separated pools of glycosylated and unglycosylated forms of a construct exhibiting only the DNA-binding domain and the C-terminal tail of HIC1 (residues 399-714) and supershift experiments with wheat germ agglutinin or RL-2, an antibody raised against O-GlcNAc residues, fully corroborated these results.
15373830	7	33	theme	BTB-POZ-deleted	1168:1182	arg1	proteins					1184:1191	BTB-POZ-deleted proteins	1168:1191	BTB-POZ-deleted proteins	1168:1191	Intriguingly, N-terminal truncated forms corresponding to BTB-POZ-deleted proteins exhibited a strikingly differential activity, as the glycosylated truncated forms are unable to bind DNA whereas the unglycosylated ones do.
15373830	1	34	theme	N-terminal	206:215	arg1	dimerization					217:228	an N-terminal dimerization and autonomous repression domain	203:261	dimerization	217:228	HIC1 (hypermethylated in cancer 1) is a transcriptional repressor containing five Krüppel-like C(2)H(2) zinc fingers and an N-terminal dimerization and autonomous repression domain called BTB/POZ.
15373830	0	35	theme	suppressor	10:19	arg1	HIC1					21:24	The tumor suppressor HIC1	0:24	The tumor suppressor HIC1 (hypermethylated in cancer 1)	0:54	The tumor suppressor HIC1 (hypermethylated in cancer 1) is O-GlcNAc glycosylated.
15373830	7	36	theme	unglycosylated	1310:1323	arg1	ones					1325:1328	the unglycosylated ones	1306:1328	the unglycosylated ones	1306:1328	Intriguingly, N-terminal truncated forms corresponding to BTB-POZ-deleted proteins exhibited a strikingly differential activity, as the glycosylated truncated forms are unable to bind DNA whereas the unglycosylated ones do.
15373830	8	37	theme	wheat	1581:1585	arg1	agglutinin					1592:1601	wheat germ agglutinin	1581:1601	wheat germ agglutinin	1581:1601	Electrophoretic mobility shift assays performed with separated pools of glycosylated and unglycosylated forms of a construct exhibiting only the DNA-binding domain and the C-terminal tail of HIC1 (residues 399-714) and supershift experiments with wheat germ agglutinin or RL-2, an antibody raised against O-GlcNAc residues, fully corroborated these results.
15373830	7	38	theme	truncated	1135:1143	arg1	forms					1145:1149	N-terminal truncated forms	1124:1149	N-terminal truncated forms corresponding to BTB-POZ-deleted proteins	1124:1191	Intriguingly, N-terminal truncated forms corresponding to BTB-POZ-deleted proteins exhibited a strikingly differential activity, as the glycosylated truncated forms are unable to bind DNA whereas the unglycosylated ones do.
15373830	1	39	theme	repression	245:254	arg1	domain					256:261	an N-terminal dimerization and autonomous repression domain	203:261	domain	256:261	HIC1 (hypermethylated in cancer 1) is a transcriptional repressor containing five Krüppel-like C(2)H(2) zinc fingers and an N-terminal dimerization and autonomous repression domain called BTB/POZ.
15373830	9	40	theme	full-length	1844:1854	arg1	proteins					1856:1863	the full-length proteins	1840:1863	the full-length proteins	1840:1863	Interestingly, these truncated proteins are O-GlcNAc modified in their C-terminal tail (residues 670-711) and not in the DNA-binding domain, as for the full-length proteins.
15373830	8	41	theme	forms	1438:1442	arg1	pools					1397:1401	separated pools	1387:1401	separated pools of glycosylated and unglycosylated forms of a construct exhibiting only the DNA-binding domain and the C-terminal tail of HIC1 (residues 399-714)	1387:1547	Electrophoretic mobility shift assays performed with separated pools of glycosylated and unglycosylated forms of a construct exhibiting only the DNA-binding domain and the C-terminal tail of HIC1 (residues 399-714) and supershift experiments with wheat germ agglutinin or RL-2, an antibody raised against O-GlcNAc residues, fully corroborated these results.
15373830	5	42	theme	HIC1	722:725	arg1	proteins					727:734	HIC1 proteins	722:734	HIC1 proteins	722:734	Using C-terminal deletion mutants, we have shown that O-GlcNAc modification of HIC1 proteins occurred preferentially in the DNA-binding domain.
15373830	6	43	theme	HIC1	1104:1107	arg1	recognition					1089:1099	the specific DNA recognition	1072:1099	the specific DNA recognition of HIC1	1072:1107	Nonglycosylated and glycosylated forms of full-length HIC1 proteins separated by wheat germ agglutinin affinity purification, displayed the same specific DNA-binding activity in electrophoretic mobility shift assays proving that the O-GlcNAc modification is not directly implicated in the specific DNA recognition of HIC1.
15373830	4	44	contain	has	593:595	arg1	HIC1					588:591	HIC1	588:591	HIC1	588:591	Analysis of [(3)H]Gal-labeled tryptic peptides indicates that HIC1 has three major sites for O-GlcNAc glycosylation.
15373830	4	44	contain	has	593:595	arg2	sites					609:613	three major sites	597:613	three major sites for O-GlcNAc glycosylation	597:640	Analysis of [(3)H]Gal-labeled tryptic peptides indicates that HIC1 has three major sites for O-GlcNAc glycosylation.
15373830	8	45	gly	glycosylated	1406:1417	arg1	forms					1438:1442	glycosylated and unglycosylated forms	1406:1442	glycosylated and unglycosylated forms of a construct exhibiting only the DNA-binding domain and the C-terminal tail of HIC1 (residues 399-714)	1406:1547	Electrophoretic mobility shift assays performed with separated pools of glycosylated and unglycosylated forms of a construct exhibiting only the DNA-binding domain and the C-terminal tail of HIC1 (residues 399-714) and supershift experiments with wheat germ agglutinin or RL-2, an antibody raised against O-GlcNAc residues, fully corroborated these results.
15373830	8	45	gly	glycosylated	1406:1417	arg1	construct					1449:1457	a construct	1447:1457	a construct exhibiting only the DNA-binding domain and the C-terminal tail of HIC1 (residues 399-714)	1447:1547	Electrophoretic mobility shift assays performed with separated pools of glycosylated and unglycosylated forms of a construct exhibiting only the DNA-binding domain and the C-terminal tail of HIC1 (residues 399-714) and supershift experiments with wheat germ agglutinin or RL-2, an antibody raised against O-GlcNAc residues, fully corroborated these results.
15373830	10	46	theme	O-GlcNAc	1876:1883	arg1	sensitive					1970:1978	sensitive	1970:1978	sensitive	1970:1978	Thus, the O-GlcNAc modification of HIC1 does not affect its specific DNA-binding activity and is highly sensitive to conformational effects, notably its dimerization through the BTB/POZ domain.
15373830	10	46	theme	O-GlcNAc	1876:1883	arg1	modification					1885:1896	the O-GlcNAc modification	1872:1896	the O-GlcNAc modification of HIC1	1872:1904	Thus, the O-GlcNAc modification of HIC1 does not affect its specific DNA-binding activity and is highly sensitive to conformational effects, notably its dimerization through the BTB/POZ domain.
15373830	2	47	theme	HIC1	317:320	arg1	proteins					322:329	full-length HIC1 proteins	305:329	full-length HIC1 proteins	305:329	Here, we demonstrate that full-length HIC1 proteins are modified both in vivo and in vitro with O-linked N-acetylglucosamine (O-GlcNAc).
15373830	8	48	gly	unglycosylated	1423:1436	arg1	forms					1438:1442	glycosylated and unglycosylated forms	1406:1442	glycosylated and unglycosylated forms of a construct exhibiting only the DNA-binding domain and the C-terminal tail of HIC1 (residues 399-714)	1406:1547	Electrophoretic mobility shift assays performed with separated pools of glycosylated and unglycosylated forms of a construct exhibiting only the DNA-binding domain and the C-terminal tail of HIC1 (residues 399-714) and supershift experiments with wheat germ agglutinin or RL-2, an antibody raised against O-GlcNAc residues, fully corroborated these results.
15373830	8	48	gly	unglycosylated	1423:1436	arg1	construct					1449:1457	a construct	1447:1457	a construct exhibiting only the DNA-binding domain and the C-terminal tail of HIC1 (residues 399-714)	1447:1547	Electrophoretic mobility shift assays performed with separated pools of glycosylated and unglycosylated forms of a construct exhibiting only the DNA-binding domain and the C-terminal tail of HIC1 (residues 399-714) and supershift experiments with wheat germ agglutinin or RL-2, an antibody raised against O-GlcNAc residues, fully corroborated these results.
15373830	6	49	theme	germ	874:877	arg1	agglutinin					879:888	wheat germ agglutinin	868:888	wheat germ agglutinin affinity purification	868:910	Nonglycosylated and glycosylated forms of full-length HIC1 proteins separated by wheat germ agglutinin affinity purification, displayed the same specific DNA-binding activity in electrophoretic mobility shift assays proving that the O-GlcNAc modification is not directly implicated in the specific DNA recognition of HIC1.
15373830	6	50	theme	specific	1076:1083	arg1	recognition					1089:1099	the specific DNA recognition	1072:1099	the specific DNA recognition of HIC1	1072:1107	Nonglycosylated and glycosylated forms of full-length HIC1 proteins separated by wheat germ agglutinin affinity purification, displayed the same specific DNA-binding activity in electrophoretic mobility shift assays proving that the O-GlcNAc modification is not directly implicated in the specific DNA recognition of HIC1.
15373830	3	51	theme	dynamic	433:439	arg1	glycosylation					441:453	a highly dynamic glycosylation	424:453	a highly dynamic glycosylation found within the cytosolic and the nuclear compartments of eukaryotes	424:523	This is a highly dynamic glycosylation found within the cytosolic and the nuclear compartments of eukaryotes.
15373830	3	51	theme	dynamic	433:439	arg1	This					416:419	This	416:419	This	416:419	This is a highly dynamic glycosylation found within the cytosolic and the nuclear compartments of eukaryotes.
15373830	1	52	theme	zinc	186:189	arg1	fingers					191:197	five Krüppel-like C(2)H(2) zinc fingers	159:197	five Krüppel-like C(2)H(2) zinc fingers	159:197	HIC1 (hypermethylated in cancer 1) is a transcriptional repressor containing five Krüppel-like C(2)H(2) zinc fingers and an N-terminal dimerization and autonomous repression domain called BTB/POZ.
15373830	7	53	theme	glycosylated	1246:1257	arg1	unable					1279:1284	unable	1279:1284	unable	1279:1284	Intriguingly, N-terminal truncated forms corresponding to BTB-POZ-deleted proteins exhibited a strikingly differential activity, as the glycosylated truncated forms are unable to bind DNA whereas the unglycosylated ones do.
15373830	7	53	theme	glycosylated	1246:1257	arg1	forms					1269:1273	the glycosylated truncated forms	1242:1273	the glycosylated truncated forms	1242:1273	Intriguingly, N-terminal truncated forms corresponding to BTB-POZ-deleted proteins exhibited a strikingly differential activity, as the glycosylated truncated forms are unable to bind DNA whereas the unglycosylated ones do.
15373830	8	54	theme	O-GlcNAc	1639:1646	arg1	residues					1648:1655	O-GlcNAc residues	1639:1655	O-GlcNAc residues	1639:1655	Electrophoretic mobility shift assays performed with separated pools of glycosylated and unglycosylated forms of a construct exhibiting only the DNA-binding domain and the C-terminal tail of HIC1 (residues 399-714) and supershift experiments with wheat germ agglutinin or RL-2, an antibody raised against O-GlcNAc residues, fully corroborated these results.
15373830	6	55	theme	proteins	846:853	arg1	forms					820:824	Nonglycosylated and glycosylated forms	787:824	Nonglycosylated and glycosylated forms	787:824	Nonglycosylated and glycosylated forms of full-length HIC1 proteins separated by wheat germ agglutinin affinity purification, displayed the same specific DNA-binding activity in electrophoretic mobility shift assays proving that the O-GlcNAc modification is not directly implicated in the specific DNA recognition of HIC1.
15373830	6	56	theme	full-length	829:839	arg1	proteins					846:853	full-length HIC1 proteins	829:853	full-length HIC1 proteins separated by wheat germ agglutinin affinity purification	829:910	Nonglycosylated and glycosylated forms of full-length HIC1 proteins separated by wheat germ agglutinin affinity purification, displayed the same specific DNA-binding activity in electrophoretic mobility shift assays proving that the O-GlcNAc modification is not directly implicated in the specific DNA recognition of HIC1.
15373830	10	57	theme	specific	1926:1933	arg1	activity					1947:1954	its specific DNA-binding activity	1922:1954	its specific DNA-binding activity	1922:1954	Thus, the O-GlcNAc modification of HIC1 does not affect its specific DNA-binding activity and is highly sensitive to conformational effects, notably its dimerization through the BTB/POZ domain.
15373830	6	58	theme	specific	932:939	arg1	activity					953:960	the same specific DNA-binding activity	923:960	the same specific DNA-binding activity	923:960	Nonglycosylated and glycosylated forms of full-length HIC1 proteins separated by wheat germ agglutinin affinity purification, displayed the same specific DNA-binding activity in electrophoretic mobility shift assays proving that the O-GlcNAc modification is not directly implicated in the specific DNA recognition of HIC1.
15373830	9	59	theme	truncated	1713:1721	arg1	proteins					1723:1730	these truncated proteins	1707:1730	these truncated proteins	1707:1730	Interestingly, these truncated proteins are O-GlcNAc modified in their C-terminal tail (residues 670-711) and not in the DNA-binding domain, as for the full-length proteins.
15373830	3	60	theme	nuclear	490:496	arg1	compartments					498:509	the nuclear compartments	486:509	the nuclear compartments	486:509	This is a highly dynamic glycosylation found within the cytosolic and the nuclear compartments of eukaryotes.
15373830	1	61	theme	C	177:177	arg1	H					181:181	Krüppel-like C(2)H(2)	164:184	five Krüppel-like C(2)H(2) zinc fingers	159:197	HIC1 (hypermethylated in cancer 1) is a transcriptional repressor containing five Krüppel-like C(2)H(2) zinc fingers and an N-terminal dimerization and autonomous repression domain called BTB/POZ.
15373830	4	62	theme	tryptic	556:562	arg1	peptides					564:571	[(3)H]Gal-labeled tryptic peptides	538:571	[(3)H]Gal-labeled tryptic peptides	538:571	Analysis of [(3)H]Gal-labeled tryptic peptides indicates that HIC1 has three major sites for O-GlcNAc glycosylation.
15373830	5	63	mod	modification	706:717	arg3	O-GlcNAc					697:704	O-GlcNAc modification	697:717	O-GlcNAc modification of HIC1 proteins	697:734	Using C-terminal deletion mutants, we have shown that O-GlcNAc modification of HIC1 proteins occurred preferentially in the DNA-binding domain.
15373830	5	63	mod	modification	706:717	arg1	proteins					727:734	HIC1 proteins	722:734	HIC1 proteins	722:734	Using C-terminal deletion mutants, we have shown that O-GlcNAc modification of HIC1 proteins occurred preferentially in the DNA-binding domain.
15373830	3	64	located	found	455:459	arg1	compartments					498:509	the nuclear compartments	486:509	the nuclear compartments	486:509	This is a highly dynamic glycosylation found within the cytosolic and the nuclear compartments of eukaryotes.
15373830	3	64	located	found	455:459	arg2	glycosylation					441:453	a highly dynamic glycosylation	424:453	a highly dynamic glycosylation found within the cytosolic and the nuclear compartments of eukaryotes	424:523	This is a highly dynamic glycosylation found within the cytosolic and the nuclear compartments of eukaryotes.
15373830	3	64	located	found	455:459	arg1	cytosolic					472:480	cytosolic	472:480	cytosolic	472:480	This is a highly dynamic glycosylation found within the cytosolic and the nuclear compartments of eukaryotes.
15373830	3	64	located	found	455:459	arg2	This					416:419	This	416:419	This	416:419	This is a highly dynamic glycosylation found within the cytosolic and the nuclear compartments of eukaryotes.
15373830	6	65	theme	affinity	890:897	arg1	purification					899:910	wheat germ agglutinin affinity purification	868:910	wheat germ agglutinin affinity purification	868:910	Nonglycosylated and glycosylated forms of full-length HIC1 proteins separated by wheat germ agglutinin affinity purification, displayed the same specific DNA-binding activity in electrophoretic mobility shift assays proving that the O-GlcNAc modification is not directly implicated in the specific DNA recognition of HIC1.
15373830	4	66	theme	O-GlcNAc	619:626	arg1	glycosylation					628:640	O-GlcNAc glycosylation	619:640	O-GlcNAc glycosylation	619:640	Analysis of [(3)H]Gal-labeled tryptic peptides indicates that HIC1 has three major sites for O-GlcNAc glycosylation.
15373830	10	67	theme	conformational	1983:1996	arg1	effects					1998:2004	conformational effects	1983:2004	conformational effects	1983:2004	Thus, the O-GlcNAc modification of HIC1 does not affect its specific DNA-binding activity and is highly sensitive to conformational effects, notably its dimerization through the BTB/POZ domain.
15373830	10	67	theme	conformational	1983:1996	arg1	dimerization					2019:2030	its dimerization	2015:2030	its dimerization through the BTB/POZ domain	2015:2057	Thus, the O-GlcNAc modification of HIC1 does not affect its specific DNA-binding activity and is highly sensitive to conformational effects, notably its dimerization through the BTB/POZ domain.
15373830	8	68	with	assays	1365:1370	arg1	RL-2					1606:1609	RL-2	1606:1609	RL-2	1606:1609	Electrophoretic mobility shift assays performed with separated pools of glycosylated and unglycosylated forms of a construct exhibiting only the DNA-binding domain and the C-terminal tail of HIC1 (residues 399-714) and supershift experiments with wheat germ agglutinin or RL-2, an antibody raised against O-GlcNAc residues, fully corroborated these results.
15373830	8	68	with	assays	1365:1370	arg1	antibody					1615:1622	an antibody	1612:1622	an antibody raised against O-GlcNAc residues	1612:1655	Electrophoretic mobility shift assays performed with separated pools of glycosylated and unglycosylated forms of a construct exhibiting only the DNA-binding domain and the C-terminal tail of HIC1 (residues 399-714) and supershift experiments with wheat germ agglutinin or RL-2, an antibody raised against O-GlcNAc residues, fully corroborated these results.
15373830	8	68	with	assays	1365:1370	arg1	agglutinin					1592:1601	wheat germ agglutinin	1581:1601	wheat germ agglutinin	1581:1601	Electrophoretic mobility shift assays performed with separated pools of glycosylated and unglycosylated forms of a construct exhibiting only the DNA-binding domain and the C-terminal tail of HIC1 (residues 399-714) and supershift experiments with wheat germ agglutinin or RL-2, an antibody raised against O-GlcNAc residues, fully corroborated these results.
15373830	6	69	theme	shift	990:994	arg1	assays					996:1001	electrophoretic mobility shift assays	965:1001	electrophoretic mobility shift assays proving that the O-GlcNAc modification is not directly implicated in the specific DNA recognition of HIC1	965:1107	Nonglycosylated and glycosylated forms of full-length HIC1 proteins separated by wheat germ agglutinin affinity purification, displayed the same specific DNA-binding activity in electrophoretic mobility shift assays proving that the O-GlcNAc modification is not directly implicated in the specific DNA recognition of HIC1.
15373830	8	70	theme	HIC1	1525:1528	arg1	residues					1531:1538	residues 399-714	1531:1546	residues 399-714	1531:1546	Electrophoretic mobility shift assays performed with separated pools of glycosylated and unglycosylated forms of a construct exhibiting only the DNA-binding domain and the C-terminal tail of HIC1 (residues 399-714) and supershift experiments with wheat germ agglutinin or RL-2, an antibody raised against O-GlcNAc residues, fully corroborated these results.
15373830	8	70	theme	HIC1	1525:1528	arg1	domain					1491:1496	only the DNA-binding domain	1470:1496	only the DNA-binding domain	1470:1496	Electrophoretic mobility shift assays performed with separated pools of glycosylated and unglycosylated forms of a construct exhibiting only the DNA-binding domain and the C-terminal tail of HIC1 (residues 399-714) and supershift experiments with wheat germ agglutinin or RL-2, an antibody raised against O-GlcNAc residues, fully corroborated these results.
15373830	8	70	theme	HIC1	1525:1528	arg1	HIC1					1525:1528	HIC1	1525:1528	HIC1	1525:1528	Electrophoretic mobility shift assays performed with separated pools of glycosylated and unglycosylated forms of a construct exhibiting only the DNA-binding domain and the C-terminal tail of HIC1 (residues 399-714) and supershift experiments with wheat germ agglutinin or RL-2, an antibody raised against O-GlcNAc residues, fully corroborated these results.
15373830	8	70	theme	HIC1	1525:1528	arg1	tail					1517:1520	the C-terminal tail	1502:1520	the C-terminal tail of HIC1 (residues 399-714)	1502:1547	Electrophoretic mobility shift assays performed with separated pools of glycosylated and unglycosylated forms of a construct exhibiting only the DNA-binding domain and the C-terminal tail of HIC1 (residues 399-714) and supershift experiments with wheat germ agglutinin or RL-2, an antibody raised against O-GlcNAc residues, fully corroborated these results.
15373830	1	71	theme	H	181:181	arg1	fingers					191:197	five Krüppel-like C(2)H(2) zinc fingers	159:197	five Krüppel-like C(2)H(2) zinc fingers	159:197	HIC1 (hypermethylated in cancer 1) is a transcriptional repressor containing five Krüppel-like C(2)H(2) zinc fingers and an N-terminal dimerization and autonomous repression domain called BTB/POZ.
15373830	7	72	theme	differential	1216:1227	arg1	activity					1229:1236	a strikingly differential activity	1203:1236	a strikingly differential activity	1203:1236	Intriguingly, N-terminal truncated forms corresponding to BTB-POZ-deleted proteins exhibited a strikingly differential activity, as the glycosylated truncated forms are unable to bind DNA whereas the unglycosylated ones do.
15373830	7	73	gly	unglycosylated	1310:1323	arg1	ones					1325:1328	the unglycosylated ones	1306:1328	the unglycosylated ones	1306:1328	Intriguingly, N-terminal truncated forms corresponding to BTB-POZ-deleted proteins exhibited a strikingly differential activity, as the glycosylated truncated forms are unable to bind DNA whereas the unglycosylated ones do.
15373830	6	74	theme	electrophoretic	965:979	arg1	assays					996:1001	electrophoretic mobility shift assays	965:1001	electrophoretic mobility shift assays proving that the O-GlcNAc modification is not directly implicated in the specific DNA recognition of HIC1	965:1107	Nonglycosylated and glycosylated forms of full-length HIC1 proteins separated by wheat germ agglutinin affinity purification, displayed the same specific DNA-binding activity in electrophoretic mobility shift assays proving that the O-GlcNAc modification is not directly implicated in the specific DNA recognition of HIC1.
15373830	5	75	theme	C-terminal	649:658	arg1	mutants					669:675	C-terminal deletion mutants	649:675	C-terminal deletion mutants	649:675	Using C-terminal deletion mutants, we have shown that O-GlcNAc modification of HIC1 proteins occurred preferentially in the DNA-binding domain.
15373830	8	76	theme	mobility	1350:1357	arg1	assays					1365:1370	Electrophoretic mobility shift assays	1334:1370	Electrophoretic mobility shift assays performed with separated pools of glycosylated and unglycosylated forms of a construct exhibiting only the DNA-binding domain and the C-terminal tail of HIC1 (residues 399-714)	1334:1547	Electrophoretic mobility shift assays performed with separated pools of glycosylated and unglycosylated forms of a construct exhibiting only the DNA-binding domain and the C-terminal tail of HIC1 (residues 399-714) and supershift experiments with wheat germ agglutinin or RL-2, an antibody raised against O-GlcNAc residues, fully corroborated these results.
15373830	10	77	theme	BTB/POZ	2044:2050	arg1	domain					2052:2057	the BTB/POZ domain	2040:2057	the BTB/POZ domain	2040:2057	Thus, the O-GlcNAc modification of HIC1 does not affect its specific DNA-binding activity and is highly sensitive to conformational effects, notably its dimerization through the BTB/POZ domain.
15373830	8	78	theme	supershift	1553:1562	arg1	experiments					1564:1574	supershift experiments	1553:1574	supershift experiments with wheat germ agglutinin or RL-2, an antibody raised against O-GlcNAc residues,	1553:1656	Electrophoretic mobility shift assays performed with separated pools of glycosylated and unglycosylated forms of a construct exhibiting only the DNA-binding domain and the C-terminal tail of HIC1 (residues 399-714) and supershift experiments with wheat germ agglutinin or RL-2, an antibody raised against O-GlcNAc residues, fully corroborated these results.
15373830	5	79	theme	proteins	727:734	arg1	modification					706:717	O-GlcNAc modification	697:717	O-GlcNAc modification of HIC1 proteins	697:734	Using C-terminal deletion mutants, we have shown that O-GlcNAc modification of HIC1 proteins occurred preferentially in the DNA-binding domain.
15373830	0	80	gly	glycosylated	68:79	arg1	HIC1					21:24	The tumor suppressor HIC1	0:24	The tumor suppressor HIC1 (hypermethylated in cancer 1)	0:54	The tumor suppressor HIC1 (hypermethylated in cancer 1) is O-GlcNAc glycosylated.
15373830	2	81	theme	O-linked	375:382	arg1	O-GlcNAc					405:412	O-GlcNAc	405:412	O-GlcNAc	405:412	Here, we demonstrate that full-length HIC1 proteins are modified both in vivo and in vitro with O-linked N-acetylglucosamine (O-GlcNAc).
15373830	2	81	theme	O-linked	375:382	arg1	N-acetylglucosamine					384:402	O-linked N-acetylglucosamine	375:402	O-linked N-acetylglucosamine (O-GlcNAc)	375:413	Here, we demonstrate that full-length HIC1 proteins are modified both in vivo and in vitro with O-linked N-acetylglucosamine (O-GlcNAc).
15373830	6	82	gly	glycosylated	807:818	arg1	proteins					846:853	full-length HIC1 proteins	829:853	full-length HIC1 proteins separated by wheat germ agglutinin affinity purification	829:910	Nonglycosylated and glycosylated forms of full-length HIC1 proteins separated by wheat germ agglutinin affinity purification, displayed the same specific DNA-binding activity in electrophoretic mobility shift assays proving that the O-GlcNAc modification is not directly implicated in the specific DNA recognition of HIC1.
15373830	6	82	gly	glycosylated	807:818	arg1	forms					820:824	Nonglycosylated and glycosylated forms	787:824	Nonglycosylated and glycosylated forms	787:824	Nonglycosylated and glycosylated forms of full-length HIC1 proteins separated by wheat germ agglutinin affinity purification, displayed the same specific DNA-binding activity in electrophoretic mobility shift assays proving that the O-GlcNAc modification is not directly implicated in the specific DNA recognition of HIC1.
15373830	8	83	theme	germ	1587:1590	arg1	agglutinin					1592:1601	wheat germ agglutinin	1581:1601	wheat germ agglutinin	1581:1601	Electrophoretic mobility shift assays performed with separated pools of glycosylated and unglycosylated forms of a construct exhibiting only the DNA-binding domain and the C-terminal tail of HIC1 (residues 399-714) and supershift experiments with wheat germ agglutinin or RL-2, an antibody raised against O-GlcNAc residues, fully corroborated these results.
15373830	6	84	gly	Nonglycosylated	787:801	arg1	proteins					846:853	full-length HIC1 proteins	829:853	full-length HIC1 proteins separated by wheat germ agglutinin affinity purification	829:910	Nonglycosylated and glycosylated forms of full-length HIC1 proteins separated by wheat germ agglutinin affinity purification, displayed the same specific DNA-binding activity in electrophoretic mobility shift assays proving that the O-GlcNAc modification is not directly implicated in the specific DNA recognition of HIC1.
15373830	6	84	gly	Nonglycosylated	787:801	arg1	forms					820:824	Nonglycosylated and glycosylated forms	787:824	Nonglycosylated and glycosylated forms	787:824	Nonglycosylated and glycosylated forms of full-length HIC1 proteins separated by wheat germ agglutinin affinity purification, displayed the same specific DNA-binding activity in electrophoretic mobility shift assays proving that the O-GlcNAc modification is not directly implicated in the specific DNA recognition of HIC1.
15373830	6	85	theme	DNA	1085:1087	arg1	recognition					1089:1099	the specific DNA recognition	1072:1099	the specific DNA recognition of HIC1	1072:1107	Nonglycosylated and glycosylated forms of full-length HIC1 proteins separated by wheat germ agglutinin affinity purification, displayed the same specific DNA-binding activity in electrophoretic mobility shift assays proving that the O-GlcNAc modification is not directly implicated in the specific DNA recognition of HIC1.
15373830	7	86	theme	N-terminal	1124:1133	arg1	forms					1145:1149	N-terminal truncated forms	1124:1149	N-terminal truncated forms corresponding to BTB-POZ-deleted proteins	1124:1191	Intriguingly, N-terminal truncated forms corresponding to BTB-POZ-deleted proteins exhibited a strikingly differential activity, as the glycosylated truncated forms are unable to bind DNA whereas the unglycosylated ones do.
15373830	1	87	theme	autonomous	234:243	arg1	domain					256:261	an N-terminal dimerization and autonomous repression domain	203:261	domain	256:261	HIC1 (hypermethylated in cancer 1) is a transcriptional repressor containing five Krüppel-like C(2)H(2) zinc fingers and an N-terminal dimerization and autonomous repression domain called BTB/POZ.
15373830	7	88	gly	glycosylated	1246:1257	arg1	unable					1279:1284	unable	1279:1284	unable	1279:1284	Intriguingly, N-terminal truncated forms corresponding to BTB-POZ-deleted proteins exhibited a strikingly differential activity, as the glycosylated truncated forms are unable to bind DNA whereas the unglycosylated ones do.
15373830	7	88	gly	glycosylated	1246:1257	arg1	forms					1269:1273	the glycosylated truncated forms	1242:1273	the glycosylated truncated forms	1242:1273	Intriguingly, N-terminal truncated forms corresponding to BTB-POZ-deleted proteins exhibited a strikingly differential activity, as the glycosylated truncated forms are unable to bind DNA whereas the unglycosylated ones do.
15373830	6	89	theme	glycosylated	807:818	arg1	forms					820:824	Nonglycosylated and glycosylated forms	787:824	Nonglycosylated and glycosylated forms	787:824	Nonglycosylated and glycosylated forms of full-length HIC1 proteins separated by wheat germ agglutinin affinity purification, displayed the same specific DNA-binding activity in electrophoretic mobility shift assays proving that the O-GlcNAc modification is not directly implicated in the specific DNA recognition of HIC1.
15373830	4	90	theme	major	603:607	arg1	sites					609:613	three major sites	597:613	three major sites for O-GlcNAc glycosylation	597:640	Analysis of [(3)H]Gal-labeled tryptic peptides indicates that HIC1 has three major sites for O-GlcNAc glycosylation.
15373830	1	91	contain	containing	148:157	arg1	repressor					138:146	a transcriptional repressor	120:146	a transcriptional repressor containing five Krüppel-like C(2)H(2) zinc fingers and an N-terminal dimerization and autonomous repression domain called BTB/POZ	120:276	HIC1 (hypermethylated in cancer 1) is a transcriptional repressor containing five Krüppel-like C(2)H(2) zinc fingers and an N-terminal dimerization and autonomous repression domain called BTB/POZ.
15373830	1	91	contain	containing	148:157	arg1	HIC1					82:85	HIC1	82:85	HIC1 (hypermethylated in cancer 1)	82:115	HIC1 (hypermethylated in cancer 1) is a transcriptional repressor containing five Krüppel-like C(2)H(2) zinc fingers and an N-terminal dimerization and autonomous repression domain called BTB/POZ.
15373830	1	91	contain	containing	148:157	arg2	fingers					191:197	five Krüppel-like C(2)H(2) zinc fingers	159:197	five Krüppel-like C(2)H(2) zinc fingers	159:197	HIC1 (hypermethylated in cancer 1) is a transcriptional repressor containing five Krüppel-like C(2)H(2) zinc fingers and an N-terminal dimerization and autonomous repression domain called BTB/POZ.
15373830	1	91	contain	containing	148:157	arg2	dimerization					217:228	an N-terminal dimerization and autonomous repression domain	203:261	dimerization	217:228	HIC1 (hypermethylated in cancer 1) is a transcriptional repressor containing five Krüppel-like C(2)H(2) zinc fingers and an N-terminal dimerization and autonomous repression domain called BTB/POZ.
15373830	8	92	theme	glycosylated	1406:1417	arg1	forms					1438:1442	glycosylated and unglycosylated forms	1406:1442	glycosylated and unglycosylated forms of a construct exhibiting only the DNA-binding domain and the C-terminal tail of HIC1 (residues 399-714)	1406:1547	Electrophoretic mobility shift assays performed with separated pools of glycosylated and unglycosylated forms of a construct exhibiting only the DNA-binding domain and the C-terminal tail of HIC1 (residues 399-714) and supershift experiments with wheat germ agglutinin or RL-2, an antibody raised against O-GlcNAc residues, fully corroborated these results.
15373830	6	93	theme	Nonglycosylated	787:801	arg1	forms					820:824	Nonglycosylated and glycosylated forms	787:824	Nonglycosylated and glycosylated forms	787:824	Nonglycosylated and glycosylated forms of full-length HIC1 proteins separated by wheat germ agglutinin affinity purification, displayed the same specific DNA-binding activity in electrophoretic mobility shift assays proving that the O-GlcNAc modification is not directly implicated in the specific DNA recognition of HIC1.
15373830	4	94	dep	Gal-labeled	544:554	arg1	H					542:542	(3)H	539:542	(3)H	539:542	Analysis of [(3)H]Gal-labeled tryptic peptides indicates that HIC1 has three major sites for O-GlcNAc glycosylation.
15373830	10	95	theme	HIC1	1901:1904	arg1	sensitive					1970:1978	sensitive	1970:1978	sensitive	1970:1978	Thus, the O-GlcNAc modification of HIC1 does not affect its specific DNA-binding activity and is highly sensitive to conformational effects, notably its dimerization through the BTB/POZ domain.
15373830	10	95	theme	HIC1	1901:1904	arg1	modification					1885:1896	the O-GlcNAc modification	1872:1896	the O-GlcNAc modification of HIC1	1872:1904	Thus, the O-GlcNAc modification of HIC1 does not affect its specific DNA-binding activity and is highly sensitive to conformational effects, notably its dimerization through the BTB/POZ domain.
15373830	8	96	theme	unglycosylated	1423:1436	arg1	forms					1438:1442	glycosylated and unglycosylated forms	1406:1442	glycosylated and unglycosylated forms of a construct exhibiting only the DNA-binding domain and the C-terminal tail of HIC1 (residues 399-714)	1406:1547	Electrophoretic mobility shift assays performed with separated pools of glycosylated and unglycosylated forms of a construct exhibiting only the DNA-binding domain and the C-terminal tail of HIC1 (residues 399-714) and supershift experiments with wheat germ agglutinin or RL-2, an antibody raised against O-GlcNAc residues, fully corroborated these results.
15373830	2	97	theme	full-length	305:315	arg1	proteins					322:329	full-length HIC1 proteins	305:329	full-length HIC1 proteins	305:329	Here, we demonstrate that full-length HIC1 proteins are modified both in vivo and in vitro with O-linked N-acetylglucosamine (O-GlcNAc).
15373830	7	98	theme	truncated	1259:1267	arg1	unable					1279:1284	unable	1279:1284	unable	1279:1284	Intriguingly, N-terminal truncated forms corresponding to BTB-POZ-deleted proteins exhibited a strikingly differential activity, as the glycosylated truncated forms are unable to bind DNA whereas the unglycosylated ones do.
15373830	7	98	theme	truncated	1259:1267	arg1	forms					1269:1273	the glycosylated truncated forms	1242:1273	the glycosylated truncated forms	1242:1273	Intriguingly, N-terminal truncated forms corresponding to BTB-POZ-deleted proteins exhibited a strikingly differential activity, as the glycosylated truncated forms are unable to bind DNA whereas the unglycosylated ones do.
15373830	8	99	theme	construct	1449:1457	arg1	forms					1438:1442	glycosylated and unglycosylated forms	1406:1442	glycosylated and unglycosylated forms of a construct exhibiting only the DNA-binding domain and the C-terminal tail of HIC1 (residues 399-714)	1406:1547	Electrophoretic mobility shift assays performed with separated pools of glycosylated and unglycosylated forms of a construct exhibiting only the DNA-binding domain and the C-terminal tail of HIC1 (residues 399-714) and supershift experiments with wheat germ agglutinin or RL-2, an antibody raised against O-GlcNAc residues, fully corroborated these results.
15373830	0	100	theme	tumor	4:8	arg1	HIC1					21:24	The tumor suppressor HIC1	0:24	The tumor suppressor HIC1 (hypermethylated in cancer 1)	0:54	The tumor suppressor HIC1 (hypermethylated in cancer 1) is O-GlcNAc glycosylated.
17488724	0	0	theme	potentiation	77:88	arg1	mechanism					56:64	the likely mechanism	45:64	the likely mechanism of heparin potentiation and conformational disease	45:115	C1 inhibitor serpin domain structure reveals the likely mechanism of heparin potentiation and conformational disease.
17488724	5	1	theme	potential	762:770	arg1	role					772:775	its potential role	758:775	its potential role as a barrier in the active-latent transition	758:820	The unique conformation of the C-terminal six residues suggests its potential role as a barrier in the active-latent transition.
17488724	6	2	theme	heparin	863:869	arg1	measurements					880:891	heparin affinity measurements	863:891	heparin affinity measurements	863:891	On the basis of surface charge pattern, heparin affinity measurements, and docking of a heparin disaccharide, a heparin binding site is proposed in the contact area of the serpin-proteinase encounter complex.
17488724	5	3	theme	residues	740:747	arg1	conformation					705:716	The unique conformation	694:716	The unique conformation of the C-terminal six residues	694:747	The unique conformation of the C-terminal six residues suggests its potential role as a barrier in the active-latent transition.
17488724	6	4	theme	contact	975:981	arg1	area					983:986	the contact area	971:986	the contact area of the serpin-proteinase encounter complex	971:1029	On the basis of surface charge pattern, heparin affinity measurements, and docking of a heparin disaccharide, a heparin binding site is proposed in the contact area of the serpin-proteinase encounter complex.
17488724	0	5	theme	heparin	69:75	arg1	potentiation					77:88	heparin potentiation	69:88	heparin potentiation	69:88	C1 inhibitor serpin domain structure reveals the likely mechanism of heparin potentiation and conformational disease.
17488724	7	6	theme	inhibitor	1085:1093	arg1	activity					1066:1073	the activity	1062:1073	the activity of the C1 inhibitor by a novel "sandwich" mechanism	1062:1125	We show how polyanions change the activity of the C1 inhibitor by a novel "sandwich" mechanism, explaining earlier reaction kinetic and mutagenesis studies.
17488724	1	7	theme	serpin	148:153	arg1	family					155:160	the serpin family	144:160	the serpin family	144:160	C1 inhibitor, a member of the serpin family, is a major down-regulator of inflammatory processes in blood.
17488724	0	8	theme	conformational	94:107	arg1	disease					109:115	conformational disease	94:115	conformational disease	94:115	C1 inhibitor serpin domain structure reveals the likely mechanism of heparin potentiation and conformational disease.
17488724	7	9	theme	C1	1082:1083	arg1	inhibitor					1085:1093	the C1 inhibitor	1078:1093	the C1 inhibitor	1078:1093	We show how polyanions change the activity of the C1 inhibitor by a novel "sandwich" mechanism, explaining earlier reaction kinetic and mutagenesis studies.
17488724	3	10	theme	crystal	373:379	arg1	structure					381:389	the first crystal structure	363:389	the first crystal structure of the serpin domain of human C1 inhibitor	363:432	Here we report the first crystal structure of the serpin domain of human C1 inhibitor, representing a previously unreported latent form, which explains functional consequences of several naturally occurring mutations, two of which are discussed in detail.
17488724	2	11	theme	hereditary	271:280	arg1	disease					339:345	a dominantly inheritable, potentially lethal disease	294:345	a dominantly inheritable, potentially lethal disease	294:345	Genetic deficiency of C1 inhibitor results in hereditary angioedema, a dominantly inheritable, potentially lethal disease.
17488724	2	11	theme	hereditary	271:280	arg1	angioedema					282:291	hereditary angioedema	271:291	hereditary angioedema	271:291	Genetic deficiency of C1 inhibitor results in hereditary angioedema, a dominantly inheritable, potentially lethal disease.
17488724	8	12	theme	attack	1347:1352	arg1	treatment					1273:1281	the treatment	1269:1281	the treatment of hereditary angioedema, organ transplant rejection, and heart attack	1269:1352	These results may help to improve therapeutic C1 inhibitor preparations used in the treatment of hereditary angioedema, organ transplant rejection, and heart attack.
17488724	5	13	theme	C-terminal	725:734	arg1	residues					740:747	the C-terminal six residues	721:747	the C-terminal six residues	721:747	The unique conformation of the C-terminal six residues suggests its potential role as a barrier in the active-latent transition.
17488724	6	14	dep	pattern	854:860	arg1	basis					830:834	basis	830:834	basis	830:834	On the basis of surface charge pattern, heparin affinity measurements, and docking of a heparin disaccharide, a heparin binding site is proposed in the contact area of the serpin-proteinase encounter complex.
17488724	6	14	dep	pattern	854:860	arg1	the					826:828	the	826:828	the	826:828	On the basis of surface charge pattern, heparin affinity measurements, and docking of a heparin disaccharide, a heparin binding site is proposed in the contact area of the serpin-proteinase encounter complex.
17488724	8	15	theme	organ	1309:1313	arg1	rejection					1326:1334	organ transplant rejection	1309:1334	organ transplant rejection	1309:1334	These results may help to improve therapeutic C1 inhibitor preparations used in the treatment of hereditary angioedema, organ transplant rejection, and heart attack.
17488724	3	16	theme	unreported	461:470	arg1	form					479:482	a previously unreported latent form	448:482	a previously unreported latent form	448:482	Here we report the first crystal structure of the serpin domain of human C1 inhibitor, representing a previously unreported latent form, which explains functional consequences of several naturally occurring mutations, two of which are discussed in detail.
17488724	3	17	theme	latent	472:477	arg1	form					479:482	a previously unreported latent form	448:482	a previously unreported latent form	448:482	Here we report the first crystal structure of the serpin domain of human C1 inhibitor, representing a previously unreported latent form, which explains functional consequences of several naturally occurring mutations, two of which are discussed in detail.
17488724	8	18	theme	therapeutic	1223:1233	arg1	preparations					1248:1259	therapeutic C1 inhibitor preparations	1223:1259	therapeutic C1 inhibitor preparations used in the treatment of hereditary angioedema, organ transplant rejection, and heart attack	1223:1352	These results may help to improve therapeutic C1 inhibitor preparations used in the treatment of hereditary angioedema, organ transplant rejection, and heart attack.
17488724	3	19	theme	consequences	511:522	arg1	consequences					511:522	functional consequences	500:522	functional consequences	500:522	Here we report the first crystal structure of the serpin domain of human C1 inhibitor, representing a previously unreported latent form, which explains functional consequences of several naturally occurring mutations, two of which are discussed in detail.
17488724	3	19	theme	consequences	511:522	arg1	two					566:568	two	566:568	two	566:568	Here we report the first crystal structure of the serpin domain of human C1 inhibitor, representing a previously unreported latent form, which explains functional consequences of several naturally occurring mutations, two of which are discussed in detail.
17488724	1	20	theme	family	155:160	arg1	inhibitor					121:129	C1 inhibitor	118:129	C1 inhibitor	118:129	C1 inhibitor, a member of the serpin family, is a major down-regulator of inflammatory processes in blood.
17488724	1	20	theme	family	155:160	arg1	member					134:139	a member	132:139	a member of the serpin family	132:160	C1 inhibitor, a member of the serpin family, is a major down-regulator of inflammatory processes in blood.
17488724	0	21	theme	disease	109:115	arg1	mechanism					56:64	the likely mechanism	45:64	the likely mechanism of heparin potentiation and conformational disease	45:115	C1 inhibitor serpin domain structure reveals the likely mechanism of heparin potentiation and conformational disease.
17488724	6	22	theme	affinity	871:878	arg1	measurements					880:891	heparin affinity measurements	863:891	heparin affinity measurements	863:891	On the basis of surface charge pattern, heparin affinity measurements, and docking of a heparin disaccharide, a heparin binding site is proposed in the contact area of the serpin-proteinase encounter complex.
17488724	6	23	theme	surface	839:845	arg1	pattern					854:860	surface charge pattern	839:860	surface charge pattern	839:860	On the basis of surface charge pattern, heparin affinity measurements, and docking of a heparin disaccharide, a heparin binding site is proposed in the contact area of the serpin-proteinase encounter complex.
17488724	2	24	theme	inhibitor	250:258	arg1	deficiency					233:242	Genetic deficiency	225:242	Genetic deficiency of C1 inhibitor	225:258	Genetic deficiency of C1 inhibitor results in hereditary angioedema, a dominantly inheritable, potentially lethal disease.
17488724	3	25	theme	C1	421:422	arg1	inhibitor					424:432	human C1 inhibitor	415:432	human C1 inhibitor	415:432	Here we report the first crystal structure of the serpin domain of human C1 inhibitor, representing a previously unreported latent form, which explains functional consequences of several naturally occurring mutations, two of which are discussed in detail.
17488724	0	26	theme	inhibitor	3:11	arg1	structure					27:35	C1 inhibitor serpin domain structure	0:35	C1 inhibitor serpin domain structure	0:35	C1 inhibitor serpin domain structure reveals the likely mechanism of heparin potentiation and conformational disease.
17488724	3	27	theme	functional	500:509	arg1	consequences					511:522	functional consequences	500:522	functional consequences	500:522	Here we report the first crystal structure of the serpin domain of human C1 inhibitor, representing a previously unreported latent form, which explains functional consequences of several naturally occurring mutations, two of which are discussed in detail.
17488724	8	28	theme	heart	1341:1345	arg1	attack					1347:1352	heart attack	1341:1352	heart attack	1341:1352	These results may help to improve therapeutic C1 inhibitor preparations used in the treatment of hereditary angioedema, organ transplant rejection, and heart attack.
17488724	6	29	theme	serpin-proteinase	995:1011	arg1	complex					1023:1029	the serpin-proteinase encounter complex	991:1029	the serpin-proteinase encounter complex	991:1029	On the basis of surface charge pattern, heparin affinity measurements, and docking of a heparin disaccharide, a heparin binding site is proposed in the contact area of the serpin-proteinase encounter complex.
17488724	3	30	theme	domain	405:410	arg1	structure					381:389	the first crystal structure	363:389	the first crystal structure of the serpin domain of human C1 inhibitor	363:432	Here we report the first crystal structure of the serpin domain of human C1 inhibitor, representing a previously unreported latent form, which explains functional consequences of several naturally occurring mutations, two of which are discussed in detail.
17488724	0	31	theme	C1	0:1	arg1	structure					27:35	C1 inhibitor serpin domain structure	0:35	C1 inhibitor serpin domain structure	0:35	C1 inhibitor serpin domain structure reveals the likely mechanism of heparin potentiation and conformational disease.
17488724	8	32	theme	transplant	1315:1324	arg1	rejection					1326:1334	organ transplant rejection	1309:1334	organ transplant rejection	1309:1334	These results may help to improve therapeutic C1 inhibitor preparations used in the treatment of hereditary angioedema, organ transplant rejection, and heart attack.
17488724	2	33	dep	inheritable	307:317	arg1	lethal					332:337	lethal	332:337	lethal	332:337	Genetic deficiency of C1 inhibitor results in hereditary angioedema, a dominantly inheritable, potentially lethal disease.
17488724	0	34	theme	domain	20:25	arg1	structure					27:35	C1 inhibitor serpin domain structure	0:35	C1 inhibitor serpin domain structure	0:35	C1 inhibitor serpin domain structure reveals the likely mechanism of heparin potentiation and conformational disease.
17488724	5	35	theme	active-latent	797:809	arg1	transition					811:820	the active-latent transition	793:820	the active-latent transition	793:820	The unique conformation of the C-terminal six residues suggests its potential role as a barrier in the active-latent transition.
17488724	3	36	theme	occurring	545:553	arg1	mutations					555:563	several naturally occurring mutations	527:563	several naturally occurring mutations	527:563	Here we report the first crystal structure of the serpin domain of human C1 inhibitor, representing a previously unreported latent form, which explains functional consequences of several naturally occurring mutations, two of which are discussed in detail.
17488724	1	37	theme	major	168:172	arg1	down-regulator					174:187	a major down-regulator	166:187	a major down-regulator of inflammatory processes in blood	166:222	C1 inhibitor, a member of the serpin family, is a major down-regulator of inflammatory processes in blood.
17488724	1	37	theme	major	168:172	arg1	inhibitor					121:129	C1 inhibitor	118:129	C1 inhibitor	118:129	C1 inhibitor, a member of the serpin family, is a major down-regulator of inflammatory processes in blood.
17488724	0	38	theme	serpin	13:18	arg1	structure					27:35	C1 inhibitor serpin domain structure	0:35	C1 inhibitor serpin domain structure	0:35	C1 inhibitor serpin domain structure reveals the likely mechanism of heparin potentiation and conformational disease.
17488724	6	39	theme	binding	943:949	arg1	site					951:954	a heparin binding site	933:954	a heparin binding site	933:954	On the basis of surface charge pattern, heparin affinity measurements, and docking of a heparin disaccharide, a heparin binding site is proposed in the contact area of the serpin-proteinase encounter complex.
17488724	5	40	theme	unique	698:703	arg1	conformation					705:716	The unique conformation	694:716	The unique conformation of the C-terminal six residues	694:747	The unique conformation of the C-terminal six residues suggests its potential role as a barrier in the active-latent transition.
17488724	3	41	theme	mutations	555:563	arg1	consequences					511:522	functional consequences	500:522	functional consequences	500:522	Here we report the first crystal structure of the serpin domain of human C1 inhibitor, representing a previously unreported latent form, which explains functional consequences of several naturally occurring mutations, two of which are discussed in detail.
17488724	4	42	theme	presented	608:616	arg1	structure					618:626	The presented structure	604:626	The presented structure	604:626	The presented structure displays a novel conformation with a seven-stranded beta-sheet A.
17488724	7	43	theme	sandwich	1107:1114	arg1	mechanism					1117:1125	a novel "sandwich" mechanism	1098:1125	a novel "sandwich" mechanism	1098:1125	We show how polyanions change the activity of the C1 inhibitor by a novel "sandwich" mechanism, explaining earlier reaction kinetic and mutagenesis studies.
17488724	6	44	theme	heparin	935:941	arg1	site					951:954	a heparin binding site	933:954	a heparin binding site	933:954	On the basis of surface charge pattern, heparin affinity measurements, and docking of a heparin disaccharide, a heparin binding site is proposed in the contact area of the serpin-proteinase encounter complex.
17488724	6	45	theme	complex	1023:1029	arg1	area					983:986	the contact area	971:986	the contact area of the serpin-proteinase encounter complex	971:1029	On the basis of surface charge pattern, heparin affinity measurements, and docking of a heparin disaccharide, a heparin binding site is proposed in the contact area of the serpin-proteinase encounter complex.
17488724	8	46	theme	hereditary	1286:1295	arg1	angioedema					1297:1306	hereditary angioedema	1286:1306	hereditary angioedema	1286:1306	These results may help to improve therapeutic C1 inhibitor preparations used in the treatment of hereditary angioedema, organ transplant rejection, and heart attack.
17488724	3	47	theme	inhibitor	424:432	arg1	domain					405:410	the serpin domain	394:410	the serpin domain of human C1 inhibitor	394:432	Here we report the first crystal structure of the serpin domain of human C1 inhibitor, representing a previously unreported latent form, which explains functional consequences of several naturally occurring mutations, two of which are discussed in detail.
17488724	3	47	theme	inhibitor	424:432	arg1	inhibitor					424:432	human C1 inhibitor	415:432	human C1 inhibitor	415:432	Here we report the first crystal structure of the serpin domain of human C1 inhibitor, representing a previously unreported latent form, which explains functional consequences of several naturally occurring mutations, two of which are discussed in detail.
17488724	3	48	theme	serpin	398:403	arg1	domain					405:410	the serpin domain	394:410	the serpin domain of human C1 inhibitor	394:432	Here we report the first crystal structure of the serpin domain of human C1 inhibitor, representing a previously unreported latent form, which explains functional consequences of several naturally occurring mutations, two of which are discussed in detail.
17488724	3	48	theme	serpin	398:403	arg1	inhibitor					424:432	human C1 inhibitor	415:432	human C1 inhibitor	415:432	Here we report the first crystal structure of the serpin domain of human C1 inhibitor, representing a previously unreported latent form, which explains functional consequences of several naturally occurring mutations, two of which are discussed in detail.
17488724	7	49	theme	"	1115:1115	arg1	mechanism					1117:1125	a novel "sandwich" mechanism	1098:1125	a novel "sandwich" mechanism	1098:1125	We show how polyanions change the activity of the C1 inhibitor by a novel "sandwich" mechanism, explaining earlier reaction kinetic and mutagenesis studies.
17488724	4	50	with	conformation	645:656	arg1	A					691:691	a seven-stranded beta-sheet A	663:691	a seven-stranded beta-sheet A	663:691	The presented structure displays a novel conformation with a seven-stranded beta-sheet A.
17488724	1	51	theme	inflammatory	192:203	arg1	processes					205:213	inflammatory processes	192:213	inflammatory processes in blood	192:222	C1 inhibitor, a member of the serpin family, is a major down-regulator of inflammatory processes in blood.
17488724	0	52	theme	likely	49:54	arg1	mechanism					56:64	the likely mechanism	45:64	the likely mechanism of heparin potentiation and conformational disease	45:115	C1 inhibitor serpin domain structure reveals the likely mechanism of heparin potentiation and conformational disease.
17488724	1	53	from	blood	218:222	arg1	down-regulator					174:187	a major down-regulator	166:187	a major down-regulator of inflammatory processes in blood	166:222	C1 inhibitor, a member of the serpin family, is a major down-regulator of inflammatory processes in blood.
17488724	1	53	from	blood	218:222	arg1	inhibitor					121:129	C1 inhibitor	118:129	C1 inhibitor	118:129	C1 inhibitor, a member of the serpin family, is a major down-regulator of inflammatory processes in blood.
17488724	3	54	theme	human	415:419	arg1	inhibitor					424:432	human C1 inhibitor	415:432	human C1 inhibitor	415:432	Here we report the first crystal structure of the serpin domain of human C1 inhibitor, representing a previously unreported latent form, which explains functional consequences of several naturally occurring mutations, two of which are discussed in detail.
17488724	1	55	theme	C1	118:119	arg1	down-regulator					174:187	a major down-regulator	166:187	a major down-regulator of inflammatory processes in blood	166:222	C1 inhibitor, a member of the serpin family, is a major down-regulator of inflammatory processes in blood.
17488724	1	55	theme	C1	118:119	arg1	inhibitor					121:129	C1 inhibitor	118:129	C1 inhibitor	118:129	C1 inhibitor, a member of the serpin family, is a major down-regulator of inflammatory processes in blood.
17488724	1	55	theme	C1	118:119	arg1	member					134:139	a member	132:139	a member of the serpin family	132:160	C1 inhibitor, a member of the serpin family, is a major down-regulator of inflammatory processes in blood.
17488724	6	56	theme	disaccharide	919:930	arg1	measurements					880:891	heparin affinity measurements	863:891	heparin affinity measurements	863:891	On the basis of surface charge pattern, heparin affinity measurements, and docking of a heparin disaccharide, a heparin binding site is proposed in the contact area of the serpin-proteinase encounter complex.
17488724	6	56	theme	disaccharide	919:930	arg1	docking					898:904	docking	898:904	docking of a heparin disaccharide	898:930	On the basis of surface charge pattern, heparin affinity measurements, and docking of a heparin disaccharide, a heparin binding site is proposed in the contact area of the serpin-proteinase encounter complex.
17488724	6	56	theme	disaccharide	919:930	arg1	pattern					854:860	surface charge pattern	839:860	surface charge pattern	839:860	On the basis of surface charge pattern, heparin affinity measurements, and docking of a heparin disaccharide, a heparin binding site is proposed in the contact area of the serpin-proteinase encounter complex.
17488724	7	57	dep	kinetic	1156:1162	arg1	earlier					1139:1145	earlier	1139:1145	earlier	1139:1145	We show how polyanions change the activity of the C1 inhibitor by a novel "sandwich" mechanism, explaining earlier reaction kinetic and mutagenesis studies.
17488724	8	58	theme	angioedema	1297:1306	arg1	treatment					1273:1281	the treatment	1269:1281	the treatment of hereditary angioedema, organ transplant rejection, and heart attack	1269:1352	These results may help to improve therapeutic C1 inhibitor preparations used in the treatment of hereditary angioedema, organ transplant rejection, and heart attack.
17488724	6	59	theme	charge	847:852	arg1	pattern					854:860	surface charge pattern	839:860	surface charge pattern	839:860	On the basis of surface charge pattern, heparin affinity measurements, and docking of a heparin disaccharide, a heparin binding site is proposed in the contact area of the serpin-proteinase encounter complex.
17488724	6	60	theme	heparin	911:917	arg1	disaccharide					919:930	a heparin disaccharide	909:930	a heparin disaccharide	909:930	On the basis of surface charge pattern, heparin affinity measurements, and docking of a heparin disaccharide, a heparin binding site is proposed in the contact area of the serpin-proteinase encounter complex.
17488724	1	61	from	processes	205:213	arg1	blood					218:222	blood	218:222	blood	218:222	C1 inhibitor, a member of the serpin family, is a major down-regulator of inflammatory processes in blood.
17488724	5	62	from	role	772:775	arg1	transition					811:820	the active-latent transition	793:820	the active-latent transition	793:820	The unique conformation of the C-terminal six residues suggests its potential role as a barrier in the active-latent transition.
17488724	2	63	theme	C1	247:248	arg1	inhibitor					250:258	C1 inhibitor	247:258	C1 inhibitor	247:258	Genetic deficiency of C1 inhibitor results in hereditary angioedema, a dominantly inheritable, potentially lethal disease.
17488724	1	64	from	down-regulator	174:187	arg1	blood					218:222	blood	218:222	blood	218:222	C1 inhibitor, a member of the serpin family, is a major down-regulator of inflammatory processes in blood.
17488724	1	65	theme	processes	205:213	arg1	down-regulator					174:187	a major down-regulator	166:187	a major down-regulator of inflammatory processes in blood	166:222	C1 inhibitor, a member of the serpin family, is a major down-regulator of inflammatory processes in blood.
17488724	1	65	theme	processes	205:213	arg1	inhibitor					121:129	C1 inhibitor	118:129	C1 inhibitor	118:129	C1 inhibitor, a member of the serpin family, is a major down-regulator of inflammatory processes in blood.
17488724	8	66	theme	rejection	1326:1334	arg1	treatment					1273:1281	the treatment	1269:1281	the treatment of hereditary angioedema, organ transplant rejection, and heart attack	1269:1352	These results may help to improve therapeutic C1 inhibitor preparations used in the treatment of hereditary angioedema, organ transplant rejection, and heart attack.
17488724	3	67	theme	several	527:533	arg1	mutations					555:563	several naturally occurring mutations	527:563	several naturally occurring mutations	527:563	Here we report the first crystal structure of the serpin domain of human C1 inhibitor, representing a previously unreported latent form, which explains functional consequences of several naturally occurring mutations, two of which are discussed in detail.
17488724	2	68	theme	inheritable	307:317	arg1	angioedema					282:291	hereditary angioedema	271:291	hereditary angioedema	271:291	Genetic deficiency of C1 inhibitor results in hereditary angioedema, a dominantly inheritable, potentially lethal disease.
17488724	2	68	theme	inheritable	307:317	arg1	disease					339:345	a dominantly inheritable, potentially lethal disease	294:345	a dominantly inheritable, potentially lethal disease	294:345	Genetic deficiency of C1 inhibitor results in hereditary angioedema, a dominantly inheritable, potentially lethal disease.
17488724	4	69	theme	seven-stranded	665:678	arg1	A					691:691	a seven-stranded beta-sheet A	663:691	a seven-stranded beta-sheet A	663:691	The presented structure displays a novel conformation with a seven-stranded beta-sheet A.
17488724	6	70	theme	encounter	1013:1021	arg1	complex					1023:1029	the serpin-proteinase encounter complex	991:1029	the serpin-proteinase encounter complex	991:1029	On the basis of surface charge pattern, heparin affinity measurements, and docking of a heparin disaccharide, a heparin binding site is proposed in the contact area of the serpin-proteinase encounter complex.
17488724	8	71	theme	inhibitor	1238:1246	arg1	preparations					1248:1259	therapeutic C1 inhibitor preparations	1223:1259	therapeutic C1 inhibitor preparations used in the treatment of hereditary angioedema, organ transplant rejection, and heart attack	1223:1352	These results may help to improve therapeutic C1 inhibitor preparations used in the treatment of hereditary angioedema, organ transplant rejection, and heart attack.
17488724	8	72	theme	C1	1235:1236	arg1	preparations					1248:1259	therapeutic C1 inhibitor preparations	1223:1259	therapeutic C1 inhibitor preparations used in the treatment of hereditary angioedema, organ transplant rejection, and heart attack	1223:1352	These results may help to improve therapeutic C1 inhibitor preparations used in the treatment of hereditary angioedema, organ transplant rejection, and heart attack.
17488724	4	73	theme	beta-sheet	680:689	arg1	A					691:691	a seven-stranded beta-sheet A	663:691	a seven-stranded beta-sheet A	663:691	The presented structure displays a novel conformation with a seven-stranded beta-sheet A.
17488724	4	74	theme	novel	639:643	arg1	conformation					645:656	a novel conformation	637:656	a novel conformation with a seven-stranded beta-sheet A	637:691	The presented structure displays a novel conformation with a seven-stranded beta-sheet A.
17488724	7	75	theme	novel	1100:1104	arg1	mechanism					1117:1125	a novel "sandwich" mechanism	1098:1125	a novel "sandwich" mechanism	1098:1125	We show how polyanions change the activity of the C1 inhibitor by a novel "sandwich" mechanism, explaining earlier reaction kinetic and mutagenesis studies.
17488724	2	76	theme	Genetic	225:231	arg1	deficiency					233:242	Genetic deficiency	225:242	Genetic deficiency of C1 inhibitor	225:258	Genetic deficiency of C1 inhibitor results in hereditary angioedema, a dominantly inheritable, potentially lethal disease.
17488724	3	77	theme	first	367:371	arg1	structure					381:389	the first crystal structure	363:389	the first crystal structure of the serpin domain of human C1 inhibitor	363:432	Here we report the first crystal structure of the serpin domain of human C1 inhibitor, representing a previously unreported latent form, which explains functional consequences of several naturally occurring mutations, two of which are discussed in detail.
17488724	7	78	theme	mutagenesis	1168:1178	arg1	studies					1180:1186	earlier reaction kinetic and mutagenesis studies	1139:1186	studies	1180:1186	We show how polyanions change the activity of the C1 inhibitor by a novel "sandwich" mechanism, explaining earlier reaction kinetic and mutagenesis studies.
15327282	1	0	theme	cell	169:172	arg1	lysates					174:180	cell lysates	169:180	cell lysates	169:180	We report a new strategy for the parallel identification of O-GlcNAc-glycosylated proteins from cell lysates.
15327282	0	1	from	identification	9:22	arg1	lysates					64:70	cell lysates	59:70	cell lysates	59:70	Parallel identification of O-GlcNAc-modified proteins from cell lysates.
15327282	1	2	from	lysates	174:180	arg1	identification					115:128	the parallel identification	102:128	the parallel identification of O-GlcNAc-glycosylated proteins from cell lysates	102:180	We report a new strategy for the parallel identification of O-GlcNAc-glycosylated proteins from cell lysates.
15327282	1	2	from	lysates	174:180	arg1	proteins					155:162	O-GlcNAc-glycosylated proteins	133:162	O-GlcNAc-glycosylated proteins from cell lysates	133:180	We report a new strategy for the parallel identification of O-GlcNAc-glycosylated proteins from cell lysates.
15327282	2	3	theme	cell	299:302	arg1	type					304:307	any tissue or cell type	285:307	type	304:307	The approach permits specific proteins of interest to be rapidly interrogated for the modification in any tissue or cell type and can be extended to peptides to facilitate the mapping of glycosylation sites.
15327282	0	4	from	lysates	64:70	arg1	identification					9:22	Parallel identification	0:22	Parallel identification of O-GlcNAc-modified proteins from cell lysates.	0:71	Parallel identification of O-GlcNAc-modified proteins from cell lysates.
15327282	0	4	from	lysates	64:70	arg1	proteins					45:52	O-GlcNAc-modified proteins	27:52	O-GlcNAc-modified proteins from cell lysates	27:70	Parallel identification of O-GlcNAc-modified proteins from cell lysates.
15327282	3	5	theme	low	484:486	arg1	abundance					497:505	low cellular abundance	484:505	low cellular abundance (c-Fos, c-Jun, ATF-1, and CBP)	484:536	As an illustration of the approach, we identified four new O-GlcNAc-glycosylated proteins of low cellular abundance (c-Fos, c-Jun, ATF-1, and CBP) and two short regions of glycosylation in the enzyme O-GlcNAc transferase (OGT).
15327282	3	6	theme	cellular	488:495	arg1	abundance					497:505	low cellular abundance	484:505	low cellular abundance (c-Fos, c-Jun, ATF-1, and CBP)	484:536	As an illustration of the approach, we identified four new O-GlcNAc-glycosylated proteins of low cellular abundance (c-Fos, c-Jun, ATF-1, and CBP) and two short regions of glycosylation in the enzyme O-GlcNAc transferase (OGT).
15327282	2	7	theme	tissue	289:294	arg1	type					304:307	any tissue or cell type	285:307	type	304:307	The approach permits specific proteins of interest to be rapidly interrogated for the modification in any tissue or cell type and can be extended to peptides to facilitate the mapping of glycosylation sites.
15327282	3	8	theme	approach	417:424	arg1	illustration					397:408	an illustration	394:408	an illustration of the approach	394:424	As an illustration of the approach, we identified four new O-GlcNAc-glycosylated proteins of low cellular abundance (c-Fos, c-Jun, ATF-1, and CBP) and two short regions of glycosylation in the enzyme O-GlcNAc transferase (OGT).
15327282	3	8	theme	approach	417:424	arg1	regions					552:558	two short regions	542:558	two short regions of glycosylation	542:575	As an illustration of the approach, we identified four new O-GlcNAc-glycosylated proteins of low cellular abundance (c-Fos, c-Jun, ATF-1, and CBP) and two short regions of glycosylation in the enzyme O-GlcNAc transferase (OGT).
15327282	3	8	theme	approach	417:424	arg1	proteins					472:479	four new O-GlcNAc-glycosylated proteins	441:479	four new O-GlcNAc-glycosylated proteins of low cellular abundance (c-Fos, c-Jun, ATF-1, and CBP)	441:536	As an illustration of the approach, we identified four new O-GlcNAc-glycosylated proteins of low cellular abundance (c-Fos, c-Jun, ATF-1, and CBP) and two short regions of glycosylation in the enzyme O-GlcNAc transferase (OGT).
15327282	4	9	theme	important	784:792	arg1	modification					812:823	this important posttranslational modification	779:823	this important posttranslational modification	779:823	The ability to target specific proteins across various tissue or cell types complements emerging proteomic technologies and should advance our understanding of this important posttranslational modification.
15327282	3	10	dep	abundance	497:505	arg1	c-Fos					508:512	c-Fos	508:512	c-Fos	508:512	As an illustration of the approach, we identified four new O-GlcNAc-glycosylated proteins of low cellular abundance (c-Fos, c-Jun, ATF-1, and CBP) and two short regions of glycosylation in the enzyme O-GlcNAc transferase (OGT).
15327282	3	10	dep	abundance	497:505	arg1	ATF-1					522:526	ATF-1	522:526	ATF-1	522:526	As an illustration of the approach, we identified four new O-GlcNAc-glycosylated proteins of low cellular abundance (c-Fos, c-Jun, ATF-1, and CBP) and two short regions of glycosylation in the enzyme O-GlcNAc transferase (OGT).
15327282	3	10	dep	abundance	497:505	arg1	CBP					533:535	CBP	533:535	CBP	533:535	As an illustration of the approach, we identified four new O-GlcNAc-glycosylated proteins of low cellular abundance (c-Fos, c-Jun, ATF-1, and CBP) and two short regions of glycosylation in the enzyme O-GlcNAc transferase (OGT).
15327282	3	10	dep	abundance	497:505	arg1	c-Jun					515:519	c-Jun	515:519	c-Jun	515:519	As an illustration of the approach, we identified four new O-GlcNAc-glycosylated proteins of low cellular abundance (c-Fos, c-Jun, ATF-1, and CBP) and two short regions of glycosylation in the enzyme O-GlcNAc transferase (OGT).
15327282	2	11	gly	glycosylation	370:382	arg2	sites					384:388	glycosylation sites	370:388	glycosylation sites	370:388	The approach permits specific proteins of interest to be rapidly interrogated for the modification in any tissue or cell type and can be extended to peptides to facilitate the mapping of glycosylation sites.
15327282	1	12	theme	new	85:87	arg1	strategy					89:96	a new strategy	83:96	a new strategy for the parallel identification of O-GlcNAc-glycosylated proteins from cell lysates	83:180	We report a new strategy for the parallel identification of O-GlcNAc-glycosylated proteins from cell lysates.
15327282	2	13	theme	sites	384:388	arg1	mapping					359:365	the mapping	355:365	the mapping of glycosylation sites	355:388	The approach permits specific proteins of interest to be rapidly interrogated for the modification in any tissue or cell type and can be extended to peptides to facilitate the mapping of glycosylation sites.
15327282	0	14	theme	Parallel	0:7	arg1	identification					9:22	Parallel identification	0:22	Parallel identification of O-GlcNAc-modified proteins from cell lysates.	0:71	Parallel identification of O-GlcNAc-modified proteins from cell lysates.
15327282	2	15	theme	glycosylation	370:382	arg1	sites					384:388	glycosylation sites	370:388	glycosylation sites	370:388	The approach permits specific proteins of interest to be rapidly interrogated for the modification in any tissue or cell type and can be extended to peptides to facilitate the mapping of glycosylation sites.
15327282	0	16	theme	O-GlcNAc-modified	27:43	arg1	proteins					45:52	O-GlcNAc-modified proteins	27:52	O-GlcNAc-modified proteins from cell lysates	27:70	Parallel identification of O-GlcNAc-modified proteins from cell lysates.
15327282	1	17	from	identification	115:128	arg1	lysates					174:180	cell lysates	169:180	cell lysates	169:180	We report a new strategy for the parallel identification of O-GlcNAc-glycosylated proteins from cell lysates.
15327282	4	18	theme	proteomic	716:724	arg1	technologies					726:737	emerging proteomic technologies	707:737	emerging proteomic technologies	707:737	The ability to target specific proteins across various tissue or cell types complements emerging proteomic technologies and should advance our understanding of this important posttranslational modification.
15327282	3	19	theme	O-GlcNAc-glycosylated	450:470	arg1	illustration					397:408	an illustration	394:408	an illustration of the approach	394:424	As an illustration of the approach, we identified four new O-GlcNAc-glycosylated proteins of low cellular abundance (c-Fos, c-Jun, ATF-1, and CBP) and two short regions of glycosylation in the enzyme O-GlcNAc transferase (OGT).
15327282	3	19	theme	O-GlcNAc-glycosylated	450:470	arg1	regions					552:558	two short regions	542:558	two short regions of glycosylation	542:575	As an illustration of the approach, we identified four new O-GlcNAc-glycosylated proteins of low cellular abundance (c-Fos, c-Jun, ATF-1, and CBP) and two short regions of glycosylation in the enzyme O-GlcNAc transferase (OGT).
15327282	3	19	theme	O-GlcNAc-glycosylated	450:470	arg1	proteins					472:479	four new O-GlcNAc-glycosylated proteins	441:479	four new O-GlcNAc-glycosylated proteins of low cellular abundance (c-Fos, c-Jun, ATF-1, and CBP)	441:536	As an illustration of the approach, we identified four new O-GlcNAc-glycosylated proteins of low cellular abundance (c-Fos, c-Jun, ATF-1, and CBP) and two short regions of glycosylation in the enzyme O-GlcNAc transferase (OGT).
15327282	4	20	theme	emerging	707:714	arg1	technologies					726:737	emerging proteomic technologies	707:737	emerging proteomic technologies	707:737	The ability to target specific proteins across various tissue or cell types complements emerging proteomic technologies and should advance our understanding of this important posttranslational modification.
15327282	4	21	theme	specific	641:648	arg1	proteins					650:657	specific proteins	641:657	specific proteins	641:657	The ability to target specific proteins across various tissue or cell types complements emerging proteomic technologies and should advance our understanding of this important posttranslational modification.
15327282	4	22	theme	various	666:672	arg1	tissue					674:679	various tissue or cell types	666:693	tissue	674:679	The ability to target specific proteins across various tissue or cell types complements emerging proteomic technologies and should advance our understanding of this important posttranslational modification.
15327282	1	23	gly	O-GlcNAc-glycosylated	133:153	arg1	proteins					155:162	O-GlcNAc-glycosylated proteins	133:162	O-GlcNAc-glycosylated proteins from cell lysates	133:180	We report a new strategy for the parallel identification of O-GlcNAc-glycosylated proteins from cell lysates.
15327282	4	24	theme	posttranslational	794:810	arg1	modification					812:823	this important posttranslational modification	779:823	this important posttranslational modification	779:823	The ability to target specific proteins across various tissue or cell types complements emerging proteomic technologies and should advance our understanding of this important posttranslational modification.
15327282	2	25	from	modification	269:280	arg1	type					304:307	any tissue or cell type	285:307	type	304:307	The approach permits specific proteins of interest to be rapidly interrogated for the modification in any tissue or cell type and can be extended to peptides to facilitate the mapping of glycosylation sites.
15327282	0	26	theme	proteins	45:52	arg1	identification					9:22	Parallel identification	0:22	Parallel identification of O-GlcNAc-modified proteins from cell lysates.	0:71	Parallel identification of O-GlcNAc-modified proteins from cell lysates.
15327282	3	27	gly	O-GlcNAc-glycosylated	450:470	arg1	illustration					397:408	an illustration	394:408	an illustration of the approach	394:424	As an illustration of the approach, we identified four new O-GlcNAc-glycosylated proteins of low cellular abundance (c-Fos, c-Jun, ATF-1, and CBP) and two short regions of glycosylation in the enzyme O-GlcNAc transferase (OGT).
15327282	3	27	gly	O-GlcNAc-glycosylated	450:470	arg1	regions					552:558	two short regions	542:558	two short regions of glycosylation	542:575	As an illustration of the approach, we identified four new O-GlcNAc-glycosylated proteins of low cellular abundance (c-Fos, c-Jun, ATF-1, and CBP) and two short regions of glycosylation in the enzyme O-GlcNAc transferase (OGT).
15327282	3	27	gly	O-GlcNAc-glycosylated	450:470	arg1	proteins					472:479	four new O-GlcNAc-glycosylated proteins	441:479	four new O-GlcNAc-glycosylated proteins of low cellular abundance (c-Fos, c-Jun, ATF-1, and CBP)	441:536	As an illustration of the approach, we identified four new O-GlcNAc-glycosylated proteins of low cellular abundance (c-Fos, c-Jun, ATF-1, and CBP) and two short regions of glycosylation in the enzyme O-GlcNAc transferase (OGT).
15327282	3	28	theme	new	446:448	arg1	illustration					397:408	an illustration	394:408	an illustration of the approach	394:424	As an illustration of the approach, we identified four new O-GlcNAc-glycosylated proteins of low cellular abundance (c-Fos, c-Jun, ATF-1, and CBP) and two short regions of glycosylation in the enzyme O-GlcNAc transferase (OGT).
15327282	3	28	theme	new	446:448	arg1	regions					552:558	two short regions	542:558	two short regions of glycosylation	542:575	As an illustration of the approach, we identified four new O-GlcNAc-glycosylated proteins of low cellular abundance (c-Fos, c-Jun, ATF-1, and CBP) and two short regions of glycosylation in the enzyme O-GlcNAc transferase (OGT).
15327282	3	28	theme	new	446:448	arg1	proteins					472:479	four new O-GlcNAc-glycosylated proteins	441:479	four new O-GlcNAc-glycosylated proteins of low cellular abundance (c-Fos, c-Jun, ATF-1, and CBP)	441:536	As an illustration of the approach, we identified four new O-GlcNAc-glycosylated proteins of low cellular abundance (c-Fos, c-Jun, ATF-1, and CBP) and two short regions of glycosylation in the enzyme O-GlcNAc transferase (OGT).
15327282	3	29	theme	short	546:550	arg1	illustration					397:408	an illustration	394:408	an illustration of the approach	394:424	As an illustration of the approach, we identified four new O-GlcNAc-glycosylated proteins of low cellular abundance (c-Fos, c-Jun, ATF-1, and CBP) and two short regions of glycosylation in the enzyme O-GlcNAc transferase (OGT).
15327282	3	29	theme	short	546:550	arg1	regions					552:558	two short regions	542:558	two short regions of glycosylation	542:575	As an illustration of the approach, we identified four new O-GlcNAc-glycosylated proteins of low cellular abundance (c-Fos, c-Jun, ATF-1, and CBP) and two short regions of glycosylation in the enzyme O-GlcNAc transferase (OGT).
15327282	3	29	theme	short	546:550	arg1	proteins					472:479	four new O-GlcNAc-glycosylated proteins	441:479	four new O-GlcNAc-glycosylated proteins of low cellular abundance (c-Fos, c-Jun, ATF-1, and CBP)	441:536	As an illustration of the approach, we identified four new O-GlcNAc-glycosylated proteins of low cellular abundance (c-Fos, c-Jun, ATF-1, and CBP) and two short regions of glycosylation in the enzyme O-GlcNAc transferase (OGT).
15327282	1	30	theme	parallel	106:113	arg1	identification					115:128	the parallel identification	102:128	the parallel identification of O-GlcNAc-glycosylated proteins from cell lysates	102:180	We report a new strategy for the parallel identification of O-GlcNAc-glycosylated proteins from cell lysates.
15327282	0	31	theme	cell	59:62	arg1	lysates					64:70	cell lysates	59:70	cell lysates	59:70	Parallel identification of O-GlcNAc-modified proteins from cell lysates.
15327282	2	32	theme	interest	225:232	arg1	proteins					213:220	specific proteins	204:220	specific proteins of interest	204:232	The approach permits specific proteins of interest to be rapidly interrogated for the modification in any tissue or cell type and can be extended to peptides to facilitate the mapping of glycosylation sites.
15327282	4	33	theme	modification	812:823	arg1	understanding					762:774	our understanding	758:774	our understanding of this important posttranslational modification	758:823	The ability to target specific proteins across various tissue or cell types complements emerging proteomic technologies and should advance our understanding of this important posttranslational modification.
15327282	3	34	theme	abundance	497:505	arg1	illustration					397:408	an illustration	394:408	an illustration of the approach	394:424	As an illustration of the approach, we identified four new O-GlcNAc-glycosylated proteins of low cellular abundance (c-Fos, c-Jun, ATF-1, and CBP) and two short regions of glycosylation in the enzyme O-GlcNAc transferase (OGT).
15327282	3	34	theme	abundance	497:505	arg1	regions					552:558	two short regions	542:558	two short regions of glycosylation	542:575	As an illustration of the approach, we identified four new O-GlcNAc-glycosylated proteins of low cellular abundance (c-Fos, c-Jun, ATF-1, and CBP) and two short regions of glycosylation in the enzyme O-GlcNAc transferase (OGT).
15327282	3	34	theme	abundance	497:505	arg1	proteins					472:479	four new O-GlcNAc-glycosylated proteins	441:479	four new O-GlcNAc-glycosylated proteins of low cellular abundance (c-Fos, c-Jun, ATF-1, and CBP)	441:536	As an illustration of the approach, we identified four new O-GlcNAc-glycosylated proteins of low cellular abundance (c-Fos, c-Jun, ATF-1, and CBP) and two short regions of glycosylation in the enzyme O-GlcNAc transferase (OGT).
15327282	3	35	theme	enzyme	584:589	arg1	OGT					613:615	OGT	613:615	OGT	613:615	As an illustration of the approach, we identified four new O-GlcNAc-glycosylated proteins of low cellular abundance (c-Fos, c-Jun, ATF-1, and CBP) and two short regions of glycosylation in the enzyme O-GlcNAc transferase (OGT).
15327282	3	35	theme	enzyme	584:589	arg1	transferase					600:610	the enzyme O-GlcNAc transferase	580:610	the enzyme O-GlcNAc transferase (OGT)	580:616	As an illustration of the approach, we identified four new O-GlcNAc-glycosylated proteins of low cellular abundance (c-Fos, c-Jun, ATF-1, and CBP) and two short regions of glycosylation in the enzyme O-GlcNAc transferase (OGT).
15327282	3	36	theme	glycosylation	563:575	arg1	illustration					397:408	an illustration	394:408	an illustration of the approach	394:424	As an illustration of the approach, we identified four new O-GlcNAc-glycosylated proteins of low cellular abundance (c-Fos, c-Jun, ATF-1, and CBP) and two short regions of glycosylation in the enzyme O-GlcNAc transferase (OGT).
15327282	3	36	theme	glycosylation	563:575	arg1	regions					552:558	two short regions	542:558	two short regions of glycosylation	542:575	As an illustration of the approach, we identified four new O-GlcNAc-glycosylated proteins of low cellular abundance (c-Fos, c-Jun, ATF-1, and CBP) and two short regions of glycosylation in the enzyme O-GlcNAc transferase (OGT).
15327282	3	36	theme	glycosylation	563:575	arg1	proteins					472:479	four new O-GlcNAc-glycosylated proteins	441:479	four new O-GlcNAc-glycosylated proteins of low cellular abundance (c-Fos, c-Jun, ATF-1, and CBP)	441:536	As an illustration of the approach, we identified four new O-GlcNAc-glycosylated proteins of low cellular abundance (c-Fos, c-Jun, ATF-1, and CBP) and two short regions of glycosylation in the enzyme O-GlcNAc transferase (OGT).
15327282	4	37	theme	cell	684:687	arg1	types					689:693	various tissue or cell types	666:693	types	689:693	The ability to target specific proteins across various tissue or cell types complements emerging proteomic technologies and should advance our understanding of this important posttranslational modification.
15327282	3	38	theme	O-GlcNAc	591:598	arg1	OGT					613:615	OGT	613:615	OGT	613:615	As an illustration of the approach, we identified four new O-GlcNAc-glycosylated proteins of low cellular abundance (c-Fos, c-Jun, ATF-1, and CBP) and two short regions of glycosylation in the enzyme O-GlcNAc transferase (OGT).
15327282	3	38	theme	O-GlcNAc	591:598	arg1	transferase					600:610	the enzyme O-GlcNAc transferase	580:610	the enzyme O-GlcNAc transferase (OGT)	580:616	As an illustration of the approach, we identified four new O-GlcNAc-glycosylated proteins of low cellular abundance (c-Fos, c-Jun, ATF-1, and CBP) and two short regions of glycosylation in the enzyme O-GlcNAc transferase (OGT).
15327282	1	39	theme	O-GlcNAc-glycosylated	133:153	arg1	proteins					155:162	O-GlcNAc-glycosylated proteins	133:162	O-GlcNAc-glycosylated proteins from cell lysates	133:180	We report a new strategy for the parallel identification of O-GlcNAc-glycosylated proteins from cell lysates.
15327282	2	40	theme	specific	204:211	arg1	proteins					213:220	specific proteins	204:220	specific proteins of interest	204:232	The approach permits specific proteins of interest to be rapidly interrogated for the modification in any tissue or cell type and can be extended to peptides to facilitate the mapping of glycosylation sites.
15327282	1	41	theme	proteins	155:162	arg1	identification					115:128	the parallel identification	102:128	the parallel identification of O-GlcNAc-glycosylated proteins from cell lysates	102:180	We report a new strategy for the parallel identification of O-GlcNAc-glycosylated proteins from cell lysates.
10585855	0	0	theme	human	95:99	arg1	band					127:130	band 3	127:132	band 3	127:132	Topology studies with biosynthetic fragments identify interacting transmembrane regions of the human red-cell anion exchanger (band 3; AE1).
10585855	0	0	theme	human	95:99	arg1	exchanger					116:124	the human red-cell anion exchanger	91:124	the human red-cell anion exchanger (band 3; AE1)	91:138	Topology studies with biosynthetic fragments identify interacting transmembrane regions of the human red-cell anion exchanger (band 3; AE1).
10585855	1	1	dep	14	253:254	arg1	to					250:251	to	250:251	to	250:251	The red-cell anion exchanger (band 3; AE1) is a multispanning membrane protein that traverses the bilayer up to 14 times and is N-glycosylated at Asn-642.
10585855	7	2	dep	region	1202:1207	arg1	the					1171:1173	the	1171:1173	the	1171:1173	The results suggest the span 8 region is required for the correct folding of spans 9-10, at least in the presence of the span 11-12 region.
10585855	7	2	dep	region	1202:1207	arg1	presence					1175:1182	presence	1175:1182	presence	1175:1182	The results suggest the span 8 region is required for the correct folding of spans 9-10, at least in the presence of the span 11-12 region.
10585855	3	3	theme	N-glycosylation	453:467	arg1	approach					481:488	an N-glycosylation mutagenesis approach	450:488	an N-glycosylation mutagenesis approach	450:488	We used an N-glycosylation mutagenesis approach to examine the orientation of the N-terminus and the endogenous glycosylation site of each C-terminal fragment by cell-free translation.
10585855	6	4	theme	luminal	954:960	arg1	exposure					962:969	the luminal exposure	950:969	the luminal exposure of the C-terminus of span 7	950:997	The correct integration of spans 2-3 required the presence of the region containing span 4 and that the luminal exposure of the C-terminus of span 7 is increased in the presence of the region including span 6 or span 8.
10585855	2	5	theme	different	336:344	arg1	loops					346:350	six different loops	332:350	six different loops	332:350	We have shown that the integrity of six different loops are not essential for stilbene disulphonate-sensitive chloride uptake in Xenopus oocytes.
10585855	1	6	theme	red-cell	145:152	arg1	band					171:174	band 3	171:176	band 3	171:176	The red-cell anion exchanger (band 3; AE1) is a multispanning membrane protein that traverses the bilayer up to 14 times and is N-glycosylated at Asn-642.
10585855	1	6	theme	red-cell	145:152	arg1	exchanger					160:168	The red-cell anion exchanger	141:168	The red-cell anion exchanger (band 3; AE1)	141:182	The red-cell anion exchanger (band 3; AE1) is a multispanning membrane protein that traverses the bilayer up to 14 times and is N-glycosylated at Asn-642.
10585855	1	6	theme	red-cell	145:152	arg1	protein					212:218	a multispanning membrane protein	187:218	a multispanning membrane protein that traverses the bilayer up to 14 times and is N-glycosylated at Asn-642	187:293	The red-cell anion exchanger (band 3; AE1) is a multispanning membrane protein that traverses the bilayer up to 14 times and is N-glycosylated at Asn-642.
10585855	1	6	theme	red-cell	145:152	arg1	N-glycosylated					269:282	N-glycosylated	269:282	N-glycosylated	269:282	The red-cell anion exchanger (band 3; AE1) is a multispanning membrane protein that traverses the bilayer up to 14 times and is N-glycosylated at Asn-642.
10585855	0	7	theme	anion	110:114	arg1	band					127:130	band 3	127:132	band 3	127:132	Topology studies with biosynthetic fragments identify interacting transmembrane regions of the human red-cell anion exchanger (band 3; AE1).
10585855	0	7	theme	anion	110:114	arg1	exchanger					116:124	the human red-cell anion exchanger	91:124	the human red-cell anion exchanger (band 3; AE1)	91:138	Topology studies with biosynthetic fragments identify interacting transmembrane regions of the human red-cell anion exchanger (band 3; AE1).
10585855	10	8	theme	polytopic	1588:1596	arg1	proteins					1607:1614	polytopic membrane proteins	1588:1614	polytopic membrane proteins	1588:1614	This approach might provide a general method for dissecting the interactions between membrane-spanning regions of polytopic membrane proteins.
10585855	3	9	theme	N-terminus	524:533	arg1	orientation					505:515	the orientation	501:515	the orientation of the N-terminus and the endogenous glycosylation site of each C-terminal fragment by cell-free translation	501:624	We used an N-glycosylation mutagenesis approach to examine the orientation of the N-terminus and the endogenous glycosylation site of each C-terminal fragment by cell-free translation.
10585855	0	10	theme	red-cell	101:108	arg1	band					127:130	band 3	127:132	band 3	127:132	Topology studies with biosynthetic fragments identify interacting transmembrane regions of the human red-cell anion exchanger (band 3; AE1).
10585855	0	10	theme	red-cell	101:108	arg1	exchanger					116:124	the human red-cell anion exchanger	91:124	the human red-cell anion exchanger (band 3; AE1)	91:138	Topology studies with biosynthetic fragments identify interacting transmembrane regions of the human red-cell anion exchanger (band 3; AE1).
10585855	10	11	theme	membrane-spanning	1559:1575	arg1	regions					1577:1583	membrane-spanning regions	1559:1583	membrane-spanning regions of polytopic membrane proteins	1559:1614	This approach might provide a general method for dissecting the interactions between membrane-spanning regions of polytopic membrane proteins.
10585855	2	12	theme	stilbene	374:381	arg1	uptake					415:420	stilbene disulphonate-sensitive chloride uptake	374:420	stilbene disulphonate-sensitive chloride uptake in Xenopus oocytes	374:439	We have shown that the integrity of six different loops are not essential for stilbene disulphonate-sensitive chloride uptake in Xenopus oocytes.
10585855	8	13	dep	1	1316:1316	arg1	9-10					1358:1361	9-10	1358:1361	9-10	1358:1361	Our results suggest that there are intramolecular interactions between the regions of transmembrane spans 1 and 2, 2 and 4, 4 and 5, 7 and 8, 8 and 9-10, and 9-10 and 11-12.
10585855	8	13	dep	1	1316:1316	arg1	7					1343:1343	7	1343:1343	7	1343:1343	Our results suggest that there are intramolecular interactions between the regions of transmembrane spans 1 and 2, 2 and 4, 4 and 5, 7 and 8, 8 and 9-10, and 9-10 and 11-12.
10585855	8	13	dep	1	1316:1316	arg1	8					1349:1349	8	1349:1349	8	1349:1349	Our results suggest that there are intramolecular interactions between the regions of transmembrane spans 1 and 2, 2 and 4, 4 and 5, 7 and 8, 8 and 9-10, and 9-10 and 11-12.
10585855	8	13	dep	1	1316:1316	arg1	4					1334:1334	4	1334:1334	4	1334:1334	Our results suggest that there are intramolecular interactions between the regions of transmembrane spans 1 and 2, 2 and 4, 4 and 5, 7 and 8, 8 and 9-10, and 9-10 and 11-12.
10585855	8	13	dep	1	1316:1316	arg1	5					1340:1340	5	1340:1340	5	1340:1340	Our results suggest that there are intramolecular interactions between the regions of transmembrane spans 1 and 2, 2 and 4, 4 and 5, 7 and 8, 8 and 9-10, and 9-10 and 11-12.
10585855	8	13	dep	1	1316:1316	arg1	8					1352:1352	8	1352:1352	8	1352:1352	Our results suggest that there are intramolecular interactions between the regions of transmembrane spans 1 and 2, 2 and 4, 4 and 5, 7 and 8, 8 and 9-10, and 9-10 and 11-12.
10585855	2	14	from	uptake	415:420	arg1	oocytes					433:439	Xenopus oocytes	425:439	Xenopus oocytes	425:439	We have shown that the integrity of six different loops are not essential for stilbene disulphonate-sensitive chloride uptake in Xenopus oocytes.
10585855	1	15	theme	anion	154:158	arg1	band					171:174	band 3	171:176	band 3	171:176	The red-cell anion exchanger (band 3; AE1) is a multispanning membrane protein that traverses the bilayer up to 14 times and is N-glycosylated at Asn-642.
10585855	1	15	theme	anion	154:158	arg1	exchanger					160:168	The red-cell anion exchanger	141:168	The red-cell anion exchanger (band 3; AE1)	141:182	The red-cell anion exchanger (band 3; AE1) is a multispanning membrane protein that traverses the bilayer up to 14 times and is N-glycosylated at Asn-642.
10585855	1	15	theme	anion	154:158	arg1	protein					212:218	a multispanning membrane protein	187:218	a multispanning membrane protein that traverses the bilayer up to 14 times and is N-glycosylated at Asn-642	187:293	The red-cell anion exchanger (band 3; AE1) is a multispanning membrane protein that traverses the bilayer up to 14 times and is N-glycosylated at Asn-642.
10585855	1	15	theme	anion	154:158	arg1	N-glycosylated					269:282	N-glycosylated	269:282	N-glycosylated	269:282	The red-cell anion exchanger (band 3; AE1) is a multispanning membrane protein that traverses the bilayer up to 14 times and is N-glycosylated at Asn-642.
10585855	0	16	theme	exchanger	116:124	arg1	regions					80:86	interacting transmembrane regions	54:86	interacting transmembrane regions of the human red-cell anion exchanger (band 3; AE1)	54:138	Topology studies with biosynthetic fragments identify interacting transmembrane regions of the human red-cell anion exchanger (band 3; AE1).
10585855	8	17	dep	regions	1285:1291	arg1	spans					1310:1314	spans	1310:1314	spans 1 and 2, 2 and 4, 4 and 5, 7 and 8, 8 and 9-10, and 9-10 and 11-12	1310:1381	Our results suggest that there are intramolecular interactions between the regions of transmembrane spans 1 and 2, 2 and 4, 4 and 5, 7 and 8, 8 and 9-10, and 9-10 and 11-12.
10585855	2	18	theme	disulphonate-sensitive	383:404	arg1	uptake					415:420	stilbene disulphonate-sensitive chloride uptake	374:420	stilbene disulphonate-sensitive chloride uptake in Xenopus oocytes	374:439	We have shown that the integrity of six different loops are not essential for stilbene disulphonate-sensitive chloride uptake in Xenopus oocytes.
10585855	2	19	theme	chloride	406:413	arg1	uptake					415:420	stilbene disulphonate-sensitive chloride uptake	374:420	stilbene disulphonate-sensitive chloride uptake in Xenopus oocytes	374:439	We have shown that the integrity of six different loops are not essential for stilbene disulphonate-sensitive chloride uptake in Xenopus oocytes.
10585855	7	20	theme	correct	1128:1134	arg1	folding					1136:1142	the correct folding	1124:1142	the correct folding of spans 9-10, at least in the presence of the span 11-12 region	1124:1207	The results suggest the span 8 region is required for the correct folding of spans 9-10, at least in the presence of the span 11-12 region.
10585855	6	21	theme	correct	854:860	arg1	integration					862:872	The correct integration	850:872	The correct integration of	850:875	The correct integration of spans 2-3 required the presence of the region containing span 4 and that the luminal exposure of the C-terminus of span 7 is increased in the presence of the region including span 6 or span 8.
10585855	5	22	theme	span	842:845	arg1	integration					827:837	the membrane integration	814:837	the membrane integration of span 7	814:847	Furthermore, N-glycosylation of Asn-642 might facilitate the membrane integration of span 7.
10585855	0	23	theme	Topology	0:7	arg1	studies					9:15	Topology studies	0:15	Topology studies with biosynthetic fragments	0:43	Topology studies with biosynthetic fragments identify interacting transmembrane regions of the human red-cell anion exchanger (band 3; AE1).
10585855	1	24	theme	bilayer	239:245	arg1	times					256:260	the bilayer up to 14 times	235:260	the bilayer up to 14 times	235:260	The red-cell anion exchanger (band 3; AE1) is a multispanning membrane protein that traverses the bilayer up to 14 times and is N-glycosylated at Asn-642.
10585855	8	25	theme	intramolecular	1245:1258	arg1	interactions					1260:1271	intramolecular interactions	1245:1271	intramolecular interactions between the regions of transmembrane spans 1 and 2, 2 and 4, 4 and 5, 7 and 8, 8 and 9-10, and 9-10 and 11-12	1245:1381	Our results suggest that there are intramolecular interactions between the regions of transmembrane spans 1 and 2, 2 and 4, 4 and 5, 7 and 8, 8 and 9-10, and 9-10 and 11-12.
10585855	0	26	theme	interacting	54:64	arg1	regions					80:86	interacting transmembrane regions	54:86	interacting transmembrane regions of the human red-cell anion exchanger (band 3; AE1)	54:138	Topology studies with biosynthetic fragments identify interacting transmembrane regions of the human red-cell anion exchanger (band 3; AE1).
10585855	0	27	theme	biosynthetic	22:33	arg1	fragments					35:43	biosynthetic fragments	22:43	biosynthetic fragments	22:43	Topology studies with biosynthetic fragments identify interacting transmembrane regions of the human red-cell anion exchanger (band 3; AE1).
10585855	3	28	theme	glycosylation	554:566	arg1	site					568:571	the endogenous glycosylation site	539:571	the endogenous glycosylation site of each C-terminal fragment	539:599	We used an N-glycosylation mutagenesis approach to examine the orientation of the N-terminus and the endogenous glycosylation site of each C-terminal fragment by cell-free translation.
10585855	3	28	theme	glycosylation	554:566	arg1	fragment					592:599	each C-terminal fragment	576:599	each C-terminal fragment	576:599	We used an N-glycosylation mutagenesis approach to examine the orientation of the N-terminus and the endogenous glycosylation site of each C-terminal fragment by cell-free translation.
10585855	5	29	gly	N-glycosylation	770:784	arg1	Asn-642					789:795	Asn-642	789:795	Asn-642	789:795	Furthermore, N-glycosylation of Asn-642 might facilitate the membrane integration of span 7.
10585855	7	30	theme	span	1191:1194	arg1	region					1202:1207	the span 11-12 region	1187:1207	the span 11-12 region	1187:1207	The results suggest the span 8 region is required for the correct folding of spans 9-10, at least in the presence of the span 11-12 region.
10585855	5	31	theme	Asn-642	789:795	arg1	N-glycosylation					770:784	N-glycosylation	770:784	N-glycosylation of Asn-642	770:795	Furthermore, N-glycosylation of Asn-642 might facilitate the membrane integration of span 7.
10585855	4	32	with	membrane	717:724	arg1	orientation					744:754	the expected orientation	731:754	the expected orientation	731:754	The fragments initiating in the loops preceding spans 2, 9 and 11 did not insert into the membrane with the expected orientation.
10585855	0	33	dep	band	127:130	arg1	AE1					135:137	AE1	135:137	AE1	135:137	Topology studies with biosynthetic fragments identify interacting transmembrane regions of the human red-cell anion exchanger (band 3; AE1).
10585855	7	34	theme	11-12	1196:1200	arg1	region					1202:1207	the span 11-12 region	1187:1207	the span 11-12 region	1187:1207	The results suggest the span 8 region is required for the correct folding of spans 9-10, at least in the presence of the span 11-12 region.
10585855	6	35	theme	region	916:921	arg1	presence					900:907	the presence	896:907	the presence of the region containing span 4	896:939	The correct integration of spans 2-3 required the presence of the region containing span 4 and that the luminal exposure of the C-terminus of span 7 is increased in the presence of the region including span 6 or span 8.
10585855	6	36	theme	span	992:995	arg1	C-terminus					978:987	the C-terminus	974:987	the C-terminus of span 7	974:997	The correct integration of spans 2-3 required the presence of the region containing span 4 and that the luminal exposure of the C-terminus of span 7 is increased in the presence of the region including span 6 or span 8.
10585855	3	37	theme	site	568:571	arg1	orientation					505:515	the orientation	501:515	the orientation of the N-terminus and the endogenous glycosylation site of each C-terminal fragment by cell-free translation	501:624	We used an N-glycosylation mutagenesis approach to examine the orientation of the N-terminus and the endogenous glycosylation site of each C-terminal fragment by cell-free translation.
10585855	3	38	gly	glycosylation	554:566	arg2	fragment					592:599	each C-terminal fragment	576:599	each C-terminal fragment	576:599	We used an N-glycosylation mutagenesis approach to examine the orientation of the N-terminus and the endogenous glycosylation site of each C-terminal fragment by cell-free translation.
10585855	3	38	gly	glycosylation	554:566	arg1	fragment					592:599	each C-terminal fragment	576:599	each C-terminal fragment	576:599	We used an N-glycosylation mutagenesis approach to examine the orientation of the N-terminus and the endogenous glycosylation site of each C-terminal fragment by cell-free translation.
10585855	3	38	gly	glycosylation	554:566	arg2	site					568:571	the endogenous glycosylation site	539:571	the endogenous glycosylation site of each C-terminal fragment	539:599	We used an N-glycosylation mutagenesis approach to examine the orientation of the N-terminus and the endogenous glycosylation site of each C-terminal fragment by cell-free translation.
10585855	2	39	theme	Xenopus	425:431	arg1	oocytes					433:439	Xenopus oocytes	425:439	Xenopus oocytes	425:439	We have shown that the integrity of six different loops are not essential for stilbene disulphonate-sensitive chloride uptake in Xenopus oocytes.
10585855	3	40	theme	cell-free	604:612	arg1	translation					614:624	cell-free translation	604:624	cell-free translation	604:624	We used an N-glycosylation mutagenesis approach to examine the orientation of the N-terminus and the endogenous glycosylation site of each C-terminal fragment by cell-free translation.
10585855	1	41	dep	band	171:174	arg1	AE1					179:181	AE1	179:181	AE1	179:181	The red-cell anion exchanger (band 3; AE1) is a multispanning membrane protein that traverses the bilayer up to 14 times and is N-glycosylated at Asn-642.
10585855	2	42	theme	loops	346:350	arg1	integrity					319:327	the integrity	315:327	the integrity of six different loops	315:350	We have shown that the integrity of six different loops are not essential for stilbene disulphonate-sensitive chloride uptake in Xenopus oocytes.
10585855	2	42	theme	loops	346:350	arg1	essential					360:368	essential	360:368	essential	360:368	We have shown that the integrity of six different loops are not essential for stilbene disulphonate-sensitive chloride uptake in Xenopus oocytes.
10585855	0	43	theme	transmembrane	66:78	arg1	regions					80:86	interacting transmembrane regions	54:86	interacting transmembrane regions of the human red-cell anion exchanger (band 3; AE1)	54:138	Topology studies with biosynthetic fragments identify interacting transmembrane regions of the human red-cell anion exchanger (band 3; AE1).
10585855	10	44	theme	proteins	1607:1614	arg1	regions					1577:1583	membrane-spanning regions	1559:1583	membrane-spanning regions of polytopic membrane proteins	1559:1614	This approach might provide a general method for dissecting the interactions between membrane-spanning regions of polytopic membrane proteins.
10585855	3	45	theme	endogenous	543:552	arg1	site					568:571	the endogenous glycosylation site	539:571	the endogenous glycosylation site of each C-terminal fragment	539:599	We used an N-glycosylation mutagenesis approach to examine the orientation of the N-terminus and the endogenous glycosylation site of each C-terminal fragment by cell-free translation.
10585855	3	45	theme	endogenous	543:552	arg1	fragment					592:599	each C-terminal fragment	576:599	each C-terminal fragment	576:599	We used an N-glycosylation mutagenesis approach to examine the orientation of the N-terminus and the endogenous glycosylation site of each C-terminal fragment by cell-free translation.
10585855	1	46	from	Asn-642	287:293	arg1	exchanger					160:168	The red-cell anion exchanger	141:168	The red-cell anion exchanger (band 3; AE1)	141:182	The red-cell anion exchanger (band 3; AE1) is a multispanning membrane protein that traverses the bilayer up to 14 times and is N-glycosylated at Asn-642.
10585855	1	46	from	Asn-642	287:293	arg1	protein					212:218	a multispanning membrane protein	187:218	a multispanning membrane protein that traverses the bilayer up to 14 times and is N-glycosylated at Asn-642	187:293	The red-cell anion exchanger (band 3; AE1) is a multispanning membrane protein that traverses the bilayer up to 14 times and is N-glycosylated at Asn-642.
10585855	1	46	from	Asn-642	287:293	arg1	N-glycosylated					269:282	N-glycosylated	269:282	N-glycosylated	269:282	The red-cell anion exchanger (band 3; AE1) is a multispanning membrane protein that traverses the bilayer up to 14 times and is N-glycosylated at Asn-642.
10585855	10	47	theme	membrane	1598:1605	arg1	proteins					1607:1614	polytopic membrane proteins	1588:1614	polytopic membrane proteins	1588:1614	This approach might provide a general method for dissecting the interactions between membrane-spanning regions of polytopic membrane proteins.
10585855	3	48	used	used	445:448	arg2	We					442:443	We	442:443	We	442:443	We used an N-glycosylation mutagenesis approach to examine the orientation of the N-terminus and the endogenous glycosylation site of each C-terminal fragment by cell-free translation.
10585855	0	49	with	studies	9:15	arg1	fragments					35:43	biosynthetic fragments	22:43	biosynthetic fragments	22:43	Topology studies with biosynthetic fragments identify interacting transmembrane regions of the human red-cell anion exchanger (band 3; AE1).
10585855	10	50	theme	general	1504:1510	arg1	method					1512:1517	a general method	1502:1517	a general method for dissecting the interactions between membrane-spanning regions of polytopic membrane proteins	1502:1614	This approach might provide a general method for dissecting the interactions between membrane-spanning regions of polytopic membrane proteins.
10585855	3	51	theme	mutagenesis	469:479	arg1	approach					481:488	an N-glycosylation mutagenesis approach	450:488	an N-glycosylation mutagenesis approach	450:488	We used an N-glycosylation mutagenesis approach to examine the orientation of the N-terminus and the endogenous glycosylation site of each C-terminal fragment by cell-free translation.
10585855	3	52	theme	fragment	592:599	arg1	site					568:571	the endogenous glycosylation site	539:571	the endogenous glycosylation site of each C-terminal fragment	539:599	We used an N-glycosylation mutagenesis approach to examine the orientation of the N-terminus and the endogenous glycosylation site of each C-terminal fragment by cell-free translation.
10585855	3	52	theme	fragment	592:599	arg1	N-terminus					524:533	N-terminus	524:533	N-terminus	524:533	We used an N-glycosylation mutagenesis approach to examine the orientation of the N-terminus and the endogenous glycosylation site of each C-terminal fragment by cell-free translation.
10585855	3	52	theme	fragment	592:599	arg1	fragment					592:599	each C-terminal fragment	576:599	each C-terminal fragment	576:599	We used an N-glycosylation mutagenesis approach to examine the orientation of the N-terminus and the endogenous glycosylation site of each C-terminal fragment by cell-free translation.
10585855	6	53	contain	containing	923:932	arg2	span					934:937	span 4	934:939	span 4	934:939	The correct integration of spans 2-3 required the presence of the region containing span 4 and that the luminal exposure of the C-terminus of span 7 is increased in the presence of the region including span 6 or span 8.
10585855	6	53	contain	containing	923:932	arg1	region					916:921	the region	912:921	the region containing span 4	912:939	The correct integration of spans 2-3 required the presence of the region containing span 4 and that the luminal exposure of the C-terminus of span 7 is increased in the presence of the region including span 6 or span 8.
10585855	6	54	theme	C-terminus	978:987	arg1	exposure					962:969	the luminal exposure	950:969	the luminal exposure of the C-terminus of span 7	950:997	The correct integration of spans 2-3 required the presence of the region containing span 4 and that the luminal exposure of the C-terminus of span 7 is increased in the presence of the region including span 6 or span 8.
10585855	4	55	theme	expected	735:742	arg1	orientation					744:754	the expected orientation	731:754	the expected orientation	731:754	The fragments initiating in the loops preceding spans 2, 9 and 11 did not insert into the membrane with the expected orientation.
10585855	6	56	theme	region	1035:1040	arg1	presence					1019:1026	the presence	1015:1026	the presence of the region including span 6 or span 8	1015:1067	The correct integration of spans 2-3 required the presence of the region containing span 4 and that the luminal exposure of the C-terminus of span 7 is increased in the presence of the region including span 6 or span 8.
10585855	5	57	theme	membrane	818:825	arg1	integration					827:837	the membrane integration	814:837	the membrane integration of span 7	814:847	Furthermore, N-glycosylation of Asn-642 might facilitate the membrane integration of span 7.
10585855	7	58	theme	span	1094:1097	arg1	region					1101:1106	the span 8 region	1090:1106	the span 8 region	1090:1106	The results suggest the span 8 region is required for the correct folding of spans 9-10, at least in the presence of the span 11-12 region.
10585855	1	59	theme	multispanning	189:201	arg1	exchanger					160:168	The red-cell anion exchanger	141:168	The red-cell anion exchanger (band 3; AE1)	141:182	The red-cell anion exchanger (band 3; AE1) is a multispanning membrane protein that traverses the bilayer up to 14 times and is N-glycosylated at Asn-642.
10585855	1	59	theme	multispanning	189:201	arg1	protein					212:218	a multispanning membrane protein	187:218	a multispanning membrane protein that traverses the bilayer up to 14 times and is N-glycosylated at Asn-642	187:293	The red-cell anion exchanger (band 3; AE1) is a multispanning membrane protein that traverses the bilayer up to 14 times and is N-glycosylated at Asn-642.
10585855	1	59	theme	multispanning	189:201	arg1	N-glycosylated					269:282	N-glycosylated	269:282	N-glycosylated	269:282	The red-cell anion exchanger (band 3; AE1) is a multispanning membrane protein that traverses the bilayer up to 14 times and is N-glycosylated at Asn-642.
10585855	3	60	theme	C-terminal	581:590	arg1	fragment					592:599	each C-terminal fragment	576:599	each C-terminal fragment	576:599	We used an N-glycosylation mutagenesis approach to examine the orientation of the N-terminus and the endogenous glycosylation site of each C-terminal fragment by cell-free translation.
10585855	1	61	gly	N-glycosylated	269:282	arg1	N-glycosylated					269:282	N-glycosylated	269:282	N-glycosylated	269:282	The red-cell anion exchanger (band 3; AE1) is a multispanning membrane protein that traverses the bilayer up to 14 times and is N-glycosylated at Asn-642.
10585855	1	61	gly	N-glycosylated	269:282	arg2	Asn-642					287:293	Asn-642	287:293	Asn-642	287:293	The red-cell anion exchanger (band 3; AE1) is a multispanning membrane protein that traverses the bilayer up to 14 times and is N-glycosylated at Asn-642.
10585855	1	61	gly	N-glycosylated	269:282	arg1	protein					212:218	a multispanning membrane protein	187:218	a multispanning membrane protein that traverses the bilayer up to 14 times and is N-glycosylated at Asn-642	187:293	The red-cell anion exchanger (band 3; AE1) is a multispanning membrane protein that traverses the bilayer up to 14 times and is N-glycosylated at Asn-642.
10585855	1	61	gly	N-glycosylated	269:282	arg1	exchanger					160:168	The red-cell anion exchanger	141:168	The red-cell anion exchanger (band 3; AE1)	141:182	The red-cell anion exchanger (band 3; AE1) is a multispanning membrane protein that traverses the bilayer up to 14 times and is N-glycosylated at Asn-642.
10585855	3	62	dep	N-terminus	524:533	arg1	the					520:522	the	520:522	the	520:522	We used an N-glycosylation mutagenesis approach to examine the orientation of the N-terminus and the endogenous glycosylation site of each C-terminal fragment by cell-free translation.
10585855	8	63	theme	transmembrane	1296:1308	arg1	regions					1285:1291	the regions	1281:1291	the regions of transmembrane spans 1 and 2, 2 and 4, 4 and 5, 7 and 8, 8 and 9-10, and 9-10 and 11-12	1281:1381	Our results suggest that there are intramolecular interactions between the regions of transmembrane spans 1 and 2, 2 and 4, 4 and 5, 7 and 8, 8 and 9-10, and 9-10 and 11-12.
10585855	1	64	theme	membrane	203:210	arg1	exchanger					160:168	The red-cell anion exchanger	141:168	The red-cell anion exchanger (band 3; AE1)	141:182	The red-cell anion exchanger (band 3; AE1) is a multispanning membrane protein that traverses the bilayer up to 14 times and is N-glycosylated at Asn-642.
10585855	1	64	theme	membrane	203:210	arg1	protein					212:218	a multispanning membrane protein	187:218	a multispanning membrane protein that traverses the bilayer up to 14 times and is N-glycosylated at Asn-642	187:293	The red-cell anion exchanger (band 3; AE1) is a multispanning membrane protein that traverses the bilayer up to 14 times and is N-glycosylated at Asn-642.
10585855	1	64	theme	membrane	203:210	arg1	N-glycosylated					269:282	N-glycosylated	269:282	N-glycosylated	269:282	The red-cell anion exchanger (band 3; AE1) is a multispanning membrane protein that traverses the bilayer up to 14 times and is N-glycosylated at Asn-642.
19139490	0	0	theme	glycoproteins	74:86	arg1	identification					39:52	precise and large scale identification	15:52	identification	39:52	A strategy for precise and large scale identification of core fucosylated glycoproteins.
19139490	8	1	theme	results	1137:1143	arg1	scale					1113:1117	The scale	1109:1117	The scale of identification results	1109:1143	The scale of identification results indicates great progress for finding biomarkers with a particular and attractive prospect, and the candidate spectra will be a useful resource for the improvement of database searching methods for glycopeptides.
19139490	6	2	with	subjects	940:947	arg1	carcinoma					982:990	hepatocellular carcinoma	967:990	hepatocellular carcinoma	967:990	The efficacy of this strategy was demonstrated by implementation for plasma from healthy subjects and subjects with hepatocellular carcinoma.
19139490	7	3	theme	mass	1065:1068	arg1	spectra					1070:1076	over 10,000 mass spectra	1053:1076	over 10,000 mass spectra of CF glycopeptide	1053:1095	Over 100 CF glycoproteins and CF sites were identified, and over 10,000 mass spectra of CF glycopeptide were found.
19139490	4	4	theme	neutral	579:585	arg1	3					605:605	3	605:605	3	605:605	Here we developed a robust strategy that integrates molecular weight cutoff, neutral loss-dependent MS(3), database-independent candidate spectrum filtering, and optimization to effectively identify CF glycoproteins.
19139490	4	4	theme	neutral	579:585	arg1	MS					602:603	neutral loss-dependent MS	579:603	neutral loss-dependent MS(3)	579:606	Here we developed a robust strategy that integrates molecular weight cutoff, neutral loss-dependent MS(3), database-independent candidate spectrum filtering, and optimization to effectively identify CF glycoproteins.
19139490	4	4	theme	neutral	579:585	arg1	cutoff					571:576	molecular weight cutoff	554:576	molecular weight cutoff	554:576	Here we developed a robust strategy that integrates molecular weight cutoff, neutral loss-dependent MS(3), database-independent candidate spectrum filtering, and optimization to effectively identify CF glycoproteins.
19139490	0	5	theme	fucosylated	62:72	arg1	glycoproteins					74:86	core fucosylated glycoproteins	57:86	core fucosylated glycoproteins	57:86	A strategy for precise and large scale identification of core fucosylated glycoproteins.
19139490	6	6	theme	healthy	932:938	arg1	subjects					940:947	healthy subjects	932:947	healthy subjects	932:947	The efficacy of this strategy was demonstrated by implementation for plasma from healthy subjects and subjects with hepatocellular carcinoma.
19139490	8	7	theme	candidate	1244:1252	arg1	resource					1279:1286	a useful resource	1270:1286	a useful resource for the improvement of database searching methods for glycopeptides	1270:1354	The scale of identification results indicates great progress for finding biomarkers with a particular and attractive prospect, and the candidate spectra will be a useful resource for the improvement of database searching methods for glycopeptides.
19139490	8	7	theme	candidate	1244:1252	arg1	spectra					1254:1260	the candidate spectra	1240:1260	the candidate spectra	1240:1260	The scale of identification results indicates great progress for finding biomarkers with a particular and attractive prospect, and the candidate spectra will be a useful resource for the improvement of database searching methods for glycopeptides.
19139490	2	8	theme	glycoproteins	338:350	arg1	profiling					288:296	Global profiling	281:296	Global profiling	281:296	Global profiling and quantitative characterization of CF glycoproteins may reveal potent biomarkers for clinical applications.
19139490	2	8	theme	glycoproteins	338:350	arg1	characterization					315:330	quantitative characterization	302:330	quantitative characterization	302:330	Global profiling and quantitative characterization of CF glycoproteins may reveal potent biomarkers for clinical applications.
19139490	5	9	theme	spectrum	737:744	arg1	treatment					746:754	spectrum treatment	737:754	spectrum treatment	737:754	The rationale for spectrum treatment was innovatively based on computation of the mass distribution in spectra of CF glycopeptides.
19139490	7	10	theme	CF	1002:1003	arg1	glycoproteins					1005:1017	Over 100 CF glycoproteins	993:1017	Over 100 CF glycoproteins	993:1017	Over 100 CF glycoproteins and CF sites were identified, and over 10,000 mass spectra of CF glycopeptide were found.
19139490	1	11	theme	many	249:252	arg1	cancers					272:278	cancers	272:278	cancers	272:278	Core fucosylation (CF) patterns of some glycoproteins are more sensitive and specific than evaluation of their total respective protein levels for diagnosis of many diseases, such as cancers.
19139490	1	11	theme	many	249:252	arg1	diseases					254:261	many diseases	249:261	many diseases	249:261	Core fucosylation (CF) patterns of some glycoproteins are more sensitive and specific than evaluation of their total respective protein levels for diagnosis of many diseases, such as cancers.
19139490	8	12	theme	identification	1122:1135	arg1	results					1137:1143	identification results	1122:1143	identification results	1122:1143	The scale of identification results indicates great progress for finding biomarkers with a particular and attractive prospect, and the candidate spectra will be a useful resource for the improvement of database searching methods for glycopeptides.
19139490	1	13	theme	diseases	254:261	arg1	diagnosis					236:244	diagnosis	236:244	diagnosis of many diseases, such as cancers	236:278	Core fucosylation (CF) patterns of some glycoproteins are more sensitive and specific than evaluation of their total respective protein levels for diagnosis of many diseases, such as cancers.
19139490	8	14	theme	particular	1200:1209	arg1	prospect					1226:1233	a particular and attractive prospect	1198:1233	a particular and attractive prospect	1198:1233	The scale of identification results indicates great progress for finding biomarkers with a particular and attractive prospect, and the candidate spectra will be a useful resource for the improvement of database searching methods for glycopeptides.
19139490	3	15	theme	large	489:493	arg1	scale					495:499	a large scale	487:499	a large scale	487:499	However, current techniques are unable to reveal CF glycoproteins precisely on a large scale.
19139490	4	16	theme	loss-dependent	587:600	arg1	3					605:605	3	605:605	3	605:605	Here we developed a robust strategy that integrates molecular weight cutoff, neutral loss-dependent MS(3), database-independent candidate spectrum filtering, and optimization to effectively identify CF glycoproteins.
19139490	4	16	theme	loss-dependent	587:600	arg1	MS					602:603	neutral loss-dependent MS	579:603	neutral loss-dependent MS(3)	579:606	Here we developed a robust strategy that integrates molecular weight cutoff, neutral loss-dependent MS(3), database-independent candidate spectrum filtering, and optimization to effectively identify CF glycoproteins.
19139490	4	16	theme	loss-dependent	587:600	arg1	cutoff					571:576	molecular weight cutoff	554:576	molecular weight cutoff	554:576	Here we developed a robust strategy that integrates molecular weight cutoff, neutral loss-dependent MS(3), database-independent candidate spectrum filtering, and optimization to effectively identify CF glycoproteins.
19139490	0	17	gly	fucosylated	62:72	arg1	glycoproteins					74:86	core fucosylated glycoproteins	57:86	core fucosylated glycoproteins	57:86	A strategy for precise and large scale identification of core fucosylated glycoproteins.
19139490	1	18	gly	fucosylation	94:105	arg1	glycoproteins					129:141	some glycoproteins	124:141	some glycoproteins	124:141	Core fucosylation (CF) patterns of some glycoproteins are more sensitive and specific than evaluation of their total respective protein levels for diagnosis of many diseases, such as cancers.
19139490	5	19	from	spectra	822:828	arg1	computation					782:792	computation	782:792	computation of the mass distribution in spectra of CF glycopeptides	782:848	The rationale for spectrum treatment was innovatively based on computation of the mass distribution in spectra of CF glycopeptides.
19139490	6	20	with	subjects	953:960	arg1	carcinoma					982:990	hepatocellular carcinoma	967:990	hepatocellular carcinoma	967:990	The efficacy of this strategy was demonstrated by implementation for plasma from healthy subjects and subjects with hepatocellular carcinoma.
19139490	8	21	theme	database	1311:1318	arg1	improvement					1296:1306	the improvement	1292:1306	the improvement of database searching methods for glycopeptides	1292:1354	The scale of identification results indicates great progress for finding biomarkers with a particular and attractive prospect, and the candidate spectra will be a useful resource for the improvement of database searching methods for glycopeptides.
19139490	0	22	gly	glycoproteins	74:86	arg1	glycoproteins					74:86	core fucosylated glycoproteins	57:86	core fucosylated glycoproteins	57:86	A strategy for precise and large scale identification of core fucosylated glycoproteins.
19139490	2	23	theme	clinical	385:392	arg1	applications					394:405	clinical applications	385:405	clinical applications	385:405	Global profiling and quantitative characterization of CF glycoproteins may reveal potent biomarkers for clinical applications.
19139490	8	24	theme	attractive	1215:1224	arg1	prospect					1226:1233	a particular and attractive prospect	1198:1233	a particular and attractive prospect	1198:1233	The scale of identification results indicates great progress for finding biomarkers with a particular and attractive prospect, and the candidate spectra will be a useful resource for the improvement of database searching methods for glycopeptides.
19139490	6	25	from	subjects	940:947	arg1	plasma					920:925	plasma	920:925	plasma from healthy subjects and subjects with hepatocellular carcinoma	920:990	The efficacy of this strategy was demonstrated by implementation for plasma from healthy subjects and subjects with hepatocellular carcinoma.
19139490	8	26	gly	glycopeptides	1342:1354	arg2	glycopeptides					1342:1354	glycopeptides	1342:1354	glycopeptides	1342:1354	The scale of identification results indicates great progress for finding biomarkers with a particular and attractive prospect, and the candidate spectra will be a useful resource for the improvement of database searching methods for glycopeptides.
19139490	8	27	theme	useful	1272:1277	arg1	resource					1279:1286	a useful resource	1270:1286	a useful resource for the improvement of database searching methods for glycopeptides	1270:1354	The scale of identification results indicates great progress for finding biomarkers with a particular and attractive prospect, and the candidate spectra will be a useful resource for the improvement of database searching methods for glycopeptides.
19139490	8	27	theme	useful	1272:1277	arg1	spectra					1254:1260	the candidate spectra	1240:1260	the candidate spectra	1240:1260	The scale of identification results indicates great progress for finding biomarkers with a particular and attractive prospect, and the candidate spectra will be a useful resource for the improvement of database searching methods for glycopeptides.
19139490	4	28	theme	molecular	554:562	arg1	MS					602:603	neutral loss-dependent MS	579:603	neutral loss-dependent MS(3)	579:606	Here we developed a robust strategy that integrates molecular weight cutoff, neutral loss-dependent MS(3), database-independent candidate spectrum filtering, and optimization to effectively identify CF glycoproteins.
19139490	4	28	theme	molecular	554:562	arg1	cutoff					571:576	molecular weight cutoff	554:576	molecular weight cutoff	554:576	Here we developed a robust strategy that integrates molecular weight cutoff, neutral loss-dependent MS(3), database-independent candidate spectrum filtering, and optimization to effectively identify CF glycoproteins.
19139490	7	29	theme	CF	1081:1082	arg1	glycopeptide					1084:1095	CF glycopeptide	1081:1095	CF glycopeptide	1081:1095	Over 100 CF glycoproteins and CF sites were identified, and over 10,000 mass spectra of CF glycopeptide were found.
19139490	1	30	theme	Core	89:92	arg1	CF					108:109	CF	108:109	CF	108:109	Core fucosylation (CF) patterns of some glycoproteins are more sensitive and specific than evaluation of their total respective protein levels for diagnosis of many diseases, such as cancers.
19139490	1	30	theme	Core	89:92	arg1	fucosylation					94:105	Core fucosylation	89:105	Core fucosylation (CF) patterns of some glycoproteins	89:141	Core fucosylation (CF) patterns of some glycoproteins are more sensitive and specific than evaluation of their total respective protein levels for diagnosis of many diseases, such as cancers.
19139490	0	31	theme	precise	15:21	arg1	identification					39:52	precise and large scale identification	15:52	identification	39:52	A strategy for precise and large scale identification of core fucosylated glycoproteins.
19139490	7	32	theme	glycopeptide	1084:1095	arg1	spectra					1070:1076	over 10,000 mass spectra	1053:1076	over 10,000 mass spectra of CF glycopeptide	1053:1095	Over 100 CF glycoproteins and CF sites were identified, and over 10,000 mass spectra of CF glycopeptide were found.
19139490	8	33	with	biomarkers	1182:1191	arg1	prospect					1226:1233	a particular and attractive prospect	1198:1233	a particular and attractive prospect	1198:1233	The scale of identification results indicates great progress for finding biomarkers with a particular and attractive prospect, and the candidate spectra will be a useful resource for the improvement of database searching methods for glycopeptides.
19139490	1	34	theme	fucosylation	94:105	arg1	patterns					112:119	Core fucosylation (CF) patterns	89:119	Core fucosylation (CF) patterns of some glycoproteins	89:141	Core fucosylation (CF) patterns of some glycoproteins are more sensitive and specific than evaluation of their total respective protein levels for diagnosis of many diseases, such as cancers.
19139490	4	35	theme	candidate	630:638	arg1	filtering					649:657	database-independent candidate spectrum filtering	609:657	database-independent candidate spectrum filtering	609:657	Here we developed a robust strategy that integrates molecular weight cutoff, neutral loss-dependent MS(3), database-independent candidate spectrum filtering, and optimization to effectively identify CF glycoproteins.
19139490	5	36	theme	glycopeptides	836:848	arg1	spectra					822:828	spectra	822:828	spectra of CF glycopeptides	822:848	The rationale for spectrum treatment was innovatively based on computation of the mass distribution in spectra of CF glycopeptides.
19139490	7	37	gly	glycopeptide	1084:1095	arg2	glycopeptide					1084:1095	CF glycopeptide	1081:1095	CF glycopeptide	1081:1095	Over 100 CF glycoproteins and CF sites were identified, and over 10,000 mass spectra of CF glycopeptide were found.
19139490	4	38	theme	CF	701:702	arg1	glycoproteins					704:716	CF glycoproteins	701:716	CF glycoproteins	701:716	Here we developed a robust strategy that integrates molecular weight cutoff, neutral loss-dependent MS(3), database-independent candidate spectrum filtering, and optimization to effectively identify CF glycoproteins.
19139490	4	39	theme	database-independent	609:628	arg1	filtering					649:657	database-independent candidate spectrum filtering	609:657	database-independent candidate spectrum filtering	609:657	Here we developed a robust strategy that integrates molecular weight cutoff, neutral loss-dependent MS(3), database-independent candidate spectrum filtering, and optimization to effectively identify CF glycoproteins.
19139490	0	40	theme	large	27:31	arg1	identification					39:52	precise and large scale identification	15:52	identification	39:52	A strategy for precise and large scale identification of core fucosylated glycoproteins.
19139490	4	41	theme	weight	564:569	arg1	MS					602:603	neutral loss-dependent MS	579:603	neutral loss-dependent MS(3)	579:606	Here we developed a robust strategy that integrates molecular weight cutoff, neutral loss-dependent MS(3), database-independent candidate spectrum filtering, and optimization to effectively identify CF glycoproteins.
19139490	4	41	theme	weight	564:569	arg1	cutoff					571:576	molecular weight cutoff	554:576	molecular weight cutoff	554:576	Here we developed a robust strategy that integrates molecular weight cutoff, neutral loss-dependent MS(3), database-independent candidate spectrum filtering, and optimization to effectively identify CF glycoproteins.
19139490	2	42	gly	glycoproteins	338:350	arg1	glycoproteins					338:350	CF glycoproteins	335:350	CF glycoproteins	335:350	Global profiling and quantitative characterization of CF glycoproteins may reveal potent biomarkers for clinical applications.
19139490	4	43	theme	spectrum	640:647	arg1	filtering					649:657	database-independent candidate spectrum filtering	609:657	database-independent candidate spectrum filtering	609:657	Here we developed a robust strategy that integrates molecular weight cutoff, neutral loss-dependent MS(3), database-independent candidate spectrum filtering, and optimization to effectively identify CF glycoproteins.
19139490	3	44	theme	current	417:423	arg1	techniques					425:434	current techniques	417:434	current techniques	417:434	However, current techniques are unable to reveal CF glycoproteins precisely on a large scale.
19139490	4	45	theme	robust	522:527	arg1	strategy					529:536	a robust strategy	520:536	a robust strategy that integrates molecular weight cutoff, neutral loss-dependent MS(3), database-independent candidate spectrum filtering, and optimization to effectively identify CF glycoproteins	520:716	Here we developed a robust strategy that integrates molecular weight cutoff, neutral loss-dependent MS(3), database-independent candidate spectrum filtering, and optimization to effectively identify CF glycoproteins.
19139490	5	46	theme	mass	801:804	arg1	distribution					806:817	the mass distribution	797:817	the mass distribution in spectra of CF glycopeptides	797:848	The rationale for spectrum treatment was innovatively based on computation of the mass distribution in spectra of CF glycopeptides.
19139490	6	47	theme	strategy	872:879	arg1	efficacy					855:862	The efficacy	851:862	The efficacy of this strategy	851:879	The efficacy of this strategy was demonstrated by implementation for plasma from healthy subjects and subjects with hepatocellular carcinoma.
19139490	3	48	gly	glycoproteins	460:472	arg1	glycoproteins					460:472	CF glycoproteins	457:472	CF glycoproteins	457:472	However, current techniques are unable to reveal CF glycoproteins precisely on a large scale.
19139490	1	49	theme	total	200:204	arg1	levels					225:230	their total respective protein levels	194:230	their total respective protein levels	194:230	Core fucosylation (CF) patterns of some glycoproteins are more sensitive and specific than evaluation of their total respective protein levels for diagnosis of many diseases, such as cancers.
19139490	5	50	theme	distribution	806:817	arg1	computation					782:792	computation	782:792	computation of the mass distribution in spectra of CF glycopeptides	782:848	The rationale for spectrum treatment was innovatively based on computation of the mass distribution in spectra of CF glycopeptides.
19139490	6	51	theme	hepatocellular	967:980	arg1	carcinoma					982:990	hepatocellular carcinoma	967:990	hepatocellular carcinoma	967:990	The efficacy of this strategy was demonstrated by implementation for plasma from healthy subjects and subjects with hepatocellular carcinoma.
19139490	1	52	gly	glycoproteins	129:141	arg1	glycoproteins					129:141	some glycoproteins	124:141	some glycoproteins	124:141	Core fucosylation (CF) patterns of some glycoproteins are more sensitive and specific than evaluation of their total respective protein levels for diagnosis of many diseases, such as cancers.
19139490	5	53	gly	glycopeptides	836:848	arg2	glycopeptides					836:848	CF glycopeptides	833:848	CF glycopeptides	833:848	The rationale for spectrum treatment was innovatively based on computation of the mass distribution in spectra of CF glycopeptides.
19139490	2	54	theme	CF	335:336	arg1	glycoproteins					338:350	CF glycoproteins	335:350	CF glycoproteins	335:350	Global profiling and quantitative characterization of CF glycoproteins may reveal potent biomarkers for clinical applications.
19139490	0	55	theme	scale	33:37	arg1	identification					39:52	precise and large scale identification	15:52	identification	39:52	A strategy for precise and large scale identification of core fucosylated glycoproteins.
19139490	6	56	from	subjects	953:960	arg1	plasma					920:925	plasma	920:925	plasma from healthy subjects and subjects with hepatocellular carcinoma	920:990	The efficacy of this strategy was demonstrated by implementation for plasma from healthy subjects and subjects with hepatocellular carcinoma.
19139490	5	57	from	computation	782:792	arg1	spectra					822:828	spectra	822:828	spectra of CF glycopeptides	822:848	The rationale for spectrum treatment was innovatively based on computation of the mass distribution in spectra of CF glycopeptides.
19139490	5	58	theme	CF	833:834	arg1	glycopeptides					836:848	CF glycopeptides	833:848	CF glycopeptides	833:848	The rationale for spectrum treatment was innovatively based on computation of the mass distribution in spectra of CF glycopeptides.
19139490	2	59	theme	Global	281:286	arg1	profiling					288:296	Global profiling	281:296	Global profiling	281:296	Global profiling and quantitative characterization of CF glycoproteins may reveal potent biomarkers for clinical applications.
19139490	1	60	theme	respective	206:215	arg1	levels					225:230	their total respective protein levels	194:230	their total respective protein levels	194:230	Core fucosylation (CF) patterns of some glycoproteins are more sensitive and specific than evaluation of their total respective protein levels for diagnosis of many diseases, such as cancers.
19139490	4	61	gly	glycoproteins	704:716	arg1	glycoproteins					704:716	CF glycoproteins	701:716	CF glycoproteins	701:716	Here we developed a robust strategy that integrates molecular weight cutoff, neutral loss-dependent MS(3), database-independent candidate spectrum filtering, and optimization to effectively identify CF glycoproteins.
19139490	7	62	theme	CF	1023:1024	arg1	sites					1026:1030	CF sites	1023:1030	CF sites	1023:1030	Over 100 CF glycoproteins and CF sites were identified, and over 10,000 mass spectra of CF glycopeptide were found.
19139490	2	63	theme	quantitative	302:313	arg1	characterization					315:330	quantitative characterization	302:330	quantitative characterization	302:330	Global profiling and quantitative characterization of CF glycoproteins may reveal potent biomarkers for clinical applications.
19139490	1	64	theme	protein	217:223	arg1	levels					225:230	their total respective protein levels	194:230	their total respective protein levels	194:230	Core fucosylation (CF) patterns of some glycoproteins are more sensitive and specific than evaluation of their total respective protein levels for diagnosis of many diseases, such as cancers.
19139490	0	65	theme	core	57:60	arg1	glycoproteins					74:86	core fucosylated glycoproteins	57:86	core fucosylated glycoproteins	57:86	A strategy for precise and large scale identification of core fucosylated glycoproteins.
19139490	3	66	theme	CF	457:458	arg1	glycoproteins					460:472	CF glycoproteins	457:472	CF glycoproteins	457:472	However, current techniques are unable to reveal CF glycoproteins precisely on a large scale.
19139490	2	67	theme	potent	363:368	arg1	biomarkers					370:379	potent biomarkers	363:379	potent biomarkers for clinical applications	363:405	Global profiling and quantitative characterization of CF glycoproteins may reveal potent biomarkers for clinical applications.
19139490	1	68	theme	levels	225:230	arg1	evaluation					180:189	evaluation	180:189	evaluation of their total respective protein levels for diagnosis of many diseases, such as cancers	180:278	Core fucosylation (CF) patterns of some glycoproteins are more sensitive and specific than evaluation of their total respective protein levels for diagnosis of many diseases, such as cancers.
19139490	8	69	theme	great	1155:1159	arg1	progress					1161:1168	great progress	1155:1168	great progress for finding biomarkers with a particular and attractive prospect	1155:1233	The scale of identification results indicates great progress for finding biomarkers with a particular and attractive prospect, and the candidate spectra will be a useful resource for the improvement of database searching methods for glycopeptides.
19139490	5	70	from	distribution	806:817	arg1	spectra					822:828	spectra	822:828	spectra of CF glycopeptides	822:848	The rationale for spectrum treatment was innovatively based on computation of the mass distribution in spectra of CF glycopeptides.
19139490	1	71	theme	glycoproteins	129:141	arg1	patterns					112:119	Core fucosylation (CF) patterns	89:119	Core fucosylation (CF) patterns of some glycoproteins	89:141	Core fucosylation (CF) patterns of some glycoproteins are more sensitive and specific than evaluation of their total respective protein levels for diagnosis of many diseases, such as cancers.
19139490	7	72	gly	glycoproteins	1005:1017	arg1	glycoproteins					1005:1017	Over 100 CF glycoproteins	993:1017	Over 100 CF glycoproteins	993:1017	Over 100 CF glycoproteins and CF sites were identified, and over 10,000 mass spectra of CF glycopeptide were found.
9705299	6	0	dep	in	950:951	arg1	vitro					953:957	vitro	953:957	vitro	953:957	Western blot and in vitro translation studies showed that G6Pase is glycosylated only at Asn96, further validating the nine-transmembrane topology model.
9705299	1	1	theme	reticulum	172:180	arg1	glycoprotein					196:207	an endoplasmic reticulum transmembrane glycoprotein	157:207	an endoplasmic reticulum transmembrane glycoprotein	157:207	Deficiency of glucose-6-phosphatase (G6Pase), an endoplasmic reticulum transmembrane glycoprotein, causes glycogen storage disease type 1a.
9705299	1	1	theme	reticulum	172:180	arg1	glucose-6-phosphatase					125:145	glucose-6-phosphatase	125:145	glucose-6-phosphatase (G6Pase)	125:154	Deficiency of glucose-6-phosphatase (G6Pase), an endoplasmic reticulum transmembrane glycoprotein, causes glycogen storage disease type 1a.
9705299	0	2	theme	human	82:86	arg1	glucose-6-phosphatase					88:108	human glucose-6-phosphatase	82:108	human glucose-6-phosphatase	82:108	Asparagine-linked oligosaccharides are localized to a luminal hydrophilic loop in human glucose-6-phosphatase.
9705299	1	3	gly	glycoprotein	196:207	arg1	glycoprotein					196:207	an endoplasmic reticulum transmembrane glycoprotein	157:207	an endoplasmic reticulum transmembrane glycoprotein	157:207	Deficiency of glucose-6-phosphatase (G6Pase), an endoplasmic reticulum transmembrane glycoprotein, causes glycogen storage disease type 1a.
9705299	1	3	gly	glycoprotein	196:207	arg1	glucose-6-phosphatase					125:145	glucose-6-phosphatase	125:145	glucose-6-phosphatase (G6Pase)	125:154	Deficiency of glucose-6-phosphatase (G6Pase), an endoplasmic reticulum transmembrane glycoprotein, causes glycogen storage disease type 1a.
9705299	1	4	theme	transmembrane	182:194	arg1	glycoprotein					196:207	an endoplasmic reticulum transmembrane glycoprotein	157:207	an endoplasmic reticulum transmembrane glycoprotein	157:207	Deficiency of glucose-6-phosphatase (G6Pase), an endoplasmic reticulum transmembrane glycoprotein, causes glycogen storage disease type 1a.
9705299	1	4	theme	transmembrane	182:194	arg1	glucose-6-phosphatase					125:145	glucose-6-phosphatase	125:145	glucose-6-phosphatase (G6Pase)	125:154	Deficiency of glucose-6-phosphatase (G6Pase), an endoplasmic reticulum transmembrane glycoprotein, causes glycogen storage disease type 1a.
9705299	6	5	theme	translation	959:969	arg1	studies					971:977	Western blot and in vitro translation studies	933:977	Western blot and in vitro translation studies	933:977	Western blot and in vitro translation studies showed that G6Pase is glycosylated only at Asn96, further validating the nine-transmembrane topology model.
9705299	6	6	theme	topology	1071:1078	arg1	model					1080:1084	the nine-transmembrane topology model	1048:1084	the nine-transmembrane topology model	1048:1084	Western blot and in vitro translation studies showed that G6Pase is glycosylated only at Asn96, further validating the nine-transmembrane topology model.
9705299	4	7	dep	acceptor	654:661	arg1	whereas					685:691	whereas	685:691	whereas	685:691	According to this model, Asn96, located in a 37-residue luminal loop, is a potential acceptor for oligosaccharides, whereas Asn203 and Asn276, located in a 12-residue cytoplasmic loop and helix 7, respectively, would not be utilized for this purpose.
9705299	4	8	from	helix	757:761	arg1	located					712:718	located	712:718	located	712:718	According to this model, Asn96, located in a 37-residue luminal loop, is a potential acceptor for oligosaccharides, whereas Asn203 and Asn276, located in a 12-residue cytoplasmic loop and helix 7, respectively, would not be utilized for this purpose.
9705299	3	9	theme	mammalian	550:558	arg1	G6Pases					560:566	mammalian G6Pases	550:566	mammalian G6Pases	550:566	Sequence analysis predicts the presence of three potential asparagine (N)-linked glycosylation sites, N96TS, N203AS, and N276SS, conserved among mammalian G6Pases.
9705299	4	10	theme	12-residue	725:734	arg1	loop					748:751	a 12-residue cytoplasmic loop	723:751	a 12-residue cytoplasmic loop	723:751	According to this model, Asn96, located in a 37-residue luminal loop, is a potential acceptor for oligosaccharides, whereas Asn203 and Asn276, located in a 12-residue cytoplasmic loop and helix 7, respectively, would not be utilized for this purpose.
9705299	9	11	theme	G6Pase	1554:1559	arg1	stability					1561:1569	G6Pase stability	1554:1569	G6Pase stability	1554:1569	We present additional evidence suggesting that the integrity of transmembrane helices is essential for G6Pase stability and catalytic activity.
9705299	5	12	theme	potential	893:901	arg1	sites					926:930	all three potential N-linked glycosylation sites	883:930	all three potential N-linked glycosylation sites	883:930	We therefore characterized mutant G6Pases lacking one, two, or all three potential N-linked glycosylation sites.
9705299	4	13	theme	luminal	625:631	arg1	loop					633:636	a 37-residue luminal loop	612:636	a 37-residue luminal loop	612:636	According to this model, Asn96, located in a 37-residue luminal loop, is a potential acceptor for oligosaccharides, whereas Asn203 and Asn276, located in a 12-residue cytoplasmic loop and helix 7, respectively, would not be utilized for this purpose.
9705299	7	14	theme	G6Pase	1184:1189	arg1	synthesis					1191:1199	G6Pase synthesis	1184:1199	G6Pase synthesis	1184:1199	Substituting Asn96 with an Ala (N96A) moderately reduced enzymatic activity and had no effect on G6Pase synthesis or degradation, suggesting that oligosaccharide chains do not play a major role in protecting the enzyme from proteolytic degradation.
9705299	2	15	theme	odd	304:306	arg1	number					308:313	an odd number	301:313	an odd number of transmembrane segments	301:339	We have recently shown that human G6Pase contains an odd number of transmembrane segments, supporting a nine-transmembrane helical model for this enzyme.
9705299	4	16	used	utilized	793:800	arg2	Asn276					704:709	Asn276	704:709	Asn276	704:709	According to this model, Asn96, located in a 37-residue luminal loop, is a potential acceptor for oligosaccharides, whereas Asn203 and Asn276, located in a 12-residue cytoplasmic loop and helix 7, respectively, would not be utilized for this purpose.
9705299	4	16	used	utilized	793:800	arg2	Asn203					693:698	Asn203	693:698	Asn203	693:698	According to this model, Asn96, located in a 37-residue luminal loop, is a potential acceptor for oligosaccharides, whereas Asn203 and Asn276, located in a 12-residue cytoplasmic loop and helix 7, respectively, would not be utilized for this purpose.
9705299	6	17	theme	in	950:951	arg1	translation					959:969	in vitro translation	950:969	in vitro translation	950:969	Western blot and in vitro translation studies showed that G6Pase is glycosylated only at Asn96, further validating the nine-transmembrane topology model.
9705299	0	18	link	Asparagine-linked	0:16	arg1	oligosaccharides					18:33	Asparagine-linked oligosaccharides	0:33	Asparagine-linked oligosaccharides	0:33	Asparagine-linked oligosaccharides are localized to a luminal hydrophilic loop in human glucose-6-phosphatase.
9705299	9	19	theme	transmembrane	1515:1527	arg1	helices					1529:1535	transmembrane helices	1515:1535	transmembrane helices	1515:1535	We present additional evidence suggesting that the integrity of transmembrane helices is essential for G6Pase stability and catalytic activity.
9705299	5	20	theme	mutant	847:852	arg1	G6Pases					854:860	mutant G6Pases	847:860	mutant G6Pases lacking one, two, or all three potential N-linked glycosylation sites	847:930	We therefore characterized mutant G6Pases lacking one, two, or all three potential N-linked glycosylation sites.
9705299	4	21	theme	potential	644:652	arg1	Asn96					594:598	Asn96	594:598	Asn96	594:598	According to this model, Asn96, located in a 37-residue luminal loop, is a potential acceptor for oligosaccharides, whereas Asn203 and Asn276, located in a 12-residue cytoplasmic loop and helix 7, respectively, would not be utilized for this purpose.
9705299	4	21	theme	potential	644:652	arg1	acceptor					654:661	a potential acceptor	642:661	a potential acceptor for oligosaccharides	642:682	According to this model, Asn96, located in a 37-residue luminal loop, is a potential acceptor for oligosaccharides, whereas Asn203 and Asn276, located in a 12-residue cytoplasmic loop and helix 7, respectively, would not be utilized for this purpose.
9705299	5	22	gly	glycosylation	912:924	arg2	three					887:891	three	887:891	three	887:891	We therefore characterized mutant G6Pases lacking one, two, or all three potential N-linked glycosylation sites.
9705299	5	22	gly	glycosylation	912:924	arg2	sites					926:930	all three potential N-linked glycosylation sites	883:930	all three potential N-linked glycosylation sites	883:930	We therefore characterized mutant G6Pases lacking one, two, or all three potential N-linked glycosylation sites.
9705299	9	23	theme	helices	1529:1535	arg1	essential					1540:1548	essential	1540:1548	essential	1540:1548	We present additional evidence suggesting that the integrity of transmembrane helices is essential for G6Pase stability and catalytic activity.
9705299	9	23	theme	helices	1529:1535	arg1	integrity					1502:1510	the integrity	1498:1510	the integrity of transmembrane helices	1498:1535	We present additional evidence suggesting that the integrity of transmembrane helices is essential for G6Pase stability and catalytic activity.
9705299	6	24	theme	nine-transmembrane	1052:1069	arg1	model					1080:1084	the nine-transmembrane topology model	1048:1084	the nine-transmembrane topology model	1048:1084	Western blot and in vitro translation studies showed that G6Pase is glycosylated only at Asn96, further validating the nine-transmembrane topology model.
9705299	7	25	theme	enzymatic	1144:1152	arg1	activity					1154:1161	enzymatic activity	1144:1161	enzymatic activity	1144:1161	Substituting Asn96 with an Ala (N96A) moderately reduced enzymatic activity and had no effect on G6Pase synthesis or degradation, suggesting that oligosaccharide chains do not play a major role in protecting the enzyme from proteolytic degradation.
9705299	4	26	from	located	601:607	arg1	loop					633:636	a 37-residue luminal loop	612:636	a 37-residue luminal loop	612:636	According to this model, Asn96, located in a 37-residue luminal loop, is a potential acceptor for oligosaccharides, whereas Asn203 and Asn276, located in a 12-residue cytoplasmic loop and helix 7, respectively, would not be utilized for this purpose.
9705299	3	27	link	-linked	478:484	arg1	N203AS					514:519	N203AS	514:519	N203AS	514:519	Sequence analysis predicts the presence of three potential asparagine (N)-linked glycosylation sites, N96TS, N203AS, and N276SS, conserved among mammalian G6Pases.
9705299	3	27	link	-linked	478:484	arg1	N276SS					526:531	N276SS	526:531	N276SS	526:531	Sequence analysis predicts the presence of three potential asparagine (N)-linked glycosylation sites, N96TS, N203AS, and N276SS, conserved among mammalian G6Pases.
9705299	3	27	link	-linked	478:484	arg1	N96TS					507:511	N96TS	507:511	N96TS	507:511	Sequence analysis predicts the presence of three potential asparagine (N)-linked glycosylation sites, N96TS, N203AS, and N276SS, conserved among mammalian G6Pases.
9705299	3	27	link	-linked	478:484	arg1	sites					500:504	three potential asparagine (N)-linked glycosylation sites	448:504	three potential asparagine (N)-linked glycosylation sites	448:504	Sequence analysis predicts the presence of three potential asparagine (N)-linked glycosylation sites, N96TS, N203AS, and N276SS, conserved among mammalian G6Pases.
9705299	5	28	theme	glycosylation	912:924	arg1	sites					926:930	all three potential N-linked glycosylation sites	883:930	all three potential N-linked glycosylation sites	883:930	We therefore characterized mutant G6Pases lacking one, two, or all three potential N-linked glycosylation sites.
9705299	3	29	theme	potential	454:462	arg1	N203AS					514:519	N203AS	514:519	N203AS	514:519	Sequence analysis predicts the presence of three potential asparagine (N)-linked glycosylation sites, N96TS, N203AS, and N276SS, conserved among mammalian G6Pases.
9705299	3	29	theme	potential	454:462	arg1	N276SS					526:531	N276SS	526:531	N276SS	526:531	Sequence analysis predicts the presence of three potential asparagine (N)-linked glycosylation sites, N96TS, N203AS, and N276SS, conserved among mammalian G6Pases.
9705299	3	29	theme	potential	454:462	arg1	N96TS					507:511	N96TS	507:511	N96TS	507:511	Sequence analysis predicts the presence of three potential asparagine (N)-linked glycosylation sites, N96TS, N203AS, and N276SS, conserved among mammalian G6Pases.
9705299	3	29	theme	potential	454:462	arg1	sites					500:504	three potential asparagine (N)-linked glycosylation sites	448:504	three potential asparagine (N)-linked glycosylation sites	448:504	Sequence analysis predicts the presence of three potential asparagine (N)-linked glycosylation sites, N96TS, N203AS, and N276SS, conserved among mammalian G6Pases.
9705299	0	30	theme	Asparagine-linked	0:16	arg1	oligosaccharides					18:33	Asparagine-linked oligosaccharides	0:33	Asparagine-linked oligosaccharides	0:33	Asparagine-linked oligosaccharides are localized to a luminal hydrophilic loop in human glucose-6-phosphatase.
9705299	2	31	contain	contains	292:299	arg2	number					308:313	an odd number	301:313	an odd number of transmembrane segments	301:339	We have recently shown that human G6Pase contains an odd number of transmembrane segments, supporting a nine-transmembrane helical model for this enzyme.
9705299	2	31	contain	contains	292:299	arg1	G6Pase					285:290	human G6Pase	279:290	human G6Pase	279:290	We have recently shown that human G6Pase contains an odd number of transmembrane segments, supporting a nine-transmembrane helical model for this enzyme.
9705299	2	32	theme	segments	332:339	arg1	number					308:313	an odd number	301:313	an odd number of transmembrane segments	301:339	We have recently shown that human G6Pase contains an odd number of transmembrane segments, supporting a nine-transmembrane helical model for this enzyme.
9705299	1	33	theme	glycogen	217:224	arg1	1a					247:248	glycogen storage disease type 1a	217:248	glycogen storage disease type 1a	217:248	Deficiency of glucose-6-phosphatase (G6Pase), an endoplasmic reticulum transmembrane glycoprotein, causes glycogen storage disease type 1a.
9705299	3	34	theme	sites	500:504	arg1	presence					436:443	the presence	432:443	the presence of three potential asparagine (N)-linked glycosylation sites, N96TS, N203AS, and N276SS, conserved among mammalian G6Pases	432:566	Sequence analysis predicts the presence of three potential asparagine (N)-linked glycosylation sites, N96TS, N203AS, and N276SS, conserved among mammalian G6Pases.
9705299	6	35	theme	blot	941:944	arg1	studies					971:977	Western blot and in vitro translation studies	933:977	Western blot and in vitro translation studies	933:977	Western blot and in vitro translation studies showed that G6Pase is glycosylated only at Asn96, further validating the nine-transmembrane topology model.
9705299	4	36	from	loop	748:751	arg1	located					712:718	located	712:718	located	712:718	According to this model, Asn96, located in a 37-residue luminal loop, is a potential acceptor for oligosaccharides, whereas Asn203 and Asn276, located in a 12-residue cytoplasmic loop and helix 7, respectively, would not be utilized for this purpose.
9705299	2	37	theme	transmembrane	318:330	arg1	segments					332:339	transmembrane segments	318:339	transmembrane segments	318:339	We have recently shown that human G6Pase contains an odd number of transmembrane segments, supporting a nine-transmembrane helical model for this enzyme.
9705299	1	38	theme	storage	226:232	arg1	1a					247:248	glycogen storage disease type 1a	217:248	glycogen storage disease type 1a	217:248	Deficiency of glucose-6-phosphatase (G6Pase), an endoplasmic reticulum transmembrane glycoprotein, causes glycogen storage disease type 1a.
9705299	3	39	theme	Sequence	405:412	arg1	analysis					414:421	Sequence analysis	405:421	Sequence analysis	405:421	Sequence analysis predicts the presence of three potential asparagine (N)-linked glycosylation sites, N96TS, N203AS, and N276SS, conserved among mammalian G6Pases.
9705299	6	40	theme	Western	933:939	arg1	blot					941:944	Western blot	933:944	Western blot	933:944	Western blot and in vitro translation studies showed that G6Pase is glycosylated only at Asn96, further validating the nine-transmembrane topology model.
9705299	5	41	theme	N-linked	903:910	arg1	sites					926:930	all three potential N-linked glycosylation sites	883:930	all three potential N-linked glycosylation sites	883:930	We therefore characterized mutant G6Pases lacking one, two, or all three potential N-linked glycosylation sites.
9705299	1	42	theme	glucose-6-phosphatase	125:145	arg1	Deficiency					111:120	Deficiency	111:120	Deficiency of glucose-6-phosphatase (G6Pase), an endoplasmic reticulum transmembrane glycoprotein,	111:208	Deficiency of glucose-6-phosphatase (G6Pase), an endoplasmic reticulum transmembrane glycoprotein, causes glycogen storage disease type 1a.
9705299	4	43	from	loop	633:636	arg1	located					601:607	located	601:607	located	601:607	According to this model, Asn96, located in a 37-residue luminal loop, is a potential acceptor for oligosaccharides, whereas Asn203 and Asn276, located in a 12-residue cytoplasmic loop and helix 7, respectively, would not be utilized for this purpose.
9705299	1	44	theme	disease	234:240	arg1	1a					247:248	glycogen storage disease type 1a	217:248	glycogen storage disease type 1a	217:248	Deficiency of glucose-6-phosphatase (G6Pase), an endoplasmic reticulum transmembrane glycoprotein, causes glycogen storage disease type 1a.
9705299	6	45	gly	glycosylated	1001:1012	arg2	Asn96					1022:1026	Asn96	1022:1026	Asn96	1022:1026	Western blot and in vitro translation studies showed that G6Pase is glycosylated only at Asn96, further validating the nine-transmembrane topology model.
9705299	6	45	gly	glycosylated	1001:1012	arg1	G6Pase					991:996	G6Pase	991:996	G6Pase	991:996	Western blot and in vitro translation studies showed that G6Pase is glycosylated only at Asn96, further validating the nine-transmembrane topology model.
9705299	8	46	theme	Asn276	1361:1366	arg1	mutation					1349:1356	mutation	1349:1356	mutation of Asn276 to an Ala (N276A)	1349:1384	In contrast, mutation of Asn276 to an Ala (N276A) destabilized the enzyme and markedly reduced enzymatic activity.
9705299	1	47	theme	type	242:245	arg1	1a					247:248	glycogen storage disease type 1a	217:248	glycogen storage disease type 1a	217:248	Deficiency of glucose-6-phosphatase (G6Pase), an endoplasmic reticulum transmembrane glycoprotein, causes glycogen storage disease type 1a.
9705299	3	48	gly	glycosylation	486:498	arg2	sites					500:504	three potential asparagine (N)-linked glycosylation sites	448:504	three potential asparagine (N)-linked glycosylation sites	448:504	Sequence analysis predicts the presence of three potential asparagine (N)-linked glycosylation sites, N96TS, N203AS, and N276SS, conserved among mammalian G6Pases.
9705299	3	48	gly	glycosylation	486:498	arg2	three					448:452	three	448:452	three	448:452	Sequence analysis predicts the presence of three potential asparagine (N)-linked glycosylation sites, N96TS, N203AS, and N276SS, conserved among mammalian G6Pases.
9705299	3	48	gly	glycosylation	486:498	arg2	N276SS					526:531	N276SS	526:531	N276SS	526:531	Sequence analysis predicts the presence of three potential asparagine (N)-linked glycosylation sites, N96TS, N203AS, and N276SS, conserved among mammalian G6Pases.
9705299	3	48	gly	glycosylation	486:498	arg2	N203AS					514:519	N203AS	514:519	N203AS	514:519	Sequence analysis predicts the presence of three potential asparagine (N)-linked glycosylation sites, N96TS, N203AS, and N276SS, conserved among mammalian G6Pases.
9705299	3	48	gly	glycosylation	486:498	arg2	N96TS					507:511	N96TS	507:511	N96TS	507:511	Sequence analysis predicts the presence of three potential asparagine (N)-linked glycosylation sites, N96TS, N203AS, and N276SS, conserved among mammalian G6Pases.
9705299	3	49	theme	-linked	478:484	arg1	N203AS					514:519	N203AS	514:519	N203AS	514:519	Sequence analysis predicts the presence of three potential asparagine (N)-linked glycosylation sites, N96TS, N203AS, and N276SS, conserved among mammalian G6Pases.
9705299	3	49	theme	-linked	478:484	arg1	N276SS					526:531	N276SS	526:531	N276SS	526:531	Sequence analysis predicts the presence of three potential asparagine (N)-linked glycosylation sites, N96TS, N203AS, and N276SS, conserved among mammalian G6Pases.
9705299	3	49	theme	-linked	478:484	arg1	N96TS					507:511	N96TS	507:511	N96TS	507:511	Sequence analysis predicts the presence of three potential asparagine (N)-linked glycosylation sites, N96TS, N203AS, and N276SS, conserved among mammalian G6Pases.
9705299	3	49	theme	-linked	478:484	arg1	sites					500:504	three potential asparagine (N)-linked glycosylation sites	448:504	three potential asparagine (N)-linked glycosylation sites	448:504	Sequence analysis predicts the presence of three potential asparagine (N)-linked glycosylation sites, N96TS, N203AS, and N276SS, conserved among mammalian G6Pases.
9705299	0	50	theme	hydrophilic	62:72	arg1	loop					74:77	a luminal hydrophilic loop	52:77	a luminal hydrophilic loop in human glucose-6-phosphatase	52:108	Asparagine-linked oligosaccharides are localized to a luminal hydrophilic loop in human glucose-6-phosphatase.
9705299	0	51	from	loop	74:77	arg1	glucose-6-phosphatase					88:108	human glucose-6-phosphatase	82:108	human glucose-6-phosphatase	82:108	Asparagine-linked oligosaccharides are localized to a luminal hydrophilic loop in human glucose-6-phosphatase.
9705299	9	52	theme	catalytic	1575:1583	arg1	activity					1585:1592	catalytic activity	1575:1592	catalytic activity	1575:1592	We present additional evidence suggesting that the integrity of transmembrane helices is essential for G6Pase stability and catalytic activity.
9705299	2	53	theme	helical	374:380	arg1	model					382:386	a nine-transmembrane helical model	353:386	a nine-transmembrane helical model for this enzyme	353:402	We have recently shown that human G6Pase contains an odd number of transmembrane segments, supporting a nine-transmembrane helical model for this enzyme.
9705299	0	54	theme	luminal	54:60	arg1	loop					74:77	a luminal hydrophilic loop	52:77	a luminal hydrophilic loop in human glucose-6-phosphatase	52:108	Asparagine-linked oligosaccharides are localized to a luminal hydrophilic loop in human glucose-6-phosphatase.
9705299	2	55	theme	nine-transmembrane	355:372	arg1	model					382:386	a nine-transmembrane helical model	353:386	a nine-transmembrane helical model for this enzyme	353:402	We have recently shown that human G6Pase contains an odd number of transmembrane segments, supporting a nine-transmembrane helical model for this enzyme.
9705299	4	56	from	located	712:718	arg1	helix					757:761	helix 7	757:763	helix 7	757:763	According to this model, Asn96, located in a 37-residue luminal loop, is a potential acceptor for oligosaccharides, whereas Asn203 and Asn276, located in a 12-residue cytoplasmic loop and helix 7, respectively, would not be utilized for this purpose.
9705299	4	56	from	located	712:718	arg1	loop					748:751	a 12-residue cytoplasmic loop	723:751	a 12-residue cytoplasmic loop	723:751	According to this model, Asn96, located in a 37-residue luminal loop, is a potential acceptor for oligosaccharides, whereas Asn203 and Asn276, located in a 12-residue cytoplasmic loop and helix 7, respectively, would not be utilized for this purpose.
9705299	4	57	theme	located	712:718	arg1	Asn203					693:698	Asn203	693:698	Asn203	693:698	According to this model, Asn96, located in a 37-residue luminal loop, is a potential acceptor for oligosaccharides, whereas Asn203 and Asn276, located in a 12-residue cytoplasmic loop and helix 7, respectively, would not be utilized for this purpose.
9705299	4	58	theme	cytoplasmic	736:746	arg1	loop					748:751	a 12-residue cytoplasmic loop	723:751	a 12-residue cytoplasmic loop	723:751	According to this model, Asn96, located in a 37-residue luminal loop, is a potential acceptor for oligosaccharides, whereas Asn203 and Asn276, located in a 12-residue cytoplasmic loop and helix 7, respectively, would not be utilized for this purpose.
9705299	2	59	theme	human	279:283	arg1	G6Pase					285:290	human G6Pase	279:290	human G6Pase	279:290	We have recently shown that human G6Pase contains an odd number of transmembrane segments, supporting a nine-transmembrane helical model for this enzyme.
9705299	9	60	theme	additional	1462:1471	arg1	evidence					1473:1480	additional evidence	1462:1480	additional evidence suggesting that the integrity of transmembrane helices is essential for G6Pase stability and catalytic activity	1462:1592	We present additional evidence suggesting that the integrity of transmembrane helices is essential for G6Pase stability and catalytic activity.
9705299	5	61	link	N-linked	903:910	arg1	sites					926:930	all three potential N-linked glycosylation sites	883:930	all three potential N-linked glycosylation sites	883:930	We therefore characterized mutant G6Pases lacking one, two, or all three potential N-linked glycosylation sites.
9705299	4	62	theme	located	601:607	arg1	Asn96					594:598	Asn96	594:598	Asn96	594:598	According to this model, Asn96, located in a 37-residue luminal loop, is a potential acceptor for oligosaccharides, whereas Asn203 and Asn276, located in a 12-residue cytoplasmic loop and helix 7, respectively, would not be utilized for this purpose.
9705299	4	62	theme	located	601:607	arg1	acceptor					654:661	a potential acceptor	642:661	a potential acceptor for oligosaccharides	642:682	According to this model, Asn96, located in a 37-residue luminal loop, is a potential acceptor for oligosaccharides, whereas Asn203 and Asn276, located in a 12-residue cytoplasmic loop and helix 7, respectively, would not be utilized for this purpose.
9705299	8	63	theme	enzymatic	1431:1439	arg1	activity					1441:1448	enzymatic activity	1431:1448	enzymatic activity	1431:1448	In contrast, mutation of Asn276 to an Ala (N276A) destabilized the enzyme and markedly reduced enzymatic activity.
9705299	3	64	theme	glycosylation	486:498	arg1	N203AS					514:519	N203AS	514:519	N203AS	514:519	Sequence analysis predicts the presence of three potential asparagine (N)-linked glycosylation sites, N96TS, N203AS, and N276SS, conserved among mammalian G6Pases.
9705299	3	64	theme	glycosylation	486:498	arg1	N276SS					526:531	N276SS	526:531	N276SS	526:531	Sequence analysis predicts the presence of three potential asparagine (N)-linked glycosylation sites, N96TS, N203AS, and N276SS, conserved among mammalian G6Pases.
9705299	3	64	theme	glycosylation	486:498	arg1	N96TS					507:511	N96TS	507:511	N96TS	507:511	Sequence analysis predicts the presence of three potential asparagine (N)-linked glycosylation sites, N96TS, N203AS, and N276SS, conserved among mammalian G6Pases.
9705299	3	64	theme	glycosylation	486:498	arg1	sites					500:504	three potential asparagine (N)-linked glycosylation sites	448:504	three potential asparagine (N)-linked glycosylation sites	448:504	Sequence analysis predicts the presence of three potential asparagine (N)-linked glycosylation sites, N96TS, N203AS, and N276SS, conserved among mammalian G6Pases.
9705299	7	65	theme	major	1270:1274	arg1	role					1276:1279	a major role	1268:1279	a major role	1268:1279	Substituting Asn96 with an Ala (N96A) moderately reduced enzymatic activity and had no effect on G6Pase synthesis or degradation, suggesting that oligosaccharide chains do not play a major role in protecting the enzyme from proteolytic degradation.
9705299	4	66	theme	37-residue	614:623	arg1	loop					633:636	a 37-residue luminal loop	612:636	a 37-residue luminal loop	612:636	According to this model, Asn96, located in a 37-residue luminal loop, is a potential acceptor for oligosaccharides, whereas Asn203 and Asn276, located in a 12-residue cytoplasmic loop and helix 7, respectively, would not be utilized for this purpose.
9705299	7	67	theme	proteolytic	1311:1321	arg1	degradation					1323:1333	proteolytic degradation	1311:1333	proteolytic degradation	1311:1333	Substituting Asn96 with an Ala (N96A) moderately reduced enzymatic activity and had no effect on G6Pase synthesis or degradation, suggesting that oligosaccharide chains do not play a major role in protecting the enzyme from proteolytic degradation.
9705299	7	68	theme	oligosaccharide	1233:1247	arg1	chains					1249:1254	oligosaccharide chains	1233:1254	oligosaccharide chains	1233:1254	Substituting Asn96 with an Ala (N96A) moderately reduced enzymatic activity and had no effect on G6Pase synthesis or degradation, suggesting that oligosaccharide chains do not play a major role in protecting the enzyme from proteolytic degradation.
9705299	1	69	theme	endoplasmic	160:170	arg1	reticulum					172:180	an endoplasmic reticulum	157:180	an endoplasmic reticulum transmembrane glycoprotein	157:207	Deficiency of glucose-6-phosphatase (G6Pase), an endoplasmic reticulum transmembrane glycoprotein, causes glycogen storage disease type 1a.
7744025	1	0	dep	in	395:396	arg1	vitro					398:402	vitro	398:402	vitro	398:402	A synthetic peptide [TAP25, (T1aAPPAHGVT9S10APDT14RPAPGS20)T1bAPPA5b] corresponding to one repeat (T1a-S20) and five overlapping amino acids (T1b-A5b) of the MUC1 core protein served as an acceptor substrate for in vitro glycosylation.
7744025	6	1	theme	peptides	1310:1317	arg1	%					1288:1288	at least 20%	1277:1288	at least 20% of the glycosylated peptides	1277:1317	In addition, evidence was obtained that at least 20% of the glycosylated peptides exhibited GalNAc incorporation at Ser20.
7744025	6	1	theme	peptides	1310:1317	arg1	peptides					1310:1317	the glycosylated peptides	1293:1317	the glycosylated peptides	1293:1317	In addition, evidence was obtained that at least 20% of the glycosylated peptides exhibited GalNAc incorporation at Ser20.
7744025	2	2	dep	line	563:566	arg1	T47D					568:571	T47D	568:571	the breast carcinoma cell line T47D	537:571	TAP25 was glycosylated using the detergent-solubilized UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases from the breast carcinoma cell line T47D, the colon carcinoma cell line HT29 and from human premature skim milk.
7744025	8	3	theme	motif	1762:1766	arg1	epitopes					1745:1752	overlapping epitopes	1733:1752	overlapping epitopes of this motif	1733:1766	Although Thr14 within the PDTRP motif of the tandem repeats remained non-glycosylated, the introduction of GalNAc into adjacent positions significantly decreased the immunoreactivity of antibodies SM-3, HMFG-1 and HMFG-2 defining overlapping epitopes of this motif.
7744025	7	4	theme	acceptor	1445:1452	arg1	sites					1454:1458	the three acceptor sites	1435:1458	the three acceptor sites	1435:1458	On the basis of kinetic studies a preferred sequence of GalNAc addition to the three acceptor sites has been concluded (Thr9-->Thr1b-->Ser20).
7744025	4	5	theme	triglycosylated	862:876	arg1	species					838:844	Three different glycosylation species	808:844	Three different glycosylation species	808:844	Three different glycosylation species, mono-, di- and triglycosylated peptides were identified.
7744025	4	5	theme	triglycosylated	862:876	arg1	peptides					878:885	triglycosylated peptides	862:885	triglycosylated peptides	862:885	Three different glycosylation species, mono-, di- and triglycosylated peptides were identified.
7744025	5	6	dep	residues	1056:1063	arg1	Thr9					1065:1068	Thr9	1065:1068	Thr9	1065:1068	Automated Edman sequencing and LSIMS of proteolytic fragments independently revealed the sites of GalNAc incorporation and confirmed that the threonine residues Thr9 and Thr1b are the preferred sites of glycosylation independent of the enzyme source, while Thr14 remained non-glycosylated even with the enzyme preparation from milk.
7744025	5	6	dep	residues	1056:1063	arg1	residues					1056:1063	the threonine residues	1042:1063	the threonine residues Thr9 and Thr1b	1042:1078	Automated Edman sequencing and LSIMS of proteolytic fragments independently revealed the sites of GalNAc incorporation and confirmed that the threonine residues Thr9 and Thr1b are the preferred sites of glycosylation independent of the enzyme source, while Thr14 remained non-glycosylated even with the enzyme preparation from milk.
7744025	5	6	dep	residues	1056:1063	arg1	Thr1b					1074:1078	Thr1b	1074:1078	Thr1b	1074:1078	Automated Edman sequencing and LSIMS of proteolytic fragments independently revealed the sites of GalNAc incorporation and confirmed that the threonine residues Thr9 and Thr1b are the preferred sites of glycosylation independent of the enzyme source, while Thr14 remained non-glycosylated even with the enzyme preparation from milk.
7744025	3	7	theme	secondary	767:775	arg1	spectrometry					786:797	liquid secondary ion mass spectrometry	760:797	liquid secondary ion mass spectrometry (LSIMS)	760:805	The glycosylated peptides were isolated by ultrafiltration, purified by reverse-phase HPLC and further analysed by liquid secondary ion mass spectrometry (LSIMS).
7744025	3	7	theme	secondary	767:775	arg1	LSIMS					800:804	LSIMS	800:804	LSIMS	800:804	The glycosylated peptides were isolated by ultrafiltration, purified by reverse-phase HPLC and further analysed by liquid secondary ion mass spectrometry (LSIMS).
7744025	1	8	theme	synthetic	185:193	arg1	T1aAPPAHGVT9S10APDT14RPAPGS20					212:240	T1aAPPAHGVT9S10APDT14RPAPGS20	212:240	T1aAPPAHGVT9S10APDT14RPAPGS20	212:240	A synthetic peptide [TAP25, (T1aAPPAHGVT9S10APDT14RPAPGS20)T1bAPPA5b] corresponding to one repeat (T1a-S20) and five overlapping amino acids (T1b-A5b) of the MUC1 core protein served as an acceptor substrate for in vitro glycosylation.
7744025	1	8	theme	synthetic	185:193	arg1	substrate					381:389	an acceptor substrate	369:389	an acceptor substrate for in vitro glycosylation	369:416	A synthetic peptide [TAP25, (T1aAPPAHGVT9S10APDT14RPAPGS20)T1bAPPA5b] corresponding to one repeat (T1a-S20) and five overlapping amino acids (T1b-A5b) of the MUC1 core protein served as an acceptor substrate for in vitro glycosylation.
7744025	1	8	theme	synthetic	185:193	arg1	peptide					195:201	A synthetic peptide [TAP25	183:208	A synthetic peptide [TAP25, (T1aAPPAHGVT9S10APDT14RPAPGS20)T1bAPPA5b] corresponding to one repeat (T1a-S20) and five overlapping amino acids (T1b-A5b) of the MUC1 core protein	183:357	A synthetic peptide [TAP25, (T1aAPPAHGVT9S10APDT14RPAPGS20)T1bAPPA5b] corresponding to one repeat (T1a-S20) and five overlapping amino acids (T1b-A5b) of the MUC1 core protein served as an acceptor substrate for in vitro glycosylation.
7744025	7	9	theme	addition	1423:1430	arg1	sequence					1404:1411	a preferred sequence	1392:1411	a preferred sequence of GalNAc addition to the three acceptor sites	1392:1458	On the basis of kinetic studies a preferred sequence of GalNAc addition to the three acceptor sites has been concluded (Thr9-->Thr1b-->Ser20).
7744025	9	10	gly	glycosylation	1788:1800	arg2	Thr9					1805:1808	Thr9	1805:1808	Thr9	1805:1808	It is assumed that glycosylation at Thr9, Thr1b and Ser20 distorts the peptide conformation of the binding epitope.
7744025	9	10	gly	glycosylation	1788:1800	arg1	Ser20					1821:1825	Ser20	1821:1825	Ser20	1821:1825	It is assumed that glycosylation at Thr9, Thr1b and Ser20 distorts the peptide conformation of the binding epitope.
7744025	9	10	gly	glycosylation	1788:1800	arg2	Thr1b					1811:1815	Thr1b	1811:1815	Thr1b	1811:1815	It is assumed that glycosylation at Thr9, Thr1b and Ser20 distorts the peptide conformation of the binding epitope.
7744025	9	10	gly	glycosylation	1788:1800	arg2	Ser20					1821:1825	Ser20	1821:1825	Ser20	1821:1825	It is assumed that glycosylation at Thr9, Thr1b and Ser20 distorts the peptide conformation of the binding epitope.
7744025	9	10	gly	glycosylation	1788:1800	arg1	Thr9					1805:1808	Thr9	1805:1808	Thr9	1805:1808	It is assumed that glycosylation at Thr9, Thr1b and Ser20 distorts the peptide conformation of the binding epitope.
7744025	9	10	gly	glycosylation	1788:1800	arg1	Thr1b					1811:1815	Thr1b	1811:1815	Thr1b	1811:1815	It is assumed that glycosylation at Thr9, Thr1b and Ser20 distorts the peptide conformation of the binding epitope.
7744025	5	11	theme	independent	1121:1131	arg1	glycosylation					1107:1119	glycosylation	1107:1119	glycosylation	1107:1119	Automated Edman sequencing and LSIMS of proteolytic fragments independently revealed the sites of GalNAc incorporation and confirmed that the threonine residues Thr9 and Thr1b are the preferred sites of glycosylation independent of the enzyme source, while Thr14 remained non-glycosylated even with the enzyme preparation from milk.
7744025	5	11	theme	independent	1121:1131	arg1	sites					1098:1102	the preferred sites	1084:1102	the preferred sites of glycosylation independent of the enzyme source	1084:1152	Automated Edman sequencing and LSIMS of proteolytic fragments independently revealed the sites of GalNAc incorporation and confirmed that the threonine residues Thr9 and Thr1b are the preferred sites of glycosylation independent of the enzyme source, while Thr14 remained non-glycosylated even with the enzyme preparation from milk.
7744025	5	11	theme	independent	1121:1131	arg1	residues					1056:1063	the threonine residues	1042:1063	the threonine residues Thr9 and Thr1b	1042:1078	Automated Edman sequencing and LSIMS of proteolytic fragments independently revealed the sites of GalNAc incorporation and confirmed that the threonine residues Thr9 and Thr1b are the preferred sites of glycosylation independent of the enzyme source, while Thr14 remained non-glycosylated even with the enzyme preparation from milk.
7744025	4	12	gly	triglycosylated	862:876	arg1	species					838:844	Three different glycosylation species	808:844	Three different glycosylation species	808:844	Three different glycosylation species, mono-, di- and triglycosylated peptides were identified.
7744025	4	12	gly	triglycosylated	862:876	arg1	peptides					878:885	triglycosylated peptides	862:885	triglycosylated peptides	862:885	Three different glycosylation species, mono-, di- and triglycosylated peptides were identified.
7744025	2	13	theme	cell	594:597	arg1	line					599:602	colon carcinoma cell line	578:602	the colon carcinoma cell line HT29	574:607	TAP25 was glycosylated using the detergent-solubilized UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases from the breast carcinoma cell line T47D, the colon carcinoma cell line HT29 and from human premature skim milk.
7744025	2	13	theme	cell	594:597	arg1	line					563:566	breast carcinoma cell line	541:566	the breast carcinoma cell line T47D	537:571	TAP25 was glycosylated using the detergent-solubilized UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases from the breast carcinoma cell line T47D, the colon carcinoma cell line HT29 and from human premature skim milk.
7744025	7	14	theme	preferred	1394:1402	arg1	sequence					1404:1411	a preferred sequence	1392:1411	a preferred sequence of GalNAc addition to the three acceptor sites	1392:1458	On the basis of kinetic studies a preferred sequence of GalNAc addition to the three acceptor sites has been concluded (Thr9-->Thr1b-->Ser20).
7744025	3	15	theme	mass	781:784	arg1	spectrometry					786:797	liquid secondary ion mass spectrometry	760:797	liquid secondary ion mass spectrometry (LSIMS)	760:805	The glycosylated peptides were isolated by ultrafiltration, purified by reverse-phase HPLC and further analysed by liquid secondary ion mass spectrometry (LSIMS).
7744025	3	15	theme	mass	781:784	arg1	LSIMS					800:804	LSIMS	800:804	LSIMS	800:804	The glycosylated peptides were isolated by ultrafiltration, purified by reverse-phase HPLC and further analysed by liquid secondary ion mass spectrometry (LSIMS).
7744025	2	16	theme	colon	578:582	arg1	line					599:602	colon carcinoma cell line	578:602	the colon carcinoma cell line HT29	574:607	TAP25 was glycosylated using the detergent-solubilized UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases from the breast carcinoma cell line T47D, the colon carcinoma cell line HT29 and from human premature skim milk.
7744025	2	16	theme	colon	578:582	arg1	line					563:566	breast carcinoma cell line	541:566	the breast carcinoma cell line T47D	537:571	TAP25 was glycosylated using the detergent-solubilized UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases from the breast carcinoma cell line T47D, the colon carcinoma cell line HT29 and from human premature skim milk.
7744025	6	17	theme	GalNAc	1329:1334	arg1	incorporation					1336:1348	GalNAc incorporation	1329:1348	GalNAc incorporation	1329:1348	In addition, evidence was obtained that at least 20% of the glycosylated peptides exhibited GalNAc incorporation at Ser20.
7744025	1	18	theme	in	395:396	arg1	glycosylation					404:416	in vitro glycosylation	395:416	in vitro glycosylation	395:416	A synthetic peptide [TAP25, (T1aAPPAHGVT9S10APDT14RPAPGS20)T1bAPPA5b] corresponding to one repeat (T1a-S20) and five overlapping amino acids (T1b-A5b) of the MUC1 core protein served as an acceptor substrate for in vitro glycosylation.
7744025	5	19	theme	fragments	956:964	arg1	sequencing					920:929	Automated Edman sequencing	904:929	Automated Edman sequencing	904:929	Automated Edman sequencing and LSIMS of proteolytic fragments independently revealed the sites of GalNAc incorporation and confirmed that the threonine residues Thr9 and Thr1b are the preferred sites of glycosylation independent of the enzyme source, while Thr14 remained non-glycosylated even with the enzyme preparation from milk.
7744025	5	19	theme	fragments	956:964	arg1	LSIMS					935:939	LSIMS	935:939	LSIMS	935:939	Automated Edman sequencing and LSIMS of proteolytic fragments independently revealed the sites of GalNAc incorporation and confirmed that the threonine residues Thr9 and Thr1b are the preferred sites of glycosylation independent of the enzyme source, while Thr14 remained non-glycosylated even with the enzyme preparation from milk.
7744025	0	20	theme	GalNAc	45:50	arg1	order					15:19	order	15:19	order	15:19	Studies on the order and site specificity of GalNAc transfer to MUC1 tandem repeats by UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferase from milk or mammary carcinoma cells.
7744025	0	20	theme	GalNAc	45:50	arg1	specificity					30:40	site specificity	25:40	site specificity	25:40	Studies on the order and site specificity of GalNAc transfer to MUC1 tandem repeats by UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferase from milk or mammary carcinoma cells.
7744025	5	21	theme	Edman	914:918	arg1	sequencing					920:929	Automated Edman sequencing	904:929	Automated Edman sequencing	904:929	Automated Edman sequencing and LSIMS of proteolytic fragments independently revealed the sites of GalNAc incorporation and confirmed that the threonine residues Thr9 and Thr1b are the preferred sites of glycosylation independent of the enzyme source, while Thr14 remained non-glycosylated even with the enzyme preparation from milk.
7744025	0	22	theme	mammary	158:164	arg1	cells					176:180	mammary carcinoma cells	158:180	mammary carcinoma cells	158:180	Studies on the order and site specificity of GalNAc transfer to MUC1 tandem repeats by UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferase from milk or mammary carcinoma cells.
7744025	5	23	theme	preferred	1088:1096	arg1	glycosylation					1107:1119	glycosylation	1107:1119	glycosylation	1107:1119	Automated Edman sequencing and LSIMS of proteolytic fragments independently revealed the sites of GalNAc incorporation and confirmed that the threonine residues Thr9 and Thr1b are the preferred sites of glycosylation independent of the enzyme source, while Thr14 remained non-glycosylated even with the enzyme preparation from milk.
7744025	5	23	theme	preferred	1088:1096	arg1	sites					1098:1102	the preferred sites	1084:1102	the preferred sites of glycosylation independent of the enzyme source	1084:1152	Automated Edman sequencing and LSIMS of proteolytic fragments independently revealed the sites of GalNAc incorporation and confirmed that the threonine residues Thr9 and Thr1b are the preferred sites of glycosylation independent of the enzyme source, while Thr14 remained non-glycosylated even with the enzyme preparation from milk.
7744025	5	23	theme	preferred	1088:1096	arg1	residues					1056:1063	the threonine residues	1042:1063	the threonine residues Thr9 and Thr1b	1042:1078	Automated Edman sequencing and LSIMS of proteolytic fragments independently revealed the sites of GalNAc incorporation and confirmed that the threonine residues Thr9 and Thr1b are the preferred sites of glycosylation independent of the enzyme source, while Thr14 remained non-glycosylated even with the enzyme preparation from milk.
7744025	6	24	gly	glycosylated	1297:1308	arg1	peptides					1310:1317	the glycosylated peptides	1293:1317	the glycosylated peptides	1293:1317	In addition, evidence was obtained that at least 20% of the glycosylated peptides exhibited GalNAc incorporation at Ser20.
7744025	2	25	theme	carcinoma	548:556	arg1	line					599:602	colon carcinoma cell line	578:602	the colon carcinoma cell line HT29	574:607	TAP25 was glycosylated using the detergent-solubilized UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases from the breast carcinoma cell line T47D, the colon carcinoma cell line HT29 and from human premature skim milk.
7744025	2	25	theme	carcinoma	548:556	arg1	line					563:566	breast carcinoma cell line	541:566	the breast carcinoma cell line T47D	537:571	TAP25 was glycosylated using the detergent-solubilized UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases from the breast carcinoma cell line T47D, the colon carcinoma cell line HT29 and from human premature skim milk.
7744025	0	26	from	Studies	0:6	arg1	order					15:19	order	15:19	order	15:19	Studies on the order and site specificity of GalNAc transfer to MUC1 tandem repeats by UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferase from milk or mammary carcinoma cells.
7744025	0	26	from	Studies	0:6	arg1	specificity					30:40	site specificity	25:40	site specificity	25:40	Studies on the order and site specificity of GalNAc transfer to MUC1 tandem repeats by UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferase from milk or mammary carcinoma cells.
7744025	0	27	theme	tandem	69:74	arg1	repeats					76:82	MUC1 tandem repeats	64:82	MUC1 tandem repeats	64:82	Studies on the order and site specificity of GalNAc transfer to MUC1 tandem repeats by UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferase from milk or mammary carcinoma cells.
7744025	5	28	theme	GalNAc	1002:1007	arg1	incorporation					1009:1021	GalNAc incorporation	1002:1021	GalNAc incorporation	1002:1021	Automated Edman sequencing and LSIMS of proteolytic fragments independently revealed the sites of GalNAc incorporation and confirmed that the threonine residues Thr9 and Thr1b are the preferred sites of glycosylation independent of the enzyme source, while Thr14 remained non-glycosylated even with the enzyme preparation from milk.
7744025	8	29	theme	antibodies	1689:1698	arg1	immunoreactivity					1669:1684	the immunoreactivity	1665:1684	the immunoreactivity of antibodies SM-3, HMFG-1 and HMFG-2 defining overlapping epitopes of this motif	1665:1766	Although Thr14 within the PDTRP motif of the tandem repeats remained non-glycosylated, the introduction of GalNAc into adjacent positions significantly decreased the immunoreactivity of antibodies SM-3, HMFG-1 and HMFG-2 defining overlapping epitopes of this motif.
7744025	1	30	theme	core	346:349	arg1	protein					351:357	the MUC1 core protein	337:357	the MUC1 core protein	337:357	A synthetic peptide [TAP25, (T1aAPPAHGVT9S10APDT14RPAPGS20)T1bAPPA5b] corresponding to one repeat (T1a-S20) and five overlapping amino acids (T1b-A5b) of the MUC1 core protein served as an acceptor substrate for in vitro glycosylation.
7744025	9	31	theme	binding	1868:1874	arg1	epitope					1876:1882	the binding epitope	1864:1882	the binding epitope	1864:1882	It is assumed that glycosylation at Thr9, Thr1b and Ser20 distorts the peptide conformation of the binding epitope.
7744025	9	32	theme	peptide	1840:1846	arg1	conformation					1848:1859	the peptide conformation	1836:1859	the peptide conformation of the binding epitope	1836:1882	It is assumed that glycosylation at Thr9, Thr1b and Ser20 distorts the peptide conformation of the binding epitope.
7744025	8	33	theme	repeats	1555:1561	arg1	motif					1535:1539	the PDTRP motif	1525:1539	the PDTRP motif of the tandem repeats	1525:1561	Although Thr14 within the PDTRP motif of the tandem repeats remained non-glycosylated, the introduction of GalNAc into adjacent positions significantly decreased the immunoreactivity of antibodies SM-3, HMFG-1 and HMFG-2 defining overlapping epitopes of this motif.
7744025	2	34	theme	detergent-solubilized	452:472	arg1	N-acetylgalactosaminyltransferases					497:530	the detergent-solubilized UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases	448:530	the detergent-solubilized UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases from the breast carcinoma cell line T47D, the colon carcinoma cell line HT29 and from human premature skim milk	448:642	TAP25 was glycosylated using the detergent-solubilized UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases from the breast carcinoma cell line T47D, the colon carcinoma cell line HT29 and from human premature skim milk.
7744025	0	35	from	cells	176:180	arg1	N-acetylgalactosaminyltransferase					111:143	polypeptide N-acetylgalactosaminyltransferase	99:143	UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferase from milk or mammary carcinoma cells	87:180	Studies on the order and site specificity of GalNAc transfer to MUC1 tandem repeats by UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferase from milk or mammary carcinoma cells.
7744025	7	36	dep	concluded	1469:1477	arg1	Thr9-->Thr1b-->Ser20					1480:1499	Thr9-->Thr1b-->Ser20	1480:1499	Thr9-->Thr1b-->Ser20	1480:1499	On the basis of kinetic studies a preferred sequence of GalNAc addition to the three acceptor sites has been concluded (Thr9-->Thr1b-->Ser20).
7744025	1	37	theme	amino	312:316	arg1	T1b-A5b					325:331	T1b-A5b	325:331	T1b-A5b	325:331	A synthetic peptide [TAP25, (T1aAPPAHGVT9S10APDT14RPAPGS20)T1bAPPA5b] corresponding to one repeat (T1a-S20) and five overlapping amino acids (T1b-A5b) of the MUC1 core protein served as an acceptor substrate for in vitro glycosylation.
7744025	1	37	theme	amino	312:316	arg1	acids					318:322	five overlapping amino acids	295:322	five overlapping amino acids (T1b-A5b) of the MUC1 core protein	295:357	A synthetic peptide [TAP25, (T1aAPPAHGVT9S10APDT14RPAPGS20)T1bAPPA5b] corresponding to one repeat (T1a-S20) and five overlapping amino acids (T1b-A5b) of the MUC1 core protein served as an acceptor substrate for in vitro glycosylation.
7744025	5	38	gly	glycosylation	1107:1119	arg2	glycosylation					1107:1119	glycosylation	1107:1119	glycosylation	1107:1119	Automated Edman sequencing and LSIMS of proteolytic fragments independently revealed the sites of GalNAc incorporation and confirmed that the threonine residues Thr9 and Thr1b are the preferred sites of glycosylation independent of the enzyme source, while Thr14 remained non-glycosylated even with the enzyme preparation from milk.
7744025	5	38	gly	glycosylation	1107:1119	arg2	sites					1098:1102	the preferred sites	1084:1102	the preferred sites of glycosylation independent of the enzyme source	1084:1152	Automated Edman sequencing and LSIMS of proteolytic fragments independently revealed the sites of GalNAc incorporation and confirmed that the threonine residues Thr9 and Thr1b are the preferred sites of glycosylation independent of the enzyme source, while Thr14 remained non-glycosylated even with the enzyme preparation from milk.
7744025	5	38	gly	glycosylation	1107:1119	arg2	residues					1056:1063	the threonine residues	1042:1063	the threonine residues Thr9 and Thr1b	1042:1078	Automated Edman sequencing and LSIMS of proteolytic fragments independently revealed the sites of GalNAc incorporation and confirmed that the threonine residues Thr9 and Thr1b are the preferred sites of glycosylation independent of the enzyme source, while Thr14 remained non-glycosylated even with the enzyme preparation from milk.
7744025	4	39	theme	different	814:822	arg1	species					838:844	Three different glycosylation species	808:844	Three different glycosylation species	808:844	Three different glycosylation species, mono-, di- and triglycosylated peptides were identified.
7744025	4	39	theme	different	814:822	arg1	di-					854:856	di-	854:856	di-	854:856	Three different glycosylation species, mono-, di- and triglycosylated peptides were identified.
7744025	4	39	theme	different	814:822	arg1	peptides					878:885	triglycosylated peptides	862:885	triglycosylated peptides	862:885	Three different glycosylation species, mono-, di- and triglycosylated peptides were identified.
7744025	4	39	theme	different	814:822	arg1	mono-					847:851	mono-	847:851	mono-	847:851	Three different glycosylation species, mono-, di- and triglycosylated peptides were identified.
7744025	5	40	theme	threonine	1046:1054	arg1	glycosylation					1107:1119	glycosylation	1107:1119	glycosylation	1107:1119	Automated Edman sequencing and LSIMS of proteolytic fragments independently revealed the sites of GalNAc incorporation and confirmed that the threonine residues Thr9 and Thr1b are the preferred sites of glycosylation independent of the enzyme source, while Thr14 remained non-glycosylated even with the enzyme preparation from milk.
7744025	5	40	theme	threonine	1046:1054	arg1	Thr9					1065:1068	Thr9	1065:1068	Thr9	1065:1068	Automated Edman sequencing and LSIMS of proteolytic fragments independently revealed the sites of GalNAc incorporation and confirmed that the threonine residues Thr9 and Thr1b are the preferred sites of glycosylation independent of the enzyme source, while Thr14 remained non-glycosylated even with the enzyme preparation from milk.
7744025	5	40	theme	threonine	1046:1054	arg1	sites					1098:1102	the preferred sites	1084:1102	the preferred sites of glycosylation independent of the enzyme source	1084:1152	Automated Edman sequencing and LSIMS of proteolytic fragments independently revealed the sites of GalNAc incorporation and confirmed that the threonine residues Thr9 and Thr1b are the preferred sites of glycosylation independent of the enzyme source, while Thr14 remained non-glycosylated even with the enzyme preparation from milk.
7744025	5	40	theme	threonine	1046:1054	arg1	residues					1056:1063	the threonine residues	1042:1063	the threonine residues Thr9 and Thr1b	1042:1078	Automated Edman sequencing and LSIMS of proteolytic fragments independently revealed the sites of GalNAc incorporation and confirmed that the threonine residues Thr9 and Thr1b are the preferred sites of glycosylation independent of the enzyme source, while Thr14 remained non-glycosylated even with the enzyme preparation from milk.
7744025	5	40	theme	threonine	1046:1054	arg1	Thr1b					1074:1078	Thr1b	1074:1078	Thr1b	1074:1078	Automated Edman sequencing and LSIMS of proteolytic fragments independently revealed the sites of GalNAc incorporation and confirmed that the threonine residues Thr9 and Thr1b are the preferred sites of glycosylation independent of the enzyme source, while Thr14 remained non-glycosylated even with the enzyme preparation from milk.
7744025	3	41	theme	reverse-phase	717:729	arg1	HPLC					731:734	reverse-phase HPLC	717:734	reverse-phase HPLC	717:734	The glycosylated peptides were isolated by ultrafiltration, purified by reverse-phase HPLC and further analysed by liquid secondary ion mass spectrometry (LSIMS).
7744025	2	42	theme	premature	624:632	arg1	milk					639:642	human premature skim milk	618:642	human premature skim milk	618:642	TAP25 was glycosylated using the detergent-solubilized UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases from the breast carcinoma cell line T47D, the colon carcinoma cell line HT29 and from human premature skim milk.
7744025	3	43	gly	glycosylated	649:660	arg1	peptides					662:669	The glycosylated peptides	645:669	The glycosylated peptides	645:669	The glycosylated peptides were isolated by ultrafiltration, purified by reverse-phase HPLC and further analysed by liquid secondary ion mass spectrometry (LSIMS).
7744025	6	44	theme	glycosylated	1297:1308	arg1	peptides					1310:1317	the glycosylated peptides	1293:1317	the glycosylated peptides	1293:1317	In addition, evidence was obtained that at least 20% of the glycosylated peptides exhibited GalNAc incorporation at Ser20.
7744025	0	45	from	milk	150:153	arg1	N-acetylgalactosaminyltransferase					111:143	polypeptide N-acetylgalactosaminyltransferase	99:143	UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferase from milk or mammary carcinoma cells	87:180	Studies on the order and site specificity of GalNAc transfer to MUC1 tandem repeats by UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferase from milk or mammary carcinoma cells.
7744025	5	46	from	milk	1231:1234	arg1	preparation					1214:1224	the enzyme preparation	1203:1224	the enzyme preparation from milk	1203:1234	Automated Edman sequencing and LSIMS of proteolytic fragments independently revealed the sites of GalNAc incorporation and confirmed that the threonine residues Thr9 and Thr1b are the preferred sites of glycosylation independent of the enzyme source, while Thr14 remained non-glycosylated even with the enzyme preparation from milk.
7744025	2	47	theme	skim	634:637	arg1	milk					639:642	human premature skim milk	618:642	human premature skim milk	618:642	TAP25 was glycosylated using the detergent-solubilized UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases from the breast carcinoma cell line T47D, the colon carcinoma cell line HT29 and from human premature skim milk.
7744025	8	48	theme	adjacent	1622:1629	arg1	positions					1631:1639	adjacent positions	1622:1639	adjacent positions	1622:1639	Although Thr14 within the PDTRP motif of the tandem repeats remained non-glycosylated, the introduction of GalNAc into adjacent positions significantly decreased the immunoreactivity of antibodies SM-3, HMFG-1 and HMFG-2 defining overlapping epitopes of this motif.
7744025	2	49	theme	human	618:622	arg1	milk					639:642	human premature skim milk	618:642	human premature skim milk	618:642	TAP25 was glycosylated using the detergent-solubilized UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases from the breast carcinoma cell line T47D, the colon carcinoma cell line HT29 and from human premature skim milk.
7744025	3	50	theme	ion	777:779	arg1	spectrometry					786:797	liquid secondary ion mass spectrometry	760:797	liquid secondary ion mass spectrometry (LSIMS)	760:805	The glycosylated peptides were isolated by ultrafiltration, purified by reverse-phase HPLC and further analysed by liquid secondary ion mass spectrometry (LSIMS).
7744025	3	50	theme	ion	777:779	arg1	LSIMS					800:804	LSIMS	800:804	LSIMS	800:804	The glycosylated peptides were isolated by ultrafiltration, purified by reverse-phase HPLC and further analysed by liquid secondary ion mass spectrometry (LSIMS).
7744025	0	51	theme	polypeptide	99:109	arg1	N-acetylgalactosaminyltransferase					111:143	polypeptide N-acetylgalactosaminyltransferase	99:143	UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferase from milk or mammary carcinoma cells	87:180	Studies on the order and site specificity of GalNAc transfer to MUC1 tandem repeats by UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferase from milk or mammary carcinoma cells.
7744025	3	52	theme	liquid	760:765	arg1	spectrometry					786:797	liquid secondary ion mass spectrometry	760:797	liquid secondary ion mass spectrometry (LSIMS)	760:805	The glycosylated peptides were isolated by ultrafiltration, purified by reverse-phase HPLC and further analysed by liquid secondary ion mass spectrometry (LSIMS).
7744025	3	52	theme	liquid	760:765	arg1	LSIMS					800:804	LSIMS	800:804	LSIMS	800:804	The glycosylated peptides were isolated by ultrafiltration, purified by reverse-phase HPLC and further analysed by liquid secondary ion mass spectrometry (LSIMS).
7744025	5	53	theme	glycosylation	1107:1119	arg1	glycosylation					1107:1119	glycosylation	1107:1119	glycosylation	1107:1119	Automated Edman sequencing and LSIMS of proteolytic fragments independently revealed the sites of GalNAc incorporation and confirmed that the threonine residues Thr9 and Thr1b are the preferred sites of glycosylation independent of the enzyme source, while Thr14 remained non-glycosylated even with the enzyme preparation from milk.
7744025	5	53	theme	glycosylation	1107:1119	arg1	sites					1098:1102	the preferred sites	1084:1102	the preferred sites of glycosylation independent of the enzyme source	1084:1152	Automated Edman sequencing and LSIMS of proteolytic fragments independently revealed the sites of GalNAc incorporation and confirmed that the threonine residues Thr9 and Thr1b are the preferred sites of glycosylation independent of the enzyme source, while Thr14 remained non-glycosylated even with the enzyme preparation from milk.
7744025	5	53	theme	glycosylation	1107:1119	arg1	residues					1056:1063	the threonine residues	1042:1063	the threonine residues Thr9 and Thr1b	1042:1078	Automated Edman sequencing and LSIMS of proteolytic fragments independently revealed the sites of GalNAc incorporation and confirmed that the threonine residues Thr9 and Thr1b are the preferred sites of glycosylation independent of the enzyme source, while Thr14 remained non-glycosylated even with the enzyme preparation from milk.
7744025	7	54	dep	studies	1384:1390	arg1	the					1363:1365	the	1363:1365	the	1363:1365	On the basis of kinetic studies a preferred sequence of GalNAc addition to the three acceptor sites has been concluded (Thr9-->Thr1b-->Ser20).
7744025	7	54	dep	studies	1384:1390	arg1	basis					1367:1371	basis	1367:1371	basis	1367:1371	On the basis of kinetic studies a preferred sequence of GalNAc addition to the three acceptor sites has been concluded (Thr9-->Thr1b-->Ser20).
7744025	2	55	dep	line	599:602	arg1	HT29					604:607	HT29	604:607	the colon carcinoma cell line HT29	574:607	TAP25 was glycosylated using the detergent-solubilized UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases from the breast carcinoma cell line T47D, the colon carcinoma cell line HT29 and from human premature skim milk.
7744025	2	56	theme	cell	558:561	arg1	line					599:602	colon carcinoma cell line	578:602	the colon carcinoma cell line HT29	574:607	TAP25 was glycosylated using the detergent-solubilized UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases from the breast carcinoma cell line T47D, the colon carcinoma cell line HT29 and from human premature skim milk.
7744025	2	56	theme	cell	558:561	arg1	line					563:566	breast carcinoma cell line	541:566	the breast carcinoma cell line T47D	537:571	TAP25 was glycosylated using the detergent-solubilized UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases from the breast carcinoma cell line T47D, the colon carcinoma cell line HT29 and from human premature skim milk.
7744025	1	57	dep	T1aAPPAHGVT9S10APDT14RPAPGS20	212:240	arg1	T1bAPPA5b					242:250	T1bAPPA5b	242:250	T1bAPPA5b	242:250	A synthetic peptide [TAP25, (T1aAPPAHGVT9S10APDT14RPAPGS20)T1bAPPA5b] corresponding to one repeat (T1a-S20) and five overlapping amino acids (T1b-A5b) of the MUC1 core protein served as an acceptor substrate for in vitro glycosylation.
7744025	7	58	theme	GalNAc	1416:1421	arg1	addition					1423:1430	GalNAc addition	1416:1430	GalNAc addition	1416:1430	On the basis of kinetic studies a preferred sequence of GalNAc addition to the three acceptor sites has been concluded (Thr9-->Thr1b-->Ser20).
7744025	1	59	theme	acceptor	372:379	arg1	peptide					195:201	A synthetic peptide [TAP25	183:208	A synthetic peptide [TAP25, (T1aAPPAHGVT9S10APDT14RPAPGS20)T1bAPPA5b] corresponding to one repeat (T1a-S20) and five overlapping amino acids (T1b-A5b) of the MUC1 core protein	183:357	A synthetic peptide [TAP25, (T1aAPPAHGVT9S10APDT14RPAPGS20)T1bAPPA5b] corresponding to one repeat (T1a-S20) and five overlapping amino acids (T1b-A5b) of the MUC1 core protein served as an acceptor substrate for in vitro glycosylation.
7744025	1	59	theme	acceptor	372:379	arg1	substrate					381:389	an acceptor substrate	369:389	an acceptor substrate for in vitro glycosylation	369:416	A synthetic peptide [TAP25, (T1aAPPAHGVT9S10APDT14RPAPGS20)T1bAPPA5b] corresponding to one repeat (T1a-S20) and five overlapping amino acids (T1b-A5b) of the MUC1 core protein served as an acceptor substrate for in vitro glycosylation.
7744025	2	60	theme	carcinoma	584:592	arg1	line					599:602	colon carcinoma cell line	578:602	the colon carcinoma cell line HT29	574:607	TAP25 was glycosylated using the detergent-solubilized UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases from the breast carcinoma cell line T47D, the colon carcinoma cell line HT29 and from human premature skim milk.
7744025	2	60	theme	carcinoma	584:592	arg1	line					563:566	breast carcinoma cell line	541:566	the breast carcinoma cell line T47D	537:571	TAP25 was glycosylated using the detergent-solubilized UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases from the breast carcinoma cell line T47D, the colon carcinoma cell line HT29 and from human premature skim milk.
7744025	0	61	theme	carcinoma	166:174	arg1	cells					176:180	mammary carcinoma cells	158:180	mammary carcinoma cells	158:180	Studies on the order and site specificity of GalNAc transfer to MUC1 tandem repeats by UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferase from milk or mammary carcinoma cells.
7744025	5	62	theme	proteolytic	944:954	arg1	fragments					956:964	proteolytic fragments	944:964	proteolytic fragments	944:964	Automated Edman sequencing and LSIMS of proteolytic fragments independently revealed the sites of GalNAc incorporation and confirmed that the threonine residues Thr9 and Thr1b are the preferred sites of glycosylation independent of the enzyme source, while Thr14 remained non-glycosylated even with the enzyme preparation from milk.
7744025	5	63	theme	Automated	904:912	arg1	sequencing					920:929	Automated Edman sequencing	904:929	Automated Edman sequencing	904:929	Automated Edman sequencing and LSIMS of proteolytic fragments independently revealed the sites of GalNAc incorporation and confirmed that the threonine residues Thr9 and Thr1b are the preferred sites of glycosylation independent of the enzyme source, while Thr14 remained non-glycosylated even with the enzyme preparation from milk.
7744025	2	64	theme	polypeptide	485:495	arg1	N-acetylgalactosaminyltransferases					497:530	the detergent-solubilized UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases	448:530	the detergent-solubilized UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases from the breast carcinoma cell line T47D, the colon carcinoma cell line HT29 and from human premature skim milk	448:642	TAP25 was glycosylated using the detergent-solubilized UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases from the breast carcinoma cell line T47D, the colon carcinoma cell line HT29 and from human premature skim milk.
7744025	8	65	theme	PDTRP	1529:1533	arg1	motif					1535:1539	the PDTRP motif	1525:1539	the PDTRP motif of the tandem repeats	1525:1561	Although Thr14 within the PDTRP motif of the tandem repeats remained non-glycosylated, the introduction of GalNAc into adjacent positions significantly decreased the immunoreactivity of antibodies SM-3, HMFG-1 and HMFG-2 defining overlapping epitopes of this motif.
7744025	7	66	theme	kinetic	1376:1382	arg1	studies					1384:1390	kinetic studies	1376:1390	kinetic studies	1376:1390	On the basis of kinetic studies a preferred sequence of GalNAc addition to the three acceptor sites has been concluded (Thr9-->Thr1b-->Ser20).
7744025	0	67	theme	MUC1	64:67	arg1	repeats					76:82	MUC1 tandem repeats	64:82	MUC1 tandem repeats	64:82	Studies on the order and site specificity of GalNAc transfer to MUC1 tandem repeats by UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferase from milk or mammary carcinoma cells.
7744025	8	68	dep	antibodies	1689:1698	arg1	HMFG-2					1717:1722	HMFG-2	1717:1722	HMFG-2	1717:1722	Although Thr14 within the PDTRP motif of the tandem repeats remained non-glycosylated, the introduction of GalNAc into adjacent positions significantly decreased the immunoreactivity of antibodies SM-3, HMFG-1 and HMFG-2 defining overlapping epitopes of this motif.
7744025	8	68	dep	antibodies	1689:1698	arg1	antibodies					1689:1698	antibodies SM-3, HMFG-1 and HMFG-2	1689:1722	antibodies SM-3, HMFG-1 and HMFG-2 defining overlapping epitopes of this motif	1689:1766	Although Thr14 within the PDTRP motif of the tandem repeats remained non-glycosylated, the introduction of GalNAc into adjacent positions significantly decreased the immunoreactivity of antibodies SM-3, HMFG-1 and HMFG-2 defining overlapping epitopes of this motif.
7744025	8	68	dep	antibodies	1689:1698	arg1	HMFG-1					1706:1711	HMFG-1	1706:1711	HMFG-1	1706:1711	Although Thr14 within the PDTRP motif of the tandem repeats remained non-glycosylated, the introduction of GalNAc into adjacent positions significantly decreased the immunoreactivity of antibodies SM-3, HMFG-1 and HMFG-2 defining overlapping epitopes of this motif.
7744025	8	68	dep	antibodies	1689:1698	arg1	SM-3					1700:1703	SM-3	1700:1703	SM-3	1700:1703	Although Thr14 within the PDTRP motif of the tandem repeats remained non-glycosylated, the introduction of GalNAc into adjacent positions significantly decreased the immunoreactivity of antibodies SM-3, HMFG-1 and HMFG-2 defining overlapping epitopes of this motif.
7744025	2	69	theme	UDP-GalNAc	474:483	arg1	N-acetylgalactosaminyltransferases					497:530	the detergent-solubilized UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases	448:530	the detergent-solubilized UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases from the breast carcinoma cell line T47D, the colon carcinoma cell line HT29 and from human premature skim milk	448:642	TAP25 was glycosylated using the detergent-solubilized UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases from the breast carcinoma cell line T47D, the colon carcinoma cell line HT29 and from human premature skim milk.
7744025	0	70	dep	UDP-GalNAc	87:96	arg1	N-acetylgalactosaminyltransferase					111:143	polypeptide N-acetylgalactosaminyltransferase	99:143	UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferase from milk or mammary carcinoma cells	87:180	Studies on the order and site specificity of GalNAc transfer to MUC1 tandem repeats by UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferase from milk or mammary carcinoma cells.
7744025	2	71	theme	breast	541:546	arg1	line					599:602	colon carcinoma cell line	578:602	the colon carcinoma cell line HT29	574:607	TAP25 was glycosylated using the detergent-solubilized UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases from the breast carcinoma cell line T47D, the colon carcinoma cell line HT29 and from human premature skim milk.
7744025	2	71	theme	breast	541:546	arg1	line					563:566	breast carcinoma cell line	541:566	the breast carcinoma cell line T47D	537:571	TAP25 was glycosylated using the detergent-solubilized UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases from the breast carcinoma cell line T47D, the colon carcinoma cell line HT29 and from human premature skim milk.
7744025	8	72	theme	tandem	1548:1553	arg1	repeats					1555:1561	the tandem repeats	1544:1561	the tandem repeats	1544:1561	Although Thr14 within the PDTRP motif of the tandem repeats remained non-glycosylated, the introduction of GalNAc into adjacent positions significantly decreased the immunoreactivity of antibodies SM-3, HMFG-1 and HMFG-2 defining overlapping epitopes of this motif.
7744025	1	73	theme	MUC1	341:344	arg1	protein					351:357	the MUC1 core protein	337:357	the MUC1 core protein	337:357	A synthetic peptide [TAP25, (T1aAPPAHGVT9S10APDT14RPAPGS20)T1bAPPA5b] corresponding to one repeat (T1a-S20) and five overlapping amino acids (T1b-A5b) of the MUC1 core protein served as an acceptor substrate for in vitro glycosylation.
7744025	5	74	theme	incorporation	1009:1021	arg1	sites					993:997	the sites	989:997	the sites of GalNAc incorporation	989:1021	Automated Edman sequencing and LSIMS of proteolytic fragments independently revealed the sites of GalNAc incorporation and confirmed that the threonine residues Thr9 and Thr1b are the preferred sites of glycosylation independent of the enzyme source, while Thr14 remained non-glycosylated even with the enzyme preparation from milk.
7744025	5	74	theme	incorporation	1009:1021	arg1	incorporation					1009:1021	GalNAc incorporation	1002:1021	GalNAc incorporation	1002:1021	Automated Edman sequencing and LSIMS of proteolytic fragments independently revealed the sites of GalNAc incorporation and confirmed that the threonine residues Thr9 and Thr1b are the preferred sites of glycosylation independent of the enzyme source, while Thr14 remained non-glycosylated even with the enzyme preparation from milk.
7744025	1	75	theme	protein	351:357	arg1	T1a-S20					282:288	T1a-S20	282:288	T1a-S20	282:288	A synthetic peptide [TAP25, (T1aAPPAHGVT9S10APDT14RPAPGS20)T1bAPPA5b] corresponding to one repeat (T1a-S20) and five overlapping amino acids (T1b-A5b) of the MUC1 core protein served as an acceptor substrate for in vitro glycosylation.
7744025	1	75	theme	protein	351:357	arg1	acids					318:322	five overlapping amino acids	295:322	five overlapping amino acids (T1b-A5b) of the MUC1 core protein	295:357	A synthetic peptide [TAP25, (T1aAPPAHGVT9S10APDT14RPAPGS20)T1bAPPA5b] corresponding to one repeat (T1a-S20) and five overlapping amino acids (T1b-A5b) of the MUC1 core protein served as an acceptor substrate for in vitro glycosylation.
7744025	1	75	theme	protein	351:357	arg1	T1b-A5b					325:331	T1b-A5b	325:331	T1b-A5b	325:331	A synthetic peptide [TAP25, (T1aAPPAHGVT9S10APDT14RPAPGS20)T1bAPPA5b] corresponding to one repeat (T1a-S20) and five overlapping amino acids (T1b-A5b) of the MUC1 core protein served as an acceptor substrate for in vitro glycosylation.
7744025	1	75	theme	protein	351:357	arg1	repeat					274:279	one repeat	270:279	one repeat (T1a-S20)	270:289	A synthetic peptide [TAP25, (T1aAPPAHGVT9S10APDT14RPAPGS20)T1bAPPA5b] corresponding to one repeat (T1a-S20) and five overlapping amino acids (T1b-A5b) of the MUC1 core protein served as an acceptor substrate for in vitro glycosylation.
7744025	5	76	theme	enzyme	1140:1145	arg1	source					1147:1152	the enzyme source	1136:1152	the enzyme source	1136:1152	Automated Edman sequencing and LSIMS of proteolytic fragments independently revealed the sites of GalNAc incorporation and confirmed that the threonine residues Thr9 and Thr1b are the preferred sites of glycosylation independent of the enzyme source, while Thr14 remained non-glycosylated even with the enzyme preparation from milk.
7744025	3	77	theme	glycosylated	649:660	arg1	peptides					662:669	The glycosylated peptides	645:669	The glycosylated peptides	645:669	The glycosylated peptides were isolated by ultrafiltration, purified by reverse-phase HPLC and further analysed by liquid secondary ion mass spectrometry (LSIMS).
7744025	0	78	theme	site	25:28	arg1	specificity					30:40	site specificity	25:40	site specificity	25:40	Studies on the order and site specificity of GalNAc transfer to MUC1 tandem repeats by UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferase from milk or mammary carcinoma cells.
7744025	9	79	theme	epitope	1876:1882	arg1	conformation					1848:1859	the peptide conformation	1836:1859	the peptide conformation of the binding epitope	1836:1882	It is assumed that glycosylation at Thr9, Thr1b and Ser20 distorts the peptide conformation of the binding epitope.
7744025	8	80	theme	GalNAc	1610:1615	arg1	introduction					1594:1605	the introduction	1590:1605	the introduction of GalNAc into adjacent positions	1590:1639	Although Thr14 within the PDTRP motif of the tandem repeats remained non-glycosylated, the introduction of GalNAc into adjacent positions significantly decreased the immunoreactivity of antibodies SM-3, HMFG-1 and HMFG-2 defining overlapping epitopes of this motif.
7744025	4	81	theme	glycosylation	824:836	arg1	species					838:844	Three different glycosylation species	808:844	Three different glycosylation species	808:844	Three different glycosylation species, mono-, di- and triglycosylated peptides were identified.
7744025	4	81	theme	glycosylation	824:836	arg1	di-					854:856	di-	854:856	di-	854:856	Three different glycosylation species, mono-, di- and triglycosylated peptides were identified.
7744025	4	81	theme	glycosylation	824:836	arg1	peptides					878:885	triglycosylated peptides	862:885	triglycosylated peptides	862:885	Three different glycosylation species, mono-, di- and triglycosylated peptides were identified.
7744025	4	81	theme	glycosylation	824:836	arg1	mono-					847:851	mono-	847:851	mono-	847:851	Three different glycosylation species, mono-, di- and triglycosylated peptides were identified.
7744025	1	82	theme	overlapping	300:310	arg1	T1b-A5b					325:331	T1b-A5b	325:331	T1b-A5b	325:331	A synthetic peptide [TAP25, (T1aAPPAHGVT9S10APDT14RPAPGS20)T1bAPPA5b] corresponding to one repeat (T1a-S20) and five overlapping amino acids (T1b-A5b) of the MUC1 core protein served as an acceptor substrate for in vitro glycosylation.
7744025	1	82	theme	overlapping	300:310	arg1	acids					318:322	five overlapping amino acids	295:322	five overlapping amino acids (T1b-A5b) of the MUC1 core protein	295:357	A synthetic peptide [TAP25, (T1aAPPAHGVT9S10APDT14RPAPGS20)T1bAPPA5b] corresponding to one repeat (T1a-S20) and five overlapping amino acids (T1b-A5b) of the MUC1 core protein served as an acceptor substrate for in vitro glycosylation.
7744025	9	83	from	Ser20	1821:1825	arg1	glycosylation					1788:1800	glycosylation	1788:1800	glycosylation at Thr9, Thr1b and Ser20	1788:1825	It is assumed that glycosylation at Thr9, Thr1b and Ser20 distorts the peptide conformation of the binding epitope.
7744025	2	84	gly	glycosylated	429:440	arg1	TAP25					419:423	TAP25	419:423	TAP25	419:423	TAP25 was glycosylated using the detergent-solubilized UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases from the breast carcinoma cell line T47D, the colon carcinoma cell line HT29 and from human premature skim milk.
7744025	5	85	theme	source	1147:1152	arg1	independent					1121:1131	independent	1121:1131	independent	1121:1131	Automated Edman sequencing and LSIMS of proteolytic fragments independently revealed the sites of GalNAc incorporation and confirmed that the threonine residues Thr9 and Thr1b are the preferred sites of glycosylation independent of the enzyme source, while Thr14 remained non-glycosylated even with the enzyme preparation from milk.
7744025	2	86	from	milk	639:642	arg1	N-acetylgalactosaminyltransferases					497:530	the detergent-solubilized UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases	448:530	the detergent-solubilized UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases from the breast carcinoma cell line T47D, the colon carcinoma cell line HT29 and from human premature skim milk	448:642	TAP25 was glycosylated using the detergent-solubilized UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases from the breast carcinoma cell line T47D, the colon carcinoma cell line HT29 and from human premature skim milk.
7744025	5	87	theme	enzyme	1207:1212	arg1	preparation					1214:1224	the enzyme preparation	1203:1224	the enzyme preparation from milk	1203:1234	Automated Edman sequencing and LSIMS of proteolytic fragments independently revealed the sites of GalNAc incorporation and confirmed that the threonine residues Thr9 and Thr1b are the preferred sites of glycosylation independent of the enzyme source, while Thr14 remained non-glycosylated even with the enzyme preparation from milk.
7744025	9	88	from	Thr1b	1811:1815	arg1	glycosylation					1788:1800	glycosylation	1788:1800	glycosylation at Thr9, Thr1b and Ser20	1788:1825	It is assumed that glycosylation at Thr9, Thr1b and Ser20 distorts the peptide conformation of the binding epitope.
7744025	0	89	dep	order	15:19	arg1	the					11:13	the	11:13	the	11:13	Studies on the order and site specificity of GalNAc transfer to MUC1 tandem repeats by UDP-GalNAc: polypeptide N-acetylgalactosaminyltransferase from milk or mammary carcinoma cells.
7744025	2	90	from	line	563:566	arg1	N-acetylgalactosaminyltransferases					497:530	the detergent-solubilized UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases	448:530	the detergent-solubilized UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases from the breast carcinoma cell line T47D, the colon carcinoma cell line HT29 and from human premature skim milk	448:642	TAP25 was glycosylated using the detergent-solubilized UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases from the breast carcinoma cell line T47D, the colon carcinoma cell line HT29 and from human premature skim milk.
7744025	9	91	from	Thr9	1805:1808	arg1	glycosylation					1788:1800	glycosylation	1788:1800	glycosylation at Thr9, Thr1b and Ser20	1788:1825	It is assumed that glycosylation at Thr9, Thr1b and Ser20 distorts the peptide conformation of the binding epitope.
7744025	8	92	theme	overlapping	1733:1743	arg1	epitopes					1745:1752	overlapping epitopes	1733:1752	overlapping epitopes of this motif	1733:1766	Although Thr14 within the PDTRP motif of the tandem repeats remained non-glycosylated, the introduction of GalNAc into adjacent positions significantly decreased the immunoreactivity of antibodies SM-3, HMFG-1 and HMFG-2 defining overlapping epitopes of this motif.
7925474	4	0	theme	epidermal-growth-factor	474:496	arg1	motifs					498:503	six well conserved epidermal-growth-factor motifs	455:503	six well conserved epidermal-growth-factor motifs	455:503	FA1 has six well conserved epidermal-growth-factor motifs and contains up to ten O-glycosylation and N-glycosylation sites, six of which are differentially glycosylated.
7925474	7	1	theme	close	1081:1085	arg1	contact					1087:1093	close contact	1081:1093	close contact to the vascular structure	1081:1119	Immunohistochemical analysis demonstrated the presence of FA1 in 10 out of 14 lung tumors containing neuroendocrine elements, and in the placental villi where FA1 was exclusively seen in stromal cells in close contact to the vascular structure.
7925474	6	2	theme	99	707:708	arg1	%					709:709	%	709:709	%	709:709	musculus dlk and human dlk revealed 86% and 99% identity, respectively, to a 259-amino-acid residue overlap, and this high similarity extends with minor corrections to the human adrenal-specific mRNA, pG2 as well.
7925474	2	3	theme	second-trimester	324:339	arg1	fluid					356:360	second-trimester human amniotic fluid	324:360	second-trimester human amniotic fluid	324:360	The present paper describes the primary structure, glycosylation and tissue localization of fetal antigen 1 (FA1) isolated from second-trimester human amniotic fluid.
7925474	4	4	dep	ten	524:526	arg1	to					521:522	to	521:522	to	521:522	FA1 has six well conserved epidermal-growth-factor motifs and contains up to ten O-glycosylation and N-glycosylation sites, six of which are differentially glycosylated.
7925474	5	5	theme	Mus	658:660	arg1	sequences					645:653	the translated sequences	630:653	the translated sequences of Mus	630:660	Alignment to the translated sequences of Mus.
7925474	8	6	theme	secretory	1184:1192	arg1	granules					1194:1201	the insulin secretory granules	1172:1201	the insulin secretory granules of the beta cells within the islets of Langerhans	1172:1251	In the pancreas, FA1 co-localized with insulin in the insulin secretory granules of the beta cells within the islets of Langerhans.
7925474	9	7	theme	dlk	1480:1482	arg1	product					1463:1469	the post-translationally modified gene product	1424:1469	the post-translationally modified gene product of human dlk which, in turn, is identical to human adrenal-specific mRNA pG2	1424:1546	Our findings suggest that FA1 is synthesized as a membrane anchored protein and released into the circulation after enzymic cleavage, and that circulating FA1 represents the post-translationally modified gene product of human dlk which, in turn, is identical to human adrenal-specific mRNA pG2.
7925474	9	7	theme	dlk	1480:1482	arg1	FA1					1280:1282	FA1	1280:1282	FA1	1280:1282	Our findings suggest that FA1 is synthesized as a membrane anchored protein and released into the circulation after enzymic cleavage, and that circulating FA1 represents the post-translationally modified gene product of human dlk which, in turn, is identical to human adrenal-specific mRNA pG2.
7925474	9	7	theme	dlk	1480:1482	arg1	identical					1503:1511	identical	1503:1511	identical	1503:1511	Our findings suggest that FA1 is synthesized as a membrane anchored protein and released into the circulation after enzymic cleavage, and that circulating FA1 represents the post-translationally modified gene product of human dlk which, in turn, is identical to human adrenal-specific mRNA pG2.
7925474	9	7	theme	dlk	1480:1482	arg1	protein					1322:1328	a membrane anchored protein	1302:1328	a membrane anchored protein	1302:1328	Our findings suggest that FA1 is synthesized as a membrane anchored protein and released into the circulation after enzymic cleavage, and that circulating FA1 represents the post-translationally modified gene product of human dlk which, in turn, is identical to human adrenal-specific mRNA pG2.
7925474	4	8	gly	glycosylated	603:614	arg1	six					571:573	six	571:573	six	571:573	FA1 has six well conserved epidermal-growth-factor motifs and contains up to ten O-glycosylation and N-glycosylation sites, six of which are differentially glycosylated.
7925474	4	8	gly	glycosylated	603:614	arg1	O-glycosylation					528:542	up to ten O-glycosylation and N-glycosylation sites	518:568	O-glycosylation	528:542	FA1 has six well conserved epidermal-growth-factor motifs and contains up to ten O-glycosylation and N-glycosylation sites, six of which are differentially glycosylated.
7925474	4	8	gly	glycosylated	603:614	arg1	sites					564:568	up to ten O-glycosylation and N-glycosylation sites	518:568	sites	564:568	FA1 has six well conserved epidermal-growth-factor motifs and contains up to ten O-glycosylation and N-glycosylation sites, six of which are differentially glycosylated.
7925474	9	9	from	turn	1494:1497	arg1	product					1463:1469	the post-translationally modified gene product	1424:1469	the post-translationally modified gene product of human dlk which, in turn, is identical to human adrenal-specific mRNA pG2	1424:1546	Our findings suggest that FA1 is synthesized as a membrane anchored protein and released into the circulation after enzymic cleavage, and that circulating FA1 represents the post-translationally modified gene product of human dlk which, in turn, is identical to human adrenal-specific mRNA pG2.
7925474	9	9	from	turn	1494:1497	arg1	identical					1503:1511	identical	1503:1511	identical	1503:1511	Our findings suggest that FA1 is synthesized as a membrane anchored protein and released into the circulation after enzymic cleavage, and that circulating FA1 represents the post-translationally modified gene product of human dlk which, in turn, is identical to human adrenal-specific mRNA pG2.
7925474	9	10	theme	enzymic	1370:1376	arg1	cleavage					1378:1385	enzymic cleavage	1370:1385	enzymic cleavage	1370:1385	Our findings suggest that FA1 is synthesized as a membrane anchored protein and released into the circulation after enzymic cleavage, and that circulating FA1 represents the post-translationally modified gene product of human dlk which, in turn, is identical to human adrenal-specific mRNA pG2.
7925474	7	11	contain	containing	967:976	arg1	tumors					960:965	10 out of 14 lung tumors	942:965	10 out of 14 lung tumors containing neuroendocrine elements	942:1000	Immunohistochemical analysis demonstrated the presence of FA1 in 10 out of 14 lung tumors containing neuroendocrine elements, and in the placental villi where FA1 was exclusively seen in stromal cells in close contact to the vascular structure.
7925474	7	11	contain	containing	967:976	arg2	elements					993:1000	neuroendocrine elements	978:1000	neuroendocrine elements	978:1000	Immunohistochemical analysis demonstrated the presence of FA1 in 10 out of 14 lung tumors containing neuroendocrine elements, and in the placental villi where FA1 was exclusively seen in stromal cells in close contact to the vascular structure.
7925474	9	12	dep	anchored	1313:1320	arg1	membrane					1304:1311	membrane	1304:1311	membrane	1304:1311	Our findings suggest that FA1 is synthesized as a membrane anchored protein and released into the circulation after enzymic cleavage, and that circulating FA1 represents the post-translationally modified gene product of human dlk which, in turn, is identical to human adrenal-specific mRNA pG2.
7925474	7	13	theme	FA1	935:937	arg1	presence					923:930	the presence	919:930	the presence of FA1 in 10 out of 14 lung tumors containing neuroendocrine elements, and in the placental villi where FA1 was exclusively seen in stromal cells in close contact to the vascular structure	919:1119	Immunohistochemical analysis demonstrated the presence of FA1 in 10 out of 14 lung tumors containing neuroendocrine elements, and in the placental villi where FA1 was exclusively seen in stromal cells in close contact to the vascular structure.
7925474	2	14	theme	tissue	265:270	arg1	localization					272:283	tissue localization	265:283	tissue localization	265:283	The present paper describes the primary structure, glycosylation and tissue localization of fetal antigen 1 (FA1) isolated from second-trimester human amniotic fluid.
7925474	8	15	theme	Langerhans	1242:1251	arg1	islets					1232:1237	the islets	1228:1237	the islets of Langerhans	1228:1251	In the pancreas, FA1 co-localized with insulin in the insulin secretory granules of the beta cells within the islets of Langerhans.
7925474	2	16	gly	glycosylation	247:259	arg1	antigen					294:300	fetal antigen 1	288:302	fetal antigen 1 (FA1) isolated from second-trimester human amniotic fluid	288:360	The present paper describes the primary structure, glycosylation and tissue localization of fetal antigen 1 (FA1) isolated from second-trimester human amniotic fluid.
7925474	2	16	gly	glycosylation	247:259	arg1	FA1					305:307	FA1	305:307	FA1	305:307	The present paper describes the primary structure, glycosylation and tissue localization of fetal antigen 1 (FA1) isolated from second-trimester human amniotic fluid.
7925474	2	17	attach	isolated	310:317	arg1	fluid					356:360	second-trimester human amniotic fluid	324:360	second-trimester human amniotic fluid	324:360	The present paper describes the primary structure, glycosylation and tissue localization of fetal antigen 1 (FA1) isolated from second-trimester human amniotic fluid.
7925474	2	17	attach	isolated	310:317	arg2	antigen					294:300	fetal antigen 1	288:302	fetal antigen 1 (FA1) isolated from second-trimester human amniotic fluid	288:360	The present paper describes the primary structure, glycosylation and tissue localization of fetal antigen 1 (FA1) isolated from second-trimester human amniotic fluid.
7925474	2	17	attach	isolated	310:317	arg2	FA1					305:307	FA1	305:307	FA1	305:307	The present paper describes the primary structure, glycosylation and tissue localization of fetal antigen 1 (FA1) isolated from second-trimester human amniotic fluid.
7925474	3	18	theme	225-262	418:424	arg1	residues					437:444	225-262 amino acid residues	418:444	225-262 amino acid residues	418:444	FA1 is a single-chained, heterogeneous glycoprotein of 225-262 amino acid residues.
7925474	5	19	dep	Alignment	617:625	arg1	sequences					645:653	the translated sequences	630:653	the translated sequences of Mus	630:660	Alignment to the translated sequences of Mus.
7925474	4	20	theme	conserved	464:472	arg1	motifs					498:503	six well conserved epidermal-growth-factor motifs	455:503	six well conserved epidermal-growth-factor motifs	455:503	FA1 has six well conserved epidermal-growth-factor motifs and contains up to ten O-glycosylation and N-glycosylation sites, six of which are differentially glycosylated.
7925474	3	21	dep	single-chained	372:385	arg1	heterogeneous					388:400	heterogeneous	388:400	heterogeneous	388:400	FA1 is a single-chained, heterogeneous glycoprotein of 225-262 amino acid residues.
7925474	9	22	theme	human	1474:1478	arg1	dlk					1480:1482	human dlk	1474:1482	human dlk	1474:1482	Our findings suggest that FA1 is synthesized as a membrane anchored protein and released into the circulation after enzymic cleavage, and that circulating FA1 represents the post-translationally modified gene product of human dlk which, in turn, is identical to human adrenal-specific mRNA pG2.
7925474	1	23	theme	novel	46:50	arg1	protein					99:105	A novel circulating human epidermal-growth-factor-like protein	44:105	A novel circulating human epidermal-growth-factor-like protein	44:105	A novel circulating human epidermal-growth-factor-like protein expressed in neuroendocrine tumors and its relation to the gene products of dlk and pG2.
7925474	1	24	theme	gene	166:169	arg1	products					171:178	the gene products	162:178	the gene products of dlk and pG2	162:193	A novel circulating human epidermal-growth-factor-like protein expressed in neuroendocrine tumors and its relation to the gene products of dlk and pG2.
7925474	5	25	theme	translated	634:643	arg1	sequences					645:653	the translated sequences	630:653	the translated sequences of Mus	630:660	Alignment to the translated sequences of Mus.
7925474	6	26	theme	overlap	763:769	arg1	residue					755:761	a 259-amino-acid residue	738:761	a 259-amino-acid residue overlap	738:769	musculus dlk and human dlk revealed 86% and 99% identity, respectively, to a 259-amino-acid residue overlap, and this high similarity extends with minor corrections to the human adrenal-specific mRNA, pG2 as well.
7925474	1	27	theme	circulating	52:62	arg1	protein					99:105	A novel circulating human epidermal-growth-factor-like protein	44:105	A novel circulating human epidermal-growth-factor-like protein	44:105	A novel circulating human epidermal-growth-factor-like protein expressed in neuroendocrine tumors and its relation to the gene products of dlk and pG2.
7925474	0	28	theme	Protein	0:6	arg1	structure					8:16	Protein structure	0:16	Protein structure of fetal antigen 1 (FA1).	0:42	Protein structure of fetal antigen 1 (FA1).
7925474	4	29	theme	N-glycosylation	548:562	arg1	sites					564:568	up to ten O-glycosylation and N-glycosylation sites	518:568	sites	564:568	FA1 has six well conserved epidermal-growth-factor motifs and contains up to ten O-glycosylation and N-glycosylation sites, six of which are differentially glycosylated.
7925474	7	30	attach	presence	923:930	arg1	tumors					960:965	10 out of 14 lung tumors	942:965	10 out of 14 lung tumors containing neuroendocrine elements	942:1000	Immunohistochemical analysis demonstrated the presence of FA1 in 10 out of 14 lung tumors containing neuroendocrine elements, and in the placental villi where FA1 was exclusively seen in stromal cells in close contact to the vascular structure.
7925474	7	30	attach	presence	923:930	arg2	FA1					935:937	FA1	935:937	FA1	935:937	Immunohistochemical analysis demonstrated the presence of FA1 in 10 out of 14 lung tumors containing neuroendocrine elements, and in the placental villi where FA1 was exclusively seen in stromal cells in close contact to the vascular structure.
7925474	7	30	attach	presence	923:930	arg1	villi					1024:1028	the placental villi	1010:1028	the placental villi where FA1 was exclusively seen in stromal cells in close contact to the vascular structure	1010:1119	Immunohistochemical analysis demonstrated the presence of FA1 in 10 out of 14 lung tumors containing neuroendocrine elements, and in the placental villi where FA1 was exclusively seen in stromal cells in close contact to the vascular structure.
7925474	9	31	theme	anchored	1313:1320	arg1	product					1463:1469	the post-translationally modified gene product	1424:1469	the post-translationally modified gene product of human dlk which, in turn, is identical to human adrenal-specific mRNA pG2	1424:1546	Our findings suggest that FA1 is synthesized as a membrane anchored protein and released into the circulation after enzymic cleavage, and that circulating FA1 represents the post-translationally modified gene product of human dlk which, in turn, is identical to human adrenal-specific mRNA pG2.
7925474	9	31	theme	anchored	1313:1320	arg1	FA1					1280:1282	FA1	1280:1282	FA1	1280:1282	Our findings suggest that FA1 is synthesized as a membrane anchored protein and released into the circulation after enzymic cleavage, and that circulating FA1 represents the post-translationally modified gene product of human dlk which, in turn, is identical to human adrenal-specific mRNA pG2.
7925474	9	31	theme	anchored	1313:1320	arg1	protein					1322:1328	a membrane anchored protein	1302:1328	a membrane anchored protein	1302:1328	Our findings suggest that FA1 is synthesized as a membrane anchored protein and released into the circulation after enzymic cleavage, and that circulating FA1 represents the post-translationally modified gene product of human dlk which, in turn, is identical to human adrenal-specific mRNA pG2.
7925474	1	32	theme	human	64:68	arg1	protein					99:105	A novel circulating human epidermal-growth-factor-like protein	44:105	A novel circulating human epidermal-growth-factor-like protein	44:105	A novel circulating human epidermal-growth-factor-like protein expressed in neuroendocrine tumors and its relation to the gene products of dlk and pG2.
7925474	6	33	theme	human	835:839	arg1	pG2					864:866	pG2	864:866	pG2	864:866	musculus dlk and human dlk revealed 86% and 99% identity, respectively, to a 259-amino-acid residue overlap, and this high similarity extends with minor corrections to the human adrenal-specific mRNA, pG2 as well.
7925474	6	33	theme	human	835:839	arg1	mRNA					858:861	the human adrenal-specific mRNA	831:861	the human adrenal-specific mRNA	831:861	musculus dlk and human dlk revealed 86% and 99% identity, respectively, to a 259-amino-acid residue overlap, and this high similarity extends with minor corrections to the human adrenal-specific mRNA, pG2 as well.
7925474	0	34	theme	fetal	21:25	arg1	antigen					27:33	fetal antigen 1	21:35	fetal antigen 1 (FA1)	21:41	Protein structure of fetal antigen 1 (FA1).
7925474	0	34	theme	fetal	21:25	arg1	FA1					38:40	FA1	38:40	FA1	38:40	Protein structure of fetal antigen 1 (FA1).
7925474	6	35	theme	259-amino-acid	740:753	arg1	residue					755:761	a 259-amino-acid residue	738:761	a 259-amino-acid residue overlap	738:769	musculus dlk and human dlk revealed 86% and 99% identity, respectively, to a 259-amino-acid residue overlap, and this high similarity extends with minor corrections to the human adrenal-specific mRNA, pG2 as well.
7925474	2	36	theme	fetal	288:292	arg1	antigen					294:300	fetal antigen 1	288:302	fetal antigen 1 (FA1) isolated from second-trimester human amniotic fluid	288:360	The present paper describes the primary structure, glycosylation and tissue localization of fetal antigen 1 (FA1) isolated from second-trimester human amniotic fluid.
7925474	2	36	theme	fetal	288:292	arg1	FA1					305:307	FA1	305:307	FA1	305:307	The present paper describes the primary structure, glycosylation and tissue localization of fetal antigen 1 (FA1) isolated from second-trimester human amniotic fluid.
7925474	6	37	theme	human	680:684	arg1	dlk					686:688	human dlk	680:688	human dlk	680:688	musculus dlk and human dlk revealed 86% and 99% identity, respectively, to a 259-amino-acid residue overlap, and this high similarity extends with minor corrections to the human adrenal-specific mRNA, pG2 as well.
7925474	1	38	theme	dlk	183:185	arg1	products					171:178	the gene products	162:178	the gene products of dlk and pG2	162:193	A novel circulating human epidermal-growth-factor-like protein expressed in neuroendocrine tumors and its relation to the gene products of dlk and pG2.
7925474	2	39	theme	antigen	294:300	arg1	glycosylation					247:259	glycosylation	247:259	glycosylation	247:259	The present paper describes the primary structure, glycosylation and tissue localization of fetal antigen 1 (FA1) isolated from second-trimester human amniotic fluid.
7925474	2	39	theme	antigen	294:300	arg1	localization					272:283	tissue localization	265:283	tissue localization	265:283	The present paper describes the primary structure, glycosylation and tissue localization of fetal antigen 1 (FA1) isolated from second-trimester human amniotic fluid.
7925474	2	39	theme	antigen	294:300	arg1	structure					236:244	the primary structure	224:244	the primary structure	224:244	The present paper describes the primary structure, glycosylation and tissue localization of fetal antigen 1 (FA1) isolated from second-trimester human amniotic fluid.
7925474	6	40	theme	adrenal-specific	841:856	arg1	pG2					864:866	pG2	864:866	pG2	864:866	musculus dlk and human dlk revealed 86% and 99% identity, respectively, to a 259-amino-acid residue overlap, and this high similarity extends with minor corrections to the human adrenal-specific mRNA, pG2 as well.
7925474	6	40	theme	adrenal-specific	841:856	arg1	mRNA					858:861	the human adrenal-specific mRNA	831:861	the human adrenal-specific mRNA	831:861	musculus dlk and human dlk revealed 86% and 99% identity, respectively, to a 259-amino-acid residue overlap, and this high similarity extends with minor corrections to the human adrenal-specific mRNA, pG2 as well.
7925474	9	41	theme	adrenal-specific	1522:1537	arg1	pG2					1544:1546	human adrenal-specific mRNA pG2	1516:1546	human adrenal-specific mRNA pG2	1516:1546	Our findings suggest that FA1 is synthesized as a membrane anchored protein and released into the circulation after enzymic cleavage, and that circulating FA1 represents the post-translationally modified gene product of human dlk which, in turn, is identical to human adrenal-specific mRNA pG2.
7925474	7	42	from	presence	923:930	arg1	tumors					960:965	10 out of 14 lung tumors	942:965	10 out of 14 lung tumors containing neuroendocrine elements	942:1000	Immunohistochemical analysis demonstrated the presence of FA1 in 10 out of 14 lung tumors containing neuroendocrine elements, and in the placental villi where FA1 was exclusively seen in stromal cells in close contact to the vascular structure.
7925474	7	42	from	presence	923:930	arg1	villi					1024:1028	the placental villi	1010:1028	the placental villi where FA1 was exclusively seen in stromal cells in close contact to the vascular structure	1010:1119	Immunohistochemical analysis demonstrated the presence of FA1 in 10 out of 14 lung tumors containing neuroendocrine elements, and in the placental villi where FA1 was exclusively seen in stromal cells in close contact to the vascular structure.
7925474	8	43	theme	beta	1210:1213	arg1	cells					1215:1219	the beta cells	1206:1219	the beta cells within the islets of Langerhans	1206:1251	In the pancreas, FA1 co-localized with insulin in the insulin secretory granules of the beta cells within the islets of Langerhans.
7925474	7	44	theme	vascular	1102:1109	arg1	structure					1111:1119	the vascular structure	1098:1119	the vascular structure	1098:1119	Immunohistochemical analysis demonstrated the presence of FA1 in 10 out of 14 lung tumors containing neuroendocrine elements, and in the placental villi where FA1 was exclusively seen in stromal cells in close contact to the vascular structure.
7925474	4	45	theme	sites	564:568	arg1	six					571:573	six	571:573	six	571:573	FA1 has six well conserved epidermal-growth-factor motifs and contains up to ten O-glycosylation and N-glycosylation sites, six of which are differentially glycosylated.
7925474	4	45	theme	sites	564:568	arg1	O-glycosylation					528:542	up to ten O-glycosylation and N-glycosylation sites	518:568	O-glycosylation	528:542	FA1 has six well conserved epidermal-growth-factor motifs and contains up to ten O-glycosylation and N-glycosylation sites, six of which are differentially glycosylated.
7925474	4	45	theme	sites	564:568	arg1	sites					564:568	up to ten O-glycosylation and N-glycosylation sites	518:568	sites	564:568	FA1 has six well conserved epidermal-growth-factor motifs and contains up to ten O-glycosylation and N-glycosylation sites, six of which are differentially glycosylated.
7925474	9	46	theme	human	1516:1520	arg1	pG2					1544:1546	human adrenal-specific mRNA pG2	1516:1546	human adrenal-specific mRNA pG2	1516:1546	Our findings suggest that FA1 is synthesized as a membrane anchored protein and released into the circulation after enzymic cleavage, and that circulating FA1 represents the post-translationally modified gene product of human dlk which, in turn, is identical to human adrenal-specific mRNA pG2.
7925474	3	47	theme	acid	432:435	arg1	residues					437:444	225-262 amino acid residues	418:444	225-262 amino acid residues	418:444	FA1 is a single-chained, heterogeneous glycoprotein of 225-262 amino acid residues.
7925474	9	48	theme	mRNA	1539:1542	arg1	pG2					1544:1546	human adrenal-specific mRNA pG2	1516:1546	human adrenal-specific mRNA pG2	1516:1546	Our findings suggest that FA1 is synthesized as a membrane anchored protein and released into the circulation after enzymic cleavage, and that circulating FA1 represents the post-translationally modified gene product of human dlk which, in turn, is identical to human adrenal-specific mRNA pG2.
7925474	9	49	theme	circulating	1397:1407	arg1	FA1					1409:1411	circulating FA1	1397:1411	circulating FA1	1397:1411	Our findings suggest that FA1 is synthesized as a membrane anchored protein and released into the circulation after enzymic cleavage, and that circulating FA1 represents the post-translationally modified gene product of human dlk which, in turn, is identical to human adrenal-specific mRNA pG2.
7925474	1	50	theme	pG2	191:193	arg1	products					171:178	the gene products	162:178	the gene products of dlk and pG2	162:193	A novel circulating human epidermal-growth-factor-like protein expressed in neuroendocrine tumors and its relation to the gene products of dlk and pG2.
7925474	0	51	theme	antigen	27:33	arg1	structure					8:16	Protein structure	0:16	Protein structure of fetal antigen 1 (FA1).	0:42	Protein structure of fetal antigen 1 (FA1).
7925474	7	52	from	cells	1072:1076	arg1	contact					1087:1093	close contact	1081:1093	close contact to the vascular structure	1081:1119	Immunohistochemical analysis demonstrated the presence of FA1 in 10 out of 14 lung tumors containing neuroendocrine elements, and in the placental villi where FA1 was exclusively seen in stromal cells in close contact to the vascular structure.
7925474	3	53	theme	residues	437:444	arg1	FA1					363:365	FA1	363:365	FA1	363:365	FA1 is a single-chained, heterogeneous glycoprotein of 225-262 amino acid residues.
7925474	3	53	theme	residues	437:444	arg1	glycoprotein					402:413	a single-chained, heterogeneous glycoprotein	370:413	a single-chained, heterogeneous glycoprotein of 225-262 amino acid residues	370:444	FA1 is a single-chained, heterogeneous glycoprotein of 225-262 amino acid residues.
7925474	8	54	theme	insulin	1176:1182	arg1	granules					1194:1201	the insulin secretory granules	1172:1201	the insulin secretory granules of the beta cells within the islets of Langerhans	1172:1251	In the pancreas, FA1 co-localized with insulin in the insulin secretory granules of the beta cells within the islets of Langerhans.
7925474	2	55	theme	present	200:206	arg1	paper					208:212	The present paper	196:212	The present paper	196:212	The present paper describes the primary structure, glycosylation and tissue localization of fetal antigen 1 (FA1) isolated from second-trimester human amniotic fluid.
7925474	4	56	gly	N-glycosylation	548:562	arg2	sites					564:568	up to ten O-glycosylation and N-glycosylation sites	518:568	sites	564:568	FA1 has six well conserved epidermal-growth-factor motifs and contains up to ten O-glycosylation and N-glycosylation sites, six of which are differentially glycosylated.
7925474	9	57	theme	modified	1449:1456	arg1	product					1463:1469	the post-translationally modified gene product	1424:1469	the post-translationally modified gene product of human dlk which, in turn, is identical to human adrenal-specific mRNA pG2	1424:1546	Our findings suggest that FA1 is synthesized as a membrane anchored protein and released into the circulation after enzymic cleavage, and that circulating FA1 represents the post-translationally modified gene product of human dlk which, in turn, is identical to human adrenal-specific mRNA pG2.
7925474	9	57	theme	modified	1449:1456	arg1	FA1					1280:1282	FA1	1280:1282	FA1	1280:1282	Our findings suggest that FA1 is synthesized as a membrane anchored protein and released into the circulation after enzymic cleavage, and that circulating FA1 represents the post-translationally modified gene product of human dlk which, in turn, is identical to human adrenal-specific mRNA pG2.
7925474	9	57	theme	modified	1449:1456	arg1	identical					1503:1511	identical	1503:1511	identical	1503:1511	Our findings suggest that FA1 is synthesized as a membrane anchored protein and released into the circulation after enzymic cleavage, and that circulating FA1 represents the post-translationally modified gene product of human dlk which, in turn, is identical to human adrenal-specific mRNA pG2.
7925474	9	57	theme	modified	1449:1456	arg1	protein					1322:1328	a membrane anchored protein	1302:1328	a membrane anchored protein	1302:1328	Our findings suggest that FA1 is synthesized as a membrane anchored protein and released into the circulation after enzymic cleavage, and that circulating FA1 represents the post-translationally modified gene product of human dlk which, in turn, is identical to human adrenal-specific mRNA pG2.
7925474	3	58	theme	single-chained	372:385	arg1	FA1					363:365	FA1	363:365	FA1	363:365	FA1 is a single-chained, heterogeneous glycoprotein of 225-262 amino acid residues.
7925474	3	58	theme	single-chained	372:385	arg1	glycoprotein					402:413	a single-chained, heterogeneous glycoprotein	370:413	a single-chained, heterogeneous glycoprotein of 225-262 amino acid residues	370:444	FA1 is a single-chained, heterogeneous glycoprotein of 225-262 amino acid residues.
7925474	4	59	theme	O-glycosylation	528:542	arg1	six					571:573	six	571:573	six	571:573	FA1 has six well conserved epidermal-growth-factor motifs and contains up to ten O-glycosylation and N-glycosylation sites, six of which are differentially glycosylated.
7925474	4	59	theme	O-glycosylation	528:542	arg1	O-glycosylation					528:542	up to ten O-glycosylation and N-glycosylation sites	518:568	O-glycosylation	528:542	FA1 has six well conserved epidermal-growth-factor motifs and contains up to ten O-glycosylation and N-glycosylation sites, six of which are differentially glycosylated.
7925474	4	59	theme	O-glycosylation	528:542	arg1	sites					564:568	up to ten O-glycosylation and N-glycosylation sites	518:568	sites	564:568	FA1 has six well conserved epidermal-growth-factor motifs and contains up to ten O-glycosylation and N-glycosylation sites, six of which are differentially glycosylated.
7925474	7	60	theme	placental	1014:1022	arg1	villi					1024:1028	the placental villi	1010:1028	the placental villi where FA1 was exclusively seen in stromal cells in close contact to the vascular structure	1010:1119	Immunohistochemical analysis demonstrated the presence of FA1 in 10 out of 14 lung tumors containing neuroendocrine elements, and in the placental villi where FA1 was exclusively seen in stromal cells in close contact to the vascular structure.
7925474	7	61	theme	stromal	1064:1070	arg1	cells					1072:1076	stromal cells	1064:1076	stromal cells in close contact to the vascular structure	1064:1119	Immunohistochemical analysis demonstrated the presence of FA1 in 10 out of 14 lung tumors containing neuroendocrine elements, and in the placental villi where FA1 was exclusively seen in stromal cells in close contact to the vascular structure.
7925474	9	62	theme	gene	1458:1461	arg1	product					1463:1469	the post-translationally modified gene product	1424:1469	the post-translationally modified gene product of human dlk which, in turn, is identical to human adrenal-specific mRNA pG2	1424:1546	Our findings suggest that FA1 is synthesized as a membrane anchored protein and released into the circulation after enzymic cleavage, and that circulating FA1 represents the post-translationally modified gene product of human dlk which, in turn, is identical to human adrenal-specific mRNA pG2.
7925474	9	62	theme	gene	1458:1461	arg1	FA1					1280:1282	FA1	1280:1282	FA1	1280:1282	Our findings suggest that FA1 is synthesized as a membrane anchored protein and released into the circulation after enzymic cleavage, and that circulating FA1 represents the post-translationally modified gene product of human dlk which, in turn, is identical to human adrenal-specific mRNA pG2.
7925474	9	62	theme	gene	1458:1461	arg1	identical					1503:1511	identical	1503:1511	identical	1503:1511	Our findings suggest that FA1 is synthesized as a membrane anchored protein and released into the circulation after enzymic cleavage, and that circulating FA1 represents the post-translationally modified gene product of human dlk which, in turn, is identical to human adrenal-specific mRNA pG2.
7925474	9	62	theme	gene	1458:1461	arg1	protein					1322:1328	a membrane anchored protein	1302:1328	a membrane anchored protein	1302:1328	Our findings suggest that FA1 is synthesized as a membrane anchored protein and released into the circulation after enzymic cleavage, and that circulating FA1 represents the post-translationally modified gene product of human dlk which, in turn, is identical to human adrenal-specific mRNA pG2.
7925474	6	63	theme	musculus	663:670	arg1	dlk					672:674	musculus dlk	663:674	musculus dlk	663:674	musculus dlk and human dlk revealed 86% and 99% identity, respectively, to a 259-amino-acid residue overlap, and this high similarity extends with minor corrections to the human adrenal-specific mRNA, pG2 as well.
7925474	6	64	theme	minor	810:814	arg1	corrections					816:826	minor corrections	810:826	minor corrections to the human adrenal-specific mRNA, pG2	810:866	musculus dlk and human dlk revealed 86% and 99% identity, respectively, to a 259-amino-acid residue overlap, and this high similarity extends with minor corrections to the human adrenal-specific mRNA, pG2 as well.
7925474	6	65	theme	high	781:784	arg1	similarity					786:795	this high similarity	776:795	this high similarity	776:795	musculus dlk and human dlk revealed 86% and 99% identity, respectively, to a 259-amino-acid residue overlap, and this high similarity extends with minor corrections to the human adrenal-specific mRNA, pG2 as well.
7925474	1	66	theme	neuroendocrine	120:133	arg1	tumors					135:140	neuroendocrine tumors	120:140	neuroendocrine tumors	120:140	A novel circulating human epidermal-growth-factor-like protein expressed in neuroendocrine tumors and its relation to the gene products of dlk and pG2.
7925474	1	67	theme	epidermal-growth-factor-like	70:97	arg1	protein					99:105	A novel circulating human epidermal-growth-factor-like protein	44:105	A novel circulating human epidermal-growth-factor-like protein	44:105	A novel circulating human epidermal-growth-factor-like protein expressed in neuroendocrine tumors and its relation to the gene products of dlk and pG2.
7925474	7	68	theme	neuroendocrine	978:991	arg1	elements					993:1000	neuroendocrine elements	978:1000	neuroendocrine elements	978:1000	Immunohistochemical analysis demonstrated the presence of FA1 in 10 out of 14 lung tumors containing neuroendocrine elements, and in the placental villi where FA1 was exclusively seen in stromal cells in close contact to the vascular structure.
7925474	7	69	theme	lung	955:958	arg1	tumors					960:965	10 out of 14 lung tumors	942:965	10 out of 14 lung tumors containing neuroendocrine elements	942:1000	Immunohistochemical analysis demonstrated the presence of FA1 in 10 out of 14 lung tumors containing neuroendocrine elements, and in the placental villi where FA1 was exclusively seen in stromal cells in close contact to the vascular structure.
7925474	4	70	contain	contains	509:516	arg2	sites					564:568	up to ten O-glycosylation and N-glycosylation sites	518:568	sites	564:568	FA1 has six well conserved epidermal-growth-factor motifs and contains up to ten O-glycosylation and N-glycosylation sites, six of which are differentially glycosylated.
7925474	4	70	contain	contains	509:516	arg2	O-glycosylation					528:542	up to ten O-glycosylation and N-glycosylation sites	518:568	O-glycosylation	528:542	FA1 has six well conserved epidermal-growth-factor motifs and contains up to ten O-glycosylation and N-glycosylation sites, six of which are differentially glycosylated.
7925474	4	70	contain	contains	509:516	arg1	FA1					447:449	FA1	447:449	FA1	447:449	FA1 has six well conserved epidermal-growth-factor motifs and contains up to ten O-glycosylation and N-glycosylation sites, six of which are differentially glycosylated.
7925474	9	71	from	identical	1503:1511	arg1	turn					1494:1497	turn	1494:1497	turn	1494:1497	Our findings suggest that FA1 is synthesized as a membrane anchored protein and released into the circulation after enzymic cleavage, and that circulating FA1 represents the post-translationally modified gene product of human dlk which, in turn, is identical to human adrenal-specific mRNA pG2.
7925474	4	72	contain	has	451:453	arg2	motifs					498:503	six well conserved epidermal-growth-factor motifs	455:503	six well conserved epidermal-growth-factor motifs	455:503	FA1 has six well conserved epidermal-growth-factor motifs and contains up to ten O-glycosylation and N-glycosylation sites, six of which are differentially glycosylated.
7925474	4	72	contain	has	451:453	arg1	FA1					447:449	FA1	447:449	FA1	447:449	FA1 has six well conserved epidermal-growth-factor motifs and contains up to ten O-glycosylation and N-glycosylation sites, six of which are differentially glycosylated.
7925474	2	73	theme	primary	228:234	arg1	structure					236:244	the primary structure	224:244	the primary structure	224:244	The present paper describes the primary structure, glycosylation and tissue localization of fetal antigen 1 (FA1) isolated from second-trimester human amniotic fluid.
7925474	8	74	theme	cells	1215:1219	arg1	granules					1194:1201	the insulin secretory granules	1172:1201	the insulin secretory granules of the beta cells within the islets of Langerhans	1172:1251	In the pancreas, FA1 co-localized with insulin in the insulin secretory granules of the beta cells within the islets of Langerhans.
7925474	2	75	theme	amniotic	347:354	arg1	fluid					356:360	second-trimester human amniotic fluid	324:360	second-trimester human amniotic fluid	324:360	The present paper describes the primary structure, glycosylation and tissue localization of fetal antigen 1 (FA1) isolated from second-trimester human amniotic fluid.
7925474	3	76	theme	amino	426:430	arg1	residues					437:444	225-262 amino acid residues	418:444	225-262 amino acid residues	418:444	FA1 is a single-chained, heterogeneous glycoprotein of 225-262 amino acid residues.
7925474	7	77	theme	Immunohistochemical	877:895	arg1	analysis					897:904	Immunohistochemical analysis	877:904	Immunohistochemical analysis	877:904	Immunohistochemical analysis demonstrated the presence of FA1 in 10 out of 14 lung tumors containing neuroendocrine elements, and in the placental villi where FA1 was exclusively seen in stromal cells in close contact to the vascular structure.
7925474	3	78	gly	glycoprotein	402:413	arg1	FA1					363:365	FA1	363:365	FA1	363:365	FA1 is a single-chained, heterogeneous glycoprotein of 225-262 amino acid residues.
7925474	3	78	gly	glycoprotein	402:413	arg1	glycoprotein					402:413	a single-chained, heterogeneous glycoprotein	370:413	a single-chained, heterogeneous glycoprotein of 225-262 amino acid residues	370:444	FA1 is a single-chained, heterogeneous glycoprotein of 225-262 amino acid residues.
7925474	6	79	theme	%	709:709	arg1	identity					711:718	99% identity	707:718	99% identity	707:718	musculus dlk and human dlk revealed 86% and 99% identity, respectively, to a 259-amino-acid residue overlap, and this high similarity extends with minor corrections to the human adrenal-specific mRNA, pG2 as well.
7925474	2	80	theme	human	341:345	arg1	fluid					356:360	second-trimester human amniotic fluid	324:360	second-trimester human amniotic fluid	324:360	The present paper describes the primary structure, glycosylation and tissue localization of fetal antigen 1 (FA1) isolated from second-trimester human amniotic fluid.
29485866	0	0	theme	Tetratricopeptide	85:101	arg1	TPR					111:113	TPR	111:113	TPR	111:113	O-GlcNAc Transferase Recognizes Protein Substrates Using an Asparagine Ladder in the Tetratricopeptide Repeat (TPR) Superhelix.
29485866	0	0	theme	Tetratricopeptide	85:101	arg1	Repeat					103:108	Tetratricopeptide Repeat	85:108	the Tetratricopeptide Repeat (TPR) Superhelix	81:125	O-GlcNAc Transferase Recognizes Protein Substrates Using an Asparagine Ladder in the Tetratricopeptide Repeat (TPR) Superhelix.
29485866	2	1	theme	de	496:497	arg1	glycosylation					513:525	glycosylation	513:525	glycosylation	513:525	To address this question, we developed a protein microarray assay that chemoenzymatically labels de novo sites of glycosylation with biotin, allowing us to simultaneously assess OGT activity across >6000 human proteins.
29485866	2	1	theme	de	496:497	arg1	sites					504:508	de novo sites	496:508	de novo sites of glycosylation with biotin	496:537	To address this question, we developed a protein microarray assay that chemoenzymatically labels de novo sites of glycosylation with biotin, allowing us to simultaneously assess OGT activity across >6000 human proteins.
29485866	4	2	theme	short	876:880	arg1	peptides					882:889	short peptides	876:889	short peptides	876:889	When five asparagines were mutated, OGT retained significant activity against short peptides, but showed limited limited glycosylation of protein substrates on the microarray.
29485866	1	3	theme	O-GlcNAc	159:166	arg1	responsible					198:208	responsible	198:208	responsible	198:208	The essential mammalian enzyme O-GlcNAc Transferase (OGT) is uniquely responsible for transferring N-acetylglucosamine to over a thousand nuclear and cytoplasmic proteins, yet there is no known consensus sequence and it remains unclear how OGT recognizes its substrates.
29485866	1	3	theme	O-GlcNAc	159:166	arg1	OGT					181:183	OGT	181:183	OGT	181:183	The essential mammalian enzyme O-GlcNAc Transferase (OGT) is uniquely responsible for transferring N-acetylglucosamine to over a thousand nuclear and cytoplasmic proteins, yet there is no known consensus sequence and it remains unclear how OGT recognizes its substrates.
29485866	1	3	theme	O-GlcNAc	159:166	arg1	Transferase					168:178	The essential mammalian enzyme O-GlcNAc Transferase	128:178	The essential mammalian enzyme O-GlcNAc Transferase (OGT)	128:184	The essential mammalian enzyme O-GlcNAc Transferase (OGT) is uniquely responsible for transferring N-acetylglucosamine to over a thousand nuclear and cytoplasmic proteins, yet there is no known consensus sequence and it remains unclear how OGT recognizes its substrates.
29485866	1	4	theme	thousand	257:264	arg1	proteins					290:297	a thousand nuclear and cytoplasmic proteins	255:297	a thousand nuclear and cytoplasmic proteins	255:297	The essential mammalian enzyme O-GlcNAc Transferase (OGT) is uniquely responsible for transferring N-acetylglucosamine to over a thousand nuclear and cytoplasmic proteins, yet there is no known consensus sequence and it remains unclear how OGT recognizes its substrates.
29485866	3	5	theme	ladder	713:718	arg1	selection					677:685	substrate selection	667:685	substrate selection of a conserved asparagine ladder within the lumen of OGT's superhelical tetratricopeptide repeat (TPR) domain	667:795	With this assay we examined the contribution to substrate selection of a conserved asparagine ladder within the lumen of OGT's superhelical tetratricopeptide repeat (TPR) domain.
29485866	2	6	theme	human	603:607	arg1	proteins					609:616	>6000 human proteins	597:616	>6000 human proteins	597:616	To address this question, we developed a protein microarray assay that chemoenzymatically labels de novo sites of glycosylation with biotin, allowing us to simultaneously assess OGT activity across >6000 human proteins.
29485866	5	7	from	O-GlcNAcylation	974:988	arg1	extracts					1020:1027	cell extracts	1015:1027	cell extracts	1015:1027	O-GlcNAcylation of protein substrates in cell extracts was also greatly attenuated.
29485866	1	8	theme	nuclear	266:272	arg1	proteins					290:297	a thousand nuclear and cytoplasmic proteins	255:297	a thousand nuclear and cytoplasmic proteins	255:297	The essential mammalian enzyme O-GlcNAc Transferase (OGT) is uniquely responsible for transferring N-acetylglucosamine to over a thousand nuclear and cytoplasmic proteins, yet there is no known consensus sequence and it remains unclear how OGT recognizes its substrates.
29485866	3	9	theme	conserved	692:700	arg1	ladder					713:718	a conserved asparagine ladder	690:718	a conserved asparagine ladder	690:718	With this assay we examined the contribution to substrate selection of a conserved asparagine ladder within the lumen of OGT's superhelical tetratricopeptide repeat (TPR) domain.
29485866	0	10	theme	Repeat	103:108	arg1	Superhelix					116:125	the Tetratricopeptide Repeat (TPR) Superhelix	81:125	the Tetratricopeptide Repeat (TPR) Superhelix	81:125	O-GlcNAc Transferase Recognizes Protein Substrates Using an Asparagine Ladder in the Tetratricopeptide Repeat (TPR) Superhelix.
29485866	2	11	with	sites	504:508	arg1	biotin					532:537	biotin	532:537	biotin	532:537	To address this question, we developed a protein microarray assay that chemoenzymatically labels de novo sites of glycosylation with biotin, allowing us to simultaneously assess OGT activity across >6000 human proteins.
29485866	6	12	theme	substrates	1110:1119	arg1	majority					1094:1101	the majority	1090:1101	the majority of its substrates	1090:1119	We conclude that OGT recognizes the majority of its substrates by binding them to the asparagine ladder in the TPR lumen proximal to the catalytic domain.
29485866	1	13	theme	cytoplasmic	278:288	arg1	proteins					290:297	a thousand nuclear and cytoplasmic proteins	255:297	a thousand nuclear and cytoplasmic proteins	255:297	The essential mammalian enzyme O-GlcNAc Transferase (OGT) is uniquely responsible for transferring N-acetylglucosamine to over a thousand nuclear and cytoplasmic proteins, yet there is no known consensus sequence and it remains unclear how OGT recognizes its substrates.
29485866	2	14	theme	glycosylation	513:525	arg1	glycosylation					513:525	glycosylation	513:525	glycosylation	513:525	To address this question, we developed a protein microarray assay that chemoenzymatically labels de novo sites of glycosylation with biotin, allowing us to simultaneously assess OGT activity across >6000 human proteins.
29485866	2	14	theme	glycosylation	513:525	arg1	sites					504:508	de novo sites	496:508	de novo sites of glycosylation with biotin	496:537	To address this question, we developed a protein microarray assay that chemoenzymatically labels de novo sites of glycosylation with biotin, allowing us to simultaneously assess OGT activity across >6000 human proteins.
29485866	6	15	theme	asparagine	1144:1153	arg1	ladder					1155:1160	the asparagine ladder	1140:1160	the asparagine ladder in the TPR lumen proximal to the catalytic domain	1140:1210	We conclude that OGT recognizes the majority of its substrates by binding them to the asparagine ladder in the TPR lumen proximal to the catalytic domain.
29485866	5	16	theme	protein	993:999	arg1	substrates					1001:1010	protein substrates	993:1010	protein substrates	993:1010	O-GlcNAcylation of protein substrates in cell extracts was also greatly attenuated.
29485866	2	17	gly	glycosylation	513:525	arg2	glycosylation					513:525	glycosylation	513:525	glycosylation	513:525	To address this question, we developed a protein microarray assay that chemoenzymatically labels de novo sites of glycosylation with biotin, allowing us to simultaneously assess OGT activity across >6000 human proteins.
29485866	2	17	gly	glycosylation	513:525	arg2	sites					504:508	de novo sites	496:508	de novo sites of glycosylation with biotin	496:537	To address this question, we developed a protein microarray assay that chemoenzymatically labels de novo sites of glycosylation with biotin, allowing us to simultaneously assess OGT activity across >6000 human proteins.
29485866	3	18	theme	repeat	777:782	arg1	domain					790:795	OGT's superhelical tetratricopeptide repeat (TPR) domain	740:795	OGT's superhelical tetratricopeptide repeat (TPR) domain	740:795	With this assay we examined the contribution to substrate selection of a conserved asparagine ladder within the lumen of OGT's superhelical tetratricopeptide repeat (TPR) domain.
29485866	2	19	theme	protein	440:446	arg1	assay					459:463	a protein microarray assay	438:463	a protein microarray assay that chemoenzymatically labels de novo sites of glycosylation with biotin, allowing us to simultaneously assess OGT activity across >6000 human proteins	438:616	To address this question, we developed a protein microarray assay that chemoenzymatically labels de novo sites of glycosylation with biotin, allowing us to simultaneously assess OGT activity across >6000 human proteins.
29485866	6	20	theme	TPR	1169:1171	arg1	lumen					1173:1177	the TPR lumen	1165:1177	the TPR lumen proximal to the catalytic domain	1165:1210	We conclude that OGT recognizes the majority of its substrates by binding them to the asparagine ladder in the TPR lumen proximal to the catalytic domain.
29485866	0	21	theme	O-GlcNAc	0:7	arg1	Transferase					9:19	O-GlcNAc Transferase	0:19	O-GlcNAc Transferase	0:19	O-GlcNAc Transferase Recognizes Protein Substrates Using an Asparagine Ladder in the Tetratricopeptide Repeat (TPR) Superhelix.
29485866	3	22	theme	superhelical	746:757	arg1	domain					790:795	OGT's superhelical tetratricopeptide repeat (TPR) domain	740:795	OGT's superhelical tetratricopeptide repeat (TPR) domain	740:795	With this assay we examined the contribution to substrate selection of a conserved asparagine ladder within the lumen of OGT's superhelical tetratricopeptide repeat (TPR) domain.
29485866	4	23	theme	significant	847:857	arg1	activity					859:866	significant activity	847:866	significant activity	847:866	When five asparagines were mutated, OGT retained significant activity against short peptides, but showed limited limited glycosylation of protein substrates on the microarray.
29485866	5	24	theme	substrates	1001:1010	arg1	O-GlcNAcylation					974:988	O-GlcNAcylation	974:988	O-GlcNAcylation of protein substrates in cell extracts	974:1027	O-GlcNAcylation of protein substrates in cell extracts was also greatly attenuated.
29485866	0	25	theme	Protein	32:38	arg1	Substrates					40:49	Protein Substrates	32:49	Protein Substrates Using an Asparagine Ladder in the Tetratricopeptide Repeat (TPR) Superhelix	32:125	O-GlcNAc Transferase Recognizes Protein Substrates Using an Asparagine Ladder in the Tetratricopeptide Repeat (TPR) Superhelix.
29485866	3	26	theme	tetratricopeptide	759:775	arg1	domain					790:795	OGT's superhelical tetratricopeptide repeat (TPR) domain	740:795	OGT's superhelical tetratricopeptide repeat (TPR) domain	740:795	With this assay we examined the contribution to substrate selection of a conserved asparagine ladder within the lumen of OGT's superhelical tetratricopeptide repeat (TPR) domain.
29485866	6	27	from	ladder	1155:1160	arg1	lumen					1173:1177	the TPR lumen	1165:1177	the TPR lumen proximal to the catalytic domain	1165:1210	We conclude that OGT recognizes the majority of its substrates by binding them to the asparagine ladder in the TPR lumen proximal to the catalytic domain.
29485866	6	28	theme	proximal	1179:1186	arg1	lumen					1173:1177	the TPR lumen	1165:1177	the TPR lumen proximal to the catalytic domain	1165:1210	We conclude that OGT recognizes the majority of its substrates by binding them to the asparagine ladder in the TPR lumen proximal to the catalytic domain.
29485866	4	29	theme	substrates	944:953	arg1	glycosylation					919:931	limited limited glycosylation	903:931	limited limited glycosylation of protein substrates	903:953	When five asparagines were mutated, OGT retained significant activity against short peptides, but showed limited limited glycosylation of protein substrates on the microarray.
29485866	3	30	theme	TPR	785:787	arg1	domain					790:795	OGT's superhelical tetratricopeptide repeat (TPR) domain	740:795	OGT's superhelical tetratricopeptide repeat (TPR) domain	740:795	With this assay we examined the contribution to substrate selection of a conserved asparagine ladder within the lumen of OGT's superhelical tetratricopeptide repeat (TPR) domain.
29485866	4	31	theme	protein	936:942	arg1	substrates					944:953	protein substrates	936:953	protein substrates	936:953	When five asparagines were mutated, OGT retained significant activity against short peptides, but showed limited limited glycosylation of protein substrates on the microarray.
29485866	0	32	theme	Asparagine	60:69	arg1	Ladder					71:76	an Asparagine Ladder	57:76	an Asparagine Ladder in the Tetratricopeptide Repeat (TPR) Superhelix	57:125	O-GlcNAc Transferase Recognizes Protein Substrates Using an Asparagine Ladder in the Tetratricopeptide Repeat (TPR) Superhelix.
29485866	2	33	dep	de	496:497	arg1	novo					499:502	novo	499:502	novo	499:502	To address this question, we developed a protein microarray assay that chemoenzymatically labels de novo sites of glycosylation with biotin, allowing us to simultaneously assess OGT activity across >6000 human proteins.
29485866	0	34	from	Ladder	71:76	arg1	Superhelix					116:125	the Tetratricopeptide Repeat (TPR) Superhelix	81:125	the Tetratricopeptide Repeat (TPR) Superhelix	81:125	O-GlcNAc Transferase Recognizes Protein Substrates Using an Asparagine Ladder in the Tetratricopeptide Repeat (TPR) Superhelix.
29485866	4	35	gly	glycosylation	919:931	arg1	microarray					962:971	the microarray	958:971	the microarray	958:971	When five asparagines were mutated, OGT retained significant activity against short peptides, but showed limited limited glycosylation of protein substrates on the microarray.
29485866	4	35	gly	glycosylation	919:931	arg1	substrates					944:953	protein substrates	936:953	protein substrates	936:953	When five asparagines were mutated, OGT retained significant activity against short peptides, but showed limited limited glycosylation of protein substrates on the microarray.
29485866	2	36	theme	microarray	448:457	arg1	assay					459:463	a protein microarray assay	438:463	a protein microarray assay that chemoenzymatically labels de novo sites of glycosylation with biotin, allowing us to simultaneously assess OGT activity across >6000 human proteins	438:616	To address this question, we developed a protein microarray assay that chemoenzymatically labels de novo sites of glycosylation with biotin, allowing us to simultaneously assess OGT activity across >6000 human proteins.
29485866	1	37	theme	known	316:320	arg1	sequence					332:339	no known consensus sequence	313:339	no known consensus sequence	313:339	The essential mammalian enzyme O-GlcNAc Transferase (OGT) is uniquely responsible for transferring N-acetylglucosamine to over a thousand nuclear and cytoplasmic proteins, yet there is no known consensus sequence and it remains unclear how OGT recognizes its substrates.
29485866	2	38	theme	OGT	577:579	arg1	activity					581:588	OGT activity	577:588	OGT activity across >6000 human proteins	577:616	To address this question, we developed a protein microarray assay that chemoenzymatically labels de novo sites of glycosylation with biotin, allowing us to simultaneously assess OGT activity across >6000 human proteins.
29485866	1	39	theme	consensus	322:330	arg1	sequence					332:339	no known consensus sequence	313:339	no known consensus sequence	313:339	The essential mammalian enzyme O-GlcNAc Transferase (OGT) is uniquely responsible for transferring N-acetylglucosamine to over a thousand nuclear and cytoplasmic proteins, yet there is no known consensus sequence and it remains unclear how OGT recognizes its substrates.
29485866	4	40	theme	limited	911:917	arg1	glycosylation					919:931	limited limited glycosylation	903:931	limited limited glycosylation of protein substrates	903:953	When five asparagines were mutated, OGT retained significant activity against short peptides, but showed limited limited glycosylation of protein substrates on the microarray.
29485866	4	41	theme	limited	903:909	arg1	glycosylation					919:931	limited limited glycosylation	903:931	limited limited glycosylation of protein substrates	903:953	When five asparagines were mutated, OGT retained significant activity against short peptides, but showed limited limited glycosylation of protein substrates on the microarray.
29485866	5	42	theme	cell	1015:1018	arg1	extracts					1020:1027	cell extracts	1015:1027	cell extracts	1015:1027	O-GlcNAcylation of protein substrates in cell extracts was also greatly attenuated.
29485866	1	43	theme	essential	132:140	arg1	responsible					198:208	responsible	198:208	responsible	198:208	The essential mammalian enzyme O-GlcNAc Transferase (OGT) is uniquely responsible for transferring N-acetylglucosamine to over a thousand nuclear and cytoplasmic proteins, yet there is no known consensus sequence and it remains unclear how OGT recognizes its substrates.
29485866	1	43	theme	essential	132:140	arg1	OGT					181:183	OGT	181:183	OGT	181:183	The essential mammalian enzyme O-GlcNAc Transferase (OGT) is uniquely responsible for transferring N-acetylglucosamine to over a thousand nuclear and cytoplasmic proteins, yet there is no known consensus sequence and it remains unclear how OGT recognizes its substrates.
29485866	1	43	theme	essential	132:140	arg1	Transferase					168:178	The essential mammalian enzyme O-GlcNAc Transferase	128:178	The essential mammalian enzyme O-GlcNAc Transferase (OGT)	128:184	The essential mammalian enzyme O-GlcNAc Transferase (OGT) is uniquely responsible for transferring N-acetylglucosamine to over a thousand nuclear and cytoplasmic proteins, yet there is no known consensus sequence and it remains unclear how OGT recognizes its substrates.
29485866	3	44	theme	substrate	667:675	arg1	selection					677:685	substrate selection	667:685	substrate selection of a conserved asparagine ladder within the lumen of OGT's superhelical tetratricopeptide repeat (TPR) domain	667:795	With this assay we examined the contribution to substrate selection of a conserved asparagine ladder within the lumen of OGT's superhelical tetratricopeptide repeat (TPR) domain.
29485866	1	45	theme	mammalian	142:150	arg1	responsible					198:208	responsible	198:208	responsible	198:208	The essential mammalian enzyme O-GlcNAc Transferase (OGT) is uniquely responsible for transferring N-acetylglucosamine to over a thousand nuclear and cytoplasmic proteins, yet there is no known consensus sequence and it remains unclear how OGT recognizes its substrates.
29485866	1	45	theme	mammalian	142:150	arg1	OGT					181:183	OGT	181:183	OGT	181:183	The essential mammalian enzyme O-GlcNAc Transferase (OGT) is uniquely responsible for transferring N-acetylglucosamine to over a thousand nuclear and cytoplasmic proteins, yet there is no known consensus sequence and it remains unclear how OGT recognizes its substrates.
29485866	1	45	theme	mammalian	142:150	arg1	Transferase					168:178	The essential mammalian enzyme O-GlcNAc Transferase	128:178	The essential mammalian enzyme O-GlcNAc Transferase (OGT)	128:184	The essential mammalian enzyme O-GlcNAc Transferase (OGT) is uniquely responsible for transferring N-acetylglucosamine to over a thousand nuclear and cytoplasmic proteins, yet there is no known consensus sequence and it remains unclear how OGT recognizes its substrates.
29485866	3	46	theme	domain	790:795	arg1	lumen					731:735	the lumen	727:735	the lumen of OGT's superhelical tetratricopeptide repeat (TPR) domain	727:795	With this assay we examined the contribution to substrate selection of a conserved asparagine ladder within the lumen of OGT's superhelical tetratricopeptide repeat (TPR) domain.
29485866	3	47	theme	asparagine	702:711	arg1	ladder					713:718	a conserved asparagine ladder	690:718	a conserved asparagine ladder	690:718	With this assay we examined the contribution to substrate selection of a conserved asparagine ladder within the lumen of OGT's superhelical tetratricopeptide repeat (TPR) domain.
29485866	6	48	theme	catalytic	1195:1203	arg1	domain					1205:1210	the catalytic domain	1191:1210	the catalytic domain	1191:1210	We conclude that OGT recognizes the majority of its substrates by binding them to the asparagine ladder in the TPR lumen proximal to the catalytic domain.
29485866	1	49	theme	enzyme	152:157	arg1	responsible					198:208	responsible	198:208	responsible	198:208	The essential mammalian enzyme O-GlcNAc Transferase (OGT) is uniquely responsible for transferring N-acetylglucosamine to over a thousand nuclear and cytoplasmic proteins, yet there is no known consensus sequence and it remains unclear how OGT recognizes its substrates.
29485866	1	49	theme	enzyme	152:157	arg1	OGT					181:183	OGT	181:183	OGT	181:183	The essential mammalian enzyme O-GlcNAc Transferase (OGT) is uniquely responsible for transferring N-acetylglucosamine to over a thousand nuclear and cytoplasmic proteins, yet there is no known consensus sequence and it remains unclear how OGT recognizes its substrates.
29485866	1	49	theme	enzyme	152:157	arg1	Transferase					168:178	The essential mammalian enzyme O-GlcNAc Transferase	128:178	The essential mammalian enzyme O-GlcNAc Transferase (OGT)	128:184	The essential mammalian enzyme O-GlcNAc Transferase (OGT) is uniquely responsible for transferring N-acetylglucosamine to over a thousand nuclear and cytoplasmic proteins, yet there is no known consensus sequence and it remains unclear how OGT recognizes its substrates.
7841792	0	0	theme	solid-phase	82:92	arg1	degradation					100:110	solid-phase Edman degradation	82:110	solid-phase Edman degradation	82:110	Characterization of a single glycosylated asparagine site on a glycopeptide using solid-phase Edman degradation.
7841792	6	1	dep	Glu-C	1056:1060	arg1	glycopeptide					1062:1073	glycopeptide	1062:1073	glycopeptide	1062:1073	Comparison between an endoproteinase Glu-C glycopeptide and a tryptic glycopeptide showed that the oligosaccharide attached to Asn494 was stable after at least 10 cycles of Edman degradation.
7841792	6	2	gly	glycopeptide	1089:1100	arg2	glycopeptide					1089:1100	a tryptic glycopeptide	1079:1100	a tryptic glycopeptide	1079:1100	Comparison between an endoproteinase Glu-C glycopeptide and a tryptic glycopeptide showed that the oligosaccharide attached to Asn494 was stable after at least 10 cycles of Edman degradation.
7841792	3	3	theme	new	530:532	arg1	method					534:539	a new method	528:539	a new method to gain site-specific compositional data on the oligosaccharides attached to a single amino acid	528:636	Here we introduce a new method to gain site-specific compositional data on the oligosaccharides attached to a single amino acid.
7841792	4	4	theme	amperometric	910:921	arg1	detection					923:931	pulsed amperometric detection	903:931	pulsed amperometric detection	903:931	Using a model glycopeptide from a mutant human albumin Casebrook, glycosylated PTH-Asn was recovered after sequential solid-phase Edman degradation, subjected to acid hydrolysis and the sugars were identified by high performance anion exchange chromatography with pulsed amperometric detection.
7841792	1	5	gly	glycosylated	264:275	arg1	residue					277:283	each glycosylated residue	259:283	each glycosylated residue	259:283	The characterization of site-specific glycosylation is traditionally dependent on the availability of suitable proteolytic cleavage sites between each glycosylated residue, so that peptides containing individual glycosylation sites are recovered.
7841792	2	6	theme	domains	396:402	arg1	case					367:370	the case	363:370	the case of heavily glycosylated domains such as the O-glycosylated mucins, which have no available protease sites	363:476	In the case of heavily glycosylated domains such as the O-glycosylated mucins, which have no available protease sites, this approach is not possible.
7841792	3	7	from	data	577:580	arg1	oligosaccharides					589:604	the oligosaccharides	585:604	the oligosaccharides attached to a single amino acid	585:636	Here we introduce a new method to gain site-specific compositional data on the oligosaccharides attached to a single amino acid.
7841792	0	8	from	Characterization	0:15	arg1	glycopeptide					63:74	a glycopeptide	61:74	a glycopeptide using solid-phase Edman degradation	61:110	Characterization of a single glycosylated asparagine site on a glycopeptide using solid-phase Edman degradation.
7841792	2	9	from	case	367:370	arg1	possible					500:507	possible	500:507	possible	500:507	In the case of heavily glycosylated domains such as the O-glycosylated mucins, which have no available protease sites, this approach is not possible.
7841792	5	10	theme	Sac	946:948	arg1	derivative					951:960	The PTH-Asn(Sac) derivative	934:960	The PTH-Asn(Sac) derivative	934:960	The PTH-Asn(Sac) derivative was further characterized by ionspray mass spectrometry.
7841792	4	11	with	chromatography	883:896	arg1	detection					923:931	pulsed amperometric detection	903:931	pulsed amperometric detection	903:931	Using a model glycopeptide from a mutant human albumin Casebrook, glycosylated PTH-Asn was recovered after sequential solid-phase Edman degradation, subjected to acid hydrolysis and the sugars were identified by high performance anion exchange chromatography with pulsed amperometric detection.
7841792	0	12	theme	Edman	94:98	arg1	degradation					100:110	solid-phase Edman degradation	82:110	solid-phase Edman degradation	82:110	Characterization of a single glycosylated asparagine site on a glycopeptide using solid-phase Edman degradation.
7841792	4	13	theme	glycopeptide	653:664	arg1	model					647:651	a model	645:651	a model glycopeptide from a mutant human albumin Casebrook	645:702	Using a model glycopeptide from a mutant human albumin Casebrook, glycosylated PTH-Asn was recovered after sequential solid-phase Edman degradation, subjected to acid hydrolysis and the sugars were identified by high performance anion exchange chromatography with pulsed amperometric detection.
7841792	4	14	theme	acid	801:804	arg1	hydrolysis					806:815	acid hydrolysis	801:815	acid hydrolysis	801:815	Using a model glycopeptide from a mutant human albumin Casebrook, glycosylated PTH-Asn was recovered after sequential solid-phase Edman degradation, subjected to acid hydrolysis and the sugars were identified by high performance anion exchange chromatography with pulsed amperometric detection.
7841792	0	15	gly	glycopeptide	63:74	arg2	glycopeptide					63:74	a glycopeptide	61:74	a glycopeptide using solid-phase Edman degradation	61:110	Characterization of a single glycosylated asparagine site on a glycopeptide using solid-phase Edman degradation.
7841792	4	16	theme	solid-phase	757:767	arg1	degradation					775:785	sequential solid-phase Edman degradation	746:785	sequential solid-phase Edman degradation	746:785	Using a model glycopeptide from a mutant human albumin Casebrook, glycosylated PTH-Asn was recovered after sequential solid-phase Edman degradation, subjected to acid hydrolysis and the sugars were identified by high performance anion exchange chromatography with pulsed amperometric detection.
7841792	0	17	from	site	53:56	arg1	glycopeptide					63:74	a glycopeptide	61:74	a glycopeptide using solid-phase Edman degradation	61:110	Characterization of a single glycosylated asparagine site on a glycopeptide using solid-phase Edman degradation.
7841792	4	18	gly	glycopeptide	653:664	arg2	glycopeptide					653:664	glycopeptide	653:664	glycopeptide	653:664	Using a model glycopeptide from a mutant human albumin Casebrook, glycosylated PTH-Asn was recovered after sequential solid-phase Edman degradation, subjected to acid hydrolysis and the sugars were identified by high performance anion exchange chromatography with pulsed amperometric detection.
7841792	4	18	gly	glycopeptide	653:664	arg1	Casebrook					694:702	a mutant human albumin Casebrook	671:702	a mutant human albumin Casebrook	671:702	Using a model glycopeptide from a mutant human albumin Casebrook, glycosylated PTH-Asn was recovered after sequential solid-phase Edman degradation, subjected to acid hydrolysis and the sugars were identified by high performance anion exchange chromatography with pulsed amperometric detection.
7841792	2	19	theme	available	453:461	arg1	sites					472:476	no available protease sites	450:476	no available protease sites	450:476	In the case of heavily glycosylated domains such as the O-glycosylated mucins, which have no available protease sites, this approach is not possible.
7841792	3	20	theme	site-specific	549:561	arg1	data					577:580	site-specific compositional data	549:580	site-specific compositional data on the oligosaccharides attached to a single amino acid	549:636	Here we introduce a new method to gain site-specific compositional data on the oligosaccharides attached to a single amino acid.
7841792	3	21	attach	attached	606:613	arg2	oligosaccharides					589:604	the oligosaccharides	585:604	the oligosaccharides attached to a single amino acid	585:636	Here we introduce a new method to gain site-specific compositional data on the oligosaccharides attached to a single amino acid.
7841792	3	21	attach	attached	606:613	arg1	acid					633:636	a single amino acid	618:636	a single amino acid	618:636	Here we introduce a new method to gain site-specific compositional data on the oligosaccharides attached to a single amino acid.
7841792	4	22	theme	albumin	686:692	arg1	Casebrook					694:702	a mutant human albumin Casebrook	671:702	a mutant human albumin Casebrook	671:702	Using a model glycopeptide from a mutant human albumin Casebrook, glycosylated PTH-Asn was recovered after sequential solid-phase Edman degradation, subjected to acid hydrolysis and the sugars were identified by high performance anion exchange chromatography with pulsed amperometric detection.
7841792	6	23	theme	Edman	1192:1196	arg1	degradation					1198:1208	Edman degradation	1192:1208	Edman degradation	1192:1208	Comparison between an endoproteinase Glu-C glycopeptide and a tryptic glycopeptide showed that the oligosaccharide attached to Asn494 was stable after at least 10 cycles of Edman degradation.
7841792	3	24	theme	compositional	563:575	arg1	data					577:580	site-specific compositional data	549:580	site-specific compositional data on the oligosaccharides attached to a single amino acid	549:636	Here we introduce a new method to gain site-specific compositional data on the oligosaccharides attached to a single amino acid.
7841792	4	25	theme	human	680:684	arg1	Casebrook					694:702	a mutant human albumin Casebrook	671:702	a mutant human albumin Casebrook	671:702	Using a model glycopeptide from a mutant human albumin Casebrook, glycosylated PTH-Asn was recovered after sequential solid-phase Edman degradation, subjected to acid hydrolysis and the sugars were identified by high performance anion exchange chromatography with pulsed amperometric detection.
7841792	2	26	from	possible	500:507	arg1	case					367:370	the case	363:370	the case of heavily glycosylated domains such as the O-glycosylated mucins, which have no available protease sites	363:476	In the case of heavily glycosylated domains such as the O-glycosylated mucins, which have no available protease sites, this approach is not possible.
7841792	2	27	gly	O-glycosylated	416:429	arg1	mucins					431:436	the O-glycosylated mucins	412:436	the O-glycosylated mucins	412:436	In the case of heavily glycosylated domains such as the O-glycosylated mucins, which have no available protease sites, this approach is not possible.
7841792	6	28	theme	endoproteinase	1041:1054	arg1	Glu-C					1056:1060	an endoproteinase Glu-C glycopeptide and a tryptic glycopeptide	1038:1100	Glu-C	1056:1060	Comparison between an endoproteinase Glu-C glycopeptide and a tryptic glycopeptide showed that the oligosaccharide attached to Asn494 was stable after at least 10 cycles of Edman degradation.
7841792	5	29	theme	ionspray	991:998	arg1	spectrometry					1005:1016	ionspray mass spectrometry	991:1016	ionspray mass spectrometry	991:1016	The PTH-Asn(Sac) derivative was further characterized by ionspray mass spectrometry.
7841792	6	30	theme	degradation	1198:1208	arg1	cycles					1182:1187	at least 10 cycles	1170:1187	at least 10 cycles of Edman degradation	1170:1208	Comparison between an endoproteinase Glu-C glycopeptide and a tryptic glycopeptide showed that the oligosaccharide attached to Asn494 was stable after at least 10 cycles of Edman degradation.
7841792	1	31	theme	individual	314:323	arg1	sites					339:343	individual glycosylation sites	314:343	individual glycosylation sites	314:343	The characterization of site-specific glycosylation is traditionally dependent on the availability of suitable proteolytic cleavage sites between each glycosylated residue, so that peptides containing individual glycosylation sites are recovered.
7841792	4	32	theme	pulsed	903:908	arg1	detection					923:931	pulsed amperometric detection	903:931	pulsed amperometric detection	903:931	Using a model glycopeptide from a mutant human albumin Casebrook, glycosylated PTH-Asn was recovered after sequential solid-phase Edman degradation, subjected to acid hydrolysis and the sugars were identified by high performance anion exchange chromatography with pulsed amperometric detection.
7841792	5	33	theme	mass	1000:1003	arg1	spectrometry					1005:1016	ionspray mass spectrometry	991:1016	ionspray mass spectrometry	991:1016	The PTH-Asn(Sac) derivative was further characterized by ionspray mass spectrometry.
7841792	1	34	theme	suitable	215:222	arg1	sites					245:249	suitable proteolytic cleavage sites	215:249	suitable proteolytic cleavage sites	215:249	The characterization of site-specific glycosylation is traditionally dependent on the availability of suitable proteolytic cleavage sites between each glycosylated residue, so that peptides containing individual glycosylation sites are recovered.
7841792	0	35	theme	single	22:27	arg1	site					53:56	a single glycosylated asparagine site	20:56	a single glycosylated asparagine site on a glycopeptide using solid-phase Edman degradation	20:110	Characterization of a single glycosylated asparagine site on a glycopeptide using solid-phase Edman degradation.
7841792	1	36	theme	glycosylation	325:337	arg1	sites					339:343	individual glycosylation sites	314:343	individual glycosylation sites	314:343	The characterization of site-specific glycosylation is traditionally dependent on the availability of suitable proteolytic cleavage sites between each glycosylated residue, so that peptides containing individual glycosylation sites are recovered.
7841792	4	37	theme	anion	868:872	arg1	chromatography					883:896	high performance anion exchange chromatography	851:896	high performance anion exchange chromatography with pulsed amperometric detection	851:931	Using a model glycopeptide from a mutant human albumin Casebrook, glycosylated PTH-Asn was recovered after sequential solid-phase Edman degradation, subjected to acid hydrolysis and the sugars were identified by high performance anion exchange chromatography with pulsed amperometric detection.
7841792	4	38	theme	performance	856:866	arg1	chromatography					883:896	high performance anion exchange chromatography	851:896	high performance anion exchange chromatography with pulsed amperometric detection	851:931	Using a model glycopeptide from a mutant human albumin Casebrook, glycosylated PTH-Asn was recovered after sequential solid-phase Edman degradation, subjected to acid hydrolysis and the sugars were identified by high performance anion exchange chromatography with pulsed amperometric detection.
7841792	1	39	theme	proteolytic	224:234	arg1	sites					245:249	suitable proteolytic cleavage sites	215:249	suitable proteolytic cleavage sites	215:249	The characterization of site-specific glycosylation is traditionally dependent on the availability of suitable proteolytic cleavage sites between each glycosylated residue, so that peptides containing individual glycosylation sites are recovered.
7841792	1	40	theme	cleavage	236:243	arg1	sites					245:249	suitable proteolytic cleavage sites	215:249	suitable proteolytic cleavage sites	215:249	The characterization of site-specific glycosylation is traditionally dependent on the availability of suitable proteolytic cleavage sites between each glycosylated residue, so that peptides containing individual glycosylation sites are recovered.
7841792	0	41	theme	asparagine	42:51	arg1	site					53:56	a single glycosylated asparagine site	20:56	a single glycosylated asparagine site on a glycopeptide using solid-phase Edman degradation	20:110	Characterization of a single glycosylated asparagine site on a glycopeptide using solid-phase Edman degradation.
7841792	4	42	from	Casebrook	694:702	arg1	glycopeptide					653:664	glycopeptide	653:664	glycopeptide	653:664	Using a model glycopeptide from a mutant human albumin Casebrook, glycosylated PTH-Asn was recovered after sequential solid-phase Edman degradation, subjected to acid hydrolysis and the sugars were identified by high performance anion exchange chromatography with pulsed amperometric detection.
7841792	4	43	theme	mutant	673:678	arg1	Casebrook					694:702	a mutant human albumin Casebrook	671:702	a mutant human albumin Casebrook	671:702	Using a model glycopeptide from a mutant human albumin Casebrook, glycosylated PTH-Asn was recovered after sequential solid-phase Edman degradation, subjected to acid hydrolysis and the sugars were identified by high performance anion exchange chromatography with pulsed amperometric detection.
7841792	3	44	theme	amino	627:631	arg1	acid					633:636	a single amino acid	618:636	a single amino acid	618:636	Here we introduce a new method to gain site-specific compositional data on the oligosaccharides attached to a single amino acid.
7841792	2	45	theme	O-glycosylated	416:429	arg1	mucins					431:436	the O-glycosylated mucins	412:436	the O-glycosylated mucins	412:436	In the case of heavily glycosylated domains such as the O-glycosylated mucins, which have no available protease sites, this approach is not possible.
7841792	1	46	theme	sites	245:249	arg1	availability					199:210	the availability	195:210	the availability of suitable proteolytic cleavage sites between each glycosylated residue, so that peptides containing individual glycosylation sites are recovered	195:357	The characterization of site-specific glycosylation is traditionally dependent on the availability of suitable proteolytic cleavage sites between each glycosylated residue, so that peptides containing individual glycosylation sites are recovered.
7841792	0	47	theme	glycosylated	29:40	arg1	site					53:56	a single glycosylated asparagine site	20:56	a single glycosylated asparagine site on a glycopeptide using solid-phase Edman degradation	20:110	Characterization of a single glycosylated asparagine site on a glycopeptide using solid-phase Edman degradation.
7841792	0	48	from	glycopeptide	63:74	arg1	Characterization					0:15	Characterization	0:15	Characterization of a single glycosylated asparagine site on a glycopeptide using solid-phase Edman degradation.	0:111	Characterization of a single glycosylated asparagine site on a glycopeptide using solid-phase Edman degradation.
7841792	4	49	theme	high	851:854	arg1	chromatography					883:896	high performance anion exchange chromatography	851:896	high performance anion exchange chromatography with pulsed amperometric detection	851:931	Using a model glycopeptide from a mutant human albumin Casebrook, glycosylated PTH-Asn was recovered after sequential solid-phase Edman degradation, subjected to acid hydrolysis and the sugars were identified by high performance anion exchange chromatography with pulsed amperometric detection.
7841792	1	50	gly	glycosylation	325:337	arg2	sites					339:343	individual glycosylation sites	314:343	individual glycosylation sites	314:343	The characterization of site-specific glycosylation is traditionally dependent on the availability of suitable proteolytic cleavage sites between each glycosylated residue, so that peptides containing individual glycosylation sites are recovered.
7841792	4	51	gly	glycosylated	705:716	arg1	PTH-Asn					718:724	glycosylated PTH-Asn	705:724	glycosylated PTH-Asn	705:724	Using a model glycopeptide from a mutant human albumin Casebrook, glycosylated PTH-Asn was recovered after sequential solid-phase Edman degradation, subjected to acid hydrolysis and the sugars were identified by high performance anion exchange chromatography with pulsed amperometric detection.
7841792	4	52	theme	exchange	874:881	arg1	chromatography					883:896	high performance anion exchange chromatography	851:896	high performance anion exchange chromatography with pulsed amperometric detection	851:931	Using a model glycopeptide from a mutant human albumin Casebrook, glycosylated PTH-Asn was recovered after sequential solid-phase Edman degradation, subjected to acid hydrolysis and the sugars were identified by high performance anion exchange chromatography with pulsed amperometric detection.
7841792	2	53	theme	glycosylated	383:394	arg1	mucins					431:436	the O-glycosylated mucins	412:436	the O-glycosylated mucins	412:436	In the case of heavily glycosylated domains such as the O-glycosylated mucins, which have no available protease sites, this approach is not possible.
7841792	2	53	theme	glycosylated	383:394	arg1	domains					396:402	heavily glycosylated domains	375:402	heavily glycosylated domains such as the O-glycosylated mucins, which have no available protease sites	375:476	In the case of heavily glycosylated domains such as the O-glycosylated mucins, which have no available protease sites, this approach is not possible.
7841792	0	54	theme	site	53:56	arg1	Characterization					0:15	Characterization	0:15	Characterization of a single glycosylated asparagine site on a glycopeptide using solid-phase Edman degradation.	0:111	Characterization of a single glycosylated asparagine site on a glycopeptide using solid-phase Edman degradation.
7841792	2	55	gly	glycosylated	383:394	arg1	mucins					431:436	the O-glycosylated mucins	412:436	the O-glycosylated mucins	412:436	In the case of heavily glycosylated domains such as the O-glycosylated mucins, which have no available protease sites, this approach is not possible.
7841792	2	55	gly	glycosylated	383:394	arg1	domains					396:402	heavily glycosylated domains	375:402	heavily glycosylated domains such as the O-glycosylated mucins, which have no available protease sites	375:476	In the case of heavily glycosylated domains such as the O-glycosylated mucins, which have no available protease sites, this approach is not possible.
7841792	2	56	contain	have	445:448	arg2	sites					472:476	no available protease sites	450:476	no available protease sites	450:476	In the case of heavily glycosylated domains such as the O-glycosylated mucins, which have no available protease sites, this approach is not possible.
7841792	2	56	contain	have	445:448	arg1	mucins					431:436	the O-glycosylated mucins	412:436	the O-glycosylated mucins	412:436	In the case of heavily glycosylated domains such as the O-glycosylated mucins, which have no available protease sites, this approach is not possible.
7841792	3	57	theme	single	620:625	arg1	acid					633:636	a single amino acid	618:636	a single amino acid	618:636	Here we introduce a new method to gain site-specific compositional data on the oligosaccharides attached to a single amino acid.
7841792	4	58	theme	Edman	769:773	arg1	degradation					775:785	sequential solid-phase Edman degradation	746:785	sequential solid-phase Edman degradation	746:785	Using a model glycopeptide from a mutant human albumin Casebrook, glycosylated PTH-Asn was recovered after sequential solid-phase Edman degradation, subjected to acid hydrolysis and the sugars were identified by high performance anion exchange chromatography with pulsed amperometric detection.
7841792	4	59	theme	sequential	746:755	arg1	degradation					775:785	sequential solid-phase Edman degradation	746:785	sequential solid-phase Edman degradation	746:785	Using a model glycopeptide from a mutant human albumin Casebrook, glycosylated PTH-Asn was recovered after sequential solid-phase Edman degradation, subjected to acid hydrolysis and the sugars were identified by high performance anion exchange chromatography with pulsed amperometric detection.
7841792	1	60	contain	containing	303:312	arg1	peptides					294:301	peptides	294:301	peptides containing individual glycosylation sites	294:343	The characterization of site-specific glycosylation is traditionally dependent on the availability of suitable proteolytic cleavage sites between each glycosylated residue, so that peptides containing individual glycosylation sites are recovered.
7841792	1	60	contain	containing	303:312	arg2	sites					339:343	individual glycosylation sites	314:343	individual glycosylation sites	314:343	The characterization of site-specific glycosylation is traditionally dependent on the availability of suitable proteolytic cleavage sites between each glycosylated residue, so that peptides containing individual glycosylation sites are recovered.
7841792	0	61	gly	glycosylated	29:40	arg1	site					53:56	a single glycosylated asparagine site	20:56	a single glycosylated asparagine site on a glycopeptide using solid-phase Edman degradation	20:110	Characterization of a single glycosylated asparagine site on a glycopeptide using solid-phase Edman degradation.
7841792	6	62	gly	glycopeptide	1062:1073	arg2	glycopeptide					1062:1073	glycopeptide	1062:1073	glycopeptide	1062:1073	Comparison between an endoproteinase Glu-C glycopeptide and a tryptic glycopeptide showed that the oligosaccharide attached to Asn494 was stable after at least 10 cycles of Edman degradation.
7841792	1	63	theme	site-specific	137:149	arg1	glycosylation					151:163	site-specific glycosylation	137:163	site-specific glycosylation	137:163	The characterization of site-specific glycosylation is traditionally dependent on the availability of suitable proteolytic cleavage sites between each glycosylated residue, so that peptides containing individual glycosylation sites are recovered.
7841792	5	64	theme	PTH-Asn	938:944	arg1	derivative					951:960	The PTH-Asn(Sac) derivative	934:960	The PTH-Asn(Sac) derivative	934:960	The PTH-Asn(Sac) derivative was further characterized by ionspray mass spectrometry.
7841792	1	65	theme	glycosylation	151:163	arg1	characterization					117:132	The characterization	113:132	The characterization of site-specific glycosylation	113:163	The characterization of site-specific glycosylation is traditionally dependent on the availability of suitable proteolytic cleavage sites between each glycosylated residue, so that peptides containing individual glycosylation sites are recovered.
7841792	1	65	theme	glycosylation	151:163	arg1	dependent					182:190	dependent	182:190	dependent	182:190	The characterization of site-specific glycosylation is traditionally dependent on the availability of suitable proteolytic cleavage sites between each glycosylated residue, so that peptides containing individual glycosylation sites are recovered.
7841792	1	66	theme	glycosylated	264:275	arg1	residue					277:283	each glycosylated residue	259:283	each glycosylated residue	259:283	The characterization of site-specific glycosylation is traditionally dependent on the availability of suitable proteolytic cleavage sites between each glycosylated residue, so that peptides containing individual glycosylation sites are recovered.
7841792	2	67	theme	protease	463:470	arg1	sites					472:476	no available protease sites	450:476	no available protease sites	450:476	In the case of heavily glycosylated domains such as the O-glycosylated mucins, which have no available protease sites, this approach is not possible.
7841792	6	68	attach	attached	1134:1141	arg2	stable					1157:1162	stable	1157:1162	stable	1157:1162	Comparison between an endoproteinase Glu-C glycopeptide and a tryptic glycopeptide showed that the oligosaccharide attached to Asn494 was stable after at least 10 cycles of Edman degradation.
7841792	6	68	attach	attached	1134:1141	arg1	Asn494					1146:1151	Asn494	1146:1151	Asn494	1146:1151	Comparison between an endoproteinase Glu-C glycopeptide and a tryptic glycopeptide showed that the oligosaccharide attached to Asn494 was stable after at least 10 cycles of Edman degradation.
7841792	6	68	attach	attached	1134:1141	arg2	oligosaccharide					1118:1132	the oligosaccharide	1114:1132	the oligosaccharide attached to Asn494	1114:1151	Comparison between an endoproteinase Glu-C glycopeptide and a tryptic glycopeptide showed that the oligosaccharide attached to Asn494 was stable after at least 10 cycles of Edman degradation.
7841792	4	69	theme	glycosylated	705:716	arg1	PTH-Asn					718:724	glycosylated PTH-Asn	705:724	glycosylated PTH-Asn	705:724	Using a model glycopeptide from a mutant human albumin Casebrook, glycosylated PTH-Asn was recovered after sequential solid-phase Edman degradation, subjected to acid hydrolysis and the sugars were identified by high performance anion exchange chromatography with pulsed amperometric detection.
7841792	6	70	theme	tryptic	1081:1087	arg1	glycopeptide					1089:1100	a tryptic glycopeptide	1079:1100	a tryptic glycopeptide	1079:1100	Comparison between an endoproteinase Glu-C glycopeptide and a tryptic glycopeptide showed that the oligosaccharide attached to Asn494 was stable after at least 10 cycles of Edman degradation.
9278435	3	0	from	each	567:570	arg1	oligosaccharides					512:527	the oligosaccharides	508:527	the oligosaccharides of recombinant alpha-L-iduronidase at each of its six N-glycosylation sites	508:603	Because of the importance of carbohydrate residues for endocytosis and lysosomal targeting, we examined the oligosaccharides of recombinant alpha-L-iduronidase at each of its six N-glycosylation sites.
9278435	7	1	theme	mixed	1535:1539	arg1	mannose					1546:1552	mixed high mannose	1535:1552	mixed high mannose	1535:1552	The major oligosaccharide structures found at each site were as follows: Asn-110, complex; Asn-190, complex; Asn-336, bisphosphorylated (P2Man7GlcNAc2); Asn-372, high mannose (mainly Man9GlcNAc2, some of which was monoglucosylated); Asn-415, mixed high mannose and complex; Asn-451, bisphosphorylated (P2Man7GlcNAc2).
9278435	2	2	theme	cell	327:330	arg1	line					332:335	an overexpressing Chinese hamster ovary cell line	287:335	an overexpressing Chinese hamster ovary cell line	287:335	Recombinant human alpha-L-iduronidase, isolated from secretions of an overexpressing Chinese hamster ovary cell line, is potentially useful for replacement therapy of these disorders.
9278435	5	3	theme	molecular	1013:1021	arg1	mass					1023:1026	their molecular mass	1007:1026	their molecular mass	1007:1026	For structural analysis, tryptic and chymotryptic glycopeptides were isolated by lectin binding and reverse phase high pressure liquid chromatography; their molecular mass was determined by matrix-assisted laser desorption-time of flight mass spectrometry before and after treatment with endo- or exoglycosidases or with alkaline phosphatase.
9278435	4	4	theme	endo-beta-N-acetylglucosaminidase	726:758	arg1	H					760:760	endo-beta-N-acetylglucosaminidase H	726:760	endo-beta-N-acetylglucosaminidase H	726:760	Biosynthetic radiolabeling showed that three or four of the six oligosaccharides of the secreted enzyme were cleaved by endo-beta-N-acetylglucosaminidase H, with phosphate present on the sensitive oligosaccharides and L-fucose on the resistant ones.
9278435	2	5	theme	hamster	313:319	arg1	line					332:335	an overexpressing Chinese hamster ovary cell line	287:335	an overexpressing Chinese hamster ovary cell line	287:335	Recombinant human alpha-L-iduronidase, isolated from secretions of an overexpressing Chinese hamster ovary cell line, is potentially useful for replacement therapy of these disorders.
9278435	5	6	theme	phase	964:968	arg1	chromatography					991:1004	reverse phase high pressure liquid chromatography	956:1004	reverse phase high pressure liquid chromatography	956:1004	For structural analysis, tryptic and chymotryptic glycopeptides were isolated by lectin binding and reverse phase high pressure liquid chromatography; their molecular mass was determined by matrix-assisted laser desorption-time of flight mass spectrometry before and after treatment with endo- or exoglycosidases or with alkaline phosphatase.
9278435	5	7	theme	pressure	975:982	arg1	chromatography					991:1004	reverse phase high pressure liquid chromatography	956:1004	reverse phase high pressure liquid chromatography	956:1004	For structural analysis, tryptic and chymotryptic glycopeptides were isolated by lectin binding and reverse phase high pressure liquid chromatography; their molecular mass was determined by matrix-assisted laser desorption-time of flight mass spectrometry before and after treatment with endo- or exoglycosidases or with alkaline phosphatase.
9278435	9	8	theme	carbohydrate	1828:1839	arg1	structures					1841:1850	carbohydrate structures	1828:1850	carbohydrate structures	1828:1850	The heterogeneity of carbohydrate structures must represent the accessibility of the glycosylation sites as well as the processing capability of the overexpressing Chinese hamster ovary cells.
9278435	4	9	theme	enzyme	703:708	arg1	oligosaccharides					670:685	the six oligosaccharides	662:685	the six oligosaccharides of the secreted enzyme	662:708	Biosynthetic radiolabeling showed that three or four of the six oligosaccharides of the secreted enzyme were cleaved by endo-beta-N-acetylglucosaminidase H, with phosphate present on the sensitive oligosaccharides and L-fucose on the resistant ones.
9278435	5	10	theme	lectin	937:942	arg1	binding					944:950	lectin binding	937:950	lectin binding	937:950	For structural analysis, tryptic and chymotryptic glycopeptides were isolated by lectin binding and reverse phase high pressure liquid chromatography; their molecular mass was determined by matrix-assisted laser desorption-time of flight mass spectrometry before and after treatment with endo- or exoglycosidases or with alkaline phosphatase.
9278435	7	11	theme	oligosaccharide	1303:1317	arg1	structures					1319:1328	The major oligosaccharide structures	1293:1328	The major oligosaccharide structures found at each site	1293:1347	The major oligosaccharide structures found at each site were as follows: Asn-110, complex; Asn-190, complex; Asn-336, bisphosphorylated (P2Man7GlcNAc2); Asn-372, high mannose (mainly Man9GlcNAc2, some of which was monoglucosylated); Asn-415, mixed high mannose and complex; Asn-451, bisphosphorylated (P2Man7GlcNAc2).
9278435	7	12	dep	Man9GlcNAc2	1476:1486	arg1	mainly					1469:1474	mainly	1469:1474	mainly	1469:1474	The major oligosaccharide structures found at each site were as follows: Asn-110, complex; Asn-190, complex; Asn-336, bisphosphorylated (P2Man7GlcNAc2); Asn-372, high mannose (mainly Man9GlcNAc2, some of which was monoglucosylated); Asn-415, mixed high mannose and complex; Asn-451, bisphosphorylated (P2Man7GlcNAc2).
9278435	4	13	theme	sensitive	793:801	arg1	oligosaccharides					803:818	the sensitive oligosaccharides	789:818	the sensitive oligosaccharides	789:818	Biosynthetic radiolabeling showed that three or four of the six oligosaccharides of the secreted enzyme were cleaved by endo-beta-N-acetylglucosaminidase H, with phosphate present on the sensitive oligosaccharides and L-fucose on the resistant ones.
9278435	5	14	theme	alkaline	1177:1184	arg1	phosphatase					1186:1196	alkaline phosphatase	1177:1196	alkaline phosphatase	1177:1196	For structural analysis, tryptic and chymotryptic glycopeptides were isolated by lectin binding and reverse phase high pressure liquid chromatography; their molecular mass was determined by matrix-assisted laser desorption-time of flight mass spectrometry before and after treatment with endo- or exoglycosidases or with alkaline phosphatase.
9278435	2	15	theme	overexpressing	290:303	arg1	line					332:335	an overexpressing Chinese hamster ovary cell line	287:335	an overexpressing Chinese hamster ovary cell line	287:335	Recombinant human alpha-L-iduronidase, isolated from secretions of an overexpressing Chinese hamster ovary cell line, is potentially useful for replacement therapy of these disorders.
9278435	9	16	theme	glycosylation	1892:1904	arg1	sites					1906:1910	the glycosylation sites	1888:1910	the glycosylation sites	1888:1910	The heterogeneity of carbohydrate structures must represent the accessibility of the glycosylation sites as well as the processing capability of the overexpressing Chinese hamster ovary cells.
9278435	4	17	theme	phosphate	768:776	arg1	present					778:784	phosphate present	768:784	phosphate present on the sensitive oligosaccharides	768:818	Biosynthetic radiolabeling showed that three or four of the six oligosaccharides of the secreted enzyme were cleaved by endo-beta-N-acetylglucosaminidase H, with phosphate present on the sensitive oligosaccharides and L-fucose on the resistant ones.
9278435	0	18	theme	Chinese	77:83	arg1	cells					99:103	Chinese hamster ovary cells	77:103	Chinese hamster ovary cells	77:103	Carbohydrate structures of recombinant human alpha-L-iduronidase secreted by Chinese hamster ovary cells.
9278435	8	19	gly	glycopeptide	1623:1634	arg2	resistant					1653:1661	resistant	1653:1661	resistant	1653:1661	The Asn-451 glycopeptide was unexpectedly resistant to digestion by N-glycanase unless first dephosphorylated, but it was sensitive to endo-beta-N-acetylglucosaminidase H and to glycopeptidase A.
9278435	8	19	gly	glycopeptide	1623:1634	arg2	glycopeptide					1623:1634	The Asn-451 glycopeptide	1611:1634	The Asn-451 glycopeptide	1611:1634	The Asn-451 glycopeptide was unexpectedly resistant to digestion by N-glycanase unless first dephosphorylated, but it was sensitive to endo-beta-N-acetylglucosaminidase H and to glycopeptidase A.
9278435	0	20	theme	ovary	93:97	arg1	cells					99:103	Chinese hamster ovary cells	77:103	Chinese hamster ovary cells	77:103	Carbohydrate structures of recombinant human alpha-L-iduronidase secreted by Chinese hamster ovary cells.
9278435	1	21	from	deficient	159:167	arg1	syndrome					179:186	Hurler syndrome	172:186	Hurler syndrome	172:186	alpha-L-Iduronidase is a lysosomal hydrolase that is deficient in Hurler syndrome and clinically milder variants.
9278435	5	22	theme	flight	1087:1092	arg1	spectrometry					1099:1110	flight mass spectrometry	1087:1110	flight mass spectrometry	1087:1110	For structural analysis, tryptic and chymotryptic glycopeptides were isolated by lectin binding and reverse phase high pressure liquid chromatography; their molecular mass was determined by matrix-assisted laser desorption-time of flight mass spectrometry before and after treatment with endo- or exoglycosidases or with alkaline phosphatase.
9278435	2	23	attach	isolated	259:266	arg2	alpha-L-iduronidase					238:256	Recombinant human alpha-L-iduronidase	220:256	Recombinant human alpha-L-iduronidase	220:256	Recombinant human alpha-L-iduronidase, isolated from secretions of an overexpressing Chinese hamster ovary cell line, is potentially useful for replacement therapy of these disorders.
9278435	2	23	attach	isolated	259:266	arg1	secretions					273:282	secretions	273:282	secretions of an overexpressing Chinese hamster ovary cell line	273:335	Recombinant human alpha-L-iduronidase, isolated from secretions of an overexpressing Chinese hamster ovary cell line, is potentially useful for replacement therapy of these disorders.
9278435	9	24	theme	processing	1927:1936	arg1	capability					1938:1947	the processing capability	1923:1947	the accessibility of the glycosylation sites as well as the processing capability of the overexpressing Chinese hamster ovary cells	1867:1997	The heterogeneity of carbohydrate structures must represent the accessibility of the glycosylation sites as well as the processing capability of the overexpressing Chinese hamster ovary cells.
9278435	8	25	theme	Asn-451	1615:1621	arg1	glycopeptide					1623:1634	The Asn-451 glycopeptide	1611:1634	The Asn-451 glycopeptide	1611:1634	The Asn-451 glycopeptide was unexpectedly resistant to digestion by N-glycanase unless first dephosphorylated, but it was sensitive to endo-beta-N-acetylglucosaminidase H and to glycopeptidase A.
9278435	8	25	theme	Asn-451	1615:1621	arg1	resistant					1653:1661	resistant	1653:1661	resistant	1653:1661	The Asn-451 glycopeptide was unexpectedly resistant to digestion by N-glycanase unless first dephosphorylated, but it was sensitive to endo-beta-N-acetylglucosaminidase H and to glycopeptidase A.
9278435	5	26	theme	spectrometry	1099:1110	arg1	desorption-time					1068:1082	matrix-assisted laser desorption-time	1046:1082	matrix-assisted laser desorption-time of flight mass spectrometry	1046:1110	For structural analysis, tryptic and chymotryptic glycopeptides were isolated by lectin binding and reverse phase high pressure liquid chromatography; their molecular mass was determined by matrix-assisted laser desorption-time of flight mass spectrometry before and after treatment with endo- or exoglycosidases or with alkaline phosphatase.
9278435	7	27	theme	high	1455:1458	arg1	mannose					1460:1466	high mannose	1455:1466	high mannose (mainly Man9GlcNAc2, some of which was monoglucosylated)	1455:1523	The major oligosaccharide structures found at each site were as follows: Asn-110, complex; Asn-190, complex; Asn-336, bisphosphorylated (P2Man7GlcNAc2); Asn-372, high mannose (mainly Man9GlcNAc2, some of which was monoglucosylated); Asn-415, mixed high mannose and complex; Asn-451, bisphosphorylated (P2Man7GlcNAc2).
9278435	7	27	theme	high	1455:1458	arg1	Asn-336					1402:1408	Asn-336	1402:1408	Asn-336	1402:1408	The major oligosaccharide structures found at each site were as follows: Asn-110, complex; Asn-190, complex; Asn-336, bisphosphorylated (P2Man7GlcNAc2); Asn-372, high mannose (mainly Man9GlcNAc2, some of which was monoglucosylated); Asn-415, mixed high mannose and complex; Asn-451, bisphosphorylated (P2Man7GlcNAc2).
9278435	0	28	theme	Carbohydrate	0:11	arg1	structures					13:22	Carbohydrate structures	0:22	Carbohydrate structures of recombinant human alpha-L-iduronidase	0:63	Carbohydrate structures of recombinant human alpha-L-iduronidase secreted by Chinese hamster ovary cells.
9278435	5	29	theme	matrix-assisted	1046:1060	arg1	desorption-time					1068:1082	matrix-assisted laser desorption-time	1046:1082	matrix-assisted laser desorption-time of flight mass spectrometry	1046:1110	For structural analysis, tryptic and chymotryptic glycopeptides were isolated by lectin binding and reverse phase high pressure liquid chromatography; their molecular mass was determined by matrix-assisted laser desorption-time of flight mass spectrometry before and after treatment with endo- or exoglycosidases or with alkaline phosphatase.
9278435	9	30	theme	overexpressing	1956:1969	arg1	cells					1993:1997	the overexpressing Chinese hamster ovary cells	1952:1997	the overexpressing Chinese hamster ovary cells	1952:1997	The heterogeneity of carbohydrate structures must represent the accessibility of the glycosylation sites as well as the processing capability of the overexpressing Chinese hamster ovary cells.
9278435	4	31	theme	resistant	840:848	arg1	ones					850:853	the resistant ones	836:853	the resistant ones	836:853	Biosynthetic radiolabeling showed that three or four of the six oligosaccharides of the secreted enzyme were cleaved by endo-beta-N-acetylglucosaminidase H, with phosphate present on the sensitive oligosaccharides and L-fucose on the resistant ones.
9278435	3	32	theme	N-glycosylation	583:597	arg1	sites					599:603	its six N-glycosylation sites	575:603	its six N-glycosylation sites	575:603	Because of the importance of carbohydrate residues for endocytosis and lysosomal targeting, we examined the oligosaccharides of recombinant alpha-L-iduronidase at each of its six N-glycosylation sites.
9278435	9	33	theme	hamster	1979:1985	arg1	cells					1993:1997	the overexpressing Chinese hamster ovary cells	1952:1997	the overexpressing Chinese hamster ovary cells	1952:1997	The heterogeneity of carbohydrate structures must represent the accessibility of the glycosylation sites as well as the processing capability of the overexpressing Chinese hamster ovary cells.
9278435	5	34	gly	glycopeptides	906:918	arg2	glycopeptides					906:918	tryptic and chymotryptic glycopeptides	881:918	tryptic and chymotryptic glycopeptides	881:918	For structural analysis, tryptic and chymotryptic glycopeptides were isolated by lectin binding and reverse phase high pressure liquid chromatography; their molecular mass was determined by matrix-assisted laser desorption-time of flight mass spectrometry before and after treatment with endo- or exoglycosidases or with alkaline phosphatase.
9278435	0	35	theme	human	39:43	arg1	alpha-L-iduronidase					45:63	recombinant human alpha-L-iduronidase	27:63	recombinant human alpha-L-iduronidase	27:63	Carbohydrate structures of recombinant human alpha-L-iduronidase secreted by Chinese hamster ovary cells.
9278435	7	36	theme	major	1297:1301	arg1	structures					1319:1328	The major oligosaccharide structures	1293:1328	The major oligosaccharide structures found at each site	1293:1347	The major oligosaccharide structures found at each site were as follows: Asn-110, complex; Asn-190, complex; Asn-336, bisphosphorylated (P2Man7GlcNAc2); Asn-372, high mannose (mainly Man9GlcNAc2, some of which was monoglucosylated); Asn-415, mixed high mannose and complex; Asn-451, bisphosphorylated (P2Man7GlcNAc2).
9278435	9	37	theme	cells	1993:1997	arg1	accessibility					1871:1883	the accessibility	1867:1883	the accessibility of the glycosylation sites as well as the processing capability of the overexpressing Chinese hamster ovary cells	1867:1997	The heterogeneity of carbohydrate structures must represent the accessibility of the glycosylation sites as well as the processing capability of the overexpressing Chinese hamster ovary cells.
9278435	9	37	theme	cells	1993:1997	arg1	capability					1938:1947	the processing capability	1923:1947	the accessibility of the glycosylation sites as well as the processing capability of the overexpressing Chinese hamster ovary cells	1867:1997	The heterogeneity of carbohydrate structures must represent the accessibility of the glycosylation sites as well as the processing capability of the overexpressing Chinese hamster ovary cells.
9278435	3	38	theme	alpha-L-iduronidase	544:562	arg1	oligosaccharides					512:527	the oligosaccharides	508:527	the oligosaccharides of recombinant alpha-L-iduronidase at each of its six N-glycosylation sites	508:603	Because of the importance of carbohydrate residues for endocytosis and lysosomal targeting, we examined the oligosaccharides of recombinant alpha-L-iduronidase at each of its six N-glycosylation sites.
9278435	6	39	theme	carboxyl-terminal	1256:1272	arg1	analysis					1283:1290	amino- or carboxyl-terminal sequence analysis	1246:1290	amino- or carboxyl-terminal sequence analysis	1246:1290	Identification of the peptides was assisted by amino- or carboxyl-terminal sequence analysis.
9278435	7	40	dep	were	1349:1352	arg1	complex					1375:1381	complex	1375:1381	complex	1375:1381	The major oligosaccharide structures found at each site were as follows: Asn-110, complex; Asn-190, complex; Asn-336, bisphosphorylated (P2Man7GlcNAc2); Asn-372, high mannose (mainly Man9GlcNAc2, some of which was monoglucosylated); Asn-415, mixed high mannose and complex; Asn-451, bisphosphorylated (P2Man7GlcNAc2).
9278435	7	40	dep	were	1349:1352	arg1	Asn-190					1384:1390	Asn-190	1384:1390	Asn-190	1384:1390	The major oligosaccharide structures found at each site were as follows: Asn-110, complex; Asn-190, complex; Asn-336, bisphosphorylated (P2Man7GlcNAc2); Asn-372, high mannose (mainly Man9GlcNAc2, some of which was monoglucosylated); Asn-415, mixed high mannose and complex; Asn-451, bisphosphorylated (P2Man7GlcNAc2).
9278435	7	40	dep	were	1349:1352	arg1	bisphosphorylated					1576:1592	bisphosphorylated	1576:1592	bisphosphorylated	1576:1592	The major oligosaccharide structures found at each site were as follows: Asn-110, complex; Asn-190, complex; Asn-336, bisphosphorylated (P2Man7GlcNAc2); Asn-372, high mannose (mainly Man9GlcNAc2, some of which was monoglucosylated); Asn-415, mixed high mannose and complex; Asn-451, bisphosphorylated (P2Man7GlcNAc2).
9278435	7	40	dep	were	1349:1352	arg1	bisphosphorylated					1411:1427	bisphosphorylated	1411:1427	bisphosphorylated	1411:1427	The major oligosaccharide structures found at each site were as follows: Asn-110, complex; Asn-190, complex; Asn-336, bisphosphorylated (P2Man7GlcNAc2); Asn-372, high mannose (mainly Man9GlcNAc2, some of which was monoglucosylated); Asn-415, mixed high mannose and complex; Asn-451, bisphosphorylated (P2Man7GlcNAc2).
9278435	7	40	dep	were	1349:1352	arg1	mannose					1460:1466	high mannose	1455:1466	high mannose (mainly Man9GlcNAc2, some of which was monoglucosylated)	1455:1523	The major oligosaccharide structures found at each site were as follows: Asn-110, complex; Asn-190, complex; Asn-336, bisphosphorylated (P2Man7GlcNAc2); Asn-372, high mannose (mainly Man9GlcNAc2, some of which was monoglucosylated); Asn-415, mixed high mannose and complex; Asn-451, bisphosphorylated (P2Man7GlcNAc2).
9278435	7	40	dep	were	1349:1352	arg1	Asn-110					1366:1372	Asn-110	1366:1372	Asn-110	1366:1372	The major oligosaccharide structures found at each site were as follows: Asn-110, complex; Asn-190, complex; Asn-336, bisphosphorylated (P2Man7GlcNAc2); Asn-372, high mannose (mainly Man9GlcNAc2, some of which was monoglucosylated); Asn-415, mixed high mannose and complex; Asn-451, bisphosphorylated (P2Man7GlcNAc2).
9278435	7	40	dep	were	1349:1352	arg1	complex					1393:1399	complex	1393:1399	complex	1393:1399	The major oligosaccharide structures found at each site were as follows: Asn-110, complex; Asn-190, complex; Asn-336, bisphosphorylated (P2Man7GlcNAc2); Asn-372, high mannose (mainly Man9GlcNAc2, some of which was monoglucosylated); Asn-415, mixed high mannose and complex; Asn-451, bisphosphorylated (P2Man7GlcNAc2).
9278435	7	40	dep	were	1349:1352	arg1	Asn-336					1402:1408	Asn-336	1402:1408	Asn-336	1402:1408	The major oligosaccharide structures found at each site were as follows: Asn-110, complex; Asn-190, complex; Asn-336, bisphosphorylated (P2Man7GlcNAc2); Asn-372, high mannose (mainly Man9GlcNAc2, some of which was monoglucosylated); Asn-415, mixed high mannose and complex; Asn-451, bisphosphorylated (P2Man7GlcNAc2).
9278435	2	41	theme	human	232:236	arg1	alpha-L-iduronidase					238:256	Recombinant human alpha-L-iduronidase	220:256	Recombinant human alpha-L-iduronidase	220:256	Recombinant human alpha-L-iduronidase, isolated from secretions of an overexpressing Chinese hamster ovary cell line, is potentially useful for replacement therapy of these disorders.
9278435	2	42	theme	replacement	364:374	arg1	therapy					376:382	replacement therapy	364:382	replacement therapy of these disorders	364:401	Recombinant human alpha-L-iduronidase, isolated from secretions of an overexpressing Chinese hamster ovary cell line, is potentially useful for replacement therapy of these disorders.
9278435	6	43	theme	amino-	1246:1251	arg1	analysis					1283:1290	amino- or carboxyl-terminal sequence analysis	1246:1290	amino- or carboxyl-terminal sequence analysis	1246:1290	Identification of the peptides was assisted by amino- or carboxyl-terminal sequence analysis.
9278435	8	44	theme	glycopeptidase	1789:1802	arg1	A					1804:1804	glycopeptidase A	1789:1804	glycopeptidase A	1789:1804	The Asn-451 glycopeptide was unexpectedly resistant to digestion by N-glycanase unless first dephosphorylated, but it was sensitive to endo-beta-N-acetylglucosaminidase H and to glycopeptidase A.
9278435	3	45	theme	carbohydrate	433:444	arg1	residues					446:453	carbohydrate residues	433:453	carbohydrate residues	433:453	Because of the importance of carbohydrate residues for endocytosis and lysosomal targeting, we examined the oligosaccharides of recombinant alpha-L-iduronidase at each of its six N-glycosylation sites.
9278435	2	46	theme	disorders	393:401	arg1	therapy					376:382	replacement therapy	364:382	replacement therapy of these disorders	364:401	Recombinant human alpha-L-iduronidase, isolated from secretions of an overexpressing Chinese hamster ovary cell line, is potentially useful for replacement therapy of these disorders.
9278435	4	47	from	present	778:784	arg1	oligosaccharides					803:818	the sensitive oligosaccharides	789:818	the sensitive oligosaccharides	789:818	Biosynthetic radiolabeling showed that three or four of the six oligosaccharides of the secreted enzyme were cleaved by endo-beta-N-acetylglucosaminidase H, with phosphate present on the sensitive oligosaccharides and L-fucose on the resistant ones.
9278435	4	47	from	present	778:784	arg1	ones					850:853	the resistant ones	836:853	the resistant ones	836:853	Biosynthetic radiolabeling showed that three or four of the six oligosaccharides of the secreted enzyme were cleaved by endo-beta-N-acetylglucosaminidase H, with phosphate present on the sensitive oligosaccharides and L-fucose on the resistant ones.
9278435	6	48	theme	peptides	1221:1228	arg1	Identification					1199:1212	Identification	1199:1212	Identification of the peptides	1199:1228	Identification of the peptides was assisted by amino- or carboxyl-terminal sequence analysis.
9278435	2	49	theme	line	332:335	arg1	secretions					273:282	secretions	273:282	secretions of an overexpressing Chinese hamster ovary cell line	273:335	Recombinant human alpha-L-iduronidase, isolated from secretions of an overexpressing Chinese hamster ovary cell line, is potentially useful for replacement therapy of these disorders.
9278435	9	50	gly	heterogeneity	1811:1823	arg1	structures					1841:1850	carbohydrate structures	1828:1850	carbohydrate structures	1828:1850	The heterogeneity of carbohydrate structures must represent the accessibility of the glycosylation sites as well as the processing capability of the overexpressing Chinese hamster ovary cells.
9278435	7	51	theme	high	1541:1544	arg1	mannose					1546:1552	mixed high mannose	1535:1552	mixed high mannose	1535:1552	The major oligosaccharide structures found at each site were as follows: Asn-110, complex; Asn-190, complex; Asn-336, bisphosphorylated (P2Man7GlcNAc2); Asn-372, high mannose (mainly Man9GlcNAc2, some of which was monoglucosylated); Asn-415, mixed high mannose and complex; Asn-451, bisphosphorylated (P2Man7GlcNAc2).
9278435	8	52	theme	endo-beta-N-acetylglucosaminidase	1746:1778	arg1	H					1780:1780	endo-beta-N-acetylglucosaminidase H	1746:1780	endo-beta-N-acetylglucosaminidase H	1746:1780	The Asn-451 glycopeptide was unexpectedly resistant to digestion by N-glycanase unless first dephosphorylated, but it was sensitive to endo-beta-N-acetylglucosaminidase H and to glycopeptidase A.
9278435	2	53	theme	ovary	321:325	arg1	line					332:335	an overexpressing Chinese hamster ovary cell line	287:335	an overexpressing Chinese hamster ovary cell line	287:335	Recombinant human alpha-L-iduronidase, isolated from secretions of an overexpressing Chinese hamster ovary cell line, is potentially useful for replacement therapy of these disorders.
9278435	1	54	theme	milder	203:208	arg1	variants					210:217	milder variants	203:217	milder variants	203:217	alpha-L-Iduronidase is a lysosomal hydrolase that is deficient in Hurler syndrome and clinically milder variants.
9278435	5	55	theme	reverse	956:962	arg1	chromatography					991:1004	reverse phase high pressure liquid chromatography	956:1004	reverse phase high pressure liquid chromatography	956:1004	For structural analysis, tryptic and chymotryptic glycopeptides were isolated by lectin binding and reverse phase high pressure liquid chromatography; their molecular mass was determined by matrix-assisted laser desorption-time of flight mass spectrometry before and after treatment with endo- or exoglycosidases or with alkaline phosphatase.
9278435	5	56	theme	structural	860:869	arg1	analysis					871:878	structural analysis	860:878	structural analysis	860:878	For structural analysis, tryptic and chymotryptic glycopeptides were isolated by lectin binding and reverse phase high pressure liquid chromatography; their molecular mass was determined by matrix-assisted laser desorption-time of flight mass spectrometry before and after treatment with endo- or exoglycosidases or with alkaline phosphatase.
9278435	7	57	located	found	1330:1334	arg2	structures					1319:1328	The major oligosaccharide structures	1293:1328	The major oligosaccharide structures found at each site	1293:1347	The major oligosaccharide structures found at each site were as follows: Asn-110, complex; Asn-190, complex; Asn-336, bisphosphorylated (P2Man7GlcNAc2); Asn-372, high mannose (mainly Man9GlcNAc2, some of which was monoglucosylated); Asn-415, mixed high mannose and complex; Asn-451, bisphosphorylated (P2Man7GlcNAc2).
9278435	7	57	located	found	1330:1334	arg1	site					1344:1347	each site	1339:1347	each site	1339:1347	The major oligosaccharide structures found at each site were as follows: Asn-110, complex; Asn-190, complex; Asn-336, bisphosphorylated (P2Man7GlcNAc2); Asn-372, high mannose (mainly Man9GlcNAc2, some of which was monoglucosylated); Asn-415, mixed high mannose and complex; Asn-451, bisphosphorylated (P2Man7GlcNAc2).
9278435	5	58	theme	high	970:973	arg1	chromatography					991:1004	reverse phase high pressure liquid chromatography	956:1004	reverse phase high pressure liquid chromatography	956:1004	For structural analysis, tryptic and chymotryptic glycopeptides were isolated by lectin binding and reverse phase high pressure liquid chromatography; their molecular mass was determined by matrix-assisted laser desorption-time of flight mass spectrometry before and after treatment with endo- or exoglycosidases or with alkaline phosphatase.
9278435	7	59	dep	mannose	1460:1466	arg1	Man9GlcNAc2					1476:1486	Man9GlcNAc2	1476:1486	Man9GlcNAc2	1476:1486	The major oligosaccharide structures found at each site were as follows: Asn-110, complex; Asn-190, complex; Asn-336, bisphosphorylated (P2Man7GlcNAc2); Asn-372, high mannose (mainly Man9GlcNAc2, some of which was monoglucosylated); Asn-415, mixed high mannose and complex; Asn-451, bisphosphorylated (P2Man7GlcNAc2).
9278435	9	60	theme	structures	1841:1850	arg1	heterogeneity					1811:1823	The heterogeneity	1807:1823	The heterogeneity of carbohydrate structures	1807:1850	The heterogeneity of carbohydrate structures must represent the accessibility of the glycosylation sites as well as the processing capability of the overexpressing Chinese hamster ovary cells.
9278435	4	61	theme	secreted	694:701	arg1	enzyme					703:708	the secreted enzyme	690:708	the secreted enzyme	690:708	Biosynthetic radiolabeling showed that three or four of the six oligosaccharides of the secreted enzyme were cleaved by endo-beta-N-acetylglucosaminidase H, with phosphate present on the sensitive oligosaccharides and L-fucose on the resistant ones.
9278435	9	62	gly	glycosylation	1892:1904	arg2	sites					1906:1910	the glycosylation sites	1888:1910	the glycosylation sites	1888:1910	The heterogeneity of carbohydrate structures must represent the accessibility of the glycosylation sites as well as the processing capability of the overexpressing Chinese hamster ovary cells.
9278435	1	63	theme	lysosomal	131:139	arg1	alpha-L-Iduronidase					106:124	alpha-L-Iduronidase	106:124	alpha-L-Iduronidase	106:124	alpha-L-Iduronidase is a lysosomal hydrolase that is deficient in Hurler syndrome and clinically milder variants.
9278435	1	63	theme	lysosomal	131:139	arg1	hydrolase					141:149	a lysosomal hydrolase	129:149	a lysosomal hydrolase that is deficient in Hurler syndrome and clinically milder variants	129:217	alpha-L-Iduronidase is a lysosomal hydrolase that is deficient in Hurler syndrome and clinically milder variants.
9278435	1	63	theme	lysosomal	131:139	arg1	deficient					159:167	deficient	159:167	deficient	159:167	alpha-L-Iduronidase is a lysosomal hydrolase that is deficient in Hurler syndrome and clinically milder variants.
9278435	2	64	theme	Chinese	305:311	arg1	line					332:335	an overexpressing Chinese hamster ovary cell line	287:335	an overexpressing Chinese hamster ovary cell line	287:335	Recombinant human alpha-L-iduronidase, isolated from secretions of an overexpressing Chinese hamster ovary cell line, is potentially useful for replacement therapy of these disorders.
9278435	0	65	theme	hamster	85:91	arg1	cells					99:103	Chinese hamster ovary cells	77:103	Chinese hamster ovary cells	77:103	Carbohydrate structures of recombinant human alpha-L-iduronidase secreted by Chinese hamster ovary cells.
9278435	5	66	theme	liquid	984:989	arg1	chromatography					991:1004	reverse phase high pressure liquid chromatography	956:1004	reverse phase high pressure liquid chromatography	956:1004	For structural analysis, tryptic and chymotryptic glycopeptides were isolated by lectin binding and reverse phase high pressure liquid chromatography; their molecular mass was determined by matrix-assisted laser desorption-time of flight mass spectrometry before and after treatment with endo- or exoglycosidases or with alkaline phosphatase.
9278435	9	67	theme	sites	1906:1910	arg1	accessibility					1871:1883	the accessibility	1867:1883	the accessibility of the glycosylation sites as well as the processing capability of the overexpressing Chinese hamster ovary cells	1867:1997	The heterogeneity of carbohydrate structures must represent the accessibility of the glycosylation sites as well as the processing capability of the overexpressing Chinese hamster ovary cells.
9278435	9	67	theme	sites	1906:1910	arg1	capability					1938:1947	the processing capability	1923:1947	the accessibility of the glycosylation sites as well as the processing capability of the overexpressing Chinese hamster ovary cells	1867:1997	The heterogeneity of carbohydrate structures must represent the accessibility of the glycosylation sites as well as the processing capability of the overexpressing Chinese hamster ovary cells.
9278435	1	68	theme	Hurler	172:177	arg1	syndrome					179:186	Hurler syndrome	172:186	Hurler syndrome	172:186	alpha-L-Iduronidase is a lysosomal hydrolase that is deficient in Hurler syndrome and clinically milder variants.
9278435	3	69	gly	N-glycosylation	583:597	arg2	six					579:581	six	579:581	six	579:581	Because of the importance of carbohydrate residues for endocytosis and lysosomal targeting, we examined the oligosaccharides of recombinant alpha-L-iduronidase at each of its six N-glycosylation sites.
9278435	3	69	gly	N-glycosylation	583:597	arg2	sites					599:603	its six N-glycosylation sites	575:603	its six N-glycosylation sites	575:603	Because of the importance of carbohydrate residues for endocytosis and lysosomal targeting, we examined the oligosaccharides of recombinant alpha-L-iduronidase at each of its six N-glycosylation sites.
9278435	1	70	from	syndrome	179:186	arg1	alpha-L-Iduronidase					106:124	alpha-L-Iduronidase	106:124	alpha-L-Iduronidase	106:124	alpha-L-Iduronidase is a lysosomal hydrolase that is deficient in Hurler syndrome and clinically milder variants.
9278435	1	70	from	syndrome	179:186	arg1	hydrolase					141:149	a lysosomal hydrolase	129:149	a lysosomal hydrolase that is deficient in Hurler syndrome and clinically milder variants	129:217	alpha-L-Iduronidase is a lysosomal hydrolase that is deficient in Hurler syndrome and clinically milder variants.
9278435	1	70	from	syndrome	179:186	arg1	deficient					159:167	deficient	159:167	deficient	159:167	alpha-L-Iduronidase is a lysosomal hydrolase that is deficient in Hurler syndrome and clinically milder variants.
9278435	7	71	dep	Asn-336	1402:1408	arg1	complex					1558:1564	complex	1558:1564	complex	1558:1564	The major oligosaccharide structures found at each site were as follows: Asn-110, complex; Asn-190, complex; Asn-336, bisphosphorylated (P2Man7GlcNAc2); Asn-372, high mannose (mainly Man9GlcNAc2, some of which was monoglucosylated); Asn-415, mixed high mannose and complex; Asn-451, bisphosphorylated (P2Man7GlcNAc2).
9278435	7	71	dep	Asn-336	1402:1408	arg1	Asn-372					1446:1452	Asn-372	1446:1452	Asn-372	1446:1452	The major oligosaccharide structures found at each site were as follows: Asn-110, complex; Asn-190, complex; Asn-336, bisphosphorylated (P2Man7GlcNAc2); Asn-372, high mannose (mainly Man9GlcNAc2, some of which was monoglucosylated); Asn-415, mixed high mannose and complex; Asn-451, bisphosphorylated (P2Man7GlcNAc2).
9278435	7	71	dep	Asn-336	1402:1408	arg1	mannose					1546:1552	mixed high mannose	1535:1552	mixed high mannose	1535:1552	The major oligosaccharide structures found at each site were as follows: Asn-110, complex; Asn-190, complex; Asn-336, bisphosphorylated (P2Man7GlcNAc2); Asn-372, high mannose (mainly Man9GlcNAc2, some of which was monoglucosylated); Asn-415, mixed high mannose and complex; Asn-451, bisphosphorylated (P2Man7GlcNAc2).
9278435	7	71	dep	Asn-336	1402:1408	arg1	Asn-415					1526:1532	Asn-415	1526:1532	Asn-415	1526:1532	The major oligosaccharide structures found at each site were as follows: Asn-110, complex; Asn-190, complex; Asn-336, bisphosphorylated (P2Man7GlcNAc2); Asn-372, high mannose (mainly Man9GlcNAc2, some of which was monoglucosylated); Asn-415, mixed high mannose and complex; Asn-451, bisphosphorylated (P2Man7GlcNAc2).
9278435	7	71	dep	Asn-336	1402:1408	arg1	Asn-451					1567:1573	Asn-451	1567:1573	Asn-451	1567:1573	The major oligosaccharide structures found at each site were as follows: Asn-110, complex; Asn-190, complex; Asn-336, bisphosphorylated (P2Man7GlcNAc2); Asn-372, high mannose (mainly Man9GlcNAc2, some of which was monoglucosylated); Asn-415, mixed high mannose and complex; Asn-451, bisphosphorylated (P2Man7GlcNAc2).
9278435	5	72	theme	chymotryptic	893:904	arg1	glycopeptides					906:918	tryptic and chymotryptic glycopeptides	881:918	tryptic and chymotryptic glycopeptides	881:918	For structural analysis, tryptic and chymotryptic glycopeptides were isolated by lectin binding and reverse phase high pressure liquid chromatography; their molecular mass was determined by matrix-assisted laser desorption-time of flight mass spectrometry before and after treatment with endo- or exoglycosidases or with alkaline phosphatase.
9278435	3	73	theme	lysosomal	475:483	arg1	targeting					485:493	lysosomal targeting	475:493	lysosomal targeting	475:493	Because of the importance of carbohydrate residues for endocytosis and lysosomal targeting, we examined the oligosaccharides of recombinant alpha-L-iduronidase at each of its six N-glycosylation sites.
9278435	0	74	theme	recombinant	27:37	arg1	alpha-L-iduronidase					45:63	recombinant human alpha-L-iduronidase	27:63	recombinant human alpha-L-iduronidase	27:63	Carbohydrate structures of recombinant human alpha-L-iduronidase secreted by Chinese hamster ovary cells.
9278435	4	75	from	L-fucose	824:831	arg1	oligosaccharides					803:818	the sensitive oligosaccharides	789:818	the sensitive oligosaccharides	789:818	Biosynthetic radiolabeling showed that three or four of the six oligosaccharides of the secreted enzyme were cleaved by endo-beta-N-acetylglucosaminidase H, with phosphate present on the sensitive oligosaccharides and L-fucose on the resistant ones.
9278435	4	75	from	L-fucose	824:831	arg1	ones					850:853	the resistant ones	836:853	the resistant ones	836:853	Biosynthetic radiolabeling showed that three or four of the six oligosaccharides of the secreted enzyme were cleaved by endo-beta-N-acetylglucosaminidase H, with phosphate present on the sensitive oligosaccharides and L-fucose on the resistant ones.
9278435	5	76	theme	laser	1062:1066	arg1	desorption-time					1068:1082	matrix-assisted laser desorption-time	1046:1082	matrix-assisted laser desorption-time of flight mass spectrometry	1046:1110	For structural analysis, tryptic and chymotryptic glycopeptides were isolated by lectin binding and reverse phase high pressure liquid chromatography; their molecular mass was determined by matrix-assisted laser desorption-time of flight mass spectrometry before and after treatment with endo- or exoglycosidases or with alkaline phosphatase.
9278435	9	77	theme	Chinese	1971:1977	arg1	cells					1993:1997	the overexpressing Chinese hamster ovary cells	1952:1997	the overexpressing Chinese hamster ovary cells	1952:1997	The heterogeneity of carbohydrate structures must represent the accessibility of the glycosylation sites as well as the processing capability of the overexpressing Chinese hamster ovary cells.
9278435	5	78	theme	mass	1094:1097	arg1	spectrometry					1099:1110	flight mass spectrometry	1087:1110	flight mass spectrometry	1087:1110	For structural analysis, tryptic and chymotryptic glycopeptides were isolated by lectin binding and reverse phase high pressure liquid chromatography; their molecular mass was determined by matrix-assisted laser desorption-time of flight mass spectrometry before and after treatment with endo- or exoglycosidases or with alkaline phosphatase.
9278435	0	79	theme	alpha-L-iduronidase	45:63	arg1	structures					13:22	Carbohydrate structures	0:22	Carbohydrate structures of recombinant human alpha-L-iduronidase	0:63	Carbohydrate structures of recombinant human alpha-L-iduronidase secreted by Chinese hamster ovary cells.
9278435	9	80	theme	ovary	1987:1991	arg1	cells					1993:1997	the overexpressing Chinese hamster ovary cells	1952:1997	the overexpressing Chinese hamster ovary cells	1952:1997	The heterogeneity of carbohydrate structures must represent the accessibility of the glycosylation sites as well as the processing capability of the overexpressing Chinese hamster ovary cells.
9278435	5	81	theme	tryptic	881:887	arg1	glycopeptides					906:918	tryptic and chymotryptic glycopeptides	881:918	tryptic and chymotryptic glycopeptides	881:918	For structural analysis, tryptic and chymotryptic glycopeptides were isolated by lectin binding and reverse phase high pressure liquid chromatography; their molecular mass was determined by matrix-assisted laser desorption-time of flight mass spectrometry before and after treatment with endo- or exoglycosidases or with alkaline phosphatase.
9278435	6	82	theme	sequence	1274:1281	arg1	analysis					1283:1290	amino- or carboxyl-terminal sequence analysis	1246:1290	amino- or carboxyl-terminal sequence analysis	1246:1290	Identification of the peptides was assisted by amino- or carboxyl-terminal sequence analysis.
9278435	3	83	theme	residues	446:453	arg1	importance					419:428	the importance	415:428	the importance of carbohydrate residues for endocytosis and lysosomal targeting	415:493	Because of the importance of carbohydrate residues for endocytosis and lysosomal targeting, we examined the oligosaccharides of recombinant alpha-L-iduronidase at each of its six N-glycosylation sites.
9278435	4	84	theme	Biosynthetic	606:617	arg1	radiolabeling					619:631	Biosynthetic radiolabeling	606:631	Biosynthetic radiolabeling	606:631	Biosynthetic radiolabeling showed that three or four of the six oligosaccharides of the secreted enzyme were cleaved by endo-beta-N-acetylglucosaminidase H, with phosphate present on the sensitive oligosaccharides and L-fucose on the resistant ones.
9278435	4	85	theme	oligosaccharides	670:685	arg1	oligosaccharides					670:685	the six oligosaccharides	662:685	the six oligosaccharides of the secreted enzyme	662:708	Biosynthetic radiolabeling showed that three or four of the six oligosaccharides of the secreted enzyme were cleaved by endo-beta-N-acetylglucosaminidase H, with phosphate present on the sensitive oligosaccharides and L-fucose on the resistant ones.
9278435	4	85	theme	oligosaccharides	670:685	arg1	three					645:649	three	645:649	three	645:649	Biosynthetic radiolabeling showed that three or four of the six oligosaccharides of the secreted enzyme were cleaved by endo-beta-N-acetylglucosaminidase H, with phosphate present on the sensitive oligosaccharides and L-fucose on the resistant ones.
9278435	2	86	theme	Recombinant	220:230	arg1	alpha-L-iduronidase					238:256	Recombinant human alpha-L-iduronidase	220:256	Recombinant human alpha-L-iduronidase	220:256	Recombinant human alpha-L-iduronidase, isolated from secretions of an overexpressing Chinese hamster ovary cell line, is potentially useful for replacement therapy of these disorders.
9278435	3	87	theme	recombinant	532:542	arg1	alpha-L-iduronidase					544:562	recombinant alpha-L-iduronidase	532:562	recombinant alpha-L-iduronidase	532:562	Because of the importance of carbohydrate residues for endocytosis and lysosomal targeting, we examined the oligosaccharides of recombinant alpha-L-iduronidase at each of its six N-glycosylation sites.
9278435	5	88	with	treatment	1129:1137	arg1	endo-					1144:1148	endo-	1144:1148	endo-	1144:1148	For structural analysis, tryptic and chymotryptic glycopeptides were isolated by lectin binding and reverse phase high pressure liquid chromatography; their molecular mass was determined by matrix-assisted laser desorption-time of flight mass spectrometry before and after treatment with endo- or exoglycosidases or with alkaline phosphatase.
9278435	5	88	with	treatment	1129:1137	arg1	phosphatase					1186:1196	alkaline phosphatase	1177:1196	alkaline phosphatase	1177:1196	For structural analysis, tryptic and chymotryptic glycopeptides were isolated by lectin binding and reverse phase high pressure liquid chromatography; their molecular mass was determined by matrix-assisted laser desorption-time of flight mass spectrometry before and after treatment with endo- or exoglycosidases or with alkaline phosphatase.
19909832	8	0	contain	had	1403:1405	arg1	glucosamine					1391:1401	glucosamine	1391:1401	glucosamine	1391:1401	Although glucosamine had no effect on furin mRNA levels, western blot of furin from glucosamine-treated cells suggested altered post-translational modification.
19909832	8	0	contain	had	1403:1405	arg2	effect					1410:1415	no effect	1407:1415	no effect	1407:1415	Although glucosamine had no effect on furin mRNA levels, western blot of furin from glucosamine-treated cells suggested altered post-translational modification.
19909832	10	1	theme	peptide	1700:1706	arg1	F					1720:1720	peptide N-glycanase F	1700:1720	peptide N-glycanase F	1700:1720	Recombinant furin treated with peptide N-glycanase F had reduced activity against a synthetic peptide substrate.
19909832	12	2	theme	ADAMTS5	2167:2173	arg1	activity					2155:2162	reduced aggrecanase activity	2135:2162	reduced aggrecanase activity of ADAMTS5	2135:2173	CONCLUSIONS: Ten mM glucosamine reduces excision of the ADAMTS5 propeptide via interference with post-translational modification of furin and leads to reduced aggrecanase activity of ADAMTS5.
19909832	5	3	from	Effects	755:761	arg1	processing					781:790	furin-mediated processing	766:790	furin-mediated processing of ADAMTS5 zymogen	766:809	Effects on furin-mediated processing of ADAMTS5 zymogen, and aggrecan processing by glucosamine-treated cells, were determined by western blotting.
19909832	6	4	theme	mutants	973:979	arg1	modification					922:933	Post-translational modification	903:933	Post-translational modification of furin and N-glycan deficient furin mutants generated by site-directed mutagenesis	903:1018	Post-translational modification of furin and N-glycan deficient furin mutants generated by site-directed mutagenesis was analyzed by western blotting, and the mutants were evaluated for their ADAMTS5 processing ability in furin-deficient CHO-RPE.40 cells.
19909832	4	5	theme	FURIN	695:699	arg1	transcription					701:713	FURIN transcription	695:713	FURIN transcription	695:713	Glucosamine effects on FURIN transcription were determined by quantitative RT-PCR.
19909832	10	6	theme	reduced	1726:1732	arg1	activity					1734:1741	reduced activity	1726:1741	reduced activity against a synthetic peptide substrate	1726:1779	Recombinant furin treated with peptide N-glycanase F had reduced activity against a synthetic peptide substrate.
19909832	11	7	theme	sites	1845:1849	arg1	mutagenesis					1804:1814	site-directed mutagenesis	1790:1814	site-directed mutagenesis of two furin N-glycosylation sites, Asn(387) and Asn(440),	1790:1873	Indeed, site-directed mutagenesis of two furin N-glycosylation sites, Asn(387) and Asn(440), abrogated furin activation and this mutant was unable to rescue ADAMTS5 processing in furin-deficient cells.
19909832	3	8	theme	CHO-K1	548:553	arg1	cells					555:559	HEK293F and CHO-K1 cells	536:559	HEK293F and CHO-K1 cells transiently transfected with ADAMTS5 cDNA	536:601	DESIGN: HEK293F and CHO-K1 cells transiently transfected with ADAMTS5 cDNA were treated with glucosamine or the related hexosamine mannosamine.
19909832	9	9	theme	cellular	1599:1606	arg1	furin					1608:1612	cellular furin	1599:1612	cellular furin	1599:1612	Glucosamine treatment led to decreased glycosylation of cellular furin, with reduced furin autoactivation as the consequence.
19909832	12	10	theme	reduced	2135:2141	arg1	activity					2155:2162	reduced aggrecanase activity	2135:2162	reduced aggrecanase activity of ADAMTS5	2135:2173	CONCLUSIONS: Ten mM glucosamine reduces excision of the ADAMTS5 propeptide via interference with post-translational modification of furin and leads to reduced aggrecanase activity of ADAMTS5.
19909832	6	11	theme	deficient	957:965	arg1	furin					967:971	N-glycan deficient furin	948:971	N-glycan deficient furin	948:971	Post-translational modification of furin and N-glycan deficient furin mutants generated by site-directed mutagenesis was analyzed by western blotting, and the mutants were evaluated for their ADAMTS5 processing ability in furin-deficient CHO-RPE.40 cells.
19909832	7	12	with	interference	1265:1276	arg1	mechanism					1307:1315	the propeptide excision mechanism	1283:1315	the propeptide excision mechanism	1283:1315	RESULTS: Ten mM glucosamine and 5-10mM mannosamine reduced excision of the ADAMTS5 propeptide, indicating interference with the propeptide excision mechanism, although mannosamine compromised cell viability at these doses.
19909832	11	13	theme	ADAMTS5	1939:1945	arg1	processing					1947:1956	ADAMTS5 processing	1939:1956	ADAMTS5 processing in furin-deficient cells	1939:1981	Indeed, site-directed mutagenesis of two furin N-glycosylation sites, Asn(387) and Asn(440), abrogated furin activation and this mutant was unable to rescue ADAMTS5 processing in furin-deficient cells.
19909832	0	14	with	interference	91:102	arg1	modification					128:139	post-translational modification	109:139	post-translational modification of furin	109:148	10mM glucosamine prevents activation of proADAMTS5 (aggrecanase-2) in transfected cells by interference with post-translational modification of furin.
19909832	2	15	theme	disintegrin-like	317:332	arg1	domain					354:359	a disintegrin-like and metalloprotease domain	315:359	domain	354:359	We determined the effect of glucosamine on ADAMTS5 (a disintegrin-like and metalloprotease domain (reprolysin type) with thrombospondin type-1 motifs 5), a major aggrecanase in osteoarthritis, and investigated a potential mechanism underlying the observed effects.
19909832	2	15	theme	disintegrin-like	317:332	arg1	type					373:376	reprolysin type	362:376	reprolysin type	362:376	We determined the effect of glucosamine on ADAMTS5 (a disintegrin-like and metalloprotease domain (reprolysin type) with thrombospondin type-1 motifs 5), a major aggrecanase in osteoarthritis, and investigated a potential mechanism underlying the observed effects.
19909832	4	16	from	effects	684:690	arg1	transcription					701:713	FURIN transcription	695:713	FURIN transcription	695:713	Glucosamine effects on FURIN transcription were determined by quantitative RT-PCR.
19909832	11	17	gly	N-glycosylation	1829:1843	arg2	Asn					1852:1854	Asn	1852:1854	Asn(387)	1852:1859	Indeed, site-directed mutagenesis of two furin N-glycosylation sites, Asn(387) and Asn(440), abrogated furin activation and this mutant was unable to rescue ADAMTS5 processing in furin-deficient cells.
19909832	11	17	gly	N-glycosylation	1829:1843	arg2	Asn					1865:1867	Asn	1865:1867	Asn(440)	1865:1872	Indeed, site-directed mutagenesis of two furin N-glycosylation sites, Asn(387) and Asn(440), abrogated furin activation and this mutant was unable to rescue ADAMTS5 processing in furin-deficient cells.
19909832	11	17	gly	N-glycosylation	1829:1843	arg2	sites					1845:1849	two furin N-glycosylation sites	1819:1849	two furin N-glycosylation sites	1819:1849	Indeed, site-directed mutagenesis of two furin N-glycosylation sites, Asn(387) and Asn(440), abrogated furin activation and this mutant was unable to rescue ADAMTS5 processing in furin-deficient cells.
19909832	11	17	gly	N-glycosylation	1829:1843	arg2	two					1819:1821	two	1819:1821	two	1819:1821	Indeed, site-directed mutagenesis of two furin N-glycosylation sites, Asn(387) and Asn(440), abrogated furin activation and this mutant was unable to rescue ADAMTS5 processing in furin-deficient cells.
19909832	10	18	theme	synthetic	1753:1761	arg1	substrate					1771:1779	a synthetic peptide substrate	1751:1779	a synthetic peptide substrate	1751:1779	Recombinant furin treated with peptide N-glycanase F had reduced activity against a synthetic peptide substrate.
19909832	7	19	theme	mM	1172:1173	arg1	glucosamine					1175:1185	Ten mM glucosamine	1168:1185	Ten mM glucosamine	1168:1185	RESULTS: Ten mM glucosamine and 5-10mM mannosamine reduced excision of the ADAMTS5 propeptide, indicating interference with the propeptide excision mechanism, although mannosamine compromised cell viability at these doses.
19909832	9	20	theme	reduced	1620:1626	arg1	autoactivation					1634:1647	reduced furin autoactivation	1620:1647	reduced furin autoactivation as the consequence	1620:1666	Glucosamine treatment led to decreased glycosylation of cellular furin, with reduced furin autoactivation as the consequence.
19909832	12	21	theme	furin	2116:2120	arg1	modification					2100:2111	post-translational modification	2081:2111	post-translational modification of furin	2081:2120	CONCLUSIONS: Ten mM glucosamine reduces excision of the ADAMTS5 propeptide via interference with post-translational modification of furin and leads to reduced aggrecanase activity of ADAMTS5.
19909832	0	22	theme	furin	144:148	arg1	modification					128:139	post-translational modification	109:139	post-translational modification of furin	109:148	10mM glucosamine prevents activation of proADAMTS5 (aggrecanase-2) in transfected cells by interference with post-translational modification of furin.
19909832	6	23	theme	western	1036:1042	arg1	blotting					1044:1051	western blotting	1036:1051	western blotting	1036:1051	Post-translational modification of furin and N-glycan deficient furin mutants generated by site-directed mutagenesis was analyzed by western blotting, and the mutants were evaluated for their ADAMTS5 processing ability in furin-deficient CHO-RPE.40 cells.
19909832	8	24	theme	mRNA	1426:1429	arg1	levels					1431:1436	furin mRNA levels	1420:1436	furin mRNA levels	1420:1436	Although glucosamine had no effect on furin mRNA levels, western blot of furin from glucosamine-treated cells suggested altered post-translational modification.
19909832	3	25	theme	hexosamine	648:657	arg1	mannosamine					659:669	the related hexosamine mannosamine	636:669	the related hexosamine mannosamine	636:669	DESIGN: HEK293F and CHO-K1 cells transiently transfected with ADAMTS5 cDNA were treated with glucosamine or the related hexosamine mannosamine.
19909832	6	26	theme	ADAMTS5	1095:1101	arg1	ability					1114:1120	their ADAMTS5 processing ability	1089:1120	their ADAMTS5 processing ability	1089:1120	Post-translational modification of furin and N-glycan deficient furin mutants generated by site-directed mutagenesis was analyzed by western blotting, and the mutants were evaluated for their ADAMTS5 processing ability in furin-deficient CHO-RPE.40 cells.
19909832	2	27	dep	ADAMTS5	306:312	arg1	domain					354:359	a disintegrin-like and metalloprotease domain	315:359	domain	354:359	We determined the effect of glucosamine on ADAMTS5 (a disintegrin-like and metalloprotease domain (reprolysin type) with thrombospondin type-1 motifs 5), a major aggrecanase in osteoarthritis, and investigated a potential mechanism underlying the observed effects.
19909832	2	27	dep	ADAMTS5	306:312	arg1	type					373:376	reprolysin type	362:376	reprolysin type	362:376	We determined the effect of glucosamine on ADAMTS5 (a disintegrin-like and metalloprotease domain (reprolysin type) with thrombospondin type-1 motifs 5), a major aggrecanase in osteoarthritis, and investigated a potential mechanism underlying the observed effects.
19909832	0	28	theme	transfected	70:80	arg1	cells					82:86	transfected cells	70:86	transfected cells	70:86	10mM glucosamine prevents activation of proADAMTS5 (aggrecanase-2) in transfected cells by interference with post-translational modification of furin.
19909832	2	29	with	domain	354:359	arg1	motifs					406:411	thrombospondin type-1 motifs 5	384:413	thrombospondin type-1 motifs 5	384:413	We determined the effect of glucosamine on ADAMTS5 (a disintegrin-like and metalloprotease domain (reprolysin type) with thrombospondin type-1 motifs 5), a major aggrecanase in osteoarthritis, and investigated a potential mechanism underlying the observed effects.
19909832	8	30	theme	furin	1455:1459	arg1	blot					1447:1450	western blot	1439:1450	western blot of furin from glucosamine-treated cells	1439:1490	Although glucosamine had no effect on furin mRNA levels, western blot of furin from glucosamine-treated cells suggested altered post-translational modification.
19909832	12	31	theme	post-translational	2081:2098	arg1	modification					2100:2111	post-translational modification	2081:2111	post-translational modification of furin	2081:2120	CONCLUSIONS: Ten mM glucosamine reduces excision of the ADAMTS5 propeptide via interference with post-translational modification of furin and leads to reduced aggrecanase activity of ADAMTS5.
19909832	8	32	theme	glucosamine-treated	1466:1484	arg1	cells					1486:1490	glucosamine-treated cells	1466:1490	glucosamine-treated cells	1466:1490	Although glucosamine had no effect on furin mRNA levels, western blot of furin from glucosamine-treated cells suggested altered post-translational modification.
19909832	5	33	theme	zymogen	803:809	arg1	processing					781:790	furin-mediated processing	766:790	furin-mediated processing of ADAMTS5 zymogen	766:809	Effects on furin-mediated processing of ADAMTS5 zymogen, and aggrecan processing by glucosamine-treated cells, were determined by western blotting.
19909832	10	34	contain	had	1722:1724	arg1	furin					1681:1685	Recombinant furin	1669:1685	Recombinant furin treated with peptide N-glycanase F	1669:1720	Recombinant furin treated with peptide N-glycanase F had reduced activity against a synthetic peptide substrate.
19909832	10	34	contain	had	1722:1724	arg2	activity					1734:1741	reduced activity	1726:1741	reduced activity against a synthetic peptide substrate	1726:1779	Recombinant furin treated with peptide N-glycanase F had reduced activity against a synthetic peptide substrate.
19909832	0	35	theme	10mM	0:3	arg1	glucosamine					5:15	10mM glucosamine	0:15	10mM glucosamine	0:15	10mM glucosamine prevents activation of proADAMTS5 (aggrecanase-2) in transfected cells by interference with post-translational modification of furin.
19909832	12	36	theme	propeptide	2048:2057	arg1	excision					2024:2031	excision	2024:2031	excision of the ADAMTS5 propeptide	2024:2057	CONCLUSIONS: Ten mM glucosamine reduces excision of the ADAMTS5 propeptide via interference with post-translational modification of furin and leads to reduced aggrecanase activity of ADAMTS5.
19909832	8	37	theme	post-translational	1510:1527	arg1	modification					1529:1540	altered post-translational modification	1502:1540	altered post-translational modification	1502:1540	Although glucosamine had no effect on furin mRNA levels, western blot of furin from glucosamine-treated cells suggested altered post-translational modification.
19909832	5	38	theme	western	885:891	arg1	blotting					893:900	western blotting	885:900	western blotting	885:900	Effects on furin-mediated processing of ADAMTS5 zymogen, and aggrecan processing by glucosamine-treated cells, were determined by western blotting.
19909832	6	39	theme	N-glycan	948:955	arg1	furin					967:971	N-glycan deficient furin	948:971	N-glycan deficient furin	948:971	Post-translational modification of furin and N-glycan deficient furin mutants generated by site-directed mutagenesis was analyzed by western blotting, and the mutants were evaluated for their ADAMTS5 processing ability in furin-deficient CHO-RPE.40 cells.
19909832	2	40	from	effect	281:286	arg1	ADAMTS5					306:312	ADAMTS5	306:312	ADAMTS5 (a disintegrin-like and metalloprotease domain (reprolysin type) with thrombospondin type-1 motifs 5)	306:414	We determined the effect of glucosamine on ADAMTS5 (a disintegrin-like and metalloprotease domain (reprolysin type) with thrombospondin type-1 motifs 5), a major aggrecanase in osteoarthritis, and investigated a potential mechanism underlying the observed effects.
19909832	2	40	from	effect	281:286	arg1	aggrecanase					425:435	a major aggrecanase	417:435	a major aggrecanase in osteoarthritis	417:453	We determined the effect of glucosamine on ADAMTS5 (a disintegrin-like and metalloprotease domain (reprolysin type) with thrombospondin type-1 motifs 5), a major aggrecanase in osteoarthritis, and investigated a potential mechanism underlying the observed effects.
19909832	7	41	theme	propeptide	1287:1296	arg1	mechanism					1307:1315	the propeptide excision mechanism	1283:1315	the propeptide excision mechanism	1283:1315	RESULTS: Ten mM glucosamine and 5-10mM mannosamine reduced excision of the ADAMTS5 propeptide, indicating interference with the propeptide excision mechanism, although mannosamine compromised cell viability at these doses.
19909832	5	42	theme	glucosamine-treated	839:857	arg1	cells					859:863	glucosamine-treated cells	839:863	glucosamine-treated cells	839:863	Effects on furin-mediated processing of ADAMTS5 zymogen, and aggrecan processing by glucosamine-treated cells, were determined by western blotting.
19909832	6	43	theme	furin	938:942	arg1	mutants					973:979	furin and N-glycan deficient furin mutants	938:979	furin and N-glycan deficient furin mutants generated by site-directed mutagenesis	938:1018	Post-translational modification of furin and N-glycan deficient furin mutants generated by site-directed mutagenesis was analyzed by western blotting, and the mutants were evaluated for their ADAMTS5 processing ability in furin-deficient CHO-RPE.40 cells.
19909832	6	44	theme	furin-deficient	1125:1139	arg1	cells					1152:1156	furin-deficient CHO-RPE.40 cells	1125:1156	furin-deficient CHO-RPE.40 cells	1125:1156	Post-translational modification of furin and N-glycan deficient furin mutants generated by site-directed mutagenesis was analyzed by western blotting, and the mutants were evaluated for their ADAMTS5 processing ability in furin-deficient CHO-RPE.40 cells.
19909832	2	45	theme	reprolysin	362:371	arg1	domain					354:359	a disintegrin-like and metalloprotease domain	315:359	domain	354:359	We determined the effect of glucosamine on ADAMTS5 (a disintegrin-like and metalloprotease domain (reprolysin type) with thrombospondin type-1 motifs 5), a major aggrecanase in osteoarthritis, and investigated a potential mechanism underlying the observed effects.
19909832	2	45	theme	reprolysin	362:371	arg1	type					373:376	reprolysin type	362:376	reprolysin type	362:376	We determined the effect of glucosamine on ADAMTS5 (a disintegrin-like and metalloprotease domain (reprolysin type) with thrombospondin type-1 motifs 5), a major aggrecanase in osteoarthritis, and investigated a potential mechanism underlying the observed effects.
19909832	7	46	theme	propeptide	1242:1251	arg1	excision					1218:1225	excision	1218:1225	excision of the ADAMTS5 propeptide	1218:1251	RESULTS: Ten mM glucosamine and 5-10mM mannosamine reduced excision of the ADAMTS5 propeptide, indicating interference with the propeptide excision mechanism, although mannosamine compromised cell viability at these doses.
19909832	2	47	dep	motifs	406:411	arg1	5					413:413	5	413:413	5	413:413	We determined the effect of glucosamine on ADAMTS5 (a disintegrin-like and metalloprotease domain (reprolysin type) with thrombospondin type-1 motifs 5), a major aggrecanase in osteoarthritis, and investigated a potential mechanism underlying the observed effects.
19909832	12	48	theme	Ten	1997:1999	arg1	mM					2001:2002	mM	2001:2002	mM	2001:2002	CONCLUSIONS: Ten mM glucosamine reduces excision of the ADAMTS5 propeptide via interference with post-translational modification of furin and leads to reduced aggrecanase activity of ADAMTS5.
19909832	9	49	gly	glycosylation	1582:1594	arg1	furin					1608:1612	cellular furin	1599:1612	cellular furin	1599:1612	Glucosamine treatment led to decreased glycosylation of cellular furin, with reduced furin autoactivation as the consequence.
19909832	2	50	theme	thrombospondin	384:397	arg1	motifs					406:411	thrombospondin type-1 motifs 5	384:413	thrombospondin type-1 motifs 5	384:413	We determined the effect of glucosamine on ADAMTS5 (a disintegrin-like and metalloprotease domain (reprolysin type) with thrombospondin type-1 motifs 5), a major aggrecanase in osteoarthritis, and investigated a potential mechanism underlying the observed effects.
19909832	9	51	theme	Glucosamine	1543:1553	arg1	treatment					1555:1563	Glucosamine treatment	1543:1563	Glucosamine treatment	1543:1563	Glucosamine treatment led to decreased glycosylation of cellular furin, with reduced furin autoactivation as the consequence.
19909832	7	52	theme	excision	1298:1305	arg1	mechanism					1307:1315	the propeptide excision mechanism	1283:1315	the propeptide excision mechanism	1283:1315	RESULTS: Ten mM glucosamine and 5-10mM mannosamine reduced excision of the ADAMTS5 propeptide, indicating interference with the propeptide excision mechanism, although mannosamine compromised cell viability at these doses.
19909832	2	53	from	aggrecanase	425:435	arg1	osteoarthritis					440:453	osteoarthritis	440:453	osteoarthritis	440:453	We determined the effect of glucosamine on ADAMTS5 (a disintegrin-like and metalloprotease domain (reprolysin type) with thrombospondin type-1 motifs 5), a major aggrecanase in osteoarthritis, and investigated a potential mechanism underlying the observed effects.
19909832	10	54	theme	N-glycanase	1708:1718	arg1	F					1720:1720	peptide N-glycanase F	1700:1720	peptide N-glycanase F	1700:1720	Recombinant furin treated with peptide N-glycanase F had reduced activity against a synthetic peptide substrate.
19909832	11	55	theme	N-glycosylation	1829:1843	arg1	Asn					1865:1867	Asn	1865:1867	Asn(440)	1865:1872	Indeed, site-directed mutagenesis of two furin N-glycosylation sites, Asn(387) and Asn(440), abrogated furin activation and this mutant was unable to rescue ADAMTS5 processing in furin-deficient cells.
19909832	11	55	theme	N-glycosylation	1829:1843	arg1	Asn					1852:1854	Asn	1852:1854	Asn(387)	1852:1859	Indeed, site-directed mutagenesis of two furin N-glycosylation sites, Asn(387) and Asn(440), abrogated furin activation and this mutant was unable to rescue ADAMTS5 processing in furin-deficient cells.
19909832	11	55	theme	N-glycosylation	1829:1843	arg1	sites					1845:1849	two furin N-glycosylation sites	1819:1849	two furin N-glycosylation sites	1819:1849	Indeed, site-directed mutagenesis of two furin N-glycosylation sites, Asn(387) and Asn(440), abrogated furin activation and this mutant was unable to rescue ADAMTS5 processing in furin-deficient cells.
19909832	6	56	theme	site-directed	994:1006	arg1	mutagenesis					1008:1018	site-directed mutagenesis	994:1018	site-directed mutagenesis	994:1018	Post-translational modification of furin and N-glycan deficient furin mutants generated by site-directed mutagenesis was analyzed by western blotting, and the mutants were evaluated for their ADAMTS5 processing ability in furin-deficient CHO-RPE.40 cells.
19909832	8	57	from	cells	1486:1490	arg1	blot					1447:1450	western blot	1439:1450	western blot of furin from glucosamine-treated cells	1439:1490	Although glucosamine had no effect on furin mRNA levels, western blot of furin from glucosamine-treated cells suggested altered post-translational modification.
19909832	9	58	theme	decreased	1572:1580	arg1	glycosylation					1582:1594	decreased glycosylation	1572:1594	decreased glycosylation of cellular furin	1572:1612	Glucosamine treatment led to decreased glycosylation of cellular furin, with reduced furin autoactivation as the consequence.
19909832	7	59	theme	5-10mM	1191:1196	arg1	mannosamine					1198:1208	5-10mM mannosamine	1191:1208	5-10mM mannosamine	1191:1208	RESULTS: Ten mM glucosamine and 5-10mM mannosamine reduced excision of the ADAMTS5 propeptide, indicating interference with the propeptide excision mechanism, although mannosamine compromised cell viability at these doses.
19909832	2	60	theme	glucosamine	291:301	arg1	effect					281:286	the effect	277:286	the effect of glucosamine on ADAMTS5 (a disintegrin-like and metalloprotease domain (reprolysin type) with thrombospondin type-1 motifs 5), a major aggrecanase in osteoarthritis,	277:454	We determined the effect of glucosamine on ADAMTS5 (a disintegrin-like and metalloprotease domain (reprolysin type) with thrombospondin type-1 motifs 5), a major aggrecanase in osteoarthritis, and investigated a potential mechanism underlying the observed effects.
19909832	6	61	theme	furin	967:971	arg1	mutants					973:979	furin and N-glycan deficient furin mutants	938:979	furin and N-glycan deficient furin mutants generated by site-directed mutagenesis	938:1018	Post-translational modification of furin and N-glycan deficient furin mutants generated by site-directed mutagenesis was analyzed by western blotting, and the mutants were evaluated for their ADAMTS5 processing ability in furin-deficient CHO-RPE.40 cells.
19909832	3	62	theme	ADAMTS5	590:596	arg1	cDNA					598:601	ADAMTS5 cDNA	590:601	ADAMTS5 cDNA	590:601	DESIGN: HEK293F and CHO-K1 cells transiently transfected with ADAMTS5 cDNA were treated with glucosamine or the related hexosamine mannosamine.
19909832	9	63	theme	furin	1608:1612	arg1	glycosylation					1582:1594	decreased glycosylation	1572:1594	decreased glycosylation of cellular furin	1572:1612	Glucosamine treatment led to decreased glycosylation of cellular furin, with reduced furin autoactivation as the consequence.
19909832	11	64	from	processing	1947:1956	arg1	cells					1977:1981	furin-deficient cells	1961:1981	furin-deficient cells	1961:1981	Indeed, site-directed mutagenesis of two furin N-glycosylation sites, Asn(387) and Asn(440), abrogated furin activation and this mutant was unable to rescue ADAMTS5 processing in furin-deficient cells.
19909832	10	65	theme	peptide	1763:1769	arg1	substrate					1771:1779	a synthetic peptide substrate	1751:1779	a synthetic peptide substrate	1751:1779	Recombinant furin treated with peptide N-glycanase F had reduced activity against a synthetic peptide substrate.
19909832	7	66	theme	Ten	1168:1170	arg1	mM					1172:1173	mM	1172:1173	mM	1172:1173	RESULTS: Ten mM glucosamine and 5-10mM mannosamine reduced excision of the ADAMTS5 propeptide, indicating interference with the propeptide excision mechanism, although mannosamine compromised cell viability at these doses.
19909832	12	67	theme	aggrecanase	2143:2153	arg1	activity					2155:2162	reduced aggrecanase activity	2135:2162	reduced aggrecanase activity of ADAMTS5	2135:2173	CONCLUSIONS: Ten mM glucosamine reduces excision of the ADAMTS5 propeptide via interference with post-translational modification of furin and leads to reduced aggrecanase activity of ADAMTS5.
19909832	8	68	theme	western	1439:1445	arg1	blot					1447:1450	western blot	1439:1450	western blot of furin from glucosamine-treated cells	1439:1490	Although glucosamine had no effect on furin mRNA levels, western blot of furin from glucosamine-treated cells suggested altered post-translational modification.
19909832	1	69	theme	aggrecan	222:229	arg1	catabolism					231:240	cartilage aggrecan catabolism	212:240	cartilage aggrecan catabolism in explant cultures	212:260	OBJECTIVE: Glucosamine has been previously shown to suppress cartilage aggrecan catabolism in explant cultures.
19909832	4	70	theme	Glucosamine	672:682	arg1	effects					684:690	Glucosamine effects	672:690	Glucosamine effects on FURIN transcription	672:713	Glucosamine effects on FURIN transcription were determined by quantitative RT-PCR.
19909832	1	71	from	catabolism	231:240	arg1	cultures					253:260	explant cultures	245:260	explant cultures	245:260	OBJECTIVE: Glucosamine has been previously shown to suppress cartilage aggrecan catabolism in explant cultures.
19909832	11	72	theme	furin-deficient	1961:1975	arg1	cells					1977:1981	furin-deficient cells	1961:1981	furin-deficient cells	1961:1981	Indeed, site-directed mutagenesis of two furin N-glycosylation sites, Asn(387) and Asn(440), abrogated furin activation and this mutant was unable to rescue ADAMTS5 processing in furin-deficient cells.
19909832	5	73	from	processing	825:834	arg1	processing					781:790	furin-mediated processing	766:790	furin-mediated processing of ADAMTS5 zymogen	766:809	Effects on furin-mediated processing of ADAMTS5 zymogen, and aggrecan processing by glucosamine-treated cells, were determined by western blotting.
19909832	3	74	theme	related	640:646	arg1	mannosamine					659:669	the related hexosamine mannosamine	636:669	the related hexosamine mannosamine	636:669	DESIGN: HEK293F and CHO-K1 cells transiently transfected with ADAMTS5 cDNA were treated with glucosamine or the related hexosamine mannosamine.
19909832	8	75	theme	furin	1420:1424	arg1	levels					1431:1436	furin mRNA levels	1420:1436	furin mRNA levels	1420:1436	Although glucosamine had no effect on furin mRNA levels, western blot of furin from glucosamine-treated cells suggested altered post-translational modification.
19909832	7	76	theme	cell	1351:1354	arg1	viability					1356:1364	cell viability	1351:1364	cell viability	1351:1364	RESULTS: Ten mM glucosamine and 5-10mM mannosamine reduced excision of the ADAMTS5 propeptide, indicating interference with the propeptide excision mechanism, although mannosamine compromised cell viability at these doses.
19909832	6	77	theme	processing	1103:1112	arg1	ability					1114:1120	their ADAMTS5 processing ability	1089:1120	their ADAMTS5 processing ability	1089:1120	Post-translational modification of furin and N-glycan deficient furin mutants generated by site-directed mutagenesis was analyzed by western blotting, and the mutants were evaluated for their ADAMTS5 processing ability in furin-deficient CHO-RPE.40 cells.
19909832	2	78	theme	observed	510:517	arg1	effects					519:525	the observed effects	506:525	the observed effects	506:525	We determined the effect of glucosamine on ADAMTS5 (a disintegrin-like and metalloprotease domain (reprolysin type) with thrombospondin type-1 motifs 5), a major aggrecanase in osteoarthritis, and investigated a potential mechanism underlying the observed effects.
19909832	0	79	from	activation	26:35	arg1	cells					82:86	transfected cells	70:86	transfected cells	70:86	10mM glucosamine prevents activation of proADAMTS5 (aggrecanase-2) in transfected cells by interference with post-translational modification of furin.
19909832	11	80	theme	furin	1885:1889	arg1	activation					1891:1900	furin activation	1885:1900	furin activation	1885:1900	Indeed, site-directed mutagenesis of two furin N-glycosylation sites, Asn(387) and Asn(440), abrogated furin activation and this mutant was unable to rescue ADAMTS5 processing in furin-deficient cells.
19909832	5	81	theme	aggrecan	816:823	arg1	processing					825:834	aggrecan processing	816:834	aggrecan processing by glucosamine-treated cells	816:863	Effects on furin-mediated processing of ADAMTS5 zymogen, and aggrecan processing by glucosamine-treated cells, were determined by western blotting.
19909832	4	82	theme	quantitative	734:745	arg1	RT-PCR					747:752	quantitative RT-PCR	734:752	quantitative RT-PCR	734:752	Glucosamine effects on FURIN transcription were determined by quantitative RT-PCR.
19909832	0	83	theme	post-translational	109:126	arg1	modification					128:139	post-translational modification	109:139	post-translational modification of furin	109:148	10mM glucosamine prevents activation of proADAMTS5 (aggrecanase-2) in transfected cells by interference with post-translational modification of furin.
19909832	12	84	theme	ADAMTS5	2040:2046	arg1	propeptide					2048:2057	the ADAMTS5 propeptide	2036:2057	the ADAMTS5 propeptide	2036:2057	CONCLUSIONS: Ten mM glucosamine reduces excision of the ADAMTS5 propeptide via interference with post-translational modification of furin and leads to reduced aggrecanase activity of ADAMTS5.
19909832	1	85	theme	cartilage	212:220	arg1	catabolism					231:240	cartilage aggrecan catabolism	212:240	cartilage aggrecan catabolism in explant cultures	212:260	OBJECTIVE: Glucosamine has been previously shown to suppress cartilage aggrecan catabolism in explant cultures.
19909832	5	86	theme	ADAMTS5	795:801	arg1	zymogen					803:809	ADAMTS5 zymogen	795:809	ADAMTS5 zymogen	795:809	Effects on furin-mediated processing of ADAMTS5 zymogen, and aggrecan processing by glucosamine-treated cells, were determined by western blotting.
19909832	2	87	theme	type-1	399:404	arg1	motifs					406:411	thrombospondin type-1 motifs 5	384:413	thrombospondin type-1 motifs 5	384:413	We determined the effect of glucosamine on ADAMTS5 (a disintegrin-like and metalloprotease domain (reprolysin type) with thrombospondin type-1 motifs 5), a major aggrecanase in osteoarthritis, and investigated a potential mechanism underlying the observed effects.
19909832	8	88	theme	altered	1502:1508	arg1	modification					1529:1540	altered post-translational modification	1502:1540	altered post-translational modification	1502:1540	Although glucosamine had no effect on furin mRNA levels, western blot of furin from glucosamine-treated cells suggested altered post-translational modification.
19909832	2	89	theme	major	419:423	arg1	ADAMTS5					306:312	ADAMTS5	306:312	ADAMTS5 (a disintegrin-like and metalloprotease domain (reprolysin type) with thrombospondin type-1 motifs 5)	306:414	We determined the effect of glucosamine on ADAMTS5 (a disintegrin-like and metalloprotease domain (reprolysin type) with thrombospondin type-1 motifs 5), a major aggrecanase in osteoarthritis, and investigated a potential mechanism underlying the observed effects.
19909832	2	89	theme	major	419:423	arg1	aggrecanase					425:435	a major aggrecanase	417:435	a major aggrecanase in osteoarthritis	417:453	We determined the effect of glucosamine on ADAMTS5 (a disintegrin-like and metalloprotease domain (reprolysin type) with thrombospondin type-1 motifs 5), a major aggrecanase in osteoarthritis, and investigated a potential mechanism underlying the observed effects.
19909832	0	90	theme	proADAMTS5	40:49	arg1	activation					26:35	activation	26:35	activation of proADAMTS5 (aggrecanase-2) in transfected cells	26:86	10mM glucosamine prevents activation of proADAMTS5 (aggrecanase-2) in transfected cells by interference with post-translational modification of furin.
19909832	12	91	with	interference	2063:2074	arg1	modification					2100:2111	post-translational modification	2081:2111	post-translational modification of furin	2081:2120	CONCLUSIONS: Ten mM glucosamine reduces excision of the ADAMTS5 propeptide via interference with post-translational modification of furin and leads to reduced aggrecanase activity of ADAMTS5.
19909832	9	92	theme	furin	1628:1632	arg1	autoactivation					1634:1647	reduced furin autoactivation	1620:1647	reduced furin autoactivation as the consequence	1620:1666	Glucosamine treatment led to decreased glycosylation of cellular furin, with reduced furin autoactivation as the consequence.
19909832	6	93	theme	CHO-RPE.40	1141:1150	arg1	cells					1152:1156	furin-deficient CHO-RPE.40 cells	1125:1156	furin-deficient CHO-RPE.40 cells	1125:1156	Post-translational modification of furin and N-glycan deficient furin mutants generated by site-directed mutagenesis was analyzed by western blotting, and the mutants were evaluated for their ADAMTS5 processing ability in furin-deficient CHO-RPE.40 cells.
19909832	2	94	theme	potential	475:483	arg1	mechanism					485:493	a potential mechanism	473:493	a potential mechanism underlying the observed effects	473:525	We determined the effect of glucosamine on ADAMTS5 (a disintegrin-like and metalloprotease domain (reprolysin type) with thrombospondin type-1 motifs 5), a major aggrecanase in osteoarthritis, and investigated a potential mechanism underlying the observed effects.
19909832	7	95	theme	ADAMTS5	1234:1240	arg1	propeptide					1242:1251	the ADAMTS5 propeptide	1230:1251	the ADAMTS5 propeptide	1230:1251	RESULTS: Ten mM glucosamine and 5-10mM mannosamine reduced excision of the ADAMTS5 propeptide, indicating interference with the propeptide excision mechanism, although mannosamine compromised cell viability at these doses.
19909832	5	96	theme	furin-mediated	766:779	arg1	processing					781:790	furin-mediated processing	766:790	furin-mediated processing of ADAMTS5 zymogen	766:809	Effects on furin-mediated processing of ADAMTS5 zymogen, and aggrecan processing by glucosamine-treated cells, were determined by western blotting.
19909832	12	97	theme	mM	2001:2002	arg1	glucosamine					2004:2014	Ten mM glucosamine	1997:2014	Ten mM glucosamine	1997:2014	CONCLUSIONS: Ten mM glucosamine reduces excision of the ADAMTS5 propeptide via interference with post-translational modification of furin and leads to reduced aggrecanase activity of ADAMTS5.
19909832	6	98	theme	Post-translational	903:920	arg1	modification					922:933	Post-translational modification	903:933	Post-translational modification of furin and N-glycan deficient furin mutants generated by site-directed mutagenesis	903:1018	Post-translational modification of furin and N-glycan deficient furin mutants generated by site-directed mutagenesis was analyzed by western blotting, and the mutants were evaluated for their ADAMTS5 processing ability in furin-deficient CHO-RPE.40 cells.
19909832	10	99	theme	Recombinant	1669:1679	arg1	furin					1681:1685	Recombinant furin	1669:1685	Recombinant furin treated with peptide N-glycanase F	1669:1720	Recombinant furin treated with peptide N-glycanase F had reduced activity against a synthetic peptide substrate.
19909832	11	100	theme	site-directed	1790:1802	arg1	mutagenesis					1804:1814	site-directed mutagenesis	1790:1814	site-directed mutagenesis of two furin N-glycosylation sites, Asn(387) and Asn(440),	1790:1873	Indeed, site-directed mutagenesis of two furin N-glycosylation sites, Asn(387) and Asn(440), abrogated furin activation and this mutant was unable to rescue ADAMTS5 processing in furin-deficient cells.
19909832	2	101	theme	metalloprotease	338:352	arg1	domain					354:359	a disintegrin-like and metalloprotease domain	315:359	domain	354:359	We determined the effect of glucosamine on ADAMTS5 (a disintegrin-like and metalloprotease domain (reprolysin type) with thrombospondin type-1 motifs 5), a major aggrecanase in osteoarthritis, and investigated a potential mechanism underlying the observed effects.
19909832	2	101	theme	metalloprotease	338:352	arg1	type					373:376	reprolysin type	362:376	reprolysin type	362:376	We determined the effect of glucosamine on ADAMTS5 (a disintegrin-like and metalloprotease domain (reprolysin type) with thrombospondin type-1 motifs 5), a major aggrecanase in osteoarthritis, and investigated a potential mechanism underlying the observed effects.
19909832	1	102	theme	explant	245:251	arg1	cultures					253:260	explant cultures	245:260	explant cultures	245:260	OBJECTIVE: Glucosamine has been previously shown to suppress cartilage aggrecan catabolism in explant cultures.
19909832	11	103	theme	furin	1823:1827	arg1	Asn					1865:1867	Asn	1865:1867	Asn(440)	1865:1872	Indeed, site-directed mutagenesis of two furin N-glycosylation sites, Asn(387) and Asn(440), abrogated furin activation and this mutant was unable to rescue ADAMTS5 processing in furin-deficient cells.
19909832	11	103	theme	furin	1823:1827	arg1	Asn					1852:1854	Asn	1852:1854	Asn(387)	1852:1859	Indeed, site-directed mutagenesis of two furin N-glycosylation sites, Asn(387) and Asn(440), abrogated furin activation and this mutant was unable to rescue ADAMTS5 processing in furin-deficient cells.
19909832	11	103	theme	furin	1823:1827	arg1	sites					1845:1849	two furin N-glycosylation sites	1819:1849	two furin N-glycosylation sites	1819:1849	Indeed, site-directed mutagenesis of two furin N-glycosylation sites, Asn(387) and Asn(440), abrogated furin activation and this mutant was unable to rescue ADAMTS5 processing in furin-deficient cells.
19909832	3	104	theme	HEK293F	536:542	arg1	cells					555:559	HEK293F and CHO-K1 cells	536:559	HEK293F and CHO-K1 cells transiently transfected with ADAMTS5 cDNA	536:601	DESIGN: HEK293F and CHO-K1 cells transiently transfected with ADAMTS5 cDNA were treated with glucosamine or the related hexosamine mannosamine.
10029548	0	0	theme	transferrin	76:86	arg1	N-lobe					60:65	the N-lobe	56:65	the N-lobe of human transferrin expressed in Pichia pastoris	56:115	X-ray crystallography and mass spectroscopy reveal that the N-lobe of human transferrin expressed in Pichia pastoris is folded correctly but is glycosylated on serine-32.
10029548	0	0	theme	transferrin	76:86	arg1	transferrin					76:86	human transferrin	70:86	human transferrin expressed in Pichia pastoris	70:115	X-ray crystallography and mass spectroscopy reveal that the N-lobe of human transferrin expressed in Pichia pastoris is folded correctly but is glycosylated on serine-32.
10029548	1	1	theme	Pichia	282:287	arg1	pastoris					289:296	Pichia pastoris	282:296	Pichia pastoris	282:296	The ferric form of the N-lobe of human serum transferrin (Fe(III)-hTF/2N) has been expressed at high levels in Pichia pastoris.
10029548	7	2	from	site	1081:1084	arg1	distance					1050:1057	its distance	1046:1057	its distance from the iron-binding site	1046:1084	Because of its distance from the iron-binding site, glycosylation of Ser-32 should not affect the iron-binding properties of hTF/2N expressed in P. pastoris, making this an excellent expression system for the production of hTF/2N.
10029548	2	3	theme	Fe	303:304	arg1	-hTF/2N					310:316	The Fe(III)-hTF/2N	299:316	The Fe(III)-hTF/2N	299:316	The Fe(III)-hTF/2N was crystallized in the space group P41212, and X-ray crystallography was used to solve the structure of the recombinant protein at 2.5 A resolution.
10029548	1	4	theme	Fe	229:230	arg1	transferrin					216:226	human serum transferrin	204:226	human serum transferrin (Fe(III)-hTF/2N)	204:243	The ferric form of the N-lobe of human serum transferrin (Fe(III)-hTF/2N) has been expressed at high levels in Pichia pastoris.
10029548	1	4	theme	Fe	229:230	arg1	-hTF/2N					236:242	Fe(III)-hTF/2N	229:242	Fe(III)-hTF/2N	229:242	The ferric form of the N-lobe of human serum transferrin (Fe(III)-hTF/2N) has been expressed at high levels in Pichia pastoris.
10029548	0	5	theme	human	70:74	arg1	transferrin					76:86	human transferrin	70:86	human transferrin expressed in Pichia pastoris	70:115	X-ray crystallography and mass spectroscopy reveal that the N-lobe of human transferrin expressed in Pichia pastoris is folded correctly but is glycosylated on serine-32.
10029548	1	6	dep	-hTF/2N	236:242	arg1	III					232:234	III	232:234	III	232:234	The ferric form of the N-lobe of human serum transferrin (Fe(III)-hTF/2N) has been expressed at high levels in Pichia pastoris.
10029548	1	7	from	levels	272:277	arg1	pastoris					289:296	Pichia pastoris	282:296	Pichia pastoris	282:296	The ferric form of the N-lobe of human serum transferrin (Fe(III)-hTF/2N) has been expressed at high levels in Pichia pastoris.
10029548	6	8	link	pastoris-derived	1009:1024	arg1	protein					1026:1032	a P. pastoris-derived protein	1004:1032	a P. pastoris-derived protein	1004:1032	This represents the first localization of an O-linked glycan in a P. pastoris-derived protein.
10029548	6	9	theme	first	960:964	arg1	localization					966:977	the first localization	956:977	the first localization of an O-linked glycan in a P. pastoris-derived protein	956:1032	This represents the first localization of an O-linked glycan in a P. pastoris-derived protein.
10029548	3	10	theme	recombinant	605:615	arg1	-hTF/2N					624:630	recombinant Fe(III)-hTF/2N	605:630	recombinant Fe(III)-hTF/2N expressed in P. pastoris	605:655	This represents only the second P. pastoris-derived protein structure determined to date, and allows the comparison of the structures of recombinant Fe(III)-hTF/2N expressed in P. pastoris and mammalian cells with serum-derived transferrin.
10029548	2	11	theme	protein	439:445	arg1	structure					410:418	the structure	406:418	the structure of the recombinant protein	406:445	The Fe(III)-hTF/2N was crystallized in the space group P41212, and X-ray crystallography was used to solve the structure of the recombinant protein at 2.5 A resolution.
10029548	3	12	theme	-hTF/2N	624:630	arg1	cells					671:675	mammalian cells	661:675	mammalian cells	661:675	This represents only the second P. pastoris-derived protein structure determined to date, and allows the comparison of the structures of recombinant Fe(III)-hTF/2N expressed in P. pastoris and mammalian cells with serum-derived transferrin.
10029548	3	12	theme	-hTF/2N	624:630	arg1	structures					591:600	the structures	587:600	the structures of recombinant Fe(III)-hTF/2N expressed in P. pastoris	587:655	This represents only the second P. pastoris-derived protein structure determined to date, and allows the comparison of the structures of recombinant Fe(III)-hTF/2N expressed in P. pastoris and mammalian cells with serum-derived transferrin.
10029548	3	13	with	comparison	573:582	arg1	transferrin					696:706	serum-derived transferrin	682:706	serum-derived transferrin	682:706	This represents only the second P. pastoris-derived protein structure determined to date, and allows the comparison of the structures of recombinant Fe(III)-hTF/2N expressed in P. pastoris and mammalian cells with serum-derived transferrin.
10029548	2	14	theme	recombinant	427:437	arg1	protein					439:445	the recombinant protein	423:445	the recombinant protein	423:445	The Fe(III)-hTF/2N was crystallized in the space group P41212, and X-ray crystallography was used to solve the structure of the recombinant protein at 2.5 A resolution.
10029548	4	15	from	all	769:771	arg1	pattern					733:739	The polypeptide folding pattern	709:739	The polypeptide folding pattern	709:739	The polypeptide folding pattern is essentially identical in all of the three proteins.
10029548	4	15	from	all	769:771	arg1	identical					756:764	identical	756:764	identical	756:764	The polypeptide folding pattern is essentially identical in all of the three proteins.
10029548	5	16	theme	Ser-32	911:916	arg1	glycosylation					894:906	glycosylation	894:906	glycosylation of Ser-32 with a single hexose	894:937	Mass spectroscopic analyses of P. pastoris- hTF/2N and proteolytically derived fragments revealed glycosylation of Ser-32 with a single hexose.
10029548	4	17	theme	folding	725:731	arg1	pattern					733:739	The polypeptide folding pattern	709:739	The polypeptide folding pattern	709:739	The polypeptide folding pattern is essentially identical in all of the three proteins.
10029548	4	17	theme	folding	725:731	arg1	identical					756:764	identical	756:764	identical	756:764	The polypeptide folding pattern is essentially identical in all of the three proteins.
10029548	0	18	theme	Pichia	101:106	arg1	pastoris					108:115	Pichia pastoris	101:115	Pichia pastoris	101:115	X-ray crystallography and mass spectroscopy reveal that the N-lobe of human transferrin expressed in Pichia pastoris is folded correctly but is glycosylated on serine-32.
10029548	6	19	link	O-linked	985:992	arg1	glycan					994:999	an O-linked glycan	982:999	an O-linked glycan	982:999	This represents the first localization of an O-linked glycan in a P. pastoris-derived protein.
10029548	3	20	theme	mammalian	661:669	arg1	cells					671:675	mammalian cells	661:675	mammalian cells	661:675	This represents only the second P. pastoris-derived protein structure determined to date, and allows the comparison of the structures of recombinant Fe(III)-hTF/2N expressed in P. pastoris and mammalian cells with serum-derived transferrin.
10029548	2	21	theme	X-ray	366:370	arg1	crystallography					372:386	X-ray crystallography	366:386	X-ray crystallography	366:386	The Fe(III)-hTF/2N was crystallized in the space group P41212, and X-ray crystallography was used to solve the structure of the recombinant protein at 2.5 A resolution.
10029548	4	22	from	identical	756:764	arg1	all					769:771	all	769:771	all	769:771	The polypeptide folding pattern is essentially identical in all of the three proteins.
10029548	4	22	from	identical	756:764	arg1	proteins					786:793	the three proteins	776:793	the three proteins	776:793	The polypeptide folding pattern is essentially identical in all of the three proteins.
10029548	6	23	from	localization	966:977	arg1	protein					1026:1032	a P. pastoris-derived protein	1004:1032	a P. pastoris-derived protein	1004:1032	This represents the first localization of an O-linked glycan in a P. pastoris-derived protein.
10029548	7	24	theme	Ser-32	1104:1109	arg1	glycosylation					1087:1099	glycosylation	1087:1099	glycosylation of Ser-32	1087:1109	Because of its distance from the iron-binding site, glycosylation of Ser-32 should not affect the iron-binding properties of hTF/2N expressed in P. pastoris, making this an excellent expression system for the production of hTF/2N.
10029548	1	25	theme	ferric	175:180	arg1	form					182:185	The ferric form	171:185	The ferric form of the N-lobe of human serum transferrin (Fe(III)-hTF/2N)	171:243	The ferric form of the N-lobe of human serum transferrin (Fe(III)-hTF/2N) has been expressed at high levels in Pichia pastoris.
10029548	0	26	theme	X-ray	0:4	arg1	crystallography					6:20	X-ray crystallography	0:20	X-ray crystallography	0:20	X-ray crystallography and mass spectroscopy reveal that the N-lobe of human transferrin expressed in Pichia pastoris is folded correctly but is glycosylated on serine-32.
10029548	5	27	theme	derived	867:873	arg1	fragments					875:883	proteolytically derived fragments	851:883	proteolytically derived fragments	851:883	Mass spectroscopic analyses of P. pastoris- hTF/2N and proteolytically derived fragments revealed glycosylation of Ser-32 with a single hexose.
10029548	6	28	theme	glycan	994:999	arg1	localization					966:977	the first localization	956:977	the first localization of an O-linked glycan in a P. pastoris-derived protein	956:1032	This represents the first localization of an O-linked glycan in a P. pastoris-derived protein.
10029548	0	29	theme	mass	26:29	arg1	spectroscopy					31:42	mass spectroscopy	26:42	mass spectroscopy	26:42	X-ray crystallography and mass spectroscopy reveal that the N-lobe of human transferrin expressed in Pichia pastoris is folded correctly but is glycosylated on serine-32.
10029548	5	30	theme	fragments	875:883	arg1	analyses					815:822	Mass spectroscopic analyses	796:822	Mass spectroscopic analyses of P. pastoris- hTF/2N and proteolytically derived fragments	796:883	Mass spectroscopic analyses of P. pastoris- hTF/2N and proteolytically derived fragments revealed glycosylation of Ser-32 with a single hexose.
10029548	2	31	theme	group	348:352	arg1	P41212					354:359	the space group P41212	338:359	the space group P41212	338:359	The Fe(III)-hTF/2N was crystallized in the space group P41212, and X-ray crystallography was used to solve the structure of the recombinant protein at 2.5 A resolution.
10029548	6	32	theme	pastoris-derived	1009:1024	arg1	protein					1026:1032	a P. pastoris-derived protein	1004:1032	a P. pastoris-derived protein	1004:1032	This represents the first localization of an O-linked glycan in a P. pastoris-derived protein.
10029548	2	33	theme	space	342:346	arg1	P41212					354:359	the space group P41212	338:359	the space group P41212	338:359	The Fe(III)-hTF/2N was crystallized in the space group P41212, and X-ray crystallography was used to solve the structure of the recombinant protein at 2.5 A resolution.
10029548	5	34	with	glycosylation	894:906	arg1	hexose					932:937	a single hexose	923:937	a single hexose	923:937	Mass spectroscopic analyses of P. pastoris- hTF/2N and proteolytically derived fragments revealed glycosylation of Ser-32 with a single hexose.
10029548	7	35	theme	excellent	1208:1216	arg1	system					1229:1234	an excellent expression system	1205:1234	an excellent expression system for the production of hTF/2N	1205:1263	Because of its distance from the iron-binding site, glycosylation of Ser-32 should not affect the iron-binding properties of hTF/2N expressed in P. pastoris, making this an excellent expression system for the production of hTF/2N.
10029548	7	36	theme	expression	1218:1227	arg1	system					1229:1234	an excellent expression system	1205:1234	an excellent expression system for the production of hTF/2N	1205:1263	Because of its distance from the iron-binding site, glycosylation of Ser-32 should not affect the iron-binding properties of hTF/2N expressed in P. pastoris, making this an excellent expression system for the production of hTF/2N.
10029548	3	37	theme	pastoris-derived	503:518	arg1	structure					528:536	only the second P. pastoris-derived protein structure	484:536	only the second P. pastoris-derived protein structure determined to date	484:555	This represents only the second P. pastoris-derived protein structure determined to date, and allows the comparison of the structures of recombinant Fe(III)-hTF/2N expressed in P. pastoris and mammalian cells with serum-derived transferrin.
10029548	1	38	theme	N-lobe	194:199	arg1	form					182:185	The ferric form	171:185	The ferric form of the N-lobe of human serum transferrin (Fe(III)-hTF/2N)	171:243	The ferric form of the N-lobe of human serum transferrin (Fe(III)-hTF/2N) has been expressed at high levels in Pichia pastoris.
10029548	6	39	theme	P.	1006:1007	arg1	protein					1026:1032	a P. pastoris-derived protein	1004:1032	a P. pastoris-derived protein	1004:1032	This represents the first localization of an O-linked glycan in a P. pastoris-derived protein.
10029548	7	40	theme	hTF/2N	1258:1263	arg1	production					1244:1253	the production	1240:1253	the production of hTF/2N	1240:1263	Because of its distance from the iron-binding site, glycosylation of Ser-32 should not affect the iron-binding properties of hTF/2N expressed in P. pastoris, making this an excellent expression system for the production of hTF/2N.
10029548	3	41	theme	protein	520:526	arg1	structure					528:536	only the second P. pastoris-derived protein structure	484:536	only the second P. pastoris-derived protein structure determined to date	484:555	This represents only the second P. pastoris-derived protein structure determined to date, and allows the comparison of the structures of recombinant Fe(III)-hTF/2N expressed in P. pastoris and mammalian cells with serum-derived transferrin.
10029548	3	42	link	pastoris-derived	503:518	arg1	structure					528:536	only the second P. pastoris-derived protein structure	484:536	only the second P. pastoris-derived protein structure determined to date	484:555	This represents only the second P. pastoris-derived protein structure determined to date, and allows the comparison of the structures of recombinant Fe(III)-hTF/2N expressed in P. pastoris and mammalian cells with serum-derived transferrin.
10029548	3	43	theme	serum-derived	682:694	arg1	transferrin					696:706	serum-derived transferrin	682:706	serum-derived transferrin	682:706	This represents only the second P. pastoris-derived protein structure determined to date, and allows the comparison of the structures of recombinant Fe(III)-hTF/2N expressed in P. pastoris and mammalian cells with serum-derived transferrin.
10029548	3	44	theme	second	493:498	arg1	structure					528:536	only the second P. pastoris-derived protein structure	484:536	only the second P. pastoris-derived protein structure determined to date	484:555	This represents only the second P. pastoris-derived protein structure determined to date, and allows the comparison of the structures of recombinant Fe(III)-hTF/2N expressed in P. pastoris and mammalian cells with serum-derived transferrin.
10029548	5	45	theme	P.	827:828	arg1	hTF/2N					840:845	P. pastoris- hTF/2N	827:845	P. pastoris- hTF/2N	827:845	Mass spectroscopic analyses of P. pastoris- hTF/2N and proteolytically derived fragments revealed glycosylation of Ser-32 with a single hexose.
10029548	7	46	theme	iron-binding	1068:1079	arg1	site					1081:1084	the iron-binding site	1064:1084	the iron-binding site	1064:1084	Because of its distance from the iron-binding site, glycosylation of Ser-32 should not affect the iron-binding properties of hTF/2N expressed in P. pastoris, making this an excellent expression system for the production of hTF/2N.
10029548	1	47	theme	high	267:270	arg1	levels					272:277	high levels	267:277	high levels in Pichia pastoris	267:296	The ferric form of the N-lobe of human serum transferrin (Fe(III)-hTF/2N) has been expressed at high levels in Pichia pastoris.
10029548	3	48	theme	P.	500:501	arg1	structure					528:536	only the second P. pastoris-derived protein structure	484:536	only the second P. pastoris-derived protein structure determined to date	484:555	This represents only the second P. pastoris-derived protein structure determined to date, and allows the comparison of the structures of recombinant Fe(III)-hTF/2N expressed in P. pastoris and mammalian cells with serum-derived transferrin.
10029548	5	49	theme	pastoris-	830:838	arg1	hTF/2N					840:845	P. pastoris- hTF/2N	827:845	P. pastoris- hTF/2N	827:845	Mass spectroscopic analyses of P. pastoris- hTF/2N and proteolytically derived fragments revealed glycosylation of Ser-32 with a single hexose.
10029548	3	50	theme	cells	671:675	arg1	comparison					573:582	the comparison	569:582	the comparison of the structures of recombinant Fe(III)-hTF/2N expressed in P. pastoris and mammalian cells with serum-derived transferrin	569:706	This represents only the second P. pastoris-derived protein structure determined to date, and allows the comparison of the structures of recombinant Fe(III)-hTF/2N expressed in P. pastoris and mammalian cells with serum-derived transferrin.
10029548	3	51	theme	structures	591:600	arg1	comparison					573:582	the comparison	569:582	the comparison of the structures of recombinant Fe(III)-hTF/2N expressed in P. pastoris and mammalian cells with serum-derived transferrin	569:706	This represents only the second P. pastoris-derived protein structure determined to date, and allows the comparison of the structures of recombinant Fe(III)-hTF/2N expressed in P. pastoris and mammalian cells with serum-derived transferrin.
10029548	3	52	link	serum-derived	682:694	arg1	transferrin					696:706	serum-derived transferrin	682:706	serum-derived transferrin	682:706	This represents only the second P. pastoris-derived protein structure determined to date, and allows the comparison of the structures of recombinant Fe(III)-hTF/2N expressed in P. pastoris and mammalian cells with serum-derived transferrin.
10029548	5	53	theme	hTF/2N	840:845	arg1	analyses					815:822	Mass spectroscopic analyses	796:822	Mass spectroscopic analyses of P. pastoris- hTF/2N and proteolytically derived fragments	796:883	Mass spectroscopic analyses of P. pastoris- hTF/2N and proteolytically derived fragments revealed glycosylation of Ser-32 with a single hexose.
10029548	1	54	theme	human	204:208	arg1	transferrin					216:226	human serum transferrin	204:226	human serum transferrin (Fe(III)-hTF/2N)	204:243	The ferric form of the N-lobe of human serum transferrin (Fe(III)-hTF/2N) has been expressed at high levels in Pichia pastoris.
10029548	1	54	theme	human	204:208	arg1	-hTF/2N					236:242	Fe(III)-hTF/2N	229:242	Fe(III)-hTF/2N	229:242	The ferric form of the N-lobe of human serum transferrin (Fe(III)-hTF/2N) has been expressed at high levels in Pichia pastoris.
10029548	5	55	theme	single	925:930	arg1	hexose					932:937	a single hexose	923:937	a single hexose	923:937	Mass spectroscopic analyses of P. pastoris- hTF/2N and proteolytically derived fragments revealed glycosylation of Ser-32 with a single hexose.
10029548	5	56	theme	spectroscopic	801:813	arg1	analyses					815:822	Mass spectroscopic analyses	796:822	Mass spectroscopic analyses of P. pastoris- hTF/2N and proteolytically derived fragments	796:883	Mass spectroscopic analyses of P. pastoris- hTF/2N and proteolytically derived fragments revealed glycosylation of Ser-32 with a single hexose.
10029548	5	57	link	derived	867:873	arg1	fragments					875:883	proteolytically derived fragments	851:883	proteolytically derived fragments	851:883	Mass spectroscopic analyses of P. pastoris- hTF/2N and proteolytically derived fragments revealed glycosylation of Ser-32 with a single hexose.
10029548	1	58	theme	serum	210:214	arg1	transferrin					216:226	human serum transferrin	204:226	human serum transferrin (Fe(III)-hTF/2N)	204:243	The ferric form of the N-lobe of human serum transferrin (Fe(III)-hTF/2N) has been expressed at high levels in Pichia pastoris.
10029548	1	58	theme	serum	210:214	arg1	-hTF/2N					236:242	Fe(III)-hTF/2N	229:242	Fe(III)-hTF/2N	229:242	The ferric form of the N-lobe of human serum transferrin (Fe(III)-hTF/2N) has been expressed at high levels in Pichia pastoris.
10029548	7	59	theme	hTF/2N	1160:1165	arg1	properties					1146:1155	the iron-binding properties	1129:1155	the iron-binding properties of hTF/2N expressed in P. pastoris	1129:1190	Because of its distance from the iron-binding site, glycosylation of Ser-32 should not affect the iron-binding properties of hTF/2N expressed in P. pastoris, making this an excellent expression system for the production of hTF/2N.
10029548	4	60	theme	polypeptide	713:723	arg1	pattern					733:739	The polypeptide folding pattern	709:739	The polypeptide folding pattern	709:739	The polypeptide folding pattern is essentially identical in all of the three proteins.
10029548	4	60	theme	polypeptide	713:723	arg1	identical					756:764	identical	756:764	identical	756:764	The polypeptide folding pattern is essentially identical in all of the three proteins.
10029548	6	61	theme	O-linked	985:992	arg1	glycan					994:999	an O-linked glycan	982:999	an O-linked glycan	982:999	This represents the first localization of an O-linked glycan in a P. pastoris-derived protein.
10029548	5	62	theme	Mass	796:799	arg1	analyses					815:822	Mass spectroscopic analyses	796:822	Mass spectroscopic analyses of P. pastoris- hTF/2N and proteolytically derived fragments	796:883	Mass spectroscopic analyses of P. pastoris- hTF/2N and proteolytically derived fragments revealed glycosylation of Ser-32 with a single hexose.
10029548	2	63	used	used	392:395	arg2	crystallography					372:386	X-ray crystallography	366:386	X-ray crystallography	366:386	The Fe(III)-hTF/2N was crystallized in the space group P41212, and X-ray crystallography was used to solve the structure of the recombinant protein at 2.5 A resolution.
10029548	1	64	theme	transferrin	216:226	arg1	transferrin					216:226	human serum transferrin	204:226	human serum transferrin (Fe(III)-hTF/2N)	204:243	The ferric form of the N-lobe of human serum transferrin (Fe(III)-hTF/2N) has been expressed at high levels in Pichia pastoris.
10029548	1	64	theme	transferrin	216:226	arg1	N-lobe					194:199	the N-lobe	190:199	the N-lobe of human serum transferrin (Fe(III)-hTF/2N)	190:243	The ferric form of the N-lobe of human serum transferrin (Fe(III)-hTF/2N) has been expressed at high levels in Pichia pastoris.
10029548	5	65	gly	glycosylation	894:906	arg1	Ser-32					911:916	Ser-32	911:916	Ser-32	911:916	Mass spectroscopic analyses of P. pastoris- hTF/2N and proteolytically derived fragments revealed glycosylation of Ser-32 with a single hexose.
10029548	3	66	theme	Fe	617:618	arg1	-hTF/2N					624:630	recombinant Fe(III)-hTF/2N	605:630	recombinant Fe(III)-hTF/2N expressed in P. pastoris	605:655	This represents only the second P. pastoris-derived protein structure determined to date, and allows the comparison of the structures of recombinant Fe(III)-hTF/2N expressed in P. pastoris and mammalian cells with serum-derived transferrin.
10029548	7	67	gly	glycosylation	1087:1099	arg1	Ser-32					1104:1109	Ser-32	1104:1109	Ser-32	1104:1109	Because of its distance from the iron-binding site, glycosylation of Ser-32 should not affect the iron-binding properties of hTF/2N expressed in P. pastoris, making this an excellent expression system for the production of hTF/2N.
10029548	7	67	gly	glycosylation	1087:1099	arg1	hTF/2N					1160:1165	hTF/2N	1160:1165	hTF/2N expressed in P. pastoris	1160:1190	Because of its distance from the iron-binding site, glycosylation of Ser-32 should not affect the iron-binding properties of hTF/2N expressed in P. pastoris, making this an excellent expression system for the production of hTF/2N.
10029548	0	68	gly	glycosylated	144:155	arg2	N-lobe					60:65	the N-lobe	56:65	the N-lobe of human transferrin expressed in Pichia pastoris	56:115	X-ray crystallography and mass spectroscopy reveal that the N-lobe of human transferrin expressed in Pichia pastoris is folded correctly but is glycosylated on serine-32.
10029548	0	68	gly	glycosylated	144:155	arg2	transferrin					76:86	human transferrin	70:86	human transferrin expressed in Pichia pastoris	70:115	X-ray crystallography and mass spectroscopy reveal that the N-lobe of human transferrin expressed in Pichia pastoris is folded correctly but is glycosylated on serine-32.
10029548	0	68	gly	glycosylated	144:155	arg1	N-lobe					60:65	the N-lobe	56:65	the N-lobe of human transferrin expressed in Pichia pastoris	56:115	X-ray crystallography and mass spectroscopy reveal that the N-lobe of human transferrin expressed in Pichia pastoris is folded correctly but is glycosylated on serine-32.
10029548	0	68	gly	glycosylated	144:155	arg1	serine-32					160:168	serine-32	160:168	serine-32	160:168	X-ray crystallography and mass spectroscopy reveal that the N-lobe of human transferrin expressed in Pichia pastoris is folded correctly but is glycosylated on serine-32.
10029548	0	68	gly	glycosylated	144:155	arg1	transferrin					76:86	human transferrin	70:86	human transferrin expressed in Pichia pastoris	70:115	X-ray crystallography and mass spectroscopy reveal that the N-lobe of human transferrin expressed in Pichia pastoris is folded correctly but is glycosylated on serine-32.
10029548	0	68	gly	glycosylated	144:155	arg2	serine-32					160:168	serine-32	160:168	serine-32	160:168	X-ray crystallography and mass spectroscopy reveal that the N-lobe of human transferrin expressed in Pichia pastoris is folded correctly but is glycosylated on serine-32.
10029548	7	69	theme	iron-binding	1133:1144	arg1	properties					1146:1155	the iron-binding properties	1129:1155	the iron-binding properties of hTF/2N expressed in P. pastoris	1129:1190	Because of its distance from the iron-binding site, glycosylation of Ser-32 should not affect the iron-binding properties of hTF/2N expressed in P. pastoris, making this an excellent expression system for the production of hTF/2N.
12874386	1	0	gly	glycosylation	77:89	arg1	serine					94:99	serine	94:99	serine	94:99	The glycosylation of serine and threonine residues with a single GlcNAc moiety is a dynamic posttranslational modification of many nuclear and cytoplasmic proteins.
12874386	1	0	gly	glycosylation	77:89	arg1	threonine					105:113	threonine	105:113	threonine	105:113	The glycosylation of serine and threonine residues with a single GlcNAc moiety is a dynamic posttranslational modification of many nuclear and cytoplasmic proteins.
12874386	3	1	from	enzyme	410:415	arg1	pathway					443:449	the hexosamine salvage pathway	420:449	the hexosamine salvage pathway	420:449	We demonstrate, in vitro, that each enzyme in the hexosamine salvage pathway, and the enzymes that affect this dynamic modification (UDP-GlcNAc:polypeptidtyltransferase and O-GlcNAcase), tolerate analogues of their natural substrates in which the N-acyl side chain has been modified to bear a bio-orthogonal azide moiety.
12874386	6	2	theme	p62	1110:1112	arg1	labeling					1077:1084	metabolic labeling	1067:1084	metabolic labeling	1067:1084	The approach was validated by metabolic labeling of nuclear pore protein p62, which is known to be posttranslationally modified with O-GlcNAc.
12874386	7	3	theme	residues	1306:1313	arg1	identification					1225:1238	the identification	1221:1238	the identification of O-GlcNAc-modified proteins	1221:1268	This strategy will prove useful for both the identification of O-GlcNAc-modified proteins and the elucidation of the specific residues that bear this saccharide.
12874386	7	3	theme	residues	1306:1313	arg1	elucidation					1278:1288	the elucidation	1274:1288	the elucidation of the specific residues that bear this saccharide	1274:1339	This strategy will prove useful for both the identification of O-GlcNAc-modified proteins and the elucidation of the specific residues that bear this saccharide.
12874386	1	4	dep	serine	94:99	arg1	residues					115:122	residues	115:122	residues	115:122	The glycosylation of serine and threonine residues with a single GlcNAc moiety is a dynamic posttranslational modification of many nuclear and cytoplasmic proteins.
12874386	4	5	with	treatment	709:717	arg1	N-azidoacetylglucosamine					733:756	N-azidoacetylglucosamine	733:756	N-azidoacetylglucosamine	733:756	Accordingly, treatment of cells with N-azidoacetylglucosamine results in the metabolic incorporation of the azido sugar into nuclear and cytoplasmic proteins.
12874386	5	6	theme	Staudinger	1016:1025	arg1	ligation					1027:1034	the Staudinger ligation	1012:1034	the Staudinger ligation	1012:1034	These O-azidoacetylglucosamine-modified proteins can be covalently derivatized with various biochemical probes at the site of protein glycosylation by using the Staudinger ligation.
12874386	2	7	from	cells	337:341	arg1	proteins					346:353	proteins	346:353	proteins modified in vitro	346:371	We describe a chemical strategy directed toward identifying O-GlcNAc-modified proteins from living cells or proteins modified in vitro.
12874386	2	7	from	cells	337:341	arg1	proteins					316:323	O-GlcNAc-modified proteins	298:323	O-GlcNAc-modified proteins from living cells	298:341	We describe a chemical strategy directed toward identifying O-GlcNAc-modified proteins from living cells or proteins modified in vitro.
12874386	5	8	gly	glycosylation	989:1001	arg2	glycosylation					989:1001	protein glycosylation	981:1001	protein glycosylation	981:1001	These O-azidoacetylglucosamine-modified proteins can be covalently derivatized with various biochemical probes at the site of protein glycosylation by using the Staudinger ligation.
12874386	5	8	gly	glycosylation	989:1001	arg2	site					973:976	the site	969:976	the site of protein glycosylation	969:1001	These O-azidoacetylglucosamine-modified proteins can be covalently derivatized with various biochemical probes at the site of protein glycosylation by using the Staudinger ligation.
12874386	4	9	theme	metabolic	773:781	arg1	incorporation					783:795	the metabolic incorporation	769:795	the metabolic incorporation of the azido sugar into nuclear and cytoplasmic proteins	769:852	Accordingly, treatment of cells with N-azidoacetylglucosamine results in the metabolic incorporation of the azido sugar into nuclear and cytoplasmic proteins.
12874386	2	10	theme	O-GlcNAc-modified	298:314	arg1	proteins					316:323	O-GlcNAc-modified proteins	298:323	O-GlcNAc-modified proteins from living cells	298:341	We describe a chemical strategy directed toward identifying O-GlcNAc-modified proteins from living cells or proteins modified in vitro.
12874386	4	11	theme	cells	722:726	arg1	treatment					709:717	treatment	709:717	treatment of cells with N-azidoacetylglucosamine	709:756	Accordingly, treatment of cells with N-azidoacetylglucosamine results in the metabolic incorporation of the azido sugar into nuclear and cytoplasmic proteins.
12874386	7	12	theme	O-GlcNAc-modified	1243:1259	arg1	proteins					1261:1268	O-GlcNAc-modified proteins	1243:1268	O-GlcNAc-modified proteins	1243:1268	This strategy will prove useful for both the identification of O-GlcNAc-modified proteins and the elucidation of the specific residues that bear this saccharide.
12874386	0	13	from	proteins	54:61	arg1	cells					66:70	cells	66:70	cells	66:70	A chemical approach for identifying O-GlcNAc-modified proteins in cells.
12874386	5	14	theme	O-azidoacetylglucosamine-modified	861:893	arg1	proteins					895:902	These O-azidoacetylglucosamine-modified proteins	855:902	These O-azidoacetylglucosamine-modified proteins	855:902	These O-azidoacetylglucosamine-modified proteins can be covalently derivatized with various biochemical probes at the site of protein glycosylation by using the Staudinger ligation.
12874386	6	15	theme	nuclear	1089:1095	arg1	p62					1110:1112	nuclear pore protein p62	1089:1112	nuclear pore protein p62	1089:1112	The approach was validated by metabolic labeling of nuclear pore protein p62, which is known to be posttranslationally modified with O-GlcNAc.
12874386	1	16	theme	dynamic	157:163	arg1	modification					183:194	a dynamic posttranslational modification	155:194	a dynamic posttranslational modification of many nuclear and cytoplasmic proteins	155:235	The glycosylation of serine and threonine residues with a single GlcNAc moiety is a dynamic posttranslational modification of many nuclear and cytoplasmic proteins.
12874386	1	16	theme	dynamic	157:163	arg1	glycosylation					77:89	The glycosylation	73:89	The glycosylation of serine and threonine residues with a single GlcNAc moiety	73:150	The glycosylation of serine and threonine residues with a single GlcNAc moiety is a dynamic posttranslational modification of many nuclear and cytoplasmic proteins.
12874386	7	17	theme	proteins	1261:1268	arg1	identification					1225:1238	the identification	1221:1238	the identification of O-GlcNAc-modified proteins	1221:1268	This strategy will prove useful for both the identification of O-GlcNAc-modified proteins and the elucidation of the specific residues that bear this saccharide.
12874386	7	17	theme	proteins	1261:1268	arg1	elucidation					1278:1288	the elucidation	1274:1288	the elucidation of the specific residues that bear this saccharide	1274:1339	This strategy will prove useful for both the identification of O-GlcNAc-modified proteins and the elucidation of the specific residues that bear this saccharide.
12874386	3	18	dep	modification	493:504	arg1	UDP-GlcNAc					507:516	UDP-GlcNAc	507:516	UDP-GlcNAc:polypeptidtyltransferase and O-GlcNAcase	507:557	We demonstrate, in vitro, that each enzyme in the hexosamine salvage pathway, and the enzymes that affect this dynamic modification (UDP-GlcNAc:polypeptidtyltransferase and O-GlcNAcase), tolerate analogues of their natural substrates in which the N-acyl side chain has been modified to bear a bio-orthogonal azide moiety.
12874386	1	19	theme	posttranslational	165:181	arg1	modification					183:194	a dynamic posttranslational modification	155:194	a dynamic posttranslational modification of many nuclear and cytoplasmic proteins	155:235	The glycosylation of serine and threonine residues with a single GlcNAc moiety is a dynamic posttranslational modification of many nuclear and cytoplasmic proteins.
12874386	1	19	theme	posttranslational	165:181	arg1	glycosylation					77:89	The glycosylation	73:89	The glycosylation of serine and threonine residues with a single GlcNAc moiety	73:150	The glycosylation of serine and threonine residues with a single GlcNAc moiety is a dynamic posttranslational modification of many nuclear and cytoplasmic proteins.
12874386	0	20	theme	chemical	2:9	arg1	approach					11:18	A chemical approach	0:18	A chemical approach for identifying O-GlcNAc-modified proteins in cells	0:70	A chemical approach for identifying O-GlcNAc-modified proteins in cells.
12874386	5	21	theme	glycosylation	989:1001	arg1	site					973:976	the site	969:976	the site of protein glycosylation	969:1001	These O-azidoacetylglucosamine-modified proteins can be covalently derivatized with various biochemical probes at the site of protein glycosylation by using the Staudinger ligation.
12874386	5	21	theme	glycosylation	989:1001	arg1	glycosylation					989:1001	protein glycosylation	981:1001	protein glycosylation	981:1001	These O-azidoacetylglucosamine-modified proteins can be covalently derivatized with various biochemical probes at the site of protein glycosylation by using the Staudinger ligation.
12874386	3	22	theme	hexosamine	424:433	arg1	pathway					443:449	the hexosamine salvage pathway	420:449	the hexosamine salvage pathway	420:449	We demonstrate, in vitro, that each enzyme in the hexosamine salvage pathway, and the enzymes that affect this dynamic modification (UDP-GlcNAc:polypeptidtyltransferase and O-GlcNAcase), tolerate analogues of their natural substrates in which the N-acyl side chain has been modified to bear a bio-orthogonal azide moiety.
12874386	1	23	theme	serine	94:99	arg1	modification					183:194	a dynamic posttranslational modification	155:194	a dynamic posttranslational modification of many nuclear and cytoplasmic proteins	155:235	The glycosylation of serine and threonine residues with a single GlcNAc moiety is a dynamic posttranslational modification of many nuclear and cytoplasmic proteins.
12874386	1	23	theme	serine	94:99	arg1	glycosylation					77:89	The glycosylation	73:89	The glycosylation of serine and threonine residues with a single GlcNAc moiety	73:150	The glycosylation of serine and threonine residues with a single GlcNAc moiety is a dynamic posttranslational modification of many nuclear and cytoplasmic proteins.
12874386	3	24	theme	salvage	435:441	arg1	pathway					443:449	the hexosamine salvage pathway	420:449	the hexosamine salvage pathway	420:449	We demonstrate, in vitro, that each enzyme in the hexosamine salvage pathway, and the enzymes that affect this dynamic modification (UDP-GlcNAc:polypeptidtyltransferase and O-GlcNAcase), tolerate analogues of their natural substrates in which the N-acyl side chain has been modified to bear a bio-orthogonal azide moiety.
12874386	4	25	theme	nuclear	821:827	arg1	proteins					845:852	nuclear and cytoplasmic proteins	821:852	nuclear and cytoplasmic proteins	821:852	Accordingly, treatment of cells with N-azidoacetylglucosamine results in the metabolic incorporation of the azido sugar into nuclear and cytoplasmic proteins.
12874386	5	26	theme	protein	981:987	arg1	glycosylation					989:1001	protein glycosylation	981:1001	protein glycosylation	981:1001	These O-azidoacetylglucosamine-modified proteins can be covalently derivatized with various biochemical probes at the site of protein glycosylation by using the Staudinger ligation.
12874386	2	27	theme	living	330:335	arg1	cells					337:341	living cells	330:341	living cells	330:341	We describe a chemical strategy directed toward identifying O-GlcNAc-modified proteins from living cells or proteins modified in vitro.
12874386	1	28	theme	many	199:202	arg1	proteins					228:235	many nuclear and cytoplasmic proteins	199:235	many nuclear and cytoplasmic proteins	199:235	The glycosylation of serine and threonine residues with a single GlcNAc moiety is a dynamic posttranslational modification of many nuclear and cytoplasmic proteins.
12874386	3	29	dep	UDP-GlcNAc	507:516	arg1	O-GlcNAcase					547:557	O-GlcNAcase	547:557	O-GlcNAcase	547:557	We demonstrate, in vitro, that each enzyme in the hexosamine salvage pathway, and the enzymes that affect this dynamic modification (UDP-GlcNAc:polypeptidtyltransferase and O-GlcNAcase), tolerate analogues of their natural substrates in which the N-acyl side chain has been modified to bear a bio-orthogonal azide moiety.
12874386	3	29	dep	UDP-GlcNAc	507:516	arg1	polypeptidtyltransferase					518:541	polypeptidtyltransferase	518:541	polypeptidtyltransferase	518:541	We demonstrate, in vitro, that each enzyme in the hexosamine salvage pathway, and the enzymes that affect this dynamic modification (UDP-GlcNAc:polypeptidtyltransferase and O-GlcNAcase), tolerate analogues of their natural substrates in which the N-acyl side chain has been modified to bear a bio-orthogonal azide moiety.
12874386	1	30	theme	threonine	105:113	arg1	modification					183:194	a dynamic posttranslational modification	155:194	a dynamic posttranslational modification of many nuclear and cytoplasmic proteins	155:235	The glycosylation of serine and threonine residues with a single GlcNAc moiety is a dynamic posttranslational modification of many nuclear and cytoplasmic proteins.
12874386	1	30	theme	threonine	105:113	arg1	glycosylation					77:89	The glycosylation	73:89	The glycosylation of serine and threonine residues with a single GlcNAc moiety	73:150	The glycosylation of serine and threonine residues with a single GlcNAc moiety is a dynamic posttranslational modification of many nuclear and cytoplasmic proteins.
12874386	6	31	mod	modified	1156:1163	arg1	labeling					1077:1084	metabolic labeling	1067:1084	metabolic labeling	1067:1084	The approach was validated by metabolic labeling of nuclear pore protein p62, which is known to be posttranslationally modified with O-GlcNAc.
12874386	6	31	mod	modified	1156:1163	arg3	O-GlcNAc					1170:1177	O-GlcNAc	1170:1177	O-GlcNAc	1170:1177	The approach was validated by metabolic labeling of nuclear pore protein p62, which is known to be posttranslationally modified with O-GlcNAc.
12874386	1	32	theme	nuclear	204:210	arg1	proteins					228:235	many nuclear and cytoplasmic proteins	199:235	many nuclear and cytoplasmic proteins	199:235	The glycosylation of serine and threonine residues with a single GlcNAc moiety is a dynamic posttranslational modification of many nuclear and cytoplasmic proteins.
12874386	0	33	theme	O-GlcNAc-modified	36:52	arg1	proteins					54:61	O-GlcNAc-modified proteins	36:61	O-GlcNAc-modified proteins in cells	36:70	A chemical approach for identifying O-GlcNAc-modified proteins in cells.
12874386	4	34	theme	cytoplasmic	833:843	arg1	proteins					845:852	nuclear and cytoplasmic proteins	821:852	nuclear and cytoplasmic proteins	821:852	Accordingly, treatment of cells with N-azidoacetylglucosamine results in the metabolic incorporation of the azido sugar into nuclear and cytoplasmic proteins.
12874386	6	35	theme	protein	1102:1108	arg1	p62					1110:1112	nuclear pore protein p62	1089:1112	nuclear pore protein p62	1089:1112	The approach was validated by metabolic labeling of nuclear pore protein p62, which is known to be posttranslationally modified with O-GlcNAc.
12874386	1	36	with	glycosylation	77:89	arg1	moiety					145:150	a single GlcNAc moiety	129:150	a single GlcNAc moiety	129:150	The glycosylation of serine and threonine residues with a single GlcNAc moiety is a dynamic posttranslational modification of many nuclear and cytoplasmic proteins.
12874386	1	37	theme	cytoplasmic	216:226	arg1	proteins					228:235	many nuclear and cytoplasmic proteins	199:235	many nuclear and cytoplasmic proteins	199:235	The glycosylation of serine and threonine residues with a single GlcNAc moiety is a dynamic posttranslational modification of many nuclear and cytoplasmic proteins.
12874386	5	38	theme	various	939:945	arg1	probes					959:964	various biochemical probes	939:964	various biochemical probes at the site of protein glycosylation	939:1001	These O-azidoacetylglucosamine-modified proteins can be covalently derivatized with various biochemical probes at the site of protein glycosylation by using the Staudinger ligation.
12874386	3	39	theme	natural	589:595	arg1	substrates					597:606	their natural substrates	583:606	their natural substrates	583:606	We demonstrate, in vitro, that each enzyme in the hexosamine salvage pathway, and the enzymes that affect this dynamic modification (UDP-GlcNAc:polypeptidtyltransferase and O-GlcNAcase), tolerate analogues of their natural substrates in which the N-acyl side chain has been modified to bear a bio-orthogonal azide moiety.
12874386	3	40	theme	dynamic	485:491	arg1	modification					493:504	this dynamic modification	480:504	this dynamic modification (UDP-GlcNAc:polypeptidtyltransferase and O-GlcNAcase)	480:558	We demonstrate, in vitro, that each enzyme in the hexosamine salvage pathway, and the enzymes that affect this dynamic modification (UDP-GlcNAc:polypeptidtyltransferase and O-GlcNAcase), tolerate analogues of their natural substrates in which the N-acyl side chain has been modified to bear a bio-orthogonal azide moiety.
12874386	7	41	contain	bear	1320:1323	arg1	residues					1306:1313	the specific residues	1293:1313	the specific residues that bear this saccharide	1293:1339	This strategy will prove useful for both the identification of O-GlcNAc-modified proteins and the elucidation of the specific residues that bear this saccharide.
12874386	7	41	contain	bear	1320:1323	arg2	saccharide					1330:1339	this saccharide	1325:1339	this saccharide	1325:1339	This strategy will prove useful for both the identification of O-GlcNAc-modified proteins and the elucidation of the specific residues that bear this saccharide.
12874386	3	42	theme	bio-orthogonal	667:680	arg1	moiety					688:693	a bio-orthogonal azide moiety	665:693	a bio-orthogonal azide moiety	665:693	We demonstrate, in vitro, that each enzyme in the hexosamine salvage pathway, and the enzymes that affect this dynamic modification (UDP-GlcNAc:polypeptidtyltransferase and O-GlcNAcase), tolerate analogues of their natural substrates in which the N-acyl side chain has been modified to bear a bio-orthogonal azide moiety.
12874386	3	43	theme	substrates	597:606	arg1	analogues					570:578	analogues	570:578	analogues of their natural substrates in which the N-acyl side chain has been modified to bear a bio-orthogonal azide moiety	570:693	We demonstrate, in vitro, that each enzyme in the hexosamine salvage pathway, and the enzymes that affect this dynamic modification (UDP-GlcNAc:polypeptidtyltransferase and O-GlcNAcase), tolerate analogues of their natural substrates in which the N-acyl side chain has been modified to bear a bio-orthogonal azide moiety.
12874386	3	44	from	enzymes	460:466	arg1	pathway					443:449	the hexosamine salvage pathway	420:449	the hexosamine salvage pathway	420:449	We demonstrate, in vitro, that each enzyme in the hexosamine salvage pathway, and the enzymes that affect this dynamic modification (UDP-GlcNAc:polypeptidtyltransferase and O-GlcNAcase), tolerate analogues of their natural substrates in which the N-acyl side chain has been modified to bear a bio-orthogonal azide moiety.
12874386	5	45	from	site	973:976	arg1	probes					959:964	various biochemical probes	939:964	various biochemical probes at the site of protein glycosylation	939:1001	These O-azidoacetylglucosamine-modified proteins can be covalently derivatized with various biochemical probes at the site of protein glycosylation by using the Staudinger ligation.
12874386	3	46	theme	azide	682:686	arg1	moiety					688:693	a bio-orthogonal azide moiety	665:693	a bio-orthogonal azide moiety	665:693	We demonstrate, in vitro, that each enzyme in the hexosamine salvage pathway, and the enzymes that affect this dynamic modification (UDP-GlcNAc:polypeptidtyltransferase and O-GlcNAcase), tolerate analogues of their natural substrates in which the N-acyl side chain has been modified to bear a bio-orthogonal azide moiety.
12874386	3	47	theme	side	628:631	arg1	chain					633:637	the N-acyl side chain	617:637	the N-acyl side chain	617:637	We demonstrate, in vitro, that each enzyme in the hexosamine salvage pathway, and the enzymes that affect this dynamic modification (UDP-GlcNAc:polypeptidtyltransferase and O-GlcNAcase), tolerate analogues of their natural substrates in which the N-acyl side chain has been modified to bear a bio-orthogonal azide moiety.
12874386	1	48	theme	proteins	228:235	arg1	modification					183:194	a dynamic posttranslational modification	155:194	a dynamic posttranslational modification of many nuclear and cytoplasmic proteins	155:235	The glycosylation of serine and threonine residues with a single GlcNAc moiety is a dynamic posttranslational modification of many nuclear and cytoplasmic proteins.
12874386	1	48	theme	proteins	228:235	arg1	glycosylation					77:89	The glycosylation	73:89	The glycosylation of serine and threonine residues with a single GlcNAc moiety	73:150	The glycosylation of serine and threonine residues with a single GlcNAc moiety is a dynamic posttranslational modification of many nuclear and cytoplasmic proteins.
12874386	4	49	theme	azido	804:808	arg1	sugar					810:814	the azido sugar	800:814	the azido sugar	800:814	Accordingly, treatment of cells with N-azidoacetylglucosamine results in the metabolic incorporation of the azido sugar into nuclear and cytoplasmic proteins.
12874386	1	50	theme	single	131:136	arg1	moiety					145:150	a single GlcNAc moiety	129:150	a single GlcNAc moiety	129:150	The glycosylation of serine and threonine residues with a single GlcNAc moiety is a dynamic posttranslational modification of many nuclear and cytoplasmic proteins.
12874386	4	51	theme	sugar	810:814	arg1	incorporation					783:795	the metabolic incorporation	769:795	the metabolic incorporation of the azido sugar into nuclear and cytoplasmic proteins	769:852	Accordingly, treatment of cells with N-azidoacetylglucosamine results in the metabolic incorporation of the azido sugar into nuclear and cytoplasmic proteins.
12874386	6	52	theme	pore	1097:1100	arg1	p62					1110:1112	nuclear pore protein p62	1089:1112	nuclear pore protein p62	1089:1112	The approach was validated by metabolic labeling of nuclear pore protein p62, which is known to be posttranslationally modified with O-GlcNAc.
12874386	2	53	theme	chemical	252:259	arg1	strategy					261:268	a chemical strategy	250:268	a chemical strategy directed toward identifying O-GlcNAc-modified proteins from living cells or proteins modified in vitro	250:371	We describe a chemical strategy directed toward identifying O-GlcNAc-modified proteins from living cells or proteins modified in vitro.
12874386	1	54	theme	GlcNAc	138:143	arg1	moiety					145:150	a single GlcNAc moiety	129:150	a single GlcNAc moiety	129:150	The glycosylation of serine and threonine residues with a single GlcNAc moiety is a dynamic posttranslational modification of many nuclear and cytoplasmic proteins.
12874386	3	55	contain	bear	660:663	arg2	moiety					688:693	a bio-orthogonal azide moiety	665:693	a bio-orthogonal azide moiety	665:693	We demonstrate, in vitro, that each enzyme in the hexosamine salvage pathway, and the enzymes that affect this dynamic modification (UDP-GlcNAc:polypeptidtyltransferase and O-GlcNAcase), tolerate analogues of their natural substrates in which the N-acyl side chain has been modified to bear a bio-orthogonal azide moiety.
12874386	3	55	contain	bear	660:663	arg1	chain					633:637	the N-acyl side chain	617:637	the N-acyl side chain	617:637	We demonstrate, in vitro, that each enzyme in the hexosamine salvage pathway, and the enzymes that affect this dynamic modification (UDP-GlcNAc:polypeptidtyltransferase and O-GlcNAcase), tolerate analogues of their natural substrates in which the N-acyl side chain has been modified to bear a bio-orthogonal azide moiety.
12874386	7	56	theme	specific	1297:1304	arg1	residues					1306:1313	the specific residues	1293:1313	the specific residues that bear this saccharide	1293:1339	This strategy will prove useful for both the identification of O-GlcNAc-modified proteins and the elucidation of the specific residues that bear this saccharide.
12874386	3	57	theme	N-acyl	621:626	arg1	chain					633:637	the N-acyl side chain	617:637	the N-acyl side chain	617:637	We demonstrate, in vitro, that each enzyme in the hexosamine salvage pathway, and the enzymes that affect this dynamic modification (UDP-GlcNAc:polypeptidtyltransferase and O-GlcNAcase), tolerate analogues of their natural substrates in which the N-acyl side chain has been modified to bear a bio-orthogonal azide moiety.
12874386	5	58	theme	biochemical	947:957	arg1	probes					959:964	various biochemical probes	939:964	various biochemical probes at the site of protein glycosylation	939:1001	These O-azidoacetylglucosamine-modified proteins can be covalently derivatized with various biochemical probes at the site of protein glycosylation by using the Staudinger ligation.
12874386	6	59	theme	metabolic	1067:1075	arg1	labeling					1077:1084	metabolic labeling	1067:1084	metabolic labeling	1067:1084	The approach was validated by metabolic labeling of nuclear pore protein p62, which is known to be posttranslationally modified with O-GlcNAc.
11231274	0	0	from	study	14:18	arg1	siglec-7					75:82	siglec-7	75:82	siglec-7	75:82	A comparative study of the asparagine-linked oligosaccharides on siglec-5, siglec-7 and siglec-8, expressed in a CHO cell line, and their contribution to ligand recognition.
11231274	0	0	from	study	14:18	arg1	siglec-5					65:72	siglec-5	65:72	siglec-5	65:72	A comparative study of the asparagine-linked oligosaccharides on siglec-5, siglec-7 and siglec-8, expressed in a CHO cell line, and their contribution to ligand recognition.
11231274	0	0	from	study	14:18	arg1	siglec-8					88:95	siglec-8	88:95	siglec-8	88:95	A comparative study of the asparagine-linked oligosaccharides on siglec-5, siglec-7 and siglec-8, expressed in a CHO cell line, and their contribution to ligand recognition.
11231274	0	1	theme	ligand	154:159	arg1	recognition					161:171	ligand recognition	154:171	ligand recognition	154:171	A comparative study of the asparagine-linked oligosaccharides on siglec-5, siglec-7 and siglec-8, expressed in a CHO cell line, and their contribution to ligand recognition.
11231274	5	2	theme	N-linked	1028:1035	arg1	distribution					1053:1064	the N-linked oligosaccharide distribution	1024:1064	the N-linked oligosaccharide distribution	1024:1064	To determine any differences in the glycan composition of siglec-5, siglec-7 and siglec-8 that may modify their function, we released and characterized the N-linked oligosaccharide distribution in these three glycoproteins.
11231274	0	3	from	contribution	138:149	arg1	siglec-7					75:82	siglec-7	75:82	siglec-7	75:82	A comparative study of the asparagine-linked oligosaccharides on siglec-5, siglec-7 and siglec-8, expressed in a CHO cell line, and their contribution to ligand recognition.
11231274	0	3	from	contribution	138:149	arg1	siglec-5					65:72	siglec-5	65:72	siglec-5	65:72	A comparative study of the asparagine-linked oligosaccharides on siglec-5, siglec-7 and siglec-8, expressed in a CHO cell line, and their contribution to ligand recognition.
11231274	0	3	from	contribution	138:149	arg1	siglec-8					88:95	siglec-8	88:95	siglec-8	88:95	A comparative study of the asparagine-linked oligosaccharides on siglec-5, siglec-7 and siglec-8, expressed in a CHO cell line, and their contribution to ligand recognition.
11231274	7	4	theme	glycosylation	1511:1523	arg1	site					1525:1528	the conserved potentially N-linked glycosylation site	1476:1528	the conserved potentially N-linked glycosylation site in the first domain	1476:1548	In addition, we show that, in contrast with CD22 and CD33, mutating the conserved potentially N-linked glycosylation site in the first domain has no effect on binding mediated by siglec-5 or siglec-7.
11231274	6	5	theme	larger	1152:1157	arg1	proportion					1159:1168	a larger proportion	1150:1168	a larger proportion of sialylated and core-fucosylated biantennary, triantennary and tetra-antennary oligosaccharides	1150:1266	The glycan pools from siglec-5 and siglec-7 contained a larger proportion of sialylated and core-fucosylated biantennary, triantennary and tetra-antennary oligosaccharides, whereas the carbohydrate mixture released from siglec-8 is noticeably less sialylated and is more abundant in 'high-mannose'-type glycans.
11231274	3	6	theme	expression	646:655	arg1	pattern					657:663	their expression pattern	640:663	their expression pattern on immune cells	640:679	Although these novel receptors have generated considerable interest as therapeutic targets because of their expression pattern on immune cells, very little is known about how their lectin activity is regulated.
11231274	1	7	theme	sialic	244:249	arg1	interactions					275:286	sialic acid-dependent cellular interactions	244:286	sialic acid-dependent cellular interactions	244:286	The siglecs (sialic acid-binding immunoglobulin-like lectins) mediate sialic acid-dependent cellular interactions and may in some cases signal through SH2-binding domains.
11231274	5	8	theme	siglec-8	953:960	arg1	composition					915:925	the glycan composition	904:925	the glycan composition of siglec-5, siglec-7 and siglec-8	904:960	To determine any differences in the glycan composition of siglec-5, siglec-7 and siglec-8 that may modify their function, we released and characterized the N-linked oligosaccharide distribution in these three glycoproteins.
11231274	1	9	theme	acid-dependent	251:264	arg1	interactions					275:286	sialic acid-dependent cellular interactions	244:286	sialic acid-dependent cellular interactions	244:286	The siglecs (sialic acid-binding immunoglobulin-like lectins) mediate sialic acid-dependent cellular interactions and may in some cases signal through SH2-binding domains.
11231274	3	10	theme	lectin	719:724	arg1	activity					726:733	their lectin activity	713:733	their lectin activity	713:733	Although these novel receptors have generated considerable interest as therapeutic targets because of their expression pattern on immune cells, very little is known about how their lectin activity is regulated.
11231274	6	11	theme	biantennary	1205:1215	arg1	oligosaccharides					1251:1266	sialylated and core-fucosylated biantennary, triantennary and tetra-antennary oligosaccharides	1173:1266	sialylated and core-fucosylated biantennary, triantennary and tetra-antennary oligosaccharides	1173:1266	The glycan pools from siglec-5 and siglec-7 contained a larger proportion of sialylated and core-fucosylated biantennary, triantennary and tetra-antennary oligosaccharides, whereas the carbohydrate mixture released from siglec-8 is noticeably less sialylated and is more abundant in 'high-mannose'-type glycans.
11231274	1	12	theme	cellular	266:273	arg1	interactions					275:286	sialic acid-dependent cellular interactions	244:286	sialic acid-dependent cellular interactions	244:286	The siglecs (sialic acid-binding immunoglobulin-like lectins) mediate sialic acid-dependent cellular interactions and may in some cases signal through SH2-binding domains.
11231274	3	13	from	pattern	657:663	arg1	cells					675:679	immune cells	668:679	immune cells	668:679	Although these novel receptors have generated considerable interest as therapeutic targets because of their expression pattern on immune cells, very little is known about how their lectin activity is regulated.
11231274	0	14	from	oligosaccharides	45:60	arg1	siglec-7					75:82	siglec-7	75:82	siglec-7	75:82	A comparative study of the asparagine-linked oligosaccharides on siglec-5, siglec-7 and siglec-8, expressed in a CHO cell line, and their contribution to ligand recognition.
11231274	0	14	from	oligosaccharides	45:60	arg1	siglec-5					65:72	siglec-5	65:72	siglec-5	65:72	A comparative study of the asparagine-linked oligosaccharides on siglec-5, siglec-7 and siglec-8, expressed in a CHO cell line, and their contribution to ligand recognition.
11231274	0	14	from	oligosaccharides	45:60	arg1	siglec-8					88:95	siglec-8	88:95	siglec-8	88:95	A comparative study of the asparagine-linked oligosaccharides on siglec-5, siglec-7 and siglec-8, expressed in a CHO cell line, and their contribution to ligand recognition.
11231274	4	15	theme	significant	840:850	arg1	effects					852:858	significant effects	840:858	significant effects	840:858	Previous studies with sialoadhesin, CD22 and CD33 have shown that siglec glycosylation has significant effects on binding.
11231274	5	16	from	differences	889:899	arg1	composition					915:925	the glycan composition	904:925	the glycan composition of siglec-5, siglec-7 and siglec-8	904:960	To determine any differences in the glycan composition of siglec-5, siglec-7 and siglec-8 that may modify their function, we released and characterized the N-linked oligosaccharide distribution in these three glycoproteins.
11231274	6	17	theme	core-fucosylated	1188:1203	arg1	oligosaccharides					1251:1266	sialylated and core-fucosylated biantennary, triantennary and tetra-antennary oligosaccharides	1173:1266	sialylated and core-fucosylated biantennary, triantennary and tetra-antennary oligosaccharides	1173:1266	The glycan pools from siglec-5 and siglec-7 contained a larger proportion of sialylated and core-fucosylated biantennary, triantennary and tetra-antennary oligosaccharides, whereas the carbohydrate mixture released from siglec-8 is noticeably less sialylated and is more abundant in 'high-mannose'-type glycans.
11231274	3	18	from	targets	621:627	arg1	cells					675:679	immune cells	668:679	immune cells	668:679	Although these novel receptors have generated considerable interest as therapeutic targets because of their expression pattern on immune cells, very little is known about how their lectin activity is regulated.
11231274	6	19	gly	core-fucosylated	1188:1203	arg1	oligosaccharides					1251:1266	sialylated and core-fucosylated biantennary, triantennary and tetra-antennary oligosaccharides	1173:1266	sialylated and core-fucosylated biantennary, triantennary and tetra-antennary oligosaccharides	1173:1266	The glycan pools from siglec-5 and siglec-7 contained a larger proportion of sialylated and core-fucosylated biantennary, triantennary and tetra-antennary oligosaccharides, whereas the carbohydrate mixture released from siglec-8 is noticeably less sialylated and is more abundant in 'high-mannose'-type glycans.
11231274	2	20	theme	several	460:466	arg1	siglec-7					488:495	siglec-7	488:495	siglec-7	488:495	In addition to the previously characterized siglecs, sialoadhesin, CD22, CD33 and myelin-associated glycoprotein, several new ones, siglec-5, siglec-7 and siglec-8, have recently been cloned.
11231274	2	20	theme	several	460:466	arg1	siglec-5					478:485	siglec-5	478:485	siglec-5	478:485	In addition to the previously characterized siglecs, sialoadhesin, CD22, CD33 and myelin-associated glycoprotein, several new ones, siglec-5, siglec-7 and siglec-8, have recently been cloned.
11231274	2	20	theme	several	460:466	arg1	ones					472:475	several new ones	460:475	several new ones	460:475	In addition to the previously characterized siglecs, sialoadhesin, CD22, CD33 and myelin-associated glycoprotein, several new ones, siglec-5, siglec-7 and siglec-8, have recently been cloned.
11231274	2	20	theme	several	460:466	arg1	siglec-8					501:508	siglec-8	501:508	siglec-8	501:508	In addition to the previously characterized siglecs, sialoadhesin, CD22, CD33 and myelin-associated glycoprotein, several new ones, siglec-5, siglec-7 and siglec-8, have recently been cloned.
11231274	7	21	with	contrast	1438:1445	arg1	CD33					1461:1464	CD33	1461:1464	CD33	1461:1464	In addition, we show that, in contrast with CD22 and CD33, mutating the conserved potentially N-linked glycosylation site in the first domain has no effect on binding mediated by siglec-5 or siglec-7.
11231274	7	21	with	contrast	1438:1445	arg1	CD22					1452:1455	CD22	1452:1455	CD22	1452:1455	In addition, we show that, in contrast with CD22 and CD33, mutating the conserved potentially N-linked glycosylation site in the first domain has no effect on binding mediated by siglec-5 or siglec-7.
11231274	6	22	theme	glycan	1100:1105	arg1	pools					1107:1111	The glycan pools	1096:1111	The glycan pools from siglec-5 and siglec-7	1096:1138	The glycan pools from siglec-5 and siglec-7 contained a larger proportion of sialylated and core-fucosylated biantennary, triantennary and tetra-antennary oligosaccharides, whereas the carbohydrate mixture released from siglec-8 is noticeably less sialylated and is more abundant in 'high-mannose'-type glycans.
11231274	0	23	theme	comparative	2:12	arg1	study					14:18	A comparative study	0:18	A comparative study of the asparagine-linked oligosaccharides on siglec-5, siglec-7 and siglec-8, expressed in a CHO cell line,	0:126	A comparative study of the asparagine-linked oligosaccharides on siglec-5, siglec-7 and siglec-8, expressed in a CHO cell line, and their contribution to ligand recognition.
11231274	7	24	theme	conserved	1480:1488	arg1	site					1525:1528	the conserved potentially N-linked glycosylation site	1476:1528	the conserved potentially N-linked glycosylation site in the first domain	1476:1548	In addition, we show that, in contrast with CD22 and CD33, mutating the conserved potentially N-linked glycosylation site in the first domain has no effect on binding mediated by siglec-5 or siglec-7.
11231274	6	25	theme	sialylated	1173:1182	arg1	oligosaccharides					1251:1266	sialylated and core-fucosylated biantennary, triantennary and tetra-antennary oligosaccharides	1173:1266	sialylated and core-fucosylated biantennary, triantennary and tetra-antennary oligosaccharides	1173:1266	The glycan pools from siglec-5 and siglec-7 contained a larger proportion of sialylated and core-fucosylated biantennary, triantennary and tetra-antennary oligosaccharides, whereas the carbohydrate mixture released from siglec-8 is noticeably less sialylated and is more abundant in 'high-mannose'-type glycans.
11231274	6	26	attach	released	1302:1309	arg2	mixture					1294:1300	the carbohydrate mixture	1277:1300	the carbohydrate mixture released from siglec-8	1277:1323	The glycan pools from siglec-5 and siglec-7 contained a larger proportion of sialylated and core-fucosylated biantennary, triantennary and tetra-antennary oligosaccharides, whereas the carbohydrate mixture released from siglec-8 is noticeably less sialylated and is more abundant in 'high-mannose'-type glycans.
11231274	6	26	attach	released	1302:1309	arg1	siglec-8					1316:1323	siglec-8	1316:1323	siglec-8	1316:1323	The glycan pools from siglec-5 and siglec-7 contained a larger proportion of sialylated and core-fucosylated biantennary, triantennary and tetra-antennary oligosaccharides, whereas the carbohydrate mixture released from siglec-8 is noticeably less sialylated and is more abundant in 'high-mannose'-type glycans.
11231274	6	26	attach	released	1302:1309	arg2	abundant					1367:1374	abundant	1367:1374	abundant	1367:1374	The glycan pools from siglec-5 and siglec-7 contained a larger proportion of sialylated and core-fucosylated biantennary, triantennary and tetra-antennary oligosaccharides, whereas the carbohydrate mixture released from siglec-8 is noticeably less sialylated and is more abundant in 'high-mannose'-type glycans.
11231274	6	27	gly	sialylated	1173:1182	arg1	oligosaccharides					1251:1266	sialylated and core-fucosylated biantennary, triantennary and tetra-antennary oligosaccharides	1173:1266	sialylated and core-fucosylated biantennary, triantennary and tetra-antennary oligosaccharides	1173:1266	The glycan pools from siglec-5 and siglec-7 contained a larger proportion of sialylated and core-fucosylated biantennary, triantennary and tetra-antennary oligosaccharides, whereas the carbohydrate mixture released from siglec-8 is noticeably less sialylated and is more abundant in 'high-mannose'-type glycans.
11231274	7	28	theme	N-linked	1502:1509	arg1	site					1525:1528	the conserved potentially N-linked glycosylation site	1476:1528	the conserved potentially N-linked glycosylation site in the first domain	1476:1548	In addition, we show that, in contrast with CD22 and CD33, mutating the conserved potentially N-linked glycosylation site in the first domain has no effect on binding mediated by siglec-5 or siglec-7.
11231274	0	29	link	asparagine-linked	27:43	arg1	oligosaccharides					45:60	the asparagine-linked oligosaccharides	23:60	the asparagine-linked oligosaccharides on siglec-5, siglec-7 and siglec-8, expressed in a CHO cell line,	23:126	A comparative study of the asparagine-linked oligosaccharides on siglec-5, siglec-7 and siglec-8, expressed in a CHO cell line, and their contribution to ligand recognition.
11231274	5	30	theme	siglec-7	940:947	arg1	composition					915:925	the glycan composition	904:925	the glycan composition of siglec-5, siglec-7 and siglec-8	904:960	To determine any differences in the glycan composition of siglec-5, siglec-7 and siglec-8 that may modify their function, we released and characterized the N-linked oligosaccharide distribution in these three glycoproteins.
11231274	2	31	theme	characterized	376:388	arg1	glycoprotein					446:457	myelin-associated glycoprotein	428:457	myelin-associated glycoprotein	428:457	In addition to the previously characterized siglecs, sialoadhesin, CD22, CD33 and myelin-associated glycoprotein, several new ones, siglec-5, siglec-7 and siglec-8, have recently been cloned.
11231274	2	31	theme	characterized	376:388	arg1	CD22					413:416	CD22	413:416	CD22	413:416	In addition to the previously characterized siglecs, sialoadhesin, CD22, CD33 and myelin-associated glycoprotein, several new ones, siglec-5, siglec-7 and siglec-8, have recently been cloned.
11231274	2	31	theme	characterized	376:388	arg1	sialoadhesin					399:410	sialoadhesin	399:410	sialoadhesin	399:410	In addition to the previously characterized siglecs, sialoadhesin, CD22, CD33 and myelin-associated glycoprotein, several new ones, siglec-5, siglec-7 and siglec-8, have recently been cloned.
11231274	2	31	theme	characterized	376:388	arg1	siglecs					390:396	the previously characterized siglecs	361:396	the previously characterized siglecs	361:396	In addition to the previously characterized siglecs, sialoadhesin, CD22, CD33 and myelin-associated glycoprotein, several new ones, siglec-5, siglec-7 and siglec-8, have recently been cloned.
11231274	2	31	theme	characterized	376:388	arg1	CD33					419:422	CD33	419:422	CD33	419:422	In addition to the previously characterized siglecs, sialoadhesin, CD22, CD33 and myelin-associated glycoprotein, several new ones, siglec-5, siglec-7 and siglec-8, have recently been cloned.
11231274	2	32	theme	myelin-associated	428:444	arg1	glycoprotein					446:457	myelin-associated glycoprotein	428:457	myelin-associated glycoprotein	428:457	In addition to the previously characterized siglecs, sialoadhesin, CD22, CD33 and myelin-associated glycoprotein, several new ones, siglec-5, siglec-7 and siglec-8, have recently been cloned.
11231274	2	32	theme	myelin-associated	428:444	arg1	siglecs					390:396	the previously characterized siglecs	361:396	the previously characterized siglecs	361:396	In addition to the previously characterized siglecs, sialoadhesin, CD22, CD33 and myelin-associated glycoprotein, several new ones, siglec-5, siglec-7 and siglec-8, have recently been cloned.
11231274	0	33	theme	CHO	113:115	arg1	line					122:125	a CHO cell line	111:125	a CHO cell line	111:125	A comparative study of the asparagine-linked oligosaccharides on siglec-5, siglec-7 and siglec-8, expressed in a CHO cell line, and their contribution to ligand recognition.
11231274	4	34	theme	siglec	815:820	arg1	glycosylation					822:834	siglec glycosylation	815:834	siglec glycosylation	815:834	Previous studies with sialoadhesin, CD22 and CD33 have shown that siglec glycosylation has significant effects on binding.
11231274	4	35	theme	Previous	749:756	arg1	studies					758:764	Previous studies	749:764	Previous studies with sialoadhesin, CD22 and CD33	749:797	Previous studies with sialoadhesin, CD22 and CD33 have shown that siglec glycosylation has significant effects on binding.
11231274	6	36	from	glycans	1399:1405	arg1	mixture					1294:1300	the carbohydrate mixture	1277:1300	the carbohydrate mixture released from siglec-8	1277:1323	The glycan pools from siglec-5 and siglec-7 contained a larger proportion of sialylated and core-fucosylated biantennary, triantennary and tetra-antennary oligosaccharides, whereas the carbohydrate mixture released from siglec-8 is noticeably less sialylated and is more abundant in 'high-mannose'-type glycans.
11231274	6	36	from	glycans	1399:1405	arg1	abundant					1367:1374	abundant	1367:1374	abundant	1367:1374	The glycan pools from siglec-5 and siglec-7 contained a larger proportion of sialylated and core-fucosylated biantennary, triantennary and tetra-antennary oligosaccharides, whereas the carbohydrate mixture released from siglec-8 is noticeably less sialylated and is more abundant in 'high-mannose'-type glycans.
11231274	6	37	theme	high-mannose'-type	1380:1397	arg1	glycans					1399:1405	'high-mannose'-type glycans	1379:1405	'high-mannose'-type glycans	1379:1405	The glycan pools from siglec-5 and siglec-7 contained a larger proportion of sialylated and core-fucosylated biantennary, triantennary and tetra-antennary oligosaccharides, whereas the carbohydrate mixture released from siglec-8 is noticeably less sialylated and is more abundant in 'high-mannose'-type glycans.
11231274	3	38	theme	pattern	657:663	arg1	interest					597:604	considerable interest	584:604	considerable interest	584:604	Although these novel receptors have generated considerable interest as therapeutic targets because of their expression pattern on immune cells, very little is known about how their lectin activity is regulated.
11231274	3	38	theme	pattern	657:663	arg1	targets					621:627	therapeutic targets	609:627	therapeutic targets because of their expression pattern on immune cells	609:679	Although these novel receptors have generated considerable interest as therapeutic targets because of their expression pattern on immune cells, very little is known about how their lectin activity is regulated.
11231274	3	39	theme	novel	553:557	arg1	receptors					559:567	these novel receptors	547:567	these novel receptors	547:567	Although these novel receptors have generated considerable interest as therapeutic targets because of their expression pattern on immune cells, very little is known about how their lectin activity is regulated.
11231274	0	40	theme	asparagine-linked	27:43	arg1	oligosaccharides					45:60	the asparagine-linked oligosaccharides	23:60	the asparagine-linked oligosaccharides on siglec-5, siglec-7 and siglec-8, expressed in a CHO cell line,	23:126	A comparative study of the asparagine-linked oligosaccharides on siglec-5, siglec-7 and siglec-8, expressed in a CHO cell line, and their contribution to ligand recognition.
11231274	4	41	with	studies	758:764	arg1	CD33					794:797	CD33	794:797	CD33	794:797	Previous studies with sialoadhesin, CD22 and CD33 have shown that siglec glycosylation has significant effects on binding.
11231274	4	41	with	studies	758:764	arg1	CD22					785:788	CD22	785:788	CD22	785:788	Previous studies with sialoadhesin, CD22 and CD33 have shown that siglec glycosylation has significant effects on binding.
11231274	4	41	with	studies	758:764	arg1	sialoadhesin					771:782	sialoadhesin	771:782	sialoadhesin	771:782	Previous studies with sialoadhesin, CD22 and CD33 have shown that siglec glycosylation has significant effects on binding.
11231274	0	42	from	siglec-7	75:82	arg1	study					14:18	A comparative study	0:18	A comparative study of the asparagine-linked oligosaccharides on siglec-5, siglec-7 and siglec-8, expressed in a CHO cell line,	0:126	A comparative study of the asparagine-linked oligosaccharides on siglec-5, siglec-7 and siglec-8, expressed in a CHO cell line, and their contribution to ligand recognition.
11231274	0	42	from	siglec-7	75:82	arg1	contribution					138:149	their contribution	132:149	their contribution to ligand recognition	132:171	A comparative study of the asparagine-linked oligosaccharides on siglec-5, siglec-7 and siglec-8, expressed in a CHO cell line, and their contribution to ligand recognition.
11231274	6	43	theme	carbohydrate	1281:1292	arg1	mixture					1294:1300	the carbohydrate mixture	1277:1300	the carbohydrate mixture released from siglec-8	1277:1323	The glycan pools from siglec-5 and siglec-7 contained a larger proportion of sialylated and core-fucosylated biantennary, triantennary and tetra-antennary oligosaccharides, whereas the carbohydrate mixture released from siglec-8 is noticeably less sialylated and is more abundant in 'high-mannose'-type glycans.
11231274	6	43	theme	carbohydrate	1281:1292	arg1	abundant					1367:1374	abundant	1367:1374	abundant	1367:1374	The glycan pools from siglec-5 and siglec-7 contained a larger proportion of sialylated and core-fucosylated biantennary, triantennary and tetra-antennary oligosaccharides, whereas the carbohydrate mixture released from siglec-8 is noticeably less sialylated and is more abundant in 'high-mannose'-type glycans.
11231274	7	44	gly	glycosylation	1511:1523	arg2	site					1525:1528	the conserved potentially N-linked glycosylation site	1476:1528	the conserved potentially N-linked glycosylation site in the first domain	1476:1548	In addition, we show that, in contrast with CD22 and CD33, mutating the conserved potentially N-linked glycosylation site in the first domain has no effect on binding mediated by siglec-5 or siglec-7.
11231274	5	45	link	N-linked	1028:1035	arg1	distribution					1053:1064	the N-linked oligosaccharide distribution	1024:1064	the N-linked oligosaccharide distribution	1024:1064	To determine any differences in the glycan composition of siglec-5, siglec-7 and siglec-8 that may modify their function, we released and characterized the N-linked oligosaccharide distribution in these three glycoproteins.
11231274	0	46	theme	cell	117:120	arg1	line					122:125	a CHO cell line	111:125	a CHO cell line	111:125	A comparative study of the asparagine-linked oligosaccharides on siglec-5, siglec-7 and siglec-8, expressed in a CHO cell line, and their contribution to ligand recognition.
11231274	6	47	contain	contained	1140:1148	arg1	pools					1107:1111	The glycan pools	1096:1111	The glycan pools from siglec-5 and siglec-7	1096:1138	The glycan pools from siglec-5 and siglec-7 contained a larger proportion of sialylated and core-fucosylated biantennary, triantennary and tetra-antennary oligosaccharides, whereas the carbohydrate mixture released from siglec-8 is noticeably less sialylated and is more abundant in 'high-mannose'-type glycans.
11231274	6	47	contain	contained	1140:1148	arg2	proportion					1159:1168	a larger proportion	1150:1168	a larger proportion of sialylated and core-fucosylated biantennary, triantennary and tetra-antennary oligosaccharides	1150:1266	The glycan pools from siglec-5 and siglec-7 contained a larger proportion of sialylated and core-fucosylated biantennary, triantennary and tetra-antennary oligosaccharides, whereas the carbohydrate mixture released from siglec-8 is noticeably less sialylated and is more abundant in 'high-mannose'-type glycans.
11231274	6	48	from	siglec-7	1131:1138	arg1	pools					1107:1111	The glycan pools	1096:1111	The glycan pools from siglec-5 and siglec-7	1096:1138	The glycan pools from siglec-5 and siglec-7 contained a larger proportion of sialylated and core-fucosylated biantennary, triantennary and tetra-antennary oligosaccharides, whereas the carbohydrate mixture released from siglec-8 is noticeably less sialylated and is more abundant in 'high-mannose'-type glycans.
11231274	1	49	theme	sialic	187:192	arg1	lectins					227:233	sialic acid-binding immunoglobulin-like lectins	187:233	sialic acid-binding immunoglobulin-like lectins	187:233	The siglecs (sialic acid-binding immunoglobulin-like lectins) mediate sialic acid-dependent cellular interactions and may in some cases signal through SH2-binding domains.
11231274	1	49	theme	sialic	187:192	arg1	siglecs					178:184	The siglecs	174:184	The siglecs (sialic acid-binding immunoglobulin-like lectins)	174:234	The siglecs (sialic acid-binding immunoglobulin-like lectins) mediate sialic acid-dependent cellular interactions and may in some cases signal through SH2-binding domains.
11231274	2	50	theme	new	468:470	arg1	siglec-7					488:495	siglec-7	488:495	siglec-7	488:495	In addition to the previously characterized siglecs, sialoadhesin, CD22, CD33 and myelin-associated glycoprotein, several new ones, siglec-5, siglec-7 and siglec-8, have recently been cloned.
11231274	2	50	theme	new	468:470	arg1	siglec-5					478:485	siglec-5	478:485	siglec-5	478:485	In addition to the previously characterized siglecs, sialoadhesin, CD22, CD33 and myelin-associated glycoprotein, several new ones, siglec-5, siglec-7 and siglec-8, have recently been cloned.
11231274	2	50	theme	new	468:470	arg1	ones					472:475	several new ones	460:475	several new ones	460:475	In addition to the previously characterized siglecs, sialoadhesin, CD22, CD33 and myelin-associated glycoprotein, several new ones, siglec-5, siglec-7 and siglec-8, have recently been cloned.
11231274	2	50	theme	new	468:470	arg1	siglec-8					501:508	siglec-8	501:508	siglec-8	501:508	In addition to the previously characterized siglecs, sialoadhesin, CD22, CD33 and myelin-associated glycoprotein, several new ones, siglec-5, siglec-7 and siglec-8, have recently been cloned.
11231274	0	51	from	siglec-5	65:72	arg1	study					14:18	A comparative study	0:18	A comparative study of the asparagine-linked oligosaccharides on siglec-5, siglec-7 and siglec-8, expressed in a CHO cell line,	0:126	A comparative study of the asparagine-linked oligosaccharides on siglec-5, siglec-7 and siglec-8, expressed in a CHO cell line, and their contribution to ligand recognition.
11231274	0	51	from	siglec-5	65:72	arg1	contribution					138:149	their contribution	132:149	their contribution to ligand recognition	132:171	A comparative study of the asparagine-linked oligosaccharides on siglec-5, siglec-7 and siglec-8, expressed in a CHO cell line, and their contribution to ligand recognition.
11231274	7	52	link	N-linked	1502:1509	arg1	site					1525:1528	the conserved potentially N-linked glycosylation site	1476:1528	the conserved potentially N-linked glycosylation site in the first domain	1476:1548	In addition, we show that, in contrast with CD22 and CD33, mutating the conserved potentially N-linked glycosylation site in the first domain has no effect on binding mediated by siglec-5 or siglec-7.
11231274	5	53	theme	glycan	908:913	arg1	composition					915:925	the glycan composition	904:925	the glycan composition of siglec-5, siglec-7 and siglec-8	904:960	To determine any differences in the glycan composition of siglec-5, siglec-7 and siglec-8 that may modify their function, we released and characterized the N-linked oligosaccharide distribution in these three glycoproteins.
11231274	0	54	theme	oligosaccharides	45:60	arg1	study					14:18	A comparative study	0:18	A comparative study of the asparagine-linked oligosaccharides on siglec-5, siglec-7 and siglec-8, expressed in a CHO cell line,	0:126	A comparative study of the asparagine-linked oligosaccharides on siglec-5, siglec-7 and siglec-8, expressed in a CHO cell line, and their contribution to ligand recognition.
11231274	0	54	theme	oligosaccharides	45:60	arg1	contribution					138:149	their contribution	132:149	their contribution to ligand recognition	132:171	A comparative study of the asparagine-linked oligosaccharides on siglec-5, siglec-7 and siglec-8, expressed in a CHO cell line, and their contribution to ligand recognition.
11231274	6	55	from	abundant	1367:1374	arg1	glycans					1399:1405	'high-mannose'-type glycans	1379:1405	'high-mannose'-type glycans	1379:1405	The glycan pools from siglec-5 and siglec-7 contained a larger proportion of sialylated and core-fucosylated biantennary, triantennary and tetra-antennary oligosaccharides, whereas the carbohydrate mixture released from siglec-8 is noticeably less sialylated and is more abundant in 'high-mannose'-type glycans.
11231274	5	56	theme	oligosaccharide	1037:1051	arg1	distribution					1053:1064	the N-linked oligosaccharide distribution	1024:1064	the N-linked oligosaccharide distribution	1024:1064	To determine any differences in the glycan composition of siglec-5, siglec-7 and siglec-8 that may modify their function, we released and characterized the N-linked oligosaccharide distribution in these three glycoproteins.
11231274	3	57	theme	considerable	584:595	arg1	interest					597:604	considerable interest	584:604	considerable interest	584:604	Although these novel receptors have generated considerable interest as therapeutic targets because of their expression pattern on immune cells, very little is known about how their lectin activity is regulated.
11231274	3	57	theme	considerable	584:595	arg1	targets					621:627	therapeutic targets	609:627	therapeutic targets because of their expression pattern on immune cells	609:679	Although these novel receptors have generated considerable interest as therapeutic targets because of their expression pattern on immune cells, very little is known about how their lectin activity is regulated.
11231274	5	58	gly	glycoproteins	1081:1093	arg1	glycoproteins					1081:1093	these three glycoproteins	1069:1093	these three glycoproteins	1069:1093	To determine any differences in the glycan composition of siglec-5, siglec-7 and siglec-8 that may modify their function, we released and characterized the N-linked oligosaccharide distribution in these three glycoproteins.
11231274	6	59	theme	oligosaccharides	1251:1266	arg1	proportion					1159:1168	a larger proportion	1150:1168	a larger proportion of sialylated and core-fucosylated biantennary, triantennary and tetra-antennary oligosaccharides	1150:1266	The glycan pools from siglec-5 and siglec-7 contained a larger proportion of sialylated and core-fucosylated biantennary, triantennary and tetra-antennary oligosaccharides, whereas the carbohydrate mixture released from siglec-8 is noticeably less sialylated and is more abundant in 'high-mannose'-type glycans.
11231274	2	60	gly	glycoprotein	446:457	arg1	glycoprotein					446:457	myelin-associated glycoprotein	428:457	myelin-associated glycoprotein	428:457	In addition to the previously characterized siglecs, sialoadhesin, CD22, CD33 and myelin-associated glycoprotein, several new ones, siglec-5, siglec-7 and siglec-8, have recently been cloned.
11231274	2	60	gly	glycoprotein	446:457	arg1	siglecs					390:396	the previously characterized siglecs	361:396	the previously characterized siglecs	361:396	In addition to the previously characterized siglecs, sialoadhesin, CD22, CD33 and myelin-associated glycoprotein, several new ones, siglec-5, siglec-7 and siglec-8, have recently been cloned.
11231274	7	61	from	site	1525:1528	arg1	domain					1543:1548	the first domain	1533:1548	the first domain	1533:1548	In addition, we show that, in contrast with CD22 and CD33, mutating the conserved potentially N-linked glycosylation site in the first domain has no effect on binding mediated by siglec-5 or siglec-7.
11231274	1	62	theme	acid-binding	194:205	arg1	lectins					227:233	sialic acid-binding immunoglobulin-like lectins	187:233	sialic acid-binding immunoglobulin-like lectins	187:233	The siglecs (sialic acid-binding immunoglobulin-like lectins) mediate sialic acid-dependent cellular interactions and may in some cases signal through SH2-binding domains.
11231274	1	62	theme	acid-binding	194:205	arg1	siglecs					178:184	The siglecs	174:184	The siglecs (sialic acid-binding immunoglobulin-like lectins)	174:234	The siglecs (sialic acid-binding immunoglobulin-like lectins) mediate sialic acid-dependent cellular interactions and may in some cases signal through SH2-binding domains.
11231274	3	63	theme	immune	668:673	arg1	cells					675:679	immune cells	668:679	immune cells	668:679	Although these novel receptors have generated considerable interest as therapeutic targets because of their expression pattern on immune cells, very little is known about how their lectin activity is regulated.
11231274	6	64	theme	tetra-antennary	1235:1249	arg1	oligosaccharides					1251:1266	sialylated and core-fucosylated biantennary, triantennary and tetra-antennary oligosaccharides	1173:1266	sialylated and core-fucosylated biantennary, triantennary and tetra-antennary oligosaccharides	1173:1266	The glycan pools from siglec-5 and siglec-7 contained a larger proportion of sialylated and core-fucosylated biantennary, triantennary and tetra-antennary oligosaccharides, whereas the carbohydrate mixture released from siglec-8 is noticeably less sialylated and is more abundant in 'high-mannose'-type glycans.
11231274	5	65	theme	siglec-5	930:937	arg1	composition					915:925	the glycan composition	904:925	the glycan composition of siglec-5, siglec-7 and siglec-8	904:960	To determine any differences in the glycan composition of siglec-5, siglec-7 and siglec-8 that may modify their function, we released and characterized the N-linked oligosaccharide distribution in these three glycoproteins.
11231274	4	66	contain	has	836:838	arg2	effects					852:858	significant effects	840:858	significant effects	840:858	Previous studies with sialoadhesin, CD22 and CD33 have shown that siglec glycosylation has significant effects on binding.
11231274	4	66	contain	has	836:838	arg1	glycosylation					822:834	siglec glycosylation	815:834	siglec glycosylation	815:834	Previous studies with sialoadhesin, CD22 and CD33 have shown that siglec glycosylation has significant effects on binding.
11231274	1	67	theme	immunoglobulin-like	207:225	arg1	lectins					227:233	sialic acid-binding immunoglobulin-like lectins	187:233	sialic acid-binding immunoglobulin-like lectins	187:233	The siglecs (sialic acid-binding immunoglobulin-like lectins) mediate sialic acid-dependent cellular interactions and may in some cases signal through SH2-binding domains.
11231274	1	67	theme	immunoglobulin-like	207:225	arg1	siglecs					178:184	The siglecs	174:184	The siglecs (sialic acid-binding immunoglobulin-like lectins)	174:234	The siglecs (sialic acid-binding immunoglobulin-like lectins) mediate sialic acid-dependent cellular interactions and may in some cases signal through SH2-binding domains.
11231274	0	68	from	siglec-8	88:95	arg1	study					14:18	A comparative study	0:18	A comparative study of the asparagine-linked oligosaccharides on siglec-5, siglec-7 and siglec-8, expressed in a CHO cell line,	0:126	A comparative study of the asparagine-linked oligosaccharides on siglec-5, siglec-7 and siglec-8, expressed in a CHO cell line, and their contribution to ligand recognition.
11231274	0	68	from	siglec-8	88:95	arg1	contribution					138:149	their contribution	132:149	their contribution to ligand recognition	132:171	A comparative study of the asparagine-linked oligosaccharides on siglec-5, siglec-7 and siglec-8, expressed in a CHO cell line, and their contribution to ligand recognition.
11231274	3	69	theme	therapeutic	609:619	arg1	interest					597:604	considerable interest	584:604	considerable interest	584:604	Although these novel receptors have generated considerable interest as therapeutic targets because of their expression pattern on immune cells, very little is known about how their lectin activity is regulated.
11231274	3	69	theme	therapeutic	609:619	arg1	targets					621:627	therapeutic targets	609:627	therapeutic targets because of their expression pattern on immune cells	609:679	Although these novel receptors have generated considerable interest as therapeutic targets because of their expression pattern on immune cells, very little is known about how their lectin activity is regulated.
11231274	7	70	theme	first	1537:1541	arg1	domain					1543:1548	the first domain	1533:1548	the first domain	1533:1548	In addition, we show that, in contrast with CD22 and CD33, mutating the conserved potentially N-linked glycosylation site in the first domain has no effect on binding mediated by siglec-5 or siglec-7.
11231274	3	71	from	cells	675:679	arg1	interest					597:604	considerable interest	584:604	considerable interest	584:604	Although these novel receptors have generated considerable interest as therapeutic targets because of their expression pattern on immune cells, very little is known about how their lectin activity is regulated.
11231274	3	71	from	cells	675:679	arg1	targets					621:627	therapeutic targets	609:627	therapeutic targets because of their expression pattern on immune cells	609:679	Although these novel receptors have generated considerable interest as therapeutic targets because of their expression pattern on immune cells, very little is known about how their lectin activity is regulated.
11231274	1	72	theme	SH2-binding	325:335	arg1	domains					337:343	SH2-binding domains	325:343	SH2-binding domains	325:343	The siglecs (sialic acid-binding immunoglobulin-like lectins) mediate sialic acid-dependent cellular interactions and may in some cases signal through SH2-binding domains.
11231274	6	73	theme	triantennary	1218:1229	arg1	oligosaccharides					1251:1266	sialylated and core-fucosylated biantennary, triantennary and tetra-antennary oligosaccharides	1173:1266	sialylated and core-fucosylated biantennary, triantennary and tetra-antennary oligosaccharides	1173:1266	The glycan pools from siglec-5 and siglec-7 contained a larger proportion of sialylated and core-fucosylated biantennary, triantennary and tetra-antennary oligosaccharides, whereas the carbohydrate mixture released from siglec-8 is noticeably less sialylated and is more abundant in 'high-mannose'-type glycans.
11231274	6	74	from	siglec-5	1118:1125	arg1	pools					1107:1111	The glycan pools	1096:1111	The glycan pools from siglec-5 and siglec-7	1096:1138	The glycan pools from siglec-5 and siglec-7 contained a larger proportion of sialylated and core-fucosylated biantennary, triantennary and tetra-antennary oligosaccharides, whereas the carbohydrate mixture released from siglec-8 is noticeably less sialylated and is more abundant in 'high-mannose'-type glycans.
11231274	6	75	gly	sialylated	1344:1353	arg1	mixture					1294:1300	the carbohydrate mixture	1277:1300	the carbohydrate mixture released from siglec-8	1277:1323	The glycan pools from siglec-5 and siglec-7 contained a larger proportion of sialylated and core-fucosylated biantennary, triantennary and tetra-antennary oligosaccharides, whereas the carbohydrate mixture released from siglec-8 is noticeably less sialylated and is more abundant in 'high-mannose'-type glycans.
11231274	6	75	gly	sialylated	1344:1353	arg1	abundant					1367:1374	abundant	1367:1374	abundant	1367:1374	The glycan pools from siglec-5 and siglec-7 contained a larger proportion of sialylated and core-fucosylated biantennary, triantennary and tetra-antennary oligosaccharides, whereas the carbohydrate mixture released from siglec-8 is noticeably less sialylated and is more abundant in 'high-mannose'-type glycans.
12663789	6	0	theme	north	1187:1191	arg1	rim					1193:1195	the north rim	1183:1195	the north rim of the canyon, especially the region immediately outside the viral hydrophobic pocket that normally binds a cellular "pocket factor,"	1183:1329	In contrast, the interaction of CD155 with the north rim of the canyon, especially the region immediately outside the viral hydrophobic pocket that normally binds a cellular "pocket factor," may be critical for the release of the pocket factor, decreasing the virus stability and hence initiating uncoating.
12663789	5	1	theme	receptor-mediated	1105:1121	arg1	uncoating					1129:1137	the receptor-mediated viral uncoating	1101:1137	the receptor-mediated viral uncoating	1101:1137	The footprints of CD155 on PV surfaces indicate that the south rim of the canyon dominates the virus-receptor interactions and may correspond to the initial CD155 binding state of the receptor-mediated viral uncoating.
12663789	5	2	theme	uncoating	1129:1137	arg1	state					1092:1096	the initial CD155 binding state	1066:1096	the initial CD155 binding state of the receptor-mediated viral uncoating	1066:1137	The footprints of CD155 on PV surfaces indicate that the south rim of the canyon dominates the virus-receptor interactions and may correspond to the initial CD155 binding state of the receptor-mediated viral uncoating.
12663789	7	3	from	limitation	1587:1596	arg1	viability					1605:1613	the viability	1601:1613	the viability of PV escape mutants from antibody neutralization	1601:1663	The large area of the CD155 footprint on the PV surface, in comparison with other picornavirus-receptor interactions, could be a potential limitation on the viability of PV escape mutants from antibody neutralization.
12663789	7	3	from	limitation	1587:1596	arg1	comparison					1508:1517	comparison	1508:1517	comparison with other picornavirus-receptor interactions	1508:1563	The large area of the CD155 footprint on the PV surface, in comparison with other picornavirus-receptor interactions, could be a potential limitation on the viability of PV escape mutants from antibody neutralization.
12663789	7	4	theme	antibody	1641:1648	arg1	neutralization					1650:1663	antibody neutralization	1641:1663	antibody neutralization	1641:1663	The large area of the CD155 footprint on the PV surface, in comparison with other picornavirus-receptor interactions, could be a potential limitation on the viability of PV escape mutants from antibody neutralization.
12663789	7	5	theme	mutants	1628:1634	arg1	viability					1605:1613	the viability	1601:1613	the viability of PV escape mutants from antibody neutralization	1601:1663	The large area of the CD155 footprint on the PV surface, in comparison with other picornavirus-receptor interactions, could be a potential limitation on the viability of PV escape mutants from antibody neutralization.
12663789	3	6	theme	receptor	656:663	arg1	position					640:647	the position	636:647	the position of the receptor relative to the viral surface	636:693	Difference maps between the glycosylated and deglycosylated CD155 complexes determined the sites of the carbohydrate moieties that, in turn, helped to verify the position of the receptor relative to the viral surface.
12663789	5	7	from	footprints	925:934	arg1	surfaces					951:958	PV surfaces	948:958	PV surfaces	948:958	The footprints of CD155 on PV surfaces indicate that the south rim of the canyon dominates the virus-receptor interactions and may correspond to the initial CD155 binding state of the receptor-mediated viral uncoating.
12663789	2	8	theme	cell	466:469	arg1	entry					471:475	cell entry	466:475	cell entry	466:475	Both glycosylated and fully deglycosylated CD155 exhibited similar binding sites and orientations in the viral canyon for all three PV serotypes, showing that all three serotypes use a common mechanism for cell entry.
12663789	8	9	theme	PV	1769:1770	arg1	serotypes					1772:1780	only three PV serotypes	1758:1780	only three PV serotypes	1758:1780	Many of these are likely to have lost their ability to bind CD155, resulting in there being only three PV serotypes.
12663789	3	10	theme	CD155	538:542	arg1	complexes					544:552	deglycosylated CD155 complexes	523:552	deglycosylated CD155 complexes	523:552	Difference maps between the glycosylated and deglycosylated CD155 complexes determined the sites of the carbohydrate moieties that, in turn, helped to verify the position of the receptor relative to the viral surface.
12663789	4	11	from	Asn105	744:749	arg1	site					736:739	the CD155 carbohydrate site	713:739	the CD155 carbohydrate site at Asn105	713:749	The proximity of the CD155 carbohydrate site at Asn105 to the viral surface in the receptor-virus complex suggests that it might interfere with receptor docking, an observation consistent with the properties of mutant CD155.
12663789	4	11	from	Asn105	744:749	arg1	proximity					700:708	The proximity	696:708	The proximity of the CD155 carbohydrate site at Asn105 to the viral surface in the receptor-virus complex	696:800	The proximity of the CD155 carbohydrate site at Asn105 to the viral surface in the receptor-virus complex suggests that it might interfere with receptor docking, an observation consistent with the properties of mutant CD155.
12663789	3	12	theme	viral	681:685	arg1	surface					687:693	the viral surface	677:693	the viral surface	677:693	Difference maps between the glycosylated and deglycosylated CD155 complexes determined the sites of the carbohydrate moieties that, in turn, helped to verify the position of the receptor relative to the viral surface.
12663789	6	13	theme	canyon	1204:1209	arg1	rim					1193:1195	the north rim	1183:1195	the north rim of the canyon, especially the region immediately outside the viral hydrophobic pocket that normally binds a cellular "pocket factor,"	1183:1329	In contrast, the interaction of CD155 with the north rim of the canyon, especially the region immediately outside the viral hydrophobic pocket that normally binds a cellular "pocket factor," may be critical for the release of the pocket factor, decreasing the virus stability and hence initiating uncoating.
12663789	5	14	theme	PV	948:949	arg1	surfaces					951:958	PV surfaces	948:958	PV surfaces	948:958	The footprints of CD155 on PV surfaces indicate that the south rim of the canyon dominates the virus-receptor interactions and may correspond to the initial CD155 binding state of the receptor-mediated viral uncoating.
12663789	7	15	theme	footprint	1476:1484	arg1	limitation					1587:1596	a potential limitation	1575:1596	a potential limitation on the viability of PV escape mutants from antibody neutralization	1575:1663	The large area of the CD155 footprint on the PV surface, in comparison with other picornavirus-receptor interactions, could be a potential limitation on the viability of PV escape mutants from antibody neutralization.
12663789	7	15	theme	footprint	1476:1484	arg1	area					1458:1461	The large area	1448:1461	The large area of the CD155 footprint on the PV surface	1448:1502	The large area of the CD155 footprint on the PV surface, in comparison with other picornavirus-receptor interactions, could be a potential limitation on the viability of PV escape mutants from antibody neutralization.
12663789	6	16	from	contrast	1143:1150	arg1	critical					1338:1345	critical	1338:1345	critical	1338:1345	In contrast, the interaction of CD155 with the north rim of the canyon, especially the region immediately outside the viral hydrophobic pocket that normally binds a cellular "pocket factor," may be critical for the release of the pocket factor, decreasing the virus stability and hence initiating uncoating.
12663789	6	16	from	contrast	1143:1150	arg1	interaction					1157:1167	the interaction	1153:1167	the interaction of CD155 with the north rim of the canyon, especially the region immediately outside the viral hydrophobic pocket that normally binds a cellular "pocket factor,"	1153:1329	In contrast, the interaction of CD155 with the north rim of the canyon, especially the region immediately outside the viral hydrophobic pocket that normally binds a cellular "pocket factor," may be critical for the release of the pocket factor, decreasing the virus stability and hence initiating uncoating.
12663789	5	17	theme	virus-receptor	1016:1029	arg1	interactions					1031:1042	the virus-receptor interactions	1012:1042	the virus-receptor interactions	1012:1042	The footprints of CD155 on PV surfaces indicate that the south rim of the canyon dominates the virus-receptor interactions and may correspond to the initial CD155 binding state of the receptor-mediated viral uncoating.
12663789	7	18	from	footprint	1476:1484	arg1	surface					1496:1502	the PV surface	1489:1502	the PV surface	1489:1502	The large area of the CD155 footprint on the PV surface, in comparison with other picornavirus-receptor interactions, could be a potential limitation on the viability of PV escape mutants from antibody neutralization.
12663789	6	19	theme	viral	1258:1262	arg1	pocket					1276:1281	the viral hydrophobic pocket	1254:1281	the viral hydrophobic pocket that normally binds a cellular "pocket factor,"	1254:1329	In contrast, the interaction of CD155 with the north rim of the canyon, especially the region immediately outside the viral hydrophobic pocket that normally binds a cellular "pocket factor," may be critical for the release of the pocket factor, decreasing the virus stability and hence initiating uncoating.
12663789	4	20	from	surface	764:770	arg1	complex					794:800	the receptor-virus complex	775:800	the receptor-virus complex	775:800	The proximity of the CD155 carbohydrate site at Asn105 to the viral surface in the receptor-virus complex suggests that it might interfere with receptor docking, an observation consistent with the properties of mutant CD155.
12663789	7	21	from	surface	1496:1502	arg1	limitation					1587:1596	a potential limitation	1575:1596	a potential limitation on the viability of PV escape mutants from antibody neutralization	1575:1663	The large area of the CD155 footprint on the PV surface, in comparison with other picornavirus-receptor interactions, could be a potential limitation on the viability of PV escape mutants from antibody neutralization.
12663789	7	21	from	surface	1496:1502	arg1	area					1458:1461	The large area	1448:1461	The large area of the CD155 footprint on the PV surface	1448:1502	The large area of the CD155 footprint on the PV surface, in comparison with other picornavirus-receptor interactions, could be a potential limitation on the viability of PV escape mutants from antibody neutralization.
12663789	2	22	theme	binding	327:333	arg1	sites					335:339	similar binding sites	319:339	similar binding sites	319:339	Both glycosylated and fully deglycosylated CD155 exhibited similar binding sites and orientations in the viral canyon for all three PV serotypes, showing that all three serotypes use a common mechanism for cell entry.
12663789	5	23	theme	CD155	1078:1082	arg1	state					1092:1096	the initial CD155 binding state	1066:1096	the initial CD155 binding state of the receptor-mediated viral uncoating	1066:1137	The footprints of CD155 on PV surfaces indicate that the south rim of the canyon dominates the virus-receptor interactions and may correspond to the initial CD155 binding state of the receptor-mediated viral uncoating.
12663789	7	24	theme	other	1524:1528	arg1	interactions					1552:1563	other picornavirus-receptor interactions	1524:1563	other picornavirus-receptor interactions	1524:1563	The large area of the CD155 footprint on the PV surface, in comparison with other picornavirus-receptor interactions, could be a potential limitation on the viability of PV escape mutants from antibody neutralization.
12663789	1	25	dep	serotypes	118:126	arg1	PV2					134:136	PV2	134:136	PV2	134:136	Structures of all three poliovirus (PV) serotypes (PV1, PV2, and PV3) complexed with their cellular receptor, PV receptor (PVR or CD155), were determined by cryoelectron microscopy.
12663789	1	25	dep	serotypes	118:126	arg1	PV3					143:145	PV3	143:145	PV3	143:145	Structures of all three poliovirus (PV) serotypes (PV1, PV2, and PV3) complexed with their cellular receptor, PV receptor (PVR or CD155), were determined by cryoelectron microscopy.
12663789	1	25	dep	serotypes	118:126	arg1	PV1					129:131	PV1	129:131	PV1	129:131	Structures of all three poliovirus (PV) serotypes (PV1, PV2, and PV3) complexed with their cellular receptor, PV receptor (PVR or CD155), were determined by cryoelectron microscopy.
12663789	1	25	dep	serotypes	118:126	arg1	serotypes					118:126	all three poliovirus (PV) serotypes	92:126	all three poliovirus (PV) serotypes (PV1, PV2, and PV3) complexed with their cellular receptor, PV receptor (PVR or CD155),	92:214	Structures of all three poliovirus (PV) serotypes (PV1, PV2, and PV3) complexed with their cellular receptor, PV receptor (PVR or CD155), were determined by cryoelectron microscopy.
12663789	2	26	theme	viral	365:369	arg1	canyon					371:376	the viral canyon	361:376	the viral canyon for all three PV serotypes	361:403	Both glycosylated and fully deglycosylated CD155 exhibited similar binding sites and orientations in the viral canyon for all three PV serotypes, showing that all three serotypes use a common mechanism for cell entry.
12663789	0	27	theme	poliovirus	13:22	arg1	serotypes					24:32	poliovirus serotypes	13:32	poliovirus serotypes	13:32	Complexes of poliovirus serotypes with their common cellular receptor, CD155.
12663789	4	28	theme	CD155	914:918	arg1	properties					893:902	the properties	889:902	the properties of mutant CD155	889:918	The proximity of the CD155 carbohydrate site at Asn105 to the viral surface in the receptor-virus complex suggests that it might interfere with receptor docking, an observation consistent with the properties of mutant CD155.
12663789	3	29	theme	moieties	595:602	arg1	moieties					595:602	the carbohydrate moieties	578:602	the carbohydrate moieties that, in turn, helped to verify the position of the receptor relative to the viral surface	578:693	Difference maps between the glycosylated and deglycosylated CD155 complexes determined the sites of the carbohydrate moieties that, in turn, helped to verify the position of the receptor relative to the viral surface.
12663789	3	29	theme	moieties	595:602	arg1	sites					569:573	the sites	565:573	the sites of the carbohydrate moieties that, in turn, helped to verify the position of the receptor relative to the viral surface	565:693	Difference maps between the glycosylated and deglycosylated CD155 complexes determined the sites of the carbohydrate moieties that, in turn, helped to verify the position of the receptor relative to the viral surface.
12663789	4	30	theme	site	736:739	arg1	proximity					700:708	The proximity	696:708	The proximity of the CD155 carbohydrate site at Asn105 to the viral surface in the receptor-virus complex	696:800	The proximity of the CD155 carbohydrate site at Asn105 to the viral surface in the receptor-virus complex suggests that it might interfere with receptor docking, an observation consistent with the properties of mutant CD155.
12663789	2	31	gly	glycosylated	265:276	arg1	CD155					303:307	Both glycosylated and fully deglycosylated CD155	260:307	Both glycosylated and fully deglycosylated CD155	260:307	Both glycosylated and fully deglycosylated CD155 exhibited similar binding sites and orientations in the viral canyon for all three PV serotypes, showing that all three serotypes use a common mechanism for cell entry.
12663789	0	32	theme	common	45:50	arg1	CD155					71:75	CD155	71:75	CD155	71:75	Complexes of poliovirus serotypes with their common cellular receptor, CD155.
12663789	0	32	theme	common	45:50	arg1	receptor					61:68	their common cellular receptor	39:68	their common cellular receptor	39:68	Complexes of poliovirus serotypes with their common cellular receptor, CD155.
12663789	1	33	theme	cryoelectron	235:246	arg1	microscopy					248:257	cryoelectron microscopy	235:257	cryoelectron microscopy	235:257	Structures of all three poliovirus (PV) serotypes (PV1, PV2, and PV3) complexed with their cellular receptor, PV receptor (PVR or CD155), were determined by cryoelectron microscopy.
12663789	7	34	from	area	1458:1461	arg1	surface					1496:1502	the PV surface	1489:1502	the PV surface	1489:1502	The large area of the CD155 footprint on the PV surface, in comparison with other picornavirus-receptor interactions, could be a potential limitation on the viability of PV escape mutants from antibody neutralization.
12663789	0	35	with	Complexes	0:8	arg1	CD155					71:75	CD155	71:75	CD155	71:75	Complexes of poliovirus serotypes with their common cellular receptor, CD155.
12663789	0	35	with	Complexes	0:8	arg1	receptor					61:68	their common cellular receptor	39:68	their common cellular receptor	39:68	Complexes of poliovirus serotypes with their common cellular receptor, CD155.
12663789	1	36	theme	cellular	169:176	arg1	receptor					178:185	their cellular receptor	163:185	their cellular receptor	163:185	Structures of all three poliovirus (PV) serotypes (PV1, PV2, and PV3) complexed with their cellular receptor, PV receptor (PVR or CD155), were determined by cryoelectron microscopy.
12663789	1	36	theme	cellular	169:176	arg1	receptor					191:198	PV receptor	188:198	PV receptor (PVR or CD155)	188:213	Structures of all three poliovirus (PV) serotypes (PV1, PV2, and PV3) complexed with their cellular receptor, PV receptor (PVR or CD155), were determined by cryoelectron microscopy.
12663789	4	37	with	consistent	873:882	arg1	properties					893:902	the properties	889:902	the properties of mutant CD155	889:918	The proximity of the CD155 carbohydrate site at Asn105 to the viral surface in the receptor-virus complex suggests that it might interfere with receptor docking, an observation consistent with the properties of mutant CD155.
12663789	4	38	theme	CD155	717:721	arg1	site					736:739	the CD155 carbohydrate site	713:739	the CD155 carbohydrate site at Asn105	713:749	The proximity of the CD155 carbohydrate site at Asn105 to the viral surface in the receptor-virus complex suggests that it might interfere with receptor docking, an observation consistent with the properties of mutant CD155.
12663789	6	39	theme	cellular	1305:1312	arg1	"					1329:1329	"	1329:1329	"	1329:1329	In contrast, the interaction of CD155 with the north rim of the canyon, especially the region immediately outside the viral hydrophobic pocket that normally binds a cellular "pocket factor," may be critical for the release of the pocket factor, decreasing the virus stability and hence initiating uncoating.
12663789	6	39	theme	cellular	1305:1312	arg1	factor					1322:1327	a cellular "pocket factor	1303:1327	a cellular "pocket factor	1303:1327	In contrast, the interaction of CD155 with the north rim of the canyon, especially the region immediately outside the viral hydrophobic pocket that normally binds a cellular "pocket factor," may be critical for the release of the pocket factor, decreasing the virus stability and hence initiating uncoating.
12663789	2	40	theme	deglycosylated	288:301	arg1	CD155					303:307	Both glycosylated and fully deglycosylated CD155	260:307	Both glycosylated and fully deglycosylated CD155	260:307	Both glycosylated and fully deglycosylated CD155 exhibited similar binding sites and orientations in the viral canyon for all three PV serotypes, showing that all three serotypes use a common mechanism for cell entry.
12663789	5	41	theme	viral	1123:1127	arg1	uncoating					1129:1137	the receptor-mediated viral uncoating	1101:1137	the receptor-mediated viral uncoating	1101:1137	The footprints of CD155 on PV surfaces indicate that the south rim of the canyon dominates the virus-receptor interactions and may correspond to the initial CD155 binding state of the receptor-mediated viral uncoating.
12663789	4	42	theme	receptor-virus	779:792	arg1	complex					794:800	the receptor-virus complex	775:800	the receptor-virus complex	775:800	The proximity of the CD155 carbohydrate site at Asn105 to the viral surface in the receptor-virus complex suggests that it might interfere with receptor docking, an observation consistent with the properties of mutant CD155.
12663789	6	43	theme	CD155	1172:1176	arg1	interaction					1157:1167	the interaction	1153:1167	the interaction of CD155 with the north rim of the canyon, especially the region immediately outside the viral hydrophobic pocket that normally binds a cellular "pocket factor,"	1153:1329	In contrast, the interaction of CD155 with the north rim of the canyon, especially the region immediately outside the viral hydrophobic pocket that normally binds a cellular "pocket factor," may be critical for the release of the pocket factor, decreasing the virus stability and hence initiating uncoating.
12663789	6	43	theme	CD155	1172:1176	arg1	critical					1338:1345	critical	1338:1345	critical	1338:1345	In contrast, the interaction of CD155 with the north rim of the canyon, especially the region immediately outside the viral hydrophobic pocket that normally binds a cellular "pocket factor," may be critical for the release of the pocket factor, decreasing the virus stability and hence initiating uncoating.
12663789	6	44	theme	virus	1400:1404	arg1	stability					1406:1414	the virus stability	1396:1414	the virus stability	1396:1414	In contrast, the interaction of CD155 with the north rim of the canyon, especially the region immediately outside the viral hydrophobic pocket that normally binds a cellular "pocket factor," may be critical for the release of the pocket factor, decreasing the virus stability and hence initiating uncoating.
12663789	4	45	theme	viral	758:762	arg1	surface					764:770	the viral surface	754:770	the viral surface in the receptor-virus complex	754:800	The proximity of the CD155 carbohydrate site at Asn105 to the viral surface in the receptor-virus complex suggests that it might interfere with receptor docking, an observation consistent with the properties of mutant CD155.
12663789	7	46	theme	escape	1621:1626	arg1	mutants					1628:1634	PV escape mutants	1618:1634	PV escape mutants from antibody neutralization	1618:1663	The large area of the CD155 footprint on the PV surface, in comparison with other picornavirus-receptor interactions, could be a potential limitation on the viability of PV escape mutants from antibody neutralization.
12663789	7	47	from	viability	1605:1613	arg1	neutralization					1650:1663	antibody neutralization	1641:1663	antibody neutralization	1641:1663	The large area of the CD155 footprint on the PV surface, in comparison with other picornavirus-receptor interactions, could be a potential limitation on the viability of PV escape mutants from antibody neutralization.
12663789	3	48	theme	Difference	478:487	arg1	maps					489:492	Difference maps	478:492	Difference maps between the glycosylated and deglycosylated CD155 complexes	478:552	Difference maps between the glycosylated and deglycosylated CD155 complexes determined the sites of the carbohydrate moieties that, in turn, helped to verify the position of the receptor relative to the viral surface.
12663789	7	49	theme	PV	1493:1494	arg1	surface					1496:1502	the PV surface	1489:1502	the PV surface	1489:1502	The large area of the CD155 footprint on the PV surface, in comparison with other picornavirus-receptor interactions, could be a potential limitation on the viability of PV escape mutants from antibody neutralization.
12663789	7	50	with	comparison	1508:1517	arg1	interactions					1552:1563	other picornavirus-receptor interactions	1524:1563	other picornavirus-receptor interactions	1524:1563	The large area of the CD155 footprint on the PV surface, in comparison with other picornavirus-receptor interactions, could be a potential limitation on the viability of PV escape mutants from antibody neutralization.
12663789	3	51	gly	deglycosylated	523:536	arg1	complexes					544:552	deglycosylated CD155 complexes	523:552	deglycosylated CD155 complexes	523:552	Difference maps between the glycosylated and deglycosylated CD155 complexes determined the sites of the carbohydrate moieties that, in turn, helped to verify the position of the receptor relative to the viral surface.
12663789	5	52	theme	south	978:982	arg1	rim					984:986	the south rim	974:986	the south rim of the canyon	974:1000	The footprints of CD155 on PV surfaces indicate that the south rim of the canyon dominates the virus-receptor interactions and may correspond to the initial CD155 binding state of the receptor-mediated viral uncoating.
12663789	3	53	theme	deglycosylated	523:536	arg1	complexes					544:552	deglycosylated CD155 complexes	523:552	deglycosylated CD155 complexes	523:552	Difference maps between the glycosylated and deglycosylated CD155 complexes determined the sites of the carbohydrate moieties that, in turn, helped to verify the position of the receptor relative to the viral surface.
12663789	6	54	theme	factor	1377:1382	arg1	release					1355:1361	the release	1351:1361	the release of the pocket factor	1351:1382	In contrast, the interaction of CD155 with the north rim of the canyon, especially the region immediately outside the viral hydrophobic pocket that normally binds a cellular "pocket factor," may be critical for the release of the pocket factor, decreasing the virus stability and hence initiating uncoating.
12663789	4	55	theme	receptor	840:847	arg1	docking					849:855	receptor docking	840:855	receptor docking	840:855	The proximity of the CD155 carbohydrate site at Asn105 to the viral surface in the receptor-virus complex suggests that it might interfere with receptor docking, an observation consistent with the properties of mutant CD155.
12663789	1	56	theme	poliovirus	102:111	arg1	PV2					134:136	PV2	134:136	PV2	134:136	Structures of all three poliovirus (PV) serotypes (PV1, PV2, and PV3) complexed with their cellular receptor, PV receptor (PVR or CD155), were determined by cryoelectron microscopy.
12663789	1	56	theme	poliovirus	102:111	arg1	PV3					143:145	PV3	143:145	PV3	143:145	Structures of all three poliovirus (PV) serotypes (PV1, PV2, and PV3) complexed with their cellular receptor, PV receptor (PVR or CD155), were determined by cryoelectron microscopy.
12663789	1	56	theme	poliovirus	102:111	arg1	PV1					129:131	PV1	129:131	PV1	129:131	Structures of all three poliovirus (PV) serotypes (PV1, PV2, and PV3) complexed with their cellular receptor, PV receptor (PVR or CD155), were determined by cryoelectron microscopy.
12663789	1	56	theme	poliovirus	102:111	arg1	serotypes					118:126	all three poliovirus (PV) serotypes	92:126	all three poliovirus (PV) serotypes (PV1, PV2, and PV3) complexed with their cellular receptor, PV receptor (PVR or CD155),	92:214	Structures of all three poliovirus (PV) serotypes (PV1, PV2, and PV3) complexed with their cellular receptor, PV receptor (PVR or CD155), were determined by cryoelectron microscopy.
12663789	7	57	theme	CD155	1470:1474	arg1	footprint					1476:1484	the CD155 footprint	1466:1484	the CD155 footprint on the PV surface	1466:1502	The large area of the CD155 footprint on the PV surface, in comparison with other picornavirus-receptor interactions, could be a potential limitation on the viability of PV escape mutants from antibody neutralization.
12663789	7	58	theme	PV	1618:1619	arg1	mutants					1628:1634	PV escape mutants	1618:1634	PV escape mutants from antibody neutralization	1618:1663	The large area of the CD155 footprint on the PV surface, in comparison with other picornavirus-receptor interactions, could be a potential limitation on the viability of PV escape mutants from antibody neutralization.
12663789	1	59	dep	receptor	191:198	arg1	CD155					208:212	CD155	208:212	CD155	208:212	Structures of all three poliovirus (PV) serotypes (PV1, PV2, and PV3) complexed with their cellular receptor, PV receptor (PVR or CD155), were determined by cryoelectron microscopy.
12663789	1	59	dep	receptor	191:198	arg1	PVR					201:203	PVR	201:203	PVR	201:203	Structures of all three poliovirus (PV) serotypes (PV1, PV2, and PV3) complexed with their cellular receptor, PV receptor (PVR or CD155), were determined by cryoelectron microscopy.
12663789	1	60	theme	serotypes	118:126	arg1	Structures					78:87	Structures	78:87	Structures of all three poliovirus (PV) serotypes (PV1, PV2, and PV3) complexed with their cellular receptor, PV receptor (PVR or CD155),	78:214	Structures of all three poliovirus (PV) serotypes (PV1, PV2, and PV3) complexed with their cellular receptor, PV receptor (PVR or CD155), were determined by cryoelectron microscopy.
12663789	7	61	theme	large	1452:1456	arg1	limitation					1587:1596	a potential limitation	1575:1596	a potential limitation on the viability of PV escape mutants from antibody neutralization	1575:1663	The large area of the CD155 footprint on the PV surface, in comparison with other picornavirus-receptor interactions, could be a potential limitation on the viability of PV escape mutants from antibody neutralization.
12663789	7	61	theme	large	1452:1456	arg1	area					1458:1461	The large area	1448:1461	The large area of the CD155 footprint on the PV surface	1448:1502	The large area of the CD155 footprint on the PV surface, in comparison with other picornavirus-receptor interactions, could be a potential limitation on the viability of PV escape mutants from antibody neutralization.
12663789	4	62	from	proximity	700:708	arg1	Asn105					744:749	Asn105	744:749	Asn105	744:749	The proximity of the CD155 carbohydrate site at Asn105 to the viral surface in the receptor-virus complex suggests that it might interfere with receptor docking, an observation consistent with the properties of mutant CD155.
12663789	6	63	theme	hydrophobic	1264:1274	arg1	pocket					1276:1281	the viral hydrophobic pocket	1254:1281	the viral hydrophobic pocket that normally binds a cellular "pocket factor,"	1254:1329	In contrast, the interaction of CD155 with the north rim of the canyon, especially the region immediately outside the viral hydrophobic pocket that normally binds a cellular "pocket factor," may be critical for the release of the pocket factor, decreasing the virus stability and hence initiating uncoating.
12663789	8	64	theme	these	1674:1678	arg1	these					1674:1678	these	1674:1678	these	1674:1678	Many of these are likely to have lost their ability to bind CD155, resulting in there being only three PV serotypes.
12663789	8	64	theme	these	1674:1678	arg1	Many					1666:1669	Many	1666:1669	Many	1666:1669	Many of these are likely to have lost their ability to bind CD155, resulting in there being only three PV serotypes.
12663789	7	65	theme	potential	1577:1585	arg1	limitation					1587:1596	a potential limitation	1575:1596	a potential limitation on the viability of PV escape mutants from antibody neutralization	1575:1663	The large area of the CD155 footprint on the PV surface, in comparison with other picornavirus-receptor interactions, could be a potential limitation on the viability of PV escape mutants from antibody neutralization.
12663789	7	65	theme	potential	1577:1585	arg1	area					1458:1461	The large area	1448:1461	The large area of the CD155 footprint on the PV surface	1448:1502	The large area of the CD155 footprint on the PV surface, in comparison with other picornavirus-receptor interactions, could be a potential limitation on the viability of PV escape mutants from antibody neutralization.
12663789	2	66	theme	common	445:450	arg1	mechanism					452:460	a common mechanism	443:460	a common mechanism for cell entry	443:475	Both glycosylated and fully deglycosylated CD155 exhibited similar binding sites and orientations in the viral canyon for all three PV serotypes, showing that all three serotypes use a common mechanism for cell entry.
12663789	5	67	theme	canyon	995:1000	arg1	rim					984:986	the south rim	974:986	the south rim of the canyon	974:1000	The footprints of CD155 on PV surfaces indicate that the south rim of the canyon dominates the virus-receptor interactions and may correspond to the initial CD155 binding state of the receptor-mediated viral uncoating.
12663789	2	68	theme	similar	319:325	arg1	sites					335:339	similar binding sites	319:339	similar binding sites	319:339	Both glycosylated and fully deglycosylated CD155 exhibited similar binding sites and orientations in the viral canyon for all three PV serotypes, showing that all three serotypes use a common mechanism for cell entry.
12663789	0	69	theme	serotypes	24:32	arg1	Complexes					0:8	Complexes	0:8	Complexes of poliovirus serotypes with their common cellular receptor, CD155	0:75	Complexes of poliovirus serotypes with their common cellular receptor, CD155.
12663789	5	70	theme	binding	1084:1090	arg1	state					1092:1096	the initial CD155 binding state	1066:1096	the initial CD155 binding state of the receptor-mediated viral uncoating	1066:1137	The footprints of CD155 on PV surfaces indicate that the south rim of the canyon dominates the virus-receptor interactions and may correspond to the initial CD155 binding state of the receptor-mediated viral uncoating.
12663789	7	71	theme	picornavirus-receptor	1530:1550	arg1	interactions					1552:1563	other picornavirus-receptor interactions	1524:1563	other picornavirus-receptor interactions	1524:1563	The large area of the CD155 footprint on the PV surface, in comparison with other picornavirus-receptor interactions, could be a potential limitation on the viability of PV escape mutants from antibody neutralization.
12663789	3	72	theme	carbohydrate	582:593	arg1	moieties					595:602	the carbohydrate moieties	578:602	the carbohydrate moieties that, in turn, helped to verify the position of the receptor relative to the viral surface	578:693	Difference maps between the glycosylated and deglycosylated CD155 complexes determined the sites of the carbohydrate moieties that, in turn, helped to verify the position of the receptor relative to the viral surface.
12663789	6	73	theme	pocket	1315:1320	arg1	"					1329:1329	"	1329:1329	"	1329:1329	In contrast, the interaction of CD155 with the north rim of the canyon, especially the region immediately outside the viral hydrophobic pocket that normally binds a cellular "pocket factor," may be critical for the release of the pocket factor, decreasing the virus stability and hence initiating uncoating.
12663789	6	73	theme	pocket	1315:1320	arg1	factor					1322:1327	a cellular "pocket factor	1303:1327	a cellular "pocket factor	1303:1327	In contrast, the interaction of CD155 with the north rim of the canyon, especially the region immediately outside the viral hydrophobic pocket that normally binds a cellular "pocket factor," may be critical for the release of the pocket factor, decreasing the virus stability and hence initiating uncoating.
12663789	4	74	theme	mutant	907:912	arg1	CD155					914:918	mutant CD155	907:918	mutant CD155	907:918	The proximity of the CD155 carbohydrate site at Asn105 to the viral surface in the receptor-virus complex suggests that it might interfere with receptor docking, an observation consistent with the properties of mutant CD155.
12663789	2	75	gly	deglycosylated	288:301	arg1	CD155					303:307	Both glycosylated and fully deglycosylated CD155	260:307	Both glycosylated and fully deglycosylated CD155	260:307	Both glycosylated and fully deglycosylated CD155 exhibited similar binding sites and orientations in the viral canyon for all three PV serotypes, showing that all three serotypes use a common mechanism for cell entry.
12663789	4	76	theme	carbohydrate	723:734	arg1	site					736:739	the CD155 carbohydrate site	713:739	the CD155 carbohydrate site at Asn105	713:749	The proximity of the CD155 carbohydrate site at Asn105 to the viral surface in the receptor-virus complex suggests that it might interfere with receptor docking, an observation consistent with the properties of mutant CD155.
12663789	0	77	theme	cellular	52:59	arg1	CD155					71:75	CD155	71:75	CD155	71:75	Complexes of poliovirus serotypes with their common cellular receptor, CD155.
12663789	0	77	theme	cellular	52:59	arg1	receptor					61:68	their common cellular receptor	39:68	their common cellular receptor	39:68	Complexes of poliovirus serotypes with their common cellular receptor, CD155.
12663789	5	78	theme	CD155	939:943	arg1	footprints					925:934	The footprints	921:934	The footprints of CD155 on PV surfaces	921:958	The footprints of CD155 on PV surfaces indicate that the south rim of the canyon dominates the virus-receptor interactions and may correspond to the initial CD155 binding state of the receptor-mediated viral uncoating.
12663789	2	79	theme	PV	392:393	arg1	serotypes					395:403	all three PV serotypes	382:403	all three PV serotypes	382:403	Both glycosylated and fully deglycosylated CD155 exhibited similar binding sites and orientations in the viral canyon for all three PV serotypes, showing that all three serotypes use a common mechanism for cell entry.
12663789	2	80	theme	glycosylated	265:276	arg1	CD155					303:307	Both glycosylated and fully deglycosylated CD155	260:307	Both glycosylated and fully deglycosylated CD155	260:307	Both glycosylated and fully deglycosylated CD155 exhibited similar binding sites and orientations in the viral canyon for all three PV serotypes, showing that all three serotypes use a common mechanism for cell entry.
12663789	6	81	theme	pocket	1370:1375	arg1	factor					1377:1382	the pocket factor	1366:1382	the pocket factor	1366:1382	In contrast, the interaction of CD155 with the north rim of the canyon, especially the region immediately outside the viral hydrophobic pocket that normally binds a cellular "pocket factor," may be critical for the release of the pocket factor, decreasing the virus stability and hence initiating uncoating.
12663789	5	82	theme	initial	1070:1076	arg1	state					1092:1096	the initial CD155 binding state	1066:1096	the initial CD155 binding state of the receptor-mediated viral uncoating	1066:1137	The footprints of CD155 on PV surfaces indicate that the south rim of the canyon dominates the virus-receptor interactions and may correspond to the initial CD155 binding state of the receptor-mediated viral uncoating.
12663789	6	83	from	critical	1338:1345	arg1	contrast					1143:1150	contrast	1143:1150	contrast	1143:1150	In contrast, the interaction of CD155 with the north rim of the canyon, especially the region immediately outside the viral hydrophobic pocket that normally binds a cellular "pocket factor," may be critical for the release of the pocket factor, decreasing the virus stability and hence initiating uncoating.
12663789	7	84	from	neutralization	1650:1663	arg1	viability					1605:1613	the viability	1601:1613	the viability of PV escape mutants from antibody neutralization	1601:1663	The large area of the CD155 footprint on the PV surface, in comparison with other picornavirus-receptor interactions, could be a potential limitation on the viability of PV escape mutants from antibody neutralization.
12663789	7	84	from	neutralization	1650:1663	arg1	mutants					1628:1634	PV escape mutants	1618:1634	PV escape mutants from antibody neutralization	1618:1663	The large area of the CD155 footprint on the PV surface, in comparison with other picornavirus-receptor interactions, could be a potential limitation on the viability of PV escape mutants from antibody neutralization.
12663789	6	85	with	interaction	1157:1167	arg1	rim					1193:1195	the north rim	1183:1195	the north rim of the canyon, especially the region immediately outside the viral hydrophobic pocket that normally binds a cellular "pocket factor,"	1183:1329	In contrast, the interaction of CD155 with the north rim of the canyon, especially the region immediately outside the viral hydrophobic pocket that normally binds a cellular "pocket factor," may be critical for the release of the pocket factor, decreasing the virus stability and hence initiating uncoating.
12663789	1	86	theme	PV	188:189	arg1	receptor					178:185	their cellular receptor	163:185	their cellular receptor	163:185	Structures of all three poliovirus (PV) serotypes (PV1, PV2, and PV3) complexed with their cellular receptor, PV receptor (PVR or CD155), were determined by cryoelectron microscopy.
12663789	1	86	theme	PV	188:189	arg1	receptor					191:198	PV receptor	188:198	PV receptor (PVR or CD155)	188:213	Structures of all three poliovirus (PV) serotypes (PV1, PV2, and PV3) complexed with their cellular receptor, PV receptor (PVR or CD155), were determined by cryoelectron microscopy.
8344280	2	0	with	proteins	229:236	arg1	N-glycosylation					268:282	artificially introduced N-glycosylation or O-glycosylation sites	244:307	N-glycosylation	268:282	Human interleukin 2 (IL-2) and human IL-2 mutant proteins, with artificially introduced N-glycosylation or O-glycosylation sites, have been expressed in a lepidopteran cell line (Sf21, Spodoptera frugiperda) using recombinant baculovirus vectors.
8344280	2	0	with	proteins	229:236	arg1	sites					303:307	artificially introduced N-glycosylation or O-glycosylation sites	244:307	sites	303:307	Human interleukin 2 (IL-2) and human IL-2 mutant proteins, with artificially introduced N-glycosylation or O-glycosylation sites, have been expressed in a lepidopteran cell line (Sf21, Spodoptera frugiperda) using recombinant baculovirus vectors.
8344280	10	1	theme	mammalian-type	1491:1504	arg1	glycoforms					1506:1515	mammalian-type glycoforms	1491:1515	mammalian-type glycoforms	1491:1515	The Gal(beta 1-3)GalNAc protein forms could be partially altered in vitro to mammalian-type glycoforms by porcine liver beta-galactoside alpha-2,3-sialyltransferase in the presence of CMP-N-acetylneuraminic acid.
8344280	11	2	theme	mutant	1635:1640	arg1	form					1642:1645	An IL-2 mutant form	1627:1645	An IL-2 mutant form	1627:1645	An IL-2 mutant form, with an 11-amino-acid peptide of human interferon-beta at position 4, which includes its only N-glycosylation site, had exclusively truncated proximally fucosylated oligomannosidic glycans; Man3GlcNAc[Fuc(alpha 1-6)]GlcNAc or Man2GlcNAc[Fuc(alpha 1-6)]GlcNAc structures, in a ratio of 3:1, were detected in the secreted proteins.
8344280	2	3	theme	Spodoptera	365:374	arg1	Sf21					359:362	Sf21	359:362	Sf21	359:362	Human interleukin 2 (IL-2) and human IL-2 mutant proteins, with artificially introduced N-glycosylation or O-glycosylation sites, have been expressed in a lepidopteran cell line (Sf21, Spodoptera frugiperda) using recombinant baculovirus vectors.
8344280	2	3	theme	Spodoptera	365:374	arg1	frugiperda					376:385	Spodoptera frugiperda	365:385	Spodoptera frugiperda	365:385	Human interleukin 2 (IL-2) and human IL-2 mutant proteins, with artificially introduced N-glycosylation or O-glycosylation sites, have been expressed in a lepidopteran cell line (Sf21, Spodoptera frugiperda) using recombinant baculovirus vectors.
8344280	9	4	theme	mutant	1398:1403	arg1	protein					1405:1411	each individual IL-2 mutant protein	1377:1411	each individual IL-2 mutant protein	1377:1411	Fast atom bombardment mass spectrometry, compositional analysis and methylation analysis, of the tryptic glycopeptide APTPPPK, revealed the presence of either GalNAc or the disaccharide Gal(beta 1-3)GalNAc as the only carbohydrate constituents attached exclusively to Thr in this peptide, in a specific ratio for each individual IL-2 mutant protein.
8344280	8	5	theme	IL-2	962:965	arg1	chain					979:983	the IL-2 polypeptide chain	958:983	the IL-2 polypeptide chain	958:983	, to the C-terminus or between positions 80 and 81 of the IL-2 polypeptide chain, resulted in the secretion of unglycosylated and O-glycosylated variant forms.
8344280	5	6	from	forms	715:719	arg1	absent					685:690	absent	685:690	absent	685:690	Alanine and proline were absent in the major truncated forms; the first 3-5 amino acids were also absent in a small proportion of the purified proteins.
8344280	8	7	theme	chain	979:983	arg1	positions					935:943	positions 80 and 81	935:953	positions	935:943	, to the C-terminus or between positions 80 and 81 of the IL-2 polypeptide chain, resulted in the secretion of unglycosylated and O-glycosylated variant forms.
8344280	12	8	theme	cell-culture	2098:2109	arg1	conditions					2111:2120	the cell-culture conditions	2094:2120	the cell-culture conditions used	2094:2125	No evidence was obtained for the presence of secreted proteins with complex oligosaccharide chains, irrespective of the cell-culture conditions used or the harvesting time, for infected cells with recombinant baculovirus constructs.
8344280	10	9	theme	liver	1528:1532	arg1	alpha-2,3-sialyltransferase					1551:1577	porcine liver beta-galactoside alpha-2,3-sialyltransferase	1520:1577	porcine liver beta-galactoside alpha-2,3-sialyltransferase	1520:1577	The Gal(beta 1-3)GalNAc protein forms could be partially altered in vitro to mammalian-type glycoforms by porcine liver beta-galactoside alpha-2,3-sialyltransferase in the presence of CMP-N-acetylneuraminic acid.
8344280	2	10	theme	Human	180:184	arg1	interleukin					186:196	Human interleukin 2	180:198	Human interleukin 2 (IL-2)	180:205	Human interleukin 2 (IL-2) and human IL-2 mutant proteins, with artificially introduced N-glycosylation or O-glycosylation sites, have been expressed in a lepidopteran cell line (Sf21, Spodoptera frugiperda) using recombinant baculovirus vectors.
8344280	2	10	theme	Human	180:184	arg1	IL-2					201:204	IL-2	201:204	IL-2	201:204	Human interleukin 2 (IL-2) and human IL-2 mutant proteins, with artificially introduced N-glycosylation or O-glycosylation sites, have been expressed in a lepidopteran cell line (Sf21, Spodoptera frugiperda) using recombinant baculovirus vectors.
8344280	11	11	theme	oligomannosidic	1813:1827	arg1	glycans					1829:1835	truncated proximally fucosylated oligomannosidic glycans	1780:1835	truncated proximally fucosylated oligomannosidic glycans	1780:1835	An IL-2 mutant form, with an 11-amino-acid peptide of human interferon-beta at position 4, which includes its only N-glycosylation site, had exclusively truncated proximally fucosylated oligomannosidic glycans; Man3GlcNAc[Fuc(alpha 1-6)]GlcNAc or Man2GlcNAc[Fuc(alpha 1-6)]GlcNAc structures, in a ratio of 3:1, were detected in the secreted proteins.
8344280	9	12	theme	GalNAc	1223:1228	arg1	presence					1204:1211	the presence	1200:1211	the presence of either GalNAc or the disaccharide Gal(beta 1-3)GalNAc	1200:1268	Fast atom bombardment mass spectrometry, compositional analysis and methylation analysis, of the tryptic glycopeptide APTPPPK, revealed the presence of either GalNAc or the disaccharide Gal(beta 1-3)GalNAc as the only carbohydrate constituents attached exclusively to Thr in this peptide, in a specific ratio for each individual IL-2 mutant protein.
8344280	9	12	theme	GalNAc	1223:1228	arg1	constituents					1295:1306	the only carbohydrate constituents	1273:1306	the only carbohydrate constituents attached exclusively to Thr	1273:1334	Fast atom bombardment mass spectrometry, compositional analysis and methylation analysis, of the tryptic glycopeptide APTPPPK, revealed the presence of either GalNAc or the disaccharide Gal(beta 1-3)GalNAc as the only carbohydrate constituents attached exclusively to Thr in this peptide, in a specific ratio for each individual IL-2 mutant protein.
8344280	2	13	theme	lepidopteran	335:346	arg1	line					353:356	a lepidopteran cell line	333:356	a lepidopteran cell line (Sf21, Spodoptera frugiperda) using recombinant baculovirus vectors	333:424	Human interleukin 2 (IL-2) and human IL-2 mutant proteins, with artificially introduced N-glycosylation or O-glycosylation sites, have been expressed in a lepidopteran cell line (Sf21, Spodoptera frugiperda) using recombinant baculovirus vectors.
8344280	11	14	contain	had	1764:1766	arg2	glycans					1829:1835	truncated proximally fucosylated oligomannosidic glycans	1780:1835	truncated proximally fucosylated oligomannosidic glycans	1780:1835	An IL-2 mutant form, with an 11-amino-acid peptide of human interferon-beta at position 4, which includes its only N-glycosylation site, had exclusively truncated proximally fucosylated oligomannosidic glycans; Man3GlcNAc[Fuc(alpha 1-6)]GlcNAc or Man2GlcNAc[Fuc(alpha 1-6)]GlcNAc structures, in a ratio of 3:1, were detected in the secreted proteins.
8344280	11	14	contain	had	1764:1766	arg1	form					1642:1645	An IL-2 mutant form	1627:1645	An IL-2 mutant form	1627:1645	An IL-2 mutant form, with an 11-amino-acid peptide of human interferon-beta at position 4, which includes its only N-glycosylation site, had exclusively truncated proximally fucosylated oligomannosidic glycans; Man3GlcNAc[Fuc(alpha 1-6)]GlcNAc or Man2GlcNAc[Fuc(alpha 1-6)]GlcNAc structures, in a ratio of 3:1, were detected in the secreted proteins.
8344280	4	15	theme	molecules	648:656	arg1	%					639:639	up to 85%	631:639	up to 85% of the molecules	631:656	Significant N-terminal truncations were detected in the secreted polypeptides (up to 85% of the molecules).
8344280	4	15	theme	molecules	648:656	arg1	molecules					648:656	the molecules	644:656	the molecules	644:656	Significant N-terminal truncations were detected in the secreted polypeptides (up to 85% of the molecules).
8344280	11	16	gly	N-glycosylation	1742:1756	arg2	site					1758:1761	its only N-glycosylation site	1733:1761	its only N-glycosylation site	1733:1761	An IL-2 mutant form, with an 11-amino-acid peptide of human interferon-beta at position 4, which includes its only N-glycosylation site, had exclusively truncated proximally fucosylated oligomannosidic glycans; Man3GlcNAc[Fuc(alpha 1-6)]GlcNAc or Man2GlcNAc[Fuc(alpha 1-6)]GlcNAc structures, in a ratio of 3:1, were detected in the secreted proteins.
8344280	11	17	theme	proximally	1790:1799	arg1	glycans					1829:1835	truncated proximally fucosylated oligomannosidic glycans	1780:1835	truncated proximally fucosylated oligomannosidic glycans	1780:1835	An IL-2 mutant form, with an 11-amino-acid peptide of human interferon-beta at position 4, which includes its only N-glycosylation site, had exclusively truncated proximally fucosylated oligomannosidic glycans; Man3GlcNAc[Fuc(alpha 1-6)]GlcNAc or Man2GlcNAc[Fuc(alpha 1-6)]GlcNAc structures, in a ratio of 3:1, were detected in the secreted proteins.
8344280	9	18	theme	Gal	1250:1252	arg1	beta					1254:1257	beta 1-3	1254:1261	beta 1-3	1254:1261	Fast atom bombardment mass spectrometry, compositional analysis and methylation analysis, of the tryptic glycopeptide APTPPPK, revealed the presence of either GalNAc or the disaccharide Gal(beta 1-3)GalNAc as the only carbohydrate constituents attached exclusively to Thr in this peptide, in a specific ratio for each individual IL-2 mutant protein.
8344280	9	18	theme	Gal	1250:1252	arg1	GalNAc					1263:1268	the disaccharide Gal(beta 1-3)GalNAc	1233:1268	the disaccharide Gal(beta 1-3)GalNAc	1233:1268	Fast atom bombardment mass spectrometry, compositional analysis and methylation analysis, of the tryptic glycopeptide APTPPPK, revealed the presence of either GalNAc or the disaccharide Gal(beta 1-3)GalNAc as the only carbohydrate constituents attached exclusively to Thr in this peptide, in a specific ratio for each individual IL-2 mutant protein.
8344280	10	19	theme	acid	1621:1624	arg1	presence					1586:1593	the presence	1582:1593	the presence of CMP-N-acetylneuraminic acid	1582:1624	The Gal(beta 1-3)GalNAc protein forms could be partially altered in vitro to mammalian-type glycoforms by porcine liver beta-galactoside alpha-2,3-sialyltransferase in the presence of CMP-N-acetylneuraminic acid.
8344280	5	20	from	absent	758:763	arg1	proportion					776:785	a small proportion	768:785	a small proportion of the purified proteins	768:810	Alanine and proline were absent in the major truncated forms; the first 3-5 amino acids were also absent in a small proportion of the purified proteins.
8344280	12	21	theme	oligosaccharide	2054:2068	arg1	chains					2070:2075	complex oligosaccharide chains	2046:2075	complex oligosaccharide chains	2046:2075	No evidence was obtained for the presence of secreted proteins with complex oligosaccharide chains, irrespective of the cell-culture conditions used or the harvesting time, for infected cells with recombinant baculovirus constructs.
8344280	8	22	gly	unglycosylated	1015:1028	arg1	forms					1057:1061	unglycosylated and O-glycosylated variant forms	1015:1061	unglycosylated and O-glycosylated variant forms	1015:1061	, to the C-terminus or between positions 80 and 81 of the IL-2 polypeptide chain, resulted in the secretion of unglycosylated and O-glycosylated variant forms.
8344280	11	23	theme	N-glycosylation	1742:1756	arg1	site					1758:1761	its only N-glycosylation site	1733:1761	its only N-glycosylation site	1733:1761	An IL-2 mutant form, with an 11-amino-acid peptide of human interferon-beta at position 4, which includes its only N-glycosylation site, had exclusively truncated proximally fucosylated oligomannosidic glycans; Man3GlcNAc[Fuc(alpha 1-6)]GlcNAc or Man2GlcNAc[Fuc(alpha 1-6)]GlcNAc structures, in a ratio of 3:1, were detected in the secreted proteins.
8344280	5	24	theme	major	699:703	arg1	forms					715:719	the major truncated forms	695:719	the major truncated forms; the first 3-5 amino acids were also absent in a small proportion of the purified proteins	695:810	Alanine and proline were absent in the major truncated forms; the first 3-5 amino acids were also absent in a small proportion of the purified proteins.
8344280	4	25	dep	85	637:638	arg1	to					634:635	to	634:635	to	634:635	Significant N-terminal truncations were detected in the secreted polypeptides (up to 85% of the molecules).
8344280	2	26	theme	O-glycosylation	287:301	arg1	sites					303:307	artificially introduced N-glycosylation or O-glycosylation sites	244:307	sites	303:307	Human interleukin 2 (IL-2) and human IL-2 mutant proteins, with artificially introduced N-glycosylation or O-glycosylation sites, have been expressed in a lepidopteran cell line (Sf21, Spodoptera frugiperda) using recombinant baculovirus vectors.
8344280	1	27	theme	modifications	165:177	arg1	Characterization					110:125	Characterization	110:125	Characterization of polypeptides and posttranslational modifications.	110:178	Characterization of polypeptides and posttranslational modifications.
8344280	0	28	from	cells	103:107	arg1	secretion					17:25	secretion	17:25	secretion	17:25	Biosynthesis and secretion of human interleukin 2 glycoprotein variants from baculovirus-infected Sf21 cells.
8344280	0	28	from	cells	103:107	arg1	Biosynthesis					0:11	Biosynthesis	0:11	Biosynthesis	0:11	Biosynthesis and secretion of human interleukin 2 glycoprotein variants from baculovirus-infected Sf21 cells.
8344280	8	29	gly	O-glycosylated	1034:1047	arg1	forms					1057:1061	unglycosylated and O-glycosylated variant forms	1015:1061	unglycosylated and O-glycosylated variant forms	1015:1061	, to the C-terminus or between positions 80 and 81 of the IL-2 polypeptide chain, resulted in the secretion of unglycosylated and O-glycosylated variant forms.
8344280	10	30	dep	Gal	1418:1420	arg1	beta					1422:1425	beta 1-3	1422:1429	beta 1-3	1422:1429	The Gal(beta 1-3)GalNAc protein forms could be partially altered in vitro to mammalian-type glycoforms by porcine liver beta-galactoside alpha-2,3-sialyltransferase in the presence of CMP-N-acetylneuraminic acid.
8344280	0	31	theme	variants	63:70	arg1	secretion					17:25	secretion	17:25	secretion	17:25	Biosynthesis and secretion of human interleukin 2 glycoprotein variants from baculovirus-infected Sf21 cells.
8344280	0	31	theme	variants	63:70	arg1	Biosynthesis					0:11	Biosynthesis	0:11	Biosynthesis	0:11	Biosynthesis and secretion of human interleukin 2 glycoprotein variants from baculovirus-infected Sf21 cells.
8344280	5	32	from	proportion	776:785	arg1	acids					742:746	the first 3-5 amino acids	722:746	the first 3-5 amino acids	722:746	Alanine and proline were absent in the major truncated forms; the first 3-5 amino acids were also absent in a small proportion of the purified proteins.
8344280	5	32	from	proportion	776:785	arg1	absent					758:763	absent	758:763	absent	758:763	Alanine and proline were absent in the major truncated forms; the first 3-5 amino acids were also absent in a small proportion of the purified proteins.
8344280	12	33	theme	secreted	2023:2030	arg1	proteins					2032:2039	secreted proteins	2023:2039	secreted proteins with complex oligosaccharide chains	2023:2075	No evidence was obtained for the presence of secreted proteins with complex oligosaccharide chains, irrespective of the cell-culture conditions used or the harvesting time, for infected cells with recombinant baculovirus constructs.
8344280	0	34	theme	baculovirus-infected	77:96	arg1	cells					103:107	baculovirus-infected Sf21 cells	77:107	baculovirus-infected Sf21 cells	77:107	Biosynthesis and secretion of human interleukin 2 glycoprotein variants from baculovirus-infected Sf21 cells.
8344280	9	35	theme	only	1277:1280	arg1	presence					1204:1211	the presence	1200:1211	the presence of either GalNAc or the disaccharide Gal(beta 1-3)GalNAc	1200:1268	Fast atom bombardment mass spectrometry, compositional analysis and methylation analysis, of the tryptic glycopeptide APTPPPK, revealed the presence of either GalNAc or the disaccharide Gal(beta 1-3)GalNAc as the only carbohydrate constituents attached exclusively to Thr in this peptide, in a specific ratio for each individual IL-2 mutant protein.
8344280	9	35	theme	only	1277:1280	arg1	constituents					1295:1306	the only carbohydrate constituents	1273:1306	the only carbohydrate constituents attached exclusively to Thr	1273:1334	Fast atom bombardment mass spectrometry, compositional analysis and methylation analysis, of the tryptic glycopeptide APTPPPK, revealed the presence of either GalNAc or the disaccharide Gal(beta 1-3)GalNAc as the only carbohydrate constituents attached exclusively to Thr in this peptide, in a specific ratio for each individual IL-2 mutant protein.
8344280	10	36	theme	Gal	1418:1420	arg1	GalNAc					1431:1436	The Gal(beta 1-3)GalNAc	1414:1436	The Gal(beta 1-3)GalNAc protein forms	1414:1450	The Gal(beta 1-3)GalNAc protein forms could be partially altered in vitro to mammalian-type glycoforms by porcine liver beta-galactoside alpha-2,3-sialyltransferase in the presence of CMP-N-acetylneuraminic acid.
8344280	9	37	theme	Fast	1064:1067	arg1	spectrometry					1091:1102	Fast atom bombardment mass spectrometry	1064:1102	Fast atom bombardment mass spectrometry	1064:1102	Fast atom bombardment mass spectrometry, compositional analysis and methylation analysis, of the tryptic glycopeptide APTPPPK, revealed the presence of either GalNAc or the disaccharide Gal(beta 1-3)GalNAc as the only carbohydrate constituents attached exclusively to Thr in this peptide, in a specific ratio for each individual IL-2 mutant protein.
8344280	10	38	theme	protein	1438:1444	arg1	forms					1446:1450	The Gal(beta 1-3)GalNAc protein forms	1414:1450	The Gal(beta 1-3)GalNAc protein forms	1414:1450	The Gal(beta 1-3)GalNAc protein forms could be partially altered in vitro to mammalian-type glycoforms by porcine liver beta-galactoside alpha-2,3-sialyltransferase in the presence of CMP-N-acetylneuraminic acid.
8344280	9	39	theme	bombardment	1074:1084	arg1	spectrometry					1091:1102	Fast atom bombardment mass spectrometry	1064:1102	Fast atom bombardment mass spectrometry	1064:1102	Fast atom bombardment mass spectrometry, compositional analysis and methylation analysis, of the tryptic glycopeptide APTPPPK, revealed the presence of either GalNAc or the disaccharide Gal(beta 1-3)GalNAc as the only carbohydrate constituents attached exclusively to Thr in this peptide, in a specific ratio for each individual IL-2 mutant protein.
8344280	3	40	theme	total	457:461	arg1	protein					480:486	the total recombinant IL-2 protein	453:486	the total recombinant IL-2 protein synthesized by Sf21 cells	453:512	Only approximately 25% of the total recombinant IL-2 protein synthesized by Sf21 cells was secreted into the culture medium.
8344280	8	41	theme	variant	1049:1055	arg1	forms					1057:1061	unglycosylated and O-glycosylated variant forms	1015:1061	unglycosylated and O-glycosylated variant forms	1015:1061	, to the C-terminus or between positions 80 and 81 of the IL-2 polypeptide chain, resulted in the secretion of unglycosylated and O-glycosylated variant forms.
8344280	12	42	theme	recombinant	2175:2185	arg1	constructs					2199:2208	recombinant baculovirus constructs	2175:2208	recombinant baculovirus constructs	2175:2208	No evidence was obtained for the presence of secreted proteins with complex oligosaccharide chains, irrespective of the cell-culture conditions used or the harvesting time, for infected cells with recombinant baculovirus constructs.
8344280	2	43	theme	baculovirus	406:416	arg1	vectors					418:424	recombinant baculovirus vectors	394:424	recombinant baculovirus vectors	394:424	Human interleukin 2 (IL-2) and human IL-2 mutant proteins, with artificially introduced N-glycosylation or O-glycosylation sites, have been expressed in a lepidopteran cell line (Sf21, Spodoptera frugiperda) using recombinant baculovirus vectors.
8344280	5	44	theme	purified	794:801	arg1	proteins					803:810	the purified proteins	790:810	the purified proteins	790:810	Alanine and proline were absent in the major truncated forms; the first 3-5 amino acids were also absent in a small proportion of the purified proteins.
8344280	11	45	from	peptide	1670:1676	arg1	position					1706:1713	position 4	1706:1715	position 4	1706:1715	An IL-2 mutant form, with an 11-amino-acid peptide of human interferon-beta at position 4, which includes its only N-glycosylation site, had exclusively truncated proximally fucosylated oligomannosidic glycans; Man3GlcNAc[Fuc(alpha 1-6)]GlcNAc or Man2GlcNAc[Fuc(alpha 1-6)]GlcNAc structures, in a ratio of 3:1, were detected in the secreted proteins.
8344280	9	46	theme	compositional	1105:1117	arg1	analysis					1119:1126	compositional analysis	1105:1126	compositional analysis	1105:1126	Fast atom bombardment mass spectrometry, compositional analysis and methylation analysis, of the tryptic glycopeptide APTPPPK, revealed the presence of either GalNAc or the disaccharide Gal(beta 1-3)GalNAc as the only carbohydrate constituents attached exclusively to Thr in this peptide, in a specific ratio for each individual IL-2 mutant protein.
8344280	6	47	theme	sequences	878:886	arg1	introduction					817:828	The introduction	813:828	The introduction of potential artificial O-glycosylation peptide sequences (	813:888	The introduction of potential artificial O-glycosylation peptide sequences (.
8344280	3	48	theme	IL-2	475:478	arg1	protein					480:486	the total recombinant IL-2 protein	453:486	the total recombinant IL-2 protein synthesized by Sf21 cells	453:512	Only approximately 25% of the total recombinant IL-2 protein synthesized by Sf21 cells was secreted into the culture medium.
8344280	0	49	theme	human	30:34	arg1	variants					63:70	human interleukin 2 glycoprotein variants	30:70	human interleukin 2 glycoprotein variants	30:70	Biosynthesis and secretion of human interleukin 2 glycoprotein variants from baculovirus-infected Sf21 cells.
8344280	5	50	theme	small	770:774	arg1	proportion					776:785	a small proportion	768:785	a small proportion of the purified proteins	768:810	Alanine and proline were absent in the major truncated forms; the first 3-5 amino acids were also absent in a small proportion of the purified proteins.
8344280	6	51	theme	O-glycosylation	854:868	arg1	sequences					878:886	potential artificial O-glycosylation peptide sequences	833:886	potential artificial O-glycosylation peptide sequences	833:886	The introduction of potential artificial O-glycosylation peptide sequences (.
8344280	11	52	theme	interferon-beta	1687:1701	arg1	peptide					1670:1676	an 11-amino-acid peptide	1653:1676	an 11-amino-acid peptide of human interferon-beta at position 4	1653:1715	An IL-2 mutant form, with an 11-amino-acid peptide of human interferon-beta at position 4, which includes its only N-glycosylation site, had exclusively truncated proximally fucosylated oligomannosidic glycans; Man3GlcNAc[Fuc(alpha 1-6)]GlcNAc or Man2GlcNAc[Fuc(alpha 1-6)]GlcNAc structures, in a ratio of 3:1, were detected in the secreted proteins.
8344280	6	53	theme	potential	833:841	arg1	sequences					878:886	potential artificial O-glycosylation peptide sequences	833:886	potential artificial O-glycosylation peptide sequences	833:886	The introduction of potential artificial O-glycosylation peptide sequences (.
8344280	4	54	theme	N-terminal	564:573	arg1	truncations					575:585	Significant N-terminal truncations	552:585	Significant N-terminal truncations	552:585	Significant N-terminal truncations were detected in the secreted polypeptides (up to 85% of the molecules).
8344280	2	55	theme	mutant	222:227	arg1	proteins					229:236	Human interleukin 2 (IL-2) and human IL-2 mutant proteins	180:236	Human interleukin 2 (IL-2) and human IL-2 mutant proteins	180:236	Human interleukin 2 (IL-2) and human IL-2 mutant proteins, with artificially introduced N-glycosylation or O-glycosylation sites, have been expressed in a lepidopteran cell line (Sf21, Spodoptera frugiperda) using recombinant baculovirus vectors.
8344280	3	56	theme	Sf21	503:506	arg1	cells					508:512	Sf21 cells	503:512	Sf21 cells	503:512	Only approximately 25% of the total recombinant IL-2 protein synthesized by Sf21 cells was secreted into the culture medium.
8344280	10	57	theme	porcine	1520:1526	arg1	alpha-2,3-sialyltransferase					1551:1577	porcine liver beta-galactoside alpha-2,3-sialyltransferase	1520:1577	porcine liver beta-galactoside alpha-2,3-sialyltransferase	1520:1577	The Gal(beta 1-3)GalNAc protein forms could be partially altered in vitro to mammalian-type glycoforms by porcine liver beta-galactoside alpha-2,3-sialyltransferase in the presence of CMP-N-acetylneuraminic acid.
8344280	2	58	theme	human	211:215	arg1	IL-2					217:220	human IL-2	211:220	human IL-2	211:220	Human interleukin 2 (IL-2) and human IL-2 mutant proteins, with artificially introduced N-glycosylation or O-glycosylation sites, have been expressed in a lepidopteran cell line (Sf21, Spodoptera frugiperda) using recombinant baculovirus vectors.
8344280	11	59	gly	fucosylated	1801:1811	arg1	glycans					1829:1835	truncated proximally fucosylated oligomannosidic glycans	1780:1835	truncated proximally fucosylated oligomannosidic glycans	1780:1835	An IL-2 mutant form, with an 11-amino-acid peptide of human interferon-beta at position 4, which includes its only N-glycosylation site, had exclusively truncated proximally fucosylated oligomannosidic glycans; Man3GlcNAc[Fuc(alpha 1-6)]GlcNAc or Man2GlcNAc[Fuc(alpha 1-6)]GlcNAc structures, in a ratio of 3:1, were detected in the secreted proteins.
8344280	9	60	theme	tryptic	1161:1167	arg1	APTPPPK					1182:1188	the tryptic glycopeptide APTPPPK	1157:1188	the tryptic glycopeptide APTPPPK	1157:1188	Fast atom bombardment mass spectrometry, compositional analysis and methylation analysis, of the tryptic glycopeptide APTPPPK, revealed the presence of either GalNAc or the disaccharide Gal(beta 1-3)GalNAc as the only carbohydrate constituents attached exclusively to Thr in this peptide, in a specific ratio for each individual IL-2 mutant protein.
8344280	3	61	theme	culture	536:542	arg1	medium					544:549	the culture medium	532:549	the culture medium	532:549	Only approximately 25% of the total recombinant IL-2 protein synthesized by Sf21 cells was secreted into the culture medium.
8344280	5	62	from	absent	685:690	arg1	forms					715:719	the major truncated forms	695:719	the major truncated forms; the first 3-5 amino acids were also absent in a small proportion of the purified proteins	695:810	Alanine and proline were absent in the major truncated forms; the first 3-5 amino acids were also absent in a small proportion of the purified proteins.
8344280	0	63	gly	glycoprotein	50:61	arg1	glycoprotein					50:61	human interleukin 2 glycoprotein variants	30:70	human interleukin 2 glycoprotein variants	30:70	Biosynthesis and secretion of human interleukin 2 glycoprotein variants from baculovirus-infected Sf21 cells.
8344280	10	64	theme	CMP-N-acetylneuraminic	1598:1619	arg1	acid					1621:1624	CMP-N-acetylneuraminic acid	1598:1624	CMP-N-acetylneuraminic acid	1598:1624	The Gal(beta 1-3)GalNAc protein forms could be partially altered in vitro to mammalian-type glycoforms by porcine liver beta-galactoside alpha-2,3-sialyltransferase in the presence of CMP-N-acetylneuraminic acid.
8344280	11	65	located	detected	1943:1950	arg1	proteins					1968:1975	the secreted proteins	1955:1975	the secreted proteins	1955:1975	An IL-2 mutant form, with an 11-amino-acid peptide of human interferon-beta at position 4, which includes its only N-glycosylation site, had exclusively truncated proximally fucosylated oligomannosidic glycans; Man3GlcNAc[Fuc(alpha 1-6)]GlcNAc or Man2GlcNAc[Fuc(alpha 1-6)]GlcNAc structures, in a ratio of 3:1, were detected in the secreted proteins.
8344280	11	65	located	detected	1943:1950	arg2	structures					1907:1916	Man3GlcNAc[Fuc(alpha 1-6)]GlcNAc or Man2GlcNAc[Fuc(alpha 1-6)]GlcNAc structures	1838:1916	Man3GlcNAc[Fuc(alpha 1-6)]GlcNAc or Man2GlcNAc[Fuc(alpha 1-6)]GlcNAc structures	1838:1916	An IL-2 mutant form, with an 11-amino-acid peptide of human interferon-beta at position 4, which includes its only N-glycosylation site, had exclusively truncated proximally fucosylated oligomannosidic glycans; Man3GlcNAc[Fuc(alpha 1-6)]GlcNAc or Man2GlcNAc[Fuc(alpha 1-6)]GlcNAc structures, in a ratio of 3:1, were detected in the secreted proteins.
8344280	9	66	theme	APTPPPK	1182:1188	arg1	spectrometry					1091:1102	Fast atom bombardment mass spectrometry	1064:1102	Fast atom bombardment mass spectrometry	1064:1102	Fast atom bombardment mass spectrometry, compositional analysis and methylation analysis, of the tryptic glycopeptide APTPPPK, revealed the presence of either GalNAc or the disaccharide Gal(beta 1-3)GalNAc as the only carbohydrate constituents attached exclusively to Thr in this peptide, in a specific ratio for each individual IL-2 mutant protein.
8344280	9	66	theme	APTPPPK	1182:1188	arg1	analysis					1119:1126	compositional analysis	1105:1126	compositional analysis	1105:1126	Fast atom bombardment mass spectrometry, compositional analysis and methylation analysis, of the tryptic glycopeptide APTPPPK, revealed the presence of either GalNAc or the disaccharide Gal(beta 1-3)GalNAc as the only carbohydrate constituents attached exclusively to Thr in this peptide, in a specific ratio for each individual IL-2 mutant protein.
8344280	9	66	theme	APTPPPK	1182:1188	arg1	analysis					1144:1151	methylation analysis	1132:1151	methylation analysis	1132:1151	Fast atom bombardment mass spectrometry, compositional analysis and methylation analysis, of the tryptic glycopeptide APTPPPK, revealed the presence of either GalNAc or the disaccharide Gal(beta 1-3)GalNAc as the only carbohydrate constituents attached exclusively to Thr in this peptide, in a specific ratio for each individual IL-2 mutant protein.
8344280	11	67	with	form	1642:1645	arg1	peptide					1670:1676	an 11-amino-acid peptide	1653:1676	an 11-amino-acid peptide of human interferon-beta at position 4	1653:1715	An IL-2 mutant form, with an 11-amino-acid peptide of human interferon-beta at position 4, which includes its only N-glycosylation site, had exclusively truncated proximally fucosylated oligomannosidic glycans; Man3GlcNAc[Fuc(alpha 1-6)]GlcNAc or Man2GlcNAc[Fuc(alpha 1-6)]GlcNAc structures, in a ratio of 3:1, were detected in the secreted proteins.
8344280	9	68	theme	IL-2	1393:1396	arg1	protein					1405:1411	each individual IL-2 mutant protein	1377:1411	each individual IL-2 mutant protein	1377:1411	Fast atom bombardment mass spectrometry, compositional analysis and methylation analysis, of the tryptic glycopeptide APTPPPK, revealed the presence of either GalNAc or the disaccharide Gal(beta 1-3)GalNAc as the only carbohydrate constituents attached exclusively to Thr in this peptide, in a specific ratio for each individual IL-2 mutant protein.
8344280	8	69	theme	polypeptide	967:977	arg1	chain					979:983	the IL-2 polypeptide chain	958:983	the IL-2 polypeptide chain	958:983	, to the C-terminus or between positions 80 and 81 of the IL-2 polypeptide chain, resulted in the secretion of unglycosylated and O-glycosylated variant forms.
8344280	4	70	theme	secreted	608:615	arg1	polypeptides					617:628	the secreted polypeptides	604:628	the secreted polypeptides (up to 85% of the molecules)	604:657	Significant N-terminal truncations were detected in the secreted polypeptides (up to 85% of the molecules).
8344280	10	71	theme	beta-galactoside	1534:1549	arg1	alpha-2,3-sialyltransferase					1551:1577	porcine liver beta-galactoside alpha-2,3-sialyltransferase	1520:1577	porcine liver beta-galactoside alpha-2,3-sialyltransferase	1520:1577	The Gal(beta 1-3)GalNAc protein forms could be partially altered in vitro to mammalian-type glycoforms by porcine liver beta-galactoside alpha-2,3-sialyltransferase in the presence of CMP-N-acetylneuraminic acid.
8344280	2	72	theme	interleukin	186:196	arg1	proteins					229:236	Human interleukin 2 (IL-2) and human IL-2 mutant proteins	180:236	Human interleukin 2 (IL-2) and human IL-2 mutant proteins	180:236	Human interleukin 2 (IL-2) and human IL-2 mutant proteins, with artificially introduced N-glycosylation or O-glycosylation sites, have been expressed in a lepidopteran cell line (Sf21, Spodoptera frugiperda) using recombinant baculovirus vectors.
8344280	12	73	with	proteins	2032:2039	arg1	chains					2070:2075	complex oligosaccharide chains	2046:2075	complex oligosaccharide chains	2046:2075	No evidence was obtained for the presence of secreted proteins with complex oligosaccharide chains, irrespective of the cell-culture conditions used or the harvesting time, for infected cells with recombinant baculovirus constructs.
8344280	11	74	theme	secreted	1959:1966	arg1	proteins					1968:1975	the secreted proteins	1955:1975	the secreted proteins	1955:1975	An IL-2 mutant form, with an 11-amino-acid peptide of human interferon-beta at position 4, which includes its only N-glycosylation site, had exclusively truncated proximally fucosylated oligomannosidic glycans; Man3GlcNAc[Fuc(alpha 1-6)]GlcNAc or Man2GlcNAc[Fuc(alpha 1-6)]GlcNAc structures, in a ratio of 3:1, were detected in the secreted proteins.
8344280	9	75	gly	glycopeptide	1169:1180	arg2	glycopeptide					1169:1180	the tryptic glycopeptide APTPPPK	1157:1188	the tryptic glycopeptide APTPPPK	1157:1188	Fast atom bombardment mass spectrometry, compositional analysis and methylation analysis, of the tryptic glycopeptide APTPPPK, revealed the presence of either GalNAc or the disaccharide Gal(beta 1-3)GalNAc as the only carbohydrate constituents attached exclusively to Thr in this peptide, in a specific ratio for each individual IL-2 mutant protein.
8344280	2	76	gly	O-glycosylation	287:301	arg2	sites					303:307	artificially introduced N-glycosylation or O-glycosylation sites	244:307	sites	303:307	Human interleukin 2 (IL-2) and human IL-2 mutant proteins, with artificially introduced N-glycosylation or O-glycosylation sites, have been expressed in a lepidopteran cell line (Sf21, Spodoptera frugiperda) using recombinant baculovirus vectors.
8344280	11	77	theme	11-amino-acid	1656:1668	arg1	peptide					1670:1676	an 11-amino-acid peptide	1653:1676	an 11-amino-acid peptide of human interferon-beta at position 4	1653:1715	An IL-2 mutant form, with an 11-amino-acid peptide of human interferon-beta at position 4, which includes its only N-glycosylation site, had exclusively truncated proximally fucosylated oligomannosidic glycans; Man3GlcNAc[Fuc(alpha 1-6)]GlcNAc or Man2GlcNAc[Fuc(alpha 1-6)]GlcNAc structures, in a ratio of 3:1, were detected in the secreted proteins.
8344280	2	78	theme	cell	348:351	arg1	line					353:356	a lepidopteran cell line	333:356	a lepidopteran cell line (Sf21, Spodoptera frugiperda) using recombinant baculovirus vectors	333:424	Human interleukin 2 (IL-2) and human IL-2 mutant proteins, with artificially introduced N-glycosylation or O-glycosylation sites, have been expressed in a lepidopteran cell line (Sf21, Spodoptera frugiperda) using recombinant baculovirus vectors.
8344280	2	79	gly	N-glycosylation	268:282	arg1	proteins					229:236	Human interleukin 2 (IL-2) and human IL-2 mutant proteins	180:236	Human interleukin 2 (IL-2) and human IL-2 mutant proteins	180:236	Human interleukin 2 (IL-2) and human IL-2 mutant proteins, with artificially introduced N-glycosylation or O-glycosylation sites, have been expressed in a lepidopteran cell line (Sf21, Spodoptera frugiperda) using recombinant baculovirus vectors.
8344280	5	80	theme	truncated	705:713	arg1	forms					715:719	the major truncated forms	695:719	the major truncated forms; the first 3-5 amino acids were also absent in a small proportion of the purified proteins	695:810	Alanine and proline were absent in the major truncated forms; the first 3-5 amino acids were also absent in a small proportion of the purified proteins.
8344280	11	81	theme	fucosylated	1801:1811	arg1	glycans					1829:1835	truncated proximally fucosylated oligomannosidic glycans	1780:1835	truncated proximally fucosylated oligomannosidic glycans	1780:1835	An IL-2 mutant form, with an 11-amino-acid peptide of human interferon-beta at position 4, which includes its only N-glycosylation site, had exclusively truncated proximally fucosylated oligomannosidic glycans; Man3GlcNAc[Fuc(alpha 1-6)]GlcNAc or Man2GlcNAc[Fuc(alpha 1-6)]GlcNAc structures, in a ratio of 3:1, were detected in the secreted proteins.
8344280	9	82	theme	disaccharide	1237:1248	arg1	beta					1254:1257	beta 1-3	1254:1261	beta 1-3	1254:1261	Fast atom bombardment mass spectrometry, compositional analysis and methylation analysis, of the tryptic glycopeptide APTPPPK, revealed the presence of either GalNAc or the disaccharide Gal(beta 1-3)GalNAc as the only carbohydrate constituents attached exclusively to Thr in this peptide, in a specific ratio for each individual IL-2 mutant protein.
8344280	9	82	theme	disaccharide	1237:1248	arg1	GalNAc					1263:1268	the disaccharide Gal(beta 1-3)GalNAc	1233:1268	the disaccharide Gal(beta 1-3)GalNAc	1233:1268	Fast atom bombardment mass spectrometry, compositional analysis and methylation analysis, of the tryptic glycopeptide APTPPPK, revealed the presence of either GalNAc or the disaccharide Gal(beta 1-3)GalNAc as the only carbohydrate constituents attached exclusively to Thr in this peptide, in a specific ratio for each individual IL-2 mutant protein.
8344280	2	83	theme	introduced	257:266	arg1	N-glycosylation					268:282	artificially introduced N-glycosylation or O-glycosylation sites	244:307	N-glycosylation	268:282	Human interleukin 2 (IL-2) and human IL-2 mutant proteins, with artificially introduced N-glycosylation or O-glycosylation sites, have been expressed in a lepidopteran cell line (Sf21, Spodoptera frugiperda) using recombinant baculovirus vectors.
8344280	11	84	from	structures	1907:1916	arg1	ratio					1924:1928	a ratio	1922:1928	a ratio of 3:1	1922:1935	An IL-2 mutant form, with an 11-amino-acid peptide of human interferon-beta at position 4, which includes its only N-glycosylation site, had exclusively truncated proximally fucosylated oligomannosidic glycans; Man3GlcNAc[Fuc(alpha 1-6)]GlcNAc or Man2GlcNAc[Fuc(alpha 1-6)]GlcNAc structures, in a ratio of 3:1, were detected in the secreted proteins.
8344280	1	85	theme	polypeptides	130:141	arg1	Characterization					110:125	Characterization	110:125	Characterization of polypeptides and posttranslational modifications.	110:178	Characterization of polypeptides and posttranslational modifications.
8344280	12	86	theme	proteins	2032:2039	arg1	presence					2011:2018	the presence	2007:2018	the presence of secreted proteins with complex oligosaccharide chains	2007:2075	No evidence was obtained for the presence of secreted proteins with complex oligosaccharide chains, irrespective of the cell-culture conditions used or the harvesting time, for infected cells with recombinant baculovirus constructs.
8344280	11	87	theme	Man3GlcNAc[Fuc	1838:1851	arg1	structures					1907:1916	Man3GlcNAc[Fuc(alpha 1-6)]GlcNAc or Man2GlcNAc[Fuc(alpha 1-6)]GlcNAc structures	1838:1916	Man3GlcNAc[Fuc(alpha 1-6)]GlcNAc or Man2GlcNAc[Fuc(alpha 1-6)]GlcNAc structures	1838:1916	An IL-2 mutant form, with an 11-amino-acid peptide of human interferon-beta at position 4, which includes its only N-glycosylation site, had exclusively truncated proximally fucosylated oligomannosidic glycans; Man3GlcNAc[Fuc(alpha 1-6)]GlcNAc or Man2GlcNAc[Fuc(alpha 1-6)]GlcNAc structures, in a ratio of 3:1, were detected in the secreted proteins.
8344280	1	88	theme	posttranslational	147:163	arg1	modifications					165:177	posttranslational modifications	147:177	posttranslational modifications	147:177	Characterization of polypeptides and posttranslational modifications.
8344280	12	89	theme	complex	2046:2052	arg1	chains					2070:2075	complex oligosaccharide chains	2046:2075	complex oligosaccharide chains	2046:2075	No evidence was obtained for the presence of secreted proteins with complex oligosaccharide chains, irrespective of the cell-culture conditions used or the harvesting time, for infected cells with recombinant baculovirus constructs.
8344280	9	90	theme	GalNAc	1263:1268	arg1	presence					1204:1211	the presence	1200:1211	the presence of either GalNAc or the disaccharide Gal(beta 1-3)GalNAc	1200:1268	Fast atom bombardment mass spectrometry, compositional analysis and methylation analysis, of the tryptic glycopeptide APTPPPK, revealed the presence of either GalNAc or the disaccharide Gal(beta 1-3)GalNAc as the only carbohydrate constituents attached exclusively to Thr in this peptide, in a specific ratio for each individual IL-2 mutant protein.
8344280	9	90	theme	GalNAc	1263:1268	arg1	constituents					1295:1306	the only carbohydrate constituents	1273:1306	the only carbohydrate constituents attached exclusively to Thr	1273:1334	Fast atom bombardment mass spectrometry, compositional analysis and methylation analysis, of the tryptic glycopeptide APTPPPK, revealed the presence of either GalNAc or the disaccharide Gal(beta 1-3)GalNAc as the only carbohydrate constituents attached exclusively to Thr in this peptide, in a specific ratio for each individual IL-2 mutant protein.
8344280	11	91	theme	only	1737:1740	arg1	site					1758:1761	its only N-glycosylation site	1733:1761	its only N-glycosylation site	1733:1761	An IL-2 mutant form, with an 11-amino-acid peptide of human interferon-beta at position 4, which includes its only N-glycosylation site, had exclusively truncated proximally fucosylated oligomannosidic glycans; Man3GlcNAc[Fuc(alpha 1-6)]GlcNAc or Man2GlcNAc[Fuc(alpha 1-6)]GlcNAc structures, in a ratio of 3:1, were detected in the secreted proteins.
8344280	0	92	theme	Sf21	98:101	arg1	cells					103:107	baculovirus-infected Sf21 cells	77:107	baculovirus-infected Sf21 cells	77:107	Biosynthesis and secretion of human interleukin 2 glycoprotein variants from baculovirus-infected Sf21 cells.
8344280	8	93	theme	unglycosylated	1015:1028	arg1	forms					1057:1061	unglycosylated and O-glycosylated variant forms	1015:1061	unglycosylated and O-glycosylated variant forms	1015:1061	, to the C-terminus or between positions 80 and 81 of the IL-2 polypeptide chain, resulted in the secretion of unglycosylated and O-glycosylated variant forms.
8344280	5	94	dep	forms	715:719	arg1	acids					742:746	the first 3-5 amino acids	722:746	the first 3-5 amino acids	722:746	Alanine and proline were absent in the major truncated forms; the first 3-5 amino acids were also absent in a small proportion of the purified proteins.
8344280	5	94	dep	forms	715:719	arg1	absent					758:763	absent	758:763	absent	758:763	Alanine and proline were absent in the major truncated forms; the first 3-5 amino acids were also absent in a small proportion of the purified proteins.
8344280	11	95	theme	truncated	1780:1788	arg1	glycans					1829:1835	truncated proximally fucosylated oligomannosidic glycans	1780:1835	truncated proximally fucosylated oligomannosidic glycans	1780:1835	An IL-2 mutant form, with an 11-amino-acid peptide of human interferon-beta at position 4, which includes its only N-glycosylation site, had exclusively truncated proximally fucosylated oligomannosidic glycans; Man3GlcNAc[Fuc(alpha 1-6)]GlcNAc or Man2GlcNAc[Fuc(alpha 1-6)]GlcNAc structures, in a ratio of 3:1, were detected in the secreted proteins.
8344280	5	96	theme	first	726:730	arg1	acids					742:746	the first 3-5 amino acids	722:746	the first 3-5 amino acids	722:746	Alanine and proline were absent in the major truncated forms; the first 3-5 amino acids were also absent in a small proportion of the purified proteins.
8344280	5	96	theme	first	726:730	arg1	absent					758:763	absent	758:763	absent	758:763	Alanine and proline were absent in the major truncated forms; the first 3-5 amino acids were also absent in a small proportion of the purified proteins.
8344280	9	97	theme	carbohydrate	1282:1293	arg1	presence					1204:1211	the presence	1200:1211	the presence of either GalNAc or the disaccharide Gal(beta 1-3)GalNAc	1200:1268	Fast atom bombardment mass spectrometry, compositional analysis and methylation analysis, of the tryptic glycopeptide APTPPPK, revealed the presence of either GalNAc or the disaccharide Gal(beta 1-3)GalNAc as the only carbohydrate constituents attached exclusively to Thr in this peptide, in a specific ratio for each individual IL-2 mutant protein.
8344280	9	97	theme	carbohydrate	1282:1293	arg1	constituents					1295:1306	the only carbohydrate constituents	1273:1306	the only carbohydrate constituents attached exclusively to Thr	1273:1334	Fast atom bombardment mass spectrometry, compositional analysis and methylation analysis, of the tryptic glycopeptide APTPPPK, revealed the presence of either GalNAc or the disaccharide Gal(beta 1-3)GalNAc as the only carbohydrate constituents attached exclusively to Thr in this peptide, in a specific ratio for each individual IL-2 mutant protein.
8344280	8	98	theme	O-glycosylated	1034:1047	arg1	forms					1057:1061	unglycosylated and O-glycosylated variant forms	1015:1061	unglycosylated and O-glycosylated variant forms	1015:1061	, to the C-terminus or between positions 80 and 81 of the IL-2 polypeptide chain, resulted in the secretion of unglycosylated and O-glycosylated variant forms.
8344280	4	99	located	detected	592:599	arg2	truncations					575:585	Significant N-terminal truncations	552:585	Significant N-terminal truncations	552:585	Significant N-terminal truncations were detected in the secreted polypeptides (up to 85% of the molecules).
8344280	4	99	located	detected	592:599	arg1	polypeptides					617:628	the secreted polypeptides	604:628	the secreted polypeptides (up to 85% of the molecules)	604:657	Significant N-terminal truncations were detected in the secreted polypeptides (up to 85% of the molecules).
8344280	9	100	theme	atom	1069:1072	arg1	spectrometry					1091:1102	Fast atom bombardment mass spectrometry	1064:1102	Fast atom bombardment mass spectrometry	1064:1102	Fast atom bombardment mass spectrometry, compositional analysis and methylation analysis, of the tryptic glycopeptide APTPPPK, revealed the presence of either GalNAc or the disaccharide Gal(beta 1-3)GalNAc as the only carbohydrate constituents attached exclusively to Thr in this peptide, in a specific ratio for each individual IL-2 mutant protein.
8344280	5	101	theme	amino	736:740	arg1	acids					742:746	the first 3-5 amino acids	722:746	the first 3-5 amino acids	722:746	Alanine and proline were absent in the major truncated forms; the first 3-5 amino acids were also absent in a small proportion of the purified proteins.
8344280	5	101	theme	amino	736:740	arg1	absent					758:763	absent	758:763	absent	758:763	Alanine and proline were absent in the major truncated forms; the first 3-5 amino acids were also absent in a small proportion of the purified proteins.
8344280	12	102	with	cells	2164:2168	arg1	constructs					2199:2208	recombinant baculovirus constructs	2175:2208	recombinant baculovirus constructs	2175:2208	No evidence was obtained for the presence of secreted proteins with complex oligosaccharide chains, irrespective of the cell-culture conditions used or the harvesting time, for infected cells with recombinant baculovirus constructs.
8344280	8	103	theme	forms	1057:1061	arg1	secretion					1002:1010	the secretion	998:1010	the secretion of unglycosylated and O-glycosylated variant forms	998:1061	, to the C-terminus or between positions 80 and 81 of the IL-2 polypeptide chain, resulted in the secretion of unglycosylated and O-glycosylated variant forms.
8344280	11	104	from	position	1706:1713	arg1	peptide					1670:1676	an 11-amino-acid peptide	1653:1676	an 11-amino-acid peptide of human interferon-beta at position 4	1653:1715	An IL-2 mutant form, with an 11-amino-acid peptide of human interferon-beta at position 4, which includes its only N-glycosylation site, had exclusively truncated proximally fucosylated oligomannosidic glycans; Man3GlcNAc[Fuc(alpha 1-6)]GlcNAc or Man2GlcNAc[Fuc(alpha 1-6)]GlcNAc structures, in a ratio of 3:1, were detected in the secreted proteins.
8344280	11	104	from	position	1706:1713	arg1	interferon-beta					1687:1701	human interferon-beta	1681:1701	human interferon-beta at position 4	1681:1715	An IL-2 mutant form, with an 11-amino-acid peptide of human interferon-beta at position 4, which includes its only N-glycosylation site, had exclusively truncated proximally fucosylated oligomannosidic glycans; Man3GlcNAc[Fuc(alpha 1-6)]GlcNAc or Man2GlcNAc[Fuc(alpha 1-6)]GlcNAc structures, in a ratio of 3:1, were detected in the secreted proteins.
8344280	10	105	theme	GalNAc	1431:1436	arg1	forms					1446:1450	The Gal(beta 1-3)GalNAc protein forms	1414:1450	The Gal(beta 1-3)GalNAc protein forms	1414:1450	The Gal(beta 1-3)GalNAc protein forms could be partially altered in vitro to mammalian-type glycoforms by porcine liver beta-galactoside alpha-2,3-sialyltransferase in the presence of CMP-N-acetylneuraminic acid.
8344280	9	106	theme	mass	1086:1089	arg1	spectrometry					1091:1102	Fast atom bombardment mass spectrometry	1064:1102	Fast atom bombardment mass spectrometry	1064:1102	Fast atom bombardment mass spectrometry, compositional analysis and methylation analysis, of the tryptic glycopeptide APTPPPK, revealed the presence of either GalNAc or the disaccharide Gal(beta 1-3)GalNAc as the only carbohydrate constituents attached exclusively to Thr in this peptide, in a specific ratio for each individual IL-2 mutant protein.
8344280	3	107	theme	recombinant	463:473	arg1	protein					480:486	the total recombinant IL-2 protein	453:486	the total recombinant IL-2 protein synthesized by Sf21 cells	453:512	Only approximately 25% of the total recombinant IL-2 protein synthesized by Sf21 cells was secreted into the culture medium.
8344280	11	108	dep	alpha	1853:1857	arg1	Man2GlcNAc[Fuc					1874:1887	Man2GlcNAc[Fuc	1874:1887	Man2GlcNAc[Fuc	1874:1887	An IL-2 mutant form, with an 11-amino-acid peptide of human interferon-beta at position 4, which includes its only N-glycosylation site, had exclusively truncated proximally fucosylated oligomannosidic glycans; Man3GlcNAc[Fuc(alpha 1-6)]GlcNAc or Man2GlcNAc[Fuc(alpha 1-6)]GlcNAc structures, in a ratio of 3:1, were detected in the secreted proteins.
8344280	11	108	dep	alpha	1853:1857	arg1	1-6					1859:1861	1-6	1859:1861	1-6	1859:1861	An IL-2 mutant form, with an 11-amino-acid peptide of human interferon-beta at position 4, which includes its only N-glycosylation site, had exclusively truncated proximally fucosylated oligomannosidic glycans; Man3GlcNAc[Fuc(alpha 1-6)]GlcNAc or Man2GlcNAc[Fuc(alpha 1-6)]GlcNAc structures, in a ratio of 3:1, were detected in the secreted proteins.
8344280	11	108	dep	alpha	1853:1857	arg1	GlcNAc					1864:1869	GlcNAc	1864:1869	GlcNAc	1864:1869	An IL-2 mutant form, with an 11-amino-acid peptide of human interferon-beta at position 4, which includes its only N-glycosylation site, had exclusively truncated proximally fucosylated oligomannosidic glycans; Man3GlcNAc[Fuc(alpha 1-6)]GlcNAc or Man2GlcNAc[Fuc(alpha 1-6)]GlcNAc structures, in a ratio of 3:1, were detected in the secreted proteins.
8344280	2	109	dep	line	353:356	arg1	Sf21					359:362	Sf21	359:362	Sf21	359:362	Human interleukin 2 (IL-2) and human IL-2 mutant proteins, with artificially introduced N-glycosylation or O-glycosylation sites, have been expressed in a lepidopteran cell line (Sf21, Spodoptera frugiperda) using recombinant baculovirus vectors.
8344280	2	109	dep	line	353:356	arg1	frugiperda					376:385	Spodoptera frugiperda	365:385	Spodoptera frugiperda	365:385	Human interleukin 2 (IL-2) and human IL-2 mutant proteins, with artificially introduced N-glycosylation or O-glycosylation sites, have been expressed in a lepidopteran cell line (Sf21, Spodoptera frugiperda) using recombinant baculovirus vectors.
8344280	9	110	attach	attached	1308:1315	arg1	Thr					1332:1334	Thr	1332:1334	Thr	1332:1334	Fast atom bombardment mass spectrometry, compositional analysis and methylation analysis, of the tryptic glycopeptide APTPPPK, revealed the presence of either GalNAc or the disaccharide Gal(beta 1-3)GalNAc as the only carbohydrate constituents attached exclusively to Thr in this peptide, in a specific ratio for each individual IL-2 mutant protein.
8344280	9	110	attach	attached	1308:1315	arg2	presence					1204:1211	the presence	1200:1211	the presence of either GalNAc or the disaccharide Gal(beta 1-3)GalNAc	1200:1268	Fast atom bombardment mass spectrometry, compositional analysis and methylation analysis, of the tryptic glycopeptide APTPPPK, revealed the presence of either GalNAc or the disaccharide Gal(beta 1-3)GalNAc as the only carbohydrate constituents attached exclusively to Thr in this peptide, in a specific ratio for each individual IL-2 mutant protein.
8344280	9	110	attach	attached	1308:1315	arg2	constituents					1295:1306	the only carbohydrate constituents	1273:1306	the only carbohydrate constituents attached exclusively to Thr	1273:1334	Fast atom bombardment mass spectrometry, compositional analysis and methylation analysis, of the tryptic glycopeptide APTPPPK, revealed the presence of either GalNAc or the disaccharide Gal(beta 1-3)GalNAc as the only carbohydrate constituents attached exclusively to Thr in this peptide, in a specific ratio for each individual IL-2 mutant protein.
8344280	2	111	theme	recombinant	394:404	arg1	vectors					418:424	recombinant baculovirus vectors	394:424	recombinant baculovirus vectors	394:424	Human interleukin 2 (IL-2) and human IL-2 mutant proteins, with artificially introduced N-glycosylation or O-glycosylation sites, have been expressed in a lepidopteran cell line (Sf21, Spodoptera frugiperda) using recombinant baculovirus vectors.
8344280	5	112	theme	proteins	803:810	arg1	proportion					776:785	a small proportion	768:785	a small proportion of the purified proteins	768:810	Alanine and proline were absent in the major truncated forms; the first 3-5 amino acids were also absent in a small proportion of the purified proteins.
8344280	11	113	theme	3:1	1933:1935	arg1	ratio					1924:1928	a ratio	1922:1928	a ratio of 3:1	1922:1935	An IL-2 mutant form, with an 11-amino-acid peptide of human interferon-beta at position 4, which includes its only N-glycosylation site, had exclusively truncated proximally fucosylated oligomannosidic glycans; Man3GlcNAc[Fuc(alpha 1-6)]GlcNAc or Man2GlcNAc[Fuc(alpha 1-6)]GlcNAc structures, in a ratio of 3:1, were detected in the secreted proteins.
8344280	11	114	theme	IL-2	1630:1633	arg1	form					1642:1645	An IL-2 mutant form	1627:1645	An IL-2 mutant form	1627:1645	An IL-2 mutant form, with an 11-amino-acid peptide of human interferon-beta at position 4, which includes its only N-glycosylation site, had exclusively truncated proximally fucosylated oligomannosidic glycans; Man3GlcNAc[Fuc(alpha 1-6)]GlcNAc or Man2GlcNAc[Fuc(alpha 1-6)]GlcNAc structures, in a ratio of 3:1, were detected in the secreted proteins.
8344280	12	115	theme	baculovirus	2187:2197	arg1	constructs					2199:2208	recombinant baculovirus constructs	2175:2208	recombinant baculovirus constructs	2175:2208	No evidence was obtained for the presence of secreted proteins with complex oligosaccharide chains, irrespective of the cell-culture conditions used or the harvesting time, for infected cells with recombinant baculovirus constructs.
8344280	0	116	theme	interleukin	36:46	arg1	variants					63:70	human interleukin 2 glycoprotein variants	30:70	human interleukin 2 glycoprotein variants	30:70	Biosynthesis and secretion of human interleukin 2 glycoprotein variants from baculovirus-infected Sf21 cells.
8344280	6	117	theme	peptide	870:876	arg1	sequences					878:886	potential artificial O-glycosylation peptide sequences	833:886	potential artificial O-glycosylation peptide sequences	833:886	The introduction of potential artificial O-glycosylation peptide sequences (.
8344280	4	118	theme	Significant	552:562	arg1	truncations					575:585	Significant N-terminal truncations	552:585	Significant N-terminal truncations	552:585	Significant N-terminal truncations were detected in the secreted polypeptides (up to 85% of the molecules).
8344280	11	119	theme	human	1681:1685	arg1	interferon-beta					1687:1701	human interferon-beta	1681:1701	human interferon-beta at position 4	1681:1715	An IL-2 mutant form, with an 11-amino-acid peptide of human interferon-beta at position 4, which includes its only N-glycosylation site, had exclusively truncated proximally fucosylated oligomannosidic glycans; Man3GlcNAc[Fuc(alpha 1-6)]GlcNAc or Man2GlcNAc[Fuc(alpha 1-6)]GlcNAc structures, in a ratio of 3:1, were detected in the secreted proteins.
8344280	9	120	theme	methylation	1132:1142	arg1	analysis					1144:1151	methylation analysis	1132:1151	methylation analysis	1132:1151	Fast atom bombardment mass spectrometry, compositional analysis and methylation analysis, of the tryptic glycopeptide APTPPPK, revealed the presence of either GalNAc or the disaccharide Gal(beta 1-3)GalNAc as the only carbohydrate constituents attached exclusively to Thr in this peptide, in a specific ratio for each individual IL-2 mutant protein.
8344280	3	121	theme	protein	480:486	arg1	protein					480:486	the total recombinant IL-2 protein	453:486	the total recombinant IL-2 protein synthesized by Sf21 cells	453:512	Only approximately 25% of the total recombinant IL-2 protein synthesized by Sf21 cells was secreted into the culture medium.
8344280	3	121	theme	protein	480:486	arg1	%					448:448	Only approximately 25%	427:448	Only approximately 25% of the total recombinant IL-2 protein synthesized by Sf21 cells	427:512	Only approximately 25% of the total recombinant IL-2 protein synthesized by Sf21 cells was secreted into the culture medium.
8344280	0	122	theme	glycoprotein	50:61	arg1	variants					63:70	human interleukin 2 glycoprotein variants	30:70	human interleukin 2 glycoprotein variants	30:70	Biosynthesis and secretion of human interleukin 2 glycoprotein variants from baculovirus-infected Sf21 cells.
8344280	6	123	theme	artificial	843:852	arg1	sequences					878:886	potential artificial O-glycosylation peptide sequences	833:886	potential artificial O-glycosylation peptide sequences	833:886	The introduction of potential artificial O-glycosylation peptide sequences (.
8344280	12	124	theme	infected	2155:2162	arg1	cells					2164:2168	infected cells	2155:2168	infected cells with recombinant baculovirus constructs	2155:2208	No evidence was obtained for the presence of secreted proteins with complex oligosaccharide chains, irrespective of the cell-culture conditions used or the harvesting time, for infected cells with recombinant baculovirus constructs.
8344280	4	125	dep	polypeptides	617:628	arg1	%					639:639	up to 85%	631:639	up to 85% of the molecules	631:656	Significant N-terminal truncations were detected in the secreted polypeptides (up to 85% of the molecules).
8344280	4	125	dep	polypeptides	617:628	arg1	molecules					648:656	the molecules	644:656	the molecules	644:656	Significant N-terminal truncations were detected in the secreted polypeptides (up to 85% of the molecules).
8344280	9	126	theme	specific	1358:1365	arg1	ratio					1367:1371	a specific ratio	1356:1371	a specific ratio for each individual IL-2 mutant protein	1356:1411	Fast atom bombardment mass spectrometry, compositional analysis and methylation analysis, of the tryptic glycopeptide APTPPPK, revealed the presence of either GalNAc or the disaccharide Gal(beta 1-3)GalNAc as the only carbohydrate constituents attached exclusively to Thr in this peptide, in a specific ratio for each individual IL-2 mutant protein.
8344280	2	127	theme	IL-2	217:220	arg1	proteins					229:236	Human interleukin 2 (IL-2) and human IL-2 mutant proteins	180:236	Human interleukin 2 (IL-2) and human IL-2 mutant proteins	180:236	Human interleukin 2 (IL-2) and human IL-2 mutant proteins, with artificially introduced N-glycosylation or O-glycosylation sites, have been expressed in a lepidopteran cell line (Sf21, Spodoptera frugiperda) using recombinant baculovirus vectors.
8344280	11	128	theme	GlcNAc	1900:1905	arg1	structures					1907:1916	Man3GlcNAc[Fuc(alpha 1-6)]GlcNAc or Man2GlcNAc[Fuc(alpha 1-6)]GlcNAc structures	1838:1916	Man3GlcNAc[Fuc(alpha 1-6)]GlcNAc or Man2GlcNAc[Fuc(alpha 1-6)]GlcNAc structures	1838:1916	An IL-2 mutant form, with an 11-amino-acid peptide of human interferon-beta at position 4, which includes its only N-glycosylation site, had exclusively truncated proximally fucosylated oligomannosidic glycans; Man3GlcNAc[Fuc(alpha 1-6)]GlcNAc or Man2GlcNAc[Fuc(alpha 1-6)]GlcNAc structures, in a ratio of 3:1, were detected in the secreted proteins.
8344280	12	129	theme	harvesting	2134:2143	arg1	time					2145:2148	the harvesting time	2130:2148	the harvesting time	2130:2148	No evidence was obtained for the presence of secreted proteins with complex oligosaccharide chains, irrespective of the cell-culture conditions used or the harvesting time, for infected cells with recombinant baculovirus constructs.
8344280	9	130	theme	glycopeptide	1169:1180	arg1	APTPPPK					1182:1188	the tryptic glycopeptide APTPPPK	1157:1188	the tryptic glycopeptide APTPPPK	1157:1188	Fast atom bombardment mass spectrometry, compositional analysis and methylation analysis, of the tryptic glycopeptide APTPPPK, revealed the presence of either GalNAc or the disaccharide Gal(beta 1-3)GalNAc as the only carbohydrate constituents attached exclusively to Thr in this peptide, in a specific ratio for each individual IL-2 mutant protein.
8344280	9	131	theme	individual	1382:1391	arg1	protein					1405:1411	each individual IL-2 mutant protein	1377:1411	each individual IL-2 mutant protein	1377:1411	Fast atom bombardment mass spectrometry, compositional analysis and methylation analysis, of the tryptic glycopeptide APTPPPK, revealed the presence of either GalNAc or the disaccharide Gal(beta 1-3)GalNAc as the only carbohydrate constituents attached exclusively to Thr in this peptide, in a specific ratio for each individual IL-2 mutant protein.
10864452	6	0	with	agreement	691:699	arg1	that					706:709	that	706:709	that	706:709	The pattern of disulfide bridges is in agreement with that predicted from the X-ray crystallographic structure of canine myeloperoxidase (MPO) (Zeng, J., and Fenna, R. E. (1992) J. Mol.
10864452	1	1	from	status	187:192	arg1	peroxidase					214:223	human eosinophil peroxidase	197:223	human eosinophil peroxidase (EPO)	197:229	The determination by protein chemistry methods of the half-cystine status in human eosinophil peroxidase (EPO) is reported.
10864452	1	1	from	status	187:192	arg1	EPO					226:228	EPO	226:228	EPO	226:228	The determination by protein chemistry methods of the half-cystine status in human eosinophil peroxidase (EPO) is reported.
10864452	4	2	theme	disulfide	528:536	arg1	bridges					538:544	five intrachain disulfide bridges	512:544	five intrachain disulfide bridges in the heavy chain of EPO	512:570	Disulfide bridges connect Cys253 and Cys263, Cys257 and Cys287, Cys359 and Cys370, Cys570 and Cys635, and Cys676 and Cys701, forming five intrachain disulfide bridges in the heavy chain of EPO.
10864452	0	3	theme	residues	79:86	arg1	locations					40:48	locations	40:48	locations of N-glycosylated asparagine residues in human eosinophil peroxidase	40:117	The status of half-cystine residues and locations of N-glycosylated asparagine residues in human eosinophil peroxidase.
10864452	0	3	theme	residues	79:86	arg1	status					4:9	The status	0:9	The status of half-cystine residues	0:34	The status of half-cystine residues and locations of N-glycosylated asparagine residues in human eosinophil peroxidase.
10864452	0	4	from	status	4:9	arg1	peroxidase					108:117	human eosinophil peroxidase	91:117	human eosinophil peroxidase	91:117	The status of half-cystine residues and locations of N-glycosylated asparagine residues in human eosinophil peroxidase.
10864452	4	5	theme	intrachain	517:526	arg1	bridges					538:544	five intrachain disulfide bridges	512:544	five intrachain disulfide bridges in the heavy chain of EPO	512:570	Disulfide bridges connect Cys253 and Cys263, Cys257 and Cys287, Cys359 and Cys370, Cys570 and Cys635, and Cys676 and Cys701, forming five intrachain disulfide bridges in the heavy chain of EPO.
10864452	0	6	theme	eosinophil	97:106	arg1	peroxidase					108:117	human eosinophil peroxidase	91:117	human eosinophil peroxidase	91:117	The status of half-cystine residues and locations of N-glycosylated asparagine residues in human eosinophil peroxidase.
10864452	6	7	theme	crystallographic	736:751	arg1	structure					753:761	the X-ray crystallographic structure	726:761	the X-ray crystallographic structure of canine myeloperoxidase (MPO) (Zeng, J., and Fenna, R. E. (1992) J. Mol	726:835	The pattern of disulfide bridges is in agreement with that predicted from the X-ray crystallographic structure of canine myeloperoxidase (MPO) (Zeng, J., and Fenna, R. E. (1992) J. Mol.
10864452	0	8	gly	N-glycosylated	53:66	arg1	residues					79:86	N-glycosylated asparagine residues	53:86	N-glycosylated asparagine residues in human eosinophil peroxidase	53:117	The status of half-cystine residues and locations of N-glycosylated asparagine residues in human eosinophil peroxidase.
10864452	10	9	from	discrepancy	1158:1168	arg1	literature					1177:1186	the literature	1173:1186	the literature regarding the sequence of residues 645-659	1173:1229	Furthermore, a discrepancy in the literature regarding the sequence of residues 645-659 is resolved.
10864452	0	10	theme	human	91:95	arg1	peroxidase					108:117	human eosinophil peroxidase	91:117	human eosinophil peroxidase	91:117	The status of half-cystine residues and locations of N-glycosylated asparagine residues in human eosinophil peroxidase.
10864452	6	11	theme	X-ray	730:734	arg1	structure					753:761	the X-ray crystallographic structure	726:761	the X-ray crystallographic structure of canine myeloperoxidase (MPO) (Zeng, J., and Fenna, R. E. (1992) J. Mol	726:835	The pattern of disulfide bridges is in agreement with that predicted from the X-ray crystallographic structure of canine myeloperoxidase (MPO) (Zeng, J., and Fenna, R. E. (1992) J. Mol.
10864452	0	12	from	locations	40:48	arg1	peroxidase					108:117	human eosinophil peroxidase	91:117	human eosinophil peroxidase	91:117	The status of half-cystine residues and locations of N-glycosylated asparagine residues in human eosinophil peroxidase.
10864452	8	13	theme	peroxidases	899:909	arg1	class					880:884	the class	876:884	the class of mammalian peroxidases, including EPO, MPO, lactoperoxidase (LPO), and thyroid peroxidase (TPO)	876:982	226, 185-207) to be general for the class of mammalian peroxidases, including EPO, MPO, lactoperoxidase (LPO), and thyroid peroxidase (TPO).
10864452	1	14	from	methods	159:165	arg1	peroxidase					214:223	human eosinophil peroxidase	197:223	human eosinophil peroxidase (EPO)	197:229	The determination by protein chemistry methods of the half-cystine status in human eosinophil peroxidase (EPO) is reported.
10864452	1	14	from	methods	159:165	arg1	EPO					226:228	EPO	226:228	EPO	226:228	The determination by protein chemistry methods of the half-cystine status in human eosinophil peroxidase (EPO) is reported.
10864452	1	15	theme	half-cystine	174:185	arg1	status					187:192	the half-cystine status	170:192	the half-cystine status in human eosinophil peroxidase (EPO)	170:229	The determination by protein chemistry methods of the half-cystine status in human eosinophil peroxidase (EPO) is reported.
10864452	3	16	theme	intrachain	334:343	arg1	bridge					345:350	an intrachain bridge	331:350	an intrachain bridge	331:350	Cys141 and Cys152 form an intrachain bridge in the light chain of EPO.
10864452	8	17	theme	mammalian	889:897	arg1	MPO					927:929	MPO	927:929	MPO	927:929	226, 185-207) to be general for the class of mammalian peroxidases, including EPO, MPO, lactoperoxidase (LPO), and thyroid peroxidase (TPO).
10864452	8	17	theme	mammalian	889:897	arg1	peroxidases					899:909	mammalian peroxidases	889:909	mammalian peroxidases	889:909	226, 185-207) to be general for the class of mammalian peroxidases, including EPO, MPO, lactoperoxidase (LPO), and thyroid peroxidase (TPO).
10864452	8	17	theme	mammalian	889:897	arg1	EPO					922:924	EPO	922:924	EPO	922:924	226, 185-207) to be general for the class of mammalian peroxidases, including EPO, MPO, lactoperoxidase (LPO), and thyroid peroxidase (TPO).
10864452	8	17	theme	mammalian	889:897	arg1	peroxidase					967:976	thyroid peroxidase	959:976	thyroid peroxidase (TPO)	959:982	226, 185-207) to be general for the class of mammalian peroxidases, including EPO, MPO, lactoperoxidase (LPO), and thyroid peroxidase (TPO).
10864452	8	17	theme	mammalian	889:897	arg1	lactoperoxidase					932:946	lactoperoxidase	932:946	lactoperoxidase (LPO)	932:952	226, 185-207) to be general for the class of mammalian peroxidases, including EPO, MPO, lactoperoxidase (LPO), and thyroid peroxidase (TPO).
10864452	9	18	theme	glucosamine-based	1034:1050	arg1	carbohydrate					1052:1063	glucosamine-based carbohydrate	1034:1063	glucosamine-based carbohydrate	1034:1063	Of four candidate sites in EPO for attachment of glucosamine-based carbohydrate, Asn327 and Asn363 are occupied, whereas Asn700 and Asn708 are unsubstituted.
10864452	1	19	theme	status	187:192	arg1	methods					159:165	protein chemistry methods	141:165	protein chemistry methods of the half-cystine status in human eosinophil peroxidase (EPO)	141:229	The determination by protein chemistry methods of the half-cystine status in human eosinophil peroxidase (EPO) is reported.
10864452	8	20	theme	thyroid	959:965	arg1	TPO					979:981	TPO	979:981	TPO	979:981	226, 185-207) to be general for the class of mammalian peroxidases, including EPO, MPO, lactoperoxidase (LPO), and thyroid peroxidase (TPO).
10864452	8	20	theme	thyroid	959:965	arg1	EPO					922:924	EPO	922:924	EPO	922:924	226, 185-207) to be general for the class of mammalian peroxidases, including EPO, MPO, lactoperoxidase (LPO), and thyroid peroxidase (TPO).
10864452	8	20	theme	thyroid	959:965	arg1	peroxidase					967:976	thyroid peroxidase	959:976	thyroid peroxidase (TPO)	959:982	226, 185-207) to be general for the class of mammalian peroxidases, including EPO, MPO, lactoperoxidase (LPO), and thyroid peroxidase (TPO).
10864452	8	20	theme	thyroid	959:965	arg1	peroxidases					899:909	mammalian peroxidases	889:909	mammalian peroxidases	889:909	226, 185-207) to be general for the class of mammalian peroxidases, including EPO, MPO, lactoperoxidase (LPO), and thyroid peroxidase (TPO).
10864452	2	21	contain	has	267:269	arg1	EPO					244:246	EPO	244:246	EPO	244:246	EPO is two-chained and has a total of 14 half-cystine residues.
10864452	2	21	contain	has	267:269	arg2	total					273:277	a total	271:277	a total of 14 half-cystine residues	271:305	EPO is two-chained and has a total of 14 half-cystine residues.
10864452	9	22	used	occupied	1088:1095	arg2	Asn363					1077:1082	Asn363	1077:1082	Asn363	1077:1082	Of four candidate sites in EPO for attachment of glucosamine-based carbohydrate, Asn327 and Asn363 are occupied, whereas Asn700 and Asn708 are unsubstituted.
10864452	9	22	used	occupied	1088:1095	arg2	Asn327					1066:1071	Asn327	1066:1071	Asn327	1066:1071	Of four candidate sites in EPO for attachment of glucosamine-based carbohydrate, Asn327 and Asn363 are occupied, whereas Asn700 and Asn708 are unsubstituted.
10864452	2	23	theme	residues	298:305	arg1	total					273:277	a total	271:277	a total of 14 half-cystine residues	271:305	EPO is two-chained and has a total of 14 half-cystine residues.
10864452	1	24	theme	human	197:201	arg1	peroxidase					214:223	human eosinophil peroxidase	197:223	human eosinophil peroxidase (EPO)	197:229	The determination by protein chemistry methods of the half-cystine status in human eosinophil peroxidase (EPO) is reported.
10864452	1	24	theme	human	197:201	arg1	EPO					226:228	EPO	226:228	EPO	226:228	The determination by protein chemistry methods of the half-cystine status in human eosinophil peroxidase (EPO) is reported.
10864452	0	25	theme	half-cystine	14:25	arg1	residues					27:34	half-cystine residues	14:34	half-cystine residues	14:34	The status of half-cystine residues and locations of N-glycosylated asparagine residues in human eosinophil peroxidase.
10864452	5	26	theme	free	628:631	arg1	groups					644:649	free sulfhydryl groups	628:649	free sulfhydryl groups	628:649	Cys291 and Cys455 are found to be unpaired, containing free sulfhydryl groups.
10864452	4	27	theme	Disulfide	379:387	arg1	bridges					389:395	Disulfide bridges	379:395	Disulfide bridges	379:395	Disulfide bridges connect Cys253 and Cys263, Cys257 and Cys287, Cys359 and Cys370, Cys570 and Cys635, and Cys676 and Cys701, forming five intrachain disulfide bridges in the heavy chain of EPO.
10864452	2	28	theme	half-cystine	285:296	arg1	residues					298:305	14 half-cystine residues	282:305	14 half-cystine residues	282:305	EPO is two-chained and has a total of 14 half-cystine residues.
10864452	9	29	from	sites	1003:1007	arg1	EPO					1012:1014	EPO	1012:1014	EPO	1012:1014	Of four candidate sites in EPO for attachment of glucosamine-based carbohydrate, Asn327 and Asn363 are occupied, whereas Asn700 and Asn708 are unsubstituted.
10864452	1	30	theme	eosinophil	203:212	arg1	peroxidase					214:223	human eosinophil peroxidase	197:223	human eosinophil peroxidase (EPO)	197:229	The determination by protein chemistry methods of the half-cystine status in human eosinophil peroxidase (EPO) is reported.
10864452	1	30	theme	eosinophil	203:212	arg1	EPO					226:228	EPO	226:228	EPO	226:228	The determination by protein chemistry methods of the half-cystine status in human eosinophil peroxidase (EPO) is reported.
10864452	3	31	theme	light	359:363	arg1	chain					365:369	the light chain	355:369	the light chain of EPO	355:376	Cys141 and Cys152 form an intrachain bridge in the light chain of EPO.
10864452	9	32	dep	occupied	1088:1095	arg1	whereas					1098:1104	whereas	1098:1104	whereas	1098:1104	Of four candidate sites in EPO for attachment of glucosamine-based carbohydrate, Asn327 and Asn363 are occupied, whereas Asn700 and Asn708 are unsubstituted.
10864452	5	33	theme	sulfhydryl	633:642	arg1	groups					644:649	free sulfhydryl groups	628:649	free sulfhydryl groups	628:649	Cys291 and Cys455 are found to be unpaired, containing free sulfhydryl groups.
10864452	8	34	dep	226	844:846	arg1	185-207					849:855	185-207	849:855	185-207	849:855	226, 185-207) to be general for the class of mammalian peroxidases, including EPO, MPO, lactoperoxidase (LPO), and thyroid peroxidase (TPO).
10864452	4	35	theme	EPO	568:570	arg1	chain					559:563	the heavy chain	549:563	the heavy chain of EPO	549:570	Disulfide bridges connect Cys253 and Cys263, Cys257 and Cys287, Cys359 and Cys370, Cys570 and Cys635, and Cys676 and Cys701, forming five intrachain disulfide bridges in the heavy chain of EPO.
10864452	6	36	dep	myeloperoxidase	773:787	arg1	1992					824:827	1992	824:827	1992	824:827	The pattern of disulfide bridges is in agreement with that predicted from the X-ray crystallographic structure of canine myeloperoxidase (MPO) (Zeng, J., and Fenna, R. E. (1992) J. Mol.
10864452	6	36	dep	myeloperoxidase	773:787	arg1	R.					817:818	R.	817:818	R.	817:818	The pattern of disulfide bridges is in agreement with that predicted from the X-ray crystallographic structure of canine myeloperoxidase (MPO) (Zeng, J., and Fenna, R. E. (1992) J. Mol.
10864452	6	36	dep	myeloperoxidase	773:787	arg1	J.					802:803	J.	802:803	J.	802:803	The pattern of disulfide bridges is in agreement with that predicted from the X-ray crystallographic structure of canine myeloperoxidase (MPO) (Zeng, J., and Fenna, R. E. (1992) J. Mol.
10864452	6	36	dep	myeloperoxidase	773:787	arg1	E					820:820	E	820:820	E	820:820	The pattern of disulfide bridges is in agreement with that predicted from the X-ray crystallographic structure of canine myeloperoxidase (MPO) (Zeng, J., and Fenna, R. E. (1992) J. Mol.
10864452	0	37	from	residues	79:86	arg1	peroxidase					108:117	human eosinophil peroxidase	91:117	human eosinophil peroxidase	91:117	The status of half-cystine residues and locations of N-glycosylated asparagine residues in human eosinophil peroxidase.
10864452	0	38	theme	residues	27:34	arg1	locations					40:48	locations	40:48	locations of N-glycosylated asparagine residues in human eosinophil peroxidase	40:117	The status of half-cystine residues and locations of N-glycosylated asparagine residues in human eosinophil peroxidase.
10864452	0	38	theme	residues	27:34	arg1	status					4:9	The status	0:9	The status of half-cystine residues	0:34	The status of half-cystine residues and locations of N-glycosylated asparagine residues in human eosinophil peroxidase.
10864452	9	39	theme	carbohydrate	1052:1063	arg1	attachment					1020:1029	attachment	1020:1029	attachment of glucosamine-based carbohydrate	1020:1063	Of four candidate sites in EPO for attachment of glucosamine-based carbohydrate, Asn327 and Asn363 are occupied, whereas Asn700 and Asn708 are unsubstituted.
10864452	3	40	theme	EPO	374:376	arg1	chain					365:369	the light chain	355:369	the light chain of EPO	355:376	Cys141 and Cys152 form an intrachain bridge in the light chain of EPO.
10864452	9	41	theme	candidate	993:1001	arg1	sites					1003:1007	four candidate sites	988:1007	four candidate sites in EPO for attachment of glucosamine-based carbohydrate	988:1063	Of four candidate sites in EPO for attachment of glucosamine-based carbohydrate, Asn327 and Asn363 are occupied, whereas Asn700 and Asn708 are unsubstituted.
10864452	6	42	theme	myeloperoxidase	773:787	arg1	structure					753:761	the X-ray crystallographic structure	726:761	the X-ray crystallographic structure of canine myeloperoxidase (MPO) (Zeng, J., and Fenna, R. E. (1992) J. Mol	726:835	The pattern of disulfide bridges is in agreement with that predicted from the X-ray crystallographic structure of canine myeloperoxidase (MPO) (Zeng, J., and Fenna, R. E. (1992) J. Mol.
10864452	10	43	theme	residues	1214:1221	arg1	sequence					1202:1209	the sequence	1198:1209	the sequence of residues 645-659	1198:1229	Furthermore, a discrepancy in the literature regarding the sequence of residues 645-659 is resolved.
10864452	0	44	from	peroxidase	108:117	arg1	locations					40:48	locations	40:48	locations of N-glycosylated asparagine residues in human eosinophil peroxidase	40:117	The status of half-cystine residues and locations of N-glycosylated asparagine residues in human eosinophil peroxidase.
10864452	0	44	from	peroxidase	108:117	arg1	status					4:9	The status	0:9	The status of half-cystine residues	0:34	The status of half-cystine residues and locations of N-glycosylated asparagine residues in human eosinophil peroxidase.
10864452	1	45	from	peroxidase	214:223	arg1	methods					159:165	protein chemistry methods	141:165	protein chemistry methods of the half-cystine status in human eosinophil peroxidase (EPO)	141:229	The determination by protein chemistry methods of the half-cystine status in human eosinophil peroxidase (EPO) is reported.
10864452	4	46	theme	heavy	553:557	arg1	chain					559:563	the heavy chain	549:563	the heavy chain of EPO	549:570	Disulfide bridges connect Cys253 and Cys263, Cys257 and Cys287, Cys359 and Cys370, Cys570 and Cys635, and Cys676 and Cys701, forming five intrachain disulfide bridges in the heavy chain of EPO.
10864452	6	47	theme	bridges	677:683	arg1	pattern					656:662	The pattern	652:662	The pattern of disulfide bridges	652:683	The pattern of disulfide bridges is in agreement with that predicted from the X-ray crystallographic structure of canine myeloperoxidase (MPO) (Zeng, J., and Fenna, R. E. (1992) J. Mol.
10864452	6	48	theme	canine	766:771	arg1	myeloperoxidase					773:787	canine myeloperoxidase	766:787	canine myeloperoxidase (MPO) (Zeng, J., and Fenna, R. E. (1992) J. Mol	766:835	The pattern of disulfide bridges is in agreement with that predicted from the X-ray crystallographic structure of canine myeloperoxidase (MPO) (Zeng, J., and Fenna, R. E. (1992) J. Mol.
10864452	6	48	theme	canine	766:771	arg1	MPO					790:792	MPO	790:792	MPO	790:792	The pattern of disulfide bridges is in agreement with that predicted from the X-ray crystallographic structure of canine myeloperoxidase (MPO) (Zeng, J., and Fenna, R. E. (1992) J. Mol.
10864452	6	49	theme	disulfide	667:675	arg1	bridges					677:683	disulfide bridges	667:683	disulfide bridges	667:683	The pattern of disulfide bridges is in agreement with that predicted from the X-ray crystallographic structure of canine myeloperoxidase (MPO) (Zeng, J., and Fenna, R. E. (1992) J. Mol.
10864452	1	50	theme	protein	141:147	arg1	methods					159:165	protein chemistry methods	141:165	protein chemistry methods of the half-cystine status in human eosinophil peroxidase (EPO)	141:229	The determination by protein chemistry methods of the half-cystine status in human eosinophil peroxidase (EPO) is reported.
10864452	0	51	theme	asparagine	68:77	arg1	residues					79:86	N-glycosylated asparagine residues	53:86	N-glycosylated asparagine residues in human eosinophil peroxidase	53:117	The status of half-cystine residues and locations of N-glycosylated asparagine residues in human eosinophil peroxidase.
10864452	1	52	theme	chemistry	149:157	arg1	methods					159:165	protein chemistry methods	141:165	protein chemistry methods of the half-cystine status in human eosinophil peroxidase (EPO)	141:229	The determination by protein chemistry methods of the half-cystine status in human eosinophil peroxidase (EPO) is reported.
10864452	0	53	theme	N-glycosylated	53:66	arg1	residues					79:86	N-glycosylated asparagine residues	53:86	N-glycosylated asparagine residues in human eosinophil peroxidase	53:117	The status of half-cystine residues and locations of N-glycosylated asparagine residues in human eosinophil peroxidase.
10864452	6	54	dep	J.	802:803	arg1	Mol					833:835	Mol	833:835	Mol	833:835	The pattern of disulfide bridges is in agreement with that predicted from the X-ray crystallographic structure of canine myeloperoxidase (MPO) (Zeng, J., and Fenna, R. E. (1992) J. Mol.
10864452	4	55	from	bridges	538:544	arg1	chain					559:563	the heavy chain	549:563	the heavy chain of EPO	549:570	Disulfide bridges connect Cys253 and Cys263, Cys257 and Cys287, Cys359 and Cys370, Cys570 and Cys635, and Cys676 and Cys701, forming five intrachain disulfide bridges in the heavy chain of EPO.
10887202	2	0	theme	cerebral	114:121	arg1	deposition					123:132	The cerebral deposition	110:132	The cerebral deposition of amyloid beta-peptide	110:156	The cerebral deposition of amyloid beta-peptide is an early and critical feature of Alzheimer's disease.
10887202	2	0	theme	cerebral	114:121	arg1	feature					183:189	an early and critical feature	161:189	an early and critical feature of Alzheimer's disease	161:212	The cerebral deposition of amyloid beta-peptide is an early and critical feature of Alzheimer's disease.
10887202	3	1	theme	Amyloid	215:221	arg1	beta-peptide					223:234	Amyloid beta-peptide	215:234	Amyloid beta-peptide	215:234	Amyloid beta-peptide is released from the amyloid precursor protein by the sequential action of two proteases, beta-secretase and gamma-secretase, and these proteases are prime targets for therapeutic intervention.
10887202	9	2	theme	aspartic	1291:1298	arg1	proteases					1300:1308	other aspartic proteases	1285:1308	other aspartic proteases	1285:1308	Despite the conservation of the active site residues and the 30-37% amino acid homology with known aspartic proteases, the disulfide motif is fundamentally different from that of other aspartic proteases.
10887202	9	3	theme	amino	1174:1178	arg1	homology					1185:1192	the 30-37% amino acid homology	1163:1192	the 30-37% amino acid homology with known aspartic proteases	1163:1222	Despite the conservation of the active site residues and the 30-37% amino acid homology with known aspartic proteases, the disulfide motif is fundamentally different from that of other aspartic proteases.
10887202	3	4	theme	proteases	315:323	arg1	action					301:306	the sequential action	286:306	the sequential action of two proteases, beta-secretase and gamma-secretase,	286:360	Amyloid beta-peptide is released from the amyloid precursor protein by the sequential action of two proteases, beta-secretase and gamma-secretase, and these proteases are prime targets for therapeutic intervention.
10887202	4	5	theme	known	500:504	arg1	properties					506:515	all the known properties	492:515	all the known properties of beta-secretase	492:533	We have recently cloned a novel aspartic protease, BACE, with all the known properties of beta-secretase.
10887202	8	6	dep	linkages	1034:1041	arg1	443					1076:1078	443	1076:1078	443	1076:1078	The six Cys residues in the ectodomain form three intramolecular disulfide linkages (Cys(216)-Cys(420), Cys(278)-Cys(443), and Cys(330)-Cys(380)).
10887202	8	6	dep	linkages	1034:1041	arg1	Cys					1063:1065	Cys(278)-Cys	1063:1074	Cys(278)-Cys(443)	1063:1079	The six Cys residues in the ectodomain form three intramolecular disulfide linkages (Cys(216)-Cys(420), Cys(278)-Cys(443), and Cys(330)-Cys(380)).
10887202	8	6	dep	linkages	1034:1041	arg1	linkages					1034:1041	three intramolecular disulfide linkages	1003:1041	three intramolecular disulfide linkages (Cys(216)-Cys(420), Cys(278)-Cys(443), and Cys(330)-Cys(380))	1003:1103	The six Cys residues in the ectodomain form three intramolecular disulfide linkages (Cys(216)-Cys(420), Cys(278)-Cys(443), and Cys(330)-Cys(380)).
10887202	8	6	dep	linkages	1034:1041	arg1	Cys					1044:1046	Cys(216)-Cys	1044:1055	Cys(216)-Cys(420)	1044:1060	The six Cys residues in the ectodomain form three intramolecular disulfide linkages (Cys(216)-Cys(420), Cys(278)-Cys(443), and Cys(330)-Cys(380)).
10887202	8	6	dep	linkages	1034:1041	arg1	Cys					1086:1088	Cys(330)-Cys	1086:1097	Cys(330)-Cys(380)	1086:1102	The six Cys residues in the ectodomain form three intramolecular disulfide linkages (Cys(216)-Cys(420), Cys(278)-Cys(443), and Cys(330)-Cys(380)).
10887202	8	6	dep	linkages	1034:1041	arg1	420					1057:1059	420	1057:1059	420	1057:1059	The six Cys residues in the ectodomain form three intramolecular disulfide linkages (Cys(216)-Cys(420), Cys(278)-Cys(443), and Cys(330)-Cys(380)).
10887202	8	6	dep	linkages	1034:1041	arg1	380					1099:1101	380	1099:1101	380	1099:1101	The six Cys residues in the ectodomain form three intramolecular disulfide linkages (Cys(216)-Cys(420), Cys(278)-Cys(443), and Cys(330)-Cys(380)).
10887202	5	7	theme	integral	587:594	arg1	BACE					561:564	BACE	561:564	BACE	561:564	Here we demonstrate that BACE is an N-glycosylated integral membrane protein that undergoes constitutive N-terminal processing in the Golgi apparatus.
10887202	5	7	theme	integral	587:594	arg1	protein					605:611	an N-glycosylated integral membrane protein	569:611	an N-glycosylated integral membrane protein that undergoes constitutive N-terminal processing in the Golgi apparatus	569:684	Here we demonstrate that BACE is an N-glycosylated integral membrane protein that undergoes constitutive N-terminal processing in the Golgi apparatus.
10887202	4	8	with	protease	471:478	arg1	properties					506:515	all the known properties	492:515	all the known properties of beta-secretase	492:533	We have recently cloned a novel aspartic protease, BACE, with all the known properties of beta-secretase.
10887202	9	9	theme	acid	1180:1183	arg1	homology					1185:1192	the 30-37% amino acid homology	1163:1192	the 30-37% amino acid homology with known aspartic proteases	1163:1222	Despite the conservation of the active site residues and the 30-37% amino acid homology with known aspartic proteases, the disulfide motif is fundamentally different from that of other aspartic proteases.
10887202	11	10	theme	family	1532:1537	arg1	BACE					1505:1508	BACE	1505:1508	BACE	1505:1508	Taken together, both the presence of a transmembrane domain and the unusual disulfide bond structure lead us to conclude that BACE is an atypical pepsin family member.
10887202	11	10	theme	family	1532:1537	arg1	member					1539:1544	an atypical pepsin family member	1513:1544	an atypical pepsin family member	1513:1544	Taken together, both the presence of a transmembrane domain and the unusual disulfide bond structure lead us to conclude that BACE is an atypical pepsin family member.
10887202	5	11	theme	Golgi	670:674	arg1	apparatus					676:684	the Golgi apparatus	666:684	the Golgi apparatus	666:684	Here we demonstrate that BACE is an N-glycosylated integral membrane protein that undergoes constitutive N-terminal processing in the Golgi apparatus.
10887202	5	12	theme	membrane	596:603	arg1	BACE					561:564	BACE	561:564	BACE	561:564	Here we demonstrate that BACE is an N-glycosylated integral membrane protein that undergoes constitutive N-terminal processing in the Golgi apparatus.
10887202	5	12	theme	membrane	596:603	arg1	protein					605:611	an N-glycosylated integral membrane protein	569:611	an N-glycosylated integral membrane protein that undergoes constitutive N-terminal processing in the Golgi apparatus	569:684	Here we demonstrate that BACE is an N-glycosylated integral membrane protein that undergoes constitutive N-terminal processing in the Golgi apparatus.
10887202	5	13	gly	N-glycosylated	572:585	arg1	BACE					561:564	BACE	561:564	BACE	561:564	Here we demonstrate that BACE is an N-glycosylated integral membrane protein that undergoes constitutive N-terminal processing in the Golgi apparatus.
10887202	5	13	gly	N-glycosylated	572:585	arg1	protein					605:611	an N-glycosylated integral membrane protein	569:611	an N-glycosylated integral membrane protein that undergoes constitutive N-terminal processing in the Golgi apparatus	569:684	Here we demonstrate that BACE is an N-glycosylated integral membrane protein that undergoes constitutive N-terminal processing in the Golgi apparatus.
10887202	10	14	theme	enzyme	1371:1376	arg1	specificity					1352:1362	the substrate specificity	1338:1362	the substrate specificity of the enzyme	1338:1376	This difference may affect the substrate specificity of the enzyme.
10887202	7	15	dep	sites	907:911	arg1	Asn					934:936	Asn(223)	934:941	Asn(223)	934:941	This molecule starts at Glu(46) and contains four N-glycosylation sites (Asn(153), Asn(172), Asn(223), and Asn(354)).
10887202	7	15	dep	sites	907:911	arg1	Asn					924:926	Asn(172)	924:931	Asn(172)	924:931	This molecule starts at Glu(46) and contains four N-glycosylation sites (Asn(153), Asn(172), Asn(223), and Asn(354)).
10887202	7	15	dep	sites	907:911	arg1	Asn					914:916	Asn(153)	914:921	Asn(153)	914:921	This molecule starts at Glu(46) and contains four N-glycosylation sites (Asn(153), Asn(172), Asn(223), and Asn(354)).
10887202	7	15	dep	sites	907:911	arg1	sites					907:911	four N-glycosylation sites	886:911	four N-glycosylation sites (Asn(153), Asn(172), Asn(223), and Asn(354))	886:956	This molecule starts at Glu(46) and contains four N-glycosylation sites (Asn(153), Asn(172), Asn(223), and Asn(354)).
10887202	7	15	dep	sites	907:911	arg1	Asn					948:950	Asn(354)	948:955	Asn(354)	948:955	This molecule starts at Glu(46) and contains four N-glycosylation sites (Asn(153), Asn(172), Asn(223), and Asn(354)).
10887202	11	16	theme	pepsin	1525:1530	arg1	BACE					1505:1508	BACE	1505:1508	BACE	1505:1508	Taken together, both the presence of a transmembrane domain and the unusual disulfide bond structure lead us to conclude that BACE is an atypical pepsin family member.
10887202	11	16	theme	pepsin	1525:1530	arg1	member					1539:1544	an atypical pepsin family member	1513:1544	an atypical pepsin family member	1513:1544	Taken together, both the presence of a transmembrane domain and the unusual disulfide bond structure lead us to conclude that BACE is an atypical pepsin family member.
10887202	2	17	theme	beta-peptide	145:156	arg1	deposition					123:132	The cerebral deposition	110:132	The cerebral deposition of amyloid beta-peptide	110:156	The cerebral deposition of amyloid beta-peptide is an early and critical feature of Alzheimer's disease.
10887202	2	17	theme	beta-peptide	145:156	arg1	feature					183:189	an early and critical feature	161:189	an early and critical feature of Alzheimer's disease	161:212	The cerebral deposition of amyloid beta-peptide is an early and critical feature of Alzheimer's disease.
10887202	6	18	theme	detailed	787:794	arg1	analysis					796:803	a detailed analysis	785:803	a detailed analysis of posttranslational modifications	785:838	We have used a secreted Fc fusion-form of BACE (BACE-IgG) that contains the entire ectodomain for a detailed analysis of posttranslational modifications.
10887202	1	19	theme	pepsin	64:69	arg1	member					78:83	A pepsin family member	62:83	A pepsin family member with unusual properties	62:107	A pepsin family member with unusual properties.
10887202	6	20	theme	Fc	711:712	arg1	fusion-form					714:724	a secreted Fc fusion-form	700:724	a secreted Fc fusion-form of BACE (BACE-IgG) that contains the entire ectodomain for a detailed analysis of posttranslational modifications	700:838	We have used a secreted Fc fusion-form of BACE (BACE-IgG) that contains the entire ectodomain for a detailed analysis of posttranslational modifications.
10887202	9	21	theme	known	1199:1203	arg1	proteases					1214:1222	known aspartic proteases	1199:1222	known aspartic proteases	1199:1222	Despite the conservation of the active site residues and the 30-37% amino acid homology with known aspartic proteases, the disulfide motif is fundamentally different from that of other aspartic proteases.
10887202	2	22	theme	amyloid	137:143	arg1	beta-peptide					145:156	amyloid beta-peptide	137:156	amyloid beta-peptide	137:156	The cerebral deposition of amyloid beta-peptide is an early and critical feature of Alzheimer's disease.
10887202	0	23	theme	-secretase	37:46	arg1	BACE					56:59	Alzheimer's beta -secretase protein BACE	20:59	Alzheimer's beta -secretase protein BACE	20:59	Characterization of Alzheimer's beta -secretase protein BACE.
10887202	9	24	with	conservation	1118:1129	arg1	proteases					1214:1222	known aspartic proteases	1199:1222	known aspartic proteases	1199:1222	Despite the conservation of the active site residues and the 30-37% amino acid homology with known aspartic proteases, the disulfide motif is fundamentally different from that of other aspartic proteases.
10887202	1	25	theme	family	71:76	arg1	member					78:83	A pepsin family member	62:83	A pepsin family member with unusual properties	62:107	A pepsin family member with unusual properties.
10887202	6	26	theme	secreted	702:709	arg1	fusion-form					714:724	a secreted Fc fusion-form	700:724	a secreted Fc fusion-form of BACE (BACE-IgG) that contains the entire ectodomain for a detailed analysis of posttranslational modifications	700:838	We have used a secreted Fc fusion-form of BACE (BACE-IgG) that contains the entire ectodomain for a detailed analysis of posttranslational modifications.
10887202	9	27	theme	aspartic	1205:1212	arg1	proteases					1214:1222	known aspartic proteases	1199:1222	known aspartic proteases	1199:1222	Despite the conservation of the active site residues and the 30-37% amino acid homology with known aspartic proteases, the disulfide motif is fundamentally different from that of other aspartic proteases.
10887202	11	28	theme	domain	1432:1437	arg1	structure					1470:1478	the unusual disulfide bond structure	1443:1478	the unusual disulfide bond structure	1443:1478	Taken together, both the presence of a transmembrane domain and the unusual disulfide bond structure lead us to conclude that BACE is an atypical pepsin family member.
10887202	11	28	theme	domain	1432:1437	arg1	presence					1404:1411	the presence	1400:1411	the presence of a transmembrane domain	1400:1437	Taken together, both the presence of a transmembrane domain and the unusual disulfide bond structure lead us to conclude that BACE is an atypical pepsin family member.
10887202	5	29	theme	N-terminal	641:650	arg1	processing					652:661	constitutive N-terminal processing	628:661	constitutive N-terminal processing in the Golgi apparatus	628:684	Here we demonstrate that BACE is an N-glycosylated integral membrane protein that undergoes constitutive N-terminal processing in the Golgi apparatus.
10887202	9	30	from	that	1277:1280	arg1	motif					1239:1243	the disulfide motif	1225:1243	the disulfide motif	1225:1243	Despite the conservation of the active site residues and the 30-37% amino acid homology with known aspartic proteases, the disulfide motif is fundamentally different from that of other aspartic proteases.
10887202	9	30	from	that	1277:1280	arg1	different					1262:1270	different	1262:1270	different	1262:1270	Despite the conservation of the active site residues and the 30-37% amino acid homology with known aspartic proteases, the disulfide motif is fundamentally different from that of other aspartic proteases.
10887202	11	31	theme	bond	1465:1468	arg1	structure					1470:1478	the unusual disulfide bond structure	1443:1478	the unusual disulfide bond structure	1443:1478	Taken together, both the presence of a transmembrane domain and the unusual disulfide bond structure lead us to conclude that BACE is an atypical pepsin family member.
10887202	3	32	theme	prime	386:390	arg1	proteases					372:380	these proteases	366:380	these proteases	366:380	Amyloid beta-peptide is released from the amyloid precursor protein by the sequential action of two proteases, beta-secretase and gamma-secretase, and these proteases are prime targets for therapeutic intervention.
10887202	3	32	theme	prime	386:390	arg1	targets					392:398	prime targets	386:398	prime targets for therapeutic intervention	386:427	Amyloid beta-peptide is released from the amyloid precursor protein by the sequential action of two proteases, beta-secretase and gamma-secretase, and these proteases are prime targets for therapeutic intervention.
10887202	1	33	with	member	78:83	arg1	properties					98:107	unusual properties	90:107	unusual properties	90:107	A pepsin family member with unusual properties.
10887202	5	34	from	processing	652:661	arg1	apparatus					676:684	the Golgi apparatus	666:684	the Golgi apparatus	666:684	Here we demonstrate that BACE is an N-glycosylated integral membrane protein that undergoes constitutive N-terminal processing in the Golgi apparatus.
10887202	5	35	theme	N-glycosylated	572:585	arg1	BACE					561:564	BACE	561:564	BACE	561:564	Here we demonstrate that BACE is an N-glycosylated integral membrane protein that undergoes constitutive N-terminal processing in the Golgi apparatus.
10887202	5	35	theme	N-glycosylated	572:585	arg1	protein					605:611	an N-glycosylated integral membrane protein	569:611	an N-glycosylated integral membrane protein that undergoes constitutive N-terminal processing in the Golgi apparatus	569:684	Here we demonstrate that BACE is an N-glycosylated integral membrane protein that undergoes constitutive N-terminal processing in the Golgi apparatus.
10887202	1	36	theme	unusual	90:96	arg1	properties					98:107	unusual properties	90:107	unusual properties	90:107	A pepsin family member with unusual properties.
10887202	6	37	theme	posttranslational	808:824	arg1	modifications					826:838	posttranslational modifications	808:838	posttranslational modifications	808:838	We have used a secreted Fc fusion-form of BACE (BACE-IgG) that contains the entire ectodomain for a detailed analysis of posttranslational modifications.
10887202	9	38	theme	disulfide	1229:1237	arg1	motif					1239:1243	the disulfide motif	1225:1243	the disulfide motif	1225:1243	Despite the conservation of the active site residues and the 30-37% amino acid homology with known aspartic proteases, the disulfide motif is fundamentally different from that of other aspartic proteases.
10887202	9	38	theme	disulfide	1229:1237	arg1	different					1262:1270	different	1262:1270	different	1262:1270	Despite the conservation of the active site residues and the 30-37% amino acid homology with known aspartic proteases, the disulfide motif is fundamentally different from that of other aspartic proteases.
10887202	8	39	theme	Cys	967:969	arg1	residues					971:978	The six Cys residues	959:978	The six Cys residues in the ectodomain	959:996	The six Cys residues in the ectodomain form three intramolecular disulfide linkages (Cys(216)-Cys(420), Cys(278)-Cys(443), and Cys(330)-Cys(380)).
10887202	2	40	theme	critical	174:181	arg1	deposition					123:132	The cerebral deposition	110:132	The cerebral deposition of amyloid beta-peptide	110:156	The cerebral deposition of amyloid beta-peptide is an early and critical feature of Alzheimer's disease.
10887202	2	40	theme	critical	174:181	arg1	feature					183:189	an early and critical feature	161:189	an early and critical feature of Alzheimer's disease	161:212	The cerebral deposition of amyloid beta-peptide is an early and critical feature of Alzheimer's disease.
10887202	8	41	from	residues	971:978	arg1	ectodomain					987:996	the ectodomain	983:996	the ectodomain	983:996	The six Cys residues in the ectodomain form three intramolecular disulfide linkages (Cys(216)-Cys(420), Cys(278)-Cys(443), and Cys(330)-Cys(380)).
10887202	3	42	theme	therapeutic	404:414	arg1	intervention					416:427	therapeutic intervention	404:427	therapeutic intervention	404:427	Amyloid beta-peptide is released from the amyloid precursor protein by the sequential action of two proteases, beta-secretase and gamma-secretase, and these proteases are prime targets for therapeutic intervention.
10887202	11	43	theme	transmembrane	1418:1430	arg1	domain					1432:1437	a transmembrane domain	1416:1437	a transmembrane domain	1416:1437	Taken together, both the presence of a transmembrane domain and the unusual disulfide bond structure lead us to conclude that BACE is an atypical pepsin family member.
10887202	3	44	theme	amyloid	257:263	arg1	protein					275:281	the amyloid precursor protein	253:281	the amyloid precursor protein	253:281	Amyloid beta-peptide is released from the amyloid precursor protein by the sequential action of two proteases, beta-secretase and gamma-secretase, and these proteases are prime targets for therapeutic intervention.
10887202	7	45	contain	contains	877:884	arg2	Asn					914:916	Asn(153)	914:921	Asn(153)	914:921	This molecule starts at Glu(46) and contains four N-glycosylation sites (Asn(153), Asn(172), Asn(223), and Asn(354)).
10887202	7	45	contain	contains	877:884	arg1	molecule					846:853	This molecule	841:853	This molecule	841:853	This molecule starts at Glu(46) and contains four N-glycosylation sites (Asn(153), Asn(172), Asn(223), and Asn(354)).
10887202	7	45	contain	contains	877:884	arg2	Asn					924:926	Asn(172)	924:931	Asn(172)	924:931	This molecule starts at Glu(46) and contains four N-glycosylation sites (Asn(153), Asn(172), Asn(223), and Asn(354)).
10887202	7	45	contain	contains	877:884	arg2	sites					907:911	four N-glycosylation sites	886:911	four N-glycosylation sites (Asn(153), Asn(172), Asn(223), and Asn(354))	886:956	This molecule starts at Glu(46) and contains four N-glycosylation sites (Asn(153), Asn(172), Asn(223), and Asn(354)).
10887202	7	45	contain	contains	877:884	arg2	Asn					934:936	Asn(223)	934:941	Asn(223)	934:941	This molecule starts at Glu(46) and contains four N-glycosylation sites (Asn(153), Asn(172), Asn(223), and Asn(354)).
10887202	7	45	contain	contains	877:884	arg2	Asn					948:950	Asn(354)	948:955	Asn(354)	948:955	This molecule starts at Glu(46) and contains four N-glycosylation sites (Asn(153), Asn(172), Asn(223), and Asn(354)).
10887202	0	46	theme	beta	32:35	arg1	BACE					56:59	Alzheimer's beta -secretase protein BACE	20:59	Alzheimer's beta -secretase protein BACE	20:59	Characterization of Alzheimer's beta -secretase protein BACE.
10887202	3	47	theme	precursor	265:273	arg1	protein					275:281	the amyloid precursor protein	253:281	the amyloid precursor protein	253:281	Amyloid beta-peptide is released from the amyloid precursor protein by the sequential action of two proteases, beta-secretase and gamma-secretase, and these proteases are prime targets for therapeutic intervention.
10887202	2	48	theme	early	164:168	arg1	deposition					123:132	The cerebral deposition	110:132	The cerebral deposition of amyloid beta-peptide	110:156	The cerebral deposition of amyloid beta-peptide is an early and critical feature of Alzheimer's disease.
10887202	2	48	theme	early	164:168	arg1	feature					183:189	an early and critical feature	161:189	an early and critical feature of Alzheimer's disease	161:212	The cerebral deposition of amyloid beta-peptide is an early and critical feature of Alzheimer's disease.
10887202	6	49	contain	contains	750:757	arg2	ectodomain					770:779	the entire ectodomain	759:779	the entire ectodomain for a detailed analysis of posttranslational modifications	759:838	We have used a secreted Fc fusion-form of BACE (BACE-IgG) that contains the entire ectodomain for a detailed analysis of posttranslational modifications.
10887202	6	49	contain	contains	750:757	arg1	fusion-form					714:724	a secreted Fc fusion-form	700:724	a secreted Fc fusion-form of BACE (BACE-IgG) that contains the entire ectodomain for a detailed analysis of posttranslational modifications	700:838	We have used a secreted Fc fusion-form of BACE (BACE-IgG) that contains the entire ectodomain for a detailed analysis of posttranslational modifications.
10887202	9	50	with	homology	1185:1192	arg1	proteases					1214:1222	known aspartic proteases	1199:1222	known aspartic proteases	1199:1222	Despite the conservation of the active site residues and the 30-37% amino acid homology with known aspartic proteases, the disulfide motif is fundamentally different from that of other aspartic proteases.
10887202	9	51	theme	residues	1150:1157	arg1	conservation					1118:1129	the conservation	1114:1129	the conservation of the active site residues	1114:1157	Despite the conservation of the active site residues and the 30-37% amino acid homology with known aspartic proteases, the disulfide motif is fundamentally different from that of other aspartic proteases.
10887202	9	51	theme	residues	1150:1157	arg1	homology					1185:1192	the 30-37% amino acid homology	1163:1192	the 30-37% amino acid homology with known aspartic proteases	1163:1222	Despite the conservation of the active site residues and the 30-37% amino acid homology with known aspartic proteases, the disulfide motif is fundamentally different from that of other aspartic proteases.
10887202	0	52	theme	BACE	56:59	arg1	Characterization					0:15	Characterization	0:15	Characterization of Alzheimer's beta -secretase protein BACE.	0:60	Characterization of Alzheimer's beta -secretase protein BACE.
10887202	9	53	theme	active	1138:1143	arg1	residues					1150:1157	the active site residues	1134:1157	the active site residues	1134:1157	Despite the conservation of the active site residues and the 30-37% amino acid homology with known aspartic proteases, the disulfide motif is fundamentally different from that of other aspartic proteases.
10887202	4	54	theme	novel	456:460	arg1	BACE					481:484	BACE	481:484	BACE	481:484	We have recently cloned a novel aspartic protease, BACE, with all the known properties of beta-secretase.
10887202	4	54	theme	novel	456:460	arg1	protease					471:478	a novel aspartic protease	454:478	a novel aspartic protease	454:478	We have recently cloned a novel aspartic protease, BACE, with all the known properties of beta-secretase.
10887202	6	55	theme	entire	763:768	arg1	ectodomain					770:779	the entire ectodomain	759:779	the entire ectodomain for a detailed analysis of posttranslational modifications	759:838	We have used a secreted Fc fusion-form of BACE (BACE-IgG) that contains the entire ectodomain for a detailed analysis of posttranslational modifications.
10887202	11	56	theme	atypical	1516:1523	arg1	BACE					1505:1508	BACE	1505:1508	BACE	1505:1508	Taken together, both the presence of a transmembrane domain and the unusual disulfide bond structure lead us to conclude that BACE is an atypical pepsin family member.
10887202	11	56	theme	atypical	1516:1523	arg1	member					1539:1544	an atypical pepsin family member	1513:1544	an atypical pepsin family member	1513:1544	Taken together, both the presence of a transmembrane domain and the unusual disulfide bond structure lead us to conclude that BACE is an atypical pepsin family member.
10887202	0	57	theme	protein	48:54	arg1	BACE					56:59	Alzheimer's beta -secretase protein BACE	20:59	Alzheimer's beta -secretase protein BACE	20:59	Characterization of Alzheimer's beta -secretase protein BACE.
10887202	9	58	theme	site	1145:1148	arg1	residues					1150:1157	the active site residues	1134:1157	the active site residues	1134:1157	Despite the conservation of the active site residues and the 30-37% amino acid homology with known aspartic proteases, the disulfide motif is fundamentally different from that of other aspartic proteases.
10887202	5	59	theme	constitutive	628:639	arg1	processing					652:661	constitutive N-terminal processing	628:661	constitutive N-terminal processing in the Golgi apparatus	628:684	Here we demonstrate that BACE is an N-glycosylated integral membrane protein that undergoes constitutive N-terminal processing in the Golgi apparatus.
10887202	4	60	theme	aspartic	462:469	arg1	BACE					481:484	BACE	481:484	BACE	481:484	We have recently cloned a novel aspartic protease, BACE, with all the known properties of beta-secretase.
10887202	4	60	theme	aspartic	462:469	arg1	protease					471:478	a novel aspartic protease	454:478	a novel aspartic protease	454:478	We have recently cloned a novel aspartic protease, BACE, with all the known properties of beta-secretase.
10887202	4	61	theme	beta-secretase	520:533	arg1	properties					506:515	all the known properties	492:515	all the known properties of beta-secretase	492:533	We have recently cloned a novel aspartic protease, BACE, with all the known properties of beta-secretase.
10887202	8	62	theme	intramolecular	1009:1022	arg1	Cys					1044:1046	Cys(216)-Cys	1044:1055	Cys(216)-Cys(420)	1044:1060	The six Cys residues in the ectodomain form three intramolecular disulfide linkages (Cys(216)-Cys(420), Cys(278)-Cys(443), and Cys(330)-Cys(380)).
10887202	8	62	theme	intramolecular	1009:1022	arg1	Cys					1086:1088	Cys(330)-Cys	1086:1097	Cys(330)-Cys(380)	1086:1102	The six Cys residues in the ectodomain form three intramolecular disulfide linkages (Cys(216)-Cys(420), Cys(278)-Cys(443), and Cys(330)-Cys(380)).
10887202	8	62	theme	intramolecular	1009:1022	arg1	linkages					1034:1041	three intramolecular disulfide linkages	1003:1041	three intramolecular disulfide linkages (Cys(216)-Cys(420), Cys(278)-Cys(443), and Cys(330)-Cys(380))	1003:1103	The six Cys residues in the ectodomain form three intramolecular disulfide linkages (Cys(216)-Cys(420), Cys(278)-Cys(443), and Cys(330)-Cys(380)).
10887202	8	62	theme	intramolecular	1009:1022	arg1	Cys					1063:1065	Cys(278)-Cys	1063:1074	Cys(278)-Cys(443)	1063:1079	The six Cys residues in the ectodomain form three intramolecular disulfide linkages (Cys(216)-Cys(420), Cys(278)-Cys(443), and Cys(330)-Cys(380)).
10887202	10	63	theme	substrate	1342:1350	arg1	specificity					1352:1362	the substrate specificity	1338:1362	the substrate specificity of the enzyme	1338:1376	This difference may affect the substrate specificity of the enzyme.
10887202	3	64	theme	sequential	290:299	arg1	action					301:306	the sequential action	286:306	the sequential action of two proteases, beta-secretase and gamma-secretase,	286:360	Amyloid beta-peptide is released from the amyloid precursor protein by the sequential action of two proteases, beta-secretase and gamma-secretase, and these proteases are prime targets for therapeutic intervention.
10887202	7	65	gly	N-glycosylation	891:905	arg2	Asn					914:916	Asn(153)	914:921	Asn(153)	914:921	This molecule starts at Glu(46) and contains four N-glycosylation sites (Asn(153), Asn(172), Asn(223), and Asn(354)).
10887202	7	65	gly	N-glycosylation	891:905	arg2	four					886:889	four	886:889	four	886:889	This molecule starts at Glu(46) and contains four N-glycosylation sites (Asn(153), Asn(172), Asn(223), and Asn(354)).
10887202	7	65	gly	N-glycosylation	891:905	arg2	Asn					924:926	Asn(172)	924:931	Asn(172)	924:931	This molecule starts at Glu(46) and contains four N-glycosylation sites (Asn(153), Asn(172), Asn(223), and Asn(354)).
10887202	7	65	gly	N-glycosylation	891:905	arg2	sites					907:911	four N-glycosylation sites	886:911	four N-glycosylation sites (Asn(153), Asn(172), Asn(223), and Asn(354))	886:956	This molecule starts at Glu(46) and contains four N-glycosylation sites (Asn(153), Asn(172), Asn(223), and Asn(354)).
10887202	7	65	gly	N-glycosylation	891:905	arg2	Asn					934:936	Asn(223)	934:941	Asn(223)	934:941	This molecule starts at Glu(46) and contains four N-glycosylation sites (Asn(153), Asn(172), Asn(223), and Asn(354)).
10887202	7	65	gly	N-glycosylation	891:905	arg2	Asn					948:950	Asn(354)	948:955	Asn(354)	948:955	This molecule starts at Glu(46) and contains four N-glycosylation sites (Asn(153), Asn(172), Asn(223), and Asn(354)).
10887202	9	66	theme	30-37	1167:1171	arg1	%					1172:1172	%	1172:1172	%	1172:1172	Despite the conservation of the active site residues and the 30-37% amino acid homology with known aspartic proteases, the disulfide motif is fundamentally different from that of other aspartic proteases.
10887202	9	67	theme	other	1285:1289	arg1	proteases					1300:1308	other aspartic proteases	1285:1308	other aspartic proteases	1285:1308	Despite the conservation of the active site residues and the 30-37% amino acid homology with known aspartic proteases, the disulfide motif is fundamentally different from that of other aspartic proteases.
10887202	6	68	theme	modifications	826:838	arg1	analysis					796:803	a detailed analysis	785:803	a detailed analysis of posttranslational modifications	785:838	We have used a secreted Fc fusion-form of BACE (BACE-IgG) that contains the entire ectodomain for a detailed analysis of posttranslational modifications.
10887202	11	69	theme	unusual	1447:1453	arg1	structure					1470:1478	the unusual disulfide bond structure	1443:1478	the unusual disulfide bond structure	1443:1478	Taken together, both the presence of a transmembrane domain and the unusual disulfide bond structure lead us to conclude that BACE is an atypical pepsin family member.
10887202	7	70	theme	N-glycosylation	891:905	arg1	Asn					934:936	Asn(223)	934:941	Asn(223)	934:941	This molecule starts at Glu(46) and contains four N-glycosylation sites (Asn(153), Asn(172), Asn(223), and Asn(354)).
10887202	7	70	theme	N-glycosylation	891:905	arg1	Asn					924:926	Asn(172)	924:931	Asn(172)	924:931	This molecule starts at Glu(46) and contains four N-glycosylation sites (Asn(153), Asn(172), Asn(223), and Asn(354)).
10887202	7	70	theme	N-glycosylation	891:905	arg1	Asn					914:916	Asn(153)	914:921	Asn(153)	914:921	This molecule starts at Glu(46) and contains four N-glycosylation sites (Asn(153), Asn(172), Asn(223), and Asn(354)).
10887202	7	70	theme	N-glycosylation	891:905	arg1	sites					907:911	four N-glycosylation sites	886:911	four N-glycosylation sites (Asn(153), Asn(172), Asn(223), and Asn(354))	886:956	This molecule starts at Glu(46) and contains four N-glycosylation sites (Asn(153), Asn(172), Asn(223), and Asn(354)).
10887202	7	70	theme	N-glycosylation	891:905	arg1	Asn					948:950	Asn(354)	948:955	Asn(354)	948:955	This molecule starts at Glu(46) and contains four N-glycosylation sites (Asn(153), Asn(172), Asn(223), and Asn(354)).
10887202	3	71	attach	released	239:246	arg1	protein					275:281	the amyloid precursor protein	253:281	the amyloid precursor protein	253:281	Amyloid beta-peptide is released from the amyloid precursor protein by the sequential action of two proteases, beta-secretase and gamma-secretase, and these proteases are prime targets for therapeutic intervention.
10887202	3	71	attach	released	239:246	arg2	beta-peptide					223:234	Amyloid beta-peptide	215:234	Amyloid beta-peptide	215:234	Amyloid beta-peptide is released from the amyloid precursor protein by the sequential action of two proteases, beta-secretase and gamma-secretase, and these proteases are prime targets for therapeutic intervention.
10887202	8	72	theme	disulfide	1024:1032	arg1	Cys					1044:1046	Cys(216)-Cys	1044:1055	Cys(216)-Cys(420)	1044:1060	The six Cys residues in the ectodomain form three intramolecular disulfide linkages (Cys(216)-Cys(420), Cys(278)-Cys(443), and Cys(330)-Cys(380)).
10887202	8	72	theme	disulfide	1024:1032	arg1	Cys					1086:1088	Cys(330)-Cys	1086:1097	Cys(330)-Cys(380)	1086:1102	The six Cys residues in the ectodomain form three intramolecular disulfide linkages (Cys(216)-Cys(420), Cys(278)-Cys(443), and Cys(330)-Cys(380)).
10887202	8	72	theme	disulfide	1024:1032	arg1	linkages					1034:1041	three intramolecular disulfide linkages	1003:1041	three intramolecular disulfide linkages (Cys(216)-Cys(420), Cys(278)-Cys(443), and Cys(330)-Cys(380))	1003:1103	The six Cys residues in the ectodomain form three intramolecular disulfide linkages (Cys(216)-Cys(420), Cys(278)-Cys(443), and Cys(330)-Cys(380)).
10887202	8	72	theme	disulfide	1024:1032	arg1	Cys					1063:1065	Cys(278)-Cys	1063:1074	Cys(278)-Cys(443)	1063:1079	The six Cys residues in the ectodomain form three intramolecular disulfide linkages (Cys(216)-Cys(420), Cys(278)-Cys(443), and Cys(330)-Cys(380)).
10887202	6	73	theme	BACE	729:732	arg1	fusion-form					714:724	a secreted Fc fusion-form	700:724	a secreted Fc fusion-form of BACE (BACE-IgG) that contains the entire ectodomain for a detailed analysis of posttranslational modifications	700:838	We have used a secreted Fc fusion-form of BACE (BACE-IgG) that contains the entire ectodomain for a detailed analysis of posttranslational modifications.
10887202	6	74	used	used	695:698	arg2	We					687:688	We	687:688	We	687:688	We have used a secreted Fc fusion-form of BACE (BACE-IgG) that contains the entire ectodomain for a detailed analysis of posttranslational modifications.
10887202	11	75	theme	disulfide	1455:1463	arg1	structure					1470:1478	the unusual disulfide bond structure	1443:1478	the unusual disulfide bond structure	1443:1478	Taken together, both the presence of a transmembrane domain and the unusual disulfide bond structure lead us to conclude that BACE is an atypical pepsin family member.
10887202	9	76	theme	%	1172:1172	arg1	homology					1185:1192	the 30-37% amino acid homology	1163:1192	the 30-37% amino acid homology with known aspartic proteases	1163:1222	Despite the conservation of the active site residues and the 30-37% amino acid homology with known aspartic proteases, the disulfide motif is fundamentally different from that of other aspartic proteases.
12096136	6	0	theme	time-of-flight	969:982	arg1	approach					1009:1016	a recently established nano-electrospray ionization quadrupole time-of-flight tandem-mass spectrometry approach	906:1016	a recently established nano-electrospray ionization quadrupole time-of-flight tandem-mass spectrometry approach	906:1016	O-Fucosylation sites were determined by a recently established nano-electrospray ionization quadrupole time-of-flight tandem-mass spectrometry approach.
12096136	7	1	theme	disaccharide	1047:1058	arg1	Hex-dHex-O-Ser/Thr					1060:1077	the disaccharide Hex-dHex-O-Ser/Thr	1043:1077	the disaccharide Hex-dHex-O-Ser/Thr in close proximity to the C-mannosylation sites	1043:1125	Four of five TSRs carry the disaccharide Hex-dHex-O-Ser/Thr in close proximity to the C-mannosylation sites.
12096136	4	2	theme	F-spondin	697:705	arg1	TSRs					648:651	TSRs	648:651	TSRs	648:651	Their analysis by a combined mass spectrometric approach is illustrated with peptides from the thrombospondin type 1 repeats (TSRs) of the recombinant axonal guidance protein F-spondin.
12096136	4	2	theme	F-spondin	697:705	arg1	repeats					639:645	the thrombospondin type 1 repeats	613:645	the thrombospondin type 1 repeats (TSRs) of the recombinant axonal guidance protein F-spondin	613:705	Their analysis by a combined mass spectrometric approach is illustrated with peptides from the thrombospondin type 1 repeats (TSRs) of the recombinant axonal guidance protein F-spondin.
12096136	2	3	theme	analysis	382:389	arg1	methods					391:397	suitable analysis methods	373:397	suitable analysis methods	373:397	Ideally, a comprehensive proteome analysis includes this aspect, a task that is complicated by our incomplete knowledge of the range of possible modifications and often by the lack of suitable analysis methods.
12096136	6	4	theme	quadrupole	958:967	arg1	approach					1009:1016	a recently established nano-electrospray ionization quadrupole time-of-flight tandem-mass spectrometry approach	906:1016	a recently established nano-electrospray ionization quadrupole time-of-flight tandem-mass spectrometry approach	906:1016	O-Fucosylation sites were determined by a recently established nano-electrospray ionization quadrupole time-of-flight tandem-mass spectrometry approach.
12096136	1	5	theme	further	158:164	arg1	modification					175:186	further covalent modification	158:186	further covalent modification	158:186	The final chemical structure of a newly synthesized protein is often only attained after further covalent modification.
12096136	6	6	theme	ionization	947:956	arg1	approach					1009:1016	a recently established nano-electrospray ionization quadrupole time-of-flight tandem-mass spectrometry approach	906:1016	a recently established nano-electrospray ionization quadrupole time-of-flight tandem-mass spectrometry approach	906:1016	O-Fucosylation sites were determined by a recently established nano-electrospray ionization quadrupole time-of-flight tandem-mass spectrometry approach.
12096136	6	7	theme	nano-electrospray	929:945	arg1	approach					1009:1016	a recently established nano-electrospray ionization quadrupole time-of-flight tandem-mass spectrometry approach	906:1016	a recently established nano-electrospray ionization quadrupole time-of-flight tandem-mass spectrometry approach	906:1016	O-Fucosylation sites were determined by a recently established nano-electrospray ionization quadrupole time-of-flight tandem-mass spectrometry approach.
12096136	3	8	theme	glycosylation	466:478	arg1	O-fucosylation					506:519	O-fucosylation	506:519	O-fucosylation	506:519	Here we present two recently discovered, unusual forms of protein glycosylation, i.e. C-mannosylation and O-fucosylation.
12096136	3	8	theme	glycosylation	466:478	arg1	forms					449:453	two recently discovered, unusual forms	416:453	two recently discovered, unusual forms of protein glycosylation	416:478	Here we present two recently discovered, unusual forms of protein glycosylation, i.e. C-mannosylation and O-fucosylation.
12096136	3	8	theme	glycosylation	466:478	arg1	C-mannosylation					486:500	C-mannosylation	486:500	C-mannosylation	486:500	Here we present two recently discovered, unusual forms of protein glycosylation, i.e. C-mannosylation and O-fucosylation.
12096136	4	9	theme	protein	689:695	arg1	F-spondin					697:705	the recombinant axonal guidance protein F-spondin	657:705	the recombinant axonal guidance protein F-spondin	657:705	Their analysis by a combined mass spectrometric approach is illustrated with peptides from the thrombospondin type 1 repeats (TSRs) of the recombinant axonal guidance protein F-spondin.
12096136	2	10	theme	modifications	334:346	arg1	range					316:320	the range	312:320	the range of possible modifications	312:346	Ideally, a comprehensive proteome analysis includes this aspect, a task that is complicated by our incomplete knowledge of the range of possible modifications and often by the lack of suitable analysis methods.
12096136	5	11	gly	C-mannosylated	850:863	arg1	residues					812:819	eight of ten Trp residues	795:819	eight of ten Trp residues in the TSRs of F-spondin	795:844	Nano-electrospray ionization tandem-mass spectrometry of isolated peptides showed that eight of ten Trp residues in the TSRs of F-spondin are C-mannosylated.
12096136	1	12	theme	final	73:77	arg1	structure					88:96	The final chemical structure	69:96	The final chemical structure of a newly synthesized protein	69:127	The final chemical structure of a newly synthesized protein is often only attained after further covalent modification.
12096136	7	13	from	Hex-dHex-O-Ser/Thr	1060:1077	arg1	proximity					1088:1096	close proximity	1082:1096	close proximity to the C-mannosylation sites	1082:1125	Four of five TSRs carry the disaccharide Hex-dHex-O-Ser/Thr in close proximity to the C-mannosylation sites.
12096136	1	14	theme	covalent	166:173	arg1	modification					175:186	further covalent modification	158:186	further covalent modification	158:186	The final chemical structure of a newly synthesized protein is often only attained after further covalent modification.
12096136	5	15	theme	peptides	774:781	arg1	spectrometry					749:760	Nano-electrospray ionization tandem-mass spectrometry	708:760	Nano-electrospray ionization tandem-mass spectrometry of isolated peptides	708:781	Nano-electrospray ionization tandem-mass spectrometry of isolated peptides showed that eight of ten Trp residues in the TSRs of F-spondin are C-mannosylated.
12096136	1	16	theme	chemical	79:86	arg1	structure					88:96	The final chemical structure	69:96	The final chemical structure of a newly synthesized protein	69:127	The final chemical structure of a newly synthesized protein is often only attained after further covalent modification.
12096136	2	17	theme	suitable	373:380	arg1	methods					391:397	suitable analysis methods	373:397	suitable analysis methods	373:397	Ideally, a comprehensive proteome analysis includes this aspect, a task that is complicated by our incomplete knowledge of the range of possible modifications and often by the lack of suitable analysis methods.
12096136	4	18	theme	spectrometric	556:568	arg1	approach					570:577	a combined mass spectrometric approach	540:577	a combined mass spectrometric approach	540:577	Their analysis by a combined mass spectrometric approach is illustrated with peptides from the thrombospondin type 1 repeats (TSRs) of the recombinant axonal guidance protein F-spondin.
12096136	6	19	theme	established	917:927	arg1	approach					1009:1016	a recently established nano-electrospray ionization quadrupole time-of-flight tandem-mass spectrometry approach	906:1016	a recently established nano-electrospray ionization quadrupole time-of-flight tandem-mass spectrometry approach	906:1016	O-Fucosylation sites were determined by a recently established nano-electrospray ionization quadrupole time-of-flight tandem-mass spectrometry approach.
12096136	4	20	theme	recombinant	661:671	arg1	F-spondin					697:705	the recombinant axonal guidance protein F-spondin	657:705	the recombinant axonal guidance protein F-spondin	657:705	Their analysis by a combined mass spectrometric approach is illustrated with peptides from the thrombospondin type 1 repeats (TSRs) of the recombinant axonal guidance protein F-spondin.
12096136	4	21	theme	mass	551:554	arg1	approach					570:577	a combined mass spectrometric approach	540:577	a combined mass spectrometric approach	540:577	Their analysis by a combined mass spectrometric approach is illustrated with peptides from the thrombospondin type 1 repeats (TSRs) of the recombinant axonal guidance protein F-spondin.
12096136	6	22	theme	O-Fucosylation	866:879	arg1	sites					881:885	O-Fucosylation sites	866:885	O-Fucosylation sites	866:885	O-Fucosylation sites were determined by a recently established nano-electrospray ionization quadrupole time-of-flight tandem-mass spectrometry approach.
12096136	4	23	theme	combined	542:549	arg1	approach					570:577	a combined mass spectrometric approach	540:577	a combined mass spectrometric approach	540:577	Their analysis by a combined mass spectrometric approach is illustrated with peptides from the thrombospondin type 1 repeats (TSRs) of the recombinant axonal guidance protein F-spondin.
12096136	5	24	theme	F-spondin	836:844	arg1	TSRs					828:831	the TSRs	824:831	the TSRs of F-spondin	824:844	Nano-electrospray ionization tandem-mass spectrometry of isolated peptides showed that eight of ten Trp residues in the TSRs of F-spondin are C-mannosylated.
12096136	5	25	theme	Nano-electrospray	708:724	arg1	spectrometry					749:760	Nano-electrospray ionization tandem-mass spectrometry	708:760	Nano-electrospray ionization tandem-mass spectrometry of isolated peptides	708:781	Nano-electrospray ionization tandem-mass spectrometry of isolated peptides showed that eight of ten Trp residues in the TSRs of F-spondin are C-mannosylated.
12096136	2	26	theme	incomplete	288:297	arg1	knowledge					299:307	our incomplete knowledge	284:307	our incomplete knowledge of the range of possible modifications	284:346	Ideally, a comprehensive proteome analysis includes this aspect, a task that is complicated by our incomplete knowledge of the range of possible modifications and often by the lack of suitable analysis methods.
12096136	4	27	from	repeats	639:645	arg1	peptides					599:606	peptides	599:606	peptides from the thrombospondin type 1 repeats (TSRs) of the recombinant axonal guidance protein F-spondin	599:705	Their analysis by a combined mass spectrometric approach is illustrated with peptides from the thrombospondin type 1 repeats (TSRs) of the recombinant axonal guidance protein F-spondin.
12096136	0	28	theme	type	53:56	arg1	repeats					60:66	thrombospondin type 1 repeats	38:66	thrombospondin type 1 repeats	38:66	C-mannosylation and o-fucosylation of thrombospondin type 1 repeats.
12096136	2	29	theme	possible	325:332	arg1	modifications					334:346	possible modifications	325:346	possible modifications	325:346	Ideally, a comprehensive proteome analysis includes this aspect, a task that is complicated by our incomplete knowledge of the range of possible modifications and often by the lack of suitable analysis methods.
12096136	5	30	theme	ionization	726:735	arg1	spectrometry					749:760	Nano-electrospray ionization tandem-mass spectrometry	708:760	Nano-electrospray ionization tandem-mass spectrometry of isolated peptides	708:781	Nano-electrospray ionization tandem-mass spectrometry of isolated peptides showed that eight of ten Trp residues in the TSRs of F-spondin are C-mannosylated.
12096136	0	31	gly	C-mannosylation	0:14	arg1	repeats					60:66	thrombospondin type 1 repeats	38:66	thrombospondin type 1 repeats	38:66	C-mannosylation and o-fucosylation of thrombospondin type 1 repeats.
12096136	0	32	theme	thrombospondin	38:51	arg1	repeats					60:66	thrombospondin type 1 repeats	38:66	thrombospondin type 1 repeats	38:66	C-mannosylation and o-fucosylation of thrombospondin type 1 repeats.
12096136	5	33	theme	Trp	808:810	arg1	residues					812:819	eight of ten Trp residues	795:819	eight of ten Trp residues in the TSRs of F-spondin	795:844	Nano-electrospray ionization tandem-mass spectrometry of isolated peptides showed that eight of ten Trp residues in the TSRs of F-spondin are C-mannosylated.
12096136	9	34	theme	current	1204:1210	arg1	knowledge					1212:1220	Our current knowledge	1200:1220	Our current knowledge of these glycosylations	1200:1244	Our current knowledge of these glycosylations will be discussed.
12096136	2	35	theme	methods	391:397	arg1	lack					365:368	the lack	361:368	the lack of suitable analysis methods	361:397	Ideally, a comprehensive proteome analysis includes this aspect, a task that is complicated by our incomplete knowledge of the range of possible modifications and often by the lack of suitable analysis methods.
12096136	0	36	theme	repeats	60:66	arg1	o-fucosylation					20:33	o-fucosylation	20:33	o-fucosylation	20:33	C-mannosylation and o-fucosylation of thrombospondin type 1 repeats.
12096136	0	36	theme	repeats	60:66	arg1	C-mannosylation					0:14	C-mannosylation	0:14	C-mannosylation	0:14	C-mannosylation and o-fucosylation of thrombospondin type 1 repeats.
12096136	8	37	dep	thrombospondin-1	1142:1157	arg1	analogy					1131:1137	analogy	1131:1137	analogy	1131:1137	In analogy to thrombospondin-1, we assume this to be Glc-Fuc-O-Ser/Thr.
12096136	0	38	gly	o-fucosylation	20:33	arg1	repeats					60:66	thrombospondin type 1 repeats	38:66	thrombospondin type 1 repeats	38:66	C-mannosylation and o-fucosylation of thrombospondin type 1 repeats.
12096136	1	39	theme	synthesized	109:119	arg1	protein					121:127	a newly synthesized protein	101:127	a newly synthesized protein	101:127	The final chemical structure of a newly synthesized protein is often only attained after further covalent modification.
12096136	5	40	theme	tandem-mass	737:747	arg1	spectrometry					749:760	Nano-electrospray ionization tandem-mass spectrometry	708:760	Nano-electrospray ionization tandem-mass spectrometry of isolated peptides	708:781	Nano-electrospray ionization tandem-mass spectrometry of isolated peptides showed that eight of ten Trp residues in the TSRs of F-spondin are C-mannosylated.
12096136	6	41	theme	tandem-mass	984:994	arg1	approach					1009:1016	a recently established nano-electrospray ionization quadrupole time-of-flight tandem-mass spectrometry approach	906:1016	a recently established nano-electrospray ionization quadrupole time-of-flight tandem-mass spectrometry approach	906:1016	O-Fucosylation sites were determined by a recently established nano-electrospray ionization quadrupole time-of-flight tandem-mass spectrometry approach.
12096136	2	42	theme	proteome	214:221	arg1	analysis					223:230	a comprehensive proteome analysis	198:230	a comprehensive proteome analysis	198:230	Ideally, a comprehensive proteome analysis includes this aspect, a task that is complicated by our incomplete knowledge of the range of possible modifications and often by the lack of suitable analysis methods.
12096136	3	43	dep	discovered	429:438	arg1	unusual					441:447	unusual	441:447	unusual	441:447	Here we present two recently discovered, unusual forms of protein glycosylation, i.e. C-mannosylation and O-fucosylation.
12096136	7	44	theme	close	1082:1086	arg1	proximity					1088:1096	close proximity	1082:1096	close proximity to the C-mannosylation sites	1082:1125	Four of five TSRs carry the disaccharide Hex-dHex-O-Ser/Thr in close proximity to the C-mannosylation sites.
12096136	1	45	theme	protein	121:127	arg1	structure					88:96	The final chemical structure	69:96	The final chemical structure of a newly synthesized protein	69:127	The final chemical structure of a newly synthesized protein is often only attained after further covalent modification.
12096136	6	46	theme	spectrometry	996:1007	arg1	approach					1009:1016	a recently established nano-electrospray ionization quadrupole time-of-flight tandem-mass spectrometry approach	906:1016	a recently established nano-electrospray ionization quadrupole time-of-flight tandem-mass spectrometry approach	906:1016	O-Fucosylation sites were determined by a recently established nano-electrospray ionization quadrupole time-of-flight tandem-mass spectrometry approach.
12096136	7	47	theme	C-mannosylation	1105:1119	arg1	sites					1121:1125	the C-mannosylation sites	1101:1125	the C-mannosylation sites	1101:1125	Four of five TSRs carry the disaccharide Hex-dHex-O-Ser/Thr in close proximity to the C-mannosylation sites.
12096136	2	48	theme	comprehensive	200:212	arg1	analysis					223:230	a comprehensive proteome analysis	198:230	a comprehensive proteome analysis	198:230	Ideally, a comprehensive proteome analysis includes this aspect, a task that is complicated by our incomplete knowledge of the range of possible modifications and often by the lack of suitable analysis methods.
12096136	3	49	theme	protein	458:464	arg1	glycosylation					466:478	protein glycosylation	458:478	protein glycosylation	458:478	Here we present two recently discovered, unusual forms of protein glycosylation, i.e. C-mannosylation and O-fucosylation.
12096136	5	50	theme	isolated	765:772	arg1	peptides					774:781	isolated peptides	765:781	isolated peptides	765:781	Nano-electrospray ionization tandem-mass spectrometry of isolated peptides showed that eight of ten Trp residues in the TSRs of F-spondin are C-mannosylated.
12096136	9	51	theme	glycosylations	1231:1244	arg1	knowledge					1212:1220	Our current knowledge	1200:1220	Our current knowledge of these glycosylations	1200:1244	Our current knowledge of these glycosylations will be discussed.
12096136	2	52	theme	range	316:320	arg1	knowledge					299:307	our incomplete knowledge	284:307	our incomplete knowledge of the range of possible modifications	284:346	Ideally, a comprehensive proteome analysis includes this aspect, a task that is complicated by our incomplete knowledge of the range of possible modifications and often by the lack of suitable analysis methods.
12096136	7	53	gly	C-mannosylation	1105:1119	arg2	sites					1121:1125	the C-mannosylation sites	1101:1125	the C-mannosylation sites	1101:1125	Four of five TSRs carry the disaccharide Hex-dHex-O-Ser/Thr in close proximity to the C-mannosylation sites.
12096136	3	54	dep	forms	449:453	arg1	forms					449:453	two recently discovered, unusual forms	416:453	two recently discovered, unusual forms of protein glycosylation	416:478	Here we present two recently discovered, unusual forms of protein glycosylation, i.e. C-mannosylation and O-fucosylation.
12096136	3	54	dep	forms	449:453	arg1	O-fucosylation					506:519	O-fucosylation	506:519	O-fucosylation	506:519	Here we present two recently discovered, unusual forms of protein glycosylation, i.e. C-mannosylation and O-fucosylation.
12096136	3	54	dep	forms	449:453	arg1	C-mannosylation					486:500	C-mannosylation	486:500	C-mannosylation	486:500	Here we present two recently discovered, unusual forms of protein glycosylation, i.e. C-mannosylation and O-fucosylation.
12096136	4	55	theme	guidance	680:687	arg1	F-spondin					697:705	the recombinant axonal guidance protein F-spondin	657:705	the recombinant axonal guidance protein F-spondin	657:705	Their analysis by a combined mass spectrometric approach is illustrated with peptides from the thrombospondin type 1 repeats (TSRs) of the recombinant axonal guidance protein F-spondin.
12096136	3	56	theme	discovered	429:438	arg1	O-fucosylation					506:519	O-fucosylation	506:519	O-fucosylation	506:519	Here we present two recently discovered, unusual forms of protein glycosylation, i.e. C-mannosylation and O-fucosylation.
12096136	3	56	theme	discovered	429:438	arg1	forms					449:453	two recently discovered, unusual forms	416:453	two recently discovered, unusual forms of protein glycosylation	416:478	Here we present two recently discovered, unusual forms of protein glycosylation, i.e. C-mannosylation and O-fucosylation.
12096136	3	56	theme	discovered	429:438	arg1	C-mannosylation					486:500	C-mannosylation	486:500	C-mannosylation	486:500	Here we present two recently discovered, unusual forms of protein glycosylation, i.e. C-mannosylation and O-fucosylation.
12096136	4	57	theme	type	632:635	arg1	TSRs					648:651	TSRs	648:651	TSRs	648:651	Their analysis by a combined mass spectrometric approach is illustrated with peptides from the thrombospondin type 1 repeats (TSRs) of the recombinant axonal guidance protein F-spondin.
12096136	4	57	theme	type	632:635	arg1	repeats					639:645	the thrombospondin type 1 repeats	613:645	the thrombospondin type 1 repeats (TSRs) of the recombinant axonal guidance protein F-spondin	613:705	Their analysis by a combined mass spectrometric approach is illustrated with peptides from the thrombospondin type 1 repeats (TSRs) of the recombinant axonal guidance protein F-spondin.
12096136	7	58	contain	carry	1037:1041	arg1	TSRs					1032:1035	Four of five TSRs	1019:1035	Four of five TSRs	1019:1035	Four of five TSRs carry the disaccharide Hex-dHex-O-Ser/Thr in close proximity to the C-mannosylation sites.
12096136	7	58	contain	carry	1037:1041	arg2	Hex-dHex-O-Ser/Thr					1060:1077	the disaccharide Hex-dHex-O-Ser/Thr	1043:1077	the disaccharide Hex-dHex-O-Ser/Thr in close proximity to the C-mannosylation sites	1043:1125	Four of five TSRs carry the disaccharide Hex-dHex-O-Ser/Thr in close proximity to the C-mannosylation sites.
12096136	5	59	from	residues	812:819	arg1	TSRs					828:831	the TSRs	824:831	the TSRs of F-spondin	824:844	Nano-electrospray ionization tandem-mass spectrometry of isolated peptides showed that eight of ten Trp residues in the TSRs of F-spondin are C-mannosylated.
12096136	4	60	theme	axonal	673:678	arg1	F-spondin					697:705	the recombinant axonal guidance protein F-spondin	657:705	the recombinant axonal guidance protein F-spondin	657:705	Their analysis by a combined mass spectrometric approach is illustrated with peptides from the thrombospondin type 1 repeats (TSRs) of the recombinant axonal guidance protein F-spondin.
12096136	4	61	theme	thrombospondin	617:630	arg1	TSRs					648:651	TSRs	648:651	TSRs	648:651	Their analysis by a combined mass spectrometric approach is illustrated with peptides from the thrombospondin type 1 repeats (TSRs) of the recombinant axonal guidance protein F-spondin.
12096136	4	61	theme	thrombospondin	617:630	arg1	repeats					639:645	the thrombospondin type 1 repeats	613:645	the thrombospondin type 1 repeats (TSRs) of the recombinant axonal guidance protein F-spondin	613:705	Their analysis by a combined mass spectrometric approach is illustrated with peptides from the thrombospondin type 1 repeats (TSRs) of the recombinant axonal guidance protein F-spondin.
12847106	8	0	theme	potential	1033:1041	arg1	implications					1043:1054	potential implications	1033:1054	potential implications for understanding the roles of plakoglobin	1033:1097	This finding has potential implications for understanding the roles of plakoglobin.
12847106	1	1	theme	classical	152:160	arg1	cadherins					162:170	desmosomal and classical cadherins	137:170	cadherins	162:170	Plakoglobin provides a key linkage in protein chains that connect desmosomal and classical cadherins to the cytoskeleton.
12847106	8	2	theme	plakoglobin	1087:1097	arg1	roles					1078:1082	the roles	1074:1082	the roles of plakoglobin	1074:1097	This finding has potential implications for understanding the roles of plakoglobin.
12847106	6	3	theme	destruction	781:791	arg1	box					793:795	the destruction box	777:795	the destruction box	777:795	We report that plakoglobin is modified by the addition of O-GlcNAc at a single site in close proximity to the destruction box.
12847106	2	4	theme	partner	337:343	arg1	proteins					345:352	partner proteins	337:352	partner proteins of beta-catenin	337:368	It is also present in a significant cytosolic pool that has the capacity to impact on canonical Wnt signaling by competing for interaction with partner proteins of beta-catenin.
12847106	5	5	located	found	624:628	arg2	box					612:614	This destruction box	595:614	This destruction box	595:614	This destruction box is also found in the N-terminal domain of plakoglobin.
12847106	5	5	located	found	624:628	arg1	plakoglobin					658:668	plakoglobin	658:668	plakoglobin	658:668	This destruction box is also found in the N-terminal domain of plakoglobin.
12847106	5	5	located	found	624:628	arg1	domain					648:653	the N-terminal domain	633:653	the N-terminal domain of plakoglobin	633:668	This destruction box is also found in the N-terminal domain of plakoglobin.
12847106	5	6	theme	N-terminal	637:646	arg1	plakoglobin					658:668	plakoglobin	658:668	plakoglobin	658:668	This destruction box is also found in the N-terminal domain of plakoglobin.
12847106	5	6	theme	N-terminal	637:646	arg1	domain					648:653	the N-terminal domain	633:653	the N-terminal domain of plakoglobin	633:668	This destruction box is also found in the N-terminal domain of plakoglobin.
12847106	7	7	from	degradation	905:915	arg1	protection					877:886	protection	877:886	protection from proteasomal degradation	877:915	O-GlcNAc modification has been proposed to counteract phosphorylation, provide protection from proteasomal degradation, mediate signal transduction, silence transcription, and regulate multimolecular protein assembly.
12847106	2	8	contain	has	249:251	arg2	capacity					257:264	the capacity	253:264	the capacity to impact on canonical Wnt signaling	253:301	It is also present in a significant cytosolic pool that has the capacity to impact on canonical Wnt signaling by competing for interaction with partner proteins of beta-catenin.
12847106	2	8	contain	has	249:251	arg1	pool					239:242	a significant cytosolic pool	215:242	a significant cytosolic pool that has the capacity to impact on canonical Wnt signaling by competing for interaction with partner proteins of beta-catenin	215:368	It is also present in a significant cytosolic pool that has the capacity to impact on canonical Wnt signaling by competing for interaction with partner proteins of beta-catenin.
12847106	3	9	theme	box	499:501	arg1	"					502:502	a "destruction box"	484:502	a "destruction box" within the N-terminal domain	484:531	The closely related protein, beta-catenin, is rapidly targeted for proteasomal degradation by phosphorylation of a "destruction box" within the N-terminal domain.
12847106	2	10	from	present	204:210	arg1	pool					239:242	a significant cytosolic pool	215:242	a significant cytosolic pool that has the capacity to impact on canonical Wnt signaling by competing for interaction with partner proteins of beta-catenin	215:368	It is also present in a significant cytosolic pool that has the capacity to impact on canonical Wnt signaling by competing for interaction with partner proteins of beta-catenin.
12847106	5	11	theme	destruction	600:610	arg1	box					612:614	This destruction box	595:614	This destruction box	595:614	This destruction box is also found in the N-terminal domain of plakoglobin.
12847106	3	12	theme	N-terminal	515:524	arg1	domain					526:531	the N-terminal domain	511:531	the N-terminal domain	511:531	The closely related protein, beta-catenin, is rapidly targeted for proteasomal degradation by phosphorylation of a "destruction box" within the N-terminal domain.
12847106	6	13	theme	close	758:762	arg1	proximity					764:772	close proximity	758:772	close proximity to the destruction box	758:795	We report that plakoglobin is modified by the addition of O-GlcNAc at a single site in close proximity to the destruction box.
12847106	2	14	attach	present	204:210	arg2	It					193:194	It	193:194	It	193:194	It is also present in a significant cytosolic pool that has the capacity to impact on canonical Wnt signaling by competing for interaction with partner proteins of beta-catenin.
12847106	2	14	attach	present	204:210	arg1	pool					239:242	a significant cytosolic pool	215:242	a significant cytosolic pool that has the capacity to impact on canonical Wnt signaling by competing for interaction with partner proteins of beta-catenin	215:368	It is also present in a significant cytosolic pool that has the capacity to impact on canonical Wnt signaling by competing for interaction with partner proteins of beta-catenin.
12847106	6	15	mod	modified	701:708	arg1	plakoglobin					686:696	plakoglobin	686:696	plakoglobin	686:696	We report that plakoglobin is modified by the addition of O-GlcNAc at a single site in close proximity to the destruction box.
12847106	6	15	mod	modified	701:708	arg3	addition					717:724	the addition	713:724	the addition of O-GlcNAc at a single site in close proximity to the destruction box	713:795	We report that plakoglobin is modified by the addition of O-GlcNAc at a single site in close proximity to the destruction box.
12847106	5	16	theme	plakoglobin	658:668	arg1	plakoglobin					658:668	plakoglobin	658:668	plakoglobin	658:668	This destruction box is also found in the N-terminal domain of plakoglobin.
12847106	5	16	theme	plakoglobin	658:668	arg1	domain					648:653	the N-terminal domain	633:653	the N-terminal domain of plakoglobin	633:668	This destruction box is also found in the N-terminal domain of plakoglobin.
12847106	3	17	theme	related	383:389	arg1	beta-catenin					400:411	beta-catenin	400:411	beta-catenin	400:411	The closely related protein, beta-catenin, is rapidly targeted for proteasomal degradation by phosphorylation of a "destruction box" within the N-terminal domain.
12847106	3	17	theme	related	383:389	arg1	protein					391:397	The closely related protein	371:397	The closely related protein	371:397	The closely related protein, beta-catenin, is rapidly targeted for proteasomal degradation by phosphorylation of a "destruction box" within the N-terminal domain.
12847106	1	18	theme	key	94:96	arg1	linkage					98:104	a key linkage	92:104	a key linkage in protein chains that connect desmosomal and classical cadherins to the cytoskeleton	92:190	Plakoglobin provides a key linkage in protein chains that connect desmosomal and classical cadherins to the cytoskeleton.
12847106	7	19	theme	O-GlcNAc	798:805	arg1	modification					807:818	O-GlcNAc modification	798:818	O-GlcNAc modification	798:818	O-GlcNAc modification has been proposed to counteract phosphorylation, provide protection from proteasomal degradation, mediate signal transduction, silence transcription, and regulate multimolecular protein assembly.
12847106	6	20	theme	single	743:748	arg1	site					750:753	a single site	741:753	a single site in close proximity to the destruction box	741:795	We report that plakoglobin is modified by the addition of O-GlcNAc at a single site in close proximity to the destruction box.
12847106	2	21	theme	Wnt	289:291	arg1	signaling					293:301	canonical Wnt signaling	279:301	canonical Wnt signaling	279:301	It is also present in a significant cytosolic pool that has the capacity to impact on canonical Wnt signaling by competing for interaction with partner proteins of beta-catenin.
12847106	2	22	from	pool	239:242	arg1	present					204:210	present	204:210	present	204:210	It is also present in a significant cytosolic pool that has the capacity to impact on canonical Wnt signaling by competing for interaction with partner proteins of beta-catenin.
12847106	6	23	from	site	750:753	arg1	addition					717:724	the addition	713:724	the addition of O-GlcNAc at a single site in close proximity to the destruction box	713:795	We report that plakoglobin is modified by the addition of O-GlcNAc at a single site in close proximity to the destruction box.
12847106	6	23	from	site	750:753	arg1	proximity					764:772	close proximity	758:772	close proximity to the destruction box	758:795	We report that plakoglobin is modified by the addition of O-GlcNAc at a single site in close proximity to the destruction box.
12847106	6	24	theme	O-GlcNAc	729:736	arg1	addition					717:724	the addition	713:724	the addition of O-GlcNAc at a single site in close proximity to the destruction box	713:795	We report that plakoglobin is modified by the addition of O-GlcNAc at a single site in close proximity to the destruction box.
12847106	2	25	theme	canonical	279:287	arg1	signaling					293:301	canonical Wnt signaling	279:301	canonical Wnt signaling	279:301	It is also present in a significant cytosolic pool that has the capacity to impact on canonical Wnt signaling by competing for interaction with partner proteins of beta-catenin.
12847106	1	26	theme	desmosomal	137:146	arg1	cadherins					162:170	desmosomal and classical cadherins	137:170	cadherins	162:170	Plakoglobin provides a key linkage in protein chains that connect desmosomal and classical cadherins to the cytoskeleton.
12847106	4	27	theme	process	553:559	arg1	Inhibition					534:543	Inhibition	534:543	Inhibition of this process	534:559	Inhibition of this process forms the basis of Wnt signaling.
12847106	8	28	contain	has	1029:1031	arg2	implications					1043:1054	potential implications	1033:1054	potential implications for understanding the roles of plakoglobin	1033:1097	This finding has potential implications for understanding the roles of plakoglobin.
12847106	8	28	contain	has	1029:1031	arg1	finding					1021:1027	This finding	1016:1027	This finding	1016:1027	This finding has potential implications for understanding the roles of plakoglobin.
12847106	2	29	theme	cytosolic	229:237	arg1	pool					239:242	a significant cytosolic pool	215:242	a significant cytosolic pool that has the capacity to impact on canonical Wnt signaling by competing for interaction with partner proteins of beta-catenin	215:368	It is also present in a significant cytosolic pool that has the capacity to impact on canonical Wnt signaling by competing for interaction with partner proteins of beta-catenin.
12847106	3	30	theme	proteasomal	438:448	arg1	degradation					450:460	proteasomal degradation	438:460	proteasomal degradation	438:460	The closely related protein, beta-catenin, is rapidly targeted for proteasomal degradation by phosphorylation of a "destruction box" within the N-terminal domain.
12847106	7	31	theme	proteasomal	893:903	arg1	degradation					905:915	proteasomal degradation	893:915	proteasomal degradation	893:915	O-GlcNAc modification has been proposed to counteract phosphorylation, provide protection from proteasomal degradation, mediate signal transduction, silence transcription, and regulate multimolecular protein assembly.
12847106	2	32	theme	significant	217:227	arg1	pool					239:242	a significant cytosolic pool	215:242	a significant cytosolic pool that has the capacity to impact on canonical Wnt signaling by competing for interaction with partner proteins of beta-catenin	215:368	It is also present in a significant cytosolic pool that has the capacity to impact on canonical Wnt signaling by competing for interaction with partner proteins of beta-catenin.
12847106	0	33	theme	destruction	54:64	arg1	box					66:68	the N-terminal destruction box	39:68	the N-terminal destruction box	39:68	Plakoglobin is O-glycosylated close to the N-terminal destruction box.
12847106	2	34	with	interaction	320:330	arg1	proteins					345:352	partner proteins	337:352	partner proteins of beta-catenin	337:368	It is also present in a significant cytosolic pool that has the capacity to impact on canonical Wnt signaling by competing for interaction with partner proteins of beta-catenin.
12847106	0	35	gly	O-glycosylated	15:28	arg1	Plakoglobin					0:10	Plakoglobin	0:10	Plakoglobin	0:10	Plakoglobin is O-glycosylated close to the N-terminal destruction box.
12847106	1	36	theme	protein	109:115	arg1	chains					117:122	protein chains	109:122	protein chains that connect desmosomal and classical cadherins to the cytoskeleton	109:190	Plakoglobin provides a key linkage in protein chains that connect desmosomal and classical cadherins to the cytoskeleton.
12847106	0	37	theme	N-terminal	43:52	arg1	box					66:68	the N-terminal destruction box	39:68	the N-terminal destruction box	39:68	Plakoglobin is O-glycosylated close to the N-terminal destruction box.
12847106	2	38	located	present	204:210	arg2	It					193:194	It	193:194	It	193:194	It is also present in a significant cytosolic pool that has the capacity to impact on canonical Wnt signaling by competing for interaction with partner proteins of beta-catenin.
12847106	2	38	located	present	204:210	arg1	pool					239:242	a significant cytosolic pool	215:242	a significant cytosolic pool that has the capacity to impact on canonical Wnt signaling by competing for interaction with partner proteins of beta-catenin	215:368	It is also present in a significant cytosolic pool that has the capacity to impact on canonical Wnt signaling by competing for interaction with partner proteins of beta-catenin.
12847106	3	39	theme	"	502:502	arg1	phosphorylation					465:479	phosphorylation	465:479	phosphorylation of a "destruction box" within the N-terminal domain	465:531	The closely related protein, beta-catenin, is rapidly targeted for proteasomal degradation by phosphorylation of a "destruction box" within the N-terminal domain.
12847106	3	40	theme	destruction	487:497	arg1	"					502:502	a "destruction box"	484:502	a "destruction box" within the N-terminal domain	484:531	The closely related protein, beta-catenin, is rapidly targeted for proteasomal degradation by phosphorylation of a "destruction box" within the N-terminal domain.
12847106	1	41	from	linkage	98:104	arg1	chains					117:122	protein chains	109:122	protein chains that connect desmosomal and classical cadherins to the cytoskeleton	109:190	Plakoglobin provides a key linkage in protein chains that connect desmosomal and classical cadherins to the cytoskeleton.
12847106	7	42	theme	signal	926:931	arg1	transduction					933:944	signal transduction	926:944	signal transduction	926:944	O-GlcNAc modification has been proposed to counteract phosphorylation, provide protection from proteasomal degradation, mediate signal transduction, silence transcription, and regulate multimolecular protein assembly.
12847106	7	43	theme	multimolecular	983:996	arg1	assembly					1006:1013	multimolecular protein assembly	983:1013	multimolecular protein assembly	983:1013	O-GlcNAc modification has been proposed to counteract phosphorylation, provide protection from proteasomal degradation, mediate signal transduction, silence transcription, and regulate multimolecular protein assembly.
12847106	4	44	theme	signaling	584:592	arg1	basis					571:575	the basis	567:575	the basis of Wnt signaling	567:592	Inhibition of this process forms the basis of Wnt signaling.
12847106	7	45	theme	protein	998:1004	arg1	assembly					1006:1013	multimolecular protein assembly	983:1013	multimolecular protein assembly	983:1013	O-GlcNAc modification has been proposed to counteract phosphorylation, provide protection from proteasomal degradation, mediate signal transduction, silence transcription, and regulate multimolecular protein assembly.
12847106	2	46	theme	beta-catenin	357:368	arg1	proteins					345:352	partner proteins	337:352	partner proteins of beta-catenin	337:368	It is also present in a significant cytosolic pool that has the capacity to impact on canonical Wnt signaling by competing for interaction with partner proteins of beta-catenin.
12847106	2	47	from	impact	269:274	arg1	signaling					293:301	canonical Wnt signaling	279:301	canonical Wnt signaling	279:301	It is also present in a significant cytosolic pool that has the capacity to impact on canonical Wnt signaling by competing for interaction with partner proteins of beta-catenin.
12847106	4	48	theme	Wnt	580:582	arg1	signaling					584:592	Wnt signaling	580:592	Wnt signaling	580:592	Inhibition of this process forms the basis of Wnt signaling.
22279061	12	0	theme	atherogenesis	1970:1982	arg1	development					1955:1965	the development	1951:1965	the development of atherogenesis	1951:1982	These data indicate that Asn(289)-, Asn(382)- and Asn(393)-linked N-glycans of SREC-I have distinct functions in regulating proteolytic resistance, ligand-binding affinity and subcellular localization, all of which might be involved in the development of atherogenesis.
22279061	12	1	theme	ligand-binding	1863:1876	arg1	affinity					1878:1885	ligand-binding affinity	1863:1885	ligand-binding affinity	1863:1885	These data indicate that Asn(289)-, Asn(382)- and Asn(393)-linked N-glycans of SREC-I have distinct functions in regulating proteolytic resistance, ligand-binding affinity and subcellular localization, all of which might be involved in the development of atherogenesis.
22279061	4	2	theme	cellular	826:833	arg1	incorporation					835:847	the cellular incorporation	822:847	the cellular incorporation of Ac-LDL	822:857	N382Q/N393Q and N289Q/N382Q/N393Q were sequestered in the endoplasmic reticulum, resulting in a severe reduction in the cellular incorporation of Ac-LDL.
22279061	1	3	theme	Scavenger	135:143	arg1	receptor					145:152	Scavenger receptor	135:152	Scavenger receptor expressed by endothelial cells (SREC-I)	135:192	Scavenger receptor expressed by endothelial cells (SREC-I) mediates the endocytosis of chemically modified lipoproteins such as acetylated low-density lipoprotein (Ac-LDL) and oxidized LDL and is implicated in atherogenesis.
22279061	1	4	theme	modified	233:240	arg1	lipoprotein					286:296	acetylated low-density lipoprotein	263:296	acetylated low-density lipoprotein (Ac-LDL)	263:305	Scavenger receptor expressed by endothelial cells (SREC-I) mediates the endocytosis of chemically modified lipoproteins such as acetylated low-density lipoprotein (Ac-LDL) and oxidized LDL and is implicated in atherogenesis.
22279061	1	4	theme	modified	233:240	arg1	lipoproteins					242:253	chemically modified lipoproteins	222:253	chemically modified lipoproteins such as acetylated low-density lipoprotein (Ac-LDL) and oxidized LDL	222:322	Scavenger receptor expressed by endothelial cells (SREC-I) mediates the endocytosis of chemically modified lipoproteins such as acetylated low-density lipoprotein (Ac-LDL) and oxidized LDL and is implicated in atherogenesis.
22279061	1	4	theme	modified	233:240	arg1	LDL					320:322	oxidized LDL	311:322	oxidized LDL	311:322	Scavenger receptor expressed by endothelial cells (SREC-I) mediates the endocytosis of chemically modified lipoproteins such as acetylated low-density lipoprotein (Ac-LDL) and oxidized LDL and is implicated in atherogenesis.
22279061	12	5	theme	subcellular	1891:1901	arg1	localization					1903:1914	subcellular localization	1891:1914	subcellular localization	1891:1914	These data indicate that Asn(289)-, Asn(382)- and Asn(393)-linked N-glycans of SREC-I have distinct functions in regulating proteolytic resistance, ligand-binding affinity and subcellular localization, all of which might be involved in the development of atherogenesis.
22279061	1	6	theme	lipoproteins	242:253	arg1	endocytosis					207:217	the endocytosis	203:217	the endocytosis of chemically modified lipoproteins such as acetylated low-density lipoprotein (Ac-LDL) and oxidized LDL	203:322	Scavenger receptor expressed by endothelial cells (SREC-I) mediates the endocytosis of chemically modified lipoproteins such as acetylated low-density lipoprotein (Ac-LDL) and oxidized LDL and is implicated in atherogenesis.
22279061	11	7	theme	homology	1542:1549	arg1	modeling					1551:1558	homology modeling	1542:1558	homology modeling of SREC-I	1542:1568	Structural analyses and homology modeling of SREC-I suggest that the N-glycan bearing a β1-6GlcNAc branch at Asn(289) protects from proteinase attack and thus confers a higher stability on SREC-I.
22279061	9	8	located	detected	1411:1418	arg2	tri-					1381:1384	tri-	1381:1384	tri-	1381:1384	In addition, tri- and tetra-antennary were detected as minor constituents at Asn(289).
22279061	9	8	located	detected	1411:1418	arg1	addition					1371:1378	addition	1371:1378	addition	1371:1378	In addition, tri- and tetra-antennary were detected as minor constituents at Asn(289).
22279061	9	8	located	detected	1411:1418	arg2	constituents					1429:1440	minor constituents	1423:1440	minor constituents at Asn(289)	1423:1452	In addition, tri- and tetra-antennary were detected as minor constituents at Asn(289).
22279061	9	8	located	detected	1411:1418	arg2	tetra-antennary					1390:1404	tetra-antennary	1390:1404	tetra-antennary	1390:1404	In addition, tri- and tetra-antennary were detected as minor constituents at Asn(289).
22279061	6	9	theme	SREC-I	1090:1095	arg1	sorting					1079:1085	the intracellular sorting	1061:1085	the intracellular sorting of SREC-I	1061:1095	These results indicate that the N-glycan of Asn(393) regulates the intracellular sorting of SREC-I and that the N-glycan of Asn(382) controls ligand-binding affinity.
22279061	11	10	theme	proteinase	1650:1659	arg1	attack					1661:1666	proteinase attack	1650:1666	proteinase attack	1650:1666	Structural analyses and homology modeling of SREC-I suggest that the N-glycan bearing a β1-6GlcNAc branch at Asn(289) protects from proteinase attack and thus confers a higher stability on SREC-I.
22279061	0	11	theme	essential	73:81	arg1	role					83:86	essential role	73:86	N-glycans of SREC-I (scavenger receptor expressed by endothelial cells): essential role for ligand binding, trafficking and stability.	0:133	N-glycans of SREC-I (scavenger receptor expressed by endothelial cells): essential role for ligand binding, trafficking and stability.
22279061	3	12	theme	cellular	667:674	arg1	rate					690:693	the cellular incorporation rate	663:693	the cellular incorporation rate of Ac-LDL	663:703	To determine the function of N-glycans in SREC-I, we characterized SREC-I mutant proteins by intracellular distribution and the cellular incorporation rate of Ac-LDL.
22279061	6	13	theme	Asn	1122:1124	arg1	N-glycan					1110:1117	the N-glycan	1106:1117	the N-glycan of Asn(382)	1106:1129	These results indicate that the N-glycan of Asn(393) regulates the intracellular sorting of SREC-I and that the N-glycan of Asn(382) controls ligand-binding affinity.
22279061	8	14	theme	Glycan	1236:1241	arg1	analyses					1253:1260	Glycan structure analyses	1236:1260	Glycan structure analyses	1236:1260	Glycan structure analyses revealed that the core-fucosylated bi-antennary is the common major structure at all glycosylation sites.
22279061	0	15	theme	ligand	92:97	arg1	binding					99:105	ligand binding	92:105	ligand binding	92:105	N-glycans of SREC-I (scavenger receptor expressed by endothelial cells): essential role for ligand binding, trafficking and stability.
22279061	3	16	theme	incorporation	676:688	arg1	rate					690:693	the cellular incorporation rate	663:693	the cellular incorporation rate of Ac-LDL	663:703	To determine the function of N-glycans in SREC-I, we characterized SREC-I mutant proteins by intracellular distribution and the cellular incorporation rate of Ac-LDL.
22279061	4	17	theme	severe	802:807	arg1	reduction					809:817	a severe reduction	800:817	a severe reduction in the cellular incorporation of Ac-LDL	800:857	N382Q/N393Q and N289Q/N382Q/N393Q were sequestered in the endoplasmic reticulum, resulting in a severe reduction in the cellular incorporation of Ac-LDL.
22279061	9	18	theme	minor	1423:1427	arg1	constituents					1429:1440	minor constituents	1423:1440	minor constituents at Asn(289)	1423:1452	In addition, tri- and tetra-antennary were detected as minor constituents at Asn(289).
22279061	9	18	theme	minor	1423:1427	arg1	tetra-antennary					1390:1404	tetra-antennary	1390:1404	tetra-antennary	1390:1404	In addition, tri- and tetra-antennary were detected as minor constituents at Asn(289).
22279061	9	18	theme	minor	1423:1427	arg1	tri-					1381:1384	tri-	1381:1384	tri-	1381:1384	In addition, tri- and tetra-antennary were detected as minor constituents at Asn(289).
22279061	1	19	theme	endothelial	167:177	arg1	SREC-I					186:191	SREC-I	186:191	SREC-I	186:191	Scavenger receptor expressed by endothelial cells (SREC-I) mediates the endocytosis of chemically modified lipoproteins such as acetylated low-density lipoprotein (Ac-LDL) and oxidized LDL and is implicated in atherogenesis.
22279061	1	19	theme	endothelial	167:177	arg1	cells					179:183	endothelial cells	167:183	endothelial cells (SREC-I)	167:192	Scavenger receptor expressed by endothelial cells (SREC-I) mediates the endocytosis of chemically modified lipoproteins such as acetylated low-density lipoprotein (Ac-LDL) and oxidized LDL and is implicated in atherogenesis.
22279061	6	20	theme	Asn	1042:1044	arg1	N-glycan					1030:1037	the N-glycan	1026:1037	the N-glycan of Asn(393)	1026:1049	These results indicate that the N-glycan of Asn(393) regulates the intracellular sorting of SREC-I and that the N-glycan of Asn(382) controls ligand-binding affinity.
22279061	11	21	theme	SREC-I	1563:1568	arg1	modeling					1551:1558	homology modeling	1542:1558	homology modeling of SREC-I	1542:1568	Structural analyses and homology modeling of SREC-I suggest that the N-glycan bearing a β1-6GlcNAc branch at Asn(289) protects from proteinase attack and thus confers a higher stability on SREC-I.
22279061	11	21	theme	SREC-I	1563:1568	arg1	analyses					1529:1536	Structural analyses	1518:1536	Structural analyses	1518:1536	Structural analyses and homology modeling of SREC-I suggest that the N-glycan bearing a β1-6GlcNAc branch at Asn(289) protects from proteinase attack and thus confers a higher stability on SREC-I.
22279061	8	22	gly	glycosylation	1347:1359	arg2	sites					1361:1365	all glycosylation sites	1343:1365	all glycosylation sites	1343:1365	Glycan structure analyses revealed that the core-fucosylated bi-antennary is the common major structure at all glycosylation sites.
22279061	3	23	from	function	556:563	arg1	SREC-I					581:586	SREC-I	581:586	SREC-I	581:586	To determine the function of N-glycans in SREC-I, we characterized SREC-I mutant proteins by intracellular distribution and the cellular incorporation rate of Ac-LDL.
22279061	12	24	link	-linked	1773:1779	arg1	N-glycans					1781:1789	Asn(289)-, Asn(382)- and Asn(393)-linked N-glycans	1740:1789	Asn(289)-, Asn(382)- and Asn(393)-linked N-glycans of SREC-I	1740:1799	These data indicate that Asn(289)-, Asn(382)- and Asn(393)-linked N-glycans of SREC-I have distinct functions in regulating proteolytic resistance, ligand-binding affinity and subcellular localization, all of which might be involved in the development of atherogenesis.
22279061	2	25	theme	potential	446:454	arg1	sites					470:474	three potential glycosylation sites	440:474	three potential glycosylation sites	440:474	We produced recombinant SREC-I in Chinese hamster ovary-K1 cells and identified three potential glycosylation sites, Asn(289), Asn(382) and Asn(393), which were all glycosylated.
22279061	2	25	theme	potential	446:454	arg1	Asn					500:502	Asn(393)	500:507	Asn(393)	500:507	We produced recombinant SREC-I in Chinese hamster ovary-K1 cells and identified three potential glycosylation sites, Asn(289), Asn(382) and Asn(393), which were all glycosylated.
22279061	2	25	theme	potential	446:454	arg1	Asn					487:489	Asn(382)	487:494	Asn(382)	487:494	We produced recombinant SREC-I in Chinese hamster ovary-K1 cells and identified three potential glycosylation sites, Asn(289), Asn(382) and Asn(393), which were all glycosylated.
22279061	2	25	theme	potential	446:454	arg1	Asn					477:479	Asn	477:479	Asn(289)	477:484	We produced recombinant SREC-I in Chinese hamster ovary-K1 cells and identified three potential glycosylation sites, Asn(289), Asn(382) and Asn(393), which were all glycosylated.
22279061	3	26	theme	Ac-LDL	698:703	arg1	rate					690:693	the cellular incorporation rate	663:693	the cellular incorporation rate of Ac-LDL	663:703	To determine the function of N-glycans in SREC-I, we characterized SREC-I mutant proteins by intracellular distribution and the cellular incorporation rate of Ac-LDL.
22279061	3	26	theme	Ac-LDL	698:703	arg1	distribution					646:657	intracellular distribution	632:657	intracellular distribution	632:657	To determine the function of N-glycans in SREC-I, we characterized SREC-I mutant proteins by intracellular distribution and the cellular incorporation rate of Ac-LDL.
22279061	8	27	theme	major	1324:1328	arg1	structure					1330:1338	the common major structure	1313:1338	the common major structure at all glycosylation sites	1313:1365	Glycan structure analyses revealed that the core-fucosylated bi-antennary is the common major structure at all glycosylation sites.
22279061	8	27	theme	major	1324:1328	arg1	bi-antennary					1297:1308	bi-antennary	1297:1308	bi-antennary	1297:1308	Glycan structure analyses revealed that the core-fucosylated bi-antennary is the common major structure at all glycosylation sites.
22279061	4	28	from	reduction	809:817	arg1	incorporation					835:847	the cellular incorporation	822:847	the cellular incorporation of Ac-LDL	822:857	N382Q/N393Q and N289Q/N382Q/N393Q were sequestered in the endoplasmic reticulum, resulting in a severe reduction in the cellular incorporation of Ac-LDL.
22279061	2	29	theme	recombinant	372:382	arg1	SREC-I					384:389	recombinant SREC-I	372:389	recombinant SREC-I in Chinese hamster ovary-K1 cells	372:423	We produced recombinant SREC-I in Chinese hamster ovary-K1 cells and identified three potential glycosylation sites, Asn(289), Asn(382) and Asn(393), which were all glycosylated.
22279061	1	30	theme	acetylated	263:272	arg1	lipoprotein					286:296	acetylated low-density lipoprotein	263:296	acetylated low-density lipoprotein (Ac-LDL)	263:305	Scavenger receptor expressed by endothelial cells (SREC-I) mediates the endocytosis of chemically modified lipoproteins such as acetylated low-density lipoprotein (Ac-LDL) and oxidized LDL and is implicated in atherogenesis.
22279061	1	30	theme	acetylated	263:272	arg1	Ac-LDL					299:304	Ac-LDL	299:304	Ac-LDL	299:304	Scavenger receptor expressed by endothelial cells (SREC-I) mediates the endocytosis of chemically modified lipoproteins such as acetylated low-density lipoprotein (Ac-LDL) and oxidized LDL and is implicated in atherogenesis.
22279061	11	31	from	stability	1694:1702	arg1	SREC-I					1707:1712	SREC-I	1707:1712	SREC-I	1707:1712	Structural analyses and homology modeling of SREC-I suggest that the N-glycan bearing a β1-6GlcNAc branch at Asn(289) protects from proteinase attack and thus confers a higher stability on SREC-I.
22279061	9	32	from	Asn	1445:1447	arg1	constituents					1429:1440	minor constituents	1423:1440	minor constituents at Asn(289)	1423:1452	In addition, tri- and tetra-antennary were detected as minor constituents at Asn(289).
22279061	9	32	from	Asn	1445:1447	arg1	tetra-antennary					1390:1404	tetra-antennary	1390:1404	tetra-antennary	1390:1404	In addition, tri- and tetra-antennary were detected as minor constituents at Asn(289).
22279061	9	32	from	Asn	1445:1447	arg1	tri-					1381:1384	tri-	1381:1384	tri-	1381:1384	In addition, tri- and tetra-antennary were detected as minor constituents at Asn(289).
22279061	8	33	theme	common	1317:1322	arg1	structure					1330:1338	the common major structure	1313:1338	the common major structure at all glycosylation sites	1313:1365	Glycan structure analyses revealed that the core-fucosylated bi-antennary is the common major structure at all glycosylation sites.
22279061	8	33	theme	common	1317:1322	arg1	bi-antennary					1297:1308	bi-antennary	1297:1308	bi-antennary	1297:1308	Glycan structure analyses revealed that the core-fucosylated bi-antennary is the common major structure at all glycosylation sites.
22279061	11	34	theme	β1-6GlcNAc	1606:1615	arg1	branch					1617:1622	a β1-6GlcNAc branch	1604:1622	a β1-6GlcNAc branch	1604:1622	Structural analyses and homology modeling of SREC-I suggest that the N-glycan bearing a β1-6GlcNAc branch at Asn(289) protects from proteinase attack and thus confers a higher stability on SREC-I.
22279061	1	35	theme	low-density	274:284	arg1	lipoprotein					286:296	acetylated low-density lipoprotein	263:296	acetylated low-density lipoprotein (Ac-LDL)	263:305	Scavenger receptor expressed by endothelial cells (SREC-I) mediates the endocytosis of chemically modified lipoproteins such as acetylated low-density lipoprotein (Ac-LDL) and oxidized LDL and is implicated in atherogenesis.
22279061	1	35	theme	low-density	274:284	arg1	Ac-LDL					299:304	Ac-LDL	299:304	Ac-LDL	299:304	Scavenger receptor expressed by endothelial cells (SREC-I) mediates the endocytosis of chemically modified lipoproteins such as acetylated low-density lipoprotein (Ac-LDL) and oxidized LDL and is implicated in atherogenesis.
22279061	8	36	theme	glycosylation	1347:1359	arg1	sites					1361:1365	all glycosylation sites	1343:1365	all glycosylation sites	1343:1365	Glycan structure analyses revealed that the core-fucosylated bi-antennary is the common major structure at all glycosylation sites.
22279061	0	37	theme	SREC-I	13:18	arg1	N-glycans					0:8	N-glycans	0:8	N-glycans of SREC-I (scavenger receptor expressed by endothelial cells): essential role for ligand binding, trafficking and stability.	0:133	N-glycans of SREC-I (scavenger receptor expressed by endothelial cells): essential role for ligand binding, trafficking and stability.
22279061	12	38	theme	SREC-I	1794:1799	arg1	N-glycans					1781:1789	Asn(289)-, Asn(382)- and Asn(393)-linked N-glycans	1740:1789	Asn(289)-, Asn(382)- and Asn(393)-linked N-glycans of SREC-I	1740:1799	These data indicate that Asn(289)-, Asn(382)- and Asn(393)-linked N-glycans of SREC-I have distinct functions in regulating proteolytic resistance, ligand-binding affinity and subcellular localization, all of which might be involved in the development of atherogenesis.
22279061	11	39	theme	higher	1687:1692	arg1	stability					1694:1702	a higher stability	1685:1702	a higher stability on SREC-I	1685:1712	Structural analyses and homology modeling of SREC-I suggest that the N-glycan bearing a β1-6GlcNAc branch at Asn(289) protects from proteinase attack and thus confers a higher stability on SREC-I.
22279061	5	40	theme	enhanced	912:919	arg1	affinity					921:928	an enhanced affinity	909:928	an enhanced affinity for Ac-LDL	909:939	N382Q showed a normal cell surface residency and an enhanced affinity for Ac-LDL, resulting in an elevated Ac-LDL cellular incorporation.
22279061	12	41	theme	distinct	1806:1813	arg1	functions					1815:1823	distinct functions	1806:1823	distinct functions	1806:1823	These data indicate that Asn(289)-, Asn(382)- and Asn(393)-linked N-glycans of SREC-I have distinct functions in regulating proteolytic resistance, ligand-binding affinity and subcellular localization, all of which might be involved in the development of atherogenesis.
22279061	2	42	theme	ovary-K1	410:417	arg1	cells					419:423	Chinese hamster ovary-K1 cells	394:423	Chinese hamster ovary-K1 cells	394:423	We produced recombinant SREC-I in Chinese hamster ovary-K1 cells and identified three potential glycosylation sites, Asn(289), Asn(382) and Asn(393), which were all glycosylated.
22279061	5	43	theme	elevated	958:965	arg1	incorporation					983:995	an elevated Ac-LDL cellular incorporation	955:995	an elevated Ac-LDL cellular incorporation	955:995	N382Q showed a normal cell surface residency and an enhanced affinity for Ac-LDL, resulting in an elevated Ac-LDL cellular incorporation.
22279061	7	44	theme	N289Q	1229:1233	arg1	sensitivity					1210:1220	an enhanced trypsin sensitivity	1190:1220	an enhanced trypsin sensitivity of the N289Q	1190:1233	Furthermore, we detected an enhanced trypsin sensitivity of the N289Q.
22279061	5	45	theme	Ac-LDL	967:972	arg1	incorporation					983:995	an elevated Ac-LDL cellular incorporation	955:995	an elevated Ac-LDL cellular incorporation	955:995	N382Q showed a normal cell surface residency and an enhanced affinity for Ac-LDL, resulting in an elevated Ac-LDL cellular incorporation.
22279061	8	46	theme	structure	1243:1251	arg1	analyses					1253:1260	Glycan structure analyses	1236:1260	Glycan structure analyses	1236:1260	Glycan structure analyses revealed that the core-fucosylated bi-antennary is the common major structure at all glycosylation sites.
22279061	2	47	theme	hamster	402:408	arg1	cells					419:423	Chinese hamster ovary-K1 cells	394:423	Chinese hamster ovary-K1 cells	394:423	We produced recombinant SREC-I in Chinese hamster ovary-K1 cells and identified three potential glycosylation sites, Asn(289), Asn(382) and Asn(393), which were all glycosylated.
22279061	0	48	theme	scavenger	21:29	arg1	receptor					31:38	scavenger receptor	21:38	scavenger receptor expressed by endothelial cells	21:69	N-glycans of SREC-I (scavenger receptor expressed by endothelial cells): essential role for ligand binding, trafficking and stability.
22279061	12	49	theme	Asn	1751:1753	arg1	N-glycans					1781:1789	Asn(289)-, Asn(382)- and Asn(393)-linked N-glycans	1740:1789	Asn(289)-, Asn(382)- and Asn(393)-linked N-glycans of SREC-I	1740:1799	These data indicate that Asn(289)-, Asn(382)- and Asn(393)-linked N-glycans of SREC-I have distinct functions in regulating proteolytic resistance, ligand-binding affinity and subcellular localization, all of which might be involved in the development of atherogenesis.
22279061	3	50	theme	N-glycans	568:576	arg1	function					556:563	the function	552:563	the function of N-glycans in SREC-I	552:586	To determine the function of N-glycans in SREC-I, we characterized SREC-I mutant proteins by intracellular distribution and the cellular incorporation rate of Ac-LDL.
22279061	5	51	theme	cellular	974:981	arg1	incorporation					983:995	an elevated Ac-LDL cellular incorporation	955:995	an elevated Ac-LDL cellular incorporation	955:995	N382Q showed a normal cell surface residency and an enhanced affinity for Ac-LDL, resulting in an elevated Ac-LDL cellular incorporation.
22279061	12	52	theme	Asn	1765:1767	arg1	N-glycans					1781:1789	Asn(289)-, Asn(382)- and Asn(393)-linked N-glycans	1740:1789	Asn(289)-, Asn(382)- and Asn(393)-linked N-glycans of SREC-I	1740:1799	These data indicate that Asn(289)-, Asn(382)- and Asn(393)-linked N-glycans of SREC-I have distinct functions in regulating proteolytic resistance, ligand-binding affinity and subcellular localization, all of which might be involved in the development of atherogenesis.
22279061	2	53	theme	Chinese	394:400	arg1	cells					419:423	Chinese hamster ovary-K1 cells	394:423	Chinese hamster ovary-K1 cells	394:423	We produced recombinant SREC-I in Chinese hamster ovary-K1 cells and identified three potential glycosylation sites, Asn(289), Asn(382) and Asn(393), which were all glycosylated.
22279061	12	54	theme	-linked	1773:1779	arg1	N-glycans					1781:1789	Asn(289)-, Asn(382)- and Asn(393)-linked N-glycans	1740:1789	Asn(289)-, Asn(382)- and Asn(393)-linked N-glycans of SREC-I	1740:1799	These data indicate that Asn(289)-, Asn(382)- and Asn(393)-linked N-glycans of SREC-I have distinct functions in regulating proteolytic resistance, ligand-binding affinity and subcellular localization, all of which might be involved in the development of atherogenesis.
22279061	12	55	theme	proteolytic	1839:1849	arg1	resistance					1851:1860	proteolytic resistance	1839:1860	proteolytic resistance	1839:1860	These data indicate that Asn(289)-, Asn(382)- and Asn(393)-linked N-glycans of SREC-I have distinct functions in regulating proteolytic resistance, ligand-binding affinity and subcellular localization, all of which might be involved in the development of atherogenesis.
22279061	2	56	gly	glycosylation	456:468	arg2	Asn					477:479	Asn	477:479	Asn(289)	477:484	We produced recombinant SREC-I in Chinese hamster ovary-K1 cells and identified three potential glycosylation sites, Asn(289), Asn(382) and Asn(393), which were all glycosylated.
22279061	2	56	gly	glycosylation	456:468	arg2	sites					470:474	three potential glycosylation sites	440:474	three potential glycosylation sites	440:474	We produced recombinant SREC-I in Chinese hamster ovary-K1 cells and identified three potential glycosylation sites, Asn(289), Asn(382) and Asn(393), which were all glycosylated.
22279061	2	56	gly	glycosylation	456:468	arg2	Asn					487:489	Asn(382)	487:494	Asn(382)	487:494	We produced recombinant SREC-I in Chinese hamster ovary-K1 cells and identified three potential glycosylation sites, Asn(289), Asn(382) and Asn(393), which were all glycosylated.
22279061	2	56	gly	glycosylation	456:468	arg2	Asn					500:502	Asn(393)	500:507	Asn(393)	500:507	We produced recombinant SREC-I in Chinese hamster ovary-K1 cells and identified three potential glycosylation sites, Asn(289), Asn(382) and Asn(393), which were all glycosylated.
22279061	2	56	gly	glycosylation	456:468	arg2	three					440:444	three	440:444	three	440:444	We produced recombinant SREC-I in Chinese hamster ovary-K1 cells and identified three potential glycosylation sites, Asn(289), Asn(382) and Asn(393), which were all glycosylated.
22279061	10	57	theme	bisecting	1457:1465	arg1	GlcNAc					1467:1472	A bisecting GlcNAc	1455:1472	A bisecting GlcNAc	1455:1472	A bisecting GlcNAc was also detected at Asn(382) and Asn(393).
22279061	2	58	theme	glycosylation	456:468	arg1	sites					470:474	three potential glycosylation sites	440:474	three potential glycosylation sites	440:474	We produced recombinant SREC-I in Chinese hamster ovary-K1 cells and identified three potential glycosylation sites, Asn(289), Asn(382) and Asn(393), which were all glycosylated.
22279061	2	58	theme	glycosylation	456:468	arg1	Asn					500:502	Asn(393)	500:507	Asn(393)	500:507	We produced recombinant SREC-I in Chinese hamster ovary-K1 cells and identified three potential glycosylation sites, Asn(289), Asn(382) and Asn(393), which were all glycosylated.
22279061	2	58	theme	glycosylation	456:468	arg1	Asn					487:489	Asn(382)	487:494	Asn(382)	487:494	We produced recombinant SREC-I in Chinese hamster ovary-K1 cells and identified three potential glycosylation sites, Asn(289), Asn(382) and Asn(393), which were all glycosylated.
22279061	2	58	theme	glycosylation	456:468	arg1	Asn					477:479	Asn	477:479	Asn(289)	477:484	We produced recombinant SREC-I in Chinese hamster ovary-K1 cells and identified three potential glycosylation sites, Asn(289), Asn(382) and Asn(393), which were all glycosylated.
22279061	4	59	theme	Ac-LDL	852:857	arg1	incorporation					835:847	the cellular incorporation	822:847	the cellular incorporation of Ac-LDL	822:857	N382Q/N393Q and N289Q/N382Q/N393Q were sequestered in the endoplasmic reticulum, resulting in a severe reduction in the cellular incorporation of Ac-LDL.
22279061	3	60	theme	SREC-I	606:611	arg1	proteins					620:627	SREC-I mutant proteins	606:627	SREC-I mutant proteins	606:627	To determine the function of N-glycans in SREC-I, we characterized SREC-I mutant proteins by intracellular distribution and the cellular incorporation rate of Ac-LDL.
22279061	5	61	theme	normal	875:880	arg1	residency					895:903	a normal cell surface residency	873:903	a normal cell surface residency	873:903	N382Q showed a normal cell surface residency and an enhanced affinity for Ac-LDL, resulting in an elevated Ac-LDL cellular incorporation.
22279061	1	62	theme	oxidized	311:318	arg1	LDL					320:322	oxidized LDL	311:322	oxidized LDL	311:322	Scavenger receptor expressed by endothelial cells (SREC-I) mediates the endocytosis of chemically modified lipoproteins such as acetylated low-density lipoprotein (Ac-LDL) and oxidized LDL and is implicated in atherogenesis.
22279061	12	63	theme	Asn	1740:1742	arg1	N-glycans					1781:1789	Asn(289)-, Asn(382)- and Asn(393)-linked N-glycans	1740:1789	Asn(289)-, Asn(382)- and Asn(393)-linked N-glycans of SREC-I	1740:1799	These data indicate that Asn(289)-, Asn(382)- and Asn(393)-linked N-glycans of SREC-I have distinct functions in regulating proteolytic resistance, ligand-binding affinity and subcellular localization, all of which might be involved in the development of atherogenesis.
22279061	3	64	theme	mutant	613:618	arg1	proteins					620:627	SREC-I mutant proteins	606:627	SREC-I mutant proteins	606:627	To determine the function of N-glycans in SREC-I, we characterized SREC-I mutant proteins by intracellular distribution and the cellular incorporation rate of Ac-LDL.
22279061	6	65	theme	ligand-binding	1140:1153	arg1	affinity					1155:1162	ligand-binding affinity	1140:1162	ligand-binding affinity	1140:1162	These results indicate that the N-glycan of Asn(393) regulates the intracellular sorting of SREC-I and that the N-glycan of Asn(382) controls ligand-binding affinity.
22279061	2	66	from	SREC-I	384:389	arg1	cells					419:423	Chinese hamster ovary-K1 cells	394:423	Chinese hamster ovary-K1 cells	394:423	We produced recombinant SREC-I in Chinese hamster ovary-K1 cells and identified three potential glycosylation sites, Asn(289), Asn(382) and Asn(393), which were all glycosylated.
22279061	5	67	theme	cell	882:885	arg1	residency					895:903	a normal cell surface residency	873:903	a normal cell surface residency	873:903	N382Q showed a normal cell surface residency and an enhanced affinity for Ac-LDL, resulting in an elevated Ac-LDL cellular incorporation.
22279061	12	68	contain	have	1801:1804	arg2	functions					1815:1823	distinct functions	1806:1823	distinct functions	1806:1823	These data indicate that Asn(289)-, Asn(382)- and Asn(393)-linked N-glycans of SREC-I have distinct functions in regulating proteolytic resistance, ligand-binding affinity and subcellular localization, all of which might be involved in the development of atherogenesis.
22279061	12	68	contain	have	1801:1804	arg1	N-glycans					1781:1789	Asn(289)-, Asn(382)- and Asn(393)-linked N-glycans	1740:1789	Asn(289)-, Asn(382)- and Asn(393)-linked N-glycans of SREC-I	1740:1799	These data indicate that Asn(289)-, Asn(382)- and Asn(393)-linked N-glycans of SREC-I have distinct functions in regulating proteolytic resistance, ligand-binding affinity and subcellular localization, all of which might be involved in the development of atherogenesis.
22279061	11	69	theme	Structural	1518:1527	arg1	analyses					1529:1536	Structural analyses	1518:1536	Structural analyses	1518:1536	Structural analyses and homology modeling of SREC-I suggest that the N-glycan bearing a β1-6GlcNAc branch at Asn(289) protects from proteinase attack and thus confers a higher stability on SREC-I.
22279061	5	70	theme	surface	887:893	arg1	residency					895:903	a normal cell surface residency	873:903	a normal cell surface residency	873:903	N382Q showed a normal cell surface residency and an enhanced affinity for Ac-LDL, resulting in an elevated Ac-LDL cellular incorporation.
22279061	6	71	theme	intracellular	1065:1077	arg1	sorting					1079:1085	the intracellular sorting	1061:1085	the intracellular sorting of SREC-I	1061:1095	These results indicate that the N-glycan of Asn(393) regulates the intracellular sorting of SREC-I and that the N-glycan of Asn(382) controls ligand-binding affinity.
22279061	2	72	gly	glycosylated	525:536	arg1	sites					470:474	three potential glycosylation sites	440:474	three potential glycosylation sites	440:474	We produced recombinant SREC-I in Chinese hamster ovary-K1 cells and identified three potential glycosylation sites, Asn(289), Asn(382) and Asn(393), which were all glycosylated.
22279061	2	72	gly	glycosylated	525:536	arg1	Asn					500:502	Asn(393)	500:507	Asn(393)	500:507	We produced recombinant SREC-I in Chinese hamster ovary-K1 cells and identified three potential glycosylation sites, Asn(289), Asn(382) and Asn(393), which were all glycosylated.
22279061	2	72	gly	glycosylated	525:536	arg1	Asn					487:489	Asn(382)	487:494	Asn(382)	487:494	We produced recombinant SREC-I in Chinese hamster ovary-K1 cells and identified three potential glycosylation sites, Asn(289), Asn(382) and Asn(393), which were all glycosylated.
22279061	2	72	gly	glycosylated	525:536	arg1	Asn					477:479	Asn	477:479	Asn(289)	477:484	We produced recombinant SREC-I in Chinese hamster ovary-K1 cells and identified three potential glycosylation sites, Asn(289), Asn(382) and Asn(393), which were all glycosylated.
22279061	4	73	theme	endoplasmic	764:774	arg1	reticulum					776:784	the endoplasmic reticulum	760:784	the endoplasmic reticulum	760:784	N382Q/N393Q and N289Q/N382Q/N393Q were sequestered in the endoplasmic reticulum, resulting in a severe reduction in the cellular incorporation of Ac-LDL.
22279061	8	74	from	sites	1361:1365	arg1	structure					1330:1338	the common major structure	1313:1338	the common major structure at all glycosylation sites	1313:1365	Glycan structure analyses revealed that the core-fucosylated bi-antennary is the common major structure at all glycosylation sites.
22279061	8	74	from	sites	1361:1365	arg1	bi-antennary					1297:1308	bi-antennary	1297:1308	bi-antennary	1297:1308	Glycan structure analyses revealed that the core-fucosylated bi-antennary is the common major structure at all glycosylation sites.
22279061	0	75	theme	endothelial	53:63	arg1	cells					65:69	endothelial cells	53:69	endothelial cells	53:69	N-glycans of SREC-I (scavenger receptor expressed by endothelial cells): essential role for ligand binding, trafficking and stability.
22279061	3	76	theme	intracellular	632:644	arg1	distribution					646:657	intracellular distribution	632:657	intracellular distribution	632:657	To determine the function of N-glycans in SREC-I, we characterized SREC-I mutant proteins by intracellular distribution and the cellular incorporation rate of Ac-LDL.
22279061	0	77	dep	N-glycans	0:8	arg1	receptor					31:38	scavenger receptor	21:38	scavenger receptor expressed by endothelial cells	21:69	N-glycans of SREC-I (scavenger receptor expressed by endothelial cells): essential role for ligand binding, trafficking and stability.
22279061	0	77	dep	N-glycans	0:8	arg1	role					83:86	essential role	73:86	N-glycans of SREC-I (scavenger receptor expressed by endothelial cells): essential role for ligand binding, trafficking and stability.	0:133	N-glycans of SREC-I (scavenger receptor expressed by endothelial cells): essential role for ligand binding, trafficking and stability.
22279061	7	78	theme	trypsin	1202:1208	arg1	sensitivity					1210:1220	an enhanced trypsin sensitivity	1190:1220	an enhanced trypsin sensitivity of the N289Q	1190:1233	Furthermore, we detected an enhanced trypsin sensitivity of the N289Q.
22279061	7	79	theme	enhanced	1193:1200	arg1	sensitivity					1210:1220	an enhanced trypsin sensitivity	1190:1220	an enhanced trypsin sensitivity of the N289Q	1190:1233	Furthermore, we detected an enhanced trypsin sensitivity of the N289Q.
22279061	10	80	located	detected	1483:1490	arg2	GlcNAc					1467:1472	A bisecting GlcNAc	1455:1472	A bisecting GlcNAc	1455:1472	A bisecting GlcNAc was also detected at Asn(382) and Asn(393).
22279061	10	80	located	detected	1483:1490	arg1	393					1512:1514	393	1512:1514	393	1512:1514	A bisecting GlcNAc was also detected at Asn(382) and Asn(393).
22279061	10	80	located	detected	1483:1490	arg1	382					1499:1501	382	1499:1501	382	1499:1501	A bisecting GlcNAc was also detected at Asn(382) and Asn(393).
22279061	10	80	located	detected	1483:1490	arg1	Asn					1508:1510	Asn	1508:1510	Asn(393)	1508:1515	A bisecting GlcNAc was also detected at Asn(382) and Asn(393).
22279061	10	80	located	detected	1483:1490	arg1	Asn					1495:1497	Asn	1495:1497	Asn(382)	1495:1502	A bisecting GlcNAc was also detected at Asn(382) and Asn(393).
7642555	7	0	theme	GlcNAc	682:687	arg1	moieties					689:696	its GlcNAc moieties	678:696	its GlcNAc moieties	678:696	c-Myc purified from sf9 insect cells was trypsinized, and its GlcNAc moieties were enzymically labeled with [3H]galactose.
7642555	8	1	theme	desorption/ionization	933:953	arg1	spectrometry					960:971	laser desorption/ionization mass spectrometry	927:971	laser desorption/ionization mass spectrometry	927:971	The [3H]galactose-labeled glycopeptides were isolated by reverse phase high performance liquid chromatography and then subjected to gas-phase sequencing, manual Edman degradation, and laser desorption/ionization mass spectrometry.
7642555	9	2	dep	in	1016:1017	arg1	vivo					1019:1022	vivo	1019:1022	vivo	1019:1022	These analyses show that threonine 58, an in vivo phosphorylation site in the transactivation domain, is the major O-GlcNAc glycosylation site of c-Myc.
7642555	1	3	theme	helix-loop	119:128	arg1	zipper					138:143	helix-loop leucine zipper	119:143	a helix-loop leucine zipper phosphoprotein that heterodimerizes with Max and regulates gene transcription in cell proliferation, cell differentiation, and programmed cell death	117:292	c-Myc is a helix-loop leucine zipper phosphoprotein that heterodimerizes with Max and regulates gene transcription in cell proliferation, cell differentiation, and programmed cell death.
7642555	2	4	mod	modified	337:344	arg3	N-acetylglucosamine					358:376	O-linked N-acetylglucosamine	349:376	O-linked N-acetylglucosamine (O-GlcNAc)	349:387	Previously, we demonstrated that c-Myc is modified by O-linked N-acetylglucosamine (O-GlcNAc) within or nearby the N-terminal transcriptional activation domain (Chou, T.-Y., Dang, C.V., and Hart, G.W. (1995) Proc.
7642555	2	4	mod	modified	337:344	arg3	O-GlcNAc					379:386	O-GlcNAc	379:386	O-GlcNAc	379:386	Previously, we demonstrated that c-Myc is modified by O-linked N-acetylglucosamine (O-GlcNAc) within or nearby the N-terminal transcriptional activation domain (Chou, T.-Y., Dang, C.V., and Hart, G.W. (1995) Proc.
7642555	2	4	mod	modified	337:344	arg1	c-Myc					328:332	c-Myc	328:332	c-Myc	328:332	Previously, we demonstrated that c-Myc is modified by O-linked N-acetylglucosamine (O-GlcNAc) within or nearby the N-terminal transcriptional activation domain (Chou, T.-Y., Dang, C.V., and Hart, G.W. (1995) Proc.
7642555	8	5	theme	laser	927:931	arg1	spectrometry					960:971	laser desorption/ionization mass spectrometry	927:971	laser desorption/ionization mass spectrometry	927:971	The [3H]galactose-labeled glycopeptides were isolated by reverse phase high performance liquid chromatography and then subjected to gas-phase sequencing, manual Edman degradation, and laser desorption/ionization mass spectrometry.
7642555	9	6	theme	major	1083:1087	arg1	c-Myc					1120:1124	c-Myc	1120:1124	c-Myc	1120:1124	These analyses show that threonine 58, an in vivo phosphorylation site in the transactivation domain, is the major O-GlcNAc glycosylation site of c-Myc.
7642555	9	6	theme	major	1083:1087	arg1	site					1112:1115	the major O-GlcNAc glycosylation site	1079:1115	the major O-GlcNAc glycosylation site of c-Myc	1079:1124	These analyses show that threonine 58, an in vivo phosphorylation site in the transactivation domain, is the major O-GlcNAc glycosylation site of c-Myc.
7642555	9	6	theme	major	1083:1087	arg1	threonine					999:1007	threonine 58	999:1010	threonine 58	999:1010	These analyses show that threonine 58, an in vivo phosphorylation site in the transactivation domain, is the major O-GlcNAc glycosylation site of c-Myc.
7642555	1	7	theme	leucine	130:136	arg1	zipper					138:143	helix-loop leucine zipper	119:143	a helix-loop leucine zipper phosphoprotein that heterodimerizes with Max and regulates gene transcription in cell proliferation, cell differentiation, and programmed cell death	117:292	c-Myc is a helix-loop leucine zipper phosphoprotein that heterodimerizes with Max and regulates gene transcription in cell proliferation, cell differentiation, and programmed cell death.
7642555	8	8	theme	[3H	747:749	arg1	glycopeptides					769:781	The [3H]galactose-labeled glycopeptides	743:781	The [3H]galactose-labeled glycopeptides	743:781	The [3H]galactose-labeled glycopeptides were isolated by reverse phase high performance liquid chromatography and then subjected to gas-phase sequencing, manual Edman degradation, and laser desorption/ionization mass spectrometry.
7642555	0	9	theme	mutational	74:83	arg1	threonine					25:33	threonine 58	25:36	threonine 58	25:36	c-Myc is glycosylated at threonine 58, a known phosphorylation site and a mutational hot spot in lymphomas.
7642555	0	9	theme	mutational	74:83	arg1	spot					89:92	a mutational hot spot	72:92	a mutational hot spot in lymphomas	72:105	c-Myc is glycosylated at threonine 58, a known phosphorylation site and a mutational hot spot in lymphomas.
7642555	9	10	theme	c-Myc	1120:1124	arg1	c-Myc					1120:1124	c-Myc	1120:1124	c-Myc	1120:1124	These analyses show that threonine 58, an in vivo phosphorylation site in the transactivation domain, is the major O-GlcNAc glycosylation site of c-Myc.
7642555	9	10	theme	c-Myc	1120:1124	arg1	site					1112:1115	the major O-GlcNAc glycosylation site	1079:1115	the major O-GlcNAc glycosylation site of c-Myc	1079:1124	These analyses show that threonine 58, an in vivo phosphorylation site in the transactivation domain, is the major O-GlcNAc glycosylation site of c-Myc.
7642555	9	10	theme	c-Myc	1120:1124	arg1	threonine					999:1007	threonine 58	999:1010	threonine 58	999:1010	These analyses show that threonine 58, an in vivo phosphorylation site in the transactivation domain, is the major O-GlcNAc glycosylation site of c-Myc.
7642555	2	11	dep	T.-Y.	462:466	arg1	Proc					503:506	Proc	503:506	Proc	503:506	Previously, we demonstrated that c-Myc is modified by O-linked N-acetylglucosamine (O-GlcNAc) within or nearby the N-terminal transcriptional activation domain (Chou, T.-Y., Dang, C.V., and Hart, G.W. (1995) Proc.
7642555	8	12	theme	gas-phase	875:883	arg1	sequencing					885:894	gas-phase sequencing	875:894	gas-phase sequencing	875:894	The [3H]galactose-labeled glycopeptides were isolated by reverse phase high performance liquid chromatography and then subjected to gas-phase sequencing, manual Edman degradation, and laser desorption/ionization mass spectrometry.
7642555	2	13	dep	modified	337:344	arg1	1995					497:500	1995	497:500	1995	497:500	Previously, we demonstrated that c-Myc is modified by O-linked N-acetylglucosamine (O-GlcNAc) within or nearby the N-terminal transcriptional activation domain (Chou, T.-Y., Dang, C.V., and Hart, G.W. (1995) Proc.
7642555	2	13	dep	modified	337:344	arg1	G.W.					491:494	G.W.	491:494	G.W.	491:494	Previously, we demonstrated that c-Myc is modified by O-linked N-acetylglucosamine (O-GlcNAc) within or nearby the N-terminal transcriptional activation domain (Chou, T.-Y., Dang, C.V., and Hart, G.W. (1995) Proc.
7642555	2	13	dep	modified	337:344	arg1	C.V.					475:478	C.V.	475:478	C.V.	475:478	Previously, we demonstrated that c-Myc is modified by O-linked N-acetylglucosamine (O-GlcNAc) within or nearby the N-terminal transcriptional activation domain (Chou, T.-Y., Dang, C.V., and Hart, G.W. (1995) Proc.
7642555	2	13	dep	modified	337:344	arg1	Dang					469:472	Dang	469:472	Dang	469:472	Previously, we demonstrated that c-Myc is modified by O-linked N-acetylglucosamine (O-GlcNAc) within or nearby the N-terminal transcriptional activation domain (Chou, T.-Y., Dang, C.V., and Hart, G.W. (1995) Proc.
7642555	2	13	dep	modified	337:344	arg1	T.-Y.					462:466	T.-Y.	462:466	T.-Y.	462:466	Previously, we demonstrated that c-Myc is modified by O-linked N-acetylglucosamine (O-GlcNAc) within or nearby the N-terminal transcriptional activation domain (Chou, T.-Y., Dang, C.V., and Hart, G.W. (1995) Proc.
7642555	1	14	theme	cell	246:249	arg1	differentiation					251:265	cell differentiation	246:265	cell differentiation	246:265	c-Myc is a helix-loop leucine zipper phosphoprotein that heterodimerizes with Max and regulates gene transcription in cell proliferation, cell differentiation, and programmed cell death.
7642555	8	15	theme	mass	955:958	arg1	spectrometry					960:971	laser desorption/ionization mass spectrometry	927:971	laser desorption/ionization mass spectrometry	927:971	The [3H]galactose-labeled glycopeptides were isolated by reverse phase high performance liquid chromatography and then subjected to gas-phase sequencing, manual Edman degradation, and laser desorption/ionization mass spectrometry.
7642555	8	16	theme	manual	897:902	arg1	degradation					910:920	manual Edman degradation	897:920	manual Edman degradation	897:920	The [3H]galactose-labeled glycopeptides were isolated by reverse phase high performance liquid chromatography and then subjected to gas-phase sequencing, manual Edman degradation, and laser desorption/ionization mass spectrometry.
7642555	6	17	from	s	607:607	arg1	c-Myc					613:617	c-Myc	613:617	c-Myc	613:617	In this paper, we identified the O-GlcNAc attachment site(s) on c-Myc.
7642555	8	18	theme	galactose-labeled	751:767	arg1	glycopeptides					769:781	The [3H]galactose-labeled glycopeptides	743:781	The [3H]galactose-labeled glycopeptides	743:781	The [3H]galactose-labeled glycopeptides were isolated by reverse phase high performance liquid chromatography and then subjected to gas-phase sequencing, manual Edman degradation, and laser desorption/ionization mass spectrometry.
7642555	11	19	theme	reciprocal	1322:1331	arg1	glycosylation					1333:1345	reciprocal glycosylation	1322:1345	reciprocal glycosylation	1322:1345	The reciprocal glycosylation and phosphorylation at this biologically significant amino acid residue may play an important role in the regulation of the functions of c-Myc.
7642555	5	20	dep	U.S.A.	526:531	arg1	4417-4421					537:545	4417-4421	537:545	4417-4421	537:545	U.S.A. 92, 4417-4421).
7642555	11	21	theme	significant	1388:1398	arg1	residue					1411:1417	this biologically significant amino acid residue	1370:1417	this biologically significant amino acid residue	1370:1417	The reciprocal glycosylation and phosphorylation at this biologically significant amino acid residue may play an important role in the regulation of the functions of c-Myc.
7642555	1	22	theme	zipper	138:143	arg1	c-Myc					108:112	c-Myc	108:112	c-Myc	108:112	c-Myc is a helix-loop leucine zipper phosphoprotein that heterodimerizes with Max and regulates gene transcription in cell proliferation, cell differentiation, and programmed cell death.
7642555	1	22	theme	zipper	138:143	arg1	phosphoprotein					145:158	a helix-loop leucine zipper phosphoprotein	117:158	a helix-loop leucine zipper phosphoprotein that heterodimerizes with Max and regulates gene transcription in cell proliferation, cell differentiation, and programmed cell death	117:292	c-Myc is a helix-loop leucine zipper phosphoprotein that heterodimerizes with Max and regulates gene transcription in cell proliferation, cell differentiation, and programmed cell death.
7642555	0	23	theme	hot	85:87	arg1	threonine					25:33	threonine 58	25:36	threonine 58	25:36	c-Myc is glycosylated at threonine 58, a known phosphorylation site and a mutational hot spot in lymphomas.
7642555	0	23	theme	hot	85:87	arg1	spot					89:92	a mutational hot spot	72:92	a mutational hot spot in lymphomas	72:105	c-Myc is glycosylated at threonine 58, a known phosphorylation site and a mutational hot spot in lymphomas.
7642555	2	24	link	O-linked	349:356	arg1	O-GlcNAc					379:386	O-GlcNAc	379:386	O-GlcNAc	379:386	Previously, we demonstrated that c-Myc is modified by O-linked N-acetylglucosamine (O-GlcNAc) within or nearby the N-terminal transcriptional activation domain (Chou, T.-Y., Dang, C.V., and Hart, G.W. (1995) Proc.
7642555	2	24	link	O-linked	349:356	arg1	N-acetylglucosamine					358:376	O-linked N-acetylglucosamine	349:376	O-linked N-acetylglucosamine (O-GlcNAc)	349:387	Previously, we demonstrated that c-Myc is modified by O-linked N-acetylglucosamine (O-GlcNAc) within or nearby the N-terminal transcriptional activation domain (Chou, T.-Y., Dang, C.V., and Hart, G.W. (1995) Proc.
7642555	10	25	theme	human	1206:1210	arg1	Burkitt					1212:1218	human Burkitt and AIDS-related lymphomas	1206:1245	Burkitt	1212:1218	Mutation of threonine 58, frequently found in retroviral v-Myc proteins and in human Burkitt and AIDS-related lymphomas, is associated with enhanced transforming activity and tumorigenicity.
7642555	2	26	dep	domain	448:453	arg1	nearby					399:404	nearby	399:404	nearby	399:404	Previously, we demonstrated that c-Myc is modified by O-linked N-acetylglucosamine (O-GlcNAc) within or nearby the N-terminal transcriptional activation domain (Chou, T.-Y., Dang, C.V., and Hart, G.W. (1995) Proc.
7642555	8	27	theme	Edman	904:908	arg1	degradation					910:920	manual Edman degradation	897:920	manual Edman degradation	897:920	The [3H]galactose-labeled glycopeptides were isolated by reverse phase high performance liquid chromatography and then subjected to gas-phase sequencing, manual Edman degradation, and laser desorption/ionization mass spectrometry.
7642555	10	28	theme	v-Myc	1184:1188	arg1	proteins					1190:1197	retroviral v-Myc proteins	1173:1197	retroviral v-Myc proteins	1173:1197	Mutation of threonine 58, frequently found in retroviral v-Myc proteins and in human Burkitt and AIDS-related lymphomas, is associated with enhanced transforming activity and tumorigenicity.
7642555	2	29	theme	activation	437:446	arg1	domain					448:453	the N-terminal transcriptional activation domain	406:453	the N-terminal transcriptional activation domain	406:453	Previously, we demonstrated that c-Myc is modified by O-linked N-acetylglucosamine (O-GlcNAc) within or nearby the N-terminal transcriptional activation domain (Chou, T.-Y., Dang, C.V., and Hart, G.W. (1995) Proc.
7642555	9	30	theme	phosphorylation	1024:1038	arg1	site					1040:1043	an in vivo phosphorylation site	1013:1043	an in vivo phosphorylation site in the transactivation domain	1013:1073	These analyses show that threonine 58, an in vivo phosphorylation site in the transactivation domain, is the major O-GlcNAc glycosylation site of c-Myc.
7642555	9	30	theme	phosphorylation	1024:1038	arg1	threonine					999:1007	threonine 58	999:1010	threonine 58	999:1010	These analyses show that threonine 58, an in vivo phosphorylation site in the transactivation domain, is the major O-GlcNAc glycosylation site of c-Myc.
7642555	2	31	theme	transcriptional	421:435	arg1	domain					448:453	the N-terminal transcriptional activation domain	406:453	the N-terminal transcriptional activation domain	406:453	Previously, we demonstrated that c-Myc is modified by O-linked N-acetylglucosamine (O-GlcNAc) within or nearby the N-terminal transcriptional activation domain (Chou, T.-Y., Dang, C.V., and Hart, G.W. (1995) Proc.
7642555	8	32	theme	phase	808:812	arg1	chromatography					838:851	reverse phase high performance liquid chromatography	800:851	reverse phase high performance liquid chromatography	800:851	The [3H]galactose-labeled glycopeptides were isolated by reverse phase high performance liquid chromatography and then subjected to gas-phase sequencing, manual Edman degradation, and laser desorption/ionization mass spectrometry.
7642555	11	33	theme	functions	1471:1479	arg1	regulation					1453:1462	the regulation	1449:1462	the regulation of the functions of c-Myc	1449:1488	The reciprocal glycosylation and phosphorylation at this biologically significant amino acid residue may play an important role in the regulation of the functions of c-Myc.
7642555	9	34	theme	O-GlcNAc	1089:1096	arg1	c-Myc					1120:1124	c-Myc	1120:1124	c-Myc	1120:1124	These analyses show that threonine 58, an in vivo phosphorylation site in the transactivation domain, is the major O-GlcNAc glycosylation site of c-Myc.
7642555	9	34	theme	O-GlcNAc	1089:1096	arg1	site					1112:1115	the major O-GlcNAc glycosylation site	1079:1115	the major O-GlcNAc glycosylation site of c-Myc	1079:1124	These analyses show that threonine 58, an in vivo phosphorylation site in the transactivation domain, is the major O-GlcNAc glycosylation site of c-Myc.
7642555	9	34	theme	O-GlcNAc	1089:1096	arg1	threonine					999:1007	threonine 58	999:1010	threonine 58	999:1010	These analyses show that threonine 58, an in vivo phosphorylation site in the transactivation domain, is the major O-GlcNAc glycosylation site of c-Myc.
7642555	6	35	theme	site	602:605	arg1	s					607:607	the O-GlcNAc attachment site(s)	578:608	the O-GlcNAc attachment site(s) on c-Myc	578:617	In this paper, we identified the O-GlcNAc attachment site(s) on c-Myc.
7642555	2	36	theme	N-terminal	410:419	arg1	domain					448:453	the N-terminal transcriptional activation domain	406:453	the N-terminal transcriptional activation domain	406:453	Previously, we demonstrated that c-Myc is modified by O-linked N-acetylglucosamine (O-GlcNAc) within or nearby the N-terminal transcriptional activation domain (Chou, T.-Y., Dang, C.V., and Hart, G.W. (1995) Proc.
7642555	1	37	theme	programmed	272:281	arg1	death					288:292	programmed cell death	272:292	programmed cell death	272:292	c-Myc is a helix-loop leucine zipper phosphoprotein that heterodimerizes with Max and regulates gene transcription in cell proliferation, cell differentiation, and programmed cell death.
7642555	8	38	theme	reverse	800:806	arg1	chromatography					838:851	reverse phase high performance liquid chromatography	800:851	reverse phase high performance liquid chromatography	800:851	The [3H]galactose-labeled glycopeptides were isolated by reverse phase high performance liquid chromatography and then subjected to gas-phase sequencing, manual Edman degradation, and laser desorption/ionization mass spectrometry.
7642555	6	39	theme	attachment	591:600	arg1	s					607:607	the O-GlcNAc attachment site(s)	578:608	the O-GlcNAc attachment site(s) on c-Myc	578:617	In this paper, we identified the O-GlcNAc attachment site(s) on c-Myc.
7642555	10	40	theme	AIDS-related	1224:1235	arg1	lymphomas					1237:1245	human Burkitt and AIDS-related lymphomas	1206:1245	lymphomas	1237:1245	Mutation of threonine 58, frequently found in retroviral v-Myc proteins and in human Burkitt and AIDS-related lymphomas, is associated with enhanced transforming activity and tumorigenicity.
7642555	11	41	theme	acid	1406:1409	arg1	residue					1411:1417	this biologically significant amino acid residue	1370:1417	this biologically significant amino acid residue	1370:1417	The reciprocal glycosylation and phosphorylation at this biologically significant amino acid residue may play an important role in the regulation of the functions of c-Myc.
7642555	1	42	theme	cell	283:286	arg1	death					288:292	programmed cell death	272:292	programmed cell death	272:292	c-Myc is a helix-loop leucine zipper phosphoprotein that heterodimerizes with Max and regulates gene transcription in cell proliferation, cell differentiation, and programmed cell death.
7642555	8	43	gly	glycopeptides	769:781	arg2	glycopeptides					769:781	The [3H]galactose-labeled glycopeptides	743:781	The [3H]galactose-labeled glycopeptides	743:781	The [3H]galactose-labeled glycopeptides were isolated by reverse phase high performance liquid chromatography and then subjected to gas-phase sequencing, manual Edman degradation, and laser desorption/ionization mass spectrometry.
7642555	0	44	from	site	63:66	arg1	lymphomas					97:105	lymphomas	97:105	lymphomas	97:105	c-Myc is glycosylated at threonine 58, a known phosphorylation site and a mutational hot spot in lymphomas.
7642555	6	45	theme	O-GlcNAc	582:589	arg1	s					607:607	the O-GlcNAc attachment site(s)	578:608	the O-GlcNAc attachment site(s) on c-Myc	578:617	In this paper, we identified the O-GlcNAc attachment site(s) on c-Myc.
7642555	9	46	from	site	1040:1043	arg1	domain					1068:1073	the transactivation domain	1048:1073	the transactivation domain	1048:1073	These analyses show that threonine 58, an in vivo phosphorylation site in the transactivation domain, is the major O-GlcNAc glycosylation site of c-Myc.
7642555	11	47	theme	amino	1400:1404	arg1	residue					1411:1417	this biologically significant amino acid residue	1370:1417	this biologically significant amino acid residue	1370:1417	The reciprocal glycosylation and phosphorylation at this biologically significant amino acid residue may play an important role in the regulation of the functions of c-Myc.
7642555	8	48	theme	performance	819:829	arg1	chromatography					838:851	reverse phase high performance liquid chromatography	800:851	reverse phase high performance liquid chromatography	800:851	The [3H]galactose-labeled glycopeptides were isolated by reverse phase high performance liquid chromatography and then subjected to gas-phase sequencing, manual Edman degradation, and laser desorption/ionization mass spectrometry.
7642555	11	49	from	residue	1411:1417	arg1	glycosylation					1333:1345	reciprocal glycosylation	1322:1345	reciprocal glycosylation	1322:1345	The reciprocal glycosylation and phosphorylation at this biologically significant amino acid residue may play an important role in the regulation of the functions of c-Myc.
7642555	11	49	from	residue	1411:1417	arg1	phosphorylation					1351:1365	phosphorylation	1351:1365	phosphorylation	1351:1365	The reciprocal glycosylation and phosphorylation at this biologically significant amino acid residue may play an important role in the regulation of the functions of c-Myc.
7642555	9	50	theme	glycosylation	1098:1110	arg1	c-Myc					1120:1124	c-Myc	1120:1124	c-Myc	1120:1124	These analyses show that threonine 58, an in vivo phosphorylation site in the transactivation domain, is the major O-GlcNAc glycosylation site of c-Myc.
7642555	9	50	theme	glycosylation	1098:1110	arg1	site					1112:1115	the major O-GlcNAc glycosylation site	1079:1115	the major O-GlcNAc glycosylation site of c-Myc	1079:1124	These analyses show that threonine 58, an in vivo phosphorylation site in the transactivation domain, is the major O-GlcNAc glycosylation site of c-Myc.
7642555	9	50	theme	glycosylation	1098:1110	arg1	threonine					999:1007	threonine 58	999:1010	threonine 58	999:1010	These analyses show that threonine 58, an in vivo phosphorylation site in the transactivation domain, is the major O-GlcNAc glycosylation site of c-Myc.
7642555	10	51	located	found	1164:1168	arg2	Mutation					1127:1134	Mutation	1127:1134	Mutation	1127:1134	Mutation of threonine 58, frequently found in retroviral v-Myc proteins and in human Burkitt and AIDS-related lymphomas, is associated with enhanced transforming activity and tumorigenicity.
7642555	10	51	located	found	1164:1168	arg1	Burkitt					1212:1218	human Burkitt and AIDS-related lymphomas	1206:1245	Burkitt	1212:1218	Mutation of threonine 58, frequently found in retroviral v-Myc proteins and in human Burkitt and AIDS-related lymphomas, is associated with enhanced transforming activity and tumorigenicity.
7642555	10	51	located	found	1164:1168	arg1	lymphomas					1237:1245	human Burkitt and AIDS-related lymphomas	1206:1245	lymphomas	1237:1245	Mutation of threonine 58, frequently found in retroviral v-Myc proteins and in human Burkitt and AIDS-related lymphomas, is associated with enhanced transforming activity and tumorigenicity.
7642555	10	51	located	found	1164:1168	arg1	proteins					1190:1197	retroviral v-Myc proteins	1173:1197	retroviral v-Myc proteins	1173:1197	Mutation of threonine 58, frequently found in retroviral v-Myc proteins and in human Burkitt and AIDS-related lymphomas, is associated with enhanced transforming activity and tumorigenicity.
7642555	0	52	gly	glycosylated	9:20	arg2	spot					89:92	a mutational hot spot	72:92	a mutational hot spot in lymphomas	72:105	c-Myc is glycosylated at threonine 58, a known phosphorylation site and a mutational hot spot in lymphomas.
7642555	0	52	gly	glycosylated	9:20	arg1	c-Myc					0:4	c-Myc	0:4	c-Myc	0:4	c-Myc is glycosylated at threonine 58, a known phosphorylation site and a mutational hot spot in lymphomas.
7642555	0	52	gly	glycosylated	9:20	arg2	threonine					25:33	threonine 58	25:36	threonine 58	25:36	c-Myc is glycosylated at threonine 58, a known phosphorylation site and a mutational hot spot in lymphomas.
7642555	0	52	gly	glycosylated	9:20	arg2	site					63:66	a known phosphorylation site	39:66	a known phosphorylation site	39:66	c-Myc is glycosylated at threonine 58, a known phosphorylation site and a mutational hot spot in lymphomas.
7642555	8	53	theme	high	814:817	arg1	chromatography					838:851	reverse phase high performance liquid chromatography	800:851	reverse phase high performance liquid chromatography	800:851	The [3H]galactose-labeled glycopeptides were isolated by reverse phase high performance liquid chromatography and then subjected to gas-phase sequencing, manual Edman degradation, and laser desorption/ionization mass spectrometry.
7642555	11	54	dep	glycosylation	1333:1345	arg1	The					1318:1320	The	1318:1320	The	1318:1320	The reciprocal glycosylation and phosphorylation at this biologically significant amino acid residue may play an important role in the regulation of the functions of c-Myc.
7642555	0	55	from	spot	89:92	arg1	lymphomas					97:105	lymphomas	97:105	lymphomas	97:105	c-Myc is glycosylated at threonine 58, a known phosphorylation site and a mutational hot spot in lymphomas.
7642555	11	56	theme	c-Myc	1484:1488	arg1	functions					1471:1479	the functions	1467:1479	the functions of c-Myc	1467:1488	The reciprocal glycosylation and phosphorylation at this biologically significant amino acid residue may play an important role in the regulation of the functions of c-Myc.
7642555	11	57	theme	important	1431:1439	arg1	role					1441:1444	an important role	1428:1444	an important role	1428:1444	The reciprocal glycosylation and phosphorylation at this biologically significant amino acid residue may play an important role in the regulation of the functions of c-Myc.
7642555	8	58	theme	liquid	831:836	arg1	chromatography					838:851	reverse phase high performance liquid chromatography	800:851	reverse phase high performance liquid chromatography	800:851	The [3H]galactose-labeled glycopeptides were isolated by reverse phase high performance liquid chromatography and then subjected to gas-phase sequencing, manual Edman degradation, and laser desorption/ionization mass spectrometry.
7642555	1	59	theme	gene	204:207	arg1	transcription					209:221	gene transcription	204:221	gene transcription	204:221	c-Myc is a helix-loop leucine zipper phosphoprotein that heterodimerizes with Max and regulates gene transcription in cell proliferation, cell differentiation, and programmed cell death.
7642555	9	60	theme	transactivation	1052:1066	arg1	domain					1068:1073	the transactivation domain	1048:1073	the transactivation domain	1048:1073	These analyses show that threonine 58, an in vivo phosphorylation site in the transactivation domain, is the major O-GlcNAc glycosylation site of c-Myc.
7642555	9	61	theme	in	1016:1017	arg1	site					1040:1043	an in vivo phosphorylation site	1013:1043	an in vivo phosphorylation site in the transactivation domain	1013:1073	These analyses show that threonine 58, an in vivo phosphorylation site in the transactivation domain, is the major O-GlcNAc glycosylation site of c-Myc.
7642555	9	61	theme	in	1016:1017	arg1	threonine					999:1007	threonine 58	999:1010	threonine 58	999:1010	These analyses show that threonine 58, an in vivo phosphorylation site in the transactivation domain, is the major O-GlcNAc glycosylation site of c-Myc.
7642555	10	62	theme	threonine	1139:1147	arg1	Mutation					1127:1134	Mutation	1127:1134	Mutation	1127:1134	Mutation of threonine 58, frequently found in retroviral v-Myc proteins and in human Burkitt and AIDS-related lymphomas, is associated with enhanced transforming activity and tumorigenicity.
7642555	9	63	gly	glycosylation	1098:1110	arg1	c-Myc					1120:1124	c-Myc	1120:1124	c-Myc	1120:1124	These analyses show that threonine 58, an in vivo phosphorylation site in the transactivation domain, is the major O-GlcNAc glycosylation site of c-Myc.
7642555	9	63	gly	glycosylation	1098:1110	arg2	c-Myc					1120:1124	c-Myc	1120:1124	c-Myc	1120:1124	These analyses show that threonine 58, an in vivo phosphorylation site in the transactivation domain, is the major O-GlcNAc glycosylation site of c-Myc.
7642555	9	63	gly	glycosylation	1098:1110	arg2	site					1112:1115	the major O-GlcNAc glycosylation site	1079:1115	the major O-GlcNAc glycosylation site of c-Myc	1079:1124	These analyses show that threonine 58, an in vivo phosphorylation site in the transactivation domain, is the major O-GlcNAc glycosylation site of c-Myc.
7642555	9	63	gly	glycosylation	1098:1110	arg2	threonine					999:1007	threonine 58	999:1010	threonine 58	999:1010	These analyses show that threonine 58, an in vivo phosphorylation site in the transactivation domain, is the major O-GlcNAc glycosylation site of c-Myc.
7642555	0	64	theme	phosphorylation	47:61	arg1	site					63:66	a known phosphorylation site	39:66	a known phosphorylation site	39:66	c-Myc is glycosylated at threonine 58, a known phosphorylation site and a mutational hot spot in lymphomas.
7642555	0	64	theme	phosphorylation	47:61	arg1	threonine					25:33	threonine 58	25:36	threonine 58	25:36	c-Myc is glycosylated at threonine 58, a known phosphorylation site and a mutational hot spot in lymphomas.
7642555	10	65	theme	transforming	1276:1287	arg1	activity					1289:1296	enhanced transforming activity	1267:1296	enhanced transforming activity	1267:1296	Mutation of threonine 58, frequently found in retroviral v-Myc proteins and in human Burkitt and AIDS-related lymphomas, is associated with enhanced transforming activity and tumorigenicity.
7642555	2	66	theme	O-linked	349:356	arg1	O-GlcNAc					379:386	O-GlcNAc	379:386	O-GlcNAc	379:386	Previously, we demonstrated that c-Myc is modified by O-linked N-acetylglucosamine (O-GlcNAc) within or nearby the N-terminal transcriptional activation domain (Chou, T.-Y., Dang, C.V., and Hart, G.W. (1995) Proc.
7642555	2	66	theme	O-linked	349:356	arg1	N-acetylglucosamine					358:376	O-linked N-acetylglucosamine	349:376	O-linked N-acetylglucosamine (O-GlcNAc)	349:387	Previously, we demonstrated that c-Myc is modified by O-linked N-acetylglucosamine (O-GlcNAc) within or nearby the N-terminal transcriptional activation domain (Chou, T.-Y., Dang, C.V., and Hart, G.W. (1995) Proc.
7642555	7	67	theme	sf9	640:642	arg1	cells					651:655	sf9 insect cells	640:655	sf9 insect cells	640:655	c-Myc purified from sf9 insect cells was trypsinized, and its GlcNAc moieties were enzymically labeled with [3H]galactose.
7642555	0	68	theme	known	41:45	arg1	site					63:66	a known phosphorylation site	39:66	a known phosphorylation site	39:66	c-Myc is glycosylated at threonine 58, a known phosphorylation site and a mutational hot spot in lymphomas.
7642555	0	68	theme	known	41:45	arg1	threonine					25:33	threonine 58	25:36	threonine 58	25:36	c-Myc is glycosylated at threonine 58, a known phosphorylation site and a mutational hot spot in lymphomas.
7642555	11	69	gly	glycosylation	1333:1345	arg2	residue					1411:1417	this biologically significant amino acid residue	1370:1417	this biologically significant amino acid residue	1370:1417	The reciprocal glycosylation and phosphorylation at this biologically significant amino acid residue may play an important role in the regulation of the functions of c-Myc.
7642555	11	69	gly	glycosylation	1333:1345	arg1	residue					1411:1417	this biologically significant amino acid residue	1370:1417	this biologically significant amino acid residue	1370:1417	The reciprocal glycosylation and phosphorylation at this biologically significant amino acid residue may play an important role in the regulation of the functions of c-Myc.
7642555	7	70	theme	insect	644:649	arg1	cells					651:655	sf9 insect cells	640:655	sf9 insect cells	640:655	c-Myc purified from sf9 insect cells was trypsinized, and its GlcNAc moieties were enzymically labeled with [3H]galactose.
7642555	10	71	theme	enhanced	1267:1274	arg1	activity					1289:1296	enhanced transforming activity	1267:1296	enhanced transforming activity	1267:1296	Mutation of threonine 58, frequently found in retroviral v-Myc proteins and in human Burkitt and AIDS-related lymphomas, is associated with enhanced transforming activity and tumorigenicity.
7642555	10	72	theme	retroviral	1173:1182	arg1	proteins					1190:1197	retroviral v-Myc proteins	1173:1197	retroviral v-Myc proteins	1173:1197	Mutation of threonine 58, frequently found in retroviral v-Myc proteins and in human Burkitt and AIDS-related lymphomas, is associated with enhanced transforming activity and tumorigenicity.
7642555	1	73	theme	cell	226:229	arg1	proliferation					231:243	cell proliferation	226:243	cell proliferation	226:243	c-Myc is a helix-loop leucine zipper phosphoprotein that heterodimerizes with Max and regulates gene transcription in cell proliferation, cell differentiation, and programmed cell death.
7994575	0	0	theme	molecule	73:80	arg1	CD2					82:84	the human cell adhesion molecule CD2	49:84	the human cell adhesion molecule CD2	49:84	Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at 2.5 A resolution.
7994575	5	1	from	orientation	785:795	arg1	homologues					823:832	the two homologues	815:832	the two homologues	815:832	It is composed of two immunoglobulin superfamily domains similar to those of rat sCD2, but the relative orientation of the domains in the two homologues differs by up to 20 degrees.
7994575	1	2	theme	antigen	136:142	arg1	BACKGROUND					107:116	BACKGROUND	107:116	BACKGROUND: The T-lymphocyte antigen CD2 is an adhesion molecule implicated in immune responses in vivo.	107:210	BACKGROUND: The T-lymphocyte antigen CD2 is an adhesion molecule implicated in immune responses in vivo.
7994575	1	2	theme	antigen	136:142	arg1	molecule					163:170	an adhesion molecule	151:170	an adhesion molecule implicated in immune responses in vivo	151:209	BACKGROUND: The T-lymphocyte antigen CD2 is an adhesion molecule implicated in immune responses in vivo.
7994575	1	2	theme	antigen	136:142	arg1	CD2					144:146	The T-lymphocyte antigen CD2	119:146	The T-lymphocyte antigen CD2	119:146	BACKGROUND: The T-lymphocyte antigen CD2 is an adhesion molecule implicated in immune responses in vivo.
7994575	6	3	theme	charged	905:911	arg1	faces					937:941	ligand binding GFCC'C" faces	914:941	ligand binding GFCC'C" faces	914:941	An interaction involving the flat, highly charged, ligand binding GFCC'C" faces of crystallographically related human sCD2 molecules duplicates, in a different lattice, that observed in the rat sCD2 crystals.
7994575	0	4	theme	adhesion	64:71	arg1	CD2					82:84	the human cell adhesion molecule CD2	49:84	the human cell adhesion molecule CD2	49:84	Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at 2.5 A resolution.
7994575	5	5	theme	immunoglobulin	703:716	arg1	domains					730:736	two immunoglobulin superfamily domains	699:736	two immunoglobulin superfamily domains similar to those of rat sCD2	699:765	It is composed of two immunoglobulin superfamily domains similar to those of rat sCD2, but the relative orientation of the domains in the two homologues differs by up to 20 degrees.
7994575	9	6	theme	residues	1366:1373	arg1	distribution					1342:1353	the distribution	1338:1353	the distribution of charged residues on the binding face	1338:1393	Ligand specificity may be influenced by the distribution of charged residues on the binding face.
7994575	5	7	dep	20	851:852	arg1	to					848:849	to	848:849	to	848:849	It is composed of two immunoglobulin superfamily domains similar to those of rat sCD2, but the relative orientation of the domains in the two homologues differs by up to 20 degrees.
7994575	6	8	theme	flat	892:895	arg1	faces					937:941	ligand binding GFCC'C" faces	914:941	ligand binding GFCC'C" faces	914:941	An interaction involving the flat, highly charged, ligand binding GFCC'C" faces of crystallographically related human sCD2 molecules duplicates, in a different lattice, that observed in the rat sCD2 crystals.
7994575	4	9	theme	crystal	524:530	arg1	structure					532:540	the crystal structure	520:540	the crystal structure of a form of human sCD2 with single N-acetylglucosamine residues	520:605	RESULTS: We therefore determined the crystal structure of a form of human sCD2 with single N-acetylglucosamine residues at each glycosylation site to 2.5 A resolution with an R-factor of 19.3%.
7994575	6	10	theme	molecules	986:994	arg1	faces					937:941	ligand binding GFCC'C" faces	914:941	ligand binding GFCC'C" faces	914:941	An interaction involving the flat, highly charged, ligand binding GFCC'C" faces of crystallographically related human sCD2 molecules duplicates, in a different lattice, that observed in the rat sCD2 crystals.
7994575	4	11	theme	human	555:559	arg1	sCD2					561:564	human sCD2	555:564	human sCD2	555:564	RESULTS: We therefore determined the crystal structure of a form of human sCD2 with single N-acetylglucosamine residues at each glycosylation site to 2.5 A resolution with an R-factor of 19.3%.
7994575	4	12	gly	glycosylation	615:627	arg2	site					629:632	each glycosylation site	610:632	each glycosylation site	610:632	RESULTS: We therefore determined the crystal structure of a form of human sCD2 with single N-acetylglucosamine residues at each glycosylation site to 2.5 A resolution with an R-factor of 19.3%.
7994575	2	13	theme	homologues	259:268	arg1	regions					230:236	The extracellular regions	212:236	The extracellular regions of the human and rat homologues of CD2	212:275	The extracellular regions of the human and rat homologues of CD2 share only 45% sequence identity and bind different protein ligands.
7994575	8	14	theme	structural	1280:1289	arg1	class					1291:1295	this structural class	1275:1295	this structural class	1275:1295	The head-to-head interaction between molecules represents a general model for interactions between adhesion molecules of this structural class.
7994575	0	15	theme	CD2	82:84	arg1	region					39:44	the extracellular region	21:44	the extracellular region of the human cell adhesion molecule CD2	21:84	Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at 2.5 A resolution.
7994575	4	16	with	resolution	643:652	arg1	R-factor					662:669	an R-factor	659:669	an R-factor of 19.3%	659:678	RESULTS: We therefore determined the crystal structure of a form of human sCD2 with single N-acetylglucosamine residues at each glycosylation site to 2.5 A resolution with an R-factor of 19.3%.
7994575	6	17	theme	sCD2	1057:1060	arg1	crystals					1062:1069	the rat sCD2 crystals	1049:1069	the rat sCD2 crystals	1049:1069	An interaction involving the flat, highly charged, ligand binding GFCC'C" faces of crystallographically related human sCD2 molecules duplicates, in a different lattice, that observed in the rat sCD2 crystals.
7994575	7	18	theme	conserved	1128:1136	arg1	feature					1138:1144	a conserved feature	1126:1144	a conserved feature of CD2	1126:1151	CONCLUSIONS: Intramolecular flexibility appears to be a conserved feature of CD2.
7994575	7	18	theme	conserved	1128:1136	arg1	flexibility					1100:1110	Intramolecular flexibility	1085:1110	Intramolecular flexibility	1085:1110	CONCLUSIONS: Intramolecular flexibility appears to be a conserved feature of CD2.
7994575	2	19	theme	rat	255:257	arg1	homologues					259:268	the human and rat homologues	241:268	the human and rat homologues of CD2	241:275	The extracellular regions of the human and rat homologues of CD2 share only 45% sequence identity and bind different protein ligands.
7994575	5	20	theme	relative	776:783	arg1	orientation					785:795	the relative orientation	772:795	the relative orientation of the domains in the two homologues	772:832	It is composed of two immunoglobulin superfamily domains similar to those of rat sCD2, but the relative orientation of the domains in the two homologues differs by up to 20 degrees.
7994575	0	21	theme	A	93:93	arg1	resolution					95:104	2.5 A resolution	89:104	2.5 A resolution	89:104	Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at 2.5 A resolution.
7994575	4	22	theme	%	678:678	arg1	R-factor					662:669	an R-factor	659:669	an R-factor of 19.3%	659:678	RESULTS: We therefore determined the crystal structure of a form of human sCD2 with single N-acetylglucosamine residues at each glycosylation site to 2.5 A resolution with an R-factor of 19.3%.
7994575	3	23	theme	recognition	474:484	arg1	basis					452:456	the structural basis	437:456	the structural basis of cell surface recognition	437:484	Comparison of the human and rat soluble CD2 (sCD2) structures should provide insights into the structural basis of cell surface recognition.
7994575	3	24	theme	soluble	378:384	arg1	structures					397:406	soluble CD2 (sCD2) structures	378:406	soluble CD2 (sCD2) structures	378:406	Comparison of the human and rat soluble CD2 (sCD2) structures should provide insights into the structural basis of cell surface recognition.
7994575	5	25	theme	superfamily	718:728	arg1	domains					730:736	two immunoglobulin superfamily domains	699:736	two immunoglobulin superfamily domains similar to those of rat sCD2	699:765	It is composed of two immunoglobulin superfamily domains similar to those of rat sCD2, but the relative orientation of the domains in the two homologues differs by up to 20 degrees.
7994575	5	26	theme	similar	738:744	arg1	domains					730:736	two immunoglobulin superfamily domains	699:736	two immunoglobulin superfamily domains similar to those of rat sCD2	699:765	It is composed of two immunoglobulin superfamily domains similar to those of rat sCD2, but the relative orientation of the domains in the two homologues differs by up to 20 degrees.
7994575	3	27	dep	human	364:368	arg1	structures					397:406	soluble CD2 (sCD2) structures	378:406	soluble CD2 (sCD2) structures	378:406	Comparison of the human and rat soluble CD2 (sCD2) structures should provide insights into the structural basis of cell surface recognition.
7994575	3	27	dep	human	364:368	arg1	the					360:362	the	360:362	the	360:362	Comparison of the human and rat soluble CD2 (sCD2) structures should provide insights into the structural basis of cell surface recognition.
7994575	2	28	theme	human	245:249	arg1	homologues					259:268	the human and rat homologues	241:268	the human and rat homologues of CD2	241:275	The extracellular regions of the human and rat homologues of CD2 share only 45% sequence identity and bind different protein ligands.
7994575	3	29	theme	sCD2	391:394	arg1	structures					397:406	soluble CD2 (sCD2) structures	378:406	soluble CD2 (sCD2) structures	378:406	Comparison of the human and rat soluble CD2 (sCD2) structures should provide insights into the structural basis of cell surface recognition.
7994575	3	30	theme	surface	466:472	arg1	recognition					474:484	cell surface recognition	461:484	cell surface recognition	461:484	Comparison of the human and rat soluble CD2 (sCD2) structures should provide insights into the structural basis of cell surface recognition.
7994575	6	31	theme	human	975:979	arg1	molecules					986:994	crystallographically related human sCD2 molecules	946:994	crystallographically related human sCD2 molecules	946:994	An interaction involving the flat, highly charged, ligand binding GFCC'C" faces of crystallographically related human sCD2 molecules duplicates, in a different lattice, that observed in the rat sCD2 crystals.
7994575	2	32	dep	%	290:290	arg1	45					288:289	45	288:289	45	288:289	The extracellular regions of the human and rat homologues of CD2 share only 45% sequence identity and bind different protein ligands.
7994575	1	33	theme	adhesion	154:161	arg1	BACKGROUND					107:116	BACKGROUND	107:116	BACKGROUND: The T-lymphocyte antigen CD2 is an adhesion molecule implicated in immune responses in vivo.	107:210	BACKGROUND: The T-lymphocyte antigen CD2 is an adhesion molecule implicated in immune responses in vivo.
7994575	1	33	theme	adhesion	154:161	arg1	molecule					163:170	an adhesion molecule	151:170	an adhesion molecule implicated in immune responses in vivo	151:209	BACKGROUND: The T-lymphocyte antigen CD2 is an adhesion molecule implicated in immune responses in vivo.
7994575	1	33	theme	adhesion	154:161	arg1	CD2					144:146	The T-lymphocyte antigen CD2	119:146	The T-lymphocyte antigen CD2	119:146	BACKGROUND: The T-lymphocyte antigen CD2 is an adhesion molecule implicated in immune responses in vivo.
7994575	0	34	theme	Crystal	0:6	arg1	structure					8:16	Crystal structure	0:16	Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at 2.5 A resolution.	0:105	Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at 2.5 A resolution.
7994575	3	35	theme	CD2	386:388	arg1	structures					397:406	soluble CD2 (sCD2) structures	378:406	soluble CD2 (sCD2) structures	378:406	Comparison of the human and rat soluble CD2 (sCD2) structures should provide insights into the structural basis of cell surface recognition.
7994575	2	36	theme	CD2	273:275	arg1	homologues					259:268	the human and rat homologues	241:268	the human and rat homologues of CD2	241:275	The extracellular regions of the human and rat homologues of CD2 share only 45% sequence identity and bind different protein ligands.
7994575	4	37	theme	single	571:576	arg1	residues					598:605	single N-acetylglucosamine residues	571:605	single N-acetylglucosamine residues	571:605	RESULTS: We therefore determined the crystal structure of a form of human sCD2 with single N-acetylglucosamine residues at each glycosylation site to 2.5 A resolution with an R-factor of 19.3%.
7994575	5	38	theme	rat	758:760	arg1	sCD2					762:765	rat sCD2	758:765	rat sCD2	758:765	It is composed of two immunoglobulin superfamily domains similar to those of rat sCD2, but the relative orientation of the domains in the two homologues differs by up to 20 degrees.
7994575	6	39	theme	rat	1053:1055	arg1	crystals					1062:1069	the rat sCD2 crystals	1049:1069	the rat sCD2 crystals	1049:1069	An interaction involving the flat, highly charged, ligand binding GFCC'C" faces of crystallographically related human sCD2 molecules duplicates, in a different lattice, that observed in the rat sCD2 crystals.
7994575	6	40	theme	different	1013:1021	arg1	lattice					1023:1029	a different lattice	1011:1029	a different lattice	1011:1029	An interaction involving the flat, highly charged, ligand binding GFCC'C" faces of crystallographically related human sCD2 molecules duplicates, in a different lattice, that observed in the rat sCD2 crystals.
7994575	6	41	theme	sCD2	981:984	arg1	molecules					986:994	crystallographically related human sCD2 molecules	946:994	crystallographically related human sCD2 molecules	946:994	An interaction involving the flat, highly charged, ligand binding GFCC'C" faces of crystallographically related human sCD2 molecules duplicates, in a different lattice, that observed in the rat sCD2 crystals.
7994575	3	42	theme	cell	461:464	arg1	recognition					474:484	cell surface recognition	461:484	cell surface recognition	461:484	Comparison of the human and rat soluble CD2 (sCD2) structures should provide insights into the structural basis of cell surface recognition.
7994575	0	43	theme	region	39:44	arg1	structure					8:16	Crystal structure	0:16	Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at 2.5 A resolution.	0:105	Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at 2.5 A resolution.
7994575	3	44	theme	structural	441:450	arg1	basis					452:456	the structural basis	437:456	the structural basis of cell surface recognition	437:484	Comparison of the human and rat soluble CD2 (sCD2) structures should provide insights into the structural basis of cell surface recognition.
7994575	6	45	theme	C	934:934	arg1	faces					937:941	ligand binding GFCC'C" faces	914:941	ligand binding GFCC'C" faces	914:941	An interaction involving the flat, highly charged, ligand binding GFCC'C" faces of crystallographically related human sCD2 molecules duplicates, in a different lattice, that observed in the rat sCD2 crystals.
7994575	4	46	theme	glycosylation	615:627	arg1	site					629:632	each glycosylation site	610:632	each glycosylation site	610:632	RESULTS: We therefore determined the crystal structure of a form of human sCD2 with single N-acetylglucosamine residues at each glycosylation site to 2.5 A resolution with an R-factor of 19.3%.
7994575	1	47	theme	immune	186:191	arg1	responses					193:201	immune responses	186:201	immune responses in vivo	186:209	BACKGROUND: The T-lymphocyte antigen CD2 is an adhesion molecule implicated in immune responses in vivo.
7994575	0	48	theme	extracellular	25:37	arg1	region					39:44	the extracellular region	21:44	the extracellular region of the human cell adhesion molecule CD2	21:84	Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at 2.5 A resolution.
7994575	3	49	theme	rat	374:376	arg1	Comparison					346:355	Comparison	346:355	Comparison of the human and rat soluble CD2 (sCD2) structures	346:406	Comparison of the human and rat soluble CD2 (sCD2) structures should provide insights into the structural basis of cell surface recognition.
7994575	8	50	theme	head-to-head	1158:1169	arg1	interaction					1171:1181	The head-to-head interaction	1154:1181	The head-to-head interaction between molecules	1154:1199	The head-to-head interaction between molecules represents a general model for interactions between adhesion molecules of this structural class.
7994575	6	51	theme	ligand	914:919	arg1	faces					937:941	ligand binding GFCC'C" faces	914:941	ligand binding GFCC'C" faces	914:941	An interaction involving the flat, highly charged, ligand binding GFCC'C" faces of crystallographically related human sCD2 molecules duplicates, in a different lattice, that observed in the rat sCD2 crystals.
7994575	6	52	theme	"	935:935	arg1	faces					937:941	ligand binding GFCC'C" faces	914:941	ligand binding GFCC'C" faces	914:941	An interaction involving the flat, highly charged, ligand binding GFCC'C" faces of crystallographically related human sCD2 molecules duplicates, in a different lattice, that observed in the rat sCD2 crystals.
7994575	4	53	theme	N-acetylglucosamine	578:596	arg1	residues					598:605	single N-acetylglucosamine residues	571:605	single N-acetylglucosamine residues	571:605	RESULTS: We therefore determined the crystal structure of a form of human sCD2 with single N-acetylglucosamine residues at each glycosylation site to 2.5 A resolution with an R-factor of 19.3%.
7994575	5	54	theme	domains	804:810	arg1	orientation					785:795	the relative orientation	772:795	the relative orientation of the domains in the two homologues	772:832	It is composed of two immunoglobulin superfamily domains similar to those of rat sCD2, but the relative orientation of the domains in the two homologues differs by up to 20 degrees.
7994575	9	55	theme	binding	1382:1388	arg1	face					1390:1393	the binding face	1378:1393	the binding face	1378:1393	Ligand specificity may be influenced by the distribution of charged residues on the binding face.
7994575	1	56	from	responses	193:201	arg1	vivo					206:209	vivo	206:209	vivo	206:209	BACKGROUND: The T-lymphocyte antigen CD2 is an adhesion molecule implicated in immune responses in vivo.
7994575	3	57	theme	human	364:368	arg1	Comparison					346:355	Comparison	346:355	Comparison of the human and rat soluble CD2 (sCD2) structures	346:406	Comparison of the human and rat soluble CD2 (sCD2) structures should provide insights into the structural basis of cell surface recognition.
7994575	9	58	theme	Ligand	1298:1303	arg1	specificity					1305:1315	Ligand specificity	1298:1315	Ligand specificity	1298:1315	Ligand specificity may be influenced by the distribution of charged residues on the binding face.
7994575	7	59	theme	Intramolecular	1085:1098	arg1	feature					1138:1144	a conserved feature	1126:1144	a conserved feature of CD2	1126:1151	CONCLUSIONS: Intramolecular flexibility appears to be a conserved feature of CD2.
7994575	7	59	theme	Intramolecular	1085:1098	arg1	flexibility					1100:1110	Intramolecular flexibility	1085:1110	Intramolecular flexibility	1085:1110	CONCLUSIONS: Intramolecular flexibility appears to be a conserved feature of CD2.
7994575	2	60	theme	sequence	292:299	arg1	identity					301:308	only 45% sequence identity	283:308	only 45% sequence identity	283:308	The extracellular regions of the human and rat homologues of CD2 share only 45% sequence identity and bind different protein ligands.
7994575	6	61	theme	binding	921:927	arg1	faces					937:941	ligand binding GFCC'C" faces	914:941	ligand binding GFCC'C" faces	914:941	An interaction involving the flat, highly charged, ligand binding GFCC'C" faces of crystallographically related human sCD2 molecules duplicates, in a different lattice, that observed in the rat sCD2 crystals.
7994575	7	62	theme	CD2	1149:1151	arg1	feature					1138:1144	a conserved feature	1126:1144	a conserved feature of CD2	1126:1151	CONCLUSIONS: Intramolecular flexibility appears to be a conserved feature of CD2.
7994575	7	62	theme	CD2	1149:1151	arg1	flexibility					1100:1110	Intramolecular flexibility	1085:1110	Intramolecular flexibility	1085:1110	CONCLUSIONS: Intramolecular flexibility appears to be a conserved feature of CD2.
7994575	2	63	dep	identity	301:308	arg1	%					290:290	%	290:290	%	290:290	The extracellular regions of the human and rat homologues of CD2 share only 45% sequence identity and bind different protein ligands.
7994575	6	64	theme	GFCC	929:932	arg1	faces					937:941	ligand binding GFCC'C" faces	914:941	ligand binding GFCC'C" faces	914:941	An interaction involving the flat, highly charged, ligand binding GFCC'C" faces of crystallographically related human sCD2 molecules duplicates, in a different lattice, that observed in the rat sCD2 crystals.
7994575	8	65	theme	adhesion	1253:1260	arg1	molecules					1262:1270	adhesion molecules	1253:1270	adhesion molecules of this structural class	1253:1295	The head-to-head interaction between molecules represents a general model for interactions between adhesion molecules of this structural class.
7994575	8	66	theme	general	1214:1220	arg1	model					1222:1226	a general model	1212:1226	a general model for interactions between adhesion molecules of this structural class	1212:1295	The head-to-head interaction between molecules represents a general model for interactions between adhesion molecules of this structural class.
7994575	1	67	theme	T-lymphocyte	123:134	arg1	BACKGROUND					107:116	BACKGROUND	107:116	BACKGROUND: The T-lymphocyte antigen CD2 is an adhesion molecule implicated in immune responses in vivo.	107:210	BACKGROUND: The T-lymphocyte antigen CD2 is an adhesion molecule implicated in immune responses in vivo.
7994575	1	67	theme	T-lymphocyte	123:134	arg1	molecule					163:170	an adhesion molecule	151:170	an adhesion molecule implicated in immune responses in vivo	151:209	BACKGROUND: The T-lymphocyte antigen CD2 is an adhesion molecule implicated in immune responses in vivo.
7994575	1	67	theme	T-lymphocyte	123:134	arg1	CD2					144:146	The T-lymphocyte antigen CD2	119:146	The T-lymphocyte antigen CD2	119:146	BACKGROUND: The T-lymphocyte antigen CD2 is an adhesion molecule implicated in immune responses in vivo.
7994575	4	68	theme	form	547:550	arg1	structure					532:540	the crystal structure	520:540	the crystal structure of a form of human sCD2 with single N-acetylglucosamine residues	520:605	RESULTS: We therefore determined the crystal structure of a form of human sCD2 with single N-acetylglucosamine residues at each glycosylation site to 2.5 A resolution with an R-factor of 19.3%.
7994575	0	69	theme	cell	59:62	arg1	CD2					82:84	the human cell adhesion molecule CD2	49:84	the human cell adhesion molecule CD2	49:84	Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at 2.5 A resolution.
7994575	8	70	theme	class	1291:1295	arg1	molecules					1262:1270	adhesion molecules	1253:1270	adhesion molecules of this structural class	1253:1295	The head-to-head interaction between molecules represents a general model for interactions between adhesion molecules of this structural class.
7994575	4	71	with	structure	532:540	arg1	residues					598:605	single N-acetylglucosamine residues	571:605	single N-acetylglucosamine residues	571:605	RESULTS: We therefore determined the crystal structure of a form of human sCD2 with single N-acetylglucosamine residues at each glycosylation site to 2.5 A resolution with an R-factor of 19.3%.
7994575	2	72	theme	protein	329:335	arg1	ligands					337:343	different protein ligands	319:343	different protein ligands	319:343	The extracellular regions of the human and rat homologues of CD2 share only 45% sequence identity and bind different protein ligands.
7994575	6	73	theme	related	967:973	arg1	molecules					986:994	crystallographically related human sCD2 molecules	946:994	crystallographically related human sCD2 molecules	946:994	An interaction involving the flat, highly charged, ligand binding GFCC'C" faces of crystallographically related human sCD2 molecules duplicates, in a different lattice, that observed in the rat sCD2 crystals.
7994575	4	74	theme	sCD2	561:564	arg1	form					547:550	a form	545:550	a form of human sCD2	545:564	RESULTS: We therefore determined the crystal structure of a form of human sCD2 with single N-acetylglucosamine residues at each glycosylation site to 2.5 A resolution with an R-factor of 19.3%.
7994575	0	75	theme	human	53:57	arg1	CD2					82:84	the human cell adhesion molecule CD2	49:84	the human cell adhesion molecule CD2	49:84	Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at 2.5 A resolution.
7994575	9	76	theme	charged	1358:1364	arg1	residues					1366:1373	charged residues	1358:1373	charged residues	1358:1373	Ligand specificity may be influenced by the distribution of charged residues on the binding face.
7994575	2	77	theme	extracellular	216:228	arg1	regions					230:236	The extracellular regions	212:236	The extracellular regions of the human and rat homologues of CD2	212:275	The extracellular regions of the human and rat homologues of CD2 share only 45% sequence identity and bind different protein ligands.
7994575	9	78	from	distribution	1342:1353	arg1	face					1390:1393	the binding face	1378:1393	the binding face	1378:1393	Ligand specificity may be influenced by the distribution of charged residues on the binding face.
7994575	2	79	theme	different	319:327	arg1	ligands					337:343	different protein ligands	319:343	different protein ligands	319:343	The extracellular regions of the human and rat homologues of CD2 share only 45% sequence identity and bind different protein ligands.
7994575	0	80	from	resolution	95:104	arg1	structure					8:16	Crystal structure	0:16	Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at 2.5 A resolution.	0:105	Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at 2.5 A resolution.
9151832	3	0	from	pretreatment	579:590	arg1	Mutation					493:500	Mutation	493:500	Mutation of the two N-linked glycosylation sites on CXCR-4 (N11-->I, and N176-->Q) or pretreatment of CCC or Mv-1-lu cells expressing wild-type CXCR-4 with the glycosylation inhibitor tunicamycin	493:687	Mutation of the two N-linked glycosylation sites on CXCR-4 (N11-->I, and N176-->Q) or pretreatment of CCC or Mv-1-lu cells expressing wild-type CXCR-4 with the glycosylation inhibitor tunicamycin increased fusion and entry by ROD/B.
9151832	1	1	theme	CD4-negative	290:301	arg1	cells					303:307	CD4-negative cells	290:307	CD4-negative cells	290:307	The human immunodeficiency virus type 2 (HIV-2) strain ROD/B can efficiently use the 7tm chemokine receptor CXCR-4 as a primary receptor to enter CD4-negative cells.
9151832	3	2	theme	cells	610:614	arg1	pretreatment					579:590	pretreatment	579:590	pretreatment of CCC or Mv-1-lu cells expressing wild-type CXCR-4 with the glycosylation inhibitor tunicamycin	579:687	Mutation of the two N-linked glycosylation sites on CXCR-4 (N11-->I, and N176-->Q) or pretreatment of CCC or Mv-1-lu cells expressing wild-type CXCR-4 with the glycosylation inhibitor tunicamycin increased fusion and entry by ROD/B.
9151832	3	2	theme	cells	610:614	arg1	CXCR-4					545:550	CXCR-4	545:550	CXCR-4 (N11-->I, and N176-->Q)	545:574	Mutation of the two N-linked glycosylation sites on CXCR-4 (N11-->I, and N176-->Q) or pretreatment of CCC or Mv-1-lu cells expressing wild-type CXCR-4 with the glycosylation inhibitor tunicamycin increased fusion and entry by ROD/B.
9151832	3	3	theme	CCC	595:597	arg1	cells					610:614	CCC or Mv-1-lu cells	595:614	CCC or Mv-1-lu cells expressing wild-type CXCR-4 with the glycosylation inhibitor tunicamycin	595:687	Mutation of the two N-linked glycosylation sites on CXCR-4 (N11-->I, and N176-->Q) or pretreatment of CCC or Mv-1-lu cells expressing wild-type CXCR-4 with the glycosylation inhibitor tunicamycin increased fusion and entry by ROD/B.
9151832	6	4	theme	domain	1129:1134	arg1	Deletion					1086:1093	Deletion	1086:1093	Deletion of the C-terminal (intracellular) domain of CXCR-4	1086:1144	Deletion of the C-terminal (intracellular) domain of CXCR-4 did not significantly affect entry by ROD/B, indicating that intracellular signalling through this domain does not play a significant role in entry by HIV-2.
9151832	4	5	theme	cell-free	815:823	arg1	infection					825:833	cell-free infection	815:833	cell-free infection by ROD/B and complete inhibition of cell-cell fusion by both ROD/B and another HIV-2 strain, CBL23	815:932	Deletion of portions of the N terminus of CXCR-4 resulted in a 3- to 10-fold decrease in cell-free infection by ROD/B and complete inhibition of cell-cell fusion by both ROD/B and another HIV-2 strain, CBL23.
9151832	5	6	theme	ROD/B	1055:1059	arg1	fusion					1045:1050	the efficient fusion	1031:1050	the efficient fusion of ROD/B with CD4-negative cells	1031:1083	These data suggest that the N-terminal domain of CXCR-4 is involved in but is not essential for the efficient fusion of ROD/B with CD4-negative cells.
9151832	2	7	dep	have	313:316	arg1	restrictive					401:411	restrictive	401:411	restrictive	401:411	We have stably expressed CXCR-4 on mink lung Mv-1-lu and feline kidney CCC cells (normally restrictive to HIV entry) and have shown efficient fusion, entry, and replication of ROD/B.
9151832	6	8	theme	intracellular	1114:1126	arg1	CXCR-4					1139:1144	CXCR-4	1139:1144	CXCR-4	1139:1144	Deletion of the C-terminal (intracellular) domain of CXCR-4 did not significantly affect entry by ROD/B, indicating that intracellular signalling through this domain does not play a significant role in entry by HIV-2.
9151832	6	8	theme	intracellular	1114:1126	arg1	domain					1129:1134	the C-terminal (intracellular) domain	1098:1134	the C-terminal (intracellular) domain of CXCR-4	1098:1144	Deletion of the C-terminal (intracellular) domain of CXCR-4 did not significantly affect entry by ROD/B, indicating that intracellular signalling through this domain does not play a significant role in entry by HIV-2.
9151832	5	9	theme	CXCR-4	984:989	arg1	CXCR-4					984:989	CXCR-4	984:989	CXCR-4	984:989	These data suggest that the N-terminal domain of CXCR-4 is involved in but is not essential for the efficient fusion of ROD/B with CD4-negative cells.
9151832	5	9	theme	CXCR-4	984:989	arg1	domain					974:979	the N-terminal domain	959:979	the N-terminal domain of CXCR-4	959:989	These data suggest that the N-terminal domain of CXCR-4 is involved in but is not essential for the efficient fusion of ROD/B with CD4-negative cells.
9151832	5	9	theme	CXCR-4	984:989	arg1	essential					1017:1025	essential	1017:1025	essential	1017:1025	These data suggest that the N-terminal domain of CXCR-4 is involved in but is not essential for the efficient fusion of ROD/B with CD4-negative cells.
9151832	3	10	from	sites	536:540	arg1	CXCR-4					545:550	CXCR-4	545:550	CXCR-4 (N11-->I, and N176-->Q)	545:574	Mutation of the two N-linked glycosylation sites on CXCR-4 (N11-->I, and N176-->Q) or pretreatment of CCC or Mv-1-lu cells expressing wild-type CXCR-4 with the glycosylation inhibitor tunicamycin increased fusion and entry by ROD/B.
9151832	3	10	from	sites	536:540	arg1	pretreatment					579:590	pretreatment	579:590	pretreatment of CCC or Mv-1-lu cells expressing wild-type CXCR-4 with the glycosylation inhibitor tunicamycin	579:687	Mutation of the two N-linked glycosylation sites on CXCR-4 (N11-->I, and N176-->Q) or pretreatment of CCC or Mv-1-lu cells expressing wild-type CXCR-4 with the glycosylation inhibitor tunicamycin increased fusion and entry by ROD/B.
9151832	1	11	theme	7tm	229:231	arg1	CXCR-4					252:257	the 7tm chemokine receptor CXCR-4	225:257	the 7tm chemokine receptor CXCR-4 as a primary receptor	225:279	The human immunodeficiency virus type 2 (HIV-2) strain ROD/B can efficiently use the 7tm chemokine receptor CXCR-4 as a primary receptor to enter CD4-negative cells.
9151832	0	12	theme	N-terminal	95:104	arg1	CXCR-4					116:121	CXCR-4	116:121	CXCR-4	116:121	CD4-independent infection by human immunodeficiency virus type 2 strain ROD/B: the role of the N-terminal domain of CXCR-4 in fusion and entry.
9151832	0	12	theme	N-terminal	95:104	arg1	domain					106:111	the N-terminal domain	91:111	the N-terminal domain of CXCR-4	91:121	CD4-independent infection by human immunodeficiency virus type 2 strain ROD/B: the role of the N-terminal domain of CXCR-4 in fusion and entry.
9151832	2	13	contain	have	313:316	arg2	CXCR-4					335:340	stably expressed CXCR-4	318:340	stably expressed CXCR-4 on mink lung Mv-1-lu and feline kidney CCC cells	318:389	We have stably expressed CXCR-4 on mink lung Mv-1-lu and feline kidney CCC cells (normally restrictive to HIV entry) and have shown efficient fusion, entry, and replication of ROD/B.
9151832	2	13	contain	have	313:316	arg1	We					310:311	We	310:311	We	310:311	We have stably expressed CXCR-4 on mink lung Mv-1-lu and feline kidney CCC cells (normally restrictive to HIV entry) and have shown efficient fusion, entry, and replication of ROD/B.
9151832	4	14	theme	terminus	756:763	arg1	portions					738:745	portions	738:745	portions of the N terminus of CXCR-4	738:773	Deletion of portions of the N terminus of CXCR-4 resulted in a 3- to 10-fold decrease in cell-free infection by ROD/B and complete inhibition of cell-cell fusion by both ROD/B and another HIV-2 strain, CBL23.
9151832	2	15	theme	lung	350:353	arg1	Mv-1-lu					355:361	mink lung Mv-1-lu and feline kidney CCC cells	345:389	Mv-1-lu	355:361	We have stably expressed CXCR-4 on mink lung Mv-1-lu and feline kidney CCC cells (normally restrictive to HIV entry) and have shown efficient fusion, entry, and replication of ROD/B.
9151832	2	16	theme	efficient	442:450	arg1	fusion					452:457	efficient fusion	442:457	efficient fusion	442:457	We have stably expressed CXCR-4 on mink lung Mv-1-lu and feline kidney CCC cells (normally restrictive to HIV entry) and have shown efficient fusion, entry, and replication of ROD/B.
9151832	4	17	theme	N	754:754	arg1	terminus					756:763	the N terminus	750:763	the N terminus of CXCR-4	750:773	Deletion of portions of the N terminus of CXCR-4 resulted in a 3- to 10-fold decrease in cell-free infection by ROD/B and complete inhibition of cell-cell fusion by both ROD/B and another HIV-2 strain, CBL23.
9151832	3	18	from	CXCR-4	545:550	arg1	Mutation					493:500	Mutation	493:500	Mutation of the two N-linked glycosylation sites on CXCR-4 (N11-->I, and N176-->Q) or pretreatment of CCC or Mv-1-lu cells expressing wild-type CXCR-4 with the glycosylation inhibitor tunicamycin	493:687	Mutation of the two N-linked glycosylation sites on CXCR-4 (N11-->I, and N176-->Q) or pretreatment of CCC or Mv-1-lu cells expressing wild-type CXCR-4 with the glycosylation inhibitor tunicamycin increased fusion and entry by ROD/B.
9151832	1	19	theme	human	148:152	arg1	type					177:180	The human immunodeficiency virus type 2	144:182	The human immunodeficiency virus type 2 (HIV-2) strain ROD/B	144:203	The human immunodeficiency virus type 2 (HIV-2) strain ROD/B can efficiently use the 7tm chemokine receptor CXCR-4 as a primary receptor to enter CD4-negative cells.
9151832	1	19	theme	human	148:152	arg1	HIV-2					185:189	HIV-2	185:189	HIV-2	185:189	The human immunodeficiency virus type 2 (HIV-2) strain ROD/B can efficiently use the 7tm chemokine receptor CXCR-4 as a primary receptor to enter CD4-negative cells.
9151832	2	20	theme	HIV	416:418	arg1	entry					420:424	HIV entry	416:424	HIV entry	416:424	We have stably expressed CXCR-4 on mink lung Mv-1-lu and feline kidney CCC cells (normally restrictive to HIV entry) and have shown efficient fusion, entry, and replication of ROD/B.
9151832	3	21	theme	wild-type	627:635	arg1	CXCR-4					637:642	wild-type CXCR-4	627:642	wild-type CXCR-4	627:642	Mutation of the two N-linked glycosylation sites on CXCR-4 (N11-->I, and N176-->Q) or pretreatment of CCC or Mv-1-lu cells expressing wild-type CXCR-4 with the glycosylation inhibitor tunicamycin increased fusion and entry by ROD/B.
9151832	4	22	theme	CXCR-4	768:773	arg1	terminus					756:763	the N terminus	750:763	the N terminus of CXCR-4	750:773	Deletion of portions of the N terminus of CXCR-4 resulted in a 3- to 10-fold decrease in cell-free infection by ROD/B and complete inhibition of cell-cell fusion by both ROD/B and another HIV-2 strain, CBL23.
9151832	3	23	theme	inhibitor	667:675	arg1	tunicamycin					677:687	the glycosylation inhibitor tunicamycin	649:687	the glycosylation inhibitor tunicamycin	649:687	Mutation of the two N-linked glycosylation sites on CXCR-4 (N11-->I, and N176-->Q) or pretreatment of CCC or Mv-1-lu cells expressing wild-type CXCR-4 with the glycosylation inhibitor tunicamycin increased fusion and entry by ROD/B.
9151832	4	24	theme	complete	848:855	arg1	inhibition					857:866	complete inhibition	848:866	complete inhibition of cell-cell fusion by both ROD/B and another HIV-2 strain, CBL23	848:932	Deletion of portions of the N terminus of CXCR-4 resulted in a 3- to 10-fold decrease in cell-free infection by ROD/B and complete inhibition of cell-cell fusion by both ROD/B and another HIV-2 strain, CBL23.
9151832	1	25	theme	immunodeficiency	154:169	arg1	type					177:180	The human immunodeficiency virus type 2	144:182	The human immunodeficiency virus type 2 (HIV-2) strain ROD/B	144:203	The human immunodeficiency virus type 2 (HIV-2) strain ROD/B can efficiently use the 7tm chemokine receptor CXCR-4 as a primary receptor to enter CD4-negative cells.
9151832	1	25	theme	immunodeficiency	154:169	arg1	HIV-2					185:189	HIV-2	185:189	HIV-2	185:189	The human immunodeficiency virus type 2 (HIV-2) strain ROD/B can efficiently use the 7tm chemokine receptor CXCR-4 as a primary receptor to enter CD4-negative cells.
9151832	0	26	theme	CD4-independent	0:14	arg1	infection					16:24	CD4-independent infection	0:24	CD4-independent infection by human immunodeficiency virus type 2 strain ROD/B: the role of the N-terminal domain of CXCR-4 in fusion and entry.	0:142	CD4-independent infection by human immunodeficiency virus type 2 strain ROD/B: the role of the N-terminal domain of CXCR-4 in fusion and entry.
9151832	1	27	theme	chemokine	233:241	arg1	CXCR-4					252:257	the 7tm chemokine receptor CXCR-4	225:257	the 7tm chemokine receptor CXCR-4 as a primary receptor	225:279	The human immunodeficiency virus type 2 (HIV-2) strain ROD/B can efficiently use the 7tm chemokine receptor CXCR-4 as a primary receptor to enter CD4-negative cells.
9151832	4	28	theme	HIV-2	914:918	arg1	CBL23					928:932	CBL23	928:932	CBL23	928:932	Deletion of portions of the N terminus of CXCR-4 resulted in a 3- to 10-fold decrease in cell-free infection by ROD/B and complete inhibition of cell-cell fusion by both ROD/B and another HIV-2 strain, CBL23.
9151832	4	28	theme	HIV-2	914:918	arg1	strain					920:925	another HIV-2 strain	906:925	another HIV-2 strain	906:925	Deletion of portions of the N terminus of CXCR-4 resulted in a 3- to 10-fold decrease in cell-free infection by ROD/B and complete inhibition of cell-cell fusion by both ROD/B and another HIV-2 strain, CBL23.
9151832	6	29	theme	CXCR-4	1139:1144	arg1	CXCR-4					1139:1144	CXCR-4	1139:1144	CXCR-4	1139:1144	Deletion of the C-terminal (intracellular) domain of CXCR-4 did not significantly affect entry by ROD/B, indicating that intracellular signalling through this domain does not play a significant role in entry by HIV-2.
9151832	6	29	theme	CXCR-4	1139:1144	arg1	domain					1129:1134	the C-terminal (intracellular) domain	1098:1134	the C-terminal (intracellular) domain of CXCR-4	1098:1144	Deletion of the C-terminal (intracellular) domain of CXCR-4 did not significantly affect entry by ROD/B, indicating that intracellular signalling through this domain does not play a significant role in entry by HIV-2.
9151832	6	30	theme	intracellular	1207:1219	arg1	signalling					1221:1230	intracellular signalling	1207:1230	intracellular signalling through this domain	1207:1250	Deletion of the C-terminal (intracellular) domain of CXCR-4 did not significantly affect entry by ROD/B, indicating that intracellular signalling through this domain does not play a significant role in entry by HIV-2.
9151832	1	31	theme	virus	171:175	arg1	type					177:180	The human immunodeficiency virus type 2	144:182	The human immunodeficiency virus type 2 (HIV-2) strain ROD/B	144:203	The human immunodeficiency virus type 2 (HIV-2) strain ROD/B can efficiently use the 7tm chemokine receptor CXCR-4 as a primary receptor to enter CD4-negative cells.
9151832	1	31	theme	virus	171:175	arg1	HIV-2					185:189	HIV-2	185:189	HIV-2	185:189	The human immunodeficiency virus type 2 (HIV-2) strain ROD/B can efficiently use the 7tm chemokine receptor CXCR-4 as a primary receptor to enter CD4-negative cells.
9151832	0	32	theme	human	29:33	arg1	type					58:61	human immunodeficiency virus type 2	29:63	human immunodeficiency virus type 2 strain ROD/B	29:76	CD4-independent infection by human immunodeficiency virus type 2 strain ROD/B: the role of the N-terminal domain of CXCR-4 in fusion and entry.
9151832	1	33	theme	receptor	243:250	arg1	CXCR-4					252:257	the 7tm chemokine receptor CXCR-4	225:257	the 7tm chemokine receptor CXCR-4 as a primary receptor	225:279	The human immunodeficiency virus type 2 (HIV-2) strain ROD/B can efficiently use the 7tm chemokine receptor CXCR-4 as a primary receptor to enter CD4-negative cells.
9151832	4	34	theme	portions	738:745	arg1	Deletion					726:733	Deletion	726:733	Deletion of portions of the N terminus of CXCR-4	726:773	Deletion of portions of the N terminus of CXCR-4 resulted in a 3- to 10-fold decrease in cell-free infection by ROD/B and complete inhibition of cell-cell fusion by both ROD/B and another HIV-2 strain, CBL23.
9151832	1	35	theme	type	177:180	arg1	ROD/B					199:203	The human immunodeficiency virus type 2 (HIV-2) strain ROD/B	144:203	The human immunodeficiency virus type 2 (HIV-2) strain ROD/B	144:203	The human immunodeficiency virus type 2 (HIV-2) strain ROD/B can efficiently use the 7tm chemokine receptor CXCR-4 as a primary receptor to enter CD4-negative cells.
9151832	2	36	theme	CCC	381:383	arg1	cells					385:389	mink lung Mv-1-lu and feline kidney CCC cells	345:389	cells	385:389	We have stably expressed CXCR-4 on mink lung Mv-1-lu and feline kidney CCC cells (normally restrictive to HIV entry) and have shown efficient fusion, entry, and replication of ROD/B.
9151832	0	37	theme	domain	106:111	arg1	role					83:86	the role	79:86	CD4-independent infection by human immunodeficiency virus type 2 strain ROD/B: the role of the N-terminal domain of CXCR-4 in fusion and entry.	0:142	CD4-independent infection by human immunodeficiency virus type 2 strain ROD/B: the role of the N-terminal domain of CXCR-4 in fusion and entry.
9151832	4	38	dep	10-fold	795:801	arg1	to					792:793	to	792:793	to	792:793	Deletion of portions of the N terminus of CXCR-4 resulted in a 3- to 10-fold decrease in cell-free infection by ROD/B and complete inhibition of cell-cell fusion by both ROD/B and another HIV-2 strain, CBL23.
9151832	2	39	theme	feline	367:372	arg1	cells					385:389	mink lung Mv-1-lu and feline kidney CCC cells	345:389	cells	385:389	We have stably expressed CXCR-4 on mink lung Mv-1-lu and feline kidney CCC cells (normally restrictive to HIV entry) and have shown efficient fusion, entry, and replication of ROD/B.
9151832	0	40	theme	virus	52:56	arg1	type					58:61	human immunodeficiency virus type 2	29:63	human immunodeficiency virus type 2 strain ROD/B	29:76	CD4-independent infection by human immunodeficiency virus type 2 strain ROD/B: the role of the N-terminal domain of CXCR-4 in fusion and entry.
9151832	3	41	theme	glycosylation	653:665	arg1	tunicamycin					677:687	the glycosylation inhibitor tunicamycin	649:687	the glycosylation inhibitor tunicamycin	649:687	Mutation of the two N-linked glycosylation sites on CXCR-4 (N11-->I, and N176-->Q) or pretreatment of CCC or Mv-1-lu cells expressing wild-type CXCR-4 with the glycosylation inhibitor tunicamycin increased fusion and entry by ROD/B.
9151832	5	42	theme	N-terminal	963:972	arg1	CXCR-4					984:989	CXCR-4	984:989	CXCR-4	984:989	These data suggest that the N-terminal domain of CXCR-4 is involved in but is not essential for the efficient fusion of ROD/B with CD4-negative cells.
9151832	5	42	theme	N-terminal	963:972	arg1	domain					974:979	the N-terminal domain	959:979	the N-terminal domain of CXCR-4	959:989	These data suggest that the N-terminal domain of CXCR-4 is involved in but is not essential for the efficient fusion of ROD/B with CD4-negative cells.
9151832	5	42	theme	N-terminal	963:972	arg1	essential					1017:1025	essential	1017:1025	essential	1017:1025	These data suggest that the N-terminal domain of CXCR-4 is involved in but is not essential for the efficient fusion of ROD/B with CD4-negative cells.
9151832	3	43	theme	N-linked	513:520	arg1	sites					536:540	the two N-linked glycosylation sites	505:540	the two N-linked glycosylation sites on CXCR-4 (N11-->I, and N176-->Q) or pretreatment of CCC or Mv-1-lu cells expressing wild-type CXCR-4 with the glycosylation inhibitor tunicamycin	505:687	Mutation of the two N-linked glycosylation sites on CXCR-4 (N11-->I, and N176-->Q) or pretreatment of CCC or Mv-1-lu cells expressing wild-type CXCR-4 with the glycosylation inhibitor tunicamycin increased fusion and entry by ROD/B.
9151832	3	44	gly	glycosylation	522:534	arg2	sites					536:540	the two N-linked glycosylation sites	505:540	the two N-linked glycosylation sites on CXCR-4 (N11-->I, and N176-->Q) or pretreatment of CCC or Mv-1-lu cells expressing wild-type CXCR-4 with the glycosylation inhibitor tunicamycin	505:687	Mutation of the two N-linked glycosylation sites on CXCR-4 (N11-->I, and N176-->Q) or pretreatment of CCC or Mv-1-lu cells expressing wild-type CXCR-4 with the glycosylation inhibitor tunicamycin increased fusion and entry by ROD/B.
9151832	3	44	gly	glycosylation	522:534	arg2	two					509:511	two	509:511	two	509:511	Mutation of the two N-linked glycosylation sites on CXCR-4 (N11-->I, and N176-->Q) or pretreatment of CCC or Mv-1-lu cells expressing wild-type CXCR-4 with the glycosylation inhibitor tunicamycin increased fusion and entry by ROD/B.
9151832	3	45	dep	CXCR-4	545:550	arg1	N11-->I					553:559	N11-->I	553:559	N11-->I	553:559	Mutation of the two N-linked glycosylation sites on CXCR-4 (N11-->I, and N176-->Q) or pretreatment of CCC or Mv-1-lu cells expressing wild-type CXCR-4 with the glycosylation inhibitor tunicamycin increased fusion and entry by ROD/B.
9151832	3	45	dep	CXCR-4	545:550	arg1	N176-->Q					566:573	N176-->Q	566:573	N176-->Q	566:573	Mutation of the two N-linked glycosylation sites on CXCR-4 (N11-->I, and N176-->Q) or pretreatment of CCC or Mv-1-lu cells expressing wild-type CXCR-4 with the glycosylation inhibitor tunicamycin increased fusion and entry by ROD/B.
9151832	0	46	theme	immunodeficiency	35:50	arg1	type					58:61	human immunodeficiency virus type 2	29:63	human immunodeficiency virus type 2 strain ROD/B	29:76	CD4-independent infection by human immunodeficiency virus type 2 strain ROD/B: the role of the N-terminal domain of CXCR-4 in fusion and entry.
9151832	0	47	theme	CXCR-4	116:121	arg1	CXCR-4					116:121	CXCR-4	116:121	CXCR-4	116:121	CD4-independent infection by human immunodeficiency virus type 2 strain ROD/B: the role of the N-terminal domain of CXCR-4 in fusion and entry.
9151832	0	47	theme	CXCR-4	116:121	arg1	domain					106:111	the N-terminal domain	91:111	the N-terminal domain of CXCR-4	91:121	CD4-independent infection by human immunodeficiency virus type 2 strain ROD/B: the role of the N-terminal domain of CXCR-4 in fusion and entry.
9151832	3	48	theme	glycosylation	522:534	arg1	sites					536:540	the two N-linked glycosylation sites	505:540	the two N-linked glycosylation sites on CXCR-4 (N11-->I, and N176-->Q) or pretreatment of CCC or Mv-1-lu cells expressing wild-type CXCR-4 with the glycosylation inhibitor tunicamycin	505:687	Mutation of the two N-linked glycosylation sites on CXCR-4 (N11-->I, and N176-->Q) or pretreatment of CCC or Mv-1-lu cells expressing wild-type CXCR-4 with the glycosylation inhibitor tunicamycin increased fusion and entry by ROD/B.
9151832	5	49	theme	CD4-negative	1066:1077	arg1	cells					1079:1083	CD4-negative cells	1066:1083	CD4-negative cells	1066:1083	These data suggest that the N-terminal domain of CXCR-4 is involved in but is not essential for the efficient fusion of ROD/B with CD4-negative cells.
9151832	3	50	link	N-linked	513:520	arg1	sites					536:540	the two N-linked glycosylation sites	505:540	the two N-linked glycosylation sites on CXCR-4 (N11-->I, and N176-->Q) or pretreatment of CCC or Mv-1-lu cells expressing wild-type CXCR-4 with the glycosylation inhibitor tunicamycin	505:687	Mutation of the two N-linked glycosylation sites on CXCR-4 (N11-->I, and N176-->Q) or pretreatment of CCC or Mv-1-lu cells expressing wild-type CXCR-4 with the glycosylation inhibitor tunicamycin increased fusion and entry by ROD/B.
9151832	1	51	theme	primary	264:270	arg1	receptor					272:279	a primary receptor	262:279	a primary receptor	262:279	The human immunodeficiency virus type 2 (HIV-2) strain ROD/B can efficiently use the 7tm chemokine receptor CXCR-4 as a primary receptor to enter CD4-negative cells.
9151832	4	52	theme	10-fold	795:801	arg1	decrease					803:810	a 3- to 10-fold decrease	787:810	a 3- to 10-fold decrease in cell-free infection by ROD/B and complete inhibition of cell-cell fusion by both ROD/B and another HIV-2 strain, CBL23	787:932	Deletion of portions of the N terminus of CXCR-4 resulted in a 3- to 10-fold decrease in cell-free infection by ROD/B and complete inhibition of cell-cell fusion by both ROD/B and another HIV-2 strain, CBL23.
9151832	4	53	theme	cell-cell	871:879	arg1	fusion					881:886	cell-cell fusion	871:886	cell-cell fusion	871:886	Deletion of portions of the N terminus of CXCR-4 resulted in a 3- to 10-fold decrease in cell-free infection by ROD/B and complete inhibition of cell-cell fusion by both ROD/B and another HIV-2 strain, CBL23.
9151832	6	54	theme	C-terminal	1102:1111	arg1	CXCR-4					1139:1144	CXCR-4	1139:1144	CXCR-4	1139:1144	Deletion of the C-terminal (intracellular) domain of CXCR-4 did not significantly affect entry by ROD/B, indicating that intracellular signalling through this domain does not play a significant role in entry by HIV-2.
9151832	6	54	theme	C-terminal	1102:1111	arg1	domain					1129:1134	the C-terminal (intracellular) domain	1098:1134	the C-terminal (intracellular) domain of CXCR-4	1098:1144	Deletion of the C-terminal (intracellular) domain of CXCR-4 did not significantly affect entry by ROD/B, indicating that intracellular signalling through this domain does not play a significant role in entry by HIV-2.
9151832	2	55	from	CXCR-4	335:340	arg1	cells					385:389	mink lung Mv-1-lu and feline kidney CCC cells	345:389	cells	385:389	We have stably expressed CXCR-4 on mink lung Mv-1-lu and feline kidney CCC cells (normally restrictive to HIV entry) and have shown efficient fusion, entry, and replication of ROD/B.
9151832	2	55	from	CXCR-4	335:340	arg1	Mv-1-lu					355:361	mink lung Mv-1-lu and feline kidney CCC cells	345:389	Mv-1-lu	355:361	We have stably expressed CXCR-4 on mink lung Mv-1-lu and feline kidney CCC cells (normally restrictive to HIV entry) and have shown efficient fusion, entry, and replication of ROD/B.
9151832	0	56	theme	type	58:61	arg1	ROD/B					72:76	human immunodeficiency virus type 2 strain ROD/B	29:76	human immunodeficiency virus type 2 strain ROD/B	29:76	CD4-independent infection by human immunodeficiency virus type 2 strain ROD/B: the role of the N-terminal domain of CXCR-4 in fusion and entry.
9151832	5	57	theme	efficient	1035:1043	arg1	fusion					1045:1050	the efficient fusion	1031:1050	the efficient fusion of ROD/B with CD4-negative cells	1031:1083	These data suggest that the N-terminal domain of CXCR-4 is involved in but is not essential for the efficient fusion of ROD/B with CD4-negative cells.
9151832	4	58	from	decrease	803:810	arg1	infection					825:833	cell-free infection	815:833	cell-free infection by ROD/B and complete inhibition of cell-cell fusion by both ROD/B and another HIV-2 strain, CBL23	815:932	Deletion of portions of the N terminus of CXCR-4 resulted in a 3- to 10-fold decrease in cell-free infection by ROD/B and complete inhibition of cell-cell fusion by both ROD/B and another HIV-2 strain, CBL23.
9151832	5	59	with	fusion	1045:1050	arg1	cells					1079:1083	CD4-negative cells	1066:1083	CD4-negative cells	1066:1083	These data suggest that the N-terminal domain of CXCR-4 is involved in but is not essential for the efficient fusion of ROD/B with CD4-negative cells.
9151832	3	60	theme	sites	536:540	arg1	Mutation					493:500	Mutation	493:500	Mutation of the two N-linked glycosylation sites on CXCR-4 (N11-->I, and N176-->Q) or pretreatment of CCC or Mv-1-lu cells expressing wild-type CXCR-4 with the glycosylation inhibitor tunicamycin	493:687	Mutation of the two N-linked glycosylation sites on CXCR-4 (N11-->I, and N176-->Q) or pretreatment of CCC or Mv-1-lu cells expressing wild-type CXCR-4 with the glycosylation inhibitor tunicamycin increased fusion and entry by ROD/B.
9151832	2	61	theme	ROD/B	486:490	arg1	replication					471:481	replication	471:481	replication	471:481	We have stably expressed CXCR-4 on mink lung Mv-1-lu and feline kidney CCC cells (normally restrictive to HIV entry) and have shown efficient fusion, entry, and replication of ROD/B.
9151832	2	61	theme	ROD/B	486:490	arg1	fusion					452:457	efficient fusion	442:457	efficient fusion	442:457	We have stably expressed CXCR-4 on mink lung Mv-1-lu and feline kidney CCC cells (normally restrictive to HIV entry) and have shown efficient fusion, entry, and replication of ROD/B.
9151832	2	61	theme	ROD/B	486:490	arg1	entry					460:464	entry	460:464	entry	460:464	We have stably expressed CXCR-4 on mink lung Mv-1-lu and feline kidney CCC cells (normally restrictive to HIV entry) and have shown efficient fusion, entry, and replication of ROD/B.
9151832	6	62	theme	significant	1268:1278	arg1	role					1280:1283	a significant role	1266:1283	a significant role	1266:1283	Deletion of the C-terminal (intracellular) domain of CXCR-4 did not significantly affect entry by ROD/B, indicating that intracellular signalling through this domain does not play a significant role in entry by HIV-2.
9151832	3	63	from	Mutation	493:500	arg1	CXCR-4					545:550	CXCR-4	545:550	CXCR-4 (N11-->I, and N176-->Q)	545:574	Mutation of the two N-linked glycosylation sites on CXCR-4 (N11-->I, and N176-->Q) or pretreatment of CCC or Mv-1-lu cells expressing wild-type CXCR-4 with the glycosylation inhibitor tunicamycin increased fusion and entry by ROD/B.
9151832	3	63	from	Mutation	493:500	arg1	pretreatment					579:590	pretreatment	579:590	pretreatment of CCC or Mv-1-lu cells expressing wild-type CXCR-4 with the glycosylation inhibitor tunicamycin	579:687	Mutation of the two N-linked glycosylation sites on CXCR-4 (N11-->I, and N176-->Q) or pretreatment of CCC or Mv-1-lu cells expressing wild-type CXCR-4 with the glycosylation inhibitor tunicamycin increased fusion and entry by ROD/B.
9151832	1	64	theme	strain	192:197	arg1	ROD/B					199:203	The human immunodeficiency virus type 2 (HIV-2) strain ROD/B	144:203	The human immunodeficiency virus type 2 (HIV-2) strain ROD/B	144:203	The human immunodeficiency virus type 2 (HIV-2) strain ROD/B can efficiently use the 7tm chemokine receptor CXCR-4 as a primary receptor to enter CD4-negative cells.
9151832	4	65	theme	fusion	881:886	arg1	inhibition					857:866	complete inhibition	848:866	complete inhibition of cell-cell fusion by both ROD/B and another HIV-2 strain, CBL23	848:932	Deletion of portions of the N terminus of CXCR-4 resulted in a 3- to 10-fold decrease in cell-free infection by ROD/B and complete inhibition of cell-cell fusion by both ROD/B and another HIV-2 strain, CBL23.
9151832	4	65	theme	fusion	881:886	arg1	ROD/B					838:842	ROD/B	838:842	ROD/B	838:842	Deletion of portions of the N terminus of CXCR-4 resulted in a 3- to 10-fold decrease in cell-free infection by ROD/B and complete inhibition of cell-cell fusion by both ROD/B and another HIV-2 strain, CBL23.
9151832	0	66	from	role	83:86	arg1	entry					137:141	entry	137:141	entry	137:141	CD4-independent infection by human immunodeficiency virus type 2 strain ROD/B: the role of the N-terminal domain of CXCR-4 in fusion and entry.
9151832	0	66	from	role	83:86	arg1	fusion					126:131	fusion	126:131	fusion	126:131	CD4-independent infection by human immunodeficiency virus type 2 strain ROD/B: the role of the N-terminal domain of CXCR-4 in fusion and entry.
9151832	0	67	dep	infection	16:24	arg1	role					83:86	the role	79:86	CD4-independent infection by human immunodeficiency virus type 2 strain ROD/B: the role of the N-terminal domain of CXCR-4 in fusion and entry.	0:142	CD4-independent infection by human immunodeficiency virus type 2 strain ROD/B: the role of the N-terminal domain of CXCR-4 in fusion and entry.
9151832	2	68	theme	kidney	374:379	arg1	cells					385:389	mink lung Mv-1-lu and feline kidney CCC cells	345:389	cells	385:389	We have stably expressed CXCR-4 on mink lung Mv-1-lu and feline kidney CCC cells (normally restrictive to HIV entry) and have shown efficient fusion, entry, and replication of ROD/B.
9151832	2	69	theme	expressed	325:333	arg1	CXCR-4					335:340	stably expressed CXCR-4	318:340	stably expressed CXCR-4 on mink lung Mv-1-lu and feline kidney CCC cells	318:389	We have stably expressed CXCR-4 on mink lung Mv-1-lu and feline kidney CCC cells (normally restrictive to HIV entry) and have shown efficient fusion, entry, and replication of ROD/B.
9151832	2	70	theme	mink	345:348	arg1	Mv-1-lu					355:361	mink lung Mv-1-lu and feline kidney CCC cells	345:389	Mv-1-lu	355:361	We have stably expressed CXCR-4 on mink lung Mv-1-lu and feline kidney CCC cells (normally restrictive to HIV entry) and have shown efficient fusion, entry, and replication of ROD/B.
9151832	0	71	theme	strain	65:70	arg1	ROD/B					72:76	human immunodeficiency virus type 2 strain ROD/B	29:76	human immunodeficiency virus type 2 strain ROD/B	29:76	CD4-independent infection by human immunodeficiency virus type 2 strain ROD/B: the role of the N-terminal domain of CXCR-4 in fusion and entry.
9151832	3	72	theme	Mv-1-lu	602:608	arg1	cells					610:614	CCC or Mv-1-lu cells	595:614	CCC or Mv-1-lu cells expressing wild-type CXCR-4 with the glycosylation inhibitor tunicamycin	595:687	Mutation of the two N-linked glycosylation sites on CXCR-4 (N11-->I, and N176-->Q) or pretreatment of CCC or Mv-1-lu cells expressing wild-type CXCR-4 with the glycosylation inhibitor tunicamycin increased fusion and entry by ROD/B.
1421756	0	0	theme	transferrin	73:83	arg1	receptor					85:92	the human transferrin receptor	63:92	the human transferrin receptor	63:92	Presence of O-linked oligosaccharide on a threonine residue in the human transferrin receptor.
1421756	5	1	theme	remaining	710:718	arg1	fragment					727:734	the remaining 20 kDa fragment	706:734	the remaining 20 kDa fragment	706:734	In the remaining 20 kDa fragment there are three potential sites (Thr96, Thr104 and Ser106) for O-glycosylation in the extracellular domain.
1421756	5	2	dep	sites	762:766	arg1	Thr104					776:781	Thr104	776:781	Thr104	776:781	In the remaining 20 kDa fragment there are three potential sites (Thr96, Thr104 and Ser106) for O-glycosylation in the extracellular domain.
1421756	5	2	dep	sites	762:766	arg1	sites					762:766	three potential sites	746:766	three potential sites (Thr96, Thr104 and Ser106) for O-glycosylation in the extracellular domain	746:841	In the remaining 20 kDa fragment there are three potential sites (Thr96, Thr104 and Ser106) for O-glycosylation in the extracellular domain.
1421756	5	2	dep	sites	762:766	arg1	Ser106					787:792	Ser106	787:792	Ser106	787:792	In the remaining 20 kDa fragment there are three potential sites (Thr96, Thr104 and Ser106) for O-glycosylation in the extracellular domain.
1421756	10	3	contain	contains	1577:1584	arg1	s-TfR					1571:1575	the s-TfR	1567:1575	the s-TfR	1567:1575	The s-TfR was sensitive to O-glycanase and bound to Jacalin lectin, indicating that the s-TfR contains an O-linked oligosaccharide.
1421756	10	3	contain	contains	1577:1584	arg2	oligosaccharide					1598:1612	an O-linked oligosaccharide	1586:1612	an O-linked oligosaccharide	1586:1612	The s-TfR was sensitive to O-glycanase and bound to Jacalin lectin, indicating that the s-TfR contains an O-linked oligosaccharide.
1421756	2	4	theme	O-linked	330:337	arg1	oligosaccharides					339:354	the O-linked oligosaccharides	326:354	the O-linked oligosaccharides in the receptor	326:370	In the present study, we report our identification of the site of attachment of the O-linked oligosaccharides in the receptor.
1421756	0	5	from	residue	52:58	arg1	receptor					85:92	the human transferrin receptor	63:92	the human transferrin receptor	63:92	Presence of O-linked oligosaccharide on a threonine residue in the human transferrin receptor.
1421756	0	6	theme	human	67:71	arg1	receptor					85:92	the human transferrin receptor	63:92	the human transferrin receptor	63:92	Presence of O-linked oligosaccharide on a threonine residue in the human transferrin receptor.
1421756	1	7	link	Ser/Thr-linked	202:215	arg1	oligosaccharides					228:243	Ser/Thr-linked (O-linked) oligosaccharides	202:243	Ser/Thr-linked (O-linked) oligosaccharides	202:243	We have previously demonstrated that the human transferrin receptor (TfR) of approximately 90 kDa contains Ser/Thr-linked (O-linked) oligosaccharides.
1421756	5	8	theme	extracellular	822:834	arg1	domain					836:841	the extracellular domain	818:841	the extracellular domain	818:841	In the remaining 20 kDa fragment there are three potential sites (Thr96, Thr104 and Ser106) for O-glycosylation in the extracellular domain.
1421756	7	9	theme	Ser	1149:1151	arg1	Ser					1149:1151	radiolabelled Ser	1135:1151	radiolabelled Ser	1135:1151	Approximately 2% of the total radiolabelled Thr, but no radiolabelled Ser, was converted to expected beta-elimination products by this treatment.
1421756	7	9	theme	Ser	1149:1151	arg1	Thr					1123:1125	the total radiolabelled Thr	1099:1125	the total radiolabelled Thr	1099:1125	Approximately 2% of the total radiolabelled Thr, but no radiolabelled Ser, was converted to expected beta-elimination products by this treatment.
1421756	7	9	theme	Ser	1149:1151	arg1	%					1094:1094	Approximately 2%	1079:1094	Approximately 2% of the total radiolabelled Thr, but no radiolabelled Ser,	1079:1152	Approximately 2% of the total radiolabelled Thr, but no radiolabelled Ser, was converted to expected beta-elimination products by this treatment.
1421756	6	10	theme	Thr-	913:916	arg1	TfR					939:941	both the [3H]Thr- and [3H]Ser-labelled TfR	900:941	TfR	939:941	To identify which of these residues are O-glycosylated, both the [3H]Thr- and [3H]Ser-labelled TfR were directly treated with mild base to effect beta-elimination, and the radiolabelled amino acids and their derivatives were analysed.
1421756	7	11	theme	total	1103:1107	arg1	Thr					1123:1125	the total radiolabelled Thr	1099:1125	the total radiolabelled Thr	1099:1125	Approximately 2% of the total radiolabelled Thr, but no radiolabelled Ser, was converted to expected beta-elimination products by this treatment.
1421756	0	12	from	Presence	0:7	arg1	residue					52:58	a threonine residue	40:58	a threonine residue in the human transferrin receptor	40:92	Presence of O-linked oligosaccharide on a threonine residue in the human transferrin receptor.
1421756	0	13	link	O-linked	12:19	arg1	oligosaccharide					21:35	O-linked oligosaccharide	12:35	O-linked oligosaccharide	12:35	Presence of O-linked oligosaccharide on a threonine residue in the human transferrin receptor.
1421756	7	14	theme	Thr	1123:1125	arg1	Ser					1149:1151	radiolabelled Ser	1135:1151	radiolabelled Ser	1135:1151	Approximately 2% of the total radiolabelled Thr, but no radiolabelled Ser, was converted to expected beta-elimination products by this treatment.
1421756	7	14	theme	Thr	1123:1125	arg1	Thr					1123:1125	the total radiolabelled Thr	1099:1125	the total radiolabelled Thr	1099:1125	Approximately 2% of the total radiolabelled Thr, but no radiolabelled Ser, was converted to expected beta-elimination products by this treatment.
1421756	7	14	theme	Thr	1123:1125	arg1	%					1094:1094	Approximately 2%	1079:1094	Approximately 2% of the total radiolabelled Thr, but no radiolabelled Ser,	1079:1152	Approximately 2% of the total radiolabelled Thr, but no radiolabelled Ser, was converted to expected beta-elimination products by this treatment.
1421756	5	15	from	sites	762:766	arg1	domain					836:841	the extracellular domain	818:841	the extracellular domain	818:841	In the remaining 20 kDa fragment there are three potential sites (Thr96, Thr104 and Ser106) for O-glycosylation in the extracellular domain.
1421756	4	16	theme	intact	563:568	arg1	TfR					570:572	the intact TfR	559:572	the intact TfR	559:572	The beta-elimination of the intact TfR, but not the 70 kDa fragment, released Gal-[3H]Gal-NAcitol, indicating that the 70 kDa fragment lacks O-linked oligosaccharides.
1421756	4	17	theme	O-linked	676:683	arg1	oligosaccharides					685:700	O-linked oligosaccharides	676:700	O-linked oligosaccharides	676:700	The beta-elimination of the intact TfR, but not the 70 kDa fragment, released Gal-[3H]Gal-NAcitol, indicating that the 70 kDa fragment lacks O-linked oligosaccharides.
1421756	2	18	link	O-linked	330:337	arg1	oligosaccharides					339:354	the O-linked oligosaccharides	326:354	the O-linked oligosaccharides in the receptor	326:370	In the present study, we report our identification of the site of attachment of the O-linked oligosaccharides in the receptor.
1421756	3	19	theme	human	517:521	arg1	cells					528:532	human K562 cells	517:532	human K562 cells	517:532	A 70 kDa fragment from the external domain of the TfR was generated by trypsin treatment of the [3H]glucosamine-labelled receptor purified from human K562 cells.
1421756	8	20	from	TfR	1318:1320	arg1	present					1303:1309	present	1303:1309	present	1303:1309	These and other results demonstrate that only one O-linked oligosaccharide is present in the TfR and that it occurs on either Thr96 or Thr104.
1421756	3	21	theme	trypsin	444:450	arg1	treatment					452:460	trypsin treatment	444:460	trypsin treatment of the [3H]glucosamine-labelled receptor purified from human K562 cells	444:532	A 70 kDa fragment from the external domain of the TfR was generated by trypsin treatment of the [3H]glucosamine-labelled receptor purified from human K562 cells.
1421756	10	22	theme	O-linked	1589:1596	arg1	oligosaccharide					1598:1612	an O-linked oligosaccharide	1586:1612	an O-linked oligosaccharide	1586:1612	The s-TfR was sensitive to O-glycanase and bound to Jacalin lectin, indicating that the s-TfR contains an O-linked oligosaccharide.
1421756	9	23	dep	cleaved	1401:1407	arg1	soluble					1410:1416	soluble	1410:1416	soluble	1410:1416	From human serum we purified the cleaved, soluble form of the TfR (s-TfR), which contains Thr104, but lacks Thr96.
1421756	2	24	from	attachment	312:321	arg1	receptor					363:370	the receptor	359:370	the receptor	359:370	In the present study, we report our identification of the site of attachment of the O-linked oligosaccharides in the receptor.
1421756	3	25	theme	receptor	494:501	arg1	treatment					452:460	trypsin treatment	444:460	trypsin treatment of the [3H]glucosamine-labelled receptor purified from human K562 cells	444:532	A 70 kDa fragment from the external domain of the TfR was generated by trypsin treatment of the [3H]glucosamine-labelled receptor purified from human K562 cells.
1421756	6	26	theme	effect	983:988	arg1	beta-elimination					990:1005	mild base to effect beta-elimination	970:1005	mild base to effect beta-elimination	970:1005	To identify which of these residues are O-glycosylated, both the [3H]Thr- and [3H]Ser-labelled TfR were directly treated with mild base to effect beta-elimination, and the radiolabelled amino acids and their derivatives were analysed.
1421756	3	27	theme	kDa	378:380	arg1	fragment					382:389	A 70 kDa fragment	373:389	A 70 kDa fragment from the external domain of the TfR	373:425	A 70 kDa fragment from the external domain of the TfR was generated by trypsin treatment of the [3H]glucosamine-labelled receptor purified from human K562 cells.
1421756	6	28	dep	TfR	939:941	arg1	both					900:903	both	900:903	both	900:903	To identify which of these residues are O-glycosylated, both the [3H]Thr- and [3H]Ser-labelled TfR were directly treated with mild base to effect beta-elimination, and the radiolabelled amino acids and their derivatives were analysed.
1421756	4	29	theme	TfR	570:572	arg1	beta-elimination					539:554	The beta-elimination	535:554	The beta-elimination of the intact TfR	535:572	The beta-elimination of the intact TfR, but not the 70 kDa fragment, released Gal-[3H]Gal-NAcitol, indicating that the 70 kDa fragment lacks O-linked oligosaccharides.
1421756	8	30	attach	present	1303:1309	arg2	oligosaccharide					1284:1298	only one O-linked oligosaccharide	1266:1298	only one O-linked oligosaccharide	1266:1298	These and other results demonstrate that only one O-linked oligosaccharide is present in the TfR and that it occurs on either Thr96 or Thr104.
1421756	8	30	attach	present	1303:1309	arg1	TfR					1318:1320	the TfR	1314:1320	the TfR	1314:1320	These and other results demonstrate that only one O-linked oligosaccharide is present in the TfR and that it occurs on either Thr96 or Thr104.
1421756	3	31	theme	glucosamine-labelled	473:492	arg1	receptor					494:501	the [3H]glucosamine-labelled receptor	465:501	the [3H]glucosamine-labelled receptor purified from human K562 cells	465:532	A 70 kDa fragment from the external domain of the TfR was generated by trypsin treatment of the [3H]glucosamine-labelled receptor purified from human K562 cells.
1421756	4	32	link	O-linked	676:683	arg1	oligosaccharides					685:700	O-linked oligosaccharides	676:700	O-linked oligosaccharides	676:700	The beta-elimination of the intact TfR, but not the 70 kDa fragment, released Gal-[3H]Gal-NAcitol, indicating that the 70 kDa fragment lacks O-linked oligosaccharides.
1421756	8	33	from	present	1303:1309	arg1	TfR					1318:1320	the TfR	1314:1320	the TfR	1314:1320	These and other results demonstrate that only one O-linked oligosaccharide is present in the TfR and that it occurs on either Thr96 or Thr104.
1421756	6	34	theme	base	975:978	arg1	beta-elimination					990:1005	mild base to effect beta-elimination	970:1005	mild base to effect beta-elimination	970:1005	To identify which of these residues are O-glycosylated, both the [3H]Thr- and [3H]Ser-labelled TfR were directly treated with mild base to effect beta-elimination, and the radiolabelled amino acids and their derivatives were analysed.
1421756	5	35	theme	potential	752:760	arg1	Thr104					776:781	Thr104	776:781	Thr104	776:781	In the remaining 20 kDa fragment there are three potential sites (Thr96, Thr104 and Ser106) for O-glycosylation in the extracellular domain.
1421756	5	35	theme	potential	752:760	arg1	sites					762:766	three potential sites	746:766	three potential sites (Thr96, Thr104 and Ser106) for O-glycosylation in the extracellular domain	746:841	In the remaining 20 kDa fragment there are three potential sites (Thr96, Thr104 and Ser106) for O-glycosylation in the extracellular domain.
1421756	5	35	theme	potential	752:760	arg1	Ser106					787:792	Ser106	787:792	Ser106	787:792	In the remaining 20 kDa fragment there are three potential sites (Thr96, Thr104 and Ser106) for O-glycosylation in the extracellular domain.
1421756	10	36	link	O-linked	1589:1596	arg1	oligosaccharide					1598:1612	an O-linked oligosaccharide	1586:1612	an O-linked oligosaccharide	1586:1612	The s-TfR was sensitive to O-glycanase and bound to Jacalin lectin, indicating that the s-TfR contains an O-linked oligosaccharide.
1421756	4	37	theme	kDa	657:659	arg1	fragment					661:668	the 70 kDa fragment	650:668	the 70 kDa fragment	650:668	The beta-elimination of the intact TfR, but not the 70 kDa fragment, released Gal-[3H]Gal-NAcitol, indicating that the 70 kDa fragment lacks O-linked oligosaccharides.
1421756	6	38	gly	O-glycosylated	884:897	arg1	which					856:860	which	856:860	which	856:860	To identify which of these residues are O-glycosylated, both the [3H]Thr- and [3H]Ser-labelled TfR were directly treated with mild base to effect beta-elimination, and the radiolabelled amino acids and their derivatives were analysed.
1421756	3	39	theme	external	400:407	arg1	domain					409:414	the external domain	396:414	the external domain of the TfR	396:425	A 70 kDa fragment from the external domain of the TfR was generated by trypsin treatment of the [3H]glucosamine-labelled receptor purified from human K562 cells.
1421756	3	39	theme	external	400:407	arg1	TfR					423:425	the TfR	419:425	the TfR	419:425	A 70 kDa fragment from the external domain of the TfR was generated by trypsin treatment of the [3H]glucosamine-labelled receptor purified from human K562 cells.
1421756	0	40	theme	oligosaccharide	21:35	arg1	Presence					0:7	Presence	0:7	Presence of O-linked oligosaccharide on a threonine residue in the human transferrin receptor	0:92	Presence of O-linked oligosaccharide on a threonine residue in the human transferrin receptor.
1421756	1	41	link	O-linked	218:225	arg1	oligosaccharides					228:243	Ser/Thr-linked (O-linked) oligosaccharides	202:243	Ser/Thr-linked (O-linked) oligosaccharides	202:243	We have previously demonstrated that the human transferrin receptor (TfR) of approximately 90 kDa contains Ser/Thr-linked (O-linked) oligosaccharides.
1421756	3	42	theme	K562	523:526	arg1	cells					528:532	human K562 cells	517:532	human K562 cells	517:532	A 70 kDa fragment from the external domain of the TfR was generated by trypsin treatment of the [3H]glucosamine-labelled receptor purified from human K562 cells.
1421756	4	43	theme	70	587:588	arg1	kDa					590:592	kDa	590:592	kDa	590:592	The beta-elimination of the intact TfR, but not the 70 kDa fragment, released Gal-[3H]Gal-NAcitol, indicating that the 70 kDa fragment lacks O-linked oligosaccharides.
1421756	0	44	theme	O-linked	12:19	arg1	oligosaccharide					21:35	O-linked oligosaccharide	12:35	O-linked oligosaccharide	12:35	Presence of O-linked oligosaccharide on a threonine residue in the human transferrin receptor.
1421756	9	45	theme	TfR	1430:1432	arg1	form					1418:1421	the cleaved, soluble form	1397:1421	the cleaved, soluble form of the TfR (s-TfR), which contains Thr104, but lacks Thr96	1397:1480	From human serum we purified the cleaved, soluble form of the TfR (s-TfR), which contains Thr104, but lacks Thr96.
1421756	8	46	located	present	1303:1309	arg2	oligosaccharide					1284:1298	only one O-linked oligosaccharide	1266:1298	only one O-linked oligosaccharide	1266:1298	These and other results demonstrate that only one O-linked oligosaccharide is present in the TfR and that it occurs on either Thr96 or Thr104.
1421756	8	46	located	present	1303:1309	arg1	TfR					1318:1320	the TfR	1314:1320	the TfR	1314:1320	These and other results demonstrate that only one O-linked oligosaccharide is present in the TfR and that it occurs on either Thr96 or Thr104.
1421756	1	47	theme	kDa	189:191	arg1	TfR					164:166	TfR	164:166	TfR	164:166	We have previously demonstrated that the human transferrin receptor (TfR) of approximately 90 kDa contains Ser/Thr-linked (O-linked) oligosaccharides.
1421756	1	47	theme	kDa	189:191	arg1	receptor					154:161	the human transferrin receptor	132:161	the human transferrin receptor (TfR) of approximately 90 kDa	132:191	We have previously demonstrated that the human transferrin receptor (TfR) of approximately 90 kDa contains Ser/Thr-linked (O-linked) oligosaccharides.
1421756	5	48	theme	kDa	723:725	arg1	fragment					727:734	the remaining 20 kDa fragment	706:734	the remaining 20 kDa fragment	706:734	In the remaining 20 kDa fragment there are three potential sites (Thr96, Thr104 and Ser106) for O-glycosylation in the extracellular domain.
1421756	7	49	theme	beta-elimination	1180:1195	arg1	products					1197:1204	expected beta-elimination products	1171:1204	expected beta-elimination products	1171:1204	Approximately 2% of the total radiolabelled Thr, but no radiolabelled Ser, was converted to expected beta-elimination products by this treatment.
1421756	4	50	theme	kDa	590:592	arg1	fragment					594:601	the 70 kDa fragment	583:601	the 70 kDa fragment	583:601	The beta-elimination of the intact TfR, but not the 70 kDa fragment, released Gal-[3H]Gal-NAcitol, indicating that the 70 kDa fragment lacks O-linked oligosaccharides.
1421756	6	51	theme	mild	970:973	arg1	beta-elimination					990:1005	mild base to effect beta-elimination	970:1005	mild base to effect beta-elimination	970:1005	To identify which of these residues are O-glycosylated, both the [3H]Thr- and [3H]Ser-labelled TfR were directly treated with mild base to effect beta-elimination, and the radiolabelled amino acids and their derivatives were analysed.
1421756	6	52	dep	beta-elimination	990:1005	arg1	to					980:981	to	980:981	to	980:981	To identify which of these residues are O-glycosylated, both the [3H]Thr- and [3H]Ser-labelled TfR were directly treated with mild base to effect beta-elimination, and the radiolabelled amino acids and their derivatives were analysed.
1421756	2	53	from	receptor	363:370	arg1	attachment					312:321	attachment	312:321	attachment of the O-linked oligosaccharides in the receptor	312:370	In the present study, we report our identification of the site of attachment of the O-linked oligosaccharides in the receptor.
1421756	1	54	theme	Ser/Thr-linked	202:215	arg1	oligosaccharides					228:243	Ser/Thr-linked (O-linked) oligosaccharides	202:243	Ser/Thr-linked (O-linked) oligosaccharides	202:243	We have previously demonstrated that the human transferrin receptor (TfR) of approximately 90 kDa contains Ser/Thr-linked (O-linked) oligosaccharides.
1421756	3	55	theme	70	375:376	arg1	kDa					378:380	kDa	378:380	kDa	378:380	A 70 kDa fragment from the external domain of the TfR was generated by trypsin treatment of the [3H]glucosamine-labelled receptor purified from human K562 cells.
1421756	8	56	theme	O-linked	1275:1282	arg1	oligosaccharide					1284:1298	only one O-linked oligosaccharide	1266:1298	only one O-linked oligosaccharide	1266:1298	These and other results demonstrate that only one O-linked oligosaccharide is present in the TfR and that it occurs on either Thr96 or Thr104.
1421756	7	57	theme	expected	1171:1178	arg1	products					1197:1204	expected beta-elimination products	1171:1204	expected beta-elimination products	1171:1204	Approximately 2% of the total radiolabelled Thr, but no radiolabelled Ser, was converted to expected beta-elimination products by this treatment.
1421756	0	58	theme	threonine	42:50	arg1	residue					52:58	a threonine residue	40:58	a threonine residue in the human transferrin receptor	40:92	Presence of O-linked oligosaccharide on a threonine residue in the human transferrin receptor.
1421756	8	59	link	O-linked	1275:1282	arg1	oligosaccharide					1284:1298	only one O-linked oligosaccharide	1266:1298	only one O-linked oligosaccharide	1266:1298	These and other results demonstrate that only one O-linked oligosaccharide is present in the TfR and that it occurs on either Thr96 or Thr104.
1421756	10	60	theme	Jacalin	1535:1541	arg1	lectin					1543:1548	Jacalin lectin	1535:1548	Jacalin lectin	1535:1548	The s-TfR was sensitive to O-glycanase and bound to Jacalin lectin, indicating that the s-TfR contains an O-linked oligosaccharide.
1421756	1	61	theme	transferrin	142:152	arg1	TfR					164:166	TfR	164:166	TfR	164:166	We have previously demonstrated that the human transferrin receptor (TfR) of approximately 90 kDa contains Ser/Thr-linked (O-linked) oligosaccharides.
1421756	1	61	theme	transferrin	142:152	arg1	receptor					154:161	the human transferrin receptor	132:161	the human transferrin receptor (TfR) of approximately 90 kDa	132:191	We have previously demonstrated that the human transferrin receptor (TfR) of approximately 90 kDa contains Ser/Thr-linked (O-linked) oligosaccharides.
1421756	2	62	theme	attachment	312:321	arg1	attachment					312:321	attachment	312:321	attachment of the O-linked oligosaccharides in the receptor	312:370	In the present study, we report our identification of the site of attachment of the O-linked oligosaccharides in the receptor.
1421756	2	62	theme	attachment	312:321	arg1	site					304:307	the site	300:307	the site of attachment of the O-linked oligosaccharides in the receptor	300:370	In the present study, we report our identification of the site of attachment of the O-linked oligosaccharides in the receptor.
1421756	2	63	from	oligosaccharides	339:354	arg1	receptor					363:370	the receptor	359:370	the receptor	359:370	In the present study, we report our identification of the site of attachment of the O-linked oligosaccharides in the receptor.
1421756	1	64	contain	contains	193:200	arg2	oligosaccharides					228:243	Ser/Thr-linked (O-linked) oligosaccharides	202:243	Ser/Thr-linked (O-linked) oligosaccharides	202:243	We have previously demonstrated that the human transferrin receptor (TfR) of approximately 90 kDa contains Ser/Thr-linked (O-linked) oligosaccharides.
1421756	1	64	contain	contains	193:200	arg1	TfR					164:166	TfR	164:166	TfR	164:166	We have previously demonstrated that the human transferrin receptor (TfR) of approximately 90 kDa contains Ser/Thr-linked (O-linked) oligosaccharides.
1421756	1	64	contain	contains	193:200	arg1	receptor					154:161	the human transferrin receptor	132:161	the human transferrin receptor (TfR) of approximately 90 kDa	132:191	We have previously demonstrated that the human transferrin receptor (TfR) of approximately 90 kDa contains Ser/Thr-linked (O-linked) oligosaccharides.
1421756	2	65	theme	present	253:259	arg1	study					261:265	the present study	249:265	the present study	249:265	In the present study, we report our identification of the site of attachment of the O-linked oligosaccharides in the receptor.
1421756	6	66	theme	Ser-labelled	926:937	arg1	TfR					939:941	both the [3H]Thr- and [3H]Ser-labelled TfR	900:941	TfR	939:941	To identify which of these residues are O-glycosylated, both the [3H]Thr- and [3H]Ser-labelled TfR were directly treated with mild base to effect beta-elimination, and the radiolabelled amino acids and their derivatives were analysed.
1421756	6	67	theme	amino	1030:1034	arg1	acids					1036:1040	the radiolabelled amino acids	1012:1040	the radiolabelled amino acids	1012:1040	To identify which of these residues are O-glycosylated, both the [3H]Thr- and [3H]Ser-labelled TfR were directly treated with mild base to effect beta-elimination, and the radiolabelled amino acids and their derivatives were analysed.
1421756	6	68	theme	radiolabelled	1016:1028	arg1	acids					1036:1040	the radiolabelled amino acids	1012:1040	the radiolabelled amino acids	1012:1040	To identify which of these residues are O-glycosylated, both the [3H]Thr- and [3H]Ser-labelled TfR were directly treated with mild base to effect beta-elimination, and the radiolabelled amino acids and their derivatives were analysed.
1421756	4	69	dep	Gal-NAcitol	621:631	arg1	Gal-[3H					613:619	Gal-[3H	613:619	Gal-[3H	613:619	The beta-elimination of the intact TfR, but not the 70 kDa fragment, released Gal-[3H]Gal-NAcitol, indicating that the 70 kDa fragment lacks O-linked oligosaccharides.
1421756	8	70	theme	These	1225:1229	arg1	results					1241:1247	These and other results	1225:1247	results	1241:1247	These and other results demonstrate that only one O-linked oligosaccharide is present in the TfR and that it occurs on either Thr96 or Thr104.
1421756	2	71	theme	site	304:307	arg1	identification					282:295	our identification	278:295	our identification of the site of attachment of the O-linked oligosaccharides in the receptor	278:370	In the present study, we report our identification of the site of attachment of the O-linked oligosaccharides in the receptor.
1421756	8	72	theme	other	1235:1239	arg1	results					1241:1247	These and other results	1225:1247	results	1241:1247	These and other results demonstrate that only one O-linked oligosaccharide is present in the TfR and that it occurs on either Thr96 or Thr104.
1421756	1	73	theme	O-linked	218:225	arg1	oligosaccharides					228:243	Ser/Thr-linked (O-linked) oligosaccharides	202:243	Ser/Thr-linked (O-linked) oligosaccharides	202:243	We have previously demonstrated that the human transferrin receptor (TfR) of approximately 90 kDa contains Ser/Thr-linked (O-linked) oligosaccharides.
1421756	9	74	theme	human	1373:1377	arg1	serum					1379:1383	human serum	1373:1383	human serum	1373:1383	From human serum we purified the cleaved, soluble form of the TfR (s-TfR), which contains Thr104, but lacks Thr96.
1421756	3	75	theme	TfR	423:425	arg1	domain					409:414	the external domain	396:414	the external domain of the TfR	396:425	A 70 kDa fragment from the external domain of the TfR was generated by trypsin treatment of the [3H]glucosamine-labelled receptor purified from human K562 cells.
1421756	3	75	theme	TfR	423:425	arg1	TfR					423:425	the TfR	419:425	the TfR	419:425	A 70 kDa fragment from the external domain of the TfR was generated by trypsin treatment of the [3H]glucosamine-labelled receptor purified from human K562 cells.
1421756	9	76	theme	cleaved	1401:1407	arg1	form					1418:1421	the cleaved, soluble form	1397:1421	the cleaved, soluble form of the TfR (s-TfR), which contains Thr104, but lacks Thr96	1397:1480	From human serum we purified the cleaved, soluble form of the TfR (s-TfR), which contains Thr104, but lacks Thr96.
1421756	1	77	theme	human	136:140	arg1	TfR					164:166	TfR	164:166	TfR	164:166	We have previously demonstrated that the human transferrin receptor (TfR) of approximately 90 kDa contains Ser/Thr-linked (O-linked) oligosaccharides.
1421756	1	77	theme	human	136:140	arg1	receptor					154:161	the human transferrin receptor	132:161	the human transferrin receptor (TfR) of approximately 90 kDa	132:191	We have previously demonstrated that the human transferrin receptor (TfR) of approximately 90 kDa contains Ser/Thr-linked (O-linked) oligosaccharides.
1421756	9	78	contain	contains	1449:1456	arg1	TfR					1430:1432	the TfR	1426:1432	the TfR (s-TfR)	1426:1440	From human serum we purified the cleaved, soluble form of the TfR (s-TfR), which contains Thr104, but lacks Thr96.
1421756	9	78	contain	contains	1449:1456	arg1	s-TfR					1435:1439	s-TfR	1435:1439	s-TfR	1435:1439	From human serum we purified the cleaved, soluble form of the TfR (s-TfR), which contains Thr104, but lacks Thr96.
1421756	9	78	contain	contains	1449:1456	arg2	Thr104					1458:1463	Thr104	1458:1463	Thr104	1458:1463	From human serum we purified the cleaved, soluble form of the TfR (s-TfR), which contains Thr104, but lacks Thr96.
1421756	3	79	from	domain	409:414	arg1	fragment					382:389	A 70 kDa fragment	373:389	A 70 kDa fragment from the external domain of the TfR	373:425	A 70 kDa fragment from the external domain of the TfR was generated by trypsin treatment of the [3H]glucosamine-labelled receptor purified from human K562 cells.
1421756	2	80	theme	oligosaccharides	339:354	arg1	attachment					312:321	attachment	312:321	attachment of the O-linked oligosaccharides in the receptor	312:370	In the present study, we report our identification of the site of attachment of the O-linked oligosaccharides in the receptor.
1421756	7	81	theme	radiolabelled	1135:1147	arg1	Ser					1149:1151	radiolabelled Ser	1135:1151	radiolabelled Ser	1135:1151	Approximately 2% of the total radiolabelled Thr, but no radiolabelled Ser, was converted to expected beta-elimination products by this treatment.
1421756	7	82	theme	radiolabelled	1109:1121	arg1	Thr					1123:1125	the total radiolabelled Thr	1099:1125	the total radiolabelled Thr	1099:1125	Approximately 2% of the total radiolabelled Thr, but no radiolabelled Ser, was converted to expected beta-elimination products by this treatment.
23603833	8	0	theme	RPLGLL	1124:1129	arg1	motif					1131:1135	the RPLGLL motif	1120:1135	the RPLGLL motif	1120:1135	Within this region, the RPLGLL motif and the PDZ binding motifs (QERL/KESL) appear to be involved in initiating and completing the process of ligand internalization.
23603833	5	1	theme	type	784:787	arg1	LDLR-A					792:797	LDLR-A	792:797	LDLR-A	792:797	Deleting the cysteine-rich region (aa 95-141) that separates the two low-density lipoprotein receptor type A (LDLR-A) domains does not affect TC-Cbl binding (Ka = 19-24 nM(-1)).
23603833	5	1	theme	type	784:787	arg1	A					789:789	low-density lipoprotein receptor type A	751:789	the two low-density lipoprotein receptor type A (LDLR-A) domains	743:806	Deleting the cysteine-rich region (aa 95-141) that separates the two low-density lipoprotein receptor type A (LDLR-A) domains does not affect TC-Cbl binding (Ka = 19-24 nM(-1)).
23603833	3	2	from	mutations	473:481	arg1	TCblR					510:514	TCblR	510:514	TCblR	510:514	The high-affinity interaction of TCblR with TC-Cbl (Ka=10 nM(-1)) was investigated using deletions and mutations of amino acid sequences in TCblR.
23603833	1	3	theme	cellular	233:240	arg1	uptake					242:247	cellular uptake	233:247	cellular uptake of the vitamin	233:262	The membrane receptor TCblR/CD320 binds transcobalamin (TC) saturated with vitamin B12 [cobalamin (Cbl)] and mediates cellular uptake of the vitamin.
23603833	0	4	theme	cellular	64:71	arg1	uptake					73:78	cellular uptake	64:78	cellular uptake of transcobalamin-bound cobalamin	64:112	Mapping the functional domains of TCblR/CD320, the receptor for cellular uptake of transcobalamin-bound cobalamin.
23603833	8	5	theme	PDZ	1145:1147	arg1	QERL/KESL					1165:1173	QERL/KESL	1165:1173	QERL/KESL	1165:1173	Within this region, the RPLGLL motif and the PDZ binding motifs (QERL/KESL) appear to be involved in initiating and completing the process of ligand internalization.
23603833	8	5	theme	PDZ	1145:1147	arg1	motifs					1157:1162	the PDZ binding motifs	1141:1162	the PDZ binding motifs (QERL/KESL)	1141:1174	Within this region, the RPLGLL motif and the PDZ binding motifs (QERL/KESL) appear to be involved in initiating and completing the process of ligand internalization.
23603833	5	6	theme	A	789:789	arg1	domains					800:806	the two low-density lipoprotein receptor type A (LDLR-A) domains	743:806	the two low-density lipoprotein receptor type A (LDLR-A) domains	743:806	Deleting the cysteine-rich region (aa 95-141) that separates the two low-density lipoprotein receptor type A (LDLR-A) domains does not affect TC-Cbl binding (Ka = 19-24 nM(-1)).
23603833	0	7	theme	transcobalamin-bound	83:102	arg1	cobalamin					104:112	transcobalamin-bound cobalamin	83:112	transcobalamin-bound cobalamin	83:112	Mapping the functional domains of TCblR/CD320, the receptor for cellular uptake of transcobalamin-bound cobalamin.
23603833	3	8	from	sequences	497:505	arg1	TCblR					510:514	TCblR	510:514	TCblR	510:514	The high-affinity interaction of TCblR with TC-Cbl (Ka=10 nM(-1)) was investigated using deletions and mutations of amino acid sequences in TCblR.
23603833	6	9	theme	critical	981:988	arg1	domains					875:881	The two LDLR-A domains	860:881	The two LDLR-A domains (aa 54-89 and 132-167) with the negatively charged acidic residues involved in Ca(2+) binding	860:975	The two LDLR-A domains (aa 54-89 and 132-167) with the negatively charged acidic residues involved in Ca(2+) binding are critical determinants of ligand binding.
23603833	6	9	theme	critical	981:988	arg1	determinants					990:1001	critical determinants	981:1001	critical determinants of ligand binding	981:1019	The two LDLR-A domains (aa 54-89 and 132-167) with the negatively charged acidic residues involved in Ca(2+) binding are critical determinants of ligand binding.
23603833	5	10	theme	TC-Cbl	824:829	arg1	binding					831:837	TC-Cbl binding	824:837	TC-Cbl binding (Ka = 19-24 nM(-1))	824:857	Deleting the cysteine-rich region (aa 95-141) that separates the two low-density lipoprotein receptor type A (LDLR-A) domains does not affect TC-Cbl binding (Ka = 19-24 nM(-1)).
23603833	4	11	theme	extracellular	526:538	arg1	aa					548:549	aa 32-229	548:556	aa 32-229	548:556	Only the extracellular region (aa 32-229) is needed for TC-Cbl binding, but the N-glycosylation sites (N126, N195, and N213) are of no importance for this function.
23603833	4	11	theme	extracellular	526:538	arg1	region					540:545	Only the extracellular region	517:545	Only the extracellular region (aa 32-229)	517:557	Only the extracellular region (aa 32-229) is needed for TC-Cbl binding, but the N-glycosylation sites (N126, N195, and N213) are of no importance for this function.
23603833	4	12	dep	sites	613:617	arg1	sites					613:617	the N-glycosylation sites	593:617	the N-glycosylation sites (N126, N195, and N213)	593:640	Only the extracellular region (aa 32-229) is needed for TC-Cbl binding, but the N-glycosylation sites (N126, N195, and N213) are of no importance for this function.
23603833	4	12	dep	sites	613:617	arg1	N195					626:629	N195	626:629	N195	626:629	Only the extracellular region (aa 32-229) is needed for TC-Cbl binding, but the N-glycosylation sites (N126, N195, and N213) are of no importance for this function.
23603833	4	12	dep	sites	613:617	arg1	N213					636:639	N213	636:639	N213	636:639	Only the extracellular region (aa 32-229) is needed for TC-Cbl binding, but the N-glycosylation sites (N126, N195, and N213) are of no importance for this function.
23603833	4	12	dep	sites	613:617	arg1	N126					620:623	N126	620:623	N126	620:623	Only the extracellular region (aa 32-229) is needed for TC-Cbl binding, but the N-glycosylation sites (N126, N195, and N213) are of no importance for this function.
23603833	3	13	theme	amino	486:490	arg1	sequences					497:505	amino acid sequences	486:505	amino acid sequences in TCblR	486:514	The high-affinity interaction of TCblR with TC-Cbl (Ka=10 nM(-1)) was investigated using deletions and mutations of amino acid sequences in TCblR.
23603833	9	14	theme	regions	1299:1305	arg1	deletions					1280:1288	deletions	1280:1288	deletions	1280:1288	Mutations and deletions of these regions involved in binding and internalization of TC-Cbl are likely to produce the biochemical and clinical phenotype of Cbl deficiency.
23603833	9	14	theme	regions	1299:1305	arg1	Mutations					1266:1274	Mutations	1266:1274	Mutations	1266:1274	Mutations and deletions of these regions involved in binding and internalization of TC-Cbl are likely to produce the biochemical and clinical phenotype of Cbl deficiency.
23603833	3	15	from	deletions	459:467	arg1	TCblR					510:514	TCblR	510:514	TCblR	510:514	The high-affinity interaction of TCblR with TC-Cbl (Ka=10 nM(-1)) was investigated using deletions and mutations of amino acid sequences in TCblR.
23603833	8	16	theme	binding	1149:1155	arg1	QERL/KESL					1165:1173	QERL/KESL	1165:1173	QERL/KESL	1165:1173	Within this region, the RPLGLL motif and the PDZ binding motifs (QERL/KESL) appear to be involved in initiating and completing the process of ligand internalization.
23603833	8	16	theme	binding	1149:1155	arg1	motifs					1157:1162	the PDZ binding motifs	1141:1162	the PDZ binding motifs (QERL/KESL)	1141:1174	Within this region, the RPLGLL motif and the PDZ binding motifs (QERL/KESL) appear to be involved in initiating and completing the process of ligand internalization.
23603833	3	17	theme	TCblR	403:407	arg1	interaction					388:398	The high-affinity interaction	370:398	The high-affinity interaction of TCblR with TC-Cbl (Ka=10 nM(-1))	370:434	The high-affinity interaction of TCblR with TC-Cbl (Ka=10 nM(-1)) was investigated using deletions and mutations of amino acid sequences in TCblR.
23603833	0	18	theme	cobalamin	104:112	arg1	uptake					73:78	cellular uptake	64:78	cellular uptake of transcobalamin-bound cobalamin	64:112	Mapping the functional domains of TCblR/CD320, the receptor for cellular uptake of transcobalamin-bound cobalamin.
23603833	6	19	theme	acidic	934:939	arg1	residues					941:948	the negatively charged acidic residues	911:948	the negatively charged acidic residues involved in Ca(2+) binding	911:975	The two LDLR-A domains (aa 54-89 and 132-167) with the negatively charged acidic residues involved in Ca(2+) binding are critical determinants of ligand binding.
23603833	5	20	theme	=	843:843	arg1	Ka					840:841	Ka	840:841	Ka = 19-24 nM(-1)	840:856	Deleting the cysteine-rich region (aa 95-141) that separates the two low-density lipoprotein receptor type A (LDLR-A) domains does not affect TC-Cbl binding (Ka = 19-24 nM(-1)).
23603833	8	21	theme	internalization	1249:1263	arg1	process					1231:1237	the process	1227:1237	the process of ligand internalization	1227:1263	Within this region, the RPLGLL motif and the PDZ binding motifs (QERL/KESL) appear to be involved in initiating and completing the process of ligand internalization.
23603833	2	22	theme	Cbl	354:356	arg1	uptake					344:349	efficient uptake	334:349	efficient uptake of Cbl into cells	334:367	The specificity of TC for Cbl and of the receptor for TC-Cbl ensures efficient uptake of Cbl into cells.
23603833	4	23	theme	TC-Cbl	573:578	arg1	binding					580:586	TC-Cbl binding	573:586	TC-Cbl binding	573:586	Only the extracellular region (aa 32-229) is needed for TC-Cbl binding, but the N-glycosylation sites (N126, N195, and N213) are of no importance for this function.
23603833	5	24	theme	cysteine-rich	695:707	arg1	aa					717:718	aa 95-141	717:725	aa 95-141	717:725	Deleting the cysteine-rich region (aa 95-141) that separates the two low-density lipoprotein receptor type A (LDLR-A) domains does not affect TC-Cbl binding (Ka = 19-24 nM(-1)).
23603833	5	24	theme	cysteine-rich	695:707	arg1	region					709:714	the cysteine-rich region	691:714	the cysteine-rich region (aa 95-141) that separates the two low-density lipoprotein receptor type A (LDLR-A) domains	691:806	Deleting the cysteine-rich region (aa 95-141) that separates the two low-density lipoprotein receptor type A (LDLR-A) domains does not affect TC-Cbl binding (Ka = 19-24 nM(-1)).
23603833	1	25	theme	vitamin	256:262	arg1	uptake					242:247	cellular uptake	233:247	cellular uptake of the vitamin	233:262	The membrane receptor TCblR/CD320 binds transcobalamin (TC) saturated with vitamin B12 [cobalamin (Cbl)] and mediates cellular uptake of the vitamin.
23603833	9	26	theme	Cbl	1421:1423	arg1	deficiency					1425:1434	Cbl deficiency	1421:1434	Cbl deficiency	1421:1434	Mutations and deletions of these regions involved in binding and internalization of TC-Cbl are likely to produce the biochemical and clinical phenotype of Cbl deficiency.
23603833	1	27	theme	vitamin	190:196	arg1	[cobalamin					202:211	vitamin B12 [cobalamin	190:211	vitamin B12 [cobalamin (Cbl)]	190:218	The membrane receptor TCblR/CD320 binds transcobalamin (TC) saturated with vitamin B12 [cobalamin (Cbl)] and mediates cellular uptake of the vitamin.
23603833	1	27	theme	vitamin	190:196	arg1	Cbl					214:216	Cbl	214:216	Cbl	214:216	The membrane receptor TCblR/CD320 binds transcobalamin (TC) saturated with vitamin B12 [cobalamin (Cbl)] and mediates cellular uptake of the vitamin.
23603833	3	28	theme	acid	492:495	arg1	sequences					497:505	amino acid sequences	486:505	amino acid sequences in TCblR	486:514	The high-affinity interaction of TCblR with TC-Cbl (Ka=10 nM(-1)) was investigated using deletions and mutations of amino acid sequences in TCblR.
23603833	1	29	theme	B12	198:200	arg1	[cobalamin					202:211	vitamin B12 [cobalamin	190:211	vitamin B12 [cobalamin (Cbl)]	190:218	The membrane receptor TCblR/CD320 binds transcobalamin (TC) saturated with vitamin B12 [cobalamin (Cbl)] and mediates cellular uptake of the vitamin.
23603833	1	29	theme	B12	198:200	arg1	Cbl					214:216	Cbl	214:216	Cbl	214:216	The membrane receptor TCblR/CD320 binds transcobalamin (TC) saturated with vitamin B12 [cobalamin (Cbl)] and mediates cellular uptake of the vitamin.
23603833	0	30	theme	functional	12:21	arg1	TCblR/CD320					34:44	TCblR/CD320	34:44	TCblR/CD320	34:44	Mapping the functional domains of TCblR/CD320, the receptor for cellular uptake of transcobalamin-bound cobalamin.
23603833	0	30	theme	functional	12:21	arg1	domains					23:29	the functional domains	8:29	the functional domains of TCblR/CD320, the receptor for cellular uptake of transcobalamin-bound cobalamin	8:112	Mapping the functional domains of TCblR/CD320, the receptor for cellular uptake of transcobalamin-bound cobalamin.
23603833	9	31	theme	TC-Cbl	1350:1355	arg1	internalization					1331:1345	internalization	1331:1345	internalization	1331:1345	Mutations and deletions of these regions involved in binding and internalization of TC-Cbl are likely to produce the biochemical and clinical phenotype of Cbl deficiency.
23603833	9	31	theme	TC-Cbl	1350:1355	arg1	binding					1319:1325	binding	1319:1325	binding	1319:1325	Mutations and deletions of these regions involved in binding and internalization of TC-Cbl are likely to produce the biochemical and clinical phenotype of Cbl deficiency.
23603833	3	32	theme	sequences	497:505	arg1	mutations					473:481	mutations	473:481	mutations	473:481	The high-affinity interaction of TCblR with TC-Cbl (Ka=10 nM(-1)) was investigated using deletions and mutations of amino acid sequences in TCblR.
23603833	3	32	theme	sequences	497:505	arg1	deletions					459:467	deletions	459:467	deletions	459:467	The high-affinity interaction of TCblR with TC-Cbl (Ka=10 nM(-1)) was investigated using deletions and mutations of amino acid sequences in TCblR.
23603833	4	33	theme	N-glycosylation	597:611	arg1	sites					613:617	the N-glycosylation sites	593:617	the N-glycosylation sites (N126, N195, and N213)	593:640	Only the extracellular region (aa 32-229) is needed for TC-Cbl binding, but the N-glycosylation sites (N126, N195, and N213) are of no importance for this function.
23603833	4	33	theme	N-glycosylation	597:611	arg1	N195					626:629	N195	626:629	N195	626:629	Only the extracellular region (aa 32-229) is needed for TC-Cbl binding, but the N-glycosylation sites (N126, N195, and N213) are of no importance for this function.
23603833	4	33	theme	N-glycosylation	597:611	arg1	N213					636:639	N213	636:639	N213	636:639	Only the extracellular region (aa 32-229) is needed for TC-Cbl binding, but the N-glycosylation sites (N126, N195, and N213) are of no importance for this function.
23603833	4	33	theme	N-glycosylation	597:611	arg1	N126					620:623	N126	620:623	N126	620:623	Only the extracellular region (aa 32-229) is needed for TC-Cbl binding, but the N-glycosylation sites (N126, N195, and N213) are of no importance for this function.
23603833	0	34	theme	TCblR/CD320	34:44	arg1	TCblR/CD320					34:44	TCblR/CD320	34:44	TCblR/CD320	34:44	Mapping the functional domains of TCblR/CD320, the receptor for cellular uptake of transcobalamin-bound cobalamin.
23603833	0	34	theme	TCblR/CD320	34:44	arg1	domains					23:29	the functional domains	8:29	the functional domains of TCblR/CD320, the receptor for cellular uptake of transcobalamin-bound cobalamin	8:112	Mapping the functional domains of TCblR/CD320, the receptor for cellular uptake of transcobalamin-bound cobalamin.
23603833	5	35	dep	=	843:843	arg1	-1					854:855	-1	854:855	-1	854:855	Deleting the cysteine-rich region (aa 95-141) that separates the two low-density lipoprotein receptor type A (LDLR-A) domains does not affect TC-Cbl binding (Ka = 19-24 nM(-1)).
23603833	5	35	dep	=	843:843	arg1	nM					851:852	19-24 nM	845:852	19-24 nM(-1)	845:856	Deleting the cysteine-rich region (aa 95-141) that separates the two low-density lipoprotein receptor type A (LDLR-A) domains does not affect TC-Cbl binding (Ka = 19-24 nM(-1)).
23603833	9	36	theme	biochemical	1383:1393	arg1	phenotype					1408:1416	the biochemical and clinical phenotype	1379:1416	the biochemical and clinical phenotype of Cbl deficiency	1379:1434	Mutations and deletions of these regions involved in binding and internalization of TC-Cbl are likely to produce the biochemical and clinical phenotype of Cbl deficiency.
23603833	5	37	theme	low-density	751:761	arg1	LDLR-A					792:797	LDLR-A	792:797	LDLR-A	792:797	Deleting the cysteine-rich region (aa 95-141) that separates the two low-density lipoprotein receptor type A (LDLR-A) domains does not affect TC-Cbl binding (Ka = 19-24 nM(-1)).
23603833	5	37	theme	low-density	751:761	arg1	A					789:789	low-density lipoprotein receptor type A	751:789	the two low-density lipoprotein receptor type A (LDLR-A) domains	743:806	Deleting the cysteine-rich region (aa 95-141) that separates the two low-density lipoprotein receptor type A (LDLR-A) domains does not affect TC-Cbl binding (Ka = 19-24 nM(-1)).
23603833	6	38	theme	LDLR-A	868:873	arg1	domains					875:881	The two LDLR-A domains	860:881	The two LDLR-A domains (aa 54-89 and 132-167) with the negatively charged acidic residues involved in Ca(2+) binding	860:975	The two LDLR-A domains (aa 54-89 and 132-167) with the negatively charged acidic residues involved in Ca(2+) binding are critical determinants of ligand binding.
23603833	6	38	theme	LDLR-A	868:873	arg1	determinants					990:1001	critical determinants	981:1001	critical determinants of ligand binding	981:1019	The two LDLR-A domains (aa 54-89 and 132-167) with the negatively charged acidic residues involved in Ca(2+) binding are critical determinants of ligand binding.
23603833	6	38	theme	LDLR-A	868:873	arg1	aa					884:885	aa 54-89 and 132-167	884:903	aa	884:885	The two LDLR-A domains (aa 54-89 and 132-167) with the negatively charged acidic residues involved in Ca(2+) binding are critical determinants of ligand binding.
23603833	6	38	theme	LDLR-A	868:873	arg1	132-167					897:903	132-167	897:903	132-167	897:903	The two LDLR-A domains (aa 54-89 and 132-167) with the negatively charged acidic residues involved in Ca(2+) binding are critical determinants of ligand binding.
23603833	3	39	theme	high-affinity	374:386	arg1	interaction					388:398	The high-affinity interaction	370:398	The high-affinity interaction of TCblR with TC-Cbl (Ka=10 nM(-1))	370:434	The high-affinity interaction of TCblR with TC-Cbl (Ka=10 nM(-1)) was investigated using deletions and mutations of amino acid sequences in TCblR.
23603833	8	40	theme	ligand	1242:1247	arg1	internalization					1249:1263	ligand internalization	1242:1263	ligand internalization	1242:1263	Within this region, the RPLGLL motif and the PDZ binding motifs (QERL/KESL) appear to be involved in initiating and completing the process of ligand internalization.
23603833	5	41	theme	lipoprotein	763:773	arg1	LDLR-A					792:797	LDLR-A	792:797	LDLR-A	792:797	Deleting the cysteine-rich region (aa 95-141) that separates the two low-density lipoprotein receptor type A (LDLR-A) domains does not affect TC-Cbl binding (Ka = 19-24 nM(-1)).
23603833	5	41	theme	lipoprotein	763:773	arg1	A					789:789	low-density lipoprotein receptor type A	751:789	the two low-density lipoprotein receptor type A (LDLR-A) domains	743:806	Deleting the cysteine-rich region (aa 95-141) that separates the two low-density lipoprotein receptor type A (LDLR-A) domains does not affect TC-Cbl binding (Ka = 19-24 nM(-1)).
23603833	3	42	with	interaction	388:398	arg1	TC-Cbl					414:419	TC-Cbl	414:419	TC-Cbl (Ka=10 nM(-1))	414:434	The high-affinity interaction of TCblR with TC-Cbl (Ka=10 nM(-1)) was investigated using deletions and mutations of amino acid sequences in TCblR.
23603833	9	43	theme	clinical	1399:1406	arg1	phenotype					1408:1416	the biochemical and clinical phenotype	1379:1416	the biochemical and clinical phenotype of Cbl deficiency	1379:1434	Mutations and deletions of these regions involved in binding and internalization of TC-Cbl are likely to produce the biochemical and clinical phenotype of Cbl deficiency.
23603833	2	44	theme	receptor	306:313	arg1	specificity					269:279	The specificity	265:279	The specificity of TC for Cbl and of the receptor for TC-Cbl	265:324	The specificity of TC for Cbl and of the receptor for TC-Cbl ensures efficient uptake of Cbl into cells.
23603833	4	45	gly	N-glycosylation	597:611	arg2	N195					626:629	N195	626:629	N195	626:629	Only the extracellular region (aa 32-229) is needed for TC-Cbl binding, but the N-glycosylation sites (N126, N195, and N213) are of no importance for this function.
23603833	4	45	gly	N-glycosylation	597:611	arg2	N126					620:623	N126	620:623	N126	620:623	Only the extracellular region (aa 32-229) is needed for TC-Cbl binding, but the N-glycosylation sites (N126, N195, and N213) are of no importance for this function.
23603833	4	45	gly	N-glycosylation	597:611	arg2	N213					636:639	N213	636:639	N213	636:639	Only the extracellular region (aa 32-229) is needed for TC-Cbl binding, but the N-glycosylation sites (N126, N195, and N213) are of no importance for this function.
23603833	4	45	gly	N-glycosylation	597:611	arg2	sites					613:617	the N-glycosylation sites	593:617	the N-glycosylation sites (N126, N195, and N213)	593:640	Only the extracellular region (aa 32-229) is needed for TC-Cbl binding, but the N-glycosylation sites (N126, N195, and N213) are of no importance for this function.
23603833	6	46	theme	Ca	962:963	arg1	binding					969:975	Ca(2+) binding	962:975	Ca(2+) binding	962:975	The two LDLR-A domains (aa 54-89 and 132-167) with the negatively charged acidic residues involved in Ca(2+) binding are critical determinants of ligand binding.
23603833	1	47	theme	membrane	119:126	arg1	TCblR/CD320					137:147	The membrane receptor TCblR/CD320	115:147	The membrane receptor TCblR/CD320	115:147	The membrane receptor TCblR/CD320 binds transcobalamin (TC) saturated with vitamin B12 [cobalamin (Cbl)] and mediates cellular uptake of the vitamin.
23603833	6	48	theme	binding	1013:1019	arg1	domains					875:881	The two LDLR-A domains	860:881	The two LDLR-A domains (aa 54-89 and 132-167) with the negatively charged acidic residues involved in Ca(2+) binding	860:975	The two LDLR-A domains (aa 54-89 and 132-167) with the negatively charged acidic residues involved in Ca(2+) binding are critical determinants of ligand binding.
23603833	6	48	theme	binding	1013:1019	arg1	determinants					990:1001	critical determinants	981:1001	critical determinants of ligand binding	981:1019	The two LDLR-A domains (aa 54-89 and 132-167) with the negatively charged acidic residues involved in Ca(2+) binding are critical determinants of ligand binding.
23603833	3	49	dep	TC-Cbl	414:419	arg1	-1					431:432	-1	431:432	-1	431:432	The high-affinity interaction of TCblR with TC-Cbl (Ka=10 nM(-1)) was investigated using deletions and mutations of amino acid sequences in TCblR.
23603833	3	49	dep	TC-Cbl	414:419	arg1	nM					428:429	Ka=10 nM	422:429	Ka=10 nM(-1)	422:433	The high-affinity interaction of TCblR with TC-Cbl (Ka=10 nM(-1)) was investigated using deletions and mutations of amino acid sequences in TCblR.
23603833	1	50	theme	receptor	128:135	arg1	TCblR/CD320					137:147	The membrane receptor TCblR/CD320	115:147	The membrane receptor TCblR/CD320	115:147	The membrane receptor TCblR/CD320 binds transcobalamin (TC) saturated with vitamin B12 [cobalamin (Cbl)] and mediates cellular uptake of the vitamin.
23603833	2	51	theme	TC	284:285	arg1	specificity					269:279	The specificity	265:279	The specificity of TC for Cbl and of the receptor for TC-Cbl	265:324	The specificity of TC for Cbl and of the receptor for TC-Cbl ensures efficient uptake of Cbl into cells.
23603833	1	52	with	saturated	175:183	arg1	[cobalamin					202:211	vitamin B12 [cobalamin	190:211	vitamin B12 [cobalamin (Cbl)]	190:218	The membrane receptor TCblR/CD320 binds transcobalamin (TC) saturated with vitamin B12 [cobalamin (Cbl)] and mediates cellular uptake of the vitamin.
23603833	1	52	with	saturated	175:183	arg1	Cbl					214:216	Cbl	214:216	Cbl	214:216	The membrane receptor TCblR/CD320 binds transcobalamin (TC) saturated with vitamin B12 [cobalamin (Cbl)] and mediates cellular uptake of the vitamin.
23603833	6	53	theme	ligand	1006:1011	arg1	binding					1013:1019	ligand binding	1006:1019	ligand binding	1006:1019	The two LDLR-A domains (aa 54-89 and 132-167) with the negatively charged acidic residues involved in Ca(2+) binding are critical determinants of ligand binding.
23603833	6	54	theme	charged	926:932	arg1	residues					941:948	the negatively charged acidic residues	911:948	the negatively charged acidic residues involved in Ca(2+) binding	911:975	The two LDLR-A domains (aa 54-89 and 132-167) with the negatively charged acidic residues involved in Ca(2+) binding are critical determinants of ligand binding.
23603833	5	55	dep	binding	831:837	arg1	Ka					840:841	Ka	840:841	Ka = 19-24 nM(-1)	840:856	Deleting the cysteine-rich region (aa 95-141) that separates the two low-density lipoprotein receptor type A (LDLR-A) domains does not affect TC-Cbl binding (Ka = 19-24 nM(-1)).
23603833	7	56	theme	cytoplasmic	1026:1036	arg1	crucial					1057:1063	crucial	1057:1063	crucial	1057:1063	The cytoplasmic tail is apparently crucial for internalization of the ligand.
23603833	7	56	theme	cytoplasmic	1026:1036	arg1	tail					1038:1041	The cytoplasmic tail	1022:1041	The cytoplasmic tail	1022:1041	The cytoplasmic tail is apparently crucial for internalization of the ligand.
23603833	6	57	with	domains	875:881	arg1	residues					941:948	the negatively charged acidic residues	911:948	the negatively charged acidic residues involved in Ca(2+) binding	911:975	The two LDLR-A domains (aa 54-89 and 132-167) with the negatively charged acidic residues involved in Ca(2+) binding are critical determinants of ligand binding.
23603833	9	58	theme	deficiency	1425:1434	arg1	phenotype					1408:1416	the biochemical and clinical phenotype	1379:1416	the biochemical and clinical phenotype of Cbl deficiency	1379:1434	Mutations and deletions of these regions involved in binding and internalization of TC-Cbl are likely to produce the biochemical and clinical phenotype of Cbl deficiency.
23603833	2	59	theme	efficient	334:342	arg1	uptake					344:349	efficient uptake	334:349	efficient uptake of Cbl into cells	334:367	The specificity of TC for Cbl and of the receptor for TC-Cbl ensures efficient uptake of Cbl into cells.
23603833	3	60	from	TCblR	510:514	arg1	mutations					473:481	mutations	473:481	mutations	473:481	The high-affinity interaction of TCblR with TC-Cbl (Ka=10 nM(-1)) was investigated using deletions and mutations of amino acid sequences in TCblR.
23603833	3	60	from	TCblR	510:514	arg1	deletions					459:467	deletions	459:467	deletions	459:467	The high-affinity interaction of TCblR with TC-Cbl (Ka=10 nM(-1)) was investigated using deletions and mutations of amino acid sequences in TCblR.
23603833	7	61	theme	ligand	1092:1097	arg1	internalization					1069:1083	internalization	1069:1083	internalization of the ligand	1069:1097	The cytoplasmic tail is apparently crucial for internalization of the ligand.
23603833	5	62	theme	receptor	775:782	arg1	LDLR-A					792:797	LDLR-A	792:797	LDLR-A	792:797	Deleting the cysteine-rich region (aa 95-141) that separates the two low-density lipoprotein receptor type A (LDLR-A) domains does not affect TC-Cbl binding (Ka = 19-24 nM(-1)).
23603833	5	62	theme	receptor	775:782	arg1	A					789:789	low-density lipoprotein receptor type A	751:789	the two low-density lipoprotein receptor type A (LDLR-A) domains	743:806	Deleting the cysteine-rich region (aa 95-141) that separates the two low-density lipoprotein receptor type A (LDLR-A) domains does not affect TC-Cbl binding (Ka = 19-24 nM(-1)).
12724313	0	0	theme	protein	83:89	arg1	specificity					101:111	protein substrate specificity	83:111	protein substrate specificity	83:111	Roles of the tetratricopeptide repeat domain in O-GlcNAc transferase targeting and protein substrate specificity.
12724313	11	1	theme	isolated	1174:1181	arg1	domain					1187:1192	the isolated TPR domain	1170:1192	the isolated TPR domain of OGT	1170:1199	Furthermore, the isolated TPR domain of OGT competitively inhibited glycosylation of the OID protein, but did not inhibit glycosylation of a 12-amino acid casein kinase II peptide substrate, providing kinetic evidence for the role of the TPR domain as a protein substrate docking site.
12724313	11	1	theme	isolated	1174:1181	arg1	OGT					1197:1199	OGT	1197:1199	OGT	1197:1199	Furthermore, the isolated TPR domain of OGT competitively inhibited glycosylation of the OID protein, but did not inhibit glycosylation of a 12-amino acid casein kinase II peptide substrate, providing kinetic evidence for the role of the TPR domain as a protein substrate docking site.
12724313	5	2	mod	modified	577:584	arg1	Members					550:556	Members	550:556	Members of this family	550:571	Members of this family are modified by O-GlcNAc and are excellent substrates of OGT.
12724313	5	2	mod	modified	577:584	arg3	O-GlcNAc					589:596	O-GlcNAc	589:596	O-GlcNAc	589:596	Members of this family are modified by O-GlcNAc and are excellent substrates of OGT.
12724313	11	3	theme	casein	1312:1317	arg1	substrate					1337:1345	a 12-amino acid casein kinase II peptide substrate	1296:1345	a 12-amino acid casein kinase II peptide substrate	1296:1345	Furthermore, the isolated TPR domain of OGT competitively inhibited glycosylation of the OID protein, but did not inhibit glycosylation of a 12-amino acid casein kinase II peptide substrate, providing kinetic evidence for the role of the TPR domain as a protein substrate docking site.
12724313	1	4	theme	nuclear	174:180	arg1	proteins					196:203	nuclear and cytosolic proteins	174:203	nuclear and cytosolic proteins	174:203	The abundant and dynamic post-translational modification of nuclear and cytosolic proteins by beta-O-linked N-acetylglucosamine (O-GlcNAc) is catalyzed by O-GlcNAc-transferase (OGT).
12724313	11	5	theme	kinase	1319:1324	arg1	substrate					1337:1345	a 12-amino acid casein kinase II peptide substrate	1296:1345	a 12-amino acid casein kinase II peptide substrate	1296:1345	Furthermore, the isolated TPR domain of OGT competitively inhibited glycosylation of the OID protein, but did not inhibit glycosylation of a 12-amino acid casein kinase II peptide substrate, providing kinetic evidence for the role of the TPR domain as a protein substrate docking site.
12724313	11	6	theme	TPR	1183:1185	arg1	domain					1187:1192	the isolated TPR domain	1170:1192	the isolated TPR domain of OGT	1170:1199	Furthermore, the isolated TPR domain of OGT competitively inhibited glycosylation of the OID protein, but did not inhibit glycosylation of a 12-amino acid casein kinase II peptide substrate, providing kinetic evidence for the role of the TPR domain as a protein substrate docking site.
12724313	11	6	theme	TPR	1183:1185	arg1	OGT					1197:1199	OGT	1197:1199	OGT	1197:1199	Furthermore, the isolated TPR domain of OGT competitively inhibited glycosylation of the OID protein, but did not inhibit glycosylation of a 12-amino acid casein kinase II peptide substrate, providing kinetic evidence for the role of the TPR domain as a protein substrate docking site.
12724313	11	7	theme	protein	1411:1417	arg1	site					1437:1440	a protein substrate docking site	1409:1440	a protein substrate docking site	1409:1440	Furthermore, the isolated TPR domain of OGT competitively inhibited glycosylation of the OID protein, but did not inhibit glycosylation of a 12-amino acid casein kinase II peptide substrate, providing kinetic evidence for the role of the TPR domain as a protein substrate docking site.
12724313	11	7	theme	protein	1411:1417	arg1	evidence					1366:1373	kinetic evidence	1358:1373	kinetic evidence for the role of the TPR domain	1358:1404	Furthermore, the isolated TPR domain of OGT competitively inhibited glycosylation of the OID protein, but did not inhibit glycosylation of a 12-amino acid casein kinase II peptide substrate, providing kinetic evidence for the role of the TPR domain as a protein substrate docking site.
12724313	5	8	theme	family	566:571	arg1	Members					550:556	Members	550:556	Members of this family	550:571	Members of this family are modified by O-GlcNAc and are excellent substrates of OGT.
12724313	11	9	gly	glycosylation	1225:1237	arg1	protein					1250:1256	the OID protein	1242:1256	the OID protein	1242:1256	Furthermore, the isolated TPR domain of OGT competitively inhibited glycosylation of the OID protein, but did not inhibit glycosylation of a 12-amino acid casein kinase II peptide substrate, providing kinetic evidence for the role of the TPR domain as a protein substrate docking site.
12724313	2	10	theme	proteins	375:382	arg1	family					349:354	a novel family	341:354	a novel family of OGT-interacting proteins (OIPs) that interact strongly with the tetratricopeptide repeat (TPR) domain of OGT (Iyer, S. P., Akimoto, Y., and Hart, G. W. (2003) J. Biol	341:524	Recently, we reported the identification of a novel family of OGT-interacting proteins (OIPs) that interact strongly with the tetratricopeptide repeat (TPR) domain of OGT (Iyer, S. P., Akimoto, Y., and Hart, G. W. (2003) J. Biol.
12724313	11	11	theme	12-amino	1298:1305	arg1	substrate					1337:1345	a 12-amino acid casein kinase II peptide substrate	1296:1345	a 12-amino acid casein kinase II peptide substrate	1296:1345	Furthermore, the isolated TPR domain of OGT competitively inhibited glycosylation of the OID protein, but did not inhibit glycosylation of a 12-amino acid casein kinase II peptide substrate, providing kinetic evidence for the role of the TPR domain as a protein substrate docking site.
12724313	0	12	from	Roles	0:4	arg1	specificity					101:111	protein substrate specificity	83:111	protein substrate specificity	83:111	Roles of the tetratricopeptide repeat domain in O-GlcNAc transferase targeting and protein substrate specificity.
12724313	0	12	from	Roles	0:4	arg1	targeting					69:77	O-GlcNAc transferase targeting	48:77	O-GlcNAc transferase targeting	48:77	Roles of the tetratricopeptide repeat domain in O-GlcNAc transferase targeting and protein substrate specificity.
12724313	10	13	gly	glycosylation	1067:1079	arg1	OID					1088:1090	the OID	1084:1090	the OID	1084:1090	Unlike small peptide substrates, glycosylation of the OID was dependent upon its interaction with the first 6 TPRs of OGT.
12724313	11	14	theme	substrate	1419:1427	arg1	site					1437:1440	a protein substrate docking site	1409:1440	a protein substrate docking site	1409:1440	Furthermore, the isolated TPR domain of OGT competitively inhibited glycosylation of the OID protein, but did not inhibit glycosylation of a 12-amino acid casein kinase II peptide substrate, providing kinetic evidence for the role of the TPR domain as a protein substrate docking site.
12724313	11	14	theme	substrate	1419:1427	arg1	evidence					1366:1373	kinetic evidence	1358:1373	kinetic evidence for the role of the TPR domain	1358:1404	Furthermore, the isolated TPR domain of OGT competitively inhibited glycosylation of the OID protein, but did not inhibit glycosylation of a 12-amino acid casein kinase II peptide substrate, providing kinetic evidence for the role of the TPR domain as a protein substrate docking site.
12724313	13	15	theme	proteins	1731:1738	arg1	variety					1710:1716	a variety	1708:1716	a variety of targeting proteins	1708:1738	These studies support the model that the catalytic subunit of OGT achieves both high specificity and a remarkable diversity of substrates by complexing with a variety of targeting proteins via its TPR protein-protein interaction domains.
12724313	13	15	theme	proteins	1731:1738	arg1	proteins					1731:1738	targeting proteins	1721:1738	targeting proteins	1721:1738	These studies support the model that the catalytic subunit of OGT achieves both high specificity and a remarkable diversity of substrates by complexing with a variety of targeting proteins via its TPR protein-protein interaction domains.
12724313	11	16	theme	acid	1307:1310	arg1	substrate					1337:1345	a 12-amino acid casein kinase II peptide substrate	1296:1345	a 12-amino acid casein kinase II peptide substrate	1296:1345	Furthermore, the isolated TPR domain of OGT competitively inhibited glycosylation of the OID protein, but did not inhibit glycosylation of a 12-amino acid casein kinase II peptide substrate, providing kinetic evidence for the role of the TPR domain as a protein substrate docking site.
12724313	0	17	theme	substrate	91:99	arg1	specificity					101:111	protein substrate specificity	83:111	protein substrate specificity	83:111	Roles of the tetratricopeptide repeat domain in O-GlcNAc transferase targeting and protein substrate specificity.
12724313	8	18	theme	Deletion	891:898	arg1	analysis					900:907	Deletion analysis	891:907	Deletion analysis	891:907	Deletion analysis indicated that TPRs 2-6 of OGT interact with the OID of OIP106.
12724313	9	19	theme	OIP106	1011:1016	arg1	OID					1004:1006	the OID	1000:1006	the OID of OIP106	1000:1016	The apparent Km of OGT for the OID of OIP106 is 3.35 microm.
12724313	13	20	theme	OGT	1613:1615	arg1	subunit					1602:1608	the catalytic subunit	1588:1608	the catalytic subunit of OGT	1588:1615	These studies support the model that the catalytic subunit of OGT achieves both high specificity and a remarkable diversity of substrates by complexing with a variety of targeting proteins via its TPR protein-protein interaction domains.
12724313	11	21	theme	OID	1246:1248	arg1	protein					1250:1256	the OID protein	1242:1256	the OID protein	1242:1256	Furthermore, the isolated TPR domain of OGT competitively inhibited glycosylation of the OID protein, but did not inhibit glycosylation of a 12-amino acid casein kinase II peptide substrate, providing kinetic evidence for the role of the TPR domain as a protein substrate docking site.
12724313	2	22	theme	novel	343:347	arg1	family					349:354	a novel family	341:354	a novel family of OGT-interacting proteins (OIPs) that interact strongly with the tetratricopeptide repeat (TPR) domain of OGT (Iyer, S. P., Akimoto, Y., and Hart, G. W. (2003) J. Biol	341:524	Recently, we reported the identification of a novel family of OGT-interacting proteins (OIPs) that interact strongly with the tetratricopeptide repeat (TPR) domain of OGT (Iyer, S. P., Akimoto, Y., and Hart, G. W. (2003) J. Biol.
12724313	11	23	theme	OGT	1197:1199	arg1	domain					1187:1192	the isolated TPR domain	1170:1192	the isolated TPR domain of OGT	1170:1199	Furthermore, the isolated TPR domain of OGT competitively inhibited glycosylation of the OID protein, but did not inhibit glycosylation of a 12-amino acid casein kinase II peptide substrate, providing kinetic evidence for the role of the TPR domain as a protein substrate docking site.
12724313	11	23	theme	OGT	1197:1199	arg1	OGT					1197:1199	OGT	1197:1199	OGT	1197:1199	Furthermore, the isolated TPR domain of OGT competitively inhibited glycosylation of the OID protein, but did not inhibit glycosylation of a 12-amino acid casein kinase II peptide substrate, providing kinetic evidence for the role of the TPR domain as a protein substrate docking site.
12724313	2	24	theme	OGT-interacting	359:373	arg1	OIPs					385:388	OIPs	385:388	OIPs	385:388	Recently, we reported the identification of a novel family of OGT-interacting proteins (OIPs) that interact strongly with the tetratricopeptide repeat (TPR) domain of OGT (Iyer, S. P., Akimoto, Y., and Hart, G. W. (2003) J. Biol.
12724313	2	24	theme	OGT-interacting	359:373	arg1	proteins					375:382	OGT-interacting proteins	359:382	OGT-interacting proteins (OIPs) that interact strongly with the tetratricopeptide repeat (TPR) domain of OGT (Iyer, S. P., Akimoto, Y., and Hart, G. W. (2003) J. Biol	359:524	Recently, we reported the identification of a novel family of OGT-interacting proteins (OIPs) that interact strongly with the tetratricopeptide repeat (TPR) domain of OGT (Iyer, S. P., Akimoto, Y., and Hart, G. W. (2003) J. Biol.
12724313	7	25	theme	OIP106	827:832	arg1	region					817:822	the region	813:822	the region of OIP106 that binds OGT, termed the OGT-interacting domain (OID)	813:888	Using N-terminal deletions, we first identified the region of OIP106 that binds OGT, termed the OGT-interacting domain (OID).
12724313	13	26	theme	remarkable	1654:1663	arg1	diversity					1665:1673	a remarkable diversity	1652:1673	a remarkable diversity of substrates	1652:1687	These studies support the model that the catalytic subunit of OGT achieves both high specificity and a remarkable diversity of substrates by complexing with a variety of targeting proteins via its TPR protein-protein interaction domains.
12724313	10	27	theme	peptide	1047:1053	arg1	substrates					1055:1064	small peptide substrates	1041:1064	small peptide substrates	1041:1064	Unlike small peptide substrates, glycosylation of the OID was dependent upon its interaction with the first 6 TPRs of OGT.
12724313	1	28	theme	cytosolic	186:194	arg1	proteins					196:203	nuclear and cytosolic proteins	174:203	nuclear and cytosolic proteins	174:203	The abundant and dynamic post-translational modification of nuclear and cytosolic proteins by beta-O-linked N-acetylglucosamine (O-GlcNAc) is catalyzed by O-GlcNAc-transferase (OGT).
12724313	6	29	theme	family	757:762	arg1	members					737:743	the members	733:743	the members of this OIP family	733:762	Here, we further investigated the role of the TPR domain in the O-GlcNAcylation of OIP106, one of the members of this OIP family.
12724313	1	30	link	beta-O-linked	208:220	arg1	O-GlcNAc					243:250	O-GlcNAc	243:250	O-GlcNAc	243:250	The abundant and dynamic post-translational modification of nuclear and cytosolic proteins by beta-O-linked N-acetylglucosamine (O-GlcNAc) is catalyzed by O-GlcNAc-transferase (OGT).
12724313	1	30	link	beta-O-linked	208:220	arg1	N-acetylglucosamine					222:240	beta-O-linked N-acetylglucosamine	208:240	beta-O-linked N-acetylglucosamine (O-GlcNAc)	208:251	The abundant and dynamic post-translational modification of nuclear and cytosolic proteins by beta-O-linked N-acetylglucosamine (O-GlcNAc) is catalyzed by O-GlcNAc-transferase (OGT).
12724313	6	31	theme	domain	685:690	arg1	role					669:672	the role	665:672	the role of the TPR domain in the O-GlcNAcylation of OIP106, one of the members of this OIP family	665:762	Here, we further investigated the role of the TPR domain in the O-GlcNAcylation of OIP106, one of the members of this OIP family.
12724313	1	32	theme	proteins	196:203	arg1	modification					158:169	The abundant and dynamic post-translational modification	114:169	The abundant and dynamic post-translational modification of nuclear and cytosolic proteins by beta-O-linked N-acetylglucosamine (O-GlcNAc)	114:251	The abundant and dynamic post-translational modification of nuclear and cytosolic proteins by beta-O-linked N-acetylglucosamine (O-GlcNAc) is catalyzed by O-GlcNAc-transferase (OGT).
12724313	6	33	theme	OIP	753:755	arg1	family					757:762	this OIP family	748:762	this OIP family	748:762	Here, we further investigated the role of the TPR domain in the O-GlcNAcylation of OIP106, one of the members of this OIP family.
12724313	6	34	theme	TPR	681:683	arg1	domain					685:690	the TPR domain	677:690	the TPR domain	677:690	Here, we further investigated the role of the TPR domain in the O-GlcNAcylation of OIP106, one of the members of this OIP family.
12724313	10	35	theme	first	1136:1140	arg1	TPRs					1144:1147	the first 6 TPRs	1132:1147	the first 6 TPRs of OGT	1132:1154	Unlike small peptide substrates, glycosylation of the OID was dependent upon its interaction with the first 6 TPRs of OGT.
12724313	1	36	theme	beta-O-linked	208:220	arg1	O-GlcNAc					243:250	O-GlcNAc	243:250	O-GlcNAc	243:250	The abundant and dynamic post-translational modification of nuclear and cytosolic proteins by beta-O-linked N-acetylglucosamine (O-GlcNAc) is catalyzed by O-GlcNAc-transferase (OGT).
12724313	1	36	theme	beta-O-linked	208:220	arg1	N-acetylglucosamine					222:240	beta-O-linked N-acetylglucosamine	208:240	beta-O-linked N-acetylglucosamine (O-GlcNAc)	208:251	The abundant and dynamic post-translational modification of nuclear and cytosolic proteins by beta-O-linked N-acetylglucosamine (O-GlcNAc) is catalyzed by O-GlcNAc-transferase (OGT).
12724313	0	37	theme	tetratricopeptide	13:29	arg1	domain					38:43	the tetratricopeptide repeat domain	9:43	the tetratricopeptide repeat domain	9:43	Roles of the tetratricopeptide repeat domain in O-GlcNAc transferase targeting and protein substrate specificity.
12724313	5	38	theme	excellent	606:614	arg1	substrates					616:625	excellent substrates	606:625	excellent substrates of OGT	606:632	Members of this family are modified by O-GlcNAc and are excellent substrates of OGT.
12724313	11	39	theme	peptide	1329:1335	arg1	substrate					1337:1345	a 12-amino acid casein kinase II peptide substrate	1296:1345	a 12-amino acid casein kinase II peptide substrate	1296:1345	Furthermore, the isolated TPR domain of OGT competitively inhibited glycosylation of the OID protein, but did not inhibit glycosylation of a 12-amino acid casein kinase II peptide substrate, providing kinetic evidence for the role of the TPR domain as a protein substrate docking site.
12724313	11	40	theme	substrate	1337:1345	arg1	glycosylation					1279:1291	glycosylation	1279:1291	glycosylation of a 12-amino acid casein kinase II peptide substrate	1279:1345	Furthermore, the isolated TPR domain of OGT competitively inhibited glycosylation of the OID protein, but did not inhibit glycosylation of a 12-amino acid casein kinase II peptide substrate, providing kinetic evidence for the role of the TPR domain as a protein substrate docking site.
12724313	11	41	theme	domain	1399:1404	arg1	role					1383:1386	the role	1379:1386	the role of the TPR domain	1379:1404	Furthermore, the isolated TPR domain of OGT competitively inhibited glycosylation of the OID protein, but did not inhibit glycosylation of a 12-amino acid casein kinase II peptide substrate, providing kinetic evidence for the role of the TPR domain as a protein substrate docking site.
12724313	2	42	theme	TPR	449:451	arg1	domain					454:459	the tetratricopeptide repeat (TPR) domain	419:459	the tetratricopeptide repeat (TPR) domain of OGT	419:466	Recently, we reported the identification of a novel family of OGT-interacting proteins (OIPs) that interact strongly with the tetratricopeptide repeat (TPR) domain of OGT (Iyer, S. P., Akimoto, Y., and Hart, G. W. (2003) J. Biol.
12724313	2	42	theme	TPR	449:451	arg1	OGT					464:466	OGT	464:466	OGT	464:466	Recently, we reported the identification of a novel family of OGT-interacting proteins (OIPs) that interact strongly with the tetratricopeptide repeat (TPR) domain of OGT (Iyer, S. P., Akimoto, Y., and Hart, G. W. (2003) J. Biol.
12724313	9	43	theme	apparent	977:984	arg1	microm					1026:1031	3.35 microm	1021:1031	3.35 microm	1021:1031	The apparent Km of OGT for the OID of OIP106 is 3.35 microm.
12724313	9	43	theme	apparent	977:984	arg1	Km					986:987	The apparent Km	973:987	The apparent Km of OGT for the OID of OIP106	973:1016	The apparent Km of OGT for the OID of OIP106 is 3.35 microm.
12724313	13	44	theme	interaction	1768:1778	arg1	domains					1780:1786	its TPR protein-protein interaction domains	1744:1786	its TPR protein-protein interaction domains	1744:1786	These studies support the model that the catalytic subunit of OGT achieves both high specificity and a remarkable diversity of substrates by complexing with a variety of targeting proteins via its TPR protein-protein interaction domains.
12724313	13	45	theme	targeting	1721:1729	arg1	proteins					1731:1738	targeting proteins	1721:1738	targeting proteins	1721:1738	These studies support the model that the catalytic subunit of OGT achieves both high specificity and a remarkable diversity of substrates by complexing with a variety of targeting proteins via its TPR protein-protein interaction domains.
12724313	2	46	theme	repeat	441:446	arg1	domain					454:459	the tetratricopeptide repeat (TPR) domain	419:459	the tetratricopeptide repeat (TPR) domain of OGT	419:466	Recently, we reported the identification of a novel family of OGT-interacting proteins (OIPs) that interact strongly with the tetratricopeptide repeat (TPR) domain of OGT (Iyer, S. P., Akimoto, Y., and Hart, G. W. (2003) J. Biol.
12724313	2	46	theme	repeat	441:446	arg1	OGT					464:466	OGT	464:466	OGT	464:466	Recently, we reported the identification of a novel family of OGT-interacting proteins (OIPs) that interact strongly with the tetratricopeptide repeat (TPR) domain of OGT (Iyer, S. P., Akimoto, Y., and Hart, G. W. (2003) J. Biol.
12724313	0	47	theme	domain	38:43	arg1	Roles					0:4	Roles	0:4	Roles of the tetratricopeptide repeat domain in O-GlcNAc transferase targeting and protein substrate specificity.	0:112	Roles of the tetratricopeptide repeat domain in O-GlcNAc transferase targeting and protein substrate specificity.
12724313	11	48	theme	protein	1250:1256	arg1	glycosylation					1225:1237	glycosylation	1225:1237	glycosylation of the OID protein	1225:1256	Furthermore, the isolated TPR domain of OGT competitively inhibited glycosylation of the OID protein, but did not inhibit glycosylation of a 12-amino acid casein kinase II peptide substrate, providing kinetic evidence for the role of the TPR domain as a protein substrate docking site.
12724313	13	49	theme	catalytic	1592:1600	arg1	subunit					1602:1608	the catalytic subunit	1588:1608	the catalytic subunit of OGT	1588:1615	These studies support the model that the catalytic subunit of OGT achieves both high specificity and a remarkable diversity of substrates by complexing with a variety of targeting proteins via its TPR protein-protein interaction domains.
12724313	12	50	theme	OIP106	1473:1478	arg1	p62					1496:1498	nucleoporin p62	1484:1498	nucleoporin p62	1484:1498	Additionally, both the OID of OIP106 and nucleoporin p62 competed with each other for glycosylation by OGT.
12724313	12	50	theme	OIP106	1473:1478	arg1	OID					1466:1468	the OID	1462:1468	the OID of OIP106	1462:1478	Additionally, both the OID of OIP106 and nucleoporin p62 competed with each other for glycosylation by OGT.
12724313	13	51	theme	substrates	1678:1687	arg1	diversity					1665:1673	a remarkable diversity	1652:1673	a remarkable diversity of substrates	1652:1687	These studies support the model that the catalytic subunit of OGT achieves both high specificity and a remarkable diversity of substrates by complexing with a variety of targeting proteins via its TPR protein-protein interaction domains.
12724313	13	51	theme	substrates	1678:1687	arg1	specificity					1636:1646	high specificity	1631:1646	high specificity	1631:1646	These studies support the model that the catalytic subunit of OGT achieves both high specificity and a remarkable diversity of substrates by complexing with a variety of targeting proteins via its TPR protein-protein interaction domains.
12724313	2	52	theme	tetratricopeptide	423:439	arg1	domain					454:459	the tetratricopeptide repeat (TPR) domain	419:459	the tetratricopeptide repeat (TPR) domain of OGT	419:466	Recently, we reported the identification of a novel family of OGT-interacting proteins (OIPs) that interact strongly with the tetratricopeptide repeat (TPR) domain of OGT (Iyer, S. P., Akimoto, Y., and Hart, G. W. (2003) J. Biol.
12724313	2	52	theme	tetratricopeptide	423:439	arg1	OGT					464:466	OGT	464:466	OGT	464:466	Recently, we reported the identification of a novel family of OGT-interacting proteins (OIPs) that interact strongly with the tetratricopeptide repeat (TPR) domain of OGT (Iyer, S. P., Akimoto, Y., and Hart, G. W. (2003) J. Biol.
12724313	0	53	theme	repeat	31:36	arg1	domain					38:43	the tetratricopeptide repeat domain	9:43	the tetratricopeptide repeat domain	9:43	Roles of the tetratricopeptide repeat domain in O-GlcNAc transferase targeting and protein substrate specificity.
12724313	5	54	theme	OGT	630:632	arg1	substrates					616:625	excellent substrates	606:625	excellent substrates of OGT	606:632	Members of this family are modified by O-GlcNAc and are excellent substrates of OGT.
12724313	6	55	theme	members	737:743	arg1	one					726:728	one	726:728	one	726:728	Here, we further investigated the role of the TPR domain in the O-GlcNAcylation of OIP106, one of the members of this OIP family.
12724313	6	55	theme	members	737:743	arg1	members					737:743	the members	733:743	the members of this OIP family	733:762	Here, we further investigated the role of the TPR domain in the O-GlcNAcylation of OIP106, one of the members of this OIP family.
12724313	6	55	theme	members	737:743	arg1	OIP106					718:723	OIP106	718:723	OIP106	718:723	Here, we further investigated the role of the TPR domain in the O-GlcNAcylation of OIP106, one of the members of this OIP family.
12724313	10	56	theme	OGT	1152:1154	arg1	TPRs					1144:1147	the first 6 TPRs	1132:1147	the first 6 TPRs of OGT	1132:1154	Unlike small peptide substrates, glycosylation of the OID was dependent upon its interaction with the first 6 TPRs of OGT.
12724313	0	57	theme	O-GlcNAc	48:55	arg1	targeting					69:77	O-GlcNAc transferase targeting	48:77	O-GlcNAc transferase targeting	48:77	Roles of the tetratricopeptide repeat domain in O-GlcNAc transferase targeting and protein substrate specificity.
12724313	2	58	dep	P.	478:479	arg1	W					508:508	W	508:508	Iyer, S. P., Akimoto, Y., and Hart, G. W. (2003) J. Biol	469:524	Recently, we reported the identification of a novel family of OGT-interacting proteins (OIPs) that interact strongly with the tetratricopeptide repeat (TPR) domain of OGT (Iyer, S. P., Akimoto, Y., and Hart, G. W. (2003) J. Biol.
12724313	2	58	dep	P.	478:479	arg1	Biol					521:524	Biol	521:524	Biol	521:524	Recently, we reported the identification of a novel family of OGT-interacting proteins (OIPs) that interact strongly with the tetratricopeptide repeat (TPR) domain of OGT (Iyer, S. P., Akimoto, Y., and Hart, G. W. (2003) J. Biol.
12724313	11	59	gly	glycosylation	1279:1291	arg1	substrate					1337:1345	a 12-amino acid casein kinase II peptide substrate	1296:1345	a 12-amino acid casein kinase II peptide substrate	1296:1345	Furthermore, the isolated TPR domain of OGT competitively inhibited glycosylation of the OID protein, but did not inhibit glycosylation of a 12-amino acid casein kinase II peptide substrate, providing kinetic evidence for the role of the TPR domain as a protein substrate docking site.
12724313	1	60	theme	abundant	118:125	arg1	modification					158:169	The abundant and dynamic post-translational modification	114:169	The abundant and dynamic post-translational modification of nuclear and cytosolic proteins by beta-O-linked N-acetylglucosamine (O-GlcNAc)	114:251	The abundant and dynamic post-translational modification of nuclear and cytosolic proteins by beta-O-linked N-acetylglucosamine (O-GlcNAc) is catalyzed by O-GlcNAc-transferase (OGT).
12724313	2	61	theme	OGT	464:466	arg1	domain					454:459	the tetratricopeptide repeat (TPR) domain	419:459	the tetratricopeptide repeat (TPR) domain of OGT	419:466	Recently, we reported the identification of a novel family of OGT-interacting proteins (OIPs) that interact strongly with the tetratricopeptide repeat (TPR) domain of OGT (Iyer, S. P., Akimoto, Y., and Hart, G. W. (2003) J. Biol.
12724313	2	61	theme	OGT	464:466	arg1	OGT					464:466	OGT	464:466	OGT	464:466	Recently, we reported the identification of a novel family of OGT-interacting proteins (OIPs) that interact strongly with the tetratricopeptide repeat (TPR) domain of OGT (Iyer, S. P., Akimoto, Y., and Hart, G. W. (2003) J. Biol.
12724313	8	62	theme	OGT	936:938	arg1	TPRs					924:927	TPRs 2-6	924:931	TPRs 2-6 of OGT	924:938	Deletion analysis indicated that TPRs 2-6 of OGT interact with the OID of OIP106.
12724313	10	63	with	interaction	1115:1125	arg1	TPRs					1144:1147	the first 6 TPRs	1132:1147	the first 6 TPRs of OGT	1132:1154	Unlike small peptide substrates, glycosylation of the OID was dependent upon its interaction with the first 6 TPRs of OGT.
12724313	7	64	theme	OGT-interacting	861:875	arg1	domain					877:882	the OGT-interacting domain	857:882	the OGT-interacting domain (OID)	857:888	Using N-terminal deletions, we first identified the region of OIP106 that binds OGT, termed the OGT-interacting domain (OID).
12724313	7	64	theme	OGT-interacting	861:875	arg1	OID					885:887	OID	885:887	OID	885:887	Using N-terminal deletions, we first identified the region of OIP106 that binds OGT, termed the OGT-interacting domain (OID).
12724313	12	65	theme	nucleoporin	1484:1494	arg1	p62					1496:1498	nucleoporin p62	1484:1498	nucleoporin p62	1484:1498	Additionally, both the OID of OIP106 and nucleoporin p62 competed with each other for glycosylation by OGT.
12724313	11	66	theme	kinetic	1358:1364	arg1	site					1437:1440	a protein substrate docking site	1409:1440	a protein substrate docking site	1409:1440	Furthermore, the isolated TPR domain of OGT competitively inhibited glycosylation of the OID protein, but did not inhibit glycosylation of a 12-amino acid casein kinase II peptide substrate, providing kinetic evidence for the role of the TPR domain as a protein substrate docking site.
12724313	11	66	theme	kinetic	1358:1364	arg1	evidence					1366:1373	kinetic evidence	1358:1373	kinetic evidence for the role of the TPR domain	1358:1404	Furthermore, the isolated TPR domain of OGT competitively inhibited glycosylation of the OID protein, but did not inhibit glycosylation of a 12-amino acid casein kinase II peptide substrate, providing kinetic evidence for the role of the TPR domain as a protein substrate docking site.
12724313	8	67	theme	OIP106	965:970	arg1	OID					958:960	the OID	954:960	the OID of OIP106	954:970	Deletion analysis indicated that TPRs 2-6 of OGT interact with the OID of OIP106.
12724313	6	68	from	role	669:672	arg1	O-GlcNAcylation					699:713	the O-GlcNAcylation	695:713	the O-GlcNAcylation of OIP106, one of the members of this OIP family	695:762	Here, we further investigated the role of the TPR domain in the O-GlcNAcylation of OIP106, one of the members of this OIP family.
12724313	2	69	dep	interact	396:403	arg1	G.					505:506	G.	505:506	G.	505:506	Recently, we reported the identification of a novel family of OGT-interacting proteins (OIPs) that interact strongly with the tetratricopeptide repeat (TPR) domain of OGT (Iyer, S. P., Akimoto, Y., and Hart, G. W. (2003) J. Biol.
12724313	2	69	dep	interact	396:403	arg1	Y.					491:492	Y.	491:492	Y.	491:492	Recently, we reported the identification of a novel family of OGT-interacting proteins (OIPs) that interact strongly with the tetratricopeptide repeat (TPR) domain of OGT (Iyer, S. P., Akimoto, Y., and Hart, G. W. (2003) J. Biol.
12724313	2	69	dep	interact	396:403	arg1	S.					475:476	S.	475:476	S.	475:476	Recently, we reported the identification of a novel family of OGT-interacting proteins (OIPs) that interact strongly with the tetratricopeptide repeat (TPR) domain of OGT (Iyer, S. P., Akimoto, Y., and Hart, G. W. (2003) J. Biol.
12724313	2	69	dep	interact	396:403	arg1	2003					512:515	2003	512:515	2003	512:515	Recently, we reported the identification of a novel family of OGT-interacting proteins (OIPs) that interact strongly with the tetratricopeptide repeat (TPR) domain of OGT (Iyer, S. P., Akimoto, Y., and Hart, G. W. (2003) J. Biol.
12724313	2	69	dep	interact	396:403	arg1	P.					478:479	P.	478:479	P.	478:479	Recently, we reported the identification of a novel family of OGT-interacting proteins (OIPs) that interact strongly with the tetratricopeptide repeat (TPR) domain of OGT (Iyer, S. P., Akimoto, Y., and Hart, G. W. (2003) J. Biol.
12724313	13	70	theme	high	1631:1634	arg1	specificity					1636:1646	high specificity	1631:1646	high specificity	1631:1646	These studies support the model that the catalytic subunit of OGT achieves both high specificity and a remarkable diversity of substrates by complexing with a variety of targeting proteins via its TPR protein-protein interaction domains.
12724313	1	71	theme	dynamic	131:137	arg1	modification					158:169	The abundant and dynamic post-translational modification	114:169	The abundant and dynamic post-translational modification of nuclear and cytosolic proteins by beta-O-linked N-acetylglucosamine (O-GlcNAc)	114:251	The abundant and dynamic post-translational modification of nuclear and cytosolic proteins by beta-O-linked N-acetylglucosamine (O-GlcNAc) is catalyzed by O-GlcNAc-transferase (OGT).
12724313	4	72	dep	278	533:535	arg1	5399-5409					538:546	5399-5409	538:546	5399-5409	538:546	278, 5399-5409).
12724313	13	73	theme	protein-protein	1752:1766	arg1	domains					1780:1786	its TPR protein-protein interaction domains	1744:1786	its TPR protein-protein interaction domains	1744:1786	These studies support the model that the catalytic subunit of OGT achieves both high specificity and a remarkable diversity of substrates by complexing with a variety of targeting proteins via its TPR protein-protein interaction domains.
12724313	1	74	theme	post-translational	139:156	arg1	modification					158:169	The abundant and dynamic post-translational modification	114:169	The abundant and dynamic post-translational modification of nuclear and cytosolic proteins by beta-O-linked N-acetylglucosamine (O-GlcNAc)	114:251	The abundant and dynamic post-translational modification of nuclear and cytosolic proteins by beta-O-linked N-acetylglucosamine (O-GlcNAc) is catalyzed by O-GlcNAc-transferase (OGT).
12724313	7	75	theme	N-terminal	771:780	arg1	deletions					782:790	N-terminal deletions	771:790	N-terminal deletions	771:790	Using N-terminal deletions, we first identified the region of OIP106 that binds OGT, termed the OGT-interacting domain (OID).
12724313	2	76	theme	family	349:354	arg1	identification					323:336	the identification	319:336	the identification of a novel family of OGT-interacting proteins (OIPs) that interact strongly with the tetratricopeptide repeat (TPR) domain of OGT (Iyer, S. P., Akimoto, Y., and Hart, G. W. (2003) J. Biol	319:524	Recently, we reported the identification of a novel family of OGT-interacting proteins (OIPs) that interact strongly with the tetratricopeptide repeat (TPR) domain of OGT (Iyer, S. P., Akimoto, Y., and Hart, G. W. (2003) J. Biol.
12724313	6	77	theme	OIP106	718:723	arg1	O-GlcNAcylation					699:713	the O-GlcNAcylation	695:713	the O-GlcNAcylation of OIP106, one of the members of this OIP family	695:762	Here, we further investigated the role of the TPR domain in the O-GlcNAcylation of OIP106, one of the members of this OIP family.
12724313	13	78	theme	TPR	1748:1750	arg1	domains					1780:1786	its TPR protein-protein interaction domains	1744:1786	its TPR protein-protein interaction domains	1744:1786	These studies support the model that the catalytic subunit of OGT achieves both high specificity and a remarkable diversity of substrates by complexing with a variety of targeting proteins via its TPR protein-protein interaction domains.
12724313	9	79	theme	OGT	992:994	arg1	microm					1026:1031	3.35 microm	1021:1031	3.35 microm	1021:1031	The apparent Km of OGT for the OID of OIP106 is 3.35 microm.
12724313	9	79	theme	OGT	992:994	arg1	Km					986:987	The apparent Km	973:987	The apparent Km of OGT for the OID of OIP106	973:1016	The apparent Km of OGT for the OID of OIP106 is 3.35 microm.
12724313	10	80	theme	small	1041:1045	arg1	substrates					1055:1064	small peptide substrates	1041:1064	small peptide substrates	1041:1064	Unlike small peptide substrates, glycosylation of the OID was dependent upon its interaction with the first 6 TPRs of OGT.
12724313	0	81	theme	transferase	57:67	arg1	targeting					69:77	O-GlcNAc transferase targeting	48:77	O-GlcNAc transferase targeting	48:77	Roles of the tetratricopeptide repeat domain in O-GlcNAc transferase targeting and protein substrate specificity.
12724313	11	82	theme	docking	1429:1435	arg1	site					1437:1440	a protein substrate docking site	1409:1440	a protein substrate docking site	1409:1440	Furthermore, the isolated TPR domain of OGT competitively inhibited glycosylation of the OID protein, but did not inhibit glycosylation of a 12-amino acid casein kinase II peptide substrate, providing kinetic evidence for the role of the TPR domain as a protein substrate docking site.
12724313	11	82	theme	docking	1429:1435	arg1	evidence					1366:1373	kinetic evidence	1358:1373	kinetic evidence for the role of the TPR domain	1358:1404	Furthermore, the isolated TPR domain of OGT competitively inhibited glycosylation of the OID protein, but did not inhibit glycosylation of a 12-amino acid casein kinase II peptide substrate, providing kinetic evidence for the role of the TPR domain as a protein substrate docking site.
12724313	11	83	theme	TPR	1395:1397	arg1	domain					1399:1404	the TPR domain	1391:1404	the TPR domain	1391:1404	Furthermore, the isolated TPR domain of OGT competitively inhibited glycosylation of the OID protein, but did not inhibit glycosylation of a 12-amino acid casein kinase II peptide substrate, providing kinetic evidence for the role of the TPR domain as a protein substrate docking site.
12724313	10	84	theme	OID	1088:1090	arg1	glycosylation					1067:1079	glycosylation	1067:1079	glycosylation of the OID	1067:1090	Unlike small peptide substrates, glycosylation of the OID was dependent upon its interaction with the first 6 TPRs of OGT.
7654718	2	0	theme	large-scale	343:353	arg1	purification					355:366	A large-scale purification	341:366	A large-scale purification method	341:373	A large-scale purification method has been devised to purify the C-tail fragment from human milk BAL.
7654718	7	1	theme	pronase	1117:1123	arg1	subfragment					1125:1135	its pronase subfragment	1113:1135	its pronase subfragment	1113:1135	Edman degradation of C-tail fragment and its pronase subfragment suggest a number of glycosylation sites which are flanked by a consensus motif of PVPP.
7654718	3	2	theme	sieve	548:552	arg1	chromatography					554:567	subsequent molecular sieve chromatography	527:567	subsequent molecular sieve chromatography	527:567	Chymotryptic, tryptic, and cyanogen bromide cleavages of partially purified BAL and subsequent molecular sieve chromatography yielded 20-30 mg of C-tail fragment from 1 L of human milk.
7654718	10	3	theme	C-tail	1520:1525	arg1	fragment					1527:1534	C-tail fragment	1520:1534	C-tail fragment	1520:1534	C-tail fragment was also found to bind jacalin lectin.
7654718	9	4	contain	contain	1416:1422	arg1	chains					1381:1386	the oligosaccharide chains	1361:1386	the oligosaccharide chains in the C-tail region of BAL	1361:1414	Immunochemical studies indicated that the oligosaccharide chains in the C-tail region of BAL contain Lewis x and Lewis a antigens and, less prominently, sialyl Lewis x and sialyl Lewis a antigens.
7654718	9	4	contain	contain	1416:1422	arg2	antigens					1444:1451	Lewis x and Lewis a antigens	1424:1451	Lewis x and Lewis a antigens	1424:1451	Immunochemical studies indicated that the oligosaccharide chains in the C-tail region of BAL contain Lewis x and Lewis a antigens and, less prominently, sialyl Lewis x and sialyl Lewis a antigens.
7654718	9	4	contain	contain	1416:1422	arg2	x					1489:1489	sialyl Lewis x	1476:1489	sialyl Lewis x	1476:1489	Immunochemical studies indicated that the oligosaccharide chains in the C-tail region of BAL contain Lewis x and Lewis a antigens and, less prominently, sialyl Lewis x and sialyl Lewis a antigens.
7654718	3	5	theme	subsequent	527:536	arg1	chromatography					554:567	subsequent molecular sieve chromatography	527:567	subsequent molecular sieve chromatography	527:567	Chymotryptic, tryptic, and cyanogen bromide cleavages of partially purified BAL and subsequent molecular sieve chromatography yielded 20-30 mg of C-tail fragment from 1 L of human milk.
7654718	9	6	theme	x	1430:1430	arg1	antigens					1444:1451	Lewis x and Lewis a antigens	1424:1451	Lewis x and Lewis a antigens	1424:1451	Immunochemical studies indicated that the oligosaccharide chains in the C-tail region of BAL contain Lewis x and Lewis a antigens and, less prominently, sialyl Lewis x and sialyl Lewis a antigens.
7654718	4	7	theme	acid	663:666	arg1	composition					668:678	amino acid composition	657:678	amino acid composition	657:678	The N-terminal sequence and amino acid composition of the purified C-tail fragment establish that it is derived from residues 528-712 of the enzyme.
7654718	7	8	theme	C-tail	1093:1098	arg1	fragment					1100:1107	C-tail fragment	1093:1107	C-tail fragment	1093:1107	Edman degradation of C-tail fragment and its pronase subfragment suggest a number of glycosylation sites which are flanked by a consensus motif of PVPP.
7654718	9	9	theme	Lewis	1436:1440	arg1	a					1442:1442	Lewis a	1436:1442	Lewis a	1436:1442	Immunochemical studies indicated that the oligosaccharide chains in the C-tail region of BAL contain Lewis x and Lewis a antigens and, less prominently, sialyl Lewis x and sialyl Lewis a antigens.
7654718	6	10	theme	beta-Elimination	956:971	arg1	reaction					973:980	beta-Elimination reaction	956:980	beta-Elimination reaction	956:980	beta-Elimination reaction revealed that nine threonine residues and less than one serine residue were glycosylated.
7654718	1	11	theme	human	212:216	arg1	milk					218:221	human milk bile salt-activated lipase (BAL)	212:254	human milk bile salt-activated lipase (BAL)	212:254	Glycosylation positions and oligosaccharide characteristics in the proline-rich, mucin-like, C-terminal region (C-tail) of human milk bile salt-activated lipase (BAL) were studied in order to assess the possible physiological functions of this region.
7654718	4	12	theme	N-terminal	633:642	arg1	sequence					644:651	The N-terminal sequence	629:651	The N-terminal sequence	629:651	The N-terminal sequence and amino acid composition of the purified C-tail fragment establish that it is derived from residues 528-712 of the enzyme.
7654718	1	13	theme	bile	223:226	arg1	BAL					251:253	BAL	251:253	BAL	251:253	Glycosylation positions and oligosaccharide characteristics in the proline-rich, mucin-like, C-terminal region (C-tail) of human milk bile salt-activated lipase (BAL) were studied in order to assess the possible physiological functions of this region.
7654718	1	13	theme	bile	223:226	arg1	lipase					243:248	bile salt-activated lipase	223:248	human milk bile salt-activated lipase (BAL)	212:254	Glycosylation positions and oligosaccharide characteristics in the proline-rich, mucin-like, C-terminal region (C-tail) of human milk bile salt-activated lipase (BAL) were studied in order to assess the possible physiological functions of this region.
7654718	4	14	theme	fragment	703:710	arg1	composition					668:678	amino acid composition	657:678	amino acid composition	657:678	The N-terminal sequence and amino acid composition of the purified C-tail fragment establish that it is derived from residues 528-712 of the enzyme.
7654718	4	14	theme	fragment	703:710	arg1	sequence					644:651	The N-terminal sequence	629:651	The N-terminal sequence	629:651	The N-terminal sequence and amino acid composition of the purified C-tail fragment establish that it is derived from residues 528-712 of the enzyme.
7654718	4	15	attach	derived	733:739	arg2	it					727:728	it	727:728	it	727:728	The N-terminal sequence and amino acid composition of the purified C-tail fragment establish that it is derived from residues 528-712 of the enzyme.
7654718	4	15	attach	derived	733:739	arg1	enzyme					770:775	the enzyme	766:775	the enzyme	766:775	The N-terminal sequence and amino acid composition of the purified C-tail fragment establish that it is derived from residues 528-712 of the enzyme.
7654718	4	15	attach	derived	733:739	arg1	residues					746:753	residues 528-712	746:761	residues 528-712 of the enzyme	746:775	The N-terminal sequence and amino acid composition of the purified C-tail fragment establish that it is derived from residues 528-712 of the enzyme.
7654718	3	16	theme	C-tail	589:594	arg1	fragment					596:603	C-tail fragment	589:603	C-tail fragment	589:603	Chymotryptic, tryptic, and cyanogen bromide cleavages of partially purified BAL and subsequent molecular sieve chromatography yielded 20-30 mg of C-tail fragment from 1 L of human milk.
7654718	3	17	theme	human	617:621	arg1	milk					623:626	human milk	617:626	human milk	617:626	Chymotryptic, tryptic, and cyanogen bromide cleavages of partially purified BAL and subsequent molecular sieve chromatography yielded 20-30 mg of C-tail fragment from 1 L of human milk.
7654718	9	18	theme	sialyl	1476:1481	arg1	x					1489:1489	sialyl Lewis x	1476:1489	sialyl Lewis x	1476:1489	Immunochemical studies indicated that the oligosaccharide chains in the C-tail region of BAL contain Lewis x and Lewis a antigens and, less prominently, sialyl Lewis x and sialyl Lewis a antigens.
7654718	8	19	theme	C-tail	1301:1306	arg1	region					1308:1313	the C-tail region	1297:1313	the C-tail region of BAL	1297:1320	We suggest that this motif may serve as a signal for O-glycosylation in the C-tail region of BAL.
7654718	0	20	theme	lipase	65:70	arg1	fragment					79:86	lipase C-tail fragment	65:86	lipase C-tail fragment	65:86	Isolation and characterization of human milk bile salt-activated lipase C-tail fragment.
7654718	1	21	theme	mucin-like	170:179	arg1	C-tail					201:206	C-tail	201:206	C-tail	201:206	Glycosylation positions and oligosaccharide characteristics in the proline-rich, mucin-like, C-terminal region (C-tail) of human milk bile salt-activated lipase (BAL) were studied in order to assess the possible physiological functions of this region.
7654718	1	21	theme	mucin-like	170:179	arg1	region					193:198	C-terminal region	182:198	C-terminal region (C-tail)	182:207	Glycosylation positions and oligosaccharide characteristics in the proline-rich, mucin-like, C-terminal region (C-tail) of human milk bile salt-activated lipase (BAL) were studied in order to assess the possible physiological functions of this region.
7654718	4	22	theme	purified	687:694	arg1	fragment					703:710	the purified C-tail fragment	683:710	the purified C-tail fragment	683:710	The N-terminal sequence and amino acid composition of the purified C-tail fragment establish that it is derived from residues 528-712 of the enzyme.
7654718	7	23	theme	PVPP	1219:1222	arg1	motif					1210:1214	a consensus motif	1198:1214	a consensus motif of PVPP	1198:1222	Edman degradation of C-tail fragment and its pronase subfragment suggest a number of glycosylation sites which are flanked by a consensus motif of PVPP.
7654718	1	24	theme	C-terminal	182:191	arg1	C-tail					201:206	C-tail	201:206	C-tail	201:206	Glycosylation positions and oligosaccharide characteristics in the proline-rich, mucin-like, C-terminal region (C-tail) of human milk bile salt-activated lipase (BAL) were studied in order to assess the possible physiological functions of this region.
7654718	1	24	theme	C-terminal	182:191	arg1	region					193:198	C-terminal region	182:198	C-terminal region (C-tail)	182:207	Glycosylation positions and oligosaccharide characteristics in the proline-rich, mucin-like, C-terminal region (C-tail) of human milk bile salt-activated lipase (BAL) were studied in order to assess the possible physiological functions of this region.
7654718	2	25	from	BAL	438:440	arg1	fragment					413:420	the C-tail fragment	402:420	the C-tail fragment from human milk BAL	402:440	A large-scale purification method has been devised to purify the C-tail fragment from human milk BAL.
7654718	9	26	theme	a	1508:1508	arg1	antigens					1510:1517	a antigens	1508:1517	a antigens	1508:1517	Immunochemical studies indicated that the oligosaccharide chains in the C-tail region of BAL contain Lewis x and Lewis a antigens and, less prominently, sialyl Lewis x and sialyl Lewis a antigens.
7654718	5	27	theme	molar	914:918	arg1	ratio					920:924	a molar ratio	912:924	a molar ratio of 1:3:2:1:0.3, respectively	912:953	The O-glycosylated carbohydrates of the C-tail fragment contain fucose, galactose, glucosamine, galactosamine, and neuraminic acid in a molar ratio of 1:3:2:1:0.3, respectively.
7654718	3	28	from	L	612:612	arg1	mg					583:584	20-30 mg	577:584	20-30 mg of C-tail fragment from 1 L of human milk	577:626	Chymotryptic, tryptic, and cyanogen bromide cleavages of partially purified BAL and subsequent molecular sieve chromatography yielded 20-30 mg of C-tail fragment from 1 L of human milk.
7654718	1	29	theme	proline-rich	156:167	arg1	C-tail					201:206	C-tail	201:206	C-tail	201:206	Glycosylation positions and oligosaccharide characteristics in the proline-rich, mucin-like, C-terminal region (C-tail) of human milk bile salt-activated lipase (BAL) were studied in order to assess the possible physiological functions of this region.
7654718	1	29	theme	proline-rich	156:167	arg1	region					193:198	C-terminal region	182:198	C-terminal region (C-tail)	182:207	Glycosylation positions and oligosaccharide characteristics in the proline-rich, mucin-like, C-terminal region (C-tail) of human milk bile salt-activated lipase (BAL) were studied in order to assess the possible physiological functions of this region.
7654718	1	30	from	characteristics	133:147	arg1	C-tail					201:206	C-tail	201:206	C-tail	201:206	Glycosylation positions and oligosaccharide characteristics in the proline-rich, mucin-like, C-terminal region (C-tail) of human milk bile salt-activated lipase (BAL) were studied in order to assess the possible physiological functions of this region.
7654718	1	30	from	characteristics	133:147	arg1	region					193:198	C-terminal region	182:198	C-terminal region (C-tail)	182:207	Glycosylation positions and oligosaccharide characteristics in the proline-rich, mucin-like, C-terminal region (C-tail) of human milk bile salt-activated lipase (BAL) were studied in order to assess the possible physiological functions of this region.
7654718	2	31	theme	milk	433:436	arg1	BAL					438:440	human milk BAL	427:440	human milk BAL	427:440	A large-scale purification method has been devised to purify the C-tail fragment from human milk BAL.
7654718	3	32	theme	tryptic	457:463	arg1	cleavages					487:495	Chymotryptic, tryptic, and cyanogen bromide cleavages	443:495	Chymotryptic, tryptic, and cyanogen bromide cleavages of partially purified BAL and subsequent molecular sieve chromatography	443:567	Chymotryptic, tryptic, and cyanogen bromide cleavages of partially purified BAL and subsequent molecular sieve chromatography yielded 20-30 mg of C-tail fragment from 1 L of human milk.
7654718	5	33	theme	C-tail	818:823	arg1	fragment					825:832	the C-tail fragment	814:832	the C-tail fragment	814:832	The O-glycosylated carbohydrates of the C-tail fragment contain fucose, galactose, glucosamine, galactosamine, and neuraminic acid in a molar ratio of 1:3:2:1:0.3, respectively.
7654718	9	34	theme	Immunochemical	1323:1336	arg1	studies					1338:1344	Immunochemical studies	1323:1344	Immunochemical studies	1323:1344	Immunochemical studies indicated that the oligosaccharide chains in the C-tail region of BAL contain Lewis x and Lewis a antigens and, less prominently, sialyl Lewis x and sialyl Lewis a antigens.
7654718	1	35	theme	oligosaccharide	117:131	arg1	characteristics					133:147	oligosaccharide characteristics	117:147	oligosaccharide characteristics	117:147	Glycosylation positions and oligosaccharide characteristics in the proline-rich, mucin-like, C-terminal region (C-tail) of human milk bile salt-activated lipase (BAL) were studied in order to assess the possible physiological functions of this region.
7654718	3	36	theme	Chymotryptic	443:454	arg1	cleavages					487:495	Chymotryptic, tryptic, and cyanogen bromide cleavages	443:495	Chymotryptic, tryptic, and cyanogen bromide cleavages of partially purified BAL and subsequent molecular sieve chromatography	443:567	Chymotryptic, tryptic, and cyanogen bromide cleavages of partially purified BAL and subsequent molecular sieve chromatography yielded 20-30 mg of C-tail fragment from 1 L of human milk.
7654718	7	37	gly	glycosylation	1157:1169	arg2	sites					1171:1175	glycosylation sites	1157:1175	glycosylation sites which are flanked by a consensus motif of PVPP	1157:1222	Edman degradation of C-tail fragment and its pronase subfragment suggest a number of glycosylation sites which are flanked by a consensus motif of PVPP.
7654718	2	38	theme	C-tail	406:411	arg1	fragment					413:420	the C-tail fragment	402:420	the C-tail fragment from human milk BAL	402:440	A large-scale purification method has been devised to purify the C-tail fragment from human milk BAL.
7654718	0	39	theme	human	34:38	arg1	bile					45:48	human milk bile	34:48	human milk bile	34:48	Isolation and characterization of human milk bile salt-activated lipase C-tail fragment.
7654718	1	40	theme	possible	292:299	arg1	functions					315:323	the possible physiological functions	288:323	the possible physiological functions of this region	288:338	Glycosylation positions and oligosaccharide characteristics in the proline-rich, mucin-like, C-terminal region (C-tail) of human milk bile salt-activated lipase (BAL) were studied in order to assess the possible physiological functions of this region.
7654718	7	41	theme	glycosylation	1157:1169	arg1	sites					1171:1175	glycosylation sites	1157:1175	glycosylation sites which are flanked by a consensus motif of PVPP	1157:1222	Edman degradation of C-tail fragment and its pronase subfragment suggest a number of glycosylation sites which are flanked by a consensus motif of PVPP.
7654718	3	42	theme	bromide	479:485	arg1	cleavages					487:495	Chymotryptic, tryptic, and cyanogen bromide cleavages	443:495	Chymotryptic, tryptic, and cyanogen bromide cleavages of partially purified BAL and subsequent molecular sieve chromatography	443:567	Chymotryptic, tryptic, and cyanogen bromide cleavages of partially purified BAL and subsequent molecular sieve chromatography yielded 20-30 mg of C-tail fragment from 1 L of human milk.
7654718	5	43	theme	O-glycosylated	782:795	arg1	carbohydrates					797:809	The O-glycosylated carbohydrates	778:809	The O-glycosylated carbohydrates of the C-tail fragment	778:832	The O-glycosylated carbohydrates of the C-tail fragment contain fucose, galactose, glucosamine, galactosamine, and neuraminic acid in a molar ratio of 1:3:2:1:0.3, respectively.
7654718	6	44	gly	glycosylated	1058:1069	arg1	residue					1045:1051	less than one serine residue	1024:1051	less than one serine residue	1024:1051	beta-Elimination reaction revealed that nine threonine residues and less than one serine residue were glycosylated.
7654718	6	44	gly	glycosylated	1058:1069	arg1	residues					1011:1018	nine threonine residues	996:1018	nine threonine residues	996:1018	beta-Elimination reaction revealed that nine threonine residues and less than one serine residue were glycosylated.
7654718	1	45	dep	milk	218:221	arg1	BAL					251:253	BAL	251:253	BAL	251:253	Glycosylation positions and oligosaccharide characteristics in the proline-rich, mucin-like, C-terminal region (C-tail) of human milk bile salt-activated lipase (BAL) were studied in order to assess the possible physiological functions of this region.
7654718	1	45	dep	milk	218:221	arg1	lipase					243:248	bile salt-activated lipase	223:248	human milk bile salt-activated lipase (BAL)	212:254	Glycosylation positions and oligosaccharide characteristics in the proline-rich, mucin-like, C-terminal region (C-tail) of human milk bile salt-activated lipase (BAL) were studied in order to assess the possible physiological functions of this region.
7654718	1	46	theme	salt-activated	228:241	arg1	BAL					251:253	BAL	251:253	BAL	251:253	Glycosylation positions and oligosaccharide characteristics in the proline-rich, mucin-like, C-terminal region (C-tail) of human milk bile salt-activated lipase (BAL) were studied in order to assess the possible physiological functions of this region.
7654718	1	46	theme	salt-activated	228:241	arg1	lipase					243:248	bile salt-activated lipase	223:248	human milk bile salt-activated lipase (BAL)	212:254	Glycosylation positions and oligosaccharide characteristics in the proline-rich, mucin-like, C-terminal region (C-tail) of human milk bile salt-activated lipase (BAL) were studied in order to assess the possible physiological functions of this region.
7654718	5	47	gly	O-glycosylated	782:795	arg1	carbohydrates					797:809	The O-glycosylated carbohydrates	778:809	The O-glycosylated carbohydrates of the C-tail fragment	778:832	The O-glycosylated carbohydrates of the C-tail fragment contain fucose, galactose, glucosamine, galactosamine, and neuraminic acid in a molar ratio of 1:3:2:1:0.3, respectively.
7654718	3	48	theme	purified	510:517	arg1	BAL					519:521	partially purified BAL	500:521	partially purified BAL	500:521	Chymotryptic, tryptic, and cyanogen bromide cleavages of partially purified BAL and subsequent molecular sieve chromatography yielded 20-30 mg of C-tail fragment from 1 L of human milk.
7654718	1	49	from	positions	103:111	arg1	C-tail					201:206	C-tail	201:206	C-tail	201:206	Glycosylation positions and oligosaccharide characteristics in the proline-rich, mucin-like, C-terminal region (C-tail) of human milk bile salt-activated lipase (BAL) were studied in order to assess the possible physiological functions of this region.
7654718	1	49	from	positions	103:111	arg1	region					193:198	C-terminal region	182:198	C-terminal region (C-tail)	182:207	Glycosylation positions and oligosaccharide characteristics in the proline-rich, mucin-like, C-terminal region (C-tail) of human milk bile salt-activated lipase (BAL) were studied in order to assess the possible physiological functions of this region.
7654718	2	50	theme	purification	355:366	arg1	method					368:373	A large-scale purification method	341:373	A large-scale purification method	341:373	A large-scale purification method has been devised to purify the C-tail fragment from human milk BAL.
7654718	3	51	theme	molecular	538:546	arg1	chromatography					554:567	subsequent molecular sieve chromatography	527:567	subsequent molecular sieve chromatography	527:567	Chymotryptic, tryptic, and cyanogen bromide cleavages of partially purified BAL and subsequent molecular sieve chromatography yielded 20-30 mg of C-tail fragment from 1 L of human milk.
7654718	9	52	theme	BAL	1412:1414	arg1	region					1402:1407	the C-tail region	1391:1407	the C-tail region of BAL	1391:1414	Immunochemical studies indicated that the oligosaccharide chains in the C-tail region of BAL contain Lewis x and Lewis a antigens and, less prominently, sialyl Lewis x and sialyl Lewis a antigens.
7654718	7	53	theme	fragment	1100:1107	arg1	subfragment					1125:1135	its pronase subfragment	1113:1135	its pronase subfragment	1113:1135	Edman degradation of C-tail fragment and its pronase subfragment suggest a number of glycosylation sites which are flanked by a consensus motif of PVPP.
7654718	7	53	theme	fragment	1100:1107	arg1	degradation					1078:1088	Edman degradation	1072:1088	Edman degradation of C-tail fragment	1072:1107	Edman degradation of C-tail fragment and its pronase subfragment suggest a number of glycosylation sites which are flanked by a consensus motif of PVPP.
7654718	9	54	theme	Lewis	1424:1428	arg1	x					1430:1430	Lewis x	1424:1430	Lewis x	1424:1430	Immunochemical studies indicated that the oligosaccharide chains in the C-tail region of BAL contain Lewis x and Lewis a antigens and, less prominently, sialyl Lewis x and sialyl Lewis a antigens.
7654718	0	55	theme	bile	45:48	arg1	characterization					14:29	characterization	14:29	characterization	14:29	Isolation and characterization of human milk bile salt-activated lipase C-tail fragment.
7654718	0	55	theme	bile	45:48	arg1	Isolation					0:8	Isolation	0:8	Isolation	0:8	Isolation and characterization of human milk bile salt-activated lipase C-tail fragment.
7654718	10	56	theme	jacalin	1559:1565	arg1	lectin					1567:1572	jacalin lectin	1559:1572	jacalin lectin	1559:1572	C-tail fragment was also found to bind jacalin lectin.
7654718	11	57	theme	C-tail	1627:1632	arg1	region					1634:1639	the C-tail region	1623:1639	the C-tail region	1623:1639	These observations suggest the possibility that the C-tail region may contribute to adhesive activity in the physiological function of BAL.
7654718	4	58	theme	amino	657:661	arg1	composition					668:678	amino acid composition	657:678	amino acid composition	657:678	The N-terminal sequence and amino acid composition of the purified C-tail fragment establish that it is derived from residues 528-712 of the enzyme.
7654718	7	59	theme	Edman	1072:1076	arg1	degradation					1078:1088	Edman degradation	1072:1088	Edman degradation of C-tail fragment	1072:1107	Edman degradation of C-tail fragment and its pronase subfragment suggest a number of glycosylation sites which are flanked by a consensus motif of PVPP.
7654718	3	60	theme	chromatography	554:567	arg1	cleavages					487:495	Chymotryptic, tryptic, and cyanogen bromide cleavages	443:495	Chymotryptic, tryptic, and cyanogen bromide cleavages of partially purified BAL and subsequent molecular sieve chromatography	443:567	Chymotryptic, tryptic, and cyanogen bromide cleavages of partially purified BAL and subsequent molecular sieve chromatography yielded 20-30 mg of C-tail fragment from 1 L of human milk.
7654718	9	61	theme	a	1442:1442	arg1	antigens					1444:1451	Lewis x and Lewis a antigens	1424:1451	Lewis x and Lewis a antigens	1424:1451	Immunochemical studies indicated that the oligosaccharide chains in the C-tail region of BAL contain Lewis x and Lewis a antigens and, less prominently, sialyl Lewis x and sialyl Lewis a antigens.
7654718	5	62	theme	neuraminic	893:902	arg1	acid					904:907	neuraminic acid	893:907	neuraminic acid	893:907	The O-glycosylated carbohydrates of the C-tail fragment contain fucose, galactose, glucosamine, galactosamine, and neuraminic acid in a molar ratio of 1:3:2:1:0.3, respectively.
7654718	9	63	theme	sialyl	1495:1500	arg1	Lewis					1502:1506	sialyl Lewis	1495:1506	sialyl Lewis	1495:1506	Immunochemical studies indicated that the oligosaccharide chains in the C-tail region of BAL contain Lewis x and Lewis a antigens and, less prominently, sialyl Lewis x and sialyl Lewis a antigens.
7654718	3	64	theme	fragment	596:603	arg1	mg					583:584	20-30 mg	577:584	20-30 mg of C-tail fragment from 1 L of human milk	577:626	Chymotryptic, tryptic, and cyanogen bromide cleavages of partially purified BAL and subsequent molecular sieve chromatography yielded 20-30 mg of C-tail fragment from 1 L of human milk.
7654718	1	65	theme	milk	218:221	arg1	C-tail					201:206	C-tail	201:206	C-tail	201:206	Glycosylation positions and oligosaccharide characteristics in the proline-rich, mucin-like, C-terminal region (C-tail) of human milk bile salt-activated lipase (BAL) were studied in order to assess the possible physiological functions of this region.
7654718	1	65	theme	milk	218:221	arg1	region					193:198	C-terminal region	182:198	C-terminal region (C-tail)	182:207	Glycosylation positions and oligosaccharide characteristics in the proline-rich, mucin-like, C-terminal region (C-tail) of human milk bile salt-activated lipase (BAL) were studied in order to assess the possible physiological functions of this region.
7654718	4	66	theme	C-tail	696:701	arg1	fragment					703:710	the purified C-tail fragment	683:710	the purified C-tail fragment	683:710	The N-terminal sequence and amino acid composition of the purified C-tail fragment establish that it is derived from residues 528-712 of the enzyme.
7654718	0	67	theme	C-tail	72:77	arg1	fragment					79:86	lipase C-tail fragment	65:86	lipase C-tail fragment	65:86	Isolation and characterization of human milk bile salt-activated lipase C-tail fragment.
7654718	5	68	theme	fragment	825:832	arg1	carbohydrates					797:809	The O-glycosylated carbohydrates	778:809	The O-glycosylated carbohydrates of the C-tail fragment	778:832	The O-glycosylated carbohydrates of the C-tail fragment contain fucose, galactose, glucosamine, galactosamine, and neuraminic acid in a molar ratio of 1:3:2:1:0.3, respectively.
7654718	9	69	theme	Lewis	1483:1487	arg1	x					1489:1489	sialyl Lewis x	1476:1489	sialyl Lewis x	1476:1489	Immunochemical studies indicated that the oligosaccharide chains in the C-tail region of BAL contain Lewis x and Lewis a antigens and, less prominently, sialyl Lewis x and sialyl Lewis a antigens.
7654718	11	70	theme	BAL	1710:1712	arg1	function					1698:1705	the physiological function	1680:1705	the physiological function of BAL	1680:1712	These observations suggest the possibility that the C-tail region may contribute to adhesive activity in the physiological function of BAL.
7654718	1	71	theme	region	333:338	arg1	functions					315:323	the possible physiological functions	288:323	the possible physiological functions of this region	288:338	Glycosylation positions and oligosaccharide characteristics in the proline-rich, mucin-like, C-terminal region (C-tail) of human milk bile salt-activated lipase (BAL) were studied in order to assess the possible physiological functions of this region.
7654718	6	72	theme	threonine	1001:1009	arg1	residues					1011:1018	nine threonine residues	996:1018	nine threonine residues	996:1018	beta-Elimination reaction revealed that nine threonine residues and less than one serine residue were glycosylated.
7654718	7	73	theme	consensus	1200:1208	arg1	motif					1210:1214	a consensus motif	1198:1214	a consensus motif of PVPP	1198:1222	Edman degradation of C-tail fragment and its pronase subfragment suggest a number of glycosylation sites which are flanked by a consensus motif of PVPP.
7654718	8	74	theme	BAL	1318:1320	arg1	region					1308:1313	the C-tail region	1297:1313	the C-tail region of BAL	1297:1320	We suggest that this motif may serve as a signal for O-glycosylation in the C-tail region of BAL.
7654718	8	75	from	signal	1267:1272	arg1	region					1308:1313	the C-tail region	1297:1313	the C-tail region of BAL	1297:1320	We suggest that this motif may serve as a signal for O-glycosylation in the C-tail region of BAL.
7654718	11	76	from	activity	1668:1675	arg1	function					1698:1705	the physiological function	1680:1705	the physiological function of BAL	1680:1712	These observations suggest the possibility that the C-tail region may contribute to adhesive activity in the physiological function of BAL.
7654718	1	77	theme	Glycosylation	89:101	arg1	positions					103:111	Glycosylation positions	89:111	Glycosylation positions	89:111	Glycosylation positions and oligosaccharide characteristics in the proline-rich, mucin-like, C-terminal region (C-tail) of human milk bile salt-activated lipase (BAL) were studied in order to assess the possible physiological functions of this region.
7654718	5	78	contain	contain	834:840	arg2	galactosamine					874:886	galactosamine	874:886	galactosamine	874:886	The O-glycosylated carbohydrates of the C-tail fragment contain fucose, galactose, glucosamine, galactosamine, and neuraminic acid in a molar ratio of 1:3:2:1:0.3, respectively.
7654718	5	78	contain	contain	834:840	arg2	galactose					850:858	galactose	850:858	galactose	850:858	The O-glycosylated carbohydrates of the C-tail fragment contain fucose, galactose, glucosamine, galactosamine, and neuraminic acid in a molar ratio of 1:3:2:1:0.3, respectively.
7654718	5	78	contain	contain	834:840	arg2	glucosamine					861:871	glucosamine	861:871	glucosamine	861:871	The O-glycosylated carbohydrates of the C-tail fragment contain fucose, galactose, glucosamine, galactosamine, and neuraminic acid in a molar ratio of 1:3:2:1:0.3, respectively.
7654718	5	78	contain	contain	834:840	arg2	acid					904:907	neuraminic acid	893:907	neuraminic acid	893:907	The O-glycosylated carbohydrates of the C-tail fragment contain fucose, galactose, glucosamine, galactosamine, and neuraminic acid in a molar ratio of 1:3:2:1:0.3, respectively.
7654718	5	78	contain	contain	834:840	arg1	carbohydrates					797:809	The O-glycosylated carbohydrates	778:809	The O-glycosylated carbohydrates of the C-tail fragment	778:832	The O-glycosylated carbohydrates of the C-tail fragment contain fucose, galactose, glucosamine, galactosamine, and neuraminic acid in a molar ratio of 1:3:2:1:0.3, respectively.
7654718	5	78	contain	contain	834:840	arg1	ratio					920:924	a molar ratio	912:924	a molar ratio of 1:3:2:1:0.3, respectively	912:953	The O-glycosylated carbohydrates of the C-tail fragment contain fucose, galactose, glucosamine, galactosamine, and neuraminic acid in a molar ratio of 1:3:2:1:0.3, respectively.
7654718	5	78	contain	contain	834:840	arg2	carbohydrates					797:809	The O-glycosylated carbohydrates	778:809	The O-glycosylated carbohydrates of the C-tail fragment	778:832	The O-glycosylated carbohydrates of the C-tail fragment contain fucose, galactose, glucosamine, galactosamine, and neuraminic acid in a molar ratio of 1:3:2:1:0.3, respectively.
7654718	5	78	contain	contain	834:840	arg2	fucose					842:847	fucose	842:847	fucose	842:847	The O-glycosylated carbohydrates of the C-tail fragment contain fucose, galactose, glucosamine, galactosamine, and neuraminic acid in a molar ratio of 1:3:2:1:0.3, respectively.
7654718	7	79	theme	sites	1171:1175	arg1	number					1147:1152	a number	1145:1152	a number of glycosylation sites which are flanked by a consensus motif of PVPP	1145:1222	Edman degradation of C-tail fragment and its pronase subfragment suggest a number of glycosylation sites which are flanked by a consensus motif of PVPP.
7654718	5	80	theme	1:3:2:1:0.3	929:939	arg1	ratio					920:924	a molar ratio	912:924	a molar ratio of 1:3:2:1:0.3, respectively	912:953	The O-glycosylated carbohydrates of the C-tail fragment contain fucose, galactose, glucosamine, galactosamine, and neuraminic acid in a molar ratio of 1:3:2:1:0.3, respectively.
7654718	2	81	theme	human	427:431	arg1	BAL					438:440	human milk BAL	427:440	human milk BAL	427:440	A large-scale purification method has been devised to purify the C-tail fragment from human milk BAL.
7654718	11	82	theme	adhesive	1659:1666	arg1	activity					1668:1675	adhesive activity	1659:1675	adhesive activity in the physiological function of BAL	1659:1712	These observations suggest the possibility that the C-tail region may contribute to adhesive activity in the physiological function of BAL.
7654718	9	83	dep	x	1489:1489	arg1	antigens					1510:1517	a antigens	1508:1517	a antigens	1508:1517	Immunochemical studies indicated that the oligosaccharide chains in the C-tail region of BAL contain Lewis x and Lewis a antigens and, less prominently, sialyl Lewis x and sialyl Lewis a antigens.
7654718	0	84	theme	milk	40:43	arg1	bile					45:48	human milk bile	34:48	human milk bile	34:48	Isolation and characterization of human milk bile salt-activated lipase C-tail fragment.
7654718	6	85	theme	serine	1038:1043	arg1	residue					1045:1051	less than one serine residue	1024:1051	less than one serine residue	1024:1051	beta-Elimination reaction revealed that nine threonine residues and less than one serine residue were glycosylated.
7654718	3	86	theme	milk	623:626	arg1	L					612:612	1 L	610:612	1 L of human milk	610:626	Chymotryptic, tryptic, and cyanogen bromide cleavages of partially purified BAL and subsequent molecular sieve chromatography yielded 20-30 mg of C-tail fragment from 1 L of human milk.
7654718	1	87	theme	physiological	301:313	arg1	functions					315:323	the possible physiological functions	288:323	the possible physiological functions of this region	288:338	Glycosylation positions and oligosaccharide characteristics in the proline-rich, mucin-like, C-terminal region (C-tail) of human milk bile salt-activated lipase (BAL) were studied in order to assess the possible physiological functions of this region.
7654718	11	88	theme	physiological	1684:1696	arg1	function					1698:1705	the physiological function	1680:1705	the physiological function of BAL	1680:1712	These observations suggest the possibility that the C-tail region may contribute to adhesive activity in the physiological function of BAL.
7654718	9	89	theme	oligosaccharide	1365:1379	arg1	chains					1381:1386	the oligosaccharide chains	1361:1386	the oligosaccharide chains in the C-tail region of BAL	1361:1414	Immunochemical studies indicated that the oligosaccharide chains in the C-tail region of BAL contain Lewis x and Lewis a antigens and, less prominently, sialyl Lewis x and sialyl Lewis a antigens.
7654718	9	90	from	chains	1381:1386	arg1	region					1402:1407	the C-tail region	1391:1407	the C-tail region of BAL	1391:1414	Immunochemical studies indicated that the oligosaccharide chains in the C-tail region of BAL contain Lewis x and Lewis a antigens and, less prominently, sialyl Lewis x and sialyl Lewis a antigens.
7654718	4	91	theme	enzyme	770:775	arg1	enzyme					770:775	the enzyme	766:775	the enzyme	766:775	The N-terminal sequence and amino acid composition of the purified C-tail fragment establish that it is derived from residues 528-712 of the enzyme.
7654718	4	91	theme	enzyme	770:775	arg1	residues					746:753	residues 528-712	746:761	residues 528-712 of the enzyme	746:775	The N-terminal sequence and amino acid composition of the purified C-tail fragment establish that it is derived from residues 528-712 of the enzyme.
7654718	3	92	theme	cyanogen	470:477	arg1	bromide					479:485	bromide	479:485	bromide	479:485	Chymotryptic, tryptic, and cyanogen bromide cleavages of partially purified BAL and subsequent molecular sieve chromatography yielded 20-30 mg of C-tail fragment from 1 L of human milk.
7654718	3	93	theme	BAL	519:521	arg1	cleavages					487:495	Chymotryptic, tryptic, and cyanogen bromide cleavages	443:495	Chymotryptic, tryptic, and cyanogen bromide cleavages of partially purified BAL and subsequent molecular sieve chromatography	443:567	Chymotryptic, tryptic, and cyanogen bromide cleavages of partially purified BAL and subsequent molecular sieve chromatography yielded 20-30 mg of C-tail fragment from 1 L of human milk.
7654718	9	94	theme	C-tail	1395:1400	arg1	region					1402:1407	the C-tail region	1391:1407	the C-tail region of BAL	1391:1414	Immunochemical studies indicated that the oligosaccharide chains in the C-tail region of BAL contain Lewis x and Lewis a antigens and, less prominently, sialyl Lewis x and sialyl Lewis a antigens.
2842863	2	0	theme	70-kilodalton	429:441	arg1	precursor					443:451	the 70-kilodalton precursor	425:451	the 70-kilodalton precursor of SAP-1 (SAP precursor cDNA)	425:481	The nucleotide sequence of the largest cDNA was colinear with the derived amino acid sequence of SAP-2 and with the nucleotide sequence of the cDNA coding for the 70-kilodalton precursor of SAP-1 (SAP precursor cDNA).
2842863	8	1	theme	Protein	1224:1230	arg1	experiments					1247:1257	Protein immunoblotting experiments	1224:1257	Protein immunoblotting experiments	1224:1257	Protein immunoblotting experiments indicated that SAP precursor protein (70 kilodaltons) as well as immunoreactive SAP-like proteins of intermediate sizes (65, 50, and 31 kilodaltons) are present in most human tissues.
2842863	6	2	theme	glycosylation	966:978	arg1	sites					980:984	potential glycosylation sites	956:984	potential glycosylation sites	956:984	Each of the four domains was approximately 80 amino acid residues long, had nearly identical placement of cysteine residues, potential glycosylation sites, and proline residues.
2842863	1	3	theme	human	208:212	arg1	library					223:229	a lambda gt-11 human hepatoma library	193:229	a lambda gt-11 human hepatoma library	193:229	Several complementary DNAs (cDNAs) coding for sphingolipid activator protein-2 (SAP-2) were isolated from a lambda gt-11 human hepatoma library by means of polyclonal antibodies.
2842863	3	4	theme	SAP	568:570	arg1	cDNA					582:585	the SAP precursor cDNA	564:585	the SAP precursor cDNA	564:585	The coding sequence for mature SAP-2 was located 3' to that coding for SAP-1 in the SAP precursor cDNA.
2842863	6	5	theme	residues	999:1006	arg1	placement					924:932	nearly identical placement	907:932	nearly identical placement of cysteine residues, potential glycosylation sites, and proline residues	907:1006	Each of the four domains was approximately 80 amino acid residues long, had nearly identical placement of cysteine residues, potential glycosylation sites, and proline residues.
2842863	1	6	theme	hepatoma	214:221	arg1	library					223:229	a lambda gt-11 human hepatoma library	193:229	a lambda gt-11 human hepatoma library	193:229	Several complementary DNAs (cDNAs) coding for sphingolipid activator protein-2 (SAP-2) were isolated from a lambda gt-11 human hepatoma library by means of polyclonal antibodies.
2842863	0	7	theme	genetic	72:78	arg1	locus					80:84	same genetic locus	67:84	same genetic locus	67:84	Coding of two sphingolipid activator proteins (SAP-1 and SAP-2) by same genetic locus.
2842863	4	8	theme	human	718:722	arg1	chromosome					724:733	human chromosome 10	718:736	human chromosome 10	718:736	Both SAP-1 and SAP-2 appeared to be derived by proteolytic processing from a common precursor that is coded by a genetic locus on human chromosome 10.
2842863	4	9	theme	common	665:670	arg1	precursor					672:680	a common precursor	663:680	a common precursor that is coded by a genetic locus on human chromosome 10	663:736	Both SAP-1 and SAP-2 appeared to be derived by proteolytic processing from a common precursor that is coded by a genetic locus on human chromosome 10.
2842863	2	10	theme	SAP	463:465	arg1	cDNA					477:480	SAP precursor cDNA	463:480	SAP precursor cDNA	463:480	The nucleotide sequence of the largest cDNA was colinear with the derived amino acid sequence of SAP-2 and with the nucleotide sequence of the cDNA coding for the 70-kilodalton precursor of SAP-1 (SAP precursor cDNA).
2842863	2	10	theme	SAP	463:465	arg1	SAP-1					456:460	SAP-1	456:460	SAP-1 (SAP precursor cDNA)	456:481	The nucleotide sequence of the largest cDNA was colinear with the derived amino acid sequence of SAP-2 and with the nucleotide sequence of the cDNA coding for the 70-kilodalton precursor of SAP-1 (SAP precursor cDNA).
2842863	6	11	dep	residues	888:895	arg1	had					903:905	had	903:905	had nearly identical placement of cysteine residues, potential glycosylation sites, and proline residues	903:1006	Each of the four domains was approximately 80 amino acid residues long, had nearly identical placement of cysteine residues, potential glycosylation sites, and proline residues.
2842863	6	12	gly	glycosylation	966:978	arg2	sites					980:984	potential glycosylation sites	956:984	potential glycosylation sites	956:984	Each of the four domains was approximately 80 amino acid residues long, had nearly identical placement of cysteine residues, potential glycosylation sites, and proline residues.
2842863	4	13	from	precursor	672:680	arg1	processing					647:656	proteolytic processing	635:656	proteolytic processing from a common precursor that is coded by a genetic locus on human chromosome 10	635:736	Both SAP-1 and SAP-2 appeared to be derived by proteolytic processing from a common precursor that is coded by a genetic locus on human chromosome 10.
2842863	8	14	located	present	1412:1418	arg1	tissues					1434:1440	most human tissues	1423:1440	most human tissues	1423:1440	Protein immunoblotting experiments indicated that SAP precursor protein (70 kilodaltons) as well as immunoreactive SAP-like proteins of intermediate sizes (65, 50, and 31 kilodaltons) are present in most human tissues.
2842863	8	14	located	present	1412:1418	arg2	proteins					1348:1355	immunoreactive SAP-like proteins	1324:1355	SAP precursor protein (70 kilodaltons) as well as immunoreactive SAP-like proteins of intermediate sizes (65, 50, and 31 kilodaltons)	1274:1406	Protein immunoblotting experiments indicated that SAP precursor protein (70 kilodaltons) as well as immunoreactive SAP-like proteins of intermediate sizes (65, 50, and 31 kilodaltons) are present in most human tissues.
2842863	8	14	located	present	1412:1418	arg2	protein					1288:1294	SAP precursor protein	1274:1294	SAP precursor protein (70 kilodaltons) as well as immunoreactive SAP-like proteins of intermediate sizes (65, 50, and 31 kilodaltons)	1274:1406	Protein immunoblotting experiments indicated that SAP precursor protein (70 kilodaltons) as well as immunoreactive SAP-like proteins of intermediate sizes (65, 50, and 31 kilodaltons) are present in most human tissues.
2842863	8	14	located	present	1412:1418	arg2	kilodaltons					1300:1310	70 kilodaltons	1297:1310	70 kilodaltons	1297:1310	Protein immunoblotting experiments indicated that SAP precursor protein (70 kilodaltons) as well as immunoreactive SAP-like proteins of intermediate sizes (65, 50, and 31 kilodaltons) are present in most human tissues.
2842863	5	15	theme	other	743:747	arg1	domains					749:755	Two other domains	739:755	Two other domains similar to SAP-1 and SAP-2	739:782	Two other domains similar to SAP-1 and SAP-2 were also identified in SAP precursor protein.
2842863	7	16	contain	contained	1026:1034	arg2	sequences					1056:1064	internal amino acid sequences	1036:1064	internal amino acid sequences capable of forming amphipathic helices separated by helix breakers to give a cylindrical hydrophobic domain that is probably stabilized by disulfide bridges	1036:1221	Each domain also contained internal amino acid sequences capable of forming amphipathic helices separated by helix breakers to give a cylindrical hydrophobic domain that is probably stabilized by disulfide bridges.
2842863	7	16	contain	contained	1026:1034	arg1	domain					1014:1019	Each domain	1009:1019	Each domain	1009:1019	Each domain also contained internal amino acid sequences capable of forming amphipathic helices separated by helix breakers to give a cylindrical hydrophobic domain that is probably stabilized by disulfide bridges.
2842863	2	17	theme	cDNA	305:308	arg1	colinear					314:321	colinear	314:321	colinear	314:321	The nucleotide sequence of the largest cDNA was colinear with the derived amino acid sequence of SAP-2 and with the nucleotide sequence of the cDNA coding for the 70-kilodalton precursor of SAP-1 (SAP precursor cDNA).
2842863	2	17	theme	cDNA	305:308	arg1	sequence					281:288	The nucleotide sequence	266:288	The nucleotide sequence of the largest cDNA	266:308	The nucleotide sequence of the largest cDNA was colinear with the derived amino acid sequence of SAP-2 and with the nucleotide sequence of the cDNA coding for the 70-kilodalton precursor of SAP-1 (SAP precursor cDNA).
2842863	7	18	theme	amino	1045:1049	arg1	sequences					1056:1064	internal amino acid sequences	1036:1064	internal amino acid sequences capable of forming amphipathic helices separated by helix breakers to give a cylindrical hydrophobic domain that is probably stabilized by disulfide bridges	1036:1221	Each domain also contained internal amino acid sequences capable of forming amphipathic helices separated by helix breakers to give a cylindrical hydrophobic domain that is probably stabilized by disulfide bridges.
2842863	8	19	theme	immunoblotting	1232:1245	arg1	experiments					1247:1257	Protein immunoblotting experiments	1224:1257	Protein immunoblotting experiments	1224:1257	Protein immunoblotting experiments indicated that SAP precursor protein (70 kilodaltons) as well as immunoreactive SAP-like proteins of intermediate sizes (65, 50, and 31 kilodaltons) are present in most human tissues.
2842863	5	20	theme	similar	757:763	arg1	domains					749:755	Two other domains	739:755	Two other domains similar to SAP-1 and SAP-2	739:782	Two other domains similar to SAP-1 and SAP-2 were also identified in SAP precursor protein.
2842863	1	21	theme	sphingolipid	133:144	arg1	protein-2					156:164	sphingolipid activator protein-2	133:164	sphingolipid activator protein-2 (SAP-2)	133:172	Several complementary DNAs (cDNAs) coding for sphingolipid activator protein-2 (SAP-2) were isolated from a lambda gt-11 human hepatoma library by means of polyclonal antibodies.
2842863	1	21	theme	sphingolipid	133:144	arg1	SAP-2					167:171	SAP-2	167:171	SAP-2	167:171	Several complementary DNAs (cDNAs) coding for sphingolipid activator protein-2 (SAP-2) were isolated from a lambda gt-11 human hepatoma library by means of polyclonal antibodies.
2842863	2	22	theme	SAP-1	456:460	arg1	precursor					443:451	the 70-kilodalton precursor	425:451	the 70-kilodalton precursor of SAP-1 (SAP precursor cDNA)	425:481	The nucleotide sequence of the largest cDNA was colinear with the derived amino acid sequence of SAP-2 and with the nucleotide sequence of the cDNA coding for the 70-kilodalton precursor of SAP-1 (SAP precursor cDNA).
2842863	6	23	theme	amino	877:881	arg1	residues					888:895	approximately 80 amino acid residues	860:895	approximately 80 amino acid residues	860:895	Each of the four domains was approximately 80 amino acid residues long, had nearly identical placement of cysteine residues, potential glycosylation sites, and proline residues.
2842863	5	24	theme	precursor	812:820	arg1	protein					822:828	SAP precursor protein	808:828	SAP precursor protein	808:828	Two other domains similar to SAP-1 and SAP-2 were also identified in SAP precursor protein.
2842863	2	25	theme	acid	346:349	arg1	sequence					351:358	the derived amino acid sequence	328:358	the derived amino acid sequence of SAP-2	328:367	The nucleotide sequence of the largest cDNA was colinear with the derived amino acid sequence of SAP-2 and with the nucleotide sequence of the cDNA coding for the 70-kilodalton precursor of SAP-1 (SAP precursor cDNA).
2842863	7	26	theme	acid	1051:1054	arg1	sequences					1056:1064	internal amino acid sequences	1036:1064	internal amino acid sequences capable of forming amphipathic helices separated by helix breakers to give a cylindrical hydrophobic domain that is probably stabilized by disulfide bridges	1036:1221	Each domain also contained internal amino acid sequences capable of forming amphipathic helices separated by helix breakers to give a cylindrical hydrophobic domain that is probably stabilized by disulfide bridges.
2842863	4	27	theme	proteolytic	635:645	arg1	processing					647:656	proteolytic processing	635:656	proteolytic processing from a common precursor that is coded by a genetic locus on human chromosome 10	635:736	Both SAP-1 and SAP-2 appeared to be derived by proteolytic processing from a common precursor that is coded by a genetic locus on human chromosome 10.
2842863	7	28	theme	hydrophobic	1155:1165	arg1	domain					1167:1172	a cylindrical hydrophobic domain	1141:1172	a cylindrical hydrophobic domain that is probably stabilized by disulfide bridges	1141:1221	Each domain also contained internal amino acid sequences capable of forming amphipathic helices separated by helix breakers to give a cylindrical hydrophobic domain that is probably stabilized by disulfide bridges.
2842863	2	29	theme	amino	340:344	arg1	sequence					351:358	the derived amino acid sequence	328:358	the derived amino acid sequence of SAP-2	328:367	The nucleotide sequence of the largest cDNA was colinear with the derived amino acid sequence of SAP-2 and with the nucleotide sequence of the cDNA coding for the 70-kilodalton precursor of SAP-1 (SAP precursor cDNA).
2842863	8	30	theme	human	1428:1432	arg1	tissues					1434:1440	most human tissues	1423:1440	most human tissues	1423:1440	Protein immunoblotting experiments indicated that SAP precursor protein (70 kilodaltons) as well as immunoreactive SAP-like proteins of intermediate sizes (65, 50, and 31 kilodaltons) are present in most human tissues.
2842863	2	31	theme	nucleotide	270:279	arg1	colinear					314:321	colinear	314:321	colinear	314:321	The nucleotide sequence of the largest cDNA was colinear with the derived amino acid sequence of SAP-2 and with the nucleotide sequence of the cDNA coding for the 70-kilodalton precursor of SAP-1 (SAP precursor cDNA).
2842863	2	31	theme	nucleotide	270:279	arg1	sequence					281:288	The nucleotide sequence	266:288	The nucleotide sequence of the largest cDNA	266:308	The nucleotide sequence of the largest cDNA was colinear with the derived amino acid sequence of SAP-2 and with the nucleotide sequence of the cDNA coding for the 70-kilodalton precursor of SAP-1 (SAP precursor cDNA).
2842863	2	32	theme	derived	332:338	arg1	sequence					351:358	the derived amino acid sequence	328:358	the derived amino acid sequence of SAP-2	328:367	The nucleotide sequence of the largest cDNA was colinear with the derived amino acid sequence of SAP-2 and with the nucleotide sequence of the cDNA coding for the 70-kilodalton precursor of SAP-1 (SAP precursor cDNA).
2842863	0	33	theme	sphingolipid	14:25	arg1	proteins					37:44	two sphingolipid activator proteins	10:44	two sphingolipid activator proteins (SAP-1 and SAP-2)	10:62	Coding of two sphingolipid activator proteins (SAP-1 and SAP-2) by same genetic locus.
2842863	0	33	theme	sphingolipid	14:25	arg1	SAP-2					57:61	SAP-2	57:61	SAP-2	57:61	Coding of two sphingolipid activator proteins (SAP-1 and SAP-2) by same genetic locus.
2842863	0	33	theme	sphingolipid	14:25	arg1	SAP-1					47:51	SAP-1	47:51	SAP-1	47:51	Coding of two sphingolipid activator proteins (SAP-1 and SAP-2) by same genetic locus.
2842863	6	34	theme	residues	946:953	arg1	placement					924:932	nearly identical placement	907:932	nearly identical placement of cysteine residues, potential glycosylation sites, and proline residues	907:1006	Each of the four domains was approximately 80 amino acid residues long, had nearly identical placement of cysteine residues, potential glycosylation sites, and proline residues.
2842863	8	35	theme	intermediate	1360:1371	arg1	kilodaltons					1395:1405	65, 50, and 31 kilodaltons	1380:1405	65, 50, and 31 kilodaltons	1380:1405	Protein immunoblotting experiments indicated that SAP precursor protein (70 kilodaltons) as well as immunoreactive SAP-like proteins of intermediate sizes (65, 50, and 31 kilodaltons) are present in most human tissues.
2842863	8	35	theme	intermediate	1360:1371	arg1	sizes					1373:1377	intermediate sizes	1360:1377	intermediate sizes (65, 50, and 31 kilodaltons)	1360:1406	Protein immunoblotting experiments indicated that SAP precursor protein (70 kilodaltons) as well as immunoreactive SAP-like proteins of intermediate sizes (65, 50, and 31 kilodaltons) are present in most human tissues.
2842863	3	36	theme	coding	488:493	arg1	sequence					495:502	The coding sequence	484:502	The coding sequence for mature SAP-2	484:519	The coding sequence for mature SAP-2 was located 3' to that coding for SAP-1 in the SAP precursor cDNA.
2842863	3	37	theme	mature	508:513	arg1	SAP-2					515:519	mature SAP-2	508:519	mature SAP-2	508:519	The coding sequence for mature SAP-2 was located 3' to that coding for SAP-1 in the SAP precursor cDNA.
2842863	1	38	theme	polyclonal	243:252	arg1	antibodies					254:263	polyclonal antibodies	243:263	polyclonal antibodies	243:263	Several complementary DNAs (cDNAs) coding for sphingolipid activator protein-2 (SAP-2) were isolated from a lambda gt-11 human hepatoma library by means of polyclonal antibodies.
2842863	6	39	theme	acid	883:886	arg1	residues					888:895	approximately 80 amino acid residues	860:895	approximately 80 amino acid residues	860:895	Each of the four domains was approximately 80 amino acid residues long, had nearly identical placement of cysteine residues, potential glycosylation sites, and proline residues.
2842863	6	40	theme	potential	956:964	arg1	sites					980:984	potential glycosylation sites	956:984	potential glycosylation sites	956:984	Each of the four domains was approximately 80 amino acid residues long, had nearly identical placement of cysteine residues, potential glycosylation sites, and proline residues.
2842863	8	41	attach	present	1412:1418	arg1	tissues					1434:1440	most human tissues	1423:1440	most human tissues	1423:1440	Protein immunoblotting experiments indicated that SAP precursor protein (70 kilodaltons) as well as immunoreactive SAP-like proteins of intermediate sizes (65, 50, and 31 kilodaltons) are present in most human tissues.
2842863	8	41	attach	present	1412:1418	arg2	proteins					1348:1355	immunoreactive SAP-like proteins	1324:1355	SAP precursor protein (70 kilodaltons) as well as immunoreactive SAP-like proteins of intermediate sizes (65, 50, and 31 kilodaltons)	1274:1406	Protein immunoblotting experiments indicated that SAP precursor protein (70 kilodaltons) as well as immunoreactive SAP-like proteins of intermediate sizes (65, 50, and 31 kilodaltons) are present in most human tissues.
2842863	8	41	attach	present	1412:1418	arg2	protein					1288:1294	SAP precursor protein	1274:1294	SAP precursor protein (70 kilodaltons) as well as immunoreactive SAP-like proteins of intermediate sizes (65, 50, and 31 kilodaltons)	1274:1406	Protein immunoblotting experiments indicated that SAP precursor protein (70 kilodaltons) as well as immunoreactive SAP-like proteins of intermediate sizes (65, 50, and 31 kilodaltons) are present in most human tissues.
2842863	8	41	attach	present	1412:1418	arg2	kilodaltons					1300:1310	70 kilodaltons	1297:1310	70 kilodaltons	1297:1310	Protein immunoblotting experiments indicated that SAP precursor protein (70 kilodaltons) as well as immunoreactive SAP-like proteins of intermediate sizes (65, 50, and 31 kilodaltons) are present in most human tissues.
2842863	6	42	theme	identical	914:922	arg1	placement					924:932	nearly identical placement	907:932	nearly identical placement of cysteine residues, potential glycosylation sites, and proline residues	907:1006	Each of the four domains was approximately 80 amino acid residues long, had nearly identical placement of cysteine residues, potential glycosylation sites, and proline residues.
2842863	0	43	theme	proteins	37:44	arg1	Coding					0:5	Coding	0:5	Coding of two sphingolipid activator proteins (SAP-1 and SAP-2) by same genetic locus	0:84	Coding of two sphingolipid activator proteins (SAP-1 and SAP-2) by same genetic locus.
2842863	2	44	theme	largest	297:303	arg1	cDNA					305:308	the largest cDNA	293:308	the largest cDNA	293:308	The nucleotide sequence of the largest cDNA was colinear with the derived amino acid sequence of SAP-2 and with the nucleotide sequence of the cDNA coding for the 70-kilodalton precursor of SAP-1 (SAP precursor cDNA).
2842863	2	45	link	derived	332:338	arg1	sequence					351:358	the derived amino acid sequence	328:358	the derived amino acid sequence of SAP-2	328:367	The nucleotide sequence of the largest cDNA was colinear with the derived amino acid sequence of SAP-2 and with the nucleotide sequence of the cDNA coding for the 70-kilodalton precursor of SAP-1 (SAP precursor cDNA).
2842863	2	46	theme	SAP-2	363:367	arg1	sequence					351:358	the derived amino acid sequence	328:358	the derived amino acid sequence of SAP-2	328:367	The nucleotide sequence of the largest cDNA was colinear with the derived amino acid sequence of SAP-2 and with the nucleotide sequence of the cDNA coding for the 70-kilodalton precursor of SAP-1 (SAP precursor cDNA).
2842863	0	47	theme	activator	27:35	arg1	proteins					37:44	two sphingolipid activator proteins	10:44	two sphingolipid activator proteins (SAP-1 and SAP-2)	10:62	Coding of two sphingolipid activator proteins (SAP-1 and SAP-2) by same genetic locus.
2842863	0	47	theme	activator	27:35	arg1	SAP-2					57:61	SAP-2	57:61	SAP-2	57:61	Coding of two sphingolipid activator proteins (SAP-1 and SAP-2) by same genetic locus.
2842863	0	47	theme	activator	27:35	arg1	SAP-1					47:51	SAP-1	47:51	SAP-1	47:51	Coding of two sphingolipid activator proteins (SAP-1 and SAP-2) by same genetic locus.
2842863	8	48	from	present	1412:1418	arg1	tissues					1434:1440	most human tissues	1423:1440	most human tissues	1423:1440	Protein immunoblotting experiments indicated that SAP precursor protein (70 kilodaltons) as well as immunoreactive SAP-like proteins of intermediate sizes (65, 50, and 31 kilodaltons) are present in most human tissues.
2842863	8	49	theme	sizes	1373:1377	arg1	proteins					1348:1355	immunoreactive SAP-like proteins	1324:1355	SAP precursor protein (70 kilodaltons) as well as immunoreactive SAP-like proteins of intermediate sizes (65, 50, and 31 kilodaltons)	1274:1406	Protein immunoblotting experiments indicated that SAP precursor protein (70 kilodaltons) as well as immunoreactive SAP-like proteins of intermediate sizes (65, 50, and 31 kilodaltons) are present in most human tissues.
2842863	8	49	theme	sizes	1373:1377	arg1	protein					1288:1294	SAP precursor protein	1274:1294	SAP precursor protein (70 kilodaltons) as well as immunoreactive SAP-like proteins of intermediate sizes (65, 50, and 31 kilodaltons)	1274:1406	Protein immunoblotting experiments indicated that SAP precursor protein (70 kilodaltons) as well as immunoreactive SAP-like proteins of intermediate sizes (65, 50, and 31 kilodaltons) are present in most human tissues.
2842863	8	49	theme	sizes	1373:1377	arg1	kilodaltons					1300:1310	70 kilodaltons	1297:1310	70 kilodaltons	1297:1310	Protein immunoblotting experiments indicated that SAP precursor protein (70 kilodaltons) as well as immunoreactive SAP-like proteins of intermediate sizes (65, 50, and 31 kilodaltons) are present in most human tissues.
2842863	2	50	theme	nucleotide	382:391	arg1	sequence					393:400	the nucleotide sequence	378:400	the nucleotide sequence of the cDNA coding for the 70-kilodalton precursor of SAP-1 (SAP precursor cDNA)	378:481	The nucleotide sequence of the largest cDNA was colinear with the derived amino acid sequence of SAP-2 and with the nucleotide sequence of the cDNA coding for the 70-kilodalton precursor of SAP-1 (SAP precursor cDNA).
2842863	6	51	theme	cysteine	937:944	arg1	residues					946:953	cysteine residues	937:953	cysteine residues	937:953	Each of the four domains was approximately 80 amino acid residues long, had nearly identical placement of cysteine residues, potential glycosylation sites, and proline residues.
2842863	2	52	theme	cDNA	409:412	arg1	sequence					393:400	the nucleotide sequence	378:400	the nucleotide sequence of the cDNA coding for the 70-kilodalton precursor of SAP-1 (SAP precursor cDNA)	378:481	The nucleotide sequence of the largest cDNA was colinear with the derived amino acid sequence of SAP-2 and with the nucleotide sequence of the cDNA coding for the 70-kilodalton precursor of SAP-1 (SAP precursor cDNA).
2842863	2	53	theme	precursor	467:475	arg1	cDNA					477:480	SAP precursor cDNA	463:480	SAP precursor cDNA	463:480	The nucleotide sequence of the largest cDNA was colinear with the derived amino acid sequence of SAP-2 and with the nucleotide sequence of the cDNA coding for the 70-kilodalton precursor of SAP-1 (SAP precursor cDNA).
2842863	2	53	theme	precursor	467:475	arg1	SAP-1					456:460	SAP-1	456:460	SAP-1 (SAP precursor cDNA)	456:481	The nucleotide sequence of the largest cDNA was colinear with the derived amino acid sequence of SAP-2 and with the nucleotide sequence of the cDNA coding for the 70-kilodalton precursor of SAP-1 (SAP precursor cDNA).
2842863	8	54	theme	precursor	1278:1286	arg1	protein					1288:1294	SAP precursor protein	1274:1294	SAP precursor protein (70 kilodaltons) as well as immunoreactive SAP-like proteins of intermediate sizes (65, 50, and 31 kilodaltons)	1274:1406	Protein immunoblotting experiments indicated that SAP precursor protein (70 kilodaltons) as well as immunoreactive SAP-like proteins of intermediate sizes (65, 50, and 31 kilodaltons) are present in most human tissues.
2842863	8	54	theme	precursor	1278:1286	arg1	kilodaltons					1300:1310	70 kilodaltons	1297:1310	70 kilodaltons	1297:1310	Protein immunoblotting experiments indicated that SAP precursor protein (70 kilodaltons) as well as immunoreactive SAP-like proteins of intermediate sizes (65, 50, and 31 kilodaltons) are present in most human tissues.
2842863	7	55	theme	amphipathic	1085:1095	arg1	helices					1097:1103	amphipathic helices	1085:1103	amphipathic helices separated by helix breakers	1085:1131	Each domain also contained internal amino acid sequences capable of forming amphipathic helices separated by helix breakers to give a cylindrical hydrophobic domain that is probably stabilized by disulfide bridges.
2842863	0	56	dep	proteins	37:44	arg1	proteins					37:44	two sphingolipid activator proteins	10:44	two sphingolipid activator proteins (SAP-1 and SAP-2)	10:62	Coding of two sphingolipid activator proteins (SAP-1 and SAP-2) by same genetic locus.
2842863	0	56	dep	proteins	37:44	arg1	SAP-2					57:61	SAP-2	57:61	SAP-2	57:61	Coding of two sphingolipid activator proteins (SAP-1 and SAP-2) by same genetic locus.
2842863	0	56	dep	proteins	37:44	arg1	SAP-1					47:51	SAP-1	47:51	SAP-1	47:51	Coding of two sphingolipid activator proteins (SAP-1 and SAP-2) by same genetic locus.
2842863	8	57	theme	SAP	1274:1276	arg1	protein					1288:1294	SAP precursor protein	1274:1294	SAP precursor protein (70 kilodaltons) as well as immunoreactive SAP-like proteins of intermediate sizes (65, 50, and 31 kilodaltons)	1274:1406	Protein immunoblotting experiments indicated that SAP precursor protein (70 kilodaltons) as well as immunoreactive SAP-like proteins of intermediate sizes (65, 50, and 31 kilodaltons) are present in most human tissues.
2842863	8	57	theme	SAP	1274:1276	arg1	kilodaltons					1300:1310	70 kilodaltons	1297:1310	70 kilodaltons	1297:1310	Protein immunoblotting experiments indicated that SAP precursor protein (70 kilodaltons) as well as immunoreactive SAP-like proteins of intermediate sizes (65, 50, and 31 kilodaltons) are present in most human tissues.
2842863	1	58	theme	Several	87:93	arg1	DNAs					109:112	Several complementary DNAs	87:112	Several complementary DNAs (cDNAs) coding for sphingolipid activator protein-2 (SAP-2)	87:172	Several complementary DNAs (cDNAs) coding for sphingolipid activator protein-2 (SAP-2) were isolated from a lambda gt-11 human hepatoma library by means of polyclonal antibodies.
2842863	1	58	theme	Several	87:93	arg1	cDNAs					115:119	cDNAs	115:119	cDNAs	115:119	Several complementary DNAs (cDNAs) coding for sphingolipid activator protein-2 (SAP-2) were isolated from a lambda gt-11 human hepatoma library by means of polyclonal antibodies.
2842863	2	59	with	colinear	314:321	arg1	sequence					393:400	the nucleotide sequence	378:400	the nucleotide sequence of the cDNA coding for the 70-kilodalton precursor of SAP-1 (SAP precursor cDNA)	378:481	The nucleotide sequence of the largest cDNA was colinear with the derived amino acid sequence of SAP-2 and with the nucleotide sequence of the cDNA coding for the 70-kilodalton precursor of SAP-1 (SAP precursor cDNA).
2842863	2	59	with	colinear	314:321	arg1	sequence					351:358	the derived amino acid sequence	328:358	the derived amino acid sequence of SAP-2	328:367	The nucleotide sequence of the largest cDNA was colinear with the derived amino acid sequence of SAP-2 and with the nucleotide sequence of the cDNA coding for the 70-kilodalton precursor of SAP-1 (SAP precursor cDNA).
2842863	8	60	theme	immunoreactive	1324:1337	arg1	proteins					1348:1355	immunoreactive SAP-like proteins	1324:1355	SAP precursor protein (70 kilodaltons) as well as immunoreactive SAP-like proteins of intermediate sizes (65, 50, and 31 kilodaltons)	1274:1406	Protein immunoblotting experiments indicated that SAP precursor protein (70 kilodaltons) as well as immunoreactive SAP-like proteins of intermediate sizes (65, 50, and 31 kilodaltons) are present in most human tissues.
2842863	4	61	from	locus	709:713	arg1	chromosome					724:733	human chromosome 10	718:736	human chromosome 10	718:736	Both SAP-1 and SAP-2 appeared to be derived by proteolytic processing from a common precursor that is coded by a genetic locus on human chromosome 10.
2842863	1	62	theme	complementary	95:107	arg1	DNAs					109:112	Several complementary DNAs	87:112	Several complementary DNAs (cDNAs) coding for sphingolipid activator protein-2 (SAP-2)	87:172	Several complementary DNAs (cDNAs) coding for sphingolipid activator protein-2 (SAP-2) were isolated from a lambda gt-11 human hepatoma library by means of polyclonal antibodies.
2842863	1	62	theme	complementary	95:107	arg1	cDNAs					115:119	cDNAs	115:119	cDNAs	115:119	Several complementary DNAs (cDNAs) coding for sphingolipid activator protein-2 (SAP-2) were isolated from a lambda gt-11 human hepatoma library by means of polyclonal antibodies.
2842863	7	63	theme	internal	1036:1043	arg1	sequences					1056:1064	internal amino acid sequences	1036:1064	internal amino acid sequences capable of forming amphipathic helices separated by helix breakers to give a cylindrical hydrophobic domain that is probably stabilized by disulfide bridges	1036:1221	Each domain also contained internal amino acid sequences capable of forming amphipathic helices separated by helix breakers to give a cylindrical hydrophobic domain that is probably stabilized by disulfide bridges.
2842863	8	64	from	tissues	1434:1440	arg1	present					1412:1418	present	1412:1418	present	1412:1418	Protein immunoblotting experiments indicated that SAP precursor protein (70 kilodaltons) as well as immunoreactive SAP-like proteins of intermediate sizes (65, 50, and 31 kilodaltons) are present in most human tissues.
2842863	4	65	theme	genetic	701:707	arg1	locus					709:713	a genetic locus	699:713	a genetic locus on human chromosome 10	699:736	Both SAP-1 and SAP-2 appeared to be derived by proteolytic processing from a common precursor that is coded by a genetic locus on human chromosome 10.
2842863	6	66	theme	proline	991:997	arg1	residues					999:1006	proline residues	991:1006	proline residues	991:1006	Each of the four domains was approximately 80 amino acid residues long, had nearly identical placement of cysteine residues, potential glycosylation sites, and proline residues.
2842863	1	67	attach	isolated	179:186	arg1	library					223:229	a lambda gt-11 human hepatoma library	193:229	a lambda gt-11 human hepatoma library	193:229	Several complementary DNAs (cDNAs) coding for sphingolipid activator protein-2 (SAP-2) were isolated from a lambda gt-11 human hepatoma library by means of polyclonal antibodies.
2842863	1	67	attach	isolated	179:186	arg2	cDNAs					115:119	cDNAs	115:119	cDNAs	115:119	Several complementary DNAs (cDNAs) coding for sphingolipid activator protein-2 (SAP-2) were isolated from a lambda gt-11 human hepatoma library by means of polyclonal antibodies.
2842863	1	67	attach	isolated	179:186	arg2	DNAs					109:112	Several complementary DNAs	87:112	Several complementary DNAs (cDNAs) coding for sphingolipid activator protein-2 (SAP-2)	87:172	Several complementary DNAs (cDNAs) coding for sphingolipid activator protein-2 (SAP-2) were isolated from a lambda gt-11 human hepatoma library by means of polyclonal antibodies.
2842863	5	68	theme	SAP	808:810	arg1	protein					822:828	SAP precursor protein	808:828	SAP precursor protein	808:828	Two other domains similar to SAP-1 and SAP-2 were also identified in SAP precursor protein.
2842863	7	69	theme	disulfide	1205:1213	arg1	bridges					1215:1221	disulfide bridges	1205:1221	disulfide bridges	1205:1221	Each domain also contained internal amino acid sequences capable of forming amphipathic helices separated by helix breakers to give a cylindrical hydrophobic domain that is probably stabilized by disulfide bridges.
2842863	7	70	theme	cylindrical	1143:1153	arg1	domain					1167:1172	a cylindrical hydrophobic domain	1141:1172	a cylindrical hydrophobic domain that is probably stabilized by disulfide bridges	1141:1221	Each domain also contained internal amino acid sequences capable of forming amphipathic helices separated by helix breakers to give a cylindrical hydrophobic domain that is probably stabilized by disulfide bridges.
2842863	3	71	theme	precursor	572:580	arg1	cDNA					582:585	the SAP precursor cDNA	564:585	the SAP precursor cDNA	564:585	The coding sequence for mature SAP-2 was located 3' to that coding for SAP-1 in the SAP precursor cDNA.
2842863	8	72	theme	SAP-like	1339:1346	arg1	proteins					1348:1355	immunoreactive SAP-like proteins	1324:1355	SAP precursor protein (70 kilodaltons) as well as immunoreactive SAP-like proteins of intermediate sizes (65, 50, and 31 kilodaltons)	1274:1406	Protein immunoblotting experiments indicated that SAP precursor protein (70 kilodaltons) as well as immunoreactive SAP-like proteins of intermediate sizes (65, 50, and 31 kilodaltons) are present in most human tissues.
2842863	8	73	theme	most	1423:1426	arg1	tissues					1434:1440	most human tissues	1423:1440	most human tissues	1423:1440	Protein immunoblotting experiments indicated that SAP precursor protein (70 kilodaltons) as well as immunoreactive SAP-like proteins of intermediate sizes (65, 50, and 31 kilodaltons) are present in most human tissues.
2842863	1	74	theme	activator	146:154	arg1	protein-2					156:164	sphingolipid activator protein-2	133:164	sphingolipid activator protein-2 (SAP-2)	133:172	Several complementary DNAs (cDNAs) coding for sphingolipid activator protein-2 (SAP-2) were isolated from a lambda gt-11 human hepatoma library by means of polyclonal antibodies.
2842863	1	74	theme	activator	146:154	arg1	SAP-2					167:171	SAP-2	167:171	SAP-2	167:171	Several complementary DNAs (cDNAs) coding for sphingolipid activator protein-2 (SAP-2) were isolated from a lambda gt-11 human hepatoma library by means of polyclonal antibodies.
2842863	1	75	theme	lambda	195:200	arg1	library					223:229	a lambda gt-11 human hepatoma library	193:229	a lambda gt-11 human hepatoma library	193:229	Several complementary DNAs (cDNAs) coding for sphingolipid activator protein-2 (SAP-2) were isolated from a lambda gt-11 human hepatoma library by means of polyclonal antibodies.
2842863	7	76	theme	helix	1118:1122	arg1	breakers					1124:1131	helix breakers	1118:1131	helix breakers	1118:1131	Each domain also contained internal amino acid sequences capable of forming amphipathic helices separated by helix breakers to give a cylindrical hydrophobic domain that is probably stabilized by disulfide bridges.
2842863	7	77	theme	capable	1066:1072	arg1	sequences					1056:1064	internal amino acid sequences	1036:1064	internal amino acid sequences capable of forming amphipathic helices separated by helix breakers to give a cylindrical hydrophobic domain that is probably stabilized by disulfide bridges	1036:1221	Each domain also contained internal amino acid sequences capable of forming amphipathic helices separated by helix breakers to give a cylindrical hydrophobic domain that is probably stabilized by disulfide bridges.
2842863	1	78	theme	gt-11	202:206	arg1	library					223:229	a lambda gt-11 human hepatoma library	193:229	a lambda gt-11 human hepatoma library	193:229	Several complementary DNAs (cDNAs) coding for sphingolipid activator protein-2 (SAP-2) were isolated from a lambda gt-11 human hepatoma library by means of polyclonal antibodies.
2842863	3	79	from	SAP-1	555:559	arg1	cDNA					582:585	the SAP precursor cDNA	564:585	the SAP precursor cDNA	564:585	The coding sequence for mature SAP-2 was located 3' to that coding for SAP-1 in the SAP precursor cDNA.
2842863	6	80	theme	sites	980:984	arg1	placement					924:932	nearly identical placement	907:932	nearly identical placement of cysteine residues, potential glycosylation sites, and proline residues	907:1006	Each of the four domains was approximately 80 amino acid residues long, had nearly identical placement of cysteine residues, potential glycosylation sites, and proline residues.
2842863	0	81	theme	same	67:70	arg1	locus					80:84	same genetic locus	67:84	same genetic locus	67:84	Coding of two sphingolipid activator proteins (SAP-1 and SAP-2) by same genetic locus.
9719680	11	0	link	linked	1624:1629	arg1	acid					1638:1641	alpha2-6 linked sialic acid	1615:1641	alpha2-6 linked sialic acid	1615:1641	Maackia amurensis agglutinins (MAA-1 and MAA-2), specific for sialic acid in alpha2-3 linkage to Gal, bind SPACR, while Sambucus nigra agglutinin (SNA), specific for alpha2-6 linked sialic acid, does not, indicating that the dominant glycoconjugate determinant on SPACR is the O-linked carbohydrate, NeuAcalpha2-3Galbeta1-3GalNAc.
9719680	11	1	theme	nigra	1578:1582	arg1	SNA					1596:1598	SNA	1596:1598	SNA	1596:1598	Maackia amurensis agglutinins (MAA-1 and MAA-2), specific for sialic acid in alpha2-3 linkage to Gal, bind SPACR, while Sambucus nigra agglutinin (SNA), specific for alpha2-6 linked sialic acid, does not, indicating that the dominant glycoconjugate determinant on SPACR is the O-linked carbohydrate, NeuAcalpha2-3Galbeta1-3GalNAc.
9719680	11	1	theme	nigra	1578:1582	arg1	agglutinin					1584:1593	Sambucus nigra agglutinin	1569:1593	Sambucus nigra agglutinin (SNA)	1569:1599	Maackia amurensis agglutinins (MAA-1 and MAA-2), specific for sialic acid in alpha2-3 linkage to Gal, bind SPACR, while Sambucus nigra agglutinin (SNA), specific for alpha2-6 linked sialic acid, does not, indicating that the dominant glycoconjugate determinant on SPACR is the O-linked carbohydrate, NeuAcalpha2-3Galbeta1-3GalNAc.
9719680	0	2	theme	binding	160:166	arg1	analysis					168:175	immunological and lectin binding analysis	135:175	analysis	168:175	Characterization of SPACR, a sialoprotein associated with cones and rods present in the interphotoreceptor matrix of the human retina: immunological and lectin binding analysis.
9719680	6	3	theme	polyclonal	761:770	arg1	antibody					772:779	A polyclonal antibody	759:779	A polyclonal antibody to SPACR	759:788	A polyclonal antibody to SPACR was prepared that colocalizes in tissue preparations with WGA-binding domains in the IPM.
9719680	8	4	theme	molecular	1129:1137	arg1	mass					1139:1142	the relative molecular mass	1116:1142	the relative molecular mass of SPACR by about 30%	1116:1164	Complete deglycosylation results in a reduction in the relative molecular mass of SPACR by about 30%.
9719680	11	5	theme	specific	1602:1609	arg1	SNA					1596:1598	SNA	1596:1598	SNA	1596:1598	Maackia amurensis agglutinins (MAA-1 and MAA-2), specific for sialic acid in alpha2-3 linkage to Gal, bind SPACR, while Sambucus nigra agglutinin (SNA), specific for alpha2-6 linked sialic acid, does not, indicating that the dominant glycoconjugate determinant on SPACR is the O-linked carbohydrate, NeuAcalpha2-3Galbeta1-3GalNAc.
9719680	11	5	theme	specific	1602:1609	arg1	agglutinin					1584:1593	Sambucus nigra agglutinin	1569:1593	Sambucus nigra agglutinin (SNA)	1569:1599	Maackia amurensis agglutinins (MAA-1 and MAA-2), specific for sialic acid in alpha2-3 linkage to Gal, bind SPACR, while Sambucus nigra agglutinin (SNA), specific for alpha2-6 linked sialic acid, does not, indicating that the dominant glycoconjugate determinant on SPACR is the O-linked carbohydrate, NeuAcalpha2-3Galbeta1-3GalNAc.
9719680	10	6	theme	peanut	1374:1379	arg1	agglutinin					1381:1390	peanut agglutinin	1374:1390	positive peanut agglutinin (PNA) staining	1365:1405	Treatment with neuraminidase exposes Galbeta1-3GalNAc disaccharide as indicated by positive peanut agglutinin (PNA) staining, accompanied by the loss of WGA staining.
9719680	10	6	theme	peanut	1374:1379	arg1	PNA					1393:1395	PNA	1393:1395	PNA	1393:1395	Treatment with neuraminidase exposes Galbeta1-3GalNAc disaccharide as indicated by positive peanut agglutinin (PNA) staining, accompanied by the loss of WGA staining.
9719680	1	7	theme	carbohydrate-rich	252:268	arg1	IPM					297:299	IPM	297:299	IPM	297:299	Rod and cone photoreceptors project from the outer retinal surface into a carbohydrate-rich interphotoreceptor matrix (IPM).
9719680	1	7	theme	carbohydrate-rich	252:268	arg1	matrix					289:294	a carbohydrate-rich interphotoreceptor matrix	250:294	a carbohydrate-rich interphotoreceptor matrix (IPM)	250:300	Rod and cone photoreceptors project from the outer retinal surface into a carbohydrate-rich interphotoreceptor matrix (IPM).
9719680	11	8	theme	alpha2-3	1526:1533	arg1	linkage					1535:1541	alpha2-3 linkage	1526:1541	alpha2-3 linkage to Gal	1526:1548	Maackia amurensis agglutinins (MAA-1 and MAA-2), specific for sialic acid in alpha2-3 linkage to Gal, bind SPACR, while Sambucus nigra agglutinin (SNA), specific for alpha2-6 linked sialic acid, does not, indicating that the dominant glycoconjugate determinant on SPACR is the O-linked carbohydrate, NeuAcalpha2-3Galbeta1-3GalNAc.
9719680	6	9	theme	tissue	823:828	arg1	preparations					830:841	tissue preparations	823:841	tissue preparations	823:841	A polyclonal antibody to SPACR was prepared that colocalizes in tissue preparations with WGA-binding domains in the IPM.
9719680	11	10	theme	O-linked	1726:1733	arg1	NeuAcalpha2-3Galbeta1-3GalNAc					1749:1777	NeuAcalpha2-3Galbeta1-3GalNAc	1749:1777	NeuAcalpha2-3Galbeta1-3GalNAc	1749:1777	Maackia amurensis agglutinins (MAA-1 and MAA-2), specific for sialic acid in alpha2-3 linkage to Gal, bind SPACR, while Sambucus nigra agglutinin (SNA), specific for alpha2-6 linked sialic acid, does not, indicating that the dominant glycoconjugate determinant on SPACR is the O-linked carbohydrate, NeuAcalpha2-3Galbeta1-3GalNAc.
9719680	11	10	theme	O-linked	1726:1733	arg1	carbohydrate					1735:1746	the O-linked carbohydrate	1722:1746	the O-linked carbohydrate	1722:1746	Maackia amurensis agglutinins (MAA-1 and MAA-2), specific for sialic acid in alpha2-3 linkage to Gal, bind SPACR, while Sambucus nigra agglutinin (SNA), specific for alpha2-6 linked sialic acid, does not, indicating that the dominant glycoconjugate determinant on SPACR is the O-linked carbohydrate, NeuAcalpha2-3Galbeta1-3GalNAc.
9719680	11	10	theme	O-linked	1726:1733	arg1	determinant					1698:1708	the dominant glycoconjugate determinant	1670:1708	the dominant glycoconjugate determinant on SPACR	1670:1717	Maackia amurensis agglutinins (MAA-1 and MAA-2), specific for sialic acid in alpha2-3 linkage to Gal, bind SPACR, while Sambucus nigra agglutinin (SNA), specific for alpha2-6 linked sialic acid, does not, indicating that the dominant glycoconjugate determinant on SPACR is the O-linked carbohydrate, NeuAcalpha2-3Galbeta1-3GalNAc.
9719680	7	11	theme	O-linked	1039:1046	arg1	glycoconjugates					1048:1062	O-linked glycoconjugates	1039:1062	O-linked glycoconjugates	1039:1062	Sequential digestion of SPACR with N- and O-glycosidases results in a systematic increase in electrophorectic mobility, indicating the presence of both N- and O-linked glycoconjugates.
9719680	2	12	theme	Unique	303:308	arg1	glycoconjugates					314:328	Unique IPM glycoconjugates	303:328	Unique IPM glycoconjugates	303:328	Unique IPM glycoconjugates are distributed around rods and cones.
9719680	1	13	theme	Rod	178:180	arg1	photoreceptors					191:204	Rod and cone photoreceptors	178:204	Rod and cone photoreceptors	178:204	Rod and cone photoreceptors project from the outer retinal surface into a carbohydrate-rich interphotoreceptor matrix (IPM).
9719680	7	14	theme	N-	1032:1033	arg1	presence					1015:1022	the presence	1011:1022	the presence of both N- and O-linked glycoconjugates	1011:1062	Sequential digestion of SPACR with N- and O-glycosidases results in a systematic increase in electrophorectic mobility, indicating the presence of both N- and O-linked glycoconjugates.
9719680	9	15	theme	lectin	1179:1184	arg1	binding					1186:1192	lectin binding	1179:1192	lectin binding	1179:1192	Analysis of lectin binding allowed us to identify some of the structural characteristics of SPACR glycoconjugates.
9719680	1	16	theme	cone	186:189	arg1	photoreceptors					191:204	Rod and cone photoreceptors	178:204	Rod and cone photoreceptors	178:204	Rod and cone photoreceptors project from the outer retinal surface into a carbohydrate-rich interphotoreceptor matrix (IPM).
9719680	0	17	theme	human	121:125	arg1	retina					127:132	the human retina	117:132	the human retina	117:132	Characterization of SPACR, a sialoprotein associated with cones and rods present in the interphotoreceptor matrix of the human retina: immunological and lectin binding analysis.
9719680	12	18	theme	IPM	1912:1914	arg1	nature					1898:1903	the polyanionic nature	1882:1903	the polyanionic nature of the IPM	1882:1914	The abundance of sialic acid in SPACR suggests that this glycoprotein may contribute substantially to the polyanionic nature of the IPM.
9719680	7	19	theme	systematic	950:959	arg1	increase					961:968	a systematic increase	948:968	a systematic increase in electrophorectic mobility	948:997	Sequential digestion of SPACR with N- and O-glycosidases results in a systematic increase in electrophorectic mobility, indicating the presence of both N- and O-linked glycoconjugates.
9719680	12	20	from	abundance	1784:1792	arg1	SPACR					1812:1816	SPACR	1812:1816	SPACR	1812:1816	The abundance of sialic acid in SPACR suggests that this glycoprotein may contribute substantially to the polyanionic nature of the IPM.
9719680	11	21	theme	sialic	1511:1516	arg1	acid					1518:1521	sialic acid	1511:1521	sialic acid in alpha2-3 linkage to Gal	1511:1548	Maackia amurensis agglutinins (MAA-1 and MAA-2), specific for sialic acid in alpha2-3 linkage to Gal, bind SPACR, while Sambucus nigra agglutinin (SNA), specific for alpha2-6 linked sialic acid, does not, indicating that the dominant glycoconjugate determinant on SPACR is the O-linked carbohydrate, NeuAcalpha2-3Galbeta1-3GalNAc.
9719680	4	22	dep	SPACR	584:588	arg1	sialoprotein					591:602	sialoprotein	591:602	sialoprotein associated with cones and rods	591:633	This study characterizes the major WGA-binding glycoprotein in the human IPM, which we refer to as SPACR (sialoprotein associated with cones and rods).
9719680	11	23	theme	amurensis	1457:1465	arg1	agglutinins					1467:1477	Maackia amurensis agglutinins	1449:1477	Maackia amurensis agglutinins (MAA-1 and MAA-2)	1449:1495	Maackia amurensis agglutinins (MAA-1 and MAA-2), specific for sialic acid in alpha2-3 linkage to Gal, bind SPACR, while Sambucus nigra agglutinin (SNA), specific for alpha2-6 linked sialic acid, does not, indicating that the dominant glycoconjugate determinant on SPACR is the O-linked carbohydrate, NeuAcalpha2-3Galbeta1-3GalNAc.
9719680	11	23	theme	amurensis	1457:1465	arg1	MAA-2					1490:1494	MAA-2	1490:1494	MAA-2	1490:1494	Maackia amurensis agglutinins (MAA-1 and MAA-2), specific for sialic acid in alpha2-3 linkage to Gal, bind SPACR, while Sambucus nigra agglutinin (SNA), specific for alpha2-6 linked sialic acid, does not, indicating that the dominant glycoconjugate determinant on SPACR is the O-linked carbohydrate, NeuAcalpha2-3Galbeta1-3GalNAc.
9719680	11	23	theme	amurensis	1457:1465	arg1	MAA-1					1480:1484	MAA-1	1480:1484	MAA-1	1480:1484	Maackia amurensis agglutinins (MAA-1 and MAA-2), specific for sialic acid in alpha2-3 linkage to Gal, bind SPACR, while Sambucus nigra agglutinin (SNA), specific for alpha2-6 linked sialic acid, does not, indicating that the dominant glycoconjugate determinant on SPACR is the O-linked carbohydrate, NeuAcalpha2-3Galbeta1-3GalNAc.
9719680	4	24	gly	glycoprotein	532:543	arg1	glycoprotein					532:543	the major WGA-binding glycoprotein	510:543	the major WGA-binding glycoprotein	510:543	This study characterizes the major WGA-binding glycoprotein in the human IPM, which we refer to as SPACR (sialoprotein associated with cones and rods).
9719680	12	25	gly	glycoprotein	1837:1848	arg1	glycoprotein					1837:1848	this glycoprotein	1832:1848	this glycoprotein	1832:1848	The abundance of sialic acid in SPACR suggests that this glycoprotein may contribute substantially to the polyanionic nature of the IPM.
9719680	13	26	theme	IPM	2058:2060	arg1	lattice					2062:2068	the ordered IPM lattice	2046:2068	the ordered IPM lattice that surrounds the elongate photoreceptors projecting from the outer retinal surface	2046:2153	The carbohydrate chains present on SPACR could also provide sites for extensive crosslinking and participate in the formation of the ordered IPM lattice that surrounds the elongate photoreceptors projecting from the outer retinal surface.
9719680	13	27	theme	carbohydrate	1921:1932	arg1	chains					1934:1939	The carbohydrate chains	1917:1939	The carbohydrate chains present on SPACR	1917:1956	The carbohydrate chains present on SPACR could also provide sites for extensive crosslinking and participate in the formation of the ordered IPM lattice that surrounds the elongate photoreceptors projecting from the outer retinal surface.
9719680	11	28	theme	glycoconjugate	1683:1696	arg1	determinant					1698:1708	the dominant glycoconjugate determinant	1670:1708	the dominant glycoconjugate determinant on SPACR	1670:1717	Maackia amurensis agglutinins (MAA-1 and MAA-2), specific for sialic acid in alpha2-3 linkage to Gal, bind SPACR, while Sambucus nigra agglutinin (SNA), specific for alpha2-6 linked sialic acid, does not, indicating that the dominant glycoconjugate determinant on SPACR is the O-linked carbohydrate, NeuAcalpha2-3Galbeta1-3GalNAc.
9719680	11	28	theme	glycoconjugate	1683:1696	arg1	carbohydrate					1735:1746	the O-linked carbohydrate	1722:1746	the O-linked carbohydrate	1722:1746	Maackia amurensis agglutinins (MAA-1 and MAA-2), specific for sialic acid in alpha2-3 linkage to Gal, bind SPACR, while Sambucus nigra agglutinin (SNA), specific for alpha2-6 linked sialic acid, does not, indicating that the dominant glycoconjugate determinant on SPACR is the O-linked carbohydrate, NeuAcalpha2-3Galbeta1-3GalNAc.
9719680	9	29	theme	SPACR	1259:1263	arg1	glycoconjugates					1265:1279	SPACR glycoconjugates	1259:1279	SPACR glycoconjugates	1259:1279	Analysis of lectin binding allowed us to identify some of the structural characteristics of SPACR glycoconjugates.
9719680	7	30	theme	SPACR	904:908	arg1	digestion					891:899	Sequential digestion	880:899	Sequential digestion of SPACR with N- and O-glycosidases	880:935	Sequential digestion of SPACR with N- and O-glycosidases results in a systematic increase in electrophorectic mobility, indicating the presence of both N- and O-linked glycoconjugates.
9719680	3	31	theme	matrix	424:429	arg1	domains					431:437	the rod matrix domains	416:437	the rod matrix domains	416:437	Wheat germ agglutinin (WGA) strongly decorates the rod matrix domains and weakly decorates the cone matrix domains.
9719680	0	32	theme	interphotoreceptor	88:105	arg1	matrix					107:112	the interphotoreceptor matrix	84:112	the interphotoreceptor matrix of the human retina	84:132	Characterization of SPACR, a sialoprotein associated with cones and rods present in the interphotoreceptor matrix of the human retina: immunological and lectin binding analysis.
9719680	10	33	theme	WGA	1435:1437	arg1	staining					1439:1446	WGA staining	1435:1446	WGA staining	1435:1446	Treatment with neuraminidase exposes Galbeta1-3GalNAc disaccharide as indicated by positive peanut agglutinin (PNA) staining, accompanied by the loss of WGA staining.
9719680	1	34	theme	interphotoreceptor	270:287	arg1	IPM					297:299	IPM	297:299	IPM	297:299	Rod and cone photoreceptors project from the outer retinal surface into a carbohydrate-rich interphotoreceptor matrix (IPM).
9719680	1	34	theme	interphotoreceptor	270:287	arg1	matrix					289:294	a carbohydrate-rich interphotoreceptor matrix	250:294	a carbohydrate-rich interphotoreceptor matrix (IPM)	250:300	Rod and cone photoreceptors project from the outer retinal surface into a carbohydrate-rich interphotoreceptor matrix (IPM).
9719680	3	35	theme	Wheat	369:373	arg1	agglutinin					380:389	Wheat germ agglutinin	369:389	Wheat germ agglutinin (WGA)	369:395	Wheat germ agglutinin (WGA) strongly decorates the rod matrix domains and weakly decorates the cone matrix domains.
9719680	3	35	theme	Wheat	369:373	arg1	WGA					392:394	WGA	392:394	WGA	392:394	Wheat germ agglutinin (WGA) strongly decorates the rod matrix domains and weakly decorates the cone matrix domains.
9719680	11	36	theme	specific	1498:1505	arg1	agglutinins					1467:1477	Maackia amurensis agglutinins	1449:1477	Maackia amurensis agglutinins (MAA-1 and MAA-2)	1449:1495	Maackia amurensis agglutinins (MAA-1 and MAA-2), specific for sialic acid in alpha2-3 linkage to Gal, bind SPACR, while Sambucus nigra agglutinin (SNA), specific for alpha2-6 linked sialic acid, does not, indicating that the dominant glycoconjugate determinant on SPACR is the O-linked carbohydrate, NeuAcalpha2-3Galbeta1-3GalNAc.
9719680	11	36	theme	specific	1498:1505	arg1	MAA-2					1490:1494	MAA-2	1490:1494	MAA-2	1490:1494	Maackia amurensis agglutinins (MAA-1 and MAA-2), specific for sialic acid in alpha2-3 linkage to Gal, bind SPACR, while Sambucus nigra agglutinin (SNA), specific for alpha2-6 linked sialic acid, does not, indicating that the dominant glycoconjugate determinant on SPACR is the O-linked carbohydrate, NeuAcalpha2-3Galbeta1-3GalNAc.
9719680	11	36	theme	specific	1498:1505	arg1	MAA-1					1480:1484	MAA-1	1480:1484	MAA-1	1480:1484	Maackia amurensis agglutinins (MAA-1 and MAA-2), specific for sialic acid in alpha2-3 linkage to Gal, bind SPACR, while Sambucus nigra agglutinin (SNA), specific for alpha2-6 linked sialic acid, does not, indicating that the dominant glycoconjugate determinant on SPACR is the O-linked carbohydrate, NeuAcalpha2-3Galbeta1-3GalNAc.
9719680	0	37	theme	SPACR	20:24	arg1	Characterization					0:15	Characterization	0:15	Characterization of SPACR, a sialoprotein associated with cones and rods present in the interphotoreceptor matrix of the human retina: immunological and lectin binding analysis.	0:176	Characterization of SPACR, a sialoprotein associated with cones and rods present in the interphotoreceptor matrix of the human retina: immunological and lectin binding analysis.
9719680	4	38	from	glycoprotein	532:543	arg1	IPM					558:560	the human IPM	548:560	the human IPM	548:560	This study characterizes the major WGA-binding glycoprotein in the human IPM, which we refer to as SPACR (sialoprotein associated with cones and rods).
9719680	8	39	from	reduction	1103:1111	arg1	mass					1139:1142	the relative molecular mass	1116:1142	the relative molecular mass of SPACR by about 30%	1116:1164	Complete deglycosylation results in a reduction in the relative molecular mass of SPACR by about 30%.
9719680	5	40	contain	has	650:652	arg2	weight					666:671	a molecular weight	654:671	a molecular weight of 147 kDa	654:682	SPACR, which has a molecular weight of 147 kDa, was isolated and purified from the IPM by lectin affinity chromatography.
9719680	5	40	contain	has	650:652	arg1	SPACR					637:641	SPACR	637:641	SPACR	637:641	SPACR, which has a molecular weight of 147 kDa, was isolated and purified from the IPM by lectin affinity chromatography.
9719680	11	41	theme	linked	1624:1629	arg1	acid					1638:1641	alpha2-6 linked sialic acid	1615:1641	alpha2-6 linked sialic acid	1615:1641	Maackia amurensis agglutinins (MAA-1 and MAA-2), specific for sialic acid in alpha2-3 linkage to Gal, bind SPACR, while Sambucus nigra agglutinin (SNA), specific for alpha2-6 linked sialic acid, does not, indicating that the dominant glycoconjugate determinant on SPACR is the O-linked carbohydrate, NeuAcalpha2-3Galbeta1-3GalNAc.
9719680	5	42	theme	affinity	734:741	arg1	chromatography					743:756	lectin affinity chromatography	727:756	lectin affinity chromatography	727:756	SPACR, which has a molecular weight of 147 kDa, was isolated and purified from the IPM by lectin affinity chromatography.
9719680	8	43	theme	Complete	1065:1072	arg1	deglycosylation					1074:1088	Complete deglycosylation	1065:1088	Complete deglycosylation	1065:1088	Complete deglycosylation results in a reduction in the relative molecular mass of SPACR by about 30%.
9719680	3	44	theme	cone	464:467	arg1	domains					476:482	the cone matrix domains	460:482	the cone matrix domains	460:482	Wheat germ agglutinin (WGA) strongly decorates the rod matrix domains and weakly decorates the cone matrix domains.
9719680	13	45	theme	outer	2133:2137	arg1	surface					2147:2153	the outer retinal surface	2129:2153	the outer retinal surface	2129:2153	The carbohydrate chains present on SPACR could also provide sites for extensive crosslinking and participate in the formation of the ordered IPM lattice that surrounds the elongate photoreceptors projecting from the outer retinal surface.
9719680	12	46	theme	sialic	1797:1802	arg1	acid					1804:1807	sialic acid	1797:1807	sialic acid	1797:1807	The abundance of sialic acid in SPACR suggests that this glycoprotein may contribute substantially to the polyanionic nature of the IPM.
9719680	11	47	theme	Sambucus	1569:1576	arg1	SNA					1596:1598	SNA	1596:1598	SNA	1596:1598	Maackia amurensis agglutinins (MAA-1 and MAA-2), specific for sialic acid in alpha2-3 linkage to Gal, bind SPACR, while Sambucus nigra agglutinin (SNA), specific for alpha2-6 linked sialic acid, does not, indicating that the dominant glycoconjugate determinant on SPACR is the O-linked carbohydrate, NeuAcalpha2-3Galbeta1-3GalNAc.
9719680	11	47	theme	Sambucus	1569:1576	arg1	agglutinin					1584:1593	Sambucus nigra agglutinin	1569:1593	Sambucus nigra agglutinin (SNA)	1569:1599	Maackia amurensis agglutinins (MAA-1 and MAA-2), specific for sialic acid in alpha2-3 linkage to Gal, bind SPACR, while Sambucus nigra agglutinin (SNA), specific for alpha2-6 linked sialic acid, does not, indicating that the dominant glycoconjugate determinant on SPACR is the O-linked carbohydrate, NeuAcalpha2-3Galbeta1-3GalNAc.
9719680	1	48	theme	outer	223:227	arg1	surface					237:243	the outer retinal surface	219:243	the outer retinal surface	219:243	Rod and cone photoreceptors project from the outer retinal surface into a carbohydrate-rich interphotoreceptor matrix (IPM).
9719680	0	49	dep	Characterization	0:15	arg1	analysis					168:175	immunological and lectin binding analysis	135:175	analysis	168:175	Characterization of SPACR, a sialoprotein associated with cones and rods present in the interphotoreceptor matrix of the human retina: immunological and lectin binding analysis.
9719680	4	50	theme	major	514:518	arg1	glycoprotein					532:543	the major WGA-binding glycoprotein	510:543	the major WGA-binding glycoprotein	510:543	This study characterizes the major WGA-binding glycoprotein in the human IPM, which we refer to as SPACR (sialoprotein associated with cones and rods).
9719680	10	51	theme	agglutinin	1381:1390	arg1	staining					1398:1405	positive peanut agglutinin (PNA) staining	1365:1405	positive peanut agglutinin (PNA) staining	1365:1405	Treatment with neuraminidase exposes Galbeta1-3GalNAc disaccharide as indicated by positive peanut agglutinin (PNA) staining, accompanied by the loss of WGA staining.
9719680	8	52	theme	relative	1120:1127	arg1	mass					1139:1142	the relative molecular mass	1116:1142	the relative molecular mass of SPACR by about 30%	1116:1164	Complete deglycosylation results in a reduction in the relative molecular mass of SPACR by about 30%.
9719680	6	53	theme	WGA-binding	848:858	arg1	domains					860:866	WGA-binding domains	848:866	WGA-binding domains in the IPM	848:877	A polyclonal antibody to SPACR was prepared that colocalizes in tissue preparations with WGA-binding domains in the IPM.
9719680	7	54	theme	glycoconjugates	1048:1062	arg1	presence					1015:1022	the presence	1011:1022	the presence of both N- and O-linked glycoconjugates	1011:1062	Sequential digestion of SPACR with N- and O-glycosidases results in a systematic increase in electrophorectic mobility, indicating the presence of both N- and O-linked glycoconjugates.
9719680	10	55	theme	positive	1365:1372	arg1	staining					1398:1405	positive peanut agglutinin (PNA) staining	1365:1405	positive peanut agglutinin (PNA) staining	1365:1405	Treatment with neuraminidase exposes Galbeta1-3GalNAc disaccharide as indicated by positive peanut agglutinin (PNA) staining, accompanied by the loss of WGA staining.
9719680	10	56	dep	disaccharide	1336:1347	arg1	indicated					1352:1360	indicated	1352:1360	indicated by positive peanut agglutinin (PNA) staining	1352:1405	Treatment with neuraminidase exposes Galbeta1-3GalNAc disaccharide as indicated by positive peanut agglutinin (PNA) staining, accompanied by the loss of WGA staining.
9719680	2	57	theme	IPM	310:312	arg1	glycoconjugates					314:328	Unique IPM glycoconjugates	303:328	Unique IPM glycoconjugates	303:328	Unique IPM glycoconjugates are distributed around rods and cones.
9719680	8	58	theme	SPACR	1147:1151	arg1	mass					1139:1142	the relative molecular mass	1116:1142	the relative molecular mass of SPACR by about 30%	1116:1164	Complete deglycosylation results in a reduction in the relative molecular mass of SPACR by about 30%.
9719680	5	59	theme	molecular	656:664	arg1	weight					666:671	a molecular weight	654:671	a molecular weight of 147 kDa	654:682	SPACR, which has a molecular weight of 147 kDa, was isolated and purified from the IPM by lectin affinity chromatography.
9719680	7	60	with	digestion	891:899	arg1	O-glycosidases					922:935	O-glycosidases	922:935	O-glycosidases	922:935	Sequential digestion of SPACR with N- and O-glycosidases results in a systematic increase in electrophorectic mobility, indicating the presence of both N- and O-linked glycoconjugates.
9719680	7	60	with	digestion	891:899	arg1	N-					915:916	N-	915:916	N-	915:916	Sequential digestion of SPACR with N- and O-glycosidases results in a systematic increase in electrophorectic mobility, indicating the presence of both N- and O-linked glycoconjugates.
9719680	11	61	from	determinant	1698:1708	arg1	SPACR					1713:1717	SPACR	1713:1717	SPACR	1713:1717	Maackia amurensis agglutinins (MAA-1 and MAA-2), specific for sialic acid in alpha2-3 linkage to Gal, bind SPACR, while Sambucus nigra agglutinin (SNA), specific for alpha2-6 linked sialic acid, does not, indicating that the dominant glycoconjugate determinant on SPACR is the O-linked carbohydrate, NeuAcalpha2-3Galbeta1-3GalNAc.
9719680	0	62	from	present	73:79	arg1	matrix					107:112	the interphotoreceptor matrix	84:112	the interphotoreceptor matrix of the human retina	84:132	Characterization of SPACR, a sialoprotein associated with cones and rods present in the interphotoreceptor matrix of the human retina: immunological and lectin binding analysis.
9719680	7	63	from	increase	961:968	arg1	mobility					990:997	electrophorectic mobility	973:997	electrophorectic mobility	973:997	Sequential digestion of SPACR with N- and O-glycosidases results in a systematic increase in electrophorectic mobility, indicating the presence of both N- and O-linked glycoconjugates.
9719680	1	64	from	surface	237:243	arg1	project					206:212	project	206:212	project	206:212	Rod and cone photoreceptors project from the outer retinal surface into a carbohydrate-rich interphotoreceptor matrix (IPM).
9719680	9	65	theme	binding	1186:1192	arg1	Analysis					1167:1174	Analysis	1167:1174	Analysis of lectin binding	1167:1192	Analysis of lectin binding allowed us to identify some of the structural characteristics of SPACR glycoconjugates.
9719680	0	66	theme	immunological	135:147	arg1	analysis					168:175	immunological and lectin binding analysis	135:175	analysis	168:175	Characterization of SPACR, a sialoprotein associated with cones and rods present in the interphotoreceptor matrix of the human retina: immunological and lectin binding analysis.
9719680	13	67	theme	elongate	2089:2096	arg1	photoreceptors					2098:2111	the elongate photoreceptors	2085:2111	the elongate photoreceptors projecting from the outer retinal surface	2085:2153	The carbohydrate chains present on SPACR could also provide sites for extensive crosslinking and participate in the formation of the ordered IPM lattice that surrounds the elongate photoreceptors projecting from the outer retinal surface.
9719680	7	68	theme	electrophorectic	973:988	arg1	mobility					990:997	electrophorectic mobility	973:997	electrophorectic mobility	973:997	Sequential digestion of SPACR with N- and O-glycosidases results in a systematic increase in electrophorectic mobility, indicating the presence of both N- and O-linked glycoconjugates.
9719680	11	69	from	acid	1518:1521	arg1	linkage					1535:1541	alpha2-3 linkage	1526:1541	alpha2-3 linkage to Gal	1526:1548	Maackia amurensis agglutinins (MAA-1 and MAA-2), specific for sialic acid in alpha2-3 linkage to Gal, bind SPACR, while Sambucus nigra agglutinin (SNA), specific for alpha2-6 linked sialic acid, does not, indicating that the dominant glycoconjugate determinant on SPACR is the O-linked carbohydrate, NeuAcalpha2-3Galbeta1-3GalNAc.
9719680	0	70	from	matrix	107:112	arg1	present					73:79	present	73:79	present	73:79	Characterization of SPACR, a sialoprotein associated with cones and rods present in the interphotoreceptor matrix of the human retina: immunological and lectin binding analysis.
9719680	0	71	theme	lectin	153:158	arg1	analysis					168:175	immunological and lectin binding analysis	135:175	analysis	168:175	Characterization of SPACR, a sialoprotein associated with cones and rods present in the interphotoreceptor matrix of the human retina: immunological and lectin binding analysis.
9719680	13	72	theme	ordered	2050:2056	arg1	lattice					2062:2068	the ordered IPM lattice	2046:2068	the ordered IPM lattice that surrounds the elongate photoreceptors projecting from the outer retinal surface	2046:2153	The carbohydrate chains present on SPACR could also provide sites for extensive crosslinking and participate in the formation of the ordered IPM lattice that surrounds the elongate photoreceptors projecting from the outer retinal surface.
9719680	11	73	theme	dominant	1674:1681	arg1	determinant					1698:1708	the dominant glycoconjugate determinant	1670:1708	the dominant glycoconjugate determinant on SPACR	1670:1717	Maackia amurensis agglutinins (MAA-1 and MAA-2), specific for sialic acid in alpha2-3 linkage to Gal, bind SPACR, while Sambucus nigra agglutinin (SNA), specific for alpha2-6 linked sialic acid, does not, indicating that the dominant glycoconjugate determinant on SPACR is the O-linked carbohydrate, NeuAcalpha2-3Galbeta1-3GalNAc.
9719680	11	73	theme	dominant	1674:1681	arg1	carbohydrate					1735:1746	the O-linked carbohydrate	1722:1746	the O-linked carbohydrate	1722:1746	Maackia amurensis agglutinins (MAA-1 and MAA-2), specific for sialic acid in alpha2-3 linkage to Gal, bind SPACR, while Sambucus nigra agglutinin (SNA), specific for alpha2-6 linked sialic acid, does not, indicating that the dominant glycoconjugate determinant on SPACR is the O-linked carbohydrate, NeuAcalpha2-3Galbeta1-3GalNAc.
9719680	13	74	theme	lattice	2062:2068	arg1	formation					2033:2041	the formation	2029:2041	the formation of the ordered IPM lattice that surrounds the elongate photoreceptors projecting from the outer retinal surface	2029:2153	The carbohydrate chains present on SPACR could also provide sites for extensive crosslinking and participate in the formation of the ordered IPM lattice that surrounds the elongate photoreceptors projecting from the outer retinal surface.
9719680	11	75	link	O-linked	1726:1733	arg1	NeuAcalpha2-3Galbeta1-3GalNAc					1749:1777	NeuAcalpha2-3Galbeta1-3GalNAc	1749:1777	NeuAcalpha2-3Galbeta1-3GalNAc	1749:1777	Maackia amurensis agglutinins (MAA-1 and MAA-2), specific for sialic acid in alpha2-3 linkage to Gal, bind SPACR, while Sambucus nigra agglutinin (SNA), specific for alpha2-6 linked sialic acid, does not, indicating that the dominant glycoconjugate determinant on SPACR is the O-linked carbohydrate, NeuAcalpha2-3Galbeta1-3GalNAc.
9719680	11	75	link	O-linked	1726:1733	arg1	carbohydrate					1735:1746	the O-linked carbohydrate	1722:1746	the O-linked carbohydrate	1722:1746	Maackia amurensis agglutinins (MAA-1 and MAA-2), specific for sialic acid in alpha2-3 linkage to Gal, bind SPACR, while Sambucus nigra agglutinin (SNA), specific for alpha2-6 linked sialic acid, does not, indicating that the dominant glycoconjugate determinant on SPACR is the O-linked carbohydrate, NeuAcalpha2-3Galbeta1-3GalNAc.
9719680	11	75	link	O-linked	1726:1733	arg1	determinant					1698:1708	the dominant glycoconjugate determinant	1670:1708	the dominant glycoconjugate determinant on SPACR	1670:1717	Maackia amurensis agglutinins (MAA-1 and MAA-2), specific for sialic acid in alpha2-3 linkage to Gal, bind SPACR, while Sambucus nigra agglutinin (SNA), specific for alpha2-6 linked sialic acid, does not, indicating that the dominant glycoconjugate determinant on SPACR is the O-linked carbohydrate, NeuAcalpha2-3Galbeta1-3GalNAc.
9719680	0	76	theme	present	73:79	arg1	cones					58:62	cones	58:62	cones	58:62	Characterization of SPACR, a sialoprotein associated with cones and rods present in the interphotoreceptor matrix of the human retina: immunological and lectin binding analysis.
9719680	9	77	theme	structural	1229:1238	arg1	characteristics					1240:1254	the structural characteristics	1225:1254	the structural characteristics of SPACR glycoconjugates	1225:1279	Analysis of lectin binding allowed us to identify some of the structural characteristics of SPACR glycoconjugates.
9719680	13	78	theme	extensive	1987:1995	arg1	crosslinking					1997:2008	extensive crosslinking	1987:2008	extensive crosslinking	1987:2008	The carbohydrate chains present on SPACR could also provide sites for extensive crosslinking and participate in the formation of the ordered IPM lattice that surrounds the elongate photoreceptors projecting from the outer retinal surface.
9719680	5	79	theme	kDa	680:682	arg1	weight					666:671	a molecular weight	654:671	a molecular weight of 147 kDa	654:682	SPACR, which has a molecular weight of 147 kDa, was isolated and purified from the IPM by lectin affinity chromatography.
9719680	12	80	theme	polyanionic	1886:1896	arg1	nature					1898:1903	the polyanionic nature	1882:1903	the polyanionic nature of the IPM	1882:1914	The abundance of sialic acid in SPACR suggests that this glycoprotein may contribute substantially to the polyanionic nature of the IPM.
9719680	11	81	dep	agglutinins	1467:1477	arg1	agglutinins					1467:1477	Maackia amurensis agglutinins	1449:1477	Maackia amurensis agglutinins (MAA-1 and MAA-2)	1449:1495	Maackia amurensis agglutinins (MAA-1 and MAA-2), specific for sialic acid in alpha2-3 linkage to Gal, bind SPACR, while Sambucus nigra agglutinin (SNA), specific for alpha2-6 linked sialic acid, does not, indicating that the dominant glycoconjugate determinant on SPACR is the O-linked carbohydrate, NeuAcalpha2-3Galbeta1-3GalNAc.
9719680	11	81	dep	agglutinins	1467:1477	arg1	MAA-2					1490:1494	MAA-2	1490:1494	MAA-2	1490:1494	Maackia amurensis agglutinins (MAA-1 and MAA-2), specific for sialic acid in alpha2-3 linkage to Gal, bind SPACR, while Sambucus nigra agglutinin (SNA), specific for alpha2-6 linked sialic acid, does not, indicating that the dominant glycoconjugate determinant on SPACR is the O-linked carbohydrate, NeuAcalpha2-3Galbeta1-3GalNAc.
9719680	11	81	dep	agglutinins	1467:1477	arg1	MAA-1					1480:1484	MAA-1	1480:1484	MAA-1	1480:1484	Maackia amurensis agglutinins (MAA-1 and MAA-2), specific for sialic acid in alpha2-3 linkage to Gal, bind SPACR, while Sambucus nigra agglutinin (SNA), specific for alpha2-6 linked sialic acid, does not, indicating that the dominant glycoconjugate determinant on SPACR is the O-linked carbohydrate, NeuAcalpha2-3Galbeta1-3GalNAc.
9719680	9	82	theme	glycoconjugates	1265:1279	arg1	characteristics					1240:1254	the structural characteristics	1225:1254	the structural characteristics of SPACR glycoconjugates	1225:1279	Analysis of lectin binding allowed us to identify some of the structural characteristics of SPACR glycoconjugates.
9719680	10	83	theme	staining	1439:1446	arg1	loss					1427:1430	the loss	1423:1430	the loss of WGA staining	1423:1446	Treatment with neuraminidase exposes Galbeta1-3GalNAc disaccharide as indicated by positive peanut agglutinin (PNA) staining, accompanied by the loss of WGA staining.
9719680	13	84	theme	retinal	2139:2145	arg1	surface					2147:2153	the outer retinal surface	2129:2153	the outer retinal surface	2129:2153	The carbohydrate chains present on SPACR could also provide sites for extensive crosslinking and participate in the formation of the ordered IPM lattice that surrounds the elongate photoreceptors projecting from the outer retinal surface.
9719680	7	85	link	O-linked	1039:1046	arg1	glycoconjugates					1048:1062	O-linked glycoconjugates	1039:1062	O-linked glycoconjugates	1039:1062	Sequential digestion of SPACR with N- and O-glycosidases results in a systematic increase in electrophorectic mobility, indicating the presence of both N- and O-linked glycoconjugates.
9719680	10	86	with	Treatment	1282:1290	arg1	neuraminidase					1297:1309	neuraminidase	1297:1309	neuraminidase	1297:1309	Treatment with neuraminidase exposes Galbeta1-3GalNAc disaccharide as indicated by positive peanut agglutinin (PNA) staining, accompanied by the loss of WGA staining.
9719680	0	87	theme	retina	127:132	arg1	matrix					107:112	the interphotoreceptor matrix	84:112	the interphotoreceptor matrix of the human retina	84:132	Characterization of SPACR, a sialoprotein associated with cones and rods present in the interphotoreceptor matrix of the human retina: immunological and lectin binding analysis.
9719680	4	88	theme	human	552:556	arg1	IPM					558:560	the human IPM	548:560	the human IPM	548:560	This study characterizes the major WGA-binding glycoprotein in the human IPM, which we refer to as SPACR (sialoprotein associated with cones and rods).
9719680	3	89	theme	rod	420:422	arg1	domains					431:437	the rod matrix domains	416:437	the rod matrix domains	416:437	Wheat germ agglutinin (WGA) strongly decorates the rod matrix domains and weakly decorates the cone matrix domains.
9719680	7	90	theme	Sequential	880:889	arg1	digestion					891:899	Sequential digestion	880:899	Sequential digestion of SPACR with N- and O-glycosidases	880:935	Sequential digestion of SPACR with N- and O-glycosidases results in a systematic increase in electrophorectic mobility, indicating the presence of both N- and O-linked glycoconjugates.
9719680	3	91	theme	germ	375:378	arg1	agglutinin					380:389	Wheat germ agglutinin	369:389	Wheat germ agglutinin (WGA)	369:395	Wheat germ agglutinin (WGA) strongly decorates the rod matrix domains and weakly decorates the cone matrix domains.
9719680	3	91	theme	germ	375:378	arg1	WGA					392:394	WGA	392:394	WGA	392:394	Wheat germ agglutinin (WGA) strongly decorates the rod matrix domains and weakly decorates the cone matrix domains.
9719680	11	92	theme	sialic	1631:1636	arg1	acid					1638:1641	alpha2-6 linked sialic acid	1615:1641	alpha2-6 linked sialic acid	1615:1641	Maackia amurensis agglutinins (MAA-1 and MAA-2), specific for sialic acid in alpha2-3 linkage to Gal, bind SPACR, while Sambucus nigra agglutinin (SNA), specific for alpha2-6 linked sialic acid, does not, indicating that the dominant glycoconjugate determinant on SPACR is the O-linked carbohydrate, NeuAcalpha2-3Galbeta1-3GalNAc.
9719680	4	93	theme	WGA-binding	520:530	arg1	glycoprotein					532:543	the major WGA-binding glycoprotein	510:543	the major WGA-binding glycoprotein	510:543	This study characterizes the major WGA-binding glycoprotein in the human IPM, which we refer to as SPACR (sialoprotein associated with cones and rods).
9719680	10	94	theme	Galbeta1-3GalNAc	1319:1334	arg1	disaccharide					1336:1347	Galbeta1-3GalNAc disaccharide	1319:1347	Galbeta1-3GalNAc disaccharide as indicated by positive peanut agglutinin (PNA) staining	1319:1405	Treatment with neuraminidase exposes Galbeta1-3GalNAc disaccharide as indicated by positive peanut agglutinin (PNA) staining, accompanied by the loss of WGA staining.
9719680	5	95	theme	lectin	727:732	arg1	chromatography					743:756	lectin affinity chromatography	727:756	lectin affinity chromatography	727:756	SPACR, which has a molecular weight of 147 kDa, was isolated and purified from the IPM by lectin affinity chromatography.
9719680	13	96	attach	present	1941:1947	arg2	chains					1934:1939	The carbohydrate chains	1917:1939	The carbohydrate chains present on SPACR	1917:1956	The carbohydrate chains present on SPACR could also provide sites for extensive crosslinking and participate in the formation of the ordered IPM lattice that surrounds the elongate photoreceptors projecting from the outer retinal surface.
9719680	13	96	attach	present	1941:1947	arg1	SPACR					1952:1956	SPACR	1952:1956	SPACR	1952:1956	The carbohydrate chains present on SPACR could also provide sites for extensive crosslinking and participate in the formation of the ordered IPM lattice that surrounds the elongate photoreceptors projecting from the outer retinal surface.
9719680	12	97	theme	acid	1804:1807	arg1	abundance					1784:1792	The abundance	1780:1792	The abundance of sialic acid in SPACR	1780:1816	The abundance of sialic acid in SPACR suggests that this glycoprotein may contribute substantially to the polyanionic nature of the IPM.
9719680	0	98	attach	present	73:79	arg2	cones					58:62	cones	58:62	cones	58:62	Characterization of SPACR, a sialoprotein associated with cones and rods present in the interphotoreceptor matrix of the human retina: immunological and lectin binding analysis.
9719680	0	98	attach	present	73:79	arg1	matrix					107:112	the interphotoreceptor matrix	84:112	the interphotoreceptor matrix of the human retina	84:132	Characterization of SPACR, a sialoprotein associated with cones and rods present in the interphotoreceptor matrix of the human retina: immunological and lectin binding analysis.
9719680	13	99	theme	present	1941:1947	arg1	chains					1934:1939	The carbohydrate chains	1917:1939	The carbohydrate chains present on SPACR	1917:1956	The carbohydrate chains present on SPACR could also provide sites for extensive crosslinking and participate in the formation of the ordered IPM lattice that surrounds the elongate photoreceptors projecting from the outer retinal surface.
9719680	3	100	theme	matrix	469:474	arg1	domains					476:482	the cone matrix domains	460:482	the cone matrix domains	460:482	Wheat germ agglutinin (WGA) strongly decorates the rod matrix domains and weakly decorates the cone matrix domains.
9719680	11	101	dep	linked	1624:1629	arg1	alpha2-6					1615:1622	alpha2-6	1615:1622	alpha2-6	1615:1622	Maackia amurensis agglutinins (MAA-1 and MAA-2), specific for sialic acid in alpha2-3 linkage to Gal, bind SPACR, while Sambucus nigra agglutinin (SNA), specific for alpha2-6 linked sialic acid, does not, indicating that the dominant glycoconjugate determinant on SPACR is the O-linked carbohydrate, NeuAcalpha2-3Galbeta1-3GalNAc.
9719680	6	102	from	domains	860:866	arg1	IPM					875:877	the IPM	871:877	the IPM	871:877	A polyclonal antibody to SPACR was prepared that colocalizes in tissue preparations with WGA-binding domains in the IPM.
9719680	1	103	theme	retinal	229:235	arg1	surface					237:243	the outer retinal surface	219:243	the outer retinal surface	219:243	Rod and cone photoreceptors project from the outer retinal surface into a carbohydrate-rich interphotoreceptor matrix (IPM).
9054441	0	0	theme	plasminogen	75:85	arg1	Ser-248					58:64	Ser-248	58:64	Ser-248 of human plasminogen 2	58:87	Evidence for a novel O-linked sialylated trisaccharide on Ser-248 of human plasminogen 2.
9054441	4	1	theme	functional	498:507	arg1	consequences					509:520	functional consequences	498:520	functional consequences	498:520	However, plasminogen 2 displays a further well documented microheterogeneity dependent on the N-acetylneuraminic acid content, which has functional consequences with regard to activation of plasminogen.
9054441	7	2	theme	analysis	1165:1172	arg1	combination					1069:1079	a combination	1067:1079	a combination of lectin affinity chromatography, desialylation experiments, and mass spectrometry analysis	1067:1172	Direct evidence for the structure of the carbohydrate was obtained from a combination of lectin affinity chromatography, desialylation experiments, and mass spectrometry analysis.
9054441	6	3	gly	glycosylation	952:964	arg1	plasminogen					969:979	plasminogen 2	969:981	plasminogen 2	969:981	In the present study, a combination of trypsin digestion, lectin affinity chromatography, Edman degradation amino acid sequence analysis, carbohydrate composition analysis, and mass spectrometry revealed the existence of a novel site for O-linked glycosylation on plasminogen 2 at Ser-248.
9054441	6	3	gly	glycosylation	952:964	arg1	Ser-248					986:992	Ser-248	986:992	Ser-248	986:992	In the present study, a combination of trypsin digestion, lectin affinity chromatography, Edman degradation amino acid sequence analysis, carbohydrate composition analysis, and mass spectrometry revealed the existence of a novel site for O-linked glycosylation on plasminogen 2 at Ser-248.
9054441	6	3	gly	glycosylation	952:964	arg2	Ser-248					986:992	Ser-248	986:992	Ser-248	986:992	In the present study, a combination of trypsin digestion, lectin affinity chromatography, Edman degradation amino acid sequence analysis, carbohydrate composition analysis, and mass spectrometry revealed the existence of a novel site for O-linked glycosylation on plasminogen 2 at Ser-248.
9054441	0	4	theme	human	69:73	arg1	plasminogen					75:85	human plasminogen 2	69:87	human plasminogen 2	69:87	Evidence for a novel O-linked sialylated trisaccharide on Ser-248 of human plasminogen 2.
9054441	7	5	theme	spectrometry	1152:1163	arg1	analysis					1165:1172	mass spectrometry analysis	1147:1172	mass spectrometry analysis	1147:1172	Direct evidence for the structure of the carbohydrate was obtained from a combination of lectin affinity chromatography, desialylation experiments, and mass spectrometry analysis.
9054441	6	6	theme	analysis	868:875	arg1	combination					729:739	a combination	727:739	a combination of trypsin digestion, lectin affinity chromatography, Edman degradation amino acid sequence analysis, carbohydrate composition analysis, and mass spectrometry	727:898	In the present study, a combination of trypsin digestion, lectin affinity chromatography, Edman degradation amino acid sequence analysis, carbohydrate composition analysis, and mass spectrometry revealed the existence of a novel site for O-linked glycosylation on plasminogen 2 at Ser-248.
9054441	5	7	theme	oligosaccharide	607:621	arg1	linkages					623:630	known oligosaccharide linkages	601:630	known oligosaccharide linkages	601:630	The proposed structure and number of known oligosaccharide linkages in plasminogen 2 is insufficient to account for this microheterogeneity.
9054441	6	8	theme	mass	882:885	arg1	spectrometry					887:898	mass spectrometry	882:898	mass spectrometry	882:898	In the present study, a combination of trypsin digestion, lectin affinity chromatography, Edman degradation amino acid sequence analysis, carbohydrate composition analysis, and mass spectrometry revealed the existence of a novel site for O-linked glycosylation on plasminogen 2 at Ser-248.
9054441	6	9	theme	spectrometry	887:898	arg1	combination					729:739	a combination	727:739	a combination of trypsin digestion, lectin affinity chromatography, Edman degradation amino acid sequence analysis, carbohydrate composition analysis, and mass spectrometry	727:898	In the present study, a combination of trypsin digestion, lectin affinity chromatography, Edman degradation amino acid sequence analysis, carbohydrate composition analysis, and mass spectrometry revealed the existence of a novel site for O-linked glycosylation on plasminogen 2 at Ser-248.
9054441	6	10	theme	site	934:937	arg1	existence					913:921	the existence	909:921	the existence of a novel site for O-linked glycosylation on plasminogen 2 at Ser-248	909:992	In the present study, a combination of trypsin digestion, lectin affinity chromatography, Edman degradation amino acid sequence analysis, carbohydrate composition analysis, and mass spectrometry revealed the existence of a novel site for O-linked glycosylation on plasminogen 2 at Ser-248.
9054441	7	11	theme	mass	1147:1150	arg1	analysis					1165:1172	mass spectrometry analysis	1147:1172	mass spectrometry analysis	1147:1172	Direct evidence for the structure of the carbohydrate was obtained from a combination of lectin affinity chromatography, desialylation experiments, and mass spectrometry analysis.
9054441	5	12	theme	linkages	623:630	arg1	number					591:596	number	591:596	number	591:596	The proposed structure and number of known oligosaccharide linkages in plasminogen 2 is insufficient to account for this microheterogeneity.
9054441	5	12	theme	linkages	623:630	arg1	structure					577:585	proposed structure	568:585	proposed structure	568:585	The proposed structure and number of known oligosaccharide linkages in plasminogen 2 is insufficient to account for this microheterogeneity.
9054441	3	13	link	O-linked	324:331	arg1	oligosaccharide					333:347	only an O-linked oligosaccharide	316:347	only an O-linked oligosaccharide	316:347	Plasminogen 2 is known to contain only an O-linked oligosaccharide at Thr-345.
9054441	2	14	link	O-linked	245:252	arg1	oligosaccharide					254:268	an O-linked oligosaccharide	242:268	an O-linked oligosaccharide at Thr-345	242:279	Plasminogen 1 contains an N-linked oligosaccharide at Asn-289 and an O-linked oligosaccharide at Thr-345.
9054441	8	15	theme	structural	1200:1209	arg1	basis					1211:1215	a structural basis	1198:1215	a structural basis for some of the observed microheterogeneity	1198:1259	These findings provide a structural basis for some of the observed microheterogeneity, and have implications with regard to the known functional consequences of the extent of sialylation of plasminogen.
9054441	6	16	theme	novel	928:932	arg1	site					934:937	a novel site	926:937	a novel site for O-linked glycosylation on plasminogen 2 at Ser-248	926:992	In the present study, a combination of trypsin digestion, lectin affinity chromatography, Edman degradation amino acid sequence analysis, carbohydrate composition analysis, and mass spectrometry revealed the existence of a novel site for O-linked glycosylation on plasminogen 2 at Ser-248.
9054441	6	17	theme	chromatography	779:792	arg1	combination					729:739	a combination	727:739	a combination of trypsin digestion, lectin affinity chromatography, Edman degradation amino acid sequence analysis, carbohydrate composition analysis, and mass spectrometry	727:898	In the present study, a combination of trypsin digestion, lectin affinity chromatography, Edman degradation amino acid sequence analysis, carbohydrate composition analysis, and mass spectrometry revealed the existence of a novel site for O-linked glycosylation on plasminogen 2 at Ser-248.
9054441	4	18	theme	further	395:401	arg1	microheterogeneity					419:436	a further well documented microheterogeneity	393:436	a further well documented microheterogeneity dependent on the N-acetylneuraminic acid content, which has functional consequences with regard to activation of plasminogen	393:561	However, plasminogen 2 displays a further well documented microheterogeneity dependent on the N-acetylneuraminic acid content, which has functional consequences with regard to activation of plasminogen.
9054441	3	19	theme	O-linked	324:331	arg1	oligosaccharide					333:347	only an O-linked oligosaccharide	316:347	only an O-linked oligosaccharide	316:347	Plasminogen 2 is known to contain only an O-linked oligosaccharide at Thr-345.
9054441	0	20	from	trisaccharide	41:53	arg1	Ser-248					58:64	Ser-248	58:64	Ser-248 of human plasminogen 2	58:87	Evidence for a novel O-linked sialylated trisaccharide on Ser-248 of human plasminogen 2.
9054441	6	21	theme	sequence	824:831	arg1	analysis					833:840	Edman degradation amino acid sequence analysis	795:840	Edman degradation amino acid sequence analysis	795:840	In the present study, a combination of trypsin digestion, lectin affinity chromatography, Edman degradation amino acid sequence analysis, carbohydrate composition analysis, and mass spectrometry revealed the existence of a novel site for O-linked glycosylation on plasminogen 2 at Ser-248.
9054441	5	22	dep	structure	577:585	arg1	The					564:566	The	564:566	The	564:566	The proposed structure and number of known oligosaccharide linkages in plasminogen 2 is insufficient to account for this microheterogeneity.
9054441	8	23	theme	plasminogen	1365:1375	arg1	sialylation					1350:1360	sialylation	1350:1360	sialylation of plasminogen	1350:1375	These findings provide a structural basis for some of the observed microheterogeneity, and have implications with regard to the known functional consequences of the extent of sialylation of plasminogen.
9054441	6	24	theme	acid	819:822	arg1	sequence					824:831	Edman degradation amino acid sequence	795:831	Edman degradation amino acid sequence analysis	795:840	In the present study, a combination of trypsin digestion, lectin affinity chromatography, Edman degradation amino acid sequence analysis, carbohydrate composition analysis, and mass spectrometry revealed the existence of a novel site for O-linked glycosylation on plasminogen 2 at Ser-248.
9054441	7	25	theme	desialylation	1116:1128	arg1	experiments					1130:1140	desialylation experiments	1116:1140	desialylation experiments	1116:1140	Direct evidence for the structure of the carbohydrate was obtained from a combination of lectin affinity chromatography, desialylation experiments, and mass spectrometry analysis.
9054441	6	26	theme	amino	813:817	arg1	sequence					824:831	Edman degradation amino acid sequence	795:831	Edman degradation amino acid sequence analysis	795:840	In the present study, a combination of trypsin digestion, lectin affinity chromatography, Edman degradation amino acid sequence analysis, carbohydrate composition analysis, and mass spectrometry revealed the existence of a novel site for O-linked glycosylation on plasminogen 2 at Ser-248.
9054441	1	27	theme	major	158:162	arg1	glycoforms					164:173	two major glycoforms	154:173	two major glycoforms	154:173	Human plasminogen, the inactive precursor of plasmin, exists in two major glycoforms.
9054441	6	28	from	Ser-248	986:992	arg1	glycosylation					952:964	O-linked glycosylation	943:964	O-linked glycosylation on plasminogen 2 at Ser-248	943:992	In the present study, a combination of trypsin digestion, lectin affinity chromatography, Edman degradation amino acid sequence analysis, carbohydrate composition analysis, and mass spectrometry revealed the existence of a novel site for O-linked glycosylation on plasminogen 2 at Ser-248.
9054441	7	29	theme	experiments	1130:1140	arg1	combination					1069:1079	a combination	1067:1079	a combination of lectin affinity chromatography, desialylation experiments, and mass spectrometry analysis	1067:1172	Direct evidence for the structure of the carbohydrate was obtained from a combination of lectin affinity chromatography, desialylation experiments, and mass spectrometry analysis.
9054441	6	30	theme	degradation	801:811	arg1	sequence					824:831	Edman degradation amino acid sequence	795:831	Edman degradation amino acid sequence analysis	795:840	In the present study, a combination of trypsin digestion, lectin affinity chromatography, Edman degradation amino acid sequence analysis, carbohydrate composition analysis, and mass spectrometry revealed the existence of a novel site for O-linked glycosylation on plasminogen 2 at Ser-248.
9054441	6	31	theme	present	712:718	arg1	study					720:724	the present study	708:724	the present study	708:724	In the present study, a combination of trypsin digestion, lectin affinity chromatography, Edman degradation amino acid sequence analysis, carbohydrate composition analysis, and mass spectrometry revealed the existence of a novel site for O-linked glycosylation on plasminogen 2 at Ser-248.
9054441	6	32	link	O-linked	943:950	arg1	glycosylation					952:964	O-linked glycosylation	943:964	O-linked glycosylation on plasminogen 2 at Ser-248	943:992	In the present study, a combination of trypsin digestion, lectin affinity chromatography, Edman degradation amino acid sequence analysis, carbohydrate composition analysis, and mass spectrometry revealed the existence of a novel site for O-linked glycosylation on plasminogen 2 at Ser-248.
9054441	0	33	theme	novel	15:19	arg1	trisaccharide					41:53	a novel O-linked sialylated trisaccharide	13:53	a novel O-linked sialylated trisaccharide on Ser-248 of human plasminogen 2	13:87	Evidence for a novel O-linked sialylated trisaccharide on Ser-248 of human plasminogen 2.
9054441	7	34	theme	chromatography	1100:1113	arg1	combination					1069:1079	a combination	1067:1079	a combination of lectin affinity chromatography, desialylation experiments, and mass spectrometry analysis	1067:1172	Direct evidence for the structure of the carbohydrate was obtained from a combination of lectin affinity chromatography, desialylation experiments, and mass spectrometry analysis.
9054441	0	35	link	O-linked	21:28	arg1	trisaccharide					41:53	a novel O-linked sialylated trisaccharide	13:53	a novel O-linked sialylated trisaccharide on Ser-248 of human plasminogen 2	13:87	Evidence for a novel O-linked sialylated trisaccharide on Ser-248 of human plasminogen 2.
9054441	1	36	theme	Human	90:94	arg1	precursor					122:130	the inactive precursor	109:130	the inactive precursor of plasmin	109:141	Human plasminogen, the inactive precursor of plasmin, exists in two major glycoforms.
9054441	1	36	theme	Human	90:94	arg1	plasminogen					96:106	Human plasminogen	90:106	Human plasminogen	90:106	Human plasminogen, the inactive precursor of plasmin, exists in two major glycoforms.
9054441	6	37	theme	carbohydrate	843:854	arg1	analysis					868:875	carbohydrate composition analysis	843:875	carbohydrate composition analysis	843:875	In the present study, a combination of trypsin digestion, lectin affinity chromatography, Edman degradation amino acid sequence analysis, carbohydrate composition analysis, and mass spectrometry revealed the existence of a novel site for O-linked glycosylation on plasminogen 2 at Ser-248.
9054441	8	38	theme	functional	1309:1318	arg1	consequences					1320:1331	the known functional consequences	1299:1331	the known functional consequences of the extent of sialylation of plasminogen	1299:1375	These findings provide a structural basis for some of the observed microheterogeneity, and have implications with regard to the known functional consequences of the extent of sialylation of plasminogen.
9054441	8	39	theme	observed	1233:1240	arg1	microheterogeneity					1242:1259	the observed microheterogeneity	1229:1259	the observed microheterogeneity	1229:1259	These findings provide a structural basis for some of the observed microheterogeneity, and have implications with regard to the known functional consequences of the extent of sialylation of plasminogen.
9054441	6	40	theme	affinity	770:777	arg1	chromatography					779:792	lectin affinity chromatography	763:792	lectin affinity chromatography	763:792	In the present study, a combination of trypsin digestion, lectin affinity chromatography, Edman degradation amino acid sequence analysis, carbohydrate composition analysis, and mass spectrometry revealed the existence of a novel site for O-linked glycosylation on plasminogen 2 at Ser-248.
9054441	6	41	theme	O-linked	943:950	arg1	glycosylation					952:964	O-linked glycosylation	943:964	O-linked glycosylation on plasminogen 2 at Ser-248	943:992	In the present study, a combination of trypsin digestion, lectin affinity chromatography, Edman degradation amino acid sequence analysis, carbohydrate composition analysis, and mass spectrometry revealed the existence of a novel site for O-linked glycosylation on plasminogen 2 at Ser-248.
9054441	5	42	from	structure	577:585	arg1	plasminogen					635:645	plasminogen 2	635:647	plasminogen 2	635:647	The proposed structure and number of known oligosaccharide linkages in plasminogen 2 is insufficient to account for this microheterogeneity.
9054441	0	43	theme	sialylated	30:39	arg1	trisaccharide					41:53	a novel O-linked sialylated trisaccharide	13:53	a novel O-linked sialylated trisaccharide on Ser-248 of human plasminogen 2	13:87	Evidence for a novel O-linked sialylated trisaccharide on Ser-248 of human plasminogen 2.
9054441	7	44	theme	lectin	1084:1089	arg1	chromatography					1100:1113	lectin affinity chromatography	1084:1113	lectin affinity chromatography	1084:1113	Direct evidence for the structure of the carbohydrate was obtained from a combination of lectin affinity chromatography, desialylation experiments, and mass spectrometry analysis.
9054441	8	45	contain	have	1266:1269	arg2	implications					1271:1282	implications	1271:1282	implications with regard to the known functional consequences of the extent of sialylation of plasminogen	1271:1375	These findings provide a structural basis for some of the observed microheterogeneity, and have implications with regard to the known functional consequences of the extent of sialylation of plasminogen.
9054441	8	45	contain	have	1266:1269	arg1	findings					1181:1188	These findings	1175:1188	These findings	1175:1188	These findings provide a structural basis for some of the observed microheterogeneity, and have implications with regard to the known functional consequences of the extent of sialylation of plasminogen.
9054441	0	46	theme	O-linked	21:28	arg1	trisaccharide					41:53	a novel O-linked sialylated trisaccharide	13:53	a novel O-linked sialylated trisaccharide on Ser-248 of human plasminogen 2	13:87	Evidence for a novel O-linked sialylated trisaccharide on Ser-248 of human plasminogen 2.
9054441	7	47	theme	affinity	1091:1098	arg1	chromatography					1100:1113	lectin affinity chromatography	1084:1113	lectin affinity chromatography	1084:1113	Direct evidence for the structure of the carbohydrate was obtained from a combination of lectin affinity chromatography, desialylation experiments, and mass spectrometry analysis.
9054441	4	48	theme	acid	474:477	arg1	content					479:485	the N-acetylneuraminic acid content	451:485	the N-acetylneuraminic acid content	451:485	However, plasminogen 2 displays a further well documented microheterogeneity dependent on the N-acetylneuraminic acid content, which has functional consequences with regard to activation of plasminogen.
9054441	2	49	contain	contains	190:197	arg1	Plasminogen					176:186	Plasminogen 1	176:188	Plasminogen 1	176:188	Plasminogen 1 contains an N-linked oligosaccharide at Asn-289 and an O-linked oligosaccharide at Thr-345.
9054441	2	49	contain	contains	190:197	arg2	Plasminogen					176:186	Plasminogen 1	176:188	Plasminogen 1	176:188	Plasminogen 1 contains an N-linked oligosaccharide at Asn-289 and an O-linked oligosaccharide at Thr-345.
9054441	2	49	contain	contains	190:197	arg1	oligosaccharide					254:268	an O-linked oligosaccharide	242:268	an O-linked oligosaccharide at Thr-345	242:279	Plasminogen 1 contains an N-linked oligosaccharide at Asn-289 and an O-linked oligosaccharide at Thr-345.
9054441	2	49	contain	contains	190:197	arg1	Asn-289					230:236	Asn-289	230:236	Asn-289	230:236	Plasminogen 1 contains an N-linked oligosaccharide at Asn-289 and an O-linked oligosaccharide at Thr-345.
9054441	2	49	contain	contains	190:197	arg2	oligosaccharide					211:225	an N-linked oligosaccharide	199:225	an N-linked oligosaccharide	199:225	Plasminogen 1 contains an N-linked oligosaccharide at Asn-289 and an O-linked oligosaccharide at Thr-345.
9054441	6	50	theme	analysis	833:840	arg1	combination					729:739	a combination	727:739	a combination of trypsin digestion, lectin affinity chromatography, Edman degradation amino acid sequence analysis, carbohydrate composition analysis, and mass spectrometry	727:898	In the present study, a combination of trypsin digestion, lectin affinity chromatography, Edman degradation amino acid sequence analysis, carbohydrate composition analysis, and mass spectrometry revealed the existence of a novel site for O-linked glycosylation on plasminogen 2 at Ser-248.
9054441	4	51	theme	N-acetylneuraminic	455:472	arg1	content					479:485	the N-acetylneuraminic acid content	451:485	the N-acetylneuraminic acid content	451:485	However, plasminogen 2 displays a further well documented microheterogeneity dependent on the N-acetylneuraminic acid content, which has functional consequences with regard to activation of plasminogen.
9054441	2	52	theme	N-linked	202:209	arg1	oligosaccharide					211:225	an N-linked oligosaccharide	199:225	an N-linked oligosaccharide	199:225	Plasminogen 1 contains an N-linked oligosaccharide at Asn-289 and an O-linked oligosaccharide at Thr-345.
9054441	6	53	theme	Edman	795:799	arg1	sequence					824:831	Edman degradation amino acid sequence	795:831	Edman degradation amino acid sequence analysis	795:840	In the present study, a combination of trypsin digestion, lectin affinity chromatography, Edman degradation amino acid sequence analysis, carbohydrate composition analysis, and mass spectrometry revealed the existence of a novel site for O-linked glycosylation on plasminogen 2 at Ser-248.
9054441	8	54	theme	extent	1340:1345	arg1	consequences					1320:1331	the known functional consequences	1299:1331	the known functional consequences of the extent of sialylation of plasminogen	1299:1375	These findings provide a structural basis for some of the observed microheterogeneity, and have implications with regard to the known functional consequences of the extent of sialylation of plasminogen.
9054441	8	55	gly	sialylation	1350:1360	arg1	plasminogen					1365:1375	plasminogen	1365:1375	plasminogen	1365:1375	These findings provide a structural basis for some of the observed microheterogeneity, and have implications with regard to the known functional consequences of the extent of sialylation of plasminogen.
9054441	4	56	theme	plasminogen	551:561	arg1	activation					537:546	activation	537:546	activation of plasminogen	537:561	However, plasminogen 2 displays a further well documented microheterogeneity dependent on the N-acetylneuraminic acid content, which has functional consequences with regard to activation of plasminogen.
9054441	4	57	theme	documented	408:417	arg1	microheterogeneity					419:436	a further well documented microheterogeneity	393:436	a further well documented microheterogeneity dependent on the N-acetylneuraminic acid content, which has functional consequences with regard to activation of plasminogen	393:561	However, plasminogen 2 displays a further well documented microheterogeneity dependent on the N-acetylneuraminic acid content, which has functional consequences with regard to activation of plasminogen.
9054441	5	58	theme	proposed	568:575	arg1	structure					577:585	proposed structure	568:585	proposed structure	568:585	The proposed structure and number of known oligosaccharide linkages in plasminogen 2 is insufficient to account for this microheterogeneity.
9054441	4	59	contain	has	494:496	arg1	content					479:485	the N-acetylneuraminic acid content	451:485	the N-acetylneuraminic acid content	451:485	However, plasminogen 2 displays a further well documented microheterogeneity dependent on the N-acetylneuraminic acid content, which has functional consequences with regard to activation of plasminogen.
9054441	4	59	contain	has	494:496	arg2	consequences					509:520	functional consequences	498:520	functional consequences	498:520	However, plasminogen 2 displays a further well documented microheterogeneity dependent on the N-acetylneuraminic acid content, which has functional consequences with regard to activation of plasminogen.
9054441	5	60	theme	known	601:605	arg1	linkages					623:630	known oligosaccharide linkages	601:630	known oligosaccharide linkages	601:630	The proposed structure and number of known oligosaccharide linkages in plasminogen 2 is insufficient to account for this microheterogeneity.
9054441	2	61	theme	O-linked	245:252	arg1	oligosaccharide					254:268	an O-linked oligosaccharide	242:268	an O-linked oligosaccharide at Thr-345	242:279	Plasminogen 1 contains an N-linked oligosaccharide at Asn-289 and an O-linked oligosaccharide at Thr-345.
9054441	6	62	theme	lectin	763:768	arg1	chromatography					779:792	lectin affinity chromatography	763:792	lectin affinity chromatography	763:792	In the present study, a combination of trypsin digestion, lectin affinity chromatography, Edman degradation amino acid sequence analysis, carbohydrate composition analysis, and mass spectrometry revealed the existence of a novel site for O-linked glycosylation on plasminogen 2 at Ser-248.
9054441	1	63	theme	inactive	113:120	arg1	precursor					122:130	the inactive precursor	109:130	the inactive precursor of plasmin	109:141	Human plasminogen, the inactive precursor of plasmin, exists in two major glycoforms.
9054441	1	63	theme	inactive	113:120	arg1	plasminogen					96:106	Human plasminogen	90:106	Human plasminogen	90:106	Human plasminogen, the inactive precursor of plasmin, exists in two major glycoforms.
9054441	2	64	link	N-linked	202:209	arg1	oligosaccharide					211:225	an N-linked oligosaccharide	199:225	an N-linked oligosaccharide	199:225	Plasminogen 1 contains an N-linked oligosaccharide at Asn-289 and an O-linked oligosaccharide at Thr-345.
9054441	7	65	theme	carbohydrate	1036:1047	arg1	structure					1019:1027	the structure	1015:1027	the structure of the carbohydrate	1015:1047	Direct evidence for the structure of the carbohydrate was obtained from a combination of lectin affinity chromatography, desialylation experiments, and mass spectrometry analysis.
9054441	4	66	theme	dependent	438:446	arg1	microheterogeneity					419:436	a further well documented microheterogeneity	393:436	a further well documented microheterogeneity dependent on the N-acetylneuraminic acid content, which has functional consequences with regard to activation of plasminogen	393:561	However, plasminogen 2 displays a further well documented microheterogeneity dependent on the N-acetylneuraminic acid content, which has functional consequences with regard to activation of plasminogen.
9054441	0	67	gly	sialylated	30:39	arg1	trisaccharide					41:53	a novel O-linked sialylated trisaccharide	13:53	a novel O-linked sialylated trisaccharide on Ser-248 of human plasminogen 2	13:87	Evidence for a novel O-linked sialylated trisaccharide on Ser-248 of human plasminogen 2.
9054441	3	68	contain	contain	308:314	arg2	oligosaccharide					333:347	only an O-linked oligosaccharide	316:347	only an O-linked oligosaccharide	316:347	Plasminogen 2 is known to contain only an O-linked oligosaccharide at Thr-345.
9054441	3	68	contain	contain	308:314	arg2	Plasminogen					282:292	Plasminogen 2	282:294	Plasminogen 2	282:294	Plasminogen 2 is known to contain only an O-linked oligosaccharide at Thr-345.
9054441	3	68	contain	contain	308:314	arg1	Plasminogen					282:292	Plasminogen 2	282:294	Plasminogen 2	282:294	Plasminogen 2 is known to contain only an O-linked oligosaccharide at Thr-345.
9054441	3	68	contain	contain	308:314	arg1	Thr-345					352:358	Thr-345	352:358	Thr-345	352:358	Plasminogen 2 is known to contain only an O-linked oligosaccharide at Thr-345.
9054441	5	69	from	number	591:596	arg1	plasminogen					635:645	plasminogen 2	635:647	plasminogen 2	635:647	The proposed structure and number of known oligosaccharide linkages in plasminogen 2 is insufficient to account for this microheterogeneity.
9054441	8	70	theme	sialylation	1350:1360	arg1	extent					1340:1345	the extent	1336:1345	the extent of sialylation of plasminogen	1336:1375	These findings provide a structural basis for some of the observed microheterogeneity, and have implications with regard to the known functional consequences of the extent of sialylation of plasminogen.
9054441	6	71	theme	composition	856:866	arg1	analysis					868:875	carbohydrate composition analysis	843:875	carbohydrate composition analysis	843:875	In the present study, a combination of trypsin digestion, lectin affinity chromatography, Edman degradation amino acid sequence analysis, carbohydrate composition analysis, and mass spectrometry revealed the existence of a novel site for O-linked glycosylation on plasminogen 2 at Ser-248.
9054441	6	72	theme	digestion	752:760	arg1	combination					729:739	a combination	727:739	a combination of trypsin digestion, lectin affinity chromatography, Edman degradation amino acid sequence analysis, carbohydrate composition analysis, and mass spectrometry	727:898	In the present study, a combination of trypsin digestion, lectin affinity chromatography, Edman degradation amino acid sequence analysis, carbohydrate composition analysis, and mass spectrometry revealed the existence of a novel site for O-linked glycosylation on plasminogen 2 at Ser-248.
9054441	7	73	theme	Direct	995:1000	arg1	evidence					1002:1009	Direct evidence	995:1009	Direct evidence for the structure of the carbohydrate	995:1047	Direct evidence for the structure of the carbohydrate was obtained from a combination of lectin affinity chromatography, desialylation experiments, and mass spectrometry analysis.
9054441	2	74	from	Thr-345	273:279	arg1	oligosaccharide					254:268	an O-linked oligosaccharide	242:268	an O-linked oligosaccharide at Thr-345	242:279	Plasminogen 1 contains an N-linked oligosaccharide at Asn-289 and an O-linked oligosaccharide at Thr-345.
9054441	2	74	from	Thr-345	273:279	arg1	Asn-289					230:236	Asn-289	230:236	Asn-289	230:236	Plasminogen 1 contains an N-linked oligosaccharide at Asn-289 and an O-linked oligosaccharide at Thr-345.
9054441	8	75	theme	known	1303:1307	arg1	consequences					1320:1331	the known functional consequences	1299:1331	the known functional consequences of the extent of sialylation of plasminogen	1299:1375	These findings provide a structural basis for some of the observed microheterogeneity, and have implications with regard to the known functional consequences of the extent of sialylation of plasminogen.
9054441	6	76	theme	trypsin	744:750	arg1	digestion					752:760	trypsin digestion	744:760	trypsin digestion	744:760	In the present study, a combination of trypsin digestion, lectin affinity chromatography, Edman degradation amino acid sequence analysis, carbohydrate composition analysis, and mass spectrometry revealed the existence of a novel site for O-linked glycosylation on plasminogen 2 at Ser-248.
9054441	1	77	theme	plasmin	135:141	arg1	precursor					122:130	the inactive precursor	109:130	the inactive precursor of plasmin	109:141	Human plasminogen, the inactive precursor of plasmin, exists in two major glycoforms.
9054441	1	77	theme	plasmin	135:141	arg1	plasminogen					96:106	Human plasminogen	90:106	Human plasminogen	90:106	Human plasminogen, the inactive precursor of plasmin, exists in two major glycoforms.
9054441	6	78	from	glycosylation	952:964	arg1	plasminogen					969:979	plasminogen 2	969:981	plasminogen 2	969:981	In the present study, a combination of trypsin digestion, lectin affinity chromatography, Edman degradation amino acid sequence analysis, carbohydrate composition analysis, and mass spectrometry revealed the existence of a novel site for O-linked glycosylation on plasminogen 2 at Ser-248.
8323299	6	0	theme	amino	875:879	arg1	sequences					886:894	The amino acid sequences	871:894	The amino acid sequences of these O-glycosylation sites	871:925	The amino acid sequences of these O-glycosylation sites are consistent with the previous reports that residues at positions -1 and +3 may influence the glycosylation reaction.
8323299	6	0	theme	amino	875:879	arg1	consistent					931:940	consistent	931:940	consistent	931:940	The amino acid sequences of these O-glycosylation sites are consistent with the previous reports that residues at positions -1 and +3 may influence the glycosylation reaction.
8323299	7	1	theme	lamp-1	1218:1223	arg1	lamp-1					1218:1223	lamp-1	1218:1223	lamp-1	1218:1223	Circular dichroism and nuclear magnetic resonance spectroscopy was used for the structural characterization of a synthetic peptide corresponding to residues 167 to 190 of lamp-1.
8323299	7	1	theme	lamp-1	1218:1223	arg1	residues					1195:1202	residues 167 to 190	1195:1213	residues 167 to 190 of lamp-1	1195:1223	Circular dichroism and nuclear magnetic resonance spectroscopy was used for the structural characterization of a synthetic peptide corresponding to residues 167 to 190 of lamp-1.
8323299	2	2	theme	O-linked	351:358	arg1	oligosaccharides					360:375	O-linked oligosaccharides	351:375	O-linked oligosaccharides	351:375	In the present paper, we report the localization of O-linked oligosaccharides exclusively to the hinge-like regions of lamp-1 and lamp-2 isolated from human chronic myelogenous leukemia cells.
8323299	1	3	theme	N-linked	271:278	arg1	type					293:296	both N-linked and O-linked type	266:296	both N-linked and O-linked type	266:296	The lysosomal membrane glycoproteins lamp-1 and lamp-2 are extensively glycosylated with a variety of different carbohydrate structures of both N-linked and O-linked type.
8323299	7	4	theme	resonance	1087:1095	arg1	spectroscopy					1097:1108	Circular dichroism and nuclear magnetic resonance spectroscopy	1047:1108	Circular dichroism and nuclear magnetic resonance spectroscopy	1047:1108	Circular dichroism and nuclear magnetic resonance spectroscopy was used for the structural characterization of a synthetic peptide corresponding to residues 167 to 190 of lamp-1.
8323299	1	5	theme	O-linked	284:291	arg1	type					293:296	both N-linked and O-linked type	266:296	both N-linked and O-linked type	266:296	The lysosomal membrane glycoproteins lamp-1 and lamp-2 are extensively glycosylated with a variety of different carbohydrate structures of both N-linked and O-linked type.
8323299	7	6	theme	nuclear	1070:1076	arg1	resonance					1087:1095	nuclear magnetic resonance	1070:1095	nuclear magnetic resonance	1070:1095	Circular dichroism and nuclear magnetic resonance spectroscopy was used for the structural characterization of a synthetic peptide corresponding to residues 167 to 190 of lamp-1.
8323299	6	7	from	+3	1002:1003	arg1	residues					973:980	residues	973:980	residues at positions -1 and +3	973:1003	The amino acid sequences of these O-glycosylation sites are consistent with the previous reports that residues at positions -1 and +3 may influence the glycosylation reaction.
8323299	11	8	theme	typical	1775:1781	arg1	structure					1791:1799	any typical ordered structure	1771:1799	any typical ordered structure	1771:1799	These results, taken together, strongly suggest that a hinge region does not display any typical ordered structure.
8323299	7	9	theme	dichroism	1056:1064	arg1	spectroscopy					1097:1108	Circular dichroism and nuclear magnetic resonance spectroscopy	1047:1108	Circular dichroism and nuclear magnetic resonance spectroscopy	1047:1108	Circular dichroism and nuclear magnetic resonance spectroscopy was used for the structural characterization of a synthetic peptide corresponding to residues 167 to 190 of lamp-1.
8323299	2	10	theme	present	306:312	arg1	paper					314:318	the present paper	302:318	the present paper	302:318	In the present paper, we report the localization of O-linked oligosaccharides exclusively to the hinge-like regions of lamp-1 and lamp-2 isolated from human chronic myelogenous leukemia cells.
8323299	6	11	theme	sites	921:925	arg1	sequences					886:894	The amino acid sequences	871:894	The amino acid sequences of these O-glycosylation sites	871:925	The amino acid sequences of these O-glycosylation sites are consistent with the previous reports that residues at positions -1 and +3 may influence the glycosylation reaction.
8323299	6	11	theme	sites	921:925	arg1	consistent					931:940	consistent	931:940	consistent	931:940	The amino acid sequences of these O-glycosylation sites are consistent with the previous reports that residues at positions -1 and +3 may influence the glycosylation reaction.
8323299	8	12	theme	proline-rich	1257:1268	arg1	region					1288:1293	the proline-rich O-glycan acceptor region	1253:1293	the proline-rich O-glycan acceptor region	1253:1293	The results indicated that the proline-rich O-glycan acceptor region does not adopt any typical periodic structure but differs from random-coil structure.
8323299	10	13	theme	magnetic	1602:1609	arg1	resonance					1611:1619	the nuclear magnetic resonance	1590:1619	the nuclear magnetic resonance time scale	1590:1630	A significant conformational variability was observed in this region, presumably due to a slow (on the nuclear magnetic resonance time scale) cis-trans isomerization of several proline residues.
8323299	5	14	from	Ser-167	724:730	arg1	Ser-179					820:826	Ser-179	820:826	Ser-179	820:826	In lamp-2, complete glycosylation was found at Ser-167, Thr-168, Thr-172, Thr-175, Thr-176, Thr-182, and Thr-183, and partial glycosylation at Ser-179 and Thr-181, and possibly also at Thr-185.
8323299	9	15	theme	porcine	1460:1466	arg1	apomucin					1481:1488	porcine submaxillary apomucin	1460:1488	porcine submaxillary apomucin	1460:1488	The circular dichroism spectrum of the peptide is, however, similar to that of porcine submaxillary apomucin.
8323299	8	16	theme	acceptor	1279:1286	arg1	region					1288:1293	the proline-rich O-glycan acceptor region	1253:1293	the proline-rich O-glycan acceptor region	1253:1293	The results indicated that the proline-rich O-glycan acceptor region does not adopt any typical periodic structure but differs from random-coil structure.
8323299	5	17	from	Thr-175	751:757	arg1	Ser-179					820:826	Ser-179	820:826	Ser-179	820:826	In lamp-2, complete glycosylation was found at Ser-167, Thr-168, Thr-172, Thr-175, Thr-176, Thr-182, and Thr-183, and partial glycosylation at Ser-179 and Thr-181, and possibly also at Thr-185.
8323299	4	18	gly	glycosylated	663:674	arg1	Ser-169					641:647	Ser-169	641:647	Ser-169	641:647	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	6	19	gly	O-glycosylation	905:919	arg2	sites					921:925	these O-glycosylation sites	899:925	these O-glycosylation sites	899:925	The amino acid sequences of these O-glycosylation sites are consistent with the previous reports that residues at positions -1 and +3 may influence the glycosylation reaction.
8323299	10	20	located	observed	1536:1543	arg1	region					1553:1558	this region	1548:1558	this region	1548:1558	A significant conformational variability was observed in this region, presumably due to a slow (on the nuclear magnetic resonance time scale) cis-trans isomerization of several proline residues.
8323299	10	20	located	observed	1536:1543	arg2	variability					1520:1530	A significant conformational variability	1491:1530	A significant conformational variability	1491:1530	A significant conformational variability was observed in this region, presumably due to a slow (on the nuclear magnetic resonance time scale) cis-trans isomerization of several proline residues.
8323299	5	21	theme	complete	688:695	arg1	glycosylation					697:709	complete glycosylation	688:709	complete glycosylation	688:709	In lamp-2, complete glycosylation was found at Ser-167, Thr-168, Thr-172, Thr-175, Thr-176, Thr-182, and Thr-183, and partial glycosylation at Ser-179 and Thr-181, and possibly also at Thr-185.
8323299	5	22	from	Thr-172	742:748	arg1	Ser-179					820:826	Ser-179	820:826	Ser-179	820:826	In lamp-2, complete glycosylation was found at Ser-167, Thr-168, Thr-172, Thr-175, Thr-176, Thr-182, and Thr-183, and partial glycosylation at Ser-179 and Thr-181, and possibly also at Thr-185.
8323299	1	23	theme	lysosomal	131:139	arg1	glycoproteins					150:162	The lysosomal membrane glycoproteins	127:162	The lysosomal membrane glycoproteins lamp-1 and lamp-2	127:180	The lysosomal membrane glycoproteins lamp-1 and lamp-2 are extensively glycosylated with a variety of different carbohydrate structures of both N-linked and O-linked type.
8323299	1	23	theme	lysosomal	131:139	arg1	lamp-2					175:180	lamp-2	175:180	lamp-2	175:180	The lysosomal membrane glycoproteins lamp-1 and lamp-2 are extensively glycosylated with a variety of different carbohydrate structures of both N-linked and O-linked type.
8323299	1	23	theme	lysosomal	131:139	arg1	lamp-1					164:169	lamp-1	164:169	lamp-1	164:169	The lysosomal membrane glycoproteins lamp-1 and lamp-2 are extensively glycosylated with a variety of different carbohydrate structures of both N-linked and O-linked type.
8323299	5	24	from	Thr-182	769:775	arg1	Ser-179					820:826	Ser-179	820:826	Ser-179	820:826	In lamp-2, complete glycosylation was found at Ser-167, Thr-168, Thr-172, Thr-175, Thr-176, Thr-182, and Thr-183, and partial glycosylation at Ser-179 and Thr-181, and possibly also at Thr-185.
8323299	8	25	theme	typical	1314:1320	arg1	structure					1331:1339	any typical periodic structure	1310:1339	any typical periodic structure	1310:1339	The results indicated that the proline-rich O-glycan acceptor region does not adopt any typical periodic structure but differs from random-coil structure.
8323299	0	26	theme	human	69:73	arg1	glycoproteins					94:106	human lysosomal membrane glycoproteins lamp-1 and lamp-2	69:124	human lysosomal membrane glycoproteins lamp-1 and lamp-2	69:124	Assignment of O-glycan attachment sites to the hinge-like regions of human lysosomal membrane glycoproteins lamp-1 and lamp-2.
8323299	0	26	theme	human	69:73	arg1	lamp-2					119:124	lamp-2	119:124	lamp-2	119:124	Assignment of O-glycan attachment sites to the hinge-like regions of human lysosomal membrane glycoproteins lamp-1 and lamp-2.
8323299	0	26	theme	human	69:73	arg1	lamp-1					108:113	lamp-1	108:113	lamp-1	108:113	Assignment of O-glycan attachment sites to the hinge-like regions of human lysosomal membrane glycoproteins lamp-1 and lamp-2.
8323299	5	27	from	Thr-176	760:766	arg1	Ser-179					820:826	Ser-179	820:826	Ser-179	820:826	In lamp-2, complete glycosylation was found at Ser-167, Thr-168, Thr-172, Thr-175, Thr-176, Thr-182, and Thr-183, and partial glycosylation at Ser-179 and Thr-181, and possibly also at Thr-185.
8323299	6	28	dep	reports	960:966	arg1	influence					1009:1017	influence	1009:1017	may influence the glycosylation reaction	1005:1044	The amino acid sequences of these O-glycosylation sites are consistent with the previous reports that residues at positions -1 and +3 may influence the glycosylation reaction.
8323299	11	29	theme	hinge	1741:1745	arg1	region					1747:1752	a hinge region	1739:1752	a hinge region	1739:1752	These results, taken together, strongly suggest that a hinge region does not display any typical ordered structure.
8323299	0	30	theme	membrane	85:92	arg1	glycoproteins					94:106	human lysosomal membrane glycoproteins lamp-1 and lamp-2	69:124	human lysosomal membrane glycoproteins lamp-1 and lamp-2	69:124	Assignment of O-glycan attachment sites to the hinge-like regions of human lysosomal membrane glycoproteins lamp-1 and lamp-2.
8323299	0	30	theme	membrane	85:92	arg1	lamp-2					119:124	lamp-2	119:124	lamp-2	119:124	Assignment of O-glycan attachment sites to the hinge-like regions of human lysosomal membrane glycoproteins lamp-1 and lamp-2.
8323299	0	30	theme	membrane	85:92	arg1	lamp-1					108:113	lamp-1	108:113	lamp-1	108:113	Assignment of O-glycan attachment sites to the hinge-like regions of human lysosomal membrane glycoproteins lamp-1 and lamp-2.
8323299	10	31	theme	several	1660:1666	arg1	residues					1676:1683	several proline residues	1660:1683	several proline residues	1660:1683	A significant conformational variability was observed in this region, presumably due to a slow (on the nuclear magnetic resonance time scale) cis-trans isomerization of several proline residues.
8323299	10	32	theme	cis-trans	1633:1641	arg1	isomerization					1643:1655	a slow (on the nuclear magnetic resonance time scale) cis-trans isomerization	1579:1655	a slow (on the nuclear magnetic resonance time scale) cis-trans isomerization of several proline residues	1579:1683	A significant conformational variability was observed in this region, presumably due to a slow (on the nuclear magnetic resonance time scale) cis-trans isomerization of several proline residues.
8323299	12	33	theme	intralumenal	1866:1877	arg1	proteases					1889:1897	intralumenal lysosomal proteases	1866:1897	intralumenal lysosomal proteases	1866:1897	The presence of O-glycans thus likely protects this region from intralumenal lysosomal proteases.
8323299	2	34	theme	myelogenous	464:474	arg1	leukemia					476:483	chronic myelogenous leukemia	456:483	human chronic myelogenous leukemia cells	450:489	In the present paper, we report the localization of O-linked oligosaccharides exclusively to the hinge-like regions of lamp-1 and lamp-2 isolated from human chronic myelogenous leukemia cells.
8323299	8	35	theme	random-coil	1358:1368	arg1	structure					1370:1378	random-coil structure	1358:1378	random-coil structure	1358:1378	The results indicated that the proline-rich O-glycan acceptor region does not adopt any typical periodic structure but differs from random-coil structure.
8323299	2	36	theme	hinge-like	396:405	arg1	regions					407:413	the hinge-like regions	392:413	the hinge-like regions of lamp-1 and lamp-2 isolated from human chronic myelogenous leukemia cells	392:489	In the present paper, we report the localization of O-linked oligosaccharides exclusively to the hinge-like regions of lamp-1 and lamp-2 isolated from human chronic myelogenous leukemia cells.
8323299	7	37	theme	synthetic	1160:1168	arg1	peptide					1170:1176	a synthetic peptide	1158:1176	a synthetic peptide corresponding to residues 167 to 190 of lamp-1	1158:1223	Circular dichroism and nuclear magnetic resonance spectroscopy was used for the structural characterization of a synthetic peptide corresponding to residues 167 to 190 of lamp-1.
8323299	1	38	theme	type	293:296	arg1	structures					252:261	different carbohydrate structures	229:261	different carbohydrate structures of both N-linked and O-linked type	229:296	The lysosomal membrane glycoproteins lamp-1 and lamp-2 are extensively glycosylated with a variety of different carbohydrate structures of both N-linked and O-linked type.
8323299	0	39	gly	glycoproteins	94:106	arg1	glycoproteins					94:106	human lysosomal membrane glycoproteins lamp-1 and lamp-2	69:124	human lysosomal membrane glycoproteins lamp-1 and lamp-2	69:124	Assignment of O-glycan attachment sites to the hinge-like regions of human lysosomal membrane glycoproteins lamp-1 and lamp-2.
8323299	0	39	gly	glycoproteins	94:106	arg1	lamp-2					119:124	lamp-2	119:124	lamp-2	119:124	Assignment of O-glycan attachment sites to the hinge-like regions of human lysosomal membrane glycoproteins lamp-1 and lamp-2.
8323299	0	39	gly	glycoproteins	94:106	arg1	lamp-1					108:113	lamp-1	108:113	lamp-1	108:113	Assignment of O-glycan attachment sites to the hinge-like regions of human lysosomal membrane glycoproteins lamp-1 and lamp-2.
8323299	2	40	theme	human	450:454	arg1	cells					485:489	human chronic myelogenous leukemia cells	450:489	human chronic myelogenous leukemia cells	450:489	In the present paper, we report the localization of O-linked oligosaccharides exclusively to the hinge-like regions of lamp-1 and lamp-2 isolated from human chronic myelogenous leukemia cells.
8323299	3	41	gly	glycoproteins	500:512	arg1	glycoproteins					500:512	both glycoproteins	495:512	both glycoproteins	495:512	In both glycoproteins, the O-glycans appear in clusters.
8323299	10	42	theme	proline	1668:1674	arg1	residues					1676:1683	several proline residues	1660:1683	several proline residues	1660:1683	A significant conformational variability was observed in this region, presumably due to a slow (on the nuclear magnetic resonance time scale) cis-trans isomerization of several proline residues.
8323299	0	43	theme	O-glycan	14:21	arg1	sites					34:38	O-glycan attachment sites	14:38	O-glycan attachment sites	14:38	Assignment of O-glycan attachment sites to the hinge-like regions of human lysosomal membrane glycoproteins lamp-1 and lamp-2.
8323299	0	44	theme	sites	34:38	arg1	Assignment					0:9	Assignment	0:9	Assignment of O-glycan attachment sites to the hinge-like regions of human lysosomal membrane glycoproteins lamp-1 and lamp-2	0:124	Assignment of O-glycan attachment sites to the hinge-like regions of human lysosomal membrane glycoproteins lamp-1 and lamp-2.
8323299	7	45	theme	structural	1127:1136	arg1	characterization					1138:1153	the structural characterization	1123:1153	the structural characterization of a synthetic peptide corresponding to residues 167 to 190 of lamp-1	1123:1223	Circular dichroism and nuclear magnetic resonance spectroscopy was used for the structural characterization of a synthetic peptide corresponding to residues 167 to 190 of lamp-1.
8323299	7	46	used	used	1114:1117	arg2	spectroscopy					1097:1108	Circular dichroism and nuclear magnetic resonance spectroscopy	1047:1108	Circular dichroism and nuclear magnetic resonance spectroscopy	1047:1108	Circular dichroism and nuclear magnetic resonance spectroscopy was used for the structural characterization of a synthetic peptide corresponding to residues 167 to 190 of lamp-1.
8323299	10	47	theme	conformational	1505:1518	arg1	variability					1520:1530	A significant conformational variability	1491:1530	A significant conformational variability	1491:1530	A significant conformational variability was observed in this region, presumably due to a slow (on the nuclear magnetic resonance time scale) cis-trans isomerization of several proline residues.
8323299	1	48	theme	different	229:237	arg1	structures					252:261	different carbohydrate structures	229:261	different carbohydrate structures of both N-linked and O-linked type	229:296	The lysosomal membrane glycoproteins lamp-1 and lamp-2 are extensively glycosylated with a variety of different carbohydrate structures of both N-linked and O-linked type.
8323299	7	49	theme	magnetic	1078:1085	arg1	resonance					1087:1095	nuclear magnetic resonance	1070:1095	nuclear magnetic resonance	1070:1095	Circular dichroism and nuclear magnetic resonance spectroscopy was used for the structural characterization of a synthetic peptide corresponding to residues 167 to 190 of lamp-1.
8323299	1	50	theme	structures	252:261	arg1	structures					252:261	different carbohydrate structures	229:261	different carbohydrate structures of both N-linked and O-linked type	229:296	The lysosomal membrane glycoproteins lamp-1 and lamp-2 are extensively glycosylated with a variety of different carbohydrate structures of both N-linked and O-linked type.
8323299	1	50	theme	structures	252:261	arg1	variety					218:224	a variety	216:224	a variety of different carbohydrate structures of both N-linked and O-linked type	216:296	The lysosomal membrane glycoproteins lamp-1 and lamp-2 are extensively glycosylated with a variety of different carbohydrate structures of both N-linked and O-linked type.
8323299	6	51	theme	acid	881:884	arg1	sequences					886:894	The amino acid sequences	871:894	The amino acid sequences of these O-glycosylation sites	871:925	The amino acid sequences of these O-glycosylation sites are consistent with the previous reports that residues at positions -1 and +3 may influence the glycosylation reaction.
8323299	6	51	theme	acid	881:884	arg1	consistent					931:940	consistent	931:940	consistent	931:940	The amino acid sequences of these O-glycosylation sites are consistent with the previous reports that residues at positions -1 and +3 may influence the glycosylation reaction.
8323299	2	52	theme	oligosaccharides	360:375	arg1	localization					335:346	the localization	331:346	the localization of O-linked oligosaccharides exclusively to the hinge-like regions of lamp-1 and lamp-2 isolated from human chronic myelogenous leukemia cells	331:489	In the present paper, we report the localization of O-linked oligosaccharides exclusively to the hinge-like regions of lamp-1 and lamp-2 isolated from human chronic myelogenous leukemia cells.
8323299	1	53	gly	glycosylated	198:209	arg1	glycoproteins					150:162	The lysosomal membrane glycoproteins	127:162	The lysosomal membrane glycoproteins lamp-1 and lamp-2	127:180	The lysosomal membrane glycoproteins lamp-1 and lamp-2 are extensively glycosylated with a variety of different carbohydrate structures of both N-linked and O-linked type.
8323299	1	53	gly	glycosylated	198:209	arg1	lamp-2					175:180	lamp-2	175:180	lamp-2	175:180	The lysosomal membrane glycoproteins lamp-1 and lamp-2 are extensively glycosylated with a variety of different carbohydrate structures of both N-linked and O-linked type.
8323299	1	53	gly	glycosylated	198:209	arg1	lamp-1					164:169	lamp-1	164:169	lamp-1	164:169	The lysosomal membrane glycoproteins lamp-1 and lamp-2 are extensively glycosylated with a variety of different carbohydrate structures of both N-linked and O-linked type.
8323299	1	54	link	O-linked	284:291	arg1	type					293:296	both N-linked and O-linked type	266:296	both N-linked and O-linked type	266:296	The lysosomal membrane glycoproteins lamp-1 and lamp-2 are extensively glycosylated with a variety of different carbohydrate structures of both N-linked and O-linked type.
8323299	9	55	theme	peptide	1420:1426	arg1	similar					1441:1447	similar	1441:1447	similar	1441:1447	The circular dichroism spectrum of the peptide is, however, similar to that of porcine submaxillary apomucin.
8323299	9	55	theme	peptide	1420:1426	arg1	spectrum					1404:1411	The circular dichroism spectrum	1381:1411	The circular dichroism spectrum of the peptide	1381:1426	The circular dichroism spectrum of the peptide is, however, similar to that of porcine submaxillary apomucin.
8323299	8	56	theme	O-glycan	1270:1277	arg1	region					1288:1293	the proline-rich O-glycan acceptor region	1253:1293	the proline-rich O-glycan acceptor region	1253:1293	The results indicated that the proline-rich O-glycan acceptor region does not adopt any typical periodic structure but differs from random-coil structure.
8323299	2	57	link	O-linked	351:358	arg1	oligosaccharides					360:375	O-linked oligosaccharides	351:375	O-linked oligosaccharides	351:375	In the present paper, we report the localization of O-linked oligosaccharides exclusively to the hinge-like regions of lamp-1 and lamp-2 isolated from human chronic myelogenous leukemia cells.
8323299	4	58	gly	glycosylated	619:630	arg1	Ser-181					587:593	Ser-181	587:593	Ser-181	587:593	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg1	Thr-171					560:566	Thr-171	560:566	Thr-171	560:566	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg2	Ser-179					578:584	Ser-179	578:584	Ser-179	578:584	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg1	Thr-172					569:575	Thr-172	569:575	Thr-172	569:575	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg1	Ser-183					600:606	Ser-183	600:606	Ser-183	600:606	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg2	Thr-171					560:566	Thr-171	560:566	Thr-171	560:566	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg2	Ser-181					587:593	Ser-181	587:593	Ser-181	587:593	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg1	lamp-1					552:557	lamp-1	552:557	lamp-1	552:557	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg1	Ser-179					578:584	Ser-179	578:584	Ser-179	578:584	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg2	Thr-172					569:575	Thr-172	569:575	Thr-172	569:575	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	4	58	gly	glycosylated	619:630	arg2	Ser-183					600:606	Ser-183	600:606	Ser-183	600:606	In lamp-1, Thr-171, Thr-172, Ser-179, Ser-181, and Ser-183 were fully glycosylated, whereas Ser-169 was partially glycosylated.
8323299	1	59	link	N-linked	271:278	arg1	type					293:296	both N-linked and O-linked type	266:296	both N-linked and O-linked type	266:296	The lysosomal membrane glycoproteins lamp-1 and lamp-2 are extensively glycosylated with a variety of different carbohydrate structures of both N-linked and O-linked type.
8323299	6	60	with	consistent	931:940	arg1	reports					960:966	the previous reports	947:966	the previous reports that residues at positions -1 and +3 may influence the glycosylation reaction	947:1044	The amino acid sequences of these O-glycosylation sites are consistent with the previous reports that residues at positions -1 and +3 may influence the glycosylation reaction.
8323299	7	61	theme	Circular	1047:1054	arg1	dichroism					1056:1064	Circular dichroism	1047:1064	Circular dichroism	1047:1064	Circular dichroism and nuclear magnetic resonance spectroscopy was used for the structural characterization of a synthetic peptide corresponding to residues 167 to 190 of lamp-1.
8323299	5	62	located	found	715:719	arg1	Ser-179					820:826	Ser-179	820:826	Ser-179	820:826	In lamp-2, complete glycosylation was found at Ser-167, Thr-168, Thr-172, Thr-175, Thr-176, Thr-182, and Thr-183, and partial glycosylation at Ser-179 and Thr-181, and possibly also at Thr-185.
8323299	5	62	located	found	715:719	arg1	lamp-2					680:685	lamp-2	680:685	lamp-2	680:685	In lamp-2, complete glycosylation was found at Ser-167, Thr-168, Thr-172, Thr-175, Thr-176, Thr-182, and Thr-183, and partial glycosylation at Ser-179 and Thr-181, and possibly also at Thr-185.
8323299	5	62	located	found	715:719	arg2	glycosylation					697:709	complete glycosylation	688:709	complete glycosylation	688:709	In lamp-2, complete glycosylation was found at Ser-167, Thr-168, Thr-172, Thr-175, Thr-176, Thr-182, and Thr-183, and partial glycosylation at Ser-179 and Thr-181, and possibly also at Thr-185.
8323299	10	63	theme	slow	1581:1584	arg1	isomerization					1643:1655	a slow (on the nuclear magnetic resonance time scale) cis-trans isomerization	1579:1655	a slow (on the nuclear magnetic resonance time scale) cis-trans isomerization of several proline residues	1579:1683	A significant conformational variability was observed in this region, presumably due to a slow (on the nuclear magnetic resonance time scale) cis-trans isomerization of several proline residues.
8323299	11	64	theme	ordered	1783:1789	arg1	structure					1791:1799	any typical ordered structure	1771:1799	any typical ordered structure	1771:1799	These results, taken together, strongly suggest that a hinge region does not display any typical ordered structure.
8323299	5	65	theme	partial	795:801	arg1	glycosylation					803:815	partial glycosylation	795:815	partial glycosylation	795:815	In lamp-2, complete glycosylation was found at Ser-167, Thr-168, Thr-172, Thr-175, Thr-176, Thr-182, and Thr-183, and partial glycosylation at Ser-179 and Thr-181, and possibly also at Thr-185.
8323299	10	66	theme	resonance	1611:1619	arg1	scale					1626:1630	the nuclear magnetic resonance time scale	1590:1630	the nuclear magnetic resonance time scale	1590:1630	A significant conformational variability was observed in this region, presumably due to a slow (on the nuclear magnetic resonance time scale) cis-trans isomerization of several proline residues.
8323299	6	67	theme	O-glycosylation	905:919	arg1	sites					921:925	these O-glycosylation sites	899:925	these O-glycosylation sites	899:925	The amino acid sequences of these O-glycosylation sites are consistent with the previous reports that residues at positions -1 and +3 may influence the glycosylation reaction.
8323299	10	68	theme	nuclear	1594:1600	arg1	resonance					1611:1619	the nuclear magnetic resonance	1590:1619	the nuclear magnetic resonance time scale	1590:1630	A significant conformational variability was observed in this region, presumably due to a slow (on the nuclear magnetic resonance time scale) cis-trans isomerization of several proline residues.
8323299	1	69	gly	glycoproteins	150:162	arg1	glycoproteins					150:162	The lysosomal membrane glycoproteins	127:162	The lysosomal membrane glycoproteins lamp-1 and lamp-2	127:180	The lysosomal membrane glycoproteins lamp-1 and lamp-2 are extensively glycosylated with a variety of different carbohydrate structures of both N-linked and O-linked type.
8323299	1	69	gly	glycoproteins	150:162	arg1	lamp-2					175:180	lamp-2	175:180	lamp-2	175:180	The lysosomal membrane glycoproteins lamp-1 and lamp-2 are extensively glycosylated with a variety of different carbohydrate structures of both N-linked and O-linked type.
8323299	1	69	gly	glycoproteins	150:162	arg1	lamp-1					164:169	lamp-1	164:169	lamp-1	164:169	The lysosomal membrane glycoproteins lamp-1 and lamp-2 are extensively glycosylated with a variety of different carbohydrate structures of both N-linked and O-linked type.
8323299	9	70	theme	submaxillary	1468:1479	arg1	apomucin					1481:1488	porcine submaxillary apomucin	1460:1488	porcine submaxillary apomucin	1460:1488	The circular dichroism spectrum of the peptide is, however, similar to that of porcine submaxillary apomucin.
8323299	5	71	gly	glycosylation	697:709	arg1	Thr-185					862:868	Thr-185	862:868	Thr-185	862:868	In lamp-2, complete glycosylation was found at Ser-167, Thr-168, Thr-172, Thr-175, Thr-176, Thr-182, and Thr-183, and partial glycosylation at Ser-179 and Thr-181, and possibly also at Thr-185.
8323299	5	71	gly	glycosylation	697:709	arg2	Thr-185					862:868	Thr-185	862:868	Thr-185	862:868	In lamp-2, complete glycosylation was found at Ser-167, Thr-168, Thr-172, Thr-175, Thr-176, Thr-182, and Thr-183, and partial glycosylation at Ser-179 and Thr-181, and possibly also at Thr-185.
8323299	5	71	gly	glycosylation	697:709	arg1	Ser-179					820:826	Ser-179	820:826	Ser-179	820:826	In lamp-2, complete glycosylation was found at Ser-167, Thr-168, Thr-172, Thr-175, Thr-176, Thr-182, and Thr-183, and partial glycosylation at Ser-179 and Thr-181, and possibly also at Thr-185.
8323299	5	71	gly	glycosylation	697:709	arg2	Ser-179					820:826	Ser-179	820:826	Ser-179	820:826	In lamp-2, complete glycosylation was found at Ser-167, Thr-168, Thr-172, Thr-175, Thr-176, Thr-182, and Thr-183, and partial glycosylation at Ser-179 and Thr-181, and possibly also at Thr-185.
8323299	5	71	gly	glycosylation	697:709	arg1	lamp-2					680:685	lamp-2	680:685	lamp-2	680:685	In lamp-2, complete glycosylation was found at Ser-167, Thr-168, Thr-172, Thr-175, Thr-176, Thr-182, and Thr-183, and partial glycosylation at Ser-179 and Thr-181, and possibly also at Thr-185.
8323299	5	72	from	glycosylation	803:815	arg1	Ser-179					820:826	Ser-179	820:826	Ser-179	820:826	In lamp-2, complete glycosylation was found at Ser-167, Thr-168, Thr-172, Thr-175, Thr-176, Thr-182, and Thr-183, and partial glycosylation at Ser-179 and Thr-181, and possibly also at Thr-185.
8323299	1	73	theme	membrane	141:148	arg1	glycoproteins					150:162	The lysosomal membrane glycoproteins	127:162	The lysosomal membrane glycoproteins lamp-1 and lamp-2	127:180	The lysosomal membrane glycoproteins lamp-1 and lamp-2 are extensively glycosylated with a variety of different carbohydrate structures of both N-linked and O-linked type.
8323299	1	73	theme	membrane	141:148	arg1	lamp-2					175:180	lamp-2	175:180	lamp-2	175:180	The lysosomal membrane glycoproteins lamp-1 and lamp-2 are extensively glycosylated with a variety of different carbohydrate structures of both N-linked and O-linked type.
8323299	1	73	theme	membrane	141:148	arg1	lamp-1					164:169	lamp-1	164:169	lamp-1	164:169	The lysosomal membrane glycoproteins lamp-1 and lamp-2 are extensively glycosylated with a variety of different carbohydrate structures of both N-linked and O-linked type.
8323299	0	74	theme	lysosomal	75:83	arg1	glycoproteins					94:106	human lysosomal membrane glycoproteins lamp-1 and lamp-2	69:124	human lysosomal membrane glycoproteins lamp-1 and lamp-2	69:124	Assignment of O-glycan attachment sites to the hinge-like regions of human lysosomal membrane glycoproteins lamp-1 and lamp-2.
8323299	0	74	theme	lysosomal	75:83	arg1	lamp-2					119:124	lamp-2	119:124	lamp-2	119:124	Assignment of O-glycan attachment sites to the hinge-like regions of human lysosomal membrane glycoproteins lamp-1 and lamp-2.
8323299	0	74	theme	lysosomal	75:83	arg1	lamp-1					108:113	lamp-1	108:113	lamp-1	108:113	Assignment of O-glycan attachment sites to the hinge-like regions of human lysosomal membrane glycoproteins lamp-1 and lamp-2.
8323299	10	75	theme	significant	1493:1503	arg1	variability					1520:1530	A significant conformational variability	1491:1530	A significant conformational variability	1491:1530	A significant conformational variability was observed in this region, presumably due to a slow (on the nuclear magnetic resonance time scale) cis-trans isomerization of several proline residues.
8323299	0	76	theme	glycoproteins	94:106	arg1	regions					58:64	the hinge-like regions	43:64	the hinge-like regions of human lysosomal membrane glycoproteins lamp-1 and lamp-2	43:124	Assignment of O-glycan attachment sites to the hinge-like regions of human lysosomal membrane glycoproteins lamp-1 and lamp-2.
8323299	6	77	theme	previous	951:958	arg1	reports					960:966	the previous reports	947:966	the previous reports that residues at positions -1 and +3 may influence the glycosylation reaction	947:1044	The amino acid sequences of these O-glycosylation sites are consistent with the previous reports that residues at positions -1 and +3 may influence the glycosylation reaction.
8323299	6	78	from	positions	985:993	arg1	residues					973:980	residues	973:980	residues at positions -1 and +3	973:1003	The amino acid sequences of these O-glycosylation sites are consistent with the previous reports that residues at positions -1 and +3 may influence the glycosylation reaction.
8323299	8	79	theme	periodic	1322:1329	arg1	structure					1331:1339	any typical periodic structure	1310:1339	any typical periodic structure	1310:1339	The results indicated that the proline-rich O-glycan acceptor region does not adopt any typical periodic structure but differs from random-coil structure.
8323299	7	80	theme	peptide	1170:1176	arg1	characterization					1138:1153	the structural characterization	1123:1153	the structural characterization of a synthetic peptide corresponding to residues 167 to 190 of lamp-1	1123:1223	Circular dichroism and nuclear magnetic resonance spectroscopy was used for the structural characterization of a synthetic peptide corresponding to residues 167 to 190 of lamp-1.
8323299	12	81	theme	lysosomal	1879:1887	arg1	proteases					1889:1897	intralumenal lysosomal proteases	1866:1897	intralumenal lysosomal proteases	1866:1897	The presence of O-glycans thus likely protects this region from intralumenal lysosomal proteases.
8323299	0	82	dep	glycoproteins	94:106	arg1	glycoproteins					94:106	human lysosomal membrane glycoproteins lamp-1 and lamp-2	69:124	human lysosomal membrane glycoproteins lamp-1 and lamp-2	69:124	Assignment of O-glycan attachment sites to the hinge-like regions of human lysosomal membrane glycoproteins lamp-1 and lamp-2.
8323299	0	82	dep	glycoproteins	94:106	arg1	lamp-2					119:124	lamp-2	119:124	lamp-2	119:124	Assignment of O-glycan attachment sites to the hinge-like regions of human lysosomal membrane glycoproteins lamp-1 and lamp-2.
8323299	0	82	dep	glycoproteins	94:106	arg1	lamp-1					108:113	lamp-1	108:113	lamp-1	108:113	Assignment of O-glycan attachment sites to the hinge-like regions of human lysosomal membrane glycoproteins lamp-1 and lamp-2.
8323299	1	83	theme	carbohydrate	239:250	arg1	structures					252:261	different carbohydrate structures	229:261	different carbohydrate structures of both N-linked and O-linked type	229:296	The lysosomal membrane glycoproteins lamp-1 and lamp-2 are extensively glycosylated with a variety of different carbohydrate structures of both N-linked and O-linked type.
8323299	5	84	from	Thr-183	782:788	arg1	Ser-179					820:826	Ser-179	820:826	Ser-179	820:826	In lamp-2, complete glycosylation was found at Ser-167, Thr-168, Thr-172, Thr-175, Thr-176, Thr-182, and Thr-183, and partial glycosylation at Ser-179 and Thr-181, and possibly also at Thr-185.
8323299	6	85	theme	glycosylation	1023:1035	arg1	reaction					1037:1044	the glycosylation reaction	1019:1044	the glycosylation reaction	1019:1044	The amino acid sequences of these O-glycosylation sites are consistent with the previous reports that residues at positions -1 and +3 may influence the glycosylation reaction.
8323299	2	86	theme	chronic	456:462	arg1	leukemia					476:483	chronic myelogenous leukemia	456:483	human chronic myelogenous leukemia cells	450:489	In the present paper, we report the localization of O-linked oligosaccharides exclusively to the hinge-like regions of lamp-1 and lamp-2 isolated from human chronic myelogenous leukemia cells.
8323299	10	87	theme	time	1621:1624	arg1	scale					1626:1630	the nuclear magnetic resonance time scale	1590:1630	the nuclear magnetic resonance time scale	1590:1630	A significant conformational variability was observed in this region, presumably due to a slow (on the nuclear magnetic resonance time scale) cis-trans isomerization of several proline residues.
8323299	0	88	theme	attachment	23:32	arg1	sites					34:38	O-glycan attachment sites	14:38	O-glycan attachment sites	14:38	Assignment of O-glycan attachment sites to the hinge-like regions of human lysosomal membrane glycoproteins lamp-1 and lamp-2.
8323299	1	89	dep	glycoproteins	150:162	arg1	glycoproteins					150:162	The lysosomal membrane glycoproteins	127:162	The lysosomal membrane glycoproteins lamp-1 and lamp-2	127:180	The lysosomal membrane glycoproteins lamp-1 and lamp-2 are extensively glycosylated with a variety of different carbohydrate structures of both N-linked and O-linked type.
8323299	1	89	dep	glycoproteins	150:162	arg1	lamp-2					175:180	lamp-2	175:180	lamp-2	175:180	The lysosomal membrane glycoproteins lamp-1 and lamp-2 are extensively glycosylated with a variety of different carbohydrate structures of both N-linked and O-linked type.
8323299	1	89	dep	glycoproteins	150:162	arg1	lamp-1					164:169	lamp-1	164:169	lamp-1	164:169	The lysosomal membrane glycoproteins lamp-1 and lamp-2 are extensively glycosylated with a variety of different carbohydrate structures of both N-linked and O-linked type.
8323299	2	90	theme	lamp-2	429:434	arg1	regions					407:413	the hinge-like regions	392:413	the hinge-like regions of lamp-1 and lamp-2 isolated from human chronic myelogenous leukemia cells	392:489	In the present paper, we report the localization of O-linked oligosaccharides exclusively to the hinge-like regions of lamp-1 and lamp-2 isolated from human chronic myelogenous leukemia cells.
8323299	2	91	attach	isolated	436:443	arg1	cells					485:489	human chronic myelogenous leukemia cells	450:489	human chronic myelogenous leukemia cells	450:489	In the present paper, we report the localization of O-linked oligosaccharides exclusively to the hinge-like regions of lamp-1 and lamp-2 isolated from human chronic myelogenous leukemia cells.
8323299	2	91	attach	isolated	436:443	arg2	regions					407:413	the hinge-like regions	392:413	the hinge-like regions of lamp-1 and lamp-2 isolated from human chronic myelogenous leukemia cells	392:489	In the present paper, we report the localization of O-linked oligosaccharides exclusively to the hinge-like regions of lamp-1 and lamp-2 isolated from human chronic myelogenous leukemia cells.
8323299	9	92	theme	dichroism	1394:1402	arg1	similar					1441:1447	similar	1441:1447	similar	1441:1447	The circular dichroism spectrum of the peptide is, however, similar to that of porcine submaxillary apomucin.
8323299	9	92	theme	dichroism	1394:1402	arg1	spectrum					1404:1411	The circular dichroism spectrum	1381:1411	The circular dichroism spectrum of the peptide	1381:1426	The circular dichroism spectrum of the peptide is, however, similar to that of porcine submaxillary apomucin.
8323299	2	93	theme	lamp-1	418:423	arg1	regions					407:413	the hinge-like regions	392:413	the hinge-like regions of lamp-1 and lamp-2 isolated from human chronic myelogenous leukemia cells	392:489	In the present paper, we report the localization of O-linked oligosaccharides exclusively to the hinge-like regions of lamp-1 and lamp-2 isolated from human chronic myelogenous leukemia cells.
8323299	0	94	theme	hinge-like	47:56	arg1	regions					58:64	the hinge-like regions	43:64	the hinge-like regions of human lysosomal membrane glycoproteins lamp-1 and lamp-2	43:124	Assignment of O-glycan attachment sites to the hinge-like regions of human lysosomal membrane glycoproteins lamp-1 and lamp-2.
8323299	12	95	theme	O-glycans	1818:1826	arg1	presence					1806:1813	The presence	1802:1813	The presence of O-glycans	1802:1826	The presence of O-glycans thus likely protects this region from intralumenal lysosomal proteases.
8323299	2	96	theme	leukemia	476:483	arg1	cells					485:489	human chronic myelogenous leukemia cells	450:489	human chronic myelogenous leukemia cells	450:489	In the present paper, we report the localization of O-linked oligosaccharides exclusively to the hinge-like regions of lamp-1 and lamp-2 isolated from human chronic myelogenous leukemia cells.
8323299	7	97	dep	residues	1195:1202	arg1	to					1208:1209	to	1208:1209	to	1208:1209	Circular dichroism and nuclear magnetic resonance spectroscopy was used for the structural characterization of a synthetic peptide corresponding to residues 167 to 190 of lamp-1.
8323299	10	98	theme	residues	1676:1683	arg1	isomerization					1643:1655	a slow (on the nuclear magnetic resonance time scale) cis-trans isomerization	1579:1655	a slow (on the nuclear magnetic resonance time scale) cis-trans isomerization of several proline residues	1579:1683	A significant conformational variability was observed in this region, presumably due to a slow (on the nuclear magnetic resonance time scale) cis-trans isomerization of several proline residues.
8323299	9	99	theme	circular	1385:1392	arg1	similar					1441:1447	similar	1441:1447	similar	1441:1447	The circular dichroism spectrum of the peptide is, however, similar to that of porcine submaxillary apomucin.
8323299	9	99	theme	circular	1385:1392	arg1	spectrum					1404:1411	The circular dichroism spectrum	1381:1411	The circular dichroism spectrum of the peptide	1381:1426	The circular dichroism spectrum of the peptide is, however, similar to that of porcine submaxillary apomucin.
8323299	10	100	from	isomerization	1643:1655	arg1	scale					1626:1630	the nuclear magnetic resonance time scale	1590:1630	the nuclear magnetic resonance time scale	1590:1630	A significant conformational variability was observed in this region, presumably due to a slow (on the nuclear magnetic resonance time scale) cis-trans isomerization of several proline residues.
11733580	0	0	theme	chemokine	77:85	arg1	receptor					87:94	CC chemokine receptor 5	74:96	CC chemokine receptor 5	74:96	Sialylated O-glycans and sulfated tyrosines in the NH2-terminal domain of CC chemokine receptor 5 contribute to high affinity binding of chemokines.
11733580	5	1	theme	beta-chemokine	726:739	arg1	binding					741:747	efficient beta-chemokine binding	716:747	efficient beta-chemokine binding	716:747	Sulfation of specific tyrosine residues in the CCR5 NH2 terminus was important for efficient beta-chemokine binding.
11733580	6	2	theme	O-linked	825:832	arg1	carbohydrates					834:846	O-linked carbohydrates	825:846	O-linked carbohydrates	825:846	Thus, as has been observed for the binding of selectins and their ligands, O-linked carbohydrates and tyrosine sulfates play major roles in promoting the interaction of chemokines with CCR5.
11733580	8	3	theme	many	1287:1290	arg1	receptors					1305:1313	many CC chemokine receptors	1287:1313	many CC chemokine receptors	1287:1313	Although this is the first example of O-linked oligosaccharides and tyrosine sulfates playing a role in chemokine binding, the high density of serines, threonines and tyrosines in the N-termini of many CC chemokine receptors suggests that these posttranslational modifications may commonly contribute to chemokine binding.
11733580	0	4	theme	CC	74:75	arg1	receptor					87:94	CC chemokine receptor 5	74:96	CC chemokine receptor 5	74:96	Sialylated O-glycans and sulfated tyrosines in the NH2-terminal domain of CC chemokine receptor 5 contribute to high affinity binding of chemokines.
11733580	0	5	from	O-glycans	11:19	arg1	domain					64:69	the NH2-terminal domain	47:69	the NH2-terminal domain of CC chemokine receptor 5	47:96	Sialylated O-glycans and sulfated tyrosines in the NH2-terminal domain of CC chemokine receptor 5 contribute to high affinity binding of chemokines.
11733580	0	5	from	O-glycans	11:19	arg1	receptor					87:94	CC chemokine receptor 5	74:96	CC chemokine receptor 5	74:96	Sialylated O-glycans and sulfated tyrosines in the NH2-terminal domain of CC chemokine receptor 5 contribute to high affinity binding of chemokines.
11733580	2	6	gly	O-glycosylated	375:388	arg1	CCR5					367:370	CCR5	367:370	CCR5	367:370	We provide evidence that CCR5 is O-glycosylated on serine 6 in the NH2 terminus.
11733580	2	6	gly	O-glycosylated	375:388	arg2	CCR5					367:370	CCR5	367:370	CCR5	367:370	We provide evidence that CCR5 is O-glycosylated on serine 6 in the NH2 terminus.
11733580	2	6	gly	O-glycosylated	375:388	arg1	terminus					413:420	the NH2 terminus	405:420	the NH2 terminus	405:420	We provide evidence that CCR5 is O-glycosylated on serine 6 in the NH2 terminus.
11733580	2	6	gly	O-glycosylated	375:388	arg1	serine					393:398	serine 6	393:400	serine 6	393:400	We provide evidence that CCR5 is O-glycosylated on serine 6 in the NH2 terminus.
11733580	1	7	theme	chemokine	153:161	arg1	CCR5					172:175	The chemokine receptor CCR5	149:175	The chemokine receptor CCR5	149:175	The chemokine receptor CCR5 plays an important role in leukocyte chemotaxis and activation, and also acts as a coreceptor for human and simian immunodeficiency viruses (HIV-1, HIV-2, and SIV).
11733580	1	7	theme	chemokine	153:161	arg1	coreceptor					260:269	a coreceptor	258:269	a coreceptor for human and simian immunodeficiency viruses (HIV-1, HIV-2, and SIV)	258:339	The chemokine receptor CCR5 plays an important role in leukocyte chemotaxis and activation, and also acts as a coreceptor for human and simian immunodeficiency viruses (HIV-1, HIV-2, and SIV).
11733580	5	8	theme	NH2	685:687	arg1	terminus					689:696	the CCR5 NH2 terminus	676:696	the CCR5 NH2 terminus	676:696	Sulfation of specific tyrosine residues in the CCR5 NH2 terminus was important for efficient beta-chemokine binding.
11733580	7	9	theme	chemokine	1071:1079	arg1	ligands					1081:1087	diverse chemokine ligands	1063:1087	diverse chemokine ligands	1063:1087	The resulting flexible arrays of negative charges on the CCR5 surface may allow specific, high-affinity interactions with diverse chemokine ligands.
11733580	8	10	theme	chemokine	1295:1303	arg1	receptors					1305:1313	many CC chemokine receptors	1287:1313	many CC chemokine receptors	1287:1313	Although this is the first example of O-linked oligosaccharides and tyrosine sulfates playing a role in chemokine binding, the high density of serines, threonines and tyrosines in the N-termini of many CC chemokine receptors suggests that these posttranslational modifications may commonly contribute to chemokine binding.
11733580	8	11	theme	posttranslational	1335:1351	arg1	modifications					1353:1365	these posttranslational modifications	1329:1365	these posttranslational modifications	1329:1365	Although this is the first example of O-linked oligosaccharides and tyrosine sulfates playing a role in chemokine binding, the high density of serines, threonines and tyrosines in the N-termini of many CC chemokine receptors suggests that these posttranslational modifications may commonly contribute to chemokine binding.
11733580	5	12	from	residues	664:671	arg1	terminus					689:696	the CCR5 NH2 terminus	676:696	the CCR5 NH2 terminus	676:696	Sulfation of specific tyrosine residues in the CCR5 NH2 terminus was important for efficient beta-chemokine binding.
11733580	0	13	theme	receptor	87:94	arg1	domain					64:69	the NH2-terminal domain	47:69	the NH2-terminal domain of CC chemokine receptor 5	47:96	Sialylated O-glycans and sulfated tyrosines in the NH2-terminal domain of CC chemokine receptor 5 contribute to high affinity binding of chemokines.
11733580	0	13	theme	receptor	87:94	arg1	receptor					87:94	CC chemokine receptor 5	74:96	CC chemokine receptor 5	74:96	Sialylated O-glycans and sulfated tyrosines in the NH2-terminal domain of CC chemokine receptor 5 contribute to high affinity binding of chemokines.
11733580	6	14	theme	tyrosine	852:859	arg1	sulfates					861:868	tyrosine sulfates	852:868	tyrosine sulfates	852:868	Thus, as has been observed for the binding of selectins and their ligands, O-linked carbohydrates and tyrosine sulfates play major roles in promoting the interaction of chemokines with CCR5.
11733580	8	15	theme	CC	1292:1293	arg1	receptors					1305:1313	many CC chemokine receptors	1287:1313	many CC chemokine receptors	1287:1313	Although this is the first example of O-linked oligosaccharides and tyrosine sulfates playing a role in chemokine binding, the high density of serines, threonines and tyrosines in the N-termini of many CC chemokine receptors suggests that these posttranslational modifications may commonly contribute to chemokine binding.
11733580	7	16	dep	specific	1021:1028	arg1	high-affinity					1031:1043	high-affinity	1031:1043	high-affinity	1031:1043	The resulting flexible arrays of negative charges on the CCR5 surface may allow specific, high-affinity interactions with diverse chemokine ligands.
11733580	8	17	theme	tyrosines	1257:1265	arg1	density					1222:1228	the high density	1213:1228	the high density of serines, threonines and tyrosines in the N-termini of many CC chemokine receptors	1213:1313	Although this is the first example of O-linked oligosaccharides and tyrosine sulfates playing a role in chemokine binding, the high density of serines, threonines and tyrosines in the N-termini of many CC chemokine receptors suggests that these posttranslational modifications may commonly contribute to chemokine binding.
11733580	8	18	theme	oligosaccharides	1137:1152	arg1	this					1099:1102	this	1099:1102	this	1099:1102	Although this is the first example of O-linked oligosaccharides and tyrosine sulfates playing a role in chemokine binding, the high density of serines, threonines and tyrosines in the N-termini of many CC chemokine receptors suggests that these posttranslational modifications may commonly contribute to chemokine binding.
11733580	8	18	theme	oligosaccharides	1137:1152	arg1	example					1117:1123	the first example	1107:1123	the first example of O-linked oligosaccharides and tyrosine sulfates playing a role in chemokine binding	1107:1210	Although this is the first example of O-linked oligosaccharides and tyrosine sulfates playing a role in chemokine binding, the high density of serines, threonines and tyrosines in the N-termini of many CC chemokine receptors suggests that these posttranslational modifications may commonly contribute to chemokine binding.
11733580	1	19	dep	viruses	309:315	arg1	HIV-2					325:329	HIV-2	325:329	HIV-2	325:329	The chemokine receptor CCR5 plays an important role in leukocyte chemotaxis and activation, and also acts as a coreceptor for human and simian immunodeficiency viruses (HIV-1, HIV-2, and SIV).
11733580	1	19	dep	viruses	309:315	arg1	SIV					336:338	SIV	336:338	SIV	336:338	The chemokine receptor CCR5 plays an important role in leukocyte chemotaxis and activation, and also acts as a coreceptor for human and simian immunodeficiency viruses (HIV-1, HIV-2, and SIV).
11733580	1	19	dep	viruses	309:315	arg1	HIV-1					318:322	HIV-1	318:322	HIV-1	318:322	The chemokine receptor CCR5 plays an important role in leukocyte chemotaxis and activation, and also acts as a coreceptor for human and simian immunodeficiency viruses (HIV-1, HIV-2, and SIV).
11733580	1	19	dep	viruses	309:315	arg1	viruses					309:315	human and simian immunodeficiency viruses	275:315	human and simian immunodeficiency viruses (HIV-1, HIV-2, and SIV)	275:339	The chemokine receptor CCR5 plays an important role in leukocyte chemotaxis and activation, and also acts as a coreceptor for human and simian immunodeficiency viruses (HIV-1, HIV-2, and SIV).
11733580	6	20	link	O-linked	825:832	arg1	carbohydrates					834:846	O-linked carbohydrates	825:846	O-linked carbohydrates	825:846	Thus, as has been observed for the binding of selectins and their ligands, O-linked carbohydrates and tyrosine sulfates play major roles in promoting the interaction of chemokines with CCR5.
11733580	8	21	theme	sulfates	1167:1174	arg1	this					1099:1102	this	1099:1102	this	1099:1102	Although this is the first example of O-linked oligosaccharides and tyrosine sulfates playing a role in chemokine binding, the high density of serines, threonines and tyrosines in the N-termini of many CC chemokine receptors suggests that these posttranslational modifications may commonly contribute to chemokine binding.
11733580	8	21	theme	sulfates	1167:1174	arg1	example					1117:1123	the first example	1107:1123	the first example of O-linked oligosaccharides and tyrosine sulfates playing a role in chemokine binding	1107:1210	Although this is the first example of O-linked oligosaccharides and tyrosine sulfates playing a role in chemokine binding, the high density of serines, threonines and tyrosines in the N-termini of many CC chemokine receptors suggests that these posttranslational modifications may commonly contribute to chemokine binding.
11733580	1	22	theme	receptor	163:170	arg1	CCR5					172:175	The chemokine receptor CCR5	149:175	The chemokine receptor CCR5	149:175	The chemokine receptor CCR5 plays an important role in leukocyte chemotaxis and activation, and also acts as a coreceptor for human and simian immunodeficiency viruses (HIV-1, HIV-2, and SIV).
11733580	1	22	theme	receptor	163:170	arg1	coreceptor					260:269	a coreceptor	258:269	a coreceptor for human and simian immunodeficiency viruses (HIV-1, HIV-2, and SIV)	258:339	The chemokine receptor CCR5 plays an important role in leukocyte chemotaxis and activation, and also acts as a coreceptor for human and simian immunodeficiency viruses (HIV-1, HIV-2, and SIV).
11733580	8	23	theme	O-linked	1128:1135	arg1	oligosaccharides					1137:1152	O-linked oligosaccharides	1128:1152	O-linked oligosaccharides	1128:1152	Although this is the first example of O-linked oligosaccharides and tyrosine sulfates playing a role in chemokine binding, the high density of serines, threonines and tyrosines in the N-termini of many CC chemokine receptors suggests that these posttranslational modifications may commonly contribute to chemokine binding.
11733580	7	24	theme	diverse	1063:1069	arg1	ligands					1081:1087	diverse chemokine ligands	1063:1087	diverse chemokine ligands	1063:1087	The resulting flexible arrays of negative charges on the CCR5 surface may allow specific, high-affinity interactions with diverse chemokine ligands.
11733580	8	25	theme	receptors	1305:1313	arg1	N-termini					1274:1282	the N-termini	1270:1282	the N-termini of many CC chemokine receptors	1270:1313	Although this is the first example of O-linked oligosaccharides and tyrosine sulfates playing a role in chemokine binding, the high density of serines, threonines and tyrosines in the N-termini of many CC chemokine receptors suggests that these posttranslational modifications may commonly contribute to chemokine binding.
11733580	8	26	theme	tyrosine	1158:1165	arg1	sulfates					1167:1174	tyrosine sulfates	1158:1174	tyrosine sulfates	1158:1174	Although this is the first example of O-linked oligosaccharides and tyrosine sulfates playing a role in chemokine binding, the high density of serines, threonines and tyrosines in the N-termini of many CC chemokine receptors suggests that these posttranslational modifications may commonly contribute to chemokine binding.
11733580	0	27	from	tyrosines	34:42	arg1	domain					64:69	the NH2-terminal domain	47:69	the NH2-terminal domain of CC chemokine receptor 5	47:96	Sialylated O-glycans and sulfated tyrosines in the NH2-terminal domain of CC chemokine receptor 5 contribute to high affinity binding of chemokines.
11733580	0	27	from	tyrosines	34:42	arg1	receptor					87:94	CC chemokine receptor 5	74:96	CC chemokine receptor 5	74:96	Sialylated O-glycans and sulfated tyrosines in the NH2-terminal domain of CC chemokine receptor 5 contribute to high affinity binding of chemokines.
11733580	3	28	link	O-linked	427:434	arg1	glycans					436:442	The O-linked glycans	423:442	The O-linked glycans	423:442	The O-linked glycans, particularly sialic acid moieties, significantly contribute to binding of the chemokine ligands.
11733580	3	28	link	O-linked	427:434	arg1	moieties					470:477	sialic acid moieties	458:477	particularly sialic acid moieties	445:477	The O-linked glycans, particularly sialic acid moieties, significantly contribute to binding of the chemokine ligands.
11733580	8	29	theme	high	1217:1220	arg1	density					1222:1228	the high density	1213:1228	the high density of serines, threonines and tyrosines in the N-termini of many CC chemokine receptors	1213:1313	Although this is the first example of O-linked oligosaccharides and tyrosine sulfates playing a role in chemokine binding, the high density of serines, threonines and tyrosines in the N-termini of many CC chemokine receptors suggests that these posttranslational modifications may commonly contribute to chemokine binding.
11733580	0	30	theme	Sialylated	0:9	arg1	O-glycans					11:19	Sialylated O-glycans	0:19	Sialylated O-glycans	0:19	Sialylated O-glycans and sulfated tyrosines in the NH2-terminal domain of CC chemokine receptor 5 contribute to high affinity binding of chemokines.
11733580	8	31	theme	first	1111:1115	arg1	this					1099:1102	this	1099:1102	this	1099:1102	Although this is the first example of O-linked oligosaccharides and tyrosine sulfates playing a role in chemokine binding, the high density of serines, threonines and tyrosines in the N-termini of many CC chemokine receptors suggests that these posttranslational modifications may commonly contribute to chemokine binding.
11733580	8	31	theme	first	1111:1115	arg1	example					1117:1123	the first example	1107:1123	the first example of O-linked oligosaccharides and tyrosine sulfates playing a role in chemokine binding	1107:1210	Although this is the first example of O-linked oligosaccharides and tyrosine sulfates playing a role in chemokine binding, the high density of serines, threonines and tyrosines in the N-termini of many CC chemokine receptors suggests that these posttranslational modifications may commonly contribute to chemokine binding.
11733580	3	32	theme	chemokine	523:531	arg1	ligands					533:539	the chemokine ligands	519:539	the chemokine ligands	519:539	The O-linked glycans, particularly sialic acid moieties, significantly contribute to binding of the chemokine ligands.
11733580	7	33	theme	specific	1021:1028	arg1	interactions					1045:1056	specific, high-affinity interactions	1021:1056	specific, high-affinity interactions with diverse chemokine ligands	1021:1087	The resulting flexible arrays of negative charges on the CCR5 surface may allow specific, high-affinity interactions with diverse chemokine ligands.
11733580	7	34	from	arrays	964:969	arg1	surface					1003:1009	the CCR5 surface	994:1009	the CCR5 surface	994:1009	The resulting flexible arrays of negative charges on the CCR5 surface may allow specific, high-affinity interactions with diverse chemokine ligands.
11733580	0	35	theme	sulfated	25:32	arg1	tyrosines					34:42	sulfated tyrosines	25:42	sulfated tyrosines	25:42	Sialylated O-glycans and sulfated tyrosines in the NH2-terminal domain of CC chemokine receptor 5 contribute to high affinity binding of chemokines.
11733580	0	36	theme	affinity	117:124	arg1	binding					126:132	high affinity binding	112:132	high affinity binding of chemokines	112:146	Sialylated O-glycans and sulfated tyrosines in the NH2-terminal domain of CC chemokine receptor 5 contribute to high affinity binding of chemokines.
11733580	6	37	with	interaction	904:914	arg1	CCR5					935:938	CCR5	935:938	CCR5	935:938	Thus, as has been observed for the binding of selectins and their ligands, O-linked carbohydrates and tyrosine sulfates play major roles in promoting the interaction of chemokines with CCR5.
11733580	1	38	theme	important	186:194	arg1	role					196:199	an important role	183:199	an important role	183:199	The chemokine receptor CCR5 plays an important role in leukocyte chemotaxis and activation, and also acts as a coreceptor for human and simian immunodeficiency viruses (HIV-1, HIV-2, and SIV).
11733580	8	39	link	O-linked	1128:1135	arg1	oligosaccharides					1137:1152	O-linked oligosaccharides	1128:1152	O-linked oligosaccharides	1128:1152	Although this is the first example of O-linked oligosaccharides and tyrosine sulfates playing a role in chemokine binding, the high density of serines, threonines and tyrosines in the N-termini of many CC chemokine receptors suggests that these posttranslational modifications may commonly contribute to chemokine binding.
11733580	6	40	theme	chemokines	919:928	arg1	interaction					904:914	the interaction	900:914	the interaction of chemokines with CCR5	900:938	Thus, as has been observed for the binding of selectins and their ligands, O-linked carbohydrates and tyrosine sulfates play major roles in promoting the interaction of chemokines with CCR5.
11733580	0	41	theme	high	112:115	arg1	binding					126:132	high affinity binding	112:132	high affinity binding of chemokines	112:146	Sialylated O-glycans and sulfated tyrosines in the NH2-terminal domain of CC chemokine receptor 5 contribute to high affinity binding of chemokines.
11733580	4	42	link	O-linked	566:573	arg1	oligosaccharide					575:589	O-linked oligosaccharide	566:589	O-linked oligosaccharide	566:589	By contrast, removal of O-linked oligosaccharide exerted little effect on HIV-1 infection.
11733580	3	43	theme	sialic	458:463	arg1	glycans					436:442	The O-linked glycans	423:442	The O-linked glycans	423:442	The O-linked glycans, particularly sialic acid moieties, significantly contribute to binding of the chemokine ligands.
11733580	3	43	theme	sialic	458:463	arg1	moieties					470:477	sialic acid moieties	458:477	particularly sialic acid moieties	445:477	The O-linked glycans, particularly sialic acid moieties, significantly contribute to binding of the chemokine ligands.
11733580	6	44	theme	major	875:879	arg1	roles					881:885	major roles	875:885	major roles	875:885	Thus, as has been observed for the binding of selectins and their ligands, O-linked carbohydrates and tyrosine sulfates play major roles in promoting the interaction of chemokines with CCR5.
11733580	4	45	theme	oligosaccharide	575:589	arg1	removal					555:561	removal	555:561	removal of O-linked oligosaccharide	555:589	By contrast, removal of O-linked oligosaccharide exerted little effect on HIV-1 infection.
11733580	1	46	theme	human	275:279	arg1	HIV-2					325:329	HIV-2	325:329	HIV-2	325:329	The chemokine receptor CCR5 plays an important role in leukocyte chemotaxis and activation, and also acts as a coreceptor for human and simian immunodeficiency viruses (HIV-1, HIV-2, and SIV).
11733580	1	46	theme	human	275:279	arg1	SIV					336:338	SIV	336:338	SIV	336:338	The chemokine receptor CCR5 plays an important role in leukocyte chemotaxis and activation, and also acts as a coreceptor for human and simian immunodeficiency viruses (HIV-1, HIV-2, and SIV).
11733580	1	46	theme	human	275:279	arg1	HIV-1					318:322	HIV-1	318:322	HIV-1	318:322	The chemokine receptor CCR5 plays an important role in leukocyte chemotaxis and activation, and also acts as a coreceptor for human and simian immunodeficiency viruses (HIV-1, HIV-2, and SIV).
11733580	1	46	theme	human	275:279	arg1	viruses					309:315	human and simian immunodeficiency viruses	275:315	human and simian immunodeficiency viruses (HIV-1, HIV-2, and SIV)	275:339	The chemokine receptor CCR5 plays an important role in leukocyte chemotaxis and activation, and also acts as a coreceptor for human and simian immunodeficiency viruses (HIV-1, HIV-2, and SIV).
11733580	6	47	theme	ligands	816:822	arg1	binding					785:791	the binding	781:791	the binding of selectins and their ligands	781:822	Thus, as has been observed for the binding of selectins and their ligands, O-linked carbohydrates and tyrosine sulfates play major roles in promoting the interaction of chemokines with CCR5.
11733580	4	48	theme	HIV-1	616:620	arg1	infection					622:630	HIV-1 infection	616:630	HIV-1 infection	616:630	By contrast, removal of O-linked oligosaccharide exerted little effect on HIV-1 infection.
11733580	5	49	theme	CCR5	680:683	arg1	terminus					689:696	the CCR5 NH2 terminus	676:696	the CCR5 NH2 terminus	676:696	Sulfation of specific tyrosine residues in the CCR5 NH2 terminus was important for efficient beta-chemokine binding.
11733580	5	50	from	Sulfation	633:641	arg1	terminus					689:696	the CCR5 NH2 terminus	676:696	the CCR5 NH2 terminus	676:696	Sulfation of specific tyrosine residues in the CCR5 NH2 terminus was important for efficient beta-chemokine binding.
11733580	7	51	theme	negative	974:981	arg1	charges					983:989	negative charges	974:989	negative charges on the CCR5 surface	974:1009	The resulting flexible arrays of negative charges on the CCR5 surface may allow specific, high-affinity interactions with diverse chemokine ligands.
11733580	1	52	theme	leukocyte	204:212	arg1	chemotaxis					214:223	leukocyte chemotaxis	204:223	leukocyte chemotaxis	204:223	The chemokine receptor CCR5 plays an important role in leukocyte chemotaxis and activation, and also acts as a coreceptor for human and simian immunodeficiency viruses (HIV-1, HIV-2, and SIV).
11733580	0	53	theme	NH2-terminal	51:62	arg1	domain					64:69	the NH2-terminal domain	47:69	the NH2-terminal domain of CC chemokine receptor 5	47:96	Sialylated O-glycans and sulfated tyrosines in the NH2-terminal domain of CC chemokine receptor 5 contribute to high affinity binding of chemokines.
11733580	0	53	theme	NH2-terminal	51:62	arg1	receptor					87:94	CC chemokine receptor 5	74:96	CC chemokine receptor 5	74:96	Sialylated O-glycans and sulfated tyrosines in the NH2-terminal domain of CC chemokine receptor 5 contribute to high affinity binding of chemokines.
11733580	1	54	theme	simian	285:290	arg1	HIV-2					325:329	HIV-2	325:329	HIV-2	325:329	The chemokine receptor CCR5 plays an important role in leukocyte chemotaxis and activation, and also acts as a coreceptor for human and simian immunodeficiency viruses (HIV-1, HIV-2, and SIV).
11733580	1	54	theme	simian	285:290	arg1	SIV					336:338	SIV	336:338	SIV	336:338	The chemokine receptor CCR5 plays an important role in leukocyte chemotaxis and activation, and also acts as a coreceptor for human and simian immunodeficiency viruses (HIV-1, HIV-2, and SIV).
11733580	1	54	theme	simian	285:290	arg1	HIV-1					318:322	HIV-1	318:322	HIV-1	318:322	The chemokine receptor CCR5 plays an important role in leukocyte chemotaxis and activation, and also acts as a coreceptor for human and simian immunodeficiency viruses (HIV-1, HIV-2, and SIV).
11733580	1	54	theme	simian	285:290	arg1	viruses					309:315	human and simian immunodeficiency viruses	275:315	human and simian immunodeficiency viruses (HIV-1, HIV-2, and SIV)	275:339	The chemokine receptor CCR5 plays an important role in leukocyte chemotaxis and activation, and also acts as a coreceptor for human and simian immunodeficiency viruses (HIV-1, HIV-2, and SIV).
11733580	7	55	theme	CCR5	998:1001	arg1	surface					1003:1009	the CCR5 surface	994:1009	the CCR5 surface	994:1009	The resulting flexible arrays of negative charges on the CCR5 surface may allow specific, high-affinity interactions with diverse chemokine ligands.
11733580	5	56	theme	efficient	716:724	arg1	binding					741:747	efficient beta-chemokine binding	716:747	efficient beta-chemokine binding	716:747	Sulfation of specific tyrosine residues in the CCR5 NH2 terminus was important for efficient beta-chemokine binding.
11733580	3	57	theme	ligands	533:539	arg1	binding					508:514	binding	508:514	binding of the chemokine ligands	508:539	The O-linked glycans, particularly sialic acid moieties, significantly contribute to binding of the chemokine ligands.
11733580	7	58	theme	charges	983:989	arg1	arrays					964:969	The resulting flexible arrays	941:969	The resulting flexible arrays of negative charges on the CCR5 surface	941:1009	The resulting flexible arrays of negative charges on the CCR5 surface may allow specific, high-affinity interactions with diverse chemokine ligands.
11733580	1	59	theme	immunodeficiency	292:307	arg1	HIV-2					325:329	HIV-2	325:329	HIV-2	325:329	The chemokine receptor CCR5 plays an important role in leukocyte chemotaxis and activation, and also acts as a coreceptor for human and simian immunodeficiency viruses (HIV-1, HIV-2, and SIV).
11733580	1	59	theme	immunodeficiency	292:307	arg1	SIV					336:338	SIV	336:338	SIV	336:338	The chemokine receptor CCR5 plays an important role in leukocyte chemotaxis and activation, and also acts as a coreceptor for human and simian immunodeficiency viruses (HIV-1, HIV-2, and SIV).
11733580	1	59	theme	immunodeficiency	292:307	arg1	HIV-1					318:322	HIV-1	318:322	HIV-1	318:322	The chemokine receptor CCR5 plays an important role in leukocyte chemotaxis and activation, and also acts as a coreceptor for human and simian immunodeficiency viruses (HIV-1, HIV-2, and SIV).
11733580	1	59	theme	immunodeficiency	292:307	arg1	viruses					309:315	human and simian immunodeficiency viruses	275:315	human and simian immunodeficiency viruses (HIV-1, HIV-2, and SIV)	275:339	The chemokine receptor CCR5 plays an important role in leukocyte chemotaxis and activation, and also acts as a coreceptor for human and simian immunodeficiency viruses (HIV-1, HIV-2, and SIV).
11733580	0	60	theme	chemokines	137:146	arg1	binding					126:132	high affinity binding	112:132	high affinity binding of chemokines	112:146	Sialylated O-glycans and sulfated tyrosines in the NH2-terminal domain of CC chemokine receptor 5 contribute to high affinity binding of chemokines.
11733580	6	61	theme	selectins	796:804	arg1	binding					785:791	the binding	781:791	the binding of selectins and their ligands	781:822	Thus, as has been observed for the binding of selectins and their ligands, O-linked carbohydrates and tyrosine sulfates play major roles in promoting the interaction of chemokines with CCR5.
11733580	7	62	with	interactions	1045:1056	arg1	ligands					1081:1087	diverse chemokine ligands	1063:1087	diverse chemokine ligands	1063:1087	The resulting flexible arrays of negative charges on the CCR5 surface may allow specific, high-affinity interactions with diverse chemokine ligands.
11733580	5	63	theme	specific	646:653	arg1	residues					664:671	specific tyrosine residues	646:671	specific tyrosine residues in the CCR5 NH2 terminus	646:696	Sulfation of specific tyrosine residues in the CCR5 NH2 terminus was important for efficient beta-chemokine binding.
11733580	8	64	theme	serines	1233:1239	arg1	density					1222:1228	the high density	1213:1228	the high density of serines, threonines and tyrosines in the N-termini of many CC chemokine receptors	1213:1313	Although this is the first example of O-linked oligosaccharides and tyrosine sulfates playing a role in chemokine binding, the high density of serines, threonines and tyrosines in the N-termini of many CC chemokine receptors suggests that these posttranslational modifications may commonly contribute to chemokine binding.
11733580	5	65	theme	tyrosine	655:662	arg1	residues					664:671	specific tyrosine residues	646:671	specific tyrosine residues in the CCR5 NH2 terminus	646:696	Sulfation of specific tyrosine residues in the CCR5 NH2 terminus was important for efficient beta-chemokine binding.
11733580	8	66	from	density	1222:1228	arg1	N-termini					1274:1282	the N-termini	1270:1282	the N-termini of many CC chemokine receptors	1270:1313	Although this is the first example of O-linked oligosaccharides and tyrosine sulfates playing a role in chemokine binding, the high density of serines, threonines and tyrosines in the N-termini of many CC chemokine receptors suggests that these posttranslational modifications may commonly contribute to chemokine binding.
11733580	8	67	theme	chemokine	1394:1402	arg1	binding					1404:1410	chemokine binding	1394:1410	chemokine binding	1394:1410	Although this is the first example of O-linked oligosaccharides and tyrosine sulfates playing a role in chemokine binding, the high density of serines, threonines and tyrosines in the N-termini of many CC chemokine receptors suggests that these posttranslational modifications may commonly contribute to chemokine binding.
11733580	7	68	theme	resulting	945:953	arg1	arrays					964:969	The resulting flexible arrays	941:969	The resulting flexible arrays of negative charges on the CCR5 surface	941:1009	The resulting flexible arrays of negative charges on the CCR5 surface may allow specific, high-affinity interactions with diverse chemokine ligands.
11733580	3	69	theme	O-linked	427:434	arg1	glycans					436:442	The O-linked glycans	423:442	The O-linked glycans	423:442	The O-linked glycans, particularly sialic acid moieties, significantly contribute to binding of the chemokine ligands.
11733580	3	69	theme	O-linked	427:434	arg1	moieties					470:477	sialic acid moieties	458:477	particularly sialic acid moieties	445:477	The O-linked glycans, particularly sialic acid moieties, significantly contribute to binding of the chemokine ligands.
11733580	8	70	theme	chemokine	1194:1202	arg1	binding					1204:1210	chemokine binding	1194:1210	chemokine binding	1194:1210	Although this is the first example of O-linked oligosaccharides and tyrosine sulfates playing a role in chemokine binding, the high density of serines, threonines and tyrosines in the N-termini of many CC chemokine receptors suggests that these posttranslational modifications may commonly contribute to chemokine binding.
11733580	4	71	theme	little	599:604	arg1	effect					606:611	little effect	599:611	little effect	599:611	By contrast, removal of O-linked oligosaccharide exerted little effect on HIV-1 infection.
11733580	7	72	theme	flexible	955:962	arg1	arrays					964:969	The resulting flexible arrays	941:969	The resulting flexible arrays of negative charges on the CCR5 surface	941:1009	The resulting flexible arrays of negative charges on the CCR5 surface may allow specific, high-affinity interactions with diverse chemokine ligands.
11733580	3	73	theme	acid	465:468	arg1	glycans					436:442	The O-linked glycans	423:442	The O-linked glycans	423:442	The O-linked glycans, particularly sialic acid moieties, significantly contribute to binding of the chemokine ligands.
11733580	3	73	theme	acid	465:468	arg1	moieties					470:477	sialic acid moieties	458:477	particularly sialic acid moieties	445:477	The O-linked glycans, particularly sialic acid moieties, significantly contribute to binding of the chemokine ligands.
11733580	5	74	from	terminus	689:696	arg1	Sulfation					633:641	Sulfation	633:641	Sulfation of specific tyrosine residues in the CCR5 NH2 terminus	633:696	Sulfation of specific tyrosine residues in the CCR5 NH2 terminus was important for efficient beta-chemokine binding.
11733580	4	75	theme	O-linked	566:573	arg1	oligosaccharide					575:589	O-linked oligosaccharide	566:589	O-linked oligosaccharide	566:589	By contrast, removal of O-linked oligosaccharide exerted little effect on HIV-1 infection.
11733580	2	76	theme	NH2	409:411	arg1	terminus					413:420	the NH2 terminus	405:420	the NH2 terminus	405:420	We provide evidence that CCR5 is O-glycosylated on serine 6 in the NH2 terminus.
11733580	7	77	from	charges	983:989	arg1	surface					1003:1009	the CCR5 surface	994:1009	the CCR5 surface	994:1009	The resulting flexible arrays of negative charges on the CCR5 surface may allow specific, high-affinity interactions with diverse chemokine ligands.
11733580	5	78	theme	residues	664:671	arg1	Sulfation					633:641	Sulfation	633:641	Sulfation of specific tyrosine residues in the CCR5 NH2 terminus	633:696	Sulfation of specific tyrosine residues in the CCR5 NH2 terminus was important for efficient beta-chemokine binding.
11733580	2	79	from	O-glycosylated	375:388	arg1	terminus					413:420	the NH2 terminus	405:420	the NH2 terminus	405:420	We provide evidence that CCR5 is O-glycosylated on serine 6 in the NH2 terminus.
11733580	2	79	from	O-glycosylated	375:388	arg1	serine					393:398	serine 6	393:400	serine 6	393:400	We provide evidence that CCR5 is O-glycosylated on serine 6 in the NH2 terminus.
11733580	8	80	theme	threonines	1242:1251	arg1	density					1222:1228	the high density	1213:1228	the high density of serines, threonines and tyrosines in the N-termini of many CC chemokine receptors	1213:1313	Although this is the first example of O-linked oligosaccharides and tyrosine sulfates playing a role in chemokine binding, the high density of serines, threonines and tyrosines in the N-termini of many CC chemokine receptors suggests that these posttranslational modifications may commonly contribute to chemokine binding.
11733580	7	81	from	surface	1003:1009	arg1	arrays					964:969	The resulting flexible arrays	941:969	The resulting flexible arrays of negative charges on the CCR5 surface	941:1009	The resulting flexible arrays of negative charges on the CCR5 surface may allow specific, high-affinity interactions with diverse chemokine ligands.
15084671	5	0	theme	lectin	535:540	arg1	chromatography					551:564	lectin affinity chromatography	535:564	lectin affinity chromatography	535:564	Using lectin affinity chromatography and enzymatically labeling of asparagine residues carrying glycan moieties by (18)O, we have identified a total of 33 glycosylation sites.
15084671	7	1	theme	differential	873:884	arg1	proteomics					886:895	differential proteomics	873:895	differential proteomics	873:895	In combination with "tagging" approaches for differential proteomics, our method could be used for identification of cancer biomarkers from any body fluid.
15084671	6	2	theme	most	810:813	arg1	fluids					820:825	most body fluids	810:825	most body fluids	810:825	The strategy described in this study should be generally applicable for a detailed proteomic analysis of most body fluids.
15084671	7	3	theme	"	856:856	arg1	approaches					858:867	"tagging" approaches	848:867	"tagging" approaches for differential proteomics	848:895	In combination with "tagging" approaches for differential proteomics, our method could be used for identification of cancer biomarkers from any body fluid.
15084671	3	4	theme	several	363:369	arg1	proteins					377:384	several novel proteins	363:384	several novel proteins as well as known proteins whose functions are unknown	363:438	Overall, we identified 87 unique proteins, including several novel proteins as well as known proteins whose functions are unknown.
15084671	5	5	theme	glycan	625:630	arg1	O					648:648	glycan moieties by (18)O	625:648	glycan moieties by (18)O	625:648	Using lectin affinity chromatography and enzymatically labeling of asparagine residues carrying glycan moieties by (18)O, we have identified a total of 33 glycosylation sites.
15084671	3	6	theme	novel	371:375	arg1	proteins					377:384	several novel proteins	363:384	several novel proteins as well as known proteins whose functions are unknown	363:438	Overall, we identified 87 unique proteins, including several novel proteins as well as known proteins whose functions are unknown.
15084671	4	7	theme	proteins	476:483	arg1	majority					449:456	A large majority	441:456	A large majority of the identified proteins	441:483	A large majority of the identified proteins have not been previously described in bile.
15084671	5	8	theme	moieties	632:639	arg1	O					648:648	glycan moieties by (18)O	625:648	glycan moieties by (18)O	625:648	Using lectin affinity chromatography and enzymatically labeling of asparagine residues carrying glycan moieties by (18)O, we have identified a total of 33 glycosylation sites.
15084671	2	9	theme	mass	291:294	arg1	spectrometry					296:307	liquid chromatography tandem mass spectrometry	262:307	liquid chromatography tandem mass spectrometry	262:307	Our approach involved fractionation of bile by one-dimensional gel electrophoresis and lectin affinity chromatography followed by liquid chromatography tandem mass spectrometry.
15084671	4	10	theme	identified	465:474	arg1	proteins					476:483	the identified proteins	461:483	the identified proteins	461:483	A large majority of the identified proteins have not been previously described in bile.
15084671	5	11	theme	by	641:642	arg1	O					648:648	glycan moieties by (18)O	625:648	glycan moieties by (18)O	625:648	Using lectin affinity chromatography and enzymatically labeling of asparagine residues carrying glycan moieties by (18)O, we have identified a total of 33 glycosylation sites.
15084671	2	12	theme	tandem	284:289	arg1	spectrometry					296:307	liquid chromatography tandem mass spectrometry	262:307	liquid chromatography tandem mass spectrometry	262:307	Our approach involved fractionation of bile by one-dimensional gel electrophoresis and lectin affinity chromatography followed by liquid chromatography tandem mass spectrometry.
15084671	7	13	theme	tagging	849:855	arg1	approaches					858:867	"tagging" approaches	848:867	"tagging" approaches for differential proteomics	848:895	In combination with "tagging" approaches for differential proteomics, our method could be used for identification of cancer biomarkers from any body fluid.
15084671	6	14	theme	detailed	779:786	arg1	analysis					798:805	a detailed proteomic analysis	777:805	a detailed proteomic analysis of most body fluids	777:825	The strategy described in this study should be generally applicable for a detailed proteomic analysis of most body fluids.
15084671	2	15	theme	chromatography	269:282	arg1	spectrometry					296:307	liquid chromatography tandem mass spectrometry	262:307	liquid chromatography tandem mass spectrometry	262:307	Our approach involved fractionation of bile by one-dimensional gel electrophoresis and lectin affinity chromatography followed by liquid chromatography tandem mass spectrometry.
15084671	0	16	theme	proteomic	2:10	arg1	analysis					12:19	A proteomic analysis	0:19	A proteomic analysis of human bile	0:33	A proteomic analysis of human bile.
15084671	1	17	theme	comprehensive	58:70	arg1	characterization					72:87	a comprehensive characterization	56:87	a comprehensive characterization of human bile	56:101	We have carried out a comprehensive characterization of human bile to define the bile proteome.
15084671	6	18	theme	body	815:818	arg1	fluids					820:825	most body fluids	810:825	most body fluids	810:825	The strategy described in this study should be generally applicable for a detailed proteomic analysis of most body fluids.
15084671	5	19	theme	asparagine	596:605	arg1	residues					607:614	asparagine residues	596:614	asparagine residues carrying glycan moieties by (18)O	596:648	Using lectin affinity chromatography and enzymatically labeling of asparagine residues carrying glycan moieties by (18)O, we have identified a total of 33 glycosylation sites.
15084671	7	20	with	combination	831:841	arg1	approaches					858:867	"tagging" approaches	848:867	"tagging" approaches for differential proteomics	848:895	In combination with "tagging" approaches for differential proteomics, our method could be used for identification of cancer biomarkers from any body fluid.
15084671	5	21	contain	carrying	616:623	arg1	residues					607:614	asparagine residues	596:614	asparagine residues carrying glycan moieties by (18)O	596:648	Using lectin affinity chromatography and enzymatically labeling of asparagine residues carrying glycan moieties by (18)O, we have identified a total of 33 glycosylation sites.
15084671	5	21	contain	carrying	616:623	arg2	O					648:648	glycan moieties by (18)O	625:648	glycan moieties by (18)O	625:648	Using lectin affinity chromatography and enzymatically labeling of asparagine residues carrying glycan moieties by (18)O, we have identified a total of 33 glycosylation sites.
15084671	5	22	theme	glycosylation	684:696	arg1	sites					698:702	33 glycosylation sites	681:702	33 glycosylation sites	681:702	Using lectin affinity chromatography and enzymatically labeling of asparagine residues carrying glycan moieties by (18)O, we have identified a total of 33 glycosylation sites.
15084671	5	23	theme	residues	607:614	arg1	chromatography					551:564	lectin affinity chromatography	535:564	lectin affinity chromatography	535:564	Using lectin affinity chromatography and enzymatically labeling of asparagine residues carrying glycan moieties by (18)O, we have identified a total of 33 glycosylation sites.
15084671	5	23	theme	residues	607:614	arg1	labeling					584:591	labeling	584:591	labeling of asparagine residues carrying glycan moieties by (18)O	584:648	Using lectin affinity chromatography and enzymatically labeling of asparagine residues carrying glycan moieties by (18)O, we have identified a total of 33 glycosylation sites.
15084671	7	24	theme	cancer	945:950	arg1	biomarkers					952:961	cancer biomarkers	945:961	cancer biomarkers from any body fluid	945:981	In combination with "tagging" approaches for differential proteomics, our method could be used for identification of cancer biomarkers from any body fluid.
15084671	5	25	theme	sites	698:702	arg1	total					672:676	a total	670:676	a total of 33 glycosylation sites	670:702	Using lectin affinity chromatography and enzymatically labeling of asparagine residues carrying glycan moieties by (18)O, we have identified a total of 33 glycosylation sites.
15084671	1	26	theme	human	92:96	arg1	bile					98:101	human bile	92:101	human bile	92:101	We have carried out a comprehensive characterization of human bile to define the bile proteome.
15084671	7	27	from	identification	927:940	arg1	fluid					977:981	any body fluid	968:981	any body fluid	968:981	In combination with "tagging" approaches for differential proteomics, our method could be used for identification of cancer biomarkers from any body fluid.
15084671	0	28	theme	bile	30:33	arg1	analysis					12:19	A proteomic analysis	0:19	A proteomic analysis of human bile	0:33	A proteomic analysis of human bile.
15084671	4	29	theme	large	443:447	arg1	majority					449:456	A large majority	441:456	A large majority of the identified proteins	441:483	A large majority of the identified proteins have not been previously described in bile.
15084671	2	30	theme	affinity	226:233	arg1	chromatography					235:248	lectin affinity chromatography	219:248	lectin affinity chromatography	219:248	Our approach involved fractionation of bile by one-dimensional gel electrophoresis and lectin affinity chromatography followed by liquid chromatography tandem mass spectrometry.
15084671	7	31	used	used	918:921	arg2	method					902:907	our method	898:907	our method	898:907	In combination with "tagging" approaches for differential proteomics, our method could be used for identification of cancer biomarkers from any body fluid.
15084671	0	32	theme	human	24:28	arg1	bile					30:33	human bile	24:33	human bile	24:33	A proteomic analysis of human bile.
15084671	2	33	theme	lectin	219:224	arg1	chromatography					235:248	lectin affinity chromatography	219:248	lectin affinity chromatography	219:248	Our approach involved fractionation of bile by one-dimensional gel electrophoresis and lectin affinity chromatography followed by liquid chromatography tandem mass spectrometry.
15084671	5	34	theme	affinity	542:549	arg1	chromatography					551:564	lectin affinity chromatography	535:564	lectin affinity chromatography	535:564	Using lectin affinity chromatography and enzymatically labeling of asparagine residues carrying glycan moieties by (18)O, we have identified a total of 33 glycosylation sites.
15084671	3	35	theme	known	397:401	arg1	proteins					403:410	known proteins	397:410	several novel proteins as well as known proteins whose functions are unknown	363:438	Overall, we identified 87 unique proteins, including several novel proteins as well as known proteins whose functions are unknown.
15084671	7	36	from	fluid	977:981	arg1	identification					927:940	identification	927:940	identification of cancer biomarkers from any body fluid	927:981	In combination with "tagging" approaches for differential proteomics, our method could be used for identification of cancer biomarkers from any body fluid.
15084671	7	36	from	fluid	977:981	arg1	biomarkers					952:961	cancer biomarkers	945:961	cancer biomarkers from any body fluid	945:981	In combination with "tagging" approaches for differential proteomics, our method could be used for identification of cancer biomarkers from any body fluid.
15084671	1	37	theme	bile	98:101	arg1	characterization					72:87	a comprehensive characterization	56:87	a comprehensive characterization of human bile	56:101	We have carried out a comprehensive characterization of human bile to define the bile proteome.
15084671	2	38	theme	gel	195:197	arg1	electrophoresis					199:213	one-dimensional gel electrophoresis	179:213	one-dimensional gel electrophoresis	179:213	Our approach involved fractionation of bile by one-dimensional gel electrophoresis and lectin affinity chromatography followed by liquid chromatography tandem mass spectrometry.
15084671	5	39	gly	glycosylation	684:696	arg2	sites					698:702	33 glycosylation sites	681:702	33 glycosylation sites	681:702	Using lectin affinity chromatography and enzymatically labeling of asparagine residues carrying glycan moieties by (18)O, we have identified a total of 33 glycosylation sites.
15084671	5	39	gly	glycosylation	684:696	arg2	33					681:682	33	681:682	33	681:682	Using lectin affinity chromatography and enzymatically labeling of asparagine residues carrying glycan moieties by (18)O, we have identified a total of 33 glycosylation sites.
15084671	2	40	theme	one-dimensional	179:193	arg1	electrophoresis					199:213	one-dimensional gel electrophoresis	179:213	one-dimensional gel electrophoresis	179:213	Our approach involved fractionation of bile by one-dimensional gel electrophoresis and lectin affinity chromatography followed by liquid chromatography tandem mass spectrometry.
15084671	2	41	theme	liquid	262:267	arg1	spectrometry					296:307	liquid chromatography tandem mass spectrometry	262:307	liquid chromatography tandem mass spectrometry	262:307	Our approach involved fractionation of bile by one-dimensional gel electrophoresis and lectin affinity chromatography followed by liquid chromatography tandem mass spectrometry.
15084671	7	42	theme	biomarkers	952:961	arg1	identification					927:940	identification	927:940	identification of cancer biomarkers from any body fluid	927:981	In combination with "tagging" approaches for differential proteomics, our method could be used for identification of cancer biomarkers from any body fluid.
15084671	6	43	theme	fluids	820:825	arg1	analysis					798:805	a detailed proteomic analysis	777:805	a detailed proteomic analysis of most body fluids	777:825	The strategy described in this study should be generally applicable for a detailed proteomic analysis of most body fluids.
15084671	7	44	theme	body	972:975	arg1	fluid					977:981	any body fluid	968:981	any body fluid	968:981	In combination with "tagging" approaches for differential proteomics, our method could be used for identification of cancer biomarkers from any body fluid.
15084671	1	45	dep	carried	44:50	arg1	out					52:54	out	52:54	out	52:54	We have carried out a comprehensive characterization of human bile to define the bile proteome.
15084671	6	46	theme	proteomic	788:796	arg1	analysis					798:805	a detailed proteomic analysis	777:805	a detailed proteomic analysis of most body fluids	777:825	The strategy described in this study should be generally applicable for a detailed proteomic analysis of most body fluids.
15084671	3	47	theme	unique	336:341	arg1	proteins					403:410	known proteins	397:410	several novel proteins as well as known proteins whose functions are unknown	363:438	Overall, we identified 87 unique proteins, including several novel proteins as well as known proteins whose functions are unknown.
15084671	3	47	theme	unique	336:341	arg1	proteins					377:384	several novel proteins	363:384	several novel proteins as well as known proteins whose functions are unknown	363:438	Overall, we identified 87 unique proteins, including several novel proteins as well as known proteins whose functions are unknown.
15084671	3	47	theme	unique	336:341	arg1	proteins					343:350	87 unique proteins	333:350	87 unique proteins	333:350	Overall, we identified 87 unique proteins, including several novel proteins as well as known proteins whose functions are unknown.
15084671	2	48	theme	bile	171:174	arg1	fractionation					154:166	fractionation	154:166	fractionation of bile	154:174	Our approach involved fractionation of bile by one-dimensional gel electrophoresis and lectin affinity chromatography followed by liquid chromatography tandem mass spectrometry.
15084671	1	49	theme	bile	117:120	arg1	proteome					122:129	the bile proteome	113:129	the bile proteome	113:129	We have carried out a comprehensive characterization of human bile to define the bile proteome.
7781780	0	0	theme	human	113:117	arg1	erythropoietin					119:132	human erythropoietin	113:132	human erythropoietin	113:132	Identification and structural characterization of a mannose-6-phosphate containing oligomannosidic N-glycan from human erythropoietin secreted by recombinant BHK-21 cells.
7781780	2	1	theme	type	532:535	arg1	structure					537:545	a high mannose type structure	517:545	a high mannose type structure (Man6)	517:552	Mass spectrometry and both 1- and 2-dimensional NMR techniques revealed a high mannose type structure (Man6) with a phospho-diesterbridged N-acetylglucosamine as follows: [formula: see text]
7781780	2	1	theme	type	532:535	arg1	Man6					548:551	Man6	548:551	Man6	548:551	Mass spectrometry and both 1- and 2-dimensional NMR techniques revealed a high mannose type structure (Man6) with a phospho-diesterbridged N-acetylglucosamine as follows: [formula: see text]
7781780	2	2	dep	revealed	508:515	arg1	[formula					616:623	[formula	616:623	[formula: see text]	616:634	Mass spectrometry and both 1- and 2-dimensional NMR techniques revealed a high mannose type structure (Man6) with a phospho-diesterbridged N-acetylglucosamine as follows: [formula: see text]
7781780	1	3	theme	mono-charged	194:205	arg1	N-glycan					207:214	A sialidase resistant mono-charged N-glycan	172:214	A sialidase resistant mono-charged N-glycan	172:214	A sialidase resistant mono-charged N-glycan was isolated from glycosylation site I (Asn-24) of recombinant human erythropoietin expressed from baby hamster kidney (BHK-21) cells and constituted approximately 2-4% of the oligosaccharide material at this glycosylation site.
7781780	1	4	theme	erythropoietin	285:298	arg1	erythropoietin					285:298	recombinant human erythropoietin	267:298	recombinant human erythropoietin expressed from baby hamster kidney (BHK-21) cells	267:348	A sialidase resistant mono-charged N-glycan was isolated from glycosylation site I (Asn-24) of recombinant human erythropoietin expressed from baby hamster kidney (BHK-21) cells and constituted approximately 2-4% of the oligosaccharide material at this glycosylation site.
7781780	1	4	theme	erythropoietin	285:298	arg1	site					248:251	glycosylation site I	234:253	glycosylation site I (Asn-24) of recombinant human erythropoietin expressed from baby hamster kidney (BHK-21) cells	234:348	A sialidase resistant mono-charged N-glycan was isolated from glycosylation site I (Asn-24) of recombinant human erythropoietin expressed from baby hamster kidney (BHK-21) cells and constituted approximately 2-4% of the oligosaccharide material at this glycosylation site.
7781780	1	4	theme	erythropoietin	285:298	arg1	Asn-24					256:261	Asn-24	256:261	Asn-24	256:261	A sialidase resistant mono-charged N-glycan was isolated from glycosylation site I (Asn-24) of recombinant human erythropoietin expressed from baby hamster kidney (BHK-21) cells and constituted approximately 2-4% of the oligosaccharide material at this glycosylation site.
7781780	2	5	theme	mannose	524:530	arg1	structure					537:545	a high mannose type structure	517:545	a high mannose type structure (Man6)	517:552	Mass spectrometry and both 1- and 2-dimensional NMR techniques revealed a high mannose type structure (Man6) with a phospho-diesterbridged N-acetylglucosamine as follows: [formula: see text]
7781780	2	5	theme	mannose	524:530	arg1	Man6					548:551	Man6	548:551	Man6	548:551	Mass spectrometry and both 1- and 2-dimensional NMR techniques revealed a high mannose type structure (Man6) with a phospho-diesterbridged N-acetylglucosamine as follows: [formula: see text]
7781780	0	6	from	Identification	0:13	arg1	erythropoietin					119:132	human erythropoietin	113:132	human erythropoietin	113:132	Identification and structural characterization of a mannose-6-phosphate containing oligomannosidic N-glycan from human erythropoietin secreted by recombinant BHK-21 cells.
7781780	1	7	gly	glycosylation	234:246	arg2	Asn-24					256:261	Asn-24	256:261	Asn-24	256:261	A sialidase resistant mono-charged N-glycan was isolated from glycosylation site I (Asn-24) of recombinant human erythropoietin expressed from baby hamster kidney (BHK-21) cells and constituted approximately 2-4% of the oligosaccharide material at this glycosylation site.
7781780	1	7	gly	glycosylation	234:246	arg2	I					253:253	I	253:253	I	253:253	A sialidase resistant mono-charged N-glycan was isolated from glycosylation site I (Asn-24) of recombinant human erythropoietin expressed from baby hamster kidney (BHK-21) cells and constituted approximately 2-4% of the oligosaccharide material at this glycosylation site.
7781780	1	7	gly	glycosylation	234:246	arg2	site					248:251	glycosylation site I	234:253	glycosylation site I (Asn-24) of recombinant human erythropoietin expressed from baby hamster kidney (BHK-21) cells	234:348	A sialidase resistant mono-charged N-glycan was isolated from glycosylation site I (Asn-24) of recombinant human erythropoietin expressed from baby hamster kidney (BHK-21) cells and constituted approximately 2-4% of the oligosaccharide material at this glycosylation site.
7781780	1	7	gly	glycosylation	234:246	arg1	erythropoietin					285:298	recombinant human erythropoietin	267:298	recombinant human erythropoietin expressed from baby hamster kidney (BHK-21) cells	267:348	A sialidase resistant mono-charged N-glycan was isolated from glycosylation site I (Asn-24) of recombinant human erythropoietin expressed from baby hamster kidney (BHK-21) cells and constituted approximately 2-4% of the oligosaccharide material at this glycosylation site.
7781780	1	7	gly	glycosylation	234:246	arg2	erythropoietin					285:298	recombinant human erythropoietin	267:298	recombinant human erythropoietin expressed from baby hamster kidney (BHK-21) cells	267:348	A sialidase resistant mono-charged N-glycan was isolated from glycosylation site I (Asn-24) of recombinant human erythropoietin expressed from baby hamster kidney (BHK-21) cells and constituted approximately 2-4% of the oligosaccharide material at this glycosylation site.
7781780	1	8	theme	baby	315:318	arg1	BHK-21					336:341	BHK-21	336:341	BHK-21	336:341	A sialidase resistant mono-charged N-glycan was isolated from glycosylation site I (Asn-24) of recombinant human erythropoietin expressed from baby hamster kidney (BHK-21) cells and constituted approximately 2-4% of the oligosaccharide material at this glycosylation site.
7781780	1	8	theme	baby	315:318	arg1	kidney					328:333	baby hamster kidney	315:333	baby hamster kidney (BHK-21) cells	315:348	A sialidase resistant mono-charged N-glycan was isolated from glycosylation site I (Asn-24) of recombinant human erythropoietin expressed from baby hamster kidney (BHK-21) cells and constituted approximately 2-4% of the oligosaccharide material at this glycosylation site.
7781780	0	9	theme	recombinant	146:156	arg1	cells					165:169	recombinant BHK-21 cells	146:169	recombinant BHK-21 cells	146:169	Identification and structural characterization of a mannose-6-phosphate containing oligomannosidic N-glycan from human erythropoietin secreted by recombinant BHK-21 cells.
7781780	1	10	theme	oligosaccharide	392:406	arg1	material					408:415	the oligosaccharide material	388:415	the oligosaccharide material	388:415	A sialidase resistant mono-charged N-glycan was isolated from glycosylation site I (Asn-24) of recombinant human erythropoietin expressed from baby hamster kidney (BHK-21) cells and constituted approximately 2-4% of the oligosaccharide material at this glycosylation site.
7781780	1	11	theme	material	408:415	arg1	%					383:383	approximately 2-4%	366:383	approximately 2-4% of the oligosaccharide material	366:415	A sialidase resistant mono-charged N-glycan was isolated from glycosylation site I (Asn-24) of recombinant human erythropoietin expressed from baby hamster kidney (BHK-21) cells and constituted approximately 2-4% of the oligosaccharide material at this glycosylation site.
7781780	1	11	theme	material	408:415	arg1	material					408:415	the oligosaccharide material	388:415	the oligosaccharide material	388:415	A sialidase resistant mono-charged N-glycan was isolated from glycosylation site I (Asn-24) of recombinant human erythropoietin expressed from baby hamster kidney (BHK-21) cells and constituted approximately 2-4% of the oligosaccharide material at this glycosylation site.
7781780	2	12	theme	NMR	493:495	arg1	techniques					497:506	2-dimensional NMR techniques	479:506	2-dimensional NMR techniques	479:506	Mass spectrometry and both 1- and 2-dimensional NMR techniques revealed a high mannose type structure (Man6) with a phospho-diesterbridged N-acetylglucosamine as follows: [formula: see text]
7781780	2	13	dep	[formula	616:623	arg1	see					626:628	see	626:628	see text	626:633	Mass spectrometry and both 1- and 2-dimensional NMR techniques revealed a high mannose type structure (Man6) with a phospho-diesterbridged N-acetylglucosamine as follows: [formula: see text]
7781780	2	14	theme	2-dimensional	479:491	arg1	techniques					497:506	2-dimensional NMR techniques	479:506	2-dimensional NMR techniques	479:506	Mass spectrometry and both 1- and 2-dimensional NMR techniques revealed a high mannose type structure (Man6) with a phospho-diesterbridged N-acetylglucosamine as follows: [formula: see text]
7781780	1	15	theme	hamster	320:326	arg1	BHK-21					336:341	BHK-21	336:341	BHK-21	336:341	A sialidase resistant mono-charged N-glycan was isolated from glycosylation site I (Asn-24) of recombinant human erythropoietin expressed from baby hamster kidney (BHK-21) cells and constituted approximately 2-4% of the oligosaccharide material at this glycosylation site.
7781780	1	15	theme	hamster	320:326	arg1	kidney					328:333	baby hamster kidney	315:333	baby hamster kidney (BHK-21) cells	315:348	A sialidase resistant mono-charged N-glycan was isolated from glycosylation site I (Asn-24) of recombinant human erythropoietin expressed from baby hamster kidney (BHK-21) cells and constituted approximately 2-4% of the oligosaccharide material at this glycosylation site.
7781780	1	16	theme	glycosylation	234:246	arg1	erythropoietin					285:298	recombinant human erythropoietin	267:298	recombinant human erythropoietin expressed from baby hamster kidney (BHK-21) cells	267:348	A sialidase resistant mono-charged N-glycan was isolated from glycosylation site I (Asn-24) of recombinant human erythropoietin expressed from baby hamster kidney (BHK-21) cells and constituted approximately 2-4% of the oligosaccharide material at this glycosylation site.
7781780	1	16	theme	glycosylation	234:246	arg1	site					248:251	glycosylation site I	234:253	glycosylation site I (Asn-24) of recombinant human erythropoietin expressed from baby hamster kidney (BHK-21) cells	234:348	A sialidase resistant mono-charged N-glycan was isolated from glycosylation site I (Asn-24) of recombinant human erythropoietin expressed from baby hamster kidney (BHK-21) cells and constituted approximately 2-4% of the oligosaccharide material at this glycosylation site.
7781780	1	16	theme	glycosylation	234:246	arg1	Asn-24					256:261	Asn-24	256:261	Asn-24	256:261	A sialidase resistant mono-charged N-glycan was isolated from glycosylation site I (Asn-24) of recombinant human erythropoietin expressed from baby hamster kidney (BHK-21) cells and constituted approximately 2-4% of the oligosaccharide material at this glycosylation site.
7781780	1	17	theme	kidney	328:333	arg1	cells					344:348	baby hamster kidney (BHK-21) cells	315:348	baby hamster kidney (BHK-21) cells	315:348	A sialidase resistant mono-charged N-glycan was isolated from glycosylation site I (Asn-24) of recombinant human erythropoietin expressed from baby hamster kidney (BHK-21) cells and constituted approximately 2-4% of the oligosaccharide material at this glycosylation site.
7781780	0	18	theme	structural	19:28	arg1	characterization					30:45	structural characterization	19:45	structural characterization	19:45	Identification and structural characterization of a mannose-6-phosphate containing oligomannosidic N-glycan from human erythropoietin secreted by recombinant BHK-21 cells.
7781780	0	19	theme	BHK-21	158:163	arg1	cells					165:169	recombinant BHK-21 cells	146:169	recombinant BHK-21 cells	146:169	Identification and structural characterization of a mannose-6-phosphate containing oligomannosidic N-glycan from human erythropoietin secreted by recombinant BHK-21 cells.
7781780	1	20	attach	isolated	220:227	arg2	N-glycan					207:214	A sialidase resistant mono-charged N-glycan	172:214	A sialidase resistant mono-charged N-glycan	172:214	A sialidase resistant mono-charged N-glycan was isolated from glycosylation site I (Asn-24) of recombinant human erythropoietin expressed from baby hamster kidney (BHK-21) cells and constituted approximately 2-4% of the oligosaccharide material at this glycosylation site.
7781780	1	20	attach	isolated	220:227	arg1	erythropoietin					285:298	recombinant human erythropoietin	267:298	recombinant human erythropoietin expressed from baby hamster kidney (BHK-21) cells	267:348	A sialidase resistant mono-charged N-glycan was isolated from glycosylation site I (Asn-24) of recombinant human erythropoietin expressed from baby hamster kidney (BHK-21) cells and constituted approximately 2-4% of the oligosaccharide material at this glycosylation site.
7781780	1	20	attach	isolated	220:227	arg1	site					248:251	glycosylation site I	234:253	glycosylation site I (Asn-24) of recombinant human erythropoietin expressed from baby hamster kidney (BHK-21) cells	234:348	A sialidase resistant mono-charged N-glycan was isolated from glycosylation site I (Asn-24) of recombinant human erythropoietin expressed from baby hamster kidney (BHK-21) cells and constituted approximately 2-4% of the oligosaccharide material at this glycosylation site.
7781780	1	20	attach	isolated	220:227	arg1	Asn-24					256:261	Asn-24	256:261	Asn-24	256:261	A sialidase resistant mono-charged N-glycan was isolated from glycosylation site I (Asn-24) of recombinant human erythropoietin expressed from baby hamster kidney (BHK-21) cells and constituted approximately 2-4% of the oligosaccharide material at this glycosylation site.
7781780	2	21	theme	high	519:522	arg1	structure					537:545	a high mannose type structure	517:545	a high mannose type structure (Man6)	517:552	Mass spectrometry and both 1- and 2-dimensional NMR techniques revealed a high mannose type structure (Man6) with a phospho-diesterbridged N-acetylglucosamine as follows: [formula: see text]
7781780	2	21	theme	high	519:522	arg1	Man6					548:551	Man6	548:551	Man6	548:551	Mass spectrometry and both 1- and 2-dimensional NMR techniques revealed a high mannose type structure (Man6) with a phospho-diesterbridged N-acetylglucosamine as follows: [formula: see text]
7781780	1	22	theme	glycosylation	425:437	arg1	site					439:442	this glycosylation site	420:442	this glycosylation site	420:442	A sialidase resistant mono-charged N-glycan was isolated from glycosylation site I (Asn-24) of recombinant human erythropoietin expressed from baby hamster kidney (BHK-21) cells and constituted approximately 2-4% of the oligosaccharide material at this glycosylation site.
7781780	2	23	theme	phospho-diesterbridged	561:582	arg1	N-acetylglucosamine					584:602	a phospho-diesterbridged N-acetylglucosamine	559:602	a phospho-diesterbridged N-acetylglucosamine	559:602	Mass spectrometry and both 1- and 2-dimensional NMR techniques revealed a high mannose type structure (Man6) with a phospho-diesterbridged N-acetylglucosamine as follows: [formula: see text]
7781780	2	24	theme	Mass	445:448	arg1	spectrometry					450:461	Mass spectrometry	445:461	Mass spectrometry	445:461	Mass spectrometry and both 1- and 2-dimensional NMR techniques revealed a high mannose type structure (Man6) with a phospho-diesterbridged N-acetylglucosamine as follows: [formula: see text]
7781780	0	25	theme	containing	72:81	arg1	N-glycan					99:106	a mannose-6-phosphate containing oligomannosidic N-glycan	50:106	a mannose-6-phosphate containing oligomannosidic N-glycan from human erythropoietin	50:132	Identification and structural characterization of a mannose-6-phosphate containing oligomannosidic N-glycan from human erythropoietin secreted by recombinant BHK-21 cells.
7781780	0	26	theme	mannose-6-phosphate	52:70	arg1	N-glycan					99:106	a mannose-6-phosphate containing oligomannosidic N-glycan	50:106	a mannose-6-phosphate containing oligomannosidic N-glycan from human erythropoietin	50:132	Identification and structural characterization of a mannose-6-phosphate containing oligomannosidic N-glycan from human erythropoietin secreted by recombinant BHK-21 cells.
7781780	1	27	gly	glycosylation	425:437	arg2	site					439:442	this glycosylation site	420:442	this glycosylation site	420:442	A sialidase resistant mono-charged N-glycan was isolated from glycosylation site I (Asn-24) of recombinant human erythropoietin expressed from baby hamster kidney (BHK-21) cells and constituted approximately 2-4% of the oligosaccharide material at this glycosylation site.
7781780	0	28	theme	N-glycan	99:106	arg1	Identification					0:13	Identification	0:13	Identification	0:13	Identification and structural characterization of a mannose-6-phosphate containing oligomannosidic N-glycan from human erythropoietin secreted by recombinant BHK-21 cells.
7781780	0	28	theme	N-glycan	99:106	arg1	characterization					30:45	structural characterization	19:45	structural characterization	19:45	Identification and structural characterization of a mannose-6-phosphate containing oligomannosidic N-glycan from human erythropoietin secreted by recombinant BHK-21 cells.
7781780	0	29	from	erythropoietin	119:132	arg1	Identification					0:13	Identification	0:13	Identification	0:13	Identification and structural characterization of a mannose-6-phosphate containing oligomannosidic N-glycan from human erythropoietin secreted by recombinant BHK-21 cells.
7781780	0	29	from	erythropoietin	119:132	arg1	characterization					30:45	structural characterization	19:45	structural characterization	19:45	Identification and structural characterization of a mannose-6-phosphate containing oligomannosidic N-glycan from human erythropoietin secreted by recombinant BHK-21 cells.
7781780	0	29	from	erythropoietin	119:132	arg1	N-glycan					99:106	a mannose-6-phosphate containing oligomannosidic N-glycan	50:106	a mannose-6-phosphate containing oligomannosidic N-glycan from human erythropoietin	50:132	Identification and structural characterization of a mannose-6-phosphate containing oligomannosidic N-glycan from human erythropoietin secreted by recombinant BHK-21 cells.
7781780	1	30	theme	sialidase	174:182	arg1	N-glycan					207:214	A sialidase resistant mono-charged N-glycan	172:214	A sialidase resistant mono-charged N-glycan	172:214	A sialidase resistant mono-charged N-glycan was isolated from glycosylation site I (Asn-24) of recombinant human erythropoietin expressed from baby hamster kidney (BHK-21) cells and constituted approximately 2-4% of the oligosaccharide material at this glycosylation site.
7781780	1	31	theme	recombinant	267:277	arg1	erythropoietin					285:298	recombinant human erythropoietin	267:298	recombinant human erythropoietin expressed from baby hamster kidney (BHK-21) cells	267:348	A sialidase resistant mono-charged N-glycan was isolated from glycosylation site I (Asn-24) of recombinant human erythropoietin expressed from baby hamster kidney (BHK-21) cells and constituted approximately 2-4% of the oligosaccharide material at this glycosylation site.
7781780	0	32	theme	oligomannosidic	83:97	arg1	N-glycan					99:106	a mannose-6-phosphate containing oligomannosidic N-glycan	50:106	a mannose-6-phosphate containing oligomannosidic N-glycan from human erythropoietin	50:132	Identification and structural characterization of a mannose-6-phosphate containing oligomannosidic N-glycan from human erythropoietin secreted by recombinant BHK-21 cells.
7781780	0	33	from	characterization	30:45	arg1	erythropoietin					119:132	human erythropoietin	113:132	human erythropoietin	113:132	Identification and structural characterization of a mannose-6-phosphate containing oligomannosidic N-glycan from human erythropoietin secreted by recombinant BHK-21 cells.
7781780	1	34	theme	resistant	184:192	arg1	N-glycan					207:214	A sialidase resistant mono-charged N-glycan	172:214	A sialidase resistant mono-charged N-glycan	172:214	A sialidase resistant mono-charged N-glycan was isolated from glycosylation site I (Asn-24) of recombinant human erythropoietin expressed from baby hamster kidney (BHK-21) cells and constituted approximately 2-4% of the oligosaccharide material at this glycosylation site.
7781780	1	35	theme	human	279:283	arg1	erythropoietin					285:298	recombinant human erythropoietin	267:298	recombinant human erythropoietin expressed from baby hamster kidney (BHK-21) cells	267:348	A sialidase resistant mono-charged N-glycan was isolated from glycosylation site I (Asn-24) of recombinant human erythropoietin expressed from baby hamster kidney (BHK-21) cells and constituted approximately 2-4% of the oligosaccharide material at this glycosylation site.
11371615	7	0	theme	transcriptional	1288:1302	arg1	activation					1304:1313	transcriptional activation	1288:1313	transcriptional activation by native Sp1 in cells	1288:1336	Furthermore, overexpression of O-GlcNAc transferase specifically inhibits transcriptional activation by native Sp1 in cells.
11371615	5	1	theme	transcriptional	725:739	arg1	regulation					741:750	transcriptional regulation	725:750	transcriptional regulation	725:750	A linkage between transcription factor O-GlcNAcylation and transcriptional regulation therefore has been postulated.
11371615	4	2	mod	modified	644:651	arg1	factors					607:613	transcription factors	593:613	transcription factors	593:613	Meanwhile, transcription factors and RNA polymerase II can be modified by O-GlcNAc.
11371615	4	2	mod	modified	644:651	arg1	polymerase					623:632	RNA polymerase II	619:635	RNA polymerase II	619:635	Meanwhile, transcription factors and RNA polymerase II can be modified by O-GlcNAc.
11371615	4	2	mod	modified	644:651	arg3	O-GlcNAc					656:663	O-GlcNAc	656:663	O-GlcNAc	656:663	Meanwhile, transcription factors and RNA polymerase II can be modified by O-GlcNAc.
11371615	4	2	mod	modified	644:651	arg1	Meanwhile					582:590	Meanwhile	582:590	Meanwhile	582:590	Meanwhile, transcription factors and RNA polymerase II can be modified by O-GlcNAc.
11371615	6	3	theme	transcriptional	919:933	arg1	activity					935:942	its transcriptional activity	915:942	its transcriptional activity both in an in vitro transcription system and in living cells, which is in concert with our observation that O-GlcNAcylation of Sp1 activation domain blocks its in vitro and in vivo interactions with other Sp1 molecules and TATA-binding protein-associated factor II 110	915:1211	Here, we show that O-GlcNAcylation of a chimeric transcriptional activator containing the second activation domain of Sp1 decreases its transcriptional activity both in an in vitro transcription system and in living cells, which is in concert with our observation that O-GlcNAcylation of Sp1 activation domain blocks its in vitro and in vivo interactions with other Sp1 molecules and TATA-binding protein-associated factor II 110.
11371615	3	4	theme	genes	575:579	arg1	levels					560:565	transcriptional levels	544:565	transcriptional levels of some genes	544:579	The availability of UDP-GlcNAc correlates with glycosylation levels of intracellular proteins as well as with transcriptional levels of some genes.
11371615	8	5	theme	transcriptional	1442:1456	arg1	regulation					1458:1467	transcriptional regulation	1442:1467	transcriptional regulation	1442:1467	Thus, our studies provide direct evidence that O-GlcNAcylation of transcription factors is involved in transcriptional regulation.
11371615	6	6	dep	in	1104:1105	arg1	vitro					1107:1111	vitro	1107:1111	vitro	1107:1111	Here, we show that O-GlcNAcylation of a chimeric transcriptional activator containing the second activation domain of Sp1 decreases its transcriptional activity both in an in vitro transcription system and in living cells, which is in concert with our observation that O-GlcNAcylation of Sp1 activation domain blocks its in vitro and in vivo interactions with other Sp1 molecules and TATA-binding protein-associated factor II 110.
11371615	6	7	theme	domain	1086:1091	arg1	O-GlcNAcylation					1052:1066	O-GlcNAcylation	1052:1066	O-GlcNAcylation of Sp1 activation domain	1052:1091	Here, we show that O-GlcNAcylation of a chimeric transcriptional activator containing the second activation domain of Sp1 decreases its transcriptional activity both in an in vitro transcription system and in living cells, which is in concert with our observation that O-GlcNAcylation of Sp1 activation domain blocks its in vitro and in vivo interactions with other Sp1 molecules and TATA-binding protein-associated factor II 110.
11371615	7	8	theme	transferase	1254:1264	arg1	overexpression					1227:1240	overexpression	1227:1240	overexpression of O-GlcNAc transferase	1227:1264	Furthermore, overexpression of O-GlcNAc transferase specifically inhibits transcriptional activation by native Sp1 in cells.
11371615	8	9	theme	factors	1419:1425	arg1	O-GlcNAcylation					1386:1400	O-GlcNAcylation	1386:1400	O-GlcNAcylation of transcription factors	1386:1425	Thus, our studies provide direct evidence that O-GlcNAcylation of transcription factors is involved in transcriptional regulation.
11371615	6	10	theme	activation	1075:1084	arg1	domain					1086:1091	Sp1 activation domain	1071:1091	Sp1 activation domain	1071:1091	Here, we show that O-GlcNAcylation of a chimeric transcriptional activator containing the second activation domain of Sp1 decreases its transcriptional activity both in an in vitro transcription system and in living cells, which is in concert with our observation that O-GlcNAcylation of Sp1 activation domain blocks its in vitro and in vivo interactions with other Sp1 molecules and TATA-binding protein-associated factor II 110.
11371615	7	11	theme	native	1318:1323	arg1	Sp1					1325:1327	native Sp1	1318:1327	native Sp1	1318:1327	Furthermore, overexpression of O-GlcNAc transferase specifically inhibits transcriptional activation by native Sp1 in cells.
11371615	1	12	theme	eukaryotic	137:146	arg1	proteins					162:169	eukaryotic intracellular proteins	137:169	eukaryotic intracellular proteins	137:169	The posttranslational modification of eukaryotic intracellular proteins by O-linked N-acetylglucosamine (O-GlcNAc) monosaccharides is essential for cell viability, yet its precise functional roles are largely unknown.
11371615	5	13	theme	transcription	684:696	arg1	O-GlcNAcylation					705:719	transcription factor O-GlcNAcylation	684:719	transcription factor O-GlcNAcylation	684:719	A linkage between transcription factor O-GlcNAcylation and transcriptional regulation therefore has been postulated.
11371615	6	14	theme	Sp1	901:903	arg1	domain					891:896	the second activation domain	869:896	the second activation domain of Sp1	869:903	Here, we show that O-GlcNAcylation of a chimeric transcriptional activator containing the second activation domain of Sp1 decreases its transcriptional activity both in an in vitro transcription system and in living cells, which is in concert with our observation that O-GlcNAcylation of Sp1 activation domain blocks its in vitro and in vivo interactions with other Sp1 molecules and TATA-binding protein-associated factor II 110.
11371615	6	14	theme	Sp1	901:903	arg1	Sp1					901:903	Sp1	901:903	Sp1	901:903	Here, we show that O-GlcNAcylation of a chimeric transcriptional activator containing the second activation domain of Sp1 decreases its transcriptional activity both in an in vitro transcription system and in living cells, which is in concert with our observation that O-GlcNAcylation of Sp1 activation domain blocks its in vitro and in vivo interactions with other Sp1 molecules and TATA-binding protein-associated factor II 110.
11371615	2	15	theme	O-GlcNAc	317:324	arg1	transferase					326:336	O-GlcNAc transferase	317:336	O-GlcNAc transferase	317:336	O-GlcNAc transferase utilizes UDP-GlcNAc, the end product of hexosamine biosynthesis, to catalyze this modification.
11371615	6	16	theme	TATA-binding	1167:1178	arg1	factor					1199:1204	TATA-binding protein-associated factor II	1167:1207	TATA-binding protein-associated factor II 110	1167:1211	Here, we show that O-GlcNAcylation of a chimeric transcriptional activator containing the second activation domain of Sp1 decreases its transcriptional activity both in an in vitro transcription system and in living cells, which is in concert with our observation that O-GlcNAcylation of Sp1 activation domain blocks its in vitro and in vivo interactions with other Sp1 molecules and TATA-binding protein-associated factor II 110.
11371615	7	17	theme	O-GlcNAc	1245:1252	arg1	transferase					1254:1264	O-GlcNAc transferase	1245:1264	O-GlcNAc transferase	1245:1264	Furthermore, overexpression of O-GlcNAc transferase specifically inhibits transcriptional activation by native Sp1 in cells.
11371615	6	18	dep	in	1117:1118	arg1	vivo					1120:1123	vivo	1120:1123	vivo	1120:1123	Here, we show that O-GlcNAcylation of a chimeric transcriptional activator containing the second activation domain of Sp1 decreases its transcriptional activity both in an in vitro transcription system and in living cells, which is in concert with our observation that O-GlcNAcylation of Sp1 activation domain blocks its in vitro and in vivo interactions with other Sp1 molecules and TATA-binding protein-associated factor II 110.
11371615	5	19	theme	factor	698:703	arg1	O-GlcNAcylation					705:719	transcription factor O-GlcNAcylation	684:719	transcription factor O-GlcNAcylation	684:719	A linkage between transcription factor O-GlcNAcylation and transcriptional regulation therefore has been postulated.
11371615	3	20	theme	intracellular	505:517	arg1	proteins					519:526	intracellular proteins	505:526	intracellular proteins	505:526	The availability of UDP-GlcNAc correlates with glycosylation levels of intracellular proteins as well as with transcriptional levels of some genes.
11371615	2	21	theme	end	363:365	arg1	product					367:373	the end product	359:373	the end product of hexosamine biosynthesis	359:400	O-GlcNAc transferase utilizes UDP-GlcNAc, the end product of hexosamine biosynthesis, to catalyze this modification.
11371615	2	21	theme	end	363:365	arg1	UDP-GlcNAc					347:356	UDP-GlcNAc	347:356	UDP-GlcNAc	347:356	O-GlcNAc transferase utilizes UDP-GlcNAc, the end product of hexosamine biosynthesis, to catalyze this modification.
11371615	6	22	theme	living	992:997	arg1	cells					999:1003	living cells	992:1003	living cells	992:1003	Here, we show that O-GlcNAcylation of a chimeric transcriptional activator containing the second activation domain of Sp1 decreases its transcriptional activity both in an in vitro transcription system and in living cells, which is in concert with our observation that O-GlcNAcylation of Sp1 activation domain blocks its in vitro and in vivo interactions with other Sp1 molecules and TATA-binding protein-associated factor II 110.
11371615	3	23	theme	glycosylation	481:493	arg1	levels					495:500	glycosylation levels	481:500	glycosylation levels of intracellular proteins	481:526	The availability of UDP-GlcNAc correlates with glycosylation levels of intracellular proteins as well as with transcriptional levels of some genes.
11371615	6	24	with	concert	1018:1024	arg1	observation					1035:1045	our observation	1031:1045	our observation that O-GlcNAcylation of Sp1 activation domain blocks its in vitro and in vivo interactions with other Sp1 molecules and TATA-binding protein-associated factor II 110	1031:1211	Here, we show that O-GlcNAcylation of a chimeric transcriptional activator containing the second activation domain of Sp1 decreases its transcriptional activity both in an in vitro transcription system and in living cells, which is in concert with our observation that O-GlcNAcylation of Sp1 activation domain blocks its in vitro and in vivo interactions with other Sp1 molecules and TATA-binding protein-associated factor II 110.
11371615	6	25	theme	Sp1	1071:1073	arg1	domain					1086:1091	Sp1 activation domain	1071:1091	Sp1 activation domain	1071:1091	Here, we show that O-GlcNAcylation of a chimeric transcriptional activator containing the second activation domain of Sp1 decreases its transcriptional activity both in an in vitro transcription system and in living cells, which is in concert with our observation that O-GlcNAcylation of Sp1 activation domain blocks its in vitro and in vivo interactions with other Sp1 molecules and TATA-binding protein-associated factor II 110.
11371615	6	26	theme	activation	880:889	arg1	domain					891:896	the second activation domain	869:896	the second activation domain of Sp1	869:903	Here, we show that O-GlcNAcylation of a chimeric transcriptional activator containing the second activation domain of Sp1 decreases its transcriptional activity both in an in vitro transcription system and in living cells, which is in concert with our observation that O-GlcNAcylation of Sp1 activation domain blocks its in vitro and in vivo interactions with other Sp1 molecules and TATA-binding protein-associated factor II 110.
11371615	6	26	theme	activation	880:889	arg1	Sp1					901:903	Sp1	901:903	Sp1	901:903	Here, we show that O-GlcNAcylation of a chimeric transcriptional activator containing the second activation domain of Sp1 decreases its transcriptional activity both in an in vitro transcription system and in living cells, which is in concert with our observation that O-GlcNAcylation of Sp1 activation domain blocks its in vitro and in vivo interactions with other Sp1 molecules and TATA-binding protein-associated factor II 110.
11371615	1	27	theme	posttranslational	103:119	arg1	essential					233:241	essential	233:241	essential	233:241	The posttranslational modification of eukaryotic intracellular proteins by O-linked N-acetylglucosamine (O-GlcNAc) monosaccharides is essential for cell viability, yet its precise functional roles are largely unknown.
11371615	1	27	theme	posttranslational	103:119	arg1	modification					121:132	The posttranslational modification	99:132	The posttranslational modification of eukaryotic intracellular proteins by O-linked N-acetylglucosamine (O-GlcNAc) monosaccharides	99:228	The posttranslational modification of eukaryotic intracellular proteins by O-linked N-acetylglucosamine (O-GlcNAc) monosaccharides is essential for cell viability, yet its precise functional roles are largely unknown.
11371615	6	28	theme	Sp1	1149:1151	arg1	molecules					1153:1161	other Sp1 molecules	1143:1161	other Sp1 molecules	1143:1161	Here, we show that O-GlcNAcylation of a chimeric transcriptional activator containing the second activation domain of Sp1 decreases its transcriptional activity both in an in vitro transcription system and in living cells, which is in concert with our observation that O-GlcNAcylation of Sp1 activation domain blocks its in vitro and in vivo interactions with other Sp1 molecules and TATA-binding protein-associated factor II 110.
11371615	6	29	contain	containing	858:867	arg1	activator					848:856	a chimeric transcriptional activator	821:856	a chimeric transcriptional activator containing the second activation domain of Sp1	821:903	Here, we show that O-GlcNAcylation of a chimeric transcriptional activator containing the second activation domain of Sp1 decreases its transcriptional activity both in an in vitro transcription system and in living cells, which is in concert with our observation that O-GlcNAcylation of Sp1 activation domain blocks its in vitro and in vivo interactions with other Sp1 molecules and TATA-binding protein-associated factor II 110.
11371615	6	29	contain	containing	858:867	arg2	Sp1					901:903	Sp1	901:903	Sp1	901:903	Here, we show that O-GlcNAcylation of a chimeric transcriptional activator containing the second activation domain of Sp1 decreases its transcriptional activity both in an in vitro transcription system and in living cells, which is in concert with our observation that O-GlcNAcylation of Sp1 activation domain blocks its in vitro and in vivo interactions with other Sp1 molecules and TATA-binding protein-associated factor II 110.
11371615	6	29	contain	containing	858:867	arg2	domain					891:896	the second activation domain	869:896	the second activation domain of Sp1	869:903	Here, we show that O-GlcNAcylation of a chimeric transcriptional activator containing the second activation domain of Sp1 decreases its transcriptional activity both in an in vitro transcription system and in living cells, which is in concert with our observation that O-GlcNAcylation of Sp1 activation domain blocks its in vitro and in vivo interactions with other Sp1 molecules and TATA-binding protein-associated factor II 110.
11371615	4	30	theme	RNA	619:621	arg1	polymerase					623:632	RNA polymerase II	619:635	RNA polymerase II	619:635	Meanwhile, transcription factors and RNA polymerase II can be modified by O-GlcNAc.
11371615	6	31	theme	second	873:878	arg1	domain					891:896	the second activation domain	869:896	the second activation domain of Sp1	869:903	Here, we show that O-GlcNAcylation of a chimeric transcriptional activator containing the second activation domain of Sp1 decreases its transcriptional activity both in an in vitro transcription system and in living cells, which is in concert with our observation that O-GlcNAcylation of Sp1 activation domain blocks its in vitro and in vivo interactions with other Sp1 molecules and TATA-binding protein-associated factor II 110.
11371615	6	31	theme	second	873:878	arg1	Sp1					901:903	Sp1	901:903	Sp1	901:903	Here, we show that O-GlcNAcylation of a chimeric transcriptional activator containing the second activation domain of Sp1 decreases its transcriptional activity both in an in vitro transcription system and in living cells, which is in concert with our observation that O-GlcNAcylation of Sp1 activation domain blocks its in vitro and in vivo interactions with other Sp1 molecules and TATA-binding protein-associated factor II 110.
11371615	6	32	theme	other	1143:1147	arg1	molecules					1153:1161	other Sp1 molecules	1143:1161	other Sp1 molecules	1143:1161	Here, we show that O-GlcNAcylation of a chimeric transcriptional activator containing the second activation domain of Sp1 decreases its transcriptional activity both in an in vitro transcription system and in living cells, which is in concert with our observation that O-GlcNAcylation of Sp1 activation domain blocks its in vitro and in vivo interactions with other Sp1 molecules and TATA-binding protein-associated factor II 110.
11371615	0	33	theme	N-acetylglucosamine	13:31	arg1	O-linkage					0:8	O-linkage	0:8	O-linkage of N-acetylglucosamine to Sp1 activation domain	0:56	O-linkage of N-acetylglucosamine to Sp1 activation domain inhibits its transcriptional capability.
11371615	6	34	theme	protein-associated	1180:1197	arg1	factor					1199:1204	TATA-binding protein-associated factor II	1167:1207	TATA-binding protein-associated factor II 110	1167:1211	Here, we show that O-GlcNAcylation of a chimeric transcriptional activator containing the second activation domain of Sp1 decreases its transcriptional activity both in an in vitro transcription system and in living cells, which is in concert with our observation that O-GlcNAcylation of Sp1 activation domain blocks its in vitro and in vivo interactions with other Sp1 molecules and TATA-binding protein-associated factor II 110.
11371615	1	35	theme	cell	247:250	arg1	viability					252:260	cell viability	247:260	cell viability	247:260	The posttranslational modification of eukaryotic intracellular proteins by O-linked N-acetylglucosamine (O-GlcNAc) monosaccharides is essential for cell viability, yet its precise functional roles are largely unknown.
11371615	0	36	theme	activation	40:49	arg1	domain					51:56	Sp1 activation domain	36:56	Sp1 activation domain	36:56	O-linkage of N-acetylglucosamine to Sp1 activation domain inhibits its transcriptional capability.
11371615	2	37	theme	hexosamine	378:387	arg1	biosynthesis					389:400	hexosamine biosynthesis	378:400	hexosamine biosynthesis	378:400	O-GlcNAc transferase utilizes UDP-GlcNAc, the end product of hexosamine biosynthesis, to catalyze this modification.
11371615	1	38	link	O-linked	174:181	arg1	N-acetylglucosamine					183:201	O-linked N-acetylglucosamine	174:201	O-linked N-acetylglucosamine (O-GlcNAc) monosaccharides	174:228	The posttranslational modification of eukaryotic intracellular proteins by O-linked N-acetylglucosamine (O-GlcNAc) monosaccharides is essential for cell viability, yet its precise functional roles are largely unknown.
11371615	1	38	link	O-linked	174:181	arg1	O-GlcNAc					204:211	O-GlcNAc	204:211	O-GlcNAc	204:211	The posttranslational modification of eukaryotic intracellular proteins by O-linked N-acetylglucosamine (O-GlcNAc) monosaccharides is essential for cell viability, yet its precise functional roles are largely unknown.
11371615	6	39	theme	transcription	964:976	arg1	system					978:983	an in vitro transcription system	952:983	an in vitro transcription system	952:983	Here, we show that O-GlcNAcylation of a chimeric transcriptional activator containing the second activation domain of Sp1 decreases its transcriptional activity both in an in vitro transcription system and in living cells, which is in concert with our observation that O-GlcNAcylation of Sp1 activation domain blocks its in vitro and in vivo interactions with other Sp1 molecules and TATA-binding protein-associated factor II 110.
11371615	8	40	theme	direct	1365:1370	arg1	evidence					1372:1379	direct evidence that O-GlcNAcylation of transcription factors is involved in transcriptional regulation	1365:1467	direct evidence that O-GlcNAcylation of transcription factors is involved in transcriptional regulation	1365:1467	Thus, our studies provide direct evidence that O-GlcNAcylation of transcription factors is involved in transcriptional regulation.
11371615	3	41	theme	proteins	519:526	arg1	levels					495:500	glycosylation levels	481:500	glycosylation levels of intracellular proteins	481:526	The availability of UDP-GlcNAc correlates with glycosylation levels of intracellular proteins as well as with transcriptional levels of some genes.
11371615	0	42	theme	Sp1	36:38	arg1	domain					51:56	Sp1 activation domain	36:56	Sp1 activation domain	36:56	O-linkage of N-acetylglucosamine to Sp1 activation domain inhibits its transcriptional capability.
11371615	4	43	theme	transcription	593:605	arg1	factors					607:613	transcription factors	593:613	transcription factors	593:613	Meanwhile, transcription factors and RNA polymerase II can be modified by O-GlcNAc.
11371615	6	44	from	activity	935:942	arg1	cells					999:1003	living cells	992:1003	living cells	992:1003	Here, we show that O-GlcNAcylation of a chimeric transcriptional activator containing the second activation domain of Sp1 decreases its transcriptional activity both in an in vitro transcription system and in living cells, which is in concert with our observation that O-GlcNAcylation of Sp1 activation domain blocks its in vitro and in vivo interactions with other Sp1 molecules and TATA-binding protein-associated factor II 110.
11371615	6	44	from	activity	935:942	arg1	system					978:983	an in vitro transcription system	952:983	an in vitro transcription system	952:983	Here, we show that O-GlcNAcylation of a chimeric transcriptional activator containing the second activation domain of Sp1 decreases its transcriptional activity both in an in vitro transcription system and in living cells, which is in concert with our observation that O-GlcNAcylation of Sp1 activation domain blocks its in vitro and in vivo interactions with other Sp1 molecules and TATA-binding protein-associated factor II 110.
11371615	6	45	dep	observation	1035:1045	arg1	blocks					1093:1098	blocks	1093:1098	blocks its in vitro and in vivo interactions with other Sp1 molecules and TATA-binding protein-associated factor II 110	1093:1211	Here, we show that O-GlcNAcylation of a chimeric transcriptional activator containing the second activation domain of Sp1 decreases its transcriptional activity both in an in vitro transcription system and in living cells, which is in concert with our observation that O-GlcNAcylation of Sp1 activation domain blocks its in vitro and in vivo interactions with other Sp1 molecules and TATA-binding protein-associated factor II 110.
11371615	6	46	dep	in	955:956	arg1	vitro					958:962	vitro	958:962	vitro	958:962	Here, we show that O-GlcNAcylation of a chimeric transcriptional activator containing the second activation domain of Sp1 decreases its transcriptional activity both in an in vitro transcription system and in living cells, which is in concert with our observation that O-GlcNAcylation of Sp1 activation domain blocks its in vitro and in vivo interactions with other Sp1 molecules and TATA-binding protein-associated factor II 110.
11371615	6	47	theme	in	955:956	arg1	system					978:983	an in vitro transcription system	952:983	an in vitro transcription system	952:983	Here, we show that O-GlcNAcylation of a chimeric transcriptional activator containing the second activation domain of Sp1 decreases its transcriptional activity both in an in vitro transcription system and in living cells, which is in concert with our observation that O-GlcNAcylation of Sp1 activation domain blocks its in vitro and in vivo interactions with other Sp1 molecules and TATA-binding protein-associated factor II 110.
11371615	7	48	from	activation	1304:1313	arg1	cells					1332:1336	cells	1332:1336	cells	1332:1336	Furthermore, overexpression of O-GlcNAc transferase specifically inhibits transcriptional activation by native Sp1 in cells.
11371615	2	49	theme	biosynthesis	389:400	arg1	product					367:373	the end product	359:373	the end product of hexosamine biosynthesis	359:400	O-GlcNAc transferase utilizes UDP-GlcNAc, the end product of hexosamine biosynthesis, to catalyze this modification.
11371615	2	49	theme	biosynthesis	389:400	arg1	UDP-GlcNAc					347:356	UDP-GlcNAc	347:356	UDP-GlcNAc	347:356	O-GlcNAc transferase utilizes UDP-GlcNAc, the end product of hexosamine biosynthesis, to catalyze this modification.
11371615	3	50	theme	UDP-GlcNAc	454:463	arg1	availability					438:449	The availability	434:449	The availability of UDP-GlcNAc	434:463	The availability of UDP-GlcNAc correlates with glycosylation levels of intracellular proteins as well as with transcriptional levels of some genes.
11371615	6	51	with	interactions	1125:1136	arg1	molecules					1153:1161	other Sp1 molecules	1143:1161	other Sp1 molecules	1143:1161	Here, we show that O-GlcNAcylation of a chimeric transcriptional activator containing the second activation domain of Sp1 decreases its transcriptional activity both in an in vitro transcription system and in living cells, which is in concert with our observation that O-GlcNAcylation of Sp1 activation domain blocks its in vitro and in vivo interactions with other Sp1 molecules and TATA-binding protein-associated factor II 110.
11371615	6	51	with	interactions	1125:1136	arg1	factor					1199:1204	TATA-binding protein-associated factor II	1167:1207	TATA-binding protein-associated factor II 110	1167:1211	Here, we show that O-GlcNAcylation of a chimeric transcriptional activator containing the second activation domain of Sp1 decreases its transcriptional activity both in an in vitro transcription system and in living cells, which is in concert with our observation that O-GlcNAcylation of Sp1 activation domain blocks its in vitro and in vivo interactions with other Sp1 molecules and TATA-binding protein-associated factor II 110.
11371615	6	52	theme	activator	848:856	arg1	O-GlcNAcylation					802:816	O-GlcNAcylation	802:816	O-GlcNAcylation of a chimeric transcriptional activator containing the second activation domain of Sp1	802:903	Here, we show that O-GlcNAcylation of a chimeric transcriptional activator containing the second activation domain of Sp1 decreases its transcriptional activity both in an in vitro transcription system and in living cells, which is in concert with our observation that O-GlcNAcylation of Sp1 activation domain blocks its in vitro and in vivo interactions with other Sp1 molecules and TATA-binding protein-associated factor II 110.
11371615	1	53	theme	intracellular	148:160	arg1	proteins					162:169	eukaryotic intracellular proteins	137:169	eukaryotic intracellular proteins	137:169	The posttranslational modification of eukaryotic intracellular proteins by O-linked N-acetylglucosamine (O-GlcNAc) monosaccharides is essential for cell viability, yet its precise functional roles are largely unknown.
11371615	8	54	theme	transcription	1405:1417	arg1	factors					1419:1425	transcription factors	1405:1425	transcription factors	1405:1425	Thus, our studies provide direct evidence that O-GlcNAcylation of transcription factors is involved in transcriptional regulation.
11371615	8	55	gly	O-GlcNAcylation	1386:1400	arg1	regulation					1458:1467	transcriptional regulation	1442:1467	transcriptional regulation	1442:1467	Thus, our studies provide direct evidence that O-GlcNAcylation of transcription factors is involved in transcriptional regulation.
11371615	6	56	theme	transcriptional	832:846	arg1	activator					848:856	a chimeric transcriptional activator	821:856	a chimeric transcriptional activator containing the second activation domain of Sp1	821:903	Here, we show that O-GlcNAcylation of a chimeric transcriptional activator containing the second activation domain of Sp1 decreases its transcriptional activity both in an in vitro transcription system and in living cells, which is in concert with our observation that O-GlcNAcylation of Sp1 activation domain blocks its in vitro and in vivo interactions with other Sp1 molecules and TATA-binding protein-associated factor II 110.
11371615	1	57	theme	proteins	162:169	arg1	essential					233:241	essential	233:241	essential	233:241	The posttranslational modification of eukaryotic intracellular proteins by O-linked N-acetylglucosamine (O-GlcNAc) monosaccharides is essential for cell viability, yet its precise functional roles are largely unknown.
11371615	1	57	theme	proteins	162:169	arg1	modification					121:132	The posttranslational modification	99:132	The posttranslational modification of eukaryotic intracellular proteins by O-linked N-acetylglucosamine (O-GlcNAc) monosaccharides	99:228	The posttranslational modification of eukaryotic intracellular proteins by O-linked N-acetylglucosamine (O-GlcNAc) monosaccharides is essential for cell viability, yet its precise functional roles are largely unknown.
11371615	6	58	theme	in	1117:1118	arg1	interactions					1125:1136	its in vitro and in vivo interactions	1100:1136	its in vitro and in vivo interactions with other Sp1 molecules and TATA-binding protein-associated factor II 110	1100:1211	Here, we show that O-GlcNAcylation of a chimeric transcriptional activator containing the second activation domain of Sp1 decreases its transcriptional activity both in an in vitro transcription system and in living cells, which is in concert with our observation that O-GlcNAcylation of Sp1 activation domain blocks its in vitro and in vivo interactions with other Sp1 molecules and TATA-binding protein-associated factor II 110.
11371615	6	59	theme	chimeric	823:830	arg1	activator					848:856	a chimeric transcriptional activator	821:856	a chimeric transcriptional activator containing the second activation domain of Sp1	821:903	Here, we show that O-GlcNAcylation of a chimeric transcriptional activator containing the second activation domain of Sp1 decreases its transcriptional activity both in an in vitro transcription system and in living cells, which is in concert with our observation that O-GlcNAcylation of Sp1 activation domain blocks its in vitro and in vivo interactions with other Sp1 molecules and TATA-binding protein-associated factor II 110.
11371615	3	60	theme	transcriptional	544:558	arg1	levels					560:565	transcriptional levels	544:565	transcriptional levels of some genes	544:579	The availability of UDP-GlcNAc correlates with glycosylation levels of intracellular proteins as well as with transcriptional levels of some genes.
11371615	0	61	theme	transcriptional	71:85	arg1	capability					87:96	its transcriptional capability	67:96	its transcriptional capability	67:96	O-linkage of N-acetylglucosamine to Sp1 activation domain inhibits its transcriptional capability.
11371615	1	62	theme	O-linked	174:181	arg1	N-acetylglucosamine					183:201	O-linked N-acetylglucosamine	174:201	O-linked N-acetylglucosamine (O-GlcNAc) monosaccharides	174:228	The posttranslational modification of eukaryotic intracellular proteins by O-linked N-acetylglucosamine (O-GlcNAc) monosaccharides is essential for cell viability, yet its precise functional roles are largely unknown.
11371615	1	62	theme	O-linked	174:181	arg1	O-GlcNAc					204:211	O-GlcNAc	204:211	O-GlcNAc	204:211	The posttranslational modification of eukaryotic intracellular proteins by O-linked N-acetylglucosamine (O-GlcNAc) monosaccharides is essential for cell viability, yet its precise functional roles are largely unknown.
11371615	1	63	theme	precise	271:277	arg1	roles					290:294	its precise functional roles	267:294	its precise functional roles	267:294	The posttranslational modification of eukaryotic intracellular proteins by O-linked N-acetylglucosamine (O-GlcNAc) monosaccharides is essential for cell viability, yet its precise functional roles are largely unknown.
11371615	6	64	theme	in	1104:1105	arg1	interactions					1125:1136	its in vitro and in vivo interactions	1100:1136	its in vitro and in vivo interactions with other Sp1 molecules and TATA-binding protein-associated factor II 110	1100:1211	Here, we show that O-GlcNAcylation of a chimeric transcriptional activator containing the second activation domain of Sp1 decreases its transcriptional activity both in an in vitro transcription system and in living cells, which is in concert with our observation that O-GlcNAcylation of Sp1 activation domain blocks its in vitro and in vivo interactions with other Sp1 molecules and TATA-binding protein-associated factor II 110.
11371615	1	65	theme	N-acetylglucosamine	183:201	arg1	monosaccharides					214:228	O-linked N-acetylglucosamine (O-GlcNAc) monosaccharides	174:228	O-linked N-acetylglucosamine (O-GlcNAc) monosaccharides	174:228	The posttranslational modification of eukaryotic intracellular proteins by O-linked N-acetylglucosamine (O-GlcNAc) monosaccharides is essential for cell viability, yet its precise functional roles are largely unknown.
11371615	1	66	theme	functional	279:288	arg1	roles					290:294	its precise functional roles	267:294	its precise functional roles	267:294	The posttranslational modification of eukaryotic intracellular proteins by O-linked N-acetylglucosamine (O-GlcNAc) monosaccharides is essential for cell viability, yet its precise functional roles are largely unknown.
1898343	1	0	contain	containing	106:115	arg1	elastase					72:79	Human pancreatic elastase 1	55:81	Human pancreatic elastase 1 (E1)	55:86	Human pancreatic elastase 1 (E1) is a glycoprotein containing two potential N-glycosylation sites, one of which carries a carbohydrate moiety [Wendorf, Geyer, Sziegoleit & Linder (1989) FEBS Lett.
1898343	1	0	contain	containing	106:115	arg2	sites					147:151	two potential N-glycosylation sites	117:151	two potential N-glycosylation sites	117:151	Human pancreatic elastase 1 (E1) is a glycoprotein containing two potential N-glycosylation sites, one of which carries a carbohydrate moiety [Wendorf, Geyer, Sziegoleit & Linder (1989) FEBS Lett.
1898343	1	0	contain	containing	106:115	arg1	glycoprotein					93:104	a glycoprotein	91:104	a glycoprotein containing two potential N-glycosylation sites, one of which carries a carbohydrate moiety [Wendorf, Geyer, Sziegoleit & Linder (1989) FEBS Lett	91:249	Human pancreatic elastase 1 (E1) is a glycoprotein containing two potential N-glycosylation sites, one of which carries a carbohydrate moiety [Wendorf, Geyer, Sziegoleit & Linder (1989) FEBS Lett.
1898343	5	1	theme	Major	624:628	arg1	fractions					654:662	Major oligosaccharide alditol fractions	624:662	Major oligosaccharide alditol fractions	624:662	Major oligosaccharide alditol fractions, representing 67.8 mol% of total glycans, were characterized by methylation analysis and sequential degradation with exoglycosidases.
1898343	1	2	theme	sites	147:151	arg1	one					154:156	one	154:156	one	154:156	Human pancreatic elastase 1 (E1) is a glycoprotein containing two potential N-glycosylation sites, one of which carries a carbohydrate moiety [Wendorf, Geyer, Sziegoleit & Linder (1989) FEBS Lett.
1898343	1	2	theme	sites	147:151	arg1	sites					147:151	two potential N-glycosylation sites	117:151	two potential N-glycosylation sites	117:151	Human pancreatic elastase 1 (E1) is a glycoprotein containing two potential N-glycosylation sites, one of which carries a carbohydrate moiety [Wendorf, Geyer, Sziegoleit & Linder (1989) FEBS Lett.
1898343	6	3	theme	A	966:966	arg1	determinants					983:994	blood group A, B, Lea (or X), difucosyl A or difucosyl B determinants	926:994	blood group A, B, Lea (or X), difucosyl A or difucosyl B determinants	926:994	The results revealed that about two-fifths of the partially truncated, mainly biantennary, complex-type glycans found comprised blood group A, B, Lea (or X), difucosyl A or difucosyl B determinants, which could be assigned to lactosamine antennae linked to Man(alpha 1-3)- residues of the sugar chains.
1898343	5	4	theme	sequential	753:762	arg1	degradation					764:774	sequential degradation	753:774	sequential degradation	753:774	Major oligosaccharide alditol fractions, representing 67.8 mol% of total glycans, were characterized by methylation analysis and sequential degradation with exoglycosidases.
1898343	4	5	theme	peptide-N4-	478:488	arg1	F					537:537	peptide-N4-(N-acetyl-beta-glycosaminyl)-asparagine amidase F	478:537	peptide-N4-(N-acetyl-beta-glycosaminyl)-asparagine amidase F	478:537	Oligosaccharides were liberated from resulting glycopeptides by treatment with peptide-N4-(N-acetyl-beta-glycosaminyl)-asparagine amidase F, radiolabelled by reduction with KB3H4 and separated by h.p.l.c. and gel filtration.
1898343	5	6	theme	oligosaccharide	630:644	arg1	fractions					654:662	Major oligosaccharide alditol fractions	624:662	Major oligosaccharide alditol fractions	624:662	Major oligosaccharide alditol fractions, representing 67.8 mol% of total glycans, were characterized by methylation analysis and sequential degradation with exoglycosidases.
1898343	6	7	theme	difucosyl	956:964	arg1	A					966:966	difucosyl A	956:966	difucosyl A	956:966	The results revealed that about two-fifths of the partially truncated, mainly biantennary, complex-type glycans found comprised blood group A, B, Lea (or X), difucosyl A or difucosyl B determinants, which could be assigned to lactosamine antennae linked to Man(alpha 1-3)- residues of the sugar chains.
1898343	5	8	theme	alditol	646:652	arg1	fractions					654:662	Major oligosaccharide alditol fractions	624:662	Major oligosaccharide alditol fractions	624:662	Major oligosaccharide alditol fractions, representing 67.8 mol% of total glycans, were characterized by methylation analysis and sequential degradation with exoglycosidases.
1898343	6	9	theme	chains	1093:1098	arg1	residues					1071:1078	residues	1071:1078	residues of the sugar chains	1071:1098	The results revealed that about two-fifths of the partially truncated, mainly biantennary, complex-type glycans found comprised blood group A, B, Lea (or X), difucosyl A or difucosyl B determinants, which could be assigned to lactosamine antennae linked to Man(alpha 1-3)- residues of the sugar chains.
1898343	6	9	theme	chains	1093:1098	arg1	chains					1093:1098	the sugar chains	1083:1098	the sugar chains	1083:1098	The results revealed that about two-fifths of the partially truncated, mainly biantennary, complex-type glycans found comprised blood group A, B, Lea (or X), difucosyl A or difucosyl B determinants, which could be assigned to lactosamine antennae linked to Man(alpha 1-3)- residues of the sugar chains.
1898343	1	10	theme	Human	55:59	arg1	elastase					72:79	Human pancreatic elastase 1	55:81	Human pancreatic elastase 1 (E1)	55:86	Human pancreatic elastase 1 (E1) is a glycoprotein containing two potential N-glycosylation sites, one of which carries a carbohydrate moiety [Wendorf, Geyer, Sziegoleit & Linder (1989) FEBS Lett.
1898343	1	10	theme	Human	55:59	arg1	E1					84:85	E1	84:85	E1	84:85	Human pancreatic elastase 1 (E1) is a glycoprotein containing two potential N-glycosylation sites, one of which carries a carbohydrate moiety [Wendorf, Geyer, Sziegoleit & Linder (1989) FEBS Lett.
1898343	1	10	theme	Human	55:59	arg1	glycoprotein					93:104	a glycoprotein	91:104	a glycoprotein containing two potential N-glycosylation sites, one of which carries a carbohydrate moiety [Wendorf, Geyer, Sziegoleit & Linder (1989) FEBS Lett	91:249	Human pancreatic elastase 1 (E1) is a glycoprotein containing two potential N-glycosylation sites, one of which carries a carbohydrate moiety [Wendorf, Geyer, Sziegoleit & Linder (1989) FEBS Lett.
1898343	6	11	theme	glycans	902:908	arg1	two-fifths					830:839	about two-fifths	824:839	about two-fifths of the partially truncated, mainly biantennary, complex-type glycans found	824:914	The results revealed that about two-fifths of the partially truncated, mainly biantennary, complex-type glycans found comprised blood group A, B, Lea (or X), difucosyl A or difucosyl B determinants, which could be assigned to lactosamine antennae linked to Man(alpha 1-3)- residues of the sugar chains.
1898343	1	12	theme	pancreatic	61:70	arg1	elastase					72:79	Human pancreatic elastase 1	55:81	Human pancreatic elastase 1 (E1)	55:86	Human pancreatic elastase 1 (E1) is a glycoprotein containing two potential N-glycosylation sites, one of which carries a carbohydrate moiety [Wendorf, Geyer, Sziegoleit & Linder (1989) FEBS Lett.
1898343	1	12	theme	pancreatic	61:70	arg1	E1					84:85	E1	84:85	E1	84:85	Human pancreatic elastase 1 (E1) is a glycoprotein containing two potential N-glycosylation sites, one of which carries a carbohydrate moiety [Wendorf, Geyer, Sziegoleit & Linder (1989) FEBS Lett.
1898343	1	12	theme	pancreatic	61:70	arg1	glycoprotein					93:104	a glycoprotein	91:104	a glycoprotein containing two potential N-glycosylation sites, one of which carries a carbohydrate moiety [Wendorf, Geyer, Sziegoleit & Linder (1989) FEBS Lett	91:249	Human pancreatic elastase 1 (E1) is a glycoprotein containing two potential N-glycosylation sites, one of which carries a carbohydrate moiety [Wendorf, Geyer, Sziegoleit & Linder (1989) FEBS Lett.
1898343	6	13	dep	truncated	858:866	arg1	complex-type					889:900	complex-type	889:900	complex-type	889:900	The results revealed that about two-fifths of the partially truncated, mainly biantennary, complex-type glycans found comprised blood group A, B, Lea (or X), difucosyl A or difucosyl B determinants, which could be assigned to lactosamine antennae linked to Man(alpha 1-3)- residues of the sugar chains.
1898343	6	13	dep	truncated	858:866	arg1	biantennary					876:886	biantennary	876:886	biantennary	876:886	The results revealed that about two-fifths of the partially truncated, mainly biantennary, complex-type glycans found comprised blood group A, B, Lea (or X), difucosyl A or difucosyl B determinants, which could be assigned to lactosamine antennae linked to Man(alpha 1-3)- residues of the sugar chains.
1898343	5	14	with	degradation	764:774	arg1	exoglycosidases					781:795	exoglycosidases	781:795	exoglycosidases	781:795	Major oligosaccharide alditol fractions, representing 67.8 mol% of total glycans, were characterized by methylation analysis and sequential degradation with exoglycosidases.
1898343	0	15	theme	Carbohydrate	0:11	arg1	structure					13:21	Carbohydrate structure	0:21	Carbohydrate structure of human pancreatic elastase 1.	0:53	Carbohydrate structure of human pancreatic elastase 1.
1898343	6	16	theme	lactosamine	1024:1034	arg1	antennae					1036:1043	lactosamine antennae	1024:1043	lactosamine antennae linked to Man(alpha 1-3)- residues of the sugar chains	1024:1098	The results revealed that about two-fifths of the partially truncated, mainly biantennary, complex-type glycans found comprised blood group A, B, Lea (or X), difucosyl A or difucosyl B determinants, which could be assigned to lactosamine antennae linked to Man(alpha 1-3)- residues of the sugar chains.
1898343	4	17	theme	resulting	436:444	arg1	glycopeptides					446:458	resulting glycopeptides	436:458	resulting glycopeptides	436:458	Oligosaccharides were liberated from resulting glycopeptides by treatment with peptide-N4-(N-acetyl-beta-glycosaminyl)-asparagine amidase F, radiolabelled by reduction with KB3H4 and separated by h.p.l.c. and gel filtration.
1898343	6	18	theme	sugar	1087:1091	arg1	chains					1093:1098	the sugar chains	1083:1098	the sugar chains	1083:1098	The results revealed that about two-fifths of the partially truncated, mainly biantennary, complex-type glycans found comprised blood group A, B, Lea (or X), difucosyl A or difucosyl B determinants, which could be assigned to lactosamine antennae linked to Man(alpha 1-3)- residues of the sugar chains.
1898343	3	19	theme	donors	365:370	arg1	tissue					352:357	post-mortem pancreas tissue	331:357	post-mortem pancreas tissue of 75 donors	331:370	In order to study its glycosylation, glycoprotein isolated from post-mortem pancreas tissue of 75 donors was digested with trypsin.
1898343	3	20	theme	post-mortem	331:341	arg1	tissue					352:357	post-mortem pancreas tissue	331:357	post-mortem pancreas tissue of 75 donors	331:370	In order to study its glycosylation, glycoprotein isolated from post-mortem pancreas tissue of 75 donors was digested with trypsin.
1898343	3	21	gly	glycoprotein	304:315	arg1	glycoprotein					304:315	glycoprotein	304:315	glycoprotein isolated from post-mortem pancreas tissue of 75 donors	304:370	In order to study its glycosylation, glycoprotein isolated from post-mortem pancreas tissue of 75 donors was digested with trypsin.
1898343	0	22	theme	human	26:30	arg1	elastase					43:50	human pancreatic elastase 1	26:52	human pancreatic elastase 1	26:52	Carbohydrate structure of human pancreatic elastase 1.
1898343	1	23	theme	FEBS	241:244	arg1	Lett					246:249	FEBS Lett	241:249	Geyer, Sziegoleit & Linder (1989) FEBS Lett	207:249	Human pancreatic elastase 1 (E1) is a glycoprotein containing two potential N-glycosylation sites, one of which carries a carbohydrate moiety [Wendorf, Geyer, Sziegoleit & Linder (1989) FEBS Lett.
1898343	1	24	gly	glycoprotein	93:104	arg1	elastase					72:79	Human pancreatic elastase 1	55:81	Human pancreatic elastase 1 (E1)	55:86	Human pancreatic elastase 1 (E1) is a glycoprotein containing two potential N-glycosylation sites, one of which carries a carbohydrate moiety [Wendorf, Geyer, Sziegoleit & Linder (1989) FEBS Lett.
1898343	1	24	gly	glycoprotein	93:104	arg1	glycoprotein					93:104	a glycoprotein	91:104	a glycoprotein containing two potential N-glycosylation sites, one of which carries a carbohydrate moiety [Wendorf, Geyer, Sziegoleit & Linder (1989) FEBS Lett	91:249	Human pancreatic elastase 1 (E1) is a glycoprotein containing two potential N-glycosylation sites, one of which carries a carbohydrate moiety [Wendorf, Geyer, Sziegoleit & Linder (1989) FEBS Lett.
1898343	4	25	theme	gel	608:610	arg1	filtration					612:621	gel filtration	608:621	gel filtration	608:621	Oligosaccharides were liberated from resulting glycopeptides by treatment with peptide-N4-(N-acetyl-beta-glycosaminyl)-asparagine amidase F, radiolabelled by reduction with KB3H4 and separated by h.p.l.c. and gel filtration.
1898343	4	26	theme	radiolabelled	540:552	arg1	F					537:537	peptide-N4-(N-acetyl-beta-glycosaminyl)-asparagine amidase F	478:537	peptide-N4-(N-acetyl-beta-glycosaminyl)-asparagine amidase F	478:537	Oligosaccharides were liberated from resulting glycopeptides by treatment with peptide-N4-(N-acetyl-beta-glycosaminyl)-asparagine amidase F, radiolabelled by reduction with KB3H4 and separated by h.p.l.c. and gel filtration.
1898343	1	27	contain	carries	167:173	arg2	[Wendorf					197:204	a carbohydrate moiety [Wendorf	175:204	a carbohydrate moiety [Wendorf	175:204	Human pancreatic elastase 1 (E1) is a glycoprotein containing two potential N-glycosylation sites, one of which carries a carbohydrate moiety [Wendorf, Geyer, Sziegoleit & Linder (1989) FEBS Lett.
1898343	1	27	contain	carries	167:173	arg1	one					154:156	one	154:156	one	154:156	Human pancreatic elastase 1 (E1) is a glycoprotein containing two potential N-glycosylation sites, one of which carries a carbohydrate moiety [Wendorf, Geyer, Sziegoleit & Linder (1989) FEBS Lett.
1898343	1	27	contain	carries	167:173	arg1	sites					147:151	two potential N-glycosylation sites	117:151	two potential N-glycosylation sites	117:151	Human pancreatic elastase 1 (E1) is a glycoprotein containing two potential N-glycosylation sites, one of which carries a carbohydrate moiety [Wendorf, Geyer, Sziegoleit & Linder (1989) FEBS Lett.
1898343	1	27	contain	carries	167:173	arg2	Linder					227:232	Linder	227:232	Linder	227:232	Human pancreatic elastase 1 (E1) is a glycoprotein containing two potential N-glycosylation sites, one of which carries a carbohydrate moiety [Wendorf, Geyer, Sziegoleit & Linder (1989) FEBS Lett.
1898343	6	28	theme	blood	926:930	arg1	A					938:938	blood group A	926:938	blood group A	926:938	The results revealed that about two-fifths of the partially truncated, mainly biantennary, complex-type glycans found comprised blood group A, B, Lea (or X), difucosyl A or difucosyl B determinants, which could be assigned to lactosamine antennae linked to Man(alpha 1-3)- residues of the sugar chains.
1898343	1	29	theme	carbohydrate	177:188	arg1	moiety					190:195	a carbohydrate moiety	175:195	a carbohydrate moiety [Wendorf	175:204	Human pancreatic elastase 1 (E1) is a glycoprotein containing two potential N-glycosylation sites, one of which carries a carbohydrate moiety [Wendorf, Geyer, Sziegoleit & Linder (1989) FEBS Lett.
1898343	0	30	theme	elastase	43:50	arg1	structure					13:21	Carbohydrate structure	0:21	Carbohydrate structure of human pancreatic elastase 1.	0:53	Carbohydrate structure of human pancreatic elastase 1.
1898343	6	31	theme	Lea	944:946	arg1	determinants					983:994	blood group A, B, Lea (or X), difucosyl A or difucosyl B determinants	926:994	blood group A, B, Lea (or X), difucosyl A or difucosyl B determinants	926:994	The results revealed that about two-fifths of the partially truncated, mainly biantennary, complex-type glycans found comprised blood group A, B, Lea (or X), difucosyl A or difucosyl B determinants, which could be assigned to lactosamine antennae linked to Man(alpha 1-3)- residues of the sugar chains.
1898343	5	32	theme	total	691:695	arg1	glycans					697:703	total glycans	691:703	total glycans	691:703	Major oligosaccharide alditol fractions, representing 67.8 mol% of total glycans, were characterized by methylation analysis and sequential degradation with exoglycosidases.
1898343	4	33	gly	glycopeptides	446:458	arg2	glycopeptides					446:458	resulting glycopeptides	436:458	resulting glycopeptides	436:458	Oligosaccharides were liberated from resulting glycopeptides by treatment with peptide-N4-(N-acetyl-beta-glycosaminyl)-asparagine amidase F, radiolabelled by reduction with KB3H4 and separated by h.p.l.c. and gel filtration.
1898343	1	34	theme	moiety	190:195	arg1	Linder					227:232	Linder	227:232	Linder	227:232	Human pancreatic elastase 1 (E1) is a glycoprotein containing two potential N-glycosylation sites, one of which carries a carbohydrate moiety [Wendorf, Geyer, Sziegoleit & Linder (1989) FEBS Lett.
1898343	1	34	theme	moiety	190:195	arg1	[Wendorf					197:204	a carbohydrate moiety [Wendorf	175:204	a carbohydrate moiety [Wendorf	175:204	Human pancreatic elastase 1 (E1) is a glycoprotein containing two potential N-glycosylation sites, one of which carries a carbohydrate moiety [Wendorf, Geyer, Sziegoleit & Linder (1989) FEBS Lett.
1898343	0	35	theme	pancreatic	32:41	arg1	elastase					43:50	human pancreatic elastase 1	26:52	human pancreatic elastase 1	26:52	Carbohydrate structure of human pancreatic elastase 1.
1898343	4	36	theme	N-acetyl-beta-glycosaminyl	490:515	arg1	F					537:537	peptide-N4-(N-acetyl-beta-glycosaminyl)-asparagine amidase F	478:537	peptide-N4-(N-acetyl-beta-glycosaminyl)-asparagine amidase F	478:537	Oligosaccharides were liberated from resulting glycopeptides by treatment with peptide-N4-(N-acetyl-beta-glycosaminyl)-asparagine amidase F, radiolabelled by reduction with KB3H4 and separated by h.p.l.c. and gel filtration.
1898343	5	37	theme	glycans	697:703	arg1	%					686:686	67.8 mol%	678:686	67.8 mol% of total glycans	678:703	Major oligosaccharide alditol fractions, representing 67.8 mol% of total glycans, were characterized by methylation analysis and sequential degradation with exoglycosidases.
1898343	5	37	theme	glycans	697:703	arg1	glycans					697:703	total glycans	691:703	total glycans	691:703	Major oligosaccharide alditol fractions, representing 67.8 mol% of total glycans, were characterized by methylation analysis and sequential degradation with exoglycosidases.
1898343	6	38	attach	linked	1045:1050	arg2	antennae					1036:1043	lactosamine antennae	1024:1043	lactosamine antennae linked to Man(alpha 1-3)- residues of the sugar chains	1024:1098	The results revealed that about two-fifths of the partially truncated, mainly biantennary, complex-type glycans found comprised blood group A, B, Lea (or X), difucosyl A or difucosyl B determinants, which could be assigned to lactosamine antennae linked to Man(alpha 1-3)- residues of the sugar chains.
1898343	6	38	attach	linked	1045:1050	arg1	Man					1055:1057	Man	1055:1057	Man(alpha 1-3)	1055:1068	The results revealed that about two-fifths of the partially truncated, mainly biantennary, complex-type glycans found comprised blood group A, B, Lea (or X), difucosyl A or difucosyl B determinants, which could be assigned to lactosamine antennae linked to Man(alpha 1-3)- residues of the sugar chains.
1898343	6	38	attach	linked	1045:1050	arg1	residues					1071:1078	residues	1071:1078	residues of the sugar chains	1071:1098	The results revealed that about two-fifths of the partially truncated, mainly biantennary, complex-type glycans found comprised blood group A, B, Lea (or X), difucosyl A or difucosyl B determinants, which could be assigned to lactosamine antennae linked to Man(alpha 1-3)- residues of the sugar chains.
1898343	6	38	attach	linked	1045:1050	arg1	chains					1093:1098	the sugar chains	1083:1098	the sugar chains	1083:1098	The results revealed that about two-fifths of the partially truncated, mainly biantennary, complex-type glycans found comprised blood group A, B, Lea (or X), difucosyl A or difucosyl B determinants, which could be assigned to lactosamine antennae linked to Man(alpha 1-3)- residues of the sugar chains.
1898343	6	38	attach	linked	1045:1050	arg1	alpha					1059:1063	alpha 1-3	1059:1067	alpha 1-3	1059:1067	The results revealed that about two-fifths of the partially truncated, mainly biantennary, complex-type glycans found comprised blood group A, B, Lea (or X), difucosyl A or difucosyl B determinants, which could be assigned to lactosamine antennae linked to Man(alpha 1-3)- residues of the sugar chains.
1898343	3	39	theme	pancreas	343:350	arg1	tissue					352:357	post-mortem pancreas tissue	331:357	post-mortem pancreas tissue of 75 donors	331:370	In order to study its glycosylation, glycoprotein isolated from post-mortem pancreas tissue of 75 donors was digested with trypsin.
1898343	6	40	theme	B	941:941	arg1	determinants					983:994	blood group A, B, Lea (or X), difucosyl A or difucosyl B determinants	926:994	blood group A, B, Lea (or X), difucosyl A or difucosyl B determinants	926:994	The results revealed that about two-fifths of the partially truncated, mainly biantennary, complex-type glycans found comprised blood group A, B, Lea (or X), difucosyl A or difucosyl B determinants, which could be assigned to lactosamine antennae linked to Man(alpha 1-3)- residues of the sugar chains.
1898343	1	41	gly	N-glycosylation	131:145	arg2	sites					147:151	two potential N-glycosylation sites	117:151	two potential N-glycosylation sites	117:151	Human pancreatic elastase 1 (E1) is a glycoprotein containing two potential N-glycosylation sites, one of which carries a carbohydrate moiety [Wendorf, Geyer, Sziegoleit & Linder (1989) FEBS Lett.
1898343	1	41	gly	N-glycosylation	131:145	arg2	two					117:119	two	117:119	two	117:119	Human pancreatic elastase 1 (E1) is a glycoprotein containing two potential N-glycosylation sites, one of which carries a carbohydrate moiety [Wendorf, Geyer, Sziegoleit & Linder (1989) FEBS Lett.
1898343	4	42	theme	amidase	529:535	arg1	F					537:537	peptide-N4-(N-acetyl-beta-glycosaminyl)-asparagine amidase F	478:537	peptide-N4-(N-acetyl-beta-glycosaminyl)-asparagine amidase F	478:537	Oligosaccharides were liberated from resulting glycopeptides by treatment with peptide-N4-(N-acetyl-beta-glycosaminyl)-asparagine amidase F, radiolabelled by reduction with KB3H4 and separated by h.p.l.c. and gel filtration.
1898343	4	43	theme	-asparagine	517:527	arg1	F					537:537	peptide-N4-(N-acetyl-beta-glycosaminyl)-asparagine amidase F	478:537	peptide-N4-(N-acetyl-beta-glycosaminyl)-asparagine amidase F	478:537	Oligosaccharides were liberated from resulting glycopeptides by treatment with peptide-N4-(N-acetyl-beta-glycosaminyl)-asparagine amidase F, radiolabelled by reduction with KB3H4 and separated by h.p.l.c. and gel filtration.
1898343	6	44	theme	truncated	858:866	arg1	glycans					902:908	the partially truncated, mainly biantennary, complex-type glycans	844:908	the partially truncated, mainly biantennary, complex-type glycans found	844:914	The results revealed that about two-fifths of the partially truncated, mainly biantennary, complex-type glycans found comprised blood group A, B, Lea (or X), difucosyl A or difucosyl B determinants, which could be assigned to lactosamine antennae linked to Man(alpha 1-3)- residues of the sugar chains.
1898343	6	45	theme	A	938:938	arg1	determinants					983:994	blood group A, B, Lea (or X), difucosyl A or difucosyl B determinants	926:994	blood group A, B, Lea (or X), difucosyl A or difucosyl B determinants	926:994	The results revealed that about two-fifths of the partially truncated, mainly biantennary, complex-type glycans found comprised blood group A, B, Lea (or X), difucosyl A or difucosyl B determinants, which could be assigned to lactosamine antennae linked to Man(alpha 1-3)- residues of the sugar chains.
1898343	6	46	theme	B	981:981	arg1	determinants					983:994	blood group A, B, Lea (or X), difucosyl A or difucosyl B determinants	926:994	blood group A, B, Lea (or X), difucosyl A or difucosyl B determinants	926:994	The results revealed that about two-fifths of the partially truncated, mainly biantennary, complex-type glycans found comprised blood group A, B, Lea (or X), difucosyl A or difucosyl B determinants, which could be assigned to lactosamine antennae linked to Man(alpha 1-3)- residues of the sugar chains.
1898343	4	47	with	treatment	463:471	arg1	F					537:537	peptide-N4-(N-acetyl-beta-glycosaminyl)-asparagine amidase F	478:537	peptide-N4-(N-acetyl-beta-glycosaminyl)-asparagine amidase F	478:537	Oligosaccharides were liberated from resulting glycopeptides by treatment with peptide-N4-(N-acetyl-beta-glycosaminyl)-asparagine amidase F, radiolabelled by reduction with KB3H4 and separated by h.p.l.c. and gel filtration.
1898343	4	48	theme	separated	582:590	arg1	F					537:537	peptide-N4-(N-acetyl-beta-glycosaminyl)-asparagine amidase F	478:537	peptide-N4-(N-acetyl-beta-glycosaminyl)-asparagine amidase F	478:537	Oligosaccharides were liberated from resulting glycopeptides by treatment with peptide-N4-(N-acetyl-beta-glycosaminyl)-asparagine amidase F, radiolabelled by reduction with KB3H4 and separated by h.p.l.c. and gel filtration.
1898343	5	49	theme	mol	683:685	arg1	%					686:686	67.8 mol%	678:686	67.8 mol% of total glycans	678:703	Major oligosaccharide alditol fractions, representing 67.8 mol% of total glycans, were characterized by methylation analysis and sequential degradation with exoglycosidases.
1898343	5	49	theme	mol	683:685	arg1	glycans					697:703	total glycans	691:703	total glycans	691:703	Major oligosaccharide alditol fractions, representing 67.8 mol% of total glycans, were characterized by methylation analysis and sequential degradation with exoglycosidases.
1898343	3	50	attach	isolated	317:324	arg2	glycoprotein					304:315	glycoprotein	304:315	glycoprotein isolated from post-mortem pancreas tissue of 75 donors	304:370	In order to study its glycosylation, glycoprotein isolated from post-mortem pancreas tissue of 75 donors was digested with trypsin.
1898343	3	50	attach	isolated	317:324	arg1	tissue					352:357	post-mortem pancreas tissue	331:357	post-mortem pancreas tissue of 75 donors	331:370	In order to study its glycosylation, glycoprotein isolated from post-mortem pancreas tissue of 75 donors was digested with trypsin.
1898343	4	51	attach	liberated	421:429	arg2	Oligosaccharides					399:414	Oligosaccharides	399:414	Oligosaccharides	399:414	Oligosaccharides were liberated from resulting glycopeptides by treatment with peptide-N4-(N-acetyl-beta-glycosaminyl)-asparagine amidase F, radiolabelled by reduction with KB3H4 and separated by h.p.l.c. and gel filtration.
1898343	4	51	attach	liberated	421:429	arg1	glycopeptides					446:458	resulting glycopeptides	436:458	resulting glycopeptides	436:458	Oligosaccharides were liberated from resulting glycopeptides by treatment with peptide-N4-(N-acetyl-beta-glycosaminyl)-asparagine amidase F, radiolabelled by reduction with KB3H4 and separated by h.p.l.c. and gel filtration.
1898343	5	52	theme	methylation	728:738	arg1	analysis					740:747	methylation analysis	728:747	methylation analysis	728:747	Major oligosaccharide alditol fractions, representing 67.8 mol% of total glycans, were characterized by methylation analysis and sequential degradation with exoglycosidases.
1898343	1	53	dep	Linder	227:232	arg1	Lett					246:249	FEBS Lett	241:249	Geyer, Sziegoleit & Linder (1989) FEBS Lett	207:249	Human pancreatic elastase 1 (E1) is a glycoprotein containing two potential N-glycosylation sites, one of which carries a carbohydrate moiety [Wendorf, Geyer, Sziegoleit & Linder (1989) FEBS Lett.
1898343	4	54	with	reduction	557:565	arg1	KB3H4					572:576	KB3H4	572:576	KB3H4	572:576	Oligosaccharides were liberated from resulting glycopeptides by treatment with peptide-N4-(N-acetyl-beta-glycosaminyl)-asparagine amidase F, radiolabelled by reduction with KB3H4 and separated by h.p.l.c. and gel filtration.
1898343	1	55	theme	potential	121:129	arg1	sites					147:151	two potential N-glycosylation sites	117:151	two potential N-glycosylation sites	117:151	Human pancreatic elastase 1 (E1) is a glycoprotein containing two potential N-glycosylation sites, one of which carries a carbohydrate moiety [Wendorf, Geyer, Sziegoleit & Linder (1989) FEBS Lett.
1898343	6	56	theme	difucosyl	971:979	arg1	B					981:981	difucosyl B	971:981	difucosyl B	971:981	The results revealed that about two-fifths of the partially truncated, mainly biantennary, complex-type glycans found comprised blood group A, B, Lea (or X), difucosyl A or difucosyl B determinants, which could be assigned to lactosamine antennae linked to Man(alpha 1-3)- residues of the sugar chains.
1898343	6	57	theme	group	932:936	arg1	A					938:938	blood group A	926:938	blood group A	926:938	The results revealed that about two-fifths of the partially truncated, mainly biantennary, complex-type glycans found comprised blood group A, B, Lea (or X), difucosyl A or difucosyl B determinants, which could be assigned to lactosamine antennae linked to Man(alpha 1-3)- residues of the sugar chains.
1898343	5	58	with	analysis	740:747	arg1	exoglycosidases					781:795	exoglycosidases	781:795	exoglycosidases	781:795	Major oligosaccharide alditol fractions, representing 67.8 mol% of total glycans, were characterized by methylation analysis and sequential degradation with exoglycosidases.
1898343	1	59	theme	N-glycosylation	131:145	arg1	sites					147:151	two potential N-glycosylation sites	117:151	two potential N-glycosylation sites	117:151	Human pancreatic elastase 1 (E1) is a glycoprotein containing two potential N-glycosylation sites, one of which carries a carbohydrate moiety [Wendorf, Geyer, Sziegoleit & Linder (1989) FEBS Lett.
2393398	5	0	theme	fucose	786:791	arg1	ratio					765:769	an equimolar ratio	752:769	an equimolar ratio of peptide and fucose in the glycopeptide	752:811	A combination of these methodologies showed an equimolar ratio of peptide and fucose in the glycopeptide.
2393398	6	1	theme	amino	951:955	arg1	composition					962:972	amino acid composition	951:972	amino acid composition	951:972	This modification is not detected without mass spectrometry because the fucose residue is hydrolyzed under standard acidic conditions of amino acid composition and N-terminal sequence analysis.
2393398	7	2	theme	protein	1135:1141	arg1	N-terminus					1087:1096	the N-terminus	1083:1096	the N-terminus (within first 23 amino acids) of the protein	1083:1141	The site of attachment of fucose to the peptide has been localized towards the N-terminus (within first 23 amino acids) of the protein.
2393398	7	3	theme	attachment	1020:1029	arg1	attachment					1020:1029	attachment	1020:1029	attachment of fucose to the peptide	1020:1054	The site of attachment of fucose to the peptide has been localized towards the N-terminus (within first 23 amino acids) of the protein.
2393398	7	3	theme	attachment	1020:1029	arg1	site					1012:1015	The site	1008:1015	The site of attachment of fucose to the peptide	1008:1054	The site of attachment of fucose to the peptide has been localized towards the N-terminus (within first 23 amino acids) of the protein.
2393398	3	4	theme	high	516:519	arg1	chromatography					540:553	semi-preparative reversed phase high performance liquid chromatography	484:553	semi-preparative reversed phase high performance liquid chromatography	484:553	The glycopeptide was isolated by semi-preparative reversed phase high performance liquid chromatography.
2393398	0	5	from	composition	13:23	arg1	pro-urokinase					87:99	pro-urokinase	87:99	pro-urokinase	87:99	Carbohydrate composition and presence of a fucose-protein linkage in recombinant human pro-urokinase.
2393398	2	6	theme	tryptic	364:370	arg1	digest					372:377	the tryptic digest	360:377	the tryptic digest of pro-urokinase expressed in a mouse hybridoma cell line Sp 2/0 Ag 14	360:448	A glycopeptide containing the monosaccharide, fucose, covalently linked directly to the peptide backbone has been isolated from the tryptic digest of pro-urokinase expressed in a mouse hybridoma cell line Sp 2/0 Ag 14.
2393398	3	7	theme	liquid	533:538	arg1	chromatography					540:553	semi-preparative reversed phase high performance liquid chromatography	484:553	semi-preparative reversed phase high performance liquid chromatography	484:553	The glycopeptide was isolated by semi-preparative reversed phase high performance liquid chromatography.
2393398	4	8	theme	carbohydrate	617:628	arg1	analysis					630:637	carbohydrate analysis	617:637	carbohydrate analysis	617:637	The identity of a fucose containing peptide was confirmed by carbohydrate analysis, amino acid analysis and plasma desorption mass spectrometry (PDMS).
2393398	5	9	theme	equimolar	755:763	arg1	ratio					765:769	an equimolar ratio	752:769	an equimolar ratio of peptide and fucose in the glycopeptide	752:811	A combination of these methodologies showed an equimolar ratio of peptide and fucose in the glycopeptide.
2393398	6	10	theme	acidic	930:935	arg1	conditions					937:946	standard acidic conditions	921:946	standard acidic conditions of amino acid composition and N-terminal sequence analysis	921:1005	This modification is not detected without mass spectrometry because the fucose residue is hydrolyzed under standard acidic conditions of amino acid composition and N-terminal sequence analysis.
2393398	8	11	theme	pro-urokinase	1194:1206	arg1	composition					1167:1177	the carbohydrate composition	1150:1177	the carbohydrate composition of recombinant pro-urokinase	1150:1206	Also, the carbohydrate composition of recombinant pro-urokinase is reported.
2393398	3	12	theme	reversed	501:508	arg1	chromatography					540:553	semi-preparative reversed phase high performance liquid chromatography	484:553	semi-preparative reversed phase high performance liquid chromatography	484:553	The glycopeptide was isolated by semi-preparative reversed phase high performance liquid chromatography.
2393398	0	13	attach	presence	29:36	arg2	linkage					58:64	a fucose-protein linkage	41:64	a fucose-protein linkage	41:64	Carbohydrate composition and presence of a fucose-protein linkage in recombinant human pro-urokinase.
2393398	0	13	attach	presence	29:36	arg1	pro-urokinase					87:99	pro-urokinase	87:99	pro-urokinase	87:99	Carbohydrate composition and presence of a fucose-protein linkage in recombinant human pro-urokinase.
2393398	1	14	theme	urinary	176:182	arg1	activator					201:209	urinary type plasminogen activator	176:209	urinary type plasminogen activator	176:209	A new post-translational modification site in the growth factor domain of urinary type plasminogen activator has been identified.
2393398	0	15	theme	fucose-protein	43:56	arg1	linkage					58:64	a fucose-protein linkage	41:64	a fucose-protein linkage	41:64	Carbohydrate composition and presence of a fucose-protein linkage in recombinant human pro-urokinase.
2393398	1	16	theme	type	184:187	arg1	activator					201:209	urinary type plasminogen activator	176:209	urinary type plasminogen activator	176:209	A new post-translational modification site in the growth factor domain of urinary type plasminogen activator has been identified.
2393398	2	17	attach	isolated	346:353	arg1	digest					372:377	the tryptic digest	360:377	the tryptic digest of pro-urokinase expressed in a mouse hybridoma cell line Sp 2/0 Ag 14	360:448	A glycopeptide containing the monosaccharide, fucose, covalently linked directly to the peptide backbone has been isolated from the tryptic digest of pro-urokinase expressed in a mouse hybridoma cell line Sp 2/0 Ag 14.
2393398	2	17	attach	isolated	346:353	arg2	glycopeptide					234:245	A glycopeptide	232:245	A glycopeptide containing the monosaccharide, fucose, covalently linked directly to the peptide backbone	232:335	A glycopeptide containing the monosaccharide, fucose, covalently linked directly to the peptide backbone has been isolated from the tryptic digest of pro-urokinase expressed in a mouse hybridoma cell line Sp 2/0 Ag 14.
2393398	6	18	theme	standard	921:928	arg1	conditions					937:946	standard acidic conditions	921:946	standard acidic conditions of amino acid composition and N-terminal sequence analysis	921:1005	This modification is not detected without mass spectrometry because the fucose residue is hydrolyzed under standard acidic conditions of amino acid composition and N-terminal sequence analysis.
2393398	1	19	theme	plasminogen	189:199	arg1	activator					201:209	urinary type plasminogen activator	176:209	urinary type plasminogen activator	176:209	A new post-translational modification site in the growth factor domain of urinary type plasminogen activator has been identified.
2393398	0	20	theme	Carbohydrate	0:11	arg1	composition					13:23	Carbohydrate composition	0:23	Carbohydrate composition	0:23	Carbohydrate composition and presence of a fucose-protein linkage in recombinant human pro-urokinase.
2393398	4	21	theme	fucose	574:579	arg1	peptide					592:598	a fucose containing peptide	572:598	a fucose containing peptide	572:598	The identity of a fucose containing peptide was confirmed by carbohydrate analysis, amino acid analysis and plasma desorption mass spectrometry (PDMS).
2393398	6	22	theme	composition	962:972	arg1	conditions					937:946	standard acidic conditions	921:946	standard acidic conditions of amino acid composition and N-terminal sequence analysis	921:1005	This modification is not detected without mass spectrometry because the fucose residue is hydrolyzed under standard acidic conditions of amino acid composition and N-terminal sequence analysis.
2393398	8	23	theme	carbohydrate	1154:1165	arg1	composition					1167:1177	the carbohydrate composition	1150:1177	the carbohydrate composition of recombinant pro-urokinase	1150:1206	Also, the carbohydrate composition of recombinant pro-urokinase is reported.
2393398	1	24	theme	activator	201:209	arg1	activator					201:209	urinary type plasminogen activator	176:209	urinary type plasminogen activator	176:209	A new post-translational modification site in the growth factor domain of urinary type plasminogen activator has been identified.
2393398	1	24	theme	activator	201:209	arg1	domain					166:171	the growth factor domain	148:171	the growth factor domain of urinary type plasminogen activator	148:209	A new post-translational modification site in the growth factor domain of urinary type plasminogen activator has been identified.
2393398	7	25	attach	attachment	1020:1029	arg2	fucose					1034:1039	fucose	1034:1039	fucose	1034:1039	The site of attachment of fucose to the peptide has been localized towards the N-terminus (within first 23 amino acids) of the protein.
2393398	7	25	attach	attachment	1020:1029	arg1	peptide					1048:1054	the peptide	1044:1054	the peptide	1044:1054	The site of attachment of fucose to the peptide has been localized towards the N-terminus (within first 23 amino acids) of the protein.
2393398	1	26	from	site	140:143	arg1	activator					201:209	urinary type plasminogen activator	176:209	urinary type plasminogen activator	176:209	A new post-translational modification site in the growth factor domain of urinary type plasminogen activator has been identified.
2393398	1	26	from	site	140:143	arg1	domain					166:171	the growth factor domain	148:171	the growth factor domain of urinary type plasminogen activator	148:209	A new post-translational modification site in the growth factor domain of urinary type plasminogen activator has been identified.
2393398	1	27	theme	new	104:106	arg1	site					140:143	A new post-translational modification site	102:143	A new post-translational modification site in the growth factor domain of urinary type plasminogen activator	102:209	A new post-translational modification site in the growth factor domain of urinary type plasminogen activator has been identified.
2393398	2	28	theme	Sp	437:438	arg1	Ag					444:445	Sp 2/0 Ag 14	437:448	a mouse hybridoma cell line Sp 2/0 Ag 14	409:448	A glycopeptide containing the monosaccharide, fucose, covalently linked directly to the peptide backbone has been isolated from the tryptic digest of pro-urokinase expressed in a mouse hybridoma cell line Sp 2/0 Ag 14.
2393398	2	29	theme	2/0	440:442	arg1	Ag					444:445	Sp 2/0 Ag 14	437:448	a mouse hybridoma cell line Sp 2/0 Ag 14	409:448	A glycopeptide containing the monosaccharide, fucose, covalently linked directly to the peptide backbone has been isolated from the tryptic digest of pro-urokinase expressed in a mouse hybridoma cell line Sp 2/0 Ag 14.
2393398	4	30	theme	peptide	592:598	arg1	identity					560:567	The identity	556:567	The identity of a fucose containing peptide	556:598	The identity of a fucose containing peptide was confirmed by carbohydrate analysis, amino acid analysis and plasma desorption mass spectrometry (PDMS).
2393398	7	31	theme	first	1106:1110	arg1	acids					1121:1125	first 23 amino acids	1106:1125	first 23 amino acids	1106:1125	The site of attachment of fucose to the peptide has been localized towards the N-terminus (within first 23 amino acids) of the protein.
2393398	5	32	from	ratio	765:769	arg1	glycopeptide					800:811	the glycopeptide	796:811	the glycopeptide	796:811	A combination of these methodologies showed an equimolar ratio of peptide and fucose in the glycopeptide.
2393398	1	33	theme	post-translational	108:125	arg1	site					140:143	A new post-translational modification site	102:143	A new post-translational modification site in the growth factor domain of urinary type plasminogen activator	102:209	A new post-translational modification site in the growth factor domain of urinary type plasminogen activator has been identified.
2393398	2	34	theme	pro-urokinase	382:394	arg1	digest					372:377	the tryptic digest	360:377	the tryptic digest of pro-urokinase expressed in a mouse hybridoma cell line Sp 2/0 Ag 14	360:448	A glycopeptide containing the monosaccharide, fucose, covalently linked directly to the peptide backbone has been isolated from the tryptic digest of pro-urokinase expressed in a mouse hybridoma cell line Sp 2/0 Ag 14.
2393398	4	35	theme	containing	581:590	arg1	peptide					592:598	a fucose containing peptide	572:598	a fucose containing peptide	572:598	The identity of a fucose containing peptide was confirmed by carbohydrate analysis, amino acid analysis and plasma desorption mass spectrometry (PDMS).
2393398	5	36	theme	methodologies	731:743	arg1	combination					710:720	A combination	708:720	A combination of these methodologies	708:743	A combination of these methodologies showed an equimolar ratio of peptide and fucose in the glycopeptide.
2393398	4	37	theme	desorption	671:680	arg1	spectrometry					687:698	plasma desorption mass spectrometry	664:698	plasma desorption mass spectrometry (PDMS)	664:705	The identity of a fucose containing peptide was confirmed by carbohydrate analysis, amino acid analysis and plasma desorption mass spectrometry (PDMS).
2393398	4	37	theme	desorption	671:680	arg1	PDMS					701:704	PDMS	701:704	PDMS	701:704	The identity of a fucose containing peptide was confirmed by carbohydrate analysis, amino acid analysis and plasma desorption mass spectrometry (PDMS).
2393398	6	38	theme	analysis	998:1005	arg1	conditions					937:946	standard acidic conditions	921:946	standard acidic conditions of amino acid composition and N-terminal sequence analysis	921:1005	This modification is not detected without mass spectrometry because the fucose residue is hydrolyzed under standard acidic conditions of amino acid composition and N-terminal sequence analysis.
2393398	2	39	theme	cell	427:430	arg1	line					432:435	a mouse hybridoma cell line Sp 2/0 Ag 14	409:448	a mouse hybridoma cell line Sp 2/0 Ag 14	409:448	A glycopeptide containing the monosaccharide, fucose, covalently linked directly to the peptide backbone has been isolated from the tryptic digest of pro-urokinase expressed in a mouse hybridoma cell line Sp 2/0 Ag 14.
2393398	2	40	theme	mouse	411:415	arg1	line					432:435	a mouse hybridoma cell line Sp 2/0 Ag 14	409:448	a mouse hybridoma cell line Sp 2/0 Ag 14	409:448	A glycopeptide containing the monosaccharide, fucose, covalently linked directly to the peptide backbone has been isolated from the tryptic digest of pro-urokinase expressed in a mouse hybridoma cell line Sp 2/0 Ag 14.
2393398	6	41	theme	sequence	989:996	arg1	analysis					998:1005	N-terminal sequence analysis	978:1005	N-terminal sequence analysis	978:1005	This modification is not detected without mass spectrometry because the fucose residue is hydrolyzed under standard acidic conditions of amino acid composition and N-terminal sequence analysis.
2393398	6	42	theme	fucose	886:891	arg1	residue					893:899	the fucose residue	882:899	the fucose residue	882:899	This modification is not detected without mass spectrometry because the fucose residue is hydrolyzed under standard acidic conditions of amino acid composition and N-terminal sequence analysis.
2393398	4	43	theme	acid	646:649	arg1	analysis					651:658	amino acid analysis	640:658	amino acid analysis	640:658	The identity of a fucose containing peptide was confirmed by carbohydrate analysis, amino acid analysis and plasma desorption mass spectrometry (PDMS).
2393398	2	44	theme	hybridoma	417:425	arg1	line					432:435	a mouse hybridoma cell line Sp 2/0 Ag 14	409:448	a mouse hybridoma cell line Sp 2/0 Ag 14	409:448	A glycopeptide containing the monosaccharide, fucose, covalently linked directly to the peptide backbone has been isolated from the tryptic digest of pro-urokinase expressed in a mouse hybridoma cell line Sp 2/0 Ag 14.
2393398	0	45	theme	linkage	58:64	arg1	presence					29:36	presence	29:36	presence	29:36	Carbohydrate composition and presence of a fucose-protein linkage in recombinant human pro-urokinase.
2393398	0	45	theme	linkage	58:64	arg1	composition					13:23	Carbohydrate composition	0:23	Carbohydrate composition	0:23	Carbohydrate composition and presence of a fucose-protein linkage in recombinant human pro-urokinase.
2393398	6	46	theme	N-terminal	978:987	arg1	analysis					998:1005	N-terminal sequence analysis	978:1005	N-terminal sequence analysis	978:1005	This modification is not detected without mass spectrometry because the fucose residue is hydrolyzed under standard acidic conditions of amino acid composition and N-terminal sequence analysis.
2393398	3	47	gly	glycopeptide	455:466	arg2	glycopeptide					455:466	The glycopeptide	451:466	The glycopeptide	451:466	The glycopeptide was isolated by semi-preparative reversed phase high performance liquid chromatography.
2393398	1	48	theme	modification	127:138	arg1	site					140:143	A new post-translational modification site	102:143	A new post-translational modification site in the growth factor domain of urinary type plasminogen activator	102:209	A new post-translational modification site in the growth factor domain of urinary type plasminogen activator has been identified.
2393398	2	49	gly	glycopeptide	234:245	arg2	glycopeptide					234:245	A glycopeptide	232:245	A glycopeptide containing the monosaccharide, fucose, covalently linked directly to the peptide backbone	232:335	A glycopeptide containing the monosaccharide, fucose, covalently linked directly to the peptide backbone has been isolated from the tryptic digest of pro-urokinase expressed in a mouse hybridoma cell line Sp 2/0 Ag 14.
2393398	6	50	theme	acid	957:960	arg1	composition					962:972	amino acid composition	951:972	amino acid composition	951:972	This modification is not detected without mass spectrometry because the fucose residue is hydrolyzed under standard acidic conditions of amino acid composition and N-terminal sequence analysis.
2393398	2	51	dep	line	432:435	arg1	Ag					444:445	Sp 2/0 Ag 14	437:448	a mouse hybridoma cell line Sp 2/0 Ag 14	409:448	A glycopeptide containing the monosaccharide, fucose, covalently linked directly to the peptide backbone has been isolated from the tryptic digest of pro-urokinase expressed in a mouse hybridoma cell line Sp 2/0 Ag 14.
2393398	3	52	theme	performance	521:531	arg1	chromatography					540:553	semi-preparative reversed phase high performance liquid chromatography	484:553	semi-preparative reversed phase high performance liquid chromatography	484:553	The glycopeptide was isolated by semi-preparative reversed phase high performance liquid chromatography.
2393398	3	53	theme	phase	510:514	arg1	chromatography					540:553	semi-preparative reversed phase high performance liquid chromatography	484:553	semi-preparative reversed phase high performance liquid chromatography	484:553	The glycopeptide was isolated by semi-preparative reversed phase high performance liquid chromatography.
2393398	2	54	attach	linked	297:302	arg2	fucose					278:283	the monosaccharide, fucose,	258:284	fucose	278:283	A glycopeptide containing the monosaccharide, fucose, covalently linked directly to the peptide backbone has been isolated from the tryptic digest of pro-urokinase expressed in a mouse hybridoma cell line Sp 2/0 Ag 14.
2393398	2	54	attach	linked	297:302	arg1	backbone					328:335	the peptide backbone	316:335	the peptide backbone	316:335	A glycopeptide containing the monosaccharide, fucose, covalently linked directly to the peptide backbone has been isolated from the tryptic digest of pro-urokinase expressed in a mouse hybridoma cell line Sp 2/0 Ag 14.
2393398	5	55	gly	glycopeptide	800:811	arg2	glycopeptide					800:811	the glycopeptide	796:811	the glycopeptide	796:811	A combination of these methodologies showed an equimolar ratio of peptide and fucose in the glycopeptide.
2393398	2	56	theme	peptide	320:326	arg1	backbone					328:335	the peptide backbone	316:335	the peptide backbone	316:335	A glycopeptide containing the monosaccharide, fucose, covalently linked directly to the peptide backbone has been isolated from the tryptic digest of pro-urokinase expressed in a mouse hybridoma cell line Sp 2/0 Ag 14.
2393398	6	57	theme	mass	856:859	arg1	spectrometry					861:872	mass spectrometry	856:872	mass spectrometry	856:872	This modification is not detected without mass spectrometry because the fucose residue is hydrolyzed under standard acidic conditions of amino acid composition and N-terminal sequence analysis.
2393398	3	58	theme	semi-preparative	484:499	arg1	chromatography					540:553	semi-preparative reversed phase high performance liquid chromatography	484:553	semi-preparative reversed phase high performance liquid chromatography	484:553	The glycopeptide was isolated by semi-preparative reversed phase high performance liquid chromatography.
2393398	7	59	theme	amino	1115:1119	arg1	acids					1121:1125	first 23 amino acids	1106:1125	first 23 amino acids	1106:1125	The site of attachment of fucose to the peptide has been localized towards the N-terminus (within first 23 amino acids) of the protein.
2393398	5	60	theme	peptide	774:780	arg1	ratio					765:769	an equimolar ratio	752:769	an equimolar ratio of peptide and fucose in the glycopeptide	752:811	A combination of these methodologies showed an equimolar ratio of peptide and fucose in the glycopeptide.
2393398	4	61	theme	plasma	664:669	arg1	spectrometry					687:698	plasma desorption mass spectrometry	664:698	plasma desorption mass spectrometry (PDMS)	664:705	The identity of a fucose containing peptide was confirmed by carbohydrate analysis, amino acid analysis and plasma desorption mass spectrometry (PDMS).
2393398	4	61	theme	plasma	664:669	arg1	PDMS					701:704	PDMS	701:704	PDMS	701:704	The identity of a fucose containing peptide was confirmed by carbohydrate analysis, amino acid analysis and plasma desorption mass spectrometry (PDMS).
2393398	7	62	theme	fucose	1034:1039	arg1	attachment					1020:1029	attachment	1020:1029	attachment of fucose to the peptide	1020:1054	The site of attachment of fucose to the peptide has been localized towards the N-terminus (within first 23 amino acids) of the protein.
2393398	1	63	theme	growth	152:157	arg1	activator					201:209	urinary type plasminogen activator	176:209	urinary type plasminogen activator	176:209	A new post-translational modification site in the growth factor domain of urinary type plasminogen activator has been identified.
2393398	1	63	theme	growth	152:157	arg1	domain					166:171	the growth factor domain	148:171	the growth factor domain of urinary type plasminogen activator	148:209	A new post-translational modification site in the growth factor domain of urinary type plasminogen activator has been identified.
2393398	4	64	theme	mass	682:685	arg1	spectrometry					687:698	plasma desorption mass spectrometry	664:698	plasma desorption mass spectrometry (PDMS)	664:705	The identity of a fucose containing peptide was confirmed by carbohydrate analysis, amino acid analysis and plasma desorption mass spectrometry (PDMS).
2393398	4	64	theme	mass	682:685	arg1	PDMS					701:704	PDMS	701:704	PDMS	701:704	The identity of a fucose containing peptide was confirmed by carbohydrate analysis, amino acid analysis and plasma desorption mass spectrometry (PDMS).
2393398	2	65	contain	containing	247:256	arg2	fucose					278:283	the monosaccharide, fucose,	258:284	fucose	278:283	A glycopeptide containing the monosaccharide, fucose, covalently linked directly to the peptide backbone has been isolated from the tryptic digest of pro-urokinase expressed in a mouse hybridoma cell line Sp 2/0 Ag 14.
2393398	2	65	contain	containing	247:256	arg1	glycopeptide					234:245	A glycopeptide	232:245	A glycopeptide containing the monosaccharide, fucose, covalently linked directly to the peptide backbone	232:335	A glycopeptide containing the monosaccharide, fucose, covalently linked directly to the peptide backbone has been isolated from the tryptic digest of pro-urokinase expressed in a mouse hybridoma cell line Sp 2/0 Ag 14.
2393398	0	66	from	presence	29:36	arg1	pro-urokinase					87:99	pro-urokinase	87:99	pro-urokinase	87:99	Carbohydrate composition and presence of a fucose-protein linkage in recombinant human pro-urokinase.
2393398	2	67	theme	monosaccharide	262:275	arg1	fucose					278:283	the monosaccharide, fucose,	258:284	fucose	278:283	A glycopeptide containing the monosaccharide, fucose, covalently linked directly to the peptide backbone has been isolated from the tryptic digest of pro-urokinase expressed in a mouse hybridoma cell line Sp 2/0 Ag 14.
2393398	1	68	theme	factor	159:164	arg1	activator					201:209	urinary type plasminogen activator	176:209	urinary type plasminogen activator	176:209	A new post-translational modification site in the growth factor domain of urinary type plasminogen activator has been identified.
2393398	1	68	theme	factor	159:164	arg1	domain					166:171	the growth factor domain	148:171	the growth factor domain of urinary type plasminogen activator	148:209	A new post-translational modification site in the growth factor domain of urinary type plasminogen activator has been identified.
2393398	4	69	theme	amino	640:644	arg1	analysis					651:658	amino acid analysis	640:658	amino acid analysis	640:658	The identity of a fucose containing peptide was confirmed by carbohydrate analysis, amino acid analysis and plasma desorption mass spectrometry (PDMS).
2793860	7	0	theme	conditions	1245:1254	arg1	independent					1198:1208	independent	1198:1208	independent	1198:1208	The proportions of O-glycosylated versus nonglycosylated forms of the protein secreted by each recombinant cell line were independent of productivity or of cell culture conditions.
2793860	7	1	theme	nonglycosylated	1117:1131	arg1	forms					1133:1137	O-glycosylated versus nonglycosylated forms	1095:1137	O-glycosylated versus nonglycosylated forms of the protein secreted by each recombinant cell line	1095:1191	The proportions of O-glycosylated versus nonglycosylated forms of the protein secreted by each recombinant cell line were independent of productivity or of cell culture conditions.
2793860	3	2	theme	high	550:553	arg1	amounts					555:561	high amounts	550:561	high amounts	550:561	Human interleukin-2 was constitutively expressed in several mammalian cell lines in high amounts.
2793860	2	3	from	similarity	198:207	arg1	glycoproteins					243:255	glycoproteins	243:255	glycoproteins from natural sources or produced in heterologous cell lines	243:315	The similarity or identity of O-glycosylation in glycoproteins from natural sources or produced in heterologous cell lines, a central problem for the development of many biotechnologically relevant production processes, was examined using interleukin-2 (IL-2) as a model.
2793860	2	4	theme	relevant	383:390	arg1	production					392:401	biotechnologically relevant production	364:401	many biotechnologically relevant production processes	359:411	The similarity or identity of O-glycosylation in glycoproteins from natural sources or produced in heterologous cell lines, a central problem for the development of many biotechnologically relevant production processes, was examined using interleukin-2 (IL-2) as a model.
2793860	7	5	gly	O-glycosylated	1095:1108	arg1	forms					1133:1137	O-glycosylated versus nonglycosylated forms	1095:1137	O-glycosylated versus nonglycosylated forms of the protein secreted by each recombinant cell line	1095:1191	The proportions of O-glycosylated versus nonglycosylated forms of the protein secreted by each recombinant cell line were independent of productivity or of cell culture conditions.
2793860	7	5	gly	O-glycosylated	1095:1108	arg1	protein					1146:1152	the protein	1142:1152	the protein secreted by each recombinant cell line	1142:1191	The proportions of O-glycosylated versus nonglycosylated forms of the protein secreted by each recombinant cell line were independent of productivity or of cell culture conditions.
2793860	7	6	theme	O-glycosylated	1095:1108	arg1	forms					1133:1137	O-glycosylated versus nonglycosylated forms	1095:1137	O-glycosylated versus nonglycosylated forms of the protein secreted by each recombinant cell line	1095:1191	The proportions of O-glycosylated versus nonglycosylated forms of the protein secreted by each recombinant cell line were independent of productivity or of cell culture conditions.
2793860	7	7	theme	cell	1183:1186	arg1	line					1188:1191	each recombinant cell line	1166:1191	each recombinant cell line	1166:1191	The proportions of O-glycosylated versus nonglycosylated forms of the protein secreted by each recombinant cell line were independent of productivity or of cell culture conditions.
2793860	2	8	gly	glycoproteins	243:255	arg1	glycoproteins					243:255	glycoproteins	243:255	glycoproteins from natural sources or produced in heterologous cell lines	243:315	The similarity or identity of O-glycosylation in glycoproteins from natural sources or produced in heterologous cell lines, a central problem for the development of many biotechnologically relevant production processes, was examined using interleukin-2 (IL-2) as a model.
2793860	2	9	theme	heterologous	293:304	arg1	lines					311:315	heterologous cell lines	293:315	heterologous cell lines	293:315	The similarity or identity of O-glycosylation in glycoproteins from natural sources or produced in heterologous cell lines, a central problem for the development of many biotechnologically relevant production processes, was examined using interleukin-2 (IL-2) as a model.
2793860	7	10	gly	nonglycosylated	1117:1131	arg1	forms					1133:1137	O-glycosylated versus nonglycosylated forms	1095:1137	O-glycosylated versus nonglycosylated forms of the protein secreted by each recombinant cell line	1095:1191	The proportions of O-glycosylated versus nonglycosylated forms of the protein secreted by each recombinant cell line were independent of productivity or of cell culture conditions.
2793860	7	10	gly	nonglycosylated	1117:1131	arg1	protein					1146:1152	the protein	1142:1152	the protein secreted by each recombinant cell line	1142:1191	The proportions of O-glycosylated versus nonglycosylated forms of the protein secreted by each recombinant cell line were independent of productivity or of cell culture conditions.
2793860	2	11	gly	O-glycosylation	224:238	arg1	glycoproteins					243:255	glycoproteins	243:255	glycoproteins from natural sources or produced in heterologous cell lines	243:315	The similarity or identity of O-glycosylation in glycoproteins from natural sources or produced in heterologous cell lines, a central problem for the development of many biotechnologically relevant production processes, was examined using interleukin-2 (IL-2) as a model.
2793860	5	12	theme	oligosaccharide	727:741	arg1	structure					743:751	the NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc oligosaccharide structure	672:751	the NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc oligosaccharide structure	672:751	Only the NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc oligosaccharide structure or the NeuAc alpha 2-3Gal beta 1-3GalNAc were found in all IL-2 preparations secreted from recombinant Ltk-, Chinese hamster ovary, and baby hamster kidney cell lines.
2793860	6	13	attach	linked	958:963	arg2	chains					934:939	The O-linked chains	921:939	The O-linked chains	921:939	The O-linked chains were exclusively linked to Thr in position 3 of the polypeptide chain which is the carbohydrate attachment site in natural human IL-2.
2793860	6	13	attach	linked	958:963	arg1	Thr					968:970	Thr	968:970	Thr in position 3 of the polypeptide chain which is the carbohydrate attachment site in natural human IL-2	968:1073	The O-linked chains were exclusively linked to Thr in position 3 of the polypeptide chain which is the carbohydrate attachment site in natural human IL-2.
2793860	5	14	theme	Chinese	862:868	arg1	ovary					878:882	Chinese hamster ovary	862:882	Chinese hamster ovary	862:882	Only the NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc oligosaccharide structure or the NeuAc alpha 2-3Gal beta 1-3GalNAc were found in all IL-2 preparations secreted from recombinant Ltk-, Chinese hamster ovary, and baby hamster kidney cell lines.
2793860	5	15	theme	beta	695:698	arg1	structure					743:751	the NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc oligosaccharide structure	672:751	the NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc oligosaccharide structure	672:751	Only the NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc oligosaccharide structure or the NeuAc alpha 2-3Gal beta 1-3GalNAc were found in all IL-2 preparations secreted from recombinant Ltk-, Chinese hamster ovary, and baby hamster kidney cell lines.
2793860	8	16	theme	natural	1488:1494	arg1	lymphocytes					1498:1508	natural T lymphocytes	1488:1508	natural T lymphocytes	1488:1508	Our results show that O-glycosylated human IL-2 can be produced by applying recombinant DNA technology in heterologous cell lines with the same type of post-translational modification that is observed for the protein secreted from natural T lymphocytes.
2793860	5	17	theme	alpha	710:714	arg1	structure					743:751	the NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc oligosaccharide structure	672:751	the NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc oligosaccharide structure	672:751	Only the NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc oligosaccharide structure or the NeuAc alpha 2-3Gal beta 1-3GalNAc were found in all IL-2 preparations secreted from recombinant Ltk-, Chinese hamster ovary, and baby hamster kidney cell lines.
2793860	8	18	gly	O-glycosylated	1279:1292	arg1	IL-2					1300:1303	O-glycosylated human IL-2	1279:1303	O-glycosylated human IL-2	1279:1303	Our results show that O-glycosylated human IL-2 can be produced by applying recombinant DNA technology in heterologous cell lines with the same type of post-translational modification that is observed for the protein secreted from natural T lymphocytes.
2793860	5	19	theme	alpha	682:686	arg1	2-3Gal					688:693	the NeuAc alpha 2-3Gal	672:693	the NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc oligosaccharide structure	672:751	Only the NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc oligosaccharide structure or the NeuAc alpha 2-3Gal beta 1-3GalNAc were found in all IL-2 preparations secreted from recombinant Ltk-, Chinese hamster ovary, and baby hamster kidney cell lines.
2793860	5	20	theme	2-3Gal	772:777	arg1	1-3GalNAc					784:792	the NeuAc alpha 2-3Gal beta 1-3GalNAc	756:792	the NeuAc alpha 2-3Gal beta 1-3GalNAc	756:792	Only the NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc oligosaccharide structure or the NeuAc alpha 2-3Gal beta 1-3GalNAc were found in all IL-2 preparations secreted from recombinant Ltk-, Chinese hamster ovary, and baby hamster kidney cell lines.
2793860	0	21	theme	human	14:18	arg1	interleukin-2					20:32	human interleukin-2	14:32	human interleukin-2	14:32	Expression of human interleukin-2 in recombinant baby hamster kidney, Ltk-, and Chinese hamster ovary cells.
2793860	5	22	theme	hamster	894:900	arg1	kidney					902:907	baby hamster kidney	889:907	baby hamster kidney cell lines	889:918	Only the NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc oligosaccharide structure or the NeuAc alpha 2-3Gal beta 1-3GalNAc were found in all IL-2 preparations secreted from recombinant Ltk-, Chinese hamster ovary, and baby hamster kidney cell lines.
2793860	6	23	theme	chain	1005:1009	arg1	position					975:982	position 3	975:984	position 3 of the polypeptide chain which is the carbohydrate attachment site in natural human IL-2	975:1073	The O-linked chains were exclusively linked to Thr in position 3 of the polypeptide chain which is the carbohydrate attachment site in natural human IL-2.
2793860	8	24	theme	DNA	1345:1347	arg1	technology					1349:1358	recombinant DNA technology	1333:1358	recombinant DNA technology	1333:1358	Our results show that O-glycosylated human IL-2 can be produced by applying recombinant DNA technology in heterologous cell lines with the same type of post-translational modification that is observed for the protein secreted from natural T lymphocytes.
2793860	3	25	from	lines	541:545	arg1	amounts					555:561	high amounts	550:561	high amounts	550:561	Human interleukin-2 was constitutively expressed in several mammalian cell lines in high amounts.
2793860	0	26	theme	Ltk-	70:73	arg1	cells					102:106	recombinant baby hamster kidney, Ltk-, and Chinese hamster ovary cells	37:106	recombinant baby hamster kidney, Ltk-, and Chinese hamster ovary cells	37:106	Expression of human interleukin-2 in recombinant baby hamster kidney, Ltk-, and Chinese hamster ovary cells.
2793860	5	27	theme	cell	909:912	arg1	lines					914:918	baby hamster kidney cell lines	889:918	baby hamster kidney cell lines	889:918	Only the NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc oligosaccharide structure or the NeuAc alpha 2-3Gal beta 1-3GalNAc were found in all IL-2 preparations secreted from recombinant Ltk-, Chinese hamster ovary, and baby hamster kidney cell lines.
2793860	0	28	from	Expression	0:9	arg1	cells					102:106	recombinant baby hamster kidney, Ltk-, and Chinese hamster ovary cells	37:106	recombinant baby hamster kidney, Ltk-, and Chinese hamster ovary cells	37:106	Expression of human interleukin-2 in recombinant baby hamster kidney, Ltk-, and Chinese hamster ovary cells.
2793860	7	29	theme	productivity	1213:1224	arg1	independent					1198:1208	independent	1198:1208	independent	1198:1208	The proportions of O-glycosylated versus nonglycosylated forms of the protein secreted by each recombinant cell line were independent of productivity or of cell culture conditions.
2793860	7	29	theme	productivity	1213:1224	arg1	proportions					1080:1090	The proportions	1076:1090	The proportions of O-glycosylated versus nonglycosylated forms of the protein secreted by each recombinant cell line	1076:1191	The proportions of O-glycosylated versus nonglycosylated forms of the protein secreted by each recombinant cell line were independent of productivity or of cell culture conditions.
2793860	2	30	from	identity	212:219	arg1	glycoproteins					243:255	glycoproteins	243:255	glycoproteins from natural sources or produced in heterologous cell lines	243:315	The similarity or identity of O-glycosylation in glycoproteins from natural sources or produced in heterologous cell lines, a central problem for the development of many biotechnologically relevant production processes, was examined using interleukin-2 (IL-2) as a model.
2793860	8	31	theme	cell	1376:1379	arg1	lines					1381:1385	heterologous cell lines	1363:1385	heterologous cell lines with the same type of post-translational modification that is observed for the protein secreted from natural T lymphocytes	1363:1508	Our results show that O-glycosylated human IL-2 can be produced by applying recombinant DNA technology in heterologous cell lines with the same type of post-translational modification that is observed for the protein secreted from natural T lymphocytes.
2793860	2	32	theme	processes	403:411	arg1	development					344:354	the development	340:354	the development of many biotechnologically relevant production processes	340:411	The similarity or identity of O-glycosylation in glycoproteins from natural sources or produced in heterologous cell lines, a central problem for the development of many biotechnologically relevant production processes, was examined using interleukin-2 (IL-2) as a model.
2793860	5	33	theme	NeuAc	760:764	arg1	2-3Gal					772:777	NeuAc alpha 2-3Gal	760:777	the NeuAc alpha 2-3Gal beta 1-3GalNAc	756:792	Only the NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc oligosaccharide structure or the NeuAc alpha 2-3Gal beta 1-3GalNAc were found in all IL-2 preparations secreted from recombinant Ltk-, Chinese hamster ovary, and baby hamster kidney cell lines.
2793860	5	34	located	found	799:803	arg2	1-3GalNAc					784:792	the NeuAc alpha 2-3Gal beta 1-3GalNAc	756:792	the NeuAc alpha 2-3Gal beta 1-3GalNAc	756:792	Only the NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc oligosaccharide structure or the NeuAc alpha 2-3Gal beta 1-3GalNAc were found in all IL-2 preparations secreted from recombinant Ltk-, Chinese hamster ovary, and baby hamster kidney cell lines.
2793860	5	34	located	found	799:803	arg1	preparations					817:828	all IL-2 preparations	808:828	all IL-2 preparations secreted from recombinant Ltk-, Chinese hamster ovary, and baby hamster kidney cell lines	808:918	Only the NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc oligosaccharide structure or the NeuAc alpha 2-3Gal beta 1-3GalNAc were found in all IL-2 preparations secreted from recombinant Ltk-, Chinese hamster ovary, and baby hamster kidney cell lines.
2793860	5	34	located	found	799:803	arg2	structure					743:751	the NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc oligosaccharide structure	672:751	the NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc oligosaccharide structure	672:751	Only the NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc oligosaccharide structure or the NeuAc alpha 2-3Gal beta 1-3GalNAc were found in all IL-2 preparations secreted from recombinant Ltk-, Chinese hamster ovary, and baby hamster kidney cell lines.
2793860	2	35	from	O-glycosylation	224:238	arg1	glycoproteins					243:255	glycoproteins	243:255	glycoproteins from natural sources or produced in heterologous cell lines	243:315	The similarity or identity of O-glycosylation in glycoproteins from natural sources or produced in heterologous cell lines, a central problem for the development of many biotechnologically relevant production processes, was examined using interleukin-2 (IL-2) as a model.
2793860	2	35	from	O-glycosylation	224:238	arg1	sources					270:276	natural sources	262:276	natural sources or produced in heterologous cell lines	262:315	The similarity or identity of O-glycosylation in glycoproteins from natural sources or produced in heterologous cell lines, a central problem for the development of many biotechnologically relevant production processes, was examined using interleukin-2 (IL-2) as a model.
2793860	5	36	theme	alpha	766:770	arg1	2-3Gal					772:777	NeuAc alpha 2-3Gal	760:777	the NeuAc alpha 2-3Gal beta 1-3GalNAc	756:792	Only the NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc oligosaccharide structure or the NeuAc alpha 2-3Gal beta 1-3GalNAc were found in all IL-2 preparations secreted from recombinant Ltk-, Chinese hamster ovary, and baby hamster kidney cell lines.
2793860	6	37	link	O-linked	925:932	arg1	chains					934:939	The O-linked chains	921:939	The O-linked chains	921:939	The O-linked chains were exclusively linked to Thr in position 3 of the polypeptide chain which is the carbohydrate attachment site in natural human IL-2.
2793860	2	38	from	glycoproteins	243:255	arg1	identity					212:219	identity	212:219	identity	212:219	The similarity or identity of O-glycosylation in glycoproteins from natural sources or produced in heterologous cell lines, a central problem for the development of many biotechnologically relevant production processes, was examined using interleukin-2 (IL-2) as a model.
2793860	2	38	from	glycoproteins	243:255	arg1	similarity					198:207	similarity	198:207	similarity	198:207	The similarity or identity of O-glycosylation in glycoproteins from natural sources or produced in heterologous cell lines, a central problem for the development of many biotechnologically relevant production processes, was examined using interleukin-2 (IL-2) as a model.
2793860	6	39	theme	natural	1056:1062	arg1	IL-2					1070:1073	natural human IL-2	1056:1073	natural human IL-2	1056:1073	The O-linked chains were exclusively linked to Thr in position 3 of the polypeptide chain which is the carbohydrate attachment site in natural human IL-2.
2793860	6	40	from	Thr	968:970	arg1	position					975:982	position 3	975:984	position 3 of the polypeptide chain which is the carbohydrate attachment site in natural human IL-2	975:1073	The O-linked chains were exclusively linked to Thr in position 3 of the polypeptide chain which is the carbohydrate attachment site in natural human IL-2.
2793860	8	41	theme	same	1396:1399	arg1	type					1401:1404	the same type	1392:1404	the same type of post-translational modification that is observed for the protein secreted from natural T lymphocytes	1392:1508	Our results show that O-glycosylated human IL-2 can be produced by applying recombinant DNA technology in heterologous cell lines with the same type of post-translational modification that is observed for the protein secreted from natural T lymphocytes.
2793860	7	42	theme	recombinant	1171:1181	arg1	line					1188:1191	each recombinant cell line	1166:1191	each recombinant cell line	1166:1191	The proportions of O-glycosylated versus nonglycosylated forms of the protein secreted by each recombinant cell line were independent of productivity or of cell culture conditions.
2793860	1	43	theme	O-linked	122:129	arg1	chains					144:149	O-linked carbohydrate chains	122:149	O-linked carbohydrate chains	122:149	Structure of O-linked carbohydrate chains and their location within the polypeptide.
2793860	0	44	theme	kidney	62:67	arg1	cells					102:106	recombinant baby hamster kidney, Ltk-, and Chinese hamster ovary cells	37:106	recombinant baby hamster kidney, Ltk-, and Chinese hamster ovary cells	37:106	Expression of human interleukin-2 in recombinant baby hamster kidney, Ltk-, and Chinese hamster ovary cells.
2793860	1	45	link	O-linked	122:129	arg1	chains					144:149	O-linked carbohydrate chains	122:149	O-linked carbohydrate chains	122:149	Structure of O-linked carbohydrate chains and their location within the polypeptide.
2793860	6	46	theme	carbohydrate	1024:1035	arg1	site					1048:1051	the carbohydrate attachment site	1020:1051	the carbohydrate attachment site in natural human IL-2	1020:1073	The O-linked chains were exclusively linked to Thr in position 3 of the polypeptide chain which is the carbohydrate attachment site in natural human IL-2.
2793860	6	46	theme	carbohydrate	1024:1035	arg1	chain					1005:1009	the polypeptide chain	989:1009	the polypeptide chain which is the carbohydrate attachment site in natural human IL-2	989:1073	The O-linked chains were exclusively linked to Thr in position 3 of the polypeptide chain which is the carbohydrate attachment site in natural human IL-2.
2793860	7	47	theme	culture	1237:1243	arg1	conditions					1245:1254	cell culture conditions	1232:1254	cell culture conditions	1232:1254	The proportions of O-glycosylated versus nonglycosylated forms of the protein secreted by each recombinant cell line were independent of productivity or of cell culture conditions.
2793860	8	48	theme	modification	1428:1439	arg1	type					1401:1404	the same type	1392:1404	the same type of post-translational modification that is observed for the protein secreted from natural T lymphocytes	1392:1508	Our results show that O-glycosylated human IL-2 can be produced by applying recombinant DNA technology in heterologous cell lines with the same type of post-translational modification that is observed for the protein secreted from natural T lymphocytes.
2793860	7	49	theme	protein	1146:1152	arg1	forms					1133:1137	O-glycosylated versus nonglycosylated forms	1095:1137	O-glycosylated versus nonglycosylated forms of the protein secreted by each recombinant cell line	1095:1191	The proportions of O-glycosylated versus nonglycosylated forms of the protein secreted by each recombinant cell line were independent of productivity or of cell culture conditions.
2793860	2	50	theme	central	320:326	arg1	problem					328:334	a central problem	318:334	a central problem for the development of many biotechnologically relevant production processes	318:411	The similarity or identity of O-glycosylation in glycoproteins from natural sources or produced in heterologous cell lines, a central problem for the development of many biotechnologically relevant production processes, was examined using interleukin-2 (IL-2) as a model.
2793860	2	50	theme	central	320:326	arg1	O-glycosylation					224:238	O-glycosylation	224:238	O-glycosylation in glycoproteins from natural sources or produced in heterologous cell lines	224:315	The similarity or identity of O-glycosylation in glycoproteins from natural sources or produced in heterologous cell lines, a central problem for the development of many biotechnologically relevant production processes, was examined using interleukin-2 (IL-2) as a model.
2793860	1	51	theme	carbohydrate	131:142	arg1	chains					144:149	O-linked carbohydrate chains	122:149	O-linked carbohydrate chains	122:149	Structure of O-linked carbohydrate chains and their location within the polypeptide.
2793860	3	52	theme	several	518:524	arg1	lines					541:545	several mammalian cell lines	518:545	several mammalian cell lines in high amounts	518:561	Human interleukin-2 was constitutively expressed in several mammalian cell lines in high amounts.
2793860	6	53	theme	O-linked	925:932	arg1	chains					934:939	The O-linked chains	921:939	The O-linked chains	921:939	The O-linked chains were exclusively linked to Thr in position 3 of the polypeptide chain which is the carbohydrate attachment site in natural human IL-2.
2793860	7	54	theme	forms	1133:1137	arg1	proportions					1080:1090	The proportions	1076:1090	The proportions of O-glycosylated versus nonglycosylated forms of the protein secreted by each recombinant cell line	1076:1191	The proportions of O-glycosylated versus nonglycosylated forms of the protein secreted by each recombinant cell line were independent of productivity or of cell culture conditions.
2793860	7	54	theme	forms	1133:1137	arg1	independent					1198:1208	independent	1198:1208	independent	1198:1208	The proportions of O-glycosylated versus nonglycosylated forms of the protein secreted by each recombinant cell line were independent of productivity or of cell culture conditions.
2793860	5	55	theme	NeuAc	676:680	arg1	2-3Gal					688:693	the NeuAc alpha 2-3Gal	672:693	the NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc oligosaccharide structure	672:751	Only the NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc oligosaccharide structure or the NeuAc alpha 2-3Gal beta 1-3GalNAc were found in all IL-2 preparations secreted from recombinant Ltk-, Chinese hamster ovary, and baby hamster kidney cell lines.
2793860	5	56	theme	kidney	902:907	arg1	lines					914:918	baby hamster kidney cell lines	889:918	baby hamster kidney cell lines	889:918	Only the NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc oligosaccharide structure or the NeuAc alpha 2-3Gal beta 1-3GalNAc were found in all IL-2 preparations secreted from recombinant Ltk-, Chinese hamster ovary, and baby hamster kidney cell lines.
2793860	3	57	theme	cell	536:539	arg1	lines					541:545	several mammalian cell lines	518:545	several mammalian cell lines in high amounts	518:561	Human interleukin-2 was constitutively expressed in several mammalian cell lines in high amounts.
2793860	5	58	theme	hamster	870:876	arg1	ovary					878:882	Chinese hamster ovary	862:882	Chinese hamster ovary	862:882	Only the NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc oligosaccharide structure or the NeuAc alpha 2-3Gal beta 1-3GalNAc were found in all IL-2 preparations secreted from recombinant Ltk-, Chinese hamster ovary, and baby hamster kidney cell lines.
2793860	0	59	theme	baby	49:52	arg1	kidney					62:67	recombinant baby hamster kidney	37:67	recombinant baby hamster kidney	37:67	Expression of human interleukin-2 in recombinant baby hamster kidney, Ltk-, and Chinese hamster ovary cells.
2793860	6	60	from	site	1048:1051	arg1	IL-2					1070:1073	natural human IL-2	1056:1073	natural human IL-2	1056:1073	The O-linked chains were exclusively linked to Thr in position 3 of the polypeptide chain which is the carbohydrate attachment site in natural human IL-2.
2793860	2	61	theme	cell	306:309	arg1	lines					311:315	heterologous cell lines	293:315	heterologous cell lines	293:315	The similarity or identity of O-glycosylation in glycoproteins from natural sources or produced in heterologous cell lines, a central problem for the development of many biotechnologically relevant production processes, was examined using interleukin-2 (IL-2) as a model.
2793860	5	62	theme	recombinant	844:854	arg1	Ltk-					856:859	recombinant Ltk-	844:859	recombinant Ltk-	844:859	Only the NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc oligosaccharide structure or the NeuAc alpha 2-3Gal beta 1-3GalNAc were found in all IL-2 preparations secreted from recombinant Ltk-, Chinese hamster ovary, and baby hamster kidney cell lines.
2793860	5	63	theme	GalNAc	720:725	arg1	structure					743:751	the NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc oligosaccharide structure	672:751	the NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc oligosaccharide structure	672:751	Only the NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc oligosaccharide structure or the NeuAc alpha 2-3Gal beta 1-3GalNAc were found in all IL-2 preparations secreted from recombinant Ltk-, Chinese hamster ovary, and baby hamster kidney cell lines.
2793860	2	64	theme	O-glycosylation	224:238	arg1	identity					212:219	identity	212:219	identity	212:219	The similarity or identity of O-glycosylation in glycoproteins from natural sources or produced in heterologous cell lines, a central problem for the development of many biotechnologically relevant production processes, was examined using interleukin-2 (IL-2) as a model.
2793860	2	64	theme	O-glycosylation	224:238	arg1	similarity					198:207	similarity	198:207	similarity	198:207	The similarity or identity of O-glycosylation in glycoproteins from natural sources or produced in heterologous cell lines, a central problem for the development of many biotechnologically relevant production processes, was examined using interleukin-2 (IL-2) as a model.
2793860	8	65	theme	O-glycosylated	1279:1292	arg1	IL-2					1300:1303	O-glycosylated human IL-2	1279:1303	O-glycosylated human IL-2	1279:1303	Our results show that O-glycosylated human IL-2 can be produced by applying recombinant DNA technology in heterologous cell lines with the same type of post-translational modification that is observed for the protein secreted from natural T lymphocytes.
2793860	5	66	theme	2-3Gal	688:693	arg1	structure					743:751	the NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc oligosaccharide structure	672:751	the NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc oligosaccharide structure	672:751	Only the NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc oligosaccharide structure or the NeuAc alpha 2-3Gal beta 1-3GalNAc were found in all IL-2 preparations secreted from recombinant Ltk-, Chinese hamster ovary, and baby hamster kidney cell lines.
2793860	8	67	theme	T	1496:1496	arg1	lymphocytes					1498:1508	natural T lymphocytes	1488:1508	natural T lymphocytes	1488:1508	Our results show that O-glycosylated human IL-2 can be produced by applying recombinant DNA technology in heterologous cell lines with the same type of post-translational modification that is observed for the protein secreted from natural T lymphocytes.
2793860	5	68	theme	1-3[NeuAc	700:708	arg1	structure					743:751	the NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc oligosaccharide structure	672:751	the NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc oligosaccharide structure	672:751	Only the NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc oligosaccharide structure or the NeuAc alpha 2-3Gal beta 1-3GalNAc were found in all IL-2 preparations secreted from recombinant Ltk-, Chinese hamster ovary, and baby hamster kidney cell lines.
2793860	2	69	theme	natural	262:268	arg1	sources					270:276	natural sources	262:276	natural sources or produced in heterologous cell lines	262:315	The similarity or identity of O-glycosylation in glycoproteins from natural sources or produced in heterologous cell lines, a central problem for the development of many biotechnologically relevant production processes, was examined using interleukin-2 (IL-2) as a model.
2793860	2	70	from	sources	270:276	arg1	problem					328:334	a central problem	318:334	a central problem for the development of many biotechnologically relevant production processes	318:411	The similarity or identity of O-glycosylation in glycoproteins from natural sources or produced in heterologous cell lines, a central problem for the development of many biotechnologically relevant production processes, was examined using interleukin-2 (IL-2) as a model.
2793860	2	70	from	sources	270:276	arg1	glycoproteins					243:255	glycoproteins	243:255	glycoproteins from natural sources or produced in heterologous cell lines	243:315	The similarity or identity of O-glycosylation in glycoproteins from natural sources or produced in heterologous cell lines, a central problem for the development of many biotechnologically relevant production processes, was examined using interleukin-2 (IL-2) as a model.
2793860	2	70	from	sources	270:276	arg1	O-glycosylation					224:238	O-glycosylation	224:238	O-glycosylation in glycoproteins from natural sources or produced in heterologous cell lines	224:315	The similarity or identity of O-glycosylation in glycoproteins from natural sources or produced in heterologous cell lines, a central problem for the development of many biotechnologically relevant production processes, was examined using interleukin-2 (IL-2) as a model.
2793860	3	71	theme	Human	466:470	arg1	interleukin-2					472:484	Human interleukin-2	466:484	Human interleukin-2	466:484	Human interleukin-2 was constitutively expressed in several mammalian cell lines in high amounts.
2793860	7	72	theme	cell	1232:1235	arg1	conditions					1245:1254	cell culture conditions	1232:1254	cell culture conditions	1232:1254	The proportions of O-glycosylated versus nonglycosylated forms of the protein secreted by each recombinant cell line were independent of productivity or of cell culture conditions.
2793860	5	73	theme	baby	889:892	arg1	kidney					902:907	baby hamster kidney	889:907	baby hamster kidney cell lines	889:918	Only the NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc oligosaccharide structure or the NeuAc alpha 2-3Gal beta 1-3GalNAc were found in all IL-2 preparations secreted from recombinant Ltk-, Chinese hamster ovary, and baby hamster kidney cell lines.
2793860	2	74	dep	sources	270:276	arg1	produced					281:288	produced	281:288	produced in heterologous cell lines	281:315	The similarity or identity of O-glycosylation in glycoproteins from natural sources or produced in heterologous cell lines, a central problem for the development of many biotechnologically relevant production processes, was examined using interleukin-2 (IL-2) as a model.
2793860	5	75	theme	beta	779:782	arg1	1-3GalNAc					784:792	the NeuAc alpha 2-3Gal beta 1-3GalNAc	756:792	the NeuAc alpha 2-3Gal beta 1-3GalNAc	756:792	Only the NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc oligosaccharide structure or the NeuAc alpha 2-3Gal beta 1-3GalNAc were found in all IL-2 preparations secreted from recombinant Ltk-, Chinese hamster ovary, and baby hamster kidney cell lines.
2793860	1	76	theme	chains	144:149	arg1	Structure					109:117	Structure	109:117	Structure of O-linked carbohydrate chains	109:149	Structure of O-linked carbohydrate chains and their location within the polypeptide.
2793860	1	76	theme	chains	144:149	arg1	location					161:168	their location	155:168	their location within the polypeptide	155:191	Structure of O-linked carbohydrate chains and their location within the polypeptide.
2793860	6	77	theme	polypeptide	993:1003	arg1	site					1048:1051	the carbohydrate attachment site	1020:1051	the carbohydrate attachment site in natural human IL-2	1020:1073	The O-linked chains were exclusively linked to Thr in position 3 of the polypeptide chain which is the carbohydrate attachment site in natural human IL-2.
2793860	6	77	theme	polypeptide	993:1003	arg1	chain					1005:1009	the polypeptide chain	989:1009	the polypeptide chain which is the carbohydrate attachment site in natural human IL-2	989:1073	The O-linked chains were exclusively linked to Thr in position 3 of the polypeptide chain which is the carbohydrate attachment site in natural human IL-2.
2793860	8	78	theme	recombinant	1333:1343	arg1	technology					1349:1358	recombinant DNA technology	1333:1358	recombinant DNA technology	1333:1358	Our results show that O-glycosylated human IL-2 can be produced by applying recombinant DNA technology in heterologous cell lines with the same type of post-translational modification that is observed for the protein secreted from natural T lymphocytes.
2793860	0	79	theme	Chinese	80:86	arg1	ovary					96:100	Chinese hamster ovary	80:100	Chinese hamster ovary	80:100	Expression of human interleukin-2 in recombinant baby hamster kidney, Ltk-, and Chinese hamster ovary cells.
2793860	8	80	with	lines	1381:1385	arg1	type					1401:1404	the same type	1392:1404	the same type of post-translational modification that is observed for the protein secreted from natural T lymphocytes	1392:1508	Our results show that O-glycosylated human IL-2 can be produced by applying recombinant DNA technology in heterologous cell lines with the same type of post-translational modification that is observed for the protein secreted from natural T lymphocytes.
2793860	0	81	theme	ovary	96:100	arg1	cells					102:106	recombinant baby hamster kidney, Ltk-, and Chinese hamster ovary cells	37:106	recombinant baby hamster kidney, Ltk-, and Chinese hamster ovary cells	37:106	Expression of human interleukin-2 in recombinant baby hamster kidney, Ltk-, and Chinese hamster ovary cells.
2793860	8	82	theme	heterologous	1363:1374	arg1	lines					1381:1385	heterologous cell lines	1363:1385	heterologous cell lines with the same type of post-translational modification that is observed for the protein secreted from natural T lymphocytes	1363:1508	Our results show that O-glycosylated human IL-2 can be produced by applying recombinant DNA technology in heterologous cell lines with the same type of post-translational modification that is observed for the protein secreted from natural T lymphocytes.
2793860	2	83	theme	production	392:401	arg1	processes					403:411	many biotechnologically relevant production processes	359:411	many biotechnologically relevant production processes	359:411	The similarity or identity of O-glycosylation in glycoproteins from natural sources or produced in heterologous cell lines, a central problem for the development of many biotechnologically relevant production processes, was examined using interleukin-2 (IL-2) as a model.
2793860	5	84	theme	IL-2	812:815	arg1	preparations					817:828	all IL-2 preparations	808:828	all IL-2 preparations secreted from recombinant Ltk-, Chinese hamster ovary, and baby hamster kidney cell lines	808:918	Only the NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc oligosaccharide structure or the NeuAc alpha 2-3Gal beta 1-3GalNAc were found in all IL-2 preparations secreted from recombinant Ltk-, Chinese hamster ovary, and baby hamster kidney cell lines.
2793860	6	85	theme	human	1064:1068	arg1	IL-2					1070:1073	natural human IL-2	1056:1073	natural human IL-2	1056:1073	The O-linked chains were exclusively linked to Thr in position 3 of the polypeptide chain which is the carbohydrate attachment site in natural human IL-2.
2793860	0	86	theme	interleukin-2	20:32	arg1	Expression					0:9	Expression	0:9	Expression of human interleukin-2 in recombinant baby hamster kidney, Ltk-, and Chinese hamster ovary cells.	0:107	Expression of human interleukin-2 in recombinant baby hamster kidney, Ltk-, and Chinese hamster ovary cells.
2793860	4	87	theme	recombinant	568:578	arg1	proteins					580:587	The recombinant proteins	564:587	The recombinant proteins	564:587	The recombinant proteins were purified to homogeneity and their carbohydrate structures were analyzed.
2793860	2	88	theme	many	359:362	arg1	processes					403:411	many biotechnologically relevant production processes	359:411	many biotechnologically relevant production processes	359:411	The similarity or identity of O-glycosylation in glycoproteins from natural sources or produced in heterologous cell lines, a central problem for the development of many biotechnologically relevant production processes, was examined using interleukin-2 (IL-2) as a model.
2793860	0	89	theme	recombinant	37:47	arg1	kidney					62:67	recombinant baby hamster kidney	37:67	recombinant baby hamster kidney	37:67	Expression of human interleukin-2 in recombinant baby hamster kidney, Ltk-, and Chinese hamster ovary cells.
2793860	8	90	theme	human	1294:1298	arg1	IL-2					1300:1303	O-glycosylated human IL-2	1279:1303	O-glycosylated human IL-2	1279:1303	Our results show that O-glycosylated human IL-2 can be produced by applying recombinant DNA technology in heterologous cell lines with the same type of post-translational modification that is observed for the protein secreted from natural T lymphocytes.
2793860	6	91	theme	attachment	1037:1046	arg1	site					1048:1051	the carbohydrate attachment site	1020:1051	the carbohydrate attachment site in natural human IL-2	1020:1073	The O-linked chains were exclusively linked to Thr in position 3 of the polypeptide chain which is the carbohydrate attachment site in natural human IL-2.
2793860	6	91	theme	attachment	1037:1046	arg1	chain					1005:1009	the polypeptide chain	989:1009	the polypeptide chain which is the carbohydrate attachment site in natural human IL-2	989:1073	The O-linked chains were exclusively linked to Thr in position 3 of the polypeptide chain which is the carbohydrate attachment site in natural human IL-2.
2793860	2	92	dep	similarity	198:207	arg1	The					194:196	The	194:196	The	194:196	The similarity or identity of O-glycosylation in glycoproteins from natural sources or produced in heterologous cell lines, a central problem for the development of many biotechnologically relevant production processes, was examined using interleukin-2 (IL-2) as a model.
2793860	0	93	theme	hamster	88:94	arg1	ovary					96:100	Chinese hamster ovary	80:100	Chinese hamster ovary	80:100	Expression of human interleukin-2 in recombinant baby hamster kidney, Ltk-, and Chinese hamster ovary cells.
2793860	0	94	theme	hamster	54:60	arg1	kidney					62:67	recombinant baby hamster kidney	37:67	recombinant baby hamster kidney	37:67	Expression of human interleukin-2 in recombinant baby hamster kidney, Ltk-, and Chinese hamster ovary cells.
2793860	8	95	theme	post-translational	1409:1426	arg1	modification					1428:1439	post-translational modification	1409:1439	post-translational modification that is observed for the protein secreted from natural T lymphocytes	1409:1508	Our results show that O-glycosylated human IL-2 can be produced by applying recombinant DNA technology in heterologous cell lines with the same type of post-translational modification that is observed for the protein secreted from natural T lymphocytes.
2793860	4	96	theme	carbohydrate	628:639	arg1	structures					641:650	their carbohydrate structures	622:650	their carbohydrate structures	622:650	The recombinant proteins were purified to homogeneity and their carbohydrate structures were analyzed.
2793860	3	97	theme	mammalian	526:534	arg1	lines					541:545	several mammalian cell lines	518:545	several mammalian cell lines in high amounts	518:561	Human interleukin-2 was constitutively expressed in several mammalian cell lines in high amounts.
8486697	7	0	theme	CTD	841:843	arg1	digestion					824:832	proteolytic digestion	812:832	proteolytic digestion of the CTD	812:843	Glycopeptides obtained by proteolytic digestion of the CTD were purified by reverse-phase high performance liquid chromatography and sequenced.
8486697	12	1	theme	differential	1427:1438	arg1	modification					1440:1451	The differential modification	1423:1451	The differential modification of the CTD	1423:1462	The differential modification of the CTD may play an important role in the regulated expression of genes transcribed by RNA polymerase II.
8486697	5	2	mod	modified	612:619	arg3	O-GlcNAc					663:670	O-GlcNAc	663:670	O-GlcNAc	663:670	We show here that the CTD is also modified by a novel form of protein glycosylation, O-GlcNAc.
8486697	5	2	mod	modified	612:619	arg3	form					632:635	a novel form	624:635	a novel form of protein glycosylation	624:660	We show here that the CTD is also modified by a novel form of protein glycosylation, O-GlcNAc.
8486697	5	2	mod	modified	612:619	arg1	CTD					600:602	the CTD	596:602	the CTD	596:602	We show here that the CTD is also modified by a novel form of protein glycosylation, O-GlcNAc.
8486697	8	3	theme	such	943:946	arg1	experiments					948:958	such experiments	943:958	such experiments	943:958	Results from such experiments suggest that glycosylation occurs at multiple sites throughout the CTD, similar to the phosphorylation of this domain.
8486697	9	4	theme	enzyme	1158:1163	arg1	form					1146:1149	the phosphorylated form	1127:1149	the phosphorylated form of the enzyme	1127:1163	The carbohydrate, however, is not detectable on the phosphorylated form of the enzyme.
8486697	4	5	theme	regulatory	542:551	arg1	role					553:556	an important regulatory role	529:556	an important regulatory role	529:556	Indeed, phosphorylation of the CTD may play an important regulatory role in this transition.
8486697	2	6	theme	tandem	221:226	arg1	repeats					228:234	52 tandem repeats	218:234	52 tandem repeats of the consensus sequence Tyr-Ser-Pro-Thr-Ser-Pro-Ser	218:288	The largest subunit of mammalian RNA polymerase II (RNAP II) contains at its carboxyl terminus an unusual domain consisting of 52 tandem repeats of the consensus sequence Tyr-Ser-Pro-Thr-Ser-Pro-Ser.
8486697	6	7	theme	cytosolic	762:770	arg1	2					782:782	2	782:782	2	782:782	This modification has been found on numerous transcription factors and other nuclear and cytosolic proteins (2).
8486697	6	7	theme	cytosolic	762:770	arg1	proteins					772:779	other nuclear and cytosolic proteins	744:779	other nuclear and cytosolic proteins (2)	744:783	This modification has been found on numerous transcription factors and other nuclear and cytosolic proteins (2).
8486697	2	8	theme	sequence	253:260	arg1	Tyr-Ser-Pro-Thr-Ser-Pro-Ser					262:288	the consensus sequence Tyr-Ser-Pro-Thr-Ser-Pro-Ser	239:288	the consensus sequence Tyr-Ser-Pro-Thr-Ser-Pro-Ser	239:288	The largest subunit of mammalian RNA polymerase II (RNAP II) contains at its carboxyl terminus an unusual domain consisting of 52 tandem repeats of the consensus sequence Tyr-Ser-Pro-Thr-Ser-Pro-Ser.
8486697	12	9	theme	regulated	1498:1506	arg1	expression					1508:1517	the regulated expression	1494:1517	the regulated expression of genes transcribed by RNA polymerase II	1494:1559	The differential modification of the CTD may play an important role in the regulated expression of genes transcribed by RNA polymerase II.
8486697	11	10	theme	unmodified	1377:1386	arg1	states					1369:1374	three distinct conformational states	1339:1374	three distinct conformational states: unmodified, phosphorylated, and glycosylated	1339:1420	The CTD of RNAP II, therefore, appears to exist in three distinct conformational states: unmodified, phosphorylated, and glycosylated.
8486697	11	11	gly	glycosylated	1409:1420	arg1	states					1369:1374	three distinct conformational states	1339:1374	three distinct conformational states: unmodified, phosphorylated, and glycosylated	1339:1420	The CTD of RNAP II, therefore, appears to exist in three distinct conformational states: unmodified, phosphorylated, and glycosylated.
8486697	2	12	theme	consensus	243:251	arg1	Tyr-Ser-Pro-Thr-Ser-Pro-Ser					262:288	the consensus sequence Tyr-Ser-Pro-Thr-Ser-Pro-Ser	239:288	the consensus sequence Tyr-Ser-Pro-Thr-Ser-Pro-Ser	239:288	The largest subunit of mammalian RNA polymerase II (RNAP II) contains at its carboxyl terminus an unusual domain consisting of 52 tandem repeats of the consensus sequence Tyr-Ser-Pro-Thr-Ser-Pro-Ser.
8486697	10	13	theme	exclusive	1263:1271	arg1	glycosylation					1236:1248	glycosylation	1236:1248	glycosylation	1236:1248	This observation is consistent with the idea that phosphorylation and glycosylation are mutually exclusive modifications.
8486697	10	13	theme	exclusive	1263:1271	arg1	phosphorylation					1216:1230	phosphorylation	1216:1230	phosphorylation	1216:1230	This observation is consistent with the idea that phosphorylation and glycosylation are mutually exclusive modifications.
8486697	10	13	theme	exclusive	1263:1271	arg1	modifications					1273:1285	mutually exclusive modifications	1254:1285	mutually exclusive modifications	1254:1285	This observation is consistent with the idea that phosphorylation and glycosylation are mutually exclusive modifications.
8486697	11	14	theme	phosphorylated	1389:1402	arg1	states					1369:1374	three distinct conformational states	1339:1374	three distinct conformational states: unmodified, phosphorylated, and glycosylated	1339:1420	The CTD of RNAP II, therefore, appears to exist in three distinct conformational states: unmodified, phosphorylated, and glycosylated.
8486697	11	15	theme	conformational	1354:1367	arg1	states					1369:1374	three distinct conformational states	1339:1374	three distinct conformational states: unmodified, phosphorylated, and glycosylated	1339:1420	The CTD of RNAP II, therefore, appears to exist in three distinct conformational states: unmodified, phosphorylated, and glycosylated.
8486697	6	16	theme	nuclear	750:756	arg1	2					782:782	2	782:782	2	782:782	This modification has been found on numerous transcription factors and other nuclear and cytosolic proteins (2).
8486697	6	16	theme	nuclear	750:756	arg1	proteins					772:779	other nuclear and cytosolic proteins	744:779	other nuclear and cytosolic proteins (2)	744:783	This modification has been found on numerous transcription factors and other nuclear and cytosolic proteins (2).
8486697	1	17	theme	COOH-terminal	57:69	arg1	domain					71:76	the COOH-terminal domain	53:76	the COOH-terminal domain	53:76	Modification of the COOH-terminal domain by O-GlcNAc.
8486697	7	18	theme	proteolytic	812:822	arg1	digestion					824:832	proteolytic digestion	812:832	proteolytic digestion of the CTD	812:843	Glycopeptides obtained by proteolytic digestion of the CTD were purified by reverse-phase high performance liquid chromatography and sequenced.
8486697	6	19	located	found	700:704	arg1	2					782:782	2	782:782	2	782:782	This modification has been found on numerous transcription factors and other nuclear and cytosolic proteins (2).
8486697	6	19	located	found	700:704	arg1	proteins					772:779	other nuclear and cytosolic proteins	744:779	other nuclear and cytosolic proteins (2)	744:783	This modification has been found on numerous transcription factors and other nuclear and cytosolic proteins (2).
8486697	6	19	located	found	700:704	arg1	factors					732:738	numerous transcription factors	709:738	numerous transcription factors	709:738	This modification has been found on numerous transcription factors and other nuclear and cytosolic proteins (2).
8486697	6	19	located	found	700:704	arg2	modification					678:689	This modification	673:689	This modification	673:689	This modification has been found on numerous transcription factors and other nuclear and cytosolic proteins (2).
8486697	2	20	theme	polymerase	128:137	arg1	subunit					103:109	The largest subunit	91:109	The largest subunit of mammalian RNA polymerase II (RNAP II)	91:150	The largest subunit of mammalian RNA polymerase II (RNAP II) contains at its carboxyl terminus an unusual domain consisting of 52 tandem repeats of the consensus sequence Tyr-Ser-Pro-Thr-Ser-Pro-Ser.
8486697	6	21	theme	other	744:748	arg1	2					782:782	2	782:782	2	782:782	This modification has been found on numerous transcription factors and other nuclear and cytosolic proteins (2).
8486697	6	21	theme	other	744:748	arg1	proteins					772:779	other nuclear and cytosolic proteins	744:779	other nuclear and cytosolic proteins (2)	744:783	This modification has been found on numerous transcription factors and other nuclear and cytosolic proteins (2).
8486697	1	22	theme	domain	71:76	arg1	Modification					37:48	Modification	37:48	Modification of the COOH-terminal domain by O-GlcNAc	37:88	Modification of the COOH-terminal domain by O-GlcNAc.
8486697	2	23	theme	RNA	124:126	arg1	polymerase					128:137	mammalian RNA polymerase II	114:140	mammalian RNA polymerase II (RNAP II)	114:150	The largest subunit of mammalian RNA polymerase II (RNAP II) contains at its carboxyl terminus an unusual domain consisting of 52 tandem repeats of the consensus sequence Tyr-Ser-Pro-Thr-Ser-Pro-Ser.
8486697	2	23	theme	RNA	124:126	arg1	II					148:149	RNAP II	143:149	RNAP II	143:149	The largest subunit of mammalian RNA polymerase II (RNAP II) contains at its carboxyl terminus an unusual domain consisting of 52 tandem repeats of the consensus sequence Tyr-Ser-Pro-Thr-Ser-Pro-Ser.
8486697	8	24	theme	domain	1071:1076	arg1	phosphorylation					1047:1061	the phosphorylation	1043:1061	the phosphorylation of this domain	1043:1076	Results from such experiments suggest that glycosylation occurs at multiple sites throughout the CTD, similar to the phosphorylation of this domain.
8486697	0	25	theme	RNA	0:2	arg1	glycoprotein					23:34	a glycoprotein	21:34	a glycoprotein	21:34	RNA polymerase II is a glycoprotein.
8486697	0	25	theme	RNA	0:2	arg1	polymerase					4:13	RNA polymerase II	0:16	RNA polymerase II	0:16	RNA polymerase II is a glycoprotein.
8486697	8	26	theme	similar	1032:1038	arg1	CTD					1027:1029	the CTD	1023:1029	the CTD	1023:1029	Results from such experiments suggest that glycosylation occurs at multiple sites throughout the CTD, similar to the phosphorylation of this domain.
8486697	7	27	theme	high	876:879	arg1	chromatography					900:913	reverse-phase high performance liquid chromatography	862:913	reverse-phase high performance liquid chromatography	862:913	Glycopeptides obtained by proteolytic digestion of the CTD were purified by reverse-phase high performance liquid chromatography and sequenced.
8486697	2	28	contain	contains	152:159	arg1	terminus					177:184	its carboxyl terminus	164:184	its carboxyl terminus	164:184	The largest subunit of mammalian RNA polymerase II (RNAP II) contains at its carboxyl terminus an unusual domain consisting of 52 tandem repeats of the consensus sequence Tyr-Ser-Pro-Thr-Ser-Pro-Ser.
8486697	2	28	contain	contains	152:159	arg1	subunit					103:109	The largest subunit	91:109	The largest subunit of mammalian RNA polymerase II (RNAP II)	91:150	The largest subunit of mammalian RNA polymerase II (RNAP II) contains at its carboxyl terminus an unusual domain consisting of 52 tandem repeats of the consensus sequence Tyr-Ser-Pro-Thr-Ser-Pro-Ser.
8486697	2	28	contain	contains	152:159	arg2	subunit					103:109	The largest subunit	91:109	The largest subunit of mammalian RNA polymerase II (RNAP II)	91:150	The largest subunit of mammalian RNA polymerase II (RNAP II) contains at its carboxyl terminus an unusual domain consisting of 52 tandem repeats of the consensus sequence Tyr-Ser-Pro-Thr-Ser-Pro-Ser.
8486697	2	28	contain	contains	152:159	arg2	domain					197:202	an unusual domain	186:202	an unusual domain consisting of 52 tandem repeats of the consensus sequence Tyr-Ser-Pro-Thr-Ser-Pro-Ser	186:288	The largest subunit of mammalian RNA polymerase II (RNAP II) contains at its carboxyl terminus an unusual domain consisting of 52 tandem repeats of the consensus sequence Tyr-Ser-Pro-Thr-Ser-Pro-Ser.
8486697	5	29	theme	protein	640:646	arg1	glycosylation					648:660	protein glycosylation	640:660	protein glycosylation	640:660	We show here that the CTD is also modified by a novel form of protein glycosylation, O-GlcNAc.
8486697	6	30	theme	transcription	718:730	arg1	factors					732:738	numerous transcription factors	709:738	numerous transcription factors	709:738	This modification has been found on numerous transcription factors and other nuclear and cytosolic proteins (2).
8486697	9	31	theme	phosphorylated	1131:1144	arg1	form					1146:1149	the phosphorylated form	1127:1149	the phosphorylated form of the enzyme	1127:1163	The carbohydrate, however, is not detectable on the phosphorylated form of the enzyme.
8486697	3	32	theme	complex	449:455	arg1	assembly					457:464	preinitiation complex assembly	435:464	preinitiation complex assembly	435:464	This domain, designated the COOH-terminal domain (CTD), is essential for viability and is extensively phosphorylated during the transition from preinitiation complex assembly to elongation (1).
8486697	11	33	theme	RNAP	1299:1302	arg1	CTD					1292:1294	The CTD	1288:1294	The CTD of RNAP II	1288:1305	The CTD of RNAP II, therefore, appears to exist in three distinct conformational states: unmodified, phosphorylated, and glycosylated.
8486697	4	34	theme	important	532:540	arg1	role					553:556	an important regulatory role	529:556	an important regulatory role	529:556	Indeed, phosphorylation of the CTD may play an important regulatory role in this transition.
8486697	5	35	theme	glycosylation	648:660	arg1	form					632:635	a novel form	624:635	a novel form of protein glycosylation	624:660	We show here that the CTD is also modified by a novel form of protein glycosylation, O-GlcNAc.
8486697	5	35	theme	glycosylation	648:660	arg1	O-GlcNAc					663:670	O-GlcNAc	663:670	O-GlcNAc	663:670	We show here that the CTD is also modified by a novel form of protein glycosylation, O-GlcNAc.
8486697	2	36	theme	Tyr-Ser-Pro-Thr-Ser-Pro-Ser	262:288	arg1	repeats					228:234	52 tandem repeats	218:234	52 tandem repeats of the consensus sequence Tyr-Ser-Pro-Thr-Ser-Pro-Ser	218:288	The largest subunit of mammalian RNA polymerase II (RNAP II) contains at its carboxyl terminus an unusual domain consisting of 52 tandem repeats of the consensus sequence Tyr-Ser-Pro-Thr-Ser-Pro-Ser.
8486697	11	37	theme	glycosylated	1409:1420	arg1	states					1369:1374	three distinct conformational states	1339:1374	three distinct conformational states: unmodified, phosphorylated, and glycosylated	1339:1420	The CTD of RNAP II, therefore, appears to exist in three distinct conformational states: unmodified, phosphorylated, and glycosylated.
8486697	11	38	theme	distinct	1345:1352	arg1	states					1369:1374	three distinct conformational states	1339:1374	three distinct conformational states: unmodified, phosphorylated, and glycosylated	1339:1420	The CTD of RNAP II, therefore, appears to exist in three distinct conformational states: unmodified, phosphorylated, and glycosylated.
8486697	8	39	gly	glycosylation	973:985	arg2	sites					1006:1010	multiple sites	997:1010	multiple sites throughout the CTD, similar to the phosphorylation of this domain	997:1076	Results from such experiments suggest that glycosylation occurs at multiple sites throughout the CTD, similar to the phosphorylation of this domain.
8486697	12	40	theme	RNA	1543:1545	arg1	polymerase					1547:1556	RNA polymerase II	1543:1559	RNA polymerase II	1543:1559	The differential modification of the CTD may play an important role in the regulated expression of genes transcribed by RNA polymerase II.
8486697	12	41	theme	important	1476:1484	arg1	role					1486:1489	an important role	1473:1489	an important role	1473:1489	The differential modification of the CTD may play an important role in the regulated expression of genes transcribed by RNA polymerase II.
8486697	6	42	theme	numerous	709:716	arg1	factors					732:738	numerous transcription factors	709:738	numerous transcription factors	709:738	This modification has been found on numerous transcription factors and other nuclear and cytosolic proteins (2).
8486697	3	43	theme	preinitiation	435:447	arg1	assembly					457:464	preinitiation complex assembly	435:464	preinitiation complex assembly	435:464	This domain, designated the COOH-terminal domain (CTD), is essential for viability and is extensively phosphorylated during the transition from preinitiation complex assembly to elongation (1).
8486697	2	44	theme	RNAP	143:146	arg1	polymerase					128:137	mammalian RNA polymerase II	114:140	mammalian RNA polymerase II (RNAP II)	114:150	The largest subunit of mammalian RNA polymerase II (RNAP II) contains at its carboxyl terminus an unusual domain consisting of 52 tandem repeats of the consensus sequence Tyr-Ser-Pro-Thr-Ser-Pro-Ser.
8486697	2	44	theme	RNAP	143:146	arg1	II					148:149	RNAP II	143:149	RNAP II	143:149	The largest subunit of mammalian RNA polymerase II (RNAP II) contains at its carboxyl terminus an unusual domain consisting of 52 tandem repeats of the consensus sequence Tyr-Ser-Pro-Thr-Ser-Pro-Ser.
8486697	2	45	theme	unusual	189:195	arg1	domain					197:202	an unusual domain	186:202	an unusual domain consisting of 52 tandem repeats of the consensus sequence Tyr-Ser-Pro-Thr-Ser-Pro-Ser	186:288	The largest subunit of mammalian RNA polymerase II (RNAP II) contains at its carboxyl terminus an unusual domain consisting of 52 tandem repeats of the consensus sequence Tyr-Ser-Pro-Thr-Ser-Pro-Ser.
8486697	2	46	theme	largest	95:101	arg1	subunit					103:109	The largest subunit	91:109	The largest subunit of mammalian RNA polymerase II (RNAP II)	91:150	The largest subunit of mammalian RNA polymerase II (RNAP II) contains at its carboxyl terminus an unusual domain consisting of 52 tandem repeats of the consensus sequence Tyr-Ser-Pro-Thr-Ser-Pro-Ser.
8486697	4	47	theme	CTD	516:518	arg1	phosphorylation					493:507	phosphorylation	493:507	phosphorylation of the CTD	493:518	Indeed, phosphorylation of the CTD may play an important regulatory role in this transition.
8486697	5	48	theme	novel	626:630	arg1	form					632:635	a novel form	624:635	a novel form of protein glycosylation	624:660	We show here that the CTD is also modified by a novel form of protein glycosylation, O-GlcNAc.
8486697	5	48	theme	novel	626:630	arg1	O-GlcNAc					663:670	O-GlcNAc	663:670	O-GlcNAc	663:670	We show here that the CTD is also modified by a novel form of protein glycosylation, O-GlcNAc.
8486697	7	49	theme	liquid	893:898	arg1	chromatography					900:913	reverse-phase high performance liquid chromatography	862:913	reverse-phase high performance liquid chromatography	862:913	Glycopeptides obtained by proteolytic digestion of the CTD were purified by reverse-phase high performance liquid chromatography and sequenced.
8486697	8	50	from	experiments	948:958	arg1	Results					930:936	Results	930:936	Results from such experiments	930:958	Results from such experiments suggest that glycosylation occurs at multiple sites throughout the CTD, similar to the phosphorylation of this domain.
8486697	7	51	theme	performance	881:891	arg1	chromatography					900:913	reverse-phase high performance liquid chromatography	862:913	reverse-phase high performance liquid chromatography	862:913	Glycopeptides obtained by proteolytic digestion of the CTD were purified by reverse-phase high performance liquid chromatography and sequenced.
8486697	2	52	theme	carboxyl	168:175	arg1	terminus					177:184	its carboxyl terminus	164:184	its carboxyl terminus	164:184	The largest subunit of mammalian RNA polymerase II (RNAP II) contains at its carboxyl terminus an unusual domain consisting of 52 tandem repeats of the consensus sequence Tyr-Ser-Pro-Thr-Ser-Pro-Ser.
8486697	3	53	from	assembly	457:464	arg1	transition					419:428	the transition	415:428	the transition from preinitiation complex assembly to elongation (1)	415:482	This domain, designated the COOH-terminal domain (CTD), is essential for viability and is extensively phosphorylated during the transition from preinitiation complex assembly to elongation (1).
8486697	7	54	theme	reverse-phase	862:874	arg1	chromatography					900:913	reverse-phase high performance liquid chromatography	862:913	reverse-phase high performance liquid chromatography	862:913	Glycopeptides obtained by proteolytic digestion of the CTD were purified by reverse-phase high performance liquid chromatography and sequenced.
8486697	12	55	theme	CTD	1460:1462	arg1	modification					1440:1451	The differential modification	1423:1451	The differential modification of the CTD	1423:1462	The differential modification of the CTD may play an important role in the regulated expression of genes transcribed by RNA polymerase II.
8486697	0	56	gly	glycoprotein	23:34	arg1	glycoprotein					23:34	a glycoprotein	21:34	a glycoprotein	21:34	RNA polymerase II is a glycoprotein.
8486697	0	56	gly	glycoprotein	23:34	arg1	polymerase					4:13	RNA polymerase II	0:16	RNA polymerase II	0:16	RNA polymerase II is a glycoprotein.
8486697	10	57	with	consistent	1186:1195	arg1	idea					1206:1209	the idea that phosphorylation and glycosylation are mutually exclusive modifications	1202:1285	the idea that phosphorylation and glycosylation are mutually exclusive modifications	1202:1285	This observation is consistent with the idea that phosphorylation and glycosylation are mutually exclusive modifications.
8486697	8	58	theme	multiple	997:1004	arg1	sites					1006:1010	multiple sites	997:1010	multiple sites throughout the CTD, similar to the phosphorylation of this domain	997:1076	Results from such experiments suggest that glycosylation occurs at multiple sites throughout the CTD, similar to the phosphorylation of this domain.
8486697	3	59	theme	COOH-terminal	319:331	arg1	CTD					341:343	CTD	341:343	CTD	341:343	This domain, designated the COOH-terminal domain (CTD), is essential for viability and is extensively phosphorylated during the transition from preinitiation complex assembly to elongation (1).
8486697	3	59	theme	COOH-terminal	319:331	arg1	domain					333:338	the COOH-terminal domain	315:338	the COOH-terminal domain (CTD)	315:344	This domain, designated the COOH-terminal domain (CTD), is essential for viability and is extensively phosphorylated during the transition from preinitiation complex assembly to elongation (1).
8486697	2	60	theme	mammalian	114:122	arg1	polymerase					128:137	mammalian RNA polymerase II	114:140	mammalian RNA polymerase II (RNAP II)	114:150	The largest subunit of mammalian RNA polymerase II (RNAP II) contains at its carboxyl terminus an unusual domain consisting of 52 tandem repeats of the consensus sequence Tyr-Ser-Pro-Thr-Ser-Pro-Ser.
8486697	2	60	theme	mammalian	114:122	arg1	II					148:149	RNAP II	143:149	RNAP II	143:149	The largest subunit of mammalian RNA polymerase II (RNAP II) contains at its carboxyl terminus an unusual domain consisting of 52 tandem repeats of the consensus sequence Tyr-Ser-Pro-Thr-Ser-Pro-Ser.
8486697	12	61	theme	genes	1522:1526	arg1	expression					1508:1517	the regulated expression	1494:1517	the regulated expression of genes transcribed by RNA polymerase II	1494:1559	The differential modification of the CTD may play an important role in the regulated expression of genes transcribed by RNA polymerase II.
18676855	2	0	theme	polyclonal	449:458	arg1	sera					470:473	polyclonal anti-NGEP sera	449:473	polyclonal anti-NGEP sera	449:473	To determine if NGEP is a useful target for antibody-based therapy of prostate cancer, we performed an immunohistochemical analysis of 126 human prostate carcinoma samples using polyclonal anti-NGEP sera and found that 91% of the cancers express NGEP protein.
18676855	3	1	theme	extracellular	640:652	arg1	regions					654:660	the extracellular regions	636:660	the extracellular regions of NGEP	636:668	To elucidate the topology of NGEP and guide the development of monoclonal antibodies (mAb) reacting with the extracellular regions of NGEP, a hemagglutinin epitope tag was inserted at several positions within the NGEP sequence.
18676855	9	2	theme	mAb	1593:1595	arg1	development					1578:1588	the development	1574:1588	the development of mAb targeting the extracellular regions of NGEP that could be used for prostate cancer immunotherapy	1574:1692	Our findings on the expression and the orientation of the NGEP protein serve as an important framework for the development of mAb targeting the extracellular regions of NGEP that could be used for prostate cancer immunotherapy.
18676855	5	3	contain	contains	937:944	arg2	domains					966:972	eight transmembrane domains	946:972	eight transmembrane domains with both the NH(2) and COOH termini of NGEP located inside the cell	946:1041	The results indicate that NGEP contains eight transmembrane domains with both the NH(2) and COOH termini of NGEP located inside the cell.
18676855	5	3	contain	contains	937:944	arg1	NGEP					932:935	NGEP	932:935	NGEP	932:935	The results indicate that NGEP contains eight transmembrane domains with both the NH(2) and COOH termini of NGEP located inside the cell.
18676855	4	4	theme	293T	797:800	arg1	cells					802:806	293T cells	797:806	293T cells	797:806	The tagged proteins were expressed in 293T cells and locations of the tags were determined by immunofluorescence in intact or permeabilized cells.
18676855	9	5	theme	extracellular	1611:1623	arg1	regions					1625:1631	the extracellular regions	1607:1631	the extracellular regions of NGEP that could be used for prostate cancer immunotherapy	1607:1692	Our findings on the expression and the orientation of the NGEP protein serve as an important framework for the development of mAb targeting the extracellular regions of NGEP that could be used for prostate cancer immunotherapy.
18676855	2	6	theme	useful	297:302	arg1	target					304:309	a useful target	295:309	a useful target for antibody-based therapy of prostate cancer	295:355	To determine if NGEP is a useful target for antibody-based therapy of prostate cancer, we performed an immunohistochemical analysis of 126 human prostate carcinoma samples using polyclonal anti-NGEP sera and found that 91% of the cancers express NGEP protein.
18676855	2	6	theme	useful	297:302	arg1	NGEP					287:290	NGEP	287:290	NGEP	287:290	To determine if NGEP is a useful target for antibody-based therapy of prostate cancer, we performed an immunohistochemical analysis of 126 human prostate carcinoma samples using polyclonal anti-NGEP sera and found that 91% of the cancers express NGEP protein.
18676855	1	7	theme	high	221:224	arg1	concentrations					226:239	high concentrations	221:239	high concentrations at cell:cell contact regions	221:268	New gene expressed in prostate (NGEP) is a prostate-specific polytopic membrane protein found at high concentrations at cell:cell contact regions.
18676855	1	8	from	regions	262:268	arg1	concentrations					226:239	high concentrations	221:239	high concentrations at cell:cell contact regions	221:268	New gene expressed in prostate (NGEP) is a prostate-specific polytopic membrane protein found at high concentrations at cell:cell contact regions.
18676855	4	9	theme	tagged	763:768	arg1	proteins					770:777	The tagged proteins	759:777	The tagged proteins	759:777	The tagged proteins were expressed in 293T cells and locations of the tags were determined by immunofluorescence in intact or permeabilized cells.
18676855	4	10	theme	permeabilized	885:897	arg1	cells					899:903	intact or permeabilized cells	875:903	intact or permeabilized cells	875:903	The tagged proteins were expressed in 293T cells and locations of the tags were determined by immunofluorescence in intact or permeabilized cells.
18676855	4	11	theme	intact	875:880	arg1	cells					899:903	intact or permeabilized cells	875:903	intact or permeabilized cells	875:903	The tagged proteins were expressed in 293T cells and locations of the tags were determined by immunofluorescence in intact or permeabilized cells.
18676855	3	12	theme	NGEP	665:668	arg1	regions					654:660	the extracellular regions	636:660	the extracellular regions of NGEP	636:668	To elucidate the topology of NGEP and guide the development of monoclonal antibodies (mAb) reacting with the extracellular regions of NGEP, a hemagglutinin epitope tag was inserted at several positions within the NGEP sequence.
18676855	7	13	theme	predicted	1293:1301	arg1	sites					1317:1321	predicted glycosylation sites	1293:1321	predicted glycosylation sites at N809 and N824	1293:1338	NGEP is a glycoprotein with predicted glycosylation sites at N809 and N824.
18676855	5	14	dep	NH	988:989	arg1	the					984:986	the	984:986	the	984:986	The results indicate that NGEP contains eight transmembrane domains with both the NH(2) and COOH termini of NGEP located inside the cell.
18676855	7	15	gly	glycoprotein	1275:1286	arg1	NGEP					1265:1268	NGEP	1265:1268	NGEP	1265:1268	NGEP is a glycoprotein with predicted glycosylation sites at N809 and N824.
18676855	7	15	gly	glycoprotein	1275:1286	arg1	glycoprotein					1275:1286	a glycoprotein	1273:1286	a glycoprotein with predicted glycosylation sites at N809 and N824	1273:1338	NGEP is a glycoprotein with predicted glycosylation sites at N809 and N824.
18676855	5	16	theme	NGEP	1014:1017	arg1	NH					988:989	NH(2)	988:992	NH(2)	988:992	The results indicate that NGEP contains eight transmembrane domains with both the NH(2) and COOH termini of NGEP located inside the cell.
18676855	5	16	theme	NGEP	1014:1017	arg1	termini					1003:1009	COOH termini	998:1009	COOH termini of NGEP located inside the cell	998:1041	The results indicate that NGEP contains eight transmembrane domains with both the NH(2) and COOH termini of NGEP located inside the cell.
18676855	9	17	theme	NGEP	1525:1528	arg1	protein					1530:1536	the NGEP protein	1521:1536	the NGEP protein	1521:1536	Our findings on the expression and the orientation of the NGEP protein serve as an important framework for the development of mAb targeting the extracellular regions of NGEP that could be used for prostate cancer immunotherapy.
18676855	9	18	theme	prostate	1664:1671	arg1	immunotherapy					1680:1692	prostate cancer immunotherapy	1664:1692	prostate cancer immunotherapy	1664:1692	Our findings on the expression and the orientation of the NGEP protein serve as an important framework for the development of mAb targeting the extracellular regions of NGEP that could be used for prostate cancer immunotherapy.
18676855	2	19	theme	cancer	350:355	arg1	therapy					330:336	antibody-based therapy	315:336	antibody-based therapy of prostate cancer	315:355	To determine if NGEP is a useful target for antibody-based therapy of prostate cancer, we performed an immunohistochemical analysis of 126 human prostate carcinoma samples using polyclonal anti-NGEP sera and found that 91% of the cancers express NGEP protein.
18676855	0	20	theme	many	85:88	arg1	cancers					90:96	many cancers	85:96	many cancers of different grade level	85:121	Topology of NGEP, a prostate-specific cell:cell junction protein widely expressed in many cancers of different grade level.
18676855	5	21	theme	located	1019:1025	arg1	termini					1003:1009	COOH termini	998:1009	COOH termini of NGEP located inside the cell	998:1041	The results indicate that NGEP contains eight transmembrane domains with both the NH(2) and COOH termini of NGEP located inside the cell.
18676855	2	22	theme	samples	435:441	arg1	analysis					394:401	an immunohistochemical analysis	371:401	an immunohistochemical analysis of 126 human prostate carcinoma samples	371:441	To determine if NGEP is a useful target for antibody-based therapy of prostate cancer, we performed an immunohistochemical analysis of 126 human prostate carcinoma samples using polyclonal anti-NGEP sera and found that 91% of the cancers express NGEP protein.
18676855	3	23	theme	NGEP	744:747	arg1	sequence					749:756	the NGEP sequence	740:756	the NGEP sequence	740:756	To elucidate the topology of NGEP and guide the development of monoclonal antibodies (mAb) reacting with the extracellular regions of NGEP, a hemagglutinin epitope tag was inserted at several positions within the NGEP sequence.
18676855	2	24	theme	prostate	341:348	arg1	cancer					350:355	prostate cancer	341:355	prostate cancer	341:355	To determine if NGEP is a useful target for antibody-based therapy of prostate cancer, we performed an immunohistochemical analysis of 126 human prostate carcinoma samples using polyclonal anti-NGEP sera and found that 91% of the cancers express NGEP protein.
18676855	3	25	theme	hemagglutinin	673:685	arg1	tag					695:697	a hemagglutinin epitope tag	671:697	a hemagglutinin epitope tag	671:697	To elucidate the topology of NGEP and guide the development of monoclonal antibodies (mAb) reacting with the extracellular regions of NGEP, a hemagglutinin epitope tag was inserted at several positions within the NGEP sequence.
18676855	3	26	theme	epitope	687:693	arg1	tag					695:697	a hemagglutinin epitope tag	671:697	a hemagglutinin epitope tag	671:697	To elucidate the topology of NGEP and guide the development of monoclonal antibodies (mAb) reacting with the extracellular regions of NGEP, a hemagglutinin epitope tag was inserted at several positions within the NGEP sequence.
18676855	7	27	gly	glycosylation	1303:1315	arg2	N824					1335:1338	N824	1335:1338	N824	1335:1338	NGEP is a glycoprotein with predicted glycosylation sites at N809 and N824.
18676855	7	27	gly	glycosylation	1303:1315	arg2	N809					1326:1329	N809	1326:1329	N809	1326:1329	NGEP is a glycoprotein with predicted glycosylation sites at N809 and N824.
18676855	7	27	gly	glycosylation	1303:1315	arg2	sites					1317:1321	predicted glycosylation sites	1293:1321	predicted glycosylation sites at N809 and N824	1293:1338	NGEP is a glycoprotein with predicted glycosylation sites at N809 and N824.
18676855	7	28	from	N809	1326:1329	arg1	sites					1317:1321	predicted glycosylation sites	1293:1321	predicted glycosylation sites at N809 and N824	1293:1338	NGEP is a glycoprotein with predicted glycosylation sites at N809 and N824.
18676855	1	29	theme	cell	244:247	arg1	regions					262:268	cell:cell contact regions	244:268	cell:cell contact regions	244:268	New gene expressed in prostate (NGEP) is a prostate-specific polytopic membrane protein found at high concentrations at cell:cell contact regions.
18676855	7	30	theme	glycosylation	1303:1315	arg1	sites					1317:1321	predicted glycosylation sites	1293:1321	predicted glycosylation sites at N809 and N824	1293:1338	NGEP is a glycoprotein with predicted glycosylation sites at N809 and N824.
18676855	0	31	theme	different	101:109	arg1	level					117:121	different grade level	101:121	different grade level	101:121	Topology of NGEP, a prostate-specific cell:cell junction protein widely expressed in many cancers of different grade level.
18676855	6	32	theme	tag	1137:1139	arg1	data					1141:1144	the epitope tag data	1125:1144	the epitope tag data (amino acids 1-352, 441-501, and 868-933)	1125:1186	We produced mAb to three regions that are predicted to be intracellular based on the epitope tag data (amino acids 1-352, 441-501, and 868-933), and as predicted, the mAb only detected the protein in permeabilized cells.
18676855	6	32	theme	tag	1137:1139	arg1	acids					1153:1157	amino acids 1-352, 441-501, and 868-933	1147:1185	amino acids 1-352, 441-501, and 868-933	1147:1185	We produced mAb to three regions that are predicted to be intracellular based on the epitope tag data (amino acids 1-352, 441-501, and 868-933), and as predicted, the mAb only detected the protein in permeabilized cells.
18676855	0	33	theme	NGEP	12:15	arg1	Topology					0:7	Topology	0:7	Topology of NGEP, a prostate-specific cell:cell junction protein widely expressed in many cancers of different grade level.	0:122	Topology of NGEP, a prostate-specific cell:cell junction protein widely expressed in many cancers of different grade level.
18676855	1	34	theme	cell	249:252	arg1	regions					262:268	cell:cell contact regions	244:268	cell:cell contact regions	244:268	New gene expressed in prostate (NGEP) is a prostate-specific polytopic membrane protein found at high concentrations at cell:cell contact regions.
18676855	9	35	theme	important	1550:1558	arg1	framework					1560:1568	an important framework	1547:1568	an important framework for the development of mAb targeting the extracellular regions of NGEP that could be used for prostate cancer immunotherapy	1547:1692	Our findings on the expression and the orientation of the NGEP protein serve as an important framework for the development of mAb targeting the extracellular regions of NGEP that could be used for prostate cancer immunotherapy.
18676855	9	35	theme	important	1550:1558	arg1	findings					1471:1478	Our findings	1467:1478	Our findings on the expression	1467:1496	Our findings on the expression and the orientation of the NGEP protein serve as an important framework for the development of mAb targeting the extracellular regions of NGEP that could be used for prostate cancer immunotherapy.
18676855	9	35	theme	important	1550:1558	arg1	orientation					1506:1516	the orientation	1502:1516	the orientation of the NGEP protein	1502:1536	Our findings on the expression and the orientation of the NGEP protein serve as an important framework for the development of mAb targeting the extracellular regions of NGEP that could be used for prostate cancer immunotherapy.
18676855	7	36	with	glycoprotein	1275:1286	arg1	sites					1317:1321	predicted glycosylation sites	1293:1321	predicted glycosylation sites at N809 and N824	1293:1338	NGEP is a glycoprotein with predicted glycosylation sites at N809 and N824.
18676855	9	37	from	orientation	1506:1516	arg1	expression					1487:1496	the expression	1483:1496	the expression	1483:1496	Our findings on the expression and the orientation of the NGEP protein serve as an important framework for the development of mAb targeting the extracellular regions of NGEP that could be used for prostate cancer immunotherapy.
18676855	0	38	theme	prostate-specific	20:36	arg1	NGEP					12:15	NGEP	12:15	NGEP	12:15	Topology of NGEP, a prostate-specific cell:cell junction protein widely expressed in many cancers of different grade level.
18676855	0	38	theme	prostate-specific	20:36	arg1	cell					38:41	a prostate-specific cell	18:41	a prostate-specific cell	18:41	Topology of NGEP, a prostate-specific cell:cell junction protein widely expressed in many cancers of different grade level.
18676855	1	39	theme	contact	254:260	arg1	regions					262:268	cell:cell contact regions	244:268	cell:cell contact regions	244:268	New gene expressed in prostate (NGEP) is a prostate-specific polytopic membrane protein found at high concentrations at cell:cell contact regions.
18676855	0	40	theme	level	117:121	arg1	cancers					90:96	many cancers	85:96	many cancers of different grade level	85:121	Topology of NGEP, a prostate-specific cell:cell junction protein widely expressed in many cancers of different grade level.
18676855	3	41	theme	monoclonal	594:603	arg1	mAb					617:619	mAb	617:619	mAb	617:619	To elucidate the topology of NGEP and guide the development of monoclonal antibodies (mAb) reacting with the extracellular regions of NGEP, a hemagglutinin epitope tag was inserted at several positions within the NGEP sequence.
18676855	3	41	theme	monoclonal	594:603	arg1	antibodies					605:614	monoclonal antibodies	594:614	monoclonal antibodies (mAb) reacting with the extracellular regions of NGEP	594:668	To elucidate the topology of NGEP and guide the development of monoclonal antibodies (mAb) reacting with the extracellular regions of NGEP, a hemagglutinin epitope tag was inserted at several positions within the NGEP sequence.
18676855	5	42	theme	transmembrane	952:964	arg1	domains					966:972	eight transmembrane domains	946:972	eight transmembrane domains with both the NH(2) and COOH termini of NGEP located inside the cell	946:1041	The results indicate that NGEP contains eight transmembrane domains with both the NH(2) and COOH termini of NGEP located inside the cell.
18676855	2	43	theme	carcinoma	425:433	arg1	samples					435:441	126 human prostate carcinoma samples	406:441	126 human prostate carcinoma samples	406:441	To determine if NGEP is a useful target for antibody-based therapy of prostate cancer, we performed an immunohistochemical analysis of 126 human prostate carcinoma samples using polyclonal anti-NGEP sera and found that 91% of the cancers express NGEP protein.
18676855	5	44	dep	located	1019:1025	arg1	inside					1027:1032	inside	1027:1032	inside the cell	1027:1041	The results indicate that NGEP contains eight transmembrane domains with both the NH(2) and COOH termini of NGEP located inside the cell.
18676855	0	45	theme	grade	111:115	arg1	level					117:121	different grade level	101:121	different grade level	101:121	Topology of NGEP, a prostate-specific cell:cell junction protein widely expressed in many cancers of different grade level.
18676855	5	46	theme	COOH	998:1001	arg1	termini					1003:1009	COOH termini	998:1009	COOH termini of NGEP located inside the cell	998:1041	The results indicate that NGEP contains eight transmembrane domains with both the NH(2) and COOH termini of NGEP located inside the cell.
18676855	6	47	theme	epitope	1129:1135	arg1	tag					1137:1139	epitope tag	1129:1139	the epitope tag data (amino acids 1-352, 441-501, and 868-933)	1125:1186	We produced mAb to three regions that are predicted to be intracellular based on the epitope tag data (amino acids 1-352, 441-501, and 868-933), and as predicted, the mAb only detected the protein in permeabilized cells.
18676855	1	48	theme	prostate-specific	167:183	arg1	protein					204:210	a prostate-specific polytopic membrane protein	165:210	a prostate-specific polytopic membrane protein found at high concentrations at cell:cell contact regions	165:268	New gene expressed in prostate (NGEP) is a prostate-specific polytopic membrane protein found at high concentrations at cell:cell contact regions.
18676855	1	48	theme	prostate-specific	167:183	arg1	gene					128:131	New gene	124:131	New gene expressed in prostate (NGEP)	124:160	New gene expressed in prostate (NGEP) is a prostate-specific polytopic membrane protein found at high concentrations at cell:cell contact regions.
18676855	2	49	theme	prostate	416:423	arg1	samples					435:441	126 human prostate carcinoma samples	406:441	126 human prostate carcinoma samples	406:441	To determine if NGEP is a useful target for antibody-based therapy of prostate cancer, we performed an immunohistochemical analysis of 126 human prostate carcinoma samples using polyclonal anti-NGEP sera and found that 91% of the cancers express NGEP protein.
18676855	3	50	theme	several	715:721	arg1	positions					723:731	several positions	715:731	several positions within the NGEP sequence	715:756	To elucidate the topology of NGEP and guide the development of monoclonal antibodies (mAb) reacting with the extracellular regions of NGEP, a hemagglutinin epitope tag was inserted at several positions within the NGEP sequence.
18676855	0	51	theme	cell	43:46	arg1	protein					57:63	cell junction protein	43:63	Topology of NGEP, a prostate-specific cell:cell junction protein widely expressed in many cancers of different grade level.	0:122	Topology of NGEP, a prostate-specific cell:cell junction protein widely expressed in many cancers of different grade level.
18676855	1	52	located	found	212:216	arg2	gene					128:131	New gene	124:131	New gene expressed in prostate (NGEP)	124:160	New gene expressed in prostate (NGEP) is a prostate-specific polytopic membrane protein found at high concentrations at cell:cell contact regions.
18676855	1	52	located	found	212:216	arg1	concentrations					226:239	high concentrations	221:239	high concentrations at cell:cell contact regions	221:268	New gene expressed in prostate (NGEP) is a prostate-specific polytopic membrane protein found at high concentrations at cell:cell contact regions.
18676855	1	52	located	found	212:216	arg2	protein					204:210	a prostate-specific polytopic membrane protein	165:210	a prostate-specific polytopic membrane protein found at high concentrations at cell:cell contact regions	165:268	New gene expressed in prostate (NGEP) is a prostate-specific polytopic membrane protein found at high concentrations at cell:cell contact regions.
18676855	5	53	with	domains	966:972	arg1	NH					988:989	NH(2)	988:992	NH(2)	988:992	The results indicate that NGEP contains eight transmembrane domains with both the NH(2) and COOH termini of NGEP located inside the cell.
18676855	5	53	with	domains	966:972	arg1	termini					1003:1009	COOH termini	998:1009	COOH termini of NGEP located inside the cell	998:1041	The results indicate that NGEP contains eight transmembrane domains with both the NH(2) and COOH termini of NGEP located inside the cell.
18676855	2	54	theme	human	410:414	arg1	samples					435:441	126 human prostate carcinoma samples	406:441	126 human prostate carcinoma samples	406:441	To determine if NGEP is a useful target for antibody-based therapy of prostate cancer, we performed an immunohistochemical analysis of 126 human prostate carcinoma samples using polyclonal anti-NGEP sera and found that 91% of the cancers express NGEP protein.
18676855	9	55	used	used	1655:1658	arg2	regions					1625:1631	the extracellular regions	1607:1631	the extracellular regions of NGEP that could be used for prostate cancer immunotherapy	1607:1692	Our findings on the expression and the orientation of the NGEP protein serve as an important framework for the development of mAb targeting the extracellular regions of NGEP that could be used for prostate cancer immunotherapy.
18676855	2	56	theme	cancers	501:507	arg1	%					492:492	91%	490:492	91% of the cancers	490:507	To determine if NGEP is a useful target for antibody-based therapy of prostate cancer, we performed an immunohistochemical analysis of 126 human prostate carcinoma samples using polyclonal anti-NGEP sera and found that 91% of the cancers express NGEP protein.
18676855	2	56	theme	cancers	501:507	arg1	cancers					501:507	the cancers	497:507	the cancers	497:507	To determine if NGEP is a useful target for antibody-based therapy of prostate cancer, we performed an immunohistochemical analysis of 126 human prostate carcinoma samples using polyclonal anti-NGEP sera and found that 91% of the cancers express NGEP protein.
18676855	6	57	theme	amino	1147:1151	arg1	data					1141:1144	the epitope tag data	1125:1144	the epitope tag data (amino acids 1-352, 441-501, and 868-933)	1125:1186	We produced mAb to three regions that are predicted to be intracellular based on the epitope tag data (amino acids 1-352, 441-501, and 868-933), and as predicted, the mAb only detected the protein in permeabilized cells.
18676855	6	57	theme	amino	1147:1151	arg1	acids					1153:1157	amino acids 1-352, 441-501, and 868-933	1147:1185	amino acids 1-352, 441-501, and 868-933	1147:1185	We produced mAb to three regions that are predicted to be intracellular based on the epitope tag data (amino acids 1-352, 441-501, and 868-933), and as predicted, the mAb only detected the protein in permeabilized cells.
18676855	3	58	theme	NGEP	560:563	arg1	topology					548:555	the topology	544:555	the topology of NGEP	544:563	To elucidate the topology of NGEP and guide the development of monoclonal antibodies (mAb) reacting with the extracellular regions of NGEP, a hemagglutinin epitope tag was inserted at several positions within the NGEP sequence.
18676855	2	59	theme	NGEP	517:520	arg1	protein					522:528	NGEP protein	517:528	NGEP protein	517:528	To determine if NGEP is a useful target for antibody-based therapy of prostate cancer, we performed an immunohistochemical analysis of 126 human prostate carcinoma samples using polyclonal anti-NGEP sera and found that 91% of the cancers express NGEP protein.
18676855	7	60	from	N824	1335:1338	arg1	sites					1317:1321	predicted glycosylation sites	1293:1321	predicted glycosylation sites at N809 and N824	1293:1338	NGEP is a glycoprotein with predicted glycosylation sites at N809 and N824.
18676855	1	61	theme	polytopic	185:193	arg1	protein					204:210	a prostate-specific polytopic membrane protein	165:210	a prostate-specific polytopic membrane protein found at high concentrations at cell:cell contact regions	165:268	New gene expressed in prostate (NGEP) is a prostate-specific polytopic membrane protein found at high concentrations at cell:cell contact regions.
18676855	1	61	theme	polytopic	185:193	arg1	gene					128:131	New gene	124:131	New gene expressed in prostate (NGEP)	124:160	New gene expressed in prostate (NGEP) is a prostate-specific polytopic membrane protein found at high concentrations at cell:cell contact regions.
18676855	4	62	theme	tags	829:832	arg1	locations					812:820	locations	812:820	locations of the tags	812:832	The tagged proteins were expressed in 293T cells and locations of the tags were determined by immunofluorescence in intact or permeabilized cells.
18676855	3	63	theme	antibodies	605:614	arg1	development					579:589	the development	575:589	the development of monoclonal antibodies (mAb) reacting with the extracellular regions of NGEP	575:668	To elucidate the topology of NGEP and guide the development of monoclonal antibodies (mAb) reacting with the extracellular regions of NGEP, a hemagglutinin epitope tag was inserted at several positions within the NGEP sequence.
18676855	6	64	theme	permeabilized	1244:1256	arg1	cells					1258:1262	permeabilized cells	1244:1262	permeabilized cells	1244:1262	We produced mAb to three regions that are predicted to be intracellular based on the epitope tag data (amino acids 1-352, 441-501, and 868-933), and as predicted, the mAb only detected the protein in permeabilized cells.
18676855	9	65	from	findings	1471:1478	arg1	expression					1487:1496	the expression	1483:1496	the expression	1483:1496	Our findings on the expression and the orientation of the NGEP protein serve as an important framework for the development of mAb targeting the extracellular regions of NGEP that could be used for prostate cancer immunotherapy.
18676855	9	66	theme	cancer	1673:1678	arg1	immunotherapy					1680:1692	prostate cancer immunotherapy	1664:1692	prostate cancer immunotherapy	1664:1692	Our findings on the expression and the orientation of the NGEP protein serve as an important framework for the development of mAb targeting the extracellular regions of NGEP that could be used for prostate cancer immunotherapy.
18676855	1	67	theme	membrane	195:202	arg1	protein					204:210	a prostate-specific polytopic membrane protein	165:210	a prostate-specific polytopic membrane protein found at high concentrations at cell:cell contact regions	165:268	New gene expressed in prostate (NGEP) is a prostate-specific polytopic membrane protein found at high concentrations at cell:cell contact regions.
18676855	1	67	theme	membrane	195:202	arg1	gene					128:131	New gene	124:131	New gene expressed in prostate (NGEP)	124:160	New gene expressed in prostate (NGEP) is a prostate-specific polytopic membrane protein found at high concentrations at cell:cell contact regions.
18676855	0	68	theme	junction	48:55	arg1	protein					57:63	cell junction protein	43:63	Topology of NGEP, a prostate-specific cell:cell junction protein widely expressed in many cancers of different grade level.	0:122	Topology of NGEP, a prostate-specific cell:cell junction protein widely expressed in many cancers of different grade level.
18676855	2	69	theme	immunohistochemical	374:392	arg1	analysis					394:401	an immunohistochemical analysis	371:401	an immunohistochemical analysis of 126 human prostate carcinoma samples	371:441	To determine if NGEP is a useful target for antibody-based therapy of prostate cancer, we performed an immunohistochemical analysis of 126 human prostate carcinoma samples using polyclonal anti-NGEP sera and found that 91% of the cancers express NGEP protein.
18676855	2	70	theme	antibody-based	315:328	arg1	therapy					330:336	antibody-based therapy	315:336	antibody-based therapy of prostate cancer	315:355	To determine if NGEP is a useful target for antibody-based therapy of prostate cancer, we performed an immunohistochemical analysis of 126 human prostate carcinoma samples using polyclonal anti-NGEP sera and found that 91% of the cancers express NGEP protein.
18676855	9	71	theme	protein	1530:1536	arg1	framework					1560:1568	an important framework	1547:1568	an important framework for the development of mAb targeting the extracellular regions of NGEP that could be used for prostate cancer immunotherapy	1547:1692	Our findings on the expression and the orientation of the NGEP protein serve as an important framework for the development of mAb targeting the extracellular regions of NGEP that could be used for prostate cancer immunotherapy.
18676855	9	71	theme	protein	1530:1536	arg1	findings					1471:1478	Our findings	1467:1478	Our findings on the expression	1467:1496	Our findings on the expression and the orientation of the NGEP protein serve as an important framework for the development of mAb targeting the extracellular regions of NGEP that could be used for prostate cancer immunotherapy.
18676855	9	71	theme	protein	1530:1536	arg1	orientation					1506:1516	the orientation	1502:1516	the orientation of the NGEP protein	1502:1536	Our findings on the expression and the orientation of the NGEP protein serve as an important framework for the development of mAb targeting the extracellular regions of NGEP that could be used for prostate cancer immunotherapy.
18676855	2	72	theme	anti-NGEP	460:468	arg1	sera					470:473	polyclonal anti-NGEP sera	449:473	polyclonal anti-NGEP sera	449:473	To determine if NGEP is a useful target for antibody-based therapy of prostate cancer, we performed an immunohistochemical analysis of 126 human prostate carcinoma samples using polyclonal anti-NGEP sera and found that 91% of the cancers express NGEP protein.
18676855	6	73	from	protein	1233:1239	arg1	cells					1258:1262	permeabilized cells	1244:1262	permeabilized cells	1244:1262	We produced mAb to three regions that are predicted to be intracellular based on the epitope tag data (amino acids 1-352, 441-501, and 868-933), and as predicted, the mAb only detected the protein in permeabilized cells.
18676855	0	74	dep	Topology	0:7	arg1	protein					57:63	cell junction protein	43:63	Topology of NGEP, a prostate-specific cell:cell junction protein widely expressed in many cancers of different grade level.	0:122	Topology of NGEP, a prostate-specific cell:cell junction protein widely expressed in many cancers of different grade level.
18676855	1	75	theme	New	124:126	arg1	protein					204:210	a prostate-specific polytopic membrane protein	165:210	a prostate-specific polytopic membrane protein found at high concentrations at cell:cell contact regions	165:268	New gene expressed in prostate (NGEP) is a prostate-specific polytopic membrane protein found at high concentrations at cell:cell contact regions.
18676855	1	75	theme	New	124:126	arg1	gene					128:131	New gene	124:131	New gene expressed in prostate (NGEP)	124:160	New gene expressed in prostate (NGEP) is a prostate-specific polytopic membrane protein found at high concentrations at cell:cell contact regions.
18676855	9	76	theme	NGEP	1636:1639	arg1	regions					1625:1631	the extracellular regions	1607:1631	the extracellular regions of NGEP that could be used for prostate cancer immunotherapy	1607:1692	Our findings on the expression and the orientation of the NGEP protein serve as an important framework for the development of mAb targeting the extracellular regions of NGEP that could be used for prostate cancer immunotherapy.
8336134	5	0	theme	conservative	825:836	arg1	exchange					849:856	A conservative amino acid exchange	823:856	A conservative amino acid exchange (Thr instead of Ser)	823:877	A conservative amino acid exchange (Thr instead of Ser) was detected at amino acid position 154 of the beta-trace polypeptide chain in the corresponding tryptic peptide.
8336134	7	1	theme	2-6-linked	1305:1314	arg1	acid					1335:1338	2-6-linked N-acetylneuraminic acid	1305:1338	2-6-linked N-acetylneuraminic acid	1305:1338	Carbohydrate compositional as well as methylation analysis indicated that Asn29 and Asn56 bear exclusively complex-type oligosaccharide structures (partially sialylated with alpha 2-3- and/or alpha 2-6-linked N-acetylneuraminic acid) that are almost quantitatively alpha 1-6 fucosylated at the proximal N-acetylglucosamine; approximately 70% of these molecules contain a bisecting N-acetylglucosamine.
8336134	5	2	from	position	906:913	arg1	peptide					984:990	the corresponding tryptic peptide	958:990	the corresponding tryptic peptide	958:990	A conservative amino acid exchange (Thr instead of Ser) was detected at amino acid position 154 of the beta-trace polypeptide chain in the corresponding tryptic peptide.
8336134	1	3	theme	pooled	169:174	arg1	CSF					182:184	pooled human CSF	169:184	pooled human CSF	169:184	beta-Trace protein from pooled human CSF was purified to homogeneity.
8336134	4	4	theme	protein	655:661	arg1	identification					626:639	the identification	622:639	the identification of beta-trace protein	622:661	Alignment of amino acid sequences obtained from tryptic peptides with the sequence previously deduced from a cDNA clone isolated by other investigators allowed the identification of beta-trace protein as prostaglandin D synthase [prostaglandin-H2 D-isomerase; (5Z, 13E)-(15S)-9 alpha, 11 alpha-epidioxy-15-hydroxyprosta-5,13-dienoate D-isomerase; EC 5.3.99.2].
8336134	3	5	theme	Amino-terminal	352:365	arg1	sequencing					367:376	Amino-terminal sequencing	352:376	Amino-terminal sequencing of the polypeptide	352:395	Amino-terminal sequencing of the polypeptide yielded the unique amino acid sequence APEAQVSVQPNFQQDKFLGRWFSA.
8336134	5	6	theme	polypeptide	937:947	arg1	chain					949:953	the beta-trace polypeptide chain	922:953	the beta-trace polypeptide chain	922:953	A conservative amino acid exchange (Thr instead of Ser) was detected at amino acid position 154 of the beta-trace polypeptide chain in the corresponding tryptic peptide.
8336134	1	7	theme	human	176:180	arg1	CSF					182:184	pooled human CSF	169:184	pooled human CSF	169:184	beta-Trace protein from pooled human CSF was purified to homogeneity.
8336134	5	8	located	detected	883:890	arg1	position					906:913	amino acid position 154	895:917	amino acid position 154 of the beta-trace polypeptide chain in the corresponding tryptic peptide	895:990	A conservative amino acid exchange (Thr instead of Ser) was detected at amino acid position 154 of the beta-trace polypeptide chain in the corresponding tryptic peptide.
8336134	5	8	located	detected	883:890	arg2	exchange					849:856	A conservative amino acid exchange	823:856	A conservative amino acid exchange (Thr instead of Ser)	823:877	A conservative amino acid exchange (Thr instead of Ser) was detected at amino acid position 154 of the beta-trace polypeptide chain in the corresponding tryptic peptide.
8336134	4	9	theme	beta-trace	644:653	arg1	protein					655:661	beta-trace protein	644:661	beta-trace protein	644:661	Alignment of amino acid sequences obtained from tryptic peptides with the sequence previously deduced from a cDNA clone isolated by other investigators allowed the identification of beta-trace protein as prostaglandin D synthase [prostaglandin-H2 D-isomerase; (5Z, 13E)-(15S)-9 alpha, 11 alpha-epidioxy-15-hydroxyprosta-5,13-dienoate D-isomerase; EC 5.3.99.2].
8336134	4	10	theme	cDNA	571:574	arg1	clone					576:580	a cDNA clone	569:580	a cDNA clone isolated by other investigators	569:612	Alignment of amino acid sequences obtained from tryptic peptides with the sequence previously deduced from a cDNA clone isolated by other investigators allowed the identification of beta-trace protein as prostaglandin D synthase [prostaglandin-H2 D-isomerase; (5Z, 13E)-(15S)-9 alpha, 11 alpha-epidioxy-15-hydroxyprosta-5,13-dienoate D-isomerase; EC 5.3.99.2].
8336134	7	11	dep	sialylated	1265:1274	arg1	partially					1255:1263	partially	1255:1263	partially	1255:1263	Carbohydrate compositional as well as methylation analysis indicated that Asn29 and Asn56 bear exclusively complex-type oligosaccharide structures (partially sialylated with alpha 2-3- and/or alpha 2-6-linked N-acetylneuraminic acid) that are almost quantitatively alpha 1-6 fucosylated at the proximal N-acetylglucosamine; approximately 70% of these molecules contain a bisecting N-acetylglucosamine.
8336134	5	12	theme	beta-trace	926:935	arg1	chain					949:953	the beta-trace polypeptide chain	922:953	the beta-trace polypeptide chain	922:953	A conservative amino acid exchange (Thr instead of Ser) was detected at amino acid position 154 of the beta-trace polypeptide chain in the corresponding tryptic peptide.
8336134	4	13	theme	prostaglandin	666:678	arg1	synthase					682:689	prostaglandin D synthase	666:689	prostaglandin D synthase [prostaglandin-H2 D-isomerase; (5Z, 13E)	666:730	Alignment of amino acid sequences obtained from tryptic peptides with the sequence previously deduced from a cDNA clone isolated by other investigators allowed the identification of beta-trace protein as prostaglandin D synthase [prostaglandin-H2 D-isomerase; (5Z, 13E)-(15S)-9 alpha, 11 alpha-epidioxy-15-hydroxyprosta-5,13-dienoate D-isomerase; EC 5.3.99.2].
8336134	7	14	link	2-6-linked	1305:1314	arg1	acid					1335:1338	2-6-linked N-acetylneuraminic acid	1305:1338	2-6-linked N-acetylneuraminic acid	1305:1338	Carbohydrate compositional as well as methylation analysis indicated that Asn29 and Asn56 bear exclusively complex-type oligosaccharide structures (partially sialylated with alpha 2-3- and/or alpha 2-6-linked N-acetylneuraminic acid) that are almost quantitatively alpha 1-6 fucosylated at the proximal N-acetylglucosamine; approximately 70% of these molecules contain a bisecting N-acetylglucosamine.
8336134	6	15	theme	polypeptide	1030:1040	arg1	sites					1017:1021	The two N-glycosylation sites	993:1021	The two N-glycosylation sites of the polypeptide	993:1040	The two N-glycosylation sites of the polypeptide were shown to be almost quantitatively occupied by carbohydrate.
8336134	6	15	theme	polypeptide	1030:1040	arg1	polypeptide					1030:1040	the polypeptide	1026:1040	the polypeptide	1026:1040	The two N-glycosylation sites of the polypeptide were shown to be almost quantitatively occupied by carbohydrate.
8336134	7	16	theme	oligosaccharide	1227:1241	arg1	structures					1243:1252	complex-type oligosaccharide structures	1214:1252	complex-type oligosaccharide structures (partially sialylated with alpha 2-3- and/or alpha 2-6-linked N-acetylneuraminic acid) that are almost quantitatively alpha 1-6 fucosylated at the proximal N-acetylglucosamine	1214:1428	Carbohydrate compositional as well as methylation analysis indicated that Asn29 and Asn56 bear exclusively complex-type oligosaccharide structures (partially sialylated with alpha 2-3- and/or alpha 2-6-linked N-acetylneuraminic acid) that are almost quantitatively alpha 1-6 fucosylated at the proximal N-acetylglucosamine; approximately 70% of these molecules contain a bisecting N-acetylglucosamine.
8336134	7	16	theme	oligosaccharide	1227:1241	arg1	fucosylated					1382:1392	alpha 1-6 fucosylated	1372:1392	alpha 1-6 fucosylated at the proximal N-acetylglucosamine	1372:1428	Carbohydrate compositional as well as methylation analysis indicated that Asn29 and Asn56 bear exclusively complex-type oligosaccharide structures (partially sialylated with alpha 2-3- and/or alpha 2-6-linked N-acetylneuraminic acid) that are almost quantitatively alpha 1-6 fucosylated at the proximal N-acetylglucosamine; approximately 70% of these molecules contain a bisecting N-acetylglucosamine.
8336134	4	17	theme	alpha	740:744	arg1	D-isomerase					796:806	(15S)-9 alpha, 11 alpha-epidioxy-15-hydroxyprosta-5,13-dienoate D-isomerase	732:806	D-isomerase	796:806	Alignment of amino acid sequences obtained from tryptic peptides with the sequence previously deduced from a cDNA clone isolated by other investigators allowed the identification of beta-trace protein as prostaglandin D synthase [prostaglandin-H2 D-isomerase; (5Z, 13E)-(15S)-9 alpha, 11 alpha-epidioxy-15-hydroxyprosta-5,13-dienoate D-isomerase; EC 5.3.99.2].
8336134	4	18	theme	alpha-epidioxy-15-hydroxyprosta-5,13-dienoate	750:794	arg1	D-isomerase					796:806	(15S)-9 alpha, 11 alpha-epidioxy-15-hydroxyprosta-5,13-dienoate D-isomerase	732:806	D-isomerase	796:806	Alignment of amino acid sequences obtained from tryptic peptides with the sequence previously deduced from a cDNA clone isolated by other investigators allowed the identification of beta-trace protein as prostaglandin D synthase [prostaglandin-H2 D-isomerase; (5Z, 13E)-(15S)-9 alpha, 11 alpha-epidioxy-15-hydroxyprosta-5,13-dienoate D-isomerase; EC 5.3.99.2].
8336134	0	19	theme	prostaglandin	119:131	arg1	synthase					135:142	prostaglandin D synthase	119:142	prostaglandin D synthase	119:142	Purification and chemical characterization of beta-trace protein from human cerebrospinal fluid: its identification as prostaglandin D synthase.
8336134	4	20	dep	D-isomerase	709:719	arg1	5Z					723:724	5Z	723:724	5Z	723:724	Alignment of amino acid sequences obtained from tryptic peptides with the sequence previously deduced from a cDNA clone isolated by other investigators allowed the identification of beta-trace protein as prostaglandin D synthase [prostaglandin-H2 D-isomerase; (5Z, 13E)-(15S)-9 alpha, 11 alpha-epidioxy-15-hydroxyprosta-5,13-dienoate D-isomerase; EC 5.3.99.2].
8336134	4	20	dep	D-isomerase	709:719	arg1	13E					727:729	13E	727:729	13E	727:729	Alignment of amino acid sequences obtained from tryptic peptides with the sequence previously deduced from a cDNA clone isolated by other investigators allowed the identification of beta-trace protein as prostaglandin D synthase [prostaglandin-H2 D-isomerase; (5Z, 13E)-(15S)-9 alpha, 11 alpha-epidioxy-15-hydroxyprosta-5,13-dienoate D-isomerase; EC 5.3.99.2].
8336134	5	21	theme	acid	901:904	arg1	position					906:913	amino acid position 154	895:917	amino acid position 154 of the beta-trace polypeptide chain in the corresponding tryptic peptide	895:990	A conservative amino acid exchange (Thr instead of Ser) was detected at amino acid position 154 of the beta-trace polypeptide chain in the corresponding tryptic peptide.
8336134	3	22	theme	polypeptide	385:395	arg1	sequencing					367:376	Amino-terminal sequencing	352:376	Amino-terminal sequencing of the polypeptide	352:395	Amino-terminal sequencing of the polypeptide yielded the unique amino acid sequence APEAQVSVQPNFQQDKFLGRWFSA.
8336134	5	23	theme	acid	844:847	arg1	exchange					849:856	A conservative amino acid exchange	823:856	A conservative amino acid exchange (Thr instead of Ser)	823:877	A conservative amino acid exchange (Thr instead of Ser) was detected at amino acid position 154 of the beta-trace polypeptide chain in the corresponding tryptic peptide.
8336134	4	24	with	peptides	518:525	arg1	sequence					536:543	the sequence	532:543	the sequence previously deduced from a cDNA clone isolated by other investigators	532:612	Alignment of amino acid sequences obtained from tryptic peptides with the sequence previously deduced from a cDNA clone isolated by other investigators allowed the identification of beta-trace protein as prostaglandin D synthase [prostaglandin-H2 D-isomerase; (5Z, 13E)-(15S)-9 alpha, 11 alpha-epidioxy-15-hydroxyprosta-5,13-dienoate D-isomerase; EC 5.3.99.2].
8336134	3	25	theme	acid	422:425	arg1	sequence					427:434	the unique amino acid sequence	405:434	the unique amino acid sequence	405:434	Amino-terminal sequencing of the polypeptide yielded the unique amino acid sequence APEAQVSVQPNFQQDKFLGRWFSA.
8336134	5	26	theme	amino	838:842	arg1	exchange					849:856	A conservative amino acid exchange	823:856	A conservative amino acid exchange (Thr instead of Ser)	823:877	A conservative amino acid exchange (Thr instead of Ser) was detected at amino acid position 154 of the beta-trace polypeptide chain in the corresponding tryptic peptide.
8336134	7	27	theme	methylation	1145:1155	arg1	analysis					1157:1164	methylation analysis	1145:1164	Carbohydrate compositional as well as methylation analysis	1107:1164	Carbohydrate compositional as well as methylation analysis indicated that Asn29 and Asn56 bear exclusively complex-type oligosaccharide structures (partially sialylated with alpha 2-3- and/or alpha 2-6-linked N-acetylneuraminic acid) that are almost quantitatively alpha 1-6 fucosylated at the proximal N-acetylglucosamine; approximately 70% of these molecules contain a bisecting N-acetylglucosamine.
8336134	4	28	dep	D-isomerase	796:806	arg1	EC					809:810	EC 5.3.99.2	809:819	EC 5.3.99.2	809:819	Alignment of amino acid sequences obtained from tryptic peptides with the sequence previously deduced from a cDNA clone isolated by other investigators allowed the identification of beta-trace protein as prostaglandin D synthase [prostaglandin-H2 D-isomerase; (5Z, 13E)-(15S)-9 alpha, 11 alpha-epidioxy-15-hydroxyprosta-5,13-dienoate D-isomerase; EC 5.3.99.2].
8336134	7	29	theme	Carbohydrate	1107:1118	arg1	compositional					1120:1132	Carbohydrate compositional	1107:1132	Carbohydrate compositional as well as methylation analysis	1107:1164	Carbohydrate compositional as well as methylation analysis indicated that Asn29 and Asn56 bear exclusively complex-type oligosaccharide structures (partially sialylated with alpha 2-3- and/or alpha 2-6-linked N-acetylneuraminic acid) that are almost quantitatively alpha 1-6 fucosylated at the proximal N-acetylglucosamine; approximately 70% of these molecules contain a bisecting N-acetylglucosamine.
8336134	5	30	dep	exchange	849:856	arg1	Thr					859:861	Thr	859:861	Thr instead of Ser	859:876	A conservative amino acid exchange (Thr instead of Ser) was detected at amino acid position 154 of the beta-trace polypeptide chain in the corresponding tryptic peptide.
8336134	5	30	dep	exchange	849:856	arg1	Ser					874:876	Ser	874:876	Thr instead of Ser	859:876	A conservative amino acid exchange (Thr instead of Ser) was detected at amino acid position 154 of the beta-trace polypeptide chain in the corresponding tryptic peptide.
8336134	4	31	theme	acid	481:484	arg1	sequences					486:494	amino acid sequences	475:494	amino acid sequences obtained from tryptic peptides with the sequence previously deduced from a cDNA clone isolated by other investigators	475:612	Alignment of amino acid sequences obtained from tryptic peptides with the sequence previously deduced from a cDNA clone isolated by other investigators allowed the identification of beta-trace protein as prostaglandin D synthase [prostaglandin-H2 D-isomerase; (5Z, 13E)-(15S)-9 alpha, 11 alpha-epidioxy-15-hydroxyprosta-5,13-dienoate D-isomerase; EC 5.3.99.2].
8336134	2	32	theme	gel	331:333	arg1	electrophoresis					335:349	sodium dodecyl sulfate-polyacrylamide gel electrophoresis	293:349	sodium dodecyl sulfate-polyacrylamide gel electrophoresis	293:349	An apparent molecular mass of 23-29 kDa was determined for the polypeptide on sodium dodecyl sulfate-polyacrylamide gel electrophoresis.
8336134	3	33	theme	unique	409:414	arg1	sequence					427:434	the unique amino acid sequence	405:434	the unique amino acid sequence	405:434	Amino-terminal sequencing of the polypeptide yielded the unique amino acid sequence APEAQVSVQPNFQQDKFLGRWFSA.
8336134	6	34	gly	N-glycosylation	1001:1015	arg2	polypeptide					1030:1040	the polypeptide	1026:1040	the polypeptide	1026:1040	The two N-glycosylation sites of the polypeptide were shown to be almost quantitatively occupied by carbohydrate.
8336134	6	34	gly	N-glycosylation	1001:1015	arg2	sites					1017:1021	The two N-glycosylation sites	993:1021	The two N-glycosylation sites of the polypeptide	993:1040	The two N-glycosylation sites of the polypeptide were shown to be almost quantitatively occupied by carbohydrate.
8336134	6	34	gly	N-glycosylation	1001:1015	arg2	two					997:999	two	997:999	two	997:999	The two N-glycosylation sites of the polypeptide were shown to be almost quantitatively occupied by carbohydrate.
8336134	6	34	gly	N-glycosylation	1001:1015	arg1	polypeptide					1030:1040	the polypeptide	1026:1040	the polypeptide	1026:1040	The two N-glycosylation sites of the polypeptide were shown to be almost quantitatively occupied by carbohydrate.
8336134	5	35	theme	tryptic	976:982	arg1	peptide					984:990	the corresponding tryptic peptide	958:990	the corresponding tryptic peptide	958:990	A conservative amino acid exchange (Thr instead of Ser) was detected at amino acid position 154 of the beta-trace polypeptide chain in the corresponding tryptic peptide.
8336134	2	36	theme	sulfate-polyacrylamide	308:329	arg1	electrophoresis					335:349	sodium dodecyl sulfate-polyacrylamide gel electrophoresis	293:349	sodium dodecyl sulfate-polyacrylamide gel electrophoresis	293:349	An apparent molecular mass of 23-29 kDa was determined for the polypeptide on sodium dodecyl sulfate-polyacrylamide gel electrophoresis.
8336134	7	37	dep	2-3-	1287:1290	arg1	acid					1335:1338	2-6-linked N-acetylneuraminic acid	1305:1338	2-6-linked N-acetylneuraminic acid	1305:1338	Carbohydrate compositional as well as methylation analysis indicated that Asn29 and Asn56 bear exclusively complex-type oligosaccharide structures (partially sialylated with alpha 2-3- and/or alpha 2-6-linked N-acetylneuraminic acid) that are almost quantitatively alpha 1-6 fucosylated at the proximal N-acetylglucosamine; approximately 70% of these molecules contain a bisecting N-acetylglucosamine.
8336134	3	38	theme	amino	416:420	arg1	sequence					427:434	the unique amino acid sequence	405:434	the unique amino acid sequence	405:434	Amino-terminal sequencing of the polypeptide yielded the unique amino acid sequence APEAQVSVQPNFQQDKFLGRWFSA.
8336134	0	39	theme	D	133:133	arg1	synthase					135:142	prostaglandin D synthase	119:142	prostaglandin D synthase	119:142	Purification and chemical characterization of beta-trace protein from human cerebrospinal fluid: its identification as prostaglandin D synthase.
8336134	4	40	theme	tryptic	510:516	arg1	peptides					518:525	tryptic peptides	510:525	tryptic peptides with the sequence previously deduced from a cDNA clone isolated by other investigators	510:612	Alignment of amino acid sequences obtained from tryptic peptides with the sequence previously deduced from a cDNA clone isolated by other investigators allowed the identification of beta-trace protein as prostaglandin D synthase [prostaglandin-H2 D-isomerase; (5Z, 13E)-(15S)-9 alpha, 11 alpha-epidioxy-15-hydroxyprosta-5,13-dienoate D-isomerase; EC 5.3.99.2].
8336134	5	41	theme	chain	949:953	arg1	position					906:913	amino acid position 154	895:917	amino acid position 154 of the beta-trace polypeptide chain in the corresponding tryptic peptide	895:990	A conservative amino acid exchange (Thr instead of Ser) was detected at amino acid position 154 of the beta-trace polypeptide chain in the corresponding tryptic peptide.
8336134	0	42	theme	beta-trace	46:55	arg1	protein					57:63	beta-trace protein	46:63	beta-trace protein	46:63	Purification and chemical characterization of beta-trace protein from human cerebrospinal fluid: its identification as prostaglandin D synthase.
8336134	6	43	theme	N-glycosylation	1001:1015	arg1	sites					1017:1021	The two N-glycosylation sites	993:1021	The two N-glycosylation sites of the polypeptide	993:1040	The two N-glycosylation sites of the polypeptide were shown to be almost quantitatively occupied by carbohydrate.
8336134	6	43	theme	N-glycosylation	1001:1015	arg1	polypeptide					1030:1040	the polypeptide	1026:1040	the polypeptide	1026:1040	The two N-glycosylation sites of the polypeptide were shown to be almost quantitatively occupied by carbohydrate.
8336134	7	44	theme	alpha	1281:1285	arg1	2-3-					1287:1290	alpha 2-3-	1281:1290	alpha 2-3-	1281:1290	Carbohydrate compositional as well as methylation analysis indicated that Asn29 and Asn56 bear exclusively complex-type oligosaccharide structures (partially sialylated with alpha 2-3- and/or alpha 2-6-linked N-acetylneuraminic acid) that are almost quantitatively alpha 1-6 fucosylated at the proximal N-acetylglucosamine; approximately 70% of these molecules contain a bisecting N-acetylglucosamine.
8336134	0	45	from	fluid	90:94	arg1	Purification					0:11	Purification	0:11	Purification	0:11	Purification and chemical characterization of beta-trace protein from human cerebrospinal fluid: its identification as prostaglandin D synthase.
8336134	0	45	from	fluid	90:94	arg1	characterization					26:41	chemical characterization	17:41	chemical characterization	17:41	Purification and chemical characterization of beta-trace protein from human cerebrospinal fluid: its identification as prostaglandin D synthase.
8336134	7	46	theme	proximal	1401:1408	arg1	N-acetylglucosamine					1410:1428	the proximal N-acetylglucosamine	1397:1428	the proximal N-acetylglucosamine	1397:1428	Carbohydrate compositional as well as methylation analysis indicated that Asn29 and Asn56 bear exclusively complex-type oligosaccharide structures (partially sialylated with alpha 2-3- and/or alpha 2-6-linked N-acetylneuraminic acid) that are almost quantitatively alpha 1-6 fucosylated at the proximal N-acetylglucosamine; approximately 70% of these molecules contain a bisecting N-acetylglucosamine.
8336134	0	47	theme	chemical	17:24	arg1	characterization					26:41	chemical characterization	17:41	chemical characterization	17:41	Purification and chemical characterization of beta-trace protein from human cerebrospinal fluid: its identification as prostaglandin D synthase.
8336134	7	48	theme	N-acetylneuraminic	1316:1333	arg1	acid					1335:1338	2-6-linked N-acetylneuraminic acid	1305:1338	2-6-linked N-acetylneuraminic acid	1305:1338	Carbohydrate compositional as well as methylation analysis indicated that Asn29 and Asn56 bear exclusively complex-type oligosaccharide structures (partially sialylated with alpha 2-3- and/or alpha 2-6-linked N-acetylneuraminic acid) that are almost quantitatively alpha 1-6 fucosylated at the proximal N-acetylglucosamine; approximately 70% of these molecules contain a bisecting N-acetylglucosamine.
8336134	6	49	used	occupied	1081:1088	arg2	polypeptide					1030:1040	the polypeptide	1026:1040	the polypeptide	1026:1040	The two N-glycosylation sites of the polypeptide were shown to be almost quantitatively occupied by carbohydrate.
8336134	6	49	used	occupied	1081:1088	arg2	sites					1017:1021	The two N-glycosylation sites	993:1021	The two N-glycosylation sites of the polypeptide	993:1040	The two N-glycosylation sites of the polypeptide were shown to be almost quantitatively occupied by carbohydrate.
8336134	5	50	theme	amino	895:899	arg1	position					906:913	amino acid position 154	895:917	amino acid position 154 of the beta-trace polypeptide chain in the corresponding tryptic peptide	895:990	A conservative amino acid exchange (Thr instead of Ser) was detected at amino acid position 154 of the beta-trace polypeptide chain in the corresponding tryptic peptide.
8336134	4	51	theme	other	594:598	arg1	investigators					600:612	other investigators	594:612	other investigators	594:612	Alignment of amino acid sequences obtained from tryptic peptides with the sequence previously deduced from a cDNA clone isolated by other investigators allowed the identification of beta-trace protein as prostaglandin D synthase [prostaglandin-H2 D-isomerase; (5Z, 13E)-(15S)-9 alpha, 11 alpha-epidioxy-15-hydroxyprosta-5,13-dienoate D-isomerase; EC 5.3.99.2].
8336134	7	52	theme	bisecting	1478:1486	arg1	N-acetylglucosamine					1488:1506	a bisecting N-acetylglucosamine	1476:1506	a bisecting N-acetylglucosamine	1476:1506	Carbohydrate compositional as well as methylation analysis indicated that Asn29 and Asn56 bear exclusively complex-type oligosaccharide structures (partially sialylated with alpha 2-3- and/or alpha 2-6-linked N-acetylneuraminic acid) that are almost quantitatively alpha 1-6 fucosylated at the proximal N-acetylglucosamine; approximately 70% of these molecules contain a bisecting N-acetylglucosamine.
8336134	7	53	theme	alpha	1372:1376	arg1	structures					1243:1252	complex-type oligosaccharide structures	1214:1252	complex-type oligosaccharide structures (partially sialylated with alpha 2-3- and/or alpha 2-6-linked N-acetylneuraminic acid) that are almost quantitatively alpha 1-6 fucosylated at the proximal N-acetylglucosamine	1214:1428	Carbohydrate compositional as well as methylation analysis indicated that Asn29 and Asn56 bear exclusively complex-type oligosaccharide structures (partially sialylated with alpha 2-3- and/or alpha 2-6-linked N-acetylneuraminic acid) that are almost quantitatively alpha 1-6 fucosylated at the proximal N-acetylglucosamine; approximately 70% of these molecules contain a bisecting N-acetylglucosamine.
8336134	7	53	theme	alpha	1372:1376	arg1	fucosylated					1382:1392	alpha 1-6 fucosylated	1372:1392	alpha 1-6 fucosylated at the proximal N-acetylglucosamine	1372:1428	Carbohydrate compositional as well as methylation analysis indicated that Asn29 and Asn56 bear exclusively complex-type oligosaccharide structures (partially sialylated with alpha 2-3- and/or alpha 2-6-linked N-acetylneuraminic acid) that are almost quantitatively alpha 1-6 fucosylated at the proximal N-acetylglucosamine; approximately 70% of these molecules contain a bisecting N-acetylglucosamine.
8336134	0	54	theme	protein	57:63	arg1	Purification					0:11	Purification	0:11	Purification	0:11	Purification and chemical characterization of beta-trace protein from human cerebrospinal fluid: its identification as prostaglandin D synthase.
8336134	0	54	theme	protein	57:63	arg1	characterization					26:41	chemical characterization	17:41	chemical characterization	17:41	Purification and chemical characterization of beta-trace protein from human cerebrospinal fluid: its identification as prostaglandin D synthase.
8336134	7	55	gly	fucosylated	1382:1392	arg1	structures					1243:1252	complex-type oligosaccharide structures	1214:1252	complex-type oligosaccharide structures (partially sialylated with alpha 2-3- and/or alpha 2-6-linked N-acetylneuraminic acid) that are almost quantitatively alpha 1-6 fucosylated at the proximal N-acetylglucosamine	1214:1428	Carbohydrate compositional as well as methylation analysis indicated that Asn29 and Asn56 bear exclusively complex-type oligosaccharide structures (partially sialylated with alpha 2-3- and/or alpha 2-6-linked N-acetylneuraminic acid) that are almost quantitatively alpha 1-6 fucosylated at the proximal N-acetylglucosamine; approximately 70% of these molecules contain a bisecting N-acetylglucosamine.
8336134	7	55	gly	fucosylated	1382:1392	arg1	fucosylated					1382:1392	alpha 1-6 fucosylated	1372:1392	alpha 1-6 fucosylated at the proximal N-acetylglucosamine	1372:1428	Carbohydrate compositional as well as methylation analysis indicated that Asn29 and Asn56 bear exclusively complex-type oligosaccharide structures (partially sialylated with alpha 2-3- and/or alpha 2-6-linked N-acetylneuraminic acid) that are almost quantitatively alpha 1-6 fucosylated at the proximal N-acetylglucosamine; approximately 70% of these molecules contain a bisecting N-acetylglucosamine.
8336134	2	56	theme	apparent	218:225	arg1	mass					237:240	An apparent molecular mass	215:240	An apparent molecular mass of 23-29 kDa	215:253	An apparent molecular mass of 23-29 kDa was determined for the polypeptide on sodium dodecyl sulfate-polyacrylamide gel electrophoresis.
8336134	2	57	theme	molecular	227:235	arg1	mass					237:240	An apparent molecular mass	215:240	An apparent molecular mass of 23-29 kDa	215:253	An apparent molecular mass of 23-29 kDa was determined for the polypeptide on sodium dodecyl sulfate-polyacrylamide gel electrophoresis.
8336134	7	58	from	N-acetylglucosamine	1410:1428	arg1	structures					1243:1252	complex-type oligosaccharide structures	1214:1252	complex-type oligosaccharide structures (partially sialylated with alpha 2-3- and/or alpha 2-6-linked N-acetylneuraminic acid) that are almost quantitatively alpha 1-6 fucosylated at the proximal N-acetylglucosamine	1214:1428	Carbohydrate compositional as well as methylation analysis indicated that Asn29 and Asn56 bear exclusively complex-type oligosaccharide structures (partially sialylated with alpha 2-3- and/or alpha 2-6-linked N-acetylneuraminic acid) that are almost quantitatively alpha 1-6 fucosylated at the proximal N-acetylglucosamine; approximately 70% of these molecules contain a bisecting N-acetylglucosamine.
8336134	7	58	from	N-acetylglucosamine	1410:1428	arg1	fucosylated					1382:1392	alpha 1-6 fucosylated	1372:1392	alpha 1-6 fucosylated at the proximal N-acetylglucosamine	1372:1428	Carbohydrate compositional as well as methylation analysis indicated that Asn29 and Asn56 bear exclusively complex-type oligosaccharide structures (partially sialylated with alpha 2-3- and/or alpha 2-6-linked N-acetylneuraminic acid) that are almost quantitatively alpha 1-6 fucosylated at the proximal N-acetylglucosamine; approximately 70% of these molecules contain a bisecting N-acetylglucosamine.
8336134	2	59	from	polypeptide	278:288	arg1	electrophoresis					335:349	sodium dodecyl sulfate-polyacrylamide gel electrophoresis	293:349	sodium dodecyl sulfate-polyacrylamide gel electrophoresis	293:349	An apparent molecular mass of 23-29 kDa was determined for the polypeptide on sodium dodecyl sulfate-polyacrylamide gel electrophoresis.
8336134	2	60	theme	kDa	251:253	arg1	mass					237:240	An apparent molecular mass	215:240	An apparent molecular mass of 23-29 kDa	215:253	An apparent molecular mass of 23-29 kDa was determined for the polypeptide on sodium dodecyl sulfate-polyacrylamide gel electrophoresis.
8336134	7	61	theme	complex-type	1214:1225	arg1	structures					1243:1252	complex-type oligosaccharide structures	1214:1252	complex-type oligosaccharide structures (partially sialylated with alpha 2-3- and/or alpha 2-6-linked N-acetylneuraminic acid) that are almost quantitatively alpha 1-6 fucosylated at the proximal N-acetylglucosamine	1214:1428	Carbohydrate compositional as well as methylation analysis indicated that Asn29 and Asn56 bear exclusively complex-type oligosaccharide structures (partially sialylated with alpha 2-3- and/or alpha 2-6-linked N-acetylneuraminic acid) that are almost quantitatively alpha 1-6 fucosylated at the proximal N-acetylglucosamine; approximately 70% of these molecules contain a bisecting N-acetylglucosamine.
8336134	7	61	theme	complex-type	1214:1225	arg1	fucosylated					1382:1392	alpha 1-6 fucosylated	1372:1392	alpha 1-6 fucosylated at the proximal N-acetylglucosamine	1372:1428	Carbohydrate compositional as well as methylation analysis indicated that Asn29 and Asn56 bear exclusively complex-type oligosaccharide structures (partially sialylated with alpha 2-3- and/or alpha 2-6-linked N-acetylneuraminic acid) that are almost quantitatively alpha 1-6 fucosylated at the proximal N-acetylglucosamine; approximately 70% of these molecules contain a bisecting N-acetylglucosamine.
8336134	4	62	theme	amino	475:479	arg1	sequences					486:494	amino acid sequences	475:494	amino acid sequences obtained from tryptic peptides with the sequence previously deduced from a cDNA clone isolated by other investigators	475:612	Alignment of amino acid sequences obtained from tryptic peptides with the sequence previously deduced from a cDNA clone isolated by other investigators allowed the identification of beta-trace protein as prostaglandin D synthase [prostaglandin-H2 D-isomerase; (5Z, 13E)-(15S)-9 alpha, 11 alpha-epidioxy-15-hydroxyprosta-5,13-dienoate D-isomerase; EC 5.3.99.2].
8336134	7	63	theme	molecules	1458:1466	arg1	%					1447:1447	approximately 70%	1431:1447	approximately 70% of these molecules	1431:1466	Carbohydrate compositional as well as methylation analysis indicated that Asn29 and Asn56 bear exclusively complex-type oligosaccharide structures (partially sialylated with alpha 2-3- and/or alpha 2-6-linked N-acetylneuraminic acid) that are almost quantitatively alpha 1-6 fucosylated at the proximal N-acetylglucosamine; approximately 70% of these molecules contain a bisecting N-acetylglucosamine.
8336134	7	63	theme	molecules	1458:1466	arg1	molecules					1458:1466	these molecules	1452:1466	these molecules	1452:1466	Carbohydrate compositional as well as methylation analysis indicated that Asn29 and Asn56 bear exclusively complex-type oligosaccharide structures (partially sialylated with alpha 2-3- and/or alpha 2-6-linked N-acetylneuraminic acid) that are almost quantitatively alpha 1-6 fucosylated at the proximal N-acetylglucosamine; approximately 70% of these molecules contain a bisecting N-acetylglucosamine.
8336134	7	64	contain	contain	1468:1474	arg2	N-acetylglucosamine					1488:1506	a bisecting N-acetylglucosamine	1476:1506	a bisecting N-acetylglucosamine	1476:1506	Carbohydrate compositional as well as methylation analysis indicated that Asn29 and Asn56 bear exclusively complex-type oligosaccharide structures (partially sialylated with alpha 2-3- and/or alpha 2-6-linked N-acetylneuraminic acid) that are almost quantitatively alpha 1-6 fucosylated at the proximal N-acetylglucosamine; approximately 70% of these molecules contain a bisecting N-acetylglucosamine.
8336134	7	64	contain	contain	1468:1474	arg1	%					1447:1447	approximately 70%	1431:1447	approximately 70% of these molecules	1431:1466	Carbohydrate compositional as well as methylation analysis indicated that Asn29 and Asn56 bear exclusively complex-type oligosaccharide structures (partially sialylated with alpha 2-3- and/or alpha 2-6-linked N-acetylneuraminic acid) that are almost quantitatively alpha 1-6 fucosylated at the proximal N-acetylglucosamine; approximately 70% of these molecules contain a bisecting N-acetylglucosamine.
8336134	7	64	contain	contain	1468:1474	arg1	molecules					1458:1466	these molecules	1452:1466	these molecules	1452:1466	Carbohydrate compositional as well as methylation analysis indicated that Asn29 and Asn56 bear exclusively complex-type oligosaccharide structures (partially sialylated with alpha 2-3- and/or alpha 2-6-linked N-acetylneuraminic acid) that are almost quantitatively alpha 1-6 fucosylated at the proximal N-acetylglucosamine; approximately 70% of these molecules contain a bisecting N-acetylglucosamine.
8336134	5	65	theme	corresponding	962:974	arg1	peptide					984:990	the corresponding tryptic peptide	958:990	the corresponding tryptic peptide	958:990	A conservative amino acid exchange (Thr instead of Ser) was detected at amino acid position 154 of the beta-trace polypeptide chain in the corresponding tryptic peptide.
8336134	8	66	theme	Agalacto	1509:1516	arg1	structures					1518:1527	Agalacto structures	1509:1527	Agalacto structures as well as those with a peripheral fucose	1509:1569	Agalacto structures as well as those with a peripheral fucose are also present.
8336134	4	67	theme	synthase	682:689	arg1	D-isomerase					709:719	prostaglandin D synthase [prostaglandin-H2 D-isomerase	666:719	prostaglandin D synthase [prostaglandin-H2 D-isomerase; (5Z, 13E)	666:730	Alignment of amino acid sequences obtained from tryptic peptides with the sequence previously deduced from a cDNA clone isolated by other investigators allowed the identification of beta-trace protein as prostaglandin D synthase [prostaglandin-H2 D-isomerase; (5Z, 13E)-(15S)-9 alpha, 11 alpha-epidioxy-15-hydroxyprosta-5,13-dienoate D-isomerase; EC 5.3.99.2].
8336134	7	68	theme	1-6	1378:1380	arg1	structures					1243:1252	complex-type oligosaccharide structures	1214:1252	complex-type oligosaccharide structures (partially sialylated with alpha 2-3- and/or alpha 2-6-linked N-acetylneuraminic acid) that are almost quantitatively alpha 1-6 fucosylated at the proximal N-acetylglucosamine	1214:1428	Carbohydrate compositional as well as methylation analysis indicated that Asn29 and Asn56 bear exclusively complex-type oligosaccharide structures (partially sialylated with alpha 2-3- and/or alpha 2-6-linked N-acetylneuraminic acid) that are almost quantitatively alpha 1-6 fucosylated at the proximal N-acetylglucosamine; approximately 70% of these molecules contain a bisecting N-acetylglucosamine.
8336134	7	68	theme	1-6	1378:1380	arg1	fucosylated					1382:1392	alpha 1-6 fucosylated	1372:1392	alpha 1-6 fucosylated at the proximal N-acetylglucosamine	1372:1428	Carbohydrate compositional as well as methylation analysis indicated that Asn29 and Asn56 bear exclusively complex-type oligosaccharide structures (partially sialylated with alpha 2-3- and/or alpha 2-6-linked N-acetylneuraminic acid) that are almost quantitatively alpha 1-6 fucosylated at the proximal N-acetylglucosamine; approximately 70% of these molecules contain a bisecting N-acetylglucosamine.
8336134	7	69	gly	sialylated	1265:1274	arg1	structures					1243:1252	complex-type oligosaccharide structures	1214:1252	complex-type oligosaccharide structures (partially sialylated with alpha 2-3- and/or alpha 2-6-linked N-acetylneuraminic acid) that are almost quantitatively alpha 1-6 fucosylated at the proximal N-acetylglucosamine	1214:1428	Carbohydrate compositional as well as methylation analysis indicated that Asn29 and Asn56 bear exclusively complex-type oligosaccharide structures (partially sialylated with alpha 2-3- and/or alpha 2-6-linked N-acetylneuraminic acid) that are almost quantitatively alpha 1-6 fucosylated at the proximal N-acetylglucosamine; approximately 70% of these molecules contain a bisecting N-acetylglucosamine.
8336134	7	69	gly	sialylated	1265:1274	arg1	fucosylated					1382:1392	alpha 1-6 fucosylated	1372:1392	alpha 1-6 fucosylated at the proximal N-acetylglucosamine	1372:1428	Carbohydrate compositional as well as methylation analysis indicated that Asn29 and Asn56 bear exclusively complex-type oligosaccharide structures (partially sialylated with alpha 2-3- and/or alpha 2-6-linked N-acetylneuraminic acid) that are almost quantitatively alpha 1-6 fucosylated at the proximal N-acetylglucosamine; approximately 70% of these molecules contain a bisecting N-acetylglucosamine.
8336134	1	70	theme	beta-Trace	145:154	arg1	protein					156:162	beta-Trace protein	145:162	beta-Trace protein from pooled human CSF	145:184	beta-Trace protein from pooled human CSF was purified to homogeneity.
8336134	4	71	theme	D	680:680	arg1	synthase					682:689	prostaglandin D synthase	666:689	prostaglandin D synthase [prostaglandin-H2 D-isomerase; (5Z, 13E)	666:730	Alignment of amino acid sequences obtained from tryptic peptides with the sequence previously deduced from a cDNA clone isolated by other investigators allowed the identification of beta-trace protein as prostaglandin D synthase [prostaglandin-H2 D-isomerase; (5Z, 13E)-(15S)-9 alpha, 11 alpha-epidioxy-15-hydroxyprosta-5,13-dienoate D-isomerase; EC 5.3.99.2].
8336134	0	72	theme	cerebrospinal	76:88	arg1	fluid					90:94	human cerebrospinal fluid	70:94	human cerebrospinal fluid	70:94	Purification and chemical characterization of beta-trace protein from human cerebrospinal fluid: its identification as prostaglandin D synthase.
8336134	4	73	theme	sequences	486:494	arg1	Alignment					462:470	Alignment	462:470	Alignment of amino acid sequences obtained from tryptic peptides with the sequence previously deduced from a cDNA clone isolated by other investigators	462:612	Alignment of amino acid sequences obtained from tryptic peptides with the sequence previously deduced from a cDNA clone isolated by other investigators allowed the identification of beta-trace protein as prostaglandin D synthase [prostaglandin-H2 D-isomerase; (5Z, 13E)-(15S)-9 alpha, 11 alpha-epidioxy-15-hydroxyprosta-5,13-dienoate D-isomerase; EC 5.3.99.2].
8336134	8	74	theme	peripheral	1553:1562	arg1	fucose					1564:1569	a peripheral fucose	1551:1569	a peripheral fucose	1551:1569	Agalacto structures as well as those with a peripheral fucose are also present.
8336134	7	75	dep	structures	1243:1252	arg1	sialylated					1265:1274	sialylated	1265:1274	sialylated with alpha 2-3- and/or alpha 2-6-linked N-acetylneuraminic acid	1265:1338	Carbohydrate compositional as well as methylation analysis indicated that Asn29 and Asn56 bear exclusively complex-type oligosaccharide structures (partially sialylated with alpha 2-3- and/or alpha 2-6-linked N-acetylneuraminic acid) that are almost quantitatively alpha 1-6 fucosylated at the proximal N-acetylglucosamine; approximately 70% of these molecules contain a bisecting N-acetylglucosamine.
8336134	0	76	theme	human	70:74	arg1	fluid					90:94	human cerebrospinal fluid	70:94	human cerebrospinal fluid	70:94	Purification and chemical characterization of beta-trace protein from human cerebrospinal fluid: its identification as prostaglandin D synthase.
8336134	7	77	contain	bear	1197:1200	arg1	Asn56					1191:1195	Asn56	1191:1195	Asn56	1191:1195	Carbohydrate compositional as well as methylation analysis indicated that Asn29 and Asn56 bear exclusively complex-type oligosaccharide structures (partially sialylated with alpha 2-3- and/or alpha 2-6-linked N-acetylneuraminic acid) that are almost quantitatively alpha 1-6 fucosylated at the proximal N-acetylglucosamine; approximately 70% of these molecules contain a bisecting N-acetylglucosamine.
8336134	7	77	contain	bear	1197:1200	arg2	fucosylated					1382:1392	alpha 1-6 fucosylated	1372:1392	alpha 1-6 fucosylated at the proximal N-acetylglucosamine	1372:1428	Carbohydrate compositional as well as methylation analysis indicated that Asn29 and Asn56 bear exclusively complex-type oligosaccharide structures (partially sialylated with alpha 2-3- and/or alpha 2-6-linked N-acetylneuraminic acid) that are almost quantitatively alpha 1-6 fucosylated at the proximal N-acetylglucosamine; approximately 70% of these molecules contain a bisecting N-acetylglucosamine.
8336134	7	77	contain	bear	1197:1200	arg2	structures					1243:1252	complex-type oligosaccharide structures	1214:1252	complex-type oligosaccharide structures (partially sialylated with alpha 2-3- and/or alpha 2-6-linked N-acetylneuraminic acid) that are almost quantitatively alpha 1-6 fucosylated at the proximal N-acetylglucosamine	1214:1428	Carbohydrate compositional as well as methylation analysis indicated that Asn29 and Asn56 bear exclusively complex-type oligosaccharide structures (partially sialylated with alpha 2-3- and/or alpha 2-6-linked N-acetylneuraminic acid) that are almost quantitatively alpha 1-6 fucosylated at the proximal N-acetylglucosamine; approximately 70% of these molecules contain a bisecting N-acetylglucosamine.
8336134	7	77	contain	bear	1197:1200	arg1	Asn29					1181:1185	Asn29	1181:1185	Asn29	1181:1185	Carbohydrate compositional as well as methylation analysis indicated that Asn29 and Asn56 bear exclusively complex-type oligosaccharide structures (partially sialylated with alpha 2-3- and/or alpha 2-6-linked N-acetylneuraminic acid) that are almost quantitatively alpha 1-6 fucosylated at the proximal N-acetylglucosamine; approximately 70% of these molecules contain a bisecting N-acetylglucosamine.
8336134	0	78	dep	Purification	0:11	arg1	identification					101:114	its identification	97:114	Purification and chemical characterization of beta-trace protein from human cerebrospinal fluid: its identification as prostaglandin D synthase.	0:143	Purification and chemical characterization of beta-trace protein from human cerebrospinal fluid: its identification as prostaglandin D synthase.
8336134	1	79	from	CSF	182:184	arg1	protein					156:162	beta-Trace protein	145:162	beta-Trace protein from pooled human CSF	145:184	beta-Trace protein from pooled human CSF was purified to homogeneity.
8336134	4	80	theme	15S	733:735	arg1	D-isomerase					796:806	(15S)-9 alpha, 11 alpha-epidioxy-15-hydroxyprosta-5,13-dienoate D-isomerase	732:806	D-isomerase	796:806	Alignment of amino acid sequences obtained from tryptic peptides with the sequence previously deduced from a cDNA clone isolated by other investigators allowed the identification of beta-trace protein as prostaglandin D synthase [prostaglandin-H2 D-isomerase; (5Z, 13E)-(15S)-9 alpha, 11 alpha-epidioxy-15-hydroxyprosta-5,13-dienoate D-isomerase; EC 5.3.99.2].
8336134	4	81	theme	[prostaglandin-H2	691:707	arg1	D-isomerase					709:719	prostaglandin D synthase [prostaglandin-H2 D-isomerase	666:719	prostaglandin D synthase [prostaglandin-H2 D-isomerase; (5Z, 13E)	666:730	Alignment of amino acid sequences obtained from tryptic peptides with the sequence previously deduced from a cDNA clone isolated by other investigators allowed the identification of beta-trace protein as prostaglandin D synthase [prostaglandin-H2 D-isomerase; (5Z, 13E)-(15S)-9 alpha, 11 alpha-epidioxy-15-hydroxyprosta-5,13-dienoate D-isomerase; EC 5.3.99.2].
8702840	0	0	theme	motif	72:76	arg1	modification					21:32	Cytoplasmic O-GlcNAc modification	0:32	Cytoplasmic O-GlcNAc modification of the head domain and the KSP repeat motif of the neurofilament protein neurofilament-H.	0:122	Cytoplasmic O-GlcNAc modification of the head domain and the KSP repeat motif of the neurofilament protein neurofilament-H.
8702840	7	1	theme	identified	1027:1036	arg1	sites					1038:1042	the earlier identified sites	1015:1042	the earlier identified sites on NF-M and NF-L	1015:1059	Beyond the earlier identified sites on NF-M and NF-L, O-GlcNAc sites on Thr19 and Ser34 of NF-M and Ser34 and Ser48 of NF-L are also determined here, all of which are localized in head domain sequences critical for filament assembly.
8702840	7	2	theme	head	1188:1191	arg1	sequences					1200:1208	head domain sequences	1188:1208	head domain sequences critical for filament assembly	1188:1239	Beyond the earlier identified sites on NF-M and NF-L, O-GlcNAc sites on Thr19 and Ser34 of NF-M and Ser34 and Ser48 of NF-L are also determined here, all of which are localized in head domain sequences critical for filament assembly.
8702840	7	3	theme	filament	1223:1230	arg1	assembly					1232:1239	filament assembly	1223:1239	filament assembly	1223:1239	Beyond the earlier identified sites on NF-M and NF-L, O-GlcNAc sites on Thr19 and Ser34 of NF-M and Ser34 and Ser48 of NF-L are also determined here, all of which are localized in head domain sequences critical for filament assembly.
8702840	1	4	theme	intermediate	150:161	arg1	Neurofilaments					124:137	Neurofilaments	124:137	Neurofilaments	124:137	Neurofilaments, the major intermediate filaments in large myelinated neurons, are essential for specifying proper axonal caliber.
8702840	1	4	theme	intermediate	150:161	arg1	filaments					163:171	the major intermediate filaments	140:171	the major intermediate filaments in large myelinated neurons	140:199	Neurofilaments, the major intermediate filaments in large myelinated neurons, are essential for specifying proper axonal caliber.
8702840	8	5	theme	network	1442:1448	arg1	formation					1450:1458	network formation	1442:1458	network formation	1442:1458	The proximity of O-GlcNAc and phosphorylation sites in both head and tail domains of each subunit indicates that these modifications may influence one another and play a role in filament assembly and network formation.
8702840	0	6	theme	repeat	65:70	arg1	motif					72:76	the KSP repeat motif	57:76	the KSP repeat motif	57:76	Cytoplasmic O-GlcNAc modification of the head domain and the KSP repeat motif of the neurofilament protein neurofilament-H.
8702840	6	7	mod	modified	704:711	arg1	NF-H					684:687	NF-H	684:687	NF-H	684:687	Here we further report that NF-H is extensively modified by O-GlcNAc at Thr53, Ser54, and Ser56 in the head domain and, somewhat surprisingly, at multiple sites within the Lys-Ser-Pro repeat motif in the tail domain, a region in assembled neurofilaments known to be nearly stoichiometrically phosphorylated on each of the approximately 50 KSP repeats.
8702840	6	7	mod	modified	704:711	arg3	O-GlcNAc					716:723	O-GlcNAc	716:723	O-GlcNAc	716:723	Here we further report that NF-H is extensively modified by O-GlcNAc at Thr53, Ser54, and Ser56 in the head domain and, somewhat surprisingly, at multiple sites within the Lys-Ser-Pro repeat motif in the tail domain, a region in assembled neurofilaments known to be nearly stoichiometrically phosphorylated on each of the approximately 50 KSP repeats.
8702840	8	8	from	proximity	1246:1254	arg1	domains					1316:1322	both head and tail domains	1297:1322	both head and tail domains of each subunit	1297:1338	The proximity of O-GlcNAc and phosphorylation sites in both head and tail domains of each subunit indicates that these modifications may influence one another and play a role in filament assembly and network formation.
8702840	8	8	from	proximity	1246:1254	arg1	subunit					1332:1338	each subunit	1327:1338	each subunit	1327:1338	The proximity of O-GlcNAc and phosphorylation sites in both head and tail domains of each subunit indicates that these modifications may influence one another and play a role in filament assembly and network formation.
8702840	3	9	dep	Xu	538:539	arg1	W					612:612	W	612:612	W	612:612	NF-M and NF-L are known to be modified by O-linked N-acetylglucosamine (O-GlcNAc) (Dong, D. L.-Y., Xu, Z.-S., Chevrier, M. R., Cotter, R. J., Cleveland, D. W., and Hart, G. W. (1993) J. Biol.
8702840	3	9	dep	Xu	538:539	arg1	Biol					625:628	Biol	625:628	Biol	625:628	NF-M and NF-L are known to be modified by O-linked N-acetylglucosamine (O-GlcNAc) (Dong, D. L.-Y., Xu, Z.-S., Chevrier, M. R., Cotter, R. J., Cleveland, D. W., and Hart, G. W. (1993) J. Biol.
8702840	6	10	from	Thr53	728:732	arg1	domain					764:769	the head domain	755:769	the head domain	755:769	Here we further report that NF-H is extensively modified by O-GlcNAc at Thr53, Ser54, and Ser56 in the head domain and, somewhat surprisingly, at multiple sites within the Lys-Ser-Pro repeat motif in the tail domain, a region in assembled neurofilaments known to be nearly stoichiometrically phosphorylated on each of the approximately 50 KSP repeats.
8702840	8	11	theme	sites	1288:1292	arg1	proximity					1246:1254	The proximity	1242:1254	The proximity of O-GlcNAc and phosphorylation sites in both head and tail domains of each subunit	1242:1338	The proximity of O-GlcNAc and phosphorylation sites in both head and tail domains of each subunit indicates that these modifications may influence one another and play a role in filament assembly and network formation.
8702840	6	12	from	motif	847:851	arg1	domain					865:870	the tail domain	856:870	the tail domain	856:870	Here we further report that NF-H is extensively modified by O-GlcNAc at Thr53, Ser54, and Ser56 in the head domain and, somewhat surprisingly, at multiple sites within the Lys-Ser-Pro repeat motif in the tail domain, a region in assembled neurofilaments known to be nearly stoichiometrically phosphorylated on each of the approximately 50 KSP repeats.
8702840	6	12	from	motif	847:851	arg1	region					875:880	a region	873:880	a region in assembled neurofilaments known to be nearly stoichiometrically phosphorylated on each of the approximately 50 KSP repeats	873:1005	Here we further report that NF-H is extensively modified by O-GlcNAc at Thr53, Ser54, and Ser56 in the head domain and, somewhat surprisingly, at multiple sites within the Lys-Ser-Pro repeat motif in the tail domain, a region in assembled neurofilaments known to be nearly stoichiometrically phosphorylated on each of the approximately 50 KSP repeats.
8702840	1	13	from	filaments	163:171	arg1	neurons					193:199	large myelinated neurons	176:199	large myelinated neurons	176:199	Neurofilaments, the major intermediate filaments in large myelinated neurons, are essential for specifying proper axonal caliber.
8702840	6	14	theme	multiple	802:809	arg1	sites					811:815	multiple sites	802:815	multiple sites within the Lys-Ser-Pro repeat motif in the tail domain, a region in assembled neurofilaments known to be nearly stoichiometrically phosphorylated on each of the approximately 50 KSP repeats	802:1005	Here we further report that NF-H is extensively modified by O-GlcNAc at Thr53, Ser54, and Ser56 in the head domain and, somewhat surprisingly, at multiple sites within the Lys-Ser-Pro repeat motif in the tail domain, a region in assembled neurofilaments known to be nearly stoichiometrically phosphorylated on each of the approximately 50 KSP repeats.
8702840	8	15	theme	head	1302:1305	arg1	domains					1316:1322	both head and tail domains	1297:1322	both head and tail domains of each subunit	1297:1338	The proximity of O-GlcNAc and phosphorylation sites in both head and tail domains of each subunit indicates that these modifications may influence one another and play a role in filament assembly and network formation.
8702840	8	15	theme	head	1302:1305	arg1	subunit					1332:1338	each subunit	1327:1338	each subunit	1327:1338	The proximity of O-GlcNAc and phosphorylation sites in both head and tail domains of each subunit indicates that these modifications may influence one another and play a role in filament assembly and network formation.
8702840	6	16	theme	KSP	995:997	arg1	repeats					999:1005	the approximately 50 KSP repeats	974:1005	the approximately 50 KSP repeats	974:1005	Here we further report that NF-H is extensively modified by O-GlcNAc at Thr53, Ser54, and Ser56 in the head domain and, somewhat surprisingly, at multiple sites within the Lys-Ser-Pro repeat motif in the tail domain, a region in assembled neurofilaments known to be nearly stoichiometrically phosphorylated on each of the approximately 50 KSP repeats.
8702840	3	17	theme	O-linked	481:488	arg1	N-acetylglucosamine					490:508	O-linked N-acetylglucosamine	481:508	O-linked N-acetylglucosamine (O-GlcNAc)	481:519	NF-M and NF-L are known to be modified by O-linked N-acetylglucosamine (O-GlcNAc) (Dong, D. L.-Y., Xu, Z.-S., Chevrier, M. R., Cotter, R. J., Cleveland, D. W., and Hart, G. W. (1993) J. Biol.
8702840	3	17	theme	O-linked	481:488	arg1	O-GlcNAc					511:518	O-GlcNAc	511:518	O-GlcNAc	511:518	NF-M and NF-L are known to be modified by O-linked N-acetylglucosamine (O-GlcNAc) (Dong, D. L.-Y., Xu, Z.-S., Chevrier, M. R., Cotter, R. J., Cleveland, D. W., and Hart, G. W. (1993) J. Biol.
8702840	0	18	theme	protein	99:105	arg1	neurofilament-H					107:121	the neurofilament protein neurofilament-H	81:121	the neurofilament protein neurofilament-H	81:121	Cytoplasmic O-GlcNAc modification of the head domain and the KSP repeat motif of the neurofilament protein neurofilament-H.
8702840	8	19	dep	one	1389:1391	arg1	another					1393:1399	another	1393:1399	another	1393:1399	The proximity of O-GlcNAc and phosphorylation sites in both head and tail domains of each subunit indicates that these modifications may influence one another and play a role in filament assembly and network formation.
8702840	6	20	from	region	875:880	arg1	neurofilaments					895:908	assembled neurofilaments	885:908	assembled neurofilaments known to be nearly stoichiometrically phosphorylated on each of the approximately 50 KSP repeats	885:1005	Here we further report that NF-H is extensively modified by O-GlcNAc at Thr53, Ser54, and Ser56 in the head domain and, somewhat surprisingly, at multiple sites within the Lys-Ser-Pro repeat motif in the tail domain, a region in assembled neurofilaments known to be nearly stoichiometrically phosphorylated on each of the approximately 50 KSP repeats.
8702840	3	21	dep	modified	469:476	arg1	G.					609:610	G.	609:610	G.	609:610	NF-M and NF-L are known to be modified by O-linked N-acetylglucosamine (O-GlcNAc) (Dong, D. L.-Y., Xu, Z.-S., Chevrier, M. R., Cotter, R. J., Cleveland, D. W., and Hart, G. W. (1993) J. Biol.
8702840	3	21	dep	modified	469:476	arg1	Chevrier					549:556	Chevrier	549:556	Chevrier	549:556	NF-M and NF-L are known to be modified by O-linked N-acetylglucosamine (O-GlcNAc) (Dong, D. L.-Y., Xu, Z.-S., Chevrier, M. R., Cotter, R. J., Cleveland, D. W., and Hart, G. W. (1993) J. Biol.
8702840	3	21	dep	modified	469:476	arg1	D.					528:529	D.	528:529	D.	528:529	NF-M and NF-L are known to be modified by O-linked N-acetylglucosamine (O-GlcNAc) (Dong, D. L.-Y., Xu, Z.-S., Chevrier, M. R., Cotter, R. J., Cleveland, D. W., and Hart, G. W. (1993) J. Biol.
8702840	3	21	dep	modified	469:476	arg1	R.					574:575	R.	574:575	R.	574:575	NF-M and NF-L are known to be modified by O-linked N-acetylglucosamine (O-GlcNAc) (Dong, D. L.-Y., Xu, Z.-S., Chevrier, M. R., Cotter, R. J., Cleveland, D. W., and Hart, G. W. (1993) J. Biol.
8702840	3	21	dep	modified	469:476	arg1	W.					595:596	W.	595:596	W.	595:596	NF-M and NF-L are known to be modified by O-linked N-acetylglucosamine (O-GlcNAc) (Dong, D. L.-Y., Xu, Z.-S., Chevrier, M. R., Cotter, R. J., Cleveland, D. W., and Hart, G. W. (1993) J. Biol.
8702840	3	21	dep	modified	469:476	arg1	Xu					538:539	Xu	538:539	Xu	538:539	NF-M and NF-L are known to be modified by O-linked N-acetylglucosamine (O-GlcNAc) (Dong, D. L.-Y., Xu, Z.-S., Chevrier, M. R., Cotter, R. J., Cleveland, D. W., and Hart, G. W. (1993) J. Biol.
8702840	3	21	dep	modified	469:476	arg1	M.					559:560	M.	559:560	M.	559:560	NF-M and NF-L are known to be modified by O-linked N-acetylglucosamine (O-GlcNAc) (Dong, D. L.-Y., Xu, Z.-S., Chevrier, M. R., Cotter, R. J., Cleveland, D. W., and Hart, G. W. (1993) J. Biol.
8702840	3	21	dep	modified	469:476	arg1	R.					562:563	R.	562:563	R.	562:563	NF-M and NF-L are known to be modified by O-linked N-acetylglucosamine (O-GlcNAc) (Dong, D. L.-Y., Xu, Z.-S., Chevrier, M. R., Cotter, R. J., Cleveland, D. W., and Hart, G. W. (1993) J. Biol.
8702840	3	21	dep	modified	469:476	arg1	1993					616:619	1993	616:619	1993	616:619	NF-M and NF-L are known to be modified by O-linked N-acetylglucosamine (O-GlcNAc) (Dong, D. L.-Y., Xu, Z.-S., Chevrier, M. R., Cotter, R. J., Cleveland, D. W., and Hart, G. W. (1993) J. Biol.
8702840	3	21	dep	modified	469:476	arg1	Cleveland					581:589	Cleveland	581:589	Cleveland	581:589	NF-M and NF-L are known to be modified by O-linked N-acetylglucosamine (O-GlcNAc) (Dong, D. L.-Y., Xu, Z.-S., Chevrier, M. R., Cotter, R. J., Cleveland, D. W., and Hart, G. W. (1993) J. Biol.
8702840	3	21	dep	modified	469:476	arg1	D.					592:593	D.	592:593	D.	592:593	NF-M and NF-L are known to be modified by O-linked N-acetylglucosamine (O-GlcNAc) (Dong, D. L.-Y., Xu, Z.-S., Chevrier, M. R., Cotter, R. J., Cleveland, D. W., and Hart, G. W. (1993) J. Biol.
8702840	7	22	theme	Ser34	1108:1112	arg1	Ser48					1118:1122	Ser48	1118:1122	Ser48 of NF-L	1118:1130	Beyond the earlier identified sites on NF-M and NF-L, O-GlcNAc sites on Thr19 and Ser34 of NF-M and Ser34 and Ser48 of NF-L are also determined here, all of which are localized in head domain sequences critical for filament assembly.
8702840	7	22	theme	Ser34	1108:1112	arg1	Ser34					1090:1094	Ser34	1090:1094	Ser34	1090:1094	Beyond the earlier identified sites on NF-M and NF-L, O-GlcNAc sites on Thr19 and Ser34 of NF-M and Ser34 and Ser48 of NF-L are also determined here, all of which are localized in head domain sequences critical for filament assembly.
8702840	7	22	theme	Ser34	1108:1112	arg1	Thr19					1080:1084	Thr19	1080:1084	Thr19	1080:1084	Beyond the earlier identified sites on NF-M and NF-L, O-GlcNAc sites on Thr19 and Ser34 of NF-M and Ser34 and Ser48 of NF-L are also determined here, all of which are localized in head domain sequences critical for filament assembly.
8702840	0	23	theme	neurofilament	85:97	arg1	neurofilament-H					107:121	the neurofilament protein neurofilament-H	81:121	the neurofilament protein neurofilament-H	81:121	Cytoplasmic O-GlcNAc modification of the head domain and the KSP repeat motif of the neurofilament protein neurofilament-H.
8702840	8	24	theme	tail	1311:1314	arg1	domains					1316:1322	both head and tail domains	1297:1322	both head and tail domains of each subunit	1297:1338	The proximity of O-GlcNAc and phosphorylation sites in both head and tail domains of each subunit indicates that these modifications may influence one another and play a role in filament assembly and network formation.
8702840	8	24	theme	tail	1311:1314	arg1	subunit					1332:1338	each subunit	1327:1338	each subunit	1327:1338	The proximity of O-GlcNAc and phosphorylation sites in both head and tail domains of each subunit indicates that these modifications may influence one another and play a role in filament assembly and network formation.
8702840	7	25	from	sites	1071:1075	arg1	Thr19					1080:1084	Thr19	1080:1084	Thr19	1080:1084	Beyond the earlier identified sites on NF-M and NF-L, O-GlcNAc sites on Thr19 and Ser34 of NF-M and Ser34 and Ser48 of NF-L are also determined here, all of which are localized in head domain sequences critical for filament assembly.
8702840	7	25	from	sites	1071:1075	arg1	Ser34					1090:1094	Ser34	1090:1094	Ser34	1090:1094	Beyond the earlier identified sites on NF-M and NF-L, O-GlcNAc sites on Thr19 and Ser34 of NF-M and Ser34 and Ser48 of NF-L are also determined here, all of which are localized in head domain sequences critical for filament assembly.
8702840	7	25	from	sites	1071:1075	arg1	Ser48					1118:1122	Ser48	1118:1122	Ser48 of NF-L	1118:1130	Beyond the earlier identified sites on NF-M and NF-L, O-GlcNAc sites on Thr19 and Ser34 of NF-M and Ser34 and Ser48 of NF-L are also determined here, all of which are localized in head domain sequences critical for filament assembly.
8702840	2	26	theme	obligate	283:290	arg1	neurofilaments					264:277	Mammalian neurofilaments	254:277	Mammalian neurofilaments	254:277	Mammalian neurofilaments are obligate heteropolymers assembled from three polypeptides, neurofilament (NF)-H, NF-M, and NF-L, each of which undergoes phosphorylation at multiple sites.
8702840	2	26	theme	obligate	283:290	arg1	heteropolymers					292:305	obligate heteropolymers	283:305	obligate heteropolymers assembled from three polypeptides, neurofilament (NF)-H, NF-M, and NF-L, each of which undergoes phosphorylation at multiple sites	283:436	Mammalian neurofilaments are obligate heteropolymers assembled from three polypeptides, neurofilament (NF)-H, NF-M, and NF-L, each of which undergoes phosphorylation at multiple sites.
8702840	1	27	theme	large	176:180	arg1	neurons					193:199	large myelinated neurons	176:199	large myelinated neurons	176:199	Neurofilaments, the major intermediate filaments in large myelinated neurons, are essential for specifying proper axonal caliber.
8702840	0	28	theme	O-GlcNAc	12:19	arg1	modification					21:32	Cytoplasmic O-GlcNAc modification	0:32	Cytoplasmic O-GlcNAc modification of the head domain and the KSP repeat motif of the neurofilament protein neurofilament-H.	0:122	Cytoplasmic O-GlcNAc modification of the head domain and the KSP repeat motif of the neurofilament protein neurofilament-H.
8702840	6	29	from	Ser56	746:750	arg1	domain					764:769	the head domain	755:769	the head domain	755:769	Here we further report that NF-H is extensively modified by O-GlcNAc at Thr53, Ser54, and Ser56 in the head domain and, somewhat surprisingly, at multiple sites within the Lys-Ser-Pro repeat motif in the tail domain, a region in assembled neurofilaments known to be nearly stoichiometrically phosphorylated on each of the approximately 50 KSP repeats.
8702840	5	30	dep	268	637:639	arg1	16679-16687					642:652	16679-16687	642:652	16679-16687	642:652	268, 16679-16687).
8702840	2	31	theme	neurofilament	342:354	arg1	polypeptides					328:339	three polypeptides, neurofilament (NF)-H, NF-M, and NF-L	322:377	polypeptides	328:339	Mammalian neurofilaments are obligate heteropolymers assembled from three polypeptides, neurofilament (NF)-H, NF-M, and NF-L, each of which undergoes phosphorylation at multiple sites.
8702840	2	31	theme	neurofilament	342:354	arg1	-H					360:361	neurofilament (NF)-H	342:361	neurofilament (NF)-H	342:361	Mammalian neurofilaments are obligate heteropolymers assembled from three polypeptides, neurofilament (NF)-H, NF-M, and NF-L, each of which undergoes phosphorylation at multiple sites.
8702840	1	32	theme	myelinated	182:191	arg1	neurons					193:199	large myelinated neurons	176:199	large myelinated neurons	176:199	Neurofilaments, the major intermediate filaments in large myelinated neurons, are essential for specifying proper axonal caliber.
8702840	0	33	theme	Cytoplasmic	0:10	arg1	modification					21:32	Cytoplasmic O-GlcNAc modification	0:32	Cytoplasmic O-GlcNAc modification of the head domain and the KSP repeat motif of the neurofilament protein neurofilament-H.	0:122	Cytoplasmic O-GlcNAc modification of the head domain and the KSP repeat motif of the neurofilament protein neurofilament-H.
8702840	7	34	located	localized	1175:1183	arg2	which					1165:1169	which	1165:1169	which	1165:1169	Beyond the earlier identified sites on NF-M and NF-L, O-GlcNAc sites on Thr19 and Ser34 of NF-M and Ser34 and Ser48 of NF-L are also determined here, all of which are localized in head domain sequences critical for filament assembly.
8702840	7	34	located	localized	1175:1183	arg2	all					1158:1160	all	1158:1160	all	1158:1160	Beyond the earlier identified sites on NF-M and NF-L, O-GlcNAc sites on Thr19 and Ser34 of NF-M and Ser34 and Ser48 of NF-L are also determined here, all of which are localized in head domain sequences critical for filament assembly.
8702840	7	34	located	localized	1175:1183	arg1	sequences					1200:1208	head domain sequences	1188:1208	head domain sequences critical for filament assembly	1188:1239	Beyond the earlier identified sites on NF-M and NF-L, O-GlcNAc sites on Thr19 and Ser34 of NF-M and Ser34 and Ser48 of NF-L are also determined here, all of which are localized in head domain sequences critical for filament assembly.
8702840	3	35	link	O-linked	481:488	arg1	N-acetylglucosamine					490:508	O-linked N-acetylglucosamine	481:508	O-linked N-acetylglucosamine (O-GlcNAc)	481:519	NF-M and NF-L are known to be modified by O-linked N-acetylglucosamine (O-GlcNAc) (Dong, D. L.-Y., Xu, Z.-S., Chevrier, M. R., Cotter, R. J., Cleveland, D. W., and Hart, G. W. (1993) J. Biol.
8702840	3	35	link	O-linked	481:488	arg1	O-GlcNAc					511:518	O-GlcNAc	511:518	O-GlcNAc	511:518	NF-M and NF-L are known to be modified by O-linked N-acetylglucosamine (O-GlcNAc) (Dong, D. L.-Y., Xu, Z.-S., Chevrier, M. R., Cotter, R. J., Cleveland, D. W., and Hart, G. W. (1993) J. Biol.
8702840	7	36	theme	NF-M	1099:1102	arg1	Ser48					1118:1122	Ser48	1118:1122	Ser48 of NF-L	1118:1130	Beyond the earlier identified sites on NF-M and NF-L, O-GlcNAc sites on Thr19 and Ser34 of NF-M and Ser34 and Ser48 of NF-L are also determined here, all of which are localized in head domain sequences critical for filament assembly.
8702840	7	36	theme	NF-M	1099:1102	arg1	Ser34					1090:1094	Ser34	1090:1094	Ser34	1090:1094	Beyond the earlier identified sites on NF-M and NF-L, O-GlcNAc sites on Thr19 and Ser34 of NF-M and Ser34 and Ser48 of NF-L are also determined here, all of which are localized in head domain sequences critical for filament assembly.
8702840	7	36	theme	NF-M	1099:1102	arg1	Thr19					1080:1084	Thr19	1080:1084	Thr19	1080:1084	Beyond the earlier identified sites on NF-M and NF-L, O-GlcNAc sites on Thr19 and Ser34 of NF-M and Ser34 and Ser48 of NF-L are also determined here, all of which are localized in head domain sequences critical for filament assembly.
8702840	2	37	theme	multiple	423:430	arg1	sites					432:436	multiple sites	423:436	multiple sites	423:436	Mammalian neurofilaments are obligate heteropolymers assembled from three polypeptides, neurofilament (NF)-H, NF-M, and NF-L, each of which undergoes phosphorylation at multiple sites.
8702840	8	38	theme	subunit	1332:1338	arg1	domains					1316:1322	both head and tail domains	1297:1322	both head and tail domains of each subunit	1297:1338	The proximity of O-GlcNAc and phosphorylation sites in both head and tail domains of each subunit indicates that these modifications may influence one another and play a role in filament assembly and network formation.
8702840	8	38	theme	subunit	1332:1338	arg1	subunit					1332:1338	each subunit	1327:1338	each subunit	1327:1338	The proximity of O-GlcNAc and phosphorylation sites in both head and tail domains of each subunit indicates that these modifications may influence one another and play a role in filament assembly and network formation.
8702840	0	39	theme	neurofilament-H	107:121	arg1	neurofilament-H					107:121	the neurofilament protein neurofilament-H	81:121	the neurofilament protein neurofilament-H	81:121	Cytoplasmic O-GlcNAc modification of the head domain and the KSP repeat motif of the neurofilament protein neurofilament-H.
8702840	0	39	theme	neurofilament-H	107:121	arg1	motif					72:76	the KSP repeat motif	57:76	the KSP repeat motif	57:76	Cytoplasmic O-GlcNAc modification of the head domain and the KSP repeat motif of the neurofilament protein neurofilament-H.
8702840	0	39	theme	neurofilament-H	107:121	arg1	domain					46:51	the head domain	37:51	the head domain	37:51	Cytoplasmic O-GlcNAc modification of the head domain and the KSP repeat motif of the neurofilament protein neurofilament-H.
8702840	6	40	theme	assembled	885:893	arg1	neurofilaments					895:908	assembled neurofilaments	885:908	assembled neurofilaments known to be nearly stoichiometrically phosphorylated on each of the approximately 50 KSP repeats	885:1005	Here we further report that NF-H is extensively modified by O-GlcNAc at Thr53, Ser54, and Ser56 in the head domain and, somewhat surprisingly, at multiple sites within the Lys-Ser-Pro repeat motif in the tail domain, a region in assembled neurofilaments known to be nearly stoichiometrically phosphorylated on each of the approximately 50 KSP repeats.
8702840	6	41	theme	tail	860:863	arg1	domain					865:870	the tail domain	856:870	the tail domain	856:870	Here we further report that NF-H is extensively modified by O-GlcNAc at Thr53, Ser54, and Ser56 in the head domain and, somewhat surprisingly, at multiple sites within the Lys-Ser-Pro repeat motif in the tail domain, a region in assembled neurofilaments known to be nearly stoichiometrically phosphorylated on each of the approximately 50 KSP repeats.
8702840	6	41	theme	tail	860:863	arg1	region					875:880	a region	873:880	a region in assembled neurofilaments known to be nearly stoichiometrically phosphorylated on each of the approximately 50 KSP repeats	873:1005	Here we further report that NF-H is extensively modified by O-GlcNAc at Thr53, Ser54, and Ser56 in the head domain and, somewhat surprisingly, at multiple sites within the Lys-Ser-Pro repeat motif in the tail domain, a region in assembled neurofilaments known to be nearly stoichiometrically phosphorylated on each of the approximately 50 KSP repeats.
8702840	0	42	theme	head	41:44	arg1	neurofilament-H					107:121	the neurofilament protein neurofilament-H	81:121	the neurofilament protein neurofilament-H	81:121	Cytoplasmic O-GlcNAc modification of the head domain and the KSP repeat motif of the neurofilament protein neurofilament-H.
8702840	0	42	theme	head	41:44	arg1	domain					46:51	the head domain	37:51	the head domain	37:51	Cytoplasmic O-GlcNAc modification of the head domain and the KSP repeat motif of the neurofilament protein neurofilament-H.
8702840	7	43	theme	critical	1210:1217	arg1	sequences					1200:1208	head domain sequences	1188:1208	head domain sequences critical for filament assembly	1188:1239	Beyond the earlier identified sites on NF-M and NF-L, O-GlcNAc sites on Thr19 and Ser34 of NF-M and Ser34 and Ser48 of NF-L are also determined here, all of which are localized in head domain sequences critical for filament assembly.
8702840	0	44	mod	modification	21:32	arg1	neurofilament-H					107:121	the neurofilament protein neurofilament-H	81:121	the neurofilament protein neurofilament-H	81:121	Cytoplasmic O-GlcNAc modification of the head domain and the KSP repeat motif of the neurofilament protein neurofilament-H.
8702840	0	44	mod	modification	21:32	arg3	O-GlcNAc					12:19	Cytoplasmic O-GlcNAc modification	0:32	Cytoplasmic O-GlcNAc modification of the head domain and the KSP repeat motif of the neurofilament protein neurofilament-H.	0:122	Cytoplasmic O-GlcNAc modification of the head domain and the KSP repeat motif of the neurofilament protein neurofilament-H.
8702840	0	44	mod	modification	21:32	arg1	domain					46:51	the head domain	37:51	the head domain	37:51	Cytoplasmic O-GlcNAc modification of the head domain and the KSP repeat motif of the neurofilament protein neurofilament-H.
8702840	0	44	mod	modification	21:32	arg1	motif					72:76	the KSP repeat motif	57:76	the KSP repeat motif	57:76	Cytoplasmic O-GlcNAc modification of the head domain and the KSP repeat motif of the neurofilament protein neurofilament-H.
8702840	6	45	theme	Lys-Ser-Pro	828:838	arg1	motif					847:851	the Lys-Ser-Pro repeat motif	824:851	the Lys-Ser-Pro repeat motif in the tail domain, a region in assembled neurofilaments known to be nearly stoichiometrically phosphorylated on each of the approximately 50 KSP repeats	824:1005	Here we further report that NF-H is extensively modified by O-GlcNAc at Thr53, Ser54, and Ser56 in the head domain and, somewhat surprisingly, at multiple sites within the Lys-Ser-Pro repeat motif in the tail domain, a region in assembled neurofilaments known to be nearly stoichiometrically phosphorylated on each of the approximately 50 KSP repeats.
8702840	3	46	mod	modified	469:476	arg1	NF-L					448:451	NF-L	448:451	NF-L	448:451	NF-M and NF-L are known to be modified by O-linked N-acetylglucosamine (O-GlcNAc) (Dong, D. L.-Y., Xu, Z.-S., Chevrier, M. R., Cotter, R. J., Cleveland, D. W., and Hart, G. W. (1993) J. Biol.
8702840	3	46	mod	modified	469:476	arg1	NF-M					439:442	NF-M	439:442	NF-M	439:442	NF-M and NF-L are known to be modified by O-linked N-acetylglucosamine (O-GlcNAc) (Dong, D. L.-Y., Xu, Z.-S., Chevrier, M. R., Cotter, R. J., Cleveland, D. W., and Hart, G. W. (1993) J. Biol.
8702840	3	46	mod	modified	469:476	arg3	O-GlcNAc					511:518	O-GlcNAc	511:518	O-GlcNAc	511:518	NF-M and NF-L are known to be modified by O-linked N-acetylglucosamine (O-GlcNAc) (Dong, D. L.-Y., Xu, Z.-S., Chevrier, M. R., Cotter, R. J., Cleveland, D. W., and Hart, G. W. (1993) J. Biol.
8702840	3	46	mod	modified	469:476	arg3	N-acetylglucosamine					490:508	O-linked N-acetylglucosamine	481:508	O-linked N-acetylglucosamine (O-GlcNAc)	481:519	NF-M and NF-L are known to be modified by O-linked N-acetylglucosamine (O-GlcNAc) (Dong, D. L.-Y., Xu, Z.-S., Chevrier, M. R., Cotter, R. J., Cleveland, D. W., and Hart, G. W. (1993) J. Biol.
8702840	7	47	theme	NF-L	1127:1130	arg1	Ser48					1118:1122	Ser48	1118:1122	Ser48 of NF-L	1118:1130	Beyond the earlier identified sites on NF-M and NF-L, O-GlcNAc sites on Thr19 and Ser34 of NF-M and Ser34 and Ser48 of NF-L are also determined here, all of which are localized in head domain sequences critical for filament assembly.
8702840	7	47	theme	NF-L	1127:1130	arg1	Ser34					1090:1094	Ser34	1090:1094	Ser34	1090:1094	Beyond the earlier identified sites on NF-M and NF-L, O-GlcNAc sites on Thr19 and Ser34 of NF-M and Ser34 and Ser48 of NF-L are also determined here, all of which are localized in head domain sequences critical for filament assembly.
8702840	7	47	theme	NF-L	1127:1130	arg1	Thr19					1080:1084	Thr19	1080:1084	Thr19	1080:1084	Beyond the earlier identified sites on NF-M and NF-L, O-GlcNAc sites on Thr19 and Ser34 of NF-M and Ser34 and Ser48 of NF-L are also determined here, all of which are localized in head domain sequences critical for filament assembly.
8702840	2	48	dep	polypeptides	328:339	arg1	NF-M					364:367	NF-M	364:367	NF-M	364:367	Mammalian neurofilaments are obligate heteropolymers assembled from three polypeptides, neurofilament (NF)-H, NF-M, and NF-L, each of which undergoes phosphorylation at multiple sites.
8702840	2	48	dep	polypeptides	328:339	arg1	NF-L					374:377	NF-L	374:377	NF-L	374:377	Mammalian neurofilaments are obligate heteropolymers assembled from three polypeptides, neurofilament (NF)-H, NF-M, and NF-L, each of which undergoes phosphorylation at multiple sites.
8702840	2	48	dep	polypeptides	328:339	arg1	-H					360:361	neurofilament (NF)-H	342:361	neurofilament (NF)-H	342:361	Mammalian neurofilaments are obligate heteropolymers assembled from three polypeptides, neurofilament (NF)-H, NF-M, and NF-L, each of which undergoes phosphorylation at multiple sites.
8702840	2	48	dep	polypeptides	328:339	arg1	polypeptides					328:339	three polypeptides, neurofilament (NF)-H, NF-M, and NF-L	322:377	polypeptides	328:339	Mammalian neurofilaments are obligate heteropolymers assembled from three polypeptides, neurofilament (NF)-H, NF-M, and NF-L, each of which undergoes phosphorylation at multiple sites.
8702840	0	49	theme	domain	46:51	arg1	modification					21:32	Cytoplasmic O-GlcNAc modification	0:32	Cytoplasmic O-GlcNAc modification of the head domain and the KSP repeat motif of the neurofilament protein neurofilament-H.	0:122	Cytoplasmic O-GlcNAc modification of the head domain and the KSP repeat motif of the neurofilament protein neurofilament-H.
8702840	6	50	theme	head	759:762	arg1	domain					764:769	the head domain	755:769	the head domain	755:769	Here we further report that NF-H is extensively modified by O-GlcNAc at Thr53, Ser54, and Ser56 in the head domain and, somewhat surprisingly, at multiple sites within the Lys-Ser-Pro repeat motif in the tail domain, a region in assembled neurofilaments known to be nearly stoichiometrically phosphorylated on each of the approximately 50 KSP repeats.
8702840	8	51	theme	phosphorylation	1272:1286	arg1	sites					1288:1292	O-GlcNAc and phosphorylation sites	1259:1292	sites	1288:1292	The proximity of O-GlcNAc and phosphorylation sites in both head and tail domains of each subunit indicates that these modifications may influence one another and play a role in filament assembly and network formation.
8702840	8	52	theme	filament	1420:1427	arg1	assembly					1429:1436	filament assembly	1420:1436	filament assembly	1420:1436	The proximity of O-GlcNAc and phosphorylation sites in both head and tail domains of each subunit indicates that these modifications may influence one another and play a role in filament assembly and network formation.
8702840	7	53	from	sites	1038:1042	arg1	NF-L					1056:1059	NF-L	1056:1059	NF-L	1056:1059	Beyond the earlier identified sites on NF-M and NF-L, O-GlcNAc sites on Thr19 and Ser34 of NF-M and Ser34 and Ser48 of NF-L are also determined here, all of which are localized in head domain sequences critical for filament assembly.
8702840	7	53	from	sites	1038:1042	arg1	NF-M					1047:1050	NF-M	1047:1050	NF-M	1047:1050	Beyond the earlier identified sites on NF-M and NF-L, O-GlcNAc sites on Thr19 and Ser34 of NF-M and Ser34 and Ser48 of NF-L are also determined here, all of which are localized in head domain sequences critical for filament assembly.
8702840	6	54	from	Ser54	735:739	arg1	domain					764:769	the head domain	755:769	the head domain	755:769	Here we further report that NF-H is extensively modified by O-GlcNAc at Thr53, Ser54, and Ser56 in the head domain and, somewhat surprisingly, at multiple sites within the Lys-Ser-Pro repeat motif in the tail domain, a region in assembled neurofilaments known to be nearly stoichiometrically phosphorylated on each of the approximately 50 KSP repeats.
8702840	6	55	theme	repeat	840:845	arg1	motif					847:851	the Lys-Ser-Pro repeat motif	824:851	the Lys-Ser-Pro repeat motif in the tail domain, a region in assembled neurofilaments known to be nearly stoichiometrically phosphorylated on each of the approximately 50 KSP repeats	824:1005	Here we further report that NF-H is extensively modified by O-GlcNAc at Thr53, Ser54, and Ser56 in the head domain and, somewhat surprisingly, at multiple sites within the Lys-Ser-Pro repeat motif in the tail domain, a region in assembled neurofilaments known to be nearly stoichiometrically phosphorylated on each of the approximately 50 KSP repeats.
8702840	2	56	theme	NF	357:358	arg1	polypeptides					328:339	three polypeptides, neurofilament (NF)-H, NF-M, and NF-L	322:377	polypeptides	328:339	Mammalian neurofilaments are obligate heteropolymers assembled from three polypeptides, neurofilament (NF)-H, NF-M, and NF-L, each of which undergoes phosphorylation at multiple sites.
8702840	2	56	theme	NF	357:358	arg1	-H					360:361	neurofilament (NF)-H	342:361	neurofilament (NF)-H	342:361	Mammalian neurofilaments are obligate heteropolymers assembled from three polypeptides, neurofilament (NF)-H, NF-M, and NF-L, each of which undergoes phosphorylation at multiple sites.
8702840	7	57	theme	domain	1193:1198	arg1	sequences					1200:1208	head domain sequences	1188:1208	head domain sequences critical for filament assembly	1188:1239	Beyond the earlier identified sites on NF-M and NF-L, O-GlcNAc sites on Thr19 and Ser34 of NF-M and Ser34 and Ser48 of NF-L are also determined here, all of which are localized in head domain sequences critical for filament assembly.
8702840	8	58	theme	O-GlcNAc	1259:1266	arg1	sites					1288:1292	O-GlcNAc and phosphorylation sites	1259:1292	sites	1288:1292	The proximity of O-GlcNAc and phosphorylation sites in both head and tail domains of each subunit indicates that these modifications may influence one another and play a role in filament assembly and network formation.
8702840	7	59	theme	O-GlcNAc	1062:1069	arg1	sites					1071:1075	O-GlcNAc sites	1062:1075	O-GlcNAc sites on Thr19 and Ser34 of NF-M and Ser34 and Ser48 of NF-L	1062:1130	Beyond the earlier identified sites on NF-M and NF-L, O-GlcNAc sites on Thr19 and Ser34 of NF-M and Ser34 and Ser48 of NF-L are also determined here, all of which are localized in head domain sequences critical for filament assembly.
8702840	1	60	theme	proper	231:236	arg1	caliber					245:251	proper axonal caliber	231:251	proper axonal caliber	231:251	Neurofilaments, the major intermediate filaments in large myelinated neurons, are essential for specifying proper axonal caliber.
8702840	0	61	theme	KSP	61:63	arg1	motif					72:76	the KSP repeat motif	57:76	the KSP repeat motif	57:76	Cytoplasmic O-GlcNAc modification of the head domain and the KSP repeat motif of the neurofilament protein neurofilament-H.
8702840	2	62	theme	Mammalian	254:262	arg1	neurofilaments					264:277	Mammalian neurofilaments	254:277	Mammalian neurofilaments	254:277	Mammalian neurofilaments are obligate heteropolymers assembled from three polypeptides, neurofilament (NF)-H, NF-M, and NF-L, each of which undergoes phosphorylation at multiple sites.
8702840	2	62	theme	Mammalian	254:262	arg1	heteropolymers					292:305	obligate heteropolymers	283:305	obligate heteropolymers assembled from three polypeptides, neurofilament (NF)-H, NF-M, and NF-L, each of which undergoes phosphorylation at multiple sites	283:436	Mammalian neurofilaments are obligate heteropolymers assembled from three polypeptides, neurofilament (NF)-H, NF-M, and NF-L, each of which undergoes phosphorylation at multiple sites.
8702840	1	63	theme	axonal	238:243	arg1	caliber					245:251	proper axonal caliber	231:251	proper axonal caliber	231:251	Neurofilaments, the major intermediate filaments in large myelinated neurons, are essential for specifying proper axonal caliber.
8702840	2	64	from	sites	432:436	arg1	phosphorylation					404:418	phosphorylation	404:418	phosphorylation at multiple sites	404:436	Mammalian neurofilaments are obligate heteropolymers assembled from three polypeptides, neurofilament (NF)-H, NF-M, and NF-L, each of which undergoes phosphorylation at multiple sites.
8702840	1	65	theme	major	144:148	arg1	Neurofilaments					124:137	Neurofilaments	124:137	Neurofilaments	124:137	Neurofilaments, the major intermediate filaments in large myelinated neurons, are essential for specifying proper axonal caliber.
8702840	1	65	theme	major	144:148	arg1	filaments					163:171	the major intermediate filaments	140:171	the major intermediate filaments in large myelinated neurons	140:199	Neurofilaments, the major intermediate filaments in large myelinated neurons, are essential for specifying proper axonal caliber.
8567640	10	0	theme	SGLT1	1214:1218	arg1	structure					1230:1238	SGLT1 secondary structure	1214:1238	SGLT1 secondary structure	1214:1238	The model of SGLT1 secondary structure and the predicted helix ends signify information prerequisite for the rational design of further experiments on structure/function relationships.
8567640	10	1	theme	further	1329:1335	arg1	experiments					1337:1347	further experiments	1329:1347	further experiments on structure/function relationships	1329:1383	The model of SGLT1 secondary structure and the predicted helix ends signify information prerequisite for the rational design of further experiments on structure/function relationships.
8567640	5	2	theme	charged	585:591	arg1	cytoplasmic					623:633	cytoplasmic	623:633	cytoplasmic	623:633	The N terminus resides extracellularly, and two hydrophobic regions form newly recognized membrane spans 4 and 12; the large charged domain near the C terminus is cytoplasmic.
8567640	5	2	theme	charged	585:591	arg1	domain					593:598	the large charged domain	575:598	the large charged domain near the C terminus	575:618	The N terminus resides extracellularly, and two hydrophobic regions form newly recognized membrane spans 4 and 12; the large charged domain near the C terminus is cytoplasmic.
8567640	1	3	theme	N-glycosylation	153:167	arg1	mutants					178:184	N-glycosylation scanning mutants	153:184	N-glycosylation scanning mutants	153:184	The membrane topology of the human Na+/glucose cotransporter SGLT1 has been probed using N-glycosylation scanning mutants and nested truncations.
8567640	3	4	theme	structure	372:380	arg1	suppositions					356:367	previously held suppositions	340:367	previously held suppositions of structure based primarily on hydropathy analysis	340:419	The resultant model diverges significantly from previously held suppositions of structure based primarily on hydropathy analysis.
8567640	1	5	theme	scanning	169:176	arg1	mutants					178:184	N-glycosylation scanning mutants	153:184	N-glycosylation scanning mutants	153:184	The membrane topology of the human Na+/glucose cotransporter SGLT1 has been probed using N-glycosylation scanning mutants and nested truncations.
8567640	8	6	theme	14th	969:972	arg1	helix					988:992	a 14th transmembrane helix	967:992	a 14th transmembrane helix	967:992	Several considerations suggest the hydrophobic C terminus forms a 14th transmembrane helix, differentiating the eukaryotic members of the SGLT1 family from bacterial homologues.
8567640	8	7	theme	transmembrane	974:986	arg1	helix					988:992	a 14th transmembrane helix	967:992	a 14th transmembrane helix	967:992	Several considerations suggest the hydrophobic C terminus forms a 14th transmembrane helix, differentiating the eukaryotic members of the SGLT1 family from bacterial homologues.
8567640	7	8	theme	thermo-dynamically-based	786:809	arg1	algorithms					811:820	thermo-dynamically-based algorithms	786:820	thermo-dynamically-based algorithms known to predict x-ray crystallographically determined transmembrane helix ends	786:900	Helix ends were predicted using thermo-dynamically-based algorithms known to predict x-ray crystallographically determined transmembrane helix ends.
8567640	9	9	theme	N	1189:1189	arg1	terminus					1191:1198	an extracellular N terminus	1172:1198	an extracellular N terminus	1172:1198	Our data inferentially indicate that these bacterial homologues incorporate 13 spans, with an extracellular N terminus.
8567640	10	10	theme	predicted	1248:1256	arg1	ends					1264:1267	the predicted helix ends	1244:1267	the predicted helix ends	1244:1267	The model of SGLT1 secondary structure and the predicted helix ends signify information prerequisite for the rational design of further experiments on structure/function relationships.
8567640	8	11	theme	bacterial	1059:1067	arg1	homologues					1069:1078	bacterial homologues	1059:1078	bacterial homologues	1059:1078	Several considerations suggest the hydrophobic C terminus forms a 14th transmembrane helix, differentiating the eukaryotic members of the SGLT1 family from bacterial homologues.
8567640	6	12	theme	helices	745:751	arg1	predictive					717:726	predictive	717:726	predictive	717:726	This model was evaluated further using two advanced empirically-based algorithms predictive of transmembrane helices.
8567640	9	13	dep	13	1157:1158	arg1	spans					1160:1164	spans	1160:1164	spans	1160:1164	Our data inferentially indicate that these bacterial homologues incorporate 13 spans, with an extracellular N terminus.
8567640	1	14	theme	membrane	68:75	arg1	topology					77:84	The membrane topology	64:84	The membrane topology of the human Na+/glucose cotransporter SGLT1	64:129	The membrane topology of the human Na+/glucose cotransporter SGLT1 has been probed using N-glycosylation scanning mutants and nested truncations.
8567640	3	15	theme	hydropathy	401:410	arg1	analysis					412:419	hydropathy analysis	401:419	hydropathy analysis	401:419	The resultant model diverges significantly from previously held suppositions of structure based primarily on hydropathy analysis.
8567640	8	16	theme	C	950:950	arg1	terminus					952:959	the hydrophobic C terminus	934:959	the hydrophobic C terminus	934:959	Several considerations suggest the hydrophobic C terminus forms a 14th transmembrane helix, differentiating the eukaryotic members of the SGLT1 family from bacterial homologues.
8567640	7	17	theme	x-ray	839:843	arg1	ends					897:900	x-ray crystallographically determined transmembrane helix ends	839:900	x-ray crystallographically determined transmembrane helix ends	839:900	Helix ends were predicted using thermo-dynamically-based algorithms known to predict x-ray crystallographically determined transmembrane helix ends.
8567640	8	18	theme	eukaryotic	1015:1024	arg1	members					1026:1032	the eukaryotic members	1011:1032	the eukaryotic members of the SGLT1 family	1011:1052	Several considerations suggest the hydrophobic C terminus forms a 14th transmembrane helix, differentiating the eukaryotic members of the SGLT1 family from bacterial homologues.
8567640	9	19	theme	bacterial	1124:1132	arg1	homologues					1134:1143	these bacterial homologues	1118:1143	these bacterial homologues	1118:1143	Our data inferentially indicate that these bacterial homologues incorporate 13 spans, with an extracellular N terminus.
8567640	10	20	theme	structure	1230:1238	arg1	model					1205:1209	The model	1201:1209	The model of SGLT1 secondary structure	1201:1238	The model of SGLT1 secondary structure and the predicted helix ends signify information prerequisite for the rational design of further experiments on structure/function relationships.
8567640	10	20	theme	structure	1230:1238	arg1	ends					1264:1267	the predicted helix ends	1244:1267	the predicted helix ends	1244:1267	The model of SGLT1 secondary structure and the predicted helix ends signify information prerequisite for the rational design of further experiments on structure/function relationships.
8567640	1	21	theme	nested	190:195	arg1	truncations					197:207	nested truncations	190:207	nested truncations	190:207	The membrane topology of the human Na+/glucose cotransporter SGLT1 has been probed using N-glycosylation scanning mutants and nested truncations.
8567640	0	22	theme	Membrane	0:7	arg1	topology					9:16	Membrane topology	0:16	Membrane topology of the human Na+/glucose cotransporter	0:55	Membrane topology of the human Na+/glucose cotransporter SGLT1.
8567640	10	23	theme	information	1277:1287	arg1	prerequisite					1289:1300	information prerequisite	1277:1300	information prerequisite for the rational design of further experiments on structure/function relationships	1277:1383	The model of SGLT1 secondary structure and the predicted helix ends signify information prerequisite for the rational design of further experiments on structure/function relationships.
8567640	9	24	theme	extracellular	1175:1187	arg1	terminus					1191:1198	an extracellular N terminus	1172:1198	an extracellular N terminus	1172:1198	Our data inferentially indicate that these bacterial homologues incorporate 13 spans, with an extracellular N terminus.
8567640	8	25	theme	SGLT1	1041:1045	arg1	family					1047:1052	the SGLT1 family	1037:1052	the SGLT1 family	1037:1052	Several considerations suggest the hydrophobic C terminus forms a 14th transmembrane helix, differentiating the eukaryotic members of the SGLT1 family from bacterial homologues.
8567640	1	26	theme	human	93:97	arg1	SGLT1					125:129	the human Na+/glucose cotransporter SGLT1	89:129	the human Na+/glucose cotransporter SGLT1	89:129	The membrane topology of the human Na+/glucose cotransporter SGLT1 has been probed using N-glycosylation scanning mutants and nested truncations.
8567640	8	27	theme	hydrophobic	938:948	arg1	terminus					952:959	the hydrophobic C terminus	934:959	the hydrophobic C terminus	934:959	Several considerations suggest the hydrophobic C terminus forms a 14th transmembrane helix, differentiating the eukaryotic members of the SGLT1 family from bacterial homologues.
8567640	10	28	from	design	1319:1324	arg1	relationships					1371:1383	structure/function relationships	1352:1383	structure/function relationships	1352:1383	The model of SGLT1 secondary structure and the predicted helix ends signify information prerequisite for the rational design of further experiments on structure/function relationships.
8567640	1	29	theme	Na+/glucose	99:109	arg1	SGLT1					125:129	the human Na+/glucose cotransporter SGLT1	89:129	the human Na+/glucose cotransporter SGLT1	89:129	The membrane topology of the human Na+/glucose cotransporter SGLT1 has been probed using N-glycosylation scanning mutants and nested truncations.
8567640	5	30	theme	recognized	539:548	arg1	membrane					550:557	newly recognized membrane	533:557	newly recognized membrane spans 4 and 12; the large charged domain near the C terminus is cytoplasmic	533:633	The N terminus resides extracellularly, and two hydrophobic regions form newly recognized membrane spans 4 and 12; the large charged domain near the C terminus is cytoplasmic.
8567640	0	31	theme	Na+/glucose	31:41	arg1	cotransporter					43:55	the human Na+/glucose cotransporter	21:55	the human Na+/glucose cotransporter	21:55	Membrane topology of the human Na+/glucose cotransporter SGLT1.
8567640	10	32	theme	helix	1258:1262	arg1	ends					1264:1267	the predicted helix ends	1244:1267	the predicted helix ends	1244:1267	The model of SGLT1 secondary structure and the predicted helix ends signify information prerequisite for the rational design of further experiments on structure/function relationships.
8567640	3	33	theme	resultant	296:304	arg1	model					306:310	The resultant model	292:310	The resultant model	292:310	The resultant model diverges significantly from previously held suppositions of structure based primarily on hydropathy analysis.
8567640	0	34	dep	SGLT1	57:61	arg1	topology					9:16	Membrane topology	0:16	Membrane topology of the human Na+/glucose cotransporter	0:55	Membrane topology of the human Na+/glucose cotransporter SGLT1.
8567640	6	35	theme	transmembrane	731:743	arg1	helices					745:751	transmembrane helices	731:751	transmembrane helices	731:751	This model was evaluated further using two advanced empirically-based algorithms predictive of transmembrane helices.
8567640	0	36	theme	human	25:29	arg1	cotransporter					43:55	the human Na+/glucose cotransporter	21:55	the human Na+/glucose cotransporter	21:55	Membrane topology of the human Na+/glucose cotransporter SGLT1.
8567640	10	37	theme	rational	1310:1317	arg1	design					1319:1324	the rational design	1306:1324	the rational design of further experiments on structure/function relationships	1306:1383	The model of SGLT1 secondary structure and the predicted helix ends signify information prerequisite for the rational design of further experiments on structure/function relationships.
8567640	8	38	theme	Several	903:909	arg1	considerations					911:924	Several considerations	903:924	Several considerations	903:924	Several considerations suggest the hydrophobic C terminus forms a 14th transmembrane helix, differentiating the eukaryotic members of the SGLT1 family from bacterial homologues.
8567640	3	39	theme	held	351:354	arg1	suppositions					356:367	previously held suppositions	340:367	previously held suppositions of structure based primarily on hydropathy analysis	340:419	The resultant model diverges significantly from previously held suppositions of structure based primarily on hydropathy analysis.
8567640	8	40	theme	family	1047:1052	arg1	members					1026:1032	the eukaryotic members	1011:1032	the eukaryotic members of the SGLT1 family	1011:1052	Several considerations suggest the hydrophobic C terminus forms a 14th transmembrane helix, differentiating the eukaryotic members of the SGLT1 family from bacterial homologues.
8567640	1	41	theme	cotransporter	111:123	arg1	SGLT1					125:129	the human Na+/glucose cotransporter SGLT1	89:129	the human Na+/glucose cotransporter SGLT1	89:129	The membrane topology of the human Na+/glucose cotransporter SGLT1 has been probed using N-glycosylation scanning mutants and nested truncations.
8567640	0	42	theme	cotransporter	43:55	arg1	topology					9:16	Membrane topology	0:16	Membrane topology of the human Na+/glucose cotransporter	0:55	Membrane topology of the human Na+/glucose cotransporter SGLT1.
8567640	7	43	theme	transmembrane	877:889	arg1	ends					897:900	x-ray crystallographically determined transmembrane helix ends	839:900	x-ray crystallographically determined transmembrane helix ends	839:900	Helix ends were predicted using thermo-dynamically-based algorithms known to predict x-ray crystallographically determined transmembrane helix ends.
8567640	10	44	from	experiments	1337:1347	arg1	relationships					1371:1383	structure/function relationships	1352:1383	structure/function relationships	1352:1383	The model of SGLT1 secondary structure and the predicted helix ends signify information prerequisite for the rational design of further experiments on structure/function relationships.
8567640	1	45	theme	SGLT1	125:129	arg1	topology					77:84	The membrane topology	64:84	The membrane topology of the human Na+/glucose cotransporter SGLT1	64:129	The membrane topology of the human Na+/glucose cotransporter SGLT1 has been probed using N-glycosylation scanning mutants and nested truncations.
8567640	4	46	dep	membrane	444:451	arg1	spans					453:457	spans	453:457	spans	453:457	SGLT1 incorporates 14 membrane spans.
8567640	7	47	theme	helix	891:895	arg1	ends					897:900	x-ray crystallographically determined transmembrane helix ends	839:900	x-ray crystallographically determined transmembrane helix ends	839:900	Helix ends were predicted using thermo-dynamically-based algorithms known to predict x-ray crystallographically determined transmembrane helix ends.
8567640	7	48	theme	Helix	754:758	arg1	ends					760:763	Helix ends	754:763	Helix ends	754:763	Helix ends were predicted using thermo-dynamically-based algorithms known to predict x-ray crystallographically determined transmembrane helix ends.
8567640	5	49	theme	C	609:609	arg1	terminus					611:618	the C terminus	605:618	the C terminus	605:618	The N terminus resides extracellularly, and two hydrophobic regions form newly recognized membrane spans 4 and 12; the large charged domain near the C terminus is cytoplasmic.
8567640	6	50	theme	predictive	717:726	arg1	algorithms					706:715	two advanced empirically-based algorithms	675:715	two advanced empirically-based algorithms predictive of transmembrane helices	675:751	This model was evaluated further using two advanced empirically-based algorithms predictive of transmembrane helices.
8567640	10	51	theme	experiments	1337:1347	arg1	design					1319:1324	the rational design	1306:1324	the rational design of further experiments on structure/function relationships	1306:1383	The model of SGLT1 secondary structure and the predicted helix ends signify information prerequisite for the rational design of further experiments on structure/function relationships.
8567640	5	52	dep	4	565:565	arg1	cytoplasmic					623:633	cytoplasmic	623:633	cytoplasmic	623:633	The N terminus resides extracellularly, and two hydrophobic regions form newly recognized membrane spans 4 and 12; the large charged domain near the C terminus is cytoplasmic.
8567640	5	52	dep	4	565:565	arg1	domain					593:598	the large charged domain	575:598	the large charged domain near the C terminus	575:618	The N terminus resides extracellularly, and two hydrophobic regions form newly recognized membrane spans 4 and 12; the large charged domain near the C terminus is cytoplasmic.
8567640	2	53	theme	Functional	210:219	arg1	analysis					221:228	Functional analysis	210:228	Functional analysis	210:228	Functional analysis proved essential for establishment of signal-anchor topology.
8567640	5	54	theme	hydrophobic	508:518	arg1	regions					520:526	two hydrophobic regions	504:526	two hydrophobic regions	504:526	The N terminus resides extracellularly, and two hydrophobic regions form newly recognized membrane spans 4 and 12; the large charged domain near the C terminus is cytoplasmic.
8567640	7	55	theme	determined	866:875	arg1	ends					897:900	x-ray crystallographically determined transmembrane helix ends	839:900	x-ray crystallographically determined transmembrane helix ends	839:900	Helix ends were predicted using thermo-dynamically-based algorithms known to predict x-ray crystallographically determined transmembrane helix ends.
8567640	10	56	from	relationships	1371:1383	arg1	design					1319:1324	the rational design	1306:1324	the rational design of further experiments on structure/function relationships	1306:1383	The model of SGLT1 secondary structure and the predicted helix ends signify information prerequisite for the rational design of further experiments on structure/function relationships.
8567640	2	57	theme	topology	282:289	arg1	establishment					251:263	establishment	251:263	establishment of signal-anchor topology	251:289	Functional analysis proved essential for establishment of signal-anchor topology.
8567640	5	58	dep	membrane	550:557	arg1	spans					559:563	spans	559:563	spans 4 and 12; the large charged domain near the C terminus is cytoplasmic	559:633	The N terminus resides extracellularly, and two hydrophobic regions form newly recognized membrane spans 4 and 12; the large charged domain near the C terminus is cytoplasmic.
8567640	6	59	theme	empirically-based	688:704	arg1	algorithms					706:715	two advanced empirically-based algorithms	675:715	two advanced empirically-based algorithms predictive of transmembrane helices	675:751	This model was evaluated further using two advanced empirically-based algorithms predictive of transmembrane helices.
8567640	10	60	theme	structure/function	1352:1369	arg1	relationships					1371:1383	structure/function relationships	1352:1383	structure/function relationships	1352:1383	The model of SGLT1 secondary structure and the predicted helix ends signify information prerequisite for the rational design of further experiments on structure/function relationships.
8567640	10	61	theme	secondary	1220:1228	arg1	structure					1230:1238	SGLT1 secondary structure	1214:1238	SGLT1 secondary structure	1214:1238	The model of SGLT1 secondary structure and the predicted helix ends signify information prerequisite for the rational design of further experiments on structure/function relationships.
8567640	2	62	theme	signal-anchor	268:280	arg1	topology					282:289	signal-anchor topology	268:289	signal-anchor topology	268:289	Functional analysis proved essential for establishment of signal-anchor topology.
8567640	5	63	theme	large	579:583	arg1	cytoplasmic					623:633	cytoplasmic	623:633	cytoplasmic	623:633	The N terminus resides extracellularly, and two hydrophobic regions form newly recognized membrane spans 4 and 12; the large charged domain near the C terminus is cytoplasmic.
8567640	5	63	theme	large	579:583	arg1	domain					593:598	the large charged domain	575:598	the large charged domain near the C terminus	575:618	The N terminus resides extracellularly, and two hydrophobic regions form newly recognized membrane spans 4 and 12; the large charged domain near the C terminus is cytoplasmic.
8567640	6	64	theme	advanced	679:686	arg1	algorithms					706:715	two advanced empirically-based algorithms	675:715	two advanced empirically-based algorithms predictive of transmembrane helices	675:751	This model was evaluated further using two advanced empirically-based algorithms predictive of transmembrane helices.
8567640	5	65	theme	N	464:464	arg1	terminus					466:473	The N terminus	460:473	The N terminus	460:473	The N terminus resides extracellularly, and two hydrophobic regions form newly recognized membrane spans 4 and 12; the large charged domain near the C terminus is cytoplasmic.
8631363	5	0	theme	two	821:823	arg1	structures					807:816	the structures	803:816	the structures of two of them	803:831	Three oligosaccharide-alditols were obtained, and the structures of two of them were identified by methylation analysis and exoglycosidase digestion.
8631363	4	1	theme	necrosis	541:548	arg1	factor-alpha					550:561	tumor necrosis factor-alpha	535:561	tumor necrosis factor-alpha	535:561	To prepare sugar chains, tumor necrosis factor-alpha was treated with alkaline borodeuteride and the oligosaccharide-alditols liberated were fractionated by gel-filtration chromatography on a Bio-Gel P-4 column, followed by normal-phase HPLC.
8631363	9	2	theme	0-glycosylation	1551:1565	arg1	Ser					1607:1609	Ser 4	1607:1611	Ser 4	1607:1611	An amino acid sequence analysis of the glycosylated peptides was performed after Staphylococcus aureus V8 protease digestion of tumor necrosis factor-alpha had been completed, and it was proved that the 0-glycosylation site of tumor necrosis factor-alpha was Ser 4.
8631363	9	2	theme	0-glycosylation	1551:1565	arg1	factor-alpha					1590:1601	tumor necrosis factor-alpha	1575:1601	tumor necrosis factor-alpha	1575:1601	An amino acid sequence analysis of the glycosylated peptides was performed after Staphylococcus aureus V8 protease digestion of tumor necrosis factor-alpha had been completed, and it was proved that the 0-glycosylation site of tumor necrosis factor-alpha was Ser 4.
8631363	9	2	theme	0-glycosylation	1551:1565	arg1	site					1567:1570	the 0-glycosylation site	1547:1570	the 0-glycosylation site of tumor necrosis factor-alpha	1547:1601	An amino acid sequence analysis of the glycosylated peptides was performed after Staphylococcus aureus V8 protease digestion of tumor necrosis factor-alpha had been completed, and it was proved that the 0-glycosylation site of tumor necrosis factor-alpha was Ser 4.
8631363	8	3	theme	sugar	1306:1310	arg1	composition					1312:1322	the sugar composition	1302:1322	the sugar composition	1302:1322	About 20% of tumor necrosis factor-alpha was found to be 0-glycosylated, based on the results of the sugar composition and structure analyses.
8631363	6	4	theme	Gal	957:959	arg1	alpha					976:980	NeuAc alpha 2-6	970:984	NeuAc alpha 2-6	970:984	The structures of these oligosaccharide-alditols were Gal beta 1-3(NeuAc alpha 2-6)GalNAcol and Gal beta 1-3GalNAcol (GalNAcol, N-acetylgalactosaminitol).
8631363	6	4	theme	Gal	957:959	arg1	beta					961:964	Gal beta 1-3	957:968	Gal beta 1-3(NeuAc alpha 2-6)GalNAcol	957:993	The structures of these oligosaccharide-alditols were Gal beta 1-3(NeuAc alpha 2-6)GalNAcol and Gal beta 1-3GalNAcol (GalNAcol, N-acetylgalactosaminitol).
8631363	3	5	theme	composition	351:361	arg1	analyses					363:370	Sugar composition analyses	345:370	Sugar composition analyses	345:370	Sugar composition analyses revealed that the tumor necrosis factor-alpha contained galactose, N-acetylgalactosamine and N-acetylneuraminic acid as sugar components.
8631363	4	6	theme	tumor	535:539	arg1	factor-alpha					550:561	tumor necrosis factor-alpha	535:561	tumor necrosis factor-alpha	535:561	To prepare sugar chains, tumor necrosis factor-alpha was treated with alkaline borodeuteride and the oligosaccharide-alditols liberated were fractionated by gel-filtration chromatography on a Bio-Gel P-4 column, followed by normal-phase HPLC.
8631363	1	7	theme	Tumor-necrosis	69:82	arg1	factor-alpha					84:95	Tumor-necrosis factor-alpha	69:95	Tumor-necrosis factor-alpha	69:95	Tumor-necrosis factor-alpha, produced by human B-cell lymphoblastoid cell line BALL-1, was expressed as four protein bands on SDS/PAGE analysis.
8631363	1	7	theme	Tumor-necrosis	69:82	arg1	bands					186:190	four protein bands	173:190	four protein bands	173:190	Tumor-necrosis factor-alpha, produced by human B-cell lymphoblastoid cell line BALL-1, was expressed as four protein bands on SDS/PAGE analysis.
8631363	9	8	theme	glycosylated	1387:1398	arg1	peptides					1400:1407	the glycosylated peptides	1383:1407	the glycosylated peptides	1383:1407	An amino acid sequence analysis of the glycosylated peptides was performed after Staphylococcus aureus V8 protease digestion of tumor necrosis factor-alpha had been completed, and it was proved that the 0-glycosylation site of tumor necrosis factor-alpha was Ser 4.
8631363	9	9	theme	peptides	1400:1407	arg1	analysis					1371:1378	An amino acid sequence analysis	1348:1378	An amino acid sequence analysis of the glycosylated peptides	1348:1407	An amino acid sequence analysis of the glycosylated peptides was performed after Staphylococcus aureus V8 protease digestion of tumor necrosis factor-alpha had been completed, and it was proved that the 0-glycosylation site of tumor necrosis factor-alpha was Ser 4.
8631363	9	10	theme	factor-alpha	1590:1601	arg1	Ser					1607:1609	Ser 4	1607:1611	Ser 4	1607:1611	An amino acid sequence analysis of the glycosylated peptides was performed after Staphylococcus aureus V8 protease digestion of tumor necrosis factor-alpha had been completed, and it was proved that the 0-glycosylation site of tumor necrosis factor-alpha was Ser 4.
8631363	9	10	theme	factor-alpha	1590:1601	arg1	factor-alpha					1590:1601	tumor necrosis factor-alpha	1575:1601	tumor necrosis factor-alpha	1575:1601	An amino acid sequence analysis of the glycosylated peptides was performed after Staphylococcus aureus V8 protease digestion of tumor necrosis factor-alpha had been completed, and it was proved that the 0-glycosylation site of tumor necrosis factor-alpha was Ser 4.
8631363	9	10	theme	factor-alpha	1590:1601	arg1	site					1567:1570	the 0-glycosylation site	1547:1570	the 0-glycosylation site of tumor necrosis factor-alpha	1547:1601	An amino acid sequence analysis of the glycosylated peptides was performed after Staphylococcus aureus V8 protease digestion of tumor necrosis factor-alpha had been completed, and it was proved that the 0-glycosylation site of tumor necrosis factor-alpha was Ser 4.
8631363	3	11	contain	contained	418:426	arg2	galactose					428:436	galactose	428:436	galactose	428:436	Sugar composition analyses revealed that the tumor necrosis factor-alpha contained galactose, N-acetylgalactosamine and N-acetylneuraminic acid as sugar components.
8631363	3	11	contain	contained	418:426	arg1	factor-alpha					405:416	the tumor necrosis factor-alpha	386:416	the tumor necrosis factor-alpha	386:416	Sugar composition analyses revealed that the tumor necrosis factor-alpha contained galactose, N-acetylgalactosamine and N-acetylneuraminic acid as sugar components.
8631363	3	11	contain	contained	418:426	arg2	acid					484:487	N-acetylneuraminic acid	465:487	N-acetylneuraminic acid	465:487	Sugar composition analyses revealed that the tumor necrosis factor-alpha contained galactose, N-acetylgalactosamine and N-acetylneuraminic acid as sugar components.
8631363	3	11	contain	contained	418:426	arg2	N-acetylgalactosamine					439:459	N-acetylgalactosamine	439:459	N-acetylgalactosamine	439:459	Sugar composition analyses revealed that the tumor necrosis factor-alpha contained galactose, N-acetylgalactosamine and N-acetylneuraminic acid as sugar components.
8631363	3	11	contain	contained	418:426	arg2	components					498:507	sugar components	492:507	sugar components	492:507	Sugar composition analyses revealed that the tumor necrosis factor-alpha contained galactose, N-acetylgalactosamine and N-acetylneuraminic acid as sugar components.
8631363	1	12	theme	protein	178:184	arg1	bands					186:190	four protein bands	173:190	four protein bands	173:190	Tumor-necrosis factor-alpha, produced by human B-cell lymphoblastoid cell line BALL-1, was expressed as four protein bands on SDS/PAGE analysis.
8631363	1	12	theme	protein	178:184	arg1	factor-alpha					84:95	Tumor-necrosis factor-alpha	69:95	Tumor-necrosis factor-alpha	69:95	Tumor-necrosis factor-alpha, produced by human B-cell lymphoblastoid cell line BALL-1, was expressed as four protein bands on SDS/PAGE analysis.
8631363	3	13	theme	Sugar	345:349	arg1	analyses					363:370	Sugar composition analyses	345:370	Sugar composition analyses	345:370	Sugar composition analyses revealed that the tumor necrosis factor-alpha contained galactose, N-acetylgalactosamine and N-acetylneuraminic acid as sugar components.
8631363	4	14	theme	sugar	521:525	arg1	chains					527:532	sugar chains	521:532	sugar chains	521:532	To prepare sugar chains, tumor necrosis factor-alpha was treated with alkaline borodeuteride and the oligosaccharide-alditols liberated were fractionated by gel-filtration chromatography on a Bio-Gel P-4 column, followed by normal-phase HPLC.
8631363	0	15	theme	tumor-necrosis	40:53	arg1	factor-alpha					55:66	natural human tumor-necrosis factor-alpha	26:66	natural human tumor-necrosis factor-alpha	26:66	O-glycosylated species of natural human tumor-necrosis factor-alpha.
8631363	0	16	theme	O-glycosylated	0:13	arg1	species					15:21	O-glycosylated species	0:21	O-glycosylated species of natural human tumor-necrosis factor-alpha.	0:67	O-glycosylated species of natural human tumor-necrosis factor-alpha.
8631363	3	17	theme	N-acetylneuraminic	465:482	arg1	galactose					428:436	galactose	428:436	galactose	428:436	Sugar composition analyses revealed that the tumor necrosis factor-alpha contained galactose, N-acetylgalactosamine and N-acetylneuraminic acid as sugar components.
8631363	3	17	theme	N-acetylneuraminic	465:482	arg1	N-acetylgalactosamine					439:459	N-acetylgalactosamine	439:459	N-acetylgalactosamine	439:459	Sugar composition analyses revealed that the tumor necrosis factor-alpha contained galactose, N-acetylgalactosamine and N-acetylneuraminic acid as sugar components.
8631363	3	17	theme	N-acetylneuraminic	465:482	arg1	acid					484:487	N-acetylneuraminic acid	465:487	N-acetylneuraminic acid	465:487	Sugar composition analyses revealed that the tumor necrosis factor-alpha contained galactose, N-acetylgalactosamine and N-acetylneuraminic acid as sugar components.
8631363	3	17	theme	N-acetylneuraminic	465:482	arg1	components					498:507	sugar components	492:507	sugar components	492:507	Sugar composition analyses revealed that the tumor necrosis factor-alpha contained galactose, N-acetylgalactosamine and N-acetylneuraminic acid as sugar components.
8631363	5	18	theme	exoglycosidase	877:890	arg1	digestion					892:900	exoglycosidase digestion	877:900	exoglycosidase digestion	877:900	Three oligosaccharide-alditols were obtained, and the structures of two of them were identified by methylation analysis and exoglycosidase digestion.
8631363	9	19	theme	sequence	1362:1369	arg1	analysis					1371:1378	An amino acid sequence analysis	1348:1378	An amino acid sequence analysis of the glycosylated peptides	1348:1407	An amino acid sequence analysis of the glycosylated peptides was performed after Staphylococcus aureus V8 protease digestion of tumor necrosis factor-alpha had been completed, and it was proved that the 0-glycosylation site of tumor necrosis factor-alpha was Ser 4.
8631363	7	20	theme	methylation	1183:1193	arg1	analyses					1195:1202	composition and methylation analyses	1167:1202	composition and methylation analyses	1167:1202	The structure of the remaining oligosaccharide-alditol was determined to be NeuAc alpha 2-3Gal1-3GalNAcol by composition and methylation analyses.
8631363	2	21	theme	bands	296:300	arg1	two					280:282	two	280:282	two	280:282	It may have been glycosylated, based on the fact that the heavier two of the four bands disappeared after neuraminidase treatment.
8631363	2	21	theme	bands	296:300	arg1	bands					296:300	the four bands	287:300	the four bands	287:300	It may have been glycosylated, based on the fact that the heavier two of the four bands disappeared after neuraminidase treatment.
8631363	4	22	theme	normal-phase	734:745	arg1	HPLC					747:750	normal-phase HPLC	734:750	normal-phase HPLC	734:750	To prepare sugar chains, tumor necrosis factor-alpha was treated with alkaline borodeuteride and the oligosaccharide-alditols liberated were fractionated by gel-filtration chromatography on a Bio-Gel P-4 column, followed by normal-phase HPLC.
8631363	3	23	theme	tumor	390:394	arg1	factor-alpha					405:416	the tumor necrosis factor-alpha	386:416	the tumor necrosis factor-alpha	386:416	Sugar composition analyses revealed that the tumor necrosis factor-alpha contained galactose, N-acetylgalactosamine and N-acetylneuraminic acid as sugar components.
8631363	9	24	theme	Staphylococcus	1429:1442	arg1	protease					1454:1461	Staphylococcus aureus V8 protease	1429:1461	Staphylococcus aureus V8 protease digestion of tumor necrosis factor-alpha had been completed	1429:1521	An amino acid sequence analysis of the glycosylated peptides was performed after Staphylococcus aureus V8 protease digestion of tumor necrosis factor-alpha had been completed, and it was proved that the 0-glycosylation site of tumor necrosis factor-alpha was Ser 4.
8631363	8	25	theme	structure	1328:1336	arg1	analyses					1338:1345	structure analyses	1328:1345	structure analyses	1328:1345	About 20% of tumor necrosis factor-alpha was found to be 0-glycosylated, based on the results of the sugar composition and structure analyses.
8631363	1	26	theme	human	110:114	arg1	line					143:146	human B-cell lymphoblastoid cell line BALL-1	110:153	human B-cell lymphoblastoid cell line BALL-1	110:153	Tumor-necrosis factor-alpha, produced by human B-cell lymphoblastoid cell line BALL-1, was expressed as four protein bands on SDS/PAGE analysis.
8631363	1	27	theme	SDS/PAGE	195:202	arg1	analysis					204:211	SDS/PAGE analysis	195:211	SDS/PAGE analysis	195:211	Tumor-necrosis factor-alpha, produced by human B-cell lymphoblastoid cell line BALL-1, was expressed as four protein bands on SDS/PAGE analysis.
8631363	0	28	theme	natural	26:32	arg1	factor-alpha					55:66	natural human tumor-necrosis factor-alpha	26:66	natural human tumor-necrosis factor-alpha	26:66	O-glycosylated species of natural human tumor-necrosis factor-alpha.
8631363	4	29	theme	alkaline	580:587	arg1	borodeuteride					589:601	alkaline borodeuteride	580:601	alkaline borodeuteride	580:601	To prepare sugar chains, tumor necrosis factor-alpha was treated with alkaline borodeuteride and the oligosaccharide-alditols liberated were fractionated by gel-filtration chromatography on a Bio-Gel P-4 column, followed by normal-phase HPLC.
8631363	7	30	theme	composition	1167:1177	arg1	analyses					1195:1202	composition and methylation analyses	1167:1202	composition and methylation analyses	1167:1202	The structure of the remaining oligosaccharide-alditol was determined to be NeuAc alpha 2-3Gal1-3GalNAcol by composition and methylation analyses.
8631363	1	31	theme	B-cell	116:121	arg1	line					143:146	human B-cell lymphoblastoid cell line BALL-1	110:153	human B-cell lymphoblastoid cell line BALL-1	110:153	Tumor-necrosis factor-alpha, produced by human B-cell lymphoblastoid cell line BALL-1, was expressed as four protein bands on SDS/PAGE analysis.
8631363	9	32	theme	necrosis	1482:1489	arg1	factor-alpha					1491:1502	tumor necrosis factor-alpha	1476:1502	tumor necrosis factor-alpha had been completed	1476:1521	An amino acid sequence analysis of the glycosylated peptides was performed after Staphylococcus aureus V8 protease digestion of tumor necrosis factor-alpha had been completed, and it was proved that the 0-glycosylation site of tumor necrosis factor-alpha was Ser 4.
8631363	3	33	theme	sugar	492:496	arg1	galactose					428:436	galactose	428:436	galactose	428:436	Sugar composition analyses revealed that the tumor necrosis factor-alpha contained galactose, N-acetylgalactosamine and N-acetylneuraminic acid as sugar components.
8631363	3	33	theme	sugar	492:496	arg1	N-acetylgalactosamine					439:459	N-acetylgalactosamine	439:459	N-acetylgalactosamine	439:459	Sugar composition analyses revealed that the tumor necrosis factor-alpha contained galactose, N-acetylgalactosamine and N-acetylneuraminic acid as sugar components.
8631363	3	33	theme	sugar	492:496	arg1	acid					484:487	N-acetylneuraminic acid	465:487	N-acetylneuraminic acid	465:487	Sugar composition analyses revealed that the tumor necrosis factor-alpha contained galactose, N-acetylgalactosamine and N-acetylneuraminic acid as sugar components.
8631363	3	33	theme	sugar	492:496	arg1	components					498:507	sugar components	492:507	sugar components	492:507	Sugar composition analyses revealed that the tumor necrosis factor-alpha contained galactose, N-acetylgalactosamine and N-acetylneuraminic acid as sugar components.
8631363	9	34	theme	V8	1451:1452	arg1	protease					1454:1461	Staphylococcus aureus V8 protease	1429:1461	Staphylococcus aureus V8 protease digestion of tumor necrosis factor-alpha had been completed	1429:1521	An amino acid sequence analysis of the glycosylated peptides was performed after Staphylococcus aureus V8 protease digestion of tumor necrosis factor-alpha had been completed, and it was proved that the 0-glycosylation site of tumor necrosis factor-alpha was Ser 4.
8631363	6	35	dep	1-3GalNAcol	1008:1018	arg1	N-acetylgalactosaminitol					1031:1054	N-acetylgalactosaminitol	1031:1054	N-acetylgalactosaminitol	1031:1054	The structures of these oligosaccharide-alditols were Gal beta 1-3(NeuAc alpha 2-6)GalNAcol and Gal beta 1-3GalNAcol (GalNAcol, N-acetylgalactosaminitol).
8631363	6	35	dep	1-3GalNAcol	1008:1018	arg1	GalNAcol					1021:1028	GalNAcol	1021:1028	GalNAcol	1021:1028	The structures of these oligosaccharide-alditols were Gal beta 1-3(NeuAc alpha 2-6)GalNAcol and Gal beta 1-3GalNAcol (GalNAcol, N-acetylgalactosaminitol).
8631363	1	36	theme	lymphoblastoid	123:136	arg1	line					143:146	human B-cell lymphoblastoid cell line BALL-1	110:153	human B-cell lymphoblastoid cell line BALL-1	110:153	Tumor-necrosis factor-alpha, produced by human B-cell lymphoblastoid cell line BALL-1, was expressed as four protein bands on SDS/PAGE analysis.
8631363	2	37	gly	glycosylated	231:242	arg1	It					214:215	It	214:215	It	214:215	It may have been glycosylated, based on the fact that the heavier two of the four bands disappeared after neuraminidase treatment.
8631363	9	38	theme	protease	1454:1461	arg1	digestion					1463:1471	Staphylococcus aureus V8 protease digestion	1429:1471	Staphylococcus aureus V8 protease digestion of tumor necrosis factor-alpha had been completed	1429:1521	An amino acid sequence analysis of the glycosylated peptides was performed after Staphylococcus aureus V8 protease digestion of tumor necrosis factor-alpha had been completed, and it was proved that the 0-glycosylation site of tumor necrosis factor-alpha was Ser 4.
8631363	6	39	theme	beta	961:964	arg1	GalNAcol					986:993	Gal beta 1-3(NeuAc alpha 2-6)GalNAcol	957:993	Gal beta 1-3(NeuAc alpha 2-6)GalNAcol	957:993	The structures of these oligosaccharide-alditols were Gal beta 1-3(NeuAc alpha 2-6)GalNAcol and Gal beta 1-3GalNAcol (GalNAcol, N-acetylgalactosaminitol).
8631363	6	39	theme	beta	961:964	arg1	structures					907:916	The structures	903:916	The structures of these oligosaccharide-alditols	903:950	The structures of these oligosaccharide-alditols were Gal beta 1-3(NeuAc alpha 2-6)GalNAcol and Gal beta 1-3GalNAcol (GalNAcol, N-acetylgalactosaminitol).
8631363	0	40	gly	O-glycosylated	0:13	arg1	species					15:21	O-glycosylated species	0:21	O-glycosylated species of natural human tumor-necrosis factor-alpha.	0:67	O-glycosylated species of natural human tumor-necrosis factor-alpha.
8631363	8	41	theme	analyses	1338:1345	arg1	results					1291:1297	the results	1287:1297	the results of the sugar composition and structure analyses	1287:1345	About 20% of tumor necrosis factor-alpha was found to be 0-glycosylated, based on the results of the sugar composition and structure analyses.
8631363	9	42	theme	tumor	1575:1579	arg1	factor-alpha					1590:1601	tumor necrosis factor-alpha	1575:1601	tumor necrosis factor-alpha	1575:1601	An amino acid sequence analysis of the glycosylated peptides was performed after Staphylococcus aureus V8 protease digestion of tumor necrosis factor-alpha had been completed, and it was proved that the 0-glycosylation site of tumor necrosis factor-alpha was Ser 4.
8631363	0	43	theme	human	34:38	arg1	factor-alpha					55:66	natural human tumor-necrosis factor-alpha	26:66	natural human tumor-necrosis factor-alpha	26:66	O-glycosylated species of natural human tumor-necrosis factor-alpha.
8631363	5	44	theme	methylation	852:862	arg1	analysis					864:871	methylation analysis	852:871	methylation analysis	852:871	Three oligosaccharide-alditols were obtained, and the structures of two of them were identified by methylation analysis and exoglycosidase digestion.
8631363	4	45	dep	liberated	636:644	arg1	fractionated					651:662	fractionated	651:662	liberated were fractionated by gel-filtration chromatography on a Bio-Gel P-4 column, followed by normal-phase HPLC	636:750	To prepare sugar chains, tumor necrosis factor-alpha was treated with alkaline borodeuteride and the oligosaccharide-alditols liberated were fractionated by gel-filtration chromatography on a Bio-Gel P-4 column, followed by normal-phase HPLC.
8631363	9	46	theme	aureus	1444:1449	arg1	protease					1454:1461	Staphylococcus aureus V8 protease	1429:1461	Staphylococcus aureus V8 protease digestion of tumor necrosis factor-alpha had been completed	1429:1521	An amino acid sequence analysis of the glycosylated peptides was performed after Staphylococcus aureus V8 protease digestion of tumor necrosis factor-alpha had been completed, and it was proved that the 0-glycosylation site of tumor necrosis factor-alpha was Ser 4.
8631363	4	47	theme	P-4	710:712	arg1	column					714:719	a Bio-Gel P-4 column	700:719	a Bio-Gel P-4 column	700:719	To prepare sugar chains, tumor necrosis factor-alpha was treated with alkaline borodeuteride and the oligosaccharide-alditols liberated were fractionated by gel-filtration chromatography on a Bio-Gel P-4 column, followed by normal-phase HPLC.
8631363	3	48	theme	necrosis	396:403	arg1	factor-alpha					405:416	the tumor necrosis factor-alpha	386:416	the tumor necrosis factor-alpha	386:416	Sugar composition analyses revealed that the tumor necrosis factor-alpha contained galactose, N-acetylgalactosamine and N-acetylneuraminic acid as sugar components.
8631363	7	49	theme	NeuAc	1134:1138	arg1	structure					1062:1070	The structure	1058:1070	The structure of the remaining oligosaccharide-alditol	1058:1111	The structure of the remaining oligosaccharide-alditol was determined to be NeuAc alpha 2-3Gal1-3GalNAcol by composition and methylation analyses.
8631363	7	49	theme	NeuAc	1134:1138	arg1	2-3Gal1-3GalNAcol					1146:1162	NeuAc alpha 2-3Gal1-3GalNAcol	1134:1162	NeuAc alpha 2-3Gal1-3GalNAcol	1134:1162	The structure of the remaining oligosaccharide-alditol was determined to be NeuAc alpha 2-3Gal1-3GalNAcol by composition and methylation analyses.
8631363	8	50	theme	necrosis	1224:1231	arg1	factor-alpha					1233:1244	tumor necrosis factor-alpha	1218:1244	tumor necrosis factor-alpha	1218:1244	About 20% of tumor necrosis factor-alpha was found to be 0-glycosylated, based on the results of the sugar composition and structure analyses.
8631363	6	51	theme	NeuAc	970:974	arg1	alpha					976:980	NeuAc alpha 2-6	970:984	NeuAc alpha 2-6	970:984	The structures of these oligosaccharide-alditols were Gal beta 1-3(NeuAc alpha 2-6)GalNAcol and Gal beta 1-3GalNAcol (GalNAcol, N-acetylgalactosaminitol).
8631363	6	51	theme	NeuAc	970:974	arg1	beta					961:964	Gal beta 1-3	957:968	Gal beta 1-3(NeuAc alpha 2-6)GalNAcol	957:993	The structures of these oligosaccharide-alditols were Gal beta 1-3(NeuAc alpha 2-6)GalNAcol and Gal beta 1-3GalNAcol (GalNAcol, N-acetylgalactosaminitol).
8631363	1	52	theme	cell	138:141	arg1	line					143:146	human B-cell lymphoblastoid cell line BALL-1	110:153	human B-cell lymphoblastoid cell line BALL-1	110:153	Tumor-necrosis factor-alpha, produced by human B-cell lymphoblastoid cell line BALL-1, was expressed as four protein bands on SDS/PAGE analysis.
8631363	0	53	theme	factor-alpha	55:66	arg1	species					15:21	O-glycosylated species	0:21	O-glycosylated species of natural human tumor-necrosis factor-alpha.	0:67	O-glycosylated species of natural human tumor-necrosis factor-alpha.
8631363	9	54	theme	tumor	1476:1480	arg1	factor-alpha					1491:1502	tumor necrosis factor-alpha	1476:1502	tumor necrosis factor-alpha had been completed	1476:1521	An amino acid sequence analysis of the glycosylated peptides was performed after Staphylococcus aureus V8 protease digestion of tumor necrosis factor-alpha had been completed, and it was proved that the 0-glycosylation site of tumor necrosis factor-alpha was Ser 4.
8631363	7	55	theme	alpha	1140:1144	arg1	structure					1062:1070	The structure	1058:1070	The structure of the remaining oligosaccharide-alditol	1058:1111	The structure of the remaining oligosaccharide-alditol was determined to be NeuAc alpha 2-3Gal1-3GalNAcol by composition and methylation analyses.
8631363	7	55	theme	alpha	1140:1144	arg1	2-3Gal1-3GalNAcol					1146:1162	NeuAc alpha 2-3Gal1-3GalNAcol	1134:1162	NeuAc alpha 2-3Gal1-3GalNAcol	1134:1162	The structure of the remaining oligosaccharide-alditol was determined to be NeuAc alpha 2-3Gal1-3GalNAcol by composition and methylation analyses.
8631363	6	56	theme	oligosaccharide-alditols	927:950	arg1	GalNAcol					986:993	Gal beta 1-3(NeuAc alpha 2-6)GalNAcol	957:993	Gal beta 1-3(NeuAc alpha 2-6)GalNAcol	957:993	The structures of these oligosaccharide-alditols were Gal beta 1-3(NeuAc alpha 2-6)GalNAcol and Gal beta 1-3GalNAcol (GalNAcol, N-acetylgalactosaminitol).
8631363	6	56	theme	oligosaccharide-alditols	927:950	arg1	structures					907:916	The structures	903:916	The structures of these oligosaccharide-alditols	903:950	The structures of these oligosaccharide-alditols were Gal beta 1-3(NeuAc alpha 2-6)GalNAcol and Gal beta 1-3GalNAcol (GalNAcol, N-acetylgalactosaminitol).
8631363	9	57	theme	amino	1351:1355	arg1	analysis					1371:1378	An amino acid sequence analysis	1348:1378	An amino acid sequence analysis of the glycosylated peptides	1348:1407	An amino acid sequence analysis of the glycosylated peptides was performed after Staphylococcus aureus V8 protease digestion of tumor necrosis factor-alpha had been completed, and it was proved that the 0-glycosylation site of tumor necrosis factor-alpha was Ser 4.
8631363	7	58	theme	remaining	1079:1087	arg1	oligosaccharide-alditol					1089:1111	the remaining oligosaccharide-alditol	1075:1111	the remaining oligosaccharide-alditol	1075:1111	The structure of the remaining oligosaccharide-alditol was determined to be NeuAc alpha 2-3Gal1-3GalNAcol by composition and methylation analyses.
8631363	2	59	theme	neuraminidase	320:332	arg1	treatment					334:342	neuraminidase treatment	320:342	neuraminidase treatment	320:342	It may have been glycosylated, based on the fact that the heavier two of the four bands disappeared after neuraminidase treatment.
8631363	6	60	theme	beta	1003:1006	arg1	1-3GalNAcol					1008:1018	Gal beta 1-3GalNAcol	999:1018	Gal beta 1-3GalNAcol (GalNAcol, N-acetylgalactosaminitol)	999:1055	The structures of these oligosaccharide-alditols were Gal beta 1-3(NeuAc alpha 2-6)GalNAcol and Gal beta 1-3GalNAcol (GalNAcol, N-acetylgalactosaminitol).
8631363	8	61	theme	tumor	1218:1222	arg1	factor-alpha					1233:1244	tumor necrosis factor-alpha	1218:1244	tumor necrosis factor-alpha	1218:1244	About 20% of tumor necrosis factor-alpha was found to be 0-glycosylated, based on the results of the sugar composition and structure analyses.
8631363	9	62	gly	0-glycosylation	1551:1565	arg2	factor-alpha					1590:1601	tumor necrosis factor-alpha	1575:1601	tumor necrosis factor-alpha	1575:1601	An amino acid sequence analysis of the glycosylated peptides was performed after Staphylococcus aureus V8 protease digestion of tumor necrosis factor-alpha had been completed, and it was proved that the 0-glycosylation site of tumor necrosis factor-alpha was Ser 4.
8631363	9	62	gly	0-glycosylation	1551:1565	arg1	factor-alpha					1590:1601	tumor necrosis factor-alpha	1575:1601	tumor necrosis factor-alpha	1575:1601	An amino acid sequence analysis of the glycosylated peptides was performed after Staphylococcus aureus V8 protease digestion of tumor necrosis factor-alpha had been completed, and it was proved that the 0-glycosylation site of tumor necrosis factor-alpha was Ser 4.
8631363	9	62	gly	0-glycosylation	1551:1565	arg2	site					1567:1570	the 0-glycosylation site	1547:1570	the 0-glycosylation site of tumor necrosis factor-alpha	1547:1601	An amino acid sequence analysis of the glycosylated peptides was performed after Staphylococcus aureus V8 protease digestion of tumor necrosis factor-alpha had been completed, and it was proved that the 0-glycosylation site of tumor necrosis factor-alpha was Ser 4.
8631363	9	62	gly	0-glycosylation	1551:1565	arg2	Ser					1607:1609	Ser 4	1607:1611	Ser 4	1607:1611	An amino acid sequence analysis of the glycosylated peptides was performed after Staphylococcus aureus V8 protease digestion of tumor necrosis factor-alpha had been completed, and it was proved that the 0-glycosylation site of tumor necrosis factor-alpha was Ser 4.
8631363	7	63	theme	oligosaccharide-alditol	1089:1111	arg1	structure					1062:1070	The structure	1058:1070	The structure of the remaining oligosaccharide-alditol	1058:1111	The structure of the remaining oligosaccharide-alditol was determined to be NeuAc alpha 2-3Gal1-3GalNAcol by composition and methylation analyses.
8631363	7	63	theme	oligosaccharide-alditol	1089:1111	arg1	2-3Gal1-3GalNAcol					1146:1162	NeuAc alpha 2-3Gal1-3GalNAcol	1134:1162	NeuAc alpha 2-3Gal1-3GalNAcol	1134:1162	The structure of the remaining oligosaccharide-alditol was determined to be NeuAc alpha 2-3Gal1-3GalNAcol by composition and methylation analyses.
8631363	9	64	gly	glycosylated	1387:1398	arg1	peptides					1400:1407	the glycosylated peptides	1383:1407	the glycosylated peptides	1383:1407	An amino acid sequence analysis of the glycosylated peptides was performed after Staphylococcus aureus V8 protease digestion of tumor necrosis factor-alpha had been completed, and it was proved that the 0-glycosylation site of tumor necrosis factor-alpha was Ser 4.
8631363	4	65	theme	gel-filtration	667:680	arg1	chromatography					682:695	gel-filtration chromatography	667:695	gel-filtration chromatography	667:695	To prepare sugar chains, tumor necrosis factor-alpha was treated with alkaline borodeuteride and the oligosaccharide-alditols liberated were fractionated by gel-filtration chromatography on a Bio-Gel P-4 column, followed by normal-phase HPLC.
8631363	9	66	theme	acid	1357:1360	arg1	analysis					1371:1378	An amino acid sequence analysis	1348:1378	An amino acid sequence analysis of the glycosylated peptides	1348:1407	An amino acid sequence analysis of the glycosylated peptides was performed after Staphylococcus aureus V8 protease digestion of tumor necrosis factor-alpha had been completed, and it was proved that the 0-glycosylation site of tumor necrosis factor-alpha was Ser 4.
8631363	8	67	theme	composition	1312:1322	arg1	results					1291:1297	the results	1287:1297	the results of the sugar composition and structure analyses	1287:1345	About 20% of tumor necrosis factor-alpha was found to be 0-glycosylated, based on the results of the sugar composition and structure analyses.
8631363	8	68	theme	factor-alpha	1233:1244	arg1	%					1213:1213	About 20%	1205:1213	About 20% of tumor necrosis factor-alpha	1205:1244	About 20% of tumor necrosis factor-alpha was found to be 0-glycosylated, based on the results of the sugar composition and structure analyses.
8631363	8	68	theme	factor-alpha	1233:1244	arg1	factor-alpha					1233:1244	tumor necrosis factor-alpha	1218:1244	tumor necrosis factor-alpha	1218:1244	About 20% of tumor necrosis factor-alpha was found to be 0-glycosylated, based on the results of the sugar composition and structure analyses.
8631363	9	69	theme	necrosis	1581:1588	arg1	factor-alpha					1590:1601	tumor necrosis factor-alpha	1575:1601	tumor necrosis factor-alpha	1575:1601	An amino acid sequence analysis of the glycosylated peptides was performed after Staphylococcus aureus V8 protease digestion of tumor necrosis factor-alpha had been completed, and it was proved that the 0-glycosylation site of tumor necrosis factor-alpha was Ser 4.
8631363	4	70	theme	Bio-Gel	702:708	arg1	column					714:719	a Bio-Gel P-4 column	700:719	a Bio-Gel P-4 column	700:719	To prepare sugar chains, tumor necrosis factor-alpha was treated with alkaline borodeuteride and the oligosaccharide-alditols liberated were fractionated by gel-filtration chromatography on a Bio-Gel P-4 column, followed by normal-phase HPLC.
8631363	5	71	theme	them	828:831	arg1	them					828:831	them	828:831	them	828:831	Three oligosaccharide-alditols were obtained, and the structures of two of them were identified by methylation analysis and exoglycosidase digestion.
8631363	5	71	theme	them	828:831	arg1	two					821:823	two	821:823	two	821:823	Three oligosaccharide-alditols were obtained, and the structures of two of them were identified by methylation analysis and exoglycosidase digestion.
8631363	6	72	theme	Gal	999:1001	arg1	1-3GalNAcol					1008:1018	Gal beta 1-3GalNAcol	999:1018	Gal beta 1-3GalNAcol (GalNAcol, N-acetylgalactosaminitol)	999:1055	The structures of these oligosaccharide-alditols were Gal beta 1-3(NeuAc alpha 2-6)GalNAcol and Gal beta 1-3GalNAcol (GalNAcol, N-acetylgalactosaminitol).
8631363	8	73	gly	0-glycosylated	1262:1275	arg1	%					1213:1213	About 20%	1205:1213	About 20% of tumor necrosis factor-alpha	1205:1244	About 20% of tumor necrosis factor-alpha was found to be 0-glycosylated, based on the results of the sugar composition and structure analyses.
8631363	8	73	gly	0-glycosylated	1262:1275	arg1	factor-alpha					1233:1244	tumor necrosis factor-alpha	1218:1244	tumor necrosis factor-alpha	1218:1244	About 20% of tumor necrosis factor-alpha was found to be 0-glycosylated, based on the results of the sugar composition and structure analyses.
8631363	9	74	theme	factor-alpha	1491:1502	arg1	digestion					1463:1471	Staphylococcus aureus V8 protease digestion	1429:1471	Staphylococcus aureus V8 protease digestion of tumor necrosis factor-alpha had been completed	1429:1521	An amino acid sequence analysis of the glycosylated peptides was performed after Staphylococcus aureus V8 protease digestion of tumor necrosis factor-alpha had been completed, and it was proved that the 0-glycosylation site of tumor necrosis factor-alpha was Ser 4.
9450956	0	0	theme	sequence	71:78	arg1	Trp-x-x-Trp					80:90	sequence Trp-x-x-Trp	71:90	sequence Trp-x-x-Trp	71:90	Recognition signal for C-mannosylation of Trp-7 in RNase 2 consists of sequence Trp-x-x-Trp.
9450956	8	1	theme	tertiary	1074:1081	arg1	structure					1084:1092	the primary, rather than the tertiary, structure	1045:1092	the primary, rather than the tertiary, structure	1045:1092	Interpretation of the data in the context of the three-dimensional structure of RNase 2 strongly suggests that the primary, rather than the tertiary, structure forms the determinant.
9450956	7	2	theme	reaction	914:921	arg1	efficiency					896:905	the efficiency	892:905	the efficiency of the reaction	892:921	The Trp residue at position +3 can be replaced by Phe, which reduces the efficiency of the reaction threefold.
9450956	9	3	theme	present	1179:1185	arg1	proteins					1160:1167	336 mammalian proteins	1146:1167	336 mammalian proteins currently present in protein databases	1146:1206	The sequence motif occurs in 336 mammalian proteins currently present in protein databases.
9450956	5	4	theme	deletion	589:596	arg1	mutants					598:604	deletion mutants	589:604	deletion mutants	589:604	Expression of chimeras of RNase 2 and nonglycosylated RNase 4 and deletion mutants in HEK293 cells identified residues 1-13 to be sufficient for C-mannosylation.
9450956	5	5	theme	chimeras	537:544	arg1	Expression					523:532	Expression	523:532	Expression of chimeras of RNase 2 and nonglycosylated RNase 4 and deletion mutants in HEK293 cells	523:620	Expression of chimeras of RNase 2 and nonglycosylated RNase 4 and deletion mutants in HEK293 cells identified residues 1-13 to be sufficient for C-mannosylation.
9450956	8	6	from	Interpretation	934:947	arg1	context					968:974	the context	964:974	the context of the three-dimensional structure of RNase 2	964:1020	Interpretation of the data in the context of the three-dimensional structure of RNase 2 strongly suggests that the primary, rather than the tertiary, structure forms the determinant.
9450956	7	7	theme	Trp	827:829	arg1	residue					831:837	The Trp residue	823:837	The Trp residue at position +3	823:852	The Trp residue at position +3 can be replaced by Phe, which reduces the efficiency of the reaction threefold.
9450956	4	8	theme	reaction	513:520	arg1	specificity					494:504	the specificity	490:504	the specificity of the reaction	490:520	In this article, we address which structural features provide the specificity of the reaction.
9450956	5	9	theme	mutants	598:604	arg1	Expression					523:532	Expression	523:532	Expression of chimeras of RNase 2 and nonglycosylated RNase 4 and deletion mutants in HEK293 cells	523:620	Expression of chimeras of RNase 2 and nonglycosylated RNase 4 and deletion mutants in HEK293 cells identified residues 1-13 to be sufficient for C-mannosylation.
9450956	6	10	theme	first	759:763	arg1	Trp					765:767	the first Trp	755:767	the first Trp	755:767	Site-directed mutagenesis revealed the sequence Trp-x-x-Trp, in which the first Trp becomes mannosylated, as the specificity determinant.
9450956	11	11	theme	more	1457:1460	arg1	proteins					1462:1469	more proteins	1457:1469	more proteins	1457:1469	The frequent occurrence of the protein recognition motif suggests that C-glycosides could be part of the structure of more proteins than assumed so far.
9450956	6	12	theme	Site-directed	685:697	arg1	mutagenesis					699:709	Site-directed mutagenesis	685:709	Site-directed mutagenesis	685:709	Site-directed mutagenesis revealed the sequence Trp-x-x-Trp, in which the first Trp becomes mannosylated, as the specificity determinant.
9450956	5	13	theme	RNase	549:553	arg1	mutants					598:604	deletion mutants	589:604	deletion mutants	589:604	Expression of chimeras of RNase 2 and nonglycosylated RNase 4 and deletion mutants in HEK293 cells identified residues 1-13 to be sufficient for C-mannosylation.
9450956	5	13	theme	RNase	549:553	arg1	chimeras					537:544	chimeras	537:544	chimeras of RNase 2 and nonglycosylated RNase 4	537:583	Expression of chimeras of RNase 2 and nonglycosylated RNase 4 and deletion mutants in HEK293 cells identified residues 1-13 to be sufficient for C-mannosylation.
9450956	2	14	theme	carbohydrate	263:274	arg1	way					246:248	a novel way	238:248	a novel way of attaching carbohydrate to a protein	238:287	It represents a novel way of attaching carbohydrate to a protein in addition to the well-known N- and O-glycosylations.
9450956	10	15	theme	proteins	1222:1229	arg1	Two					1209:1211	Two	1209:1211	Two	1209:1211	Two of these proteins were analyzed protein chemically, which showed partial C-glycosylation of recombinant human interleukin 12.
9450956	10	15	theme	proteins	1222:1229	arg1	proteins					1222:1229	these proteins	1216:1229	these proteins	1216:1229	Two of these proteins were analyzed protein chemically, which showed partial C-glycosylation of recombinant human interleukin 12.
9450956	11	16	theme	frequent	1343:1350	arg1	occurrence					1352:1361	The frequent occurrence	1339:1361	The frequent occurrence of the protein recognition motif	1339:1394	The frequent occurrence of the protein recognition motif suggests that C-glycosides could be part of the structure of more proteins than assumed so far.
9450956	11	17	theme	motif	1390:1394	arg1	occurrence					1352:1361	The frequent occurrence	1339:1361	The frequent occurrence of the protein recognition motif	1339:1394	The frequent occurrence of the protein recognition motif suggests that C-glycosides could be part of the structure of more proteins than assumed so far.
9450956	8	18	theme	three-dimensional	983:999	arg1	structure					1001:1009	the three-dimensional structure	979:1009	the three-dimensional structure of RNase 2	979:1020	Interpretation of the data in the context of the three-dimensional structure of RNase 2 strongly suggests that the primary, rather than the tertiary, structure forms the determinant.
9450956	9	19	theme	sequence	1121:1128	arg1	motif					1130:1134	The sequence motif	1117:1134	The sequence motif	1117:1134	The sequence motif occurs in 336 mammalian proteins currently present in protein databases.
9450956	2	20	theme	attaching	253:261	arg1	carbohydrate					263:274	attaching carbohydrate	253:274	attaching carbohydrate	253:274	It represents a novel way of attaching carbohydrate to a protein in addition to the well-known N- and O-glycosylations.
9450956	3	21	from	specific	360:367	arg1	modified					418:425	modified	418:425	is modified	415:425	The reaction is specific, as in RNase 2 Trp-7, but never Trp-10, which is modified.
9450956	3	21	from	specific	360:367	arg1	Trp-7					384:388	RNase 2 Trp-7	376:388	RNase 2 Trp-7	376:388	The reaction is specific, as in RNase 2 Trp-7, but never Trp-10, which is modified.
9450956	3	21	from	specific	360:367	arg1	Trp-10					401:406	Trp-10	401:406	Trp-10	401:406	The reaction is specific, as in RNase 2 Trp-7, but never Trp-10, which is modified.
9450956	0	22	theme	Trp-7	42:46	arg1	C-mannosylation					23:37	Recognition signal for C-mannosylation	0:37	Recognition signal for C-mannosylation of Trp-7 in RNase 2	0:57	Recognition signal for C-mannosylation of Trp-7 in RNase 2 consists of sequence Trp-x-x-Trp.
9450956	3	23	from	modified	418:425	arg1	specific					360:367	specific	360:367	specific	360:367	The reaction is specific, as in RNase 2 Trp-7, but never Trp-10, which is modified.
9450956	3	23	from	modified	418:425	arg1	reaction					348:355	The reaction	344:355	The reaction	344:355	The reaction is specific, as in RNase 2 Trp-7, but never Trp-10, which is modified.
9450956	7	24	from	position	842:849	arg1	residue					831:837	The Trp residue	823:837	The Trp residue at position +3	823:852	The Trp residue at position +3 can be replaced by Phe, which reduces the efficiency of the reaction threefold.
9450956	11	25	theme	protein	1370:1376	arg1	motif					1390:1394	the protein recognition motif	1366:1394	the protein recognition motif	1366:1394	The frequent occurrence of the protein recognition motif suggests that C-glycosides could be part of the structure of more proteins than assumed so far.
9450956	0	26	theme	signal	12:17	arg1	C-mannosylation					23:37	Recognition signal for C-mannosylation	0:37	Recognition signal for C-mannosylation of Trp-7 in RNase 2	0:57	Recognition signal for C-mannosylation of Trp-7 in RNase 2 consists of sequence Trp-x-x-Trp.
9450956	5	27	theme	RNase	577:581	arg1	mutants					598:604	deletion mutants	589:604	deletion mutants	589:604	Expression of chimeras of RNase 2 and nonglycosylated RNase 4 and deletion mutants in HEK293 cells identified residues 1-13 to be sufficient for C-mannosylation.
9450956	5	27	theme	RNase	577:581	arg1	chimeras					537:544	chimeras	537:544	chimeras of RNase 2 and nonglycosylated RNase 4	537:583	Expression of chimeras of RNase 2 and nonglycosylated RNase 4 and deletion mutants in HEK293 cells identified residues 1-13 to be sufficient for C-mannosylation.
9450956	5	28	theme	nonglycosylated	561:575	arg1	RNase					577:581	nonglycosylated RNase 4	561:583	nonglycosylated RNase 4	561:583	Expression of chimeras of RNase 2 and nonglycosylated RNase 4 and deletion mutants in HEK293 cells identified residues 1-13 to be sufficient for C-mannosylation.
9450956	11	29	theme	recognition	1378:1388	arg1	motif					1390:1394	the protein recognition motif	1366:1394	the protein recognition motif	1366:1394	The frequent occurrence of the protein recognition motif suggests that C-glycosides could be part of the structure of more proteins than assumed so far.
9450956	0	30	theme	Recognition	0:10	arg1	C-mannosylation					23:37	Recognition signal for C-mannosylation	0:37	Recognition signal for C-mannosylation of Trp-7 in RNase 2	0:57	Recognition signal for C-mannosylation of Trp-7 in RNase 2 consists of sequence Trp-x-x-Trp.
9450956	8	31	theme	structure	1001:1009	arg1	context					968:974	the context	964:974	the context of the three-dimensional structure of RNase 2	964:1020	Interpretation of the data in the context of the three-dimensional structure of RNase 2 strongly suggests that the primary, rather than the tertiary, structure forms the determinant.
9450956	8	32	theme	data	956:959	arg1	Interpretation					934:947	Interpretation	934:947	Interpretation of the data in the context of the three-dimensional structure of RNase 2	934:1020	Interpretation of the data in the context of the three-dimensional structure of RNase 2 strongly suggests that the primary, rather than the tertiary, structure forms the determinant.
9450956	10	33	theme	partial	1278:1284	arg1	C-glycosylation					1286:1300	partial C-glycosylation	1278:1300	partial C-glycosylation of recombinant human interleukin 12	1278:1336	Two of these proteins were analyzed protein chemically, which showed partial C-glycosylation of recombinant human interleukin 12.
9450956	10	34	theme	interleukin	1323:1333	arg1	C-glycosylation					1286:1300	partial C-glycosylation	1278:1300	partial C-glycosylation of recombinant human interleukin 12	1278:1336	Two of these proteins were analyzed protein chemically, which showed partial C-glycosylation of recombinant human interleukin 12.
9450956	2	35	dep	N-	319:320	arg1	the					304:306	the	304:306	the	304:306	It represents a novel way of attaching carbohydrate to a protein in addition to the well-known N- and O-glycosylations.
9450956	2	35	dep	N-	319:320	arg1	addition					292:299	addition	292:299	addition	292:299	It represents a novel way of attaching carbohydrate to a protein in addition to the well-known N- and O-glycosylations.
9450956	5	36	gly	nonglycosylated	561:575	arg1	RNase					577:581	nonglycosylated RNase 4	561:583	nonglycosylated RNase 4	561:583	Expression of chimeras of RNase 2 and nonglycosylated RNase 4 and deletion mutants in HEK293 cells identified residues 1-13 to be sufficient for C-mannosylation.
9450956	0	37	theme	for	19:21	arg1	C-mannosylation					23:37	Recognition signal for C-mannosylation	0:37	Recognition signal for C-mannosylation of Trp-7 in RNase 2	0:57	Recognition signal for C-mannosylation of Trp-7 in RNase 2 consists of sequence Trp-x-x-Trp.
9450956	8	38	theme	RNase	1014:1018	arg1	structure					1001:1009	the three-dimensional structure	979:1009	the three-dimensional structure of RNase 2	979:1020	Interpretation of the data in the context of the three-dimensional structure of RNase 2 strongly suggests that the primary, rather than the tertiary, structure forms the determinant.
9450956	9	39	theme	mammalian	1150:1158	arg1	proteins					1160:1167	336 mammalian proteins	1146:1167	336 mammalian proteins currently present in protein databases	1146:1206	The sequence motif occurs in 336 mammalian proteins currently present in protein databases.
9450956	3	40	theme	RNase	376:380	arg1	Trp-7					384:388	RNase 2 Trp-7	376:388	RNase 2 Trp-7	376:388	The reaction is specific, as in RNase 2 Trp-7, but never Trp-10, which is modified.
9450956	4	41	theme	structural	462:471	arg1	features					473:480	structural features	462:480	structural features	462:480	In this article, we address which structural features provide the specificity of the reaction.
9450956	6	42	theme	sequence	724:731	arg1	Trp-x-x-Trp					733:743	the sequence Trp-x-x-Trp	720:743	the sequence Trp-x-x-Trp	720:743	Site-directed mutagenesis revealed the sequence Trp-x-x-Trp, in which the first Trp becomes mannosylated, as the specificity determinant.
9450956	3	43	from	Trp-10	401:406	arg1	specific					360:367	specific	360:367	specific	360:367	The reaction is specific, as in RNase 2 Trp-7, but never Trp-10, which is modified.
9450956	3	43	from	Trp-10	401:406	arg1	reaction					348:355	The reaction	344:355	The reaction	344:355	The reaction is specific, as in RNase 2 Trp-7, but never Trp-10, which is modified.
9450956	5	44	theme	HEK293	609:614	arg1	cells					616:620	HEK293 cells	609:620	HEK293 cells	609:620	Expression of chimeras of RNase 2 and nonglycosylated RNase 4 and deletion mutants in HEK293 cells identified residues 1-13 to be sufficient for C-mannosylation.
9450956	6	45	theme	specificity	798:808	arg1	determinant					810:820	the specificity determinant	794:820	the specificity determinant	794:820	Site-directed mutagenesis revealed the sequence Trp-x-x-Trp, in which the first Trp becomes mannosylated, as the specificity determinant.
9450956	10	46	theme	human	1317:1321	arg1	interleukin					1323:1333	recombinant human interleukin 12	1305:1336	recombinant human interleukin 12	1305:1336	Two of these proteins were analyzed protein chemically, which showed partial C-glycosylation of recombinant human interleukin 12.
9450956	5	47	from	Expression	523:532	arg1	cells					616:620	HEK293 cells	609:620	HEK293 cells	609:620	Expression of chimeras of RNase 2 and nonglycosylated RNase 4 and deletion mutants in HEK293 cells identified residues 1-13 to be sufficient for C-mannosylation.
9450956	0	48	gly	C-mannosylation	23:37	arg1	Trp-7					42:46	Trp-7	42:46	Trp-7	42:46	Recognition signal for C-mannosylation of Trp-7 in RNase 2 consists of sequence Trp-x-x-Trp.
9450956	0	48	gly	C-mannosylation	23:37	arg1	RNase					51:55	RNase 2	51:57	RNase 2	51:57	Recognition signal for C-mannosylation of Trp-7 in RNase 2 consists of sequence Trp-x-x-Trp.
9450956	10	49	dep	chemically	1253:1262	arg1	protein					1245:1251	protein	1245:1251	protein	1245:1251	Two of these proteins were analyzed protein chemically, which showed partial C-glycosylation of recombinant human interleukin 12.
9450956	2	50	theme	well-known	308:317	arg1	N-					319:320	well-known N-	308:320	well-known N-	308:320	It represents a novel way of attaching carbohydrate to a protein in addition to the well-known N- and O-glycosylations.
9450956	9	51	theme	protein	1190:1196	arg1	databases					1198:1206	protein databases	1190:1206	protein databases	1190:1206	The sequence motif occurs in 336 mammalian proteins currently present in protein databases.
9450956	1	52	theme	human	139:143	arg1	RNase					145:149	human RNase 2	139:151	human RNase 2	139:151	C2-alpha-Mannosyltryptophan was discovered in human RNase 2, an enzyme that occurs in eosinophils and is involved in host defense.
9450956	1	52	theme	human	139:143	arg1	enzyme					157:162	an enzyme	154:162	an enzyme that occurs in eosinophils and is involved in host defense	154:221	C2-alpha-Mannosyltryptophan was discovered in human RNase 2, an enzyme that occurs in eosinophils and is involved in host defense.
9450956	10	53	gly	C-glycosylation	1286:1300	arg1	interleukin					1323:1333	recombinant human interleukin 12	1305:1336	recombinant human interleukin 12	1305:1336	Two of these proteins were analyzed protein chemically, which showed partial C-glycosylation of recombinant human interleukin 12.
9450956	1	54	theme	host	210:213	arg1	defense					215:221	host defense	210:221	host defense	210:221	C2-alpha-Mannosyltryptophan was discovered in human RNase 2, an enzyme that occurs in eosinophils and is involved in host defense.
9450956	8	55	theme	primary	1049:1055	arg1	structure					1084:1092	the primary, rather than the tertiary, structure	1045:1092	the primary, rather than the tertiary, structure	1045:1092	Interpretation of the data in the context of the three-dimensional structure of RNase 2 strongly suggests that the primary, rather than the tertiary, structure forms the determinant.
9450956	2	56	theme	novel	240:244	arg1	way					246:248	a novel way	238:248	a novel way of attaching carbohydrate to a protein	238:287	It represents a novel way of attaching carbohydrate to a protein in addition to the well-known N- and O-glycosylations.
9450956	3	57	from	Trp-7	384:388	arg1	specific					360:367	specific	360:367	specific	360:367	The reaction is specific, as in RNase 2 Trp-7, but never Trp-10, which is modified.
9450956	3	57	from	Trp-7	384:388	arg1	reaction					348:355	The reaction	344:355	The reaction	344:355	The reaction is specific, as in RNase 2 Trp-7, but never Trp-10, which is modified.
9450956	9	58	attach	present	1179:1185	arg1	databases					1198:1206	protein databases	1190:1206	protein databases	1190:1206	The sequence motif occurs in 336 mammalian proteins currently present in protein databases.
9450956	9	58	attach	present	1179:1185	arg2	proteins					1160:1167	336 mammalian proteins	1146:1167	336 mammalian proteins currently present in protein databases	1146:1206	The sequence motif occurs in 336 mammalian proteins currently present in protein databases.
9450956	9	59	from	databases	1198:1206	arg1	present					1179:1185	present	1179:1185	present	1179:1185	The sequence motif occurs in 336 mammalian proteins currently present in protein databases.
9450956	10	60	theme	recombinant	1305:1315	arg1	interleukin					1323:1333	recombinant human interleukin 12	1305:1336	recombinant human interleukin 12	1305:1336	Two of these proteins were analyzed protein chemically, which showed partial C-glycosylation of recombinant human interleukin 12.
9450956	11	61	theme	structure	1444:1452	arg1	part					1432:1435	part	1432:1435	part of the structure of more proteins	1432:1469	The frequent occurrence of the protein recognition motif suggests that C-glycosides could be part of the structure of more proteins than assumed so far.
9450956	0	62	from	C-mannosylation	23:37	arg1	RNase					51:55	RNase 2	51:57	RNase 2	51:57	Recognition signal for C-mannosylation of Trp-7 in RNase 2 consists of sequence Trp-x-x-Trp.
9450956	11	63	theme	proteins	1462:1469	arg1	structure					1444:1452	the structure	1440:1452	the structure of more proteins	1440:1469	The frequent occurrence of the protein recognition motif suggests that C-glycosides could be part of the structure of more proteins than assumed so far.
9450956	9	64	from	present	1179:1185	arg1	databases					1198:1206	protein databases	1190:1206	protein databases	1190:1206	The sequence motif occurs in 336 mammalian proteins currently present in protein databases.
20406422	6	0	theme	sorting	854:860	arg1	motifs					862:867	these sorting motifs	848:867	these sorting motifs	848:867	Mutation of these sorting motifs resulted in cell surface redistribution of CD4 chimeras.
20406422	1	1	theme	storage	264:270	arg1	lipofuscinosis					218:231	variant late infantile neuronal ceroid lipofuscinosis	179:231	variant late infantile neuronal ceroid lipofuscinosis	179:231	CLN7 is a polytopic lysosomal membrane protein deficient in variant late infantile neuronal ceroid lipofuscinosis, a neurodegenerative lysosomal storage disorder.
20406422	1	1	theme	storage	264:270	arg1	disorder					272:279	a neurodegenerative lysosomal storage disorder	234:279	a neurodegenerative lysosomal storage disorder	234:279	CLN7 is a polytopic lysosomal membrane protein deficient in variant late infantile neuronal ceroid lipofuscinosis, a neurodegenerative lysosomal storage disorder.
20406422	10	2	theme	N-terminal	1427:1436	arg1	motif					1454:1458	the N-terminal dileucine-based motif	1423:1458	the N-terminal dileucine-based motif	1423:1458	Our data demonstrate that CLN7 contains several cytoplasmic lysosomal targeting signals of which the N-terminal dileucine-based motif is required for the predominant lysosomal targeting along the indirect pathway and clathrin-mediated endocytosis of CLN7.
20406422	9	3	theme	mutant	1248:1253	arg1	K44A					1263:1266	dominant-negative mutant dynamin K44A	1230:1266	dominant-negative mutant dynamin K44A	1230:1266	Mutation of the dileucine motif or the co-expression of dominant-negative mutant dynamin K44A led to a further increase of CLN7 at the plasma membrane.
20406422	1	4	theme	deficient	166:174	arg1	CLN7					119:122	CLN7	119:122	CLN7	119:122	CLN7 is a polytopic lysosomal membrane protein deficient in variant late infantile neuronal ceroid lipofuscinosis, a neurodegenerative lysosomal storage disorder.
20406422	1	4	theme	deficient	166:174	arg1	protein					158:164	a polytopic lysosomal membrane protein	127:164	a polytopic lysosomal membrane protein deficient in variant late infantile neuronal ceroid lipofuscinosis, a neurodegenerative lysosomal storage disorder	127:279	CLN7 is a polytopic lysosomal membrane protein deficient in variant late infantile neuronal ceroid lipofuscinosis, a neurodegenerative lysosomal storage disorder.
20406422	6	5	theme	chimeras	916:923	arg1	redistribution					894:907	cell surface redistribution	881:907	cell surface redistribution of CD4 chimeras	881:923	Mutation of these sorting motifs resulted in cell surface redistribution of CD4 chimeras.
20406422	2	6	from	N-	373:374	arg1	cytosol					412:418	the cytosol	408:418	the cytosol	408:418	In this study fluorescence protease protection assays and mutational analyses revealed the N- and C-terminal tails of CLN7 in the cytosol and two N-glycosylation sites at N371 and N376.
20406422	9	7	theme	K44A	1263:1266	arg1	Mutation					1174:1181	Mutation	1174:1181	Mutation of the dileucine motif	1174:1204	Mutation of the dileucine motif or the co-expression of dominant-negative mutant dynamin K44A led to a further increase of CLN7 at the plasma membrane.
20406422	9	7	theme	K44A	1263:1266	arg1	co-expression					1213:1225	the co-expression	1209:1225	the co-expression of dominant-negative mutant dynamin K44A	1209:1266	Mutation of the dileucine motif or the co-expression of dominant-negative mutant dynamin K44A led to a further increase of CLN7 at the plasma membrane.
20406422	1	8	theme	variant	179:185	arg1	lipofuscinosis					218:231	variant late infantile neuronal ceroid lipofuscinosis	179:231	variant late infantile neuronal ceroid lipofuscinosis	179:231	CLN7 is a polytopic lysosomal membrane protein deficient in variant late infantile neuronal ceroid lipofuscinosis, a neurodegenerative lysosomal storage disorder.
20406422	1	8	theme	variant	179:185	arg1	disorder					272:279	a neurodegenerative lysosomal storage disorder	234:279	a neurodegenerative lysosomal storage disorder	234:279	CLN7 is a polytopic lysosomal membrane protein deficient in variant late infantile neuronal ceroid lipofuscinosis, a neurodegenerative lysosomal storage disorder.
20406422	5	9	theme	acidic	732:737	arg1	motif					755:759	a consensus acidic dileucine-based motif	720:759	a consensus acidic dileucine-based motif in the N-terminus	720:777	Lysosomal localization of the chimeric proteins requires a consensus acidic dileucine-based motif in the N-terminus and two tandem tyrosine-based signals in the C-terminus.
20406422	2	10	theme	protease	309:316	arg1	assays					329:334	fluorescence protease protection assays	296:334	fluorescence protease protection assays	296:334	In this study fluorescence protease protection assays and mutational analyses revealed the N- and C-terminal tails of CLN7 in the cytosol and two N-glycosylation sites at N371 and N376.
20406422	1	11	theme	infantile	192:200	arg1	lipofuscinosis					218:231	variant late infantile neuronal ceroid lipofuscinosis	179:231	variant late infantile neuronal ceroid lipofuscinosis	179:231	CLN7 is a polytopic lysosomal membrane protein deficient in variant late infantile neuronal ceroid lipofuscinosis, a neurodegenerative lysosomal storage disorder.
20406422	1	11	theme	infantile	192:200	arg1	disorder					272:279	a neurodegenerative lysosomal storage disorder	234:279	a neurodegenerative lysosomal storage disorder	234:279	CLN7 is a polytopic lysosomal membrane protein deficient in variant late infantile neuronal ceroid lipofuscinosis, a neurodegenerative lysosomal storage disorder.
20406422	5	12	from	motif	755:759	arg1	C-terminus					824:833	the C-terminus	820:833	the C-terminus	820:833	Lysosomal localization of the chimeric proteins requires a consensus acidic dileucine-based motif in the N-terminus and two tandem tyrosine-based signals in the C-terminus.
20406422	5	12	from	motif	755:759	arg1	N-terminus					768:777	the N-terminus	764:777	the N-terminus	764:777	Lysosomal localization of the chimeric proteins requires a consensus acidic dileucine-based motif in the N-terminus and two tandem tyrosine-based signals in the C-terminus.
20406422	9	13	theme	further	1277:1283	arg1	increase					1285:1292	a further increase	1275:1292	a further increase of CLN7 at the plasma membrane	1275:1323	Mutation of the dileucine motif or the co-expression of dominant-negative mutant dynamin K44A led to a further increase of CLN7 at the plasma membrane.
20406422	1	14	theme	ceroid	211:216	arg1	lipofuscinosis					218:231	variant late infantile neuronal ceroid lipofuscinosis	179:231	variant late infantile neuronal ceroid lipofuscinosis	179:231	CLN7 is a polytopic lysosomal membrane protein deficient in variant late infantile neuronal ceroid lipofuscinosis, a neurodegenerative lysosomal storage disorder.
20406422	1	14	theme	ceroid	211:216	arg1	disorder					272:279	a neurodegenerative lysosomal storage disorder	234:279	a neurodegenerative lysosomal storage disorder	234:279	CLN7 is a polytopic lysosomal membrane protein deficient in variant late infantile neuronal ceroid lipofuscinosis, a neurodegenerative lysosomal storage disorder.
20406422	5	15	theme	proteins	702:709	arg1	localization					673:684	Lysosomal localization	663:684	Lysosomal localization of the chimeric proteins	663:709	Lysosomal localization of the chimeric proteins requires a consensus acidic dileucine-based motif in the N-terminus and two tandem tyrosine-based signals in the C-terminus.
20406422	5	16	from	signals	809:815	arg1	C-terminus					824:833	the C-terminus	820:833	the C-terminus	820:833	Lysosomal localization of the chimeric proteins requires a consensus acidic dileucine-based motif in the N-terminus and two tandem tyrosine-based signals in the C-terminus.
20406422	5	16	from	signals	809:815	arg1	N-terminus					768:777	the N-terminus	764:777	the N-terminus	764:777	Lysosomal localization of the chimeric proteins requires a consensus acidic dileucine-based motif in the N-terminus and two tandem tyrosine-based signals in the C-terminus.
20406422	7	17	theme	cell	1051:1054	arg1	lines					1056:1060	different cell lines	1041:1060	different cell lines	1041:1060	However, the dileucine-based motif is of critical importance for lysosomal localization of the full-length CLN7 in different cell lines.
20406422	4	18	dep	N-	628:629	arg1	the					624:626	the	624:626	the	624:626	To identify lysosomal targeting motifs, we generated CD4-chimera fused to the N- and C-terminal domains of CLN7.
20406422	8	19	located	localized	1140:1148	arg2	%					1121:1121	at equilibrium 22%	1104:1121	at equilibrium 22% of total CLN7	1104:1135	Cell surface biotinylation revealed that at equilibrium 22% of total CLN7 is localized at the plasma membrane.
20406422	8	19	located	localized	1140:1148	arg1	membrane					1164:1171	the plasma membrane	1153:1171	the plasma membrane	1153:1171	Cell surface biotinylation revealed that at equilibrium 22% of total CLN7 is localized at the plasma membrane.
20406422	8	19	located	localized	1140:1148	arg2	CLN7					1132:1135	total CLN7	1126:1135	total CLN7	1126:1135	Cell surface biotinylation revealed that at equilibrium 22% of total CLN7 is localized at the plasma membrane.
20406422	5	20	theme	tandem	787:792	arg1	signals					809:815	two tandem tyrosine-based signals	783:815	two tandem tyrosine-based signals in the C-terminus	783:833	Lysosomal localization of the chimeric proteins requires a consensus acidic dileucine-based motif in the N-terminus and two tandem tyrosine-based signals in the C-terminus.
20406422	9	21	theme	plasma	1309:1314	arg1	membrane					1316:1323	the plasma membrane	1305:1323	the plasma membrane	1305:1323	Mutation of the dileucine motif or the co-expression of dominant-negative mutant dynamin K44A led to a further increase of CLN7 at the plasma membrane.
20406422	7	22	theme	full-length	1021:1031	arg1	CLN7					1033:1036	the full-length CLN7	1017:1036	the full-length CLN7	1017:1036	However, the dileucine-based motif is of critical importance for lysosomal localization of the full-length CLN7 in different cell lines.
20406422	1	23	theme	polytopic	129:137	arg1	CLN7					119:122	CLN7	119:122	CLN7	119:122	CLN7 is a polytopic lysosomal membrane protein deficient in variant late infantile neuronal ceroid lipofuscinosis, a neurodegenerative lysosomal storage disorder.
20406422	1	23	theme	polytopic	129:137	arg1	protein					158:164	a polytopic lysosomal membrane protein	127:164	a polytopic lysosomal membrane protein deficient in variant late infantile neuronal ceroid lipofuscinosis, a neurodegenerative lysosomal storage disorder	127:279	CLN7 is a polytopic lysosomal membrane protein deficient in variant late infantile neuronal ceroid lipofuscinosis, a neurodegenerative lysosomal storage disorder.
20406422	2	24	from	sites	444:448	arg1	cytosol					412:418	the cytosol	408:418	the cytosol	408:418	In this study fluorescence protease protection assays and mutational analyses revealed the N- and C-terminal tails of CLN7 in the cytosol and two N-glycosylation sites at N371 and N376.
20406422	8	25	theme	surface	1068:1074	arg1	biotinylation					1076:1088	Cell surface biotinylation	1063:1088	Cell surface biotinylation	1063:1088	Cell surface biotinylation revealed that at equilibrium 22% of total CLN7 is localized at the plasma membrane.
20406422	1	26	theme	membrane	149:156	arg1	CLN7					119:122	CLN7	119:122	CLN7	119:122	CLN7 is a polytopic lysosomal membrane protein deficient in variant late infantile neuronal ceroid lipofuscinosis, a neurodegenerative lysosomal storage disorder.
20406422	1	26	theme	membrane	149:156	arg1	protein					158:164	a polytopic lysosomal membrane protein	127:164	a polytopic lysosomal membrane protein deficient in variant late infantile neuronal ceroid lipofuscinosis, a neurodegenerative lysosomal storage disorder	127:279	CLN7 is a polytopic lysosomal membrane protein deficient in variant late infantile neuronal ceroid lipofuscinosis, a neurodegenerative lysosomal storage disorder.
20406422	2	27	from	N371	453:456	arg1	sites					444:448	two N-glycosylation sites	424:448	two N-glycosylation sites at N371 and N376	424:465	In this study fluorescence protease protection assays and mutational analyses revealed the N- and C-terminal tails of CLN7 in the cytosol and two N-glycosylation sites at N371 and N376.
20406422	2	27	from	N371	453:456	arg1	CLN7					400:403	CLN7	400:403	CLN7	400:403	In this study fluorescence protease protection assays and mutational analyses revealed the N- and C-terminal tails of CLN7 in the cytosol and two N-glycosylation sites at N371 and N376.
20406422	2	27	from	N371	453:456	arg1	N-					373:374	N-	373:374	N-	373:374	In this study fluorescence protease protection assays and mutational analyses revealed the N- and C-terminal tails of CLN7 in the cytosol and two N-glycosylation sites at N371 and N376.
20406422	2	27	from	N371	453:456	arg1	tails					391:395	C-terminal tails	380:395	C-terminal tails	380:395	In this study fluorescence protease protection assays and mutational analyses revealed the N- and C-terminal tails of CLN7 in the cytosol and two N-glycosylation sites at N371 and N376.
20406422	10	28	theme	lysosomal	1492:1500	arg1	targeting					1502:1510	the predominant lysosomal targeting	1476:1510	the predominant lysosomal targeting along the indirect pathway	1476:1537	Our data demonstrate that CLN7 contains several cytoplasmic lysosomal targeting signals of which the N-terminal dileucine-based motif is required for the predominant lysosomal targeting along the indirect pathway and clathrin-mediated endocytosis of CLN7.
20406422	7	29	theme	lysosomal	991:999	arg1	localization					1001:1012	lysosomal localization	991:1012	lysosomal localization of the full-length CLN7 in different cell lines	991:1060	However, the dileucine-based motif is of critical importance for lysosomal localization of the full-length CLN7 in different cell lines.
20406422	2	30	from	N376	462:465	arg1	sites					444:448	two N-glycosylation sites	424:448	two N-glycosylation sites at N371 and N376	424:465	In this study fluorescence protease protection assays and mutational analyses revealed the N- and C-terminal tails of CLN7 in the cytosol and two N-glycosylation sites at N371 and N376.
20406422	2	30	from	N376	462:465	arg1	CLN7					400:403	CLN7	400:403	CLN7	400:403	In this study fluorescence protease protection assays and mutational analyses revealed the N- and C-terminal tails of CLN7 in the cytosol and two N-glycosylation sites at N371 and N376.
20406422	2	30	from	N376	462:465	arg1	N-					373:374	N-	373:374	N-	373:374	In this study fluorescence protease protection assays and mutational analyses revealed the N- and C-terminal tails of CLN7 in the cytosol and two N-glycosylation sites at N371 and N376.
20406422	2	30	from	N376	462:465	arg1	tails					391:395	C-terminal tails	380:395	C-terminal tails	380:395	In this study fluorescence protease protection assays and mutational analyses revealed the N- and C-terminal tails of CLN7 in the cytosol and two N-glycosylation sites at N371 and N376.
20406422	8	31	theme	at	1104:1105	arg1	CLN7					1132:1135	total CLN7	1126:1135	total CLN7	1126:1135	Cell surface biotinylation revealed that at equilibrium 22% of total CLN7 is localized at the plasma membrane.
20406422	8	31	theme	at	1104:1105	arg1	%					1121:1121	at equilibrium 22%	1104:1121	at equilibrium 22% of total CLN7	1104:1135	Cell surface biotinylation revealed that at equilibrium 22% of total CLN7 is localized at the plasma membrane.
20406422	10	32	theme	indirect	1522:1529	arg1	pathway					1531:1537	the indirect pathway	1518:1537	the indirect pathway	1518:1537	Our data demonstrate that CLN7 contains several cytoplasmic lysosomal targeting signals of which the N-terminal dileucine-based motif is required for the predominant lysosomal targeting along the indirect pathway and clathrin-mediated endocytosis of CLN7.
20406422	2	33	theme	CLN7	400:403	arg1	sites					444:448	two N-glycosylation sites	424:448	two N-glycosylation sites at N371 and N376	424:465	In this study fluorescence protease protection assays and mutational analyses revealed the N- and C-terminal tails of CLN7 in the cytosol and two N-glycosylation sites at N371 and N376.
20406422	2	33	theme	CLN7	400:403	arg1	CLN7					400:403	CLN7	400:403	CLN7	400:403	In this study fluorescence protease protection assays and mutational analyses revealed the N- and C-terminal tails of CLN7 in the cytosol and two N-glycosylation sites at N371 and N376.
20406422	2	33	theme	CLN7	400:403	arg1	N-					373:374	N-	373:374	N-	373:374	In this study fluorescence protease protection assays and mutational analyses revealed the N- and C-terminal tails of CLN7 in the cytosol and two N-glycosylation sites at N371 and N376.
20406422	2	33	theme	CLN7	400:403	arg1	tails					391:395	C-terminal tails	380:395	C-terminal tails	380:395	In this study fluorescence protease protection assays and mutational analyses revealed the N- and C-terminal tails of CLN7 in the cytosol and two N-glycosylation sites at N371 and N376.
20406422	0	34	theme	Lysosomal	0:8	arg1	targeting					10:18	Lysosomal targeting	0:18	Lysosomal targeting of the CLN7 membrane glycoprotein	0:52	Lysosomal targeting of the CLN7 membrane glycoprotein and transport via the plasma membrane require a dileucine motif.
20406422	10	35	contain	contains	1357:1364	arg2	signals					1406:1412	several cytoplasmic lysosomal targeting signals	1366:1412	several cytoplasmic lysosomal targeting signals of which the N-terminal dileucine-based motif is required for the predominant lysosomal targeting along the indirect pathway and clathrin-mediated endocytosis of CLN7	1366:1579	Our data demonstrate that CLN7 contains several cytoplasmic lysosomal targeting signals of which the N-terminal dileucine-based motif is required for the predominant lysosomal targeting along the indirect pathway and clathrin-mediated endocytosis of CLN7.
20406422	10	35	contain	contains	1357:1364	arg1	CLN7					1352:1355	CLN7	1352:1355	CLN7	1352:1355	Our data demonstrate that CLN7 contains several cytoplasmic lysosomal targeting signals of which the N-terminal dileucine-based motif is required for the predominant lysosomal targeting along the indirect pathway and clathrin-mediated endocytosis of CLN7.
20406422	4	36	theme	targeting	572:580	arg1	motifs					582:587	lysosomal targeting motifs	562:587	lysosomal targeting motifs	562:587	To identify lysosomal targeting motifs, we generated CD4-chimera fused to the N- and C-terminal domains of CLN7.
20406422	10	37	theme	CLN7	1576:1579	arg1	targeting					1502:1510	the predominant lysosomal targeting	1476:1510	the predominant lysosomal targeting along the indirect pathway	1476:1537	Our data demonstrate that CLN7 contains several cytoplasmic lysosomal targeting signals of which the N-terminal dileucine-based motif is required for the predominant lysosomal targeting along the indirect pathway and clathrin-mediated endocytosis of CLN7.
20406422	10	37	theme	CLN7	1576:1579	arg1	endocytosis					1561:1571	clathrin-mediated endocytosis	1543:1571	clathrin-mediated endocytosis of CLN7	1543:1579	Our data demonstrate that CLN7 contains several cytoplasmic lysosomal targeting signals of which the N-terminal dileucine-based motif is required for the predominant lysosomal targeting along the indirect pathway and clathrin-mediated endocytosis of CLN7.
20406422	3	38	gly	non-glycosylated	487:502	arg1	CLN7					504:507	Both partially and non-glycosylated CLN7	468:507	Both partially and non-glycosylated CLN7	468:507	Both partially and non-glycosylated CLN7 were correctly transported to lysosomes.
20406422	2	39	theme	N-glycosylation	428:442	arg1	sites					444:448	two N-glycosylation sites	424:448	two N-glycosylation sites at N371 and N376	424:465	In this study fluorescence protease protection assays and mutational analyses revealed the N- and C-terminal tails of CLN7 in the cytosol and two N-glycosylation sites at N371 and N376.
20406422	2	39	theme	N-glycosylation	428:442	arg1	CLN7					400:403	CLN7	400:403	CLN7	400:403	In this study fluorescence protease protection assays and mutational analyses revealed the N- and C-terminal tails of CLN7 in the cytosol and two N-glycosylation sites at N371 and N376.
20406422	6	40	theme	CD4	912:914	arg1	chimeras					916:923	CD4 chimeras	912:923	CD4 chimeras	912:923	Mutation of these sorting motifs resulted in cell surface redistribution of CD4 chimeras.
20406422	0	41	theme	CLN7	27:30	arg1	glycoprotein					41:52	the CLN7 membrane glycoprotein	23:52	the CLN7 membrane glycoprotein	23:52	Lysosomal targeting of the CLN7 membrane glycoprotein and transport via the plasma membrane require a dileucine motif.
20406422	8	42	theme	CLN7	1132:1135	arg1	CLN7					1132:1135	total CLN7	1126:1135	total CLN7	1126:1135	Cell surface biotinylation revealed that at equilibrium 22% of total CLN7 is localized at the plasma membrane.
20406422	8	42	theme	CLN7	1132:1135	arg1	%					1121:1121	at equilibrium 22%	1104:1121	at equilibrium 22% of total CLN7	1104:1135	Cell surface biotinylation revealed that at equilibrium 22% of total CLN7 is localized at the plasma membrane.
20406422	10	43	theme	cytoplasmic	1374:1384	arg1	signals					1406:1412	several cytoplasmic lysosomal targeting signals	1366:1412	several cytoplasmic lysosomal targeting signals of which the N-terminal dileucine-based motif is required for the predominant lysosomal targeting along the indirect pathway and clathrin-mediated endocytosis of CLN7	1366:1579	Our data demonstrate that CLN7 contains several cytoplasmic lysosomal targeting signals of which the N-terminal dileucine-based motif is required for the predominant lysosomal targeting along the indirect pathway and clathrin-mediated endocytosis of CLN7.
20406422	0	44	theme	glycoprotein	41:52	arg1	transport					58:66	transport	58:66	transport via the plasma membrane	58:90	Lysosomal targeting of the CLN7 membrane glycoprotein and transport via the plasma membrane require a dileucine motif.
20406422	0	44	theme	glycoprotein	41:52	arg1	targeting					10:18	Lysosomal targeting	0:18	Lysosomal targeting of the CLN7 membrane glycoprotein	0:52	Lysosomal targeting of the CLN7 membrane glycoprotein and transport via the plasma membrane require a dileucine motif.
20406422	6	45	theme	cell	881:884	arg1	redistribution					894:907	cell surface redistribution	881:907	cell surface redistribution of CD4 chimeras	881:923	Mutation of these sorting motifs resulted in cell surface redistribution of CD4 chimeras.
20406422	9	46	theme	dileucine	1190:1198	arg1	motif					1200:1204	the dileucine motif	1186:1204	the dileucine motif	1186:1204	Mutation of the dileucine motif or the co-expression of dominant-negative mutant dynamin K44A led to a further increase of CLN7 at the plasma membrane.
20406422	7	47	theme	dileucine-based	939:953	arg1	motif					955:959	the dileucine-based motif	935:959	the dileucine-based motif	935:959	However, the dileucine-based motif is of critical importance for lysosomal localization of the full-length CLN7 in different cell lines.
20406422	5	48	theme	tyrosine-based	794:807	arg1	signals					809:815	two tandem tyrosine-based signals	783:815	two tandem tyrosine-based signals in the C-terminus	783:833	Lysosomal localization of the chimeric proteins requires a consensus acidic dileucine-based motif in the N-terminus and two tandem tyrosine-based signals in the C-terminus.
20406422	5	49	theme	Lysosomal	663:671	arg1	localization					673:684	Lysosomal localization	663:684	Lysosomal localization of the chimeric proteins	663:709	Lysosomal localization of the chimeric proteins requires a consensus acidic dileucine-based motif in the N-terminus and two tandem tyrosine-based signals in the C-terminus.
20406422	10	50	theme	targeting	1396:1404	arg1	signals					1406:1412	several cytoplasmic lysosomal targeting signals	1366:1412	several cytoplasmic lysosomal targeting signals of which the N-terminal dileucine-based motif is required for the predominant lysosomal targeting along the indirect pathway and clathrin-mediated endocytosis of CLN7	1366:1579	Our data demonstrate that CLN7 contains several cytoplasmic lysosomal targeting signals of which the N-terminal dileucine-based motif is required for the predominant lysosomal targeting along the indirect pathway and clathrin-mediated endocytosis of CLN7.
20406422	1	51	theme	lysosomal	254:262	arg1	lipofuscinosis					218:231	variant late infantile neuronal ceroid lipofuscinosis	179:231	variant late infantile neuronal ceroid lipofuscinosis	179:231	CLN7 is a polytopic lysosomal membrane protein deficient in variant late infantile neuronal ceroid lipofuscinosis, a neurodegenerative lysosomal storage disorder.
20406422	1	51	theme	lysosomal	254:262	arg1	disorder					272:279	a neurodegenerative lysosomal storage disorder	234:279	a neurodegenerative lysosomal storage disorder	234:279	CLN7 is a polytopic lysosomal membrane protein deficient in variant late infantile neuronal ceroid lipofuscinosis, a neurodegenerative lysosomal storage disorder.
20406422	10	52	theme	dileucine-based	1438:1452	arg1	motif					1454:1458	the N-terminal dileucine-based motif	1423:1458	the N-terminal dileucine-based motif	1423:1458	Our data demonstrate that CLN7 contains several cytoplasmic lysosomal targeting signals of which the N-terminal dileucine-based motif is required for the predominant lysosomal targeting along the indirect pathway and clathrin-mediated endocytosis of CLN7.
20406422	2	53	theme	fluorescence	296:307	arg1	assays					329:334	fluorescence protease protection assays	296:334	fluorescence protease protection assays	296:334	In this study fluorescence protease protection assays and mutational analyses revealed the N- and C-terminal tails of CLN7 in the cytosol and two N-glycosylation sites at N371 and N376.
20406422	7	54	theme	CLN7	1033:1036	arg1	localization					1001:1012	lysosomal localization	991:1012	lysosomal localization of the full-length CLN7 in different cell lines	991:1060	However, the dileucine-based motif is of critical importance for lysosomal localization of the full-length CLN7 in different cell lines.
20406422	9	55	from	increase	1285:1292	arg1	membrane					1316:1323	the plasma membrane	1305:1323	the plasma membrane	1305:1323	Mutation of the dileucine motif or the co-expression of dominant-negative mutant dynamin K44A led to a further increase of CLN7 at the plasma membrane.
20406422	9	56	theme	dominant-negative	1230:1246	arg1	K44A					1263:1266	dominant-negative mutant dynamin K44A	1230:1266	dominant-negative mutant dynamin K44A	1230:1266	Mutation of the dileucine motif or the co-expression of dominant-negative mutant dynamin K44A led to a further increase of CLN7 at the plasma membrane.
20406422	9	57	theme	dynamin	1255:1261	arg1	K44A					1263:1266	dominant-negative mutant dynamin K44A	1230:1266	dominant-negative mutant dynamin K44A	1230:1266	Mutation of the dileucine motif or the co-expression of dominant-negative mutant dynamin K44A led to a further increase of CLN7 at the plasma membrane.
20406422	8	58	theme	Cell	1063:1066	arg1	biotinylation					1076:1088	Cell surface biotinylation	1063:1088	Cell surface biotinylation	1063:1088	Cell surface biotinylation revealed that at equilibrium 22% of total CLN7 is localized at the plasma membrane.
20406422	2	59	from	tails	391:395	arg1	cytosol					412:418	the cytosol	408:418	the cytosol	408:418	In this study fluorescence protease protection assays and mutational analyses revealed the N- and C-terminal tails of CLN7 in the cytosol and two N-glycosylation sites at N371 and N376.
20406422	5	60	theme	consensus	722:730	arg1	motif					755:759	a consensus acidic dileucine-based motif	720:759	a consensus acidic dileucine-based motif in the N-terminus	720:777	Lysosomal localization of the chimeric proteins requires a consensus acidic dileucine-based motif in the N-terminus and two tandem tyrosine-based signals in the C-terminus.
20406422	2	61	theme	protection	318:327	arg1	assays					329:334	fluorescence protease protection assays	296:334	fluorescence protease protection assays	296:334	In this study fluorescence protease protection assays and mutational analyses revealed the N- and C-terminal tails of CLN7 in the cytosol and two N-glycosylation sites at N371 and N376.
20406422	1	62	theme	late	187:190	arg1	lipofuscinosis					218:231	variant late infantile neuronal ceroid lipofuscinosis	179:231	variant late infantile neuronal ceroid lipofuscinosis	179:231	CLN7 is a polytopic lysosomal membrane protein deficient in variant late infantile neuronal ceroid lipofuscinosis, a neurodegenerative lysosomal storage disorder.
20406422	1	62	theme	late	187:190	arg1	disorder					272:279	a neurodegenerative lysosomal storage disorder	234:279	a neurodegenerative lysosomal storage disorder	234:279	CLN7 is a polytopic lysosomal membrane protein deficient in variant late infantile neuronal ceroid lipofuscinosis, a neurodegenerative lysosomal storage disorder.
20406422	5	63	theme	dileucine-based	739:753	arg1	motif					755:759	a consensus acidic dileucine-based motif	720:759	a consensus acidic dileucine-based motif in the N-terminus	720:777	Lysosomal localization of the chimeric proteins requires a consensus acidic dileucine-based motif in the N-terminus and two tandem tyrosine-based signals in the C-terminus.
20406422	1	64	theme	neuronal	202:209	arg1	lipofuscinosis					218:231	variant late infantile neuronal ceroid lipofuscinosis	179:231	variant late infantile neuronal ceroid lipofuscinosis	179:231	CLN7 is a polytopic lysosomal membrane protein deficient in variant late infantile neuronal ceroid lipofuscinosis, a neurodegenerative lysosomal storage disorder.
20406422	1	64	theme	neuronal	202:209	arg1	disorder					272:279	a neurodegenerative lysosomal storage disorder	234:279	a neurodegenerative lysosomal storage disorder	234:279	CLN7 is a polytopic lysosomal membrane protein deficient in variant late infantile neuronal ceroid lipofuscinosis, a neurodegenerative lysosomal storage disorder.
20406422	8	65	from	%	1121:1121	arg1	equilibrium					1107:1117	at equilibrium 22%	1104:1121	at equilibrium 22% of total CLN7	1104:1135	Cell surface biotinylation revealed that at equilibrium 22% of total CLN7 is localized at the plasma membrane.
20406422	8	65	from	%	1121:1121	arg1	at					1104:1105	at equilibrium 22%	1104:1121	at equilibrium 22% of total CLN7	1104:1135	Cell surface biotinylation revealed that at equilibrium 22% of total CLN7 is localized at the plasma membrane.
20406422	4	66	theme	CLN7	657:660	arg1	CLN7					657:660	CLN7	657:660	CLN7	657:660	To identify lysosomal targeting motifs, we generated CD4-chimera fused to the N- and C-terminal domains of CLN7.
20406422	4	66	theme	CLN7	657:660	arg1	N-					628:629	N-	628:629	N-	628:629	To identify lysosomal targeting motifs, we generated CD4-chimera fused to the N- and C-terminal domains of CLN7.
20406422	4	66	theme	CLN7	657:660	arg1	domains					646:652	C-terminal domains	635:652	C-terminal domains	635:652	To identify lysosomal targeting motifs, we generated CD4-chimera fused to the N- and C-terminal domains of CLN7.
20406422	5	67	theme	chimeric	693:700	arg1	proteins					702:709	the chimeric proteins	689:709	the chimeric proteins	689:709	Lysosomal localization of the chimeric proteins requires a consensus acidic dileucine-based motif in the N-terminus and two tandem tyrosine-based signals in the C-terminus.
20406422	9	68	from	membrane	1316:1323	arg1	CLN7					1297:1300	CLN7	1297:1300	CLN7 at the plasma membrane	1297:1323	Mutation of the dileucine motif or the co-expression of dominant-negative mutant dynamin K44A led to a further increase of CLN7 at the plasma membrane.
20406422	9	68	from	membrane	1316:1323	arg1	increase					1285:1292	a further increase	1275:1292	a further increase of CLN7 at the plasma membrane	1275:1323	Mutation of the dileucine motif or the co-expression of dominant-negative mutant dynamin K44A led to a further increase of CLN7 at the plasma membrane.
20406422	1	69	from	lipofuscinosis	218:231	arg1	deficient					166:174	deficient	166:174	deficient	166:174	CLN7 is a polytopic lysosomal membrane protein deficient in variant late infantile neuronal ceroid lipofuscinosis, a neurodegenerative lysosomal storage disorder.
20406422	9	70	theme	CLN7	1297:1300	arg1	increase					1285:1292	a further increase	1275:1292	a further increase of CLN7 at the plasma membrane	1275:1323	Mutation of the dileucine motif or the co-expression of dominant-negative mutant dynamin K44A led to a further increase of CLN7 at the plasma membrane.
20406422	7	71	theme	different	1041:1049	arg1	lines					1056:1060	different cell lines	1041:1060	different cell lines	1041:1060	However, the dileucine-based motif is of critical importance for lysosomal localization of the full-length CLN7 in different cell lines.
20406422	7	72	from	localization	1001:1012	arg1	lines					1056:1060	different cell lines	1041:1060	different cell lines	1041:1060	However, the dileucine-based motif is of critical importance for lysosomal localization of the full-length CLN7 in different cell lines.
20406422	0	73	theme	plasma	76:81	arg1	membrane					83:90	the plasma membrane	72:90	the plasma membrane	72:90	Lysosomal targeting of the CLN7 membrane glycoprotein and transport via the plasma membrane require a dileucine motif.
20406422	1	74	from	deficient	166:174	arg1	lipofuscinosis					218:231	variant late infantile neuronal ceroid lipofuscinosis	179:231	variant late infantile neuronal ceroid lipofuscinosis	179:231	CLN7 is a polytopic lysosomal membrane protein deficient in variant late infantile neuronal ceroid lipofuscinosis, a neurodegenerative lysosomal storage disorder.
20406422	1	74	from	deficient	166:174	arg1	disorder					272:279	a neurodegenerative lysosomal storage disorder	234:279	a neurodegenerative lysosomal storage disorder	234:279	CLN7 is a polytopic lysosomal membrane protein deficient in variant late infantile neuronal ceroid lipofuscinosis, a neurodegenerative lysosomal storage disorder.
20406422	1	75	theme	lysosomal	139:147	arg1	CLN7					119:122	CLN7	119:122	CLN7	119:122	CLN7 is a polytopic lysosomal membrane protein deficient in variant late infantile neuronal ceroid lipofuscinosis, a neurodegenerative lysosomal storage disorder.
20406422	1	75	theme	lysosomal	139:147	arg1	protein					158:164	a polytopic lysosomal membrane protein	127:164	a polytopic lysosomal membrane protein deficient in variant late infantile neuronal ceroid lipofuscinosis, a neurodegenerative lysosomal storage disorder	127:279	CLN7 is a polytopic lysosomal membrane protein deficient in variant late infantile neuronal ceroid lipofuscinosis, a neurodegenerative lysosomal storage disorder.
20406422	2	76	gly	N-glycosylation	428:442	arg2	two					424:426	two	424:426	two	424:426	In this study fluorescence protease protection assays and mutational analyses revealed the N- and C-terminal tails of CLN7 in the cytosol and two N-glycosylation sites at N371 and N376.
20406422	2	76	gly	N-glycosylation	428:442	arg2	N376					462:465	N376	462:465	N376	462:465	In this study fluorescence protease protection assays and mutational analyses revealed the N- and C-terminal tails of CLN7 in the cytosol and two N-glycosylation sites at N371 and N376.
20406422	2	76	gly	N-glycosylation	428:442	arg2	CLN7					400:403	CLN7	400:403	CLN7	400:403	In this study fluorescence protease protection assays and mutational analyses revealed the N- and C-terminal tails of CLN7 in the cytosol and two N-glycosylation sites at N371 and N376.
20406422	2	76	gly	N-glycosylation	428:442	arg2	sites					444:448	two N-glycosylation sites	424:448	two N-glycosylation sites at N371 and N376	424:465	In this study fluorescence protease protection assays and mutational analyses revealed the N- and C-terminal tails of CLN7 in the cytosol and two N-glycosylation sites at N371 and N376.
20406422	2	76	gly	N-glycosylation	428:442	arg1	CLN7					400:403	CLN7	400:403	CLN7	400:403	In this study fluorescence protease protection assays and mutational analyses revealed the N- and C-terminal tails of CLN7 in the cytosol and two N-glycosylation sites at N371 and N376.
20406422	2	76	gly	N-glycosylation	428:442	arg2	N371					453:456	N371	453:456	N371	453:456	In this study fluorescence protease protection assays and mutational analyses revealed the N- and C-terminal tails of CLN7 in the cytosol and two N-glycosylation sites at N371 and N376.
20406422	10	77	theme	predominant	1480:1490	arg1	targeting					1502:1510	the predominant lysosomal targeting	1476:1510	the predominant lysosomal targeting along the indirect pathway	1476:1537	Our data demonstrate that CLN7 contains several cytoplasmic lysosomal targeting signals of which the N-terminal dileucine-based motif is required for the predominant lysosomal targeting along the indirect pathway and clathrin-mediated endocytosis of CLN7.
20406422	2	78	dep	N-	373:374	arg1	the					369:371	the	369:371	the	369:371	In this study fluorescence protease protection assays and mutational analyses revealed the N- and C-terminal tails of CLN7 in the cytosol and two N-glycosylation sites at N371 and N376.
20406422	0	79	theme	dileucine	102:110	arg1	motif					112:116	a dileucine motif	100:116	a dileucine motif	100:116	Lysosomal targeting of the CLN7 membrane glycoprotein and transport via the plasma membrane require a dileucine motif.
20406422	8	80	theme	equilibrium	1107:1117	arg1	CLN7					1132:1135	total CLN7	1126:1135	total CLN7	1126:1135	Cell surface biotinylation revealed that at equilibrium 22% of total CLN7 is localized at the plasma membrane.
20406422	8	80	theme	equilibrium	1107:1117	arg1	%					1121:1121	at equilibrium 22%	1104:1121	at equilibrium 22% of total CLN7	1104:1135	Cell surface biotinylation revealed that at equilibrium 22% of total CLN7 is localized at the plasma membrane.
20406422	3	81	dep	CLN7	504:507	arg1	Both					468:471	Both	468:471	Both	468:471	Both partially and non-glycosylated CLN7 were correctly transported to lysosomes.
20406422	3	81	dep	CLN7	504:507	arg1	non-glycosylated					487:502	non-glycosylated	487:502	non-glycosylated	487:502	Both partially and non-glycosylated CLN7 were correctly transported to lysosomes.
20406422	0	82	gly	glycoprotein	41:52	arg1	glycoprotein					41:52	the CLN7 membrane glycoprotein	23:52	the CLN7 membrane glycoprotein	23:52	Lysosomal targeting of the CLN7 membrane glycoprotein and transport via the plasma membrane require a dileucine motif.
20406422	8	83	theme	total	1126:1130	arg1	CLN7					1132:1135	total CLN7	1126:1135	total CLN7	1126:1135	Cell surface biotinylation revealed that at equilibrium 22% of total CLN7 is localized at the plasma membrane.
20406422	7	84	theme	critical	967:974	arg1	importance					976:985	critical importance	967:985	critical importance	967:985	However, the dileucine-based motif is of critical importance for lysosomal localization of the full-length CLN7 in different cell lines.
20406422	0	85	theme	membrane	32:39	arg1	glycoprotein					41:52	the CLN7 membrane glycoprotein	23:52	the CLN7 membrane glycoprotein	23:52	Lysosomal targeting of the CLN7 membrane glycoprotein and transport via the plasma membrane require a dileucine motif.
20406422	10	86	theme	clathrin-mediated	1543:1559	arg1	endocytosis					1561:1571	clathrin-mediated endocytosis	1543:1571	clathrin-mediated endocytosis of CLN7	1543:1579	Our data demonstrate that CLN7 contains several cytoplasmic lysosomal targeting signals of which the N-terminal dileucine-based motif is required for the predominant lysosomal targeting along the indirect pathway and clathrin-mediated endocytosis of CLN7.
20406422	10	87	theme	lysosomal	1386:1394	arg1	signals					1406:1412	several cytoplasmic lysosomal targeting signals	1366:1412	several cytoplasmic lysosomal targeting signals of which the N-terminal dileucine-based motif is required for the predominant lysosomal targeting along the indirect pathway and clathrin-mediated endocytosis of CLN7	1366:1579	Our data demonstrate that CLN7 contains several cytoplasmic lysosomal targeting signals of which the N-terminal dileucine-based motif is required for the predominant lysosomal targeting along the indirect pathway and clathrin-mediated endocytosis of CLN7.
20406422	6	88	theme	surface	886:892	arg1	redistribution					894:907	cell surface redistribution	881:907	cell surface redistribution of CD4 chimeras	881:923	Mutation of these sorting motifs resulted in cell surface redistribution of CD4 chimeras.
20406422	4	89	theme	lysosomal	562:570	arg1	motifs					582:587	lysosomal targeting motifs	562:587	lysosomal targeting motifs	562:587	To identify lysosomal targeting motifs, we generated CD4-chimera fused to the N- and C-terminal domains of CLN7.
20406422	10	90	theme	several	1366:1372	arg1	signals					1406:1412	several cytoplasmic lysosomal targeting signals	1366:1412	several cytoplasmic lysosomal targeting signals of which the N-terminal dileucine-based motif is required for the predominant lysosomal targeting along the indirect pathway and clathrin-mediated endocytosis of CLN7	1366:1579	Our data demonstrate that CLN7 contains several cytoplasmic lysosomal targeting signals of which the N-terminal dileucine-based motif is required for the predominant lysosomal targeting along the indirect pathway and clathrin-mediated endocytosis of CLN7.
20406422	8	91	theme	plasma	1157:1162	arg1	membrane					1164:1171	the plasma membrane	1153:1171	the plasma membrane	1153:1171	Cell surface biotinylation revealed that at equilibrium 22% of total CLN7 is localized at the plasma membrane.
20406422	2	92	theme	mutational	340:349	arg1	analyses					351:358	mutational analyses	340:358	mutational analyses	340:358	In this study fluorescence protease protection assays and mutational analyses revealed the N- and C-terminal tails of CLN7 in the cytosol and two N-glycosylation sites at N371 and N376.
20406422	6	93	theme	motifs	862:867	arg1	Mutation					836:843	Mutation	836:843	Mutation of these sorting motifs	836:867	Mutation of these sorting motifs resulted in cell surface redistribution of CD4 chimeras.
20406422	3	94	dep	Both	468:471	arg1	partially					473:481	partially	473:481	partially	473:481	Both partially and non-glycosylated CLN7 were correctly transported to lysosomes.
20406422	4	95	theme	C-terminal	635:644	arg1	CLN7					657:660	CLN7	657:660	CLN7	657:660	To identify lysosomal targeting motifs, we generated CD4-chimera fused to the N- and C-terminal domains of CLN7.
20406422	4	95	theme	C-terminal	635:644	arg1	domains					646:652	C-terminal domains	635:652	C-terminal domains	635:652	To identify lysosomal targeting motifs, we generated CD4-chimera fused to the N- and C-terminal domains of CLN7.
20406422	9	96	theme	motif	1200:1204	arg1	Mutation					1174:1181	Mutation	1174:1181	Mutation of the dileucine motif	1174:1204	Mutation of the dileucine motif or the co-expression of dominant-negative mutant dynamin K44A led to a further increase of CLN7 at the plasma membrane.
20406422	9	96	theme	motif	1200:1204	arg1	co-expression					1213:1225	the co-expression	1209:1225	the co-expression of dominant-negative mutant dynamin K44A	1209:1266	Mutation of the dileucine motif or the co-expression of dominant-negative mutant dynamin K44A led to a further increase of CLN7 at the plasma membrane.
20406422	2	97	theme	C-terminal	380:389	arg1	tails					391:395	C-terminal tails	380:395	C-terminal tails	380:395	In this study fluorescence protease protection assays and mutational analyses revealed the N- and C-terminal tails of CLN7 in the cytosol and two N-glycosylation sites at N371 and N376.
20406422	1	98	theme	neurodegenerative	236:252	arg1	lipofuscinosis					218:231	variant late infantile neuronal ceroid lipofuscinosis	179:231	variant late infantile neuronal ceroid lipofuscinosis	179:231	CLN7 is a polytopic lysosomal membrane protein deficient in variant late infantile neuronal ceroid lipofuscinosis, a neurodegenerative lysosomal storage disorder.
20406422	1	98	theme	neurodegenerative	236:252	arg1	disorder					272:279	a neurodegenerative lysosomal storage disorder	234:279	a neurodegenerative lysosomal storage disorder	234:279	CLN7 is a polytopic lysosomal membrane protein deficient in variant late infantile neuronal ceroid lipofuscinosis, a neurodegenerative lysosomal storage disorder.
8940148	2	0	contain	contain	336:342	arg1	ankyrins					327:334	these ankyrins	321:334	these ankyrins	321:334	This study presents evidence that these ankyrins contain O-linked GlcNAc residues and identifies as the site of glycosylation a serine-rich domain that distinguishes them from other ankyrin isoforms.
8940148	2	0	contain	contain	336:342	arg2	residues					360:367	O-linked GlcNAc residues	344:367	O-linked GlcNAc residues	344:367	This study presents evidence that these ankyrins contain O-linked GlcNAc residues and identifies as the site of glycosylation a serine-rich domain that distinguishes them from other ankyrin isoforms.
8940148	5	1	theme	binding	986:992	arg1	activity					994:1001	wheat germ agglutinin binding activity	964:1001	wheat germ agglutinin binding activity of polypeptides produced by in vitro translation in reticulocyte lysates	964:1074	The serine-rich domain is the site of glycosylation based on wheat germ agglutinin binding activity of polypeptides produced by in vitro translation in reticulocyte lysates.
8940148	6	2	theme	ankyrinG	1124:1131	arg1	co-localization					1105:1119	co-localization	1105:1119	co-localization of ankyrinG and O-GlcNAc immunoreactivity	1105:1161	Immunofluorescence revealed co-localization of ankyrinG and O-GlcNAc immunoreactivity at nodes of Ranvier.
8940148	6	3	dep	ankyrinG	1124:1131	arg1	immunoreactivity					1146:1161	immunoreactivity	1146:1161	immunoreactivity	1146:1161	Immunofluorescence revealed co-localization of ankyrinG and O-GlcNAc immunoreactivity at nodes of Ranvier.
8940148	5	4	gly	glycosylation	941:953	arg2	domain					919:924	The serine-rich domain	903:924	The serine-rich domain	903:924	The serine-rich domain is the site of glycosylation based on wheat germ agglutinin binding activity of polypeptides produced by in vitro translation in reticulocyte lysates.
8940148	5	4	gly	glycosylation	941:953	arg2	glycosylation					941:953	glycosylation	941:953	glycosylation	941:953	The serine-rich domain is the site of glycosylation based on wheat germ agglutinin binding activity of polypeptides produced by in vitro translation in reticulocyte lysates.
8940148	5	4	gly	glycosylation	941:953	arg2	site					933:936	the site	929:936	the site of glycosylation based on wheat germ agglutinin binding activity of polypeptides produced by in vitro translation in reticulocyte lysates	929:1074	The serine-rich domain is the site of glycosylation based on wheat germ agglutinin binding activity of polypeptides produced by in vitro translation in reticulocyte lysates.
8940148	3	5	theme	brain	524:528	arg1	membranes					530:538	brain membranes	524:538	brain membranes associated with wheat germ agglutinin-affinity columns	524:593	The 480-kDa ankyrinG, extracted from brain membranes associated with wheat germ agglutinin-affinity columns, was [3H]galactose-labeled with UDP-[3H] galactose and galactosyltransferase, and cross-reacted with an antibody against O-GlcNAc monosaccharides.
8940148	2	6	link	O-linked	344:351	arg1	residues					360:367	O-linked GlcNAc residues	344:367	O-linked GlcNAc residues	344:367	This study presents evidence that these ankyrins contain O-linked GlcNAc residues and identifies as the site of glycosylation a serine-rich domain that distinguishes them from other ankyrin isoforms.
8940148	0	7	link	O-linked	18:25	arg1	N-acetylglucosamine					27:45	O-linked N-acetylglucosamine	18:45	O-linked N-acetylglucosamine modification of ankyrinG isoforms	18:79	Identification of O-linked N-acetylglucosamine modification of ankyrinG isoforms targeted to nodes of Ranvier.
8940148	3	8	theme	germ	562:565	arg1	columns					587:593	wheat germ agglutinin-affinity columns	556:593	wheat germ agglutinin-affinity columns	556:593	The 480-kDa ankyrinG, extracted from brain membranes associated with wheat germ agglutinin-affinity columns, was [3H]galactose-labeled with UDP-[3H] galactose and galactosyltransferase, and cross-reacted with an antibody against O-GlcNAc monosaccharides.
8940148	0	9	theme	Ranvier	102:108	arg1	nodes					93:97	nodes	93:97	nodes of Ranvier	93:108	Identification of O-linked N-acetylglucosamine modification of ankyrinG isoforms targeted to nodes of Ranvier.
8940148	1	10	located	localized	144:152	arg2	AnkyrinGs					111:119	AnkyrinGs	111:119	AnkyrinGs of 270 and 480 kDa	111:138	AnkyrinGs of 270 and 480 kDa are localized at nodes of Ranvier and are candidates to couple the voltage-dependent sodium channel and neurofascin to the spectrin/actin network.
8940148	1	10	located	localized	144:152	arg1	nodes					157:161	nodes	157:161	nodes of Ranvier	157:172	AnkyrinGs of 270 and 480 kDa are localized at nodes of Ranvier and are candidates to couple the voltage-dependent sodium channel and neurofascin to the spectrin/actin network.
8940148	7	11	theme	Ranvier	1239:1245	arg1	node					1231:1234	the node	1227:1234	the node of Ranvier	1227:1245	These observations suggest that ankyrin at the node of Ranvier is O-GlcNAc-glycosylated and are the first demonstration of a post-translational modification that is concentrated at the node of Ranvier and not in adjacent areas of myelinated axons.
8940148	3	12	theme	agglutinin-affinity	567:585	arg1	columns					587:593	wheat germ agglutinin-affinity columns	556:593	wheat germ agglutinin-affinity columns	556:593	The 480-kDa ankyrinG, extracted from brain membranes associated with wheat germ agglutinin-affinity columns, was [3H]galactose-labeled with UDP-[3H] galactose and galactosyltransferase, and cross-reacted with an antibody against O-GlcNAc monosaccharides.
8940148	5	13	dep	in	1031:1032	arg1	vitro					1034:1038	vitro	1034:1038	vitro	1034:1038	The serine-rich domain is the site of glycosylation based on wheat germ agglutinin binding activity of polypeptides produced by in vitro translation in reticulocyte lysates.
8940148	1	14	theme	spectrin/actin	263:276	arg1	network					278:284	the spectrin/actin network	259:284	the spectrin/actin network	259:284	AnkyrinGs of 270 and 480 kDa are localized at nodes of Ranvier and are candidates to couple the voltage-dependent sodium channel and neurofascin to the spectrin/actin network.
8940148	7	15	theme	modification	1328:1339	arg1	demonstration					1290:1302	the first demonstration	1280:1302	the first demonstration of a post-translational modification that is concentrated at the node of Ranvier and not in adjacent areas of myelinated axons	1280:1429	These observations suggest that ankyrin at the node of Ranvier is O-GlcNAc-glycosylated and are the first demonstration of a post-translational modification that is concentrated at the node of Ranvier and not in adjacent areas of myelinated axons.
8940148	4	16	theme	O-linked	773:780	arg1	sugars					762:767	AnkyrinG-associated sugars	742:767	AnkyrinG-associated sugars	742:767	AnkyrinG-associated sugars are O-linked monosaccharides based on resistance to peptide-N-glycosidase F and analysis of saccharides released by beta-elimination.
8940148	4	16	theme	O-linked	773:780	arg1	monosaccharides					782:796	O-linked monosaccharides	773:796	O-linked monosaccharides based on resistance to peptide-N-glycosidase F and analysis of saccharides released by beta-elimination	773:900	AnkyrinG-associated sugars are O-linked monosaccharides based on resistance to peptide-N-glycosidase F and analysis of saccharides released by beta-elimination.
8940148	4	17	link	O-linked	773:780	arg1	sugars					762:767	AnkyrinG-associated sugars	742:767	AnkyrinG-associated sugars	742:767	AnkyrinG-associated sugars are O-linked monosaccharides based on resistance to peptide-N-glycosidase F and analysis of saccharides released by beta-elimination.
8940148	4	17	link	O-linked	773:780	arg1	monosaccharides					782:796	O-linked monosaccharides	773:796	O-linked monosaccharides based on resistance to peptide-N-glycosidase F and analysis of saccharides released by beta-elimination	773:900	AnkyrinG-associated sugars are O-linked monosaccharides based on resistance to peptide-N-glycosidase F and analysis of saccharides released by beta-elimination.
8940148	2	18	theme	glycosylation	399:411	arg1	glycosylation					399:411	glycosylation	399:411	glycosylation	399:411	This study presents evidence that these ankyrins contain O-linked GlcNAc residues and identifies as the site of glycosylation a serine-rich domain that distinguishes them from other ankyrin isoforms.
8940148	2	18	theme	glycosylation	399:411	arg1	domain					427:432	a serine-rich domain	413:432	a serine-rich domain that distinguishes them from other ankyrin isoforms	413:484	This study presents evidence that these ankyrins contain O-linked GlcNAc residues and identifies as the site of glycosylation a serine-rich domain that distinguishes them from other ankyrin isoforms.
8940148	2	18	theme	glycosylation	399:411	arg1	site					391:394	the site	387:394	the site of glycosylation	387:411	This study presents evidence that these ankyrins contain O-linked GlcNAc residues and identifies as the site of glycosylation a serine-rich domain that distinguishes them from other ankyrin isoforms.
8940148	2	19	theme	ankyrin	469:475	arg1	isoforms					477:484	other ankyrin isoforms	463:484	other ankyrin isoforms	463:484	This study presents evidence that these ankyrins contain O-linked GlcNAc residues and identifies as the site of glycosylation a serine-rich domain that distinguishes them from other ankyrin isoforms.
8940148	2	20	gly	glycosylation	399:411	arg2	domain					427:432	a serine-rich domain	413:432	a serine-rich domain that distinguishes them from other ankyrin isoforms	413:484	This study presents evidence that these ankyrins contain O-linked GlcNAc residues and identifies as the site of glycosylation a serine-rich domain that distinguishes them from other ankyrin isoforms.
8940148	2	20	gly	glycosylation	399:411	arg2	glycosylation					399:411	glycosylation	399:411	glycosylation	399:411	This study presents evidence that these ankyrins contain O-linked GlcNAc residues and identifies as the site of glycosylation a serine-rich domain that distinguishes them from other ankyrin isoforms.
8940148	2	20	gly	glycosylation	399:411	arg2	site					391:394	the site	387:394	the site of glycosylation	387:411	This study presents evidence that these ankyrins contain O-linked GlcNAc residues and identifies as the site of glycosylation a serine-rich domain that distinguishes them from other ankyrin isoforms.
8940148	3	21	theme	wheat	556:560	arg1	columns					587:593	wheat germ agglutinin-affinity columns	556:593	wheat germ agglutinin-affinity columns	556:593	The 480-kDa ankyrinG, extracted from brain membranes associated with wheat germ agglutinin-affinity columns, was [3H]galactose-labeled with UDP-[3H] galactose and galactosyltransferase, and cross-reacted with an antibody against O-GlcNAc monosaccharides.
8940148	1	22	theme	Ranvier	166:172	arg1	nodes					157:161	nodes	157:161	nodes of Ranvier	157:172	AnkyrinGs of 270 and 480 kDa are localized at nodes of Ranvier and are candidates to couple the voltage-dependent sodium channel and neurofascin to the spectrin/actin network.
8940148	2	23	theme	other	463:467	arg1	isoforms					477:484	other ankyrin isoforms	463:484	other ankyrin isoforms	463:484	This study presents evidence that these ankyrins contain O-linked GlcNAc residues and identifies as the site of glycosylation a serine-rich domain that distinguishes them from other ankyrin isoforms.
8940148	7	24	from	node	1231:1234	arg1	ankyrin					1216:1222	ankyrin	1216:1222	ankyrin at the node of Ranvier	1216:1245	These observations suggest that ankyrin at the node of Ranvier is O-GlcNAc-glycosylated and are the first demonstration of a post-translational modification that is concentrated at the node of Ranvier and not in adjacent areas of myelinated axons.
8940148	5	25	theme	in	1031:1032	arg1	translation					1040:1050	in vitro translation	1031:1050	in vitro translation in reticulocyte lysates	1031:1074	The serine-rich domain is the site of glycosylation based on wheat germ agglutinin binding activity of polypeptides produced by in vitro translation in reticulocyte lysates.
8940148	7	26	theme	post-translational	1309:1326	arg1	modification					1328:1339	a post-translational modification	1307:1339	a post-translational modification that is concentrated at the node of Ranvier and not in adjacent areas of myelinated axons	1307:1429	These observations suggest that ankyrin at the node of Ranvier is O-GlcNAc-glycosylated and are the first demonstration of a post-translational modification that is concentrated at the node of Ranvier and not in adjacent areas of myelinated axons.
8940148	5	27	theme	glycosylation	941:953	arg1	site					933:936	the site	929:936	the site of glycosylation based on wheat germ agglutinin binding activity of polypeptides produced by in vitro translation in reticulocyte lysates	929:1074	The serine-rich domain is the site of glycosylation based on wheat germ agglutinin binding activity of polypeptides produced by in vitro translation in reticulocyte lysates.
8940148	5	27	theme	glycosylation	941:953	arg1	glycosylation					941:953	glycosylation	941:953	glycosylation	941:953	The serine-rich domain is the site of glycosylation based on wheat germ agglutinin binding activity of polypeptides produced by in vitro translation in reticulocyte lysates.
8940148	5	27	theme	glycosylation	941:953	arg1	domain					919:924	The serine-rich domain	903:924	The serine-rich domain	903:924	The serine-rich domain is the site of glycosylation based on wheat germ agglutinin binding activity of polypeptides produced by in vitro translation in reticulocyte lysates.
8940148	5	28	theme	wheat	964:968	arg1	agglutinin					975:984	wheat germ agglutinin	964:984	wheat germ agglutinin binding activity of polypeptides produced by in vitro translation in reticulocyte lysates	964:1074	The serine-rich domain is the site of glycosylation based on wheat germ agglutinin binding activity of polypeptides produced by in vitro translation in reticulocyte lysates.
8940148	0	29	theme	N-acetylglucosamine	27:45	arg1	modification					47:58	O-linked N-acetylglucosamine modification	18:58	O-linked N-acetylglucosamine modification of ankyrinG isoforms	18:79	Identification of O-linked N-acetylglucosamine modification of ankyrinG isoforms targeted to nodes of Ranvier.
8940148	4	30	theme	peptide-N-glycosidase	821:841	arg1	F					843:843	peptide-N-glycosidase F	821:843	peptide-N-glycosidase F	821:843	AnkyrinG-associated sugars are O-linked monosaccharides based on resistance to peptide-N-glycosidase F and analysis of saccharides released by beta-elimination.
8940148	5	31	theme	reticulocyte	1055:1066	arg1	lysates					1068:1074	reticulocyte lysates	1055:1074	reticulocyte lysates	1055:1074	The serine-rich domain is the site of glycosylation based on wheat germ agglutinin binding activity of polypeptides produced by in vitro translation in reticulocyte lysates.
8940148	0	32	theme	O-linked	18:25	arg1	N-acetylglucosamine					27:45	O-linked N-acetylglucosamine	18:45	O-linked N-acetylglucosamine modification of ankyrinG isoforms	18:79	Identification of O-linked N-acetylglucosamine modification of ankyrinG isoforms targeted to nodes of Ranvier.
8940148	0	33	mod	modification	47:58	arg3	N-acetylglucosamine					27:45	O-linked N-acetylglucosamine	18:45	O-linked N-acetylglucosamine modification of ankyrinG isoforms	18:79	Identification of O-linked N-acetylglucosamine modification of ankyrinG isoforms targeted to nodes of Ranvier.
8940148	0	33	mod	modification	47:58	arg1	isoforms					72:79	ankyrinG isoforms	63:79	ankyrinG isoforms	63:79	Identification of O-linked N-acetylglucosamine modification of ankyrinG isoforms targeted to nodes of Ranvier.
8940148	4	34	theme	AnkyrinG-associated	742:760	arg1	sugars					762:767	AnkyrinG-associated sugars	742:767	AnkyrinG-associated sugars	742:767	AnkyrinG-associated sugars are O-linked monosaccharides based on resistance to peptide-N-glycosidase F and analysis of saccharides released by beta-elimination.
8940148	4	34	theme	AnkyrinG-associated	742:760	arg1	monosaccharides					782:796	O-linked monosaccharides	773:796	O-linked monosaccharides based on resistance to peptide-N-glycosidase F and analysis of saccharides released by beta-elimination	773:900	AnkyrinG-associated sugars are O-linked monosaccharides based on resistance to peptide-N-glycosidase F and analysis of saccharides released by beta-elimination.
8940148	6	35	theme	Ranvier	1175:1181	arg1	nodes					1166:1170	nodes	1166:1170	nodes of Ranvier	1166:1181	Immunofluorescence revealed co-localization of ankyrinG and O-GlcNAc immunoreactivity at nodes of Ranvier.
8940148	5	36	theme	polypeptides	1006:1017	arg1	activity					994:1001	wheat germ agglutinin binding activity	964:1001	wheat germ agglutinin binding activity of polypeptides produced by in vitro translation in reticulocyte lysates	964:1074	The serine-rich domain is the site of glycosylation based on wheat germ agglutinin binding activity of polypeptides produced by in vitro translation in reticulocyte lysates.
8940148	7	37	theme	axons	1425:1429	arg1	areas					1405:1409	adjacent areas	1396:1409	adjacent areas of myelinated axons	1396:1429	These observations suggest that ankyrin at the node of Ranvier is O-GlcNAc-glycosylated and are the first demonstration of a post-translational modification that is concentrated at the node of Ranvier and not in adjacent areas of myelinated axons.
8940148	2	38	theme	serine-rich	415:425	arg1	glycosylation					399:411	glycosylation	399:411	glycosylation	399:411	This study presents evidence that these ankyrins contain O-linked GlcNAc residues and identifies as the site of glycosylation a serine-rich domain that distinguishes them from other ankyrin isoforms.
8940148	2	38	theme	serine-rich	415:425	arg1	domain					427:432	a serine-rich domain	413:432	a serine-rich domain that distinguishes them from other ankyrin isoforms	413:484	This study presents evidence that these ankyrins contain O-linked GlcNAc residues and identifies as the site of glycosylation a serine-rich domain that distinguishes them from other ankyrin isoforms.
8940148	2	38	theme	serine-rich	415:425	arg1	site					391:394	the site	387:394	the site of glycosylation	387:411	This study presents evidence that these ankyrins contain O-linked GlcNAc residues and identifies as the site of glycosylation a serine-rich domain that distinguishes them from other ankyrin isoforms.
8940148	0	39	theme	modification	47:58	arg1	Identification					0:13	Identification	0:13	Identification of O-linked N-acetylglucosamine modification of ankyrinG isoforms	0:79	Identification of O-linked N-acetylglucosamine modification of ankyrinG isoforms targeted to nodes of Ranvier.
8940148	7	40	theme	first	1284:1288	arg1	demonstration					1290:1302	the first demonstration	1280:1302	the first demonstration of a post-translational modification that is concentrated at the node of Ranvier and not in adjacent areas of myelinated axons	1280:1429	These observations suggest that ankyrin at the node of Ranvier is O-GlcNAc-glycosylated and are the first demonstration of a post-translational modification that is concentrated at the node of Ranvier and not in adjacent areas of myelinated axons.
8940148	5	41	theme	serine-rich	907:917	arg1	site					933:936	the site	929:936	the site of glycosylation based on wheat germ agglutinin binding activity of polypeptides produced by in vitro translation in reticulocyte lysates	929:1074	The serine-rich domain is the site of glycosylation based on wheat germ agglutinin binding activity of polypeptides produced by in vitro translation in reticulocyte lysates.
8940148	5	41	theme	serine-rich	907:917	arg1	glycosylation					941:953	glycosylation	941:953	glycosylation	941:953	The serine-rich domain is the site of glycosylation based on wheat germ agglutinin binding activity of polypeptides produced by in vitro translation in reticulocyte lysates.
8940148	5	41	theme	serine-rich	907:917	arg1	domain					919:924	The serine-rich domain	903:924	The serine-rich domain	903:924	The serine-rich domain is the site of glycosylation based on wheat germ agglutinin binding activity of polypeptides produced by in vitro translation in reticulocyte lysates.
8940148	0	42	theme	isoforms	72:79	arg1	modification					47:58	O-linked N-acetylglucosamine modification	18:58	O-linked N-acetylglucosamine modification of ankyrinG isoforms	18:79	Identification of O-linked N-acetylglucosamine modification of ankyrinG isoforms targeted to nodes of Ranvier.
8940148	2	43	theme	GlcNAc	353:358	arg1	residues					360:367	O-linked GlcNAc residues	344:367	O-linked GlcNAc residues	344:367	This study presents evidence that these ankyrins contain O-linked GlcNAc residues and identifies as the site of glycosylation a serine-rich domain that distinguishes them from other ankyrin isoforms.
8940148	0	44	theme	ankyrinG	63:70	arg1	isoforms					72:79	ankyrinG isoforms	63:79	ankyrinG isoforms	63:79	Identification of O-linked N-acetylglucosamine modification of ankyrinG isoforms targeted to nodes of Ranvier.
8940148	2	45	theme	O-linked	344:351	arg1	residues					360:367	O-linked GlcNAc residues	344:367	O-linked GlcNAc residues	344:367	This study presents evidence that these ankyrins contain O-linked GlcNAc residues and identifies as the site of glycosylation a serine-rich domain that distinguishes them from other ankyrin isoforms.
8940148	5	46	from	translation	1040:1050	arg1	lysates					1068:1074	reticulocyte lysates	1055:1074	reticulocyte lysates	1055:1074	The serine-rich domain is the site of glycosylation based on wheat germ agglutinin binding activity of polypeptides produced by in vitro translation in reticulocyte lysates.
8940148	3	47	theme	O-GlcNAc	716:723	arg1	monosaccharides					725:739	O-GlcNAc monosaccharides	716:739	O-GlcNAc monosaccharides	716:739	The 480-kDa ankyrinG, extracted from brain membranes associated with wheat germ agglutinin-affinity columns, was [3H]galactose-labeled with UDP-[3H] galactose and galactosyltransferase, and cross-reacted with an antibody against O-GlcNAc monosaccharides.
8940148	3	48	theme	480-kDa	491:497	arg1	ankyrinG					499:506	The 480-kDa ankyrinG	487:506	The 480-kDa ankyrinG	487:506	The 480-kDa ankyrinG, extracted from brain membranes associated with wheat germ agglutinin-affinity columns, was [3H]galactose-labeled with UDP-[3H] galactose and galactosyltransferase, and cross-reacted with an antibody against O-GlcNAc monosaccharides.
8940148	3	48	theme	480-kDa	491:497	arg1	galactose-labeled					604:620	galactose-labeled	604:620	galactose-labeled	604:620	The 480-kDa ankyrinG, extracted from brain membranes associated with wheat germ agglutinin-affinity columns, was [3H]galactose-labeled with UDP-[3H] galactose and galactosyltransferase, and cross-reacted with an antibody against O-GlcNAc monosaccharides.
8940148	1	49	theme	voltage-dependent	207:223	arg1	channel					232:238	the voltage-dependent sodium channel	203:238	the voltage-dependent sodium channel	203:238	AnkyrinGs of 270 and 480 kDa are localized at nodes of Ranvier and are candidates to couple the voltage-dependent sodium channel and neurofascin to the spectrin/actin network.
8940148	4	50	theme	saccharides	861:871	arg1	analysis					849:856	analysis	849:856	analysis of saccharides released by beta-elimination	849:900	AnkyrinG-associated sugars are O-linked monosaccharides based on resistance to peptide-N-glycosidase F and analysis of saccharides released by beta-elimination.
8940148	4	50	theme	saccharides	861:871	arg1	resistance					807:816	resistance	807:816	resistance to peptide-N-glycosidase F	807:843	AnkyrinG-associated sugars are O-linked monosaccharides based on resistance to peptide-N-glycosidase F and analysis of saccharides released by beta-elimination.
8940148	1	51	theme	kDa	136:138	arg1	AnkyrinGs					111:119	AnkyrinGs	111:119	AnkyrinGs of 270 and 480 kDa	111:138	AnkyrinGs of 270 and 480 kDa are localized at nodes of Ranvier and are candidates to couple the voltage-dependent sodium channel and neurofascin to the spectrin/actin network.
8940148	1	52	theme	sodium	225:230	arg1	channel					232:238	the voltage-dependent sodium channel	203:238	the voltage-dependent sodium channel	203:238	AnkyrinGs of 270 and 480 kDa are localized at nodes of Ranvier and are candidates to couple the voltage-dependent sodium channel and neurofascin to the spectrin/actin network.
8940148	7	53	gly	O-GlcNAc-glycosylated	1250:1270	arg1	ankyrin					1216:1222	ankyrin	1216:1222	ankyrin at the node of Ranvier	1216:1245	These observations suggest that ankyrin at the node of Ranvier is O-GlcNAc-glycosylated and are the first demonstration of a post-translational modification that is concentrated at the node of Ranvier and not in adjacent areas of myelinated axons.
8940148	5	54	theme	germ	970:973	arg1	agglutinin					975:984	wheat germ agglutinin	964:984	wheat germ agglutinin binding activity of polypeptides produced by in vitro translation in reticulocyte lysates	964:1074	The serine-rich domain is the site of glycosylation based on wheat germ agglutinin binding activity of polypeptides produced by in vitro translation in reticulocyte lysates.
8940148	6	55	theme	O-GlcNAc	1137:1144	arg1	co-localization					1105:1119	co-localization	1105:1119	co-localization of ankyrinG and O-GlcNAc immunoreactivity	1105:1161	Immunofluorescence revealed co-localization of ankyrinG and O-GlcNAc immunoreactivity at nodes of Ranvier.
8940148	7	56	theme	myelinated	1414:1423	arg1	axons					1425:1429	myelinated axons	1414:1429	myelinated axons	1414:1429	These observations suggest that ankyrin at the node of Ranvier is O-GlcNAc-glycosylated and are the first demonstration of a post-translational modification that is concentrated at the node of Ranvier and not in adjacent areas of myelinated axons.
8940148	7	57	theme	adjacent	1396:1403	arg1	areas					1405:1409	adjacent areas	1396:1409	adjacent areas of myelinated axons	1396:1429	These observations suggest that ankyrin at the node of Ranvier is O-GlcNAc-glycosylated and are the first demonstration of a post-translational modification that is concentrated at the node of Ranvier and not in adjacent areas of myelinated axons.
8940148	5	58	theme	agglutinin	975:984	arg1	activity					994:1001	wheat germ agglutinin binding activity	964:1001	wheat germ agglutinin binding activity of polypeptides produced by in vitro translation in reticulocyte lysates	964:1074	The serine-rich domain is the site of glycosylation based on wheat germ agglutinin binding activity of polypeptides produced by in vitro translation in reticulocyte lysates.
8940148	7	59	theme	Ranvier	1377:1383	arg1	node					1369:1372	the node	1365:1372	the node of Ranvier	1365:1383	These observations suggest that ankyrin at the node of Ranvier is O-GlcNAc-glycosylated and are the first demonstration of a post-translational modification that is concentrated at the node of Ranvier and not in adjacent areas of myelinated axons.
8940148	3	60	with	galactose-labeled	604:620	arg1	galactose					636:644	UDP-[3H] galactose	627:644	UDP-[3H] galactose	627:644	The 480-kDa ankyrinG, extracted from brain membranes associated with wheat germ agglutinin-affinity columns, was [3H]galactose-labeled with UDP-[3H] galactose and galactosyltransferase, and cross-reacted with an antibody against O-GlcNAc monosaccharides.
8940148	3	60	with	galactose-labeled	604:620	arg1	galactosyltransferase					650:670	galactosyltransferase	650:670	galactosyltransferase	650:670	The 480-kDa ankyrinG, extracted from brain membranes associated with wheat germ agglutinin-affinity columns, was [3H]galactose-labeled with UDP-[3H] galactose and galactosyltransferase, and cross-reacted with an antibody against O-GlcNAc monosaccharides.
17956937	4	0	theme	complexed	817:825	arg1	molecules					827:835	the free and complexed molecules	804:835	the free and complexed molecules	804:835	The profiles of the PSA N-glycans from the free and complexed molecules were quite similar to each other and consisted of fucosylated biantennary oligosaccharides as the major class.
17956937	0	1	theme	glycopeptide	150:161	arg1	approach					163:170	a glycopeptide approach	148:170	a glycopeptide approach	148:170	Oligosaccharide profiles of the prostate specific antigen in free and complexed forms from the prostate cancer patient serum and in seminal plasma: a glycopeptide approach.
17956937	8	2	theme	alpha2,3-linked	1668:1682	arg1	acids					1691:1695	alpha2,3-linked sialic acids	1668:1695	alpha2,3-linked sialic acids	1668:1695	The results suggest that identification of alpha2,3-linked sialic acids on PSA potentially discriminates malignant from benign conditions, if the analysis is applied to oligosaccharides specifically attached to the N-glycosylation site of PSA in either a free or a complexed form in the serum.
17956937	6	3	attach	attached	1241:1248	arg2	alpha2,6-linked					1324:1338	alpha2,6-linked	1324:1338	alpha2,6-linked	1324:1338	In the seminal plasma PSA, high-mannose and hybrid types of oligosaccharides were predominant, and the sialic acids attached to the latter as well as to biantennary oligosaccahrides were exclusively alpha2,6-linked because they were removed by Arthrobacter ureafaciens neuraminidase but resistant to S. pneumoniae neuraminidase.
17956937	6	3	attach	attached	1241:1248	arg1	latter					1257:1262	latter	1257:1262	latter	1257:1262	In the seminal plasma PSA, high-mannose and hybrid types of oligosaccharides were predominant, and the sialic acids attached to the latter as well as to biantennary oligosaccahrides were exclusively alpha2,6-linked because they were removed by Arthrobacter ureafaciens neuraminidase but resistant to S. pneumoniae neuraminidase.
17956937	6	3	attach	attached	1241:1248	arg1	oligosaccahrides					1290:1305	biantennary oligosaccahrides	1278:1305	biantennary oligosaccahrides	1278:1305	In the seminal plasma PSA, high-mannose and hybrid types of oligosaccharides were predominant, and the sialic acids attached to the latter as well as to biantennary oligosaccahrides were exclusively alpha2,6-linked because they were removed by Arthrobacter ureafaciens neuraminidase but resistant to S. pneumoniae neuraminidase.
17956937	6	3	attach	attached	1241:1248	arg2	acids					1235:1239	the sialic acids	1224:1239	the sialic acids attached to the latter as well as to biantennary oligosaccahrides	1224:1305	In the seminal plasma PSA, high-mannose and hybrid types of oligosaccharides were predominant, and the sialic acids attached to the latter as well as to biantennary oligosaccahrides were exclusively alpha2,6-linked because they were removed by Arthrobacter ureafaciens neuraminidase but resistant to S. pneumoniae neuraminidase.
17956937	4	4	theme	free	808:811	arg1	molecules					827:835	the free and complexed molecules	804:835	the free and complexed molecules	804:835	The profiles of the PSA N-glycans from the free and complexed molecules were quite similar to each other and consisted of fucosylated biantennary oligosaccharides as the major class.
17956937	6	5	theme	plasma	1140:1145	arg1	PSA					1147:1149	the seminal plasma PSA	1128:1149	the seminal plasma PSA	1128:1149	In the seminal plasma PSA, high-mannose and hybrid types of oligosaccharides were predominant, and the sialic acids attached to the latter as well as to biantennary oligosaccahrides were exclusively alpha2,6-linked because they were removed by Arthrobacter ureafaciens neuraminidase but resistant to S. pneumoniae neuraminidase.
17956937	5	6	gly	glycopeptides	1110:1122	arg2	glycopeptides					1110:1122	the glycopeptides	1106:1122	the glycopeptides	1106:1122	They were mostly sialylated, and a considerable sialic acid fraction was alpha2,3-linked as determined by Streptococcus pneumoniae neuraminidase digestion of the glycopeptides.
17956937	8	7	theme	complexed	1890:1898	arg1	form					1900:1903	a complexed form	1888:1903	a complexed form in the serum	1888:1916	The results suggest that identification of alpha2,3-linked sialic acids on PSA potentially discriminates malignant from benign conditions, if the analysis is applied to oligosaccharides specifically attached to the N-glycosylation site of PSA in either a free or a complexed form in the serum.
17956937	8	8	from	site	1856:1859	arg1	free					1880:1883	free	1880:1883	free	1880:1883	The results suggest that identification of alpha2,3-linked sialic acids on PSA potentially discriminates malignant from benign conditions, if the analysis is applied to oligosaccharides specifically attached to the N-glycosylation site of PSA in either a free or a complexed form in the serum.
17956937	8	8	from	site	1856:1859	arg1	form					1900:1903	a complexed form	1888:1903	a complexed form in the serum	1888:1916	The results suggest that identification of alpha2,3-linked sialic acids on PSA potentially discriminates malignant from benign conditions, if the analysis is applied to oligosaccharides specifically attached to the N-glycosylation site of PSA in either a free or a complexed form in the serum.
17956937	3	9	theme	lysylendopeptidase	671:688	arg1	digestion					690:698	lysylendopeptidase digestion	671:698	lysylendopeptidase digestion of the electrophoretically separated PSA with mass spectrometry	671:762	In the present study, the glycan profiles of free and complexed forms of PSA from cancer patient serum and of seminal plasma PSA were compared by analyzing the glycopeptides obtained by lysylendopeptidase digestion of the electrophoretically separated PSA with mass spectrometry.
17956937	0	10	theme	patient	111:117	arg1	serum					119:123	the prostate cancer patient serum	91:123	the prostate cancer patient serum	91:123	Oligosaccharide profiles of the prostate specific antigen in free and complexed forms from the prostate cancer patient serum and in seminal plasma: a glycopeptide approach.
17956937	3	11	theme	PSA	737:739	arg1	digestion					690:698	lysylendopeptidase digestion	671:698	lysylendopeptidase digestion of the electrophoretically separated PSA with mass spectrometry	671:762	In the present study, the glycan profiles of free and complexed forms of PSA from cancer patient serum and of seminal plasma PSA were compared by analyzing the glycopeptides obtained by lysylendopeptidase digestion of the electrophoretically separated PSA with mass spectrometry.
17956937	3	12	theme	complexed	539:547	arg1	forms					549:553	free and complexed forms	530:553	free and complexed forms of PSA from cancer patient serum	530:586	In the present study, the glycan profiles of free and complexed forms of PSA from cancer patient serum and of seminal plasma PSA were compared by analyzing the glycopeptides obtained by lysylendopeptidase digestion of the electrophoretically separated PSA with mass spectrometry.
17956937	2	13	with	complex	413:419	arg1	-antichymotrypsin					450:466	alpha(1)-antichymotrypsin	442:466	alpha(1)-antichymotrypsin	442:466	A large proportion of PSA forms a covalent complex with a glycoprotein, alpha(1)-antichymotrypsin, in human blood.
17956937	2	13	with	complex	413:419	arg1	glycoprotein					428:439	a glycoprotein	426:439	a glycoprotein	426:439	A large proportion of PSA forms a covalent complex with a glycoprotein, alpha(1)-antichymotrypsin, in human blood.
17956937	1	14	theme	prostate	207:214	arg1	PSA					234:236	PSA	234:236	PSA	234:236	The oligosaccharide structures of prostate specific antigen (PSA) are expected to be useful in discriminating prostate cancer from benign conditions both accompanied by increased serum PSA levels.
17956937	1	14	theme	prostate	207:214	arg1	antigen					225:231	prostate specific antigen	207:231	prostate specific antigen (PSA)	207:237	The oligosaccharide structures of prostate specific antigen (PSA) are expected to be useful in discriminating prostate cancer from benign conditions both accompanied by increased serum PSA levels.
17956937	0	15	theme	seminal	132:138	arg1	plasma					140:145	seminal plasma	132:145	seminal plasma	132:145	Oligosaccharide profiles of the prostate specific antigen in free and complexed forms from the prostate cancer patient serum and in seminal plasma: a glycopeptide approach.
17956937	5	16	theme	sialic	996:1001	arg1	fraction					1008:1015	a considerable sialic acid fraction	981:1015	a considerable sialic acid fraction	981:1015	They were mostly sialylated, and a considerable sialic acid fraction was alpha2,3-linked as determined by Streptococcus pneumoniae neuraminidase digestion of the glycopeptides.
17956937	5	16	theme	sialic	996:1001	arg1	alpha2,3-linked					1021:1035	alpha2,3-linked	1021:1035	alpha2,3-linked	1021:1035	They were mostly sialylated, and a considerable sialic acid fraction was alpha2,3-linked as determined by Streptococcus pneumoniae neuraminidase digestion of the glycopeptides.
17956937	3	17	theme	free	530:533	arg1	forms					549:553	free and complexed forms	530:553	free and complexed forms of PSA from cancer patient serum	530:586	In the present study, the glycan profiles of free and complexed forms of PSA from cancer patient serum and of seminal plasma PSA were compared by analyzing the glycopeptides obtained by lysylendopeptidase digestion of the electrophoretically separated PSA with mass spectrometry.
17956937	8	18	link	alpha2,3-linked	1668:1682	arg1	acids					1691:1695	alpha2,3-linked sialic acids	1668:1695	alpha2,3-linked sialic acids	1668:1695	The results suggest that identification of alpha2,3-linked sialic acids on PSA potentially discriminates malignant from benign conditions, if the analysis is applied to oligosaccharides specifically attached to the N-glycosylation site of PSA in either a free or a complexed form in the serum.
17956937	6	19	theme	oligosaccharides	1185:1200	arg1	types					1176:1180	high-mannose and hybrid types	1152:1180	high-mannose and hybrid types of oligosaccharides	1152:1200	In the seminal plasma PSA, high-mannose and hybrid types of oligosaccharides were predominant, and the sialic acids attached to the latter as well as to biantennary oligosaccahrides were exclusively alpha2,6-linked because they were removed by Arthrobacter ureafaciens neuraminidase but resistant to S. pneumoniae neuraminidase.
17956937	4	20	theme	major	935:939	arg1	class					941:945	the major class	931:945	the major class	931:945	The profiles of the PSA N-glycans from the free and complexed molecules were quite similar to each other and consisted of fucosylated biantennary oligosaccharides as the major class.
17956937	3	21	theme	mass	746:749	arg1	spectrometry					751:762	mass spectrometry	746:762	mass spectrometry	746:762	In the present study, the glycan profiles of free and complexed forms of PSA from cancer patient serum and of seminal plasma PSA were compared by analyzing the glycopeptides obtained by lysylendopeptidase digestion of the electrophoretically separated PSA with mass spectrometry.
17956937	6	22	theme	ureafaciens	1382:1392	arg1	neuraminidase					1394:1406	Arthrobacter ureafaciens neuraminidase	1369:1406	Arthrobacter ureafaciens neuraminidase	1369:1406	In the seminal plasma PSA, high-mannose and hybrid types of oligosaccharides were predominant, and the sialic acids attached to the latter as well as to biantennary oligosaccahrides were exclusively alpha2,6-linked because they were removed by Arthrobacter ureafaciens neuraminidase but resistant to S. pneumoniae neuraminidase.
17956937	1	23	dep	discriminating	268:281	arg1	both					322:325	both	322:325	both	322:325	The oligosaccharide structures of prostate specific antigen (PSA) are expected to be useful in discriminating prostate cancer from benign conditions both accompanied by increased serum PSA levels.
17956937	0	24	theme	complexed	70:78	arg1	forms					80:84	free and complexed forms	61:84	free and complexed forms from the prostate cancer patient serum	61:123	Oligosaccharide profiles of the prostate specific antigen in free and complexed forms from the prostate cancer patient serum and in seminal plasma: a glycopeptide approach.
17956937	5	25	theme	glycopeptides	1110:1122	arg1	digestion					1093:1101	Streptococcus pneumoniae neuraminidase digestion	1054:1101	Streptococcus pneumoniae neuraminidase digestion of the glycopeptides	1054:1122	They were mostly sialylated, and a considerable sialic acid fraction was alpha2,3-linked as determined by Streptococcus pneumoniae neuraminidase digestion of the glycopeptides.
17956937	8	26	theme	PSA	1864:1866	arg1	PSA					1864:1866	PSA	1864:1866	PSA	1864:1866	The results suggest that identification of alpha2,3-linked sialic acids on PSA potentially discriminates malignant from benign conditions, if the analysis is applied to oligosaccharides specifically attached to the N-glycosylation site of PSA in either a free or a complexed form in the serum.
17956937	8	26	theme	PSA	1864:1866	arg1	site					1856:1859	the N-glycosylation site	1836:1859	the N-glycosylation site of PSA in either a free or a complexed form in the serum	1836:1916	The results suggest that identification of alpha2,3-linked sialic acids on PSA potentially discriminates malignant from benign conditions, if the analysis is applied to oligosaccharides specifically attached to the N-glycosylation site of PSA in either a free or a complexed form in the serum.
17956937	4	27	theme	biantennary	899:909	arg1	oligosaccharides					911:926	fucosylated biantennary oligosaccharides	887:926	fucosylated biantennary oligosaccharides	887:926	The profiles of the PSA N-glycans from the free and complexed molecules were quite similar to each other and consisted of fucosylated biantennary oligosaccharides as the major class.
17956937	8	28	from	form	1900:1903	arg1	serum					1912:1916	the serum	1908:1916	the serum	1908:1916	The results suggest that identification of alpha2,3-linked sialic acids on PSA potentially discriminates malignant from benign conditions, if the analysis is applied to oligosaccharides specifically attached to the N-glycosylation site of PSA in either a free or a complexed form in the serum.
17956937	1	29	theme	increased	342:350	arg1	levels					362:367	increased serum PSA levels	342:367	increased serum PSA levels	342:367	The oligosaccharide structures of prostate specific antigen (PSA) are expected to be useful in discriminating prostate cancer from benign conditions both accompanied by increased serum PSA levels.
17956937	7	30	theme	Complex-type	1454:1465	arg1	oligosaccharides					1467:1482	Complex-type oligosaccharides	1454:1482	Complex-type oligosaccharides from other sources	1454:1501	Complex-type oligosaccharides from other sources were found in the seminal plasma sample, indicating that analysis of released glycans carries a risk of being misleading.
17956937	7	31	theme	glycans	1581:1587	arg1	analysis					1560:1567	analysis	1560:1567	analysis of released glycans	1560:1587	Complex-type oligosaccharides from other sources were found in the seminal plasma sample, indicating that analysis of released glycans carries a risk of being misleading.
17956937	2	32	theme	human	472:476	arg1	blood					478:482	human blood	472:482	human blood	472:482	A large proportion of PSA forms a covalent complex with a glycoprotein, alpha(1)-antichymotrypsin, in human blood.
17956937	6	33	from	PSA	1147:1149	arg1	predominant					1207:1217	predominant	1207:1217	predominant	1207:1217	In the seminal plasma PSA, high-mannose and hybrid types of oligosaccharides were predominant, and the sialic acids attached to the latter as well as to biantennary oligosaccahrides were exclusively alpha2,6-linked because they were removed by Arthrobacter ureafaciens neuraminidase but resistant to S. pneumoniae neuraminidase.
17956937	0	34	theme	prostate	95:102	arg1	serum					119:123	the prostate cancer patient serum	91:123	the prostate cancer patient serum	91:123	Oligosaccharide profiles of the prostate specific antigen in free and complexed forms from the prostate cancer patient serum and in seminal plasma: a glycopeptide approach.
17956937	1	35	theme	PSA	358:360	arg1	levels					362:367	increased serum PSA levels	342:367	increased serum PSA levels	342:367	The oligosaccharide structures of prostate specific antigen (PSA) are expected to be useful in discriminating prostate cancer from benign conditions both accompanied by increased serum PSA levels.
17956937	0	36	theme	specific	41:48	arg1	antigen					50:56	the prostate specific antigen	28:56	the prostate specific antigen	28:56	Oligosaccharide profiles of the prostate specific antigen in free and complexed forms from the prostate cancer patient serum and in seminal plasma: a glycopeptide approach.
17956937	8	37	attach	attached	1824:1831	arg1	PSA					1864:1866	PSA	1864:1866	PSA	1864:1866	The results suggest that identification of alpha2,3-linked sialic acids on PSA potentially discriminates malignant from benign conditions, if the analysis is applied to oligosaccharides specifically attached to the N-glycosylation site of PSA in either a free or a complexed form in the serum.
17956937	8	37	attach	attached	1824:1831	arg2	oligosaccharides					1794:1809	oligosaccharides	1794:1809	oligosaccharides specifically attached to the N-glycosylation site of PSA in either a free or a complexed form in the serum	1794:1916	The results suggest that identification of alpha2,3-linked sialic acids on PSA potentially discriminates malignant from benign conditions, if the analysis is applied to oligosaccharides specifically attached to the N-glycosylation site of PSA in either a free or a complexed form in the serum.
17956937	8	37	attach	attached	1824:1831	arg1	site					1856:1859	the N-glycosylation site	1836:1859	the N-glycosylation site of PSA in either a free or a complexed form in the serum	1836:1916	The results suggest that identification of alpha2,3-linked sialic acids on PSA potentially discriminates malignant from benign conditions, if the analysis is applied to oligosaccharides specifically attached to the N-glycosylation site of PSA in either a free or a complexed form in the serum.
17956937	0	38	theme	Oligosaccharide	0:14	arg1	profiles					16:23	Oligosaccharide profiles	0:23	Oligosaccharide profiles of the prostate specific antigen in free and complexed forms from the prostate cancer patient serum and in seminal plasma	0:145	Oligosaccharide profiles of the prostate specific antigen in free and complexed forms from the prostate cancer patient serum and in seminal plasma: a glycopeptide approach.
17956937	0	39	theme	free	61:64	arg1	forms					80:84	free and complexed forms	61:84	free and complexed forms from the prostate cancer patient serum	61:123	Oligosaccharide profiles of the prostate specific antigen in free and complexed forms from the prostate cancer patient serum and in seminal plasma: a glycopeptide approach.
17956937	2	40	theme	PSA	392:394	arg1	proportion					378:387	A large proportion	370:387	A large proportion of PSA	370:394	A large proportion of PSA forms a covalent complex with a glycoprotein, alpha(1)-antichymotrypsin, in human blood.
17956937	0	41	theme	prostate	32:39	arg1	antigen					50:56	the prostate specific antigen	28:56	the prostate specific antigen	28:56	Oligosaccharide profiles of the prostate specific antigen in free and complexed forms from the prostate cancer patient serum and in seminal plasma: a glycopeptide approach.
17956937	1	42	theme	prostate	283:290	arg1	cancer					292:297	prostate cancer	283:297	prostate cancer	283:297	The oligosaccharide structures of prostate specific antigen (PSA) are expected to be useful in discriminating prostate cancer from benign conditions both accompanied by increased serum PSA levels.
17956937	5	43	gly	sialylated	965:974	arg1	They					948:951	They	948:951	They	948:951	They were mostly sialylated, and a considerable sialic acid fraction was alpha2,3-linked as determined by Streptococcus pneumoniae neuraminidase digestion of the glycopeptides.
17956937	3	44	theme	patient	574:580	arg1	serum					582:586	cancer patient serum	567:586	cancer patient serum	567:586	In the present study, the glycan profiles of free and complexed forms of PSA from cancer patient serum and of seminal plasma PSA were compared by analyzing the glycopeptides obtained by lysylendopeptidase digestion of the electrophoretically separated PSA with mass spectrometry.
17956937	4	45	theme	PSA	785:787	arg1	N-glycans					789:797	the PSA N-glycans	781:797	the PSA N-glycans from the free and complexed molecules	781:835	The profiles of the PSA N-glycans from the free and complexed molecules were quite similar to each other and consisted of fucosylated biantennary oligosaccharides as the major class.
17956937	0	46	theme	antigen	50:56	arg1	profiles					16:23	Oligosaccharide profiles	0:23	Oligosaccharide profiles of the prostate specific antigen in free and complexed forms from the prostate cancer patient serum and in seminal plasma	0:145	Oligosaccharide profiles of the prostate specific antigen in free and complexed forms from the prostate cancer patient serum and in seminal plasma: a glycopeptide approach.
17956937	7	47	contain	carries	1589:1595	arg1	analysis					1560:1567	analysis	1560:1567	analysis of released glycans	1560:1587	Complex-type oligosaccharides from other sources were found in the seminal plasma sample, indicating that analysis of released glycans carries a risk of being misleading.
17956937	7	47	contain	carries	1589:1595	arg2	risk					1599:1602	a risk	1597:1602	a risk of being misleading	1597:1622	Complex-type oligosaccharides from other sources were found in the seminal plasma sample, indicating that analysis of released glycans carries a risk of being misleading.
17956937	3	48	theme	PSA	610:612	arg1	profiles					518:525	the glycan profiles	507:525	the glycan profiles of free and complexed forms of PSA from cancer patient serum and of seminal plasma PSA	507:612	In the present study, the glycan profiles of free and complexed forms of PSA from cancer patient serum and of seminal plasma PSA were compared by analyzing the glycopeptides obtained by lysylendopeptidase digestion of the electrophoretically separated PSA with mass spectrometry.
17956937	8	49	theme	sialic	1684:1689	arg1	acids					1691:1695	alpha2,3-linked sialic acids	1668:1695	alpha2,3-linked sialic acids	1668:1695	The results suggest that identification of alpha2,3-linked sialic acids on PSA potentially discriminates malignant from benign conditions, if the analysis is applied to oligosaccharides specifically attached to the N-glycosylation site of PSA in either a free or a complexed form in the serum.
17956937	1	50	theme	specific	216:223	arg1	PSA					234:236	PSA	234:236	PSA	234:236	The oligosaccharide structures of prostate specific antigen (PSA) are expected to be useful in discriminating prostate cancer from benign conditions both accompanied by increased serum PSA levels.
17956937	1	50	theme	specific	216:223	arg1	antigen					225:231	prostate specific antigen	207:231	prostate specific antigen (PSA)	207:237	The oligosaccharide structures of prostate specific antigen (PSA) are expected to be useful in discriminating prostate cancer from benign conditions both accompanied by increased serum PSA levels.
17956937	7	51	theme	seminal	1521:1527	arg1	sample					1536:1541	the seminal plasma sample	1517:1541	the seminal plasma sample	1517:1541	Complex-type oligosaccharides from other sources were found in the seminal plasma sample, indicating that analysis of released glycans carries a risk of being misleading.
17956937	3	52	theme	seminal	595:601	arg1	PSA					610:612	seminal plasma PSA	595:612	seminal plasma PSA	595:612	In the present study, the glycan profiles of free and complexed forms of PSA from cancer patient serum and of seminal plasma PSA were compared by analyzing the glycopeptides obtained by lysylendopeptidase digestion of the electrophoretically separated PSA with mass spectrometry.
17956937	8	53	from	conditions	1752:1761	arg1	malignant					1730:1738	malignant	1730:1738	malignant	1730:1738	The results suggest that identification of alpha2,3-linked sialic acids on PSA potentially discriminates malignant from benign conditions, if the analysis is applied to oligosaccharides specifically attached to the N-glycosylation site of PSA in either a free or a complexed form in the serum.
17956937	3	54	theme	present	492:498	arg1	study					500:504	the present study	488:504	the present study	488:504	In the present study, the glycan profiles of free and complexed forms of PSA from cancer patient serum and of seminal plasma PSA were compared by analyzing the glycopeptides obtained by lysylendopeptidase digestion of the electrophoretically separated PSA with mass spectrometry.
17956937	7	55	theme	other	1489:1493	arg1	sources					1495:1501	other sources	1489:1501	other sources	1489:1501	Complex-type oligosaccharides from other sources were found in the seminal plasma sample, indicating that analysis of released glycans carries a risk of being misleading.
17956937	6	56	theme	high-mannose	1152:1163	arg1	types					1176:1180	high-mannose and hybrid types	1152:1180	high-mannose and hybrid types of oligosaccharides	1152:1200	In the seminal plasma PSA, high-mannose and hybrid types of oligosaccharides were predominant, and the sialic acids attached to the latter as well as to biantennary oligosaccahrides were exclusively alpha2,6-linked because they were removed by Arthrobacter ureafaciens neuraminidase but resistant to S. pneumoniae neuraminidase.
17956937	3	57	from	serum	582:586	arg1	PSA					558:560	PSA	558:560	PSA from cancer patient serum	558:586	In the present study, the glycan profiles of free and complexed forms of PSA from cancer patient serum and of seminal plasma PSA were compared by analyzing the glycopeptides obtained by lysylendopeptidase digestion of the electrophoretically separated PSA with mass spectrometry.
17956937	3	57	from	serum	582:586	arg1	forms					549:553	free and complexed forms	530:553	free and complexed forms of PSA from cancer patient serum	530:586	In the present study, the glycan profiles of free and complexed forms of PSA from cancer patient serum and of seminal plasma PSA were compared by analyzing the glycopeptides obtained by lysylendopeptidase digestion of the electrophoretically separated PSA with mass spectrometry.
17956937	8	58	theme	benign	1745:1750	arg1	conditions					1752:1761	benign conditions	1745:1761	benign conditions	1745:1761	The results suggest that identification of alpha2,3-linked sialic acids on PSA potentially discriminates malignant from benign conditions, if the analysis is applied to oligosaccharides specifically attached to the N-glycosylation site of PSA in either a free or a complexed form in the serum.
17956937	0	59	gly	glycopeptide	150:161	arg2	glycopeptide					150:161	glycopeptide	150:161	glycopeptide	150:161	Oligosaccharide profiles of the prostate specific antigen in free and complexed forms from the prostate cancer patient serum and in seminal plasma: a glycopeptide approach.
17956937	4	60	theme	N-glycans	789:797	arg1	similar					848:854	similar	848:854	similar	848:854	The profiles of the PSA N-glycans from the free and complexed molecules were quite similar to each other and consisted of fucosylated biantennary oligosaccharides as the major class.
17956937	4	60	theme	N-glycans	789:797	arg1	profiles					769:776	The profiles	765:776	The profiles of the PSA N-glycans from the free and complexed molecules	765:835	The profiles of the PSA N-glycans from the free and complexed molecules were quite similar to each other and consisted of fucosylated biantennary oligosaccharides as the major class.
17956937	6	61	theme	sialic	1228:1233	arg1	acids					1235:1239	the sialic acids	1224:1239	the sialic acids attached to the latter as well as to biantennary oligosaccahrides	1224:1305	In the seminal plasma PSA, high-mannose and hybrid types of oligosaccharides were predominant, and the sialic acids attached to the latter as well as to biantennary oligosaccahrides were exclusively alpha2,6-linked because they were removed by Arthrobacter ureafaciens neuraminidase but resistant to S. pneumoniae neuraminidase.
17956937	6	61	theme	sialic	1228:1233	arg1	alpha2,6-linked					1324:1338	alpha2,6-linked	1324:1338	alpha2,6-linked	1324:1338	In the seminal plasma PSA, high-mannose and hybrid types of oligosaccharides were predominant, and the sialic acids attached to the latter as well as to biantennary oligosaccahrides were exclusively alpha2,6-linked because they were removed by Arthrobacter ureafaciens neuraminidase but resistant to S. pneumoniae neuraminidase.
17956937	3	62	theme	glycan	511:516	arg1	profiles					518:525	the glycan profiles	507:525	the glycan profiles of free and complexed forms of PSA from cancer patient serum and of seminal plasma PSA	507:612	In the present study, the glycan profiles of free and complexed forms of PSA from cancer patient serum and of seminal plasma PSA were compared by analyzing the glycopeptides obtained by lysylendopeptidase digestion of the electrophoretically separated PSA with mass spectrometry.
17956937	6	63	theme	seminal	1132:1138	arg1	PSA					1147:1149	the seminal plasma PSA	1128:1149	the seminal plasma PSA	1128:1149	In the seminal plasma PSA, high-mannose and hybrid types of oligosaccharides were predominant, and the sialic acids attached to the latter as well as to biantennary oligosaccahrides were exclusively alpha2,6-linked because they were removed by Arthrobacter ureafaciens neuraminidase but resistant to S. pneumoniae neuraminidase.
17956937	5	64	theme	considerable	983:994	arg1	fraction					1008:1015	a considerable sialic acid fraction	981:1015	a considerable sialic acid fraction	981:1015	They were mostly sialylated, and a considerable sialic acid fraction was alpha2,3-linked as determined by Streptococcus pneumoniae neuraminidase digestion of the glycopeptides.
17956937	5	64	theme	considerable	983:994	arg1	alpha2,3-linked					1021:1035	alpha2,3-linked	1021:1035	alpha2,3-linked	1021:1035	They were mostly sialylated, and a considerable sialic acid fraction was alpha2,3-linked as determined by Streptococcus pneumoniae neuraminidase digestion of the glycopeptides.
17956937	1	65	theme	oligosaccharide	177:191	arg1	structures					193:202	The oligosaccharide structures	173:202	The oligosaccharide structures of prostate specific antigen (PSA)	173:237	The oligosaccharide structures of prostate specific antigen (PSA) are expected to be useful in discriminating prostate cancer from benign conditions both accompanied by increased serum PSA levels.
17956937	1	65	theme	oligosaccharide	177:191	arg1	useful					258:263	useful	258:263	useful	258:263	The oligosaccharide structures of prostate specific antigen (PSA) are expected to be useful in discriminating prostate cancer from benign conditions both accompanied by increased serum PSA levels.
17956937	7	66	from	sources	1495:1501	arg1	oligosaccharides					1467:1482	Complex-type oligosaccharides	1454:1482	Complex-type oligosaccharides from other sources	1454:1501	Complex-type oligosaccharides from other sources were found in the seminal plasma sample, indicating that analysis of released glycans carries a risk of being misleading.
17956937	0	67	dep	approach	163:170	arg1	profiles					16:23	Oligosaccharide profiles	0:23	Oligosaccharide profiles of the prostate specific antigen in free and complexed forms from the prostate cancer patient serum and in seminal plasma	0:145	Oligosaccharide profiles of the prostate specific antigen in free and complexed forms from the prostate cancer patient serum and in seminal plasma: a glycopeptide approach.
17956937	6	68	theme	biantennary	1278:1288	arg1	oligosaccahrides					1290:1305	biantennary oligosaccahrides	1278:1305	biantennary oligosaccahrides	1278:1305	In the seminal plasma PSA, high-mannose and hybrid types of oligosaccharides were predominant, and the sialic acids attached to the latter as well as to biantennary oligosaccahrides were exclusively alpha2,6-linked because they were removed by Arthrobacter ureafaciens neuraminidase but resistant to S. pneumoniae neuraminidase.
17956937	6	69	from	predominant	1207:1217	arg1	PSA					1147:1149	the seminal plasma PSA	1128:1149	the seminal plasma PSA	1128:1149	In the seminal plasma PSA, high-mannose and hybrid types of oligosaccharides were predominant, and the sialic acids attached to the latter as well as to biantennary oligosaccahrides were exclusively alpha2,6-linked because they were removed by Arthrobacter ureafaciens neuraminidase but resistant to S. pneumoniae neuraminidase.
17956937	6	70	attach	predominant	1207:1217	arg1	PSA					1147:1149	the seminal plasma PSA	1128:1149	the seminal plasma PSA	1128:1149	In the seminal plasma PSA, high-mannose and hybrid types of oligosaccharides were predominant, and the sialic acids attached to the latter as well as to biantennary oligosaccahrides were exclusively alpha2,6-linked because they were removed by Arthrobacter ureafaciens neuraminidase but resistant to S. pneumoniae neuraminidase.
17956937	6	70	attach	predominant	1207:1217	arg2	types					1176:1180	high-mannose and hybrid types	1152:1180	high-mannose and hybrid types of oligosaccharides	1152:1200	In the seminal plasma PSA, high-mannose and hybrid types of oligosaccharides were predominant, and the sialic acids attached to the latter as well as to biantennary oligosaccahrides were exclusively alpha2,6-linked because they were removed by Arthrobacter ureafaciens neuraminidase but resistant to S. pneumoniae neuraminidase.
17956937	8	71	from	identification	1650:1663	arg1	PSA					1700:1702	PSA	1700:1702	PSA	1700:1702	The results suggest that identification of alpha2,3-linked sialic acids on PSA potentially discriminates malignant from benign conditions, if the analysis is applied to oligosaccharides specifically attached to the N-glycosylation site of PSA in either a free or a complexed form in the serum.
17956937	5	72	theme	acid	1003:1006	arg1	fraction					1008:1015	a considerable sialic acid fraction	981:1015	a considerable sialic acid fraction	981:1015	They were mostly sialylated, and a considerable sialic acid fraction was alpha2,3-linked as determined by Streptococcus pneumoniae neuraminidase digestion of the glycopeptides.
17956937	5	72	theme	acid	1003:1006	arg1	alpha2,3-linked					1021:1035	alpha2,3-linked	1021:1035	alpha2,3-linked	1021:1035	They were mostly sialylated, and a considerable sialic acid fraction was alpha2,3-linked as determined by Streptococcus pneumoniae neuraminidase digestion of the glycopeptides.
17956937	3	73	theme	PSA	558:560	arg1	forms					549:553	free and complexed forms	530:553	free and complexed forms of PSA from cancer patient serum	530:586	In the present study, the glycan profiles of free and complexed forms of PSA from cancer patient serum and of seminal plasma PSA were compared by analyzing the glycopeptides obtained by lysylendopeptidase digestion of the electrophoretically separated PSA with mass spectrometry.
17956937	4	74	from	profiles	769:776	arg1	molecules					827:835	the free and complexed molecules	804:835	the free and complexed molecules	804:835	The profiles of the PSA N-glycans from the free and complexed molecules were quite similar to each other and consisted of fucosylated biantennary oligosaccharides as the major class.
17956937	3	75	theme	separated	727:735	arg1	PSA					737:739	the electrophoretically separated PSA	703:739	the electrophoretically separated PSA	703:739	In the present study, the glycan profiles of free and complexed forms of PSA from cancer patient serum and of seminal plasma PSA were compared by analyzing the glycopeptides obtained by lysylendopeptidase digestion of the electrophoretically separated PSA with mass spectrometry.
17956937	3	76	theme	forms	549:553	arg1	profiles					518:525	the glycan profiles	507:525	the glycan profiles of free and complexed forms of PSA from cancer patient serum and of seminal plasma PSA	507:612	In the present study, the glycan profiles of free and complexed forms of PSA from cancer patient serum and of seminal plasma PSA were compared by analyzing the glycopeptides obtained by lysylendopeptidase digestion of the electrophoretically separated PSA with mass spectrometry.
17956937	6	77	theme	hybrid	1169:1174	arg1	types					1176:1180	high-mannose and hybrid types	1152:1180	high-mannose and hybrid types of oligosaccharides	1152:1200	In the seminal plasma PSA, high-mannose and hybrid types of oligosaccharides were predominant, and the sialic acids attached to the latter as well as to biantennary oligosaccahrides were exclusively alpha2,6-linked because they were removed by Arthrobacter ureafaciens neuraminidase but resistant to S. pneumoniae neuraminidase.
17956937	6	78	theme	Arthrobacter	1369:1380	arg1	neuraminidase					1394:1406	Arthrobacter ureafaciens neuraminidase	1369:1406	Arthrobacter ureafaciens neuraminidase	1369:1406	In the seminal plasma PSA, high-mannose and hybrid types of oligosaccharides were predominant, and the sialic acids attached to the latter as well as to biantennary oligosaccahrides were exclusively alpha2,6-linked because they were removed by Arthrobacter ureafaciens neuraminidase but resistant to S. pneumoniae neuraminidase.
17956937	4	79	from	molecules	827:835	arg1	N-glycans					789:797	the PSA N-glycans	781:797	the PSA N-glycans from the free and complexed molecules	781:835	The profiles of the PSA N-glycans from the free and complexed molecules were quite similar to each other and consisted of fucosylated biantennary oligosaccharides as the major class.
17956937	4	79	from	molecules	827:835	arg1	similar					848:854	similar	848:854	similar	848:854	The profiles of the PSA N-glycans from the free and complexed molecules were quite similar to each other and consisted of fucosylated biantennary oligosaccharides as the major class.
17956937	4	79	from	molecules	827:835	arg1	profiles					769:776	The profiles	765:776	The profiles of the PSA N-glycans from the free and complexed molecules	765:835	The profiles of the PSA N-glycans from the free and complexed molecules were quite similar to each other and consisted of fucosylated biantennary oligosaccharides as the major class.
17956937	8	80	theme	N-glycosylation	1840:1854	arg1	PSA					1864:1866	PSA	1864:1866	PSA	1864:1866	The results suggest that identification of alpha2,3-linked sialic acids on PSA potentially discriminates malignant from benign conditions, if the analysis is applied to oligosaccharides specifically attached to the N-glycosylation site of PSA in either a free or a complexed form in the serum.
17956937	8	80	theme	N-glycosylation	1840:1854	arg1	site					1856:1859	the N-glycosylation site	1836:1859	the N-glycosylation site of PSA in either a free or a complexed form in the serum	1836:1916	The results suggest that identification of alpha2,3-linked sialic acids on PSA potentially discriminates malignant from benign conditions, if the analysis is applied to oligosaccharides specifically attached to the N-glycosylation site of PSA in either a free or a complexed form in the serum.
17956937	7	81	located	found	1508:1512	arg1	sample					1536:1541	the seminal plasma sample	1517:1541	the seminal plasma sample	1517:1541	Complex-type oligosaccharides from other sources were found in the seminal plasma sample, indicating that analysis of released glycans carries a risk of being misleading.
17956937	7	81	located	found	1508:1512	arg2	oligosaccharides					1467:1482	Complex-type oligosaccharides	1454:1482	Complex-type oligosaccharides from other sources	1454:1501	Complex-type oligosaccharides from other sources were found in the seminal plasma sample, indicating that analysis of released glycans carries a risk of being misleading.
17956937	5	82	theme	Streptococcus	1054:1066	arg1	digestion					1093:1101	Streptococcus pneumoniae neuraminidase digestion	1054:1101	Streptococcus pneumoniae neuraminidase digestion of the glycopeptides	1054:1122	They were mostly sialylated, and a considerable sialic acid fraction was alpha2,3-linked as determined by Streptococcus pneumoniae neuraminidase digestion of the glycopeptides.
17956937	0	83	from	profiles	16:23	arg1	plasma					140:145	seminal plasma	132:145	seminal plasma	132:145	Oligosaccharide profiles of the prostate specific antigen in free and complexed forms from the prostate cancer patient serum and in seminal plasma: a glycopeptide approach.
17956937	0	83	from	profiles	16:23	arg1	forms					80:84	free and complexed forms	61:84	free and complexed forms from the prostate cancer patient serum	61:123	Oligosaccharide profiles of the prostate specific antigen in free and complexed forms from the prostate cancer patient serum and in seminal plasma: a glycopeptide approach.
17956937	0	83	from	profiles	16:23	arg1	serum					119:123	the prostate cancer patient serum	91:123	the prostate cancer patient serum	91:123	Oligosaccharide profiles of the prostate specific antigen in free and complexed forms from the prostate cancer patient serum and in seminal plasma: a glycopeptide approach.
17956937	7	84	theme	released	1572:1579	arg1	glycans					1581:1587	released glycans	1572:1587	released glycans	1572:1587	Complex-type oligosaccharides from other sources were found in the seminal plasma sample, indicating that analysis of released glycans carries a risk of being misleading.
17956937	4	85	theme	fucosylated	887:897	arg1	oligosaccharides					911:926	fucosylated biantennary oligosaccharides	887:926	fucosylated biantennary oligosaccharides	887:926	The profiles of the PSA N-glycans from the free and complexed molecules were quite similar to each other and consisted of fucosylated biantennary oligosaccharides as the major class.
17956937	3	86	from	forms	549:553	arg1	serum					582:586	cancer patient serum	567:586	cancer patient serum	567:586	In the present study, the glycan profiles of free and complexed forms of PSA from cancer patient serum and of seminal plasma PSA were compared by analyzing the glycopeptides obtained by lysylendopeptidase digestion of the electrophoretically separated PSA with mass spectrometry.
17956937	0	87	theme	cancer	104:109	arg1	serum					119:123	the prostate cancer patient serum	91:123	the prostate cancer patient serum	91:123	Oligosaccharide profiles of the prostate specific antigen in free and complexed forms from the prostate cancer patient serum and in seminal plasma: a glycopeptide approach.
17956937	1	88	theme	serum	352:356	arg1	levels					362:367	increased serum PSA levels	342:367	increased serum PSA levels	342:367	The oligosaccharide structures of prostate specific antigen (PSA) are expected to be useful in discriminating prostate cancer from benign conditions both accompanied by increased serum PSA levels.
17956937	2	89	theme	large	372:376	arg1	proportion					378:387	A large proportion	370:387	A large proportion of PSA	370:394	A large proportion of PSA forms a covalent complex with a glycoprotein, alpha(1)-antichymotrypsin, in human blood.
17956937	3	90	with	digestion	690:698	arg1	spectrometry					751:762	mass spectrometry	746:762	mass spectrometry	746:762	In the present study, the glycan profiles of free and complexed forms of PSA from cancer patient serum and of seminal plasma PSA were compared by analyzing the glycopeptides obtained by lysylendopeptidase digestion of the electrophoretically separated PSA with mass spectrometry.
17956937	4	91	gly	fucosylated	887:897	arg1	oligosaccharides					911:926	fucosylated biantennary oligosaccharides	887:926	fucosylated biantennary oligosaccharides	887:926	The profiles of the PSA N-glycans from the free and complexed molecules were quite similar to each other and consisted of fucosylated biantennary oligosaccharides as the major class.
17956937	2	92	theme	covalent	404:411	arg1	complex					413:419	a covalent complex	402:419	a covalent complex with a glycoprotein, alpha(1)-antichymotrypsin,	402:467	A large proportion of PSA forms a covalent complex with a glycoprotein, alpha(1)-antichymotrypsin, in human blood.
17956937	3	93	gly	glycopeptides	645:657	arg2	glycopeptides					645:657	the glycopeptides	641:657	the glycopeptides obtained by lysylendopeptidase digestion of the electrophoretically separated PSA with mass spectrometry	641:762	In the present study, the glycan profiles of free and complexed forms of PSA from cancer patient serum and of seminal plasma PSA were compared by analyzing the glycopeptides obtained by lysylendopeptidase digestion of the electrophoretically separated PSA with mass spectrometry.
17956937	6	94	theme	S.	1425:1426	arg1	neuraminidase					1439:1451	S. pneumoniae neuraminidase	1425:1451	S. pneumoniae neuraminidase	1425:1451	In the seminal plasma PSA, high-mannose and hybrid types of oligosaccharides were predominant, and the sialic acids attached to the latter as well as to biantennary oligosaccahrides were exclusively alpha2,6-linked because they were removed by Arthrobacter ureafaciens neuraminidase but resistant to S. pneumoniae neuraminidase.
17956937	6	95	dep	S.	1425:1426	arg1	pneumoniae					1428:1437	pneumoniae	1428:1437	pneumoniae	1428:1437	In the seminal plasma PSA, high-mannose and hybrid types of oligosaccharides were predominant, and the sialic acids attached to the latter as well as to biantennary oligosaccahrides were exclusively alpha2,6-linked because they were removed by Arthrobacter ureafaciens neuraminidase but resistant to S. pneumoniae neuraminidase.
17956937	2	96	theme	alpha	442:446	arg1	-antichymotrypsin					450:466	alpha(1)-antichymotrypsin	442:466	alpha(1)-antichymotrypsin	442:466	A large proportion of PSA forms a covalent complex with a glycoprotein, alpha(1)-antichymotrypsin, in human blood.
17956937	2	96	theme	alpha	442:446	arg1	glycoprotein					428:439	a glycoprotein	426:439	a glycoprotein	426:439	A large proportion of PSA forms a covalent complex with a glycoprotein, alpha(1)-antichymotrypsin, in human blood.
17956937	3	97	theme	cancer	567:572	arg1	serum					582:586	cancer patient serum	567:586	cancer patient serum	567:586	In the present study, the glycan profiles of free and complexed forms of PSA from cancer patient serum and of seminal plasma PSA were compared by analyzing the glycopeptides obtained by lysylendopeptidase digestion of the electrophoretically separated PSA with mass spectrometry.
17956937	2	98	gly	glycoprotein	428:439	arg1	-antichymotrypsin					450:466	alpha(1)-antichymotrypsin	442:466	alpha(1)-antichymotrypsin	442:466	A large proportion of PSA forms a covalent complex with a glycoprotein, alpha(1)-antichymotrypsin, in human blood.
17956937	2	98	gly	glycoprotein	428:439	arg1	glycoprotein					428:439	a glycoprotein	426:439	a glycoprotein	426:439	A large proportion of PSA forms a covalent complex with a glycoprotein, alpha(1)-antichymotrypsin, in human blood.
17956937	5	99	theme	neuraminidase	1079:1091	arg1	digestion					1093:1101	Streptococcus pneumoniae neuraminidase digestion	1054:1101	Streptococcus pneumoniae neuraminidase digestion of the glycopeptides	1054:1122	They were mostly sialylated, and a considerable sialic acid fraction was alpha2,3-linked as determined by Streptococcus pneumoniae neuraminidase digestion of the glycopeptides.
17956937	5	100	dep	Streptococcus	1054:1066	arg1	pneumoniae					1068:1077	pneumoniae	1068:1077	pneumoniae	1068:1077	They were mostly sialylated, and a considerable sialic acid fraction was alpha2,3-linked as determined by Streptococcus pneumoniae neuraminidase digestion of the glycopeptides.
17956937	3	101	theme	plasma	603:608	arg1	PSA					610:612	seminal plasma PSA	595:612	seminal plasma PSA	595:612	In the present study, the glycan profiles of free and complexed forms of PSA from cancer patient serum and of seminal plasma PSA were compared by analyzing the glycopeptides obtained by lysylendopeptidase digestion of the electrophoretically separated PSA with mass spectrometry.
17956937	8	102	theme	acids	1691:1695	arg1	identification					1650:1663	identification	1650:1663	identification of alpha2,3-linked sialic acids on PSA	1650:1702	The results suggest that identification of alpha2,3-linked sialic acids on PSA potentially discriminates malignant from benign conditions, if the analysis is applied to oligosaccharides specifically attached to the N-glycosylation site of PSA in either a free or a complexed form in the serum.
17956937	1	103	theme	benign	304:309	arg1	conditions					311:320	benign conditions	304:320	benign conditions	304:320	The oligosaccharide structures of prostate specific antigen (PSA) are expected to be useful in discriminating prostate cancer from benign conditions both accompanied by increased serum PSA levels.
17956937	8	104	gly	N-glycosylation	1840:1854	arg2	site					1856:1859	the N-glycosylation site	1836:1859	the N-glycosylation site of PSA in either a free or a complexed form in the serum	1836:1916	The results suggest that identification of alpha2,3-linked sialic acids on PSA potentially discriminates malignant from benign conditions, if the analysis is applied to oligosaccharides specifically attached to the N-glycosylation site of PSA in either a free or a complexed form in the serum.
17956937	8	104	gly	N-glycosylation	1840:1854	arg1	PSA					1864:1866	PSA	1864:1866	PSA	1864:1866	The results suggest that identification of alpha2,3-linked sialic acids on PSA potentially discriminates malignant from benign conditions, if the analysis is applied to oligosaccharides specifically attached to the N-glycosylation site of PSA in either a free or a complexed form in the serum.
17956937	8	104	gly	N-glycosylation	1840:1854	arg2	PSA					1864:1866	PSA	1864:1866	PSA	1864:1866	The results suggest that identification of alpha2,3-linked sialic acids on PSA potentially discriminates malignant from benign conditions, if the analysis is applied to oligosaccharides specifically attached to the N-glycosylation site of PSA in either a free or a complexed form in the serum.
17956937	1	105	theme	antigen	225:231	arg1	structures					193:202	The oligosaccharide structures	173:202	The oligosaccharide structures of prostate specific antigen (PSA)	173:237	The oligosaccharide structures of prostate specific antigen (PSA) are expected to be useful in discriminating prostate cancer from benign conditions both accompanied by increased serum PSA levels.
17956937	1	105	theme	antigen	225:231	arg1	useful					258:263	useful	258:263	useful	258:263	The oligosaccharide structures of prostate specific antigen (PSA) are expected to be useful in discriminating prostate cancer from benign conditions both accompanied by increased serum PSA levels.
17956937	7	106	theme	plasma	1529:1534	arg1	sample					1536:1541	the seminal plasma sample	1517:1541	the seminal plasma sample	1517:1541	Complex-type oligosaccharides from other sources were found in the seminal plasma sample, indicating that analysis of released glycans carries a risk of being misleading.
17956937	0	107	from	serum	119:123	arg1	forms					80:84	free and complexed forms	61:84	free and complexed forms from the prostate cancer patient serum	61:123	Oligosaccharide profiles of the prostate specific antigen in free and complexed forms from the prostate cancer patient serum and in seminal plasma: a glycopeptide approach.
17956937	0	107	from	serum	119:123	arg1	profiles					16:23	Oligosaccharide profiles	0:23	Oligosaccharide profiles of the prostate specific antigen in free and complexed forms from the prostate cancer patient serum and in seminal plasma	0:145	Oligosaccharide profiles of the prostate specific antigen in free and complexed forms from the prostate cancer patient serum and in seminal plasma: a glycopeptide approach.
2023947	0	0	theme	urinary	84:90	arg1	activator					104:112	urinary plasminogen activator	84:112	urinary plasminogen activator	84:112	Characterization of a posttranslational fucosylation in the growth factor domain of urinary plasminogen activator.
2023947	5	1	theme	acidic	912:917	arg1	conditions					919:928	standard acidic conditions	903:928	standard acidic conditions of the amino acid analysis and Edman sequencing	903:976	This type of modification is normally not detected without mass spectrometry because the fucose-threonine bond is hydrolyzed under standard acidic conditions of the amino acid analysis and Edman sequencing.
2023947	2	2	theme	plasminogen	348:358	arg1	activator					360:368	urinary plasminogen activator	340:368	urinary plasminogen activator	340:368	This is the region of urinary plasminogen activator responsible for its specific receptor binding.
2023947	2	3	theme	receptor	399:406	arg1	binding					408:414	its specific receptor binding	386:414	its specific receptor binding	386:414	This is the region of urinary plasminogen activator responsible for its specific receptor binding.
2023947	2	4	theme	urinary	340:346	arg1	activator					360:368	urinary plasminogen activator	340:368	urinary plasminogen activator	340:368	This is the region of urinary plasminogen activator responsible for its specific receptor binding.
2023947	6	5	theme	other	1020:1024	arg1	proteins					1026:1033	other proteins	1020:1033	other proteins	1020:1033	This modification may be widely found in other proteins.
2023947	0	6	theme	activator	104:112	arg1	activator					104:112	urinary plasminogen activator	84:112	urinary plasminogen activator	84:112	Characterization of a posttranslational fucosylation in the growth factor domain of urinary plasminogen activator.
2023947	0	6	theme	activator	104:112	arg1	domain					74:79	the growth factor domain	56:79	the growth factor domain of urinary plasminogen activator	56:112	Characterization of a posttranslational fucosylation in the growth factor domain of urinary plasminogen activator.
2023947	0	7	from	Characterization	0:15	arg1	activator					104:112	urinary plasminogen activator	84:112	urinary plasminogen activator	84:112	Characterization of a posttranslational fucosylation in the growth factor domain of urinary plasminogen activator.
2023947	0	7	from	Characterization	0:15	arg1	domain					74:79	the growth factor domain	56:79	the growth factor domain of urinary plasminogen activator	56:112	Characterization of a posttranslational fucosylation in the growth factor domain of urinary plasminogen activator.
2023947	0	8	theme	plasminogen	92:102	arg1	activator					104:112	urinary plasminogen activator	84:112	urinary plasminogen activator	84:112	Characterization of a posttranslational fucosylation in the growth factor domain of urinary plasminogen activator.
2023947	4	9	theme	Edman	711:715	arg1	degradation					717:727	Edman degradation	711:727	Edman degradation	711:727	The glycan moiety and the site of modification have been identified with mass spectrometry and confirmed by carbohydrate composition analysis, Edman degradation, and one- and two-dimensional NMR studies.
2023947	5	10	theme	amino	937:941	arg1	analysis					948:955	the amino acid analysis	933:955	the amino acid analysis	933:955	This type of modification is normally not detected without mass spectrometry because the fucose-threonine bond is hydrolyzed under standard acidic conditions of the amino acid analysis and Edman sequencing.
2023947	6	11	located	found	1011:1015	arg1	proteins					1026:1033	other proteins	1020:1033	other proteins	1020:1033	This modification may be widely found in other proteins.
2023947	6	11	located	found	1011:1015	arg2	modification					984:995	This modification	979:995	This modification	979:995	This modification may be widely found in other proteins.
2023947	4	12	theme	carbohydrate	676:687	arg1	analysis					701:708	carbohydrate composition analysis	676:708	carbohydrate composition analysis	676:708	The glycan moiety and the site of modification have been identified with mass spectrometry and confirmed by carbohydrate composition analysis, Edman degradation, and one- and two-dimensional NMR studies.
2023947	1	13	theme	plasminogen	193:203	arg1	activators					205:214	plasminogen activators	193:214	plasminogen activators (urokinases; EC 3.4.21.31)	193:241	A posttranslational modification site in natural and recombinant urinary-type plasminogen activators (urokinases; EC 3.4.21.31) has been localized to Thr-18, in the growth factor domain of the molecule.
2023947	1	14	from	site	148:151	arg1	natural					156:162	natural	156:162	natural	156:162	A posttranslational modification site in natural and recombinant urinary-type plasminogen activators (urokinases; EC 3.4.21.31) has been localized to Thr-18, in the growth factor domain of the molecule.
2023947	1	14	from	site	148:151	arg1	urinary-type					180:191	urinary-type	180:191	urinary-type	180:191	A posttranslational modification site in natural and recombinant urinary-type plasminogen activators (urokinases; EC 3.4.21.31) has been localized to Thr-18, in the growth factor domain of the molecule.
2023947	5	15	theme	Edman	961:965	arg1	sequencing					967:976	Edman sequencing	961:976	Edman sequencing	961:976	This type of modification is normally not detected without mass spectrometry because the fucose-threonine bond is hydrolyzed under standard acidic conditions of the amino acid analysis and Edman sequencing.
2023947	2	16	theme	specific	390:397	arg1	binding					408:414	its specific receptor binding	386:414	its specific receptor binding	386:414	This is the region of urinary plasminogen activator responsible for its specific receptor binding.
2023947	0	17	from	fucosylation	40:51	arg1	activator					104:112	urinary plasminogen activator	84:112	urinary plasminogen activator	84:112	Characterization of a posttranslational fucosylation in the growth factor domain of urinary plasminogen activator.
2023947	0	17	from	fucosylation	40:51	arg1	domain					74:79	the growth factor domain	56:79	the growth factor domain of urinary plasminogen activator	56:112	Characterization of a posttranslational fucosylation in the growth factor domain of urinary plasminogen activator.
2023947	4	18	theme	two-dimensional	743:757	arg1	studies					763:769	one- and two-dimensional NMR studies	734:769	one- and two-dimensional NMR studies	734:769	The glycan moiety and the site of modification have been identified with mass spectrometry and confirmed by carbohydrate composition analysis, Edman degradation, and one- and two-dimensional NMR studies.
2023947	3	19	theme	carbohydrate-protein	428:447	arg1	monosaccharide					467:480	a single monosaccharide	458:480	a single monosaccharide	458:480	An unusual carbohydrate-protein linkage, a single monosaccharide, fucose, covalently attached directly to threonine in the peptide, is described here.
2023947	3	19	theme	carbohydrate-protein	428:447	arg1	linkage					449:455	An unusual carbohydrate-protein linkage	417:455	An unusual carbohydrate-protein linkage	417:455	An unusual carbohydrate-protein linkage, a single monosaccharide, fucose, covalently attached directly to threonine in the peptide, is described here.
2023947	1	20	theme	growth	280:285	arg1	domain					294:299	the growth factor domain	276:299	the growth factor domain of the molecule	276:315	A posttranslational modification site in natural and recombinant urinary-type plasminogen activators (urokinases; EC 3.4.21.31) has been localized to Thr-18, in the growth factor domain of the molecule.
2023947	1	20	theme	growth	280:285	arg1	molecule					308:315	the molecule	304:315	the molecule	304:315	A posttranslational modification site in natural and recombinant urinary-type plasminogen activators (urokinases; EC 3.4.21.31) has been localized to Thr-18, in the growth factor domain of the molecule.
2023947	5	21	theme	sequencing	967:976	arg1	conditions					919:928	standard acidic conditions	903:928	standard acidic conditions of the amino acid analysis and Edman sequencing	903:976	This type of modification is normally not detected without mass spectrometry because the fucose-threonine bond is hydrolyzed under standard acidic conditions of the amino acid analysis and Edman sequencing.
2023947	5	22	theme	standard	903:910	arg1	conditions					919:928	standard acidic conditions	903:928	standard acidic conditions of the amino acid analysis and Edman sequencing	903:976	This type of modification is normally not detected without mass spectrometry because the fucose-threonine bond is hydrolyzed under standard acidic conditions of the amino acid analysis and Edman sequencing.
2023947	0	23	theme	posttranslational	22:38	arg1	fucosylation					40:51	a posttranslational fucosylation	20:51	a posttranslational fucosylation in the growth factor domain of urinary plasminogen activator	20:112	Characterization of a posttranslational fucosylation in the growth factor domain of urinary plasminogen activator.
2023947	1	24	theme	factor	287:292	arg1	domain					294:299	the growth factor domain	276:299	the growth factor domain of the molecule	276:315	A posttranslational modification site in natural and recombinant urinary-type plasminogen activators (urokinases; EC 3.4.21.31) has been localized to Thr-18, in the growth factor domain of the molecule.
2023947	1	24	theme	factor	287:292	arg1	molecule					308:315	the molecule	304:315	the molecule	304:315	A posttranslational modification site in natural and recombinant urinary-type plasminogen activators (urokinases; EC 3.4.21.31) has been localized to Thr-18, in the growth factor domain of the molecule.
2023947	1	25	located	localized	252:260	arg1	domain					294:299	the growth factor domain	276:299	the growth factor domain of the molecule	276:315	A posttranslational modification site in natural and recombinant urinary-type plasminogen activators (urokinases; EC 3.4.21.31) has been localized to Thr-18, in the growth factor domain of the molecule.
2023947	1	25	located	localized	252:260	arg1	molecule					308:315	the molecule	304:315	the molecule	304:315	A posttranslational modification site in natural and recombinant urinary-type plasminogen activators (urokinases; EC 3.4.21.31) has been localized to Thr-18, in the growth factor domain of the molecule.
2023947	1	25	located	localized	252:260	arg2	site					148:151	A posttranslational modification site	115:151	A posttranslational modification site in natural and recombinant urinary-type plasminogen activators (urokinases; EC 3.4.21.31)	115:241	A posttranslational modification site in natural and recombinant urinary-type plasminogen activators (urokinases; EC 3.4.21.31) has been localized to Thr-18, in the growth factor domain of the molecule.
2023947	1	26	dep	natural	156:162	arg1	activators					205:214	plasminogen activators	193:214	plasminogen activators (urokinases; EC 3.4.21.31)	193:241	A posttranslational modification site in natural and recombinant urinary-type plasminogen activators (urokinases; EC 3.4.21.31) has been localized to Thr-18, in the growth factor domain of the molecule.
2023947	4	27	theme	glycan	572:577	arg1	moiety					579:584	The glycan moiety	568:584	The glycan moiety	568:584	The glycan moiety and the site of modification have been identified with mass spectrometry and confirmed by carbohydrate composition analysis, Edman degradation, and one- and two-dimensional NMR studies.
2023947	4	28	theme	NMR	759:761	arg1	studies					763:769	one- and two-dimensional NMR studies	734:769	one- and two-dimensional NMR studies	734:769	The glycan moiety and the site of modification have been identified with mass spectrometry and confirmed by carbohydrate composition analysis, Edman degradation, and one- and two-dimensional NMR studies.
2023947	5	29	theme	mass	831:834	arg1	spectrometry					836:847	mass spectrometry	831:847	mass spectrometry	831:847	This type of modification is normally not detected without mass spectrometry because the fucose-threonine bond is hydrolyzed under standard acidic conditions of the amino acid analysis and Edman sequencing.
2023947	5	30	theme	modification	785:796	arg1	type					777:780	This type	772:780	This type of modification	772:796	This type of modification is normally not detected without mass spectrometry because the fucose-threonine bond is hydrolyzed under standard acidic conditions of the amino acid analysis and Edman sequencing.
2023947	5	31	theme	acid	943:946	arg1	analysis					948:955	the amino acid analysis	933:955	the amino acid analysis	933:955	This type of modification is normally not detected without mass spectrometry because the fucose-threonine bond is hydrolyzed under standard acidic conditions of the amino acid analysis and Edman sequencing.
2023947	5	32	theme	fucose-threonine	861:876	arg1	bond					878:881	the fucose-threonine bond	857:881	the fucose-threonine bond	857:881	This type of modification is normally not detected without mass spectrometry because the fucose-threonine bond is hydrolyzed under standard acidic conditions of the amino acid analysis and Edman sequencing.
2023947	3	33	theme	single	460:465	arg1	monosaccharide					467:480	a single monosaccharide	458:480	a single monosaccharide	458:480	An unusual carbohydrate-protein linkage, a single monosaccharide, fucose, covalently attached directly to threonine in the peptide, is described here.
2023947	3	33	theme	single	460:465	arg1	linkage					449:455	An unusual carbohydrate-protein linkage	417:455	An unusual carbohydrate-protein linkage	417:455	An unusual carbohydrate-protein linkage, a single monosaccharide, fucose, covalently attached directly to threonine in the peptide, is described here.
2023947	3	33	theme	single	460:465	arg1	fucose					483:488	fucose	483:488	fucose	483:488	An unusual carbohydrate-protein linkage, a single monosaccharide, fucose, covalently attached directly to threonine in the peptide, is described here.
2023947	0	34	theme	fucosylation	40:51	arg1	Characterization					0:15	Characterization	0:15	Characterization of a posttranslational fucosylation in the growth factor domain of urinary plasminogen activator.	0:113	Characterization of a posttranslational fucosylation in the growth factor domain of urinary plasminogen activator.
2023947	3	35	theme	unusual	420:426	arg1	monosaccharide					467:480	a single monosaccharide	458:480	a single monosaccharide	458:480	An unusual carbohydrate-protein linkage, a single monosaccharide, fucose, covalently attached directly to threonine in the peptide, is described here.
2023947	3	35	theme	unusual	420:426	arg1	linkage					449:455	An unusual carbohydrate-protein linkage	417:455	An unusual carbohydrate-protein linkage	417:455	An unusual carbohydrate-protein linkage, a single monosaccharide, fucose, covalently attached directly to threonine in the peptide, is described here.
2023947	0	36	from	domain	74:79	arg1	Characterization					0:15	Characterization	0:15	Characterization of a posttranslational fucosylation in the growth factor domain of urinary plasminogen activator.	0:113	Characterization of a posttranslational fucosylation in the growth factor domain of urinary plasminogen activator.
2023947	1	37	dep	urokinases	217:226	arg1	EC					229:230	EC 3.4.21.31	229:240	urokinases; EC 3.4.21.31	217:240	A posttranslational modification site in natural and recombinant urinary-type plasminogen activators (urokinases; EC 3.4.21.31) has been localized to Thr-18, in the growth factor domain of the molecule.
2023947	4	38	theme	mass	641:644	arg1	spectrometry					646:657	mass spectrometry	641:657	mass spectrometry	641:657	The glycan moiety and the site of modification have been identified with mass spectrometry and confirmed by carbohydrate composition analysis, Edman degradation, and one- and two-dimensional NMR studies.
2023947	0	39	theme	growth	60:65	arg1	activator					104:112	urinary plasminogen activator	84:112	urinary plasminogen activator	84:112	Characterization of a posttranslational fucosylation in the growth factor domain of urinary plasminogen activator.
2023947	0	39	theme	growth	60:65	arg1	domain					74:79	the growth factor domain	56:79	the growth factor domain of urinary plasminogen activator	56:112	Characterization of a posttranslational fucosylation in the growth factor domain of urinary plasminogen activator.
2023947	1	40	theme	molecule	308:315	arg1	domain					294:299	the growth factor domain	276:299	the growth factor domain of the molecule	276:315	A posttranslational modification site in natural and recombinant urinary-type plasminogen activators (urokinases; EC 3.4.21.31) has been localized to Thr-18, in the growth factor domain of the molecule.
2023947	1	40	theme	molecule	308:315	arg1	molecule					308:315	the molecule	304:315	the molecule	304:315	A posttranslational modification site in natural and recombinant urinary-type plasminogen activators (urokinases; EC 3.4.21.31) has been localized to Thr-18, in the growth factor domain of the molecule.
2023947	1	41	theme	posttranslational	117:133	arg1	site					148:151	A posttranslational modification site	115:151	A posttranslational modification site in natural and recombinant urinary-type plasminogen activators (urokinases; EC 3.4.21.31)	115:241	A posttranslational modification site in natural and recombinant urinary-type plasminogen activators (urokinases; EC 3.4.21.31) has been localized to Thr-18, in the growth factor domain of the molecule.
2023947	1	42	dep	activators	205:214	arg1	urokinases					217:226	urokinases	217:226	urokinases; EC 3.4.21.31	217:240	A posttranslational modification site in natural and recombinant urinary-type plasminogen activators (urokinases; EC 3.4.21.31) has been localized to Thr-18, in the growth factor domain of the molecule.
2023947	1	43	theme	modification	135:146	arg1	site					148:151	A posttranslational modification site	115:151	A posttranslational modification site in natural and recombinant urinary-type plasminogen activators (urokinases; EC 3.4.21.31)	115:241	A posttranslational modification site in natural and recombinant urinary-type plasminogen activators (urokinases; EC 3.4.21.31) has been localized to Thr-18, in the growth factor domain of the molecule.
2023947	0	44	gly	fucosylation	40:51	arg1	activator					104:112	urinary plasminogen activator	84:112	urinary plasminogen activator	84:112	Characterization of a posttranslational fucosylation in the growth factor domain of urinary plasminogen activator.
2023947	0	44	gly	fucosylation	40:51	arg1	domain					74:79	the growth factor domain	56:79	the growth factor domain of urinary plasminogen activator	56:112	Characterization of a posttranslational fucosylation in the growth factor domain of urinary plasminogen activator.
2023947	4	45	theme	one-	734:737	arg1	studies					763:769	one- and two-dimensional NMR studies	734:769	one- and two-dimensional NMR studies	734:769	The glycan moiety and the site of modification have been identified with mass spectrometry and confirmed by carbohydrate composition analysis, Edman degradation, and one- and two-dimensional NMR studies.
2023947	4	46	theme	modification	602:613	arg1	modification					602:613	modification	602:613	modification	602:613	The glycan moiety and the site of modification have been identified with mass spectrometry and confirmed by carbohydrate composition analysis, Edman degradation, and one- and two-dimensional NMR studies.
2023947	4	46	theme	modification	602:613	arg1	moiety					579:584	The glycan moiety	568:584	The glycan moiety	568:584	The glycan moiety and the site of modification have been identified with mass spectrometry and confirmed by carbohydrate composition analysis, Edman degradation, and one- and two-dimensional NMR studies.
2023947	4	46	theme	modification	602:613	arg1	site					594:597	the site	590:597	the site of modification	590:613	The glycan moiety and the site of modification have been identified with mass spectrometry and confirmed by carbohydrate composition analysis, Edman degradation, and one- and two-dimensional NMR studies.
2023947	4	47	theme	composition	689:699	arg1	analysis					701:708	carbohydrate composition analysis	676:708	carbohydrate composition analysis	676:708	The glycan moiety and the site of modification have been identified with mass spectrometry and confirmed by carbohydrate composition analysis, Edman degradation, and one- and two-dimensional NMR studies.
2023947	5	48	theme	analysis	948:955	arg1	conditions					919:928	standard acidic conditions	903:928	standard acidic conditions of the amino acid analysis and Edman sequencing	903:976	This type of modification is normally not detected without mass spectrometry because the fucose-threonine bond is hydrolyzed under standard acidic conditions of the amino acid analysis and Edman sequencing.
2023947	3	49	attach	attached	502:509	arg3	peptide					540:546	the peptide	536:546	the peptide	536:546	An unusual carbohydrate-protein linkage, a single monosaccharide, fucose, covalently attached directly to threonine in the peptide, is described here.
2023947	3	49	attach	attached	502:509	arg1	threonine					523:531	threonine	523:531	threonine	523:531	An unusual carbohydrate-protein linkage, a single monosaccharide, fucose, covalently attached directly to threonine in the peptide, is described here.
2023947	3	49	attach	attached	502:509	arg2	monosaccharide					467:480	a single monosaccharide	458:480	a single monosaccharide	458:480	An unusual carbohydrate-protein linkage, a single monosaccharide, fucose, covalently attached directly to threonine in the peptide, is described here.
2023947	3	49	attach	attached	502:509	arg2	linkage					449:455	An unusual carbohydrate-protein linkage	417:455	An unusual carbohydrate-protein linkage	417:455	An unusual carbohydrate-protein linkage, a single monosaccharide, fucose, covalently attached directly to threonine in the peptide, is described here.
2023947	3	49	attach	attached	502:509	arg2	fucose					483:488	fucose	483:488	fucose	483:488	An unusual carbohydrate-protein linkage, a single monosaccharide, fucose, covalently attached directly to threonine in the peptide, is described here.
2023947	2	50	theme	responsible	370:380	arg1	region					330:335	the region	326:335	the region of urinary plasminogen activator responsible for its specific receptor binding	326:414	This is the region of urinary plasminogen activator responsible for its specific receptor binding.
2023947	2	50	theme	responsible	370:380	arg1	This					318:321	This	318:321	This	318:321	This is the region of urinary plasminogen activator responsible for its specific receptor binding.
2023947	0	51	theme	factor	67:72	arg1	activator					104:112	urinary plasminogen activator	84:112	urinary plasminogen activator	84:112	Characterization of a posttranslational fucosylation in the growth factor domain of urinary plasminogen activator.
2023947	0	51	theme	factor	67:72	arg1	domain					74:79	the growth factor domain	56:79	the growth factor domain of urinary plasminogen activator	56:112	Characterization of a posttranslational fucosylation in the growth factor domain of urinary plasminogen activator.
2023947	2	52	theme	activator	360:368	arg1	region					330:335	the region	326:335	the region of urinary plasminogen activator responsible for its specific receptor binding	326:414	This is the region of urinary plasminogen activator responsible for its specific receptor binding.
2023947	2	52	theme	activator	360:368	arg1	This					318:321	This	318:321	This	318:321	This is the region of urinary plasminogen activator responsible for its specific receptor binding.
1900431	5	0	theme	Bowes	667:671	arg1	line					687:690	the Bowes melanoma cell line	663:690	the Bowes melanoma cell line	663:690	Fucosylation of threonine-61 was observed in t-PA isolated from the Bowes melanoma cell line and from recombinant expression systems using Chinese hamster ovary or human embryonic kidney cells.
1900431	5	1	theme	embryonic	769:777	arg1	kidney					779:784	human embryonic kidney	763:784	human embryonic kidney	763:784	Fucosylation of threonine-61 was observed in t-PA isolated from the Bowes melanoma cell line and from recombinant expression systems using Chinese hamster ovary or human embryonic kidney cells.
1900431	5	2	theme	melanoma	673:680	arg1	line					687:690	the Bowes melanoma cell line	663:690	the Bowes melanoma cell line	663:690	Fucosylation of threonine-61 was observed in t-PA isolated from the Bowes melanoma cell line and from recombinant expression systems using Chinese hamster ovary or human embryonic kidney cells.
1900431	5	3	theme	threonine-61	615:626	arg1	Fucosylation					599:610	Fucosylation	599:610	Fucosylation of threonine-61	599:626	Fucosylation of threonine-61 was observed in t-PA isolated from the Bowes melanoma cell line and from recombinant expression systems using Chinese hamster ovary or human embryonic kidney cells.
1900431	6	4	gly	Fucosylation	793:804	arg1	residue					824:830	the homologous residue	809:830	the homologous residue	809:830	Fucosylation of the homologous residue in prourokinase has also been reported recently.
1900431	0	5	theme	growth	94:99	arg1	factor					101:106	epidermal growth factor	84:106	the epidermal growth factor domain	80:113	Tissue plasminogen activator has an O-linked fucose attached to threonine-61 in the epidermal growth factor domain.
1900431	4	6	theme	residue	512:518	arg1	susceptibility					483:496	The susceptibility	479:496	The susceptibility of the fucose residue to alpha-fucosidase	479:538	The susceptibility of the fucose residue to alpha-fucosidase indicated that it was in the alpha-anomeric configuration.
1900431	5	7	theme	cell	682:685	arg1	line					687:690	the Bowes melanoma cell line	663:690	the Bowes melanoma cell line	663:690	Fucosylation of threonine-61 was observed in t-PA isolated from the Bowes melanoma cell line and from recombinant expression systems using Chinese hamster ovary or human embryonic kidney cells.
1900431	2	8	theme	epidermal	282:290	arg1	factor					299:304	epidermal growth factor	282:304	the epidermal growth factor region of t-PA	278:319	The monosaccharide fucose is glycosidically linked to threonine-61 in the epidermal growth factor region of t-PA.
1900431	7	9	theme	novel	912:916	arg1	type					918:921	this novel type	907:921	this novel type of glycosylation	907:938	Our results indicate that this novel type of glycosylation may be common to the epidermal growth factor domains found in coagulation and fibrinolytic proteins and, therefore, suggest that the modification may have functional significance.
1900431	0	10	theme	epidermal	84:92	arg1	factor					101:106	epidermal growth factor	84:106	the epidermal growth factor domain	80:113	Tissue plasminogen activator has an O-linked fucose attached to threonine-61 in the epidermal growth factor domain.
1900431	7	11	theme	factor	978:983	arg1	domains					985:991	the epidermal growth factor domains	957:991	the epidermal growth factor domains found in coagulation and fibrinolytic proteins	957:1038	Our results indicate that this novel type of glycosylation may be common to the epidermal growth factor domains found in coagulation and fibrinolytic proteins and, therefore, suggest that the modification may have functional significance.
1900431	3	12	link	O-linked	338:345	arg1	fucose					347:352	O-linked fucose	338:352	O-linked fucose	338:352	The presence of O-linked fucose was demonstrated by carbohydrate analysis and mass spectrometry of tryptic and chymotryptic peptides that contain this site.
1900431	5	13	gly	Fucosylation	599:610	arg1	t-PA					644:647	t-PA	644:647	t-PA isolated from the Bowes melanoma cell line and from recombinant expression systems using Chinese hamster ovary or human embryonic kidney cells	644:790	Fucosylation of threonine-61 was observed in t-PA isolated from the Bowes melanoma cell line and from recombinant expression systems using Chinese hamster ovary or human embryonic kidney cells.
1900431	5	13	gly	Fucosylation	599:610	arg1	threonine-61					615:626	threonine-61	615:626	threonine-61	615:626	Fucosylation of threonine-61 was observed in t-PA isolated from the Bowes melanoma cell line and from recombinant expression systems using Chinese hamster ovary or human embryonic kidney cells.
1900431	5	14	theme	human	763:767	arg1	kidney					779:784	human embryonic kidney	763:784	human embryonic kidney	763:784	Fucosylation of threonine-61 was observed in t-PA isolated from the Bowes melanoma cell line and from recombinant expression systems using Chinese hamster ovary or human embryonic kidney cells.
1900431	7	15	dep	common	947:952	arg1	suggest					1056:1062	suggest	1056:1062	suggest that the modification may have functional significance	1056:1117	Our results indicate that this novel type of glycosylation may be common to the epidermal growth factor domains found in coagulation and fibrinolytic proteins and, therefore, suggest that the modification may have functional significance.
1900431	3	16	theme	tryptic	421:427	arg1	peptides					446:453	tryptic and chymotryptic peptides	421:453	tryptic and chymotryptic peptides that contain this site	421:476	The presence of O-linked fucose was demonstrated by carbohydrate analysis and mass spectrometry of tryptic and chymotryptic peptides that contain this site.
1900431	3	17	theme	chymotryptic	433:444	arg1	peptides					446:453	tryptic and chymotryptic peptides	421:453	tryptic and chymotryptic peptides that contain this site	421:476	The presence of O-linked fucose was demonstrated by carbohydrate analysis and mass spectrometry of tryptic and chymotryptic peptides that contain this site.
1900431	0	18	theme	factor	101:106	arg1	domain					108:113	the epidermal growth factor domain	80:113	the epidermal growth factor domain	80:113	Tissue plasminogen activator has an O-linked fucose attached to threonine-61 in the epidermal growth factor domain.
1900431	3	19	gly	carbohydrate	374:385	arg1	peptides					446:453	tryptic and chymotryptic peptides	421:453	tryptic and chymotryptic peptides that contain this site	421:476	The presence of O-linked fucose was demonstrated by carbohydrate analysis and mass spectrometry of tryptic and chymotryptic peptides that contain this site.
1900431	6	20	theme	residue	824:830	arg1	Fucosylation					793:804	Fucosylation	793:804	Fucosylation of the homologous residue in prourokinase	793:846	Fucosylation of the homologous residue in prourokinase has also been reported recently.
1900431	3	21	theme	peptides	446:453	arg1	analysis					387:394	carbohydrate analysis	374:394	carbohydrate analysis	374:394	The presence of O-linked fucose was demonstrated by carbohydrate analysis and mass spectrometry of tryptic and chymotryptic peptides that contain this site.
1900431	3	21	theme	peptides	446:453	arg1	spectrometry					405:416	mass spectrometry	400:416	mass spectrometry	400:416	The presence of O-linked fucose was demonstrated by carbohydrate analysis and mass spectrometry of tryptic and chymotryptic peptides that contain this site.
1900431	3	22	theme	carbohydrate	374:385	arg1	analysis					387:394	carbohydrate analysis	374:394	carbohydrate analysis	374:394	The presence of O-linked fucose was demonstrated by carbohydrate analysis and mass spectrometry of tryptic and chymotryptic peptides that contain this site.
1900431	0	23	contain	has	29:31	arg1	activator					19:27	Tissue plasminogen activator	0:27	Tissue plasminogen activator	0:27	Tissue plasminogen activator has an O-linked fucose attached to threonine-61 in the epidermal growth factor domain.
1900431	0	23	contain	has	29:31	arg2	fucose					45:50	an O-linked fucose	33:50	an O-linked fucose attached to threonine-61	33:75	Tissue plasminogen activator has an O-linked fucose attached to threonine-61 in the epidermal growth factor domain.
1900431	1	24	theme	tissue	171:176	arg1	t-PA					201:204	t-PA	201:204	t-PA	201:204	An unusual type of glycosylation has been observed for tissue plasminogen activator (t-PA).
1900431	1	24	theme	tissue	171:176	arg1	activator					190:198	tissue plasminogen activator	171:198	tissue plasminogen activator (t-PA)	171:205	An unusual type of glycosylation has been observed for tissue plasminogen activator (t-PA).
1900431	0	25	theme	Tissue	0:5	arg1	activator					19:27	Tissue plasminogen activator	0:27	Tissue plasminogen activator	0:27	Tissue plasminogen activator has an O-linked fucose attached to threonine-61 in the epidermal growth factor domain.
1900431	0	26	link	O-linked	36:43	arg1	fucose					45:50	an O-linked fucose	33:50	an O-linked fucose attached to threonine-61	33:75	Tissue plasminogen activator has an O-linked fucose attached to threonine-61 in the epidermal growth factor domain.
1900431	5	27	theme	ovary	754:758	arg1	cells					786:790	Chinese hamster ovary or human embryonic kidney cells	738:790	Chinese hamster ovary or human embryonic kidney cells	738:790	Fucosylation of threonine-61 was observed in t-PA isolated from the Bowes melanoma cell line and from recombinant expression systems using Chinese hamster ovary or human embryonic kidney cells.
1900431	1	28	theme	plasminogen	178:188	arg1	t-PA					201:204	t-PA	201:204	t-PA	201:204	An unusual type of glycosylation has been observed for tissue plasminogen activator (t-PA).
1900431	1	28	theme	plasminogen	178:188	arg1	activator					190:198	tissue plasminogen activator	171:198	tissue plasminogen activator (t-PA)	171:205	An unusual type of glycosylation has been observed for tissue plasminogen activator (t-PA).
1900431	7	29	theme	functional	1095:1104	arg1	significance					1106:1117	functional significance	1095:1117	functional significance	1095:1117	Our results indicate that this novel type of glycosylation may be common to the epidermal growth factor domains found in coagulation and fibrinolytic proteins and, therefore, suggest that the modification may have functional significance.
1900431	0	30	attach	attached	52:59	arg2	fucose					45:50	an O-linked fucose	33:50	an O-linked fucose attached to threonine-61	33:75	Tissue plasminogen activator has an O-linked fucose attached to threonine-61 in the epidermal growth factor domain.
1900431	0	30	attach	attached	52:59	arg1	threonine-61					64:75	threonine-61	64:75	threonine-61	64:75	Tissue plasminogen activator has an O-linked fucose attached to threonine-61 in the epidermal growth factor domain.
1900431	2	31	theme	factor	299:304	arg1	region					306:311	the epidermal growth factor region	278:311	the epidermal growth factor region of t-PA	278:319	The monosaccharide fucose is glycosidically linked to threonine-61 in the epidermal growth factor region of t-PA.
1900431	5	32	located	observed	632:639	arg1	t-PA					644:647	t-PA	644:647	t-PA isolated from the Bowes melanoma cell line and from recombinant expression systems using Chinese hamster ovary or human embryonic kidney cells	644:790	Fucosylation of threonine-61 was observed in t-PA isolated from the Bowes melanoma cell line and from recombinant expression systems using Chinese hamster ovary or human embryonic kidney cells.
1900431	5	32	located	observed	632:639	arg2	Fucosylation					599:610	Fucosylation	599:610	Fucosylation of threonine-61	599:626	Fucosylation of threonine-61 was observed in t-PA isolated from the Bowes melanoma cell line and from recombinant expression systems using Chinese hamster ovary or human embryonic kidney cells.
1900431	4	33	theme	alpha-anomeric	569:582	arg1	configuration					584:596	the alpha-anomeric configuration	565:596	the alpha-anomeric configuration	565:596	The susceptibility of the fucose residue to alpha-fucosidase indicated that it was in the alpha-anomeric configuration.
1900431	3	34	contain	contain	460:466	arg2	site					473:476	this site	468:476	this site	468:476	The presence of O-linked fucose was demonstrated by carbohydrate analysis and mass spectrometry of tryptic and chymotryptic peptides that contain this site.
1900431	3	34	contain	contain	460:466	arg1	peptides					446:453	tryptic and chymotryptic peptides	421:453	tryptic and chymotryptic peptides that contain this site	421:476	The presence of O-linked fucose was demonstrated by carbohydrate analysis and mass spectrometry of tryptic and chymotryptic peptides that contain this site.
1900431	2	35	theme	growth	292:297	arg1	factor					299:304	epidermal growth factor	282:304	the epidermal growth factor region of t-PA	278:319	The monosaccharide fucose is glycosidically linked to threonine-61 in the epidermal growth factor region of t-PA.
1900431	7	36	contain	have	1090:1093	arg2	significance					1106:1117	functional significance	1095:1117	functional significance	1095:1117	Our results indicate that this novel type of glycosylation may be common to the epidermal growth factor domains found in coagulation and fibrinolytic proteins and, therefore, suggest that the modification may have functional significance.
1900431	7	36	contain	have	1090:1093	arg1	modification					1073:1084	the modification	1069:1084	the modification	1069:1084	Our results indicate that this novel type of glycosylation may be common to the epidermal growth factor domains found in coagulation and fibrinolytic proteins and, therefore, suggest that the modification may have functional significance.
1900431	0	37	theme	O-linked	36:43	arg1	fucose					45:50	an O-linked fucose	33:50	an O-linked fucose attached to threonine-61	33:75	Tissue plasminogen activator has an O-linked fucose attached to threonine-61 in the epidermal growth factor domain.
1900431	5	38	theme	Chinese	738:744	arg1	ovary					754:758	Chinese hamster ovary	738:758	Chinese hamster ovary	738:758	Fucosylation of threonine-61 was observed in t-PA isolated from the Bowes melanoma cell line and from recombinant expression systems using Chinese hamster ovary or human embryonic kidney cells.
1900431	7	39	located	found	993:997	arg1	coagulation					1002:1012	coagulation	1002:1012	coagulation	1002:1012	Our results indicate that this novel type of glycosylation may be common to the epidermal growth factor domains found in coagulation and fibrinolytic proteins and, therefore, suggest that the modification may have functional significance.
1900431	7	39	located	found	993:997	arg1	proteins					1031:1038	fibrinolytic proteins	1018:1038	fibrinolytic proteins	1018:1038	Our results indicate that this novel type of glycosylation may be common to the epidermal growth factor domains found in coagulation and fibrinolytic proteins and, therefore, suggest that the modification may have functional significance.
1900431	7	39	located	found	993:997	arg2	domains					985:991	the epidermal growth factor domains	957:991	the epidermal growth factor domains found in coagulation and fibrinolytic proteins	957:1038	Our results indicate that this novel type of glycosylation may be common to the epidermal growth factor domains found in coagulation and fibrinolytic proteins and, therefore, suggest that the modification may have functional significance.
1900431	5	40	theme	hamster	746:752	arg1	ovary					754:758	Chinese hamster ovary	738:758	Chinese hamster ovary	738:758	Fucosylation of threonine-61 was observed in t-PA isolated from the Bowes melanoma cell line and from recombinant expression systems using Chinese hamster ovary or human embryonic kidney cells.
1900431	2	41	theme	monosaccharide	212:225	arg1	fucose					227:232	The monosaccharide fucose	208:232	The monosaccharide fucose	208:232	The monosaccharide fucose is glycosidically linked to threonine-61 in the epidermal growth factor region of t-PA.
1900431	3	42	theme	O-linked	338:345	arg1	fucose					347:352	O-linked fucose	338:352	O-linked fucose	338:352	The presence of O-linked fucose was demonstrated by carbohydrate analysis and mass spectrometry of tryptic and chymotryptic peptides that contain this site.
1900431	3	43	theme	fucose	347:352	arg1	presence					326:333	The presence	322:333	The presence of O-linked fucose	322:352	The presence of O-linked fucose was demonstrated by carbohydrate analysis and mass spectrometry of tryptic and chymotryptic peptides that contain this site.
1900431	3	44	theme	mass	400:403	arg1	spectrometry					405:416	mass spectrometry	400:416	mass spectrometry	400:416	The presence of O-linked fucose was demonstrated by carbohydrate analysis and mass spectrometry of tryptic and chymotryptic peptides that contain this site.
1900431	5	45	theme	recombinant	701:711	arg1	systems					724:730	recombinant expression systems	701:730	recombinant expression systems using Chinese hamster ovary or human embryonic kidney cells	701:790	Fucosylation of threonine-61 was observed in t-PA isolated from the Bowes melanoma cell line and from recombinant expression systems using Chinese hamster ovary or human embryonic kidney cells.
1900431	7	46	theme	epidermal	961:969	arg1	factor					978:983	epidermal growth factor	961:983	the epidermal growth factor domains found in coagulation and fibrinolytic proteins	957:1038	Our results indicate that this novel type of glycosylation may be common to the epidermal growth factor domains found in coagulation and fibrinolytic proteins and, therefore, suggest that the modification may have functional significance.
1900431	1	47	theme	unusual	119:125	arg1	type					127:130	An unusual type	116:130	An unusual type of glycosylation	116:147	An unusual type of glycosylation has been observed for tissue plasminogen activator (t-PA).
1900431	2	48	from	threonine-61	262:273	arg1	region					306:311	the epidermal growth factor region	278:311	the epidermal growth factor region of t-PA	278:319	The monosaccharide fucose is glycosidically linked to threonine-61 in the epidermal growth factor region of t-PA.
1900431	2	49	attach	linked	252:257	arg1	threonine-61					262:273	threonine-61	262:273	threonine-61 in the epidermal growth factor region of t-PA	262:319	The monosaccharide fucose is glycosidically linked to threonine-61 in the epidermal growth factor region of t-PA.
1900431	2	49	attach	linked	252:257	arg2	fucose					227:232	The monosaccharide fucose	208:232	The monosaccharide fucose	208:232	The monosaccharide fucose is glycosidically linked to threonine-61 in the epidermal growth factor region of t-PA.
1900431	5	50	theme	expression	713:722	arg1	systems					724:730	recombinant expression systems	701:730	recombinant expression systems using Chinese hamster ovary or human embryonic kidney cells	701:790	Fucosylation of threonine-61 was observed in t-PA isolated from the Bowes melanoma cell line and from recombinant expression systems using Chinese hamster ovary or human embryonic kidney cells.
1900431	7	51	theme	fibrinolytic	1018:1029	arg1	proteins					1031:1038	fibrinolytic proteins	1018:1038	fibrinolytic proteins	1018:1038	Our results indicate that this novel type of glycosylation may be common to the epidermal growth factor domains found in coagulation and fibrinolytic proteins and, therefore, suggest that the modification may have functional significance.
1900431	2	52	theme	t-PA	316:319	arg1	region					306:311	the epidermal growth factor region	278:311	the epidermal growth factor region of t-PA	278:319	The monosaccharide fucose is glycosidically linked to threonine-61 in the epidermal growth factor region of t-PA.
1900431	7	53	theme	glycosylation	926:938	arg1	type					918:921	this novel type	907:921	this novel type of glycosylation	907:938	Our results indicate that this novel type of glycosylation may be common to the epidermal growth factor domains found in coagulation and fibrinolytic proteins and, therefore, suggest that the modification may have functional significance.
1900431	6	54	from	Fucosylation	793:804	arg1	prourokinase					835:846	prourokinase	835:846	prourokinase	835:846	Fucosylation of the homologous residue in prourokinase has also been reported recently.
1900431	5	55	theme	kidney	779:784	arg1	cells					786:790	Chinese hamster ovary or human embryonic kidney cells	738:790	Chinese hamster ovary or human embryonic kidney cells	738:790	Fucosylation of threonine-61 was observed in t-PA isolated from the Bowes melanoma cell line and from recombinant expression systems using Chinese hamster ovary or human embryonic kidney cells.
1900431	6	56	theme	homologous	813:822	arg1	residue					824:830	the homologous residue	809:830	the homologous residue	809:830	Fucosylation of the homologous residue in prourokinase has also been reported recently.
1900431	7	57	theme	growth	971:976	arg1	factor					978:983	epidermal growth factor	961:983	the epidermal growth factor domains found in coagulation and fibrinolytic proteins	957:1038	Our results indicate that this novel type of glycosylation may be common to the epidermal growth factor domains found in coagulation and fibrinolytic proteins and, therefore, suggest that the modification may have functional significance.
1900431	4	58	theme	fucose	505:510	arg1	residue					512:518	the fucose residue	501:518	the fucose residue	501:518	The susceptibility of the fucose residue to alpha-fucosidase indicated that it was in the alpha-anomeric configuration.
1900431	1	59	theme	glycosylation	135:147	arg1	type					127:130	An unusual type	116:130	An unusual type of glycosylation	116:147	An unusual type of glycosylation has been observed for tissue plasminogen activator (t-PA).
1900431	5	60	attach	isolated	649:656	arg2	t-PA					644:647	t-PA	644:647	t-PA isolated from the Bowes melanoma cell line and from recombinant expression systems using Chinese hamster ovary or human embryonic kidney cells	644:790	Fucosylation of threonine-61 was observed in t-PA isolated from the Bowes melanoma cell line and from recombinant expression systems using Chinese hamster ovary or human embryonic kidney cells.
1900431	5	60	attach	isolated	649:656	arg1	systems					724:730	recombinant expression systems	701:730	recombinant expression systems using Chinese hamster ovary or human embryonic kidney cells	701:790	Fucosylation of threonine-61 was observed in t-PA isolated from the Bowes melanoma cell line and from recombinant expression systems using Chinese hamster ovary or human embryonic kidney cells.
1900431	5	60	attach	isolated	649:656	arg1	line					687:690	the Bowes melanoma cell line	663:690	the Bowes melanoma cell line	663:690	Fucosylation of threonine-61 was observed in t-PA isolated from the Bowes melanoma cell line and from recombinant expression systems using Chinese hamster ovary or human embryonic kidney cells.
9425112	0	0	theme	blood	99:103	arg1	leucocytes					105:114	Sendai virus-induced human peripheral blood leucocytes	61:114	Sendai virus-induced human peripheral blood leucocytes	61:114	Identification of nine interferon-alpha subtypes produced by Sendai virus-induced human peripheral blood leucocytes.
9425112	2	1	theme	Sendai	493:498	arg1	leucocytes					537:546	Sendai virus-induced human peripheral blood leucocytes	493:546	Sendai virus-induced human peripheral blood leucocytes	493:546	To find out which of the described sequences are expressed in normal human leucocytes, we have isolated and partly characterized the components of a highly purified IFN-alpha preparation produced by Sendai virus-induced human peripheral blood leucocytes.
9425112	8	2	theme	intact	1173:1178	arg1	proteins					1180:1187	the intact proteins	1169:1187	the intact proteins	1169:1187	Molecular mass determination of the intact proteins by electrospray ionization MS showed that there are no other post-translational modifications in the IFN-alpha subtypes than the glycosylation of IFN-alpha2b and IFN-alpha14c.
9425112	2	3	theme	normal	356:361	arg1	leucocytes					369:378	normal human leucocytes	356:378	normal human leucocytes	356:378	To find out which of the described sequences are expressed in normal human leucocytes, we have isolated and partly characterized the components of a highly purified IFN-alpha preparation produced by Sendai virus-induced human peripheral blood leucocytes.
9425112	0	4	theme	peripheral	88:97	arg1	leucocytes					105:114	Sendai virus-induced human peripheral blood leucocytes	61:114	Sendai virus-induced human peripheral blood leucocytes	61:114	Identification of nine interferon-alpha subtypes produced by Sendai virus-induced human peripheral blood leucocytes.
9425112	9	5	theme	sequence	1374:1381	arg1	variant					1383:1389	Only one sequence variant	1365:1389	Only one sequence variant	1365:1389	Only one sequence variant was found for each subtype, suggesting that the other described gene sequences represent allelic variants or mutations that are more rarely found in the general population.
9425112	5	6	theme	major	954:958	arg1	subtype					960:966	the major subtype	950:966	the major subtype	950:966	IFN-alpha1a was the major subtype, comprising approx.
9425112	5	6	theme	major	954:958	arg1	IFN-alpha1a					934:944	IFN-alpha1a	934:944	IFN-alpha1a	934:944	IFN-alpha1a was the major subtype, comprising approx.
9425112	7	7	theme	only	1040:1043	arg1	subtype					1045:1051	the only subtype	1036:1051	the only subtype containing potential N-glycosylation sites	1036:1094	IFN-alpha14c, the only subtype containing potential N-glycosylation sites, was shown to be glycosylated at Asn-72.
9425112	7	7	theme	only	1040:1043	arg1	IFN-alpha14c					1022:1033	IFN-alpha14c	1022:1033	IFN-alpha14c	1022:1033	IFN-alpha14c, the only subtype containing potential N-glycosylation sites, was shown to be glycosylated at Asn-72.
9425112	8	8	theme	electrospray	1192:1203	arg1	MS					1216:1217	electrospray ionization MS	1192:1217	electrospray ionization MS	1192:1217	Molecular mass determination of the intact proteins by electrospray ionization MS showed that there are no other post-translational modifications in the IFN-alpha subtypes than the glycosylation of IFN-alpha2b and IFN-alpha14c.
9425112	8	9	theme	IFN-alpha	1290:1298	arg1	subtypes					1300:1307	the IFN-alpha subtypes	1286:1307	the IFN-alpha subtypes	1286:1307	Molecular mass determination of the intact proteins by electrospray ionization MS showed that there are no other post-translational modifications in the IFN-alpha subtypes than the glycosylation of IFN-alpha2b and IFN-alpha14c.
9425112	3	10	theme	N-terminal	590:599	arg1	sequencing					601:610	N-terminal sequencing	590:610	N-terminal sequencing	590:610	The identification protocol consisted of N-terminal sequencing and mass mapping of the proteins separated by reverse-phase HPLC and/or SDS/PAGE.
9425112	1	11	theme	potential	264:272	arg1	proteins					284:291	28 potential IFN-alpha proteins	261:291	28 potential IFN-alpha proteins	261:291	The human interferon-alpha (IFN-alpha) family is encoded by 13 different functional genes, and including all cloned sequence variants there are 28 potential IFN-alpha proteins.
9425112	7	12	contain	containing	1053:1062	arg2	sites					1090:1094	potential N-glycosylation sites	1064:1094	potential N-glycosylation sites	1064:1094	IFN-alpha14c, the only subtype containing potential N-glycosylation sites, was shown to be glycosylated at Asn-72.
9425112	7	12	contain	containing	1053:1062	arg1	subtype					1045:1051	the only subtype	1036:1051	the only subtype containing potential N-glycosylation sites	1036:1094	IFN-alpha14c, the only subtype containing potential N-glycosylation sites, was shown to be glycosylated at Asn-72.
9425112	7	12	contain	containing	1053:1062	arg1	IFN-alpha14c					1022:1033	IFN-alpha14c	1022:1033	IFN-alpha14c	1022:1033	IFN-alpha14c, the only subtype containing potential N-glycosylation sites, was shown to be glycosylated at Asn-72.
9425112	9	13	located	found	1531:1535	arg2	variants					1488:1495	allelic variants	1480:1495	allelic variants	1480:1495	Only one sequence variant was found for each subtype, suggesting that the other described gene sequences represent allelic variants or mutations that are more rarely found in the general population.
9425112	9	13	located	found	1531:1535	arg2	mutations					1500:1508	mutations	1500:1508	mutations	1500:1508	Only one sequence variant was found for each subtype, suggesting that the other described gene sequences represent allelic variants or mutations that are more rarely found in the general population.
9425112	9	13	located	found	1531:1535	arg1	population					1552:1561	the general population	1540:1561	the general population	1540:1561	Only one sequence variant was found for each subtype, suggesting that the other described gene sequences represent allelic variants or mutations that are more rarely found in the general population.
9425112	2	14	dep	find	297:300	arg1	out					302:304	out	302:304	out	302:304	To find out which of the described sequences are expressed in normal human leucocytes, we have isolated and partly characterized the components of a highly purified IFN-alpha preparation produced by Sendai virus-induced human peripheral blood leucocytes.
9425112	1	15	theme	IFN-alpha	274:282	arg1	proteins					284:291	28 potential IFN-alpha proteins	261:291	28 potential IFN-alpha proteins	261:291	The human interferon-alpha (IFN-alpha) family is encoded by 13 different functional genes, and including all cloned sequence variants there are 28 potential IFN-alpha proteins.
9425112	2	16	theme	blood	531:535	arg1	leucocytes					537:546	Sendai virus-induced human peripheral blood leucocytes	493:546	Sendai virus-induced human peripheral blood leucocytes	493:546	To find out which of the described sequences are expressed in normal human leucocytes, we have isolated and partly characterized the components of a highly purified IFN-alpha preparation produced by Sendai virus-induced human peripheral blood leucocytes.
9425112	4	17	dep	species	801:807	arg1	IFN-alpha7a					849:859	IFN-alpha7a	849:859	IFN-alpha7a	849:859	The highly purified leucocyte IFN-alpha preparation was found to contain at least nine different IFN-alpha species: IFN-alpha1a, IFN-alpha2b, IFN-alpha4b, IFN-alpha7a, IFN-alpha8b, IFN-alpha10a, IFN-alpha14c, IFN-alpha17b and IFN-alpha21b.
9425112	4	17	dep	species	801:807	arg1	IFN-alpha14c					889:900	IFN-alpha14c	889:900	IFN-alpha14c	889:900	The highly purified leucocyte IFN-alpha preparation was found to contain at least nine different IFN-alpha species: IFN-alpha1a, IFN-alpha2b, IFN-alpha4b, IFN-alpha7a, IFN-alpha8b, IFN-alpha10a, IFN-alpha14c, IFN-alpha17b and IFN-alpha21b.
9425112	4	17	dep	species	801:807	arg1	IFN-alpha1a					810:820	IFN-alpha1a	810:820	IFN-alpha1a	810:820	The highly purified leucocyte IFN-alpha preparation was found to contain at least nine different IFN-alpha species: IFN-alpha1a, IFN-alpha2b, IFN-alpha4b, IFN-alpha7a, IFN-alpha8b, IFN-alpha10a, IFN-alpha14c, IFN-alpha17b and IFN-alpha21b.
9425112	4	17	dep	species	801:807	arg1	IFN-alpha17b					903:914	IFN-alpha17b	903:914	IFN-alpha17b	903:914	The highly purified leucocyte IFN-alpha preparation was found to contain at least nine different IFN-alpha species: IFN-alpha1a, IFN-alpha2b, IFN-alpha4b, IFN-alpha7a, IFN-alpha8b, IFN-alpha10a, IFN-alpha14c, IFN-alpha17b and IFN-alpha21b.
9425112	4	17	dep	species	801:807	arg1	IFN-alpha2b					823:833	IFN-alpha2b	823:833	IFN-alpha2b	823:833	The highly purified leucocyte IFN-alpha preparation was found to contain at least nine different IFN-alpha species: IFN-alpha1a, IFN-alpha2b, IFN-alpha4b, IFN-alpha7a, IFN-alpha8b, IFN-alpha10a, IFN-alpha14c, IFN-alpha17b and IFN-alpha21b.
9425112	4	17	dep	species	801:807	arg1	IFN-alpha8b					862:872	IFN-alpha8b	862:872	IFN-alpha8b	862:872	The highly purified leucocyte IFN-alpha preparation was found to contain at least nine different IFN-alpha species: IFN-alpha1a, IFN-alpha2b, IFN-alpha4b, IFN-alpha7a, IFN-alpha8b, IFN-alpha10a, IFN-alpha14c, IFN-alpha17b and IFN-alpha21b.
9425112	4	17	dep	species	801:807	arg1	IFN-alpha10a					875:886	IFN-alpha10a	875:886	IFN-alpha10a	875:886	The highly purified leucocyte IFN-alpha preparation was found to contain at least nine different IFN-alpha species: IFN-alpha1a, IFN-alpha2b, IFN-alpha4b, IFN-alpha7a, IFN-alpha8b, IFN-alpha10a, IFN-alpha14c, IFN-alpha17b and IFN-alpha21b.
9425112	4	17	dep	species	801:807	arg1	IFN-alpha21b					920:931	IFN-alpha21b	920:931	IFN-alpha21b	920:931	The highly purified leucocyte IFN-alpha preparation was found to contain at least nine different IFN-alpha species: IFN-alpha1a, IFN-alpha2b, IFN-alpha4b, IFN-alpha7a, IFN-alpha8b, IFN-alpha10a, IFN-alpha14c, IFN-alpha17b and IFN-alpha21b.
9425112	4	17	dep	species	801:807	arg1	species					801:807	at least nine different IFN-alpha species	767:807	at least nine different IFN-alpha species: IFN-alpha1a, IFN-alpha2b, IFN-alpha4b, IFN-alpha7a, IFN-alpha8b, IFN-alpha10a, IFN-alpha14c, IFN-alpha17b and IFN-alpha21b	767:931	The highly purified leucocyte IFN-alpha preparation was found to contain at least nine different IFN-alpha species: IFN-alpha1a, IFN-alpha2b, IFN-alpha4b, IFN-alpha7a, IFN-alpha8b, IFN-alpha10a, IFN-alpha14c, IFN-alpha17b and IFN-alpha21b.
9425112	4	17	dep	species	801:807	arg1	IFN-alpha4b					836:846	IFN-alpha4b	836:846	IFN-alpha4b	836:846	The highly purified leucocyte IFN-alpha preparation was found to contain at least nine different IFN-alpha species: IFN-alpha1a, IFN-alpha2b, IFN-alpha4b, IFN-alpha7a, IFN-alpha8b, IFN-alpha10a, IFN-alpha14c, IFN-alpha17b and IFN-alpha21b.
9425112	9	18	theme	general	1544:1550	arg1	population					1552:1561	the general population	1540:1561	the general population	1540:1561	Only one sequence variant was found for each subtype, suggesting that the other described gene sequences represent allelic variants or mutations that are more rarely found in the general population.
9425112	4	19	theme	leucocyte	714:722	arg1	preparation					734:744	The highly purified leucocyte IFN-alpha preparation	694:744	The highly purified leucocyte IFN-alpha preparation	694:744	The highly purified leucocyte IFN-alpha preparation was found to contain at least nine different IFN-alpha species: IFN-alpha1a, IFN-alpha2b, IFN-alpha4b, IFN-alpha7a, IFN-alpha8b, IFN-alpha10a, IFN-alpha14c, IFN-alpha17b and IFN-alpha21b.
9425112	2	20	theme	peripheral	520:529	arg1	leucocytes					537:546	Sendai virus-induced human peripheral blood leucocytes	493:546	Sendai virus-induced human peripheral blood leucocytes	493:546	To find out which of the described sequences are expressed in normal human leucocytes, we have isolated and partly characterized the components of a highly purified IFN-alpha preparation produced by Sendai virus-induced human peripheral blood leucocytes.
9425112	3	21	theme	identification	553:566	arg1	protocol					568:575	The identification protocol	549:575	The identification protocol	549:575	The identification protocol consisted of N-terminal sequencing and mass mapping of the proteins separated by reverse-phase HPLC and/or SDS/PAGE.
9425112	1	22	theme	different	180:188	arg1	genes					201:205	13 different functional genes	177:205	13 different functional genes	177:205	The human interferon-alpha (IFN-alpha) family is encoded by 13 different functional genes, and including all cloned sequence variants there are 28 potential IFN-alpha proteins.
9425112	8	23	theme	other	1244:1248	arg1	modifications					1269:1281	no other post-translational modifications	1241:1281	no other post-translational modifications in the IFN-alpha subtypes	1241:1307	Molecular mass determination of the intact proteins by electrospray ionization MS showed that there are no other post-translational modifications in the IFN-alpha subtypes than the glycosylation of IFN-alpha2b and IFN-alpha14c.
9425112	4	24	contain	contain	759:765	arg2	IFN-alpha10a					875:886	IFN-alpha10a	875:886	IFN-alpha10a	875:886	The highly purified leucocyte IFN-alpha preparation was found to contain at least nine different IFN-alpha species: IFN-alpha1a, IFN-alpha2b, IFN-alpha4b, IFN-alpha7a, IFN-alpha8b, IFN-alpha10a, IFN-alpha14c, IFN-alpha17b and IFN-alpha21b.
9425112	4	24	contain	contain	759:765	arg2	IFN-alpha21b					920:931	IFN-alpha21b	920:931	IFN-alpha21b	920:931	The highly purified leucocyte IFN-alpha preparation was found to contain at least nine different IFN-alpha species: IFN-alpha1a, IFN-alpha2b, IFN-alpha4b, IFN-alpha7a, IFN-alpha8b, IFN-alpha10a, IFN-alpha14c, IFN-alpha17b and IFN-alpha21b.
9425112	4	24	contain	contain	759:765	arg2	species					801:807	at least nine different IFN-alpha species	767:807	at least nine different IFN-alpha species: IFN-alpha1a, IFN-alpha2b, IFN-alpha4b, IFN-alpha7a, IFN-alpha8b, IFN-alpha10a, IFN-alpha14c, IFN-alpha17b and IFN-alpha21b	767:931	The highly purified leucocyte IFN-alpha preparation was found to contain at least nine different IFN-alpha species: IFN-alpha1a, IFN-alpha2b, IFN-alpha4b, IFN-alpha7a, IFN-alpha8b, IFN-alpha10a, IFN-alpha14c, IFN-alpha17b and IFN-alpha21b.
9425112	4	24	contain	contain	759:765	arg1	preparation					734:744	The highly purified leucocyte IFN-alpha preparation	694:744	The highly purified leucocyte IFN-alpha preparation	694:744	The highly purified leucocyte IFN-alpha preparation was found to contain at least nine different IFN-alpha species: IFN-alpha1a, IFN-alpha2b, IFN-alpha4b, IFN-alpha7a, IFN-alpha8b, IFN-alpha10a, IFN-alpha14c, IFN-alpha17b and IFN-alpha21b.
9425112	4	24	contain	contain	759:765	arg2	IFN-alpha4b					836:846	IFN-alpha4b	836:846	IFN-alpha4b	836:846	The highly purified leucocyte IFN-alpha preparation was found to contain at least nine different IFN-alpha species: IFN-alpha1a, IFN-alpha2b, IFN-alpha4b, IFN-alpha7a, IFN-alpha8b, IFN-alpha10a, IFN-alpha14c, IFN-alpha17b and IFN-alpha21b.
9425112	4	24	contain	contain	759:765	arg2	IFN-alpha1a					810:820	IFN-alpha1a	810:820	IFN-alpha1a	810:820	The highly purified leucocyte IFN-alpha preparation was found to contain at least nine different IFN-alpha species: IFN-alpha1a, IFN-alpha2b, IFN-alpha4b, IFN-alpha7a, IFN-alpha8b, IFN-alpha10a, IFN-alpha14c, IFN-alpha17b and IFN-alpha21b.
9425112	4	24	contain	contain	759:765	arg2	IFN-alpha7a					849:859	IFN-alpha7a	849:859	IFN-alpha7a	849:859	The highly purified leucocyte IFN-alpha preparation was found to contain at least nine different IFN-alpha species: IFN-alpha1a, IFN-alpha2b, IFN-alpha4b, IFN-alpha7a, IFN-alpha8b, IFN-alpha10a, IFN-alpha14c, IFN-alpha17b and IFN-alpha21b.
9425112	4	24	contain	contain	759:765	arg2	IFN-alpha14c					889:900	IFN-alpha14c	889:900	IFN-alpha14c	889:900	The highly purified leucocyte IFN-alpha preparation was found to contain at least nine different IFN-alpha species: IFN-alpha1a, IFN-alpha2b, IFN-alpha4b, IFN-alpha7a, IFN-alpha8b, IFN-alpha10a, IFN-alpha14c, IFN-alpha17b and IFN-alpha21b.
9425112	4	24	contain	contain	759:765	arg2	IFN-alpha2b					823:833	IFN-alpha2b	823:833	IFN-alpha2b	823:833	The highly purified leucocyte IFN-alpha preparation was found to contain at least nine different IFN-alpha species: IFN-alpha1a, IFN-alpha2b, IFN-alpha4b, IFN-alpha7a, IFN-alpha8b, IFN-alpha10a, IFN-alpha14c, IFN-alpha17b and IFN-alpha21b.
9425112	4	24	contain	contain	759:765	arg2	IFN-alpha8b					862:872	IFN-alpha8b	862:872	IFN-alpha8b	862:872	The highly purified leucocyte IFN-alpha preparation was found to contain at least nine different IFN-alpha species: IFN-alpha1a, IFN-alpha2b, IFN-alpha4b, IFN-alpha7a, IFN-alpha8b, IFN-alpha10a, IFN-alpha14c, IFN-alpha17b and IFN-alpha21b.
9425112	4	24	contain	contain	759:765	arg2	IFN-alpha17b					903:914	IFN-alpha17b	903:914	IFN-alpha17b	903:914	The highly purified leucocyte IFN-alpha preparation was found to contain at least nine different IFN-alpha species: IFN-alpha1a, IFN-alpha2b, IFN-alpha4b, IFN-alpha7a, IFN-alpha8b, IFN-alpha10a, IFN-alpha14c, IFN-alpha17b and IFN-alpha21b.
9425112	2	25	theme	human	514:518	arg1	leucocytes					537:546	Sendai virus-induced human peripheral blood leucocytes	493:546	Sendai virus-induced human peripheral blood leucocytes	493:546	To find out which of the described sequences are expressed in normal human leucocytes, we have isolated and partly characterized the components of a highly purified IFN-alpha preparation produced by Sendai virus-induced human peripheral blood leucocytes.
9425112	4	26	theme	different	781:789	arg1	IFN-alpha7a					849:859	IFN-alpha7a	849:859	IFN-alpha7a	849:859	The highly purified leucocyte IFN-alpha preparation was found to contain at least nine different IFN-alpha species: IFN-alpha1a, IFN-alpha2b, IFN-alpha4b, IFN-alpha7a, IFN-alpha8b, IFN-alpha10a, IFN-alpha14c, IFN-alpha17b and IFN-alpha21b.
9425112	4	26	theme	different	781:789	arg1	IFN-alpha14c					889:900	IFN-alpha14c	889:900	IFN-alpha14c	889:900	The highly purified leucocyte IFN-alpha preparation was found to contain at least nine different IFN-alpha species: IFN-alpha1a, IFN-alpha2b, IFN-alpha4b, IFN-alpha7a, IFN-alpha8b, IFN-alpha10a, IFN-alpha14c, IFN-alpha17b and IFN-alpha21b.
9425112	4	26	theme	different	781:789	arg1	IFN-alpha1a					810:820	IFN-alpha1a	810:820	IFN-alpha1a	810:820	The highly purified leucocyte IFN-alpha preparation was found to contain at least nine different IFN-alpha species: IFN-alpha1a, IFN-alpha2b, IFN-alpha4b, IFN-alpha7a, IFN-alpha8b, IFN-alpha10a, IFN-alpha14c, IFN-alpha17b and IFN-alpha21b.
9425112	4	26	theme	different	781:789	arg1	IFN-alpha17b					903:914	IFN-alpha17b	903:914	IFN-alpha17b	903:914	The highly purified leucocyte IFN-alpha preparation was found to contain at least nine different IFN-alpha species: IFN-alpha1a, IFN-alpha2b, IFN-alpha4b, IFN-alpha7a, IFN-alpha8b, IFN-alpha10a, IFN-alpha14c, IFN-alpha17b and IFN-alpha21b.
9425112	4	26	theme	different	781:789	arg1	IFN-alpha2b					823:833	IFN-alpha2b	823:833	IFN-alpha2b	823:833	The highly purified leucocyte IFN-alpha preparation was found to contain at least nine different IFN-alpha species: IFN-alpha1a, IFN-alpha2b, IFN-alpha4b, IFN-alpha7a, IFN-alpha8b, IFN-alpha10a, IFN-alpha14c, IFN-alpha17b and IFN-alpha21b.
9425112	4	26	theme	different	781:789	arg1	IFN-alpha8b					862:872	IFN-alpha8b	862:872	IFN-alpha8b	862:872	The highly purified leucocyte IFN-alpha preparation was found to contain at least nine different IFN-alpha species: IFN-alpha1a, IFN-alpha2b, IFN-alpha4b, IFN-alpha7a, IFN-alpha8b, IFN-alpha10a, IFN-alpha14c, IFN-alpha17b and IFN-alpha21b.
9425112	4	26	theme	different	781:789	arg1	IFN-alpha10a					875:886	IFN-alpha10a	875:886	IFN-alpha10a	875:886	The highly purified leucocyte IFN-alpha preparation was found to contain at least nine different IFN-alpha species: IFN-alpha1a, IFN-alpha2b, IFN-alpha4b, IFN-alpha7a, IFN-alpha8b, IFN-alpha10a, IFN-alpha14c, IFN-alpha17b and IFN-alpha21b.
9425112	4	26	theme	different	781:789	arg1	IFN-alpha21b					920:931	IFN-alpha21b	920:931	IFN-alpha21b	920:931	The highly purified leucocyte IFN-alpha preparation was found to contain at least nine different IFN-alpha species: IFN-alpha1a, IFN-alpha2b, IFN-alpha4b, IFN-alpha7a, IFN-alpha8b, IFN-alpha10a, IFN-alpha14c, IFN-alpha17b and IFN-alpha21b.
9425112	4	26	theme	different	781:789	arg1	species					801:807	at least nine different IFN-alpha species	767:807	at least nine different IFN-alpha species: IFN-alpha1a, IFN-alpha2b, IFN-alpha4b, IFN-alpha7a, IFN-alpha8b, IFN-alpha10a, IFN-alpha14c, IFN-alpha17b and IFN-alpha21b	767:931	The highly purified leucocyte IFN-alpha preparation was found to contain at least nine different IFN-alpha species: IFN-alpha1a, IFN-alpha2b, IFN-alpha4b, IFN-alpha7a, IFN-alpha8b, IFN-alpha10a, IFN-alpha14c, IFN-alpha17b and IFN-alpha21b.
9425112	4	26	theme	different	781:789	arg1	IFN-alpha4b					836:846	IFN-alpha4b	836:846	IFN-alpha4b	836:846	The highly purified leucocyte IFN-alpha preparation was found to contain at least nine different IFN-alpha species: IFN-alpha1a, IFN-alpha2b, IFN-alpha4b, IFN-alpha7a, IFN-alpha8b, IFN-alpha10a, IFN-alpha14c, IFN-alpha17b and IFN-alpha21b.
9425112	1	27	theme	functional	190:199	arg1	genes					201:205	13 different functional genes	177:205	13 different functional genes	177:205	The human interferon-alpha (IFN-alpha) family is encoded by 13 different functional genes, and including all cloned sequence variants there are 28 potential IFN-alpha proteins.
9425112	4	28	theme	purified	705:712	arg1	preparation					734:744	The highly purified leucocyte IFN-alpha preparation	694:744	The highly purified leucocyte IFN-alpha preparation	694:744	The highly purified leucocyte IFN-alpha preparation was found to contain at least nine different IFN-alpha species: IFN-alpha1a, IFN-alpha2b, IFN-alpha4b, IFN-alpha7a, IFN-alpha8b, IFN-alpha10a, IFN-alpha14c, IFN-alpha17b and IFN-alpha21b.
9425112	0	29	theme	interferon-alpha	23:38	arg1	subtypes					40:47	nine interferon-alpha subtypes	18:47	nine interferon-alpha subtypes	18:47	Identification of nine interferon-alpha subtypes produced by Sendai virus-induced human peripheral blood leucocytes.
9425112	8	30	theme	Molecular	1137:1145	arg1	determination					1152:1164	Molecular mass determination	1137:1164	Molecular mass determination of the intact proteins by electrospray ionization MS	1137:1217	Molecular mass determination of the intact proteins by electrospray ionization MS showed that there are no other post-translational modifications in the IFN-alpha subtypes than the glycosylation of IFN-alpha2b and IFN-alpha14c.
9425112	8	31	theme	post-translational	1250:1267	arg1	modifications					1269:1281	no other post-translational modifications	1241:1281	no other post-translational modifications in the IFN-alpha subtypes	1241:1307	Molecular mass determination of the intact proteins by electrospray ionization MS showed that there are no other post-translational modifications in the IFN-alpha subtypes than the glycosylation of IFN-alpha2b and IFN-alpha14c.
9425112	6	32	theme	IFN-alpha	1011:1019	arg1	IFN-alpha					1011:1019	total leucocyte IFN-alpha	995:1019	total leucocyte IFN-alpha	995:1019	30% of total leucocyte IFN-alpha.
9425112	6	32	theme	IFN-alpha	1011:1019	arg1	%					990:990	30%	988:990	30% of total leucocyte IFN-alpha.	988:1020	30% of total leucocyte IFN-alpha.
9425112	7	33	gly	glycosylated	1113:1124	arg2	Asn-72					1129:1134	Asn-72	1129:1134	Asn-72	1129:1134	IFN-alpha14c, the only subtype containing potential N-glycosylation sites, was shown to be glycosylated at Asn-72.
9425112	7	33	gly	glycosylated	1113:1124	arg1	subtype					1045:1051	the only subtype	1036:1051	the only subtype containing potential N-glycosylation sites	1036:1094	IFN-alpha14c, the only subtype containing potential N-glycosylation sites, was shown to be glycosylated at Asn-72.
9425112	7	33	gly	glycosylated	1113:1124	arg1	IFN-alpha14c					1022:1033	IFN-alpha14c	1022:1033	IFN-alpha14c	1022:1033	IFN-alpha14c, the only subtype containing potential N-glycosylation sites, was shown to be glycosylated at Asn-72.
9425112	1	34	theme	human	121:125	arg1	IFN-alpha					145:153	IFN-alpha	145:153	IFN-alpha	145:153	The human interferon-alpha (IFN-alpha) family is encoded by 13 different functional genes, and including all cloned sequence variants there are 28 potential IFN-alpha proteins.
9425112	1	34	theme	human	121:125	arg1	interferon-alpha					127:142	human interferon-alpha	121:142	The human interferon-alpha (IFN-alpha) family	117:161	The human interferon-alpha (IFN-alpha) family is encoded by 13 different functional genes, and including all cloned sequence variants there are 28 potential IFN-alpha proteins.
9425112	8	35	theme	ionization	1205:1214	arg1	MS					1216:1217	electrospray ionization MS	1192:1217	electrospray ionization MS	1192:1217	Molecular mass determination of the intact proteins by electrospray ionization MS showed that there are no other post-translational modifications in the IFN-alpha subtypes than the glycosylation of IFN-alpha2b and IFN-alpha14c.
9425112	8	36	theme	IFN-alpha2b	1335:1345	arg1	glycosylation					1318:1330	the glycosylation	1314:1330	the glycosylation of IFN-alpha2b and IFN-alpha14c	1314:1362	Molecular mass determination of the intact proteins by electrospray ionization MS showed that there are no other post-translational modifications in the IFN-alpha subtypes than the glycosylation of IFN-alpha2b and IFN-alpha14c.
9425112	0	37	theme	virus-induced	68:80	arg1	leucocytes					105:114	Sendai virus-induced human peripheral blood leucocytes	61:114	Sendai virus-induced human peripheral blood leucocytes	61:114	Identification of nine interferon-alpha subtypes produced by Sendai virus-induced human peripheral blood leucocytes.
9425112	6	38	theme	leucocyte	1001:1009	arg1	IFN-alpha					1011:1019	total leucocyte IFN-alpha	995:1019	total leucocyte IFN-alpha	995:1019	30% of total leucocyte IFN-alpha.
9425112	0	39	theme	subtypes	40:47	arg1	Identification					0:13	Identification	0:13	Identification of nine interferon-alpha subtypes	0:47	Identification of nine interferon-alpha subtypes produced by Sendai virus-induced human peripheral blood leucocytes.
9425112	6	40	theme	total	995:999	arg1	IFN-alpha					1011:1019	total leucocyte IFN-alpha	995:1019	total leucocyte IFN-alpha	995:1019	30% of total leucocyte IFN-alpha.
9425112	2	41	theme	preparation	469:479	arg1	components					427:436	the components	423:436	the components of a highly purified IFN-alpha preparation produced by Sendai virus-induced human peripheral blood leucocytes	423:546	To find out which of the described sequences are expressed in normal human leucocytes, we have isolated and partly characterized the components of a highly purified IFN-alpha preparation produced by Sendai virus-induced human peripheral blood leucocytes.
9425112	8	42	gly	glycosylation	1318:1330	arg1	IFN-alpha14c					1351:1362	IFN-alpha14c	1351:1362	IFN-alpha14c	1351:1362	Molecular mass determination of the intact proteins by electrospray ionization MS showed that there are no other post-translational modifications in the IFN-alpha subtypes than the glycosylation of IFN-alpha2b and IFN-alpha14c.
9425112	8	42	gly	glycosylation	1318:1330	arg1	IFN-alpha2b					1335:1345	IFN-alpha2b	1335:1345	IFN-alpha2b	1335:1345	Molecular mass determination of the intact proteins by electrospray ionization MS showed that there are no other post-translational modifications in the IFN-alpha subtypes than the glycosylation of IFN-alpha2b and IFN-alpha14c.
9425112	7	43	theme	N-glycosylation	1074:1088	arg1	sites					1090:1094	potential N-glycosylation sites	1064:1094	potential N-glycosylation sites	1064:1094	IFN-alpha14c, the only subtype containing potential N-glycosylation sites, was shown to be glycosylated at Asn-72.
9425112	8	44	theme	IFN-alpha14c	1351:1362	arg1	glycosylation					1318:1330	the glycosylation	1314:1330	the glycosylation of IFN-alpha2b and IFN-alpha14c	1314:1362	Molecular mass determination of the intact proteins by electrospray ionization MS showed that there are no other post-translational modifications in the IFN-alpha subtypes than the glycosylation of IFN-alpha2b and IFN-alpha14c.
9425112	2	45	theme	IFN-alpha	459:467	arg1	preparation					469:479	a highly purified IFN-alpha preparation	441:479	a highly purified IFN-alpha preparation produced by Sendai virus-induced human peripheral blood leucocytes	441:546	To find out which of the described sequences are expressed in normal human leucocytes, we have isolated and partly characterized the components of a highly purified IFN-alpha preparation produced by Sendai virus-induced human peripheral blood leucocytes.
9425112	7	46	gly	N-glycosylation	1074:1088	arg2	sites					1090:1094	potential N-glycosylation sites	1064:1094	potential N-glycosylation sites	1064:1094	IFN-alpha14c, the only subtype containing potential N-glycosylation sites, was shown to be glycosylated at Asn-72.
9425112	2	47	theme	virus-induced	500:512	arg1	leucocytes					537:546	Sendai virus-induced human peripheral blood leucocytes	493:546	Sendai virus-induced human peripheral blood leucocytes	493:546	To find out which of the described sequences are expressed in normal human leucocytes, we have isolated and partly characterized the components of a highly purified IFN-alpha preparation produced by Sendai virus-induced human peripheral blood leucocytes.
9425112	3	48	theme	mass	616:619	arg1	mapping					621:627	mass mapping	616:627	mass mapping	616:627	The identification protocol consisted of N-terminal sequencing and mass mapping of the proteins separated by reverse-phase HPLC and/or SDS/PAGE.
9425112	1	49	theme	interferon-alpha	127:142	arg1	family					156:161	The human interferon-alpha (IFN-alpha) family	117:161	The human interferon-alpha (IFN-alpha) family	117:161	The human interferon-alpha (IFN-alpha) family is encoded by 13 different functional genes, and including all cloned sequence variants there are 28 potential IFN-alpha proteins.
9425112	2	50	theme	purified	450:457	arg1	preparation					469:479	a highly purified IFN-alpha preparation	441:479	a highly purified IFN-alpha preparation produced by Sendai virus-induced human peripheral blood leucocytes	441:546	To find out which of the described sequences are expressed in normal human leucocytes, we have isolated and partly characterized the components of a highly purified IFN-alpha preparation produced by Sendai virus-induced human peripheral blood leucocytes.
9425112	9	51	theme	described	1445:1453	arg1	sequences					1460:1468	the other described gene sequences	1435:1468	the other described gene sequences	1435:1468	Only one sequence variant was found for each subtype, suggesting that the other described gene sequences represent allelic variants or mutations that are more rarely found in the general population.
9425112	9	52	theme	gene	1455:1458	arg1	sequences					1460:1468	the other described gene sequences	1435:1468	the other described gene sequences	1435:1468	Only one sequence variant was found for each subtype, suggesting that the other described gene sequences represent allelic variants or mutations that are more rarely found in the general population.
9425112	8	53	theme	proteins	1180:1187	arg1	determination					1152:1164	Molecular mass determination	1137:1164	Molecular mass determination of the intact proteins by electrospray ionization MS	1137:1217	Molecular mass determination of the intact proteins by electrospray ionization MS showed that there are no other post-translational modifications in the IFN-alpha subtypes than the glycosylation of IFN-alpha2b and IFN-alpha14c.
9425112	4	54	theme	IFN-alpha	724:732	arg1	preparation					734:744	The highly purified leucocyte IFN-alpha preparation	694:744	The highly purified leucocyte IFN-alpha preparation	694:744	The highly purified leucocyte IFN-alpha preparation was found to contain at least nine different IFN-alpha species: IFN-alpha1a, IFN-alpha2b, IFN-alpha4b, IFN-alpha7a, IFN-alpha8b, IFN-alpha10a, IFN-alpha14c, IFN-alpha17b and IFN-alpha21b.
9425112	1	55	theme	cloned	226:231	arg1	variants					242:249	all cloned sequence variants	222:249	all cloned sequence variants	222:249	The human interferon-alpha (IFN-alpha) family is encoded by 13 different functional genes, and including all cloned sequence variants there are 28 potential IFN-alpha proteins.
9425112	7	56	theme	potential	1064:1072	arg1	sites					1090:1094	potential N-glycosylation sites	1064:1094	potential N-glycosylation sites	1064:1094	IFN-alpha14c, the only subtype containing potential N-glycosylation sites, was shown to be glycosylated at Asn-72.
9425112	3	57	theme	reverse-phase	658:670	arg1	HPLC					672:675	reverse-phase HPLC	658:675	reverse-phase HPLC	658:675	The identification protocol consisted of N-terminal sequencing and mass mapping of the proteins separated by reverse-phase HPLC and/or SDS/PAGE.
9425112	4	58	theme	IFN-alpha	791:799	arg1	IFN-alpha7a					849:859	IFN-alpha7a	849:859	IFN-alpha7a	849:859	The highly purified leucocyte IFN-alpha preparation was found to contain at least nine different IFN-alpha species: IFN-alpha1a, IFN-alpha2b, IFN-alpha4b, IFN-alpha7a, IFN-alpha8b, IFN-alpha10a, IFN-alpha14c, IFN-alpha17b and IFN-alpha21b.
9425112	4	58	theme	IFN-alpha	791:799	arg1	IFN-alpha14c					889:900	IFN-alpha14c	889:900	IFN-alpha14c	889:900	The highly purified leucocyte IFN-alpha preparation was found to contain at least nine different IFN-alpha species: IFN-alpha1a, IFN-alpha2b, IFN-alpha4b, IFN-alpha7a, IFN-alpha8b, IFN-alpha10a, IFN-alpha14c, IFN-alpha17b and IFN-alpha21b.
9425112	4	58	theme	IFN-alpha	791:799	arg1	IFN-alpha1a					810:820	IFN-alpha1a	810:820	IFN-alpha1a	810:820	The highly purified leucocyte IFN-alpha preparation was found to contain at least nine different IFN-alpha species: IFN-alpha1a, IFN-alpha2b, IFN-alpha4b, IFN-alpha7a, IFN-alpha8b, IFN-alpha10a, IFN-alpha14c, IFN-alpha17b and IFN-alpha21b.
9425112	4	58	theme	IFN-alpha	791:799	arg1	IFN-alpha17b					903:914	IFN-alpha17b	903:914	IFN-alpha17b	903:914	The highly purified leucocyte IFN-alpha preparation was found to contain at least nine different IFN-alpha species: IFN-alpha1a, IFN-alpha2b, IFN-alpha4b, IFN-alpha7a, IFN-alpha8b, IFN-alpha10a, IFN-alpha14c, IFN-alpha17b and IFN-alpha21b.
9425112	4	58	theme	IFN-alpha	791:799	arg1	IFN-alpha2b					823:833	IFN-alpha2b	823:833	IFN-alpha2b	823:833	The highly purified leucocyte IFN-alpha preparation was found to contain at least nine different IFN-alpha species: IFN-alpha1a, IFN-alpha2b, IFN-alpha4b, IFN-alpha7a, IFN-alpha8b, IFN-alpha10a, IFN-alpha14c, IFN-alpha17b and IFN-alpha21b.
9425112	4	58	theme	IFN-alpha	791:799	arg1	IFN-alpha8b					862:872	IFN-alpha8b	862:872	IFN-alpha8b	862:872	The highly purified leucocyte IFN-alpha preparation was found to contain at least nine different IFN-alpha species: IFN-alpha1a, IFN-alpha2b, IFN-alpha4b, IFN-alpha7a, IFN-alpha8b, IFN-alpha10a, IFN-alpha14c, IFN-alpha17b and IFN-alpha21b.
9425112	4	58	theme	IFN-alpha	791:799	arg1	IFN-alpha10a					875:886	IFN-alpha10a	875:886	IFN-alpha10a	875:886	The highly purified leucocyte IFN-alpha preparation was found to contain at least nine different IFN-alpha species: IFN-alpha1a, IFN-alpha2b, IFN-alpha4b, IFN-alpha7a, IFN-alpha8b, IFN-alpha10a, IFN-alpha14c, IFN-alpha17b and IFN-alpha21b.
9425112	4	58	theme	IFN-alpha	791:799	arg1	IFN-alpha21b					920:931	IFN-alpha21b	920:931	IFN-alpha21b	920:931	The highly purified leucocyte IFN-alpha preparation was found to contain at least nine different IFN-alpha species: IFN-alpha1a, IFN-alpha2b, IFN-alpha4b, IFN-alpha7a, IFN-alpha8b, IFN-alpha10a, IFN-alpha14c, IFN-alpha17b and IFN-alpha21b.
9425112	4	58	theme	IFN-alpha	791:799	arg1	species					801:807	at least nine different IFN-alpha species	767:807	at least nine different IFN-alpha species: IFN-alpha1a, IFN-alpha2b, IFN-alpha4b, IFN-alpha7a, IFN-alpha8b, IFN-alpha10a, IFN-alpha14c, IFN-alpha17b and IFN-alpha21b	767:931	The highly purified leucocyte IFN-alpha preparation was found to contain at least nine different IFN-alpha species: IFN-alpha1a, IFN-alpha2b, IFN-alpha4b, IFN-alpha7a, IFN-alpha8b, IFN-alpha10a, IFN-alpha14c, IFN-alpha17b and IFN-alpha21b.
9425112	4	58	theme	IFN-alpha	791:799	arg1	IFN-alpha4b					836:846	IFN-alpha4b	836:846	IFN-alpha4b	836:846	The highly purified leucocyte IFN-alpha preparation was found to contain at least nine different IFN-alpha species: IFN-alpha1a, IFN-alpha2b, IFN-alpha4b, IFN-alpha7a, IFN-alpha8b, IFN-alpha10a, IFN-alpha14c, IFN-alpha17b and IFN-alpha21b.
9425112	2	59	theme	described	319:327	arg1	sequences					329:337	the described sequences	315:337	the described sequences	315:337	To find out which of the described sequences are expressed in normal human leucocytes, we have isolated and partly characterized the components of a highly purified IFN-alpha preparation produced by Sendai virus-induced human peripheral blood leucocytes.
9425112	1	60	theme	sequence	233:240	arg1	variants					242:249	all cloned sequence variants	222:249	all cloned sequence variants	222:249	The human interferon-alpha (IFN-alpha) family is encoded by 13 different functional genes, and including all cloned sequence variants there are 28 potential IFN-alpha proteins.
9425112	0	61	theme	human	82:86	arg1	leucocytes					105:114	Sendai virus-induced human peripheral blood leucocytes	61:114	Sendai virus-induced human peripheral blood leucocytes	61:114	Identification of nine interferon-alpha subtypes produced by Sendai virus-induced human peripheral blood leucocytes.
9425112	3	62	theme	proteins	636:643	arg1	sequencing					601:610	N-terminal sequencing	590:610	N-terminal sequencing	590:610	The identification protocol consisted of N-terminal sequencing and mass mapping of the proteins separated by reverse-phase HPLC and/or SDS/PAGE.
9425112	3	62	theme	proteins	636:643	arg1	mapping					621:627	mass mapping	616:627	mass mapping	616:627	The identification protocol consisted of N-terminal sequencing and mass mapping of the proteins separated by reverse-phase HPLC and/or SDS/PAGE.
9425112	9	63	theme	allelic	1480:1486	arg1	variants					1488:1495	allelic variants	1480:1495	allelic variants	1480:1495	Only one sequence variant was found for each subtype, suggesting that the other described gene sequences represent allelic variants or mutations that are more rarely found in the general population.
9425112	0	64	theme	Sendai	61:66	arg1	leucocytes					105:114	Sendai virus-induced human peripheral blood leucocytes	61:114	Sendai virus-induced human peripheral blood leucocytes	61:114	Identification of nine interferon-alpha subtypes produced by Sendai virus-induced human peripheral blood leucocytes.
9425112	8	65	from	modifications	1269:1281	arg1	subtypes					1300:1307	the IFN-alpha subtypes	1286:1307	the IFN-alpha subtypes	1286:1307	Molecular mass determination of the intact proteins by electrospray ionization MS showed that there are no other post-translational modifications in the IFN-alpha subtypes than the glycosylation of IFN-alpha2b and IFN-alpha14c.
9425112	2	66	theme	human	363:367	arg1	leucocytes					369:378	normal human leucocytes	356:378	normal human leucocytes	356:378	To find out which of the described sequences are expressed in normal human leucocytes, we have isolated and partly characterized the components of a highly purified IFN-alpha preparation produced by Sendai virus-induced human peripheral blood leucocytes.
9425112	8	67	theme	mass	1147:1150	arg1	determination					1152:1164	Molecular mass determination	1137:1164	Molecular mass determination of the intact proteins by electrospray ionization MS	1137:1217	Molecular mass determination of the intact proteins by electrospray ionization MS showed that there are no other post-translational modifications in the IFN-alpha subtypes than the glycosylation of IFN-alpha2b and IFN-alpha14c.
9425112	9	68	theme	other	1439:1443	arg1	sequences					1460:1468	the other described gene sequences	1435:1468	the other described gene sequences	1435:1468	Only one sequence variant was found for each subtype, suggesting that the other described gene sequences represent allelic variants or mutations that are more rarely found in the general population.
1482348	3	0	theme	acid	341:344	arg1	analysis					355:362	amino acid sequence analysis	335:362	amino acid sequence analysis	335:362	Sugar analysis and amino acid sequence analysis of peptide fragments produced by limited degradation revealed that O-glycosylated oligosaccharide linked to Thr445 of the alpha chain.
1482348	0	1	theme	alpha	76:80	arg1	chain					82:86	the alpha chain	72:86	the alpha chain	72:86	Hepatocyte growth factor is linked by O-glycosylated oligosaccharide on the alpha chain.
1482348	4	2	theme	ion	563:565	arg1	spectrometry					578:589	ion spray mass spectrometry	563:589	ion spray mass spectrometry	563:589	The molecular weight of the oligosaccharide was determined with ion spray mass spectrometry.
1482348	5	3	theme	O-glycosylated	633:646	arg1	oligosaccharide					648:662	the O-glycosylated oligosaccharide	629:662	the O-glycosylated oligosaccharide on the alpha chain of HGF	629:688	From these studies, the structure of the O-glycosylated oligosaccharide on the alpha chain of HGF was concluded as [formula: see text].
1482348	1	4	theme	recombinant	167:177	arg1	HGF					185:187	recombinant human HGF	167:187	recombinant human HGF	167:187	The glycosylation site and the structure of O-glycosylated oligosaccharide of recombinant human HGF were investigated.
1482348	2	5	from	N-acetylgalactosamine	208:228	arg1	chain					252:256	the alpha chain	242:256	the alpha chain	242:256	N-acetylgalactosamine (GalNAc) in the alpha chain suggested the presence of O-glycosylated oligosaccharide.
1482348	5	6	theme	oligosaccharide	648:662	arg1	structure					616:624	the structure	612:624	the structure of the O-glycosylated oligosaccharide on the alpha chain of HGF	612:688	From these studies, the structure of the O-glycosylated oligosaccharide on the alpha chain of HGF was concluded as [formula: see text].
1482348	5	6	theme	oligosaccharide	648:662	arg1	[formula					707:714	[formula	707:714	[formula	707:714	From these studies, the structure of the O-glycosylated oligosaccharide on the alpha chain of HGF was concluded as [formula: see text].
1482348	0	7	from	oligosaccharide	53:67	arg1	chain					82:86	the alpha chain	72:86	the alpha chain	72:86	Hepatocyte growth factor is linked by O-glycosylated oligosaccharide on the alpha chain.
1482348	3	8	gly	O-glycosylated	431:444	arg1	oligosaccharide					446:460	O-glycosylated oligosaccharide	431:460	O-glycosylated oligosaccharide	431:460	Sugar analysis and amino acid sequence analysis of peptide fragments produced by limited degradation revealed that O-glycosylated oligosaccharide linked to Thr445 of the alpha chain.
1482348	2	9	theme	oligosaccharide	299:313	arg1	presence					272:279	the presence	268:279	the presence of O-glycosylated oligosaccharide	268:313	N-acetylgalactosamine (GalNAc) in the alpha chain suggested the presence of O-glycosylated oligosaccharide.
1482348	5	10	from	structure	616:624	arg1	chain					677:681	the alpha chain	667:681	the alpha chain of HGF	667:688	From these studies, the structure of the O-glycosylated oligosaccharide on the alpha chain of HGF was concluded as [formula: see text].
1482348	3	11	theme	peptide	367:373	arg1	fragments					375:383	peptide fragments	367:383	peptide fragments produced by limited degradation	367:415	Sugar analysis and amino acid sequence analysis of peptide fragments produced by limited degradation revealed that O-glycosylated oligosaccharide linked to Thr445 of the alpha chain.
1482348	5	12	theme	alpha	671:675	arg1	chain					677:681	the alpha chain	667:681	the alpha chain of HGF	667:688	From these studies, the structure of the O-glycosylated oligosaccharide on the alpha chain of HGF was concluded as [formula: see text].
1482348	2	13	theme	O-glycosylated	284:297	arg1	oligosaccharide					299:313	O-glycosylated oligosaccharide	284:313	O-glycosylated oligosaccharide	284:313	N-acetylgalactosamine (GalNAc) in the alpha chain suggested the presence of O-glycosylated oligosaccharide.
1482348	1	14	theme	human	179:183	arg1	HGF					185:187	recombinant human HGF	167:187	recombinant human HGF	167:187	The glycosylation site and the structure of O-glycosylated oligosaccharide of recombinant human HGF were investigated.
1482348	1	15	gly	glycosylation	93:105	arg2	site					107:110	The glycosylation site	89:110	The glycosylation site	89:110	The glycosylation site and the structure of O-glycosylated oligosaccharide of recombinant human HGF were investigated.
1482348	1	15	gly	glycosylation	93:105	arg1	oligosaccharide					148:162	O-glycosylated oligosaccharide	133:162	O-glycosylated oligosaccharide of recombinant human HGF	133:187	The glycosylation site and the structure of O-glycosylated oligosaccharide of recombinant human HGF were investigated.
1482348	1	15	gly	glycosylation	93:105	arg2	oligosaccharide					148:162	O-glycosylated oligosaccharide	133:162	O-glycosylated oligosaccharide of recombinant human HGF	133:187	The glycosylation site and the structure of O-glycosylated oligosaccharide of recombinant human HGF were investigated.
1482348	4	16	theme	oligosaccharide	527:541	arg1	weight					513:518	The molecular weight	499:518	The molecular weight of the oligosaccharide	499:541	The molecular weight of the oligosaccharide was determined with ion spray mass spectrometry.
1482348	0	17	attach	linked	28:33	arg3	oligosaccharide					53:67	O-glycosylated oligosaccharide	38:67	O-glycosylated oligosaccharide on the alpha chain	38:86	Hepatocyte growth factor is linked by O-glycosylated oligosaccharide on the alpha chain.
1482348	0	17	attach	linked	28:33	arg2	factor					18:23	Hepatocyte growth factor	0:23	Hepatocyte growth factor	0:23	Hepatocyte growth factor is linked by O-glycosylated oligosaccharide on the alpha chain.
1482348	1	18	theme	HGF	185:187	arg1	oligosaccharide					148:162	O-glycosylated oligosaccharide	133:162	O-glycosylated oligosaccharide of recombinant human HGF	133:187	The glycosylation site and the structure of O-glycosylated oligosaccharide of recombinant human HGF were investigated.
1482348	0	19	theme	growth	11:16	arg1	factor					18:23	Hepatocyte growth factor	0:23	Hepatocyte growth factor	0:23	Hepatocyte growth factor is linked by O-glycosylated oligosaccharide on the alpha chain.
1482348	3	20	theme	sequence	346:353	arg1	analysis					355:362	amino acid sequence analysis	335:362	amino acid sequence analysis	335:362	Sugar analysis and amino acid sequence analysis of peptide fragments produced by limited degradation revealed that O-glycosylated oligosaccharide linked to Thr445 of the alpha chain.
1482348	3	21	theme	amino	335:339	arg1	analysis					355:362	amino acid sequence analysis	335:362	amino acid sequence analysis	335:362	Sugar analysis and amino acid sequence analysis of peptide fragments produced by limited degradation revealed that O-glycosylated oligosaccharide linked to Thr445 of the alpha chain.
1482348	0	22	theme	Hepatocyte	0:9	arg1	factor					18:23	Hepatocyte growth factor	0:23	Hepatocyte growth factor	0:23	Hepatocyte growth factor is linked by O-glycosylated oligosaccharide on the alpha chain.
1482348	5	23	theme	HGF	686:688	arg1	chain					677:681	the alpha chain	667:681	the alpha chain of HGF	667:688	From these studies, the structure of the O-glycosylated oligosaccharide on the alpha chain of HGF was concluded as [formula: see text].
1482348	3	24	theme	limited	397:403	arg1	degradation					405:415	limited degradation	397:415	limited degradation	397:415	Sugar analysis and amino acid sequence analysis of peptide fragments produced by limited degradation revealed that O-glycosylated oligosaccharide linked to Thr445 of the alpha chain.
1482348	1	25	theme	glycosylation	93:105	arg1	oligosaccharide					148:162	O-glycosylated oligosaccharide	133:162	O-glycosylated oligosaccharide of recombinant human HGF	133:187	The glycosylation site and the structure of O-glycosylated oligosaccharide of recombinant human HGF were investigated.
1482348	1	25	theme	glycosylation	93:105	arg1	site					107:110	The glycosylation site	89:110	The glycosylation site	89:110	The glycosylation site and the structure of O-glycosylated oligosaccharide of recombinant human HGF were investigated.
1482348	5	26	from	oligosaccharide	648:662	arg1	chain					677:681	the alpha chain	667:681	the alpha chain of HGF	667:688	From these studies, the structure of the O-glycosylated oligosaccharide on the alpha chain of HGF was concluded as [formula: see text].
1482348	5	27	from	chain	677:681	arg1	structure					616:624	the structure	612:624	the structure of the O-glycosylated oligosaccharide on the alpha chain of HGF	612:688	From these studies, the structure of the O-glycosylated oligosaccharide on the alpha chain of HGF was concluded as [formula: see text].
1482348	5	27	from	chain	677:681	arg1	[formula					707:714	[formula	707:714	[formula	707:714	From these studies, the structure of the O-glycosylated oligosaccharide on the alpha chain of HGF was concluded as [formula: see text].
1482348	3	28	attach	linked	462:467	arg2	oligosaccharide					446:460	O-glycosylated oligosaccharide	431:460	O-glycosylated oligosaccharide	431:460	Sugar analysis and amino acid sequence analysis of peptide fragments produced by limited degradation revealed that O-glycosylated oligosaccharide linked to Thr445 of the alpha chain.
1482348	3	28	attach	linked	462:467	arg1	Thr445					472:477	Thr445	472:477	Thr445 of the alpha chain	472:496	Sugar analysis and amino acid sequence analysis of peptide fragments produced by limited degradation revealed that O-glycosylated oligosaccharide linked to Thr445 of the alpha chain.
1482348	2	29	theme	alpha	246:250	arg1	chain					252:256	the alpha chain	242:256	the alpha chain	242:256	N-acetylgalactosamine (GalNAc) in the alpha chain suggested the presence of O-glycosylated oligosaccharide.
1482348	3	30	theme	chain	492:496	arg1	Thr445					472:477	Thr445	472:477	Thr445 of the alpha chain	472:496	Sugar analysis and amino acid sequence analysis of peptide fragments produced by limited degradation revealed that O-glycosylated oligosaccharide linked to Thr445 of the alpha chain.
1482348	4	31	theme	mass	573:576	arg1	spectrometry					578:589	ion spray mass spectrometry	563:589	ion spray mass spectrometry	563:589	The molecular weight of the oligosaccharide was determined with ion spray mass spectrometry.
1482348	4	32	theme	molecular	503:511	arg1	weight					513:518	The molecular weight	499:518	The molecular weight of the oligosaccharide	499:541	The molecular weight of the oligosaccharide was determined with ion spray mass spectrometry.
1482348	2	33	gly	O-glycosylated	284:297	arg1	oligosaccharide					299:313	O-glycosylated oligosaccharide	284:313	O-glycosylated oligosaccharide	284:313	N-acetylgalactosamine (GalNAc) in the alpha chain suggested the presence of O-glycosylated oligosaccharide.
1482348	3	34	theme	O-glycosylated	431:444	arg1	oligosaccharide					446:460	O-glycosylated oligosaccharide	431:460	O-glycosylated oligosaccharide	431:460	Sugar analysis and amino acid sequence analysis of peptide fragments produced by limited degradation revealed that O-glycosylated oligosaccharide linked to Thr445 of the alpha chain.
1482348	4	35	theme	spray	567:571	arg1	spectrometry					578:589	ion spray mass spectrometry	563:589	ion spray mass spectrometry	563:589	The molecular weight of the oligosaccharide was determined with ion spray mass spectrometry.
1482348	0	36	theme	O-glycosylated	38:51	arg1	oligosaccharide					53:67	O-glycosylated oligosaccharide	38:67	O-glycosylated oligosaccharide on the alpha chain	38:86	Hepatocyte growth factor is linked by O-glycosylated oligosaccharide on the alpha chain.
1482348	1	37	gly	O-glycosylated	133:146	arg1	oligosaccharide					148:162	O-glycosylated oligosaccharide	133:162	O-glycosylated oligosaccharide of recombinant human HGF	133:187	The glycosylation site and the structure of O-glycosylated oligosaccharide of recombinant human HGF were investigated.
1482348	3	38	theme	Sugar	316:320	arg1	analysis					322:329	Sugar analysis	316:329	Sugar analysis	316:329	Sugar analysis and amino acid sequence analysis of peptide fragments produced by limited degradation revealed that O-glycosylated oligosaccharide linked to Thr445 of the alpha chain.
1482348	3	39	theme	fragments	375:383	arg1	analysis					355:362	amino acid sequence analysis	335:362	amino acid sequence analysis	335:362	Sugar analysis and amino acid sequence analysis of peptide fragments produced by limited degradation revealed that O-glycosylated oligosaccharide linked to Thr445 of the alpha chain.
1482348	3	39	theme	fragments	375:383	arg1	analysis					322:329	Sugar analysis	316:329	Sugar analysis	316:329	Sugar analysis and amino acid sequence analysis of peptide fragments produced by limited degradation revealed that O-glycosylated oligosaccharide linked to Thr445 of the alpha chain.
1482348	5	40	gly	O-glycosylated	633:646	arg1	oligosaccharide					648:662	the O-glycosylated oligosaccharide	629:662	the O-glycosylated oligosaccharide on the alpha chain of HGF	629:688	From these studies, the structure of the O-glycosylated oligosaccharide on the alpha chain of HGF was concluded as [formula: see text].
1482348	0	41	gly	O-glycosylated	38:51	arg1	oligosaccharide					53:67	O-glycosylated oligosaccharide	38:67	O-glycosylated oligosaccharide on the alpha chain	38:86	Hepatocyte growth factor is linked by O-glycosylated oligosaccharide on the alpha chain.
1482348	1	42	theme	O-glycosylated	133:146	arg1	oligosaccharide					148:162	O-glycosylated oligosaccharide	133:162	O-glycosylated oligosaccharide of recombinant human HGF	133:187	The glycosylation site and the structure of O-glycosylated oligosaccharide of recombinant human HGF were investigated.
1482348	3	43	theme	alpha	486:490	arg1	chain					492:496	the alpha chain	482:496	the alpha chain	482:496	Sugar analysis and amino acid sequence analysis of peptide fragments produced by limited degradation revealed that O-glycosylated oligosaccharide linked to Thr445 of the alpha chain.
1482348	1	44	theme	oligosaccharide	148:162	arg1	structure					120:128	the structure	116:128	the structure of O-glycosylated oligosaccharide of recombinant human HGF	116:187	The glycosylation site and the structure of O-glycosylated oligosaccharide of recombinant human HGF were investigated.
1482348	1	44	theme	oligosaccharide	148:162	arg1	oligosaccharide					148:162	O-glycosylated oligosaccharide	133:162	O-glycosylated oligosaccharide of recombinant human HGF	133:187	The glycosylation site and the structure of O-glycosylated oligosaccharide of recombinant human HGF were investigated.
1482348	1	44	theme	oligosaccharide	148:162	arg1	site					107:110	The glycosylation site	89:110	The glycosylation site	89:110	The glycosylation site and the structure of O-glycosylated oligosaccharide of recombinant human HGF were investigated.
8243461	0	0	from	chains	43:48	arg1	peptides					68:75	the activation peptides	53:75	the activation peptides of blood coagulation factor X	53:105	Identification of O-linked oligosaccharide chains in the activation peptides of blood coagulation factor X.
8243461	8	1	theme	carbohydrate	1682:1693	arg1	residues					1695:1702	carbohydrate residues	1682:1702	carbohydrate residues in factor X	1682:1714	It appears that carbohydrate residues in factor X play an important role in the activation of the zymogen.
8243461	6	2	theme	X	1518:1518	arg1	derivatives					1496:1506	derivatives	1496:1506	derivatives of factor X prepared using O-glycanase, sialidase, and/or N-glycanase	1496:1576	The effect of deglycosylation of bovine factor X1 was investigated with factor-X-activating enzyme from Russell's viper venom or extrinsic Xase (factor VIIa/tissue factor/phospholipid) by examining the activation rates of derivatives of factor X prepared using O-glycanase, sialidase, and/or N-glycanase.
8243461	2	3	link	O-linked	449:456	arg1	chains					474:479	the O-linked oligosaccharide chains	445:479	the O-linked oligosaccharide chains in these peptides	445:497	Analysis of protease-digested glycopeptides derived from the activation peptides of bovine and human blood coagulation factor X allowed the identification of sites of the O-linked oligosaccharide chains in these peptides.
8243461	0	4	link	O-linked	18:25	arg1	chains					43:48	O-linked oligosaccharide chains	18:48	O-linked oligosaccharide chains in the activation peptides of blood coagulation factor X	18:105	Identification of O-linked oligosaccharide chains in the activation peptides of blood coagulation factor X.
8243461	4	5	contain	had	725:727	arg1	X					723:723	bovine factor X	709:723	bovine factor X	709:723	By combined analysis of amino acid sequence and sialic acid content, we found that bovine factor X had an O-linked oligosaccharide chain linked to Thr26, and human factor X had four carbohydrate-attachment sites, namely, O-glycosidic linkages to Thr17 and Thr29, respectively, and N-glycosidic linkages to Asn39 and Asn49, respectively, in their activation peptides.
8243461	4	5	contain	had	725:727	arg2	chain					757:761	an O-linked oligosaccharide chain	729:761	an O-linked oligosaccharide chain linked to Thr26	729:777	By combined analysis of amino acid sequence and sialic acid content, we found that bovine factor X had an O-linked oligosaccharide chain linked to Thr26, and human factor X had four carbohydrate-attachment sites, namely, O-glycosidic linkages to Thr17 and Thr29, respectively, and N-glycosidic linkages to Asn39 and Asn49, respectively, in their activation peptides.
8243461	6	6	theme	factor	1314:1319	arg1	X1					1321:1322	bovine factor X1	1307:1322	bovine factor X1	1307:1322	The effect of deglycosylation of bovine factor X1 was investigated with factor-X-activating enzyme from Russell's viper venom or extrinsic Xase (factor VIIa/tissue factor/phospholipid) by examining the activation rates of derivatives of factor X prepared using O-glycanase, sialidase, and/or N-glycanase.
8243461	4	7	theme	acid	681:684	arg1	content					686:692	sialic acid content	674:692	sialic acid content	674:692	By combined analysis of amino acid sequence and sialic acid content, we found that bovine factor X had an O-linked oligosaccharide chain linked to Thr26, and human factor X had four carbohydrate-attachment sites, namely, O-glycosidic linkages to Thr17 and Thr29, respectively, and N-glycosidic linkages to Asn39 and Asn49, respectively, in their activation peptides.
8243461	8	8	theme	zymogen	1764:1770	arg1	activation					1746:1755	the activation	1742:1755	the activation of the zymogen	1742:1770	It appears that carbohydrate residues in factor X play an important role in the activation of the zymogen.
8243461	1	9	theme	factor	167:172	arg1	Conversion					177:186	factor X. Conversion	167:186	factor X. Conversion of factor X to factor Xa	167:211	The role of the carbohydrate moieties in the activation of factor X. Conversion of factor X to factor Xa results in release of a heavily glycosylated activation peptide.
8243461	3	10	theme	Staphylococcus	591:604	arg1	protease					616:623	Staphylococcus aureus V8 protease	591:623	Staphylococcus aureus V8 protease	591:623	Glycopeptides were prepared from the activation peptides by digestion with chymotrypsin or Staphylococcus aureus V8 protease.
8243461	1	11	theme	Conversion	177:186	arg1	activation					153:162	the activation	149:162	the activation of factor X. Conversion of factor X to factor Xa	149:211	The role of the carbohydrate moieties in the activation of factor X. Conversion of factor X to factor Xa results in release of a heavily glycosylated activation peptide.
8243461	4	12	theme	acid	656:659	arg1	sequence					661:668	amino acid sequence	650:668	amino acid sequence	650:668	By combined analysis of amino acid sequence and sialic acid content, we found that bovine factor X had an O-linked oligosaccharide chain linked to Thr26, and human factor X had four carbohydrate-attachment sites, namely, O-glycosidic linkages to Thr17 and Thr29, respectively, and N-glycosidic linkages to Asn39 and Asn49, respectively, in their activation peptides.
8243461	6	13	theme	viper	1388:1392	arg1	venom					1394:1398	Russell's viper venom	1378:1398	Russell's viper venom	1378:1398	The effect of deglycosylation of bovine factor X1 was investigated with factor-X-activating enzyme from Russell's viper venom or extrinsic Xase (factor VIIa/tissue factor/phospholipid) by examining the activation rates of derivatives of factor X prepared using O-glycanase, sialidase, and/or N-glycanase.
8243461	5	14	theme	phenylthiohydantoin	1072:1090	arg1	derivatives					1092:1102	phenylthiohydantoin derivatives	1072:1102	phenylthiohydantoin derivatives of amino acids that corresponded to their residues	1072:1153	The O-linked carbohydrate-attachment sites were identified since the yields of phenylthiohydantoin derivatives of amino acids that corresponded to their residues were increased during amino acid sequencing after deglycosylation of the glycopeptides with sialidase and O-glycanase.
8243461	1	15	theme	factor	191:196	arg1	X					198:198	factor X	191:198	factor X	191:198	The role of the carbohydrate moieties in the activation of factor X. Conversion of factor X to factor Xa results in release of a heavily glycosylated activation peptide.
8243461	0	16	from	peptides	68:75	arg1	Identification					0:13	Identification	0:13	Identification of O-linked oligosaccharide chains in the activation peptides of blood coagulation factor X.	0:106	Identification of O-linked oligosaccharide chains in the activation peptides of blood coagulation factor X.
8243461	8	17	from	residues	1695:1702	arg1	X					1714:1714	factor X	1707:1714	factor X	1707:1714	It appears that carbohydrate residues in factor X play an important role in the activation of the zymogen.
8243461	3	18	theme	V8	613:614	arg1	protease					616:623	Staphylococcus aureus V8 protease	591:623	Staphylococcus aureus V8 protease	591:623	Glycopeptides were prepared from the activation peptides by digestion with chymotrypsin or Staphylococcus aureus V8 protease.
8243461	6	19	gly	deglycosylation	1288:1302	arg1	X1					1321:1322	bovine factor X1	1307:1322	bovine factor X1	1307:1322	The effect of deglycosylation of bovine factor X1 was investigated with factor-X-activating enzyme from Russell's viper venom or extrinsic Xase (factor VIIa/tissue factor/phospholipid) by examining the activation rates of derivatives of factor X prepared using O-glycanase, sialidase, and/or N-glycanase.
8243461	4	20	theme	activation	972:981	arg1	peptides					983:990	their activation peptides	966:990	their activation peptides	966:990	By combined analysis of amino acid sequence and sialic acid content, we found that bovine factor X had an O-linked oligosaccharide chain linked to Thr26, and human factor X had four carbohydrate-attachment sites, namely, O-glycosidic linkages to Thr17 and Thr29, respectively, and N-glycosidic linkages to Asn39 and Asn49, respectively, in their activation peptides.
8243461	6	21	from	venom	1394:1398	arg1	enzyme					1366:1371	factor-X-activating enzyme	1346:1371	factor-X-activating enzyme from Russell's viper venom	1346:1398	The effect of deglycosylation of bovine factor X1 was investigated with factor-X-activating enzyme from Russell's viper venom or extrinsic Xase (factor VIIa/tissue factor/phospholipid) by examining the activation rates of derivatives of factor X prepared using O-glycanase, sialidase, and/or N-glycanase.
8243461	6	21	from	venom	1394:1398	arg1	Xase					1413:1416	extrinsic Xase	1403:1416	extrinsic Xase (factor VIIa/tissue factor/phospholipid)	1403:1457	The effect of deglycosylation of bovine factor X1 was investigated with factor-X-activating enzyme from Russell's viper venom or extrinsic Xase (factor VIIa/tissue factor/phospholipid) by examining the activation rates of derivatives of factor X prepared using O-glycanase, sialidase, and/or N-glycanase.
8243461	6	21	from	venom	1394:1398	arg1	factor/phospholipid					1438:1456	factor VIIa/tissue factor/phospholipid	1419:1456	factor VIIa/tissue factor/phospholipid	1419:1456	The effect of deglycosylation of bovine factor X1 was investigated with factor-X-activating enzyme from Russell's viper venom or extrinsic Xase (factor VIIa/tissue factor/phospholipid) by examining the activation rates of derivatives of factor X prepared using O-glycanase, sialidase, and/or N-glycanase.
8243461	4	22	theme	bovine	709:714	arg1	X					723:723	bovine factor X	709:723	bovine factor X	709:723	By combined analysis of amino acid sequence and sialic acid content, we found that bovine factor X had an O-linked oligosaccharide chain linked to Thr26, and human factor X had four carbohydrate-attachment sites, namely, O-glycosidic linkages to Thr17 and Thr29, respectively, and N-glycosidic linkages to Asn39 and Asn49, respectively, in their activation peptides.
8243461	0	23	theme	blood	80:84	arg1	X					105:105	blood coagulation factor X	80:105	blood coagulation factor X	80:105	Identification of O-linked oligosaccharide chains in the activation peptides of blood coagulation factor X.
8243461	0	24	from	Identification	0:13	arg1	peptides					68:75	the activation peptides	53:75	the activation peptides of blood coagulation factor X	53:105	Identification of O-linked oligosaccharide chains in the activation peptides of blood coagulation factor X.
8243461	0	25	theme	factor	98:103	arg1	X					105:105	blood coagulation factor X	80:105	blood coagulation factor X	80:105	Identification of O-linked oligosaccharide chains in the activation peptides of blood coagulation factor X.
8243461	5	26	theme	acids	1113:1117	arg1	derivatives					1092:1102	phenylthiohydantoin derivatives	1072:1102	phenylthiohydantoin derivatives of amino acids that corresponded to their residues	1072:1153	The O-linked carbohydrate-attachment sites were identified since the yields of phenylthiohydantoin derivatives of amino acids that corresponded to their residues were increased during amino acid sequencing after deglycosylation of the glycopeptides with sialidase and O-glycanase.
8243461	1	27	theme	carbohydrate	124:135	arg1	moieties					137:144	the carbohydrate moieties	120:144	the carbohydrate moieties	120:144	The role of the carbohydrate moieties in the activation of factor X. Conversion of factor X to factor Xa results in release of a heavily glycosylated activation peptide.
8243461	2	28	theme	factor	397:402	arg1	X					404:404	bovine and human blood coagulation factor X	362:404	bovine and human blood coagulation factor X	362:404	Analysis of protease-digested glycopeptides derived from the activation peptides of bovine and human blood coagulation factor X allowed the identification of sites of the O-linked oligosaccharide chains in these peptides.
8243461	2	29	from	chains	474:479	arg1	peptides					490:497	these peptides	484:497	these peptides	484:497	Analysis of protease-digested glycopeptides derived from the activation peptides of bovine and human blood coagulation factor X allowed the identification of sites of the O-linked oligosaccharide chains in these peptides.
8243461	5	30	gly	glycopeptides	1228:1240	arg2	glycopeptides					1228:1240	the glycopeptides	1224:1240	the glycopeptides with sialidase and O-glycanase	1224:1271	The O-linked carbohydrate-attachment sites were identified since the yields of phenylthiohydantoin derivatives of amino acids that corresponded to their residues were increased during amino acid sequencing after deglycosylation of the glycopeptides with sialidase and O-glycanase.
8243461	4	31	theme	oligosaccharide	741:755	arg1	chain					757:761	an O-linked oligosaccharide chain	729:761	an O-linked oligosaccharide chain linked to Thr26	729:777	By combined analysis of amino acid sequence and sialic acid content, we found that bovine factor X had an O-linked oligosaccharide chain linked to Thr26, and human factor X had four carbohydrate-attachment sites, namely, O-glycosidic linkages to Thr17 and Thr29, respectively, and N-glycosidic linkages to Asn39 and Asn49, respectively, in their activation peptides.
8243461	2	32	theme	blood	379:383	arg1	X					404:404	bovine and human blood coagulation factor X	362:404	bovine and human blood coagulation factor X	362:404	Analysis of protease-digested glycopeptides derived from the activation peptides of bovine and human blood coagulation factor X allowed the identification of sites of the O-linked oligosaccharide chains in these peptides.
8243461	6	33	theme	derivatives	1496:1506	arg1	rates					1487:1491	the activation rates	1472:1491	the activation rates of derivatives of factor X prepared using O-glycanase, sialidase, and/or N-glycanase	1472:1576	The effect of deglycosylation of bovine factor X1 was investigated with factor-X-activating enzyme from Russell's viper venom or extrinsic Xase (factor VIIa/tissue factor/phospholipid) by examining the activation rates of derivatives of factor X prepared using O-glycanase, sialidase, and/or N-glycanase.
8243461	1	34	theme	glycosylated	245:256	arg1	peptide					269:275	a heavily glycosylated activation peptide	235:275	a heavily glycosylated activation peptide	235:275	The role of the carbohydrate moieties in the activation of factor X. Conversion of factor X to factor Xa results in release of a heavily glycosylated activation peptide.
8243461	1	35	from	role	112:115	arg1	activation					153:162	the activation	149:162	the activation of factor X. Conversion of factor X to factor Xa	149:211	The role of the carbohydrate moieties in the activation of factor X. Conversion of factor X to factor Xa results in release of a heavily glycosylated activation peptide.
8243461	2	36	theme	sites	436:440	arg1	identification					418:431	the identification	414:431	the identification of sites of the O-linked oligosaccharide chains in these peptides	414:497	Analysis of protease-digested glycopeptides derived from the activation peptides of bovine and human blood coagulation factor X allowed the identification of sites of the O-linked oligosaccharide chains in these peptides.
8243461	0	37	theme	O-linked	18:25	arg1	chains					43:48	O-linked oligosaccharide chains	18:48	O-linked oligosaccharide chains in the activation peptides of blood coagulation factor X	18:105	Identification of O-linked oligosaccharide chains in the activation peptides of blood coagulation factor X.
8243461	1	38	theme	peptide	269:275	arg1	release					224:230	release	224:230	release of a heavily glycosylated activation peptide	224:275	The role of the carbohydrate moieties in the activation of factor X. Conversion of factor X to factor Xa results in release of a heavily glycosylated activation peptide.
8243461	7	39	theme	O-linked	1594:1601	arg1	carbohydrate					1603:1614	O-linked carbohydrate	1594:1614	O-linked carbohydrate	1594:1614	The removal of O-linked carbohydrate resulted in a decrease in the rate of activation.
8243461	4	40	theme	carbohydrate-attachment	808:830	arg1	sites					832:836	four carbohydrate-attachment sites	803:836	four carbohydrate-attachment sites	803:836	By combined analysis of amino acid sequence and sialic acid content, we found that bovine factor X had an O-linked oligosaccharide chain linked to Thr26, and human factor X had four carbohydrate-attachment sites, namely, O-glycosidic linkages to Thr17 and Thr29, respectively, and N-glycosidic linkages to Asn39 and Asn49, respectively, in their activation peptides.
8243461	0	41	theme	chains	43:48	arg1	Identification					0:13	Identification	0:13	Identification of O-linked oligosaccharide chains in the activation peptides of blood coagulation factor X.	0:106	Identification of O-linked oligosaccharide chains in the activation peptides of blood coagulation factor X.
8243461	7	42	from	decrease	1630:1637	arg1	rate					1646:1649	the rate	1642:1649	the rate of activation	1642:1663	The removal of O-linked carbohydrate resulted in a decrease in the rate of activation.
8243461	2	43	theme	oligosaccharide	458:472	arg1	chains					474:479	the O-linked oligosaccharide chains	445:479	the O-linked oligosaccharide chains in these peptides	445:497	Analysis of protease-digested glycopeptides derived from the activation peptides of bovine and human blood coagulation factor X allowed the identification of sites of the O-linked oligosaccharide chains in these peptides.
8243461	2	44	theme	activation	339:348	arg1	peptides					350:357	the activation peptides	335:357	the activation peptides of bovine and human blood coagulation factor X	335:404	Analysis of protease-digested glycopeptides derived from the activation peptides of bovine and human blood coagulation factor X allowed the identification of sites of the O-linked oligosaccharide chains in these peptides.
8243461	3	45	with	digestion	560:568	arg1	protease					616:623	Staphylococcus aureus V8 protease	591:623	Staphylococcus aureus V8 protease	591:623	Glycopeptides were prepared from the activation peptides by digestion with chymotrypsin or Staphylococcus aureus V8 protease.
8243461	3	45	with	digestion	560:568	arg1	chymotrypsin					575:586	chymotrypsin	575:586	chymotrypsin	575:586	Glycopeptides were prepared from the activation peptides by digestion with chymotrypsin or Staphylococcus aureus V8 protease.
8243461	5	46	theme	acid	1183:1186	arg1	sequencing					1188:1197	amino acid sequencing	1177:1197	amino acid sequencing	1177:1197	The O-linked carbohydrate-attachment sites were identified since the yields of phenylthiohydantoin derivatives of amino acids that corresponded to their residues were increased during amino acid sequencing after deglycosylation of the glycopeptides with sialidase and O-glycanase.
8243461	4	47	theme	factor	790:795	arg1	X					797:797	human factor X	784:797	human factor X	784:797	By combined analysis of amino acid sequence and sialic acid content, we found that bovine factor X had an O-linked oligosaccharide chain linked to Thr26, and human factor X had four carbohydrate-attachment sites, namely, O-glycosidic linkages to Thr17 and Thr29, respectively, and N-glycosidic linkages to Asn39 and Asn49, respectively, in their activation peptides.
8243461	8	48	theme	factor	1707:1712	arg1	X					1714:1714	factor X	1707:1714	factor X	1707:1714	It appears that carbohydrate residues in factor X play an important role in the activation of the zymogen.
8243461	1	49	theme	factor	203:208	arg1	Xa					210:211	factor Xa	203:211	factor Xa	203:211	The role of the carbohydrate moieties in the activation of factor X. Conversion of factor X to factor Xa results in release of a heavily glycosylated activation peptide.
8243461	5	50	theme	O-linked	997:1004	arg1	sites					1030:1034	The O-linked carbohydrate-attachment sites	993:1034	The O-linked carbohydrate-attachment sites	993:1034	The O-linked carbohydrate-attachment sites were identified since the yields of phenylthiohydantoin derivatives of amino acids that corresponded to their residues were increased during amino acid sequencing after deglycosylation of the glycopeptides with sialidase and O-glycanase.
8243461	6	51	theme	VIIa/tissue	1426:1436	arg1	Xase					1413:1416	extrinsic Xase	1403:1416	extrinsic Xase (factor VIIa/tissue factor/phospholipid)	1403:1457	The effect of deglycosylation of bovine factor X1 was investigated with factor-X-activating enzyme from Russell's viper venom or extrinsic Xase (factor VIIa/tissue factor/phospholipid) by examining the activation rates of derivatives of factor X prepared using O-glycanase, sialidase, and/or N-glycanase.
8243461	6	51	theme	VIIa/tissue	1426:1436	arg1	factor/phospholipid					1438:1456	factor VIIa/tissue factor/phospholipid	1419:1456	factor VIIa/tissue factor/phospholipid	1419:1456	The effect of deglycosylation of bovine factor X1 was investigated with factor-X-activating enzyme from Russell's viper venom or extrinsic Xase (factor VIIa/tissue factor/phospholipid) by examining the activation rates of derivatives of factor X prepared using O-glycanase, sialidase, and/or N-glycanase.
8243461	8	52	theme	important	1724:1732	arg1	role					1734:1737	an important role	1721:1737	an important role	1721:1737	It appears that carbohydrate residues in factor X play an important role in the activation of the zymogen.
8243461	5	53	theme	glycopeptides	1228:1240	arg1	deglycosylation					1205:1219	deglycosylation	1205:1219	deglycosylation of the glycopeptides with sialidase and O-glycanase	1205:1271	The O-linked carbohydrate-attachment sites were identified since the yields of phenylthiohydantoin derivatives of amino acids that corresponded to their residues were increased during amino acid sequencing after deglycosylation of the glycopeptides with sialidase and O-glycanase.
8243461	4	54	link	O-linked	732:739	arg1	chain					757:761	an O-linked oligosaccharide chain	729:761	an O-linked oligosaccharide chain linked to Thr26	729:777	By combined analysis of amino acid sequence and sialic acid content, we found that bovine factor X had an O-linked oligosaccharide chain linked to Thr26, and human factor X had four carbohydrate-attachment sites, namely, O-glycosidic linkages to Thr17 and Thr29, respectively, and N-glycosidic linkages to Asn39 and Asn49, respectively, in their activation peptides.
8243461	7	55	link	O-linked	1594:1601	arg1	carbohydrate					1603:1614	O-linked carbohydrate	1594:1614	O-linked carbohydrate	1594:1614	The removal of O-linked carbohydrate resulted in a decrease in the rate of activation.
8243461	6	56	theme	X1	1321:1322	arg1	deglycosylation					1288:1302	deglycosylation	1288:1302	deglycosylation of bovine factor X1	1288:1322	The effect of deglycosylation of bovine factor X1 was investigated with factor-X-activating enzyme from Russell's viper venom or extrinsic Xase (factor VIIa/tissue factor/phospholipid) by examining the activation rates of derivatives of factor X prepared using O-glycanase, sialidase, and/or N-glycanase.
8243461	6	57	theme	factor	1511:1516	arg1	X					1518:1518	factor X	1511:1518	factor X	1511:1518	The effect of deglycosylation of bovine factor X1 was investigated with factor-X-activating enzyme from Russell's viper venom or extrinsic Xase (factor VIIa/tissue factor/phospholipid) by examining the activation rates of derivatives of factor X prepared using O-glycanase, sialidase, and/or N-glycanase.
8243461	6	58	theme	bovine	1307:1312	arg1	X1					1321:1322	bovine factor X1	1307:1322	bovine factor X1	1307:1322	The effect of deglycosylation of bovine factor X1 was investigated with factor-X-activating enzyme from Russell's viper venom or extrinsic Xase (factor VIIa/tissue factor/phospholipid) by examining the activation rates of derivatives of factor X prepared using O-glycanase, sialidase, and/or N-glycanase.
8243461	3	59	theme	activation	537:546	arg1	peptides					548:555	the activation peptides	533:555	the activation peptides	533:555	Glycopeptides were prepared from the activation peptides by digestion with chymotrypsin or Staphylococcus aureus V8 protease.
8243461	2	60	attach	derived	322:328	arg2	glycopeptides					308:320	protease-digested glycopeptides	290:320	protease-digested glycopeptides derived from the activation peptides of bovine and human blood coagulation factor X	290:404	Analysis of protease-digested glycopeptides derived from the activation peptides of bovine and human blood coagulation factor X allowed the identification of sites of the O-linked oligosaccharide chains in these peptides.
8243461	2	60	attach	derived	322:328	arg1	peptides					350:357	the activation peptides	335:357	the activation peptides of bovine and human blood coagulation factor X	335:404	Analysis of protease-digested glycopeptides derived from the activation peptides of bovine and human blood coagulation factor X allowed the identification of sites of the O-linked oligosaccharide chains in these peptides.
8243461	4	61	theme	sialic	674:679	arg1	content					686:692	sialic acid content	674:692	sialic acid content	674:692	By combined analysis of amino acid sequence and sialic acid content, we found that bovine factor X had an O-linked oligosaccharide chain linked to Thr26, and human factor X had four carbohydrate-attachment sites, namely, O-glycosidic linkages to Thr17 and Thr29, respectively, and N-glycosidic linkages to Asn39 and Asn49, respectively, in their activation peptides.
8243461	6	62	theme	factor	1419:1424	arg1	Xase					1413:1416	extrinsic Xase	1403:1416	extrinsic Xase (factor VIIa/tissue factor/phospholipid)	1403:1457	The effect of deglycosylation of bovine factor X1 was investigated with factor-X-activating enzyme from Russell's viper venom or extrinsic Xase (factor VIIa/tissue factor/phospholipid) by examining the activation rates of derivatives of factor X prepared using O-glycanase, sialidase, and/or N-glycanase.
8243461	6	62	theme	factor	1419:1424	arg1	factor/phospholipid					1438:1456	factor VIIa/tissue factor/phospholipid	1419:1456	factor VIIa/tissue factor/phospholipid	1419:1456	The effect of deglycosylation of bovine factor X1 was investigated with factor-X-activating enzyme from Russell's viper venom or extrinsic Xase (factor VIIa/tissue factor/phospholipid) by examining the activation rates of derivatives of factor X prepared using O-glycanase, sialidase, and/or N-glycanase.
8243461	6	63	theme	deglycosylation	1288:1302	arg1	effect					1278:1283	The effect	1274:1283	The effect of deglycosylation of bovine factor X1	1274:1322	The effect of deglycosylation of bovine factor X1 was investigated with factor-X-activating enzyme from Russell's viper venom or extrinsic Xase (factor VIIa/tissue factor/phospholipid) by examining the activation rates of derivatives of factor X prepared using O-glycanase, sialidase, and/or N-glycanase.
8243461	2	64	theme	glycopeptides	308:320	arg1	Analysis					278:285	Analysis	278:285	Analysis of protease-digested glycopeptides derived from the activation peptides of bovine and human blood coagulation factor X	278:404	Analysis of protease-digested glycopeptides derived from the activation peptides of bovine and human blood coagulation factor X allowed the identification of sites of the O-linked oligosaccharide chains in these peptides.
8243461	1	65	theme	X.	174:175	arg1	Conversion					177:186	factor X. Conversion	167:186	factor X. Conversion of factor X to factor Xa	167:211	The role of the carbohydrate moieties in the activation of factor X. Conversion of factor X to factor Xa results in release of a heavily glycosylated activation peptide.
8243461	5	66	link	O-linked	997:1004	arg1	sites					1030:1034	The O-linked carbohydrate-attachment sites	993:1034	The O-linked carbohydrate-attachment sites	993:1034	The O-linked carbohydrate-attachment sites were identified since the yields of phenylthiohydantoin derivatives of amino acids that corresponded to their residues were increased during amino acid sequencing after deglycosylation of the glycopeptides with sialidase and O-glycanase.
8243461	4	67	theme	O-glycosidic	847:858	arg1	linkages					860:867	O-glycosidic linkages	847:867	O-glycosidic linkages to Thr17 and Thr29, respectively	847:900	By combined analysis of amino acid sequence and sialic acid content, we found that bovine factor X had an O-linked oligosaccharide chain linked to Thr26, and human factor X had four carbohydrate-attachment sites, namely, O-glycosidic linkages to Thr17 and Thr29, respectively, and N-glycosidic linkages to Asn39 and Asn49, respectively, in their activation peptides.
8243461	4	68	theme	content	686:692	arg1	analysis					638:645	combined analysis	629:645	combined analysis of amino acid sequence and sialic acid content	629:692	By combined analysis of amino acid sequence and sialic acid content, we found that bovine factor X had an O-linked oligosaccharide chain linked to Thr26, and human factor X had four carbohydrate-attachment sites, namely, O-glycosidic linkages to Thr17 and Thr29, respectively, and N-glycosidic linkages to Asn39 and Asn49, respectively, in their activation peptides.
8243461	2	69	theme	protease-digested	290:306	arg1	glycopeptides					308:320	protease-digested glycopeptides	290:320	protease-digested glycopeptides derived from the activation peptides of bovine and human blood coagulation factor X	290:404	Analysis of protease-digested glycopeptides derived from the activation peptides of bovine and human blood coagulation factor X allowed the identification of sites of the O-linked oligosaccharide chains in these peptides.
8243461	4	70	theme	N-glycosidic	907:918	arg1	linkages					920:927	N-glycosidic linkages	907:927	N-glycosidic linkages to Asn39 and Asn49	907:946	By combined analysis of amino acid sequence and sialic acid content, we found that bovine factor X had an O-linked oligosaccharide chain linked to Thr26, and human factor X had four carbohydrate-attachment sites, namely, O-glycosidic linkages to Thr17 and Thr29, respectively, and N-glycosidic linkages to Asn39 and Asn49, respectively, in their activation peptides.
8243461	2	71	from	peptides	490:497	arg1	chains					474:479	the O-linked oligosaccharide chains	445:479	the O-linked oligosaccharide chains in these peptides	445:497	Analysis of protease-digested glycopeptides derived from the activation peptides of bovine and human blood coagulation factor X allowed the identification of sites of the O-linked oligosaccharide chains in these peptides.
8243461	2	71	from	peptides	490:497	arg1	sites					436:440	sites	436:440	sites of the O-linked oligosaccharide chains in these peptides	436:497	Analysis of protease-digested glycopeptides derived from the activation peptides of bovine and human blood coagulation factor X allowed the identification of sites of the O-linked oligosaccharide chains in these peptides.
8243461	4	72	theme	amino	650:654	arg1	sequence					661:668	amino acid sequence	650:668	amino acid sequence	650:668	By combined analysis of amino acid sequence and sialic acid content, we found that bovine factor X had an O-linked oligosaccharide chain linked to Thr26, and human factor X had four carbohydrate-attachment sites, namely, O-glycosidic linkages to Thr17 and Thr29, respectively, and N-glycosidic linkages to Asn39 and Asn49, respectively, in their activation peptides.
8243461	5	73	theme	derivatives	1092:1102	arg1	yields					1062:1067	the yields	1058:1067	the yields of phenylthiohydantoin derivatives of amino acids that corresponded to their residues	1058:1153	The O-linked carbohydrate-attachment sites were identified since the yields of phenylthiohydantoin derivatives of amino acids that corresponded to their residues were increased during amino acid sequencing after deglycosylation of the glycopeptides with sialidase and O-glycanase.
8243461	1	74	theme	X	198:198	arg1	Conversion					177:186	factor X. Conversion	167:186	factor X. Conversion of factor X to factor Xa	167:211	The role of the carbohydrate moieties in the activation of factor X. Conversion of factor X to factor Xa results in release of a heavily glycosylated activation peptide.
8243461	5	75	gly	deglycosylation	1205:1219	arg1	glycopeptides					1228:1240	the glycopeptides	1224:1240	the glycopeptides with sialidase and O-glycanase	1224:1271	The O-linked carbohydrate-attachment sites were identified since the yields of phenylthiohydantoin derivatives of amino acids that corresponded to their residues were increased during amino acid sequencing after deglycosylation of the glycopeptides with sialidase and O-glycanase.
8243461	4	76	theme	sequence	661:668	arg1	analysis					638:645	combined analysis	629:645	combined analysis of amino acid sequence and sialic acid content	629:692	By combined analysis of amino acid sequence and sialic acid content, we found that bovine factor X had an O-linked oligosaccharide chain linked to Thr26, and human factor X had four carbohydrate-attachment sites, namely, O-glycosidic linkages to Thr17 and Thr29, respectively, and N-glycosidic linkages to Asn39 and Asn49, respectively, in their activation peptides.
8243461	5	77	theme	amino	1107:1111	arg1	acids					1113:1117	amino acids	1107:1117	amino acids that corresponded to their residues	1107:1153	The O-linked carbohydrate-attachment sites were identified since the yields of phenylthiohydantoin derivatives of amino acids that corresponded to their residues were increased during amino acid sequencing after deglycosylation of the glycopeptides with sialidase and O-glycanase.
8243461	3	78	theme	aureus	606:611	arg1	protease					616:623	Staphylococcus aureus V8 protease	591:623	Staphylococcus aureus V8 protease	591:623	Glycopeptides were prepared from the activation peptides by digestion with chymotrypsin or Staphylococcus aureus V8 protease.
8243461	1	79	gly	glycosylated	245:256	arg1	peptide					269:275	a heavily glycosylated activation peptide	235:275	a heavily glycosylated activation peptide	235:275	The role of the carbohydrate moieties in the activation of factor X. Conversion of factor X to factor Xa results in release of a heavily glycosylated activation peptide.
8243461	7	80	theme	activation	1654:1663	arg1	rate					1646:1649	the rate	1642:1649	the rate of activation	1642:1663	The removal of O-linked carbohydrate resulted in a decrease in the rate of activation.
8243461	4	81	theme	factor	716:721	arg1	X					723:723	bovine factor X	709:723	bovine factor X	709:723	By combined analysis of amino acid sequence and sialic acid content, we found that bovine factor X had an O-linked oligosaccharide chain linked to Thr26, and human factor X had four carbohydrate-attachment sites, namely, O-glycosidic linkages to Thr17 and Thr29, respectively, and N-glycosidic linkages to Asn39 and Asn49, respectively, in their activation peptides.
8243461	4	82	attach	linked	763:768	arg1	Thr26					773:777	Thr26	773:777	Thr26	773:777	By combined analysis of amino acid sequence and sialic acid content, we found that bovine factor X had an O-linked oligosaccharide chain linked to Thr26, and human factor X had four carbohydrate-attachment sites, namely, O-glycosidic linkages to Thr17 and Thr29, respectively, and N-glycosidic linkages to Asn39 and Asn49, respectively, in their activation peptides.
8243461	4	82	attach	linked	763:768	arg2	chain					757:761	an O-linked oligosaccharide chain	729:761	an O-linked oligosaccharide chain linked to Thr26	729:777	By combined analysis of amino acid sequence and sialic acid content, we found that bovine factor X had an O-linked oligosaccharide chain linked to Thr26, and human factor X had four carbohydrate-attachment sites, namely, O-glycosidic linkages to Thr17 and Thr29, respectively, and N-glycosidic linkages to Asn39 and Asn49, respectively, in their activation peptides.
8243461	6	83	theme	factor-X-activating	1346:1364	arg1	enzyme					1366:1371	factor-X-activating enzyme	1346:1371	factor-X-activating enzyme from Russell's viper venom	1346:1398	The effect of deglycosylation of bovine factor X1 was investigated with factor-X-activating enzyme from Russell's viper venom or extrinsic Xase (factor VIIa/tissue factor/phospholipid) by examining the activation rates of derivatives of factor X prepared using O-glycanase, sialidase, and/or N-glycanase.
8243461	4	84	contain	had	799:801	arg1	X					797:797	human factor X	784:797	human factor X	784:797	By combined analysis of amino acid sequence and sialic acid content, we found that bovine factor X had an O-linked oligosaccharide chain linked to Thr26, and human factor X had four carbohydrate-attachment sites, namely, O-glycosidic linkages to Thr17 and Thr29, respectively, and N-glycosidic linkages to Asn39 and Asn49, respectively, in their activation peptides.
8243461	4	84	contain	had	799:801	arg2	linkages					920:927	N-glycosidic linkages	907:927	N-glycosidic linkages to Asn39 and Asn49	907:946	By combined analysis of amino acid sequence and sialic acid content, we found that bovine factor X had an O-linked oligosaccharide chain linked to Thr26, and human factor X had four carbohydrate-attachment sites, namely, O-glycosidic linkages to Thr17 and Thr29, respectively, and N-glycosidic linkages to Asn39 and Asn49, respectively, in their activation peptides.
8243461	4	84	contain	had	799:801	arg2	sites					832:836	four carbohydrate-attachment sites	803:836	four carbohydrate-attachment sites	803:836	By combined analysis of amino acid sequence and sialic acid content, we found that bovine factor X had an O-linked oligosaccharide chain linked to Thr26, and human factor X had four carbohydrate-attachment sites, namely, O-glycosidic linkages to Thr17 and Thr29, respectively, and N-glycosidic linkages to Asn39 and Asn49, respectively, in their activation peptides.
8243461	4	84	contain	had	799:801	arg2	linkages					860:867	O-glycosidic linkages	847:867	O-glycosidic linkages to Thr17 and Thr29, respectively	847:900	By combined analysis of amino acid sequence and sialic acid content, we found that bovine factor X had an O-linked oligosaccharide chain linked to Thr26, and human factor X had four carbohydrate-attachment sites, namely, O-glycosidic linkages to Thr17 and Thr29, respectively, and N-glycosidic linkages to Asn39 and Asn49, respectively, in their activation peptides.
8243461	1	85	theme	moieties	137:144	arg1	role					112:115	The role	108:115	The role of the carbohydrate moieties in the activation of factor X. Conversion of factor X to factor Xa	108:211	The role of the carbohydrate moieties in the activation of factor X. Conversion of factor X to factor Xa results in release of a heavily glycosylated activation peptide.
8243461	2	86	from	sites	436:440	arg1	peptides					490:497	these peptides	484:497	these peptides	484:497	Analysis of protease-digested glycopeptides derived from the activation peptides of bovine and human blood coagulation factor X allowed the identification of sites of the O-linked oligosaccharide chains in these peptides.
8243461	0	87	theme	coagulation	86:96	arg1	X					105:105	blood coagulation factor X	80:105	blood coagulation factor X	80:105	Identification of O-linked oligosaccharide chains in the activation peptides of blood coagulation factor X.
8243461	0	88	theme	X	105:105	arg1	peptides					68:75	the activation peptides	53:75	the activation peptides of blood coagulation factor X	53:105	Identification of O-linked oligosaccharide chains in the activation peptides of blood coagulation factor X.
8243461	6	89	theme	extrinsic	1403:1411	arg1	Xase					1413:1416	extrinsic Xase	1403:1416	extrinsic Xase (factor VIIa/tissue factor/phospholipid)	1403:1457	The effect of deglycosylation of bovine factor X1 was investigated with factor-X-activating enzyme from Russell's viper venom or extrinsic Xase (factor VIIa/tissue factor/phospholipid) by examining the activation rates of derivatives of factor X prepared using O-glycanase, sialidase, and/or N-glycanase.
8243461	6	89	theme	extrinsic	1403:1411	arg1	factor/phospholipid					1438:1456	factor VIIa/tissue factor/phospholipid	1419:1456	factor VIIa/tissue factor/phospholipid	1419:1456	The effect of deglycosylation of bovine factor X1 was investigated with factor-X-activating enzyme from Russell's viper venom or extrinsic Xase (factor VIIa/tissue factor/phospholipid) by examining the activation rates of derivatives of factor X prepared using O-glycanase, sialidase, and/or N-glycanase.
8243461	2	90	theme	coagulation	385:395	arg1	X					404:404	bovine and human blood coagulation factor X	362:404	bovine and human blood coagulation factor X	362:404	Analysis of protease-digested glycopeptides derived from the activation peptides of bovine and human blood coagulation factor X allowed the identification of sites of the O-linked oligosaccharide chains in these peptides.
8243461	4	91	theme	O-linked	732:739	arg1	chain					757:761	an O-linked oligosaccharide chain	729:761	an O-linked oligosaccharide chain linked to Thr26	729:777	By combined analysis of amino acid sequence and sialic acid content, we found that bovine factor X had an O-linked oligosaccharide chain linked to Thr26, and human factor X had four carbohydrate-attachment sites, namely, O-glycosidic linkages to Thr17 and Thr29, respectively, and N-glycosidic linkages to Asn39 and Asn49, respectively, in their activation peptides.
8243461	2	92	theme	human	373:377	arg1	X					404:404	bovine and human blood coagulation factor X	362:404	bovine and human blood coagulation factor X	362:404	Analysis of protease-digested glycopeptides derived from the activation peptides of bovine and human blood coagulation factor X allowed the identification of sites of the O-linked oligosaccharide chains in these peptides.
8243461	0	93	theme	oligosaccharide	27:41	arg1	chains					43:48	O-linked oligosaccharide chains	18:48	O-linked oligosaccharide chains in the activation peptides of blood coagulation factor X	18:105	Identification of O-linked oligosaccharide chains in the activation peptides of blood coagulation factor X.
8243461	1	94	theme	activation	258:267	arg1	peptide					269:275	a heavily glycosylated activation peptide	235:275	a heavily glycosylated activation peptide	235:275	The role of the carbohydrate moieties in the activation of factor X. Conversion of factor X to factor Xa results in release of a heavily glycosylated activation peptide.
8243461	6	95	theme	activation	1476:1485	arg1	rates					1487:1491	the activation rates	1472:1491	the activation rates of derivatives of factor X prepared using O-glycanase, sialidase, and/or N-glycanase	1472:1576	The effect of deglycosylation of bovine factor X1 was investigated with factor-X-activating enzyme from Russell's viper venom or extrinsic Xase (factor VIIa/tissue factor/phospholipid) by examining the activation rates of derivatives of factor X prepared using O-glycanase, sialidase, and/or N-glycanase.
8243461	7	96	theme	carbohydrate	1603:1614	arg1	removal					1583:1589	The removal	1579:1589	The removal of O-linked carbohydrate	1579:1614	The removal of O-linked carbohydrate resulted in a decrease in the rate of activation.
8243461	5	97	theme	carbohydrate-attachment	1006:1028	arg1	sites					1030:1034	The O-linked carbohydrate-attachment sites	993:1034	The O-linked carbohydrate-attachment sites	993:1034	The O-linked carbohydrate-attachment sites were identified since the yields of phenylthiohydantoin derivatives of amino acids that corresponded to their residues were increased during amino acid sequencing after deglycosylation of the glycopeptides with sialidase and O-glycanase.
8243461	2	98	theme	chains	474:479	arg1	chains					474:479	the O-linked oligosaccharide chains	445:479	the O-linked oligosaccharide chains in these peptides	445:497	Analysis of protease-digested glycopeptides derived from the activation peptides of bovine and human blood coagulation factor X allowed the identification of sites of the O-linked oligosaccharide chains in these peptides.
8243461	2	98	theme	chains	474:479	arg1	sites					436:440	sites	436:440	sites of the O-linked oligosaccharide chains in these peptides	436:497	Analysis of protease-digested glycopeptides derived from the activation peptides of bovine and human blood coagulation factor X allowed the identification of sites of the O-linked oligosaccharide chains in these peptides.
8243461	2	99	theme	X	404:404	arg1	peptides					350:357	the activation peptides	335:357	the activation peptides of bovine and human blood coagulation factor X	335:404	Analysis of protease-digested glycopeptides derived from the activation peptides of bovine and human blood coagulation factor X allowed the identification of sites of the O-linked oligosaccharide chains in these peptides.
8243461	0	100	theme	activation	57:66	arg1	peptides					68:75	the activation peptides	53:75	the activation peptides of blood coagulation factor X	53:105	Identification of O-linked oligosaccharide chains in the activation peptides of blood coagulation factor X.
8243461	5	101	theme	amino	1177:1181	arg1	sequencing					1188:1197	amino acid sequencing	1177:1197	amino acid sequencing	1177:1197	The O-linked carbohydrate-attachment sites were identified since the yields of phenylthiohydantoin derivatives of amino acids that corresponded to their residues were increased during amino acid sequencing after deglycosylation of the glycopeptides with sialidase and O-glycanase.
8243461	2	102	theme	O-linked	449:456	arg1	chains					474:479	the O-linked oligosaccharide chains	445:479	the O-linked oligosaccharide chains in these peptides	445:497	Analysis of protease-digested glycopeptides derived from the activation peptides of bovine and human blood coagulation factor X allowed the identification of sites of the O-linked oligosaccharide chains in these peptides.
8243461	5	103	with	glycopeptides	1228:1240	arg1	sialidase					1247:1255	sialidase	1247:1255	sialidase	1247:1255	The O-linked carbohydrate-attachment sites were identified since the yields of phenylthiohydantoin derivatives of amino acids that corresponded to their residues were increased during amino acid sequencing after deglycosylation of the glycopeptides with sialidase and O-glycanase.
8243461	5	103	with	glycopeptides	1228:1240	arg1	O-glycanase					1261:1271	O-glycanase	1261:1271	O-glycanase	1261:1271	The O-linked carbohydrate-attachment sites were identified since the yields of phenylthiohydantoin derivatives of amino acids that corresponded to their residues were increased during amino acid sequencing after deglycosylation of the glycopeptides with sialidase and O-glycanase.
8243461	4	104	theme	combined	629:636	arg1	analysis					638:645	combined analysis	629:645	combined analysis of amino acid sequence and sialic acid content	629:692	By combined analysis of amino acid sequence and sialic acid content, we found that bovine factor X had an O-linked oligosaccharide chain linked to Thr26, and human factor X had four carbohydrate-attachment sites, namely, O-glycosidic linkages to Thr17 and Thr29, respectively, and N-glycosidic linkages to Asn39 and Asn49, respectively, in their activation peptides.
8243461	4	105	theme	human	784:788	arg1	X					797:797	human factor X	784:797	human factor X	784:797	By combined analysis of amino acid sequence and sialic acid content, we found that bovine factor X had an O-linked oligosaccharide chain linked to Thr26, and human factor X had four carbohydrate-attachment sites, namely, O-glycosidic linkages to Thr17 and Thr29, respectively, and N-glycosidic linkages to Asn39 and Asn49, respectively, in their activation peptides.
8243461	2	106	gly	glycopeptides	308:320	arg2	glycopeptides					308:320	protease-digested glycopeptides	290:320	protease-digested glycopeptides derived from the activation peptides of bovine and human blood coagulation factor X	290:404	Analysis of protease-digested glycopeptides derived from the activation peptides of bovine and human blood coagulation factor X allowed the identification of sites of the O-linked oligosaccharide chains in these peptides.
8243461	2	107	theme	bovine	362:367	arg1	X					404:404	bovine and human blood coagulation factor X	362:404	bovine and human blood coagulation factor X	362:404	Analysis of protease-digested glycopeptides derived from the activation peptides of bovine and human blood coagulation factor X allowed the identification of sites of the O-linked oligosaccharide chains in these peptides.
8407880	0	0	theme	two-dimensional	81:95	arg1	mapping					103:109	two-dimensional sugar mapping	81:109	two-dimensional sugar mapping	81:109	Structural study of the N-linked oligosaccharides of hepatocyte growth factor by two-dimensional sugar mapping.
8407880	4	1	theme	oligosaccharide	682:696	arg1	structures					698:707	oligosaccharide structures	682:707	oligosaccharide structures	682:707	There was no significant difference in oligosaccharide structures between the two glycosylation sites on each chain, that is, Asn263 and Asn371 on the alpha-chain, and Asn535 and Asn622 on the beta-chain.
8407880	6	2	from	structures	977:986	arg1	HGF					1030:1032	rat HGF	1026:1032	rat HGF	1026:1032	The structures of the N-linked oligosaccharides from rat HGF were also studied.
8407880	1	3	theme	recombinant	163:173	arg1	factor					199:204	recombinant human hepatocyte growth factor	163:204	recombinant human hepatocyte growth factor (rh-HGF) expressed by Chinese hamster ovary (CHO) cells	163:260	The structures of the N-linked oligosaccharides on recombinant human hepatocyte growth factor (rh-HGF) expressed by Chinese hamster ovary (CHO) cells were studied by two-dimensional sugar mapping.
8407880	1	3	theme	recombinant	163:173	arg1	rh-HGF					207:212	rh-HGF	207:212	rh-HGF	207:212	The structures of the N-linked oligosaccharides on recombinant human hepatocyte growth factor (rh-HGF) expressed by Chinese hamster ovary (CHO) cells were studied by two-dimensional sugar mapping.
8407880	1	4	theme	CHO	251:253	arg1	cells					256:260	Chinese hamster ovary (CHO) cells	228:260	Chinese hamster ovary (CHO) cells	228:260	The structures of the N-linked oligosaccharides on recombinant human hepatocyte growth factor (rh-HGF) expressed by Chinese hamster ovary (CHO) cells were studied by two-dimensional sugar mapping.
8407880	5	5	theme	acid	870:873	arg1	alpha					938:942	NeuAc alpha	932:942	NeuAc alpha(2-3)	932:947	The linkage of sialic acid to the non-reducing terminal galactose was identified as NeuAc alpha(2-3) by 1H-NMR spectrometry.
8407880	5	5	theme	acid	870:873	arg1	linkage					852:858	The linkage	848:858	The linkage of sialic acid to the non-reducing terminal galactose	848:912	The linkage of sialic acid to the non-reducing terminal galactose was identified as NeuAc alpha(2-3) by 1H-NMR spectrometry.
8407880	1	6	theme	human	175:179	arg1	factor					199:204	recombinant human hepatocyte growth factor	163:204	recombinant human hepatocyte growth factor (rh-HGF) expressed by Chinese hamster ovary (CHO) cells	163:260	The structures of the N-linked oligosaccharides on recombinant human hepatocyte growth factor (rh-HGF) expressed by Chinese hamster ovary (CHO) cells were studied by two-dimensional sugar mapping.
8407880	1	6	theme	human	175:179	arg1	rh-HGF					207:212	rh-HGF	207:212	rh-HGF	207:212	The structures of the N-linked oligosaccharides on recombinant human hepatocyte growth factor (rh-HGF) expressed by Chinese hamster ovary (CHO) cells were studied by two-dimensional sugar mapping.
8407880	8	7	attach	linked	1237:1242	arg2	alpha-chain					1217:1227	the alpha-chain	1213:1227	the alpha-chain	1213:1227	This result indicates that the alpha-chain is also linked by higher branched oligosaccharides than the beta-chain in rat HGF.
8407880	8	7	attach	linked	1237:1242	arg3	oligosaccharides					1263:1278	higher branched oligosaccharides	1247:1278	higher branched oligosaccharides than the beta-chain in rat HGF	1247:1309	This result indicates that the alpha-chain is also linked by higher branched oligosaccharides than the beta-chain in rat HGF.
8407880	3	8	theme	triantennary	509:520	arg1	oligosaccharides					542:557	biantennary, triantennary, and tetraantennary oligosaccharides	496:557	biantennary, triantennary, and tetraantennary oligosaccharides	496:557	The alpha-chain was linked by biantennary, triantennary, and tetraantennary oligosaccharides, but the dominant oligosaccharides linking the beta-chain were biantennary (> 85%).
8407880	0	9	theme	sugar	97:101	arg1	mapping					103:109	two-dimensional sugar mapping	81:109	two-dimensional sugar mapping	81:109	Structural study of the N-linked oligosaccharides of hepatocyte growth factor by two-dimensional sugar mapping.
8407880	8	10	from	beta-chain	1289:1298	arg1	HGF					1307:1309	rat HGF	1303:1309	rat HGF	1303:1309	This result indicates that the alpha-chain is also linked by higher branched oligosaccharides than the beta-chain in rat HGF.
8407880	2	11	theme	peptide	365:371	arg1	treatment					401:409	peptide: N-glycosidase F (PNGase F) treatment	365:409	peptide: N-glycosidase F (PNGase F) treatment	365:409	The oligosaccharides released from the glycopeptides by peptide: N-glycosidase F (PNGase F) treatment were tagged with 2-aminopyridine at the reducing ends.
8407880	4	12	from	difference	668:677	arg1	structures					698:707	oligosaccharide structures	682:707	oligosaccharide structures	682:707	There was no significant difference in oligosaccharide structures between the two glycosylation sites on each chain, that is, Asn263 and Asn371 on the alpha-chain, and Asn535 and Asn622 on the beta-chain.
8407880	4	13	theme	glycosylation	725:737	arg1	sites					739:743	the two glycosylation sites	717:743	the two glycosylation sites on each chain, that is, Asn263 and Asn371 on the alpha-chain, and Asn535 and Asn622 on the beta-chain	717:845	There was no significant difference in oligosaccharide structures between the two glycosylation sites on each chain, that is, Asn263 and Asn371 on the alpha-chain, and Asn535 and Asn622 on the beta-chain.
8407880	6	14	link	N-linked	995:1002	arg1	oligosaccharides					1004:1019	the N-linked oligosaccharides	991:1019	the N-linked oligosaccharides from rat HGF	991:1032	The structures of the N-linked oligosaccharides from rat HGF were also studied.
8407880	8	15	theme	higher	1247:1252	arg1	oligosaccharides					1263:1278	higher branched oligosaccharides	1247:1278	higher branched oligosaccharides than the beta-chain in rat HGF	1247:1309	This result indicates that the alpha-chain is also linked by higher branched oligosaccharides than the beta-chain in rat HGF.
8407880	8	16	theme	branched	1254:1261	arg1	oligosaccharides					1263:1278	higher branched oligosaccharides	1247:1278	higher branched oligosaccharides than the beta-chain in rat HGF	1247:1309	This result indicates that the alpha-chain is also linked by higher branched oligosaccharides than the beta-chain in rat HGF.
8407880	1	17	theme	hepatocyte	181:190	arg1	factor					199:204	recombinant human hepatocyte growth factor	163:204	recombinant human hepatocyte growth factor (rh-HGF) expressed by Chinese hamster ovary (CHO) cells	163:260	The structures of the N-linked oligosaccharides on recombinant human hepatocyte growth factor (rh-HGF) expressed by Chinese hamster ovary (CHO) cells were studied by two-dimensional sugar mapping.
8407880	1	17	theme	hepatocyte	181:190	arg1	rh-HGF					207:212	rh-HGF	207:212	rh-HGF	207:212	The structures of the N-linked oligosaccharides on recombinant human hepatocyte growth factor (rh-HGF) expressed by Chinese hamster ovary (CHO) cells were studied by two-dimensional sugar mapping.
8407880	2	18	attach	released	330:337	arg2	oligosaccharides					313:328	The oligosaccharides	309:328	The oligosaccharides released from the glycopeptides by peptide: N-glycosidase F (PNGase F) treatment	309:409	The oligosaccharides released from the glycopeptides by peptide: N-glycosidase F (PNGase F) treatment were tagged with 2-aminopyridine at the reducing ends.
8407880	2	18	attach	released	330:337	arg1	glycopeptides					348:360	the glycopeptides	344:360	the glycopeptides	344:360	The oligosaccharides released from the glycopeptides by peptide: N-glycosidase F (PNGase F) treatment were tagged with 2-aminopyridine at the reducing ends.
8407880	7	19	theme	biantennary	1124:1134	arg1	oligosaccharide					1136:1150	a biantennary oligosaccharide	1122:1150	a biantennary oligosaccharide	1122:1150	Triantennary oligosaccharides were obtained from the alpha-chain and a biantennary oligosaccharide was obtained from the beta-chain.
8407880	3	20	theme	tetraantennary	527:540	arg1	oligosaccharides					542:557	biantennary, triantennary, and tetraantennary oligosaccharides	496:557	biantennary, triantennary, and tetraantennary oligosaccharides	496:557	The alpha-chain was linked by biantennary, triantennary, and tetraantennary oligosaccharides, but the dominant oligosaccharides linking the beta-chain were biantennary (> 85%).
8407880	1	21	theme	growth	192:197	arg1	factor					199:204	recombinant human hepatocyte growth factor	163:204	recombinant human hepatocyte growth factor (rh-HGF) expressed by Chinese hamster ovary (CHO) cells	163:260	The structures of the N-linked oligosaccharides on recombinant human hepatocyte growth factor (rh-HGF) expressed by Chinese hamster ovary (CHO) cells were studied by two-dimensional sugar mapping.
8407880	1	21	theme	growth	192:197	arg1	rh-HGF					207:212	rh-HGF	207:212	rh-HGF	207:212	The structures of the N-linked oligosaccharides on recombinant human hepatocyte growth factor (rh-HGF) expressed by Chinese hamster ovary (CHO) cells were studied by two-dimensional sugar mapping.
8407880	4	22	from	chain	753:757	arg1	alpha-chain					794:804	the alpha-chain	790:804	the alpha-chain	790:804	There was no significant difference in oligosaccharide structures between the two glycosylation sites on each chain, that is, Asn263 and Asn371 on the alpha-chain, and Asn535 and Asn622 on the beta-chain.
8407880	4	22	from	chain	753:757	arg1	beta-chain					836:845	the beta-chain	832:845	the beta-chain	832:845	There was no significant difference in oligosaccharide structures between the two glycosylation sites on each chain, that is, Asn263 and Asn371 on the alpha-chain, and Asn535 and Asn622 on the beta-chain.
8407880	3	23	theme	dominant	568:575	arg1	biantennary					622:632	biantennary	622:632	biantennary (> 85%)	622:640	The alpha-chain was linked by biantennary, triantennary, and tetraantennary oligosaccharides, but the dominant oligosaccharides linking the beta-chain were biantennary (> 85%).
8407880	3	23	theme	dominant	568:575	arg1	oligosaccharides					577:592	the dominant oligosaccharides	564:592	the dominant oligosaccharides linking the beta-chain	564:615	The alpha-chain was linked by biantennary, triantennary, and tetraantennary oligosaccharides, but the dominant oligosaccharides linking the beta-chain were biantennary (> 85%).
8407880	2	24	gly	glycopeptides	348:360	arg2	glycopeptides					348:360	the glycopeptides	344:360	the glycopeptides	344:360	The oligosaccharides released from the glycopeptides by peptide: N-glycosidase F (PNGase F) treatment were tagged with 2-aminopyridine at the reducing ends.
8407880	0	25	theme	Structural	0:9	arg1	study					11:15	Structural study	0:15	Structural study of the N-linked oligosaccharides of hepatocyte growth factor by two-dimensional sugar mapping	0:109	Structural study of the N-linked oligosaccharides of hepatocyte growth factor by two-dimensional sugar mapping.
8407880	7	26	theme	Triantennary	1053:1064	arg1	oligosaccharides					1066:1081	Triantennary oligosaccharides	1053:1081	Triantennary oligosaccharides	1053:1081	Triantennary oligosaccharides were obtained from the alpha-chain and a biantennary oligosaccharide was obtained from the beta-chain.
8407880	1	27	from	structures	116:125	arg1	factor					199:204	recombinant human hepatocyte growth factor	163:204	recombinant human hepatocyte growth factor (rh-HGF) expressed by Chinese hamster ovary (CHO) cells	163:260	The structures of the N-linked oligosaccharides on recombinant human hepatocyte growth factor (rh-HGF) expressed by Chinese hamster ovary (CHO) cells were studied by two-dimensional sugar mapping.
8407880	1	27	from	structures	116:125	arg1	rh-HGF					207:212	rh-HGF	207:212	rh-HGF	207:212	The structures of the N-linked oligosaccharides on recombinant human hepatocyte growth factor (rh-HGF) expressed by Chinese hamster ovary (CHO) cells were studied by two-dimensional sugar mapping.
8407880	2	28	theme	F	388:388	arg1	treatment					401:409	peptide: N-glycosidase F (PNGase F) treatment	365:409	peptide: N-glycosidase F (PNGase F) treatment	365:409	The oligosaccharides released from the glycopeptides by peptide: N-glycosidase F (PNGase F) treatment were tagged with 2-aminopyridine at the reducing ends.
8407880	8	29	theme	rat	1303:1305	arg1	HGF					1307:1309	rat HGF	1303:1309	rat HGF	1303:1309	This result indicates that the alpha-chain is also linked by higher branched oligosaccharides than the beta-chain in rat HGF.
8407880	0	30	link	N-linked	24:31	arg1	oligosaccharides					33:48	the N-linked oligosaccharides	20:48	the N-linked oligosaccharides of hepatocyte growth factor	20:76	Structural study of the N-linked oligosaccharides of hepatocyte growth factor by two-dimensional sugar mapping.
8407880	6	31	theme	rat	1026:1028	arg1	HGF					1030:1032	rat HGF	1026:1032	rat HGF	1026:1032	The structures of the N-linked oligosaccharides from rat HGF were also studied.
8407880	1	32	theme	two-dimensional	278:292	arg1	mapping					300:306	two-dimensional sugar mapping	278:306	two-dimensional sugar mapping	278:306	The structures of the N-linked oligosaccharides on recombinant human hepatocyte growth factor (rh-HGF) expressed by Chinese hamster ovary (CHO) cells were studied by two-dimensional sugar mapping.
8407880	5	33	theme	NeuAc	932:936	arg1	2-3					944:946	2-3	944:946	2-3	944:946	The linkage of sialic acid to the non-reducing terminal galactose was identified as NeuAc alpha(2-3) by 1H-NMR spectrometry.
8407880	5	33	theme	NeuAc	932:936	arg1	alpha					938:942	NeuAc alpha	932:942	NeuAc alpha(2-3)	932:947	The linkage of sialic acid to the non-reducing terminal galactose was identified as NeuAc alpha(2-3) by 1H-NMR spectrometry.
8407880	5	33	theme	NeuAc	932:936	arg1	linkage					852:858	The linkage	848:858	The linkage of sialic acid to the non-reducing terminal galactose	848:912	The linkage of sialic acid to the non-reducing terminal galactose was identified as NeuAc alpha(2-3) by 1H-NMR spectrometry.
8407880	2	34	theme	N-glycosidase	374:386	arg1	F					388:388	N-glycosidase F	374:388	peptide: N-glycosidase F (PNGase F) treatment	365:409	The oligosaccharides released from the glycopeptides by peptide: N-glycosidase F (PNGase F) treatment were tagged with 2-aminopyridine at the reducing ends.
8407880	2	34	theme	N-glycosidase	374:386	arg1	F					398:398	PNGase F	391:398	PNGase F	391:398	The oligosaccharides released from the glycopeptides by peptide: N-glycosidase F (PNGase F) treatment were tagged with 2-aminopyridine at the reducing ends.
8407880	0	35	theme	oligosaccharides	33:48	arg1	study					11:15	Structural study	0:15	Structural study of the N-linked oligosaccharides of hepatocyte growth factor by two-dimensional sugar mapping	0:109	Structural study of the N-linked oligosaccharides of hepatocyte growth factor by two-dimensional sugar mapping.
8407880	1	36	theme	sugar	294:298	arg1	mapping					300:306	two-dimensional sugar mapping	278:306	two-dimensional sugar mapping	278:306	The structures of the N-linked oligosaccharides on recombinant human hepatocyte growth factor (rh-HGF) expressed by Chinese hamster ovary (CHO) cells were studied by two-dimensional sugar mapping.
8407880	4	37	gly	glycosylation	725:737	arg2	sites					739:743	the two glycosylation sites	717:743	the two glycosylation sites on each chain, that is, Asn263 and Asn371 on the alpha-chain, and Asn535 and Asn622 on the beta-chain	717:845	There was no significant difference in oligosaccharide structures between the two glycosylation sites on each chain, that is, Asn263 and Asn371 on the alpha-chain, and Asn535 and Asn622 on the beta-chain.
8407880	4	37	gly	glycosylation	725:737	arg2	two					721:723	two	721:723	two	721:723	There was no significant difference in oligosaccharide structures between the two glycosylation sites on each chain, that is, Asn263 and Asn371 on the alpha-chain, and Asn535 and Asn622 on the beta-chain.
8407880	4	38	theme	significant	656:666	arg1	difference					668:677	no significant difference	653:677	no significant difference in oligosaccharide structures between the two glycosylation sites on each chain, that is, Asn263 and Asn371 on the alpha-chain, and Asn535 and Asn622 on the beta-chain	653:845	There was no significant difference in oligosaccharide structures between the two glycosylation sites on each chain, that is, Asn263 and Asn371 on the alpha-chain, and Asn535 and Asn622 on the beta-chain.
8407880	6	39	theme	oligosaccharides	1004:1019	arg1	structures					977:986	The structures	973:986	The structures of the N-linked oligosaccharides from rat HGF	973:1032	The structures of the N-linked oligosaccharides from rat HGF were also studied.
8407880	0	40	theme	N-linked	24:31	arg1	oligosaccharides					33:48	the N-linked oligosaccharides	20:48	the N-linked oligosaccharides of hepatocyte growth factor	20:76	Structural study of the N-linked oligosaccharides of hepatocyte growth factor by two-dimensional sugar mapping.
8407880	4	41	from	Asn535	811:816	arg1	alpha-chain					794:804	the alpha-chain	790:804	the alpha-chain	790:804	There was no significant difference in oligosaccharide structures between the two glycosylation sites on each chain, that is, Asn263 and Asn371 on the alpha-chain, and Asn535 and Asn622 on the beta-chain.
8407880	4	41	from	Asn535	811:816	arg1	beta-chain					836:845	the beta-chain	832:845	the beta-chain	832:845	There was no significant difference in oligosaccharide structures between the two glycosylation sites on each chain, that is, Asn263 and Asn371 on the alpha-chain, and Asn535 and Asn622 on the beta-chain.
8407880	6	42	theme	N-linked	995:1002	arg1	oligosaccharides					1004:1019	the N-linked oligosaccharides	991:1019	the N-linked oligosaccharides from rat HGF	991:1032	The structures of the N-linked oligosaccharides from rat HGF were also studied.
8407880	0	43	theme	hepatocyte	53:62	arg1	factor					71:76	hepatocyte growth factor	53:76	hepatocyte growth factor	53:76	Structural study of the N-linked oligosaccharides of hepatocyte growth factor by two-dimensional sugar mapping.
8407880	3	44	theme	biantennary	496:506	arg1	oligosaccharides					542:557	biantennary, triantennary, and tetraantennary oligosaccharides	496:557	biantennary, triantennary, and tetraantennary oligosaccharides	496:557	The alpha-chain was linked by biantennary, triantennary, and tetraantennary oligosaccharides, but the dominant oligosaccharides linking the beta-chain were biantennary (> 85%).
8407880	4	45	from	Asn622	822:827	arg1	alpha-chain					794:804	the alpha-chain	790:804	the alpha-chain	790:804	There was no significant difference in oligosaccharide structures between the two glycosylation sites on each chain, that is, Asn263 and Asn371 on the alpha-chain, and Asn535 and Asn622 on the beta-chain.
8407880	4	45	from	Asn622	822:827	arg1	beta-chain					836:845	the beta-chain	832:845	the beta-chain	832:845	There was no significant difference in oligosaccharide structures between the two glycosylation sites on each chain, that is, Asn263 and Asn371 on the alpha-chain, and Asn535 and Asn622 on the beta-chain.
8407880	2	46	theme	reducing	451:458	arg1	ends					460:463	the reducing ends	447:463	the reducing ends	447:463	The oligosaccharides released from the glycopeptides by peptide: N-glycosidase F (PNGase F) treatment were tagged with 2-aminopyridine at the reducing ends.
8407880	1	47	link	N-linked	134:141	arg1	oligosaccharides					143:158	the N-linked oligosaccharides	130:158	the N-linked oligosaccharides	130:158	The structures of the N-linked oligosaccharides on recombinant human hepatocyte growth factor (rh-HGF) expressed by Chinese hamster ovary (CHO) cells were studied by two-dimensional sugar mapping.
8407880	5	48	theme	non-reducing	882:893	arg1	galactose					904:912	the non-reducing terminal galactose	878:912	the non-reducing terminal galactose	878:912	The linkage of sialic acid to the non-reducing terminal galactose was identified as NeuAc alpha(2-3) by 1H-NMR spectrometry.
8407880	4	49	from	sites	739:743	arg1	chain					753:757	each chain	748:757	each chain	748:757	There was no significant difference in oligosaccharide structures between the two glycosylation sites on each chain, that is, Asn263 and Asn371 on the alpha-chain, and Asn535 and Asn622 on the beta-chain.
8407880	4	49	from	sites	739:743	arg1	Asn535					811:816	Asn535	811:816	Asn535	811:816	There was no significant difference in oligosaccharide structures between the two glycosylation sites on each chain, that is, Asn263 and Asn371 on the alpha-chain, and Asn535 and Asn622 on the beta-chain.
8407880	4	49	from	sites	739:743	arg1	Asn263					769:774	Asn263	769:774	Asn263	769:774	There was no significant difference in oligosaccharide structures between the two glycosylation sites on each chain, that is, Asn263 and Asn371 on the alpha-chain, and Asn535 and Asn622 on the beta-chain.
8407880	3	50	theme	>	635:635	arg1	%					639:639	> 85%	635:639	> 85%	635:639	The alpha-chain was linked by biantennary, triantennary, and tetraantennary oligosaccharides, but the dominant oligosaccharides linking the beta-chain were biantennary (> 85%).
8407880	3	50	theme	>	635:635	arg1	biantennary					622:632	biantennary	622:632	biantennary (> 85%)	622:640	The alpha-chain was linked by biantennary, triantennary, and tetraantennary oligosaccharides, but the dominant oligosaccharides linking the beta-chain were biantennary (> 85%).
8407880	6	51	from	HGF	1030:1032	arg1	structures					977:986	The structures	973:986	The structures of the N-linked oligosaccharides from rat HGF	973:1032	The structures of the N-linked oligosaccharides from rat HGF were also studied.
8407880	6	51	from	HGF	1030:1032	arg1	oligosaccharides					1004:1019	the N-linked oligosaccharides	991:1019	the N-linked oligosaccharides from rat HGF	991:1032	The structures of the N-linked oligosaccharides from rat HGF were also studied.
8407880	5	52	theme	terminal	895:902	arg1	galactose					904:912	the non-reducing terminal galactose	878:912	the non-reducing terminal galactose	878:912	The linkage of sialic acid to the non-reducing terminal galactose was identified as NeuAc alpha(2-3) by 1H-NMR spectrometry.
8407880	1	53	theme	Chinese	228:234	arg1	cells					256:260	Chinese hamster ovary (CHO) cells	228:260	Chinese hamster ovary (CHO) cells	228:260	The structures of the N-linked oligosaccharides on recombinant human hepatocyte growth factor (rh-HGF) expressed by Chinese hamster ovary (CHO) cells were studied by two-dimensional sugar mapping.
8407880	5	54	theme	1H-NMR	952:957	arg1	spectrometry					959:970	1H-NMR spectrometry	952:970	1H-NMR spectrometry	952:970	The linkage of sialic acid to the non-reducing terminal galactose was identified as NeuAc alpha(2-3) by 1H-NMR spectrometry.
8407880	1	55	theme	N-linked	134:141	arg1	oligosaccharides					143:158	the N-linked oligosaccharides	130:158	the N-linked oligosaccharides	130:158	The structures of the N-linked oligosaccharides on recombinant human hepatocyte growth factor (rh-HGF) expressed by Chinese hamster ovary (CHO) cells were studied by two-dimensional sugar mapping.
8407880	1	56	theme	hamster	236:242	arg1	cells					256:260	Chinese hamster ovary (CHO) cells	228:260	Chinese hamster ovary (CHO) cells	228:260	The structures of the N-linked oligosaccharides on recombinant human hepatocyte growth factor (rh-HGF) expressed by Chinese hamster ovary (CHO) cells were studied by two-dimensional sugar mapping.
8407880	0	57	theme	factor	71:76	arg1	oligosaccharides					33:48	the N-linked oligosaccharides	20:48	the N-linked oligosaccharides of hepatocyte growth factor	20:76	Structural study of the N-linked oligosaccharides of hepatocyte growth factor by two-dimensional sugar mapping.
8407880	3	58	attach	linked	486:491	arg2	alpha-chain					470:480	The alpha-chain	466:480	The alpha-chain	466:480	The alpha-chain was linked by biantennary, triantennary, and tetraantennary oligosaccharides, but the dominant oligosaccharides linking the beta-chain were biantennary (> 85%).
8407880	3	58	attach	linked	486:491	arg3	oligosaccharides					542:557	biantennary, triantennary, and tetraantennary oligosaccharides	496:557	biantennary, triantennary, and tetraantennary oligosaccharides	496:557	The alpha-chain was linked by biantennary, triantennary, and tetraantennary oligosaccharides, but the dominant oligosaccharides linking the beta-chain were biantennary (> 85%).
8407880	1	59	theme	oligosaccharides	143:158	arg1	structures					116:125	The structures	112:125	The structures of the N-linked oligosaccharides on recombinant human hepatocyte growth factor (rh-HGF) expressed by Chinese hamster ovary (CHO) cells	112:260	The structures of the N-linked oligosaccharides on recombinant human hepatocyte growth factor (rh-HGF) expressed by Chinese hamster ovary (CHO) cells were studied by two-dimensional sugar mapping.
8407880	2	60	theme	PNGase	391:396	arg1	F					388:388	N-glycosidase F	374:388	peptide: N-glycosidase F (PNGase F) treatment	365:409	The oligosaccharides released from the glycopeptides by peptide: N-glycosidase F (PNGase F) treatment were tagged with 2-aminopyridine at the reducing ends.
8407880	2	60	theme	PNGase	391:396	arg1	F					398:398	PNGase F	391:398	PNGase F	391:398	The oligosaccharides released from the glycopeptides by peptide: N-glycosidase F (PNGase F) treatment were tagged with 2-aminopyridine at the reducing ends.
8407880	1	61	theme	ovary	244:248	arg1	cells					256:260	Chinese hamster ovary (CHO) cells	228:260	Chinese hamster ovary (CHO) cells	228:260	The structures of the N-linked oligosaccharides on recombinant human hepatocyte growth factor (rh-HGF) expressed by Chinese hamster ovary (CHO) cells were studied by two-dimensional sugar mapping.
8407880	0	62	theme	growth	64:69	arg1	factor					71:76	hepatocyte growth factor	53:76	hepatocyte growth factor	53:76	Structural study of the N-linked oligosaccharides of hepatocyte growth factor by two-dimensional sugar mapping.
8407880	5	63	theme	sialic	863:868	arg1	acid					870:873	sialic acid	863:873	sialic acid	863:873	The linkage of sialic acid to the non-reducing terminal galactose was identified as NeuAc alpha(2-3) by 1H-NMR spectrometry.
18404400	8	0	theme	tertiary	1485:1492	arg1	structure					1508:1516	tertiary or quaternary structure	1485:1516	tertiary or quaternary structure	1485:1516	However, mutation at this site did not result in global changes in tertiary or quaternary structure as measured by Cibacron blue binding, chemical cross linking, and native gel electrophoretic analysis, leaving open the possibility of other mechanisms by which mutation of this conserved lysine residue might decrease enzyme activity.
18404400	0	1	theme	diphosphohydrolase	78:95	arg1	activity					37:44	activity	37:44	activity of ecto-nucleoside triphosphate diphosphohydrolase 3 (NTPDase3)	37:108	Conserved lysine 79 is important for activity of ecto-nucleoside triphosphate diphosphohydrolase 3 (NTPDase3).
18404400	5	2	theme	decreased	964:972	arg1	activities					987:996	decreased nucleotidase activities	964:996	decreased nucleotidase activities	964:996	This lysine residue was mutated to several different amino acids, and all mutants displayed substantially decreased nucleotidase activities.
18404400	8	3	theme	conserved	1696:1704	arg1	residue					1713:1719	this conserved lysine residue	1691:1719	this conserved lysine residue	1691:1719	However, mutation at this site did not result in global changes in tertiary or quaternary structure as measured by Cibacron blue binding, chemical cross linking, and native gel electrophoretic analysis, leaving open the possibility of other mechanisms by which mutation of this conserved lysine residue might decrease enzyme activity.
18404400	3	4	dep	soluble	537:543	arg1	monomeric					546:554	monomeric	546:554	monomeric	546:554	The residue corresponding to lysine 79 in NTPDase3 is conserved in all known cell surface membrane NTPDases (NTPDase1, 2, 3, and 8), but not in the soluble, monomeric NTPDases (NTPDase5 and 6), or in the intracellular, two transmembrane NTPDases (NTPDase4 and 7).
18404400	7	5	theme	wild-type	1262:1270	arg1	enzyme					1272:1277	the wild-type enzyme	1258:1277	the wild-type enzyme	1258:1277	After solubilization with Triton X-100, mutants showed little or no decrease in activity, unlike the wild-type enzyme, suggesting that the lysine at this position may be important for maintaining proper folding and for stabilizing the quaternary structure.
18404400	8	6	theme	electrophoretic	1595:1609	arg1	analysis					1611:1618	native gel electrophoretic analysis	1584:1618	native gel electrophoretic analysis	1584:1618	However, mutation at this site did not result in global changes in tertiary or quaternary structure as measured by Cibacron blue binding, chemical cross linking, and native gel electrophoretic analysis, leaving open the possibility of other mechanisms by which mutation of this conserved lysine residue might decrease enzyme activity.
18404400	4	7	theme	apyrase	694:700	arg1	ACR1					722:725	ACR1	722:725	ACR1	722:725	This conserved lysine is located between apyrase conserved region 1 (ACR1) and an invariant glycosylation site (N81), in a region previously hypothesized to be important for NTPDase3 oligomeric structure.
18404400	4	7	theme	apyrase	694:700	arg1	region					712:717	apyrase conserved region 1	694:719	apyrase conserved region 1 (ACR1)	694:726	This conserved lysine is located between apyrase conserved region 1 (ACR1) and an invariant glycosylation site (N81), in a region previously hypothesized to be important for NTPDase3 oligomeric structure.
18404400	8	8	theme	Cibacron	1533:1540	arg1	binding					1547:1553	Cibacron blue binding	1533:1553	Cibacron blue binding	1533:1553	However, mutation at this site did not result in global changes in tertiary or quaternary structure as measured by Cibacron blue binding, chemical cross linking, and native gel electrophoretic analysis, leaving open the possibility of other mechanisms by which mutation of this conserved lysine residue might decrease enzyme activity.
18404400	7	9	theme	proper	1357:1362	arg1	folding					1364:1370	proper folding	1357:1370	proper folding	1357:1370	After solubilization with Triton X-100, mutants showed little or no decrease in activity, unlike the wild-type enzyme, suggesting that the lysine at this position may be important for maintaining proper folding and for stabilizing the quaternary structure.
18404400	7	10	with	solubilization	1167:1180	arg1	X-100					1194:1198	Triton X-100	1187:1198	Triton X-100	1187:1198	After solubilization with Triton X-100, mutants showed little or no decrease in activity, unlike the wild-type enzyme, suggesting that the lysine at this position may be important for maintaining proper folding and for stabilizing the quaternary structure.
18404400	8	11	theme	residue	1713:1719	arg1	mutation					1679:1686	mutation	1679:1686	mutation of this conserved lysine residue	1679:1719	However, mutation at this site did not result in global changes in tertiary or quaternary structure as measured by Cibacron blue binding, chemical cross linking, and native gel electrophoretic analysis, leaving open the possibility of other mechanisms by which mutation of this conserved lysine residue might decrease enzyme activity.
18404400	6	12	theme	nucleotidase	1081:1092	arg1	activity					1094:1101	nucleotidase activity	1081:1101	nucleotidase activity	1081:1101	A basic amino acid at this position was found to be important for the increase of nucleotidase activity observed after treatment with the lectin, concanavalin A.
18404400	8	13	theme	gel	1591:1593	arg1	analysis					1611:1618	native gel electrophoretic analysis	1584:1618	native gel electrophoretic analysis	1584:1618	However, mutation at this site did not result in global changes in tertiary or quaternary structure as measured by Cibacron blue binding, chemical cross linking, and native gel electrophoretic analysis, leaving open the possibility of other mechanisms by which mutation of this conserved lysine residue might decrease enzyme activity.
18404400	2	14	theme	triphosphate	343:354	arg1	diphosphohydrolase					356:373	human ecto-nucleoside triphosphate diphosphohydrolase 3	321:375	human ecto-nucleoside triphosphate diphosphohydrolase 3 (NTPDase3)	321:386	In this study, we mutated lysine 79 in human ecto-nucleoside triphosphate diphosphohydrolase 3 (NTPDase3).
18404400	2	14	theme	triphosphate	343:354	arg1	NTPDase3					378:385	NTPDase3	378:385	NTPDase3	378:385	In this study, we mutated lysine 79 in human ecto-nucleoside triphosphate diphosphohydrolase 3 (NTPDase3).
18404400	8	15	theme	lysine	1706:1711	arg1	residue					1713:1719	this conserved lysine residue	1691:1719	this conserved lysine residue	1691:1719	However, mutation at this site did not result in global changes in tertiary or quaternary structure as measured by Cibacron blue binding, chemical cross linking, and native gel electrophoretic analysis, leaving open the possibility of other mechanisms by which mutation of this conserved lysine residue might decrease enzyme activity.
18404400	7	16	dep	important	1331:1339	arg1	important					1331:1339	important	1331:1339	important	1331:1339	After solubilization with Triton X-100, mutants showed little or no decrease in activity, unlike the wild-type enzyme, suggesting that the lysine at this position may be important for maintaining proper folding and for stabilizing the quaternary structure.
18404400	7	16	dep	important	1331:1339	arg1	stabilizing					1380:1390	stabilizing	1380:1390	stabilizing the quaternary structure	1380:1415	After solubilization with Triton X-100, mutants showed little or no decrease in activity, unlike the wild-type enzyme, suggesting that the lysine at this position may be important for maintaining proper folding and for stabilizing the quaternary structure.
18404400	7	16	dep	important	1331:1339	arg1	maintaining					1345:1355	maintaining	1345:1355	maintaining proper folding	1345:1370	After solubilization with Triton X-100, mutants showed little or no decrease in activity, unlike the wild-type enzyme, suggesting that the lysine at this position may be important for maintaining proper folding and for stabilizing the quaternary structure.
18404400	7	16	dep	important	1331:1339	arg1	lysine					1300:1305	the lysine	1296:1305	the lysine at this position	1296:1322	After solubilization with Triton X-100, mutants showed little or no decrease in activity, unlike the wild-type enzyme, suggesting that the lysine at this position may be important for maintaining proper folding and for stabilizing the quaternary structure.
18404400	8	17	theme	native	1584:1589	arg1	analysis					1611:1618	native gel electrophoretic analysis	1584:1618	native gel electrophoretic analysis	1584:1618	However, mutation at this site did not result in global changes in tertiary or quaternary structure as measured by Cibacron blue binding, chemical cross linking, and native gel electrophoretic analysis, leaving open the possibility of other mechanisms by which mutation of this conserved lysine residue might decrease enzyme activity.
18404400	6	18	theme	basic	1001:1005	arg1	acid					1013:1016	A basic amino acid	999:1016	A basic amino acid at this position	999:1033	A basic amino acid at this position was found to be important for the increase of nucleotidase activity observed after treatment with the lectin, concanavalin A.
18404400	6	18	theme	basic	1001:1005	arg1	important					1051:1059	important	1051:1059	important	1051:1059	A basic amino acid at this position was found to be important for the increase of nucleotidase activity observed after treatment with the lectin, concanavalin A.
18404400	6	19	with	treatment	1118:1126	arg1	lectin					1137:1142	the lectin	1133:1142	the lectin	1133:1142	A basic amino acid at this position was found to be important for the increase of nucleotidase activity observed after treatment with the lectin, concanavalin A.
18404400	6	19	with	treatment	1118:1126	arg1	A					1158:1158	concanavalin A	1145:1158	concanavalin A	1145:1158	A basic amino acid at this position was found to be important for the increase of nucleotidase activity observed after treatment with the lectin, concanavalin A.
18404400	8	20	from	site	1444:1447	arg1	mutation					1427:1434	mutation	1427:1434	mutation at this site	1427:1447	However, mutation at this site did not result in global changes in tertiary or quaternary structure as measured by Cibacron blue binding, chemical cross linking, and native gel electrophoretic analysis, leaving open the possibility of other mechanisms by which mutation of this conserved lysine residue might decrease enzyme activity.
18404400	8	21	from	changes	1474:1480	arg1	structure					1508:1516	tertiary or quaternary structure	1485:1516	tertiary or quaternary structure	1485:1516	However, mutation at this site did not result in global changes in tertiary or quaternary structure as measured by Cibacron blue binding, chemical cross linking, and native gel electrophoretic analysis, leaving open the possibility of other mechanisms by which mutation of this conserved lysine residue might decrease enzyme activity.
18404400	4	22	from	located	678:684	arg1	region					776:781	a region	774:781	a region previously hypothesized to be important for NTPDase3 oligomeric structure	774:855	This conserved lysine is located between apyrase conserved region 1 (ACR1) and an invariant glycosylation site (N81), in a region previously hypothesized to be important for NTPDase3 oligomeric structure.
18404400	4	23	theme	conserved	702:710	arg1	ACR1					722:725	ACR1	722:725	ACR1	722:725	This conserved lysine is located between apyrase conserved region 1 (ACR1) and an invariant glycosylation site (N81), in a region previously hypothesized to be important for NTPDase3 oligomeric structure.
18404400	4	23	theme	conserved	702:710	arg1	region					712:717	apyrase conserved region 1	694:719	apyrase conserved region 1 (ACR1)	694:726	This conserved lysine is located between apyrase conserved region 1 (ACR1) and an invariant glycosylation site (N81), in a region previously hypothesized to be important for NTPDase3 oligomeric structure.
18404400	6	24	theme	amino	1007:1011	arg1	acid					1013:1016	A basic amino acid	999:1016	A basic amino acid at this position	999:1033	A basic amino acid at this position was found to be important for the increase of nucleotidase activity observed after treatment with the lectin, concanavalin A.
18404400	6	24	theme	amino	1007:1011	arg1	important					1051:1059	important	1051:1059	important	1051:1059	A basic amino acid at this position was found to be important for the increase of nucleotidase activity observed after treatment with the lectin, concanavalin A.
18404400	3	25	theme	known	460:464	arg1	NTPDases					488:495	all known cell surface membrane NTPDases	456:495	all known cell surface membrane NTPDases (NTPDase1, 2, 3, and 8)	456:519	The residue corresponding to lysine 79 in NTPDase3 is conserved in all known cell surface membrane NTPDases (NTPDase1, 2, 3, and 8), but not in the soluble, monomeric NTPDases (NTPDase5 and 6), or in the intracellular, two transmembrane NTPDases (NTPDase4 and 7).
18404400	3	26	from	lysine	418:423	arg1	NTPDase3					431:438	NTPDase3	431:438	NTPDase3	431:438	The residue corresponding to lysine 79 in NTPDase3 is conserved in all known cell surface membrane NTPDases (NTPDase1, 2, 3, and 8), but not in the soluble, monomeric NTPDases (NTPDase5 and 6), or in the intracellular, two transmembrane NTPDases (NTPDase4 and 7).
18404400	2	27	theme	ecto-nucleoside	327:341	arg1	diphosphohydrolase					356:373	human ecto-nucleoside triphosphate diphosphohydrolase 3	321:375	human ecto-nucleoside triphosphate diphosphohydrolase 3 (NTPDase3)	321:386	In this study, we mutated lysine 79 in human ecto-nucleoside triphosphate diphosphohydrolase 3 (NTPDase3).
18404400	2	27	theme	ecto-nucleoside	327:341	arg1	NTPDase3					378:385	NTPDase3	378:385	NTPDase3	378:385	In this study, we mutated lysine 79 in human ecto-nucleoside triphosphate diphosphohydrolase 3 (NTPDase3).
18404400	7	28	theme	Triton	1187:1192	arg1	X-100					1194:1198	Triton X-100	1187:1198	Triton X-100	1187:1198	After solubilization with Triton X-100, mutants showed little or no decrease in activity, unlike the wild-type enzyme, suggesting that the lysine at this position may be important for maintaining proper folding and for stabilizing the quaternary structure.
18404400	3	29	dep	NTPDases	556:563	arg1	6					579:579	6	579:579	6	579:579	The residue corresponding to lysine 79 in NTPDase3 is conserved in all known cell surface membrane NTPDases (NTPDase1, 2, 3, and 8), but not in the soluble, monomeric NTPDases (NTPDase5 and 6), or in the intracellular, two transmembrane NTPDases (NTPDase4 and 7).
18404400	3	29	dep	NTPDases	556:563	arg1	NTPDase5					566:573	NTPDase5	566:573	NTPDase5	566:573	The residue corresponding to lysine 79 in NTPDase3 is conserved in all known cell surface membrane NTPDases (NTPDase1, 2, 3, and 8), but not in the soluble, monomeric NTPDases (NTPDase5 and 6), or in the intracellular, two transmembrane NTPDases (NTPDase4 and 7).
18404400	0	30	theme	Conserved	0:8	arg1	lysine					10:15	Conserved lysine 79	0:18	Conserved lysine 79	0:18	Conserved lysine 79 is important for activity of ecto-nucleoside triphosphate diphosphohydrolase 3 (NTPDase3).
18404400	3	31	dep	NTPDases	626:633	arg1	NTPDase4					636:643	NTPDase4	636:643	NTPDase4	636:643	The residue corresponding to lysine 79 in NTPDase3 is conserved in all known cell surface membrane NTPDases (NTPDase1, 2, 3, and 8), but not in the soluble, monomeric NTPDases (NTPDase5 and 6), or in the intracellular, two transmembrane NTPDases (NTPDase4 and 7).
18404400	3	31	dep	NTPDases	626:633	arg1	7					649:649	7	649:649	7	649:649	The residue corresponding to lysine 79 in NTPDase3 is conserved in all known cell surface membrane NTPDases (NTPDase1, 2, 3, and 8), but not in the soluble, monomeric NTPDases (NTPDase5 and 6), or in the intracellular, two transmembrane NTPDases (NTPDase4 and 7).
18404400	2	32	theme	human	321:325	arg1	diphosphohydrolase					356:373	human ecto-nucleoside triphosphate diphosphohydrolase 3	321:375	human ecto-nucleoside triphosphate diphosphohydrolase 3 (NTPDase3)	321:386	In this study, we mutated lysine 79 in human ecto-nucleoside triphosphate diphosphohydrolase 3 (NTPDase3).
18404400	2	32	theme	human	321:325	arg1	NTPDase3					378:385	NTPDase3	378:385	NTPDase3	378:385	In this study, we mutated lysine 79 in human ecto-nucleoside triphosphate diphosphohydrolase 3 (NTPDase3).
18404400	4	33	theme	conserved	658:666	arg1	lysine					668:673	This conserved lysine	653:673	This conserved lysine	653:673	This conserved lysine is located between apyrase conserved region 1 (ACR1) and an invariant glycosylation site (N81), in a region previously hypothesized to be important for NTPDase3 oligomeric structure.
18404400	8	34	theme	enzyme	1736:1741	arg1	activity					1743:1750	enzyme activity	1736:1750	enzyme activity	1736:1750	However, mutation at this site did not result in global changes in tertiary or quaternary structure as measured by Cibacron blue binding, chemical cross linking, and native gel electrophoretic analysis, leaving open the possibility of other mechanisms by which mutation of this conserved lysine residue might decrease enzyme activity.
18404400	3	35	theme	membrane	479:486	arg1	NTPDases					488:495	all known cell surface membrane NTPDases	456:495	all known cell surface membrane NTPDases (NTPDase1, 2, 3, and 8)	456:519	The residue corresponding to lysine 79 in NTPDase3 is conserved in all known cell surface membrane NTPDases (NTPDase1, 2, 3, and 8), but not in the soluble, monomeric NTPDases (NTPDase5 and 6), or in the intracellular, two transmembrane NTPDases (NTPDase4 and 7).
18404400	3	36	theme	soluble	537:543	arg1	NTPDases					556:563	the soluble, monomeric NTPDases	533:563	the soluble, monomeric NTPDases (NTPDase5 and 6)	533:580	The residue corresponding to lysine 79 in NTPDase3 is conserved in all known cell surface membrane NTPDases (NTPDase1, 2, 3, and 8), but not in the soluble, monomeric NTPDases (NTPDase5 and 6), or in the intracellular, two transmembrane NTPDases (NTPDase4 and 7).
18404400	6	37	theme	activity	1094:1101	arg1	increase					1069:1076	the increase	1065:1076	the increase of nucleotidase activity observed after treatment with the lectin, concanavalin A	1065:1158	A basic amino acid at this position was found to be important for the increase of nucleotidase activity observed after treatment with the lectin, concanavalin A.
18404400	5	38	theme	lysine	863:868	arg1	residue					870:876	This lysine residue	858:876	This lysine residue	858:876	This lysine residue was mutated to several different amino acids, and all mutants displayed substantially decreased nucleotidase activities.
18404400	1	39	theme	quaternary	223:232	arg1	structure					234:242	native quaternary structure	216:242	native quaternary structure required for maximal enzyme activity	216:279	Cell membrane-bound ecto-nucleoside triphosphate diphosphohydrolases (NTPDases) are homooligomeric, with native quaternary structure required for maximal enzyme activity.
18404400	7	40	theme	quaternary	1396:1405	arg1	structure					1407:1415	the quaternary structure	1392:1415	the quaternary structure	1392:1415	After solubilization with Triton X-100, mutants showed little or no decrease in activity, unlike the wild-type enzyme, suggesting that the lysine at this position may be important for maintaining proper folding and for stabilizing the quaternary structure.
18404400	4	41	theme	oligomeric	836:845	arg1	structure					847:855	NTPDase3 oligomeric structure	827:855	NTPDase3 oligomeric structure	827:855	This conserved lysine is located between apyrase conserved region 1 (ACR1) and an invariant glycosylation site (N81), in a region previously hypothesized to be important for NTPDase3 oligomeric structure.
18404400	6	42	theme	concanavalin	1145:1156	arg1	lectin					1137:1142	the lectin	1133:1142	the lectin	1133:1142	A basic amino acid at this position was found to be important for the increase of nucleotidase activity observed after treatment with the lectin, concanavalin A.
18404400	6	42	theme	concanavalin	1145:1156	arg1	A					1158:1158	concanavalin A	1145:1158	concanavalin A	1145:1158	A basic amino acid at this position was found to be important for the increase of nucleotidase activity observed after treatment with the lectin, concanavalin A.
18404400	8	43	theme	linking	1571:1577	arg1	cross					1565:1569	chemical cross linking	1556:1577	chemical cross linking	1556:1577	However, mutation at this site did not result in global changes in tertiary or quaternary structure as measured by Cibacron blue binding, chemical cross linking, and native gel electrophoretic analysis, leaving open the possibility of other mechanisms by which mutation of this conserved lysine residue might decrease enzyme activity.
18404400	3	44	theme	cell	466:469	arg1	NTPDases					488:495	all known cell surface membrane NTPDases	456:495	all known cell surface membrane NTPDases (NTPDase1, 2, 3, and 8)	456:519	The residue corresponding to lysine 79 in NTPDase3 is conserved in all known cell surface membrane NTPDases (NTPDase1, 2, 3, and 8), but not in the soluble, monomeric NTPDases (NTPDase5 and 6), or in the intracellular, two transmembrane NTPDases (NTPDase4 and 7).
18404400	8	45	theme	global	1467:1472	arg1	changes					1474:1480	global changes	1467:1480	global changes in tertiary or quaternary structure	1467:1516	However, mutation at this site did not result in global changes in tertiary or quaternary structure as measured by Cibacron blue binding, chemical cross linking, and native gel electrophoretic analysis, leaving open the possibility of other mechanisms by which mutation of this conserved lysine residue might decrease enzyme activity.
18404400	4	46	theme	NTPDase3	827:834	arg1	structure					847:855	NTPDase3 oligomeric structure	827:855	NTPDase3 oligomeric structure	827:855	This conserved lysine is located between apyrase conserved region 1 (ACR1) and an invariant glycosylation site (N81), in a region previously hypothesized to be important for NTPDase3 oligomeric structure.
18404400	3	47	theme	surface	471:477	arg1	NTPDases					488:495	all known cell surface membrane NTPDases	456:495	all known cell surface membrane NTPDases (NTPDase1, 2, 3, and 8)	456:519	The residue corresponding to lysine 79 in NTPDase3 is conserved in all known cell surface membrane NTPDases (NTPDase1, 2, 3, and 8), but not in the soluble, monomeric NTPDases (NTPDase5 and 6), or in the intracellular, two transmembrane NTPDases (NTPDase4 and 7).
18404400	8	48	theme	open	1629:1632	arg1	possibility					1638:1648	open the possibility	1629:1648	open the possibility of other mechanisms by which mutation of this conserved lysine residue might decrease enzyme activity	1629:1750	However, mutation at this site did not result in global changes in tertiary or quaternary structure as measured by Cibacron blue binding, chemical cross linking, and native gel electrophoretic analysis, leaving open the possibility of other mechanisms by which mutation of this conserved lysine residue might decrease enzyme activity.
18404400	4	49	theme	glycosylation	745:757	arg1	N81					765:767	N81	765:767	N81	765:767	This conserved lysine is located between apyrase conserved region 1 (ACR1) and an invariant glycosylation site (N81), in a region previously hypothesized to be important for NTPDase3 oligomeric structure.
18404400	4	49	theme	glycosylation	745:757	arg1	site					759:762	an invariant glycosylation site	732:762	an invariant glycosylation site (N81)	732:768	This conserved lysine is located between apyrase conserved region 1 (ACR1) and an invariant glycosylation site (N81), in a region previously hypothesized to be important for NTPDase3 oligomeric structure.
18404400	6	50	from	position	1026:1033	arg1	acid					1013:1016	A basic amino acid	999:1016	A basic amino acid at this position	999:1033	A basic amino acid at this position was found to be important for the increase of nucleotidase activity observed after treatment with the lectin, concanavalin A.
18404400	6	50	from	position	1026:1033	arg1	important					1051:1059	important	1051:1059	important	1051:1059	A basic amino acid at this position was found to be important for the increase of nucleotidase activity observed after treatment with the lectin, concanavalin A.
18404400	1	51	theme	Cell	111:114	arg1	NTPDases					181:188	NTPDases	181:188	NTPDases	181:188	Cell membrane-bound ecto-nucleoside triphosphate diphosphohydrolases (NTPDases) are homooligomeric, with native quaternary structure required for maximal enzyme activity.
18404400	1	51	theme	Cell	111:114	arg1	diphosphohydrolases					160:178	Cell membrane-bound ecto-nucleoside triphosphate diphosphohydrolases	111:178	Cell membrane-bound ecto-nucleoside triphosphate diphosphohydrolases (NTPDases)	111:189	Cell membrane-bound ecto-nucleoside triphosphate diphosphohydrolases (NTPDases) are homooligomeric, with native quaternary structure required for maximal enzyme activity.
18404400	7	52	from	decrease	1229:1236	arg1	activity					1241:1248	activity	1241:1248	activity	1241:1248	After solubilization with Triton X-100, mutants showed little or no decrease in activity, unlike the wild-type enzyme, suggesting that the lysine at this position may be important for maintaining proper folding and for stabilizing the quaternary structure.
18404400	4	53	gly	glycosylation	745:757	arg2	site					759:762	an invariant glycosylation site	732:762	an invariant glycosylation site (N81)	732:768	This conserved lysine is located between apyrase conserved region 1 (ACR1) and an invariant glycosylation site (N81), in a region previously hypothesized to be important for NTPDase3 oligomeric structure.
18404400	4	53	gly	glycosylation	745:757	arg2	N81					765:767	N81	765:767	N81	765:767	This conserved lysine is located between apyrase conserved region 1 (ACR1) and an invariant glycosylation site (N81), in a region previously hypothesized to be important for NTPDase3 oligomeric structure.
18404400	4	54	theme	invariant	735:743	arg1	N81					765:767	N81	765:767	N81	765:767	This conserved lysine is located between apyrase conserved region 1 (ACR1) and an invariant glycosylation site (N81), in a region previously hypothesized to be important for NTPDase3 oligomeric structure.
18404400	4	54	theme	invariant	735:743	arg1	site					759:762	an invariant glycosylation site	732:762	an invariant glycosylation site (N81)	732:768	This conserved lysine is located between apyrase conserved region 1 (ACR1) and an invariant glycosylation site (N81), in a region previously hypothesized to be important for NTPDase3 oligomeric structure.
18404400	8	55	theme	mechanisms	1659:1668	arg1	possibility					1638:1648	open the possibility	1629:1648	open the possibility of other mechanisms by which mutation of this conserved lysine residue might decrease enzyme activity	1629:1750	However, mutation at this site did not result in global changes in tertiary or quaternary structure as measured by Cibacron blue binding, chemical cross linking, and native gel electrophoretic analysis, leaving open the possibility of other mechanisms by which mutation of this conserved lysine residue might decrease enzyme activity.
18404400	1	56	theme	membrane-bound	116:129	arg1	NTPDases					181:188	NTPDases	181:188	NTPDases	181:188	Cell membrane-bound ecto-nucleoside triphosphate diphosphohydrolases (NTPDases) are homooligomeric, with native quaternary structure required for maximal enzyme activity.
18404400	1	56	theme	membrane-bound	116:129	arg1	diphosphohydrolases					160:178	Cell membrane-bound ecto-nucleoside triphosphate diphosphohydrolases	111:178	Cell membrane-bound ecto-nucleoside triphosphate diphosphohydrolases (NTPDases)	111:189	Cell membrane-bound ecto-nucleoside triphosphate diphosphohydrolases (NTPDases) are homooligomeric, with native quaternary structure required for maximal enzyme activity.
18404400	4	57	located	located	678:684	arg2	lysine					668:673	This conserved lysine	653:673	This conserved lysine	653:673	This conserved lysine is located between apyrase conserved region 1 (ACR1) and an invariant glycosylation site (N81), in a region previously hypothesized to be important for NTPDase3 oligomeric structure.
18404400	4	57	located	located	678:684	arg1	region					776:781	a region	774:781	a region previously hypothesized to be important for NTPDase3 oligomeric structure	774:855	This conserved lysine is located between apyrase conserved region 1 (ACR1) and an invariant glycosylation site (N81), in a region previously hypothesized to be important for NTPDase3 oligomeric structure.
18404400	3	58	theme	transmembrane	612:624	arg1	NTPDases					626:633	the intracellular, two transmembrane NTPDases	589:633	NTPDases	626:633	The residue corresponding to lysine 79 in NTPDase3 is conserved in all known cell surface membrane NTPDases (NTPDase1, 2, 3, and 8), but not in the soluble, monomeric NTPDases (NTPDase5 and 6), or in the intracellular, two transmembrane NTPDases (NTPDase4 and 7).
18404400	5	59	theme	several	893:899	arg1	acids					917:921	several different amino acids	893:921	several different amino acids	893:921	This lysine residue was mutated to several different amino acids, and all mutants displayed substantially decreased nucleotidase activities.
18404400	8	60	theme	other	1653:1657	arg1	mechanisms					1659:1668	other mechanisms	1653:1668	other mechanisms by which mutation of this conserved lysine residue might decrease enzyme activity	1653:1750	However, mutation at this site did not result in global changes in tertiary or quaternary structure as measured by Cibacron blue binding, chemical cross linking, and native gel electrophoretic analysis, leaving open the possibility of other mechanisms by which mutation of this conserved lysine residue might decrease enzyme activity.
18404400	1	61	theme	ecto-nucleoside	131:145	arg1	NTPDases					181:188	NTPDases	181:188	NTPDases	181:188	Cell membrane-bound ecto-nucleoside triphosphate diphosphohydrolases (NTPDases) are homooligomeric, with native quaternary structure required for maximal enzyme activity.
18404400	1	61	theme	ecto-nucleoside	131:145	arg1	diphosphohydrolases					160:178	Cell membrane-bound ecto-nucleoside triphosphate diphosphohydrolases	111:178	Cell membrane-bound ecto-nucleoside triphosphate diphosphohydrolases (NTPDases)	111:189	Cell membrane-bound ecto-nucleoside triphosphate diphosphohydrolases (NTPDases) are homooligomeric, with native quaternary structure required for maximal enzyme activity.
18404400	8	62	theme	blue	1542:1545	arg1	binding					1547:1553	Cibacron blue binding	1533:1553	Cibacron blue binding	1533:1553	However, mutation at this site did not result in global changes in tertiary or quaternary structure as measured by Cibacron blue binding, chemical cross linking, and native gel electrophoretic analysis, leaving open the possibility of other mechanisms by which mutation of this conserved lysine residue might decrease enzyme activity.
18404400	1	63	with	homooligomeric	195:208	arg1	structure					234:242	native quaternary structure	216:242	native quaternary structure required for maximal enzyme activity	216:279	Cell membrane-bound ecto-nucleoside triphosphate diphosphohydrolases (NTPDases) are homooligomeric, with native quaternary structure required for maximal enzyme activity.
18404400	3	64	theme	intracellular	593:605	arg1	NTPDases					626:633	the intracellular, two transmembrane NTPDases	589:633	NTPDases	626:633	The residue corresponding to lysine 79 in NTPDase3 is conserved in all known cell surface membrane NTPDases (NTPDase1, 2, 3, and 8), but not in the soluble, monomeric NTPDases (NTPDase5 and 6), or in the intracellular, two transmembrane NTPDases (NTPDase4 and 7).
18404400	5	65	theme	different	901:909	arg1	acids					917:921	several different amino acids	893:921	several different amino acids	893:921	This lysine residue was mutated to several different amino acids, and all mutants displayed substantially decreased nucleotidase activities.
18404400	1	66	theme	triphosphate	147:158	arg1	NTPDases					181:188	NTPDases	181:188	NTPDases	181:188	Cell membrane-bound ecto-nucleoside triphosphate diphosphohydrolases (NTPDases) are homooligomeric, with native quaternary structure required for maximal enzyme activity.
18404400	1	66	theme	triphosphate	147:158	arg1	diphosphohydrolases					160:178	Cell membrane-bound ecto-nucleoside triphosphate diphosphohydrolases	111:178	Cell membrane-bound ecto-nucleoside triphosphate diphosphohydrolases (NTPDases)	111:189	Cell membrane-bound ecto-nucleoside triphosphate diphosphohydrolases (NTPDases) are homooligomeric, with native quaternary structure required for maximal enzyme activity.
18404400	8	67	theme	chemical	1556:1563	arg1	cross					1565:1569	chemical cross linking	1556:1577	chemical cross linking	1556:1577	However, mutation at this site did not result in global changes in tertiary or quaternary structure as measured by Cibacron blue binding, chemical cross linking, and native gel electrophoretic analysis, leaving open the possibility of other mechanisms by which mutation of this conserved lysine residue might decrease enzyme activity.
18404400	1	68	theme	maximal	257:263	arg1	activity					272:279	maximal enzyme activity	257:279	maximal enzyme activity	257:279	Cell membrane-bound ecto-nucleoside triphosphate diphosphohydrolases (NTPDases) are homooligomeric, with native quaternary structure required for maximal enzyme activity.
18404400	0	69	theme	triphosphate	65:76	arg1	diphosphohydrolase					78:95	ecto-nucleoside triphosphate diphosphohydrolase 3	49:97	ecto-nucleoside triphosphate diphosphohydrolase 3 (NTPDase3)	49:108	Conserved lysine 79 is important for activity of ecto-nucleoside triphosphate diphosphohydrolase 3 (NTPDase3).
18404400	0	69	theme	triphosphate	65:76	arg1	NTPDase3					100:107	NTPDase3	100:107	NTPDase3	100:107	Conserved lysine 79 is important for activity of ecto-nucleoside triphosphate diphosphohydrolase 3 (NTPDase3).
18404400	5	70	theme	nucleotidase	974:985	arg1	activities					987:996	decreased nucleotidase activities	964:996	decreased nucleotidase activities	964:996	This lysine residue was mutated to several different amino acids, and all mutants displayed substantially decreased nucleotidase activities.
18404400	5	71	theme	amino	911:915	arg1	acids					917:921	several different amino acids	893:921	several different amino acids	893:921	This lysine residue was mutated to several different amino acids, and all mutants displayed substantially decreased nucleotidase activities.
18404400	1	72	theme	native	216:221	arg1	structure					234:242	native quaternary structure	216:242	native quaternary structure required for maximal enzyme activity	216:279	Cell membrane-bound ecto-nucleoside triphosphate diphosphohydrolases (NTPDases) are homooligomeric, with native quaternary structure required for maximal enzyme activity.
18404400	1	73	theme	enzyme	265:270	arg1	activity					272:279	maximal enzyme activity	257:279	maximal enzyme activity	257:279	Cell membrane-bound ecto-nucleoside triphosphate diphosphohydrolases (NTPDases) are homooligomeric, with native quaternary structure required for maximal enzyme activity.
18404400	0	74	theme	ecto-nucleoside	49:63	arg1	diphosphohydrolase					78:95	ecto-nucleoside triphosphate diphosphohydrolase 3	49:97	ecto-nucleoside triphosphate diphosphohydrolase 3 (NTPDase3)	49:108	Conserved lysine 79 is important for activity of ecto-nucleoside triphosphate diphosphohydrolase 3 (NTPDase3).
18404400	0	74	theme	ecto-nucleoside	49:63	arg1	NTPDase3					100:107	NTPDase3	100:107	NTPDase3	100:107	Conserved lysine 79 is important for activity of ecto-nucleoside triphosphate diphosphohydrolase 3 (NTPDase3).
18404400	4	75	from	region	776:781	arg1	located					678:684	located	678:684	located	678:684	This conserved lysine is located between apyrase conserved region 1 (ACR1) and an invariant glycosylation site (N81), in a region previously hypothesized to be important for NTPDase3 oligomeric structure.
18404400	3	76	dep	NTPDases	488:495	arg1	NTPDase1					498:505	NTPDase1	498:505	NTPDase1	498:505	The residue corresponding to lysine 79 in NTPDase3 is conserved in all known cell surface membrane NTPDases (NTPDase1, 2, 3, and 8), but not in the soluble, monomeric NTPDases (NTPDase5 and 6), or in the intracellular, two transmembrane NTPDases (NTPDase4 and 7).
18404400	7	77	from	position	1315:1322	arg1	important					1331:1339	important	1331:1339	important	1331:1339	After solubilization with Triton X-100, mutants showed little or no decrease in activity, unlike the wild-type enzyme, suggesting that the lysine at this position may be important for maintaining proper folding and for stabilizing the quaternary structure.
18404400	7	77	from	position	1315:1322	arg1	stabilizing					1380:1390	stabilizing	1380:1390	stabilizing the quaternary structure	1380:1415	After solubilization with Triton X-100, mutants showed little or no decrease in activity, unlike the wild-type enzyme, suggesting that the lysine at this position may be important for maintaining proper folding and for stabilizing the quaternary structure.
18404400	7	77	from	position	1315:1322	arg1	lysine					1300:1305	the lysine	1296:1305	the lysine at this position	1296:1322	After solubilization with Triton X-100, mutants showed little or no decrease in activity, unlike the wild-type enzyme, suggesting that the lysine at this position may be important for maintaining proper folding and for stabilizing the quaternary structure.
18404400	7	77	from	position	1315:1322	arg1	maintaining					1345:1355	maintaining	1345:1355	maintaining proper folding	1345:1370	After solubilization with Triton X-100, mutants showed little or no decrease in activity, unlike the wild-type enzyme, suggesting that the lysine at this position may be important for maintaining proper folding and for stabilizing the quaternary structure.
18404400	8	78	theme	quaternary	1497:1506	arg1	structure					1508:1516	tertiary or quaternary structure	1485:1516	tertiary or quaternary structure	1485:1516	However, mutation at this site did not result in global changes in tertiary or quaternary structure as measured by Cibacron blue binding, chemical cross linking, and native gel electrophoretic analysis, leaving open the possibility of other mechanisms by which mutation of this conserved lysine residue might decrease enzyme activity.
11676606	6	0	dep	revealed	746:753	arg1	whereas					820:826	whereas	820:826	whereas	820:826	Detailed carbohydrate analysis revealed high-mannose structures on sCD154 purified from Pichia pastoris, whereas CD154 purified from Chinese hamster ovary E1A contained heterogeneous populations of complex carbohydrates.
11676606	7	1	from	CD69	1067:1070	arg1	cells					1105:1109	primary B cells	1095:1109	primary B cells	1095:1109	sCD154 purified from either system was trimeric, it bound to CD40 with similar affinities of 10-30 nM, and it functionally induced CD69 and CD95 expression on primary B cells.
11676606	4	2	theme	Human	505:509	arg1	CD154					511:515	Human CD154	505:515	Human CD154	505:515	Human CD154 contains a single N-linked glycosylation site at asparagine 240.
11676606	0	3	theme	ovary	176:180	arg1	cells					182:186	Chinese hamster ovary cells	160:186	Chinese hamster ovary cells	160:186	Determination of carbohydrate structures N-linked to soluble CD154 and characterization of the interactions of CD40 with CD154 expressed in Pichia pastoris and Chinese hamster ovary cells.
11676606	8	4	theme	varied	1166:1171	arg1	types					1173:1177	varied types	1166:1177	varied types of N-linked glycans	1166:1197	Together, these results indicate that the presence of varied types of N-linked glycans on asparagine 240 of CD154 does not play a significant role in the CD40-CD154 interactions.
11676606	2	5	theme	shallow	344:350	arg1	groove					352:357	a shallow groove	342:357	a shallow groove formed between two monomers of CD154	342:394	Previous studies have described the CD40 binding site as a shallow groove formed between two monomers of CD154.
11676606	2	5	theme	shallow	344:350	arg1	site					334:337	the CD40 binding site	317:337	the CD40 binding site	317:337	Previous studies have described the CD40 binding site as a shallow groove formed between two monomers of CD154.
11676606	4	6	link	N-linked	535:542	arg1	site					558:561	a single N-linked glycosylation site	526:561	a single N-linked glycosylation site at asparagine 240	526:579	Human CD154 contains a single N-linked glycosylation site at asparagine 240.
11676606	0	7	theme	interactions	95:106	arg1	characterization					71:86	characterization	71:86	characterization	71:86	Determination of carbohydrate structures N-linked to soluble CD154 and characterization of the interactions of CD40 with CD154 expressed in Pichia pastoris and Chinese hamster ovary cells.
11676606	0	7	theme	interactions	95:106	arg1	CD154					61:65	soluble CD154	53:65	soluble CD154	53:65	Determination of carbohydrate structures N-linked to soluble CD154 and characterization of the interactions of CD40 with CD154 expressed in Pichia pastoris and Chinese hamster ovary cells.
11676606	6	8	theme	carbohydrates	921:933	arg1	populations					898:908	heterogeneous populations	884:908	heterogeneous populations of complex carbohydrates	884:933	Detailed carbohydrate analysis revealed high-mannose structures on sCD154 purified from Pichia pastoris, whereas CD154 purified from Chinese hamster ovary E1A contained heterogeneous populations of complex carbohydrates.
11676606	4	9	gly	glycosylation	544:556	arg2	asparagine					566:575	asparagine 240	566:579	asparagine 240	566:579	Human CD154 contains a single N-linked glycosylation site at asparagine 240.
11676606	4	9	gly	glycosylation	544:556	arg2	site					558:561	a single N-linked glycosylation site	526:561	a single N-linked glycosylation site at asparagine 240	526:579	Human CD154 contains a single N-linked glycosylation site at asparagine 240.
11676606	8	10	link	N-linked	1182:1189	arg1	glycans					1191:1197	N-linked glycans	1182:1197	N-linked glycans	1182:1197	Together, these results indicate that the presence of varied types of N-linked glycans on asparagine 240 of CD154 does not play a significant role in the CD40-CD154 interactions.
11676606	2	11	theme	Previous	285:292	arg1	studies					294:300	Previous studies	285:300	Previous studies	285:300	Previous studies have described the CD40 binding site as a shallow groove formed between two monomers of CD154.
11676606	1	12	theme	protective	264:273	arg1	immunity					275:282	protective immunity	264:282	protective immunity	264:282	CD40-CD154 (CD40 ligand) interactions are essential for the development of protective immunity.
11676606	8	13	theme	types	1173:1177	arg1	presence					1154:1161	the presence	1150:1161	the presence of varied types of N-linked glycans on asparagine 240 of CD154	1150:1224	Together, these results indicate that the presence of varied types of N-linked glycans on asparagine 240 of CD154 does not play a significant role in the CD40-CD154 interactions.
11676606	6	14	theme	complex	913:919	arg1	carbohydrates					921:933	complex carbohydrates	913:933	complex carbohydrates	913:933	Detailed carbohydrate analysis revealed high-mannose structures on sCD154 purified from Pichia pastoris, whereas CD154 purified from Chinese hamster ovary E1A contained heterogeneous populations of complex carbohydrates.
11676606	7	15	theme	B	1103:1103	arg1	cells					1105:1109	primary B cells	1095:1109	primary B cells	1095:1109	sCD154 purified from either system was trimeric, it bound to CD40 with similar affinities of 10-30 nM, and it functionally induced CD69 and CD95 expression on primary B cells.
11676606	3	16	theme	biological	455:464	arg1	function					466:473	biological function	455:473	biological function	455:473	However, these studies have not examined the structure or biological function of the carbohydrate on CD154.
11676606	5	17	dep	soluble	638:644	arg1	s					647:647	s	647:647	s	647:647	We have characterized the interactions between CD40 and soluble (s) CD154 in which sCD154 contains different types of carbohydrates.
11676606	8	18	theme	glycans	1191:1197	arg1	types					1173:1177	varied types	1166:1177	varied types of N-linked glycans	1166:1197	Together, these results indicate that the presence of varied types of N-linked glycans on asparagine 240 of CD154 does not play a significant role in the CD40-CD154 interactions.
11676606	2	19	theme	CD154	390:394	arg1	CD154					390:394	CD154	390:394	CD154	390:394	Previous studies have described the CD40 binding site as a shallow groove formed between two monomers of CD154.
11676606	2	19	theme	CD154	390:394	arg1	monomers					378:385	two monomers	374:385	two monomers of CD154	374:394	Previous studies have described the CD40 binding site as a shallow groove formed between two monomers of CD154.
11676606	0	20	theme	CD40	111:114	arg1	interactions					95:106	the interactions	91:106	the interactions of CD40 with CD154	91:125	Determination of carbohydrate structures N-linked to soluble CD154 and characterization of the interactions of CD40 with CD154 expressed in Pichia pastoris and Chinese hamster ovary cells.
11676606	3	21	from	function	466:473	arg1	CD154					498:502	CD154	498:502	CD154	498:502	However, these studies have not examined the structure or biological function of the carbohydrate on CD154.
11676606	4	22	contain	contains	517:524	arg1	CD154					511:515	Human CD154	505:515	Human CD154	505:515	Human CD154 contains a single N-linked glycosylation site at asparagine 240.
11676606	4	22	contain	contains	517:524	arg2	site					558:561	a single N-linked glycosylation site	526:561	a single N-linked glycosylation site at asparagine 240	526:579	Human CD154 contains a single N-linked glycosylation site at asparagine 240.
11676606	7	23	from	expression	1081:1090	arg1	cells					1105:1109	primary B cells	1095:1109	primary B cells	1095:1109	sCD154 purified from either system was trimeric, it bound to CD40 with similar affinities of 10-30 nM, and it functionally induced CD69 and CD95 expression on primary B cells.
11676606	8	24	theme	N-linked	1182:1189	arg1	glycans					1191:1197	N-linked glycans	1182:1197	N-linked glycans	1182:1197	Together, these results indicate that the presence of varied types of N-linked glycans on asparagine 240 of CD154 does not play a significant role in the CD40-CD154 interactions.
11676606	4	25	theme	glycosylation	544:556	arg1	site					558:561	a single N-linked glycosylation site	526:561	a single N-linked glycosylation site at asparagine 240	526:579	Human CD154 contains a single N-linked glycosylation site at asparagine 240.
11676606	2	26	theme	CD40	321:324	arg1	groove					352:357	a shallow groove	342:357	a shallow groove formed between two monomers of CD154	342:394	Previous studies have described the CD40 binding site as a shallow groove formed between two monomers of CD154.
11676606	2	26	theme	CD40	321:324	arg1	site					334:337	the CD40 binding site	317:337	the CD40 binding site	317:337	Previous studies have described the CD40 binding site as a shallow groove formed between two monomers of CD154.
11676606	1	27	theme	immunity	275:282	arg1	development					249:259	the development	245:259	the development of protective immunity	245:282	CD40-CD154 (CD40 ligand) interactions are essential for the development of protective immunity.
11676606	5	28	theme	soluble	638:644	arg1	CD154					650:654	soluble (s) CD154	638:654	soluble (s) CD154 in which sCD154 contains different types of carbohydrates	638:712	We have characterized the interactions between CD40 and soluble (s) CD154 in which sCD154 contains different types of carbohydrates.
11676606	6	29	theme	Pichia	803:808	arg1	pastoris					810:817	Pichia pastoris	803:817	Pichia pastoris	803:817	Detailed carbohydrate analysis revealed high-mannose structures on sCD154 purified from Pichia pastoris, whereas CD154 purified from Chinese hamster ovary E1A contained heterogeneous populations of complex carbohydrates.
11676606	1	30	theme	CD40-CD154	189:198	arg1	interactions					214:225	CD40-CD154 (CD40 ligand) interactions	189:225	CD40-CD154 (CD40 ligand) interactions	189:225	CD40-CD154 (CD40 ligand) interactions are essential for the development of protective immunity.
11676606	1	30	theme	CD40-CD154	189:198	arg1	ligand					206:211	CD40 ligand	201:211	CD40 ligand	201:211	CD40-CD154 (CD40 ligand) interactions are essential for the development of protective immunity.
11676606	0	31	theme	structures	30:39	arg1	Determination					0:12	Determination	0:12	Determination of carbohydrate structures N-linked to soluble CD154 and characterization of the interactions of CD40 with CD154	0:125	Determination of carbohydrate structures N-linked to soluble CD154 and characterization of the interactions of CD40 with CD154 expressed in Pichia pastoris and Chinese hamster ovary cells.
11676606	4	32	theme	N-linked	535:542	arg1	site					558:561	a single N-linked glycosylation site	526:561	a single N-linked glycosylation site at asparagine 240	526:579	Human CD154 contains a single N-linked glycosylation site at asparagine 240.
11676606	5	33	theme	different	681:689	arg1	types					691:695	different types	681:695	different types of carbohydrates	681:712	We have characterized the interactions between CD40 and soluble (s) CD154 in which sCD154 contains different types of carbohydrates.
11676606	0	34	with	interactions	95:106	arg1	CD154					121:125	CD154	121:125	CD154	121:125	Determination of carbohydrate structures N-linked to soluble CD154 and characterization of the interactions of CD40 with CD154 expressed in Pichia pastoris and Chinese hamster ovary cells.
11676606	0	35	theme	carbohydrate	17:28	arg1	structures					30:39	carbohydrate structures	17:39	carbohydrate structures N-linked to soluble CD154 and characterization of the interactions of CD40 with CD154	17:125	Determination of carbohydrate structures N-linked to soluble CD154 and characterization of the interactions of CD40 with CD154 expressed in Pichia pastoris and Chinese hamster ovary cells.
11676606	6	36	theme	heterogeneous	884:896	arg1	populations					898:908	heterogeneous populations	884:908	heterogeneous populations of complex carbohydrates	884:933	Detailed carbohydrate analysis revealed high-mannose structures on sCD154 purified from Pichia pastoris, whereas CD154 purified from Chinese hamster ovary E1A contained heterogeneous populations of complex carbohydrates.
11676606	1	37	theme	CD40	201:204	arg1	interactions					214:225	CD40-CD154 (CD40 ligand) interactions	189:225	CD40-CD154 (CD40 ligand) interactions	189:225	CD40-CD154 (CD40 ligand) interactions are essential for the development of protective immunity.
11676606	1	37	theme	CD40	201:204	arg1	ligand					206:211	CD40 ligand	201:211	CD40 ligand	201:211	CD40-CD154 (CD40 ligand) interactions are essential for the development of protective immunity.
11676606	8	38	theme	CD40-CD154	1266:1275	arg1	interactions					1277:1288	the CD40-CD154 interactions	1262:1288	the CD40-CD154 interactions	1262:1288	Together, these results indicate that the presence of varied types of N-linked glycans on asparagine 240 of CD154 does not play a significant role in the CD40-CD154 interactions.
11676606	0	39	theme	Pichia	140:145	arg1	pastoris					147:154	Pichia pastoris	140:154	Pichia pastoris	140:154	Determination of carbohydrate structures N-linked to soluble CD154 and characterization of the interactions of CD40 with CD154 expressed in Pichia pastoris and Chinese hamster ovary cells.
11676606	8	40	theme	significant	1242:1252	arg1	role					1254:1257	a significant role	1240:1257	a significant role	1240:1257	Together, these results indicate that the presence of varied types of N-linked glycans on asparagine 240 of CD154 does not play a significant role in the CD40-CD154 interactions.
11676606	0	41	theme	N-linked	41:48	arg1	structures					30:39	carbohydrate structures	17:39	carbohydrate structures N-linked to soluble CD154 and characterization of the interactions of CD40 with CD154	17:125	Determination of carbohydrate structures N-linked to soluble CD154 and characterization of the interactions of CD40 with CD154 expressed in Pichia pastoris and Chinese hamster ovary cells.
11676606	5	42	contain	contains	672:679	arg1	sCD154					665:670	sCD154	665:670	sCD154	665:670	We have characterized the interactions between CD40 and soluble (s) CD154 in which sCD154 contains different types of carbohydrates.
11676606	5	42	contain	contains	672:679	arg2	types					691:695	different types	681:695	different types of carbohydrates	681:712	We have characterized the interactions between CD40 and soluble (s) CD154 in which sCD154 contains different types of carbohydrates.
11676606	5	42	contain	contains	672:679	arg2	sCD154					665:670	sCD154	665:670	sCD154	665:670	We have characterized the interactions between CD40 and soluble (s) CD154 in which sCD154 contains different types of carbohydrates.
11676606	5	42	contain	contains	672:679	arg1	CD154					650:654	soluble (s) CD154	638:654	soluble (s) CD154 in which sCD154 contains different types of carbohydrates	638:712	We have characterized the interactions between CD40 and soluble (s) CD154 in which sCD154 contains different types of carbohydrates.
11676606	5	43	theme	carbohydrates	700:712	arg1	types					691:695	different types	681:695	different types of carbohydrates	681:712	We have characterized the interactions between CD40 and soluble (s) CD154 in which sCD154 contains different types of carbohydrates.
11676606	7	44	theme	nM	1035:1036	arg1	affinities					1015:1024	similar affinities	1007:1024	similar affinities of 10-30 nM	1007:1036	sCD154 purified from either system was trimeric, it bound to CD40 with similar affinities of 10-30 nM, and it functionally induced CD69 and CD95 expression on primary B cells.
11676606	4	45	from	asparagine	566:575	arg1	site					558:561	a single N-linked glycosylation site	526:561	a single N-linked glycosylation site at asparagine 240	526:579	Human CD154 contains a single N-linked glycosylation site at asparagine 240.
11676606	8	46	theme	CD154	1220:1224	arg1	240					1213:1215	asparagine 240	1202:1215	asparagine 240 of CD154	1202:1224	Together, these results indicate that the presence of varied types of N-linked glycans on asparagine 240 of CD154 does not play a significant role in the CD40-CD154 interactions.
11676606	8	47	theme	asparagine	1202:1211	arg1	240					1213:1215	asparagine 240	1202:1215	asparagine 240 of CD154	1202:1224	Together, these results indicate that the presence of varied types of N-linked glycans on asparagine 240 of CD154 does not play a significant role in the CD40-CD154 interactions.
11676606	6	48	theme	ovary	864:868	arg1	E1A					870:872	Chinese hamster ovary E1A	848:872	Chinese hamster ovary E1A	848:872	Detailed carbohydrate analysis revealed high-mannose structures on sCD154 purified from Pichia pastoris, whereas CD154 purified from Chinese hamster ovary E1A contained heterogeneous populations of complex carbohydrates.
11676606	3	49	from	structure	442:450	arg1	CD154					498:502	CD154	498:502	CD154	498:502	However, these studies have not examined the structure or biological function of the carbohydrate on CD154.
11676606	0	50	theme	soluble	53:59	arg1	CD154					61:65	soluble CD154	53:65	soluble CD154	53:65	Determination of carbohydrate structures N-linked to soluble CD154 and characterization of the interactions of CD40 with CD154 expressed in Pichia pastoris and Chinese hamster ovary cells.
11676606	4	51	theme	single	528:533	arg1	site					558:561	a single N-linked glycosylation site	526:561	a single N-linked glycosylation site at asparagine 240	526:579	Human CD154 contains a single N-linked glycosylation site at asparagine 240.
11676606	7	52	theme	CD95	1076:1079	arg1	expression					1081:1090	CD95 expression	1076:1090	CD95 expression	1076:1090	sCD154 purified from either system was trimeric, it bound to CD40 with similar affinities of 10-30 nM, and it functionally induced CD69 and CD95 expression on primary B cells.
11676606	6	53	theme	hamster	856:862	arg1	ovary					864:868	Chinese hamster ovary	848:868	Chinese hamster ovary E1A	848:872	Detailed carbohydrate analysis revealed high-mannose structures on sCD154 purified from Pichia pastoris, whereas CD154 purified from Chinese hamster ovary E1A contained heterogeneous populations of complex carbohydrates.
11676606	6	54	theme	high-mannose	755:766	arg1	structures					768:777	high-mannose structures	755:777	high-mannose structures on sCD154 purified from Pichia pastoris	755:817	Detailed carbohydrate analysis revealed high-mannose structures on sCD154 purified from Pichia pastoris, whereas CD154 purified from Chinese hamster ovary E1A contained heterogeneous populations of complex carbohydrates.
11676606	3	55	theme	carbohydrate	482:493	arg1	structure					442:450	structure	442:450	structure	442:450	However, these studies have not examined the structure or biological function of the carbohydrate on CD154.
11676606	3	55	theme	carbohydrate	482:493	arg1	function					466:473	biological function	455:473	biological function	455:473	However, these studies have not examined the structure or biological function of the carbohydrate on CD154.
11676606	0	56	link	N-linked	41:48	arg1	structures					30:39	carbohydrate structures	17:39	carbohydrate structures N-linked to soluble CD154 and characterization of the interactions of CD40 with CD154	17:125	Determination of carbohydrate structures N-linked to soluble CD154 and characterization of the interactions of CD40 with CD154 expressed in Pichia pastoris and Chinese hamster ovary cells.
11676606	0	57	theme	hamster	168:174	arg1	cells					182:186	Chinese hamster ovary cells	160:186	Chinese hamster ovary cells	160:186	Determination of carbohydrate structures N-linked to soluble CD154 and characterization of the interactions of CD40 with CD154 expressed in Pichia pastoris and Chinese hamster ovary cells.
11676606	6	58	theme	Chinese	848:854	arg1	ovary					864:868	Chinese hamster ovary	848:868	Chinese hamster ovary E1A	848:872	Detailed carbohydrate analysis revealed high-mannose structures on sCD154 purified from Pichia pastoris, whereas CD154 purified from Chinese hamster ovary E1A contained heterogeneous populations of complex carbohydrates.
11676606	6	59	contain	contained	874:882	arg2	populations					898:908	heterogeneous populations	884:908	heterogeneous populations of complex carbohydrates	884:933	Detailed carbohydrate analysis revealed high-mannose structures on sCD154 purified from Pichia pastoris, whereas CD154 purified from Chinese hamster ovary E1A contained heterogeneous populations of complex carbohydrates.
11676606	6	59	contain	contained	874:882	arg1	CD154					828:832	CD154	828:832	CD154 purified from Chinese hamster ovary E1A	828:872	Detailed carbohydrate analysis revealed high-mannose structures on sCD154 purified from Pichia pastoris, whereas CD154 purified from Chinese hamster ovary E1A contained heterogeneous populations of complex carbohydrates.
11676606	0	60	theme	Chinese	160:166	arg1	cells					182:186	Chinese hamster ovary cells	160:186	Chinese hamster ovary cells	160:186	Determination of carbohydrate structures N-linked to soluble CD154 and characterization of the interactions of CD40 with CD154 expressed in Pichia pastoris and Chinese hamster ovary cells.
11676606	3	61	dep	structure	442:450	arg1	the					438:440	the	438:440	the	438:440	However, these studies have not examined the structure or biological function of the carbohydrate on CD154.
11676606	7	62	theme	similar	1007:1013	arg1	affinities					1015:1024	similar affinities	1007:1024	similar affinities of 10-30 nM	1007:1036	sCD154 purified from either system was trimeric, it bound to CD40 with similar affinities of 10-30 nM, and it functionally induced CD69 and CD95 expression on primary B cells.
11676606	2	63	theme	binding	326:332	arg1	groove					352:357	a shallow groove	342:357	a shallow groove formed between two monomers of CD154	342:394	Previous studies have described the CD40 binding site as a shallow groove formed between two monomers of CD154.
11676606	2	63	theme	binding	326:332	arg1	site					334:337	the CD40 binding site	317:337	the CD40 binding site	317:337	Previous studies have described the CD40 binding site as a shallow groove formed between two monomers of CD154.
11676606	7	64	theme	primary	1095:1101	arg1	cells					1105:1109	primary B cells	1095:1109	primary B cells	1095:1109	sCD154 purified from either system was trimeric, it bound to CD40 with similar affinities of 10-30 nM, and it functionally induced CD69 and CD95 expression on primary B cells.
11676606	8	65	from	presence	1154:1161	arg1	240					1213:1215	asparagine 240	1202:1215	asparagine 240 of CD154	1202:1224	Together, these results indicate that the presence of varied types of N-linked glycans on asparagine 240 of CD154 does not play a significant role in the CD40-CD154 interactions.
11676606	6	66	theme	carbohydrate	724:735	arg1	analysis					737:744	Detailed carbohydrate analysis	715:744	Detailed carbohydrate analysis	715:744	Detailed carbohydrate analysis revealed high-mannose structures on sCD154 purified from Pichia pastoris, whereas CD154 purified from Chinese hamster ovary E1A contained heterogeneous populations of complex carbohydrates.
11676606	8	67	attach	presence	1154:1161	arg2	types					1173:1177	varied types	1166:1177	varied types of N-linked glycans	1166:1197	Together, these results indicate that the presence of varied types of N-linked glycans on asparagine 240 of CD154 does not play a significant role in the CD40-CD154 interactions.
11676606	8	67	attach	presence	1154:1161	arg1	240					1213:1215	asparagine 240	1202:1215	asparagine 240 of CD154	1202:1224	Together, these results indicate that the presence of varied types of N-linked glycans on asparagine 240 of CD154 does not play a significant role in the CD40-CD154 interactions.
11676606	6	68	theme	Detailed	715:722	arg1	analysis					737:744	Detailed carbohydrate analysis	715:744	Detailed carbohydrate analysis	715:744	Detailed carbohydrate analysis revealed high-mannose structures on sCD154 purified from Pichia pastoris, whereas CD154 purified from Chinese hamster ovary E1A contained heterogeneous populations of complex carbohydrates.
11676606	6	69	from	structures	768:777	arg1	sCD154					782:787	sCD154	782:787	sCD154 purified from Pichia pastoris	782:817	Detailed carbohydrate analysis revealed high-mannose structures on sCD154 purified from Pichia pastoris, whereas CD154 purified from Chinese hamster ovary E1A contained heterogeneous populations of complex carbohydrates.
11876646	4	0	from	K743	498:501	arg1	cells					517:521	intact red cells	506:521	intact red cells	506:521	Trypsin, papain, and proteinase K do not cleave band 3 at or near K743 in intact red cells, even under conditions that cause cleavage on the C-terminal side of the glycosylation site (N642) in extracellular loop 4.
11876646	1	1	theme	AE1	115:117	arg1	polypeptide					120:130	the band 3 (AE1) polypeptide	103:130	the band 3 (AE1) polypeptide of the erythrocyte membrane	103:158	The topology of the band 3 (AE1) polypeptide of the erythrocyte membrane is not fully established despite extensive study.
11876646	10	2	theme	resealed	1576:1583	arg1	ghosts					1585:1590	resealed ghosts	1576:1590	resealed ghosts	1576:1590	Therefore, the actions of trypsin on intact cells, resealed ghosts, unsealed ghosts, inside-out vesicles, and microsomes from HEK293 cells all indicate that K743 is cytoplasmic and not extracellular.
11876646	2	3	from	extracellular	267:279	arg1	others					316:321	others	316:321	others	316:321	Residues near lysine 743 (K743) have been reported to be extracellular in some studies and cytoplasmic in others.
11876646	2	3	from	extracellular	267:279	arg1	studies					289:295	some studies	284:295	some studies	284:295	Residues near lysine 743 (K743) have been reported to be extracellular in some studies and cytoplasmic in others.
11876646	5	4	theme	inside-out	744:753	arg1	IOVs					765:768	IOVs	765:768	IOVs	765:768	In contrast, trypsin sealed inside red cell ghosts cleaves at K743, as does trypsin treatment of inside-out vesicles (IOVs).
11876646	5	4	theme	inside-out	744:753	arg1	vesicles					755:762	inside-out vesicles	744:762	inside-out vesicles (IOVs)	744:769	In contrast, trypsin sealed inside red cell ghosts cleaves at K743, as does trypsin treatment of inside-out vesicles (IOVs).
11876646	8	5	theme	HEK293	1210:1215	arg1	cells					1217:1221	HEK293 cells	1210:1221	HEK293 cells expressing the membrane domain of AE1 lacking the normal glycosylation site	1210:1297	Finally, microsomes were prepared from HEK293 cells expressing the membrane domain of AE1 lacking the normal glycosylation site.
11876646	9	6	theme	further	1459:1465	arg1	evidence					1467:1474	further evidence that K743 is exposed at the cytoplasmic surface	1459:1522	further evidence that K743 is exposed at the cytoplasmic surface	1459:1522	This polypeptide does not traffic to the surface membrane; trypsin treatment of microsomes containing this polypeptide produces the 20 kDa fragment, providing further evidence that K743 is exposed at the cytoplasmic surface.
11876646	4	7	from	loop	639:642	arg1	side					584:587	the C-terminal side	569:587	the C-terminal side of the glycosylation site (N642) in extracellular loop 4	569:644	Trypsin, papain, and proteinase K do not cleave band 3 at or near K743 in intact red cells, even under conditions that cause cleavage on the C-terminal side of the glycosylation site (N642) in extracellular loop 4.
11876646	4	8	theme	extracellular	625:637	arg1	loop					639:642	extracellular loop 4	625:644	extracellular loop 4	625:644	Trypsin, papain, and proteinase K do not cleave band 3 at or near K743 in intact red cells, even under conditions that cause cleavage on the C-terminal side of the glycosylation site (N642) in extracellular loop 4.
11876646	9	9	theme	microsomes	1380:1389	arg1	treatment					1367:1375	trypsin treatment	1359:1375	trypsin treatment of microsomes containing this polypeptide	1359:1417	This polypeptide does not traffic to the surface membrane; trypsin treatment of microsomes containing this polypeptide produces the 20 kDa fragment, providing further evidence that K743 is exposed at the cytoplasmic surface.
11876646	0	10	theme	lysine	75:80	arg1	sidedness					62:70	the controversial sidedness	44:70	Topology of the anion exchange protein AE1: the controversial sidedness of lysine 743.	0:85	Topology of the anion exchange protein AE1: the controversial sidedness of lysine 743.
11876646	10	11	theme	unsealed	1593:1600	arg1	ghosts					1602:1607	unsealed ghosts	1593:1607	unsealed ghosts	1593:1607	Therefore, the actions of trypsin on intact cells, resealed ghosts, unsealed ghosts, inside-out vesicles, and microsomes from HEK293 cells all indicate that K743 is cytoplasmic and not extracellular.
11876646	9	12	theme	surface	1341:1347	arg1	membrane					1349:1356	the surface membrane	1337:1356	the surface membrane	1337:1356	This polypeptide does not traffic to the surface membrane; trypsin treatment of microsomes containing this polypeptide produces the 20 kDa fragment, providing further evidence that K743 is exposed at the cytoplasmic surface.
11876646	4	13	theme	C-terminal	573:582	arg1	side					584:587	the C-terminal side	569:587	the C-terminal side of the glycosylation site (N642) in extracellular loop 4	569:644	Trypsin, papain, and proteinase K do not cleave band 3 at or near K743 in intact red cells, even under conditions that cause cleavage on the C-terminal side of the glycosylation site (N642) in extracellular loop 4.
11876646	6	14	theme	H	851:851	arg1	2'-disulfonate					835:848	2'-disulfonate	835:848	2'-disulfonate (H(2)DIDS)	835:859	The transport inhibitor 4,4'-diisothiocyanatodihydrostilbene-2,2'-disulfonate (H(2)DIDS), acting from the extracellular side, blocks trypsin cleavage at K743 in unsealed membranes by inducing a protease-resistant conformation.
11876646	6	14	theme	H	851:851	arg1	DIDS					855:858	H(2)DIDS	851:858	H(2)DIDS	851:858	The transport inhibitor 4,4'-diisothiocyanatodihydrostilbene-2,2'-disulfonate (H(2)DIDS), acting from the extracellular side, blocks trypsin cleavage at K743 in unsealed membranes by inducing a protease-resistant conformation.
11876646	5	15	theme	vesicles	755:762	arg1	treatment					731:739	trypsin treatment	723:739	trypsin treatment of inside-out vesicles (IOVs)	723:769	In contrast, trypsin sealed inside red cell ghosts cleaves at K743, as does trypsin treatment of inside-out vesicles (IOVs).
11876646	6	16	theme	extracellular	878:890	arg1	side					892:895	the extracellular side	874:895	the extracellular side	874:895	The transport inhibitor 4,4'-diisothiocyanatodihydrostilbene-2,2'-disulfonate (H(2)DIDS), acting from the extracellular side, blocks trypsin cleavage at K743 in unsealed membranes by inducing a protease-resistant conformation.
11876646	3	17	dep	in	411:412	arg1	situ					414:417	situ	414:417	situ	414:417	In the work presented here, we have attempted to establish the sidedness of K743 using in situ proteolysis.
11876646	1	18	theme	polypeptide	120:130	arg1	topology					91:98	The topology	87:98	The topology of the band 3 (AE1) polypeptide of the erythrocyte membrane	87:158	The topology of the band 3 (AE1) polypeptide of the erythrocyte membrane is not fully established despite extensive study.
11876646	6	19	theme	trypsin	905:911	arg1	cleavage					913:920	trypsin cleavage	905:920	trypsin cleavage at K743 in unsealed membranes	905:950	The transport inhibitor 4,4'-diisothiocyanatodihydrostilbene-2,2'-disulfonate (H(2)DIDS), acting from the extracellular side, blocks trypsin cleavage at K743 in unsealed membranes by inducing a protease-resistant conformation.
11876646	2	20	from	studies	289:295	arg1	extracellular					267:279	extracellular	267:279	extracellular	267:279	Residues near lysine 743 (K743) have been reported to be extracellular in some studies and cytoplasmic in others.
11876646	9	21	theme	trypsin	1359:1365	arg1	treatment					1367:1375	trypsin treatment	1359:1375	trypsin treatment of microsomes containing this polypeptide	1359:1417	This polypeptide does not traffic to the surface membrane; trypsin treatment of microsomes containing this polypeptide produces the 20 kDa fragment, providing further evidence that K743 is exposed at the cytoplasmic surface.
11876646	6	22	dep	DIDS	855:858	arg1	2					853:853	2	853:853	2	853:853	The transport inhibitor 4,4'-diisothiocyanatodihydrostilbene-2,2'-disulfonate (H(2)DIDS), acting from the extracellular side, blocks trypsin cleavage at K743 in unsealed membranes by inducing a protease-resistant conformation.
11876646	7	23	theme	H	999:999	arg1	DIDS					1003:1006	H(2)DIDS	999:1006	H(2)DIDS added to IOVs	999:1020	H(2)DIDS added to IOVs does not prevent cleavage at K743; therefore, trypsin cleavage at K743 in IOVs is not a consequence of cleavage of right-side-out or leaky vesicles.
11876646	9	24	theme	20	1432:1433	arg1	kDa					1435:1437	kDa	1435:1437	kDa	1435:1437	This polypeptide does not traffic to the surface membrane; trypsin treatment of microsomes containing this polypeptide produces the 20 kDa fragment, providing further evidence that K743 is exposed at the cytoplasmic surface.
11876646	4	25	theme	site	610:613	arg1	side					584:587	the C-terminal side	569:587	the C-terminal side of the glycosylation site (N642) in extracellular loop 4	569:644	Trypsin, papain, and proteinase K do not cleave band 3 at or near K743 in intact red cells, even under conditions that cause cleavage on the C-terminal side of the glycosylation site (N642) in extracellular loop 4.
11876646	1	26	theme	erythrocyte	139:149	arg1	membrane					151:158	the erythrocyte membrane	135:158	the erythrocyte membrane	135:158	The topology of the band 3 (AE1) polypeptide of the erythrocyte membrane is not fully established despite extensive study.
11876646	0	27	theme	anion	16:20	arg1	AE1					39:41	the anion exchange protein AE1	12:41	the anion exchange protein AE1	12:41	Topology of the anion exchange protein AE1: the controversial sidedness of lysine 743.
11876646	10	28	theme	inside-out	1610:1619	arg1	vesicles					1621:1628	inside-out vesicles	1610:1628	inside-out vesicles	1610:1628	Therefore, the actions of trypsin on intact cells, resealed ghosts, unsealed ghosts, inside-out vesicles, and microsomes from HEK293 cells all indicate that K743 is cytoplasmic and not extracellular.
11876646	4	29	from	site	610:613	arg1	loop					639:642	extracellular loop 4	625:644	extracellular loop 4	625:644	Trypsin, papain, and proteinase K do not cleave band 3 at or near K743 in intact red cells, even under conditions that cause cleavage on the C-terminal side of the glycosylation site (N642) in extracellular loop 4.
11876646	7	30	from	K743	1051:1054	arg1	cleavage					1039:1046	cleavage	1039:1046	cleavage at K743	1039:1054	H(2)DIDS added to IOVs does not prevent cleavage at K743; therefore, trypsin cleavage at K743 in IOVs is not a consequence of cleavage of right-side-out or leaky vesicles.
11876646	1	31	theme	membrane	151:158	arg1	polypeptide					120:130	the band 3 (AE1) polypeptide	103:130	the band 3 (AE1) polypeptide of the erythrocyte membrane	103:158	The topology of the band 3 (AE1) polypeptide of the erythrocyte membrane is not fully established despite extensive study.
11876646	5	32	theme	red	682:684	arg1	ghosts					691:696	red cell ghosts	682:696	red cell ghosts	682:696	In contrast, trypsin sealed inside red cell ghosts cleaves at K743, as does trypsin treatment of inside-out vesicles (IOVs).
11876646	10	33	theme	HEK293	1651:1656	arg1	cells					1658:1662	HEK293 cells	1651:1662	HEK293 cells	1651:1662	Therefore, the actions of trypsin on intact cells, resealed ghosts, unsealed ghosts, inside-out vesicles, and microsomes from HEK293 cells all indicate that K743 is cytoplasmic and not extracellular.
11876646	6	34	theme	protease-resistant	966:983	arg1	conformation					985:996	a protease-resistant conformation	964:996	a protease-resistant conformation	964:996	The transport inhibitor 4,4'-diisothiocyanatodihydrostilbene-2,2'-disulfonate (H(2)DIDS), acting from the extracellular side, blocks trypsin cleavage at K743 in unsealed membranes by inducing a protease-resistant conformation.
11876646	10	35	theme	trypsin	1551:1557	arg1	actions					1540:1546	the actions	1536:1546	the actions of trypsin on intact cells, resealed ghosts, unsealed ghosts, inside-out vesicles, and microsomes from HEK293 cells	1536:1662	Therefore, the actions of trypsin on intact cells, resealed ghosts, unsealed ghosts, inside-out vesicles, and microsomes from HEK293 cells all indicate that K743 is cytoplasmic and not extracellular.
11876646	4	36	theme	red	513:515	arg1	cells					517:521	intact red cells	506:521	intact red cells	506:521	Trypsin, papain, and proteinase K do not cleave band 3 at or near K743 in intact red cells, even under conditions that cause cleavage on the C-terminal side of the glycosylation site (N642) in extracellular loop 4.
11876646	0	37	theme	protein	31:37	arg1	AE1					39:41	the anion exchange protein AE1	12:41	the anion exchange protein AE1	12:41	Topology of the anion exchange protein AE1: the controversial sidedness of lysine 743.
11876646	9	38	theme	cytoplasmic	1504:1514	arg1	surface					1516:1522	the cytoplasmic surface	1500:1522	the cytoplasmic surface	1500:1522	This polypeptide does not traffic to the surface membrane; trypsin treatment of microsomes containing this polypeptide produces the 20 kDa fragment, providing further evidence that K743 is exposed at the cytoplasmic surface.
11876646	8	39	theme	membrane	1238:1245	arg1	AE1					1257:1259	AE1	1257:1259	AE1 lacking the normal glycosylation site	1257:1297	Finally, microsomes were prepared from HEK293 cells expressing the membrane domain of AE1 lacking the normal glycosylation site.
11876646	8	39	theme	membrane	1238:1245	arg1	domain					1247:1252	the membrane domain	1234:1252	the membrane domain of AE1 lacking the normal glycosylation site	1234:1297	Finally, microsomes were prepared from HEK293 cells expressing the membrane domain of AE1 lacking the normal glycosylation site.
11876646	9	40	contain	containing	1391:1400	arg2	polypeptide					1407:1417	this polypeptide	1402:1417	this polypeptide	1402:1417	This polypeptide does not traffic to the surface membrane; trypsin treatment of microsomes containing this polypeptide produces the 20 kDa fragment, providing further evidence that K743 is exposed at the cytoplasmic surface.
11876646	9	40	contain	containing	1391:1400	arg1	microsomes					1380:1389	microsomes	1380:1389	microsomes containing this polypeptide	1380:1417	This polypeptide does not traffic to the surface membrane; trypsin treatment of microsomes containing this polypeptide produces the 20 kDa fragment, providing further evidence that K743 is exposed at the cytoplasmic surface.
11876646	0	41	theme	exchange	22:29	arg1	AE1					39:41	the anion exchange protein AE1	12:41	the anion exchange protein AE1	12:41	Topology of the anion exchange protein AE1: the controversial sidedness of lysine 743.
11876646	6	42	theme	inhibitor	786:794	arg1	2'-disulfonate					835:848	2'-disulfonate	835:848	2'-disulfonate (H(2)DIDS)	835:859	The transport inhibitor 4,4'-diisothiocyanatodihydrostilbene-2,2'-disulfonate (H(2)DIDS), acting from the extracellular side, blocks trypsin cleavage at K743 in unsealed membranes by inducing a protease-resistant conformation.
11876646	6	42	theme	inhibitor	786:794	arg1	4,4'-diisothiocyanatodihydrostilbene-2					796:833	The transport inhibitor 4,4'-diisothiocyanatodihydrostilbene-2	772:833	The transport inhibitor 4,4'-diisothiocyanatodihydrostilbene-2	772:833	The transport inhibitor 4,4'-diisothiocyanatodihydrostilbene-2,2'-disulfonate (H(2)DIDS), acting from the extracellular side, blocks trypsin cleavage at K743 in unsealed membranes by inducing a protease-resistant conformation.
11876646	4	43	gly	glycosylation	596:608	arg2	site					610:613	the glycosylation site	592:613	the glycosylation site (N642) in extracellular loop 4	592:644	Trypsin, papain, and proteinase K do not cleave band 3 at or near K743 in intact red cells, even under conditions that cause cleavage on the C-terminal side of the glycosylation site (N642) in extracellular loop 4.
11876646	4	43	gly	glycosylation	596:608	arg2	N642					616:619	N642	616:619	N642	616:619	Trypsin, papain, and proteinase K do not cleave band 3 at or near K743 in intact red cells, even under conditions that cause cleavage on the C-terminal side of the glycosylation site (N642) in extracellular loop 4.
11876646	8	44	theme	AE1	1257:1259	arg1	AE1					1257:1259	AE1	1257:1259	AE1 lacking the normal glycosylation site	1257:1297	Finally, microsomes were prepared from HEK293 cells expressing the membrane domain of AE1 lacking the normal glycosylation site.
11876646	8	44	theme	AE1	1257:1259	arg1	domain					1247:1252	the membrane domain	1234:1252	the membrane domain of AE1 lacking the normal glycosylation site	1234:1297	Finally, microsomes were prepared from HEK293 cells expressing the membrane domain of AE1 lacking the normal glycosylation site.
11876646	4	45	theme	intact	506:511	arg1	cells					517:521	intact red cells	506:521	intact red cells	506:521	Trypsin, papain, and proteinase K do not cleave band 3 at or near K743 in intact red cells, even under conditions that cause cleavage on the C-terminal side of the glycosylation site (N642) in extracellular loop 4.
11876646	8	46	gly	glycosylation	1280:1292	arg2	site					1294:1297	the normal glycosylation site	1269:1297	the normal glycosylation site	1269:1297	Finally, microsomes were prepared from HEK293 cells expressing the membrane domain of AE1 lacking the normal glycosylation site.
11876646	6	47	theme	transport	776:784	arg1	2'-disulfonate					835:848	2'-disulfonate	835:848	2'-disulfonate (H(2)DIDS)	835:859	The transport inhibitor 4,4'-diisothiocyanatodihydrostilbene-2,2'-disulfonate (H(2)DIDS), acting from the extracellular side, blocks trypsin cleavage at K743 in unsealed membranes by inducing a protease-resistant conformation.
11876646	6	47	theme	transport	776:784	arg1	4,4'-diisothiocyanatodihydrostilbene-2					796:833	The transport inhibitor 4,4'-diisothiocyanatodihydrostilbene-2	772:833	The transport inhibitor 4,4'-diisothiocyanatodihydrostilbene-2	772:833	The transport inhibitor 4,4'-diisothiocyanatodihydrostilbene-2,2'-disulfonate (H(2)DIDS), acting from the extracellular side, blocks trypsin cleavage at K743 in unsealed membranes by inducing a protease-resistant conformation.
11876646	7	48	theme	vesicles	1161:1168	arg1	cleavage					1125:1132	cleavage	1125:1132	cleavage of right-side-out or leaky vesicles	1125:1168	H(2)DIDS added to IOVs does not prevent cleavage at K743; therefore, trypsin cleavage at K743 in IOVs is not a consequence of cleavage of right-side-out or leaky vesicles.
11876646	2	49	from	others	316:321	arg1	extracellular					267:279	extracellular	267:279	extracellular	267:279	Residues near lysine 743 (K743) have been reported to be extracellular in some studies and cytoplasmic in others.
11876646	3	50	theme	in	411:412	arg1	proteolysis					419:429	in situ proteolysis	411:429	in situ proteolysis	411:429	In the work presented here, we have attempted to establish the sidedness of K743 using in situ proteolysis.
11876646	0	51	theme	AE1	39:41	arg1	Topology					0:7	Topology	0:7	Topology of the anion exchange protein AE1: the controversial sidedness of lysine 743.	0:85	Topology of the anion exchange protein AE1: the controversial sidedness of lysine 743.
11876646	4	52	theme	proteinase	453:462	arg1	K					464:464	proteinase K	453:464	proteinase K	453:464	Trypsin, papain, and proteinase K do not cleave band 3 at or near K743 in intact red cells, even under conditions that cause cleavage on the C-terminal side of the glycosylation site (N642) in extracellular loop 4.
11876646	7	53	theme	cleavage	1125:1132	arg1	consequence					1110:1120	a consequence	1108:1120	a consequence of cleavage of right-side-out or leaky vesicles	1108:1168	H(2)DIDS added to IOVs does not prevent cleavage at K743; therefore, trypsin cleavage at K743 in IOVs is not a consequence of cleavage of right-side-out or leaky vesicles.
11876646	7	53	theme	cleavage	1125:1132	arg1	cleavage					1076:1083	trypsin cleavage	1068:1083	trypsin cleavage at K743 in IOVs	1068:1099	H(2)DIDS added to IOVs does not prevent cleavage at K743; therefore, trypsin cleavage at K743 in IOVs is not a consequence of cleavage of right-side-out or leaky vesicles.
11876646	7	54	from	K743	1088:1091	arg1	cleavage					1076:1083	trypsin cleavage	1068:1083	trypsin cleavage at K743 in IOVs	1068:1099	H(2)DIDS added to IOVs does not prevent cleavage at K743; therefore, trypsin cleavage at K743 in IOVs is not a consequence of cleavage of right-side-out or leaky vesicles.
11876646	7	54	from	K743	1088:1091	arg1	IOVs					1096:1099	IOVs	1096:1099	IOVs	1096:1099	H(2)DIDS added to IOVs does not prevent cleavage at K743; therefore, trypsin cleavage at K743 in IOVs is not a consequence of cleavage of right-side-out or leaky vesicles.
11876646	7	54	from	K743	1088:1091	arg1	consequence					1110:1120	a consequence	1108:1120	a consequence of cleavage of right-side-out or leaky vesicles	1108:1168	H(2)DIDS added to IOVs does not prevent cleavage at K743; therefore, trypsin cleavage at K743 in IOVs is not a consequence of cleavage of right-side-out or leaky vesicles.
11876646	10	55	theme	intact	1562:1567	arg1	cells					1569:1573	intact cells	1562:1573	intact cells	1562:1573	Therefore, the actions of trypsin on intact cells, resealed ghosts, unsealed ghosts, inside-out vesicles, and microsomes from HEK293 cells all indicate that K743 is cytoplasmic and not extracellular.
11876646	7	56	theme	right-side-out	1137:1150	arg1	vesicles					1161:1168	right-side-out or leaky vesicles	1137:1168	vesicles	1161:1168	H(2)DIDS added to IOVs does not prevent cleavage at K743; therefore, trypsin cleavage at K743 in IOVs is not a consequence of cleavage of right-side-out or leaky vesicles.
11876646	5	57	dep	does	718:721	arg1	as					715:716	as	715:716	as	715:716	In contrast, trypsin sealed inside red cell ghosts cleaves at K743, as does trypsin treatment of inside-out vesicles (IOVs).
11876646	4	58	theme	glycosylation	596:608	arg1	N642					616:619	N642	616:619	N642	616:619	Trypsin, papain, and proteinase K do not cleave band 3 at or near K743 in intact red cells, even under conditions that cause cleavage on the C-terminal side of the glycosylation site (N642) in extracellular loop 4.
11876646	4	58	theme	glycosylation	596:608	arg1	site					610:613	the glycosylation site	592:613	the glycosylation site (N642) in extracellular loop 4	592:644	Trypsin, papain, and proteinase K do not cleave band 3 at or near K743 in intact red cells, even under conditions that cause cleavage on the C-terminal side of the glycosylation site (N642) in extracellular loop 4.
11876646	10	59	from	actions	1540:1546	arg1	cells					1569:1573	intact cells	1562:1573	intact cells	1562:1573	Therefore, the actions of trypsin on intact cells, resealed ghosts, unsealed ghosts, inside-out vesicles, and microsomes from HEK293 cells all indicate that K743 is cytoplasmic and not extracellular.
11876646	10	59	from	actions	1540:1546	arg1	ghosts					1585:1590	resealed ghosts	1576:1590	resealed ghosts	1576:1590	Therefore, the actions of trypsin on intact cells, resealed ghosts, unsealed ghosts, inside-out vesicles, and microsomes from HEK293 cells all indicate that K743 is cytoplasmic and not extracellular.
11876646	10	59	from	actions	1540:1546	arg1	ghosts					1602:1607	unsealed ghosts	1593:1607	unsealed ghosts	1593:1607	Therefore, the actions of trypsin on intact cells, resealed ghosts, unsealed ghosts, inside-out vesicles, and microsomes from HEK293 cells all indicate that K743 is cytoplasmic and not extracellular.
11876646	10	59	from	actions	1540:1546	arg1	vesicles					1621:1628	inside-out vesicles	1610:1628	inside-out vesicles	1610:1628	Therefore, the actions of trypsin on intact cells, resealed ghosts, unsealed ghosts, inside-out vesicles, and microsomes from HEK293 cells all indicate that K743 is cytoplasmic and not extracellular.
11876646	10	59	from	actions	1540:1546	arg1	microsomes					1635:1644	microsomes	1635:1644	microsomes from HEK293 cells	1635:1662	Therefore, the actions of trypsin on intact cells, resealed ghosts, unsealed ghosts, inside-out vesicles, and microsomes from HEK293 cells all indicate that K743 is cytoplasmic and not extracellular.
11876646	8	60	theme	glycosylation	1280:1292	arg1	site					1294:1297	the normal glycosylation site	1269:1297	the normal glycosylation site	1269:1297	Finally, microsomes were prepared from HEK293 cells expressing the membrane domain of AE1 lacking the normal glycosylation site.
11876646	7	61	theme	leaky	1155:1159	arg1	vesicles					1161:1168	right-side-out or leaky vesicles	1137:1168	vesicles	1161:1168	H(2)DIDS added to IOVs does not prevent cleavage at K743; therefore, trypsin cleavage at K743 in IOVs is not a consequence of cleavage of right-side-out or leaky vesicles.
11876646	6	62	from	K743	925:928	arg1	membranes					942:950	unsealed membranes	933:950	unsealed membranes	933:950	The transport inhibitor 4,4'-diisothiocyanatodihydrostilbene-2,2'-disulfonate (H(2)DIDS), acting from the extracellular side, blocks trypsin cleavage at K743 in unsealed membranes by inducing a protease-resistant conformation.
11876646	6	62	from	K743	925:928	arg1	cleavage					913:920	trypsin cleavage	905:920	trypsin cleavage at K743 in unsealed membranes	905:950	The transport inhibitor 4,4'-diisothiocyanatodihydrostilbene-2,2'-disulfonate (H(2)DIDS), acting from the extracellular side, blocks trypsin cleavage at K743 in unsealed membranes by inducing a protease-resistant conformation.
11876646	1	63	theme	band	107:110	arg1	polypeptide					120:130	the band 3 (AE1) polypeptide	103:130	the band 3 (AE1) polypeptide of the erythrocyte membrane	103:158	The topology of the band 3 (AE1) polypeptide of the erythrocyte membrane is not fully established despite extensive study.
11876646	3	64	theme	K743	400:403	arg1	sidedness					387:395	the sidedness	383:395	the sidedness of K743	383:403	In the work presented here, we have attempted to establish the sidedness of K743 using in situ proteolysis.
11876646	0	65	theme	controversial	48:60	arg1	sidedness					62:70	the controversial sidedness	44:70	Topology of the anion exchange protein AE1: the controversial sidedness of lysine 743.	0:85	Topology of the anion exchange protein AE1: the controversial sidedness of lysine 743.
11876646	8	66	theme	normal	1273:1278	arg1	site					1294:1297	the normal glycosylation site	1269:1297	the normal glycosylation site	1269:1297	Finally, microsomes were prepared from HEK293 cells expressing the membrane domain of AE1 lacking the normal glycosylation site.
11876646	9	67	theme	kDa	1435:1437	arg1	fragment					1439:1446	the 20 kDa fragment	1428:1446	the 20 kDa fragment	1428:1446	This polypeptide does not traffic to the surface membrane; trypsin treatment of microsomes containing this polypeptide produces the 20 kDa fragment, providing further evidence that K743 is exposed at the cytoplasmic surface.
11876646	5	68	theme	cell	686:689	arg1	ghosts					691:696	red cell ghosts	682:696	red cell ghosts	682:696	In contrast, trypsin sealed inside red cell ghosts cleaves at K743, as does trypsin treatment of inside-out vesicles (IOVs).
11876646	5	69	theme	trypsin	723:729	arg1	treatment					731:739	trypsin treatment	723:739	trypsin treatment of inside-out vesicles (IOVs)	723:769	In contrast, trypsin sealed inside red cell ghosts cleaves at K743, as does trypsin treatment of inside-out vesicles (IOVs).
11876646	4	70	from	side	584:587	arg1	loop					639:642	extracellular loop 4	625:644	extracellular loop 4	625:644	Trypsin, papain, and proteinase K do not cleave band 3 at or near K743 in intact red cells, even under conditions that cause cleavage on the C-terminal side of the glycosylation site (N642) in extracellular loop 4.
11876646	1	71	theme	extensive	193:201	arg1	study					203:207	extensive study	193:207	extensive study	193:207	The topology of the band 3 (AE1) polypeptide of the erythrocyte membrane is not fully established despite extensive study.
11876646	6	72	theme	unsealed	933:940	arg1	membranes					942:950	unsealed membranes	933:950	unsealed membranes	933:950	The transport inhibitor 4,4'-diisothiocyanatodihydrostilbene-2,2'-disulfonate (H(2)DIDS), acting from the extracellular side, blocks trypsin cleavage at K743 in unsealed membranes by inducing a protease-resistant conformation.
11876646	0	73	dep	Topology	0:7	arg1	sidedness					62:70	the controversial sidedness	44:70	Topology of the anion exchange protein AE1: the controversial sidedness of lysine 743.	0:85	Topology of the anion exchange protein AE1: the controversial sidedness of lysine 743.
11876646	7	74	theme	trypsin	1068:1074	arg1	cleavage					1076:1083	trypsin cleavage	1068:1083	trypsin cleavage at K743 in IOVs	1068:1099	H(2)DIDS added to IOVs does not prevent cleavage at K743; therefore, trypsin cleavage at K743 in IOVs is not a consequence of cleavage of right-side-out or leaky vesicles.
11876646	7	74	theme	trypsin	1068:1074	arg1	consequence					1110:1120	a consequence	1108:1120	a consequence of cleavage of right-side-out or leaky vesicles	1108:1168	H(2)DIDS added to IOVs does not prevent cleavage at K743; therefore, trypsin cleavage at K743 in IOVs is not a consequence of cleavage of right-side-out or leaky vesicles.
11876646	10	75	from	cells	1658:1662	arg1	cells					1569:1573	intact cells	1562:1573	intact cells	1562:1573	Therefore, the actions of trypsin on intact cells, resealed ghosts, unsealed ghosts, inside-out vesicles, and microsomes from HEK293 cells all indicate that K743 is cytoplasmic and not extracellular.
11876646	10	75	from	cells	1658:1662	arg1	ghosts					1585:1590	resealed ghosts	1576:1590	resealed ghosts	1576:1590	Therefore, the actions of trypsin on intact cells, resealed ghosts, unsealed ghosts, inside-out vesicles, and microsomes from HEK293 cells all indicate that K743 is cytoplasmic and not extracellular.
11876646	10	75	from	cells	1658:1662	arg1	ghosts					1602:1607	unsealed ghosts	1593:1607	unsealed ghosts	1593:1607	Therefore, the actions of trypsin on intact cells, resealed ghosts, unsealed ghosts, inside-out vesicles, and microsomes from HEK293 cells all indicate that K743 is cytoplasmic and not extracellular.
11876646	10	75	from	cells	1658:1662	arg1	vesicles					1621:1628	inside-out vesicles	1610:1628	inside-out vesicles	1610:1628	Therefore, the actions of trypsin on intact cells, resealed ghosts, unsealed ghosts, inside-out vesicles, and microsomes from HEK293 cells all indicate that K743 is cytoplasmic and not extracellular.
11876646	10	75	from	cells	1658:1662	arg1	microsomes					1635:1644	microsomes	1635:1644	microsomes from HEK293 cells	1635:1662	Therefore, the actions of trypsin on intact cells, resealed ghosts, unsealed ghosts, inside-out vesicles, and microsomes from HEK293 cells all indicate that K743 is cytoplasmic and not extracellular.
1731338	7	0	theme	anti-CD43	1307:1315	arg1	antibodies					1317:1326	monoclonal anti-CD43 antibodies	1296:1326	monoclonal anti-CD43 antibodies	1296:1326	Further support of the relatedness of these molecules was obtained by immunoprecipitation of 125I-labeled galactoglycoprotein by monoclonal anti-CD43 antibodies.
1731338	3	1	theme	sites	693:697	arg1	locations					677:685	the locations	673:685	the locations of 25 sites of O-glycosylation and three serine sites that are not glycosylated	673:765	Comparison of peptide sequences from the native galactoglycoprotein and the deglycosylated derivative demonstrated the locations of 25 sites of O-glycosylation and three serine sites that are not glycosylated.
1731338	1	2	gly	galactoglycoprotein	146:164	arg1	galactoglycoprotein					146:164	galactoglycoprotein	146:164	galactoglycoprotein purified from human plasma	146:191	The amino acid sequence of galactoglycoprotein purified from human plasma was elucidated to 75% completeness by using chemical degradation of peptides and glycopeptides derived from digests of the protein with seven specific proteases.
1731338	1	3	theme	chemical	237:244	arg1	degradation					246:256	chemical degradation	237:256	chemical degradation of peptides and glycopeptides derived from digests of the protein with seven specific proteases	237:352	The amino acid sequence of galactoglycoprotein purified from human plasma was elucidated to 75% completeness by using chemical degradation of peptides and glycopeptides derived from digests of the protein with seven specific proteases.
1731338	3	4	gly	deglycosylated	634:647	arg1	derivative					649:658	the deglycosylated derivative	630:658	the deglycosylated derivative	630:658	Comparison of peptide sequences from the native galactoglycoprotein and the deglycosylated derivative demonstrated the locations of 25 sites of O-glycosylation and three serine sites that are not glycosylated.
1731338	3	5	theme	sites	735:739	arg1	locations					677:685	the locations	673:685	the locations of 25 sites of O-glycosylation and three serine sites that are not glycosylated	673:765	Comparison of peptide sequences from the native galactoglycoprotein and the deglycosylated derivative demonstrated the locations of 25 sites of O-glycosylation and three serine sites that are not glycosylated.
1731338	1	6	with	digests	301:307	arg1	proteases					344:352	seven specific proteases	329:352	seven specific proteases	329:352	The amino acid sequence of galactoglycoprotein purified from human plasma was elucidated to 75% completeness by using chemical degradation of peptides and glycopeptides derived from digests of the protein with seven specific proteases.
1731338	5	7	theme	C-terminal	822:831	arg1	analysis					833:840	C-terminal analysis	822:840	C-terminal analysis	822:840	C-terminal analysis revealed multiple C-terminal residues, suggesting that galactoglycoprotein molecules are of varying lengths.
1731338	1	8	theme	human	180:184	arg1	plasma					186:191	human plasma	180:191	human plasma	180:191	The amino acid sequence of galactoglycoprotein purified from human plasma was elucidated to 75% completeness by using chemical degradation of peptides and glycopeptides derived from digests of the protein with seven specific proteases.
1731338	2	9	theme	multiple	531:538	arg1	glycans					549:555	one N-linked and multiple O-linked glycans	514:555	one N-linked and multiple O-linked glycans	514:555	This sequence represents a polypeptide chain of approximately 220 amino acid residues including a high content of serine, threonine, alanine, and proline with one N-linked and multiple O-linked glycans.
1731338	2	10	link	O-linked	540:547	arg1	glycans					549:555	one N-linked and multiple O-linked glycans	514:555	one N-linked and multiple O-linked glycans	514:555	This sequence represents a polypeptide chain of approximately 220 amino acid residues including a high content of serine, threonine, alanine, and proline with one N-linked and multiple O-linked glycans.
1731338	5	11	theme	C-terminal	860:869	arg1	residues					871:878	multiple C-terminal residues	851:878	multiple C-terminal residues	851:878	C-terminal analysis revealed multiple C-terminal residues, suggesting that galactoglycoprotein molecules are of varying lengths.
1731338	2	12	theme	N-linked	518:525	arg1	glycans					549:555	one N-linked and multiple O-linked glycans	514:555	one N-linked and multiple O-linked glycans	514:555	This sequence represents a polypeptide chain of approximately 220 amino acid residues including a high content of serine, threonine, alanine, and proline with one N-linked and multiple O-linked glycans.
1731338	7	13	theme	Further	1167:1173	arg1	support					1175:1181	Further support	1167:1181	Further support of the relatedness of these molecules	1167:1219	Further support of the relatedness of these molecules was obtained by immunoprecipitation of 125I-labeled galactoglycoprotein by monoclonal anti-CD43 antibodies.
1731338	6	14	theme	data	973:976	arg1	base					978:981	a protein data base	963:981	a protein data base	963:981	A search of a protein data base revealed that the galactoglycoprotein polypeptide is identical to the N-terminal (extracellular) polypeptide region of the blood-cell surface molecule CD43 (sialophorin, leukosialin).
1731338	8	15	theme	molecules	1367:1375	arg1	properties					1349:1358	properties	1349:1358	properties	1349:1358	The composition and properties of the molecules together with the known structure of the gene encoding CD43 suggest that galactoprotein is derived by proteolytic cleavage from transmembrane "hexasaccharide CD43," known to be expressed on neutrophils, activated T lymphocytes, and platelets.
1731338	8	15	theme	molecules	1367:1375	arg1	composition					1333:1343	composition	1333:1343	composition	1333:1343	The composition and properties of the molecules together with the known structure of the gene encoding CD43 suggest that galactoprotein is derived by proteolytic cleavage from transmembrane "hexasaccharide CD43," known to be expressed on neutrophils, activated T lymphocytes, and platelets.
1731338	3	16	theme	peptide	572:578	arg1	sequences					580:588	peptide sequences	572:588	peptide sequences from the native galactoglycoprotein	572:624	Comparison of peptide sequences from the native galactoglycoprotein and the deglycosylated derivative demonstrated the locations of 25 sites of O-glycosylation and three serine sites that are not glycosylated.
1731338	2	17	with	content	458:464	arg1	glycans					549:555	one N-linked and multiple O-linked glycans	514:555	one N-linked and multiple O-linked glycans	514:555	This sequence represents a polypeptide chain of approximately 220 amino acid residues including a high content of serine, threonine, alanine, and proline with one N-linked and multiple O-linked glycans.
1731338	2	18	theme	alanine	488:494	arg1	content					458:464	a high content	451:464	a high content of serine, threonine, alanine, and proline with one N-linked and multiple O-linked glycans	451:555	This sequence represents a polypeptide chain of approximately 220 amino acid residues including a high content of serine, threonine, alanine, and proline with one N-linked and multiple O-linked glycans.
1731338	8	19	theme	known	1395:1399	arg1	structure					1401:1409	the known structure	1391:1409	The composition and properties of the molecules together with the known structure of the gene encoding CD43	1329:1435	The composition and properties of the molecules together with the known structure of the gene encoding CD43 suggest that galactoprotein is derived by proteolytic cleavage from transmembrane "hexasaccharide CD43," known to be expressed on neutrophils, activated T lymphocytes, and platelets.
1731338	3	20	from	Comparison	558:567	arg1	galactoglycoprotein					606:624	the native galactoglycoprotein	595:624	the native galactoglycoprotein	595:624	Comparison of peptide sequences from the native galactoglycoprotein and the deglycosylated derivative demonstrated the locations of 25 sites of O-glycosylation and three serine sites that are not glycosylated.
1731338	7	21	theme	monoclonal	1296:1305	arg1	antibodies					1317:1326	monoclonal anti-CD43 antibodies	1296:1326	monoclonal anti-CD43 antibodies	1296:1326	Further support of the relatedness of these molecules was obtained by immunoprecipitation of 125I-labeled galactoglycoprotein by monoclonal anti-CD43 antibodies.
1731338	1	22	theme	protein	316:322	arg1	digests					301:307	digests	301:307	digests of the protein with seven specific proteases	301:352	The amino acid sequence of galactoglycoprotein purified from human plasma was elucidated to 75% completeness by using chemical degradation of peptides and glycopeptides derived from digests of the protein with seven specific proteases.
1731338	3	23	theme	native	599:604	arg1	galactoglycoprotein					606:624	the native galactoglycoprotein	595:624	the native galactoglycoprotein	595:624	Comparison of peptide sequences from the native galactoglycoprotein and the deglycosylated derivative demonstrated the locations of 25 sites of O-glycosylation and three serine sites that are not glycosylated.
1731338	1	24	theme	acid	129:132	arg1	sequence					134:141	The amino acid sequence	119:141	The amino acid sequence of galactoglycoprotein purified from human plasma	119:191	The amino acid sequence of galactoglycoprotein purified from human plasma was elucidated to 75% completeness by using chemical degradation of peptides and glycopeptides derived from digests of the protein with seven specific proteases.
1731338	2	25	theme	threonine	477:485	arg1	content					458:464	a high content	451:464	a high content of serine, threonine, alanine, and proline with one N-linked and multiple O-linked glycans	451:555	This sequence represents a polypeptide chain of approximately 220 amino acid residues including a high content of serine, threonine, alanine, and proline with one N-linked and multiple O-linked glycans.
1731338	7	26	theme	galactoglycoprotein	1273:1291	arg1	immunoprecipitation					1237:1255	immunoprecipitation	1237:1255	immunoprecipitation of 125I-labeled galactoglycoprotein	1237:1291	Further support of the relatedness of these molecules was obtained by immunoprecipitation of 125I-labeled galactoglycoprotein by monoclonal anti-CD43 antibodies.
1731338	8	27	theme	activated	1580:1588	arg1	lymphocytes					1592:1602	activated T lymphocytes	1580:1602	activated T lymphocytes	1580:1602	The composition and properties of the molecules together with the known structure of the gene encoding CD43 suggest that galactoprotein is derived by proteolytic cleavage from transmembrane "hexasaccharide CD43," known to be expressed on neutrophils, activated T lymphocytes, and platelets.
1731338	4	28	theme	homogeneous	772:782	arg1	serine					814:819	serine	814:819	serine	814:819	The homogeneous N terminus was established as serine.
1731338	4	28	theme	homogeneous	772:782	arg1	terminus					786:793	The homogeneous N terminus	768:793	The homogeneous N terminus	768:793	The homogeneous N terminus was established as serine.
1731338	3	29	gly	glycosylated	754:765	arg1	O-glycosylation					702:716	O-glycosylation	702:716	O-glycosylation	702:716	Comparison of peptide sequences from the native galactoglycoprotein and the deglycosylated derivative demonstrated the locations of 25 sites of O-glycosylation and three serine sites that are not glycosylated.
1731338	3	29	gly	glycosylated	754:765	arg1	sites					693:697	25 sites	690:697	25 sites of O-glycosylation	690:716	Comparison of peptide sequences from the native galactoglycoprotein and the deglycosylated derivative demonstrated the locations of 25 sites of O-glycosylation and three serine sites that are not glycosylated.
1731338	3	29	gly	glycosylated	754:765	arg1	sites					735:739	three serine sites	722:739	three serine sites	722:739	Comparison of peptide sequences from the native galactoglycoprotein and the deglycosylated derivative demonstrated the locations of 25 sites of O-glycosylation and three serine sites that are not glycosylated.
1731338	0	30	theme	CD43	99:102	arg1	region					89:94	the extracellular region	71:94	the extracellular region of CD43 (sialophorin)	71:116	Amino acid sequence of human plasma galactoglycoprotein: identity with the extracellular region of CD43 (sialophorin).
1731338	8	31	dep	composition	1333:1343	arg1	The					1329:1331	The	1329:1331	The	1329:1331	The composition and properties of the molecules together with the known structure of the gene encoding CD43 suggest that galactoprotein is derived by proteolytic cleavage from transmembrane "hexasaccharide CD43," known to be expressed on neutrophils, activated T lymphocytes, and platelets.
1731338	6	32	theme	surface	1117:1123	arg1	sialophorin					1140:1150	sialophorin	1140:1150	sialophorin	1140:1150	A search of a protein data base revealed that the galactoglycoprotein polypeptide is identical to the N-terminal (extracellular) polypeptide region of the blood-cell surface molecule CD43 (sialophorin, leukosialin).
1731338	6	32	theme	surface	1117:1123	arg1	CD43					1134:1137	the blood-cell surface molecule CD43	1102:1137	the blood-cell surface molecule CD43 (sialophorin, leukosialin)	1102:1164	A search of a protein data base revealed that the galactoglycoprotein polypeptide is identical to the N-terminal (extracellular) polypeptide region of the blood-cell surface molecule CD43 (sialophorin, leukosialin).
1731338	0	33	theme	Amino	0:4	arg1	sequence					11:18	Amino acid sequence	0:18	Amino acid sequence of human plasma galactoglycoprotein: identity with the extracellular region of CD43 (sialophorin).	0:117	Amino acid sequence of human plasma galactoglycoprotein: identity with the extracellular region of CD43 (sialophorin).
1731338	1	34	theme	peptides	261:268	arg1	degradation					246:256	chemical degradation	237:256	chemical degradation of peptides and glycopeptides derived from digests of the protein with seven specific proteases	237:352	The amino acid sequence of galactoglycoprotein purified from human plasma was elucidated to 75% completeness by using chemical degradation of peptides and glycopeptides derived from digests of the protein with seven specific proteases.
1731338	2	35	theme	residues	432:439	arg1	chain					394:398	a polypeptide chain	380:398	a polypeptide chain of approximately 220 amino acid residues including a high content of serine, threonine, alanine, and proline with one N-linked and multiple O-linked glycans	380:555	This sequence represents a polypeptide chain of approximately 220 amino acid residues including a high content of serine, threonine, alanine, and proline with one N-linked and multiple O-linked glycans.
1731338	7	36	gly	galactoglycoprotein	1273:1291	arg1	galactoglycoprotein					1273:1291	125I-labeled galactoglycoprotein	1260:1291	125I-labeled galactoglycoprotein	1260:1291	Further support of the relatedness of these molecules was obtained by immunoprecipitation of 125I-labeled galactoglycoprotein by monoclonal anti-CD43 antibodies.
1731338	2	37	theme	amino	421:425	arg1	content					458:464	a high content	451:464	a high content of serine, threonine, alanine, and proline with one N-linked and multiple O-linked glycans	451:555	This sequence represents a polypeptide chain of approximately 220 amino acid residues including a high content of serine, threonine, alanine, and proline with one N-linked and multiple O-linked glycans.
1731338	2	37	theme	amino	421:425	arg1	residues					432:439	approximately 220 amino acid residues	403:439	approximately 220 amino acid residues including a high content of serine, threonine, alanine, and proline with one N-linked and multiple O-linked glycans	403:555	This sequence represents a polypeptide chain of approximately 220 amino acid residues including a high content of serine, threonine, alanine, and proline with one N-linked and multiple O-linked glycans.
1731338	1	38	theme	glycopeptides	274:286	arg1	degradation					246:256	chemical degradation	237:256	chemical degradation of peptides and glycopeptides derived from digests of the protein with seven specific proteases	237:352	The amino acid sequence of galactoglycoprotein purified from human plasma was elucidated to 75% completeness by using chemical degradation of peptides and glycopeptides derived from digests of the protein with seven specific proteases.
1731338	2	39	theme	serine	469:474	arg1	content					458:464	a high content	451:464	a high content of serine, threonine, alanine, and proline with one N-linked and multiple O-linked glycans	451:555	This sequence represents a polypeptide chain of approximately 220 amino acid residues including a high content of serine, threonine, alanine, and proline with one N-linked and multiple O-linked glycans.
1731338	0	40	theme	human	23:27	arg1	galactoglycoprotein					36:54	human plasma galactoglycoprotein	23:54	human plasma galactoglycoprotein	23:54	Amino acid sequence of human plasma galactoglycoprotein: identity with the extracellular region of CD43 (sialophorin).
1731338	7	41	theme	relatedness	1190:1200	arg1	support					1175:1181	Further support	1167:1181	Further support of the relatedness of these molecules	1167:1219	Further support of the relatedness of these molecules was obtained by immunoprecipitation of 125I-labeled galactoglycoprotein by monoclonal anti-CD43 antibodies.
1731338	3	42	gly	O-glycosylation	702:716	arg2	sites					693:697	25 sites	690:697	25 sites of O-glycosylation	690:716	Comparison of peptide sequences from the native galactoglycoprotein and the deglycosylated derivative demonstrated the locations of 25 sites of O-glycosylation and three serine sites that are not glycosylated.
1731338	3	42	gly	O-glycosylation	702:716	arg2	sites					735:739	three serine sites	722:739	three serine sites	722:739	Comparison of peptide sequences from the native galactoglycoprotein and the deglycosylated derivative demonstrated the locations of 25 sites of O-glycosylation and three serine sites that are not glycosylated.
1731338	3	42	gly	O-glycosylation	702:716	arg2	O-glycosylation					702:716	O-glycosylation	702:716	O-glycosylation	702:716	Comparison of peptide sequences from the native galactoglycoprotein and the deglycosylated derivative demonstrated the locations of 25 sites of O-glycosylation and three serine sites that are not glycosylated.
1731338	3	43	theme	deglycosylated	634:647	arg1	derivative					649:658	the deglycosylated derivative	630:658	the deglycosylated derivative	630:658	Comparison of peptide sequences from the native galactoglycoprotein and the deglycosylated derivative demonstrated the locations of 25 sites of O-glycosylation and three serine sites that are not glycosylated.
1731338	0	44	theme	galactoglycoprotein	36:54	arg1	sequence					11:18	Amino acid sequence	0:18	Amino acid sequence of human plasma galactoglycoprotein: identity with the extracellular region of CD43 (sialophorin).	0:117	Amino acid sequence of human plasma galactoglycoprotein: identity with the extracellular region of CD43 (sialophorin).
1731338	8	45	theme	transmembrane	1505:1517	arg1	"					1540:1540	"	1540:1540	" known to be expressed on neutrophils, activated T lymphocytes, and platelets	1540:1617	The composition and properties of the molecules together with the known structure of the gene encoding CD43 suggest that galactoprotein is derived by proteolytic cleavage from transmembrane "hexasaccharide CD43," known to be expressed on neutrophils, activated T lymphocytes, and platelets.
1731338	8	45	theme	transmembrane	1505:1517	arg1	CD43					1535:1538	transmembrane "hexasaccharide CD43	1505:1538	transmembrane "hexasaccharide CD43	1505:1538	The composition and properties of the molecules together with the known structure of the gene encoding CD43 suggest that galactoprotein is derived by proteolytic cleavage from transmembrane "hexasaccharide CD43," known to be expressed on neutrophils, activated T lymphocytes, and platelets.
1731338	1	46	theme	75	211:212	arg1	%					213:213	%	213:213	%	213:213	The amino acid sequence of galactoglycoprotein purified from human plasma was elucidated to 75% completeness by using chemical degradation of peptides and glycopeptides derived from digests of the protein with seven specific proteases.
1731338	0	47	dep	sequence	11:18	arg1	identity					57:64	identity	57:64	Amino acid sequence of human plasma galactoglycoprotein: identity with the extracellular region of CD43 (sialophorin).	0:117	Amino acid sequence of human plasma galactoglycoprotein: identity with the extracellular region of CD43 (sialophorin).
1731338	8	48	theme	hexasaccharide	1520:1533	arg1	"					1540:1540	"	1540:1540	" known to be expressed on neutrophils, activated T lymphocytes, and platelets	1540:1617	The composition and properties of the molecules together with the known structure of the gene encoding CD43 suggest that galactoprotein is derived by proteolytic cleavage from transmembrane "hexasaccharide CD43," known to be expressed on neutrophils, activated T lymphocytes, and platelets.
1731338	8	48	theme	hexasaccharide	1520:1533	arg1	CD43					1535:1538	transmembrane "hexasaccharide CD43	1505:1538	transmembrane "hexasaccharide CD43	1505:1538	The composition and properties of the molecules together with the known structure of the gene encoding CD43 suggest that galactoprotein is derived by proteolytic cleavage from transmembrane "hexasaccharide CD43," known to be expressed on neutrophils, activated T lymphocytes, and platelets.
1731338	7	49	theme	125I-labeled	1260:1271	arg1	galactoglycoprotein					1273:1291	125I-labeled galactoglycoprotein	1260:1291	125I-labeled galactoglycoprotein	1260:1291	Further support of the relatedness of these molecules was obtained by immunoprecipitation of 125I-labeled galactoglycoprotein by monoclonal anti-CD43 antibodies.
1731338	6	50	theme	CD43	1134:1137	arg1	region					1092:1097	the N-terminal (extracellular) polypeptide region	1049:1097	the N-terminal (extracellular) polypeptide region of the blood-cell surface molecule CD43 (sialophorin, leukosialin)	1049:1164	A search of a protein data base revealed that the galactoglycoprotein polypeptide is identical to the N-terminal (extracellular) polypeptide region of the blood-cell surface molecule CD43 (sialophorin, leukosialin).
1731338	8	51	attach	derived	1468:1474	arg1	"					1540:1540	"	1540:1540	" known to be expressed on neutrophils, activated T lymphocytes, and platelets	1540:1617	The composition and properties of the molecules together with the known structure of the gene encoding CD43 suggest that galactoprotein is derived by proteolytic cleavage from transmembrane "hexasaccharide CD43," known to be expressed on neutrophils, activated T lymphocytes, and platelets.
1731338	8	51	attach	derived	1468:1474	arg1	CD43					1535:1538	transmembrane "hexasaccharide CD43	1505:1538	transmembrane "hexasaccharide CD43	1505:1538	The composition and properties of the molecules together with the known structure of the gene encoding CD43 suggest that galactoprotein is derived by proteolytic cleavage from transmembrane "hexasaccharide CD43," known to be expressed on neutrophils, activated T lymphocytes, and platelets.
1731338	8	51	attach	derived	1468:1474	arg2	galactoprotein					1450:1463	galactoprotein	1450:1463	galactoprotein	1450:1463	The composition and properties of the molecules together with the known structure of the gene encoding CD43 suggest that galactoprotein is derived by proteolytic cleavage from transmembrane "hexasaccharide CD43," known to be expressed on neutrophils, activated T lymphocytes, and platelets.
1731338	5	52	gly	galactoglycoprotein	897:915	arg1	galactoglycoprotein					897:915	galactoglycoprotein molecules	897:925	galactoglycoprotein molecules	897:925	C-terminal analysis revealed multiple C-terminal residues, suggesting that galactoglycoprotein molecules are of varying lengths.
1731338	2	53	link	N-linked	518:525	arg1	glycans					549:555	one N-linked and multiple O-linked glycans	514:555	one N-linked and multiple O-linked glycans	514:555	This sequence represents a polypeptide chain of approximately 220 amino acid residues including a high content of serine, threonine, alanine, and proline with one N-linked and multiple O-linked glycans.
1731338	3	54	from	derivative	649:658	arg1	galactoglycoprotein					606:624	the native galactoglycoprotein	595:624	the native galactoglycoprotein	595:624	Comparison of peptide sequences from the native galactoglycoprotein and the deglycosylated derivative demonstrated the locations of 25 sites of O-glycosylation and three serine sites that are not glycosylated.
1731338	0	55	with	identity	57:64	arg1	region					89:94	the extracellular region	71:94	the extracellular region of CD43 (sialophorin)	71:116	Amino acid sequence of human plasma galactoglycoprotein: identity with the extracellular region of CD43 (sialophorin).
1731338	1	56	attach	derived	288:294	arg2	peptides					261:268	peptides	261:268	peptides	261:268	The amino acid sequence of galactoglycoprotein purified from human plasma was elucidated to 75% completeness by using chemical degradation of peptides and glycopeptides derived from digests of the protein with seven specific proteases.
1731338	1	56	attach	derived	288:294	arg1	digests					301:307	digests	301:307	digests of the protein with seven specific proteases	301:352	The amino acid sequence of galactoglycoprotein purified from human plasma was elucidated to 75% completeness by using chemical degradation of peptides and glycopeptides derived from digests of the protein with seven specific proteases.
1731338	1	57	theme	galactoglycoprotein	146:164	arg1	sequence					134:141	The amino acid sequence	119:141	The amino acid sequence of galactoglycoprotein purified from human plasma	119:191	The amino acid sequence of galactoglycoprotein purified from human plasma was elucidated to 75% completeness by using chemical degradation of peptides and glycopeptides derived from digests of the protein with seven specific proteases.
1731338	3	58	gly	galactoglycoprotein	606:624	arg1	galactoglycoprotein					606:624	the native galactoglycoprotein	595:624	the native galactoglycoprotein	595:624	Comparison of peptide sequences from the native galactoglycoprotein and the deglycosylated derivative demonstrated the locations of 25 sites of O-glycosylation and three serine sites that are not glycosylated.
1731338	3	59	theme	serine	728:733	arg1	O-glycosylation					702:716	O-glycosylation	702:716	O-glycosylation	702:716	Comparison of peptide sequences from the native galactoglycoprotein and the deglycosylated derivative demonstrated the locations of 25 sites of O-glycosylation and three serine sites that are not glycosylated.
1731338	3	59	theme	serine	728:733	arg1	sites					735:739	three serine sites	722:739	three serine sites	722:739	Comparison of peptide sequences from the native galactoglycoprotein and the deglycosylated derivative demonstrated the locations of 25 sites of O-glycosylation and three serine sites that are not glycosylated.
1731338	6	60	gly	galactoglycoprotein	1001:1019	arg1	galactoglycoprotein					1001:1019	the galactoglycoprotein polypeptide	997:1031	the galactoglycoprotein polypeptide	997:1031	A search of a protein data base revealed that the galactoglycoprotein polypeptide is identical to the N-terminal (extracellular) polypeptide region of the blood-cell surface molecule CD43 (sialophorin, leukosialin).
1731338	5	61	theme	galactoglycoprotein	897:915	arg1	molecules					917:925	galactoglycoprotein molecules	897:925	galactoglycoprotein molecules	897:925	C-terminal analysis revealed multiple C-terminal residues, suggesting that galactoglycoprotein molecules are of varying lengths.
1731338	6	62	theme	galactoglycoprotein	1001:1019	arg1	identical					1036:1044	identical	1036:1044	identical	1036:1044	A search of a protein data base revealed that the galactoglycoprotein polypeptide is identical to the N-terminal (extracellular) polypeptide region of the blood-cell surface molecule CD43 (sialophorin, leukosialin).
1731338	6	62	theme	galactoglycoprotein	1001:1019	arg1	polypeptide					1021:1031	the galactoglycoprotein polypeptide	997:1031	the galactoglycoprotein polypeptide	997:1031	A search of a protein data base revealed that the galactoglycoprotein polypeptide is identical to the N-terminal (extracellular) polypeptide region of the blood-cell surface molecule CD43 (sialophorin, leukosialin).
1731338	8	63	theme	proteolytic	1479:1489	arg1	cleavage					1491:1498	proteolytic cleavage	1479:1498	proteolytic cleavage	1479:1498	The composition and properties of the molecules together with the known structure of the gene encoding CD43 suggest that galactoprotein is derived by proteolytic cleavage from transmembrane "hexasaccharide CD43," known to be expressed on neutrophils, activated T lymphocytes, and platelets.
1731338	5	64	theme	multiple	851:858	arg1	residues					871:878	multiple C-terminal residues	851:878	multiple C-terminal residues	851:878	C-terminal analysis revealed multiple C-terminal residues, suggesting that galactoglycoprotein molecules are of varying lengths.
1731338	3	65	theme	sequences	580:588	arg1	derivative					649:658	the deglycosylated derivative	630:658	the deglycosylated derivative	630:658	Comparison of peptide sequences from the native galactoglycoprotein and the deglycosylated derivative demonstrated the locations of 25 sites of O-glycosylation and three serine sites that are not glycosylated.
1731338	3	65	theme	sequences	580:588	arg1	Comparison					558:567	Comparison	558:567	Comparison of peptide sequences from the native galactoglycoprotein	558:624	Comparison of peptide sequences from the native galactoglycoprotein and the deglycosylated derivative demonstrated the locations of 25 sites of O-glycosylation and three serine sites that are not glycosylated.
1731338	6	66	theme	base	978:981	arg1	search					953:958	A search	951:958	A search of a protein data base	951:981	A search of a protein data base revealed that the galactoglycoprotein polypeptide is identical to the N-terminal (extracellular) polypeptide region of the blood-cell surface molecule CD43 (sialophorin, leukosialin).
1731338	6	67	theme	protein	965:971	arg1	base					978:981	a protein data base	963:981	a protein data base	963:981	A search of a protein data base revealed that the galactoglycoprotein polypeptide is identical to the N-terminal (extracellular) polypeptide region of the blood-cell surface molecule CD43 (sialophorin, leukosialin).
1731338	1	68	gly	glycopeptides	274:286	arg2	glycopeptides					274:286	glycopeptides	274:286	glycopeptides	274:286	The amino acid sequence of galactoglycoprotein purified from human plasma was elucidated to 75% completeness by using chemical degradation of peptides and glycopeptides derived from digests of the protein with seven specific proteases.
1731338	6	69	theme	extracellular	1065:1077	arg1	region					1092:1097	the N-terminal (extracellular) polypeptide region	1049:1097	the N-terminal (extracellular) polypeptide region of the blood-cell surface molecule CD43 (sialophorin, leukosialin)	1049:1164	A search of a protein data base revealed that the galactoglycoprotein polypeptide is identical to the N-terminal (extracellular) polypeptide region of the blood-cell surface molecule CD43 (sialophorin, leukosialin).
1731338	2	70	theme	O-linked	540:547	arg1	glycans					549:555	one N-linked and multiple O-linked glycans	514:555	one N-linked and multiple O-linked glycans	514:555	This sequence represents a polypeptide chain of approximately 220 amino acid residues including a high content of serine, threonine, alanine, and proline with one N-linked and multiple O-linked glycans.
1731338	8	71	theme	gene	1418:1421	arg1	structure					1401:1409	the known structure	1391:1409	The composition and properties of the molecules together with the known structure of the gene encoding CD43	1329:1435	The composition and properties of the molecules together with the known structure of the gene encoding CD43 suggest that galactoprotein is derived by proteolytic cleavage from transmembrane "hexasaccharide CD43," known to be expressed on neutrophils, activated T lymphocytes, and platelets.
1731338	1	72	theme	amino	123:127	arg1	sequence					134:141	The amino acid sequence	119:141	The amino acid sequence of galactoglycoprotein purified from human plasma	119:191	The amino acid sequence of galactoglycoprotein purified from human plasma was elucidated to 75% completeness by using chemical degradation of peptides and glycopeptides derived from digests of the protein with seven specific proteases.
1731338	6	73	theme	N-terminal	1053:1062	arg1	region					1092:1097	the N-terminal (extracellular) polypeptide region	1049:1097	the N-terminal (extracellular) polypeptide region of the blood-cell surface molecule CD43 (sialophorin, leukosialin)	1049:1164	A search of a protein data base revealed that the galactoglycoprotein polypeptide is identical to the N-terminal (extracellular) polypeptide region of the blood-cell surface molecule CD43 (sialophorin, leukosialin).
1731338	0	74	theme	extracellular	75:87	arg1	region					89:94	the extracellular region	71:94	the extracellular region of CD43 (sialophorin)	71:116	Amino acid sequence of human plasma galactoglycoprotein: identity with the extracellular region of CD43 (sialophorin).
1731338	5	75	theme	varying	934:940	arg1	lengths					942:948	varying lengths	934:948	varying lengths	934:948	C-terminal analysis revealed multiple C-terminal residues, suggesting that galactoglycoprotein molecules are of varying lengths.
1731338	8	76	theme	T	1590:1590	arg1	lymphocytes					1592:1602	activated T lymphocytes	1580:1602	activated T lymphocytes	1580:1602	The composition and properties of the molecules together with the known structure of the gene encoding CD43 suggest that galactoprotein is derived by proteolytic cleavage from transmembrane "hexasaccharide CD43," known to be expressed on neutrophils, activated T lymphocytes, and platelets.
1731338	1	77	theme	specific	335:342	arg1	proteases					344:352	seven specific proteases	329:352	seven specific proteases	329:352	The amino acid sequence of galactoglycoprotein purified from human plasma was elucidated to 75% completeness by using chemical degradation of peptides and glycopeptides derived from digests of the protein with seven specific proteases.
1731338	2	78	theme	proline	501:507	arg1	content					458:464	a high content	451:464	a high content of serine, threonine, alanine, and proline with one N-linked and multiple O-linked glycans	451:555	This sequence represents a polypeptide chain of approximately 220 amino acid residues including a high content of serine, threonine, alanine, and proline with one N-linked and multiple O-linked glycans.
1731338	6	79	theme	molecule	1125:1132	arg1	sialophorin					1140:1150	sialophorin	1140:1150	sialophorin	1140:1150	A search of a protein data base revealed that the galactoglycoprotein polypeptide is identical to the N-terminal (extracellular) polypeptide region of the blood-cell surface molecule CD43 (sialophorin, leukosialin).
1731338	6	79	theme	molecule	1125:1132	arg1	CD43					1134:1137	the blood-cell surface molecule CD43	1102:1137	the blood-cell surface molecule CD43 (sialophorin, leukosialin)	1102:1164	A search of a protein data base revealed that the galactoglycoprotein polypeptide is identical to the N-terminal (extracellular) polypeptide region of the blood-cell surface molecule CD43 (sialophorin, leukosialin).
1731338	4	80	theme	N	784:784	arg1	serine					814:819	serine	814:819	serine	814:819	The homogeneous N terminus was established as serine.
1731338	4	80	theme	N	784:784	arg1	terminus					786:793	The homogeneous N terminus	768:793	The homogeneous N terminus	768:793	The homogeneous N terminus was established as serine.
1731338	3	81	from	galactoglycoprotein	606:624	arg1	sequences					580:588	peptide sequences	572:588	peptide sequences from the native galactoglycoprotein	572:624	Comparison of peptide sequences from the native galactoglycoprotein and the deglycosylated derivative demonstrated the locations of 25 sites of O-glycosylation and three serine sites that are not glycosylated.
1731338	3	81	from	galactoglycoprotein	606:624	arg1	derivative					649:658	the deglycosylated derivative	630:658	the deglycosylated derivative	630:658	Comparison of peptide sequences from the native galactoglycoprotein and the deglycosylated derivative demonstrated the locations of 25 sites of O-glycosylation and three serine sites that are not glycosylated.
1731338	3	81	from	galactoglycoprotein	606:624	arg1	Comparison					558:567	Comparison	558:567	Comparison of peptide sequences from the native galactoglycoprotein	558:624	Comparison of peptide sequences from the native galactoglycoprotein and the deglycosylated derivative demonstrated the locations of 25 sites of O-glycosylation and three serine sites that are not glycosylated.
1731338	2	82	theme	polypeptide	382:392	arg1	chain					394:398	a polypeptide chain	380:398	a polypeptide chain of approximately 220 amino acid residues including a high content of serine, threonine, alanine, and proline with one N-linked and multiple O-linked glycans	380:555	This sequence represents a polypeptide chain of approximately 220 amino acid residues including a high content of serine, threonine, alanine, and proline with one N-linked and multiple O-linked glycans.
1731338	0	83	theme	acid	6:9	arg1	sequence					11:18	Amino acid sequence	0:18	Amino acid sequence of human plasma galactoglycoprotein: identity with the extracellular region of CD43 (sialophorin).	0:117	Amino acid sequence of human plasma galactoglycoprotein: identity with the extracellular region of CD43 (sialophorin).
1731338	6	84	theme	blood-cell	1106:1115	arg1	sialophorin					1140:1150	sialophorin	1140:1150	sialophorin	1140:1150	A search of a protein data base revealed that the galactoglycoprotein polypeptide is identical to the N-terminal (extracellular) polypeptide region of the blood-cell surface molecule CD43 (sialophorin, leukosialin).
1731338	6	84	theme	blood-cell	1106:1115	arg1	CD43					1134:1137	the blood-cell surface molecule CD43	1102:1137	the blood-cell surface molecule CD43 (sialophorin, leukosialin)	1102:1164	A search of a protein data base revealed that the galactoglycoprotein polypeptide is identical to the N-terminal (extracellular) polypeptide region of the blood-cell surface molecule CD43 (sialophorin, leukosialin).
1731338	2	85	theme	acid	427:430	arg1	content					458:464	a high content	451:464	a high content of serine, threonine, alanine, and proline with one N-linked and multiple O-linked glycans	451:555	This sequence represents a polypeptide chain of approximately 220 amino acid residues including a high content of serine, threonine, alanine, and proline with one N-linked and multiple O-linked glycans.
1731338	2	85	theme	acid	427:430	arg1	residues					432:439	approximately 220 amino acid residues	403:439	approximately 220 amino acid residues including a high content of serine, threonine, alanine, and proline with one N-linked and multiple O-linked glycans	403:555	This sequence represents a polypeptide chain of approximately 220 amino acid residues including a high content of serine, threonine, alanine, and proline with one N-linked and multiple O-linked glycans.
1731338	8	86	dep	together	1377:1384	arg1	with					1386:1389	with	1386:1389	with	1386:1389	The composition and properties of the molecules together with the known structure of the gene encoding CD43 suggest that galactoprotein is derived by proteolytic cleavage from transmembrane "hexasaccharide CD43," known to be expressed on neutrophils, activated T lymphocytes, and platelets.
1731338	0	87	theme	plasma	29:34	arg1	galactoglycoprotein					36:54	human plasma galactoglycoprotein	23:54	human plasma galactoglycoprotein	23:54	Amino acid sequence of human plasma galactoglycoprotein: identity with the extracellular region of CD43 (sialophorin).
1731338	6	88	theme	polypeptide	1080:1090	arg1	region					1092:1097	the N-terminal (extracellular) polypeptide region	1049:1097	the N-terminal (extracellular) polypeptide region of the blood-cell surface molecule CD43 (sialophorin, leukosialin)	1049:1164	A search of a protein data base revealed that the galactoglycoprotein polypeptide is identical to the N-terminal (extracellular) polypeptide region of the blood-cell surface molecule CD43 (sialophorin, leukosialin).
1731338	2	89	theme	high	453:456	arg1	content					458:464	a high content	451:464	a high content of serine, threonine, alanine, and proline with one N-linked and multiple O-linked glycans	451:555	This sequence represents a polypeptide chain of approximately 220 amino acid residues including a high content of serine, threonine, alanine, and proline with one N-linked and multiple O-linked glycans.
1731338	6	90	dep	sialophorin	1140:1150	arg1	leukosialin					1153:1163	leukosialin	1153:1163	leukosialin	1153:1163	A search of a protein data base revealed that the galactoglycoprotein polypeptide is identical to the N-terminal (extracellular) polypeptide region of the blood-cell surface molecule CD43 (sialophorin, leukosialin).
1731338	1	91	theme	%	213:213	arg1	completeness					215:226	75% completeness	211:226	75% completeness	211:226	The amino acid sequence of galactoglycoprotein purified from human plasma was elucidated to 75% completeness by using chemical degradation of peptides and glycopeptides derived from digests of the protein with seven specific proteases.
1731338	0	92	gly	galactoglycoprotein	36:54	arg1	galactoglycoprotein					36:54	human plasma galactoglycoprotein	23:54	human plasma galactoglycoprotein	23:54	Amino acid sequence of human plasma galactoglycoprotein: identity with the extracellular region of CD43 (sialophorin).
1731338	3	93	theme	O-glycosylation	702:716	arg1	O-glycosylation					702:716	O-glycosylation	702:716	O-glycosylation	702:716	Comparison of peptide sequences from the native galactoglycoprotein and the deglycosylated derivative demonstrated the locations of 25 sites of O-glycosylation and three serine sites that are not glycosylated.
1731338	3	93	theme	O-glycosylation	702:716	arg1	sites					693:697	25 sites	690:697	25 sites of O-glycosylation	690:716	Comparison of peptide sequences from the native galactoglycoprotein and the deglycosylated derivative demonstrated the locations of 25 sites of O-glycosylation and three serine sites that are not glycosylated.
1731338	3	93	theme	O-glycosylation	702:716	arg1	sites					735:739	three serine sites	722:739	three serine sites	722:739	Comparison of peptide sequences from the native galactoglycoprotein and the deglycosylated derivative demonstrated the locations of 25 sites of O-glycosylation and three serine sites that are not glycosylated.
1731338	7	94	theme	molecules	1211:1219	arg1	relatedness					1190:1200	the relatedness	1186:1200	the relatedness of these molecules	1186:1219	Further support of the relatedness of these molecules was obtained by immunoprecipitation of 125I-labeled galactoglycoprotein by monoclonal anti-CD43 antibodies.
16083266	2	0	theme	modifications	1200:1212	arg1	attachment					1167:1176	attachment	1167:1176	attachment of post-translational modifications as well as structural features from the accurate precursor mass	1167:1276	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	6	1	theme	on-line	2172:2178	arg1	LC-MS					2180:2184	on-line LC-MS	2172:2184	on-line LC-MS	2172:2184	In parallel, the linear ion trap provides MS(2) and MS(3) fragmentation spectra, with a scan speed sufficiently fast for on-line LC-MS.
16083266	2	2	theme	LC	788:789	arg1	separation					791:800	(ii) high-performance LC separation	766:800	(ii) high-performance LC separation of the resulting fragments	766:827	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	5	3	theme	typical	1846:1852	arg1	operation					1854:1862	typical operation	1846:1862	typical operation	1846:1862	In typical operation, the FTICR cell provides a survey scan with the high mass resolution (> 100 000) and accurate mass (<2 ppm) to characterize the higher charge-state precursor ions of the larger peptides.
16083266	0	4	theme	modifications-comprehensive	158:184	arg1	analysis					186:193	extensive post-translational modifications-comprehensive analysis	129:193	extensive post-translational modifications-comprehensive analysis of beta-casein and epidermal growth factor receptor (EGFR)	129:252	Extended Range Proteomic Analysis (ERPA): a new and sensitive LC-MS platform for high sequence coverage of complex proteins with extensive post-translational modifications-comprehensive analysis of beta-casein and epidermal growth factor receptor (EGFR).
16083266	8	5	theme	glycosylated	2417:2428	arg1	proteins					2430:2437	two heavily phosphorylated and glycosylated proteins	2386:2437	two heavily phosphorylated and glycosylated proteins	2386:2437	Using ERPA, we demonstrate >95% sequence coverage in the analysis of two heavily phosphorylated and glycosylated proteins, beta-casein at the 50 fmole level and the epidermal growth factor receptor (EGFR) at the 1 pmole level.
16083266	8	5	theme	glycosylated	2417:2428	arg1	beta-casein					2440:2450	beta-casein	2440:2450	beta-casein at the 50 fmole level	2440:2472	Using ERPA, we demonstrate >95% sequence coverage in the analysis of two heavily phosphorylated and glycosylated proteins, beta-casein at the 50 fmole level and the epidermal growth factor receptor (EGFR) at the 1 pmole level.
16083266	8	5	theme	glycosylated	2417:2428	arg1	receptor					2506:2513	the epidermal growth factor receptor	2478:2513	the epidermal growth factor receptor (EGFR) at the 1 pmole level	2478:2541	Using ERPA, we demonstrate >95% sequence coverage in the analysis of two heavily phosphorylated and glycosylated proteins, beta-casein at the 50 fmole level and the epidermal growth factor receptor (EGFR) at the 1 pmole level.
16083266	9	6	theme	comprehensive	2667:2679	arg1	characterization					2681:2696	comprehensive characterization	2667:2696	comprehensive characterization of large proteins, including posttranslational modifications	2667:2757	In summary, the combination of digestion strategy, high-performance separation, and the hybrid LTQ-FTMS instrument enables comprehensive characterization of large proteins, including posttranslational modifications.
16083266	5	7	theme	accurate	1949:1956	arg1	mass					1958:1961	accurate mass	1949:1961	accurate mass (<2 ppm)	1949:1970	In typical operation, the FTICR cell provides a survey scan with the high mass resolution (> 100 000) and accurate mass (<2 ppm) to characterize the higher charge-state precursor ions of the larger peptides.
16083266	5	7	theme	accurate	1949:1956	arg1	ppm					1967:1969	<2 ppm	1964:1969	<2 ppm	1964:1969	In typical operation, the FTICR cell provides a survey scan with the high mass resolution (> 100 000) and accurate mass (<2 ppm) to characterize the higher charge-state precursor ions of the larger peptides.
16083266	2	8	theme	structural	1225:1234	arg1	features					1236:1243	well as structural features	1217:1243	well as structural features from the accurate precursor mass	1217:1276	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	2	9	theme	protein	624:630	arg1	digestion					607:615	(i) digestion	603:615	(i) digestion of the protein	603:630	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	9	10	theme	separation	2612:2621	arg1	combination					2560:2570	the combination	2556:2570	the combination of digestion strategy, high-performance separation, and the hybrid LTQ-FTMS instrument	2556:2657	In summary, the combination of digestion strategy, high-performance separation, and the hybrid LTQ-FTMS instrument enables comprehensive characterization of large proteins, including posttranslational modifications.
16083266	2	11	theme	average	718:724	arg1	size					760:763	average a higher molecular weight peptide size	718:763	average a higher molecular weight peptide size	718:763	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	2	12	theme	methods	1092:1098	arg1	fragmentations					1308:1321	average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations	718:1321	average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations	718:1321	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	4	13	theme	arginine	1652:1659	arg1	residues					1672:1679	additional positively charged arginine and lysine residues	1622:1679	additional positively charged arginine and lysine residues in the Lys-C fragments	1622:1702	Furthermore, additional positively charged arginine and lysine residues in the Lys-C fragments enhance the sensitivity of the post-translationally modified phospho- and glycopeptides by at least 10-fold relative to tryptic fragments.
16083266	1	14	theme	post-translational	442:459	arg1	modifications					461:473	post-translational modifications	442:473	post-translational modifications in complex proteins	442:493	We have developed a new and sensitive LC-MS platform, Extended Range Proteomic Analysis (ERPA), which is able to achieve very high sequence coverage and comprehensive characterization of post-translational modifications in complex proteins.
16083266	7	15	theme	complicated	2296:2306	arg1	peptide					2308:2314	large or complicated peptide	2287:2314	large or complicated peptide	2287:2314	Together, these data provide multiple means to determine or enhance the confidence of assignment of large or complicated peptide.
16083266	0	16	theme	growth	224:229	arg1	EGFR					248:251	EGFR	248:251	EGFR	248:251	Extended Range Proteomic Analysis (ERPA): a new and sensitive LC-MS platform for high sequence coverage of complex proteins with extensive post-translational modifications-comprehensive analysis of beta-casein and epidermal growth factor receptor (EGFR).
16083266	0	16	theme	growth	224:229	arg1	receptor					238:245	epidermal growth factor receptor	214:245	epidermal growth factor receptor (EGFR)	214:252	Extended Range Proteomic Analysis (ERPA): a new and sensitive LC-MS platform for high sequence coverage of complex proteins with extensive post-translational modifications-comprehensive analysis of beta-casein and epidermal growth factor receptor (EGFR).
16083266	8	17	theme	50	2459:2460	arg1	fmole					2462:2466	fmole	2462:2466	fmole	2462:2466	Using ERPA, we demonstrate >95% sequence coverage in the analysis of two heavily phosphorylated and glycosylated proteins, beta-casein at the 50 fmole level and the epidermal growth factor receptor (EGFR) at the 1 pmole level.
16083266	3	18	theme	Lys-C	1348:1352	arg1	fragments					1354:1362	the Lys-C fragments	1344:1362	the Lys-C fragments	1344:1362	The LC retention of the Lys-C fragments is increased, relative to a tryptic digest, due to the generally greater hydrophobicity of the larger peptides, a result that is particularly important for peptides containing hydrophilic modifications such as glycosylation and phosphorylation.
16083266	6	19	theme	MS	2093:2094	arg1	spectra					2123:2129	MS(2) and MS(3) fragmentation spectra	2093:2129	MS(2) and MS(3) fragmentation spectra	2093:2129	In parallel, the linear ion trap provides MS(2) and MS(3) fragmentation spectra, with a scan speed sufficiently fast for on-line LC-MS.
16083266	9	20	theme	hybrid	2632:2637	arg1	instrument					2648:2657	the hybrid LTQ-FTMS instrument	2628:2657	the hybrid LTQ-FTMS instrument	2628:2657	In summary, the combination of digestion strategy, high-performance separation, and the hybrid LTQ-FTMS instrument enables comprehensive characterization of large proteins, including posttranslational modifications.
16083266	2	21	theme	weight	745:750	arg1	size					760:763	average a higher molecular weight peptide size	718:763	average a higher molecular weight peptide size	718:763	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	2	22	theme	peptide	1120:1126	arg1	structures					1128:1137	large peptide structures	1114:1137	large peptide structures	1114:1137	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	8	23	from	level	2468:2472	arg1	proteins					2430:2437	two heavily phosphorylated and glycosylated proteins	2386:2437	two heavily phosphorylated and glycosylated proteins	2386:2437	Using ERPA, we demonstrate >95% sequence coverage in the analysis of two heavily phosphorylated and glycosylated proteins, beta-casein at the 50 fmole level and the epidermal growth factor receptor (EGFR) at the 1 pmole level.
16083266	8	23	from	level	2468:2472	arg1	EGFR					2516:2519	EGFR	2516:2519	EGFR	2516:2519	Using ERPA, we demonstrate >95% sequence coverage in the analysis of two heavily phosphorylated and glycosylated proteins, beta-casein at the 50 fmole level and the epidermal growth factor receptor (EGFR) at the 1 pmole level.
16083266	8	23	from	level	2468:2472	arg1	beta-casein					2440:2450	beta-casein	2440:2450	beta-casein at the 50 fmole level	2440:2472	Using ERPA, we demonstrate >95% sequence coverage in the analysis of two heavily phosphorylated and glycosylated proteins, beta-casein at the 50 fmole level and the epidermal growth factor receptor (EGFR) at the 1 pmole level.
16083266	8	23	from	level	2468:2472	arg1	receptor					2506:2513	the epidermal growth factor receptor	2478:2513	the epidermal growth factor receptor (EGFR) at the 1 pmole level	2478:2541	Using ERPA, we demonstrate >95% sequence coverage in the analysis of two heavily phosphorylated and glycosylated proteins, beta-casein at the 50 fmole level and the epidermal growth factor receptor (EGFR) at the 1 pmole level.
16083266	0	24	theme	sequence	86:93	arg1	coverage					95:102	high sequence coverage	81:102	high sequence coverage of complex proteins with extensive post-translational modifications-comprehensive analysis of beta-casein and epidermal growth factor receptor (EGFR)	81:252	Extended Range Proteomic Analysis (ERPA): a new and sensitive LC-MS platform for high sequence coverage of complex proteins with extensive post-translational modifications-comprehensive analysis of beta-casein and epidermal growth factor receptor (EGFR).
16083266	9	25	theme	instrument	2648:2657	arg1	combination					2560:2570	the combination	2556:2570	the combination of digestion strategy, high-performance separation, and the hybrid LTQ-FTMS instrument	2556:2657	In summary, the combination of digestion strategy, high-performance separation, and the hybrid LTQ-FTMS instrument enables comprehensive characterization of large proteins, including posttranslational modifications.
16083266	2	26	theme	higher	728:733	arg1	weight					745:750	a higher molecular weight	726:750	average a higher molecular weight peptide size	718:763	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	4	27	theme	Lys-C	1688:1692	arg1	fragments					1694:1702	the Lys-C fragments	1684:1702	the Lys-C fragments	1684:1702	Furthermore, additional positively charged arginine and lysine residues in the Lys-C fragments enhance the sensitivity of the post-translationally modified phospho- and glycopeptides by at least 10-fold relative to tryptic fragments.
16083266	6	28	theme	linear	2068:2073	arg1	trap					2079:2082	the linear ion trap	2064:2082	the linear ion trap	2064:2082	In parallel, the linear ion trap provides MS(2) and MS(3) fragmentation spectra, with a scan speed sufficiently fast for on-line LC-MS.
16083266	2	29	theme	linear	930:935	arg1	trap					941:944	a linear ion trap	928:944	a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa	928:1062	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	5	30	theme	FTICR	1869:1873	arg1	cell					1875:1878	the FTICR cell	1865:1878	the FTICR cell	1865:1878	In typical operation, the FTICR cell provides a survey scan with the high mass resolution (> 100 000) and accurate mass (<2 ppm) to characterize the higher charge-state precursor ions of the larger peptides.
16083266	0	31	theme	proteins	115:122	arg1	coverage					95:102	high sequence coverage	81:102	high sequence coverage of complex proteins with extensive post-translational modifications-comprehensive analysis of beta-casein and epidermal growth factor receptor (EGFR)	81:252	Extended Range Proteomic Analysis (ERPA): a new and sensitive LC-MS platform for high sequence coverage of complex proteins with extensive post-translational modifications-comprehensive analysis of beta-casein and epidermal growth factor receptor (EGFR).
16083266	2	32	theme	proteomic	569:577	arg1	approaches					579:588	the top-down and bottom-up proteomic approaches	542:588	approaches	579:588	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	3	33	theme	fragments	1354:1362	arg1	retention					1331:1339	The LC retention	1324:1339	The LC retention of the Lys-C fragments	1324:1362	The LC retention of the Lys-C fragments is increased, relative to a tryptic digest, due to the generally greater hydrophobicity of the larger peptides, a result that is particularly important for peptides containing hydrophilic modifications such as glycosylation and phosphorylation.
16083266	0	34	theme	extensive	129:137	arg1	analysis					186:193	extensive post-translational modifications-comprehensive analysis	129:193	extensive post-translational modifications-comprehensive analysis of beta-casein and epidermal growth factor receptor (EGFR)	129:252	Extended Range Proteomic Analysis (ERPA): a new and sensitive LC-MS platform for high sequence coverage of complex proteins with extensive post-translational modifications-comprehensive analysis of beta-casein and epidermal growth factor receptor (EGFR).
16083266	1	35	theme	sequence	386:393	arg1	coverage					395:402	very high sequence coverage	376:402	very high sequence coverage	376:402	We have developed a new and sensitive LC-MS platform, Extended Range Proteomic Analysis (ERPA), which is able to achieve very high sequence coverage and comprehensive characterization of post-translational modifications in complex proteins.
16083266	2	36	theme	new	501:503	arg1	platform					505:512	This new platform	496:512	This new platform	496:512	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	9	37	theme	proteins	2707:2714	arg1	characterization					2681:2696	comprehensive characterization	2667:2696	comprehensive characterization of large proteins, including posttranslational modifications	2667:2757	In summary, the combination of digestion strategy, high-performance separation, and the hybrid LTQ-FTMS instrument enables comprehensive characterization of large proteins, including posttranslational modifications.
16083266	2	38	from	mass	1273:1276	arg1	features					1236:1243	well as structural features	1217:1243	well as structural features from the accurate precursor mass	1217:1276	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	1	39	from	coverage	395:402	arg1	proteins					486:493	complex proteins	478:493	complex proteins	478:493	We have developed a new and sensitive LC-MS platform, Extended Range Proteomic Analysis (ERPA), which is able to achieve very high sequence coverage and comprehensive characterization of post-translational modifications in complex proteins.
16083266	1	40	theme	Range	318:322	arg1	Analysis					334:341	Extended Range Proteomic Analysis	309:341	Extended Range Proteomic Analysis (ERPA)	309:348	We have developed a new and sensitive LC-MS platform, Extended Range Proteomic Analysis (ERPA), which is able to achieve very high sequence coverage and comprehensive characterization of post-translational modifications in complex proteins.
16083266	1	40	theme	Range	318:322	arg1	platform					299:306	a new and sensitive LC-MS platform	273:306	a new and sensitive LC-MS platform	273:306	We have developed a new and sensitive LC-MS platform, Extended Range Proteomic Analysis (ERPA), which is able to achieve very high sequence coverage and comprehensive characterization of post-translational modifications in complex proteins.
16083266	1	40	theme	Range	318:322	arg1	ERPA					344:347	ERPA	344:347	ERPA	344:347	We have developed a new and sensitive LC-MS platform, Extended Range Proteomic Analysis (ERPA), which is able to achieve very high sequence coverage and comprehensive characterization of post-translational modifications in complex proteins.
16083266	2	41	theme	hybrid	890:895	arg1	spectrometer					902:913	a hybrid mass spectrometer	888:913	a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa	888:1062	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	2	41	theme	hybrid	890:895	arg1	LTQ-FTMS					878:885	the LTQ-FTMS	874:885	the LTQ-FTMS	874:885	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	5	42	theme	peptides	2041:2048	arg1	ions					2022:2025	the higher charge-state precursor ions	1988:2025	the higher charge-state precursor ions of the larger peptides	1988:2048	In typical operation, the FTICR cell provides a survey scan with the high mass resolution (> 100 000) and accurate mass (<2 ppm) to characterize the higher charge-state precursor ions of the larger peptides.
16083266	4	43	theme	modified	1756:1763	arg1	phospho-					1765:1772	the post-translationally modified phospho-	1731:1772	the post-translationally modified phospho-	1731:1772	Furthermore, additional positively charged arginine and lysine residues in the Lys-C fragments enhance the sensitivity of the post-translationally modified phospho- and glycopeptides by at least 10-fold relative to tryptic fragments.
16083266	8	44	from	level	2537:2541	arg1	proteins					2430:2437	two heavily phosphorylated and glycosylated proteins	2386:2437	two heavily phosphorylated and glycosylated proteins	2386:2437	Using ERPA, we demonstrate >95% sequence coverage in the analysis of two heavily phosphorylated and glycosylated proteins, beta-casein at the 50 fmole level and the epidermal growth factor receptor (EGFR) at the 1 pmole level.
16083266	8	44	from	level	2537:2541	arg1	EGFR					2516:2519	EGFR	2516:2519	EGFR	2516:2519	Using ERPA, we demonstrate >95% sequence coverage in the analysis of two heavily phosphorylated and glycosylated proteins, beta-casein at the 50 fmole level and the epidermal growth factor receptor (EGFR) at the 1 pmole level.
16083266	8	44	from	level	2537:2541	arg1	beta-casein					2440:2450	beta-casein	2440:2450	beta-casein at the 50 fmole level	2440:2472	Using ERPA, we demonstrate >95% sequence coverage in the analysis of two heavily phosphorylated and glycosylated proteins, beta-casein at the 50 fmole level and the epidermal growth factor receptor (EGFR) at the 1 pmole level.
16083266	8	44	from	level	2537:2541	arg1	receptor					2506:2513	the epidermal growth factor receptor	2478:2513	the epidermal growth factor receptor (EGFR) at the 1 pmole level	2478:2541	Using ERPA, we demonstrate >95% sequence coverage in the analysis of two heavily phosphorylated and glycosylated proteins, beta-casein at the 50 fmole level and the epidermal growth factor receptor (EGFR) at the 1 pmole level.
16083266	9	45	theme	high-performance	2595:2610	arg1	separation					2612:2621	high-performance separation	2595:2621	high-performance separation	2595:2621	In summary, the combination of digestion strategy, high-performance separation, and the hybrid LTQ-FTMS instrument enables comprehensive characterization of large proteins, including posttranslational modifications.
16083266	5	46	theme	high	1912:1915	arg1	000					1940:1942	> 100 000	1934:1942	> 100 000	1934:1942	In typical operation, the FTICR cell provides a survey scan with the high mass resolution (> 100 000) and accurate mass (<2 ppm) to characterize the higher charge-state precursor ions of the larger peptides.
16083266	5	46	theme	high	1912:1915	arg1	resolution					1922:1931	the high mass resolution	1908:1931	the high mass resolution (> 100 000)	1908:1943	In typical operation, the FTICR cell provides a survey scan with the high mass resolution (> 100 000) and accurate mass (<2 ppm) to characterize the higher charge-state precursor ions of the larger peptides.
16083266	0	47	theme	LC-MS	62:66	arg1	platform					68:75	a new and sensitive LC-MS platform	42:75	Extended Range Proteomic Analysis (ERPA): a new and sensitive LC-MS platform for high sequence coverage of complex proteins with extensive post-translational modifications-comprehensive analysis of beta-casein and epidermal growth factor receptor (EGFR).	0:253	Extended Range Proteomic Analysis (ERPA): a new and sensitive LC-MS platform for high sequence coverage of complex proteins with extensive post-translational modifications-comprehensive analysis of beta-casein and epidermal growth factor receptor (EGFR).
16083266	7	48	theme	peptide	2308:2314	arg1	assignment					2273:2282	assignment	2273:2282	assignment of large or complicated peptide	2273:2314	Together, these data provide multiple means to determine or enhance the confidence of assignment of large or complicated peptide.
16083266	8	49	theme	growth	2492:2497	arg1	proteins					2430:2437	two heavily phosphorylated and glycosylated proteins	2386:2437	two heavily phosphorylated and glycosylated proteins	2386:2437	Using ERPA, we demonstrate >95% sequence coverage in the analysis of two heavily phosphorylated and glycosylated proteins, beta-casein at the 50 fmole level and the epidermal growth factor receptor (EGFR) at the 1 pmole level.
16083266	8	49	theme	growth	2492:2497	arg1	EGFR					2516:2519	EGFR	2516:2519	EGFR	2516:2519	Using ERPA, we demonstrate >95% sequence coverage in the analysis of two heavily phosphorylated and glycosylated proteins, beta-casein at the 50 fmole level and the epidermal growth factor receptor (EGFR) at the 1 pmole level.
16083266	8	49	theme	growth	2492:2497	arg1	receptor					2506:2513	the epidermal growth factor receptor	2478:2513	the epidermal growth factor receptor (EGFR) at the 1 pmole level	2478:2541	Using ERPA, we demonstrate >95% sequence coverage in the analysis of two heavily phosphorylated and glycosylated proteins, beta-casein at the 50 fmole level and the epidermal growth factor receptor (EGFR) at the 1 pmole level.
16083266	5	50	theme	>	1934:1934	arg1	000					1940:1942	> 100 000	1934:1942	> 100 000	1934:1942	In typical operation, the FTICR cell provides a survey scan with the high mass resolution (> 100 000) and accurate mass (<2 ppm) to characterize the higher charge-state precursor ions of the larger peptides.
16083266	5	50	theme	>	1934:1934	arg1	resolution					1922:1931	the high mass resolution	1908:1931	the high mass resolution (> 100 000)	1908:1943	In typical operation, the FTICR cell provides a survey scan with the high mass resolution (> 100 000) and accurate mass (<2 ppm) to characterize the higher charge-state precursor ions of the larger peptides.
16083266	8	51	theme	fmole	2462:2466	arg1	level					2468:2472	the 50 fmole level	2455:2472	the 50 fmole level	2455:2472	Using ERPA, we demonstrate >95% sequence coverage in the analysis of two heavily phosphorylated and glycosylated proteins, beta-casein at the 50 fmole level and the epidermal growth factor receptor (EGFR) at the 1 pmole level.
16083266	0	52	theme	Extended	0:7	arg1	ERPA					35:38	ERPA	35:38	ERPA	35:38	Extended Range Proteomic Analysis (ERPA): a new and sensitive LC-MS platform for high sequence coverage of complex proteins with extensive post-translational modifications-comprehensive analysis of beta-casein and epidermal growth factor receptor (EGFR).
16083266	0	52	theme	Extended	0:7	arg1	Analysis					25:32	Extended Range Proteomic Analysis	0:32	Extended Range Proteomic Analysis (ERPA): a new and sensitive LC-MS platform for high sequence coverage of complex proteins with extensive post-translational modifications-comprehensive analysis of beta-casein and epidermal growth factor receptor (EGFR).	0:253	Extended Range Proteomic Analysis (ERPA): a new and sensitive LC-MS platform for high sequence coverage of complex proteins with extensive post-translational modifications-comprehensive analysis of beta-casein and epidermal growth factor receptor (EGFR).
16083266	6	53	theme	scan	2139:2142	arg1	speed					2144:2148	a scan speed	2137:2148	a scan speed sufficiently fast for on-line LC-MS	2137:2184	In parallel, the linear ion trap provides MS(2) and MS(3) fragmentation spectra, with a scan speed sufficiently fast for on-line LC-MS.
16083266	9	54	theme	digestion	2575:2583	arg1	strategy					2585:2592	digestion strategy	2575:2592	digestion strategy	2575:2592	In summary, the combination of digestion strategy, high-performance separation, and the hybrid LTQ-FTMS instrument enables comprehensive characterization of large proteins, including posttranslational modifications.
16083266	2	55	theme	data	842:845	arg1	strategy					859:866	new data acquisition strategy	838:866	(iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2)	830:1296	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	0	56	theme	Proteomic	15:23	arg1	ERPA					35:38	ERPA	35:38	ERPA	35:38	Extended Range Proteomic Analysis (ERPA): a new and sensitive LC-MS platform for high sequence coverage of complex proteins with extensive post-translational modifications-comprehensive analysis of beta-casein and epidermal growth factor receptor (EGFR).
16083266	0	56	theme	Proteomic	15:23	arg1	Analysis					25:32	Extended Range Proteomic Analysis	0:32	Extended Range Proteomic Analysis (ERPA): a new and sensitive LC-MS platform for high sequence coverage of complex proteins with extensive post-translational modifications-comprehensive analysis of beta-casein and epidermal growth factor receptor (EGFR).	0:253	Extended Range Proteomic Analysis (ERPA): a new and sensitive LC-MS platform for high sequence coverage of complex proteins with extensive post-translational modifications-comprehensive analysis of beta-casein and epidermal growth factor receptor (EGFR).
16083266	2	57	theme	precursor	1263:1271	arg1	mass					1273:1276	the accurate precursor mass	1250:1276	the accurate precursor mass	1250:1276	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	8	58	theme	%	2347:2347	arg1	coverage					2358:2365	>95% sequence coverage	2344:2365	>95% sequence coverage in the analysis of two heavily phosphorylated and glycosylated proteins, beta-casein at the 50 fmole level and the epidermal growth factor receptor (EGFR) at the 1 pmole level	2344:2541	Using ERPA, we demonstrate >95% sequence coverage in the analysis of two heavily phosphorylated and glycosylated proteins, beta-casein at the 50 fmole level and the epidermal growth factor receptor (EGFR) at the 1 pmole level.
16083266	3	59	theme	due	1408:1410	arg1	digest					1400:1405	a tryptic digest	1390:1405	a tryptic digest	1390:1405	The LC retention of the Lys-C fragments is increased, relative to a tryptic digest, due to the generally greater hydrophobicity of the larger peptides, a result that is particularly important for peptides containing hydrophilic modifications such as glycosylation and phosphorylation.
16083266	4	60	theme	additional	1622:1631	arg1	residues					1672:1679	additional positively charged arginine and lysine residues	1622:1679	additional positively charged arginine and lysine residues in the Lys-C fragments	1622:1702	Furthermore, additional positively charged arginine and lysine residues in the Lys-C fragments enhance the sensitivity of the post-translationally modified phospho- and glycopeptides by at least 10-fold relative to tryptic fragments.
16083266	2	61	theme	FTICR	996:1000	arg1	cell					1003:1006	ion cyclotron resonance (FTICR) cell	971:1006	ion cyclotron resonance (FTICR) cell	971:1006	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	4	62	theme	tryptic	1824:1830	arg1	fragments					1832:1840	tryptic fragments	1824:1840	tryptic fragments	1824:1840	Furthermore, additional positively charged arginine and lysine residues in the Lys-C fragments enhance the sensitivity of the post-translationally modified phospho- and glycopeptides by at least 10-fold relative to tryptic fragments.
16083266	1	63	theme	LC-MS	293:297	arg1	Analysis					334:341	Extended Range Proteomic Analysis	309:341	Extended Range Proteomic Analysis (ERPA)	309:348	We have developed a new and sensitive LC-MS platform, Extended Range Proteomic Analysis (ERPA), which is able to achieve very high sequence coverage and comprehensive characterization of post-translational modifications in complex proteins.
16083266	1	63	theme	LC-MS	293:297	arg1	platform					299:306	a new and sensitive LC-MS platform	273:306	a new and sensitive LC-MS platform	273:306	We have developed a new and sensitive LC-MS platform, Extended Range Proteomic Analysis (ERPA), which is able to achieve very high sequence coverage and comprehensive characterization of post-translational modifications in complex proteins.
16083266	1	63	theme	LC-MS	293:297	arg1	able					360:363	able	360:363	able	360:363	We have developed a new and sensitive LC-MS platform, Extended Range Proteomic Analysis (ERPA), which is able to achieve very high sequence coverage and comprehensive characterization of post-translational modifications in complex proteins.
16083266	4	64	from	residues	1672:1679	arg1	fragments					1694:1702	the Lys-C fragments	1684:1702	the Lys-C fragments	1684:1702	Furthermore, additional positively charged arginine and lysine residues in the Lys-C fragments enhance the sensitivity of the post-translationally modified phospho- and glycopeptides by at least 10-fold relative to tryptic fragments.
16083266	2	65	theme	resonance	985:993	arg1	cell					1003:1006	ion cyclotron resonance (FTICR) cell	971:1006	ion cyclotron resonance (FTICR) cell	971:1006	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	2	66	theme	strategy	859:866	arg1	methods					1092:1098	a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods	836:1098	(iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2)	830:1296	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	1	67	from	modifications	461:473	arg1	proteins					486:493	complex proteins	478:493	complex proteins	478:493	We have developed a new and sensitive LC-MS platform, Extended Range Proteomic Analysis (ERPA), which is able to achieve very high sequence coverage and comprehensive characterization of post-translational modifications in complex proteins.
16083266	2	68	theme	resulting	809:817	arg1	fragments					819:827	the resulting fragments	805:827	the resulting fragments	805:827	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	4	69	gly	glycopeptides	1778:1790	arg2	glycopeptides					1778:1790	glycopeptides	1778:1790	glycopeptides	1778:1790	Furthermore, additional positively charged arginine and lysine residues in the Lys-C fragments enhance the sensitivity of the post-translationally modified phospho- and glycopeptides by at least 10-fold relative to tryptic fragments.
16083266	5	70	dep	survey	1891:1896	arg1	scan					1898:1901	scan	1898:1901	scan with the high mass resolution (> 100 000) and accurate mass (<2 ppm) to characterize the higher charge-state precursor ions of the larger peptides	1898:2048	In typical operation, the FTICR cell provides a survey scan with the high mass resolution (> 100 000) and accurate mass (<2 ppm) to characterize the higher charge-state precursor ions of the larger peptides.
16083266	2	71	from	range	1041:1045	arg1	analysis					1013:1020	analysis	1013:1020	analysis of peptides in the range of 0.5 to 10 kDa	1013:1062	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	3	72	theme	larger	1459:1464	arg1	peptides					1466:1473	the larger peptides	1455:1473	the larger peptides	1455:1473	The LC retention of the Lys-C fragments is increased, relative to a tryptic digest, due to the generally greater hydrophobicity of the larger peptides, a result that is particularly important for peptides containing hydrophilic modifications such as glycosylation and phosphorylation.
16083266	3	72	theme	larger	1459:1464	arg1	result					1478:1483	a result	1476:1483	a result that is particularly important for peptides containing hydrophilic modifications such as glycosylation and phosphorylation	1476:1606	The LC retention of the Lys-C fragments is increased, relative to a tryptic digest, due to the generally greater hydrophobicity of the larger peptides, a result that is particularly important for peptides containing hydrophilic modifications such as glycosylation and phosphorylation.
16083266	3	72	theme	larger	1459:1464	arg1	important					1506:1514	important	1506:1514	important	1506:1514	The LC retention of the Lys-C fragments is increased, relative to a tryptic digest, due to the generally greater hydrophobicity of the larger peptides, a result that is particularly important for peptides containing hydrophilic modifications such as glycosylation and phosphorylation.
16083266	2	73	theme	post-translational	1181:1198	arg1	modifications					1200:1212	post-translational modifications	1181:1212	post-translational modifications as well as structural features from the accurate precursor mass	1181:1276	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	9	74	theme	strategy	2585:2592	arg1	combination					2560:2570	the combination	2556:2570	the combination of digestion strategy, high-performance separation, and the hybrid LTQ-FTMS instrument	2556:2657	In summary, the combination of digestion strategy, high-performance separation, and the hybrid LTQ-FTMS instrument enables comprehensive characterization of large proteins, including posttranslational modifications.
16083266	2	75	theme	high-performance	771:786	arg1	separation					791:800	(ii) high-performance LC separation	766:800	(ii) high-performance LC separation of the resulting fragments	766:827	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	4	76	theme	charged	1644:1650	arg1	arginine					1652:1659	positively charged arginine	1633:1659	positively charged arginine	1633:1659	Furthermore, additional positively charged arginine and lysine residues in the Lys-C fragments enhance the sensitivity of the post-translationally modified phospho- and glycopeptides by at least 10-fold relative to tryptic fragments.
16083266	0	77	theme	beta-casein	198:208	arg1	analysis					186:193	extensive post-translational modifications-comprehensive analysis	129:193	extensive post-translational modifications-comprehensive analysis of beta-casein and epidermal growth factor receptor (EGFR)	129:252	Extended Range Proteomic Analysis (ERPA): a new and sensitive LC-MS platform for high sequence coverage of complex proteins with extensive post-translational modifications-comprehensive analysis of beta-casein and epidermal growth factor receptor (EGFR).
16083266	1	78	theme	comprehensive	408:420	arg1	characterization					422:437	comprehensive characterization	408:437	comprehensive characterization	408:437	We have developed a new and sensitive LC-MS platform, Extended Range Proteomic Analysis (ERPA), which is able to achieve very high sequence coverage and comprehensive characterization of post-translational modifications in complex proteins.
16083266	3	79	theme	hydrophilic	1540:1550	arg1	phosphorylation					1592:1606	phosphorylation	1592:1606	phosphorylation	1592:1606	The LC retention of the Lys-C fragments is increased, relative to a tryptic digest, due to the generally greater hydrophobicity of the larger peptides, a result that is particularly important for peptides containing hydrophilic modifications such as glycosylation and phosphorylation.
16083266	3	79	theme	hydrophilic	1540:1550	arg1	modifications					1552:1564	hydrophilic modifications	1540:1564	hydrophilic modifications such as glycosylation and phosphorylation	1540:1606	The LC retention of the Lys-C fragments is increased, relative to a tryptic digest, due to the generally greater hydrophobicity of the larger peptides, a result that is particularly important for peptides containing hydrophilic modifications such as glycosylation and phosphorylation.
16083266	3	79	theme	hydrophilic	1540:1550	arg1	glycosylation					1574:1586	glycosylation	1574:1586	glycosylation	1574:1586	The LC retention of the Lys-C fragments is increased, relative to a tryptic digest, due to the generally greater hydrophobicity of the larger peptides, a result that is particularly important for peptides containing hydrophilic modifications such as glycosylation and phosphorylation.
16083266	2	80	dep	separation	791:800	arg1	ii					767:768	ii	767:768	ii	767:768	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	5	81	theme	higher	1992:1997	arg1	ions					2022:2025	the higher charge-state precursor ions	1988:2025	the higher charge-state precursor ions of the larger peptides	1988:2048	In typical operation, the FTICR cell provides a survey scan with the high mass resolution (> 100 000) and accurate mass (<2 ppm) to characterize the higher charge-state precursor ions of the larger peptides.
16083266	0	82	theme	epidermal	214:222	arg1	EGFR					248:251	EGFR	248:251	EGFR	248:251	Extended Range Proteomic Analysis (ERPA): a new and sensitive LC-MS platform for high sequence coverage of complex proteins with extensive post-translational modifications-comprehensive analysis of beta-casein and epidermal growth factor receptor (EGFR).
16083266	0	82	theme	epidermal	214:222	arg1	receptor					238:245	epidermal growth factor receptor	214:245	epidermal growth factor receptor (EGFR)	214:252	Extended Range Proteomic Analysis (ERPA): a new and sensitive LC-MS platform for high sequence coverage of complex proteins with extensive post-translational modifications-comprehensive analysis of beta-casein and epidermal growth factor receptor (EGFR).
16083266	8	83	theme	proteins	2430:2437	arg1	analysis					2374:2381	the analysis	2370:2381	the analysis of two heavily phosphorylated and glycosylated proteins, beta-casein at the 50 fmole level and the epidermal growth factor receptor (EGFR) at the 1 pmole level	2370:2541	Using ERPA, we demonstrate >95% sequence coverage in the analysis of two heavily phosphorylated and glycosylated proteins, beta-casein at the 50 fmole level and the epidermal growth factor receptor (EGFR) at the 1 pmole level.
16083266	3	84	theme	peptides	1466:1473	arg1	hydrophobicity					1437:1450	the generally greater hydrophobicity	1415:1450	the generally greater hydrophobicity of the larger peptides, a result that is particularly important for peptides containing hydrophilic modifications such as glycosylation and phosphorylation	1415:1606	The LC retention of the Lys-C fragments is increased, relative to a tryptic digest, due to the generally greater hydrophobicity of the larger peptides, a result that is particularly important for peptides containing hydrophilic modifications such as glycosylation and phosphorylation.
16083266	5	85	theme	charge-state	1999:2010	arg1	ions					2022:2025	the higher charge-state precursor ions	1988:2025	the higher charge-state precursor ions of the larger peptides	1988:2048	In typical operation, the FTICR cell provides a survey scan with the high mass resolution (> 100 000) and accurate mass (<2 ppm) to characterize the higher charge-state precursor ions of the larger peptides.
16083266	8	86	gly	glycosylated	2417:2428	arg1	proteins					2430:2437	two heavily phosphorylated and glycosylated proteins	2386:2437	two heavily phosphorylated and glycosylated proteins	2386:2437	Using ERPA, we demonstrate >95% sequence coverage in the analysis of two heavily phosphorylated and glycosylated proteins, beta-casein at the 50 fmole level and the epidermal growth factor receptor (EGFR) at the 1 pmole level.
16083266	8	86	gly	glycosylated	2417:2428	arg1	beta-casein					2440:2450	beta-casein	2440:2450	beta-casein at the 50 fmole level	2440:2472	Using ERPA, we demonstrate >95% sequence coverage in the analysis of two heavily phosphorylated and glycosylated proteins, beta-casein at the 50 fmole level and the epidermal growth factor receptor (EGFR) at the 1 pmole level.
16083266	8	86	gly	glycosylated	2417:2428	arg1	receptor					2506:2513	the epidermal growth factor receptor	2478:2513	the epidermal growth factor receptor (EGFR) at the 1 pmole level	2478:2541	Using ERPA, we demonstrate >95% sequence coverage in the analysis of two heavily phosphorylated and glycosylated proteins, beta-casein at the 50 fmole level and the epidermal growth factor receptor (EGFR) at the 1 pmole level.
16083266	5	87	theme	precursor	2012:2020	arg1	ions					2022:2025	the higher charge-state precursor ions	1988:2025	the higher charge-state precursor ions of the larger peptides	1988:2048	In typical operation, the FTICR cell provides a survey scan with the high mass resolution (> 100 000) and accurate mass (<2 ppm) to characterize the higher charge-state precursor ions of the larger peptides.
16083266	2	88	theme	analysis	1083:1090	arg1	methods					1092:1098	a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods	836:1098	(iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2)	830:1296	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	0	89	theme	factor	231:236	arg1	EGFR					248:251	EGFR	248:251	EGFR	248:251	Extended Range Proteomic Analysis (ERPA): a new and sensitive LC-MS platform for high sequence coverage of complex proteins with extensive post-translational modifications-comprehensive analysis of beta-casein and epidermal growth factor receptor (EGFR).
16083266	0	89	theme	factor	231:236	arg1	receptor					238:245	epidermal growth factor receptor	214:245	epidermal growth factor receptor (EGFR)	214:252	Extended Range Proteomic Analysis (ERPA): a new and sensitive LC-MS platform for high sequence coverage of complex proteins with extensive post-translational modifications-comprehensive analysis of beta-casein and epidermal growth factor receptor (EGFR).
16083266	1	90	theme	modifications	461:473	arg1	characterization					422:437	comprehensive characterization	408:437	comprehensive characterization	408:437	We have developed a new and sensitive LC-MS platform, Extended Range Proteomic Analysis (ERPA), which is able to achieve very high sequence coverage and comprehensive characterization of post-translational modifications in complex proteins.
16083266	1	90	theme	modifications	461:473	arg1	coverage					395:402	very high sequence coverage	376:402	very high sequence coverage	376:402	We have developed a new and sensitive LC-MS platform, Extended Range Proteomic Analysis (ERPA), which is able to achieve very high sequence coverage and comprehensive characterization of post-translational modifications in complex proteins.
16083266	2	91	dep	10	1057:1058	arg1	to					1054:1055	to	1054:1055	to	1054:1055	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	2	92	dep	digestion	607:615	arg1	i					604:604	i	604:604	i	604:604	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	2	93	theme	peptide	752:758	arg1	size					760:763	average a higher molecular weight peptide size	718:763	average a higher molecular weight peptide size	718:763	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	2	94	theme	new	1074:1076	arg1	data					1078:1081	the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data	874:1081	the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data	874:1081	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	1	95	theme	complex	478:484	arg1	proteins					486:493	complex proteins	478:493	complex proteins	478:493	We have developed a new and sensitive LC-MS platform, Extended Range Proteomic Analysis (ERPA), which is able to achieve very high sequence coverage and comprehensive characterization of post-translational modifications in complex proteins.
16083266	2	96	theme	top-down	546:553	arg1	Lys-C					656:660	Lys-C	656:660	Lys-C	656:660	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	2	96	theme	top-down	546:553	arg1	advantages					523:532	advantages	523:532	advantages	523:532	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	3	97	theme	LC	1328:1329	arg1	retention					1331:1339	The LC retention	1324:1339	The LC retention of the Lys-C fragments	1324:1362	The LC retention of the Lys-C fragments is increased, relative to a tryptic digest, due to the generally greater hydrophobicity of the larger peptides, a result that is particularly important for peptides containing hydrophilic modifications such as glycosylation and phosphorylation.
16083266	2	98	theme	molecular	735:743	arg1	weight					745:750	a higher molecular weight	726:750	average a higher molecular weight peptide size	718:763	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	2	99	theme	large	1114:1118	arg1	structures					1128:1137	large peptide structures	1114:1137	large peptide structures	1114:1137	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	0	100	theme	complex	107:113	arg1	proteins					115:122	complex proteins	107:122	complex proteins	107:122	Extended Range Proteomic Analysis (ERPA): a new and sensitive LC-MS platform for high sequence coverage of complex proteins with extensive post-translational modifications-comprehensive analysis of beta-casein and epidermal growth factor receptor (EGFR).
16083266	2	101	theme	attachment	1167:1176	arg1	attachment					1167:1176	attachment	1167:1176	attachment of post-translational modifications as well as structural features from the accurate precursor mass	1167:1276	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	2	101	theme	attachment	1167:1176	arg1	site					1159:1162	the site	1155:1162	the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass	1155:1276	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	2	102	theme	ion	937:939	arg1	trap					941:944	a linear ion trap	928:944	a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa	928:1062	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	3	103	theme	greater	1429:1435	arg1	hydrophobicity					1437:1450	the generally greater hydrophobicity	1415:1450	the generally greater hydrophobicity of the larger peptides, a result that is particularly important for peptides containing hydrophilic modifications such as glycosylation and phosphorylation	1415:1606	The LC retention of the Lys-C fragments is increased, relative to a tryptic digest, due to the generally greater hydrophobicity of the larger peptides, a result that is particularly important for peptides containing hydrophilic modifications such as glycosylation and phosphorylation.
16083266	2	104	theme	approaches	579:588	arg1	Lys-C					656:660	Lys-C	656:660	Lys-C	656:660	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	2	104	theme	approaches	579:588	arg1	advantages					523:532	advantages	523:532	advantages	523:532	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	2	105	theme	ion	971:973	arg1	cell					1003:1006	ion cyclotron resonance (FTICR) cell	971:1006	ion cyclotron resonance (FTICR) cell	971:1006	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	2	106	theme	kDa	1060:1062	arg1	range					1041:1045	the range	1037:1045	the range of 0.5 to 10 kDa	1037:1062	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	0	107	theme	post-translational	139:156	arg1	analysis					186:193	extensive post-translational modifications-comprehensive analysis	129:193	extensive post-translational modifications-comprehensive analysis of beta-casein and epidermal growth factor receptor (EGFR)	129:252	Extended Range Proteomic Analysis (ERPA): a new and sensitive LC-MS platform for high sequence coverage of complex proteins with extensive post-translational modifications-comprehensive analysis of beta-casein and epidermal growth factor receptor (EGFR).
16083266	1	108	theme	high	381:384	arg1	coverage					395:402	very high sequence coverage	376:402	very high sequence coverage	376:402	We have developed a new and sensitive LC-MS platform, Extended Range Proteomic Analysis (ERPA), which is able to achieve very high sequence coverage and comprehensive characterization of post-translational modifications in complex proteins.
16083266	6	109	theme	fragmentation	2109:2121	arg1	spectra					2123:2129	MS(2) and MS(3) fragmentation spectra	2093:2129	MS(2) and MS(3) fragmentation spectra	2093:2129	In parallel, the linear ion trap provides MS(2) and MS(3) fragmentation spectra, with a scan speed sufficiently fast for on-line LC-MS.
16083266	2	110	theme	bottom-up	559:567	arg1	approaches					579:588	the top-down and bottom-up proteomic approaches	542:588	approaches	579:588	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	9	111	theme	large	2701:2705	arg1	modifications					2745:2757	posttranslational modifications	2727:2757	posttranslational modifications	2727:2757	In summary, the combination of digestion strategy, high-performance separation, and the hybrid LTQ-FTMS instrument enables comprehensive characterization of large proteins, including posttranslational modifications.
16083266	9	111	theme	large	2701:2705	arg1	proteins					2707:2714	large proteins	2701:2714	large proteins	2701:2714	In summary, the combination of digestion strategy, high-performance separation, and the hybrid LTQ-FTMS instrument enables comprehensive characterization of large proteins, including posttranslational modifications.
16083266	7	112	theme	large	2287:2291	arg1	peptide					2308:2314	large or complicated peptide	2287:2314	large or complicated peptide	2287:2314	Together, these data provide multiple means to determine or enhance the confidence of assignment of large or complicated peptide.
16083266	0	113	with	coverage	95:102	arg1	analysis					186:193	extensive post-translational modifications-comprehensive analysis	129:193	extensive post-translational modifications-comprehensive analysis of beta-casein and epidermal growth factor receptor (EGFR)	129:252	Extended Range Proteomic Analysis (ERPA): a new and sensitive LC-MS platform for high sequence coverage of complex proteins with extensive post-translational modifications-comprehensive analysis of beta-casein and epidermal growth factor receptor (EGFR).
16083266	0	114	theme	new	44:46	arg1	platform					68:75	a new and sensitive LC-MS platform	42:75	Extended Range Proteomic Analysis (ERPA): a new and sensitive LC-MS platform for high sequence coverage of complex proteins with extensive post-translational modifications-comprehensive analysis of beta-casein and epidermal growth factor receptor (EGFR).	0:253	Extended Range Proteomic Analysis (ERPA): a new and sensitive LC-MS platform for high sequence coverage of complex proteins with extensive post-translational modifications-comprehensive analysis of beta-casein and epidermal growth factor receptor (EGFR).
16083266	2	115	dep	methods	1092:1098	arg1	iii					831:833	iii	831:833	iii	831:833	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	2	116	theme	mass	897:900	arg1	spectrometer					902:913	a hybrid mass spectrometer	888:913	a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa	888:1062	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	2	116	theme	mass	897:900	arg1	LTQ-FTMS					878:885	the LTQ-FTMS	874:885	the LTQ-FTMS	874:885	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	5	117	theme	larger	2034:2039	arg1	peptides					2041:2048	the larger peptides	2030:2048	the larger peptides	2030:2048	In typical operation, the FTICR cell provides a survey scan with the high mass resolution (> 100 000) and accurate mass (<2 ppm) to characterize the higher charge-state precursor ions of the larger peptides.
16083266	2	118	theme	iv	1070:1071	arg1	data					1078:1081	the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data	874:1081	the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data	874:1081	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	4	119	theme	phospho-	1765:1772	arg1	sensitivity					1716:1726	the sensitivity	1712:1726	the sensitivity of the post-translationally modified phospho- and glycopeptides	1712:1790	Furthermore, additional positively charged arginine and lysine residues in the Lys-C fragments enhance the sensitivity of the post-translationally modified phospho- and glycopeptides by at least 10-fold relative to tryptic fragments.
16083266	0	120	theme	sensitive	52:60	arg1	platform					68:75	a new and sensitive LC-MS platform	42:75	Extended Range Proteomic Analysis (ERPA): a new and sensitive LC-MS platform for high sequence coverage of complex proteins with extensive post-translational modifications-comprehensive analysis of beta-casein and epidermal growth factor receptor (EGFR).	0:253	Extended Range Proteomic Analysis (ERPA): a new and sensitive LC-MS platform for high sequence coverage of complex proteins with extensive post-translational modifications-comprehensive analysis of beta-casein and epidermal growth factor receptor (EGFR).
16083266	1	121	theme	Proteomic	324:332	arg1	Analysis					334:341	Extended Range Proteomic Analysis	309:341	Extended Range Proteomic Analysis (ERPA)	309:348	We have developed a new and sensitive LC-MS platform, Extended Range Proteomic Analysis (ERPA), which is able to achieve very high sequence coverage and comprehensive characterization of post-translational modifications in complex proteins.
16083266	1	121	theme	Proteomic	324:332	arg1	platform					299:306	a new and sensitive LC-MS platform	273:306	a new and sensitive LC-MS platform	273:306	We have developed a new and sensitive LC-MS platform, Extended Range Proteomic Analysis (ERPA), which is able to achieve very high sequence coverage and comprehensive characterization of post-translational modifications in complex proteins.
16083266	1	121	theme	Proteomic	324:332	arg1	ERPA					344:347	ERPA	344:347	ERPA	344:347	We have developed a new and sensitive LC-MS platform, Extended Range Proteomic Analysis (ERPA), which is able to achieve very high sequence coverage and comprehensive characterization of post-translational modifications in complex proteins.
16083266	2	122	theme	MS	1302:1303	arg1	fragmentations					1308:1321	average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations	718:1321	average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations	718:1321	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	6	123	theme	MS	2103:2104	arg1	spectra					2123:2129	MS(2) and MS(3) fragmentation spectra	2093:2129	MS(2) and MS(3) fragmentation spectra	2093:2129	In parallel, the linear ion trap provides MS(2) and MS(3) fragmentation spectra, with a scan speed sufficiently fast for on-line LC-MS.
16083266	9	124	theme	posttranslational	2727:2743	arg1	modifications					2745:2757	posttranslational modifications	2727:2757	posttranslational modifications	2727:2757	In summary, the combination of digestion strategy, high-performance separation, and the hybrid LTQ-FTMS instrument enables comprehensive characterization of large proteins, including posttranslational modifications.
16083266	3	125	contain	containing	1529:1538	arg2	modifications					1552:1564	hydrophilic modifications	1540:1564	hydrophilic modifications such as glycosylation and phosphorylation	1540:1606	The LC retention of the Lys-C fragments is increased, relative to a tryptic digest, due to the generally greater hydrophobicity of the larger peptides, a result that is particularly important for peptides containing hydrophilic modifications such as glycosylation and phosphorylation.
16083266	3	125	contain	containing	1529:1538	arg1	peptides					1520:1527	peptides	1520:1527	peptides containing hydrophilic modifications such as glycosylation and phosphorylation	1520:1606	The LC retention of the Lys-C fragments is increased, relative to a tryptic digest, due to the generally greater hydrophobicity of the larger peptides, a result that is particularly important for peptides containing hydrophilic modifications such as glycosylation and phosphorylation.
16083266	3	125	contain	containing	1529:1538	arg2	phosphorylation					1592:1606	phosphorylation	1592:1606	phosphorylation	1592:1606	The LC retention of the Lys-C fragments is increased, relative to a tryptic digest, due to the generally greater hydrophobicity of the larger peptides, a result that is particularly important for peptides containing hydrophilic modifications such as glycosylation and phosphorylation.
16083266	3	125	contain	containing	1529:1538	arg2	glycosylation					1574:1586	glycosylation	1574:1586	glycosylation	1574:1586	The LC retention of the Lys-C fragments is increased, relative to a tryptic digest, due to the generally greater hydrophobicity of the larger peptides, a result that is particularly important for peptides containing hydrophilic modifications such as glycosylation and phosphorylation.
16083266	4	126	theme	glycopeptides	1778:1790	arg1	sensitivity					1716:1726	the sensitivity	1712:1726	the sensitivity of the post-translationally modified phospho- and glycopeptides	1712:1790	Furthermore, additional positively charged arginine and lysine residues in the Lys-C fragments enhance the sensitivity of the post-translationally modified phospho- and glycopeptides by at least 10-fold relative to tryptic fragments.
16083266	9	127	theme	LTQ-FTMS	2639:2646	arg1	instrument					2648:2657	the hybrid LTQ-FTMS instrument	2628:2657	the hybrid LTQ-FTMS instrument	2628:2657	In summary, the combination of digestion strategy, high-performance separation, and the hybrid LTQ-FTMS instrument enables comprehensive characterization of large proteins, including posttranslational modifications.
16083266	0	128	theme	receptor	238:245	arg1	analysis					186:193	extensive post-translational modifications-comprehensive analysis	129:193	extensive post-translational modifications-comprehensive analysis of beta-casein and epidermal growth factor receptor (EGFR)	129:252	Extended Range Proteomic Analysis (ERPA): a new and sensitive LC-MS platform for high sequence coverage of complex proteins with extensive post-translational modifications-comprehensive analysis of beta-casein and epidermal growth factor receptor (EGFR).
16083266	3	129	theme	tryptic	1392:1398	arg1	digest					1400:1405	a tryptic digest	1390:1405	a tryptic digest	1390:1405	The LC retention of the Lys-C fragments is increased, relative to a tryptic digest, due to the generally greater hydrophobicity of the larger peptides, a result that is particularly important for peptides containing hydrophilic modifications such as glycosylation and phosphorylation.
16083266	2	130	theme	peptides	1025:1032	arg1	analysis					1013:1020	analysis	1013:1020	analysis of peptides in the range of 0.5 to 10 kDa	1013:1062	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	2	131	dep	trap	941:944	arg1	transform					961:969	transform	961:969	transform	961:969	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	0	132	theme	high	81:84	arg1	coverage					95:102	high sequence coverage	81:102	high sequence coverage of complex proteins with extensive post-translational modifications-comprehensive analysis of beta-casein and epidermal growth factor receptor (EGFR)	81:252	Extended Range Proteomic Analysis (ERPA): a new and sensitive LC-MS platform for high sequence coverage of complex proteins with extensive post-translational modifications-comprehensive analysis of beta-casein and epidermal growth factor receptor (EGFR).
16083266	6	133	theme	fast	2163:2166	arg1	speed					2144:2148	a scan speed	2137:2148	a scan speed sufficiently fast for on-line LC-MS	2137:2184	In parallel, the linear ion trap provides MS(2) and MS(3) fragmentation spectra, with a scan speed sufficiently fast for on-line LC-MS.
16083266	5	134	theme	mass	1917:1920	arg1	000					1940:1942	> 100 000	1934:1942	> 100 000	1934:1942	In typical operation, the FTICR cell provides a survey scan with the high mass resolution (> 100 000) and accurate mass (<2 ppm) to characterize the higher charge-state precursor ions of the larger peptides.
16083266	5	134	theme	mass	1917:1920	arg1	resolution					1922:1931	the high mass resolution	1908:1931	the high mass resolution (> 100 000)	1908:1943	In typical operation, the FTICR cell provides a survey scan with the high mass resolution (> 100 000) and accurate mass (<2 ppm) to characterize the higher charge-state precursor ions of the larger peptides.
16083266	8	135	theme	epidermal	2482:2490	arg1	proteins					2430:2437	two heavily phosphorylated and glycosylated proteins	2386:2437	two heavily phosphorylated and glycosylated proteins	2386:2437	Using ERPA, we demonstrate >95% sequence coverage in the analysis of two heavily phosphorylated and glycosylated proteins, beta-casein at the 50 fmole level and the epidermal growth factor receptor (EGFR) at the 1 pmole level.
16083266	8	135	theme	epidermal	2482:2490	arg1	EGFR					2516:2519	EGFR	2516:2519	EGFR	2516:2519	Using ERPA, we demonstrate >95% sequence coverage in the analysis of two heavily phosphorylated and glycosylated proteins, beta-casein at the 50 fmole level and the epidermal growth factor receptor (EGFR) at the 1 pmole level.
16083266	8	135	theme	epidermal	2482:2490	arg1	receptor					2506:2513	the epidermal growth factor receptor	2478:2513	the epidermal growth factor receptor (EGFR) at the 1 pmole level	2478:2541	Using ERPA, we demonstrate >95% sequence coverage in the analysis of two heavily phosphorylated and glycosylated proteins, beta-casein at the 50 fmole level and the epidermal growth factor receptor (EGFR) at the 1 pmole level.
16083266	0	136	theme	Range	9:13	arg1	ERPA					35:38	ERPA	35:38	ERPA	35:38	Extended Range Proteomic Analysis (ERPA): a new and sensitive LC-MS platform for high sequence coverage of complex proteins with extensive post-translational modifications-comprehensive analysis of beta-casein and epidermal growth factor receptor (EGFR).
16083266	0	136	theme	Range	9:13	arg1	Analysis					25:32	Extended Range Proteomic Analysis	0:32	Extended Range Proteomic Analysis (ERPA): a new and sensitive LC-MS platform for high sequence coverage of complex proteins with extensive post-translational modifications-comprehensive analysis of beta-casein and epidermal growth factor receptor (EGFR).	0:253	Extended Range Proteomic Analysis (ERPA): a new and sensitive LC-MS platform for high sequence coverage of complex proteins with extensive post-translational modifications-comprehensive analysis of beta-casein and epidermal growth factor receptor (EGFR).
16083266	2	137	theme	acquisition	847:857	arg1	strategy					859:866	new data acquisition strategy	838:866	(iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2)	830:1296	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	8	138	theme	factor	2499:2504	arg1	proteins					2430:2437	two heavily phosphorylated and glycosylated proteins	2386:2437	two heavily phosphorylated and glycosylated proteins	2386:2437	Using ERPA, we demonstrate >95% sequence coverage in the analysis of two heavily phosphorylated and glycosylated proteins, beta-casein at the 50 fmole level and the epidermal growth factor receptor (EGFR) at the 1 pmole level.
16083266	8	138	theme	factor	2499:2504	arg1	EGFR					2516:2519	EGFR	2516:2519	EGFR	2516:2519	Using ERPA, we demonstrate >95% sequence coverage in the analysis of two heavily phosphorylated and glycosylated proteins, beta-casein at the 50 fmole level and the epidermal growth factor receptor (EGFR) at the 1 pmole level.
16083266	8	138	theme	factor	2499:2504	arg1	receptor					2506:2513	the epidermal growth factor receptor	2478:2513	the epidermal growth factor receptor (EGFR) at the 1 pmole level	2478:2541	Using ERPA, we demonstrate >95% sequence coverage in the analysis of two heavily phosphorylated and glycosylated proteins, beta-casein at the 50 fmole level and the epidermal growth factor receptor (EGFR) at the 1 pmole level.
16083266	8	139	theme	>95	2344:2346	arg1	%					2347:2347	%	2347:2347	%	2347:2347	Using ERPA, we demonstrate >95% sequence coverage in the analysis of two heavily phosphorylated and glycosylated proteins, beta-casein at the 50 fmole level and the epidermal growth factor receptor (EGFR) at the 1 pmole level.
16083266	8	140	from	coverage	2358:2365	arg1	analysis					2374:2381	the analysis	2370:2381	the analysis of two heavily phosphorylated and glycosylated proteins, beta-casein at the 50 fmole level and the epidermal growth factor receptor (EGFR) at the 1 pmole level	2370:2541	Using ERPA, we demonstrate >95% sequence coverage in the analysis of two heavily phosphorylated and glycosylated proteins, beta-casein at the 50 fmole level and the epidermal growth factor receptor (EGFR) at the 1 pmole level.
16083266	1	141	theme	new	275:277	arg1	Analysis					334:341	Extended Range Proteomic Analysis	309:341	Extended Range Proteomic Analysis (ERPA)	309:348	We have developed a new and sensitive LC-MS platform, Extended Range Proteomic Analysis (ERPA), which is able to achieve very high sequence coverage and comprehensive characterization of post-translational modifications in complex proteins.
16083266	1	141	theme	new	275:277	arg1	platform					299:306	a new and sensitive LC-MS platform	273:306	a new and sensitive LC-MS platform	273:306	We have developed a new and sensitive LC-MS platform, Extended Range Proteomic Analysis (ERPA), which is able to achieve very high sequence coverage and comprehensive characterization of post-translational modifications in complex proteins.
16083266	1	141	theme	new	275:277	arg1	able					360:363	able	360:363	able	360:363	We have developed a new and sensitive LC-MS platform, Extended Range Proteomic Analysis (ERPA), which is able to achieve very high sequence coverage and comprehensive characterization of post-translational modifications in complex proteins.
16083266	2	142	theme	new	838:840	arg1	data					842:845	new data	838:845	(iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2)	830:1296	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	7	143	theme	assignment	2273:2282	arg1	confidence					2259:2268	the confidence	2255:2268	the confidence of assignment of large or complicated peptide	2255:2314	Together, these data provide multiple means to determine or enhance the confidence of assignment of large or complicated peptide.
16083266	8	144	theme	sequence	2349:2356	arg1	coverage					2358:2365	>95% sequence coverage	2344:2365	>95% sequence coverage in the analysis of two heavily phosphorylated and glycosylated proteins, beta-casein at the 50 fmole level and the epidermal growth factor receptor (EGFR) at the 1 pmole level	2344:2541	Using ERPA, we demonstrate >95% sequence coverage in the analysis of two heavily phosphorylated and glycosylated proteins, beta-casein at the 50 fmole level and the epidermal growth factor receptor (EGFR) at the 1 pmole level.
16083266	1	145	theme	sensitive	283:291	arg1	Analysis					334:341	Extended Range Proteomic Analysis	309:341	Extended Range Proteomic Analysis (ERPA)	309:348	We have developed a new and sensitive LC-MS platform, Extended Range Proteomic Analysis (ERPA), which is able to achieve very high sequence coverage and comprehensive characterization of post-translational modifications in complex proteins.
16083266	1	145	theme	sensitive	283:291	arg1	platform					299:306	a new and sensitive LC-MS platform	273:306	a new and sensitive LC-MS platform	273:306	We have developed a new and sensitive LC-MS platform, Extended Range Proteomic Analysis (ERPA), which is able to achieve very high sequence coverage and comprehensive characterization of post-translational modifications in complex proteins.
16083266	1	145	theme	sensitive	283:291	arg1	able					360:363	able	360:363	able	360:363	We have developed a new and sensitive LC-MS platform, Extended Range Proteomic Analysis (ERPA), which is able to achieve very high sequence coverage and comprehensive characterization of post-translational modifications in complex proteins.
16083266	2	146	theme	accurate	1254:1261	arg1	mass					1273:1276	the accurate precursor mass	1250:1276	the accurate precursor mass	1250:1276	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	2	147	theme	size	760:763	arg1	fragmentations					1308:1321	average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations	718:1321	average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations	718:1321	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	1	148	from	proteins	486:493	arg1	characterization					422:437	comprehensive characterization	408:437	comprehensive characterization	408:437	We have developed a new and sensitive LC-MS platform, Extended Range Proteomic Analysis (ERPA), which is able to achieve very high sequence coverage and comprehensive characterization of post-translational modifications in complex proteins.
16083266	1	148	from	proteins	486:493	arg1	coverage					395:402	very high sequence coverage	376:402	very high sequence coverage	376:402	We have developed a new and sensitive LC-MS platform, Extended Range Proteomic Analysis (ERPA), which is able to achieve very high sequence coverage and comprehensive characterization of post-translational modifications in complex proteins.
16083266	2	149	theme	LTQ-FTMS	878:885	arg1	data					1078:1081	the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data	874:1081	the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data	874:1081	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	6	150	theme	ion	2075:2077	arg1	trap					2079:2082	the linear ion trap	2064:2082	the linear ion trap	2064:2082	In parallel, the linear ion trap provides MS(2) and MS(3) fragmentation spectra, with a scan speed sufficiently fast for on-line LC-MS.
16083266	7	151	theme	multiple	2216:2223	arg1	means					2225:2229	multiple means	2216:2229	multiple means to determine or enhance the confidence of assignment of large or complicated peptide	2216:2314	Together, these data provide multiple means to determine or enhance the confidence of assignment of large or complicated peptide.
16083266	2	152	theme	cyclotron	975:983	arg1	cell					1003:1006	ion cyclotron resonance (FTICR) cell	971:1006	ion cyclotron resonance (FTICR) cell	971:1006	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	1	153	theme	Extended	309:316	arg1	Analysis					334:341	Extended Range Proteomic Analysis	309:341	Extended Range Proteomic Analysis (ERPA)	309:348	We have developed a new and sensitive LC-MS platform, Extended Range Proteomic Analysis (ERPA), which is able to achieve very high sequence coverage and comprehensive characterization of post-translational modifications in complex proteins.
16083266	1	153	theme	Extended	309:316	arg1	platform					299:306	a new and sensitive LC-MS platform	273:306	a new and sensitive LC-MS platform	273:306	We have developed a new and sensitive LC-MS platform, Extended Range Proteomic Analysis (ERPA), which is able to achieve very high sequence coverage and comprehensive characterization of post-translational modifications in complex proteins.
16083266	1	153	theme	Extended	309:316	arg1	ERPA					344:347	ERPA	344:347	ERPA	344:347	We have developed a new and sensitive LC-MS platform, Extended Range Proteomic Analysis (ERPA), which is able to achieve very high sequence coverage and comprehensive characterization of post-translational modifications in complex proteins.
16083266	0	154	dep	Analysis	25:32	arg1	platform					68:75	a new and sensitive LC-MS platform	42:75	Extended Range Proteomic Analysis (ERPA): a new and sensitive LC-MS platform for high sequence coverage of complex proteins with extensive post-translational modifications-comprehensive analysis of beta-casein and epidermal growth factor receptor (EGFR).	0:253	Extended Range Proteomic Analysis (ERPA): a new and sensitive LC-MS platform for high sequence coverage of complex proteins with extensive post-translational modifications-comprehensive analysis of beta-casein and epidermal growth factor receptor (EGFR).
16083266	2	155	from	analysis	1013:1020	arg1	range					1041:1045	the range	1037:1045	the range of 0.5 to 10 kDa	1037:1062	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	2	156	theme	fragments	819:827	arg1	size					760:763	average a higher molecular weight peptide size	718:763	average a higher molecular weight peptide size	718:763	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	2	156	theme	fragments	819:827	arg1	methods					1092:1098	a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods	836:1098	(iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2)	830:1296	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	2	156	theme	fragments	819:827	arg1	MS					1302:1303	MS(3)	1302:1306	MS(3)	1302:1306	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	2	156	theme	fragments	819:827	arg1	separation					791:800	(ii) high-performance LC separation	766:800	(ii) high-performance LC separation of the resulting fragments	766:827	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	8	157	theme	pmole	2531:2535	arg1	level					2537:2541	the 1 pmole level	2525:2541	the 1 pmole level	2525:2541	Using ERPA, we demonstrate >95% sequence coverage in the analysis of two heavily phosphorylated and glycosylated proteins, beta-casein at the 50 fmole level and the epidermal growth factor receptor (EGFR) at the 1 pmole level.
16083266	2	158	theme	separation	791:800	arg1	fragmentations					1308:1321	average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations	718:1321	average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations	718:1321	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	1	159	from	characterization	422:437	arg1	proteins					486:493	complex proteins	478:493	complex proteins	478:493	We have developed a new and sensitive LC-MS platform, Extended Range Proteomic Analysis (ERPA), which is able to achieve very high sequence coverage and comprehensive characterization of post-translational modifications in complex proteins.
16083266	2	160	from	peptides	1025:1032	arg1	range					1041:1045	the range	1037:1045	the range of 0.5 to 10 kDa	1037:1062	This new platform provides advantages of both the top-down and bottom-up proteomic approaches by combining (i) digestion of the protein with an enzyme, such as Lys-C, which cuts less frequently than trypsin, leading to on average a higher molecular weight peptide size, (ii) high-performance LC separation of the resulting fragments, (iii) a new data acquisition strategy using the LTQ-FTMS, a hybrid mass spectrometer that couples a linear ion trap with a Fourier transform ion cyclotron resonance (FTICR) cell, for analysis of peptides in the range of 0.5 to 10 kDa, and (iv) new data analysis methods for assigning large peptide structures and determining the site of attachment of post-translational modifications as well as structural features from the accurate precursor mass together with MS(2) and MS(3) fragmentations.
16083266	4	161	theme	lysine	1665:1670	arg1	residues					1672:1679	additional positively charged arginine and lysine residues	1622:1679	additional positively charged arginine and lysine residues in the Lys-C fragments	1622:1702	Furthermore, additional positively charged arginine and lysine residues in the Lys-C fragments enhance the sensitivity of the post-translationally modified phospho- and glycopeptides by at least 10-fold relative to tryptic fragments.
16083266	8	162	theme	phosphorylated	2398:2411	arg1	proteins					2430:2437	two heavily phosphorylated and glycosylated proteins	2386:2437	two heavily phosphorylated and glycosylated proteins	2386:2437	Using ERPA, we demonstrate >95% sequence coverage in the analysis of two heavily phosphorylated and glycosylated proteins, beta-casein at the 50 fmole level and the epidermal growth factor receptor (EGFR) at the 1 pmole level.
16083266	8	162	theme	phosphorylated	2398:2411	arg1	beta-casein					2440:2450	beta-casein	2440:2450	beta-casein at the 50 fmole level	2440:2472	Using ERPA, we demonstrate >95% sequence coverage in the analysis of two heavily phosphorylated and glycosylated proteins, beta-casein at the 50 fmole level and the epidermal growth factor receptor (EGFR) at the 1 pmole level.
16083266	8	162	theme	phosphorylated	2398:2411	arg1	receptor					2506:2513	the epidermal growth factor receptor	2478:2513	the epidermal growth factor receptor (EGFR) at the 1 pmole level	2478:2541	Using ERPA, we demonstrate >95% sequence coverage in the analysis of two heavily phosphorylated and glycosylated proteins, beta-casein at the 50 fmole level and the epidermal growth factor receptor (EGFR) at the 1 pmole level.
6619128	6	0	with	identical	661:669	arg1	structure					680:688	the structure	676:688	the structure of the predominant oligosaccharide in the hinge region of human IgA1 myeloma proteins	676:774	Approximately 50% of these molecules have the structure Gal beta 1 leads to 3 GalNAc which is identical with the structure of the predominant oligosaccharide in the hinge region of human IgA1 myeloma proteins (Baenziger, J. U., and Kornfeld, S. (1974) J. Biol.
6619128	6	1	dep	identical	661:669	arg1	1974					813:816	1974	813:816	1974	813:816	Approximately 50% of these molecules have the structure Gal beta 1 leads to 3 GalNAc which is identical with the structure of the predominant oligosaccharide in the hinge region of human IgA1 myeloma proteins (Baenziger, J. U., and Kornfeld, S. (1974) J. Biol.
6619128	6	1	dep	identical	661:669	arg1	Baenziger					777:785	Baenziger	777:785	Baenziger	777:785	Approximately 50% of these molecules have the structure Gal beta 1 leads to 3 GalNAc which is identical with the structure of the predominant oligosaccharide in the hinge region of human IgA1 myeloma proteins (Baenziger, J. U., and Kornfeld, S. (1974) J. Biol.
6619128	6	1	dep	identical	661:669	arg1	U.					791:792	U.	791:792	U.	791:792	Approximately 50% of these molecules have the structure Gal beta 1 leads to 3 GalNAc which is identical with the structure of the predominant oligosaccharide in the hinge region of human IgA1 myeloma proteins (Baenziger, J. U., and Kornfeld, S. (1974) J. Biol.
6619128	6	1	dep	identical	661:669	arg1	S					809:809	S	809:809	S	809:809	Approximately 50% of these molecules have the structure Gal beta 1 leads to 3 GalNAc which is identical with the structure of the predominant oligosaccharide in the hinge region of human IgA1 myeloma proteins (Baenziger, J. U., and Kornfeld, S. (1974) J. Biol.
6619128	10	2	theme	other	1236:1240	arg1	chains					1269:1274	other human immunoglobulin heavy chains	1236:1274	other human immunoglobulin heavy chains	1236:1274	The sialylated molecules have not been encountered previously on other human immunoglobulin heavy chains.
6619128	6	3	theme	oligosaccharide	709:723	arg1	structure					680:688	the structure	676:688	the structure of the predominant oligosaccharide in the hinge region of human IgA1 myeloma proteins	676:774	Approximately 50% of these molecules have the structure Gal beta 1 leads to 3 GalNAc which is identical with the structure of the predominant oligosaccharide in the hinge region of human IgA1 myeloma proteins (Baenziger, J. U., and Kornfeld, S. (1974) J. Biol.
6619128	12	4	theme	IgD	1450:1452	arg1	hinge					1454:1458	the IgD hinge	1446:1458	the IgD hinge	1446:1458	Examination of oligosaccharides isolated from different subregions of the IgD hinge indicated that a specific distribution of the sialylated structures among the glycosylated amino acids of the hinge region is not likely.
6619128	5	5	contain	bear	520:523	arg1	residue					498:504	one serine residue	487:504	one serine residue	487:504	Three or four threonine residues and one serine residue in the region bear O-glycosidically linked oligosaccharides.
6619128	5	5	contain	bear	520:523	arg2	oligosaccharides					549:564	O-glycosidically linked oligosaccharides	525:564	O-glycosidically linked oligosaccharides	525:564	Three or four threonine residues and one serine residue in the region bear O-glycosidically linked oligosaccharides.
6619128	5	5	contain	bear	520:523	arg1	residues					474:481	Three or four threonine residues	450:481	Three or four threonine residues	450:481	Three or four threonine residues and one serine residue in the region bear O-glycosidically linked oligosaccharides.
6619128	5	6	theme	linked	542:547	arg1	oligosaccharides					549:564	O-glycosidically linked oligosaccharides	525:564	O-glycosidically linked oligosaccharides	525:564	Three or four threonine residues and one serine residue in the region bear O-glycosidically linked oligosaccharides.
6619128	12	7	gly	sialylated	1506:1515	arg1	structures					1517:1526	the sialylated structures	1502:1526	the sialylated structures	1502:1526	Examination of oligosaccharides isolated from different subregions of the IgD hinge indicated that a specific distribution of the sialylated structures among the glycosylated amino acids of the hinge region is not likely.
6619128	6	8	contain	have	604:607	arg1	%					583:583	Approximately 50%	567:583	Approximately 50% of these molecules	567:602	Approximately 50% of these molecules have the structure Gal beta 1 leads to 3 GalNAc which is identical with the structure of the predominant oligosaccharide in the hinge region of human IgA1 myeloma proteins (Baenziger, J. U., and Kornfeld, S. (1974) J. Biol.
6619128	6	8	contain	have	604:607	arg2	structure					613:621	the structure	609:621	the structure Gal beta 1 leads to 3 GalNAc which is identical with the structure of the predominant oligosaccharide in the hinge region of human IgA1 myeloma proteins (Baenziger, J. U., and Kornfeld, S. (1974) J. Biol	609:825	Approximately 50% of these molecules have the structure Gal beta 1 leads to 3 GalNAc which is identical with the structure of the predominant oligosaccharide in the hinge region of human IgA1 myeloma proteins (Baenziger, J. U., and Kornfeld, S. (1974) J. Biol.
6619128	6	8	contain	have	604:607	arg1	molecules					594:602	these molecules	588:602	these molecules	588:602	Approximately 50% of these molecules have the structure Gal beta 1 leads to 3 GalNAc which is identical with the structure of the predominant oligosaccharide in the hinge region of human IgA1 myeloma proteins (Baenziger, J. U., and Kornfeld, S. (1974) J. Biol.
6619128	0	9	link	linked	35:40	arg1	oligosaccharides					42:57	the O-glycosidically linked oligosaccharides	14:57	the O-glycosidically linked oligosaccharides of human IgD	14:70	Structures of the O-glycosidically linked oligosaccharides of human IgD.
6619128	10	10	theme	immunoglobulin	1248:1261	arg1	chains					1269:1274	other human immunoglobulin heavy chains	1236:1274	other human immunoglobulin heavy chains	1236:1274	The sialylated molecules have not been encountered previously on other human immunoglobulin heavy chains.
6619128	9	11	theme	Gal	1023:1025	arg1	beta					1027:1030	Gal beta 1	1023:1032	Gal beta 1	1023:1032	The remainder of the oligosaccharides contain 1 or 2 residues of N-acetylneuraminic acid and have the structures NeuAc alpha 2 leads to 3Gal beta 1 leads to 3GalNAc (30%), Gal beta 1 leads to (NeuAc alpha 2 leads to 6)GalNAc (12%), and NeuAc alpha 2 leads to 3Gal beta 1 leads to 3(NeuAc alpha 2 leads to 6)GalNAc (8%).
6619128	5	12	from	residues	474:481	arg1	region					513:518	the region	509:518	the region	509:518	Three or four threonine residues and one serine residue in the region bear O-glycosidically linked oligosaccharides.
6619128	5	13	theme	threonine	464:472	arg1	residues					474:481	Three or four threonine residues	450:481	Three or four threonine residues	450:481	Three or four threonine residues and one serine residue in the region bear O-glycosidically linked oligosaccharides.
6619128	5	14	from	residue	498:504	arg1	region					513:518	the region	509:518	the region	509:518	Three or four threonine residues and one serine residue in the region bear O-glycosidically linked oligosaccharides.
6619128	3	15	theme	present	220:226	arg1	oligosaccharides					203:218	the oligosaccharides	199:218	the oligosaccharides present at the 3 asparagine glycosylation sites of a human IgD myeloma protein	199:297	258, 11546-11556), the structures of the oligosaccharides present at the 3 asparagine glycosylation sites of a human IgD myeloma protein were defined.
6619128	9	16	theme	NeuAc	1044:1048	arg1	alpha					1050:1054	NeuAc alpha 2	1044:1056	NeuAc alpha 2	1044:1056	The remainder of the oligosaccharides contain 1 or 2 residues of N-acetylneuraminic acid and have the structures NeuAc alpha 2 leads to 3Gal beta 1 leads to 3GalNAc (30%), Gal beta 1 leads to (NeuAc alpha 2 leads to 6)GalNAc (12%), and NeuAc alpha 2 leads to 3Gal beta 1 leads to 3(NeuAc alpha 2 leads to 6)GalNAc (8%).
6619128	12	17	theme	oligosaccharides	1391:1406	arg1	Examination					1376:1386	Examination	1376:1386	Examination of oligosaccharides isolated from different subregions of the IgD hinge	1376:1458	Examination of oligosaccharides isolated from different subregions of the IgD hinge indicated that a specific distribution of the sialylated structures among the glycosylated amino acids of the hinge region is not likely.
6619128	11	18	gly	glycoproteins	1361:1373	arg1	glycoproteins					1361:1373	membrane glycoproteins	1352:1373	membrane glycoproteins	1352:1373	These structures, however, have been described on a number of secreted and membrane glycoproteins.
6619128	0	19	theme	IgD	68:70	arg1	oligosaccharides					42:57	the O-glycosidically linked oligosaccharides	14:57	the O-glycosidically linked oligosaccharides of human IgD	14:70	Structures of the O-glycosidically linked oligosaccharides of human IgD.
6619128	3	20	theme	asparagine	237:246	arg1	sites					262:266	the 3 asparagine glycosylation sites	231:266	the 3 asparagine glycosylation sites of a human IgD myeloma protein	231:297	258, 11546-11556), the structures of the oligosaccharides present at the 3 asparagine glycosylation sites of a human IgD myeloma protein were defined.
6619128	3	20	theme	asparagine	237:246	arg1	protein					291:297	a human IgD myeloma protein	271:297	a human IgD myeloma protein	271:297	258, 11546-11556), the structures of the oligosaccharides present at the 3 asparagine glycosylation sites of a human IgD myeloma protein were defined.
6619128	4	21	theme	hinge	425:429	arg1	region					431:436	the hinge region	421:436	the hinge region of IgD	421:443	In this communication, we present the structures of the O-glycosidically linked oligosaccharides located in the hinge region of IgD:WAH.
6619128	12	22	attach	isolated	1408:1415	arg2	oligosaccharides					1391:1406	oligosaccharides	1391:1406	oligosaccharides isolated from different subregions of the IgD hinge	1391:1458	Examination of oligosaccharides isolated from different subregions of the IgD hinge indicated that a specific distribution of the sialylated structures among the glycosylated amino acids of the hinge region is not likely.
6619128	12	22	attach	isolated	1408:1415	arg1	subregions					1432:1441	different subregions	1422:1441	different subregions of the IgD hinge	1422:1458	Examination of oligosaccharides isolated from different subregions of the IgD hinge indicated that a specific distribution of the sialylated structures among the glycosylated amino acids of the hinge region is not likely.
6619128	3	23	from	sites	262:266	arg1	present					220:226	present	220:226	present	220:226	258, 11546-11556), the structures of the oligosaccharides present at the 3 asparagine glycosylation sites of a human IgD myeloma protein were defined.
6619128	3	24	theme	IgD	279:281	arg1	protein					291:297	a human IgD myeloma protein	271:297	a human IgD myeloma protein	271:297	258, 11546-11556), the structures of the oligosaccharides present at the 3 asparagine glycosylation sites of a human IgD myeloma protein were defined.
6619128	1	25	dep	J.	115:116	arg1	communication					89:101	the previous communication	76:101	the previous communication	76:101	In the previous communication (Mellis, S. J., and Baenziger, J. U. (1983) J. Biol.
6619128	1	25	dep	J.	115:116	arg1	Biol					150:153	Biol	150:153	Biol	150:153	In the previous communication (Mellis, S. J., and Baenziger, J. U. (1983) J. Biol.
6619128	4	26	theme	oligosaccharides	393:408	arg1	structures					351:360	the structures	347:360	the structures of the O-glycosidically linked oligosaccharides located in the hinge region of IgD:WAH	347:447	In this communication, we present the structures of the O-glycosidically linked oligosaccharides located in the hinge region of IgD:WAH.
6619128	9	27	contain	have	944:947	arg2	structures					953:962	the structures	949:962	the structures NeuAc alpha 2 leads to 3Gal beta 1	949:997	The remainder of the oligosaccharides contain 1 or 2 residues of N-acetylneuraminic acid and have the structures NeuAc alpha 2 leads to 3Gal beta 1 leads to 3GalNAc (30%), Gal beta 1 leads to (NeuAc alpha 2 leads to 6)GalNAc (12%), and NeuAc alpha 2 leads to 3Gal beta 1 leads to 3(NeuAc alpha 2 leads to 6)GalNAc (8%).
6619128	9	27	contain	have	944:947	arg1	oligosaccharides					872:887	the oligosaccharides	868:887	the oligosaccharides	868:887	The remainder of the oligosaccharides contain 1 or 2 residues of N-acetylneuraminic acid and have the structures NeuAc alpha 2 leads to 3Gal beta 1 leads to 3GalNAc (30%), Gal beta 1 leads to (NeuAc alpha 2 leads to 6)GalNAc (12%), and NeuAc alpha 2 leads to 3Gal beta 1 leads to 3(NeuAc alpha 2 leads to 6)GalNAc (8%).
6619128	12	28	theme	hinge	1570:1574	arg1	region					1576:1581	the hinge region	1566:1581	the hinge region	1566:1581	Examination of oligosaccharides isolated from different subregions of the IgD hinge indicated that a specific distribution of the sialylated structures among the glycosylated amino acids of the hinge region is not likely.
6619128	6	29	dep	structure	613:621	arg1	leads					634:638	leads	634:638	leads to 3 GalNAc which is identical with the structure of the predominant oligosaccharide in the hinge region of human IgA1 myeloma proteins (Baenziger, J. U., and Kornfeld, S. (1974) J. Biol	634:825	Approximately 50% of these molecules have the structure Gal beta 1 leads to 3 GalNAc which is identical with the structure of the predominant oligosaccharide in the hinge region of human IgA1 myeloma proteins (Baenziger, J. U., and Kornfeld, S. (1974) J. Biol.
6619128	9	30	theme	acid	935:938	arg1	residues					904:911	1 or 2 residues	897:911	1 or 2 residues of N-acetylneuraminic acid	897:938	The remainder of the oligosaccharides contain 1 or 2 residues of N-acetylneuraminic acid and have the structures NeuAc alpha 2 leads to 3Gal beta 1 leads to 3GalNAc (30%), Gal beta 1 leads to (NeuAc alpha 2 leads to 6)GalNAc (12%), and NeuAc alpha 2 leads to 3Gal beta 1 leads to 3(NeuAc alpha 2 leads to 6)GalNAc (8%).
6619128	9	30	theme	acid	935:938	arg1	acid					935:938	N-acetylneuraminic acid	916:938	N-acetylneuraminic acid	916:938	The remainder of the oligosaccharides contain 1 or 2 residues of N-acetylneuraminic acid and have the structures NeuAc alpha 2 leads to 3Gal beta 1 leads to 3GalNAc (30%), Gal beta 1 leads to (NeuAc alpha 2 leads to 6)GalNAc (12%), and NeuAc alpha 2 leads to 3Gal beta 1 leads to 3(NeuAc alpha 2 leads to 6)GalNAc (8%).
6619128	5	31	theme	serine	491:496	arg1	residue					498:504	one serine residue	487:504	one serine residue	487:504	Three or four threonine residues and one serine residue in the region bear O-glycosidically linked oligosaccharides.
6619128	3	32	theme	protein	291:297	arg1	sites					262:266	the 3 asparagine glycosylation sites	231:266	the 3 asparagine glycosylation sites of a human IgD myeloma protein	231:297	258, 11546-11556), the structures of the oligosaccharides present at the 3 asparagine glycosylation sites of a human IgD myeloma protein were defined.
6619128	3	32	theme	protein	291:297	arg1	protein					291:297	a human IgD myeloma protein	271:297	a human IgD myeloma protein	271:297	258, 11546-11556), the structures of the oligosaccharides present at the 3 asparagine glycosylation sites of a human IgD myeloma protein were defined.
6619128	8	33	dep	249	834:836	arg1	7270-7281					839:847	7270-7281	839:847	7270-7281	839:847	249, 7270-7281).
6619128	12	34	theme	amino	1551:1555	arg1	acids					1557:1561	the glycosylated amino acids	1534:1561	the glycosylated amino acids of the hinge region	1534:1581	Examination of oligosaccharides isolated from different subregions of the IgD hinge indicated that a specific distribution of the sialylated structures among the glycosylated amino acids of the hinge region is not likely.
6619128	3	35	attach	present	220:226	arg1	sites					262:266	the 3 asparagine glycosylation sites	231:266	the 3 asparagine glycosylation sites of a human IgD myeloma protein	231:297	258, 11546-11556), the structures of the oligosaccharides present at the 3 asparagine glycosylation sites of a human IgD myeloma protein were defined.
6619128	3	35	attach	present	220:226	arg1	protein					291:297	a human IgD myeloma protein	271:297	a human IgD myeloma protein	271:297	258, 11546-11556), the structures of the oligosaccharides present at the 3 asparagine glycosylation sites of a human IgD myeloma protein were defined.
6619128	3	35	attach	present	220:226	arg2	oligosaccharides					203:218	the oligosaccharides	199:218	the oligosaccharides present at the 3 asparagine glycosylation sites of a human IgD myeloma protein	199:297	258, 11546-11556), the structures of the oligosaccharides present at the 3 asparagine glycosylation sites of a human IgD myeloma protein were defined.
6619128	11	36	theme	glycoproteins	1361:1373	arg1	number					1329:1334	a number	1327:1334	a number of secreted and membrane glycoproteins	1327:1373	These structures, however, have been described on a number of secreted and membrane glycoproteins.
6619128	12	37	gly	glycosylated	1538:1549	arg1	acids					1557:1561	the glycosylated amino acids	1534:1561	the glycosylated amino acids of the hinge region	1534:1581	Examination of oligosaccharides isolated from different subregions of the IgD hinge indicated that a specific distribution of the sialylated structures among the glycosylated amino acids of the hinge region is not likely.
6619128	0	38	theme	linked	35:40	arg1	oligosaccharides					42:57	the O-glycosidically linked oligosaccharides	14:57	the O-glycosidically linked oligosaccharides of human IgD	14:70	Structures of the O-glycosidically linked oligosaccharides of human IgD.
6619128	9	39	theme	NeuAc	1087:1091	arg1	alpha					1093:1097	NeuAc alpha 2	1087:1099	NeuAc alpha 2	1087:1099	The remainder of the oligosaccharides contain 1 or 2 residues of N-acetylneuraminic acid and have the structures NeuAc alpha 2 leads to 3Gal beta 1 leads to 3GalNAc (30%), Gal beta 1 leads to (NeuAc alpha 2 leads to 6)GalNAc (12%), and NeuAc alpha 2 leads to 3Gal beta 1 leads to 3(NeuAc alpha 2 leads to 6)GalNAc (8%).
6619128	6	40	theme	myeloma	759:765	arg1	proteins					767:774	human IgA1 myeloma proteins	748:774	human IgA1 myeloma proteins	748:774	Approximately 50% of these molecules have the structure Gal beta 1 leads to 3 GalNAc which is identical with the structure of the predominant oligosaccharide in the hinge region of human IgA1 myeloma proteins (Baenziger, J. U., and Kornfeld, S. (1974) J. Biol.
6619128	12	41	theme	structures	1517:1526	arg1	likely					1590:1595	likely	1590:1595	likely	1590:1595	Examination of oligosaccharides isolated from different subregions of the IgD hinge indicated that a specific distribution of the sialylated structures among the glycosylated amino acids of the hinge region is not likely.
6619128	12	41	theme	structures	1517:1526	arg1	distribution					1486:1497	a specific distribution	1475:1497	a specific distribution of the sialylated structures among the glycosylated amino acids of the hinge region	1475:1581	Examination of oligosaccharides isolated from different subregions of the IgD hinge indicated that a specific distribution of the sialylated structures among the glycosylated amino acids of the hinge region is not likely.
6619128	6	42	theme	human	748:752	arg1	proteins					767:774	human IgA1 myeloma proteins	748:774	human IgA1 myeloma proteins	748:774	Approximately 50% of these molecules have the structure Gal beta 1 leads to 3 GalNAc which is identical with the structure of the predominant oligosaccharide in the hinge region of human IgA1 myeloma proteins (Baenziger, J. U., and Kornfeld, S. (1974) J. Biol.
6619128	12	43	theme	sialylated	1506:1515	arg1	structures					1517:1526	the sialylated structures	1502:1526	the sialylated structures	1502:1526	Examination of oligosaccharides isolated from different subregions of the IgD hinge indicated that a specific distribution of the sialylated structures among the glycosylated amino acids of the hinge region is not likely.
6619128	9	44	dep	GalNAc	1069:1074	arg1	leads					1058:1062	leads	1058:1062	leads to 6	1058:1067	The remainder of the oligosaccharides contain 1 or 2 residues of N-acetylneuraminic acid and have the structures NeuAc alpha 2 leads to 3Gal beta 1 leads to 3GalNAc (30%), Gal beta 1 leads to (NeuAc alpha 2 leads to 6)GalNAc (12%), and NeuAc alpha 2 leads to 3Gal beta 1 leads to 3(NeuAc alpha 2 leads to 6)GalNAc (8%).
6619128	4	45	dep	structures	351:360	arg1	WAH					445:447	WAH	445:447	WAH	445:447	In this communication, we present the structures of the O-glycosidically linked oligosaccharides located in the hinge region of IgD:WAH.
6619128	6	46	dep	Baenziger	777:785	arg1	Biol					822:825	Biol	822:825	Biol	822:825	Approximately 50% of these molecules have the structure Gal beta 1 leads to 3 GalNAc which is identical with the structure of the predominant oligosaccharide in the hinge region of human IgA1 myeloma proteins (Baenziger, J. U., and Kornfeld, S. (1974) J. Biol.
6619128	9	47	theme	3Gal	987:990	arg1	beta					992:995	3Gal beta 1	987:997	3Gal beta 1	987:997	The remainder of the oligosaccharides contain 1 or 2 residues of N-acetylneuraminic acid and have the structures NeuAc alpha 2 leads to 3Gal beta 1 leads to 3GalNAc (30%), Gal beta 1 leads to (NeuAc alpha 2 leads to 6)GalNAc (12%), and NeuAc alpha 2 leads to 3Gal beta 1 leads to 3(NeuAc alpha 2 leads to 6)GalNAc (8%).
6619128	12	48	theme	specific	1477:1484	arg1	likely					1590:1595	likely	1590:1595	likely	1590:1595	Examination of oligosaccharides isolated from different subregions of the IgD hinge indicated that a specific distribution of the sialylated structures among the glycosylated amino acids of the hinge region is not likely.
6619128	12	48	theme	specific	1477:1484	arg1	distribution					1486:1497	a specific distribution	1475:1497	a specific distribution of the sialylated structures among the glycosylated amino acids of the hinge region	1475:1581	Examination of oligosaccharides isolated from different subregions of the IgD hinge indicated that a specific distribution of the sialylated structures among the glycosylated amino acids of the hinge region is not likely.
6619128	10	49	theme	human	1242:1246	arg1	chains					1269:1274	other human immunoglobulin heavy chains	1236:1274	other human immunoglobulin heavy chains	1236:1274	The sialylated molecules have not been encountered previously on other human immunoglobulin heavy chains.
6619128	4	50	from	region	431:436	arg1	located					410:416	located	410:416	located	410:416	In this communication, we present the structures of the O-glycosidically linked oligosaccharides located in the hinge region of IgD:WAH.
6619128	9	51	theme	3	1131:1131	arg1	%					1167:1167	8%	1166:1167	8%	1166:1167	The remainder of the oligosaccharides contain 1 or 2 residues of N-acetylneuraminic acid and have the structures NeuAc alpha 2 leads to 3Gal beta 1 leads to 3GalNAc (30%), Gal beta 1 leads to (NeuAc alpha 2 leads to 6)GalNAc (12%), and NeuAc alpha 2 leads to 3Gal beta 1 leads to 3(NeuAc alpha 2 leads to 6)GalNAc (8%).
6619128	9	51	theme	3	1131:1131	arg1	GalNAc					1158:1163	3(NeuAc alpha 2 leads to 6)GalNAc	1131:1163	3(NeuAc alpha 2 leads to 6)GalNAc (8%)	1131:1168	The remainder of the oligosaccharides contain 1 or 2 residues of N-acetylneuraminic acid and have the structures NeuAc alpha 2 leads to 3Gal beta 1 leads to 3GalNAc (30%), Gal beta 1 leads to (NeuAc alpha 2 leads to 6)GalNAc (12%), and NeuAc alpha 2 leads to 3Gal beta 1 leads to 3(NeuAc alpha 2 leads to 6)GalNAc (8%).
6619128	12	52	theme	hinge	1454:1458	arg1	subregions					1432:1441	different subregions	1422:1441	different subregions of the IgD hinge	1422:1458	Examination of oligosaccharides isolated from different subregions of the IgD hinge indicated that a specific distribution of the sialylated structures among the glycosylated amino acids of the hinge region is not likely.
6619128	10	53	gly	sialylated	1175:1184	arg1	molecules					1186:1194	The sialylated molecules	1171:1194	The sialylated molecules	1171:1194	The sialylated molecules have not been encountered previously on other human immunoglobulin heavy chains.
6619128	6	54	theme	predominant	697:707	arg1	oligosaccharide					709:723	the predominant oligosaccharide	693:723	the predominant oligosaccharide in the hinge region of human IgA1 myeloma proteins	693:774	Approximately 50% of these molecules have the structure Gal beta 1 leads to 3 GalNAc which is identical with the structure of the predominant oligosaccharide in the hinge region of human IgA1 myeloma proteins (Baenziger, J. U., and Kornfeld, S. (1974) J. Biol.
6619128	9	55	theme	NeuAc	1133:1137	arg1	alpha					1139:1143	NeuAc alpha 2	1133:1145	NeuAc alpha 2	1133:1145	The remainder of the oligosaccharides contain 1 or 2 residues of N-acetylneuraminic acid and have the structures NeuAc alpha 2 leads to 3Gal beta 1 leads to 3GalNAc (30%), Gal beta 1 leads to (NeuAc alpha 2 leads to 6)GalNAc (12%), and NeuAc alpha 2 leads to 3Gal beta 1 leads to 3(NeuAc alpha 2 leads to 6)GalNAc (8%).
6619128	4	56	from	located	410:416	arg1	region					431:436	the hinge region	421:436	the hinge region of IgD	421:443	In this communication, we present the structures of the O-glycosidically linked oligosaccharides located in the hinge region of IgD:WAH.
6619128	3	57	dep	258	162:164	arg1	11546-11556					167:177	11546-11556	167:177	11546-11556	167:177	258, 11546-11556), the structures of the oligosaccharides present at the 3 asparagine glycosylation sites of a human IgD myeloma protein were defined.
6619128	3	58	theme	oligosaccharides	203:218	arg1	258					162:164	258	162:164	258	162:164	258, 11546-11556), the structures of the oligosaccharides present at the 3 asparagine glycosylation sites of a human IgD myeloma protein were defined.
6619128	3	58	theme	oligosaccharides	203:218	arg1	structures					185:194	the structures	181:194	the structures of the oligosaccharides present at the 3 asparagine glycosylation sites of a human IgD myeloma protein	181:297	258, 11546-11556), the structures of the oligosaccharides present at the 3 asparagine glycosylation sites of a human IgD myeloma protein were defined.
6619128	6	59	from	region	738:743	arg1	structure					680:688	the structure	676:688	the structure of the predominant oligosaccharide in the hinge region of human IgA1 myeloma proteins	676:774	Approximately 50% of these molecules have the structure Gal beta 1 leads to 3 GalNAc which is identical with the structure of the predominant oligosaccharide in the hinge region of human IgA1 myeloma proteins (Baenziger, J. U., and Kornfeld, S. (1974) J. Biol.
6619128	4	60	theme	linked	386:391	arg1	oligosaccharides					393:408	the O-glycosidically linked oligosaccharides	365:408	the O-glycosidically linked oligosaccharides located in the hinge region of IgD	365:443	In this communication, we present the structures of the O-glycosidically linked oligosaccharides located in the hinge region of IgD:WAH.
6619128	10	61	theme	heavy	1263:1267	arg1	chains					1269:1274	other human immunoglobulin heavy chains	1236:1274	other human immunoglobulin heavy chains	1236:1274	The sialylated molecules have not been encountered previously on other human immunoglobulin heavy chains.
6619128	12	62	theme	glycosylated	1538:1549	arg1	acids					1557:1561	the glycosylated amino acids	1534:1561	the glycosylated amino acids of the hinge region	1534:1581	Examination of oligosaccharides isolated from different subregions of the IgD hinge indicated that a specific distribution of the sialylated structures among the glycosylated amino acids of the hinge region is not likely.
6619128	9	63	dep	3	1131:1131	arg1	leads					1147:1151	leads	1147:1151	leads to 6	1147:1156	The remainder of the oligosaccharides contain 1 or 2 residues of N-acetylneuraminic acid and have the structures NeuAc alpha 2 leads to 3Gal beta 1 leads to 3GalNAc (30%), Gal beta 1 leads to (NeuAc alpha 2 leads to 6)GalNAc (12%), and NeuAc alpha 2 leads to 3Gal beta 1 leads to 3(NeuAc alpha 2 leads to 6)GalNAc (8%).
6619128	12	64	theme	different	1422:1430	arg1	subregions					1432:1441	different subregions	1422:1441	different subregions of the IgD hinge	1422:1458	Examination of oligosaccharides isolated from different subregions of the IgD hinge indicated that a specific distribution of the sialylated structures among the glycosylated amino acids of the hinge region is not likely.
6619128	4	65	link	linked	386:391	arg1	oligosaccharides					393:408	the O-glycosidically linked oligosaccharides	365:408	the O-glycosidically linked oligosaccharides located in the hinge region of IgD	365:443	In this communication, we present the structures of the O-glycosidically linked oligosaccharides located in the hinge region of IgD:WAH.
6619128	9	66	contain	contain	889:895	arg2	residues					904:911	1 or 2 residues	897:911	1 or 2 residues of N-acetylneuraminic acid	897:938	The remainder of the oligosaccharides contain 1 or 2 residues of N-acetylneuraminic acid and have the structures NeuAc alpha 2 leads to 3Gal beta 1 leads to 3GalNAc (30%), Gal beta 1 leads to (NeuAc alpha 2 leads to 6)GalNAc (12%), and NeuAc alpha 2 leads to 3Gal beta 1 leads to 3(NeuAc alpha 2 leads to 6)GalNAc (8%).
6619128	9	66	contain	contain	889:895	arg1	oligosaccharides					872:887	the oligosaccharides	868:887	the oligosaccharides	868:887	The remainder of the oligosaccharides contain 1 or 2 residues of N-acetylneuraminic acid and have the structures NeuAc alpha 2 leads to 3Gal beta 1 leads to 3GalNAc (30%), Gal beta 1 leads to (NeuAc alpha 2 leads to 6)GalNAc (12%), and NeuAc alpha 2 leads to 3Gal beta 1 leads to 3(NeuAc alpha 2 leads to 6)GalNAc (8%).
6619128	9	66	contain	contain	889:895	arg2	acid					935:938	N-acetylneuraminic acid	916:938	N-acetylneuraminic acid	916:938	The remainder of the oligosaccharides contain 1 or 2 residues of N-acetylneuraminic acid and have the structures NeuAc alpha 2 leads to 3Gal beta 1 leads to 3GalNAc (30%), Gal beta 1 leads to (NeuAc alpha 2 leads to 6)GalNAc (12%), and NeuAc alpha 2 leads to 3Gal beta 1 leads to 3(NeuAc alpha 2 leads to 6)GalNAc (8%).
6619128	3	67	theme	glycosylation	248:260	arg1	sites					262:266	the 3 asparagine glycosylation sites	231:266	the 3 asparagine glycosylation sites of a human IgD myeloma protein	231:297	258, 11546-11556), the structures of the oligosaccharides present at the 3 asparagine glycosylation sites of a human IgD myeloma protein were defined.
6619128	3	67	theme	glycosylation	248:260	arg1	protein					291:297	a human IgD myeloma protein	271:297	a human IgD myeloma protein	271:297	258, 11546-11556), the structures of the oligosaccharides present at the 3 asparagine glycosylation sites of a human IgD myeloma protein were defined.
6619128	4	68	theme	IgD	441:443	arg1	region					431:436	the hinge region	421:436	the hinge region of IgD	421:443	In this communication, we present the structures of the O-glycosidically linked oligosaccharides located in the hinge region of IgD:WAH.
6619128	3	69	theme	myeloma	283:289	arg1	protein					291:297	a human IgD myeloma protein	271:297	a human IgD myeloma protein	271:297	258, 11546-11556), the structures of the oligosaccharides present at the 3 asparagine glycosylation sites of a human IgD myeloma protein were defined.
6619128	4	70	theme	located	410:416	arg1	oligosaccharides					393:408	the O-glycosidically linked oligosaccharides	365:408	the O-glycosidically linked oligosaccharides located in the hinge region of IgD	365:443	In this communication, we present the structures of the O-glycosidically linked oligosaccharides located in the hinge region of IgD:WAH.
6619128	12	71	theme	region	1576:1581	arg1	acids					1557:1561	the glycosylated amino acids	1534:1561	the glycosylated amino acids of the hinge region	1534:1581	Examination of oligosaccharides isolated from different subregions of the IgD hinge indicated that a specific distribution of the sialylated structures among the glycosylated amino acids of the hinge region is not likely.
6619128	6	72	from	oligosaccharide	709:723	arg1	region					738:743	the hinge region	728:743	the hinge region of human IgA1 myeloma proteins	728:774	Approximately 50% of these molecules have the structure Gal beta 1 leads to 3 GalNAc which is identical with the structure of the predominant oligosaccharide in the hinge region of human IgA1 myeloma proteins (Baenziger, J. U., and Kornfeld, S. (1974) J. Biol.
6619128	3	73	theme	human	273:277	arg1	protein					291:297	a human IgD myeloma protein	271:297	a human IgD myeloma protein	271:297	258, 11546-11556), the structures of the oligosaccharides present at the 3 asparagine glycosylation sites of a human IgD myeloma protein were defined.
6619128	9	74	theme	N-acetylneuraminic	916:933	arg1	acid					935:938	N-acetylneuraminic acid	916:938	N-acetylneuraminic acid	916:938	The remainder of the oligosaccharides contain 1 or 2 residues of N-acetylneuraminic acid and have the structures NeuAc alpha 2 leads to 3Gal beta 1 leads to 3GalNAc (30%), Gal beta 1 leads to (NeuAc alpha 2 leads to 6)GalNAc (12%), and NeuAc alpha 2 leads to 3Gal beta 1 leads to 3(NeuAc alpha 2 leads to 6)GalNAc (8%).
6619128	1	75	theme	previous	80:87	arg1	communication					89:101	the previous communication	76:101	the previous communication	76:101	In the previous communication (Mellis, S. J., and Baenziger, J. U. (1983) J. Biol.
6619128	6	76	theme	Gal	623:625	arg1	beta					627:630	Gal beta 1	623:632	Gal beta 1	623:632	Approximately 50% of these molecules have the structure Gal beta 1 leads to 3 GalNAc which is identical with the structure of the predominant oligosaccharide in the hinge region of human IgA1 myeloma proteins (Baenziger, J. U., and Kornfeld, S. (1974) J. Biol.
6619128	5	77	link	linked	542:547	arg1	oligosaccharides					549:564	O-glycosidically linked oligosaccharides	525:564	O-glycosidically linked oligosaccharides	525:564	Three or four threonine residues and one serine residue in the region bear O-glycosidically linked oligosaccharides.
6619128	6	78	from	structure	680:688	arg1	region					738:743	the hinge region	728:743	the hinge region of human IgA1 myeloma proteins	728:774	Approximately 50% of these molecules have the structure Gal beta 1 leads to 3 GalNAc which is identical with the structure of the predominant oligosaccharide in the hinge region of human IgA1 myeloma proteins (Baenziger, J. U., and Kornfeld, S. (1974) J. Biol.
6619128	11	79	theme	membrane	1352:1359	arg1	glycoproteins					1361:1373	membrane glycoproteins	1352:1373	membrane glycoproteins	1352:1373	These structures, however, have been described on a number of secreted and membrane glycoproteins.
6619128	6	80	theme	molecules	594:602	arg1	%					583:583	Approximately 50%	567:583	Approximately 50% of these molecules	567:602	Approximately 50% of these molecules have the structure Gal beta 1 leads to 3 GalNAc which is identical with the structure of the predominant oligosaccharide in the hinge region of human IgA1 myeloma proteins (Baenziger, J. U., and Kornfeld, S. (1974) J. Biol.
6619128	6	80	theme	molecules	594:602	arg1	molecules					594:602	these molecules	588:602	these molecules	588:602	Approximately 50% of these molecules have the structure Gal beta 1 leads to 3 GalNAc which is identical with the structure of the predominant oligosaccharide in the hinge region of human IgA1 myeloma proteins (Baenziger, J. U., and Kornfeld, S. (1974) J. Biol.
6619128	4	81	attach	present	339:345	arg2	we					336:337	we	336:337	we	336:337	In this communication, we present the structures of the O-glycosidically linked oligosaccharides located in the hinge region of IgD:WAH.
6619128	4	81	attach	present	339:345	arg1	communication					321:333	this communication	316:333	this communication	316:333	In this communication, we present the structures of the O-glycosidically linked oligosaccharides located in the hinge region of IgD:WAH.
6619128	0	82	theme	oligosaccharides	42:57	arg1	Structures					0:9	Structures	0:9	Structures of the O-glycosidically linked oligosaccharides of human IgD	0:70	Structures of the O-glycosidically linked oligosaccharides of human IgD.
6619128	6	83	theme	proteins	767:774	arg1	region					738:743	the hinge region	728:743	the hinge region of human IgA1 myeloma proteins	728:774	Approximately 50% of these molecules have the structure Gal beta 1 leads to 3 GalNAc which is identical with the structure of the predominant oligosaccharide in the hinge region of human IgA1 myeloma proteins (Baenziger, J. U., and Kornfeld, S. (1974) J. Biol.
6619128	11	84	theme	secreted	1339:1346	arg1	number					1329:1334	a number	1327:1334	a number of secreted and membrane glycoproteins	1327:1373	These structures, however, have been described on a number of secreted and membrane glycoproteins.
6619128	9	85	theme	NeuAc	964:968	arg1	alpha					970:974	NeuAc alpha 2	964:976	NeuAc alpha 2	964:976	The remainder of the oligosaccharides contain 1 or 2 residues of N-acetylneuraminic acid and have the structures NeuAc alpha 2 leads to 3Gal beta 1 leads to 3GalNAc (30%), Gal beta 1 leads to (NeuAc alpha 2 leads to 6)GalNAc (12%), and NeuAc alpha 2 leads to 3Gal beta 1 leads to 3(NeuAc alpha 2 leads to 6)GalNAc (8%).
6619128	0	86	theme	human	62:66	arg1	IgD					68:70	human IgD	62:70	human IgD	62:70	Structures of the O-glycosidically linked oligosaccharides of human IgD.
6619128	6	87	theme	IgA1	754:757	arg1	proteins					767:774	human IgA1 myeloma proteins	748:774	human IgA1 myeloma proteins	748:774	Approximately 50% of these molecules have the structure Gal beta 1 leads to 3 GalNAc which is identical with the structure of the predominant oligosaccharide in the hinge region of human IgA1 myeloma proteins (Baenziger, J. U., and Kornfeld, S. (1974) J. Biol.
6619128	10	88	theme	sialylated	1175:1184	arg1	molecules					1186:1194	The sialylated molecules	1171:1194	The sialylated molecules	1171:1194	The sialylated molecules have not been encountered previously on other human immunoglobulin heavy chains.
6619128	3	89	gly	glycosylation	248:260	arg2	3					235:235	3	235:235	3	235:235	258, 11546-11556), the structures of the oligosaccharides present at the 3 asparagine glycosylation sites of a human IgD myeloma protein were defined.
6619128	3	89	gly	glycosylation	248:260	arg2	protein					291:297	a human IgD myeloma protein	271:297	a human IgD myeloma protein	271:297	258, 11546-11556), the structures of the oligosaccharides present at the 3 asparagine glycosylation sites of a human IgD myeloma protein were defined.
6619128	3	89	gly	glycosylation	248:260	arg1	protein					291:297	a human IgD myeloma protein	271:297	a human IgD myeloma protein	271:297	258, 11546-11556), the structures of the oligosaccharides present at the 3 asparagine glycosylation sites of a human IgD myeloma protein were defined.
6619128	3	89	gly	glycosylation	248:260	arg2	sites					262:266	the 3 asparagine glycosylation sites	231:266	the 3 asparagine glycosylation sites of a human IgD myeloma protein	231:297	258, 11546-11556), the structures of the oligosaccharides present at the 3 asparagine glycosylation sites of a human IgD myeloma protein were defined.
6619128	9	90	theme	3Gal	1110:1113	arg1	beta					1115:1118	3Gal beta 1	1110:1120	3Gal beta 1	1110:1120	The remainder of the oligosaccharides contain 1 or 2 residues of N-acetylneuraminic acid and have the structures NeuAc alpha 2 leads to 3Gal beta 1 leads to 3GalNAc (30%), Gal beta 1 leads to (NeuAc alpha 2 leads to 6)GalNAc (12%), and NeuAc alpha 2 leads to 3Gal beta 1 leads to 3(NeuAc alpha 2 leads to 6)GalNAc (8%).
6619128	6	91	theme	hinge	732:736	arg1	region					738:743	the hinge region	728:743	the hinge region of human IgA1 myeloma proteins	728:774	Approximately 50% of these molecules have the structure Gal beta 1 leads to 3 GalNAc which is identical with the structure of the predominant oligosaccharide in the hinge region of human IgA1 myeloma proteins (Baenziger, J. U., and Kornfeld, S. (1974) J. Biol.
6619128	9	92	dep	structures	953:962	arg1	leads					978:982	leads	978:982	leads to 3Gal beta 1	978:997	The remainder of the oligosaccharides contain 1 or 2 residues of N-acetylneuraminic acid and have the structures NeuAc alpha 2 leads to 3Gal beta 1 leads to 3GalNAc (30%), Gal beta 1 leads to (NeuAc alpha 2 leads to 6)GalNAc (12%), and NeuAc alpha 2 leads to 3Gal beta 1 leads to 3(NeuAc alpha 2 leads to 6)GalNAc (8%).
2001369	6	0	theme	fast-atom	1039:1047	arg1	spectrometry					1066:1077	fast-atom bombardment mass spectrometry	1039:1077	fast-atom bombardment mass spectrometry	1039:1077	The structures of the oligosaccharides were determined by methylation analysis, high-pH anion-exchange chromatography, fast-atom bombardment mass spectrometry, and 1H NMR spectroscopy at 500 MHz.
2001369	3	1	theme	present	586:592	arg1	study					594:598	the present study	582:598	the present study	582:598	In the present study, the structures of the Asn-linked oligosaccharides of soluble rCD4 have been elucidated.
2001369	11	2	theme	N-acetyllactosamine	1721:1739	arg1	structures					1741:1750	the N-acetyllactosamine structures	1717:1750	the N-acetyllactosamine structures at Asn-300	1717:1761	Approximately 9% of the hybrid structures and 40% of the N-acetyllactosamine structures at Asn-300 were found to contain fucose alpha(1-->6) linked to the innermost GlcNAc residue.
2001369	2	3	theme	therapeutic	498:508	arg1	agent					510:514	a potential therapeutic agent	486:514	a potential therapeutic agent in the treatment of acquired immunodeficiency syndrome (AIDS)	486:576	A soluble, recombinant CD4 molecule (rCD4), produced by expression of a truncated CD4 gene in Chinese hamster ovary (CHO) cells [Smith et al. (1987) Science 238, 1704-1707], is in clinical trials as a potential therapeutic agent in the treatment of acquired immunodeficiency syndrome (AIDS).
2001369	1	4	theme	macrophages	130:140	arg1	Infection					99:107	Infection	99:107	Infection of T-lymphocytes and macrophages by human immunodeficiency virus (HIV)	99:178	Infection of T-lymphocytes and macrophages by human immunodeficiency virus (HIV) is mediated by the binding of the HIV envelope glycoprotein to the cell-surface receptor glycoprotein CD4.
2001369	1	5	theme	receptor	260:267	arg1	CD4					282:284	the cell-surface receptor glycoprotein CD4	243:284	the cell-surface receptor glycoprotein CD4	243:284	Infection of T-lymphocytes and macrophages by human immunodeficiency virus (HIV) is mediated by the binding of the HIV envelope glycoprotein to the cell-surface receptor glycoprotein CD4.
2001369	2	6	theme	acquired	536:543	arg1	AIDS					572:575	AIDS	572:575	AIDS	572:575	A soluble, recombinant CD4 molecule (rCD4), produced by expression of a truncated CD4 gene in Chinese hamster ovary (CHO) cells [Smith et al. (1987) Science 238, 1704-1707], is in clinical trials as a potential therapeutic agent in the treatment of acquired immunodeficiency syndrome (AIDS).
2001369	2	6	theme	acquired	536:543	arg1	syndrome					562:569	acquired immunodeficiency syndrome	536:569	acquired immunodeficiency syndrome (AIDS)	536:576	A soluble, recombinant CD4 molecule (rCD4), produced by expression of a truncated CD4 gene in Chinese hamster ovary (CHO) cells [Smith et al. (1987) Science 238, 1704-1707], is in clinical trials as a potential therapeutic agent in the treatment of acquired immunodeficiency syndrome (AIDS).
2001369	3	7	link	Asn-linked	623:632	arg1	oligosaccharides					634:649	the Asn-linked oligosaccharides	619:649	the Asn-linked oligosaccharides of soluble rCD4	619:665	In the present study, the structures of the Asn-linked oligosaccharides of soluble rCD4 have been elucidated.
2001369	3	8	theme	soluble	654:660	arg1	rCD4					662:665	soluble rCD4	654:665	soluble rCD4	654:665	In the present study, the structures of the Asn-linked oligosaccharides of soluble rCD4 have been elucidated.
2001369	3	9	theme	oligosaccharides	634:649	arg1	structures					605:614	the structures	601:614	the structures of the Asn-linked oligosaccharides of soluble rCD4	601:665	In the present study, the structures of the Asn-linked oligosaccharides of soluble rCD4 have been elucidated.
2001369	2	10	theme	soluble	289:295	arg1	rCD4					324:327	rCD4	324:327	rCD4	324:327	A soluble, recombinant CD4 molecule (rCD4), produced by expression of a truncated CD4 gene in Chinese hamster ovary (CHO) cells [Smith et al. (1987) Science 238, 1704-1707], is in clinical trials as a potential therapeutic agent in the treatment of acquired immunodeficiency syndrome (AIDS).
2001369	2	10	theme	soluble	289:295	arg1	molecule					314:321	A soluble, recombinant CD4 molecule	287:321	A soluble, recombinant CD4 molecule (rCD4)	287:328	A soluble, recombinant CD4 molecule (rCD4), produced by expression of a truncated CD4 gene in Chinese hamster ovary (CHO) cells [Smith et al. (1987) Science 238, 1704-1707], is in clinical trials as a potential therapeutic agent in the treatment of acquired immunodeficiency syndrome (AIDS).
2001369	11	11	theme	hybrid	1688:1693	arg1	structures					1695:1704	the hybrid structures	1684:1704	the hybrid structures	1684:1704	Approximately 9% of the hybrid structures and 40% of the N-acetyllactosamine structures at Asn-300 were found to contain fucose alpha(1-->6) linked to the innermost GlcNAc residue.
2001369	6	12	theme	mass	1061:1064	arg1	spectrometry					1066:1077	fast-atom bombardment mass spectrometry	1039:1077	fast-atom bombardment mass spectrometry	1039:1077	The structures of the oligosaccharides were determined by methylation analysis, high-pH anion-exchange chromatography, fast-atom bombardment mass spectrometry, and 1H NMR spectroscopy at 500 MHz.
2001369	5	13	gly	glycopeptides	781:793	arg2	glycopeptides					781:793	Tryptic glycopeptides	773:793	Tryptic glycopeptides containing either of the sites	773:824	Tryptic glycopeptides containing either of the sites were purified by reversed-phase HPLC, and their oligosaccharides were released enzymatically.
2001369	9	14	theme	hybrid	1400:1405	arg1	structures					1407:1416	Two different hybrid structures	1386:1416	Two different hybrid structures	1386:1416	Two different hybrid structures were found to account for 34% of the oligosaccharides attached to Asn-300.
2001369	6	15	theme	oligosaccharides	942:957	arg1	structures					924:933	The structures	920:933	The structures of the oligosaccharides	920:957	The structures of the oligosaccharides were determined by methylation analysis, high-pH anion-exchange chromatography, fast-atom bombardment mass spectrometry, and 1H NMR spectroscopy at 500 MHz.
2001369	8	16	theme	GlcNAc	1370:1375	arg1	residue					1377:1383	the reducing GlcNAc residue	1357:1383	the reducing GlcNAc residue	1357:1383	Approximately 18% of these structures contained fucose alpha(1-->6) linked to the reducing GlcNAc residue.
2001369	7	17	theme	complex	1182:1188	arg1	"					1189:1189	"complex"	1181:1189	"complex"	1181:1189	Asn-271 was found to carry diantennary N-acetyllactosamine-type ("complex") oligosaccharides, of which 8% were asialo, 55% were monosialyl, and 37% were disialyl.
2001369	11	18	theme	innermost	1819:1827	arg1	residue					1836:1842	the innermost GlcNAc residue	1815:1842	the innermost GlcNAc residue	1815:1842	Approximately 9% of the hybrid structures and 40% of the N-acetyllactosamine structures at Asn-300 were found to contain fucose alpha(1-->6) linked to the innermost GlcNAc residue.
2001369	1	19	theme	immunodeficiency	151:166	arg1	HIV					175:177	HIV	175:177	HIV	175:177	Infection of T-lymphocytes and macrophages by human immunodeficiency virus (HIV) is mediated by the binding of the HIV envelope glycoprotein to the cell-surface receptor glycoprotein CD4.
2001369	1	19	theme	immunodeficiency	151:166	arg1	virus					168:172	human immunodeficiency virus	145:172	human immunodeficiency virus (HIV)	145:178	Infection of T-lymphocytes and macrophages by human immunodeficiency virus (HIV) is mediated by the binding of the HIV envelope glycoprotein to the cell-surface receptor glycoprotein CD4.
2001369	5	20	contain	containing	795:804	arg2	either					806:811	either	806:811	either	806:811	Tryptic glycopeptides containing either of the sites were purified by reversed-phase HPLC, and their oligosaccharides were released enzymatically.
2001369	5	20	contain	containing	795:804	arg1	glycopeptides					781:793	Tryptic glycopeptides	773:793	Tryptic glycopeptides containing either of the sites	773:824	Tryptic glycopeptides containing either of the sites were purified by reversed-phase HPLC, and their oligosaccharides were released enzymatically.
2001369	0	21	theme	hamster	78:84	arg1	cells					92:96	Chinese hamster ovary cells	70:96	Chinese hamster ovary cells	70:96	Carbohydrate structures of recombinant soluble human CD4 expressed in Chinese hamster ovary cells.
2001369	11	22	contain	contain	1777:1783	arg1	%					1679:1679	Approximately 9%	1664:1679	Approximately 9% of the hybrid structures	1664:1704	Approximately 9% of the hybrid structures and 40% of the N-acetyllactosamine structures at Asn-300 were found to contain fucose alpha(1-->6) linked to the innermost GlcNAc residue.
2001369	11	22	contain	contain	1777:1783	arg1	%					1712:1712	40%	1710:1712	40% of the N-acetyllactosamine structures at Asn-300	1710:1761	Approximately 9% of the hybrid structures and 40% of the N-acetyllactosamine structures at Asn-300 were found to contain fucose alpha(1-->6) linked to the innermost GlcNAc residue.
2001369	11	22	contain	contain	1777:1783	arg2	1-->6					1798:1802	1-->6	1798:1802	1-->6	1798:1802	Approximately 9% of the hybrid structures and 40% of the N-acetyllactosamine structures at Asn-300 were found to contain fucose alpha(1-->6) linked to the innermost GlcNAc residue.
2001369	11	22	contain	contain	1777:1783	arg2	alpha					1792:1796	fucose alpha	1785:1796	fucose alpha(1-->6) linked to the innermost GlcNAc residue	1785:1842	Approximately 9% of the hybrid structures and 40% of the N-acetyllactosamine structures at Asn-300 were found to contain fucose alpha(1-->6) linked to the innermost GlcNAc residue.
2001369	11	22	contain	contain	1777:1783	arg1	structures					1695:1704	the hybrid structures	1684:1704	the hybrid structures	1684:1704	Approximately 9% of the hybrid structures and 40% of the N-acetyllactosamine structures at Asn-300 were found to contain fucose alpha(1-->6) linked to the innermost GlcNAc residue.
2001369	11	22	contain	contain	1777:1783	arg1	structures					1741:1750	the N-acetyllactosamine structures	1717:1750	the N-acetyllactosamine structures at Asn-300	1717:1761	Approximately 9% of the hybrid structures and 40% of the N-acetyllactosamine structures at Asn-300 were found to contain fucose alpha(1-->6) linked to the innermost GlcNAc residue.
2001369	11	23	attach	linked	1805:1810	arg2	1-->6					1798:1802	1-->6	1798:1802	1-->6	1798:1802	Approximately 9% of the hybrid structures and 40% of the N-acetyllactosamine structures at Asn-300 were found to contain fucose alpha(1-->6) linked to the innermost GlcNAc residue.
2001369	11	23	attach	linked	1805:1810	arg2	alpha					1792:1796	fucose alpha	1785:1796	fucose alpha(1-->6) linked to the innermost GlcNAc residue	1785:1842	Approximately 9% of the hybrid structures and 40% of the N-acetyllactosamine structures at Asn-300 were found to contain fucose alpha(1-->6) linked to the innermost GlcNAc residue.
2001369	11	23	attach	linked	1805:1810	arg1	residue					1836:1842	the innermost GlcNAc residue	1815:1842	the innermost GlcNAc residue	1815:1842	Approximately 9% of the hybrid structures and 40% of the N-acetyllactosamine structures at Asn-300 were found to contain fucose alpha(1-->6) linked to the innermost GlcNAc residue.
2001369	1	24	gly	glycoprotein	227:238	arg1	glycoprotein					227:238	the HIV envelope glycoprotein	210:238	the HIV envelope glycoprotein	210:238	Infection of T-lymphocytes and macrophages by human immunodeficiency virus (HIV) is mediated by the binding of the HIV envelope glycoprotein to the cell-surface receptor glycoprotein CD4.
2001369	2	25	theme	immunodeficiency	545:560	arg1	AIDS					572:575	AIDS	572:575	AIDS	572:575	A soluble, recombinant CD4 molecule (rCD4), produced by expression of a truncated CD4 gene in Chinese hamster ovary (CHO) cells [Smith et al. (1987) Science 238, 1704-1707], is in clinical trials as a potential therapeutic agent in the treatment of acquired immunodeficiency syndrome (AIDS).
2001369	2	25	theme	immunodeficiency	545:560	arg1	syndrome					562:569	acquired immunodeficiency syndrome	536:569	acquired immunodeficiency syndrome (AIDS)	536:576	A soluble, recombinant CD4 molecule (rCD4), produced by expression of a truncated CD4 gene in Chinese hamster ovary (CHO) cells [Smith et al. (1987) Science 238, 1704-1707], is in clinical trials as a potential therapeutic agent in the treatment of acquired immunodeficiency syndrome (AIDS).
2001369	2	26	theme	CD4	369:371	arg1	gene					373:376	a truncated CD4 gene	357:376	a truncated CD4 gene	357:376	A soluble, recombinant CD4 molecule (rCD4), produced by expression of a truncated CD4 gene in Chinese hamster ovary (CHO) cells [Smith et al. (1987) Science 238, 1704-1707], is in clinical trials as a potential therapeutic agent in the treatment of acquired immunodeficiency syndrome (AIDS).
2001369	6	27	theme	anion-exchange	1008:1021	arg1	chromatography					1023:1036	high-pH anion-exchange chromatography	1000:1036	high-pH anion-exchange chromatography	1000:1036	The structures of the oligosaccharides were determined by methylation analysis, high-pH anion-exchange chromatography, fast-atom bombardment mass spectrometry, and 1H NMR spectroscopy at 500 MHz.
2001369	10	28	attach	attached	1531:1538	arg2	oligosaccharides					1514:1529	the oligosaccharides	1510:1529	the oligosaccharides attached to Asn-300	1510:1549	The remainder of the oligosaccharides attached to Asn-300 were diantennary N-acetyllactosamine-type, of which 10% were asialo, 61% were monosialyl, and 29% were disialyl.
2001369	10	28	attach	attached	1531:1538	arg1	Asn-300					1543:1549	Asn-300	1543:1549	Asn-300	1543:1549	The remainder of the oligosaccharides attached to Asn-300 were diantennary N-acetyllactosamine-type, of which 10% were asialo, 61% were monosialyl, and 29% were disialyl.
2001369	0	29	theme	Carbohydrate	0:11	arg1	structures					13:22	Carbohydrate structures	0:22	Carbohydrate structures of recombinant soluble human CD4	0:55	Carbohydrate structures of recombinant soluble human CD4 expressed in Chinese hamster ovary cells.
2001369	1	30	theme	glycoprotein	269:280	arg1	CD4					282:284	the cell-surface receptor glycoprotein CD4	243:284	the cell-surface receptor glycoprotein CD4	243:284	Infection of T-lymphocytes and macrophages by human immunodeficiency virus (HIV) is mediated by the binding of the HIV envelope glycoprotein to the cell-surface receptor glycoprotein CD4.
2001369	8	31	contain	contained	1317:1325	arg2	1-->6					1340:1344	1-->6	1340:1344	1-->6	1340:1344	Approximately 18% of these structures contained fucose alpha(1-->6) linked to the reducing GlcNAc residue.
2001369	8	31	contain	contained	1317:1325	arg1	%					1295:1295	Approximately 18%	1279:1295	Approximately 18% of these structures	1279:1315	Approximately 18% of these structures contained fucose alpha(1-->6) linked to the reducing GlcNAc residue.
2001369	8	31	contain	contained	1317:1325	arg2	alpha					1334:1338	fucose alpha	1327:1338	fucose alpha(1-->6) linked to the reducing GlcNAc residue	1327:1383	Approximately 18% of these structures contained fucose alpha(1-->6) linked to the reducing GlcNAc residue.
2001369	8	31	contain	contained	1317:1325	arg1	structures					1306:1315	these structures	1300:1315	these structures	1300:1315	Approximately 18% of these structures contained fucose alpha(1-->6) linked to the reducing GlcNAc residue.
2001369	7	32	dep	N-acetyllactosamine-type	1155:1178	arg1	"					1189:1189	"complex"	1181:1189	"complex"	1181:1189	Asn-271 was found to carry diantennary N-acetyllactosamine-type ("complex") oligosaccharides, of which 8% were asialo, 55% were monosialyl, and 37% were disialyl.
2001369	4	33	theme	potential	715:723	arg1	sites					725:729	two potential sites	711:729	two potential sites for N-glycosylation, Asn-271 and Asn-300	711:770	The rCD4 molecule has two potential sites for N-glycosylation, Asn-271 and Asn-300.
2001369	2	34	theme	hamster	389:395	arg1	cells					409:413	Chinese hamster ovary (CHO) cells	381:413	Chinese hamster ovary (CHO) cells [Smith et al	381:426	A soluble, recombinant CD4 molecule (rCD4), produced by expression of a truncated CD4 gene in Chinese hamster ovary (CHO) cells [Smith et al. (1987) Science 238, 1704-1707], is in clinical trials as a potential therapeutic agent in the treatment of acquired immunodeficiency syndrome (AIDS).
2001369	6	35	theme	methylation	978:988	arg1	analysis					990:997	methylation analysis	978:997	methylation analysis	978:997	The structures of the oligosaccharides were determined by methylation analysis, high-pH anion-exchange chromatography, fast-atom bombardment mass spectrometry, and 1H NMR spectroscopy at 500 MHz.
2001369	2	36	from	agent	510:514	arg1	treatment					523:531	the treatment	519:531	the treatment of acquired immunodeficiency syndrome (AIDS)	519:576	A soluble, recombinant CD4 molecule (rCD4), produced by expression of a truncated CD4 gene in Chinese hamster ovary (CHO) cells [Smith et al. (1987) Science 238, 1704-1707], is in clinical trials as a potential therapeutic agent in the treatment of acquired immunodeficiency syndrome (AIDS).
2001369	10	37	dep	N-acetyllactosamine-type	1568:1591	arg1	N-acetyllactosamine-type					1568:1591	N-acetyllactosamine-type	1568:1591	N-acetyllactosamine-type	1568:1591	The remainder of the oligosaccharides attached to Asn-300 were diantennary N-acetyllactosamine-type, of which 10% were asialo, 61% were monosialyl, and 29% were disialyl.
2001369	10	37	dep	N-acetyllactosamine-type	1568:1591	arg1	remainder					1497:1505	The remainder	1493:1505	The remainder of the oligosaccharides attached to Asn-300	1493:1549	The remainder of the oligosaccharides attached to Asn-300 were diantennary N-acetyllactosamine-type, of which 10% were asialo, 61% were monosialyl, and 29% were disialyl.
2001369	10	37	dep	N-acetyllactosamine-type	1568:1591	arg1	asialo					1612:1617	asialo	1612:1617	asialo	1612:1617	The remainder of the oligosaccharides attached to Asn-300 were diantennary N-acetyllactosamine-type, of which 10% were asialo, 61% were monosialyl, and 29% were disialyl.
2001369	10	37	dep	N-acetyllactosamine-type	1568:1591	arg1	disialyl					1654:1661	disialyl	1654:1661	disialyl	1654:1661	The remainder of the oligosaccharides attached to Asn-300 were diantennary N-acetyllactosamine-type, of which 10% were asialo, 61% were monosialyl, and 29% were disialyl.
2001369	0	38	theme	soluble	39:45	arg1	CD4					53:55	recombinant soluble human CD4	27:55	recombinant soluble human CD4	27:55	Carbohydrate structures of recombinant soluble human CD4 expressed in Chinese hamster ovary cells.
2001369	2	39	theme	[Smith	415:420	arg1	cells					409:413	Chinese hamster ovary (CHO) cells	381:413	Chinese hamster ovary (CHO) cells [Smith et al	381:426	A soluble, recombinant CD4 molecule (rCD4), produced by expression of a truncated CD4 gene in Chinese hamster ovary (CHO) cells [Smith et al. (1987) Science 238, 1704-1707], is in clinical trials as a potential therapeutic agent in the treatment of acquired immunodeficiency syndrome (AIDS).
2001369	8	40	theme	structures	1306:1315	arg1	%					1295:1295	Approximately 18%	1279:1295	Approximately 18% of these structures	1279:1315	Approximately 18% of these structures contained fucose alpha(1-->6) linked to the reducing GlcNAc residue.
2001369	8	40	theme	structures	1306:1315	arg1	structures					1306:1315	these structures	1300:1315	these structures	1300:1315	Approximately 18% of these structures contained fucose alpha(1-->6) linked to the reducing GlcNAc residue.
2001369	0	41	theme	CD4	53:55	arg1	structures					13:22	Carbohydrate structures	0:22	Carbohydrate structures of recombinant soluble human CD4	0:55	Carbohydrate structures of recombinant soluble human CD4 expressed in Chinese hamster ovary cells.
2001369	8	42	theme	fucose	1327:1332	arg1	1-->6					1340:1344	1-->6	1340:1344	1-->6	1340:1344	Approximately 18% of these structures contained fucose alpha(1-->6) linked to the reducing GlcNAc residue.
2001369	8	42	theme	fucose	1327:1332	arg1	alpha					1334:1338	fucose alpha	1327:1338	fucose alpha(1-->6) linked to the reducing GlcNAc residue	1327:1383	Approximately 18% of these structures contained fucose alpha(1-->6) linked to the reducing GlcNAc residue.
2001369	7	43	contain	carry	1137:1141	arg1	Asn-271					1116:1122	Asn-271	1116:1122	Asn-271	1116:1122	Asn-271 was found to carry diantennary N-acetyllactosamine-type ("complex") oligosaccharides, of which 8% were asialo, 55% were monosialyl, and 37% were disialyl.
2001369	7	43	contain	carry	1137:1141	arg2	oligosaccharides					1192:1207	diantennary N-acetyllactosamine-type ("complex") oligosaccharides	1143:1207	diantennary N-acetyllactosamine-type ("complex") oligosaccharides	1143:1207	Asn-271 was found to carry diantennary N-acetyllactosamine-type ("complex") oligosaccharides, of which 8% were asialo, 55% were monosialyl, and 37% were disialyl.
2001369	2	44	dep	1987	430:433	arg1	Science					436:442	Science	436:442	Science	436:442	A soluble, recombinant CD4 molecule (rCD4), produced by expression of a truncated CD4 gene in Chinese hamster ovary (CHO) cells [Smith et al. (1987) Science 238, 1704-1707], is in clinical trials as a potential therapeutic agent in the treatment of acquired immunodeficiency syndrome (AIDS).
2001369	2	45	theme	gene	373:376	arg1	1987					430:433	1987	430:433	1987	430:433	A soluble, recombinant CD4 molecule (rCD4), produced by expression of a truncated CD4 gene in Chinese hamster ovary (CHO) cells [Smith et al. (1987) Science 238, 1704-1707], is in clinical trials as a potential therapeutic agent in the treatment of acquired immunodeficiency syndrome (AIDS).
2001369	2	45	theme	gene	373:376	arg1	expression					343:352	expression	343:352	expression of a truncated CD4 gene in Chinese hamster ovary (CHO) cells [Smith et al. (1987) Science 238, 1704-1707]	343:458	A soluble, recombinant CD4 molecule (rCD4), produced by expression of a truncated CD4 gene in Chinese hamster ovary (CHO) cells [Smith et al. (1987) Science 238, 1704-1707], is in clinical trials as a potential therapeutic agent in the treatment of acquired immunodeficiency syndrome (AIDS).
2001369	11	46	theme	structures	1741:1750	arg1	%					1712:1712	40%	1710:1712	40% of the N-acetyllactosamine structures at Asn-300	1710:1761	Approximately 9% of the hybrid structures and 40% of the N-acetyllactosamine structures at Asn-300 were found to contain fucose alpha(1-->6) linked to the innermost GlcNAc residue.
2001369	11	46	theme	structures	1741:1750	arg1	%					1679:1679	Approximately 9%	1664:1679	Approximately 9% of the hybrid structures	1664:1704	Approximately 9% of the hybrid structures and 40% of the N-acetyllactosamine structures at Asn-300 were found to contain fucose alpha(1-->6) linked to the innermost GlcNAc residue.
2001369	11	46	theme	structures	1741:1750	arg1	structures					1741:1750	the N-acetyllactosamine structures	1717:1750	the N-acetyllactosamine structures at Asn-300	1717:1761	Approximately 9% of the hybrid structures and 40% of the N-acetyllactosamine structures at Asn-300 were found to contain fucose alpha(1-->6) linked to the innermost GlcNAc residue.
2001369	11	46	theme	structures	1741:1750	arg1	structures					1695:1704	the hybrid structures	1684:1704	the hybrid structures	1684:1704	Approximately 9% of the hybrid structures and 40% of the N-acetyllactosamine structures at Asn-300 were found to contain fucose alpha(1-->6) linked to the innermost GlcNAc residue.
2001369	1	47	theme	envelope	218:225	arg1	glycoprotein					227:238	the HIV envelope glycoprotein	210:238	the HIV envelope glycoprotein	210:238	Infection of T-lymphocytes and macrophages by human immunodeficiency virus (HIV) is mediated by the binding of the HIV envelope glycoprotein to the cell-surface receptor glycoprotein CD4.
2001369	6	48	theme	bombardment	1049:1059	arg1	spectrometry					1066:1077	fast-atom bombardment mass spectrometry	1039:1077	fast-atom bombardment mass spectrometry	1039:1077	The structures of the oligosaccharides were determined by methylation analysis, high-pH anion-exchange chromatography, fast-atom bombardment mass spectrometry, and 1H NMR spectroscopy at 500 MHz.
2001369	7	49	theme	N-acetyllactosamine-type	1155:1178	arg1	oligosaccharides					1192:1207	diantennary N-acetyllactosamine-type ("complex") oligosaccharides	1143:1207	diantennary N-acetyllactosamine-type ("complex") oligosaccharides	1143:1207	Asn-271 was found to carry diantennary N-acetyllactosamine-type ("complex") oligosaccharides, of which 8% were asialo, 55% were monosialyl, and 37% were disialyl.
2001369	1	50	theme	cell-surface	247:258	arg1	CD4					282:284	the cell-surface receptor glycoprotein CD4	243:284	the cell-surface receptor glycoprotein CD4	243:284	Infection of T-lymphocytes and macrophages by human immunodeficiency virus (HIV) is mediated by the binding of the HIV envelope glycoprotein to the cell-surface receptor glycoprotein CD4.
2001369	2	51	theme	potential	488:496	arg1	agent					510:514	a potential therapeutic agent	486:514	a potential therapeutic agent in the treatment of acquired immunodeficiency syndrome (AIDS)	486:576	A soluble, recombinant CD4 molecule (rCD4), produced by expression of a truncated CD4 gene in Chinese hamster ovary (CHO) cells [Smith et al. (1987) Science 238, 1704-1707], is in clinical trials as a potential therapeutic agent in the treatment of acquired immunodeficiency syndrome (AIDS).
2001369	9	52	attach	attached	1472:1479	arg2	oligosaccharides					1455:1470	the oligosaccharides	1451:1470	the oligosaccharides attached to Asn-300	1451:1490	Two different hybrid structures were found to account for 34% of the oligosaccharides attached to Asn-300.
2001369	9	52	attach	attached	1472:1479	arg1	Asn-300					1484:1490	Asn-300	1484:1490	Asn-300	1484:1490	Two different hybrid structures were found to account for 34% of the oligosaccharides attached to Asn-300.
2001369	3	53	theme	Asn-linked	623:632	arg1	oligosaccharides					634:649	the Asn-linked oligosaccharides	619:649	the Asn-linked oligosaccharides of soluble rCD4	619:665	In the present study, the structures of the Asn-linked oligosaccharides of soluble rCD4 have been elucidated.
2001369	2	54	theme	CD4	310:312	arg1	rCD4					324:327	rCD4	324:327	rCD4	324:327	A soluble, recombinant CD4 molecule (rCD4), produced by expression of a truncated CD4 gene in Chinese hamster ovary (CHO) cells [Smith et al. (1987) Science 238, 1704-1707], is in clinical trials as a potential therapeutic agent in the treatment of acquired immunodeficiency syndrome (AIDS).
2001369	2	54	theme	CD4	310:312	arg1	molecule					314:321	A soluble, recombinant CD4 molecule	287:321	A soluble, recombinant CD4 molecule (rCD4)	287:328	A soluble, recombinant CD4 molecule (rCD4), produced by expression of a truncated CD4 gene in Chinese hamster ovary (CHO) cells [Smith et al. (1987) Science 238, 1704-1707], is in clinical trials as a potential therapeutic agent in the treatment of acquired immunodeficiency syndrome (AIDS).
2001369	5	55	theme	Tryptic	773:779	arg1	glycopeptides					781:793	Tryptic glycopeptides	773:793	Tryptic glycopeptides containing either of the sites	773:824	Tryptic glycopeptides containing either of the sites were purified by reversed-phase HPLC, and their oligosaccharides were released enzymatically.
2001369	11	56	from	%	1679:1679	arg1	Asn-300					1755:1761	Asn-300	1755:1761	Asn-300	1755:1761	Approximately 9% of the hybrid structures and 40% of the N-acetyllactosamine structures at Asn-300 were found to contain fucose alpha(1-->6) linked to the innermost GlcNAc residue.
2001369	2	57	from	expression	343:352	arg1	cells					409:413	Chinese hamster ovary (CHO) cells	381:413	Chinese hamster ovary (CHO) cells [Smith et al	381:426	A soluble, recombinant CD4 molecule (rCD4), produced by expression of a truncated CD4 gene in Chinese hamster ovary (CHO) cells [Smith et al. (1987) Science 238, 1704-1707], is in clinical trials as a potential therapeutic agent in the treatment of acquired immunodeficiency syndrome (AIDS).
2001369	3	58	theme	rCD4	662:665	arg1	oligosaccharides					634:649	the Asn-linked oligosaccharides	619:649	the Asn-linked oligosaccharides of soluble rCD4	619:665	In the present study, the structures of the Asn-linked oligosaccharides of soluble rCD4 have been elucidated.
2001369	6	59	theme	NMR	1087:1089	arg1	spectroscopy					1091:1102	1H NMR spectroscopy	1084:1102	1H NMR spectroscopy	1084:1102	The structures of the oligosaccharides were determined by methylation analysis, high-pH anion-exchange chromatography, fast-atom bombardment mass spectrometry, and 1H NMR spectroscopy at 500 MHz.
2001369	10	60	theme	oligosaccharides	1514:1529	arg1	N-acetyllactosamine-type					1568:1591	N-acetyllactosamine-type	1568:1591	N-acetyllactosamine-type	1568:1591	The remainder of the oligosaccharides attached to Asn-300 were diantennary N-acetyllactosamine-type, of which 10% were asialo, 61% were monosialyl, and 29% were disialyl.
2001369	10	60	theme	oligosaccharides	1514:1529	arg1	asialo					1612:1617	asialo	1612:1617	asialo	1612:1617	The remainder of the oligosaccharides attached to Asn-300 were diantennary N-acetyllactosamine-type, of which 10% were asialo, 61% were monosialyl, and 29% were disialyl.
2001369	10	60	theme	oligosaccharides	1514:1529	arg1	remainder					1497:1505	The remainder	1493:1505	The remainder of the oligosaccharides attached to Asn-300	1493:1549	The remainder of the oligosaccharides attached to Asn-300 were diantennary N-acetyllactosamine-type, of which 10% were asialo, 61% were monosialyl, and 29% were disialyl.
2001369	10	60	theme	oligosaccharides	1514:1529	arg1	disialyl					1654:1661	disialyl	1654:1661	disialyl	1654:1661	The remainder of the oligosaccharides attached to Asn-300 were diantennary N-acetyllactosamine-type, of which 10% were asialo, 61% were monosialyl, and 29% were disialyl.
2001369	11	61	theme	structures	1695:1704	arg1	%					1712:1712	40%	1710:1712	40% of the N-acetyllactosamine structures at Asn-300	1710:1761	Approximately 9% of the hybrid structures and 40% of the N-acetyllactosamine structures at Asn-300 were found to contain fucose alpha(1-->6) linked to the innermost GlcNAc residue.
2001369	11	61	theme	structures	1695:1704	arg1	%					1679:1679	Approximately 9%	1664:1679	Approximately 9% of the hybrid structures	1664:1704	Approximately 9% of the hybrid structures and 40% of the N-acetyllactosamine structures at Asn-300 were found to contain fucose alpha(1-->6) linked to the innermost GlcNAc residue.
2001369	11	61	theme	structures	1695:1704	arg1	structures					1741:1750	the N-acetyllactosamine structures	1717:1750	the N-acetyllactosamine structures at Asn-300	1717:1761	Approximately 9% of the hybrid structures and 40% of the N-acetyllactosamine structures at Asn-300 were found to contain fucose alpha(1-->6) linked to the innermost GlcNAc residue.
2001369	11	61	theme	structures	1695:1704	arg1	structures					1695:1704	the hybrid structures	1684:1704	the hybrid structures	1684:1704	Approximately 9% of the hybrid structures and 40% of the N-acetyllactosamine structures at Asn-300 were found to contain fucose alpha(1-->6) linked to the innermost GlcNAc residue.
2001369	1	62	gly	glycoprotein	269:280	arg1	glycoprotein					269:280	the cell-surface receptor glycoprotein CD4	243:284	the cell-surface receptor glycoprotein CD4	243:284	Infection of T-lymphocytes and macrophages by human immunodeficiency virus (HIV) is mediated by the binding of the HIV envelope glycoprotein to the cell-surface receptor glycoprotein CD4.
2001369	1	63	theme	T-lymphocytes	112:124	arg1	Infection					99:107	Infection	99:107	Infection of T-lymphocytes and macrophages by human immunodeficiency virus (HIV)	99:178	Infection of T-lymphocytes and macrophages by human immunodeficiency virus (HIV) is mediated by the binding of the HIV envelope glycoprotein to the cell-surface receptor glycoprotein CD4.
2001369	8	64	theme	reducing	1361:1368	arg1	residue					1377:1383	the reducing GlcNAc residue	1357:1383	the reducing GlcNAc residue	1357:1383	Approximately 18% of these structures contained fucose alpha(1-->6) linked to the reducing GlcNAc residue.
2001369	2	65	dep	soluble	289:295	arg1	recombinant					298:308	recombinant	298:308	recombinant	298:308	A soluble, recombinant CD4 molecule (rCD4), produced by expression of a truncated CD4 gene in Chinese hamster ovary (CHO) cells [Smith et al. (1987) Science 238, 1704-1707], is in clinical trials as a potential therapeutic agent in the treatment of acquired immunodeficiency syndrome (AIDS).
2001369	4	66	theme	rCD4	693:696	arg1	molecule					698:705	The rCD4 molecule	689:705	The rCD4 molecule	689:705	The rCD4 molecule has two potential sites for N-glycosylation, Asn-271 and Asn-300.
2001369	11	67	theme	GlcNAc	1829:1834	arg1	residue					1836:1842	the innermost GlcNAc residue	1815:1842	the innermost GlcNAc residue	1815:1842	Approximately 9% of the hybrid structures and 40% of the N-acetyllactosamine structures at Asn-300 were found to contain fucose alpha(1-->6) linked to the innermost GlcNAc residue.
2001369	9	68	theme	different	1390:1398	arg1	structures					1407:1416	Two different hybrid structures	1386:1416	Two different hybrid structures	1386:1416	Two different hybrid structures were found to account for 34% of the oligosaccharides attached to Asn-300.
2001369	2	69	theme	clinical	467:474	arg1	trials					476:481	clinical trials	467:481	clinical trials	467:481	A soluble, recombinant CD4 molecule (rCD4), produced by expression of a truncated CD4 gene in Chinese hamster ovary (CHO) cells [Smith et al. (1987) Science 238, 1704-1707], is in clinical trials as a potential therapeutic agent in the treatment of acquired immunodeficiency syndrome (AIDS).
2001369	11	70	from	Asn-300	1755:1761	arg1	%					1712:1712	40%	1710:1712	40% of the N-acetyllactosamine structures at Asn-300	1710:1761	Approximately 9% of the hybrid structures and 40% of the N-acetyllactosamine structures at Asn-300 were found to contain fucose alpha(1-->6) linked to the innermost GlcNAc residue.
2001369	11	70	from	Asn-300	1755:1761	arg1	%					1679:1679	Approximately 9%	1664:1679	Approximately 9% of the hybrid structures	1664:1704	Approximately 9% of the hybrid structures and 40% of the N-acetyllactosamine structures at Asn-300 were found to contain fucose alpha(1-->6) linked to the innermost GlcNAc residue.
2001369	11	70	from	Asn-300	1755:1761	arg1	structures					1741:1750	the N-acetyllactosamine structures	1717:1750	the N-acetyllactosamine structures at Asn-300	1717:1761	Approximately 9% of the hybrid structures and 40% of the N-acetyllactosamine structures at Asn-300 were found to contain fucose alpha(1-->6) linked to the innermost GlcNAc residue.
2001369	11	70	from	Asn-300	1755:1761	arg1	structures					1695:1704	the hybrid structures	1684:1704	the hybrid structures	1684:1704	Approximately 9% of the hybrid structures and 40% of the N-acetyllactosamine structures at Asn-300 were found to contain fucose alpha(1-->6) linked to the innermost GlcNAc residue.
2001369	4	71	contain	has	707:709	arg1	molecule					698:705	The rCD4 molecule	689:705	The rCD4 molecule	689:705	The rCD4 molecule has two potential sites for N-glycosylation, Asn-271 and Asn-300.
2001369	4	71	contain	has	707:709	arg2	sites					725:729	two potential sites	711:729	two potential sites for N-glycosylation, Asn-271 and Asn-300	711:770	The rCD4 molecule has two potential sites for N-glycosylation, Asn-271 and Asn-300.
2001369	0	72	theme	Chinese	70:76	arg1	cells					92:96	Chinese hamster ovary cells	70:96	Chinese hamster ovary cells	70:96	Carbohydrate structures of recombinant soluble human CD4 expressed in Chinese hamster ovary cells.
2001369	1	73	theme	human	145:149	arg1	HIV					175:177	HIV	175:177	HIV	175:177	Infection of T-lymphocytes and macrophages by human immunodeficiency virus (HIV) is mediated by the binding of the HIV envelope glycoprotein to the cell-surface receptor glycoprotein CD4.
2001369	1	73	theme	human	145:149	arg1	virus					168:172	human immunodeficiency virus	145:172	human immunodeficiency virus (HIV)	145:178	Infection of T-lymphocytes and macrophages by human immunodeficiency virus (HIV) is mediated by the binding of the HIV envelope glycoprotein to the cell-surface receptor glycoprotein CD4.
2001369	7	74	theme	diantennary	1143:1153	arg1	oligosaccharides					1192:1207	diantennary N-acetyllactosamine-type ("complex") oligosaccharides	1143:1207	diantennary N-acetyllactosamine-type ("complex") oligosaccharides	1143:1207	Asn-271 was found to carry diantennary N-acetyllactosamine-type ("complex") oligosaccharides, of which 8% were asialo, 55% were monosialyl, and 37% were disialyl.
2001369	0	75	theme	ovary	86:90	arg1	cells					92:96	Chinese hamster ovary cells	70:96	Chinese hamster ovary cells	70:96	Carbohydrate structures of recombinant soluble human CD4 expressed in Chinese hamster ovary cells.
2001369	2	76	theme	syndrome	562:569	arg1	treatment					523:531	the treatment	519:531	the treatment of acquired immunodeficiency syndrome (AIDS)	519:576	A soluble, recombinant CD4 molecule (rCD4), produced by expression of a truncated CD4 gene in Chinese hamster ovary (CHO) cells [Smith et al. (1987) Science 238, 1704-1707], is in clinical trials as a potential therapeutic agent in the treatment of acquired immunodeficiency syndrome (AIDS).
2001369	2	77	theme	truncated	359:367	arg1	gene					373:376	a truncated CD4 gene	357:376	a truncated CD4 gene	357:376	A soluble, recombinant CD4 molecule (rCD4), produced by expression of a truncated CD4 gene in Chinese hamster ovary (CHO) cells [Smith et al. (1987) Science 238, 1704-1707], is in clinical trials as a potential therapeutic agent in the treatment of acquired immunodeficiency syndrome (AIDS).
2001369	5	78	theme	reversed-phase	843:856	arg1	HPLC					858:861	reversed-phase HPLC	843:861	reversed-phase HPLC	843:861	Tryptic glycopeptides containing either of the sites were purified by reversed-phase HPLC, and their oligosaccharides were released enzymatically.
2001369	6	79	theme	high-pH	1000:1006	arg1	chromatography					1023:1036	high-pH anion-exchange chromatography	1000:1036	high-pH anion-exchange chromatography	1000:1036	The structures of the oligosaccharides were determined by methylation analysis, high-pH anion-exchange chromatography, fast-atom bombardment mass spectrometry, and 1H NMR spectroscopy at 500 MHz.
2001369	2	80	theme	CHO	404:406	arg1	cells					409:413	Chinese hamster ovary (CHO) cells	381:413	Chinese hamster ovary (CHO) cells [Smith et al	381:426	A soluble, recombinant CD4 molecule (rCD4), produced by expression of a truncated CD4 gene in Chinese hamster ovary (CHO) cells [Smith et al. (1987) Science 238, 1704-1707], is in clinical trials as a potential therapeutic agent in the treatment of acquired immunodeficiency syndrome (AIDS).
2001369	11	81	from	%	1712:1712	arg1	Asn-300					1755:1761	Asn-300	1755:1761	Asn-300	1755:1761	Approximately 9% of the hybrid structures and 40% of the N-acetyllactosamine structures at Asn-300 were found to contain fucose alpha(1-->6) linked to the innermost GlcNAc residue.
2001369	0	82	theme	recombinant	27:37	arg1	CD4					53:55	recombinant soluble human CD4	27:55	recombinant soluble human CD4	27:55	Carbohydrate structures of recombinant soluble human CD4 expressed in Chinese hamster ovary cells.
2001369	9	83	theme	oligosaccharides	1455:1470	arg1	%					1446:1446	34%	1444:1446	34% of the oligosaccharides attached to Asn-300	1444:1490	Two different hybrid structures were found to account for 34% of the oligosaccharides attached to Asn-300.
2001369	9	83	theme	oligosaccharides	1455:1470	arg1	oligosaccharides					1455:1470	the oligosaccharides	1451:1470	the oligosaccharides attached to Asn-300	1451:1490	Two different hybrid structures were found to account for 34% of the oligosaccharides attached to Asn-300.
2001369	2	84	theme	ovary	397:401	arg1	cells					409:413	Chinese hamster ovary (CHO) cells	381:413	Chinese hamster ovary (CHO) cells [Smith et al	381:426	A soluble, recombinant CD4 molecule (rCD4), produced by expression of a truncated CD4 gene in Chinese hamster ovary (CHO) cells [Smith et al. (1987) Science 238, 1704-1707], is in clinical trials as a potential therapeutic agent in the treatment of acquired immunodeficiency syndrome (AIDS).
2001369	2	85	theme	Chinese	381:387	arg1	cells					409:413	Chinese hamster ovary (CHO) cells	381:413	Chinese hamster ovary (CHO) cells [Smith et al	381:426	A soluble, recombinant CD4 molecule (rCD4), produced by expression of a truncated CD4 gene in Chinese hamster ovary (CHO) cells [Smith et al. (1987) Science 238, 1704-1707], is in clinical trials as a potential therapeutic agent in the treatment of acquired immunodeficiency syndrome (AIDS).
2001369	0	86	theme	human	47:51	arg1	CD4					53:55	recombinant soluble human CD4	27:55	recombinant soluble human CD4	27:55	Carbohydrate structures of recombinant soluble human CD4 expressed in Chinese hamster ovary cells.
2001369	11	87	theme	fucose	1785:1790	arg1	1-->6					1798:1802	1-->6	1798:1802	1-->6	1798:1802	Approximately 9% of the hybrid structures and 40% of the N-acetyllactosamine structures at Asn-300 were found to contain fucose alpha(1-->6) linked to the innermost GlcNAc residue.
2001369	11	87	theme	fucose	1785:1790	arg1	alpha					1792:1796	fucose alpha	1785:1796	fucose alpha(1-->6) linked to the innermost GlcNAc residue	1785:1842	Approximately 9% of the hybrid structures and 40% of the N-acetyllactosamine structures at Asn-300 were found to contain fucose alpha(1-->6) linked to the innermost GlcNAc residue.
2001369	6	88	theme	1H	1084:1085	arg1	spectroscopy					1091:1102	1H NMR spectroscopy	1084:1102	1H NMR spectroscopy	1084:1102	The structures of the oligosaccharides were determined by methylation analysis, high-pH anion-exchange chromatography, fast-atom bombardment mass spectrometry, and 1H NMR spectroscopy at 500 MHz.
2001369	10	89	theme	which	1597:1601	arg1	N-acetyllactosamine-type					1568:1591	N-acetyllactosamine-type	1568:1591	N-acetyllactosamine-type	1568:1591	The remainder of the oligosaccharides attached to Asn-300 were diantennary N-acetyllactosamine-type, of which 10% were asialo, 61% were monosialyl, and 29% were disialyl.
2001369	10	89	theme	which	1597:1601	arg1	remainder					1497:1505	The remainder	1493:1505	The remainder of the oligosaccharides attached to Asn-300	1493:1549	The remainder of the oligosaccharides attached to Asn-300 were diantennary N-acetyllactosamine-type, of which 10% were asialo, 61% were monosialyl, and 29% were disialyl.
2001369	10	89	theme	which	1597:1601	arg1	asialo					1612:1617	asialo	1612:1617	asialo	1612:1617	The remainder of the oligosaccharides attached to Asn-300 were diantennary N-acetyllactosamine-type, of which 10% were asialo, 61% were monosialyl, and 29% were disialyl.
2001369	10	89	theme	which	1597:1601	arg1	disialyl					1654:1661	disialyl	1654:1661	disialyl	1654:1661	The remainder of the oligosaccharides attached to Asn-300 were diantennary N-acetyllactosamine-type, of which 10% were asialo, 61% were monosialyl, and 29% were disialyl.
2001369	8	90	attach	linked	1347:1352	arg2	1-->6					1340:1344	1-->6	1340:1344	1-->6	1340:1344	Approximately 18% of these structures contained fucose alpha(1-->6) linked to the reducing GlcNAc residue.
2001369	8	90	attach	linked	1347:1352	arg2	alpha					1334:1338	fucose alpha	1327:1338	fucose alpha(1-->6) linked to the reducing GlcNAc residue	1327:1383	Approximately 18% of these structures contained fucose alpha(1-->6) linked to the reducing GlcNAc residue.
2001369	8	90	attach	linked	1347:1352	arg1	residue					1377:1383	the reducing GlcNAc residue	1357:1383	the reducing GlcNAc residue	1357:1383	Approximately 18% of these structures contained fucose alpha(1-->6) linked to the reducing GlcNAc residue.
2001369	1	91	theme	HIV	214:216	arg1	glycoprotein					227:238	the HIV envelope glycoprotein	210:238	the HIV envelope glycoprotein	210:238	Infection of T-lymphocytes and macrophages by human immunodeficiency virus (HIV) is mediated by the binding of the HIV envelope glycoprotein to the cell-surface receptor glycoprotein CD4.
2001369	7	92	theme	oligosaccharides	1192:1207	arg1	asialo					1227:1232	asialo	1227:1232	asialo	1227:1232	Asn-271 was found to carry diantennary N-acetyllactosamine-type ("complex") oligosaccharides, of which 8% were asialo, 55% were monosialyl, and 37% were disialyl.
2001369	1	93	theme	glycoprotein	227:238	arg1	binding					199:205	the binding	195:205	the binding of the HIV envelope glycoprotein to the cell-surface receptor glycoprotein CD4	195:284	Infection of T-lymphocytes and macrophages by human immunodeficiency virus (HIV) is mediated by the binding of the HIV envelope glycoprotein to the cell-surface receptor glycoprotein CD4.
3949763	4	0	theme	secondary	496:504	arg1	structure					506:514	secondary structure	496:514	secondary structure	496:514	In addition, the sites of glycosylation, assignment of disulfide bonds, and the circular dichroism of the hormone analyzed for secondary structure in comparison with the prediction from the sequence are presented.
3949763	4	1	theme	hormone	475:481	arg1	sites					386:390	the sites	382:390	the sites of glycosylation	382:407	In addition, the sites of glycosylation, assignment of disulfide bonds, and the circular dichroism of the hormone analyzed for secondary structure in comparison with the prediction from the sequence are presented.
3949763	4	1	theme	hormone	475:481	arg1	bonds					434:438	disulfide bonds	424:438	disulfide bonds	424:438	In addition, the sites of glycosylation, assignment of disulfide bonds, and the circular dichroism of the hormone analyzed for secondary structure in comparison with the prediction from the sequence are presented.
3949763	4	1	theme	hormone	475:481	arg1	hormone					475:481	the hormone	471:481	the hormone analyzed for secondary structure in comparison with the prediction from the sequence	471:566	In addition, the sites of glycosylation, assignment of disulfide bonds, and the circular dichroism of the hormone analyzed for secondary structure in comparison with the prediction from the sequence are presented.
3949763	4	1	theme	hormone	475:481	arg1	glycosylation					395:407	glycosylation	395:407	glycosylation	395:407	In addition, the sites of glycosylation, assignment of disulfide bonds, and the circular dichroism of the hormone analyzed for secondary structure in comparison with the prediction from the sequence are presented.
3949763	4	1	theme	hormone	475:481	arg1	assignment					410:419	assignment	410:419	assignment of disulfide bonds	410:438	In addition, the sites of glycosylation, assignment of disulfide bonds, and the circular dichroism of the hormone analyzed for secondary structure in comparison with the prediction from the sequence are presented.
3949763	4	1	theme	hormone	475:481	arg1	dichroism					458:466	the circular dichroism	445:466	the circular dichroism of the hormone analyzed for secondary structure in comparison with the prediction from the sequence	445:566	In addition, the sites of glycosylation, assignment of disulfide bonds, and the circular dichroism of the hormone analyzed for secondary structure in comparison with the prediction from the sequence are presented.
3949763	4	2	theme	glycosylation	395:407	arg1	sites					386:390	the sites	382:390	the sites of glycosylation	382:407	In addition, the sites of glycosylation, assignment of disulfide bonds, and the circular dichroism of the hormone analyzed for secondary structure in comparison with the prediction from the sequence are presented.
3949763	4	2	theme	glycosylation	395:407	arg1	bonds					434:438	disulfide bonds	424:438	disulfide bonds	424:438	In addition, the sites of glycosylation, assignment of disulfide bonds, and the circular dichroism of the hormone analyzed for secondary structure in comparison with the prediction from the sequence are presented.
3949763	4	2	theme	glycosylation	395:407	arg1	hormone					475:481	the hormone	471:481	the hormone analyzed for secondary structure in comparison with the prediction from the sequence	471:566	In addition, the sites of glycosylation, assignment of disulfide bonds, and the circular dichroism of the hormone analyzed for secondary structure in comparison with the prediction from the sequence are presented.
3949763	4	2	theme	glycosylation	395:407	arg1	glycosylation					395:407	glycosylation	395:407	glycosylation	395:407	In addition, the sites of glycosylation, assignment of disulfide bonds, and the circular dichroism of the hormone analyzed for secondary structure in comparison with the prediction from the sequence are presented.
3949763	4	2	theme	glycosylation	395:407	arg1	assignment					410:419	assignment	410:419	assignment of disulfide bonds	410:438	In addition, the sites of glycosylation, assignment of disulfide bonds, and the circular dichroism of the hormone analyzed for secondary structure in comparison with the prediction from the sequence are presented.
3949763	4	2	theme	glycosylation	395:407	arg1	dichroism					458:466	the circular dichroism	445:466	the circular dichroism of the hormone analyzed for secondary structure in comparison with the prediction from the sequence	445:566	In addition, the sites of glycosylation, assignment of disulfide bonds, and the circular dichroism of the hormone analyzed for secondary structure in comparison with the prediction from the sequence are presented.
3949763	2	3	theme	scarcity	156:163	arg1	available					193:201	available	193:201	available	193:201	Because of its extreme scarcity, very little information is available regarding structural features of this important glycoprotein.
3949763	1	4	theme	primary	75:81	arg1	regulator					83:91	the primary regulator	71:91	the primary regulator of red blood cell formation in mammals	71:130	Erythropoietin is the primary regulator of red blood cell formation in mammals.
3949763	1	4	theme	primary	75:81	arg1	Erythropoietin					53:66	Erythropoietin	53:66	Erythropoietin	53:66	Erythropoietin is the primary regulator of red blood cell formation in mammals.
3949763	2	5	theme	extreme	148:154	arg1	scarcity					156:163	its extreme scarcity	144:163	its extreme scarcity	144:163	Because of its extreme scarcity, very little information is available regarding structural features of this important glycoprotein.
3949763	1	6	theme	red	96:98	arg1	formation					111:119	red blood cell formation	96:119	red blood cell formation	96:119	Erythropoietin is the primary regulator of red blood cell formation in mammals.
3949763	0	7	theme	Structural	0:9	arg1	characterization					11:26	Structural characterization	0:26	Structural characterization of human erythropoietin.	0:51	Structural characterization of human erythropoietin.
3949763	4	8	theme	bonds	434:438	arg1	sites					386:390	the sites	382:390	the sites of glycosylation	382:407	In addition, the sites of glycosylation, assignment of disulfide bonds, and the circular dichroism of the hormone analyzed for secondary structure in comparison with the prediction from the sequence are presented.
3949763	4	8	theme	bonds	434:438	arg1	bonds					434:438	disulfide bonds	424:438	disulfide bonds	424:438	In addition, the sites of glycosylation, assignment of disulfide bonds, and the circular dichroism of the hormone analyzed for secondary structure in comparison with the prediction from the sequence are presented.
3949763	4	8	theme	bonds	434:438	arg1	hormone					475:481	the hormone	471:481	the hormone analyzed for secondary structure in comparison with the prediction from the sequence	471:566	In addition, the sites of glycosylation, assignment of disulfide bonds, and the circular dichroism of the hormone analyzed for secondary structure in comparison with the prediction from the sequence are presented.
3949763	4	8	theme	bonds	434:438	arg1	glycosylation					395:407	glycosylation	395:407	glycosylation	395:407	In addition, the sites of glycosylation, assignment of disulfide bonds, and the circular dichroism of the hormone analyzed for secondary structure in comparison with the prediction from the sequence are presented.
3949763	4	8	theme	bonds	434:438	arg1	assignment					410:419	assignment	410:419	assignment of disulfide bonds	410:438	In addition, the sites of glycosylation, assignment of disulfide bonds, and the circular dichroism of the hormone analyzed for secondary structure in comparison with the prediction from the sequence are presented.
3949763	4	8	theme	bonds	434:438	arg1	dichroism					458:466	the circular dichroism	445:466	the circular dichroism of the hormone analyzed for secondary structure in comparison with the prediction from the sequence	445:566	In addition, the sites of glycosylation, assignment of disulfide bonds, and the circular dichroism of the hormone analyzed for secondary structure in comparison with the prediction from the sequence are presented.
3949763	1	9	theme	blood	100:104	arg1	formation					111:119	red blood cell formation	96:119	red blood cell formation	96:119	Erythropoietin is the primary regulator of red blood cell formation in mammals.
3949763	2	10	gly	glycoprotein	251:262	arg1	glycoprotein					251:262	this important glycoprotein	236:262	this important glycoprotein	236:262	Because of its extreme scarcity, very little information is available regarding structural features of this important glycoprotein.
3949763	3	11	theme	primary	284:290	arg1	structure					292:300	the primary structure	280:300	the primary structure	280:300	We report here the primary structure of human urinary erythropoietin, determined by protein sequencing.
3949763	1	12	theme	cell	106:109	arg1	formation					111:119	red blood cell formation	96:119	red blood cell formation	96:119	Erythropoietin is the primary regulator of red blood cell formation in mammals.
3949763	4	13	theme	circular	449:456	arg1	dichroism					458:466	the circular dichroism	445:466	the circular dichroism of the hormone analyzed for secondary structure in comparison with the prediction from the sequence	445:566	In addition, the sites of glycosylation, assignment of disulfide bonds, and the circular dichroism of the hormone analyzed for secondary structure in comparison with the prediction from the sequence are presented.
3949763	1	14	theme	formation	111:119	arg1	regulator					83:91	the primary regulator	71:91	the primary regulator of red blood cell formation in mammals	71:130	Erythropoietin is the primary regulator of red blood cell formation in mammals.
3949763	1	14	theme	formation	111:119	arg1	Erythropoietin					53:66	Erythropoietin	53:66	Erythropoietin	53:66	Erythropoietin is the primary regulator of red blood cell formation in mammals.
3949763	2	15	theme	little	171:176	arg1	information					178:188	very little information	166:188	very little information	166:188	Because of its extreme scarcity, very little information is available regarding structural features of this important glycoprotein.
3949763	2	16	theme	important	241:249	arg1	glycoprotein					251:262	this important glycoprotein	236:262	this important glycoprotein	236:262	Because of its extreme scarcity, very little information is available regarding structural features of this important glycoprotein.
3949763	0	17	theme	erythropoietin	37:50	arg1	characterization					11:26	Structural characterization	0:26	Structural characterization of human erythropoietin.	0:51	Structural characterization of human erythropoietin.
3949763	0	18	theme	human	31:35	arg1	erythropoietin					37:50	human erythropoietin	31:50	human erythropoietin	31:50	Structural characterization of human erythropoietin.
3949763	4	19	from	sequence	559:566	arg1	prediction					539:548	the prediction	535:548	the prediction from the sequence	535:566	In addition, the sites of glycosylation, assignment of disulfide bonds, and the circular dichroism of the hormone analyzed for secondary structure in comparison with the prediction from the sequence are presented.
3949763	3	20	theme	urinary	311:317	arg1	erythropoietin					319:332	human urinary erythropoietin	305:332	human urinary erythropoietin	305:332	We report here the primary structure of human urinary erythropoietin, determined by protein sequencing.
3949763	4	21	with	comparison	519:528	arg1	prediction					539:548	the prediction	535:548	the prediction from the sequence	535:566	In addition, the sites of glycosylation, assignment of disulfide bonds, and the circular dichroism of the hormone analyzed for secondary structure in comparison with the prediction from the sequence are presented.
3949763	3	22	theme	erythropoietin	319:332	arg1	structure					292:300	the primary structure	280:300	the primary structure	280:300	We report here the primary structure of human urinary erythropoietin, determined by protein sequencing.
3949763	2	23	theme	structural	213:222	arg1	features					224:231	structural features	213:231	structural features of this important glycoprotein	213:262	Because of its extreme scarcity, very little information is available regarding structural features of this important glycoprotein.
3949763	4	24	theme	disulfide	424:432	arg1	bonds					434:438	disulfide bonds	424:438	disulfide bonds	424:438	In addition, the sites of glycosylation, assignment of disulfide bonds, and the circular dichroism of the hormone analyzed for secondary structure in comparison with the prediction from the sequence are presented.
3949763	4	25	gly	glycosylation	395:407	arg2	bonds					434:438	disulfide bonds	424:438	disulfide bonds	424:438	In addition, the sites of glycosylation, assignment of disulfide bonds, and the circular dichroism of the hormone analyzed for secondary structure in comparison with the prediction from the sequence are presented.
3949763	4	25	gly	glycosylation	395:407	arg2	glycosylation					395:407	glycosylation	395:407	glycosylation	395:407	In addition, the sites of glycosylation, assignment of disulfide bonds, and the circular dichroism of the hormone analyzed for secondary structure in comparison with the prediction from the sequence are presented.
3949763	4	25	gly	glycosylation	395:407	arg2	hormone					475:481	the hormone	471:481	the hormone analyzed for secondary structure in comparison with the prediction from the sequence	471:566	In addition, the sites of glycosylation, assignment of disulfide bonds, and the circular dichroism of the hormone analyzed for secondary structure in comparison with the prediction from the sequence are presented.
3949763	4	25	gly	glycosylation	395:407	arg2	sites					386:390	the sites	382:390	the sites of glycosylation	382:407	In addition, the sites of glycosylation, assignment of disulfide bonds, and the circular dichroism of the hormone analyzed for secondary structure in comparison with the prediction from the sequence are presented.
3949763	3	26	theme	human	305:309	arg1	erythropoietin					319:332	human urinary erythropoietin	305:332	human urinary erythropoietin	305:332	We report here the primary structure of human urinary erythropoietin, determined by protein sequencing.
3949763	3	27	theme	protein	349:355	arg1	sequencing					357:366	protein sequencing	349:366	protein sequencing	349:366	We report here the primary structure of human urinary erythropoietin, determined by protein sequencing.
3949763	2	28	theme	glycoprotein	251:262	arg1	features					224:231	structural features	213:231	structural features of this important glycoprotein	213:262	Because of its extreme scarcity, very little information is available regarding structural features of this important glycoprotein.
3949763	1	29	from	regulator	83:91	arg1	mammals					124:130	mammals	124:130	mammals	124:130	Erythropoietin is the primary regulator of red blood cell formation in mammals.
7106126	3	0	contain	contain	484:490	arg1	fragment					437:444	The fragment	433:444	The fragment	433:444	The fragment, comprising 47 residues, was found to contain an average of about 12 O-glycosidically linked oligosaccharides and one asparagine-linked carbohydrate chain.
7106126	3	0	contain	contain	484:490	arg2	average					495:501	an average	492:501	an average of about 12 O-glycosidically linked oligosaccharides and one asparagine-linked carbohydrate chain	492:599	The fragment, comprising 47 residues, was found to contain an average of about 12 O-glycosidically linked oligosaccharides and one asparagine-linked carbohydrate chain.
7106126	1	1	theme	N-terminal	135:144	arg1	glycopeptide					154:165	the N-terminal tryptic glycopeptide	131:165	the N-terminal tryptic glycopeptide from a minor human erythrocyte membrane sialoglycoprotein (component D or glycophorin C)	131:254	The amino acid sequence of the N-terminal tryptic glycopeptide from a minor human erythrocyte membrane sialoglycoprotein (component D or glycophorin C) was determined by manual sequencing.
7106126	1	2	theme	glycophorin	241:251	arg1	C					253:253	glycophorin C	241:253	glycophorin C	241:253	The amino acid sequence of the N-terminal tryptic glycopeptide from a minor human erythrocyte membrane sialoglycoprotein (component D or glycophorin C) was determined by manual sequencing.
7106126	3	3	link	asparagine-linked	564:580	arg1	chain					595:599	one asparagine-linked carbohydrate chain	560:599	one asparagine-linked carbohydrate chain	560:599	The fragment, comprising 47 residues, was found to contain an average of about 12 O-glycosidically linked oligosaccharides and one asparagine-linked carbohydrate chain.
7106126	1	4	gly	glycopeptide	154:165	arg2	glycopeptide					154:165	the N-terminal tryptic glycopeptide	131:165	the N-terminal tryptic glycopeptide from a minor human erythrocyte membrane sialoglycoprotein (component D or glycophorin C)	131:254	The amino acid sequence of the N-terminal tryptic glycopeptide from a minor human erythrocyte membrane sialoglycoprotein (component D or glycophorin C) was determined by manual sequencing.
7106126	1	4	gly	glycopeptide	154:165	arg1	sialoglycoprotein					207:223	a minor human erythrocyte membrane sialoglycoprotein	172:223	a minor human erythrocyte membrane sialoglycoprotein (component D or glycophorin C)	172:254	The amino acid sequence of the N-terminal tryptic glycopeptide from a minor human erythrocyte membrane sialoglycoprotein (component D or glycophorin C) was determined by manual sequencing.
7106126	1	5	theme	tryptic	146:152	arg1	glycopeptide					154:165	the N-terminal tryptic glycopeptide	131:165	the N-terminal tryptic glycopeptide from a minor human erythrocyte membrane sialoglycoprotein (component D or glycophorin C)	131:254	The amino acid sequence of the N-terminal tryptic glycopeptide from a minor human erythrocyte membrane sialoglycoprotein (component D or glycophorin C) was determined by manual sequencing.
7106126	0	6	theme	erythrocyte	81:91	arg1	membranes					93:101	human erythrocyte membranes	75:101	human erythrocyte membranes	75:101	N-terminal amino acid sequence of sialoglycoprotein D (glycophorin C) from human erythrocyte membranes.
7106126	1	7	dep	sialoglycoprotein	207:223	arg1	D					236:236	component D	226:236	component D	226:236	The amino acid sequence of the N-terminal tryptic glycopeptide from a minor human erythrocyte membrane sialoglycoprotein (component D or glycophorin C) was determined by manual sequencing.
7106126	1	7	dep	sialoglycoprotein	207:223	arg1	C					253:253	glycophorin C	241:253	glycophorin C	241:253	The amino acid sequence of the N-terminal tryptic glycopeptide from a minor human erythrocyte membrane sialoglycoprotein (component D or glycophorin C) was determined by manual sequencing.
7106126	5	8	theme	MN	879:880	arg1	region					865:870	a certain region	855:870	a certain region of the MN and Ss erythrocyte membrane sialoglycoproteins (glycophorins A and B)	855:950	In addition, a part of its structure shows a striking similarity to the sequence of a certain region of the MN and Ss erythrocyte membrane sialoglycoproteins (glycophorins A and B), suggesting that the molecules might be related.
7106126	4	9	theme	glycopeptide	668:679	arg1	regions					653:659	two regions	649:659	two regions of the glycopeptide	649:679	An identical hexapeptide sequence occurring in two regions of the glycopeptide provides evidence that it has developed by an internal gene duplication during evolution.
7106126	0	10	theme	human	75:79	arg1	membranes					93:101	human erythrocyte membranes	75:101	human erythrocyte membranes	75:101	N-terminal amino acid sequence of sialoglycoprotein D (glycophorin C) from human erythrocyte membranes.
7106126	3	11	theme	linked	532:537	arg1	oligosaccharides					539:554	about 12 O-glycosidically linked oligosaccharides	506:554	about 12 O-glycosidically linked oligosaccharides	506:554	The fragment, comprising 47 residues, was found to contain an average of about 12 O-glycosidically linked oligosaccharides and one asparagine-linked carbohydrate chain.
7106126	5	12	dep	glycophorins	930:941	arg1	glycophorins					930:941	glycophorins A and B	930:949	glycophorins A and B	930:949	In addition, a part of its structure shows a striking similarity to the sequence of a certain region of the MN and Ss erythrocyte membrane sialoglycoproteins (glycophorins A and B), suggesting that the molecules might be related.
7106126	5	12	dep	glycophorins	930:941	arg1	B					949:949	B	949:949	B	949:949	In addition, a part of its structure shows a striking similarity to the sequence of a certain region of the MN and Ss erythrocyte membrane sialoglycoproteins (glycophorins A and B), suggesting that the molecules might be related.
7106126	5	12	dep	glycophorins	930:941	arg1	A					943:943	A	943:943	A	943:943	In addition, a part of its structure shows a striking similarity to the sequence of a certain region of the MN and Ss erythrocyte membrane sialoglycoproteins (glycophorins A and B), suggesting that the molecules might be related.
7106126	5	13	theme	sialoglycoproteins	910:927	arg1	region					865:870	a certain region	855:870	a certain region of the MN and Ss erythrocyte membrane sialoglycoproteins (glycophorins A and B)	855:950	In addition, a part of its structure shows a striking similarity to the sequence of a certain region of the MN and Ss erythrocyte membrane sialoglycoproteins (glycophorins A and B), suggesting that the molecules might be related.
7106126	1	14	theme	glycopeptide	154:165	arg1	sequence					119:126	The amino acid sequence	104:126	The amino acid sequence of the N-terminal tryptic glycopeptide from a minor human erythrocyte membrane sialoglycoprotein (component D or glycophorin C)	104:254	The amino acid sequence of the N-terminal tryptic glycopeptide from a minor human erythrocyte membrane sialoglycoprotein (component D or glycophorin C) was determined by manual sequencing.
7106126	3	15	link	linked	532:537	arg1	oligosaccharides					539:554	about 12 O-glycosidically linked oligosaccharides	506:554	about 12 O-glycosidically linked oligosaccharides	506:554	The fragment, comprising 47 residues, was found to contain an average of about 12 O-glycosidically linked oligosaccharides and one asparagine-linked carbohydrate chain.
7106126	5	16	theme	Ss	886:887	arg1	sialoglycoproteins					910:927	the MN and Ss erythrocyte membrane sialoglycoproteins	875:927	sialoglycoproteins	910:927	In addition, a part of its structure shows a striking similarity to the sequence of a certain region of the MN and Ss erythrocyte membrane sialoglycoproteins (glycophorins A and B), suggesting that the molecules might be related.
7106126	2	17	gly	glycosylated	377:388	arg1	derivatives					390:400	the glycosylated derivatives	373:400	the glycosylated derivatives released by Edman degradation	373:430	The glycosylation sites were identified by a new procedure for the detection of the glycosylated derivatives released by Edman degradation.
7106126	4	18	theme	identical	605:613	arg1	sequence					627:634	An identical hexapeptide sequence	602:634	An identical hexapeptide sequence occurring in two regions of the glycopeptide	602:679	An identical hexapeptide sequence occurring in two regions of the glycopeptide provides evidence that it has developed by an internal gene duplication during evolution.
7106126	5	19	theme	certain	857:863	arg1	region					865:870	a certain region	855:870	a certain region of the MN and Ss erythrocyte membrane sialoglycoproteins (glycophorins A and B)	855:950	In addition, a part of its structure shows a striking similarity to the sequence of a certain region of the MN and Ss erythrocyte membrane sialoglycoproteins (glycophorins A and B), suggesting that the molecules might be related.
7106126	0	20	theme	amino	11:15	arg1	sequence					22:29	N-terminal amino acid sequence	0:29	N-terminal amino acid sequence of sialoglycoprotein D (glycophorin C) from human erythrocyte membranes	0:101	N-terminal amino acid sequence of sialoglycoprotein D (glycophorin C) from human erythrocyte membranes.
7106126	1	21	gly	sialoglycoprotein	207:223	arg1	sialoglycoprotein					207:223	a minor human erythrocyte membrane sialoglycoprotein	172:223	a minor human erythrocyte membrane sialoglycoprotein (component D or glycophorin C)	172:254	The amino acid sequence of the N-terminal tryptic glycopeptide from a minor human erythrocyte membrane sialoglycoprotein (component D or glycophorin C) was determined by manual sequencing.
7106126	1	22	from	sequence	119:126	arg1	sialoglycoprotein					207:223	a minor human erythrocyte membrane sialoglycoprotein	172:223	a minor human erythrocyte membrane sialoglycoprotein (component D or glycophorin C)	172:254	The amino acid sequence of the N-terminal tryptic glycopeptide from a minor human erythrocyte membrane sialoglycoprotein (component D or glycophorin C) was determined by manual sequencing.
7106126	5	23	theme	region	865:870	arg1	sequence					843:850	the sequence	839:850	the sequence of a certain region of the MN and Ss erythrocyte membrane sialoglycoproteins (glycophorins A and B)	839:950	In addition, a part of its structure shows a striking similarity to the sequence of a certain region of the MN and Ss erythrocyte membrane sialoglycoproteins (glycophorins A and B), suggesting that the molecules might be related.
7106126	0	24	theme	N-terminal	0:9	arg1	sequence					22:29	N-terminal amino acid sequence	0:29	N-terminal amino acid sequence of sialoglycoprotein D (glycophorin C) from human erythrocyte membranes	0:101	N-terminal amino acid sequence of sialoglycoprotein D (glycophorin C) from human erythrocyte membranes.
7106126	4	25	gly	glycopeptide	668:679	arg2	glycopeptide					668:679	the glycopeptide	664:679	the glycopeptide	664:679	An identical hexapeptide sequence occurring in two regions of the glycopeptide provides evidence that it has developed by an internal gene duplication during evolution.
7106126	2	26	theme	glycosylation	297:309	arg1	sites					311:315	The glycosylation sites	293:315	The glycosylation sites	293:315	The glycosylation sites were identified by a new procedure for the detection of the glycosylated derivatives released by Edman degradation.
7106126	1	27	theme	minor	174:178	arg1	sialoglycoprotein					207:223	a minor human erythrocyte membrane sialoglycoprotein	172:223	a minor human erythrocyte membrane sialoglycoprotein (component D or glycophorin C)	172:254	The amino acid sequence of the N-terminal tryptic glycopeptide from a minor human erythrocyte membrane sialoglycoprotein (component D or glycophorin C) was determined by manual sequencing.
7106126	5	28	theme	striking	816:823	arg1	similarity					825:834	a striking similarity	814:834	a striking similarity to the sequence of a certain region of the MN and Ss erythrocyte membrane sialoglycoproteins (glycophorins A and B)	814:950	In addition, a part of its structure shows a striking similarity to the sequence of a certain region of the MN and Ss erythrocyte membrane sialoglycoproteins (glycophorins A and B), suggesting that the molecules might be related.
7106126	3	29	theme	oligosaccharides	539:554	arg1	average					495:501	an average	492:501	an average of about 12 O-glycosidically linked oligosaccharides and one asparagine-linked carbohydrate chain	492:599	The fragment, comprising 47 residues, was found to contain an average of about 12 O-glycosidically linked oligosaccharides and one asparagine-linked carbohydrate chain.
7106126	1	30	theme	human	180:184	arg1	sialoglycoprotein					207:223	a minor human erythrocyte membrane sialoglycoprotein	172:223	a minor human erythrocyte membrane sialoglycoprotein (component D or glycophorin C)	172:254	The amino acid sequence of the N-terminal tryptic glycopeptide from a minor human erythrocyte membrane sialoglycoprotein (component D or glycophorin C) was determined by manual sequencing.
7106126	0	31	theme	acid	17:20	arg1	sequence					22:29	N-terminal amino acid sequence	0:29	N-terminal amino acid sequence of sialoglycoprotein D (glycophorin C) from human erythrocyte membranes	0:101	N-terminal amino acid sequence of sialoglycoprotein D (glycophorin C) from human erythrocyte membranes.
7106126	1	32	theme	manual	274:279	arg1	sequencing					281:290	manual sequencing	274:290	manual sequencing	274:290	The amino acid sequence of the N-terminal tryptic glycopeptide from a minor human erythrocyte membrane sialoglycoprotein (component D or glycophorin C) was determined by manual sequencing.
7106126	2	33	theme	new	338:340	arg1	procedure					342:350	a new procedure	336:350	a new procedure for the detection of the glycosylated derivatives released by Edman degradation	336:430	The glycosylation sites were identified by a new procedure for the detection of the glycosylated derivatives released by Edman degradation.
7106126	1	34	theme	erythrocyte	186:196	arg1	sialoglycoprotein					207:223	a minor human erythrocyte membrane sialoglycoprotein	172:223	a minor human erythrocyte membrane sialoglycoprotein (component D or glycophorin C)	172:254	The amino acid sequence of the N-terminal tryptic glycopeptide from a minor human erythrocyte membrane sialoglycoprotein (component D or glycophorin C) was determined by manual sequencing.
7106126	0	35	theme	sialoglycoprotein	34:50	arg1	D					52:52	sialoglycoprotein D	34:52	sialoglycoprotein D (glycophorin C)	34:68	N-terminal amino acid sequence of sialoglycoprotein D (glycophorin C) from human erythrocyte membranes.
7106126	0	35	theme	sialoglycoprotein	34:50	arg1	C					67:67	glycophorin C	55:67	glycophorin C	55:67	N-terminal amino acid sequence of sialoglycoprotein D (glycophorin C) from human erythrocyte membranes.
7106126	5	36	theme	membrane	901:908	arg1	sialoglycoproteins					910:927	the MN and Ss erythrocyte membrane sialoglycoproteins	875:927	sialoglycoproteins	910:927	In addition, a part of its structure shows a striking similarity to the sequence of a certain region of the MN and Ss erythrocyte membrane sialoglycoproteins (glycophorins A and B), suggesting that the molecules might be related.
7106126	1	37	theme	membrane	198:205	arg1	sialoglycoprotein					207:223	a minor human erythrocyte membrane sialoglycoprotein	172:223	a minor human erythrocyte membrane sialoglycoprotein (component D or glycophorin C)	172:254	The amino acid sequence of the N-terminal tryptic glycopeptide from a minor human erythrocyte membrane sialoglycoprotein (component D or glycophorin C) was determined by manual sequencing.
7106126	2	38	theme	glycosylated	377:388	arg1	derivatives					390:400	the glycosylated derivatives	373:400	the glycosylated derivatives released by Edman degradation	373:430	The glycosylation sites were identified by a new procedure for the detection of the glycosylated derivatives released by Edman degradation.
7106126	5	39	gly	sialoglycoproteins	910:927	arg1	sialoglycoproteins					910:927	the MN and Ss erythrocyte membrane sialoglycoproteins	875:927	sialoglycoproteins	910:927	In addition, a part of its structure shows a striking similarity to the sequence of a certain region of the MN and Ss erythrocyte membrane sialoglycoproteins (glycophorins A and B), suggesting that the molecules might be related.
7106126	2	40	theme	derivatives	390:400	arg1	detection					360:368	the detection	356:368	the detection of the glycosylated derivatives released by Edman degradation	356:430	The glycosylation sites were identified by a new procedure for the detection of the glycosylated derivatives released by Edman degradation.
7106126	5	41	theme	structure	798:806	arg1	part					786:789	a part	784:789	a part of its structure	784:806	In addition, a part of its structure shows a striking similarity to the sequence of a certain region of the MN and Ss erythrocyte membrane sialoglycoproteins (glycophorins A and B), suggesting that the molecules might be related.
7106126	3	42	theme	carbohydrate	582:593	arg1	chain					595:599	one asparagine-linked carbohydrate chain	560:599	one asparagine-linked carbohydrate chain	560:599	The fragment, comprising 47 residues, was found to contain an average of about 12 O-glycosidically linked oligosaccharides and one asparagine-linked carbohydrate chain.
7106126	1	43	from	sialoglycoprotein	207:223	arg1	glycopeptide					154:165	the N-terminal tryptic glycopeptide	131:165	the N-terminal tryptic glycopeptide from a minor human erythrocyte membrane sialoglycoprotein (component D or glycophorin C)	131:254	The amino acid sequence of the N-terminal tryptic glycopeptide from a minor human erythrocyte membrane sialoglycoprotein (component D or glycophorin C) was determined by manual sequencing.
7106126	1	43	from	sialoglycoprotein	207:223	arg1	sequence					119:126	The amino acid sequence	104:126	The amino acid sequence of the N-terminal tryptic glycopeptide from a minor human erythrocyte membrane sialoglycoprotein (component D or glycophorin C)	104:254	The amino acid sequence of the N-terminal tryptic glycopeptide from a minor human erythrocyte membrane sialoglycoprotein (component D or glycophorin C) was determined by manual sequencing.
7106126	5	44	theme	erythrocyte	889:899	arg1	sialoglycoproteins					910:927	the MN and Ss erythrocyte membrane sialoglycoproteins	875:927	sialoglycoproteins	910:927	In addition, a part of its structure shows a striking similarity to the sequence of a certain region of the MN and Ss erythrocyte membrane sialoglycoproteins (glycophorins A and B), suggesting that the molecules might be related.
7106126	0	45	theme	D	52:52	arg1	sequence					22:29	N-terminal amino acid sequence	0:29	N-terminal amino acid sequence of sialoglycoprotein D (glycophorin C) from human erythrocyte membranes	0:101	N-terminal amino acid sequence of sialoglycoprotein D (glycophorin C) from human erythrocyte membranes.
7106126	3	46	theme	chain	595:599	arg1	average					495:501	an average	492:501	an average of about 12 O-glycosidically linked oligosaccharides and one asparagine-linked carbohydrate chain	492:599	The fragment, comprising 47 residues, was found to contain an average of about 12 O-glycosidically linked oligosaccharides and one asparagine-linked carbohydrate chain.
7106126	1	47	theme	amino	108:112	arg1	sequence					119:126	The amino acid sequence	104:126	The amino acid sequence of the N-terminal tryptic glycopeptide from a minor human erythrocyte membrane sialoglycoprotein (component D or glycophorin C)	104:254	The amino acid sequence of the N-terminal tryptic glycopeptide from a minor human erythrocyte membrane sialoglycoprotein (component D or glycophorin C) was determined by manual sequencing.
7106126	4	48	theme	gene	736:739	arg1	duplication					741:751	an internal gene duplication	724:751	an internal gene duplication	724:751	An identical hexapeptide sequence occurring in two regions of the glycopeptide provides evidence that it has developed by an internal gene duplication during evolution.
7106126	0	49	from	membranes	93:101	arg1	sequence					22:29	N-terminal amino acid sequence	0:29	N-terminal amino acid sequence of sialoglycoprotein D (glycophorin C) from human erythrocyte membranes	0:101	N-terminal amino acid sequence of sialoglycoprotein D (glycophorin C) from human erythrocyte membranes.
7106126	1	50	theme	acid	114:117	arg1	sequence					119:126	The amino acid sequence	104:126	The amino acid sequence of the N-terminal tryptic glycopeptide from a minor human erythrocyte membrane sialoglycoprotein (component D or glycophorin C)	104:254	The amino acid sequence of the N-terminal tryptic glycopeptide from a minor human erythrocyte membrane sialoglycoprotein (component D or glycophorin C) was determined by manual sequencing.
7106126	4	51	theme	hexapeptide	615:625	arg1	sequence					627:634	An identical hexapeptide sequence	602:634	An identical hexapeptide sequence occurring in two regions of the glycopeptide	602:679	An identical hexapeptide sequence occurring in two regions of the glycopeptide provides evidence that it has developed by an internal gene duplication during evolution.
7106126	0	52	gly	sialoglycoprotein	34:50	arg1	sialoglycoprotein					34:50	sialoglycoprotein D	34:52	sialoglycoprotein D (glycophorin C)	34:68	N-terminal amino acid sequence of sialoglycoprotein D (glycophorin C) from human erythrocyte membranes.
7106126	4	53	theme	internal	727:734	arg1	duplication					741:751	an internal gene duplication	724:751	an internal gene duplication	724:751	An identical hexapeptide sequence occurring in two regions of the glycopeptide provides evidence that it has developed by an internal gene duplication during evolution.
7106126	1	54	theme	component	226:234	arg1	D					236:236	component D	226:236	component D	226:236	The amino acid sequence of the N-terminal tryptic glycopeptide from a minor human erythrocyte membrane sialoglycoprotein (component D or glycophorin C) was determined by manual sequencing.
7106126	2	55	gly	glycosylation	297:309	arg2	sites					311:315	The glycosylation sites	293:315	The glycosylation sites	293:315	The glycosylation sites were identified by a new procedure for the detection of the glycosylated derivatives released by Edman degradation.
7106126	2	56	theme	Edman	414:418	arg1	degradation					420:430	Edman degradation	414:430	Edman degradation	414:430	The glycosylation sites were identified by a new procedure for the detection of the glycosylated derivatives released by Edman degradation.
7106126	0	57	theme	glycophorin	55:65	arg1	D					52:52	sialoglycoprotein D	34:52	sialoglycoprotein D (glycophorin C)	34:68	N-terminal amino acid sequence of sialoglycoprotein D (glycophorin C) from human erythrocyte membranes.
7106126	0	57	theme	glycophorin	55:65	arg1	C					67:67	glycophorin C	55:67	glycophorin C	55:67	N-terminal amino acid sequence of sialoglycoprotein D (glycophorin C) from human erythrocyte membranes.
7106126	3	58	theme	asparagine-linked	564:580	arg1	chain					595:599	one asparagine-linked carbohydrate chain	560:599	one asparagine-linked carbohydrate chain	560:599	The fragment, comprising 47 residues, was found to contain an average of about 12 O-glycosidically linked oligosaccharides and one asparagine-linked carbohydrate chain.
1468573	0	0	theme	N-linked	108:115	arg1	chains					130:135	N-linked carbohydrate chains	108:135	N-linked carbohydrate chains	108:135	Human urokinase contains GalNAc beta (1-4)[Fuc alpha (1-3)]GlcNAc beta (1-2) as a novel terminal element in N-linked carbohydrate chains.
1468573	1	1	theme	beta	470:473	arg1	element					481:487	the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta (1-2) element	418:487	the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta (1-2) element in the upper or the lower branch	418:520	Structural analysis of enzymically released N-linked carbohydrate chains of human urokinase (urinary-type plasminogen activator) by 1H NMR spectroscopy and FAB-MS demonstrated that the N-linked oligosaccharides on the only N-glycosylation site contain diantennary structures with the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta (1-2) element in the upper or the lower branch.
1468573	0	2	from	element	97:103	arg1	chains					130:135	N-linked carbohydrate chains	108:135	N-linked carbohydrate chains	108:135	Human urokinase contains GalNAc beta (1-4)[Fuc alpha (1-3)]GlcNAc beta (1-2) as a novel terminal element in N-linked carbohydrate chains.
1468573	1	3	theme	human	214:218	arg1	activator					256:264	urinary-type plasminogen activator	231:264	urinary-type plasminogen activator	231:264	Structural analysis of enzymically released N-linked carbohydrate chains of human urokinase (urinary-type plasminogen activator) by 1H NMR spectroscopy and FAB-MS demonstrated that the N-linked oligosaccharides on the only N-glycosylation site contain diantennary structures with the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta (1-2) element in the upper or the lower branch.
1468573	1	3	theme	human	214:218	arg1	urokinase					220:228	human urokinase	214:228	human urokinase (urinary-type plasminogen activator)	214:265	Structural analysis of enzymically released N-linked carbohydrate chains of human urokinase (urinary-type plasminogen activator) by 1H NMR spectroscopy and FAB-MS demonstrated that the N-linked oligosaccharides on the only N-glycosylation site contain diantennary structures with the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta (1-2) element in the upper or the lower branch.
1468573	0	4	theme	carbohydrate	117:128	arg1	chains					130:135	N-linked carbohydrate chains	108:135	N-linked carbohydrate chains	108:135	Human urokinase contains GalNAc beta (1-4)[Fuc alpha (1-3)]GlcNAc beta (1-2) as a novel terminal element in N-linked carbohydrate chains.
1468573	1	5	theme	novel	422:426	arg1	alpha					451:455	1-4) [Fuc alpha (1-3)	441:461	1-4) [Fuc alpha (1-3)	441:461	Structural analysis of enzymically released N-linked carbohydrate chains of human urokinase (urinary-type plasminogen activator) by 1H NMR spectroscopy and FAB-MS demonstrated that the N-linked oligosaccharides on the only N-glycosylation site contain diantennary structures with the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta (1-2) element in the upper or the lower branch.
1468573	1	5	theme	novel	422:426	arg1	beta					435:438	the novel GalNAc beta	418:438	the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta (1-2) element in the upper or the lower branch	418:520	Structural analysis of enzymically released N-linked carbohydrate chains of human urokinase (urinary-type plasminogen activator) by 1H NMR spectroscopy and FAB-MS demonstrated that the N-linked oligosaccharides on the only N-glycosylation site contain diantennary structures with the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta (1-2) element in the upper or the lower branch.
1468573	1	6	link	N-linked	323:330	arg1	oligosaccharides					332:347	the N-linked oligosaccharides	319:347	the N-linked oligosaccharides on the only N-glycosylation site	319:380	Structural analysis of enzymically released N-linked carbohydrate chains of human urokinase (urinary-type plasminogen activator) by 1H NMR spectroscopy and FAB-MS demonstrated that the N-linked oligosaccharides on the only N-glycosylation site contain diantennary structures with the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta (1-2) element in the upper or the lower branch.
1468573	1	7	theme	urokinase	220:228	arg1	chains					204:209	enzymically released N-linked carbohydrate chains	161:209	enzymically released N-linked carbohydrate chains of human urokinase (urinary-type plasminogen activator)	161:265	Structural analysis of enzymically released N-linked carbohydrate chains of human urokinase (urinary-type plasminogen activator) by 1H NMR spectroscopy and FAB-MS demonstrated that the N-linked oligosaccharides on the only N-glycosylation site contain diantennary structures with the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta (1-2) element in the upper or the lower branch.
1468573	1	8	theme	GalNAc	428:433	arg1	alpha					451:455	1-4) [Fuc alpha (1-3)	441:461	1-4) [Fuc alpha (1-3)	441:461	Structural analysis of enzymically released N-linked carbohydrate chains of human urokinase (urinary-type plasminogen activator) by 1H NMR spectroscopy and FAB-MS demonstrated that the N-linked oligosaccharides on the only N-glycosylation site contain diantennary structures with the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta (1-2) element in the upper or the lower branch.
1468573	1	8	theme	GalNAc	428:433	arg1	beta					435:438	the novel GalNAc beta	418:438	the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta (1-2) element in the upper or the lower branch	418:520	Structural analysis of enzymically released N-linked carbohydrate chains of human urokinase (urinary-type plasminogen activator) by 1H NMR spectroscopy and FAB-MS demonstrated that the N-linked oligosaccharides on the only N-glycosylation site contain diantennary structures with the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta (1-2) element in the upper or the lower branch.
1468573	0	9	link	N-linked	108:115	arg1	chains					130:135	N-linked carbohydrate chains	108:135	N-linked carbohydrate chains	108:135	Human urokinase contains GalNAc beta (1-4)[Fuc alpha (1-3)]GlcNAc beta (1-2) as a novel terminal element in N-linked carbohydrate chains.
1468573	0	10	theme	GlcNAc	59:64	arg1	element					97:103	a novel terminal element	80:103	a novel terminal element in N-linked carbohydrate chains	80:135	Human urokinase contains GalNAc beta (1-4)[Fuc alpha (1-3)]GlcNAc beta (1-2) as a novel terminal element in N-linked carbohydrate chains.
1468573	0	10	theme	GlcNAc	59:64	arg1	beta					66:69	GalNAc beta (1-4)[Fuc alpha (1-3)]GlcNAc beta (1-2)	25:75	GalNAc beta (1-4)[Fuc alpha (1-3)]GlcNAc beta (1-2)	25:75	Human urokinase contains GalNAc beta (1-4)[Fuc alpha (1-3)]GlcNAc beta (1-2) as a novel terminal element in N-linked carbohydrate chains.
1468573	1	11	theme	N-linked	323:330	arg1	oligosaccharides					332:347	the N-linked oligosaccharides	319:347	the N-linked oligosaccharides on the only N-glycosylation site	319:380	Structural analysis of enzymically released N-linked carbohydrate chains of human urokinase (urinary-type plasminogen activator) by 1H NMR spectroscopy and FAB-MS demonstrated that the N-linked oligosaccharides on the only N-glycosylation site contain diantennary structures with the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta (1-2) element in the upper or the lower branch.
1468573	1	12	theme	chains	204:209	arg1	analysis					149:156	Structural analysis	138:156	Structural analysis of enzymically released N-linked carbohydrate chains of human urokinase (urinary-type plasminogen activator) by 1H NMR spectroscopy and FAB-MS	138:299	Structural analysis of enzymically released N-linked carbohydrate chains of human urokinase (urinary-type plasminogen activator) by 1H NMR spectroscopy and FAB-MS demonstrated that the N-linked oligosaccharides on the only N-glycosylation site contain diantennary structures with the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta (1-2) element in the upper or the lower branch.
1468573	0	13	contain	contains	16:23	arg2	beta					66:69	GalNAc beta (1-4)[Fuc alpha (1-3)]GlcNAc beta (1-2)	25:75	GalNAc beta (1-4)[Fuc alpha (1-3)]GlcNAc beta (1-2)	25:75	Human urokinase contains GalNAc beta (1-4)[Fuc alpha (1-3)]GlcNAc beta (1-2) as a novel terminal element in N-linked carbohydrate chains.
1468573	0	13	contain	contains	16:23	arg2	element					97:103	a novel terminal element	80:103	a novel terminal element in N-linked carbohydrate chains	80:135	Human urokinase contains GalNAc beta (1-4)[Fuc alpha (1-3)]GlcNAc beta (1-2) as a novel terminal element in N-linked carbohydrate chains.
1468573	0	13	contain	contains	16:23	arg1	urokinase					6:14	Human urokinase	0:14	Human urokinase	0:14	Human urokinase contains GalNAc beta (1-4)[Fuc alpha (1-3)]GlcNAc beta (1-2) as a novel terminal element in N-linked carbohydrate chains.
1468573	1	14	from	oligosaccharides	332:347	arg1	site					377:380	the only N-glycosylation site	352:380	the only N-glycosylation site	352:380	Structural analysis of enzymically released N-linked carbohydrate chains of human urokinase (urinary-type plasminogen activator) by 1H NMR spectroscopy and FAB-MS demonstrated that the N-linked oligosaccharides on the only N-glycosylation site contain diantennary structures with the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta (1-2) element in the upper or the lower branch.
1468573	0	15	theme	Human	0:4	arg1	urokinase					6:14	Human urokinase	0:14	Human urokinase	0:14	Human urokinase contains GalNAc beta (1-4)[Fuc alpha (1-3)]GlcNAc beta (1-2) as a novel terminal element in N-linked carbohydrate chains.
1468573	0	16	theme	GalNAc	25:30	arg1	alpha					47:51	1-4)[Fuc alpha (1-3)	38:57	1-4)[Fuc alpha (1-3)	38:57	Human urokinase contains GalNAc beta (1-4)[Fuc alpha (1-3)]GlcNAc beta (1-2) as a novel terminal element in N-linked carbohydrate chains.
1468573	0	16	theme	GalNAc	25:30	arg1	beta					32:35	GalNAc beta	25:35	GalNAc beta (1-4)[Fuc alpha (1-3)]GlcNAc beta (1-2)	25:75	Human urokinase contains GalNAc beta (1-4)[Fuc alpha (1-3)]GlcNAc beta (1-2) as a novel terminal element in N-linked carbohydrate chains.
1468573	1	17	theme	urinary-type	231:242	arg1	activator					256:264	urinary-type plasminogen activator	231:264	urinary-type plasminogen activator	231:264	Structural analysis of enzymically released N-linked carbohydrate chains of human urokinase (urinary-type plasminogen activator) by 1H NMR spectroscopy and FAB-MS demonstrated that the N-linked oligosaccharides on the only N-glycosylation site contain diantennary structures with the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta (1-2) element in the upper or the lower branch.
1468573	1	17	theme	urinary-type	231:242	arg1	urokinase					220:228	human urokinase	214:228	human urokinase (urinary-type plasminogen activator)	214:265	Structural analysis of enzymically released N-linked carbohydrate chains of human urokinase (urinary-type plasminogen activator) by 1H NMR spectroscopy and FAB-MS demonstrated that the N-linked oligosaccharides on the only N-glycosylation site contain diantennary structures with the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta (1-2) element in the upper or the lower branch.
1468573	1	18	theme	plasminogen	244:254	arg1	activator					256:264	urinary-type plasminogen activator	231:264	urinary-type plasminogen activator	231:264	Structural analysis of enzymically released N-linked carbohydrate chains of human urokinase (urinary-type plasminogen activator) by 1H NMR spectroscopy and FAB-MS demonstrated that the N-linked oligosaccharides on the only N-glycosylation site contain diantennary structures with the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta (1-2) element in the upper or the lower branch.
1468573	1	18	theme	plasminogen	244:254	arg1	urokinase					220:228	human urokinase	214:228	human urokinase (urinary-type plasminogen activator)	214:265	Structural analysis of enzymically released N-linked carbohydrate chains of human urokinase (urinary-type plasminogen activator) by 1H NMR spectroscopy and FAB-MS demonstrated that the N-linked oligosaccharides on the only N-glycosylation site contain diantennary structures with the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta (1-2) element in the upper or the lower branch.
1468573	1	19	theme	Structural	138:147	arg1	analysis					149:156	Structural analysis	138:156	Structural analysis of enzymically released N-linked carbohydrate chains of human urokinase (urinary-type plasminogen activator) by 1H NMR spectroscopy and FAB-MS	138:299	Structural analysis of enzymically released N-linked carbohydrate chains of human urokinase (urinary-type plasminogen activator) by 1H NMR spectroscopy and FAB-MS demonstrated that the N-linked oligosaccharides on the only N-glycosylation site contain diantennary structures with the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta (1-2) element in the upper or the lower branch.
1468573	1	20	with	structures	402:411	arg1	element					481:487	the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta (1-2) element	418:487	the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta (1-2) element in the upper or the lower branch	418:520	Structural analysis of enzymically released N-linked carbohydrate chains of human urokinase (urinary-type plasminogen activator) by 1H NMR spectroscopy and FAB-MS demonstrated that the N-linked oligosaccharides on the only N-glycosylation site contain diantennary structures with the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta (1-2) element in the upper or the lower branch.
1468573	1	21	contain	contain	382:388	arg2	structures					402:411	diantennary structures	390:411	diantennary structures with the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta (1-2) element in the upper or the lower branch	390:520	Structural analysis of enzymically released N-linked carbohydrate chains of human urokinase (urinary-type plasminogen activator) by 1H NMR spectroscopy and FAB-MS demonstrated that the N-linked oligosaccharides on the only N-glycosylation site contain diantennary structures with the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta (1-2) element in the upper or the lower branch.
1468573	1	21	contain	contain	382:388	arg1	oligosaccharides					332:347	the N-linked oligosaccharides	319:347	the N-linked oligosaccharides on the only N-glycosylation site	319:380	Structural analysis of enzymically released N-linked carbohydrate chains of human urokinase (urinary-type plasminogen activator) by 1H NMR spectroscopy and FAB-MS demonstrated that the N-linked oligosaccharides on the only N-glycosylation site contain diantennary structures with the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta (1-2) element in the upper or the lower branch.
1468573	0	22	theme	beta	32:35	arg1	element					97:103	a novel terminal element	80:103	a novel terminal element in N-linked carbohydrate chains	80:135	Human urokinase contains GalNAc beta (1-4)[Fuc alpha (1-3)]GlcNAc beta (1-2) as a novel terminal element in N-linked carbohydrate chains.
1468573	0	22	theme	beta	32:35	arg1	beta					66:69	GalNAc beta (1-4)[Fuc alpha (1-3)]GlcNAc beta (1-2)	25:75	GalNAc beta (1-4)[Fuc alpha (1-3)]GlcNAc beta (1-2)	25:75	Human urokinase contains GalNAc beta (1-4)[Fuc alpha (1-3)]GlcNAc beta (1-2) as a novel terminal element in N-linked carbohydrate chains.
1468573	1	23	theme	only	356:359	arg1	site					377:380	the only N-glycosylation site	352:380	the only N-glycosylation site	352:380	Structural analysis of enzymically released N-linked carbohydrate chains of human urokinase (urinary-type plasminogen activator) by 1H NMR spectroscopy and FAB-MS demonstrated that the N-linked oligosaccharides on the only N-glycosylation site contain diantennary structures with the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta (1-2) element in the upper or the lower branch.
1468573	1	24	theme	[Fuc	446:449	arg1	alpha					451:455	1-4) [Fuc alpha (1-3)	441:461	1-4) [Fuc alpha (1-3)	441:461	Structural analysis of enzymically released N-linked carbohydrate chains of human urokinase (urinary-type plasminogen activator) by 1H NMR spectroscopy and FAB-MS demonstrated that the N-linked oligosaccharides on the only N-glycosylation site contain diantennary structures with the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta (1-2) element in the upper or the lower branch.
1468573	1	24	theme	[Fuc	446:449	arg1	beta					435:438	the novel GalNAc beta	418:438	the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta (1-2) element in the upper or the lower branch	418:520	Structural analysis of enzymically released N-linked carbohydrate chains of human urokinase (urinary-type plasminogen activator) by 1H NMR spectroscopy and FAB-MS demonstrated that the N-linked oligosaccharides on the only N-glycosylation site contain diantennary structures with the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta (1-2) element in the upper or the lower branch.
1468573	0	25	theme	novel	82:86	arg1	beta					66:69	GalNAc beta (1-4)[Fuc alpha (1-3)]GlcNAc beta (1-2)	25:75	GalNAc beta (1-4)[Fuc alpha (1-3)]GlcNAc beta (1-2)	25:75	Human urokinase contains GalNAc beta (1-4)[Fuc alpha (1-3)]GlcNAc beta (1-2) as a novel terminal element in N-linked carbohydrate chains.
1468573	0	25	theme	novel	82:86	arg1	element					97:103	a novel terminal element	80:103	a novel terminal element in N-linked carbohydrate chains	80:135	Human urokinase contains GalNAc beta (1-4)[Fuc alpha (1-3)]GlcNAc beta (1-2) as a novel terminal element in N-linked carbohydrate chains.
1468573	1	26	theme	N-glycosylation	361:375	arg1	site					377:380	the only N-glycosylation site	352:380	the only N-glycosylation site	352:380	Structural analysis of enzymically released N-linked carbohydrate chains of human urokinase (urinary-type plasminogen activator) by 1H NMR spectroscopy and FAB-MS demonstrated that the N-linked oligosaccharides on the only N-glycosylation site contain diantennary structures with the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta (1-2) element in the upper or the lower branch.
1468573	1	27	theme	beta	435:438	arg1	1-2					476:478	1-2	476:478	1-2	476:478	Structural analysis of enzymically released N-linked carbohydrate chains of human urokinase (urinary-type plasminogen activator) by 1H NMR spectroscopy and FAB-MS demonstrated that the N-linked oligosaccharides on the only N-glycosylation site contain diantennary structures with the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta (1-2) element in the upper or the lower branch.
1468573	1	27	theme	beta	435:438	arg1	beta					470:473	the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta	418:473	the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta (1-2) element in the upper or the lower branch	418:520	Structural analysis of enzymically released N-linked carbohydrate chains of human urokinase (urinary-type plasminogen activator) by 1H NMR spectroscopy and FAB-MS demonstrated that the N-linked oligosaccharides on the only N-glycosylation site contain diantennary structures with the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta (1-2) element in the upper or the lower branch.
1468573	1	28	theme	1H	270:271	arg1	spectroscopy					277:288	1H NMR spectroscopy	270:288	1H NMR spectroscopy	270:288	Structural analysis of enzymically released N-linked carbohydrate chains of human urokinase (urinary-type plasminogen activator) by 1H NMR spectroscopy and FAB-MS demonstrated that the N-linked oligosaccharides on the only N-glycosylation site contain diantennary structures with the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta (1-2) element in the upper or the lower branch.
1468573	1	29	theme	NMR	273:275	arg1	spectroscopy					277:288	1H NMR spectroscopy	270:288	1H NMR spectroscopy	270:288	Structural analysis of enzymically released N-linked carbohydrate chains of human urokinase (urinary-type plasminogen activator) by 1H NMR spectroscopy and FAB-MS demonstrated that the N-linked oligosaccharides on the only N-glycosylation site contain diantennary structures with the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta (1-2) element in the upper or the lower branch.
1468573	1	30	link	N-linked	182:189	arg1	chains					204:209	enzymically released N-linked carbohydrate chains	161:209	enzymically released N-linked carbohydrate chains of human urokinase (urinary-type plasminogen activator)	161:265	Structural analysis of enzymically released N-linked carbohydrate chains of human urokinase (urinary-type plasminogen activator) by 1H NMR spectroscopy and FAB-MS demonstrated that the N-linked oligosaccharides on the only N-glycosylation site contain diantennary structures with the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta (1-2) element in the upper or the lower branch.
1468573	1	31	theme	lower	509:513	arg1	branch					515:520	the lower branch	505:520	the lower branch	505:520	Structural analysis of enzymically released N-linked carbohydrate chains of human urokinase (urinary-type plasminogen activator) by 1H NMR spectroscopy and FAB-MS demonstrated that the N-linked oligosaccharides on the only N-glycosylation site contain diantennary structures with the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta (1-2) element in the upper or the lower branch.
1468573	0	32	theme	terminal	88:95	arg1	beta					66:69	GalNAc beta (1-4)[Fuc alpha (1-3)]GlcNAc beta (1-2)	25:75	GalNAc beta (1-4)[Fuc alpha (1-3)]GlcNAc beta (1-2)	25:75	Human urokinase contains GalNAc beta (1-4)[Fuc alpha (1-3)]GlcNAc beta (1-2) as a novel terminal element in N-linked carbohydrate chains.
1468573	0	32	theme	terminal	88:95	arg1	element					97:103	a novel terminal element	80:103	a novel terminal element in N-linked carbohydrate chains	80:135	Human urokinase contains GalNAc beta (1-4)[Fuc alpha (1-3)]GlcNAc beta (1-2) as a novel terminal element in N-linked carbohydrate chains.
1468573	1	33	theme	diantennary	390:400	arg1	structures					402:411	diantennary structures	390:411	diantennary structures with the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta (1-2) element in the upper or the lower branch	390:520	Structural analysis of enzymically released N-linked carbohydrate chains of human urokinase (urinary-type plasminogen activator) by 1H NMR spectroscopy and FAB-MS demonstrated that the N-linked oligosaccharides on the only N-glycosylation site contain diantennary structures with the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta (1-2) element in the upper or the lower branch.
1468573	1	34	from	element	481:487	arg1	branch					515:520	the lower branch	505:520	the lower branch	505:520	Structural analysis of enzymically released N-linked carbohydrate chains of human urokinase (urinary-type plasminogen activator) by 1H NMR spectroscopy and FAB-MS demonstrated that the N-linked oligosaccharides on the only N-glycosylation site contain diantennary structures with the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta (1-2) element in the upper or the lower branch.
1468573	1	34	from	element	481:487	arg1	upper					496:500	upper	496:500	upper	496:500	Structural analysis of enzymically released N-linked carbohydrate chains of human urokinase (urinary-type plasminogen activator) by 1H NMR spectroscopy and FAB-MS demonstrated that the N-linked oligosaccharides on the only N-glycosylation site contain diantennary structures with the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta (1-2) element in the upper or the lower branch.
1468573	1	35	gly	N-glycosylation	361:375	arg2	site					377:380	the only N-glycosylation site	352:380	the only N-glycosylation site	352:380	Structural analysis of enzymically released N-linked carbohydrate chains of human urokinase (urinary-type plasminogen activator) by 1H NMR spectroscopy and FAB-MS demonstrated that the N-linked oligosaccharides on the only N-glycosylation site contain diantennary structures with the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta (1-2) element in the upper or the lower branch.
1468573	1	36	theme	released	173:180	arg1	chains					204:209	enzymically released N-linked carbohydrate chains	161:209	enzymically released N-linked carbohydrate chains of human urokinase (urinary-type plasminogen activator)	161:265	Structural analysis of enzymically released N-linked carbohydrate chains of human urokinase (urinary-type plasminogen activator) by 1H NMR spectroscopy and FAB-MS demonstrated that the N-linked oligosaccharides on the only N-glycosylation site contain diantennary structures with the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta (1-2) element in the upper or the lower branch.
1468573	1	37	theme	N-linked	182:189	arg1	chains					204:209	enzymically released N-linked carbohydrate chains	161:209	enzymically released N-linked carbohydrate chains of human urokinase (urinary-type plasminogen activator)	161:265	Structural analysis of enzymically released N-linked carbohydrate chains of human urokinase (urinary-type plasminogen activator) by 1H NMR spectroscopy and FAB-MS demonstrated that the N-linked oligosaccharides on the only N-glycosylation site contain diantennary structures with the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta (1-2) element in the upper or the lower branch.
1468573	0	38	theme	[Fuc	42:45	arg1	alpha					47:51	1-4)[Fuc alpha (1-3)	38:57	1-4)[Fuc alpha (1-3)	38:57	Human urokinase contains GalNAc beta (1-4)[Fuc alpha (1-3)]GlcNAc beta (1-2) as a novel terminal element in N-linked carbohydrate chains.
1468573	0	38	theme	[Fuc	42:45	arg1	beta					32:35	GalNAc beta	25:35	GalNAc beta (1-4)[Fuc alpha (1-3)]GlcNAc beta (1-2)	25:75	Human urokinase contains GalNAc beta (1-4)[Fuc alpha (1-3)]GlcNAc beta (1-2) as a novel terminal element in N-linked carbohydrate chains.
1468573	1	39	theme	GlcNAc	463:468	arg1	1-2					476:478	1-2	476:478	1-2	476:478	Structural analysis of enzymically released N-linked carbohydrate chains of human urokinase (urinary-type plasminogen activator) by 1H NMR spectroscopy and FAB-MS demonstrated that the N-linked oligosaccharides on the only N-glycosylation site contain diantennary structures with the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta (1-2) element in the upper or the lower branch.
1468573	1	39	theme	GlcNAc	463:468	arg1	beta					470:473	the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta	418:473	the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta (1-2) element in the upper or the lower branch	418:520	Structural analysis of enzymically released N-linked carbohydrate chains of human urokinase (urinary-type plasminogen activator) by 1H NMR spectroscopy and FAB-MS demonstrated that the N-linked oligosaccharides on the only N-glycosylation site contain diantennary structures with the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta (1-2) element in the upper or the lower branch.
1468573	1	40	theme	carbohydrate	191:202	arg1	chains					204:209	enzymically released N-linked carbohydrate chains	161:209	enzymically released N-linked carbohydrate chains of human urokinase (urinary-type plasminogen activator)	161:265	Structural analysis of enzymically released N-linked carbohydrate chains of human urokinase (urinary-type plasminogen activator) by 1H NMR spectroscopy and FAB-MS demonstrated that the N-linked oligosaccharides on the only N-glycosylation site contain diantennary structures with the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta (1-2) element in the upper or the lower branch.
2209609	7	0	theme	Ricinis	1136:1142	arg1	agglutinin					1153:1162	Ricinis communis agglutinin 120	1136:1166	Ricinis communis agglutinin 120	1136:1166	By enzymic microsequencing of the sialidase-treated oligosaccharides (fractionated on affinity columns of Ricinis communis agglutinin 120 and concanavalin A) in conjunction with methylation data from the earlier study, 14 sequences were identified.
2209609	7	1	from	microsequencing	1041:1055	arg1	conjunction					1191:1201	conjunction	1191:1201	conjunction with methylation data from the earlier study	1191:1246	By enzymic microsequencing of the sialidase-treated oligosaccharides (fractionated on affinity columns of Ricinis communis agglutinin 120 and concanavalin A) in conjunction with methylation data from the earlier study, 14 sequences were identified.
2209609	2	2	dep	G.	589:590	arg1	Biol					671:674	Biol	671:674	Biol	671:674	The glycoprotein has two N-glycosylation sites, Asn271 and Asn300, at both of which evidence for the presence of complex type biantennary sialo-oligosaccharides has been obtained previously by mass spectrometric analyses [Carr, S.A., Hemling, M.E., Folena-Wasserman, G., Sweet, R.W., Anumula, K., Barr, J.R., Huddleston, M.J. & Taylor, P. (1989) J. Biol.
2209609	9	3	theme	chromatographic	1626:1640	arg1	profiles					1642:1649	their chromatographic profiles	1620:1649	their chromatographic profiles	1620:1649	The spectrum of oligosaccharide structures released from each glycosylation site was assessed as being similar to that of total oligosaccharides on the basis of their chromatographic profiles on the lectin columns and on Bio-Gel P-4.
2209609	5	4	theme	acidic	810:815	arg1	oligosaccharides					825:840	neutral (12.8%) and acidic (87.2%) oligosaccharides	790:840	neutral (12.8%) and acidic (87.2%) oligosaccharides	790:840	Among oligosaccharides released from sCD4 by hydrazinolysis and labelled with NaB3H4, neutral (12.8%) and acidic (87.2%) oligosaccharides were detected by paper electrophoresis.
2209609	8	5	theme	present	1419:1425	arg1	residues					1410:1417	residues	1410:1417	residues present on only a proportion of chains	1410:1456	These accounted for over 80% of the sialidase-treated oligosaccharides of sCD4 as follows: [formula: see text] where +/- indicates residues present on only a proportion of chains.
2209609	0	6	link	N-linked	16:23	arg1	structures					41:50	N-linked oligosaccharide structures	16:50	N-linked oligosaccharide structures	16:50	The spectrum of N-linked oligosaccharide structures detected by enzymic microsequencing on a recombinant soluble CD4 glycoprotein from Chinese hamster ovary cells.
2209609	7	7	theme	concanavalin	1172:1183	arg1	A					1185:1185	concanavalin A	1172:1185	concanavalin A	1172:1185	By enzymic microsequencing of the sialidase-treated oligosaccharides (fractionated on affinity columns of Ricinis communis agglutinin 120 and concanavalin A) in conjunction with methylation data from the earlier study, 14 sequences were identified.
2209609	2	8	theme	spectrometric	520:532	arg1	analyses					534:541	mass spectrometric analyses	515:541	mass spectrometric analyses [Carr	515:547	The glycoprotein has two N-glycosylation sites, Asn271 and Asn300, at both of which evidence for the presence of complex type biantennary sialo-oligosaccharides has been obtained previously by mass spectrometric analyses [Carr, S.A., Hemling, M.E., Folena-Wasserman, G., Sweet, R.W., Anumula, K., Barr, J.R., Huddleston, M.J. & Taylor, P. (1989) J. Biol.
2209609	0	9	theme	soluble	105:111	arg1	glycoprotein					117:128	a recombinant soluble CD4 glycoprotein	91:128	a recombinant soluble CD4 glycoprotein from Chinese hamster ovary cells	91:161	The spectrum of N-linked oligosaccharide structures detected by enzymic microsequencing on a recombinant soluble CD4 glycoprotein from Chinese hamster ovary cells.
2209609	7	10	from	conjunction	1191:1201	arg1	microsequencing					1041:1055	enzymic microsequencing	1033:1055	enzymic microsequencing of the sialidase-treated oligosaccharides (fractionated on affinity columns of Ricinis communis agglutinin 120 and concanavalin A) in conjunction with methylation data from the earlier study	1033:1246	By enzymic microsequencing of the sialidase-treated oligosaccharides (fractionated on affinity columns of Ricinis communis agglutinin 120 and concanavalin A) in conjunction with methylation data from the earlier study, 14 sequences were identified.
2209609	5	11	dep	oligosaccharides	710:725	arg1	released					727:734	released	727:734	released from sCD4 by hydrazinolysis	727:762	Among oligosaccharides released from sCD4 by hydrazinolysis and labelled with NaB3H4, neutral (12.8%) and acidic (87.2%) oligosaccharides were detected by paper electrophoresis.
2209609	5	11	dep	oligosaccharides	710:725	arg1	labelled					768:775	labelled	768:775	labelled with NaB3H4	768:787	Among oligosaccharides released from sCD4 by hydrazinolysis and labelled with NaB3H4, neutral (12.8%) and acidic (87.2%) oligosaccharides were detected by paper electrophoresis.
2209609	9	12	theme	structures	1491:1500	arg1	spectrum					1463:1470	The spectrum	1459:1470	The spectrum of oligosaccharide structures released from each glycosylation site	1459:1538	The spectrum of oligosaccharide structures released from each glycosylation site was assessed as being similar to that of total oligosaccharides on the basis of their chromatographic profiles on the lectin columns and on Bio-Gel P-4.
2209609	9	13	from	basis	1611:1615	arg1	P-4					1688:1690	Bio-Gel P-4	1680:1690	Bio-Gel P-4	1680:1690	The spectrum of oligosaccharide structures released from each glycosylation site was assessed as being similar to that of total oligosaccharides on the basis of their chromatographic profiles on the lectin columns and on Bio-Gel P-4.
2209609	9	13	from	basis	1611:1615	arg1	columns					1665:1671	the lectin columns	1654:1671	the lectin columns	1654:1671	The spectrum of oligosaccharide structures released from each glycosylation site was assessed as being similar to that of total oligosaccharides on the basis of their chromatographic profiles on the lectin columns and on Bio-Gel P-4.
2209609	0	14	theme	recombinant	93:103	arg1	glycoprotein					117:128	a recombinant soluble CD4 glycoprotein	91:128	a recombinant soluble CD4 glycoprotein from Chinese hamster ovary cells	91:161	The spectrum of N-linked oligosaccharide structures detected by enzymic microsequencing on a recombinant soluble CD4 glycoprotein from Chinese hamster ovary cells.
2209609	9	15	from	oligosaccharides	1587:1602	arg1	basis					1611:1615	the basis	1607:1615	the basis of their chromatographic profiles on the lectin columns and on Bio-Gel P-4	1607:1690	The spectrum of oligosaccharide structures released from each glycosylation site was assessed as being similar to that of total oligosaccharides on the basis of their chromatographic profiles on the lectin columns and on Bio-Gel P-4.
2209609	1	16	gly	glycoprotein	251:262	arg1	sCD4					265:268	sCD4	265:268	sCD4	265:268	Structures of the N-linked oligosaccharides of a recombinant soluble form of human CD4 glycoprotein (sCD4) have been investigated by enzymic microsequencing.
2209609	1	16	gly	glycoprotein	251:262	arg1	glycoprotein					251:262	human CD4 glycoprotein	241:262	human CD4 glycoprotein (sCD4)	241:269	Structures of the N-linked oligosaccharides of a recombinant soluble form of human CD4 glycoprotein (sCD4) have been investigated by enzymic microsequencing.
2209609	0	17	from	cells	157:161	arg1	glycoprotein					117:128	a recombinant soluble CD4 glycoprotein	91:128	a recombinant soluble CD4 glycoprotein from Chinese hamster ovary cells	91:161	The spectrum of N-linked oligosaccharide structures detected by enzymic microsequencing on a recombinant soluble CD4 glycoprotein from Chinese hamster ovary cells.
2209609	2	18	theme	analyses	534:541	arg1	G.					589:590	G.	589:590	G.	589:590	The glycoprotein has two N-glycosylation sites, Asn271 and Asn300, at both of which evidence for the presence of complex type biantennary sialo-oligosaccharides has been obtained previously by mass spectrometric analyses [Carr, S.A., Hemling, M.E., Folena-Wasserman, G., Sweet, R.W., Anumula, K., Barr, J.R., Huddleston, M.J. & Taylor, P. (1989) J. Biol.
2209609	2	18	theme	analyses	534:541	arg1	[Carr					543:547	mass spectrometric analyses [Carr	515:547	mass spectrometric analyses [Carr	515:547	The glycoprotein has two N-glycosylation sites, Asn271 and Asn300, at both of which evidence for the presence of complex type biantennary sialo-oligosaccharides has been obtained previously by mass spectrometric analyses [Carr, S.A., Hemling, M.E., Folena-Wasserman, G., Sweet, R.W., Anumula, K., Barr, J.R., Huddleston, M.J. & Taylor, P. (1989) J. Biol.
2209609	7	19	from	oligosaccharides	1082:1097	arg1	conjunction					1191:1201	conjunction	1191:1201	conjunction with methylation data from the earlier study	1191:1246	By enzymic microsequencing of the sialidase-treated oligosaccharides (fractionated on affinity columns of Ricinis communis agglutinin 120 and concanavalin A) in conjunction with methylation data from the earlier study, 14 sequences were identified.
2209609	9	20	theme	Bio-Gel	1680:1686	arg1	P-4					1688:1690	Bio-Gel P-4	1680:1690	Bio-Gel P-4	1680:1690	The spectrum of oligosaccharide structures released from each glycosylation site was assessed as being similar to that of total oligosaccharides on the basis of their chromatographic profiles on the lectin columns and on Bio-Gel P-4.
2209609	7	21	theme	earlier	1234:1240	arg1	study					1242:1246	the earlier study	1230:1246	the earlier study	1230:1246	By enzymic microsequencing of the sialidase-treated oligosaccharides (fractionated on affinity columns of Ricinis communis agglutinin 120 and concanavalin A) in conjunction with methylation data from the earlier study, 14 sequences were identified.
2209609	5	22	theme	paper	859:863	arg1	electrophoresis					865:879	paper electrophoresis	859:879	paper electrophoresis	859:879	Among oligosaccharides released from sCD4 by hydrazinolysis and labelled with NaB3H4, neutral (12.8%) and acidic (87.2%) oligosaccharides were detected by paper electrophoresis.
2209609	0	23	theme	CD4	113:115	arg1	glycoprotein					117:128	a recombinant soluble CD4 glycoprotein	91:128	a recombinant soluble CD4 glycoprotein from Chinese hamster ovary cells	91:161	The spectrum of N-linked oligosaccharide structures detected by enzymic microsequencing on a recombinant soluble CD4 glycoprotein from Chinese hamster ovary cells.
2209609	7	24	with	conjunction	1191:1201	arg1	data					1220:1223	methylation data	1208:1223	methylation data from the earlier study	1208:1246	By enzymic microsequencing of the sialidase-treated oligosaccharides (fractionated on affinity columns of Ricinis communis agglutinin 120 and concanavalin A) in conjunction with methylation data from the earlier study, 14 sequences were identified.
2209609	7	25	theme	enzymic	1033:1039	arg1	microsequencing					1041:1055	enzymic microsequencing	1033:1055	enzymic microsequencing of the sialidase-treated oligosaccharides (fractionated on affinity columns of Ricinis communis agglutinin 120 and concanavalin A) in conjunction with methylation data from the earlier study	1033:1246	By enzymic microsequencing of the sialidase-treated oligosaccharides (fractionated on affinity columns of Ricinis communis agglutinin 120 and concanavalin A) in conjunction with methylation data from the earlier study, 14 sequences were identified.
2209609	5	26	dep	acidic	810:815	arg1	%					822:822	87.2%	818:822	87.2%	818:822	Among oligosaccharides released from sCD4 by hydrazinolysis and labelled with NaB3H4, neutral (12.8%) and acidic (87.2%) oligosaccharides were detected by paper electrophoresis.
2209609	1	27	theme	N-linked	182:189	arg1	oligosaccharides					191:206	the N-linked oligosaccharides	178:206	the N-linked oligosaccharides of a recombinant soluble form of human CD4 glycoprotein (sCD4)	178:269	Structures of the N-linked oligosaccharides of a recombinant soluble form of human CD4 glycoprotein (sCD4) have been investigated by enzymic microsequencing.
2209609	2	28	theme	type	443:446	arg1	sialo-oligosaccharides					460:481	complex type biantennary sialo-oligosaccharides	435:481	complex type biantennary sialo-oligosaccharides	435:481	The glycoprotein has two N-glycosylation sites, Asn271 and Asn300, at both of which evidence for the presence of complex type biantennary sialo-oligosaccharides has been obtained previously by mass spectrometric analyses [Carr, S.A., Hemling, M.E., Folena-Wasserman, G., Sweet, R.W., Anumula, K., Barr, J.R., Huddleston, M.J. & Taylor, P. (1989) J. Biol.
2209609	7	29	theme	communis	1144:1151	arg1	agglutinin					1153:1162	Ricinis communis agglutinin 120	1136:1166	Ricinis communis agglutinin 120	1136:1166	By enzymic microsequencing of the sialidase-treated oligosaccharides (fractionated on affinity columns of Ricinis communis agglutinin 120 and concanavalin A) in conjunction with methylation data from the earlier study, 14 sequences were identified.
2209609	7	30	theme	agglutinin	1153:1162	arg1	columns					1125:1131	affinity columns	1116:1131	affinity columns of Ricinis communis agglutinin 120 and concanavalin A	1116:1185	By enzymic microsequencing of the sialidase-treated oligosaccharides (fractionated on affinity columns of Ricinis communis agglutinin 120 and concanavalin A) in conjunction with methylation data from the earlier study, 14 sequences were identified.
2209609	8	31	attach	present	1419:1425	arg1	proportion					1437:1446	only a proportion	1430:1446	only a proportion of chains	1430:1456	These accounted for over 80% of the sialidase-treated oligosaccharides of sCD4 as follows: [formula: see text] where +/- indicates residues present on only a proportion of chains.
2209609	8	31	attach	present	1419:1425	arg2	residues					1410:1417	residues	1410:1417	residues present on only a proportion of chains	1410:1456	These accounted for over 80% of the sialidase-treated oligosaccharides of sCD4 as follows: [formula: see text] where +/- indicates residues present on only a proportion of chains.
2209609	1	32	theme	oligosaccharides	191:206	arg1	Structures					164:173	Structures	164:173	Structures of the N-linked oligosaccharides of a recombinant soluble form of human CD4 glycoprotein (sCD4)	164:269	Structures of the N-linked oligosaccharides of a recombinant soluble form of human CD4 glycoprotein (sCD4) have been investigated by enzymic microsequencing.
2209609	2	33	theme	complex	435:441	arg1	sialo-oligosaccharides					460:481	complex type biantennary sialo-oligosaccharides	435:481	complex type biantennary sialo-oligosaccharides	435:481	The glycoprotein has two N-glycosylation sites, Asn271 and Asn300, at both of which evidence for the presence of complex type biantennary sialo-oligosaccharides has been obtained previously by mass spectrometric analyses [Carr, S.A., Hemling, M.E., Folena-Wasserman, G., Sweet, R.W., Anumula, K., Barr, J.R., Huddleston, M.J. & Taylor, P. (1989) J. Biol.
2209609	8	34	theme	chains	1451:1456	arg1	proportion					1437:1446	only a proportion	1430:1446	only a proportion of chains	1430:1456	These accounted for over 80% of the sialidase-treated oligosaccharides of sCD4 as follows: [formula: see text] where +/- indicates residues present on only a proportion of chains.
2209609	1	35	link	N-linked	182:189	arg1	oligosaccharides					191:206	the N-linked oligosaccharides	178:206	the N-linked oligosaccharides of a recombinant soluble form of human CD4 glycoprotein (sCD4)	178:269	Structures of the N-linked oligosaccharides of a recombinant soluble form of human CD4 glycoprotein (sCD4) have been investigated by enzymic microsequencing.
2209609	9	36	theme	lectin	1658:1663	arg1	columns					1665:1671	the lectin columns	1654:1671	the lectin columns	1654:1671	The spectrum of oligosaccharide structures released from each glycosylation site was assessed as being similar to that of total oligosaccharides on the basis of their chromatographic profiles on the lectin columns and on Bio-Gel P-4.
2209609	5	37	theme	neutral	790:796	arg1	oligosaccharides					825:840	neutral (12.8%) and acidic (87.2%) oligosaccharides	790:840	neutral (12.8%) and acidic (87.2%) oligosaccharides	790:840	Among oligosaccharides released from sCD4 by hydrazinolysis and labelled with NaB3H4, neutral (12.8%) and acidic (87.2%) oligosaccharides were detected by paper electrophoresis.
2209609	0	38	theme	N-linked	16:23	arg1	structures					41:50	N-linked oligosaccharide structures	16:50	N-linked oligosaccharide structures	16:50	The spectrum of N-linked oligosaccharide structures detected by enzymic microsequencing on a recombinant soluble CD4 glycoprotein from Chinese hamster ovary cells.
2209609	0	39	theme	Chinese	135:141	arg1	cells					157:161	Chinese hamster ovary cells	135:161	Chinese hamster ovary cells	135:161	The spectrum of N-linked oligosaccharide structures detected by enzymic microsequencing on a recombinant soluble CD4 glycoprotein from Chinese hamster ovary cells.
2209609	9	40	theme	glycosylation	1521:1533	arg1	site					1535:1538	each glycosylation site	1516:1538	each glycosylation site	1516:1538	The spectrum of oligosaccharide structures released from each glycosylation site was assessed as being similar to that of total oligosaccharides on the basis of their chromatographic profiles on the lectin columns and on Bio-Gel P-4.
2209609	9	41	theme	oligosaccharide	1475:1489	arg1	structures					1491:1500	oligosaccharide structures	1475:1500	oligosaccharide structures released from each glycosylation site	1475:1538	The spectrum of oligosaccharide structures released from each glycosylation site was assessed as being similar to that of total oligosaccharides on the basis of their chromatographic profiles on the lectin columns and on Bio-Gel P-4.
2209609	7	42	theme	oligosaccharides	1082:1097	arg1	microsequencing					1041:1055	enzymic microsequencing	1033:1055	enzymic microsequencing of the sialidase-treated oligosaccharides (fractionated on affinity columns of Ricinis communis agglutinin 120 and concanavalin A) in conjunction with methylation data from the earlier study	1033:1246	By enzymic microsequencing of the sialidase-treated oligosaccharides (fractionated on affinity columns of Ricinis communis agglutinin 120 and concanavalin A) in conjunction with methylation data from the earlier study, 14 sequences were identified.
2209609	9	43	theme	total	1581:1585	arg1	oligosaccharides					1587:1602	total oligosaccharides	1581:1602	total oligosaccharides on the basis of their chromatographic profiles on the lectin columns and on Bio-Gel P-4	1581:1690	The spectrum of oligosaccharide structures released from each glycosylation site was assessed as being similar to that of total oligosaccharides on the basis of their chromatographic profiles on the lectin columns and on Bio-Gel P-4.
2209609	0	44	gly	glycoprotein	117:128	arg1	glycoprotein					117:128	a recombinant soluble CD4 glycoprotein	91:128	a recombinant soluble CD4 glycoprotein from Chinese hamster ovary cells	91:161	The spectrum of N-linked oligosaccharide structures detected by enzymic microsequencing on a recombinant soluble CD4 glycoprotein from Chinese hamster ovary cells.
2209609	1	45	theme	recombinant	213:223	arg1	form					233:236	a recombinant soluble form	211:236	a recombinant soluble form of human CD4 glycoprotein (sCD4)	211:269	Structures of the N-linked oligosaccharides of a recombinant soluble form of human CD4 glycoprotein (sCD4) have been investigated by enzymic microsequencing.
2209609	0	46	theme	structures	41:50	arg1	spectrum					4:11	The spectrum	0:11	The spectrum of N-linked oligosaccharide structures	0:50	The spectrum of N-linked oligosaccharide structures detected by enzymic microsequencing on a recombinant soluble CD4 glycoprotein from Chinese hamster ovary cells.
2209609	1	47	theme	enzymic	297:303	arg1	microsequencing					305:319	enzymic microsequencing	297:319	enzymic microsequencing	297:319	Structures of the N-linked oligosaccharides of a recombinant soluble form of human CD4 glycoprotein (sCD4) have been investigated by enzymic microsequencing.
2209609	0	48	theme	ovary	151:155	arg1	cells					157:161	Chinese hamster ovary cells	135:161	Chinese hamster ovary cells	135:161	The spectrum of N-linked oligosaccharide structures detected by enzymic microsequencing on a recombinant soluble CD4 glycoprotein from Chinese hamster ovary cells.
2209609	7	49	theme	A	1185:1185	arg1	columns					1125:1131	affinity columns	1116:1131	affinity columns of Ricinis communis agglutinin 120 and concanavalin A	1116:1185	By enzymic microsequencing of the sialidase-treated oligosaccharides (fractionated on affinity columns of Ricinis communis agglutinin 120 and concanavalin A) in conjunction with methylation data from the earlier study, 14 sequences were identified.
2209609	1	50	theme	soluble	225:231	arg1	form					233:236	a recombinant soluble form	211:236	a recombinant soluble form of human CD4 glycoprotein (sCD4)	211:269	Structures of the N-linked oligosaccharides of a recombinant soluble form of human CD4 glycoprotein (sCD4) have been investigated by enzymic microsequencing.
2209609	0	51	theme	oligosaccharide	25:39	arg1	structures					41:50	N-linked oligosaccharide structures	16:50	N-linked oligosaccharide structures	16:50	The spectrum of N-linked oligosaccharide structures detected by enzymic microsequencing on a recombinant soluble CD4 glycoprotein from Chinese hamster ovary cells.
2209609	0	52	theme	hamster	143:149	arg1	cells					157:161	Chinese hamster ovary cells	135:161	Chinese hamster ovary cells	135:161	The spectrum of N-linked oligosaccharide structures detected by enzymic microsequencing on a recombinant soluble CD4 glycoprotein from Chinese hamster ovary cells.
2209609	5	53	dep	neutral	790:796	arg1	%					803:803	12.8%	799:803	12.8%	799:803	Among oligosaccharides released from sCD4 by hydrazinolysis and labelled with NaB3H4, neutral (12.8%) and acidic (87.2%) oligosaccharides were detected by paper electrophoresis.
2209609	1	54	theme	form	233:236	arg1	oligosaccharides					191:206	the N-linked oligosaccharides	178:206	the N-linked oligosaccharides of a recombinant soluble form of human CD4 glycoprotein (sCD4)	178:269	Structures of the N-linked oligosaccharides of a recombinant soluble form of human CD4 glycoprotein (sCD4) have been investigated by enzymic microsequencing.
2209609	2	55	theme	sialo-oligosaccharides	460:481	arg1	presence					423:430	the presence	419:430	the presence of complex type biantennary sialo-oligosaccharides	419:481	The glycoprotein has two N-glycosylation sites, Asn271 and Asn300, at both of which evidence for the presence of complex type biantennary sialo-oligosaccharides has been obtained previously by mass spectrometric analyses [Carr, S.A., Hemling, M.E., Folena-Wasserman, G., Sweet, R.W., Anumula, K., Barr, J.R., Huddleston, M.J. & Taylor, P. (1989) J. Biol.
2209609	8	56	dep	[formula	1370:1377	arg1	see					1380:1382	see	1380:1382	see text	1380:1387	These accounted for over 80% of the sialidase-treated oligosaccharides of sCD4 as follows: [formula: see text] where +/- indicates residues present on only a proportion of chains.
2209609	2	57	gly	N-glycosylation	347:361	arg2	sites					363:367	two N-glycosylation sites	343:367	two N-glycosylation sites	343:367	The glycoprotein has two N-glycosylation sites, Asn271 and Asn300, at both of which evidence for the presence of complex type biantennary sialo-oligosaccharides has been obtained previously by mass spectrometric analyses [Carr, S.A., Hemling, M.E., Folena-Wasserman, G., Sweet, R.W., Anumula, K., Barr, J.R., Huddleston, M.J. & Taylor, P. (1989) J. Biol.
2209609	2	57	gly	N-glycosylation	347:361	arg2	two					343:345	two	343:345	two	343:345	The glycoprotein has two N-glycosylation sites, Asn271 and Asn300, at both of which evidence for the presence of complex type biantennary sialo-oligosaccharides has been obtained previously by mass spectrometric analyses [Carr, S.A., Hemling, M.E., Folena-Wasserman, G., Sweet, R.W., Anumula, K., Barr, J.R., Huddleston, M.J. & Taylor, P. (1989) J. Biol.
2209609	2	58	gly	glycoprotein	326:337	arg1	glycoprotein					326:337	The glycoprotein	322:337	The glycoprotein	322:337	The glycoprotein has two N-glycosylation sites, Asn271 and Asn300, at both of which evidence for the presence of complex type biantennary sialo-oligosaccharides has been obtained previously by mass spectrometric analyses [Carr, S.A., Hemling, M.E., Folena-Wasserman, G., Sweet, R.W., Anumula, K., Barr, J.R., Huddleston, M.J. & Taylor, P. (1989) J. Biol.
2209609	8	59	theme	sialidase-treated	1315:1331	arg1	oligosaccharides					1333:1348	the sialidase-treated oligosaccharides	1311:1348	the sialidase-treated oligosaccharides of sCD4 as follows: [formula: see text] where +/- indicates residues present on only a proportion of chains	1311:1456	These accounted for over 80% of the sialidase-treated oligosaccharides of sCD4 as follows: [formula: see text] where +/- indicates residues present on only a proportion of chains.
2209609	8	60	dep	follows	1361:1367	arg1	[formula					1370:1377	[formula	1370:1377	follows: [formula: see text] where +/- indicates residues present on only a proportion of chains	1361:1456	These accounted for over 80% of the sialidase-treated oligosaccharides of sCD4 as follows: [formula: see text] where +/- indicates residues present on only a proportion of chains.
2209609	2	61	theme	biantennary	448:458	arg1	sialo-oligosaccharides					460:481	complex type biantennary sialo-oligosaccharides	435:481	complex type biantennary sialo-oligosaccharides	435:481	The glycoprotein has two N-glycosylation sites, Asn271 and Asn300, at both of which evidence for the presence of complex type biantennary sialo-oligosaccharides has been obtained previously by mass spectrometric analyses [Carr, S.A., Hemling, M.E., Folena-Wasserman, G., Sweet, R.W., Anumula, K., Barr, J.R., Huddleston, M.J. & Taylor, P. (1989) J. Biol.
2209609	7	62	theme	affinity	1116:1123	arg1	columns					1125:1131	affinity columns	1116:1131	affinity columns of Ricinis communis agglutinin 120 and concanavalin A	1116:1185	By enzymic microsequencing of the sialidase-treated oligosaccharides (fractionated on affinity columns of Ricinis communis agglutinin 120 and concanavalin A) in conjunction with methylation data from the earlier study, 14 sequences were identified.
2209609	8	63	theme	sCD4	1353:1356	arg1	oligosaccharides					1333:1348	the sialidase-treated oligosaccharides	1311:1348	the sialidase-treated oligosaccharides of sCD4 as follows: [formula: see text] where +/- indicates residues present on only a proportion of chains	1311:1456	These accounted for over 80% of the sialidase-treated oligosaccharides of sCD4 as follows: [formula: see text] where +/- indicates residues present on only a proportion of chains.
2209609	2	64	theme	N-glycosylation	347:361	arg1	sites					363:367	two N-glycosylation sites	343:367	two N-glycosylation sites	343:367	The glycoprotein has two N-glycosylation sites, Asn271 and Asn300, at both of which evidence for the presence of complex type biantennary sialo-oligosaccharides has been obtained previously by mass spectrometric analyses [Carr, S.A., Hemling, M.E., Folena-Wasserman, G., Sweet, R.W., Anumula, K., Barr, J.R., Huddleston, M.J. & Taylor, P. (1989) J. Biol.
2209609	7	65	theme	sialidase-treated	1064:1080	arg1	oligosaccharides					1082:1097	the sialidase-treated oligosaccharides	1060:1097	the sialidase-treated oligosaccharides (fractionated on affinity columns of Ricinis communis agglutinin 120 and concanavalin A) in conjunction with methylation data from the earlier study	1060:1246	By enzymic microsequencing of the sialidase-treated oligosaccharides (fractionated on affinity columns of Ricinis communis agglutinin 120 and concanavalin A) in conjunction with methylation data from the earlier study, 14 sequences were identified.
2209609	9	66	gly	glycosylation	1521:1533	arg2	site					1535:1538	each glycosylation site	1516:1538	each glycosylation site	1516:1538	The spectrum of oligosaccharide structures released from each glycosylation site was assessed as being similar to that of total oligosaccharides on the basis of their chromatographic profiles on the lectin columns and on Bio-Gel P-4.
2209609	9	67	theme	profiles	1642:1649	arg1	basis					1611:1615	the basis	1607:1615	the basis of their chromatographic profiles on the lectin columns and on Bio-Gel P-4	1607:1690	The spectrum of oligosaccharide structures released from each glycosylation site was assessed as being similar to that of total oligosaccharides on the basis of their chromatographic profiles on the lectin columns and on Bio-Gel P-4.
2209609	6	68	theme	residues	1020:1027	arg1	presence					996:1003	the presence	992:1003	the presence of sialic acid residues	992:1027	The latter were rendered neutral following sialidase treatment indicating that acidity was due exclusively to the presence of sialic acid residues.
2209609	6	69	theme	sialidase	925:933	arg1	treatment					935:943	sialidase treatment	925:943	sialidase treatment indicating that acidity was due exclusively to the presence of sialic acid residues	925:1027	The latter were rendered neutral following sialidase treatment indicating that acidity was due exclusively to the presence of sialic acid residues.
2209609	8	70	theme	oligosaccharides	1333:1348	arg1	%					1306:1306	over 80%	1299:1306	over 80% of the sialidase-treated oligosaccharides of sCD4 as follows: [formula: see text] where +/- indicates residues present on only a proportion of chains	1299:1456	These accounted for over 80% of the sialidase-treated oligosaccharides of sCD4 as follows: [formula: see text] where +/- indicates residues present on only a proportion of chains.
2209609	8	70	theme	oligosaccharides	1333:1348	arg1	oligosaccharides					1333:1348	the sialidase-treated oligosaccharides	1311:1348	the sialidase-treated oligosaccharides of sCD4 as follows: [formula: see text] where +/- indicates residues present on only a proportion of chains	1311:1456	These accounted for over 80% of the sialidase-treated oligosaccharides of sCD4 as follows: [formula: see text] where +/- indicates residues present on only a proportion of chains.
2209609	7	71	from	study	1242:1246	arg1	data					1220:1223	methylation data	1208:1223	methylation data from the earlier study	1208:1246	By enzymic microsequencing of the sialidase-treated oligosaccharides (fractionated on affinity columns of Ricinis communis agglutinin 120 and concanavalin A) in conjunction with methylation data from the earlier study, 14 sequences were identified.
2209609	6	72	theme	acid	1015:1018	arg1	residues					1020:1027	sialic acid residues	1008:1027	sialic acid residues	1008:1027	The latter were rendered neutral following sialidase treatment indicating that acidity was due exclusively to the presence of sialic acid residues.
2209609	1	73	theme	human	241:245	arg1	sCD4					265:268	sCD4	265:268	sCD4	265:268	Structures of the N-linked oligosaccharides of a recombinant soluble form of human CD4 glycoprotein (sCD4) have been investigated by enzymic microsequencing.
2209609	1	73	theme	human	241:245	arg1	glycoprotein					251:262	human CD4 glycoprotein	241:262	human CD4 glycoprotein (sCD4)	241:269	Structures of the N-linked oligosaccharides of a recombinant soluble form of human CD4 glycoprotein (sCD4) have been investigated by enzymic microsequencing.
2209609	2	74	theme	mass	515:518	arg1	analyses					534:541	mass spectrometric analyses	515:541	mass spectrometric analyses [Carr	515:547	The glycoprotein has two N-glycosylation sites, Asn271 and Asn300, at both of which evidence for the presence of complex type biantennary sialo-oligosaccharides has been obtained previously by mass spectrometric analyses [Carr, S.A., Hemling, M.E., Folena-Wasserman, G., Sweet, R.W., Anumula, K., Barr, J.R., Huddleston, M.J. & Taylor, P. (1989) J. Biol.
2209609	9	75	attach	released	1502:1509	arg2	structures					1491:1500	oligosaccharide structures	1475:1500	oligosaccharide structures released from each glycosylation site	1475:1538	The spectrum of oligosaccharide structures released from each glycosylation site was assessed as being similar to that of total oligosaccharides on the basis of their chromatographic profiles on the lectin columns and on Bio-Gel P-4.
2209609	9	75	attach	released	1502:1509	arg1	site					1535:1538	each glycosylation site	1516:1538	each glycosylation site	1516:1538	The spectrum of oligosaccharide structures released from each glycosylation site was assessed as being similar to that of total oligosaccharides on the basis of their chromatographic profiles on the lectin columns and on Bio-Gel P-4.
2209609	6	76	theme	sialic	1008:1013	arg1	residues					1020:1027	sialic acid residues	1008:1027	sialic acid residues	1008:1027	The latter were rendered neutral following sialidase treatment indicating that acidity was due exclusively to the presence of sialic acid residues.
2209609	1	77	theme	CD4	247:249	arg1	sCD4					265:268	sCD4	265:268	sCD4	265:268	Structures of the N-linked oligosaccharides of a recombinant soluble form of human CD4 glycoprotein (sCD4) have been investigated by enzymic microsequencing.
2209609	1	77	theme	CD4	247:249	arg1	glycoprotein					251:262	human CD4 glycoprotein	241:262	human CD4 glycoprotein (sCD4)	241:269	Structures of the N-linked oligosaccharides of a recombinant soluble form of human CD4 glycoprotein (sCD4) have been investigated by enzymic microsequencing.
2209609	0	78	theme	enzymic	64:70	arg1	microsequencing					72:86	enzymic microsequencing	64:86	enzymic microsequencing	64:86	The spectrum of N-linked oligosaccharide structures detected by enzymic microsequencing on a recombinant soluble CD4 glycoprotein from Chinese hamster ovary cells.
2209609	2	79	contain	has	339:341	arg2	Asn300					381:386	Asn300	381:386	Asn300	381:386	The glycoprotein has two N-glycosylation sites, Asn271 and Asn300, at both of which evidence for the presence of complex type biantennary sialo-oligosaccharides has been obtained previously by mass spectrometric analyses [Carr, S.A., Hemling, M.E., Folena-Wasserman, G., Sweet, R.W., Anumula, K., Barr, J.R., Huddleston, M.J. & Taylor, P. (1989) J. Biol.
2209609	2	79	contain	has	339:341	arg2	Asn271					370:375	Asn271	370:375	Asn271	370:375	The glycoprotein has two N-glycosylation sites, Asn271 and Asn300, at both of which evidence for the presence of complex type biantennary sialo-oligosaccharides has been obtained previously by mass spectrometric analyses [Carr, S.A., Hemling, M.E., Folena-Wasserman, G., Sweet, R.W., Anumula, K., Barr, J.R., Huddleston, M.J. & Taylor, P. (1989) J. Biol.
2209609	2	79	contain	has	339:341	arg2	sites					363:367	two N-glycosylation sites	343:367	two N-glycosylation sites	343:367	The glycoprotein has two N-glycosylation sites, Asn271 and Asn300, at both of which evidence for the presence of complex type biantennary sialo-oligosaccharides has been obtained previously by mass spectrometric analyses [Carr, S.A., Hemling, M.E., Folena-Wasserman, G., Sweet, R.W., Anumula, K., Barr, J.R., Huddleston, M.J. & Taylor, P. (1989) J. Biol.
2209609	2	79	contain	has	339:341	arg1	glycoprotein					326:337	The glycoprotein	322:337	The glycoprotein	322:337	The glycoprotein has two N-glycosylation sites, Asn271 and Asn300, at both of which evidence for the presence of complex type biantennary sialo-oligosaccharides has been obtained previously by mass spectrometric analyses [Carr, S.A., Hemling, M.E., Folena-Wasserman, G., Sweet, R.W., Anumula, K., Barr, J.R., Huddleston, M.J. & Taylor, P. (1989) J. Biol.
2209609	7	80	theme	methylation	1208:1218	arg1	data					1220:1223	methylation data	1208:1223	methylation data from the earlier study	1208:1246	By enzymic microsequencing of the sialidase-treated oligosaccharides (fractionated on affinity columns of Ricinis communis agglutinin 120 and concanavalin A) in conjunction with methylation data from the earlier study, 14 sequences were identified.
2209609	1	81	theme	glycoprotein	251:262	arg1	form					233:236	a recombinant soluble form	211:236	a recombinant soluble form of human CD4 glycoprotein (sCD4)	211:269	Structures of the N-linked oligosaccharides of a recombinant soluble form of human CD4 glycoprotein (sCD4) have been investigated by enzymic microsequencing.
19202066	0	0	theme	glucosamine	82:92	arg1	modification					94:105	O-linked beta-N-acetyl glucosamine modification	59:105	O-linked beta-N-acetyl glucosamine modification	59:105	Loss of p53 enhances catalytic activity of IKKbeta through O-linked beta-N-acetyl glucosamine modification.
19202066	8	1	from	IKK	1523:1525	arg1	oncogenesis					1530:1540	oncogenesis	1530:1540	oncogenesis	1530:1540	Taken together, we propose a novel mechanism for the enhancement of NF-kappaB activity by loss of p53, which evokes positive feedback regulation from enhanced glucose metabolism to IKK in oncogenesis.
19202066	2	2	theme	positive	322:329	arg1	loop					340:343	the positive feedback loop	318:343	the positive feedback loop between IKK-NF-kappaB and glycolysis	318:380	Recently, we have shown that p53 regulates glucose metabolism through the IKK-NF-kappaB pathway and that, in the absence of p53, the positive feedback loop between IKK-NF-kappaB and glycolysis has an integral role in oncogene-induced cell transformation.
19202066	0	3	theme	beta-N-acetyl	68:80	arg1	modification					94:105	O-linked beta-N-acetyl glucosamine modification	59:105	O-linked beta-N-acetyl glucosamine modification	59:105	Loss of p53 enhances catalytic activity of IKKbeta through O-linked beta-N-acetyl glucosamine modification.
19202066	3	4	theme	human	663:667	arg1	fibroblasts					669:679	transformed human fibroblasts	651:679	transformed human fibroblasts	651:679	Here, we demonstrate that IKKbeta, a component of the IKK complex, was constitutively modified with O-linked beta-N-acetyl glucosamine (O-GlcNAc) in both p53-deficient mouse embryonic fibroblasts (MEFs) and transformed human fibroblasts.
19202066	7	5	theme	IKKbeta	1152:1158	arg1	O-GlcNAcylation					1133:1147	O-GlcNAcylation	1133:1147	O-GlcNAcylation of IKKbeta	1133:1158	Mutational analysis revealed that O-GlcNAcylation of IKKbeta occurred at Ser 733 in the C-terminal domain, which was identified as an inactivating phosphorylation site, suggesting that IKKbeta O-GlcNAcylation regulates its catalytic activity.
19202066	5	6	theme	IKKbeta	902:908	arg1	O-GlcNAcylation					883:897	the O-GlcNAcylation	879:897	the O-GlcNAcylation of IKKbeta	879:908	We also found that high glucose induced the O-GlcNAcylation of IKKbeta and sustained the TNFalpha-dependent IKKbeta activity.
19202066	8	7	theme	activity	1420:1427	arg1	enhancement					1395:1405	the enhancement	1391:1405	the enhancement of NF-kappaB activity by loss of p53, which evokes positive feedback regulation from enhanced glucose metabolism to IKK in oncogenesis	1391:1540	Taken together, we propose a novel mechanism for the enhancement of NF-kappaB activity by loss of p53, which evokes positive feedback regulation from enhanced glucose metabolism to IKK in oncogenesis.
19202066	6	8	theme	O-GlcNAcase	979:989	arg1	streptozotocin					1001:1014	the O-GlcNAcase inhibitor streptozotocin	975:1014	the O-GlcNAcase inhibitor streptozotocin	975:1014	Moreover, the O-GlcNAcase inhibitor streptozotocin intensified O-GlcNAcylation and concomitant activating phosphorylation of IKKbeta.
19202066	8	9	theme	NF-kappaB	1410:1418	arg1	activity					1420:1427	NF-kappaB activity	1410:1427	NF-kappaB activity	1410:1427	Taken together, we propose a novel mechanism for the enhancement of NF-kappaB activity by loss of p53, which evokes positive feedback regulation from enhanced glucose metabolism to IKK in oncogenesis.
19202066	7	10	theme	catalytic	1322:1330	arg1	activity					1332:1339	its catalytic activity	1318:1339	its catalytic activity	1318:1339	Mutational analysis revealed that O-GlcNAcylation of IKKbeta occurred at Ser 733 in the C-terminal domain, which was identified as an inactivating phosphorylation site, suggesting that IKKbeta O-GlcNAcylation regulates its catalytic activity.
19202066	4	11	theme	activating	741:750	arg1	phosphorylation					752:766	the activating phosphorylation	737:766	the activating phosphorylation of IKK	737:773	In p53-deficient cells, the O-GlcNAcylated IKKbeta and the activating phosphorylation of IKK were decreased by p65/NF-kappaB knockdown or glucose depletion.
19202066	8	12	theme	novel	1371:1375	arg1	mechanism					1377:1385	a novel mechanism	1369:1385	a novel mechanism for the enhancement of NF-kappaB activity by loss of p53, which evokes positive feedback regulation from enhanced glucose metabolism to IKK in oncogenesis	1369:1540	Taken together, we propose a novel mechanism for the enhancement of NF-kappaB activity by loss of p53, which evokes positive feedback regulation from enhanced glucose metabolism to IKK in oncogenesis.
19202066	7	13	theme	phosphorylation	1246:1260	arg1	domain					1198:1203	the C-terminal domain	1183:1203	the C-terminal domain	1183:1203	Mutational analysis revealed that O-GlcNAcylation of IKKbeta occurred at Ser 733 in the C-terminal domain, which was identified as an inactivating phosphorylation site, suggesting that IKKbeta O-GlcNAcylation regulates its catalytic activity.
19202066	7	13	theme	phosphorylation	1246:1260	arg1	site					1262:1265	an inactivating phosphorylation site	1230:1265	an inactivating phosphorylation site	1230:1265	Mutational analysis revealed that O-GlcNAcylation of IKKbeta occurred at Ser 733 in the C-terminal domain, which was identified as an inactivating phosphorylation site, suggesting that IKKbeta O-GlcNAcylation regulates its catalytic activity.
19202066	4	14	theme	O-GlcNAcylated	710:723	arg1	IKKbeta					725:731	the O-GlcNAcylated IKKbeta	706:731	the O-GlcNAcylated IKKbeta	706:731	In p53-deficient cells, the O-GlcNAcylated IKKbeta and the activating phosphorylation of IKK were decreased by p65/NF-kappaB knockdown or glucose depletion.
19202066	2	15	theme	IKK-NF-kappaB	263:275	arg1	pathway					277:283	the IKK-NF-kappaB pathway	259:283	the IKK-NF-kappaB pathway	259:283	Recently, we have shown that p53 regulates glucose metabolism through the IKK-NF-kappaB pathway and that, in the absence of p53, the positive feedback loop between IKK-NF-kappaB and glycolysis has an integral role in oncogene-induced cell transformation.
19202066	1	16	theme	critical	159:166	arg1	role					168:171	a critical role	157:171	a critical role	157:171	The IkappaB kinase (IKK)-NF-kappaB pathway plays a critical role in oncogenesis.
19202066	3	17	theme	complex	502:508	arg1	IKKbeta					470:476	IKKbeta	470:476	IKKbeta	470:476	Here, we demonstrate that IKKbeta, a component of the IKK complex, was constitutively modified with O-linked beta-N-acetyl glucosamine (O-GlcNAc) in both p53-deficient mouse embryonic fibroblasts (MEFs) and transformed human fibroblasts.
19202066	3	17	theme	complex	502:508	arg1	component					481:489	a component	479:489	a component of the IKK complex	479:508	Here, we demonstrate that IKKbeta, a component of the IKK complex, was constitutively modified with O-linked beta-N-acetyl glucosamine (O-GlcNAc) in both p53-deficient mouse embryonic fibroblasts (MEFs) and transformed human fibroblasts.
19202066	8	18	theme	positive	1458:1465	arg1	regulation					1476:1485	positive feedback regulation	1458:1485	positive feedback regulation	1458:1485	Taken together, we propose a novel mechanism for the enhancement of NF-kappaB activity by loss of p53, which evokes positive feedback regulation from enhanced glucose metabolism to IKK in oncogenesis.
19202066	5	19	theme	high	858:861	arg1	glucose					863:869	high glucose	858:869	high glucose	858:869	We also found that high glucose induced the O-GlcNAcylation of IKKbeta and sustained the TNFalpha-dependent IKKbeta activity.
19202066	3	20	link	O-linked	544:551	arg1	O-GlcNAc					580:587	O-GlcNAc	580:587	O-GlcNAc	580:587	Here, we demonstrate that IKKbeta, a component of the IKK complex, was constitutively modified with O-linked beta-N-acetyl glucosamine (O-GlcNAc) in both p53-deficient mouse embryonic fibroblasts (MEFs) and transformed human fibroblasts.
19202066	3	20	link	O-linked	544:551	arg1	glucosamine					567:577	O-linked beta-N-acetyl glucosamine	544:577	O-linked beta-N-acetyl glucosamine (O-GlcNAc) in both p53-deficient mouse embryonic fibroblasts (MEFs) and transformed human fibroblasts	544:679	Here, we demonstrate that IKKbeta, a component of the IKK complex, was constitutively modified with O-linked beta-N-acetyl glucosamine (O-GlcNAc) in both p53-deficient mouse embryonic fibroblasts (MEFs) and transformed human fibroblasts.
19202066	7	21	theme	IKKbeta	1284:1290	arg1	O-GlcNAcylation					1292:1306	IKKbeta O-GlcNAcylation	1284:1306	IKKbeta O-GlcNAcylation	1284:1306	Mutational analysis revealed that O-GlcNAcylation of IKKbeta occurred at Ser 733 in the C-terminal domain, which was identified as an inactivating phosphorylation site, suggesting that IKKbeta O-GlcNAcylation regulates its catalytic activity.
19202066	5	22	theme	IKKbeta	947:953	arg1	activity					955:962	the TNFalpha-dependent IKKbeta activity	924:962	the TNFalpha-dependent IKKbeta activity	924:962	We also found that high glucose induced the O-GlcNAcylation of IKKbeta and sustained the TNFalpha-dependent IKKbeta activity.
19202066	2	23	theme	cell	423:426	arg1	transformation					428:441	oncogene-induced cell transformation	406:441	oncogene-induced cell transformation	406:441	Recently, we have shown that p53 regulates glucose metabolism through the IKK-NF-kappaB pathway and that, in the absence of p53, the positive feedback loop between IKK-NF-kappaB and glycolysis has an integral role in oncogene-induced cell transformation.
19202066	6	24	theme	inhibitor	991:999	arg1	streptozotocin					1001:1014	the O-GlcNAcase inhibitor streptozotocin	975:1014	the O-GlcNAcase inhibitor streptozotocin	975:1014	Moreover, the O-GlcNAcase inhibitor streptozotocin intensified O-GlcNAcylation and concomitant activating phosphorylation of IKKbeta.
19202066	3	25	theme	O-linked	544:551	arg1	O-GlcNAc					580:587	O-GlcNAc	580:587	O-GlcNAc	580:587	Here, we demonstrate that IKKbeta, a component of the IKK complex, was constitutively modified with O-linked beta-N-acetyl glucosamine (O-GlcNAc) in both p53-deficient mouse embryonic fibroblasts (MEFs) and transformed human fibroblasts.
19202066	3	25	theme	O-linked	544:551	arg1	glucosamine					567:577	O-linked beta-N-acetyl glucosamine	544:577	O-linked beta-N-acetyl glucosamine (O-GlcNAc) in both p53-deficient mouse embryonic fibroblasts (MEFs) and transformed human fibroblasts	544:679	Here, we demonstrate that IKKbeta, a component of the IKK complex, was constitutively modified with O-linked beta-N-acetyl glucosamine (O-GlcNAc) in both p53-deficient mouse embryonic fibroblasts (MEFs) and transformed human fibroblasts.
19202066	7	26	theme	C-terminal	1187:1196	arg1	domain					1198:1203	the C-terminal domain	1183:1203	the C-terminal domain	1183:1203	Mutational analysis revealed that O-GlcNAcylation of IKKbeta occurred at Ser 733 in the C-terminal domain, which was identified as an inactivating phosphorylation site, suggesting that IKKbeta O-GlcNAcylation regulates its catalytic activity.
19202066	7	26	theme	C-terminal	1187:1196	arg1	site					1262:1265	an inactivating phosphorylation site	1230:1265	an inactivating phosphorylation site	1230:1265	Mutational analysis revealed that O-GlcNAcylation of IKKbeta occurred at Ser 733 in the C-terminal domain, which was identified as an inactivating phosphorylation site, suggesting that IKKbeta O-GlcNAcylation regulates its catalytic activity.
19202066	2	27	theme	oncogene-induced	406:421	arg1	transformation					428:441	oncogene-induced cell transformation	406:441	oncogene-induced cell transformation	406:441	Recently, we have shown that p53 regulates glucose metabolism through the IKK-NF-kappaB pathway and that, in the absence of p53, the positive feedback loop between IKK-NF-kappaB and glycolysis has an integral role in oncogene-induced cell transformation.
19202066	4	28	theme	p65/NF-kappaB	793:805	arg1	knockdown					807:815	p65/NF-kappaB knockdown	793:815	p65/NF-kappaB knockdown	793:815	In p53-deficient cells, the O-GlcNAcylated IKKbeta and the activating phosphorylation of IKK were decreased by p65/NF-kappaB knockdown or glucose depletion.
19202066	8	29	theme	feedback	1467:1474	arg1	regulation					1476:1485	positive feedback regulation	1458:1485	positive feedback regulation	1458:1485	Taken together, we propose a novel mechanism for the enhancement of NF-kappaB activity by loss of p53, which evokes positive feedback regulation from enhanced glucose metabolism to IKK in oncogenesis.
19202066	3	30	from	glucosamine	567:577	arg1	fibroblasts					628:638	p53-deficient mouse embryonic fibroblasts	598:638	p53-deficient mouse embryonic fibroblasts (MEFs)	598:645	Here, we demonstrate that IKKbeta, a component of the IKK complex, was constitutively modified with O-linked beta-N-acetyl glucosamine (O-GlcNAc) in both p53-deficient mouse embryonic fibroblasts (MEFs) and transformed human fibroblasts.
19202066	3	30	from	glucosamine	567:577	arg1	fibroblasts					669:679	transformed human fibroblasts	651:679	transformed human fibroblasts	651:679	Here, we demonstrate that IKKbeta, a component of the IKK complex, was constitutively modified with O-linked beta-N-acetyl glucosamine (O-GlcNAc) in both p53-deficient mouse embryonic fibroblasts (MEFs) and transformed human fibroblasts.
19202066	3	30	from	glucosamine	567:577	arg1	MEFs					641:644	MEFs	641:644	MEFs	641:644	Here, we demonstrate that IKKbeta, a component of the IKK complex, was constitutively modified with O-linked beta-N-acetyl glucosamine (O-GlcNAc) in both p53-deficient mouse embryonic fibroblasts (MEFs) and transformed human fibroblasts.
19202066	0	31	theme	p53	8:10	arg1	Loss					0:3	Loss	0:3	Loss of p53	0:10	Loss of p53 enhances catalytic activity of IKKbeta through O-linked beta-N-acetyl glucosamine modification.
19202066	3	32	theme	IKK	498:500	arg1	complex					502:508	the IKK complex	494:508	the IKK complex	494:508	Here, we demonstrate that IKKbeta, a component of the IKK complex, was constitutively modified with O-linked beta-N-acetyl glucosamine (O-GlcNAc) in both p53-deficient mouse embryonic fibroblasts (MEFs) and transformed human fibroblasts.
19202066	1	33	theme	IkappaB	112:118	arg1	IKK					128:130	IKK	128:130	IKK	128:130	The IkappaB kinase (IKK)-NF-kappaB pathway plays a critical role in oncogenesis.
19202066	1	33	theme	IkappaB	112:118	arg1	kinase					120:125	IkappaB kinase	112:125	The IkappaB kinase (IKK)-NF-kappaB pathway	108:149	The IkappaB kinase (IKK)-NF-kappaB pathway plays a critical role in oncogenesis.
19202066	8	34	theme	p53	1440:1442	arg1	loss					1432:1435	loss	1432:1435	loss	1432:1435	Taken together, we propose a novel mechanism for the enhancement of NF-kappaB activity by loss of p53, which evokes positive feedback regulation from enhanced glucose metabolism to IKK in oncogenesis.
19202066	2	35	theme	integral	389:396	arg1	role					398:401	an integral role	386:401	an integral role	386:401	Recently, we have shown that p53 regulates glucose metabolism through the IKK-NF-kappaB pathway and that, in the absence of p53, the positive feedback loop between IKK-NF-kappaB and glycolysis has an integral role in oncogene-induced cell transformation.
19202066	4	36	theme	p53-deficient	685:697	arg1	cells					699:703	p53-deficient cells	685:703	p53-deficient cells	685:703	In p53-deficient cells, the O-GlcNAcylated IKKbeta and the activating phosphorylation of IKK were decreased by p65/NF-kappaB knockdown or glucose depletion.
19202066	7	37	theme	inactivating	1233:1244	arg1	domain					1198:1203	the C-terminal domain	1183:1203	the C-terminal domain	1183:1203	Mutational analysis revealed that O-GlcNAcylation of IKKbeta occurred at Ser 733 in the C-terminal domain, which was identified as an inactivating phosphorylation site, suggesting that IKKbeta O-GlcNAcylation regulates its catalytic activity.
19202066	7	37	theme	inactivating	1233:1244	arg1	site					1262:1265	an inactivating phosphorylation site	1230:1265	an inactivating phosphorylation site	1230:1265	Mutational analysis revealed that O-GlcNAcylation of IKKbeta occurred at Ser 733 in the C-terminal domain, which was identified as an inactivating phosphorylation site, suggesting that IKKbeta O-GlcNAcylation regulates its catalytic activity.
19202066	3	38	mod	modified	530:537	arg1	IKKbeta					470:476	IKKbeta	470:476	IKKbeta	470:476	Here, we demonstrate that IKKbeta, a component of the IKK complex, was constitutively modified with O-linked beta-N-acetyl glucosamine (O-GlcNAc) in both p53-deficient mouse embryonic fibroblasts (MEFs) and transformed human fibroblasts.
19202066	3	38	mod	modified	530:537	arg1	component					481:489	a component	479:489	a component of the IKK complex	479:508	Here, we demonstrate that IKKbeta, a component of the IKK complex, was constitutively modified with O-linked beta-N-acetyl glucosamine (O-GlcNAc) in both p53-deficient mouse embryonic fibroblasts (MEFs) and transformed human fibroblasts.
19202066	3	38	mod	modified	530:537	arg3	glucosamine					567:577	O-linked beta-N-acetyl glucosamine	544:577	O-linked beta-N-acetyl glucosamine (O-GlcNAc) in both p53-deficient mouse embryonic fibroblasts (MEFs) and transformed human fibroblasts	544:679	Here, we demonstrate that IKKbeta, a component of the IKK complex, was constitutively modified with O-linked beta-N-acetyl glucosamine (O-GlcNAc) in both p53-deficient mouse embryonic fibroblasts (MEFs) and transformed human fibroblasts.
19202066	3	38	mod	modified	530:537	arg3	O-GlcNAc					580:587	O-GlcNAc	580:587	O-GlcNAc	580:587	Here, we demonstrate that IKKbeta, a component of the IKK complex, was constitutively modified with O-linked beta-N-acetyl glucosamine (O-GlcNAc) in both p53-deficient mouse embryonic fibroblasts (MEFs) and transformed human fibroblasts.
19202066	0	39	theme	catalytic	21:29	arg1	activity					31:38	catalytic activity	21:38	catalytic activity of IKKbeta	21:49	Loss of p53 enhances catalytic activity of IKKbeta through O-linked beta-N-acetyl glucosamine modification.
19202066	3	40	theme	mouse	612:616	arg1	fibroblasts					628:638	p53-deficient mouse embryonic fibroblasts	598:638	p53-deficient mouse embryonic fibroblasts (MEFs)	598:645	Here, we demonstrate that IKKbeta, a component of the IKK complex, was constitutively modified with O-linked beta-N-acetyl glucosamine (O-GlcNAc) in both p53-deficient mouse embryonic fibroblasts (MEFs) and transformed human fibroblasts.
19202066	3	40	theme	mouse	612:616	arg1	MEFs					641:644	MEFs	641:644	MEFs	641:644	Here, we demonstrate that IKKbeta, a component of the IKK complex, was constitutively modified with O-linked beta-N-acetyl glucosamine (O-GlcNAc) in both p53-deficient mouse embryonic fibroblasts (MEFs) and transformed human fibroblasts.
19202066	6	41	theme	IKKbeta	1090:1096	arg1	O-GlcNAcylation					1028:1042	O-GlcNAcylation	1028:1042	O-GlcNAcylation	1028:1042	Moreover, the O-GlcNAcase inhibitor streptozotocin intensified O-GlcNAcylation and concomitant activating phosphorylation of IKKbeta.
19202066	6	41	theme	IKKbeta	1090:1096	arg1	phosphorylation					1071:1085	concomitant activating phosphorylation	1048:1085	concomitant activating phosphorylation of IKKbeta	1048:1096	Moreover, the O-GlcNAcase inhibitor streptozotocin intensified O-GlcNAcylation and concomitant activating phosphorylation of IKKbeta.
19202066	0	42	theme	IKKbeta	43:49	arg1	activity					31:38	catalytic activity	21:38	catalytic activity of IKKbeta	21:49	Loss of p53 enhances catalytic activity of IKKbeta through O-linked beta-N-acetyl glucosamine modification.
19202066	7	43	theme	Mutational	1099:1108	arg1	analysis					1110:1117	Mutational analysis	1099:1117	Mutational analysis	1099:1117	Mutational analysis revealed that O-GlcNAcylation of IKKbeta occurred at Ser 733 in the C-terminal domain, which was identified as an inactivating phosphorylation site, suggesting that IKKbeta O-GlcNAcylation regulates its catalytic activity.
19202066	3	44	theme	embryonic	618:626	arg1	fibroblasts					628:638	p53-deficient mouse embryonic fibroblasts	598:638	p53-deficient mouse embryonic fibroblasts (MEFs)	598:645	Here, we demonstrate that IKKbeta, a component of the IKK complex, was constitutively modified with O-linked beta-N-acetyl glucosamine (O-GlcNAc) in both p53-deficient mouse embryonic fibroblasts (MEFs) and transformed human fibroblasts.
19202066	3	44	theme	embryonic	618:626	arg1	MEFs					641:644	MEFs	641:644	MEFs	641:644	Here, we demonstrate that IKKbeta, a component of the IKK complex, was constitutively modified with O-linked beta-N-acetyl glucosamine (O-GlcNAc) in both p53-deficient mouse embryonic fibroblasts (MEFs) and transformed human fibroblasts.
19202066	3	45	theme	beta-N-acetyl	553:565	arg1	O-GlcNAc					580:587	O-GlcNAc	580:587	O-GlcNAc	580:587	Here, we demonstrate that IKKbeta, a component of the IKK complex, was constitutively modified with O-linked beta-N-acetyl glucosamine (O-GlcNAc) in both p53-deficient mouse embryonic fibroblasts (MEFs) and transformed human fibroblasts.
19202066	3	45	theme	beta-N-acetyl	553:565	arg1	glucosamine					567:577	O-linked beta-N-acetyl glucosamine	544:577	O-linked beta-N-acetyl glucosamine (O-GlcNAc) in both p53-deficient mouse embryonic fibroblasts (MEFs) and transformed human fibroblasts	544:679	Here, we demonstrate that IKKbeta, a component of the IKK complex, was constitutively modified with O-linked beta-N-acetyl glucosamine (O-GlcNAc) in both p53-deficient mouse embryonic fibroblasts (MEFs) and transformed human fibroblasts.
19202066	1	46	theme	kinase	120:125	arg1	pathway					143:149	The IkappaB kinase (IKK)-NF-kappaB pathway	108:149	The IkappaB kinase (IKK)-NF-kappaB pathway	108:149	The IkappaB kinase (IKK)-NF-kappaB pathway plays a critical role in oncogenesis.
19202066	2	47	contain	has	382:384	arg2	role					398:401	an integral role	386:401	an integral role	386:401	Recently, we have shown that p53 regulates glucose metabolism through the IKK-NF-kappaB pathway and that, in the absence of p53, the positive feedback loop between IKK-NF-kappaB and glycolysis has an integral role in oncogene-induced cell transformation.
19202066	2	47	contain	has	382:384	arg1	loop					340:343	the positive feedback loop	318:343	the positive feedback loop between IKK-NF-kappaB and glycolysis	318:380	Recently, we have shown that p53 regulates glucose metabolism through the IKK-NF-kappaB pathway and that, in the absence of p53, the positive feedback loop between IKK-NF-kappaB and glycolysis has an integral role in oncogene-induced cell transformation.
19202066	4	48	theme	glucose	820:826	arg1	depletion					828:836	glucose depletion	820:836	glucose depletion	820:836	In p53-deficient cells, the O-GlcNAcylated IKKbeta and the activating phosphorylation of IKK were decreased by p65/NF-kappaB knockdown or glucose depletion.
19202066	0	49	link	O-linked	59:66	arg1	modification					94:105	O-linked beta-N-acetyl glucosamine modification	59:105	O-linked beta-N-acetyl glucosamine modification	59:105	Loss of p53 enhances catalytic activity of IKKbeta through O-linked beta-N-acetyl glucosamine modification.
19202066	2	50	theme	p53	313:315	arg1	absence					302:308	the absence	298:308	the absence of p53	298:315	Recently, we have shown that p53 regulates glucose metabolism through the IKK-NF-kappaB pathway and that, in the absence of p53, the positive feedback loop between IKK-NF-kappaB and glycolysis has an integral role in oncogene-induced cell transformation.
19202066	3	51	theme	transformed	651:661	arg1	fibroblasts					669:679	transformed human fibroblasts	651:679	transformed human fibroblasts	651:679	Here, we demonstrate that IKKbeta, a component of the IKK complex, was constitutively modified with O-linked beta-N-acetyl glucosamine (O-GlcNAc) in both p53-deficient mouse embryonic fibroblasts (MEFs) and transformed human fibroblasts.
19202066	8	52	theme	enhanced	1492:1499	arg1	metabolism					1509:1518	enhanced glucose metabolism	1492:1518	enhanced glucose metabolism	1492:1518	Taken together, we propose a novel mechanism for the enhancement of NF-kappaB activity by loss of p53, which evokes positive feedback regulation from enhanced glucose metabolism to IKK in oncogenesis.
19202066	4	53	theme	IKK	771:773	arg1	phosphorylation					752:766	the activating phosphorylation	737:766	the activating phosphorylation of IKK	737:773	In p53-deficient cells, the O-GlcNAcylated IKKbeta and the activating phosphorylation of IKK were decreased by p65/NF-kappaB knockdown or glucose depletion.
19202066	4	53	theme	IKK	771:773	arg1	IKKbeta					725:731	the O-GlcNAcylated IKKbeta	706:731	the O-GlcNAcylated IKKbeta	706:731	In p53-deficient cells, the O-GlcNAcylated IKKbeta and the activating phosphorylation of IKK were decreased by p65/NF-kappaB knockdown or glucose depletion.
19202066	3	54	theme	p53-deficient	598:610	arg1	fibroblasts					628:638	p53-deficient mouse embryonic fibroblasts	598:638	p53-deficient mouse embryonic fibroblasts (MEFs)	598:645	Here, we demonstrate that IKKbeta, a component of the IKK complex, was constitutively modified with O-linked beta-N-acetyl glucosamine (O-GlcNAc) in both p53-deficient mouse embryonic fibroblasts (MEFs) and transformed human fibroblasts.
19202066	3	54	theme	p53-deficient	598:610	arg1	MEFs					641:644	MEFs	641:644	MEFs	641:644	Here, we demonstrate that IKKbeta, a component of the IKK complex, was constitutively modified with O-linked beta-N-acetyl glucosamine (O-GlcNAc) in both p53-deficient mouse embryonic fibroblasts (MEFs) and transformed human fibroblasts.
19202066	5	55	theme	TNFalpha-dependent	928:945	arg1	activity					955:962	the TNFalpha-dependent IKKbeta activity	924:962	the TNFalpha-dependent IKKbeta activity	924:962	We also found that high glucose induced the O-GlcNAcylation of IKKbeta and sustained the TNFalpha-dependent IKKbeta activity.
19202066	0	56	theme	O-linked	59:66	arg1	modification					94:105	O-linked beta-N-acetyl glucosamine modification	59:105	O-linked beta-N-acetyl glucosamine modification	59:105	Loss of p53 enhances catalytic activity of IKKbeta through O-linked beta-N-acetyl glucosamine modification.
19202066	2	57	theme	glucose	232:238	arg1	metabolism					240:249	glucose metabolism	232:249	glucose metabolism	232:249	Recently, we have shown that p53 regulates glucose metabolism through the IKK-NF-kappaB pathway and that, in the absence of p53, the positive feedback loop between IKK-NF-kappaB and glycolysis has an integral role in oncogene-induced cell transformation.
19202066	1	58	theme	-NF-kappaB	132:141	arg1	pathway					143:149	The IkappaB kinase (IKK)-NF-kappaB pathway	108:149	The IkappaB kinase (IKK)-NF-kappaB pathway	108:149	The IkappaB kinase (IKK)-NF-kappaB pathway plays a critical role in oncogenesis.
19202066	6	59	theme	activating	1060:1069	arg1	phosphorylation					1071:1085	concomitant activating phosphorylation	1048:1085	concomitant activating phosphorylation of IKKbeta	1048:1096	Moreover, the O-GlcNAcase inhibitor streptozotocin intensified O-GlcNAcylation and concomitant activating phosphorylation of IKKbeta.
19202066	8	60	theme	glucose	1501:1507	arg1	metabolism					1509:1518	enhanced glucose metabolism	1492:1518	enhanced glucose metabolism	1492:1518	Taken together, we propose a novel mechanism for the enhancement of NF-kappaB activity by loss of p53, which evokes positive feedback regulation from enhanced glucose metabolism to IKK in oncogenesis.
19202066	2	61	theme	feedback	331:338	arg1	loop					340:343	the positive feedback loop	318:343	the positive feedback loop between IKK-NF-kappaB and glycolysis	318:380	Recently, we have shown that p53 regulates glucose metabolism through the IKK-NF-kappaB pathway and that, in the absence of p53, the positive feedback loop between IKK-NF-kappaB and glycolysis has an integral role in oncogene-induced cell transformation.
19202066	6	62	theme	concomitant	1048:1058	arg1	phosphorylation					1071:1085	concomitant activating phosphorylation	1048:1085	concomitant activating phosphorylation of IKKbeta	1048:1096	Moreover, the O-GlcNAcase inhibitor streptozotocin intensified O-GlcNAcylation and concomitant activating phosphorylation of IKKbeta.
9538010	0	0	theme	L-selectin	90:99	arg1	ligand					101:106	L-selectin ligand	90:106	L-selectin ligand activity	90:115	Human low-molecular-weight salivary mucin expresses the sialyl lewisx determinant and has L-selectin ligand activity.
9538010	5	1	dep	NeuAcalpha2-->3Galbeta1-->3GalNAc-ol	822:857	arg1	[type					946:950	[type	946:950	[type	946:950	Of the 41 different structures we detected, the most prominent included NeuAcalpha2-->3Galbeta1-->3GalNAc-ol (sialyl-T antigen), Galbeta1-->4(Fucalpha1-->3)GlcNAcbeta1-->6(Galbeta1 -->3)GalNAc-ol [type 2 core with Lewisx (Lex) determinant], and NeuAcalpha2-->3Galbeta1-->4(Fucalpha1-->3)GlcNAcbet a1-->6(Galbeta1--> 3) GalNAc-ol [type 2 core with sialyl Lex (sLex) determinant].
9538010	4	2	theme	magnetic	695:702	arg1	resonance					704:712	nuclear magnetic resonance	687:712	nuclear magnetic resonance spectroscopy	687:725	The released oligosaccharides were characterized by using nuclear magnetic resonance spectroscopy and mass spectrometry.
9538010	10	3	theme	L-Selectin	1510:1519	arg1	chimeras					1521:1528	L-Selectin chimeras	1510:1528	L-Selectin chimeras	1510:1528	L-Selectin chimeras also bound to MG2 immobilized on nitrocellulose.
9538010	1	4	theme	saliva	251:256	arg1	mucin					169:173	the low-molecular-weight mucin	144:173	the low-molecular-weight mucin (MG2, encoded by MUC7)	144:196	Previously we showed that the low-molecular-weight mucin (MG2, encoded by MUC7), a major component of human submandibular/sublingual saliva, is a bacterial receptor that coats the tooth surface.
9538010	1	4	theme	saliva	251:256	arg1	component					207:215	a major component	199:215	a major component of human submandibular/sublingual saliva	199:256	Previously we showed that the low-molecular-weight mucin (MG2, encoded by MUC7), a major component of human submandibular/sublingual saliva, is a bacterial receptor that coats the tooth surface.
9538010	4	5	theme	nuclear	687:693	arg1	resonance					704:712	nuclear magnetic resonance	687:712	nuclear magnetic resonance spectroscopy	687:725	The released oligosaccharides were characterized by using nuclear magnetic resonance spectroscopy and mass spectrometry.
9538010	3	6	contain	carried	539:545	arg1	fragment					523:530	the resulting Mr 90 000 fragment	499:530	the resulting Mr 90 000 fragment	499:530	Purified MG2 (Mr 120 000) was digested with trypsin, and the resulting Mr 90 000 fragment, which carried primarily O-linked oligosaccharides, was subjected to reductive beta-elimination.
9538010	3	6	contain	carried	539:545	arg2	oligosaccharides					566:581	primarily O-linked oligosaccharides	547:581	primarily O-linked oligosaccharides	547:581	Purified MG2 (Mr 120 000) was digested with trypsin, and the resulting Mr 90 000 fragment, which carried primarily O-linked oligosaccharides, was subjected to reductive beta-elimination.
9538010	8	7	theme	selectin	1372:1379	arg1	MG2					1362:1364	MG2	1362:1364	MG2	1362:1364	Therefore, we investigated whether MG2 was a selectin ligand.
9538010	8	7	theme	selectin	1372:1379	arg1	ligand					1381:1386	a selectin ligand	1370:1386	a selectin ligand	1370:1386	Therefore, we investigated whether MG2 was a selectin ligand.
9538010	3	8	theme	Mr	513:514	arg1	fragment					523:530	the resulting Mr 90 000 fragment	499:530	the resulting Mr 90 000 fragment	499:530	Purified MG2 (Mr 120 000) was digested with trypsin, and the resulting Mr 90 000 fragment, which carried primarily O-linked oligosaccharides, was subjected to reductive beta-elimination.
9538010	11	9	theme	oral	1754:1757	arg1	cavity					1759:1764	the oral cavity	1750:1764	the oral cavity	1750:1764	Together, these results suggest that the saccharides that MG2 carries could specify some of its important functions, which may include mediating leukocyte interactions in the oral cavity.
9538010	0	10	theme	ligand	101:106	arg1	activity					108:115	L-selectin ligand activity	90:115	L-selectin ligand activity	90:115	Human low-molecular-weight salivary mucin expresses the sialyl lewisx determinant and has L-selectin ligand activity.
9538010	5	11	dep	Galbeta1-->	1054:1064	arg1	3					1066:1066	3	1066:1066	3	1066:1066	Of the 41 different structures we detected, the most prominent included NeuAcalpha2-->3Galbeta1-->3GalNAc-ol (sialyl-T antigen), Galbeta1-->4(Fucalpha1-->3)GlcNAcbeta1-->6(Galbeta1 -->3)GalNAc-ol [type 2 core with Lewisx (Lex) determinant], and NeuAcalpha2-->3Galbeta1-->4(Fucalpha1-->3)GlcNAcbet a1-->6(Galbeta1--> 3) GalNAc-ol [type 2 core with sialyl Lex (sLex) determinant].
9538010	5	11	dep	Galbeta1-->	1054:1064	arg1	core					1087:1090	GalNAc-ol [type 2 core	1069:1090	Galbeta1--> 3) GalNAc-ol [type 2 core with sialyl Lex (sLex) determinant	1054:1125	Of the 41 different structures we detected, the most prominent included NeuAcalpha2-->3Galbeta1-->3GalNAc-ol (sialyl-T antigen), Galbeta1-->4(Fucalpha1-->3)GlcNAcbeta1-->6(Galbeta1 -->3)GalNAc-ol [type 2 core with Lewisx (Lex) determinant], and NeuAcalpha2-->3Galbeta1-->4(Fucalpha1-->3)GlcNAcbet a1-->6(Galbeta1--> 3) GalNAc-ol [type 2 core with sialyl Lex (sLex) determinant].
9538010	5	12	theme	sialyl	1097:1102	arg1	determinant					1115:1125	sialyl Lex (sLex) determinant	1097:1125	sialyl Lex (sLex) determinant	1097:1125	Of the 41 different structures we detected, the most prominent included NeuAcalpha2-->3Galbeta1-->3GalNAc-ol (sialyl-T antigen), Galbeta1-->4(Fucalpha1-->3)GlcNAcbeta1-->6(Galbeta1 -->3)GalNAc-ol [type 2 core with Lewisx (Lex) determinant], and NeuAcalpha2-->3Galbeta1-->4(Fucalpha1-->3)GlcNAcbet a1-->6(Galbeta1--> 3) GalNAc-ol [type 2 core with sialyl Lex (sLex) determinant].
9538010	5	13	with	[type	946:950	arg1	determinant					977:987	Lewisx (Lex) determinant	964:987	Lewisx (Lex) determinant	964:987	Of the 41 different structures we detected, the most prominent included NeuAcalpha2-->3Galbeta1-->3GalNAc-ol (sialyl-T antigen), Galbeta1-->4(Fucalpha1-->3)GlcNAcbeta1-->6(Galbeta1 -->3)GalNAc-ol [type 2 core with Lewisx (Lex) determinant], and NeuAcalpha2-->3Galbeta1-->4(Fucalpha1-->3)GlcNAcbet a1-->6(Galbeta1--> 3) GalNAc-ol [type 2 core with sialyl Lex (sLex) determinant].
9538010	7	14	theme	adhesion	1272:1279	arg1	molecules					1281:1289	adhesion molecules	1272:1289	adhesion molecules that mediate leukocyte trafficking	1272:1324	Lex, sLex, and related sulfated structures are ligands for selectins, adhesion molecules that mediate leukocyte trafficking.
9538010	7	14	theme	adhesion	1272:1279	arg1	ligands					1249:1255	ligands	1249:1255	ligands for selectins	1249:1269	Lex, sLex, and related sulfated structures are ligands for selectins, adhesion molecules that mediate leukocyte trafficking.
9538010	2	15	theme	residues	382:389	arg1	structure					352:360	the structure	348:360	the structure of its carbohydrate residues	348:389	Here we tested the hypothesis that the structure of its carbohydrate residues contains important information about its function.
9538010	5	16	theme	Lex	1104:1106	arg1	determinant					1115:1125	sialyl Lex (sLex) determinant	1097:1125	sialyl Lex (sLex) determinant	1097:1125	Of the 41 different structures we detected, the most prominent included NeuAcalpha2-->3Galbeta1-->3GalNAc-ol (sialyl-T antigen), Galbeta1-->4(Fucalpha1-->3)GlcNAcbeta1-->6(Galbeta1 -->3)GalNAc-ol [type 2 core with Lewisx (Lex) determinant], and NeuAcalpha2-->3Galbeta1-->4(Fucalpha1-->3)GlcNAcbet a1-->6(Galbeta1--> 3) GalNAc-ol [type 2 core with sialyl Lex (sLex) determinant].
9538010	9	17	theme	Ca2+-dependent	1487:1500	arg1	manner					1502:1507	a Ca2+-dependent manner	1485:1507	a Ca2+-dependent manner	1485:1507	In an enzyme-linked immunosorbent assay, L-selectin chimeras interacted with immobilized MG2 in a Ca2+-dependent manner.
9538010	3	18	theme	resulting	503:511	arg1	fragment					523:530	the resulting Mr 90 000 fragment	499:530	the resulting Mr 90 000 fragment	499:530	Purified MG2 (Mr 120 000) was digested with trypsin, and the resulting Mr 90 000 fragment, which carried primarily O-linked oligosaccharides, was subjected to reductive beta-elimination.
9538010	2	19	theme	carbohydrate	369:380	arg1	residues					382:389	its carbohydrate residues	365:389	its carbohydrate residues	365:389	Here we tested the hypothesis that the structure of its carbohydrate residues contains important information about its function.
9538010	0	20	theme	low-molecular-weight	6:25	arg1	mucin					36:40	Human low-molecular-weight salivary mucin	0:40	Human low-molecular-weight salivary mucin	0:40	Human low-molecular-weight salivary mucin expresses the sialyl lewisx determinant and has L-selectin ligand activity.
9538010	9	21	link	enzyme-linked	1395:1407	arg1	assay					1423:1427	an enzyme-linked immunosorbent assay	1392:1427	an enzyme-linked immunosorbent assay	1392:1427	In an enzyme-linked immunosorbent assay, L-selectin chimeras interacted with immobilized MG2 in a Ca2+-dependent manner.
9538010	4	22	theme	released	633:640	arg1	oligosaccharides					642:657	The released oligosaccharides	629:657	The released oligosaccharides	629:657	The released oligosaccharides were characterized by using nuclear magnetic resonance spectroscopy and mass spectrometry.
9538010	5	23	with	Galbeta1-->	1054:1064	arg1	determinant					1115:1125	sialyl Lex (sLex) determinant	1097:1125	sialyl Lex (sLex) determinant	1097:1125	Of the 41 different structures we detected, the most prominent included NeuAcalpha2-->3Galbeta1-->3GalNAc-ol (sialyl-T antigen), Galbeta1-->4(Fucalpha1-->3)GlcNAcbeta1-->6(Galbeta1 -->3)GalNAc-ol [type 2 core with Lewisx (Lex) determinant], and NeuAcalpha2-->3Galbeta1-->4(Fucalpha1-->3)GlcNAcbet a1-->6(Galbeta1--> 3) GalNAc-ol [type 2 core with sialyl Lex (sLex) determinant].
9538010	5	24	theme	Fucalpha1-->3	892:904	arg1	Galbeta1					922:929	Galbeta1 -->3	922:934	Galbeta1 -->3	922:934	Of the 41 different structures we detected, the most prominent included NeuAcalpha2-->3Galbeta1-->3GalNAc-ol (sialyl-T antigen), Galbeta1-->4(Fucalpha1-->3)GlcNAcbeta1-->6(Galbeta1 -->3)GalNAc-ol [type 2 core with Lewisx (Lex) determinant], and NeuAcalpha2-->3Galbeta1-->4(Fucalpha1-->3)GlcNAcbet a1-->6(Galbeta1--> 3) GalNAc-ol [type 2 core with sialyl Lex (sLex) determinant].
9538010	5	24	theme	Fucalpha1-->3	892:904	arg1	GlcNAcbeta1-->6					906:920	Galbeta1-->4(Fucalpha1-->3)GlcNAcbeta1-->6	879:920	Galbeta1-->4(Fucalpha1-->3)GlcNAcbeta1-->6(Galbeta1 -->3)GalNAc-ol	879:944	Of the 41 different structures we detected, the most prominent included NeuAcalpha2-->3Galbeta1-->3GalNAc-ol (sialyl-T antigen), Galbeta1-->4(Fucalpha1-->3)GlcNAcbeta1-->6(Galbeta1 -->3)GalNAc-ol [type 2 core with Lewisx (Lex) determinant], and NeuAcalpha2-->3Galbeta1-->4(Fucalpha1-->3)GlcNAcbet a1-->6(Galbeta1--> 3) GalNAc-ol [type 2 core with sialyl Lex (sLex) determinant].
9538010	0	25	theme	Human	0:4	arg1	mucin					36:40	Human low-molecular-weight salivary mucin	0:40	Human low-molecular-weight salivary mucin	0:40	Human low-molecular-weight salivary mucin expresses the sialyl lewisx determinant and has L-selectin ligand activity.
9538010	1	26	theme	bacterial	264:272	arg1	mucin					169:173	the low-molecular-weight mucin	144:173	the low-molecular-weight mucin (MG2, encoded by MUC7)	144:196	Previously we showed that the low-molecular-weight mucin (MG2, encoded by MUC7), a major component of human submandibular/sublingual saliva, is a bacterial receptor that coats the tooth surface.
9538010	1	26	theme	bacterial	264:272	arg1	receptor					274:281	a bacterial receptor	262:281	a bacterial receptor that coats the tooth surface	262:310	Previously we showed that the low-molecular-weight mucin (MG2, encoded by MUC7), a major component of human submandibular/sublingual saliva, is a bacterial receptor that coats the tooth surface.
9538010	5	27	theme	included	813:820	arg1	NeuAcalpha2-->3Galbeta1-->3GalNAc-ol					822:857	the most prominent included NeuAcalpha2-->3Galbeta1-->3GalNAc-ol	794:857	the most prominent included NeuAcalpha2-->3Galbeta1-->3GalNAc-ol (sialyl-T antigen), Galbeta1-->4(Fucalpha1-->3)GlcNAcbeta1-->6(Galbeta1 -->3)GalNAc-ol [type 2 core with Lewisx (Lex) determinant]	794:988	Of the 41 different structures we detected, the most prominent included NeuAcalpha2-->3Galbeta1-->3GalNAc-ol (sialyl-T antigen), Galbeta1-->4(Fucalpha1-->3)GlcNAcbeta1-->6(Galbeta1 -->3)GalNAc-ol [type 2 core with Lewisx (Lex) determinant], and NeuAcalpha2-->3Galbeta1-->4(Fucalpha1-->3)GlcNAcbet a1-->6(Galbeta1--> 3) GalNAc-ol [type 2 core with sialyl Lex (sLex) determinant].
9538010	5	27	theme	included	813:820	arg1	antigen					869:875	sialyl-T antigen	860:875	sialyl-T antigen	860:875	Of the 41 different structures we detected, the most prominent included NeuAcalpha2-->3Galbeta1-->3GalNAc-ol (sialyl-T antigen), Galbeta1-->4(Fucalpha1-->3)GlcNAcbeta1-->6(Galbeta1 -->3)GalNAc-ol [type 2 core with Lewisx (Lex) determinant], and NeuAcalpha2-->3Galbeta1-->4(Fucalpha1-->3)GlcNAcbet a1-->6(Galbeta1--> 3) GalNAc-ol [type 2 core with sialyl Lex (sLex) determinant].
9538010	5	28	theme	NeuAcalpha2-->3Galbeta1-->4	995:1021	arg1	Galbeta1-->					1054:1064	Galbeta1--> 3) GalNAc-ol [type 2 core with sialyl Lex (sLex) determinant	1054:1125	Galbeta1--> 3) GalNAc-ol [type 2 core with sialyl Lex (sLex) determinant	1054:1125	Of the 41 different structures we detected, the most prominent included NeuAcalpha2-->3Galbeta1-->3GalNAc-ol (sialyl-T antigen), Galbeta1-->4(Fucalpha1-->3)GlcNAcbeta1-->6(Galbeta1 -->3)GalNAc-ol [type 2 core with Lewisx (Lex) determinant], and NeuAcalpha2-->3Galbeta1-->4(Fucalpha1-->3)GlcNAcbet a1-->6(Galbeta1--> 3) GalNAc-ol [type 2 core with sialyl Lex (sLex) determinant].
9538010	5	28	theme	NeuAcalpha2-->3Galbeta1-->4	995:1021	arg1	a1-->6					1047:1052	NeuAcalpha2-->3Galbeta1-->4(Fucalpha1-->3)GlcNAcbet a1-->6	995:1052	NeuAcalpha2-->3Galbeta1-->4(Fucalpha1-->3)GlcNAcbet a1-->6(Galbeta1--> 3) GalNAc-ol [type 2 core with sialyl Lex (sLex) determinant]	995:1126	Of the 41 different structures we detected, the most prominent included NeuAcalpha2-->3Galbeta1-->3GalNAc-ol (sialyl-T antigen), Galbeta1-->4(Fucalpha1-->3)GlcNAcbeta1-->6(Galbeta1 -->3)GalNAc-ol [type 2 core with Lewisx (Lex) determinant], and NeuAcalpha2-->3Galbeta1-->4(Fucalpha1-->3)GlcNAcbet a1-->6(Galbeta1--> 3) GalNAc-ol [type 2 core with sialyl Lex (sLex) determinant].
9538010	9	29	theme	enzyme-linked	1395:1407	arg1	assay					1423:1427	an enzyme-linked immunosorbent assay	1392:1427	an enzyme-linked immunosorbent assay	1392:1427	In an enzyme-linked immunosorbent assay, L-selectin chimeras interacted with immobilized MG2 in a Ca2+-dependent manner.
9538010	3	30	theme	000	519:521	arg1	fragment					523:530	the resulting Mr 90 000 fragment	499:530	the resulting Mr 90 000 fragment	499:530	Purified MG2 (Mr 120 000) was digested with trypsin, and the resulting Mr 90 000 fragment, which carried primarily O-linked oligosaccharides, was subjected to reductive beta-elimination.
9538010	5	31	theme	Fucalpha1-->3	1023:1035	arg1	Galbeta1-->					1054:1064	Galbeta1--> 3) GalNAc-ol [type 2 core with sialyl Lex (sLex) determinant	1054:1125	Galbeta1--> 3) GalNAc-ol [type 2 core with sialyl Lex (sLex) determinant	1054:1125	Of the 41 different structures we detected, the most prominent included NeuAcalpha2-->3Galbeta1-->3GalNAc-ol (sialyl-T antigen), Galbeta1-->4(Fucalpha1-->3)GlcNAcbeta1-->6(Galbeta1 -->3)GalNAc-ol [type 2 core with Lewisx (Lex) determinant], and NeuAcalpha2-->3Galbeta1-->4(Fucalpha1-->3)GlcNAcbet a1-->6(Galbeta1--> 3) GalNAc-ol [type 2 core with sialyl Lex (sLex) determinant].
9538010	5	31	theme	Fucalpha1-->3	1023:1035	arg1	a1-->6					1047:1052	NeuAcalpha2-->3Galbeta1-->4(Fucalpha1-->3)GlcNAcbet a1-->6	995:1052	NeuAcalpha2-->3Galbeta1-->4(Fucalpha1-->3)GlcNAcbet a1-->6(Galbeta1--> 3) GalNAc-ol [type 2 core with sialyl Lex (sLex) determinant]	995:1126	Of the 41 different structures we detected, the most prominent included NeuAcalpha2-->3Galbeta1-->3GalNAc-ol (sialyl-T antigen), Galbeta1-->4(Fucalpha1-->3)GlcNAcbeta1-->6(Galbeta1 -->3)GalNAc-ol [type 2 core with Lewisx (Lex) determinant], and NeuAcalpha2-->3Galbeta1-->4(Fucalpha1-->3)GlcNAcbet a1-->6(Galbeta1--> 3) GalNAc-ol [type 2 core with sialyl Lex (sLex) determinant].
9538010	5	32	theme	sialyl-T	860:867	arg1	NeuAcalpha2-->3Galbeta1-->3GalNAc-ol					822:857	the most prominent included NeuAcalpha2-->3Galbeta1-->3GalNAc-ol	794:857	the most prominent included NeuAcalpha2-->3Galbeta1-->3GalNAc-ol (sialyl-T antigen), Galbeta1-->4(Fucalpha1-->3)GlcNAcbeta1-->6(Galbeta1 -->3)GalNAc-ol [type 2 core with Lewisx (Lex) determinant]	794:988	Of the 41 different structures we detected, the most prominent included NeuAcalpha2-->3Galbeta1-->3GalNAc-ol (sialyl-T antigen), Galbeta1-->4(Fucalpha1-->3)GlcNAcbeta1-->6(Galbeta1 -->3)GalNAc-ol [type 2 core with Lewisx (Lex) determinant], and NeuAcalpha2-->3Galbeta1-->4(Fucalpha1-->3)GlcNAcbet a1-->6(Galbeta1--> 3) GalNAc-ol [type 2 core with sialyl Lex (sLex) determinant].
9538010	5	32	theme	sialyl-T	860:867	arg1	antigen					869:875	sialyl-T antigen	860:875	sialyl-T antigen	860:875	Of the 41 different structures we detected, the most prominent included NeuAcalpha2-->3Galbeta1-->3GalNAc-ol (sialyl-T antigen), Galbeta1-->4(Fucalpha1-->3)GlcNAcbeta1-->6(Galbeta1 -->3)GalNAc-ol [type 2 core with Lewisx (Lex) determinant], and NeuAcalpha2-->3Galbeta1-->4(Fucalpha1-->3)GlcNAcbet a1-->6(Galbeta1--> 3) GalNAc-ol [type 2 core with sialyl Lex (sLex) determinant].
9538010	0	33	theme	salivary	27:34	arg1	mucin					36:40	Human low-molecular-weight salivary mucin	0:40	Human low-molecular-weight salivary mucin	0:40	Human low-molecular-weight salivary mucin expresses the sialyl lewisx determinant and has L-selectin ligand activity.
9538010	5	34	theme	GalNAc-ol	1069:1077	arg1	core					1087:1090	GalNAc-ol [type 2 core	1069:1090	Galbeta1--> 3) GalNAc-ol [type 2 core with sialyl Lex (sLex) determinant	1054:1125	Of the 41 different structures we detected, the most prominent included NeuAcalpha2-->3Galbeta1-->3GalNAc-ol (sialyl-T antigen), Galbeta1-->4(Fucalpha1-->3)GlcNAcbeta1-->6(Galbeta1 -->3)GalNAc-ol [type 2 core with Lewisx (Lex) determinant], and NeuAcalpha2-->3Galbeta1-->4(Fucalpha1-->3)GlcNAcbet a1-->6(Galbeta1--> 3) GalNAc-ol [type 2 core with sialyl Lex (sLex) determinant].
9538010	1	35	dep	mucin	169:173	arg1	MG2					176:178	MG2	176:178	MG2	176:178	Previously we showed that the low-molecular-weight mucin (MG2, encoded by MUC7), a major component of human submandibular/sublingual saliva, is a bacterial receptor that coats the tooth surface.
9538010	11	36	contain	carries	1641:1647	arg1	MG2					1637:1639	MG2	1637:1639	MG2	1637:1639	Together, these results suggest that the saccharides that MG2 carries could specify some of its important functions, which may include mediating leukocyte interactions in the oral cavity.
9538010	11	36	contain	carries	1641:1647	arg2	saccharides					1620:1630	the saccharides	1616:1630	the saccharides that MG2 carries	1616:1647	Together, these results suggest that the saccharides that MG2 carries could specify some of its important functions, which may include mediating leukocyte interactions in the oral cavity.
9538010	5	37	theme	GlcNAcbeta1-->6	906:920	arg1	GalNAc-ol					936:944	Galbeta1-->4(Fucalpha1-->3)GlcNAcbeta1-->6(Galbeta1 -->3)GalNAc-ol	879:944	Galbeta1-->4(Fucalpha1-->3)GlcNAcbeta1-->6(Galbeta1 -->3)GalNAc-ol	879:944	Of the 41 different structures we detected, the most prominent included NeuAcalpha2-->3Galbeta1-->3GalNAc-ol (sialyl-T antigen), Galbeta1-->4(Fucalpha1-->3)GlcNAcbeta1-->6(Galbeta1 -->3)GalNAc-ol [type 2 core with Lewisx (Lex) determinant], and NeuAcalpha2-->3Galbeta1-->4(Fucalpha1-->3)GlcNAcbet a1-->6(Galbeta1--> 3) GalNAc-ol [type 2 core with sialyl Lex (sLex) determinant].
9538010	5	38	theme	[type	1079:1083	arg1	core					1087:1090	GalNAc-ol [type 2 core	1069:1090	Galbeta1--> 3) GalNAc-ol [type 2 core with sialyl Lex (sLex) determinant	1054:1125	Of the 41 different structures we detected, the most prominent included NeuAcalpha2-->3Galbeta1-->3GalNAc-ol (sialyl-T antigen), Galbeta1-->4(Fucalpha1-->3)GlcNAcbeta1-->6(Galbeta1 -->3)GalNAc-ol [type 2 core with Lewisx (Lex) determinant], and NeuAcalpha2-->3Galbeta1-->4(Fucalpha1-->3)GlcNAcbet a1-->6(Galbeta1--> 3) GalNAc-ol [type 2 core with sialyl Lex (sLex) determinant].
9538010	3	39	theme	O-linked	557:564	arg1	oligosaccharides					566:581	primarily O-linked oligosaccharides	547:581	primarily O-linked oligosaccharides	547:581	Purified MG2 (Mr 120 000) was digested with trypsin, and the resulting Mr 90 000 fragment, which carried primarily O-linked oligosaccharides, was subjected to reductive beta-elimination.
9538010	2	40	theme	important	400:408	arg1	information					410:420	important information	400:420	important information about its function	400:439	Here we tested the hypothesis that the structure of its carbohydrate residues contains important information about its function.
9538010	5	41	theme	Galbeta1-->4	879:890	arg1	Galbeta1					922:929	Galbeta1 -->3	922:934	Galbeta1 -->3	922:934	Of the 41 different structures we detected, the most prominent included NeuAcalpha2-->3Galbeta1-->3GalNAc-ol (sialyl-T antigen), Galbeta1-->4(Fucalpha1-->3)GlcNAcbeta1-->6(Galbeta1 -->3)GalNAc-ol [type 2 core with Lewisx (Lex) determinant], and NeuAcalpha2-->3Galbeta1-->4(Fucalpha1-->3)GlcNAcbet a1-->6(Galbeta1--> 3) GalNAc-ol [type 2 core with sialyl Lex (sLex) determinant].
9538010	5	41	theme	Galbeta1-->4	879:890	arg1	GlcNAcbeta1-->6					906:920	Galbeta1-->4(Fucalpha1-->3)GlcNAcbeta1-->6	879:920	Galbeta1-->4(Fucalpha1-->3)GlcNAcbeta1-->6(Galbeta1 -->3)GalNAc-ol	879:944	Of the 41 different structures we detected, the most prominent included NeuAcalpha2-->3Galbeta1-->3GalNAc-ol (sialyl-T antigen), Galbeta1-->4(Fucalpha1-->3)GlcNAcbeta1-->6(Galbeta1 -->3)GalNAc-ol [type 2 core with Lewisx (Lex) determinant], and NeuAcalpha2-->3Galbeta1-->4(Fucalpha1-->3)GlcNAcbet a1-->6(Galbeta1--> 3) GalNAc-ol [type 2 core with sialyl Lex (sLex) determinant].
9538010	3	42	theme	reductive	601:609	arg1	beta-elimination					611:626	reductive beta-elimination	601:626	reductive beta-elimination	601:626	Purified MG2 (Mr 120 000) was digested with trypsin, and the resulting Mr 90 000 fragment, which carried primarily O-linked oligosaccharides, was subjected to reductive beta-elimination.
9538010	11	43	theme	leukocyte	1724:1732	arg1	interactions					1734:1745	leukocyte interactions	1724:1745	leukocyte interactions	1724:1745	Together, these results suggest that the saccharides that MG2 carries could specify some of its important functions, which may include mediating leukocyte interactions in the oral cavity.
9538010	1	44	theme	major	201:205	arg1	mucin					169:173	the low-molecular-weight mucin	144:173	the low-molecular-weight mucin (MG2, encoded by MUC7)	144:196	Previously we showed that the low-molecular-weight mucin (MG2, encoded by MUC7), a major component of human submandibular/sublingual saliva, is a bacterial receptor that coats the tooth surface.
9538010	1	44	theme	major	201:205	arg1	component					207:215	a major component	199:215	a major component of human submandibular/sublingual saliva	199:256	Previously we showed that the low-molecular-weight mucin (MG2, encoded by MUC7), a major component of human submandibular/sublingual saliva, is a bacterial receptor that coats the tooth surface.
9538010	0	45	theme	lewisx	63:68	arg1	determinant					70:80	the sialyl lewisx determinant	52:80	the sialyl lewisx determinant	52:80	Human low-molecular-weight salivary mucin expresses the sialyl lewisx determinant and has L-selectin ligand activity.
9538010	1	46	theme	tooth	298:302	arg1	surface					304:310	the tooth surface	294:310	the tooth surface	294:310	Previously we showed that the low-molecular-weight mucin (MG2, encoded by MUC7), a major component of human submandibular/sublingual saliva, is a bacterial receptor that coats the tooth surface.
9538010	7	47	theme	leukocyte	1304:1312	arg1	trafficking					1314:1324	leukocyte trafficking	1304:1324	leukocyte trafficking	1304:1324	Lex, sLex, and related sulfated structures are ligands for selectins, adhesion molecules that mediate leukocyte trafficking.
9538010	5	48	theme	different	760:768	arg1	structures					770:779	the 41 different structures	753:779	the 41 different structures	753:779	Of the 41 different structures we detected, the most prominent included NeuAcalpha2-->3Galbeta1-->3GalNAc-ol (sialyl-T antigen), Galbeta1-->4(Fucalpha1-->3)GlcNAcbeta1-->6(Galbeta1 -->3)GalNAc-ol [type 2 core with Lewisx (Lex) determinant], and NeuAcalpha2-->3Galbeta1-->4(Fucalpha1-->3)GlcNAcbet a1-->6(Galbeta1--> 3) GalNAc-ol [type 2 core with sialyl Lex (sLex) determinant].
9538010	5	49	theme	GlcNAcbet	1037:1045	arg1	Galbeta1-->					1054:1064	Galbeta1--> 3) GalNAc-ol [type 2 core with sialyl Lex (sLex) determinant	1054:1125	Galbeta1--> 3) GalNAc-ol [type 2 core with sialyl Lex (sLex) determinant	1054:1125	Of the 41 different structures we detected, the most prominent included NeuAcalpha2-->3Galbeta1-->3GalNAc-ol (sialyl-T antigen), Galbeta1-->4(Fucalpha1-->3)GlcNAcbeta1-->6(Galbeta1 -->3)GalNAc-ol [type 2 core with Lewisx (Lex) determinant], and NeuAcalpha2-->3Galbeta1-->4(Fucalpha1-->3)GlcNAcbet a1-->6(Galbeta1--> 3) GalNAc-ol [type 2 core with sialyl Lex (sLex) determinant].
9538010	5	49	theme	GlcNAcbet	1037:1045	arg1	a1-->6					1047:1052	NeuAcalpha2-->3Galbeta1-->4(Fucalpha1-->3)GlcNAcbet a1-->6	995:1052	NeuAcalpha2-->3Galbeta1-->4(Fucalpha1-->3)GlcNAcbet a1-->6(Galbeta1--> 3) GalNAc-ol [type 2 core with sialyl Lex (sLex) determinant]	995:1126	Of the 41 different structures we detected, the most prominent included NeuAcalpha2-->3Galbeta1-->3GalNAc-ol (sialyl-T antigen), Galbeta1-->4(Fucalpha1-->3)GlcNAcbeta1-->6(Galbeta1 -->3)GalNAc-ol [type 2 core with Lewisx (Lex) determinant], and NeuAcalpha2-->3Galbeta1-->4(Fucalpha1-->3)GlcNAcbet a1-->6(Galbeta1--> 3) GalNAc-ol [type 2 core with sialyl Lex (sLex) determinant].
9538010	9	50	theme	immobilized	1466:1476	arg1	MG2					1478:1480	immobilized MG2	1466:1480	immobilized MG2	1466:1480	In an enzyme-linked immunosorbent assay, L-selectin chimeras interacted with immobilized MG2 in a Ca2+-dependent manner.
9538010	0	51	theme	sialyl	56:61	arg1	determinant					70:80	the sialyl lewisx determinant	52:80	the sialyl lewisx determinant	52:80	Human low-molecular-weight salivary mucin expresses the sialyl lewisx determinant and has L-selectin ligand activity.
9538010	2	52	contain	contains	391:398	arg2	information					410:420	important information	400:420	important information about its function	400:439	Here we tested the hypothesis that the structure of its carbohydrate residues contains important information about its function.
9538010	2	52	contain	contains	391:398	arg1	structure					352:360	the structure	348:360	the structure of its carbohydrate residues	348:389	Here we tested the hypothesis that the structure of its carbohydrate residues contains important information about its function.
9538010	6	53	theme	sulfate	1187:1193	arg1	group					1195:1199	one sulfate group	1183:1199	one sulfate group	1183:1199	We also detected di-, tri-, and pentasaccharides with one sulfate group.
9538010	4	54	theme	resonance	704:712	arg1	spectroscopy					714:725	nuclear magnetic resonance spectroscopy	687:725	nuclear magnetic resonance spectroscopy	687:725	The released oligosaccharides were characterized by using nuclear magnetic resonance spectroscopy and mass spectrometry.
9538010	3	55	dep	MG2	451:453	arg1	Mr					456:457	Mr	456:457	Mr 120 000	456:465	Purified MG2 (Mr 120 000) was digested with trypsin, and the resulting Mr 90 000 fragment, which carried primarily O-linked oligosaccharides, was subjected to reductive beta-elimination.
9538010	4	56	theme	mass	731:734	arg1	spectrometry					736:747	mass spectrometry	731:747	mass spectrometry	731:747	The released oligosaccharides were characterized by using nuclear magnetic resonance spectroscopy and mass spectrometry.
9538010	5	57	theme	Lewisx	964:969	arg1	determinant					977:987	Lewisx (Lex) determinant	964:987	Lewisx (Lex) determinant	964:987	Of the 41 different structures we detected, the most prominent included NeuAcalpha2-->3Galbeta1-->3GalNAc-ol (sialyl-T antigen), Galbeta1-->4(Fucalpha1-->3)GlcNAcbeta1-->6(Galbeta1 -->3)GalNAc-ol [type 2 core with Lewisx (Lex) determinant], and NeuAcalpha2-->3Galbeta1-->4(Fucalpha1-->3)GlcNAcbet a1-->6(Galbeta1--> 3) GalNAc-ol [type 2 core with sialyl Lex (sLex) determinant].
9538010	9	58	theme	immunosorbent	1409:1421	arg1	assay					1423:1427	an enzyme-linked immunosorbent assay	1392:1427	an enzyme-linked immunosorbent assay	1392:1427	In an enzyme-linked immunosorbent assay, L-selectin chimeras interacted with immobilized MG2 in a Ca2+-dependent manner.
9538010	5	59	theme	Lex	972:974	arg1	determinant					977:987	Lewisx (Lex) determinant	964:987	Lewisx (Lex) determinant	964:987	Of the 41 different structures we detected, the most prominent included NeuAcalpha2-->3Galbeta1-->3GalNAc-ol (sialyl-T antigen), Galbeta1-->4(Fucalpha1-->3)GlcNAcbeta1-->6(Galbeta1 -->3)GalNAc-ol [type 2 core with Lewisx (Lex) determinant], and NeuAcalpha2-->3Galbeta1-->4(Fucalpha1-->3)GlcNAcbet a1-->6(Galbeta1--> 3) GalNAc-ol [type 2 core with sialyl Lex (sLex) determinant].
9538010	0	60	contain	has	86:88	arg2	activity					108:115	L-selectin ligand activity	90:115	L-selectin ligand activity	90:115	Human low-molecular-weight salivary mucin expresses the sialyl lewisx determinant and has L-selectin ligand activity.
9538010	0	60	contain	has	86:88	arg1	mucin					36:40	Human low-molecular-weight salivary mucin	0:40	Human low-molecular-weight salivary mucin	0:40	Human low-molecular-weight salivary mucin expresses the sialyl lewisx determinant and has L-selectin ligand activity.
9538010	7	61	theme	sulfated	1225:1232	arg1	ligands					1249:1255	ligands	1249:1255	ligands for selectins	1249:1269	Lex, sLex, and related sulfated structures are ligands for selectins, adhesion molecules that mediate leukocyte trafficking.
9538010	7	61	theme	sulfated	1225:1232	arg1	structures					1234:1243	related sulfated structures	1217:1243	related sulfated structures	1217:1243	Lex, sLex, and related sulfated structures are ligands for selectins, adhesion molecules that mediate leukocyte trafficking.
9538010	7	61	theme	sulfated	1225:1232	arg1	sLex					1207:1210	sLex	1207:1210	sLex	1207:1210	Lex, sLex, and related sulfated structures are ligands for selectins, adhesion molecules that mediate leukocyte trafficking.
9538010	7	61	theme	sulfated	1225:1232	arg1	Lex					1202:1204	Lex	1202:1204	Lex	1202:1204	Lex, sLex, and related sulfated structures are ligands for selectins, adhesion molecules that mediate leukocyte trafficking.
9538010	7	62	theme	related	1217:1223	arg1	ligands					1249:1255	ligands	1249:1255	ligands for selectins	1249:1269	Lex, sLex, and related sulfated structures are ligands for selectins, adhesion molecules that mediate leukocyte trafficking.
9538010	7	62	theme	related	1217:1223	arg1	structures					1234:1243	related sulfated structures	1217:1243	related sulfated structures	1217:1243	Lex, sLex, and related sulfated structures are ligands for selectins, adhesion molecules that mediate leukocyte trafficking.
9538010	7	62	theme	related	1217:1223	arg1	sLex					1207:1210	sLex	1207:1210	sLex	1207:1210	Lex, sLex, and related sulfated structures are ligands for selectins, adhesion molecules that mediate leukocyte trafficking.
9538010	7	62	theme	related	1217:1223	arg1	Lex					1202:1204	Lex	1202:1204	Lex	1202:1204	Lex, sLex, and related sulfated structures are ligands for selectins, adhesion molecules that mediate leukocyte trafficking.
9538010	3	63	dep	Mr	456:457	arg1	000					463:465	120 000	459:465	Mr 120 000	456:465	Purified MG2 (Mr 120 000) was digested with trypsin, and the resulting Mr 90 000 fragment, which carried primarily O-linked oligosaccharides, was subjected to reductive beta-elimination.
9538010	9	64	theme	L-selectin	1430:1439	arg1	chimeras					1441:1448	L-selectin chimeras	1430:1448	L-selectin chimeras	1430:1448	In an enzyme-linked immunosorbent assay, L-selectin chimeras interacted with immobilized MG2 in a Ca2+-dependent manner.
9538010	1	65	theme	low-molecular-weight	148:167	arg1	mucin					169:173	the low-molecular-weight mucin	144:173	the low-molecular-weight mucin (MG2, encoded by MUC7)	144:196	Previously we showed that the low-molecular-weight mucin (MG2, encoded by MUC7), a major component of human submandibular/sublingual saliva, is a bacterial receptor that coats the tooth surface.
9538010	1	65	theme	low-molecular-weight	148:167	arg1	component					207:215	a major component	199:215	a major component of human submandibular/sublingual saliva	199:256	Previously we showed that the low-molecular-weight mucin (MG2, encoded by MUC7), a major component of human submandibular/sublingual saliva, is a bacterial receptor that coats the tooth surface.
9538010	1	65	theme	low-molecular-weight	148:167	arg1	receptor					274:281	a bacterial receptor	262:281	a bacterial receptor that coats the tooth surface	262:310	Previously we showed that the low-molecular-weight mucin (MG2, encoded by MUC7), a major component of human submandibular/sublingual saliva, is a bacterial receptor that coats the tooth surface.
9538010	3	66	theme	Purified	442:449	arg1	MG2					451:453	Purified MG2	442:453	Purified MG2 (Mr 120 000)	442:466	Purified MG2 (Mr 120 000) was digested with trypsin, and the resulting Mr 90 000 fragment, which carried primarily O-linked oligosaccharides, was subjected to reductive beta-elimination.
9538010	1	67	theme	human	220:224	arg1	saliva					251:256	human submandibular/sublingual saliva	220:256	human submandibular/sublingual saliva	220:256	Previously we showed that the low-molecular-weight mucin (MG2, encoded by MUC7), a major component of human submandibular/sublingual saliva, is a bacterial receptor that coats the tooth surface.
9538010	3	68	link	O-linked	557:564	arg1	oligosaccharides					566:581	primarily O-linked oligosaccharides	547:581	primarily O-linked oligosaccharides	547:581	Purified MG2 (Mr 120 000) was digested with trypsin, and the resulting Mr 90 000 fragment, which carried primarily O-linked oligosaccharides, was subjected to reductive beta-elimination.
9538010	5	69	theme	sLex	1109:1112	arg1	determinant					1115:1125	sialyl Lex (sLex) determinant	1097:1125	sialyl Lex (sLex) determinant	1097:1125	Of the 41 different structures we detected, the most prominent included NeuAcalpha2-->3Galbeta1-->3GalNAc-ol (sialyl-T antigen), Galbeta1-->4(Fucalpha1-->3)GlcNAcbeta1-->6(Galbeta1 -->3)GalNAc-ol [type 2 core with Lewisx (Lex) determinant], and NeuAcalpha2-->3Galbeta1-->4(Fucalpha1-->3)GlcNAcbet a1-->6(Galbeta1--> 3) GalNAc-ol [type 2 core with sialyl Lex (sLex) determinant].
9538010	5	70	theme	prominent	803:811	arg1	NeuAcalpha2-->3Galbeta1-->3GalNAc-ol					822:857	the most prominent included NeuAcalpha2-->3Galbeta1-->3GalNAc-ol	794:857	the most prominent included NeuAcalpha2-->3Galbeta1-->3GalNAc-ol (sialyl-T antigen), Galbeta1-->4(Fucalpha1-->3)GlcNAcbeta1-->6(Galbeta1 -->3)GalNAc-ol [type 2 core with Lewisx (Lex) determinant]	794:988	Of the 41 different structures we detected, the most prominent included NeuAcalpha2-->3Galbeta1-->3GalNAc-ol (sialyl-T antigen), Galbeta1-->4(Fucalpha1-->3)GlcNAcbeta1-->6(Galbeta1 -->3)GalNAc-ol [type 2 core with Lewisx (Lex) determinant], and NeuAcalpha2-->3Galbeta1-->4(Fucalpha1-->3)GlcNAcbet a1-->6(Galbeta1--> 3) GalNAc-ol [type 2 core with sialyl Lex (sLex) determinant].
9538010	5	70	theme	prominent	803:811	arg1	antigen					869:875	sialyl-T antigen	860:875	sialyl-T antigen	860:875	Of the 41 different structures we detected, the most prominent included NeuAcalpha2-->3Galbeta1-->3GalNAc-ol (sialyl-T antigen), Galbeta1-->4(Fucalpha1-->3)GlcNAcbeta1-->6(Galbeta1 -->3)GalNAc-ol [type 2 core with Lewisx (Lex) determinant], and NeuAcalpha2-->3Galbeta1-->4(Fucalpha1-->3)GlcNAcbet a1-->6(Galbeta1--> 3) GalNAc-ol [type 2 core with sialyl Lex (sLex) determinant].
9538010	11	71	theme	important	1675:1683	arg1	functions					1685:1693	its important functions	1671:1693	its important functions	1671:1693	Together, these results suggest that the saccharides that MG2 carries could specify some of its important functions, which may include mediating leukocyte interactions in the oral cavity.
9538010	1	72	theme	submandibular/sublingual	226:249	arg1	saliva					251:256	human submandibular/sublingual saliva	220:256	human submandibular/sublingual saliva	220:256	Previously we showed that the low-molecular-weight mucin (MG2, encoded by MUC7), a major component of human submandibular/sublingual saliva, is a bacterial receptor that coats the tooth surface.
208636	0	0	theme	plasma	86:91	arg1	lipoproteins					110:121	human plasma very low density lipoproteins	80:121	human plasma very low density lipoproteins	80:121	Characterization of the oligosaccharide side chain of apolipoprotein C-III from human plasma very low density lipoproteins.
208636	5	1	theme	apolipoprotein	994:1007	arg1	C-III1					1009:1014	apolipoprotein C-III1	994:1014	apolipoprotein C-III1	994:1014	Further studies employing periodate oxidation and Smith degradation indicated that the structure of the trisaccharide from apolipoprotein C-III1 was alpha-N-acetylneuraminyl-(2 leads to 3)-beta-D-galactosyl-(1 leads to 3)-N-acetyl-D-galactosaminitol.
208636	6	2	theme	sialic	1221:1226	arg1	residue					1233:1239	one sialic acid residue	1217:1239	one sialic acid residue	1217:1239	The tetrasaccharide structure from apolipoprotein C-III2 is made up of this trisaccharide plus one sialic acid residue linked to C6 of N-acetyl-D-galactosaminitol, as was shown by the assessment of chromogens formed upon alkaline degradation.
208636	0	3	theme	human	80:84	arg1	lipoproteins					110:121	human plasma very low density lipoproteins	80:121	human plasma very low density lipoproteins	80:121	Characterization of the oligosaccharide side chain of apolipoprotein C-III from human plasma very low density lipoproteins.
208636	4	4	theme	apolipoproteins	684:698	arg1	Treatment					658:666	Treatment	658:666	Treatment of desialylated apolipoproteins with alkaline borohydride	658:724	Treatment of desialylated apolipoproteins with alkaline borohydride released the reduced disaccharide beta-D-galactosyl-(1 leads to 3)-N-acetyl-D-galactosaminitol, which was detected by gas-liquid chromatography.
208636	0	5	theme	low	98:100	arg1	lipoproteins					110:121	human plasma very low density lipoproteins	80:121	human plasma very low density lipoproteins	80:121	Characterization of the oligosaccharide side chain of apolipoprotein C-III from human plasma very low density lipoproteins.
208636	4	6	with	Treatment	658:666	arg1	borohydride					714:724	alkaline borohydride	705:724	alkaline borohydride	705:724	Treatment of desialylated apolipoproteins with alkaline borohydride released the reduced disaccharide beta-D-galactosyl-(1 leads to 3)-N-acetyl-D-galactosaminitol, which was detected by gas-liquid chromatography.
208636	4	7	theme	gas-liquid	844:853	arg1	chromatography					855:868	gas-liquid chromatography	844:868	gas-liquid chromatography	844:868	Treatment of desialylated apolipoproteins with alkaline borohydride released the reduced disaccharide beta-D-galactosyl-(1 leads to 3)-N-acetyl-D-galactosaminitol, which was detected by gas-liquid chromatography.
208636	6	8	theme	N-acetyl-D-galactosaminitol	1257:1283	arg1	C6					1251:1252	C6	1251:1252	C6 of N-acetyl-D-galactosaminitol	1251:1283	The tetrasaccharide structure from apolipoprotein C-III2 is made up of this trisaccharide plus one sialic acid residue linked to C6 of N-acetyl-D-galactosaminitol, as was shown by the assessment of chromogens formed upon alkaline degradation.
208636	1	9	theme	amino	275:279	arg1	sequence					286:293	the amino acid sequence	271:293	the amino acid sequence	271:293	Apolipoprotein C-III1 and apolipoprotein C-III2 each contain one oligosaccharide side chain, bound O-glycosidically to threonine in position 74 of the amino acid sequence.
208636	1	10	contain	contain	177:183	arg1	C-III1					139:144	Apolipoprotein C-III1	124:144	Apolipoprotein C-III1	124:144	Apolipoprotein C-III1 and apolipoprotein C-III2 each contain one oligosaccharide side chain, bound O-glycosidically to threonine in position 74 of the amino acid sequence.
208636	1	10	contain	contain	177:183	arg1	C-III2					165:170	apolipoprotein C-III2	150:170	apolipoprotein C-III2	150:170	Apolipoprotein C-III1 and apolipoprotein C-III2 each contain one oligosaccharide side chain, bound O-glycosidically to threonine in position 74 of the amino acid sequence.
208636	1	10	contain	contain	177:183	arg2	chain					210:214	one oligosaccharide side chain	185:214	one oligosaccharide side chain	185:214	Apolipoprotein C-III1 and apolipoprotein C-III2 each contain one oligosaccharide side chain, bound O-glycosidically to threonine in position 74 of the amino acid sequence.
208636	1	11	theme	acid	281:284	arg1	sequence					286:293	the amino acid sequence	271:293	the amino acid sequence	271:293	Apolipoprotein C-III1 and apolipoprotein C-III2 each contain one oligosaccharide side chain, bound O-glycosidically to threonine in position 74 of the amino acid sequence.
208636	4	12	gly	desialylated	671:682	arg1	apolipoproteins					684:698	desialylated apolipoproteins	671:698	desialylated apolipoproteins	671:698	Treatment of desialylated apolipoproteins with alkaline borohydride released the reduced disaccharide beta-D-galactosyl-(1 leads to 3)-N-acetyl-D-galactosaminitol, which was detected by gas-liquid chromatography.
208636	6	13	theme	apolipoprotein	1157:1170	arg1	C-III2					1172:1177	apolipoprotein C-III2	1157:1177	apolipoprotein C-III2	1157:1177	The tetrasaccharide structure from apolipoprotein C-III2 is made up of this trisaccharide plus one sialic acid residue linked to C6 of N-acetyl-D-galactosaminitol, as was shown by the assessment of chromogens formed upon alkaline degradation.
208636	2	14	theme	complete	408:415	arg1	structure					417:425	the complete structure	404:425	the complete structure of apolipoprotein C-III	404:449	The studies reported in this paper characterize these alkali labile oligosaccharides, thereby demonstrating the complete structure of apolipoprotein C-III.
208636	0	15	theme	density	102:108	arg1	lipoproteins					110:121	human plasma very low density lipoproteins	80:121	human plasma very low density lipoproteins	80:121	Characterization of the oligosaccharide side chain of apolipoprotein C-III from human plasma very low density lipoproteins.
208636	0	16	from	chain	45:49	arg1	lipoproteins					110:121	human plasma very low density lipoproteins	80:121	human plasma very low density lipoproteins	80:121	Characterization of the oligosaccharide side chain of apolipoprotein C-III from human plasma very low density lipoproteins.
208636	5	17	theme	Further	871:877	arg1	studies					879:885	Further studies	871:885	Further studies employing periodate oxidation and Smith degradation	871:937	Further studies employing periodate oxidation and Smith degradation indicated that the structure of the trisaccharide from apolipoprotein C-III1 was alpha-N-acetylneuraminyl-(2 leads to 3)-beta-D-galactosyl-(1 leads to 3)-N-acetyl-D-galactosaminitol.
208636	5	18	dep	-beta-D-galactosyl-	1059:1077	arg1	leads					1081:1085	leads	1081:1085	leads to 3)-N-acetyl-D-galactosaminitol	1081:1119	Further studies employing periodate oxidation and Smith degradation indicated that the structure of the trisaccharide from apolipoprotein C-III1 was alpha-N-acetylneuraminyl-(2 leads to 3)-beta-D-galactosyl-(1 leads to 3)-N-acetyl-D-galactosaminitol.
208636	5	18	dep	-beta-D-galactosyl-	1059:1077	arg1	3					1057:1057	3	1057:1057	3	1057:1057	Further studies employing periodate oxidation and Smith degradation indicated that the structure of the trisaccharide from apolipoprotein C-III1 was alpha-N-acetylneuraminyl-(2 leads to 3)-beta-D-galactosyl-(1 leads to 3)-N-acetyl-D-galactosaminitol.
208636	3	19	dep	1	571:571	arg1	1					575:575	1	575:575	1	575:575	Monosaccharide analysis revealed the following sugar composition: D-galactose/N-acetyl-D-galactosamine/sialic acid 1 : 1 : 1 and 1 : 1 : 2 for apolipoprotein C-III1 and apolipoprotein C-III2, respectively.
208636	3	19	dep	1	571:571	arg1	2					589:589	2	589:589	2	589:589	Monosaccharide analysis revealed the following sugar composition: D-galactose/N-acetyl-D-galactosamine/sialic acid 1 : 1 : 1 and 1 : 1 : 2 for apolipoprotein C-III1 and apolipoprotein C-III2, respectively.
208636	3	19	dep	1	571:571	arg1	1					585:585	1	585:585	1	585:585	Monosaccharide analysis revealed the following sugar composition: D-galactose/N-acetyl-D-galactosamine/sialic acid 1 : 1 : 1 and 1 : 1 : 2 for apolipoprotein C-III1 and apolipoprotein C-III2, respectively.
208636	3	19	dep	1	571:571	arg1	1					581:581	1	581:581	1	581:581	Monosaccharide analysis revealed the following sugar composition: D-galactose/N-acetyl-D-galactosamine/sialic acid 1 : 1 : 1 and 1 : 1 : 2 for apolipoprotein C-III1 and apolipoprotein C-III2, respectively.
208636	1	20	theme	oligosaccharide	189:203	arg1	chain					210:214	one oligosaccharide side chain	185:214	one oligosaccharide side chain	185:214	Apolipoprotein C-III1 and apolipoprotein C-III2 each contain one oligosaccharide side chain, bound O-glycosidically to threonine in position 74 of the amino acid sequence.
208636	6	21	from	C-III2	1172:1177	arg1	structure					1142:1150	The tetrasaccharide structure	1122:1150	The tetrasaccharide structure from apolipoprotein C-III2	1122:1177	The tetrasaccharide structure from apolipoprotein C-III2 is made up of this trisaccharide plus one sialic acid residue linked to C6 of N-acetyl-D-galactosaminitol, as was shown by the assessment of chromogens formed upon alkaline degradation.
208636	4	22	dep	-N-acetyl-D-galactosaminitol	792:819	arg1	3					790:790	3	790:790	3	790:790	Treatment of desialylated apolipoproteins with alkaline borohydride released the reduced disaccharide beta-D-galactosyl-(1 leads to 3)-N-acetyl-D-galactosaminitol, which was detected by gas-liquid chromatography.
208636	1	23	theme	side	205:208	arg1	chain					210:214	one oligosaccharide side chain	185:214	one oligosaccharide side chain	185:214	Apolipoprotein C-III1 and apolipoprotein C-III2 each contain one oligosaccharide side chain, bound O-glycosidically to threonine in position 74 of the amino acid sequence.
208636	1	24	theme	sequence	286:293	arg1	position					256:263	position 74	256:266	position 74 of the amino acid sequence	256:293	Apolipoprotein C-III1 and apolipoprotein C-III2 each contain one oligosaccharide side chain, bound O-glycosidically to threonine in position 74 of the amino acid sequence.
208636	1	25	dep	contain	177:183	arg1	each					172:175	each	172:175	each	172:175	Apolipoprotein C-III1 and apolipoprotein C-III2 each contain one oligosaccharide side chain, bound O-glycosidically to threonine in position 74 of the amino acid sequence.
208636	4	26	theme	reduced	739:745	arg1	beta-D-galactosyl-					760:777	the reduced disaccharide beta-D-galactosyl-	735:777	the reduced disaccharide beta-D-galactosyl-	735:777	Treatment of desialylated apolipoproteins with alkaline borohydride released the reduced disaccharide beta-D-galactosyl-(1 leads to 3)-N-acetyl-D-galactosaminitol, which was detected by gas-liquid chromatography.
208636	0	27	theme	oligosaccharide	24:38	arg1	chain					45:49	the oligosaccharide side chain	20:49	the oligosaccharide side chain of apolipoprotein C-III from human plasma very low density lipoproteins	20:121	Characterization of the oligosaccharide side chain of apolipoprotein C-III from human plasma very low density lipoproteins.
208636	5	28	dep	alpha-N-acetylneuraminyl-	1020:1044	arg1	2					1046:1046	2	1046:1046	2	1046:1046	Further studies employing periodate oxidation and Smith degradation indicated that the structure of the trisaccharide from apolipoprotein C-III1 was alpha-N-acetylneuraminyl-(2 leads to 3)-beta-D-galactosyl-(1 leads to 3)-N-acetyl-D-galactosaminitol.
208636	3	29	theme	apolipoprotein	595:608	arg1	C-III1					610:615	apolipoprotein C-III1	595:615	apolipoprotein C-III1	595:615	Monosaccharide analysis revealed the following sugar composition: D-galactose/N-acetyl-D-galactosamine/sialic acid 1 : 1 : 1 and 1 : 1 : 2 for apolipoprotein C-III1 and apolipoprotein C-III2, respectively.
208636	3	30	theme	D-galactose/N-acetyl-D-galactosamine/sialic	518:560	arg1	acid					562:565	D-galactose/N-acetyl-D-galactosamine/sialic acid 1	518:567	the following sugar composition: D-galactose/N-acetyl-D-galactosamine/sialic acid 1 : 1 : 1 and 1 : 1 : 2 for apolipoprotein C-III1 and apolipoprotein C-III2	485:641	Monosaccharide analysis revealed the following sugar composition: D-galactose/N-acetyl-D-galactosamine/sialic acid 1 : 1 : 1 and 1 : 1 : 2 for apolipoprotein C-III1 and apolipoprotein C-III2, respectively.
208636	0	31	theme	chain	45:49	arg1	Characterization					0:15	Characterization	0:15	Characterization of the oligosaccharide side chain of apolipoprotein C-III from human plasma very low density lipoproteins.	0:122	Characterization of the oligosaccharide side chain of apolipoprotein C-III from human plasma very low density lipoproteins.
208636	2	32	theme	alkali	350:355	arg1	oligosaccharides					364:379	these alkali labile oligosaccharides	344:379	these alkali labile oligosaccharides	344:379	The studies reported in this paper characterize these alkali labile oligosaccharides, thereby demonstrating the complete structure of apolipoprotein C-III.
208636	3	33	theme	sugar	499:503	arg1	composition					505:515	the following sugar composition	485:515	the following sugar composition: D-galactose/N-acetyl-D-galactosamine/sialic acid 1 : 1 : 1 and 1 : 1 : 2 for apolipoprotein C-III1 and apolipoprotein C-III2	485:641	Monosaccharide analysis revealed the following sugar composition: D-galactose/N-acetyl-D-galactosamine/sialic acid 1 : 1 : 1 and 1 : 1 : 2 for apolipoprotein C-III1 and apolipoprotein C-III2, respectively.
208636	2	34	theme	C-III	445:449	arg1	structure					417:425	the complete structure	404:425	the complete structure of apolipoprotein C-III	404:449	The studies reported in this paper characterize these alkali labile oligosaccharides, thereby demonstrating the complete structure of apolipoprotein C-III.
208636	0	35	theme	side	40:43	arg1	chain					45:49	the oligosaccharide side chain	20:49	the oligosaccharide side chain of apolipoprotein C-III from human plasma very low density lipoproteins	20:121	Characterization of the oligosaccharide side chain of apolipoprotein C-III from human plasma very low density lipoproteins.
208636	3	36	theme	Monosaccharide	452:465	arg1	analysis					467:474	Monosaccharide analysis	452:474	Monosaccharide analysis	452:474	Monosaccharide analysis revealed the following sugar composition: D-galactose/N-acetyl-D-galactosamine/sialic acid 1 : 1 : 1 and 1 : 1 : 2 for apolipoprotein C-III1 and apolipoprotein C-III2, respectively.
208636	5	37	theme	Smith	921:925	arg1	degradation					927:937	Smith degradation	921:937	Smith degradation	921:937	Further studies employing periodate oxidation and Smith degradation indicated that the structure of the trisaccharide from apolipoprotein C-III1 was alpha-N-acetylneuraminyl-(2 leads to 3)-beta-D-galactosyl-(1 leads to 3)-N-acetyl-D-galactosaminitol.
208636	2	38	theme	apolipoprotein	430:443	arg1	C-III					445:449	apolipoprotein C-III	430:449	apolipoprotein C-III	430:449	The studies reported in this paper characterize these alkali labile oligosaccharides, thereby demonstrating the complete structure of apolipoprotein C-III.
208636	0	39	theme	apolipoprotein	54:67	arg1	C-III					69:73	apolipoprotein C-III	54:73	apolipoprotein C-III from human plasma very low density lipoproteins	54:121	Characterization of the oligosaccharide side chain of apolipoprotein C-III from human plasma very low density lipoproteins.
208636	4	40	theme	disaccharide	747:758	arg1	beta-D-galactosyl-					760:777	the reduced disaccharide beta-D-galactosyl-	735:777	the reduced disaccharide beta-D-galactosyl-	735:777	Treatment of desialylated apolipoproteins with alkaline borohydride released the reduced disaccharide beta-D-galactosyl-(1 leads to 3)-N-acetyl-D-galactosaminitol, which was detected by gas-liquid chromatography.
208636	3	41	theme	apolipoprotein	621:634	arg1	C-III2					636:641	apolipoprotein C-III2	621:641	apolipoprotein C-III2	621:641	Monosaccharide analysis revealed the following sugar composition: D-galactose/N-acetyl-D-galactosamine/sialic acid 1 : 1 : 1 and 1 : 1 : 2 for apolipoprotein C-III1 and apolipoprotein C-III2, respectively.
208636	2	42	theme	labile	357:362	arg1	oligosaccharides					364:379	these alkali labile oligosaccharides	344:379	these alkali labile oligosaccharides	344:379	The studies reported in this paper characterize these alkali labile oligosaccharides, thereby demonstrating the complete structure of apolipoprotein C-III.
208636	5	43	theme	periodate	897:905	arg1	oxidation					907:915	periodate oxidation	897:915	periodate oxidation	897:915	Further studies employing periodate oxidation and Smith degradation indicated that the structure of the trisaccharide from apolipoprotein C-III1 was alpha-N-acetylneuraminyl-(2 leads to 3)-beta-D-galactosyl-(1 leads to 3)-N-acetyl-D-galactosaminitol.
208636	5	44	theme	trisaccharide	975:987	arg1	structure					958:966	the structure	954:966	the structure of the trisaccharide from apolipoprotein C-III1 was alpha-N-acetylneuraminyl-(2	954:1046	Further studies employing periodate oxidation and Smith degradation indicated that the structure of the trisaccharide from apolipoprotein C-III1 was alpha-N-acetylneuraminyl-(2 leads to 3)-beta-D-galactosyl-(1 leads to 3)-N-acetyl-D-galactosaminitol.
208636	0	45	from	lipoproteins	110:121	arg1	chain					45:49	the oligosaccharide side chain	20:49	the oligosaccharide side chain of apolipoprotein C-III from human plasma very low density lipoproteins	20:121	Characterization of the oligosaccharide side chain of apolipoprotein C-III from human plasma very low density lipoproteins.
208636	0	45	from	lipoproteins	110:121	arg1	C-III					69:73	apolipoprotein C-III	54:73	apolipoprotein C-III from human plasma very low density lipoproteins	54:121	Characterization of the oligosaccharide side chain of apolipoprotein C-III from human plasma very low density lipoproteins.
208636	6	46	theme	alkaline	1343:1350	arg1	degradation					1352:1362	alkaline degradation	1343:1362	alkaline degradation	1343:1362	The tetrasaccharide structure from apolipoprotein C-III2 is made up of this trisaccharide plus one sialic acid residue linked to C6 of N-acetyl-D-galactosaminitol, as was shown by the assessment of chromogens formed upon alkaline degradation.
208636	1	47	theme	Apolipoprotein	124:137	arg1	C-III1					139:144	Apolipoprotein C-III1	124:144	Apolipoprotein C-III1	124:144	Apolipoprotein C-III1 and apolipoprotein C-III2 each contain one oligosaccharide side chain, bound O-glycosidically to threonine in position 74 of the amino acid sequence.
208636	1	48	from	threonine	243:251	arg1	position					256:263	position 74	256:266	position 74 of the amino acid sequence	256:293	Apolipoprotein C-III1 and apolipoprotein C-III2 each contain one oligosaccharide side chain, bound O-glycosidically to threonine in position 74 of the amino acid sequence.
208636	5	49	dep	-N-acetyl-D-galactosaminitol	1092:1119	arg1	3					1090:1090	3	1090:1090	3	1090:1090	Further studies employing periodate oxidation and Smith degradation indicated that the structure of the trisaccharide from apolipoprotein C-III1 was alpha-N-acetylneuraminyl-(2 leads to 3)-beta-D-galactosyl-(1 leads to 3)-N-acetyl-D-galactosaminitol.
208636	6	50	attach	linked	1241:1246	arg2	trisaccharide					1198:1210	this trisaccharide	1193:1210	this trisaccharide	1193:1210	The tetrasaccharide structure from apolipoprotein C-III2 is made up of this trisaccharide plus one sialic acid residue linked to C6 of N-acetyl-D-galactosaminitol, as was shown by the assessment of chromogens formed upon alkaline degradation.
208636	6	50	attach	linked	1241:1246	arg1	C6					1251:1252	C6	1251:1252	C6 of N-acetyl-D-galactosaminitol	1251:1283	The tetrasaccharide structure from apolipoprotein C-III2 is made up of this trisaccharide plus one sialic acid residue linked to C6 of N-acetyl-D-galactosaminitol, as was shown by the assessment of chromogens formed upon alkaline degradation.
208636	3	51	dep	composition	505:515	arg1	acid					562:565	D-galactose/N-acetyl-D-galactosamine/sialic acid 1	518:567	the following sugar composition: D-galactose/N-acetyl-D-galactosamine/sialic acid 1 : 1 : 1 and 1 : 1 : 2 for apolipoprotein C-III1 and apolipoprotein C-III2	485:641	Monosaccharide analysis revealed the following sugar composition: D-galactose/N-acetyl-D-galactosamine/sialic acid 1 : 1 : 1 and 1 : 1 : 2 for apolipoprotein C-III1 and apolipoprotein C-III2, respectively.
208636	3	51	dep	composition	505:515	arg1	1					571:571	1	571:571	1	571:571	Monosaccharide analysis revealed the following sugar composition: D-galactose/N-acetyl-D-galactosamine/sialic acid 1 : 1 : 1 and 1 : 1 : 2 for apolipoprotein C-III1 and apolipoprotein C-III2, respectively.
208636	4	52	theme	alkaline	705:712	arg1	borohydride					714:724	alkaline borohydride	705:724	alkaline borohydride	705:724	Treatment of desialylated apolipoproteins with alkaline borohydride released the reduced disaccharide beta-D-galactosyl-(1 leads to 3)-N-acetyl-D-galactosaminitol, which was detected by gas-liquid chromatography.
208636	6	53	theme	chromogens	1320:1329	arg1	assessment					1306:1315	the assessment	1302:1315	the assessment of chromogens formed upon alkaline degradation	1302:1362	The tetrasaccharide structure from apolipoprotein C-III2 is made up of this trisaccharide plus one sialic acid residue linked to C6 of N-acetyl-D-galactosaminitol, as was shown by the assessment of chromogens formed upon alkaline degradation.
208636	1	54	theme	apolipoprotein	150:163	arg1	C-III2					165:170	apolipoprotein C-III2	150:170	apolipoprotein C-III2	150:170	Apolipoprotein C-III1 and apolipoprotein C-III2 each contain one oligosaccharide side chain, bound O-glycosidically to threonine in position 74 of the amino acid sequence.
208636	3	55	theme	following	489:497	arg1	composition					505:515	the following sugar composition	485:515	the following sugar composition: D-galactose/N-acetyl-D-galactosamine/sialic acid 1 : 1 : 1 and 1 : 1 : 2 for apolipoprotein C-III1 and apolipoprotein C-III2	485:641	Monosaccharide analysis revealed the following sugar composition: D-galactose/N-acetyl-D-galactosamine/sialic acid 1 : 1 : 1 and 1 : 1 : 2 for apolipoprotein C-III1 and apolipoprotein C-III2, respectively.
208636	4	56	theme	desialylated	671:682	arg1	apolipoproteins					684:698	desialylated apolipoproteins	671:698	desialylated apolipoproteins	671:698	Treatment of desialylated apolipoproteins with alkaline borohydride released the reduced disaccharide beta-D-galactosyl-(1 leads to 3)-N-acetyl-D-galactosaminitol, which was detected by gas-liquid chromatography.
208636	0	57	theme	C-III	69:73	arg1	chain					45:49	the oligosaccharide side chain	20:49	the oligosaccharide side chain of apolipoprotein C-III from human plasma very low density lipoproteins	20:121	Characterization of the oligosaccharide side chain of apolipoprotein C-III from human plasma very low density lipoproteins.
208636	4	58	dep	released	726:733	arg1	1					779:779	1	779:779	1	779:779	Treatment of desialylated apolipoproteins with alkaline borohydride released the reduced disaccharide beta-D-galactosyl-(1 leads to 3)-N-acetyl-D-galactosaminitol, which was detected by gas-liquid chromatography.
208636	4	58	dep	released	726:733	arg1	leads					781:785	leads	781:785	leads to 3)-N-acetyl-D-galactosaminitol, which was detected by gas-liquid chromatography	781:868	Treatment of desialylated apolipoproteins with alkaline borohydride released the reduced disaccharide beta-D-galactosyl-(1 leads to 3)-N-acetyl-D-galactosaminitol, which was detected by gas-liquid chromatography.
208636	6	59	theme	acid	1228:1231	arg1	residue					1233:1239	one sialic acid residue	1217:1239	one sialic acid residue	1217:1239	The tetrasaccharide structure from apolipoprotein C-III2 is made up of this trisaccharide plus one sialic acid residue linked to C6 of N-acetyl-D-galactosaminitol, as was shown by the assessment of chromogens formed upon alkaline degradation.
208636	6	60	theme	tetrasaccharide	1126:1140	arg1	structure					1142:1150	The tetrasaccharide structure	1122:1150	The tetrasaccharide structure from apolipoprotein C-III2	1122:1177	The tetrasaccharide structure from apolipoprotein C-III2 is made up of this trisaccharide plus one sialic acid residue linked to C6 of N-acetyl-D-galactosaminitol, as was shown by the assessment of chromogens formed upon alkaline degradation.
6689265	0	0	theme	binding	76:82	arg1	protein					84:90	the human vitamin-D binding protein	56:90	the human vitamin-D binding protein	56:90	Isolation and characterization of the O-glycan chain of the human vitamin-D binding protein.
6689265	1	1	theme	genetic	231:237	arg1	forms					239:243	two genetic forms	227:243	two genetic forms of this protein	227:259	On a highly purified preparation, the structure of the carbohydrate chain of the human vitamin D-binding protein was investigated and two genetic forms of this protein were considered (Gc 2 and Gc 1 proteins).
6689265	0	2	theme	vitamin-D	66:74	arg1	protein					84:90	the human vitamin-D binding protein	56:90	the human vitamin-D binding protein	56:90	Isolation and characterization of the O-glycan chain of the human vitamin-D binding protein.
6689265	5	3	theme	rare	725:728	arg1	protein					712:718	The vitamin D-binding protein	690:718	The vitamin D-binding protein	690:718	The vitamin D-binding protein is a rare example of a serum protein O-glycosylated only on some genetic forms.
6689265	5	3	theme	rare	725:728	arg1	example					730:736	a rare example	723:736	a rare example of a serum protein O-glycosylated	723:770	The vitamin D-binding protein is a rare example of a serum protein O-glycosylated only on some genetic forms.
6689265	3	4	dep	beta	539:542	arg1	1					545:545	1	545:545	1	545:545	The structure of this O-glycosidically linked glycan was determined to be: Neu Ac alpha (2 leads to 3) Gal beta (1 leads to 3) GaINAc alpha (1 leads to 0) Ser (or Thr).
6689265	3	4	dep	beta	539:542	arg1	2					521:521	2	521:521	2	521:521	The structure of this O-glycosidically linked glycan was determined to be: Neu Ac alpha (2 leads to 3) Gal beta (1 leads to 3) GaINAc alpha (1 leads to 0) Ser (or Thr).
6689265	0	5	theme	protein	84:90	arg1	chain					47:51	the O-glycan chain	34:51	the O-glycan chain of the human vitamin-D binding protein	34:90	Isolation and characterization of the O-glycan chain of the human vitamin-D binding protein.
6689265	3	6	dep	Ser	587:589	arg1	3					556:556	3	556:556	3	556:556	The structure of this O-glycosidically linked glycan was determined to be: Neu Ac alpha (2 leads to 3) Gal beta (1 leads to 3) GaINAc alpha (1 leads to 0) Ser (or Thr).
6689265	5	7	theme	genetic	785:791	arg1	forms					793:797	some genetic forms	780:797	some genetic forms	780:797	The vitamin D-binding protein is a rare example of a serum protein O-glycosylated only on some genetic forms.
6689265	2	8	theme	protein	423:429	arg1	%					414:414	about 1%	407:414	about 1% of the protein	407:429	It was found that only the Gc 1 protein (Gc1a isoform) was glycosylated, the glycan moiety representing about 1% of the protein.
6689265	2	8	theme	protein	423:429	arg1	protein					423:429	the protein	419:429	the protein	419:429	It was found that only the Gc 1 protein (Gc1a isoform) was glycosylated, the glycan moiety representing about 1% of the protein.
6689265	1	9	theme	carbohydrate	148:159	arg1	chain					161:165	the carbohydrate chain	144:165	the carbohydrate chain of the human vitamin D-binding protein	144:204	On a highly purified preparation, the structure of the carbohydrate chain of the human vitamin D-binding protein was investigated and two genetic forms of this protein were considered (Gc 2 and Gc 1 proteins).
6689265	3	10	theme	GaINAc	559:564	arg1	alpha					566:570	GaINAc alpha	559:570	3) GaINAc alpha (1 leads to 0) Ser	556:589	The structure of this O-glycosidically linked glycan was determined to be: Neu Ac alpha (2 leads to 3) Gal beta (1 leads to 3) GaINAc alpha (1 leads to 0) Ser (or Thr).
6689265	3	10	theme	GaINAc	559:564	arg1	1					573:573	1	573:573	1	573:573	The structure of this O-glycosidically linked glycan was determined to be: Neu Ac alpha (2 leads to 3) Gal beta (1 leads to 3) GaINAc alpha (1 leads to 0) Ser (or Thr).
6689265	1	11	theme	chain	161:165	arg1	structure					131:139	the structure	127:139	the structure of the carbohydrate chain of the human vitamin D-binding protein	127:204	On a highly purified preparation, the structure of the carbohydrate chain of the human vitamin D-binding protein was investigated and two genetic forms of this protein were considered (Gc 2 and Gc 1 proteins).
6689265	3	12	theme	alpha	566:570	arg1	Ser					587:589	3) GaINAc alpha (1 leads to 0) Ser	556:589	3) GaINAc alpha (1 leads to 0) Ser	556:589	The structure of this O-glycosidically linked glycan was determined to be: Neu Ac alpha (2 leads to 3) Gal beta (1 leads to 3) GaINAc alpha (1 leads to 0) Ser (or Thr).
6689265	3	13	link	linked	471:476	arg1	glycan					478:483	this O-glycosidically linked glycan	449:483	this O-glycosidically linked glycan	449:483	The structure of this O-glycosidically linked glycan was determined to be: Neu Ac alpha (2 leads to 3) Gal beta (1 leads to 3) GaINAc alpha (1 leads to 0) Ser (or Thr).
6689265	5	14	theme	protein	749:755	arg1	O-glycosylated					757:770	a serum protein O-glycosylated	741:770	a serum protein O-glycosylated	741:770	The vitamin D-binding protein is a rare example of a serum protein O-glycosylated only on some genetic forms.
6689265	1	15	theme	protein	253:259	arg1	forms					239:243	two genetic forms	227:243	two genetic forms of this protein	227:259	On a highly purified preparation, the structure of the carbohydrate chain of the human vitamin D-binding protein was investigated and two genetic forms of this protein were considered (Gc 2 and Gc 1 proteins).
6689265	5	16	from	example	730:736	arg1	forms					793:797	some genetic forms	780:797	some genetic forms	780:797	The vitamin D-binding protein is a rare example of a serum protein O-glycosylated only on some genetic forms.
6689265	5	17	theme	O-glycosylated	757:770	arg1	protein					712:718	The vitamin D-binding protein	690:718	The vitamin D-binding protein	690:718	The vitamin D-binding protein is a rare example of a serum protein O-glycosylated only on some genetic forms.
6689265	5	17	theme	O-glycosylated	757:770	arg1	example					730:736	a rare example	723:736	a rare example of a serum protein O-glycosylated	723:770	The vitamin D-binding protein is a rare example of a serum protein O-glycosylated only on some genetic forms.
6689265	5	18	theme	D-binding	702:710	arg1	protein					712:718	The vitamin D-binding protein	690:718	The vitamin D-binding protein	690:718	The vitamin D-binding protein is a rare example of a serum protein O-glycosylated only on some genetic forms.
6689265	5	18	theme	D-binding	702:710	arg1	example					730:736	a rare example	723:736	a rare example of a serum protein O-glycosylated	723:770	The vitamin D-binding protein is a rare example of a serum protein O-glycosylated only on some genetic forms.
6689265	4	19	theme	tetrasaccharidic	603:618	arg1	O-glycan					620:627	A tetrasaccharidic O-glycan	601:627	A tetrasaccharidic O-glycan with two N-acetylneuraminic residues	601:664	A tetrasaccharidic O-glycan with two N-acetylneuraminic residues was also characterized.
6689265	3	20	theme	linked	471:476	arg1	glycan					478:483	this O-glycosidically linked glycan	449:483	this O-glycosidically linked glycan	449:483	The structure of this O-glycosidically linked glycan was determined to be: Neu Ac alpha (2 leads to 3) Gal beta (1 leads to 3) GaINAc alpha (1 leads to 0) Ser (or Thr).
6689265	1	21	theme	human	174:178	arg1	protein					198:204	the human vitamin D-binding protein	170:204	the human vitamin D-binding protein	170:204	On a highly purified preparation, the structure of the carbohydrate chain of the human vitamin D-binding protein was investigated and two genetic forms of this protein were considered (Gc 2 and Gc 1 proteins).
6689265	3	22	theme	glycan	478:483	arg1	structure					436:444	The structure	432:444	The structure of this O-glycosidically linked glycan	432:483	The structure of this O-glycosidically linked glycan was determined to be: Neu Ac alpha (2 leads to 3) Gal beta (1 leads to 3) GaINAc alpha (1 leads to 0) Ser (or Thr).
6689265	2	23	theme	Gc1a	344:347	arg1	protein					335:341	Gc 1 protein	330:341	only the Gc 1 protein (Gc1a isoform)	321:356	It was found that only the Gc 1 protein (Gc1a isoform) was glycosylated, the glycan moiety representing about 1% of the protein.
6689265	2	23	theme	Gc1a	344:347	arg1	isoform					349:355	Gc1a isoform	344:355	Gc1a isoform	344:355	It was found that only the Gc 1 protein (Gc1a isoform) was glycosylated, the glycan moiety representing about 1% of the protein.
6689265	0	24	theme	O-glycan	38:45	arg1	chain					47:51	the O-glycan chain	34:51	the O-glycan chain of the human vitamin-D binding protein	34:90	Isolation and characterization of the O-glycan chain of the human vitamin-D binding protein.
6689265	1	25	theme	D-binding	188:196	arg1	protein					198:204	the human vitamin D-binding protein	170:204	the human vitamin D-binding protein	170:204	On a highly purified preparation, the structure of the carbohydrate chain of the human vitamin D-binding protein was investigated and two genetic forms of this protein were considered (Gc 2 and Gc 1 proteins).
6689265	3	26	dep	1	573:573	arg1	leads					575:579	leads	575:579	leads	575:579	The structure of this O-glycosidically linked glycan was determined to be: Neu Ac alpha (2 leads to 3) Gal beta (1 leads to 3) GaINAc alpha (1 leads to 0) Ser (or Thr).
6689265	3	26	dep	1	573:573	arg1	to					581:582	to	581:582	to	581:582	The structure of this O-glycosidically linked glycan was determined to be: Neu Ac alpha (2 leads to 3) Gal beta (1 leads to 3) GaINAc alpha (1 leads to 0) Ser (or Thr).
6689265	3	27	theme	Neu	507:509	arg1	beta					539:542	Neu Ac alpha (2 leads to 3) Gal beta	507:542	Neu Ac alpha (2 leads to 3) Gal beta (1	507:545	The structure of this O-glycosidically linked glycan was determined to be: Neu Ac alpha (2 leads to 3) Gal beta (1 leads to 3) GaINAc alpha (1 leads to 0) Ser (or Thr).
6689265	1	28	theme	protein	198:204	arg1	chain					161:165	the carbohydrate chain	144:165	the carbohydrate chain of the human vitamin D-binding protein	144:204	On a highly purified preparation, the structure of the carbohydrate chain of the human vitamin D-binding protein was investigated and two genetic forms of this protein were considered (Gc 2 and Gc 1 proteins).
6689265	2	29	theme	glycan	380:385	arg1	moiety					387:392	the glycan moiety	376:392	the glycan moiety representing about 1% of the protein	376:429	It was found that only the Gc 1 protein (Gc1a isoform) was glycosylated, the glycan moiety representing about 1% of the protein.
6689265	4	30	theme	N-acetylneuraminic	638:655	arg1	residues					657:664	two N-acetylneuraminic residues	634:664	two N-acetylneuraminic residues	634:664	A tetrasaccharidic O-glycan with two N-acetylneuraminic residues was also characterized.
6689265	0	31	theme	chain	47:51	arg1	characterization					14:29	characterization	14:29	characterization	14:29	Isolation and characterization of the O-glycan chain of the human vitamin-D binding protein.
6689265	0	31	theme	chain	47:51	arg1	Isolation					0:8	Isolation	0:8	Isolation	0:8	Isolation and characterization of the O-glycan chain of the human vitamin-D binding protein.
6689265	1	32	theme	purified	105:112	arg1	preparation					114:124	a highly purified preparation	96:124	a highly purified preparation	96:124	On a highly purified preparation, the structure of the carbohydrate chain of the human vitamin D-binding protein was investigated and two genetic forms of this protein were considered (Gc 2 and Gc 1 proteins).
6689265	1	33	theme	Gc	287:288	arg1	proteins					292:299	Gc 2 and Gc 1 proteins	278:299	proteins	292:299	On a highly purified preparation, the structure of the carbohydrate chain of the human vitamin D-binding protein was investigated and two genetic forms of this protein were considered (Gc 2 and Gc 1 proteins).
6689265	2	34	gly	glycosylated	362:373	arg1	protein					335:341	Gc 1 protein	330:341	only the Gc 1 protein (Gc1a isoform)	321:356	It was found that only the Gc 1 protein (Gc1a isoform) was glycosylated, the glycan moiety representing about 1% of the protein.
6689265	2	34	gly	glycosylated	362:373	arg1	isoform					349:355	Gc1a isoform	344:355	Gc1a isoform	344:355	It was found that only the Gc 1 protein (Gc1a isoform) was glycosylated, the glycan moiety representing about 1% of the protein.
6689265	3	35	theme	Gal	535:537	arg1	beta					539:542	Neu Ac alpha (2 leads to 3) Gal beta	507:542	Neu Ac alpha (2 leads to 3) Gal beta (1	507:545	The structure of this O-glycosidically linked glycan was determined to be: Neu Ac alpha (2 leads to 3) Gal beta (1 leads to 3) GaINAc alpha (1 leads to 0) Ser (or Thr).
6689265	5	36	theme	serum	743:747	arg1	O-glycosylated					757:770	a serum protein O-glycosylated	741:770	a serum protein O-glycosylated	741:770	The vitamin D-binding protein is a rare example of a serum protein O-glycosylated only on some genetic forms.
6689265	0	37	theme	human	60:64	arg1	protein					84:90	the human vitamin-D binding protein	56:90	the human vitamin-D binding protein	56:90	Isolation and characterization of the O-glycan chain of the human vitamin-D binding protein.
6689265	3	38	dep	2	521:521	arg1	3					532:532	3	532:532	3	532:532	The structure of this O-glycosidically linked glycan was determined to be: Neu Ac alpha (2 leads to 3) Gal beta (1 leads to 3) GaINAc alpha (1 leads to 0) Ser (or Thr).
6689265	3	38	dep	2	521:521	arg1	leads					523:527	leads	523:527	leads	523:527	The structure of this O-glycosidically linked glycan was determined to be: Neu Ac alpha (2 leads to 3) Gal beta (1 leads to 3) GaINAc alpha (1 leads to 0) Ser (or Thr).
6689265	3	38	dep	2	521:521	arg1	to					529:530	to	529:530	to	529:530	The structure of this O-glycosidically linked glycan was determined to be: Neu Ac alpha (2 leads to 3) Gal beta (1 leads to 3) GaINAc alpha (1 leads to 0) Ser (or Thr).
6689265	3	39	theme	Ac	511:512	arg1	beta					539:542	Neu Ac alpha (2 leads to 3) Gal beta	507:542	Neu Ac alpha (2 leads to 3) Gal beta (1	507:545	The structure of this O-glycosidically linked glycan was determined to be: Neu Ac alpha (2 leads to 3) Gal beta (1 leads to 3) GaINAc alpha (1 leads to 0) Ser (or Thr).
6689265	2	40	theme	Gc	330:331	arg1	protein					335:341	Gc 1 protein	330:341	only the Gc 1 protein (Gc1a isoform)	321:356	It was found that only the Gc 1 protein (Gc1a isoform) was glycosylated, the glycan moiety representing about 1% of the protein.
6689265	2	40	theme	Gc	330:331	arg1	isoform					349:355	Gc1a isoform	344:355	Gc1a isoform	344:355	It was found that only the Gc 1 protein (Gc1a isoform) was glycosylated, the glycan moiety representing about 1% of the protein.
6689265	3	41	theme	alpha	514:518	arg1	beta					539:542	Neu Ac alpha (2 leads to 3) Gal beta	507:542	Neu Ac alpha (2 leads to 3) Gal beta (1	507:545	The structure of this O-glycosidically linked glycan was determined to be: Neu Ac alpha (2 leads to 3) Gal beta (1 leads to 3) GaINAc alpha (1 leads to 0) Ser (or Thr).
6689265	4	42	with	O-glycan	620:627	arg1	residues					657:664	two N-acetylneuraminic residues	634:664	two N-acetylneuraminic residues	634:664	A tetrasaccharidic O-glycan with two N-acetylneuraminic residues was also characterized.
3371361	5	0	theme	major	896:900	arg1	components					902:911	two major components	892:911	two major components	892:911	Subsequently, the O-glycosidic sialyloligosaccharide-alditols were subfractionated by anion-exchange chromatography on Mono Q. Structural analysis by 500-MHz 1H-NMR spectroscopy revealed two major components in all fractions, namely: NeuAc alpha 2-3Gal beta 1-3GalNAc-ol and NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc-ol.
3371361	7	1	from	presence	1190:1197	arg1	fractions					1239:1247	Bio-Gel fractions	1231:1247	Bio-Gel fractions differing in molecular mass	1231:1275	The presence of these carbohydrate chains in Bio-Gel fractions differing in molecular mass suggested that they are derived from glycopeptides which are heterogeneous in their peptide part.
3371361	5	2	theme	O-glycosidic	723:734	arg1	sialyloligosaccharide-alditols					736:765	the O-glycosidic sialyloligosaccharide-alditols	719:765	the O-glycosidic sialyloligosaccharide-alditols	719:765	Subsequently, the O-glycosidic sialyloligosaccharide-alditols were subfractionated by anion-exchange chromatography on Mono Q. Structural analysis by 500-MHz 1H-NMR spectroscopy revealed two major components in all fractions, namely: NeuAc alpha 2-3Gal beta 1-3GalNAc-ol and NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc-ol.
3371361	6	3	theme	1-4GlcNAc	1100:1108	arg1	beta					1110:1113	NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-3Gal beta 1-4GlcNAc beta	1048:1113	NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6]GalNAc-ol	1048:1127	Furthermore, NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6]GalNAc-ol was found as a minor component in some of the fractions.
3371361	2	4	attach	presence	260:267	arg1	position					312:319	non-reducing position	299:319	non-reducing position	299:319	All pooled fractions containing carbohydrates showed the presence of small amounts of GalNAc in non-reducing position, besides free N-acetyllactosamine type of oligosaccharides as major constituents.
3371361	2	4	attach	presence	260:267	arg2	GalNAc					289:294	GalNAc	289:294	GalNAc	289:294	All pooled fractions containing carbohydrates showed the presence of small amounts of GalNAc in non-reducing position, besides free N-acetyllactosamine type of oligosaccharides as major constituents.
3371361	2	4	attach	presence	260:267	arg2	amounts					278:284	small amounts	272:284	small amounts of GalNAc	272:294	All pooled fractions containing carbohydrates showed the presence of small amounts of GalNAc in non-reducing position, besides free N-acetyllactosamine type of oligosaccharides as major constituents.
3371361	4	5	from	step	688:691	arg1	AcA					696:698	AcA 202	696:702	AcA 202	696:702	The GalNAc-ol-containing material was separated from the N-glycosidic oligosaccharides by a second gel-filtration step on AcA 202.
3371361	7	6	theme	Bio-Gel	1231:1237	arg1	fractions					1239:1247	Bio-Gel fractions	1231:1247	Bio-Gel fractions differing in molecular mass	1231:1275	The presence of these carbohydrate chains in Bio-Gel fractions differing in molecular mass suggested that they are derived from glycopeptides which are heterogeneous in their peptide part.
3371361	6	7	theme	1-6	1115:1117	arg1	component					1150:1158	a minor component	1142:1158	a minor component in some of the fractions	1142:1183	Furthermore, NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6]GalNAc-ol was found as a minor component in some of the fractions.
3371361	6	7	theme	1-6	1115:1117	arg1	GalNAc-ol					1119:1127	NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6]GalNAc-ol	1048:1127	NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6]GalNAc-ol	1048:1127	Furthermore, NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6]GalNAc-ol was found as a minor component in some of the fractions.
3371361	0	8	theme	sialidosis	115:124	arg1	patient					126:132	a sialidosis patient	113:132	a sialidosis patient	113:132	Structural analysis of O-glycosidic type of sialyloligosaccharide-alditols derived from urinary glycopeptides of a sialidosis patient.
3371361	6	9	theme	minor	1144:1148	arg1	component					1150:1158	a minor component	1142:1158	a minor component in some of the fractions	1142:1183	Furthermore, NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6]GalNAc-ol was found as a minor component in some of the fractions.
3371361	6	9	theme	minor	1144:1148	arg1	GalNAc-ol					1119:1127	NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6]GalNAc-ol	1048:1127	NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6]GalNAc-ol	1048:1127	Furthermore, NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6]GalNAc-ol was found as a minor component in some of the fractions.
3371361	4	10	theme	gel-filtration	673:686	arg1	step					688:691	a second gel-filtration step	664:691	a second gel-filtration step on AcA 202	664:702	The GalNAc-ol-containing material was separated from the N-glycosidic oligosaccharides by a second gel-filtration step on AcA 202.
3371361	5	11	theme	500-MHz	855:861	arg1	spectroscopy					870:881	500-MHz 1H-NMR spectroscopy	855:881	500-MHz 1H-NMR spectroscopy	855:881	Subsequently, the O-glycosidic sialyloligosaccharide-alditols were subfractionated by anion-exchange chromatography on Mono Q. Structural analysis by 500-MHz 1H-NMR spectroscopy revealed two major components in all fractions, namely: NeuAc alpha 2-3Gal beta 1-3GalNAc-ol and NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc-ol.
3371361	7	12	theme	carbohydrate	1208:1219	arg1	chains					1221:1226	these carbohydrate chains	1202:1226	these carbohydrate chains	1202:1226	The presence of these carbohydrate chains in Bio-Gel fractions differing in molecular mass suggested that they are derived from glycopeptides which are heterogeneous in their peptide part.
3371361	4	13	theme	second	666:671	arg1	step					688:691	a second gel-filtration step	664:691	a second gel-filtration step on AcA 202	664:702	The GalNAc-ol-containing material was separated from the N-glycosidic oligosaccharides by a second gel-filtration step on AcA 202.
3371361	5	14	theme	1H-NMR	863:868	arg1	spectroscopy					870:881	500-MHz 1H-NMR spectroscopy	855:881	500-MHz 1H-NMR spectroscopy	855:881	Subsequently, the O-glycosidic sialyloligosaccharide-alditols were subfractionated by anion-exchange chromatography on Mono Q. Structural analysis by 500-MHz 1H-NMR spectroscopy revealed two major components in all fractions, namely: NeuAc alpha 2-3Gal beta 1-3GalNAc-ol and NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc-ol.
3371361	1	15	theme	Sialidosis	135:144	arg1	urine					146:150	Sialidosis urine	135:150	Sialidosis urine	135:150	Sialidosis urine was fractionated by gel filtration on Bio-Gel P-6.
3371361	7	16	from	part	1369:1372	arg1	heterogeneous					1338:1350	heterogeneous	1338:1350	heterogeneous	1338:1350	The presence of these carbohydrate chains in Bio-Gel fractions differing in molecular mass suggested that they are derived from glycopeptides which are heterogeneous in their peptide part.
3371361	0	17	gly	glycopeptides	96:108	arg1	patient					126:132	a sialidosis patient	113:132	a sialidosis patient	113:132	Structural analysis of O-glycosidic type of sialyloligosaccharide-alditols derived from urinary glycopeptides of a sialidosis patient.
3371361	0	17	gly	glycopeptides	96:108	arg2	glycopeptides					96:108	urinary glycopeptides	88:108	urinary glycopeptides of a sialidosis patient	88:132	Structural analysis of O-glycosidic type of sialyloligosaccharide-alditols derived from urinary glycopeptides of a sialidosis patient.
3371361	1	18	theme	Bio-Gel	190:196	arg1	P-6					198:200	Bio-Gel P-6	190:200	Bio-Gel P-6	190:200	Sialidosis urine was fractionated by gel filtration on Bio-Gel P-6.
3371361	0	19	theme	patient	126:132	arg1	glycopeptides					96:108	urinary glycopeptides	88:108	urinary glycopeptides of a sialidosis patient	88:132	Structural analysis of O-glycosidic type of sialyloligosaccharide-alditols derived from urinary glycopeptides of a sialidosis patient.
3371361	3	20	theme	reductive	435:443	arg1	degradation					466:476	reductive alkaline borohydride degradation	435:476	reductive alkaline borohydride degradation	435:476	The fractions were subjected to reductive alkaline borohydride degradation, after which the major part of GalNAc was recovered as N-acetyl-D-galactosaminitol (GalNAc-ol).
3371361	3	21	theme	major	495:499	arg1	N-acetyl-D-galactosaminitol					533:559	N-acetyl-D-galactosaminitol	533:559	N-acetyl-D-galactosaminitol (GalNAc-ol)	533:571	The fractions were subjected to reductive alkaline borohydride degradation, after which the major part of GalNAc was recovered as N-acetyl-D-galactosaminitol (GalNAc-ol).
3371361	3	21	theme	major	495:499	arg1	part					501:504	the major part	491:504	the major part of GalNAc	491:514	The fractions were subjected to reductive alkaline borohydride degradation, after which the major part of GalNAc was recovered as N-acetyl-D-galactosaminitol (GalNAc-ol).
3371361	5	22	dep	Q.	829:830	arg1	GalNAc-ol					1024:1032	NeuAc alpha 2-3Gal beta 1-3GalNAc-ol and NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc-ol	939:1032	Mono Q. Structural analysis by 500-MHz 1H-NMR spectroscopy revealed two major components in all fractions, namely: NeuAc alpha 2-3Gal beta 1-3GalNAc-ol and NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc-ol	824:1032	Subsequently, the O-glycosidic sialyloligosaccharide-alditols were subfractionated by anion-exchange chromatography on Mono Q. Structural analysis by 500-MHz 1H-NMR spectroscopy revealed two major components in all fractions, namely: NeuAc alpha 2-3Gal beta 1-3GalNAc-ol and NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc-ol.
3371361	5	22	dep	Q.	829:830	arg1	revealed					883:890	revealed	883:890	revealed two major components in all fractions, namely	883:936	Subsequently, the O-glycosidic sialyloligosaccharide-alditols were subfractionated by anion-exchange chromatography on Mono Q. Structural analysis by 500-MHz 1H-NMR spectroscopy revealed two major components in all fractions, namely: NeuAc alpha 2-3Gal beta 1-3GalNAc-ol and NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc-ol.
3371361	7	23	theme	peptide	1361:1367	arg1	part					1369:1372	their peptide part	1355:1372	their peptide part	1355:1372	The presence of these carbohydrate chains in Bio-Gel fractions differing in molecular mass suggested that they are derived from glycopeptides which are heterogeneous in their peptide part.
3371361	3	24	theme	borohydride	454:464	arg1	degradation					466:476	reductive alkaline borohydride degradation	435:476	reductive alkaline borohydride degradation	435:476	The fractions were subjected to reductive alkaline borohydride degradation, after which the major part of GalNAc was recovered as N-acetyl-D-galactosaminitol (GalNAc-ol).
3371361	2	25	from	presence	260:267	arg1	position					312:319	non-reducing position	299:319	non-reducing position	299:319	All pooled fractions containing carbohydrates showed the presence of small amounts of GalNAc in non-reducing position, besides free N-acetyllactosamine type of oligosaccharides as major constituents.
3371361	5	26	theme	2-3Gal	992:997	arg1	GalNAc-ol					1024:1032	NeuAc alpha 2-3Gal beta 1-3GalNAc-ol and NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc-ol	939:1032	Mono Q. Structural analysis by 500-MHz 1H-NMR spectroscopy revealed two major components in all fractions, namely: NeuAc alpha 2-3Gal beta 1-3GalNAc-ol and NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc-ol	824:1032	Subsequently, the O-glycosidic sialyloligosaccharide-alditols were subfractionated by anion-exchange chromatography on Mono Q. Structural analysis by 500-MHz 1H-NMR spectroscopy revealed two major components in all fractions, namely: NeuAc alpha 2-3Gal beta 1-3GalNAc-ol and NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc-ol.
3371361	0	27	theme	Structural	0:9	arg1	analysis					11:18	Structural analysis	0:18	Structural analysis of O-glycosidic type of sialyloligosaccharide-alditols	0:73	Structural analysis of O-glycosidic type of sialyloligosaccharide-alditols derived from urinary glycopeptides of a sialidosis patient.
3371361	6	28	theme	beta	1095:1098	arg1	beta					1110:1113	NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-3Gal beta 1-4GlcNAc beta	1048:1113	NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6]GalNAc-ol	1048:1127	Furthermore, NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6]GalNAc-ol was found as a minor component in some of the fractions.
3371361	7	29	from	heterogeneous	1338:1350	arg1	part					1369:1372	their peptide part	1355:1372	their peptide part	1355:1372	The presence of these carbohydrate chains in Bio-Gel fractions differing in molecular mass suggested that they are derived from glycopeptides which are heterogeneous in their peptide part.
3371361	5	30	theme	NeuAc	980:984	arg1	2-3Gal					992:997	NeuAc alpha 2-3Gal beta 1-3GalNAc-ol and NeuAc alpha 2-3Gal	939:997	2-3Gal	992:997	Subsequently, the O-glycosidic sialyloligosaccharide-alditols were subfractionated by anion-exchange chromatography on Mono Q. Structural analysis by 500-MHz 1H-NMR spectroscopy revealed two major components in all fractions, namely: NeuAc alpha 2-3Gal beta 1-3GalNAc-ol and NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc-ol.
3371361	2	31	theme	N-acetyllactosamine	335:353	arg1	type					355:358	free N-acetyllactosamine type	330:358	free N-acetyllactosamine type of oligosaccharides as major constituents	330:400	All pooled fractions containing carbohydrates showed the presence of small amounts of GalNAc in non-reducing position, besides free N-acetyllactosamine type of oligosaccharides as major constituents.
3371361	5	32	theme	beta	999:1002	arg1	GalNAc-ol					1024:1032	NeuAc alpha 2-3Gal beta 1-3GalNAc-ol and NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc-ol	939:1032	Mono Q. Structural analysis by 500-MHz 1H-NMR spectroscopy revealed two major components in all fractions, namely: NeuAc alpha 2-3Gal beta 1-3GalNAc-ol and NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc-ol	824:1032	Subsequently, the O-glycosidic sialyloligosaccharide-alditols were subfractionated by anion-exchange chromatography on Mono Q. Structural analysis by 500-MHz 1H-NMR spectroscopy revealed two major components in all fractions, namely: NeuAc alpha 2-3Gal beta 1-3GalNAc-ol and NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc-ol.
3371361	0	33	theme	O-glycosidic	23:34	arg1	type					36:39	O-glycosidic type	23:39	O-glycosidic type of sialyloligosaccharide-alditols	23:73	Structural analysis of O-glycosidic type of sialyloligosaccharide-alditols derived from urinary glycopeptides of a sialidosis patient.
3371361	6	34	theme	2-3Gal	1088:1093	arg1	beta					1110:1113	NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-3Gal beta 1-4GlcNAc beta	1048:1113	NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6]GalNAc-ol	1048:1127	Furthermore, NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6]GalNAc-ol was found as a minor component in some of the fractions.
3371361	7	35	theme	chains	1221:1226	arg1	presence					1190:1197	The presence	1186:1197	The presence of these carbohydrate chains in Bio-Gel fractions differing in molecular mass	1186:1275	The presence of these carbohydrate chains in Bio-Gel fractions differing in molecular mass suggested that they are derived from glycopeptides which are heterogeneous in their peptide part.
3371361	6	36	from	component	1150:1158	arg1	some					1163:1166	some	1163:1166	some	1163:1166	Furthermore, NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6]GalNAc-ol was found as a minor component in some of the fractions.
3371361	6	36	from	component	1150:1158	arg1	fractions					1175:1183	the fractions	1171:1183	the fractions	1171:1183	Furthermore, NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6]GalNAc-ol was found as a minor component in some of the fractions.
3371361	2	37	theme	free	330:333	arg1	type					355:358	free N-acetyllactosamine type	330:358	free N-acetyllactosamine type of oligosaccharides as major constituents	330:400	All pooled fractions containing carbohydrates showed the presence of small amounts of GalNAc in non-reducing position, besides free N-acetyllactosamine type of oligosaccharides as major constituents.
3371361	3	38	theme	GalNAc	509:514	arg1	N-acetyl-D-galactosaminitol					533:559	N-acetyl-D-galactosaminitol	533:559	N-acetyl-D-galactosaminitol (GalNAc-ol)	533:571	The fractions were subjected to reductive alkaline borohydride degradation, after which the major part of GalNAc was recovered as N-acetyl-D-galactosaminitol (GalNAc-ol).
3371361	3	38	theme	GalNAc	509:514	arg1	part					501:504	the major part	491:504	the major part of GalNAc	491:514	The fractions were subjected to reductive alkaline borohydride degradation, after which the major part of GalNAc was recovered as N-acetyl-D-galactosaminitol (GalNAc-ol).
3371361	5	39	theme	alpha	945:949	arg1	1-3GalNAc-ol					963:974	NeuAc alpha 2-3Gal beta 1-3GalNAc-ol and NeuAc alpha 2-3Gal	939:997	1-3GalNAc-ol	963:974	Subsequently, the O-glycosidic sialyloligosaccharide-alditols were subfractionated by anion-exchange chromatography on Mono Q. Structural analysis by 500-MHz 1H-NMR spectroscopy revealed two major components in all fractions, namely: NeuAc alpha 2-3Gal beta 1-3GalNAc-ol and NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc-ol.
3371361	6	40	theme	alpha	1082:1086	arg1	beta					1110:1113	NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-3Gal beta 1-4GlcNAc beta	1048:1113	NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6]GalNAc-ol	1048:1127	Furthermore, NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6]GalNAc-ol was found as a minor component in some of the fractions.
3371361	2	41	theme	non-reducing	299:310	arg1	position					312:319	non-reducing position	299:319	non-reducing position	299:319	All pooled fractions containing carbohydrates showed the presence of small amounts of GalNAc in non-reducing position, besides free N-acetyllactosamine type of oligosaccharides as major constituents.
3371361	7	42	gly	glycopeptides	1314:1326	arg2	glycopeptides					1314:1326	glycopeptides	1314:1326	glycopeptides which are heterogeneous in their peptide part	1314:1372	The presence of these carbohydrate chains in Bio-Gel fractions differing in molecular mass suggested that they are derived from glycopeptides which are heterogeneous in their peptide part.
3371361	5	43	theme	beta	958:961	arg1	1-3GalNAc-ol					963:974	NeuAc alpha 2-3Gal beta 1-3GalNAc-ol and NeuAc alpha 2-3Gal	939:997	1-3GalNAc-ol	963:974	Subsequently, the O-glycosidic sialyloligosaccharide-alditols were subfractionated by anion-exchange chromatography on Mono Q. Structural analysis by 500-MHz 1H-NMR spectroscopy revealed two major components in all fractions, namely: NeuAc alpha 2-3Gal beta 1-3GalNAc-ol and NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc-ol.
3371361	4	44	theme	N-glycosidic	631:642	arg1	oligosaccharides					644:659	the N-glycosidic oligosaccharides	627:659	the N-glycosidic oligosaccharides	627:659	The GalNAc-ol-containing material was separated from the N-glycosidic oligosaccharides by a second gel-filtration step on AcA 202.
3371361	5	45	theme	Structural	832:841	arg1	analysis					843:850	Structural analysis	832:850	Structural analysis by 500-MHz 1H-NMR spectroscopy	832:881	Subsequently, the O-glycosidic sialyloligosaccharide-alditols were subfractionated by anion-exchange chromatography on Mono Q. Structural analysis by 500-MHz 1H-NMR spectroscopy revealed two major components in all fractions, namely: NeuAc alpha 2-3Gal beta 1-3GalNAc-ol and NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc-ol.
3371361	5	46	theme	1-3GalNAc-ol	963:974	arg1	GalNAc-ol					1024:1032	NeuAc alpha 2-3Gal beta 1-3GalNAc-ol and NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc-ol	939:1032	Mono Q. Structural analysis by 500-MHz 1H-NMR spectroscopy revealed two major components in all fractions, namely: NeuAc alpha 2-3Gal beta 1-3GalNAc-ol and NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc-ol	824:1032	Subsequently, the O-glycosidic sialyloligosaccharide-alditols were subfractionated by anion-exchange chromatography on Mono Q. Structural analysis by 500-MHz 1H-NMR spectroscopy revealed two major components in all fractions, namely: NeuAc alpha 2-3Gal beta 1-3GalNAc-ol and NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc-ol.
3371361	6	47	theme	1-3[NeuAc	1072:1080	arg1	beta					1110:1113	NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-3Gal beta 1-4GlcNAc beta	1048:1113	NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6]GalNAc-ol	1048:1127	Furthermore, NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6]GalNAc-ol was found as a minor component in some of the fractions.
3371361	2	48	contain	containing	224:233	arg2	carbohydrates					235:247	carbohydrates	235:247	carbohydrates	235:247	All pooled fractions containing carbohydrates showed the presence of small amounts of GalNAc in non-reducing position, besides free N-acetyllactosamine type of oligosaccharides as major constituents.
3371361	2	48	contain	containing	224:233	arg1	fractions					214:222	All pooled fractions	203:222	All pooled fractions containing carbohydrates	203:247	All pooled fractions containing carbohydrates showed the presence of small amounts of GalNAc in non-reducing position, besides free N-acetyllactosamine type of oligosaccharides as major constituents.
3371361	0	49	theme	type	36:39	arg1	analysis					11:18	Structural analysis	0:18	Structural analysis of O-glycosidic type of sialyloligosaccharide-alditols	0:73	Structural analysis of O-glycosidic type of sialyloligosaccharide-alditols derived from urinary glycopeptides of a sialidosis patient.
3371361	6	50	theme	beta	1067:1070	arg1	beta					1110:1113	NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-3Gal beta 1-4GlcNAc beta	1048:1113	NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6]GalNAc-ol	1048:1127	Furthermore, NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6]GalNAc-ol was found as a minor component in some of the fractions.
3371361	5	51	theme	NeuAc	939:943	arg1	1-3GalNAc-ol					963:974	NeuAc alpha 2-3Gal beta 1-3GalNAc-ol and NeuAc alpha 2-3Gal	939:997	1-3GalNAc-ol	963:974	Subsequently, the O-glycosidic sialyloligosaccharide-alditols were subfractionated by anion-exchange chromatography on Mono Q. Structural analysis by 500-MHz 1H-NMR spectroscopy revealed two major components in all fractions, namely: NeuAc alpha 2-3Gal beta 1-3GalNAc-ol and NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc-ol.
3371361	7	52	theme	molecular	1262:1270	arg1	mass					1272:1275	molecular mass	1262:1275	molecular mass	1262:1275	The presence of these carbohydrate chains in Bio-Gel fractions differing in molecular mass suggested that they are derived from glycopeptides which are heterogeneous in their peptide part.
3371361	3	53	theme	alkaline	445:452	arg1	degradation					466:476	reductive alkaline borohydride degradation	435:476	reductive alkaline borohydride degradation	435:476	The fractions were subjected to reductive alkaline borohydride degradation, after which the major part of GalNAc was recovered as N-acetyl-D-galactosaminitol (GalNAc-ol).
3371361	4	54	theme	GalNAc-ol-containing	578:597	arg1	material					599:606	The GalNAc-ol-containing material	574:606	The GalNAc-ol-containing material	574:606	The GalNAc-ol-containing material was separated from the N-glycosidic oligosaccharides by a second gel-filtration step on AcA 202.
3371361	7	55	attach	derived	1301:1307	arg2	they					1292:1295	they	1292:1295	they	1292:1295	The presence of these carbohydrate chains in Bio-Gel fractions differing in molecular mass suggested that they are derived from glycopeptides which are heterogeneous in their peptide part.
3371361	7	55	attach	derived	1301:1307	arg1	glycopeptides					1314:1326	glycopeptides	1314:1326	glycopeptides which are heterogeneous in their peptide part	1314:1372	The presence of these carbohydrate chains in Bio-Gel fractions differing in molecular mass suggested that they are derived from glycopeptides which are heterogeneous in their peptide part.
3371361	2	56	theme	major	383:387	arg1	constituents					389:400	major constituents	383:400	major constituents	383:400	All pooled fractions containing carbohydrates showed the presence of small amounts of GalNAc in non-reducing position, besides free N-acetyllactosamine type of oligosaccharides as major constituents.
3371361	0	57	theme	sialyloligosaccharide-alditols	44:73	arg1	type					36:39	O-glycosidic type	23:39	O-glycosidic type of sialyloligosaccharide-alditols	23:73	Structural analysis of O-glycosidic type of sialyloligosaccharide-alditols derived from urinary glycopeptides of a sialidosis patient.
3371361	6	58	theme	alpha	1054:1058	arg1	2-3Gal					1060:1065	NeuAc alpha 2-3Gal	1048:1065	NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6]GalNAc-ol	1048:1127	Furthermore, NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6]GalNAc-ol was found as a minor component in some of the fractions.
3371361	5	59	theme	anion-exchange	791:804	arg1	chromatography					806:819	anion-exchange chromatography	791:819	anion-exchange chromatography on Mono Q. Structural analysis by 500-MHz 1H-NMR spectroscopy revealed two major components in all fractions, namely: NeuAc alpha 2-3Gal beta 1-3GalNAc-ol and NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc-ol	791:1032	Subsequently, the O-glycosidic sialyloligosaccharide-alditols were subfractionated by anion-exchange chromatography on Mono Q. Structural analysis by 500-MHz 1H-NMR spectroscopy revealed two major components in all fractions, namely: NeuAc alpha 2-3Gal beta 1-3GalNAc-ol and NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc-ol.
3371361	6	60	theme	NeuAc	1048:1052	arg1	2-3Gal					1060:1065	NeuAc alpha 2-3Gal	1048:1065	NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6]GalNAc-ol	1048:1127	Furthermore, NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6]GalNAc-ol was found as a minor component in some of the fractions.
3371361	5	61	from	components	902:911	arg1	fractions					920:928	all fractions	916:928	all fractions	916:928	Subsequently, the O-glycosidic sialyloligosaccharide-alditols were subfractionated by anion-exchange chromatography on Mono Q. Structural analysis by 500-MHz 1H-NMR spectroscopy revealed two major components in all fractions, namely: NeuAc alpha 2-3Gal beta 1-3GalNAc-ol and NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc-ol.
3371361	2	62	theme	GalNAc	289:294	arg1	amounts					278:284	small amounts	272:284	small amounts of GalNAc	272:294	All pooled fractions containing carbohydrates showed the presence of small amounts of GalNAc in non-reducing position, besides free N-acetyllactosamine type of oligosaccharides as major constituents.
3371361	2	62	theme	GalNAc	289:294	arg1	GalNAc					289:294	GalNAc	289:294	GalNAc	289:294	All pooled fractions containing carbohydrates showed the presence of small amounts of GalNAc in non-reducing position, besides free N-acetyllactosamine type of oligosaccharides as major constituents.
3371361	2	63	theme	oligosaccharides	363:378	arg1	type					355:358	free N-acetyllactosamine type	330:358	free N-acetyllactosamine type of oligosaccharides as major constituents	330:400	All pooled fractions containing carbohydrates showed the presence of small amounts of GalNAc in non-reducing position, besides free N-acetyllactosamine type of oligosaccharides as major constituents.
3371361	7	64	attach	presence	1190:1197	arg2	chains					1221:1226	these carbohydrate chains	1202:1226	these carbohydrate chains	1202:1226	The presence of these carbohydrate chains in Bio-Gel fractions differing in molecular mass suggested that they are derived from glycopeptides which are heterogeneous in their peptide part.
3371361	7	64	attach	presence	1190:1197	arg1	fractions					1239:1247	Bio-Gel fractions	1231:1247	Bio-Gel fractions differing in molecular mass	1231:1275	The presence of these carbohydrate chains in Bio-Gel fractions differing in molecular mass suggested that they are derived from glycopeptides which are heterogeneous in their peptide part.
3371361	5	65	from	chromatography	806:819	arg1	Q.					829:830	Q.	829:830	Q.	829:830	Subsequently, the O-glycosidic sialyloligosaccharide-alditols were subfractionated by anion-exchange chromatography on Mono Q. Structural analysis by 500-MHz 1H-NMR spectroscopy revealed two major components in all fractions, namely: NeuAc alpha 2-3Gal beta 1-3GalNAc-ol and NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc-ol.
3371361	5	66	theme	alpha	1014:1018	arg1	GalNAc-ol					1024:1032	NeuAc alpha 2-3Gal beta 1-3GalNAc-ol and NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc-ol	939:1032	Mono Q. Structural analysis by 500-MHz 1H-NMR spectroscopy revealed two major components in all fractions, namely: NeuAc alpha 2-3Gal beta 1-3GalNAc-ol and NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc-ol	824:1032	Subsequently, the O-glycosidic sialyloligosaccharide-alditols were subfractionated by anion-exchange chromatography on Mono Q. Structural analysis by 500-MHz 1H-NMR spectroscopy revealed two major components in all fractions, namely: NeuAc alpha 2-3Gal beta 1-3GalNAc-ol and NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc-ol.
3371361	0	67	theme	urinary	88:94	arg1	glycopeptides					96:108	urinary glycopeptides	88:108	urinary glycopeptides of a sialidosis patient	88:132	Structural analysis of O-glycosidic type of sialyloligosaccharide-alditols derived from urinary glycopeptides of a sialidosis patient.
3371361	2	68	theme	pooled	207:212	arg1	fractions					214:222	All pooled fractions	203:222	All pooled fractions containing carbohydrates	203:247	All pooled fractions containing carbohydrates showed the presence of small amounts of GalNAc in non-reducing position, besides free N-acetyllactosamine type of oligosaccharides as major constituents.
3371361	2	69	theme	amounts	278:284	arg1	presence					260:267	the presence	256:267	the presence of small amounts of GalNAc in non-reducing position	256:319	All pooled fractions containing carbohydrates showed the presence of small amounts of GalNAc in non-reducing position, besides free N-acetyllactosamine type of oligosaccharides as major constituents.
3371361	5	70	theme	2-3Gal	951:956	arg1	1-3GalNAc-ol					963:974	NeuAc alpha 2-3Gal beta 1-3GalNAc-ol and NeuAc alpha 2-3Gal	939:997	1-3GalNAc-ol	963:974	Subsequently, the O-glycosidic sialyloligosaccharide-alditols were subfractionated by anion-exchange chromatography on Mono Q. Structural analysis by 500-MHz 1H-NMR spectroscopy revealed two major components in all fractions, namely: NeuAc alpha 2-3Gal beta 1-3GalNAc-ol and NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc-ol.
3371361	5	71	theme	1-3[NeuAc	1004:1012	arg1	GalNAc-ol					1024:1032	NeuAc alpha 2-3Gal beta 1-3GalNAc-ol and NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc-ol	939:1032	Mono Q. Structural analysis by 500-MHz 1H-NMR spectroscopy revealed two major components in all fractions, namely: NeuAc alpha 2-3Gal beta 1-3GalNAc-ol and NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc-ol	824:1032	Subsequently, the O-glycosidic sialyloligosaccharide-alditols were subfractionated by anion-exchange chromatography on Mono Q. Structural analysis by 500-MHz 1H-NMR spectroscopy revealed two major components in all fractions, namely: NeuAc alpha 2-3Gal beta 1-3GalNAc-ol and NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc-ol.
3371361	5	72	theme	alpha	986:990	arg1	2-3Gal					992:997	NeuAc alpha 2-3Gal beta 1-3GalNAc-ol and NeuAc alpha 2-3Gal	939:997	2-3Gal	992:997	Subsequently, the O-glycosidic sialyloligosaccharide-alditols were subfractionated by anion-exchange chromatography on Mono Q. Structural analysis by 500-MHz 1H-NMR spectroscopy revealed two major components in all fractions, namely: NeuAc alpha 2-3Gal beta 1-3GalNAc-ol and NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-6]GalNAc-ol.
3371361	6	73	theme	beta	1110:1113	arg1	component					1150:1158	a minor component	1142:1158	a minor component in some of the fractions	1142:1183	Furthermore, NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6]GalNAc-ol was found as a minor component in some of the fractions.
3371361	6	73	theme	beta	1110:1113	arg1	GalNAc-ol					1119:1127	NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6]GalNAc-ol	1048:1127	NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6]GalNAc-ol	1048:1127	Furthermore, NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6]GalNAc-ol was found as a minor component in some of the fractions.
3371361	2	74	theme	small	272:276	arg1	amounts					278:284	small amounts	272:284	small amounts of GalNAc	272:294	All pooled fractions containing carbohydrates showed the presence of small amounts of GalNAc in non-reducing position, besides free N-acetyllactosamine type of oligosaccharides as major constituents.
3371361	2	74	theme	small	272:276	arg1	GalNAc					289:294	GalNAc	289:294	GalNAc	289:294	All pooled fractions containing carbohydrates showed the presence of small amounts of GalNAc in non-reducing position, besides free N-acetyllactosamine type of oligosaccharides as major constituents.
3371361	1	75	theme	gel	172:174	arg1	filtration					176:185	gel filtration	172:185	gel filtration	172:185	Sialidosis urine was fractionated by gel filtration on Bio-Gel P-6.
3371361	6	76	theme	2-3Gal	1060:1065	arg1	beta					1110:1113	NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-3Gal beta 1-4GlcNAc beta	1048:1113	NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6]GalNAc-ol	1048:1127	Furthermore, NeuAc alpha 2-3Gal beta 1-3[NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6]GalNAc-ol was found as a minor component in some of the fractions.
3442598	0	0	theme	renal	79:83	arg1	insufficiency					85:97	chronic renal insufficiency	71:97	chronic renal insufficiency	71:97	[Sialic acid containing compounds in the hemofiltrate of patients with chronic renal insufficiency.
3442598	2	1	theme	structure	118:126	arg1	determination					128:140	structure determination	118:140	structure determination	118:140	Isolation and structure determination of sialoglycopeptides].
3442598	6	2	theme	compounds	745:753	arg1	origin					729:734	The origin	725:734	The origin of these compounds	725:753	The origin of these compounds and their possible clinical relevance is subject to further investigations.
3442598	6	2	theme	compounds	745:753	arg1	subject					796:802	subject	796:802	subject	796:802	The origin of these compounds and their possible clinical relevance is subject to further investigations.
3442598	6	2	theme	compounds	745:753	arg1	relevance					783:791	their possible clinical relevance	759:791	their possible clinical relevance	759:791	The origin of these compounds and their possible clinical relevance is subject to further investigations.
3442598	3	3	gly	glycopeptides	178:190	arg2	glycopeptides					178:190	Four sialyl glycopeptides	166:190	Four sialyl glycopeptides	166:190	Four sialyl glycopeptides have been isolated from the hemofiltrate of a patient with end stage renal disease using reverse osmosis, gel filtration and ion-exchange chromatography.
3442598	0	4	theme	chronic	71:77	arg1	insufficiency					85:97	chronic renal insufficiency	71:97	chronic renal insufficiency	71:97	[Sialic acid containing compounds in the hemofiltrate of patients with chronic renal insufficiency.
3442598	3	5	theme	patient	238:244	arg1	hemofiltrate					220:231	the hemofiltrate	216:231	the hemofiltrate of a patient with end stage renal disease	216:273	Four sialyl glycopeptides have been isolated from the hemofiltrate of a patient with end stage renal disease using reverse osmosis, gel filtration and ion-exchange chromatography.
3442598	4	6	theme	mass	425:428	arg1	spectrometry					430:441	FAB mass spectrometry	421:441	FAB mass spectrometry	421:441	Structural studies including one- and two-dimensional 1H-NMR spectroscopy, FAB mass spectrometry and enzymatic degradation indicated the following structures: (Formula: see text).
3442598	3	7	with	patient	238:244	arg1	disease					267:273	end stage renal disease	251:273	end stage renal disease	251:273	Four sialyl glycopeptides have been isolated from the hemofiltrate of a patient with end stage renal disease using reverse osmosis, gel filtration and ion-exchange chromatography.
3442598	5	8	attach	isolated	671:678	arg1	material					715:722	biological material	704:722	biological material	704:722	While the disialyl glycopeptide has been previously characterized from normal and pregnancy urine, the three other sialyl glycopeptides could be isolated for the first time from biological material.
3442598	5	8	attach	isolated	671:678	arg2	glycopeptides					648:660	the three other sialyl glycopeptides	625:660	the three other sialyl glycopeptides	625:660	While the disialyl glycopeptide has been previously characterized from normal and pregnancy urine, the three other sialyl glycopeptides could be isolated for the first time from biological material.
3442598	5	9	theme	pregnancy	608:616	arg1	urine					618:622	pregnancy urine	608:622	pregnancy urine	608:622	While the disialyl glycopeptide has been previously characterized from normal and pregnancy urine, the three other sialyl glycopeptides could be isolated for the first time from biological material.
3442598	5	10	theme	first	688:692	arg1	time					694:697	the first time	684:697	the first time	684:697	While the disialyl glycopeptide has been previously characterized from normal and pregnancy urine, the three other sialyl glycopeptides could be isolated for the first time from biological material.
3442598	4	11	theme	FAB	421:423	arg1	spectrometry					430:441	FAB mass spectrometry	421:441	FAB mass spectrometry	421:441	Structural studies including one- and two-dimensional 1H-NMR spectroscopy, FAB mass spectrometry and enzymatic degradation indicated the following structures: (Formula: see text).
3442598	4	12	dep	structures	493:502	arg1	see					515:517	see	515:517	see text	515:522	Structural studies including one- and two-dimensional 1H-NMR spectroscopy, FAB mass spectrometry and enzymatic degradation indicated the following structures: (Formula: see text).
3442598	6	13	theme	possible	765:772	arg1	relevance					783:791	their possible clinical relevance	759:791	their possible clinical relevance	759:791	The origin of these compounds and their possible clinical relevance is subject to further investigations.
3442598	5	14	theme	other	635:639	arg1	glycopeptides					648:660	the three other sialyl glycopeptides	625:660	the three other sialyl glycopeptides	625:660	While the disialyl glycopeptide has been previously characterized from normal and pregnancy urine, the three other sialyl glycopeptides could be isolated for the first time from biological material.
3442598	3	15	theme	stage	255:259	arg1	disease					267:273	end stage renal disease	251:273	end stage renal disease	251:273	Four sialyl glycopeptides have been isolated from the hemofiltrate of a patient with end stage renal disease using reverse osmosis, gel filtration and ion-exchange chromatography.
3442598	3	16	theme	sialyl	171:176	arg1	glycopeptides					178:190	Four sialyl glycopeptides	166:190	Four sialyl glycopeptides	166:190	Four sialyl glycopeptides have been isolated from the hemofiltrate of a patient with end stage renal disease using reverse osmosis, gel filtration and ion-exchange chromatography.
3442598	2	17	theme	sialoglycopeptides	145:162	arg1	Isolation					104:112	Isolation	104:112	Isolation	104:112	Isolation and structure determination of sialoglycopeptides].
3442598	2	17	theme	sialoglycopeptides	145:162	arg1	determination					128:140	structure determination	118:140	structure determination	118:140	Isolation and structure determination of sialoglycopeptides].
3442598	3	18	theme	renal	261:265	arg1	disease					267:273	end stage renal disease	251:273	end stage renal disease	251:273	Four sialyl glycopeptides have been isolated from the hemofiltrate of a patient with end stage renal disease using reverse osmosis, gel filtration and ion-exchange chromatography.
3442598	4	19	theme	1H-NMR	400:405	arg1	spectroscopy					407:418	one- and two-dimensional 1H-NMR spectroscopy	375:418	one- and two-dimensional 1H-NMR spectroscopy	375:418	Structural studies including one- and two-dimensional 1H-NMR spectroscopy, FAB mass spectrometry and enzymatic degradation indicated the following structures: (Formula: see text).
3442598	4	20	theme	two-dimensional	384:398	arg1	spectroscopy					407:418	one- and two-dimensional 1H-NMR spectroscopy	375:418	one- and two-dimensional 1H-NMR spectroscopy	375:418	Structural studies including one- and two-dimensional 1H-NMR spectroscopy, FAB mass spectrometry and enzymatic degradation indicated the following structures: (Formula: see text).
3442598	2	21	gly	sialoglycopeptides	145:162	arg2	sialoglycopeptides					145:162	sialoglycopeptides	145:162	sialoglycopeptides	145:162	Isolation and structure determination of sialoglycopeptides].
3442598	3	22	attach	isolated	202:209	arg1	hemofiltrate					220:231	the hemofiltrate	216:231	the hemofiltrate of a patient with end stage renal disease	216:273	Four sialyl glycopeptides have been isolated from the hemofiltrate of a patient with end stage renal disease using reverse osmosis, gel filtration and ion-exchange chromatography.
3442598	3	22	attach	isolated	202:209	arg2	glycopeptides					178:190	Four sialyl glycopeptides	166:190	Four sialyl glycopeptides	166:190	Four sialyl glycopeptides have been isolated from the hemofiltrate of a patient with end stage renal disease using reverse osmosis, gel filtration and ion-exchange chromatography.
3442598	0	23	theme	[Sialic	0:6	arg1	acid					8:11	[Sialic acid	0:11	[Sialic acid	0:11	[Sialic acid containing compounds in the hemofiltrate of patients with chronic renal insufficiency.
3442598	3	24	theme	end	251:253	arg1	disease					267:273	end stage renal disease	251:273	end stage renal disease	251:273	Four sialyl glycopeptides have been isolated from the hemofiltrate of a patient with end stage renal disease using reverse osmosis, gel filtration and ion-exchange chromatography.
3442598	5	25	theme	sialyl	641:646	arg1	glycopeptides					648:660	the three other sialyl glycopeptides	625:660	the three other sialyl glycopeptides	625:660	While the disialyl glycopeptide has been previously characterized from normal and pregnancy urine, the three other sialyl glycopeptides could be isolated for the first time from biological material.
3442598	4	26	dep	see	515:517	arg1	Formula					506:512	Formula	506:512	Formula	506:512	Structural studies including one- and two-dimensional 1H-NMR spectroscopy, FAB mass spectrometry and enzymatic degradation indicated the following structures: (Formula: see text).
3442598	3	27	theme	reverse	281:287	arg1	osmosis					289:295	reverse osmosis	281:295	reverse osmosis	281:295	Four sialyl glycopeptides have been isolated from the hemofiltrate of a patient with end stage renal disease using reverse osmosis, gel filtration and ion-exchange chromatography.
3442598	0	28	with	patients	57:64	arg1	insufficiency					85:97	chronic renal insufficiency	71:97	chronic renal insufficiency	71:97	[Sialic acid containing compounds in the hemofiltrate of patients with chronic renal insufficiency.
3442598	6	29	theme	further	807:813	arg1	investigations					815:828	further investigations	807:828	further investigations	807:828	The origin of these compounds and their possible clinical relevance is subject to further investigations.
3442598	5	30	gly	glycopeptides	648:660	arg2	glycopeptides					648:660	the three other sialyl glycopeptides	625:660	the three other sialyl glycopeptides	625:660	While the disialyl glycopeptide has been previously characterized from normal and pregnancy urine, the three other sialyl glycopeptides could be isolated for the first time from biological material.
3442598	4	31	theme	following	483:491	arg1	structures					493:502	the following structures	479:502	the following structures: (Formula: see text)	479:523	Structural studies including one- and two-dimensional 1H-NMR spectroscopy, FAB mass spectrometry and enzymatic degradation indicated the following structures: (Formula: see text).
3442598	6	32	theme	clinical	774:781	arg1	relevance					783:791	their possible clinical relevance	759:791	their possible clinical relevance	759:791	The origin of these compounds and their possible clinical relevance is subject to further investigations.
3442598	5	33	gly	glycopeptide	545:556	arg2	glycopeptide					545:556	the disialyl glycopeptide	532:556	the disialyl glycopeptide	532:556	While the disialyl glycopeptide has been previously characterized from normal and pregnancy urine, the three other sialyl glycopeptides could be isolated for the first time from biological material.
3442598	3	34	theme	ion-exchange	317:328	arg1	chromatography					330:343	ion-exchange chromatography	317:343	ion-exchange chromatography	317:343	Four sialyl glycopeptides have been isolated from the hemofiltrate of a patient with end stage renal disease using reverse osmosis, gel filtration and ion-exchange chromatography.
3442598	5	35	theme	biological	704:713	arg1	material					715:722	biological material	704:722	biological material	704:722	While the disialyl glycopeptide has been previously characterized from normal and pregnancy urine, the three other sialyl glycopeptides could be isolated for the first time from biological material.
3442598	4	36	theme	enzymatic	447:455	arg1	degradation					457:467	enzymatic degradation	447:467	enzymatic degradation	447:467	Structural studies including one- and two-dimensional 1H-NMR spectroscopy, FAB mass spectrometry and enzymatic degradation indicated the following structures: (Formula: see text).
3442598	4	37	theme	one-	375:378	arg1	spectroscopy					407:418	one- and two-dimensional 1H-NMR spectroscopy	375:418	one- and two-dimensional 1H-NMR spectroscopy	375:418	Structural studies including one- and two-dimensional 1H-NMR spectroscopy, FAB mass spectrometry and enzymatic degradation indicated the following structures: (Formula: see text).
3442598	3	38	theme	gel	298:300	arg1	filtration					302:311	gel filtration	298:311	gel filtration	298:311	Four sialyl glycopeptides have been isolated from the hemofiltrate of a patient with end stage renal disease using reverse osmosis, gel filtration and ion-exchange chromatography.
3442598	5	39	theme	disialyl	536:543	arg1	glycopeptide					545:556	the disialyl glycopeptide	532:556	the disialyl glycopeptide	532:556	While the disialyl glycopeptide has been previously characterized from normal and pregnancy urine, the three other sialyl glycopeptides could be isolated for the first time from biological material.
3442598	0	40	theme	patients	57:64	arg1	hemofiltrate					41:52	the hemofiltrate	37:52	the hemofiltrate of patients with chronic renal insufficiency	37:97	[Sialic acid containing compounds in the hemofiltrate of patients with chronic renal insufficiency.
3442598	4	41	theme	Structural	346:355	arg1	spectroscopy					407:418	one- and two-dimensional 1H-NMR spectroscopy	375:418	one- and two-dimensional 1H-NMR spectroscopy	375:418	Structural studies including one- and two-dimensional 1H-NMR spectroscopy, FAB mass spectrometry and enzymatic degradation indicated the following structures: (Formula: see text).
3442598	4	41	theme	Structural	346:355	arg1	spectrometry					430:441	FAB mass spectrometry	421:441	FAB mass spectrometry	421:441	Structural studies including one- and two-dimensional 1H-NMR spectroscopy, FAB mass spectrometry and enzymatic degradation indicated the following structures: (Formula: see text).
3442598	4	41	theme	Structural	346:355	arg1	degradation					457:467	enzymatic degradation	447:467	enzymatic degradation	447:467	Structural studies including one- and two-dimensional 1H-NMR spectroscopy, FAB mass spectrometry and enzymatic degradation indicated the following structures: (Formula: see text).
3442598	4	41	theme	Structural	346:355	arg1	studies					357:363	Structural studies	346:363	Structural studies including one- and two-dimensional 1H-NMR spectroscopy, FAB mass spectrometry and enzymatic degradation	346:467	Structural studies including one- and two-dimensional 1H-NMR spectroscopy, FAB mass spectrometry and enzymatic degradation indicated the following structures: (Formula: see text).
3003076	4	0	theme	Redfield	852:859	arg1	sequence					877:884	the Redfield selective pulse sequence	848:884	the Redfield selective pulse sequence in H2O	848:891	The resonances of exchangeable amide protons, observed by the Redfield selective pulse sequence in H2O, were assigned by decoupling to the resonances of H2 of the 2-acetamido sugars.
3003076	0	1	theme	field	162:166	arg1	spectroscopy					175:186	high field 1H NMR spectroscopy	157:186	high field 1H NMR spectroscopy	157:186	Characterization of the oligosaccharide alditols from ovarian cyst mucin glycoproteins of blood group A using high pressure liquid chromatography (HPLC) and high field 1H NMR spectroscopy.
3003076	1	2	theme	high	237:240	arg1	chromatography					258:271	normal phase high pressure liquid chromatography	224:271	normal phase high pressure liquid chromatography	224:271	A combination of reverse phase and normal phase high pressure liquid chromatography has been used to separate the reduced oligosaccharides produced by alkaline borohydride degradation of a blood group A ovarian cyst mucin glycoproteins.
3003076	4	3	theme	pulse	871:875	arg1	sequence					877:884	the Redfield selective pulse sequence	848:884	the Redfield selective pulse sequence in H2O	848:891	The resonances of exchangeable amide protons, observed by the Redfield selective pulse sequence in H2O, were assigned by decoupling to the resonances of H2 of the 2-acetamido sugars.
3003076	8	4	gly	glycopeptides	1822:1834	arg2	glycopeptides					1822:1834	glycopeptides	1822:1834	glycopeptides	1822:1834	These oligosaccharides, which terminate with beta-Gal, alpha-Fuc, beta-GlcNAc, and alpha-GalNAc, account for 75% of the total glycoprotein carbohydrate, the remainder being isolated as a mixture of glycopeptides and a high molecular weight polysaccharide whose NMR spectrum implies a simple repeating subunit structure closely related to that of the oligosaccharides.
3003076	3	5	theme	structures	708:717	arg1	purity					675:680	The purity	671:680	The purity of the products and their structures	671:717	The purity of the products and their structures were determined from the fully assigned high field proton NMR spectra.
3003076	0	6	theme	NMR	171:173	arg1	spectroscopy					175:186	high field 1H NMR spectroscopy	157:186	high field 1H NMR spectroscopy	157:186	Characterization of the oligosaccharide alditols from ovarian cyst mucin glycoproteins of blood group A using high pressure liquid chromatography (HPLC) and high field 1H NMR spectroscopy.
3003076	1	7	theme	liquid	251:256	arg1	chromatography					258:271	normal phase high pressure liquid chromatography	224:271	normal phase high pressure liquid chromatography	224:271	A combination of reverse phase and normal phase high pressure liquid chromatography has been used to separate the reduced oligosaccharides produced by alkaline borohydride degradation of a blood group A ovarian cyst mucin glycoproteins.
3003076	2	8	theme	normal	617:622	arg1	column					630:635	a MicroPak AX-5 normal phase column	601:635	a MicroPak AX-5 normal phase column eluted with aqueous acetonitrile	601:668	Fourteen compounds, ranging in size from a monosaccharide to a decasaccharide, have been isolated preparatively using a Zorbax C-18 reverse phase column eluted with water and a MicroPak AX-5 normal phase column eluted with aqueous acetonitrile.
3003076	6	9	attach	attached	1234:1241	arg1	carbon					1259:1264	the aglycone carbon	1246:1264	the aglycone carbon	1246:1264	In exception to earlier proposals that nuclear Overhauser effect on irradiation of the anomeric proton should always be observed at the proton attached to the aglycone carbon, we find that for the linkage of GalNAcp(1----3)Gal, nuclear Overhauser effect on irradiation of the alpha-anomeric proton resonance is observed not at H3 but at H4 of galactose.
3003076	6	9	attach	attached	1234:1241	arg2	proton					1227:1232	the proton	1223:1232	the proton attached to the aglycone carbon	1223:1264	In exception to earlier proposals that nuclear Overhauser effect on irradiation of the anomeric proton should always be observed at the proton attached to the aglycone carbon, we find that for the linkage of GalNAcp(1----3)Gal, nuclear Overhauser effect on irradiation of the alpha-anomeric proton resonance is observed not at H3 but at H4 of galactose.
3003076	6	10	dep	proposals	1115:1123	arg1	exception					1094:1102	exception	1094:1102	exception	1094:1102	In exception to earlier proposals that nuclear Overhauser effect on irradiation of the anomeric proton should always be observed at the proton attached to the aglycone carbon, we find that for the linkage of GalNAcp(1----3)Gal, nuclear Overhauser effect on irradiation of the alpha-anomeric proton resonance is observed not at H3 but at H4 of galactose.
3003076	8	11	theme	related	1951:1957	arg1	structure					1933:1941	a simple repeating subunit structure	1906:1941	a simple repeating subunit structure closely related to that of the oligosaccharides	1906:1989	These oligosaccharides, which terminate with beta-Gal, alpha-Fuc, beta-GlcNAc, and alpha-GalNAc, account for 75% of the total glycoprotein carbohydrate, the remainder being isolated as a mixture of glycopeptides and a high molecular weight polysaccharide whose NMR spectrum implies a simple repeating subunit structure closely related to that of the oligosaccharides.
3003076	2	12	theme	MicroPak	603:610	arg1	column					630:635	a MicroPak AX-5 normal phase column	601:635	a MicroPak AX-5 normal phase column eluted with aqueous acetonitrile	601:668	Fourteen compounds, ranging in size from a monosaccharide to a decasaccharide, have been isolated preparatively using a Zorbax C-18 reverse phase column eluted with water and a MicroPak AX-5 normal phase column eluted with aqueous acetonitrile.
3003076	6	13	theme	nuclear	1130:1136	arg1	effect					1149:1154	nuclear Overhauser effect	1130:1154	nuclear Overhauser effect on irradiation of the anomeric proton	1130:1192	In exception to earlier proposals that nuclear Overhauser effect on irradiation of the anomeric proton should always be observed at the proton attached to the aglycone carbon, we find that for the linkage of GalNAcp(1----3)Gal, nuclear Overhauser effect on irradiation of the alpha-anomeric proton resonance is observed not at H3 but at H4 of galactose.
3003076	6	14	theme	aglycone	1250:1257	arg1	carbon					1259:1264	the aglycone carbon	1246:1264	the aglycone carbon	1246:1264	In exception to earlier proposals that nuclear Overhauser effect on irradiation of the anomeric proton should always be observed at the proton attached to the aglycone carbon, we find that for the linkage of GalNAcp(1----3)Gal, nuclear Overhauser effect on irradiation of the alpha-anomeric proton resonance is observed not at H3 but at H4 of galactose.
3003076	2	15	theme	Zorbax	546:551	arg1	column					572:577	a Zorbax C-18 reverse phase column	544:577	a Zorbax C-18 reverse phase column eluted with water	544:595	Fourteen compounds, ranging in size from a monosaccharide to a decasaccharide, have been isolated preparatively using a Zorbax C-18 reverse phase column eluted with water and a MicroPak AX-5 normal phase column eluted with aqueous acetonitrile.
3003076	0	16	theme	pressure	115:122	arg1	chromatography					131:144	high pressure liquid chromatography	110:144	high pressure liquid chromatography (HPLC)	110:151	Characterization of the oligosaccharide alditols from ovarian cyst mucin glycoproteins of blood group A using high pressure liquid chromatography (HPLC) and high field 1H NMR spectroscopy.
3003076	0	16	theme	pressure	115:122	arg1	HPLC					147:150	HPLC	147:150	HPLC	147:150	Characterization of the oligosaccharide alditols from ovarian cyst mucin glycoproteins of blood group A using high pressure liquid chromatography (HPLC) and high field 1H NMR spectroscopy.
3003076	1	17	theme	blood	378:382	arg1	A					390:390	a blood group A	376:390	a blood group A ovarian cyst mucin glycoproteins	376:423	A combination of reverse phase and normal phase high pressure liquid chromatography has been used to separate the reduced oligosaccharides produced by alkaline borohydride degradation of a blood group A ovarian cyst mucin glycoproteins.
3003076	6	18	theme	galactose	1434:1442	arg1	H4					1428:1429	H4	1428:1429	H4 of galactose	1428:1442	In exception to earlier proposals that nuclear Overhauser effect on irradiation of the anomeric proton should always be observed at the proton attached to the aglycone carbon, we find that for the linkage of GalNAcp(1----3)Gal, nuclear Overhauser effect on irradiation of the alpha-anomeric proton resonance is observed not at H3 but at H4 of galactose.
3003076	3	19	theme	field	764:768	arg1	spectra					781:787	the fully assigned high field proton NMR spectra	740:787	the fully assigned high field proton NMR spectra	740:787	The purity of the products and their structures were determined from the fully assigned high field proton NMR spectra.
3003076	8	20	theme	high	1842:1845	arg1	polysaccharide					1864:1877	a high molecular weight polysaccharide	1840:1877	a high molecular weight polysaccharide whose NMR spectrum implies a simple repeating subunit structure closely related to that of the oligosaccharides	1840:1989	These oligosaccharides, which terminate with beta-Gal, alpha-Fuc, beta-GlcNAc, and alpha-GalNAc, account for 75% of the total glycoprotein carbohydrate, the remainder being isolated as a mixture of glycopeptides and a high molecular weight polysaccharide whose NMR spectrum implies a simple repeating subunit structure closely related to that of the oligosaccharides.
3003076	5	21	theme	protons	1056:1062	arg1	relationship					1027:1038	the relationship	1023:1038	the relationship of the anomeric protons	1023:1062	Nuclear Overhauser effects were used to establish the relationship of the anomeric protons and those of the aglycone.
3003076	6	22	theme	alpha-anomeric	1367:1380	arg1	resonance					1389:1397	the alpha-anomeric proton resonance	1363:1397	the alpha-anomeric proton resonance	1363:1397	In exception to earlier proposals that nuclear Overhauser effect on irradiation of the anomeric proton should always be observed at the proton attached to the aglycone carbon, we find that for the linkage of GalNAcp(1----3)Gal, nuclear Overhauser effect on irradiation of the alpha-anomeric proton resonance is observed not at H3 but at H4 of galactose.
3003076	7	23	theme	different	1547:1555	arg1	oligosaccharides					1557:1572	13 different oligosaccharides	1544:1572	13 different oligosaccharides of which seven have not previously been reported	1544:1621	A combination of NMR methods and enzymatic degradation was employed to determine the structures of 13 different oligosaccharides of which seven have not previously been reported.
3003076	8	24	theme	NMR	1885:1887	arg1	spectrum					1889:1896	spectrum	1889:1896	spectrum	1889:1896	These oligosaccharides, which terminate with beta-Gal, alpha-Fuc, beta-GlcNAc, and alpha-GalNAc, account for 75% of the total glycoprotein carbohydrate, the remainder being isolated as a mixture of glycopeptides and a high molecular weight polysaccharide whose NMR spectrum implies a simple repeating subunit structure closely related to that of the oligosaccharides.
3003076	3	25	theme	assigned	750:757	arg1	spectra					781:787	the fully assigned high field proton NMR spectra	740:787	the fully assigned high field proton NMR spectra	740:787	The purity of the products and their structures were determined from the fully assigned high field proton NMR spectra.
3003076	8	26	theme	weight	1857:1862	arg1	polysaccharide					1864:1877	a high molecular weight polysaccharide	1840:1877	a high molecular weight polysaccharide whose NMR spectrum implies a simple repeating subunit structure closely related to that of the oligosaccharides	1840:1989	These oligosaccharides, which terminate with beta-Gal, alpha-Fuc, beta-GlcNAc, and alpha-GalNAc, account for 75% of the total glycoprotein carbohydrate, the remainder being isolated as a mixture of glycopeptides and a high molecular weight polysaccharide whose NMR spectrum implies a simple repeating subunit structure closely related to that of the oligosaccharides.
3003076	1	27	theme	cyst	400:403	arg1	glycoproteins					411:423	a blood group A ovarian cyst mucin glycoproteins	376:423	a blood group A ovarian cyst mucin glycoproteins	376:423	A combination of reverse phase and normal phase high pressure liquid chromatography has been used to separate the reduced oligosaccharides produced by alkaline borohydride degradation of a blood group A ovarian cyst mucin glycoproteins.
3003076	6	28	from	effect	1338:1343	arg1	irradiation					1348:1358	irradiation	1348:1358	irradiation	1348:1358	In exception to earlier proposals that nuclear Overhauser effect on irradiation of the anomeric proton should always be observed at the proton attached to the aglycone carbon, we find that for the linkage of GalNAcp(1----3)Gal, nuclear Overhauser effect on irradiation of the alpha-anomeric proton resonance is observed not at H3 but at H4 of galactose.
3003076	2	29	theme	reverse	558:564	arg1	column					572:577	a Zorbax C-18 reverse phase column	544:577	a Zorbax C-18 reverse phase column eluted with water	544:595	Fourteen compounds, ranging in size from a monosaccharide to a decasaccharide, have been isolated preparatively using a Zorbax C-18 reverse phase column eluted with water and a MicroPak AX-5 normal phase column eluted with aqueous acetonitrile.
3003076	6	30	theme	proton	1187:1192	arg1	effect					1149:1154	nuclear Overhauser effect	1130:1154	nuclear Overhauser effect on irradiation of the anomeric proton	1130:1192	In exception to earlier proposals that nuclear Overhauser effect on irradiation of the anomeric proton should always be observed at the proton attached to the aglycone carbon, we find that for the linkage of GalNAcp(1----3)Gal, nuclear Overhauser effect on irradiation of the alpha-anomeric proton resonance is observed not at H3 but at H4 of galactose.
3003076	1	31	theme	glycoproteins	411:423	arg1	degradation					361:371	alkaline borohydride degradation	340:371	alkaline borohydride degradation of a blood group A ovarian cyst mucin glycoproteins	340:423	A combination of reverse phase and normal phase high pressure liquid chromatography has been used to separate the reduced oligosaccharides produced by alkaline borohydride degradation of a blood group A ovarian cyst mucin glycoproteins.
3003076	3	32	theme	NMR	777:779	arg1	spectra					781:787	the fully assigned high field proton NMR spectra	740:787	the fully assigned high field proton NMR spectra	740:787	The purity of the products and their structures were determined from the fully assigned high field proton NMR spectra.
3003076	6	33	theme	nuclear	1319:1325	arg1	effect					1338:1343	nuclear Overhauser effect	1319:1343	nuclear Overhauser effect on irradiation of the alpha-anomeric proton resonance	1319:1397	In exception to earlier proposals that nuclear Overhauser effect on irradiation of the anomeric proton should always be observed at the proton attached to the aglycone carbon, we find that for the linkage of GalNAcp(1----3)Gal, nuclear Overhauser effect on irradiation of the alpha-anomeric proton resonance is observed not at H3 but at H4 of galactose.
3003076	4	34	theme	2-acetamido	953:963	arg1	sugars					965:970	the 2-acetamido sugars	949:970	the 2-acetamido sugars	949:970	The resonances of exchangeable amide protons, observed by the Redfield selective pulse sequence in H2O, were assigned by decoupling to the resonances of H2 of the 2-acetamido sugars.
3003076	6	35	theme	Gal	1314:1316	arg1	linkage					1288:1294	the linkage	1284:1294	the linkage of GalNAcp(1----3)Gal	1284:1316	In exception to earlier proposals that nuclear Overhauser effect on irradiation of the anomeric proton should always be observed at the proton attached to the aglycone carbon, we find that for the linkage of GalNAcp(1----3)Gal, nuclear Overhauser effect on irradiation of the alpha-anomeric proton resonance is observed not at H3 but at H4 of galactose.
3003076	0	36	theme	group	96:100	arg1	A					102:102	blood group A	90:102	blood group A using high pressure liquid chromatography (HPLC) and high field 1H NMR spectroscopy	90:186	Characterization of the oligosaccharide alditols from ovarian cyst mucin glycoproteins of blood group A using high pressure liquid chromatography (HPLC) and high field 1H NMR spectroscopy.
3003076	1	37	theme	borohydride	349:359	arg1	degradation					361:371	alkaline borohydride degradation	340:371	alkaline borohydride degradation of a blood group A ovarian cyst mucin glycoproteins	340:423	A combination of reverse phase and normal phase high pressure liquid chromatography has been used to separate the reduced oligosaccharides produced by alkaline borohydride degradation of a blood group A ovarian cyst mucin glycoproteins.
3003076	8	38	theme	total	1744:1748	arg1	carbohydrate					1763:1774	the total glycoprotein carbohydrate	1740:1774	the total glycoprotein carbohydrate	1740:1774	These oligosaccharides, which terminate with beta-Gal, alpha-Fuc, beta-GlcNAc, and alpha-GalNAc, account for 75% of the total glycoprotein carbohydrate, the remainder being isolated as a mixture of glycopeptides and a high molecular weight polysaccharide whose NMR spectrum implies a simple repeating subunit structure closely related to that of the oligosaccharides.
3003076	8	38	theme	total	1744:1748	arg1	remainder					1781:1789	the remainder	1777:1789	the remainder being isolated as a mixture of glycopeptides and a high molecular weight polysaccharide whose NMR spectrum implies a simple repeating subunit structure closely related to that of the oligosaccharides	1777:1989	These oligosaccharides, which terminate with beta-Gal, alpha-Fuc, beta-GlcNAc, and alpha-GalNAc, account for 75% of the total glycoprotein carbohydrate, the remainder being isolated as a mixture of glycopeptides and a high molecular weight polysaccharide whose NMR spectrum implies a simple repeating subunit structure closely related to that of the oligosaccharides.
3003076	0	39	gly	glycoproteins	73:85	arg1	glycoproteins					73:85	ovarian cyst mucin glycoproteins	54:85	ovarian cyst mucin glycoproteins of blood group A using high pressure liquid chromatography (HPLC) and high field 1H NMR spectroscopy	54:186	Characterization of the oligosaccharide alditols from ovarian cyst mucin glycoproteins of blood group A using high pressure liquid chromatography (HPLC) and high field 1H NMR spectroscopy.
3003076	7	40	theme	enzymatic	1478:1486	arg1	degradation					1488:1498	enzymatic degradation	1478:1498	enzymatic degradation	1478:1498	A combination of NMR methods and enzymatic degradation was employed to determine the structures of 13 different oligosaccharides of which seven have not previously been reported.
3003076	2	41	theme	phase	624:628	arg1	column					630:635	a MicroPak AX-5 normal phase column	601:635	a MicroPak AX-5 normal phase column eluted with aqueous acetonitrile	601:668	Fourteen compounds, ranging in size from a monosaccharide to a decasaccharide, have been isolated preparatively using a Zorbax C-18 reverse phase column eluted with water and a MicroPak AX-5 normal phase column eluted with aqueous acetonitrile.
3003076	6	42	theme	GalNAcp	1299:1305	arg1	Gal					1314:1316	GalNAcp(1----3)Gal	1299:1316	GalNAcp(1----3)Gal	1299:1316	In exception to earlier proposals that nuclear Overhauser effect on irradiation of the anomeric proton should always be observed at the proton attached to the aglycone carbon, we find that for the linkage of GalNAcp(1----3)Gal, nuclear Overhauser effect on irradiation of the alpha-anomeric proton resonance is observed not at H3 but at H4 of galactose.
3003076	8	43	theme	carbohydrate	1763:1774	arg1	carbohydrate					1763:1774	the total glycoprotein carbohydrate	1740:1774	the total glycoprotein carbohydrate	1740:1774	These oligosaccharides, which terminate with beta-Gal, alpha-Fuc, beta-GlcNAc, and alpha-GalNAc, account for 75% of the total glycoprotein carbohydrate, the remainder being isolated as a mixture of glycopeptides and a high molecular weight polysaccharide whose NMR spectrum implies a simple repeating subunit structure closely related to that of the oligosaccharides.
3003076	8	43	theme	carbohydrate	1763:1774	arg1	%					1735:1735	75%	1733:1735	75% of the total glycoprotein carbohydrate, the remainder being isolated as a mixture of glycopeptides and a high molecular weight polysaccharide whose NMR spectrum implies a simple repeating subunit structure closely related to that of the oligosaccharides	1733:1989	These oligosaccharides, which terminate with beta-Gal, alpha-Fuc, beta-GlcNAc, and alpha-GalNAc, account for 75% of the total glycoprotein carbohydrate, the remainder being isolated as a mixture of glycopeptides and a high molecular weight polysaccharide whose NMR spectrum implies a simple repeating subunit structure closely related to that of the oligosaccharides.
3003076	8	43	theme	carbohydrate	1763:1774	arg1	remainder					1781:1789	the remainder	1777:1789	the remainder being isolated as a mixture of glycopeptides and a high molecular weight polysaccharide whose NMR spectrum implies a simple repeating subunit structure closely related to that of the oligosaccharides	1777:1989	These oligosaccharides, which terminate with beta-Gal, alpha-Fuc, beta-GlcNAc, and alpha-GalNAc, account for 75% of the total glycoprotein carbohydrate, the remainder being isolated as a mixture of glycopeptides and a high molecular weight polysaccharide whose NMR spectrum implies a simple repeating subunit structure closely related to that of the oligosaccharides.
3003076	6	44	theme	proton	1382:1387	arg1	resonance					1389:1397	the alpha-anomeric proton resonance	1363:1397	the alpha-anomeric proton resonance	1363:1397	In exception to earlier proposals that nuclear Overhauser effect on irradiation of the anomeric proton should always be observed at the proton attached to the aglycone carbon, we find that for the linkage of GalNAcp(1----3)Gal, nuclear Overhauser effect on irradiation of the alpha-anomeric proton resonance is observed not at H3 but at H4 of galactose.
3003076	2	45	theme	aqueous	649:655	arg1	acetonitrile					657:668	aqueous acetonitrile	649:668	aqueous acetonitrile	649:668	Fourteen compounds, ranging in size from a monosaccharide to a decasaccharide, have been isolated preparatively using a Zorbax C-18 reverse phase column eluted with water and a MicroPak AX-5 normal phase column eluted with aqueous acetonitrile.
3003076	7	46	theme	NMR	1462:1464	arg1	methods					1466:1472	NMR methods	1462:1472	NMR methods	1462:1472	A combination of NMR methods and enzymatic degradation was employed to determine the structures of 13 different oligosaccharides of which seven have not previously been reported.
3003076	8	47	gly	glycoprotein	1750:1761	arg1	glycoprotein					1750:1761	the total glycoprotein carbohydrate	1740:1774	the total glycoprotein carbohydrate	1740:1774	These oligosaccharides, which terminate with beta-Gal, alpha-Fuc, beta-GlcNAc, and alpha-GalNAc, account for 75% of the total glycoprotein carbohydrate, the remainder being isolated as a mixture of glycopeptides and a high molecular weight polysaccharide whose NMR spectrum implies a simple repeating subunit structure closely related to that of the oligosaccharides.
3003076	0	48	theme	alditols	40:47	arg1	Characterization					0:15	Characterization	0:15	Characterization of the oligosaccharide alditols from ovarian cyst mucin glycoproteins of blood group A using high pressure liquid chromatography (HPLC) and high field 1H NMR spectroscopy.	0:187	Characterization of the oligosaccharide alditols from ovarian cyst mucin glycoproteins of blood group A using high pressure liquid chromatography (HPLC) and high field 1H NMR spectroscopy.
3003076	6	49	located	observed	1402:1409	arg2	effect					1338:1343	nuclear Overhauser effect	1319:1343	nuclear Overhauser effect on irradiation of the alpha-anomeric proton resonance	1319:1397	In exception to earlier proposals that nuclear Overhauser effect on irradiation of the anomeric proton should always be observed at the proton attached to the aglycone carbon, we find that for the linkage of GalNAcp(1----3)Gal, nuclear Overhauser effect on irradiation of the alpha-anomeric proton resonance is observed not at H3 but at H4 of galactose.
3003076	6	49	located	observed	1402:1409	arg1	H3					1418:1419	H3	1418:1419	H3	1418:1419	In exception to earlier proposals that nuclear Overhauser effect on irradiation of the anomeric proton should always be observed at the proton attached to the aglycone carbon, we find that for the linkage of GalNAcp(1----3)Gal, nuclear Overhauser effect on irradiation of the alpha-anomeric proton resonance is observed not at H3 but at H4 of galactose.
3003076	6	50	located	observed	1211:1218	arg1	proton					1227:1232	the proton	1223:1232	the proton attached to the aglycone carbon	1223:1264	In exception to earlier proposals that nuclear Overhauser effect on irradiation of the anomeric proton should always be observed at the proton attached to the aglycone carbon, we find that for the linkage of GalNAcp(1----3)Gal, nuclear Overhauser effect on irradiation of the alpha-anomeric proton resonance is observed not at H3 but at H4 of galactose.
3003076	6	50	located	observed	1211:1218	arg2	effect					1149:1154	nuclear Overhauser effect	1130:1154	nuclear Overhauser effect on irradiation of the anomeric proton	1130:1192	In exception to earlier proposals that nuclear Overhauser effect on irradiation of the anomeric proton should always be observed at the proton attached to the aglycone carbon, we find that for the linkage of GalNAcp(1----3)Gal, nuclear Overhauser effect on irradiation of the alpha-anomeric proton resonance is observed not at H3 but at H4 of galactose.
3003076	0	51	theme	mucin	67:71	arg1	glycoproteins					73:85	ovarian cyst mucin glycoproteins	54:85	ovarian cyst mucin glycoproteins of blood group A using high pressure liquid chromatography (HPLC) and high field 1H NMR spectroscopy	54:186	Characterization of the oligosaccharide alditols from ovarian cyst mucin glycoproteins of blood group A using high pressure liquid chromatography (HPLC) and high field 1H NMR spectroscopy.
3003076	4	52	theme	amide	821:825	arg1	protons					827:833	exchangeable amide protons	808:833	exchangeable amide protons	808:833	The resonances of exchangeable amide protons, observed by the Redfield selective pulse sequence in H2O, were assigned by decoupling to the resonances of H2 of the 2-acetamido sugars.
3003076	0	53	theme	ovarian	54:60	arg1	glycoproteins					73:85	ovarian cyst mucin glycoproteins	54:85	ovarian cyst mucin glycoproteins of blood group A using high pressure liquid chromatography (HPLC) and high field 1H NMR spectroscopy	54:186	Characterization of the oligosaccharide alditols from ovarian cyst mucin glycoproteins of blood group A using high pressure liquid chromatography (HPLC) and high field 1H NMR spectroscopy.
3003076	2	54	theme	AX-5	612:615	arg1	column					630:635	a MicroPak AX-5 normal phase column	601:635	a MicroPak AX-5 normal phase column eluted with aqueous acetonitrile	601:668	Fourteen compounds, ranging in size from a monosaccharide to a decasaccharide, have been isolated preparatively using a Zorbax C-18 reverse phase column eluted with water and a MicroPak AX-5 normal phase column eluted with aqueous acetonitrile.
3003076	1	55	theme	reverse	206:212	arg1	phase					214:218	reverse phase	206:218	reverse phase	206:218	A combination of reverse phase and normal phase high pressure liquid chromatography has been used to separate the reduced oligosaccharides produced by alkaline borohydride degradation of a blood group A ovarian cyst mucin glycoproteins.
3003076	5	56	theme	Overhauser	981:990	arg1	effects					992:998	Nuclear Overhauser effects	973:998	Nuclear Overhauser effects	973:998	Nuclear Overhauser effects were used to establish the relationship of the anomeric protons and those of the aglycone.
3003076	3	57	theme	products	689:696	arg1	purity					675:680	The purity	671:680	The purity of the products and their structures	671:717	The purity of the products and their structures were determined from the fully assigned high field proton NMR spectra.
3003076	0	58	theme	1H	168:169	arg1	spectroscopy					175:186	high field 1H NMR spectroscopy	157:186	high field 1H NMR spectroscopy	157:186	Characterization of the oligosaccharide alditols from ovarian cyst mucin glycoproteins of blood group A using high pressure liquid chromatography (HPLC) and high field 1H NMR spectroscopy.
3003076	1	59	theme	phase	231:235	arg1	chromatography					258:271	normal phase high pressure liquid chromatography	224:271	normal phase high pressure liquid chromatography	224:271	A combination of reverse phase and normal phase high pressure liquid chromatography has been used to separate the reduced oligosaccharides produced by alkaline borohydride degradation of a blood group A ovarian cyst mucin glycoproteins.
3003076	1	60	gly	glycoproteins	411:423	arg1	glycoproteins					411:423	a blood group A ovarian cyst mucin glycoproteins	376:423	a blood group A ovarian cyst mucin glycoproteins	376:423	A combination of reverse phase and normal phase high pressure liquid chromatography has been used to separate the reduced oligosaccharides produced by alkaline borohydride degradation of a blood group A ovarian cyst mucin glycoproteins.
3003076	1	61	theme	pressure	242:249	arg1	chromatography					258:271	normal phase high pressure liquid chromatography	224:271	normal phase high pressure liquid chromatography	224:271	A combination of reverse phase and normal phase high pressure liquid chromatography has been used to separate the reduced oligosaccharides produced by alkaline borohydride degradation of a blood group A ovarian cyst mucin glycoproteins.
3003076	1	62	used	used	282:285	arg2	chromatography					258:271	normal phase high pressure liquid chromatography	224:271	normal phase high pressure liquid chromatography	224:271	A combination of reverse phase and normal phase high pressure liquid chromatography has been used to separate the reduced oligosaccharides produced by alkaline borohydride degradation of a blood group A ovarian cyst mucin glycoproteins.
3003076	1	62	used	used	282:285	arg2	combination					191:201	A combination	189:201	A combination of reverse phase	189:218	A combination of reverse phase and normal phase high pressure liquid chromatography has been used to separate the reduced oligosaccharides produced by alkaline borohydride degradation of a blood group A ovarian cyst mucin glycoproteins.
3003076	4	63	theme	selective	861:869	arg1	sequence					877:884	the Redfield selective pulse sequence	848:884	the Redfield selective pulse sequence in H2O	848:891	The resonances of exchangeable amide protons, observed by the Redfield selective pulse sequence in H2O, were assigned by decoupling to the resonances of H2 of the 2-acetamido sugars.
3003076	4	64	theme	protons	827:833	arg1	resonances					794:803	The resonances	790:803	The resonances	790:803	The resonances of exchangeable amide protons, observed by the Redfield selective pulse sequence in H2O, were assigned by decoupling to the resonances of H2 of the 2-acetamido sugars.
3003076	6	65	theme	Overhauser	1138:1147	arg1	effect					1149:1154	nuclear Overhauser effect	1130:1154	nuclear Overhauser effect on irradiation of the anomeric proton	1130:1192	In exception to earlier proposals that nuclear Overhauser effect on irradiation of the anomeric proton should always be observed at the proton attached to the aglycone carbon, we find that for the linkage of GalNAcp(1----3)Gal, nuclear Overhauser effect on irradiation of the alpha-anomeric proton resonance is observed not at H3 but at H4 of galactose.
3003076	8	66	theme	glycopeptides	1822:1834	arg1	mixture					1811:1817	a mixture	1809:1817	a mixture of glycopeptides	1809:1834	These oligosaccharides, which terminate with beta-Gal, alpha-Fuc, beta-GlcNAc, and alpha-GalNAc, account for 75% of the total glycoprotein carbohydrate, the remainder being isolated as a mixture of glycopeptides and a high molecular weight polysaccharide whose NMR spectrum implies a simple repeating subunit structure closely related to that of the oligosaccharides.
3003076	8	66	theme	glycopeptides	1822:1834	arg1	polysaccharide					1864:1877	a high molecular weight polysaccharide	1840:1877	a high molecular weight polysaccharide whose NMR spectrum implies a simple repeating subunit structure closely related to that of the oligosaccharides	1840:1989	These oligosaccharides, which terminate with beta-Gal, alpha-Fuc, beta-GlcNAc, and alpha-GalNAc, account for 75% of the total glycoprotein carbohydrate, the remainder being isolated as a mixture of glycopeptides and a high molecular weight polysaccharide whose NMR spectrum implies a simple repeating subunit structure closely related to that of the oligosaccharides.
3003076	0	67	theme	liquid	124:129	arg1	chromatography					131:144	high pressure liquid chromatography	110:144	high pressure liquid chromatography (HPLC)	110:151	Characterization of the oligosaccharide alditols from ovarian cyst mucin glycoproteins of blood group A using high pressure liquid chromatography (HPLC) and high field 1H NMR spectroscopy.
3003076	0	67	theme	liquid	124:129	arg1	HPLC					147:150	HPLC	147:150	HPLC	147:150	Characterization of the oligosaccharide alditols from ovarian cyst mucin glycoproteins of blood group A using high pressure liquid chromatography (HPLC) and high field 1H NMR spectroscopy.
3003076	7	68	theme	oligosaccharides	1557:1572	arg1	structures					1530:1539	the structures	1526:1539	the structures of 13 different oligosaccharides of which seven have not previously been reported	1526:1621	A combination of NMR methods and enzymatic degradation was employed to determine the structures of 13 different oligosaccharides of which seven have not previously been reported.
3003076	6	69	theme	earlier	1107:1113	arg1	proposals					1115:1123	earlier proposals	1107:1123	earlier proposals that nuclear Overhauser effect on irradiation of the anomeric proton should always be observed at the proton attached to the aglycone carbon	1107:1264	In exception to earlier proposals that nuclear Overhauser effect on irradiation of the anomeric proton should always be observed at the proton attached to the aglycone carbon, we find that for the linkage of GalNAcp(1----3)Gal, nuclear Overhauser effect on irradiation of the alpha-anomeric proton resonance is observed not at H3 but at H4 of galactose.
3003076	8	70	theme	molecular	1847:1855	arg1	polysaccharide					1864:1877	a high molecular weight polysaccharide	1840:1877	a high molecular weight polysaccharide whose NMR spectrum implies a simple repeating subunit structure closely related to that of the oligosaccharides	1840:1989	These oligosaccharides, which terminate with beta-Gal, alpha-Fuc, beta-GlcNAc, and alpha-GalNAc, account for 75% of the total glycoprotein carbohydrate, the remainder being isolated as a mixture of glycopeptides and a high molecular weight polysaccharide whose NMR spectrum implies a simple repeating subunit structure closely related to that of the oligosaccharides.
3003076	5	71	theme	anomeric	1047:1054	arg1	protons					1056:1062	the anomeric protons	1043:1062	the anomeric protons	1043:1062	Nuclear Overhauser effects were used to establish the relationship of the anomeric protons and those of the aglycone.
3003076	0	72	from	glycoproteins	73:85	arg1	Characterization					0:15	Characterization	0:15	Characterization of the oligosaccharide alditols from ovarian cyst mucin glycoproteins of blood group A using high pressure liquid chromatography (HPLC) and high field 1H NMR spectroscopy.	0:187	Characterization of the oligosaccharide alditols from ovarian cyst mucin glycoproteins of blood group A using high pressure liquid chromatography (HPLC) and high field 1H NMR spectroscopy.
3003076	3	73	theme	proton	770:775	arg1	spectra					781:787	the fully assigned high field proton NMR spectra	740:787	the fully assigned high field proton NMR spectra	740:787	The purity of the products and their structures were determined from the fully assigned high field proton NMR spectra.
3003076	1	74	theme	ovarian	392:398	arg1	glycoproteins					411:423	a blood group A ovarian cyst mucin glycoproteins	376:423	a blood group A ovarian cyst mucin glycoproteins	376:423	A combination of reverse phase and normal phase high pressure liquid chromatography has been used to separate the reduced oligosaccharides produced by alkaline borohydride degradation of a blood group A ovarian cyst mucin glycoproteins.
3003076	2	75	theme	phase	566:570	arg1	column					572:577	a Zorbax C-18 reverse phase column	544:577	a Zorbax C-18 reverse phase column eluted with water	544:595	Fourteen compounds, ranging in size from a monosaccharide to a decasaccharide, have been isolated preparatively using a Zorbax C-18 reverse phase column eluted with water and a MicroPak AX-5 normal phase column eluted with aqueous acetonitrile.
3003076	3	76	theme	high	759:762	arg1	spectra					781:787	the fully assigned high field proton NMR spectra	740:787	the fully assigned high field proton NMR spectra	740:787	The purity of the products and their structures were determined from the fully assigned high field proton NMR spectra.
3003076	0	77	theme	high	157:160	arg1	spectroscopy					175:186	high field 1H NMR spectroscopy	157:186	high field 1H NMR spectroscopy	157:186	Characterization of the oligosaccharide alditols from ovarian cyst mucin glycoproteins of blood group A using high pressure liquid chromatography (HPLC) and high field 1H NMR spectroscopy.
3003076	1	78	theme	mucin	405:409	arg1	glycoproteins					411:423	a blood group A ovarian cyst mucin glycoproteins	376:423	a blood group A ovarian cyst mucin glycoproteins	376:423	A combination of reverse phase and normal phase high pressure liquid chromatography has been used to separate the reduced oligosaccharides produced by alkaline borohydride degradation of a blood group A ovarian cyst mucin glycoproteins.
3003076	2	79	theme	C-18	553:556	arg1	column					572:577	a Zorbax C-18 reverse phase column	544:577	a Zorbax C-18 reverse phase column eluted with water	544:595	Fourteen compounds, ranging in size from a monosaccharide to a decasaccharide, have been isolated preparatively using a Zorbax C-18 reverse phase column eluted with water and a MicroPak AX-5 normal phase column eluted with aqueous acetonitrile.
3003076	6	80	theme	anomeric	1178:1185	arg1	proton					1187:1192	the anomeric proton	1174:1192	the anomeric proton	1174:1192	In exception to earlier proposals that nuclear Overhauser effect on irradiation of the anomeric proton should always be observed at the proton attached to the aglycone carbon, we find that for the linkage of GalNAcp(1----3)Gal, nuclear Overhauser effect on irradiation of the alpha-anomeric proton resonance is observed not at H3 but at H4 of galactose.
3003076	6	81	theme	Overhauser	1327:1336	arg1	effect					1338:1343	nuclear Overhauser effect	1319:1343	nuclear Overhauser effect on irradiation of the alpha-anomeric proton resonance	1319:1397	In exception to earlier proposals that nuclear Overhauser effect on irradiation of the anomeric proton should always be observed at the proton attached to the aglycone carbon, we find that for the linkage of GalNAcp(1----3)Gal, nuclear Overhauser effect on irradiation of the alpha-anomeric proton resonance is observed not at H3 but at H4 of galactose.
3003076	4	82	from	sequence	877:884	arg1	H2O					889:891	H2O	889:891	H2O	889:891	The resonances of exchangeable amide protons, observed by the Redfield selective pulse sequence in H2O, were assigned by decoupling to the resonances of H2 of the 2-acetamido sugars.
3003076	4	83	theme	H2	943:944	arg1	resonances					929:938	the resonances	925:938	the resonances of H2 of the 2-acetamido sugars	925:970	The resonances of exchangeable amide protons, observed by the Redfield selective pulse sequence in H2O, were assigned by decoupling to the resonances of H2 of the 2-acetamido sugars.
3003076	6	84	theme	1----3	1307:1312	arg1	Gal					1314:1316	GalNAcp(1----3)Gal	1299:1316	GalNAcp(1----3)Gal	1299:1316	In exception to earlier proposals that nuclear Overhauser effect on irradiation of the anomeric proton should always be observed at the proton attached to the aglycone carbon, we find that for the linkage of GalNAcp(1----3)Gal, nuclear Overhauser effect on irradiation of the alpha-anomeric proton resonance is observed not at H3 but at H4 of galactose.
3003076	0	85	theme	blood	90:94	arg1	A					102:102	blood group A	90:102	blood group A using high pressure liquid chromatography (HPLC) and high field 1H NMR spectroscopy	90:186	Characterization of the oligosaccharide alditols from ovarian cyst mucin glycoproteins of blood group A using high pressure liquid chromatography (HPLC) and high field 1H NMR spectroscopy.
3003076	8	86	theme	subunit	1925:1931	arg1	structure					1933:1941	a simple repeating subunit structure	1906:1941	a simple repeating subunit structure closely related to that of the oligosaccharides	1906:1989	These oligosaccharides, which terminate with beta-Gal, alpha-Fuc, beta-GlcNAc, and alpha-GalNAc, account for 75% of the total glycoprotein carbohydrate, the remainder being isolated as a mixture of glycopeptides and a high molecular weight polysaccharide whose NMR spectrum implies a simple repeating subunit structure closely related to that of the oligosaccharides.
3003076	0	87	theme	A	102:102	arg1	glycoproteins					73:85	ovarian cyst mucin glycoproteins	54:85	ovarian cyst mucin glycoproteins of blood group A using high pressure liquid chromatography (HPLC) and high field 1H NMR spectroscopy	54:186	Characterization of the oligosaccharide alditols from ovarian cyst mucin glycoproteins of blood group A using high pressure liquid chromatography (HPLC) and high field 1H NMR spectroscopy.
3003076	1	88	theme	alkaline	340:347	arg1	degradation					361:371	alkaline borohydride degradation	340:371	alkaline borohydride degradation of a blood group A ovarian cyst mucin glycoproteins	340:423	A combination of reverse phase and normal phase high pressure liquid chromatography has been used to separate the reduced oligosaccharides produced by alkaline borohydride degradation of a blood group A ovarian cyst mucin glycoproteins.
3003076	6	89	from	effect	1149:1154	arg1	irradiation					1159:1169	irradiation	1159:1169	irradiation	1159:1169	In exception to earlier proposals that nuclear Overhauser effect on irradiation of the anomeric proton should always be observed at the proton attached to the aglycone carbon, we find that for the linkage of GalNAcp(1----3)Gal, nuclear Overhauser effect on irradiation of the alpha-anomeric proton resonance is observed not at H3 but at H4 of galactose.
3003076	0	90	theme	high	110:113	arg1	chromatography					131:144	high pressure liquid chromatography	110:144	high pressure liquid chromatography (HPLC)	110:151	Characterization of the oligosaccharide alditols from ovarian cyst mucin glycoproteins of blood group A using high pressure liquid chromatography (HPLC) and high field 1H NMR spectroscopy.
3003076	0	90	theme	high	110:113	arg1	HPLC					147:150	HPLC	147:150	HPLC	147:150	Characterization of the oligosaccharide alditols from ovarian cyst mucin glycoproteins of blood group A using high pressure liquid chromatography (HPLC) and high field 1H NMR spectroscopy.
3003076	8	91	theme	repeating	1915:1923	arg1	structure					1933:1941	a simple repeating subunit structure	1906:1941	a simple repeating subunit structure closely related to that of the oligosaccharides	1906:1989	These oligosaccharides, which terminate with beta-Gal, alpha-Fuc, beta-GlcNAc, and alpha-GalNAc, account for 75% of the total glycoprotein carbohydrate, the remainder being isolated as a mixture of glycopeptides and a high molecular weight polysaccharide whose NMR spectrum implies a simple repeating subunit structure closely related to that of the oligosaccharides.
3003076	6	92	theme	resonance	1389:1397	arg1	effect					1338:1343	nuclear Overhauser effect	1319:1343	nuclear Overhauser effect on irradiation of the alpha-anomeric proton resonance	1319:1397	In exception to earlier proposals that nuclear Overhauser effect on irradiation of the anomeric proton should always be observed at the proton attached to the aglycone carbon, we find that for the linkage of GalNAcp(1----3)Gal, nuclear Overhauser effect on irradiation of the alpha-anomeric proton resonance is observed not at H3 but at H4 of galactose.
3003076	8	93	theme	glycoprotein	1750:1761	arg1	carbohydrate					1763:1774	the total glycoprotein carbohydrate	1740:1774	the total glycoprotein carbohydrate	1740:1774	These oligosaccharides, which terminate with beta-Gal, alpha-Fuc, beta-GlcNAc, and alpha-GalNAc, account for 75% of the total glycoprotein carbohydrate, the remainder being isolated as a mixture of glycopeptides and a high molecular weight polysaccharide whose NMR spectrum implies a simple repeating subunit structure closely related to that of the oligosaccharides.
3003076	8	93	theme	glycoprotein	1750:1761	arg1	remainder					1781:1789	the remainder	1777:1789	the remainder being isolated as a mixture of glycopeptides and a high molecular weight polysaccharide whose NMR spectrum implies a simple repeating subunit structure closely related to that of the oligosaccharides	1777:1989	These oligosaccharides, which terminate with beta-Gal, alpha-Fuc, beta-GlcNAc, and alpha-GalNAc, account for 75% of the total glycoprotein carbohydrate, the remainder being isolated as a mixture of glycopeptides and a high molecular weight polysaccharide whose NMR spectrum implies a simple repeating subunit structure closely related to that of the oligosaccharides.
3003076	1	94	theme	group	384:388	arg1	A					390:390	a blood group A	376:390	a blood group A ovarian cyst mucin glycoproteins	376:423	A combination of reverse phase and normal phase high pressure liquid chromatography has been used to separate the reduced oligosaccharides produced by alkaline borohydride degradation of a blood group A ovarian cyst mucin glycoproteins.
3003076	0	95	theme	oligosaccharide	24:38	arg1	alditols					40:47	the oligosaccharide alditols	20:47	the oligosaccharide alditols	20:47	Characterization of the oligosaccharide alditols from ovarian cyst mucin glycoproteins of blood group A using high pressure liquid chromatography (HPLC) and high field 1H NMR spectroscopy.
3003076	7	96	theme	methods	1466:1472	arg1	degradation					1488:1498	enzymatic degradation	1478:1498	enzymatic degradation	1478:1498	A combination of NMR methods and enzymatic degradation was employed to determine the structures of 13 different oligosaccharides of which seven have not previously been reported.
3003076	7	96	theme	methods	1466:1472	arg1	combination					1447:1457	A combination	1445:1457	A combination of NMR methods	1445:1472	A combination of NMR methods and enzymatic degradation was employed to determine the structures of 13 different oligosaccharides of which seven have not previously been reported.
3003076	4	97	theme	sugars	965:970	arg1	H2					943:944	H2	943:944	H2 of the 2-acetamido sugars	943:970	The resonances of exchangeable amide protons, observed by the Redfield selective pulse sequence in H2O, were assigned by decoupling to the resonances of H2 of the 2-acetamido sugars.
3003076	8	98	theme	simple	1908:1913	arg1	structure					1933:1941	a simple repeating subunit structure	1906:1941	a simple repeating subunit structure closely related to that of the oligosaccharides	1906:1989	These oligosaccharides, which terminate with beta-Gal, alpha-Fuc, beta-GlcNAc, and alpha-GalNAc, account for 75% of the total glycoprotein carbohydrate, the remainder being isolated as a mixture of glycopeptides and a high molecular weight polysaccharide whose NMR spectrum implies a simple repeating subunit structure closely related to that of the oligosaccharides.
3003076	0	99	theme	cyst	62:65	arg1	glycoproteins					73:85	ovarian cyst mucin glycoproteins	54:85	ovarian cyst mucin glycoproteins of blood group A using high pressure liquid chromatography (HPLC) and high field 1H NMR spectroscopy	54:186	Characterization of the oligosaccharide alditols from ovarian cyst mucin glycoproteins of blood group A using high pressure liquid chromatography (HPLC) and high field 1H NMR spectroscopy.
3003076	4	100	theme	exchangeable	808:819	arg1	protons					827:833	exchangeable amide protons	808:833	exchangeable amide protons	808:833	The resonances of exchangeable amide protons, observed by the Redfield selective pulse sequence in H2O, were assigned by decoupling to the resonances of H2 of the 2-acetamido sugars.
3003076	1	101	theme	A	390:390	arg1	glycoproteins					411:423	a blood group A ovarian cyst mucin glycoproteins	376:423	a blood group A ovarian cyst mucin glycoproteins	376:423	A combination of reverse phase and normal phase high pressure liquid chromatography has been used to separate the reduced oligosaccharides produced by alkaline borohydride degradation of a blood group A ovarian cyst mucin glycoproteins.
3003076	1	102	theme	reduced	303:309	arg1	oligosaccharides					311:326	the reduced oligosaccharides	299:326	the reduced oligosaccharides produced by alkaline borohydride degradation of a blood group A ovarian cyst mucin glycoproteins	299:423	A combination of reverse phase and normal phase high pressure liquid chromatography has been used to separate the reduced oligosaccharides produced by alkaline borohydride degradation of a blood group A ovarian cyst mucin glycoproteins.
3003076	1	103	theme	phase	214:218	arg1	chromatography					258:271	normal phase high pressure liquid chromatography	224:271	normal phase high pressure liquid chromatography	224:271	A combination of reverse phase and normal phase high pressure liquid chromatography has been used to separate the reduced oligosaccharides produced by alkaline borohydride degradation of a blood group A ovarian cyst mucin glycoproteins.
3003076	1	103	theme	phase	214:218	arg1	combination					191:201	A combination	189:201	A combination of reverse phase	189:218	A combination of reverse phase and normal phase high pressure liquid chromatography has been used to separate the reduced oligosaccharides produced by alkaline borohydride degradation of a blood group A ovarian cyst mucin glycoproteins.
3003076	5	104	theme	Nuclear	973:979	arg1	effects					992:998	Nuclear Overhauser effects	973:998	Nuclear Overhauser effects	973:998	Nuclear Overhauser effects were used to establish the relationship of the anomeric protons and those of the aglycone.
3003076	5	105	used	used	1005:1008	arg2	effects					992:998	Nuclear Overhauser effects	973:998	Nuclear Overhauser effects	973:998	Nuclear Overhauser effects were used to establish the relationship of the anomeric protons and those of the aglycone.
3003076	1	106	theme	normal	224:229	arg1	chromatography					258:271	normal phase high pressure liquid chromatography	224:271	normal phase high pressure liquid chromatography	224:271	A combination of reverse phase and normal phase high pressure liquid chromatography has been used to separate the reduced oligosaccharides produced by alkaline borohydride degradation of a blood group A ovarian cyst mucin glycoproteins.
7622940	0	0	theme	pancreatic	86:95	arg1	juice					97:101	human pancreatic juice	80:101	human pancreatic juice	80:101	Chemical structure of the carbohydrate moiety of fucose-rich glycopeptides from human pancreatic juice.
7622940	4	1	theme	-NMR	578:581	arg1	spectroscopy					583:594	500-MHz [1H]-NMR spectroscopy	566:594	500-MHz [1H]-NMR spectroscopy	566:594	The chemical structures of the three glycopeptides were determined using 500-MHz [1H]-NMR spectroscopy.
7622940	0	2	theme	human	80:84	arg1	juice					97:101	human pancreatic juice	80:101	human pancreatic juice	80:101	Chemical structure of the carbohydrate moiety of fucose-rich glycopeptides from human pancreatic juice.
7622940	1	3	theme	partial	162:168	arg1	excision					170:177	partial excision	162:177	partial excision of the pancreas for bile duct cancer	162:214	Human pancreatic juice, obtained from nine patients after partial excision of the pancreas for bile duct cancer, was fractionated in order to isolate its glycopeptides.
7622940	5	4	theme	biantennary	642:652	arg1	structure					654:662	a biantennary structure	640:662	a biantennary structure with three L-fucose residues	640:691	One of them, glycopeptide, GP-4, possessed a biantennary structure with three L-fucose residues.
7622940	7	5	theme	sialic	943:948	arg1	acid					950:953	sialic acid	943:953	sialic acid	943:953	The chemical compositions of these glycopeptides, including the absence of sialic acid and the high L-fucose content, indicate that they represent a new class of glycopeptide present in the normal human pancreas.
7622940	0	6	gly	glycopeptides	61:73	arg2	glycopeptides					61:73	fucose-rich glycopeptides	49:73	fucose-rich glycopeptides from human pancreatic juice	49:101	Chemical structure of the carbohydrate moiety of fucose-rich glycopeptides from human pancreatic juice.
7622940	0	6	gly	glycopeptides	61:73	arg1	juice					97:101	human pancreatic juice	80:101	human pancreatic juice	80:101	Chemical structure of the carbohydrate moiety of fucose-rich glycopeptides from human pancreatic juice.
7622940	2	7	gly	glycopeptides	279:291	arg2	glycopeptides					279:291	Three glycopeptides	273:291	Three glycopeptides	273:291	Three glycopeptides were purified employing ion-exchange chromatography and gel filtration.
7622940	5	8	theme	them	604:607	arg1	GP-4					624:627	GP-4	624:627	GP-4	624:627	One of them, glycopeptide, GP-4, possessed a biantennary structure with three L-fucose residues.
7622940	5	8	theme	them	604:607	arg1	glycopeptide					610:621	glycopeptide	610:621	glycopeptide	610:621	One of them, glycopeptide, GP-4, possessed a biantennary structure with three L-fucose residues.
7622940	5	8	theme	them	604:607	arg1	them					604:607	them	604:607	them	604:607	One of them, glycopeptide, GP-4, possessed a biantennary structure with three L-fucose residues.
7622940	5	8	theme	them	604:607	arg1	One					597:599	One	597:599	One	597:599	One of them, glycopeptide, GP-4, possessed a biantennary structure with three L-fucose residues.
7622940	6	9	contain	had	807:809	arg2	structure					829:837	a tetra-antennary structure	811:837	a tetra-antennary structure with five L-fucose residues	811:865	The second glycopeptide, GP-3, had a triantennary structure with four L-fucose residues, and the third one, G-2, had a tetra-antennary structure with five L-fucose residues.
7622940	6	9	contain	had	807:809	arg1	G-2					802:804	G-2	802:804	G-2	802:804	The second glycopeptide, GP-3, had a triantennary structure with four L-fucose residues, and the third one, G-2, had a tetra-antennary structure with five L-fucose residues.
7622940	6	9	contain	had	807:809	arg1	one					797:799	one	797:799	one	797:799	The second glycopeptide, GP-3, had a triantennary structure with four L-fucose residues, and the third one, G-2, had a tetra-antennary structure with five L-fucose residues.
7622940	3	10	theme	high	467:470	arg1	content					472:478	an unusually high content	454:478	an unusually high content of L-fucose	454:490	All the glycopeptides were found to be free of sialic acid and galactosamine but to have an unusually high content of L-fucose.
7622940	6	11	theme	second	698:703	arg1	GP-3					719:722	GP-3	719:722	GP-3	719:722	The second glycopeptide, GP-3, had a triantennary structure with four L-fucose residues, and the third one, G-2, had a tetra-antennary structure with five L-fucose residues.
7622940	6	11	theme	second	698:703	arg1	glycopeptide					705:716	The second glycopeptide	694:716	The second glycopeptide	694:716	The second glycopeptide, GP-3, had a triantennary structure with four L-fucose residues, and the third one, G-2, had a tetra-antennary structure with five L-fucose residues.
7622940	0	12	from	moiety	39:44	arg1	juice					97:101	human pancreatic juice	80:101	human pancreatic juice	80:101	Chemical structure of the carbohydrate moiety of fucose-rich glycopeptides from human pancreatic juice.
7622940	3	13	theme	sialic	412:417	arg1	acid					419:422	sialic acid	412:422	sialic acid	412:422	All the glycopeptides were found to be free of sialic acid and galactosamine but to have an unusually high content of L-fucose.
7622940	5	14	gly	glycopeptide	610:621	arg2	glycopeptide					610:621	glycopeptide	610:621	glycopeptide	610:621	One of them, glycopeptide, GP-4, possessed a biantennary structure with three L-fucose residues.
7622940	5	14	gly	glycopeptide	610:621	arg2	them					604:607	them	604:607	them	604:607	One of them, glycopeptide, GP-4, possessed a biantennary structure with three L-fucose residues.
7622940	5	14	gly	glycopeptide	610:621	arg2	One					597:599	One	597:599	One	597:599	One of them, glycopeptide, GP-4, possessed a biantennary structure with three L-fucose residues.
7622940	7	15	theme	chemical	872:879	arg1	content					977:983	the high L-fucose content	959:983	the high L-fucose content	959:983	The chemical compositions of these glycopeptides, including the absence of sialic acid and the high L-fucose content, indicate that they represent a new class of glycopeptide present in the normal human pancreas.
7622940	7	15	theme	chemical	872:879	arg1	compositions					881:892	The chemical compositions	868:892	The chemical compositions	868:892	The chemical compositions of these glycopeptides, including the absence of sialic acid and the high L-fucose content, indicate that they represent a new class of glycopeptide present in the normal human pancreas.
7622940	7	15	theme	chemical	872:879	arg1	absence					932:938	the absence	928:938	the absence of sialic acid	928:953	The chemical compositions of these glycopeptides, including the absence of sialic acid and the high L-fucose content, indicate that they represent a new class of glycopeptide present in the normal human pancreas.
7622940	6	16	with	structure	744:752	arg1	residues					773:780	four L-fucose residues	759:780	four L-fucose residues	759:780	The second glycopeptide, GP-3, had a triantennary structure with four L-fucose residues, and the third one, G-2, had a tetra-antennary structure with five L-fucose residues.
7622940	7	17	theme	present	1043:1049	arg1	class					1021:1025	a new class	1015:1025	a new class of glycopeptide present in the normal human pancreas	1015:1078	The chemical compositions of these glycopeptides, including the absence of sialic acid and the high L-fucose content, indicate that they represent a new class of glycopeptide present in the normal human pancreas.
7622940	2	18	theme	ion-exchange	317:328	arg1	chromatography					330:343	ion-exchange chromatography	317:343	ion-exchange chromatography	317:343	Three glycopeptides were purified employing ion-exchange chromatography and gel filtration.
7622940	0	19	theme	Chemical	0:7	arg1	structure					9:17	Chemical structure	0:17	Chemical structure of the carbohydrate moiety of fucose-rich glycopeptides from human pancreatic juice	0:101	Chemical structure of the carbohydrate moiety of fucose-rich glycopeptides from human pancreatic juice.
7622940	7	20	from	present	1043:1049	arg1	pancreas					1071:1078	the normal human pancreas	1054:1078	the normal human pancreas	1054:1078	The chemical compositions of these glycopeptides, including the absence of sialic acid and the high L-fucose content, indicate that they represent a new class of glycopeptide present in the normal human pancreas.
7622940	6	21	theme	L-fucose	764:771	arg1	residues					773:780	four L-fucose residues	759:780	four L-fucose residues	759:780	The second glycopeptide, GP-3, had a triantennary structure with four L-fucose residues, and the third one, G-2, had a tetra-antennary structure with five L-fucose residues.
7622940	1	22	theme	pancreas	186:193	arg1	excision					170:177	partial excision	162:177	partial excision of the pancreas for bile duct cancer	162:214	Human pancreatic juice, obtained from nine patients after partial excision of the pancreas for bile duct cancer, was fractionated in order to isolate its glycopeptides.
7622940	3	23	gly	glycopeptides	373:385	arg2	glycopeptides					373:385	All the glycopeptides	365:385	All the glycopeptides	365:385	All the glycopeptides were found to be free of sialic acid and galactosamine but to have an unusually high content of L-fucose.
7622940	7	24	theme	glycopeptides	903:915	arg1	content					977:983	the high L-fucose content	959:983	the high L-fucose content	959:983	The chemical compositions of these glycopeptides, including the absence of sialic acid and the high L-fucose content, indicate that they represent a new class of glycopeptide present in the normal human pancreas.
7622940	7	24	theme	glycopeptides	903:915	arg1	compositions					881:892	The chemical compositions	868:892	The chemical compositions	868:892	The chemical compositions of these glycopeptides, including the absence of sialic acid and the high L-fucose content, indicate that they represent a new class of glycopeptide present in the normal human pancreas.
7622940	7	24	theme	glycopeptides	903:915	arg1	absence					932:938	the absence	928:938	the absence of sialic acid	928:953	The chemical compositions of these glycopeptides, including the absence of sialic acid and the high L-fucose content, indicate that they represent a new class of glycopeptide present in the normal human pancreas.
7622940	1	25	theme	Human	104:108	arg1	juice					121:125	Human pancreatic juice	104:125	Human pancreatic juice	104:125	Human pancreatic juice, obtained from nine patients after partial excision of the pancreas for bile duct cancer, was fractionated in order to isolate its glycopeptides.
7622940	4	26	theme	[1H	574:576	arg1	spectroscopy					583:594	500-MHz [1H]-NMR spectroscopy	566:594	500-MHz [1H]-NMR spectroscopy	566:594	The chemical structures of the three glycopeptides were determined using 500-MHz [1H]-NMR spectroscopy.
7622940	7	27	theme	L-fucose	968:975	arg1	content					977:983	the high L-fucose content	959:983	the high L-fucose content	959:983	The chemical compositions of these glycopeptides, including the absence of sialic acid and the high L-fucose content, indicate that they represent a new class of glycopeptide present in the normal human pancreas.
7622940	1	28	theme	pancreatic	110:119	arg1	juice					121:125	Human pancreatic juice	104:125	Human pancreatic juice	104:125	Human pancreatic juice, obtained from nine patients after partial excision of the pancreas for bile duct cancer, was fractionated in order to isolate its glycopeptides.
7622940	1	29	theme	bile	199:202	arg1	cancer					209:214	bile duct cancer	199:214	bile duct cancer	199:214	Human pancreatic juice, obtained from nine patients after partial excision of the pancreas for bile duct cancer, was fractionated in order to isolate its glycopeptides.
7622940	0	30	theme	moiety	39:44	arg1	structure					9:17	Chemical structure	0:17	Chemical structure of the carbohydrate moiety of fucose-rich glycopeptides from human pancreatic juice	0:101	Chemical structure of the carbohydrate moiety of fucose-rich glycopeptides from human pancreatic juice.
7622940	4	31	theme	500-MHz	566:572	arg1	spectroscopy					583:594	500-MHz [1H]-NMR spectroscopy	566:594	500-MHz [1H]-NMR spectroscopy	566:594	The chemical structures of the three glycopeptides were determined using 500-MHz [1H]-NMR spectroscopy.
7622940	7	32	theme	new	1017:1019	arg1	class					1021:1025	a new class	1015:1025	a new class of glycopeptide present in the normal human pancreas	1015:1078	The chemical compositions of these glycopeptides, including the absence of sialic acid and the high L-fucose content, indicate that they represent a new class of glycopeptide present in the normal human pancreas.
7622940	3	33	theme	galactosamine	428:440	arg1	free					404:407	free	404:407	free	404:407	All the glycopeptides were found to be free of sialic acid and galactosamine but to have an unusually high content of L-fucose.
7622940	1	34	theme	duct	204:207	arg1	cancer					209:214	bile duct cancer	199:214	bile duct cancer	199:214	Human pancreatic juice, obtained from nine patients after partial excision of the pancreas for bile duct cancer, was fractionated in order to isolate its glycopeptides.
7622940	0	35	theme	carbohydrate	26:37	arg1	moiety					39:44	the carbohydrate moiety	22:44	the carbohydrate moiety of fucose-rich glycopeptides from human pancreatic juice	22:101	Chemical structure of the carbohydrate moiety of fucose-rich glycopeptides from human pancreatic juice.
7622940	3	36	theme	acid	419:422	arg1	free					404:407	free	404:407	free	404:407	All the glycopeptides were found to be free of sialic acid and galactosamine but to have an unusually high content of L-fucose.
7622940	6	37	theme	tetra-antennary	813:827	arg1	structure					829:837	a tetra-antennary structure	811:837	a tetra-antennary structure with five L-fucose residues	811:865	The second glycopeptide, GP-3, had a triantennary structure with four L-fucose residues, and the third one, G-2, had a tetra-antennary structure with five L-fucose residues.
7622940	7	38	gly	glycopeptides	903:915	arg2	glycopeptides					903:915	these glycopeptides	897:915	these glycopeptides	897:915	The chemical compositions of these glycopeptides, including the absence of sialic acid and the high L-fucose content, indicate that they represent a new class of glycopeptide present in the normal human pancreas.
7622940	0	39	theme	fucose-rich	49:59	arg1	glycopeptides					61:73	fucose-rich glycopeptides	49:73	fucose-rich glycopeptides from human pancreatic juice	49:101	Chemical structure of the carbohydrate moiety of fucose-rich glycopeptides from human pancreatic juice.
7622940	7	40	from	pancreas	1071:1078	arg1	present					1043:1049	present	1043:1049	present	1043:1049	The chemical compositions of these glycopeptides, including the absence of sialic acid and the high L-fucose content, indicate that they represent a new class of glycopeptide present in the normal human pancreas.
7622940	1	41	gly	glycopeptides	258:270	arg2	glycopeptides					258:270	its glycopeptides	254:270	its glycopeptides	254:270	Human pancreatic juice, obtained from nine patients after partial excision of the pancreas for bile duct cancer, was fractionated in order to isolate its glycopeptides.
7622940	3	42	theme	L-fucose	483:490	arg1	content					472:478	an unusually high content	454:478	an unusually high content of L-fucose	454:490	All the glycopeptides were found to be free of sialic acid and galactosamine but to have an unusually high content of L-fucose.
7622940	6	43	contain	had	725:727	arg2	structure					744:752	a triantennary structure	729:752	a triantennary structure with four L-fucose residues	729:780	The second glycopeptide, GP-3, had a triantennary structure with four L-fucose residues, and the third one, G-2, had a tetra-antennary structure with five L-fucose residues.
7622940	6	43	contain	had	725:727	arg1	GP-3					719:722	GP-3	719:722	GP-3	719:722	The second glycopeptide, GP-3, had a triantennary structure with four L-fucose residues, and the third one, G-2, had a tetra-antennary structure with five L-fucose residues.
7622940	6	43	contain	had	725:727	arg1	glycopeptide					705:716	The second glycopeptide	694:716	The second glycopeptide	694:716	The second glycopeptide, GP-3, had a triantennary structure with four L-fucose residues, and the third one, G-2, had a tetra-antennary structure with five L-fucose residues.
7622940	7	44	theme	normal	1058:1063	arg1	pancreas					1071:1078	the normal human pancreas	1054:1078	the normal human pancreas	1054:1078	The chemical compositions of these glycopeptides, including the absence of sialic acid and the high L-fucose content, indicate that they represent a new class of glycopeptide present in the normal human pancreas.
7622940	6	45	theme	triantennary	731:742	arg1	structure					744:752	a triantennary structure	729:752	a triantennary structure with four L-fucose residues	729:780	The second glycopeptide, GP-3, had a triantennary structure with four L-fucose residues, and the third one, G-2, had a tetra-antennary structure with five L-fucose residues.
7622940	2	46	theme	gel	349:351	arg1	filtration					353:362	gel filtration	349:362	gel filtration	349:362	Three glycopeptides were purified employing ion-exchange chromatography and gel filtration.
7622940	4	47	theme	glycopeptides	530:542	arg1	structures					506:515	The chemical structures	493:515	The chemical structures of the three glycopeptides	493:542	The chemical structures of the three glycopeptides were determined using 500-MHz [1H]-NMR spectroscopy.
7622940	5	48	theme	L-fucose	675:682	arg1	residues					684:691	three L-fucose residues	669:691	three L-fucose residues	669:691	One of them, glycopeptide, GP-4, possessed a biantennary structure with three L-fucose residues.
7622940	6	49	gly	glycopeptide	705:716	arg2	glycopeptide					705:716	The second glycopeptide	694:716	The second glycopeptide	694:716	The second glycopeptide, GP-3, had a triantennary structure with four L-fucose residues, and the third one, G-2, had a tetra-antennary structure with five L-fucose residues.
7622940	6	49	gly	glycopeptide	705:716	arg2	GP-3					719:722	GP-3	719:722	GP-3	719:722	The second glycopeptide, GP-3, had a triantennary structure with four L-fucose residues, and the third one, G-2, had a tetra-antennary structure with five L-fucose residues.
7622940	7	50	theme	acid	950:953	arg1	absence					932:938	the absence	928:938	the absence of sialic acid	928:953	The chemical compositions of these glycopeptides, including the absence of sialic acid and the high L-fucose content, indicate that they represent a new class of glycopeptide present in the normal human pancreas.
7622940	7	50	theme	acid	950:953	arg1	content					977:983	the high L-fucose content	959:983	the high L-fucose content	959:983	The chemical compositions of these glycopeptides, including the absence of sialic acid and the high L-fucose content, indicate that they represent a new class of glycopeptide present in the normal human pancreas.
7622940	7	51	theme	glycopeptide	1030:1041	arg1	class					1021:1025	a new class	1015:1025	a new class of glycopeptide present in the normal human pancreas	1015:1078	The chemical compositions of these glycopeptides, including the absence of sialic acid and the high L-fucose content, indicate that they represent a new class of glycopeptide present in the normal human pancreas.
7622940	7	52	theme	human	1065:1069	arg1	pancreas					1071:1078	the normal human pancreas	1054:1078	the normal human pancreas	1054:1078	The chemical compositions of these glycopeptides, including the absence of sialic acid and the high L-fucose content, indicate that they represent a new class of glycopeptide present in the normal human pancreas.
7622940	0	53	from	juice	97:101	arg1	moiety					39:44	the carbohydrate moiety	22:44	the carbohydrate moiety of fucose-rich glycopeptides from human pancreatic juice	22:101	Chemical structure of the carbohydrate moiety of fucose-rich glycopeptides from human pancreatic juice.
7622940	0	53	from	juice	97:101	arg1	glycopeptides					61:73	fucose-rich glycopeptides	49:73	fucose-rich glycopeptides from human pancreatic juice	49:101	Chemical structure of the carbohydrate moiety of fucose-rich glycopeptides from human pancreatic juice.
7622940	6	54	theme	L-fucose	849:856	arg1	residues					858:865	five L-fucose residues	844:865	five L-fucose residues	844:865	The second glycopeptide, GP-3, had a triantennary structure with four L-fucose residues, and the third one, G-2, had a tetra-antennary structure with five L-fucose residues.
7622940	7	55	theme	high	963:966	arg1	content					977:983	the high L-fucose content	959:983	the high L-fucose content	959:983	The chemical compositions of these glycopeptides, including the absence of sialic acid and the high L-fucose content, indicate that they represent a new class of glycopeptide present in the normal human pancreas.
7622940	7	56	gly	glycopeptide	1030:1041	arg2	glycopeptide					1030:1041	glycopeptide	1030:1041	glycopeptide	1030:1041	The chemical compositions of these glycopeptides, including the absence of sialic acid and the high L-fucose content, indicate that they represent a new class of glycopeptide present in the normal human pancreas.
7622940	7	57	attach	present	1043:1049	arg1	pancreas					1071:1078	the normal human pancreas	1054:1078	the normal human pancreas	1054:1078	The chemical compositions of these glycopeptides, including the absence of sialic acid and the high L-fucose content, indicate that they represent a new class of glycopeptide present in the normal human pancreas.
7622940	7	57	attach	present	1043:1049	arg2	class					1021:1025	a new class	1015:1025	a new class of glycopeptide present in the normal human pancreas	1015:1078	The chemical compositions of these glycopeptides, including the absence of sialic acid and the high L-fucose content, indicate that they represent a new class of glycopeptide present in the normal human pancreas.
7622940	6	58	with	structure	829:837	arg1	residues					858:865	five L-fucose residues	844:865	five L-fucose residues	844:865	The second glycopeptide, GP-3, had a triantennary structure with four L-fucose residues, and the third one, G-2, had a tetra-antennary structure with five L-fucose residues.
7622940	0	59	theme	glycopeptides	61:73	arg1	moiety					39:44	the carbohydrate moiety	22:44	the carbohydrate moiety of fucose-rich glycopeptides from human pancreatic juice	22:101	Chemical structure of the carbohydrate moiety of fucose-rich glycopeptides from human pancreatic juice.
7622940	4	60	theme	chemical	497:504	arg1	structures					506:515	The chemical structures	493:515	The chemical structures of the three glycopeptides	493:542	The chemical structures of the three glycopeptides were determined using 500-MHz [1H]-NMR spectroscopy.
7622940	4	61	gly	glycopeptides	530:542	arg2	glycopeptides					530:542	the three glycopeptides	520:542	the three glycopeptides	520:542	The chemical structures of the three glycopeptides were determined using 500-MHz [1H]-NMR spectroscopy.
7622940	5	62	with	structure	654:662	arg1	residues					684:691	three L-fucose residues	669:691	three L-fucose residues	669:691	One of them, glycopeptide, GP-4, possessed a biantennary structure with three L-fucose residues.
7622940	5	63	contain	possessed	630:638	arg2	structure					654:662	a biantennary structure	640:662	a biantennary structure with three L-fucose residues	640:691	One of them, glycopeptide, GP-4, possessed a biantennary structure with three L-fucose residues.
7622940	5	63	contain	possessed	630:638	arg1	GP-4					624:627	GP-4	624:627	GP-4	624:627	One of them, glycopeptide, GP-4, possessed a biantennary structure with three L-fucose residues.
7622940	5	63	contain	possessed	630:638	arg1	glycopeptide					610:621	glycopeptide	610:621	glycopeptide	610:621	One of them, glycopeptide, GP-4, possessed a biantennary structure with three L-fucose residues.
7622940	5	63	contain	possessed	630:638	arg1	them					604:607	them	604:607	them	604:607	One of them, glycopeptide, GP-4, possessed a biantennary structure with three L-fucose residues.
7622940	5	63	contain	possessed	630:638	arg1	One					597:599	One	597:599	One	597:599	One of them, glycopeptide, GP-4, possessed a biantennary structure with three L-fucose residues.
3667593	0	0	theme	recombinant	76:86	arg1	line					115:118	a recombinant Chinese hamster ovary cell line	74:118	a recombinant Chinese hamster ovary cell line	74:118	Structure of the carbohydrate moiety of human interferon-beta secreted by a recombinant Chinese hamster ovary cell line.
3667593	2	1	theme	exoglycosidase	376:389	arg1	treatment					391:399	sequential exoglycosidase treatment	365:399	sequential exoglycosidase treatment	365:399	Analysis of the glycopeptidase F-released carbohydrates by sequential exoglycosidase treatment, methylation analysis, and fast atom bombardment-mass spectrometry revealed that 95% of the IFN-beta oligosaccharides had the following structure: (Formula: see text).
3667593	1	2	theme	Chinese	253:259	arg1	line					280:283	a genetically engineered Chinese hamster ovary cell line	228:283	a genetically engineered Chinese hamster ovary cell line	228:283	The carbohydrate structure of the major oligosaccharide of human interferon-beta (IFN-beta) synthesized by a genetically engineered Chinese hamster ovary cell line has been determined.
3667593	1	3	theme	major	155:159	arg1	oligosaccharide					161:175	the major oligosaccharide	151:175	the major oligosaccharide of human interferon-beta (IFN-beta) synthesized by a genetically engineered Chinese hamster ovary cell line	151:283	The carbohydrate structure of the major oligosaccharide of human interferon-beta (IFN-beta) synthesized by a genetically engineered Chinese hamster ovary cell line has been determined.
3667593	1	4	theme	hamster	261:267	arg1	line					280:283	a genetically engineered Chinese hamster ovary cell line	228:283	a genetically engineered Chinese hamster ovary cell line	228:283	The carbohydrate structure of the major oligosaccharide of human interferon-beta (IFN-beta) synthesized by a genetically engineered Chinese hamster ovary cell line has been determined.
3667593	0	5	theme	hamster	96:102	arg1	line					115:118	a recombinant Chinese hamster ovary cell line	74:118	a recombinant Chinese hamster ovary cell line	74:118	Structure of the carbohydrate moiety of human interferon-beta secreted by a recombinant Chinese hamster ovary cell line.
3667593	5	6	theme	liver	1016:1020	arg1	alpha					1041:1045	rat liver Gal beta 1-4GlcNAc alpha 2-6	1012:1049	rat liver Gal beta 1-4GlcNAc alpha 2-6 sialyltransferase	1012:1067	NeuAc, which is alpha 2-3-linked to galactose in the human IFN-beta secreted by Chinese hamster ovary cells, can be re-incorporated with an alpha 2-6 linkage in vitro, into enzymatically desialylated IFN-beta using rat liver Gal beta 1-4GlcNAc alpha 2-6 sialyltransferase.
3667593	3	7	theme	remaining	573:581	arg1	carbohydrates					593:605	the carbohydrates	589:605	the carbohydrates	589:605	The remaining 5% of the carbohydrates are probably tri- or higher antennary oligosaccharide chains.
3667593	3	7	theme	remaining	573:581	arg1	tri-					620:623	tri-	620:623	tri-	620:623	The remaining 5% of the carbohydrates are probably tri- or higher antennary oligosaccharide chains.
3667593	3	7	theme	remaining	573:581	arg1	%					584:584	The remaining 5%	569:584	The remaining 5% of the carbohydrates	569:605	The remaining 5% of the carbohydrates are probably tri- or higher antennary oligosaccharide chains.
3667593	1	8	theme	ovary	269:273	arg1	line					280:283	a genetically engineered Chinese hamster ovary cell line	228:283	a genetically engineered Chinese hamster ovary cell line	228:283	The carbohydrate structure of the major oligosaccharide of human interferon-beta (IFN-beta) synthesized by a genetically engineered Chinese hamster ovary cell line has been determined.
3667593	0	9	theme	Chinese	88:94	arg1	line					115:118	a recombinant Chinese hamster ovary cell line	74:118	a recombinant Chinese hamster ovary cell line	74:118	Structure of the carbohydrate moiety of human interferon-beta secreted by a recombinant Chinese hamster ovary cell line.
3667593	6	10	theme	glycopeptidase	1217:1230	arg1	F					1232:1232	glycopeptidase F	1217:1232	glycopeptidase F	1217:1232	The sugar chain is important for maintaining protein solubility as shown by the fact that IFN-beta protein precipitates after deglycosylation with glycopeptidase F.
3667593	5	11	theme	desialylated	984:995	arg1	IFN-beta					997:1004	enzymatically desialylated IFN-beta	970:1004	enzymatically desialylated IFN-beta using rat liver Gal beta 1-4GlcNAc alpha 2-6 sialyltransferase	970:1067	NeuAc, which is alpha 2-3-linked to galactose in the human IFN-beta secreted by Chinese hamster ovary cells, can be re-incorporated with an alpha 2-6 linkage in vitro, into enzymatically desialylated IFN-beta using rat liver Gal beta 1-4GlcNAc alpha 2-6 sialyltransferase.
3667593	1	12	theme	cell	275:278	arg1	line					280:283	a genetically engineered Chinese hamster ovary cell line	228:283	a genetically engineered Chinese hamster ovary cell line	228:283	The carbohydrate structure of the major oligosaccharide of human interferon-beta (IFN-beta) synthesized by a genetically engineered Chinese hamster ovary cell line has been determined.
3667593	0	13	theme	cell	110:113	arg1	line					115:118	a recombinant Chinese hamster ovary cell line	74:118	a recombinant Chinese hamster ovary cell line	74:118	Structure of the carbohydrate moiety of human interferon-beta secreted by a recombinant Chinese hamster ovary cell line.
3667593	6	14	theme	sugar	1074:1078	arg1	important					1089:1097	important	1089:1097	important	1089:1097	The sugar chain is important for maintaining protein solubility as shown by the fact that IFN-beta protein precipitates after deglycosylation with glycopeptidase F.
3667593	6	14	theme	sugar	1074:1078	arg1	chain					1080:1084	The sugar chain	1070:1084	The sugar chain	1070:1084	The sugar chain is important for maintaining protein solubility as shown by the fact that IFN-beta protein precipitates after deglycosylation with glycopeptidase F.
3667593	1	15	theme	oligosaccharide	161:175	arg1	structure					138:146	The carbohydrate structure	121:146	The carbohydrate structure of the major oligosaccharide of human interferon-beta (IFN-beta) synthesized by a genetically engineered Chinese hamster ovary cell line	121:283	The carbohydrate structure of the major oligosaccharide of human interferon-beta (IFN-beta) synthesized by a genetically engineered Chinese hamster ovary cell line has been determined.
3667593	0	16	theme	ovary	104:108	arg1	line					115:118	a recombinant Chinese hamster ovary cell line	74:118	a recombinant Chinese hamster ovary cell line	74:118	Structure of the carbohydrate moiety of human interferon-beta secreted by a recombinant Chinese hamster ovary cell line.
3667593	5	17	from	galactose	833:841	arg1	IFN-beta					856:863	the human IFN-beta	846:863	the human IFN-beta secreted by Chinese hamster ovary cells	846:903	NeuAc, which is alpha 2-3-linked to galactose in the human IFN-beta secreted by Chinese hamster ovary cells, can be re-incorporated with an alpha 2-6 linkage in vitro, into enzymatically desialylated IFN-beta using rat liver Gal beta 1-4GlcNAc alpha 2-6 sialyltransferase.
3667593	2	18	theme	glycopeptidase	322:335	arg1	carbohydrates					348:360	the glycopeptidase F-released carbohydrates	318:360	the glycopeptidase F-released carbohydrates	318:360	Analysis of the glycopeptidase F-released carbohydrates by sequential exoglycosidase treatment, methylation analysis, and fast atom bombardment-mass spectrometry revealed that 95% of the IFN-beta oligosaccharides had the following structure: (Formula: see text).
3667593	6	19	theme	protein	1115:1121	arg1	solubility					1123:1132	protein solubility	1115:1132	protein solubility	1115:1132	The sugar chain is important for maintaining protein solubility as shown by the fact that IFN-beta protein precipitates after deglycosylation with glycopeptidase F.
3667593	5	20	theme	ovary	893:897	arg1	cells					899:903	Chinese hamster ovary cells	877:903	Chinese hamster ovary cells	877:903	NeuAc, which is alpha 2-3-linked to galactose in the human IFN-beta secreted by Chinese hamster ovary cells, can be re-incorporated with an alpha 2-6 linkage in vitro, into enzymatically desialylated IFN-beta using rat liver Gal beta 1-4GlcNAc alpha 2-6 sialyltransferase.
3667593	4	21	theme	terminal	765:772	arg1	sialylation					784:794	terminal galactose sialylation	765:794	terminal galactose sialylation	765:794	The major oligosaccharide of the recombinant IFN-beta is remarkably homogeneous with respect to terminal galactose sialylation.
3667593	1	22	theme	human	180:184	arg1	IFN-beta					203:210	IFN-beta	203:210	IFN-beta	203:210	The carbohydrate structure of the major oligosaccharide of human interferon-beta (IFN-beta) synthesized by a genetically engineered Chinese hamster ovary cell line has been determined.
3667593	1	22	theme	human	180:184	arg1	interferon-beta					186:200	human interferon-beta	180:200	human interferon-beta (IFN-beta) synthesized by a genetically engineered Chinese hamster ovary cell line	180:283	The carbohydrate structure of the major oligosaccharide of human interferon-beta (IFN-beta) synthesized by a genetically engineered Chinese hamster ovary cell line has been determined.
3667593	4	23	theme	major	673:677	arg1	homogeneous					737:747	homogeneous	737:747	homogeneous	737:747	The major oligosaccharide of the recombinant IFN-beta is remarkably homogeneous with respect to terminal galactose sialylation.
3667593	4	23	theme	major	673:677	arg1	oligosaccharide					679:693	The major oligosaccharide	669:693	The major oligosaccharide of the recombinant IFN-beta	669:721	The major oligosaccharide of the recombinant IFN-beta is remarkably homogeneous with respect to terminal galactose sialylation.
3667593	1	24	theme	interferon-beta	186:200	arg1	oligosaccharide					161:175	the major oligosaccharide	151:175	the major oligosaccharide of human interferon-beta (IFN-beta) synthesized by a genetically engineered Chinese hamster ovary cell line	151:283	The carbohydrate structure of the major oligosaccharide of human interferon-beta (IFN-beta) synthesized by a genetically engineered Chinese hamster ovary cell line has been determined.
3667593	0	25	theme	carbohydrate	17:28	arg1	moiety					30:35	the carbohydrate moiety	13:35	the carbohydrate moiety of human interferon-beta	13:60	Structure of the carbohydrate moiety of human interferon-beta secreted by a recombinant Chinese hamster ovary cell line.
3667593	5	26	theme	Gal	1022:1024	arg1	alpha					1041:1045	rat liver Gal beta 1-4GlcNAc alpha 2-6	1012:1049	rat liver Gal beta 1-4GlcNAc alpha 2-6 sialyltransferase	1012:1067	NeuAc, which is alpha 2-3-linked to galactose in the human IFN-beta secreted by Chinese hamster ovary cells, can be re-incorporated with an alpha 2-6 linkage in vitro, into enzymatically desialylated IFN-beta using rat liver Gal beta 1-4GlcNAc alpha 2-6 sialyltransferase.
3667593	5	27	attach	2-3-linked	819:828	arg2	NeuAc					797:801	NeuAc	797:801	NeuAc	797:801	NeuAc, which is alpha 2-3-linked to galactose in the human IFN-beta secreted by Chinese hamster ovary cells, can be re-incorporated with an alpha 2-6 linkage in vitro, into enzymatically desialylated IFN-beta using rat liver Gal beta 1-4GlcNAc alpha 2-6 sialyltransferase.
3667593	5	27	attach	2-3-linked	819:828	arg1	galactose					833:841	galactose	833:841	galactose in the human IFN-beta secreted by Chinese hamster ovary cells	833:903	NeuAc, which is alpha 2-3-linked to galactose in the human IFN-beta secreted by Chinese hamster ovary cells, can be re-incorporated with an alpha 2-6 linkage in vitro, into enzymatically desialylated IFN-beta using rat liver Gal beta 1-4GlcNAc alpha 2-6 sialyltransferase.
3667593	5	28	theme	1-4GlcNAc	1031:1039	arg1	alpha					1041:1045	rat liver Gal beta 1-4GlcNAc alpha 2-6	1012:1049	rat liver Gal beta 1-4GlcNAc alpha 2-6 sialyltransferase	1012:1067	NeuAc, which is alpha 2-3-linked to galactose in the human IFN-beta secreted by Chinese hamster ovary cells, can be re-incorporated with an alpha 2-6 linkage in vitro, into enzymatically desialylated IFN-beta using rat liver Gal beta 1-4GlcNAc alpha 2-6 sialyltransferase.
3667593	5	29	theme	human	850:854	arg1	IFN-beta					856:863	the human IFN-beta	846:863	the human IFN-beta secreted by Chinese hamster ovary cells	846:903	NeuAc, which is alpha 2-3-linked to galactose in the human IFN-beta secreted by Chinese hamster ovary cells, can be re-incorporated with an alpha 2-6 linkage in vitro, into enzymatically desialylated IFN-beta using rat liver Gal beta 1-4GlcNAc alpha 2-6 sialyltransferase.
3667593	2	30	theme	sequential	365:374	arg1	treatment					391:399	sequential exoglycosidase treatment	365:399	sequential exoglycosidase treatment	365:399	Analysis of the glycopeptidase F-released carbohydrates by sequential exoglycosidase treatment, methylation analysis, and fast atom bombardment-mass spectrometry revealed that 95% of the IFN-beta oligosaccharides had the following structure: (Formula: see text).
3667593	2	31	theme	bombardment-mass	438:453	arg1	spectrometry					455:466	fast atom bombardment-mass spectrometry	428:466	fast atom bombardment-mass spectrometry	428:466	Analysis of the glycopeptidase F-released carbohydrates by sequential exoglycosidase treatment, methylation analysis, and fast atom bombardment-mass spectrometry revealed that 95% of the IFN-beta oligosaccharides had the following structure: (Formula: see text).
3667593	2	32	theme	oligosaccharides	502:517	arg1	%					484:484	95%	482:484	95% of the IFN-beta oligosaccharides	482:517	Analysis of the glycopeptidase F-released carbohydrates by sequential exoglycosidase treatment, methylation analysis, and fast atom bombardment-mass spectrometry revealed that 95% of the IFN-beta oligosaccharides had the following structure: (Formula: see text).
3667593	2	32	theme	oligosaccharides	502:517	arg1	oligosaccharides					502:517	the IFN-beta oligosaccharides	489:517	the IFN-beta oligosaccharides	489:517	Analysis of the glycopeptidase F-released carbohydrates by sequential exoglycosidase treatment, methylation analysis, and fast atom bombardment-mass spectrometry revealed that 95% of the IFN-beta oligosaccharides had the following structure: (Formula: see text).
3667593	5	33	theme	alpha	937:941	arg1	linkage					947:953	an alpha 2-6 linkage	934:953	an alpha 2-6 linkage	934:953	NeuAc, which is alpha 2-3-linked to galactose in the human IFN-beta secreted by Chinese hamster ovary cells, can be re-incorporated with an alpha 2-6 linkage in vitro, into enzymatically desialylated IFN-beta using rat liver Gal beta 1-4GlcNAc alpha 2-6 sialyltransferase.
3667593	3	34	theme	carbohydrates	593:605	arg1	carbohydrates					593:605	the carbohydrates	589:605	the carbohydrates	589:605	The remaining 5% of the carbohydrates are probably tri- or higher antennary oligosaccharide chains.
3667593	3	34	theme	carbohydrates	593:605	arg1	tri-					620:623	tri-	620:623	tri-	620:623	The remaining 5% of the carbohydrates are probably tri- or higher antennary oligosaccharide chains.
3667593	3	34	theme	carbohydrates	593:605	arg1	%					584:584	The remaining 5%	569:584	The remaining 5% of the carbohydrates	569:605	The remaining 5% of the carbohydrates are probably tri- or higher antennary oligosaccharide chains.
3667593	2	35	theme	methylation	402:412	arg1	analysis					414:421	methylation analysis	402:421	methylation analysis	402:421	Analysis of the glycopeptidase F-released carbohydrates by sequential exoglycosidase treatment, methylation analysis, and fast atom bombardment-mass spectrometry revealed that 95% of the IFN-beta oligosaccharides had the following structure: (Formula: see text).
3667593	2	36	theme	atom	433:436	arg1	spectrometry					455:466	fast atom bombardment-mass spectrometry	428:466	fast atom bombardment-mass spectrometry	428:466	Analysis of the glycopeptidase F-released carbohydrates by sequential exoglycosidase treatment, methylation analysis, and fast atom bombardment-mass spectrometry revealed that 95% of the IFN-beta oligosaccharides had the following structure: (Formula: see text).
3667593	2	37	theme	IFN-beta	493:500	arg1	oligosaccharides					502:517	the IFN-beta oligosaccharides	489:517	the IFN-beta oligosaccharides	489:517	Analysis of the glycopeptidase F-released carbohydrates by sequential exoglycosidase treatment, methylation analysis, and fast atom bombardment-mass spectrometry revealed that 95% of the IFN-beta oligosaccharides had the following structure: (Formula: see text).
3667593	0	38	theme	moiety	30:35	arg1	Structure					0:8	Structure	0:8	Structure of the carbohydrate moiety of human interferon-beta	0:60	Structure of the carbohydrate moiety of human interferon-beta secreted by a recombinant Chinese hamster ovary cell line.
3667593	3	39	theme	antennary	635:643	arg1	chains					661:666	higher antennary oligosaccharide chains	628:666	higher antennary oligosaccharide chains	628:666	The remaining 5% of the carbohydrates are probably tri- or higher antennary oligosaccharide chains.
3667593	5	40	theme	alpha	1041:1045	arg1	sialyltransferase					1051:1067	rat liver Gal beta 1-4GlcNAc alpha 2-6 sialyltransferase	1012:1067	rat liver Gal beta 1-4GlcNAc alpha 2-6 sialyltransferase	1012:1067	NeuAc, which is alpha 2-3-linked to galactose in the human IFN-beta secreted by Chinese hamster ovary cells, can be re-incorporated with an alpha 2-6 linkage in vitro, into enzymatically desialylated IFN-beta using rat liver Gal beta 1-4GlcNAc alpha 2-6 sialyltransferase.
3667593	2	41	contain	had	519:521	arg1	%					484:484	95%	482:484	95% of the IFN-beta oligosaccharides	482:517	Analysis of the glycopeptidase F-released carbohydrates by sequential exoglycosidase treatment, methylation analysis, and fast atom bombardment-mass spectrometry revealed that 95% of the IFN-beta oligosaccharides had the following structure: (Formula: see text).
3667593	2	41	contain	had	519:521	arg2	structure					537:545	the following structure	523:545	the following structure	523:545	Analysis of the glycopeptidase F-released carbohydrates by sequential exoglycosidase treatment, methylation analysis, and fast atom bombardment-mass spectrometry revealed that 95% of the IFN-beta oligosaccharides had the following structure: (Formula: see text).
3667593	2	41	contain	had	519:521	arg1	oligosaccharides					502:517	the IFN-beta oligosaccharides	489:517	the IFN-beta oligosaccharides	489:517	Analysis of the glycopeptidase F-released carbohydrates by sequential exoglycosidase treatment, methylation analysis, and fast atom bombardment-mass spectrometry revealed that 95% of the IFN-beta oligosaccharides had the following structure: (Formula: see text).
3667593	2	42	theme	fast	428:431	arg1	spectrometry					455:466	fast atom bombardment-mass spectrometry	428:466	fast atom bombardment-mass spectrometry	428:466	Analysis of the glycopeptidase F-released carbohydrates by sequential exoglycosidase treatment, methylation analysis, and fast atom bombardment-mass spectrometry revealed that 95% of the IFN-beta oligosaccharides had the following structure: (Formula: see text).
3667593	0	43	theme	interferon-beta	46:60	arg1	moiety					30:35	the carbohydrate moiety	13:35	the carbohydrate moiety of human interferon-beta	13:60	Structure of the carbohydrate moiety of human interferon-beta secreted by a recombinant Chinese hamster ovary cell line.
3667593	3	44	theme	oligosaccharide	645:659	arg1	chains					661:666	higher antennary oligosaccharide chains	628:666	higher antennary oligosaccharide chains	628:666	The remaining 5% of the carbohydrates are probably tri- or higher antennary oligosaccharide chains.
3667593	5	45	theme	hamster	885:891	arg1	cells					899:903	Chinese hamster ovary cells	877:903	Chinese hamster ovary cells	877:903	NeuAc, which is alpha 2-3-linked to galactose in the human IFN-beta secreted by Chinese hamster ovary cells, can be re-incorporated with an alpha 2-6 linkage in vitro, into enzymatically desialylated IFN-beta using rat liver Gal beta 1-4GlcNAc alpha 2-6 sialyltransferase.
3667593	0	46	theme	human	40:44	arg1	interferon-beta					46:60	human interferon-beta	40:60	human interferon-beta	40:60	Structure of the carbohydrate moiety of human interferon-beta secreted by a recombinant Chinese hamster ovary cell line.
3667593	2	47	theme	carbohydrates	348:360	arg1	Analysis					306:313	Analysis	306:313	Analysis of the glycopeptidase F-released carbohydrates by sequential exoglycosidase treatment, methylation analysis, and fast atom bombardment-mass spectrometry	306:466	Analysis of the glycopeptidase F-released carbohydrates by sequential exoglycosidase treatment, methylation analysis, and fast atom bombardment-mass spectrometry revealed that 95% of the IFN-beta oligosaccharides had the following structure: (Formula: see text).
3667593	5	48	theme	rat	1012:1014	arg1	alpha					1041:1045	rat liver Gal beta 1-4GlcNAc alpha 2-6	1012:1049	rat liver Gal beta 1-4GlcNAc alpha 2-6 sialyltransferase	1012:1067	NeuAc, which is alpha 2-3-linked to galactose in the human IFN-beta secreted by Chinese hamster ovary cells, can be re-incorporated with an alpha 2-6 linkage in vitro, into enzymatically desialylated IFN-beta using rat liver Gal beta 1-4GlcNAc alpha 2-6 sialyltransferase.
3667593	2	49	theme	F-released	337:346	arg1	carbohydrates					348:360	the glycopeptidase F-released carbohydrates	318:360	the glycopeptidase F-released carbohydrates	318:360	Analysis of the glycopeptidase F-released carbohydrates by sequential exoglycosidase treatment, methylation analysis, and fast atom bombardment-mass spectrometry revealed that 95% of the IFN-beta oligosaccharides had the following structure: (Formula: see text).
3667593	4	50	theme	IFN-beta	714:721	arg1	homogeneous					737:747	homogeneous	737:747	homogeneous	737:747	The major oligosaccharide of the recombinant IFN-beta is remarkably homogeneous with respect to terminal galactose sialylation.
3667593	4	50	theme	IFN-beta	714:721	arg1	oligosaccharide					679:693	The major oligosaccharide	669:693	The major oligosaccharide of the recombinant IFN-beta	669:721	The major oligosaccharide of the recombinant IFN-beta is remarkably homogeneous with respect to terminal galactose sialylation.
3667593	3	51	theme	higher	628:633	arg1	chains					661:666	higher antennary oligosaccharide chains	628:666	higher antennary oligosaccharide chains	628:666	The remaining 5% of the carbohydrates are probably tri- or higher antennary oligosaccharide chains.
3667593	4	52	theme	galactose	774:782	arg1	sialylation					784:794	terminal galactose sialylation	765:794	terminal galactose sialylation	765:794	The major oligosaccharide of the recombinant IFN-beta is remarkably homogeneous with respect to terminal galactose sialylation.
3667593	1	53	theme	carbohydrate	125:136	arg1	structure					138:146	The carbohydrate structure	121:146	The carbohydrate structure of the major oligosaccharide of human interferon-beta (IFN-beta) synthesized by a genetically engineered Chinese hamster ovary cell line	121:283	The carbohydrate structure of the major oligosaccharide of human interferon-beta (IFN-beta) synthesized by a genetically engineered Chinese hamster ovary cell line has been determined.
3667593	5	54	gly	desialylated	984:995	arg1	IFN-beta					997:1004	enzymatically desialylated IFN-beta	970:1004	enzymatically desialylated IFN-beta using rat liver Gal beta 1-4GlcNAc alpha 2-6 sialyltransferase	970:1067	NeuAc, which is alpha 2-3-linked to galactose in the human IFN-beta secreted by Chinese hamster ovary cells, can be re-incorporated with an alpha 2-6 linkage in vitro, into enzymatically desialylated IFN-beta using rat liver Gal beta 1-4GlcNAc alpha 2-6 sialyltransferase.
3667593	5	55	theme	Chinese	877:883	arg1	cells					899:903	Chinese hamster ovary cells	877:903	Chinese hamster ovary cells	877:903	NeuAc, which is alpha 2-3-linked to galactose in the human IFN-beta secreted by Chinese hamster ovary cells, can be re-incorporated with an alpha 2-6 linkage in vitro, into enzymatically desialylated IFN-beta using rat liver Gal beta 1-4GlcNAc alpha 2-6 sialyltransferase.
3667593	2	56	dep	see	558:560	arg1	Formula					549:555	Formula	549:555	Formula	549:555	Analysis of the glycopeptidase F-released carbohydrates by sequential exoglycosidase treatment, methylation analysis, and fast atom bombardment-mass spectrometry revealed that 95% of the IFN-beta oligosaccharides had the following structure: (Formula: see text).
3667593	6	57	with	deglycosylation	1196:1210	arg1	F					1232:1232	glycopeptidase F	1217:1232	glycopeptidase F	1217:1232	The sugar chain is important for maintaining protein solubility as shown by the fact that IFN-beta protein precipitates after deglycosylation with glycopeptidase F.
3667593	4	58	theme	recombinant	702:712	arg1	IFN-beta					714:721	the recombinant IFN-beta	698:721	the recombinant IFN-beta	698:721	The major oligosaccharide of the recombinant IFN-beta is remarkably homogeneous with respect to terminal galactose sialylation.
3667593	2	59	theme	following	527:535	arg1	structure					537:545	the following structure	523:545	the following structure	523:545	Analysis of the glycopeptidase F-released carbohydrates by sequential exoglycosidase treatment, methylation analysis, and fast atom bombardment-mass spectrometry revealed that 95% of the IFN-beta oligosaccharides had the following structure: (Formula: see text).
3667593	6	60	theme	IFN-beta	1160:1167	arg1	protein					1169:1175	IFN-beta protein	1160:1175	IFN-beta protein	1160:1175	The sugar chain is important for maintaining protein solubility as shown by the fact that IFN-beta protein precipitates after deglycosylation with glycopeptidase F.
3667593	5	61	theme	beta	1026:1029	arg1	alpha					1041:1045	rat liver Gal beta 1-4GlcNAc alpha 2-6	1012:1049	rat liver Gal beta 1-4GlcNAc alpha 2-6 sialyltransferase	1012:1067	NeuAc, which is alpha 2-3-linked to galactose in the human IFN-beta secreted by Chinese hamster ovary cells, can be re-incorporated with an alpha 2-6 linkage in vitro, into enzymatically desialylated IFN-beta using rat liver Gal beta 1-4GlcNAc alpha 2-6 sialyltransferase.
3667593	1	62	theme	engineered	242:251	arg1	line					280:283	a genetically engineered Chinese hamster ovary cell line	228:283	a genetically engineered Chinese hamster ovary cell line	228:283	The carbohydrate structure of the major oligosaccharide of human interferon-beta (IFN-beta) synthesized by a genetically engineered Chinese hamster ovary cell line has been determined.
7240157	0	0	theme	glycopeptide	94:105	arg1	preparations					107:118	glycopeptide preparations	94:118	glycopeptide preparations	94:118	Characterization of the microheterogeneity in glycoproteins by 500-MHz 1H-NMR spectroscopy of glycopeptide preparations.
7240157	1	1	theme	human	197:201	arg1	glycoprotein					223:234	human plasma alpha 1-acid glycoprotein	197:234	human plasma alpha 1-acid glycoprotein	197:234	Application to a monofucosylated tetra-antennary glycopeptide fraction from human plasma alpha 1-acid glycoprotein.
7240157	6	2	theme	Fuc	958:960	arg1	alpha-					962:967	Fuc alpha-	958:967	Fuc alpha-	958:967	The major form contains Fuc alpha-(1 leads to 3) linked to GlcNac 7 of the tetra-antennary structure, as shown earlier.
7240157	7	3	theme	alpha-	1132:1137	arg1	linkage					1153:1159	alpha-(1 leads to 3) linkage	1132:1159	alpha-(1 leads to 3) linkage to GlcNAc 7' or 5'	1132:1178	The two minor compounds, representing new structures, possess Fuc attached in alpha-(1 leads to 3) linkage to GlcNAc 7' or 5'.
7240157	4	4	theme	type	815:818	arg1	elucidation					794:804	the elucidation	790:804	the elucidation of a new type of microheterogeneity	790:840	The combination of the improved resolving power and the enhanced sensitivity of the 500-MHz 1H-NMR spectrometer afforded the elucidation of a new type of microheterogeneity with regard to the position of attachment of Fuc.
7240157	1	5	theme	plasma	203:208	arg1	glycoprotein					223:234	human plasma alpha 1-acid glycoprotein	197:234	human plasma alpha 1-acid glycoprotein	197:234	Application to a monofucosylated tetra-antennary glycopeptide fraction from human plasma alpha 1-acid glycoprotein.
7240157	8	6	theme	glycopeptide	1314:1325	arg1	mixture					1327:1333	a glycopeptide mixture	1312:1333	a glycopeptide mixture	1312:1333	It is thus noteworthy that this spectral technique allows elucidation of structures of very closely related carbohydrate chains in a glycopeptide mixture.
7240157	6	7	theme	tetra-antennary	1009:1023	arg1	structure					1025:1033	the tetra-antennary structure	1005:1033	the tetra-antennary structure	1005:1033	The major form contains Fuc alpha-(1 leads to 3) linked to GlcNac 7 of the tetra-antennary structure, as shown earlier.
7240157	0	8	from	Characterization	0:15	arg1	glycoproteins					46:58	glycoproteins	46:58	glycoproteins	46:58	Characterization of the microheterogeneity in glycoproteins by 500-MHz 1H-NMR spectroscopy of glycopeptide preparations.
7240157	8	9	theme	carbohydrate	1289:1300	arg1	chains					1302:1307	very closely related carbohydrate chains	1268:1307	very closely related carbohydrate chains	1268:1307	It is thus noteworthy that this spectral technique allows elucidation of structures of very closely related carbohydrate chains in a glycopeptide mixture.
7240157	3	10	theme	360-MHz	469:475	arg1	analysis					498:505	360-MHz 1H-NMR spectroscopic analysis	469:505	360-MHz 1H-NMR spectroscopic analysis (Fournet, B., Montreuil, J., Strecker, G., Dorland, L., Haverkamp, J., Vliegenthart, J. F. G., Binette, J. P., and Schmid, K. (1978) Biochemistry 17, 5206-5214)	469:666	This fraction was earlier judged to be homogeneous by 360-MHz 1H-NMR spectroscopic analysis (Fournet, B., Montreuil, J., Strecker, G., Dorland, L., Haverkamp, J., Vliegenthart, J. F. G., Binette, J. P., and Schmid, K. (1978) Biochemistry 17, 5206-5214).
7240157	0	11	theme	preparations	107:118	arg1	spectroscopy					78:89	500-MHz 1H-NMR spectroscopy	63:89	500-MHz 1H-NMR spectroscopy of glycopeptide preparations	63:118	Characterization of the microheterogeneity in glycoproteins by 500-MHz 1H-NMR spectroscopy of glycopeptide preparations.
7240157	1	12	gly	glycoprotein	223:234	arg1	glycoprotein					223:234	human plasma alpha 1-acid glycoprotein	197:234	human plasma alpha 1-acid glycoprotein	197:234	Application to a monofucosylated tetra-antennary glycopeptide fraction from human plasma alpha 1-acid glycoprotein.
7240157	4	13	theme	power	711:715	arg1	sensitivity					734:744	the enhanced sensitivity	721:744	the enhanced sensitivity of the 500-MHz 1H-NMR spectrometer	721:779	The combination of the improved resolving power and the enhanced sensitivity of the 500-MHz 1H-NMR spectrometer afforded the elucidation of a new type of microheterogeneity with regard to the position of attachment of Fuc.
7240157	4	13	theme	power	711:715	arg1	combination					673:683	The combination	669:683	The combination of the improved resolving power	669:715	The combination of the improved resolving power and the enhanced sensitivity of the 500-MHz 1H-NMR spectrometer afforded the elucidation of a new type of microheterogeneity with regard to the position of attachment of Fuc.
7240157	2	14	theme	1-acid	394:399	arg1	glycoprotein					401:412	human plasma alpha 1-acid glycoprotein	375:412	human plasma alpha 1-acid glycoprotein	375:412	Five hundred-MHz 1H-NMR spectroscopy was employed to study a monofucosylated tetra-antennary glycopeptide fraction which was derived from human plasma alpha 1-acid glycoprotein.
7240157	4	15	theme	enhanced	725:732	arg1	sensitivity					734:744	the enhanced sensitivity	721:744	the enhanced sensitivity of the 500-MHz 1H-NMR spectrometer	721:779	The combination of the improved resolving power and the enhanced sensitivity of the 500-MHz 1H-NMR spectrometer afforded the elucidation of a new type of microheterogeneity with regard to the position of attachment of Fuc.
7240157	1	16	theme	alpha	210:214	arg1	glycoprotein					223:234	human plasma alpha 1-acid glycoprotein	197:234	human plasma alpha 1-acid glycoprotein	197:234	Application to a monofucosylated tetra-antennary glycopeptide fraction from human plasma alpha 1-acid glycoprotein.
7240157	6	17	theme	major	938:942	arg1	form					944:947	The major form	934:947	The major form	934:947	The major form contains Fuc alpha-(1 leads to 3) linked to GlcNac 7 of the tetra-antennary structure, as shown earlier.
7240157	0	18	from	glycoproteins	46:58	arg1	Characterization					0:15	Characterization	0:15	Characterization of the microheterogeneity in glycoproteins by 500-MHz 1H-NMR spectroscopy of glycopeptide preparations.	0:119	Characterization of the microheterogeneity in glycoproteins by 500-MHz 1H-NMR spectroscopy of glycopeptide preparations.
7240157	7	19	theme	minor	1062:1066	arg1	compounds					1068:1076	The two minor compounds	1054:1076	The two minor compounds	1054:1076	The two minor compounds, representing new structures, possess Fuc attached in alpha-(1 leads to 3) linkage to GlcNAc 7' or 5'.
7240157	0	20	gly	glycopeptide	94:105	arg2	glycopeptide					94:105	glycopeptide preparations	94:118	glycopeptide preparations	94:118	Characterization of the microheterogeneity in glycoproteins by 500-MHz 1H-NMR spectroscopy of glycopeptide preparations.
7240157	4	21	theme	Fuc	887:889	arg1	attachment					873:882	attachment	873:882	attachment of Fuc	873:889	The combination of the improved resolving power and the enhanced sensitivity of the 500-MHz 1H-NMR spectrometer afforded the elucidation of a new type of microheterogeneity with regard to the position of attachment of Fuc.
7240157	1	22	theme	1-acid	216:221	arg1	glycoprotein					223:234	human plasma alpha 1-acid glycoprotein	197:234	human plasma alpha 1-acid glycoprotein	197:234	Application to a monofucosylated tetra-antennary glycopeptide fraction from human plasma alpha 1-acid glycoprotein.
7240157	7	23	theme	new	1092:1094	arg1	structures					1096:1105	new structures	1092:1105	new structures	1092:1105	The two minor compounds, representing new structures, possess Fuc attached in alpha-(1 leads to 3) linkage to GlcNAc 7' or 5'.
7240157	8	24	theme	related	1281:1287	arg1	chains					1302:1307	very closely related carbohydrate chains	1268:1307	very closely related carbohydrate chains	1268:1307	It is thus noteworthy that this spectral technique allows elucidation of structures of very closely related carbohydrate chains in a glycopeptide mixture.
7240157	4	25	theme	new	811:813	arg1	type					815:818	a new type	809:818	a new type of microheterogeneity	809:840	The combination of the improved resolving power and the enhanced sensitivity of the 500-MHz 1H-NMR spectrometer afforded the elucidation of a new type of microheterogeneity with regard to the position of attachment of Fuc.
7240157	2	26	theme	alpha	388:392	arg1	glycoprotein					401:412	human plasma alpha 1-acid glycoprotein	375:412	human plasma alpha 1-acid glycoprotein	375:412	Five hundred-MHz 1H-NMR spectroscopy was employed to study a monofucosylated tetra-antennary glycopeptide fraction which was derived from human plasma alpha 1-acid glycoprotein.
7240157	2	27	gly	glycopeptide	330:341	arg2	glycopeptide					330:341	a monofucosylated tetra-antennary glycopeptide fraction	296:350	a monofucosylated tetra-antennary glycopeptide fraction which was derived from human plasma alpha 1-acid glycoprotein	296:412	Five hundred-MHz 1H-NMR spectroscopy was employed to study a monofucosylated tetra-antennary glycopeptide fraction which was derived from human plasma alpha 1-acid glycoprotein.
7240157	3	28	dep	analysis	498:505	arg1	K					630:630	K	630:630	K	630:630	This fraction was earlier judged to be homogeneous by 360-MHz 1H-NMR spectroscopic analysis (Fournet, B., Montreuil, J., Strecker, G., Dorland, L., Haverkamp, J., Vliegenthart, J. F. G., Binette, J. P., and Schmid, K. (1978) Biochemistry 17, 5206-5214).
7240157	3	28	dep	analysis	498:505	arg1	Schmid					622:627	Schmid	622:627	Schmid	622:627	This fraction was earlier judged to be homogeneous by 360-MHz 1H-NMR spectroscopic analysis (Fournet, B., Montreuil, J., Strecker, G., Dorland, L., Haverkamp, J., Vliegenthart, J. F. G., Binette, J. P., and Schmid, K. (1978) Biochemistry 17, 5206-5214).
7240157	3	28	dep	analysis	498:505	arg1	L.					559:560	L.	559:560	L.	559:560	This fraction was earlier judged to be homogeneous by 360-MHz 1H-NMR spectroscopic analysis (Fournet, B., Montreuil, J., Strecker, G., Dorland, L., Haverkamp, J., Vliegenthart, J. F. G., Binette, J. P., and Schmid, K. (1978) Biochemistry 17, 5206-5214).
7240157	3	28	dep	analysis	498:505	arg1	B.					517:518	B.	517:518	B.	517:518	This fraction was earlier judged to be homogeneous by 360-MHz 1H-NMR spectroscopic analysis (Fournet, B., Montreuil, J., Strecker, G., Dorland, L., Haverkamp, J., Vliegenthart, J. F. G., Binette, J. P., and Schmid, K. (1978) Biochemistry 17, 5206-5214).
7240157	3	28	dep	analysis	498:505	arg1	J.					592:593	J.	592:593	J.	592:593	This fraction was earlier judged to be homogeneous by 360-MHz 1H-NMR spectroscopic analysis (Fournet, B., Montreuil, J., Strecker, G., Dorland, L., Haverkamp, J., Vliegenthart, J. F. G., Binette, J. P., and Schmid, K. (1978) Biochemistry 17, 5206-5214).
7240157	3	28	dep	analysis	498:505	arg1	Binette					602:608	Binette	602:608	Binette	602:608	This fraction was earlier judged to be homogeneous by 360-MHz 1H-NMR spectroscopic analysis (Fournet, B., Montreuil, J., Strecker, G., Dorland, L., Haverkamp, J., Vliegenthart, J. F. G., Binette, J. P., and Schmid, K. (1978) Biochemistry 17, 5206-5214).
7240157	3	28	dep	analysis	498:505	arg1	J.					611:612	J.	611:612	J.	611:612	This fraction was earlier judged to be homogeneous by 360-MHz 1H-NMR spectroscopic analysis (Fournet, B., Montreuil, J., Strecker, G., Dorland, L., Haverkamp, J., Vliegenthart, J. F. G., Binette, J. P., and Schmid, K. (1978) Biochemistry 17, 5206-5214).
7240157	3	28	dep	analysis	498:505	arg1	G.					546:547	G.	546:547	G.	546:547	This fraction was earlier judged to be homogeneous by 360-MHz 1H-NMR spectroscopic analysis (Fournet, B., Montreuil, J., Strecker, G., Dorland, L., Haverkamp, J., Vliegenthart, J. F. G., Binette, J. P., and Schmid, K. (1978) Biochemistry 17, 5206-5214).
7240157	3	28	dep	analysis	498:505	arg1	P.					614:615	P.	614:615	P.	614:615	This fraction was earlier judged to be homogeneous by 360-MHz 1H-NMR spectroscopic analysis (Fournet, B., Montreuil, J., Strecker, G., Dorland, L., Haverkamp, J., Vliegenthart, J. F. G., Binette, J. P., and Schmid, K. (1978) Biochemistry 17, 5206-5214).
7240157	3	28	dep	analysis	498:505	arg1	Montreuil					521:529	Montreuil	521:529	Montreuil	521:529	This fraction was earlier judged to be homogeneous by 360-MHz 1H-NMR spectroscopic analysis (Fournet, B., Montreuil, J., Strecker, G., Dorland, L., Haverkamp, J., Vliegenthart, J. F. G., Binette, J. P., and Schmid, K. (1978) Biochemistry 17, 5206-5214).
7240157	3	28	dep	analysis	498:505	arg1	J.					574:575	J.	574:575	J.	574:575	This fraction was earlier judged to be homogeneous by 360-MHz 1H-NMR spectroscopic analysis (Fournet, B., Montreuil, J., Strecker, G., Dorland, L., Haverkamp, J., Vliegenthart, J. F. G., Binette, J. P., and Schmid, K. (1978) Biochemistry 17, 5206-5214).
7240157	3	28	dep	analysis	498:505	arg1	1978					634:637	1978	634:637	1978	634:637	This fraction was earlier judged to be homogeneous by 360-MHz 1H-NMR spectroscopic analysis (Fournet, B., Montreuil, J., Strecker, G., Dorland, L., Haverkamp, J., Vliegenthart, J. F. G., Binette, J. P., and Schmid, K. (1978) Biochemistry 17, 5206-5214).
7240157	3	28	dep	analysis	498:505	arg1	J.					532:533	J.	532:533	J.	532:533	This fraction was earlier judged to be homogeneous by 360-MHz 1H-NMR spectroscopic analysis (Fournet, B., Montreuil, J., Strecker, G., Dorland, L., Haverkamp, J., Vliegenthart, J. F. G., Binette, J. P., and Schmid, K. (1978) Biochemistry 17, 5206-5214).
7240157	2	29	theme	plasma	381:386	arg1	glycoprotein					401:412	human plasma alpha 1-acid glycoprotein	375:412	human plasma alpha 1-acid glycoprotein	375:412	Five hundred-MHz 1H-NMR spectroscopy was employed to study a monofucosylated tetra-antennary glycopeptide fraction which was derived from human plasma alpha 1-acid glycoprotein.
7240157	8	30	theme	spectral	1213:1220	arg1	technique					1222:1230	this spectral technique	1208:1230	this spectral technique	1208:1230	It is thus noteworthy that this spectral technique allows elucidation of structures of very closely related carbohydrate chains in a glycopeptide mixture.
7240157	0	31	theme	microheterogeneity	24:41	arg1	Characterization					0:15	Characterization	0:15	Characterization of the microheterogeneity in glycoproteins by 500-MHz 1H-NMR spectroscopy of glycopeptide preparations.	0:119	Characterization of the microheterogeneity in glycoproteins by 500-MHz 1H-NMR spectroscopy of glycopeptide preparations.
7240157	4	32	theme	500-MHz	753:759	arg1	spectrometer					768:779	the 500-MHz 1H-NMR spectrometer	749:779	the 500-MHz 1H-NMR spectrometer	749:779	The combination of the improved resolving power and the enhanced sensitivity of the 500-MHz 1H-NMR spectrometer afforded the elucidation of a new type of microheterogeneity with regard to the position of attachment of Fuc.
7240157	1	33	gly	monofucosylated	138:152	arg1	fraction					183:190	a monofucosylated tetra-antennary glycopeptide fraction	136:190	a monofucosylated tetra-antennary glycopeptide fraction from human plasma alpha 1-acid glycoprotein	136:234	Application to a monofucosylated tetra-antennary glycopeptide fraction from human plasma alpha 1-acid glycoprotein.
7240157	2	34	theme	human	375:379	arg1	glycoprotein					401:412	human plasma alpha 1-acid glycoprotein	375:412	human plasma alpha 1-acid glycoprotein	375:412	Five hundred-MHz 1H-NMR spectroscopy was employed to study a monofucosylated tetra-antennary glycopeptide fraction which was derived from human plasma alpha 1-acid glycoprotein.
7240157	2	35	gly	monofucosylated	298:312	arg1	fraction					343:350	a monofucosylated tetra-antennary glycopeptide fraction	296:350	a monofucosylated tetra-antennary glycopeptide fraction which was derived from human plasma alpha 1-acid glycoprotein	296:412	Five hundred-MHz 1H-NMR spectroscopy was employed to study a monofucosylated tetra-antennary glycopeptide fraction which was derived from human plasma alpha 1-acid glycoprotein.
7240157	7	36	dep	alpha-	1132:1137	arg1	leads					1141:1145	leads	1141:1145	leads to 3	1141:1150	The two minor compounds, representing new structures, possess Fuc attached in alpha-(1 leads to 3) linkage to GlcNAc 7' or 5'.
7240157	5	37	theme	isomeric	898:905	arg1	compounds					907:915	Three isomeric compounds	892:915	Three isomeric compounds	892:915	Three isomeric compounds were identified.
7240157	4	38	theme	improved	692:699	arg1	power					711:715	the improved resolving power	688:715	the improved resolving power	688:715	The combination of the improved resolving power and the enhanced sensitivity of the 500-MHz 1H-NMR spectrometer afforded the elucidation of a new type of microheterogeneity with regard to the position of attachment of Fuc.
7240157	3	39	theme	spectroscopic	484:496	arg1	analysis					498:505	360-MHz 1H-NMR spectroscopic analysis	469:505	360-MHz 1H-NMR spectroscopic analysis (Fournet, B., Montreuil, J., Strecker, G., Dorland, L., Haverkamp, J., Vliegenthart, J. F. G., Binette, J. P., and Schmid, K. (1978) Biochemistry 17, 5206-5214)	469:666	This fraction was earlier judged to be homogeneous by 360-MHz 1H-NMR spectroscopic analysis (Fournet, B., Montreuil, J., Strecker, G., Dorland, L., Haverkamp, J., Vliegenthart, J. F. G., Binette, J. P., and Schmid, K. (1978) Biochemistry 17, 5206-5214).
7240157	1	40	gly	glycopeptide	170:181	arg2	glycopeptide					170:181	a monofucosylated tetra-antennary glycopeptide fraction	136:190	a monofucosylated tetra-antennary glycopeptide fraction from human plasma alpha 1-acid glycoprotein	136:234	Application to a monofucosylated tetra-antennary glycopeptide fraction from human plasma alpha 1-acid glycoprotein.
7240157	4	41	theme	spectrometer	768:779	arg1	sensitivity					734:744	the enhanced sensitivity	721:744	the enhanced sensitivity of the 500-MHz 1H-NMR spectrometer	721:779	The combination of the improved resolving power and the enhanced sensitivity of the 500-MHz 1H-NMR spectrometer afforded the elucidation of a new type of microheterogeneity with regard to the position of attachment of Fuc.
7240157	4	41	theme	spectrometer	768:779	arg1	combination					673:683	The combination	669:683	The combination of the improved resolving power	669:715	The combination of the improved resolving power and the enhanced sensitivity of the 500-MHz 1H-NMR spectrometer afforded the elucidation of a new type of microheterogeneity with regard to the position of attachment of Fuc.
7240157	4	42	theme	1H-NMR	761:766	arg1	spectrometer					768:779	the 500-MHz 1H-NMR spectrometer	749:779	the 500-MHz 1H-NMR spectrometer	749:779	The combination of the improved resolving power and the enhanced sensitivity of the 500-MHz 1H-NMR spectrometer afforded the elucidation of a new type of microheterogeneity with regard to the position of attachment of Fuc.
7240157	7	43	attach	attached	1120:1127	arg3	linkage					1153:1159	alpha-(1 leads to 3) linkage	1132:1159	alpha-(1 leads to 3) linkage to GlcNAc 7' or 5'	1132:1178	The two minor compounds, representing new structures, possess Fuc attached in alpha-(1 leads to 3) linkage to GlcNAc 7' or 5'.
7240157	7	43	attach	attached	1120:1127	arg2	Fuc					1116:1118	Fuc	1116:1118	Fuc attached in alpha-(1 leads to 3) linkage to GlcNAc 7' or 5'	1116:1178	The two minor compounds, representing new structures, possess Fuc attached in alpha-(1 leads to 3) linkage to GlcNAc 7' or 5'.
7240157	0	44	theme	500-MHz	63:69	arg1	spectroscopy					78:89	500-MHz 1H-NMR spectroscopy	63:89	500-MHz 1H-NMR spectroscopy of glycopeptide preparations	63:118	Characterization of the microheterogeneity in glycoproteins by 500-MHz 1H-NMR spectroscopy of glycopeptide preparations.
7240157	2	45	attach	derived	362:368	arg2	fraction					343:350	a monofucosylated tetra-antennary glycopeptide fraction	296:350	a monofucosylated tetra-antennary glycopeptide fraction which was derived from human plasma alpha 1-acid glycoprotein	296:412	Five hundred-MHz 1H-NMR spectroscopy was employed to study a monofucosylated tetra-antennary glycopeptide fraction which was derived from human plasma alpha 1-acid glycoprotein.
7240157	2	45	attach	derived	362:368	arg1	glycoprotein					401:412	human plasma alpha 1-acid glycoprotein	375:412	human plasma alpha 1-acid glycoprotein	375:412	Five hundred-MHz 1H-NMR spectroscopy was employed to study a monofucosylated tetra-antennary glycopeptide fraction which was derived from human plasma alpha 1-acid glycoprotein.
7240157	3	46	theme	1H-NMR	477:482	arg1	analysis					498:505	360-MHz 1H-NMR spectroscopic analysis	469:505	360-MHz 1H-NMR spectroscopic analysis (Fournet, B., Montreuil, J., Strecker, G., Dorland, L., Haverkamp, J., Vliegenthart, J. F. G., Binette, J. P., and Schmid, K. (1978) Biochemistry 17, 5206-5214)	469:666	This fraction was earlier judged to be homogeneous by 360-MHz 1H-NMR spectroscopic analysis (Fournet, B., Montreuil, J., Strecker, G., Dorland, L., Haverkamp, J., Vliegenthart, J. F. G., Binette, J. P., and Schmid, K. (1978) Biochemistry 17, 5206-5214).
7240157	6	47	dep	contains	949:956	arg1	linked					983:988	linked	983:988	linked	983:988	The major form contains Fuc alpha-(1 leads to 3) linked to GlcNac 7 of the tetra-antennary structure, as shown earlier.
7240157	4	48	theme	attachment	873:882	arg1	position					861:868	the position	857:868	the position of attachment of Fuc	857:889	The combination of the improved resolving power and the enhanced sensitivity of the 500-MHz 1H-NMR spectrometer afforded the elucidation of a new type of microheterogeneity with regard to the position of attachment of Fuc.
7240157	8	49	theme	chains	1302:1307	arg1	structures					1254:1263	structures	1254:1263	structures of very closely related carbohydrate chains	1254:1307	It is thus noteworthy that this spectral technique allows elucidation of structures of very closely related carbohydrate chains in a glycopeptide mixture.
7240157	1	50	theme	monofucosylated	138:152	arg1	fraction					183:190	a monofucosylated tetra-antennary glycopeptide fraction	136:190	a monofucosylated tetra-antennary glycopeptide fraction from human plasma alpha 1-acid glycoprotein	136:234	Application to a monofucosylated tetra-antennary glycopeptide fraction from human plasma alpha 1-acid glycoprotein.
7240157	7	51	contain	possess	1108:1114	arg1	compounds					1068:1076	The two minor compounds	1054:1076	The two minor compounds	1054:1076	The two minor compounds, representing new structures, possess Fuc attached in alpha-(1 leads to 3) linkage to GlcNAc 7' or 5'.
7240157	7	51	contain	possess	1108:1114	arg2	Fuc					1116:1118	Fuc	1116:1118	Fuc attached in alpha-(1 leads to 3) linkage to GlcNAc 7' or 5'	1116:1178	The two minor compounds, representing new structures, possess Fuc attached in alpha-(1 leads to 3) linkage to GlcNAc 7' or 5'.
7240157	2	52	theme	1H-NMR	254:259	arg1	spectroscopy					261:272	Five hundred-MHz 1H-NMR spectroscopy	237:272	Five hundred-MHz 1H-NMR spectroscopy	237:272	Five hundred-MHz 1H-NMR spectroscopy was employed to study a monofucosylated tetra-antennary glycopeptide fraction which was derived from human plasma alpha 1-acid glycoprotein.
7240157	2	53	theme	glycopeptide	330:341	arg1	fraction					343:350	a monofucosylated tetra-antennary glycopeptide fraction	296:350	a monofucosylated tetra-antennary glycopeptide fraction which was derived from human plasma alpha 1-acid glycoprotein	296:412	Five hundred-MHz 1H-NMR spectroscopy was employed to study a monofucosylated tetra-antennary glycopeptide fraction which was derived from human plasma alpha 1-acid glycoprotein.
7240157	8	54	theme	structures	1254:1263	arg1	elucidation					1239:1249	elucidation	1239:1249	elucidation of structures of very closely related carbohydrate chains	1239:1307	It is thus noteworthy that this spectral technique allows elucidation of structures of very closely related carbohydrate chains in a glycopeptide mixture.
7240157	1	55	theme	tetra-antennary	154:168	arg1	fraction					183:190	a monofucosylated tetra-antennary glycopeptide fraction	136:190	a monofucosylated tetra-antennary glycopeptide fraction from human plasma alpha 1-acid glycoprotein	136:234	Application to a monofucosylated tetra-antennary glycopeptide fraction from human plasma alpha 1-acid glycoprotein.
7240157	4	56	theme	resolving	701:709	arg1	power					711:715	the improved resolving power	688:715	the improved resolving power	688:715	The combination of the improved resolving power and the enhanced sensitivity of the 500-MHz 1H-NMR spectrometer afforded the elucidation of a new type of microheterogeneity with regard to the position of attachment of Fuc.
7240157	2	57	gly	glycoprotein	401:412	arg1	glycoprotein					401:412	human plasma alpha 1-acid glycoprotein	375:412	human plasma alpha 1-acid glycoprotein	375:412	Five hundred-MHz 1H-NMR spectroscopy was employed to study a monofucosylated tetra-antennary glycopeptide fraction which was derived from human plasma alpha 1-acid glycoprotein.
7240157	2	58	theme	hundred-MHz	242:252	arg1	spectroscopy					261:272	Five hundred-MHz 1H-NMR spectroscopy	237:272	Five hundred-MHz 1H-NMR spectroscopy	237:272	Five hundred-MHz 1H-NMR spectroscopy was employed to study a monofucosylated tetra-antennary glycopeptide fraction which was derived from human plasma alpha 1-acid glycoprotein.
7240157	0	59	gly	glycoproteins	46:58	arg1	glycoproteins					46:58	glycoproteins	46:58	glycoproteins	46:58	Characterization of the microheterogeneity in glycoproteins by 500-MHz 1H-NMR spectroscopy of glycopeptide preparations.
7240157	1	60	from	glycoprotein	223:234	arg1	fraction					183:190	a monofucosylated tetra-antennary glycopeptide fraction	136:190	a monofucosylated tetra-antennary glycopeptide fraction from human plasma alpha 1-acid glycoprotein	136:234	Application to a monofucosylated tetra-antennary glycopeptide fraction from human plasma alpha 1-acid glycoprotein.
7240157	1	61	theme	glycopeptide	170:181	arg1	fraction					183:190	a monofucosylated tetra-antennary glycopeptide fraction	136:190	a monofucosylated tetra-antennary glycopeptide fraction from human plasma alpha 1-acid glycoprotein	136:234	Application to a monofucosylated tetra-antennary glycopeptide fraction from human plasma alpha 1-acid glycoprotein.
7240157	4	62	theme	microheterogeneity	823:840	arg1	type					815:818	a new type	809:818	a new type of microheterogeneity	809:840	The combination of the improved resolving power and the enhanced sensitivity of the 500-MHz 1H-NMR spectrometer afforded the elucidation of a new type of microheterogeneity with regard to the position of attachment of Fuc.
7240157	6	63	contain	contains	949:956	arg1	form					944:947	The major form	934:947	The major form	934:947	The major form contains Fuc alpha-(1 leads to 3) linked to GlcNac 7 of the tetra-antennary structure, as shown earlier.
7240157	6	63	contain	contains	949:956	arg2	alpha-					962:967	Fuc alpha-	958:967	Fuc alpha-	958:967	The major form contains Fuc alpha-(1 leads to 3) linked to GlcNac 7 of the tetra-antennary structure, as shown earlier.
7240157	2	64	theme	monofucosylated	298:312	arg1	fraction					343:350	a monofucosylated tetra-antennary glycopeptide fraction	296:350	a monofucosylated tetra-antennary glycopeptide fraction which was derived from human plasma alpha 1-acid glycoprotein	296:412	Five hundred-MHz 1H-NMR spectroscopy was employed to study a monofucosylated tetra-antennary glycopeptide fraction which was derived from human plasma alpha 1-acid glycoprotein.
7240157	8	65	gly	glycopeptide	1314:1325	arg2	glycopeptide					1314:1325	a glycopeptide mixture	1312:1333	a glycopeptide mixture	1312:1333	It is thus noteworthy that this spectral technique allows elucidation of structures of very closely related carbohydrate chains in a glycopeptide mixture.
7240157	0	66	theme	1H-NMR	71:76	arg1	spectroscopy					78:89	500-MHz 1H-NMR spectroscopy	63:89	500-MHz 1H-NMR spectroscopy of glycopeptide preparations	63:118	Characterization of the microheterogeneity in glycoproteins by 500-MHz 1H-NMR spectroscopy of glycopeptide preparations.
7240157	0	67	from	microheterogeneity	24:41	arg1	glycoproteins					46:58	glycoproteins	46:58	glycoproteins	46:58	Characterization of the microheterogeneity in glycoproteins by 500-MHz 1H-NMR spectroscopy of glycopeptide preparations.
7240157	3	68	dep	J.	532:533	arg1	Biochemistry					640:651	Biochemistry	640:651	Biochemistry	640:651	This fraction was earlier judged to be homogeneous by 360-MHz 1H-NMR spectroscopic analysis (Fournet, B., Montreuil, J., Strecker, G., Dorland, L., Haverkamp, J., Vliegenthart, J. F. G., Binette, J. P., and Schmid, K. (1978) Biochemistry 17, 5206-5214).
7240157	6	69	theme	structure	1025:1033	arg1	GlcNac					993:998	GlcNac 7	993:1000	GlcNac 7 of the tetra-antennary structure	993:1033	The major form contains Fuc alpha-(1 leads to 3) linked to GlcNac 7 of the tetra-antennary structure, as shown earlier.
7240157	2	70	theme	tetra-antennary	314:328	arg1	fraction					343:350	a monofucosylated tetra-antennary glycopeptide fraction	296:350	a monofucosylated tetra-antennary glycopeptide fraction which was derived from human plasma alpha 1-acid glycoprotein	296:412	Five hundred-MHz 1H-NMR spectroscopy was employed to study a monofucosylated tetra-antennary glycopeptide fraction which was derived from human plasma alpha 1-acid glycoprotein.
4172099	7	0	contain	had	984:986	arg1	presence					927:934	the presence	923:934	the presence	923:934	Central heterogeneity was shown by the presence of three completely different core units, which had the following compositions: (1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2).
4172099	7	0	contain	had	984:986	arg2	compositions					1002:1013	the following compositions	988:1013	the following compositions	988:1013	Central heterogeneity was shown by the presence of three completely different core units, which had the following compositions: (1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2).
4172099	5	1	theme	sialic	646:651	arg1	acid					640:643	N-acetylneuraminic acid	621:643	N-acetylneuraminic acid (sialic acid)	621:657	2 residues of 6-deoxy-l-galactose (l-fucose), 14-15 of d-mannose, 12-13 of d-galactose, 12-13 of 2-acetamido-2-deoxy-d-glucose (N-acetyl-d-glucosamine), 6 of 2-acetamido-2-deoxy-d-galactose (N-acetyl-d-galactosamine) and 5 of N-acetylneuraminic acid (sialic acid), and these were distributed between six oligosaccharide units all of which were present on the heavy polypeptide chains.
4172099	5	1	theme	sialic	646:651	arg1	acid					653:656	sialic acid	646:656	sialic acid	646:656	2 residues of 6-deoxy-l-galactose (l-fucose), 14-15 of d-mannose, 12-13 of d-galactose, 12-13 of 2-acetamido-2-deoxy-d-glucose (N-acetyl-d-glucosamine), 6 of 2-acetamido-2-deoxy-d-galactose (N-acetyl-d-galactosamine) and 5 of N-acetylneuraminic acid (sialic acid), and these were distributed between six oligosaccharide units all of which were present on the heavy polypeptide chains.
4172099	5	2	theme	2-acetamido-2-deoxy-d-glucose	492:520	arg1	N-acetyl-d-glucosamine					523:544	N-acetyl-d-glucosamine	523:544	N-acetyl-d-glucosamine	523:544	2 residues of 6-deoxy-l-galactose (l-fucose), 14-15 of d-mannose, 12-13 of d-galactose, 12-13 of 2-acetamido-2-deoxy-d-glucose (N-acetyl-d-glucosamine), 6 of 2-acetamido-2-deoxy-d-galactose (N-acetyl-d-galactosamine) and 5 of N-acetylneuraminic acid (sialic acid), and these were distributed between six oligosaccharide units all of which were present on the heavy polypeptide chains.
4172099	5	2	theme	2-acetamido-2-deoxy-d-glucose	492:520	arg1	2-acetamido-2-deoxy-d-glucose					492:520	2-acetamido-2-deoxy-d-glucose	492:520	2-acetamido-2-deoxy-d-glucose (N-acetyl-d-glucosamine)	492:545	2 residues of 6-deoxy-l-galactose (l-fucose), 14-15 of d-mannose, 12-13 of d-galactose, 12-13 of 2-acetamido-2-deoxy-d-glucose (N-acetyl-d-glucosamine), 6 of 2-acetamido-2-deoxy-d-galactose (N-acetyl-d-galactosamine) and 5 of N-acetylneuraminic acid (sialic acid), and these were distributed between six oligosaccharide units all of which were present on the heavy polypeptide chains.
4172099	5	2	theme	2-acetamido-2-deoxy-d-glucose	492:520	arg1	12-13					483:487	12-13	483:487	12-13	483:487	2 residues of 6-deoxy-l-galactose (l-fucose), 14-15 of d-mannose, 12-13 of d-galactose, 12-13 of 2-acetamido-2-deoxy-d-glucose (N-acetyl-d-glucosamine), 6 of 2-acetamido-2-deoxy-d-galactose (N-acetyl-d-galactosamine) and 5 of N-acetylneuraminic acid (sialic acid), and these were distributed between six oligosaccharide units all of which were present on the heavy polypeptide chains.
4172099	11	3	theme	glycopeptides	1887:1899	arg1	mobility					1834:1841	electrophoretic mobility	1818:1841	electrophoretic mobility	1818:1841	Explanations are given for the electrophoretic mobility and staining characteristics of the various glycopeptides.
4172099	11	3	theme	glycopeptides	1887:1899	arg1	characteristics					1856:1870	staining characteristics	1847:1870	staining characteristics	1847:1870	Explanations are given for the electrophoretic mobility and staining characteristics of the various glycopeptides.
4172099	8	4	theme	oligosaccharide	1458:1472	arg1	units					1474:1478	The core oligosaccharide units	1449:1478	The core oligosaccharide units	1449:1478	The core oligosaccharide units showed peripheral heterogeneity in the attachment of 6-deoxy-l-galactose, 2-acetamido-2-deoxy-d-glucose and N-acetylneuraminic acid.
4172099	2	5	attach	isolated	210:217	arg2	protein					198:204	the protein	194:204	the protein	194:204	The carbohydrate content was found to be unchanged when the protein was isolated from the patient over a period of 18 months.
4172099	2	5	attach	isolated	210:217	arg1	patient					228:234	the patient	224:234	the patient	224:234	The carbohydrate content was found to be unchanged when the protein was isolated from the patient over a period of 18 months.
4172099	5	6	theme	heavy	754:758	arg1	chains					772:777	the heavy polypeptide chains	750:777	the heavy polypeptide chains	750:777	2 residues of 6-deoxy-l-galactose (l-fucose), 14-15 of d-mannose, 12-13 of d-galactose, 12-13 of 2-acetamido-2-deoxy-d-glucose (N-acetyl-d-glucosamine), 6 of 2-acetamido-2-deoxy-d-galactose (N-acetyl-d-galactosamine) and 5 of N-acetylneuraminic acid (sialic acid), and these were distributed between six oligosaccharide units all of which were present on the heavy polypeptide chains.
4172099	7	7	theme	3	1050:1050	arg1	3					1050:1050	3	1050:1050	3	1050:1050	Central heterogeneity was shown by the presence of three completely different core units, which had the following compositions: (1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2).
4172099	7	7	theme	3	1050:1050	arg1	d-galactose					1034:1044	d-galactose	1034:1044	d-galactose	1034:1044	Central heterogeneity was shown by the presence of three completely different core units, which had the following compositions: (1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2).
4172099	7	7	theme	3	1050:1050	arg1	residues					1022:1029	(1) 3 residues	1016:1029	(1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2)	1016:1446	Central heterogeneity was shown by the presence of three completely different core units, which had the following compositions: (1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2).
4172099	7	8	theme	different	956:964	arg1	units					971:975	three completely different core units	939:975	three completely different core units	939:975	Central heterogeneity was shown by the presence of three completely different core units, which had the following compositions: (1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2).
4172099	9	9	theme	various	1657:1663	arg1	types					1665:1669	these various types	1651:1669	these various types of oligosaccharide unit	1651:1693	Tentative structures are proposed for these various types of oligosaccharide unit.
4172099	7	10	dep	residues	1175:1182	arg1	2					1170:1170	2	1170:1170	2	1170:1170	Central heterogeneity was shown by the presence of three completely different core units, which had the following compositions: (1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2).
4172099	0	11	from	Investigations	0:13	arg1	units					38:42	the oligosaccharide units	18:42	the oligosaccharide units of an A myeloma globulin	18:67	Investigations on the oligosaccharide units of an A myeloma globulin.
4172099	8	12	from	heterogeneity	1498:1510	arg1	attachment					1519:1528	the attachment	1515:1528	the attachment of 6-deoxy-l-galactose, 2-acetamido-2-deoxy-d-glucose and N-acetylneuraminic acid	1515:1610	The core oligosaccharide units showed peripheral heterogeneity in the attachment of 6-deoxy-l-galactose, 2-acetamido-2-deoxy-d-glucose and N-acetylneuraminic acid.
4172099	4	13	theme	myeloma	360:366	arg1	globulin					368:375	The A myeloma globulin	354:375	The A myeloma globulin	354:375	The A myeloma globulin contained approx.
4172099	2	14	theme	months	256:261	arg1	period					243:248	a period	241:248	a period of 18 months	241:261	The carbohydrate content was found to be unchanged when the protein was isolated from the patient over a period of 18 months.
4172099	2	15	theme	carbohydrate	142:153	arg1	unchanged					179:187	unchanged	179:187	unchanged	179:187	The carbohydrate content was found to be unchanged when the protein was isolated from the patient over a period of 18 months.
4172099	2	15	theme	carbohydrate	142:153	arg1	content					155:161	The carbohydrate content	138:161	The carbohydrate content	138:161	The carbohydrate content was found to be unchanged when the protein was isolated from the patient over a period of 18 months.
4172099	3	16	contain	contained	307:315	arg1	forms					286:290	The various polymeric forms	264:290	The various polymeric forms of the protein	264:305	The various polymeric forms of the protein contained similar proportions of carbohydrate.
4172099	3	16	contain	contained	307:315	arg2	proportions					325:335	similar proportions	317:335	similar proportions of carbohydrate	317:351	The various polymeric forms of the protein contained similar proportions of carbohydrate.
4172099	7	17	theme	2-acetamido-2-deoxy-d-glucose	1380:1408	arg1	d-mannose					1361:1369	d-mannose	1361:1369	d-mannose	1361:1369	Central heterogeneity was shown by the presence of three completely different core units, which had the following compositions: (1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2).
4172099	7	18	theme	similar	1425:1431	arg1	linkage					1417:1423	a linkage	1415:1423	a linkage similar to that in (2)	1415:1446	Central heterogeneity was shown by the presence of three completely different core units, which had the following compositions: (1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2).
4172099	7	19	theme	2-acetamido-2-deoxy-d-glucose	1224:1252	arg1	d-mannose					1187:1195	d-mannose	1187:1195	d-mannose	1187:1195	Central heterogeneity was shown by the presence of three completely different core units, which had the following compositions: (1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2).
4172099	7	19	theme	2-acetamido-2-deoxy-d-glucose	1224:1252	arg1	2-acetamido-2-deoxy-d-glucose					1224:1252	2-acetamido-2-deoxy-d-glucose	1224:1252	2-acetamido-2-deoxy-d-glucose	1224:1252	Central heterogeneity was shown by the presence of three completely different core units, which had the following compositions: (1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2).
4172099	7	19	theme	2-acetamido-2-deoxy-d-glucose	1224:1252	arg1	residues					1175:1182	(2) 3 residues	1169:1182	(2) 3 residues of d-mannose	1169:1195	Central heterogeneity was shown by the presence of three completely different core units, which had the following compositions: (1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2).
4172099	7	19	theme	2-acetamido-2-deoxy-d-glucose	1224:1252	arg1	3					1219:1219	3	1219:1219	3	1219:1219	Central heterogeneity was shown by the presence of three completely different core units, which had the following compositions: (1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2).
4172099	7	20	theme	2-acetamido-2-deoxy-d-galactose	1055:1085	arg1	d-galactose					1034:1044	d-galactose	1034:1044	d-galactose	1034:1044	Central heterogeneity was shown by the presence of three completely different core units, which had the following compositions: (1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2).
4172099	6	21	theme	oligosaccharide	784:798	arg1	units					800:804	The oligosaccharide units	780:804	The oligosaccharide units	780:804	The oligosaccharide units showed two kinds of heterogeneity, which have been termed central and peripheral.
4172099	3	22	theme	similar	317:323	arg1	proportions					325:335	similar proportions	317:335	similar proportions of carbohydrate	317:351	The various polymeric forms of the protein contained similar proportions of carbohydrate.
4172099	5	23	theme	N-acetylneuraminic	621:638	arg1	acid					640:643	N-acetylneuraminic acid	621:643	N-acetylneuraminic acid (sialic acid)	621:657	2 residues of 6-deoxy-l-galactose (l-fucose), 14-15 of d-mannose, 12-13 of d-galactose, 12-13 of 2-acetamido-2-deoxy-d-glucose (N-acetyl-d-glucosamine), 6 of 2-acetamido-2-deoxy-d-galactose (N-acetyl-d-galactosamine) and 5 of N-acetylneuraminic acid (sialic acid), and these were distributed between six oligosaccharide units all of which were present on the heavy polypeptide chains.
4172099	5	23	theme	N-acetylneuraminic	621:638	arg1	acid					653:656	sialic acid	646:656	sialic acid	646:656	2 residues of 6-deoxy-l-galactose (l-fucose), 14-15 of d-mannose, 12-13 of d-galactose, 12-13 of 2-acetamido-2-deoxy-d-glucose (N-acetyl-d-glucosamine), 6 of 2-acetamido-2-deoxy-d-galactose (N-acetyl-d-galactosamine) and 5 of N-acetylneuraminic acid (sialic acid), and these were distributed between six oligosaccharide units all of which were present on the heavy polypeptide chains.
4172099	7	24	theme	3	1375:1375	arg1	3					1375:1375	3	1375:1375	3	1375:1375	Central heterogeneity was shown by the presence of three completely different core units, which had the following compositions: (1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2).
4172099	7	24	theme	3	1375:1375	arg1	d-mannose					1361:1369	d-mannose	1361:1369	d-mannose	1361:1369	Central heterogeneity was shown by the presence of three completely different core units, which had the following compositions: (1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2).
4172099	7	24	theme	3	1375:1375	arg1	residues					1349:1356	4 residues	1347:1356	(1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2)	1016:1446	Central heterogeneity was shown by the presence of three completely different core units, which had the following compositions: (1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2).
4172099	8	25	theme	peripheral	1487:1496	arg1	heterogeneity					1498:1510	peripheral heterogeneity	1487:1510	peripheral heterogeneity in the attachment of 6-deoxy-l-galactose, 2-acetamido-2-deoxy-d-glucose and N-acetylneuraminic acid	1487:1610	The core oligosaccharide units showed peripheral heterogeneity in the attachment of 6-deoxy-l-galactose, 2-acetamido-2-deoxy-d-glucose and N-acetylneuraminic acid.
4172099	5	26	theme	acid	640:643	arg1	acid					640:643	N-acetylneuraminic acid	621:643	N-acetylneuraminic acid (sialic acid)	621:657	2 residues of 6-deoxy-l-galactose (l-fucose), 14-15 of d-mannose, 12-13 of d-galactose, 12-13 of 2-acetamido-2-deoxy-d-glucose (N-acetyl-d-glucosamine), 6 of 2-acetamido-2-deoxy-d-galactose (N-acetyl-d-galactosamine) and 5 of N-acetylneuraminic acid (sialic acid), and these were distributed between six oligosaccharide units all of which were present on the heavy polypeptide chains.
4172099	5	26	theme	acid	640:643	arg1	acid					653:656	sialic acid	646:656	sialic acid	646:656	2 residues of 6-deoxy-l-galactose (l-fucose), 14-15 of d-mannose, 12-13 of d-galactose, 12-13 of 2-acetamido-2-deoxy-d-glucose (N-acetyl-d-glucosamine), 6 of 2-acetamido-2-deoxy-d-galactose (N-acetyl-d-galactosamine) and 5 of N-acetylneuraminic acid (sialic acid), and these were distributed between six oligosaccharide units all of which were present on the heavy polypeptide chains.
4172099	5	26	theme	acid	640:643	arg1	d-mannose					450:458	d-mannose	450:458	d-mannose	450:458	2 residues of 6-deoxy-l-galactose (l-fucose), 14-15 of d-mannose, 12-13 of d-galactose, 12-13 of 2-acetamido-2-deoxy-d-glucose (N-acetyl-d-glucosamine), 6 of 2-acetamido-2-deoxy-d-galactose (N-acetyl-d-galactosamine) and 5 of N-acetylneuraminic acid (sialic acid), and these were distributed between six oligosaccharide units all of which were present on the heavy polypeptide chains.
4172099	5	26	theme	acid	640:643	arg1	14-15					441:445	14-15	441:445	14-15	441:445	2 residues of 6-deoxy-l-galactose (l-fucose), 14-15 of d-mannose, 12-13 of d-galactose, 12-13 of 2-acetamido-2-deoxy-d-glucose (N-acetyl-d-glucosamine), 6 of 2-acetamido-2-deoxy-d-galactose (N-acetyl-d-galactosamine) and 5 of N-acetylneuraminic acid (sialic acid), and these were distributed between six oligosaccharide units all of which were present on the heavy polypeptide chains.
4172099	7	27	theme	d-mannose	1187:1195	arg1	2					1198:1198	2	1198:1198	2	1198:1198	Central heterogeneity was shown by the presence of three completely different core units, which had the following compositions: (1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2).
4172099	7	27	theme	d-mannose	1187:1195	arg1	d-galactose					1203:1213	d-galactose	1203:1213	d-galactose	1203:1213	Central heterogeneity was shown by the presence of three completely different core units, which had the following compositions: (1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2).
4172099	7	27	theme	d-mannose	1187:1195	arg1	residues					1175:1182	(2) 3 residues	1169:1182	(2) 3 residues of d-mannose	1169:1195	Central heterogeneity was shown by the presence of three completely different core units, which had the following compositions: (1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2).
4172099	7	27	theme	d-mannose	1187:1195	arg1	d-mannose					1187:1195	d-mannose	1187:1195	d-mannose	1187:1195	Central heterogeneity was shown by the presence of three completely different core units, which had the following compositions: (1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2).
4172099	7	27	theme	d-mannose	1187:1195	arg1	3					1219:1219	3	1219:1219	3	1219:1219	Central heterogeneity was shown by the presence of three completely different core units, which had the following compositions: (1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2).
4172099	7	27	theme	d-mannose	1187:1195	arg1	2-acetamido-2-deoxy-d-glucose					1224:1252	2-acetamido-2-deoxy-d-glucose	1224:1252	2-acetamido-2-deoxy-d-glucose	1224:1252	Central heterogeneity was shown by the presence of three completely different core units, which had the following compositions: (1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2).
4172099	1	28	theme	carbohydrate	74:85	arg1	content					87:93	The carbohydrate content	70:93	The carbohydrate content of an A myeloma globulin	70:118	The carbohydrate content of an A myeloma globulin was investigated.
4172099	5	29	theme	d-galactose	470:480	arg1	12-13					461:465	12-13	461:465	12-13	461:465	2 residues of 6-deoxy-l-galactose (l-fucose), 14-15 of d-mannose, 12-13 of d-galactose, 12-13 of 2-acetamido-2-deoxy-d-glucose (N-acetyl-d-glucosamine), 6 of 2-acetamido-2-deoxy-d-galactose (N-acetyl-d-galactosamine) and 5 of N-acetylneuraminic acid (sialic acid), and these were distributed between six oligosaccharide units all of which were present on the heavy polypeptide chains.
4172099	5	29	theme	d-galactose	470:480	arg1	d-galactose					470:480	d-galactose	470:480	d-galactose	470:480	2 residues of 6-deoxy-l-galactose (l-fucose), 14-15 of d-mannose, 12-13 of d-galactose, 12-13 of 2-acetamido-2-deoxy-d-glucose (N-acetyl-d-glucosamine), 6 of 2-acetamido-2-deoxy-d-galactose (N-acetyl-d-galactosamine) and 5 of N-acetylneuraminic acid (sialic acid), and these were distributed between six oligosaccharide units all of which were present on the heavy polypeptide chains.
4172099	9	30	theme	unit	1690:1693	arg1	types					1665:1669	these various types	1651:1669	these various types of oligosaccharide unit	1651:1693	Tentative structures are proposed for these various types of oligosaccharide unit.
4172099	4	31	theme	A	358:358	arg1	globulin					368:375	The A myeloma globulin	354:375	The A myeloma globulin	354:375	The A myeloma globulin contained approx.
4172099	7	32	theme	d-mannose	1361:1369	arg1	3					1375:1375	3	1375:1375	3	1375:1375	Central heterogeneity was shown by the presence of three completely different core units, which had the following compositions: (1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2).
4172099	7	32	theme	d-mannose	1361:1369	arg1	d-mannose					1361:1369	d-mannose	1361:1369	d-mannose	1361:1369	Central heterogeneity was shown by the presence of three completely different core units, which had the following compositions: (1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2).
4172099	7	32	theme	d-mannose	1361:1369	arg1	residues					1349:1356	4 residues	1347:1356	(1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2)	1016:1446	Central heterogeneity was shown by the presence of three completely different core units, which had the following compositions: (1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2).
4172099	7	33	theme	N-glycosidic	1279:1290	arg1	linkage					1292:1298	an N-glycosidic linkage	1276:1298	an N-glycosidic linkage between acetamidohexose and aspartic acid	1276:1340	Central heterogeneity was shown by the presence of three completely different core units, which had the following compositions: (1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2).
4172099	3	34	theme	carbohydrate	340:351	arg1	proportions					325:335	similar proportions	317:335	similar proportions of carbohydrate	317:351	The various polymeric forms of the protein contained similar proportions of carbohydrate.
4172099	5	35	theme	2-acetamido-2-deoxy-d-galactose	553:583	arg1	2-acetamido-2-deoxy-d-galactose					553:583	2-acetamido-2-deoxy-d-galactose	553:583	2-acetamido-2-deoxy-d-galactose (N-acetyl-d-galactosamine)	553:610	2 residues of 6-deoxy-l-galactose (l-fucose), 14-15 of d-mannose, 12-13 of d-galactose, 12-13 of 2-acetamido-2-deoxy-d-glucose (N-acetyl-d-glucosamine), 6 of 2-acetamido-2-deoxy-d-galactose (N-acetyl-d-galactosamine) and 5 of N-acetylneuraminic acid (sialic acid), and these were distributed between six oligosaccharide units all of which were present on the heavy polypeptide chains.
4172099	5	35	theme	2-acetamido-2-deoxy-d-galactose	553:583	arg1	6					548:548	6	548:548	6	548:548	2 residues of 6-deoxy-l-galactose (l-fucose), 14-15 of d-mannose, 12-13 of d-galactose, 12-13 of 2-acetamido-2-deoxy-d-glucose (N-acetyl-d-glucosamine), 6 of 2-acetamido-2-deoxy-d-galactose (N-acetyl-d-galactosamine) and 5 of N-acetylneuraminic acid (sialic acid), and these were distributed between six oligosaccharide units all of which were present on the heavy polypeptide chains.
4172099	5	35	theme	2-acetamido-2-deoxy-d-galactose	553:583	arg1	N-acetyl-d-galactosamine					586:609	N-acetyl-d-galactosamine	586:609	N-acetyl-d-galactosamine	586:609	2 residues of 6-deoxy-l-galactose (l-fucose), 14-15 of d-mannose, 12-13 of d-galactose, 12-13 of 2-acetamido-2-deoxy-d-glucose (N-acetyl-d-glucosamine), 6 of 2-acetamido-2-deoxy-d-galactose (N-acetyl-d-galactosamine) and 5 of N-acetylneuraminic acid (sialic acid), and these were distributed between six oligosaccharide units all of which were present on the heavy polypeptide chains.
4172099	7	36	theme	d-galactose	1034:1044	arg1	3					1050:1050	3	1050:1050	3	1050:1050	Central heterogeneity was shown by the presence of three completely different core units, which had the following compositions: (1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2).
4172099	7	36	theme	d-galactose	1034:1044	arg1	d-galactose					1034:1044	d-galactose	1034:1044	d-galactose	1034:1044	Central heterogeneity was shown by the presence of three completely different core units, which had the following compositions: (1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2).
4172099	7	36	theme	d-galactose	1034:1044	arg1	residues					1022:1029	(1) 3 residues	1016:1029	(1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2)	1016:1446	Central heterogeneity was shown by the presence of three completely different core units, which had the following compositions: (1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2).
4172099	9	37	theme	oligosaccharide	1674:1688	arg1	unit					1690:1693	oligosaccharide unit	1674:1693	oligosaccharide unit	1674:1693	Tentative structures are proposed for these various types of oligosaccharide unit.
4172099	7	38	with	2-acetamido-2-deoxy-d-glucose	1380:1408	arg1	linkage					1417:1423	a linkage	1415:1423	a linkage similar to that in (2)	1415:1446	Central heterogeneity was shown by the presence of three completely different core units, which had the following compositions: (1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2).
4172099	8	39	theme	core	1453:1456	arg1	units					1474:1478	The core oligosaccharide units	1449:1478	The core oligosaccharide units	1449:1478	The core oligosaccharide units showed peripheral heterogeneity in the attachment of 6-deoxy-l-galactose, 2-acetamido-2-deoxy-d-glucose and N-acetylneuraminic acid.
4172099	10	40	theme	acid	1744:1747	arg1	content					1749:1755	the sialic acid content	1733:1755	the sialic acid content	1733:1755	Glycopeptides were isolated in which the sialic acid content exceeded that of d-galactose.
4172099	10	41	theme	sialic	1737:1742	arg1	content					1749:1755	the sialic acid content	1733:1755	the sialic acid content	1733:1755	Glycopeptides were isolated in which the sialic acid content exceeded that of d-galactose.
4172099	5	42	theme	polypeptide	760:770	arg1	chains					772:777	the heavy polypeptide chains	750:777	the heavy polypeptide chains	750:777	2 residues of 6-deoxy-l-galactose (l-fucose), 14-15 of d-mannose, 12-13 of d-galactose, 12-13 of 2-acetamido-2-deoxy-d-glucose (N-acetyl-d-glucosamine), 6 of 2-acetamido-2-deoxy-d-galactose (N-acetyl-d-galactosamine) and 5 of N-acetylneuraminic acid (sialic acid), and these were distributed between six oligosaccharide units all of which were present on the heavy polypeptide chains.
4172099	11	43	theme	various	1879:1885	arg1	glycopeptides					1887:1899	the various glycopeptides	1875:1899	the various glycopeptides	1875:1899	Explanations are given for the electrophoretic mobility and staining characteristics of the various glycopeptides.
4172099	5	44	theme	oligosaccharide	699:713	arg1	units					715:719	six oligosaccharide units	695:719	six oligosaccharide units all of which were present on the heavy polypeptide chains	695:777	2 residues of 6-deoxy-l-galactose (l-fucose), 14-15 of d-mannose, 12-13 of d-galactose, 12-13 of 2-acetamido-2-deoxy-d-glucose (N-acetyl-d-glucosamine), 6 of 2-acetamido-2-deoxy-d-galactose (N-acetyl-d-galactosamine) and 5 of N-acetylneuraminic acid (sialic acid), and these were distributed between six oligosaccharide units all of which were present on the heavy polypeptide chains.
4172099	11	45	gly	glycopeptides	1887:1899	arg2	glycopeptides					1887:1899	the various glycopeptides	1875:1899	the various glycopeptides	1875:1899	Explanations are given for the electrophoretic mobility and staining characteristics of the various glycopeptides.
4172099	5	46	theme	d-mannose	450:458	arg1	acid					640:643	N-acetylneuraminic acid	621:643	N-acetylneuraminic acid (sialic acid)	621:657	2 residues of 6-deoxy-l-galactose (l-fucose), 14-15 of d-mannose, 12-13 of d-galactose, 12-13 of 2-acetamido-2-deoxy-d-glucose (N-acetyl-d-glucosamine), 6 of 2-acetamido-2-deoxy-d-galactose (N-acetyl-d-galactosamine) and 5 of N-acetylneuraminic acid (sialic acid), and these were distributed between six oligosaccharide units all of which were present on the heavy polypeptide chains.
4172099	5	46	theme	d-mannose	450:458	arg1	acid					653:656	sialic acid	646:656	sialic acid	646:656	2 residues of 6-deoxy-l-galactose (l-fucose), 14-15 of d-mannose, 12-13 of d-galactose, 12-13 of 2-acetamido-2-deoxy-d-glucose (N-acetyl-d-glucosamine), 6 of 2-acetamido-2-deoxy-d-galactose (N-acetyl-d-galactosamine) and 5 of N-acetylneuraminic acid (sialic acid), and these were distributed between six oligosaccharide units all of which were present on the heavy polypeptide chains.
4172099	5	46	theme	d-mannose	450:458	arg1	d-mannose					450:458	d-mannose	450:458	d-mannose	450:458	2 residues of 6-deoxy-l-galactose (l-fucose), 14-15 of d-mannose, 12-13 of d-galactose, 12-13 of 2-acetamido-2-deoxy-d-glucose (N-acetyl-d-glucosamine), 6 of 2-acetamido-2-deoxy-d-galactose (N-acetyl-d-galactosamine) and 5 of N-acetylneuraminic acid (sialic acid), and these were distributed between six oligosaccharide units all of which were present on the heavy polypeptide chains.
4172099	5	46	theme	d-mannose	450:458	arg1	14-15					441:445	14-15	441:445	14-15	441:445	2 residues of 6-deoxy-l-galactose (l-fucose), 14-15 of d-mannose, 12-13 of d-galactose, 12-13 of 2-acetamido-2-deoxy-d-glucose (N-acetyl-d-glucosamine), 6 of 2-acetamido-2-deoxy-d-galactose (N-acetyl-d-galactosamine) and 5 of N-acetylneuraminic acid (sialic acid), and these were distributed between six oligosaccharide units all of which were present on the heavy polypeptide chains.
4172099	0	47	theme	oligosaccharide	22:36	arg1	units					38:42	the oligosaccharide units	18:42	the oligosaccharide units of an A myeloma globulin	18:67	Investigations on the oligosaccharide units of an A myeloma globulin.
4172099	0	48	theme	A	50:50	arg1	globulin					60:67	an A myeloma globulin	47:67	an A myeloma globulin	47:67	Investigations on the oligosaccharide units of an A myeloma globulin.
4172099	11	49	theme	staining	1847:1854	arg1	characteristics					1856:1870	staining characteristics	1847:1870	staining characteristics	1847:1870	Explanations are given for the electrophoretic mobility and staining characteristics of the various glycopeptides.
4172099	3	50	theme	various	268:274	arg1	forms					286:290	The various polymeric forms	264:290	The various polymeric forms of the protein	264:305	The various polymeric forms of the protein contained similar proportions of carbohydrate.
4172099	3	51	theme	protein	299:305	arg1	forms					286:290	The various polymeric forms	264:290	The various polymeric forms of the protein	264:305	The various polymeric forms of the protein contained similar proportions of carbohydrate.
4172099	5	52	located	present	739:745	arg2	units					715:719	six oligosaccharide units	695:719	six oligosaccharide units all of which were present on the heavy polypeptide chains	695:777	2 residues of 6-deoxy-l-galactose (l-fucose), 14-15 of d-mannose, 12-13 of d-galactose, 12-13 of 2-acetamido-2-deoxy-d-glucose (N-acetyl-d-glucosamine), 6 of 2-acetamido-2-deoxy-d-galactose (N-acetyl-d-galactosamine) and 5 of N-acetylneuraminic acid (sialic acid), and these were distributed between six oligosaccharide units all of which were present on the heavy polypeptide chains.
4172099	5	52	located	present	739:745	arg2	all					721:723	all	721:723	all	721:723	2 residues of 6-deoxy-l-galactose (l-fucose), 14-15 of d-mannose, 12-13 of d-galactose, 12-13 of 2-acetamido-2-deoxy-d-glucose (N-acetyl-d-glucosamine), 6 of 2-acetamido-2-deoxy-d-galactose (N-acetyl-d-galactosamine) and 5 of N-acetylneuraminic acid (sialic acid), and these were distributed between six oligosaccharide units all of which were present on the heavy polypeptide chains.
4172099	5	52	located	present	739:745	arg1	chains					772:777	the heavy polypeptide chains	750:777	the heavy polypeptide chains	750:777	2 residues of 6-deoxy-l-galactose (l-fucose), 14-15 of d-mannose, 12-13 of d-galactose, 12-13 of 2-acetamido-2-deoxy-d-glucose (N-acetyl-d-glucosamine), 6 of 2-acetamido-2-deoxy-d-galactose (N-acetyl-d-galactosamine) and 5 of N-acetylneuraminic acid (sialic acid), and these were distributed between six oligosaccharide units all of which were present on the heavy polypeptide chains.
4172099	1	53	theme	A	101:101	arg1	globulin					111:118	an A myeloma globulin	98:118	an A myeloma globulin	98:118	The carbohydrate content of an A myeloma globulin was investigated.
4172099	7	54	theme	O-glycosidic	1112:1123	arg1	linkage					1125:1131	an O-glycosidic linkage	1109:1131	an O-glycosidic linkage between acetamidohexose and serine	1109:1166	Central heterogeneity was shown by the presence of three completely different core units, which had the following compositions: (1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2).
4172099	11	55	theme	electrophoretic	1818:1832	arg1	mobility					1834:1841	electrophoretic mobility	1818:1841	electrophoretic mobility	1818:1841	Explanations are given for the electrophoretic mobility and staining characteristics of the various glycopeptides.
4172099	3	56	theme	polymeric	276:284	arg1	forms					286:290	The various polymeric forms	264:290	The various polymeric forms of the protein	264:305	The various polymeric forms of the protein contained similar proportions of carbohydrate.
4172099	11	57	dep	mobility	1834:1841	arg1	the					1814:1816	the	1814:1816	the	1814:1816	Explanations are given for the electrophoretic mobility and staining characteristics of the various glycopeptides.
4172099	1	58	theme	myeloma	103:109	arg1	globulin					111:118	an A myeloma globulin	98:118	an A myeloma globulin	98:118	The carbohydrate content of an A myeloma globulin was investigated.
4172099	5	59	theme	6-deoxy-l-galactose	409:427	arg1	residues					397:404	2 residues	395:404	2 residues of 6-deoxy-l-galactose (l-fucose)	395:438	2 residues of 6-deoxy-l-galactose (l-fucose), 14-15 of d-mannose, 12-13 of d-galactose, 12-13 of 2-acetamido-2-deoxy-d-glucose (N-acetyl-d-glucosamine), 6 of 2-acetamido-2-deoxy-d-galactose (N-acetyl-d-galactosamine) and 5 of N-acetylneuraminic acid (sialic acid), and these were distributed between six oligosaccharide units all of which were present on the heavy polypeptide chains.
4172099	5	59	theme	6-deoxy-l-galactose	409:427	arg1	6-deoxy-l-galactose					409:427	6-deoxy-l-galactose	409:427	6-deoxy-l-galactose (l-fucose)	409:438	2 residues of 6-deoxy-l-galactose (l-fucose), 14-15 of d-mannose, 12-13 of d-galactose, 12-13 of 2-acetamido-2-deoxy-d-glucose (N-acetyl-d-glucosamine), 6 of 2-acetamido-2-deoxy-d-galactose (N-acetyl-d-galactosamine) and 5 of N-acetylneuraminic acid (sialic acid), and these were distributed between six oligosaccharide units all of which were present on the heavy polypeptide chains.
4172099	8	60	theme	6-deoxy-l-galactose	1533:1551	arg1	attachment					1519:1528	the attachment	1515:1528	the attachment of 6-deoxy-l-galactose, 2-acetamido-2-deoxy-d-glucose and N-acetylneuraminic acid	1515:1610	The core oligosaccharide units showed peripheral heterogeneity in the attachment of 6-deoxy-l-galactose, 2-acetamido-2-deoxy-d-glucose and N-acetylneuraminic acid.
4172099	6	61	theme	heterogeneity	826:838	arg1	kinds					817:821	two kinds	813:821	two kinds	813:821	The oligosaccharide units showed two kinds of heterogeneity, which have been termed central and peripheral.
4172099	7	62	theme	aspartic	1328:1335	arg1	acid					1337:1340	aspartic acid	1328:1340	aspartic acid	1328:1340	Central heterogeneity was shown by the presence of three completely different core units, which had the following compositions: (1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2).
4172099	7	63	theme	core	966:969	arg1	units					971:975	three completely different core units	939:975	three completely different core units	939:975	Central heterogeneity was shown by the presence of three completely different core units, which had the following compositions: (1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2).
4172099	1	64	theme	globulin	111:118	arg1	content					87:93	The carbohydrate content	70:93	The carbohydrate content of an A myeloma globulin	70:118	The carbohydrate content of an A myeloma globulin was investigated.
4172099	7	65	theme	following	992:1000	arg1	compositions					1002:1013	the following compositions	988:1013	the following compositions	988:1013	Central heterogeneity was shown by the presence of three completely different core units, which had the following compositions: (1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2).
4172099	9	66	theme	Tentative	1613:1621	arg1	structures					1623:1632	Tentative structures	1613:1632	Tentative structures	1613:1632	Tentative structures are proposed for these various types of oligosaccharide unit.
4172099	7	67	theme	Central	888:894	arg1	heterogeneity					896:908	Central heterogeneity	888:908	Central heterogeneity	888:908	Central heterogeneity was shown by the presence of three completely different core units, which had the following compositions: (1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2).
4172099	8	68	theme	2-acetamido-2-deoxy-d-glucose	1554:1582	arg1	attachment					1519:1528	the attachment	1515:1528	the attachment of 6-deoxy-l-galactose, 2-acetamido-2-deoxy-d-glucose and N-acetylneuraminic acid	1515:1610	The core oligosaccharide units showed peripheral heterogeneity in the attachment of 6-deoxy-l-galactose, 2-acetamido-2-deoxy-d-glucose and N-acetylneuraminic acid.
4172099	0	69	theme	globulin	60:67	arg1	units					38:42	the oligosaccharide units	18:42	the oligosaccharide units of an A myeloma globulin	18:67	Investigations on the oligosaccharide units of an A myeloma globulin.
4172099	7	70	dep	residues	1022:1029	arg1	2					1198:1198	2	1198:1198	2	1198:1198	Central heterogeneity was shown by the presence of three completely different core units, which had the following compositions: (1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2).
4172099	7	70	dep	residues	1022:1029	arg1	d-mannose					1361:1369	d-mannose	1361:1369	d-mannose	1361:1369	Central heterogeneity was shown by the presence of three completely different core units, which had the following compositions: (1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2).
4172099	7	70	dep	residues	1022:1029	arg1	1					1017:1017	1	1017:1017	1	1017:1017	Central heterogeneity was shown by the presence of three completely different core units, which had the following compositions: (1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2).
4172099	7	70	dep	residues	1022:1029	arg1	d-galactose					1203:1213	d-galactose	1203:1213	d-galactose	1203:1213	Central heterogeneity was shown by the presence of three completely different core units, which had the following compositions: (1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2).
4172099	7	70	dep	residues	1022:1029	arg1	residues					1175:1182	(2) 3 residues	1169:1182	(2) 3 residues of d-mannose	1169:1195	Central heterogeneity was shown by the presence of three completely different core units, which had the following compositions: (1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2).
4172099	7	70	dep	residues	1022:1029	arg1	3					1375:1375	3	1375:1375	3	1375:1375	Central heterogeneity was shown by the presence of three completely different core units, which had the following compositions: (1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2).
4172099	7	70	dep	residues	1022:1029	arg1	d-mannose					1187:1195	d-mannose	1187:1195	d-mannose	1187:1195	Central heterogeneity was shown by the presence of three completely different core units, which had the following compositions: (1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2).
4172099	7	70	dep	residues	1022:1029	arg1	3					1219:1219	3	1219:1219	3	1219:1219	Central heterogeneity was shown by the presence of three completely different core units, which had the following compositions: (1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2).
4172099	7	70	dep	residues	1022:1029	arg1	2-acetamido-2-deoxy-d-glucose					1224:1252	2-acetamido-2-deoxy-d-glucose	1224:1252	2-acetamido-2-deoxy-d-glucose	1224:1252	Central heterogeneity was shown by the presence of three completely different core units, which had the following compositions: (1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2).
4172099	7	70	dep	residues	1022:1029	arg1	residues					1349:1356	4 residues	1347:1356	(1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2)	1016:1446	Central heterogeneity was shown by the presence of three completely different core units, which had the following compositions: (1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2).
4172099	7	71	theme	d-galactose	1203:1213	arg1	d-galactose					1203:1213	d-galactose	1203:1213	d-galactose	1203:1213	Central heterogeneity was shown by the presence of three completely different core units, which had the following compositions: (1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2).
4172099	7	71	theme	d-galactose	1203:1213	arg1	2					1198:1198	2	1198:1198	2	1198:1198	Central heterogeneity was shown by the presence of three completely different core units, which had the following compositions: (1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2).
4172099	7	71	theme	d-galactose	1203:1213	arg1	d-mannose					1187:1195	d-mannose	1187:1195	d-mannose	1187:1195	Central heterogeneity was shown by the presence of three completely different core units, which had the following compositions: (1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2).
4172099	7	71	theme	d-galactose	1203:1213	arg1	residues					1175:1182	(2) 3 residues	1169:1182	(2) 3 residues of d-mannose	1169:1195	Central heterogeneity was shown by the presence of three completely different core units, which had the following compositions: (1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2).
4172099	8	72	theme	acid	1607:1610	arg1	attachment					1519:1528	the attachment	1515:1528	the attachment of 6-deoxy-l-galactose, 2-acetamido-2-deoxy-d-glucose and N-acetylneuraminic acid	1515:1610	The core oligosaccharide units showed peripheral heterogeneity in the attachment of 6-deoxy-l-galactose, 2-acetamido-2-deoxy-d-glucose and N-acetylneuraminic acid.
4172099	0	73	theme	myeloma	52:58	arg1	globulin					60:67	an A myeloma globulin	47:67	an A myeloma globulin	47:67	Investigations on the oligosaccharide units of an A myeloma globulin.
4172099	5	74	attach	present	739:745	arg2	units					715:719	six oligosaccharide units	695:719	six oligosaccharide units all of which were present on the heavy polypeptide chains	695:777	2 residues of 6-deoxy-l-galactose (l-fucose), 14-15 of d-mannose, 12-13 of d-galactose, 12-13 of 2-acetamido-2-deoxy-d-glucose (N-acetyl-d-glucosamine), 6 of 2-acetamido-2-deoxy-d-galactose (N-acetyl-d-galactosamine) and 5 of N-acetylneuraminic acid (sialic acid), and these were distributed between six oligosaccharide units all of which were present on the heavy polypeptide chains.
4172099	5	74	attach	present	739:745	arg2	all					721:723	all	721:723	all	721:723	2 residues of 6-deoxy-l-galactose (l-fucose), 14-15 of d-mannose, 12-13 of d-galactose, 12-13 of 2-acetamido-2-deoxy-d-glucose (N-acetyl-d-glucosamine), 6 of 2-acetamido-2-deoxy-d-galactose (N-acetyl-d-galactosamine) and 5 of N-acetylneuraminic acid (sialic acid), and these were distributed between six oligosaccharide units all of which were present on the heavy polypeptide chains.
4172099	5	74	attach	present	739:745	arg1	chains					772:777	the heavy polypeptide chains	750:777	the heavy polypeptide chains	750:777	2 residues of 6-deoxy-l-galactose (l-fucose), 14-15 of d-mannose, 12-13 of d-galactose, 12-13 of 2-acetamido-2-deoxy-d-glucose (N-acetyl-d-glucosamine), 6 of 2-acetamido-2-deoxy-d-galactose (N-acetyl-d-galactosamine) and 5 of N-acetylneuraminic acid (sialic acid), and these were distributed between six oligosaccharide units all of which were present on the heavy polypeptide chains.
4172099	7	75	theme	units	971:975	arg1	presence					927:934	the presence	923:934	the presence	923:934	Central heterogeneity was shown by the presence of three completely different core units, which had the following compositions: (1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2).
4172099	7	76	dep	residues	1349:1356	arg1	3					1344:1344	3	1344:1344	3	1344:1344	Central heterogeneity was shown by the presence of three completely different core units, which had the following compositions: (1) 3 residues of d-galactose and 3 of 2-acetamido-2-deoxy-d-galactose, joined to protein by an O-glycosidic linkage between acetamidohexose and serine; (2) 3 residues of d-mannose, 2 of d-galactose and 3 of 2-acetamido-2-deoxy-d-glucose, joined to protein by an N-glycosidic linkage between acetamidohexose and aspartic acid; (3) 4 residues of d-mannose and 3 of 2-acetamido-2-deoxy-d-glucose with a linkage similar to that in (2).
4172099	8	77	theme	N-acetylneuraminic	1588:1605	arg1	acid					1607:1610	N-acetylneuraminic acid	1588:1610	N-acetylneuraminic acid	1588:1610	The core oligosaccharide units showed peripheral heterogeneity in the attachment of 6-deoxy-l-galactose, 2-acetamido-2-deoxy-d-glucose and N-acetylneuraminic acid.
4091823	2	0	theme	group	518:522	arg1	cells					532:536	the three blood group Cad red cells	502:536	the three blood group Cad red cells under study (samples Cad., Bui	502:567	Structure determination of the major acid components by methylation analysis, g.l.c.-m.s. and 1H-n.m.r. indicated that the three blood group Cad red cells under study (samples Cad., Bui.
4091823	1	1	theme	a+	182:183	arg1	membranes					149:157	the erythrocyte membranes	133:157	the erythrocyte membranes of blood group Cad, Sd(a+) and Sd(a-) donors	133:202	Glycophorin A was purified from the erythrocyte membranes of blood group Cad, Sd(a+) and Sd(a-) donors and the oligosaccharide alditols, obtained after alkaline borohydride degradation, separated by h.p.l.c. on an alkylamine silica gel column, were characterized by sugar analysis.
4091823	7	2	from	samples	1096:1102	arg1	present					1081:1087	present	1081:1087	present	1081:1087	carries about 12 O-glycosidically linked pentasaccharide chains per molecule whereas only 2-3 of these chains were present in the samples from the two other unrelated Cad individuals (Bui.
4091823	6	3	theme	glycophorin	917:927	arg1	A					929:929	glycophorin A	917:929	glycophorin A	917:929	It was calculated that glycophorin A from the original Cad donor (Cad.)
4091823	4	4	dep	Gal	645:647	arg1	2-3					640:642	alpha 2-3	634:642	alpha 2-3	634:642	carry the same pentasaccharide GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc -ol(Cad determinant) but in different amounts.
4091823	4	4	dep	Gal	645:647	arg1	alpha					665:669	alpha 2-6	665:673	alpha 2-6	665:673	carry the same pentasaccharide GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc -ol(Cad determinant) but in different amounts.
4091823	4	4	dep	Gal	645:647	arg1	[NeuAc					627:632	the same pentasaccharide GalNAc(beta 1-4)[NeuAc	586:632	the same pentasaccharide GalNAc(beta 1-4)[NeuAc(alpha 2-3)	586:643	carry the same pentasaccharide GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc -ol(Cad determinant) but in different amounts.
4091823	4	4	dep	Gal	645:647	arg1	[NeuAc					658:663	beta 1-3)[NeuAc	649:663	beta 1-3)[NeuAc(alpha 2-6)	649:674	carry the same pentasaccharide GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc -ol(Cad determinant) but in different amounts.
4091823	2	5	theme	red	528:530	arg1	cells					532:536	the three blood group Cad red cells	502:536	the three blood group Cad red cells under study (samples Cad., Bui	502:567	Structure determination of the major acid components by methylation analysis, g.l.c.-m.s. and 1H-n.m.r. indicated that the three blood group Cad red cells under study (samples Cad., Bui.
4091823	6	6	dep	calculated	901:910	arg1	Cad					960:962	Cad	960:962	Cad	960:962	It was calculated that glycophorin A from the original Cad donor (Cad.)
4091823	16	7	theme	glycoprotein	1810:1821	arg1	molecules					1823:1831	glycoprotein molecules	1810:1831	glycoprotein molecules with varying amounts of Cad determinants	1810:1872	do not carry a mixture of glycophorin A molecules with or without the Cad pentasaccharides but a spectrum of glycoprotein molecules with varying amounts of Cad determinants.
4091823	14	8	theme	dodecyl	1587:1593	arg1	electrophoresis					1623:1637	sodium dodecyl sulphate/polyacrylamide-gel electrophoresis	1580:1637	sodium dodecyl sulphate/polyacrylamide-gel electrophoresis studies	1580:1645	From the results presented above and sodium dodecyl sulphate/polyacrylamide-gel electrophoresis studies it is suggested that Cad red cells from Bui.
4091823	4	9	theme	different	711:719	arg1	amounts					721:727	different amounts	711:727	different amounts	711:727	carry the same pentasaccharide GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc -ol(Cad determinant) but in different amounts.
4091823	7	10	theme	unrelated	1123:1131	arg1	individuals					1137:1147	the two other unrelated Cad individuals	1109:1147	the two other unrelated Cad individuals	1109:1147	carries about 12 O-glycosidically linked pentasaccharide chains per molecule whereas only 2-3 of these chains were present in the samples from the two other unrelated Cad individuals (Bui.
4091823	0	11	theme	Sd	80:81	arg1	erythrocytes					87:98	human Cad, Sd(a+) and Sd(a-) erythrocytes	58:98	human Cad, Sd(a+) and Sd(a-) erythrocytes	58:98	Comparative study of glycophorin A derived O-glycans from human Cad, Sd(a+) and Sd(a-) erythrocytes.
4091823	11	12	dep	agglutinated	1438:1449	arg1	Bui					1452:1454	Bui	1452:1454	Bui	1452:1454	donor) whereas others are only partially agglutinated (Bui.
4091823	16	13	gly	glycoprotein	1810:1821	arg1	glycoprotein					1810:1821	glycoprotein molecules	1810:1831	glycoprotein molecules with varying amounts of Cad determinants	1810:1872	do not carry a mixture of glycophorin A molecules with or without the Cad pentasaccharides but a spectrum of glycoprotein molecules with varying amounts of Cad determinants.
4091823	9	14	theme	quantitative	1187:1198	arg1	studies					1214:1220	quantitative agglutination studies	1187:1220	quantitative agglutination studies	1187:1220	It is well known from quantitative agglutination studies that the proportion of red cells which can be agglutinated by the Dolichos biflorus lectin varies from one Cad blood sample to another.
4091823	7	15	link	linked	1000:1005	arg1	chains					1023:1028	about 12 O-glycosidically linked pentasaccharide chains	974:1028	about 12 O-glycosidically linked pentasaccharide chains per molecule	974:1041	carries about 12 O-glycosidically linked pentasaccharide chains per molecule whereas only 2-3 of these chains were present in the samples from the two other unrelated Cad individuals (Bui.
4091823	4	16	theme	same	590:593	arg1	[NeuAc					627:632	the same pentasaccharide GalNAc(beta 1-4)[NeuAc	586:632	the same pentasaccharide GalNAc(beta 1-4)[NeuAc(alpha 2-3)	586:643	carry the same pentasaccharide GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc -ol(Cad determinant) but in different amounts.
4091823	4	16	theme	same	590:593	arg1	2-3					640:642	alpha 2-3	634:642	alpha 2-3	634:642	carry the same pentasaccharide GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc -ol(Cad determinant) but in different amounts.
4091823	16	17	theme	Cad	1857:1859	arg1	determinants					1861:1872	Cad determinants	1857:1872	Cad determinants	1857:1872	do not carry a mixture of glycophorin A molecules with or without the Cad pentasaccharides but a spectrum of glycoprotein molecules with varying amounts of Cad determinants.
4091823	5	18	theme	Sd	805:806	arg1	donors					813:818	glycophorin A of Sd(a+) and Sd (a-) donors	777:818	glycophorin A of Sd(a+) and Sd (a-) donors	777:818	This pentasaccharide, however, was absent from glycophorin A of Sd(a+) and Sd (a-) donors, suggesting that the Sda determinant is not associated with glycophorins.
4091823	4	19	theme	GalNAc	611:616	arg1	[NeuAc					627:632	the same pentasaccharide GalNAc(beta 1-4)[NeuAc	586:632	the same pentasaccharide GalNAc(beta 1-4)[NeuAc(alpha 2-3)	586:643	carry the same pentasaccharide GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc -ol(Cad determinant) but in different amounts.
4091823	4	19	theme	GalNAc	611:616	arg1	2-3					640:642	alpha 2-3	634:642	alpha 2-3	634:642	carry the same pentasaccharide GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc -ol(Cad determinant) but in different amounts.
4091823	1	20	theme	silica	326:331	arg1	column					337:342	an alkylamine silica gel column	312:342	an alkylamine silica gel column	312:342	Glycophorin A was purified from the erythrocyte membranes of blood group Cad, Sd(a+) and Sd(a-) donors and the oligosaccharide alditols, obtained after alkaline borohydride degradation, separated by h.p.l.c. on an alkylamine silica gel column, were characterized by sugar analysis.
4091823	7	21	from	individuals	1137:1147	arg1	samples					1096:1102	the samples	1092:1102	the samples from the two other unrelated Cad individuals	1092:1147	carries about 12 O-glycosidically linked pentasaccharide chains per molecule whereas only 2-3 of these chains were present in the samples from the two other unrelated Cad individuals (Bui.
4091823	13	22	contain	carry	1515:1519	arg1	cells					1499:1503	some red cells	1490:1503	some red cells	1490:1503	donors) suggesting that some red cells might not carry the Cad determinants.
4091823	13	22	contain	carry	1515:1519	arg2	determinants					1529:1540	the Cad determinants	1521:1540	the Cad determinants	1521:1540	donors) suggesting that some red cells might not carry the Cad determinants.
4091823	6	23	theme	original	940:947	arg1	donor					953:957	the original Cad donor	936:957	the original Cad donor	936:957	It was calculated that glycophorin A from the original Cad donor (Cad.)
4091823	9	24	dep	Dolichos	1288:1295	arg1	biflorus					1297:1304	biflorus	1297:1304	biflorus	1297:1304	It is well known from quantitative agglutination studies that the proportion of red cells which can be agglutinated by the Dolichos biflorus lectin varies from one Cad blood sample to another.
4091823	5	25	theme	glycophorin	777:787	arg1	a+					797:798	a+	797:798	a+	797:798	This pentasaccharide, however, was absent from glycophorin A of Sd(a+) and Sd (a-) donors, suggesting that the Sda determinant is not associated with glycophorins.
4091823	5	25	theme	glycophorin	777:787	arg1	A					789:789	glycophorin A	777:789	glycophorin A of Sd(a+)	777:799	This pentasaccharide, however, was absent from glycophorin A of Sd(a+) and Sd (a-) donors, suggesting that the Sda determinant is not associated with glycophorins.
4091823	9	26	theme	cells	1249:1253	arg1	proportion					1231:1240	the proportion	1227:1240	the proportion of red cells which can be agglutinated by the Dolichos biflorus lectin	1227:1311	It is well known from quantitative agglutination studies that the proportion of red cells which can be agglutinated by the Dolichos biflorus lectin varies from one Cad blood sample to another.
4091823	1	27	theme	alkaline	253:260	arg1	degradation					274:284	alkaline borohydride degradation	253:284	alkaline borohydride degradation	253:284	Glycophorin A was purified from the erythrocyte membranes of blood group Cad, Sd(a+) and Sd(a-) donors and the oligosaccharide alditols, obtained after alkaline borohydride degradation, separated by h.p.l.c. on an alkylamine silica gel column, were characterized by sugar analysis.
4091823	7	28	from	present	1081:1087	arg1	samples					1096:1102	the samples	1092:1102	the samples from the two other unrelated Cad individuals	1092:1147	carries about 12 O-glycosidically linked pentasaccharide chains per molecule whereas only 2-3 of these chains were present in the samples from the two other unrelated Cad individuals (Bui.
4091823	2	29	theme	acid	420:423	arg1	components					425:434	the major acid components	410:434	the major acid components	410:434	Structure determination of the major acid components by methylation analysis, g.l.c.-m.s. and 1H-n.m.r. indicated that the three blood group Cad red cells under study (samples Cad., Bui.
4091823	0	30	theme	Comparative	0:10	arg1	study					12:16	Comparative study	0:16	Comparative study of glycophorin A	0:33	Comparative study of glycophorin A derived O-glycans from human Cad, Sd(a+) and Sd(a-) erythrocytes.
4091823	1	31	theme	Sd	190:191	arg1	a-					193:194	a-	193:194	a-	193:194	Glycophorin A was purified from the erythrocyte membranes of blood group Cad, Sd(a+) and Sd(a-) donors and the oligosaccharide alditols, obtained after alkaline borohydride degradation, separated by h.p.l.c. on an alkylamine silica gel column, were characterized by sugar analysis.
4091823	1	31	theme	Sd	190:191	arg1	donors					197:202	blood group Cad, Sd(a+) and Sd(a-) donors	162:202	donors	197:202	Glycophorin A was purified from the erythrocyte membranes of blood group Cad, Sd(a+) and Sd(a-) donors and the oligosaccharide alditols, obtained after alkaline borohydride degradation, separated by h.p.l.c. on an alkylamine silica gel column, were characterized by sugar analysis.
4091823	1	32	dep	a+	182:183	arg1	Sd					179:180	blood group Cad, Sd(a+) and Sd(a-) donors	162:202	Sd	179:180	Glycophorin A was purified from the erythrocyte membranes of blood group Cad, Sd(a+) and Sd(a-) donors and the oligosaccharide alditols, obtained after alkaline borohydride degradation, separated by h.p.l.c. on an alkylamine silica gel column, were characterized by sugar analysis.
4091823	0	33	theme	human	58:62	arg1	erythrocytes					87:98	human Cad, Sd(a+) and Sd(a-) erythrocytes	58:98	human Cad, Sd(a+) and Sd(a-) erythrocytes	58:98	Comparative study of glycophorin A derived O-glycans from human Cad, Sd(a+) and Sd(a-) erythrocytes.
4091823	16	34	theme	glycophorin	1727:1737	arg1	A					1739:1739	glycophorin A	1727:1739	glycophorin A molecules with or without the Cad pentasaccharides	1727:1790	do not carry a mixture of glycophorin A molecules with or without the Cad pentasaccharides but a spectrum of glycoprotein molecules with varying amounts of Cad determinants.
4091823	11	35	theme	whereas	1404:1410	arg1	others					1412:1417	donor) whereas others	1397:1417	donor) whereas others	1397:1417	donor) whereas others are only partially agglutinated (Bui.
4091823	10	36	dep	agglutinated	1378:1389	arg1	Cad					1392:1394	Cad	1392:1394	Cad	1392:1394	Some are completely agglutinated (Cad.
4091823	0	37	theme	A	33:33	arg1	study					12:16	Comparative study	0:16	Comparative study of glycophorin A	0:33	Comparative study of glycophorin A derived O-glycans from human Cad, Sd(a+) and Sd(a-) erythrocytes.
4091823	1	38	theme	donors	197:202	arg1	membranes					149:157	the erythrocyte membranes	133:157	the erythrocyte membranes of blood group Cad, Sd(a+) and Sd(a-) donors	133:202	Glycophorin A was purified from the erythrocyte membranes of blood group Cad, Sd(a+) and Sd(a-) donors and the oligosaccharide alditols, obtained after alkaline borohydride degradation, separated by h.p.l.c. on an alkylamine silica gel column, were characterized by sugar analysis.
4091823	16	39	theme	molecules	1741:1749	arg1	mixture					1716:1722	a mixture	1714:1722	a mixture of glycophorin A molecules with or without the Cad pentasaccharides	1714:1790	do not carry a mixture of glycophorin A molecules with or without the Cad pentasaccharides but a spectrum of glycoprotein molecules with varying amounts of Cad determinants.
4091823	11	40	theme	donor	1397:1401	arg1	others					1412:1417	donor) whereas others	1397:1417	donor) whereas others	1397:1417	donor) whereas others are only partially agglutinated (Bui.
4091823	14	41	theme	Cad	1668:1670	arg1	cells					1676:1680	Cad red cells	1668:1680	Cad red cells from Bui	1668:1689	From the results presented above and sodium dodecyl sulphate/polyacrylamide-gel electrophoresis studies it is suggested that Cad red cells from Bui.
4091823	16	42	with	molecules	1823:1831	arg1	amounts					1846:1852	varying amounts	1838:1852	varying amounts of Cad determinants	1838:1872	do not carry a mixture of glycophorin A molecules with or without the Cad pentasaccharides but a spectrum of glycoprotein molecules with varying amounts of Cad determinants.
4091823	16	42	with	molecules	1823:1831	arg1	determinants					1861:1872	Cad determinants	1857:1872	Cad determinants	1857:1872	do not carry a mixture of glycophorin A molecules with or without the Cad pentasaccharides but a spectrum of glycoprotein molecules with varying amounts of Cad determinants.
4091823	1	43	theme	group	168:172	arg1	a+					182:183	blood group Cad, Sd(a+) and Sd(a-) donors	162:202	a+	182:183	Glycophorin A was purified from the erythrocyte membranes of blood group Cad, Sd(a+) and Sd(a-) donors and the oligosaccharide alditols, obtained after alkaline borohydride degradation, separated by h.p.l.c. on an alkylamine silica gel column, were characterized by sugar analysis.
4091823	9	44	theme	blood	1333:1337	arg1	sample					1339:1344	one Cad blood sample	1325:1344	one Cad blood sample	1325:1344	It is well known from quantitative agglutination studies that the proportion of red cells which can be agglutinated by the Dolichos biflorus lectin varies from one Cad blood sample to another.
4091823	7	45	theme	pentasaccharide	1007:1021	arg1	chains					1023:1028	about 12 O-glycosidically linked pentasaccharide chains	974:1028	about 12 O-glycosidically linked pentasaccharide chains per molecule	974:1041	carries about 12 O-glycosidically linked pentasaccharide chains per molecule whereas only 2-3 of these chains were present in the samples from the two other unrelated Cad individuals (Bui.
4091823	13	46	theme	red	1495:1497	arg1	cells					1499:1503	some red cells	1490:1503	some red cells	1490:1503	donors) suggesting that some red cells might not carry the Cad determinants.
4091823	14	47	theme	electrophoresis	1623:1637	arg1	studies					1639:1645	sodium dodecyl sulphate/polyacrylamide-gel electrophoresis studies	1580:1645	sodium dodecyl sulphate/polyacrylamide-gel electrophoresis studies	1580:1645	From the results presented above and sodium dodecyl sulphate/polyacrylamide-gel electrophoresis studies it is suggested that Cad red cells from Bui.
4091823	5	48	theme	Sd	794:795	arg1	a-					809:810	a-	809:810	a-	809:810	This pentasaccharide, however, was absent from glycophorin A of Sd(a+) and Sd (a-) donors, suggesting that the Sda determinant is not associated with glycophorins.
4091823	5	48	theme	Sd	794:795	arg1	a+					797:798	a+	797:798	a+	797:798	This pentasaccharide, however, was absent from glycophorin A of Sd(a+) and Sd (a-) donors, suggesting that the Sda determinant is not associated with glycophorins.
4091823	5	48	theme	Sd	794:795	arg1	Sd					805:806	Sd	805:806	Sd (a-)	805:811	This pentasaccharide, however, was absent from glycophorin A of Sd(a+) and Sd (a-) donors, suggesting that the Sda determinant is not associated with glycophorins.
4091823	5	48	theme	Sd	794:795	arg1	A					789:789	glycophorin A	777:789	glycophorin A of Sd(a+)	777:799	This pentasaccharide, however, was absent from glycophorin A of Sd(a+) and Sd (a-) donors, suggesting that the Sda determinant is not associated with glycophorins.
4091823	2	49	dep	indicated	487:495	arg1	cells					532:536	the three blood group Cad red cells	502:536	the three blood group Cad red cells under study (samples Cad., Bui	502:567	Structure determination of the major acid components by methylation analysis, g.l.c.-m.s. and 1H-n.m.r. indicated that the three blood group Cad red cells under study (samples Cad., Bui.
4091823	2	50	theme	blood	512:516	arg1	cells					532:536	the three blood group Cad red cells	502:536	the three blood group Cad red cells under study (samples Cad., Bui	502:567	Structure determination of the major acid components by methylation analysis, g.l.c.-m.s. and 1H-n.m.r. indicated that the three blood group Cad red cells under study (samples Cad., Bui.
4091823	9	51	theme	red	1245:1247	arg1	cells					1249:1253	red cells	1245:1253	red cells which can be agglutinated by the Dolichos biflorus lectin	1245:1311	It is well known from quantitative agglutination studies that the proportion of red cells which can be agglutinated by the Dolichos biflorus lectin varies from one Cad blood sample to another.
4091823	16	52	theme	molecules	1823:1831	arg1	spectrum					1798:1805	a spectrum	1796:1805	a spectrum of glycoprotein molecules with varying amounts of Cad determinants	1796:1872	do not carry a mixture of glycophorin A molecules with or without the Cad pentasaccharides but a spectrum of glycoprotein molecules with varying amounts of Cad determinants.
4091823	1	53	theme	sugar	367:371	arg1	analysis					373:380	sugar analysis	367:380	sugar analysis	367:380	Glycophorin A was purified from the erythrocyte membranes of blood group Cad, Sd(a+) and Sd(a-) donors and the oligosaccharide alditols, obtained after alkaline borohydride degradation, separated by h.p.l.c. on an alkylamine silica gel column, were characterized by sugar analysis.
4091823	14	54	theme	sulphate/polyacrylamide-gel	1595:1621	arg1	electrophoresis					1623:1637	sodium dodecyl sulphate/polyacrylamide-gel electrophoresis	1580:1637	sodium dodecyl sulphate/polyacrylamide-gel electrophoresis studies	1580:1645	From the results presented above and sodium dodecyl sulphate/polyacrylamide-gel electrophoresis studies it is suggested that Cad red cells from Bui.
4091823	2	55	theme	Cad	524:526	arg1	cells					532:536	the three blood group Cad red cells	502:536	the three blood group Cad red cells under study (samples Cad., Bui	502:567	Structure determination of the major acid components by methylation analysis, g.l.c.-m.s. and 1H-n.m.r. indicated that the three blood group Cad red cells under study (samples Cad., Bui.
4091823	16	56	theme	varying	1838:1844	arg1	amounts					1846:1852	varying amounts	1838:1852	varying amounts of Cad determinants	1838:1872	do not carry a mixture of glycophorin A molecules with or without the Cad pentasaccharides but a spectrum of glycoprotein molecules with varying amounts of Cad determinants.
4091823	16	56	theme	varying	1838:1844	arg1	determinants					1861:1872	Cad determinants	1857:1872	Cad determinants	1857:1872	do not carry a mixture of glycophorin A molecules with or without the Cad pentasaccharides but a spectrum of glycoprotein molecules with varying amounts of Cad determinants.
4091823	1	57	theme	erythrocyte	137:147	arg1	membranes					149:157	the erythrocyte membranes	133:157	the erythrocyte membranes of blood group Cad, Sd(a+) and Sd(a-) donors	133:202	Glycophorin A was purified from the erythrocyte membranes of blood group Cad, Sd(a+) and Sd(a-) donors and the oligosaccharide alditols, obtained after alkaline borohydride degradation, separated by h.p.l.c. on an alkylamine silica gel column, were characterized by sugar analysis.
4091823	2	58	dep	cells	532:536	arg1	samples					551:557	samples Cad., Bui	551:567	the three blood group Cad red cells under study (samples Cad., Bui	502:567	Structure determination of the major acid components by methylation analysis, g.l.c.-m.s. and 1H-n.m.r. indicated that the three blood group Cad red cells under study (samples Cad., Bui.
4091823	7	59	theme	Cad	1133:1135	arg1	individuals					1137:1147	the two other unrelated Cad individuals	1109:1147	the two other unrelated Cad individuals	1109:1147	carries about 12 O-glycosidically linked pentasaccharide chains per molecule whereas only 2-3 of these chains were present in the samples from the two other unrelated Cad individuals (Bui.
4091823	2	60	theme	methylation	439:449	arg1	analysis					451:458	methylation analysis	439:458	methylation analysis	439:458	Structure determination of the major acid components by methylation analysis, g.l.c.-m.s. and 1H-n.m.r. indicated that the three blood group Cad red cells under study (samples Cad., Bui.
4091823	7	61	theme	other	1117:1121	arg1	individuals					1137:1147	the two other unrelated Cad individuals	1109:1147	the two other unrelated Cad individuals	1109:1147	carries about 12 O-glycosidically linked pentasaccharide chains per molecule whereas only 2-3 of these chains were present in the samples from the two other unrelated Cad individuals (Bui.
4091823	16	62	theme	determinants	1861:1872	arg1	amounts					1846:1852	varying amounts	1838:1852	varying amounts of Cad determinants	1838:1872	do not carry a mixture of glycophorin A molecules with or without the Cad pentasaccharides but a spectrum of glycoprotein molecules with varying amounts of Cad determinants.
4091823	16	62	theme	determinants	1861:1872	arg1	determinants					1861:1872	Cad determinants	1857:1872	Cad determinants	1857:1872	do not carry a mixture of glycophorin A molecules with or without the Cad pentasaccharides but a spectrum of glycoprotein molecules with varying amounts of Cad determinants.
4091823	9	63	theme	agglutination	1200:1212	arg1	studies					1214:1220	quantitative agglutination studies	1187:1220	quantitative agglutination studies	1187:1220	It is well known from quantitative agglutination studies that the proportion of red cells which can be agglutinated by the Dolichos biflorus lectin varies from one Cad blood sample to another.
4091823	4	64	theme	Cad	687:689	arg1	-ol					683:685	the same pentasaccharide GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc -ol	586:685	the same pentasaccharide GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc -ol(Cad determinant)	586:702	carry the same pentasaccharide GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc -ol(Cad determinant) but in different amounts.
4091823	4	64	theme	Cad	687:689	arg1	determinant					691:701	Cad determinant	687:701	Cad determinant	687:701	carry the same pentasaccharide GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc -ol(Cad determinant) but in different amounts.
4091823	1	65	theme	alkylamine	315:324	arg1	column					337:342	an alkylamine silica gel column	312:342	an alkylamine silica gel column	312:342	Glycophorin A was purified from the erythrocyte membranes of blood group Cad, Sd(a+) and Sd(a-) donors and the oligosaccharide alditols, obtained after alkaline borohydride degradation, separated by h.p.l.c. on an alkylamine silica gel column, were characterized by sugar analysis.
4091823	6	66	theme	Cad	949:951	arg1	donor					953:957	the original Cad donor	936:957	the original Cad donor	936:957	It was calculated that glycophorin A from the original Cad donor (Cad.)
4091823	4	67	theme	pentasaccharide	595:609	arg1	beta					618:621	beta 1-4	618:625	beta 1-4	618:625	carry the same pentasaccharide GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc -ol(Cad determinant) but in different amounts.
4091823	4	67	theme	pentasaccharide	595:609	arg1	GalNAc					611:616	pentasaccharide GalNAc	595:616	the same pentasaccharide GalNAc(beta 1-4)[NeuAc(alpha 2-3)	586:643	carry the same pentasaccharide GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc -ol(Cad determinant) but in different amounts.
4091823	0	68	theme	Cad	64:66	arg1	erythrocytes					87:98	human Cad, Sd(a+) and Sd(a-) erythrocytes	58:98	human Cad, Sd(a+) and Sd(a-) erythrocytes	58:98	Comparative study of glycophorin A derived O-glycans from human Cad, Sd(a+) and Sd(a-) erythrocytes.
4091823	1	69	theme	gel	333:335	arg1	column					337:342	an alkylamine silica gel column	312:342	an alkylamine silica gel column	312:342	Glycophorin A was purified from the erythrocyte membranes of blood group Cad, Sd(a+) and Sd(a-) donors and the oligosaccharide alditols, obtained after alkaline borohydride degradation, separated by h.p.l.c. on an alkylamine silica gel column, were characterized by sugar analysis.
4091823	14	70	theme	sodium	1580:1585	arg1	electrophoresis					1623:1637	sodium dodecyl sulphate/polyacrylamide-gel electrophoresis	1580:1637	sodium dodecyl sulphate/polyacrylamide-gel electrophoresis studies	1580:1645	From the results presented above and sodium dodecyl sulphate/polyacrylamide-gel electrophoresis studies it is suggested that Cad red cells from Bui.
4091823	7	71	attach	present	1081:1087	arg2	chains					1069:1074	these chains	1063:1074	these chains	1063:1074	carries about 12 O-glycosidically linked pentasaccharide chains per molecule whereas only 2-3 of these chains were present in the samples from the two other unrelated Cad individuals (Bui.
4091823	7	71	attach	present	1081:1087	arg1	samples					1096:1102	the samples	1092:1102	the samples from the two other unrelated Cad individuals	1092:1147	carries about 12 O-glycosidically linked pentasaccharide chains per molecule whereas only 2-3 of these chains were present in the samples from the two other unrelated Cad individuals (Bui.
4091823	7	71	attach	present	1081:1087	arg2	2-3					1056:1058	2-3	1056:1058	2-3	1056:1058	carries about 12 O-glycosidically linked pentasaccharide chains per molecule whereas only 2-3 of these chains were present in the samples from the two other unrelated Cad individuals (Bui.
4091823	0	72	theme	Sd	69:70	arg1	erythrocytes					87:98	human Cad, Sd(a+) and Sd(a-) erythrocytes	58:98	human Cad, Sd(a+) and Sd(a-) erythrocytes	58:98	Comparative study of glycophorin A derived O-glycans from human Cad, Sd(a+) and Sd(a-) erythrocytes.
4091823	1	73	theme	Glycophorin	101:111	arg1	A					113:113	Glycophorin A	101:113	Glycophorin A	101:113	Glycophorin A was purified from the erythrocyte membranes of blood group Cad, Sd(a+) and Sd(a-) donors and the oligosaccharide alditols, obtained after alkaline borohydride degradation, separated by h.p.l.c. on an alkylamine silica gel column, were characterized by sugar analysis.
4091823	2	74	theme	Structure	383:391	arg1	determination					393:405	Structure determination	383:405	Structure determination of the major acid components by methylation analysis, g.l.c.-m.s. and 1H-n.m.r.	383:485	Structure determination of the major acid components by methylation analysis, g.l.c.-m.s. and 1H-n.m.r. indicated that the three blood group Cad red cells under study (samples Cad., Bui.
4091823	5	75	theme	A	789:789	arg1	donors					813:818	glycophorin A of Sd(a+) and Sd (a-) donors	777:818	glycophorin A of Sd(a+) and Sd (a-) donors	777:818	This pentasaccharide, however, was absent from glycophorin A of Sd(a+) and Sd (a-) donors, suggesting that the Sda determinant is not associated with glycophorins.
4091823	2	76	dep	samples	551:557	arg1	Bui					565:567	Bui	565:567	Bui	565:567	Structure determination of the major acid components by methylation analysis, g.l.c.-m.s. and 1H-n.m.r. indicated that the three blood group Cad red cells under study (samples Cad., Bui.
4091823	2	77	theme	components	425:434	arg1	determination					393:405	Structure determination	383:405	Structure determination of the major acid components by methylation analysis, g.l.c.-m.s. and 1H-n.m.r.	383:485	Structure determination of the major acid components by methylation analysis, g.l.c.-m.s. and 1H-n.m.r. indicated that the three blood group Cad red cells under study (samples Cad., Bui.
4091823	16	78	theme	Cad	1771:1773	arg1	pentasaccharides					1775:1790	the Cad pentasaccharides	1767:1790	the Cad pentasaccharides	1767:1790	do not carry a mixture of glycophorin A molecules with or without the Cad pentasaccharides but a spectrum of glycoprotein molecules with varying amounts of Cad determinants.
4091823	5	79	from	donors	813:818	arg1	absent					765:770	absent	765:770	absent	765:770	This pentasaccharide, however, was absent from glycophorin A of Sd(a+) and Sd (a-) donors, suggesting that the Sda determinant is not associated with glycophorins.
4091823	1	80	theme	borohydride	262:272	arg1	degradation					274:284	alkaline borohydride degradation	253:284	alkaline borohydride degradation	253:284	Glycophorin A was purified from the erythrocyte membranes of blood group Cad, Sd(a+) and Sd(a-) donors and the oligosaccharide alditols, obtained after alkaline borohydride degradation, separated by h.p.l.c. on an alkylamine silica gel column, were characterized by sugar analysis.
4091823	4	81	theme	GalNAc	676:681	arg1	-ol					683:685	the same pentasaccharide GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc -ol	586:685	the same pentasaccharide GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc -ol(Cad determinant)	586:702	carry the same pentasaccharide GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc -ol(Cad determinant) but in different amounts.
4091823	4	81	theme	GalNAc	676:681	arg1	determinant					691:701	Cad determinant	687:701	Cad determinant	687:701	carry the same pentasaccharide GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc -ol(Cad determinant) but in different amounts.
4091823	2	82	theme	major	414:418	arg1	components					425:434	the major acid components	410:434	the major acid components	410:434	Structure determination of the major acid components by methylation analysis, g.l.c.-m.s. and 1H-n.m.r. indicated that the three blood group Cad red cells under study (samples Cad., Bui.
4091823	4	83	theme	alpha	634:638	arg1	[NeuAc					627:632	the same pentasaccharide GalNAc(beta 1-4)[NeuAc	586:632	the same pentasaccharide GalNAc(beta 1-4)[NeuAc(alpha 2-3)	586:643	carry the same pentasaccharide GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc -ol(Cad determinant) but in different amounts.
4091823	4	83	theme	alpha	634:638	arg1	2-3					640:642	alpha 2-3	634:642	alpha 2-3	634:642	carry the same pentasaccharide GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc -ol(Cad determinant) but in different amounts.
4091823	14	84	from	Bui	1687:1689	arg1	cells					1676:1680	Cad red cells	1668:1680	Cad red cells from Bui	1668:1689	From the results presented above and sodium dodecyl sulphate/polyacrylamide-gel electrophoresis studies it is suggested that Cad red cells from Bui.
4091823	5	85	theme	Sda	841:843	arg1	determinant					845:855	the Sda determinant	837:855	the Sda determinant	837:855	This pentasaccharide, however, was absent from glycophorin A of Sd(a+) and Sd (a-) donors, suggesting that the Sda determinant is not associated with glycophorins.
4091823	0	86	theme	glycophorin	21:31	arg1	A					33:33	glycophorin A	21:33	glycophorin A	21:33	Comparative study of glycophorin A derived O-glycans from human Cad, Sd(a+) and Sd(a-) erythrocytes.
4091823	9	87	theme	Dolichos	1288:1295	arg1	lectin					1306:1311	the Dolichos biflorus lectin	1284:1311	the Dolichos biflorus lectin	1284:1311	It is well known from quantitative agglutination studies that the proportion of red cells which can be agglutinated by the Dolichos biflorus lectin varies from one Cad blood sample to another.
4091823	13	88	theme	Cad	1525:1527	arg1	determinants					1529:1540	the Cad determinants	1521:1540	the Cad determinants	1521:1540	donors) suggesting that some red cells might not carry the Cad determinants.
4091823	7	89	theme	chains	1069:1074	arg1	2-3					1056:1058	2-3	1056:1058	2-3	1056:1058	carries about 12 O-glycosidically linked pentasaccharide chains per molecule whereas only 2-3 of these chains were present in the samples from the two other unrelated Cad individuals (Bui.
4091823	7	89	theme	chains	1069:1074	arg1	chains					1069:1074	these chains	1063:1074	these chains	1063:1074	carries about 12 O-glycosidically linked pentasaccharide chains per molecule whereas only 2-3 of these chains were present in the samples from the two other unrelated Cad individuals (Bui.
4091823	4	90	theme	beta	649:652	arg1	alpha					665:669	alpha 2-6	665:673	alpha 2-6	665:673	carry the same pentasaccharide GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc -ol(Cad determinant) but in different amounts.
4091823	4	90	theme	beta	649:652	arg1	[NeuAc					658:663	beta 1-3)[NeuAc	649:663	beta 1-3)[NeuAc(alpha 2-6)	649:674	carry the same pentasaccharide GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc -ol(Cad determinant) but in different amounts.
4091823	7	91	dep	present	1081:1087	arg1	Bui					1150:1152	Bui	1150:1152	Bui	1150:1152	carries about 12 O-glycosidically linked pentasaccharide chains per molecule whereas only 2-3 of these chains were present in the samples from the two other unrelated Cad individuals (Bui.
4091823	14	92	theme	red	1672:1674	arg1	cells					1676:1680	Cad red cells	1668:1680	Cad red cells from Bui	1668:1689	From the results presented above and sodium dodecyl sulphate/polyacrylamide-gel electrophoresis studies it is suggested that Cad red cells from Bui.
4091823	16	93	theme	A	1739:1739	arg1	molecules					1741:1749	glycophorin A molecules	1727:1749	glycophorin A molecules with or without the Cad pentasaccharides	1727:1790	do not carry a mixture of glycophorin A molecules with or without the Cad pentasaccharides but a spectrum of glycoprotein molecules with varying amounts of Cad determinants.
4091823	1	94	theme	oligosaccharide	212:226	arg1	alditols					228:235	the oligosaccharide alditols	208:235	the oligosaccharide alditols	208:235	Glycophorin A was purified from the erythrocyte membranes of blood group Cad, Sd(a+) and Sd(a-) donors and the oligosaccharide alditols, obtained after alkaline borohydride degradation, separated by h.p.l.c. on an alkylamine silica gel column, were characterized by sugar analysis.
4091823	9	95	theme	Cad	1329:1331	arg1	sample					1339:1344	one Cad blood sample	1325:1344	one Cad blood sample	1325:1344	It is well known from quantitative agglutination studies that the proportion of red cells which can be agglutinated by the Dolichos biflorus lectin varies from one Cad blood sample to another.
4091823	7	96	theme	linked	1000:1005	arg1	chains					1023:1028	about 12 O-glycosidically linked pentasaccharide chains	974:1028	about 12 O-glycosidically linked pentasaccharide chains per molecule	974:1041	carries about 12 O-glycosidically linked pentasaccharide chains per molecule whereas only 2-3 of these chains were present in the samples from the two other unrelated Cad individuals (Bui.
4091823	1	97	theme	Cad	174:176	arg1	a+					182:183	blood group Cad, Sd(a+) and Sd(a-) donors	162:202	a+	182:183	Glycophorin A was purified from the erythrocyte membranes of blood group Cad, Sd(a+) and Sd(a-) donors and the oligosaccharide alditols, obtained after alkaline borohydride degradation, separated by h.p.l.c. on an alkylamine silica gel column, were characterized by sugar analysis.
4091823	1	98	theme	blood	162:166	arg1	a+					182:183	blood group Cad, Sd(a+) and Sd(a-) donors	162:202	a+	182:183	Glycophorin A was purified from the erythrocyte membranes of blood group Cad, Sd(a+) and Sd(a-) donors and the oligosaccharide alditols, obtained after alkaline borohydride degradation, separated by h.p.l.c. on an alkylamine silica gel column, were characterized by sugar analysis.
4091823	4	99	theme	Gal	645:647	arg1	GalNAc					676:681	the same pentasaccharide GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc	586:681	the same pentasaccharide GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc -ol(Cad determinant)	586:702	carry the same pentasaccharide GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc -ol(Cad determinant) but in different amounts.
4091823	7	100	located	present	1081:1087	arg2	chains					1069:1074	these chains	1063:1074	these chains	1063:1074	carries about 12 O-glycosidically linked pentasaccharide chains per molecule whereas only 2-3 of these chains were present in the samples from the two other unrelated Cad individuals (Bui.
4091823	7	100	located	present	1081:1087	arg1	samples					1096:1102	the samples	1092:1102	the samples from the two other unrelated Cad individuals	1092:1147	carries about 12 O-glycosidically linked pentasaccharide chains per molecule whereas only 2-3 of these chains were present in the samples from the two other unrelated Cad individuals (Bui.
4091823	7	100	located	present	1081:1087	arg2	2-3					1056:1058	2-3	1056:1058	2-3	1056:1058	carries about 12 O-glycosidically linked pentasaccharide chains per molecule whereas only 2-3 of these chains were present in the samples from the two other unrelated Cad individuals (Bui.
3967649	5	0	theme	potent	1152:1157	arg1	inhibitor					1159:1167	a potent inhibitor	1150:1167	a potent inhibitor of human anti-Sda antibody	1150:1194	The major pentasaccharide (oligosaccharide 6) carries the blood group Cad determinant and is a potent inhibitor of human anti-Sda antibody.
3967649	5	1	theme	anti-Sda	1178:1185	arg1	antibody					1187:1194	human anti-Sda antibody	1172:1194	human anti-Sda antibody	1172:1194	The major pentasaccharide (oligosaccharide 6) carries the blood group Cad determinant and is a potent inhibitor of human anti-Sda antibody.
3967649	1	2	theme	Cad	273:275	arg1	individual					238:247	one individual	234:247	one individual of the rare blood group Cad	234:275	Alkaline borohydride reductive cleavage (beta-elimination) of glycophorin A isolated from one individual of the rare blood group Cad, resulted in the release of six acidic oligosaccharide-alditols which were separated by high-performance liquid chromatography (HPLC) on an alkyl amine silicagel column.
3967649	0	3	theme	permethylation	87:100	arg1	analysis					102:109	permethylation analysis	87:109	permethylation analysis	87:109	Structure determination of oligosaccharides isolated from Cad erythrocyte membranes by permethylation analysis and 500-MHz 1H-NMR spectroscopy.
3967649	1	4	theme	high-performance	365:380	arg1	HPLC					405:408	HPLC	405:408	HPLC	405:408	Alkaline borohydride reductive cleavage (beta-elimination) of glycophorin A isolated from one individual of the rare blood group Cad, resulted in the release of six acidic oligosaccharide-alditols which were separated by high-performance liquid chromatography (HPLC) on an alkyl amine silicagel column.
3967649	1	4	theme	high-performance	365:380	arg1	chromatography					389:402	high-performance liquid chromatography	365:402	high-performance liquid chromatography (HPLC) on an alkyl amine silicagel column	365:444	Alkaline borohydride reductive cleavage (beta-elimination) of glycophorin A isolated from one individual of the rare blood group Cad, resulted in the release of six acidic oligosaccharide-alditols which were separated by high-performance liquid chromatography (HPLC) on an alkyl amine silicagel column.
3967649	4	5	theme	other	990:994	arg1	oligosaccharides					996:1011	The two other oligosaccharides	982:1011	The two other oligosaccharides (2 and 4)	982:1021	The two other oligosaccharides (2 and 4) were obtained in very low amount.
3967649	1	6	theme	alkyl	417:421	arg1	column					439:444	an alkyl amine silicagel column	414:444	an alkyl amine silicagel column	414:444	Alkaline borohydride reductive cleavage (beta-elimination) of glycophorin A isolated from one individual of the rare blood group Cad, resulted in the release of six acidic oligosaccharide-alditols which were separated by high-performance liquid chromatography (HPLC) on an alkyl amine silicagel column.
3967649	0	7	theme	500-MHz	115:121	arg1	spectroscopy					130:141	500-MHz 1H-NMR spectroscopy	115:141	500-MHz 1H-NMR spectroscopy	115:141	Structure determination of oligosaccharides isolated from Cad erythrocyte membranes by permethylation analysis and 500-MHz 1H-NMR spectroscopy.
3967649	1	8	theme	liquid	382:387	arg1	HPLC					405:408	HPLC	405:408	HPLC	405:408	Alkaline borohydride reductive cleavage (beta-elimination) of glycophorin A isolated from one individual of the rare blood group Cad, resulted in the release of six acidic oligosaccharide-alditols which were separated by high-performance liquid chromatography (HPLC) on an alkyl amine silicagel column.
3967649	1	8	theme	liquid	382:387	arg1	chromatography					389:402	high-performance liquid chromatography	365:402	high-performance liquid chromatography (HPLC) on an alkyl amine silicagel column	365:444	Alkaline borohydride reductive cleavage (beta-elimination) of glycophorin A isolated from one individual of the rare blood group Cad, resulted in the release of six acidic oligosaccharide-alditols which were separated by high-performance liquid chromatography (HPLC) on an alkyl amine silicagel column.
3967649	5	9	theme	blood	1115:1119	arg1	determinant					1131:1141	the blood group Cad determinant	1111:1141	the blood group Cad determinant	1111:1141	The major pentasaccharide (oligosaccharide 6) carries the blood group Cad determinant and is a potent inhibitor of human anti-Sda antibody.
3967649	3	10	dep	GalNAc-ol	860:868	arg1	[NeuAc					914:919	GalNAc(beta 1-4)[NeuAc	898:919	GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)	860:930	The structures and relative amounts were as follows: oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (71.2%).
3967649	3	10	dep	GalNAc-ol	860:868	arg1	2-3					927:929	alpha 2-3	921:929	alpha 2-3	921:929	The structures and relative amounts were as follows: oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (71.2%).
3967649	3	10	dep	GalNAc-ol	860:868	arg1	oligosaccharide					879:893	oligosaccharide 6	879:895	GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)	860:930	The structures and relative amounts were as follows: oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (71.2%).
3967649	2	11	theme	methylation	533:543	arg1	analysis					545:552	methylation analysis	533:552	methylation analysis	533:552	The structure of four of them has been determined by the application of methanolysis, methylation analysis and 1H-NMR spectroscopy at 500 MHz.
3967649	3	12	theme	Gal	678:680	arg1	GalNAc-ol					691:699	NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol	662:699	oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)	643:961	The structures and relative amounts were as follows: oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (71.2%).
3967649	3	12	theme	Gal	678:680	arg1	%					705:705	3.5%	702:705	3.5%	702:705	The structures and relative amounts were as follows: oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (71.2%).
3967649	5	13	theme	human	1172:1176	arg1	antibody					1187:1194	human anti-Sda antibody	1172:1194	human anti-Sda antibody	1172:1194	The major pentasaccharide (oligosaccharide 6) carries the blood group Cad determinant and is a potent inhibitor of human anti-Sda antibody.
3967649	5	14	theme	group	1121:1125	arg1	determinant					1131:1141	the blood group Cad determinant	1111:1141	the blood group Cad determinant	1111:1141	The major pentasaccharide (oligosaccharide 6) carries the blood group Cad determinant and is a potent inhibitor of human anti-Sda antibody.
3967649	3	15	theme	alpha	751:755	arg1	[NeuAc					744:749	GalNAc(beta 1-4)[NeuAc	728:749	oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)	643:961	The structures and relative amounts were as follows: oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (71.2%).
3967649	3	15	theme	alpha	751:755	arg1	2-3					757:759	alpha 2-3	751:759	alpha 2-3	751:759	The structures and relative amounts were as follows: oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (71.2%).
3967649	3	16	theme	GalNAc	728:733	arg1	[NeuAc					744:749	GalNAc(beta 1-4)[NeuAc	728:749	oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)	643:961	The structures and relative amounts were as follows: oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (71.2%).
3967649	3	16	theme	GalNAc	728:733	arg1	2-3					757:759	alpha 2-3	751:759	alpha 2-3	751:759	The structures and relative amounts were as follows: oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (71.2%).
3967649	3	17	theme	[NeuAc	842:847	arg1	beta					936:939	beta 1-3	936:943	beta 1-3	936:943	The structures and relative amounts were as follows: oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (71.2%).
3967649	3	17	theme	[NeuAc	842:847	arg1	Gal					932:934	NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal	813:934	oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)	643:961	The structures and relative amounts were as follows: oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (71.2%).
3967649	3	17	theme	[NeuAc	842:847	arg1	alpha					849:853	alpha 2-6	849:857	alpha 2-6	849:857	The structures and relative amounts were as follows: oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (71.2%).
3967649	0	18	theme	1H-NMR	123:128	arg1	spectroscopy					130:141	500-MHz 1H-NMR spectroscopy	115:141	500-MHz 1H-NMR spectroscopy	115:141	Structure determination of oligosaccharides isolated from Cad erythrocyte membranes by permethylation analysis and 500-MHz 1H-NMR spectroscopy.
3967649	3	19	theme	GalNAc	898:903	arg1	[NeuAc					914:919	GalNAc(beta 1-4)[NeuAc	898:919	GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)	860:930	The structures and relative amounts were as follows: oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (71.2%).
3967649	3	19	theme	GalNAc	898:903	arg1	2-3					927:929	alpha 2-3	921:929	alpha 2-3	921:929	The structures and relative amounts were as follows: oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (71.2%).
3967649	2	20	from	MHz	585:587	arg1	application					504:514	the application	500:514	the application of methanolysis, methylation analysis and 1H-NMR spectroscopy at 500 MHz	500:587	The structure of four of them has been determined by the application of methanolysis, methylation analysis and 1H-NMR spectroscopy at 500 MHz.
3967649	2	21	theme	four	464:467	arg1	structure					451:459	The structure	447:459	The structure of four of them	447:475	The structure of four of them has been determined by the application of methanolysis, methylation analysis and 1H-NMR spectroscopy at 500 MHz.
3967649	1	22	theme	glycophorin	206:216	arg1	A					218:218	glycophorin A	206:218	glycophorin A	206:218	Alkaline borohydride reductive cleavage (beta-elimination) of glycophorin A isolated from one individual of the rare blood group Cad, resulted in the release of six acidic oligosaccharide-alditols which were separated by high-performance liquid chromatography (HPLC) on an alkyl amine silicagel column.
3967649	3	23	dep	GalNAc-ol	963:971	arg1	GalNAc-ol					775:783	oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol	643:783	oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)	643:961	The structures and relative amounts were as follows: oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (71.2%).
3967649	3	23	dep	GalNAc-ol	963:971	arg1	%					790:790	10.5%	786:790	10.5%	786:790	The structures and relative amounts were as follows: oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (71.2%).
3967649	5	24	theme	antibody	1187:1194	arg1	inhibitor					1159:1167	a potent inhibitor	1150:1167	a potent inhibitor of human anti-Sda antibody	1150:1194	The major pentasaccharide (oligosaccharide 6) carries the blood group Cad determinant and is a potent inhibitor of human anti-Sda antibody.
3967649	1	25	theme	A	218:218	arg1	beta-elimination					185:200	Alkaline borohydride reductive cleavage (beta-elimination)	144:201	Alkaline borohydride reductive cleavage (beta-elimination)	144:201	Alkaline borohydride reductive cleavage (beta-elimination) of glycophorin A isolated from one individual of the rare blood group Cad, resulted in the release of six acidic oligosaccharide-alditols which were separated by high-performance liquid chromatography (HPLC) on an alkyl amine silicagel column.
3967649	0	26	theme	Structure	0:8	arg1	determination					10:22	Structure determination	0:22	Structure determination of oligosaccharides	0:42	Structure determination of oligosaccharides isolated from Cad erythrocyte membranes by permethylation analysis and 500-MHz 1H-NMR spectroscopy.
3967649	3	27	dep	GalNAc-ol	775:783	arg1	alpha					952:956	alpha 2-6	952:960	alpha 2-6	952:960	The structures and relative amounts were as follows: oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (71.2%).
3967649	3	27	dep	GalNAc-ol	775:783	arg1	[NeuAc					945:950	NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc	813:950	oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)	643:961	The structures and relative amounts were as follows: oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (71.2%).
3967649	3	27	dep	GalNAc-ol	775:783	arg1	oligosaccharide					794:808	oligosaccharide 5	794:810	oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)	643:961	The structures and relative amounts were as follows: oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (71.2%).
3967649	0	28	theme	oligosaccharides	27:42	arg1	determination					10:22	Structure determination	0:22	Structure determination of oligosaccharides	0:42	Structure determination of oligosaccharides isolated from Cad erythrocyte membranes by permethylation analysis and 500-MHz 1H-NMR spectroscopy.
3967649	5	29	theme	Cad	1127:1129	arg1	determinant					1131:1141	the blood group Cad determinant	1111:1141	the blood group Cad determinant	1111:1141	The major pentasaccharide (oligosaccharide 6) carries the blood group Cad determinant and is a potent inhibitor of human anti-Sda antibody.
3967649	4	30	theme	low	1045:1047	arg1	amount					1049:1054	very low amount	1040:1054	very low amount	1040:1054	The two other oligosaccharides (2 and 4) were obtained in very low amount.
3967649	3	31	theme	NeuAc	813:817	arg1	beta					936:939	beta 1-3	936:943	beta 1-3	936:943	The structures and relative amounts were as follows: oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (71.2%).
3967649	3	31	theme	NeuAc	813:817	arg1	Gal					932:934	NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal	813:934	oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)	643:961	The structures and relative amounts were as follows: oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (71.2%).
3967649	3	31	theme	NeuAc	813:817	arg1	alpha					849:853	alpha 2-6	849:857	alpha 2-6	849:857	The structures and relative amounts were as follows: oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (71.2%).
3967649	2	32	theme	analysis	545:552	arg1	application					504:514	the application	500:514	the application of methanolysis, methylation analysis and 1H-NMR spectroscopy at 500 MHz	500:587	The structure of four of them has been determined by the application of methanolysis, methylation analysis and 1H-NMR spectroscopy at 500 MHz.
3967649	2	33	theme	spectroscopy	565:576	arg1	application					504:514	the application	500:514	the application of methanolysis, methylation analysis and 1H-NMR spectroscopy at 500 MHz	500:587	The structure of four of them has been determined by the application of methanolysis, methylation analysis and 1H-NMR spectroscopy at 500 MHz.
3967649	3	34	theme	oligosaccharide	643:657	arg1	beta					766:769	beta 1-3	766:773	beta 1-3	766:773	The structures and relative amounts were as follows: oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (71.2%).
3967649	3	34	theme	oligosaccharide	643:657	arg1	Gal					762:764	oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal	643:764	oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)	643:961	The structures and relative amounts were as follows: oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (71.2%).
3967649	2	35	theme	1H-NMR	558:563	arg1	spectroscopy					565:576	1H-NMR spectroscopy	558:576	1H-NMR spectroscopy	558:576	The structure of four of them has been determined by the application of methanolysis, methylation analysis and 1H-NMR spectroscopy at 500 MHz.
3967649	3	36	theme	NeuAc	662:666	arg1	GalNAc-ol					691:699	NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol	662:699	oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)	643:961	The structures and relative amounts were as follows: oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (71.2%).
3967649	3	36	theme	NeuAc	662:666	arg1	%					705:705	3.5%	702:705	3.5%	702:705	The structures and relative amounts were as follows: oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (71.2%).
3967649	3	37	theme	relative	609:616	arg1	amounts					618:624	relative amounts	609:624	relative amounts	609:624	The structures and relative amounts were as follows: oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (71.2%).
3967649	3	38	dep	alpha	849:853	arg1	%					875:875	10.4%	871:875	10.4%	871:875	The structures and relative amounts were as follows: oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (71.2%).
3967649	3	38	dep	alpha	849:853	arg1	GalNAc-ol					860:868	GalNAc-ol	860:868	GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)	860:930	The structures and relative amounts were as follows: oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (71.2%).
3967649	1	39	theme	acidic	309:314	arg1	oligosaccharide-alditols					316:339	six acidic oligosaccharide-alditols	305:339	six acidic oligosaccharide-alditols which were separated by high-performance liquid chromatography (HPLC) on an alkyl amine silicagel column	305:444	Alkaline borohydride reductive cleavage (beta-elimination) of glycophorin A isolated from one individual of the rare blood group Cad, resulted in the release of six acidic oligosaccharide-alditols which were separated by high-performance liquid chromatography (HPLC) on an alkyl amine silicagel column.
3967649	1	40	attach	isolated	220:227	arg2	beta-elimination					185:200	Alkaline borohydride reductive cleavage (beta-elimination)	144:201	Alkaline borohydride reductive cleavage (beta-elimination)	144:201	Alkaline borohydride reductive cleavage (beta-elimination) of glycophorin A isolated from one individual of the rare blood group Cad, resulted in the release of six acidic oligosaccharide-alditols which were separated by high-performance liquid chromatography (HPLC) on an alkyl amine silicagel column.
3967649	1	40	attach	isolated	220:227	arg1	individual					238:247	one individual	234:247	one individual of the rare blood group Cad	234:275	Alkaline borohydride reductive cleavage (beta-elimination) of glycophorin A isolated from one individual of the rare blood group Cad, resulted in the release of six acidic oligosaccharide-alditols which were separated by high-performance liquid chromatography (HPLC) on an alkyl amine silicagel column.
3967649	1	41	from	chromatography	389:402	arg1	column					439:444	an alkyl amine silicagel column	414:444	an alkyl amine silicagel column	414:444	Alkaline borohydride reductive cleavage (beta-elimination) of glycophorin A isolated from one individual of the rare blood group Cad, resulted in the release of six acidic oligosaccharide-alditols which were separated by high-performance liquid chromatography (HPLC) on an alkyl amine silicagel column.
3967649	2	42	theme	methanolysis	519:530	arg1	application					504:514	the application	500:514	the application of methanolysis, methylation analysis and 1H-NMR spectroscopy at 500 MHz	500:587	The structure of four of them has been determined by the application of methanolysis, methylation analysis and 1H-NMR spectroscopy at 500 MHz.
3967649	0	43	theme	erythrocyte	62:72	arg1	membranes					74:82	Cad erythrocyte membranes	58:82	Cad erythrocyte membranes	58:82	Structure determination of oligosaccharides isolated from Cad erythrocyte membranes by permethylation analysis and 500-MHz 1H-NMR spectroscopy.
3967649	1	44	theme	oligosaccharide-alditols	316:339	arg1	release					294:300	the release	290:300	the release of six acidic oligosaccharide-alditols which were separated by high-performance liquid chromatography (HPLC) on an alkyl amine silicagel column	290:444	Alkaline borohydride reductive cleavage (beta-elimination) of glycophorin A isolated from one individual of the rare blood group Cad, resulted in the release of six acidic oligosaccharide-alditols which were separated by high-performance liquid chromatography (HPLC) on an alkyl amine silicagel column.
3967649	4	45	dep	oligosaccharides	996:1011	arg1	4					1020:1020	4	1020:1020	4	1020:1020	The two other oligosaccharides (2 and 4) were obtained in very low amount.
3967649	4	45	dep	oligosaccharides	996:1011	arg1	2					1014:1014	2	1014:1014	2	1014:1014	The two other oligosaccharides (2 and 4) were obtained in very low amount.
3967649	1	46	theme	amine	423:427	arg1	column					439:444	an alkyl amine silicagel column	414:444	an alkyl amine silicagel column	414:444	Alkaline borohydride reductive cleavage (beta-elimination) of glycophorin A isolated from one individual of the rare blood group Cad, resulted in the release of six acidic oligosaccharide-alditols which were separated by high-performance liquid chromatography (HPLC) on an alkyl amine silicagel column.
3967649	5	47	theme	major	1061:1065	arg1	oligosaccharide					1084:1098	oligosaccharide 6	1084:1100	oligosaccharide 6	1084:1100	The major pentasaccharide (oligosaccharide 6) carries the blood group Cad determinant and is a potent inhibitor of human anti-Sda antibody.
3967649	5	47	theme	major	1061:1065	arg1	pentasaccharide					1067:1081	The major pentasaccharide	1057:1081	The major pentasaccharide (oligosaccharide 6)	1057:1101	The major pentasaccharide (oligosaccharide 6) carries the blood group Cad determinant and is a potent inhibitor of human anti-Sda antibody.
3967649	0	48	theme	Cad	58:60	arg1	membranes					74:82	Cad erythrocyte membranes	58:82	Cad erythrocyte membranes	58:82	Structure determination of oligosaccharides isolated from Cad erythrocyte membranes by permethylation analysis and 500-MHz 1H-NMR spectroscopy.
3967649	3	49	theme	alpha	921:925	arg1	[NeuAc					914:919	GalNAc(beta 1-4)[NeuAc	898:919	GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)	860:930	The structures and relative amounts were as follows: oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (71.2%).
3967649	3	49	theme	alpha	921:925	arg1	2-3					927:929	alpha 2-3	921:929	alpha 2-3	921:929	The structures and relative amounts were as follows: oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (71.2%).
3967649	1	50	theme	silicagel	429:437	arg1	column					439:444	an alkyl amine silicagel column	414:444	an alkyl amine silicagel column	414:444	Alkaline borohydride reductive cleavage (beta-elimination) of glycophorin A isolated from one individual of the rare blood group Cad, resulted in the release of six acidic oligosaccharide-alditols which were separated by high-performance liquid chromatography (HPLC) on an alkyl amine silicagel column.
3967649	1	51	theme	Alkaline	144:151	arg1	beta-elimination					185:200	Alkaline borohydride reductive cleavage (beta-elimination)	144:201	Alkaline borohydride reductive cleavage (beta-elimination)	144:201	Alkaline borohydride reductive cleavage (beta-elimination) of glycophorin A isolated from one individual of the rare blood group Cad, resulted in the release of six acidic oligosaccharide-alditols which were separated by high-performance liquid chromatography (HPLC) on an alkyl amine silicagel column.
3967649	3	52	theme	alpha	819:823	arg1	beta					936:939	beta 1-3	936:943	beta 1-3	936:943	The structures and relative amounts were as follows: oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (71.2%).
3967649	3	52	theme	alpha	819:823	arg1	Gal					932:934	NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal	813:934	oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)	643:961	The structures and relative amounts were as follows: oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (71.2%).
3967649	3	52	theme	alpha	819:823	arg1	alpha					849:853	alpha 2-6	849:857	alpha 2-6	849:857	The structures and relative amounts were as follows: oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (71.2%).
3967649	1	53	theme	borohydride	153:163	arg1	beta-elimination					185:200	Alkaline borohydride reductive cleavage (beta-elimination)	144:201	Alkaline borohydride reductive cleavage (beta-elimination)	144:201	Alkaline borohydride reductive cleavage (beta-elimination) of glycophorin A isolated from one individual of the rare blood group Cad, resulted in the release of six acidic oligosaccharide-alditols which were separated by high-performance liquid chromatography (HPLC) on an alkyl amine silicagel column.
3967649	3	54	dep	oligosaccharide	643:657	arg1	GalNAc-ol					691:699	NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol	662:699	oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)	643:961	The structures and relative amounts were as follows: oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (71.2%).
3967649	3	54	dep	oligosaccharide	643:657	arg1	%					705:705	3.5%	702:705	3.5%	702:705	The structures and relative amounts were as follows: oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (71.2%).
3967649	3	54	dep	oligosaccharide	643:657	arg1	[NeuAc					744:749	GalNAc(beta 1-4)[NeuAc	728:749	oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)	643:961	The structures and relative amounts were as follows: oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (71.2%).
3967649	3	54	dep	oligosaccharide	643:657	arg1	2-3					757:759	alpha 2-3	751:759	alpha 2-3	751:759	The structures and relative amounts were as follows: oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (71.2%).
3967649	3	54	dep	oligosaccharide	643:657	arg1	oligosaccharide					709:723	oligosaccharide 3	709:725	oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)	643:961	The structures and relative amounts were as follows: oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (71.2%).
3967649	3	55	theme	beta	833:836	arg1	beta					936:939	beta 1-3	936:943	beta 1-3	936:943	The structures and relative amounts were as follows: oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (71.2%).
3967649	3	55	theme	beta	833:836	arg1	Gal					932:934	NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal	813:934	oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)	643:961	The structures and relative amounts were as follows: oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (71.2%).
3967649	3	55	theme	beta	833:836	arg1	alpha					849:853	alpha 2-6	849:857	alpha 2-6	849:857	The structures and relative amounts were as follows: oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (71.2%).
3967649	1	56	theme	reductive	165:173	arg1	beta-elimination					185:200	Alkaline borohydride reductive cleavage (beta-elimination)	144:201	Alkaline borohydride reductive cleavage (beta-elimination)	144:201	Alkaline borohydride reductive cleavage (beta-elimination) of glycophorin A isolated from one individual of the rare blood group Cad, resulted in the release of six acidic oligosaccharide-alditols which were separated by high-performance liquid chromatography (HPLC) on an alkyl amine silicagel column.
3967649	2	57	theme	them	472:475	arg1	four					464:467	four	464:467	four	464:467	The structure of four of them has been determined by the application of methanolysis, methylation analysis and 1H-NMR spectroscopy at 500 MHz.
3967649	2	57	theme	them	472:475	arg1	them					472:475	them	472:475	them	472:475	The structure of four of them has been determined by the application of methanolysis, methylation analysis and 1H-NMR spectroscopy at 500 MHz.
3967649	1	58	theme	rare	256:259	arg1	Cad					273:275	the rare blood group Cad	252:275	the rare blood group Cad	252:275	Alkaline borohydride reductive cleavage (beta-elimination) of glycophorin A isolated from one individual of the rare blood group Cad, resulted in the release of six acidic oligosaccharide-alditols which were separated by high-performance liquid chromatography (HPLC) on an alkyl amine silicagel column.
3967649	3	59	theme	alpha	668:672	arg1	GalNAc-ol					691:699	NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol	662:699	oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)	643:961	The structures and relative amounts were as follows: oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (71.2%).
3967649	3	59	theme	alpha	668:672	arg1	%					705:705	3.5%	702:705	3.5%	702:705	The structures and relative amounts were as follows: oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (71.2%).
3967649	5	60	contain	carries	1103:1109	arg2	determinant					1131:1141	the blood group Cad determinant	1111:1141	the blood group Cad determinant	1111:1141	The major pentasaccharide (oligosaccharide 6) carries the blood group Cad determinant and is a potent inhibitor of human anti-Sda antibody.
3967649	5	60	contain	carries	1103:1109	arg1	oligosaccharide					1084:1098	oligosaccharide 6	1084:1100	oligosaccharide 6	1084:1100	The major pentasaccharide (oligosaccharide 6) carries the blood group Cad determinant and is a potent inhibitor of human anti-Sda antibody.
3967649	5	60	contain	carries	1103:1109	arg1	pentasaccharide					1067:1081	The major pentasaccharide	1057:1081	The major pentasaccharide (oligosaccharide 6)	1057:1101	The major pentasaccharide (oligosaccharide 6) carries the blood group Cad determinant and is a potent inhibitor of human anti-Sda antibody.
3967649	1	61	theme	cleavage	175:182	arg1	beta-elimination					185:200	Alkaline borohydride reductive cleavage (beta-elimination)	144:201	Alkaline borohydride reductive cleavage (beta-elimination)	144:201	Alkaline borohydride reductive cleavage (beta-elimination) of glycophorin A isolated from one individual of the rare blood group Cad, resulted in the release of six acidic oligosaccharide-alditols which were separated by high-performance liquid chromatography (HPLC) on an alkyl amine silicagel column.
3967649	3	62	theme	Gal	762:764	arg1	GalNAc-ol					775:783	oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol	643:783	oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)	643:961	The structures and relative amounts were as follows: oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (71.2%).
3967649	3	62	theme	Gal	762:764	arg1	%					790:790	10.5%	786:790	10.5%	786:790	The structures and relative amounts were as follows: oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (71.2%).
3967649	1	63	theme	blood	261:265	arg1	Cad					273:275	the rare blood group Cad	252:275	the rare blood group Cad	252:275	Alkaline borohydride reductive cleavage (beta-elimination) of glycophorin A isolated from one individual of the rare blood group Cad, resulted in the release of six acidic oligosaccharide-alditols which were separated by high-performance liquid chromatography (HPLC) on an alkyl amine silicagel column.
3967649	3	64	theme	Gal	932:934	arg1	alpha					952:956	alpha 2-6	952:960	alpha 2-6	952:960	The structures and relative amounts were as follows: oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (71.2%).
3967649	3	64	theme	Gal	932:934	arg1	[NeuAc					945:950	NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc	813:950	oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)	643:961	The structures and relative amounts were as follows: oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (71.2%).
3967649	3	65	theme	beta	682:685	arg1	GalNAc-ol					691:699	NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol	662:699	oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)	643:961	The structures and relative amounts were as follows: oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (71.2%).
3967649	3	65	theme	beta	682:685	arg1	%					705:705	3.5%	702:705	3.5%	702:705	The structures and relative amounts were as follows: oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (71.2%).
3967649	3	66	theme	Gal	829:831	arg1	beta					936:939	beta 1-3	936:943	beta 1-3	936:943	The structures and relative amounts were as follows: oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (71.2%).
3967649	3	66	theme	Gal	829:831	arg1	Gal					932:934	NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal	813:934	oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)	643:961	The structures and relative amounts were as follows: oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (71.2%).
3967649	3	66	theme	Gal	829:831	arg1	alpha					849:853	alpha 2-6	849:857	alpha 2-6	849:857	The structures and relative amounts were as follows: oligosaccharide 1: NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol (3.5%); oligosaccharide 3: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)GalNAc-ol (10.5%); oligosaccharide 5: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (10.4%); oligosaccharide 6: GalNAc(beta 1-4)[NeuAc(alpha 2-3)]Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol (71.2%).
3967649	1	67	theme	group	267:271	arg1	Cad					273:275	the rare blood group Cad	252:275	the rare blood group Cad	252:275	Alkaline borohydride reductive cleavage (beta-elimination) of glycophorin A isolated from one individual of the rare blood group Cad, resulted in the release of six acidic oligosaccharide-alditols which were separated by high-performance liquid chromatography (HPLC) on an alkyl amine silicagel column.
6190803	4	0	theme	blood	506:510	arg1	Cad-negative					521:532	Cad-negative	521:532	Cad-negative	521:532	Lipid-free glycophorin A, purified from Cad red cells, showed an increased GalNAc content in comparison to blood group B, Cad-negative, control cells.
6190803	4	0	theme	blood	506:510	arg1	cells					543:547	control cells	535:547	control cells	535:547	Lipid-free glycophorin A, purified from Cad red cells, showed an increased GalNAc content in comparison to blood group B, Cad-negative, control cells.
6190803	4	0	theme	blood	506:510	arg1	B					518:518	blood group B	506:518	blood group B	506:518	Lipid-free glycophorin A, purified from Cad red cells, showed an increased GalNAc content in comparison to blood group B, Cad-negative, control cells.
6190803	0	1	theme	specificity	72:82	arg1	determinant					41:51	the oligosaccharide determinant	21:51	the oligosaccharide determinant of blood group Cad specificity	21:82	Primary structure of the oligosaccharide determinant of blood group Cad specificity.
6190803	2	2	from	erythrocytes	317:328	arg1	glycophorins					291:302	the corresponding glycophorins	273:302	the corresponding glycophorins from control erythrocytes	273:328	They are characterized by a significant increase in molecular mass, as compared to the corresponding glycophorins from control erythrocytes (Cartron, J.-P., and Blanchard, D. (1982) Biochem.
6190803	2	3	dep	compared	261:268	arg1	D					362:362	D	362:362	D	362:362	They are characterized by a significant increase in molecular mass, as compared to the corresponding glycophorins from control erythrocytes (Cartron, J.-P., and Blanchard, D. (1982) Biochem.
6190803	2	3	dep	compared	261:268	arg1	J.-P.					340:344	J.-P.	340:344	J.-P.	340:344	They are characterized by a significant increase in molecular mass, as compared to the corresponding glycophorins from control erythrocytes (Cartron, J.-P., and Blanchard, D. (1982) Biochem.
6190803	2	3	dep	compared	261:268	arg1	Blanchard					351:359	Blanchard	351:359	Blanchard	351:359	They are characterized by a significant increase in molecular mass, as compared to the corresponding glycophorins from control erythrocytes (Cartron, J.-P., and Blanchard, D. (1982) Biochem.
6190803	2	3	dep	compared	261:268	arg1	Cartron					331:337	Cartron	331:337	Cartron	331:337	They are characterized by a significant increase in molecular mass, as compared to the corresponding glycophorins from control erythrocytes (Cartron, J.-P., and Blanchard, D. (1982) Biochem.
6190803	4	4	theme	red	443:445	arg1	cells					447:451	Cad red cells	439:451	Cad red cells	439:451	Lipid-free glycophorin A, purified from Cad red cells, showed an increased GalNAc content in comparison to blood group B, Cad-negative, control cells.
6190803	5	5	theme	Cad	589:591	arg1	A					605:605	this Cad glycophorin A	584:605	this Cad glycophorin A	584:605	Alkaline-borohydride treatment of this Cad glycophorin A released as a predominant species a pentasaccharide; its structure was determined, by methylation analysis and by 500-MHz 1H-NMR studies, to be: (formula; see text) This novel oligosaccharide inhibited strongly the hemagglutination of Cad erythrocytes by the Dolichos biflorus lectin.
6190803	5	6	theme	Dolichos	866:873	arg1	lectin					884:889	the Dolichos biflorus lectin	862:889	the Dolichos biflorus lectin	862:889	Alkaline-borohydride treatment of this Cad glycophorin A released as a predominant species a pentasaccharide; its structure was determined, by methylation analysis and by 500-MHz 1H-NMR studies, to be: (formula; see text) This novel oligosaccharide inhibited strongly the hemagglutination of Cad erythrocytes by the Dolichos biflorus lectin.
6190803	5	7	theme	Cad	842:844	arg1	erythrocytes					846:857	Cad erythrocytes	842:857	Cad erythrocytes	842:857	Alkaline-borohydride treatment of this Cad glycophorin A released as a predominant species a pentasaccharide; its structure was determined, by methylation analysis and by 500-MHz 1H-NMR studies, to be: (formula; see text) This novel oligosaccharide inhibited strongly the hemagglutination of Cad erythrocytes by the Dolichos biflorus lectin.
6190803	5	8	theme	glycophorin	593:603	arg1	A					605:605	this Cad glycophorin A	584:605	this Cad glycophorin A	584:605	Alkaline-borohydride treatment of this Cad glycophorin A released as a predominant species a pentasaccharide; its structure was determined, by methylation analysis and by 500-MHz 1H-NMR studies, to be: (formula; see text) This novel oligosaccharide inhibited strongly the hemagglutination of Cad erythrocytes by the Dolichos biflorus lectin.
6190803	4	9	theme	group	512:516	arg1	Cad-negative					521:532	Cad-negative	521:532	Cad-negative	521:532	Lipid-free glycophorin A, purified from Cad red cells, showed an increased GalNAc content in comparison to blood group B, Cad-negative, control cells.
6190803	4	9	theme	group	512:516	arg1	cells					543:547	control cells	535:547	control cells	535:547	Lipid-free glycophorin A, purified from Cad red cells, showed an increased GalNAc content in comparison to blood group B, Cad-negative, control cells.
6190803	4	9	theme	group	512:516	arg1	B					518:518	blood group B	506:518	blood group B	506:518	Lipid-free glycophorin A, purified from Cad red cells, showed an increased GalNAc content in comparison to blood group B, Cad-negative, control cells.
6190803	4	10	theme	glycophorin	410:420	arg1	A					422:422	Lipid-free glycophorin A	399:422	Lipid-free glycophorin A	399:422	Lipid-free glycophorin A, purified from Cad red cells, showed an increased GalNAc content in comparison to blood group B, Cad-negative, control cells.
6190803	6	11	theme	Sda	923:925	arg1	determinant					927:937	the blood group Sda determinant	907:937	the blood group Sda determinant	907:937	It shares with the blood group Sda determinant a terminal GalNAc beta (1 leads to 4)Gal beta (1 leads to .)
6190803	1	12	theme	blood	160:164	arg1	determinants					176:187	the blood group Cad determinants	156:187	the blood group Cad determinants	156:187	Glycophorin A and B from Cad erythrocyte membranes are the carriers of the blood group Cad determinants.
6190803	5	13	theme	1H-NMR	729:734	arg1	studies					736:742	500-MHz 1H-NMR studies	721:742	500-MHz 1H-NMR studies	721:742	Alkaline-borohydride treatment of this Cad glycophorin A released as a predominant species a pentasaccharide; its structure was determined, by methylation analysis and by 500-MHz 1H-NMR studies, to be: (formula; see text) This novel oligosaccharide inhibited strongly the hemagglutination of Cad erythrocytes by the Dolichos biflorus lectin.
6190803	5	14	theme	methylation	693:703	arg1	analysis					705:712	methylation analysis	693:712	methylation analysis	693:712	Alkaline-borohydride treatment of this Cad glycophorin A released as a predominant species a pentasaccharide; its structure was determined, by methylation analysis and by 500-MHz 1H-NMR studies, to be: (formula; see text) This novel oligosaccharide inhibited strongly the hemagglutination of Cad erythrocytes by the Dolichos biflorus lectin.
6190803	5	15	theme	Alkaline-borohydride	550:569	arg1	treatment					571:579	Alkaline-borohydride treatment	550:579	Alkaline-borohydride treatment of this Cad glycophorin A	550:605	Alkaline-borohydride treatment of this Cad glycophorin A released as a predominant species a pentasaccharide; its structure was determined, by methylation analysis and by 500-MHz 1H-NMR studies, to be: (formula; see text) This novel oligosaccharide inhibited strongly the hemagglutination of Cad erythrocytes by the Dolichos biflorus lectin.
6190803	1	16	from	membranes	126:134	arg1	A					97:97	Glycophorin A	85:97	Glycophorin A	85:97	Glycophorin A and B from Cad erythrocyte membranes are the carriers of the blood group Cad determinants.
6190803	1	16	from	membranes	126:134	arg1	carriers					144:151	the carriers	140:151	the carriers of the blood group Cad determinants	140:187	Glycophorin A and B from Cad erythrocyte membranes are the carriers of the blood group Cad determinants.
6190803	1	16	from	membranes	126:134	arg1	B					103:103	B	103:103	B	103:103	Glycophorin A and B from Cad erythrocyte membranes are the carriers of the blood group Cad determinants.
6190803	1	17	theme	Glycophorin	85:95	arg1	A					97:97	Glycophorin A	85:97	Glycophorin A	85:97	Glycophorin A and B from Cad erythrocyte membranes are the carriers of the blood group Cad determinants.
6190803	1	17	theme	Glycophorin	85:95	arg1	carriers					144:151	the carriers	140:151	the carriers of the blood group Cad determinants	140:187	Glycophorin A and B from Cad erythrocyte membranes are the carriers of the blood group Cad determinants.
6190803	1	17	theme	Glycophorin	85:95	arg1	B					103:103	B	103:103	B	103:103	Glycophorin A and B from Cad erythrocyte membranes are the carriers of the blood group Cad determinants.
6190803	1	18	theme	group	166:170	arg1	determinants					176:187	the blood group Cad determinants	156:187	the blood group Cad determinants	156:187	Glycophorin A and B from Cad erythrocyte membranes are the carriers of the blood group Cad determinants.
6190803	0	19	theme	Primary	0:6	arg1	structure					8:16	Primary structure	0:16	Primary structure of the oligosaccharide determinant of blood group Cad specificity	0:82	Primary structure of the oligosaccharide determinant of blood group Cad specificity.
6190803	5	20	theme	erythrocytes	846:857	arg1	hemagglutination					822:837	the hemagglutination	818:837	the hemagglutination of Cad erythrocytes by the Dolichos biflorus lectin	818:889	Alkaline-borohydride treatment of this Cad glycophorin A released as a predominant species a pentasaccharide; its structure was determined, by methylation analysis and by 500-MHz 1H-NMR studies, to be: (formula; see text) This novel oligosaccharide inhibited strongly the hemagglutination of Cad erythrocytes by the Dolichos biflorus lectin.
6190803	1	21	theme	Cad	172:174	arg1	determinants					176:187	the blood group Cad determinants	156:187	the blood group Cad determinants	156:187	Glycophorin A and B from Cad erythrocyte membranes are the carriers of the blood group Cad determinants.
6190803	4	22	from	content	481:487	arg1	comparison					492:501	comparison	492:501	comparison to blood group B, Cad-negative, control cells	492:547	Lipid-free glycophorin A, purified from Cad red cells, showed an increased GalNAc content in comparison to blood group B, Cad-negative, control cells.
6190803	4	23	theme	GalNAc	474:479	arg1	content					481:487	an increased GalNAc content	461:487	an increased GalNAc content in comparison to blood group B, Cad-negative, control cells	461:547	Lipid-free glycophorin A, purified from Cad red cells, showed an increased GalNAc content in comparison to blood group B, Cad-negative, control cells.
6190803	5	24	theme	predominant	621:631	arg1	species					633:639	a predominant species	619:639	a predominant species	619:639	Alkaline-borohydride treatment of this Cad glycophorin A released as a predominant species a pentasaccharide; its structure was determined, by methylation analysis and by 500-MHz 1H-NMR studies, to be: (formula; see text) This novel oligosaccharide inhibited strongly the hemagglutination of Cad erythrocytes by the Dolichos biflorus lectin.
6190803	5	24	theme	predominant	621:631	arg1	pentasaccharide					643:657	a pentasaccharide	641:657	a pentasaccharide	641:657	Alkaline-borohydride treatment of this Cad glycophorin A released as a predominant species a pentasaccharide; its structure was determined, by methylation analysis and by 500-MHz 1H-NMR studies, to be: (formula; see text) This novel oligosaccharide inhibited strongly the hemagglutination of Cad erythrocytes by the Dolichos biflorus lectin.
6190803	2	25	theme	corresponding	277:289	arg1	glycophorins					291:302	the corresponding glycophorins	273:302	the corresponding glycophorins from control erythrocytes	273:328	They are characterized by a significant increase in molecular mass, as compared to the corresponding glycophorins from control erythrocytes (Cartron, J.-P., and Blanchard, D. (1982) Biochem.
6190803	2	26	from	increase	230:237	arg1	mass					252:255	molecular mass	242:255	molecular mass	242:255	They are characterized by a significant increase in molecular mass, as compared to the corresponding glycophorins from control erythrocytes (Cartron, J.-P., and Blanchard, D. (1982) Biochem.
6190803	1	27	theme	determinants	176:187	arg1	A					97:97	Glycophorin A	85:97	Glycophorin A	85:97	Glycophorin A and B from Cad erythrocyte membranes are the carriers of the blood group Cad determinants.
6190803	1	27	theme	determinants	176:187	arg1	carriers					144:151	the carriers	140:151	the carriers of the blood group Cad determinants	140:187	Glycophorin A and B from Cad erythrocyte membranes are the carriers of the blood group Cad determinants.
6190803	1	27	theme	determinants	176:187	arg1	B					103:103	B	103:103	B	103:103	Glycophorin A and B from Cad erythrocyte membranes are the carriers of the blood group Cad determinants.
6190803	5	28	dep	oligosaccharide	783:797	arg1	see					762:764	see	762:764	see text	762:769	Alkaline-borohydride treatment of this Cad glycophorin A released as a predominant species a pentasaccharide; its structure was determined, by methylation analysis and by 500-MHz 1H-NMR studies, to be: (formula; see text) This novel oligosaccharide inhibited strongly the hemagglutination of Cad erythrocytes by the Dolichos biflorus lectin.
6190803	6	29	theme	GalNAc	950:955	arg1	beta					957:960	a terminal GalNAc beta	939:960	a terminal GalNAc beta (1	939:963	It shares with the blood group Sda determinant a terminal GalNAc beta (1 leads to 4)Gal beta (1 leads to .)
6190803	0	30	theme	determinant	41:51	arg1	structure					8:16	Primary structure	0:16	Primary structure of the oligosaccharide determinant of blood group Cad specificity	0:82	Primary structure of the oligosaccharide determinant of blood group Cad specificity.
6190803	2	31	theme	significant	218:228	arg1	increase					230:237	a significant increase	216:237	a significant increase in molecular mass	216:255	They are characterized by a significant increase in molecular mass, as compared to the corresponding glycophorins from control erythrocytes (Cartron, J.-P., and Blanchard, D. (1982) Biochem.
6190803	6	32	theme	terminal	941:948	arg1	beta					957:960	a terminal GalNAc beta	939:960	a terminal GalNAc beta (1	939:963	It shares with the blood group Sda determinant a terminal GalNAc beta (1 leads to 4)Gal beta (1 leads to .)
6190803	0	33	theme	oligosaccharide	25:39	arg1	determinant					41:51	the oligosaccharide determinant	21:51	the oligosaccharide determinant of blood group Cad specificity	21:82	Primary structure of the oligosaccharide determinant of blood group Cad specificity.
6190803	4	34	theme	Lipid-free	399:408	arg1	A					422:422	Lipid-free glycophorin A	399:422	Lipid-free glycophorin A	399:422	Lipid-free glycophorin A, purified from Cad red cells, showed an increased GalNAc content in comparison to blood group B, Cad-negative, control cells.
6190803	6	35	theme	group	917:921	arg1	determinant					927:937	the blood group Sda determinant	907:937	the blood group Sda determinant	907:937	It shares with the blood group Sda determinant a terminal GalNAc beta (1 leads to 4)Gal beta (1 leads to .)
6190803	0	36	theme	blood	56:60	arg1	specificity					72:82	blood group Cad specificity	56:82	blood group Cad specificity	56:82	Primary structure of the oligosaccharide determinant of blood group Cad specificity.
6190803	5	37	theme	A	605:605	arg1	treatment					571:579	Alkaline-borohydride treatment	550:579	Alkaline-borohydride treatment of this Cad glycophorin A	550:605	Alkaline-borohydride treatment of this Cad glycophorin A released as a predominant species a pentasaccharide; its structure was determined, by methylation analysis and by 500-MHz 1H-NMR studies, to be: (formula; see text) This novel oligosaccharide inhibited strongly the hemagglutination of Cad erythrocytes by the Dolichos biflorus lectin.
6190803	6	38	dep	beta	980:983	arg1	4					974:974	4	974:974	4	974:974	It shares with the blood group Sda determinant a terminal GalNAc beta (1 leads to 4)Gal beta (1 leads to .)
6190803	6	38	dep	beta	980:983	arg1	leads					988:992	leads	988:992	leads to	988:995	It shares with the blood group Sda determinant a terminal GalNAc beta (1 leads to 4)Gal beta (1 leads to .)
6190803	5	39	theme	500-MHz	721:727	arg1	studies					736:742	500-MHz 1H-NMR studies	721:742	500-MHz 1H-NMR studies	721:742	Alkaline-borohydride treatment of this Cad glycophorin A released as a predominant species a pentasaccharide; its structure was determined, by methylation analysis and by 500-MHz 1H-NMR studies, to be: (formula; see text) This novel oligosaccharide inhibited strongly the hemagglutination of Cad erythrocytes by the Dolichos biflorus lectin.
6190803	4	40	theme	increased	464:472	arg1	content					481:487	an increased GalNAc content	461:487	an increased GalNAc content in comparison to blood group B, Cad-negative, control cells	461:547	Lipid-free glycophorin A, purified from Cad red cells, showed an increased GalNAc content in comparison to blood group B, Cad-negative, control cells.
6190803	5	41	dep	see	762:764	arg1	formula					753:759	formula	753:759	formula	753:759	Alkaline-borohydride treatment of this Cad glycophorin A released as a predominant species a pentasaccharide; its structure was determined, by methylation analysis and by 500-MHz 1H-NMR studies, to be: (formula; see text) This novel oligosaccharide inhibited strongly the hemagglutination of Cad erythrocytes by the Dolichos biflorus lectin.
6190803	1	42	theme	Cad	110:112	arg1	membranes					126:134	Cad erythrocyte membranes	110:134	Cad erythrocyte membranes	110:134	Glycophorin A and B from Cad erythrocyte membranes are the carriers of the blood group Cad determinants.
6190803	1	43	theme	erythrocyte	114:124	arg1	membranes					126:134	Cad erythrocyte membranes	110:134	Cad erythrocyte membranes	110:134	Glycophorin A and B from Cad erythrocyte membranes are the carriers of the blood group Cad determinants.
6190803	2	44	dep	Cartron	331:337	arg1	Biochem					372:378	Biochem	372:378	Cartron, J.-P., and Blanchard, D. (1982) Biochem	331:378	They are characterized by a significant increase in molecular mass, as compared to the corresponding glycophorins from control erythrocytes (Cartron, J.-P., and Blanchard, D. (1982) Biochem.
6190803	2	45	theme	molecular	242:250	arg1	mass					252:255	molecular mass	242:255	molecular mass	242:255	They are characterized by a significant increase in molecular mass, as compared to the corresponding glycophorins from control erythrocytes (Cartron, J.-P., and Blanchard, D. (1982) Biochem.
6190803	2	46	theme	control	309:315	arg1	erythrocytes					317:328	control erythrocytes	309:328	control erythrocytes	309:328	They are characterized by a significant increase in molecular mass, as compared to the corresponding glycophorins from control erythrocytes (Cartron, J.-P., and Blanchard, D. (1982) Biochem.
6190803	5	47	dep	Dolichos	866:873	arg1	biflorus					875:882	biflorus	875:882	biflorus	875:882	Alkaline-borohydride treatment of this Cad glycophorin A released as a predominant species a pentasaccharide; its structure was determined, by methylation analysis and by 500-MHz 1H-NMR studies, to be: (formula; see text) This novel oligosaccharide inhibited strongly the hemagglutination of Cad erythrocytes by the Dolichos biflorus lectin.
6190803	0	48	theme	Cad	68:70	arg1	specificity					72:82	blood group Cad specificity	56:82	blood group Cad specificity	56:82	Primary structure of the oligosaccharide determinant of blood group Cad specificity.
6190803	6	49	theme	Gal	976:978	arg1	beta					980:983	4)Gal beta	974:983	4)Gal beta (1 leads to .)	974:998	It shares with the blood group Sda determinant a terminal GalNAc beta (1 leads to 4)Gal beta (1 leads to .)
6190803	4	50	theme	control	535:541	arg1	cells					543:547	control cells	535:547	control cells	535:547	Lipid-free glycophorin A, purified from Cad red cells, showed an increased GalNAc content in comparison to blood group B, Cad-negative, control cells.
6190803	4	50	theme	control	535:541	arg1	B					518:518	blood group B	506:518	blood group B	506:518	Lipid-free glycophorin A, purified from Cad red cells, showed an increased GalNAc content in comparison to blood group B, Cad-negative, control cells.
6190803	0	51	theme	group	62:66	arg1	specificity					72:82	blood group Cad specificity	56:82	blood group Cad specificity	56:82	Primary structure of the oligosaccharide determinant of blood group Cad specificity.
6190803	4	52	theme	Cad	439:441	arg1	cells					447:451	Cad red cells	439:451	Cad red cells	439:451	Lipid-free glycophorin A, purified from Cad red cells, showed an increased GalNAc content in comparison to blood group B, Cad-negative, control cells.
6190803	5	53	theme	novel	777:781	arg1	oligosaccharide					783:797	This novel oligosaccharide	772:797	(formula; see text) This novel oligosaccharide	752:797	Alkaline-borohydride treatment of this Cad glycophorin A released as a predominant species a pentasaccharide; its structure was determined, by methylation analysis and by 500-MHz 1H-NMR studies, to be: (formula; see text) This novel oligosaccharide inhibited strongly the hemagglutination of Cad erythrocytes by the Dolichos biflorus lectin.
6190803	6	54	theme	blood	911:915	arg1	determinant					927:937	the blood group Sda determinant	907:937	the blood group Sda determinant	907:937	It shares with the blood group Sda determinant a terminal GalNAc beta (1 leads to 4)Gal beta (1 leads to .)
8460945	2	0	theme	sugar	481:485	arg1	chains					487:492	mucin-type sugar chains	470:492	mucin-type sugar chains	470:492	In this study, we purified urinary human erythropoietin from three independent groups of aplastic anemia patients, and analyzed the structures of mucin-type sugar chains as well as that obtained from recombinant human erythropoietin produced by Chinese hamster ovary cells.
8460945	4	1	theme	recombinant	888:898	arg1	erythropoietin					906:919	recombinant human erythropoietin	888:919	recombinant human erythropoietin	888:919	All of the three independent samples of urinary erythropoietin contained oligosaccharides with the structures of +/- Neu5Ac alpha 2-->6GalNAc, while recombinant human erythropoietin contained those with the structures of Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc, Neu5Ac alpha 2-->3Gal beta 1-->3GalNAc, and Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc.
8460945	2	2	theme	mucin-type	470:479	arg1	chains					487:492	mucin-type sugar chains	470:492	mucin-type sugar chains	470:492	In this study, we purified urinary human erythropoietin from three independent groups of aplastic anemia patients, and analyzed the structures of mucin-type sugar chains as well as that obtained from recombinant human erythropoietin produced by Chinese hamster ovary cells.
8460945	4	3	theme	human	900:904	arg1	erythropoietin					906:919	recombinant human erythropoietin	888:919	recombinant human erythropoietin	888:919	All of the three independent samples of urinary erythropoietin contained oligosaccharides with the structures of +/- Neu5Ac alpha 2-->6GalNAc, while recombinant human erythropoietin contained those with the structures of Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc, Neu5Ac alpha 2-->3Gal beta 1-->3GalNAc, and Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc.
8460945	4	4	theme	1-->3	1073:1077	arg1	GalNAc					1098:1103	Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc	1064:1103	Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc	1064:1103	All of the three independent samples of urinary erythropoietin contained oligosaccharides with the structures of +/- Neu5Ac alpha 2-->6GalNAc, while recombinant human erythropoietin contained those with the structures of Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc, Neu5Ac alpha 2-->3Gal beta 1-->3GalNAc, and Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc.
8460945	4	4	theme	1-->3	1073:1077	arg1	2-->6					1092:1096	Neu5Ac alpha 2-->6	1079:1096	Neu5Ac alpha 2-->6	1079:1096	All of the three independent samples of urinary erythropoietin contained oligosaccharides with the structures of +/- Neu5Ac alpha 2-->6GalNAc, while recombinant human erythropoietin contained those with the structures of Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc, Neu5Ac alpha 2-->3Gal beta 1-->3GalNAc, and Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc.
8460945	1	5	theme	N-linked	248:255	arg1	chains					263:268	N-linked sugar chains	248:268	N-linked sugar chains which structures and function have been well studied	248:321	Less is known about the mucin-type sugar chains attached to human erythropoietin as compared with N-linked sugar chains which structures and function have been well studied.
8460945	0	6	theme	culture	91:97	arg1	medium					99:104	the culture medium	87:104	the culture medium of recombinant Chinese hamster ovary cells	87:147	Structures of mucin-type sugar chains on human erythropoietins purified from urine and the culture medium of recombinant Chinese hamster ovary cells.
8460945	0	7	from	Structures	0:9	arg1	erythropoietins					47:61	human erythropoietins	41:61	human erythropoietins	41:61	Structures of mucin-type sugar chains on human erythropoietins purified from urine and the culture medium of recombinant Chinese hamster ovary cells.
8460945	4	8	theme	beta	1068:1071	arg1	GalNAc					1098:1103	Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc	1064:1103	Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc	1064:1103	All of the three independent samples of urinary erythropoietin contained oligosaccharides with the structures of +/- Neu5Ac alpha 2-->6GalNAc, while recombinant human erythropoietin contained those with the structures of Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc, Neu5Ac alpha 2-->3Gal beta 1-->3GalNAc, and Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc.
8460945	4	8	theme	beta	1068:1071	arg1	2-->6					1092:1096	Neu5Ac alpha 2-->6	1079:1096	Neu5Ac alpha 2-->6	1079:1096	All of the three independent samples of urinary erythropoietin contained oligosaccharides with the structures of +/- Neu5Ac alpha 2-->6GalNAc, while recombinant human erythropoietin contained those with the structures of Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc, Neu5Ac alpha 2-->3Gal beta 1-->3GalNAc, and Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc.
8460945	1	9	theme	sugar	257:261	arg1	chains					263:268	N-linked sugar chains	248:268	N-linked sugar chains which structures and function have been well studied	248:321	Less is known about the mucin-type sugar chains attached to human erythropoietin as compared with N-linked sugar chains which structures and function have been well studied.
8460945	4	10	theme	2-->3Gal	973:980	arg1	2-->6					1006:1010	Neu5Ac alpha 2-->6	993:1010	Neu5Ac alpha 2-->6	993:1010	All of the three independent samples of urinary erythropoietin contained oligosaccharides with the structures of +/- Neu5Ac alpha 2-->6GalNAc, while recombinant human erythropoietin contained those with the structures of Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc, Neu5Ac alpha 2-->3Gal beta 1-->3GalNAc, and Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc.
8460945	4	10	theme	2-->3Gal	973:980	arg1	beta					982:985	Neu5Ac alpha 2-->3Gal beta 1-->3	960:991	Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc	960:1017	All of the three independent samples of urinary erythropoietin contained oligosaccharides with the structures of +/- Neu5Ac alpha 2-->6GalNAc, while recombinant human erythropoietin contained those with the structures of Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc, Neu5Ac alpha 2-->3Gal beta 1-->3GalNAc, and Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc.
8460945	2	11	theme	ovary	585:589	arg1	cells					591:595	Chinese hamster ovary cells	569:595	Chinese hamster ovary cells	569:595	In this study, we purified urinary human erythropoietin from three independent groups of aplastic anemia patients, and analyzed the structures of mucin-type sugar chains as well as that obtained from recombinant human erythropoietin produced by Chinese hamster ovary cells.
8460945	4	12	with	oligosaccharides	812:827	arg1	structures					838:847	the structures	834:847	the structures of +/- Neu5Ac alpha 2-->6GalNAc	834:879	All of the three independent samples of urinary erythropoietin contained oligosaccharides with the structures of +/- Neu5Ac alpha 2-->6GalNAc, while recombinant human erythropoietin contained those with the structures of Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc, Neu5Ac alpha 2-->3Gal beta 1-->3GalNAc, and Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc.
8460945	4	13	theme	independent	756:766	arg1	samples					768:774	the three independent samples	746:774	the three independent samples of urinary erythropoietin	746:800	All of the three independent samples of urinary erythropoietin contained oligosaccharides with the structures of +/- Neu5Ac alpha 2-->6GalNAc, while recombinant human erythropoietin contained those with the structures of Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc, Neu5Ac alpha 2-->3Gal beta 1-->3GalNAc, and Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc.
8460945	4	14	theme	GalNAc	1012:1017	arg1	structures					946:955	the structures	942:955	the structures of Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc, Neu5Ac alpha 2-->3Gal beta 1-->3GalNAc, and Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc	942:1103	All of the three independent samples of urinary erythropoietin contained oligosaccharides with the structures of +/- Neu5Ac alpha 2-->6GalNAc, while recombinant human erythropoietin contained those with the structures of Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc, Neu5Ac alpha 2-->3Gal beta 1-->3GalNAc, and Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc.
8460945	4	15	theme	2-->3Gal	1033:1040	arg1	beta					1042:1045	Neu5Ac alpha 2-->3Gal beta	1020:1045	Neu5Ac alpha 2-->3Gal beta 1-->3GalNAc	1020:1057	All of the three independent samples of urinary erythropoietin contained oligosaccharides with the structures of +/- Neu5Ac alpha 2-->6GalNAc, while recombinant human erythropoietin contained those with the structures of Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc, Neu5Ac alpha 2-->3Gal beta 1-->3GalNAc, and Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc.
8460945	2	16	theme	human	536:540	arg1	erythropoietin					542:555	recombinant human erythropoietin	524:555	recombinant human erythropoietin produced by Chinese hamster ovary cells	524:595	In this study, we purified urinary human erythropoietin from three independent groups of aplastic anemia patients, and analyzed the structures of mucin-type sugar chains as well as that obtained from recombinant human erythropoietin produced by Chinese hamster ovary cells.
8460945	1	17	link	N-linked	248:255	arg1	chains					263:268	N-linked sugar chains	248:268	N-linked sugar chains which structures and function have been well studied	248:321	Less is known about the mucin-type sugar chains attached to human erythropoietin as compared with N-linked sugar chains which structures and function have been well studied.
8460945	4	18	theme	urinary	779:785	arg1	erythropoietin					787:800	urinary erythropoietin	779:800	urinary erythropoietin	779:800	All of the three independent samples of urinary erythropoietin contained oligosaccharides with the structures of +/- Neu5Ac alpha 2-->6GalNAc, while recombinant human erythropoietin contained those with the structures of Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc, Neu5Ac alpha 2-->3Gal beta 1-->3GalNAc, and Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc.
8460945	4	19	theme	Neu5Ac	1020:1025	arg1	beta					1042:1045	Neu5Ac alpha 2-->3Gal beta	1020:1045	Neu5Ac alpha 2-->3Gal beta 1-->3GalNAc	1020:1057	All of the three independent samples of urinary erythropoietin contained oligosaccharides with the structures of +/- Neu5Ac alpha 2-->6GalNAc, while recombinant human erythropoietin contained those with the structures of Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc, Neu5Ac alpha 2-->3Gal beta 1-->3GalNAc, and Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc.
8460945	4	20	theme	Neu5Ac	856:861	arg1	2-->6GalNAc					869:879	+/- Neu5Ac alpha 2-->6GalNAc	852:879	+/- Neu5Ac alpha 2-->6GalNAc	852:879	All of the three independent samples of urinary erythropoietin contained oligosaccharides with the structures of +/- Neu5Ac alpha 2-->6GalNAc, while recombinant human erythropoietin contained those with the structures of Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc, Neu5Ac alpha 2-->3Gal beta 1-->3GalNAc, and Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc.
8460945	3	21	link	N-linked	609:616	arg1	chains					624:629	the N-linked sugar chains	605:629	the N-linked sugar chains	605:629	Unlike the N-linked sugar chains, the mucin-type sugar chains are totally different between the urinary and the recombinant erythropoietins.
8460945	4	22	contain	contained	921:929	arg2	those					931:935	those	931:935	those	931:935	All of the three independent samples of urinary erythropoietin contained oligosaccharides with the structures of +/- Neu5Ac alpha 2-->6GalNAc, while recombinant human erythropoietin contained those with the structures of Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc, Neu5Ac alpha 2-->3Gal beta 1-->3GalNAc, and Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc.
8460945	4	22	contain	contained	921:929	arg1	erythropoietin					906:919	recombinant human erythropoietin	888:919	recombinant human erythropoietin	888:919	All of the three independent samples of urinary erythropoietin contained oligosaccharides with the structures of +/- Neu5Ac alpha 2-->6GalNAc, while recombinant human erythropoietin contained those with the structures of Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc, Neu5Ac alpha 2-->3Gal beta 1-->3GalNAc, and Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc.
8460945	4	23	theme	beta	1042:1045	arg1	1-->3GalNAc					1047:1057	Neu5Ac alpha 2-->3Gal beta 1-->3GalNAc	1020:1057	Neu5Ac alpha 2-->3Gal beta 1-->3GalNAc	1020:1057	All of the three independent samples of urinary erythropoietin contained oligosaccharides with the structures of +/- Neu5Ac alpha 2-->6GalNAc, while recombinant human erythropoietin contained those with the structures of Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc, Neu5Ac alpha 2-->3Gal beta 1-->3GalNAc, and Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc.
8460945	2	24	theme	Chinese	569:575	arg1	cells					591:595	Chinese hamster ovary cells	569:595	Chinese hamster ovary cells	569:595	In this study, we purified urinary human erythropoietin from three independent groups of aplastic anemia patients, and analyzed the structures of mucin-type sugar chains as well as that obtained from recombinant human erythropoietin produced by Chinese hamster ovary cells.
8460945	2	25	theme	recombinant	524:534	arg1	erythropoietin					542:555	recombinant human erythropoietin	524:555	recombinant human erythropoietin produced by Chinese hamster ovary cells	524:595	In this study, we purified urinary human erythropoietin from three independent groups of aplastic anemia patients, and analyzed the structures of mucin-type sugar chains as well as that obtained from recombinant human erythropoietin produced by Chinese hamster ovary cells.
8460945	4	26	theme	alpha	967:971	arg1	2-->6					1006:1010	Neu5Ac alpha 2-->6	993:1010	Neu5Ac alpha 2-->6	993:1010	All of the three independent samples of urinary erythropoietin contained oligosaccharides with the structures of +/- Neu5Ac alpha 2-->6GalNAc, while recombinant human erythropoietin contained those with the structures of Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc, Neu5Ac alpha 2-->3Gal beta 1-->3GalNAc, and Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc.
8460945	4	26	theme	alpha	967:971	arg1	beta					982:985	Neu5Ac alpha 2-->3Gal beta 1-->3	960:991	Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc	960:1017	All of the three independent samples of urinary erythropoietin contained oligosaccharides with the structures of +/- Neu5Ac alpha 2-->6GalNAc, while recombinant human erythropoietin contained those with the structures of Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc, Neu5Ac alpha 2-->3Gal beta 1-->3GalNAc, and Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc.
8460945	4	27	theme	2-->6GalNAc	869:879	arg1	structures					838:847	the structures	834:847	the structures of +/- Neu5Ac alpha 2-->6GalNAc	834:879	All of the three independent samples of urinary erythropoietin contained oligosaccharides with the structures of +/- Neu5Ac alpha 2-->6GalNAc, while recombinant human erythropoietin contained those with the structures of Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc, Neu5Ac alpha 2-->3Gal beta 1-->3GalNAc, and Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc.
8460945	4	28	theme	alpha	863:867	arg1	2-->6GalNAc					869:879	+/- Neu5Ac alpha 2-->6GalNAc	852:879	+/- Neu5Ac alpha 2-->6GalNAc	852:879	All of the three independent samples of urinary erythropoietin contained oligosaccharides with the structures of +/- Neu5Ac alpha 2-->6GalNAc, while recombinant human erythropoietin contained those with the structures of Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc, Neu5Ac alpha 2-->3Gal beta 1-->3GalNAc, and Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc.
8460945	4	29	theme	GalNAc	1098:1103	arg1	structures					946:955	the structures	942:955	the structures of Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc, Neu5Ac alpha 2-->3Gal beta 1-->3GalNAc, and Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc	942:1103	All of the three independent samples of urinary erythropoietin contained oligosaccharides with the structures of +/- Neu5Ac alpha 2-->6GalNAc, while recombinant human erythropoietin contained those with the structures of Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc, Neu5Ac alpha 2-->3Gal beta 1-->3GalNAc, and Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc.
8460945	1	30	theme	mucin-type	174:183	arg1	chains					191:196	the mucin-type sugar chains	170:196	the mucin-type sugar chains attached to human erythropoietin as compared with N-linked sugar chains which structures and function have been well studied	170:321	Less is known about the mucin-type sugar chains attached to human erythropoietin as compared with N-linked sugar chains which structures and function have been well studied.
8460945	0	31	theme	sugar	25:29	arg1	chains					31:36	mucin-type sugar chains	14:36	mucin-type sugar chains	14:36	Structures of mucin-type sugar chains on human erythropoietins purified from urine and the culture medium of recombinant Chinese hamster ovary cells.
8460945	0	32	theme	Chinese	121:127	arg1	cells					143:147	recombinant Chinese hamster ovary cells	109:147	recombinant Chinese hamster ovary cells	109:147	Structures of mucin-type sugar chains on human erythropoietins purified from urine and the culture medium of recombinant Chinese hamster ovary cells.
8460945	1	33	theme	sugar	185:189	arg1	chains					191:196	the mucin-type sugar chains	170:196	the mucin-type sugar chains attached to human erythropoietin as compared with N-linked sugar chains which structures and function have been well studied	170:321	Less is known about the mucin-type sugar chains attached to human erythropoietin as compared with N-linked sugar chains which structures and function have been well studied.
8460945	2	34	theme	anemia	422:427	arg1	patients					429:436	aplastic anemia patients	413:436	aplastic anemia patients	413:436	In this study, we purified urinary human erythropoietin from three independent groups of aplastic anemia patients, and analyzed the structures of mucin-type sugar chains as well as that obtained from recombinant human erythropoietin produced by Chinese hamster ovary cells.
8460945	3	35	dep	urinary	694:700	arg1	erythropoietins					722:736	erythropoietins	722:736	erythropoietins	722:736	Unlike the N-linked sugar chains, the mucin-type sugar chains are totally different between the urinary and the recombinant erythropoietins.
8460945	0	36	theme	recombinant	109:119	arg1	cells					143:147	recombinant Chinese hamster ovary cells	109:147	recombinant Chinese hamster ovary cells	109:147	Structures of mucin-type sugar chains on human erythropoietins purified from urine and the culture medium of recombinant Chinese hamster ovary cells.
8460945	3	37	theme	mucin-type	636:645	arg1	chains					653:658	the mucin-type sugar chains	632:658	the mucin-type sugar chains	632:658	Unlike the N-linked sugar chains, the mucin-type sugar chains are totally different between the urinary and the recombinant erythropoietins.
8460945	3	37	theme	mucin-type	636:645	arg1	different					672:680	different	672:680	different	672:680	Unlike the N-linked sugar chains, the mucin-type sugar chains are totally different between the urinary and the recombinant erythropoietins.
8460945	0	38	theme	ovary	137:141	arg1	cells					143:147	recombinant Chinese hamster ovary cells	109:147	recombinant Chinese hamster ovary cells	109:147	Structures of mucin-type sugar chains on human erythropoietins purified from urine and the culture medium of recombinant Chinese hamster ovary cells.
8460945	3	39	theme	sugar	647:651	arg1	chains					653:658	the mucin-type sugar chains	632:658	the mucin-type sugar chains	632:658	Unlike the N-linked sugar chains, the mucin-type sugar chains are totally different between the urinary and the recombinant erythropoietins.
8460945	3	39	theme	sugar	647:651	arg1	different					672:680	different	672:680	different	672:680	Unlike the N-linked sugar chains, the mucin-type sugar chains are totally different between the urinary and the recombinant erythropoietins.
8460945	4	40	theme	Neu5Ac	960:965	arg1	2-->6					1006:1010	Neu5Ac alpha 2-->6	993:1010	Neu5Ac alpha 2-->6	993:1010	All of the three independent samples of urinary erythropoietin contained oligosaccharides with the structures of +/- Neu5Ac alpha 2-->6GalNAc, while recombinant human erythropoietin contained those with the structures of Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc, Neu5Ac alpha 2-->3Gal beta 1-->3GalNAc, and Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc.
8460945	4	40	theme	Neu5Ac	960:965	arg1	beta					982:985	Neu5Ac alpha 2-->3Gal beta 1-->3	960:991	Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc	960:1017	All of the three independent samples of urinary erythropoietin contained oligosaccharides with the structures of +/- Neu5Ac alpha 2-->6GalNAc, while recombinant human erythropoietin contained those with the structures of Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc, Neu5Ac alpha 2-->3Gal beta 1-->3GalNAc, and Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc.
8460945	2	41	theme	human	359:363	arg1	erythropoietin					365:378	urinary human erythropoietin	351:378	urinary human erythropoietin from three independent groups of aplastic anemia patients	351:436	In this study, we purified urinary human erythropoietin from three independent groups of aplastic anemia patients, and analyzed the structures of mucin-type sugar chains as well as that obtained from recombinant human erythropoietin produced by Chinese hamster ovary cells.
8460945	0	42	theme	chains	31:36	arg1	Structures					0:9	Structures	0:9	Structures of mucin-type sugar chains on human erythropoietins	0:61	Structures of mucin-type sugar chains on human erythropoietins purified from urine and the culture medium of recombinant Chinese hamster ovary cells.
8460945	0	43	theme	hamster	129:135	arg1	cells					143:147	recombinant Chinese hamster ovary cells	109:147	recombinant Chinese hamster ovary cells	109:147	Structures of mucin-type sugar chains on human erythropoietins purified from urine and the culture medium of recombinant Chinese hamster ovary cells.
8460945	2	44	theme	patients	429:436	arg1	groups					403:408	three independent groups	385:408	three independent groups of aplastic anemia patients	385:436	In this study, we purified urinary human erythropoietin from three independent groups of aplastic anemia patients, and analyzed the structures of mucin-type sugar chains as well as that obtained from recombinant human erythropoietin produced by Chinese hamster ovary cells.
8460945	2	44	theme	patients	429:436	arg1	patients					429:436	aplastic anemia patients	413:436	aplastic anemia patients	413:436	In this study, we purified urinary human erythropoietin from three independent groups of aplastic anemia patients, and analyzed the structures of mucin-type sugar chains as well as that obtained from recombinant human erythropoietin produced by Chinese hamster ovary cells.
8460945	2	45	theme	independent	391:401	arg1	groups					403:408	three independent groups	385:408	three independent groups of aplastic anemia patients	385:436	In this study, we purified urinary human erythropoietin from three independent groups of aplastic anemia patients, and analyzed the structures of mucin-type sugar chains as well as that obtained from recombinant human erythropoietin produced by Chinese hamster ovary cells.
8460945	2	45	theme	independent	391:401	arg1	patients					429:436	aplastic anemia patients	413:436	aplastic anemia patients	413:436	In this study, we purified urinary human erythropoietin from three independent groups of aplastic anemia patients, and analyzed the structures of mucin-type sugar chains as well as that obtained from recombinant human erythropoietin produced by Chinese hamster ovary cells.
8460945	4	46	theme	alpha	1027:1031	arg1	beta					1042:1045	Neu5Ac alpha 2-->3Gal beta	1020:1045	Neu5Ac alpha 2-->3Gal beta 1-->3GalNAc	1020:1057	All of the three independent samples of urinary erythropoietin contained oligosaccharides with the structures of +/- Neu5Ac alpha 2-->6GalNAc, while recombinant human erythropoietin contained those with the structures of Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc, Neu5Ac alpha 2-->3Gal beta 1-->3GalNAc, and Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc.
8460945	4	47	theme	beta	982:985	arg1	GalNAc					1012:1017	Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc	960:1017	Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc	960:1017	All of the three independent samples of urinary erythropoietin contained oligosaccharides with the structures of +/- Neu5Ac alpha 2-->6GalNAc, while recombinant human erythropoietin contained those with the structures of Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc, Neu5Ac alpha 2-->3Gal beta 1-->3GalNAc, and Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc.
8460945	2	48	theme	hamster	577:583	arg1	cells					591:595	Chinese hamster ovary cells	569:595	Chinese hamster ovary cells	569:595	In this study, we purified urinary human erythropoietin from three independent groups of aplastic anemia patients, and analyzed the structures of mucin-type sugar chains as well as that obtained from recombinant human erythropoietin produced by Chinese hamster ovary cells.
8460945	4	49	theme	Neu5Ac	993:998	arg1	2-->6					1006:1010	Neu5Ac alpha 2-->6	993:1010	Neu5Ac alpha 2-->6	993:1010	All of the three independent samples of urinary erythropoietin contained oligosaccharides with the structures of +/- Neu5Ac alpha 2-->6GalNAc, while recombinant human erythropoietin contained those with the structures of Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc, Neu5Ac alpha 2-->3Gal beta 1-->3GalNAc, and Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc.
8460945	4	49	theme	Neu5Ac	993:998	arg1	beta					982:985	Neu5Ac alpha 2-->3Gal beta 1-->3	960:991	Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc	960:1017	All of the three independent samples of urinary erythropoietin contained oligosaccharides with the structures of +/- Neu5Ac alpha 2-->6GalNAc, while recombinant human erythropoietin contained those with the structures of Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc, Neu5Ac alpha 2-->3Gal beta 1-->3GalNAc, and Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc.
8460945	4	50	theme	+/-	852:854	arg1	2-->6GalNAc					869:879	+/- Neu5Ac alpha 2-->6GalNAc	852:879	+/- Neu5Ac alpha 2-->6GalNAc	852:879	All of the three independent samples of urinary erythropoietin contained oligosaccharides with the structures of +/- Neu5Ac alpha 2-->6GalNAc, while recombinant human erythropoietin contained those with the structures of Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc, Neu5Ac alpha 2-->3Gal beta 1-->3GalNAc, and Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc.
8460945	0	51	theme	human	41:45	arg1	erythropoietins					47:61	human erythropoietins	41:61	human erythropoietins	41:61	Structures of mucin-type sugar chains on human erythropoietins purified from urine and the culture medium of recombinant Chinese hamster ovary cells.
8460945	0	52	theme	cells	143:147	arg1	urine					77:81	urine	77:81	urine	77:81	Structures of mucin-type sugar chains on human erythropoietins purified from urine and the culture medium of recombinant Chinese hamster ovary cells.
8460945	0	52	theme	cells	143:147	arg1	medium					99:104	the culture medium	87:104	the culture medium of recombinant Chinese hamster ovary cells	87:147	Structures of mucin-type sugar chains on human erythropoietins purified from urine and the culture medium of recombinant Chinese hamster ovary cells.
8460945	4	53	theme	Neu5Ac	1079:1084	arg1	GalNAc					1098:1103	Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc	1064:1103	Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc	1064:1103	All of the three independent samples of urinary erythropoietin contained oligosaccharides with the structures of +/- Neu5Ac alpha 2-->6GalNAc, while recombinant human erythropoietin contained those with the structures of Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc, Neu5Ac alpha 2-->3Gal beta 1-->3GalNAc, and Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc.
8460945	4	53	theme	Neu5Ac	1079:1084	arg1	2-->6					1092:1096	Neu5Ac alpha 2-->6	1079:1096	Neu5Ac alpha 2-->6	1079:1096	All of the three independent samples of urinary erythropoietin contained oligosaccharides with the structures of +/- Neu5Ac alpha 2-->6GalNAc, while recombinant human erythropoietin contained those with the structures of Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc, Neu5Ac alpha 2-->3Gal beta 1-->3GalNAc, and Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc.
8460945	3	54	theme	N-linked	609:616	arg1	chains					624:629	the N-linked sugar chains	605:629	the N-linked sugar chains	605:629	Unlike the N-linked sugar chains, the mucin-type sugar chains are totally different between the urinary and the recombinant erythropoietins.
8460945	4	55	theme	1-->3GalNAc	1047:1057	arg1	structures					946:955	the structures	942:955	the structures of Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc, Neu5Ac alpha 2-->3Gal beta 1-->3GalNAc, and Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc	942:1103	All of the three independent samples of urinary erythropoietin contained oligosaccharides with the structures of +/- Neu5Ac alpha 2-->6GalNAc, while recombinant human erythropoietin contained those with the structures of Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc, Neu5Ac alpha 2-->3Gal beta 1-->3GalNAc, and Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc.
8460945	3	56	theme	sugar	618:622	arg1	chains					624:629	the N-linked sugar chains	605:629	the N-linked sugar chains	605:629	Unlike the N-linked sugar chains, the mucin-type sugar chains are totally different between the urinary and the recombinant erythropoietins.
8460945	1	57	theme	human	210:214	arg1	erythropoietin					216:229	human erythropoietin	210:229	human erythropoietin	210:229	Less is known about the mucin-type sugar chains attached to human erythropoietin as compared with N-linked sugar chains which structures and function have been well studied.
8460945	4	58	theme	erythropoietin	787:800	arg1	samples					768:774	the three independent samples	746:774	the three independent samples of urinary erythropoietin	746:800	All of the three independent samples of urinary erythropoietin contained oligosaccharides with the structures of +/- Neu5Ac alpha 2-->6GalNAc, while recombinant human erythropoietin contained those with the structures of Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc, Neu5Ac alpha 2-->3Gal beta 1-->3GalNAc, and Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc.
8460945	2	59	from	groups	403:408	arg1	erythropoietin					365:378	urinary human erythropoietin	351:378	urinary human erythropoietin from three independent groups of aplastic anemia patients	351:436	In this study, we purified urinary human erythropoietin from three independent groups of aplastic anemia patients, and analyzed the structures of mucin-type sugar chains as well as that obtained from recombinant human erythropoietin produced by Chinese hamster ovary cells.
8460945	4	60	theme	alpha	1000:1004	arg1	2-->6					1006:1010	Neu5Ac alpha 2-->6	993:1010	Neu5Ac alpha 2-->6	993:1010	All of the three independent samples of urinary erythropoietin contained oligosaccharides with the structures of +/- Neu5Ac alpha 2-->6GalNAc, while recombinant human erythropoietin contained those with the structures of Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc, Neu5Ac alpha 2-->3Gal beta 1-->3GalNAc, and Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc.
8460945	4	60	theme	alpha	1000:1004	arg1	beta					982:985	Neu5Ac alpha 2-->3Gal beta 1-->3	960:991	Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc	960:1017	All of the three independent samples of urinary erythropoietin contained oligosaccharides with the structures of +/- Neu5Ac alpha 2-->6GalNAc, while recombinant human erythropoietin contained those with the structures of Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc, Neu5Ac alpha 2-->3Gal beta 1-->3GalNAc, and Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc.
8460945	1	61	attach	attached	198:205	arg2	chains					191:196	the mucin-type sugar chains	170:196	the mucin-type sugar chains attached to human erythropoietin as compared with N-linked sugar chains which structures and function have been well studied	170:321	Less is known about the mucin-type sugar chains attached to human erythropoietin as compared with N-linked sugar chains which structures and function have been well studied.
8460945	1	61	attach	attached	198:205	arg1	erythropoietin					216:229	human erythropoietin	210:229	human erythropoietin	210:229	Less is known about the mucin-type sugar chains attached to human erythropoietin as compared with N-linked sugar chains which structures and function have been well studied.
8460945	2	62	theme	aplastic	413:420	arg1	anemia					422:427	aplastic anemia	413:427	aplastic anemia patients	413:436	In this study, we purified urinary human erythropoietin from three independent groups of aplastic anemia patients, and analyzed the structures of mucin-type sugar chains as well as that obtained from recombinant human erythropoietin produced by Chinese hamster ovary cells.
8460945	2	63	theme	urinary	351:357	arg1	erythropoietin					365:378	urinary human erythropoietin	351:378	urinary human erythropoietin from three independent groups of aplastic anemia patients	351:436	In this study, we purified urinary human erythropoietin from three independent groups of aplastic anemia patients, and analyzed the structures of mucin-type sugar chains as well as that obtained from recombinant human erythropoietin produced by Chinese hamster ovary cells.
8460945	4	64	theme	alpha	1086:1090	arg1	GalNAc					1098:1103	Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc	1064:1103	Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc	1064:1103	All of the three independent samples of urinary erythropoietin contained oligosaccharides with the structures of +/- Neu5Ac alpha 2-->6GalNAc, while recombinant human erythropoietin contained those with the structures of Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc, Neu5Ac alpha 2-->3Gal beta 1-->3GalNAc, and Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc.
8460945	4	64	theme	alpha	1086:1090	arg1	2-->6					1092:1096	Neu5Ac alpha 2-->6	1079:1096	Neu5Ac alpha 2-->6	1079:1096	All of the three independent samples of urinary erythropoietin contained oligosaccharides with the structures of +/- Neu5Ac alpha 2-->6GalNAc, while recombinant human erythropoietin contained those with the structures of Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc, Neu5Ac alpha 2-->3Gal beta 1-->3GalNAc, and Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc.
8460945	2	65	theme	chains	487:492	arg1	structures					456:465	the structures	452:465	the structures of mucin-type sugar chains as well as that obtained from recombinant human erythropoietin produced by Chinese hamster ovary cells	452:595	In this study, we purified urinary human erythropoietin from three independent groups of aplastic anemia patients, and analyzed the structures of mucin-type sugar chains as well as that obtained from recombinant human erythropoietin produced by Chinese hamster ovary cells.
8460945	0	66	theme	mucin-type	14:23	arg1	chains					31:36	mucin-type sugar chains	14:36	mucin-type sugar chains	14:36	Structures of mucin-type sugar chains on human erythropoietins purified from urine and the culture medium of recombinant Chinese hamster ovary cells.
8460945	4	67	theme	Gal	1064:1066	arg1	GalNAc					1098:1103	Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc	1064:1103	Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc	1064:1103	All of the three independent samples of urinary erythropoietin contained oligosaccharides with the structures of +/- Neu5Ac alpha 2-->6GalNAc, while recombinant human erythropoietin contained those with the structures of Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc, Neu5Ac alpha 2-->3Gal beta 1-->3GalNAc, and Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc.
8460945	4	67	theme	Gal	1064:1066	arg1	2-->6					1092:1096	Neu5Ac alpha 2-->6	1079:1096	Neu5Ac alpha 2-->6	1079:1096	All of the three independent samples of urinary erythropoietin contained oligosaccharides with the structures of +/- Neu5Ac alpha 2-->6GalNAc, while recombinant human erythropoietin contained those with the structures of Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc, Neu5Ac alpha 2-->3Gal beta 1-->3GalNAc, and Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc.
8460945	4	68	contain	contained	802:810	arg1	samples					768:774	the three independent samples	746:774	the three independent samples of urinary erythropoietin	746:800	All of the three independent samples of urinary erythropoietin contained oligosaccharides with the structures of +/- Neu5Ac alpha 2-->6GalNAc, while recombinant human erythropoietin contained those with the structures of Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc, Neu5Ac alpha 2-->3Gal beta 1-->3GalNAc, and Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc.
8460945	4	68	contain	contained	802:810	arg1	All					739:741	All	739:741	All	739:741	All of the three independent samples of urinary erythropoietin contained oligosaccharides with the structures of +/- Neu5Ac alpha 2-->6GalNAc, while recombinant human erythropoietin contained those with the structures of Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc, Neu5Ac alpha 2-->3Gal beta 1-->3GalNAc, and Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc.
8460945	4	68	contain	contained	802:810	arg2	oligosaccharides					812:827	oligosaccharides	812:827	oligosaccharides with the structures of +/- Neu5Ac alpha 2-->6GalNAc	812:879	All of the three independent samples of urinary erythropoietin contained oligosaccharides with the structures of +/- Neu5Ac alpha 2-->6GalNAc, while recombinant human erythropoietin contained those with the structures of Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc, Neu5Ac alpha 2-->3Gal beta 1-->3GalNAc, and Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc.
6327299	8	0	theme	Ga1	1126:1128	arg1	1----3					1135:1140	1----3	1135:1140	1----3	1135:1140	The major compound was identified as NeuAc alpha(2----3)Ga1 beta(1----3)[NeuAc alpha(2----3)Ga1 beta(1----4)GlcNAc beta(1----6)]GalNAc-ol.
6327299	8	0	theme	Ga1	1126:1128	arg1	beta					1130:1133	NeuAc alpha(2----3)Ga1 beta	1107:1133	NeuAc alpha(2----3)Ga1 beta(1----3)[NeuAc alpha(2----3)Ga1 beta(1----4)GlcNAc beta(1----6)]GalNAc-ol	1107:1206	The major compound was identified as NeuAc alpha(2----3)Ga1 beta(1----3)[NeuAc alpha(2----3)Ga1 beta(1----4)GlcNAc beta(1----6)]GalNAc-ol.
6327299	8	1	theme	GlcNAc	1178:1183	arg1	beta					1185:1188	[NeuAc alpha(2----3)Ga1 beta(1----4)GlcNAc beta(1----6)	1142:1196	[NeuAc alpha(2----3)Ga1 beta(1----4)GlcNAc beta(1----6)	1142:1196	The major compound was identified as NeuAc alpha(2----3)Ga1 beta(1----3)[NeuAc alpha(2----3)Ga1 beta(1----4)GlcNAc beta(1----6)]GalNAc-ol.
6327299	8	2	theme	beta	1130:1133	arg1	compound					1080:1087	The major compound	1070:1087	The major compound	1070:1087	The major compound was identified as NeuAc alpha(2----3)Ga1 beta(1----3)[NeuAc alpha(2----3)Ga1 beta(1----4)GlcNAc beta(1----6)]GalNAc-ol.
6327299	8	2	theme	beta	1130:1133	arg1	GalNAc-ol					1198:1206	NeuAc alpha(2----3)Ga1 beta(1----3)[NeuAc alpha(2----3)Ga1 beta(1----4)GlcNAc beta(1----6)]GalNAc-ol	1107:1206	NeuAc alpha(2----3)Ga1 beta(1----3)[NeuAc alpha(2----3)Ga1 beta(1----4)GlcNAc beta(1----6)]GalNAc-ol	1107:1206	The major compound was identified as NeuAc alpha(2----3)Ga1 beta(1----3)[NeuAc alpha(2----3)Ga1 beta(1----4)GlcNAc beta(1----6)]GalNAc-ol.
6327299	0	3	theme	glycocalicin	73:84	arg1	chains					48:53	the O-linked carbohydrate chains	22:53	the O-linked carbohydrate chains of human platelet glycocalicin	22:84	Structural studies on the O-linked carbohydrate chains of human platelet glycocalicin.
6327299	0	4	from	studies	11:17	arg1	chains					48:53	the O-linked carbohydrate chains	22:53	the O-linked carbohydrate chains of human platelet glycocalicin	22:84	Structural studies on the O-linked carbohydrate chains of human platelet glycocalicin.
6327299	3	5	theme	2.5	608:610	arg1	%					611:611	%	611:611	%	611:611	The supernatant was applied to a column of wheat germ agglutinin linked to Sepharose 4B; glycocalicin was eluted from the column with 2.5% (w/v) N-acetylglucosamine.
6327299	8	6	theme	beta	1166:1169	arg1	beta					1185:1188	[NeuAc alpha(2----3)Ga1 beta(1----4)GlcNAc beta(1----6)	1142:1196	[NeuAc alpha(2----3)Ga1 beta(1----4)GlcNAc beta(1----6)	1142:1196	The major compound was identified as NeuAc alpha(2----3)Ga1 beta(1----3)[NeuAc alpha(2----3)Ga1 beta(1----4)GlcNAc beta(1----6)]GalNAc-ol.
6327299	1	7	theme	glycoprotein	141:152	arg1	Ib					154:155	glycoprotein Ib	141:155	glycoprotein Ib (160 kDa)	141:165	Glycocalicin (140 kDa), constituting the main part of glycoprotein Ib (160 kDa), was released from the human platelet membrane by the action of a Ca2+-dependent protease, present in the platelet cytoplasm and liberated during sonication of the platelet suspension.
6327299	1	7	theme	glycoprotein	141:152	arg1	kDa					162:164	160 kDa	158:164	160 kDa	158:164	Glycocalicin (140 kDa), constituting the main part of glycoprotein Ib (160 kDa), was released from the human platelet membrane by the action of a Ca2+-dependent protease, present in the platelet cytoplasm and liberated during sonication of the platelet suspension.
6327299	3	8	dep	%	611:611	arg1	w/v					614:616	w/v	614:616	w/v	614:616	The supernatant was applied to a column of wheat germ agglutinin linked to Sepharose 4B; glycocalicin was eluted from the column with 2.5% (w/v) N-acetylglucosamine.
6327299	9	9	theme	minor	1213:1217	arg1	compounds					1219:1227	Two minor compounds	1209:1227	Two minor compounds	1209:1227	Two minor compounds were found to be NeuAc alpha(2----3)Gal beta(1----3)[NeuAc alpha(2----6)]GalNAc-ol and NeuAc alpha(2----3)Gal beta(1----3)GalNAc-ol.
6327299	8	10	dep	1----3	1135:1140	arg1	beta					1185:1188	[NeuAc alpha(2----3)Ga1 beta(1----4)GlcNAc beta(1----6)	1142:1196	[NeuAc alpha(2----3)Ga1 beta(1----4)GlcNAc beta(1----6)	1142:1196	The major compound was identified as NeuAc alpha(2----3)Ga1 beta(1----3)[NeuAc alpha(2----3)Ga1 beta(1----4)GlcNAc beta(1----6)]GalNAc-ol.
6327299	5	11	from	presence	841:848	arg1	chains					791:796	The O-glycosidic chains	774:796	The O-glycosidic chains	774:796	The O-glycosidic chains were split off by alkaline cleavage in the presence of 3H-labelled NaBH4.
6327299	5	11	from	presence	841:848	arg1	split					803:807	split	803:807	split	803:807	The O-glycosidic chains were split off by alkaline cleavage in the presence of 3H-labelled NaBH4.
6327299	3	12	attach	linked	539:544	arg2	agglutinin					528:537	wheat germ agglutinin	517:537	wheat germ agglutinin linked to Sepharose 4B	517:560	The supernatant was applied to a column of wheat germ agglutinin linked to Sepharose 4B; glycocalicin was eluted from the column with 2.5% (w/v) N-acetylglucosamine.
6327299	3	12	attach	linked	539:544	arg1	Sepharose					549:557	Sepharose 4B	549:560	Sepharose 4B	549:560	The supernatant was applied to a column of wheat germ agglutinin linked to Sepharose 4B; glycocalicin was eluted from the column with 2.5% (w/v) N-acetylglucosamine.
6327299	6	13	theme	A-25	960:963	arg1	column					965:970	a DEAE-Sephadex A-25 column	944:970	a DEAE-Sephadex A-25 column	944:970	The liberated 3H-labelled oligosaccharide-alditols were fractionated on a DEAE-Sephadex A-25 column.
6327299	3	14	theme	germ	523:526	arg1	agglutinin					528:537	wheat germ agglutinin	517:537	wheat germ agglutinin linked to Sepharose 4B	517:560	The supernatant was applied to a column of wheat germ agglutinin linked to Sepharose 4B; glycocalicin was eluted from the column with 2.5% (w/v) N-acetylglucosamine.
6327299	1	15	from	present	258:264	arg1	cytoplasm					282:290	the platelet cytoplasm	269:290	the platelet cytoplasm	269:290	Glycocalicin (140 kDa), constituting the main part of glycoprotein Ib (160 kDa), was released from the human platelet membrane by the action of a Ca2+-dependent protease, present in the platelet cytoplasm and liberated during sonication of the platelet suspension.
6327299	6	16	theme	DEAE-Sephadex	946:958	arg1	column					965:970	a DEAE-Sephadex A-25 column	944:970	a DEAE-Sephadex A-25 column	944:970	The liberated 3H-labelled oligosaccharide-alditols were fractionated on a DEAE-Sephadex A-25 column.
6327299	4	17	contain	contain	666:672	arg1	Glycocalicin					640:651	Glycocalicin	640:651	Glycocalicin	640:651	Glycocalicin was found to contain 40% carbohydrate by weight, representing N- as well as O-glycosidically linked carbohydrate chains.
6327299	4	17	contain	contain	666:672	arg2	carbohydrate					678:689	40% carbohydrate	674:689	40% carbohydrate	674:689	Glycocalicin was found to contain 40% carbohydrate by weight, representing N- as well as O-glycosidically linked carbohydrate chains.
6327299	4	18	theme	%	676:676	arg1	carbohydrate					678:689	40% carbohydrate	674:689	40% carbohydrate	674:689	Glycocalicin was found to contain 40% carbohydrate by weight, representing N- as well as O-glycosidically linked carbohydrate chains.
6327299	1	19	theme	Ib	154:155	arg1	part					133:136	the main part	124:136	the main part of glycoprotein Ib (160 kDa)	124:165	Glycocalicin (140 kDa), constituting the main part of glycoprotein Ib (160 kDa), was released from the human platelet membrane by the action of a Ca2+-dependent protease, present in the platelet cytoplasm and liberated during sonication of the platelet suspension.
6327299	2	20	theme	sonicated	398:406	arg1	suspension					417:426	the sonicated platelet suspension	394:426	the sonicated platelet suspension	394:426	After activation of the protease by Ca2+, the sonicated platelet suspension was subjected to differential centrifugation.
6327299	8	21	theme	Ga1	1162:1164	arg1	beta					1185:1188	[NeuAc alpha(2----3)Ga1 beta(1----4)GlcNAc beta(1----6)	1142:1196	[NeuAc alpha(2----3)Ga1 beta(1----4)GlcNAc beta(1----6)	1142:1196	The major compound was identified as NeuAc alpha(2----3)Ga1 beta(1----3)[NeuAc alpha(2----3)Ga1 beta(1----4)GlcNAc beta(1----6)]GalNAc-ol.
6327299	8	22	theme	[NeuAc	1142:1147	arg1	beta					1185:1188	[NeuAc alpha(2----3)Ga1 beta(1----4)GlcNAc beta(1----6)	1142:1196	[NeuAc alpha(2----3)Ga1 beta(1----4)GlcNAc beta(1----6)	1142:1196	The major compound was identified as NeuAc alpha(2----3)Ga1 beta(1----3)[NeuAc alpha(2----3)Ga1 beta(1----4)GlcNAc beta(1----6)]GalNAc-ol.
6327299	9	23	theme	Gal	1265:1267	arg1	alpha					1288:1292	1----3)[NeuAc alpha(2----6)	1274:1300	1----3)[NeuAc alpha(2----6)	1274:1300	Two minor compounds were found to be NeuAc alpha(2----3)Gal beta(1----3)[NeuAc alpha(2----6)]GalNAc-ol and NeuAc alpha(2----3)Gal beta(1----3)GalNAc-ol.
6327299	9	23	theme	Gal	1265:1267	arg1	beta					1269:1272	NeuAc alpha(2----3)Gal beta	1246:1272	NeuAc alpha(2----3)Gal beta(1----3)[NeuAc alpha(2----6)]GalNAc-ol	1246:1310	Two minor compounds were found to be NeuAc alpha(2----3)Gal beta(1----3)[NeuAc alpha(2----6)]GalNAc-ol and NeuAc alpha(2----3)Gal beta(1----3)GalNAc-ol.
6327299	8	24	theme	alpha	1149:1153	arg1	beta					1185:1188	[NeuAc alpha(2----3)Ga1 beta(1----4)GlcNAc beta(1----6)	1142:1196	[NeuAc alpha(2----3)Ga1 beta(1----4)GlcNAc beta(1----6)	1142:1196	The major compound was identified as NeuAc alpha(2----3)Ga1 beta(1----3)[NeuAc alpha(2----3)Ga1 beta(1----4)GlcNAc beta(1----6)]GalNAc-ol.
6327299	8	25	theme	2----3	1119:1124	arg1	1----3					1135:1140	1----3	1135:1140	1----3	1135:1140	The major compound was identified as NeuAc alpha(2----3)Ga1 beta(1----3)[NeuAc alpha(2----3)Ga1 beta(1----4)GlcNAc beta(1----6)]GalNAc-ol.
6327299	8	25	theme	2----3	1119:1124	arg1	beta					1130:1133	NeuAc alpha(2----3)Ga1 beta	1107:1133	NeuAc alpha(2----3)Ga1 beta(1----3)[NeuAc alpha(2----3)Ga1 beta(1----4)GlcNAc beta(1----6)]GalNAc-ol	1107:1206	The major compound was identified as NeuAc alpha(2----3)Ga1 beta(1----3)[NeuAc alpha(2----3)Ga1 beta(1----4)GlcNAc beta(1----6)]GalNAc-ol.
6327299	1	26	attach	present	258:264	arg2	protease					248:255	a Ca2+-dependent protease	231:255	a Ca2+-dependent protease	231:255	Glycocalicin (140 kDa), constituting the main part of glycoprotein Ib (160 kDa), was released from the human platelet membrane by the action of a Ca2+-dependent protease, present in the platelet cytoplasm and liberated during sonication of the platelet suspension.
6327299	1	26	attach	present	258:264	arg1	cytoplasm					282:290	the platelet cytoplasm	269:290	the platelet cytoplasm	269:290	Glycocalicin (140 kDa), constituting the main part of glycoprotein Ib (160 kDa), was released from the human platelet membrane by the action of a Ca2+-dependent protease, present in the platelet cytoplasm and liberated during sonication of the platelet suspension.
6327299	9	27	theme	beta	1339:1342	arg1	GalNAc-ol					1351:1359	NeuAc alpha(2----3)Gal beta(1----3)GalNAc-ol	1316:1359	NeuAc alpha(2----3)Gal beta(1----3)GalNAc-ol	1316:1359	Two minor compounds were found to be NeuAc alpha(2----3)Gal beta(1----3)[NeuAc alpha(2----6)]GalNAc-ol and NeuAc alpha(2----3)Gal beta(1----3)GalNAc-ol.
6327299	0	28	theme	Structural	0:9	arg1	studies					11:17	Structural studies	0:17	Structural studies on the O-linked carbohydrate chains of human platelet glycocalicin	0:84	Structural studies on the O-linked carbohydrate chains of human platelet glycocalicin.
6327299	3	29	theme	agglutinin	528:537	arg1	column					507:512	a column	505:512	a column of wheat germ agglutinin linked to Sepharose 4B	505:560	The supernatant was applied to a column of wheat germ agglutinin linked to Sepharose 4B; glycocalicin was eluted from the column with 2.5% (w/v) N-acetylglucosamine.
6327299	4	30	link	linked	746:751	arg1	chains					766:771	O-glycosidically linked carbohydrate chains	729:771	N- as well as O-glycosidically linked carbohydrate chains	715:771	Glycocalicin was found to contain 40% carbohydrate by weight, representing N- as well as O-glycosidically linked carbohydrate chains.
6327299	9	31	theme	NeuAc	1246:1250	arg1	alpha					1288:1292	1----3)[NeuAc alpha(2----6)	1274:1300	1----3)[NeuAc alpha(2----6)	1274:1300	Two minor compounds were found to be NeuAc alpha(2----3)Gal beta(1----3)[NeuAc alpha(2----6)]GalNAc-ol and NeuAc alpha(2----3)Gal beta(1----3)GalNAc-ol.
6327299	9	31	theme	NeuAc	1246:1250	arg1	beta					1269:1272	NeuAc alpha(2----3)Gal beta	1246:1272	NeuAc alpha(2----3)Gal beta(1----3)[NeuAc alpha(2----6)]GalNAc-ol	1246:1310	Two minor compounds were found to be NeuAc alpha(2----3)Gal beta(1----3)[NeuAc alpha(2----6)]GalNAc-ol and NeuAc alpha(2----3)Gal beta(1----3)GalNAc-ol.
6327299	8	32	theme	major	1074:1078	arg1	compound					1080:1087	The major compound	1070:1087	The major compound	1070:1087	The major compound was identified as NeuAc alpha(2----3)Ga1 beta(1----3)[NeuAc alpha(2----3)Ga1 beta(1----4)GlcNAc beta(1----6)]GalNAc-ol.
6327299	8	32	theme	major	1074:1078	arg1	GalNAc-ol					1198:1206	NeuAc alpha(2----3)Ga1 beta(1----3)[NeuAc alpha(2----3)Ga1 beta(1----4)GlcNAc beta(1----6)]GalNAc-ol	1107:1206	NeuAc alpha(2----3)Ga1 beta(1----3)[NeuAc alpha(2----3)Ga1 beta(1----4)GlcNAc beta(1----6)]GalNAc-ol	1107:1206	The major compound was identified as NeuAc alpha(2----3)Ga1 beta(1----3)[NeuAc alpha(2----3)Ga1 beta(1----4)GlcNAc beta(1----6)]GalNAc-ol.
6327299	0	33	link	O-linked	26:33	arg1	chains					48:53	the O-linked carbohydrate chains	22:53	the O-linked carbohydrate chains of human platelet glycocalicin	22:84	Structural studies on the O-linked carbohydrate chains of human platelet glycocalicin.
6327299	2	34	theme	protease	376:383	arg1	activation					358:367	activation	358:367	activation of the protease by Ca2+	358:391	After activation of the protease by Ca2+, the sonicated platelet suspension was subjected to differential centrifugation.
6327299	4	35	theme	40	674:675	arg1	%					676:676	%	676:676	%	676:676	Glycocalicin was found to contain 40% carbohydrate by weight, representing N- as well as O-glycosidically linked carbohydrate chains.
6327299	1	36	theme	Ca2+-dependent	233:246	arg1	protease					248:255	a Ca2+-dependent protease	231:255	a Ca2+-dependent protease	231:255	Glycocalicin (140 kDa), constituting the main part of glycoprotein Ib (160 kDa), was released from the human platelet membrane by the action of a Ca2+-dependent protease, present in the platelet cytoplasm and liberated during sonication of the platelet suspension.
6327299	1	37	theme	platelet	331:338	arg1	suspension					340:349	the platelet suspension	327:349	the platelet suspension	327:349	Glycocalicin (140 kDa), constituting the main part of glycoprotein Ib (160 kDa), was released from the human platelet membrane by the action of a Ca2+-dependent protease, present in the platelet cytoplasm and liberated during sonication of the platelet suspension.
6327299	3	38	theme	wheat	517:521	arg1	agglutinin					528:537	wheat germ agglutinin	517:537	wheat germ agglutinin linked to Sepharose 4B	517:560	The supernatant was applied to a column of wheat germ agglutinin linked to Sepharose 4B; glycocalicin was eluted from the column with 2.5% (w/v) N-acetylglucosamine.
6327299	3	39	with	column	596:601	arg1	N-acetylglucosamine					619:637	2.5% (w/v) N-acetylglucosamine	608:637	2.5% (w/v) N-acetylglucosamine	608:637	The supernatant was applied to a column of wheat germ agglutinin linked to Sepharose 4B; glycocalicin was eluted from the column with 2.5% (w/v) N-acetylglucosamine.
6327299	5	40	theme	O-glycosidic	778:789	arg1	chains					791:796	The O-glycosidic chains	774:796	The O-glycosidic chains	774:796	The O-glycosidic chains were split off by alkaline cleavage in the presence of 3H-labelled NaBH4.
6327299	5	40	theme	O-glycosidic	778:789	arg1	split					803:807	split	803:807	split	803:807	The O-glycosidic chains were split off by alkaline cleavage in the presence of 3H-labelled NaBH4.
6327299	0	41	theme	carbohydrate	35:46	arg1	chains					48:53	the O-linked carbohydrate chains	22:53	the O-linked carbohydrate chains of human platelet glycocalicin	22:84	Structural studies on the O-linked carbohydrate chains of human platelet glycocalicin.
6327299	1	42	theme	protease	248:255	arg1	action					221:226	the action	217:226	the action of a Ca2+-dependent protease, present in the platelet cytoplasm	217:290	Glycocalicin (140 kDa), constituting the main part of glycoprotein Ib (160 kDa), was released from the human platelet membrane by the action of a Ca2+-dependent protease, present in the platelet cytoplasm and liberated during sonication of the platelet suspension.
6327299	7	43	theme	500-MHz	1041:1047	arg1	spectroscopy					1056:1067	500-MHz 1H-NMR spectroscopy	1041:1067	500-MHz 1H-NMR spectroscopy	1041:1067	The structures of the oligosaccharide-alditols were investigated by 500-MHz 1H-NMR spectroscopy.
6327299	1	44	theme	suspension	340:349	arg1	sonication					313:322	sonication	313:322	sonication of the platelet suspension	313:349	Glycocalicin (140 kDa), constituting the main part of glycoprotein Ib (160 kDa), was released from the human platelet membrane by the action of a Ca2+-dependent protease, present in the platelet cytoplasm and liberated during sonication of the platelet suspension.
6327299	4	45	theme	carbohydrate	753:764	arg1	chains					766:771	O-glycosidically linked carbohydrate chains	729:771	N- as well as O-glycosidically linked carbohydrate chains	715:771	Glycocalicin was found to contain 40% carbohydrate by weight, representing N- as well as O-glycosidically linked carbohydrate chains.
6327299	5	46	theme	alkaline	816:823	arg1	cleavage					825:832	alkaline cleavage	816:832	alkaline cleavage	816:832	The O-glycosidic chains were split off by alkaline cleavage in the presence of 3H-labelled NaBH4.
6327299	9	47	theme	alpha	1252:1256	arg1	alpha					1288:1292	1----3)[NeuAc alpha(2----6)	1274:1300	1----3)[NeuAc alpha(2----6)	1274:1300	Two minor compounds were found to be NeuAc alpha(2----3)Gal beta(1----3)[NeuAc alpha(2----6)]GalNAc-ol and NeuAc alpha(2----3)Gal beta(1----3)GalNAc-ol.
6327299	9	47	theme	alpha	1252:1256	arg1	beta					1269:1272	NeuAc alpha(2----3)Gal beta	1246:1272	NeuAc alpha(2----3)Gal beta(1----3)[NeuAc alpha(2----6)]GalNAc-ol	1246:1310	Two minor compounds were found to be NeuAc alpha(2----3)Gal beta(1----3)[NeuAc alpha(2----6)]GalNAc-ol and NeuAc alpha(2----3)Gal beta(1----3)GalNAc-ol.
6327299	0	48	theme	O-linked	26:33	arg1	chains					48:53	the O-linked carbohydrate chains	22:53	the O-linked carbohydrate chains of human platelet glycocalicin	22:84	Structural studies on the O-linked carbohydrate chains of human platelet glycocalicin.
6327299	9	49	theme	2----3	1258:1263	arg1	alpha					1288:1292	1----3)[NeuAc alpha(2----6)	1274:1300	1----3)[NeuAc alpha(2----6)	1274:1300	Two minor compounds were found to be NeuAc alpha(2----3)Gal beta(1----3)[NeuAc alpha(2----6)]GalNAc-ol and NeuAc alpha(2----3)Gal beta(1----3)GalNAc-ol.
6327299	9	49	theme	2----3	1258:1263	arg1	beta					1269:1272	NeuAc alpha(2----3)Gal beta	1246:1272	NeuAc alpha(2----3)Gal beta(1----3)[NeuAc alpha(2----6)]GalNAc-ol	1246:1310	Two minor compounds were found to be NeuAc alpha(2----3)Gal beta(1----3)[NeuAc alpha(2----6)]GalNAc-ol and NeuAc alpha(2----3)Gal beta(1----3)GalNAc-ol.
6327299	7	50	theme	1H-NMR	1049:1054	arg1	spectroscopy					1056:1067	500-MHz 1H-NMR spectroscopy	1041:1067	500-MHz 1H-NMR spectroscopy	1041:1067	The structures of the oligosaccharide-alditols were investigated by 500-MHz 1H-NMR spectroscopy.
6327299	4	51	theme	linked	746:751	arg1	chains					766:771	O-glycosidically linked carbohydrate chains	729:771	N- as well as O-glycosidically linked carbohydrate chains	715:771	Glycocalicin was found to contain 40% carbohydrate by weight, representing N- as well as O-glycosidically linked carbohydrate chains.
6327299	2	52	theme	platelet	408:415	arg1	suspension					417:426	the sonicated platelet suspension	394:426	the sonicated platelet suspension	394:426	After activation of the protease by Ca2+, the sonicated platelet suspension was subjected to differential centrifugation.
6327299	1	53	theme	present	258:264	arg1	protease					248:255	a Ca2+-dependent protease	231:255	a Ca2+-dependent protease	231:255	Glycocalicin (140 kDa), constituting the main part of glycoprotein Ib (160 kDa), was released from the human platelet membrane by the action of a Ca2+-dependent protease, present in the platelet cytoplasm and liberated during sonication of the platelet suspension.
6327299	2	54	theme	differential	445:456	arg1	centrifugation					458:471	differential centrifugation	445:471	differential centrifugation	445:471	After activation of the protease by Ca2+, the sonicated platelet suspension was subjected to differential centrifugation.
6327299	9	55	theme	2----3	1328:1333	arg1	beta					1339:1342	NeuAc alpha(2----3)Gal beta(1----3)	1316:1350	NeuAc alpha(2----3)Gal beta(1----3)GalNAc-ol	1316:1359	Two minor compounds were found to be NeuAc alpha(2----3)Gal beta(1----3)[NeuAc alpha(2----6)]GalNAc-ol and NeuAc alpha(2----3)Gal beta(1----3)GalNAc-ol.
6327299	7	56	theme	oligosaccharide-alditols	995:1018	arg1	structures					977:986	The structures	973:986	The structures of the oligosaccharide-alditols	973:1018	The structures of the oligosaccharide-alditols were investigated by 500-MHz 1H-NMR spectroscopy.
6327299	9	57	theme	Gal	1335:1337	arg1	beta					1339:1342	NeuAc alpha(2----3)Gal beta(1----3)	1316:1350	NeuAc alpha(2----3)Gal beta(1----3)GalNAc-ol	1316:1359	Two minor compounds were found to be NeuAc alpha(2----3)Gal beta(1----3)[NeuAc alpha(2----6)]GalNAc-ol and NeuAc alpha(2----3)Gal beta(1----3)GalNAc-ol.
6327299	1	58	from	cytoplasm	282:290	arg1	present					258:264	present	258:264	present	258:264	Glycocalicin (140 kDa), constituting the main part of glycoprotein Ib (160 kDa), was released from the human platelet membrane by the action of a Ca2+-dependent protease, present in the platelet cytoplasm and liberated during sonication of the platelet suspension.
6327299	6	59	theme	liberated	876:884	arg1	oligosaccharide-alditols					898:921	The liberated 3H-labelled oligosaccharide-alditols	872:921	The liberated 3H-labelled oligosaccharide-alditols	872:921	The liberated 3H-labelled oligosaccharide-alditols were fractionated on a DEAE-Sephadex A-25 column.
6327299	5	60	theme	3H-labelled	853:863	arg1	NaBH4					865:869	3H-labelled NaBH4	853:869	3H-labelled NaBH4	853:869	The O-glycosidic chains were split off by alkaline cleavage in the presence of 3H-labelled NaBH4.
6327299	9	61	theme	beta	1269:1272	arg1	GalNAc-ol					1302:1310	NeuAc alpha(2----3)Gal beta(1----3)[NeuAc alpha(2----6)]GalNAc-ol	1246:1310	NeuAc alpha(2----3)Gal beta(1----3)[NeuAc alpha(2----6)]GalNAc-ol	1246:1310	Two minor compounds were found to be NeuAc alpha(2----3)Gal beta(1----3)[NeuAc alpha(2----6)]GalNAc-ol and NeuAc alpha(2----3)Gal beta(1----3)GalNAc-ol.
6327299	1	62	gly	glycoprotein	141:152	arg1	glycoprotein					141:152	glycoprotein Ib	141:155	glycoprotein Ib (160 kDa)	141:165	Glycocalicin (140 kDa), constituting the main part of glycoprotein Ib (160 kDa), was released from the human platelet membrane by the action of a Ca2+-dependent protease, present in the platelet cytoplasm and liberated during sonication of the platelet suspension.
6327299	5	63	theme	NaBH4	865:869	arg1	presence					841:848	the presence	837:848	the presence of 3H-labelled NaBH4	837:869	The O-glycosidic chains were split off by alkaline cleavage in the presence of 3H-labelled NaBH4.
6327299	9	64	theme	NeuAc	1316:1320	arg1	beta					1339:1342	NeuAc alpha(2----3)Gal beta(1----3)	1316:1350	NeuAc alpha(2----3)Gal beta(1----3)GalNAc-ol	1316:1359	Two minor compounds were found to be NeuAc alpha(2----3)Gal beta(1----3)[NeuAc alpha(2----6)]GalNAc-ol and NeuAc alpha(2----3)Gal beta(1----3)GalNAc-ol.
6327299	8	65	theme	NeuAc	1107:1111	arg1	1----3					1135:1140	1----3	1135:1140	1----3	1135:1140	The major compound was identified as NeuAc alpha(2----3)Ga1 beta(1----3)[NeuAc alpha(2----3)Ga1 beta(1----4)GlcNAc beta(1----6)]GalNAc-ol.
6327299	8	65	theme	NeuAc	1107:1111	arg1	beta					1130:1133	NeuAc alpha(2----3)Ga1 beta	1107:1133	NeuAc alpha(2----3)Ga1 beta(1----3)[NeuAc alpha(2----3)Ga1 beta(1----4)GlcNAc beta(1----6)]GalNAc-ol	1107:1206	The major compound was identified as NeuAc alpha(2----3)Ga1 beta(1----3)[NeuAc alpha(2----3)Ga1 beta(1----4)GlcNAc beta(1----6)]GalNAc-ol.
6327299	1	66	attach	released	172:179	arg2	kDa					105:107	140 kDa	101:107	140 kDa	101:107	Glycocalicin (140 kDa), constituting the main part of glycoprotein Ib (160 kDa), was released from the human platelet membrane by the action of a Ca2+-dependent protease, present in the platelet cytoplasm and liberated during sonication of the platelet suspension.
6327299	1	66	attach	released	172:179	arg2	Glycocalicin					87:98	Glycocalicin	87:98	Glycocalicin (140 kDa)	87:108	Glycocalicin (140 kDa), constituting the main part of glycoprotein Ib (160 kDa), was released from the human platelet membrane by the action of a Ca2+-dependent protease, present in the platelet cytoplasm and liberated during sonication of the platelet suspension.
6327299	1	66	attach	released	172:179	arg1	membrane					205:212	the human platelet membrane	186:212	the human platelet membrane	186:212	Glycocalicin (140 kDa), constituting the main part of glycoprotein Ib (160 kDa), was released from the human platelet membrane by the action of a Ca2+-dependent protease, present in the platelet cytoplasm and liberated during sonication of the platelet suspension.
6327299	8	67	theme	alpha	1113:1117	arg1	1----3					1135:1140	1----3	1135:1140	1----3	1135:1140	The major compound was identified as NeuAc alpha(2----3)Ga1 beta(1----3)[NeuAc alpha(2----3)Ga1 beta(1----4)GlcNAc beta(1----6)]GalNAc-ol.
6327299	8	67	theme	alpha	1113:1117	arg1	beta					1130:1133	NeuAc alpha(2----3)Ga1 beta	1107:1133	NeuAc alpha(2----3)Ga1 beta(1----3)[NeuAc alpha(2----3)Ga1 beta(1----4)GlcNAc beta(1----6)]GalNAc-ol	1107:1206	The major compound was identified as NeuAc alpha(2----3)Ga1 beta(1----3)[NeuAc alpha(2----3)Ga1 beta(1----4)GlcNAc beta(1----6)]GalNAc-ol.
6327299	0	68	theme	platelet	64:71	arg1	glycocalicin					73:84	human platelet glycocalicin	58:84	human platelet glycocalicin	58:84	Structural studies on the O-linked carbohydrate chains of human platelet glycocalicin.
6327299	3	69	theme	%	611:611	arg1	N-acetylglucosamine					619:637	2.5% (w/v) N-acetylglucosamine	608:637	2.5% (w/v) N-acetylglucosamine	608:637	The supernatant was applied to a column of wheat germ agglutinin linked to Sepharose 4B; glycocalicin was eluted from the column with 2.5% (w/v) N-acetylglucosamine.
6327299	9	70	theme	alpha	1322:1326	arg1	beta					1339:1342	NeuAc alpha(2----3)Gal beta(1----3)	1316:1350	NeuAc alpha(2----3)Gal beta(1----3)GalNAc-ol	1316:1359	Two minor compounds were found to be NeuAc alpha(2----3)Gal beta(1----3)[NeuAc alpha(2----6)]GalNAc-ol and NeuAc alpha(2----3)Gal beta(1----3)GalNAc-ol.
6327299	1	71	theme	main	128:131	arg1	part					133:136	the main part	124:136	the main part of glycoprotein Ib (160 kDa)	124:165	Glycocalicin (140 kDa), constituting the main part of glycoprotein Ib (160 kDa), was released from the human platelet membrane by the action of a Ca2+-dependent protease, present in the platelet cytoplasm and liberated during sonication of the platelet suspension.
6327299	1	72	theme	human	190:194	arg1	membrane					205:212	the human platelet membrane	186:212	the human platelet membrane	186:212	Glycocalicin (140 kDa), constituting the main part of glycoprotein Ib (160 kDa), was released from the human platelet membrane by the action of a Ca2+-dependent protease, present in the platelet cytoplasm and liberated during sonication of the platelet suspension.
6327299	0	73	theme	human	58:62	arg1	glycocalicin					73:84	human platelet glycocalicin	58:84	human platelet glycocalicin	58:84	Structural studies on the O-linked carbohydrate chains of human platelet glycocalicin.
6327299	1	74	theme	platelet	273:280	arg1	cytoplasm					282:290	the platelet cytoplasm	269:290	the platelet cytoplasm	269:290	Glycocalicin (140 kDa), constituting the main part of glycoprotein Ib (160 kDa), was released from the human platelet membrane by the action of a Ca2+-dependent protease, present in the platelet cytoplasm and liberated during sonication of the platelet suspension.
6327299	9	75	theme	[NeuAc	1281:1286	arg1	alpha					1288:1292	1----3)[NeuAc alpha(2----6)	1274:1300	1----3)[NeuAc alpha(2----6)	1274:1300	Two minor compounds were found to be NeuAc alpha(2----3)Gal beta(1----3)[NeuAc alpha(2----6)]GalNAc-ol and NeuAc alpha(2----3)Gal beta(1----3)GalNAc-ol.
6327299	9	75	theme	[NeuAc	1281:1286	arg1	beta					1269:1272	NeuAc alpha(2----3)Gal beta	1246:1272	NeuAc alpha(2----3)Gal beta(1----3)[NeuAc alpha(2----6)]GalNAc-ol	1246:1310	Two minor compounds were found to be NeuAc alpha(2----3)Gal beta(1----3)[NeuAc alpha(2----6)]GalNAc-ol and NeuAc alpha(2----3)Gal beta(1----3)GalNAc-ol.
6327299	5	76	from	split	803:807	arg1	presence					841:848	the presence	837:848	the presence of 3H-labelled NaBH4	837:869	The O-glycosidic chains were split off by alkaline cleavage in the presence of 3H-labelled NaBH4.
6327299	6	77	theme	3H-labelled	886:896	arg1	oligosaccharide-alditols					898:921	The liberated 3H-labelled oligosaccharide-alditols	872:921	The liberated 3H-labelled oligosaccharide-alditols	872:921	The liberated 3H-labelled oligosaccharide-alditols were fractionated on a DEAE-Sephadex A-25 column.
6327299	1	78	theme	platelet	196:203	arg1	membrane					205:212	the human platelet membrane	186:212	the human platelet membrane	186:212	Glycocalicin (140 kDa), constituting the main part of glycoprotein Ib (160 kDa), was released from the human platelet membrane by the action of a Ca2+-dependent protease, present in the platelet cytoplasm and liberated during sonication of the platelet suspension.
12770775	5	0	theme	mucins	799:804	arg1	biosynthesis					776:787	the biosynthesis	772:787	the biosynthesis of airway mucins	772:804	This confirmed the wide diversity of the post-translational processes involved in the biosynthesis of airway mucins, which had already been observed in bronchial diseases, such as chronic bronchitis and cystic fibrosis (CF).
12770775	7	1	theme	Lewis	1148:1152	arg1	determinant					1156:1166	a sulfated Lewis A determinant	1137:1166	a sulfated Lewis A determinant	1137:1166	Six of them corresponded to 3-O-sulfated oligosaccharide chains terminated by a sulfated N-acetyllactosamine, a sulfated Lewis X or a sulfated Lewis A determinant, and the last one corresponded to a 6-O-sulfated chain terminated by a sulfated H-2 determinant.
12770775	7	1	theme	Lewis	1148:1152	arg1	chains					1062:1067	3-O-sulfated oligosaccharide chains	1033:1067	3-O-sulfated oligosaccharide chains terminated by a sulfated N-acetyllactosamine	1033:1112	Six of them corresponded to 3-O-sulfated oligosaccharide chains terminated by a sulfated N-acetyllactosamine, a sulfated Lewis X or a sulfated Lewis A determinant, and the last one corresponded to a 6-O-sulfated chain terminated by a sulfated H-2 determinant.
12770775	0	2	theme	patient	77:83	arg1	mucins					56:61	the respiratory mucins	40:61	the respiratory mucins of a secretor patient suffering from chronic bronchitis	40:117	Sulfated oligosaccharides isolated from the respiratory mucins of a secretor patient suffering from chronic bronchitis.
12770775	7	3	theme	A	1154:1154	arg1	determinant					1156:1166	a sulfated Lewis A determinant	1137:1166	a sulfated Lewis A determinant	1137:1166	Six of them corresponded to 3-O-sulfated oligosaccharide chains terminated by a sulfated N-acetyllactosamine, a sulfated Lewis X or a sulfated Lewis A determinant, and the last one corresponded to a 6-O-sulfated chain terminated by a sulfated H-2 determinant.
12770775	7	3	theme	A	1154:1154	arg1	chains					1062:1067	3-O-sulfated oligosaccharide chains	1033:1067	3-O-sulfated oligosaccharide chains terminated by a sulfated N-acetyllactosamine	1033:1112	Six of them corresponded to 3-O-sulfated oligosaccharide chains terminated by a sulfated N-acetyllactosamine, a sulfated Lewis X or a sulfated Lewis A determinant, and the last one corresponded to a 6-O-sulfated chain terminated by a sulfated H-2 determinant.
12770775	8	4	from	patient	2107:2113	arg1	mucins					2087:2092	the airway mucins	2076:2092	the airway mucins from another patient (blood group O and non-secretor) suffering from chronic bronchitis	2076:2180	Like previous data concerning the airway mucins from another patient (blood group O and non-secretor) suffering from chronic bronchitis [Lo-Guidice et al., Glycoconj.
12770775	1	5	theme	alkaline	168:175	arg1	borohydride					177:187	alkaline borohydride	168:187	alkaline borohydride treatment of the bulk of airway mucins secreted by a patient (blood group O, secretor) suffering from a mildly infected chronic bronchitis	168:326	The most acidic carbohydrate chains released by alkaline borohydride treatment of the bulk of airway mucins secreted by a patient (blood group O, secretor) suffering from a mildly infected chronic bronchitis have been fractionated using high-performance anion-exchange chromatography (HPAEC) according to a protocol already described [Lo-Guidice et al., J. Biol.
12770775	1	6	theme	blood	251:255	arg1	secretor					266:273	secretor	266:273	secretor	266:273	The most acidic carbohydrate chains released by alkaline borohydride treatment of the bulk of airway mucins secreted by a patient (blood group O, secretor) suffering from a mildly infected chronic bronchitis have been fractionated using high-performance anion-exchange chromatography (HPAEC) according to a protocol already described [Lo-Guidice et al., J. Biol.
12770775	1	6	theme	blood	251:255	arg1	O					263:263	blood group O	251:263	blood group O	251:263	The most acidic carbohydrate chains released by alkaline borohydride treatment of the bulk of airway mucins secreted by a patient (blood group O, secretor) suffering from a mildly infected chronic bronchitis have been fractionated using high-performance anion-exchange chromatography (HPAEC) according to a protocol already described [Lo-Guidice et al., J. Biol.
12770775	0	7	theme	chronic	100:106	arg1	bronchitis					108:117	chronic bronchitis	100:117	chronic bronchitis	100:117	Sulfated oligosaccharides isolated from the respiratory mucins of a secretor patient suffering from chronic bronchitis.
12770775	5	8	located	observed	830:837	arg1	fibrosis					900:907	cystic fibrosis	893:907	cystic fibrosis (CF)	893:912	This confirmed the wide diversity of the post-translational processes involved in the biosynthesis of airway mucins, which had already been observed in bronchial diseases, such as chronic bronchitis and cystic fibrosis (CF).
12770775	5	8	located	observed	830:837	arg2	diversity					714:722	the wide diversity	705:722	the wide diversity	705:722	This confirmed the wide diversity of the post-translational processes involved in the biosynthesis of airway mucins, which had already been observed in bronchial diseases, such as chronic bronchitis and cystic fibrosis (CF).
12770775	5	8	located	observed	830:837	arg1	bronchitis					878:887	chronic bronchitis	870:887	chronic bronchitis	870:887	This confirmed the wide diversity of the post-translational processes involved in the biosynthesis of airway mucins, which had already been observed in bronchial diseases, such as chronic bronchitis and cystic fibrosis (CF).
12770775	5	8	located	observed	830:837	arg1	diseases					852:859	bronchial diseases	842:859	bronchial diseases	842:859	This confirmed the wide diversity of the post-translational processes involved in the biosynthesis of airway mucins, which had already been observed in bronchial diseases, such as chronic bronchitis and cystic fibrosis (CF).
12770775	10	9	theme	important	2534:2542	arg1	differences					2544:2554	important differences	2534:2554	important differences	2534:2554	This is in contrast with the data obtained with the airway mucins secreted by the patient severely infected by Pseudomonas aeruginosa and suffering from CF, suggesting that important differences occur in the biosynthesis of airway mucins secreted by patients suffering from different bronchial diseases with or without severe infection.
12770775	1	10	theme	group	257:261	arg1	secretor					266:273	secretor	266:273	secretor	266:273	The most acidic carbohydrate chains released by alkaline borohydride treatment of the bulk of airway mucins secreted by a patient (blood group O, secretor) suffering from a mildly infected chronic bronchitis have been fractionated using high-performance anion-exchange chromatography (HPAEC) according to a protocol already described [Lo-Guidice et al., J. Biol.
12770775	1	10	theme	group	257:261	arg1	O					263:263	blood group O	251:263	blood group O	251:263	The most acidic carbohydrate chains released by alkaline borohydride treatment of the bulk of airway mucins secreted by a patient (blood group O, secretor) suffering from a mildly infected chronic bronchitis have been fractionated using high-performance anion-exchange chromatography (HPAEC) according to a protocol already described [Lo-Guidice et al., J. Biol.
12770775	10	11	dep	patient	2443:2449	arg1	suffering					2499:2507	suffering	2499:2507	suffering from CF	2499:2515	This is in contrast with the data obtained with the airway mucins secreted by the patient severely infected by Pseudomonas aeruginosa and suffering from CF, suggesting that important differences occur in the biosynthesis of airway mucins secreted by patients suffering from different bronchial diseases with or without severe infection.
12770775	10	11	dep	patient	2443:2449	arg1	infected					2460:2467	infected	2460:2467	severely infected by Pseudomonas aeruginosa	2451:2493	This is in contrast with the data obtained with the airway mucins secreted by the patient severely infected by Pseudomonas aeruginosa and suffering from CF, suggesting that important differences occur in the biosynthesis of airway mucins secreted by patients suffering from different bronchial diseases with or without severe infection.
12770775	7	12	theme	sulfated	1139:1146	arg1	determinant					1156:1166	a sulfated Lewis A determinant	1137:1166	a sulfated Lewis A determinant	1137:1166	Six of them corresponded to 3-O-sulfated oligosaccharide chains terminated by a sulfated N-acetyllactosamine, a sulfated Lewis X or a sulfated Lewis A determinant, and the last one corresponded to a 6-O-sulfated chain terminated by a sulfated H-2 determinant.
12770775	7	12	theme	sulfated	1139:1146	arg1	chains					1062:1067	3-O-sulfated oligosaccharide chains	1033:1067	3-O-sulfated oligosaccharide chains terminated by a sulfated N-acetyllactosamine	1033:1112	Six of them corresponded to 3-O-sulfated oligosaccharide chains terminated by a sulfated N-acetyllactosamine, a sulfated Lewis X or a sulfated Lewis A determinant, and the last one corresponded to a 6-O-sulfated chain terminated by a sulfated H-2 determinant.
12770775	10	13	theme	airway	2413:2418	arg1	mucins					2420:2425	the airway mucins	2409:2425	the airway mucins secreted by the patient severely infected by Pseudomonas aeruginosa and suffering from CF	2409:2515	This is in contrast with the data obtained with the airway mucins secreted by the patient severely infected by Pseudomonas aeruginosa and suffering from CF, suggesting that important differences occur in the biosynthesis of airway mucins secreted by patients suffering from different bronchial diseases with or without severe infection.
12770775	9	14	theme	disialylated	2235:2246	arg1	J.					2213:2214	J.	2213:2214	J.	2213:2214	J. 14 (1997) 113], no disialylated oligosaccharide and no sialylated and sulfated oligosaccharide bearing sialyl Lewis X epitope could be isolated.
12770775	9	14	theme	disialylated	2235:2246	arg1	oligosaccharide					2248:2262	no disialylated oligosaccharide and no	2232:2269	oligosaccharide	2248:2262	J. 14 (1997) 113], no disialylated oligosaccharide and no sialylated and sulfated oligosaccharide bearing sialyl Lewis X epitope could be isolated.
12770775	8	15	theme	previous	2051:2058	arg1	data					2060:2063	previous data	2051:2063	previous data concerning the airway mucins from another patient (blood group O and non-secretor) suffering from chronic bronchitis	2051:2180	Like previous data concerning the airway mucins from another patient (blood group O and non-secretor) suffering from chronic bronchitis [Lo-Guidice et al., Glycoconj.
12770775	1	16	theme	borohydride	177:187	arg1	treatment					189:197	alkaline borohydride treatment	168:197	alkaline borohydride treatment of the bulk of airway mucins secreted by a patient (blood group O, secretor) suffering from a mildly infected chronic bronchitis	168:326	The most acidic carbohydrate chains released by alkaline borohydride treatment of the bulk of airway mucins secreted by a patient (blood group O, secretor) suffering from a mildly infected chronic bronchitis have been fractionated using high-performance anion-exchange chromatography (HPAEC) according to a protocol already described [Lo-Guidice et al., J. Biol.
12770775	7	17	theme	6-O-sulfated	1204:1215	arg1	chain					1217:1221	a 6-O-sulfated chain	1202:1221	a 6-O-sulfated chain terminated by a sulfated H-2 determinant	1202:1262	Six of them corresponded to 3-O-sulfated oligosaccharide chains terminated by a sulfated N-acetyllactosamine, a sulfated Lewis X or a sulfated Lewis A determinant, and the last one corresponded to a 6-O-sulfated chain terminated by a sulfated H-2 determinant.
12770775	1	18	theme	high-performance	357:372	arg1	HPAEC					405:409	HPAEC	405:409	HPAEC	405:409	The most acidic carbohydrate chains released by alkaline borohydride treatment of the bulk of airway mucins secreted by a patient (blood group O, secretor) suffering from a mildly infected chronic bronchitis have been fractionated using high-performance anion-exchange chromatography (HPAEC) according to a protocol already described [Lo-Guidice et al., J. Biol.
12770775	1	18	theme	high-performance	357:372	arg1	chromatography					389:402	high-performance anion-exchange chromatography	357:402	high-performance anion-exchange chromatography (HPAEC) according to a protocol already described [Lo-Guidice et al.	357:471	The most acidic carbohydrate chains released by alkaline borohydride treatment of the bulk of airway mucins secreted by a patient (blood group O, secretor) suffering from a mildly infected chronic bronchitis have been fractionated using high-performance anion-exchange chromatography (HPAEC) according to a protocol already described [Lo-Guidice et al., J. Biol.
12770775	1	18	theme	high-performance	357:372	arg1	Biol					477:480	Biol	477:480	Biol	477:480	The most acidic carbohydrate chains released by alkaline borohydride treatment of the bulk of airway mucins secreted by a patient (blood group O, secretor) suffering from a mildly infected chronic bronchitis have been fractionated using high-performance anion-exchange chromatography (HPAEC) according to a protocol already described [Lo-Guidice et al., J. Biol.
12770775	1	19	theme	anion-exchange	374:387	arg1	HPAEC					405:409	HPAEC	405:409	HPAEC	405:409	The most acidic carbohydrate chains released by alkaline borohydride treatment of the bulk of airway mucins secreted by a patient (blood group O, secretor) suffering from a mildly infected chronic bronchitis have been fractionated using high-performance anion-exchange chromatography (HPAEC) according to a protocol already described [Lo-Guidice et al., J. Biol.
12770775	1	19	theme	anion-exchange	374:387	arg1	chromatography					389:402	high-performance anion-exchange chromatography	357:402	high-performance anion-exchange chromatography (HPAEC) according to a protocol already described [Lo-Guidice et al.	357:471	The most acidic carbohydrate chains released by alkaline borohydride treatment of the bulk of airway mucins secreted by a patient (blood group O, secretor) suffering from a mildly infected chronic bronchitis have been fractionated using high-performance anion-exchange chromatography (HPAEC) according to a protocol already described [Lo-Guidice et al., J. Biol.
12770775	1	19	theme	anion-exchange	374:387	arg1	Biol					477:480	Biol	477:480	Biol	477:480	The most acidic carbohydrate chains released by alkaline borohydride treatment of the bulk of airway mucins secreted by a patient (blood group O, secretor) suffering from a mildly infected chronic bronchitis have been fractionated using high-performance anion-exchange chromatography (HPAEC) according to a protocol already described [Lo-Guidice et al., J. Biol.
12770775	7	20	theme	sulfated	1117:1124	arg1	X					1132:1132	a sulfated Lewis X	1115:1132	a sulfated Lewis X	1115:1132	Six of them corresponded to 3-O-sulfated oligosaccharide chains terminated by a sulfated N-acetyllactosamine, a sulfated Lewis X or a sulfated Lewis A determinant, and the last one corresponded to a 6-O-sulfated chain terminated by a sulfated H-2 determinant.
12770775	7	20	theme	sulfated	1117:1124	arg1	chains					1062:1067	3-O-sulfated oligosaccharide chains	1033:1067	3-O-sulfated oligosaccharide chains terminated by a sulfated N-acetyllactosamine	1033:1112	Six of them corresponded to 3-O-sulfated oligosaccharide chains terminated by a sulfated N-acetyllactosamine, a sulfated Lewis X or a sulfated Lewis A determinant, and the last one corresponded to a 6-O-sulfated chain terminated by a sulfated H-2 determinant.
12770775	7	21	theme	sulfated	1239:1246	arg1	determinant					1252:1262	a sulfated H-2 determinant	1237:1262	a sulfated H-2 determinant	1237:1262	Six of them corresponded to 3-O-sulfated oligosaccharide chains terminated by a sulfated N-acetyllactosamine, a sulfated Lewis X or a sulfated Lewis A determinant, and the last one corresponded to a 6-O-sulfated chain terminated by a sulfated H-2 determinant.
12770775	8	22	theme	chronic	2163:2169	arg1	bronchitis					2171:2180	chronic bronchitis	2163:2180	chronic bronchitis	2163:2180	Like previous data concerning the airway mucins from another patient (blood group O and non-secretor) suffering from chronic bronchitis [Lo-Guidice et al., Glycoconj.
12770775	5	23	theme	cystic	893:898	arg1	CF					910:911	CF	910:911	CF	910:911	This confirmed the wide diversity of the post-translational processes involved in the biosynthesis of airway mucins, which had already been observed in bronchial diseases, such as chronic bronchitis and cystic fibrosis (CF).
12770775	5	23	theme	cystic	893:898	arg1	fibrosis					900:907	cystic fibrosis	893:907	cystic fibrosis (CF)	893:912	This confirmed the wide diversity of the post-translational processes involved in the biosynthesis of airway mucins, which had already been observed in bronchial diseases, such as chronic bronchitis and cystic fibrosis (CF).
12770775	0	24	theme	Sulfated	0:7	arg1	oligosaccharides					9:24	Sulfated oligosaccharides	0:24	Sulfated oligosaccharides	0:24	Sulfated oligosaccharides isolated from the respiratory mucins of a secretor patient suffering from chronic bronchitis.
12770775	7	25	theme	Lewis	1126:1130	arg1	X					1132:1132	a sulfated Lewis X	1115:1132	a sulfated Lewis X	1115:1132	Six of them corresponded to 3-O-sulfated oligosaccharide chains terminated by a sulfated N-acetyllactosamine, a sulfated Lewis X or a sulfated Lewis A determinant, and the last one corresponded to a 6-O-sulfated chain terminated by a sulfated H-2 determinant.
12770775	7	25	theme	Lewis	1126:1130	arg1	chains					1062:1067	3-O-sulfated oligosaccharide chains	1033:1067	3-O-sulfated oligosaccharide chains terminated by a sulfated N-acetyllactosamine	1033:1112	Six of them corresponded to 3-O-sulfated oligosaccharide chains terminated by a sulfated N-acetyllactosamine, a sulfated Lewis X or a sulfated Lewis A determinant, and the last one corresponded to a 6-O-sulfated chain terminated by a sulfated H-2 determinant.
12770775	10	26	theme	bronchial	2645:2653	arg1	diseases					2655:2662	different bronchial diseases	2635:2662	different bronchial diseases with or without severe infection	2635:2695	This is in contrast with the data obtained with the airway mucins secreted by the patient severely infected by Pseudomonas aeruginosa and suffering from CF, suggesting that important differences occur in the biosynthesis of airway mucins secreted by patients suffering from different bronchial diseases with or without severe infection.
12770775	5	27	theme	bronchial	842:850	arg1	fibrosis					900:907	cystic fibrosis	893:907	cystic fibrosis (CF)	893:912	This confirmed the wide diversity of the post-translational processes involved in the biosynthesis of airway mucins, which had already been observed in bronchial diseases, such as chronic bronchitis and cystic fibrosis (CF).
12770775	5	27	theme	bronchial	842:850	arg1	bronchitis					878:887	chronic bronchitis	870:887	chronic bronchitis	870:887	This confirmed the wide diversity of the post-translational processes involved in the biosynthesis of airway mucins, which had already been observed in bronchial diseases, such as chronic bronchitis and cystic fibrosis (CF).
12770775	5	27	theme	bronchial	842:850	arg1	diseases					852:859	bronchial diseases	842:859	bronchial diseases	842:859	This confirmed the wide diversity of the post-translational processes involved in the biosynthesis of airway mucins, which had already been observed in bronchial diseases, such as chronic bronchitis and cystic fibrosis (CF).
12770775	6	28	theme	structural	979:988	arg1	determination					990:1002	their structural determination	973:1002	their structural determination	973:1002	Seven fractions were directly purified by HPAEC, allowing their structural determination.
12770775	9	29	gly	disialylated	2235:2246	arg1	J.					2213:2214	J.	2213:2214	J.	2213:2214	J. 14 (1997) 113], no disialylated oligosaccharide and no sialylated and sulfated oligosaccharide bearing sialyl Lewis X epitope could be isolated.
12770775	9	29	gly	disialylated	2235:2246	arg1	oligosaccharide					2248:2262	no disialylated oligosaccharide and no	2232:2269	oligosaccharide	2248:2262	J. 14 (1997) 113], no disialylated oligosaccharide and no sialylated and sulfated oligosaccharide bearing sialyl Lewis X epitope could be isolated.
12770775	8	30	theme	group	2122:2126	arg1	O					2128:2128	blood group O	2116:2128	blood group O	2116:2128	Like previous data concerning the airway mucins from another patient (blood group O and non-secretor) suffering from chronic bronchitis [Lo-Guidice et al., Glycoconj.
12770775	1	31	theme	bulk	206:209	arg1	treatment					189:197	alkaline borohydride treatment	168:197	alkaline borohydride treatment of the bulk of airway mucins secreted by a patient (blood group O, secretor) suffering from a mildly infected chronic bronchitis	168:326	The most acidic carbohydrate chains released by alkaline borohydride treatment of the bulk of airway mucins secreted by a patient (blood group O, secretor) suffering from a mildly infected chronic bronchitis have been fractionated using high-performance anion-exchange chromatography (HPAEC) according to a protocol already described [Lo-Guidice et al., J. Biol.
12770775	7	32	theme	sulfated	1085:1092	arg1	N-acetyllactosamine					1094:1112	a sulfated N-acetyllactosamine	1083:1112	a sulfated N-acetyllactosamine	1083:1112	Six of them corresponded to 3-O-sulfated oligosaccharide chains terminated by a sulfated N-acetyllactosamine, a sulfated Lewis X or a sulfated Lewis A determinant, and the last one corresponded to a 6-O-sulfated chain terminated by a sulfated H-2 determinant.
12770775	3	33	theme	1H-NMR	531:536	arg1	spectroscopy					538:549	1H-NMR spectroscopy	531:549	1H-NMR spectroscopy	531:549	269 (1994) 18794] and were analyzed using 1H-NMR spectroscopy and matrix-assisted laser-adsorption-time-of-flight (MALDI-TOF) spectrometry.
12770775	9	34	theme	sialyl	2319:2324	arg1	Lewis					2326:2330	sialyl Lewis	2319:2330	sialyl Lewis	2319:2330	J. 14 (1997) 113], no disialylated oligosaccharide and no sialylated and sulfated oligosaccharide bearing sialyl Lewis X epitope could be isolated.
12770775	9	35	theme	sulfated	2286:2293	arg1	oligosaccharide					2295:2309	sulfated oligosaccharide	2286:2309	sulfated oligosaccharide bearing sialyl Lewis X epitope	2286:2340	J. 14 (1997) 113], no disialylated oligosaccharide and no sialylated and sulfated oligosaccharide bearing sialyl Lewis X epitope could be isolated.
12770775	0	36	theme	respiratory	44:54	arg1	mucins					56:61	the respiratory mucins	40:61	the respiratory mucins of a secretor patient suffering from chronic bronchitis	40:117	Sulfated oligosaccharides isolated from the respiratory mucins of a secretor patient suffering from chronic bronchitis.
12770775	5	37	theme	post-translational	731:748	arg1	processes					750:758	the post-translational processes	727:758	the post-translational processes involved in the biosynthesis of airway mucins	727:804	This confirmed the wide diversity of the post-translational processes involved in the biosynthesis of airway mucins, which had already been observed in bronchial diseases, such as chronic bronchitis and cystic fibrosis (CF).
12770775	1	38	dep	patient	242:248	arg1	secretor					266:273	secretor	266:273	secretor	266:273	The most acidic carbohydrate chains released by alkaline borohydride treatment of the bulk of airway mucins secreted by a patient (blood group O, secretor) suffering from a mildly infected chronic bronchitis have been fractionated using high-performance anion-exchange chromatography (HPAEC) according to a protocol already described [Lo-Guidice et al., J. Biol.
12770775	1	38	dep	patient	242:248	arg1	O					263:263	blood group O	251:263	blood group O	251:263	The most acidic carbohydrate chains released by alkaline borohydride treatment of the bulk of airway mucins secreted by a patient (blood group O, secretor) suffering from a mildly infected chronic bronchitis have been fractionated using high-performance anion-exchange chromatography (HPAEC) according to a protocol already described [Lo-Guidice et al., J. Biol.
12770775	10	39	theme	mucins	2592:2597	arg1	biosynthesis					2569:2580	the biosynthesis	2565:2580	the biosynthesis of airway mucins secreted by patients suffering from different bronchial diseases with or without severe infection	2565:2695	This is in contrast with the data obtained with the airway mucins secreted by the patient severely infected by Pseudomonas aeruginosa and suffering from CF, suggesting that important differences occur in the biosynthesis of airway mucins secreted by patients suffering from different bronchial diseases with or without severe infection.
12770775	1	40	theme	airway	214:219	arg1	mucins					221:226	airway mucins	214:226	airway mucins secreted by a patient (blood group O, secretor) suffering from a mildly infected chronic bronchitis	214:326	The most acidic carbohydrate chains released by alkaline borohydride treatment of the bulk of airway mucins secreted by a patient (blood group O, secretor) suffering from a mildly infected chronic bronchitis have been fractionated using high-performance anion-exchange chromatography (HPAEC) according to a protocol already described [Lo-Guidice et al., J. Biol.
12770775	4	41	theme	oligosaccharides	672:687	arg1	mixtures					660:667	mixtures	660:667	mixtures of oligosaccharides	660:687	Many fractions corresponded to mixtures of oligosaccharides.
12770775	5	42	theme	processes	750:758	arg1	diversity					714:722	the wide diversity	705:722	the wide diversity	705:722	This confirmed the wide diversity of the post-translational processes involved in the biosynthesis of airway mucins, which had already been observed in bronchial diseases, such as chronic bronchitis and cystic fibrosis (CF).
12770775	8	43	theme	airway	2080:2085	arg1	mucins					2087:2092	the airway mucins	2076:2092	the airway mucins from another patient (blood group O and non-secretor) suffering from chronic bronchitis	2076:2180	Like previous data concerning the airway mucins from another patient (blood group O and non-secretor) suffering from chronic bronchitis [Lo-Guidice et al., Glycoconj.
12770775	3	44	theme	MALDI-TOF	604:612	arg1	spectrometry					615:626	matrix-assisted laser-adsorption-time-of-flight (MALDI-TOF) spectrometry	555:626	matrix-assisted laser-adsorption-time-of-flight (MALDI-TOF) spectrometry	555:626	269 (1994) 18794] and were analyzed using 1H-NMR spectroscopy and matrix-assisted laser-adsorption-time-of-flight (MALDI-TOF) spectrometry.
12770775	7	45	theme	3-O-sulfated	1033:1044	arg1	X					1132:1132	a sulfated Lewis X	1115:1132	a sulfated Lewis X	1115:1132	Six of them corresponded to 3-O-sulfated oligosaccharide chains terminated by a sulfated N-acetyllactosamine, a sulfated Lewis X or a sulfated Lewis A determinant, and the last one corresponded to a 6-O-sulfated chain terminated by a sulfated H-2 determinant.
12770775	7	45	theme	3-O-sulfated	1033:1044	arg1	chains					1062:1067	3-O-sulfated oligosaccharide chains	1033:1067	3-O-sulfated oligosaccharide chains terminated by a sulfated N-acetyllactosamine	1033:1112	Six of them corresponded to 3-O-sulfated oligosaccharide chains terminated by a sulfated N-acetyllactosamine, a sulfated Lewis X or a sulfated Lewis A determinant, and the last one corresponded to a 6-O-sulfated chain terminated by a sulfated H-2 determinant.
12770775	7	45	theme	3-O-sulfated	1033:1044	arg1	determinant					1156:1166	a sulfated Lewis A determinant	1137:1166	a sulfated Lewis A determinant	1137:1166	Six of them corresponded to 3-O-sulfated oligosaccharide chains terminated by a sulfated N-acetyllactosamine, a sulfated Lewis X or a sulfated Lewis A determinant, and the last one corresponded to a 6-O-sulfated chain terminated by a sulfated H-2 determinant.
12770775	1	46	theme	mucins	221:226	arg1	bulk					206:209	the bulk	202:209	the bulk of airway mucins secreted by a patient (blood group O, secretor) suffering from a mildly infected chronic bronchitis	202:326	The most acidic carbohydrate chains released by alkaline borohydride treatment of the bulk of airway mucins secreted by a patient (blood group O, secretor) suffering from a mildly infected chronic bronchitis have been fractionated using high-performance anion-exchange chromatography (HPAEC) according to a protocol already described [Lo-Guidice et al., J. Biol.
12770775	7	47	theme	H-2	1248:1250	arg1	determinant					1252:1262	a sulfated H-2 determinant	1237:1262	a sulfated H-2 determinant	1237:1262	Six of them corresponded to 3-O-sulfated oligosaccharide chains terminated by a sulfated N-acetyllactosamine, a sulfated Lewis X or a sulfated Lewis A determinant, and the last one corresponded to a 6-O-sulfated chain terminated by a sulfated H-2 determinant.
12770775	3	48	theme	matrix-assisted	555:569	arg1	spectrometry					615:626	matrix-assisted laser-adsorption-time-of-flight (MALDI-TOF) spectrometry	555:626	matrix-assisted laser-adsorption-time-of-flight (MALDI-TOF) spectrometry	555:626	269 (1994) 18794] and were analyzed using 1H-NMR spectroscopy and matrix-assisted laser-adsorption-time-of-flight (MALDI-TOF) spectrometry.
12770775	7	49	theme	oligosaccharide	1046:1060	arg1	X					1132:1132	a sulfated Lewis X	1115:1132	a sulfated Lewis X	1115:1132	Six of them corresponded to 3-O-sulfated oligosaccharide chains terminated by a sulfated N-acetyllactosamine, a sulfated Lewis X or a sulfated Lewis A determinant, and the last one corresponded to a 6-O-sulfated chain terminated by a sulfated H-2 determinant.
12770775	7	49	theme	oligosaccharide	1046:1060	arg1	chains					1062:1067	3-O-sulfated oligosaccharide chains	1033:1067	3-O-sulfated oligosaccharide chains terminated by a sulfated N-acetyllactosamine	1033:1112	Six of them corresponded to 3-O-sulfated oligosaccharide chains terminated by a sulfated N-acetyllactosamine, a sulfated Lewis X or a sulfated Lewis A determinant, and the last one corresponded to a 6-O-sulfated chain terminated by a sulfated H-2 determinant.
12770775	7	49	theme	oligosaccharide	1046:1060	arg1	determinant					1156:1166	a sulfated Lewis A determinant	1137:1166	a sulfated Lewis A determinant	1137:1166	Six of them corresponded to 3-O-sulfated oligosaccharide chains terminated by a sulfated N-acetyllactosamine, a sulfated Lewis X or a sulfated Lewis A determinant, and the last one corresponded to a 6-O-sulfated chain terminated by a sulfated H-2 determinant.
12770775	10	50	theme	severe	2680:2685	arg1	infection					2687:2695	severe infection	2680:2695	severe infection	2680:2695	This is in contrast with the data obtained with the airway mucins secreted by the patient severely infected by Pseudomonas aeruginosa and suffering from CF, suggesting that important differences occur in the biosynthesis of airway mucins secreted by patients suffering from different bronchial diseases with or without severe infection.
12770775	3	51	theme	laser-adsorption-time-of-flight	571:601	arg1	spectrometry					615:626	matrix-assisted laser-adsorption-time-of-flight (MALDI-TOF) spectrometry	555:626	matrix-assisted laser-adsorption-time-of-flight (MALDI-TOF) spectrometry	555:626	269 (1994) 18794] and were analyzed using 1H-NMR spectroscopy and matrix-assisted laser-adsorption-time-of-flight (MALDI-TOF) spectrometry.
12770775	1	52	theme	most	124:127	arg1	chains					149:154	The most acidic carbohydrate chains	120:154	The most acidic carbohydrate chains released by alkaline borohydride treatment of the bulk of airway mucins secreted by a patient (blood group O, secretor) suffering from a mildly infected chronic bronchitis	120:326	The most acidic carbohydrate chains released by alkaline borohydride treatment of the bulk of airway mucins secreted by a patient (blood group O, secretor) suffering from a mildly infected chronic bronchitis have been fractionated using high-performance anion-exchange chromatography (HPAEC) according to a protocol already described [Lo-Guidice et al., J. Biol.
12770775	1	53	theme	infected	300:307	arg1	bronchitis					317:326	a mildly infected chronic bronchitis	291:326	a mildly infected chronic bronchitis	291:326	The most acidic carbohydrate chains released by alkaline borohydride treatment of the bulk of airway mucins secreted by a patient (blood group O, secretor) suffering from a mildly infected chronic bronchitis have been fractionated using high-performance anion-exchange chromatography (HPAEC) according to a protocol already described [Lo-Guidice et al., J. Biol.
12770775	5	54	theme	wide	709:712	arg1	diversity					714:722	the wide diversity	705:722	the wide diversity	705:722	This confirmed the wide diversity of the post-translational processes involved in the biosynthesis of airway mucins, which had already been observed in bronchial diseases, such as chronic bronchitis and cystic fibrosis (CF).
12770775	8	55	dep	patient	2107:2113	arg1	non-secretor					2134:2145	non-secretor	2134:2145	non-secretor	2134:2145	Like previous data concerning the airway mucins from another patient (blood group O and non-secretor) suffering from chronic bronchitis [Lo-Guidice et al., Glycoconj.
12770775	8	55	dep	patient	2107:2113	arg1	O					2128:2128	blood group O	2116:2128	blood group O	2116:2128	Like previous data concerning the airway mucins from another patient (blood group O and non-secretor) suffering from chronic bronchitis [Lo-Guidice et al., Glycoconj.
12770775	10	56	theme	airway	2585:2590	arg1	mucins					2592:2597	airway mucins	2585:2597	airway mucins secreted by patients suffering from different bronchial diseases with or without severe infection	2585:2695	This is in contrast with the data obtained with the airway mucins secreted by the patient severely infected by Pseudomonas aeruginosa and suffering from CF, suggesting that important differences occur in the biosynthesis of airway mucins secreted by patients suffering from different bronchial diseases with or without severe infection.
12770775	1	57	theme	acidic	129:134	arg1	chains					149:154	The most acidic carbohydrate chains	120:154	The most acidic carbohydrate chains released by alkaline borohydride treatment of the bulk of airway mucins secreted by a patient (blood group O, secretor) suffering from a mildly infected chronic bronchitis	120:326	The most acidic carbohydrate chains released by alkaline borohydride treatment of the bulk of airway mucins secreted by a patient (blood group O, secretor) suffering from a mildly infected chronic bronchitis have been fractionated using high-performance anion-exchange chromatography (HPAEC) according to a protocol already described [Lo-Guidice et al., J. Biol.
12770775	10	58	with	contrast	2372:2379	arg1	data					2390:2393	the data	2386:2393	the data obtained with the airway mucins secreted by the patient severely infected by Pseudomonas aeruginosa and suffering from CF	2386:2515	This is in contrast with the data obtained with the airway mucins secreted by the patient severely infected by Pseudomonas aeruginosa and suffering from CF, suggesting that important differences occur in the biosynthesis of airway mucins secreted by patients suffering from different bronchial diseases with or without severe infection.
12770775	1	59	theme	carbohydrate	136:147	arg1	chains					149:154	The most acidic carbohydrate chains	120:154	The most acidic carbohydrate chains released by alkaline borohydride treatment of the bulk of airway mucins secreted by a patient (blood group O, secretor) suffering from a mildly infected chronic bronchitis	120:326	The most acidic carbohydrate chains released by alkaline borohydride treatment of the bulk of airway mucins secreted by a patient (blood group O, secretor) suffering from a mildly infected chronic bronchitis have been fractionated using high-performance anion-exchange chromatography (HPAEC) according to a protocol already described [Lo-Guidice et al., J. Biol.
12770775	0	60	theme	secretor	68:75	arg1	patient					77:83	a secretor patient	66:83	a secretor patient suffering from chronic bronchitis	66:117	Sulfated oligosaccharides isolated from the respiratory mucins of a secretor patient suffering from chronic bronchitis.
12770775	5	61	theme	chronic	870:876	arg1	bronchitis					878:887	chronic bronchitis	870:887	chronic bronchitis	870:887	This confirmed the wide diversity of the post-translational processes involved in the biosynthesis of airway mucins, which had already been observed in bronchial diseases, such as chronic bronchitis and cystic fibrosis (CF).
12770775	10	62	theme	different	2635:2643	arg1	diseases					2655:2662	different bronchial diseases	2635:2662	different bronchial diseases with or without severe infection	2635:2695	This is in contrast with the data obtained with the airway mucins secreted by the patient severely infected by Pseudomonas aeruginosa and suffering from CF, suggesting that important differences occur in the biosynthesis of airway mucins secreted by patients suffering from different bronchial diseases with or without severe infection.
12770775	7	63	theme	them	1012:1015	arg1	them					1012:1015	them	1012:1015	them	1012:1015	Six of them corresponded to 3-O-sulfated oligosaccharide chains terminated by a sulfated N-acetyllactosamine, a sulfated Lewis X or a sulfated Lewis A determinant, and the last one corresponded to a 6-O-sulfated chain terminated by a sulfated H-2 determinant.
12770775	7	63	theme	them	1012:1015	arg1	Six					1005:1007	Six	1005:1007	Six	1005:1007	Six of them corresponded to 3-O-sulfated oligosaccharide chains terminated by a sulfated N-acetyllactosamine, a sulfated Lewis X or a sulfated Lewis A determinant, and the last one corresponded to a 6-O-sulfated chain terminated by a sulfated H-2 determinant.
12770775	8	64	theme	blood	2116:2120	arg1	O					2128:2128	blood group O	2116:2128	blood group O	2116:2128	Like previous data concerning the airway mucins from another patient (blood group O and non-secretor) suffering from chronic bronchitis [Lo-Guidice et al., Glycoconj.
12770775	4	65	theme	Many	629:632	arg1	fractions					634:642	Many fractions	629:642	Many fractions	629:642	Many fractions corresponded to mixtures of oligosaccharides.
12770775	5	66	theme	airway	792:797	arg1	mucins					799:804	airway mucins	792:804	airway mucins	792:804	This confirmed the wide diversity of the post-translational processes involved in the biosynthesis of airway mucins, which had already been observed in bronchial diseases, such as chronic bronchitis and cystic fibrosis (CF).
12770775	1	67	theme	chronic	309:315	arg1	bronchitis					317:326	a mildly infected chronic bronchitis	291:326	a mildly infected chronic bronchitis	291:326	The most acidic carbohydrate chains released by alkaline borohydride treatment of the bulk of airway mucins secreted by a patient (blood group O, secretor) suffering from a mildly infected chronic bronchitis have been fractionated using high-performance anion-exchange chromatography (HPAEC) according to a protocol already described [Lo-Guidice et al., J. Biol.
2018475	5	0	contain	containing	469:478	arg1	fractions					459:467	these fractions	453:467	these fractions containing a mixture of sulphated oligosaccharides	453:518	One of these fractions containing a mixture of sulphated oligosaccharides was subsequently submitted to gel-filtration chromatography and h.p.l.c. Two sulphated oligosaccharide-alditols, A and B, were prepared; their structure was determined by means of 400 MHz 1H-n.m.r. spectroscopy and fast-atom-bombardment m.s.
2018475	5	0	contain	containing	469:478	arg2	mixture					482:488	a mixture	480:488	a mixture of sulphated oligosaccharides	480:518	One of these fractions containing a mixture of sulphated oligosaccharides was subsequently submitted to gel-filtration chromatography and h.p.l.c. Two sulphated oligosaccharide-alditols, A and B, were prepared; their structure was determined by means of 400 MHz 1H-n.m.r. spectroscopy and fast-atom-bombardment m.s.
2018475	0	1	theme	patient	73:79	arg1	mucins					61:66	respiratory mucins	49:66	respiratory mucins of a patient suffering from cystic fibrosis	49:110	Structure of two sulphated oligosaccharides from respiratory mucins of a patient suffering from cystic fibrosis.
2018475	5	2	theme	fast-atom-bombardment	735:755	arg1	m.s					757:759	fast-atom-bombardment m.s	735:759	fast-atom-bombardment m.s	735:759	One of these fractions containing a mixture of sulphated oligosaccharides was subsequently submitted to gel-filtration chromatography and h.p.l.c. Two sulphated oligosaccharide-alditols, A and B, were prepared; their structure was determined by means of 400 MHz 1H-n.m.r. spectroscopy and fast-atom-bombardment m.s.
2018475	0	3	theme	cystic	96:101	arg1	fibrosis					103:110	cystic fibrosis	96:110	cystic fibrosis	96:110	Structure of two sulphated oligosaccharides from respiratory mucins of a patient suffering from cystic fibrosis.
2018475	5	4	dep	submitted	537:545	arg1	determined					677:686	determined	677:686	was determined by means of 400 MHz 1H-n.m.r. spectroscopy and fast-atom-bombardment m.s	673:759	One of these fractions containing a mixture of sulphated oligosaccharides was subsequently submitted to gel-filtration chromatography and h.p.l.c. Two sulphated oligosaccharide-alditols, A and B, were prepared; their structure was determined by means of 400 MHz 1H-n.m.r. spectroscopy and fast-atom-bombardment m.s.
2018475	1	5	dep	m.s.	137:140	arg1	A					113:113	A	113:113	A	113:113	A fast-atom-bombardment m.s. and 1H-n.m.r. spectroscopic study.
2018475	5	6	theme	sulphated	493:501	arg1	oligosaccharides					503:518	sulphated oligosaccharides	493:518	sulphated oligosaccharides	493:518	One of these fractions containing a mixture of sulphated oligosaccharides was subsequently submitted to gel-filtration chromatography and h.p.l.c. Two sulphated oligosaccharide-alditols, A and B, were prepared; their structure was determined by means of 400 MHz 1H-n.m.r. spectroscopy and fast-atom-bombardment m.s.
2018475	0	7	from	mucins	61:66	arg1	Structure					0:8	Structure	0:8	Structure of two sulphated oligosaccharides from respiratory mucins of a patient suffering from cystic fibrosis.	0:111	Structure of two sulphated oligosaccharides from respiratory mucins of a patient suffering from cystic fibrosis.
2018475	5	8	theme	h.p.l.c.	584:591	arg1	B					639:639	B	639:639	B	639:639	One of these fractions containing a mixture of sulphated oligosaccharides was subsequently submitted to gel-filtration chromatography and h.p.l.c. Two sulphated oligosaccharide-alditols, A and B, were prepared; their structure was determined by means of 400 MHz 1H-n.m.r. spectroscopy and fast-atom-bombardment m.s.
2018475	5	8	theme	h.p.l.c.	584:591	arg1	A					633:633	A	633:633	A	633:633	One of these fractions containing a mixture of sulphated oligosaccharides was subsequently submitted to gel-filtration chromatography and h.p.l.c. Two sulphated oligosaccharide-alditols, A and B, were prepared; their structure was determined by means of 400 MHz 1H-n.m.r. spectroscopy and fast-atom-bombardment m.s.
2018475	5	8	theme	h.p.l.c.	584:591	arg1	oligosaccharide-alditols					607:630	h.p.l.c. Two sulphated oligosaccharide-alditols	584:630	h.p.l.c. Two sulphated oligosaccharide-alditols	584:630	One of these fractions containing a mixture of sulphated oligosaccharides was subsequently submitted to gel-filtration chromatography and h.p.l.c. Two sulphated oligosaccharide-alditols, A and B, were prepared; their structure was determined by means of 400 MHz 1H-n.m.r. spectroscopy and fast-atom-bombardment m.s.
2018475	5	9	theme	MHz	704:706	arg1	spectroscopy					718:729	400 MHz 1H-n.m.r. spectroscopy	700:729	400 MHz 1H-n.m.r. spectroscopy	700:729	One of these fractions containing a mixture of sulphated oligosaccharides was subsequently submitted to gel-filtration chromatography and h.p.l.c. Two sulphated oligosaccharide-alditols, A and B, were prepared; their structure was determined by means of 400 MHz 1H-n.m.r. spectroscopy and fast-atom-bombardment m.s.
2018475	3	10	with	treatment	313:321	arg1	borohydride					337:347	alkaline borohydride	328:347	alkaline borohydride	328:347	They were subjected to treatment with alkaline borohydride.
2018475	5	11	theme	1H-n.m.r.	708:716	arg1	spectroscopy					718:729	400 MHz 1H-n.m.r. spectroscopy	700:729	400 MHz 1H-n.m.r. spectroscopy	700:729	One of these fractions containing a mixture of sulphated oligosaccharides was subsequently submitted to gel-filtration chromatography and h.p.l.c. Two sulphated oligosaccharide-alditols, A and B, were prepared; their structure was determined by means of 400 MHz 1H-n.m.r. spectroscopy and fast-atom-bombardment m.s.
2018475	5	12	theme	sulphated	597:605	arg1	B					639:639	B	639:639	B	639:639	One of these fractions containing a mixture of sulphated oligosaccharides was subsequently submitted to gel-filtration chromatography and h.p.l.c. Two sulphated oligosaccharide-alditols, A and B, were prepared; their structure was determined by means of 400 MHz 1H-n.m.r. spectroscopy and fast-atom-bombardment m.s.
2018475	5	12	theme	sulphated	597:605	arg1	A					633:633	A	633:633	A	633:633	One of these fractions containing a mixture of sulphated oligosaccharides was subsequently submitted to gel-filtration chromatography and h.p.l.c. Two sulphated oligosaccharide-alditols, A and B, were prepared; their structure was determined by means of 400 MHz 1H-n.m.r. spectroscopy and fast-atom-bombardment m.s.
2018475	5	12	theme	sulphated	597:605	arg1	oligosaccharide-alditols					607:630	h.p.l.c. Two sulphated oligosaccharide-alditols	584:630	h.p.l.c. Two sulphated oligosaccharide-alditols	584:630	One of these fractions containing a mixture of sulphated oligosaccharides was subsequently submitted to gel-filtration chromatography and h.p.l.c. Two sulphated oligosaccharide-alditols, A and B, were prepared; their structure was determined by means of 400 MHz 1H-n.m.r. spectroscopy and fast-atom-bombardment m.s.
2018475	1	13	dep	study	170:174	arg1	m.s.					137:140	m.s.	137:140	m.s.	137:140	A fast-atom-bombardment m.s. and 1H-n.m.r. spectroscopic study.
2018475	1	13	dep	study	170:174	arg1	1H-n.m.r.					146:154	1H-n.m.r.	146:154	1H-n.m.r.	146:154	A fast-atom-bombardment m.s. and 1H-n.m.r. spectroscopic study.
2018475	2	14	attach	isolated	220:227	arg1	sputum					238:243	the sputum	234:243	the sputum of a patient suffering from cystic fibrosis	234:287	Human respiratory-mucin glycopeptides were isolated from the sputum of a patient suffering from cystic fibrosis.
2018475	2	14	attach	isolated	220:227	arg2	glycopeptides					201:213	Human respiratory-mucin glycopeptides	177:213	Human respiratory-mucin glycopeptides	177:213	Human respiratory-mucin glycopeptides were isolated from the sputum of a patient suffering from cystic fibrosis.
2018475	6	15	contain	had	767:769	arg2	type					778:781	a core type 2	771:783	a core type 2	771:783	They had a core type 2 and the sulphate was 3-linked to a terminal galactose residue: (Formula; see text)
2018475	6	15	contain	had	767:769	arg1	They					762:765	They	762:765	They	762:765	They had a core type 2 and the sulphate was 3-linked to a terminal galactose residue: (Formula; see text)
2018475	0	16	theme	sulphated	17:25	arg1	oligosaccharides					27:42	two sulphated oligosaccharides	13:42	two sulphated oligosaccharides	13:42	Structure of two sulphated oligosaccharides from respiratory mucins of a patient suffering from cystic fibrosis.
2018475	5	17	theme	gel-filtration	550:563	arg1	chromatography					565:578	gel-filtration chromatography	550:578	gel-filtration chromatography	550:578	One of these fractions containing a mixture of sulphated oligosaccharides was subsequently submitted to gel-filtration chromatography and h.p.l.c. Two sulphated oligosaccharide-alditols, A and B, were prepared; their structure was determined by means of 400 MHz 1H-n.m.r. spectroscopy and fast-atom-bombardment m.s.
2018475	6	18	attach	3-linked	806:813	arg2	sulphate					793:800	the sulphate	789:800	the sulphate	789:800	They had a core type 2 and the sulphate was 3-linked to a terminal galactose residue: (Formula; see text)
2018475	6	18	attach	3-linked	806:813	arg1	residue					839:845	a terminal galactose residue:	818:846	a terminal galactose residue: (Formula; see text)	818:866	They had a core type 2 and the sulphate was 3-linked to a terminal galactose residue: (Formula; see text)
2018475	6	18	attach	3-linked	806:813	arg2	3-linked					806:813	3-linked	806:813	3-linked	806:813	They had a core type 2 and the sulphate was 3-linked to a terminal galactose residue: (Formula; see text)
2018475	6	19	theme	a	771:771	arg1	type					778:781	a core type 2	771:783	a core type 2	771:783	They had a core type 2 and the sulphate was 3-linked to a terminal galactose residue: (Formula; see text)
2018475	0	20	theme	oligosaccharides	27:42	arg1	Structure					0:8	Structure	0:8	Structure of two sulphated oligosaccharides from respiratory mucins of a patient suffering from cystic fibrosis.	0:111	Structure of two sulphated oligosaccharides from respiratory mucins of a patient suffering from cystic fibrosis.
2018475	2	21	theme	respiratory-mucin	183:199	arg1	glycopeptides					201:213	Human respiratory-mucin glycopeptides	177:213	Human respiratory-mucin glycopeptides	177:213	Human respiratory-mucin glycopeptides were isolated from the sputum of a patient suffering from cystic fibrosis.
2018475	2	22	theme	patient	250:256	arg1	sputum					238:243	the sputum	234:243	the sputum of a patient suffering from cystic fibrosis	234:287	Human respiratory-mucin glycopeptides were isolated from the sputum of a patient suffering from cystic fibrosis.
2018475	3	23	theme	alkaline	328:335	arg1	borohydride					337:347	alkaline borohydride	328:347	alkaline borohydride	328:347	They were subjected to treatment with alkaline borohydride.
2018475	2	24	theme	Human	177:181	arg1	glycopeptides					201:213	Human respiratory-mucin glycopeptides	177:213	Human respiratory-mucin glycopeptides	177:213	Human respiratory-mucin glycopeptides were isolated from the sputum of a patient suffering from cystic fibrosis.
2018475	4	25	theme	chromatography	378:391	arg1	Application					350:360	Application	350:360	Application of ion-exchange chromatography	350:391	Application of ion-exchange chromatography afforded carbohydrate fractions containing sulphate.
2018475	0	26	theme	respiratory	49:59	arg1	mucins					61:66	respiratory mucins	49:66	respiratory mucins of a patient suffering from cystic fibrosis	49:110	Structure of two sulphated oligosaccharides from respiratory mucins of a patient suffering from cystic fibrosis.
2018475	6	27	dep	see	858:860	arg1	Formula					849:855	Formula	849:855	Formula	849:855	They had a core type 2 and the sulphate was 3-linked to a terminal galactose residue: (Formula; see text)
2018475	6	28	theme	galactose	829:837	arg1	residue					839:845	a terminal galactose residue:	818:846	a terminal galactose residue: (Formula; see text)	818:866	They had a core type 2 and the sulphate was 3-linked to a terminal galactose residue: (Formula; see text)
2018475	4	29	contain	containing	425:434	arg2	sulphate					436:443	sulphate	436:443	sulphate	436:443	Application of ion-exchange chromatography afforded carbohydrate fractions containing sulphate.
2018475	4	29	contain	containing	425:434	arg1	fractions					415:423	carbohydrate fractions	402:423	carbohydrate fractions containing sulphate	402:443	Application of ion-exchange chromatography afforded carbohydrate fractions containing sulphate.
2018475	4	30	theme	carbohydrate	402:413	arg1	fractions					415:423	carbohydrate fractions	402:423	carbohydrate fractions containing sulphate	402:443	Application of ion-exchange chromatography afforded carbohydrate fractions containing sulphate.
2018475	6	31	theme	terminal	820:827	arg1	residue					839:845	a terminal galactose residue:	818:846	a terminal galactose residue: (Formula; see text)	818:866	They had a core type 2 and the sulphate was 3-linked to a terminal galactose residue: (Formula; see text)
2018475	6	32	theme	core	773:776	arg1	type					778:781	a core type 2	771:783	a core type 2	771:783	They had a core type 2 and the sulphate was 3-linked to a terminal galactose residue: (Formula; see text)
2018475	5	33	theme	oligosaccharides	503:518	arg1	mixture					482:488	a mixture	480:488	a mixture of sulphated oligosaccharides	480:518	One of these fractions containing a mixture of sulphated oligosaccharides was subsequently submitted to gel-filtration chromatography and h.p.l.c. Two sulphated oligosaccharide-alditols, A and B, were prepared; their structure was determined by means of 400 MHz 1H-n.m.r. spectroscopy and fast-atom-bombardment m.s.
2018475	6	34	dep	residue	839:845	arg1	see					858:860	see	858:860	see text	858:865	They had a core type 2 and the sulphate was 3-linked to a terminal galactose residue: (Formula; see text)
2018475	2	35	theme	cystic	273:278	arg1	fibrosis					280:287	cystic fibrosis	273:287	cystic fibrosis	273:287	Human respiratory-mucin glycopeptides were isolated from the sputum of a patient suffering from cystic fibrosis.
2018475	5	36	theme	fractions	459:467	arg1	One					446:448	One	446:448	One	446:448	One of these fractions containing a mixture of sulphated oligosaccharides was subsequently submitted to gel-filtration chromatography and h.p.l.c. Two sulphated oligosaccharide-alditols, A and B, were prepared; their structure was determined by means of 400 MHz 1H-n.m.r. spectroscopy and fast-atom-bombardment m.s.
2018475	5	36	theme	fractions	459:467	arg1	fractions					459:467	these fractions	453:467	these fractions containing a mixture of sulphated oligosaccharides	453:518	One of these fractions containing a mixture of sulphated oligosaccharides was subsequently submitted to gel-filtration chromatography and h.p.l.c. Two sulphated oligosaccharide-alditols, A and B, were prepared; their structure was determined by means of 400 MHz 1H-n.m.r. spectroscopy and fast-atom-bombardment m.s.
2018475	4	37	theme	ion-exchange	365:376	arg1	chromatography					378:391	ion-exchange chromatography	365:391	ion-exchange chromatography	365:391	Application of ion-exchange chromatography afforded carbohydrate fractions containing sulphate.
2018475	1	38	theme	spectroscopic	156:168	arg1	study					170:174	spectroscopic study	156:174	spectroscopic study	156:174	A fast-atom-bombardment m.s. and 1H-n.m.r. spectroscopic study.
2018475	2	39	gly	glycopeptides	201:213	arg2	glycopeptides					201:213	Human respiratory-mucin glycopeptides	177:213	Human respiratory-mucin glycopeptides	177:213	Human respiratory-mucin glycopeptides were isolated from the sputum of a patient suffering from cystic fibrosis.
8034632	0	0	from	sulfation	16:24	arg1	mucins					68:73	respiratory mucins	56:73	respiratory mucins from a patient with cystic fibrosis	56:109	Sialylation and sulfation of the carbohydrate chains in respiratory mucins from a patient with cystic fibrosis.
8034632	0	0	from	sulfation	16:24	arg1	patient					82:88	a patient	80:88	a patient with cystic fibrosis	80:109	Sialylation and sulfation of the carbohydrate chains in respiratory mucins from a patient with cystic fibrosis.
8034632	9	1	theme	X	1235:1235	arg1	A					1260:1260	the X determinant (Structure A)	1231:1261	the X determinant (Structure A)	1231:1261	The most complex structures contain sulfated derivatives of the H,X, or Y determinants or a sialylated and sulfated derivative of the X determinant (Structure A).
8034632	3	2	theme	ion-exchange	346:357	arg1	chromatography					359:372	ion-exchange chromatography	346:372	ion-exchange chromatography	346:372	Sialylated and sulfated oligosaccharide-alditols were purified by ion-exchange chromatography, gel filtration, and high performance anion-exchange chromatography.
8034632	4	3	theme	bombardment-mass	575:590	arg1	spectrometry					592:603	fast atom bombardment-mass spectrometry	565:603	fast atom bombardment-mass spectrometry	565:603	The structures of the oligosaccharide-alditols were determined by high resolution 1H NMR spectroscopy in combination with fast atom bombardment-mass spectrometry.
8034632	5	4	theme	mucins	741:746	arg1	chains					703:708	the carbohydrate chains	686:708	the carbohydrate chains of cystic fibrosis respiratory mucins	686:746	Twenty-four oligosaccharides were characterized and illustrate the diversity of the carbohydrate chains of cystic fibrosis respiratory mucins.
8034632	5	5	theme	carbohydrate	690:701	arg1	chains					703:708	the carbohydrate chains	686:708	the carbohydrate chains of cystic fibrosis respiratory mucins	686:746	Twenty-four oligosaccharides were characterized and illustrate the diversity of the carbohydrate chains of cystic fibrosis respiratory mucins.
8034632	9	6	contain	contain	1129:1135	arg1	structures					1118:1127	The most complex structures	1101:1127	The most complex structures	1101:1127	The most complex structures contain sulfated derivatives of the H,X, or Y determinants or a sialylated and sulfated derivative of the X determinant (Structure A).
8034632	9	6	contain	contain	1129:1135	arg2	derivatives					1146:1156	sulfated derivatives	1137:1156	sulfated derivatives of the H,X, or Y determinants	1137:1186	The most complex structures contain sulfated derivatives of the H,X, or Y determinants or a sialylated and sulfated derivative of the X determinant (Structure A).
8034632	9	6	contain	contain	1129:1135	arg2	derivative					1217:1226	a sialylated and sulfated derivative	1191:1226	a sialylated and sulfated derivative of the X determinant (Structure A)	1191:1261	The most complex structures contain sulfated derivatives of the H,X, or Y determinants or a sialylated and sulfated derivative of the X determinant (Structure A).
8034632	0	7	from	Sialylation	0:10	arg1	mucins					68:73	respiratory mucins	56:73	respiratory mucins from a patient with cystic fibrosis	56:109	Sialylation and sulfation of the carbohydrate chains in respiratory mucins from a patient with cystic fibrosis.
8034632	0	7	from	Sialylation	0:10	arg1	patient					82:88	a patient	80:88	a patient with cystic fibrosis	80:109	Sialylation and sulfation of the carbohydrate chains in respiratory mucins from a patient with cystic fibrosis.
8034632	5	8	theme	chains	703:708	arg1	diversity					673:681	the diversity	669:681	the diversity of the carbohydrate chains of cystic fibrosis respiratory mucins	669:746	Twenty-four oligosaccharides were characterized and illustrate the diversity of the carbohydrate chains of cystic fibrosis respiratory mucins.
8034632	7	9	from	linkage	914:920	arg1	C-3					968:970	C-3	968:970	C-3	968:970	Sialylation may occur on the C-6 of the N-acetylgalactosamine involved in the carbohydrate-peptide linkage or on a terminal galactose residue, either on C-3 or on C-6.
8034632	7	9	from	linkage	914:920	arg1	C-6					978:980	C-6	978:980	C-6	978:980	Sialylation may occur on the C-6 of the N-acetylgalactosamine involved in the carbohydrate-peptide linkage or on a terminal galactose residue, either on C-3 or on C-6.
8034632	7	9	from	linkage	914:920	arg1	residue					949:955	a terminal galactose residue	928:955	a terminal galactose residue	928:955	Sialylation may occur on the C-6 of the N-acetylgalactosamine involved in the carbohydrate-peptide linkage or on a terminal galactose residue, either on C-3 or on C-6.
8034632	9	10	theme	Structure	1250:1258	arg1	A					1260:1260	the X determinant (Structure A)	1231:1261	the X determinant (Structure A)	1231:1261	The most complex structures contain sulfated derivatives of the H,X, or Y determinants or a sialylated and sulfated derivative of the X determinant (Structure A).
8034632	9	11	theme	determinants	1175:1186	arg1	derivatives					1146:1156	sulfated derivatives	1137:1156	sulfated derivatives of the H,X, or Y determinants	1137:1186	The most complex structures contain sulfated derivatives of the H,X, or Y determinants or a sialylated and sulfated derivative of the X determinant (Structure A).
8034632	9	11	theme	determinants	1175:1186	arg1	derivative					1217:1226	a sialylated and sulfated derivative	1191:1226	a sialylated and sulfated derivative of the X determinant (Structure A)	1191:1261	The most complex structures contain sulfated derivatives of the H,X, or Y determinants or a sialylated and sulfated derivative of the X determinant (Structure A).
8034632	9	12	theme	H	1165:1165	arg1	determinants					1175:1186	the H,X, or Y determinants	1161:1186	the H,X, or Y determinants	1161:1186	The most complex structures contain sulfated derivatives of the H,X, or Y determinants or a sialylated and sulfated derivative of the X determinant (Structure A).
8034632	3	13	theme	gel	375:377	arg1	filtration					379:388	gel filtration	375:388	gel filtration	375:388	Sialylated and sulfated oligosaccharide-alditols were purified by ion-exchange chromatography, gel filtration, and high performance anion-exchange chromatography.
8034632	4	14	theme	NMR	528:530	arg1	spectroscopy					532:543	high resolution 1H NMR spectroscopy	509:543	high resolution 1H NMR spectroscopy in combination with fast atom bombardment-mass spectrometry	509:603	The structures of the oligosaccharide-alditols were determined by high resolution 1H NMR spectroscopy in combination with fast atom bombardment-mass spectrometry.
8034632	5	15	theme	fibrosis	720:727	arg1	mucins					741:746	cystic fibrosis respiratory mucins	713:746	cystic fibrosis respiratory mucins	713:746	Twenty-four oligosaccharides were characterized and illustrate the diversity of the carbohydrate chains of cystic fibrosis respiratory mucins.
8034632	5	16	theme	cystic	713:718	arg1	fibrosis					720:727	cystic fibrosis	713:727	cystic fibrosis respiratory mucins	713:746	Twenty-four oligosaccharides were characterized and illustrate the diversity of the carbohydrate chains of cystic fibrosis respiratory mucins.
8034632	9	17	theme	determinant	1237:1247	arg1	A					1260:1260	the X determinant (Structure A)	1231:1261	the X determinant (Structure A)	1231:1261	The most complex structures contain sulfated derivatives of the H,X, or Y determinants or a sialylated and sulfated derivative of the X determinant (Structure A).
8034632	0	18	theme	cystic	95:100	arg1	fibrosis					102:109	cystic fibrosis	95:109	cystic fibrosis	95:109	Sialylation and sulfation of the carbohydrate chains in respiratory mucins from a patient with cystic fibrosis.
8034632	5	19	theme	respiratory	729:739	arg1	mucins					741:746	cystic fibrosis respiratory mucins	713:746	cystic fibrosis respiratory mucins	713:746	Twenty-four oligosaccharides were characterized and illustrate the diversity of the carbohydrate chains of cystic fibrosis respiratory mucins.
8034632	8	20	theme	residue	1092:1098	arg1	C-6					1063:1065	the C-6	1059:1065	the C-6 of a N-acetylglucosamine residue	1059:1098	Sulfation may occur either on the C-3 of a terminal galactose residue or on the C-6 of a N-acetylglucosamine residue.
8034632	9	21	theme	X	1167:1167	arg1	determinants					1175:1186	the H,X, or Y determinants	1161:1186	the H,X, or Y determinants	1161:1186	The most complex structures contain sulfated derivatives of the H,X, or Y determinants or a sialylated and sulfated derivative of the X determinant (Structure A).
8034632	3	22	theme	anion-exchange	412:425	arg1	chromatography					427:440	high performance anion-exchange chromatography	395:440	high performance anion-exchange chromatography	395:440	Sialylated and sulfated oligosaccharide-alditols were purified by ion-exchange chromatography, gel filtration, and high performance anion-exchange chromatography.
8034632	4	23	from	spectroscopy	532:543	arg1	combination					548:558	combination	548:558	combination with fast atom bombardment-mass spectrometry	548:603	The structures of the oligosaccharide-alditols were determined by high resolution 1H NMR spectroscopy in combination with fast atom bombardment-mass spectrometry.
8034632	8	24	theme	N-acetylglucosamine	1072:1090	arg1	residue					1092:1098	a N-acetylglucosamine residue	1070:1098	a N-acetylglucosamine residue	1070:1098	Sulfation may occur either on the C-3 of a terminal galactose residue or on the C-6 of a N-acetylglucosamine residue.
8034632	1	25	theme	patient	167:173	arg1	sputum					155:160	the sputum	151:160	the sputum of a patient suffering from cystic fibrosis	151:204	Mucin glycopeptides were prepared from the sputum of a patient suffering from cystic fibrosis.
8034632	6	26	theme	novel	797:801	arg1	15					790:791	15	790:791	15	790:791	Among these 24 oligosaccharide-alditols, 15 are novel structures.
8034632	6	26	theme	novel	797:801	arg1	structures					803:812	novel structures	797:812	novel structures	797:812	Among these 24 oligosaccharide-alditols, 15 are novel structures.
8034632	3	27	theme	high	395:398	arg1	chromatography					427:440	high performance anion-exchange chromatography	395:440	high performance anion-exchange chromatography	395:440	Sialylated and sulfated oligosaccharide-alditols were purified by ion-exchange chromatography, gel filtration, and high performance anion-exchange chromatography.
8034632	7	28	theme	terminal	930:937	arg1	residue					949:955	a terminal galactose residue	928:955	a terminal galactose residue	928:955	Sialylation may occur on the C-6 of the N-acetylgalactosamine involved in the carbohydrate-peptide linkage or on a terminal galactose residue, either on C-3 or on C-6.
8034632	0	29	with	patient	82:88	arg1	fibrosis					102:109	cystic fibrosis	95:109	cystic fibrosis	95:109	Sialylation and sulfation of the carbohydrate chains in respiratory mucins from a patient with cystic fibrosis.
8034632	9	30	theme	Y	1173:1173	arg1	determinants					1175:1186	the H,X, or Y determinants	1161:1186	the H,X, or Y determinants	1161:1186	The most complex structures contain sulfated derivatives of the H,X, or Y determinants or a sialylated and sulfated derivative of the X determinant (Structure A).
8034632	3	31	theme	performance	400:410	arg1	chromatography					427:440	high performance anion-exchange chromatography	395:440	high performance anion-exchange chromatography	395:440	Sialylated and sulfated oligosaccharide-alditols were purified by ion-exchange chromatography, gel filtration, and high performance anion-exchange chromatography.
8034632	4	32	theme	high	509:512	arg1	spectroscopy					532:543	high resolution 1H NMR spectroscopy	509:543	high resolution 1H NMR spectroscopy in combination with fast atom bombardment-mass spectrometry	509:603	The structures of the oligosaccharide-alditols were determined by high resolution 1H NMR spectroscopy in combination with fast atom bombardment-mass spectrometry.
8034632	7	33	theme	galactose	939:947	arg1	residue					949:955	a terminal galactose residue	928:955	a terminal galactose residue	928:955	Sialylation may occur on the C-6 of the N-acetylgalactosamine involved in the carbohydrate-peptide linkage or on a terminal galactose residue, either on C-3 or on C-6.
8034632	1	34	theme	cystic	190:195	arg1	fibrosis					197:204	cystic fibrosis	190:204	cystic fibrosis	190:204	Mucin glycopeptides were prepared from the sputum of a patient suffering from cystic fibrosis.
8034632	0	35	theme	carbohydrate	33:44	arg1	chains					46:51	the carbohydrate chains	29:51	the carbohydrate chains	29:51	Sialylation and sulfation of the carbohydrate chains in respiratory mucins from a patient with cystic fibrosis.
8034632	7	36	theme	carbohydrate-peptide	893:912	arg1	linkage					914:920	the carbohydrate-peptide linkage	889:920	the carbohydrate-peptide linkage or on a terminal galactose residue, either on C-3 or on C-6	889:980	Sialylation may occur on the C-6 of the N-acetylgalactosamine involved in the carbohydrate-peptide linkage or on a terminal galactose residue, either on C-3 or on C-6.
8034632	1	37	gly	glycopeptides	118:130	arg2	glycopeptides					118:130	Mucin glycopeptides	112:130	Mucin glycopeptides	112:130	Mucin glycopeptides were prepared from the sputum of a patient suffering from cystic fibrosis.
8034632	4	38	theme	1H	525:526	arg1	spectroscopy					532:543	high resolution 1H NMR spectroscopy	509:543	high resolution 1H NMR spectroscopy in combination with fast atom bombardment-mass spectrometry	509:603	The structures of the oligosaccharide-alditols were determined by high resolution 1H NMR spectroscopy in combination with fast atom bombardment-mass spectrometry.
8034632	4	39	theme	resolution	514:523	arg1	spectroscopy					532:543	high resolution 1H NMR spectroscopy	509:543	high resolution 1H NMR spectroscopy in combination with fast atom bombardment-mass spectrometry	509:603	The structures of the oligosaccharide-alditols were determined by high resolution 1H NMR spectroscopy in combination with fast atom bombardment-mass spectrometry.
8034632	2	40	theme	carbohydrate	211:222	arg1	chains					224:229	The carbohydrate chains	207:229	The carbohydrate chains	207:229	The carbohydrate chains were released by alkaline borohydride treatment.
8034632	9	41	theme	sialylated	1193:1202	arg1	derivative					1217:1226	a sialylated and sulfated derivative	1191:1226	a sialylated and sulfated derivative of the X determinant (Structure A)	1191:1261	The most complex structures contain sulfated derivatives of the H,X, or Y determinants or a sialylated and sulfated derivative of the X determinant (Structure A).
8034632	0	42	theme	chains	46:51	arg1	sulfation					16:24	sulfation	16:24	sulfation	16:24	Sialylation and sulfation of the carbohydrate chains in respiratory mucins from a patient with cystic fibrosis.
8034632	0	42	theme	chains	46:51	arg1	Sialylation					0:10	Sialylation	0:10	Sialylation	0:10	Sialylation and sulfation of the carbohydrate chains in respiratory mucins from a patient with cystic fibrosis.
8034632	4	43	theme	oligosaccharide-alditols	465:488	arg1	structures					447:456	The structures	443:456	The structures of the oligosaccharide-alditols	443:488	The structures of the oligosaccharide-alditols were determined by high resolution 1H NMR spectroscopy in combination with fast atom bombardment-mass spectrometry.
8034632	8	44	theme	terminal	1026:1033	arg1	residue					1045:1051	a terminal galactose residue	1024:1051	a terminal galactose residue	1024:1051	Sulfation may occur either on the C-3 of a terminal galactose residue or on the C-6 of a N-acetylglucosamine residue.
8034632	1	45	theme	Mucin	112:116	arg1	glycopeptides					118:130	Mucin glycopeptides	112:130	Mucin glycopeptides	112:130	Mucin glycopeptides were prepared from the sputum of a patient suffering from cystic fibrosis.
8034632	9	46	theme	most	1105:1108	arg1	structures					1118:1127	The most complex structures	1101:1127	The most complex structures	1101:1127	The most complex structures contain sulfated derivatives of the H,X, or Y determinants or a sialylated and sulfated derivative of the X determinant (Structure A).
8034632	3	47	theme	sulfated	295:302	arg1	oligosaccharide-alditols					304:327	sulfated oligosaccharide-alditols	295:327	sulfated oligosaccharide-alditols	295:327	Sialylated and sulfated oligosaccharide-alditols were purified by ion-exchange chromatography, gel filtration, and high performance anion-exchange chromatography.
8034632	2	48	theme	borohydride	257:267	arg1	treatment					269:277	alkaline borohydride treatment	248:277	alkaline borohydride treatment	248:277	The carbohydrate chains were released by alkaline borohydride treatment.
8034632	9	49	theme	sulfated	1208:1215	arg1	derivative					1217:1226	a sialylated and sulfated derivative	1191:1226	a sialylated and sulfated derivative of the X determinant (Structure A)	1191:1261	The most complex structures contain sulfated derivatives of the H,X, or Y determinants or a sialylated and sulfated derivative of the X determinant (Structure A).
8034632	9	50	theme	complex	1110:1116	arg1	structures					1118:1127	The most complex structures	1101:1127	The most complex structures	1101:1127	The most complex structures contain sulfated derivatives of the H,X, or Y determinants or a sialylated and sulfated derivative of the X determinant (Structure A).
8034632	7	51	theme	N-acetylgalactosamine	855:875	arg1	C-6					844:846	the C-6	840:846	the C-6 of the N-acetylgalactosamine involved in the carbohydrate-peptide linkage or on a terminal galactose residue, either on C-3 or on C-6	840:980	Sialylation may occur on the C-6 of the N-acetylgalactosamine involved in the carbohydrate-peptide linkage or on a terminal galactose residue, either on C-3 or on C-6.
8034632	4	52	theme	atom	570:573	arg1	spectrometry					592:603	fast atom bombardment-mass spectrometry	565:603	fast atom bombardment-mass spectrometry	565:603	The structures of the oligosaccharide-alditols were determined by high resolution 1H NMR spectroscopy in combination with fast atom bombardment-mass spectrometry.
8034632	2	53	theme	alkaline	248:255	arg1	treatment					269:277	alkaline borohydride treatment	248:277	alkaline borohydride treatment	248:277	The carbohydrate chains were released by alkaline borohydride treatment.
8034632	8	54	theme	residue	1045:1051	arg1	C-3					1017:1019	the C-3	1013:1019	the C-3 of a terminal galactose residue	1013:1051	Sulfation may occur either on the C-3 of a terminal galactose residue or on the C-6 of a N-acetylglucosamine residue.
8034632	9	55	theme	A	1260:1260	arg1	derivatives					1146:1156	sulfated derivatives	1137:1156	sulfated derivatives of the H,X, or Y determinants	1137:1186	The most complex structures contain sulfated derivatives of the H,X, or Y determinants or a sialylated and sulfated derivative of the X determinant (Structure A).
8034632	9	55	theme	A	1260:1260	arg1	derivative					1217:1226	a sialylated and sulfated derivative	1191:1226	a sialylated and sulfated derivative of the X determinant (Structure A)	1191:1261	The most complex structures contain sulfated derivatives of the H,X, or Y determinants or a sialylated and sulfated derivative of the X determinant (Structure A).
8034632	9	56	gly	sialylated	1193:1202	arg1	derivative					1217:1226	a sialylated and sulfated derivative	1191:1226	a sialylated and sulfated derivative of the X determinant (Structure A)	1191:1261	The most complex structures contain sulfated derivatives of the H,X, or Y determinants or a sialylated and sulfated derivative of the X determinant (Structure A).
8034632	0	57	from	patient	82:88	arg1	sulfation					16:24	sulfation	16:24	sulfation	16:24	Sialylation and sulfation of the carbohydrate chains in respiratory mucins from a patient with cystic fibrosis.
8034632	0	57	from	patient	82:88	arg1	Sialylation					0:10	Sialylation	0:10	Sialylation	0:10	Sialylation and sulfation of the carbohydrate chains in respiratory mucins from a patient with cystic fibrosis.
8034632	0	57	from	patient	82:88	arg1	mucins					68:73	respiratory mucins	56:73	respiratory mucins from a patient with cystic fibrosis	56:109	Sialylation and sulfation of the carbohydrate chains in respiratory mucins from a patient with cystic fibrosis.
8034632	8	58	theme	galactose	1035:1043	arg1	residue					1045:1051	a terminal galactose residue	1024:1051	a terminal galactose residue	1024:1051	Sulfation may occur either on the C-3 of a terminal galactose residue or on the C-6 of a N-acetylglucosamine residue.
8034632	4	59	with	combination	548:558	arg1	spectrometry					592:603	fast atom bombardment-mass spectrometry	565:603	fast atom bombardment-mass spectrometry	565:603	The structures of the oligosaccharide-alditols were determined by high resolution 1H NMR spectroscopy in combination with fast atom bombardment-mass spectrometry.
8034632	0	60	theme	respiratory	56:66	arg1	mucins					68:73	respiratory mucins	56:73	respiratory mucins from a patient with cystic fibrosis	56:109	Sialylation and sulfation of the carbohydrate chains in respiratory mucins from a patient with cystic fibrosis.
8034632	4	61	theme	fast	565:568	arg1	spectrometry					592:603	fast atom bombardment-mass spectrometry	565:603	fast atom bombardment-mass spectrometry	565:603	The structures of the oligosaccharide-alditols were determined by high resolution 1H NMR spectroscopy in combination with fast atom bombardment-mass spectrometry.
8034632	9	62	theme	sulfated	1137:1144	arg1	derivatives					1146:1156	sulfated derivatives	1137:1156	sulfated derivatives of the H,X, or Y determinants	1137:1186	The most complex structures contain sulfated derivatives of the H,X, or Y determinants or a sialylated and sulfated derivative of the X determinant (Structure A).
7592613	7	0	gly	fucosylated	1365:1375	arg1	lacdiNAc					1377:1384	fucosylated lacdiNAc	1365:1384	fucosylated lacdiNAc antennae	1365:1393	Oligosaccharides with fucosylated lacdiNAc antennae have previously been shown to potently block selectin-mediated adhesions and may perform the same function in glycodelin.
7592613	7	1	from	function	1493:1500	arg1	glycodelin					1505:1514	glycodelin	1505:1514	glycodelin	1505:1514	Oligosaccharides with fucosylated lacdiNAc antennae have previously been shown to potently block selectin-mediated adhesions and may perform the same function in glycodelin.
7592613	0	2	with	glycoprotein	77:88	arg1	contraceptive					124:136	contraceptive	124:136	contraceptive	124:136	Structural analysis of the oligosaccharides derived from glycodelin, a human glycoprotein with potent immunosuppressive and contraceptive activities.
7592613	0	2	with	glycoprotein	77:88	arg1	immunosuppressive					102:118	immunosuppressive	102:118	immunosuppressive	102:118	Structural analysis of the oligosaccharides derived from glycodelin, a human glycoprotein with potent immunosuppressive and contraceptive activities.
7592613	8	3	theme	selectin-like	1690:1702	arg1	process					1713:1719	a selectin-like adhesion process	1688:1719	a selectin-like adhesion process	1688:1719	The potent inhibitory effect of glycodelin on initial human sperm-zona pellucida binding is consistent with our previous suggestion that this cell adhesion event requires a selectin-like adhesion process.
7592613	7	4	theme	selectin-mediated	1440:1456	arg1	adhesions					1458:1466	selectin-mediated adhesions	1440:1466	selectin-mediated adhesions	1440:1466	Oligosaccharides with fucosylated lacdiNAc antennae have previously been shown to potently block selectin-mediated adhesions and may perform the same function in glycodelin.
7592613	5	5	theme	beta	841:844	arg1	lacdiNAc					857:864	lacdiNAc	857:864	lacdiNAc	857:864	The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	5	5	theme	beta	841:844	arg1	1-4GlcNAc					846:854	GalNAc beta 1-4GlcNAc	834:854	GalNAc beta 1-4GlcNAc (lacdiNAc)	834:865	The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	5	6	theme	2-6Gal	880:885	arg1	lacNAc					914:919	sialylated lacNAc	903:919	sialylated lacNAc	903:919	The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	5	6	theme	2-6Gal	880:885	arg1	1-4GlcNAc					892:900	NeuAc alpha 2-6Gal beta 1-4GlcNAc	868:900	NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc)	868:920	The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	7	7	theme	lacdiNAc	1377:1384	arg1	antennae					1386:1393	fucosylated lacdiNAc antennae	1365:1393	fucosylated lacdiNAc antennae	1365:1393	Oligosaccharides with fucosylated lacdiNAc antennae have previously been shown to potently block selectin-mediated adhesions and may perform the same function in glycodelin.
7592613	4	8	contain	carries	609:615	arg2	hybrid					631:636	hybrid	631:636	hybrid	631:636	The Asn-28 site carries high mannose, hybrid and complex-type structures, whereas the second site is exclusively occupied by complex-type glycans.
7592613	4	8	contain	carries	609:615	arg2	structures					655:664	complex-type structures	642:664	complex-type structures	642:664	The Asn-28 site carries high mannose, hybrid and complex-type structures, whereas the second site is exclusively occupied by complex-type glycans.
7592613	4	8	contain	carries	609:615	arg1	site					604:607	The Asn-28 site	593:607	The Asn-28 site	593:607	The Asn-28 site carries high mannose, hybrid and complex-type structures, whereas the second site is exclusively occupied by complex-type glycans.
7592613	4	8	contain	carries	609:615	arg2	mannose					622:628	high mannose	617:628	high mannose	617:628	The Asn-28 site carries high mannose, hybrid and complex-type structures, whereas the second site is exclusively occupied by complex-type glycans.
7592613	1	9	with	glycoprotein	270:281	arg1	activities					331:340	potent immunosuppressive and contraceptive activities	288:340	potent immunosuppressive and contraceptive activities	288:340	Glycodelin, also known as placental protein 14 (PP14) or progesterone-associated endometrial protein (PAEP), is a human glycoprotein with potent immunosuppressive and contraceptive activities.
7592613	5	10	theme	non-reducing	750:761	arg1	epitopes					763:770	The major non-reducing epitopes	740:770	The major non-reducing epitopes in the complex-type glycans	740:798	The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	5	10	theme	non-reducing	750:761	arg1	1-4GlcNAc					814:822	Gal beta 1-4GlcNAc	805:822	Gal beta 1-4GlcNAc (lacNAc)	805:831	The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	1	11	theme	progesterone-associated	207:229	arg1	PAEP					252:255	PAEP	252:255	PAEP	252:255	Glycodelin, also known as placental protein 14 (PP14) or progesterone-associated endometrial protein (PAEP), is a human glycoprotein with potent immunosuppressive and contraceptive activities.
7592613	1	11	theme	progesterone-associated	207:229	arg1	protein					243:249	progesterone-associated endometrial protein	207:249	progesterone-associated endometrial protein (PAEP)	207:256	Glycodelin, also known as placental protein 14 (PP14) or progesterone-associated endometrial protein (PAEP), is a human glycoprotein with potent immunosuppressive and contraceptive activities.
7592613	5	12	theme	beta	1035:1038	arg1	GlcNAc					1058:1063	GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc	1028:1063	GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx)	1028:1093	The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	1	13	gly	glycoprotein	270:281	arg1	Glycodelin					150:159	Glycodelin	150:159	Glycodelin	150:159	Glycodelin, also known as placental protein 14 (PP14) or progesterone-associated endometrial protein (PAEP), is a human glycoprotein with potent immunosuppressive and contraceptive activities.
7592613	1	13	gly	glycoprotein	270:281	arg1	glycoprotein					270:281	a human glycoprotein	262:281	a human glycoprotein with potent immunosuppressive and contraceptive activities	262:340	Glycodelin, also known as placental protein 14 (PP14) or progesterone-associated endometrial protein (PAEP), is a human glycoprotein with potent immunosuppressive and contraceptive activities.
7592613	5	14	theme	NeuAc	868:872	arg1	lacNAc					914:919	sialylated lacNAc	903:919	sialylated lacNAc	903:919	The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	5	14	theme	NeuAc	868:872	arg1	1-4GlcNAc					892:900	NeuAc alpha 2-6Gal beta 1-4GlcNAc	868:900	NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc)	868:920	The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	5	15	gly	sialylated	903:912	arg1	lacNAc					914:919	sialylated lacNAc	903:919	sialylated lacNAc	903:919	The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	5	15	gly	sialylated	903:912	arg1	1-4GlcNAc					892:900	NeuAc alpha 2-6Gal beta 1-4GlcNAc	868:900	NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc)	868:920	The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	6	16	theme	activation-related	1261:1278	arg1	events					1280:1285	adhesive and activation-related events	1248:1285	events	1280:1285	It is possible that the oligosaccharides bearing sialylated lacNAc or lacdiNAc antennae may manifest immunosuppressive effects by specifically blocking adhesive and activation-related events mediated by CD22, the human B cell associated receptor.
7592613	5	17	theme	NeuAc	923:927	arg1	1-4GlcNAc					947:955	NeuAc alpha 2-6Gal beta 1-4GlcNAc	923:955	NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc)	923:977	The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	5	17	theme	NeuAc	923:927	arg1	lacdiNAc					969:976	sialylated lacdiNAc	958:976	sialylated lacdiNAc	958:976	The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	6	18	theme	adhesive	1248:1255	arg1	events					1280:1285	adhesive and activation-related events	1248:1285	events	1280:1285	It is possible that the oligosaccharides bearing sialylated lacNAc or lacdiNAc antennae may manifest immunosuppressive effects by specifically blocking adhesive and activation-related events mediated by CD22, the human B cell associated receptor.
7592613	5	19	theme	2-6Gal	935:940	arg1	1-4GlcNAc					947:955	NeuAc alpha 2-6Gal beta 1-4GlcNAc	923:955	NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc)	923:977	The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	5	19	theme	2-6Gal	935:940	arg1	lacdiNAc					969:976	sialylated lacdiNAc	958:976	sialylated lacdiNAc	958:976	The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	6	20	dep	lacNAc	1156:1161	arg1	antennae					1175:1182	antennae	1175:1182	antennae	1175:1182	It is possible that the oligosaccharides bearing sialylated lacNAc or lacdiNAc antennae may manifest immunosuppressive effects by specifically blocking adhesive and activation-related events mediated by CD22, the human B cell associated receptor.
7592613	5	21	theme	Gal	805:807	arg1	epitopes					763:770	The major non-reducing epitopes	740:770	The major non-reducing epitopes in the complex-type glycans	740:798	The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	5	21	theme	Gal	805:807	arg1	lacNAc					825:830	lacNAc	825:830	lacNAc	825:830	The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	5	21	theme	Gal	805:807	arg1	1-4GlcNAc					814:822	Gal beta 1-4GlcNAc	805:822	Gal beta 1-4GlcNAc (lacNAc)	805:831	The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	8	22	dep	suggestion	1638:1647	arg1	requires					1679:1686	requires	1679:1686	requires a selectin-like adhesion process	1679:1719	The potent inhibitory effect of glycodelin on initial human sperm-zona pellucida binding is consistent with our previous suggestion that this cell adhesion event requires a selectin-like adhesion process.
7592613	5	23	theme	sialylated	903:912	arg1	lacNAc					914:919	sialylated lacNAc	903:919	sialylated lacNAc	903:919	The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	5	23	theme	sialylated	903:912	arg1	1-4GlcNAc					892:900	NeuAc alpha 2-6Gal beta 1-4GlcNAc	868:900	NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc)	868:920	The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	0	24	theme	human	71:75	arg1	glycoprotein					77:88	a human glycoprotein	69:88	a human glycoprotein with potent immunosuppressive and contraceptive activities	69:147	Structural analysis of the oligosaccharides derived from glycodelin, a human glycoprotein with potent immunosuppressive and contraceptive activities.
7592613	0	24	theme	human	71:75	arg1	glycodelin					57:66	glycodelin	57:66	glycodelin	57:66	Structural analysis of the oligosaccharides derived from glycodelin, a human glycoprotein with potent immunosuppressive and contraceptive activities.
7592613	5	25	theme	complex-type	779:790	arg1	glycans					792:798	the complex-type glycans	775:798	the complex-type glycans	775:798	The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	4	26	dep	carries	609:615	arg1	whereas					667:673	whereas	667:673	whereas	667:673	The Asn-28 site carries high mannose, hybrid and complex-type structures, whereas the second site is exclusively occupied by complex-type glycans.
7592613	0	27	dep	immunosuppressive	102:118	arg1	activities					138:147	activities	138:147	activities	138:147	Structural analysis of the oligosaccharides derived from glycodelin, a human glycoprotein with potent immunosuppressive and contraceptive activities.
7592613	5	28	gly	sialylated	958:967	arg1	1-4GlcNAc					947:955	NeuAc alpha 2-6Gal beta 1-4GlcNAc	923:955	NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc)	923:977	The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	5	28	gly	sialylated	958:967	arg1	lacdiNAc					969:976	sialylated lacdiNAc	958:976	sialylated lacdiNAc	958:976	The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	2	29	theme	oligosaccharides	416:431	arg1	characterization					377:392	the first characterization	367:392	the first characterization of glycodelin-derived oligosaccharides	367:431	In this paper we report the first characterization of glycodelin-derived oligosaccharides.
7592613	7	30	with	Oligosaccharides	1343:1358	arg1	antennae					1386:1393	fucosylated lacdiNAc antennae	1365:1393	fucosylated lacdiNAc antennae	1365:1393	Oligosaccharides with fucosylated lacdiNAc antennae have previously been shown to potently block selectin-mediated adhesions and may perform the same function in glycodelin.
7592613	0	31	gly	glycoprotein	77:88	arg1	glycoprotein					77:88	a human glycoprotein	69:88	a human glycoprotein with potent immunosuppressive and contraceptive activities	69:147	Structural analysis of the oligosaccharides derived from glycodelin, a human glycoprotein with potent immunosuppressive and contraceptive activities.
7592613	0	31	gly	glycoprotein	77:88	arg1	glycodelin					57:66	glycodelin	57:66	glycodelin	57:66	Structural analysis of the oligosaccharides derived from glycodelin, a human glycoprotein with potent immunosuppressive and contraceptive activities.
7592613	9	32	theme	recognition	1807:1817	arg1	processes					1819:1827	immune and gamete recognition processes	1789:1827	immune and gamete recognition processes	1789:1827	This result also raises the possibility that a convergence between immune and gamete recognition processes may have occurred in the types of carbohydrate ligands recognized in the human.
7592613	0	33	theme	Structural	0:9	arg1	analysis					11:18	Structural analysis	0:18	Structural analysis of the oligosaccharides	0:42	Structural analysis of the oligosaccharides derived from glycodelin, a human glycoprotein with potent immunosuppressive and contraceptive activities.
7592613	1	34	theme	human	264:268	arg1	Glycodelin					150:159	Glycodelin	150:159	Glycodelin	150:159	Glycodelin, also known as placental protein 14 (PP14) or progesterone-associated endometrial protein (PAEP), is a human glycoprotein with potent immunosuppressive and contraceptive activities.
7592613	1	34	theme	human	264:268	arg1	glycoprotein					270:281	a human glycoprotein	262:281	a human glycoprotein with potent immunosuppressive and contraceptive activities	262:340	Glycodelin, also known as placental protein 14 (PP14) or progesterone-associated endometrial protein (PAEP), is a human glycoprotein with potent immunosuppressive and contraceptive activities.
7592613	8	35	theme	inhibitory	1528:1537	arg1	consistent					1609:1618	consistent	1609:1618	consistent	1609:1618	The potent inhibitory effect of glycodelin on initial human sperm-zona pellucida binding is consistent with our previous suggestion that this cell adhesion event requires a selectin-like adhesion process.
7592613	8	35	theme	inhibitory	1528:1537	arg1	effect					1539:1544	The potent inhibitory effect	1517:1544	The potent inhibitory effect of glycodelin on initial human sperm-zona pellucida binding	1517:1604	The potent inhibitory effect of glycodelin on initial human sperm-zona pellucida binding is consistent with our previous suggestion that this cell adhesion event requires a selectin-like adhesion process.
7592613	3	36	theme	mass	501:504	arg1	spectrometry					506:517	electrospray mass spectrometry	488:517	electrospray mass spectrometry	488:517	Using strategies based upon fast atom bombardment and electrospray mass spectrometry we have established that glycodelin is glycosylated at Asn-28 and Asn-63.
7592613	5	37	theme	sialylated	958:967	arg1	1-4GlcNAc					947:955	NeuAc alpha 2-6Gal beta 1-4GlcNAc	923:955	NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc)	923:977	The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	5	37	theme	sialylated	958:967	arg1	lacdiNAc					969:976	sialylated lacdiNAc	958:976	sialylated lacdiNAc	958:976	The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	5	38	dep	GlcNAc	1058:1063	arg1	analogue					1075:1082	lacdiNAc analogue	1066:1082	lacdiNAc analogue of Lewisx	1066:1092	The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	1	39	theme	placental	176:184	arg1	protein					186:192	placental protein 14	176:195	placental protein 14 (PP14)	176:202	Glycodelin, also known as placental protein 14 (PP14) or progesterone-associated endometrial protein (PAEP), is a human glycoprotein with potent immunosuppressive and contraceptive activities.
7592613	1	39	theme	placental	176:184	arg1	PP14					198:201	PP14	198:201	PP14	198:201	Glycodelin, also known as placental protein 14 (PP14) or progesterone-associated endometrial protein (PAEP), is a human glycoprotein with potent immunosuppressive and contraceptive activities.
7592613	1	40	theme	immunosuppressive	295:311	arg1	activities					331:340	potent immunosuppressive and contraceptive activities	288:340	potent immunosuppressive and contraceptive activities	288:340	Glycodelin, also known as placental protein 14 (PP14) or progesterone-associated endometrial protein (PAEP), is a human glycoprotein with potent immunosuppressive and contraceptive activities.
7592613	0	41	theme	oligosaccharides	27:42	arg1	analysis					11:18	Structural analysis	0:18	Structural analysis of the oligosaccharides	0:42	Structural analysis of the oligosaccharides derived from glycodelin, a human glycoprotein with potent immunosuppressive and contraceptive activities.
7592613	2	42	link	glycodelin-derived	397:414	arg1	oligosaccharides					416:431	glycodelin-derived oligosaccharides	397:431	glycodelin-derived oligosaccharides	397:431	In this paper we report the first characterization of glycodelin-derived oligosaccharides.
7592613	5	43	theme	Lewisx	1087:1092	arg1	analogue					1075:1082	lacdiNAc analogue	1066:1082	lacdiNAc analogue of Lewisx	1066:1092	The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	8	44	theme	human	1571:1575	arg1	binding					1598:1604	initial human sperm-zona pellucida binding	1563:1604	initial human sperm-zona pellucida binding	1563:1604	The potent inhibitory effect of glycodelin on initial human sperm-zona pellucida binding is consistent with our previous suggestion that this cell adhesion event requires a selectin-like adhesion process.
7592613	1	45	theme	endometrial	231:241	arg1	PAEP					252:255	PAEP	252:255	PAEP	252:255	Glycodelin, also known as placental protein 14 (PP14) or progesterone-associated endometrial protein (PAEP), is a human glycoprotein with potent immunosuppressive and contraceptive activities.
7592613	1	45	theme	endometrial	231:241	arg1	protein					243:249	progesterone-associated endometrial protein	207:249	progesterone-associated endometrial protein (PAEP)	207:256	Glycodelin, also known as placental protein 14 (PP14) or progesterone-associated endometrial protein (PAEP), is a human glycoprotein with potent immunosuppressive and contraceptive activities.
7592613	9	46	theme	ligands	1876:1882	arg1	types					1854:1858	the types	1850:1858	the types of carbohydrate ligands recognized in the human	1850:1906	This result also raises the possibility that a convergence between immune and gamete recognition processes may have occurred in the types of carbohydrate ligands recognized in the human.
7592613	8	47	theme	pellucida	1588:1596	arg1	binding					1598:1604	initial human sperm-zona pellucida binding	1563:1604	initial human sperm-zona pellucida binding	1563:1604	The potent inhibitory effect of glycodelin on initial human sperm-zona pellucida binding is consistent with our previous suggestion that this cell adhesion event requires a selectin-like adhesion process.
7592613	2	48	theme	first	371:375	arg1	characterization					377:392	the first characterization	367:392	the first characterization of glycodelin-derived oligosaccharides	367:431	In this paper we report the first characterization of glycodelin-derived oligosaccharides.
7592613	8	49	theme	cell	1659:1662	arg1	event					1673:1677	this cell adhesion event	1654:1677	this cell adhesion event	1654:1677	The potent inhibitory effect of glycodelin on initial human sperm-zona pellucida binding is consistent with our previous suggestion that this cell adhesion event requires a selectin-like adhesion process.
7592613	5	50	theme	Fuc	993:995	arg1	beta					984:987	Gal beta 1-4	980:991	Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx)	980:1021	The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	5	50	theme	Fuc	993:995	arg1	alpha					997:1001	Fuc alpha 1-3	993:1005	Fuc alpha 1-3	993:1005	The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	5	51	from	epitopes	763:770	arg1	glycans					792:798	the complex-type glycans	775:798	the complex-type glycans	775:798	The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	4	52	theme	high	617:620	arg1	mannose					622:628	high mannose	617:628	high mannose	617:628	The Asn-28 site carries high mannose, hybrid and complex-type structures, whereas the second site is exclusively occupied by complex-type glycans.
7592613	8	53	from	effect	1539:1544	arg1	binding					1598:1604	initial human sperm-zona pellucida binding	1563:1604	initial human sperm-zona pellucida binding	1563:1604	The potent inhibitory effect of glycodelin on initial human sperm-zona pellucida binding is consistent with our previous suggestion that this cell adhesion event requires a selectin-like adhesion process.
7592613	8	54	with	consistent	1609:1618	arg1	suggestion					1638:1647	our previous suggestion	1625:1647	our previous suggestion that this cell adhesion event requires a selectin-like adhesion process	1625:1719	The potent inhibitory effect of glycodelin on initial human sperm-zona pellucida binding is consistent with our previous suggestion that this cell adhesion event requires a selectin-like adhesion process.
7592613	8	55	theme	previous	1629:1636	arg1	suggestion					1638:1647	our previous suggestion	1625:1647	our previous suggestion that this cell adhesion event requires a selectin-like adhesion process	1625:1719	The potent inhibitory effect of glycodelin on initial human sperm-zona pellucida binding is consistent with our previous suggestion that this cell adhesion event requires a selectin-like adhesion process.
7592613	6	56	gly	sialylated	1145:1154	arg1	lacNAc					1156:1161	lacNAc	1156:1161	lacNAc	1156:1161	It is possible that the oligosaccharides bearing sialylated lacNAc or lacdiNAc antennae may manifest immunosuppressive effects by specifically blocking adhesive and activation-related events mediated by CD22, the human B cell associated receptor.
7592613	6	57	theme	immunosuppressive	1197:1213	arg1	effects					1215:1221	immunosuppressive effects	1197:1221	immunosuppressive effects	1197:1221	It is possible that the oligosaccharides bearing sialylated lacNAc or lacdiNAc antennae may manifest immunosuppressive effects by specifically blocking adhesive and activation-related events mediated by CD22, the human B cell associated receptor.
7592613	8	58	theme	adhesion	1704:1711	arg1	process					1713:1719	a selectin-like adhesion process	1688:1719	a selectin-like adhesion process	1688:1719	The potent inhibitory effect of glycodelin on initial human sperm-zona pellucida binding is consistent with our previous suggestion that this cell adhesion event requires a selectin-like adhesion process.
7592613	5	59	theme	alpha	874:878	arg1	lacNAc					914:919	sialylated lacNAc	903:919	sialylated lacNAc	903:919	The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	5	59	theme	alpha	874:878	arg1	1-4GlcNAc					892:900	NeuAc alpha 2-6Gal beta 1-4GlcNAc	868:900	NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc)	868:920	The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	1	60	theme	contraceptive	317:329	arg1	activities					331:340	potent immunosuppressive and contraceptive activities	288:340	potent immunosuppressive and contraceptive activities	288:340	Glycodelin, also known as placental protein 14 (PP14) or progesterone-associated endometrial protein (PAEP), is a human glycoprotein with potent immunosuppressive and contraceptive activities.
7592613	6	61	theme	associated	1322:1331	arg1	receptor					1333:1340	the human B cell associated receptor	1305:1340	the human B cell associated receptor	1305:1340	It is possible that the oligosaccharides bearing sialylated lacNAc or lacdiNAc antennae may manifest immunosuppressive effects by specifically blocking adhesive and activation-related events mediated by CD22, the human B cell associated receptor.
7592613	6	61	theme	associated	1322:1331	arg1	CD22					1299:1302	CD22	1299:1302	CD22	1299:1302	It is possible that the oligosaccharides bearing sialylated lacNAc or lacdiNAc antennae may manifest immunosuppressive effects by specifically blocking adhesive and activation-related events mediated by CD22, the human B cell associated receptor.
7592613	5	62	theme	beta	887:890	arg1	lacNAc					914:919	sialylated lacNAc	903:919	sialylated lacNAc	903:919	The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	5	62	theme	beta	887:890	arg1	1-4GlcNAc					892:900	NeuAc alpha 2-6Gal beta 1-4GlcNAc	868:900	NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc)	868:920	The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	5	63	theme	major	744:748	arg1	epitopes					763:770	The major non-reducing epitopes	740:770	The major non-reducing epitopes in the complex-type glycans	740:798	The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	5	63	theme	major	744:748	arg1	1-4GlcNAc					814:822	Gal beta 1-4GlcNAc	805:822	Gal beta 1-4GlcNAc (lacNAc)	805:831	The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	7	64	theme	fucosylated	1365:1375	arg1	lacdiNAc					1377:1384	fucosylated lacdiNAc	1365:1384	fucosylated lacdiNAc antennae	1365:1393	Oligosaccharides with fucosylated lacdiNAc antennae have previously been shown to potently block selectin-mediated adhesions and may perform the same function in glycodelin.
7592613	5	65	theme	GalNAc	1028:1033	arg1	alpha					1048:1052	Fuc alpha 1-3	1044:1056	Fuc alpha 1-3	1044:1056	The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	5	65	theme	GalNAc	1028:1033	arg1	beta					1035:1038	GalNAc beta 1-4	1028:1042	GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx)	1028:1093	The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	4	66	theme	second	679:684	arg1	site					686:689	the second site	675:689	the second site	675:689	The Asn-28 site carries high mannose, hybrid and complex-type structures, whereas the second site is exclusively occupied by complex-type glycans.
7592613	6	67	theme	sialylated	1145:1154	arg1	lacNAc					1156:1161	lacNAc	1156:1161	lacNAc	1156:1161	It is possible that the oligosaccharides bearing sialylated lacNAc or lacdiNAc antennae may manifest immunosuppressive effects by specifically blocking adhesive and activation-related events mediated by CD22, the human B cell associated receptor.
7592613	5	68	theme	alpha	929:933	arg1	1-4GlcNAc					947:955	NeuAc alpha 2-6Gal beta 1-4GlcNAc	923:955	NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc)	923:977	The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	5	68	theme	alpha	929:933	arg1	lacdiNAc					969:976	sialylated lacdiNAc	958:976	sialylated lacdiNAc	958:976	The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	4	69	theme	complex-type	718:729	arg1	glycans					731:737	complex-type glycans	718:737	complex-type glycans	718:737	The Asn-28 site carries high mannose, hybrid and complex-type structures, whereas the second site is exclusively occupied by complex-type glycans.
7592613	6	70	theme	B	1315:1315	arg1	receptor					1333:1340	the human B cell associated receptor	1305:1340	the human B cell associated receptor	1305:1340	It is possible that the oligosaccharides bearing sialylated lacNAc or lacdiNAc antennae may manifest immunosuppressive effects by specifically blocking adhesive and activation-related events mediated by CD22, the human B cell associated receptor.
7592613	6	70	theme	B	1315:1315	arg1	CD22					1299:1302	CD22	1299:1302	CD22	1299:1302	It is possible that the oligosaccharides bearing sialylated lacNAc or lacdiNAc antennae may manifest immunosuppressive effects by specifically blocking adhesive and activation-related events mediated by CD22, the human B cell associated receptor.
7592613	5	71	theme	beta	809:812	arg1	epitopes					763:770	The major non-reducing epitopes	740:770	The major non-reducing epitopes in the complex-type glycans	740:798	The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	5	71	theme	beta	809:812	arg1	lacNAc					825:830	lacNAc	825:830	lacNAc	825:830	The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	5	71	theme	beta	809:812	arg1	1-4GlcNAc					814:822	Gal beta 1-4GlcNAc	805:822	Gal beta 1-4GlcNAc (lacNAc)	805:831	The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	6	72	theme	cell	1317:1320	arg1	receptor					1333:1340	the human B cell associated receptor	1305:1340	the human B cell associated receptor	1305:1340	It is possible that the oligosaccharides bearing sialylated lacNAc or lacdiNAc antennae may manifest immunosuppressive effects by specifically blocking adhesive and activation-related events mediated by CD22, the human B cell associated receptor.
7592613	6	72	theme	cell	1317:1320	arg1	CD22					1299:1302	CD22	1299:1302	CD22	1299:1302	It is possible that the oligosaccharides bearing sialylated lacNAc or lacdiNAc antennae may manifest immunosuppressive effects by specifically blocking adhesive and activation-related events mediated by CD22, the human B cell associated receptor.
7592613	5	73	theme	lacdiNAc	1066:1073	arg1	analogue					1075:1082	lacdiNAc analogue	1066:1082	lacdiNAc analogue of Lewisx	1066:1092	The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	9	74	theme	immune	1789:1794	arg1	processes					1819:1827	immune and gamete recognition processes	1789:1827	immune and gamete recognition processes	1789:1827	This result also raises the possibility that a convergence between immune and gamete recognition processes may have occurred in the types of carbohydrate ligands recognized in the human.
7592613	3	75	gly	glycosylated	558:569	arg2	Asn-28					574:579	Asn-28	574:579	Asn-28	574:579	Using strategies based upon fast atom bombardment and electrospray mass spectrometry we have established that glycodelin is glycosylated at Asn-28 and Asn-63.
7592613	3	75	gly	glycosylated	558:569	arg1	glycodelin					544:553	glycodelin	544:553	glycodelin	544:553	Using strategies based upon fast atom bombardment and electrospray mass spectrometry we have established that glycodelin is glycosylated at Asn-28 and Asn-63.
7592613	3	75	gly	glycosylated	558:569	arg2	Asn-63					585:590	Asn-63	585:590	Asn-63	585:590	Using strategies based upon fast atom bombardment and electrospray mass spectrometry we have established that glycodelin is glycosylated at Asn-28 and Asn-63.
7592613	6	76	theme	human	1309:1313	arg1	receptor					1333:1340	the human B cell associated receptor	1305:1340	the human B cell associated receptor	1305:1340	It is possible that the oligosaccharides bearing sialylated lacNAc or lacdiNAc antennae may manifest immunosuppressive effects by specifically blocking adhesive and activation-related events mediated by CD22, the human B cell associated receptor.
7592613	6	76	theme	human	1309:1313	arg1	CD22					1299:1302	CD22	1299:1302	CD22	1299:1302	It is possible that the oligosaccharides bearing sialylated lacNAc or lacdiNAc antennae may manifest immunosuppressive effects by specifically blocking adhesive and activation-related events mediated by CD22, the human B cell associated receptor.
7592613	5	77	theme	Fuc	1044:1046	arg1	alpha					1048:1052	Fuc alpha 1-3	1044:1056	Fuc alpha 1-3	1044:1056	The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	5	77	theme	Fuc	1044:1046	arg1	beta					1035:1038	GalNAc beta 1-4	1028:1042	GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx)	1028:1093	The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	3	78	dep	established	527:537	arg1	Using					434:438	Using	434:438	Using strategies based upon fast atom bombardment and electrospray mass spectrometry	434:517	Using strategies based upon fast atom bombardment and electrospray mass spectrometry we have established that glycodelin is glycosylated at Asn-28 and Asn-63.
7592613	9	79	theme	gamete	1800:1805	arg1	processes					1819:1827	immune and gamete recognition processes	1789:1827	immune and gamete recognition processes	1789:1827	This result also raises the possibility that a convergence between immune and gamete recognition processes may have occurred in the types of carbohydrate ligands recognized in the human.
7592613	8	80	theme	potent	1521:1526	arg1	consistent					1609:1618	consistent	1609:1618	consistent	1609:1618	The potent inhibitory effect of glycodelin on initial human sperm-zona pellucida binding is consistent with our previous suggestion that this cell adhesion event requires a selectin-like adhesion process.
7592613	8	80	theme	potent	1521:1526	arg1	effect					1539:1544	The potent inhibitory effect	1517:1544	The potent inhibitory effect of glycodelin on initial human sperm-zona pellucida binding	1517:1604	The potent inhibitory effect of glycodelin on initial human sperm-zona pellucida binding is consistent with our previous suggestion that this cell adhesion event requires a selectin-like adhesion process.
7592613	2	81	theme	glycodelin-derived	397:414	arg1	oligosaccharides					416:431	glycodelin-derived oligosaccharides	397:431	glycodelin-derived oligosaccharides	397:431	In this paper we report the first characterization of glycodelin-derived oligosaccharides.
7592613	5	82	theme	GalNAc	834:839	arg1	lacdiNAc					857:864	lacdiNAc	857:864	lacdiNAc	857:864	The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	5	82	theme	GalNAc	834:839	arg1	1-4GlcNAc					846:854	GalNAc beta 1-4GlcNAc	834:854	GalNAc beta 1-4GlcNAc (lacdiNAc)	834:865	The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	5	83	theme	beta	942:945	arg1	1-4GlcNAc					947:955	NeuAc alpha 2-6Gal beta 1-4GlcNAc	923:955	NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc)	923:977	The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	5	83	theme	beta	942:945	arg1	lacdiNAc					969:976	sialylated lacdiNAc	958:976	sialylated lacdiNAc	958:976	The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	3	84	theme	fast	462:465	arg1	bombardment					472:482	fast atom bombardment	462:482	fast atom bombardment	462:482	Using strategies based upon fast atom bombardment and electrospray mass spectrometry we have established that glycodelin is glycosylated at Asn-28 and Asn-63.
7592613	8	85	theme	glycodelin	1549:1558	arg1	consistent					1609:1618	consistent	1609:1618	consistent	1609:1618	The potent inhibitory effect of glycodelin on initial human sperm-zona pellucida binding is consistent with our previous suggestion that this cell adhesion event requires a selectin-like adhesion process.
7592613	8	85	theme	glycodelin	1549:1558	arg1	effect					1539:1544	The potent inhibitory effect	1517:1544	The potent inhibitory effect of glycodelin on initial human sperm-zona pellucida binding	1517:1604	The potent inhibitory effect of glycodelin on initial human sperm-zona pellucida binding is consistent with our previous suggestion that this cell adhesion event requires a selectin-like adhesion process.
7592613	1	86	theme	potent	288:293	arg1	activities					331:340	potent immunosuppressive and contraceptive activities	288:340	potent immunosuppressive and contraceptive activities	288:340	Glycodelin, also known as placental protein 14 (PP14) or progesterone-associated endometrial protein (PAEP), is a human glycoprotein with potent immunosuppressive and contraceptive activities.
7592613	3	87	theme	atom	467:470	arg1	bombardment					472:482	fast atom bombardment	462:482	fast atom bombardment	462:482	Using strategies based upon fast atom bombardment and electrospray mass spectrometry we have established that glycodelin is glycosylated at Asn-28 and Asn-63.
7592613	8	88	theme	initial	1563:1569	arg1	binding					1598:1604	initial human sperm-zona pellucida binding	1563:1604	initial human sperm-zona pellucida binding	1563:1604	The potent inhibitory effect of glycodelin on initial human sperm-zona pellucida binding is consistent with our previous suggestion that this cell adhesion event requires a selectin-like adhesion process.
7592613	3	89	theme	electrospray	488:499	arg1	spectrometry					506:517	electrospray mass spectrometry	488:517	electrospray mass spectrometry	488:517	Using strategies based upon fast atom bombardment and electrospray mass spectrometry we have established that glycodelin is glycosylated at Asn-28 and Asn-63.
7592613	8	90	theme	sperm-zona	1577:1586	arg1	binding					1598:1604	initial human sperm-zona pellucida binding	1563:1604	initial human sperm-zona pellucida binding	1563:1604	The potent inhibitory effect of glycodelin on initial human sperm-zona pellucida binding is consistent with our previous suggestion that this cell adhesion event requires a selectin-like adhesion process.
7592613	5	91	theme	beta	984:987	arg1	Lewisx					1015:1020	Lewisx	1015:1020	Lewisx	1015:1020	The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	5	91	theme	beta	984:987	arg1	GlcNAc					1007:1012	Gal beta 1-4(Fuc alpha 1-3)GlcNAc	980:1012	Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx)	980:1021	The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	9	92	theme	carbohydrate	1863:1874	arg1	ligands					1876:1882	carbohydrate ligands	1863:1882	carbohydrate ligands recognized in the human	1863:1906	This result also raises the possibility that a convergence between immune and gamete recognition processes may have occurred in the types of carbohydrate ligands recognized in the human.
7592613	4	93	theme	complex-type	642:653	arg1	structures					655:664	complex-type structures	642:664	complex-type structures	642:664	The Asn-28 site carries high mannose, hybrid and complex-type structures, whereas the second site is exclusively occupied by complex-type glycans.
7592613	5	94	theme	Gal	980:982	arg1	beta					984:987	Gal beta 1-4	980:991	Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx)	980:1021	The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	5	94	theme	Gal	980:982	arg1	alpha					997:1001	Fuc alpha 1-3	993:1005	Fuc alpha 1-3	993:1005	The major non-reducing epitopes in the complex-type glycans are: Gal beta 1-4GlcNAc (lacNAc), GalNAc beta 1-4GlcNAc (lacdiNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacNAc), NeuAc alpha 2-6Gal beta 1-4GlcNAc (sialylated lacdiNAc), Gal beta 1-4(Fuc alpha 1-3)GlcNAc (Lewisx), and GalNAc beta 1-4(Fuc alpha 1-3)GlcNAc (lacdiNAc analogue of Lewisx).
7592613	4	95	used	occupied	706:713	arg2	site					686:689	the second site	675:689	the second site	675:689	The Asn-28 site carries high mannose, hybrid and complex-type structures, whereas the second site is exclusively occupied by complex-type glycans.
7592613	8	96	theme	adhesion	1664:1671	arg1	event					1673:1677	this cell adhesion event	1654:1677	this cell adhesion event	1654:1677	The potent inhibitory effect of glycodelin on initial human sperm-zona pellucida binding is consistent with our previous suggestion that this cell adhesion event requires a selectin-like adhesion process.
7592613	7	97	theme	same	1488:1491	arg1	function					1493:1500	the same function	1484:1500	the same function in glycodelin	1484:1514	Oligosaccharides with fucosylated lacdiNAc antennae have previously been shown to potently block selectin-mediated adhesions and may perform the same function in glycodelin.
1730617	6	0	theme	Chromatographic	894:908	arg1	analyses					910:917	Chromatographic analyses	894:917	Chromatographic analyses of the beta-elimination products	894:950	Chromatographic analyses of the beta-elimination products and fast atom bombardment-mass spectrometry of [3H]Gal-labeled tryptic peptides confirm the saccharide structure.
1730617	4	1	from	man	684:686	arg1	homogenates					667:677	lens homogenates	662:677	lens homogenates from man, rhesus monkey, rat, cow, and rhea (an ostrich-like bird)	662:744	An in vitro enzymatic assay that transfers [3H]Gal to terminal GlcNAc moieties labels alpha A and alpha B crystallins in lens homogenates from man, rhesus monkey, rat, cow, and rhea (an ostrich-like bird).
1730617	9	2	theme	major	1430:1434	arg1	peptide					1457:1463	the major radiolabeled tryptic peptide	1426:1463	the major radiolabeled tryptic peptide from bovine alpha-crystallin	1426:1492	Gas-phase protein sequencing and fast atom bombardment-mass spectrometry of the major radiolabeled tryptic peptide from bovine alpha-crystallin reveal that GlcNAc is attached to the alpha A subunits at serine 162.
1730617	2	3	from	role	356:359	arg1	lens					368:371	the lens	364:371	the lens	364:371	Yet many of these highly conserved proteins are also expressed in nonocular tissues, where they have alternative functions apparently unrelated to their structural role in the lens.
1730617	4	4	theme	terminal	595:602	arg1	moieties					611:618	terminal GlcNAc moieties	595:618	terminal GlcNAc moieties	595:618	An in vitro enzymatic assay that transfers [3H]Gal to terminal GlcNAc moieties labels alpha A and alpha B crystallins in lens homogenates from man, rhesus monkey, rat, cow, and rhea (an ostrich-like bird).
1730617	9	5	theme	tryptic	1449:1455	arg1	peptide					1457:1463	the major radiolabeled tryptic peptide	1426:1463	the major radiolabeled tryptic peptide from bovine alpha-crystallin	1426:1492	Gas-phase protein sequencing and fast atom bombardment-mass spectrometry of the major radiolabeled tryptic peptide from bovine alpha-crystallin reveal that GlcNAc is attached to the alpha A subunits at serine 162.
1730617	8	6	theme	Electrospray	1219:1230	arg1	spectrometry					1237:1248	Electrospray mass spectrometry	1219:1248	Electrospray mass spectrometry of bovine alpha-crystallin	1219:1275	Electrospray mass spectrometry of bovine alpha-crystallin demonstrates the presence of a single O-GlcNAc substitution on alpha A2.
1730617	7	7	theme	lens	1113:1116	arg1	proteins					1118:1125	[3H]Gal-labeled bovine lens proteins	1090:1125	[3H]Gal-labeled bovine lens proteins	1090:1125	Isoelectric focusing of [3H]Gal-labeled bovine lens proteins reveals the presence of O-GlcNAc on all four alpha-crystallin subunits, A1, A2, B1, and B2.
1730617	5	8	theme	saccharide	764:773	arg1	O-Linkage					747:755	O-Linkage	747:755	O-Linkage of the saccharide	747:773	O-Linkage of the saccharide is demonstrated by sensitivity to base-catalyzed beta-elimination and resistance to peptide:N-glycosidase F treatment.
1730617	0	9	link	O-linked	50:57	arg1	N-acetylglucosamine					59:77	O-linked N-acetylglucosamine	50:77	O-linked N-acetylglucosamine	50:77	Vertebrate lens alpha-crystallins are modified by O-linked N-acetylglucosamine.
1730617	7	10	theme	Gal-labeled	1094:1104	arg1	proteins					1118:1125	[3H]Gal-labeled bovine lens proteins	1090:1125	[3H]Gal-labeled bovine lens proteins	1090:1125	Isoelectric focusing of [3H]Gal-labeled bovine lens proteins reveals the presence of O-GlcNAc on all four alpha-crystallin subunits, A1, A2, B1, and B2.
1730617	6	11	theme	atom	961:964	arg1	spectrometry					983:994	fast atom bombardment-mass spectrometry	956:994	fast atom bombardment-mass spectrometry of [3H]Gal-labeled tryptic peptides	956:1030	Chromatographic analyses of the beta-elimination products and fast atom bombardment-mass spectrometry of [3H]Gal-labeled tryptic peptides confirm the saccharide structure.
1730617	8	12	theme	bovine	1253:1258	arg1	alpha-crystallin					1260:1275	bovine alpha-crystallin	1253:1275	bovine alpha-crystallin	1253:1275	Electrospray mass spectrometry of bovine alpha-crystallin demonstrates the presence of a single O-GlcNAc substitution on alpha A2.
1730617	10	13	theme	important	1613:1621	arg1	role					1623:1626	an important role	1610:1626	an important role	1610:1626	This post-translational modification may play an important role in the molecular organization of lens alpha-crystallin.
1730617	8	14	attach	presence	1294:1301	arg2	substitution					1324:1335	a single O-GlcNAc substitution	1306:1335	a single O-GlcNAc substitution	1306:1335	Electrospray mass spectrometry of bovine alpha-crystallin demonstrates the presence of a single O-GlcNAc substitution on alpha A2.
1730617	8	14	attach	presence	1294:1301	arg1	A2					1346:1347	alpha A2	1340:1347	alpha A2	1340:1347	Electrospray mass spectrometry of bovine alpha-crystallin demonstrates the presence of a single O-GlcNAc substitution on alpha A2.
1730617	2	15	theme	unrelated	326:334	arg1	functions					305:313	alternative functions	293:313	alternative functions apparently unrelated to their structural role in the lens	293:371	Yet many of these highly conserved proteins are also expressed in nonocular tissues, where they have alternative functions apparently unrelated to their structural role in the lens.
1730617	3	16	mod	modified	486:493	arg1	alpha-crystallins					399:415	lens alpha-crystallins	394:415	lens alpha-crystallins	394:415	Here we report that lens alpha-crystallins, some of which function as heat-shock proteins in other tissues, are modified with O-linked N-acetylglucosamine (O-GlcNAc).
1730617	3	16	mod	modified	486:493	arg3	N-acetylglucosamine					509:527	O-linked N-acetylglucosamine	500:527	O-linked N-acetylglucosamine (O-GlcNAc)	500:538	Here we report that lens alpha-crystallins, some of which function as heat-shock proteins in other tissues, are modified with O-linked N-acetylglucosamine (O-GlcNAc).
1730617	3	16	mod	modified	486:493	arg3	O-GlcNAc					530:537	O-GlcNAc	530:537	O-GlcNAc	530:537	Here we report that lens alpha-crystallins, some of which function as heat-shock proteins in other tissues, are modified with O-linked N-acetylglucosamine (O-GlcNAc).
1730617	10	17	theme	alpha-crystallin	1666:1681	arg1	organization					1645:1656	the molecular organization	1631:1656	the molecular organization of lens alpha-crystallin	1631:1681	This post-translational modification may play an important role in the molecular organization of lens alpha-crystallin.
1730617	4	18	theme	B	645:645	arg1	crystallins					647:657	alpha A and alpha B crystallins	627:657	alpha A and alpha B crystallins	627:657	An in vitro enzymatic assay that transfers [3H]Gal to terminal GlcNAc moieties labels alpha A and alpha B crystallins in lens homogenates from man, rhesus monkey, rat, cow, and rhea (an ostrich-like bird).
1730617	5	19	theme	base-catalyzed	809:822	arg1	beta-elimination					824:839	base-catalyzed beta-elimination	809:839	base-catalyzed beta-elimination	809:839	O-Linkage of the saccharide is demonstrated by sensitivity to base-catalyzed beta-elimination and resistance to peptide:N-glycosidase F treatment.
1730617	6	20	theme	beta-elimination	926:941	arg1	products					943:950	the beta-elimination products	922:950	the beta-elimination products	922:950	Chromatographic analyses of the beta-elimination products and fast atom bombardment-mass spectrometry of [3H]Gal-labeled tryptic peptides confirm the saccharide structure.
1730617	10	21	theme	molecular	1635:1643	arg1	organization					1645:1656	the molecular organization	1631:1656	the molecular organization of lens alpha-crystallin	1631:1681	This post-translational modification may play an important role in the molecular organization of lens alpha-crystallin.
1730617	1	22	theme	remarkable	149:158	arg1	properties					168:177	the remarkable optical properties	145:177	the remarkable optical properties of the lens	145:189	Crystallins are structural proteins responsible for establishing the remarkable optical properties of the lens.
1730617	3	23	link	O-linked	500:507	arg1	O-GlcNAc					530:537	O-GlcNAc	530:537	O-GlcNAc	530:537	Here we report that lens alpha-crystallins, some of which function as heat-shock proteins in other tissues, are modified with O-linked N-acetylglucosamine (O-GlcNAc).
1730617	3	23	link	O-linked	500:507	arg1	N-acetylglucosamine					509:527	O-linked N-acetylglucosamine	500:527	O-linked N-acetylglucosamine (O-GlcNAc)	500:538	Here we report that lens alpha-crystallins, some of which function as heat-shock proteins in other tissues, are modified with O-linked N-acetylglucosamine (O-GlcNAc).
1730617	9	24	from	serine	1552:1557	arg1	subunits					1540:1547	the alpha A subunits	1528:1547	the alpha A subunits at serine 162	1528:1561	Gas-phase protein sequencing and fast atom bombardment-mass spectrometry of the major radiolabeled tryptic peptide from bovine alpha-crystallin reveal that GlcNAc is attached to the alpha A subunits at serine 162.
1730617	9	25	theme	alpha	1532:1536	arg1	subunits					1540:1547	the alpha A subunits	1528:1547	the alpha A subunits at serine 162	1528:1561	Gas-phase protein sequencing and fast atom bombardment-mass spectrometry of the major radiolabeled tryptic peptide from bovine alpha-crystallin reveal that GlcNAc is attached to the alpha A subunits at serine 162.
1730617	6	26	theme	peptides	1023:1030	arg1	spectrometry					983:994	fast atom bombardment-mass spectrometry	956:994	fast atom bombardment-mass spectrometry of [3H]Gal-labeled tryptic peptides	956:1030	Chromatographic analyses of the beta-elimination products and fast atom bombardment-mass spectrometry of [3H]Gal-labeled tryptic peptides confirm the saccharide structure.
1730617	6	26	theme	peptides	1023:1030	arg1	analyses					910:917	Chromatographic analyses	894:917	Chromatographic analyses of the beta-elimination products	894:950	Chromatographic analyses of the beta-elimination products and fast atom bombardment-mass spectrometry of [3H]Gal-labeled tryptic peptides confirm the saccharide structure.
1730617	8	27	theme	O-GlcNAc	1315:1322	arg1	substitution					1324:1335	a single O-GlcNAc substitution	1306:1335	a single O-GlcNAc substitution	1306:1335	Electrospray mass spectrometry of bovine alpha-crystallin demonstrates the presence of a single O-GlcNAc substitution on alpha A2.
1730617	6	28	theme	Gal-labeled	1003:1013	arg1	peptides					1023:1030	[3H]Gal-labeled tryptic peptides	999:1030	[3H]Gal-labeled tryptic peptides	999:1030	Chromatographic analyses of the beta-elimination products and fast atom bombardment-mass spectrometry of [3H]Gal-labeled tryptic peptides confirm the saccharide structure.
1730617	4	29	theme	rhesus	689:694	arg1	monkey					696:701	rhesus monkey	689:701	rhesus monkey	689:701	An in vitro enzymatic assay that transfers [3H]Gal to terminal GlcNAc moieties labels alpha A and alpha B crystallins in lens homogenates from man, rhesus monkey, rat, cow, and rhea (an ostrich-like bird).
1730617	4	30	dep	in	544:545	arg1	vitro					547:551	vitro	547:551	vitro	547:551	An in vitro enzymatic assay that transfers [3H]Gal to terminal GlcNAc moieties labels alpha A and alpha B crystallins in lens homogenates from man, rhesus monkey, rat, cow, and rhea (an ostrich-like bird).
1730617	5	31	theme	F	881:881	arg1	treatment					883:891	peptide:N-glycosidase F treatment	859:891	peptide:N-glycosidase F treatment	859:891	O-Linkage of the saccharide is demonstrated by sensitivity to base-catalyzed beta-elimination and resistance to peptide:N-glycosidase F treatment.
1730617	9	32	from	sequencing	1368:1377	arg1	alpha-crystallin					1477:1492	bovine alpha-crystallin	1470:1492	bovine alpha-crystallin	1470:1492	Gas-phase protein sequencing and fast atom bombardment-mass spectrometry of the major radiolabeled tryptic peptide from bovine alpha-crystallin reveal that GlcNAc is attached to the alpha A subunits at serine 162.
1730617	8	33	from	presence	1294:1301	arg1	A2					1346:1347	alpha A2	1340:1347	alpha A2	1340:1347	Electrospray mass spectrometry of bovine alpha-crystallin demonstrates the presence of a single O-GlcNAc substitution on alpha A2.
1730617	4	34	from	rhea	718:721	arg1	homogenates					667:677	lens homogenates	662:677	lens homogenates from man, rhesus monkey, rat, cow, and rhea (an ostrich-like bird)	662:744	An in vitro enzymatic assay that transfers [3H]Gal to terminal GlcNAc moieties labels alpha A and alpha B crystallins in lens homogenates from man, rhesus monkey, rat, cow, and rhea (an ostrich-like bird).
1730617	1	35	theme	structural	96:105	arg1	Crystallins					80:90	Crystallins	80:90	Crystallins	80:90	Crystallins are structural proteins responsible for establishing the remarkable optical properties of the lens.
1730617	1	35	theme	structural	96:105	arg1	proteins					107:114	structural proteins	96:114	structural proteins responsible for establishing the remarkable optical properties of the lens	96:189	Crystallins are structural proteins responsible for establishing the remarkable optical properties of the lens.
1730617	0	36	theme	Vertebrate	0:9	arg1	alpha-crystallins					16:32	Vertebrate lens alpha-crystallins	0:32	Vertebrate lens alpha-crystallins	0:32	Vertebrate lens alpha-crystallins are modified by O-linked N-acetylglucosamine.
1730617	2	37	contain	have	288:291	arg2	functions					305:313	alternative functions	293:313	alternative functions apparently unrelated to their structural role in the lens	293:371	Yet many of these highly conserved proteins are also expressed in nonocular tissues, where they have alternative functions apparently unrelated to their structural role in the lens.
1730617	2	37	contain	have	288:291	arg1	they					283:286	they	283:286	they	283:286	Yet many of these highly conserved proteins are also expressed in nonocular tissues, where they have alternative functions apparently unrelated to their structural role in the lens.
1730617	1	38	theme	responsible	116:126	arg1	Crystallins					80:90	Crystallins	80:90	Crystallins	80:90	Crystallins are structural proteins responsible for establishing the remarkable optical properties of the lens.
1730617	1	38	theme	responsible	116:126	arg1	proteins					107:114	structural proteins	96:114	structural proteins responsible for establishing the remarkable optical properties of the lens	96:189	Crystallins are structural proteins responsible for establishing the remarkable optical properties of the lens.
1730617	7	39	theme	alpha-crystallin	1172:1187	arg1	A2					1203:1204	A2	1203:1204	A2	1203:1204	Isoelectric focusing of [3H]Gal-labeled bovine lens proteins reveals the presence of O-GlcNAc on all four alpha-crystallin subunits, A1, A2, B1, and B2.
1730617	7	39	theme	alpha-crystallin	1172:1187	arg1	A1					1199:1200	A1	1199:1200	A1	1199:1200	Isoelectric focusing of [3H]Gal-labeled bovine lens proteins reveals the presence of O-GlcNAc on all four alpha-crystallin subunits, A1, A2, B1, and B2.
1730617	7	39	theme	alpha-crystallin	1172:1187	arg1	subunits					1189:1196	all four alpha-crystallin subunits	1163:1196	all four alpha-crystallin subunits	1163:1196	Isoelectric focusing of [3H]Gal-labeled bovine lens proteins reveals the presence of O-GlcNAc on all four alpha-crystallin subunits, A1, A2, B1, and B2.
1730617	7	39	theme	alpha-crystallin	1172:1187	arg1	B1					1207:1208	B1	1207:1208	B1	1207:1208	Isoelectric focusing of [3H]Gal-labeled bovine lens proteins reveals the presence of O-GlcNAc on all four alpha-crystallin subunits, A1, A2, B1, and B2.
1730617	7	39	theme	alpha-crystallin	1172:1187	arg1	B2					1215:1216	B2	1215:1216	B2	1215:1216	Isoelectric focusing of [3H]Gal-labeled bovine lens proteins reveals the presence of O-GlcNAc on all four alpha-crystallin subunits, A1, A2, B1, and B2.
1730617	5	40	theme	peptide	859:865	arg1	F					881:881	peptide:N-glycosidase F	859:881	peptide:N-glycosidase F treatment	859:891	O-Linkage of the saccharide is demonstrated by sensitivity to base-catalyzed beta-elimination and resistance to peptide:N-glycosidase F treatment.
1730617	3	41	theme	other	467:471	arg1	tissues					473:479	other tissues	467:479	other tissues	467:479	Here we report that lens alpha-crystallins, some of which function as heat-shock proteins in other tissues, are modified with O-linked N-acetylglucosamine (O-GlcNAc).
1730617	9	42	theme	protein	1360:1366	arg1	sequencing					1368:1377	Gas-phase protein sequencing	1350:1377	Gas-phase protein sequencing	1350:1377	Gas-phase protein sequencing and fast atom bombardment-mass spectrometry of the major radiolabeled tryptic peptide from bovine alpha-crystallin reveal that GlcNAc is attached to the alpha A subunits at serine 162.
1730617	3	43	theme	O-linked	500:507	arg1	O-GlcNAc					530:537	O-GlcNAc	530:537	O-GlcNAc	530:537	Here we report that lens alpha-crystallins, some of which function as heat-shock proteins in other tissues, are modified with O-linked N-acetylglucosamine (O-GlcNAc).
1730617	3	43	theme	O-linked	500:507	arg1	N-acetylglucosamine					509:527	O-linked N-acetylglucosamine	500:527	O-linked N-acetylglucosamine (O-GlcNAc)	500:538	Here we report that lens alpha-crystallins, some of which function as heat-shock proteins in other tissues, are modified with O-linked N-acetylglucosamine (O-GlcNAc).
1730617	7	44	theme	O-GlcNAc	1151:1158	arg1	presence					1139:1146	the presence	1135:1146	the presence of O-GlcNAc on all four alpha-crystallin subunits, A1, A2, B1, and B2	1135:1216	Isoelectric focusing of [3H]Gal-labeled bovine lens proteins reveals the presence of O-GlcNAc on all four alpha-crystallin subunits, A1, A2, B1, and B2.
1730617	7	45	from	presence	1139:1146	arg1	A2					1203:1204	A2	1203:1204	A2	1203:1204	Isoelectric focusing of [3H]Gal-labeled bovine lens proteins reveals the presence of O-GlcNAc on all four alpha-crystallin subunits, A1, A2, B1, and B2.
1730617	7	45	from	presence	1139:1146	arg1	A1					1199:1200	A1	1199:1200	A1	1199:1200	Isoelectric focusing of [3H]Gal-labeled bovine lens proteins reveals the presence of O-GlcNAc on all four alpha-crystallin subunits, A1, A2, B1, and B2.
1730617	7	45	from	presence	1139:1146	arg1	subunits					1189:1196	all four alpha-crystallin subunits	1163:1196	all four alpha-crystallin subunits	1163:1196	Isoelectric focusing of [3H]Gal-labeled bovine lens proteins reveals the presence of O-GlcNAc on all four alpha-crystallin subunits, A1, A2, B1, and B2.
1730617	7	45	from	presence	1139:1146	arg1	B1					1207:1208	B1	1207:1208	B1	1207:1208	Isoelectric focusing of [3H]Gal-labeled bovine lens proteins reveals the presence of O-GlcNAc on all four alpha-crystallin subunits, A1, A2, B1, and B2.
1730617	7	45	from	presence	1139:1146	arg1	B2					1215:1216	B2	1215:1216	B2	1215:1216	Isoelectric focusing of [3H]Gal-labeled bovine lens proteins reveals the presence of O-GlcNAc on all four alpha-crystallin subunits, A1, A2, B1, and B2.
1730617	2	46	theme	proteins	227:234	arg1	proteins					227:234	these highly conserved proteins	204:234	these highly conserved proteins	204:234	Yet many of these highly conserved proteins are also expressed in nonocular tissues, where they have alternative functions apparently unrelated to their structural role in the lens.
1730617	2	46	theme	proteins	227:234	arg1	many					196:199	many	196:199	many	196:199	Yet many of these highly conserved proteins are also expressed in nonocular tissues, where they have alternative functions apparently unrelated to their structural role in the lens.
1730617	4	47	from	rat	704:706	arg1	homogenates					667:677	lens homogenates	662:677	lens homogenates from man, rhesus monkey, rat, cow, and rhea (an ostrich-like bird)	662:744	An in vitro enzymatic assay that transfers [3H]Gal to terminal GlcNAc moieties labels alpha A and alpha B crystallins in lens homogenates from man, rhesus monkey, rat, cow, and rhea (an ostrich-like bird).
1730617	9	48	theme	atom	1388:1391	arg1	spectrometry					1410:1421	fast atom bombardment-mass spectrometry	1383:1421	fast atom bombardment-mass spectrometry	1383:1421	Gas-phase protein sequencing and fast atom bombardment-mass spectrometry of the major radiolabeled tryptic peptide from bovine alpha-crystallin reveal that GlcNAc is attached to the alpha A subunits at serine 162.
1730617	4	49	theme	GlcNAc	604:609	arg1	moieties					611:618	terminal GlcNAc moieties	595:618	terminal GlcNAc moieties	595:618	An in vitro enzymatic assay that transfers [3H]Gal to terminal GlcNAc moieties labels alpha A and alpha B crystallins in lens homogenates from man, rhesus monkey, rat, cow, and rhea (an ostrich-like bird).
1730617	10	50	theme	post-translational	1569:1586	arg1	modification					1588:1599	This post-translational modification	1564:1599	This post-translational modification	1564:1599	This post-translational modification may play an important role in the molecular organization of lens alpha-crystallin.
1730617	4	51	from	monkey	696:701	arg1	homogenates					667:677	lens homogenates	662:677	lens homogenates from man, rhesus monkey, rat, cow, and rhea (an ostrich-like bird)	662:744	An in vitro enzymatic assay that transfers [3H]Gal to terminal GlcNAc moieties labels alpha A and alpha B crystallins in lens homogenates from man, rhesus monkey, rat, cow, and rhea (an ostrich-like bird).
1730617	7	52	attach	presence	1139:1146	arg1	A2					1203:1204	A2	1203:1204	A2	1203:1204	Isoelectric focusing of [3H]Gal-labeled bovine lens proteins reveals the presence of O-GlcNAc on all four alpha-crystallin subunits, A1, A2, B1, and B2.
1730617	7	52	attach	presence	1139:1146	arg2	O-GlcNAc					1151:1158	O-GlcNAc	1151:1158	O-GlcNAc	1151:1158	Isoelectric focusing of [3H]Gal-labeled bovine lens proteins reveals the presence of O-GlcNAc on all four alpha-crystallin subunits, A1, A2, B1, and B2.
1730617	7	52	attach	presence	1139:1146	arg1	subunits					1189:1196	all four alpha-crystallin subunits	1163:1196	all four alpha-crystallin subunits	1163:1196	Isoelectric focusing of [3H]Gal-labeled bovine lens proteins reveals the presence of O-GlcNAc on all four alpha-crystallin subunits, A1, A2, B1, and B2.
1730617	7	52	attach	presence	1139:1146	arg1	B1					1207:1208	B1	1207:1208	B1	1207:1208	Isoelectric focusing of [3H]Gal-labeled bovine lens proteins reveals the presence of O-GlcNAc on all four alpha-crystallin subunits, A1, A2, B1, and B2.
1730617	7	52	attach	presence	1139:1146	arg1	B2					1215:1216	B2	1215:1216	B2	1215:1216	Isoelectric focusing of [3H]Gal-labeled bovine lens proteins reveals the presence of O-GlcNAc on all four alpha-crystallin subunits, A1, A2, B1, and B2.
1730617	7	52	attach	presence	1139:1146	arg1	A1					1199:1200	A1	1199:1200	A1	1199:1200	Isoelectric focusing of [3H]Gal-labeled bovine lens proteins reveals the presence of O-GlcNAc on all four alpha-crystallin subunits, A1, A2, B1, and B2.
1730617	7	53	theme	proteins	1118:1125	arg1	Isoelectric					1066:1076	Isoelectric	1066:1076	Isoelectric	1066:1076	Isoelectric focusing of [3H]Gal-labeled bovine lens proteins reveals the presence of O-GlcNAc on all four alpha-crystallin subunits, A1, A2, B1, and B2.
1730617	9	54	theme	radiolabeled	1436:1447	arg1	peptide					1457:1463	the major radiolabeled tryptic peptide	1426:1463	the major radiolabeled tryptic peptide from bovine alpha-crystallin	1426:1492	Gas-phase protein sequencing and fast atom bombardment-mass spectrometry of the major radiolabeled tryptic peptide from bovine alpha-crystallin reveal that GlcNAc is attached to the alpha A subunits at serine 162.
1730617	5	55	theme	N-glycosidase	867:879	arg1	F					881:881	peptide:N-glycosidase F	859:881	peptide:N-glycosidase F treatment	859:891	O-Linkage of the saccharide is demonstrated by sensitivity to base-catalyzed beta-elimination and resistance to peptide:N-glycosidase F treatment.
1730617	7	56	theme	bovine	1106:1111	arg1	proteins					1118:1125	[3H]Gal-labeled bovine lens proteins	1090:1125	[3H]Gal-labeled bovine lens proteins	1090:1125	Isoelectric focusing of [3H]Gal-labeled bovine lens proteins reveals the presence of O-GlcNAc on all four alpha-crystallin subunits, A1, A2, B1, and B2.
1730617	2	57	theme	alternative	293:303	arg1	functions					305:313	alternative functions	293:313	alternative functions apparently unrelated to their structural role in the lens	293:371	Yet many of these highly conserved proteins are also expressed in nonocular tissues, where they have alternative functions apparently unrelated to their structural role in the lens.
1730617	9	58	theme	peptide	1457:1463	arg1	spectrometry					1410:1421	fast atom bombardment-mass spectrometry	1383:1421	fast atom bombardment-mass spectrometry	1383:1421	Gas-phase protein sequencing and fast atom bombardment-mass spectrometry of the major radiolabeled tryptic peptide from bovine alpha-crystallin reveal that GlcNAc is attached to the alpha A subunits at serine 162.
1730617	9	58	theme	peptide	1457:1463	arg1	sequencing					1368:1377	Gas-phase protein sequencing	1350:1377	Gas-phase protein sequencing	1350:1377	Gas-phase protein sequencing and fast atom bombardment-mass spectrometry of the major radiolabeled tryptic peptide from bovine alpha-crystallin reveal that GlcNAc is attached to the alpha A subunits at serine 162.
1730617	0	59	theme	O-linked	50:57	arg1	N-acetylglucosamine					59:77	O-linked N-acetylglucosamine	50:77	O-linked N-acetylglucosamine	50:77	Vertebrate lens alpha-crystallins are modified by O-linked N-acetylglucosamine.
1730617	2	60	theme	structural	345:354	arg1	role					356:359	their structural role	339:359	their structural role in the lens	339:371	Yet many of these highly conserved proteins are also expressed in nonocular tissues, where they have alternative functions apparently unrelated to their structural role in the lens.
1730617	9	61	theme	bovine	1470:1475	arg1	alpha-crystallin					1477:1492	bovine alpha-crystallin	1470:1492	bovine alpha-crystallin	1470:1492	Gas-phase protein sequencing and fast atom bombardment-mass spectrometry of the major radiolabeled tryptic peptide from bovine alpha-crystallin reveal that GlcNAc is attached to the alpha A subunits at serine 162.
1730617	6	62	theme	bombardment-mass	966:981	arg1	spectrometry					983:994	fast atom bombardment-mass spectrometry	956:994	fast atom bombardment-mass spectrometry of [3H]Gal-labeled tryptic peptides	956:1030	Chromatographic analyses of the beta-elimination products and fast atom bombardment-mass spectrometry of [3H]Gal-labeled tryptic peptides confirm the saccharide structure.
1730617	4	63	theme	lens	662:665	arg1	homogenates					667:677	lens homogenates	662:677	lens homogenates from man, rhesus monkey, rat, cow, and rhea (an ostrich-like bird)	662:744	An in vitro enzymatic assay that transfers [3H]Gal to terminal GlcNAc moieties labels alpha A and alpha B crystallins in lens homogenates from man, rhesus monkey, rat, cow, and rhea (an ostrich-like bird).
1730617	6	64	theme	fast	956:959	arg1	spectrometry					983:994	fast atom bombardment-mass spectrometry	956:994	fast atom bombardment-mass spectrometry of [3H]Gal-labeled tryptic peptides	956:1030	Chromatographic analyses of the beta-elimination products and fast atom bombardment-mass spectrometry of [3H]Gal-labeled tryptic peptides confirm the saccharide structure.
1730617	4	65	theme	A	633:633	arg1	crystallins					647:657	alpha A and alpha B crystallins	627:657	alpha A and alpha B crystallins	627:657	An in vitro enzymatic assay that transfers [3H]Gal to terminal GlcNAc moieties labels alpha A and alpha B crystallins in lens homogenates from man, rhesus monkey, rat, cow, and rhea (an ostrich-like bird).
1730617	10	66	theme	lens	1661:1664	arg1	alpha-crystallin					1666:1681	lens alpha-crystallin	1661:1681	lens alpha-crystallin	1661:1681	This post-translational modification may play an important role in the molecular organization of lens alpha-crystallin.
1730617	2	67	theme	nonocular	258:266	arg1	tissues					268:274	nonocular tissues	258:274	nonocular tissues	258:274	Yet many of these highly conserved proteins are also expressed in nonocular tissues, where they have alternative functions apparently unrelated to their structural role in the lens.
1730617	8	68	theme	mass	1232:1235	arg1	spectrometry					1237:1248	Electrospray mass spectrometry	1219:1248	Electrospray mass spectrometry of bovine alpha-crystallin	1219:1275	Electrospray mass spectrometry of bovine alpha-crystallin demonstrates the presence of a single O-GlcNAc substitution on alpha A2.
1730617	6	69	theme	products	943:950	arg1	spectrometry					983:994	fast atom bombardment-mass spectrometry	956:994	fast atom bombardment-mass spectrometry of [3H]Gal-labeled tryptic peptides	956:1030	Chromatographic analyses of the beta-elimination products and fast atom bombardment-mass spectrometry of [3H]Gal-labeled tryptic peptides confirm the saccharide structure.
1730617	6	69	theme	products	943:950	arg1	analyses					910:917	Chromatographic analyses	894:917	Chromatographic analyses of the beta-elimination products	894:950	Chromatographic analyses of the beta-elimination products and fast atom bombardment-mass spectrometry of [3H]Gal-labeled tryptic peptides confirm the saccharide structure.
1730617	4	70	theme	alpha	639:643	arg1	B					645:645	alpha B	639:645	alpha B	639:645	An in vitro enzymatic assay that transfers [3H]Gal to terminal GlcNAc moieties labels alpha A and alpha B crystallins in lens homogenates from man, rhesus monkey, rat, cow, and rhea (an ostrich-like bird).
1730617	1	71	theme	optical	160:166	arg1	properties					168:177	the remarkable optical properties	145:177	the remarkable optical properties of the lens	145:189	Crystallins are structural proteins responsible for establishing the remarkable optical properties of the lens.
1730617	9	72	theme	A	1538:1538	arg1	subunits					1540:1547	the alpha A subunits	1528:1547	the alpha A subunits at serine 162	1528:1561	Gas-phase protein sequencing and fast atom bombardment-mass spectrometry of the major radiolabeled tryptic peptide from bovine alpha-crystallin reveal that GlcNAc is attached to the alpha A subunits at serine 162.
1730617	6	73	theme	tryptic	1015:1021	arg1	peptides					1023:1030	[3H]Gal-labeled tryptic peptides	999:1030	[3H]Gal-labeled tryptic peptides	999:1030	Chromatographic analyses of the beta-elimination products and fast atom bombardment-mass spectrometry of [3H]Gal-labeled tryptic peptides confirm the saccharide structure.
1730617	8	74	theme	single	1308:1313	arg1	substitution					1324:1335	a single O-GlcNAc substitution	1306:1335	a single O-GlcNAc substitution	1306:1335	Electrospray mass spectrometry of bovine alpha-crystallin demonstrates the presence of a single O-GlcNAc substitution on alpha A2.
1730617	1	75	theme	lens	186:189	arg1	properties					168:177	the remarkable optical properties	145:177	the remarkable optical properties of the lens	145:189	Crystallins are structural proteins responsible for establishing the remarkable optical properties of the lens.
1730617	8	76	theme	substitution	1324:1335	arg1	presence					1294:1301	the presence	1290:1301	the presence of a single O-GlcNAc substitution on alpha A2	1290:1347	Electrospray mass spectrometry of bovine alpha-crystallin demonstrates the presence of a single O-GlcNAc substitution on alpha A2.
1730617	8	77	theme	alpha	1340:1344	arg1	A2					1346:1347	alpha A2	1340:1347	alpha A2	1340:1347	Electrospray mass spectrometry of bovine alpha-crystallin demonstrates the presence of a single O-GlcNAc substitution on alpha A2.
1730617	4	78	theme	ostrich-like	727:738	arg1	rhea					718:721	rhea	718:721	rhea (an ostrich-like bird)	718:744	An in vitro enzymatic assay that transfers [3H]Gal to terminal GlcNAc moieties labels alpha A and alpha B crystallins in lens homogenates from man, rhesus monkey, rat, cow, and rhea (an ostrich-like bird).
1730617	4	78	theme	ostrich-like	727:738	arg1	bird					740:743	an ostrich-like bird	724:743	an ostrich-like bird	724:743	An in vitro enzymatic assay that transfers [3H]Gal to terminal GlcNAc moieties labels alpha A and alpha B crystallins in lens homogenates from man, rhesus monkey, rat, cow, and rhea (an ostrich-like bird).
1730617	0	79	theme	lens	11:14	arg1	alpha-crystallins					16:32	Vertebrate lens alpha-crystallins	0:32	Vertebrate lens alpha-crystallins	0:32	Vertebrate lens alpha-crystallins are modified by O-linked N-acetylglucosamine.
1730617	3	80	theme	heat-shock	444:453	arg1	proteins					455:462	heat-shock proteins	444:462	heat-shock proteins in other tissues	444:479	Here we report that lens alpha-crystallins, some of which function as heat-shock proteins in other tissues, are modified with O-linked N-acetylglucosamine (O-GlcNAc).
1730617	3	80	theme	heat-shock	444:453	arg1	alpha-crystallins					399:415	lens alpha-crystallins	394:415	lens alpha-crystallins	394:415	Here we report that lens alpha-crystallins, some of which function as heat-shock proteins in other tissues, are modified with O-linked N-acetylglucosamine (O-GlcNAc).
1730617	3	80	theme	heat-shock	444:453	arg1	some					418:421	some	418:421	some	418:421	Here we report that lens alpha-crystallins, some of which function as heat-shock proteins in other tissues, are modified with O-linked N-acetylglucosamine (O-GlcNAc).
1730617	4	81	from	cow	709:711	arg1	homogenates					667:677	lens homogenates	662:677	lens homogenates from man, rhesus monkey, rat, cow, and rhea (an ostrich-like bird)	662:744	An in vitro enzymatic assay that transfers [3H]Gal to terminal GlcNAc moieties labels alpha A and alpha B crystallins in lens homogenates from man, rhesus monkey, rat, cow, and rhea (an ostrich-like bird).
1730617	3	82	theme	lens	394:397	arg1	alpha-crystallins					399:415	lens alpha-crystallins	394:415	lens alpha-crystallins	394:415	Here we report that lens alpha-crystallins, some of which function as heat-shock proteins in other tissues, are modified with O-linked N-acetylglucosamine (O-GlcNAc).
1730617	0	83	mod	modified	38:45	arg1	alpha-crystallins					16:32	Vertebrate lens alpha-crystallins	0:32	Vertebrate lens alpha-crystallins	0:32	Vertebrate lens alpha-crystallins are modified by O-linked N-acetylglucosamine.
1730617	0	83	mod	modified	38:45	arg3	N-acetylglucosamine					59:77	O-linked N-acetylglucosamine	50:77	O-linked N-acetylglucosamine	50:77	Vertebrate lens alpha-crystallins are modified by O-linked N-acetylglucosamine.
1730617	9	84	attach	attached	1516:1523	arg1	subunits					1540:1547	the alpha A subunits	1528:1547	the alpha A subunits at serine 162	1528:1561	Gas-phase protein sequencing and fast atom bombardment-mass spectrometry of the major radiolabeled tryptic peptide from bovine alpha-crystallin reveal that GlcNAc is attached to the alpha A subunits at serine 162.
1730617	9	84	attach	attached	1516:1523	arg2	GlcNAc					1506:1511	GlcNAc	1506:1511	GlcNAc	1506:1511	Gas-phase protein sequencing and fast atom bombardment-mass spectrometry of the major radiolabeled tryptic peptide from bovine alpha-crystallin reveal that GlcNAc is attached to the alpha A subunits at serine 162.
1730617	9	85	theme	Gas-phase	1350:1358	arg1	sequencing					1368:1377	Gas-phase protein sequencing	1350:1377	Gas-phase protein sequencing	1350:1377	Gas-phase protein sequencing and fast atom bombardment-mass spectrometry of the major radiolabeled tryptic peptide from bovine alpha-crystallin reveal that GlcNAc is attached to the alpha A subunits at serine 162.
1730617	6	86	theme	saccharide	1044:1053	arg1	structure					1055:1063	the saccharide structure	1040:1063	the saccharide structure	1040:1063	Chromatographic analyses of the beta-elimination products and fast atom bombardment-mass spectrometry of [3H]Gal-labeled tryptic peptides confirm the saccharide structure.
1730617	4	87	theme	in	544:545	arg1	assay					563:567	An in vitro enzymatic assay	541:567	An in vitro enzymatic assay that transfers [3H]Gal to terminal GlcNAc moieties	541:618	An in vitro enzymatic assay that transfers [3H]Gal to terminal GlcNAc moieties labels alpha A and alpha B crystallins in lens homogenates from man, rhesus monkey, rat, cow, and rhea (an ostrich-like bird).
1730617	9	88	from	spectrometry	1410:1421	arg1	alpha-crystallin					1477:1492	bovine alpha-crystallin	1470:1492	bovine alpha-crystallin	1470:1492	Gas-phase protein sequencing and fast atom bombardment-mass spectrometry of the major radiolabeled tryptic peptide from bovine alpha-crystallin reveal that GlcNAc is attached to the alpha A subunits at serine 162.
1730617	4	89	theme	enzymatic	553:561	arg1	assay					563:567	An in vitro enzymatic assay	541:567	An in vitro enzymatic assay that transfers [3H]Gal to terminal GlcNAc moieties	541:618	An in vitro enzymatic assay that transfers [3H]Gal to terminal GlcNAc moieties labels alpha A and alpha B crystallins in lens homogenates from man, rhesus monkey, rat, cow, and rhea (an ostrich-like bird).
1730617	9	90	theme	fast	1383:1386	arg1	spectrometry					1410:1421	fast atom bombardment-mass spectrometry	1383:1421	fast atom bombardment-mass spectrometry	1383:1421	Gas-phase protein sequencing and fast atom bombardment-mass spectrometry of the major radiolabeled tryptic peptide from bovine alpha-crystallin reveal that GlcNAc is attached to the alpha A subunits at serine 162.
1730617	2	91	theme	conserved	217:225	arg1	proteins					227:234	these highly conserved proteins	204:234	these highly conserved proteins	204:234	Yet many of these highly conserved proteins are also expressed in nonocular tissues, where they have alternative functions apparently unrelated to their structural role in the lens.
1730617	9	92	theme	bombardment-mass	1393:1408	arg1	spectrometry					1410:1421	fast atom bombardment-mass spectrometry	1383:1421	fast atom bombardment-mass spectrometry	1383:1421	Gas-phase protein sequencing and fast atom bombardment-mass spectrometry of the major radiolabeled tryptic peptide from bovine alpha-crystallin reveal that GlcNAc is attached to the alpha A subunits at serine 162.
1730617	8	93	theme	alpha-crystallin	1260:1275	arg1	spectrometry					1237:1248	Electrospray mass spectrometry	1219:1248	Electrospray mass spectrometry of bovine alpha-crystallin	1219:1275	Electrospray mass spectrometry of bovine alpha-crystallin demonstrates the presence of a single O-GlcNAc substitution on alpha A2.
1730617	9	94	from	alpha-crystallin	1477:1492	arg1	spectrometry					1410:1421	fast atom bombardment-mass spectrometry	1383:1421	fast atom bombardment-mass spectrometry	1383:1421	Gas-phase protein sequencing and fast atom bombardment-mass spectrometry of the major radiolabeled tryptic peptide from bovine alpha-crystallin reveal that GlcNAc is attached to the alpha A subunits at serine 162.
1730617	9	94	from	alpha-crystallin	1477:1492	arg1	sequencing					1368:1377	Gas-phase protein sequencing	1350:1377	Gas-phase protein sequencing	1350:1377	Gas-phase protein sequencing and fast atom bombardment-mass spectrometry of the major radiolabeled tryptic peptide from bovine alpha-crystallin reveal that GlcNAc is attached to the alpha A subunits at serine 162.
1730617	9	94	from	alpha-crystallin	1477:1492	arg1	peptide					1457:1463	the major radiolabeled tryptic peptide	1426:1463	the major radiolabeled tryptic peptide from bovine alpha-crystallin	1426:1492	Gas-phase protein sequencing and fast atom bombardment-mass spectrometry of the major radiolabeled tryptic peptide from bovine alpha-crystallin reveal that GlcNAc is attached to the alpha A subunits at serine 162.
1730617	4	95	theme	alpha	627:631	arg1	A					633:633	alpha A	627:633	alpha A	627:633	An in vitro enzymatic assay that transfers [3H]Gal to terminal GlcNAc moieties labels alpha A and alpha B crystallins in lens homogenates from man, rhesus monkey, rat, cow, and rhea (an ostrich-like bird).
1730617	3	96	from	proteins	455:462	arg1	tissues					473:479	other tissues	467:479	other tissues	467:479	Here we report that lens alpha-crystallins, some of which function as heat-shock proteins in other tissues, are modified with O-linked N-acetylglucosamine (O-GlcNAc).
7527189	7	0	theme	structural	1260:1269	arg1	determinations					1271:1284	structural determinations	1260:1284	structural determinations	1260:1284	The database for structural determinations was tested using the N-linked carbohydrates released from recombinant human urinary erythropoietin (baby hamster kidney) by PNGase F treatment and from bovine serum fetuin and alpha 1-acid glycoprotein by automated and manual (large-scale) hydrazinolysis, respectively.
7527189	7	1	theme	large-scale	1513:1523	arg1	hydrazinolysis					1526:1539	automated and manual (large-scale) hydrazinolysis	1491:1539	hydrazinolysis	1526:1539	The database for structural determinations was tested using the N-linked carbohydrates released from recombinant human urinary erythropoietin (baby hamster kidney) by PNGase F treatment and from bovine serum fetuin and alpha 1-acid glycoprotein by automated and manual (large-scale) hydrazinolysis, respectively.
7527189	2	2	theme	structural	376:385	arg1	assignments					387:397	carbohydrate structural assignments	363:397	carbohydrate structural assignments	363:397	The suitability of HPCE for carbohydrate structural assignments was ascertained by validation experiments.
7527189	8	3	theme	HPCE	1742:1745	arg1	system					1747:1752	the HPCE system	1738:1752	the HPCE system of a different manufacturer	1738:1780	The efficiency of the database and of the triple-correction method was further confirmed by HPCE measurements performed in a different laboratory and by a different analyst who used the HPCE system of a different manufacturer.
7527189	8	4	theme	database	1578:1585	arg1	efficiency					1560:1569	The efficiency	1556:1569	The efficiency of the database and of the triple-correction method	1556:1621	The efficiency of the database and of the triple-correction method was further confirmed by HPCE measurements performed in a different laboratory and by a different analyst who used the HPCE system of a different manufacturer.
7527189	5	5	theme	N-glycan-mapping	917:932	arg1	database					934:941	The N-glycan-mapping database	913:941	The N-glycan-mapping database	913:941	The N-glycan-mapping database was established using a newly developed and optimized buffer system containing 1,5-diaminopentane as an organic modifier.
7527189	2	6	theme	carbohydrate	363:374	arg1	assignments					387:397	carbohydrate structural assignments	363:397	carbohydrate structural assignments	363:397	The suitability of HPCE for carbohydrate structural assignments was ascertained by validation experiments.
7527189	1	7	theme	carbohydrate	263:274	arg1	analysis					287:294	a carbohydrate structural analysis	261:294	a carbohydrate structural analysis by mere comparison of migration times	261:332	We have evaluated high-performance capillary electrophoresis (HPCE) with respect to its suitability for use in establishing a carbohydrate-mapping database that would enable a carbohydrate structural analysis by mere comparison of migration times.
7527189	4	8	theme	triple-correction	774:790	arg1	method					792:797	a triple-correction method	772:797	a triple-correction method	772:797	By including mesityl oxide and sialic acid as internal standards and a triple-correction method, HPCE fulfills the analytical requirements with respect to accuracy, precision, reproducibility, and sensitivity.
7527189	4	8	theme	triple-correction	774:790	arg1	oxide					724:728	mesityl oxide	716:728	mesityl oxide	716:728	By including mesityl oxide and sialic acid as internal standards and a triple-correction method, HPCE fulfills the analytical requirements with respect to accuracy, precision, reproducibility, and sensitivity.
7527189	4	8	theme	triple-correction	774:790	arg1	acid					741:744	sialic acid	734:744	sialic acid	734:744	By including mesityl oxide and sialic acid as internal standards and a triple-correction method, HPCE fulfills the analytical requirements with respect to accuracy, precision, reproducibility, and sensitivity.
7527189	5	9	theme	optimized	987:995	arg1	system					1004:1009	a newly developed and optimized buffer system	965:1009	a newly developed and optimized buffer system containing 1,5-diaminopentane as an organic modifier	965:1062	The N-glycan-mapping database was established using a newly developed and optimized buffer system containing 1,5-diaminopentane as an organic modifier.
7527189	1	10	theme	structural	276:285	arg1	analysis					287:294	a carbohydrate structural analysis	261:294	a carbohydrate structural analysis by mere comparison of migration times	261:332	We have evaluated high-performance capillary electrophoresis (HPCE) with respect to its suitability for use in establishing a carbohydrate-mapping database that would enable a carbohydrate structural analysis by mere comparison of migration times.
7527189	4	11	theme	internal	749:756	arg1	standards					758:766	internal standards	749:766	internal standards	749:766	By including mesityl oxide and sialic acid as internal standards and a triple-correction method, HPCE fulfills the analytical requirements with respect to accuracy, precision, reproducibility, and sensitivity.
7527189	4	11	theme	internal	749:756	arg1	oxide					724:728	mesityl oxide	716:728	mesityl oxide	716:728	By including mesityl oxide and sialic acid as internal standards and a triple-correction method, HPCE fulfills the analytical requirements with respect to accuracy, precision, reproducibility, and sensitivity.
7527189	4	11	theme	internal	749:756	arg1	acid					741:744	sialic acid	734:744	sialic acid	734:744	By including mesityl oxide and sialic acid as internal standards and a triple-correction method, HPCE fulfills the analytical requirements with respect to accuracy, precision, reproducibility, and sensitivity.
7527189	6	12	theme	mapping	1225:1231	arg1	database					1233:1240	our Lotus 1-2-3 mapping database	1209:1240	our Lotus 1-2-3 mapping database	1209:1240	Approximately 80 different sialylated N-glycans of known structure, which have thus far been measured and characterized, have been entered into our Lotus 1-2-3 mapping database.
7527189	4	13	theme	mesityl	716:722	arg1	standards					758:766	internal standards	749:766	internal standards	749:766	By including mesityl oxide and sialic acid as internal standards and a triple-correction method, HPCE fulfills the analytical requirements with respect to accuracy, precision, reproducibility, and sensitivity.
7527189	4	13	theme	mesityl	716:722	arg1	method					792:797	a triple-correction method	772:797	a triple-correction method	772:797	By including mesityl oxide and sialic acid as internal standards and a triple-correction method, HPCE fulfills the analytical requirements with respect to accuracy, precision, reproducibility, and sensitivity.
7527189	4	13	theme	mesityl	716:722	arg1	oxide					724:728	mesityl oxide	716:728	mesityl oxide	716:728	By including mesityl oxide and sialic acid as internal standards and a triple-correction method, HPCE fulfills the analytical requirements with respect to accuracy, precision, reproducibility, and sensitivity.
7527189	4	13	theme	mesityl	716:722	arg1	acid					741:744	sialic acid	734:744	sialic acid	734:744	By including mesityl oxide and sialic acid as internal standards and a triple-correction method, HPCE fulfills the analytical requirements with respect to accuracy, precision, reproducibility, and sensitivity.
7527189	8	14	theme	manufacturer	1769:1780	arg1	system					1747:1752	the HPCE system	1738:1752	the HPCE system of a different manufacturer	1738:1780	The efficiency of the database and of the triple-correction method was further confirmed by HPCE measurements performed in a different laboratory and by a different analyst who used the HPCE system of a different manufacturer.
7527189	7	15	theme	1-acid	1468:1473	arg1	glycoprotein					1475:1486	alpha 1-acid glycoprotein	1462:1486	alpha 1-acid glycoprotein	1462:1486	The database for structural determinations was tested using the N-linked carbohydrates released from recombinant human urinary erythropoietin (baby hamster kidney) by PNGase F treatment and from bovine serum fetuin and alpha 1-acid glycoprotein by automated and manual (large-scale) hydrazinolysis, respectively.
7527189	7	16	theme	recombinant	1344:1354	arg1	kidney					1399:1404	baby hamster kidney	1386:1404	baby hamster kidney	1386:1404	The database for structural determinations was tested using the N-linked carbohydrates released from recombinant human urinary erythropoietin (baby hamster kidney) by PNGase F treatment and from bovine serum fetuin and alpha 1-acid glycoprotein by automated and manual (large-scale) hydrazinolysis, respectively.
7527189	7	16	theme	recombinant	1344:1354	arg1	erythropoietin					1370:1383	recombinant human urinary erythropoietin	1344:1383	recombinant human urinary erythropoietin (baby hamster kidney)	1344:1405	The database for structural determinations was tested using the N-linked carbohydrates released from recombinant human urinary erythropoietin (baby hamster kidney) by PNGase F treatment and from bovine serum fetuin and alpha 1-acid glycoprotein by automated and manual (large-scale) hydrazinolysis, respectively.
7527189	7	17	gly	glycoprotein	1475:1486	arg1	glycoprotein					1475:1486	alpha 1-acid glycoprotein	1462:1486	alpha 1-acid glycoprotein	1462:1486	The database for structural determinations was tested using the N-linked carbohydrates released from recombinant human urinary erythropoietin (baby hamster kidney) by PNGase F treatment and from bovine serum fetuin and alpha 1-acid glycoprotein by automated and manual (large-scale) hydrazinolysis, respectively.
7527189	5	18	contain	containing	1011:1020	arg2	1,5-diaminopentane					1022:1039	1,5-diaminopentane	1022:1039	1,5-diaminopentane	1022:1039	The N-glycan-mapping database was established using a newly developed and optimized buffer system containing 1,5-diaminopentane as an organic modifier.
7527189	5	18	contain	containing	1011:1020	arg1	system					1004:1009	a newly developed and optimized buffer system	965:1009	a newly developed and optimized buffer system containing 1,5-diaminopentane as an organic modifier	965:1062	The N-glycan-mapping database was established using a newly developed and optimized buffer system containing 1,5-diaminopentane as an organic modifier.
7527189	5	18	contain	containing	1011:1020	arg2	modifier					1055:1062	an organic modifier	1044:1062	an organic modifier	1044:1062	The N-glycan-mapping database was established using a newly developed and optimized buffer system containing 1,5-diaminopentane as an organic modifier.
7527189	3	19	theme	N-glycans	474:482	arg1	reproducible					550:561	reproducible	550:561	reproducible	550:561	The migration times of distinct N-glycans, prepared and measured on different days, were shown to be highly reproducible, with a coefficient of variation of usually less than 0.20%, requiring only femtomoles of N-glycan per injection for reliable measurements.
7527189	3	19	theme	N-glycans	474:482	arg1	times					456:460	The migration times	442:460	The migration times	442:460	The migration times of distinct N-glycans, prepared and measured on different days, were shown to be highly reproducible, with a coefficient of variation of usually less than 0.20%, requiring only femtomoles of N-glycan per injection for reliable measurements.
7527189	8	20	theme	triple-correction	1598:1614	arg1	method					1616:1621	the triple-correction method	1594:1621	the triple-correction method	1594:1621	The efficiency of the database and of the triple-correction method was further confirmed by HPCE measurements performed in a different laboratory and by a different analyst who used the HPCE system of a different manufacturer.
7527189	3	21	with	reproducible	550:561	arg1	coefficient					571:581	a coefficient	569:581	a coefficient of variation of usually less than 0.20%	569:621	The migration times of distinct N-glycans, prepared and measured on different days, were shown to be highly reproducible, with a coefficient of variation of usually less than 0.20%, requiring only femtomoles of N-glycan per injection for reliable measurements.
7527189	6	22	theme	Lotus	1213:1217	arg1	database					1233:1240	our Lotus 1-2-3 mapping database	1209:1240	our Lotus 1-2-3 mapping database	1209:1240	Approximately 80 different sialylated N-glycans of known structure, which have thus far been measured and characterized, have been entered into our Lotus 1-2-3 mapping database.
7527189	2	23	theme	validation	418:427	arg1	experiments					429:439	validation experiments	418:439	validation experiments	418:439	The suitability of HPCE for carbohydrate structural assignments was ascertained by validation experiments.
7527189	7	24	attach	released	1330:1337	arg1	kidney					1399:1404	baby hamster kidney	1386:1404	baby hamster kidney	1386:1404	The database for structural determinations was tested using the N-linked carbohydrates released from recombinant human urinary erythropoietin (baby hamster kidney) by PNGase F treatment and from bovine serum fetuin and alpha 1-acid glycoprotein by automated and manual (large-scale) hydrazinolysis, respectively.
7527189	7	24	attach	released	1330:1337	arg1	glycoprotein					1475:1486	alpha 1-acid glycoprotein	1462:1486	alpha 1-acid glycoprotein	1462:1486	The database for structural determinations was tested using the N-linked carbohydrates released from recombinant human urinary erythropoietin (baby hamster kidney) by PNGase F treatment and from bovine serum fetuin and alpha 1-acid glycoprotein by automated and manual (large-scale) hydrazinolysis, respectively.
7527189	7	24	attach	released	1330:1337	arg2	carbohydrates					1316:1328	the N-linked carbohydrates	1303:1328	the N-linked carbohydrates released from recombinant human urinary erythropoietin (baby hamster kidney) by PNGase F treatment and from bovine serum fetuin and alpha 1-acid glycoprotein by automated and manual (large-scale) hydrazinolysis	1303:1539	The database for structural determinations was tested using the N-linked carbohydrates released from recombinant human urinary erythropoietin (baby hamster kidney) by PNGase F treatment and from bovine serum fetuin and alpha 1-acid glycoprotein by automated and manual (large-scale) hydrazinolysis, respectively.
7527189	7	24	attach	released	1330:1337	arg1	erythropoietin					1370:1383	recombinant human urinary erythropoietin	1344:1383	recombinant human urinary erythropoietin (baby hamster kidney)	1344:1405	The database for structural determinations was tested using the N-linked carbohydrates released from recombinant human urinary erythropoietin (baby hamster kidney) by PNGase F treatment and from bovine serum fetuin and alpha 1-acid glycoprotein by automated and manual (large-scale) hydrazinolysis, respectively.
7527189	7	24	attach	released	1330:1337	arg1	fetuin					1451:1456	bovine serum fetuin	1438:1456	bovine serum fetuin	1438:1456	The database for structural determinations was tested using the N-linked carbohydrates released from recombinant human urinary erythropoietin (baby hamster kidney) by PNGase F treatment and from bovine serum fetuin and alpha 1-acid glycoprotein by automated and manual (large-scale) hydrazinolysis, respectively.
7527189	5	25	theme	organic	1047:1053	arg1	modifier					1055:1062	an organic modifier	1044:1062	an organic modifier	1044:1062	The N-glycan-mapping database was established using a newly developed and optimized buffer system containing 1,5-diaminopentane as an organic modifier.
7527189	5	25	theme	organic	1047:1053	arg1	1,5-diaminopentane					1022:1039	1,5-diaminopentane	1022:1039	1,5-diaminopentane	1022:1039	The N-glycan-mapping database was established using a newly developed and optimized buffer system containing 1,5-diaminopentane as an organic modifier.
7527189	3	26	theme	variation	586:594	arg1	coefficient					571:581	a coefficient	569:581	a coefficient of variation of usually less than 0.20%	569:621	The migration times of distinct N-glycans, prepared and measured on different days, were shown to be highly reproducible, with a coefficient of variation of usually less than 0.20%, requiring only femtomoles of N-glycan per injection for reliable measurements.
7527189	7	27	theme	hamster	1391:1397	arg1	kidney					1399:1404	baby hamster kidney	1386:1404	baby hamster kidney	1386:1404	The database for structural determinations was tested using the N-linked carbohydrates released from recombinant human urinary erythropoietin (baby hamster kidney) by PNGase F treatment and from bovine serum fetuin and alpha 1-acid glycoprotein by automated and manual (large-scale) hydrazinolysis, respectively.
7527189	7	27	theme	hamster	1391:1397	arg1	erythropoietin					1370:1383	recombinant human urinary erythropoietin	1344:1383	recombinant human urinary erythropoietin (baby hamster kidney)	1344:1405	The database for structural determinations was tested using the N-linked carbohydrates released from recombinant human urinary erythropoietin (baby hamster kidney) by PNGase F treatment and from bovine serum fetuin and alpha 1-acid glycoprotein by automated and manual (large-scale) hydrazinolysis, respectively.
7527189	7	28	link	N-linked	1307:1314	arg1	carbohydrates					1316:1328	the N-linked carbohydrates	1303:1328	the N-linked carbohydrates released from recombinant human urinary erythropoietin (baby hamster kidney) by PNGase F treatment and from bovine serum fetuin and alpha 1-acid glycoprotein by automated and manual (large-scale) hydrazinolysis	1303:1539	The database for structural determinations was tested using the N-linked carbohydrates released from recombinant human urinary erythropoietin (baby hamster kidney) by PNGase F treatment and from bovine serum fetuin and alpha 1-acid glycoprotein by automated and manual (large-scale) hydrazinolysis, respectively.
7527189	3	29	dep	times	456:460	arg1	measured					498:505	measured	498:505	measured on different days	498:523	The migration times of distinct N-glycans, prepared and measured on different days, were shown to be highly reproducible, with a coefficient of variation of usually less than 0.20%, requiring only femtomoles of N-glycan per injection for reliable measurements.
7527189	3	29	dep	times	456:460	arg1	prepared					485:492	prepared	485:492	prepared	485:492	The migration times of distinct N-glycans, prepared and measured on different days, were shown to be highly reproducible, with a coefficient of variation of usually less than 0.20%, requiring only femtomoles of N-glycan per injection for reliable measurements.
7527189	5	30	theme	developed	973:981	arg1	system					1004:1009	a newly developed and optimized buffer system	965:1009	a newly developed and optimized buffer system containing 1,5-diaminopentane as an organic modifier	965:1062	The N-glycan-mapping database was established using a newly developed and optimized buffer system containing 1,5-diaminopentane as an organic modifier.
7527189	3	31	theme	distinct	465:472	arg1	N-glycans					474:482	distinct N-glycans	465:482	distinct N-glycans	465:482	The migration times of distinct N-glycans, prepared and measured on different days, were shown to be highly reproducible, with a coefficient of variation of usually less than 0.20%, requiring only femtomoles of N-glycan per injection for reliable measurements.
7527189	1	32	theme	mere	299:302	arg1	comparison					304:313	mere comparison	299:313	mere comparison of migration times	299:332	We have evaluated high-performance capillary electrophoresis (HPCE) with respect to its suitability for use in establishing a carbohydrate-mapping database that would enable a carbohydrate structural analysis by mere comparison of migration times.
7527189	4	33	theme	analytical	818:827	arg1	requirements					829:840	the analytical requirements	814:840	the analytical requirements with respect to accuracy, precision, reproducibility, and sensitivity	814:910	By including mesityl oxide and sialic acid as internal standards and a triple-correction method, HPCE fulfills the analytical requirements with respect to accuracy, precision, reproducibility, and sensitivity.
7527189	7	34	theme	bovine	1438:1443	arg1	fetuin					1451:1456	bovine serum fetuin	1438:1456	bovine serum fetuin	1438:1456	The database for structural determinations was tested using the N-linked carbohydrates released from recombinant human urinary erythropoietin (baby hamster kidney) by PNGase F treatment and from bovine serum fetuin and alpha 1-acid glycoprotein by automated and manual (large-scale) hydrazinolysis, respectively.
7527189	5	35	theme	buffer	997:1002	arg1	system					1004:1009	a newly developed and optimized buffer system	965:1009	a newly developed and optimized buffer system containing 1,5-diaminopentane as an organic modifier	965:1062	The N-glycan-mapping database was established using a newly developed and optimized buffer system containing 1,5-diaminopentane as an organic modifier.
7527189	3	36	theme	N-glycan	653:660	arg1	femtomoles					639:648	only femtomoles	634:648	only femtomoles of N-glycan	634:660	The migration times of distinct N-glycans, prepared and measured on different days, were shown to be highly reproducible, with a coefficient of variation of usually less than 0.20%, requiring only femtomoles of N-glycan per injection for reliable measurements.
7527189	1	37	theme	high-performance	105:120	arg1	HPCE					149:152	HPCE	149:152	HPCE	149:152	We have evaluated high-performance capillary electrophoresis (HPCE) with respect to its suitability for use in establishing a carbohydrate-mapping database that would enable a carbohydrate structural analysis by mere comparison of migration times.
7527189	1	37	theme	high-performance	105:120	arg1	electrophoresis					132:146	high-performance capillary electrophoresis	105:146	high-performance capillary electrophoresis (HPCE)	105:153	We have evaluated high-performance capillary electrophoresis (HPCE) with respect to its suitability for use in establishing a carbohydrate-mapping database that would enable a carbohydrate structural analysis by mere comparison of migration times.
7527189	7	38	theme	baby	1386:1389	arg1	kidney					1399:1404	baby hamster kidney	1386:1404	baby hamster kidney	1386:1404	The database for structural determinations was tested using the N-linked carbohydrates released from recombinant human urinary erythropoietin (baby hamster kidney) by PNGase F treatment and from bovine serum fetuin and alpha 1-acid glycoprotein by automated and manual (large-scale) hydrazinolysis, respectively.
7527189	7	38	theme	baby	1386:1389	arg1	erythropoietin					1370:1383	recombinant human urinary erythropoietin	1344:1383	recombinant human urinary erythropoietin (baby hamster kidney)	1344:1405	The database for structural determinations was tested using the N-linked carbohydrates released from recombinant human urinary erythropoietin (baby hamster kidney) by PNGase F treatment and from bovine serum fetuin and alpha 1-acid glycoprotein by automated and manual (large-scale) hydrazinolysis, respectively.
7527189	3	39	theme	migration	446:454	arg1	reproducible					550:561	reproducible	550:561	reproducible	550:561	The migration times of distinct N-glycans, prepared and measured on different days, were shown to be highly reproducible, with a coefficient of variation of usually less than 0.20%, requiring only femtomoles of N-glycan per injection for reliable measurements.
7527189	3	39	theme	migration	446:454	arg1	times					456:460	The migration times	442:460	The migration times	442:460	The migration times of distinct N-glycans, prepared and measured on different days, were shown to be highly reproducible, with a coefficient of variation of usually less than 0.20%, requiring only femtomoles of N-glycan per injection for reliable measurements.
7527189	7	40	theme	human	1356:1360	arg1	kidney					1399:1404	baby hamster kidney	1386:1404	baby hamster kidney	1386:1404	The database for structural determinations was tested using the N-linked carbohydrates released from recombinant human urinary erythropoietin (baby hamster kidney) by PNGase F treatment and from bovine serum fetuin and alpha 1-acid glycoprotein by automated and manual (large-scale) hydrazinolysis, respectively.
7527189	7	40	theme	human	1356:1360	arg1	erythropoietin					1370:1383	recombinant human urinary erythropoietin	1344:1383	recombinant human urinary erythropoietin (baby hamster kidney)	1344:1405	The database for structural determinations was tested using the N-linked carbohydrates released from recombinant human urinary erythropoietin (baby hamster kidney) by PNGase F treatment and from bovine serum fetuin and alpha 1-acid glycoprotein by automated and manual (large-scale) hydrazinolysis, respectively.
7527189	6	41	gly	sialylated	1092:1101	arg1	N-glycans					1103:1111	Approximately 80 different sialylated N-glycans	1065:1111	Approximately 80 different sialylated N-glycans	1065:1111	Approximately 80 different sialylated N-glycans of known structure, which have thus far been measured and characterized, have been entered into our Lotus 1-2-3 mapping database.
7527189	7	42	theme	urinary	1362:1368	arg1	kidney					1399:1404	baby hamster kidney	1386:1404	baby hamster kidney	1386:1404	The database for structural determinations was tested using the N-linked carbohydrates released from recombinant human urinary erythropoietin (baby hamster kidney) by PNGase F treatment and from bovine serum fetuin and alpha 1-acid glycoprotein by automated and manual (large-scale) hydrazinolysis, respectively.
7527189	7	42	theme	urinary	1362:1368	arg1	erythropoietin					1370:1383	recombinant human urinary erythropoietin	1344:1383	recombinant human urinary erythropoietin (baby hamster kidney)	1344:1405	The database for structural determinations was tested using the N-linked carbohydrates released from recombinant human urinary erythropoietin (baby hamster kidney) by PNGase F treatment and from bovine serum fetuin and alpha 1-acid glycoprotein by automated and manual (large-scale) hydrazinolysis, respectively.
7527189	7	43	theme	serum	1445:1449	arg1	fetuin					1451:1456	bovine serum fetuin	1438:1456	bovine serum fetuin	1438:1456	The database for structural determinations was tested using the N-linked carbohydrates released from recombinant human urinary erythropoietin (baby hamster kidney) by PNGase F treatment and from bovine serum fetuin and alpha 1-acid glycoprotein by automated and manual (large-scale) hydrazinolysis, respectively.
7527189	6	44	theme	structure	1122:1130	arg1	N-glycans					1103:1111	Approximately 80 different sialylated N-glycans	1065:1111	Approximately 80 different sialylated N-glycans	1065:1111	Approximately 80 different sialylated N-glycans of known structure, which have thus far been measured and characterized, have been entered into our Lotus 1-2-3 mapping database.
7527189	7	45	theme	manual	1505:1510	arg1	hydrazinolysis					1526:1539	automated and manual (large-scale) hydrazinolysis	1491:1539	hydrazinolysis	1526:1539	The database for structural determinations was tested using the N-linked carbohydrates released from recombinant human urinary erythropoietin (baby hamster kidney) by PNGase F treatment and from bovine serum fetuin and alpha 1-acid glycoprotein by automated and manual (large-scale) hydrazinolysis, respectively.
7527189	1	46	theme	migration	318:326	arg1	times					328:332	migration times	318:332	migration times	318:332	We have evaluated high-performance capillary electrophoresis (HPCE) with respect to its suitability for use in establishing a carbohydrate-mapping database that would enable a carbohydrate structural analysis by mere comparison of migration times.
7527189	8	47	used	used	1733:1736	arg2	analyst					1721:1727	a different analyst	1709:1727	a different analyst who used the HPCE system of a different manufacturer	1709:1780	The efficiency of the database and of the triple-correction method was further confirmed by HPCE measurements performed in a different laboratory and by a different analyst who used the HPCE system of a different manufacturer.
7527189	1	48	theme	carbohydrate-mapping	213:232	arg1	database					234:241	a carbohydrate-mapping database	211:241	a carbohydrate-mapping database that would enable a carbohydrate structural analysis by mere comparison of migration times	211:332	We have evaluated high-performance capillary electrophoresis (HPCE) with respect to its suitability for use in establishing a carbohydrate-mapping database that would enable a carbohydrate structural analysis by mere comparison of migration times.
7527189	1	49	theme	times	328:332	arg1	comparison					304:313	mere comparison	299:313	mere comparison of migration times	299:332	We have evaluated high-performance capillary electrophoresis (HPCE) with respect to its suitability for use in establishing a carbohydrate-mapping database that would enable a carbohydrate structural analysis by mere comparison of migration times.
7527189	7	50	theme	PNGase	1410:1415	arg1	treatment					1419:1427	PNGase F treatment	1410:1427	PNGase F treatment	1410:1427	The database for structural determinations was tested using the N-linked carbohydrates released from recombinant human urinary erythropoietin (baby hamster kidney) by PNGase F treatment and from bovine serum fetuin and alpha 1-acid glycoprotein by automated and manual (large-scale) hydrazinolysis, respectively.
7527189	8	51	theme	method	1616:1621	arg1	efficiency					1560:1569	The efficiency	1556:1569	The efficiency of the database and of the triple-correction method	1556:1621	The efficiency of the database and of the triple-correction method was further confirmed by HPCE measurements performed in a different laboratory and by a different analyst who used the HPCE system of a different manufacturer.
7527189	1	52	theme	capillary	122:130	arg1	HPCE					149:152	HPCE	149:152	HPCE	149:152	We have evaluated high-performance capillary electrophoresis (HPCE) with respect to its suitability for use in establishing a carbohydrate-mapping database that would enable a carbohydrate structural analysis by mere comparison of migration times.
7527189	1	52	theme	capillary	122:130	arg1	electrophoresis					132:146	high-performance capillary electrophoresis	105:146	high-performance capillary electrophoresis (HPCE)	105:153	We have evaluated high-performance capillary electrophoresis (HPCE) with respect to its suitability for use in establishing a carbohydrate-mapping database that would enable a carbohydrate structural analysis by mere comparison of migration times.
7527189	0	53	theme	N-glycans	30:38	arg1	mapping					19:25	the mapping	15:25	the mapping of N-glycans by high-performance capillary electrophoresis	15:84	A strategy for the mapping of N-glycans by high-performance capillary electrophoresis.
7527189	3	54	theme	reliable	680:687	arg1	measurements					689:700	reliable measurements	680:700	reliable measurements	680:700	The migration times of distinct N-glycans, prepared and measured on different days, were shown to be highly reproducible, with a coefficient of variation of usually less than 0.20%, requiring only femtomoles of N-glycan per injection for reliable measurements.
7527189	7	55	theme	alpha	1462:1466	arg1	glycoprotein					1475:1486	alpha 1-acid glycoprotein	1462:1486	alpha 1-acid glycoprotein	1462:1486	The database for structural determinations was tested using the N-linked carbohydrates released from recombinant human urinary erythropoietin (baby hamster kidney) by PNGase F treatment and from bovine serum fetuin and alpha 1-acid glycoprotein by automated and manual (large-scale) hydrazinolysis, respectively.
7527189	2	56	theme	HPCE	354:357	arg1	suitability					339:349	The suitability	335:349	The suitability of HPCE for carbohydrate structural assignments	335:397	The suitability of HPCE for carbohydrate structural assignments was ascertained by validation experiments.
7527189	3	57	theme	different	510:518	arg1	days					520:523	different days	510:523	different days	510:523	The migration times of distinct N-glycans, prepared and measured on different days, were shown to be highly reproducible, with a coefficient of variation of usually less than 0.20%, requiring only femtomoles of N-glycan per injection for reliable measurements.
7527189	6	58	theme	different	1082:1090	arg1	N-glycans					1103:1111	Approximately 80 different sialylated N-glycans	1065:1111	Approximately 80 different sialylated N-glycans	1065:1111	Approximately 80 different sialylated N-glycans of known structure, which have thus far been measured and characterized, have been entered into our Lotus 1-2-3 mapping database.
7527189	7	59	theme	automated	1491:1499	arg1	hydrazinolysis					1526:1539	automated and manual (large-scale) hydrazinolysis	1491:1539	hydrazinolysis	1526:1539	The database for structural determinations was tested using the N-linked carbohydrates released from recombinant human urinary erythropoietin (baby hamster kidney) by PNGase F treatment and from bovine serum fetuin and alpha 1-acid glycoprotein by automated and manual (large-scale) hydrazinolysis, respectively.
7527189	3	60	theme	only	634:637	arg1	femtomoles					639:648	only femtomoles	634:648	only femtomoles of N-glycan	634:660	The migration times of distinct N-glycans, prepared and measured on different days, were shown to be highly reproducible, with a coefficient of variation of usually less than 0.20%, requiring only femtomoles of N-glycan per injection for reliable measurements.
7527189	4	61	theme	sialic	734:739	arg1	standards					758:766	internal standards	749:766	internal standards	749:766	By including mesityl oxide and sialic acid as internal standards and a triple-correction method, HPCE fulfills the analytical requirements with respect to accuracy, precision, reproducibility, and sensitivity.
7527189	4	61	theme	sialic	734:739	arg1	method					792:797	a triple-correction method	772:797	a triple-correction method	772:797	By including mesityl oxide and sialic acid as internal standards and a triple-correction method, HPCE fulfills the analytical requirements with respect to accuracy, precision, reproducibility, and sensitivity.
7527189	4	61	theme	sialic	734:739	arg1	oxide					724:728	mesityl oxide	716:728	mesityl oxide	716:728	By including mesityl oxide and sialic acid as internal standards and a triple-correction method, HPCE fulfills the analytical requirements with respect to accuracy, precision, reproducibility, and sensitivity.
7527189	4	61	theme	sialic	734:739	arg1	acid					741:744	sialic acid	734:744	sialic acid	734:744	By including mesityl oxide and sialic acid as internal standards and a triple-correction method, HPCE fulfills the analytical requirements with respect to accuracy, precision, reproducibility, and sensitivity.
7527189	8	62	theme	different	1759:1767	arg1	manufacturer					1769:1780	a different manufacturer	1757:1780	a different manufacturer	1757:1780	The efficiency of the database and of the triple-correction method was further confirmed by HPCE measurements performed in a different laboratory and by a different analyst who used the HPCE system of a different manufacturer.
7527189	0	63	theme	capillary	60:68	arg1	electrophoresis					70:84	high-performance capillary electrophoresis	43:84	high-performance capillary electrophoresis	43:84	A strategy for the mapping of N-glycans by high-performance capillary electrophoresis.
7527189	6	64	theme	sialylated	1092:1101	arg1	N-glycans					1103:1111	Approximately 80 different sialylated N-glycans	1065:1111	Approximately 80 different sialylated N-glycans	1065:1111	Approximately 80 different sialylated N-glycans of known structure, which have thus far been measured and characterized, have been entered into our Lotus 1-2-3 mapping database.
7527189	3	65	theme	%	621:621	arg1	variation					586:594	variation	586:594	variation of usually less than 0.20%	586:621	The migration times of distinct N-glycans, prepared and measured on different days, were shown to be highly reproducible, with a coefficient of variation of usually less than 0.20%, requiring only femtomoles of N-glycan per injection for reliable measurements.
7527189	6	66	theme	known	1116:1120	arg1	structure					1122:1130	known structure	1116:1130	known structure	1116:1130	Approximately 80 different sialylated N-glycans of known structure, which have thus far been measured and characterized, have been entered into our Lotus 1-2-3 mapping database.
7527189	7	67	theme	N-linked	1307:1314	arg1	carbohydrates					1316:1328	the N-linked carbohydrates	1303:1328	the N-linked carbohydrates released from recombinant human urinary erythropoietin (baby hamster kidney) by PNGase F treatment and from bovine serum fetuin and alpha 1-acid glycoprotein by automated and manual (large-scale) hydrazinolysis	1303:1539	The database for structural determinations was tested using the N-linked carbohydrates released from recombinant human urinary erythropoietin (baby hamster kidney) by PNGase F treatment and from bovine serum fetuin and alpha 1-acid glycoprotein by automated and manual (large-scale) hydrazinolysis, respectively.
7527189	8	68	theme	HPCE	1648:1651	arg1	measurements					1653:1664	HPCE measurements	1648:1664	HPCE measurements performed in a different laboratory	1648:1700	The efficiency of the database and of the triple-correction method was further confirmed by HPCE measurements performed in a different laboratory and by a different analyst who used the HPCE system of a different manufacturer.
7527189	0	69	theme	high-performance	43:58	arg1	electrophoresis					70:84	high-performance capillary electrophoresis	43:84	high-performance capillary electrophoresis	43:84	A strategy for the mapping of N-glycans by high-performance capillary electrophoresis.
7527189	7	70	theme	F	1417:1417	arg1	treatment					1419:1427	PNGase F treatment	1410:1427	PNGase F treatment	1410:1427	The database for structural determinations was tested using the N-linked carbohydrates released from recombinant human urinary erythropoietin (baby hamster kidney) by PNGase F treatment and from bovine serum fetuin and alpha 1-acid glycoprotein by automated and manual (large-scale) hydrazinolysis, respectively.
7527189	8	71	theme	different	1711:1719	arg1	analyst					1721:1727	a different analyst	1709:1727	a different analyst who used the HPCE system of a different manufacturer	1709:1780	The efficiency of the database and of the triple-correction method was further confirmed by HPCE measurements performed in a different laboratory and by a different analyst who used the HPCE system of a different manufacturer.
7527189	8	72	theme	different	1681:1689	arg1	laboratory					1691:1700	a different laboratory	1679:1700	a different laboratory	1679:1700	The efficiency of the database and of the triple-correction method was further confirmed by HPCE measurements performed in a different laboratory and by a different analyst who used the HPCE system of a different manufacturer.
8054720	3	0	theme	chains	514:519	arg1	structures					465:474	the structures	461:474	the structures of the intact sialylated carbohydrate chains of rHuEPO expressed in Chinese hamster ovary (CHO) cells	461:576	Prompted by conflicting literature reports on the issue, we reinvestigated the structures of the intact sialylated carbohydrate chains of rHuEPO expressed in Chinese hamster ovary (CHO) cells.
8054720	6	1	theme	methylation	966:976	arg1	analysis					978:985	methylation analysis	966:985	methylation analysis	966:985	The primary structures of the major sialylated N- and O-type oligosaccharides were identified by 500-MHz 1H-NMR spectroscopy, supported by data from composition analysis, methylation analysis, low- and high-pH anion-exchange chromatography, and fast atom bombardment-mass spectrometry.
8054720	9	2	theme	-linked	1677:1683	arg1	fucose					1685:1690	alpha(1-->6)-linked fucose	1665:1690	alpha(1-->6)-linked fucose	1665:1690	The majority (> 95%) of N-linked structures contain alpha(1-->6)-linked fucose at the proximal GlcNAc residue.
8054720	4	3	theme	asparagine-linked	583:599	arg1	oligosaccharides					601:616	The asparagine-linked oligosaccharides	579:616	The asparagine-linked oligosaccharides	579:616	The asparagine-linked oligosaccharides were released from rHuEPO with N-glycanase and fractionated by anion-exchange chromatography.
8054720	8	4	theme	tetra-antennary	1438:1452	arg1	structures					1454:1463	tetra-antennary structures	1438:1463	tetra-antennary structures	1438:1463	The major (> 95%) di-, tri- and tetra-antennary structures are fully sialylated, i.e. they have two, three and four sialic acid residues, respectively, linked exclusively alpha(2-->3) to galactose residues.
8054720	7	5	theme	2,6-branched	1211:1222	arg1	di-antennary					1169:1180	di-antennary	1169:1180	di-antennary	1169:1180	The most abundant N-linked oligosaccharides in CHO cell-derived rHuEPO were found to be di-antennary, 2,4-branched tri-antennary, 2,6-branched tri-antennary and tetra-antennary chains (in the ratio of 7:6:5:82), with the latter containing between zero and three repeating N-acetyllactosamine units, in well-defined branches.
8054720	7	5	theme	2,6-branched	1211:1222	arg1	chains					1258:1263	2,6-branched tri-antennary and tetra-antennary chains	1211:1263	2,6-branched tri-antennary and tetra-antennary chains (in the ratio of 7:6:5:82)	1211:1290	The most abundant N-linked oligosaccharides in CHO cell-derived rHuEPO were found to be di-antennary, 2,4-branched tri-antennary, 2,6-branched tri-antennary and tetra-antennary chains (in the ratio of 7:6:5:82), with the latter containing between zero and three repeating N-acetyllactosamine units, in well-defined branches.
8054720	6	6	theme	oligosaccharides	856:871	arg1	structures					807:816	The primary structures	795:816	The primary structures of the major sialylated N- and O-type oligosaccharides	795:871	The primary structures of the major sialylated N- and O-type oligosaccharides were identified by 500-MHz 1H-NMR spectroscopy, supported by data from composition analysis, methylation analysis, low- and high-pH anion-exchange chromatography, and fast atom bombardment-mass spectrometry.
8054720	3	7	theme	hamster	552:558	arg1	cells					572:576	Chinese hamster ovary (CHO) cells	544:576	Chinese hamster ovary (CHO) cells	544:576	Prompted by conflicting literature reports on the issue, we reinvestigated the structures of the intact sialylated carbohydrate chains of rHuEPO expressed in Chinese hamster ovary (CHO) cells.
8054720	1	8	theme	anaemic	269:275	arg1	patients					277:284	anaemic patients	269:284	anaemic patients	269:284	Recombinant human erythropoietin (rHuEPO) is used abundantly in the clinic to stimulate red blood cell growth in anaemic patients.
8054720	6	9	from	analysis	956:963	arg1	data					934:937	data	934:937	data from composition analysis, methylation analysis, low- and high-pH anion-exchange chromatography	934:1033	The primary structures of the major sialylated N- and O-type oligosaccharides were identified by 500-MHz 1H-NMR spectroscopy, supported by data from composition analysis, methylation analysis, low- and high-pH anion-exchange chromatography, and fast atom bombardment-mass spectrometry.
8054720	8	10	dep	alpha	1577:1581	arg1	residues					1603:1610	galactose residues	1593:1610	galactose residues	1593:1610	The major (> 95%) di-, tri- and tetra-antennary structures are fully sialylated, i.e. they have two, three and four sialic acid residues, respectively, linked exclusively alpha(2-->3) to galactose residues.
8054720	0	11	theme	Structure	0:8	arg1	determination					10:22	Structure determination	0:22	Structure determination of the intact major sialylated oligosaccharide chains of recombinant human erythropoietin	0:112	Structure determination of the intact major sialylated oligosaccharide chains of recombinant human erythropoietin expressed in Chinese hamster ovary cells.
8054720	9	12	theme	proximal	1699:1706	arg1	residue					1715:1721	the proximal GlcNAc residue	1695:1721	the proximal GlcNAc residue	1695:1721	The majority (> 95%) of N-linked structures contain alpha(1-->6)-linked fucose at the proximal GlcNAc residue.
8054720	6	13	theme	sialylated	831:840	arg1	N-					842:843	the major sialylated N-	821:843	the major sialylated N-	821:843	The primary structures of the major sialylated N- and O-type oligosaccharides were identified by 500-MHz 1H-NMR spectroscopy, supported by data from composition analysis, methylation analysis, low- and high-pH anion-exchange chromatography, and fast atom bombardment-mass spectrometry.
8054720	2	14	theme	drug	307:310	arg1	efficacy					291:298	The efficacy	287:298	The efficacy of the drug	287:310	The efficacy of the drug depends strongly on the extent of sialylation of its carbohydrate moiety.
8054720	6	15	theme	fast	1040:1043	arg1	spectrometry					1067:1078	fast atom bombardment-mass spectrometry	1040:1078	fast atom bombardment-mass spectrometry	1040:1078	The primary structures of the major sialylated N- and O-type oligosaccharides were identified by 500-MHz 1H-NMR spectroscopy, supported by data from composition analysis, methylation analysis, low- and high-pH anion-exchange chromatography, and fast atom bombardment-mass spectrometry.
8054720	0	16	theme	hamster	135:141	arg1	cells					149:153	Chinese hamster ovary cells	127:153	Chinese hamster ovary cells	127:153	Structure determination of the intact major sialylated oligosaccharide chains of recombinant human erythropoietin expressed in Chinese hamster ovary cells.
8054720	10	17	theme	linear	1795:1800	arg1	tri-					1802:1805	a linear tri-	1793:1805	a linear tri-	1793:1805	The O-type mono- and disialyl oligosaccharides were characterized as a linear tri- and a branched tetra-saccharide, respectively.
8054720	10	17	theme	linear	1795:1800	arg1	oligosaccharides					1754:1769	The O-type mono- and disialyl oligosaccharides	1724:1769	The O-type mono- and disialyl oligosaccharides	1724:1769	The O-type mono- and disialyl oligosaccharides were characterized as a linear tri- and a branched tetra-saccharide, respectively.
8054720	6	18	gly	sialylated	831:840	arg1	N-					842:843	the major sialylated N-	821:843	the major sialylated N-	821:843	The primary structures of the major sialylated N- and O-type oligosaccharides were identified by 500-MHz 1H-NMR spectroscopy, supported by data from composition analysis, methylation analysis, low- and high-pH anion-exchange chromatography, and fast atom bombardment-mass spectrometry.
8054720	5	19	theme	alkaline	762:769	arg1	conditions					783:792	alkaline borohydride conditions	762:792	alkaline borohydride conditions	762:792	The O-linked oligosaccharides were released under alkaline borohydride conditions.
8054720	7	20	theme	N-linked	1099:1106	arg1	di-antennary					1169:1180	di-antennary	1169:1180	di-antennary	1169:1180	The most abundant N-linked oligosaccharides in CHO cell-derived rHuEPO were found to be di-antennary, 2,4-branched tri-antennary, 2,6-branched tri-antennary and tetra-antennary chains (in the ratio of 7:6:5:82), with the latter containing between zero and three repeating N-acetyllactosamine units, in well-defined branches.
8054720	7	20	theme	N-linked	1099:1106	arg1	oligosaccharides					1108:1123	The most abundant N-linked oligosaccharides	1081:1123	The most abundant N-linked oligosaccharides in CHO cell-derived rHuEPO	1081:1150	The most abundant N-linked oligosaccharides in CHO cell-derived rHuEPO were found to be di-antennary, 2,4-branched tri-antennary, 2,6-branched tri-antennary and tetra-antennary chains (in the ratio of 7:6:5:82), with the latter containing between zero and three repeating N-acetyllactosamine units, in well-defined branches.
8054720	6	21	theme	anion-exchange	1005:1018	arg1	chromatography					1020:1033	high-pH anion-exchange chromatography	997:1033	high-pH anion-exchange chromatography	997:1033	The primary structures of the major sialylated N- and O-type oligosaccharides were identified by 500-MHz 1H-NMR spectroscopy, supported by data from composition analysis, methylation analysis, low- and high-pH anion-exchange chromatography, and fast atom bombardment-mass spectrometry.
8054720	10	22	theme	O-type	1728:1733	arg1	tri-					1802:1805	a linear tri-	1793:1805	a linear tri-	1793:1805	The O-type mono- and disialyl oligosaccharides were characterized as a linear tri- and a branched tetra-saccharide, respectively.
8054720	10	22	theme	O-type	1728:1733	arg1	tetra-saccharide					1822:1837	a branched tetra-saccharide	1811:1837	a branched tetra-saccharide	1811:1837	The O-type mono- and disialyl oligosaccharides were characterized as a linear tri- and a branched tetra-saccharide, respectively.
8054720	10	22	theme	O-type	1728:1733	arg1	oligosaccharides					1754:1769	The O-type mono- and disialyl oligosaccharides	1724:1769	The O-type mono- and disialyl oligosaccharides	1724:1769	The O-type mono- and disialyl oligosaccharides were characterized as a linear tri- and a branched tetra-saccharide, respectively.
8054720	7	23	link	N-linked	1099:1106	arg1	di-antennary					1169:1180	di-antennary	1169:1180	di-antennary	1169:1180	The most abundant N-linked oligosaccharides in CHO cell-derived rHuEPO were found to be di-antennary, 2,4-branched tri-antennary, 2,6-branched tri-antennary and tetra-antennary chains (in the ratio of 7:6:5:82), with the latter containing between zero and three repeating N-acetyllactosamine units, in well-defined branches.
8054720	7	23	link	N-linked	1099:1106	arg1	oligosaccharides					1108:1123	The most abundant N-linked oligosaccharides	1081:1123	The most abundant N-linked oligosaccharides in CHO cell-derived rHuEPO	1081:1150	The most abundant N-linked oligosaccharides in CHO cell-derived rHuEPO were found to be di-antennary, 2,4-branched tri-antennary, 2,6-branched tri-antennary and tetra-antennary chains (in the ratio of 7:6:5:82), with the latter containing between zero and three repeating N-acetyllactosamine units, in well-defined branches.
8054720	10	24	theme	branched	1813:1820	arg1	tetra-saccharide					1822:1837	a branched tetra-saccharide	1811:1837	a branched tetra-saccharide	1811:1837	The O-type mono- and disialyl oligosaccharides were characterized as a linear tri- and a branched tetra-saccharide, respectively.
8054720	10	24	theme	branched	1813:1820	arg1	oligosaccharides					1754:1769	The O-type mono- and disialyl oligosaccharides	1724:1769	The O-type mono- and disialyl oligosaccharides	1724:1769	The O-type mono- and disialyl oligosaccharides were characterized as a linear tri- and a branched tetra-saccharide, respectively.
8054720	8	25	theme	acid	1529:1532	arg1	residues					1534:1541	two, three and four sialic acid residues	1502:1541	two, three and four sialic acid residues	1502:1541	The major (> 95%) di-, tri- and tetra-antennary structures are fully sialylated, i.e. they have two, three and four sialic acid residues, respectively, linked exclusively alpha(2-->3) to galactose residues.
8054720	1	26	used	used	201:204	arg2	rHuEPO					190:195	rHuEPO	190:195	rHuEPO	190:195	Recombinant human erythropoietin (rHuEPO) is used abundantly in the clinic to stimulate red blood cell growth in anaemic patients.
8054720	1	26	used	used	201:204	arg2	erythropoietin					174:187	Recombinant human erythropoietin	156:187	Recombinant human erythropoietin (rHuEPO)	156:196	Recombinant human erythropoietin (rHuEPO) is used abundantly in the clinic to stimulate red blood cell growth in anaemic patients.
8054720	8	27	theme	major	1410:1414	arg1	di-					1424:1426	The major (> 95%) di-	1406:1426	The major (> 95%) di-	1406:1426	The major (> 95%) di-, tri- and tetra-antennary structures are fully sialylated, i.e. they have two, three and four sialic acid residues, respectively, linked exclusively alpha(2-->3) to galactose residues.
8054720	8	27	theme	major	1410:1414	arg1	%					1421:1421	> 95%	1417:1421	> 95%	1417:1421	The major (> 95%) di-, tri- and tetra-antennary structures are fully sialylated, i.e. they have two, three and four sialic acid residues, respectively, linked exclusively alpha(2-->3) to galactose residues.
8054720	8	28	theme	>	1417:1417	arg1	di-					1424:1426	The major (> 95%) di-	1406:1426	The major (> 95%) di-	1406:1426	The major (> 95%) di-, tri- and tetra-antennary structures are fully sialylated, i.e. they have two, three and four sialic acid residues, respectively, linked exclusively alpha(2-->3) to galactose residues.
8054720	8	28	theme	>	1417:1417	arg1	%					1421:1421	> 95%	1417:1421	> 95%	1417:1421	The major (> 95%) di-, tri- and tetra-antennary structures are fully sialylated, i.e. they have two, three and four sialic acid residues, respectively, linked exclusively alpha(2-->3) to galactose residues.
8054720	0	29	theme	chains	71:76	arg1	determination					10:22	Structure determination	0:22	Structure determination of the intact major sialylated oligosaccharide chains of recombinant human erythropoietin	0:112	Structure determination of the intact major sialylated oligosaccharide chains of recombinant human erythropoietin expressed in Chinese hamster ovary cells.
8054720	1	30	theme	human	168:172	arg1	rHuEPO					190:195	rHuEPO	190:195	rHuEPO	190:195	Recombinant human erythropoietin (rHuEPO) is used abundantly in the clinic to stimulate red blood cell growth in anaemic patients.
8054720	1	30	theme	human	168:172	arg1	erythropoietin					174:187	Recombinant human erythropoietin	156:187	Recombinant human erythropoietin (rHuEPO)	156:196	Recombinant human erythropoietin (rHuEPO) is used abundantly in the clinic to stimulate red blood cell growth in anaemic patients.
8054720	7	31	from	chains	1258:1263	arg1	ratio					1273:1277	the ratio	1269:1277	the ratio of 7:6:5:82	1269:1289	The most abundant N-linked oligosaccharides in CHO cell-derived rHuEPO were found to be di-antennary, 2,4-branched tri-antennary, 2,6-branched tri-antennary and tetra-antennary chains (in the ratio of 7:6:5:82), with the latter containing between zero and three repeating N-acetyllactosamine units, in well-defined branches.
8054720	0	32	theme	recombinant	81:91	arg1	erythropoietin					99:112	recombinant human erythropoietin	81:112	recombinant human erythropoietin	81:112	Structure determination of the intact major sialylated oligosaccharide chains of recombinant human erythropoietin expressed in Chinese hamster ovary cells.
8054720	10	33	theme	mono-	1735:1739	arg1	tri-					1802:1805	a linear tri-	1793:1805	a linear tri-	1793:1805	The O-type mono- and disialyl oligosaccharides were characterized as a linear tri- and a branched tetra-saccharide, respectively.
8054720	10	33	theme	mono-	1735:1739	arg1	tetra-saccharide					1822:1837	a branched tetra-saccharide	1811:1837	a branched tetra-saccharide	1811:1837	The O-type mono- and disialyl oligosaccharides were characterized as a linear tri- and a branched tetra-saccharide, respectively.
8054720	10	33	theme	mono-	1735:1739	arg1	oligosaccharides					1754:1769	The O-type mono- and disialyl oligosaccharides	1724:1769	The O-type mono- and disialyl oligosaccharides	1724:1769	The O-type mono- and disialyl oligosaccharides were characterized as a linear tri- and a branched tetra-saccharide, respectively.
8054720	0	34	theme	erythropoietin	99:112	arg1	chains					71:76	the intact major sialylated oligosaccharide chains	27:76	the intact major sialylated oligosaccharide chains of recombinant human erythropoietin	27:112	Structure determination of the intact major sialylated oligosaccharide chains of recombinant human erythropoietin expressed in Chinese hamster ovary cells.
8054720	6	35	theme	bombardment-mass	1050:1065	arg1	spectrometry					1067:1078	fast atom bombardment-mass spectrometry	1040:1078	fast atom bombardment-mass spectrometry	1040:1078	The primary structures of the major sialylated N- and O-type oligosaccharides were identified by 500-MHz 1H-NMR spectroscopy, supported by data from composition analysis, methylation analysis, low- and high-pH anion-exchange chromatography, and fast atom bombardment-mass spectrometry.
8054720	3	36	gly	sialylated	490:499	arg1	chains					514:519	the intact sialylated carbohydrate chains	479:519	the intact sialylated carbohydrate chains of rHuEPO expressed in Chinese hamster ovary (CHO) cells	479:576	Prompted by conflicting literature reports on the issue, we reinvestigated the structures of the intact sialylated carbohydrate chains of rHuEPO expressed in Chinese hamster ovary (CHO) cells.
8054720	2	37	theme	moiety	378:383	arg1	sialylation					346:356	sialylation	346:356	sialylation of its carbohydrate moiety	346:383	The efficacy of the drug depends strongly on the extent of sialylation of its carbohydrate moiety.
8054720	7	38	theme	7:6:5:82	1282:1289	arg1	ratio					1273:1277	the ratio	1269:1277	the ratio of 7:6:5:82	1269:1289	The most abundant N-linked oligosaccharides in CHO cell-derived rHuEPO were found to be di-antennary, 2,4-branched tri-antennary, 2,6-branched tri-antennary and tetra-antennary chains (in the ratio of 7:6:5:82), with the latter containing between zero and three repeating N-acetyllactosamine units, in well-defined branches.
8054720	8	39	theme	galactose	1593:1601	arg1	residues					1603:1610	galactose residues	1593:1610	galactose residues	1593:1610	The major (> 95%) di-, tri- and tetra-antennary structures are fully sialylated, i.e. they have two, three and four sialic acid residues, respectively, linked exclusively alpha(2-->3) to galactose residues.
8054720	3	40	theme	literature	410:419	arg1	reports					421:427	literature reports	410:427	literature reports on the issue	410:440	Prompted by conflicting literature reports on the issue, we reinvestigated the structures of the intact sialylated carbohydrate chains of rHuEPO expressed in Chinese hamster ovary (CHO) cells.
8054720	0	41	theme	intact	31:36	arg1	chains					71:76	the intact major sialylated oligosaccharide chains	27:76	the intact major sialylated oligosaccharide chains of recombinant human erythropoietin	27:112	Structure determination of the intact major sialylated oligosaccharide chains of recombinant human erythropoietin expressed in Chinese hamster ovary cells.
8054720	5	42	link	O-linked	716:723	arg1	oligosaccharides					725:740	The O-linked oligosaccharides	712:740	The O-linked oligosaccharides	712:740	The O-linked oligosaccharides were released under alkaline borohydride conditions.
8054720	0	43	theme	sialylated	44:53	arg1	chains					71:76	the intact major sialylated oligosaccharide chains	27:76	the intact major sialylated oligosaccharide chains of recombinant human erythropoietin	27:112	Structure determination of the intact major sialylated oligosaccharide chains of recombinant human erythropoietin expressed in Chinese hamster ovary cells.
8054720	4	44	link	asparagine-linked	583:599	arg1	oligosaccharides					601:616	The asparagine-linked oligosaccharides	579:616	The asparagine-linked oligosaccharides	579:616	The asparagine-linked oligosaccharides were released from rHuEPO with N-glycanase and fractionated by anion-exchange chromatography.
8054720	9	45	theme	N-linked	1637:1644	arg1	structures					1646:1655	N-linked structures	1637:1655	N-linked structures	1637:1655	The majority (> 95%) of N-linked structures contain alpha(1-->6)-linked fucose at the proximal GlcNAc residue.
8054720	7	46	theme	well-defined	1383:1394	arg1	branches					1396:1403	well-defined branches	1383:1403	well-defined branches	1383:1403	The most abundant N-linked oligosaccharides in CHO cell-derived rHuEPO were found to be di-antennary, 2,4-branched tri-antennary, 2,6-branched tri-antennary and tetra-antennary chains (in the ratio of 7:6:5:82), with the latter containing between zero and three repeating N-acetyllactosamine units, in well-defined branches.
8054720	6	47	from	chromatography	1020:1033	arg1	data					934:937	data	934:937	data from composition analysis, methylation analysis, low- and high-pH anion-exchange chromatography	934:1033	The primary structures of the major sialylated N- and O-type oligosaccharides were identified by 500-MHz 1H-NMR spectroscopy, supported by data from composition analysis, methylation analysis, low- and high-pH anion-exchange chromatography, and fast atom bombardment-mass spectrometry.
8054720	6	48	theme	primary	799:805	arg1	structures					807:816	The primary structures	795:816	The primary structures of the major sialylated N- and O-type oligosaccharides	795:871	The primary structures of the major sialylated N- and O-type oligosaccharides were identified by 500-MHz 1H-NMR spectroscopy, supported by data from composition analysis, methylation analysis, low- and high-pH anion-exchange chromatography, and fast atom bombardment-mass spectrometry.
8054720	7	49	link	cell-derived	1132:1143	arg1	rHuEPO					1145:1150	CHO cell-derived rHuEPO	1128:1150	CHO cell-derived rHuEPO	1128:1150	The most abundant N-linked oligosaccharides in CHO cell-derived rHuEPO were found to be di-antennary, 2,4-branched tri-antennary, 2,6-branched tri-antennary and tetra-antennary chains (in the ratio of 7:6:5:82), with the latter containing between zero and three repeating N-acetyllactosamine units, in well-defined branches.
8054720	6	50	theme	500-MHz	892:898	arg1	spectroscopy					907:918	500-MHz 1H-NMR spectroscopy	892:918	500-MHz 1H-NMR spectroscopy	892:918	The primary structures of the major sialylated N- and O-type oligosaccharides were identified by 500-MHz 1H-NMR spectroscopy, supported by data from composition analysis, methylation analysis, low- and high-pH anion-exchange chromatography, and fast atom bombardment-mass spectrometry.
8054720	6	51	from	analysis	978:985	arg1	data					934:937	data	934:937	data from composition analysis, methylation analysis, low- and high-pH anion-exchange chromatography	934:1033	The primary structures of the major sialylated N- and O-type oligosaccharides were identified by 500-MHz 1H-NMR spectroscopy, supported by data from composition analysis, methylation analysis, low- and high-pH anion-exchange chromatography, and fast atom bombardment-mass spectrometry.
8054720	4	52	with	rHuEPO	637:642	arg1	N-glycanase					649:659	N-glycanase	649:659	N-glycanase	649:659	The asparagine-linked oligosaccharides were released from rHuEPO with N-glycanase and fractionated by anion-exchange chromatography.
8054720	1	53	theme	red	244:246	arg1	cell					254:257	red blood cell	244:257	red blood cell growth in anaemic patients	244:284	Recombinant human erythropoietin (rHuEPO) is used abundantly in the clinic to stimulate red blood cell growth in anaemic patients.
8054720	0	54	theme	oligosaccharide	55:69	arg1	chains					71:76	the intact major sialylated oligosaccharide chains	27:76	the intact major sialylated oligosaccharide chains of recombinant human erythropoietin	27:112	Structure determination of the intact major sialylated oligosaccharide chains of recombinant human erythropoietin expressed in Chinese hamster ovary cells.
8054720	7	55	theme	N-acetyllactosamine	1353:1371	arg1	units					1373:1377	between zero and three repeating N-acetyllactosamine units	1320:1377	between zero and three repeating N-acetyllactosamine units	1320:1377	The most abundant N-linked oligosaccharides in CHO cell-derived rHuEPO were found to be di-antennary, 2,4-branched tri-antennary, 2,6-branched tri-antennary and tetra-antennary chains (in the ratio of 7:6:5:82), with the latter containing between zero and three repeating N-acetyllactosamine units, in well-defined branches.
8054720	6	56	from	low-	988:991	arg1	data					934:937	data	934:937	data from composition analysis, methylation analysis, low- and high-pH anion-exchange chromatography	934:1033	The primary structures of the major sialylated N- and O-type oligosaccharides were identified by 500-MHz 1H-NMR spectroscopy, supported by data from composition analysis, methylation analysis, low- and high-pH anion-exchange chromatography, and fast atom bombardment-mass spectrometry.
8054720	7	57	theme	tri-antennary	1224:1236	arg1	di-antennary					1169:1180	di-antennary	1169:1180	di-antennary	1169:1180	The most abundant N-linked oligosaccharides in CHO cell-derived rHuEPO were found to be di-antennary, 2,4-branched tri-antennary, 2,6-branched tri-antennary and tetra-antennary chains (in the ratio of 7:6:5:82), with the latter containing between zero and three repeating N-acetyllactosamine units, in well-defined branches.
8054720	7	57	theme	tri-antennary	1224:1236	arg1	chains					1258:1263	2,6-branched tri-antennary and tetra-antennary chains	1211:1263	2,6-branched tri-antennary and tetra-antennary chains (in the ratio of 7:6:5:82)	1211:1290	The most abundant N-linked oligosaccharides in CHO cell-derived rHuEPO were found to be di-antennary, 2,4-branched tri-antennary, 2,6-branched tri-antennary and tetra-antennary chains (in the ratio of 7:6:5:82), with the latter containing between zero and three repeating N-acetyllactosamine units, in well-defined branches.
8054720	2	58	theme	sialylation	346:356	arg1	extent					336:341	the extent	332:341	the extent of sialylation of its carbohydrate moiety	332:383	The efficacy of the drug depends strongly on the extent of sialylation of its carbohydrate moiety.
8054720	1	59	theme	cell	254:257	arg1	growth					259:264	red blood cell growth	244:264	red blood cell growth in anaemic patients	244:284	Recombinant human erythropoietin (rHuEPO) is used abundantly in the clinic to stimulate red blood cell growth in anaemic patients.
8054720	3	60	theme	Chinese	544:550	arg1	cells					572:576	Chinese hamster ovary (CHO) cells	544:576	Chinese hamster ovary (CHO) cells	544:576	Prompted by conflicting literature reports on the issue, we reinvestigated the structures of the intact sialylated carbohydrate chains of rHuEPO expressed in Chinese hamster ovary (CHO) cells.
8054720	3	61	theme	intact	483:488	arg1	chains					514:519	the intact sialylated carbohydrate chains	479:519	the intact sialylated carbohydrate chains of rHuEPO expressed in Chinese hamster ovary (CHO) cells	479:576	Prompted by conflicting literature reports on the issue, we reinvestigated the structures of the intact sialylated carbohydrate chains of rHuEPO expressed in Chinese hamster ovary (CHO) cells.
8054720	7	62	theme	2,4-branched	1183:1194	arg1	di-antennary					1169:1180	di-antennary	1169:1180	di-antennary	1169:1180	The most abundant N-linked oligosaccharides in CHO cell-derived rHuEPO were found to be di-antennary, 2,4-branched tri-antennary, 2,6-branched tri-antennary and tetra-antennary chains (in the ratio of 7:6:5:82), with the latter containing between zero and three repeating N-acetyllactosamine units, in well-defined branches.
8054720	7	62	theme	2,4-branched	1183:1194	arg1	tri-antennary					1196:1208	2,4-branched tri-antennary	1183:1208	2,4-branched tri-antennary	1183:1208	The most abundant N-linked oligosaccharides in CHO cell-derived rHuEPO were found to be di-antennary, 2,4-branched tri-antennary, 2,6-branched tri-antennary and tetra-antennary chains (in the ratio of 7:6:5:82), with the latter containing between zero and three repeating N-acetyllactosamine units, in well-defined branches.
8054720	6	63	theme	O-type	849:854	arg1	oligosaccharides					856:871	O-type oligosaccharides	849:871	O-type oligosaccharides	849:871	The primary structures of the major sialylated N- and O-type oligosaccharides were identified by 500-MHz 1H-NMR spectroscopy, supported by data from composition analysis, methylation analysis, low- and high-pH anion-exchange chromatography, and fast atom bombardment-mass spectrometry.
8054720	8	64	attach	linked	1558:1563	arg1	2-->3					1583:1587	2-->3	1583:1587	2-->3	1583:1587	The major (> 95%) di-, tri- and tetra-antennary structures are fully sialylated, i.e. they have two, three and four sialic acid residues, respectively, linked exclusively alpha(2-->3) to galactose residues.
8054720	8	64	attach	linked	1558:1563	arg1	alpha					1577:1581	alpha	1577:1581	alpha(2-->3)	1577:1588	The major (> 95%) di-, tri- and tetra-antennary structures are fully sialylated, i.e. they have two, three and four sialic acid residues, respectively, linked exclusively alpha(2-->3) to galactose residues.
8054720	8	64	attach	linked	1558:1563	arg2	they					1492:1495	they	1492:1495	they	1492:1495	The major (> 95%) di-, tri- and tetra-antennary structures are fully sialylated, i.e. they have two, three and four sialic acid residues, respectively, linked exclusively alpha(2-->3) to galactose residues.
8054720	6	65	theme	composition	944:954	arg1	analysis					956:963	composition analysis	944:963	composition analysis	944:963	The primary structures of the major sialylated N- and O-type oligosaccharides were identified by 500-MHz 1H-NMR spectroscopy, supported by data from composition analysis, methylation analysis, low- and high-pH anion-exchange chromatography, and fast atom bombardment-mass spectrometry.
8054720	6	66	theme	N-	842:843	arg1	structures					807:816	The primary structures	795:816	The primary structures of the major sialylated N- and O-type oligosaccharides	795:871	The primary structures of the major sialylated N- and O-type oligosaccharides were identified by 500-MHz 1H-NMR spectroscopy, supported by data from composition analysis, methylation analysis, low- and high-pH anion-exchange chromatography, and fast atom bombardment-mass spectrometry.
8054720	3	67	theme	CHO	567:569	arg1	cells					572:576	Chinese hamster ovary (CHO) cells	544:576	Chinese hamster ovary (CHO) cells	544:576	Prompted by conflicting literature reports on the issue, we reinvestigated the structures of the intact sialylated carbohydrate chains of rHuEPO expressed in Chinese hamster ovary (CHO) cells.
8054720	6	68	theme	atom	1045:1048	arg1	spectrometry					1067:1078	fast atom bombardment-mass spectrometry	1040:1078	fast atom bombardment-mass spectrometry	1040:1078	The primary structures of the major sialylated N- and O-type oligosaccharides were identified by 500-MHz 1H-NMR spectroscopy, supported by data from composition analysis, methylation analysis, low- and high-pH anion-exchange chromatography, and fast atom bombardment-mass spectrometry.
8054720	9	69	theme	GlcNAc	1708:1713	arg1	residue					1715:1721	the proximal GlcNAc residue	1695:1721	the proximal GlcNAc residue	1695:1721	The majority (> 95%) of N-linked structures contain alpha(1-->6)-linked fucose at the proximal GlcNAc residue.
8054720	4	70	theme	anion-exchange	681:694	arg1	chromatography					696:709	anion-exchange chromatography	681:709	anion-exchange chromatography	681:709	The asparagine-linked oligosaccharides were released from rHuEPO with N-glycanase and fractionated by anion-exchange chromatography.
8054720	0	71	theme	ovary	143:147	arg1	cells					149:153	Chinese hamster ovary cells	127:153	Chinese hamster ovary cells	127:153	Structure determination of the intact major sialylated oligosaccharide chains of recombinant human erythropoietin expressed in Chinese hamster ovary cells.
8054720	6	72	theme	major	825:829	arg1	N-					842:843	the major sialylated N-	821:843	the major sialylated N-	821:843	The primary structures of the major sialylated N- and O-type oligosaccharides were identified by 500-MHz 1H-NMR spectroscopy, supported by data from composition analysis, methylation analysis, low- and high-pH anion-exchange chromatography, and fast atom bombardment-mass spectrometry.
8054720	3	73	theme	ovary	560:564	arg1	cells					572:576	Chinese hamster ovary (CHO) cells	544:576	Chinese hamster ovary (CHO) cells	544:576	Prompted by conflicting literature reports on the issue, we reinvestigated the structures of the intact sialylated carbohydrate chains of rHuEPO expressed in Chinese hamster ovary (CHO) cells.
8054720	3	74	theme	carbohydrate	501:512	arg1	chains					514:519	the intact sialylated carbohydrate chains	479:519	the intact sialylated carbohydrate chains of rHuEPO expressed in Chinese hamster ovary (CHO) cells	479:576	Prompted by conflicting literature reports on the issue, we reinvestigated the structures of the intact sialylated carbohydrate chains of rHuEPO expressed in Chinese hamster ovary (CHO) cells.
8054720	9	75	link	N-linked	1637:1644	arg1	structures					1646:1655	N-linked structures	1637:1655	N-linked structures	1637:1655	The majority (> 95%) of N-linked structures contain alpha(1-->6)-linked fucose at the proximal GlcNAc residue.
8054720	8	76	theme	sialic	1522:1527	arg1	residues					1534:1541	two, three and four sialic acid residues	1502:1541	two, three and four sialic acid residues	1502:1541	The major (> 95%) di-, tri- and tetra-antennary structures are fully sialylated, i.e. they have two, three and four sialic acid residues, respectively, linked exclusively alpha(2-->3) to galactose residues.
8054720	7	77	from	oligosaccharides	1108:1123	arg1	rHuEPO					1145:1150	CHO cell-derived rHuEPO	1128:1150	CHO cell-derived rHuEPO	1128:1150	The most abundant N-linked oligosaccharides in CHO cell-derived rHuEPO were found to be di-antennary, 2,4-branched tri-antennary, 2,6-branched tri-antennary and tetra-antennary chains (in the ratio of 7:6:5:82), with the latter containing between zero and three repeating N-acetyllactosamine units, in well-defined branches.
8054720	9	78	contain	contain	1657:1663	arg1	majority					1617:1624	The majority	1613:1624	The majority (> 95%) of N-linked structures	1613:1655	The majority (> 95%) of N-linked structures contain alpha(1-->6)-linked fucose at the proximal GlcNAc residue.
8054720	9	78	contain	contain	1657:1663	arg1	residue					1715:1721	the proximal GlcNAc residue	1695:1721	the proximal GlcNAc residue	1695:1721	The majority (> 95%) of N-linked structures contain alpha(1-->6)-linked fucose at the proximal GlcNAc residue.
8054720	9	78	contain	contain	1657:1663	arg2	%					1631:1631	> 95%	1627:1631	> 95%	1627:1631	The majority (> 95%) of N-linked structures contain alpha(1-->6)-linked fucose at the proximal GlcNAc residue.
8054720	9	78	contain	contain	1657:1663	arg2	majority					1617:1624	The majority	1613:1624	The majority (> 95%) of N-linked structures	1613:1655	The majority (> 95%) of N-linked structures contain alpha(1-->6)-linked fucose at the proximal GlcNAc residue.
8054720	9	78	contain	contain	1657:1663	arg1	%					1631:1631	> 95%	1627:1631	> 95%	1627:1631	The majority (> 95%) of N-linked structures contain alpha(1-->6)-linked fucose at the proximal GlcNAc residue.
8054720	9	78	contain	contain	1657:1663	arg2	fucose					1685:1690	alpha(1-->6)-linked fucose	1665:1690	alpha(1-->6)-linked fucose	1665:1690	The majority (> 95%) of N-linked structures contain alpha(1-->6)-linked fucose at the proximal GlcNAc residue.
8054720	7	79	theme	cell-derived	1132:1143	arg1	rHuEPO					1145:1150	CHO cell-derived rHuEPO	1128:1150	CHO cell-derived rHuEPO	1128:1150	The most abundant N-linked oligosaccharides in CHO cell-derived rHuEPO were found to be di-antennary, 2,4-branched tri-antennary, 2,6-branched tri-antennary and tetra-antennary chains (in the ratio of 7:6:5:82), with the latter containing between zero and three repeating N-acetyllactosamine units, in well-defined branches.
8054720	4	80	attach	released	623:630	arg1	rHuEPO					637:642	rHuEPO	637:642	rHuEPO with N-glycanase	637:659	The asparagine-linked oligosaccharides were released from rHuEPO with N-glycanase and fractionated by anion-exchange chromatography.
8054720	4	80	attach	released	623:630	arg2	oligosaccharides					601:616	The asparagine-linked oligosaccharides	579:616	The asparagine-linked oligosaccharides	579:616	The asparagine-linked oligosaccharides were released from rHuEPO with N-glycanase and fractionated by anion-exchange chromatography.
8054720	6	81	theme	high-pH	997:1003	arg1	chromatography					1020:1033	high-pH anion-exchange chromatography	997:1033	high-pH anion-exchange chromatography	997:1033	The primary structures of the major sialylated N- and O-type oligosaccharides were identified by 500-MHz 1H-NMR spectroscopy, supported by data from composition analysis, methylation analysis, low- and high-pH anion-exchange chromatography, and fast atom bombardment-mass spectrometry.
8054720	5	82	theme	O-linked	716:723	arg1	oligosaccharides					725:740	The O-linked oligosaccharides	712:740	The O-linked oligosaccharides	712:740	The O-linked oligosaccharides were released under alkaline borohydride conditions.
8054720	7	83	theme	abundant	1090:1097	arg1	di-antennary					1169:1180	di-antennary	1169:1180	di-antennary	1169:1180	The most abundant N-linked oligosaccharides in CHO cell-derived rHuEPO were found to be di-antennary, 2,4-branched tri-antennary, 2,6-branched tri-antennary and tetra-antennary chains (in the ratio of 7:6:5:82), with the latter containing between zero and three repeating N-acetyllactosamine units, in well-defined branches.
8054720	7	83	theme	abundant	1090:1097	arg1	oligosaccharides					1108:1123	The most abundant N-linked oligosaccharides	1081:1123	The most abundant N-linked oligosaccharides in CHO cell-derived rHuEPO	1081:1150	The most abundant N-linked oligosaccharides in CHO cell-derived rHuEPO were found to be di-antennary, 2,4-branched tri-antennary, 2,6-branched tri-antennary and tetra-antennary chains (in the ratio of 7:6:5:82), with the latter containing between zero and three repeating N-acetyllactosamine units, in well-defined branches.
8054720	1	84	theme	Recombinant	156:166	arg1	rHuEPO					190:195	rHuEPO	190:195	rHuEPO	190:195	Recombinant human erythropoietin (rHuEPO) is used abundantly in the clinic to stimulate red blood cell growth in anaemic patients.
8054720	1	84	theme	Recombinant	156:166	arg1	erythropoietin					174:187	Recombinant human erythropoietin	156:187	Recombinant human erythropoietin (rHuEPO)	156:196	Recombinant human erythropoietin (rHuEPO) is used abundantly in the clinic to stimulate red blood cell growth in anaemic patients.
8054720	0	85	theme	human	93:97	arg1	erythropoietin					99:112	recombinant human erythropoietin	81:112	recombinant human erythropoietin	81:112	Structure determination of the intact major sialylated oligosaccharide chains of recombinant human erythropoietin expressed in Chinese hamster ovary cells.
8054720	5	86	theme	borohydride	771:781	arg1	conditions					783:792	alkaline borohydride conditions	762:792	alkaline borohydride conditions	762:792	The O-linked oligosaccharides were released under alkaline borohydride conditions.
8054720	3	87	from	reports	421:427	arg1	issue					436:440	the issue	432:440	the issue	432:440	Prompted by conflicting literature reports on the issue, we reinvestigated the structures of the intact sialylated carbohydrate chains of rHuEPO expressed in Chinese hamster ovary (CHO) cells.
8054720	0	88	theme	Chinese	127:133	arg1	cells					149:153	Chinese hamster ovary cells	127:153	Chinese hamster ovary cells	127:153	Structure determination of the intact major sialylated oligosaccharide chains of recombinant human erythropoietin expressed in Chinese hamster ovary cells.
8054720	7	89	from	di-antennary	1169:1180	arg1	branches					1396:1403	well-defined branches	1383:1403	well-defined branches	1383:1403	The most abundant N-linked oligosaccharides in CHO cell-derived rHuEPO were found to be di-antennary, 2,4-branched tri-antennary, 2,6-branched tri-antennary and tetra-antennary chains (in the ratio of 7:6:5:82), with the latter containing between zero and three repeating N-acetyllactosamine units, in well-defined branches.
8054720	2	90	theme	carbohydrate	365:376	arg1	moiety					378:383	its carbohydrate moiety	361:383	its carbohydrate moiety	361:383	The efficacy of the drug depends strongly on the extent of sialylation of its carbohydrate moiety.
8054720	9	91	theme	>	1627:1627	arg1	%					1631:1631	> 95%	1627:1631	> 95%	1627:1631	The majority (> 95%) of N-linked structures contain alpha(1-->6)-linked fucose at the proximal GlcNAc residue.
8054720	9	91	theme	>	1627:1627	arg1	majority					1617:1624	The majority	1613:1624	The majority (> 95%) of N-linked structures	1613:1655	The majority (> 95%) of N-linked structures contain alpha(1-->6)-linked fucose at the proximal GlcNAc residue.
8054720	9	92	link	-linked	1677:1683	arg1	fucose					1685:1690	alpha(1-->6)-linked fucose	1665:1690	alpha(1-->6)-linked fucose	1665:1690	The majority (> 95%) of N-linked structures contain alpha(1-->6)-linked fucose at the proximal GlcNAc residue.
8054720	0	93	theme	major	38:42	arg1	chains					71:76	the intact major sialylated oligosaccharide chains	27:76	the intact major sialylated oligosaccharide chains of recombinant human erythropoietin	27:112	Structure determination of the intact major sialylated oligosaccharide chains of recombinant human erythropoietin expressed in Chinese hamster ovary cells.
8054720	2	94	gly	sialylation	346:356	arg1	moiety					378:383	its carbohydrate moiety	361:383	its carbohydrate moiety	361:383	The efficacy of the drug depends strongly on the extent of sialylation of its carbohydrate moiety.
8054720	7	95	theme	tetra-antennary	1242:1256	arg1	di-antennary					1169:1180	di-antennary	1169:1180	di-antennary	1169:1180	The most abundant N-linked oligosaccharides in CHO cell-derived rHuEPO were found to be di-antennary, 2,4-branched tri-antennary, 2,6-branched tri-antennary and tetra-antennary chains (in the ratio of 7:6:5:82), with the latter containing between zero and three repeating N-acetyllactosamine units, in well-defined branches.
8054720	7	95	theme	tetra-antennary	1242:1256	arg1	chains					1258:1263	2,6-branched tri-antennary and tetra-antennary chains	1211:1263	2,6-branched tri-antennary and tetra-antennary chains (in the ratio of 7:6:5:82)	1211:1290	The most abundant N-linked oligosaccharides in CHO cell-derived rHuEPO were found to be di-antennary, 2,4-branched tri-antennary, 2,6-branched tri-antennary and tetra-antennary chains (in the ratio of 7:6:5:82), with the latter containing between zero and three repeating N-acetyllactosamine units, in well-defined branches.
8054720	7	96	with	di-antennary	1169:1180	arg1	latter					1302:1307	latter	1302:1307	latter	1302:1307	The most abundant N-linked oligosaccharides in CHO cell-derived rHuEPO were found to be di-antennary, 2,4-branched tri-antennary, 2,6-branched tri-antennary and tetra-antennary chains (in the ratio of 7:6:5:82), with the latter containing between zero and three repeating N-acetyllactosamine units, in well-defined branches.
8054720	1	97	from	growth	259:264	arg1	patients					277:284	anaemic patients	269:284	anaemic patients	269:284	Recombinant human erythropoietin (rHuEPO) is used abundantly in the clinic to stimulate red blood cell growth in anaemic patients.
8054720	3	98	theme	sialylated	490:499	arg1	chains					514:519	the intact sialylated carbohydrate chains	479:519	the intact sialylated carbohydrate chains of rHuEPO expressed in Chinese hamster ovary (CHO) cells	479:576	Prompted by conflicting literature reports on the issue, we reinvestigated the structures of the intact sialylated carbohydrate chains of rHuEPO expressed in Chinese hamster ovary (CHO) cells.
8054720	6	99	theme	1H-NMR	900:905	arg1	spectroscopy					907:918	500-MHz 1H-NMR spectroscopy	892:918	500-MHz 1H-NMR spectroscopy	892:918	The primary structures of the major sialylated N- and O-type oligosaccharides were identified by 500-MHz 1H-NMR spectroscopy, supported by data from composition analysis, methylation analysis, low- and high-pH anion-exchange chromatography, and fast atom bombardment-mass spectrometry.
8054720	9	100	theme	structures	1646:1655	arg1	%					1631:1631	> 95%	1627:1631	> 95%	1627:1631	The majority (> 95%) of N-linked structures contain alpha(1-->6)-linked fucose at the proximal GlcNAc residue.
8054720	9	100	theme	structures	1646:1655	arg1	majority					1617:1624	The majority	1613:1624	The majority (> 95%) of N-linked structures	1613:1655	The majority (> 95%) of N-linked structures contain alpha(1-->6)-linked fucose at the proximal GlcNAc residue.
8054720	7	101	contain	containing	1309:1318	arg2	units					1373:1377	between zero and three repeating N-acetyllactosamine units	1320:1377	between zero and three repeating N-acetyllactosamine units	1320:1377	The most abundant N-linked oligosaccharides in CHO cell-derived rHuEPO were found to be di-antennary, 2,4-branched tri-antennary, 2,6-branched tri-antennary and tetra-antennary chains (in the ratio of 7:6:5:82), with the latter containing between zero and three repeating N-acetyllactosamine units, in well-defined branches.
8054720	7	101	contain	containing	1309:1318	arg1	latter					1302:1307	latter	1302:1307	latter	1302:1307	The most abundant N-linked oligosaccharides in CHO cell-derived rHuEPO were found to be di-antennary, 2,4-branched tri-antennary, 2,6-branched tri-antennary and tetra-antennary chains (in the ratio of 7:6:5:82), with the latter containing between zero and three repeating N-acetyllactosamine units, in well-defined branches.
8054720	10	102	theme	disialyl	1745:1752	arg1	tri-					1802:1805	a linear tri-	1793:1805	a linear tri-	1793:1805	The O-type mono- and disialyl oligosaccharides were characterized as a linear tri- and a branched tetra-saccharide, respectively.
8054720	10	102	theme	disialyl	1745:1752	arg1	tetra-saccharide					1822:1837	a branched tetra-saccharide	1811:1837	a branched tetra-saccharide	1811:1837	The O-type mono- and disialyl oligosaccharides were characterized as a linear tri- and a branched tetra-saccharide, respectively.
8054720	10	102	theme	disialyl	1745:1752	arg1	oligosaccharides					1754:1769	The O-type mono- and disialyl oligosaccharides	1724:1769	The O-type mono- and disialyl oligosaccharides	1724:1769	The O-type mono- and disialyl oligosaccharides were characterized as a linear tri- and a branched tetra-saccharide, respectively.
8054720	8	103	gly	sialylated	1475:1484	arg1	tri-					1429:1432	tri-	1429:1432	tri-	1429:1432	The major (> 95%) di-, tri- and tetra-antennary structures are fully sialylated, i.e. they have two, three and four sialic acid residues, respectively, linked exclusively alpha(2-->3) to galactose residues.
8054720	8	103	gly	sialylated	1475:1484	arg1	structures					1454:1463	tetra-antennary structures	1438:1463	tetra-antennary structures	1438:1463	The major (> 95%) di-, tri- and tetra-antennary structures are fully sialylated, i.e. they have two, three and four sialic acid residues, respectively, linked exclusively alpha(2-->3) to galactose residues.
8054720	8	103	gly	sialylated	1475:1484	arg1	di-					1424:1426	The major (> 95%) di-	1406:1426	The major (> 95%) di-	1406:1426	The major (> 95%) di-, tri- and tetra-antennary structures are fully sialylated, i.e. they have two, three and four sialic acid residues, respectively, linked exclusively alpha(2-->3) to galactose residues.
8054720	8	103	gly	sialylated	1475:1484	arg1	%					1421:1421	> 95%	1417:1421	> 95%	1417:1421	The major (> 95%) di-, tri- and tetra-antennary structures are fully sialylated, i.e. they have two, three and four sialic acid residues, respectively, linked exclusively alpha(2-->3) to galactose residues.
8054720	0	104	gly	sialylated	44:53	arg1	chains					71:76	the intact major sialylated oligosaccharide chains	27:76	the intact major sialylated oligosaccharide chains of recombinant human erythropoietin	27:112	Structure determination of the intact major sialylated oligosaccharide chains of recombinant human erythropoietin expressed in Chinese hamster ovary cells.
8054720	7	105	theme	repeating	1343:1351	arg1	units					1373:1377	between zero and three repeating N-acetyllactosamine units	1320:1377	between zero and three repeating N-acetyllactosamine units	1320:1377	The most abundant N-linked oligosaccharides in CHO cell-derived rHuEPO were found to be di-antennary, 2,4-branched tri-antennary, 2,6-branched tri-antennary and tetra-antennary chains (in the ratio of 7:6:5:82), with the latter containing between zero and three repeating N-acetyllactosamine units, in well-defined branches.
8054720	3	106	theme	rHuEPO	524:529	arg1	chains					514:519	the intact sialylated carbohydrate chains	479:519	the intact sialylated carbohydrate chains of rHuEPO expressed in Chinese hamster ovary (CHO) cells	479:576	Prompted by conflicting literature reports on the issue, we reinvestigated the structures of the intact sialylated carbohydrate chains of rHuEPO expressed in Chinese hamster ovary (CHO) cells.
8054720	1	107	theme	blood	248:252	arg1	cell					254:257	red blood cell	244:257	red blood cell growth in anaemic patients	244:284	Recombinant human erythropoietin (rHuEPO) is used abundantly in the clinic to stimulate red blood cell growth in anaemic patients.
1907570	0	0	theme	N-linked	81:88	arg1	oligosaccharides					105:120	sialo N-linked tetraantennary oligosaccharides	75:120	sialo N-linked tetraantennary oligosaccharides	75:120	Determination of the branch location of extra N-acetyllactosamine units in sialo N-linked tetraantennary oligosaccharides.
1907570	1	1	from	location	184:191	arg1	chains					266:271	sialo N-linked carbohydrate chains	238:271	sialo N-linked carbohydrate chains from glycoproteins	238:290	An approach is presented for the determination of the branch location of 1 or 2 extra N-acetyllactosamine units in sialo N-linked carbohydrate chains from glycoproteins.
1907570	1	1	from	location	184:191	arg1	glycoproteins					278:290	glycoproteins	278:290	glycoproteins	278:290	An approach is presented for the determination of the branch location of 1 or 2 extra N-acetyllactosamine units in sialo N-linked carbohydrate chains from glycoproteins.
1907570	1	2	theme	carbohydrate	253:264	arg1	chains					266:271	sialo N-linked carbohydrate chains	238:271	sialo N-linked carbohydrate chains from glycoproteins	238:290	An approach is presented for the determination of the branch location of 1 or 2 extra N-acetyllactosamine units in sialo N-linked carbohydrate chains from glycoproteins.
1907570	0	3	theme	sialo	75:79	arg1	oligosaccharides					105:120	sialo N-linked tetraantennary oligosaccharides	75:120	sialo N-linked tetraantennary oligosaccharides	75:120	Determination of the branch location of extra N-acetyllactosamine units in sialo N-linked tetraantennary oligosaccharides.
1907570	0	4	from	Determination	0:12	arg1	oligosaccharides					105:120	sialo N-linked tetraantennary oligosaccharides	75:120	sialo N-linked tetraantennary oligosaccharides	75:120	Determination of the branch location of extra N-acetyllactosamine units in sialo N-linked tetraantennary oligosaccharides.
1907570	0	5	theme	tetraantennary	90:103	arg1	oligosaccharides					105:120	sialo N-linked tetraantennary oligosaccharides	75:120	sialo N-linked tetraantennary oligosaccharides	75:120	Determination of the branch location of extra N-acetyllactosamine units in sialo N-linked tetraantennary oligosaccharides.
1907570	2	6	theme	extra	593:597	arg1	units					599:603	the extra units	589:603	the extra units in the intact structures	589:628	Tetraantennary oligosaccharides containing extra N-acetyllactosamine units were digested with endo-beta-galactosidase, followed by treatment with N-acetyl-beta-glucosaminidase, yielding products which could be analysed by 1H-NMR spectroscopy, thereby giving conclusive data about the location of the extra units in the intact structures.
1907570	1	7	from	determination	156:168	arg1	chains					266:271	sialo N-linked carbohydrate chains	238:271	sialo N-linked carbohydrate chains from glycoproteins	238:290	An approach is presented for the determination of the branch location of 1 or 2 extra N-acetyllactosamine units in sialo N-linked carbohydrate chains from glycoproteins.
1907570	2	8	theme	Tetraantennary	293:306	arg1	oligosaccharides					308:323	Tetraantennary oligosaccharides	293:323	Tetraantennary oligosaccharides containing extra N-acetyllactosamine units	293:366	Tetraantennary oligosaccharides containing extra N-acetyllactosamine units were digested with endo-beta-galactosidase, followed by treatment with N-acetyl-beta-glucosaminidase, yielding products which could be analysed by 1H-NMR spectroscopy, thereby giving conclusive data about the location of the extra units in the intact structures.
1907570	1	9	theme	branch	177:182	arg1	location					184:191	the branch location	173:191	the branch location of 1 or 2 extra N-acetyllactosamine units in sialo N-linked carbohydrate chains from glycoproteins	173:290	An approach is presented for the determination of the branch location of 1 or 2 extra N-acetyllactosamine units in sialo N-linked carbohydrate chains from glycoproteins.
1907570	1	10	theme	location	184:191	arg1	determination					156:168	the determination	152:168	the determination of the branch location of 1 or 2 extra N-acetyllactosamine units in sialo N-linked carbohydrate chains from glycoproteins	152:290	An approach is presented for the determination of the branch location of 1 or 2 extra N-acetyllactosamine units in sialo N-linked carbohydrate chains from glycoproteins.
1907570	2	11	theme	conclusive	551:560	arg1	data					562:565	conclusive data	551:565	conclusive data about the location of the extra units in the intact structures	551:628	Tetraantennary oligosaccharides containing extra N-acetyllactosamine units were digested with endo-beta-galactosidase, followed by treatment with N-acetyl-beta-glucosaminidase, yielding products which could be analysed by 1H-NMR spectroscopy, thereby giving conclusive data about the location of the extra units in the intact structures.
1907570	0	12	from	location	28:35	arg1	oligosaccharides					105:120	sialo N-linked tetraantennary oligosaccharides	75:120	sialo N-linked tetraantennary oligosaccharides	75:120	Determination of the branch location of extra N-acetyllactosamine units in sialo N-linked tetraantennary oligosaccharides.
1907570	1	13	link	N-linked	244:251	arg1	chains					266:271	sialo N-linked carbohydrate chains	238:271	sialo N-linked carbohydrate chains from glycoproteins	238:290	An approach is presented for the determination of the branch location of 1 or 2 extra N-acetyllactosamine units in sialo N-linked carbohydrate chains from glycoproteins.
1907570	2	14	with	treatment	424:432	arg1	N-acetyl-beta-glucosaminidase					439:467	N-acetyl-beta-glucosaminidase	439:467	N-acetyl-beta-glucosaminidase	439:467	Tetraantennary oligosaccharides containing extra N-acetyllactosamine units were digested with endo-beta-galactosidase, followed by treatment with N-acetyl-beta-glucosaminidase, yielding products which could be analysed by 1H-NMR spectroscopy, thereby giving conclusive data about the location of the extra units in the intact structures.
1907570	1	15	gly	glycoproteins	278:290	arg1	glycoproteins					278:290	glycoproteins	278:290	glycoproteins	278:290	An approach is presented for the determination of the branch location of 1 or 2 extra N-acetyllactosamine units in sialo N-linked carbohydrate chains from glycoproteins.
1907570	2	16	dep	digested	373:380	arg1	followed					412:419	followed	412:419	followed	412:419	Tetraantennary oligosaccharides containing extra N-acetyllactosamine units were digested with endo-beta-galactosidase, followed by treatment with N-acetyl-beta-glucosaminidase, yielding products which could be analysed by 1H-NMR spectroscopy, thereby giving conclusive data about the location of the extra units in the intact structures.
1907570	0	17	theme	branch	21:26	arg1	location					28:35	the branch location	17:35	the branch location of extra N-acetyllactosamine units in sialo N-linked tetraantennary oligosaccharides	17:120	Determination of the branch location of extra N-acetyllactosamine units in sialo N-linked tetraantennary oligosaccharides.
1907570	2	18	theme	N-acetyllactosamine	342:360	arg1	units					362:366	extra N-acetyllactosamine units	336:366	extra N-acetyllactosamine units	336:366	Tetraantennary oligosaccharides containing extra N-acetyllactosamine units were digested with endo-beta-galactosidase, followed by treatment with N-acetyl-beta-glucosaminidase, yielding products which could be analysed by 1H-NMR spectroscopy, thereby giving conclusive data about the location of the extra units in the intact structures.
1907570	1	19	from	glycoproteins	278:290	arg1	chains					266:271	sialo N-linked carbohydrate chains	238:271	sialo N-linked carbohydrate chains from glycoproteins	238:290	An approach is presented for the determination of the branch location of 1 or 2 extra N-acetyllactosamine units in sialo N-linked carbohydrate chains from glycoproteins.
1907570	1	19	from	glycoproteins	278:290	arg1	location					184:191	the branch location	173:191	the branch location of 1 or 2 extra N-acetyllactosamine units in sialo N-linked carbohydrate chains from glycoproteins	173:290	An approach is presented for the determination of the branch location of 1 or 2 extra N-acetyllactosamine units in sialo N-linked carbohydrate chains from glycoproteins.
1907570	2	20	theme	extra	336:340	arg1	units					362:366	extra N-acetyllactosamine units	336:366	extra N-acetyllactosamine units	336:366	Tetraantennary oligosaccharides containing extra N-acetyllactosamine units were digested with endo-beta-galactosidase, followed by treatment with N-acetyl-beta-glucosaminidase, yielding products which could be analysed by 1H-NMR spectroscopy, thereby giving conclusive data about the location of the extra units in the intact structures.
1907570	2	21	contain	containing	325:334	arg1	oligosaccharides					308:323	Tetraantennary oligosaccharides	293:323	Tetraantennary oligosaccharides containing extra N-acetyllactosamine units	293:366	Tetraantennary oligosaccharides containing extra N-acetyllactosamine units were digested with endo-beta-galactosidase, followed by treatment with N-acetyl-beta-glucosaminidase, yielding products which could be analysed by 1H-NMR spectroscopy, thereby giving conclusive data about the location of the extra units in the intact structures.
1907570	2	21	contain	containing	325:334	arg2	units					362:366	extra N-acetyllactosamine units	336:366	extra N-acetyllactosamine units	336:366	Tetraantennary oligosaccharides containing extra N-acetyllactosamine units were digested with endo-beta-galactosidase, followed by treatment with N-acetyl-beta-glucosaminidase, yielding products which could be analysed by 1H-NMR spectroscopy, thereby giving conclusive data about the location of the extra units in the intact structures.
1907570	2	22	theme	intact	612:617	arg1	structures					619:628	the intact structures	608:628	the intact structures	608:628	Tetraantennary oligosaccharides containing extra N-acetyllactosamine units were digested with endo-beta-galactosidase, followed by treatment with N-acetyl-beta-glucosaminidase, yielding products which could be analysed by 1H-NMR spectroscopy, thereby giving conclusive data about the location of the extra units in the intact structures.
1907570	1	23	theme	extra	203:207	arg1	units					229:233	1 or 2 extra N-acetyllactosamine units	196:233	1 or 2 extra N-acetyllactosamine units	196:233	An approach is presented for the determination of the branch location of 1 or 2 extra N-acetyllactosamine units in sialo N-linked carbohydrate chains from glycoproteins.
1907570	0	24	theme	location	28:35	arg1	Determination					0:12	Determination	0:12	Determination of the branch location of extra N-acetyllactosamine units in sialo N-linked tetraantennary oligosaccharides.	0:121	Determination of the branch location of extra N-acetyllactosamine units in sialo N-linked tetraantennary oligosaccharides.
1907570	1	25	from	chains	266:271	arg1	determination					156:168	the determination	152:168	the determination of the branch location of 1 or 2 extra N-acetyllactosamine units in sialo N-linked carbohydrate chains from glycoproteins	152:290	An approach is presented for the determination of the branch location of 1 or 2 extra N-acetyllactosamine units in sialo N-linked carbohydrate chains from glycoproteins.
1907570	2	26	theme	1H-NMR	515:520	arg1	spectroscopy					522:533	1H-NMR spectroscopy	515:533	1H-NMR spectroscopy	515:533	Tetraantennary oligosaccharides containing extra N-acetyllactosamine units were digested with endo-beta-galactosidase, followed by treatment with N-acetyl-beta-glucosaminidase, yielding products which could be analysed by 1H-NMR spectroscopy, thereby giving conclusive data about the location of the extra units in the intact structures.
1907570	0	27	link	N-linked	81:88	arg1	oligosaccharides					105:120	sialo N-linked tetraantennary oligosaccharides	75:120	sialo N-linked tetraantennary oligosaccharides	75:120	Determination of the branch location of extra N-acetyllactosamine units in sialo N-linked tetraantennary oligosaccharides.
1907570	1	28	theme	N-acetyllactosamine	209:227	arg1	units					229:233	1 or 2 extra N-acetyllactosamine units	196:233	1 or 2 extra N-acetyllactosamine units	196:233	An approach is presented for the determination of the branch location of 1 or 2 extra N-acetyllactosamine units in sialo N-linked carbohydrate chains from glycoproteins.
1907570	0	29	theme	N-acetyllactosamine	46:64	arg1	units					66:70	extra N-acetyllactosamine units	40:70	extra N-acetyllactosamine units	40:70	Determination of the branch location of extra N-acetyllactosamine units in sialo N-linked tetraantennary oligosaccharides.
1907570	2	30	from	location	577:584	arg1	structures					619:628	the intact structures	608:628	the intact structures	608:628	Tetraantennary oligosaccharides containing extra N-acetyllactosamine units were digested with endo-beta-galactosidase, followed by treatment with N-acetyl-beta-glucosaminidase, yielding products which could be analysed by 1H-NMR spectroscopy, thereby giving conclusive data about the location of the extra units in the intact structures.
1907570	2	31	theme	units	599:603	arg1	location					577:584	the location	573:584	the location of the extra units in the intact structures	573:628	Tetraantennary oligosaccharides containing extra N-acetyllactosamine units were digested with endo-beta-galactosidase, followed by treatment with N-acetyl-beta-glucosaminidase, yielding products which could be analysed by 1H-NMR spectroscopy, thereby giving conclusive data about the location of the extra units in the intact structures.
1907570	0	32	theme	extra	40:44	arg1	units					66:70	extra N-acetyllactosamine units	40:70	extra N-acetyllactosamine units	40:70	Determination of the branch location of extra N-acetyllactosamine units in sialo N-linked tetraantennary oligosaccharides.
1907570	1	33	theme	units	229:233	arg1	location					184:191	the branch location	173:191	the branch location of 1 or 2 extra N-acetyllactosamine units in sialo N-linked carbohydrate chains from glycoproteins	173:290	An approach is presented for the determination of the branch location of 1 or 2 extra N-acetyllactosamine units in sialo N-linked carbohydrate chains from glycoproteins.
1907570	0	34	from	oligosaccharides	105:120	arg1	Determination					0:12	Determination	0:12	Determination of the branch location of extra N-acetyllactosamine units in sialo N-linked tetraantennary oligosaccharides.	0:121	Determination of the branch location of extra N-acetyllactosamine units in sialo N-linked tetraantennary oligosaccharides.
1907570	2	35	from	units	599:603	arg1	structures					619:628	the intact structures	608:628	the intact structures	608:628	Tetraantennary oligosaccharides containing extra N-acetyllactosamine units were digested with endo-beta-galactosidase, followed by treatment with N-acetyl-beta-glucosaminidase, yielding products which could be analysed by 1H-NMR spectroscopy, thereby giving conclusive data about the location of the extra units in the intact structures.
1907570	1	36	theme	sialo	238:242	arg1	chains					266:271	sialo N-linked carbohydrate chains	238:271	sialo N-linked carbohydrate chains from glycoproteins	238:290	An approach is presented for the determination of the branch location of 1 or 2 extra N-acetyllactosamine units in sialo N-linked carbohydrate chains from glycoproteins.
1907570	0	37	theme	units	66:70	arg1	location					28:35	the branch location	17:35	the branch location of extra N-acetyllactosamine units in sialo N-linked tetraantennary oligosaccharides	17:120	Determination of the branch location of extra N-acetyllactosamine units in sialo N-linked tetraantennary oligosaccharides.
1907570	2	38	from	structures	619:628	arg1	location					577:584	the location	573:584	the location of the extra units in the intact structures	573:628	Tetraantennary oligosaccharides containing extra N-acetyllactosamine units were digested with endo-beta-galactosidase, followed by treatment with N-acetyl-beta-glucosaminidase, yielding products which could be analysed by 1H-NMR spectroscopy, thereby giving conclusive data about the location of the extra units in the intact structures.
1907570	1	39	theme	N-linked	244:251	arg1	chains					266:271	sialo N-linked carbohydrate chains	238:271	sialo N-linked carbohydrate chains from glycoproteins	238:290	An approach is presented for the determination of the branch location of 1 or 2 extra N-acetyllactosamine units in sialo N-linked carbohydrate chains from glycoproteins.
1443598	6	0	theme	asialooligosaccharides	923:944	arg1	kinds					901:905	Seven kinds	895:905	Seven kinds of complex-type asialooligosaccharides	895:944	Seven kinds of complex-type asialooligosaccharides were identified ranging from a biantennary structure to N-acetyllactosamine-extended tetraantennary structure.
1443598	1	1	theme	Chinese	319:325	arg1	cells					347:351	Chinese hamster ovary (CHO) cells	319:351	Chinese hamster ovary (CHO) cells	319:351	A rapid quantitative analysis of the sialylated N-linked oligosaccharides of recombinant erythropoietin (EPO) expressed in Chinese hamster ovary (CHO) cells has been developed.
1443598	1	2	gly	sialylated	233:242	arg1	oligosaccharides					253:268	the sialylated N-linked oligosaccharides	229:268	the sialylated N-linked oligosaccharides of recombinant erythropoietin (EPO) expressed in Chinese hamster ovary (CHO) cells	229:351	A rapid quantitative analysis of the sialylated N-linked oligosaccharides of recombinant erythropoietin (EPO) expressed in Chinese hamster ovary (CHO) cells has been developed.
1443598	1	3	theme	ovary	335:339	arg1	cells					347:351	Chinese hamster ovary (CHO) cells	319:351	Chinese hamster ovary (CHO) cells	319:351	A rapid quantitative analysis of the sialylated N-linked oligosaccharides of recombinant erythropoietin (EPO) expressed in Chinese hamster ovary (CHO) cells has been developed.
1443598	8	4	theme	N-linked	1379:1386	arg1	oligosaccharides					1388:1403	the N-linked oligosaccharides	1375:1403	the N-linked oligosaccharides	1375:1403	Quantitative oligosaccharide mapping of four different lots of EPO from CHO cells was performed to quantify the molar balance and distribution of the N-linked oligosaccharides.
1443598	6	5	theme	N-acetyllactosamine-extended	1002:1029	arg1	structure					1046:1054	N-acetyllactosamine-extended tetraantennary structure	1002:1054	N-acetyllactosamine-extended tetraantennary structure	1002:1054	Seven kinds of complex-type asialooligosaccharides were identified ranging from a biantennary structure to N-acetyllactosamine-extended tetraantennary structure.
1443598	1	6	theme	N-linked	244:251	arg1	oligosaccharides					253:268	the sialylated N-linked oligosaccharides	229:268	the sialylated N-linked oligosaccharides of recombinant erythropoietin (EPO) expressed in Chinese hamster ovary (CHO) cells	229:351	A rapid quantitative analysis of the sialylated N-linked oligosaccharides of recombinant erythropoietin (EPO) expressed in Chinese hamster ovary (CHO) cells has been developed.
1443598	8	7	theme	molar	1341:1345	arg1	balance					1347:1353	balance	1347:1353	balance	1347:1353	Quantitative oligosaccharide mapping of four different lots of EPO from CHO cells was performed to quantify the molar balance and distribution of the N-linked oligosaccharides.
1443598	5	8	dep	171	882:884	arg1	73-90					887:891	73-90	887:891	73-90	887:891	171, 73-90).
1443598	0	9	link	N-linked	28:35	arg1	sialyloligosaccharides					37:58	the N-linked sialyloligosaccharides	24:58	the N-linked sialyloligosaccharides of recombinant erythropoietin	24:88	Quantitative mapping of the N-linked sialyloligosaccharides of recombinant erythropoietin: combination of direct high-performance anion-exchange chromatography and 2-aminopyridine derivatization.
1443598	7	10	theme	sialic	1216:1221	arg1	acid					1223:1226	an alpha(2-->3)-linked sialic acid	1193:1226	an alpha(2-->3)-linked sialic acid	1193:1226	Approximately 3% of the terminal galactose residues of the oligosaccharides released from EPO were not sialylated whereas 97% contained an alpha(2-->3)-linked sialic acid.
1443598	9	11	theme	average	1593:1599	arg1	recovery					1607:1614	an average molar recovery	1590:1614	an average molar recovery of 85% starting from 750 pmol of EPO	1590:1651	The sialyloligosaccharides were distributed with approximately 5% disialylated (single type), 20% trisialylated (six types), and 75% tetrasialylated (four types) oligosaccharides with an average molar recovery of 85% starting from 750 pmol of EPO.
1443598	9	12	theme	tetrasialylated	1539:1553	arg1	oligosaccharides					1568:1583	approximately 5% disialylated (single type), 20% trisialylated (six types), and 75% tetrasialylated (four types) oligosaccharides	1455:1583	approximately 5% disialylated (single type), 20% trisialylated (six types), and 75% tetrasialylated (four types) oligosaccharides with an average molar recovery of 85% starting from 750 pmol of EPO	1455:1651	The sialyloligosaccharides were distributed with approximately 5% disialylated (single type), 20% trisialylated (six types), and 75% tetrasialylated (four types) oligosaccharides with an average molar recovery of 85% starting from 750 pmol of EPO.
1443598	1	13	theme	erythropoietin	285:298	arg1	oligosaccharides					253:268	the sialylated N-linked oligosaccharides	229:268	the sialylated N-linked oligosaccharides of recombinant erythropoietin (EPO) expressed in Chinese hamster ovary (CHO) cells	229:351	A rapid quantitative analysis of the sialylated N-linked oligosaccharides of recombinant erythropoietin (EPO) expressed in Chinese hamster ovary (CHO) cells has been developed.
1443598	2	14	theme	high-performance	558:573	arg1	chromatography					590:603	high-performance anion-exchange chromatography	558:603	high-performance anion-exchange chromatography (HPAEC) with pulsed amperometric detection	558:646	The procedure utilizes a glycoamidase (glycopeptidase F) to release all of the N-linked oligosaccharides from the native glycoprotein, followed by direct chromatographic analysis using high-performance anion-exchange chromatography (HPAEC) with pulsed amperometric detection.
1443598	2	14	theme	high-performance	558:573	arg1	HPAEC					606:610	HPAEC	606:610	HPAEC	606:610	The procedure utilizes a glycoamidase (glycopeptidase F) to release all of the N-linked oligosaccharides from the native glycoprotein, followed by direct chromatographic analysis using high-performance anion-exchange chromatography (HPAEC) with pulsed amperometric detection.
1443598	9	15	dep	tetrasialylated	1539:1553	arg1	types					1561:1565	four types	1556:1565	four types	1556:1565	The sialyloligosaccharides were distributed with approximately 5% disialylated (single type), 20% trisialylated (six types), and 75% tetrasialylated (four types) oligosaccharides with an average molar recovery of 85% starting from 750 pmol of EPO.
1443598	0	16	theme	erythropoietin	75:88	arg1	sialyloligosaccharides					37:58	the N-linked sialyloligosaccharides	24:58	the N-linked sialyloligosaccharides of recombinant erythropoietin	24:88	Quantitative mapping of the N-linked sialyloligosaccharides of recombinant erythropoietin: combination of direct high-performance anion-exchange chromatography and 2-aminopyridine derivatization.
1443598	1	17	theme	rapid	198:202	arg1	analysis					217:224	A rapid quantitative analysis	196:224	A rapid quantitative analysis of the sialylated N-linked oligosaccharides of recombinant erythropoietin (EPO) expressed in Chinese hamster ovary (CHO) cells	196:351	A rapid quantitative analysis of the sialylated N-linked oligosaccharides of recombinant erythropoietin (EPO) expressed in Chinese hamster ovary (CHO) cells has been developed.
1443598	7	18	theme	oligosaccharides	1116:1131	arg1	residues					1100:1107	the terminal galactose residues	1077:1107	the terminal galactose residues of the oligosaccharides released from EPO	1077:1149	Approximately 3% of the terminal galactose residues of the oligosaccharides released from EPO were not sialylated whereas 97% contained an alpha(2-->3)-linked sialic acid.
1443598	7	18	theme	oligosaccharides	1116:1131	arg1	oligosaccharides					1116:1131	the oligosaccharides	1112:1131	the oligosaccharides released from EPO	1112:1149	Approximately 3% of the terminal galactose residues of the oligosaccharides released from EPO were not sialylated whereas 97% contained an alpha(2-->3)-linked sialic acid.
1443598	3	19	attach	isolated	682:689	arg2	sialyloligosaccharides					659:680	The eight sialyloligosaccharides	649:680	The eight sialyloligosaccharides isolated from HPAEC	649:700	The eight sialyloligosaccharides isolated from HPAEC were characterized by derivatizing with 2-aminopyridine followed by two-dimensional HPLC mapping of the pyridylaminated asialooligosaccharides (Tomiya et al., 1988, Anal.
1443598	3	19	attach	isolated	682:689	arg1	HPAEC					696:700	HPAEC	696:700	HPAEC	696:700	The eight sialyloligosaccharides isolated from HPAEC were characterized by derivatizing with 2-aminopyridine followed by two-dimensional HPLC mapping of the pyridylaminated asialooligosaccharides (Tomiya et al., 1988, Anal.
1443598	0	20	theme	direct	106:111	arg1	chromatography					145:158	direct high-performance anion-exchange chromatography	106:158	direct high-performance anion-exchange chromatography	106:158	Quantitative mapping of the N-linked sialyloligosaccharides of recombinant erythropoietin: combination of direct high-performance anion-exchange chromatography and 2-aminopyridine derivatization.
1443598	9	21	theme	disialylated	1472:1483	arg1	%					1470:1470	approximately 5% disialylated	1455:1483	approximately 5% disialylated (single type)	1455:1497	The sialyloligosaccharides were distributed with approximately 5% disialylated (single type), 20% trisialylated (six types), and 75% tetrasialylated (four types) oligosaccharides with an average molar recovery of 85% starting from 750 pmol of EPO.
1443598	9	21	theme	disialylated	1472:1483	arg1	type					1493:1496	single type	1486:1496	single type	1486:1496	The sialyloligosaccharides were distributed with approximately 5% disialylated (single type), 20% trisialylated (six types), and 75% tetrasialylated (four types) oligosaccharides with an average molar recovery of 85% starting from 750 pmol of EPO.
1443598	8	22	from	mapping	1258:1264	arg1	cells					1305:1309	CHO cells	1301:1309	CHO cells	1301:1309	Quantitative oligosaccharide mapping of four different lots of EPO from CHO cells was performed to quantify the molar balance and distribution of the N-linked oligosaccharides.
1443598	7	23	contain	contained	1183:1191	arg2	acid					1223:1226	an alpha(2-->3)-linked sialic acid	1193:1226	an alpha(2-->3)-linked sialic acid	1193:1226	Approximately 3% of the terminal galactose residues of the oligosaccharides released from EPO were not sialylated whereas 97% contained an alpha(2-->3)-linked sialic acid.
1443598	7	23	contain	contained	1183:1191	arg1	%					1181:1181	97%	1179:1181	97%	1179:1181	Approximately 3% of the terminal galactose residues of the oligosaccharides released from EPO were not sialylated whereas 97% contained an alpha(2-->3)-linked sialic acid.
1443598	0	24	theme	anion-exchange	130:143	arg1	chromatography					145:158	direct high-performance anion-exchange chromatography	106:158	direct high-performance anion-exchange chromatography	106:158	Quantitative mapping of the N-linked sialyloligosaccharides of recombinant erythropoietin: combination of direct high-performance anion-exchange chromatography and 2-aminopyridine derivatization.
1443598	9	25	theme	single	1486:1491	arg1	%					1470:1470	approximately 5% disialylated	1455:1483	approximately 5% disialylated (single type)	1455:1497	The sialyloligosaccharides were distributed with approximately 5% disialylated (single type), 20% trisialylated (six types), and 75% tetrasialylated (four types) oligosaccharides with an average molar recovery of 85% starting from 750 pmol of EPO.
1443598	9	25	theme	single	1486:1491	arg1	type					1493:1496	single type	1486:1496	single type	1486:1496	The sialyloligosaccharides were distributed with approximately 5% disialylated (single type), 20% trisialylated (six types), and 75% tetrasialylated (four types) oligosaccharides with an average molar recovery of 85% starting from 750 pmol of EPO.
1443598	7	26	attach	released	1133:1140	arg2	oligosaccharides					1116:1131	the oligosaccharides	1112:1131	the oligosaccharides released from EPO	1112:1149	Approximately 3% of the terminal galactose residues of the oligosaccharides released from EPO were not sialylated whereas 97% contained an alpha(2-->3)-linked sialic acid.
1443598	7	26	attach	released	1133:1140	arg1	EPO					1147:1149	EPO	1147:1149	EPO	1147:1149	Approximately 3% of the terminal galactose residues of the oligosaccharides released from EPO were not sialylated whereas 97% contained an alpha(2-->3)-linked sialic acid.
1443598	2	27	with	chromatography	590:603	arg1	detection					638:646	pulsed amperometric detection	618:646	pulsed amperometric detection	618:646	The procedure utilizes a glycoamidase (glycopeptidase F) to release all of the N-linked oligosaccharides from the native glycoprotein, followed by direct chromatographic analysis using high-performance anion-exchange chromatography (HPAEC) with pulsed amperometric detection.
1443598	0	28	theme	Quantitative	0:11	arg1	mapping					13:19	Quantitative mapping	0:19	Quantitative mapping of the N-linked sialyloligosaccharides of recombinant erythropoietin: combination of direct high-performance anion-exchange chromatography and 2-aminopyridine derivatization.	0:194	Quantitative mapping of the N-linked sialyloligosaccharides of recombinant erythropoietin: combination of direct high-performance anion-exchange chromatography and 2-aminopyridine derivatization.
1443598	2	29	theme	direct	520:525	arg1	analysis					543:550	direct chromatographic analysis	520:550	direct chromatographic analysis using high-performance anion-exchange chromatography (HPAEC) with pulsed amperometric detection	520:646	The procedure utilizes a glycoamidase (glycopeptidase F) to release all of the N-linked oligosaccharides from the native glycoprotein, followed by direct chromatographic analysis using high-performance anion-exchange chromatography (HPAEC) with pulsed amperometric detection.
1443598	0	30	theme	N-linked	28:35	arg1	sialyloligosaccharides					37:58	the N-linked sialyloligosaccharides	24:58	the N-linked sialyloligosaccharides of recombinant erythropoietin	24:88	Quantitative mapping of the N-linked sialyloligosaccharides of recombinant erythropoietin: combination of direct high-performance anion-exchange chromatography and 2-aminopyridine derivatization.
1443598	9	31	theme	trisialylated	1504:1516	arg1	%					1502:1502	20% trisialylated	1500:1516	20% trisialylated (six types)	1500:1528	The sialyloligosaccharides were distributed with approximately 5% disialylated (single type), 20% trisialylated (six types), and 75% tetrasialylated (four types) oligosaccharides with an average molar recovery of 85% starting from 750 pmol of EPO.
1443598	9	31	theme	trisialylated	1504:1516	arg1	types					1523:1527	six types	1519:1527	six types	1519:1527	The sialyloligosaccharides were distributed with approximately 5% disialylated (single type), 20% trisialylated (six types), and 75% tetrasialylated (four types) oligosaccharides with an average molar recovery of 85% starting from 750 pmol of EPO.
1443598	8	32	theme	Quantitative	1229:1240	arg1	mapping					1258:1264	Quantitative oligosaccharide mapping	1229:1264	Quantitative oligosaccharide mapping of four different lots of EPO from CHO cells	1229:1309	Quantitative oligosaccharide mapping of four different lots of EPO from CHO cells was performed to quantify the molar balance and distribution of the N-linked oligosaccharides.
1443598	6	33	theme	biantennary	977:987	arg1	structure					989:997	a biantennary structure	975:997	a biantennary structure	975:997	Seven kinds of complex-type asialooligosaccharides were identified ranging from a biantennary structure to N-acetyllactosamine-extended tetraantennary structure.
1443598	9	34	with	oligosaccharides	1568:1583	arg1	recovery					1607:1614	an average molar recovery	1590:1614	an average molar recovery of 85% starting from 750 pmol of EPO	1590:1651	The sialyloligosaccharides were distributed with approximately 5% disialylated (single type), 20% trisialylated (six types), and 75% tetrasialylated (four types) oligosaccharides with an average molar recovery of 85% starting from 750 pmol of EPO.
1443598	8	35	link	N-linked	1379:1386	arg1	oligosaccharides					1388:1403	the N-linked oligosaccharides	1375:1403	the N-linked oligosaccharides	1375:1403	Quantitative oligosaccharide mapping of four different lots of EPO from CHO cells was performed to quantify the molar balance and distribution of the N-linked oligosaccharides.
1443598	7	36	gly	sialylated	1160:1169	arg1	oligosaccharides					1116:1131	the oligosaccharides	1112:1131	the oligosaccharides released from EPO	1112:1149	Approximately 3% of the terminal galactose residues of the oligosaccharides released from EPO were not sialylated whereas 97% contained an alpha(2-->3)-linked sialic acid.
1443598	7	36	gly	sialylated	1160:1169	arg1	residues					1100:1107	the terminal galactose residues	1077:1107	the terminal galactose residues of the oligosaccharides released from EPO	1077:1149	Approximately 3% of the terminal galactose residues of the oligosaccharides released from EPO were not sialylated whereas 97% contained an alpha(2-->3)-linked sialic acid.
1443598	7	36	gly	sialylated	1160:1169	arg1	%					1072:1072	Approximately 3%	1057:1072	Approximately 3% of the terminal galactose residues of the oligosaccharides released from EPO	1057:1149	Approximately 3% of the terminal galactose residues of the oligosaccharides released from EPO were not sialylated whereas 97% contained an alpha(2-->3)-linked sialic acid.
1443598	9	37	gly	tetrasialylated	1539:1553	arg1	oligosaccharides					1568:1583	approximately 5% disialylated (single type), 20% trisialylated (six types), and 75% tetrasialylated (four types) oligosaccharides	1455:1583	approximately 5% disialylated (single type), 20% trisialylated (six types), and 75% tetrasialylated (four types) oligosaccharides with an average molar recovery of 85% starting from 750 pmol of EPO	1455:1651	The sialyloligosaccharides were distributed with approximately 5% disialylated (single type), 20% trisialylated (six types), and 75% tetrasialylated (four types) oligosaccharides with an average molar recovery of 85% starting from 750 pmol of EPO.
1443598	8	38	from	cells	1305:1309	arg1	EPO					1292:1294	EPO	1292:1294	EPO	1292:1294	Quantitative oligosaccharide mapping of four different lots of EPO from CHO cells was performed to quantify the molar balance and distribution of the N-linked oligosaccharides.
1443598	8	38	from	cells	1305:1309	arg1	lots					1284:1287	four different lots	1269:1287	four different lots of EPO from CHO cells	1269:1309	Quantitative oligosaccharide mapping of four different lots of EPO from CHO cells was performed to quantify the molar balance and distribution of the N-linked oligosaccharides.
1443598	8	38	from	cells	1305:1309	arg1	mapping					1258:1264	Quantitative oligosaccharide mapping	1229:1264	Quantitative oligosaccharide mapping of four different lots of EPO from CHO cells	1229:1309	Quantitative oligosaccharide mapping of four different lots of EPO from CHO cells was performed to quantify the molar balance and distribution of the N-linked oligosaccharides.
1443598	2	39	gly	glycoprotein	494:505	arg1	glycoprotein					494:505	the native glycoprotein	483:505	the native glycoprotein	483:505	The procedure utilizes a glycoamidase (glycopeptidase F) to release all of the N-linked oligosaccharides from the native glycoprotein, followed by direct chromatographic analysis using high-performance anion-exchange chromatography (HPAEC) with pulsed amperometric detection.
1443598	3	40	theme	HPLC	786:789	arg1	mapping					791:797	two-dimensional HPLC mapping	770:797	two-dimensional HPLC mapping of the pyridylaminated asialooligosaccharides	770:843	The eight sialyloligosaccharides isolated from HPAEC were characterized by derivatizing with 2-aminopyridine followed by two-dimensional HPLC mapping of the pyridylaminated asialooligosaccharides (Tomiya et al., 1988, Anal.
1443598	3	41	dep	followed	758:765	arg1	Anal					867:870	Anal	867:870	Anal	867:870	The eight sialyloligosaccharides isolated from HPAEC were characterized by derivatizing with 2-aminopyridine followed by two-dimensional HPLC mapping of the pyridylaminated asialooligosaccharides (Tomiya et al., 1988, Anal.
1443598	3	41	dep	followed	758:765	arg1	Tomiya					846:851	Tomiya	846:851	Tomiya	846:851	The eight sialyloligosaccharides isolated from HPAEC were characterized by derivatizing with 2-aminopyridine followed by two-dimensional HPLC mapping of the pyridylaminated asialooligosaccharides (Tomiya et al., 1988, Anal.
1443598	8	42	theme	lots	1284:1287	arg1	mapping					1258:1264	Quantitative oligosaccharide mapping	1229:1264	Quantitative oligosaccharide mapping of four different lots of EPO from CHO cells	1229:1309	Quantitative oligosaccharide mapping of four different lots of EPO from CHO cells was performed to quantify the molar balance and distribution of the N-linked oligosaccharides.
1443598	2	43	theme	amperometric	625:636	arg1	detection					638:646	pulsed amperometric detection	618:646	pulsed amperometric detection	618:646	The procedure utilizes a glycoamidase (glycopeptidase F) to release all of the N-linked oligosaccharides from the native glycoprotein, followed by direct chromatographic analysis using high-performance anion-exchange chromatography (HPAEC) with pulsed amperometric detection.
1443598	7	44	link	-linked	1208:1214	arg1	acid					1223:1226	an alpha(2-->3)-linked sialic acid	1193:1226	an alpha(2-->3)-linked sialic acid	1193:1226	Approximately 3% of the terminal galactose residues of the oligosaccharides released from EPO were not sialylated whereas 97% contained an alpha(2-->3)-linked sialic acid.
1443598	8	45	theme	EPO	1292:1294	arg1	EPO					1292:1294	EPO	1292:1294	EPO	1292:1294	Quantitative oligosaccharide mapping of four different lots of EPO from CHO cells was performed to quantify the molar balance and distribution of the N-linked oligosaccharides.
1443598	8	45	theme	EPO	1292:1294	arg1	lots					1284:1287	four different lots	1269:1287	four different lots of EPO from CHO cells	1269:1309	Quantitative oligosaccharide mapping of four different lots of EPO from CHO cells was performed to quantify the molar balance and distribution of the N-linked oligosaccharides.
1443598	9	46	from	pmol	1641:1644	arg1	recovery					1607:1614	an average molar recovery	1590:1614	an average molar recovery of 85% starting from 750 pmol of EPO	1590:1651	The sialyloligosaccharides were distributed with approximately 5% disialylated (single type), 20% trisialylated (six types), and 75% tetrasialylated (four types) oligosaccharides with an average molar recovery of 85% starting from 750 pmol of EPO.
1443598	3	47	theme	pyridylaminated	806:820	arg1	asialooligosaccharides					822:843	the pyridylaminated asialooligosaccharides	802:843	the pyridylaminated asialooligosaccharides	802:843	The eight sialyloligosaccharides isolated from HPAEC were characterized by derivatizing with 2-aminopyridine followed by two-dimensional HPLC mapping of the pyridylaminated asialooligosaccharides (Tomiya et al., 1988, Anal.
1443598	6	48	theme	complex-type	910:921	arg1	asialooligosaccharides					923:944	complex-type asialooligosaccharides	910:944	complex-type asialooligosaccharides	910:944	Seven kinds of complex-type asialooligosaccharides were identified ranging from a biantennary structure to N-acetyllactosamine-extended tetraantennary structure.
1443598	1	49	theme	hamster	327:333	arg1	cells					347:351	Chinese hamster ovary (CHO) cells	319:351	Chinese hamster ovary (CHO) cells	319:351	A rapid quantitative analysis of the sialylated N-linked oligosaccharides of recombinant erythropoietin (EPO) expressed in Chinese hamster ovary (CHO) cells has been developed.
1443598	8	50	theme	CHO	1301:1303	arg1	cells					1305:1309	CHO cells	1301:1309	CHO cells	1301:1309	Quantitative oligosaccharide mapping of four different lots of EPO from CHO cells was performed to quantify the molar balance and distribution of the N-linked oligosaccharides.
1443598	6	51	theme	tetraantennary	1031:1044	arg1	structure					1046:1054	N-acetyllactosamine-extended tetraantennary structure	1002:1054	N-acetyllactosamine-extended tetraantennary structure	1002:1054	Seven kinds of complex-type asialooligosaccharides were identified ranging from a biantennary structure to N-acetyllactosamine-extended tetraantennary structure.
1443598	1	52	theme	sialylated	233:242	arg1	oligosaccharides					253:268	the sialylated N-linked oligosaccharides	229:268	the sialylated N-linked oligosaccharides of recombinant erythropoietin (EPO) expressed in Chinese hamster ovary (CHO) cells	229:351	A rapid quantitative analysis of the sialylated N-linked oligosaccharides of recombinant erythropoietin (EPO) expressed in Chinese hamster ovary (CHO) cells has been developed.
1443598	8	53	theme	oligosaccharides	1388:1403	arg1	distribution					1359:1370	distribution	1359:1370	distribution	1359:1370	Quantitative oligosaccharide mapping of four different lots of EPO from CHO cells was performed to quantify the molar balance and distribution of the N-linked oligosaccharides.
1443598	8	53	theme	oligosaccharides	1388:1403	arg1	balance					1347:1353	balance	1347:1353	balance	1347:1353	Quantitative oligosaccharide mapping of four different lots of EPO from CHO cells was performed to quantify the molar balance and distribution of the N-linked oligosaccharides.
1443598	7	54	theme	-linked	1208:1214	arg1	acid					1223:1226	an alpha(2-->3)-linked sialic acid	1193:1226	an alpha(2-->3)-linked sialic acid	1193:1226	Approximately 3% of the terminal galactose residues of the oligosaccharides released from EPO were not sialylated whereas 97% contained an alpha(2-->3)-linked sialic acid.
1443598	1	55	theme	oligosaccharides	253:268	arg1	analysis					217:224	A rapid quantitative analysis	196:224	A rapid quantitative analysis of the sialylated N-linked oligosaccharides of recombinant erythropoietin (EPO) expressed in Chinese hamster ovary (CHO) cells	196:351	A rapid quantitative analysis of the sialylated N-linked oligosaccharides of recombinant erythropoietin (EPO) expressed in Chinese hamster ovary (CHO) cells has been developed.
1443598	2	56	theme	pulsed	618:623	arg1	detection					638:646	pulsed amperometric detection	618:646	pulsed amperometric detection	618:646	The procedure utilizes a glycoamidase (glycopeptidase F) to release all of the N-linked oligosaccharides from the native glycoprotein, followed by direct chromatographic analysis using high-performance anion-exchange chromatography (HPAEC) with pulsed amperometric detection.
1443598	9	57	theme	molar	1601:1605	arg1	recovery					1607:1614	an average molar recovery	1590:1614	an average molar recovery of 85% starting from 750 pmol of EPO	1590:1651	The sialyloligosaccharides were distributed with approximately 5% disialylated (single type), 20% trisialylated (six types), and 75% tetrasialylated (four types) oligosaccharides with an average molar recovery of 85% starting from 750 pmol of EPO.
1443598	0	58	theme	2-aminopyridine	164:178	arg1	derivatization					180:193	2-aminopyridine derivatization	164:193	2-aminopyridine derivatization	164:193	Quantitative mapping of the N-linked sialyloligosaccharides of recombinant erythropoietin: combination of direct high-performance anion-exchange chromatography and 2-aminopyridine derivatization.
1443598	9	59	theme	%	1621:1621	arg1	recovery					1607:1614	an average molar recovery	1590:1614	an average molar recovery of 85% starting from 750 pmol of EPO	1590:1651	The sialyloligosaccharides were distributed with approximately 5% disialylated (single type), 20% trisialylated (six types), and 75% tetrasialylated (four types) oligosaccharides with an average molar recovery of 85% starting from 750 pmol of EPO.
1443598	9	60	gly	disialylated	1472:1483	arg1	%					1470:1470	approximately 5% disialylated	1455:1483	approximately 5% disialylated (single type)	1455:1497	The sialyloligosaccharides were distributed with approximately 5% disialylated (single type), 20% trisialylated (six types), and 75% tetrasialylated (four types) oligosaccharides with an average molar recovery of 85% starting from 750 pmol of EPO.
1443598	9	60	gly	disialylated	1472:1483	arg1	type					1493:1496	single type	1486:1496	single type	1486:1496	The sialyloligosaccharides were distributed with approximately 5% disialylated (single type), 20% trisialylated (six types), and 75% tetrasialylated (four types) oligosaccharides with an average molar recovery of 85% starting from 750 pmol of EPO.
1443598	1	61	theme	quantitative	204:215	arg1	analysis					217:224	A rapid quantitative analysis	196:224	A rapid quantitative analysis of the sialylated N-linked oligosaccharides of recombinant erythropoietin (EPO) expressed in Chinese hamster ovary (CHO) cells	196:351	A rapid quantitative analysis of the sialylated N-linked oligosaccharides of recombinant erythropoietin (EPO) expressed in Chinese hamster ovary (CHO) cells has been developed.
1443598	2	62	theme	chromatographic	527:541	arg1	analysis					543:550	direct chromatographic analysis	520:550	direct chromatographic analysis using high-performance anion-exchange chromatography (HPAEC) with pulsed amperometric detection	520:646	The procedure utilizes a glycoamidase (glycopeptidase F) to release all of the N-linked oligosaccharides from the native glycoprotein, followed by direct chromatographic analysis using high-performance anion-exchange chromatography (HPAEC) with pulsed amperometric detection.
1443598	2	63	from	glycoprotein	494:505	arg1	oligosaccharides					461:476	the N-linked oligosaccharides	448:476	the N-linked oligosaccharides	448:476	The procedure utilizes a glycoamidase (glycopeptidase F) to release all of the N-linked oligosaccharides from the native glycoprotein, followed by direct chromatographic analysis using high-performance anion-exchange chromatography (HPAEC) with pulsed amperometric detection.
1443598	0	64	theme	high-performance	113:128	arg1	chromatography					145:158	direct high-performance anion-exchange chromatography	106:158	direct high-performance anion-exchange chromatography	106:158	Quantitative mapping of the N-linked sialyloligosaccharides of recombinant erythropoietin: combination of direct high-performance anion-exchange chromatography and 2-aminopyridine derivatization.
1443598	9	65	theme	EPO	1649:1651	arg1	pmol					1641:1644	750 pmol	1637:1644	750 pmol of EPO	1637:1651	The sialyloligosaccharides were distributed with approximately 5% disialylated (single type), 20% trisialylated (six types), and 75% tetrasialylated (four types) oligosaccharides with an average molar recovery of 85% starting from 750 pmol of EPO.
1443598	0	66	theme	chromatography	145:158	arg1	combination					91:101	combination	91:101	Quantitative mapping of the N-linked sialyloligosaccharides of recombinant erythropoietin: combination of direct high-performance anion-exchange chromatography and 2-aminopyridine derivatization.	0:194	Quantitative mapping of the N-linked sialyloligosaccharides of recombinant erythropoietin: combination of direct high-performance anion-exchange chromatography and 2-aminopyridine derivatization.
1443598	2	67	theme	anion-exchange	575:588	arg1	chromatography					590:603	high-performance anion-exchange chromatography	558:603	high-performance anion-exchange chromatography (HPAEC) with pulsed amperometric detection	558:646	The procedure utilizes a glycoamidase (glycopeptidase F) to release all of the N-linked oligosaccharides from the native glycoprotein, followed by direct chromatographic analysis using high-performance anion-exchange chromatography (HPAEC) with pulsed amperometric detection.
1443598	2	67	theme	anion-exchange	575:588	arg1	HPAEC					606:610	HPAEC	606:610	HPAEC	606:610	The procedure utilizes a glycoamidase (glycopeptidase F) to release all of the N-linked oligosaccharides from the native glycoprotein, followed by direct chromatographic analysis using high-performance anion-exchange chromatography (HPAEC) with pulsed amperometric detection.
1443598	1	68	link	N-linked	244:251	arg1	oligosaccharides					253:268	the sialylated N-linked oligosaccharides	229:268	the sialylated N-linked oligosaccharides of recombinant erythropoietin (EPO) expressed in Chinese hamster ovary (CHO) cells	229:351	A rapid quantitative analysis of the sialylated N-linked oligosaccharides of recombinant erythropoietin (EPO) expressed in Chinese hamster ovary (CHO) cells has been developed.
1443598	7	69	theme	residues	1100:1107	arg1	oligosaccharides					1116:1131	the oligosaccharides	1112:1131	the oligosaccharides released from EPO	1112:1149	Approximately 3% of the terminal galactose residues of the oligosaccharides released from EPO were not sialylated whereas 97% contained an alpha(2-->3)-linked sialic acid.
1443598	7	69	theme	residues	1100:1107	arg1	residues					1100:1107	the terminal galactose residues	1077:1107	the terminal galactose residues of the oligosaccharides released from EPO	1077:1149	Approximately 3% of the terminal galactose residues of the oligosaccharides released from EPO were not sialylated whereas 97% contained an alpha(2-->3)-linked sialic acid.
1443598	7	69	theme	residues	1100:1107	arg1	%					1072:1072	Approximately 3%	1057:1072	Approximately 3% of the terminal galactose residues of the oligosaccharides released from EPO	1057:1149	Approximately 3% of the terminal galactose residues of the oligosaccharides released from EPO were not sialylated whereas 97% contained an alpha(2-->3)-linked sialic acid.
1443598	2	70	theme	native	487:492	arg1	glycoprotein					494:505	the native glycoprotein	483:505	the native glycoprotein	483:505	The procedure utilizes a glycoamidase (glycopeptidase F) to release all of the N-linked oligosaccharides from the native glycoprotein, followed by direct chromatographic analysis using high-performance anion-exchange chromatography (HPAEC) with pulsed amperometric detection.
1443598	2	71	link	N-linked	452:459	arg1	oligosaccharides					461:476	the N-linked oligosaccharides	448:476	the N-linked oligosaccharides	448:476	The procedure utilizes a glycoamidase (glycopeptidase F) to release all of the N-linked oligosaccharides from the native glycoprotein, followed by direct chromatographic analysis using high-performance anion-exchange chromatography (HPAEC) with pulsed amperometric detection.
1443598	9	72	gly	trisialylated	1504:1516	arg1	%					1502:1502	20% trisialylated	1500:1516	20% trisialylated (six types)	1500:1528	The sialyloligosaccharides were distributed with approximately 5% disialylated (single type), 20% trisialylated (six types), and 75% tetrasialylated (four types) oligosaccharides with an average molar recovery of 85% starting from 750 pmol of EPO.
1443598	9	72	gly	trisialylated	1504:1516	arg1	types					1523:1527	six types	1519:1527	six types	1519:1527	The sialyloligosaccharides were distributed with approximately 5% disialylated (single type), 20% trisialylated (six types), and 75% tetrasialylated (four types) oligosaccharides with an average molar recovery of 85% starting from 750 pmol of EPO.
1443598	1	73	theme	CHO	342:344	arg1	cells					347:351	Chinese hamster ovary (CHO) cells	319:351	Chinese hamster ovary (CHO) cells	319:351	A rapid quantitative analysis of the sialylated N-linked oligosaccharides of recombinant erythropoietin (EPO) expressed in Chinese hamster ovary (CHO) cells has been developed.
1443598	7	74	theme	terminal	1081:1088	arg1	residues					1100:1107	the terminal galactose residues	1077:1107	the terminal galactose residues of the oligosaccharides released from EPO	1077:1149	Approximately 3% of the terminal galactose residues of the oligosaccharides released from EPO were not sialylated whereas 97% contained an alpha(2-->3)-linked sialic acid.
1443598	7	74	theme	terminal	1081:1088	arg1	oligosaccharides					1116:1131	the oligosaccharides	1112:1131	the oligosaccharides released from EPO	1112:1149	Approximately 3% of the terminal galactose residues of the oligosaccharides released from EPO were not sialylated whereas 97% contained an alpha(2-->3)-linked sialic acid.
1443598	2	75	theme	N-linked	452:459	arg1	oligosaccharides					461:476	the N-linked oligosaccharides	448:476	the N-linked oligosaccharides	448:476	The procedure utilizes a glycoamidase (glycopeptidase F) to release all of the N-linked oligosaccharides from the native glycoprotein, followed by direct chromatographic analysis using high-performance anion-exchange chromatography (HPAEC) with pulsed amperometric detection.
1443598	0	76	theme	sialyloligosaccharides	37:58	arg1	mapping					13:19	Quantitative mapping	0:19	Quantitative mapping of the N-linked sialyloligosaccharides of recombinant erythropoietin: combination of direct high-performance anion-exchange chromatography and 2-aminopyridine derivatization.	0:194	Quantitative mapping of the N-linked sialyloligosaccharides of recombinant erythropoietin: combination of direct high-performance anion-exchange chromatography and 2-aminopyridine derivatization.
1443598	8	77	theme	oligosaccharide	1242:1256	arg1	mapping					1258:1264	Quantitative oligosaccharide mapping	1229:1264	Quantitative oligosaccharide mapping of four different lots of EPO from CHO cells	1229:1309	Quantitative oligosaccharide mapping of four different lots of EPO from CHO cells was performed to quantify the molar balance and distribution of the N-linked oligosaccharides.
1443598	1	78	theme	recombinant	273:283	arg1	EPO					301:303	EPO	301:303	EPO	301:303	A rapid quantitative analysis of the sialylated N-linked oligosaccharides of recombinant erythropoietin (EPO) expressed in Chinese hamster ovary (CHO) cells has been developed.
1443598	1	78	theme	recombinant	273:283	arg1	erythropoietin					285:298	recombinant erythropoietin	273:298	recombinant erythropoietin (EPO) expressed in Chinese hamster ovary (CHO) cells	273:351	A rapid quantitative analysis of the sialylated N-linked oligosaccharides of recombinant erythropoietin (EPO) expressed in Chinese hamster ovary (CHO) cells has been developed.
1443598	8	79	dep	balance	1347:1353	arg1	the					1337:1339	the	1337:1339	the	1337:1339	Quantitative oligosaccharide mapping of four different lots of EPO from CHO cells was performed to quantify the molar balance and distribution of the N-linked oligosaccharides.
1443598	0	80	theme	recombinant	63:73	arg1	erythropoietin					75:88	recombinant erythropoietin	63:88	recombinant erythropoietin	63:88	Quantitative mapping of the N-linked sialyloligosaccharides of recombinant erythropoietin: combination of direct high-performance anion-exchange chromatography and 2-aminopyridine derivatization.
1443598	0	81	theme	derivatization	180:193	arg1	combination					91:101	combination	91:101	Quantitative mapping of the N-linked sialyloligosaccharides of recombinant erythropoietin: combination of direct high-performance anion-exchange chromatography and 2-aminopyridine derivatization.	0:194	Quantitative mapping of the N-linked sialyloligosaccharides of recombinant erythropoietin: combination of direct high-performance anion-exchange chromatography and 2-aminopyridine derivatization.
1443598	8	82	theme	different	1274:1282	arg1	EPO					1292:1294	EPO	1292:1294	EPO	1292:1294	Quantitative oligosaccharide mapping of four different lots of EPO from CHO cells was performed to quantify the molar balance and distribution of the N-linked oligosaccharides.
1443598	8	82	theme	different	1274:1282	arg1	lots					1284:1287	four different lots	1269:1287	four different lots of EPO from CHO cells	1269:1309	Quantitative oligosaccharide mapping of four different lots of EPO from CHO cells was performed to quantify the molar balance and distribution of the N-linked oligosaccharides.
1443598	7	83	theme	galactose	1090:1098	arg1	residues					1100:1107	the terminal galactose residues	1077:1107	the terminal galactose residues of the oligosaccharides released from EPO	1077:1149	Approximately 3% of the terminal galactose residues of the oligosaccharides released from EPO were not sialylated whereas 97% contained an alpha(2-->3)-linked sialic acid.
1443598	7	83	theme	galactose	1090:1098	arg1	oligosaccharides					1116:1131	the oligosaccharides	1112:1131	the oligosaccharides released from EPO	1112:1149	Approximately 3% of the terminal galactose residues of the oligosaccharides released from EPO were not sialylated whereas 97% contained an alpha(2-->3)-linked sialic acid.
1443598	3	84	theme	two-dimensional	770:784	arg1	mapping					791:797	two-dimensional HPLC mapping	770:797	two-dimensional HPLC mapping of the pyridylaminated asialooligosaccharides	770:843	The eight sialyloligosaccharides isolated from HPAEC were characterized by derivatizing with 2-aminopyridine followed by two-dimensional HPLC mapping of the pyridylaminated asialooligosaccharides (Tomiya et al., 1988, Anal.
1443598	3	85	dep	derivatizing	724:735	arg1	followed					758:765	followed	758:765	followed by two-dimensional HPLC mapping of the pyridylaminated asialooligosaccharides (Tomiya et al., 1988, Anal	758:870	The eight sialyloligosaccharides isolated from HPAEC were characterized by derivatizing with 2-aminopyridine followed by two-dimensional HPLC mapping of the pyridylaminated asialooligosaccharides (Tomiya et al., 1988, Anal.
1443598	0	86	dep	mapping	13:19	arg1	combination					91:101	combination	91:101	Quantitative mapping of the N-linked sialyloligosaccharides of recombinant erythropoietin: combination of direct high-performance anion-exchange chromatography and 2-aminopyridine derivatization.	0:194	Quantitative mapping of the N-linked sialyloligosaccharides of recombinant erythropoietin: combination of direct high-performance anion-exchange chromatography and 2-aminopyridine derivatization.
1443598	3	87	theme	asialooligosaccharides	822:843	arg1	mapping					791:797	two-dimensional HPLC mapping	770:797	two-dimensional HPLC mapping of the pyridylaminated asialooligosaccharides	770:843	The eight sialyloligosaccharides isolated from HPAEC were characterized by derivatizing with 2-aminopyridine followed by two-dimensional HPLC mapping of the pyridylaminated asialooligosaccharides (Tomiya et al., 1988, Anal.
1443598	2	88	theme	glycopeptidase	412:425	arg1	glycoamidase					398:409	a glycoamidase	396:409	a glycoamidase (glycopeptidase F)	396:428	The procedure utilizes a glycoamidase (glycopeptidase F) to release all of the N-linked oligosaccharides from the native glycoprotein, followed by direct chromatographic analysis using high-performance anion-exchange chromatography (HPAEC) with pulsed amperometric detection.
1443598	2	88	theme	glycopeptidase	412:425	arg1	F					427:427	glycopeptidase F	412:427	glycopeptidase F	412:427	The procedure utilizes a glycoamidase (glycopeptidase F) to release all of the N-linked oligosaccharides from the native glycoprotein, followed by direct chromatographic analysis using high-performance anion-exchange chromatography (HPAEC) with pulsed amperometric detection.
1141232	0	0	theme	human	73:77	arg1	urine					79:83	normal human urine	66:83	normal human urine	66:83	A new type of carbohydrate-protein linkage in a glycopeptide from normal human urine.
1141232	0	1	from	type	6:9	arg1	a					46:46	a	46:46	a	46:46	A new type of carbohydrate-protein linkage in a glycopeptide from normal human urine.
1141232	5	2	theme	residue	661:667	arg1	degradation					631:641	degradation	631:641	degradation of the amino acid residue with ninhydrin	631:682	Linkages and sequential order were established by methylation analysis of the glycopeptide after degradation of the amino acid residue with ninhydrin.
1141232	0	3	from	a	46:46	arg1	type					6:9	A new type	0:9	A new type of carbohydrate-protein linkage in a	0:46	A new type of carbohydrate-protein linkage in a glycopeptide from normal human urine.
1141232	0	4	theme	normal	66:71	arg1	urine					79:83	normal human urine	66:83	normal human urine	66:83	A new type of carbohydrate-protein linkage in a glycopeptide from normal human urine.
1141232	1	5	theme	normal	186:191	arg1	urine					199:203	normal human urine	186:203	normal human urine	186:203	A glycopeptide, 3-O-beta-D-glucopyranosyl-alpha-L-fucopyranosyl-L-threonine, has been isolated from normal human urine.
1141232	5	6	theme	glycopeptide	612:623	arg1	analysis					596:603	methylation analysis	584:603	methylation analysis of the glycopeptide	584:623	Linkages and sequential order were established by methylation analysis of the glycopeptide after degradation of the amino acid residue with ninhydrin.
1141232	2	7	theme	high	319:322	arg1	electrophoresis					332:346	high voltage electrophoresis	319:346	high voltage electrophoresis	319:346	The glycopeptide was isolated by gel chromatography, preparative zone electrophoresis, paper chromatography, and high voltage electrophoresis.
1141232	1	8	attach	isolated	172:179	arg2	glycopeptide					88:99	A glycopeptide	86:99	A glycopeptide	86:99	A glycopeptide, 3-O-beta-D-glucopyranosyl-alpha-L-fucopyranosyl-L-threonine, has been isolated from normal human urine.
1141232	1	8	attach	isolated	172:179	arg1	urine					199:203	normal human urine	186:203	normal human urine	186:203	A glycopeptide, 3-O-beta-D-glucopyranosyl-alpha-L-fucopyranosyl-L-threonine, has been isolated from normal human urine.
1141232	1	8	attach	isolated	172:179	arg2	3-O-beta-D-glucopyranosyl-alpha-L-fucopyranosyl-L-threonine					102:160	3-O-beta-D-glucopyranosyl-alpha-L-fucopyranosyl-L-threonine	102:160	3-O-beta-D-glucopyranosyl-alpha-L-fucopyranosyl-L-threonine	102:160	A glycopeptide, 3-O-beta-D-glucopyranosyl-alpha-L-fucopyranosyl-L-threonine, has been isolated from normal human urine.
1141232	6	9	theme	liquid	731:736	arg1	chromatography					738:751	gas liquid chromatography	727:751	gas liquid chromatography	727:751	The permethylated product was analyzed on gas liquid chromatography and mass spectrometry.
1141232	1	10	gly	glycopeptide	88:99	arg2	glycopeptide					88:99	A glycopeptide	86:99	A glycopeptide	86:99	A glycopeptide, 3-O-beta-D-glucopyranosyl-alpha-L-fucopyranosyl-L-threonine, has been isolated from normal human urine.
1141232	1	10	gly	glycopeptide	88:99	arg2	3-O-beta-D-glucopyranosyl-alpha-L-fucopyranosyl-L-threonine					102:160	3-O-beta-D-glucopyranosyl-alpha-L-fucopyranosyl-L-threonine	102:160	3-O-beta-D-glucopyranosyl-alpha-L-fucopyranosyl-L-threonine	102:160	A glycopeptide, 3-O-beta-D-glucopyranosyl-alpha-L-fucopyranosyl-L-threonine, has been isolated from normal human urine.
1141232	4	11	theme	equimolar	481:489	arg1	fucose					511:516	fucose	511:516	fucose	511:516	Sugar analysis and amino acid analysis gave equimolar amounts of glucose, fucose, and threonine.
1141232	4	11	theme	equimolar	481:489	arg1	threonine					523:531	threonine	523:531	threonine	523:531	Sugar analysis and amino acid analysis gave equimolar amounts of glucose, fucose, and threonine.
1141232	4	11	theme	equimolar	481:489	arg1	glucose					502:508	glucose	502:508	glucose	502:508	Sugar analysis and amino acid analysis gave equimolar amounts of glucose, fucose, and threonine.
1141232	4	11	theme	equimolar	481:489	arg1	amounts					491:497	equimolar amounts	481:497	equimolar amounts of glucose, fucose, and threonine	481:531	Sugar analysis and amino acid analysis gave equimolar amounts of glucose, fucose, and threonine.
1141232	3	12	dep	0.3	414:416	arg1	to					411:412	to	411:412	to	411:412	The average yield of the glycopeptide was in the range of 0.2 to 0.3 mg/liter of urine.
1141232	6	13	theme	gas	727:729	arg1	chromatography					738:751	gas liquid chromatography	727:751	gas liquid chromatography	727:751	The permethylated product was analyzed on gas liquid chromatography and mass spectrometry.
1141232	1	14	theme	human	193:197	arg1	urine					199:203	normal human urine	186:203	normal human urine	186:203	A glycopeptide, 3-O-beta-D-glucopyranosyl-alpha-L-fucopyranosyl-L-threonine, has been isolated from normal human urine.
1141232	0	15	from	linkage	35:41	arg1	a					46:46	a	46:46	a	46:46	A new type of carbohydrate-protein linkage in a glycopeptide from normal human urine.
1141232	7	16	theme	Anomeric	776:783	arg1	configuration					785:797	Anomeric configuration	776:797	Anomeric configuration	776:797	Anomeric configuration was deduced from optical rotation.
1141232	3	17	theme	glycopeptide	374:385	arg1	yield					361:365	The average yield	349:365	The average yield of the glycopeptide	349:385	The average yield of the glycopeptide was in the range of 0.2 to 0.3 mg/liter of urine.
1141232	0	18	theme	new	2:4	arg1	type					6:9	A new type	0:9	A new type of carbohydrate-protein linkage in a	0:46	A new type of carbohydrate-protein linkage in a glycopeptide from normal human urine.
1141232	5	19	theme	amino	650:654	arg1	residue					661:667	the amino acid residue	646:667	the amino acid residue	646:667	Linkages and sequential order were established by methylation analysis of the glycopeptide after degradation of the amino acid residue with ninhydrin.
1141232	5	20	theme	methylation	584:594	arg1	analysis					596:603	methylation analysis	584:603	methylation analysis of the glycopeptide	584:623	Linkages and sequential order were established by methylation analysis of the glycopeptide after degradation of the amino acid residue with ninhydrin.
1141232	5	21	theme	acid	656:659	arg1	residue					661:667	the amino acid residue	646:667	the amino acid residue	646:667	Linkages and sequential order were established by methylation analysis of the glycopeptide after degradation of the amino acid residue with ninhydrin.
1141232	4	22	theme	acid	462:465	arg1	analysis					467:474	amino acid analysis	456:474	amino acid analysis	456:474	Sugar analysis and amino acid analysis gave equimolar amounts of glucose, fucose, and threonine.
1141232	2	23	theme	voltage	324:330	arg1	electrophoresis					332:346	high voltage electrophoresis	319:346	high voltage electrophoresis	319:346	The glycopeptide was isolated by gel chromatography, preparative zone electrophoresis, paper chromatography, and high voltage electrophoresis.
1141232	6	24	theme	permethylated	689:701	arg1	product					703:709	The permethylated product	685:709	The permethylated product	685:709	The permethylated product was analyzed on gas liquid chromatography and mass spectrometry.
1141232	0	25	theme	linkage	35:41	arg1	type					6:9	A new type	0:9	A new type of carbohydrate-protein linkage in a	0:46	A new type of carbohydrate-protein linkage in a glycopeptide from normal human urine.
1141232	4	26	theme	amino	456:460	arg1	analysis					467:474	amino acid analysis	456:474	amino acid analysis	456:474	Sugar analysis and amino acid analysis gave equimolar amounts of glucose, fucose, and threonine.
1141232	2	27	theme	preparative	259:269	arg1	electrophoresis					276:290	preparative zone electrophoresis	259:290	preparative zone electrophoresis	259:290	The glycopeptide was isolated by gel chromatography, preparative zone electrophoresis, paper chromatography, and high voltage electrophoresis.
1141232	0	28	theme	carbohydrate-protein	14:33	arg1	linkage					35:41	carbohydrate-protein linkage	14:41	carbohydrate-protein linkage in a	14:46	A new type of carbohydrate-protein linkage in a glycopeptide from normal human urine.
1141232	7	29	theme	optical	816:822	arg1	rotation					824:831	optical rotation	816:831	optical rotation	816:831	Anomeric configuration was deduced from optical rotation.
1141232	3	30	gly	glycopeptide	374:385	arg2	glycopeptide					374:385	the glycopeptide	370:385	the glycopeptide	370:385	The average yield of the glycopeptide was in the range of 0.2 to 0.3 mg/liter of urine.
1141232	5	31	theme	sequential	547:556	arg1	order					558:562	sequential order	547:562	sequential order	547:562	Linkages and sequential order were established by methylation analysis of the glycopeptide after degradation of the amino acid residue with ninhydrin.
1141232	4	32	theme	threonine	523:531	arg1	fucose					511:516	fucose	511:516	fucose	511:516	Sugar analysis and amino acid analysis gave equimolar amounts of glucose, fucose, and threonine.
1141232	4	32	theme	threonine	523:531	arg1	threonine					523:531	threonine	523:531	threonine	523:531	Sugar analysis and amino acid analysis gave equimolar amounts of glucose, fucose, and threonine.
1141232	4	32	theme	threonine	523:531	arg1	glucose					502:508	glucose	502:508	glucose	502:508	Sugar analysis and amino acid analysis gave equimolar amounts of glucose, fucose, and threonine.
1141232	4	32	theme	threonine	523:531	arg1	amounts					491:497	equimolar amounts	481:497	equimolar amounts of glucose, fucose, and threonine	481:531	Sugar analysis and amino acid analysis gave equimolar amounts of glucose, fucose, and threonine.
1141232	4	33	theme	glucose	502:508	arg1	fucose					511:516	fucose	511:516	fucose	511:516	Sugar analysis and amino acid analysis gave equimolar amounts of glucose, fucose, and threonine.
1141232	4	33	theme	glucose	502:508	arg1	threonine					523:531	threonine	523:531	threonine	523:531	Sugar analysis and amino acid analysis gave equimolar amounts of glucose, fucose, and threonine.
1141232	4	33	theme	glucose	502:508	arg1	glucose					502:508	glucose	502:508	glucose	502:508	Sugar analysis and amino acid analysis gave equimolar amounts of glucose, fucose, and threonine.
1141232	4	33	theme	glucose	502:508	arg1	amounts					491:497	equimolar amounts	481:497	equimolar amounts of glucose, fucose, and threonine	481:531	Sugar analysis and amino acid analysis gave equimolar amounts of glucose, fucose, and threonine.
1141232	3	34	theme	average	353:359	arg1	yield					361:365	The average yield	349:365	The average yield of the glycopeptide	349:385	The average yield of the glycopeptide was in the range of 0.2 to 0.3 mg/liter of urine.
1141232	3	35	theme	mg/liter	418:425	arg1	range					398:402	the range	394:402	the range of 0.2 to 0.3 mg/liter of urine	394:434	The average yield of the glycopeptide was in the range of 0.2 to 0.3 mg/liter of urine.
1141232	4	36	theme	fucose	511:516	arg1	fucose					511:516	fucose	511:516	fucose	511:516	Sugar analysis and amino acid analysis gave equimolar amounts of glucose, fucose, and threonine.
1141232	4	36	theme	fucose	511:516	arg1	threonine					523:531	threonine	523:531	threonine	523:531	Sugar analysis and amino acid analysis gave equimolar amounts of glucose, fucose, and threonine.
1141232	4	36	theme	fucose	511:516	arg1	glucose					502:508	glucose	502:508	glucose	502:508	Sugar analysis and amino acid analysis gave equimolar amounts of glucose, fucose, and threonine.
1141232	4	36	theme	fucose	511:516	arg1	amounts					491:497	equimolar amounts	481:497	equimolar amounts of glucose, fucose, and threonine	481:531	Sugar analysis and amino acid analysis gave equimolar amounts of glucose, fucose, and threonine.
1141232	4	37	theme	Sugar	437:441	arg1	analysis					443:450	Sugar analysis	437:450	Sugar analysis	437:450	Sugar analysis and amino acid analysis gave equimolar amounts of glucose, fucose, and threonine.
1141232	2	38	theme	gel	239:241	arg1	chromatography					243:256	gel chromatography	239:256	gel chromatography	239:256	The glycopeptide was isolated by gel chromatography, preparative zone electrophoresis, paper chromatography, and high voltage electrophoresis.
1141232	2	39	theme	paper	293:297	arg1	chromatography					299:312	paper chromatography	293:312	paper chromatography	293:312	The glycopeptide was isolated by gel chromatography, preparative zone electrophoresis, paper chromatography, and high voltage electrophoresis.
1141232	5	40	gly	glycopeptide	612:623	arg2	glycopeptide					612:623	the glycopeptide	608:623	the glycopeptide	608:623	Linkages and sequential order were established by methylation analysis of the glycopeptide after degradation of the amino acid residue with ninhydrin.
1141232	0	41	gly	glycopeptide	48:59	arg2	glycopeptide					48:59	glycopeptide	48:59	glycopeptide from normal human urine	48:83	A new type of carbohydrate-protein linkage in a glycopeptide from normal human urine.
1141232	0	41	gly	glycopeptide	48:59	arg1	urine					79:83	normal human urine	66:83	normal human urine	66:83	A new type of carbohydrate-protein linkage in a glycopeptide from normal human urine.
1141232	2	42	gly	glycopeptide	210:221	arg2	glycopeptide					210:221	The glycopeptide	206:221	The glycopeptide	206:221	The glycopeptide was isolated by gel chromatography, preparative zone electrophoresis, paper chromatography, and high voltage electrophoresis.
1141232	6	43	theme	mass	757:760	arg1	spectrometry					762:773	mass spectrometry	757:773	mass spectrometry	757:773	The permethylated product was analyzed on gas liquid chromatography and mass spectrometry.
1141232	3	44	theme	urine	430:434	arg1	mg/liter					418:425	0.2 to 0.3 mg/liter	407:425	0.2 to 0.3 mg/liter of urine	407:434	The average yield of the glycopeptide was in the range of 0.2 to 0.3 mg/liter of urine.
1141232	2	45	theme	zone	271:274	arg1	electrophoresis					276:290	preparative zone electrophoresis	259:290	preparative zone electrophoresis	259:290	The glycopeptide was isolated by gel chromatography, preparative zone electrophoresis, paper chromatography, and high voltage electrophoresis.
1141232	5	46	with	degradation	631:641	arg1	ninhydrin					674:682	ninhydrin	674:682	ninhydrin	674:682	Linkages and sequential order were established by methylation analysis of the glycopeptide after degradation of the amino acid residue with ninhydrin.
6746638	7	0	theme	novel	1605:1609	arg1	element					1622:1628	a novel structural element	1603:1628	a novel structural element for mucins	1603:1639	This sequence constitutes a novel structural element for mucins.
6746638	6	1	from	Gal	1423:1425	arg1	-linkage					1454:1461	alpha(1----3)-linkage	1441:1461	alpha(1----3)-linkage	1441:1461	The simultaneous presence of sialic acid in alpha(2----3)-linkage to Gal and fucose in alpha(1----3)-linkage to GlcNAc of the same N-acetyllactosamine unit could be adequately proved by high resolution 1H NMR spectroscopy.
6746638	5	2	dep	GalNAc-o1	1214:1222	arg1	A-2					910:912	A-2	910:912	A-2	910:912	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	5	3	dep	A-1	819:821	arg1	GalNAc-o1					1214:1222	NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1	824:1222	NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1	824:1222	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	5	3	dep	A-1	819:821	arg1	beta					1330:1333	NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)	1229:1341	NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)	1229:1341	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	5	3	dep	A-1	819:821	arg1	A-6					1225:1227	A-6	1225:1227	A-6	1225:1227	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	5	4	dep	GalNAc-o1	1343:1351	arg1	A-1					819:821	A-1	819:821	A-1	819:821	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	6	5	theme	2----3	1404:1409	arg1	-linkage					1411:1418	alpha(2----3)-linkage	1398:1418	alpha(2----3)-linkage to Gal and fucose in alpha(1----3)-linkage to GlcNAc of the same N-acetyllactosamine unit	1398:1508	The simultaneous presence of sialic acid in alpha(2----3)-linkage to Gal and fucose in alpha(1----3)-linkage to GlcNAc of the same N-acetyllactosamine unit could be adequately proved by high resolution 1H NMR spectroscopy.
6746638	5	6	theme	2----3	1242:1247	arg1	beta					1254:1257	NeuAc alpha-(2----3) Gal beta(1----4)	1229:1265	NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)	1229:1341	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	5	7	theme	Glc-NAc	1169:1175	arg1	beta					1181:1184	NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)	915:1192	NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)	915:1212	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	5	8	theme	alpha	1049:1053	arg1	GalNAc-o1					1099:1107	NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1	1008:1107	NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1	1008:1107	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	4	9	theme	performance	675:685	arg1	chromatography					694:707	high performance liquid chromatography	670:707	high performance liquid chromatography	670:707	After subjecting the mucins to alkaline borohydride degradation, sialylated oligosaccharide-alditols were isolated by anion-exchange chromatography and fractionated by high performance liquid chromatography.
6746638	5	10	theme	Gal	1250:1252	arg1	beta					1254:1257	NeuAc alpha-(2----3) Gal beta(1----4)	1229:1265	NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)	1229:1341	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	5	11	theme	[Fuc	1150:1153	arg1	alpha					1155:1159	NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)	1115:1167	NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)	1115:1167	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	6	12	theme	alpha	1398:1402	arg1	-linkage					1411:1418	alpha(2----3)-linkage	1398:1418	alpha(2----3)-linkage to Gal and fucose in alpha(1----3)-linkage to GlcNAc of the same N-acetyllactosamine unit	1398:1508	The simultaneous presence of sialic acid in alpha(2----3)-linkage to Gal and fucose in alpha(1----3)-linkage to GlcNAc of the same N-acetyllactosamine unit could be adequately proved by high resolution 1H NMR spectroscopy.
6746638	3	13	from	spectroscopy	453:464	arg1	conjunction					469:479	conjunction	469:479	conjunction with sugar analysis	469:499	The structure of sialylated carbohydrate units of bronchial mucins obtained from cystic fibrosis patients was investigated by 500-MHz 1H NMR spectroscopy in conjunction with sugar analysis.
6746638	6	14	theme	1----3	1447:1452	arg1	-linkage					1454:1461	alpha(1----3)-linkage	1441:1461	alpha(1----3)-linkage	1441:1461	The simultaneous presence of sialic acid in alpha(2----3)-linkage to Gal and fucose in alpha(1----3)-linkage to GlcNAc of the same N-acetyllactosamine unit could be adequately proved by high resolution 1H NMR spectroscopy.
6746638	5	15	theme	beta	1292:1295	arg1	beta					1330:1333	NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)	1229:1341	NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)	1229:1341	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	0	16	theme	cystic	138:143	arg1	fibrosis					145:152	cystic fibrosis	138:152	cystic fibrosis	138:152	Primary structure determination of five sialylated oligosaccharides derived from bronchial mucus glycoproteins of patients suffering from cystic fibrosis.
6746638	1	17	theme	beta	200:203	arg1	1----					244:248	1----.	244:249	1----.	244:249	The occurrence of the NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)] GlcNAc beta(1----.)
6746638	1	17	theme	beta	200:203	arg1	beta					239:242	the NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)] GlcNAc beta	173:242	the NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)] GlcNAc beta(1----.)	173:250	The occurrence of the NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)] GlcNAc beta(1----.)
6746638	6	18	theme	alpha	1441:1445	arg1	-linkage					1454:1461	alpha(1----3)-linkage	1441:1461	alpha(1----3)-linkage	1441:1461	The simultaneous presence of sialic acid in alpha(2----3)-linkage to Gal and fucose in alpha(1----3)-linkage to GlcNAc of the same N-acetyllactosamine unit could be adequately proved by high resolution 1H NMR spectroscopy.
6746638	5	19	theme	alpha	1271:1275	arg1	beta					1330:1333	NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)	1229:1341	NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)	1229:1341	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	5	20	theme	-[GlcNAc	969:976	arg1	beta					1181:1184	NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)	915:1192	NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)	915:1212	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	5	21	theme	Gal	843:845	arg1	beta					847:850	NeuAc alpha(2----3)Gal beta(1----4)	824:858	NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1	824:1222	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	5	22	dep	beta	1181:1184	arg1	A-3					1003:1005	A-3	1003:1005	A-3	1003:1005	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	5	23	dep	state	760:764	arg1	be					731:732	be	731:732	could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1	725:1351	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	5	23	dep	state	760:764	arg1	established					789:799	established	789:799	were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1	784:1351	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	5	24	theme	1----3	1277:1282	arg1	beta					1330:1333	NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)	1229:1341	NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)	1229:1341	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	6	25	from	fucose	1431:1436	arg1	-linkage					1454:1461	alpha(1----3)-linkage	1441:1461	alpha(1----3)-linkage	1441:1461	The simultaneous presence of sialic acid in alpha(2----3)-linkage to Gal and fucose in alpha(1----3)-linkage to GlcNAc of the same N-acetyllactosamine unit could be adequately proved by high resolution 1H NMR spectroscopy.
6746638	5	26	theme	Gal	1082:1084	arg1	GalNAc-o1					1099:1107	NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1	1008:1107	NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1	1008:1107	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	5	27	theme	beta	957:960	arg1	beta					1181:1184	NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)	915:1192	NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)	915:1212	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	5	28	theme	beta	886:889	arg1	GalNAc-o1					1214:1222	NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1	824:1222	NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1	824:1222	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	6	29	theme	N-acetyllactosamine	1485:1503	arg1	unit					1505:1508	the same N-acetyllactosamine unit	1476:1508	the same N-acetyllactosamine unit	1476:1508	The simultaneous presence of sialic acid in alpha(2----3)-linkage to Gal and fucose in alpha(1----3)-linkage to GlcNAc of the same N-acetyllactosamine unit could be adequately proved by high resolution 1H NMR spectroscopy.
6746638	5	30	theme	GalNAc-o1	992:1000	arg1	beta					1181:1184	NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)	915:1192	NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)	915:1212	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	5	31	theme	alpha	865:869	arg1	GalNAc-o1					1214:1222	NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1	824:1222	NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1	824:1222	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	6	32	theme	acid	1390:1393	arg1	presence					1371:1378	The simultaneous presence	1354:1378	The simultaneous presence of sialic acid in alpha(2----3)-linkage to Gal and fucose in alpha(1----3)-linkage to GlcNAc of the same N-acetyllactosamine unit	1354:1508	The simultaneous presence of sialic acid in alpha(2----3)-linkage to Gal and fucose in alpha(1----3)-linkage to GlcNAc of the same N-acetyllactosamine unit could be adequately proved by high resolution 1H NMR spectroscopy.
6746638	5	33	theme	[GlcNAc	1193:1199	arg1	beta					1201:1204	NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)	915:1212	NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)	915:1212	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	5	34	theme	beta	1070:1073	arg1	GalNAc-o1					1099:1107	NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1	1008:1107	NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1	1008:1107	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	0	35	theme	mucus	91:95	arg1	glycoproteins					97:109	bronchial mucus glycoproteins	81:109	bronchial mucus glycoproteins of patients suffering from cystic fibrosis	81:152	Primary structure determination of five sialylated oligosaccharides derived from bronchial mucus glycoproteins of patients suffering from cystic fibrosis.
6746638	1	36	theme	NeuAc	177:181	arg1	1----					244:248	1----.	244:249	1----.	244:249	The occurrence of the NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)] GlcNAc beta(1----.)
6746638	1	36	theme	NeuAc	177:181	arg1	beta					239:242	the NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)] GlcNAc beta	173:242	the NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)] GlcNAc beta(1----.)	173:250	The occurrence of the NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)] GlcNAc beta(1----.)
6746638	5	37	theme	1----3	1075:1080	arg1	GalNAc-o1					1099:1107	NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1	1008:1107	NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1	1008:1107	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	5	38	theme	pure	755:758	arg1	state					760:764	a rather pure state	746:764	a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1	746:1351	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	6	39	theme	unit	1505:1508	arg1	GlcNAc					1466:1471	GlcNAc	1466:1471	GlcNAc of the same N-acetyllactosamine unit	1466:1508	The simultaneous presence of sialic acid in alpha(2----3)-linkage to Gal and fucose in alpha(1----3)-linkage to GlcNAc of the same N-acetyllactosamine unit could be adequately proved by high resolution 1H NMR spectroscopy.
6746638	5	40	theme	beta	1181:1184	arg1	beta					1201:1204	NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)	915:1212	NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)	915:1212	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	6	41	theme	NMR	1559:1561	arg1	spectroscopy					1563:1574	high resolution 1H NMR spectroscopy	1540:1574	high resolution 1H NMR spectroscopy	1540:1574	The simultaneous presence of sialic acid in alpha(2----3)-linkage to Gal and fucose in alpha(1----3)-linkage to GlcNAc of the same N-acetyllactosamine unit could be adequately proved by high resolution 1H NMR spectroscopy.
6746638	3	42	theme	fibrosis	400:407	arg1	patients					409:416	cystic fibrosis patients	393:416	cystic fibrosis patients	393:416	The structure of sialylated carbohydrate units of bronchial mucins obtained from cystic fibrosis patients was investigated by 500-MHz 1H NMR spectroscopy in conjunction with sugar analysis.
6746638	1	43	theme	GlcNAc	232:237	arg1	1----					244:248	1----.	244:249	1----.	244:249	The occurrence of the NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)] GlcNAc beta(1----.)
6746638	1	43	theme	GlcNAc	232:237	arg1	beta					239:242	the NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)] GlcNAc beta	173:242	the NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)] GlcNAc beta(1----.)	173:250	The occurrence of the NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)] GlcNAc beta(1----.)
6746638	0	44	gly	glycoproteins	97:109	arg1	glycoproteins					97:109	bronchial mucus glycoproteins	81:109	bronchial mucus glycoproteins of patients suffering from cystic fibrosis	81:152	Primary structure determination of five sialylated oligosaccharides derived from bronchial mucus glycoproteins of patients suffering from cystic fibrosis.
6746638	3	45	theme	carbohydrate	340:351	arg1	units					353:357	sialylated carbohydrate units	329:357	sialylated carbohydrate units of bronchial mucins obtained from cystic fibrosis patients	329:416	The structure of sialylated carbohydrate units of bronchial mucins obtained from cystic fibrosis patients was investigated by 500-MHz 1H NMR spectroscopy in conjunction with sugar analysis.
6746638	6	46	theme	sialic	1383:1388	arg1	acid					1390:1393	sialic acid	1383:1393	sialic acid	1383:1393	The simultaneous presence of sialic acid in alpha(2----3)-linkage to Gal and fucose in alpha(1----3)-linkage to GlcNAc of the same N-acetyllactosamine unit could be adequately proved by high resolution 1H NMR spectroscopy.
6746638	6	47	theme	resolution	1545:1554	arg1	spectroscopy					1563:1574	high resolution 1H NMR spectroscopy	1540:1574	high resolution 1H NMR spectroscopy	1540:1574	The simultaneous presence of sialic acid in alpha(2----3)-linkage to Gal and fucose in alpha(1----3)-linkage to GlcNAc of the same N-acetyllactosamine unit could be adequately proved by high resolution 1H NMR spectroscopy.
6746638	5	48	theme	alpha	1121:1125	arg1	alpha					1155:1159	NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)	1115:1167	NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)	1115:1167	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	0	49	theme	Primary	0:6	arg1	determination					18:30	Primary structure determination	0:30	Primary structure determination of five sialylated oligosaccharides	0:66	Primary structure determination of five sialylated oligosaccharides derived from bronchial mucus glycoproteins of patients suffering from cystic fibrosis.
6746638	1	50	theme	beta	239:242	arg1	occurrence					159:168	The occurrence	155:168	The occurrence of the NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)] GlcNAc beta(1----.)	155:250	The occurrence of the NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)] GlcNAc beta(1----.)
6746638	4	51	gly	sialylated	567:576	arg1	oligosaccharide-alditols					578:601	sialylated oligosaccharide-alditols	567:601	sialylated oligosaccharide-alditols	567:601	After subjecting the mucins to alkaline borohydride degradation, sialylated oligosaccharide-alditols were isolated by anion-exchange chromatography and fractionated by high performance liquid chromatography.
6746638	5	52	theme	1----3	891:896	arg1	GalNAc-o1					1214:1222	NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1	824:1222	NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1	824:1222	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	6	53	attach	presence	1371:1378	arg2	acid					1390:1393	sialic acid	1383:1393	sialic acid	1383:1393	The simultaneous presence of sialic acid in alpha(2----3)-linkage to Gal and fucose in alpha(1----3)-linkage to GlcNAc of the same N-acetyllactosamine unit could be adequately proved by high resolution 1H NMR spectroscopy.
6746638	6	53	attach	presence	1371:1378	arg1	-linkage					1411:1418	alpha(2----3)-linkage	1398:1418	alpha(2----3)-linkage to Gal and fucose in alpha(1----3)-linkage to GlcNAc of the same N-acetyllactosamine unit	1398:1508	The simultaneous presence of sialic acid in alpha(2----3)-linkage to Gal and fucose in alpha(1----3)-linkage to GlcNAc of the same N-acetyllactosamine unit could be adequately proved by high resolution 1H NMR spectroscopy.
6746638	5	54	theme	alpha	830:834	arg1	beta					847:850	NeuAc alpha(2----3)Gal beta(1----4)	824:858	NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1	824:1222	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	5	55	theme	beta-	1031:1035	arg1	GalNAc-o1					1099:1107	NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1	1008:1107	NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1	1008:1107	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	5	56	theme	Gal-NAc-ol	898:907	arg1	GalNAc-o1					1214:1222	NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1	824:1222	NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1	824:1222	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	3	57	theme	mucins	372:377	arg1	units					353:357	sialylated carbohydrate units	329:357	sialylated carbohydrate units of bronchial mucins obtained from cystic fibrosis patients	329:416	The structure of sialylated carbohydrate units of bronchial mucins obtained from cystic fibrosis patients was investigated by 500-MHz 1H NMR spectroscopy in conjunction with sugar analysis.
6746638	4	58	theme	alkaline	533:540	arg1	degradation					554:564	alkaline borohydride degradation	533:564	alkaline borohydride degradation	533:564	After subjecting the mucins to alkaline borohydride degradation, sialylated oligosaccharide-alditols were isolated by anion-exchange chromatography and fractionated by high performance liquid chromatography.
6746638	5	59	theme	NeuAc	1229:1233	arg1	beta					1254:1257	NeuAc alpha-(2----3) Gal beta(1----4)	1229:1265	NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)	1229:1341	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	5	60	theme	beta	847:850	arg1	GalNAc-o1					1214:1222	NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1	824:1222	NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1	824:1222	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	5	61	theme	NeuAc	1008:1012	arg1	GalNAc-o1					1099:1107	NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1	1008:1107	NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1	1008:1107	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	5	62	theme	beta	938:941	arg1	beta					957:960	NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)	915:968	NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)	915:1212	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	2	63	theme	NMR	294:296	arg1	spectroscopy					298:309	500-MHz 1H NMR spectroscopy	283:309	500-MHz 1H NMR spectroscopy	283:309	structural element revealed by 500-MHz 1H NMR spectroscopy.
6746638	0	64	theme	oligosaccharides	51:66	arg1	determination					18:30	Primary structure determination	0:30	Primary structure determination of five sialylated oligosaccharides	0:66	Primary structure determination of five sialylated oligosaccharides derived from bronchial mucus glycoproteins of patients suffering from cystic fibrosis.
6746638	3	65	theme	1H	446:447	arg1	spectroscopy					453:464	500-MHz 1H NMR spectroscopy	438:464	500-MHz 1H NMR spectroscopy in conjunction with sugar analysis	438:499	The structure of sialylated carbohydrate units of bronchial mucins obtained from cystic fibrosis patients was investigated by 500-MHz 1H NMR spectroscopy in conjunction with sugar analysis.
6746638	0	66	gly	sialylated	40:49	arg1	oligosaccharides					51:66	five sialylated oligosaccharides	35:66	five sialylated oligosaccharides	35:66	Primary structure determination of five sialylated oligosaccharides derived from bronchial mucus glycoproteins of patients suffering from cystic fibrosis.
6746638	5	67	theme	beta	1254:1257	arg1	beta					1330:1333	NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)	1229:1341	NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)	1229:1341	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	5	68	theme	2----3	1127:1132	arg1	alpha					1155:1159	NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)	1115:1167	NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)	1115:1167	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	3	69	theme	sugar	486:490	arg1	analysis					492:499	sugar analysis	486:499	sugar analysis	486:499	The structure of sialylated carbohydrate units of bronchial mucins obtained from cystic fibrosis patients was investigated by 500-MHz 1H NMR spectroscopy in conjunction with sugar analysis.
6746638	1	70	theme	alpha	217:221	arg1	1----					244:248	1----.	244:249	1----.	244:249	The occurrence of the NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)] GlcNAc beta(1----.)
6746638	1	70	theme	alpha	217:221	arg1	beta					239:242	the NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)] GlcNAc beta	173:242	the NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)] GlcNAc beta(1----.)	173:250	The occurrence of the NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)] GlcNAc beta(1----.)
6746638	3	71	with	conjunction	469:479	arg1	analysis					492:499	sugar analysis	486:499	sugar analysis	486:499	The structure of sialylated carbohydrate units of bronchial mucins obtained from cystic fibrosis patients was investigated by 500-MHz 1H NMR spectroscopy in conjunction with sugar analysis.
6746638	5	72	theme	Gal	1134:1136	arg1	alpha					1155:1159	NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)	1115:1167	NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)	1115:1167	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	1	73	theme	1----3	223:228	arg1	1----					244:248	1----.	244:249	1----.	244:249	The occurrence of the NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)] GlcNAc beta(1----.)
6746638	1	73	theme	1----3	223:228	arg1	beta					239:242	the NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)] GlcNAc beta	173:242	the NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)] GlcNAc beta(1----.)	173:250	The occurrence of the NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)] GlcNAc beta(1----.)
6746638	7	74	theme	structural	1611:1620	arg1	element					1622:1628	a novel structural element	1603:1628	a novel structural element for mucins	1603:1639	This sequence constitutes a novel structural element for mucins.
6746638	5	75	theme	[Fuc	1044:1047	arg1	GalNAc-o1					1099:1107	NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1	1008:1107	NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1	1008:1107	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	4	76	theme	sialylated	567:576	arg1	oligosaccharide-alditols					578:601	sialylated oligosaccharide-alditols	567:601	sialylated oligosaccharide-alditols	567:601	After subjecting the mucins to alkaline borohydride degradation, sialylated oligosaccharide-alditols were isolated by anion-exchange chromatography and fractionated by high performance liquid chromatography.
6746638	5	77	theme	NAc	1177:1179	arg1	beta					1181:1184	NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)	915:1192	NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)	915:1212	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	1	78	theme	alpha	183:187	arg1	1----					244:248	1----.	244:249	1----.	244:249	The occurrence of the NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)] GlcNAc beta(1----.)
6746638	1	78	theme	alpha	183:187	arg1	beta					239:242	the NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)] GlcNAc beta	173:242	the NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)] GlcNAc beta(1----.)	173:250	The occurrence of the NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)] GlcNAc beta(1----.)
6746638	4	79	theme	high	670:673	arg1	chromatography					694:707	high performance liquid chromatography	670:707	high performance liquid chromatography	670:707	After subjecting the mucins to alkaline borohydride degradation, sialylated oligosaccharide-alditols were isolated by anion-exchange chromatography and fractionated by high performance liquid chromatography.
6746638	1	80	theme	2----3	189:194	arg1	1----					244:248	1----.	244:249	1----.	244:249	The occurrence of the NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)] GlcNAc beta(1----.)
6746638	1	80	theme	2----3	189:194	arg1	beta					239:242	the NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)] GlcNAc beta	173:242	the NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)] GlcNAc beta(1----.)	173:250	The occurrence of the NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)] GlcNAc beta(1----.)
6746638	4	81	theme	liquid	687:692	arg1	chromatography					694:707	high performance liquid chromatography	670:707	high performance liquid chromatography	670:707	After subjecting the mucins to alkaline borohydride degradation, sialylated oligosaccharide-alditols were isolated by anion-exchange chromatography and fractionated by high performance liquid chromatography.
6746638	5	82	theme	GlcNAc	1285:1290	arg1	beta					1330:1333	NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)	1229:1341	NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)	1229:1341	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	2	83	theme	structural	252:261	arg1	element					263:269	structural element	252:269	structural element	252:269	structural element revealed by 500-MHz 1H NMR spectroscopy.
6746638	1	84	theme	Gal	196:198	arg1	1----					244:248	1----.	244:249	1----.	244:249	The occurrence of the NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)] GlcNAc beta(1----.)
6746638	1	84	theme	Gal	196:198	arg1	beta					239:242	the NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)] GlcNAc beta	173:242	the NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)] GlcNAc beta(1----.)	173:250	The occurrence of the NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)] GlcNAc beta(1----.)
6746638	5	85	theme	1----3	871:876	arg1	GalNAc-o1					1214:1222	NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1	824:1222	NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1	824:1222	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	5	86	theme	[Fuc	1266:1269	arg1	beta					1330:1333	NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)	1229:1341	NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)	1229:1341	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	5	87	theme	beta	978:981	arg1	beta					1181:1184	NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)	915:1192	NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)	915:1212	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	5	88	theme	GlcNAc	950:955	arg1	beta					957:960	NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)	915:968	NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)	915:1212	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	5	89	theme	GlcNAc	879:884	arg1	GalNAc-o1					1214:1222	NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1	824:1222	NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1	824:1222	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	6	90	from	presence	1371:1378	arg1	-linkage					1411:1418	alpha(2----3)-linkage	1398:1418	alpha(2----3)-linkage to Gal and fucose in alpha(1----3)-linkage to GlcNAc of the same N-acetyllactosamine unit	1398:1508	The simultaneous presence of sialic acid in alpha(2----3)-linkage to Gal and fucose in alpha(1----3)-linkage to GlcNAc of the same N-acetyllactosamine unit could be adequately proved by high resolution 1H NMR spectroscopy.
6746638	5	91	dep	A-2	910:912	arg1	beta					1201:1204	NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)	915:1212	NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)	915:1212	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	5	92	theme	beta	1086:1089	arg1	GalNAc-o1					1099:1107	NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1	1008:1107	NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1	1008:1107	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	2	93	theme	500-MHz	283:289	arg1	spectroscopy					298:309	500-MHz 1H NMR spectroscopy	283:309	500-MHz 1H NMR spectroscopy	283:309	structural element revealed by 500-MHz 1H NMR spectroscopy.
6746638	0	94	theme	bronchial	81:89	arg1	glycoproteins					97:109	bronchial mucus glycoproteins	81:109	bronchial mucus glycoproteins of patients suffering from cystic fibrosis	81:152	Primary structure determination of five sialylated oligosaccharides derived from bronchial mucus glycoproteins of patients suffering from cystic fibrosis.
6746638	6	95	theme	1H	1556:1557	arg1	spectroscopy					1563:1574	high resolution 1H NMR spectroscopy	1540:1574	high resolution 1H NMR spectroscopy	1540:1574	The simultaneous presence of sialic acid in alpha(2----3)-linkage to Gal and fucose in alpha(1----3)-linkage to GlcNAc of the same N-acetyllactosamine unit could be adequately proved by high resolution 1H NMR spectroscopy.
6746638	5	96	theme	[Fuc	860:863	arg1	GalNAc-o1					1214:1222	NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1	824:1222	NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1	824:1222	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	6	97	theme	same	1480:1483	arg1	unit					1505:1508	the same N-acetyllactosamine unit	1476:1508	the same N-acetyllactosamine unit	1476:1508	The simultaneous presence of sialic acid in alpha(2----3)-linkage to Gal and fucose in alpha(1----3)-linkage to GlcNAc of the same N-acetyllactosamine unit could be adequately proved by high resolution 1H NMR spectroscopy.
6746638	5	98	theme	GlcNAc	1063:1068	arg1	GalNAc-o1					1099:1107	NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1	1008:1107	NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1	1008:1107	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	5	99	theme	GlcNAc	1323:1328	arg1	beta					1330:1333	NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)	1229:1341	NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)	1229:1341	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	0	100	theme	patients	114:121	arg1	glycoproteins					97:109	bronchial mucus glycoproteins	81:109	bronchial mucus glycoproteins of patients suffering from cystic fibrosis	81:152	Primary structure determination of five sialylated oligosaccharides derived from bronchial mucus glycoproteins of patients suffering from cystic fibrosis.
6746638	5	101	theme	1----3	984:989	arg1	beta					1181:1184	NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)	915:1192	NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)	915:1212	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	5	102	theme	2----3	836:841	arg1	beta					847:850	NeuAc alpha(2----3)Gal beta(1----4)	824:858	NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1	824:1222	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	1	103	theme	[Fuc	212:215	arg1	1----					244:248	1----.	244:249	1----.	244:249	The occurrence of the NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)] GlcNAc beta(1----.)
6746638	1	103	theme	[Fuc	212:215	arg1	beta					239:242	the NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)] GlcNAc beta	173:242	the NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)] GlcNAc beta(1----.)	173:250	The occurrence of the NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)] GlcNAc beta(1----.)
6746638	5	104	theme	NeuAc	1115:1119	arg1	alpha					1155:1159	NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)	1115:1167	NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)	1115:1167	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	0	105	theme	structure	8:16	arg1	determination					18:30	Primary structure determination	0:30	Primary structure determination of five sialylated oligosaccharides	0:66	Primary structure determination of five sialylated oligosaccharides derived from bronchial mucus glycoproteins of patients suffering from cystic fibrosis.
6746638	3	106	gly	sialylated	329:338	arg1	units					353:357	sialylated carbohydrate units	329:357	sialylated carbohydrate units of bronchial mucins obtained from cystic fibrosis patients	329:416	The structure of sialylated carbohydrate units of bronchial mucins obtained from cystic fibrosis patients was investigated by 500-MHz 1H NMR spectroscopy in conjunction with sugar analysis.
6746638	3	107	theme	units	353:357	arg1	structure					316:324	The structure	312:324	The structure of sialylated carbohydrate units of bronchial mucins obtained from cystic fibrosis patients	312:416	The structure of sialylated carbohydrate units of bronchial mucins obtained from cystic fibrosis patients was investigated by 500-MHz 1H NMR spectroscopy in conjunction with sugar analysis.
6746638	5	108	dep	A-3	1003:1005	arg1	GalNAc-o1					1099:1107	NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1	1008:1107	NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1	1008:1107	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	5	108	dep	A-3	1003:1005	arg1	alpha					1155:1159	NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)	1115:1167	NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)	1115:1167	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	5	108	dep	A-3	1003:1005	arg1	A-4					1110:1112	A-4	1110:1112	A-4	1110:1112	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	6	109	theme	high	1540:1543	arg1	spectroscopy					1563:1574	high resolution 1H NMR spectroscopy	1540:1574	high resolution 1H NMR spectroscopy	1540:1574	The simultaneous presence of sialic acid in alpha(2----3)-linkage to Gal and fucose in alpha(1----3)-linkage to GlcNAc of the same N-acetyllactosamine unit could be adequately proved by high resolution 1H NMR spectroscopy.
6746638	5	110	theme	1----3	1091:1096	arg1	GalNAc-o1					1099:1107	NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1	1008:1107	NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1	1008:1107	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	3	111	theme	cystic	393:398	arg1	fibrosis					400:407	cystic fibrosis	393:407	cystic fibrosis patients	393:416	The structure of sialylated carbohydrate units of bronchial mucins obtained from cystic fibrosis patients was investigated by 500-MHz 1H NMR spectroscopy in conjunction with sugar analysis.
6746638	5	112	theme	NeuAc	824:828	arg1	beta					847:850	NeuAc alpha(2----3)Gal beta(1----4)	824:858	NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1	824:1222	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	5	113	theme	Gal	1027:1029	arg1	GalNAc-o1					1099:1107	NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1	1008:1107	NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1	1008:1107	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	3	114	theme	sialylated	329:338	arg1	units					353:357	sialylated carbohydrate units	329:357	sialylated carbohydrate units of bronchial mucins obtained from cystic fibrosis patients	329:416	The structure of sialylated carbohydrate units of bronchial mucins obtained from cystic fibrosis patients was investigated by 500-MHz 1H NMR spectroscopy in conjunction with sugar analysis.
6746638	4	115	theme	borohydride	542:552	arg1	degradation					554:564	alkaline borohydride degradation	533:564	alkaline borohydride degradation	533:564	After subjecting the mucins to alkaline borohydride degradation, sialylated oligosaccharide-alditols were isolated by anion-exchange chromatography and fractionated by high performance liquid chromatography.
6746638	3	116	theme	500-MHz	438:444	arg1	spectroscopy					453:464	500-MHz 1H NMR spectroscopy	438:464	500-MHz 1H NMR spectroscopy in conjunction with sugar analysis	438:499	The structure of sialylated carbohydrate units of bronchial mucins obtained from cystic fibrosis patients was investigated by 500-MHz 1H NMR spectroscopy in conjunction with sugar analysis.
6746638	0	117	theme	sialylated	40:49	arg1	oligosaccharides					51:66	five sialylated oligosaccharides	35:66	five sialylated oligosaccharides	35:66	Primary structure determination of five sialylated oligosaccharides derived from bronchial mucus glycoproteins of patients suffering from cystic fibrosis.
6746638	5	118	theme	Gal	934:936	arg1	beta					957:960	NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)	915:968	NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)	915:1212	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	5	119	theme	beta-	1309:1313	arg1	beta					1330:1333	NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)	1229:1341	NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)	1229:1341	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	5	120	theme	alpha-	1235:1240	arg1	beta					1254:1257	NeuAc alpha-(2----3) Gal beta(1----4)	1229:1265	NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)	1229:1341	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	5	121	theme	beta	1138:1141	arg1	alpha					1155:1159	NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)	1115:1167	NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)	1115:1167	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	5	122	theme	[Gal	1304:1307	arg1	beta					1330:1333	NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)	1229:1341	NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)	1229:1341	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	5	123	theme	following	808:816	arg1	structures					773:782	their structures	767:782	their structures	767:782	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	5	123	theme	following	808:816	arg1	GalNAc-o1					1343:1351	: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1	817:1351	the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1	804:1351	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	5	124	theme	alpha	1014:1018	arg1	GalNAc-o1					1099:1107	NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1	1008:1107	NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1	1008:1107	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	3	125	theme	bronchial	362:370	arg1	mucins					372:377	bronchial mucins	362:377	bronchial mucins obtained from cystic fibrosis patients	362:416	The structure of sialylated carbohydrate units of bronchial mucins obtained from cystic fibrosis patients was investigated by 500-MHz 1H NMR spectroscopy in conjunction with sugar analysis.
6746638	6	126	theme	simultaneous	1358:1369	arg1	presence					1371:1378	The simultaneous presence	1354:1378	The simultaneous presence of sialic acid in alpha(2----3)-linkage to Gal and fucose in alpha(1----3)-linkage to GlcNAc of the same N-acetyllactosamine unit	1354:1508	The simultaneous presence of sialic acid in alpha(2----3)-linkage to Gal and fucose in alpha(1----3)-linkage to GlcNAc of the same N-acetyllactosamine unit could be adequately proved by high resolution 1H NMR spectroscopy.
6746638	2	127	theme	1H	291:292	arg1	spectroscopy					298:309	500-MHz 1H NMR spectroscopy	283:309	500-MHz 1H NMR spectroscopy	283:309	structural element revealed by 500-MHz 1H NMR spectroscopy.
6746638	5	128	theme	2----3	1020:1025	arg1	GalNAc-o1					1099:1107	NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1	1008:1107	NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1	1008:1107	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	5	129	theme	alpha	921:925	arg1	beta					957:960	NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)	915:968	NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)	915:1212	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	5	130	theme	NeuAc	915:919	arg1	beta					957:960	NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)	915:968	NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)	915:1212	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	3	131	theme	NMR	449:451	arg1	spectroscopy					453:464	500-MHz 1H NMR spectroscopy	438:464	500-MHz 1H NMR spectroscopy in conjunction with sugar analysis	438:499	The structure of sialylated carbohydrate units of bronchial mucins obtained from cystic fibrosis patients was investigated by 500-MHz 1H NMR spectroscopy in conjunction with sugar analysis.
6746638	5	132	theme	1----3	1055:1060	arg1	GalNAc-o1					1099:1107	NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1	1008:1107	NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1	1008:1107	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	5	133	theme	2----3	927:932	arg1	beta					957:960	NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)	915:968	NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)	915:1212	Five compounds could be obtained in a rather pure state; their structures were established as the following: A-1, NeuAc alpha(2----3)Gal beta(1----4) [Fuc alpha(1----3)]GlcNAc beta(1----3)Gal-NAc-ol; A-2, NeuAc alpha(2----3)Gal beta(1----4)GlcNAc beta(1----6)-[GlcNAc beta (1----3)]GalNAc-o1; A-3, NeuAc alpha(2----3)Gal beta-(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----3)Gal beta(1----3) GalNAc-o1; A-4, NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)]Glc-NAc NAc beta(1----6)[GlcNAc beta(1----3)]GalNAc-o1; A-6,NeuAc alpha-(2----3) Gal beta(1----4)[Fuc alpha(1----3)]GlcNAc beta(1----6)[Gal beta-(1----4) GlcNAc beta(1----3)]GalNAc-o1.
6746638	4	134	theme	anion-exchange	620:633	arg1	chromatography					635:648	anion-exchange chromatography	620:648	anion-exchange chromatography	620:648	After subjecting the mucins to alkaline borohydride degradation, sialylated oligosaccharide-alditols were isolated by anion-exchange chromatography and fractionated by high performance liquid chromatography.
2033371	6	0	theme	labeled	1101:1107	arg1	CD43					1109:1112	carbohydrate labeled CD43	1088:1112	carbohydrate labeled CD43	1088:1112	To examine the O-glycan structures, carbohydrate labeled CD43 was immunoprecipitated and the released oligosaccharides identified.
2033371	9	1	theme	1----4GlcNAc	1961:1972	arg1	beta					1920:1923	NeuNAc alpha 2----3Gal beta 1----3	1897:1930	NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH on CD43	1897:2002	Analyzing the six glycosyltransferases involved in the biosynthesis of these O-glycan structures it was found that in WAS lymphocytes high levels of beta 1----6 N-acetyl-glucosaminyl transferase are responsible for the expression of NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH on CD43.
2033371	9	1	theme	1----4GlcNAc	1961:1972	arg1	beta					1974:1977	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	1933:1984	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	1933:1984	Analyzing the six glycosyltransferases involved in the biosynthesis of these O-glycan structures it was found that in WAS lymphocytes high levels of beta 1----6 N-acetyl-glucosaminyl transferase are responsible for the expression of NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH on CD43.
2033371	10	2	theme	responsible	2014:2024	arg1	gene					2009:2012	The gene	2005:2012	The gene responsible for	2005:2028	The gene responsible for WAS has not yet been identified but the results presented in this study suggest that the primary defect in WAS may affect a gene which is involved in the regulation of O-glycosylation.
2033371	7	3	theme	2----3Gal	1272:1280	arg1	beta					1282:1285	alpha 2----3Gal beta 1----3	1266:1292	predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH	1222:1356	WAS lymphocyte CD43 was found to carry predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH whereas normal lymphocytes carry the structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----6) GalNAcOH.
2033371	7	3	theme	2----3Gal	1272:1280	arg1	beta					1336:1339	NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6	1295:1346	NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6	1295:1346	WAS lymphocyte CD43 was found to carry predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH whereas normal lymphocytes carry the structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----6) GalNAcOH.
2033371	9	4	theme	GalNAcOH	1987:1994	arg1	expression					1883:1892	the expression	1879:1892	the expression of NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH on CD43	1879:2002	Analyzing the six glycosyltransferases involved in the biosynthesis of these O-glycan structures it was found that in WAS lymphocytes high levels of beta 1----6 N-acetyl-glucosaminyl transferase are responsible for the expression of NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH on CD43.
2033371	3	5	dep	carry	676:680	arg1	tested					634:639	tested	634:639	tested	634:639	Immunofluorescence analysis with the carbohydrate dependent anti-CD43 antibody T305 revealed that in 10 out of the 12 WAS patients tested increased numbers of T lymphocytes carry on CD43 an epitope which on normal lymphocytes is expressed only after activation.
2033371	3	6	theme	anti-CD43	563:571	arg1	antibody					573:580	the carbohydrate dependent anti-CD43 antibody T305	536:585	the carbohydrate dependent anti-CD43 antibody T305	536:585	Immunofluorescence analysis with the carbohydrate dependent anti-CD43 antibody T305 revealed that in 10 out of the 12 WAS patients tested increased numbers of T lymphocytes carry on CD43 an epitope which on normal lymphocytes is expressed only after activation.
2033371	5	7	theme	molecular	876:884	arg1	mass					886:889	a high molecular mass	869:889	a high molecular mass form of CD43 which reacted with the T305 antibody and which could be found on in vivo activated lymphocytes but was absent from normal unstimulated lymphocytes	869:1049	Western blots of WAS cell lysates displayed a high molecular mass form of CD43 which reacted with the T305 antibody and which could be found on in vivo activated lymphocytes but was absent from normal unstimulated lymphocytes.
2033371	9	8	from	expression	1883:1892	arg1	CD43					1999:2002	CD43	1999:2002	CD43	1999:2002	Analyzing the six glycosyltransferases involved in the biosynthesis of these O-glycan structures it was found that in WAS lymphocytes high levels of beta 1----6 N-acetyl-glucosaminyl transferase are responsible for the expression of NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH on CD43.
2033371	9	9	theme	structures	1750:1759	arg1	biosynthesis					1719:1730	the biosynthesis	1715:1730	the biosynthesis of these O-glycan structures	1715:1759	Analyzing the six glycosyltransferases involved in the biosynthesis of these O-glycan structures it was found that in WAS lymphocytes high levels of beta 1----6 N-acetyl-glucosaminyl transferase are responsible for the expression of NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH on CD43.
2033371	8	10	from	oligosaccharide	1615:1629	arg1	CD43					1634:1637	CD43	1634:1637	CD43	1634:1637	Only after activation NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH becomes the principal oligosaccharide on CD43 from normal lymphocytes.
2033371	1	11	theme	abnormal	194:201	arg1	behavior					219:226	the abnormal electrophoretic behavior	190:226	the abnormal electrophoretic behavior of the major T lymphocyte sialoglycoprotein CD43	190:275	The only molecular defect reported for the X-linked immunodeficiency Wiskott-Aldrich syndrome (WAS) is the abnormal electrophoretic behavior of the major T lymphocyte sialoglycoprotein CD43.
2033371	1	11	theme	abnormal	194:201	arg1	defect					106:111	The only molecular defect	87:111	The only molecular defect reported for the X-linked immunodeficiency Wiskott-Aldrich syndrome (WAS)	87:185	The only molecular defect reported for the X-linked immunodeficiency Wiskott-Aldrich syndrome (WAS) is the abnormal electrophoretic behavior of the major T lymphocyte sialoglycoprotein CD43.
2033371	2	12	link	O-linked	297:304	arg1	chains					319:324	the 70 to 80 O-linked carbohydrate chains	284:324	the 70 to 80 O-linked carbohydrate chains of CD43	284:332	Since the 70 to 80 O-linked carbohydrate chains of CD43 are known to influence markedly its electrophoretic mobility, we analyzed the structure and the biosynthesis of O-glycans of CD43 in lymphocytes from patients with WAS.
2033371	2	13	theme	carbohydrate	306:317	arg1	chains					319:324	the 70 to 80 O-linked carbohydrate chains	284:324	the 70 to 80 O-linked carbohydrate chains of CD43	284:332	Since the 70 to 80 O-linked carbohydrate chains of CD43 are known to influence markedly its electrophoretic mobility, we analyzed the structure and the biosynthesis of O-glycans of CD43 in lymphocytes from patients with WAS.
2033371	5	14	theme	lysates	851:857	arg1	blots					833:837	Western blots	825:837	Western blots of WAS cell lysates	825:857	Western blots of WAS cell lysates displayed a high molecular mass form of CD43 which reacted with the T305 antibody and which could be found on in vivo activated lymphocytes but was absent from normal unstimulated lymphocytes.
2033371	7	15	theme	beta	1428:1431	arg1	GalNAcOH					1462:1469	the structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----6) GalNAcOH	1391:1469	the structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----6) GalNAcOH	1391:1469	WAS lymphocyte CD43 was found to carry predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH whereas normal lymphocytes carry the structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----6) GalNAcOH.
2033371	9	16	theme	WAS	1782:1784	arg1	lymphocytes					1786:1796	WAS lymphocytes	1782:1796	WAS lymphocytes	1782:1796	Analyzing the six glycosyltransferases involved in the biosynthesis of these O-glycan structures it was found that in WAS lymphocytes high levels of beta 1----6 N-acetyl-glucosaminyl transferase are responsible for the expression of NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH on CD43.
2033371	8	17	theme	NeuNAc	1494:1499	arg1	beta					1517:1520	activation NeuNAc alpha 2----3Gal beta 1----3	1483:1527	activation NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6)	1483:1582	Only after activation NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH becomes the principal oligosaccharide on CD43 from normal lymphocytes.
2033371	8	17	theme	NeuNAc	1494:1499	arg1	beta					1571:1574	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	1530:1581	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	1530:1581	Only after activation NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH becomes the principal oligosaccharide on CD43 from normal lymphocytes.
2033371	7	18	theme	alpha	1412:1416	arg1	alpha					1448:1452	NeuNAc alpha 2----6	1441:1459	NeuNAc alpha 2----6	1441:1459	WAS lymphocyte CD43 was found to carry predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH whereas normal lymphocytes carry the structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----6) GalNAcOH.
2033371	7	18	theme	alpha	1412:1416	arg1	beta					1428:1431	structure NeuNAc alpha 2----3Gal beta 1----3	1395:1438	the structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----6) GalNAcOH	1391:1469	WAS lymphocyte CD43 was found to carry predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH whereas normal lymphocytes carry the structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----6) GalNAcOH.
2033371	9	19	theme	high	1798:1801	arg1	levels					1803:1808	high levels	1798:1808	high levels of beta 1----6 N-acetyl-glucosaminyl transferase	1798:1857	Analyzing the six glycosyltransferases involved in the biosynthesis of these O-glycan structures it was found that in WAS lymphocytes high levels of beta 1----6 N-acetyl-glucosaminyl transferase are responsible for the expression of NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH on CD43.
2033371	8	20	theme	2----3Gal	1507:1515	arg1	beta					1517:1520	activation NeuNAc alpha 2----3Gal beta 1----3	1483:1527	activation NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6)	1483:1582	Only after activation NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH becomes the principal oligosaccharide on CD43 from normal lymphocytes.
2033371	8	20	theme	2----3Gal	1507:1515	arg1	beta					1571:1574	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	1530:1581	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	1530:1581	Only after activation NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH becomes the principal oligosaccharide on CD43 from normal lymphocytes.
2033371	7	21	theme	structure	1395:1403	arg1	alpha					1448:1452	NeuNAc alpha 2----6	1441:1459	NeuNAc alpha 2----6	1441:1459	WAS lymphocyte CD43 was found to carry predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH whereas normal lymphocytes carry the structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----6) GalNAcOH.
2033371	7	21	theme	structure	1395:1403	arg1	beta					1428:1431	structure NeuNAc alpha 2----3Gal beta 1----3	1395:1438	the structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----6) GalNAcOH	1391:1469	WAS lymphocyte CD43 was found to carry predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH whereas normal lymphocytes carry the structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----6) GalNAcOH.
2033371	10	22	theme	O-glycosylation	2198:2212	arg1	regulation					2184:2193	the regulation	2180:2193	the regulation of O-glycosylation	2180:2212	The gene responsible for WAS has not yet been identified but the results presented in this study suggest that the primary defect in WAS may affect a gene which is involved in the regulation of O-glycosylation.
2033371	3	23	theme	increased	641:649	arg1	numbers					651:657	increased numbers	641:657	increased numbers of T lymphocytes	641:674	Immunofluorescence analysis with the carbohydrate dependent anti-CD43 antibody T305 revealed that in 10 out of the 12 WAS patients tested increased numbers of T lymphocytes carry on CD43 an epitope which on normal lymphocytes is expressed only after activation.
2033371	1	24	theme	immunodeficiency	139:154	arg1	syndrome					172:179	the X-linked immunodeficiency Wiskott-Aldrich syndrome	126:179	the X-linked immunodeficiency Wiskott-Aldrich syndrome (WAS)	126:185	The only molecular defect reported for the X-linked immunodeficiency Wiskott-Aldrich syndrome (WAS) is the abnormal electrophoretic behavior of the major T lymphocyte sialoglycoprotein CD43.
2033371	1	25	theme	X-linked	130:137	arg1	syndrome					172:179	the X-linked immunodeficiency Wiskott-Aldrich syndrome	126:179	the X-linked immunodeficiency Wiskott-Aldrich syndrome (WAS)	126:185	The only molecular defect reported for the X-linked immunodeficiency Wiskott-Aldrich syndrome (WAS) is the abnormal electrophoretic behavior of the major T lymphocyte sialoglycoprotein CD43.
2033371	1	26	theme	electrophoretic	203:217	arg1	behavior					219:226	the abnormal electrophoretic behavior	190:226	the abnormal electrophoretic behavior of the major T lymphocyte sialoglycoprotein CD43	190:275	The only molecular defect reported for the X-linked immunodeficiency Wiskott-Aldrich syndrome (WAS) is the abnormal electrophoretic behavior of the major T lymphocyte sialoglycoprotein CD43.
2033371	1	26	theme	electrophoretic	203:217	arg1	defect					106:111	The only molecular defect	87:111	The only molecular defect reported for the X-linked immunodeficiency Wiskott-Aldrich syndrome (WAS)	87:185	The only molecular defect reported for the X-linked immunodeficiency Wiskott-Aldrich syndrome (WAS) is the abnormal electrophoretic behavior of the major T lymphocyte sialoglycoprotein CD43.
2033371	7	27	theme	alpha	1266:1270	arg1	beta					1282:1285	alpha 2----3Gal beta 1----3	1266:1292	predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH	1222:1356	WAS lymphocyte CD43 was found to carry predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH whereas normal lymphocytes carry the structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----6) GalNAcOH.
2033371	7	27	theme	alpha	1266:1270	arg1	beta					1336:1339	NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6	1295:1346	NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6	1295:1346	WAS lymphocyte CD43 was found to carry predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH whereas normal lymphocytes carry the structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----6) GalNAcOH.
2033371	3	28	theme	patients	625:632	arg1	patients					625:632	the 12 WAS patients	614:632	the 12 WAS patients	614:632	Immunofluorescence analysis with the carbohydrate dependent anti-CD43 antibody T305 revealed that in 10 out of the 12 WAS patients tested increased numbers of T lymphocytes carry on CD43 an epitope which on normal lymphocytes is expressed only after activation.
2033371	3	28	theme	patients	625:632	arg1	10					604:605	10	604:605	10	604:605	Immunofluorescence analysis with the carbohydrate dependent anti-CD43 antibody T305 revealed that in 10 out of the 12 WAS patients tested increased numbers of T lymphocytes carry on CD43 an epitope which on normal lymphocytes is expressed only after activation.
2033371	2	29	with	patients	484:491	arg1	WAS					498:500	WAS	498:500	WAS	498:500	Since the 70 to 80 O-linked carbohydrate chains of CD43 are known to influence markedly its electrophoretic mobility, we analyzed the structure and the biosynthesis of O-glycans of CD43 in lymphocytes from patients with WAS.
2033371	5	30	theme	CD43	899:902	arg1	form					891:894	a high molecular mass form	869:894	a high molecular mass form of CD43 which reacted with the T305 antibody and which could be found on in vivo activated lymphocytes but was absent from normal unstimulated lymphocytes	869:1049	Western blots of WAS cell lysates displayed a high molecular mass form of CD43 which reacted with the T305 antibody and which could be found on in vivo activated lymphocytes but was absent from normal unstimulated lymphocytes.
2033371	9	31	from	lymphocytes	1786:1796	arg1	responsible					1863:1873	responsible	1863:1873	responsible	1863:1873	Analyzing the six glycosyltransferases involved in the biosynthesis of these O-glycan structures it was found that in WAS lymphocytes high levels of beta 1----6 N-acetyl-glucosaminyl transferase are responsible for the expression of NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH on CD43.
2033371	9	32	theme	1----6	1818:1823	arg1	transferase					1847:1857	beta 1----6 N-acetyl-glucosaminyl transferase	1813:1857	beta 1----6 N-acetyl-glucosaminyl transferase	1813:1857	Analyzing the six glycosyltransferases involved in the biosynthesis of these O-glycan structures it was found that in WAS lymphocytes high levels of beta 1----6 N-acetyl-glucosaminyl transferase are responsible for the expression of NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH on CD43.
2033371	8	33	theme	NeuNAc	1530:1535	arg1	beta					1571:1574	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	1530:1581	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	1530:1581	Only after activation NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH becomes the principal oligosaccharide on CD43 from normal lymphocytes.
2033371	8	33	theme	NeuNAc	1530:1535	arg1	beta					1517:1520	activation NeuNAc alpha 2----3Gal beta 1----3	1483:1527	activation NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6)	1483:1582	Only after activation NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH becomes the principal oligosaccharide on CD43 from normal lymphocytes.
2033371	7	34	theme	structure	1249:1257	arg1	GalNAcOH					1349:1356	predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH	1222:1356	predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH	1222:1356	WAS lymphocyte CD43 was found to carry predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH whereas normal lymphocytes carry the structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----6) GalNAcOH.
2033371	9	35	theme	transferase	1847:1857	arg1	levels					1803:1808	high levels	1798:1808	high levels of beta 1----6 N-acetyl-glucosaminyl transferase	1798:1857	Analyzing the six glycosyltransferases involved in the biosynthesis of these O-glycan structures it was found that in WAS lymphocytes high levels of beta 1----6 N-acetyl-glucosaminyl transferase are responsible for the expression of NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH on CD43.
2033371	8	36	theme	2----3Gal	1543:1551	arg1	beta					1571:1574	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	1530:1581	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	1530:1581	Only after activation NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH becomes the principal oligosaccharide on CD43 from normal lymphocytes.
2033371	8	36	theme	2----3Gal	1543:1551	arg1	beta					1517:1520	activation NeuNAc alpha 2----3Gal beta 1----3	1483:1527	activation NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6)	1483:1582	Only after activation NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH becomes the principal oligosaccharide on CD43 from normal lymphocytes.
2033371	7	37	theme	branched	1240:1247	arg1	GalNAcOH					1349:1356	predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH	1222:1356	predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH	1222:1356	WAS lymphocyte CD43 was found to carry predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH whereas normal lymphocytes carry the structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----6) GalNAcOH.
2033371	1	38	gly	sialoglycoprotein	254:270	arg1	sialoglycoprotein					254:270	the major T lymphocyte sialoglycoprotein CD43	231:275	the major T lymphocyte sialoglycoprotein CD43	231:275	The only molecular defect reported for the X-linked immunodeficiency Wiskott-Aldrich syndrome (WAS) is the abnormal electrophoretic behavior of the major T lymphocyte sialoglycoprotein CD43.
2033371	0	39	from	patients	47:54	arg1	lymphocytes					30:40	lymphocytes	30:40	lymphocytes from patients with Wiskott-Aldrich syndrome	30:84	Altered O-glycan synthesis in lymphocytes from patients with Wiskott-Aldrich syndrome.
2033371	9	40	from	CD43	1999:2002	arg1	expression					1883:1892	the expression	1879:1892	the expression of NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH on CD43	1879:2002	Analyzing the six glycosyltransferases involved in the biosynthesis of these O-glycan structures it was found that in WAS lymphocytes high levels of beta 1----6 N-acetyl-glucosaminyl transferase are responsible for the expression of NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH on CD43.
2033371	2	41	theme	CD43	459:462	arg1	O-glycans					446:454	O-glycans	446:454	O-glycans of CD43	446:462	Since the 70 to 80 O-linked carbohydrate chains of CD43 are known to influence markedly its electrophoretic mobility, we analyzed the structure and the biosynthesis of O-glycans of CD43 in lymphocytes from patients with WAS.
2033371	1	42	theme	molecular	96:104	arg1	behavior					219:226	the abnormal electrophoretic behavior	190:226	the abnormal electrophoretic behavior of the major T lymphocyte sialoglycoprotein CD43	190:275	The only molecular defect reported for the X-linked immunodeficiency Wiskott-Aldrich syndrome (WAS) is the abnormal electrophoretic behavior of the major T lymphocyte sialoglycoprotein CD43.
2033371	1	42	theme	molecular	96:104	arg1	defect					106:111	The only molecular defect	87:111	The only molecular defect reported for the X-linked immunodeficiency Wiskott-Aldrich syndrome (WAS)	87:185	The only molecular defect reported for the X-linked immunodeficiency Wiskott-Aldrich syndrome (WAS) is the abnormal electrophoretic behavior of the major T lymphocyte sialoglycoprotein CD43.
2033371	2	43	theme	O-glycans	446:454	arg1	structure					412:420	structure	412:420	structure	412:420	Since the 70 to 80 O-linked carbohydrate chains of CD43 are known to influence markedly its electrophoretic mobility, we analyzed the structure and the biosynthesis of O-glycans of CD43 in lymphocytes from patients with WAS.
2033371	2	43	theme	O-glycans	446:454	arg1	biosynthesis					430:441	the biosynthesis	426:441	the biosynthesis	426:441	Since the 70 to 80 O-linked carbohydrate chains of CD43 are known to influence markedly its electrophoretic mobility, we analyzed the structure and the biosynthesis of O-glycans of CD43 in lymphocytes from patients with WAS.
2033371	4	44	theme	Other	765:769	arg1	antigens					782:789	Other activation antigens	765:789	Other activation antigens	765:789	Other activation antigens were absent from WAS lymphocytes.
2033371	5	45	theme	WAS	842:844	arg1	lysates					851:857	WAS cell lysates	842:857	WAS cell lysates	842:857	Western blots of WAS cell lysates displayed a high molecular mass form of CD43 which reacted with the T305 antibody and which could be found on in vivo activated lymphocytes but was absent from normal unstimulated lymphocytes.
2033371	9	46	from	responsible	1863:1873	arg1	lymphocytes					1786:1796	WAS lymphocytes	1782:1796	WAS lymphocytes	1782:1796	Analyzing the six glycosyltransferases involved in the biosynthesis of these O-glycan structures it was found that in WAS lymphocytes high levels of beta 1----6 N-acetyl-glucosaminyl transferase are responsible for the expression of NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH on CD43.
2033371	9	47	theme	alpha	1904:1908	arg1	beta					1974:1977	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	1933:1984	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	1933:1984	Analyzing the six glycosyltransferases involved in the biosynthesis of these O-glycan structures it was found that in WAS lymphocytes high levels of beta 1----6 N-acetyl-glucosaminyl transferase are responsible for the expression of NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH on CD43.
2033371	9	47	theme	alpha	1904:1908	arg1	beta					1920:1923	NeuNAc alpha 2----3Gal beta 1----3	1897:1930	NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH on CD43	1897:2002	Analyzing the six glycosyltransferases involved in the biosynthesis of these O-glycan structures it was found that in WAS lymphocytes high levels of beta 1----6 N-acetyl-glucosaminyl transferase are responsible for the expression of NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH on CD43.
2033371	3	48	theme	lymphocytes	664:674	arg1	numbers					651:657	increased numbers	641:657	increased numbers of T lymphocytes	641:674	Immunofluorescence analysis with the carbohydrate dependent anti-CD43 antibody T305 revealed that in 10 out of the 12 WAS patients tested increased numbers of T lymphocytes carry on CD43 an epitope which on normal lymphocytes is expressed only after activation.
2033371	7	49	theme	WAS	1183:1185	arg1	CD43					1198:1201	WAS lymphocyte CD43	1183:1201	WAS lymphocyte CD43	1183:1201	WAS lymphocyte CD43 was found to carry predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH whereas normal lymphocytes carry the structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----6) GalNAcOH.
2033371	7	50	theme	beta	1282:1285	arg1	GalNAcOH					1349:1356	predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH	1222:1356	predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH	1222:1356	WAS lymphocyte CD43 was found to carry predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH whereas normal lymphocytes carry the structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----6) GalNAcOH.
2033371	9	51	theme	beta	1920:1923	arg1	GalNAcOH					1987:1994	NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH	1897:1994	NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH on CD43	1897:2002	Analyzing the six glycosyltransferases involved in the biosynthesis of these O-glycan structures it was found that in WAS lymphocytes high levels of beta 1----6 N-acetyl-glucosaminyl transferase are responsible for the expression of NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH on CD43.
2033371	1	52	link	X-linked	130:137	arg1	syndrome					172:179	the X-linked immunodeficiency Wiskott-Aldrich syndrome	126:179	the X-linked immunodeficiency Wiskott-Aldrich syndrome (WAS)	126:185	The only molecular defect reported for the X-linked immunodeficiency Wiskott-Aldrich syndrome (WAS) is the abnormal electrophoretic behavior of the major T lymphocyte sialoglycoprotein CD43.
2033371	0	53	theme	Wiskott-Aldrich	61:75	arg1	syndrome					77:84	Wiskott-Aldrich syndrome	61:84	Wiskott-Aldrich syndrome	61:84	Altered O-glycan synthesis in lymphocytes from patients with Wiskott-Aldrich syndrome.
2033371	5	54	theme	unstimulated	1026:1037	arg1	lymphocytes					1039:1049	normal unstimulated lymphocytes	1019:1049	normal unstimulated lymphocytes	1019:1049	Western blots of WAS cell lysates displayed a high molecular mass form of CD43 which reacted with the T305 antibody and which could be found on in vivo activated lymphocytes but was absent from normal unstimulated lymphocytes.
2033371	7	55	theme	beta	1318:1321	arg1	beta					1336:1339	NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6	1295:1346	NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6	1295:1346	WAS lymphocyte CD43 was found to carry predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH whereas normal lymphocytes carry the structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----6) GalNAcOH.
2033371	7	55	theme	beta	1318:1321	arg1	beta					1282:1285	alpha 2----3Gal beta 1----3	1266:1292	predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH	1222:1356	WAS lymphocyte CD43 was found to carry predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH whereas normal lymphocytes carry the structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----6) GalNAcOH.
2033371	4	56	theme	WAS	808:810	arg1	lymphocytes					812:822	WAS lymphocytes	808:822	WAS lymphocytes	808:822	Other activation antigens were absent from WAS lymphocytes.
2033371	1	57	theme	major	235:239	arg1	CD43					272:275	the major T lymphocyte sialoglycoprotein CD43	231:275	the major T lymphocyte sialoglycoprotein CD43	231:275	The only molecular defect reported for the X-linked immunodeficiency Wiskott-Aldrich syndrome (WAS) is the abnormal electrophoretic behavior of the major T lymphocyte sialoglycoprotein CD43.
2033371	7	58	theme	alpha	1302:1306	arg1	beta					1336:1339	NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6	1295:1346	NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6	1295:1346	WAS lymphocyte CD43 was found to carry predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH whereas normal lymphocytes carry the structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----6) GalNAcOH.
2033371	7	58	theme	alpha	1302:1306	arg1	beta					1282:1285	alpha 2----3Gal beta 1----3	1266:1292	predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH	1222:1356	WAS lymphocyte CD43 was found to carry predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH whereas normal lymphocytes carry the structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----6) GalNAcOH.
2033371	9	59	theme	alpha	1940:1944	arg1	beta					1920:1923	NeuNAc alpha 2----3Gal beta 1----3	1897:1930	NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH on CD43	1897:2002	Analyzing the six glycosyltransferases involved in the biosynthesis of these O-glycan structures it was found that in WAS lymphocytes high levels of beta 1----6 N-acetyl-glucosaminyl transferase are responsible for the expression of NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH on CD43.
2033371	9	59	theme	alpha	1940:1944	arg1	beta					1974:1977	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	1933:1984	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	1933:1984	Analyzing the six glycosyltransferases involved in the biosynthesis of these O-glycan structures it was found that in WAS lymphocytes high levels of beta 1----6 N-acetyl-glucosaminyl transferase are responsible for the expression of NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH on CD43.
2033371	8	60	theme	normal	1644:1649	arg1	lymphocytes					1651:1661	normal lymphocytes	1644:1661	normal lymphocytes	1644:1661	Only after activation NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH becomes the principal oligosaccharide on CD43 from normal lymphocytes.
2033371	0	61	with	patients	47:54	arg1	syndrome					77:84	Wiskott-Aldrich syndrome	61:84	Wiskott-Aldrich syndrome	61:84	Altered O-glycan synthesis in lymphocytes from patients with Wiskott-Aldrich syndrome.
2033371	1	62	theme	lymphocyte	243:252	arg1	CD43					272:275	the major T lymphocyte sialoglycoprotein CD43	231:275	the major T lymphocyte sialoglycoprotein CD43	231:275	The only molecular defect reported for the X-linked immunodeficiency Wiskott-Aldrich syndrome (WAS) is the abnormal electrophoretic behavior of the major T lymphocyte sialoglycoprotein CD43.
2033371	2	63	from	biosynthesis	430:441	arg1	lymphocytes					467:477	lymphocytes	467:477	lymphocytes from patients with WAS	467:500	Since the 70 to 80 O-linked carbohydrate chains of CD43 are known to influence markedly its electrophoretic mobility, we analyzed the structure and the biosynthesis of O-glycans of CD43 in lymphocytes from patients with WAS.
2033371	2	63	from	biosynthesis	430:441	arg1	patients					484:491	patients	484:491	patients with WAS	484:500	Since the 70 to 80 O-linked carbohydrate chains of CD43 are known to influence markedly its electrophoretic mobility, we analyzed the structure and the biosynthesis of O-glycans of CD43 in lymphocytes from patients with WAS.
2033371	9	64	theme	beta	1956:1959	arg1	beta					1920:1923	NeuNAc alpha 2----3Gal beta 1----3	1897:1930	NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH on CD43	1897:2002	Analyzing the six glycosyltransferases involved in the biosynthesis of these O-glycan structures it was found that in WAS lymphocytes high levels of beta 1----6 N-acetyl-glucosaminyl transferase are responsible for the expression of NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH on CD43.
2033371	9	64	theme	beta	1956:1959	arg1	beta					1974:1977	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	1933:1984	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	1933:1984	Analyzing the six glycosyltransferases involved in the biosynthesis of these O-glycan structures it was found that in WAS lymphocytes high levels of beta 1----6 N-acetyl-glucosaminyl transferase are responsible for the expression of NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH on CD43.
2033371	0	65	theme	O-glycan	8:15	arg1	synthesis					17:25	O-glycan synthesis	8:25	O-glycan synthesis	8:25	Altered O-glycan synthesis in lymphocytes from patients with Wiskott-Aldrich syndrome.
2033371	3	66	theme	normal	710:715	arg1	lymphocytes					717:727	normal lymphocytes	710:727	normal lymphocytes	710:727	Immunofluorescence analysis with the carbohydrate dependent anti-CD43 antibody T305 revealed that in 10 out of the 12 WAS patients tested increased numbers of T lymphocytes carry on CD43 an epitope which on normal lymphocytes is expressed only after activation.
2033371	3	67	with	analysis	522:529	arg1	antibody					573:580	the carbohydrate dependent anti-CD43 antibody T305	536:585	the carbohydrate dependent anti-CD43 antibody T305	536:585	Immunofluorescence analysis with the carbohydrate dependent anti-CD43 antibody T305 revealed that in 10 out of the 12 WAS patients tested increased numbers of T lymphocytes carry on CD43 an epitope which on normal lymphocytes is expressed only after activation.
2033371	1	68	theme	CD43	272:275	arg1	behavior					219:226	the abnormal electrophoretic behavior	190:226	the abnormal electrophoretic behavior of the major T lymphocyte sialoglycoprotein CD43	190:275	The only molecular defect reported for the X-linked immunodeficiency Wiskott-Aldrich syndrome (WAS) is the abnormal electrophoretic behavior of the major T lymphocyte sialoglycoprotein CD43.
2033371	1	68	theme	CD43	272:275	arg1	defect					106:111	The only molecular defect	87:111	The only molecular defect reported for the X-linked immunodeficiency Wiskott-Aldrich syndrome (WAS)	87:185	The only molecular defect reported for the X-linked immunodeficiency Wiskott-Aldrich syndrome (WAS) is the abnormal electrophoretic behavior of the major T lymphocyte sialoglycoprotein CD43.
2033371	6	69	theme	carbohydrate	1088:1099	arg1	CD43					1109:1112	carbohydrate labeled CD43	1088:1112	carbohydrate labeled CD43	1088:1112	To examine the O-glycan structures, carbohydrate labeled CD43 was immunoprecipitated and the released oligosaccharides identified.
2033371	2	70	theme	O-linked	297:304	arg1	chains					319:324	the 70 to 80 O-linked carbohydrate chains	284:324	the 70 to 80 O-linked carbohydrate chains of CD43	284:332	Since the 70 to 80 O-linked carbohydrate chains of CD43 are known to influence markedly its electrophoretic mobility, we analyzed the structure and the biosynthesis of O-glycans of CD43 in lymphocytes from patients with WAS.
2033371	7	71	theme	2----3Gal	1308:1316	arg1	beta					1336:1339	NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6	1295:1346	NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6	1295:1346	WAS lymphocyte CD43 was found to carry predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH whereas normal lymphocytes carry the structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----6) GalNAcOH.
2033371	7	71	theme	2----3Gal	1308:1316	arg1	beta					1282:1285	alpha 2----3Gal beta 1----3	1266:1292	predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH	1222:1356	WAS lymphocyte CD43 was found to carry predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH whereas normal lymphocytes carry the structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----6) GalNAcOH.
2033371	3	72	theme	dependent	553:561	arg1	antibody					573:580	the carbohydrate dependent anti-CD43 antibody T305	536:585	the carbohydrate dependent anti-CD43 antibody T305	536:585	Immunofluorescence analysis with the carbohydrate dependent anti-CD43 antibody T305 revealed that in 10 out of the 12 WAS patients tested increased numbers of T lymphocytes carry on CD43 an epitope which on normal lymphocytes is expressed only after activation.
2033371	5	73	theme	high	871:874	arg1	mass					886:889	a high molecular mass	869:889	a high molecular mass form of CD43 which reacted with the T305 antibody and which could be found on in vivo activated lymphocytes but was absent from normal unstimulated lymphocytes	869:1049	Western blots of WAS cell lysates displayed a high molecular mass form of CD43 which reacted with the T305 antibody and which could be found on in vivo activated lymphocytes but was absent from normal unstimulated lymphocytes.
2033371	9	74	theme	O-glycan	1741:1748	arg1	structures					1750:1759	these O-glycan structures	1735:1759	these O-glycan structures	1735:1759	Analyzing the six glycosyltransferases involved in the biosynthesis of these O-glycan structures it was found that in WAS lymphocytes high levels of beta 1----6 N-acetyl-glucosaminyl transferase are responsible for the expression of NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH on CD43.
2033371	3	75	contain	carry	676:680	arg2	epitope					693:699	an epitope	690:699	an epitope which on normal lymphocytes is expressed only after activation	690:762	Immunofluorescence analysis with the carbohydrate dependent anti-CD43 antibody T305 revealed that in 10 out of the 12 WAS patients tested increased numbers of T lymphocytes carry on CD43 an epitope which on normal lymphocytes is expressed only after activation.
2033371	3	75	contain	carry	676:680	arg1	numbers					651:657	increased numbers	641:657	increased numbers of T lymphocytes	641:674	Immunofluorescence analysis with the carbohydrate dependent anti-CD43 antibody T305 revealed that in 10 out of the 12 WAS patients tested increased numbers of T lymphocytes carry on CD43 an epitope which on normal lymphocytes is expressed only after activation.
2033371	3	75	contain	carry	676:680	arg3	patients					625:632	the 12 WAS patients	614:632	the 12 WAS patients	614:632	Immunofluorescence analysis with the carbohydrate dependent anti-CD43 antibody T305 revealed that in 10 out of the 12 WAS patients tested increased numbers of T lymphocytes carry on CD43 an epitope which on normal lymphocytes is expressed only after activation.
2033371	3	75	contain	carry	676:680	arg3	CD43					685:688	CD43	685:688	CD43	685:688	Immunofluorescence analysis with the carbohydrate dependent anti-CD43 antibody T305 revealed that in 10 out of the 12 WAS patients tested increased numbers of T lymphocytes carry on CD43 an epitope which on normal lymphocytes is expressed only after activation.
2033371	3	75	contain	carry	676:680	arg3	10					604:605	10	604:605	10	604:605	Immunofluorescence analysis with the carbohydrate dependent anti-CD43 antibody T305 revealed that in 10 out of the 12 WAS patients tested increased numbers of T lymphocytes carry on CD43 an epitope which on normal lymphocytes is expressed only after activation.
2033371	9	76	dep	found	1768:1772	arg1	Analyzing					1664:1672	Analyzing	1664:1672	Analyzing the six glycosyltransferases involved in the biosynthesis of these O-glycan structures	1664:1759	Analyzing the six glycosyltransferases involved in the biosynthesis of these O-glycan structures it was found that in WAS lymphocytes high levels of beta 1----6 N-acetyl-glucosaminyl transferase are responsible for the expression of NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH on CD43.
2033371	2	77	theme	CD43	329:332	arg1	chains					319:324	the 70 to 80 O-linked carbohydrate chains	284:324	the 70 to 80 O-linked carbohydrate chains of CD43	284:332	Since the 70 to 80 O-linked carbohydrate chains of CD43 are known to influence markedly its electrophoretic mobility, we analyzed the structure and the biosynthesis of O-glycans of CD43 in lymphocytes from patients with WAS.
2033371	5	78	theme	mass	886:889	arg1	form					891:894	a high molecular mass form	869:894	a high molecular mass form of CD43 which reacted with the T305 antibody and which could be found on in vivo activated lymphocytes but was absent from normal unstimulated lymphocytes	869:1049	Western blots of WAS cell lysates displayed a high molecular mass form of CD43 which reacted with the T305 antibody and which could be found on in vivo activated lymphocytes but was absent from normal unstimulated lymphocytes.
2033371	5	79	theme	cell	846:849	arg1	lysates					851:857	WAS cell lysates	842:857	WAS cell lysates	842:857	Western blots of WAS cell lysates displayed a high molecular mass form of CD43 which reacted with the T305 antibody and which could be found on in vivo activated lymphocytes but was absent from normal unstimulated lymphocytes.
2033371	8	80	theme	activation	1483:1492	arg1	beta					1517:1520	activation NeuNAc alpha 2----3Gal beta 1----3	1483:1527	activation NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6)	1483:1582	Only after activation NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH becomes the principal oligosaccharide on CD43 from normal lymphocytes.
2033371	8	80	theme	activation	1483:1492	arg1	beta					1571:1574	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	1530:1581	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	1530:1581	Only after activation NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH becomes the principal oligosaccharide on CD43 from normal lymphocytes.
2033371	7	81	theme	NeuNAc	1441:1446	arg1	alpha					1448:1452	NeuNAc alpha 2----6	1441:1459	NeuNAc alpha 2----6	1441:1459	WAS lymphocyte CD43 was found to carry predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH whereas normal lymphocytes carry the structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----6) GalNAcOH.
2033371	7	81	theme	NeuNAc	1441:1446	arg1	beta					1428:1431	structure NeuNAc alpha 2----3Gal beta 1----3	1395:1438	the structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----6) GalNAcOH	1391:1469	WAS lymphocyte CD43 was found to carry predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH whereas normal lymphocytes carry the structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----6) GalNAcOH.
2033371	8	82	from	lymphocytes	1651:1661	arg1	oligosaccharide					1615:1629	the principal oligosaccharide	1601:1629	the principal oligosaccharide on CD43 from normal lymphocytes	1601:1661	Only after activation NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH becomes the principal oligosaccharide on CD43 from normal lymphocytes.
2033371	8	83	theme	alpha	1501:1505	arg1	beta					1517:1520	activation NeuNAc alpha 2----3Gal beta 1----3	1483:1527	activation NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6)	1483:1582	Only after activation NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH becomes the principal oligosaccharide on CD43 from normal lymphocytes.
2033371	8	83	theme	alpha	1501:1505	arg1	beta					1571:1574	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	1530:1581	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	1530:1581	Only after activation NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH becomes the principal oligosaccharide on CD43 from normal lymphocytes.
2033371	7	84	theme	2----3Gal	1418:1426	arg1	alpha					1448:1452	NeuNAc alpha 2----6	1441:1459	NeuNAc alpha 2----6	1441:1459	WAS lymphocyte CD43 was found to carry predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH whereas normal lymphocytes carry the structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----6) GalNAcOH.
2033371	7	84	theme	2----3Gal	1418:1426	arg1	beta					1428:1431	structure NeuNAc alpha 2----3Gal beta 1----3	1395:1438	the structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----6) GalNAcOH	1391:1469	WAS lymphocyte CD43 was found to carry predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH whereas normal lymphocytes carry the structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----6) GalNAcOH.
2033371	5	85	theme	T305	927:930	arg1	antibody					932:939	the T305 antibody	923:939	the T305 antibody	923:939	Western blots of WAS cell lysates displayed a high molecular mass form of CD43 which reacted with the T305 antibody and which could be found on in vivo activated lymphocytes but was absent from normal unstimulated lymphocytes.
2033371	7	86	theme	NeuNAc	1405:1410	arg1	alpha					1448:1452	NeuNAc alpha 2----6	1441:1459	NeuNAc alpha 2----6	1441:1459	WAS lymphocyte CD43 was found to carry predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH whereas normal lymphocytes carry the structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----6) GalNAcOH.
2033371	7	86	theme	NeuNAc	1405:1410	arg1	beta					1428:1431	structure NeuNAc alpha 2----3Gal beta 1----3	1395:1438	the structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----6) GalNAcOH	1391:1469	WAS lymphocyte CD43 was found to carry predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH whereas normal lymphocytes carry the structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----6) GalNAcOH.
2033371	7	87	theme	NeuNAc	1259:1264	arg1	GalNAcOH					1349:1356	predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH	1222:1356	predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH	1222:1356	WAS lymphocyte CD43 was found to carry predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH whereas normal lymphocytes carry the structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----6) GalNAcOH.
2033371	3	88	theme	WAS	621:623	arg1	patients					625:632	the 12 WAS patients	614:632	the 12 WAS patients	614:632	Immunofluorescence analysis with the carbohydrate dependent anti-CD43 antibody T305 revealed that in 10 out of the 12 WAS patients tested increased numbers of T lymphocytes carry on CD43 an epitope which on normal lymphocytes is expressed only after activation.
2033371	4	89	from	lymphocytes	812:822	arg1	absent					796:801	absent	796:801	absent	796:801	Other activation antigens were absent from WAS lymphocytes.
2033371	1	90	theme	Wiskott-Aldrich	156:170	arg1	syndrome					172:179	the X-linked immunodeficiency Wiskott-Aldrich syndrome	126:179	the X-linked immunodeficiency Wiskott-Aldrich syndrome (WAS)	126:185	The only molecular defect reported for the X-linked immunodeficiency Wiskott-Aldrich syndrome (WAS) is the abnormal electrophoretic behavior of the major T lymphocyte sialoglycoprotein CD43.
2033371	9	91	theme	beta	1813:1816	arg1	transferase					1847:1857	beta 1----6 N-acetyl-glucosaminyl transferase	1813:1857	beta 1----6 N-acetyl-glucosaminyl transferase	1813:1857	Analyzing the six glycosyltransferases involved in the biosynthesis of these O-glycan structures it was found that in WAS lymphocytes high levels of beta 1----6 N-acetyl-glucosaminyl transferase are responsible for the expression of NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH on CD43.
2033371	8	92	theme	alpha	1537:1541	arg1	beta					1571:1574	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	1530:1581	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	1530:1581	Only after activation NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH becomes the principal oligosaccharide on CD43 from normal lymphocytes.
2033371	8	92	theme	alpha	1537:1541	arg1	beta					1517:1520	activation NeuNAc alpha 2----3Gal beta 1----3	1483:1527	activation NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6)	1483:1582	Only after activation NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH becomes the principal oligosaccharide on CD43 from normal lymphocytes.
2033371	9	93	from	GalNAcOH	1987:1994	arg1	CD43					1999:2002	CD43	1999:2002	CD43	1999:2002	Analyzing the six glycosyltransferases involved in the biosynthesis of these O-glycan structures it was found that in WAS lymphocytes high levels of beta 1----6 N-acetyl-glucosaminyl transferase are responsible for the expression of NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH on CD43.
2033371	5	94	from	lymphocytes	1039:1049	arg1	absent					1007:1012	absent	1007:1012	absent	1007:1012	Western blots of WAS cell lysates displayed a high molecular mass form of CD43 which reacted with the T305 antibody and which could be found on in vivo activated lymphocytes but was absent from normal unstimulated lymphocytes.
2033371	9	95	theme	N-acetyl-glucosaminyl	1825:1845	arg1	transferase					1847:1857	beta 1----6 N-acetyl-glucosaminyl transferase	1813:1857	beta 1----6 N-acetyl-glucosaminyl transferase	1813:1857	Analyzing the six glycosyltransferases involved in the biosynthesis of these O-glycan structures it was found that in WAS lymphocytes high levels of beta 1----6 N-acetyl-glucosaminyl transferase are responsible for the expression of NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH on CD43.
2033371	8	96	theme	beta	1553:1556	arg1	beta					1571:1574	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	1530:1581	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	1530:1581	Only after activation NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH becomes the principal oligosaccharide on CD43 from normal lymphocytes.
2033371	8	96	theme	beta	1553:1556	arg1	beta					1517:1520	activation NeuNAc alpha 2----3Gal beta 1----3	1483:1527	activation NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6)	1483:1582	Only after activation NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH becomes the principal oligosaccharide on CD43 from normal lymphocytes.
2033371	2	97	dep	80	294:295	arg1	to					291:292	to	291:292	to	291:292	Since the 70 to 80 O-linked carbohydrate chains of CD43 are known to influence markedly its electrophoretic mobility, we analyzed the structure and the biosynthesis of O-glycans of CD43 in lymphocytes from patients with WAS.
2033371	4	98	theme	activation	771:780	arg1	antigens					782:789	Other activation antigens	765:789	Other activation antigens	765:789	Other activation antigens were absent from WAS lymphocytes.
2033371	3	99	dep	patients	625:632	arg1	out					607:609	out	607:609	out	607:609	Immunofluorescence analysis with the carbohydrate dependent anti-CD43 antibody T305 revealed that in 10 out of the 12 WAS patients tested increased numbers of T lymphocytes carry on CD43 an epitope which on normal lymphocytes is expressed only after activation.
2033371	10	100	theme	primary	2119:2125	arg1	defect					2127:2132	the primary defect	2115:2132	the primary defect in	2115:2135	The gene responsible for WAS has not yet been identified but the results presented in this study suggest that the primary defect in WAS may affect a gene which is involved in the regulation of O-glycosylation.
2033371	7	101	theme	normal	1366:1371	arg1	lymphocytes					1373:1383	normal lymphocytes	1366:1383	normal lymphocytes	1366:1383	WAS lymphocyte CD43 was found to carry predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH whereas normal lymphocytes carry the structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----6) GalNAcOH.
2033371	2	102	from	patients	484:491	arg1	lymphocytes					467:477	lymphocytes	467:477	lymphocytes from patients with WAS	467:500	Since the 70 to 80 O-linked carbohydrate chains of CD43 are known to influence markedly its electrophoretic mobility, we analyzed the structure and the biosynthesis of O-glycans of CD43 in lymphocytes from patients with WAS.
2033371	2	102	from	patients	484:491	arg1	structure					412:420	structure	412:420	structure	412:420	Since the 70 to 80 O-linked carbohydrate chains of CD43 are known to influence markedly its electrophoretic mobility, we analyzed the structure and the biosynthesis of O-glycans of CD43 in lymphocytes from patients with WAS.
2033371	2	102	from	patients	484:491	arg1	biosynthesis					430:441	the biosynthesis	426:441	the biosynthesis	426:441	Since the 70 to 80 O-linked carbohydrate chains of CD43 are known to influence markedly its electrophoretic mobility, we analyzed the structure and the biosynthesis of O-glycans of CD43 in lymphocytes from patients with WAS.
2033371	1	103	theme	T	241:241	arg1	CD43					272:275	the major T lymphocyte sialoglycoprotein CD43	231:275	the major T lymphocyte sialoglycoprotein CD43	231:275	The only molecular defect reported for the X-linked immunodeficiency Wiskott-Aldrich syndrome (WAS) is the abnormal electrophoretic behavior of the major T lymphocyte sialoglycoprotein CD43.
2033371	5	104	theme	Western	825:831	arg1	blots					833:837	Western blots	825:837	Western blots of WAS cell lysates	825:857	Western blots of WAS cell lysates displayed a high molecular mass form of CD43 which reacted with the T305 antibody and which could be found on in vivo activated lymphocytes but was absent from normal unstimulated lymphocytes.
2033371	1	105	theme	only	91:94	arg1	behavior					219:226	the abnormal electrophoretic behavior	190:226	the abnormal electrophoretic behavior of the major T lymphocyte sialoglycoprotein CD43	190:275	The only molecular defect reported for the X-linked immunodeficiency Wiskott-Aldrich syndrome (WAS) is the abnormal electrophoretic behavior of the major T lymphocyte sialoglycoprotein CD43.
2033371	1	105	theme	only	91:94	arg1	defect					106:111	The only molecular defect	87:111	The only molecular defect reported for the X-linked immunodeficiency Wiskott-Aldrich syndrome (WAS)	87:185	The only molecular defect reported for the X-linked immunodeficiency Wiskott-Aldrich syndrome (WAS) is the abnormal electrophoretic behavior of the major T lymphocyte sialoglycoprotein CD43.
2033371	8	106	theme	1----4GlcNAc	1558:1569	arg1	beta					1571:1574	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	1530:1581	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	1530:1581	Only after activation NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH becomes the principal oligosaccharide on CD43 from normal lymphocytes.
2033371	8	106	theme	1----4GlcNAc	1558:1569	arg1	beta					1517:1520	activation NeuNAc alpha 2----3Gal beta 1----3	1483:1527	activation NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6)	1483:1582	Only after activation NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH becomes the principal oligosaccharide on CD43 from normal lymphocytes.
2033371	6	107	theme	O-glycan	1067:1074	arg1	structures					1076:1085	the O-glycan structures	1063:1085	the O-glycan structures	1063:1085	To examine the O-glycan structures, carbohydrate labeled CD43 was immunoprecipitated and the released oligosaccharides identified.
2033371	7	108	theme	lymphocyte	1187:1196	arg1	CD43					1198:1201	WAS lymphocyte CD43	1183:1201	WAS lymphocyte CD43	1183:1201	WAS lymphocyte CD43 was found to carry predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH whereas normal lymphocytes carry the structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----6) GalNAcOH.
2033371	5	109	located	found	960:964	arg1	lymphocytes					987:997	in vivo activated lymphocytes	969:997	in vivo activated lymphocytes	969:997	Western blots of WAS cell lysates displayed a high molecular mass form of CD43 which reacted with the T305 antibody and which could be found on in vivo activated lymphocytes but was absent from normal unstimulated lymphocytes.
2033371	5	109	located	found	960:964	arg2	which					945:949	which	945:949	which	945:949	Western blots of WAS cell lysates displayed a high molecular mass form of CD43 which reacted with the T305 antibody and which could be found on in vivo activated lymphocytes but was absent from normal unstimulated lymphocytes.
2033371	9	110	theme	NeuNAc	1897:1902	arg1	beta					1974:1977	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	1933:1984	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	1933:1984	Analyzing the six glycosyltransferases involved in the biosynthesis of these O-glycan structures it was found that in WAS lymphocytes high levels of beta 1----6 N-acetyl-glucosaminyl transferase are responsible for the expression of NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH on CD43.
2033371	9	110	theme	NeuNAc	1897:1902	arg1	beta					1920:1923	NeuNAc alpha 2----3Gal beta 1----3	1897:1930	NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH on CD43	1897:2002	Analyzing the six glycosyltransferases involved in the biosynthesis of these O-glycan structures it was found that in WAS lymphocytes high levels of beta 1----6 N-acetyl-glucosaminyl transferase are responsible for the expression of NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH on CD43.
2033371	8	111	theme	principal	1605:1613	arg1	oligosaccharide					1615:1629	the principal oligosaccharide	1601:1629	the principal oligosaccharide on CD43 from normal lymphocytes	1601:1661	Only after activation NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH becomes the principal oligosaccharide on CD43 from normal lymphocytes.
2033371	3	112	theme	T	662:662	arg1	lymphocytes					664:674	T lymphocytes	662:674	T lymphocytes	662:674	Immunofluorescence analysis with the carbohydrate dependent anti-CD43 antibody T305 revealed that in 10 out of the 12 WAS patients tested increased numbers of T lymphocytes carry on CD43 an epitope which on normal lymphocytes is expressed only after activation.
2033371	7	113	theme	1----4G1cNAc	1323:1334	arg1	beta					1336:1339	NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6	1295:1346	NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6	1295:1346	WAS lymphocyte CD43 was found to carry predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH whereas normal lymphocytes carry the structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----6) GalNAcOH.
2033371	7	113	theme	1----4G1cNAc	1323:1334	arg1	beta					1282:1285	alpha 2----3Gal beta 1----3	1266:1292	predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH	1222:1356	WAS lymphocyte CD43 was found to carry predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH whereas normal lymphocytes carry the structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----6) GalNAcOH.
2033371	9	114	theme	2----3Gal	1910:1918	arg1	beta					1974:1977	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	1933:1984	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	1933:1984	Analyzing the six glycosyltransferases involved in the biosynthesis of these O-glycan structures it was found that in WAS lymphocytes high levels of beta 1----6 N-acetyl-glucosaminyl transferase are responsible for the expression of NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH on CD43.
2033371	9	114	theme	2----3Gal	1910:1918	arg1	beta					1920:1923	NeuNAc alpha 2----3Gal beta 1----3	1897:1930	NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH on CD43	1897:2002	Analyzing the six glycosyltransferases involved in the biosynthesis of these O-glycan structures it was found that in WAS lymphocytes high levels of beta 1----6 N-acetyl-glucosaminyl transferase are responsible for the expression of NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH on CD43.
2033371	2	115	dep	structure	412:420	arg1	the					408:410	the	408:410	the	408:410	Since the 70 to 80 O-linked carbohydrate chains of CD43 are known to influence markedly its electrophoretic mobility, we analyzed the structure and the biosynthesis of O-glycans of CD43 in lymphocytes from patients with WAS.
2033371	7	116	contain	carry	1216:1220	arg1	CD43					1198:1201	WAS lymphocyte CD43	1183:1201	WAS lymphocyte CD43	1183:1201	WAS lymphocyte CD43 was found to carry predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH whereas normal lymphocytes carry the structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----6) GalNAcOH.
2033371	7	116	contain	carry	1216:1220	arg2	GalNAcOH					1349:1356	predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH	1222:1356	predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH	1222:1356	WAS lymphocyte CD43 was found to carry predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH whereas normal lymphocytes carry the structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----6) GalNAcOH.
2033371	5	117	theme	normal	1019:1024	arg1	lymphocytes					1039:1049	normal unstimulated lymphocytes	1019:1049	normal unstimulated lymphocytes	1019:1049	Western blots of WAS cell lysates displayed a high molecular mass form of CD43 which reacted with the T305 antibody and which could be found on in vivo activated lymphocytes but was absent from normal unstimulated lymphocytes.
2033371	6	118	theme	released	1145:1152	arg1	oligosaccharides					1154:1169	the released oligosaccharides	1141:1169	the released oligosaccharides	1141:1169	To examine the O-glycan structures, carbohydrate labeled CD43 was immunoprecipitated and the released oligosaccharides identified.
2033371	3	119	theme	Immunofluorescence	503:520	arg1	analysis					522:529	Immunofluorescence analysis	503:529	Immunofluorescence analysis with the carbohydrate dependent anti-CD43 antibody T305	503:585	Immunofluorescence analysis with the carbohydrate dependent anti-CD43 antibody T305 revealed that in 10 out of the 12 WAS patients tested increased numbers of T lymphocytes carry on CD43 an epitope which on normal lymphocytes is expressed only after activation.
2033371	5	120	theme	activated	977:985	arg1	lymphocytes					987:997	in vivo activated lymphocytes	969:997	in vivo activated lymphocytes	969:997	Western blots of WAS cell lysates displayed a high molecular mass form of CD43 which reacted with the T305 antibody and which could be found on in vivo activated lymphocytes but was absent from normal unstimulated lymphocytes.
2033371	7	121	theme	NeuNAc	1295:1300	arg1	beta					1336:1339	NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6	1295:1346	NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6	1295:1346	WAS lymphocyte CD43 was found to carry predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH whereas normal lymphocytes carry the structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----6) GalNAcOH.
2033371	7	121	theme	NeuNAc	1295:1300	arg1	beta					1282:1285	alpha 2----3Gal beta 1----3	1266:1292	predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH	1222:1356	WAS lymphocyte CD43 was found to carry predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH whereas normal lymphocytes carry the structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----6) GalNAcOH.
2033371	9	122	theme	NeuNAc	1933:1938	arg1	beta					1920:1923	NeuNAc alpha 2----3Gal beta 1----3	1897:1930	NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH on CD43	1897:2002	Analyzing the six glycosyltransferases involved in the biosynthesis of these O-glycan structures it was found that in WAS lymphocytes high levels of beta 1----6 N-acetyl-glucosaminyl transferase are responsible for the expression of NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH on CD43.
2033371	9	122	theme	NeuNAc	1933:1938	arg1	beta					1974:1977	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	1933:1984	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	1933:1984	Analyzing the six glycosyltransferases involved in the biosynthesis of these O-glycan structures it was found that in WAS lymphocytes high levels of beta 1----6 N-acetyl-glucosaminyl transferase are responsible for the expression of NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH on CD43.
2033371	2	123	theme	electrophoretic	370:384	arg1	mobility					386:393	its electrophoretic mobility	366:393	its electrophoretic mobility	366:393	Since the 70 to 80 O-linked carbohydrate chains of CD43 are known to influence markedly its electrophoretic mobility, we analyzed the structure and the biosynthesis of O-glycans of CD43 in lymphocytes from patients with WAS.
2033371	7	124	contain	carry	1385:1389	arg2	GalNAcOH					1462:1469	the structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----6) GalNAcOH	1391:1469	the structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----6) GalNAcOH	1391:1469	WAS lymphocyte CD43 was found to carry predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH whereas normal lymphocytes carry the structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----6) GalNAcOH.
2033371	7	124	contain	carry	1385:1389	arg1	lymphocytes					1373:1383	normal lymphocytes	1366:1383	normal lymphocytes	1366:1383	WAS lymphocyte CD43 was found to carry predominantly the branched structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4G1cNAc beta 1----6) GalNAcOH whereas normal lymphocytes carry the structure NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----6) GalNAcOH.
2033371	2	125	from	structure	412:420	arg1	lymphocytes					467:477	lymphocytes	467:477	lymphocytes from patients with WAS	467:500	Since the 70 to 80 O-linked carbohydrate chains of CD43 are known to influence markedly its electrophoretic mobility, we analyzed the structure and the biosynthesis of O-glycans of CD43 in lymphocytes from patients with WAS.
2033371	2	125	from	structure	412:420	arg1	patients					484:491	patients	484:491	patients with WAS	484:500	Since the 70 to 80 O-linked carbohydrate chains of CD43 are known to influence markedly its electrophoretic mobility, we analyzed the structure and the biosynthesis of O-glycans of CD43 in lymphocytes from patients with WAS.
2033371	9	126	theme	2----3Gal	1946:1954	arg1	beta					1920:1923	NeuNAc alpha 2----3Gal beta 1----3	1897:1930	NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH on CD43	1897:2002	Analyzing the six glycosyltransferases involved in the biosynthesis of these O-glycan structures it was found that in WAS lymphocytes high levels of beta 1----6 N-acetyl-glucosaminyl transferase are responsible for the expression of NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH on CD43.
2033371	9	126	theme	2----3Gal	1946:1954	arg1	beta					1974:1977	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	1933:1984	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	1933:1984	Analyzing the six glycosyltransferases involved in the biosynthesis of these O-glycan structures it was found that in WAS lymphocytes high levels of beta 1----6 N-acetyl-glucosaminyl transferase are responsible for the expression of NeuNAc alpha 2----3Gal beta 1----3 (NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6) GalNAcOH on CD43.
2033371	3	127	theme	carbohydrate	540:551	arg1	antibody					573:580	the carbohydrate dependent anti-CD43 antibody T305	536:585	the carbohydrate dependent anti-CD43 antibody T305	536:585	Immunofluorescence analysis with the carbohydrate dependent anti-CD43 antibody T305 revealed that in 10 out of the 12 WAS patients tested increased numbers of T lymphocytes carry on CD43 an epitope which on normal lymphocytes is expressed only after activation.
2033371	1	128	theme	sialoglycoprotein	254:270	arg1	CD43					272:275	the major T lymphocyte sialoglycoprotein CD43	231:275	the major T lymphocyte sialoglycoprotein CD43	231:275	The only molecular defect reported for the X-linked immunodeficiency Wiskott-Aldrich syndrome (WAS) is the abnormal electrophoretic behavior of the major T lymphocyte sialoglycoprotein CD43.
8702529	1	0	theme	mucin-like	158:167	arg1	ligand-1					106:113	P-selectin glycoprotein ligand-1	82:113	P-selectin glycoprotein ligand-1 (PSGL-1)	82:122	P-selectin glycoprotein ligand-1 (PSGL-1) is a disulfide-bonded homodimeric mucin-like glycoprotein on leukocytes that interacts with both P- and E-selectin.
8702529	1	0	theme	mucin-like	158:167	arg1	glycoprotein					169:180	a disulfide-bonded homodimeric mucin-like glycoprotein	127:180	a disulfide-bonded homodimeric mucin-like glycoprotein on leukocytes that interacts with both P- and E-selectin	127:237	P-selectin glycoprotein ligand-1 (PSGL-1) is a disulfide-bonded homodimeric mucin-like glycoprotein on leukocytes that interacts with both P- and E-selectin.
8702529	6	1	theme	major	1026:1030	arg1	species					1032:1038	two major species	1022:1038	two major species containing the sialyl Lewis x antigen	1022:1076	A minority of the O-glycans are alpha-1,3-fucosylated that occur as two major species containing the sialyl Lewis x antigen; one species is a disialylated, monofucosylated glycan, and the other is a monosialylated, trifucosylated glycan having a polylactosamine backbone.
8702529	3	2	from	O-glycans	428:436	arg1	leukosialin					447:457	leukosialin	447:457	leukosialin	447:457	In control studies, the O-glycans on CD43 (leukosialin), a mucin-like glycoprotein also expressed by HL-60 cells, were analyzed and compared to those of PSGL-1.
8702529	3	2	from	O-glycans	428:436	arg1	CD43					441:444	CD43	441:444	CD43 (leukosialin)	441:458	In control studies, the O-glycans on CD43 (leukosialin), a mucin-like glycoprotein also expressed by HL-60 cells, were analyzed and compared to those of PSGL-1.
8702529	3	2	from	O-glycans	428:436	arg1	glycoprotein					474:485	a mucin-like glycoprotein	461:485	a mucin-like glycoprotein also expressed by HL-60 cells	461:515	In control studies, the O-glycans on CD43 (leukosialin), a mucin-like glycoprotein also expressed by HL-60 cells, were analyzed and compared to those of PSGL-1.
8702529	2	3	theme	radiolabeled	365:376	arg1	cells					345:349	HL-60 cells	339:349	HL-60 cells metabolically radiolabeled	339:376	In this report we describe the structures of the Ser/Thr-linked O-glycans of PSGL-1 synthesized by HL-60 cells metabolically radiolabeled with 3H-sugar precursors.
8702529	6	4	dep	monosialylated	1153:1166	arg1	trifucosylated					1169:1182	trifucosylated	1169:1182	trifucosylated	1169:1182	A minority of the O-glycans are alpha-1,3-fucosylated that occur as two major species containing the sialyl Lewis x antigen; one species is a disialylated, monofucosylated glycan, and the other is a monosialylated, trifucosylated glycan having a polylactosamine backbone.
8702529	1	5	gly	glycoprotein	93:104	arg1	glycoprotein					93:104	P-selectin glycoprotein ligand-1	82:113	P-selectin glycoprotein ligand-1 (PSGL-1)	82:122	P-selectin glycoprotein ligand-1 (PSGL-1) is a disulfide-bonded homodimeric mucin-like glycoprotein on leukocytes that interacts with both P- and E-selectin.
8702529	0	6	from	Structures	0:9	arg1	ligand-1					55:62	P-selectin glycoprotein ligand-1	31:62	P-selectin glycoprotein ligand-1 from HL-60 cells	31:79	Structures of the O-glycans on P-selectin glycoprotein ligand-1 from HL-60 cells.
8702529	6	7	gly	disialylated	1096:1107	arg1	species					1083:1089	one species	1079:1089	one species	1079:1089	A minority of the O-glycans are alpha-1,3-fucosylated that occur as two major species containing the sialyl Lewis x antigen; one species is a disialylated, monofucosylated glycan, and the other is a monosialylated, trifucosylated glycan having a polylactosamine backbone.
8702529	6	7	gly	disialylated	1096:1107	arg1	glycan					1126:1131	a disialylated, monofucosylated glycan	1094:1131	a disialylated, monofucosylated glycan	1094:1131	A minority of the O-glycans are alpha-1,3-fucosylated that occur as two major species containing the sialyl Lewis x antigen; one species is a disialylated, monofucosylated glycan, and the other is a monosialylated, trifucosylated glycan having a polylactosamine backbone.
8702529	1	8	from	glycoprotein	169:180	arg1	leukocytes					185:194	leukocytes	185:194	leukocytes	185:194	P-selectin glycoprotein ligand-1 (PSGL-1) is a disulfide-bonded homodimeric mucin-like glycoprotein on leukocytes that interacts with both P- and E-selectin.
8702529	2	9	theme	Ser/Thr-linked	289:302	arg1	O-glycans					304:312	the Ser/Thr-linked O-glycans	285:312	the Ser/Thr-linked O-glycans of PSGL-1 synthesized by HL-60 cells metabolically radiolabeled with 3H-sugar precursors	285:401	In this report we describe the structures of the Ser/Thr-linked O-glycans of PSGL-1 synthesized by HL-60 cells metabolically radiolabeled with 3H-sugar precursors.
8702529	4	10	theme	Ser/Thr	594:600	arg1	residues					602:609	Ser/Thr residues	594:609	Ser/Thr residues	594:609	O-Glycans were released from Ser/Thr residues by mild base/borohydride treatment of purified glycoproteins, and glycan structures were determined by a combination of techniques.
8702529	7	11	located	found	1261:1265	arg1	PSGL-1					1270:1275	PSGL-1	1270:1275	PSGL-1	1270:1275	CD43 lacks the fucosylated glycans found on PSGL-1 and is enriched for the nonfucosylated, disialylated core-2 hexasaccharide.
8702529	7	11	located	found	1261:1265	arg2	glycans					1253:1259	the fucosylated glycans	1237:1259	the fucosylated glycans found on PSGL-1	1237:1275	CD43 lacks the fucosylated glycans found on PSGL-1 and is enriched for the nonfucosylated, disialylated core-2 hexasaccharide.
8702529	0	12	from	ligand-1	55:62	arg1	Structures					0:9	Structures	0:9	Structures of the O-glycans on P-selectin glycoprotein ligand-1 from HL-60 cells	0:79	Structures of the O-glycans on P-selectin glycoprotein ligand-1 from HL-60 cells.
8702529	7	13	gly	nonfucosylated	1301:1314	arg1	hexasaccharide					1337:1350	the nonfucosylated, disialylated core-2 hexasaccharide	1297:1350	the nonfucosylated, disialylated core-2 hexasaccharide	1297:1350	CD43 lacks the fucosylated glycans found on PSGL-1 and is enriched for the nonfucosylated, disialylated core-2 hexasaccharide.
8702529	6	14	contain	containing	1040:1049	arg1	species					1032:1038	two major species	1022:1038	two major species containing the sialyl Lewis x antigen	1022:1076	A minority of the O-glycans are alpha-1,3-fucosylated that occur as two major species containing the sialyl Lewis x antigen; one species is a disialylated, monofucosylated glycan, and the other is a monosialylated, trifucosylated glycan having a polylactosamine backbone.
8702529	6	14	contain	containing	1040:1049	arg2	antigen					1070:1076	the sialyl Lewis x antigen	1051:1076	the sialyl Lewis x antigen	1051:1076	A minority of the O-glycans are alpha-1,3-fucosylated that occur as two major species containing the sialyl Lewis x antigen; one species is a disialylated, monofucosylated glycan, and the other is a monosialylated, trifucosylated glycan having a polylactosamine backbone.
8702529	4	15	theme	techniques	731:740	arg1	combination					716:726	a combination	714:726	a combination of techniques	714:740	O-Glycans were released from Ser/Thr residues by mild base/borohydride treatment of purified glycoproteins, and glycan structures were determined by a combination of techniques.
8702529	5	16	gly	disialylated	839:850	arg1	GalNAcOH++					940:949	the core-2 tetrasaccharide Galbeta1-->4GlcNAcbeta1-->6(Galbeta1-->3)GalNAcOH++	872:949	the core-2 tetrasaccharide Galbeta1-->4GlcNAcbeta1-->6(Galbeta1-->3)GalNAcOH++	872:949	In contrast to expectations, PSGL-1 is not heavily fucosylated; a majority of the O-glycans are disialylated or neutral forms of the core-2 tetrasaccharide Galbeta1-->4GlcNAcbeta1-->6(Galbeta1-->3)GalNAcOH++ +.
8702529	5	16	gly	disialylated	839:850	arg1	majority					809:816	a majority	807:816	a majority of the O-glycans	807:833	In contrast to expectations, PSGL-1 is not heavily fucosylated; a majority of the O-glycans are disialylated or neutral forms of the core-2 tetrasaccharide Galbeta1-->4GlcNAcbeta1-->6(Galbeta1-->3)GalNAcOH++ +.
8702529	5	16	gly	disialylated	839:850	arg1	forms					863:867	disialylated or neutral forms	839:867	disialylated or neutral forms	839:867	In contrast to expectations, PSGL-1 is not heavily fucosylated; a majority of the O-glycans are disialylated or neutral forms of the core-2 tetrasaccharide Galbeta1-->4GlcNAcbeta1-->6(Galbeta1-->3)GalNAcOH++ +.
8702529	5	17	theme	disialylated	839:850	arg1	majority					809:816	a majority	807:816	a majority of the O-glycans	807:833	In contrast to expectations, PSGL-1 is not heavily fucosylated; a majority of the O-glycans are disialylated or neutral forms of the core-2 tetrasaccharide Galbeta1-->4GlcNAcbeta1-->6(Galbeta1-->3)GalNAcOH++ +.
8702529	5	17	theme	disialylated	839:850	arg1	forms					863:867	disialylated or neutral forms	839:867	disialylated or neutral forms	839:867	In contrast to expectations, PSGL-1 is not heavily fucosylated; a majority of the O-glycans are disialylated or neutral forms of the core-2 tetrasaccharide Galbeta1-->4GlcNAcbeta1-->6(Galbeta1-->3)GalNAcOH++ +.
8702529	5	18	theme	Galbeta1-->3	927:938	arg1	GalNAcOH++					940:949	the core-2 tetrasaccharide Galbeta1-->4GlcNAcbeta1-->6(Galbeta1-->3)GalNAcOH++	872:949	the core-2 tetrasaccharide Galbeta1-->4GlcNAcbeta1-->6(Galbeta1-->3)GalNAcOH++	872:949	In contrast to expectations, PSGL-1 is not heavily fucosylated; a majority of the O-glycans are disialylated or neutral forms of the core-2 tetrasaccharide Galbeta1-->4GlcNAcbeta1-->6(Galbeta1-->3)GalNAcOH++ +.
8702529	8	19	contain	contains	1391:1398	arg1	PSGL-1					1384:1389	PSGL-1	1384:1389	PSGL-1	1384:1389	These results demonstrate that PSGL-1 contains unique fucosylated O-glycans that are predicted to be critical for high affinity interactions between PSGL-1 and selectins.
8702529	8	19	contain	contains	1391:1398	arg2	O-glycans					1419:1427	unique fucosylated O-glycans	1400:1427	unique fucosylated O-glycans that are predicted to be critical for high affinity interactions between PSGL-1 and selectins	1400:1521	These results demonstrate that PSGL-1 contains unique fucosylated O-glycans that are predicted to be critical for high affinity interactions between PSGL-1 and selectins.
8702529	6	20	gly	alpha-1,3-fucosylated	986:1006	arg1	alpha-1,3-fucosylated					986:1006	alpha-1,3-fucosylated	986:1006	alpha-1,3-fucosylated	986:1006	A minority of the O-glycans are alpha-1,3-fucosylated that occur as two major species containing the sialyl Lewis x antigen; one species is a disialylated, monofucosylated glycan, and the other is a monosialylated, trifucosylated glycan having a polylactosamine backbone.
8702529	6	20	gly	alpha-1,3-fucosylated	986:1006	arg1	minority					956:963	A minority	954:963	A minority of the O-glycans	954:980	A minority of the O-glycans are alpha-1,3-fucosylated that occur as two major species containing the sialyl Lewis x antigen; one species is a disialylated, monofucosylated glycan, and the other is a monosialylated, trifucosylated glycan having a polylactosamine backbone.
8702529	6	21	theme	disialylated	1096:1107	arg1	species					1083:1089	one species	1079:1089	one species	1079:1089	A minority of the O-glycans are alpha-1,3-fucosylated that occur as two major species containing the sialyl Lewis x antigen; one species is a disialylated, monofucosylated glycan, and the other is a monosialylated, trifucosylated glycan having a polylactosamine backbone.
8702529	6	21	theme	disialylated	1096:1107	arg1	glycan					1126:1131	a disialylated, monofucosylated glycan	1094:1131	a disialylated, monofucosylated glycan	1094:1131	A minority of the O-glycans are alpha-1,3-fucosylated that occur as two major species containing the sialyl Lewis x antigen; one species is a disialylated, monofucosylated glycan, and the other is a monosialylated, trifucosylated glycan having a polylactosamine backbone.
8702529	3	22	theme	control	407:413	arg1	studies					415:421	control studies	407:421	control studies	407:421	In control studies, the O-glycans on CD43 (leukosialin), a mucin-like glycoprotein also expressed by HL-60 cells, were analyzed and compared to those of PSGL-1.
8702529	6	23	theme	O-glycans	972:980	arg1	alpha-1,3-fucosylated					986:1006	alpha-1,3-fucosylated	986:1006	alpha-1,3-fucosylated	986:1006	A minority of the O-glycans are alpha-1,3-fucosylated that occur as two major species containing the sialyl Lewis x antigen; one species is a disialylated, monofucosylated glycan, and the other is a monosialylated, trifucosylated glycan having a polylactosamine backbone.
8702529	6	23	theme	O-glycans	972:980	arg1	minority					956:963	A minority	954:963	A minority of the O-glycans	954:980	A minority of the O-glycans are alpha-1,3-fucosylated that occur as two major species containing the sialyl Lewis x antigen; one species is a disialylated, monofucosylated glycan, and the other is a monosialylated, trifucosylated glycan having a polylactosamine backbone.
8702529	7	24	theme	core-2	1330:1335	arg1	hexasaccharide					1337:1350	the nonfucosylated, disialylated core-2 hexasaccharide	1297:1350	the nonfucosylated, disialylated core-2 hexasaccharide	1297:1350	CD43 lacks the fucosylated glycans found on PSGL-1 and is enriched for the nonfucosylated, disialylated core-2 hexasaccharide.
8702529	7	25	theme	fucosylated	1241:1251	arg1	glycans					1253:1259	the fucosylated glycans	1237:1259	the fucosylated glycans found on PSGL-1	1237:1275	CD43 lacks the fucosylated glycans found on PSGL-1 and is enriched for the nonfucosylated, disialylated core-2 hexasaccharide.
8702529	1	26	theme	P-selectin	82:91	arg1	PSGL-1					116:121	PSGL-1	116:121	PSGL-1	116:121	P-selectin glycoprotein ligand-1 (PSGL-1) is a disulfide-bonded homodimeric mucin-like glycoprotein on leukocytes that interacts with both P- and E-selectin.
8702529	1	26	theme	P-selectin	82:91	arg1	ligand-1					106:113	P-selectin glycoprotein ligand-1	82:113	P-selectin glycoprotein ligand-1 (PSGL-1)	82:122	P-selectin glycoprotein ligand-1 (PSGL-1) is a disulfide-bonded homodimeric mucin-like glycoprotein on leukocytes that interacts with both P- and E-selectin.
8702529	1	26	theme	P-selectin	82:91	arg1	glycoprotein					169:180	a disulfide-bonded homodimeric mucin-like glycoprotein	127:180	a disulfide-bonded homodimeric mucin-like glycoprotein on leukocytes that interacts with both P- and E-selectin	127:237	P-selectin glycoprotein ligand-1 (PSGL-1) is a disulfide-bonded homodimeric mucin-like glycoprotein on leukocytes that interacts with both P- and E-selectin.
8702529	4	27	gly	glycoproteins	658:670	arg1	glycoproteins					658:670	purified glycoproteins	649:670	purified glycoproteins	649:670	O-Glycans were released from Ser/Thr residues by mild base/borohydride treatment of purified glycoproteins, and glycan structures were determined by a combination of techniques.
8702529	6	28	theme	monosialylated	1153:1166	arg1	glycan					1184:1189	a monosialylated, trifucosylated glycan	1151:1189	a monosialylated, trifucosylated glycan having a polylactosamine backbone	1151:1223	A minority of the O-glycans are alpha-1,3-fucosylated that occur as two major species containing the sialyl Lewis x antigen; one species is a disialylated, monofucosylated glycan, and the other is a monosialylated, trifucosylated glycan having a polylactosamine backbone.
8702529	6	28	theme	monosialylated	1153:1166	arg1	other					1142:1146	other	1142:1146	other	1142:1146	A minority of the O-glycans are alpha-1,3-fucosylated that occur as two major species containing the sialyl Lewis x antigen; one species is a disialylated, monofucosylated glycan, and the other is a monosialylated, trifucosylated glycan having a polylactosamine backbone.
8702529	2	29	theme	PSGL-1	317:322	arg1	O-glycans					304:312	the Ser/Thr-linked O-glycans	285:312	the Ser/Thr-linked O-glycans of PSGL-1 synthesized by HL-60 cells metabolically radiolabeled with 3H-sugar precursors	285:401	In this report we describe the structures of the Ser/Thr-linked O-glycans of PSGL-1 synthesized by HL-60 cells metabolically radiolabeled with 3H-sugar precursors.
8702529	7	30	theme	nonfucosylated	1301:1314	arg1	hexasaccharide					1337:1350	the nonfucosylated, disialylated core-2 hexasaccharide	1297:1350	the nonfucosylated, disialylated core-2 hexasaccharide	1297:1350	CD43 lacks the fucosylated glycans found on PSGL-1 and is enriched for the nonfucosylated, disialylated core-2 hexasaccharide.
8702529	4	31	theme	glycan	677:682	arg1	structures					684:693	glycan structures	677:693	glycan structures	677:693	O-Glycans were released from Ser/Thr residues by mild base/borohydride treatment of purified glycoproteins, and glycan structures were determined by a combination of techniques.
8702529	0	32	theme	O-glycans	18:26	arg1	Structures					0:9	Structures	0:9	Structures of the O-glycans on P-selectin glycoprotein ligand-1 from HL-60 cells	0:79	Structures of the O-glycans on P-selectin glycoprotein ligand-1 from HL-60 cells.
8702529	8	33	theme	affinity	1472:1479	arg1	interactions					1481:1492	high affinity interactions	1467:1492	high affinity interactions between PSGL-1 and selectins	1467:1521	These results demonstrate that PSGL-1 contains unique fucosylated O-glycans that are predicted to be critical for high affinity interactions between PSGL-1 and selectins.
8702529	6	34	theme	x	1068:1068	arg1	antigen					1070:1076	the sialyl Lewis x antigen	1051:1076	the sialyl Lewis x antigen	1051:1076	A minority of the O-glycans are alpha-1,3-fucosylated that occur as two major species containing the sialyl Lewis x antigen; one species is a disialylated, monofucosylated glycan, and the other is a monosialylated, trifucosylated glycan having a polylactosamine backbone.
8702529	3	35	theme	mucin-like	463:472	arg1	CD43					441:444	CD43	441:444	CD43 (leukosialin)	441:458	In control studies, the O-glycans on CD43 (leukosialin), a mucin-like glycoprotein also expressed by HL-60 cells, were analyzed and compared to those of PSGL-1.
8702529	3	35	theme	mucin-like	463:472	arg1	glycoprotein					474:485	a mucin-like glycoprotein	461:485	a mucin-like glycoprotein also expressed by HL-60 cells	461:515	In control studies, the O-glycans on CD43 (leukosialin), a mucin-like glycoprotein also expressed by HL-60 cells, were analyzed and compared to those of PSGL-1.
8702529	1	36	theme	glycoprotein	93:104	arg1	PSGL-1					116:121	PSGL-1	116:121	PSGL-1	116:121	P-selectin glycoprotein ligand-1 (PSGL-1) is a disulfide-bonded homodimeric mucin-like glycoprotein on leukocytes that interacts with both P- and E-selectin.
8702529	1	36	theme	glycoprotein	93:104	arg1	ligand-1					106:113	P-selectin glycoprotein ligand-1	82:113	P-selectin glycoprotein ligand-1 (PSGL-1)	82:122	P-selectin glycoprotein ligand-1 (PSGL-1) is a disulfide-bonded homodimeric mucin-like glycoprotein on leukocytes that interacts with both P- and E-selectin.
8702529	1	36	theme	glycoprotein	93:104	arg1	glycoprotein					169:180	a disulfide-bonded homodimeric mucin-like glycoprotein	127:180	a disulfide-bonded homodimeric mucin-like glycoprotein on leukocytes that interacts with both P- and E-selectin	127:237	P-selectin glycoprotein ligand-1 (PSGL-1) is a disulfide-bonded homodimeric mucin-like glycoprotein on leukocytes that interacts with both P- and E-selectin.
8702529	2	37	link	Ser/Thr-linked	289:302	arg1	O-glycans					304:312	the Ser/Thr-linked O-glycans	285:312	the Ser/Thr-linked O-glycans of PSGL-1 synthesized by HL-60 cells metabolically radiolabeled with 3H-sugar precursors	285:401	In this report we describe the structures of the Ser/Thr-linked O-glycans of PSGL-1 synthesized by HL-60 cells metabolically radiolabeled with 3H-sugar precursors.
8702529	2	38	theme	O-glycans	304:312	arg1	structures					271:280	the structures	267:280	the structures of the Ser/Thr-linked O-glycans of PSGL-1 synthesized by HL-60 cells metabolically radiolabeled with 3H-sugar precursors	267:401	In this report we describe the structures of the Ser/Thr-linked O-glycans of PSGL-1 synthesized by HL-60 cells metabolically radiolabeled with 3H-sugar precursors.
8702529	8	39	theme	fucosylated	1407:1417	arg1	O-glycans					1419:1427	unique fucosylated O-glycans	1400:1427	unique fucosylated O-glycans that are predicted to be critical for high affinity interactions between PSGL-1 and selectins	1400:1521	These results demonstrate that PSGL-1 contains unique fucosylated O-glycans that are predicted to be critical for high affinity interactions between PSGL-1 and selectins.
8702529	5	40	theme	tetrasaccharide	883:897	arg1	GalNAcOH++					940:949	the core-2 tetrasaccharide Galbeta1-->4GlcNAcbeta1-->6(Galbeta1-->3)GalNAcOH++	872:949	the core-2 tetrasaccharide Galbeta1-->4GlcNAcbeta1-->6(Galbeta1-->3)GalNAcOH++	872:949	In contrast to expectations, PSGL-1 is not heavily fucosylated; a majority of the O-glycans are disialylated or neutral forms of the core-2 tetrasaccharide Galbeta1-->4GlcNAcbeta1-->6(Galbeta1-->3)GalNAcOH++ +.
8702529	0	41	theme	P-selectin	31:40	arg1	ligand-1					55:62	P-selectin glycoprotein ligand-1	31:62	P-selectin glycoprotein ligand-1 from HL-60 cells	31:79	Structures of the O-glycans on P-selectin glycoprotein ligand-1 from HL-60 cells.
8702529	5	42	theme	GalNAcOH++	940:949	arg1	majority					809:816	a majority	807:816	a majority of the O-glycans	807:833	In contrast to expectations, PSGL-1 is not heavily fucosylated; a majority of the O-glycans are disialylated or neutral forms of the core-2 tetrasaccharide Galbeta1-->4GlcNAcbeta1-->6(Galbeta1-->3)GalNAcOH++ +.
8702529	5	42	theme	GalNAcOH++	940:949	arg1	forms					863:867	disialylated or neutral forms	839:867	disialylated or neutral forms	839:867	In contrast to expectations, PSGL-1 is not heavily fucosylated; a majority of the O-glycans are disialylated or neutral forms of the core-2 tetrasaccharide Galbeta1-->4GlcNAcbeta1-->6(Galbeta1-->3)GalNAcOH++ +.
8702529	0	43	from	cells	75:79	arg1	ligand-1					55:62	P-selectin glycoprotein ligand-1	31:62	P-selectin glycoprotein ligand-1 from HL-60 cells	31:79	Structures of the O-glycans on P-selectin glycoprotein ligand-1 from HL-60 cells.
8702529	3	44	gly	glycoprotein	474:485	arg1	CD43					441:444	CD43	441:444	CD43 (leukosialin)	441:458	In control studies, the O-glycans on CD43 (leukosialin), a mucin-like glycoprotein also expressed by HL-60 cells, were analyzed and compared to those of PSGL-1.
8702529	3	44	gly	glycoprotein	474:485	arg1	glycoprotein					474:485	a mucin-like glycoprotein	461:485	a mucin-like glycoprotein also expressed by HL-60 cells	461:515	In control studies, the O-glycans on CD43 (leukosialin), a mucin-like glycoprotein also expressed by HL-60 cells, were analyzed and compared to those of PSGL-1.
8702529	5	45	theme	core-2	876:881	arg1	GalNAcOH++					940:949	the core-2 tetrasaccharide Galbeta1-->4GlcNAcbeta1-->6(Galbeta1-->3)GalNAcOH++	872:949	the core-2 tetrasaccharide Galbeta1-->4GlcNAcbeta1-->6(Galbeta1-->3)GalNAcOH++	872:949	In contrast to expectations, PSGL-1 is not heavily fucosylated; a majority of the O-glycans are disialylated or neutral forms of the core-2 tetrasaccharide Galbeta1-->4GlcNAcbeta1-->6(Galbeta1-->3)GalNAcOH++ +.
8702529	4	46	theme	glycoproteins	658:670	arg1	treatment					636:644	mild base/borohydride treatment	614:644	mild base/borohydride treatment of purified glycoproteins	614:670	O-Glycans were released from Ser/Thr residues by mild base/borohydride treatment of purified glycoproteins, and glycan structures were determined by a combination of techniques.
8702529	6	47	contain	having	1191:1196	arg1	glycan					1184:1189	a monosialylated, trifucosylated glycan	1151:1189	a monosialylated, trifucosylated glycan having a polylactosamine backbone	1151:1223	A minority of the O-glycans are alpha-1,3-fucosylated that occur as two major species containing the sialyl Lewis x antigen; one species is a disialylated, monofucosylated glycan, and the other is a monosialylated, trifucosylated glycan having a polylactosamine backbone.
8702529	6	47	contain	having	1191:1196	arg2	backbone					1216:1223	a polylactosamine backbone	1198:1223	a polylactosamine backbone	1198:1223	A minority of the O-glycans are alpha-1,3-fucosylated that occur as two major species containing the sialyl Lewis x antigen; one species is a disialylated, monofucosylated glycan, and the other is a monosialylated, trifucosylated glycan having a polylactosamine backbone.
8702529	6	47	contain	having	1191:1196	arg1	other					1142:1146	other	1142:1146	other	1142:1146	A minority of the O-glycans are alpha-1,3-fucosylated that occur as two major species containing the sialyl Lewis x antigen; one species is a disialylated, monofucosylated glycan, and the other is a monosialylated, trifucosylated glycan having a polylactosamine backbone.
8702529	5	48	theme	neutral	855:861	arg1	majority					809:816	a majority	807:816	a majority of the O-glycans	807:833	In contrast to expectations, PSGL-1 is not heavily fucosylated; a majority of the O-glycans are disialylated or neutral forms of the core-2 tetrasaccharide Galbeta1-->4GlcNAcbeta1-->6(Galbeta1-->3)GalNAcOH++ +.
8702529	5	48	theme	neutral	855:861	arg1	forms					863:867	disialylated or neutral forms	839:867	disialylated or neutral forms	839:867	In contrast to expectations, PSGL-1 is not heavily fucosylated; a majority of the O-glycans are disialylated or neutral forms of the core-2 tetrasaccharide Galbeta1-->4GlcNAcbeta1-->6(Galbeta1-->3)GalNAcOH++ +.
8702529	4	49	theme	purified	649:656	arg1	glycoproteins					658:670	purified glycoproteins	649:670	purified glycoproteins	649:670	O-Glycans were released from Ser/Thr residues by mild base/borohydride treatment of purified glycoproteins, and glycan structures were determined by a combination of techniques.
8702529	6	50	theme	one	1079:1081	arg1	species					1083:1089	one species	1079:1089	one species	1079:1089	A minority of the O-glycans are alpha-1,3-fucosylated that occur as two major species containing the sialyl Lewis x antigen; one species is a disialylated, monofucosylated glycan, and the other is a monosialylated, trifucosylated glycan having a polylactosamine backbone.
8702529	6	50	theme	one	1079:1081	arg1	glycan					1126:1131	a disialylated, monofucosylated glycan	1094:1131	a disialylated, monofucosylated glycan	1094:1131	A minority of the O-glycans are alpha-1,3-fucosylated that occur as two major species containing the sialyl Lewis x antigen; one species is a disialylated, monofucosylated glycan, and the other is a monosialylated, trifucosylated glycan having a polylactosamine backbone.
8702529	8	51	gly	fucosylated	1407:1417	arg1	O-glycans					1419:1427	unique fucosylated O-glycans	1400:1427	unique fucosylated O-glycans that are predicted to be critical for high affinity interactions between PSGL-1 and selectins	1400:1521	These results demonstrate that PSGL-1 contains unique fucosylated O-glycans that are predicted to be critical for high affinity interactions between PSGL-1 and selectins.
8702529	6	52	theme	Lewis	1062:1066	arg1	antigen					1070:1076	the sialyl Lewis x antigen	1051:1076	the sialyl Lewis x antigen	1051:1076	A minority of the O-glycans are alpha-1,3-fucosylated that occur as two major species containing the sialyl Lewis x antigen; one species is a disialylated, monofucosylated glycan, and the other is a monosialylated, trifucosylated glycan having a polylactosamine backbone.
8702529	8	53	theme	unique	1400:1405	arg1	O-glycans					1419:1427	unique fucosylated O-glycans	1400:1427	unique fucosylated O-glycans that are predicted to be critical for high affinity interactions between PSGL-1 and selectins	1400:1521	These results demonstrate that PSGL-1 contains unique fucosylated O-glycans that are predicted to be critical for high affinity interactions between PSGL-1 and selectins.
8702529	0	54	theme	glycoprotein	42:53	arg1	ligand-1					55:62	P-selectin glycoprotein ligand-1	31:62	P-selectin glycoprotein ligand-1 from HL-60 cells	31:79	Structures of the O-glycans on P-selectin glycoprotein ligand-1 from HL-60 cells.
8702529	5	55	dep	expectations	758:769	arg1	contrast					746:753	contrast	746:753	contrast	746:753	In contrast to expectations, PSGL-1 is not heavily fucosylated; a majority of the O-glycans are disialylated or neutral forms of the core-2 tetrasaccharide Galbeta1-->4GlcNAcbeta1-->6(Galbeta1-->3)GalNAcOH++ +.
8702529	8	56	theme	high	1467:1470	arg1	interactions					1481:1492	high affinity interactions	1467:1492	high affinity interactions between PSGL-1 and selectins	1467:1521	These results demonstrate that PSGL-1 contains unique fucosylated O-glycans that are predicted to be critical for high affinity interactions between PSGL-1 and selectins.
8702529	3	57	theme	HL-60	505:509	arg1	cells					511:515	HL-60 cells	505:515	HL-60 cells	505:515	In control studies, the O-glycans on CD43 (leukosialin), a mucin-like glycoprotein also expressed by HL-60 cells, were analyzed and compared to those of PSGL-1.
8702529	6	58	theme	polylactosamine	1200:1214	arg1	backbone					1216:1223	a polylactosamine backbone	1198:1223	a polylactosamine backbone	1198:1223	A minority of the O-glycans are alpha-1,3-fucosylated that occur as two major species containing the sialyl Lewis x antigen; one species is a disialylated, monofucosylated glycan, and the other is a monosialylated, trifucosylated glycan having a polylactosamine backbone.
8702529	1	59	gly	glycoprotein	169:180	arg1	ligand-1					106:113	P-selectin glycoprotein ligand-1	82:113	P-selectin glycoprotein ligand-1 (PSGL-1)	82:122	P-selectin glycoprotein ligand-1 (PSGL-1) is a disulfide-bonded homodimeric mucin-like glycoprotein on leukocytes that interacts with both P- and E-selectin.
8702529	1	59	gly	glycoprotein	169:180	arg1	glycoprotein					169:180	a disulfide-bonded homodimeric mucin-like glycoprotein	127:180	a disulfide-bonded homodimeric mucin-like glycoprotein on leukocytes that interacts with both P- and E-selectin	127:237	P-selectin glycoprotein ligand-1 (PSGL-1) is a disulfide-bonded homodimeric mucin-like glycoprotein on leukocytes that interacts with both P- and E-selectin.
8702529	7	60	dep	nonfucosylated	1301:1314	arg1	disialylated					1317:1328	disialylated	1317:1328	disialylated	1317:1328	CD43 lacks the fucosylated glycans found on PSGL-1 and is enriched for the nonfucosylated, disialylated core-2 hexasaccharide.
8702529	5	61	gly	fucosylated	794:804	arg1	PSGL-1					772:777	PSGL-1	772:777	PSGL-1	772:777	In contrast to expectations, PSGL-1 is not heavily fucosylated; a majority of the O-glycans are disialylated or neutral forms of the core-2 tetrasaccharide Galbeta1-->4GlcNAcbeta1-->6(Galbeta1-->3)GalNAcOH++ +.
8702529	6	62	dep	disialylated	1096:1107	arg1	monofucosylated					1110:1124	monofucosylated	1110:1124	monofucosylated	1110:1124	A minority of the O-glycans are alpha-1,3-fucosylated that occur as two major species containing the sialyl Lewis x antigen; one species is a disialylated, monofucosylated glycan, and the other is a monosialylated, trifucosylated glycan having a polylactosamine backbone.
8702529	2	63	theme	HL-60	339:343	arg1	cells					345:349	HL-60 cells	339:349	HL-60 cells metabolically radiolabeled	339:376	In this report we describe the structures of the Ser/Thr-linked O-glycans of PSGL-1 synthesized by HL-60 cells metabolically radiolabeled with 3H-sugar precursors.
8702529	6	64	theme	sialyl	1055:1060	arg1	antigen					1070:1076	the sialyl Lewis x antigen	1051:1076	the sialyl Lewis x antigen	1051:1076	A minority of the O-glycans are alpha-1,3-fucosylated that occur as two major species containing the sialyl Lewis x antigen; one species is a disialylated, monofucosylated glycan, and the other is a monosialylated, trifucosylated glycan having a polylactosamine backbone.
8702529	6	65	gly	monosialylated	1153:1166	arg1	glycan					1184:1189	a monosialylated, trifucosylated glycan	1151:1189	a monosialylated, trifucosylated glycan having a polylactosamine backbone	1151:1223	A minority of the O-glycans are alpha-1,3-fucosylated that occur as two major species containing the sialyl Lewis x antigen; one species is a disialylated, monofucosylated glycan, and the other is a monosialylated, trifucosylated glycan having a polylactosamine backbone.
8702529	6	65	gly	monosialylated	1153:1166	arg1	other					1142:1146	other	1142:1146	other	1142:1146	A minority of the O-glycans are alpha-1,3-fucosylated that occur as two major species containing the sialyl Lewis x antigen; one species is a disialylated, monofucosylated glycan, and the other is a monosialylated, trifucosylated glycan having a polylactosamine backbone.
8702529	4	66	attach	released	580:587	arg2	O-Glycans					565:573	O-Glycans	565:573	O-Glycans	565:573	O-Glycans were released from Ser/Thr residues by mild base/borohydride treatment of purified glycoproteins, and glycan structures were determined by a combination of techniques.
8702529	4	66	attach	released	580:587	arg1	residues					602:609	Ser/Thr residues	594:609	Ser/Thr residues	594:609	O-Glycans were released from Ser/Thr residues by mild base/borohydride treatment of purified glycoproteins, and glycan structures were determined by a combination of techniques.
8702529	2	67	theme	3H-sugar	383:390	arg1	precursors					392:401	3H-sugar precursors	383:401	3H-sugar precursors	383:401	In this report we describe the structures of the Ser/Thr-linked O-glycans of PSGL-1 synthesized by HL-60 cells metabolically radiolabeled with 3H-sugar precursors.
8702529	0	68	theme	HL-60	69:73	arg1	cells					75:79	HL-60 cells	69:79	HL-60 cells	69:79	Structures of the O-glycans on P-selectin glycoprotein ligand-1 from HL-60 cells.
8702529	5	69	theme	Galbeta1-->4GlcNAcbeta1-->6	899:925	arg1	GalNAcOH++					940:949	the core-2 tetrasaccharide Galbeta1-->4GlcNAcbeta1-->6(Galbeta1-->3)GalNAcOH++	872:949	the core-2 tetrasaccharide Galbeta1-->4GlcNAcbeta1-->6(Galbeta1-->3)GalNAcOH++	872:949	In contrast to expectations, PSGL-1 is not heavily fucosylated; a majority of the O-glycans are disialylated or neutral forms of the core-2 tetrasaccharide Galbeta1-->4GlcNAcbeta1-->6(Galbeta1-->3)GalNAcOH++ +.
8702529	0	70	gly	glycoprotein	42:53	arg1	glycoprotein					42:53	P-selectin glycoprotein ligand-1	31:62	P-selectin glycoprotein ligand-1 from HL-60 cells	31:79	Structures of the O-glycans on P-selectin glycoprotein ligand-1 from HL-60 cells.
8702529	1	71	theme	disulfide-bonded	129:144	arg1	ligand-1					106:113	P-selectin glycoprotein ligand-1	82:113	P-selectin glycoprotein ligand-1 (PSGL-1)	82:122	P-selectin glycoprotein ligand-1 (PSGL-1) is a disulfide-bonded homodimeric mucin-like glycoprotein on leukocytes that interacts with both P- and E-selectin.
8702529	1	71	theme	disulfide-bonded	129:144	arg1	glycoprotein					169:180	a disulfide-bonded homodimeric mucin-like glycoprotein	127:180	a disulfide-bonded homodimeric mucin-like glycoprotein on leukocytes that interacts with both P- and E-selectin	127:237	P-selectin glycoprotein ligand-1 (PSGL-1) is a disulfide-bonded homodimeric mucin-like glycoprotein on leukocytes that interacts with both P- and E-selectin.
8702529	4	72	theme	base/borohydride	619:634	arg1	treatment					636:644	mild base/borohydride treatment	614:644	mild base/borohydride treatment of purified glycoproteins	614:670	O-Glycans were released from Ser/Thr residues by mild base/borohydride treatment of purified glycoproteins, and glycan structures were determined by a combination of techniques.
8702529	7	73	gly	fucosylated	1241:1251	arg1	glycans					1253:1259	the fucosylated glycans	1237:1259	the fucosylated glycans found on PSGL-1	1237:1275	CD43 lacks the fucosylated glycans found on PSGL-1 and is enriched for the nonfucosylated, disialylated core-2 hexasaccharide.
8702529	0	74	from	O-glycans	18:26	arg1	ligand-1					55:62	P-selectin glycoprotein ligand-1	31:62	P-selectin glycoprotein ligand-1 from HL-60 cells	31:79	Structures of the O-glycans on P-selectin glycoprotein ligand-1 from HL-60 cells.
8702529	5	75	theme	O-glycans	825:833	arg1	forms					863:867	disialylated or neutral forms	839:867	disialylated or neutral forms	839:867	In contrast to expectations, PSGL-1 is not heavily fucosylated; a majority of the O-glycans are disialylated or neutral forms of the core-2 tetrasaccharide Galbeta1-->4GlcNAcbeta1-->6(Galbeta1-->3)GalNAcOH++ +.
8702529	5	75	theme	O-glycans	825:833	arg1	majority					809:816	a majority	807:816	a majority of the O-glycans	807:833	In contrast to expectations, PSGL-1 is not heavily fucosylated; a majority of the O-glycans are disialylated or neutral forms of the core-2 tetrasaccharide Galbeta1-->4GlcNAcbeta1-->6(Galbeta1-->3)GalNAcOH++ +.
8702529	1	76	theme	homodimeric	146:156	arg1	ligand-1					106:113	P-selectin glycoprotein ligand-1	82:113	P-selectin glycoprotein ligand-1 (PSGL-1)	82:122	P-selectin glycoprotein ligand-1 (PSGL-1) is a disulfide-bonded homodimeric mucin-like glycoprotein on leukocytes that interacts with both P- and E-selectin.
8702529	1	76	theme	homodimeric	146:156	arg1	glycoprotein					169:180	a disulfide-bonded homodimeric mucin-like glycoprotein	127:180	a disulfide-bonded homodimeric mucin-like glycoprotein on leukocytes that interacts with both P- and E-selectin	127:237	P-selectin glycoprotein ligand-1 (PSGL-1) is a disulfide-bonded homodimeric mucin-like glycoprotein on leukocytes that interacts with both P- and E-selectin.
8702529	4	77	theme	mild	614:617	arg1	treatment					636:644	mild base/borohydride treatment	614:644	mild base/borohydride treatment of purified glycoproteins	614:670	O-Glycans were released from Ser/Thr residues by mild base/borohydride treatment of purified glycoproteins, and glycan structures were determined by a combination of techniques.
11500028	0	0	theme	human	15:19	arg1	carbohydrate					28:39	human IgG-Fc carbohydrate	15:39	human IgG-Fc carbohydrate	15:39	Sialylation of human IgG-Fc carbohydrate by transfected rat alpha2,6-sialyltransferase.
11500028	4	1	gly	sialylated	633:642	arg1	F243					614:617	F243	614:617	F243	614:617	By comparison, the wild-type IgG3 (F243) is minimally sialylated (2-3% alpha2,3-linked), thus suggesting that sialylation is controlled primarily by the protein structure local to the carbohydrate and that the two sialyltransferases compete to sialylate the nascent oligosaccharide.
11500028	4	1	gly	sialylated	633:642	arg1	IgG3					608:611	the wild-type IgG3	594:611	the wild-type IgG3 (F243)	594:618	By comparison, the wild-type IgG3 (F243) is minimally sialylated (2-3% alpha2,3-linked), thus suggesting that sialylation is controlled primarily by the protein structure local to the carbohydrate and that the two sialyltransferases compete to sialylate the nascent oligosaccharide.
11500028	3	2	theme	alpha2,6-	525:533	arg1	ratio					516:520	the ratio	512:520	the ratio of alpha2,6- to alpha2,3-linked sialic acid	512:564	Following transfection of a rat alpha2,6-sialyltransferase gene into this parental cell line, IgG-Fc-linked glycans were sialylated (60% of glycans) such that the ratio of alpha2,6- to alpha2,3-linked sialic acid was 0.9:1.0.
11500028	3	2	theme	alpha2,6-	525:533	arg1	0.9:1.0					570:576	0.9:1.0	570:576	0.9:1.0	570:576	Following transfection of a rat alpha2,6-sialyltransferase gene into this parental cell line, IgG-Fc-linked glycans were sialylated (60% of glycans) such that the ratio of alpha2,6- to alpha2,3-linked sialic acid was 0.9:1.0.
11500028	5	3	theme	antibody	939:946	arg1	function					911:918	the function	907:918	the function of the recombinant antibody	907:946	The additional alpha2,6-sialylation affected the function of the recombinant antibody.
11500028	4	4	theme	nascent	837:843	arg1	oligosaccharide					845:859	the nascent oligosaccharide	833:859	the nascent oligosaccharide	833:859	By comparison, the wild-type IgG3 (F243) is minimally sialylated (2-3% alpha2,3-linked), thus suggesting that sialylation is controlled primarily by the protein structure local to the carbohydrate and that the two sialyltransferases compete to sialylate the nascent oligosaccharide.
11500028	2	5	theme	glycans	286:292	arg1	glycans					286:292	glycans	286:292	glycans	286:292	The resulting IgG-Fc-linked carbohydrate was significantly alpha2,3-sialylated (53% of glycans), as indicated by normal- and reverse-phase HPLC analyses.
11500028	2	5	theme	glycans	286:292	arg1	carbohydrate					227:238	The resulting IgG-Fc-linked carbohydrate	199:238	The resulting IgG-Fc-linked carbohydrate	199:238	The resulting IgG-Fc-linked carbohydrate was significantly alpha2,3-sialylated (53% of glycans), as indicated by normal- and reverse-phase HPLC analyses.
11500028	2	5	theme	glycans	286:292	arg1	%					281:281	53%	279:281	53% of glycans	279:292	The resulting IgG-Fc-linked carbohydrate was significantly alpha2,3-sialylated (53% of glycans), as indicated by normal- and reverse-phase HPLC analyses.
11500028	2	5	theme	glycans	286:292	arg1	alpha2,3-sialylated					258:276	alpha2,3-sialylated	258:276	alpha2,3-sialylated	258:276	The resulting IgG-Fc-linked carbohydrate was significantly alpha2,3-sialylated (53% of glycans), as indicated by normal- and reverse-phase HPLC analyses.
11500028	5	6	theme	recombinant	927:937	arg1	antibody					939:946	the recombinant antibody	923:946	the recombinant antibody	923:946	The additional alpha2,6-sialylation affected the function of the recombinant antibody.
11500028	6	7	theme	cell	1096:1099	arg1	lysis					1101:1105	target cell lysis	1089:1105	target cell lysis by complement	1089:1119	FA243 IgG3 having both alpha2,6 and alpha2,3-sialylation restored recognition to wild-type IgG3 levels for human FcgammaRI, FcgammaRII, and target cell lysis by complement.
11500028	4	8	theme	local	750:754	arg1	structure					740:748	the protein structure	728:748	the protein structure local to the carbohydrate	728:774	By comparison, the wild-type IgG3 (F243) is minimally sialylated (2-3% alpha2,3-linked), thus suggesting that sialylation is controlled primarily by the protein structure local to the carbohydrate and that the two sialyltransferases compete to sialylate the nascent oligosaccharide.
11500028	3	9	theme	cell	436:439	arg1	line					441:444	this parental cell line	422:444	this parental cell line	422:444	Following transfection of a rat alpha2,6-sialyltransferase gene into this parental cell line, IgG-Fc-linked glycans were sialylated (60% of glycans) such that the ratio of alpha2,6- to alpha2,3-linked sialic acid was 0.9:1.0.
11500028	2	10	dep	alpha2,3-sialylated	258:276	arg1	glycans					286:292	glycans	286:292	glycans	286:292	The resulting IgG-Fc-linked carbohydrate was significantly alpha2,3-sialylated (53% of glycans), as indicated by normal- and reverse-phase HPLC analyses.
11500028	2	10	dep	alpha2,3-sialylated	258:276	arg1	carbohydrate					227:238	The resulting IgG-Fc-linked carbohydrate	199:238	The resulting IgG-Fc-linked carbohydrate	199:238	The resulting IgG-Fc-linked carbohydrate was significantly alpha2,3-sialylated (53% of glycans), as indicated by normal- and reverse-phase HPLC analyses.
11500028	2	10	dep	alpha2,3-sialylated	258:276	arg1	%					281:281	53%	279:281	53% of glycans	279:292	The resulting IgG-Fc-linked carbohydrate was significantly alpha2,3-sialylated (53% of glycans), as indicated by normal- and reverse-phase HPLC analyses.
11500028	2	10	dep	alpha2,3-sialylated	258:276	arg1	alpha2,3-sialylated					258:276	alpha2,3-sialylated	258:276	alpha2,3-sialylated	258:276	The resulting IgG-Fc-linked carbohydrate was significantly alpha2,3-sialylated (53% of glycans), as indicated by normal- and reverse-phase HPLC analyses.
11500028	1	11	theme	recombinant	90:100	arg1	antibody					107:114	A recombinant IgG3 antibody	88:114	A recombinant IgG3 antibody with Phe-243 replaced by Ala (FA243)	88:151	A recombinant IgG3 antibody with Phe-243 replaced by Ala (FA243) was expressed in a CHO-K1 parental cell line.
11500028	3	12	theme	IgG-Fc-linked	447:459	arg1	glycans					461:467	IgG-Fc-linked glycans	447:467	IgG-Fc-linked glycans	447:467	Following transfection of a rat alpha2,6-sialyltransferase gene into this parental cell line, IgG-Fc-linked glycans were sialylated (60% of glycans) such that the ratio of alpha2,6- to alpha2,3-linked sialic acid was 0.9:1.0.
11500028	3	13	theme	rat	381:383	arg1	gene					412:415	a rat alpha2,6-sialyltransferase gene	379:415	a rat alpha2,6-sialyltransferase gene	379:415	Following transfection of a rat alpha2,6-sialyltransferase gene into this parental cell line, IgG-Fc-linked glycans were sialylated (60% of glycans) such that the ratio of alpha2,6- to alpha2,3-linked sialic acid was 0.9:1.0.
11500028	1	14	theme	IgG3	102:105	arg1	antibody					107:114	A recombinant IgG3 antibody	88:114	A recombinant IgG3 antibody with Phe-243 replaced by Ala (FA243)	88:151	A recombinant IgG3 antibody with Phe-243 replaced by Ala (FA243) was expressed in a CHO-K1 parental cell line.
11500028	1	15	theme	CHO-K1	172:177	arg1	line					193:196	a CHO-K1 parental cell line	170:196	a CHO-K1 parental cell line	170:196	A recombinant IgG3 antibody with Phe-243 replaced by Ala (FA243) was expressed in a CHO-K1 parental cell line.
11500028	3	16	theme	alpha2,6-sialyltransferase	385:410	arg1	gene					412:415	a rat alpha2,6-sialyltransferase gene	379:415	a rat alpha2,6-sialyltransferase gene	379:415	Following transfection of a rat alpha2,6-sialyltransferase gene into this parental cell line, IgG-Fc-linked glycans were sialylated (60% of glycans) such that the ratio of alpha2,6- to alpha2,3-linked sialic acid was 0.9:1.0.
11500028	7	17	theme	IgG	1172:1174	arg1	function					1176:1183	IgG function	1172:1183	IgG function	1172:1183	We discuss how sialylation linkage could modulate IgG function.
11500028	3	18	link	IgG-Fc-linked	447:459	arg1	glycans					461:467	IgG-Fc-linked glycans	447:467	IgG-Fc-linked glycans	447:467	Following transfection of a rat alpha2,6-sialyltransferase gene into this parental cell line, IgG-Fc-linked glycans were sialylated (60% of glycans) such that the ratio of alpha2,6- to alpha2,3-linked sialic acid was 0.9:1.0.
11500028	1	19	theme	parental	179:186	arg1	line					193:196	a CHO-K1 parental cell line	170:196	a CHO-K1 parental cell line	170:196	A recombinant IgG3 antibody with Phe-243 replaced by Ala (FA243) was expressed in a CHO-K1 parental cell line.
11500028	0	20	theme	IgG-Fc	21:26	arg1	carbohydrate					28:39	human IgG-Fc carbohydrate	15:39	human IgG-Fc carbohydrate	15:39	Sialylation of human IgG-Fc carbohydrate by transfected rat alpha2,6-sialyltransferase.
11500028	4	21	dep	sialylated	633:642	arg1	%					648:648	2-3% alpha2,3-linked	645:664	2-3% alpha2,3-linked	645:664	By comparison, the wild-type IgG3 (F243) is minimally sialylated (2-3% alpha2,3-linked), thus suggesting that sialylation is controlled primarily by the protein structure local to the carbohydrate and that the two sialyltransferases compete to sialylate the nascent oligosaccharide.
11500028	3	22	dep	0.9:1.0	570:576	arg1	such					502:505	such	502:505	such	502:505	Following transfection of a rat alpha2,6-sialyltransferase gene into this parental cell line, IgG-Fc-linked glycans were sialylated (60% of glycans) such that the ratio of alpha2,6- to alpha2,3-linked sialic acid was 0.9:1.0.
11500028	3	23	theme	alpha2,3-linked	538:552	arg1	acid					561:564	alpha2,3-linked sialic acid	538:564	alpha2,3-linked sialic acid	538:564	Following transfection of a rat alpha2,6-sialyltransferase gene into this parental cell line, IgG-Fc-linked glycans were sialylated (60% of glycans) such that the ratio of alpha2,6- to alpha2,3-linked sialic acid was 0.9:1.0.
11500028	1	24	theme	cell	188:191	arg1	line					193:196	a CHO-K1 parental cell line	170:196	a CHO-K1 parental cell line	170:196	A recombinant IgG3 antibody with Phe-243 replaced by Ala (FA243) was expressed in a CHO-K1 parental cell line.
11500028	1	25	with	antibody	107:114	arg1	Phe-243					121:127	Phe-243	121:127	Phe-243 replaced by Ala (FA243)	121:151	A recombinant IgG3 antibody with Phe-243 replaced by Ala (FA243) was expressed in a CHO-K1 parental cell line.
11500028	6	26	theme	wild-type	1030:1038	arg1	levels					1045:1050	wild-type IgG3 levels	1030:1050	wild-type IgG3 levels for human FcgammaRI, FcgammaRII, and target cell lysis by complement	1030:1119	FA243 IgG3 having both alpha2,6 and alpha2,3-sialylation restored recognition to wild-type IgG3 levels for human FcgammaRI, FcgammaRII, and target cell lysis by complement.
11500028	3	27	theme	sialic	554:559	arg1	acid					561:564	alpha2,3-linked sialic acid	538:564	alpha2,3-linked sialic acid	538:564	Following transfection of a rat alpha2,6-sialyltransferase gene into this parental cell line, IgG-Fc-linked glycans were sialylated (60% of glycans) such that the ratio of alpha2,6- to alpha2,3-linked sialic acid was 0.9:1.0.
11500028	5	28	theme	additional	866:875	arg1	alpha2,6-sialylation					877:896	The additional alpha2,6-sialylation	862:896	The additional alpha2,6-sialylation	862:896	The additional alpha2,6-sialylation affected the function of the recombinant antibody.
11500028	3	29	theme	glycans	493:499	arg1	glycans					493:499	glycans	493:499	glycans	493:499	Following transfection of a rat alpha2,6-sialyltransferase gene into this parental cell line, IgG-Fc-linked glycans were sialylated (60% of glycans) such that the ratio of alpha2,6- to alpha2,3-linked sialic acid was 0.9:1.0.
11500028	3	29	theme	glycans	493:499	arg1	%					488:488	60%	486:488	60% of glycans	486:499	Following transfection of a rat alpha2,6-sialyltransferase gene into this parental cell line, IgG-Fc-linked glycans were sialylated (60% of glycans) such that the ratio of alpha2,6- to alpha2,3-linked sialic acid was 0.9:1.0.
11500028	6	30	contain	having	960:965	arg2	alpha2,3-sialylation					985:1004	alpha2,3-sialylation	985:1004	alpha2,3-sialylation	985:1004	FA243 IgG3 having both alpha2,6 and alpha2,3-sialylation restored recognition to wild-type IgG3 levels for human FcgammaRI, FcgammaRII, and target cell lysis by complement.
11500028	6	30	contain	having	960:965	arg1	IgG3					955:958	IgG3	955:958	IgG3	955:958	FA243 IgG3 having both alpha2,6 and alpha2,3-sialylation restored recognition to wild-type IgG3 levels for human FcgammaRI, FcgammaRII, and target cell lysis by complement.
11500028	6	30	contain	having	960:965	arg2	alpha2,6					972:979	alpha2,6	972:979	alpha2,6	972:979	FA243 IgG3 having both alpha2,6 and alpha2,3-sialylation restored recognition to wild-type IgG3 levels for human FcgammaRI, FcgammaRII, and target cell lysis by complement.
11500028	4	31	gly	sialylate	823:831	arg1	oligosaccharide					845:859	the nascent oligosaccharide	833:859	the nascent oligosaccharide	833:859	By comparison, the wild-type IgG3 (F243) is minimally sialylated (2-3% alpha2,3-linked), thus suggesting that sialylation is controlled primarily by the protein structure local to the carbohydrate and that the two sialyltransferases compete to sialylate the nascent oligosaccharide.
11500028	0	32	theme	carbohydrate	28:39	arg1	Sialylation					0:10	Sialylation	0:10	Sialylation of human IgG-Fc carbohydrate by transfected rat alpha2,6-sialyltransferase.	0:86	Sialylation of human IgG-Fc carbohydrate by transfected rat alpha2,6-sialyltransferase.
11500028	3	33	theme	parental	427:434	arg1	line					441:444	this parental cell line	422:444	this parental cell line	422:444	Following transfection of a rat alpha2,6-sialyltransferase gene into this parental cell line, IgG-Fc-linked glycans were sialylated (60% of glycans) such that the ratio of alpha2,6- to alpha2,3-linked sialic acid was 0.9:1.0.
11500028	3	34	gly	sialylated	474:483	arg1	glycans					461:467	IgG-Fc-linked glycans	447:467	IgG-Fc-linked glycans	447:467	Following transfection of a rat alpha2,6-sialyltransferase gene into this parental cell line, IgG-Fc-linked glycans were sialylated (60% of glycans) such that the ratio of alpha2,6- to alpha2,3-linked sialic acid was 0.9:1.0.
11500028	6	35	theme	human	1056:1060	arg1	FcgammaRI					1062:1070	human FcgammaRI	1056:1070	human FcgammaRI	1056:1070	FA243 IgG3 having both alpha2,6 and alpha2,3-sialylation restored recognition to wild-type IgG3 levels for human FcgammaRI, FcgammaRII, and target cell lysis by complement.
11500028	0	36	theme	rat	56:58	arg1	alpha2,6-sialyltransferase					60:85	transfected rat alpha2,6-sialyltransferase	44:85	transfected rat alpha2,6-sialyltransferase	44:85	Sialylation of human IgG-Fc carbohydrate by transfected rat alpha2,6-sialyltransferase.
11500028	5	37	gly	alpha2,6-sialylation	877:896	arg1	antibody					939:946	the recombinant antibody	923:946	the recombinant antibody	923:946	The additional alpha2,6-sialylation affected the function of the recombinant antibody.
11500028	2	38	theme	IgG-Fc-linked	213:225	arg1	carbohydrate					227:238	The resulting IgG-Fc-linked carbohydrate	199:238	The resulting IgG-Fc-linked carbohydrate	199:238	The resulting IgG-Fc-linked carbohydrate was significantly alpha2,3-sialylated (53% of glycans), as indicated by normal- and reverse-phase HPLC analyses.
11500028	2	38	theme	IgG-Fc-linked	213:225	arg1	alpha2,3-sialylated					258:276	alpha2,3-sialylated	258:276	alpha2,3-sialylated	258:276	The resulting IgG-Fc-linked carbohydrate was significantly alpha2,3-sialylated (53% of glycans), as indicated by normal- and reverse-phase HPLC analyses.
11500028	2	38	theme	IgG-Fc-linked	213:225	arg1	%					281:281	53%	279:281	53% of glycans	279:292	The resulting IgG-Fc-linked carbohydrate was significantly alpha2,3-sialylated (53% of glycans), as indicated by normal- and reverse-phase HPLC analyses.
11500028	2	38	theme	IgG-Fc-linked	213:225	arg1	glycans					286:292	glycans	286:292	glycans	286:292	The resulting IgG-Fc-linked carbohydrate was significantly alpha2,3-sialylated (53% of glycans), as indicated by normal- and reverse-phase HPLC analyses.
11500028	2	39	theme	HPLC	338:341	arg1	analyses					343:350	normal- and reverse-phase HPLC analyses	312:350	normal- and reverse-phase HPLC analyses	312:350	The resulting IgG-Fc-linked carbohydrate was significantly alpha2,3-sialylated (53% of glycans), as indicated by normal- and reverse-phase HPLC analyses.
11500028	0	40	theme	transfected	44:54	arg1	alpha2,6-sialyltransferase					60:85	transfected rat alpha2,6-sialyltransferase	44:85	transfected rat alpha2,6-sialyltransferase	44:85	Sialylation of human IgG-Fc carbohydrate by transfected rat alpha2,6-sialyltransferase.
11500028	2	41	theme	resulting	203:211	arg1	carbohydrate					227:238	The resulting IgG-Fc-linked carbohydrate	199:238	The resulting IgG-Fc-linked carbohydrate	199:238	The resulting IgG-Fc-linked carbohydrate was significantly alpha2,3-sialylated (53% of glycans), as indicated by normal- and reverse-phase HPLC analyses.
11500028	2	41	theme	resulting	203:211	arg1	alpha2,3-sialylated					258:276	alpha2,3-sialylated	258:276	alpha2,3-sialylated	258:276	The resulting IgG-Fc-linked carbohydrate was significantly alpha2,3-sialylated (53% of glycans), as indicated by normal- and reverse-phase HPLC analyses.
11500028	2	41	theme	resulting	203:211	arg1	%					281:281	53%	279:281	53% of glycans	279:292	The resulting IgG-Fc-linked carbohydrate was significantly alpha2,3-sialylated (53% of glycans), as indicated by normal- and reverse-phase HPLC analyses.
11500028	2	41	theme	resulting	203:211	arg1	glycans					286:292	glycans	286:292	glycans	286:292	The resulting IgG-Fc-linked carbohydrate was significantly alpha2,3-sialylated (53% of glycans), as indicated by normal- and reverse-phase HPLC analyses.
11500028	2	42	theme	reverse-phase	324:336	arg1	analyses					343:350	normal- and reverse-phase HPLC analyses	312:350	normal- and reverse-phase HPLC analyses	312:350	The resulting IgG-Fc-linked carbohydrate was significantly alpha2,3-sialylated (53% of glycans), as indicated by normal- and reverse-phase HPLC analyses.
11500028	7	43	theme	sialylation	1137:1147	arg1	linkage					1149:1155	sialylation linkage	1137:1155	sialylation linkage	1137:1155	We discuss how sialylation linkage could modulate IgG function.
11500028	4	44	link	alpha2,3-linked	650:664	arg1	%					648:648	2-3% alpha2,3-linked	645:664	2-3% alpha2,3-linked	645:664	By comparison, the wild-type IgG3 (F243) is minimally sialylated (2-3% alpha2,3-linked), thus suggesting that sialylation is controlled primarily by the protein structure local to the carbohydrate and that the two sialyltransferases compete to sialylate the nascent oligosaccharide.
11500028	2	45	link	IgG-Fc-linked	213:225	arg1	carbohydrate					227:238	The resulting IgG-Fc-linked carbohydrate	199:238	The resulting IgG-Fc-linked carbohydrate	199:238	The resulting IgG-Fc-linked carbohydrate was significantly alpha2,3-sialylated (53% of glycans), as indicated by normal- and reverse-phase HPLC analyses.
11500028	2	45	link	IgG-Fc-linked	213:225	arg1	alpha2,3-sialylated					258:276	alpha2,3-sialylated	258:276	alpha2,3-sialylated	258:276	The resulting IgG-Fc-linked carbohydrate was significantly alpha2,3-sialylated (53% of glycans), as indicated by normal- and reverse-phase HPLC analyses.
11500028	2	45	link	IgG-Fc-linked	213:225	arg1	%					281:281	53%	279:281	53% of glycans	279:292	The resulting IgG-Fc-linked carbohydrate was significantly alpha2,3-sialylated (53% of glycans), as indicated by normal- and reverse-phase HPLC analyses.
11500028	2	45	link	IgG-Fc-linked	213:225	arg1	glycans					286:292	glycans	286:292	glycans	286:292	The resulting IgG-Fc-linked carbohydrate was significantly alpha2,3-sialylated (53% of glycans), as indicated by normal- and reverse-phase HPLC analyses.
11500028	4	46	theme	protein	732:738	arg1	structure					740:748	the protein structure	728:748	the protein structure local to the carbohydrate	728:774	By comparison, the wild-type IgG3 (F243) is minimally sialylated (2-3% alpha2,3-linked), thus suggesting that sialylation is controlled primarily by the protein structure local to the carbohydrate and that the two sialyltransferases compete to sialylate the nascent oligosaccharide.
11500028	2	47	theme	normal-	312:318	arg1	analyses					343:350	normal- and reverse-phase HPLC analyses	312:350	normal- and reverse-phase HPLC analyses	312:350	The resulting IgG-Fc-linked carbohydrate was significantly alpha2,3-sialylated (53% of glycans), as indicated by normal- and reverse-phase HPLC analyses.
11500028	3	48	link	alpha2,3-linked	538:552	arg1	acid					561:564	alpha2,3-linked sialic acid	538:564	alpha2,3-linked sialic acid	538:564	Following transfection of a rat alpha2,6-sialyltransferase gene into this parental cell line, IgG-Fc-linked glycans were sialylated (60% of glycans) such that the ratio of alpha2,6- to alpha2,3-linked sialic acid was 0.9:1.0.
11500028	3	49	dep	sialylated	474:483	arg1	glycans					493:499	glycans	493:499	glycans	493:499	Following transfection of a rat alpha2,6-sialyltransferase gene into this parental cell line, IgG-Fc-linked glycans were sialylated (60% of glycans) such that the ratio of alpha2,6- to alpha2,3-linked sialic acid was 0.9:1.0.
11500028	3	49	dep	sialylated	474:483	arg1	%					488:488	60%	486:488	60% of glycans	486:499	Following transfection of a rat alpha2,6-sialyltransferase gene into this parental cell line, IgG-Fc-linked glycans were sialylated (60% of glycans) such that the ratio of alpha2,6- to alpha2,3-linked sialic acid was 0.9:1.0.
11500028	4	50	theme	alpha2,3-linked	650:664	arg1	%					648:648	2-3% alpha2,3-linked	645:664	2-3% alpha2,3-linked	645:664	By comparison, the wild-type IgG3 (F243) is minimally sialylated (2-3% alpha2,3-linked), thus suggesting that sialylation is controlled primarily by the protein structure local to the carbohydrate and that the two sialyltransferases compete to sialylate the nascent oligosaccharide.
11500028	6	51	theme	target	1089:1094	arg1	lysis					1101:1105	target cell lysis	1089:1105	target cell lysis by complement	1089:1119	FA243 IgG3 having both alpha2,6 and alpha2,3-sialylation restored recognition to wild-type IgG3 levels for human FcgammaRI, FcgammaRII, and target cell lysis by complement.
11500028	6	52	theme	IgG3	1040:1043	arg1	levels					1045:1050	wild-type IgG3 levels	1030:1050	wild-type IgG3 levels for human FcgammaRI, FcgammaRII, and target cell lysis by complement	1030:1119	FA243 IgG3 having both alpha2,6 and alpha2,3-sialylation restored recognition to wild-type IgG3 levels for human FcgammaRI, FcgammaRII, and target cell lysis by complement.
11500028	3	53	theme	gene	412:415	arg1	transfection					363:374	transfection	363:374	transfection of a rat alpha2,6-sialyltransferase gene into this parental cell line	363:444	Following transfection of a rat alpha2,6-sialyltransferase gene into this parental cell line, IgG-Fc-linked glycans were sialylated (60% of glycans) such that the ratio of alpha2,6- to alpha2,3-linked sialic acid was 0.9:1.0.
11500028	2	54	gly	alpha2,3-sialylated	258:276	arg1	carbohydrate					227:238	The resulting IgG-Fc-linked carbohydrate	199:238	The resulting IgG-Fc-linked carbohydrate	199:238	The resulting IgG-Fc-linked carbohydrate was significantly alpha2,3-sialylated (53% of glycans), as indicated by normal- and reverse-phase HPLC analyses.
11500028	2	54	gly	alpha2,3-sialylated	258:276	arg1	alpha2,3-sialylated					258:276	alpha2,3-sialylated	258:276	alpha2,3-sialylated	258:276	The resulting IgG-Fc-linked carbohydrate was significantly alpha2,3-sialylated (53% of glycans), as indicated by normal- and reverse-phase HPLC analyses.
11500028	2	54	gly	alpha2,3-sialylated	258:276	arg1	%					281:281	53%	279:281	53% of glycans	279:292	The resulting IgG-Fc-linked carbohydrate was significantly alpha2,3-sialylated (53% of glycans), as indicated by normal- and reverse-phase HPLC analyses.
11500028	2	54	gly	alpha2,3-sialylated	258:276	arg1	glycans					286:292	glycans	286:292	glycans	286:292	The resulting IgG-Fc-linked carbohydrate was significantly alpha2,3-sialylated (53% of glycans), as indicated by normal- and reverse-phase HPLC analyses.
11500028	4	55	theme	wild-type	598:606	arg1	F243					614:617	F243	614:617	F243	614:617	By comparison, the wild-type IgG3 (F243) is minimally sialylated (2-3% alpha2,3-linked), thus suggesting that sialylation is controlled primarily by the protein structure local to the carbohydrate and that the two sialyltransferases compete to sialylate the nascent oligosaccharide.
11500028	4	55	theme	wild-type	598:606	arg1	IgG3					608:611	the wild-type IgG3	594:611	the wild-type IgG3 (F243)	594:618	By comparison, the wild-type IgG3 (F243) is minimally sialylated (2-3% alpha2,3-linked), thus suggesting that sialylation is controlled primarily by the protein structure local to the carbohydrate and that the two sialyltransferases compete to sialylate the nascent oligosaccharide.
10871054	4	0	theme	hybridoma	836:844	arg1	cells					850:854	hybridoma 3-4 cells	836:854	hybridoma 3-4 cells	836:854	We analyzed the structures of sugar chains on the constant region of the mu-chain of IgMs produced by parental No. 12 cells and hybridoma 3-4 cells.
10871054	3	1	theme	line	690:693	arg1	hybridization					567:579	hybridization	567:579	hybridization of an IgM-producing Epstein-Barr virus transformed human B-cell line termed No. 12, and a human myeloma cell line termed P109	567:705	In this report, we describe structural changes of the N-glycans in immunoglobulin M (IgM) produced by a hybridoma cell line termed 3-4, which was established through hybridization of an IgM-producing Epstein-Barr virus transformed human B-cell line termed No. 12, and a human myeloma cell line termed P109.
10871054	4	2	theme	No.	819:821	arg1	cells					826:830	parental No. 12 cells	810:830	parental No. 12 cells	810:830	We analyzed the structures of sugar chains on the constant region of the mu-chain of IgMs produced by parental No. 12 cells and hybridoma 3-4 cells.
10871054	6	3	theme	GlcNAc	1095:1100	arg1	amount					1075:1080	the amount	1071:1080	the amount of bisecting GlcNAc	1071:1100	However, the amount of bisecting GlcNAc was markedly decreased in the hybridoma cells.
10871054	6	3	theme	GlcNAc	1095:1100	arg1	GlcNAc					1095:1100	bisecting GlcNAc	1085:1100	bisecting GlcNAc	1085:1100	However, the amount of bisecting GlcNAc was markedly decreased in the hybridoma cells.
10871054	10	4	theme	cells	1722:1726	arg1	influence					1704:1712	the influence	1700:1712	the influence of P109 cells	1700:1726	The above results demonstrated a reduction in the intracellular activity of GnT-III in the hybridoma cells, which was largely due to the influence of P109 cells.
10871054	5	5	from	N395	951:954	arg1	types					1002:1006	fully galactosylated biantennary complex types	961:1006	fully galactosylated biantennary complex types	961:1006	In both parental cells and hybridoma cells, the predominant structures at Asn171, Asn332, and N395 were fully galactosylated biantennary complex types, with or without core fucose and/or bisecting GlcNAc.
10871054	5	5	from	N395	951:954	arg1	structures					917:926	the predominant structures	901:926	the predominant structures at Asn171, Asn332, and N395	901:954	In both parental cells and hybridoma cells, the predominant structures at Asn171, Asn332, and N395 were fully galactosylated biantennary complex types, with or without core fucose and/or bisecting GlcNAc.
10871054	9	6	theme	corresponding	1461:1473	arg1	level					1475:1479	The corresponding level	1457:1479	The corresponding level of activity observed in hybridoma 3-4 cells	1457:1523	The corresponding level of activity observed in hybridoma 3-4 cells was much lower than that in No. 12 cells.
10871054	9	6	theme	corresponding	1461:1473	arg1	lower					1534:1538	lower	1534:1538	lower	1534:1538	The corresponding level of activity observed in hybridoma 3-4 cells was much lower than that in No. 12 cells.
10871054	11	7	theme	activity	1827:1834	arg1	level					1810:1814	the level	1806:1814	the level of GnT-III activity	1806:1834	Moreover, the sugar chain structures of IgMs produced by the cells reflected the level of GnT-III activity.
10871054	9	8	located	observed	1493:1500	arg1	cells					1519:1523	hybridoma 3-4 cells	1505:1523	hybridoma 3-4 cells	1505:1523	The corresponding level of activity observed in hybridoma 3-4 cells was much lower than that in No. 12 cells.
10871054	9	8	located	observed	1493:1500	arg2	lower					1534:1538	lower	1534:1538	lower	1534:1538	The corresponding level of activity observed in hybridoma 3-4 cells was much lower than that in No. 12 cells.
10871054	9	8	located	observed	1493:1500	arg2	level					1475:1479	The corresponding level	1457:1479	The corresponding level of activity observed in hybridoma 3-4 cells	1457:1523	The corresponding level of activity observed in hybridoma 3-4 cells was much lower than that in No. 12 cells.
10871054	11	9	theme	chain	1749:1753	arg1	structures					1755:1764	the sugar chain structures	1739:1764	the sugar chain structures of IgMs produced by the cells	1739:1794	Moreover, the sugar chain structures of IgMs produced by the cells reflected the level of GnT-III activity.
10871054	5	10	theme	parental	865:872	arg1	cells					874:878	parental cells	865:878	parental cells	865:878	In both parental cells and hybridoma cells, the predominant structures at Asn171, Asn332, and N395 were fully galactosylated biantennary complex types, with or without core fucose and/or bisecting GlcNAc.
10871054	7	11	theme	parental	1334:1341	arg1	cells					1343:1347	parental cells	1334:1347	parental cells	1334:1347	Therefore, the activity of UDP-N-acetylglucosamine:beta-D-mannoside beta-1,4-N-acetylglucosaminyltransferase (GnT-III) responsible for the formation of bisecting GlcNAc was measured in parental cells and hybridoma cells.
10871054	3	12	theme	transformed	620:630	arg1	line					645:648	an IgM-producing Epstein-Barr virus transformed human B-cell line	584:648	an IgM-producing Epstein-Barr virus transformed human B-cell line termed No. 12	584:662	In this report, we describe structural changes of the N-glycans in immunoglobulin M (IgM) produced by a hybridoma cell line termed 3-4, which was established through hybridization of an IgM-producing Epstein-Barr virus transformed human B-cell line termed No. 12, and a human myeloma cell line termed P109.
10871054	6	13	theme	hybridoma	1132:1140	arg1	cells					1142:1146	the hybridoma cells	1128:1146	the hybridoma cells	1128:1146	However, the amount of bisecting GlcNAc was markedly decreased in the hybridoma cells.
10871054	0	14	theme	immunoglobulins	55:69	arg1	N-glycans					25:33	the N-glycans	21:33	the N-glycans of human monoclonal immunoglobulins	21:69	Comparative study of the N-glycans of human monoclonal immunoglobulins M produced by hybridoma and parental cells.
10871054	3	15	theme	Epstein-Barr	601:612	arg1	line					645:648	an IgM-producing Epstein-Barr virus transformed human B-cell line	584:648	an IgM-producing Epstein-Barr virus transformed human B-cell line termed No. 12	584:662	In this report, we describe structural changes of the N-glycans in immunoglobulin M (IgM) produced by a hybridoma cell line termed 3-4, which was established through hybridization of an IgM-producing Epstein-Barr virus transformed human B-cell line termed No. 12, and a human myeloma cell line termed P109.
10871054	2	16	from	influence	301:309	arg1	glycosylation					345:357	the glycosylation	341:357	the glycosylation of produced antibodies	341:380	In order to clearly characterize antibodies produced by hybridomas, the influence of cell-cell hybridization on the glycosylation of produced antibodies should be studied.
10871054	9	17	theme	hybridoma	1505:1513	arg1	cells					1519:1523	hybridoma 3-4 cells	1505:1523	hybridoma 3-4 cells	1505:1523	The corresponding level of activity observed in hybridoma 3-4 cells was much lower than that in No. 12 cells.
10871054	4	18	theme	sugar	738:742	arg1	chains					744:749	sugar chains	738:749	sugar chains on the constant region of the mu-chain of IgMs produced by parental No. 12 cells and hybridoma 3-4 cells	738:854	We analyzed the structures of sugar chains on the constant region of the mu-chain of IgMs produced by parental No. 12 cells and hybridoma 3-4 cells.
10871054	0	19	theme	parental	99:106	arg1	cells					108:112	parental cells	99:112	parental cells	99:112	Comparative study of the N-glycans of human monoclonal immunoglobulins M produced by hybridoma and parental cells.
10871054	5	20	theme	bisecting	1044:1052	arg1	GlcNAc					1054:1059	bisecting GlcNAc	1044:1059	bisecting GlcNAc	1044:1059	In both parental cells and hybridoma cells, the predominant structures at Asn171, Asn332, and N395 were fully galactosylated biantennary complex types, with or without core fucose and/or bisecting GlcNAc.
10871054	4	21	from	structures	724:733	arg1	region					767:772	the constant region	754:772	the constant region of the mu-chain of IgMs produced by parental No. 12 cells and hybridoma 3-4 cells	754:854	We analyzed the structures of sugar chains on the constant region of the mu-chain of IgMs produced by parental No. 12 cells and hybridoma 3-4 cells.
10871054	11	22	theme	GnT-III	1819:1825	arg1	activity					1827:1834	GnT-III activity	1819:1834	GnT-III activity	1819:1834	Moreover, the sugar chain structures of IgMs produced by the cells reflected the level of GnT-III activity.
10871054	0	23	theme	Comparative	0:10	arg1	study					12:16	Comparative study	0:16	Comparative study of the N-glycans of human monoclonal immunoglobulins M	0:71	Comparative study of the N-glycans of human monoclonal immunoglobulins M produced by hybridoma and parental cells.
10871054	7	24	theme	bisecting	1301:1309	arg1	GlcNAc					1311:1316	bisecting GlcNAc	1301:1316	bisecting GlcNAc	1301:1316	Therefore, the activity of UDP-N-acetylglucosamine:beta-D-mannoside beta-1,4-N-acetylglucosaminyltransferase (GnT-III) responsible for the formation of bisecting GlcNAc was measured in parental cells and hybridoma cells.
10871054	10	25	theme	GnT-III	1643:1649	arg1	activity					1631:1638	the intracellular activity	1613:1638	the intracellular activity of GnT-III in the hybridoma cells	1613:1672	The above results demonstrated a reduction in the intracellular activity of GnT-III in the hybridoma cells, which was largely due to the influence of P109 cells.
10871054	8	26	dep	showed	1383:1388	arg1	whereas					1413:1419	whereas	1413:1419	whereas	1413:1419	No. 12 cells showed some GnT-III activity, whereas P109 cells showed no such activity.
10871054	4	27	theme	mu-chain	781:788	arg1	region					767:772	the constant region	754:772	the constant region of the mu-chain of IgMs produced by parental No. 12 cells and hybridoma 3-4 cells	754:854	We analyzed the structures of sugar chains on the constant region of the mu-chain of IgMs produced by parental No. 12 cells and hybridoma 3-4 cells.
10871054	0	28	theme	N-glycans	25:33	arg1	study					12:16	Comparative study	0:16	Comparative study of the N-glycans of human monoclonal immunoglobulins M	0:71	Comparative study of the N-glycans of human monoclonal immunoglobulins M produced by hybridoma and parental cells.
10871054	10	29	from	reduction	1600:1608	arg1	activity					1631:1638	the intracellular activity	1613:1638	the intracellular activity of GnT-III in the hybridoma cells	1613:1672	The above results demonstrated a reduction in the intracellular activity of GnT-III in the hybridoma cells, which was largely due to the influence of P109 cells.
10871054	3	30	theme	B-cell	638:643	arg1	line					645:648	an IgM-producing Epstein-Barr virus transformed human B-cell line	584:648	an IgM-producing Epstein-Barr virus transformed human B-cell line termed No. 12	584:662	In this report, we describe structural changes of the N-glycans in immunoglobulin M (IgM) produced by a hybridoma cell line termed 3-4, which was established through hybridization of an IgM-producing Epstein-Barr virus transformed human B-cell line termed No. 12, and a human myeloma cell line termed P109.
10871054	4	31	theme	IgMs	793:796	arg1	mu-chain					781:788	the mu-chain	777:788	the mu-chain of IgMs produced by parental No. 12 cells and hybridoma 3-4 cells	777:854	We analyzed the structures of sugar chains on the constant region of the mu-chain of IgMs produced by parental No. 12 cells and hybridoma 3-4 cells.
10871054	0	32	theme	human	38:42	arg1	immunoglobulins					55:69	human monoclonal immunoglobulins	38:69	human monoclonal immunoglobulins	38:69	Comparative study of the N-glycans of human monoclonal immunoglobulins M produced by hybridoma and parental cells.
10871054	5	33	theme	galactosylated	967:980	arg1	types					1002:1006	fully galactosylated biantennary complex types	961:1006	fully galactosylated biantennary complex types	961:1006	In both parental cells and hybridoma cells, the predominant structures at Asn171, Asn332, and N395 were fully galactosylated biantennary complex types, with or without core fucose and/or bisecting GlcNAc.
10871054	5	33	theme	galactosylated	967:980	arg1	structures					917:926	the predominant structures	901:926	the predominant structures at Asn171, Asn332, and N395	901:954	In both parental cells and hybridoma cells, the predominant structures at Asn171, Asn332, and N395 were fully galactosylated biantennary complex types, with or without core fucose and/or bisecting GlcNAc.
10871054	8	34	theme	GnT-III	1395:1401	arg1	activity					1403:1410	some GnT-III activity	1390:1410	some GnT-III activity	1390:1410	No. 12 cells showed some GnT-III activity, whereas P109 cells showed no such activity.
10871054	1	35	theme	antibodies	217:226	arg1	abundance					204:212	an abundance	201:212	an abundance of antibodies	201:226	Cell-cell hybridization is one method of establishing cell lines capable of producing an abundance of antibodies.
10871054	10	36	from	activity	1631:1638	arg1	cells					1668:1672	the hybridoma cells	1654:1672	the hybridoma cells	1654:1672	The above results demonstrated a reduction in the intracellular activity of GnT-III in the hybridoma cells, which was largely due to the influence of P109 cells.
10871054	10	37	theme	intracellular	1617:1629	arg1	activity					1631:1638	the intracellular activity	1613:1638	the intracellular activity of GnT-III in the hybridoma cells	1613:1672	The above results demonstrated a reduction in the intracellular activity of GnT-III in the hybridoma cells, which was largely due to the influence of P109 cells.
10871054	7	38	theme	beta-D-mannoside	1200:1215	arg1	GnT-III					1259:1265	GnT-III	1259:1265	GnT-III	1259:1265	Therefore, the activity of UDP-N-acetylglucosamine:beta-D-mannoside beta-1,4-N-acetylglucosaminyltransferase (GnT-III) responsible for the formation of bisecting GlcNAc was measured in parental cells and hybridoma cells.
10871054	7	38	theme	beta-D-mannoside	1200:1215	arg1	beta-1,4-N-acetylglucosaminyltransferase					1217:1256	UDP-N-acetylglucosamine:beta-D-mannoside beta-1,4-N-acetylglucosaminyltransferase	1176:1256	UDP-N-acetylglucosamine:beta-D-mannoside beta-1,4-N-acetylglucosaminyltransferase (GnT-III) responsible for the formation of bisecting GlcNAc	1176:1316	Therefore, the activity of UDP-N-acetylglucosamine:beta-D-mannoside beta-1,4-N-acetylglucosaminyltransferase (GnT-III) responsible for the formation of bisecting GlcNAc was measured in parental cells and hybridoma cells.
10871054	3	39	theme	cell	685:688	arg1	line					690:693	a human myeloma cell line	669:693	a human myeloma cell line termed P109	669:705	In this report, we describe structural changes of the N-glycans in immunoglobulin M (IgM) produced by a hybridoma cell line termed 3-4, which was established through hybridization of an IgM-producing Epstein-Barr virus transformed human B-cell line termed No. 12, and a human myeloma cell line termed P109.
10871054	2	40	theme	produced	362:369	arg1	antibodies					371:380	produced antibodies	362:380	produced antibodies	362:380	In order to clearly characterize antibodies produced by hybridomas, the influence of cell-cell hybridization on the glycosylation of produced antibodies should be studied.
10871054	5	41	from	Asn171	931:936	arg1	types					1002:1006	fully galactosylated biantennary complex types	961:1006	fully galactosylated biantennary complex types	961:1006	In both parental cells and hybridoma cells, the predominant structures at Asn171, Asn332, and N395 were fully galactosylated biantennary complex types, with or without core fucose and/or bisecting GlcNAc.
10871054	5	41	from	Asn171	931:936	arg1	structures					917:926	the predominant structures	901:926	the predominant structures at Asn171, Asn332, and N395	901:954	In both parental cells and hybridoma cells, the predominant structures at Asn171, Asn332, and N395 were fully galactosylated biantennary complex types, with or without core fucose and/or bisecting GlcNAc.
10871054	7	42	theme	UDP-N-acetylglucosamine	1176:1198	arg1	GnT-III					1259:1265	GnT-III	1259:1265	GnT-III	1259:1265	Therefore, the activity of UDP-N-acetylglucosamine:beta-D-mannoside beta-1,4-N-acetylglucosaminyltransferase (GnT-III) responsible for the formation of bisecting GlcNAc was measured in parental cells and hybridoma cells.
10871054	7	42	theme	UDP-N-acetylglucosamine	1176:1198	arg1	beta-1,4-N-acetylglucosaminyltransferase					1217:1256	UDP-N-acetylglucosamine:beta-D-mannoside beta-1,4-N-acetylglucosaminyltransferase	1176:1256	UDP-N-acetylglucosamine:beta-D-mannoside beta-1,4-N-acetylglucosaminyltransferase (GnT-III) responsible for the formation of bisecting GlcNAc	1176:1316	Therefore, the activity of UDP-N-acetylglucosamine:beta-D-mannoside beta-1,4-N-acetylglucosaminyltransferase (GnT-III) responsible for the formation of bisecting GlcNAc was measured in parental cells and hybridoma cells.
10871054	3	43	theme	human	671:675	arg1	line					690:693	a human myeloma cell line	669:693	a human myeloma cell line termed P109	669:705	In this report, we describe structural changes of the N-glycans in immunoglobulin M (IgM) produced by a hybridoma cell line termed 3-4, which was established through hybridization of an IgM-producing Epstein-Barr virus transformed human B-cell line termed No. 12, and a human myeloma cell line termed P109.
10871054	3	44	theme	cell	515:518	arg1	line					520:523	a hybridoma cell line	503:523	a hybridoma cell line	503:523	In this report, we describe structural changes of the N-glycans in immunoglobulin M (IgM) produced by a hybridoma cell line termed 3-4, which was established through hybridization of an IgM-producing Epstein-Barr virus transformed human B-cell line termed No. 12, and a human myeloma cell line termed P109.
10871054	1	45	theme	cell	169:172	arg1	lines					174:178	cell lines	169:178	cell lines capable of producing an abundance of antibodies	169:226	Cell-cell hybridization is one method of establishing cell lines capable of producing an abundance of antibodies.
10871054	5	46	dep	galactosylated	967:980	arg1	biantennary					982:992	biantennary	982:992	biantennary	982:992	In both parental cells and hybridoma cells, the predominant structures at Asn171, Asn332, and N395 were fully galactosylated biantennary complex types, with or without core fucose and/or bisecting GlcNAc.
10871054	2	47	theme	cell-cell	314:322	arg1	hybridization					324:336	cell-cell hybridization	314:336	cell-cell hybridization	314:336	In order to clearly characterize antibodies produced by hybridomas, the influence of cell-cell hybridization on the glycosylation of produced antibodies should be studied.
10871054	5	48	from	Asn332	939:944	arg1	types					1002:1006	fully galactosylated biantennary complex types	961:1006	fully galactosylated biantennary complex types	961:1006	In both parental cells and hybridoma cells, the predominant structures at Asn171, Asn332, and N395 were fully galactosylated biantennary complex types, with or without core fucose and/or bisecting GlcNAc.
10871054	5	48	from	Asn332	939:944	arg1	structures					917:926	the predominant structures	901:926	the predominant structures at Asn171, Asn332, and N395	901:954	In both parental cells and hybridoma cells, the predominant structures at Asn171, Asn332, and N395 were fully galactosylated biantennary complex types, with or without core fucose and/or bisecting GlcNAc.
10871054	1	49	theme	capable	180:186	arg1	lines					174:178	cell lines	169:178	cell lines capable of producing an abundance of antibodies	169:226	Cell-cell hybridization is one method of establishing cell lines capable of producing an abundance of antibodies.
10871054	4	50	theme	parental	810:817	arg1	cells					826:830	parental No. 12 cells	810:830	parental No. 12 cells	810:830	We analyzed the structures of sugar chains on the constant region of the mu-chain of IgMs produced by parental No. 12 cells and hybridoma 3-4 cells.
10871054	6	51	theme	bisecting	1085:1093	arg1	GlcNAc					1095:1100	bisecting GlcNAc	1085:1100	bisecting GlcNAc	1085:1100	However, the amount of bisecting GlcNAc was markedly decreased in the hybridoma cells.
10871054	2	52	dep	characterize	249:260	arg1	to					238:239	to	238:239	to	238:239	In order to clearly characterize antibodies produced by hybridomas, the influence of cell-cell hybridization on the glycosylation of produced antibodies should be studied.
10871054	11	53	theme	sugar	1743:1747	arg1	structures					1755:1764	the sugar chain structures	1739:1764	the sugar chain structures of IgMs produced by the cells	1739:1794	Moreover, the sugar chain structures of IgMs produced by the cells reflected the level of GnT-III activity.
10871054	10	54	theme	P109	1717:1720	arg1	cells					1722:1726	P109 cells	1717:1726	P109 cells	1717:1726	The above results demonstrated a reduction in the intracellular activity of GnT-III in the hybridoma cells, which was largely due to the influence of P109 cells.
10871054	8	55	theme	P109	1421:1424	arg1	cells					1426:1430	P109 cells	1421:1430	P109 cells	1421:1430	No. 12 cells showed some GnT-III activity, whereas P109 cells showed no such activity.
10871054	10	56	theme	above	1571:1575	arg1	results					1577:1583	The above results	1567:1583	The above results	1567:1583	The above results demonstrated a reduction in the intracellular activity of GnT-III in the hybridoma cells, which was largely due to the influence of P109 cells.
10871054	11	57	theme	IgMs	1769:1772	arg1	structures					1755:1764	the sugar chain structures	1739:1764	the sugar chain structures of IgMs produced by the cells	1739:1794	Moreover, the sugar chain structures of IgMs produced by the cells reflected the level of GnT-III activity.
10871054	5	58	theme	core	1025:1028	arg1	fucose					1030:1035	core fucose	1025:1035	core fucose	1025:1035	In both parental cells and hybridoma cells, the predominant structures at Asn171, Asn332, and N395 were fully galactosylated biantennary complex types, with or without core fucose and/or bisecting GlcNAc.
10871054	4	59	theme	3-4	846:848	arg1	cells					850:854	hybridoma 3-4 cells	836:854	hybridoma 3-4 cells	836:854	We analyzed the structures of sugar chains on the constant region of the mu-chain of IgMs produced by parental No. 12 cells and hybridoma 3-4 cells.
10871054	8	60	theme	such	1442:1445	arg1	activity					1447:1454	no such activity	1439:1454	no such activity	1439:1454	No. 12 cells showed some GnT-III activity, whereas P109 cells showed no such activity.
10871054	7	61	theme	hybridoma	1353:1361	arg1	cells					1363:1367	hybridoma cells	1353:1367	hybridoma cells	1353:1367	Therefore, the activity of UDP-N-acetylglucosamine:beta-D-mannoside beta-1,4-N-acetylglucosaminyltransferase (GnT-III) responsible for the formation of bisecting GlcNAc was measured in parental cells and hybridoma cells.
10871054	5	62	theme	complex	994:1000	arg1	types					1002:1006	fully galactosylated biantennary complex types	961:1006	fully galactosylated biantennary complex types	961:1006	In both parental cells and hybridoma cells, the predominant structures at Asn171, Asn332, and N395 were fully galactosylated biantennary complex types, with or without core fucose and/or bisecting GlcNAc.
10871054	5	62	theme	complex	994:1000	arg1	structures					917:926	the predominant structures	901:926	the predominant structures at Asn171, Asn332, and N395	901:954	In both parental cells and hybridoma cells, the predominant structures at Asn171, Asn332, and N395 were fully galactosylated biantennary complex types, with or without core fucose and/or bisecting GlcNAc.
10871054	3	63	theme	virus	614:618	arg1	line					645:648	an IgM-producing Epstein-Barr virus transformed human B-cell line	584:648	an IgM-producing Epstein-Barr virus transformed human B-cell line termed No. 12	584:662	In this report, we describe structural changes of the N-glycans in immunoglobulin M (IgM) produced by a hybridoma cell line termed 3-4, which was established through hybridization of an IgM-producing Epstein-Barr virus transformed human B-cell line termed No. 12, and a human myeloma cell line termed P109.
10871054	9	64	theme	3-4	1515:1517	arg1	cells					1519:1523	hybridoma 3-4 cells	1505:1523	hybridoma 3-4 cells	1505:1523	The corresponding level of activity observed in hybridoma 3-4 cells was much lower than that in No. 12 cells.
10871054	4	65	theme	constant	758:765	arg1	region					767:772	the constant region	754:772	the constant region of the mu-chain of IgMs produced by parental No. 12 cells and hybridoma 3-4 cells	754:854	We analyzed the structures of sugar chains on the constant region of the mu-chain of IgMs produced by parental No. 12 cells and hybridoma 3-4 cells.
10871054	5	66	from	types	1002:1006	arg1	cells					874:878	parental cells	865:878	parental cells	865:878	In both parental cells and hybridoma cells, the predominant structures at Asn171, Asn332, and N395 were fully galactosylated biantennary complex types, with or without core fucose and/or bisecting GlcNAc.
10871054	5	66	from	types	1002:1006	arg1	cells					894:898	hybridoma cells	884:898	hybridoma cells	884:898	In both parental cells and hybridoma cells, the predominant structures at Asn171, Asn332, and N395 were fully galactosylated biantennary complex types, with or without core fucose and/or bisecting GlcNAc.
10871054	3	67	theme	IgM-producing	587:599	arg1	line					645:648	an IgM-producing Epstein-Barr virus transformed human B-cell line	584:648	an IgM-producing Epstein-Barr virus transformed human B-cell line termed No. 12	584:662	In this report, we describe structural changes of the N-glycans in immunoglobulin M (IgM) produced by a hybridoma cell line termed 3-4, which was established through hybridization of an IgM-producing Epstein-Barr virus transformed human B-cell line termed No. 12, and a human myeloma cell line termed P109.
10871054	4	68	from	region	767:772	arg1	structures					724:733	the structures	720:733	the structures of sugar chains on the constant region of the mu-chain of IgMs produced by parental No. 12 cells and hybridoma 3-4 cells	720:854	We analyzed the structures of sugar chains on the constant region of the mu-chain of IgMs produced by parental No. 12 cells and hybridoma 3-4 cells.
10871054	9	69	theme	activity	1484:1491	arg1	level					1475:1479	The corresponding level	1457:1479	The corresponding level of activity observed in hybridoma 3-4 cells	1457:1523	The corresponding level of activity observed in hybridoma 3-4 cells was much lower than that in No. 12 cells.
10871054	9	69	theme	activity	1484:1491	arg1	lower					1534:1538	lower	1534:1538	lower	1534:1538	The corresponding level of activity observed in hybridoma 3-4 cells was much lower than that in No. 12 cells.
10871054	1	70	theme	Cell-cell	115:123	arg1	hybridization					125:137	Cell-cell hybridization	115:137	Cell-cell hybridization	115:137	Cell-cell hybridization is one method of establishing cell lines capable of producing an abundance of antibodies.
10871054	4	71	from	chains	744:749	arg1	region					767:772	the constant region	754:772	the constant region of the mu-chain of IgMs produced by parental No. 12 cells and hybridoma 3-4 cells	754:854	We analyzed the structures of sugar chains on the constant region of the mu-chain of IgMs produced by parental No. 12 cells and hybridoma 3-4 cells.
10871054	5	72	theme	predominant	905:915	arg1	types					1002:1006	fully galactosylated biantennary complex types	961:1006	fully galactosylated biantennary complex types	961:1006	In both parental cells and hybridoma cells, the predominant structures at Asn171, Asn332, and N395 were fully galactosylated biantennary complex types, with or without core fucose and/or bisecting GlcNAc.
10871054	5	72	theme	predominant	905:915	arg1	structures					917:926	the predominant structures	901:926	the predominant structures at Asn171, Asn332, and N395	901:954	In both parental cells and hybridoma cells, the predominant structures at Asn171, Asn332, and N395 were fully galactosylated biantennary complex types, with or without core fucose and/or bisecting GlcNAc.
10871054	7	73	theme	GlcNAc	1311:1316	arg1	formation					1288:1296	the formation	1284:1296	the formation of bisecting GlcNAc	1284:1316	Therefore, the activity of UDP-N-acetylglucosamine:beta-D-mannoside beta-1,4-N-acetylglucosaminyltransferase (GnT-III) responsible for the formation of bisecting GlcNAc was measured in parental cells and hybridoma cells.
10871054	4	74	theme	chains	744:749	arg1	structures					724:733	the structures	720:733	the structures of sugar chains on the constant region of the mu-chain of IgMs produced by parental No. 12 cells and hybridoma 3-4 cells	720:854	We analyzed the structures of sugar chains on the constant region of the mu-chain of IgMs produced by parental No. 12 cells and hybridoma 3-4 cells.
10871054	5	75	theme	hybridoma	884:892	arg1	cells					894:898	hybridoma cells	884:898	hybridoma cells	884:898	In both parental cells and hybridoma cells, the predominant structures at Asn171, Asn332, and N395 were fully galactosylated biantennary complex types, with or without core fucose and/or bisecting GlcNAc.
10871054	3	76	theme	structural	429:438	arg1	changes					440:446	structural changes	429:446	structural changes of the N-glycans in immunoglobulin M (IgM) produced by a hybridoma cell line termed 3-4, which was established through hybridization of an IgM-producing Epstein-Barr virus transformed human B-cell line termed No. 12, and a human myeloma cell line termed P109	429:705	In this report, we describe structural changes of the N-glycans in immunoglobulin M (IgM) produced by a hybridoma cell line termed 3-4, which was established through hybridization of an IgM-producing Epstein-Barr virus transformed human B-cell line termed No. 12, and a human myeloma cell line termed P109.
10871054	3	77	theme	line	645:648	arg1	hybridization					567:579	hybridization	567:579	hybridization of an IgM-producing Epstein-Barr virus transformed human B-cell line termed No. 12, and a human myeloma cell line termed P109	567:705	In this report, we describe structural changes of the N-glycans in immunoglobulin M (IgM) produced by a hybridoma cell line termed 3-4, which was established through hybridization of an IgM-producing Epstein-Barr virus transformed human B-cell line termed No. 12, and a human myeloma cell line termed P109.
10871054	3	78	theme	immunoglobulin	468:481	arg1	IgM					486:488	IgM	486:488	IgM	486:488	In this report, we describe structural changes of the N-glycans in immunoglobulin M (IgM) produced by a hybridoma cell line termed 3-4, which was established through hybridization of an IgM-producing Epstein-Barr virus transformed human B-cell line termed No. 12, and a human myeloma cell line termed P109.
10871054	3	78	theme	immunoglobulin	468:481	arg1	M					483:483	immunoglobulin M	468:483	immunoglobulin M (IgM) produced by a hybridoma cell line termed 3-4, which was established through hybridization of an IgM-producing Epstein-Barr virus transformed human B-cell line termed No. 12, and a human myeloma cell line termed P109	468:705	In this report, we describe structural changes of the N-glycans in immunoglobulin M (IgM) produced by a hybridoma cell line termed 3-4, which was established through hybridization of an IgM-producing Epstein-Barr virus transformed human B-cell line termed No. 12, and a human myeloma cell line termed P109.
10871054	9	79	theme	No.	1553:1555	arg1	cells					1560:1564	No. 12 cells	1553:1564	No. 12 cells	1553:1564	The corresponding level of activity observed in hybridoma 3-4 cells was much lower than that in No. 12 cells.
10871054	7	80	theme	responsible	1268:1278	arg1	GnT-III					1259:1265	GnT-III	1259:1265	GnT-III	1259:1265	Therefore, the activity of UDP-N-acetylglucosamine:beta-D-mannoside beta-1,4-N-acetylglucosaminyltransferase (GnT-III) responsible for the formation of bisecting GlcNAc was measured in parental cells and hybridoma cells.
10871054	7	80	theme	responsible	1268:1278	arg1	beta-1,4-N-acetylglucosaminyltransferase					1217:1256	UDP-N-acetylglucosamine:beta-D-mannoside beta-1,4-N-acetylglucosaminyltransferase	1176:1256	UDP-N-acetylglucosamine:beta-D-mannoside beta-1,4-N-acetylglucosaminyltransferase (GnT-III) responsible for the formation of bisecting GlcNAc	1176:1316	Therefore, the activity of UDP-N-acetylglucosamine:beta-D-mannoside beta-1,4-N-acetylglucosaminyltransferase (GnT-III) responsible for the formation of bisecting GlcNAc was measured in parental cells and hybridoma cells.
10871054	3	81	theme	human	632:636	arg1	line					645:648	an IgM-producing Epstein-Barr virus transformed human B-cell line	584:648	an IgM-producing Epstein-Barr virus transformed human B-cell line termed No. 12	584:662	In this report, we describe structural changes of the N-glycans in immunoglobulin M (IgM) produced by a hybridoma cell line termed 3-4, which was established through hybridization of an IgM-producing Epstein-Barr virus transformed human B-cell line termed No. 12, and a human myeloma cell line termed P109.
10871054	8	82	theme	No.	1370:1372	arg1	cells					1377:1381	No. 12 cells	1370:1381	No. 12 cells	1370:1381	No. 12 cells showed some GnT-III activity, whereas P109 cells showed no such activity.
10871054	3	83	theme	N-glycans	455:463	arg1	changes					440:446	structural changes	429:446	structural changes of the N-glycans in immunoglobulin M (IgM) produced by a hybridoma cell line termed 3-4, which was established through hybridization of an IgM-producing Epstein-Barr virus transformed human B-cell line termed No. 12, and a human myeloma cell line termed P109	429:705	In this report, we describe structural changes of the N-glycans in immunoglobulin M (IgM) produced by a hybridoma cell line termed 3-4, which was established through hybridization of an IgM-producing Epstein-Barr virus transformed human B-cell line termed No. 12, and a human myeloma cell line termed P109.
10871054	0	84	theme	monoclonal	44:53	arg1	immunoglobulins					55:69	human monoclonal immunoglobulins	38:69	human monoclonal immunoglobulins	38:69	Comparative study of the N-glycans of human monoclonal immunoglobulins M produced by hybridoma and parental cells.
10871054	2	85	theme	antibodies	371:380	arg1	glycosylation					345:357	the glycosylation	341:357	the glycosylation of produced antibodies	341:380	In order to clearly characterize antibodies produced by hybridomas, the influence of cell-cell hybridization on the glycosylation of produced antibodies should be studied.
10871054	2	86	gly	glycosylation	345:357	arg1	antibodies					371:380	produced antibodies	362:380	produced antibodies	362:380	In order to clearly characterize antibodies produced by hybridomas, the influence of cell-cell hybridization on the glycosylation of produced antibodies should be studied.
10871054	10	87	theme	hybridoma	1658:1666	arg1	cells					1668:1672	the hybridoma cells	1654:1672	the hybridoma cells	1654:1672	The above results demonstrated a reduction in the intracellular activity of GnT-III in the hybridoma cells, which was largely due to the influence of P109 cells.
10871054	7	88	theme	beta-1,4-N-acetylglucosaminyltransferase	1217:1256	arg1	activity					1164:1171	the activity	1160:1171	the activity of UDP-N-acetylglucosamine:beta-D-mannoside beta-1,4-N-acetylglucosaminyltransferase (GnT-III) responsible for the formation of bisecting GlcNAc	1160:1316	Therefore, the activity of UDP-N-acetylglucosamine:beta-D-mannoside beta-1,4-N-acetylglucosaminyltransferase (GnT-III) responsible for the formation of bisecting GlcNAc was measured in parental cells and hybridoma cells.
10871054	2	89	theme	hybridization	324:336	arg1	influence					301:309	the influence	297:309	the influence of cell-cell hybridization on the glycosylation of produced antibodies	297:380	In order to clearly characterize antibodies produced by hybridomas, the influence of cell-cell hybridization on the glycosylation of produced antibodies should be studied.
10871054	0	90	dep	study	12:16	arg1	M					71:71	M	71:71	Comparative study of the N-glycans of human monoclonal immunoglobulins M	0:71	Comparative study of the N-glycans of human monoclonal immunoglobulins M produced by hybridoma and parental cells.
10871054	3	91	theme	myeloma	677:683	arg1	line					690:693	a human myeloma cell line	669:693	a human myeloma cell line termed P109	669:705	In this report, we describe structural changes of the N-glycans in immunoglobulin M (IgM) produced by a hybridoma cell line termed 3-4, which was established through hybridization of an IgM-producing Epstein-Barr virus transformed human B-cell line termed No. 12, and a human myeloma cell line termed P109.
10871054	3	92	from	changes	440:446	arg1	IgM					486:488	IgM	486:488	IgM	486:488	In this report, we describe structural changes of the N-glycans in immunoglobulin M (IgM) produced by a hybridoma cell line termed 3-4, which was established through hybridization of an IgM-producing Epstein-Barr virus transformed human B-cell line termed No. 12, and a human myeloma cell line termed P109.
10871054	3	92	from	changes	440:446	arg1	M					483:483	immunoglobulin M	468:483	immunoglobulin M (IgM) produced by a hybridoma cell line termed 3-4, which was established through hybridization of an IgM-producing Epstein-Barr virus transformed human B-cell line termed No. 12, and a human myeloma cell line termed P109	468:705	In this report, we describe structural changes of the N-glycans in immunoglobulin M (IgM) produced by a hybridoma cell line termed 3-4, which was established through hybridization of an IgM-producing Epstein-Barr virus transformed human B-cell line termed No. 12, and a human myeloma cell line termed P109.
10871054	3	93	theme	hybridoma	505:513	arg1	line					520:523	a hybridoma cell line	503:523	a hybridoma cell line	503:523	In this report, we describe structural changes of the N-glycans in immunoglobulin M (IgM) produced by a hybridoma cell line termed 3-4, which was established through hybridization of an IgM-producing Epstein-Barr virus transformed human B-cell line termed No. 12, and a human myeloma cell line termed P109.
9502801	4	0	theme	non-AD	705:710	arg1	controls					724:731	non-AD age-matched controls	705:731	non-AD age-matched controls	705:731	In this study, O-GlcNAc glycosylation of proteins from autopsied human brains with confirmed AD and non-AD age-matched controls was examined.
9502801	8	1	theme	neocortical	1249:1259	arg1	regions					1261:1267	brain neocortical regions	1243:1267	brain neocortical regions	1243:1267	The reduction is more evident in brain neocortical regions, and there appears to be a negative correlation between O-glycosylated AP-3 and the density of neurofibrillary tangles.
9502801	6	2	theme	proteins	983:990	arg1	number					953:958	The number	949:958	The number of O-GlcNAc-containing proteins	949:990	The number of O-GlcNAc-containing proteins and the overall O-GlcNAc level do not appear to be different between AD and control brain tissues.
9502801	6	2	theme	proteins	983:990	arg1	level					1017:1021	the overall O-GlcNAc level	996:1021	the overall O-GlcNAc level	996:1021	The number of O-GlcNAc-containing proteins and the overall O-GlcNAc level do not appear to be different between AD and control brain tissues.
9502801	6	2	theme	proteins	983:990	arg1	different					1043:1051	different	1043:1051	different	1043:1051	The number of O-GlcNAc-containing proteins and the overall O-GlcNAc level do not appear to be different between AD and control brain tissues.
9502801	3	3	theme	intracellular	520:532	arg1	proteins					534:541	intracellular proteins	520:541	intracellular proteins	520:541	Glycosylation with O-linked N-acetylglucosamine (O-GlcNAc) to serine and threonine residues is a dynamic protein modification of intracellular proteins, and it shares similar features with protein phosphorylation.
9502801	5	4	from	galactose	818:826	arg1	presence					835:842	the presence	831:842	the presence of galactosyltransferase	831:867	O-GlcNAcylation was demonstrated by labeling protein extracts with [3H]galactose in the presence of galactosyltransferase and subsequent analyses of saccharide-protein linkage and saccharide structure.
9502801	7	5	theme	assembly	1177:1184	arg1	protein-3					1186:1194	O-GlcNAcylated clathrin assembly protein-3	1153:1194	O-GlcNAcylated clathrin assembly protein-3 (AP-3)	1153:1201	The only significant change observed is a marked reduction of O-GlcNAcylated clathrin assembly protein-3 (AP-3) in AD.
9502801	7	5	theme	assembly	1177:1184	arg1	AP-3					1197:1200	AP-3	1197:1200	AP-3	1197:1200	The only significant change observed is a marked reduction of O-GlcNAcylated clathrin assembly protein-3 (AP-3) in AD.
9502801	0	6	link	O-linked	13:20	arg1	protein-3					60:68	O-linked N-acetylglucosamine-modified assembly protein-3	13:68	O-linked N-acetylglucosamine-modified assembly protein-3	13:68	Reduction of O-linked N-acetylglucosamine-modified assembly protein-3 in Alzheimer's disease.
9502801	2	7	theme	tau	306:308	arg1	protein					310:316	tau protein	306:316	tau protein	306:316	The role of phosphorylation in AD has been studied extensively because the presumed abnormal phosphorylation of tau protein is believed to play a role in the formation of paired helical filaments.
9502801	3	8	with	Glycosylation	391:403	arg1	O-GlcNAc					440:447	O-GlcNAc	440:447	O-GlcNAc	440:447	Glycosylation with O-linked N-acetylglucosamine (O-GlcNAc) to serine and threonine residues is a dynamic protein modification of intracellular proteins, and it shares similar features with protein phosphorylation.
9502801	3	8	with	Glycosylation	391:403	arg1	N-acetylglucosamine					419:437	O-linked N-acetylglucosamine	410:437	O-linked N-acetylglucosamine (O-GlcNAc)	410:448	Glycosylation with O-linked N-acetylglucosamine (O-GlcNAc) to serine and threonine residues is a dynamic protein modification of intracellular proteins, and it shares similar features with protein phosphorylation.
9502801	2	9	from	role	198:201	arg1	AD					225:226	AD	225:226	AD	225:226	The role of phosphorylation in AD has been studied extensively because the presumed abnormal phosphorylation of tau protein is believed to play a role in the formation of paired helical filaments.
9502801	6	10	theme	O-GlcNAc-containing	963:981	arg1	proteins					983:990	O-GlcNAc-containing proteins	963:990	O-GlcNAc-containing proteins	963:990	The number of O-GlcNAc-containing proteins and the overall O-GlcNAc level do not appear to be different between AD and control brain tissues.
9502801	7	11	theme	protein-3	1186:1194	arg1	reduction					1140:1148	a marked reduction	1131:1148	a marked reduction of O-GlcNAcylated clathrin assembly protein-3 (AP-3) in AD	1131:1207	The only significant change observed is a marked reduction of O-GlcNAcylated clathrin assembly protein-3 (AP-3) in AD.
9502801	7	11	theme	protein-3	1186:1194	arg1	change					1112:1117	The only significant change	1091:1117	The only significant change observed	1091:1126	The only significant change observed is a marked reduction of O-GlcNAcylated clathrin assembly protein-3 (AP-3) in AD.
9502801	4	12	gly	glycosylation	629:641	arg1	proteins					646:653	proteins	646:653	proteins from autopsied human brains	646:681	In this study, O-GlcNAc glycosylation of proteins from autopsied human brains with confirmed AD and non-AD age-matched controls was examined.
9502801	4	12	gly	glycosylation	629:641	arg1	study					613:617	this study	608:617	this study	608:617	In this study, O-GlcNAc glycosylation of proteins from autopsied human brains with confirmed AD and non-AD age-matched controls was examined.
9502801	3	13	theme	similar	558:564	arg1	features					566:573	similar features	558:573	similar features	558:573	Glycosylation with O-linked N-acetylglucosamine (O-GlcNAc) to serine and threonine residues is a dynamic protein modification of intracellular proteins, and it shares similar features with protein phosphorylation.
9502801	4	14	theme	age-matched	712:722	arg1	controls					724:731	non-AD age-matched controls	705:731	non-AD age-matched controls	705:731	In this study, O-GlcNAc glycosylation of proteins from autopsied human brains with confirmed AD and non-AD age-matched controls was examined.
9502801	7	15	theme	O-GlcNAcylated	1153:1166	arg1	protein-3					1186:1194	O-GlcNAcylated clathrin assembly protein-3	1153:1194	O-GlcNAcylated clathrin assembly protein-3 (AP-3)	1153:1201	The only significant change observed is a marked reduction of O-GlcNAcylated clathrin assembly protein-3 (AP-3) in AD.
9502801	7	15	theme	O-GlcNAcylated	1153:1166	arg1	AP-3					1197:1200	AP-3	1197:1200	AP-3	1197:1200	The only significant change observed is a marked reduction of O-GlcNAcylated clathrin assembly protein-3 (AP-3) in AD.
9502801	4	16	theme	proteins	646:653	arg1	glycosylation					629:641	O-GlcNAc glycosylation	620:641	O-GlcNAc glycosylation of proteins from autopsied human brains with confirmed AD and non-AD age-matched controls	620:731	In this study, O-GlcNAc glycosylation of proteins from autopsied human brains with confirmed AD and non-AD age-matched controls was examined.
9502801	5	17	theme	saccharide	927:936	arg1	structure					938:946	saccharide structure	927:946	saccharide structure	927:946	O-GlcNAcylation was demonstrated by labeling protein extracts with [3H]galactose in the presence of galactosyltransferase and subsequent analyses of saccharide-protein linkage and saccharide structure.
9502801	5	18	theme	linkage	915:921	arg1	analyses					884:891	subsequent analyses	873:891	subsequent analyses of saccharide-protein linkage and saccharide structure	873:946	O-GlcNAcylation was demonstrated by labeling protein extracts with [3H]galactose in the presence of galactosyltransferase and subsequent analyses of saccharide-protein linkage and saccharide structure.
9502801	5	19	from	presence	835:842	arg1	galactose					818:826	galactose	818:826	galactose	818:826	O-GlcNAcylation was demonstrated by labeling protein extracts with [3H]galactose in the presence of galactosyltransferase and subsequent analyses of saccharide-protein linkage and saccharide structure.
9502801	7	20	theme	clathrin	1168:1175	arg1	protein-3					1186:1194	O-GlcNAcylated clathrin assembly protein-3	1153:1194	O-GlcNAcylated clathrin assembly protein-3 (AP-3)	1153:1201	The only significant change observed is a marked reduction of O-GlcNAcylated clathrin assembly protein-3 (AP-3) in AD.
9502801	7	20	theme	clathrin	1168:1175	arg1	AP-3					1197:1200	AP-3	1197:1200	AP-3	1197:1200	The only significant change observed is a marked reduction of O-GlcNAcylated clathrin assembly protein-3 (AP-3) in AD.
9502801	8	21	gly	O-glycosylated	1325:1338	arg1	AP-3					1340:1343	O-glycosylated AP-3	1325:1343	O-glycosylated AP-3	1325:1343	The reduction is more evident in brain neocortical regions, and there appears to be a negative correlation between O-glycosylated AP-3 and the density of neurofibrillary tangles.
9502801	1	22	theme	Abnormal	94:101	arg1	processing					111:120	Abnormal protein processing	94:120	Abnormal protein processing	94:120	Abnormal protein processing and modification is associated with Alzheimer's disease (AD) pathology.
9502801	9	23	theme	O-glycosylated	1443:1456	arg1	AP-3					1458:1461	the O-glycosylated AP-3	1439:1461	the O-glycosylated AP-3	1439:1461	These data suggest a possible association between the O-glycosylated AP-3 and AD pathology.
9502801	8	24	from	regions	1261:1267	arg1	reduction					1214:1222	The reduction	1210:1222	The reduction	1210:1222	The reduction is more evident in brain neocortical regions, and there appears to be a negative correlation between O-glycosylated AP-3 and the density of neurofibrillary tangles.
9502801	8	24	from	regions	1261:1267	arg1	evident					1232:1238	evident	1232:1238	evident	1232:1238	The reduction is more evident in brain neocortical regions, and there appears to be a negative correlation between O-glycosylated AP-3 and the density of neurofibrillary tangles.
9502801	8	24	from	regions	1261:1267	arg1	correlation					1305:1315	a negative correlation	1294:1315	a negative correlation between O-glycosylated AP-3 and the density of neurofibrillary tangles	1294:1386	The reduction is more evident in brain neocortical regions, and there appears to be a negative correlation between O-glycosylated AP-3 and the density of neurofibrillary tangles.
9502801	1	25	theme	protein	103:109	arg1	processing					111:120	Abnormal protein processing	94:120	Abnormal protein processing	94:120	Abnormal protein processing and modification is associated with Alzheimer's disease (AD) pathology.
9502801	4	26	from	brains	676:681	arg1	proteins					646:653	proteins	646:653	proteins from autopsied human brains	646:681	In this study, O-GlcNAc glycosylation of proteins from autopsied human brains with confirmed AD and non-AD age-matched controls was examined.
9502801	4	26	from	brains	676:681	arg1	glycosylation					629:641	O-GlcNAc glycosylation	620:641	O-GlcNAc glycosylation of proteins from autopsied human brains with confirmed AD and non-AD age-matched controls	620:731	In this study, O-GlcNAc glycosylation of proteins from autopsied human brains with confirmed AD and non-AD age-matched controls was examined.
9502801	2	27	theme	filaments	380:388	arg1	formation					352:360	the formation	348:360	the formation of paired helical filaments	348:388	The role of phosphorylation in AD has been studied extensively because the presumed abnormal phosphorylation of tau protein is believed to play a role in the formation of paired helical filaments.
9502801	7	28	from	reduction	1140:1148	arg1	AD					1206:1207	AD	1206:1207	AD	1206:1207	The only significant change observed is a marked reduction of O-GlcNAcylated clathrin assembly protein-3 (AP-3) in AD.
9502801	6	29	theme	overall	1000:1006	arg1	level					1017:1021	the overall O-GlcNAc level	996:1021	the overall O-GlcNAc level	996:1021	The number of O-GlcNAc-containing proteins and the overall O-GlcNAc level do not appear to be different between AD and control brain tissues.
9502801	6	29	theme	overall	1000:1006	arg1	different					1043:1051	different	1043:1051	different	1043:1051	The number of O-GlcNAc-containing proteins and the overall O-GlcNAc level do not appear to be different between AD and control brain tissues.
9502801	8	30	theme	negative	1296:1303	arg1	correlation					1305:1315	a negative correlation	1294:1315	a negative correlation between O-glycosylated AP-3 and the density of neurofibrillary tangles	1294:1386	The reduction is more evident in brain neocortical regions, and there appears to be a negative correlation between O-glycosylated AP-3 and the density of neurofibrillary tangles.
9502801	8	30	theme	negative	1296:1303	arg1	evident					1232:1238	evident	1232:1238	evident	1232:1238	The reduction is more evident in brain neocortical regions, and there appears to be a negative correlation between O-glycosylated AP-3 and the density of neurofibrillary tangles.
9502801	8	30	theme	negative	1296:1303	arg1	reduction					1214:1222	The reduction	1210:1222	The reduction	1210:1222	The reduction is more evident in brain neocortical regions, and there appears to be a negative correlation between O-glycosylated AP-3 and the density of neurofibrillary tangles.
9502801	2	31	theme	helical	372:378	arg1	filaments					380:388	paired helical filaments	365:388	paired helical filaments	365:388	The role of phosphorylation in AD has been studied extensively because the presumed abnormal phosphorylation of tau protein is believed to play a role in the formation of paired helical filaments.
9502801	0	32	theme	N-acetylglucosamine-modified	22:49	arg1	protein-3					60:68	O-linked N-acetylglucosamine-modified assembly protein-3	13:68	O-linked N-acetylglucosamine-modified assembly protein-3	13:68	Reduction of O-linked N-acetylglucosamine-modified assembly protein-3 in Alzheimer's disease.
9502801	8	33	theme	tangles	1380:1386	arg1	AP-3					1340:1343	O-glycosylated AP-3	1325:1343	O-glycosylated AP-3	1325:1343	The reduction is more evident in brain neocortical regions, and there appears to be a negative correlation between O-glycosylated AP-3 and the density of neurofibrillary tangles.
9502801	8	33	theme	tangles	1380:1386	arg1	density					1353:1359	the density	1349:1359	the density of neurofibrillary tangles	1349:1386	The reduction is more evident in brain neocortical regions, and there appears to be a negative correlation between O-glycosylated AP-3 and the density of neurofibrillary tangles.
9502801	5	34	theme	subsequent	873:882	arg1	analyses					884:891	subsequent analyses	873:891	subsequent analyses of saccharide-protein linkage and saccharide structure	873:946	O-GlcNAcylation was demonstrated by labeling protein extracts with [3H]galactose in the presence of galactosyltransferase and subsequent analyses of saccharide-protein linkage and saccharide structure.
9502801	0	35	theme	O-linked	13:20	arg1	protein-3					60:68	O-linked N-acetylglucosamine-modified assembly protein-3	13:68	O-linked N-acetylglucosamine-modified assembly protein-3	13:68	Reduction of O-linked N-acetylglucosamine-modified assembly protein-3 in Alzheimer's disease.
9502801	7	36	theme	marked	1133:1138	arg1	reduction					1140:1148	a marked reduction	1131:1148	a marked reduction of O-GlcNAcylated clathrin assembly protein-3 (AP-3) in AD	1131:1207	The only significant change observed is a marked reduction of O-GlcNAcylated clathrin assembly protein-3 (AP-3) in AD.
9502801	7	36	theme	marked	1133:1138	arg1	change					1112:1117	The only significant change	1091:1117	The only significant change observed	1091:1126	The only significant change observed is a marked reduction of O-GlcNAcylated clathrin assembly protein-3 (AP-3) in AD.
9502801	8	37	from	evident	1232:1238	arg1	regions					1261:1267	brain neocortical regions	1243:1267	brain neocortical regions	1243:1267	The reduction is more evident in brain neocortical regions, and there appears to be a negative correlation between O-glycosylated AP-3 and the density of neurofibrillary tangles.
9502801	2	38	theme	protein	310:316	arg1	phosphorylation					287:301	the presumed abnormal phosphorylation	265:301	the presumed abnormal phosphorylation of tau protein	265:316	The role of phosphorylation in AD has been studied extensively because the presumed abnormal phosphorylation of tau protein is believed to play a role in the formation of paired helical filaments.
9502801	2	39	theme	paired	365:370	arg1	filaments					380:388	paired helical filaments	365:388	paired helical filaments	365:388	The role of phosphorylation in AD has been studied extensively because the presumed abnormal phosphorylation of tau protein is believed to play a role in the formation of paired helical filaments.
9502801	0	40	theme	protein-3	60:68	arg1	Reduction					0:8	Reduction	0:8	Reduction of O-linked N-acetylglucosamine-modified assembly protein-3 in Alzheimer's disease	0:91	Reduction of O-linked N-acetylglucosamine-modified assembly protein-3 in Alzheimer's disease.
9502801	4	41	theme	human	670:674	arg1	brains					676:681	autopsied human brains	660:681	autopsied human brains	660:681	In this study, O-GlcNAc glycosylation of proteins from autopsied human brains with confirmed AD and non-AD age-matched controls was examined.
9502801	8	42	theme	neurofibrillary	1364:1378	arg1	tangles					1380:1386	neurofibrillary tangles	1364:1386	neurofibrillary tangles	1364:1386	The reduction is more evident in brain neocortical regions, and there appears to be a negative correlation between O-glycosylated AP-3 and the density of neurofibrillary tangles.
9502801	4	43	theme	confirmed	688:696	arg1	AD					698:699	confirmed AD	688:699	confirmed AD	688:699	In this study, O-GlcNAc glycosylation of proteins from autopsied human brains with confirmed AD and non-AD age-matched controls was examined.
9502801	3	44	mod	modification	504:515	arg3	protein					496:502	a dynamic protein modification	486:515	a dynamic protein modification of intracellular proteins	486:541	Glycosylation with O-linked N-acetylglucosamine (O-GlcNAc) to serine and threonine residues is a dynamic protein modification of intracellular proteins, and it shares similar features with protein phosphorylation.
9502801	3	44	mod	modification	504:515	arg1	proteins					534:541	intracellular proteins	520:541	intracellular proteins	520:541	Glycosylation with O-linked N-acetylglucosamine (O-GlcNAc) to serine and threonine residues is a dynamic protein modification of intracellular proteins, and it shares similar features with protein phosphorylation.
9502801	0	45	theme	assembly	51:58	arg1	protein-3					60:68	O-linked N-acetylglucosamine-modified assembly protein-3	13:68	O-linked N-acetylglucosamine-modified assembly protein-3	13:68	Reduction of O-linked N-acetylglucosamine-modified assembly protein-3 in Alzheimer's disease.
9502801	9	46	theme	possible	1410:1417	arg1	association					1419:1429	a possible association	1408:1429	a possible association between the O-glycosylated AP-3 and AD pathology	1408:1478	These data suggest a possible association between the O-glycosylated AP-3 and AD pathology.
9502801	8	47	theme	O-glycosylated	1325:1338	arg1	AP-3					1340:1343	O-glycosylated AP-3	1325:1343	O-glycosylated AP-3	1325:1343	The reduction is more evident in brain neocortical regions, and there appears to be a negative correlation between O-glycosylated AP-3 and the density of neurofibrillary tangles.
9502801	3	48	link	O-linked	410:417	arg1	O-GlcNAc					440:447	O-GlcNAc	440:447	O-GlcNAc	440:447	Glycosylation with O-linked N-acetylglucosamine (O-GlcNAc) to serine and threonine residues is a dynamic protein modification of intracellular proteins, and it shares similar features with protein phosphorylation.
9502801	3	48	link	O-linked	410:417	arg1	N-acetylglucosamine					419:437	O-linked N-acetylglucosamine	410:437	O-linked N-acetylglucosamine (O-GlcNAc)	410:448	Glycosylation with O-linked N-acetylglucosamine (O-GlcNAc) to serine and threonine residues is a dynamic protein modification of intracellular proteins, and it shares similar features with protein phosphorylation.
9502801	4	49	theme	autopsied	660:668	arg1	brains					676:681	autopsied human brains	660:681	autopsied human brains	660:681	In this study, O-GlcNAc glycosylation of proteins from autopsied human brains with confirmed AD and non-AD age-matched controls was examined.
9502801	7	50	theme	significant	1100:1110	arg1	reduction					1140:1148	a marked reduction	1131:1148	a marked reduction of O-GlcNAcylated clathrin assembly protein-3 (AP-3) in AD	1131:1207	The only significant change observed is a marked reduction of O-GlcNAcylated clathrin assembly protein-3 (AP-3) in AD.
9502801	7	50	theme	significant	1100:1110	arg1	change					1112:1117	The only significant change	1091:1117	The only significant change observed	1091:1126	The only significant change observed is a marked reduction of O-GlcNAcylated clathrin assembly protein-3 (AP-3) in AD.
9502801	5	51	theme	galactosyltransferase	847:867	arg1	presence					835:842	the presence	831:842	the presence of galactosyltransferase	831:867	O-GlcNAcylation was demonstrated by labeling protein extracts with [3H]galactose in the presence of galactosyltransferase and subsequent analyses of saccharide-protein linkage and saccharide structure.
9502801	3	52	theme	protein	496:502	arg1	modification					504:515	a dynamic protein modification	486:515	a dynamic protein modification of intracellular proteins	486:541	Glycosylation with O-linked N-acetylglucosamine (O-GlcNAc) to serine and threonine residues is a dynamic protein modification of intracellular proteins, and it shares similar features with protein phosphorylation.
9502801	3	52	theme	protein	496:502	arg1	Glycosylation					391:403	Glycosylation	391:403	Glycosylation with O-linked N-acetylglucosamine (O-GlcNAc) to serine and threonine residues	391:481	Glycosylation with O-linked N-acetylglucosamine (O-GlcNAc) to serine and threonine residues is a dynamic protein modification of intracellular proteins, and it shares similar features with protein phosphorylation.
9502801	3	53	theme	O-linked	410:417	arg1	O-GlcNAc					440:447	O-GlcNAc	440:447	O-GlcNAc	440:447	Glycosylation with O-linked N-acetylglucosamine (O-GlcNAc) to serine and threonine residues is a dynamic protein modification of intracellular proteins, and it shares similar features with protein phosphorylation.
9502801	3	53	theme	O-linked	410:417	arg1	N-acetylglucosamine					419:437	O-linked N-acetylglucosamine	410:437	O-linked N-acetylglucosamine (O-GlcNAc)	410:448	Glycosylation with O-linked N-acetylglucosamine (O-GlcNAc) to serine and threonine residues is a dynamic protein modification of intracellular proteins, and it shares similar features with protein phosphorylation.
9502801	6	54	theme	O-GlcNAc	1008:1015	arg1	level					1017:1021	the overall O-GlcNAc level	996:1021	the overall O-GlcNAc level	996:1021	The number of O-GlcNAc-containing proteins and the overall O-GlcNAc level do not appear to be different between AD and control brain tissues.
9502801	6	54	theme	O-GlcNAc	1008:1015	arg1	different					1043:1051	different	1043:1051	different	1043:1051	The number of O-GlcNAc-containing proteins and the overall O-GlcNAc level do not appear to be different between AD and control brain tissues.
9502801	3	55	dep	serine	453:458	arg1	residues					474:481	residues	474:481	residues	474:481	Glycosylation with O-linked N-acetylglucosamine (O-GlcNAc) to serine and threonine residues is a dynamic protein modification of intracellular proteins, and it shares similar features with protein phosphorylation.
9502801	3	56	theme	protein	580:586	arg1	phosphorylation					588:602	protein phosphorylation	580:602	protein phosphorylation	580:602	Glycosylation with O-linked N-acetylglucosamine (O-GlcNAc) to serine and threonine residues is a dynamic protein modification of intracellular proteins, and it shares similar features with protein phosphorylation.
9502801	2	57	theme	phosphorylation	206:220	arg1	role					198:201	The role	194:201	The role of phosphorylation in AD	194:226	The role of phosphorylation in AD has been studied extensively because the presumed abnormal phosphorylation of tau protein is believed to play a role in the formation of paired helical filaments.
9502801	2	58	theme	presumed	269:276	arg1	phosphorylation					287:301	the presumed abnormal phosphorylation	265:301	the presumed abnormal phosphorylation of tau protein	265:316	The role of phosphorylation in AD has been studied extensively because the presumed abnormal phosphorylation of tau protein is believed to play a role in the formation of paired helical filaments.
9502801	4	59	with	glycosylation	629:641	arg1	controls					724:731	non-AD age-matched controls	705:731	non-AD age-matched controls	705:731	In this study, O-GlcNAc glycosylation of proteins from autopsied human brains with confirmed AD and non-AD age-matched controls was examined.
9502801	4	59	with	glycosylation	629:641	arg1	AD					698:699	confirmed AD	688:699	confirmed AD	688:699	In this study, O-GlcNAc glycosylation of proteins from autopsied human brains with confirmed AD and non-AD age-matched controls was examined.
9502801	5	60	theme	structure	938:946	arg1	analyses					884:891	subsequent analyses	873:891	subsequent analyses of saccharide-protein linkage and saccharide structure	873:946	O-GlcNAcylation was demonstrated by labeling protein extracts with [3H]galactose in the presence of galactosyltransferase and subsequent analyses of saccharide-protein linkage and saccharide structure.
9502801	4	61	theme	O-GlcNAc	620:627	arg1	glycosylation					629:641	O-GlcNAc glycosylation	620:641	O-GlcNAc glycosylation of proteins from autopsied human brains with confirmed AD and non-AD age-matched controls	620:731	In this study, O-GlcNAc glycosylation of proteins from autopsied human brains with confirmed AD and non-AD age-matched controls was examined.
9502801	2	62	theme	abnormal	278:285	arg1	phosphorylation					287:301	the presumed abnormal phosphorylation	265:301	the presumed abnormal phosphorylation of tau protein	265:316	The role of phosphorylation in AD has been studied extensively because the presumed abnormal phosphorylation of tau protein is believed to play a role in the formation of paired helical filaments.
9502801	6	63	dep	AD	1061:1062	arg1	tissues					1082:1088	brain tissues	1076:1088	brain tissues	1076:1088	The number of O-GlcNAc-containing proteins and the overall O-GlcNAc level do not appear to be different between AD and control brain tissues.
9502801	3	64	theme	dynamic	488:494	arg1	modification					504:515	a dynamic protein modification	486:515	a dynamic protein modification of intracellular proteins	486:541	Glycosylation with O-linked N-acetylglucosamine (O-GlcNAc) to serine and threonine residues is a dynamic protein modification of intracellular proteins, and it shares similar features with protein phosphorylation.
9502801	3	64	theme	dynamic	488:494	arg1	Glycosylation					391:403	Glycosylation	391:403	Glycosylation with O-linked N-acetylglucosamine (O-GlcNAc) to serine and threonine residues	391:481	Glycosylation with O-linked N-acetylglucosamine (O-GlcNAc) to serine and threonine residues is a dynamic protein modification of intracellular proteins, and it shares similar features with protein phosphorylation.
9502801	5	65	theme	protein	792:798	arg1	extracts					800:807	protein extracts	792:807	protein extracts	792:807	O-GlcNAcylation was demonstrated by labeling protein extracts with [3H]galactose in the presence of galactosyltransferase and subsequent analyses of saccharide-protein linkage and saccharide structure.
9502801	5	66	theme	saccharide-protein	896:913	arg1	linkage					915:921	saccharide-protein linkage	896:921	saccharide-protein linkage	896:921	O-GlcNAcylation was demonstrated by labeling protein extracts with [3H]galactose in the presence of galactosyltransferase and subsequent analyses of saccharide-protein linkage and saccharide structure.
9502801	3	67	theme	proteins	534:541	arg1	modification					504:515	a dynamic protein modification	486:515	a dynamic protein modification of intracellular proteins	486:541	Glycosylation with O-linked N-acetylglucosamine (O-GlcNAc) to serine and threonine residues is a dynamic protein modification of intracellular proteins, and it shares similar features with protein phosphorylation.
9502801	3	67	theme	proteins	534:541	arg1	Glycosylation					391:403	Glycosylation	391:403	Glycosylation with O-linked N-acetylglucosamine (O-GlcNAc) to serine and threonine residues	391:481	Glycosylation with O-linked N-acetylglucosamine (O-GlcNAc) to serine and threonine residues is a dynamic protein modification of intracellular proteins, and it shares similar features with protein phosphorylation.
9502801	6	68	theme	brain	1076:1080	arg1	tissues					1082:1088	brain tissues	1076:1088	brain tissues	1076:1088	The number of O-GlcNAc-containing proteins and the overall O-GlcNAc level do not appear to be different between AD and control brain tissues.
9502801	4	69	from	glycosylation	629:641	arg1	brains					676:681	autopsied human brains	660:681	autopsied human brains	660:681	In this study, O-GlcNAc glycosylation of proteins from autopsied human brains with confirmed AD and non-AD age-matched controls was examined.
9502801	8	70	theme	brain	1243:1247	arg1	regions					1261:1267	brain neocortical regions	1243:1267	brain neocortical regions	1243:1267	The reduction is more evident in brain neocortical regions, and there appears to be a negative correlation between O-glycosylated AP-3 and the density of neurofibrillary tangles.
9502801	1	71	theme	disease	170:176	arg1	pathology					183:191	Alzheimer's disease (AD) pathology	158:191	Alzheimer's disease (AD) pathology	158:191	Abnormal protein processing and modification is associated with Alzheimer's disease (AD) pathology.
9502801	9	72	gly	O-glycosylated	1443:1456	arg1	AP-3					1458:1461	the O-glycosylated AP-3	1439:1461	the O-glycosylated AP-3	1439:1461	These data suggest a possible association between the O-glycosylated AP-3 and AD pathology.
9502801	9	73	theme	AD	1467:1468	arg1	pathology					1470:1478	AD pathology	1467:1478	AD pathology	1467:1478	These data suggest a possible association between the O-glycosylated AP-3 and AD pathology.
7655165	1	0	theme	significant	244:254	arg1	quantity					256:263	a significant quantity	242:263	a significant quantity of free glycoasparagines	242:288	During a systematic study of carbohydrate material present in human meconium, in addition to the previously described mucins, glycolipids and free oligosaccharides, we have now characterized a significant quantity of free glycoasparagines.
7655165	3	1	theme	MHz	517:519	arg1	spectroscopy					528:539	400 MHz 1H-NMR spectroscopy	513:539	400 MHz 1H-NMR spectroscopy	513:539	Their structures have been established by 400 MHz 1H-NMR spectroscopy.
7655165	4	2	theme	gastrointestinal	774:789	arg1	proteins					802:809	fetal gastrointestinal N-glycosyl proteins	768:809	fetal gastrointestinal N-glycosyl proteins	768:809	These compounds are related to N-acetyllactosaminic type structures and are based on the common core: [formula: see text] These glycoasparagines are probably derived from both protease and partial exoglycosidase hydrolysis of fetal gastrointestinal N-glycosyl proteins.
7655165	4	3	theme	exoglycosidase	739:752	arg1	hydrolysis					754:763	partial exoglycosidase hydrolysis	731:763	partial exoglycosidase hydrolysis	731:763	These compounds are related to N-acetyllactosaminic type structures and are based on the common core: [formula: see text] These glycoasparagines are probably derived from both protease and partial exoglycosidase hydrolysis of fetal gastrointestinal N-glycosyl proteins.
7655165	4	4	theme	fetal	768:772	arg1	proteins					802:809	fetal gastrointestinal N-glycosyl proteins	768:809	fetal gastrointestinal N-glycosyl proteins	768:809	These compounds are related to N-acetyllactosaminic type structures and are based on the common core: [formula: see text] These glycoasparagines are probably derived from both protease and partial exoglycosidase hydrolysis of fetal gastrointestinal N-glycosyl proteins.
7655165	1	5	theme	systematic	60:69	arg1	study					71:75	a systematic study	58:75	a systematic study of carbohydrate material present in human meconium	58:126	During a systematic study of carbohydrate material present in human meconium, in addition to the previously described mucins, glycolipids and free oligosaccharides, we have now characterized a significant quantity of free glycoasparagines.
7655165	5	6	theme	pathways	881:888	arg1	context					850:856	the context	846:856	the context of the known catabolic pathways of N-glycans	846:901	Their structures are discussed in the context of the known catabolic pathways of N-glycans.
7655165	4	7	theme	partial	731:737	arg1	hydrolysis					754:763	partial exoglycosidase hydrolysis	731:763	partial exoglycosidase hydrolysis	731:763	These compounds are related to N-acetyllactosaminic type structures and are based on the common core: [formula: see text] These glycoasparagines are probably derived from both protease and partial exoglycosidase hydrolysis of fetal gastrointestinal N-glycosyl proteins.
7655165	2	8	theme	-affinity	408:416	arg1	combination					358:368	a combination	356:368	a combination of ion-exchange, concanavalin A (ConA)-affinity and high-performance liquid (HPLC) chromatographies	356:468	These glycoasparagines have been isolated from human meconium by a combination of ion-exchange, concanavalin A (ConA)-affinity and high-performance liquid (HPLC) chromatographies.
7655165	4	9	theme	proteins	802:809	arg1	hydrolysis					754:763	partial exoglycosidase hydrolysis	731:763	partial exoglycosidase hydrolysis	731:763	These compounds are related to N-acetyllactosaminic type structures and are based on the common core: [formula: see text] These glycoasparagines are probably derived from both protease and partial exoglycosidase hydrolysis of fetal gastrointestinal N-glycosyl proteins.
7655165	4	9	theme	proteins	802:809	arg1	protease					718:725	protease	718:725	protease	718:725	These compounds are related to N-acetyllactosaminic type structures and are based on the common core: [formula: see text] These glycoasparagines are probably derived from both protease and partial exoglycosidase hydrolysis of fetal gastrointestinal N-glycosyl proteins.
7655165	5	10	theme	N-glycans	893:901	arg1	pathways					881:888	the known catabolic pathways	861:888	the known catabolic pathways of N-glycans	861:901	Their structures are discussed in the context of the known catabolic pathways of N-glycans.
7655165	1	11	theme	described	159:167	arg1	glycolipids					177:187	glycolipids	177:187	glycolipids	177:187	During a systematic study of carbohydrate material present in human meconium, in addition to the previously described mucins, glycolipids and free oligosaccharides, we have now characterized a significant quantity of free glycoasparagines.
7655165	1	11	theme	described	159:167	arg1	oligosaccharides					198:213	free oligosaccharides	193:213	free oligosaccharides	193:213	During a systematic study of carbohydrate material present in human meconium, in addition to the previously described mucins, glycolipids and free oligosaccharides, we have now characterized a significant quantity of free glycoasparagines.
7655165	1	11	theme	described	159:167	arg1	mucins					169:174	the previously described mucins	144:174	the previously described mucins	144:174	During a systematic study of carbohydrate material present in human meconium, in addition to the previously described mucins, glycolipids and free oligosaccharides, we have now characterized a significant quantity of free glycoasparagines.
7655165	4	12	theme	N-glycosyl	791:800	arg1	proteins					802:809	fetal gastrointestinal N-glycosyl proteins	768:809	fetal gastrointestinal N-glycosyl proteins	768:809	These compounds are related to N-acetyllactosaminic type structures and are based on the common core: [formula: see text] These glycoasparagines are probably derived from both protease and partial exoglycosidase hydrolysis of fetal gastrointestinal N-glycosyl proteins.
7655165	2	13	theme	A	400:400	arg1	-affinity					408:416	concanavalin A (ConA)-affinity	387:416	concanavalin A (ConA)-affinity	387:416	These glycoasparagines have been isolated from human meconium by a combination of ion-exchange, concanavalin A (ConA)-affinity and high-performance liquid (HPLC) chromatographies.
7655165	2	14	theme	HPLC	447:450	arg1	chromatographies					453:468	high-performance liquid (HPLC) chromatographies	422:468	high-performance liquid (HPLC) chromatographies	422:468	These glycoasparagines have been isolated from human meconium by a combination of ion-exchange, concanavalin A (ConA)-affinity and high-performance liquid (HPLC) chromatographies.
7655165	4	15	attach	derived	700:706	arg1	hydrolysis					754:763	partial exoglycosidase hydrolysis	731:763	partial exoglycosidase hydrolysis	731:763	These compounds are related to N-acetyllactosaminic type structures and are based on the common core: [formula: see text] These glycoasparagines are probably derived from both protease and partial exoglycosidase hydrolysis of fetal gastrointestinal N-glycosyl proteins.
7655165	4	15	attach	derived	700:706	arg2	glycoasparagines					670:685	These glycoasparagines	664:685	These glycoasparagines	664:685	These compounds are related to N-acetyllactosaminic type structures and are based on the common core: [formula: see text] These glycoasparagines are probably derived from both protease and partial exoglycosidase hydrolysis of fetal gastrointestinal N-glycosyl proteins.
7655165	4	15	attach	derived	700:706	arg1	protease					718:725	protease	718:725	protease	718:725	These compounds are related to N-acetyllactosaminic type structures and are based on the common core: [formula: see text] These glycoasparagines are probably derived from both protease and partial exoglycosidase hydrolysis of fetal gastrointestinal N-glycosyl proteins.
7655165	1	16	theme	carbohydrate	80:91	arg1	material					93:100	carbohydrate material	80:100	carbohydrate material present in human meconium	80:126	During a systematic study of carbohydrate material present in human meconium, in addition to the previously described mucins, glycolipids and free oligosaccharides, we have now characterized a significant quantity of free glycoasparagines.
7655165	2	17	theme	concanavalin	387:398	arg1	A					400:400	concanavalin A	387:400	concanavalin A (ConA)-affinity	387:416	These glycoasparagines have been isolated from human meconium by a combination of ion-exchange, concanavalin A (ConA)-affinity and high-performance liquid (HPLC) chromatographies.
7655165	2	17	theme	concanavalin	387:398	arg1	ConA					403:406	ConA	403:406	ConA	403:406	These glycoasparagines have been isolated from human meconium by a combination of ion-exchange, concanavalin A (ConA)-affinity and high-performance liquid (HPLC) chromatographies.
7655165	0	18	theme	First	0:4	arg1	evidence					6:13	First evidence	0:13	First evidence of human meconium glycoasparagines	0:48	First evidence of human meconium glycoasparagines.
7655165	1	19	theme	free	268:271	arg1	glycoasparagines					273:288	free glycoasparagines	268:288	free glycoasparagines	268:288	During a systematic study of carbohydrate material present in human meconium, in addition to the previously described mucins, glycolipids and free oligosaccharides, we have now characterized a significant quantity of free glycoasparagines.
7655165	1	20	theme	material	93:100	arg1	study					71:75	a systematic study	58:75	a systematic study of carbohydrate material present in human meconium	58:126	During a systematic study of carbohydrate material present in human meconium, in addition to the previously described mucins, glycolipids and free oligosaccharides, we have now characterized a significant quantity of free glycoasparagines.
7655165	0	21	theme	human	18:22	arg1	glycoasparagines					33:48	human meconium glycoasparagines	18:48	human meconium glycoasparagines	18:48	First evidence of human meconium glycoasparagines.
7655165	1	22	theme	glycoasparagines	273:288	arg1	quantity					256:263	a significant quantity	242:263	a significant quantity of free glycoasparagines	242:288	During a systematic study of carbohydrate material present in human meconium, in addition to the previously described mucins, glycolipids and free oligosaccharides, we have now characterized a significant quantity of free glycoasparagines.
7655165	1	23	from	meconium	119:126	arg1	present					102:108	present	102:108	present	102:108	During a systematic study of carbohydrate material present in human meconium, in addition to the previously described mucins, glycolipids and free oligosaccharides, we have now characterized a significant quantity of free glycoasparagines.
7655165	1	24	theme	present	102:108	arg1	material					93:100	carbohydrate material	80:100	carbohydrate material present in human meconium	80:126	During a systematic study of carbohydrate material present in human meconium, in addition to the previously described mucins, glycolipids and free oligosaccharides, we have now characterized a significant quantity of free glycoasparagines.
7655165	2	25	theme	high-performance	422:437	arg1	chromatographies					453:468	high-performance liquid (HPLC) chromatographies	422:468	high-performance liquid (HPLC) chromatographies	422:468	These glycoasparagines have been isolated from human meconium by a combination of ion-exchange, concanavalin A (ConA)-affinity and high-performance liquid (HPLC) chromatographies.
7655165	4	26	theme	N-acetyllactosaminic	573:592	arg1	structures					599:608	N-acetyllactosaminic type structures	573:608	N-acetyllactosaminic type structures	573:608	These compounds are related to N-acetyllactosaminic type structures and are based on the common core: [formula: see text] These glycoasparagines are probably derived from both protease and partial exoglycosidase hydrolysis of fetal gastrointestinal N-glycosyl proteins.
7655165	1	27	theme	free	193:196	arg1	oligosaccharides					198:213	free oligosaccharides	193:213	free oligosaccharides	193:213	During a systematic study of carbohydrate material present in human meconium, in addition to the previously described mucins, glycolipids and free oligosaccharides, we have now characterized a significant quantity of free glycoasparagines.
7655165	1	27	theme	free	193:196	arg1	mucins					169:174	the previously described mucins	144:174	the previously described mucins	144:174	During a systematic study of carbohydrate material present in human meconium, in addition to the previously described mucins, glycolipids and free oligosaccharides, we have now characterized a significant quantity of free glycoasparagines.
7655165	0	28	theme	glycoasparagines	33:48	arg1	evidence					6:13	First evidence	0:13	First evidence of human meconium glycoasparagines	0:48	First evidence of human meconium glycoasparagines.
7655165	5	29	theme	known	865:869	arg1	pathways					881:888	the known catabolic pathways	861:888	the known catabolic pathways of N-glycans	861:901	Their structures are discussed in the context of the known catabolic pathways of N-glycans.
7655165	0	30	theme	meconium	24:31	arg1	glycoasparagines					33:48	human meconium glycoasparagines	18:48	human meconium glycoasparagines	18:48	First evidence of human meconium glycoasparagines.
7655165	4	31	theme	type	594:597	arg1	structures					599:608	N-acetyllactosaminic type structures	573:608	N-acetyllactosaminic type structures	573:608	These compounds are related to N-acetyllactosaminic type structures and are based on the common core: [formula: see text] These glycoasparagines are probably derived from both protease and partial exoglycosidase hydrolysis of fetal gastrointestinal N-glycosyl proteins.
7655165	2	32	theme	liquid	439:444	arg1	chromatographies					453:468	high-performance liquid (HPLC) chromatographies	422:468	high-performance liquid (HPLC) chromatographies	422:468	These glycoasparagines have been isolated from human meconium by a combination of ion-exchange, concanavalin A (ConA)-affinity and high-performance liquid (HPLC) chromatographies.
7655165	5	33	theme	catabolic	871:879	arg1	pathways					881:888	the known catabolic pathways	861:888	the known catabolic pathways of N-glycans	861:901	Their structures are discussed in the context of the known catabolic pathways of N-glycans.
7655165	2	34	theme	chromatographies	453:468	arg1	combination					358:368	a combination	356:368	a combination of ion-exchange, concanavalin A (ConA)-affinity and high-performance liquid (HPLC) chromatographies	356:468	These glycoasparagines have been isolated from human meconium by a combination of ion-exchange, concanavalin A (ConA)-affinity and high-performance liquid (HPLC) chromatographies.
7655165	2	35	attach	isolated	324:331	arg1	meconium					344:351	human meconium	338:351	human meconium	338:351	These glycoasparagines have been isolated from human meconium by a combination of ion-exchange, concanavalin A (ConA)-affinity and high-performance liquid (HPLC) chromatographies.
7655165	2	35	attach	isolated	324:331	arg2	glycoasparagines					297:312	These glycoasparagines	291:312	These glycoasparagines	291:312	These glycoasparagines have been isolated from human meconium by a combination of ion-exchange, concanavalin A (ConA)-affinity and high-performance liquid (HPLC) chromatographies.
7655165	1	36	theme	human	113:117	arg1	meconium					119:126	human meconium	113:126	human meconium	113:126	During a systematic study of carbohydrate material present in human meconium, in addition to the previously described mucins, glycolipids and free oligosaccharides, we have now characterized a significant quantity of free glycoasparagines.
7655165	4	37	dep	core	638:641	arg1	see					654:656	see	654:656	see text	654:661	These compounds are related to N-acetyllactosaminic type structures and are based on the common core: [formula: see text] These glycoasparagines are probably derived from both protease and partial exoglycosidase hydrolysis of fetal gastrointestinal N-glycosyl proteins.
7655165	1	38	from	present	102:108	arg1	meconium					119:126	human meconium	113:126	human meconium	113:126	During a systematic study of carbohydrate material present in human meconium, in addition to the previously described mucins, glycolipids and free oligosaccharides, we have now characterized a significant quantity of free glycoasparagines.
7655165	1	39	attach	present	102:108	arg2	material					93:100	carbohydrate material	80:100	carbohydrate material present in human meconium	80:126	During a systematic study of carbohydrate material present in human meconium, in addition to the previously described mucins, glycolipids and free oligosaccharides, we have now characterized a significant quantity of free glycoasparagines.
7655165	1	39	attach	present	102:108	arg1	meconium					119:126	human meconium	113:126	human meconium	113:126	During a systematic study of carbohydrate material present in human meconium, in addition to the previously described mucins, glycolipids and free oligosaccharides, we have now characterized a significant quantity of free glycoasparagines.
7655165	2	40	theme	human	338:342	arg1	meconium					344:351	human meconium	338:351	human meconium	338:351	These glycoasparagines have been isolated from human meconium by a combination of ion-exchange, concanavalin A (ConA)-affinity and high-performance liquid (HPLC) chromatographies.
7655165	2	41	theme	ion-exchange	373:384	arg1	combination					358:368	a combination	356:368	a combination of ion-exchange, concanavalin A (ConA)-affinity and high-performance liquid (HPLC) chromatographies	356:468	These glycoasparagines have been isolated from human meconium by a combination of ion-exchange, concanavalin A (ConA)-affinity and high-performance liquid (HPLC) chromatographies.
7655165	4	42	theme	common	631:636	arg1	core					638:641	the common core	627:641	the common core: [formula: see text]	627:662	These compounds are related to N-acetyllactosaminic type structures and are based on the common core: [formula: see text] These glycoasparagines are probably derived from both protease and partial exoglycosidase hydrolysis of fetal gastrointestinal N-glycosyl proteins.
7655165	4	43	dep	see	654:656	arg1	[formula					644:651	[formula	644:651	[formula	644:651	These compounds are related to N-acetyllactosaminic type structures and are based on the common core: [formula: see text] These glycoasparagines are probably derived from both protease and partial exoglycosidase hydrolysis of fetal gastrointestinal N-glycosyl proteins.
7655165	3	44	theme	1H-NMR	521:526	arg1	spectroscopy					528:539	400 MHz 1H-NMR spectroscopy	513:539	400 MHz 1H-NMR spectroscopy	513:539	Their structures have been established by 400 MHz 1H-NMR spectroscopy.
6317691	4	0	theme	epidermoid	742:751	arg1	cells					769:773	human epidermoid carcinoma A-431 cells	736:773	human epidermoid carcinoma A-431 cells	736:773	In human epidermoid carcinoma A-431 cells, the receptor precursor appears to contain one N-linked high mannose oligosaccharide and approximately 6-9 N-acetylgalactosamine residues linked O-glycosidically to Ser/Thr residues.
6317691	1	1	theme	dodecyl	313:319	arg1	gels					350:353	sodium dodecyl sulfate (SDS)-polyacrylamide gels	306:353	sodium dodecyl sulfate (SDS)-polyacrylamide gels	306:353	In human fibroblasts, the receptor for low density lipoprotein (LDL) is synthesized as a precursor of apparent Mr = 120,000 which is converted to a mature form of apparent Mr = 160,000, as determined by migration in sodium dodecyl sulfate (SDS)-polyacrylamide gels (Tolleshaug, H., Goldstein, J. L., Schneider, W. J., and Brown, M. S. (1982) Cell 30, 715-724).
6317691	11	2	from	differences	2181:2191	arg1	weight					2206:2211	molecular weight	2196:2211	molecular weight	2196:2211	These studies suggest that the apparent differences in molecular weight between the precursor and mature forms of the LDL receptor are largely, if not entirely, due to the addition of sialic acid and galactose residues to the O-linked GalNAc residues.
6317691	6	3	theme	tri-	1210:1213	arg1	species					1246:1252	a tri- or tetraantennary complex-type species	1208:1252	a tri- or tetraantennary complex-type species	1208:1252	The single N-linked oligosaccharide of the mature receptor can either be a tri- or tetraantennary complex-type species.
6317691	6	3	theme	tri-	1210:1213	arg1	oligosaccharide					1155:1169	The single N-linked oligosaccharide	1135:1169	The single N-linked oligosaccharide of the mature receptor	1135:1192	The single N-linked oligosaccharide of the mature receptor can either be a tri- or tetraantennary complex-type species.
6317691	11	4	dep	not	2288:2290	arg1	if					2285:2286	if	2285:2286	if	2285:2286	These studies suggest that the apparent differences in molecular weight between the precursor and mature forms of the LDL receptor are largely, if not entirely, due to the addition of sialic acid and galactose residues to the O-linked GalNAc residues.
6317691	8	5	theme	complex-type	1650:1661	arg1	structures					1663:1672	complex-type structures	1650:1672	complex-type structures	1650:1672	Since the addition of GalNAc residues to Ser/Thr residues precedes the conversion of N-linked high mannose-type oligosaccharides to complex-type structures, the transfer of N-acetylgalactosamine must occur prior to the entry of glycoproteins into the region of the Golgi containing the processing enzyme alpha-mannosidase I.
6317691	7	6	from	unit	1472:1475	arg1	receptor					1491:1498	the mature receptor	1480:1498	the mature receptor	1480:1498	Similar results were obtained with normal human fibroblast receptor except that the O-linked oligosaccharides on the precursor are neutral disaccharides, of which one component is GalNAc and the N-linked complex type unit on the mature receptor is less branched.
6317691	4	7	theme	A-431	763:767	arg1	cells					769:773	human epidermoid carcinoma A-431 cells	736:773	human epidermoid carcinoma A-431 cells	736:773	In human epidermoid carcinoma A-431 cells, the receptor precursor appears to contain one N-linked high mannose oligosaccharide and approximately 6-9 N-acetylgalactosamine residues linked O-glycosidically to Ser/Thr residues.
6317691	7	8	theme	neutral	1386:1392	arg1	oligosaccharides					1348:1363	the O-linked oligosaccharides	1335:1363	the O-linked oligosaccharides on the precursor	1335:1380	Similar results were obtained with normal human fibroblast receptor except that the O-linked oligosaccharides on the precursor are neutral disaccharides, of which one component is GalNAc and the N-linked complex type unit on the mature receptor is less branched.
6317691	7	8	theme	neutral	1386:1392	arg1	disaccharides					1394:1406	neutral disaccharides	1386:1406	neutral disaccharides	1386:1406	Similar results were obtained with normal human fibroblast receptor except that the O-linked oligosaccharides on the precursor are neutral disaccharides, of which one component is GalNAc and the N-linked complex type unit on the mature receptor is less branched.
6317691	9	9	theme	tunicamycin-treated	1877:1895	arg1	cells					1897:1901	tunicamycin-treated cells	1877:1901	tunicamycin-treated cells	1877:1901	We also studied the receptor from tunicamycin-treated cells and after treatment with neuraminidase.
6317691	2	10	theme	current	455:461	arg1	paper					463:467	The current paper	451:467	The current paper	451:467	The current paper describes the relationship of N- and O-glycosylation to this post-translational modification.
6317691	6	11	theme	mature	1178:1183	arg1	receptor					1185:1192	the mature receptor	1174:1192	the mature receptor	1174:1192	The single N-linked oligosaccharide of the mature receptor can either be a tri- or tetraantennary complex-type species.
6317691	8	12	theme	N-acetylgalactosamine	1691:1711	arg1	transfer					1679:1686	the transfer	1675:1686	the transfer of N-acetylgalactosamine	1675:1711	Since the addition of GalNAc residues to Ser/Thr residues precedes the conversion of N-linked high mannose-type oligosaccharides to complex-type structures, the transfer of N-acetylgalactosamine must occur prior to the entry of glycoproteins into the region of the Golgi containing the processing enzyme alpha-mannosidase I.
6317691	11	13	theme	residues	2351:2358	arg1	differences					2181:2191	the apparent differences	2168:2191	the apparent differences in molecular weight between the precursor and mature forms of the LDL receptor	2168:2270	These studies suggest that the apparent differences in molecular weight between the precursor and mature forms of the LDL receptor are largely, if not entirely, due to the addition of sialic acid and galactose residues to the O-linked GalNAc residues.
6317691	11	13	theme	residues	2351:2358	arg1	addition					2313:2320	the addition	2309:2320	the addition of sialic acid and galactose residues to the O-linked GalNAc residues	2309:2390	These studies suggest that the apparent differences in molecular weight between the precursor and mature forms of the LDL receptor are largely, if not entirely, due to the addition of sialic acid and galactose residues to the O-linked GalNAc residues.
6317691	0	14	link	O-linked	23:30	arg1	oligosaccharides					32:47	O-linked oligosaccharides	23:47	O-linked oligosaccharides	23:47	Biosynthesis of N- and O-linked oligosaccharides of the low density lipoprotein receptor.
6317691	7	15	theme	O-linked	1339:1346	arg1	oligosaccharides					1348:1363	the O-linked oligosaccharides	1335:1363	the O-linked oligosaccharides on the precursor	1335:1380	Similar results were obtained with normal human fibroblast receptor except that the O-linked oligosaccharides on the precursor are neutral disaccharides, of which one component is GalNAc and the N-linked complex type unit on the mature receptor is less branched.
6317691	7	15	theme	O-linked	1339:1346	arg1	disaccharides					1394:1406	neutral disaccharides	1386:1406	neutral disaccharides	1386:1406	Similar results were obtained with normal human fibroblast receptor except that the O-linked oligosaccharides on the precursor are neutral disaccharides, of which one component is GalNAc and the N-linked complex type unit on the mature receptor is less branched.
6317691	1	16	theme	sulfate	321:327	arg1	gels					350:353	sodium dodecyl sulfate (SDS)-polyacrylamide gels	306:353	sodium dodecyl sulfate (SDS)-polyacrylamide gels	306:353	In human fibroblasts, the receptor for low density lipoprotein (LDL) is synthesized as a precursor of apparent Mr = 120,000 which is converted to a mature form of apparent Mr = 160,000, as determined by migration in sodium dodecyl sulfate (SDS)-polyacrylamide gels (Tolleshaug, H., Goldstein, J. L., Schneider, W. J., and Brown, M. S. (1982) Cell 30, 715-724).
6317691	1	17	theme	SDS	330:332	arg1	gels					350:353	sodium dodecyl sulfate (SDS)-polyacrylamide gels	306:353	sodium dodecyl sulfate (SDS)-polyacrylamide gels	306:353	In human fibroblasts, the receptor for low density lipoprotein (LDL) is synthesized as a precursor of apparent Mr = 120,000 which is converted to a mature form of apparent Mr = 160,000, as determined by migration in sodium dodecyl sulfate (SDS)-polyacrylamide gels (Tolleshaug, H., Goldstein, J. L., Schneider, W. J., and Brown, M. S. (1982) Cell 30, 715-724).
6317691	10	18	link	O-linked	2114:2121	arg1	oligosaccharides					2123:2138	O-linked oligosaccharides	2114:2138	O-linked oligosaccharides	2114:2138	In addition, we analyzed the receptor synthesized by a lectin-resistant clone of Chinese hamster ovary cells that is deficient in adding galactose residues to both N- and O-linked oligosaccharides.
6317691	3	19	theme	LDL	629:631	arg1	receptors					633:641	LDL receptors	629:641	LDL receptors	629:641	Oligosaccharides were analyzed from precursor and mature forms of LDL receptors that had been immunoprecipitated from cells grown in media containing radioactive sugars.
6317691	1	20	theme	-polyacrylamide	334:348	arg1	gels					350:353	sodium dodecyl sulfate (SDS)-polyacrylamide gels	306:353	sodium dodecyl sulfate (SDS)-polyacrylamide gels	306:353	In human fibroblasts, the receptor for low density lipoprotein (LDL) is synthesized as a precursor of apparent Mr = 120,000 which is converted to a mature form of apparent Mr = 160,000, as determined by migration in sodium dodecyl sulfate (SDS)-polyacrylamide gels (Tolleshaug, H., Goldstein, J. L., Schneider, W. J., and Brown, M. S. (1982) Cell 30, 715-724).
6317691	4	21	theme	receptor	780:787	arg1	precursor					789:797	the receptor precursor	776:797	the receptor precursor	776:797	In human epidermoid carcinoma A-431 cells, the receptor precursor appears to contain one N-linked high mannose oligosaccharide and approximately 6-9 N-acetylgalactosamine residues linked O-glycosidically to Ser/Thr residues.
6317691	6	22	theme	single	1139:1144	arg1	species					1246:1252	a tri- or tetraantennary complex-type species	1208:1252	a tri- or tetraantennary complex-type species	1208:1252	The single N-linked oligosaccharide of the mature receptor can either be a tri- or tetraantennary complex-type species.
6317691	6	22	theme	single	1139:1144	arg1	oligosaccharide					1155:1169	The single N-linked oligosaccharide	1135:1169	The single N-linked oligosaccharide of the mature receptor	1135:1192	The single N-linked oligosaccharide of the mature receptor can either be a tri- or tetraantennary complex-type species.
6317691	7	23	theme	human	1297:1301	arg1	receptor					1314:1321	normal human fibroblast receptor	1290:1321	normal human fibroblast receptor	1290:1321	Similar results were obtained with normal human fibroblast receptor except that the O-linked oligosaccharides on the precursor are neutral disaccharides, of which one component is GalNAc and the N-linked complex type unit on the mature receptor is less branched.
6317691	2	24	theme	post-translational	530:547	arg1	modification					549:560	this post-translational modification	525:560	this post-translational modification	525:560	The current paper describes the relationship of N- and O-glycosylation to this post-translational modification.
6317691	10	25	theme	lectin-resistant	1998:2013	arg1	clone					2015:2019	a lectin-resistant clone	1996:2019	a lectin-resistant clone of Chinese hamster ovary cells that is deficient in adding galactose residues to both N- and O-linked oligosaccharides	1996:2138	In addition, we analyzed the receptor synthesized by a lectin-resistant clone of Chinese hamster ovary cells that is deficient in adding galactose residues to both N- and O-linked oligosaccharides.
6317691	6	26	theme	tetraantennary	1218:1231	arg1	species					1246:1252	a tri- or tetraantennary complex-type species	1208:1252	a tri- or tetraantennary complex-type species	1208:1252	The single N-linked oligosaccharide of the mature receptor can either be a tri- or tetraantennary complex-type species.
6317691	6	26	theme	tetraantennary	1218:1231	arg1	oligosaccharide					1155:1169	The single N-linked oligosaccharide	1135:1169	The single N-linked oligosaccharide of the mature receptor	1135:1192	The single N-linked oligosaccharide of the mature receptor can either be a tri- or tetraantennary complex-type species.
6317691	5	27	theme	mature	965:970	arg1	receptor					972:979	the mature receptor	961:979	the mature receptor	961:979	In the mature receptor, the O-linked oligosaccharides are mono- and disialylated species having the core structure of galactose leads to N-acetylgalactosamine leads to Ser/Thr.
6317691	8	28	theme	glycoproteins	1746:1758	arg1	entry					1737:1741	the entry	1733:1741	the entry of glycoproteins into the region of the Golgi containing the processing enzyme alpha-mannosidase I	1733:1840	Since the addition of GalNAc residues to Ser/Thr residues precedes the conversion of N-linked high mannose-type oligosaccharides to complex-type structures, the transfer of N-acetylgalactosamine must occur prior to the entry of glycoproteins into the region of the Golgi containing the processing enzyme alpha-mannosidase I.
6317691	3	29	theme	radioactive	713:723	arg1	sugars					725:730	radioactive sugars	713:730	radioactive sugars	713:730	Oligosaccharides were analyzed from precursor and mature forms of LDL receptors that had been immunoprecipitated from cells grown in media containing radioactive sugars.
6317691	7	30	link	O-linked	1339:1346	arg1	oligosaccharides					1348:1363	the O-linked oligosaccharides	1335:1363	the O-linked oligosaccharides on the precursor	1335:1380	Similar results were obtained with normal human fibroblast receptor except that the O-linked oligosaccharides on the precursor are neutral disaccharides, of which one component is GalNAc and the N-linked complex type unit on the mature receptor is less branched.
6317691	7	30	link	O-linked	1339:1346	arg1	disaccharides					1394:1406	neutral disaccharides	1386:1406	neutral disaccharides	1386:1406	Similar results were obtained with normal human fibroblast receptor except that the O-linked oligosaccharides on the precursor are neutral disaccharides, of which one component is GalNAc and the N-linked complex type unit on the mature receptor is less branched.
6317691	0	31	theme	low	56:58	arg1	lipoprotein					68:78	low density lipoprotein	56:78	the low density lipoprotein receptor	52:87	Biosynthesis of N- and O-linked oligosaccharides of the low density lipoprotein receptor.
6317691	1	32	theme	density	133:139	arg1	LDL					154:156	LDL	154:156	LDL	154:156	In human fibroblasts, the receptor for low density lipoprotein (LDL) is synthesized as a precursor of apparent Mr = 120,000 which is converted to a mature form of apparent Mr = 160,000, as determined by migration in sodium dodecyl sulfate (SDS)-polyacrylamide gels (Tolleshaug, H., Goldstein, J. L., Schneider, W. J., and Brown, M. S. (1982) Cell 30, 715-724).
6317691	1	32	theme	density	133:139	arg1	lipoprotein					141:151	low density lipoprotein	129:151	low density lipoprotein (LDL)	129:157	In human fibroblasts, the receptor for low density lipoprotein (LDL) is synthesized as a precursor of apparent Mr = 120,000 which is converted to a mature form of apparent Mr = 160,000, as determined by migration in sodium dodecyl sulfate (SDS)-polyacrylamide gels (Tolleshaug, H., Goldstein, J. L., Schneider, W. J., and Brown, M. S. (1982) Cell 30, 715-724).
6317691	5	33	link	O-linked	986:993	arg1	species					1039:1045	mono- and disialylated species	1016:1045	mono- and disialylated species having the core structure of galactose leads to N-acetylgalactosamine leads to Ser/Thr	1016:1132	In the mature receptor, the O-linked oligosaccharides are mono- and disialylated species having the core structure of galactose leads to N-acetylgalactosamine leads to Ser/Thr.
6317691	5	33	link	O-linked	986:993	arg1	oligosaccharides					995:1010	the O-linked oligosaccharides	982:1010	the O-linked oligosaccharides	982:1010	In the mature receptor, the O-linked oligosaccharides are mono- and disialylated species having the core structure of galactose leads to N-acetylgalactosamine leads to Ser/Thr.
6317691	5	34	contain	having	1047:1052	arg2	structure					1063:1071	the core structure	1054:1071	the core structure of galactose leads to N-acetylgalactosamine leads to Ser/Thr	1054:1132	In the mature receptor, the O-linked oligosaccharides are mono- and disialylated species having the core structure of galactose leads to N-acetylgalactosamine leads to Ser/Thr.
6317691	5	34	contain	having	1047:1052	arg1	species					1039:1045	mono- and disialylated species	1016:1045	mono- and disialylated species having the core structure of galactose leads to N-acetylgalactosamine leads to Ser/Thr	1016:1132	In the mature receptor, the O-linked oligosaccharides are mono- and disialylated species having the core structure of galactose leads to N-acetylgalactosamine leads to Ser/Thr.
6317691	5	34	contain	having	1047:1052	arg1	oligosaccharides					995:1010	the O-linked oligosaccharides	982:1010	the O-linked oligosaccharides	982:1010	In the mature receptor, the O-linked oligosaccharides are mono- and disialylated species having the core structure of galactose leads to N-acetylgalactosamine leads to Ser/Thr.
6317691	10	35	theme	hamster	2032:2038	arg1	cells					2046:2050	Chinese hamster ovary cells	2024:2050	Chinese hamster ovary cells that is deficient in adding galactose residues to both N- and O-linked oligosaccharides	2024:2138	In addition, we analyzed the receptor synthesized by a lectin-resistant clone of Chinese hamster ovary cells that is deficient in adding galactose residues to both N- and O-linked oligosaccharides.
6317691	0	36	theme	lipoprotein	68:78	arg1	receptor					80:87	the low density lipoprotein receptor	52:87	the low density lipoprotein receptor	52:87	Biosynthesis of N- and O-linked oligosaccharides of the low density lipoprotein receptor.
6317691	8	37	link	N-linked	1603:1610	arg1	oligosaccharides					1630:1645	N-linked high mannose-type oligosaccharides	1603:1645	N-linked high mannose-type oligosaccharides	1603:1645	Since the addition of GalNAc residues to Ser/Thr residues precedes the conversion of N-linked high mannose-type oligosaccharides to complex-type structures, the transfer of N-acetylgalactosamine must occur prior to the entry of glycoproteins into the region of the Golgi containing the processing enzyme alpha-mannosidase I.
6317691	7	38	theme	branched	1508:1515	arg1	GalNAc					1435:1440	GalNAc	1435:1440	GalNAc	1435:1440	Similar results were obtained with normal human fibroblast receptor except that the O-linked oligosaccharides on the precursor are neutral disaccharides, of which one component is GalNAc and the N-linked complex type unit on the mature receptor is less branched.
6317691	4	39	theme	N-linked	822:829	arg1	oligosaccharide					844:858	one N-linked high mannose oligosaccharide	818:858	one N-linked high mannose oligosaccharide	818:858	In human epidermoid carcinoma A-431 cells, the receptor precursor appears to contain one N-linked high mannose oligosaccharide and approximately 6-9 N-acetylgalactosamine residues linked O-glycosidically to Ser/Thr residues.
6317691	5	40	dep	N-acetylgalactosamine	1095:1115	arg1	leads					1117:1121	leads	1117:1121	leads to Ser/Thr	1117:1132	In the mature receptor, the O-linked oligosaccharides are mono- and disialylated species having the core structure of galactose leads to N-acetylgalactosamine leads to Ser/Thr.
6317691	11	41	theme	galactose	2341:2349	arg1	residues					2351:2358	galactose residues	2341:2358	galactose residues	2341:2358	These studies suggest that the apparent differences in molecular weight between the precursor and mature forms of the LDL receptor are largely, if not entirely, due to the addition of sialic acid and galactose residues to the O-linked GalNAc residues.
6317691	8	42	theme	Golgi	1783:1787	arg1	region					1769:1774	the region	1765:1774	the region of the Golgi containing the processing enzyme alpha-mannosidase I	1765:1840	Since the addition of GalNAc residues to Ser/Thr residues precedes the conversion of N-linked high mannose-type oligosaccharides to complex-type structures, the transfer of N-acetylgalactosamine must occur prior to the entry of glycoproteins into the region of the Golgi containing the processing enzyme alpha-mannosidase I.
6317691	4	43	theme	mannose	836:842	arg1	oligosaccharide					844:858	one N-linked high mannose oligosaccharide	818:858	one N-linked high mannose oligosaccharide	818:858	In human epidermoid carcinoma A-431 cells, the receptor precursor appears to contain one N-linked high mannose oligosaccharide and approximately 6-9 N-acetylgalactosamine residues linked O-glycosidically to Ser/Thr residues.
6317691	1	44	dep	160,000	267:273	arg1	determined					279:288	determined	279:288	determined by migration in sodium dodecyl sulfate (SDS)-polyacrylamide gels (Tolleshaug, H., Goldstein, J. L., Schneider, W. J., and Brown, M. S. (1982) Cell 30, 715-724)	279:448	In human fibroblasts, the receptor for low density lipoprotein (LDL) is synthesized as a precursor of apparent Mr = 120,000 which is converted to a mature form of apparent Mr = 160,000, as determined by migration in sodium dodecyl sulfate (SDS)-polyacrylamide gels (Tolleshaug, H., Goldstein, J. L., Schneider, W. J., and Brown, M. S. (1982) Cell 30, 715-724).
6317691	11	45	theme	acid	2332:2335	arg1	differences					2181:2191	the apparent differences	2168:2191	the apparent differences in molecular weight between the precursor and mature forms of the LDL receptor	2168:2270	These studies suggest that the apparent differences in molecular weight between the precursor and mature forms of the LDL receptor are largely, if not entirely, due to the addition of sialic acid and galactose residues to the O-linked GalNAc residues.
6317691	11	45	theme	acid	2332:2335	arg1	addition					2313:2320	the addition	2309:2320	the addition of sialic acid and galactose residues to the O-linked GalNAc residues	2309:2390	These studies suggest that the apparent differences in molecular weight between the precursor and mature forms of the LDL receptor are largely, if not entirely, due to the addition of sialic acid and galactose residues to the O-linked GalNAc residues.
6317691	1	46	theme	sodium	306:311	arg1	gels					350:353	sodium dodecyl sulfate (SDS)-polyacrylamide gels	306:353	sodium dodecyl sulfate (SDS)-polyacrylamide gels	306:353	In human fibroblasts, the receptor for low density lipoprotein (LDL) is synthesized as a precursor of apparent Mr = 120,000 which is converted to a mature form of apparent Mr = 160,000, as determined by migration in sodium dodecyl sulfate (SDS)-polyacrylamide gels (Tolleshaug, H., Goldstein, J. L., Schneider, W. J., and Brown, M. S. (1982) Cell 30, 715-724).
6317691	4	47	theme	Ser/Thr	940:946	arg1	residues					948:955	Ser/Thr residues	940:955	Ser/Thr residues	940:955	In human epidermoid carcinoma A-431 cells, the receptor precursor appears to contain one N-linked high mannose oligosaccharide and approximately 6-9 N-acetylgalactosamine residues linked O-glycosidically to Ser/Thr residues.
6317691	11	48	theme	O-linked	2367:2374	arg1	residues					2383:2390	the O-linked GalNAc residues	2363:2390	the O-linked GalNAc residues	2363:2390	These studies suggest that the apparent differences in molecular weight between the precursor and mature forms of the LDL receptor are largely, if not entirely, due to the addition of sialic acid and galactose residues to the O-linked GalNAc residues.
6317691	8	49	theme	enzyme	1815:1820	arg1	alpha-mannosidase					1822:1838	the processing enzyme alpha-mannosidase I	1800:1840	the processing enzyme alpha-mannosidase I	1800:1840	Since the addition of GalNAc residues to Ser/Thr residues precedes the conversion of N-linked high mannose-type oligosaccharides to complex-type structures, the transfer of N-acetylgalactosamine must occur prior to the entry of glycoproteins into the region of the Golgi containing the processing enzyme alpha-mannosidase I.
6317691	0	50	theme	N-	16:17	arg1	Biosynthesis					0:11	Biosynthesis	0:11	Biosynthesis of N- and O-linked oligosaccharides of the low density lipoprotein receptor.	0:88	Biosynthesis of N- and O-linked oligosaccharides of the low density lipoprotein receptor.
6317691	11	51	theme	receptor	2263:2270	arg1	forms					2246:2250	the precursor and mature forms	2221:2250	the precursor and mature forms of the LDL receptor	2221:2270	These studies suggest that the apparent differences in molecular weight between the precursor and mature forms of the LDL receptor are largely, if not entirely, due to the addition of sialic acid and galactose residues to the O-linked GalNAc residues.
6317691	0	52	theme	O-linked	23:30	arg1	oligosaccharides					32:47	O-linked oligosaccharides	23:47	O-linked oligosaccharides	23:47	Biosynthesis of N- and O-linked oligosaccharides of the low density lipoprotein receptor.
6317691	1	53	theme	apparent	253:260	arg1	Mr					262:263	apparent Mr	253:263	apparent Mr = 160,000, as determined by migration in sodium dodecyl sulfate (SDS)-polyacrylamide gels (Tolleshaug, H., Goldstein, J. L., Schneider, W. J., and Brown, M. S. (1982) Cell 30, 715-724)	253:448	In human fibroblasts, the receptor for low density lipoprotein (LDL) is synthesized as a precursor of apparent Mr = 120,000 which is converted to a mature form of apparent Mr = 160,000, as determined by migration in sodium dodecyl sulfate (SDS)-polyacrylamide gels (Tolleshaug, H., Goldstein, J. L., Schneider, W. J., and Brown, M. S. (1982) Cell 30, 715-724).
6317691	9	54	with	treatment	1913:1921	arg1	neuraminidase					1928:1940	neuraminidase	1928:1940	neuraminidase	1928:1940	We also studied the receptor from tunicamycin-treated cells and after treatment with neuraminidase.
6317691	3	55	contain	containing	702:711	arg1	media					696:700	media	696:700	media containing radioactive sugars	696:730	Oligosaccharides were analyzed from precursor and mature forms of LDL receptors that had been immunoprecipitated from cells grown in media containing radioactive sugars.
6317691	3	55	contain	containing	702:711	arg2	sugars					725:730	radioactive sugars	713:730	radioactive sugars	713:730	Oligosaccharides were analyzed from precursor and mature forms of LDL receptors that had been immunoprecipitated from cells grown in media containing radioactive sugars.
6317691	5	56	theme	galactose	1076:1084	arg1	structure					1063:1071	the core structure	1054:1071	the core structure of galactose leads to N-acetylgalactosamine leads to Ser/Thr	1054:1132	In the mature receptor, the O-linked oligosaccharides are mono- and disialylated species having the core structure of galactose leads to N-acetylgalactosamine leads to Ser/Thr.
6317691	7	57	theme	complex	1459:1465	arg1	branched					1508:1515	branched	1508:1515	branched	1508:1515	Similar results were obtained with normal human fibroblast receptor except that the O-linked oligosaccharides on the precursor are neutral disaccharides, of which one component is GalNAc and the N-linked complex type unit on the mature receptor is less branched.
6317691	7	57	theme	complex	1459:1465	arg1	unit					1472:1475	the N-linked complex type unit	1446:1475	the N-linked complex type unit on the mature receptor	1446:1498	Similar results were obtained with normal human fibroblast receptor except that the O-linked oligosaccharides on the precursor are neutral disaccharides, of which one component is GalNAc and the N-linked complex type unit on the mature receptor is less branched.
6317691	4	58	link	N-linked	822:829	arg1	oligosaccharide					844:858	one N-linked high mannose oligosaccharide	818:858	one N-linked high mannose oligosaccharide	818:858	In human epidermoid carcinoma A-431 cells, the receptor precursor appears to contain one N-linked high mannose oligosaccharide and approximately 6-9 N-acetylgalactosamine residues linked O-glycosidically to Ser/Thr residues.
6317691	1	59	theme	apparent	192:199	arg1	Mr					201:202	apparent Mr	192:202	apparent Mr = 120,000 which is converted to a mature form of apparent Mr = 160,000, as determined by migration in sodium dodecyl sulfate (SDS)-polyacrylamide gels (Tolleshaug, H., Goldstein, J. L., Schneider, W. J., and Brown, M. S. (1982) Cell 30, 715-724)	192:448	In human fibroblasts, the receptor for low density lipoprotein (LDL) is synthesized as a precursor of apparent Mr = 120,000 which is converted to a mature form of apparent Mr = 160,000, as determined by migration in sodium dodecyl sulfate (SDS)-polyacrylamide gels (Tolleshaug, H., Goldstein, J. L., Schneider, W. J., and Brown, M. S. (1982) Cell 30, 715-724).
6317691	10	60	theme	cells	2046:2050	arg1	clone					2015:2019	a lectin-resistant clone	1996:2019	a lectin-resistant clone of Chinese hamster ovary cells that is deficient in adding galactose residues to both N- and O-linked oligosaccharides	1996:2138	In addition, we analyzed the receptor synthesized by a lectin-resistant clone of Chinese hamster ovary cells that is deficient in adding galactose residues to both N- and O-linked oligosaccharides.
6317691	8	61	theme	N-linked	1603:1610	arg1	oligosaccharides					1630:1645	N-linked high mannose-type oligosaccharides	1603:1645	N-linked high mannose-type oligosaccharides	1603:1645	Since the addition of GalNAc residues to Ser/Thr residues precedes the conversion of N-linked high mannose-type oligosaccharides to complex-type structures, the transfer of N-acetylgalactosamine must occur prior to the entry of glycoproteins into the region of the Golgi containing the processing enzyme alpha-mannosidase I.
6317691	1	62	theme	=	204:204	arg1	Mr					201:202	apparent Mr	192:202	apparent Mr = 120,000 which is converted to a mature form of apparent Mr = 160,000, as determined by migration in sodium dodecyl sulfate (SDS)-polyacrylamide gels (Tolleshaug, H., Goldstein, J. L., Schneider, W. J., and Brown, M. S. (1982) Cell 30, 715-724)	192:448	In human fibroblasts, the receptor for low density lipoprotein (LDL) is synthesized as a precursor of apparent Mr = 120,000 which is converted to a mature form of apparent Mr = 160,000, as determined by migration in sodium dodecyl sulfate (SDS)-polyacrylamide gels (Tolleshaug, H., Goldstein, J. L., Schneider, W. J., and Brown, M. S. (1982) Cell 30, 715-724).
6317691	10	63	theme	galactose	2080:2088	arg1	residues					2090:2097	galactose residues	2080:2097	galactose residues	2080:2097	In addition, we analyzed the receptor synthesized by a lectin-resistant clone of Chinese hamster ovary cells that is deficient in adding galactose residues to both N- and O-linked oligosaccharides.
6317691	8	64	theme	residues	1547:1554	arg1	addition					1528:1535	the addition	1524:1535	the addition of GalNAc residues to Ser/Thr residues	1524:1574	Since the addition of GalNAc residues to Ser/Thr residues precedes the conversion of N-linked high mannose-type oligosaccharides to complex-type structures, the transfer of N-acetylgalactosamine must occur prior to the entry of glycoproteins into the region of the Golgi containing the processing enzyme alpha-mannosidase I.
6317691	11	65	theme	molecular	2196:2204	arg1	weight					2206:2211	molecular weight	2196:2211	molecular weight	2196:2211	These studies suggest that the apparent differences in molecular weight between the precursor and mature forms of the LDL receptor are largely, if not entirely, due to the addition of sialic acid and galactose residues to the O-linked GalNAc residues.
6317691	8	66	theme	mannose-type	1617:1628	arg1	oligosaccharides					1630:1645	N-linked high mannose-type oligosaccharides	1603:1645	N-linked high mannose-type oligosaccharides	1603:1645	Since the addition of GalNAc residues to Ser/Thr residues precedes the conversion of N-linked high mannose-type oligosaccharides to complex-type structures, the transfer of N-acetylgalactosamine must occur prior to the entry of glycoproteins into the region of the Golgi containing the processing enzyme alpha-mannosidase I.
6317691	4	67	theme	human	736:740	arg1	cells					769:773	human epidermoid carcinoma A-431 cells	736:773	human epidermoid carcinoma A-431 cells	736:773	In human epidermoid carcinoma A-431 cells, the receptor precursor appears to contain one N-linked high mannose oligosaccharide and approximately 6-9 N-acetylgalactosamine residues linked O-glycosidically to Ser/Thr residues.
6317691	8	68	theme	Ser/Thr	1559:1565	arg1	residues					1567:1574	Ser/Thr residues	1559:1574	Ser/Thr residues	1559:1574	Since the addition of GalNAc residues to Ser/Thr residues precedes the conversion of N-linked high mannose-type oligosaccharides to complex-type structures, the transfer of N-acetylgalactosamine must occur prior to the entry of glycoproteins into the region of the Golgi containing the processing enzyme alpha-mannosidase I.
6317691	4	69	theme	carcinoma	753:761	arg1	cells					769:773	human epidermoid carcinoma A-431 cells	736:773	human epidermoid carcinoma A-431 cells	736:773	In human epidermoid carcinoma A-431 cells, the receptor precursor appears to contain one N-linked high mannose oligosaccharide and approximately 6-9 N-acetylgalactosamine residues linked O-glycosidically to Ser/Thr residues.
6317691	7	70	theme	disaccharides	1394:1406	arg1	GalNAc					1435:1440	GalNAc	1435:1440	GalNAc	1435:1440	Similar results were obtained with normal human fibroblast receptor except that the O-linked oligosaccharides on the precursor are neutral disaccharides, of which one component is GalNAc and the N-linked complex type unit on the mature receptor is less branched.
6317691	11	71	theme	LDL	2259:2261	arg1	receptor					2263:2270	the LDL receptor	2255:2270	the LDL receptor	2255:2270	These studies suggest that the apparent differences in molecular weight between the precursor and mature forms of the LDL receptor are largely, if not entirely, due to the addition of sialic acid and galactose residues to the O-linked GalNAc residues.
6317691	3	72	theme	precursor	599:607	arg1	forms					620:624	precursor and mature forms	599:624	precursor and mature forms of LDL receptors that had been immunoprecipitated from cells grown in media containing radioactive sugars	599:730	Oligosaccharides were analyzed from precursor and mature forms of LDL receptors that had been immunoprecipitated from cells grown in media containing radioactive sugars.
6317691	6	73	dep	tri-	1210:1213	arg1	complex-type					1233:1244	complex-type	1233:1244	complex-type	1233:1244	The single N-linked oligosaccharide of the mature receptor can either be a tri- or tetraantennary complex-type species.
6317691	1	74	theme	=	265:265	arg1	Mr					262:263	apparent Mr	253:263	apparent Mr = 160,000, as determined by migration in sodium dodecyl sulfate (SDS)-polyacrylamide gels (Tolleshaug, H., Goldstein, J. L., Schneider, W. J., and Brown, M. S. (1982) Cell 30, 715-724)	253:448	In human fibroblasts, the receptor for low density lipoprotein (LDL) is synthesized as a precursor of apparent Mr = 120,000 which is converted to a mature form of apparent Mr = 160,000, as determined by migration in sodium dodecyl sulfate (SDS)-polyacrylamide gels (Tolleshaug, H., Goldstein, J. L., Schneider, W. J., and Brown, M. S. (1982) Cell 30, 715-724).
6317691	6	75	theme	receptor	1185:1192	arg1	species					1246:1252	a tri- or tetraantennary complex-type species	1208:1252	a tri- or tetraantennary complex-type species	1208:1252	The single N-linked oligosaccharide of the mature receptor can either be a tri- or tetraantennary complex-type species.
6317691	6	75	theme	receptor	1185:1192	arg1	oligosaccharide					1155:1169	The single N-linked oligosaccharide	1135:1169	The single N-linked oligosaccharide of the mature receptor	1135:1192	The single N-linked oligosaccharide of the mature receptor can either be a tri- or tetraantennary complex-type species.
6317691	4	76	attach	linked	913:918	arg1	residues					948:955	Ser/Thr residues	940:955	Ser/Thr residues	940:955	In human epidermoid carcinoma A-431 cells, the receptor precursor appears to contain one N-linked high mannose oligosaccharide and approximately 6-9 N-acetylgalactosamine residues linked O-glycosidically to Ser/Thr residues.
6317691	4	76	attach	linked	913:918	arg2	oligosaccharide					844:858	one N-linked high mannose oligosaccharide	818:858	one N-linked high mannose oligosaccharide	818:858	In human epidermoid carcinoma A-431 cells, the receptor precursor appears to contain one N-linked high mannose oligosaccharide and approximately 6-9 N-acetylgalactosamine residues linked O-glycosidically to Ser/Thr residues.
6317691	6	77	link	N-linked	1146:1153	arg1	species					1246:1252	a tri- or tetraantennary complex-type species	1208:1252	a tri- or tetraantennary complex-type species	1208:1252	The single N-linked oligosaccharide of the mature receptor can either be a tri- or tetraantennary complex-type species.
6317691	6	77	link	N-linked	1146:1153	arg1	oligosaccharide					1155:1169	The single N-linked oligosaccharide	1135:1169	The single N-linked oligosaccharide of the mature receptor	1135:1192	The single N-linked oligosaccharide of the mature receptor can either be a tri- or tetraantennary complex-type species.
6317691	1	78	dep	=	204:204	arg1	120,000					206:212	120,000	206:212	120,000	206:212	In human fibroblasts, the receptor for low density lipoprotein (LDL) is synthesized as a precursor of apparent Mr = 120,000 which is converted to a mature form of apparent Mr = 160,000, as determined by migration in sodium dodecyl sulfate (SDS)-polyacrylamide gels (Tolleshaug, H., Goldstein, J. L., Schneider, W. J., and Brown, M. S. (1982) Cell 30, 715-724).
6317691	5	79	gly	disialylated	1026:1037	arg1	species					1039:1045	mono- and disialylated species	1016:1045	mono- and disialylated species having the core structure of galactose leads to N-acetylgalactosamine leads to Ser/Thr	1016:1132	In the mature receptor, the O-linked oligosaccharides are mono- and disialylated species having the core structure of galactose leads to N-acetylgalactosamine leads to Ser/Thr.
6317691	5	79	gly	disialylated	1026:1037	arg1	oligosaccharides					995:1010	the O-linked oligosaccharides	982:1010	the O-linked oligosaccharides	982:1010	In the mature receptor, the O-linked oligosaccharides are mono- and disialylated species having the core structure of galactose leads to N-acetylgalactosamine leads to Ser/Thr.
6317691	3	80	theme	mature	613:618	arg1	forms					620:624	precursor and mature forms	599:624	precursor and mature forms of LDL receptors that had been immunoprecipitated from cells grown in media containing radioactive sugars	599:730	Oligosaccharides were analyzed from precursor and mature forms of LDL receptors that had been immunoprecipitated from cells grown in media containing radioactive sugars.
6317691	11	81	theme	mature	2239:2244	arg1	forms					2246:2250	the precursor and mature forms	2221:2250	the precursor and mature forms of the LDL receptor	2221:2270	These studies suggest that the apparent differences in molecular weight between the precursor and mature forms of the LDL receptor are largely, if not entirely, due to the addition of sialic acid and galactose residues to the O-linked GalNAc residues.
6317691	6	82	theme	N-linked	1146:1153	arg1	species					1246:1252	a tri- or tetraantennary complex-type species	1208:1252	a tri- or tetraantennary complex-type species	1208:1252	The single N-linked oligosaccharide of the mature receptor can either be a tri- or tetraantennary complex-type species.
6317691	6	82	theme	N-linked	1146:1153	arg1	oligosaccharide					1155:1169	The single N-linked oligosaccharide	1135:1169	The single N-linked oligosaccharide of the mature receptor	1135:1192	The single N-linked oligosaccharide of the mature receptor can either be a tri- or tetraantennary complex-type species.
6317691	11	83	theme	GalNAc	2376:2381	arg1	residues					2383:2390	the O-linked GalNAc residues	2363:2390	the O-linked GalNAc residues	2363:2390	These studies suggest that the apparent differences in molecular weight between the precursor and mature forms of the LDL receptor are largely, if not entirely, due to the addition of sialic acid and galactose residues to the O-linked GalNAc residues.
6317691	3	84	theme	receptors	633:641	arg1	forms					620:624	precursor and mature forms	599:624	precursor and mature forms of LDL receptors that had been immunoprecipitated from cells grown in media containing radioactive sugars	599:730	Oligosaccharides were analyzed from precursor and mature forms of LDL receptors that had been immunoprecipitated from cells grown in media containing radioactive sugars.
6317691	7	85	from	oligosaccharides	1348:1363	arg1	precursor					1372:1380	the precursor	1368:1380	the precursor	1368:1380	Similar results were obtained with normal human fibroblast receptor except that the O-linked oligosaccharides on the precursor are neutral disaccharides, of which one component is GalNAc and the N-linked complex type unit on the mature receptor is less branched.
6317691	7	86	theme	fibroblast	1303:1312	arg1	receptor					1314:1321	normal human fibroblast receptor	1290:1321	normal human fibroblast receptor	1290:1321	Similar results were obtained with normal human fibroblast receptor except that the O-linked oligosaccharides on the precursor are neutral disaccharides, of which one component is GalNAc and the N-linked complex type unit on the mature receptor is less branched.
6317691	0	87	theme	density	60:66	arg1	lipoprotein					68:78	low density lipoprotein	56:78	the low density lipoprotein receptor	52:87	Biosynthesis of N- and O-linked oligosaccharides of the low density lipoprotein receptor.
6317691	1	88	theme	low	129:131	arg1	LDL					154:156	LDL	154:156	LDL	154:156	In human fibroblasts, the receptor for low density lipoprotein (LDL) is synthesized as a precursor of apparent Mr = 120,000 which is converted to a mature form of apparent Mr = 160,000, as determined by migration in sodium dodecyl sulfate (SDS)-polyacrylamide gels (Tolleshaug, H., Goldstein, J. L., Schneider, W. J., and Brown, M. S. (1982) Cell 30, 715-724).
6317691	1	88	theme	low	129:131	arg1	lipoprotein					141:151	low density lipoprotein	129:151	low density lipoprotein (LDL)	129:157	In human fibroblasts, the receptor for low density lipoprotein (LDL) is synthesized as a precursor of apparent Mr = 120,000 which is converted to a mature form of apparent Mr = 160,000, as determined by migration in sodium dodecyl sulfate (SDS)-polyacrylamide gels (Tolleshaug, H., Goldstein, J. L., Schneider, W. J., and Brown, M. S. (1982) Cell 30, 715-724).
6317691	7	89	theme	normal	1290:1295	arg1	receptor					1314:1321	normal human fibroblast receptor	1290:1321	normal human fibroblast receptor	1290:1321	Similar results were obtained with normal human fibroblast receptor except that the O-linked oligosaccharides on the precursor are neutral disaccharides, of which one component is GalNAc and the N-linked complex type unit on the mature receptor is less branched.
6317691	11	90	link	O-linked	2367:2374	arg1	residues					2383:2390	the O-linked GalNAc residues	2363:2390	the O-linked GalNAc residues	2363:2390	These studies suggest that the apparent differences in molecular weight between the precursor and mature forms of the LDL receptor are largely, if not entirely, due to the addition of sialic acid and galactose residues to the O-linked GalNAc residues.
6317691	0	91	theme	receptor	80:87	arg1	N-					16:17	N-	16:17	N-	16:17	Biosynthesis of N- and O-linked oligosaccharides of the low density lipoprotein receptor.
6317691	0	91	theme	receptor	80:87	arg1	oligosaccharides					32:47	O-linked oligosaccharides	23:47	O-linked oligosaccharides	23:47	Biosynthesis of N- and O-linked oligosaccharides of the low density lipoprotein receptor.
6317691	1	92	dep	=	265:265	arg1	160,000					267:273	160,000	267:273	160,000	267:273	In human fibroblasts, the receptor for low density lipoprotein (LDL) is synthesized as a precursor of apparent Mr = 120,000 which is converted to a mature form of apparent Mr = 160,000, as determined by migration in sodium dodecyl sulfate (SDS)-polyacrylamide gels (Tolleshaug, H., Goldstein, J. L., Schneider, W. J., and Brown, M. S. (1982) Cell 30, 715-724).
6317691	2	93	theme	N-	499:500	arg1	relationship					483:494	the relationship	479:494	the relationship of N- and O-glycosylation to this post-translational modification	479:560	The current paper describes the relationship of N- and O-glycosylation to this post-translational modification.
6317691	10	94	theme	Chinese	2024:2030	arg1	cells					2046:2050	Chinese hamster ovary cells	2024:2050	Chinese hamster ovary cells that is deficient in adding galactose residues to both N- and O-linked oligosaccharides	2024:2138	In addition, we analyzed the receptor synthesized by a lectin-resistant clone of Chinese hamster ovary cells that is deficient in adding galactose residues to both N- and O-linked oligosaccharides.
6317691	5	95	theme	core	1058:1061	arg1	structure					1063:1071	the core structure	1054:1071	the core structure of galactose leads to N-acetylgalactosamine leads to Ser/Thr	1054:1132	In the mature receptor, the O-linked oligosaccharides are mono- and disialylated species having the core structure of galactose leads to N-acetylgalactosamine leads to Ser/Thr.
6317691	8	96	gly	glycoproteins	1746:1758	arg1	glycoproteins					1746:1758	glycoproteins	1746:1758	glycoproteins	1746:1758	Since the addition of GalNAc residues to Ser/Thr residues precedes the conversion of N-linked high mannose-type oligosaccharides to complex-type structures, the transfer of N-acetylgalactosamine must occur prior to the entry of glycoproteins into the region of the Golgi containing the processing enzyme alpha-mannosidase I.
6317691	5	97	dep	galactose	1076:1084	arg1	leads					1086:1090	leads	1086:1090	leads to N-acetylgalactosamine leads to Ser/Thr	1086:1132	In the mature receptor, the O-linked oligosaccharides are mono- and disialylated species having the core structure of galactose leads to N-acetylgalactosamine leads to Ser/Thr.
6317691	11	98	theme	sialic	2325:2330	arg1	acid					2332:2335	sialic acid	2325:2335	sialic acid	2325:2335	These studies suggest that the apparent differences in molecular weight between the precursor and mature forms of the LDL receptor are largely, if not entirely, due to the addition of sialic acid and galactose residues to the O-linked GalNAc residues.
6317691	10	99	theme	O-linked	2114:2121	arg1	oligosaccharides					2123:2138	O-linked oligosaccharides	2114:2138	O-linked oligosaccharides	2114:2138	In addition, we analyzed the receptor synthesized by a lectin-resistant clone of Chinese hamster ovary cells that is deficient in adding galactose residues to both N- and O-linked oligosaccharides.
6317691	5	100	theme	mono-	1016:1020	arg1	species					1039:1045	mono- and disialylated species	1016:1045	mono- and disialylated species having the core structure of galactose leads to N-acetylgalactosamine leads to Ser/Thr	1016:1132	In the mature receptor, the O-linked oligosaccharides are mono- and disialylated species having the core structure of galactose leads to N-acetylgalactosamine leads to Ser/Thr.
6317691	5	100	theme	mono-	1016:1020	arg1	oligosaccharides					995:1010	the O-linked oligosaccharides	982:1010	the O-linked oligosaccharides	982:1010	In the mature receptor, the O-linked oligosaccharides are mono- and disialylated species having the core structure of galactose leads to N-acetylgalactosamine leads to Ser/Thr.
6317691	1	101	dep	J.	404:405	arg1	Cell					432:435	Cell	432:435	Cell	432:435	In human fibroblasts, the receptor for low density lipoprotein (LDL) is synthesized as a precursor of apparent Mr = 120,000 which is converted to a mature form of apparent Mr = 160,000, as determined by migration in sodium dodecyl sulfate (SDS)-polyacrylamide gels (Tolleshaug, H., Goldstein, J. L., Schneider, W. J., and Brown, M. S. (1982) Cell 30, 715-724).
6317691	4	102	theme	high	831:834	arg1	oligosaccharide					844:858	one N-linked high mannose oligosaccharide	818:858	one N-linked high mannose oligosaccharide	818:858	In human epidermoid carcinoma A-431 cells, the receptor precursor appears to contain one N-linked high mannose oligosaccharide and approximately 6-9 N-acetylgalactosamine residues linked O-glycosidically to Ser/Thr residues.
6317691	11	103	theme	precursor	2225:2233	arg1	forms					2246:2250	the precursor and mature forms	2221:2250	the precursor and mature forms of the LDL receptor	2221:2270	These studies suggest that the apparent differences in molecular weight between the precursor and mature forms of the LDL receptor are largely, if not entirely, due to the addition of sialic acid and galactose residues to the O-linked GalNAc residues.
6317691	5	104	theme	disialylated	1026:1037	arg1	species					1039:1045	mono- and disialylated species	1016:1045	mono- and disialylated species having the core structure of galactose leads to N-acetylgalactosamine leads to Ser/Thr	1016:1132	In the mature receptor, the O-linked oligosaccharides are mono- and disialylated species having the core structure of galactose leads to N-acetylgalactosamine leads to Ser/Thr.
6317691	5	104	theme	disialylated	1026:1037	arg1	oligosaccharides					995:1010	the O-linked oligosaccharides	982:1010	the O-linked oligosaccharides	982:1010	In the mature receptor, the O-linked oligosaccharides are mono- and disialylated species having the core structure of galactose leads to N-acetylgalactosamine leads to Ser/Thr.
6317691	7	105	theme	Similar	1255:1261	arg1	results					1263:1269	Similar results	1255:1269	Similar results	1255:1269	Similar results were obtained with normal human fibroblast receptor except that the O-linked oligosaccharides on the precursor are neutral disaccharides, of which one component is GalNAc and the N-linked complex type unit on the mature receptor is less branched.
6317691	1	106	dep	determined	279:288	arg1	H.					368:369	H.	368:369	H.	368:369	In human fibroblasts, the receptor for low density lipoprotein (LDL) is synthesized as a precursor of apparent Mr = 120,000 which is converted to a mature form of apparent Mr = 160,000, as determined by migration in sodium dodecyl sulfate (SDS)-polyacrylamide gels (Tolleshaug, H., Goldstein, J. L., Schneider, W. J., and Brown, M. S. (1982) Cell 30, 715-724).
6317691	1	106	dep	determined	279:288	arg1	1982					426:429	1982	426:429	1982	426:429	In human fibroblasts, the receptor for low density lipoprotein (LDL) is synthesized as a precursor of apparent Mr = 120,000 which is converted to a mature form of apparent Mr = 160,000, as determined by migration in sodium dodecyl sulfate (SDS)-polyacrylamide gels (Tolleshaug, H., Goldstein, J. L., Schneider, W. J., and Brown, M. S. (1982) Cell 30, 715-724).
6317691	1	106	dep	determined	279:288	arg1	Schneider					390:398	Schneider	390:398	Schneider	390:398	In human fibroblasts, the receptor for low density lipoprotein (LDL) is synthesized as a precursor of apparent Mr = 120,000 which is converted to a mature form of apparent Mr = 160,000, as determined by migration in sodium dodecyl sulfate (SDS)-polyacrylamide gels (Tolleshaug, H., Goldstein, J. L., Schneider, W. J., and Brown, M. S. (1982) Cell 30, 715-724).
6317691	1	106	dep	determined	279:288	arg1	Goldstein					372:380	Goldstein	372:380	Goldstein	372:380	In human fibroblasts, the receptor for low density lipoprotein (LDL) is synthesized as a precursor of apparent Mr = 120,000 which is converted to a mature form of apparent Mr = 160,000, as determined by migration in sodium dodecyl sulfate (SDS)-polyacrylamide gels (Tolleshaug, H., Goldstein, J. L., Schneider, W. J., and Brown, M. S. (1982) Cell 30, 715-724).
6317691	1	106	dep	determined	279:288	arg1	W.					401:402	W.	401:402	W.	401:402	In human fibroblasts, the receptor for low density lipoprotein (LDL) is synthesized as a precursor of apparent Mr = 120,000 which is converted to a mature form of apparent Mr = 160,000, as determined by migration in sodium dodecyl sulfate (SDS)-polyacrylamide gels (Tolleshaug, H., Goldstein, J. L., Schneider, W. J., and Brown, M. S. (1982) Cell 30, 715-724).
6317691	1	106	dep	determined	279:288	arg1	M.					419:420	M.	419:420	M.	419:420	In human fibroblasts, the receptor for low density lipoprotein (LDL) is synthesized as a precursor of apparent Mr = 120,000 which is converted to a mature form of apparent Mr = 160,000, as determined by migration in sodium dodecyl sulfate (SDS)-polyacrylamide gels (Tolleshaug, H., Goldstein, J. L., Schneider, W. J., and Brown, M. S. (1982) Cell 30, 715-724).
6317691	1	106	dep	determined	279:288	arg1	J.					404:405	J.	404:405	J.	404:405	In human fibroblasts, the receptor for low density lipoprotein (LDL) is synthesized as a precursor of apparent Mr = 120,000 which is converted to a mature form of apparent Mr = 160,000, as determined by migration in sodium dodecyl sulfate (SDS)-polyacrylamide gels (Tolleshaug, H., Goldstein, J. L., Schneider, W. J., and Brown, M. S. (1982) Cell 30, 715-724).
6317691	1	106	dep	determined	279:288	arg1	S					422:422	S	422:422	S	422:422	In human fibroblasts, the receptor for low density lipoprotein (LDL) is synthesized as a precursor of apparent Mr = 120,000 which is converted to a mature form of apparent Mr = 160,000, as determined by migration in sodium dodecyl sulfate (SDS)-polyacrylamide gels (Tolleshaug, H., Goldstein, J. L., Schneider, W. J., and Brown, M. S. (1982) Cell 30, 715-724).
6317691	1	106	dep	determined	279:288	arg1	J.					383:384	J.	383:384	J.	383:384	In human fibroblasts, the receptor for low density lipoprotein (LDL) is synthesized as a precursor of apparent Mr = 120,000 which is converted to a mature form of apparent Mr = 160,000, as determined by migration in sodium dodecyl sulfate (SDS)-polyacrylamide gels (Tolleshaug, H., Goldstein, J. L., Schneider, W. J., and Brown, M. S. (1982) Cell 30, 715-724).
6317691	2	107	theme	O-glycosylation	506:520	arg1	relationship					483:494	the relationship	479:494	the relationship of N- and O-glycosylation to this post-translational modification	479:560	The current paper describes the relationship of N- and O-glycosylation to this post-translational modification.
6317691	1	108	from	migration	293:301	arg1	gels					350:353	sodium dodecyl sulfate (SDS)-polyacrylamide gels	306:353	sodium dodecyl sulfate (SDS)-polyacrylamide gels	306:353	In human fibroblasts, the receptor for low density lipoprotein (LDL) is synthesized as a precursor of apparent Mr = 120,000 which is converted to a mature form of apparent Mr = 160,000, as determined by migration in sodium dodecyl sulfate (SDS)-polyacrylamide gels (Tolleshaug, H., Goldstein, J. L., Schneider, W. J., and Brown, M. S. (1982) Cell 30, 715-724).
6317691	1	109	theme	mature	238:243	arg1	form					245:248	a mature form	236:248	a mature form of apparent Mr = 160,000, as determined by migration in sodium dodecyl sulfate (SDS)-polyacrylamide gels (Tolleshaug, H., Goldstein, J. L., Schneider, W. J., and Brown, M. S. (1982) Cell 30, 715-724)	236:448	In human fibroblasts, the receptor for low density lipoprotein (LDL) is synthesized as a precursor of apparent Mr = 120,000 which is converted to a mature form of apparent Mr = 160,000, as determined by migration in sodium dodecyl sulfate (SDS)-polyacrylamide gels (Tolleshaug, H., Goldstein, J. L., Schneider, W. J., and Brown, M. S. (1982) Cell 30, 715-724).
6317691	8	110	theme	processing	1804:1813	arg1	alpha-mannosidase					1822:1838	the processing enzyme alpha-mannosidase I	1800:1840	the processing enzyme alpha-mannosidase I	1800:1840	Since the addition of GalNAc residues to Ser/Thr residues precedes the conversion of N-linked high mannose-type oligosaccharides to complex-type structures, the transfer of N-acetylgalactosamine must occur prior to the entry of glycoproteins into the region of the Golgi containing the processing enzyme alpha-mannosidase I.
6317691	1	111	theme	human	93:97	arg1	fibroblasts					99:109	human fibroblasts	93:109	human fibroblasts	93:109	In human fibroblasts, the receptor for low density lipoprotein (LDL) is synthesized as a precursor of apparent Mr = 120,000 which is converted to a mature form of apparent Mr = 160,000, as determined by migration in sodium dodecyl sulfate (SDS)-polyacrylamide gels (Tolleshaug, H., Goldstein, J. L., Schneider, W. J., and Brown, M. S. (1982) Cell 30, 715-724).
6317691	4	112	contain	contain	810:816	arg2	residues					904:911	approximately 6-9 N-acetylgalactosamine residues	864:911	approximately 6-9 N-acetylgalactosamine residues	864:911	In human epidermoid carcinoma A-431 cells, the receptor precursor appears to contain one N-linked high mannose oligosaccharide and approximately 6-9 N-acetylgalactosamine residues linked O-glycosidically to Ser/Thr residues.
6317691	4	112	contain	contain	810:816	arg2	oligosaccharide					844:858	one N-linked high mannose oligosaccharide	818:858	one N-linked high mannose oligosaccharide	818:858	In human epidermoid carcinoma A-431 cells, the receptor precursor appears to contain one N-linked high mannose oligosaccharide and approximately 6-9 N-acetylgalactosamine residues linked O-glycosidically to Ser/Thr residues.
6317691	4	112	contain	contain	810:816	arg1	precursor					789:797	the receptor precursor	776:797	the receptor precursor	776:797	In human epidermoid carcinoma A-431 cells, the receptor precursor appears to contain one N-linked high mannose oligosaccharide and approximately 6-9 N-acetylgalactosamine residues linked O-glycosidically to Ser/Thr residues.
6317691	0	113	theme	oligosaccharides	32:47	arg1	Biosynthesis					0:11	Biosynthesis	0:11	Biosynthesis of N- and O-linked oligosaccharides of the low density lipoprotein receptor.	0:88	Biosynthesis of N- and O-linked oligosaccharides of the low density lipoprotein receptor.
6317691	7	114	theme	mature	1484:1489	arg1	receptor					1491:1498	the mature receptor	1480:1498	the mature receptor	1480:1498	Similar results were obtained with normal human fibroblast receptor except that the O-linked oligosaccharides on the precursor are neutral disaccharides, of which one component is GalNAc and the N-linked complex type unit on the mature receptor is less branched.
6317691	4	115	theme	N-acetylgalactosamine	882:902	arg1	residues					904:911	approximately 6-9 N-acetylgalactosamine residues	864:911	approximately 6-9 N-acetylgalactosamine residues	864:911	In human epidermoid carcinoma A-431 cells, the receptor precursor appears to contain one N-linked high mannose oligosaccharide and approximately 6-9 N-acetylgalactosamine residues linked O-glycosidically to Ser/Thr residues.
6317691	8	116	contain	containing	1789:1798	arg2	alpha-mannosidase					1822:1838	the processing enzyme alpha-mannosidase I	1800:1840	the processing enzyme alpha-mannosidase I	1800:1840	Since the addition of GalNAc residues to Ser/Thr residues precedes the conversion of N-linked high mannose-type oligosaccharides to complex-type structures, the transfer of N-acetylgalactosamine must occur prior to the entry of glycoproteins into the region of the Golgi containing the processing enzyme alpha-mannosidase I.
6317691	8	116	contain	containing	1789:1798	arg1	Golgi					1783:1787	the Golgi	1779:1787	the Golgi containing the processing enzyme alpha-mannosidase I	1779:1840	Since the addition of GalNAc residues to Ser/Thr residues precedes the conversion of N-linked high mannose-type oligosaccharides to complex-type structures, the transfer of N-acetylgalactosamine must occur prior to the entry of glycoproteins into the region of the Golgi containing the processing enzyme alpha-mannosidase I.
6317691	5	117	from	species	1039:1045	arg1	receptor					972:979	the mature receptor	961:979	the mature receptor	961:979	In the mature receptor, the O-linked oligosaccharides are mono- and disialylated species having the core structure of galactose leads to N-acetylgalactosamine leads to Ser/Thr.
6317691	1	118	theme	Mr	262:263	arg1	form					245:248	a mature form	236:248	a mature form of apparent Mr = 160,000, as determined by migration in sodium dodecyl sulfate (SDS)-polyacrylamide gels (Tolleshaug, H., Goldstein, J. L., Schneider, W. J., and Brown, M. S. (1982) Cell 30, 715-724)	236:448	In human fibroblasts, the receptor for low density lipoprotein (LDL) is synthesized as a precursor of apparent Mr = 120,000 which is converted to a mature form of apparent Mr = 160,000, as determined by migration in sodium dodecyl sulfate (SDS)-polyacrylamide gels (Tolleshaug, H., Goldstein, J. L., Schneider, W. J., and Brown, M. S. (1982) Cell 30, 715-724).
6317691	11	119	theme	apparent	2172:2179	arg1	addition					2313:2320	the addition	2309:2320	the addition of sialic acid and galactose residues to the O-linked GalNAc residues	2309:2390	These studies suggest that the apparent differences in molecular weight between the precursor and mature forms of the LDL receptor are largely, if not entirely, due to the addition of sialic acid and galactose residues to the O-linked GalNAc residues.
6317691	11	119	theme	apparent	2172:2179	arg1	differences					2181:2191	the apparent differences	2168:2191	the apparent differences in molecular weight between the precursor and mature forms of the LDL receptor	2168:2270	These studies suggest that the apparent differences in molecular weight between the precursor and mature forms of the LDL receptor are largely, if not entirely, due to the addition of sialic acid and galactose residues to the O-linked GalNAc residues.
6317691	5	120	theme	O-linked	986:993	arg1	species					1039:1045	mono- and disialylated species	1016:1045	mono- and disialylated species having the core structure of galactose leads to N-acetylgalactosamine leads to Ser/Thr	1016:1132	In the mature receptor, the O-linked oligosaccharides are mono- and disialylated species having the core structure of galactose leads to N-acetylgalactosamine leads to Ser/Thr.
6317691	5	120	theme	O-linked	986:993	arg1	oligosaccharides					995:1010	the O-linked oligosaccharides	982:1010	the O-linked oligosaccharides	982:1010	In the mature receptor, the O-linked oligosaccharides are mono- and disialylated species having the core structure of galactose leads to N-acetylgalactosamine leads to Ser/Thr.
6317691	7	121	theme	type	1467:1470	arg1	branched					1508:1515	branched	1508:1515	branched	1508:1515	Similar results were obtained with normal human fibroblast receptor except that the O-linked oligosaccharides on the precursor are neutral disaccharides, of which one component is GalNAc and the N-linked complex type unit on the mature receptor is less branched.
6317691	7	121	theme	type	1467:1470	arg1	unit					1472:1475	the N-linked complex type unit	1446:1475	the N-linked complex type unit on the mature receptor	1446:1498	Similar results were obtained with normal human fibroblast receptor except that the O-linked oligosaccharides on the precursor are neutral disaccharides, of which one component is GalNAc and the N-linked complex type unit on the mature receptor is less branched.
6317691	7	122	link	N-linked	1450:1457	arg1	branched					1508:1515	branched	1508:1515	branched	1508:1515	Similar results were obtained with normal human fibroblast receptor except that the O-linked oligosaccharides on the precursor are neutral disaccharides, of which one component is GalNAc and the N-linked complex type unit on the mature receptor is less branched.
6317691	7	122	link	N-linked	1450:1457	arg1	unit					1472:1475	the N-linked complex type unit	1446:1475	the N-linked complex type unit on the mature receptor	1446:1498	Similar results were obtained with normal human fibroblast receptor except that the O-linked oligosaccharides on the precursor are neutral disaccharides, of which one component is GalNAc and the N-linked complex type unit on the mature receptor is less branched.
6317691	8	123	theme	GalNAc	1540:1545	arg1	residues					1547:1554	GalNAc residues	1540:1554	GalNAc residues	1540:1554	Since the addition of GalNAc residues to Ser/Thr residues precedes the conversion of N-linked high mannose-type oligosaccharides to complex-type structures, the transfer of N-acetylgalactosamine must occur prior to the entry of glycoproteins into the region of the Golgi containing the processing enzyme alpha-mannosidase I.
6317691	8	124	theme	high	1612:1615	arg1	oligosaccharides					1630:1645	N-linked high mannose-type oligosaccharides	1603:1645	N-linked high mannose-type oligosaccharides	1603:1645	Since the addition of GalNAc residues to Ser/Thr residues precedes the conversion of N-linked high mannose-type oligosaccharides to complex-type structures, the transfer of N-acetylgalactosamine must occur prior to the entry of glycoproteins into the region of the Golgi containing the processing enzyme alpha-mannosidase I.
6317691	1	125	theme	Mr	201:202	arg1	receptor					116:123	the receptor	112:123	the receptor for low density lipoprotein (LDL)	112:157	In human fibroblasts, the receptor for low density lipoprotein (LDL) is synthesized as a precursor of apparent Mr = 120,000 which is converted to a mature form of apparent Mr = 160,000, as determined by migration in sodium dodecyl sulfate (SDS)-polyacrylamide gels (Tolleshaug, H., Goldstein, J. L., Schneider, W. J., and Brown, M. S. (1982) Cell 30, 715-724).
6317691	1	125	theme	Mr	201:202	arg1	precursor					179:187	a precursor	177:187	a precursor of apparent Mr = 120,000 which is converted to a mature form of apparent Mr = 160,000, as determined by migration in sodium dodecyl sulfate (SDS)-polyacrylamide gels (Tolleshaug, H., Goldstein, J. L., Schneider, W. J., and Brown, M. S. (1982) Cell 30, 715-724)	177:448	In human fibroblasts, the receptor for low density lipoprotein (LDL) is synthesized as a precursor of apparent Mr = 120,000 which is converted to a mature form of apparent Mr = 160,000, as determined by migration in sodium dodecyl sulfate (SDS)-polyacrylamide gels (Tolleshaug, H., Goldstein, J. L., Schneider, W. J., and Brown, M. S. (1982) Cell 30, 715-724).
6317691	7	126	theme	N-linked	1450:1457	arg1	branched					1508:1515	branched	1508:1515	branched	1508:1515	Similar results were obtained with normal human fibroblast receptor except that the O-linked oligosaccharides on the precursor are neutral disaccharides, of which one component is GalNAc and the N-linked complex type unit on the mature receptor is less branched.
6317691	7	126	theme	N-linked	1450:1457	arg1	unit					1472:1475	the N-linked complex type unit	1446:1475	the N-linked complex type unit on the mature receptor	1446:1498	Similar results were obtained with normal human fibroblast receptor except that the O-linked oligosaccharides on the precursor are neutral disaccharides, of which one component is GalNAc and the N-linked complex type unit on the mature receptor is less branched.
6317691	10	127	theme	ovary	2040:2044	arg1	cells					2046:2050	Chinese hamster ovary cells	2024:2050	Chinese hamster ovary cells that is deficient in adding galactose residues to both N- and O-linked oligosaccharides	2024:2138	In addition, we analyzed the receptor synthesized by a lectin-resistant clone of Chinese hamster ovary cells that is deficient in adding galactose residues to both N- and O-linked oligosaccharides.
6317691	8	128	theme	oligosaccharides	1630:1645	arg1	conversion					1589:1598	the conversion	1585:1598	the conversion of N-linked high mannose-type oligosaccharides to complex-type structures	1585:1672	Since the addition of GalNAc residues to Ser/Thr residues precedes the conversion of N-linked high mannose-type oligosaccharides to complex-type structures, the transfer of N-acetylgalactosamine must occur prior to the entry of glycoproteins into the region of the Golgi containing the processing enzyme alpha-mannosidase I.
6619126	7	0	theme	beta	1223:1226	arg1	GlcNAc					1216:1221	Gal(beta 1,3/4)GlcNAc	1201:1221	Gal(beta 1,3/4)GlcNAc(beta 1,6)]	1201:1232	Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc and NeuAc(alpha 2,3) Gal(beta 1,3)[Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc were the predominant species present.
6619126	7	0	theme	beta	1223:1226	arg1	1,6					1228:1230	beta 1,6	1223:1230	beta 1,6	1223:1230	Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc and NeuAc(alpha 2,3) Gal(beta 1,3)[Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc were the predominant species present.
6619126	9	1	theme	beta	1476:1479	arg1	beta					1495:1498	beta 1,?	1495:1502	beta	1495:1498	[Gal(beta 1,3/4)Glc-NAc(beta 1,?)]
6619126	9	1	theme	beta	1476:1479	arg1	Glc-NAc					1487:1493	[Gal(beta 1,3/4)Glc-NAc	1471:1493	[Gal(beta 1,3/4)Glc-NAc(beta 1,?)	1471:1503	[Gal(beta 1,3/4)Glc-NAc(beta 1,?)]
6619126	12	2	located	located	1962:1968	arg1	glycooctapeptide					1986:2001	the CNBr glycooctapeptide	1977:2001	the CNBr glycooctapeptide representing the NH2 terminus	1977:2031	The saccharides were linked to about 2-3 Ser and/or Thr residues in the donor LG glycoprotein and one of the attachment sites was located within the CNBr glycooctapeptide representing the NH2 terminus.
6619126	12	2	located	located	1962:1968	arg2	one					1930:1932	one	1930:1932	one	1930:1932	The saccharides were linked to about 2-3 Ser and/or Thr residues in the donor LG glycoprotein and one of the attachment sites was located within the CNBr glycooctapeptide representing the NH2 terminus.
6619126	12	2	located	located	1962:1968	arg2	sites					1952:1956	the attachment sites	1937:1956	the attachment sites	1937:1956	The saccharides were linked to about 2-3 Ser and/or Thr residues in the donor LG glycoprotein and one of the attachment sites was located within the CNBr glycooctapeptide representing the NH2 terminus.
6619126	12	3	from	Ser	1873:1875	arg1	glycoprotein					1913:1924	the donor LG glycoprotein	1900:1924	the donor LG glycoprotein	1900:1924	The saccharides were linked to about 2-3 Ser and/or Thr residues in the donor LG glycoprotein and one of the attachment sites was located within the CNBr glycooctapeptide representing the NH2 terminus.
6619126	5	4	dep	Gal	1046:1048	arg1	residues					1061:1068	residues	1061:1068	residues	1061:1068	The 6-O-linked GlcNAc appears to serve as the focus of further chain elongation reactions, involving alternate additions of Gal and GlcNAc residues and leading to the formation of several homologous structures.
6619126	7	5	theme	GlcNAc	1216:1221	arg1	H2GalNAc					1309:1316	Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc and NeuAc(alpha 2,3) Gal(beta 1,3)[Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc	1201:1316	Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc and NeuAc(alpha 2,3) Gal(beta 1,3)[Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc	1201:1316	Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc and NeuAc(alpha 2,3) Gal(beta 1,3)[Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc were the predominant species present.
6619126	7	5	theme	GlcNAc	1216:1221	arg1	species					1339:1345	the predominant species	1323:1345	the predominant species present	1323:1353	Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc and NeuAc(alpha 2,3) Gal(beta 1,3)[Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc were the predominant species present.
6619126	2	6	theme	MN	478:479	arg1	glycoproteins					481:493	the MN glycoproteins	474:493	the MN glycoproteins	474:493	This glycoprotein was found to be a carbohydrate variant in which, for both donors, certain O-glycosidically linked saccharides retained the core structure consisting of NeuAc(alpha 2,3)Gal(beta 1,3)GalNAc that is common to all O-linked saccharides of the MN glycoproteins, and, in addition, contained substituents, of varying chain lengths, on the primary carbinol of GalNAc.
6619126	14	7	theme	secretions	2334:2343	arg1	region					2249:2254	the core region	2240:2254	the core region of O-linked saccharides of certain blood group-active mucins and ovarian cyst secretions	2240:2343	The variant saccharides bear structural similarities to the core region of O-linked saccharides of certain blood group-active mucins and ovarian cyst secretions, and to the outer sequences of N-linked carbohydrate units (I-, i-active) of the major glycoprotein of human erythrocytes, band 3.
6619126	12	8	theme	sites	1952:1956	arg1	one					1930:1932	one	1930:1932	one	1930:1932	The saccharides were linked to about 2-3 Ser and/or Thr residues in the donor LG glycoprotein and one of the attachment sites was located within the CNBr glycooctapeptide representing the NH2 terminus.
6619126	12	8	theme	sites	1952:1956	arg1	sites					1952:1956	the attachment sites	1937:1956	the attachment sites	1937:1956	The saccharides were linked to about 2-3 Ser and/or Thr residues in the donor LG glycoprotein and one of the attachment sites was located within the CNBr glycooctapeptide representing the NH2 terminus.
6619126	1	9	attach	isolated	123:130	arg1	membranes					149:157	erythrocyte membranes	137:157	erythrocyte membranes of two individual donors, a mother (L.G.) and daughter (V.W.)	137:219	A variant of the MM glycoprotein (glycophorin A) was isolated from erythrocyte membranes of two individual donors, a mother (L.G.) and daughter (V.W.).
6619126	1	9	attach	isolated	123:130	arg2	variant					72:78	A variant	70:78	A variant of the MM glycoprotein (glycophorin A)	70:117	A variant of the MM glycoprotein (glycophorin A) was isolated from erythrocyte membranes of two individual donors, a mother (L.G.) and daughter (V.W.).
6619126	1	9	attach	isolated	123:130	arg2	A					116:116	glycophorin A	104:116	glycophorin A	104:116	A variant of the MM glycoprotein (glycophorin A) was isolated from erythrocyte membranes of two individual donors, a mother (L.G.) and daughter (V.W.).
6619126	14	10	theme	glycoprotein	2432:2443	arg1	units					2398:2402	N-linked carbohydrate units	2376:2402	N-linked carbohydrate units (I-, i-active) of the major glycoprotein of human erythrocytes, band 3	2376:2473	The variant saccharides bear structural similarities to the core region of O-linked saccharides of certain blood group-active mucins and ovarian cyst secretions, and to the outer sequences of N-linked carbohydrate units (I-, i-active) of the major glycoprotein of human erythrocytes, band 3.
6619126	1	11	theme	erythrocyte	137:147	arg1	membranes					149:157	erythrocyte membranes	137:157	erythrocyte membranes of two individual donors, a mother (L.G.) and daughter (V.W.)	137:219	A variant of the MM glycoprotein (glycophorin A) was isolated from erythrocyte membranes of two individual donors, a mother (L.G.) and daughter (V.W.).
6619126	15	12	theme	erythrocytes	2682:2693	arg1	protein					2671:2677	an integral protein	2659:2677	an integral protein of erythrocytes	2659:2693	The structures of the variant saccharides suggest that they may be potential precursors of H blood group-active carbohydrates, present in varying degrees of maturity, and attached to an integral protein of erythrocytes.
6619126	11	13	gly	glycopeptides	1700:1712	arg2	glycopeptides					1700:1712	two CNBr glycopeptides	1691:1712	two CNBr glycopeptides	1691:1712	Because the peptide portion of these glycoproteins contains two methionine residues, it was possible to isolate two CNBr glycopeptides from separate regions of the molecule, and to assess the distribution of these variant structures in the polypeptide.
6619126	14	14	theme	ovarian	2321:2327	arg1	secretions					2334:2343	ovarian cyst secretions	2321:2343	ovarian cyst secretions	2321:2343	The variant saccharides bear structural similarities to the core region of O-linked saccharides of certain blood group-active mucins and ovarian cyst secretions, and to the outer sequences of N-linked carbohydrate units (I-, i-active) of the major glycoprotein of human erythrocytes, band 3.
6619126	2	15	contain	contained	514:522	arg2	saccharides					338:348	certain O-glycosidically linked saccharides	306:348	certain O-glycosidically linked saccharides	306:348	This glycoprotein was found to be a carbohydrate variant in which, for both donors, certain O-glycosidically linked saccharides retained the core structure consisting of NeuAc(alpha 2,3)Gal(beta 1,3)GalNAc that is common to all O-linked saccharides of the MN glycoproteins, and, in addition, contained substituents, of varying chain lengths, on the primary carbinol of GalNAc.
6619126	2	15	contain	contained	514:522	arg1	saccharides					338:348	certain O-glycosidically linked saccharides	306:348	certain O-glycosidically linked saccharides	306:348	This glycoprotein was found to be a carbohydrate variant in which, for both donors, certain O-glycosidically linked saccharides retained the core structure consisting of NeuAc(alpha 2,3)Gal(beta 1,3)GalNAc that is common to all O-linked saccharides of the MN glycoproteins, and, in addition, contained substituents, of varying chain lengths, on the primary carbinol of GalNAc.
6619126	2	15	contain	contained	514:522	arg1	carbinol					579:586	the primary carbinol	567:586	the primary carbinol of GalNAc	567:596	This glycoprotein was found to be a carbohydrate variant in which, for both donors, certain O-glycosidically linked saccharides retained the core structure consisting of NeuAc(alpha 2,3)Gal(beta 1,3)GalNAc that is common to all O-linked saccharides of the MN glycoproteins, and, in addition, contained substituents, of varying chain lengths, on the primary carbinol of GalNAc.
6619126	2	15	contain	contained	514:522	arg2	substituents					524:535	substituents	524:535	substituents	524:535	This glycoprotein was found to be a carbohydrate variant in which, for both donors, certain O-glycosidically linked saccharides retained the core structure consisting of NeuAc(alpha 2,3)Gal(beta 1,3)GalNAc that is common to all O-linked saccharides of the MN glycoproteins, and, in addition, contained substituents, of varying chain lengths, on the primary carbinol of GalNAc.
6619126	13	16	theme	such	2137:2140	arg1	heterogeneity					2142:2154	such heterogeneity	2137:2154	such heterogeneity	2137:2154	Considerable heterogeneity in saccharide structure was documented for this site, and it is likely that such heterogeneity occurs also at other sites.
6619126	12	17	attach	linked	1853:1858	arg2	saccharides					1836:1846	The saccharides	1832:1846	The saccharides	1832:1846	The saccharides were linked to about 2-3 Ser and/or Thr residues in the donor LG glycoprotein and one of the attachment sites was located within the CNBr glycooctapeptide representing the NH2 terminus.
6619126	12	17	attach	linked	1853:1858	arg1	Ser					1873:1875	about 2-3 Ser and/or Thr residues	1863:1895	Ser	1873:1875	The saccharides were linked to about 2-3 Ser and/or Thr residues in the donor LG glycoprotein and one of the attachment sites was located within the CNBr glycooctapeptide representing the NH2 terminus.
6619126	12	17	attach	linked	1853:1858	arg1	residues					1888:1895	about 2-3 Ser and/or Thr residues	1863:1895	residues	1888:1895	The saccharides were linked to about 2-3 Ser and/or Thr residues in the donor LG glycoprotein and one of the attachment sites was located within the CNBr glycooctapeptide representing the NH2 terminus.
6619126	14	18	theme	mucins	2310:2315	arg1	secretions					2334:2343	ovarian cyst secretions	2321:2343	ovarian cyst secretions	2321:2343	The variant saccharides bear structural similarities to the core region of O-linked saccharides of certain blood group-active mucins and ovarian cyst secretions, and to the outer sequences of N-linked carbohydrate units (I-, i-active) of the major glycoprotein of human erythrocytes, band 3.
6619126	14	18	theme	mucins	2310:2315	arg1	saccharides					2268:2278	O-linked saccharides	2259:2278	O-linked saccharides of certain blood group-active mucins	2259:2315	The variant saccharides bear structural similarities to the core region of O-linked saccharides of certain blood group-active mucins and ovarian cyst secretions, and to the outer sequences of N-linked carbohydrate units (I-, i-active) of the major glycoprotein of human erythrocytes, band 3.
6619126	14	19	theme	carbohydrate	2385:2396	arg1	units					2398:2402	N-linked carbohydrate units	2376:2402	N-linked carbohydrate units (I-, i-active) of the major glycoprotein of human erythrocytes, band 3	2376:2473	The variant saccharides bear structural similarities to the core region of O-linked saccharides of certain blood group-active mucins and ovarian cyst secretions, and to the outer sequences of N-linked carbohydrate units (I-, i-active) of the major glycoprotein of human erythrocytes, band 3.
6619126	7	20	dep	beta	1267:1270	arg1	1,3					1272:1274	1,3	1272:1274	1,3	1272:1274	Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc and NeuAc(alpha 2,3) Gal(beta 1,3)[Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc were the predominant species present.
6619126	7	20	dep	beta	1267:1270	arg1	GlcNAc					1292:1297	[Gal(beta 1,3/4)GlcNAc	1276:1297	beta 1,3)[Gal(beta 1,3/4)GlcNAc(beta 1,6)	1267:1307	Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc and NeuAc(alpha 2,3) Gal(beta 1,3)[Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc were the predominant species present.
6619126	1	21	theme	individual	166:175	arg1	daughter					205:212	daughter	205:212	daughter	205:212	A variant of the MM glycoprotein (glycophorin A) was isolated from erythrocyte membranes of two individual donors, a mother (L.G.) and daughter (V.W.).
6619126	1	21	theme	individual	166:175	arg1	donors					177:182	two individual donors	162:182	two individual donors	162:182	A variant of the MM glycoprotein (glycophorin A) was isolated from erythrocyte membranes of two individual donors, a mother (L.G.) and daughter (V.W.).
6619126	1	21	theme	individual	166:175	arg1	mother					187:192	a mother	185:192	a mother (L.G.)	185:199	A variant of the MM glycoprotein (glycophorin A) was isolated from erythrocyte membranes of two individual donors, a mother (L.G.) and daughter (V.W.).
6619126	12	22	theme	NH2	2020:2022	arg1	terminus					2024:2031	the NH2 terminus	2016:2031	the NH2 terminus	2016:2031	The saccharides were linked to about 2-3 Ser and/or Thr residues in the donor LG glycoprotein and one of the attachment sites was located within the CNBr glycooctapeptide representing the NH2 terminus.
6619126	14	23	theme	blood	2291:2295	arg1	mucins					2310:2315	certain blood group-active mucins	2283:2315	certain blood group-active mucins	2283:2315	The variant saccharides bear structural similarities to the core region of O-linked saccharides of certain blood group-active mucins and ovarian cyst secretions, and to the outer sequences of N-linked carbohydrate units (I-, i-active) of the major glycoprotein of human erythrocytes, band 3.
6619126	14	24	theme	units	2398:2402	arg1	sequences					2363:2371	the outer sequences	2353:2371	the outer sequences of N-linked carbohydrate units (I-, i-active) of the major glycoprotein of human erythrocytes, band 3	2353:2473	The variant saccharides bear structural similarities to the core region of O-linked saccharides of certain blood group-active mucins and ovarian cyst secretions, and to the outer sequences of N-linked carbohydrate units (I-, i-active) of the major glycoprotein of human erythrocytes, band 3.
6619126	10	25	theme	beta	1528:1531	arg1	1,3					1564:1566	beta 1,3	1559:1566	beta 1,3	1559:1566	Gal(beta 1,3/4)GlcNAc(beta 1,6)[NeuAc(alpha 2,3)Gal-(beta 1,3)]H2GalNAc.
6619126	10	25	theme	beta	1528:1531	arg1	Gal-					1554:1557	beta 1,3/4)GlcNAc(beta 1,6)[NeuAc(alpha 2,3)Gal-	1510:1557	beta 1,3/4)GlcNAc(beta 1,6)[NeuAc(alpha 2,3)Gal-(beta 1,3)	1510:1567	Gal(beta 1,3/4)GlcNAc(beta 1,6)[NeuAc(alpha 2,3)Gal-(beta 1,3)]H2GalNAc.
6619126	6	26	theme	such	1137:1140	arg1	structures					1142:1151	Two such structures	1133:1151	Two such structures	1133:1151	Two such structures, NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1,?)
6619126	6	26	theme	such	1137:1140	arg1	beta					1191:1194	NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1	1154:1196	NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1	1154:1196	Two such structures, NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1,?)
6619126	11	27	theme	methionine	1643:1652	arg1	residues					1654:1661	two methionine residues	1639:1661	two methionine residues	1639:1661	Because the peptide portion of these glycoproteins contains two methionine residues, it was possible to isolate two CNBr glycopeptides from separate regions of the molecule, and to assess the distribution of these variant structures in the polypeptide.
6619126	8	28	theme	partial	1402:1408	arg1	sequence					1410:1417	its partial sequence	1398:1417	its partial sequence	1398:1417	A larger saccharide was also isolated and its partial sequence was determined to be Gal(beta 1,3/4)GlcNAc(beta 1,?)
6619126	15	29	theme	potential	2543:2551	arg1	precursors					2553:2562	potential precursors	2543:2562	potential precursors of H blood group-active carbohydrates	2543:2600	The structures of the variant saccharides suggest that they may be potential precursors of H blood group-active carbohydrates, present in varying degrees of maturity, and attached to an integral protein of erythrocytes.
6619126	7	30	dep	GlcNAc	1216:1221	arg1	Gal					1263:1265	Gal	1263:1265	Gal	1263:1265	Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc and NeuAc(alpha 2,3) Gal(beta 1,3)[Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc were the predominant species present.
6619126	7	30	dep	GlcNAc	1216:1221	arg1	H2GalNAc					1233:1240	H2GalNAc	1233:1240	H2GalNAc	1233:1240	Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc and NeuAc(alpha 2,3) Gal(beta 1,3)[Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc were the predominant species present.
6619126	14	31	theme	erythrocytes	2454:2465	arg1	band					2468:2471	band 3	2468:2473	band 3	2468:2473	The variant saccharides bear structural similarities to the core region of O-linked saccharides of certain blood group-active mucins and ovarian cyst secretions, and to the outer sequences of N-linked carbohydrate units (I-, i-active) of the major glycoprotein of human erythrocytes, band 3.
6619126	14	31	theme	erythrocytes	2454:2465	arg1	glycoprotein					2432:2443	the major glycoprotein	2422:2443	the major glycoprotein of human erythrocytes	2422:2465	The variant saccharides bear structural similarities to the core region of O-linked saccharides of certain blood group-active mucins and ovarian cyst secretions, and to the outer sequences of N-linked carbohydrate units (I-, i-active) of the major glycoprotein of human erythrocytes, band 3.
6619126	13	32	from	heterogeneity	2047:2059	arg1	structure					2075:2083	saccharide structure	2064:2083	saccharide structure	2064:2083	Considerable heterogeneity in saccharide structure was documented for this site, and it is likely that such heterogeneity occurs also at other sites.
6619126	10	33	theme	GlcNAc	1521:1526	arg1	1,3					1564:1566	beta 1,3	1559:1566	beta 1,3	1559:1566	Gal(beta 1,3/4)GlcNAc(beta 1,6)[NeuAc(alpha 2,3)Gal-(beta 1,3)]H2GalNAc.
6619126	10	33	theme	GlcNAc	1521:1526	arg1	Gal-					1554:1557	beta 1,3/4)GlcNAc(beta 1,6)[NeuAc(alpha 2,3)Gal-	1510:1557	beta 1,3/4)GlcNAc(beta 1,6)[NeuAc(alpha 2,3)Gal-(beta 1,3)	1510:1567	Gal(beta 1,3/4)GlcNAc(beta 1,6)[NeuAc(alpha 2,3)Gal-(beta 1,3)]H2GalNAc.
6619126	14	34	theme	outer	2357:2361	arg1	sequences					2363:2371	the outer sequences	2353:2371	the outer sequences of N-linked carbohydrate units (I-, i-active) of the major glycoprotein of human erythrocytes, band 3	2353:2473	The variant saccharides bear structural similarities to the core region of O-linked saccharides of certain blood group-active mucins and ovarian cyst secretions, and to the outer sequences of N-linked carbohydrate units (I-, i-active) of the major glycoprotein of human erythrocytes, band 3.
6619126	1	35	theme	glycoprotein	90:101	arg1	variant					72:78	A variant	70:78	A variant of the MM glycoprotein (glycophorin A)	70:117	A variant of the MM glycoprotein (glycophorin A) was isolated from erythrocyte membranes of two individual donors, a mother (L.G.) and daughter (V.W.).
6619126	1	35	theme	glycoprotein	90:101	arg1	A					116:116	glycophorin A	104:116	glycophorin A	104:116	A variant of the MM glycoprotein (glycophorin A) was isolated from erythrocyte membranes of two individual donors, a mother (L.G.) and daughter (V.W.).
6619126	7	36	theme	beta	1281:1284	arg1	GlcNAc					1292:1297	[Gal(beta 1,3/4)GlcNAc	1276:1297	beta 1,3)[Gal(beta 1,3/4)GlcNAc(beta 1,6)	1267:1307	Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc and NeuAc(alpha 2,3) Gal(beta 1,3)[Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc were the predominant species present.
6619126	2	37	theme	O-linked	450:457	arg1	saccharides					459:469	all O-linked saccharides	446:469	all O-linked saccharides of the MN glycoproteins	446:493	This glycoprotein was found to be a carbohydrate variant in which, for both donors, certain O-glycosidically linked saccharides retained the core structure consisting of NeuAc(alpha 2,3)Gal(beta 1,3)GalNAc that is common to all O-linked saccharides of the MN glycoproteins, and, in addition, contained substituents, of varying chain lengths, on the primary carbinol of GalNAc.
6619126	14	38	theme	O-linked	2259:2266	arg1	saccharides					2268:2278	O-linked saccharides	2259:2278	O-linked saccharides of certain blood group-active mucins	2259:2315	The variant saccharides bear structural similarities to the core region of O-linked saccharides of certain blood group-active mucins and ovarian cyst secretions, and to the outer sequences of N-linked carbohydrate units (I-, i-active) of the major glycoprotein of human erythrocytes, band 3.
6619126	1	39	theme	glycophorin	104:114	arg1	variant					72:78	A variant	70:78	A variant of the MM glycoprotein (glycophorin A)	70:117	A variant of the MM glycoprotein (glycophorin A) was isolated from erythrocyte membranes of two individual donors, a mother (L.G.) and daughter (V.W.).
6619126	1	39	theme	glycophorin	104:114	arg1	A					116:116	glycophorin A	104:116	glycophorin A	104:116	A variant of the MM glycoprotein (glycophorin A) was isolated from erythrocyte membranes of two individual donors, a mother (L.G.) and daughter (V.W.).
6619126	7	40	theme	[Gal	1276:1279	arg1	GlcNAc					1292:1297	[Gal(beta 1,3/4)GlcNAc	1276:1297	beta 1,3)[Gal(beta 1,3/4)GlcNAc(beta 1,6)	1267:1307	Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc and NeuAc(alpha 2,3) Gal(beta 1,3)[Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc were the predominant species present.
6619126	2	41	theme	GalNAc	591:596	arg1	carbinol					579:586	the primary carbinol	567:586	the primary carbinol of GalNAc	567:596	This glycoprotein was found to be a carbohydrate variant in which, for both donors, certain O-glycosidically linked saccharides retained the core structure consisting of NeuAc(alpha 2,3)Gal(beta 1,3)GalNAc that is common to all O-linked saccharides of the MN glycoproteins, and, in addition, contained substituents, of varying chain lengths, on the primary carbinol of GalNAc.
6619126	5	42	theme	several	1102:1108	arg1	structures					1121:1130	several homologous structures	1102:1130	several homologous structures	1102:1130	The 6-O-linked GlcNAc appears to serve as the focus of further chain elongation reactions, involving alternate additions of Gal and GlcNAc residues and leading to the formation of several homologous structures.
6619126	6	43	theme	beta	1174:1177	arg1	structures					1142:1151	Two such structures	1133:1151	Two such structures	1133:1151	Two such structures, NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1,?)
6619126	6	43	theme	beta	1174:1177	arg1	beta					1191:1194	NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1	1154:1196	NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1	1154:1196	Two such structures, NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1,?)
6619126	8	44	theme	Gal	1440:1442	arg1	GlcNAc					1455:1460	Gal(beta 1,3/4)GlcNAc	1440:1460	Gal(beta 1,3/4)GlcNAc	1440:1460	A larger saccharide was also isolated and its partial sequence was determined to be Gal(beta 1,3/4)GlcNAc(beta 1,?)
6619126	15	45	theme	varying	2614:2620	arg1	degrees					2622:2628	varying degrees	2614:2628	varying degrees of maturity	2614:2640	The structures of the variant saccharides suggest that they may be potential precursors of H blood group-active carbohydrates, present in varying degrees of maturity, and attached to an integral protein of erythrocytes.
6619126	5	46	dep	reactions	1002:1010	arg1	leading					1074:1080	leading	1074:1080	leading to the formation of several homologous structures	1074:1130	The 6-O-linked GlcNAc appears to serve as the focus of further chain elongation reactions, involving alternate additions of Gal and GlcNAc residues and leading to the formation of several homologous structures.
6619126	5	46	dep	reactions	1002:1010	arg1	involving					1013:1021	involving	1013:1021	involving alternate additions of Gal and GlcNAc residues	1013:1068	The 6-O-linked GlcNAc appears to serve as the focus of further chain elongation reactions, involving alternate additions of Gal and GlcNAc residues and leading to the formation of several homologous structures.
6619126	3	47	theme	borohydride	698:708	arg1	presence					679:686	the presence	675:686	the presence of sodium borohydride	675:708	These saccharides were released from the polypeptide by beta-elimination in the presence of sodium borohydride, and aspects of their structure were investigated by glycosidase digestion and periodate oxidation.
6619126	6	48	theme	Gal	1170:1172	arg1	structures					1142:1151	Two such structures	1133:1151	Two such structures	1133:1151	Two such structures, NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1,?)
6619126	6	48	theme	Gal	1170:1172	arg1	beta					1191:1194	NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1	1154:1196	NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1	1154:1196	Two such structures, NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1,?)
6619126	3	49	theme	structure	732:740	arg1	aspects					715:721	aspects	715:721	aspects of their structure	715:740	These saccharides were released from the polypeptide by beta-elimination in the presence of sodium borohydride, and aspects of their structure were investigated by glycosidase digestion and periodate oxidation.
6619126	4	50	theme	smallest	820:827	arg1	H2GalNAc					912:919	NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1,6)]H2GalNAc	865:919	NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1,6)]H2GalNAc	865:919	Thus, the smallest variant structure was deduced to be NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1,6)]H2GalNAc.
6619126	4	50	theme	smallest	820:827	arg1	structure					837:845	the smallest variant structure	816:845	the smallest variant structure	816:845	Thus, the smallest variant structure was deduced to be NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1,6)]H2GalNAc.
6619126	8	51	dep	isolated	1385:1392	arg1	beta					1462:1465	beta 1,?	1462:1469	beta	1462:1465	A larger saccharide was also isolated and its partial sequence was determined to be Gal(beta 1,3/4)GlcNAc(beta 1,?)
6619126	10	52	theme	2,3	1550:1552	arg1	1,3					1564:1566	beta 1,3	1559:1566	beta 1,3	1559:1566	Gal(beta 1,3/4)GlcNAc(beta 1,6)[NeuAc(alpha 2,3)Gal-(beta 1,3)]H2GalNAc.
6619126	10	52	theme	2,3	1550:1552	arg1	Gal-					1554:1557	beta 1,3/4)GlcNAc(beta 1,6)[NeuAc(alpha 2,3)Gal-	1510:1557	beta 1,3/4)GlcNAc(beta 1,6)[NeuAc(alpha 2,3)Gal-(beta 1,3)	1510:1567	Gal(beta 1,3/4)GlcNAc(beta 1,6)[NeuAc(alpha 2,3)Gal-(beta 1,3)]H2GalNAc.
6619126	6	53	theme	2,3	1166:1168	arg1	structures					1142:1151	Two such structures	1133:1151	Two such structures	1133:1151	Two such structures, NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1,?)
6619126	6	53	theme	2,3	1166:1168	arg1	beta					1191:1194	NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1	1154:1196	NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1	1154:1196	Two such structures, NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1,?)
6619126	15	54	attach	attached	2647:2654	arg2	they					2531:2534	they	2531:2534	they	2531:2534	The structures of the variant saccharides suggest that they may be potential precursors of H blood group-active carbohydrates, present in varying degrees of maturity, and attached to an integral protein of erythrocytes.
6619126	15	54	attach	attached	2647:2654	arg1	protein					2671:2677	an integral protein	2659:2677	an integral protein of erythrocytes	2659:2693	The structures of the variant saccharides suggest that they may be potential precursors of H blood group-active carbohydrates, present in varying degrees of maturity, and attached to an integral protein of erythrocytes.
6619126	15	55	theme	carbohydrates	2588:2600	arg1	precursors					2553:2562	potential precursors	2543:2562	potential precursors of H blood group-active carbohydrates	2543:2600	The structures of the variant saccharides suggest that they may be potential precursors of H blood group-active carbohydrates, present in varying degrees of maturity, and attached to an integral protein of erythrocytes.
6619126	2	56	theme	1,3	417:419	arg1	GalNAc					421:426	NeuAc(alpha 2,3)Gal(beta 1,3)GalNAc	392:426	NeuAc(alpha 2,3)Gal(beta 1,3)GalNAc that is common to all O-linked saccharides of the MN glycoproteins	392:493	This glycoprotein was found to be a carbohydrate variant in which, for both donors, certain O-glycosidically linked saccharides retained the core structure consisting of NeuAc(alpha 2,3)Gal(beta 1,3)GalNAc that is common to all O-linked saccharides of the MN glycoproteins, and, in addition, contained substituents, of varying chain lengths, on the primary carbinol of GalNAc.
6619126	10	57	dep	Gal	1506:1508	arg1	1,3					1564:1566	beta 1,3	1559:1566	beta 1,3	1559:1566	Gal(beta 1,3/4)GlcNAc(beta 1,6)[NeuAc(alpha 2,3)Gal-(beta 1,3)]H2GalNAc.
6619126	10	57	dep	Gal	1506:1508	arg1	Gal-					1554:1557	beta 1,3/4)GlcNAc(beta 1,6)[NeuAc(alpha 2,3)Gal-	1510:1557	beta 1,3/4)GlcNAc(beta 1,6)[NeuAc(alpha 2,3)Gal-(beta 1,3)	1510:1567	Gal(beta 1,3/4)GlcNAc(beta 1,6)[NeuAc(alpha 2,3)Gal-(beta 1,3)]H2GalNAc.
6619126	2	58	theme	certain	306:312	arg1	saccharides					338:348	certain O-glycosidically linked saccharides	306:348	certain O-glycosidically linked saccharides	306:348	This glycoprotein was found to be a carbohydrate variant in which, for both donors, certain O-glycosidically linked saccharides retained the core structure consisting of NeuAc(alpha 2,3)Gal(beta 1,3)GalNAc that is common to all O-linked saccharides of the MN glycoproteins, and, in addition, contained substituents, of varying chain lengths, on the primary carbinol of GalNAc.
6619126	13	59	theme	Considerable	2034:2045	arg1	heterogeneity					2047:2059	Considerable heterogeneity	2034:2059	Considerable heterogeneity in saccharide structure	2034:2083	Considerable heterogeneity in saccharide structure was documented for this site, and it is likely that such heterogeneity occurs also at other sites.
6619126	3	60	theme	glycosidase	763:773	arg1	digestion					775:783	glycosidase digestion	763:783	glycosidase digestion	763:783	These saccharides were released from the polypeptide by beta-elimination in the presence of sodium borohydride, and aspects of their structure were investigated by glycosidase digestion and periodate oxidation.
6619126	4	61	theme	Gal	881:883	arg1	H2GalNAc					912:919	NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1,6)]H2GalNAc	865:919	NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1,6)]H2GalNAc	865:919	Thus, the smallest variant structure was deduced to be NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1,6)]H2GalNAc.
6619126	4	61	theme	Gal	881:883	arg1	structure					837:845	the smallest variant structure	816:845	the smallest variant structure	816:845	Thus, the smallest variant structure was deduced to be NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1,6)]H2GalNAc.
6619126	2	62	theme	chain	549:553	arg1	lengths					555:561	varying chain lengths	541:561	varying chain lengths	541:561	This glycoprotein was found to be a carbohydrate variant in which, for both donors, certain O-glycosidically linked saccharides retained the core structure consisting of NeuAc(alpha 2,3)Gal(beta 1,3)GalNAc that is common to all O-linked saccharides of the MN glycoproteins, and, in addition, contained substituents, of varying chain lengths, on the primary carbinol of GalNAc.
6619126	5	63	theme	further	977:983	arg1	reactions					1002:1010	further chain elongation reactions	977:1010	further chain elongation reactions	977:1010	The 6-O-linked GlcNAc appears to serve as the focus of further chain elongation reactions, involving alternate additions of Gal and GlcNAc residues and leading to the formation of several homologous structures.
6619126	14	64	theme	structural	2213:2222	arg1	similarities					2224:2235	structural similarities	2213:2235	structural similarities to the core region of O-linked saccharides of certain blood group-active mucins and ovarian cyst secretions, and to the outer sequences of N-linked carbohydrate units (I-, i-active) of the major glycoprotein of human erythrocytes, band 3	2213:2473	The variant saccharides bear structural similarities to the core region of O-linked saccharides of certain blood group-active mucins and ovarian cyst secretions, and to the outer sequences of N-linked carbohydrate units (I-, i-active) of the major glycoprotein of human erythrocytes, band 3.
6619126	2	65	theme	core	363:366	arg1	structure					368:376	the core structure	359:376	the core structure consisting of NeuAc(alpha 2,3)Gal(beta 1,3)GalNAc that is common to all O-linked saccharides of the MN glycoproteins	359:493	This glycoprotein was found to be a carbohydrate variant in which, for both donors, certain O-glycosidically linked saccharides retained the core structure consisting of NeuAc(alpha 2,3)Gal(beta 1,3)GalNAc that is common to all O-linked saccharides of the MN glycoproteins, and, in addition, contained substituents, of varying chain lengths, on the primary carbinol of GalNAc.
6619126	12	66	theme	donor	1904:1908	arg1	glycoprotein					1913:1924	the donor LG glycoprotein	1900:1924	the donor LG glycoprotein	1900:1924	The saccharides were linked to about 2-3 Ser and/or Thr residues in the donor LG glycoprotein and one of the attachment sites was located within the CNBr glycooctapeptide representing the NH2 terminus.
6619126	5	67	theme	structures	1121:1130	arg1	formation					1089:1097	the formation	1085:1097	the formation of several homologous structures	1085:1130	The 6-O-linked GlcNAc appears to serve as the focus of further chain elongation reactions, involving alternate additions of Gal and GlcNAc residues and leading to the formation of several homologous structures.
6619126	0	68	theme	structural	15:24	arg1	variant					26:32	A carbohydrate structural variant	0:32	A carbohydrate structural variant of MM glycoprotein (glycophorin A)	0:67	A carbohydrate structural variant of MM glycoprotein (glycophorin A).
6619126	0	68	theme	structural	15:24	arg1	A					66:66	glycophorin A	54:66	glycophorin A	54:66	A carbohydrate structural variant of MM glycoprotein (glycophorin A).
6619126	5	69	theme	elongation	991:1000	arg1	reactions					1002:1010	further chain elongation reactions	977:1010	further chain elongation reactions	977:1010	The 6-O-linked GlcNAc appears to serve as the focus of further chain elongation reactions, involving alternate additions of Gal and GlcNAc residues and leading to the formation of several homologous structures.
6619126	15	70	theme	integral	2662:2669	arg1	protein					2671:2677	an integral protein	2659:2677	an integral protein of erythrocytes	2659:2693	The structures of the variant saccharides suggest that they may be potential precursors of H blood group-active carbohydrates, present in varying degrees of maturity, and attached to an integral protein of erythrocytes.
6619126	2	71	theme	alpha	398:402	arg1	GalNAc					421:426	NeuAc(alpha 2,3)Gal(beta 1,3)GalNAc	392:426	NeuAc(alpha 2,3)Gal(beta 1,3)GalNAc that is common to all O-linked saccharides of the MN glycoproteins	392:493	This glycoprotein was found to be a carbohydrate variant in which, for both donors, certain O-glycosidically linked saccharides retained the core structure consisting of NeuAc(alpha 2,3)Gal(beta 1,3)GalNAc that is common to all O-linked saccharides of the MN glycoproteins, and, in addition, contained substituents, of varying chain lengths, on the primary carbinol of GalNAc.
6619126	2	72	theme	linked	331:336	arg1	saccharides					338:348	certain O-glycosidically linked saccharides	306:348	certain O-glycosidically linked saccharides	306:348	This glycoprotein was found to be a carbohydrate variant in which, for both donors, certain O-glycosidically linked saccharides retained the core structure consisting of NeuAc(alpha 2,3)Gal(beta 1,3)GalNAc that is common to all O-linked saccharides of the MN glycoproteins, and, in addition, contained substituents, of varying chain lengths, on the primary carbinol of GalNAc.
6619126	14	73	theme	human	2448:2452	arg1	erythrocytes					2454:2465	human erythrocytes	2448:2465	human erythrocytes	2448:2465	The variant saccharides bear structural similarities to the core region of O-linked saccharides of certain blood group-active mucins and ovarian cyst secretions, and to the outer sequences of N-linked carbohydrate units (I-, i-active) of the major glycoprotein of human erythrocytes, band 3.
6619126	7	74	dep	Gal	1201:1203	arg1	beta					1205:1208	beta 1,3/4	1205:1214	beta 1,3/4	1205:1214	Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc and NeuAc(alpha 2,3) Gal(beta 1,3)[Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc were the predominant species present.
6619126	15	75	from	present	2603:2609	arg1	degrees					2622:2628	varying degrees	2614:2628	varying degrees of maturity	2614:2640	The structures of the variant saccharides suggest that they may be potential precursors of H blood group-active carbohydrates, present in varying degrees of maturity, and attached to an integral protein of erythrocytes.
6619126	4	76	theme	2,3	877:879	arg1	Gal					881:883	NeuAc(alpha 2,3)Gal	865:883	NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1,6)]H2GalNAc	865:919	Thus, the smallest variant structure was deduced to be NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1,6)]H2GalNAc.
6619126	4	76	theme	2,3	877:879	arg1	beta					885:888	beta 1,3)[GlcNAc(beta 1,6)	885:910	beta 1,3)[GlcNAc(beta 1,6)	885:910	Thus, the smallest variant structure was deduced to be NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1,6)]H2GalNAc.
6619126	12	77	theme	Thr	1884:1886	arg1	residues					1888:1895	about 2-3 Ser and/or Thr residues	1863:1895	residues	1888:1895	The saccharides were linked to about 2-3 Ser and/or Thr residues in the donor LG glycoprotein and one of the attachment sites was located within the CNBr glycooctapeptide representing the NH2 terminus.
6619126	0	78	theme	glycophorin	54:64	arg1	variant					26:32	A carbohydrate structural variant	0:32	A carbohydrate structural variant of MM glycoprotein (glycophorin A)	0:67	A carbohydrate structural variant of MM glycoprotein (glycophorin A).
6619126	0	78	theme	glycophorin	54:64	arg1	A					66:66	glycophorin A	54:66	glycophorin A	54:66	A carbohydrate structural variant of MM glycoprotein (glycophorin A).
6619126	0	79	theme	glycoprotein	40:51	arg1	variant					26:32	A carbohydrate structural variant	0:32	A carbohydrate structural variant of MM glycoprotein (glycophorin A)	0:67	A carbohydrate structural variant of MM glycoprotein (glycophorin A).
6619126	0	79	theme	glycoprotein	40:51	arg1	A					66:66	glycophorin A	54:66	glycophorin A	54:66	A carbohydrate structural variant of MM glycoprotein (glycophorin A).
6619126	8	80	dep	Gal	1440:1442	arg1	beta					1444:1447	beta 1,3/4	1444:1453	beta 1,3/4	1444:1453	A larger saccharide was also isolated and its partial sequence was determined to be Gal(beta 1,3/4)GlcNAc(beta 1,?)
6619126	10	81	theme	alpha	1544:1548	arg1	1,3					1564:1566	beta 1,3	1559:1566	beta 1,3	1559:1566	Gal(beta 1,3/4)GlcNAc(beta 1,6)[NeuAc(alpha 2,3)Gal-(beta 1,3)]H2GalNAc.
6619126	10	81	theme	alpha	1544:1548	arg1	Gal-					1554:1557	beta 1,3/4)GlcNAc(beta 1,6)[NeuAc(alpha 2,3)Gal-	1510:1557	beta 1,3/4)GlcNAc(beta 1,6)[NeuAc(alpha 2,3)Gal-(beta 1,3)	1510:1567	Gal(beta 1,3/4)GlcNAc(beta 1,6)[NeuAc(alpha 2,3)Gal-(beta 1,3)]H2GalNAc.
6619126	15	82	theme	saccharides	2506:2516	arg1	structures					2480:2489	The structures	2476:2489	The structures of the variant saccharides	2476:2516	The structures of the variant saccharides suggest that they may be potential precursors of H blood group-active carbohydrates, present in varying degrees of maturity, and attached to an integral protein of erythrocytes.
6619126	10	83	theme	beta	1559:1562	arg1	1,3					1564:1566	beta 1,3	1559:1566	beta 1,3	1559:1566	Gal(beta 1,3/4)GlcNAc(beta 1,6)[NeuAc(alpha 2,3)Gal-(beta 1,3)]H2GalNAc.
6619126	10	83	theme	beta	1559:1562	arg1	Gal-					1554:1557	beta 1,3/4)GlcNAc(beta 1,6)[NeuAc(alpha 2,3)Gal-	1510:1557	beta 1,3/4)GlcNAc(beta 1,6)[NeuAc(alpha 2,3)Gal-(beta 1,3)	1510:1567	Gal(beta 1,3/4)GlcNAc(beta 1,6)[NeuAc(alpha 2,3)Gal-(beta 1,3)]H2GalNAc.
6619126	2	84	theme	NeuAc	392:396	arg1	GalNAc					421:426	NeuAc(alpha 2,3)Gal(beta 1,3)GalNAc	392:426	NeuAc(alpha 2,3)Gal(beta 1,3)GalNAc that is common to all O-linked saccharides of the MN glycoproteins	392:493	This glycoprotein was found to be a carbohydrate variant in which, for both donors, certain O-glycosidically linked saccharides retained the core structure consisting of NeuAc(alpha 2,3)Gal(beta 1,3)GalNAc that is common to all O-linked saccharides of the MN glycoproteins, and, in addition, contained substituents, of varying chain lengths, on the primary carbinol of GalNAc.
6619126	12	85	theme	CNBr	1981:1984	arg1	glycooctapeptide					1986:2001	the CNBr glycooctapeptide	1977:2001	the CNBr glycooctapeptide representing the NH2 terminus	1977:2031	The saccharides were linked to about 2-3 Ser and/or Thr residues in the donor LG glycoprotein and one of the attachment sites was located within the CNBr glycooctapeptide representing the NH2 terminus.
6619126	2	86	gly	glycoprotein	227:238	arg1	variant					271:277	a carbohydrate variant	256:277	a carbohydrate variant in which, for both donors, certain O-glycosidically linked saccharides retained the core structure consisting of NeuAc(alpha 2,3)Gal(beta 1,3)GalNAc that is common to all O-linked saccharides of the MN glycoproteins, and, in addition, contained substituents, of varying chain lengths, on the primary carbinol of GalNAc	256:596	This glycoprotein was found to be a carbohydrate variant in which, for both donors, certain O-glycosidically linked saccharides retained the core structure consisting of NeuAc(alpha 2,3)Gal(beta 1,3)GalNAc that is common to all O-linked saccharides of the MN glycoproteins, and, in addition, contained substituents, of varying chain lengths, on the primary carbinol of GalNAc.
6619126	2	86	gly	glycoprotein	227:238	arg1	glycoprotein					227:238	This glycoprotein	222:238	This glycoprotein	222:238	This glycoprotein was found to be a carbohydrate variant in which, for both donors, certain O-glycosidically linked saccharides retained the core structure consisting of NeuAc(alpha 2,3)Gal(beta 1,3)GalNAc that is common to all O-linked saccharides of the MN glycoproteins, and, in addition, contained substituents, of varying chain lengths, on the primary carbinol of GalNAc.
6619126	14	87	theme	major	2426:2430	arg1	band					2468:2471	band 3	2468:2473	band 3	2468:2473	The variant saccharides bear structural similarities to the core region of O-linked saccharides of certain blood group-active mucins and ovarian cyst secretions, and to the outer sequences of N-linked carbohydrate units (I-, i-active) of the major glycoprotein of human erythrocytes, band 3.
6619126	14	87	theme	major	2426:2430	arg1	glycoprotein					2432:2443	the major glycoprotein	2422:2443	the major glycoprotein of human erythrocytes	2422:2465	The variant saccharides bear structural similarities to the core region of O-linked saccharides of certain blood group-active mucins and ovarian cyst secretions, and to the outer sequences of N-linked carbohydrate units (I-, i-active) of the major glycoprotein of human erythrocytes, band 3.
6619126	2	88	theme	glycoproteins	481:493	arg1	saccharides					459:469	all O-linked saccharides	446:469	all O-linked saccharides of the MN glycoproteins	446:493	This glycoprotein was found to be a carbohydrate variant in which, for both donors, certain O-glycosidically linked saccharides retained the core structure consisting of NeuAc(alpha 2,3)Gal(beta 1,3)GalNAc that is common to all O-linked saccharides of the MN glycoproteins, and, in addition, contained substituents, of varying chain lengths, on the primary carbinol of GalNAc.
6619126	9	89	theme	1,3/4	1481:1485	arg1	beta					1495:1498	beta 1,?	1495:1502	beta	1495:1498	[Gal(beta 1,3/4)Glc-NAc(beta 1,?)]
6619126	9	89	theme	1,3/4	1481:1485	arg1	Glc-NAc					1487:1493	[Gal(beta 1,3/4)Glc-NAc	1471:1493	[Gal(beta 1,3/4)Glc-NAc(beta 1,?)	1471:1503	[Gal(beta 1,3/4)Glc-NAc(beta 1,?)]
6619126	5	90	theme	alternate	1023:1031	arg1	additions					1033:1041	alternate additions	1023:1041	alternate additions of Gal and GlcNAc residues	1023:1068	The 6-O-linked GlcNAc appears to serve as the focus of further chain elongation reactions, involving alternate additions of Gal and GlcNAc residues and leading to the formation of several homologous structures.
6619126	11	91	theme	peptide	1591:1597	arg1	portion					1599:1605	the peptide portion	1587:1605	the peptide portion of these glycoproteins	1587:1628	Because the peptide portion of these glycoproteins contains two methionine residues, it was possible to isolate two CNBr glycopeptides from separate regions of the molecule, and to assess the distribution of these variant structures in the polypeptide.
6619126	14	92	contain	bear	2208:2211	arg1	saccharides					2196:2206	The variant saccharides	2184:2206	The variant saccharides	2184:2206	The variant saccharides bear structural similarities to the core region of O-linked saccharides of certain blood group-active mucins and ovarian cyst secretions, and to the outer sequences of N-linked carbohydrate units (I-, i-active) of the major glycoprotein of human erythrocytes, band 3.
6619126	14	92	contain	bear	2208:2211	arg2	similarities					2224:2235	structural similarities	2213:2235	structural similarities to the core region of O-linked saccharides of certain blood group-active mucins and ovarian cyst secretions, and to the outer sequences of N-linked carbohydrate units (I-, i-active) of the major glycoprotein of human erythrocytes, band 3	2213:2473	The variant saccharides bear structural similarities to the core region of O-linked saccharides of certain blood group-active mucins and ovarian cyst secretions, and to the outer sequences of N-linked carbohydrate units (I-, i-active) of the major glycoprotein of human erythrocytes, band 3.
6619126	4	93	dep	beta	885:888	arg1	[GlcNAc					894:900	[GlcNAc	894:900	beta 1,3)[GlcNAc(beta 1,6)	885:910	Thus, the smallest variant structure was deduced to be NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1,6)]H2GalNAc.
6619126	4	93	dep	beta	885:888	arg1	1,3					890:892	1,3	890:892	1,3	890:892	Thus, the smallest variant structure was deduced to be NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1,6)]H2GalNAc.
6619126	13	94	theme	other	2171:2175	arg1	sites					2177:2181	other sites	2171:2181	other sites	2171:2181	Considerable heterogeneity in saccharide structure was documented for this site, and it is likely that such heterogeneity occurs also at other sites.
6619126	13	95	theme	saccharide	2064:2073	arg1	structure					2075:2083	saccharide structure	2064:2083	saccharide structure	2064:2083	Considerable heterogeneity in saccharide structure was documented for this site, and it is likely that such heterogeneity occurs also at other sites.
6619126	7	96	theme	Gal	1201:1203	arg1	GlcNAc					1216:1221	Gal(beta 1,3/4)GlcNAc	1201:1221	Gal(beta 1,3/4)GlcNAc(beta 1,6)]	1201:1232	Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc and NeuAc(alpha 2,3) Gal(beta 1,3)[Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc were the predominant species present.
6619126	7	96	theme	Gal	1201:1203	arg1	1,6					1228:1230	beta 1,6	1223:1230	beta 1,6	1223:1230	Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc and NeuAc(alpha 2,3) Gal(beta 1,3)[Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc were the predominant species present.
6619126	7	96	theme	Gal	1201:1203	arg1	beta					1267:1270	beta 1,3)[Gal(beta 1,3/4)GlcNAc(beta 1,6)	1267:1307	beta 1,3)[Gal(beta 1,3/4)GlcNAc(beta 1,6)	1267:1307	Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc and NeuAc(alpha 2,3) Gal(beta 1,3)[Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc were the predominant species present.
6619126	14	97	theme	cyst	2329:2332	arg1	secretions					2334:2343	ovarian cyst secretions	2321:2343	ovarian cyst secretions	2321:2343	The variant saccharides bear structural similarities to the core region of O-linked saccharides of certain blood group-active mucins and ovarian cyst secretions, and to the outer sequences of N-linked carbohydrate units (I-, i-active) of the major glycoprotein of human erythrocytes, band 3.
6619126	11	98	theme	molecule	1743:1750	arg1	regions					1728:1734	separate regions	1719:1734	separate regions of the molecule	1719:1750	Because the peptide portion of these glycoproteins contains two methionine residues, it was possible to isolate two CNBr glycopeptides from separate regions of the molecule, and to assess the distribution of these variant structures in the polypeptide.
6619126	11	99	theme	CNBr	1695:1698	arg1	glycopeptides					1700:1712	two CNBr glycopeptides	1691:1712	two CNBr glycopeptides	1691:1712	Because the peptide portion of these glycoproteins contains two methionine residues, it was possible to isolate two CNBr glycopeptides from separate regions of the molecule, and to assess the distribution of these variant structures in the polypeptide.
6619126	8	100	theme	larger	1358:1363	arg1	saccharide					1365:1374	A larger saccharide	1356:1374	A larger saccharide	1356:1374	A larger saccharide was also isolated and its partial sequence was determined to be Gal(beta 1,3/4)GlcNAc(beta 1,?)
6619126	14	101	gly	glycoprotein	2432:2443	arg1	band					2468:2471	band 3	2468:2473	band 3	2468:2473	The variant saccharides bear structural similarities to the core region of O-linked saccharides of certain blood group-active mucins and ovarian cyst secretions, and to the outer sequences of N-linked carbohydrate units (I-, i-active) of the major glycoprotein of human erythrocytes, band 3.
6619126	14	101	gly	glycoprotein	2432:2443	arg1	glycoprotein					2432:2443	the major glycoprotein	2422:2443	the major glycoprotein of human erythrocytes	2422:2465	The variant saccharides bear structural similarities to the core region of O-linked saccharides of certain blood group-active mucins and ovarian cyst secretions, and to the outer sequences of N-linked carbohydrate units (I-, i-active) of the major glycoprotein of human erythrocytes, band 3.
6619126	15	102	theme	H	2567:2567	arg1	carbohydrates					2588:2600	H blood group-active carbohydrates	2567:2600	H blood group-active carbohydrates	2567:2600	The structures of the variant saccharides suggest that they may be potential precursors of H blood group-active carbohydrates, present in varying degrees of maturity, and attached to an integral protein of erythrocytes.
6619126	11	103	theme	glycoproteins	1616:1628	arg1	portion					1599:1605	the peptide portion	1587:1605	the peptide portion of these glycoproteins	1587:1628	Because the peptide portion of these glycoproteins contains two methionine residues, it was possible to isolate two CNBr glycopeptides from separate regions of the molecule, and to assess the distribution of these variant structures in the polypeptide.
6619126	2	104	link	O-linked	450:457	arg1	saccharides					459:469	all O-linked saccharides	446:469	all O-linked saccharides of the MN glycoproteins	446:493	This glycoprotein was found to be a carbohydrate variant in which, for both donors, certain O-glycosidically linked saccharides retained the core structure consisting of NeuAc(alpha 2,3)Gal(beta 1,3)GalNAc that is common to all O-linked saccharides of the MN glycoproteins, and, in addition, contained substituents, of varying chain lengths, on the primary carbinol of GalNAc.
6619126	11	105	contain	contains	1630:1637	arg1	portion					1599:1605	the peptide portion	1587:1605	the peptide portion of these glycoproteins	1587:1628	Because the peptide portion of these glycoproteins contains two methionine residues, it was possible to isolate two CNBr glycopeptides from separate regions of the molecule, and to assess the distribution of these variant structures in the polypeptide.
6619126	11	105	contain	contains	1630:1637	arg2	residues					1654:1661	two methionine residues	1639:1661	two methionine residues	1639:1661	Because the peptide portion of these glycoproteins contains two methionine residues, it was possible to isolate two CNBr glycopeptides from separate regions of the molecule, and to assess the distribution of these variant structures in the polypeptide.
6619126	10	106	theme	beta	1510:1513	arg1	1,3					1564:1566	beta 1,3	1559:1566	beta 1,3	1559:1566	Gal(beta 1,3/4)GlcNAc(beta 1,6)[NeuAc(alpha 2,3)Gal-(beta 1,3)]H2GalNAc.
6619126	10	106	theme	beta	1510:1513	arg1	Gal-					1554:1557	beta 1,3/4)GlcNAc(beta 1,6)[NeuAc(alpha 2,3)Gal-	1510:1557	beta 1,3/4)GlcNAc(beta 1,6)[NeuAc(alpha 2,3)Gal-(beta 1,3)	1510:1567	Gal(beta 1,3/4)GlcNAc(beta 1,6)[NeuAc(alpha 2,3)Gal-(beta 1,3)]H2GalNAc.
6619126	1	107	gly	glycoprotein	90:101	arg1	glycoprotein					90:101	the MM glycoprotein	83:101	the MM glycoprotein	83:101	A variant of the MM glycoprotein (glycophorin A) was isolated from erythrocyte membranes of two individual donors, a mother (L.G.) and daughter (V.W.).
6619126	2	108	gly	glycoproteins	481:493	arg1	glycoproteins					481:493	the MN glycoproteins	474:493	the MN glycoproteins	474:493	This glycoprotein was found to be a carbohydrate variant in which, for both donors, certain O-glycosidically linked saccharides retained the core structure consisting of NeuAc(alpha 2,3)Gal(beta 1,3)GalNAc that is common to all O-linked saccharides of the MN glycoproteins, and, in addition, contained substituents, of varying chain lengths, on the primary carbinol of GalNAc.
6619126	14	109	theme	group-active	2297:2308	arg1	mucins					2310:2315	certain blood group-active mucins	2283:2315	certain blood group-active mucins	2283:2315	The variant saccharides bear structural similarities to the core region of O-linked saccharides of certain blood group-active mucins and ovarian cyst secretions, and to the outer sequences of N-linked carbohydrate units (I-, i-active) of the major glycoprotein of human erythrocytes, band 3.
6619126	12	110	theme	attachment	1941:1950	arg1	sites					1952:1956	the attachment sites	1937:1956	the attachment sites	1937:1956	The saccharides were linked to about 2-3 Ser and/or Thr residues in the donor LG glycoprotein and one of the attachment sites was located within the CNBr glycooctapeptide representing the NH2 terminus.
6619126	14	111	theme	N-linked	2376:2383	arg1	units					2398:2402	N-linked carbohydrate units	2376:2402	N-linked carbohydrate units (I-, i-active) of the major glycoprotein of human erythrocytes, band 3	2376:2473	The variant saccharides bear structural similarities to the core region of O-linked saccharides of certain blood group-active mucins and ovarian cyst secretions, and to the outer sequences of N-linked carbohydrate units (I-, i-active) of the major glycoprotein of human erythrocytes, band 3.
6619126	1	112	theme	donors	177:182	arg1	membranes					149:157	erythrocyte membranes	137:157	erythrocyte membranes of two individual donors, a mother (L.G.) and daughter (V.W.)	137:219	A variant of the MM glycoprotein (glycophorin A) was isolated from erythrocyte membranes of two individual donors, a mother (L.G.) and daughter (V.W.).
6619126	11	113	theme	structures	1801:1810	arg1	distribution					1771:1782	the distribution	1767:1782	the distribution of these variant structures in the polypeptide	1767:1829	Because the peptide portion of these glycoproteins contains two methionine residues, it was possible to isolate two CNBr glycopeptides from separate regions of the molecule, and to assess the distribution of these variant structures in the polypeptide.
6619126	7	114	theme	present	1347:1353	arg1	H2GalNAc					1309:1316	Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc and NeuAc(alpha 2,3) Gal(beta 1,3)[Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc	1201:1316	Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc and NeuAc(alpha 2,3) Gal(beta 1,3)[Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc	1201:1316	Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc and NeuAc(alpha 2,3) Gal(beta 1,3)[Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc were the predominant species present.
6619126	7	114	theme	present	1347:1353	arg1	species					1339:1345	the predominant species	1323:1345	the predominant species present	1323:1353	Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc and NeuAc(alpha 2,3) Gal(beta 1,3)[Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc were the predominant species present.
6619126	2	115	theme	primary	571:577	arg1	carbinol					579:586	the primary carbinol	567:586	the primary carbinol of GalNAc	567:596	This glycoprotein was found to be a carbohydrate variant in which, for both donors, certain O-glycosidically linked saccharides retained the core structure consisting of NeuAc(alpha 2,3)Gal(beta 1,3)GalNAc that is common to all O-linked saccharides of the MN glycoproteins, and, in addition, contained substituents, of varying chain lengths, on the primary carbinol of GalNAc.
6619126	15	116	theme	blood	2569:2573	arg1	carbohydrates					2588:2600	H blood group-active carbohydrates	2567:2600	H blood group-active carbohydrates	2567:2600	The structures of the variant saccharides suggest that they may be potential precursors of H blood group-active carbohydrates, present in varying degrees of maturity, and attached to an integral protein of erythrocytes.
6619126	11	117	from	distribution	1771:1782	arg1	polypeptide					1819:1829	the polypeptide	1815:1829	the polypeptide	1815:1829	Because the peptide portion of these glycoproteins contains two methionine residues, it was possible to isolate two CNBr glycopeptides from separate regions of the molecule, and to assess the distribution of these variant structures in the polypeptide.
6619126	15	118	from	degrees	2622:2628	arg1	present					2603:2609	present	2603:2609	present	2603:2609	The structures of the variant saccharides suggest that they may be potential precursors of H blood group-active carbohydrates, present in varying degrees of maturity, and attached to an integral protein of erythrocytes.
6619126	1	119	theme	MM	87:88	arg1	glycoprotein					90:101	the MM glycoprotein	83:101	the MM glycoprotein	83:101	A variant of the MM glycoprotein (glycophorin A) was isolated from erythrocyte membranes of two individual donors, a mother (L.G.) and daughter (V.W.).
6619126	6	120	theme	NeuAc	1154:1158	arg1	structures					1142:1151	Two such structures	1133:1151	Two such structures	1133:1151	Two such structures, NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1,?)
6619126	6	120	theme	NeuAc	1154:1158	arg1	beta					1191:1194	NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1	1154:1196	NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1	1154:1196	Two such structures, NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1,?)
6619126	14	121	theme	saccharides	2268:2278	arg1	region					2249:2254	the core region	2240:2254	the core region of O-linked saccharides of certain blood group-active mucins and ovarian cyst secretions	2240:2343	The variant saccharides bear structural similarities to the core region of O-linked saccharides of certain blood group-active mucins and ovarian cyst secretions, and to the outer sequences of N-linked carbohydrate units (I-, i-active) of the major glycoprotein of human erythrocytes, band 3.
6619126	10	122	theme	[NeuAc	1537:1542	arg1	1,3					1564:1566	beta 1,3	1559:1566	beta 1,3	1559:1566	Gal(beta 1,3/4)GlcNAc(beta 1,6)[NeuAc(alpha 2,3)Gal-(beta 1,3)]H2GalNAc.
6619126	10	122	theme	[NeuAc	1537:1542	arg1	Gal-					1554:1557	beta 1,3/4)GlcNAc(beta 1,6)[NeuAc(alpha 2,3)Gal-	1510:1557	beta 1,3/4)GlcNAc(beta 1,6)[NeuAc(alpha 2,3)Gal-(beta 1,3)	1510:1567	Gal(beta 1,3/4)GlcNAc(beta 1,6)[NeuAc(alpha 2,3)Gal-(beta 1,3)]H2GalNAc.
6619126	6	123	theme	1,3	1179:1181	arg1	structures					1142:1151	Two such structures	1133:1151	Two such structures	1133:1151	Two such structures, NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1,?)
6619126	6	123	theme	1,3	1179:1181	arg1	beta					1191:1194	NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1	1154:1196	NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1	1154:1196	Two such structures, NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1,?)
6619126	15	124	dep	present	2603:2609	arg1	precursors					2553:2562	potential precursors	2543:2562	potential precursors of H blood group-active carbohydrates	2543:2600	The structures of the variant saccharides suggest that they may be potential precursors of H blood group-active carbohydrates, present in varying degrees of maturity, and attached to an integral protein of erythrocytes.
6619126	2	125	theme	Gal	408:410	arg1	GalNAc					421:426	NeuAc(alpha 2,3)Gal(beta 1,3)GalNAc	392:426	NeuAc(alpha 2,3)Gal(beta 1,3)GalNAc that is common to all O-linked saccharides of the MN glycoproteins	392:493	This glycoprotein was found to be a carbohydrate variant in which, for both donors, certain O-glycosidically linked saccharides retained the core structure consisting of NeuAc(alpha 2,3)Gal(beta 1,3)GalNAc that is common to all O-linked saccharides of the MN glycoproteins, and, in addition, contained substituents, of varying chain lengths, on the primary carbinol of GalNAc.
6619126	14	126	theme	core	2244:2247	arg1	region					2249:2254	the core region	2240:2254	the core region of O-linked saccharides of certain blood group-active mucins and ovarian cyst secretions	2240:2343	The variant saccharides bear structural similarities to the core region of O-linked saccharides of certain blood group-active mucins and ovarian cyst secretions, and to the outer sequences of N-linked carbohydrate units (I-, i-active) of the major glycoprotein of human erythrocytes, band 3.
6619126	10	127	theme	1,6	1533:1535	arg1	1,3					1564:1566	beta 1,3	1559:1566	beta 1,3	1559:1566	Gal(beta 1,3/4)GlcNAc(beta 1,6)[NeuAc(alpha 2,3)Gal-(beta 1,3)]H2GalNAc.
6619126	10	127	theme	1,6	1533:1535	arg1	Gal-					1554:1557	beta 1,3/4)GlcNAc(beta 1,6)[NeuAc(alpha 2,3)Gal-	1510:1557	beta 1,3/4)GlcNAc(beta 1,6)[NeuAc(alpha 2,3)Gal-(beta 1,3)	1510:1567	Gal(beta 1,3/4)GlcNAc(beta 1,6)[NeuAc(alpha 2,3)Gal-(beta 1,3)]H2GalNAc.
6619126	2	128	theme	2,3	404:406	arg1	GalNAc					421:426	NeuAc(alpha 2,3)Gal(beta 1,3)GalNAc	392:426	NeuAc(alpha 2,3)Gal(beta 1,3)GalNAc that is common to all O-linked saccharides of the MN glycoproteins	392:493	This glycoprotein was found to be a carbohydrate variant in which, for both donors, certain O-glycosidically linked saccharides retained the core structure consisting of NeuAc(alpha 2,3)Gal(beta 1,3)GalNAc that is common to all O-linked saccharides of the MN glycoproteins, and, in addition, contained substituents, of varying chain lengths, on the primary carbinol of GalNAc.
6619126	15	129	theme	maturity	2633:2640	arg1	degrees					2622:2628	varying degrees	2614:2628	varying degrees of maturity	2614:2640	The structures of the variant saccharides suggest that they may be potential precursors of H blood group-active carbohydrates, present in varying degrees of maturity, and attached to an integral protein of erythrocytes.
6619126	15	130	theme	group-active	2575:2586	arg1	carbohydrates					2588:2600	H blood group-active carbohydrates	2567:2600	H blood group-active carbohydrates	2567:2600	The structures of the variant saccharides suggest that they may be potential precursors of H blood group-active carbohydrates, present in varying degrees of maturity, and attached to an integral protein of erythrocytes.
6619126	3	131	theme	sodium	691:696	arg1	borohydride					698:708	sodium borohydride	691:708	sodium borohydride	691:708	These saccharides were released from the polypeptide by beta-elimination in the presence of sodium borohydride, and aspects of their structure were investigated by glycosidase digestion and periodate oxidation.
6619126	6	132	theme	alpha	1160:1164	arg1	structures					1142:1151	Two such structures	1133:1151	Two such structures	1133:1151	Two such structures, NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1,?)
6619126	6	132	theme	alpha	1160:1164	arg1	beta					1191:1194	NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1	1154:1196	NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1	1154:1196	Two such structures, NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1,?)
6619126	12	133	gly	glycoprotein	1913:1924	arg1	glycoprotein					1913:1924	the donor LG glycoprotein	1900:1924	the donor LG glycoprotein	1900:1924	The saccharides were linked to about 2-3 Ser and/or Thr residues in the donor LG glycoprotein and one of the attachment sites was located within the CNBr glycooctapeptide representing the NH2 terminus.
6619126	3	134	theme	periodate	789:797	arg1	oxidation					799:807	periodate oxidation	789:807	periodate oxidation	789:807	These saccharides were released from the polypeptide by beta-elimination in the presence of sodium borohydride, and aspects of their structure were investigated by glycosidase digestion and periodate oxidation.
6619126	2	135	theme	beta	412:415	arg1	GalNAc					421:426	NeuAc(alpha 2,3)Gal(beta 1,3)GalNAc	392:426	NeuAc(alpha 2,3)Gal(beta 1,3)GalNAc that is common to all O-linked saccharides of the MN glycoproteins	392:493	This glycoprotein was found to be a carbohydrate variant in which, for both donors, certain O-glycosidically linked saccharides retained the core structure consisting of NeuAc(alpha 2,3)Gal(beta 1,3)GalNAc that is common to all O-linked saccharides of the MN glycoproteins, and, in addition, contained substituents, of varying chain lengths, on the primary carbinol of GalNAc.
6619126	11	136	dep	possible	1671:1678	arg1	assess					1760:1765	assess	1760:1765	to assess the distribution of these variant structures in the polypeptide	1757:1829	Because the peptide portion of these glycoproteins contains two methionine residues, it was possible to isolate two CNBr glycopeptides from separate regions of the molecule, and to assess the distribution of these variant structures in the polypeptide.
6619126	11	136	dep	possible	1671:1678	arg1	isolate					1683:1689	isolate	1683:1689	to isolate two CNBr glycopeptides from separate regions of the molecule	1680:1750	Because the peptide portion of these glycoproteins contains two methionine residues, it was possible to isolate two CNBr glycopeptides from separate regions of the molecule, and to assess the distribution of these variant structures in the polypeptide.
6619126	2	137	theme	lengths	555:561	arg1	substituents					524:535	substituents	524:535	substituents	524:535	This glycoprotein was found to be a carbohydrate variant in which, for both donors, certain O-glycosidically linked saccharides retained the core structure consisting of NeuAc(alpha 2,3)Gal(beta 1,3)GalNAc that is common to all O-linked saccharides of the MN glycoproteins, and, in addition, contained substituents, of varying chain lengths, on the primary carbinol of GalNAc.
6619126	11	138	theme	separate	1719:1726	arg1	regions					1728:1734	separate regions	1719:1734	separate regions of the molecule	1719:1750	Because the peptide portion of these glycoproteins contains two methionine residues, it was possible to isolate two CNBr glycopeptides from separate regions of the molecule, and to assess the distribution of these variant structures in the polypeptide.
6619126	0	139	theme	carbohydrate	2:13	arg1	variant					26:32	A carbohydrate structural variant	0:32	A carbohydrate structural variant of MM glycoprotein (glycophorin A)	0:67	A carbohydrate structural variant of MM glycoprotein (glycophorin A).
6619126	0	139	theme	carbohydrate	2:13	arg1	A					66:66	glycophorin A	54:66	glycophorin A	54:66	A carbohydrate structural variant of MM glycoprotein (glycophorin A).
6619126	5	140	theme	6-O-linked	926:935	arg1	focus					968:972	the focus	964:972	the focus of further chain elongation reactions, involving alternate additions of Gal and GlcNAc residues and leading to the formation of several homologous structures	964:1130	The 6-O-linked GlcNAc appears to serve as the focus of further chain elongation reactions, involving alternate additions of Gal and GlcNAc residues and leading to the formation of several homologous structures.
6619126	5	140	theme	6-O-linked	926:935	arg1	GlcNAc					937:942	The 6-O-linked GlcNAc	922:942	The 6-O-linked GlcNAc	922:942	The 6-O-linked GlcNAc appears to serve as the focus of further chain elongation reactions, involving alternate additions of Gal and GlcNAc residues and leading to the formation of several homologous structures.
6619126	7	141	theme	predominant	1327:1337	arg1	H2GalNAc					1309:1316	Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc and NeuAc(alpha 2,3) Gal(beta 1,3)[Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc	1201:1316	Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc and NeuAc(alpha 2,3) Gal(beta 1,3)[Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc	1201:1316	Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc and NeuAc(alpha 2,3) Gal(beta 1,3)[Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc were the predominant species present.
6619126	7	141	theme	predominant	1327:1337	arg1	species					1339:1345	the predominant species	1323:1345	the predominant species present	1323:1353	Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc and NeuAc(alpha 2,3) Gal(beta 1,3)[Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc were the predominant species present.
6619126	5	142	link	6-O-linked	926:935	arg1	focus					968:972	the focus	964:972	the focus of further chain elongation reactions, involving alternate additions of Gal and GlcNAc residues and leading to the formation of several homologous structures	964:1130	The 6-O-linked GlcNAc appears to serve as the focus of further chain elongation reactions, involving alternate additions of Gal and GlcNAc residues and leading to the formation of several homologous structures.
6619126	5	142	link	6-O-linked	926:935	arg1	GlcNAc					937:942	The 6-O-linked GlcNAc	922:942	The 6-O-linked GlcNAc	922:942	The 6-O-linked GlcNAc appears to serve as the focus of further chain elongation reactions, involving alternate additions of Gal and GlcNAc residues and leading to the formation of several homologous structures.
6619126	12	143	theme	LG	1910:1911	arg1	glycoprotein					1913:1924	the donor LG glycoprotein	1900:1924	the donor LG glycoprotein	1900:1924	The saccharides were linked to about 2-3 Ser and/or Thr residues in the donor LG glycoprotein and one of the attachment sites was located within the CNBr glycooctapeptide representing the NH2 terminus.
6619126	2	144	theme	varying	541:547	arg1	lengths					555:561	varying chain lengths	541:561	varying chain lengths	541:561	This glycoprotein was found to be a carbohydrate variant in which, for both donors, certain O-glycosidically linked saccharides retained the core structure consisting of NeuAc(alpha 2,3)Gal(beta 1,3)GalNAc that is common to all O-linked saccharides of the MN glycoproteins, and, in addition, contained substituents, of varying chain lengths, on the primary carbinol of GalNAc.
6619126	5	145	theme	homologous	1110:1119	arg1	structures					1121:1130	several homologous structures	1102:1130	several homologous structures	1102:1130	The 6-O-linked GlcNAc appears to serve as the focus of further chain elongation reactions, involving alternate additions of Gal and GlcNAc residues and leading to the formation of several homologous structures.
6619126	5	146	theme	chain	985:989	arg1	reactions					1002:1010	further chain elongation reactions	977:1010	further chain elongation reactions	977:1010	The 6-O-linked GlcNAc appears to serve as the focus of further chain elongation reactions, involving alternate additions of Gal and GlcNAc residues and leading to the formation of several homologous structures.
6619126	11	147	gly	glycoproteins	1616:1628	arg1	glycoproteins					1616:1628	these glycoproteins	1610:1628	these glycoproteins	1610:1628	Because the peptide portion of these glycoproteins contains two methionine residues, it was possible to isolate two CNBr glycopeptides from separate regions of the molecule, and to assess the distribution of these variant structures in the polypeptide.
6619126	0	148	theme	MM	37:38	arg1	glycoprotein					40:51	MM glycoprotein	37:51	MM glycoprotein	37:51	A carbohydrate structural variant of MM glycoprotein (glycophorin A).
6619126	5	149	theme	reactions	1002:1010	arg1	focus					968:972	the focus	964:972	the focus of further chain elongation reactions, involving alternate additions of Gal and GlcNAc residues and leading to the formation of several homologous structures	964:1130	The 6-O-linked GlcNAc appears to serve as the focus of further chain elongation reactions, involving alternate additions of Gal and GlcNAc residues and leading to the formation of several homologous structures.
6619126	5	149	theme	reactions	1002:1010	arg1	GlcNAc					937:942	The 6-O-linked GlcNAc	922:942	The 6-O-linked GlcNAc	922:942	The 6-O-linked GlcNAc appears to serve as the focus of further chain elongation reactions, involving alternate additions of Gal and GlcNAc residues and leading to the formation of several homologous structures.
6619126	7	150	theme	alpha	1252:1256	arg1	NeuAc					1246:1250	NeuAc	1246:1250	NeuAc(alpha 2,3)	1246:1261	Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc and NeuAc(alpha 2,3) Gal(beta 1,3)[Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc were the predominant species present.
6619126	7	150	theme	alpha	1252:1256	arg1	2,3					1258:1260	alpha 2,3	1252:1260	alpha 2,3	1252:1260	Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc and NeuAc(alpha 2,3) Gal(beta 1,3)[Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc were the predominant species present.
6619126	11	151	theme	variant	1793:1799	arg1	structures					1801:1810	these variant structures	1787:1810	these variant structures	1787:1810	Because the peptide portion of these glycoproteins contains two methionine residues, it was possible to isolate two CNBr glycopeptides from separate regions of the molecule, and to assess the distribution of these variant structures in the polypeptide.
6619126	14	152	theme	variant	2188:2194	arg1	saccharides					2196:2206	The variant saccharides	2184:2206	The variant saccharides	2184:2206	The variant saccharides bear structural similarities to the core region of O-linked saccharides of certain blood group-active mucins and ovarian cyst secretions, and to the outer sequences of N-linked carbohydrate units (I-, i-active) of the major glycoprotein of human erythrocytes, band 3.
6619126	4	153	theme	NeuAc	865:869	arg1	Gal					881:883	NeuAc(alpha 2,3)Gal	865:883	NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1,6)]H2GalNAc	865:919	Thus, the smallest variant structure was deduced to be NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1,6)]H2GalNAc.
6619126	4	153	theme	NeuAc	865:869	arg1	beta					885:888	beta 1,3)[GlcNAc(beta 1,6)	885:910	beta 1,3)[GlcNAc(beta 1,6)	885:910	Thus, the smallest variant structure was deduced to be NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1,6)]H2GalNAc.
6619126	4	154	theme	variant	829:835	arg1	H2GalNAc					912:919	NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1,6)]H2GalNAc	865:919	NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1,6)]H2GalNAc	865:919	Thus, the smallest variant structure was deduced to be NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1,6)]H2GalNAc.
6619126	4	154	theme	variant	829:835	arg1	structure					837:845	the smallest variant structure	816:845	the smallest variant structure	816:845	Thus, the smallest variant structure was deduced to be NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1,6)]H2GalNAc.
6619126	6	155	theme	[GlcNAc	1183:1189	arg1	structures					1142:1151	Two such structures	1133:1151	Two such structures	1133:1151	Two such structures, NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1,?)
6619126	6	155	theme	[GlcNAc	1183:1189	arg1	beta					1191:1194	NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1	1154:1196	NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1	1154:1196	Two such structures, NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1,?)
6619126	3	156	attach	released	622:629	arg1	polypeptide					640:650	the polypeptide	636:650	the polypeptide	636:650	These saccharides were released from the polypeptide by beta-elimination in the presence of sodium borohydride, and aspects of their structure were investigated by glycosidase digestion and periodate oxidation.
6619126	3	156	attach	released	622:629	arg2	saccharides					605:615	These saccharides	599:615	These saccharides	599:615	These saccharides were released from the polypeptide by beta-elimination in the presence of sodium borohydride, and aspects of their structure were investigated by glycosidase digestion and periodate oxidation.
6619126	7	157	theme	NeuAc	1246:1250	arg1	H2GalNAc					1309:1316	Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc and NeuAc(alpha 2,3) Gal(beta 1,3)[Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc	1201:1316	Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc and NeuAc(alpha 2,3) Gal(beta 1,3)[Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc	1201:1316	Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc and NeuAc(alpha 2,3) Gal(beta 1,3)[Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc were the predominant species present.
6619126	7	157	theme	NeuAc	1246:1250	arg1	species					1339:1345	the predominant species	1323:1345	the predominant species present	1323:1353	Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc and NeuAc(alpha 2,3) Gal(beta 1,3)[Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc were the predominant species present.
6619126	4	158	theme	alpha	871:875	arg1	Gal					881:883	NeuAc(alpha 2,3)Gal	865:883	NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1,6)]H2GalNAc	865:919	Thus, the smallest variant structure was deduced to be NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1,6)]H2GalNAc.
6619126	4	158	theme	alpha	871:875	arg1	beta					885:888	beta 1,3)[GlcNAc(beta 1,6)	885:910	beta 1,3)[GlcNAc(beta 1,6)	885:910	Thus, the smallest variant structure was deduced to be NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1,6)]H2GalNAc.
6619126	2	159	link	linked	331:336	arg1	saccharides					338:348	certain O-glycosidically linked saccharides	306:348	certain O-glycosidically linked saccharides	306:348	This glycoprotein was found to be a carbohydrate variant in which, for both donors, certain O-glycosidically linked saccharides retained the core structure consisting of NeuAc(alpha 2,3)Gal(beta 1,3)GalNAc that is common to all O-linked saccharides of the MN glycoproteins, and, in addition, contained substituents, of varying chain lengths, on the primary carbinol of GalNAc.
6619126	2	160	theme	carbohydrate	258:269	arg1	variant					271:277	a carbohydrate variant	256:277	a carbohydrate variant in which, for both donors, certain O-glycosidically linked saccharides retained the core structure consisting of NeuAc(alpha 2,3)Gal(beta 1,3)GalNAc that is common to all O-linked saccharides of the MN glycoproteins, and, in addition, contained substituents, of varying chain lengths, on the primary carbinol of GalNAc	256:596	This glycoprotein was found to be a carbohydrate variant in which, for both donors, certain O-glycosidically linked saccharides retained the core structure consisting of NeuAc(alpha 2,3)Gal(beta 1,3)GalNAc that is common to all O-linked saccharides of the MN glycoproteins, and, in addition, contained substituents, of varying chain lengths, on the primary carbinol of GalNAc.
6619126	2	160	theme	carbohydrate	258:269	arg1	glycoprotein					227:238	This glycoprotein	222:238	This glycoprotein	222:238	This glycoprotein was found to be a carbohydrate variant in which, for both donors, certain O-glycosidically linked saccharides retained the core structure consisting of NeuAc(alpha 2,3)Gal(beta 1,3)GalNAc that is common to all O-linked saccharides of the MN glycoproteins, and, in addition, contained substituents, of varying chain lengths, on the primary carbinol of GalNAc.
6619126	14	161	dep	units	2398:2402	arg1	i-active					2409:2416	i-active	2409:2416	i-active	2409:2416	The variant saccharides bear structural similarities to the core region of O-linked saccharides of certain blood group-active mucins and ovarian cyst secretions, and to the outer sequences of N-linked carbohydrate units (I-, i-active) of the major glycoprotein of human erythrocytes, band 3.
6619126	14	161	dep	units	2398:2402	arg1	I-					2405:2406	I-	2405:2406	I-	2405:2406	The variant saccharides bear structural similarities to the core region of O-linked saccharides of certain blood group-active mucins and ovarian cyst secretions, and to the outer sequences of N-linked carbohydrate units (I-, i-active) of the major glycoprotein of human erythrocytes, band 3.
6619126	14	162	theme	certain	2283:2289	arg1	mucins					2310:2315	certain blood group-active mucins	2283:2315	certain blood group-active mucins	2283:2315	The variant saccharides bear structural similarities to the core region of O-linked saccharides of certain blood group-active mucins and ovarian cyst secretions, and to the outer sequences of N-linked carbohydrate units (I-, i-active) of the major glycoprotein of human erythrocytes, band 3.
6619126	15	163	theme	variant	2498:2504	arg1	saccharides					2506:2516	the variant saccharides	2494:2516	the variant saccharides	2494:2516	The structures of the variant saccharides suggest that they may be potential precursors of H blood group-active carbohydrates, present in varying degrees of maturity, and attached to an integral protein of erythrocytes.
6619126	14	164	link	O-linked	2259:2266	arg1	saccharides					2268:2278	O-linked saccharides	2259:2278	O-linked saccharides of certain blood group-active mucins	2259:2315	The variant saccharides bear structural similarities to the core region of O-linked saccharides of certain blood group-active mucins and ovarian cyst secretions, and to the outer sequences of N-linked carbohydrate units (I-, i-active) of the major glycoprotein of human erythrocytes, band 3.
6619126	14	165	link	N-linked	2376:2383	arg1	units					2398:2402	N-linked carbohydrate units	2376:2402	N-linked carbohydrate units (I-, i-active) of the major glycoprotein of human erythrocytes, band 3	2376:2473	The variant saccharides bear structural similarities to the core region of O-linked saccharides of certain blood group-active mucins and ovarian cyst secretions, and to the outer sequences of N-linked carbohydrate units (I-, i-active) of the major glycoprotein of human erythrocytes, band 3.
6619126	5	166	theme	Gal	1046:1048	arg1	additions					1033:1041	alternate additions	1023:1041	alternate additions of Gal and GlcNAc residues	1023:1068	The 6-O-linked GlcNAc appears to serve as the focus of further chain elongation reactions, involving alternate additions of Gal and GlcNAc residues and leading to the formation of several homologous structures.
6619126	0	167	gly	glycoprotein	40:51	arg1	glycoprotein					40:51	MM glycoprotein	37:51	MM glycoprotein	37:51	A carbohydrate structural variant of MM glycoprotein (glycophorin A).
6619126	9	168	theme	[Gal	1471:1474	arg1	beta					1495:1498	beta 1,?	1495:1502	beta	1495:1498	[Gal(beta 1,3/4)Glc-NAc(beta 1,?)]
6619126	9	168	theme	[Gal	1471:1474	arg1	Glc-NAc					1487:1493	[Gal(beta 1,3/4)Glc-NAc	1471:1493	[Gal(beta 1,3/4)Glc-NAc(beta 1,?)	1471:1503	[Gal(beta 1,3/4)Glc-NAc(beta 1,?)]
6619126	5	169	theme	GlcNAc	1054:1059	arg1	additions					1033:1041	alternate additions	1023:1041	alternate additions of Gal and GlcNAc residues	1023:1068	The 6-O-linked GlcNAc appears to serve as the focus of further chain elongation reactions, involving alternate additions of Gal and GlcNAc residues and leading to the formation of several homologous structures.
8436110	2	0	dep	Roussel	582:588	arg1	P					590:590	P	590:590	[van Kuik A., de Waard P., Vliegenthart J. F. G., Klein A., Carnoy C., Lamblin G. Roussel P. (1991) Eur	500:602	The structures of 82 neutral and low-molecular-mass sialylated oligosaccharides have been described previously [van Kuik A., de Waard P., Vliegenthart J. F. G., Klein A., Carnoy C., Lamblin G. Roussel P. (1991) Eur.
8436110	7	1	dep	[formula	1126:1133	arg1	see					1136:1138	see	1136:1138	see text	1136:1143	[formula: see text]
8436110	5	2	dep	sialylated	665:674	arg1	medium-size					653:663	medium-size	653:663	medium-size	653:663	In the present work, medium-size sialylated oligosaccharides were obtained after ion-exchange chromatography and were subsequently separated into 36 fractions utilizing gel filtration, HPLC on normal-phase alkylamine-bonded silica and reverse-phase HPLC.
8436110	1	3	theme	pronase	373:379	arg1	digest					381:386	a pronase digest	371:386	a pronase digest	371:386	The carbohydrate chains of the respiratory-mucus glycoproteins of a patient (blood group O) suffering from bronchiectasis due to Kartagener's syndrome, were released by alkaline borohydride treatment of a pronase digest.
8436110	1	4	gly	glycoproteins	217:229	arg1	glycoproteins					217:229	the respiratory-mucus glycoproteins	195:229	the respiratory-mucus glycoproteins	195:229	The carbohydrate chains of the respiratory-mucus glycoproteins of a patient (blood group O) suffering from bronchiectasis due to Kartagener's syndrome, were released by alkaline borohydride treatment of a pronase digest.
8436110	1	5	theme	respiratory-mucus	199:215	arg1	glycoproteins					217:229	the respiratory-mucus glycoproteins	195:229	the respiratory-mucus glycoproteins	195:229	The carbohydrate chains of the respiratory-mucus glycoproteins of a patient (blood group O) suffering from bronchiectasis due to Kartagener's syndrome, were released by alkaline borohydride treatment of a pronase digest.
8436110	0	6	theme	patient	129:135	arg1	glycoproteins					110:122	respiratory-mucus glycoproteins	92:122	respiratory-mucus glycoproteins of a patient suffering from bronchiectasis	92:165	Isolation and structural characterization of novel sialylated oligosaccharide-alditols from respiratory-mucus glycoproteins of a patient suffering from bronchiectasis.
8436110	1	7	theme	digest	381:386	arg1	treatment					358:366	alkaline borohydride treatment	337:366	alkaline borohydride treatment of a pronase digest	337:386	The carbohydrate chains of the respiratory-mucus glycoproteins of a patient (blood group O) suffering from bronchiectasis due to Kartagener's syndrome, were released by alkaline borohydride treatment of a pronase digest.
8436110	2	8	gly	sialylated	441:450	arg1	oligosaccharides					452:467	sialylated oligosaccharides	441:467	sialylated oligosaccharides	441:467	The structures of 82 neutral and low-molecular-mass sialylated oligosaccharides have been described previously [van Kuik A., de Waard P., Vliegenthart J. F. G., Klein A., Carnoy C., Lamblin G. Roussel P. (1991) Eur.
8436110	6	9	theme	1H-NMR	1019:1024	arg1	spectroscopy					1026:1037	500-MHz 1H-NMR spectroscopy	1011:1037	500-MHz 1H-NMR spectroscopy	1011:1037	From these fractions, the following six sialylated hepta- and octa-saccharide-alditols have been characterized by employing 500-MHz 1H-NMR spectroscopy, in conjunction with fast-atom-bombardment mass spectroscopy and methylation analysis.
8436110	6	10	theme	500-MHz	1011:1017	arg1	spectroscopy					1026:1037	500-MHz 1H-NMR spectroscopy	1011:1037	500-MHz 1H-NMR spectroscopy	1011:1037	From these fractions, the following six sialylated hepta- and octa-saccharide-alditols have been characterized by employing 500-MHz 1H-NMR spectroscopy, in conjunction with fast-atom-bombardment mass spectroscopy and methylation analysis.
8436110	5	11	theme	ion-exchange	713:724	arg1	chromatography					726:739	ion-exchange chromatography	713:739	ion-exchange chromatography	713:739	In the present work, medium-size sialylated oligosaccharides were obtained after ion-exchange chromatography and were subsequently separated into 36 fractions utilizing gel filtration, HPLC on normal-phase alkylamine-bonded silica and reverse-phase HPLC.
8436110	5	12	theme	normal-phase	825:836	arg1	silica					856:861	normal-phase alkylamine-bonded silica and reverse-phase HPLC	825:884	silica	856:861	In the present work, medium-size sialylated oligosaccharides were obtained after ion-exchange chromatography and were subsequently separated into 36 fractions utilizing gel filtration, HPLC on normal-phase alkylamine-bonded silica and reverse-phase HPLC.
8436110	0	13	gly	glycoproteins	110:122	arg1	glycoproteins					110:122	respiratory-mucus glycoproteins	92:122	respiratory-mucus glycoproteins of a patient suffering from bronchiectasis	92:165	Isolation and structural characterization of novel sialylated oligosaccharide-alditols from respiratory-mucus glycoproteins of a patient suffering from bronchiectasis.
8436110	1	14	theme	glycoproteins	217:229	arg1	chains					185:190	The carbohydrate chains	168:190	The carbohydrate chains	168:190	The carbohydrate chains of the respiratory-mucus glycoproteins of a patient (blood group O) suffering from bronchiectasis due to Kartagener's syndrome, were released by alkaline borohydride treatment of a pronase digest.
8436110	5	15	theme	reverse-phase	867:879	arg1	HPLC					881:884	normal-phase alkylamine-bonded silica and reverse-phase HPLC	825:884	HPLC	881:884	In the present work, medium-size sialylated oligosaccharides were obtained after ion-exchange chromatography and were subsequently separated into 36 fractions utilizing gel filtration, HPLC on normal-phase alkylamine-bonded silica and reverse-phase HPLC.
8436110	5	16	theme	gel	801:803	arg1	HPLC					817:820	gel filtration, HPLC	801:820	HPLC	817:820	In the present work, medium-size sialylated oligosaccharides were obtained after ion-exchange chromatography and were subsequently separated into 36 fractions utilizing gel filtration, HPLC on normal-phase alkylamine-bonded silica and reverse-phase HPLC.
8436110	2	17	theme	neutral	410:416	arg1	structures					393:402	The structures	389:402	The structures of 82 neutral and low-molecular-mass sialylated oligosaccharides	389:467	The structures of 82 neutral and low-molecular-mass sialylated oligosaccharides have been described previously [van Kuik A., de Waard P., Vliegenthart J. F. G., Klein A., Carnoy C., Lamblin G. Roussel P. (1991) Eur.
8436110	5	18	theme	filtration	805:814	arg1	HPLC					817:820	gel filtration, HPLC	801:820	HPLC	817:820	In the present work, medium-size sialylated oligosaccharides were obtained after ion-exchange chromatography and were subsequently separated into 36 fractions utilizing gel filtration, HPLC on normal-phase alkylamine-bonded silica and reverse-phase HPLC.
8436110	1	19	theme	patient	236:242	arg1	chains					185:190	The carbohydrate chains	168:190	The carbohydrate chains	168:190	The carbohydrate chains of the respiratory-mucus glycoproteins of a patient (blood group O) suffering from bronchiectasis due to Kartagener's syndrome, were released by alkaline borohydride treatment of a pronase digest.
8436110	5	20	theme	alkylamine-bonded	838:854	arg1	silica					856:861	normal-phase alkylamine-bonded silica and reverse-phase HPLC	825:884	silica	856:861	In the present work, medium-size sialylated oligosaccharides were obtained after ion-exchange chromatography and were subsequently separated into 36 fractions utilizing gel filtration, HPLC on normal-phase alkylamine-bonded silica and reverse-phase HPLC.
8436110	6	21	theme	methylation	1104:1114	arg1	analysis					1116:1123	methylation analysis	1104:1123	methylation analysis	1104:1123	From these fractions, the following six sialylated hepta- and octa-saccharide-alditols have been characterized by employing 500-MHz 1H-NMR spectroscopy, in conjunction with fast-atom-bombardment mass spectroscopy and methylation analysis.
8436110	0	22	theme	structural	14:23	arg1	characterization					25:40	structural characterization	14:40	structural characterization	14:40	Isolation and structural characterization of novel sialylated oligosaccharide-alditols from respiratory-mucus glycoproteins of a patient suffering from bronchiectasis.
8436110	5	23	theme	sialylated	665:674	arg1	oligosaccharides					676:691	medium-size sialylated oligosaccharides	653:691	medium-size sialylated oligosaccharides	653:691	In the present work, medium-size sialylated oligosaccharides were obtained after ion-exchange chromatography and were subsequently separated into 36 fractions utilizing gel filtration, HPLC on normal-phase alkylamine-bonded silica and reverse-phase HPLC.
8436110	1	24	theme	blood	245:249	arg1	patient					236:242	a patient	234:242	a patient (blood group O) suffering from bronchiectasis due to Kartagener's syndrome	234:317	The carbohydrate chains of the respiratory-mucus glycoproteins of a patient (blood group O) suffering from bronchiectasis due to Kartagener's syndrome, were released by alkaline borohydride treatment of a pronase digest.
8436110	1	24	theme	blood	245:249	arg1	O					257:257	blood group O	245:257	blood group O	245:257	The carbohydrate chains of the respiratory-mucus glycoproteins of a patient (blood group O) suffering from bronchiectasis due to Kartagener's syndrome, were released by alkaline borohydride treatment of a pronase digest.
8436110	0	25	theme	novel	45:49	arg1	oligosaccharide-alditols					62:85	novel sialylated oligosaccharide-alditols	45:85	novel sialylated oligosaccharide-alditols	45:85	Isolation and structural characterization of novel sialylated oligosaccharide-alditols from respiratory-mucus glycoproteins of a patient suffering from bronchiectasis.
8436110	0	26	from	glycoproteins	110:122	arg1	Isolation					0:8	Isolation	0:8	Isolation	0:8	Isolation and structural characterization of novel sialylated oligosaccharide-alditols from respiratory-mucus glycoproteins of a patient suffering from bronchiectasis.
8436110	0	26	from	glycoproteins	110:122	arg1	characterization					25:40	structural characterization	14:40	structural characterization	14:40	Isolation and structural characterization of novel sialylated oligosaccharide-alditols from respiratory-mucus glycoproteins of a patient suffering from bronchiectasis.
8436110	6	27	with	conjunction	1043:1053	arg1	spectroscopy					1087:1098	fast-atom-bombardment mass spectroscopy	1060:1098	fast-atom-bombardment mass spectroscopy	1060:1098	From these fractions, the following six sialylated hepta- and octa-saccharide-alditols have been characterized by employing 500-MHz 1H-NMR spectroscopy, in conjunction with fast-atom-bombardment mass spectroscopy and methylation analysis.
8436110	6	27	with	conjunction	1043:1053	arg1	analysis					1116:1123	methylation analysis	1104:1123	methylation analysis	1104:1123	From these fractions, the following six sialylated hepta- and octa-saccharide-alditols have been characterized by employing 500-MHz 1H-NMR spectroscopy, in conjunction with fast-atom-bombardment mass spectroscopy and methylation analysis.
8436110	1	28	theme	group	251:255	arg1	patient					236:242	a patient	234:242	a patient (blood group O) suffering from bronchiectasis due to Kartagener's syndrome	234:317	The carbohydrate chains of the respiratory-mucus glycoproteins of a patient (blood group O) suffering from bronchiectasis due to Kartagener's syndrome, were released by alkaline borohydride treatment of a pronase digest.
8436110	1	28	theme	group	251:255	arg1	O					257:257	blood group O	245:257	blood group O	245:257	The carbohydrate chains of the respiratory-mucus glycoproteins of a patient (blood group O) suffering from bronchiectasis due to Kartagener's syndrome, were released by alkaline borohydride treatment of a pronase digest.
8436110	2	29	theme	low-molecular-mass	422:439	arg1	structures					393:402	The structures	389:402	The structures of 82 neutral and low-molecular-mass sialylated oligosaccharides	389:467	The structures of 82 neutral and low-molecular-mass sialylated oligosaccharides have been described previously [van Kuik A., de Waard P., Vliegenthart J. F. G., Klein A., Carnoy C., Lamblin G. Roussel P. (1991) Eur.
8436110	2	30	theme	sialylated	441:450	arg1	oligosaccharides					452:467	sialylated oligosaccharides	441:467	sialylated oligosaccharides	441:467	The structures of 82 neutral and low-molecular-mass sialylated oligosaccharides have been described previously [van Kuik A., de Waard P., Vliegenthart J. F. G., Klein A., Carnoy C., Lamblin G. Roussel P. (1991) Eur.
8436110	0	31	theme	oligosaccharide-alditols	62:85	arg1	Isolation					0:8	Isolation	0:8	Isolation	0:8	Isolation and structural characterization of novel sialylated oligosaccharide-alditols from respiratory-mucus glycoproteins of a patient suffering from bronchiectasis.
8436110	0	31	theme	oligosaccharide-alditols	62:85	arg1	characterization					25:40	structural characterization	14:40	structural characterization	14:40	Isolation and structural characterization of novel sialylated oligosaccharide-alditols from respiratory-mucus glycoproteins of a patient suffering from bronchiectasis.
8436110	1	32	theme	alkaline	337:344	arg1	borohydride					346:356	alkaline borohydride	337:356	alkaline borohydride treatment of a pronase digest	337:386	The carbohydrate chains of the respiratory-mucus glycoproteins of a patient (blood group O) suffering from bronchiectasis due to Kartagener's syndrome, were released by alkaline borohydride treatment of a pronase digest.
8436110	5	33	gly	sialylated	665:674	arg1	oligosaccharides					676:691	medium-size sialylated oligosaccharides	653:691	medium-size sialylated oligosaccharides	653:691	In the present work, medium-size sialylated oligosaccharides were obtained after ion-exchange chromatography and were subsequently separated into 36 fractions utilizing gel filtration, HPLC on normal-phase alkylamine-bonded silica and reverse-phase HPLC.
8436110	0	34	theme	sialylated	51:60	arg1	oligosaccharide-alditols					62:85	novel sialylated oligosaccharide-alditols	45:85	novel sialylated oligosaccharide-alditols	45:85	Isolation and structural characterization of novel sialylated oligosaccharide-alditols from respiratory-mucus glycoproteins of a patient suffering from bronchiectasis.
8436110	1	35	theme	borohydride	346:356	arg1	treatment					358:366	alkaline borohydride treatment	337:366	alkaline borohydride treatment of a pronase digest	337:386	The carbohydrate chains of the respiratory-mucus glycoproteins of a patient (blood group O) suffering from bronchiectasis due to Kartagener's syndrome, were released by alkaline borohydride treatment of a pronase digest.
8436110	5	36	theme	present	639:645	arg1	work					647:650	the present work	635:650	the present work	635:650	In the present work, medium-size sialylated oligosaccharides were obtained after ion-exchange chromatography and were subsequently separated into 36 fractions utilizing gel filtration, HPLC on normal-phase alkylamine-bonded silica and reverse-phase HPLC.
8436110	2	37	dep	neutral	410:416	arg1	oligosaccharides					452:467	sialylated oligosaccharides	441:467	sialylated oligosaccharides	441:467	The structures of 82 neutral and low-molecular-mass sialylated oligosaccharides have been described previously [van Kuik A., de Waard P., Vliegenthart J. F. G., Klein A., Carnoy C., Lamblin G. Roussel P. (1991) Eur.
8436110	2	38	dep	A.	510:511	arg1	Lamblin					571:577	Lamblin	571:577	Lamblin	571:577	The structures of 82 neutral and low-molecular-mass sialylated oligosaccharides have been described previously [van Kuik A., de Waard P., Vliegenthart J. F. G., Klein A., Carnoy C., Lamblin G. Roussel P. (1991) Eur.
8436110	2	38	dep	A.	510:511	arg1	Roussel					582:588	Roussel	582:588	Roussel	582:588	The structures of 82 neutral and low-molecular-mass sialylated oligosaccharides have been described previously [van Kuik A., de Waard P., Vliegenthart J. F. G., Klein A., Carnoy C., Lamblin G. Roussel P. (1991) Eur.
8436110	6	39	theme	fast-atom-bombardment	1060:1080	arg1	spectroscopy					1087:1098	fast-atom-bombardment mass spectroscopy	1060:1098	fast-atom-bombardment mass spectroscopy	1060:1098	From these fractions, the following six sialylated hepta- and octa-saccharide-alditols have been characterized by employing 500-MHz 1H-NMR spectroscopy, in conjunction with fast-atom-bombardment mass spectroscopy and methylation analysis.
8436110	1	40	theme	carbohydrate	172:183	arg1	chains					185:190	The carbohydrate chains	168:190	The carbohydrate chains	168:190	The carbohydrate chains of the respiratory-mucus glycoproteins of a patient (blood group O) suffering from bronchiectasis due to Kartagener's syndrome, were released by alkaline borohydride treatment of a pronase digest.
8436110	0	41	theme	respiratory-mucus	92:108	arg1	glycoproteins					110:122	respiratory-mucus glycoproteins	92:122	respiratory-mucus glycoproteins of a patient suffering from bronchiectasis	92:165	Isolation and structural characterization of novel sialylated oligosaccharide-alditols from respiratory-mucus glycoproteins of a patient suffering from bronchiectasis.
8436110	6	42	theme	mass	1082:1085	arg1	spectroscopy					1087:1098	fast-atom-bombardment mass spectroscopy	1060:1098	fast-atom-bombardment mass spectroscopy	1060:1098	From these fractions, the following six sialylated hepta- and octa-saccharide-alditols have been characterized by employing 500-MHz 1H-NMR spectroscopy, in conjunction with fast-atom-bombardment mass spectroscopy and methylation analysis.
8436110	0	43	gly	sialylated	51:60	arg1	oligosaccharide-alditols					62:85	novel sialylated oligosaccharide-alditols	45:85	novel sialylated oligosaccharide-alditols	45:85	Isolation and structural characterization of novel sialylated oligosaccharide-alditols from respiratory-mucus glycoproteins of a patient suffering from bronchiectasis.
2550193	4	0	theme	N-linked	485:492	arg1	chains					510:515	almost all N-linked oligosaccharide chains	474:515	almost all N-linked oligosaccharide chains of Namalwa EPO	474:530	Oligosaccharide structure analyses suggested that almost all N-linked oligosaccharide chains of Namalwa EPO are shared by urinary EPO.
2550193	5	1	theme	fucose-containing	656:672	arg1	structures					687:696	fucose-containing tetraantennary and fucose-containing triantennary structures	619:696	fucose-containing tetraantennary and fucose-containing triantennary structures	619:696	The two major N-linked oligosaccharides of Namalwa EPO were fucose-containing tetraantennary and fucose-containing triantennary structures.
2550193	5	1	theme	fucose-containing	656:672	arg1	oligosaccharides					582:597	The two major N-linked oligosaccharides	559:597	The two major N-linked oligosaccharides of Namalwa EPO	559:612	The two major N-linked oligosaccharides of Namalwa EPO were fucose-containing tetraantennary and fucose-containing triantennary structures.
2550193	5	2	theme	triantennary	674:685	arg1	structures					687:696	fucose-containing tetraantennary and fucose-containing triantennary structures	619:696	fucose-containing tetraantennary and fucose-containing triantennary structures	619:696	The two major N-linked oligosaccharides of Namalwa EPO were fucose-containing tetraantennary and fucose-containing triantennary structures.
2550193	5	2	theme	triantennary	674:685	arg1	oligosaccharides					582:597	The two major N-linked oligosaccharides	559:597	The two major N-linked oligosaccharides of Namalwa EPO	559:612	The two major N-linked oligosaccharides of Namalwa EPO were fucose-containing tetraantennary and fucose-containing triantennary structures.
2550193	3	3	theme	Namalwa	344:350	arg1	EPO					352:354	The Namalwa EPO	340:354	The Namalwa EPO	340:354	The Namalwa EPO showed an equivalent activity in vivo to that of human urinary EPO.
2550193	5	4	theme	Namalwa	602:608	arg1	EPO					610:612	Namalwa EPO	602:612	Namalwa EPO	602:612	The two major N-linked oligosaccharides of Namalwa EPO were fucose-containing tetraantennary and fucose-containing triantennary structures.
2550193	2	5	link	Namalwa-derived	238:252	arg1	EPO					266:268	The Namalwa-derived recombinant EPO	234:268	The Namalwa-derived recombinant EPO	234:268	The Namalwa-derived recombinant EPO was purified from the culture fluid by a simple three-step procedure.
2550193	5	6	theme	EPO	610:612	arg1	structures					687:696	fucose-containing tetraantennary and fucose-containing triantennary structures	619:696	fucose-containing tetraantennary and fucose-containing triantennary structures	619:696	The two major N-linked oligosaccharides of Namalwa EPO were fucose-containing tetraantennary and fucose-containing triantennary structures.
2550193	5	6	theme	EPO	610:612	arg1	oligosaccharides					582:597	The two major N-linked oligosaccharides	559:597	The two major N-linked oligosaccharides of Namalwa EPO	559:612	The two major N-linked oligosaccharides of Namalwa EPO were fucose-containing tetraantennary and fucose-containing triantennary structures.
2550193	1	7	theme	human	152:156	arg1	EPO					174:176	EPO	174:176	EPO	174:176	To establish a practical exogenous gene expression system in human cells, a cDNA coding for human erythropoietin (EPO) was expressed in human B-lymphoblastoid Namalwa cells.
2550193	1	7	theme	human	152:156	arg1	erythropoietin					158:171	human erythropoietin	152:171	human erythropoietin (EPO)	152:177	To establish a practical exogenous gene expression system in human cells, a cDNA coding for human erythropoietin (EPO) was expressed in human B-lymphoblastoid Namalwa cells.
2550193	4	8	theme	all	481:483	arg1	chains					510:515	almost all N-linked oligosaccharide chains	474:515	almost all N-linked oligosaccharide chains of Namalwa EPO	474:530	Oligosaccharide structure analyses suggested that almost all N-linked oligosaccharide chains of Namalwa EPO are shared by urinary EPO.
2550193	5	9	theme	fucose-containing	619:635	arg1	structures					687:696	fucose-containing tetraantennary and fucose-containing triantennary structures	619:696	fucose-containing tetraantennary and fucose-containing triantennary structures	619:696	The two major N-linked oligosaccharides of Namalwa EPO were fucose-containing tetraantennary and fucose-containing triantennary structures.
2550193	5	9	theme	fucose-containing	619:635	arg1	oligosaccharides					582:597	The two major N-linked oligosaccharides	559:597	The two major N-linked oligosaccharides of Namalwa EPO	559:612	The two major N-linked oligosaccharides of Namalwa EPO were fucose-containing tetraantennary and fucose-containing triantennary structures.
2550193	1	10	theme	practical	75:83	arg1	system					111:116	a practical exogenous gene expression system	73:116	a practical exogenous gene expression system in human cells	73:131	To establish a practical exogenous gene expression system in human cells, a cDNA coding for human erythropoietin (EPO) was expressed in human B-lymphoblastoid Namalwa cells.
2550193	0	11	theme	human	12:16	arg1	erythropoietin					18:31	Recombinant human erythropoietin	0:31	Recombinant human erythropoietin	0:31	Recombinant human erythropoietin produced by Namalwa cells.
2550193	3	12	from	activity	377:384	arg1	vivo					389:392	vivo	389:392	vivo	389:392	The Namalwa EPO showed an equivalent activity in vivo to that of human urinary EPO.
2550193	5	13	theme	tetraantennary	637:650	arg1	structures					687:696	fucose-containing tetraantennary and fucose-containing triantennary structures	619:696	fucose-containing tetraantennary and fucose-containing triantennary structures	619:696	The two major N-linked oligosaccharides of Namalwa EPO were fucose-containing tetraantennary and fucose-containing triantennary structures.
2550193	5	13	theme	tetraantennary	637:650	arg1	oligosaccharides					582:597	The two major N-linked oligosaccharides	559:597	The two major N-linked oligosaccharides of Namalwa EPO	559:612	The two major N-linked oligosaccharides of Namalwa EPO were fucose-containing tetraantennary and fucose-containing triantennary structures.
2550193	1	14	theme	exogenous	85:93	arg1	system					111:116	a practical exogenous gene expression system	73:116	a practical exogenous gene expression system in human cells	73:131	To establish a practical exogenous gene expression system in human cells, a cDNA coding for human erythropoietin (EPO) was expressed in human B-lymphoblastoid Namalwa cells.
2550193	0	15	theme	Recombinant	0:10	arg1	erythropoietin					18:31	Recombinant human erythropoietin	0:31	Recombinant human erythropoietin	0:31	Recombinant human erythropoietin produced by Namalwa cells.
2550193	4	16	theme	urinary	546:552	arg1	EPO					554:556	urinary EPO	546:556	urinary EPO	546:556	Oligosaccharide structure analyses suggested that almost all N-linked oligosaccharide chains of Namalwa EPO are shared by urinary EPO.
2550193	5	17	theme	major	567:571	arg1	structures					687:696	fucose-containing tetraantennary and fucose-containing triantennary structures	619:696	fucose-containing tetraantennary and fucose-containing triantennary structures	619:696	The two major N-linked oligosaccharides of Namalwa EPO were fucose-containing tetraantennary and fucose-containing triantennary structures.
2550193	5	17	theme	major	567:571	arg1	oligosaccharides					582:597	The two major N-linked oligosaccharides	559:597	The two major N-linked oligosaccharides of Namalwa EPO	559:612	The two major N-linked oligosaccharides of Namalwa EPO were fucose-containing tetraantennary and fucose-containing triantennary structures.
2550193	1	18	theme	gene	95:98	arg1	system					111:116	a practical exogenous gene expression system	73:116	a practical exogenous gene expression system in human cells	73:131	To establish a practical exogenous gene expression system in human cells, a cDNA coding for human erythropoietin (EPO) was expressed in human B-lymphoblastoid Namalwa cells.
2550193	3	19	theme	human	405:409	arg1	EPO					419:421	human urinary EPO	405:421	human urinary EPO	405:421	The Namalwa EPO showed an equivalent activity in vivo to that of human urinary EPO.
2550193	4	20	link	N-linked	485:492	arg1	chains					510:515	almost all N-linked oligosaccharide chains	474:515	almost all N-linked oligosaccharide chains of Namalwa EPO	474:530	Oligosaccharide structure analyses suggested that almost all N-linked oligosaccharide chains of Namalwa EPO are shared by urinary EPO.
2550193	2	21	theme	culture	292:298	arg1	fluid					300:304	the culture fluid	288:304	the culture fluid	288:304	The Namalwa-derived recombinant EPO was purified from the culture fluid by a simple three-step procedure.
2550193	4	22	theme	Oligosaccharide	424:438	arg1	analyses					450:457	Oligosaccharide structure analyses	424:457	Oligosaccharide structure analyses	424:457	Oligosaccharide structure analyses suggested that almost all N-linked oligosaccharide chains of Namalwa EPO are shared by urinary EPO.
2550193	0	23	theme	Namalwa	45:51	arg1	cells					53:57	Namalwa cells	45:57	Namalwa cells	45:57	Recombinant human erythropoietin produced by Namalwa cells.
2550193	2	24	theme	three-step	318:327	arg1	procedure					329:337	a simple three-step procedure	309:337	a simple three-step procedure	309:337	The Namalwa-derived recombinant EPO was purified from the culture fluid by a simple three-step procedure.
2550193	1	25	theme	expression	100:109	arg1	system					111:116	a practical exogenous gene expression system	73:116	a practical exogenous gene expression system in human cells	73:131	To establish a practical exogenous gene expression system in human cells, a cDNA coding for human erythropoietin (EPO) was expressed in human B-lymphoblastoid Namalwa cells.
2550193	3	26	theme	urinary	411:417	arg1	EPO					419:421	human urinary EPO	405:421	human urinary EPO	405:421	The Namalwa EPO showed an equivalent activity in vivo to that of human urinary EPO.
2550193	4	27	theme	EPO	528:530	arg1	chains					510:515	almost all N-linked oligosaccharide chains	474:515	almost all N-linked oligosaccharide chains of Namalwa EPO	474:530	Oligosaccharide structure analyses suggested that almost all N-linked oligosaccharide chains of Namalwa EPO are shared by urinary EPO.
2550193	4	28	theme	Namalwa	520:526	arg1	EPO					528:530	Namalwa EPO	520:530	Namalwa EPO	520:530	Oligosaccharide structure analyses suggested that almost all N-linked oligosaccharide chains of Namalwa EPO are shared by urinary EPO.
2550193	4	29	theme	structure	440:448	arg1	analyses					450:457	Oligosaccharide structure analyses	424:457	Oligosaccharide structure analyses	424:457	Oligosaccharide structure analyses suggested that almost all N-linked oligosaccharide chains of Namalwa EPO are shared by urinary EPO.
2550193	1	30	theme	human	121:125	arg1	cells					127:131	human cells	121:131	human cells	121:131	To establish a practical exogenous gene expression system in human cells, a cDNA coding for human erythropoietin (EPO) was expressed in human B-lymphoblastoid Namalwa cells.
2550193	5	31	theme	N-linked	573:580	arg1	structures					687:696	fucose-containing tetraantennary and fucose-containing triantennary structures	619:696	fucose-containing tetraantennary and fucose-containing triantennary structures	619:696	The two major N-linked oligosaccharides of Namalwa EPO were fucose-containing tetraantennary and fucose-containing triantennary structures.
2550193	5	31	theme	N-linked	573:580	arg1	oligosaccharides					582:597	The two major N-linked oligosaccharides	559:597	The two major N-linked oligosaccharides of Namalwa EPO	559:612	The two major N-linked oligosaccharides of Namalwa EPO were fucose-containing tetraantennary and fucose-containing triantennary structures.
2550193	2	32	theme	recombinant	254:264	arg1	EPO					266:268	The Namalwa-derived recombinant EPO	234:268	The Namalwa-derived recombinant EPO	234:268	The Namalwa-derived recombinant EPO was purified from the culture fluid by a simple three-step procedure.
2550193	2	33	theme	simple	311:316	arg1	procedure					329:337	a simple three-step procedure	309:337	a simple three-step procedure	309:337	The Namalwa-derived recombinant EPO was purified from the culture fluid by a simple three-step procedure.
2550193	1	34	from	system	111:116	arg1	cells					127:131	human cells	121:131	human cells	121:131	To establish a practical exogenous gene expression system in human cells, a cDNA coding for human erythropoietin (EPO) was expressed in human B-lymphoblastoid Namalwa cells.
2550193	1	35	theme	human	196:200	arg1	cells					227:231	human B-lymphoblastoid Namalwa cells	196:231	human B-lymphoblastoid Namalwa cells	196:231	To establish a practical exogenous gene expression system in human cells, a cDNA coding for human erythropoietin (EPO) was expressed in human B-lymphoblastoid Namalwa cells.
2550193	2	36	theme	Namalwa-derived	238:252	arg1	EPO					266:268	The Namalwa-derived recombinant EPO	234:268	The Namalwa-derived recombinant EPO	234:268	The Namalwa-derived recombinant EPO was purified from the culture fluid by a simple three-step procedure.
2550193	1	37	theme	B-lymphoblastoid	202:217	arg1	cells					227:231	human B-lymphoblastoid Namalwa cells	196:231	human B-lymphoblastoid Namalwa cells	196:231	To establish a practical exogenous gene expression system in human cells, a cDNA coding for human erythropoietin (EPO) was expressed in human B-lymphoblastoid Namalwa cells.
2550193	1	38	theme	Namalwa	219:225	arg1	cells					227:231	human B-lymphoblastoid Namalwa cells	196:231	human B-lymphoblastoid Namalwa cells	196:231	To establish a practical exogenous gene expression system in human cells, a cDNA coding for human erythropoietin (EPO) was expressed in human B-lymphoblastoid Namalwa cells.
2550193	4	39	theme	oligosaccharide	494:508	arg1	chains					510:515	almost all N-linked oligosaccharide chains	474:515	almost all N-linked oligosaccharide chains of Namalwa EPO	474:530	Oligosaccharide structure analyses suggested that almost all N-linked oligosaccharide chains of Namalwa EPO are shared by urinary EPO.
2550193	3	40	theme	equivalent	366:375	arg1	activity					377:384	an equivalent activity	363:384	an equivalent activity in vivo to that of human urinary EPO	363:421	The Namalwa EPO showed an equivalent activity in vivo to that of human urinary EPO.
2550193	5	41	link	N-linked	573:580	arg1	structures					687:696	fucose-containing tetraantennary and fucose-containing triantennary structures	619:696	fucose-containing tetraantennary and fucose-containing triantennary structures	619:696	The two major N-linked oligosaccharides of Namalwa EPO were fucose-containing tetraantennary and fucose-containing triantennary structures.
2550193	5	41	link	N-linked	573:580	arg1	oligosaccharides					582:597	The two major N-linked oligosaccharides	559:597	The two major N-linked oligosaccharides of Namalwa EPO	559:612	The two major N-linked oligosaccharides of Namalwa EPO were fucose-containing tetraantennary and fucose-containing triantennary structures.
9555945	2	0	theme	proline	514:520	arg1	endopeptidase					531:543	proline specific endopeptidase	514:543	proline specific endopeptidase	514:543	The analysis of the structure of oligosaccharides by fast atom bombardment mass spectrometry (FAB-MS) and linkage analysis was preceded by reduction and carboxymethylation of the intact glycoproteins and digestion with trypsin and proline specific endopeptidase.
9555945	8	1	theme	subsequent	1483:1492	arg1	studies					1505:1511	subsequent structural studies	1483:1511	subsequent structural studies	1483:1511	These findings validate the concept that the recombinant enzyme can serve as an appropriate model for structure/function studies of LCAT and provide the foundation for subsequent structural studies.
9555945	1	2	theme	N-linked	160:167	arg1	structures					182:191	The major N-linked carbohydrate structures	150:191	The major N-linked carbohydrate structures	150:191	The major N-linked carbohydrate structures were determined for recombinant human plasma lecithin:cholesterol acyltransferase (LCAT).
9555945	7	3	theme	enzyme	1254:1259	arg1	forms					1261:1265	these two enzyme forms	1244:1265	these two enzyme forms	1244:1265	The catalytic behavior of these two enzyme forms were found to be very similar if not identical.
9555945	4	4	theme	N-linked	788:795	arg1	glycans					797:803	the N-linked glycans	784:803	the N-linked glycans present on recombinant LCAT (rLCAT)	784:839	The data from the combination of FAB spectrometry and linkage analysis show that the N-linked glycans present on recombinant LCAT (rLCAT) were composed primarily of triantennary and tetraantennary structures with and without core fucosylation.
9555945	5	5	theme	minor	949:953	arg1	population					955:964	A minor population	947:964	A minor population of glycans (less than 5%)	947:990	A minor population of glycans (less than 5%) contained up to three repeats of N-acetyllactosamine in one or more antennae.
9555945	1	6	theme	carbohydrate	169:180	arg1	structures					182:191	The major N-linked carbohydrate structures	150:191	The major N-linked carbohydrate structures	150:191	The major N-linked carbohydrate structures were determined for recombinant human plasma lecithin:cholesterol acyltransferase (LCAT).
9555945	8	7	theme	appropriate	1395:1405	arg1	foundation					1468:1477	the foundation	1464:1477	the foundation for subsequent structural studies	1464:1511	These findings validate the concept that the recombinant enzyme can serve as an appropriate model for structure/function studies of LCAT and provide the foundation for subsequent structural studies.
9555945	8	7	theme	appropriate	1395:1405	arg1	enzyme					1372:1377	the recombinant enzyme	1356:1377	the recombinant enzyme	1356:1377	These findings validate the concept that the recombinant enzyme can serve as an appropriate model for structure/function studies of LCAT and provide the foundation for subsequent structural studies.
9555945	8	7	theme	appropriate	1395:1405	arg1	model					1407:1411	an appropriate model	1392:1411	an appropriate model for structure/function studies of LCAT	1392:1450	These findings validate the concept that the recombinant enzyme can serve as an appropriate model for structure/function studies of LCAT and provide the foundation for subsequent structural studies.
9555945	0	8	theme	N-linked	91:98	arg1	structures					113:122	N-linked carbohydrate structures	91:122	N-linked carbohydrate structures	91:122	Characterization of recombinant human plasma lecithin: cholesterol acyltransferase (LCAT): N-linked carbohydrate structures and catalytic properties.
9555945	1	9	dep	lecithin	238:245	arg1	acyltransferase					259:273	cholesterol acyltransferase	247:273	recombinant human plasma lecithin:cholesterol acyltransferase (LCAT)	213:280	The major N-linked carbohydrate structures were determined for recombinant human plasma lecithin:cholesterol acyltransferase (LCAT).
9555945	1	9	dep	lecithin	238:245	arg1	LCAT					276:279	LCAT	276:279	LCAT	276:279	The major N-linked carbohydrate structures were determined for recombinant human plasma lecithin:cholesterol acyltransferase (LCAT).
9555945	2	10	theme	structure	303:311	arg1	analysis					287:294	The analysis	283:294	The analysis of the structure of oligosaccharides by fast atom bombardment mass spectrometry (FAB-MS) and linkage analysis	283:404	The analysis of the structure of oligosaccharides by fast atom bombardment mass spectrometry (FAB-MS) and linkage analysis was preceded by reduction and carboxymethylation of the intact glycoproteins and digestion with trypsin and proline specific endopeptidase.
9555945	4	11	link	N-linked	788:795	arg1	glycans					797:803	the N-linked glycans	784:803	the N-linked glycans present on recombinant LCAT (rLCAT)	784:839	The data from the combination of FAB spectrometry and linkage analysis show that the N-linked glycans present on recombinant LCAT (rLCAT) were composed primarily of triantennary and tetraantennary structures with and without core fucosylation.
9555945	3	12	theme	PNGase	613:618	arg1	digestion					622:630	PNGase F digestion	613:630	PNGase F digestion	613:630	The N-glycans were subsequently released from the glycopeptides by PNGase F digestion and the oligosaccharides were separated using a C18 Sep-pak cartridge.
9555945	2	13	with	reduction	422:430	arg1	endopeptidase					531:543	proline specific endopeptidase	514:543	proline specific endopeptidase	514:543	The analysis of the structure of oligosaccharides by fast atom bombardment mass spectrometry (FAB-MS) and linkage analysis was preceded by reduction and carboxymethylation of the intact glycoproteins and digestion with trypsin and proline specific endopeptidase.
9555945	2	13	with	reduction	422:430	arg1	trypsin					502:508	trypsin	502:508	trypsin	502:508	The analysis of the structure of oligosaccharides by fast atom bombardment mass spectrometry (FAB-MS) and linkage analysis was preceded by reduction and carboxymethylation of the intact glycoproteins and digestion with trypsin and proline specific endopeptidase.
9555945	4	14	theme	core	928:931	arg1	fucosylation					933:944	core fucosylation	928:944	core fucosylation	928:944	The data from the combination of FAB spectrometry and linkage analysis show that the N-linked glycans present on recombinant LCAT (rLCAT) were composed primarily of triantennary and tetraantennary structures with and without core fucosylation.
9555945	4	15	theme	spectrometry	740:751	arg1	combination					721:731	the combination	717:731	the combination of FAB spectrometry and linkage analysis	717:772	The data from the combination of FAB spectrometry and linkage analysis show that the N-linked glycans present on recombinant LCAT (rLCAT) were composed primarily of triantennary and tetraantennary structures with and without core fucosylation.
9555945	3	16	gly	glycopeptides	596:608	arg2	glycopeptides					596:608	the glycopeptides	592:608	the glycopeptides	592:608	The N-glycans were subsequently released from the glycopeptides by PNGase F digestion and the oligosaccharides were separated using a C18 Sep-pak cartridge.
9555945	7	17	theme	catalytic	1222:1230	arg1	behavior					1232:1239	The catalytic behavior	1218:1239	The catalytic behavior of these two enzyme forms	1218:1265	The catalytic behavior of these two enzyme forms were found to be very similar if not identical.
9555945	7	17	theme	catalytic	1222:1230	arg1	similar					1289:1295	similar	1289:1295	similar	1289:1295	The catalytic behavior of these two enzyme forms were found to be very similar if not identical.
9555945	4	18	theme	tetraantennary	885:898	arg1	structures					900:909	tetraantennary structures	885:909	tetraantennary structures with and without core fucosylation	885:944	The data from the combination of FAB spectrometry and linkage analysis show that the N-linked glycans present on recombinant LCAT (rLCAT) were composed primarily of triantennary and tetraantennary structures with and without core fucosylation.
9555945	5	19	dep	three	1008:1012	arg1	to					1005:1006	to	1005:1006	to	1005:1006	A minor population of glycans (less than 5%) contained up to three repeats of N-acetyllactosamine in one or more antennae.
9555945	7	20	dep	not	1300:1302	arg1	if					1297:1298	if	1297:1298	if	1297:1298	The catalytic behavior of these two enzyme forms were found to be very similar if not identical.
9555945	6	21	theme	LCAT	1074:1077	arg1	activities					1079:1088	The LCAT activities	1070:1088	The LCAT activities of both recombinant and circulating forms of plasma LCAT	1070:1145	The LCAT activities of both recombinant and circulating forms of plasma LCAT were determined using low molecular weight and lipoprotein substrates.
9555945	0	22	theme	carbohydrate	100:111	arg1	structures					113:122	N-linked carbohydrate structures	91:122	N-linked carbohydrate structures	91:122	Characterization of recombinant human plasma lecithin: cholesterol acyltransferase (LCAT): N-linked carbohydrate structures and catalytic properties.
9555945	2	23	with	carboxymethylation	436:453	arg1	endopeptidase					531:543	proline specific endopeptidase	514:543	proline specific endopeptidase	514:543	The analysis of the structure of oligosaccharides by fast atom bombardment mass spectrometry (FAB-MS) and linkage analysis was preceded by reduction and carboxymethylation of the intact glycoproteins and digestion with trypsin and proline specific endopeptidase.
9555945	2	23	with	carboxymethylation	436:453	arg1	trypsin					502:508	trypsin	502:508	trypsin	502:508	The analysis of the structure of oligosaccharides by fast atom bombardment mass spectrometry (FAB-MS) and linkage analysis was preceded by reduction and carboxymethylation of the intact glycoproteins and digestion with trypsin and proline specific endopeptidase.
9555945	4	24	theme	recombinant	816:826	arg1	rLCAT					834:838	rLCAT	834:838	rLCAT	834:838	The data from the combination of FAB spectrometry and linkage analysis show that the N-linked glycans present on recombinant LCAT (rLCAT) were composed primarily of triantennary and tetraantennary structures with and without core fucosylation.
9555945	4	24	theme	recombinant	816:826	arg1	LCAT					828:831	recombinant LCAT	816:831	recombinant LCAT (rLCAT)	816:839	The data from the combination of FAB spectrometry and linkage analysis show that the N-linked glycans present on recombinant LCAT (rLCAT) were composed primarily of triantennary and tetraantennary structures with and without core fucosylation.
9555945	5	25	from	repeats	1014:1020	arg1	antennae					1060:1067	one or more antennae	1048:1067	one or more antennae	1048:1067	A minor population of glycans (less than 5%) contained up to three repeats of N-acetyllactosamine in one or more antennae.
9555945	6	26	theme	recombinant	1098:1108	arg1	forms					1126:1130	both recombinant and circulating forms	1093:1130	both recombinant and circulating forms of plasma LCAT	1093:1145	The LCAT activities of both recombinant and circulating forms of plasma LCAT were determined using low molecular weight and lipoprotein substrates.
9555945	2	27	theme	glycoproteins	469:481	arg1	reduction					422:430	reduction	422:430	reduction	422:430	The analysis of the structure of oligosaccharides by fast atom bombardment mass spectrometry (FAB-MS) and linkage analysis was preceded by reduction and carboxymethylation of the intact glycoproteins and digestion with trypsin and proline specific endopeptidase.
9555945	2	27	theme	glycoproteins	469:481	arg1	carboxymethylation					436:453	carboxymethylation	436:453	carboxymethylation	436:453	The analysis of the structure of oligosaccharides by fast atom bombardment mass spectrometry (FAB-MS) and linkage analysis was preceded by reduction and carboxymethylation of the intact glycoproteins and digestion with trypsin and proline specific endopeptidase.
9555945	2	27	theme	glycoproteins	469:481	arg1	digestion					487:495	digestion	487:495	digestion with trypsin and proline specific endopeptidase	487:543	The analysis of the structure of oligosaccharides by fast atom bombardment mass spectrometry (FAB-MS) and linkage analysis was preceded by reduction and carboxymethylation of the intact glycoproteins and digestion with trypsin and proline specific endopeptidase.
9555945	8	28	theme	LCAT	1447:1450	arg1	studies					1436:1442	structure/function studies	1417:1442	structure/function studies of LCAT	1417:1450	These findings validate the concept that the recombinant enzyme can serve as an appropriate model for structure/function studies of LCAT and provide the foundation for subsequent structural studies.
9555945	2	29	theme	fast	336:339	arg1	FAB-MS					377:382	FAB-MS	377:382	FAB-MS	377:382	The analysis of the structure of oligosaccharides by fast atom bombardment mass spectrometry (FAB-MS) and linkage analysis was preceded by reduction and carboxymethylation of the intact glycoproteins and digestion with trypsin and proline specific endopeptidase.
9555945	2	29	theme	fast	336:339	arg1	spectrometry					363:374	fast atom bombardment mass spectrometry	336:374	fast atom bombardment mass spectrometry (FAB-MS)	336:383	The analysis of the structure of oligosaccharides by fast atom bombardment mass spectrometry (FAB-MS) and linkage analysis was preceded by reduction and carboxymethylation of the intact glycoproteins and digestion with trypsin and proline specific endopeptidase.
9555945	5	30	contain	contained	992:1000	arg2	repeats					1014:1020	up to three repeats	1002:1020	up to three repeats of N-acetyllactosamine in one or more antennae	1002:1067	A minor population of glycans (less than 5%) contained up to three repeats of N-acetyllactosamine in one or more antennae.
9555945	5	30	contain	contained	992:1000	arg1	population					955:964	A minor population	947:964	A minor population of glycans (less than 5%)	947:990	A minor population of glycans (less than 5%) contained up to three repeats of N-acetyllactosamine in one or more antennae.
9555945	2	31	theme	intact	462:467	arg1	glycoproteins					469:481	the intact glycoproteins	458:481	the intact glycoproteins	458:481	The analysis of the structure of oligosaccharides by fast atom bombardment mass spectrometry (FAB-MS) and linkage analysis was preceded by reduction and carboxymethylation of the intact glycoproteins and digestion with trypsin and proline specific endopeptidase.
9555945	4	32	attach	present	805:811	arg2	glycans					797:803	the N-linked glycans	784:803	the N-linked glycans present on recombinant LCAT (rLCAT)	784:839	The data from the combination of FAB spectrometry and linkage analysis show that the N-linked glycans present on recombinant LCAT (rLCAT) were composed primarily of triantennary and tetraantennary structures with and without core fucosylation.
9555945	4	32	attach	present	805:811	arg1	rLCAT					834:838	rLCAT	834:838	rLCAT	834:838	The data from the combination of FAB spectrometry and linkage analysis show that the N-linked glycans present on recombinant LCAT (rLCAT) were composed primarily of triantennary and tetraantennary structures with and without core fucosylation.
9555945	4	32	attach	present	805:811	arg1	LCAT					828:831	recombinant LCAT	816:831	recombinant LCAT (rLCAT)	816:839	The data from the combination of FAB spectrometry and linkage analysis show that the N-linked glycans present on recombinant LCAT (rLCAT) were composed primarily of triantennary and tetraantennary structures with and without core fucosylation.
9555945	4	33	theme	analysis	765:772	arg1	combination					721:731	the combination	717:731	the combination of FAB spectrometry and linkage analysis	717:772	The data from the combination of FAB spectrometry and linkage analysis show that the N-linked glycans present on recombinant LCAT (rLCAT) were composed primarily of triantennary and tetraantennary structures with and without core fucosylation.
9555945	3	34	theme	F	620:620	arg1	digestion					622:630	PNGase F digestion	613:630	PNGase F digestion	613:630	The N-glycans were subsequently released from the glycopeptides by PNGase F digestion and the oligosaccharides were separated using a C18 Sep-pak cartridge.
9555945	2	35	theme	linkage	389:395	arg1	analysis					397:404	linkage analysis	389:404	linkage analysis	389:404	The analysis of the structure of oligosaccharides by fast atom bombardment mass spectrometry (FAB-MS) and linkage analysis was preceded by reduction and carboxymethylation of the intact glycoproteins and digestion with trypsin and proline specific endopeptidase.
9555945	0	36	theme	human	32:36	arg1	lecithin					45:52	recombinant human plasma lecithin	20:52	recombinant human plasma lecithin	20:52	Characterization of recombinant human plasma lecithin: cholesterol acyltransferase (LCAT): N-linked carbohydrate structures and catalytic properties.
9555945	0	37	theme	catalytic	128:136	arg1	properties					138:147	catalytic properties	128:147	catalytic properties	128:147	Characterization of recombinant human plasma lecithin: cholesterol acyltransferase (LCAT): N-linked carbohydrate structures and catalytic properties.
9555945	2	38	theme	oligosaccharides	316:331	arg1	structure					303:311	the structure	299:311	the structure of oligosaccharides	299:331	The analysis of the structure of oligosaccharides by fast atom bombardment mass spectrometry (FAB-MS) and linkage analysis was preceded by reduction and carboxymethylation of the intact glycoproteins and digestion with trypsin and proline specific endopeptidase.
9555945	1	39	theme	recombinant	213:223	arg1	lecithin					238:245	recombinant human plasma lecithin	213:245	recombinant human plasma lecithin:cholesterol acyltransferase (LCAT)	213:280	The major N-linked carbohydrate structures were determined for recombinant human plasma lecithin:cholesterol acyltransferase (LCAT).
9555945	0	40	theme	recombinant	20:30	arg1	lecithin					45:52	recombinant human plasma lecithin	20:52	recombinant human plasma lecithin	20:52	Characterization of recombinant human plasma lecithin: cholesterol acyltransferase (LCAT): N-linked carbohydrate structures and catalytic properties.
9555945	8	41	theme	structural	1494:1503	arg1	studies					1505:1511	subsequent structural studies	1483:1511	subsequent structural studies	1483:1511	These findings validate the concept that the recombinant enzyme can serve as an appropriate model for structure/function studies of LCAT and provide the foundation for subsequent structural studies.
9555945	4	42	theme	present	805:811	arg1	glycans					797:803	the N-linked glycans	784:803	the N-linked glycans present on recombinant LCAT (rLCAT)	784:839	The data from the combination of FAB spectrometry and linkage analysis show that the N-linked glycans present on recombinant LCAT (rLCAT) were composed primarily of triantennary and tetraantennary structures with and without core fucosylation.
9555945	4	43	theme	FAB	736:738	arg1	spectrometry					740:751	FAB spectrometry	736:751	FAB spectrometry	736:751	The data from the combination of FAB spectrometry and linkage analysis show that the N-linked glycans present on recombinant LCAT (rLCAT) were composed primarily of triantennary and tetraantennary structures with and without core fucosylation.
9555945	3	44	attach	released	578:585	arg2	N-glycans					550:558	The N-glycans	546:558	The N-glycans	546:558	The N-glycans were subsequently released from the glycopeptides by PNGase F digestion and the oligosaccharides were separated using a C18 Sep-pak cartridge.
9555945	3	44	attach	released	578:585	arg1	glycopeptides					596:608	the glycopeptides	592:608	the glycopeptides	592:608	The N-glycans were subsequently released from the glycopeptides by PNGase F digestion and the oligosaccharides were separated using a C18 Sep-pak cartridge.
9555945	1	45	theme	human	225:229	arg1	lecithin					238:245	recombinant human plasma lecithin	213:245	recombinant human plasma lecithin:cholesterol acyltransferase (LCAT)	213:280	The major N-linked carbohydrate structures were determined for recombinant human plasma lecithin:cholesterol acyltransferase (LCAT).
9555945	0	46	theme	lecithin	45:52	arg1	Characterization					0:15	Characterization	0:15	Characterization of recombinant human plasma lecithin: cholesterol acyltransferase (LCAT): N-linked carbohydrate structures and catalytic properties.	0:148	Characterization of recombinant human plasma lecithin: cholesterol acyltransferase (LCAT): N-linked carbohydrate structures and catalytic properties.
9555945	5	47	theme	glycans	969:975	arg1	population					955:964	A minor population	947:964	A minor population of glycans (less than 5%)	947:990	A minor population of glycans (less than 5%) contained up to three repeats of N-acetyllactosamine in one or more antennae.
9555945	8	48	theme	structure/function	1417:1434	arg1	studies					1436:1442	structure/function studies	1417:1442	structure/function studies of LCAT	1417:1450	These findings validate the concept that the recombinant enzyme can serve as an appropriate model for structure/function studies of LCAT and provide the foundation for subsequent structural studies.
9555945	6	49	theme	circulating	1114:1124	arg1	forms					1126:1130	both recombinant and circulating forms	1093:1130	both recombinant and circulating forms of plasma LCAT	1093:1145	The LCAT activities of both recombinant and circulating forms of plasma LCAT were determined using low molecular weight and lipoprotein substrates.
9555945	1	50	theme	plasma	231:236	arg1	lecithin					238:245	recombinant human plasma lecithin	213:245	recombinant human plasma lecithin:cholesterol acyltransferase (LCAT)	213:280	The major N-linked carbohydrate structures were determined for recombinant human plasma lecithin:cholesterol acyltransferase (LCAT).
9555945	0	51	theme	plasma	38:43	arg1	lecithin					45:52	recombinant human plasma lecithin	20:52	recombinant human plasma lecithin	20:52	Characterization of recombinant human plasma lecithin: cholesterol acyltransferase (LCAT): N-linked carbohydrate structures and catalytic properties.
9555945	3	52	theme	C18	680:682	arg1	cartridge					692:700	a C18 Sep-pak cartridge	678:700	a C18 Sep-pak cartridge	678:700	The N-glycans were subsequently released from the glycopeptides by PNGase F digestion and the oligosaccharides were separated using a C18 Sep-pak cartridge.
9555945	0	53	theme	cholesterol	55:65	arg1	LCAT					84:87	LCAT	84:87	LCAT	84:87	Characterization of recombinant human plasma lecithin: cholesterol acyltransferase (LCAT): N-linked carbohydrate structures and catalytic properties.
9555945	0	53	theme	cholesterol	55:65	arg1	acyltransferase					67:81	cholesterol acyltransferase	55:81	Characterization of recombinant human plasma lecithin: cholesterol acyltransferase (LCAT): N-linked carbohydrate structures and catalytic properties.	0:148	Characterization of recombinant human plasma lecithin: cholesterol acyltransferase (LCAT): N-linked carbohydrate structures and catalytic properties.
9555945	3	54	theme	Sep-pak	684:690	arg1	cartridge					692:700	a C18 Sep-pak cartridge	678:700	a C18 Sep-pak cartridge	678:700	The N-glycans were subsequently released from the glycopeptides by PNGase F digestion and the oligosaccharides were separated using a C18 Sep-pak cartridge.
9555945	4	55	theme	linkage	757:763	arg1	analysis					765:772	linkage analysis	757:772	linkage analysis	757:772	The data from the combination of FAB spectrometry and linkage analysis show that the N-linked glycans present on recombinant LCAT (rLCAT) were composed primarily of triantennary and tetraantennary structures with and without core fucosylation.
9555945	6	56	theme	forms	1126:1130	arg1	activities					1079:1088	The LCAT activities	1070:1088	The LCAT activities of both recombinant and circulating forms of plasma LCAT	1070:1145	The LCAT activities of both recombinant and circulating forms of plasma LCAT were determined using low molecular weight and lipoprotein substrates.
9555945	1	57	link	N-linked	160:167	arg1	structures					182:191	The major N-linked carbohydrate structures	150:191	The major N-linked carbohydrate structures	150:191	The major N-linked carbohydrate structures were determined for recombinant human plasma lecithin:cholesterol acyltransferase (LCAT).
9555945	6	58	theme	molecular	1173:1181	arg1	weight					1183:1188	low molecular weight	1169:1188	low molecular weight	1169:1188	The LCAT activities of both recombinant and circulating forms of plasma LCAT were determined using low molecular weight and lipoprotein substrates.
9555945	2	59	theme	mass	358:361	arg1	FAB-MS					377:382	FAB-MS	377:382	FAB-MS	377:382	The analysis of the structure of oligosaccharides by fast atom bombardment mass spectrometry (FAB-MS) and linkage analysis was preceded by reduction and carboxymethylation of the intact glycoproteins and digestion with trypsin and proline specific endopeptidase.
9555945	2	59	theme	mass	358:361	arg1	spectrometry					363:374	fast atom bombardment mass spectrometry	336:374	fast atom bombardment mass spectrometry (FAB-MS)	336:383	The analysis of the structure of oligosaccharides by fast atom bombardment mass spectrometry (FAB-MS) and linkage analysis was preceded by reduction and carboxymethylation of the intact glycoproteins and digestion with trypsin and proline specific endopeptidase.
9555945	2	60	theme	bombardment	346:356	arg1	FAB-MS					377:382	FAB-MS	377:382	FAB-MS	377:382	The analysis of the structure of oligosaccharides by fast atom bombardment mass spectrometry (FAB-MS) and linkage analysis was preceded by reduction and carboxymethylation of the intact glycoproteins and digestion with trypsin and proline specific endopeptidase.
9555945	2	60	theme	bombardment	346:356	arg1	spectrometry					363:374	fast atom bombardment mass spectrometry	336:374	fast atom bombardment mass spectrometry (FAB-MS)	336:383	The analysis of the structure of oligosaccharides by fast atom bombardment mass spectrometry (FAB-MS) and linkage analysis was preceded by reduction and carboxymethylation of the intact glycoproteins and digestion with trypsin and proline specific endopeptidase.
9555945	6	61	theme	LCAT	1142:1145	arg1	forms					1126:1130	both recombinant and circulating forms	1093:1130	both recombinant and circulating forms of plasma LCAT	1093:1145	The LCAT activities of both recombinant and circulating forms of plasma LCAT were determined using low molecular weight and lipoprotein substrates.
9555945	6	62	theme	lipoprotein	1194:1204	arg1	substrates					1206:1215	lipoprotein substrates	1194:1215	lipoprotein substrates	1194:1215	The LCAT activities of both recombinant and circulating forms of plasma LCAT were determined using low molecular weight and lipoprotein substrates.
9555945	2	63	gly	glycoproteins	469:481	arg1	glycoproteins					469:481	the intact glycoproteins	458:481	the intact glycoproteins	458:481	The analysis of the structure of oligosaccharides by fast atom bombardment mass spectrometry (FAB-MS) and linkage analysis was preceded by reduction and carboxymethylation of the intact glycoproteins and digestion with trypsin and proline specific endopeptidase.
9555945	2	64	with	digestion	487:495	arg1	endopeptidase					531:543	proline specific endopeptidase	514:543	proline specific endopeptidase	514:543	The analysis of the structure of oligosaccharides by fast atom bombardment mass spectrometry (FAB-MS) and linkage analysis was preceded by reduction and carboxymethylation of the intact glycoproteins and digestion with trypsin and proline specific endopeptidase.
9555945	2	64	with	digestion	487:495	arg1	trypsin					502:508	trypsin	502:508	trypsin	502:508	The analysis of the structure of oligosaccharides by fast atom bombardment mass spectrometry (FAB-MS) and linkage analysis was preceded by reduction and carboxymethylation of the intact glycoproteins and digestion with trypsin and proline specific endopeptidase.
9555945	2	65	theme	atom	341:344	arg1	FAB-MS					377:382	FAB-MS	377:382	FAB-MS	377:382	The analysis of the structure of oligosaccharides by fast atom bombardment mass spectrometry (FAB-MS) and linkage analysis was preceded by reduction and carboxymethylation of the intact glycoproteins and digestion with trypsin and proline specific endopeptidase.
9555945	2	65	theme	atom	341:344	arg1	spectrometry					363:374	fast atom bombardment mass spectrometry	336:374	fast atom bombardment mass spectrometry (FAB-MS)	336:383	The analysis of the structure of oligosaccharides by fast atom bombardment mass spectrometry (FAB-MS) and linkage analysis was preceded by reduction and carboxymethylation of the intact glycoproteins and digestion with trypsin and proline specific endopeptidase.
9555945	8	66	theme	recombinant	1360:1370	arg1	foundation					1468:1477	the foundation	1464:1477	the foundation for subsequent structural studies	1464:1511	These findings validate the concept that the recombinant enzyme can serve as an appropriate model for structure/function studies of LCAT and provide the foundation for subsequent structural studies.
9555945	8	66	theme	recombinant	1360:1370	arg1	enzyme					1372:1377	the recombinant enzyme	1356:1377	the recombinant enzyme	1356:1377	These findings validate the concept that the recombinant enzyme can serve as an appropriate model for structure/function studies of LCAT and provide the foundation for subsequent structural studies.
9555945	8	66	theme	recombinant	1360:1370	arg1	model					1407:1411	an appropriate model	1392:1411	an appropriate model for structure/function studies of LCAT	1392:1450	These findings validate the concept that the recombinant enzyme can serve as an appropriate model for structure/function studies of LCAT and provide the foundation for subsequent structural studies.
9555945	1	67	theme	cholesterol	247:257	arg1	acyltransferase					259:273	cholesterol acyltransferase	247:273	recombinant human plasma lecithin:cholesterol acyltransferase (LCAT)	213:280	The major N-linked carbohydrate structures were determined for recombinant human plasma lecithin:cholesterol acyltransferase (LCAT).
9555945	1	67	theme	cholesterol	247:257	arg1	LCAT					276:279	LCAT	276:279	LCAT	276:279	The major N-linked carbohydrate structures were determined for recombinant human plasma lecithin:cholesterol acyltransferase (LCAT).
9555945	7	68	theme	forms	1261:1265	arg1	behavior					1232:1239	The catalytic behavior	1218:1239	The catalytic behavior of these two enzyme forms	1218:1265	The catalytic behavior of these two enzyme forms were found to be very similar if not identical.
9555945	7	68	theme	forms	1261:1265	arg1	similar					1289:1295	similar	1289:1295	similar	1289:1295	The catalytic behavior of these two enzyme forms were found to be very similar if not identical.
9555945	4	69	from	combination	721:731	arg1	data					707:710	The data	703:710	The data from the combination of FAB spectrometry and linkage analysis	703:772	The data from the combination of FAB spectrometry and linkage analysis show that the N-linked glycans present on recombinant LCAT (rLCAT) were composed primarily of triantennary and tetraantennary structures with and without core fucosylation.
9555945	5	70	theme	N-acetyllactosamine	1025:1043	arg1	repeats					1014:1020	up to three repeats	1002:1020	up to three repeats of N-acetyllactosamine in one or more antennae	1002:1067	A minor population of glycans (less than 5%) contained up to three repeats of N-acetyllactosamine in one or more antennae.
9555945	6	71	theme	plasma	1135:1140	arg1	LCAT					1142:1145	plasma LCAT	1135:1145	plasma LCAT	1135:1145	The LCAT activities of both recombinant and circulating forms of plasma LCAT were determined using low molecular weight and lipoprotein substrates.
9555945	2	72	theme	specific	522:529	arg1	endopeptidase					531:543	proline specific endopeptidase	514:543	proline specific endopeptidase	514:543	The analysis of the structure of oligosaccharides by fast atom bombardment mass spectrometry (FAB-MS) and linkage analysis was preceded by reduction and carboxymethylation of the intact glycoproteins and digestion with trypsin and proline specific endopeptidase.
9555945	6	73	theme	low	1169:1171	arg1	weight					1183:1188	low molecular weight	1169:1188	low molecular weight	1169:1188	The LCAT activities of both recombinant and circulating forms of plasma LCAT were determined using low molecular weight and lipoprotein substrates.
9555945	0	74	dep	Characterization	0:15	arg1	properties					138:147	catalytic properties	128:147	catalytic properties	128:147	Characterization of recombinant human plasma lecithin: cholesterol acyltransferase (LCAT): N-linked carbohydrate structures and catalytic properties.
9555945	0	74	dep	Characterization	0:15	arg1	LCAT					84:87	LCAT	84:87	LCAT	84:87	Characterization of recombinant human plasma lecithin: cholesterol acyltransferase (LCAT): N-linked carbohydrate structures and catalytic properties.
9555945	0	74	dep	Characterization	0:15	arg1	acyltransferase					67:81	cholesterol acyltransferase	55:81	Characterization of recombinant human plasma lecithin: cholesterol acyltransferase (LCAT): N-linked carbohydrate structures and catalytic properties.	0:148	Characterization of recombinant human plasma lecithin: cholesterol acyltransferase (LCAT): N-linked carbohydrate structures and catalytic properties.
9555945	0	74	dep	Characterization	0:15	arg1	structures					113:122	N-linked carbohydrate structures	91:122	N-linked carbohydrate structures	91:122	Characterization of recombinant human plasma lecithin: cholesterol acyltransferase (LCAT): N-linked carbohydrate structures and catalytic properties.
9555945	0	75	link	N-linked	91:98	arg1	structures					113:122	N-linked carbohydrate structures	91:122	N-linked carbohydrate structures	91:122	Characterization of recombinant human plasma lecithin: cholesterol acyltransferase (LCAT): N-linked carbohydrate structures and catalytic properties.
9555945	1	76	theme	major	154:158	arg1	structures					182:191	The major N-linked carbohydrate structures	150:191	The major N-linked carbohydrate structures	150:191	The major N-linked carbohydrate structures were determined for recombinant human plasma lecithin:cholesterol acyltransferase (LCAT).
3709529	0	0	theme	ovarian-cyst	78:89	arg1	glycoproteins					91:103	human ovarian-cyst glycoproteins	72:103	human ovarian-cyst glycoproteins	72:103	Typing of core and backbone domains of mucin-type oligosaccharides from human ovarian-cyst glycoproteins by 500-MHz 1H-NMR spectroscopy.
3709529	0	1	from	core	10:13	arg1	glycoproteins					91:103	human ovarian-cyst glycoproteins	72:103	human ovarian-cyst glycoproteins	72:103	Typing of core and backbone domains of mucin-type oligosaccharides from human ovarian-cyst glycoproteins by 500-MHz 1H-NMR spectroscopy.
3709529	1	2	from	fluid	196:200	arg1	glycoproteins					164:176	Human blood-group A active glycoproteins	137:176	Human blood-group A active glycoproteins from ovarian-cyst fluid	137:200	Human blood-group A active glycoproteins from ovarian-cyst fluid were subjected to Smith degradation and subsequent beta-elimination.
3709529	0	3	theme	human	72:76	arg1	glycoproteins					91:103	human ovarian-cyst glycoproteins	72:103	human ovarian-cyst glycoproteins	72:103	Typing of core and backbone domains of mucin-type oligosaccharides from human ovarian-cyst glycoproteins by 500-MHz 1H-NMR spectroscopy.
3709529	5	4	theme	linkage	704:710	arg1	types					712:716	the linkage types	700:716	the linkage types of alternating Gal-GlcNAc sequences	700:752	In particular, the core types, i.e. the substitution patterns of N-acetylgalactosaminitol (GalNAc-ol) as well as the types of backbone, i.e. the linkage types of alternating Gal-GlcNAc sequences, were unambiguously identified.
3709529	6	5	theme	first	847:851	arg1	time					853:856	the first time	843:856	the first time	843:856	The core type GlcNAc beta(1-3)GalNAc-ol is described for the first time as occurring in ovarian-cyst glycoprotein.
3709529	2	6	theme	carbohydrate	366:377	arg1	chains					379:384	the O-linked carbohydrate chains	353:384	the O-linked carbohydrate chains	353:384	The resulting oligosaccharide-alditols represent the core and backbone domains of the O-linked carbohydrate chains.
3709529	2	7	theme	backbone	333:340	arg1	chains					379:384	the O-linked carbohydrate chains	353:384	the O-linked carbohydrate chains	353:384	The resulting oligosaccharide-alditols represent the core and backbone domains of the O-linked carbohydrate chains.
3709529	2	7	theme	backbone	333:340	arg1	domains					342:348	the core and backbone domains	320:348	domains	342:348	The resulting oligosaccharide-alditols represent the core and backbone domains of the O-linked carbohydrate chains.
3709529	5	8	dep	patterns	612:619	arg1	i.e.					590:593	i.e.	590:593	i.e.	590:593	In particular, the core types, i.e. the substitution patterns of N-acetylgalactosaminitol (GalNAc-ol) as well as the types of backbone, i.e. the linkage types of alternating Gal-GlcNAc sequences, were unambiguously identified.
3709529	2	9	theme	chains	379:384	arg1	chains					379:384	the O-linked carbohydrate chains	353:384	the O-linked carbohydrate chains	353:384	The resulting oligosaccharide-alditols represent the core and backbone domains of the O-linked carbohydrate chains.
3709529	2	9	theme	chains	379:384	arg1	domains					342:348	the core and backbone domains	320:348	domains	342:348	The resulting oligosaccharide-alditols represent the core and backbone domains of the O-linked carbohydrate chains.
3709529	0	10	theme	1H-NMR	116:121	arg1	spectroscopy					123:134	500-MHz 1H-NMR spectroscopy	108:134	500-MHz 1H-NMR spectroscopy	108:134	Typing of core and backbone domains of mucin-type oligosaccharides from human ovarian-cyst glycoproteins by 500-MHz 1H-NMR spectroscopy.
3709529	5	11	theme	types	676:680	arg1	patterns					612:619	the substitution patterns	595:619	the substitution patterns of N-acetylgalactosaminitol (GalNAc-ol) as well as the types of backbone, i.e. the linkage types of alternating Gal-GlcNAc sequences	595:752	In particular, the core types, i.e. the substitution patterns of N-acetylgalactosaminitol (GalNAc-ol) as well as the types of backbone, i.e. the linkage types of alternating Gal-GlcNAc sequences, were unambiguously identified.
3709529	1	12	theme	ovarian-cyst	183:194	arg1	fluid					196:200	ovarian-cyst fluid	183:200	ovarian-cyst fluid	183:200	Human blood-group A active glycoproteins from ovarian-cyst fluid were subjected to Smith degradation and subsequent beta-elimination.
3709529	0	13	theme	500-MHz	108:114	arg1	spectroscopy					123:134	500-MHz 1H-NMR spectroscopy	108:134	500-MHz 1H-NMR spectroscopy	108:134	Typing of core and backbone domains of mucin-type oligosaccharides from human ovarian-cyst glycoproteins by 500-MHz 1H-NMR spectroscopy.
3709529	0	14	from	domains	28:34	arg1	glycoproteins					91:103	human ovarian-cyst glycoproteins	72:103	human ovarian-cyst glycoproteins	72:103	Typing of core and backbone domains of mucin-type oligosaccharides from human ovarian-cyst glycoproteins by 500-MHz 1H-NMR spectroscopy.
3709529	5	15	theme	N-acetylgalactosaminitol	624:647	arg1	patterns					612:619	the substitution patterns	595:619	the substitution patterns of N-acetylgalactosaminitol (GalNAc-ol) as well as the types of backbone, i.e. the linkage types of alternating Gal-GlcNAc sequences	595:752	In particular, the core types, i.e. the substitution patterns of N-acetylgalactosaminitol (GalNAc-ol) as well as the types of backbone, i.e. the linkage types of alternating Gal-GlcNAc sequences, were unambiguously identified.
3709529	2	16	theme	core	324:327	arg1	chains					379:384	the O-linked carbohydrate chains	353:384	the O-linked carbohydrate chains	353:384	The resulting oligosaccharide-alditols represent the core and backbone domains of the O-linked carbohydrate chains.
3709529	2	16	theme	core	324:327	arg1	domains					342:348	the core and backbone domains	320:348	domains	342:348	The resulting oligosaccharide-alditols represent the core and backbone domains of the O-linked carbohydrate chains.
3709529	3	17	theme	these	395:399	arg1	Nine					387:390	Nine	387:390	Nine	387:390	Nine of these, ranging in size from disaccharides to hexasaccharides, were investigated by 1H-NMR spectroscopy.
3709529	3	17	theme	these	395:399	arg1	these					395:399	these	395:399	these	395:399	Nine of these, ranging in size from disaccharides to hexasaccharides, were investigated by 1H-NMR spectroscopy.
3709529	5	18	theme	backbone	685:692	arg1	GalNAc-ol					650:658	GalNAc-ol	650:658	GalNAc-ol	650:658	In particular, the core types, i.e. the substitution patterns of N-acetylgalactosaminitol (GalNAc-ol) as well as the types of backbone, i.e. the linkage types of alternating Gal-GlcNAc sequences, were unambiguously identified.
3709529	5	18	theme	backbone	685:692	arg1	N-acetylgalactosaminitol					624:647	N-acetylgalactosaminitol	624:647	N-acetylgalactosaminitol (GalNAc-ol) as well as the types of backbone, i.e. the linkage types of alternating Gal-GlcNAc sequences	624:752	In particular, the core types, i.e. the substitution patterns of N-acetylgalactosaminitol (GalNAc-ol) as well as the types of backbone, i.e. the linkage types of alternating Gal-GlcNAc sequences, were unambiguously identified.
3709529	5	18	theme	backbone	685:692	arg1	types					676:680	the types	672:680	the types	672:680	In particular, the core types, i.e. the substitution patterns of N-acetylgalactosaminitol (GalNAc-ol) as well as the types of backbone, i.e. the linkage types of alternating Gal-GlcNAc sequences, were unambiguously identified.
3709529	0	19	gly	glycoproteins	91:103	arg1	glycoproteins					91:103	human ovarian-cyst glycoproteins	72:103	human ovarian-cyst glycoproteins	72:103	Typing of core and backbone domains of mucin-type oligosaccharides from human ovarian-cyst glycoproteins by 500-MHz 1H-NMR spectroscopy.
3709529	5	20	dep	types	712:716	arg1	i.e.					695:698	i.e.	695:698	i.e.	695:698	In particular, the core types, i.e. the substitution patterns of N-acetylgalactosaminitol (GalNAc-ol) as well as the types of backbone, i.e. the linkage types of alternating Gal-GlcNAc sequences, were unambiguously identified.
3709529	5	21	theme	sequences	744:752	arg1	types					712:716	the linkage types	700:716	the linkage types of alternating Gal-GlcNAc sequences	700:752	In particular, the core types, i.e. the substitution patterns of N-acetylgalactosaminitol (GalNAc-ol) as well as the types of backbone, i.e. the linkage types of alternating Gal-GlcNAc sequences, were unambiguously identified.
3709529	2	22	theme	O-linked	357:364	arg1	chains					379:384	the O-linked carbohydrate chains	353:384	the O-linked carbohydrate chains	353:384	The resulting oligosaccharide-alditols represent the core and backbone domains of the O-linked carbohydrate chains.
3709529	3	23	theme	1H-NMR	478:483	arg1	spectroscopy					485:496	1H-NMR spectroscopy	478:496	1H-NMR spectroscopy	478:496	Nine of these, ranging in size from disaccharides to hexasaccharides, were investigated by 1H-NMR spectroscopy.
3709529	6	24	theme	type	795:798	arg1	beta					807:810	core type GlcNAc beta	790:810	The core type GlcNAc beta(1-3)GalNAc-ol	786:824	The core type GlcNAc beta(1-3)GalNAc-ol is described for the first time as occurring in ovarian-cyst glycoprotein.
3709529	6	24	theme	type	795:798	arg1	1-3					812:814	1-3	812:814	1-3	812:814	The core type GlcNAc beta(1-3)GalNAc-ol is described for the first time as occurring in ovarian-cyst glycoprotein.
3709529	0	25	theme	core	10:13	arg1	Typing					0:5	Typing	0:5	Typing of core and backbone domains of mucin-type oligosaccharides from human ovarian-cyst glycoproteins by 500-MHz 1H-NMR spectroscopy.	0:135	Typing of core and backbone domains of mucin-type oligosaccharides from human ovarian-cyst glycoproteins by 500-MHz 1H-NMR spectroscopy.
3709529	4	26	theme	primary	505:511	arg1	structures					513:522	Their primary structures	499:522	Their primary structures	499:522	Their primary structures could be adequately characterized.
3709529	6	27	gly	glycoprotein	887:898	arg1	glycoprotein					887:898	ovarian-cyst glycoprotein	874:898	ovarian-cyst glycoprotein	874:898	The core type GlcNAc beta(1-3)GalNAc-ol is described for the first time as occurring in ovarian-cyst glycoprotein.
3709529	1	28	theme	Smith	220:224	arg1	degradation					226:236	Smith degradation	220:236	Smith degradation	220:236	Human blood-group A active glycoproteins from ovarian-cyst fluid were subjected to Smith degradation and subsequent beta-elimination.
3709529	0	29	theme	domains	28:34	arg1	Typing					0:5	Typing	0:5	Typing of core and backbone domains of mucin-type oligosaccharides from human ovarian-cyst glycoproteins by 500-MHz 1H-NMR spectroscopy.	0:135	Typing of core and backbone domains of mucin-type oligosaccharides from human ovarian-cyst glycoproteins by 500-MHz 1H-NMR spectroscopy.
3709529	0	30	theme	backbone	19:26	arg1	domains					28:34	backbone domains	19:34	backbone domains	19:34	Typing of core and backbone domains of mucin-type oligosaccharides from human ovarian-cyst glycoproteins by 500-MHz 1H-NMR spectroscopy.
3709529	0	30	theme	backbone	19:26	arg1	oligosaccharides					50:65	mucin-type oligosaccharides	39:65	mucin-type oligosaccharides from human ovarian-cyst glycoproteins	39:103	Typing of core and backbone domains of mucin-type oligosaccharides from human ovarian-cyst glycoproteins by 500-MHz 1H-NMR spectroscopy.
3709529	0	31	theme	mucin-type	39:48	arg1	oligosaccharides					50:65	mucin-type oligosaccharides	39:65	mucin-type oligosaccharides from human ovarian-cyst glycoproteins	39:103	Typing of core and backbone domains of mucin-type oligosaccharides from human ovarian-cyst glycoproteins by 500-MHz 1H-NMR spectroscopy.
3709529	5	32	theme	substitution	599:610	arg1	patterns					612:619	the substitution patterns	595:619	the substitution patterns of N-acetylgalactosaminitol (GalNAc-ol) as well as the types of backbone, i.e. the linkage types of alternating Gal-GlcNAc sequences	595:752	In particular, the core types, i.e. the substitution patterns of N-acetylgalactosaminitol (GalNAc-ol) as well as the types of backbone, i.e. the linkage types of alternating Gal-GlcNAc sequences, were unambiguously identified.
3709529	5	33	theme	alternating	721:731	arg1	sequences					744:752	alternating Gal-GlcNAc sequences	721:752	alternating Gal-GlcNAc sequences	721:752	In particular, the core types, i.e. the substitution patterns of N-acetylgalactosaminitol (GalNAc-ol) as well as the types of backbone, i.e. the linkage types of alternating Gal-GlcNAc sequences, were unambiguously identified.
3709529	6	34	theme	ovarian-cyst	874:885	arg1	glycoprotein					887:898	ovarian-cyst glycoprotein	874:898	ovarian-cyst glycoprotein	874:898	The core type GlcNAc beta(1-3)GalNAc-ol is described for the first time as occurring in ovarian-cyst glycoprotein.
3709529	6	35	theme	beta	807:810	arg1	GalNAc-ol					816:824	The core type GlcNAc beta(1-3)GalNAc-ol	786:824	The core type GlcNAc beta(1-3)GalNAc-ol	786:824	The core type GlcNAc beta(1-3)GalNAc-ol is described for the first time as occurring in ovarian-cyst glycoprotein.
3709529	2	36	link	O-linked	357:364	arg1	chains					379:384	the O-linked carbohydrate chains	353:384	the O-linked carbohydrate chains	353:384	The resulting oligosaccharide-alditols represent the core and backbone domains of the O-linked carbohydrate chains.
3709529	5	37	theme	Gal-GlcNAc	733:742	arg1	sequences					744:752	alternating Gal-GlcNAc sequences	721:752	alternating Gal-GlcNAc sequences	721:752	In particular, the core types, i.e. the substitution patterns of N-acetylgalactosaminitol (GalNAc-ol) as well as the types of backbone, i.e. the linkage types of alternating Gal-GlcNAc sequences, were unambiguously identified.
3709529	6	38	theme	GlcNAc	800:805	arg1	beta					807:810	core type GlcNAc beta	790:810	The core type GlcNAc beta(1-3)GalNAc-ol	786:824	The core type GlcNAc beta(1-3)GalNAc-ol is described for the first time as occurring in ovarian-cyst glycoprotein.
3709529	6	38	theme	GlcNAc	800:805	arg1	1-3					812:814	1-3	812:814	1-3	812:814	The core type GlcNAc beta(1-3)GalNAc-ol is described for the first time as occurring in ovarian-cyst glycoprotein.
3709529	1	39	theme	Human	137:141	arg1	glycoproteins					164:176	Human blood-group A active glycoproteins	137:176	Human blood-group A active glycoproteins from ovarian-cyst fluid	137:200	Human blood-group A active glycoproteins from ovarian-cyst fluid were subjected to Smith degradation and subsequent beta-elimination.
3709529	1	40	theme	subsequent	242:251	arg1	beta-elimination					253:268	subsequent beta-elimination	242:268	subsequent beta-elimination	242:268	Human blood-group A active glycoproteins from ovarian-cyst fluid were subjected to Smith degradation and subsequent beta-elimination.
3709529	1	41	gly	glycoproteins	164:176	arg1	glycoproteins					164:176	Human blood-group A active glycoproteins	137:176	Human blood-group A active glycoproteins from ovarian-cyst fluid	137:200	Human blood-group A active glycoproteins from ovarian-cyst fluid were subjected to Smith degradation and subsequent beta-elimination.
3709529	5	42	theme	core	578:581	arg1	types					583:587	the core types	574:587	the core types	574:587	In particular, the core types, i.e. the substitution patterns of N-acetylgalactosaminitol (GalNAc-ol) as well as the types of backbone, i.e. the linkage types of alternating Gal-GlcNAc sequences, were unambiguously identified.
3709529	1	43	theme	blood-group	143:153	arg1	glycoproteins					164:176	Human blood-group A active glycoproteins	137:176	Human blood-group A active glycoproteins from ovarian-cyst fluid	137:200	Human blood-group A active glycoproteins from ovarian-cyst fluid were subjected to Smith degradation and subsequent beta-elimination.
3709529	0	44	from	glycoproteins	91:103	arg1	core					10:13	core	10:13	core	10:13	Typing of core and backbone domains of mucin-type oligosaccharides from human ovarian-cyst glycoproteins by 500-MHz 1H-NMR spectroscopy.
3709529	0	44	from	glycoproteins	91:103	arg1	domains					28:34	backbone domains	19:34	backbone domains	19:34	Typing of core and backbone domains of mucin-type oligosaccharides from human ovarian-cyst glycoproteins by 500-MHz 1H-NMR spectroscopy.
3709529	0	44	from	glycoproteins	91:103	arg1	oligosaccharides					50:65	mucin-type oligosaccharides	39:65	mucin-type oligosaccharides from human ovarian-cyst glycoproteins	39:103	Typing of core and backbone domains of mucin-type oligosaccharides from human ovarian-cyst glycoproteins by 500-MHz 1H-NMR spectroscopy.
3709529	6	45	theme	core	790:793	arg1	beta					807:810	core type GlcNAc beta	790:810	The core type GlcNAc beta(1-3)GalNAc-ol	786:824	The core type GlcNAc beta(1-3)GalNAc-ol is described for the first time as occurring in ovarian-cyst glycoprotein.
3709529	6	45	theme	core	790:793	arg1	1-3					812:814	1-3	812:814	1-3	812:814	The core type GlcNAc beta(1-3)GalNAc-ol is described for the first time as occurring in ovarian-cyst glycoprotein.
3709529	1	46	theme	A	155:155	arg1	glycoproteins					164:176	Human blood-group A active glycoproteins	137:176	Human blood-group A active glycoproteins from ovarian-cyst fluid	137:200	Human blood-group A active glycoproteins from ovarian-cyst fluid were subjected to Smith degradation and subsequent beta-elimination.
3709529	0	47	theme	oligosaccharides	50:65	arg1	core					10:13	core	10:13	core	10:13	Typing of core and backbone domains of mucin-type oligosaccharides from human ovarian-cyst glycoproteins by 500-MHz 1H-NMR spectroscopy.
3709529	0	47	theme	oligosaccharides	50:65	arg1	domains					28:34	backbone domains	19:34	backbone domains	19:34	Typing of core and backbone domains of mucin-type oligosaccharides from human ovarian-cyst glycoproteins by 500-MHz 1H-NMR spectroscopy.
3709529	0	47	theme	oligosaccharides	50:65	arg1	oligosaccharides					50:65	mucin-type oligosaccharides	39:65	mucin-type oligosaccharides from human ovarian-cyst glycoproteins	39:103	Typing of core and backbone domains of mucin-type oligosaccharides from human ovarian-cyst glycoproteins by 500-MHz 1H-NMR spectroscopy.
3709529	2	48	theme	resulting	275:283	arg1	oligosaccharide-alditols					285:308	The resulting oligosaccharide-alditols	271:308	The resulting oligosaccharide-alditols	271:308	The resulting oligosaccharide-alditols represent the core and backbone domains of the O-linked carbohydrate chains.
3709529	1	49	theme	active	157:162	arg1	glycoproteins					164:176	Human blood-group A active glycoproteins	137:176	Human blood-group A active glycoproteins from ovarian-cyst fluid	137:200	Human blood-group A active glycoproteins from ovarian-cyst fluid were subjected to Smith degradation and subsequent beta-elimination.
6539332	6	0	theme	chains	1930:1935	arg1	structure					1895:1903	the core structure	1886:1903	the core structure of the carbohydrate side chains in the blood group substances as proposed by K. O. Lloyd and E. A. Kabat [1968) Proc	1886:2020	Together they provide direct evidence for the core structure of the carbohydrate side chains in the blood group substances as proposed by K. O. Lloyd and E. A. Kabat [1968) Proc.
6539332	6	1	from	chains	1930:1935	arg1	substances					1956:1965	the blood group substances	1940:1965	the blood group substances as proposed by K. O. Lloyd and E. A. Kabat [1968) Proc	1940:2020	Together they provide direct evidence for the core structure of the carbohydrate side chains in the blood group substances as proposed by K. O. Lloyd and E. A. Kabat [1968) Proc.
6539332	10	2	theme	B	2177:2177	arg1	substances					2179:2188	intact human ovarian cyst fluid HLeb , Lea, and B substances	2129:2188	intact human ovarian cyst fluid HLeb , Lea, and B substances	2129:2188	Oligosaccharides previously isolated after Carlson degradation of intact human ovarian cyst fluid HLeb , Lea, and B substances and from human and horse B substances contained various alpha-linked L- fucopyranose and alpha-linked Gal substitutions on the composite structure.
6539332	6	3	theme	carbohydrate	1912:1923	arg1	chains					1930:1935	the carbohydrate side chains	1908:1935	the carbohydrate side chains in the blood group substances as proposed by K. O. Lloyd and E. A. Kabat [1968) Proc	1908:2020	Together they provide direct evidence for the core structure of the carbohydrate side chains in the blood group substances as proposed by K. O. Lloyd and E. A. Kabat [1968) Proc.
6539332	4	4	theme	methylation	711:721	arg1	analysis					723:730	methylation analysis	711:730	methylation analysis	711:730	Structures were established based on sugar composition, periodate oxidation, methylation analysis, and analysis of oligosaccharide alditols as permethylated and N-trifluoroacetylated derivatives by gas-liquid chromatography-mass spectrometry.
6539332	1	5	gly	glycoproteins	225:237	arg1	glycoproteins					225:237	blood group A active glycoproteins	204:237	blood group A active glycoproteins	204:237	Purification and characterization of radioactive 3H-reduced di- to hexasaccharides produced by alkaline beta-elimination-borohydride 3H reduction of Smith degraded blood group A active glycoproteins.
6539332	3	6	theme	paper	571:575	arg1	chromatography					577:590	paper chromatography	571:590	paper chromatography	571:590	The carbohydrate mixture was fractionated by gel filtration, elution from charcoal, paper chromatography, and high pressure liquid chromatography.
6539332	1	7	theme	group	210:214	arg1	A					216:216	blood group A	204:216	blood group A active glycoproteins	204:237	Purification and characterization of radioactive 3H-reduced di- to hexasaccharides produced by alkaline beta-elimination-borohydride 3H reduction of Smith degraded blood group A active glycoproteins.
6539332	6	8	theme	core	1890:1893	arg1	structure					1895:1903	the core structure	1886:1903	the core structure of the carbohydrate side chains in the blood group substances as proposed by K. O. Lloyd and E. A. Kabat [1968) Proc	1886:2020	Together they provide direct evidence for the core structure of the carbohydrate side chains in the blood group substances as proposed by K. O. Lloyd and E. A. Kabat [1968) Proc.
6539332	2	9	theme	Smith	333:337	arg1	degradation					339:349	Smith degradation	333:349	Smith degradation followed by alkaline beta-elimination in the presence of NaB[ 3H4	333:415	Treatment of blood group A active glycoprotein from human ovarian cyst fluid by one stage of Smith degradation followed by alkaline beta-elimination in the presence of NaB[ 3H4 ] (Carlson degradation) liberated tritiated oligosaccharide alditols.
6539332	1	10	theme	active	218:223	arg1	glycoproteins					225:237	blood group A active glycoproteins	204:237	blood group A active glycoproteins	204:237	Purification and characterization of radioactive 3H-reduced di- to hexasaccharides produced by alkaline beta-elimination-borohydride 3H reduction of Smith degraded blood group A active glycoproteins.
6539332	2	11	dep	group	259:263	arg1	glycoprotein					274:285	A active glycoprotein	265:285	blood group A active glycoprotein from human ovarian cyst fluid	253:315	Treatment of blood group A active glycoprotein from human ovarian cyst fluid by one stage of Smith degradation followed by alkaline beta-elimination in the presence of NaB[ 3H4 ] (Carlson degradation) liberated tritiated oligosaccharide alditols.
6539332	3	12	theme	high	597:600	arg1	chromatography					618:631	high pressure liquid chromatography	597:631	high pressure liquid chromatography	597:631	The carbohydrate mixture was fractionated by gel filtration, elution from charcoal, paper chromatography, and high pressure liquid chromatography.
6539332	0	13	theme	blood	26:30	arg1	groups					32:37	blood groups	26:37	blood groups	26:37	Immunochemical studies on blood groups.
6539332	6	14	theme	group	1950:1954	arg1	substances					1956:1965	the blood group substances	1940:1965	the blood group substances as proposed by K. O. Lloyd and E. A. Kabat [1968) Proc	1940:2020	Together they provide direct evidence for the core structure of the carbohydrate side chains in the blood group substances as proposed by K. O. Lloyd and E. A. Kabat [1968) Proc.
6539332	2	15	theme	blood	253:257	arg1	group					259:263	blood group	253:263	blood group A active glycoprotein from human ovarian cyst fluid	253:315	Treatment of blood group A active glycoprotein from human ovarian cyst fluid by one stage of Smith degradation followed by alkaline beta-elimination in the presence of NaB[ 3H4 ] (Carlson degradation) liberated tritiated oligosaccharide alditols.
6539332	1	16	theme	alkaline	135:142	arg1	reduction					176:184	alkaline beta-elimination-borohydride 3H reduction	135:184	alkaline beta-elimination-borohydride 3H reduction of Smith	135:193	Purification and characterization of radioactive 3H-reduced di- to hexasaccharides produced by alkaline beta-elimination-borohydride 3H reduction of Smith degraded blood group A active glycoproteins.
6539332	2	17	from	fluid	311:315	arg1	glycoprotein					274:285	A active glycoprotein	265:285	blood group A active glycoprotein from human ovarian cyst fluid	253:315	Treatment of blood group A active glycoprotein from human ovarian cyst fluid by one stage of Smith degradation followed by alkaline beta-elimination in the presence of NaB[ 3H4 ] (Carlson degradation) liberated tritiated oligosaccharide alditols.
6539332	2	18	theme	human	292:296	arg1	fluid					311:315	human ovarian cyst fluid	292:315	human ovarian cyst fluid	292:315	Treatment of blood group A active glycoprotein from human ovarian cyst fluid by one stage of Smith degradation followed by alkaline beta-elimination in the presence of NaB[ 3H4 ] (Carlson degradation) liberated tritiated oligosaccharide alditols.
6539332	1	19	theme	3H	173:174	arg1	reduction					176:184	alkaline beta-elimination-borohydride 3H reduction	135:184	alkaline beta-elimination-borohydride 3H reduction of Smith	135:193	Purification and characterization of radioactive 3H-reduced di- to hexasaccharides produced by alkaline beta-elimination-borohydride 3H reduction of Smith degraded blood group A active glycoproteins.
6539332	10	20	from	substitutions	2296:2308	arg1	structure					2327:2335	the composite structure	2313:2335	the composite structure	2313:2335	Oligosaccharides previously isolated after Carlson degradation of intact human ovarian cyst fluid HLeb , Lea, and B substances and from human and horse B substances contained various alpha-linked L- fucopyranose and alpha-linked Gal substitutions on the composite structure.
6539332	4	21	theme	oligosaccharide	749:763	arg1	alditols					765:772	oligosaccharide alditols	749:772	oligosaccharide alditols as permethylated and N-trifluoroacetylated derivatives	749:827	Structures were established based on sugar composition, periodate oxidation, methylation analysis, and analysis of oligosaccharide alditols as permethylated and N-trifluoroacetylated derivatives by gas-liquid chromatography-mass spectrometry.
6539332	10	22	theme	horse	2209:2213	arg1	substances					2217:2226	horse B substances	2209:2226	horse B substances	2209:2226	Oligosaccharides previously isolated after Carlson degradation of intact human ovarian cyst fluid HLeb , Lea, and B substances and from human and horse B substances contained various alpha-linked L- fucopyranose and alpha-linked Gal substitutions on the composite structure.
6539332	10	23	theme	L-	2259:2260	arg1	fucopyranose					2262:2273	alpha-linked L- fucopyranose	2246:2273	alpha-linked L- fucopyranose	2246:2273	Oligosaccharides previously isolated after Carlson degradation of intact human ovarian cyst fluid HLeb , Lea, and B substances and from human and horse B substances contained various alpha-linked L- fucopyranose and alpha-linked Gal substitutions on the composite structure.
6539332	1	24	theme	3H-reduced	89:98	arg1	di-					100:102	radioactive 3H-reduced di-	77:102	radioactive 3H-reduced di-	77:102	Purification and characterization of radioactive 3H-reduced di- to hexasaccharides produced by alkaline beta-elimination-borohydride 3H reduction of Smith degraded blood group A active glycoproteins.
6539332	10	25	theme	various	2238:2244	arg1	substitutions					2296:2308	various alpha-linked L- fucopyranose and alpha-linked Gal substitutions	2238:2308	various alpha-linked L- fucopyranose and alpha-linked Gal substitutions on the composite structure	2238:2335	Oligosaccharides previously isolated after Carlson degradation of intact human ovarian cyst fluid HLeb , Lea, and B substances and from human and horse B substances contained various alpha-linked L- fucopyranose and alpha-linked Gal substitutions on the composite structure.
6539332	2	26	theme	3H4	413:415	arg1	presence					396:403	the presence	392:403	the presence of NaB[ 3H4	392:415	Treatment of blood group A active glycoprotein from human ovarian cyst fluid by one stage of Smith degradation followed by alkaline beta-elimination in the presence of NaB[ 3H4 ] (Carlson degradation) liberated tritiated oligosaccharide alditols.
6539332	0	27	theme	Immunochemical	0:13	arg1	studies					15:21	Immunochemical studies	0:21	Immunochemical studies on blood groups	0:37	Immunochemical studies on blood groups.
6539332	2	28	theme	oligosaccharide	461:475	arg1	alditols					477:484	tritiated oligosaccharide alditols	451:484	tritiated oligosaccharide alditols	451:484	Treatment of blood group A active glycoprotein from human ovarian cyst fluid by one stage of Smith degradation followed by alkaline beta-elimination in the presence of NaB[ 3H4 ] (Carlson degradation) liberated tritiated oligosaccharide alditols.
6539332	10	29	link	alpha-linked	2246:2257	arg1	fucopyranose					2262:2273	alpha-linked L- fucopyranose	2246:2273	alpha-linked L- fucopyranose	2246:2273	Oligosaccharides previously isolated after Carlson degradation of intact human ovarian cyst fluid HLeb , Lea, and B substances and from human and horse B substances contained various alpha-linked L- fucopyranose and alpha-linked Gal substitutions on the composite structure.
6539332	4	30	theme	gas-liquid	832:841	arg1	spectrometry					863:874	gas-liquid chromatography-mass spectrometry	832:874	gas-liquid chromatography-mass spectrometry	832:874	Structures were established based on sugar composition, periodate oxidation, methylation analysis, and analysis of oligosaccharide alditols as permethylated and N-trifluoroacetylated derivatives by gas-liquid chromatography-mass spectrometry.
6539332	10	31	theme	Gal	2292:2294	arg1	substitutions					2296:2308	various alpha-linked L- fucopyranose and alpha-linked Gal substitutions	2238:2308	various alpha-linked L- fucopyranose and alpha-linked Gal substitutions on the composite structure	2238:2335	Oligosaccharides previously isolated after Carlson degradation of intact human ovarian cyst fluid HLeb , Lea, and B substances and from human and horse B substances contained various alpha-linked L- fucopyranose and alpha-linked Gal substitutions on the composite structure.
6539332	5	32	theme	structures	1832:1841	arg1	pieces					1811:1816	pieces	1811:1816	pieces of the larger structures	1811:1841	The smaller structures represent pieces of the larger structures.
6539332	10	33	theme	Carlson	2106:2112	arg1	degradation					2114:2124	Carlson degradation	2106:2124	Carlson degradation of intact human ovarian cyst fluid HLeb , Lea, and B substances and from human and horse B substances	2106:2226	Oligosaccharides previously isolated after Carlson degradation of intact human ovarian cyst fluid HLeb , Lea, and B substances and from human and horse B substances contained various alpha-linked L- fucopyranose and alpha-linked Gal substitutions on the composite structure.
6539332	10	34	theme	cyst	2150:2153	arg1	HLeb					2161:2164	human ovarian cyst fluid HLeb	2136:2164	human ovarian cyst fluid HLeb	2136:2164	Oligosaccharides previously isolated after Carlson degradation of intact human ovarian cyst fluid HLeb , Lea, and B substances and from human and horse B substances contained various alpha-linked L- fucopyranose and alpha-linked Gal substitutions on the composite structure.
6539332	10	35	link	alpha-linked	2279:2290	arg1	Gal					2292:2294	alpha-linked Gal	2279:2294	alpha-linked Gal	2279:2294	Oligosaccharides previously isolated after Carlson degradation of intact human ovarian cyst fluid HLeb , Lea, and B substances and from human and horse B substances contained various alpha-linked L- fucopyranose and alpha-linked Gal substitutions on the composite structure.
6539332	10	36	theme	composite	2317:2325	arg1	structure					2327:2335	the composite structure	2313:2335	the composite structure	2313:2335	Oligosaccharides previously isolated after Carlson degradation of intact human ovarian cyst fluid HLeb , Lea, and B substances and from human and horse B substances contained various alpha-linked L- fucopyranose and alpha-linked Gal substitutions on the composite structure.
6539332	3	37	theme	gel	532:534	arg1	filtration					536:545	gel filtration	532:545	gel filtration	532:545	The carbohydrate mixture was fractionated by gel filtration, elution from charcoal, paper chromatography, and high pressure liquid chromatography.
6539332	10	38	theme	human	2136:2140	arg1	HLeb					2161:2164	human ovarian cyst fluid HLeb	2136:2164	human ovarian cyst fluid HLeb	2136:2164	Oligosaccharides previously isolated after Carlson degradation of intact human ovarian cyst fluid HLeb , Lea, and B substances and from human and horse B substances contained various alpha-linked L- fucopyranose and alpha-linked Gal substitutions on the composite structure.
6539332	6	39	from	substances	1956:1965	arg1	structure					1895:1903	the core structure	1886:1903	the core structure of the carbohydrate side chains in the blood group substances as proposed by K. O. Lloyd and E. A. Kabat [1968) Proc	1886:2020	Together they provide direct evidence for the core structure of the carbohydrate side chains in the blood group substances as proposed by K. O. Lloyd and E. A. Kabat [1968) Proc.
6539332	10	40	theme	Lea	2168:2170	arg1	substances					2179:2188	intact human ovarian cyst fluid HLeb , Lea, and B substances	2129:2188	intact human ovarian cyst fluid HLeb , Lea, and B substances	2129:2188	Oligosaccharides previously isolated after Carlson degradation of intact human ovarian cyst fluid HLeb , Lea, and B substances and from human and horse B substances contained various alpha-linked L- fucopyranose and alpha-linked Gal substitutions on the composite structure.
6539332	2	41	theme	cyst	306:309	arg1	fluid					311:315	human ovarian cyst fluid	292:315	human ovarian cyst fluid	292:315	Treatment of blood group A active glycoprotein from human ovarian cyst fluid by one stage of Smith degradation followed by alkaline beta-elimination in the presence of NaB[ 3H4 ] (Carlson degradation) liberated tritiated oligosaccharide alditols.
6539332	3	42	theme	carbohydrate	491:502	arg1	mixture					504:510	The carbohydrate mixture	487:510	The carbohydrate mixture	487:510	The carbohydrate mixture was fractionated by gel filtration, elution from charcoal, paper chromatography, and high pressure liquid chromatography.
6539332	10	43	theme	HLeb	2161:2164	arg1	substances					2179:2188	intact human ovarian cyst fluid HLeb , Lea, and B substances	2129:2188	intact human ovarian cyst fluid HLeb , Lea, and B substances	2129:2188	Oligosaccharides previously isolated after Carlson degradation of intact human ovarian cyst fluid HLeb , Lea, and B substances and from human and horse B substances contained various alpha-linked L- fucopyranose and alpha-linked Gal substitutions on the composite structure.
6539332	10	44	theme	substances	2179:2188	arg1	degradation					2114:2124	Carlson degradation	2106:2124	Carlson degradation of intact human ovarian cyst fluid HLeb , Lea, and B substances and from human and horse B substances	2106:2226	Oligosaccharides previously isolated after Carlson degradation of intact human ovarian cyst fluid HLeb , Lea, and B substances and from human and horse B substances contained various alpha-linked L- fucopyranose and alpha-linked Gal substitutions on the composite structure.
6539332	6	45	theme	side	1925:1928	arg1	chains					1930:1935	the carbohydrate side chains	1908:1935	the carbohydrate side chains in the blood group substances as proposed by K. O. Lloyd and E. A. Kabat [1968) Proc	1908:2020	Together they provide direct evidence for the core structure of the carbohydrate side chains in the blood group substances as proposed by K. O. Lloyd and E. A. Kabat [1968) Proc.
6539332	6	46	from	structure	1895:1903	arg1	substances					1956:1965	the blood group substances	1940:1965	the blood group substances as proposed by K. O. Lloyd and E. A. Kabat [1968) Proc	1940:2020	Together they provide direct evidence for the core structure of the carbohydrate side chains in the blood group substances as proposed by K. O. Lloyd and E. A. Kabat [1968) Proc.
6539332	3	47	theme	pressure	602:609	arg1	chromatography					618:631	high pressure liquid chromatography	597:631	high pressure liquid chromatography	597:631	The carbohydrate mixture was fractionated by gel filtration, elution from charcoal, paper chromatography, and high pressure liquid chromatography.
6539332	3	48	from	charcoal	561:568	arg1	chromatography					577:590	paper chromatography	571:590	paper chromatography	571:590	The carbohydrate mixture was fractionated by gel filtration, elution from charcoal, paper chromatography, and high pressure liquid chromatography.
6539332	3	48	from	charcoal	561:568	arg1	elution					548:554	elution	548:554	elution from charcoal	548:568	The carbohydrate mixture was fractionated by gel filtration, elution from charcoal, paper chromatography, and high pressure liquid chromatography.
6539332	3	48	from	charcoal	561:568	arg1	chromatography					618:631	high pressure liquid chromatography	597:631	high pressure liquid chromatography	597:631	The carbohydrate mixture was fractionated by gel filtration, elution from charcoal, paper chromatography, and high pressure liquid chromatography.
6539332	3	48	from	charcoal	561:568	arg1	filtration					536:545	gel filtration	532:545	gel filtration	532:545	The carbohydrate mixture was fractionated by gel filtration, elution from charcoal, paper chromatography, and high pressure liquid chromatography.
6539332	1	49	theme	blood	204:208	arg1	A					216:216	blood group A	204:216	blood group A active glycoproteins	204:237	Purification and characterization of radioactive 3H-reduced di- to hexasaccharides produced by alkaline beta-elimination-borohydride 3H reduction of Smith degraded blood group A active glycoproteins.
6539332	10	50	from	human	2199:2203	arg1	degradation					2114:2124	Carlson degradation	2106:2124	Carlson degradation of intact human ovarian cyst fluid HLeb , Lea, and B substances and from human and horse B substances	2106:2226	Oligosaccharides previously isolated after Carlson degradation of intact human ovarian cyst fluid HLeb , Lea, and B substances and from human and horse B substances contained various alpha-linked L- fucopyranose and alpha-linked Gal substitutions on the composite structure.
6539332	2	51	theme	degradation	339:349	arg1	stage					324:328	one stage	320:328	one stage of Smith degradation followed by alkaline beta-elimination in the presence of NaB[ 3H4	320:415	Treatment of blood group A active glycoprotein from human ovarian cyst fluid by one stage of Smith degradation followed by alkaline beta-elimination in the presence of NaB[ 3H4 ] (Carlson degradation) liberated tritiated oligosaccharide alditols.
6539332	1	52	theme	A	216:216	arg1	glycoproteins					225:237	blood group A active glycoproteins	204:237	blood group A active glycoproteins	204:237	Purification and characterization of radioactive 3H-reduced di- to hexasaccharides produced by alkaline beta-elimination-borohydride 3H reduction of Smith degraded blood group A active glycoproteins.
6539332	2	53	gly	glycoprotein	274:285	arg1	glycoprotein					274:285	A active glycoprotein	265:285	blood group A active glycoprotein from human ovarian cyst fluid	253:315	Treatment of blood group A active glycoprotein from human ovarian cyst fluid by one stage of Smith degradation followed by alkaline beta-elimination in the presence of NaB[ 3H4 ] (Carlson degradation) liberated tritiated oligosaccharide alditols.
6539332	3	54	theme	liquid	611:616	arg1	chromatography					618:631	high pressure liquid chromatography	597:631	high pressure liquid chromatography	597:631	The carbohydrate mixture was fractionated by gel filtration, elution from charcoal, paper chromatography, and high pressure liquid chromatography.
6539332	10	55	from	substances	2217:2226	arg1	degradation					2114:2124	Carlson degradation	2106:2124	Carlson degradation of intact human ovarian cyst fluid HLeb , Lea, and B substances and from human and horse B substances	2106:2226	Oligosaccharides previously isolated after Carlson degradation of intact human ovarian cyst fluid HLeb , Lea, and B substances and from human and horse B substances contained various alpha-linked L- fucopyranose and alpha-linked Gal substitutions on the composite structure.
6539332	2	56	theme	active	267:272	arg1	glycoprotein					274:285	A active glycoprotein	265:285	blood group A active glycoprotein from human ovarian cyst fluid	253:315	Treatment of blood group A active glycoprotein from human ovarian cyst fluid by one stage of Smith degradation followed by alkaline beta-elimination in the presence of NaB[ 3H4 ] (Carlson degradation) liberated tritiated oligosaccharide alditols.
6539332	4	57	theme	periodate	690:698	arg1	oxidation					700:708	periodate oxidation	690:708	periodate oxidation	690:708	Structures were established based on sugar composition, periodate oxidation, methylation analysis, and analysis of oligosaccharide alditols as permethylated and N-trifluoroacetylated derivatives by gas-liquid chromatography-mass spectrometry.
6539332	2	58	theme	group	259:263	arg1	degradation					428:438	Carlson degradation	420:438	Carlson degradation	420:438	Treatment of blood group A active glycoprotein from human ovarian cyst fluid by one stage of Smith degradation followed by alkaline beta-elimination in the presence of NaB[ 3H4 ] (Carlson degradation) liberated tritiated oligosaccharide alditols.
6539332	2	58	theme	group	259:263	arg1	Treatment					240:248	Treatment	240:248	Treatment of blood group A active glycoprotein from human ovarian cyst fluid by one stage of Smith degradation followed by alkaline beta-elimination in the presence of NaB[ 3H4 ] (Carlson degradation)	240:439	Treatment of blood group A active glycoprotein from human ovarian cyst fluid by one stage of Smith degradation followed by alkaline beta-elimination in the presence of NaB[ 3H4 ] (Carlson degradation) liberated tritiated oligosaccharide alditols.
6539332	6	59	theme	blood	1944:1948	arg1	substances					1956:1965	the blood group substances	1940:1965	the blood group substances as proposed by K. O. Lloyd and E. A. Kabat [1968) Proc	1940:2020	Together they provide direct evidence for the core structure of the carbohydrate side chains in the blood group substances as proposed by K. O. Lloyd and E. A. Kabat [1968) Proc.
6539332	4	60	theme	alditols	765:772	arg1	composition					677:687	sugar composition	671:687	sugar composition	671:687	Structures were established based on sugar composition, periodate oxidation, methylation analysis, and analysis of oligosaccharide alditols as permethylated and N-trifluoroacetylated derivatives by gas-liquid chromatography-mass spectrometry.
6539332	4	60	theme	alditols	765:772	arg1	oxidation					700:708	periodate oxidation	690:708	periodate oxidation	690:708	Structures were established based on sugar composition, periodate oxidation, methylation analysis, and analysis of oligosaccharide alditols as permethylated and N-trifluoroacetylated derivatives by gas-liquid chromatography-mass spectrometry.
6539332	4	60	theme	alditols	765:772	arg1	analysis					723:730	methylation analysis	711:730	methylation analysis	711:730	Structures were established based on sugar composition, periodate oxidation, methylation analysis, and analysis of oligosaccharide alditols as permethylated and N-trifluoroacetylated derivatives by gas-liquid chromatography-mass spectrometry.
6539332	4	60	theme	alditols	765:772	arg1	analysis					737:744	analysis	737:744	analysis of oligosaccharide alditols as permethylated and N-trifluoroacetylated derivatives by gas-liquid chromatography-mass spectrometry	737:874	Structures were established based on sugar composition, periodate oxidation, methylation analysis, and analysis of oligosaccharide alditols as permethylated and N-trifluoroacetylated derivatives by gas-liquid chromatography-mass spectrometry.
6539332	2	61	theme	ovarian	298:304	arg1	fluid					311:315	human ovarian cyst fluid	292:315	human ovarian cyst fluid	292:315	Treatment of blood group A active glycoprotein from human ovarian cyst fluid by one stage of Smith degradation followed by alkaline beta-elimination in the presence of NaB[ 3H4 ] (Carlson degradation) liberated tritiated oligosaccharide alditols.
6539332	1	62	theme	beta-elimination-borohydride	144:171	arg1	reduction					176:184	alkaline beta-elimination-borohydride 3H reduction	135:184	alkaline beta-elimination-borohydride 3H reduction of Smith	135:193	Purification and characterization of radioactive 3H-reduced di- to hexasaccharides produced by alkaline beta-elimination-borohydride 3H reduction of Smith degraded blood group A active glycoproteins.
6539332	4	63	theme	permethylated	777:789	arg1	derivatives					817:827	permethylated and N-trifluoroacetylated derivatives	777:827	permethylated and N-trifluoroacetylated derivatives	777:827	Structures were established based on sugar composition, periodate oxidation, methylation analysis, and analysis of oligosaccharide alditols as permethylated and N-trifluoroacetylated derivatives by gas-liquid chromatography-mass spectrometry.
6539332	10	64	contain	contained	2228:2236	arg2	substitutions					2296:2308	various alpha-linked L- fucopyranose and alpha-linked Gal substitutions	2238:2308	various alpha-linked L- fucopyranose and alpha-linked Gal substitutions on the composite structure	2238:2335	Oligosaccharides previously isolated after Carlson degradation of intact human ovarian cyst fluid HLeb , Lea, and B substances and from human and horse B substances contained various alpha-linked L- fucopyranose and alpha-linked Gal substitutions on the composite structure.
6539332	10	64	contain	contained	2228:2236	arg1	Oligosaccharides					2063:2078	Oligosaccharides	2063:2078	Oligosaccharides previously isolated after Carlson degradation of intact human ovarian cyst fluid HLeb , Lea, and B substances and from human and horse B substances	2063:2226	Oligosaccharides previously isolated after Carlson degradation of intact human ovarian cyst fluid HLeb , Lea, and B substances and from human and horse B substances contained various alpha-linked L- fucopyranose and alpha-linked Gal substitutions on the composite structure.
6539332	6	65	dep	Lloyd	1988:1992	arg1	Kabat					2004:2008	Kabat [1968)	2004:2015	K. O. Lloyd and E. A. Kabat [1968) Proc	1982:2020	Together they provide direct evidence for the core structure of the carbohydrate side chains in the blood group substances as proposed by K. O. Lloyd and E. A. Kabat [1968) Proc.
6539332	1	66	theme	Smith	189:193	arg1	reduction					176:184	alkaline beta-elimination-borohydride 3H reduction	135:184	alkaline beta-elimination-borohydride 3H reduction of Smith	135:193	Purification and characterization of radioactive 3H-reduced di- to hexasaccharides produced by alkaline beta-elimination-borohydride 3H reduction of Smith degraded blood group A active glycoproteins.
6539332	0	67	from	studies	15:21	arg1	groups					32:37	blood groups	26:37	blood groups	26:37	Immunochemical studies on blood groups.
6539332	10	68	theme	B	2215:2215	arg1	substances					2217:2226	horse B substances	2209:2226	horse B substances	2209:2226	Oligosaccharides previously isolated after Carlson degradation of intact human ovarian cyst fluid HLeb , Lea, and B substances and from human and horse B substances contained various alpha-linked L- fucopyranose and alpha-linked Gal substitutions on the composite structure.
6539332	4	69	theme	chromatography-mass	843:861	arg1	spectrometry					863:874	gas-liquid chromatography-mass spectrometry	832:874	gas-liquid chromatography-mass spectrometry	832:874	Structures were established based on sugar composition, periodate oxidation, methylation analysis, and analysis of oligosaccharide alditols as permethylated and N-trifluoroacetylated derivatives by gas-liquid chromatography-mass spectrometry.
6539332	10	70	theme	fucopyranose	2262:2273	arg1	substitutions					2296:2308	various alpha-linked L- fucopyranose and alpha-linked Gal substitutions	2238:2308	various alpha-linked L- fucopyranose and alpha-linked Gal substitutions on the composite structure	2238:2335	Oligosaccharides previously isolated after Carlson degradation of intact human ovarian cyst fluid HLeb , Lea, and B substances and from human and horse B substances contained various alpha-linked L- fucopyranose and alpha-linked Gal substitutions on the composite structure.
6539332	1	71	theme	radioactive	77:87	arg1	di-					100:102	radioactive 3H-reduced di-	77:102	radioactive 3H-reduced di-	77:102	Purification and characterization of radioactive 3H-reduced di- to hexasaccharides produced by alkaline beta-elimination-borohydride 3H reduction of Smith degraded blood group A active glycoproteins.
6539332	10	72	theme	alpha-linked	2246:2257	arg1	fucopyranose					2262:2273	alpha-linked L- fucopyranose	2246:2273	alpha-linked L- fucopyranose	2246:2273	Oligosaccharides previously isolated after Carlson degradation of intact human ovarian cyst fluid HLeb , Lea, and B substances and from human and horse B substances contained various alpha-linked L- fucopyranose and alpha-linked Gal substitutions on the composite structure.
6539332	1	73	theme	di-	100:102	arg1	characterization					57:72	characterization	57:72	characterization	57:72	Purification and characterization of radioactive 3H-reduced di- to hexasaccharides produced by alkaline beta-elimination-borohydride 3H reduction of Smith degraded blood group A active glycoproteins.
6539332	1	73	theme	di-	100:102	arg1	Purification					40:51	Purification	40:51	Purification	40:51	Purification and characterization of radioactive 3H-reduced di- to hexasaccharides produced by alkaline beta-elimination-borohydride 3H reduction of Smith degraded blood group A active glycoproteins.
6539332	4	74	theme	N-trifluoroacetylated	795:815	arg1	derivatives					817:827	permethylated and N-trifluoroacetylated derivatives	777:827	permethylated and N-trifluoroacetylated derivatives	777:827	Structures were established based on sugar composition, periodate oxidation, methylation analysis, and analysis of oligosaccharide alditols as permethylated and N-trifluoroacetylated derivatives by gas-liquid chromatography-mass spectrometry.
6539332	2	75	theme	NaB[	408:411	arg1	3H4					413:415	NaB[ 3H4	408:415	NaB[ 3H4	408:415	Treatment of blood group A active glycoprotein from human ovarian cyst fluid by one stage of Smith degradation followed by alkaline beta-elimination in the presence of NaB[ 3H4 ] (Carlson degradation) liberated tritiated oligosaccharide alditols.
6539332	5	76	theme	larger	1825:1830	arg1	structures					1832:1841	the larger structures	1821:1841	the larger structures	1821:1841	The smaller structures represent pieces of the larger structures.
6539332	2	77	theme	tritiated	451:459	arg1	alditols					477:484	tritiated oligosaccharide alditols	451:484	tritiated oligosaccharide alditols	451:484	Treatment of blood group A active glycoprotein from human ovarian cyst fluid by one stage of Smith degradation followed by alkaline beta-elimination in the presence of NaB[ 3H4 ] (Carlson degradation) liberated tritiated oligosaccharide alditols.
6539332	10	78	theme	alpha-linked	2279:2290	arg1	Gal					2292:2294	alpha-linked Gal	2279:2294	alpha-linked Gal	2279:2294	Oligosaccharides previously isolated after Carlson degradation of intact human ovarian cyst fluid HLeb , Lea, and B substances and from human and horse B substances contained various alpha-linked L- fucopyranose and alpha-linked Gal substitutions on the composite structure.
6539332	5	79	theme	smaller	1782:1788	arg1	structures					1790:1799	The smaller structures	1778:1799	The smaller structures	1778:1799	The smaller structures represent pieces of the larger structures.
6539332	2	80	theme	Carlson	420:426	arg1	degradation					428:438	Carlson degradation	420:438	Carlson degradation	420:438	Treatment of blood group A active glycoprotein from human ovarian cyst fluid by one stage of Smith degradation followed by alkaline beta-elimination in the presence of NaB[ 3H4 ] (Carlson degradation) liberated tritiated oligosaccharide alditols.
6539332	2	80	theme	Carlson	420:426	arg1	Treatment					240:248	Treatment	240:248	Treatment of blood group A active glycoprotein from human ovarian cyst fluid by one stage of Smith degradation followed by alkaline beta-elimination in the presence of NaB[ 3H4 ] (Carlson degradation)	240:439	Treatment of blood group A active glycoprotein from human ovarian cyst fluid by one stage of Smith degradation followed by alkaline beta-elimination in the presence of NaB[ 3H4 ] (Carlson degradation) liberated tritiated oligosaccharide alditols.
6539332	10	81	theme	ovarian	2142:2148	arg1	HLeb					2161:2164	human ovarian cyst fluid HLeb	2136:2164	human ovarian cyst fluid HLeb	2136:2164	Oligosaccharides previously isolated after Carlson degradation of intact human ovarian cyst fluid HLeb , Lea, and B substances and from human and horse B substances contained various alpha-linked L- fucopyranose and alpha-linked Gal substitutions on the composite structure.
6539332	6	82	theme	direct	1866:1871	arg1	evidence					1873:1880	direct evidence	1866:1880	direct evidence for the core structure of the carbohydrate side chains in the blood group substances as proposed by K. O. Lloyd and E. A. Kabat [1968) Proc	1866:2020	Together they provide direct evidence for the core structure of the carbohydrate side chains in the blood group substances as proposed by K. O. Lloyd and E. A. Kabat [1968) Proc.
6539332	2	83	theme	alkaline	363:370	arg1	beta-elimination					372:387	alkaline beta-elimination	363:387	alkaline beta-elimination	363:387	Treatment of blood group A active glycoprotein from human ovarian cyst fluid by one stage of Smith degradation followed by alkaline beta-elimination in the presence of NaB[ 3H4 ] (Carlson degradation) liberated tritiated oligosaccharide alditols.
6539332	10	84	theme	intact	2129:2134	arg1	substances					2179:2188	intact human ovarian cyst fluid HLeb , Lea, and B substances	2129:2188	intact human ovarian cyst fluid HLeb , Lea, and B substances	2129:2188	Oligosaccharides previously isolated after Carlson degradation of intact human ovarian cyst fluid HLeb , Lea, and B substances and from human and horse B substances contained various alpha-linked L- fucopyranose and alpha-linked Gal substitutions on the composite structure.
6539332	4	85	theme	sugar	671:675	arg1	composition					677:687	sugar composition	671:687	sugar composition	671:687	Structures were established based on sugar composition, periodate oxidation, methylation analysis, and analysis of oligosaccharide alditols as permethylated and N-trifluoroacetylated derivatives by gas-liquid chromatography-mass spectrometry.
6539332	10	86	theme	fluid	2155:2159	arg1	HLeb					2161:2164	human ovarian cyst fluid HLeb	2136:2164	human ovarian cyst fluid HLeb	2136:2164	Oligosaccharides previously isolated after Carlson degradation of intact human ovarian cyst fluid HLeb , Lea, and B substances and from human and horse B substances contained various alpha-linked L- fucopyranose and alpha-linked Gal substitutions on the composite structure.
6712992	3	0	dep	pentasaccharides	1077:1092	arg1	pentasaccharides					1077:1092	pentasaccharides II and III	1077:1103	pentasaccharides II and III	1077:1103	Of the oligosaccharides 60% had a molecular size of a decasaccharide or smaller, the tetra- and pentasaccharides II and III predominating.
6712992	3	0	dep	pentasaccharides	1077:1092	arg1	III					1101:1103	III	1101:1103	III	1101:1103	Of the oligosaccharides 60% had a molecular size of a decasaccharide or smaller, the tetra- and pentasaccharides II and III predominating.
6712992	3	0	dep	pentasaccharides	1077:1092	arg1	II					1094:1095	II	1094:1095	II	1094:1095	Of the oligosaccharides 60% had a molecular size of a decasaccharide or smaller, the tetra- and pentasaccharides II and III predominating.
6712992	2	1	theme	DGal1----3	942:951	arg1	DGal1----3					958:967	beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3	798:967	beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3	798:967	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	2	2	theme	beta	798:801	arg1	DGal1----3					958:967	beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3	798:967	beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3	798:967	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	3	3	dep	predominating	1105:1117	arg1	pentasaccharides					1077:1092	pentasaccharides II and III	1077:1103	pentasaccharides II and III	1077:1103	Of the oligosaccharides 60% had a molecular size of a decasaccharide or smaller, the tetra- and pentasaccharides II and III predominating.
6712992	3	3	dep	predominating	1105:1117	arg1	III					1101:1103	III	1101:1103	III	1101:1103	Of the oligosaccharides 60% had a molecular size of a decasaccharide or smaller, the tetra- and pentasaccharides II and III predominating.
6712992	3	3	dep	predominating	1105:1117	arg1	tetra-					1066:1071	tetra-	1066:1071	tetra-	1066:1071	Of the oligosaccharides 60% had a molecular size of a decasaccharide or smaller, the tetra- and pentasaccharides II and III predominating.
6712992	3	3	dep	predominating	1105:1117	arg1	II					1094:1095	II	1094:1095	II	1094:1095	Of the oligosaccharides 60% had a molecular size of a decasaccharide or smaller, the tetra- and pentasaccharides II and III predominating.
6712992	0	4	theme	H	70:70	arg1	glycoprotein					100:111	an I, H and Lea active ovarian cyst glycoprotein	64:111	glycoprotein	100:111	Structures of oligosaccharides cleaved by base-borohydride from an I, H and Lea active ovarian cyst glycoprotein.
6712992	2	5	theme	beta	937:940	arg1	DGal1----3					958:967	beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3	798:967	beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3	798:967	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	3	6	theme	decasaccharide	1035:1048	arg1	predominating					1105:1117	a decasaccharide or smaller, the tetra- and pentasaccharides II and III predominating	1033:1117	predominating	1105:1117	Of the oligosaccharides 60% had a molecular size of a decasaccharide or smaller, the tetra- and pentasaccharides II and III predominating.
6712992	1	7	gly	glycoprotein	205:216	arg1	glycoprotein					205:216	an I, H and Lea active ovarian cyst glycoprotein	169:216	glycoprotein	205:216	Oligosaccharides were cleaved by base-borohydride from an I, H and Lea active ovarian cyst glycoprotein and purified by Bio-Gel P-6 and paper chromatography.
6712992	1	8	theme	Bio-Gel	234:240	arg1	P-6					242:244	Bio-Gel P-6 and paper chromatography	234:269	P-6	242:244	Oligosaccharides were cleaved by base-borohydride from an I, H and Lea active ovarian cyst glycoprotein and purified by Bio-Gel P-6 and paper chromatography.
6712992	0	9	theme	active	80:85	arg1	glycoprotein					100:111	an I, H and Lea active ovarian cyst glycoprotein	64:111	glycoprotein	100:111	Structures of oligosaccharides cleaved by base-borohydride from an I, H and Lea active ovarian cyst glycoprotein.
6712992	2	10	theme	DGlcNAc1----3	923:935	arg1	DGal1----3					958:967	beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3	798:967	beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3	798:967	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	4	11	theme	other	1210:1214	arg1	laboratories					1216:1227	other laboratories	1210:1227	other laboratories	1210:1227	Oligosaccharides I through IV have been previously isolated from several glycoproteins by other laboratories; the decasaccharide, V, is a new structure.
6712992	2	12	theme	DGlcNAc1----3	836:848	arg1	DGal1----3					958:967	beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3	798:967	beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3	798:967	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	0	13	theme	Lea	76:78	arg1	glycoprotein					100:111	an I, H and Lea active ovarian cyst glycoprotein	64:111	glycoprotein	100:111	Structures of oligosaccharides cleaved by base-borohydride from an I, H and Lea active ovarian cyst glycoprotein.
6712992	2	14	theme	beta	744:747	arg1	DGal1NAcol					779:788	beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol	677:788	beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol	677:788	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	2	15	theme	beta	831:834	arg1	DGal1----3					958:967	beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3	798:967	beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3	798:967	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	0	16	theme	cyst	95:98	arg1	glycoprotein					100:111	an I, H and Lea active ovarian cyst glycoprotein	64:111	glycoprotein	100:111	Structures of oligosaccharides cleaved by base-borohydride from an I, H and Lea active ovarian cyst glycoprotein.
6712992	2	17	theme	compositional	327:339	arg1	analyses					341:348	compositional analyses	327:348	compositional analyses	327:348	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	2	18	theme	DGal1----4	615:624	arg1	beta					626:629	alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6	593:643	alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol	593:670	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	2	18	theme	DGal1----4	615:624	arg1	beta					645:648	beta DGal1----3	645:659	beta DGal1----3	645:659	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	2	19	theme	beta	626:629	arg1	DGalNAc-ol					661:670	alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol	593:670	alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol	593:670	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	2	20	theme	DGal1----4	733:742	arg1	alpha					693:697	alpha LFuc1----4	693:708	alpha LFuc1----4	693:708	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	2	20	theme	DGal1----4	733:742	arg1	beta					744:747	beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6	677:761	beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol	677:788	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	2	20	theme	DGal1----4	733:742	arg1	beta					763:766	beta DGal1----3	763:777	beta DGal1----3	763:777	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	2	21	theme	acid	393:396	arg1	oxidation					398:406	chronic acid oxidation	385:406	chronic acid oxidation	385:406	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	0	22	theme	ovarian	87:93	arg1	glycoprotein					100:111	an I, H and Lea active ovarian cyst glycoprotein	64:111	glycoprotein	100:111	Structures of oligosaccharides cleaved by base-borohydride from an I, H and Lea active ovarian cyst glycoprotein.
6712992	2	23	theme	beta	610:613	arg1	beta					626:629	alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6	593:643	alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol	593:670	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	2	23	theme	beta	610:613	arg1	beta					645:648	beta DGal1----3	645:659	beta DGal1----3	645:659	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	4	24	theme	several	1185:1191	arg1	glycoproteins					1193:1205	several glycoproteins	1185:1205	several glycoproteins	1185:1205	Oligosaccharides I through IV have been previously isolated from several glycoproteins by other laboratories; the decasaccharide, V, is a new structure.
6712992	2	25	theme	DGlcNAc1----3beta	715:731	arg1	alpha					693:697	alpha LFuc1----4	693:708	alpha LFuc1----4	693:708	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	2	25	theme	DGlcNAc1----3beta	715:731	arg1	beta					744:747	beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6	677:761	beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol	677:788	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	2	25	theme	DGlcNAc1----3beta	715:731	arg1	beta					763:766	beta DGal1----3	763:777	beta DGal1----3	763:777	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	1	26	theme	I	172:172	arg1	glycoprotein					205:216	an I, H and Lea active ovarian cyst glycoprotein	169:216	glycoprotein	205:216	Oligosaccharides were cleaved by base-borohydride from an I, H and Lea active ovarian cyst glycoprotein and purified by Bio-Gel P-6 and paper chromatography.
6712992	3	27	contain	had	1009:1011	arg2	size					1025:1028	a molecular size	1013:1028	a molecular size of a decasaccharide or smaller, the tetra- and pentasaccharides II and III predominating	1013:1117	Of the oligosaccharides 60% had a molecular size of a decasaccharide or smaller, the tetra- and pentasaccharides II and III predominating.
6712992	3	27	contain	had	1009:1011	arg1	%					1007:1007	60%	1005:1007	60%	1005:1007	Of the oligosaccharides 60% had a molecular size of a decasaccharide or smaller, the tetra- and pentasaccharides II and III predominating.
6712992	2	28	theme	oligosaccharide	475:489	arg1	I					491:491	oligosaccharide I	475:491	oligosaccharide I	475:491	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	2	28	theme	oligosaccharide	475:489	arg1	DGal1----3DGalNAc-ol					499:518	beta DGal1----3DGalNAc-ol	494:518	beta DGal1----3DGalNAc-ol	494:518	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	2	29	theme	LFuc1----2	599:608	arg1	beta					626:629	alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6	593:643	alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol	593:670	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	2	29	theme	LFuc1----2	599:608	arg1	beta					645:648	beta DGal1----3	645:659	beta DGal1----3	645:659	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	3	30	theme	molecular	1015:1023	arg1	size					1025:1028	a molecular size	1013:1028	a molecular size of a decasaccharide or smaller, the tetra- and pentasaccharides II and III predominating	1013:1117	Of the oligosaccharides 60% had a molecular size of a decasaccharide or smaller, the tetra- and pentasaccharides II and III predominating.
6712992	2	31	theme	oligosaccharides	295:310	arg1	DGalNAc-ol					969:978	DGalNAc-ol	969:978	DGalNAc-ol	969:978	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	2	31	theme	oligosaccharides	295:310	arg1	structures					276:285	The structures	272:285	The structures	272:285	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	2	32	theme	beta	710:713	arg1	alpha					693:697	alpha LFuc1----4	693:708	alpha LFuc1----4	693:708	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	2	32	theme	beta	710:713	arg1	beta					744:747	beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6	677:761	beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol	677:788	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	2	32	theme	beta	710:713	arg1	beta					763:766	beta DGal1----3	763:777	beta DGal1----3	763:777	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	4	33	gly	glycoproteins	1193:1205	arg1	glycoproteins					1193:1205	several glycoproteins	1185:1205	several glycoproteins	1185:1205	Oligosaccharides I through IV have been previously isolated from several glycoproteins by other laboratories; the decasaccharide, V, is a new structure.
6712992	1	34	theme	paper	250:254	arg1	chromatography					256:269	Bio-Gel P-6 and paper chromatography	234:269	chromatography	256:269	Oligosaccharides were cleaved by base-borohydride from an I, H and Lea active ovarian cyst glycoprotein and purified by Bio-Gel P-6 and paper chromatography.
6712992	2	35	theme	alpha	593:597	arg1	beta					626:629	alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6	593:643	alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol	593:670	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	2	35	theme	alpha	593:597	arg1	beta					645:648	beta DGal1----3	645:659	beta DGal1----3	645:659	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	1	36	theme	H	175:175	arg1	glycoprotein					205:216	an I, H and Lea active ovarian cyst glycoprotein	169:216	glycoprotein	205:216	Oligosaccharides were cleaved by base-borohydride from an I, H and Lea active ovarian cyst glycoprotein and purified by Bio-Gel P-6 and paper chromatography.
6712992	2	37	theme	enzymatic	434:442	arg1	degradations					444:455	enzymatic degradations	434:455	enzymatic degradations	434:455	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	2	38	dep	beta	541:544	arg1	DGalNAc-ol					576:585	DGalNAc-ol	576:585	beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol	525:585	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	0	39	theme	oligosaccharides	14:29	arg1	Structures					0:9	Structures	0:9	Structures of oligosaccharides	0:29	Structures of oligosaccharides cleaved by base-borohydride from an I, H and Lea active ovarian cyst glycoprotein.
6712992	2	40	theme	DGlcNAc1----6[beta	871:888	arg1	DGal1----3					958:967	beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3	798:967	beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3	798:967	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	1	41	theme	Lea	181:183	arg1	glycoprotein					205:216	an I, H and Lea active ovarian cyst glycoprotein	169:216	glycoprotein	205:216	Oligosaccharides were cleaved by base-borohydride from an I, H and Lea active ovarian cyst glycoprotein and purified by Bio-Gel P-6 and paper chromatography.
6712992	2	42	theme	beta	866:869	arg1	DGal1----3					958:967	beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3	798:967	beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3	798:967	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	2	43	theme	methylation	409:419	arg1	analyses					421:428	methylation analyses	409:428	methylation analyses	409:428	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	1	44	theme	active	185:190	arg1	glycoprotein					205:216	an I, H and Lea active ovarian cyst glycoprotein	169:216	glycoprotein	205:216	Oligosaccharides were cleaved by base-borohydride from an I, H and Lea active ovarian cyst glycoprotein and purified by Bio-Gel P-6 and paper chromatography.
6712992	2	45	theme	beta	918:921	arg1	DGal1----3					958:967	beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3	798:967	beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3	798:967	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	2	46	theme	beta	850:853	arg1	DGal1----3					958:967	beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3	798:967	beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3	798:967	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	2	47	theme	DGal1----3	682:691	arg1	alpha					693:697	alpha LFuc1----4	693:708	alpha LFuc1----4	693:708	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	2	47	theme	DGal1----3	682:691	arg1	beta					744:747	beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6	677:761	beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol	677:788	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	2	47	theme	DGal1----3	682:691	arg1	beta					763:766	beta DGal1----3	763:777	beta DGal1----3	763:777	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	1	48	theme	ovarian	192:198	arg1	glycoprotein					205:216	an I, H and Lea active ovarian cyst glycoprotein	169:216	glycoprotein	205:216	Oligosaccharides were cleaved by base-borohydride from an I, H and Lea active ovarian cyst glycoprotein and purified by Bio-Gel P-6 and paper chromatography.
6712992	3	49	theme	smaller	1053:1059	arg1	predominating					1105:1117	a decasaccharide or smaller, the tetra- and pentasaccharides II and III predominating	1033:1117	predominating	1105:1117	Of the oligosaccharides 60% had a molecular size of a decasaccharide or smaller, the tetra- and pentasaccharides II and III predominating.
6712992	2	50	dep	I	491:491	arg1	III					588:590	III	588:590	III	588:590	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	2	50	dep	I	491:491	arg1	II					521:522	II	521:522	II	521:522	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	2	50	dep	I	491:491	arg1	DGal1----3					958:967	beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3	798:967	beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3	798:967	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	2	50	dep	I	491:491	arg1	beta					560:563	beta DGal1----3	560:574	beta DGal1----3	560:574	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	2	50	dep	I	491:491	arg1	IV					673:674	IV	673:674	IV	673:674	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	2	50	dep	I	491:491	arg1	V					795:795	V	795:795	V	795:795	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	2	50	dep	I	491:491	arg1	beta					541:544	beta DGal1----4 beta DGlcNAc1----6	525:558	beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol	525:585	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	2	50	dep	I	491:491	arg1	DGalNAc-ol					661:670	alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol	593:670	alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol	593:670	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	2	50	dep	I	491:491	arg1	DGal1NAcol					779:788	beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol	677:788	beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol	677:788	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	4	51	theme	new	1258:1260	arg1	decasaccharide					1234:1247	the decasaccharide	1230:1247	the decasaccharide	1230:1247	Oligosaccharides I through IV have been previously isolated from several glycoproteins by other laboratories; the decasaccharide, V, is a new structure.
6712992	4	51	theme	new	1258:1260	arg1	structure					1262:1270	a new structure	1256:1270	a new structure	1256:1270	Oligosaccharides I through IV have been previously isolated from several glycoproteins by other laboratories; the decasaccharide, V, is a new structure.
6712992	3	52	theme	predominating	1105:1117	arg1	size					1025:1028	a molecular size	1013:1028	a molecular size of a decasaccharide or smaller, the tetra- and pentasaccharides II and III predominating	1013:1117	Of the oligosaccharides 60% had a molecular size of a decasaccharide or smaller, the tetra- and pentasaccharides II and III predominating.
6712992	2	53	theme	beta	677:680	arg1	alpha					693:697	alpha LFuc1----4	693:708	alpha LFuc1----4	693:708	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	2	53	theme	beta	677:680	arg1	beta					744:747	beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6	677:761	beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol	677:788	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	2	53	theme	beta	677:680	arg1	beta					763:766	beta DGal1----3	763:777	beta DGal1----3	763:777	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	0	54	gly	glycoprotein	100:111	arg1	glycoprotein					100:111	an I, H and Lea active ovarian cyst glycoprotein	64:111	glycoprotein	100:111	Structures of oligosaccharides cleaved by base-borohydride from an I, H and Lea active ovarian cyst glycoprotein.
6712992	2	55	theme	beta	525:528	arg1	beta					541:544	beta DGal1----4 beta DGlcNAc1----6	525:558	beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol	525:585	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	2	55	theme	beta	525:528	arg1	beta					560:563	beta DGal1----3	560:574	beta DGal1----3	560:574	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	2	56	theme	alpha	901:905	arg1	DGal1----3					958:967	beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3	798:967	beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3	798:967	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	1	57	theme	cyst	200:203	arg1	glycoprotein					205:216	an I, H and Lea active ovarian cyst glycoprotein	169:216	glycoprotein	205:216	Oligosaccharides were cleaved by base-borohydride from an I, H and Lea active ovarian cyst glycoprotein and purified by Bio-Gel P-6 and paper chromatography.
6712992	3	58	dep	tetra-	1066:1071	arg1	the					1062:1064	the	1062:1064	the	1062:1064	Of the oligosaccharides 60% had a molecular size of a decasaccharide or smaller, the tetra- and pentasaccharides II and III predominating.
6712992	4	59	attach	isolated	1171:1178	arg1	glycoproteins					1193:1205	several glycoproteins	1185:1205	several glycoproteins	1185:1205	Oligosaccharides I through IV have been previously isolated from several glycoproteins by other laboratories; the decasaccharide, V, is a new structure.
6712992	4	59	attach	isolated	1171:1178	arg2	Oligosaccharides					1120:1135	Oligosaccharides I through IV	1120:1148	Oligosaccharides I through IV	1120:1148	Oligosaccharides I through IV have been previously isolated from several glycoproteins by other laboratories; the decasaccharide, V, is a new structure.
6712992	2	60	theme	beta	494:497	arg1	I					491:491	oligosaccharide I	475:491	oligosaccharide I	475:491	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	2	60	theme	beta	494:497	arg1	DGal1----3DGalNAc-ol					499:518	beta DGal1----3DGalNAc-ol	494:518	beta DGal1----3DGalNAc-ol	494:518	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	2	61	theme	periodate	364:372	arg1	oxidation					374:382	quantitative periodate oxidation	351:382	quantitative periodate oxidation	351:382	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	2	62	theme	chronic	385:391	arg1	oxidation					398:406	chronic acid oxidation	385:406	chronic acid oxidation	385:406	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	2	63	theme	alpha	814:818	arg1	DGal1----3					958:967	beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3	798:967	beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3	798:967	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	0	64	theme	I	67:67	arg1	glycoprotein					100:111	an I, H and Lea active ovarian cyst glycoprotein	64:111	glycoprotein	100:111	Structures of oligosaccharides cleaved by base-borohydride from an I, H and Lea active ovarian cyst glycoprotein.
6712992	2	65	theme	beta	953:956	arg1	DGal1----3					958:967	beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3	798:967	beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3	798:967	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	2	66	dep	DGalNAc-ol	969:978	arg1	I					491:491	oligosaccharide I	475:491	oligosaccharide I	475:491	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	2	66	dep	DGalNAc-ol	969:978	arg1	DGal1----3DGalNAc-ol					499:518	beta DGal1----3DGalNAc-ol	494:518	beta DGal1----3DGalNAc-ol	494:518	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
6712992	2	67	theme	quantitative	351:362	arg1	oxidation					374:382	quantitative periodate oxidation	351:382	quantitative periodate oxidation	351:382	The structures of five oligosaccharides, determined by compositional analyses, quantitative periodate oxidation, chronic acid oxidation, methylation analyses and enzymatic degradations, were as follows: oligosaccharide I, beta DGal1----3DGalNAc-ol; II, beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; III, alpha LFuc1----2 beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGalNAc-ol; IV, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3beta DGal1----4 beta DGlcNAc1----6(beta DGal1----3)DGal1NAcol; and V, beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----4 beta DGlcNAc1----6[beta DGal1----3(alpha LFuc1----4)beta DGlcNAc1----3 beta DGal1----3 beta DGal1----3]DGalNAc-ol.
3514617	11	0	theme	peptides	1904:1911	arg1	composition					1877:1887	the composition	1873:1887	the composition of the tryptic peptides	1873:1911	The tryptic glycopeptide pattern of the M Sta glycophorin CNBr fragment B was identical to the pattern of the corresponding control fragment, and the composition of the tryptic peptides suggested sequence identity with the control fragment.
3514617	2	1	with	Reactivities	215:226	arg1	antibodies					253:262	specific monoclonal antibodies	233:262	specific monoclonal antibodies	233:262	Reactivities with specific monoclonal antibodies indicated that two major M and N glycophorins were present.
3514617	10	2	attach	present	1610:1616	arg1	ratio					1623:1627	a ratio	1621:1627	a ratio similar to that found in controls	1621:1661	The structures of the O-linked units were inferred experimentally to be NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc and NeuAc(alpha 2,3)Gal(beta 1,3) [NeuAc(alpha 2,6)]GalNAc, present in a ratio similar to that found in controls; and the Asn-linked unit also appeared to be as in the control.
3514617	10	2	attach	present	1610:1616	arg2	structures					1445:1454	The structures	1441:1454	The structures of the O-linked units	1441:1476	The structures of the O-linked units were inferred experimentally to be NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc and NeuAc(alpha 2,3)Gal(beta 1,3) [NeuAc(alpha 2,6)]GalNAc, present in a ratio similar to that found in controls; and the Asn-linked unit also appeared to be as in the control.
3514617	10	2	attach	present	1610:1616	arg2	GalNAc					1543:1548	NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc	1513:1548	NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc	1513:1548	The structures of the O-linked units were inferred experimentally to be NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc and NeuAc(alpha 2,3)Gal(beta 1,3) [NeuAc(alpha 2,6)]GalNAc, present in a ratio similar to that found in controls; and the Asn-linked unit also appeared to be as in the control.
3514617	15	3	theme	methionine	2577:2586	arg1	substitution					2561:2572	a substitution	2559:2572	a substitution of methionine for a residue upstream from residue 40	2559:2625	However, the tryptic glycopeptide pattern of the variant differed from control M or N alpha glycophorins, suggesting a deletion of a large segment of the molecule near residues 40-61 and/or a substitution of methionine for a residue upstream from residue 40.
3514617	7	4	theme	amino-terminal	820:833	arg1	octapeptides					835:846	The amino-terminal octapeptides	816:846	The amino-terminal octapeptides of the M and N species	816:869	The amino-terminal octapeptides of the M and N species were similar in amino acid and carbohydrate composition to those isolated, respectively, from M and N alpha glycophorins.
3514617	7	4	theme	amino-terminal	820:833	arg1	similar					876:882	similar	876:882	similar	876:882	The amino-terminal octapeptides of the M and N species were similar in amino acid and carbohydrate composition to those isolated, respectively, from M and N alpha glycophorins.
3514617	8	5	theme	amino	1086:1090	arg1	residues					1097:1104	amino acid residues 9 to 81	1086:1112	amino acid residues 9 to 81	1086:1112	The studies focused on CNBr glycopeptide B that, in control alpha glycophorins, extends from amino acid residues 9 to 81.
3514617	10	6	theme	similar	1629:1635	arg1	ratio					1623:1627	a ratio	1621:1627	a ratio similar to that found in controls	1621:1661	The structures of the O-linked units were inferred experimentally to be NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc and NeuAc(alpha 2,3)Gal(beta 1,3) [NeuAc(alpha 2,6)]GalNAc, present in a ratio similar to that found in controls; and the Asn-linked unit also appeared to be as in the control.
3514617	12	7	theme	carbohydrate	2156:2167	arg1	absence					2130:2136	the absence	2126:2136	the absence of the Asn-linked carbohydrate	2126:2167	In contrast, the N Sta glycophorin yielded two CNBr glycopeptides B; both contained fewer amino acid residues and virtually lacked Man and GlcNAc, indicating the absence of the Asn-linked carbohydrate.
3514617	2	8	theme	N	295:295	arg1	glycophorins					297:308	two major M and N glycophorins	279:308	two major M and N glycophorins	279:308	Reactivities with specific monoclonal antibodies indicated that two major M and N glycophorins were present.
3514617	5	9	theme	equimolar	611:619	arg1	amounts					621:627	almost equimolar amounts	604:627	almost equimolar amounts	604:627	The two proteins were present in almost equimolar amounts.
3514617	6	10	theme	alpha	753:757	arg1	glycophorin					759:769	the usual M alpha glycophorin	741:769	the usual M alpha glycophorin	741:769	Studies of the CNBr fragments provided evidence that the structure of M Sta glycophorin is the same as that of the usual M alpha glycophorin but that the N Sta glycophorin is a variant.
3514617	2	11	theme	M	289:289	arg1	glycophorins					297:308	two major M and N glycophorins	279:308	two major M and N glycophorins	279:308	Reactivities with specific monoclonal antibodies indicated that two major M and N glycophorins were present.
3514617	15	12	theme	variant	2418:2424	arg1	pattern					2403:2409	the tryptic glycopeptide pattern	2378:2409	the tryptic glycopeptide pattern of the variant	2378:2424	However, the tryptic glycopeptide pattern of the variant differed from control M or N alpha glycophorins, suggesting a deletion of a large segment of the molecule near residues 40-61 and/or a substitution of methionine for a residue upstream from residue 40.
3514617	1	13	theme	blood	178:182	arg1	phenotype					190:198	the M Sta blood group phenotype	168:198	the M Sta blood group phenotype	168:198	Structural and immunochemical studies of glycophorins isolated from erythrocytes of an individual homozygous for the M Sta blood group phenotype are described.
3514617	9	14	from	glycophorins	1234:1245	arg1	terms					1250:1254	terms	1250:1254	terms of size, chromatographic behavior, amino acid and carbohydrate contents and compositions, the presence of O-glycosidically linked saccharides and a single Asn-linked carbohydrate unit	1250:1438	The fragment from the M species exhibited properties identical to those of the corresponding fragment of control alpha glycophorins in terms of size, chromatographic behavior, amino acid and carbohydrate contents and compositions, the presence of O-glycosidically linked saccharides and a single Asn-linked carbohydrate unit.
3514617	10	15	theme	O-linked	1463:1470	arg1	units					1472:1476	the O-linked units	1459:1476	the O-linked units	1459:1476	The structures of the O-linked units were inferred experimentally to be NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc and NeuAc(alpha 2,3)Gal(beta 1,3) [NeuAc(alpha 2,6)]GalNAc, present in a ratio similar to that found in controls; and the Asn-linked unit also appeared to be as in the control.
3514617	11	16	theme	sequence	1923:1930	arg1	identity					1932:1939	sequence identity	1923:1939	sequence identity with the control fragment	1923:1965	The tryptic glycopeptide pattern of the M Sta glycophorin CNBr fragment B was identical to the pattern of the corresponding control fragment, and the composition of the tryptic peptides suggested sequence identity with the control fragment.
3514617	12	17	contain	contained	2042:2050	arg1	both					2037:2040	both	2037:2040	both	2037:2040	In contrast, the N Sta glycophorin yielded two CNBr glycopeptides B; both contained fewer amino acid residues and virtually lacked Man and GlcNAc, indicating the absence of the Asn-linked carbohydrate.
3514617	12	17	contain	contained	2042:2050	arg2	residues					2069:2076	fewer amino acid residues	2052:2076	fewer amino acid residues	2052:2076	In contrast, the N Sta glycophorin yielded two CNBr glycopeptides B; both contained fewer amino acid residues and virtually lacked Man and GlcNAc, indicating the absence of the Asn-linked carbohydrate.
3514617	10	18	theme	2,3	1525:1527	arg1	structures					1445:1454	The structures	1441:1454	The structures of the O-linked units	1441:1476	The structures of the O-linked units were inferred experimentally to be NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc and NeuAc(alpha 2,3)Gal(beta 1,3) [NeuAc(alpha 2,6)]GalNAc, present in a ratio similar to that found in controls; and the Asn-linked unit also appeared to be as in the control.
3514617	10	18	theme	2,3	1525:1527	arg1	GalNAc					1543:1548	NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc	1513:1548	NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc	1513:1548	The structures of the O-linked units were inferred experimentally to be NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc and NeuAc(alpha 2,3)Gal(beta 1,3) [NeuAc(alpha 2,6)]GalNAc, present in a ratio similar to that found in controls; and the Asn-linked unit also appeared to be as in the control.
3514617	6	19	theme	usual	745:749	arg1	glycophorin					759:769	the usual M alpha glycophorin	741:769	the usual M alpha glycophorin	741:769	Studies of the CNBr fragments provided evidence that the structure of M Sta glycophorin is the same as that of the usual M alpha glycophorin but that the N Sta glycophorin is a variant.
3514617	9	20	theme	linked	1379:1384	arg1	saccharides					1386:1396	O-glycosidically linked saccharides	1362:1396	O-glycosidically linked saccharides	1362:1396	The fragment from the M species exhibited properties identical to those of the corresponding fragment of control alpha glycophorins in terms of size, chromatographic behavior, amino acid and carbohydrate contents and compositions, the presence of O-glycosidically linked saccharides and a single Asn-linked carbohydrate unit.
3514617	11	21	theme	fragment	1859:1866	arg1	pattern					1822:1828	the pattern	1818:1828	the pattern of the corresponding control fragment	1818:1866	The tryptic glycopeptide pattern of the M Sta glycophorin CNBr fragment B was identical to the pattern of the corresponding control fragment, and the composition of the tryptic peptides suggested sequence identity with the control fragment.
3514617	5	22	attach	present	593:599	arg1	amounts					621:627	almost equimolar amounts	604:627	almost equimolar amounts	604:627	The two proteins were present in almost equimolar amounts.
3514617	5	22	attach	present	593:599	arg2	present					593:599	present	593:599	present	593:599	The two proteins were present in almost equimolar amounts.
3514617	5	22	attach	present	593:599	arg2	proteins					579:586	The two proteins	571:586	The two proteins	571:586	The two proteins were present in almost equimolar amounts.
3514617	9	23	theme	M	1137:1137	arg1	species					1139:1145	the M species	1133:1145	the M species	1133:1145	The fragment from the M species exhibited properties identical to those of the corresponding fragment of control alpha glycophorins in terms of size, chromatographic behavior, amino acid and carbohydrate contents and compositions, the presence of O-glycosidically linked saccharides and a single Asn-linked carbohydrate unit.
3514617	15	24	theme	glycopeptide	2390:2401	arg1	pattern					2403:2409	the tryptic glycopeptide pattern	2378:2409	the tryptic glycopeptide pattern of the variant	2378:2424	However, the tryptic glycopeptide pattern of the variant differed from control M or N alpha glycophorins, suggesting a deletion of a large segment of the molecule near residues 40-61 and/or a substitution of methionine for a residue upstream from residue 40.
3514617	9	25	from	fragment	1208:1215	arg1	terms					1250:1254	terms	1250:1254	terms of size, chromatographic behavior, amino acid and carbohydrate contents and compositions, the presence of O-glycosidically linked saccharides and a single Asn-linked carbohydrate unit	1250:1438	The fragment from the M species exhibited properties identical to those of the corresponding fragment of control alpha glycophorins in terms of size, chromatographic behavior, amino acid and carbohydrate contents and compositions, the presence of O-glycosidically linked saccharides and a single Asn-linked carbohydrate unit.
3514617	11	26	theme	corresponding	1837:1849	arg1	fragment					1859:1866	the corresponding control fragment	1833:1866	the corresponding control fragment	1833:1866	The tryptic glycopeptide pattern of the M Sta glycophorin CNBr fragment B was identical to the pattern of the corresponding control fragment, and the composition of the tryptic peptides suggested sequence identity with the control fragment.
3514617	11	27	theme	control	1950:1956	arg1	fragment					1958:1965	the control fragment	1946:1965	the control fragment	1946:1965	The tryptic glycopeptide pattern of the M Sta glycophorin CNBr fragment B was identical to the pattern of the corresponding control fragment, and the composition of the tryptic peptides suggested sequence identity with the control fragment.
3514617	10	28	dep	that	1640:1643	arg1	found					1645:1649	found	1645:1649	found in controls	1645:1661	The structures of the O-linked units were inferred experimentally to be NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc and NeuAc(alpha 2,3)Gal(beta 1,3) [NeuAc(alpha 2,6)]GalNAc, present in a ratio similar to that found in controls; and the Asn-linked unit also appeared to be as in the control.
3514617	10	29	theme	beta	1534:1537	arg1	structures					1445:1454	The structures	1441:1454	The structures of the O-linked units	1441:1476	The structures of the O-linked units were inferred experimentally to be NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc and NeuAc(alpha 2,3)Gal(beta 1,3) [NeuAc(alpha 2,6)]GalNAc, present in a ratio similar to that found in controls; and the Asn-linked unit also appeared to be as in the control.
3514617	10	29	theme	beta	1534:1537	arg1	GalNAc					1543:1548	NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc	1513:1548	NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc	1513:1548	The structures of the O-linked units were inferred experimentally to be NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc and NeuAc(alpha 2,3)Gal(beta 1,3) [NeuAc(alpha 2,6)]GalNAc, present in a ratio similar to that found in controls; and the Asn-linked unit also appeared to be as in the control.
3514617	2	30	theme	monoclonal	242:251	arg1	antibodies					253:262	specific monoclonal antibodies	233:262	specific monoclonal antibodies	233:262	Reactivities with specific monoclonal antibodies indicated that two major M and N glycophorins were present.
3514617	9	31	theme	single	1404:1409	arg1	unit					1435:1438	a single Asn-linked carbohydrate unit	1402:1438	a single Asn-linked carbohydrate unit	1402:1438	The fragment from the M species exhibited properties identical to those of the corresponding fragment of control alpha glycophorins in terms of size, chromatographic behavior, amino acid and carbohydrate contents and compositions, the presence of O-glycosidically linked saccharides and a single Asn-linked carbohydrate unit.
3514617	10	32	theme	Gal-	1529:1532	arg1	structures					1445:1454	The structures	1441:1454	The structures of the O-linked units	1441:1476	The structures of the O-linked units were inferred experimentally to be NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc and NeuAc(alpha 2,3)Gal(beta 1,3) [NeuAc(alpha 2,6)]GalNAc, present in a ratio similar to that found in controls; and the Asn-linked unit also appeared to be as in the control.
3514617	10	32	theme	Gal-	1529:1532	arg1	GalNAc					1543:1548	NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc	1513:1548	NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc	1513:1548	The structures of the O-linked units were inferred experimentally to be NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc and NeuAc(alpha 2,3)Gal(beta 1,3) [NeuAc(alpha 2,6)]GalNAc, present in a ratio similar to that found in controls; and the Asn-linked unit also appeared to be as in the control.
3514617	15	33	theme	upstream	2602:2609	arg1	residue					2594:2600	a residue	2592:2600	a residue upstream from residue 40	2592:2625	However, the tryptic glycopeptide pattern of the variant differed from control M or N alpha glycophorins, suggesting a deletion of a large segment of the molecule near residues 40-61 and/or a substitution of methionine for a residue upstream from residue 40.
3514617	9	34	theme	identical	1168:1176	arg1	properties					1157:1166	properties	1157:1166	properties identical to those of the corresponding fragment of control alpha glycophorins in terms of size, chromatographic behavior, amino acid and carbohydrate contents and compositions, the presence of O-glycosidically linked saccharides and a single Asn-linked carbohydrate unit	1157:1438	The fragment from the M species exhibited properties identical to those of the corresponding fragment of control alpha glycophorins in terms of size, chromatographic behavior, amino acid and carbohydrate contents and compositions, the presence of O-glycosidically linked saccharides and a single Asn-linked carbohydrate unit.
3514617	9	35	theme	carbohydrate	1422:1433	arg1	unit					1435:1438	a single Asn-linked carbohydrate unit	1402:1438	a single Asn-linked carbohydrate unit	1402:1438	The fragment from the M species exhibited properties identical to those of the corresponding fragment of control alpha glycophorins in terms of size, chromatographic behavior, amino acid and carbohydrate contents and compositions, the presence of O-glycosidically linked saccharides and a single Asn-linked carbohydrate unit.
3514617	11	36	theme	CNBr	1785:1788	arg1	B					1799:1799	the M Sta glycophorin CNBr fragment B	1763:1799	the M Sta glycophorin CNBr fragment B	1763:1799	The tryptic glycopeptide pattern of the M Sta glycophorin CNBr fragment B was identical to the pattern of the corresponding control fragment, and the composition of the tryptic peptides suggested sequence identity with the control fragment.
3514617	13	37	from	carbohydrates	2205:2217	arg1	protein					2235:2241	the intact N protein	2222:2241	the intact N protein	2222:2241	The much decreased levels of these carbohydrates in the intact N protein, corroborated the latter finding.
3514617	11	38	theme	fragment	1790:1797	arg1	B					1799:1799	the M Sta glycophorin CNBr fragment B	1763:1799	the M Sta glycophorin CNBr fragment B	1763:1799	The tryptic glycopeptide pattern of the M Sta glycophorin CNBr fragment B was identical to the pattern of the corresponding control fragment, and the composition of the tryptic peptides suggested sequence identity with the control fragment.
3514617	1	39	theme	individual	142:151	arg1	erythrocytes					123:134	erythrocytes	123:134	erythrocytes of an individual homozygous for the M Sta blood group phenotype	123:198	Structural and immunochemical studies of glycophorins isolated from erythrocytes of an individual homozygous for the M Sta blood group phenotype are described.
3514617	3	40	theme	N	334:334	arg1	glycophorins					340:351	The M and N Sta glycophorins	324:351	The M and N Sta glycophorins	324:351	The M and N Sta glycophorins were resolved by Lens culinaris lectin affinity chromatography.
3514617	7	41	from	acid	893:896	arg1	similar					876:882	similar	876:882	similar	876:882	The amino-terminal octapeptides of the M and N species were similar in amino acid and carbohydrate composition to those isolated, respectively, from M and N alpha glycophorins.
3514617	7	41	from	acid	893:896	arg1	octapeptides					835:846	The amino-terminal octapeptides	816:846	The amino-terminal octapeptides of the M and N species	816:869	The amino-terminal octapeptides of the M and N species were similar in amino acid and carbohydrate composition to those isolated, respectively, from M and N alpha glycophorins.
3514617	11	42	theme	glycophorin	1773:1783	arg1	B					1799:1799	the M Sta glycophorin CNBr fragment B	1763:1799	the M Sta glycophorin CNBr fragment B	1763:1799	The tryptic glycopeptide pattern of the M Sta glycophorin CNBr fragment B was identical to the pattern of the corresponding control fragment, and the composition of the tryptic peptides suggested sequence identity with the control fragment.
3514617	10	43	from	present	1610:1616	arg1	ratio					1623:1627	a ratio	1621:1627	a ratio similar to that found in controls	1621:1661	The structures of the O-linked units were inferred experimentally to be NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc and NeuAc(alpha 2,3)Gal(beta 1,3) [NeuAc(alpha 2,6)]GalNAc, present in a ratio similar to that found in controls; and the Asn-linked unit also appeared to be as in the control.
3514617	3	44	theme	M	328:328	arg1	glycophorins					340:351	The M and N Sta glycophorins	324:351	The M and N Sta glycophorins	324:351	The M and N Sta glycophorins were resolved by Lens culinaris lectin affinity chromatography.
3514617	12	45	theme	acid	2064:2067	arg1	residues					2069:2076	fewer amino acid residues	2052:2076	fewer amino acid residues	2052:2076	In contrast, the N Sta glycophorin yielded two CNBr glycopeptides B; both contained fewer amino acid residues and virtually lacked Man and GlcNAc, indicating the absence of the Asn-linked carbohydrate.
3514617	8	46	dep	residues	1097:1104	arg1	81					1111:1112	81	1111:1112	81	1111:1112	The studies focused on CNBr glycopeptide B that, in control alpha glycophorins, extends from amino acid residues 9 to 81.
3514617	7	47	theme	carbohydrate	902:913	arg1	composition					915:925	amino acid and carbohydrate composition	887:925	composition	915:925	The amino-terminal octapeptides of the M and N species were similar in amino acid and carbohydrate composition to those isolated, respectively, from M and N alpha glycophorins.
3514617	1	48	theme	M	172:172	arg1	phenotype					190:198	the M Sta blood group phenotype	168:198	the M Sta blood group phenotype	168:198	Structural and immunochemical studies of glycophorins isolated from erythrocytes of an individual homozygous for the M Sta blood group phenotype are described.
3514617	4	49	theme	alpha	490:494	arg1	glycophorins					496:507	control alpha glycophorins	482:507	control alpha glycophorins	482:507	The N species was not held on the lectin but the M species, like control alpha glycophorins, was retained and could be eluted with alpha-methylmannoside.
3514617	12	50	theme	glycopeptides	2020:2032	arg1	B					2034:2034	two CNBr glycopeptides B	2011:2034	two CNBr glycopeptides B	2011:2034	In contrast, the N Sta glycophorin yielded two CNBr glycopeptides B; both contained fewer amino acid residues and virtually lacked Man and GlcNAc, indicating the absence of the Asn-linked carbohydrate.
3514617	15	51	theme	alpha	2455:2459	arg1	glycophorins					2461:2472	N alpha glycophorins	2453:2472	N alpha glycophorins	2453:2472	However, the tryptic glycopeptide pattern of the variant differed from control M or N alpha glycophorins, suggesting a deletion of a large segment of the molecule near residues 40-61 and/or a substitution of methionine for a residue upstream from residue 40.
3514617	9	52	theme	control	1220:1226	arg1	glycophorins					1234:1245	control alpha glycophorins	1220:1245	control alpha glycophorins in terms of size, chromatographic behavior, amino acid and carbohydrate contents and compositions, the presence of O-glycosidically linked saccharides and a single Asn-linked carbohydrate unit	1220:1438	The fragment from the M species exhibited properties identical to those of the corresponding fragment of control alpha glycophorins in terms of size, chromatographic behavior, amino acid and carbohydrate contents and compositions, the presence of O-glycosidically linked saccharides and a single Asn-linked carbohydrate unit.
3514617	14	53	theme	control	2341:2347	arg1	glycophorins					2355:2366	control alpha glycophorins	2341:2366	control alpha glycophorins	2341:2366	The O-glycosidic saccharides appeared similar to those found in control alpha glycophorins.
3514617	11	54	theme	glycopeptide	1739:1750	arg1	identical					1805:1813	identical	1805:1813	identical	1805:1813	The tryptic glycopeptide pattern of the M Sta glycophorin CNBr fragment B was identical to the pattern of the corresponding control fragment, and the composition of the tryptic peptides suggested sequence identity with the control fragment.
3514617	11	54	theme	glycopeptide	1739:1750	arg1	pattern					1752:1758	The tryptic glycopeptide pattern	1727:1758	The tryptic glycopeptide pattern of the M Sta glycophorin CNBr fragment B	1727:1799	The tryptic glycopeptide pattern of the M Sta glycophorin CNBr fragment B was identical to the pattern of the corresponding control fragment, and the composition of the tryptic peptides suggested sequence identity with the control fragment.
3514617	9	55	theme	glycophorins	1234:1245	arg1	fragment					1208:1215	the corresponding fragment	1190:1215	the corresponding fragment of control alpha glycophorins in terms of size, chromatographic behavior, amino acid and carbohydrate contents and compositions, the presence of O-glycosidically linked saccharides and a single Asn-linked carbohydrate unit	1190:1438	The fragment from the M species exhibited properties identical to those of the corresponding fragment of control alpha glycophorins in terms of size, chromatographic behavior, amino acid and carbohydrate contents and compositions, the presence of O-glycosidically linked saccharides and a single Asn-linked carbohydrate unit.
3514617	9	56	link	linked	1379:1384	arg1	saccharides					1386:1396	O-glycosidically linked saccharides	1362:1396	O-glycosidically linked saccharides	1362:1396	The fragment from the M species exhibited properties identical to those of the corresponding fragment of control alpha glycophorins in terms of size, chromatographic behavior, amino acid and carbohydrate contents and compositions, the presence of O-glycosidically linked saccharides and a single Asn-linked carbohydrate unit.
3514617	13	57	theme	N	2233:2233	arg1	protein					2235:2241	the intact N protein	2222:2241	the intact N protein	2222:2241	The much decreased levels of these carbohydrates in the intact N protein, corroborated the latter finding.
3514617	3	58	theme	lectin	385:390	arg1	chromatography					401:414	Lens culinaris lectin affinity chromatography	370:414	Lens culinaris lectin affinity chromatography	370:414	The M and N Sta glycophorins were resolved by Lens culinaris lectin affinity chromatography.
3514617	12	59	theme	fewer	2052:2056	arg1	residues					2069:2076	fewer amino acid residues	2052:2076	fewer amino acid residues	2052:2076	In contrast, the N Sta glycophorin yielded two CNBr glycopeptides B; both contained fewer amino acid residues and virtually lacked Man and GlcNAc, indicating the absence of the Asn-linked carbohydrate.
3514617	7	60	dep	M	965:965	arg1	glycophorins					979:990	alpha glycophorins	973:990	alpha glycophorins	973:990	The amino-terminal octapeptides of the M and N species were similar in amino acid and carbohydrate composition to those isolated, respectively, from M and N alpha glycophorins.
3514617	0	61	theme	Membrane	0:7	arg1	glycophorins					9:20	Membrane glycophorins	0:20	Membrane glycophorins in Sta blood group erythrocytes.	0:53	Membrane glycophorins in Sta blood group erythrocytes.
3514617	5	62	from	amounts	621:627	arg1	present					593:599	present	593:599	present	593:599	The two proteins were present in almost equimolar amounts.
3514617	5	62	from	amounts	621:627	arg1	proteins					579:586	The two proteins	571:586	The two proteins	571:586	The two proteins were present in almost equimolar amounts.
3514617	1	63	theme	glycophorins	96:107	arg1	studies					85:91	Structural and immunochemical studies	55:91	Structural and immunochemical studies of glycophorins isolated from erythrocytes of an individual homozygous for the M Sta blood group phenotype	55:198	Structural and immunochemical studies of glycophorins isolated from erythrocytes of an individual homozygous for the M Sta blood group phenotype are described.
3514617	3	64	theme	Lens	370:373	arg1	chromatography					401:414	Lens culinaris lectin affinity chromatography	370:414	Lens culinaris lectin affinity chromatography	370:414	The M and N Sta glycophorins were resolved by Lens culinaris lectin affinity chromatography.
3514617	11	65	theme	tryptic	1731:1737	arg1	identical					1805:1813	identical	1805:1813	identical	1805:1813	The tryptic glycopeptide pattern of the M Sta glycophorin CNBr fragment B was identical to the pattern of the corresponding control fragment, and the composition of the tryptic peptides suggested sequence identity with the control fragment.
3514617	11	65	theme	tryptic	1731:1737	arg1	pattern					1752:1758	The tryptic glycopeptide pattern	1727:1758	The tryptic glycopeptide pattern of the M Sta glycophorin CNBr fragment B	1727:1799	The tryptic glycopeptide pattern of the M Sta glycophorin CNBr fragment B was identical to the pattern of the corresponding control fragment, and the composition of the tryptic peptides suggested sequence identity with the control fragment.
3514617	5	66	located	present	593:599	arg1	amounts					621:627	almost equimolar amounts	604:627	almost equimolar amounts	604:627	The two proteins were present in almost equimolar amounts.
3514617	5	66	located	present	593:599	arg2	present					593:599	present	593:599	present	593:599	The two proteins were present in almost equimolar amounts.
3514617	5	66	located	present	593:599	arg2	proteins					579:586	The two proteins	571:586	The two proteins	571:586	The two proteins were present in almost equimolar amounts.
3514617	9	67	theme	size	1259:1262	arg1	terms					1250:1254	terms	1250:1254	terms of size, chromatographic behavior, amino acid and carbohydrate contents and compositions, the presence of O-glycosidically linked saccharides and a single Asn-linked carbohydrate unit	1250:1438	The fragment from the M species exhibited properties identical to those of the corresponding fragment of control alpha glycophorins in terms of size, chromatographic behavior, amino acid and carbohydrate contents and compositions, the presence of O-glycosidically linked saccharides and a single Asn-linked carbohydrate unit.
3514617	13	68	theme	carbohydrates	2205:2217	arg1	levels					2189:2194	The much decreased levels	2170:2194	The much decreased levels	2170:2194	The much decreased levels of these carbohydrates in the intact N protein, corroborated the latter finding.
3514617	1	69	theme	homozygous	153:162	arg1	individual					142:151	an individual	139:151	an individual homozygous for the M Sta blood group phenotype	139:198	Structural and immunochemical studies of glycophorins isolated from erythrocytes of an individual homozygous for the M Sta blood group phenotype are described.
3514617	10	70	theme	Asn-linked	1672:1681	arg1	unit					1683:1686	the Asn-linked unit	1668:1686	the Asn-linked unit	1668:1686	The structures of the O-linked units were inferred experimentally to be NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc and NeuAc(alpha 2,3)Gal(beta 1,3) [NeuAc(alpha 2,6)]GalNAc, present in a ratio similar to that found in controls; and the Asn-linked unit also appeared to be as in the control.
3514617	6	71	theme	fragments	650:658	arg1	Studies					630:636	Studies	630:636	Studies of the CNBr fragments	630:658	Studies of the CNBr fragments provided evidence that the structure of M Sta glycophorin is the same as that of the usual M alpha glycophorin but that the N Sta glycophorin is a variant.
3514617	10	72	theme	alpha	1560:1564	arg1	[NeuAc					1584:1589	alpha 2,3)Gal(beta 1,3) [NeuAc	1560:1589	alpha 2,3)Gal(beta 1,3) [NeuAc(alpha 2,6)	1560:1600	The structures of the O-linked units were inferred experimentally to be NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc and NeuAc(alpha 2,3)Gal(beta 1,3) [NeuAc(alpha 2,6)]GalNAc, present in a ratio similar to that found in controls; and the Asn-linked unit also appeared to be as in the control.
3514617	10	72	theme	alpha	1560:1564	arg1	2,6					1597:1599	alpha 2,6	1591:1599	alpha 2,6	1591:1599	The structures of the O-linked units were inferred experimentally to be NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc and NeuAc(alpha 2,3)Gal(beta 1,3) [NeuAc(alpha 2,6)]GalNAc, present in a ratio similar to that found in controls; and the Asn-linked unit also appeared to be as in the control.
3514617	9	73	theme	presence	1350:1357	arg1	terms					1250:1254	terms	1250:1254	terms of size, chromatographic behavior, amino acid and carbohydrate contents and compositions, the presence of O-glycosidically linked saccharides and a single Asn-linked carbohydrate unit	1250:1438	The fragment from the M species exhibited properties identical to those of the corresponding fragment of control alpha glycophorins in terms of size, chromatographic behavior, amino acid and carbohydrate contents and compositions, the presence of O-glycosidically linked saccharides and a single Asn-linked carbohydrate unit.
3514617	9	74	theme	chromatographic	1265:1279	arg1	behavior					1281:1288	chromatographic behavior	1265:1288	chromatographic behavior	1265:1288	The fragment from the M species exhibited properties identical to those of the corresponding fragment of control alpha glycophorins in terms of size, chromatographic behavior, amino acid and carbohydrate contents and compositions, the presence of O-glycosidically linked saccharides and a single Asn-linked carbohydrate unit.
3514617	0	75	theme	blood	29:33	arg1	erythrocytes					41:52	Sta blood group erythrocytes	25:52	Sta blood group erythrocytes	25:52	Membrane glycophorins in Sta blood group erythrocytes.
3514617	9	76	from	species	1139:1145	arg1	fragment					1119:1126	The fragment	1115:1126	The fragment from the M species	1115:1145	The fragment from the M species exhibited properties identical to those of the corresponding fragment of control alpha glycophorins in terms of size, chromatographic behavior, amino acid and carbohydrate contents and compositions, the presence of O-glycosidically linked saccharides and a single Asn-linked carbohydrate unit.
3514617	3	77	theme	Sta	336:338	arg1	glycophorins					340:351	The M and N Sta glycophorins	324:351	The M and N Sta glycophorins	324:351	The M and N Sta glycophorins were resolved by Lens culinaris lectin affinity chromatography.
3514617	12	78	theme	N	1985:1985	arg1	glycophorin					1991:2001	the N Sta glycophorin	1981:2001	the N Sta glycophorin	1981:2001	In contrast, the N Sta glycophorin yielded two CNBr glycopeptides B; both contained fewer amino acid residues and virtually lacked Man and GlcNAc, indicating the absence of the Asn-linked carbohydrate.
3514617	10	79	link	O-linked	1463:1470	arg1	units					1472:1476	the O-linked units	1459:1476	the O-linked units	1459:1476	The structures of the O-linked units were inferred experimentally to be NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc and NeuAc(alpha 2,3)Gal(beta 1,3) [NeuAc(alpha 2,6)]GalNAc, present in a ratio similar to that found in controls; and the Asn-linked unit also appeared to be as in the control.
3514617	10	80	theme	1,3	1579:1581	arg1	[NeuAc					1584:1589	alpha 2,3)Gal(beta 1,3) [NeuAc	1560:1589	alpha 2,3)Gal(beta 1,3) [NeuAc(alpha 2,6)	1560:1600	The structures of the O-linked units were inferred experimentally to be NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc and NeuAc(alpha 2,3)Gal(beta 1,3) [NeuAc(alpha 2,6)]GalNAc, present in a ratio similar to that found in controls; and the Asn-linked unit also appeared to be as in the control.
3514617	10	80	theme	1,3	1579:1581	arg1	2,6					1597:1599	alpha 2,6	1591:1599	alpha 2,6	1591:1599	The structures of the O-linked units were inferred experimentally to be NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc and NeuAc(alpha 2,3)Gal(beta 1,3) [NeuAc(alpha 2,6)]GalNAc, present in a ratio similar to that found in controls; and the Asn-linked unit also appeared to be as in the control.
3514617	8	81	theme	glycopeptide	1021:1032	arg1	B					1034:1034	CNBr glycopeptide B	1016:1034	CNBr glycopeptide B that, in control alpha glycophorins, extends from amino acid residues 9 to 81	1016:1112	The studies focused on CNBr glycopeptide B that, in control alpha glycophorins, extends from amino acid residues 9 to 81.
3514617	11	82	gly	glycopeptide	1739:1750	arg2	glycopeptide					1739:1750	The tryptic glycopeptide pattern	1727:1758	The tryptic glycopeptide pattern of the M Sta glycophorin CNBr fragment B	1727:1799	The tryptic glycopeptide pattern of the M Sta glycophorin CNBr fragment B was identical to the pattern of the corresponding control fragment, and the composition of the tryptic peptides suggested sequence identity with the control fragment.
3514617	13	83	theme	decreased	2179:2187	arg1	levels					2189:2194	The much decreased levels	2170:2194	The much decreased levels	2170:2194	The much decreased levels of these carbohydrates in the intact N protein, corroborated the latter finding.
3514617	11	84	with	identity	1932:1939	arg1	fragment					1958:1965	the control fragment	1946:1965	the control fragment	1946:1965	The tryptic glycopeptide pattern of the M Sta glycophorin CNBr fragment B was identical to the pattern of the corresponding control fragment, and the composition of the tryptic peptides suggested sequence identity with the control fragment.
3514617	10	85	dep	GalNAc	1543:1548	arg1	GalNAc					1602:1607	GalNAc	1602:1607	GalNAc	1602:1607	The structures of the O-linked units were inferred experimentally to be NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc and NeuAc(alpha 2,3)Gal(beta 1,3) [NeuAc(alpha 2,6)]GalNAc, present in a ratio similar to that found in controls; and the Asn-linked unit also appeared to be as in the control.
3514617	7	86	theme	species	863:869	arg1	octapeptides					835:846	The amino-terminal octapeptides	816:846	The amino-terminal octapeptides of the M and N species	816:869	The amino-terminal octapeptides of the M and N species were similar in amino acid and carbohydrate composition to those isolated, respectively, from M and N alpha glycophorins.
3514617	7	86	theme	species	863:869	arg1	similar					876:882	similar	876:882	similar	876:882	The amino-terminal octapeptides of the M and N species were similar in amino acid and carbohydrate composition to those isolated, respectively, from M and N alpha glycophorins.
3514617	9	87	theme	acid	1297:1300	arg1	terms					1250:1254	terms	1250:1254	terms of size, chromatographic behavior, amino acid and carbohydrate contents and compositions, the presence of O-glycosidically linked saccharides and a single Asn-linked carbohydrate unit	1250:1438	The fragment from the M species exhibited properties identical to those of the corresponding fragment of control alpha glycophorins in terms of size, chromatographic behavior, amino acid and carbohydrate contents and compositions, the presence of O-glycosidically linked saccharides and a single Asn-linked carbohydrate unit.
3514617	6	88	theme	Sta	786:788	arg1	glycophorin					790:800	the N Sta glycophorin	780:800	the N Sta glycophorin	780:800	Studies of the CNBr fragments provided evidence that the structure of M Sta glycophorin is the same as that of the usual M alpha glycophorin but that the N Sta glycophorin is a variant.
3514617	6	88	theme	Sta	786:788	arg1	variant					807:813	a variant	805:813	a variant	805:813	Studies of the CNBr fragments provided evidence that the structure of M Sta glycophorin is the same as that of the usual M alpha glycophorin but that the N Sta glycophorin is a variant.
3514617	10	89	dep	NeuAc	1554:1558	arg1	[NeuAc					1584:1589	alpha 2,3)Gal(beta 1,3) [NeuAc	1560:1589	alpha 2,3)Gal(beta 1,3) [NeuAc(alpha 2,6)	1560:1600	The structures of the O-linked units were inferred experimentally to be NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc and NeuAc(alpha 2,3)Gal(beta 1,3) [NeuAc(alpha 2,6)]GalNAc, present in a ratio similar to that found in controls; and the Asn-linked unit also appeared to be as in the control.
3514617	10	89	dep	NeuAc	1554:1558	arg1	2,6					1597:1599	alpha 2,6	1591:1599	alpha 2,6	1591:1599	The structures of the O-linked units were inferred experimentally to be NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc and NeuAc(alpha 2,3)Gal(beta 1,3) [NeuAc(alpha 2,6)]GalNAc, present in a ratio similar to that found in controls; and the Asn-linked unit also appeared to be as in the control.
3514617	10	90	theme	alpha	1591:1595	arg1	[NeuAc					1584:1589	alpha 2,3)Gal(beta 1,3) [NeuAc	1560:1589	alpha 2,3)Gal(beta 1,3) [NeuAc(alpha 2,6)	1560:1600	The structures of the O-linked units were inferred experimentally to be NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc and NeuAc(alpha 2,3)Gal(beta 1,3) [NeuAc(alpha 2,6)]GalNAc, present in a ratio similar to that found in controls; and the Asn-linked unit also appeared to be as in the control.
3514617	10	90	theme	alpha	1591:1595	arg1	2,6					1597:1599	alpha 2,6	1591:1599	alpha 2,6	1591:1599	The structures of the O-linked units were inferred experimentally to be NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc and NeuAc(alpha 2,3)Gal(beta 1,3) [NeuAc(alpha 2,6)]GalNAc, present in a ratio similar to that found in controls; and the Asn-linked unit also appeared to be as in the control.
3514617	9	91	theme	carbohydrate	1306:1317	arg1	contents					1319:1326	amino acid and carbohydrate contents	1291:1326	contents	1319:1326	The fragment from the M species exhibited properties identical to those of the corresponding fragment of control alpha glycophorins in terms of size, chromatographic behavior, amino acid and carbohydrate contents and compositions, the presence of O-glycosidically linked saccharides and a single Asn-linked carbohydrate unit.
3514617	8	92	theme	alpha	1053:1057	arg1	glycophorins					1059:1070	control alpha glycophorins	1045:1070	control alpha glycophorins	1045:1070	The studies focused on CNBr glycopeptide B that, in control alpha glycophorins, extends from amino acid residues 9 to 81.
3514617	10	93	theme	units	1472:1476	arg1	structures					1445:1454	The structures	1441:1454	The structures of the O-linked units	1441:1476	The structures of the O-linked units were inferred experimentally to be NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc and NeuAc(alpha 2,3)Gal(beta 1,3) [NeuAc(alpha 2,6)]GalNAc, present in a ratio similar to that found in controls; and the Asn-linked unit also appeared to be as in the control.
3514617	10	93	theme	units	1472:1476	arg1	GalNAc					1543:1548	NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc	1513:1548	NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc	1513:1548	The structures of the O-linked units were inferred experimentally to be NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc and NeuAc(alpha 2,3)Gal(beta 1,3) [NeuAc(alpha 2,6)]GalNAc, present in a ratio similar to that found in controls; and the Asn-linked unit also appeared to be as in the control.
3514617	6	94	theme	Sta	702:704	arg1	glycophorin					706:716	M Sta glycophorin	700:716	M Sta glycophorin	700:716	Studies of the CNBr fragments provided evidence that the structure of M Sta glycophorin is the same as that of the usual M alpha glycophorin but that the N Sta glycophorin is a variant.
3514617	15	95	from	residue	2616:2622	arg1	upstream					2602:2609	upstream	2602:2609	upstream	2602:2609	However, the tryptic glycopeptide pattern of the variant differed from control M or N alpha glycophorins, suggesting a deletion of a large segment of the molecule near residues 40-61 and/or a substitution of methionine for a residue upstream from residue 40.
3514617	10	96	theme	NeuAc	1513:1517	arg1	structures					1445:1454	The structures	1441:1454	The structures of the O-linked units	1441:1476	The structures of the O-linked units were inferred experimentally to be NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc and NeuAc(alpha 2,3)Gal(beta 1,3) [NeuAc(alpha 2,6)]GalNAc, present in a ratio similar to that found in controls; and the Asn-linked unit also appeared to be as in the control.
3514617	10	96	theme	NeuAc	1513:1517	arg1	GalNAc					1543:1548	NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc	1513:1548	NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc	1513:1548	The structures of the O-linked units were inferred experimentally to be NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc and NeuAc(alpha 2,3)Gal(beta 1,3) [NeuAc(alpha 2,6)]GalNAc, present in a ratio similar to that found in controls; and the Asn-linked unit also appeared to be as in the control.
3514617	11	97	theme	tryptic	1896:1902	arg1	peptides					1904:1911	the tryptic peptides	1892:1911	the tryptic peptides	1892:1911	The tryptic glycopeptide pattern of the M Sta glycophorin CNBr fragment B was identical to the pattern of the corresponding control fragment, and the composition of the tryptic peptides suggested sequence identity with the control fragment.
3514617	4	98	theme	N	421:421	arg1	species					423:429	The N species	417:429	The N species	417:429	The N species was not held on the lectin but the M species, like control alpha glycophorins, was retained and could be eluted with alpha-methylmannoside.
3514617	12	99	theme	Asn-linked	2145:2154	arg1	carbohydrate					2156:2167	the Asn-linked carbohydrate	2141:2167	the Asn-linked carbohydrate	2141:2167	In contrast, the N Sta glycophorin yielded two CNBr glycopeptides B; both contained fewer amino acid residues and virtually lacked Man and GlcNAc, indicating the absence of the Asn-linked carbohydrate.
3514617	11	100	theme	B	1799:1799	arg1	identical					1805:1813	identical	1805:1813	identical	1805:1813	The tryptic glycopeptide pattern of the M Sta glycophorin CNBr fragment B was identical to the pattern of the corresponding control fragment, and the composition of the tryptic peptides suggested sequence identity with the control fragment.
3514617	11	100	theme	B	1799:1799	arg1	pattern					1752:1758	The tryptic glycopeptide pattern	1727:1758	The tryptic glycopeptide pattern of the M Sta glycophorin CNBr fragment B	1727:1799	The tryptic glycopeptide pattern of the M Sta glycophorin CNBr fragment B was identical to the pattern of the corresponding control fragment, and the composition of the tryptic peptides suggested sequence identity with the control fragment.
3514617	15	101	theme	control	2440:2446	arg1	M					2448:2448	control M	2440:2448	control M	2440:2448	However, the tryptic glycopeptide pattern of the variant differed from control M or N alpha glycophorins, suggesting a deletion of a large segment of the molecule near residues 40-61 and/or a substitution of methionine for a residue upstream from residue 40.
3514617	1	102	theme	Sta	174:176	arg1	phenotype					190:198	the M Sta blood group phenotype	168:198	the M Sta blood group phenotype	168:198	Structural and immunochemical studies of glycophorins isolated from erythrocytes of an individual homozygous for the M Sta blood group phenotype are described.
3514617	8	103	theme	acid	1092:1095	arg1	residues					1097:1104	amino acid residues 9 to 81	1086:1112	amino acid residues 9 to 81	1086:1112	The studies focused on CNBr glycopeptide B that, in control alpha glycophorins, extends from amino acid residues 9 to 81.
3514617	6	104	theme	M	751:751	arg1	glycophorin					759:769	the usual M alpha glycophorin	741:769	the usual M alpha glycophorin	741:769	Studies of the CNBr fragments provided evidence that the structure of M Sta glycophorin is the same as that of the usual M alpha glycophorin but that the N Sta glycophorin is a variant.
3514617	1	105	theme	group	184:188	arg1	phenotype					190:198	the M Sta blood group phenotype	168:198	the M Sta blood group phenotype	168:198	Structural and immunochemical studies of glycophorins isolated from erythrocytes of an individual homozygous for the M Sta blood group phenotype are described.
3514617	12	106	link	Asn-linked	2145:2154	arg1	carbohydrate					2156:2167	the Asn-linked carbohydrate	2141:2167	the Asn-linked carbohydrate	2141:2167	In contrast, the N Sta glycophorin yielded two CNBr glycopeptides B; both contained fewer amino acid residues and virtually lacked Man and GlcNAc, indicating the absence of the Asn-linked carbohydrate.
3514617	10	107	theme	alpha	1519:1523	arg1	structures					1445:1454	The structures	1441:1454	The structures of the O-linked units	1441:1476	The structures of the O-linked units were inferred experimentally to be NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc and NeuAc(alpha 2,3)Gal(beta 1,3) [NeuAc(alpha 2,6)]GalNAc, present in a ratio similar to that found in controls; and the Asn-linked unit also appeared to be as in the control.
3514617	10	107	theme	alpha	1519:1523	arg1	GalNAc					1543:1548	NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc	1513:1548	NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc	1513:1548	The structures of the O-linked units were inferred experimentally to be NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc and NeuAc(alpha 2,3)Gal(beta 1,3) [NeuAc(alpha 2,6)]GalNAc, present in a ratio similar to that found in controls; and the Asn-linked unit also appeared to be as in the control.
3514617	15	108	theme	molecule	2523:2530	arg1	segment					2508:2514	a large segment	2500:2514	a large segment of the molecule near residues 40-61	2500:2550	However, the tryptic glycopeptide pattern of the variant differed from control M or N alpha glycophorins, suggesting a deletion of a large segment of the molecule near residues 40-61 and/or a substitution of methionine for a residue upstream from residue 40.
3514617	13	109	theme	latter	2261:2266	arg1	finding					2268:2274	the latter finding	2257:2274	the latter finding	2257:2274	The much decreased levels of these carbohydrates in the intact N protein, corroborated the latter finding.
3514617	10	110	theme	present	1610:1616	arg1	structures					1445:1454	The structures	1441:1454	The structures of the O-linked units	1441:1476	The structures of the O-linked units were inferred experimentally to be NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc and NeuAc(alpha 2,3)Gal(beta 1,3) [NeuAc(alpha 2,6)]GalNAc, present in a ratio similar to that found in controls; and the Asn-linked unit also appeared to be as in the control.
3514617	10	110	theme	present	1610:1616	arg1	GalNAc					1543:1548	NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc	1513:1548	NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc	1513:1548	The structures of the O-linked units were inferred experimentally to be NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc and NeuAc(alpha 2,3)Gal(beta 1,3) [NeuAc(alpha 2,6)]GalNAc, present in a ratio similar to that found in controls; and the Asn-linked unit also appeared to be as in the control.
3514617	9	111	theme	saccharides	1386:1396	arg1	presence					1350:1357	the presence	1346:1357	the presence of O-glycosidically linked saccharides	1346:1396	The fragment from the M species exhibited properties identical to those of the corresponding fragment of control alpha glycophorins in terms of size, chromatographic behavior, amino acid and carbohydrate contents and compositions, the presence of O-glycosidically linked saccharides and a single Asn-linked carbohydrate unit.
3514617	9	111	theme	saccharides	1386:1396	arg1	contents					1319:1326	amino acid and carbohydrate contents	1291:1326	contents	1319:1326	The fragment from the M species exhibited properties identical to those of the corresponding fragment of control alpha glycophorins in terms of size, chromatographic behavior, amino acid and carbohydrate contents and compositions, the presence of O-glycosidically linked saccharides and a single Asn-linked carbohydrate unit.
3514617	9	111	theme	saccharides	1386:1396	arg1	behavior					1281:1288	chromatographic behavior	1265:1288	chromatographic behavior	1265:1288	The fragment from the M species exhibited properties identical to those of the corresponding fragment of control alpha glycophorins in terms of size, chromatographic behavior, amino acid and carbohydrate contents and compositions, the presence of O-glycosidically linked saccharides and a single Asn-linked carbohydrate unit.
3514617	9	111	theme	saccharides	1386:1396	arg1	unit					1435:1438	a single Asn-linked carbohydrate unit	1402:1438	a single Asn-linked carbohydrate unit	1402:1438	The fragment from the M species exhibited properties identical to those of the corresponding fragment of control alpha glycophorins in terms of size, chromatographic behavior, amino acid and carbohydrate contents and compositions, the presence of O-glycosidically linked saccharides and a single Asn-linked carbohydrate unit.
3514617	9	111	theme	saccharides	1386:1396	arg1	compositions					1332:1343	compositions	1332:1343	compositions	1332:1343	The fragment from the M species exhibited properties identical to those of the corresponding fragment of control alpha glycophorins in terms of size, chromatographic behavior, amino acid and carbohydrate contents and compositions, the presence of O-glycosidically linked saccharides and a single Asn-linked carbohydrate unit.
3514617	9	111	theme	saccharides	1386:1396	arg1	size					1259:1262	size	1259:1262	size	1259:1262	The fragment from the M species exhibited properties identical to those of the corresponding fragment of control alpha glycophorins in terms of size, chromatographic behavior, amino acid and carbohydrate contents and compositions, the presence of O-glycosidically linked saccharides and a single Asn-linked carbohydrate unit.
3514617	9	111	theme	saccharides	1386:1396	arg1	acid					1297:1300	amino acid and carbohydrate contents	1291:1326	acid	1297:1300	The fragment from the M species exhibited properties identical to those of the corresponding fragment of control alpha glycophorins in terms of size, chromatographic behavior, amino acid and carbohydrate contents and compositions, the presence of O-glycosidically linked saccharides and a single Asn-linked carbohydrate unit.
3514617	10	112	theme	1,3	1539:1541	arg1	structures					1445:1454	The structures	1441:1454	The structures of the O-linked units	1441:1476	The structures of the O-linked units were inferred experimentally to be NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc and NeuAc(alpha 2,3)Gal(beta 1,3) [NeuAc(alpha 2,6)]GalNAc, present in a ratio similar to that found in controls; and the Asn-linked unit also appeared to be as in the control.
3514617	10	112	theme	1,3	1539:1541	arg1	GalNAc					1543:1548	NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc	1513:1548	NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc	1513:1548	The structures of the O-linked units were inferred experimentally to be NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc and NeuAc(alpha 2,3)Gal(beta 1,3) [NeuAc(alpha 2,6)]GalNAc, present in a ratio similar to that found in controls; and the Asn-linked unit also appeared to be as in the control.
3514617	11	113	theme	control	1851:1857	arg1	fragment					1859:1866	the corresponding control fragment	1833:1866	the corresponding control fragment	1833:1866	The tryptic glycopeptide pattern of the M Sta glycophorin CNBr fragment B was identical to the pattern of the corresponding control fragment, and the composition of the tryptic peptides suggested sequence identity with the control fragment.
3514617	7	114	theme	alpha	973:977	arg1	glycophorins					979:990	alpha glycophorins	973:990	alpha glycophorins	973:990	The amino-terminal octapeptides of the M and N species were similar in amino acid and carbohydrate composition to those isolated, respectively, from M and N alpha glycophorins.
3514617	2	115	theme	specific	233:240	arg1	antibodies					253:262	specific monoclonal antibodies	233:262	specific monoclonal antibodies	233:262	Reactivities with specific monoclonal antibodies indicated that two major M and N glycophorins were present.
3514617	8	116	theme	control	1045:1051	arg1	glycophorins					1059:1070	control alpha glycophorins	1045:1070	control alpha glycophorins	1045:1070	The studies focused on CNBr glycopeptide B that, in control alpha glycophorins, extends from amino acid residues 9 to 81.
3514617	9	117	theme	Asn-linked	1411:1420	arg1	unit					1435:1438	a single Asn-linked carbohydrate unit	1402:1438	a single Asn-linked carbohydrate unit	1402:1438	The fragment from the M species exhibited properties identical to those of the corresponding fragment of control alpha glycophorins in terms of size, chromatographic behavior, amino acid and carbohydrate contents and compositions, the presence of O-glycosidically linked saccharides and a single Asn-linked carbohydrate unit.
3514617	15	118	gly	glycopeptide	2390:2401	arg2	glycopeptide					2390:2401	the tryptic glycopeptide pattern	2378:2409	the tryptic glycopeptide pattern of the variant	2378:2424	However, the tryptic glycopeptide pattern of the variant differed from control M or N alpha glycophorins, suggesting a deletion of a large segment of the molecule near residues 40-61 and/or a substitution of methionine for a residue upstream from residue 40.
3514617	7	119	from	similar	876:882	arg1	acid					893:896	amino acid and carbohydrate composition	887:925	acid	893:896	The amino-terminal octapeptides of the M and N species were similar in amino acid and carbohydrate composition to those isolated, respectively, from M and N alpha glycophorins.
3514617	7	119	from	similar	876:882	arg1	composition					915:925	amino acid and carbohydrate composition	887:925	composition	915:925	The amino-terminal octapeptides of the M and N species were similar in amino acid and carbohydrate composition to those isolated, respectively, from M and N alpha glycophorins.
3514617	6	120	theme	CNBr	645:648	arg1	fragments					650:658	the CNBr fragments	641:658	the CNBr fragments	641:658	Studies of the CNBr fragments provided evidence that the structure of M Sta glycophorin is the same as that of the usual M alpha glycophorin but that the N Sta glycophorin is a variant.
3514617	1	121	attach	isolated	109:116	arg2	glycophorins					96:107	glycophorins	96:107	glycophorins isolated from erythrocytes of an individual homozygous for the M Sta blood group phenotype	96:198	Structural and immunochemical studies of glycophorins isolated from erythrocytes of an individual homozygous for the M Sta blood group phenotype are described.
3514617	1	121	attach	isolated	109:116	arg1	erythrocytes					123:134	erythrocytes	123:134	erythrocytes of an individual homozygous for the M Sta blood group phenotype	123:198	Structural and immunochemical studies of glycophorins isolated from erythrocytes of an individual homozygous for the M Sta blood group phenotype are described.
3514617	14	122	located	found	2332:2336	arg1	glycophorins					2355:2366	control alpha glycophorins	2341:2366	control alpha glycophorins	2341:2366	The O-glycosidic saccharides appeared similar to those found in control alpha glycophorins.
3514617	14	122	located	found	2332:2336	arg2	those					2326:2330	those	2326:2330	those	2326:2330	The O-glycosidic saccharides appeared similar to those found in control alpha glycophorins.
3514617	2	123	theme	major	283:287	arg1	glycophorins					297:308	two major M and N glycophorins	279:308	two major M and N glycophorins	279:308	Reactivities with specific monoclonal antibodies indicated that two major M and N glycophorins were present.
3514617	9	124	theme	unit	1435:1438	arg1	terms					1250:1254	terms	1250:1254	terms of size, chromatographic behavior, amino acid and carbohydrate contents and compositions, the presence of O-glycosidically linked saccharides and a single Asn-linked carbohydrate unit	1250:1438	The fragment from the M species exhibited properties identical to those of the corresponding fragment of control alpha glycophorins in terms of size, chromatographic behavior, amino acid and carbohydrate contents and compositions, the presence of O-glycosidically linked saccharides and a single Asn-linked carbohydrate unit.
3514617	13	125	from	levels	2189:2194	arg1	protein					2235:2241	the intact N protein	2222:2241	the intact N protein	2222:2241	The much decreased levels of these carbohydrates in the intact N protein, corroborated the latter finding.
3514617	11	126	theme	Sta	1769:1771	arg1	B					1799:1799	the M Sta glycophorin CNBr fragment B	1763:1799	the M Sta glycophorin CNBr fragment B	1763:1799	The tryptic glycopeptide pattern of the M Sta glycophorin CNBr fragment B was identical to the pattern of the corresponding control fragment, and the composition of the tryptic peptides suggested sequence identity with the control fragment.
3514617	5	127	from	present	593:599	arg1	amounts					621:627	almost equimolar amounts	604:627	almost equimolar amounts	604:627	The two proteins were present in almost equimolar amounts.
3514617	15	128	theme	tryptic	2382:2388	arg1	pattern					2403:2409	the tryptic glycopeptide pattern	2378:2409	the tryptic glycopeptide pattern of the variant	2378:2424	However, the tryptic glycopeptide pattern of the variant differed from control M or N alpha glycophorins, suggesting a deletion of a large segment of the molecule near residues 40-61 and/or a substitution of methionine for a residue upstream from residue 40.
3514617	13	129	from	protein	2235:2241	arg1	levels					2189:2194	The much decreased levels	2170:2194	The much decreased levels	2170:2194	The much decreased levels of these carbohydrates in the intact N protein, corroborated the latter finding.
3514617	7	130	attach	isolated	936:943	arg1	N					971:971	N	971:971	N	971:971	The amino-terminal octapeptides of the M and N species were similar in amino acid and carbohydrate composition to those isolated, respectively, from M and N alpha glycophorins.
3514617	7	130	attach	isolated	936:943	arg2	those					930:934	those	930:934	those	930:934	The amino-terminal octapeptides of the M and N species were similar in amino acid and carbohydrate composition to those isolated, respectively, from M and N alpha glycophorins.
3514617	7	130	attach	isolated	936:943	arg1	M					965:965	M	965:965	M	965:965	The amino-terminal octapeptides of the M and N species were similar in amino acid and carbohydrate composition to those isolated, respectively, from M and N alpha glycophorins.
3514617	4	131	theme	control	482:488	arg1	glycophorins					496:507	control alpha glycophorins	482:507	control alpha glycophorins	482:507	The N species was not held on the lectin but the M species, like control alpha glycophorins, was retained and could be eluted with alpha-methylmannoside.
3514617	9	132	theme	corresponding	1194:1206	arg1	fragment					1208:1215	the corresponding fragment	1190:1215	the corresponding fragment of control alpha glycophorins in terms of size, chromatographic behavior, amino acid and carbohydrate contents and compositions, the presence of O-glycosidically linked saccharides and a single Asn-linked carbohydrate unit	1190:1438	The fragment from the M species exhibited properties identical to those of the corresponding fragment of control alpha glycophorins in terms of size, chromatographic behavior, amino acid and carbohydrate contents and compositions, the presence of O-glycosidically linked saccharides and a single Asn-linked carbohydrate unit.
3514617	0	133	from	glycophorins	9:20	arg1	erythrocytes					41:52	Sta blood group erythrocytes	25:52	Sta blood group erythrocytes	25:52	Membrane glycophorins in Sta blood group erythrocytes.
3514617	7	134	from	composition	915:925	arg1	similar					876:882	similar	876:882	similar	876:882	The amino-terminal octapeptides of the M and N species were similar in amino acid and carbohydrate composition to those isolated, respectively, from M and N alpha glycophorins.
3514617	7	134	from	composition	915:925	arg1	octapeptides					835:846	The amino-terminal octapeptides	816:846	The amino-terminal octapeptides of the M and N species	816:869	The amino-terminal octapeptides of the M and N species were similar in amino acid and carbohydrate composition to those isolated, respectively, from M and N alpha glycophorins.
3514617	15	135	theme	N	2453:2453	arg1	glycophorins					2461:2472	N alpha glycophorins	2453:2472	N alpha glycophorins	2453:2472	However, the tryptic glycopeptide pattern of the variant differed from control M or N alpha glycophorins, suggesting a deletion of a large segment of the molecule near residues 40-61 and/or a substitution of methionine for a residue upstream from residue 40.
3514617	1	136	theme	Structural	55:64	arg1	studies					85:91	Structural and immunochemical studies	55:91	Structural and immunochemical studies of glycophorins isolated from erythrocytes of an individual homozygous for the M Sta blood group phenotype	55:198	Structural and immunochemical studies of glycophorins isolated from erythrocytes of an individual homozygous for the M Sta blood group phenotype are described.
3514617	14	137	theme	alpha	2349:2353	arg1	glycophorins					2355:2366	control alpha glycophorins	2341:2366	control alpha glycophorins	2341:2366	The O-glycosidic saccharides appeared similar to those found in control alpha glycophorins.
3514617	4	138	theme	M	466:466	arg1	species					468:474	the M species	462:474	the M species	462:474	The N species was not held on the lectin but the M species, like control alpha glycophorins, was retained and could be eluted with alpha-methylmannoside.
3514617	12	139	theme	CNBr	2015:2018	arg1	B					2034:2034	two CNBr glycopeptides B	2011:2034	two CNBr glycopeptides B	2011:2034	In contrast, the N Sta glycophorin yielded two CNBr glycopeptides B; both contained fewer amino acid residues and virtually lacked Man and GlcNAc, indicating the absence of the Asn-linked carbohydrate.
3514617	6	140	theme	M	700:700	arg1	glycophorin					706:716	M Sta glycophorin	700:716	M Sta glycophorin	700:716	Studies of the CNBr fragments provided evidence that the structure of M Sta glycophorin is the same as that of the usual M alpha glycophorin but that the N Sta glycophorin is a variant.
3514617	9	141	theme	alpha	1228:1232	arg1	glycophorins					1234:1245	control alpha glycophorins	1220:1245	control alpha glycophorins in terms of size, chromatographic behavior, amino acid and carbohydrate contents and compositions, the presence of O-glycosidically linked saccharides and a single Asn-linked carbohydrate unit	1220:1438	The fragment from the M species exhibited properties identical to those of the corresponding fragment of control alpha glycophorins in terms of size, chromatographic behavior, amino acid and carbohydrate contents and compositions, the presence of O-glycosidically linked saccharides and a single Asn-linked carbohydrate unit.
3514617	1	142	theme	immunochemical	70:83	arg1	studies					85:91	Structural and immunochemical studies	55:91	Structural and immunochemical studies of glycophorins isolated from erythrocytes of an individual homozygous for the M Sta blood group phenotype	55:198	Structural and immunochemical studies of glycophorins isolated from erythrocytes of an individual homozygous for the M Sta blood group phenotype are described.
3514617	10	143	from	ratio	1623:1627	arg1	present					1610:1616	present	1610:1616	present	1610:1616	The structures of the O-linked units were inferred experimentally to be NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc and NeuAc(alpha 2,3)Gal(beta 1,3) [NeuAc(alpha 2,6)]GalNAc, present in a ratio similar to that found in controls; and the Asn-linked unit also appeared to be as in the control.
3514617	15	144	theme	large	2502:2506	arg1	segment					2508:2514	a large segment	2500:2514	a large segment of the molecule near residues 40-61	2500:2550	However, the tryptic glycopeptide pattern of the variant differed from control M or N alpha glycophorins, suggesting a deletion of a large segment of the molecule near residues 40-61 and/or a substitution of methionine for a residue upstream from residue 40.
3514617	12	145	theme	amino	2058:2062	arg1	residues					2069:2076	fewer amino acid residues	2052:2076	fewer amino acid residues	2052:2076	In contrast, the N Sta glycophorin yielded two CNBr glycopeptides B; both contained fewer amino acid residues and virtually lacked Man and GlcNAc, indicating the absence of the Asn-linked carbohydrate.
3514617	8	146	gly	glycopeptide	1021:1032	arg2	glycopeptide					1021:1032	CNBr glycopeptide B	1016:1034	CNBr glycopeptide B that, in control alpha glycophorins, extends from amino acid residues 9 to 81	1016:1112	The studies focused on CNBr glycopeptide B that, in control alpha glycophorins, extends from amino acid residues 9 to 81.
3514617	9	147	from	terms	1250:1254	arg1	fragment					1208:1215	the corresponding fragment	1190:1215	the corresponding fragment of control alpha glycophorins in terms of size, chromatographic behavior, amino acid and carbohydrate contents and compositions, the presence of O-glycosidically linked saccharides and a single Asn-linked carbohydrate unit	1190:1438	The fragment from the M species exhibited properties identical to those of the corresponding fragment of control alpha glycophorins in terms of size, chromatographic behavior, amino acid and carbohydrate contents and compositions, the presence of O-glycosidically linked saccharides and a single Asn-linked carbohydrate unit.
3514617	7	148	theme	amino	887:891	arg1	acid					893:896	amino acid and carbohydrate composition	887:925	acid	893:896	The amino-terminal octapeptides of the M and N species were similar in amino acid and carbohydrate composition to those isolated, respectively, from M and N alpha glycophorins.
3514617	3	149	theme	affinity	392:399	arg1	chromatography					401:414	Lens culinaris lectin affinity chromatography	370:414	Lens culinaris lectin affinity chromatography	370:414	The M and N Sta glycophorins were resolved by Lens culinaris lectin affinity chromatography.
3514617	14	150	theme	O-glycosidic	2281:2292	arg1	saccharides					2294:2304	The O-glycosidic saccharides	2277:2304	The O-glycosidic saccharides	2277:2304	The O-glycosidic saccharides appeared similar to those found in control alpha glycophorins.
3514617	12	151	theme	Sta	1987:1989	arg1	glycophorin					1991:2001	the N Sta glycophorin	1981:2001	the N Sta glycophorin	1981:2001	In contrast, the N Sta glycophorin yielded two CNBr glycopeptides B; both contained fewer amino acid residues and virtually lacked Man and GlcNAc, indicating the absence of the Asn-linked carbohydrate.
3514617	10	152	link	Asn-linked	1672:1681	arg1	unit					1683:1686	the Asn-linked unit	1668:1686	the Asn-linked unit	1668:1686	The structures of the O-linked units were inferred experimentally to be NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc and NeuAc(alpha 2,3)Gal(beta 1,3) [NeuAc(alpha 2,6)]GalNAc, present in a ratio similar to that found in controls; and the Asn-linked unit also appeared to be as in the control.
3514617	0	153	theme	Sta	25:27	arg1	erythrocytes					41:52	Sta blood group erythrocytes	25:52	Sta blood group erythrocytes	25:52	Membrane glycophorins in Sta blood group erythrocytes.
3514617	12	154	gly	glycopeptides	2020:2032	arg2	glycopeptides					2020:2032	two CNBr glycopeptides B	2011:2034	two CNBr glycopeptides B	2011:2034	In contrast, the N Sta glycophorin yielded two CNBr glycopeptides B; both contained fewer amino acid residues and virtually lacked Man and GlcNAc, indicating the absence of the Asn-linked carbohydrate.
3514617	8	155	theme	CNBr	1016:1019	arg1	B					1034:1034	CNBr glycopeptide B	1016:1034	CNBr glycopeptide B that, in control alpha glycophorins, extends from amino acid residues 9 to 81	1016:1112	The studies focused on CNBr glycopeptide B that, in control alpha glycophorins, extends from amino acid residues 9 to 81.
3514617	3	156	theme	culinaris	375:383	arg1	chromatography					401:414	Lens culinaris lectin affinity chromatography	370:414	Lens culinaris lectin affinity chromatography	370:414	The M and N Sta glycophorins were resolved by Lens culinaris lectin affinity chromatography.
3514617	13	157	theme	intact	2226:2231	arg1	protein					2235:2241	the intact N protein	2222:2241	the intact N protein	2222:2241	The much decreased levels of these carbohydrates in the intact N protein, corroborated the latter finding.
3514617	10	158	theme	2,3	1566:1568	arg1	[NeuAc					1584:1589	alpha 2,3)Gal(beta 1,3) [NeuAc	1560:1589	alpha 2,3)Gal(beta 1,3) [NeuAc(alpha 2,6)	1560:1600	The structures of the O-linked units were inferred experimentally to be NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc and NeuAc(alpha 2,3)Gal(beta 1,3) [NeuAc(alpha 2,6)]GalNAc, present in a ratio similar to that found in controls; and the Asn-linked unit also appeared to be as in the control.
3514617	10	158	theme	2,3	1566:1568	arg1	2,6					1597:1599	alpha 2,6	1591:1599	alpha 2,6	1591:1599	The structures of the O-linked units were inferred experimentally to be NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc and NeuAc(alpha 2,3)Gal(beta 1,3) [NeuAc(alpha 2,6)]GalNAc, present in a ratio similar to that found in controls; and the Asn-linked unit also appeared to be as in the control.
3514617	0	159	theme	group	35:39	arg1	erythrocytes					41:52	Sta blood group erythrocytes	25:52	Sta blood group erythrocytes	25:52	Membrane glycophorins in Sta blood group erythrocytes.
3514617	15	160	dep	residues	2537:2544	arg1	40-61					2546:2550	40-61	2546:2550	40-61	2546:2550	However, the tryptic glycopeptide pattern of the variant differed from control M or N alpha glycophorins, suggesting a deletion of a large segment of the molecule near residues 40-61 and/or a substitution of methionine for a residue upstream from residue 40.
3514617	15	161	theme	segment	2508:2514	arg1	deletion					2488:2495	a deletion	2486:2495	a deletion of a large segment of the molecule near residues 40-61	2486:2550	However, the tryptic glycopeptide pattern of the variant differed from control M or N alpha glycophorins, suggesting a deletion of a large segment of the molecule near residues 40-61 and/or a substitution of methionine for a residue upstream from residue 40.
3514617	9	162	theme	behavior	1281:1288	arg1	terms					1250:1254	terms	1250:1254	terms of size, chromatographic behavior, amino acid and carbohydrate contents and compositions, the presence of O-glycosidically linked saccharides and a single Asn-linked carbohydrate unit	1250:1438	The fragment from the M species exhibited properties identical to those of the corresponding fragment of control alpha glycophorins in terms of size, chromatographic behavior, amino acid and carbohydrate contents and compositions, the presence of O-glycosidically linked saccharides and a single Asn-linked carbohydrate unit.
3514617	8	163	dep	81	1111:1112	arg1	to					1108:1109	to	1108:1109	to	1108:1109	The studies focused on CNBr glycopeptide B that, in control alpha glycophorins, extends from amino acid residues 9 to 81.
3514617	10	164	theme	beta	1574:1577	arg1	[NeuAc					1584:1589	alpha 2,3)Gal(beta 1,3) [NeuAc	1560:1589	alpha 2,3)Gal(beta 1,3) [NeuAc(alpha 2,6)	1560:1600	The structures of the O-linked units were inferred experimentally to be NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc and NeuAc(alpha 2,3)Gal(beta 1,3) [NeuAc(alpha 2,6)]GalNAc, present in a ratio similar to that found in controls; and the Asn-linked unit also appeared to be as in the control.
3514617	10	164	theme	beta	1574:1577	arg1	2,6					1597:1599	alpha 2,6	1591:1599	alpha 2,6	1591:1599	The structures of the O-linked units were inferred experimentally to be NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc and NeuAc(alpha 2,3)Gal(beta 1,3) [NeuAc(alpha 2,6)]GalNAc, present in a ratio similar to that found in controls; and the Asn-linked unit also appeared to be as in the control.
3514617	7	165	theme	N	861:861	arg1	species					863:869	the M and N species	851:869	the M and N species	851:869	The amino-terminal octapeptides of the M and N species were similar in amino acid and carbohydrate composition to those isolated, respectively, from M and N alpha glycophorins.
3514617	9	166	theme	amino	1291:1295	arg1	acid					1297:1300	amino acid and carbohydrate contents	1291:1326	acid	1297:1300	The fragment from the M species exhibited properties identical to those of the corresponding fragment of control alpha glycophorins in terms of size, chromatographic behavior, amino acid and carbohydrate contents and compositions, the presence of O-glycosidically linked saccharides and a single Asn-linked carbohydrate unit.
3514617	9	167	link	Asn-linked	1411:1420	arg1	unit					1435:1438	a single Asn-linked carbohydrate unit	1402:1438	a single Asn-linked carbohydrate unit	1402:1438	The fragment from the M species exhibited properties identical to those of the corresponding fragment of control alpha glycophorins in terms of size, chromatographic behavior, amino acid and carbohydrate contents and compositions, the presence of O-glycosidically linked saccharides and a single Asn-linked carbohydrate unit.
3514617	11	168	theme	M	1767:1767	arg1	B					1799:1799	the M Sta glycophorin CNBr fragment B	1763:1799	the M Sta glycophorin CNBr fragment B	1763:1799	The tryptic glycopeptide pattern of the M Sta glycophorin CNBr fragment B was identical to the pattern of the corresponding control fragment, and the composition of the tryptic peptides suggested sequence identity with the control fragment.
3514617	10	169	theme	Gal	1570:1572	arg1	[NeuAc					1584:1589	alpha 2,3)Gal(beta 1,3) [NeuAc	1560:1589	alpha 2,3)Gal(beta 1,3) [NeuAc(alpha 2,6)	1560:1600	The structures of the O-linked units were inferred experimentally to be NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc and NeuAc(alpha 2,3)Gal(beta 1,3) [NeuAc(alpha 2,6)]GalNAc, present in a ratio similar to that found in controls; and the Asn-linked unit also appeared to be as in the control.
3514617	10	169	theme	Gal	1570:1572	arg1	2,6					1597:1599	alpha 2,6	1591:1599	alpha 2,6	1591:1599	The structures of the O-linked units were inferred experimentally to be NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc and NeuAc(alpha 2,3)Gal(beta 1,3) [NeuAc(alpha 2,6)]GalNAc, present in a ratio similar to that found in controls; and the Asn-linked unit also appeared to be as in the control.
3514617	7	170	theme	M	855:855	arg1	species					863:869	the M and N species	851:869	the M and N species	851:869	The amino-terminal octapeptides of the M and N species were similar in amino acid and carbohydrate composition to those isolated, respectively, from M and N alpha glycophorins.
3514617	6	171	theme	N	784:784	arg1	glycophorin					790:800	the N Sta glycophorin	780:800	the N Sta glycophorin	780:800	Studies of the CNBr fragments provided evidence that the structure of M Sta glycophorin is the same as that of the usual M alpha glycophorin but that the N Sta glycophorin is a variant.
3514617	6	171	theme	N	784:784	arg1	variant					807:813	a variant	805:813	a variant	805:813	Studies of the CNBr fragments provided evidence that the structure of M Sta glycophorin is the same as that of the usual M alpha glycophorin but that the N Sta glycophorin is a variant.
3514617	6	172	theme	glycophorin	706:716	arg1	structure					687:695	the structure	683:695	the structure of M Sta glycophorin	683:716	Studies of the CNBr fragments provided evidence that the structure of M Sta glycophorin is the same as that of the usual M alpha glycophorin but that the N Sta glycophorin is a variant.
3514617	6	172	theme	glycophorin	706:716	arg1	same					725:728	same	725:728	same	725:728	Studies of the CNBr fragments provided evidence that the structure of M Sta glycophorin is the same as that of the usual M alpha glycophorin but that the N Sta glycophorin is a variant.
1421410	8	0	contain	contain	1333:1339	arg1	glycophorins					1303:1314	Tn glycophorins	1300:1314	Tn glycophorins from both donors	1300:1331	The results show that Tn glycophorins from both donors contain intact and truncated forms of trisaccharide and tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3- (NeuNAc alpha 2,6)GalNAc usually present in glycophorins A and B.
1421410	8	0	contain	contain	1333:1339	arg2	forms					1362:1366	intact and truncated forms	1341:1366	intact and truncated forms of trisaccharide and tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3- (NeuNAc alpha 2,6)GalNAc usually present in glycophorins A and B	1341:1537	The results show that Tn glycophorins from both donors contain intact and truncated forms of trisaccharide and tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3- (NeuNAc alpha 2,6)GalNAc usually present in glycophorins A and B.
1421410	7	1	with	comparison	1171:1180	arg1	standards					1187:1195	standards	1187:1195	standards	1187:1195	The reduced radiolabeled products were fractionated by Bio-Gel P-2 chromatography, and their structures were investigated by comparison with standards, by monosaccharide quantification, and by neuraminidases of known specificities.
1421410	0	2	with	individuals	73:83	arg1	syndrome					117:124	the Tn polyagglutinability syndrome	90:124	the Tn polyagglutinability syndrome	90:124	O-linked oligosaccharides of glycophorins A and B in erythrocytes of two individuals with the Tn polyagglutinability syndrome.
1421410	11	3	from	identical	1876:1884	arg1	glycophorins					1889:1900	glycophorins	1889:1900	glycophorins of these two donors	1889:1920	The proportion of the four species was not identical in glycophorins of these two donors but, in both, the truncated units predominated and the amount of the disaccharide was approximately one half of that of the monosaccharide.
1421410	11	3	from	identical	1876:1884	arg1	both					1930:1933	both	1930:1933	both	1930:1933	The proportion of the four species was not identical in glycophorins of these two donors but, in both, the truncated units predominated and the amount of the disaccharide was approximately one half of that of the monosaccharide.
1421410	12	4	theme	alpha	2240:2244	arg1	transferase					2259:2269	a specific GalNAc protein alpha 2,6 sialosyl transferase	2214:2269	a specific GalNAc protein alpha 2,6 sialosyl transferase in Tn hematopoietic precursor cells	2214:2305	The data are consistent with alterations in UDPGal:GalNAc beta 1,3galactosyl transferase that may have multiple molecular origins and with induction of a specific GalNAc protein alpha 2,6 sialosyl transferase in Tn hematopoietic precursor cells.
1421410	1	5	attach	present	304:310	arg2	anti-Tn					296:302	the naturally occurring anti-Tn	272:302	the naturally occurring anti-Tn present in normal sera	272:325	Tn polyagglutinability syndrome is an acquired condition where erythrocytes express Tn neo-antigen and become susceptible to hemagglutination by the naturally occurring anti-Tn present in normal sera.
1421410	1	5	attach	present	304:310	arg1	sera					322:325	normal sera	315:325	normal sera	315:325	Tn polyagglutinability syndrome is an acquired condition where erythrocytes express Tn neo-antigen and become susceptible to hemagglutination by the naturally occurring anti-Tn present in normal sera.
1421410	12	6	dep	UDPGal	2106:2111	arg1	transferase					2139:2149	GalNAc beta 1,3galactosyl transferase	2113:2149	UDPGal:GalNAc beta 1,3galactosyl transferase that may have multiple molecular origins	2106:2190	The data are consistent with alterations in UDPGal:GalNAc beta 1,3galactosyl transferase that may have multiple molecular origins and with induction of a specific GalNAc protein alpha 2,6 sialosyl transferase in Tn hematopoietic precursor cells.
1421410	0	7	link	O-linked	0:7	arg1	oligosaccharides					9:24	O-linked oligosaccharides	0:24	O-linked oligosaccharides of glycophorins A and B in erythrocytes of two individuals with the Tn polyagglutinability syndrome	0:124	O-linked oligosaccharides of glycophorins A and B in erythrocytes of two individuals with the Tn polyagglutinability syndrome.
1421410	6	8	link	O-linked	937:944	arg1	oligosaccharides					946:961	O-linked oligosaccharides	937:961	O-linked oligosaccharides	937:961	O-linked oligosaccharides were obtained by beta-elimination in the presence of tritiated sodium borohydride.
1421410	8	9	theme	Tn	1300:1301	arg1	glycophorins					1303:1314	Tn glycophorins	1300:1314	Tn glycophorins from both donors	1300:1331	The results show that Tn glycophorins from both donors contain intact and truncated forms of trisaccharide and tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3- (NeuNAc alpha 2,6)GalNAc usually present in glycophorins A and B.
1421410	1	10	from	sera	322:325	arg1	present					304:310	present	304:310	present	304:310	Tn polyagglutinability syndrome is an acquired condition where erythrocytes express Tn neo-antigen and become susceptible to hemagglutination by the naturally occurring anti-Tn present in normal sera.
1421410	0	11	theme	O-linked	0:7	arg1	oligosaccharides					9:24	O-linked oligosaccharides	0:24	O-linked oligosaccharides of glycophorins A and B in erythrocytes of two individuals with the Tn polyagglutinability syndrome	0:124	O-linked oligosaccharides of glycophorins A and B in erythrocytes of two individuals with the Tn polyagglutinability syndrome.
1421410	10	12	from	presence	1673:1680	arg1	population					1713:1722	the total population	1703:1722	the total population of Tn erythrocytes	1703:1741	The presence of intact glycans in the total population of Tn erythrocytes was confirmed by their susceptibility to T activation after treatment with neuraminidase.
1421410	5	13	with	composition	827:837	arg1	N-glycanase					858:868	N-glycanase	858:868	N-glycanase	858:868	Analysis of carbohydrate composition and treatment with N-glycanase showed that the Asn-linked unit of glycophorin A was not affected.
1421410	12	14	theme	molecular	2174:2182	arg1	origins					2184:2190	multiple molecular origins	2165:2190	multiple molecular origins	2165:2190	The data are consistent with alterations in UDPGal:GalNAc beta 1,3galactosyl transferase that may have multiple molecular origins and with induction of a specific GalNAc protein alpha 2,6 sialosyl transferase in Tn hematopoietic precursor cells.
1421410	12	15	with	consistent	2075:2084	arg1	induction					2201:2209	induction	2201:2209	induction of a specific GalNAc protein alpha 2,6 sialosyl transferase in Tn hematopoietic precursor cells	2201:2305	The data are consistent with alterations in UDPGal:GalNAc beta 1,3galactosyl transferase that may have multiple molecular origins and with induction of a specific GalNAc protein alpha 2,6 sialosyl transferase in Tn hematopoietic precursor cells.
1421410	12	15	with	consistent	2075:2084	arg1	alterations					2091:2101	alterations	2091:2101	alterations in UDPGal:GalNAc beta 1,3galactosyl transferase that may have multiple molecular origins	2091:2190	The data are consistent with alterations in UDPGal:GalNAc beta 1,3galactosyl transferase that may have multiple molecular origins and with induction of a specific GalNAc protein alpha 2,6 sialosyl transferase in Tn hematopoietic precursor cells.
1421410	3	16	gly	glycoproteins	597:609	arg1	glycoproteins					597:609	purified glycoproteins	588:609	purified glycoproteins	588:609	However, none of these studies were performed on purified glycoproteins.
1421410	10	17	theme	intact	1685:1690	arg1	glycans					1692:1698	intact glycans	1685:1698	intact glycans	1685:1698	The presence of intact glycans in the total population of Tn erythrocytes was confirmed by their susceptibility to T activation after treatment with neuraminidase.
1421410	8	18	theme	intact	1341:1346	arg1	forms					1362:1366	intact and truncated forms	1341:1366	intact and truncated forms of trisaccharide and tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3- (NeuNAc alpha 2,6)GalNAc usually present in glycophorins A and B	1341:1537	The results show that Tn glycophorins from both donors contain intact and truncated forms of trisaccharide and tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3- (NeuNAc alpha 2,6)GalNAc usually present in glycophorins A and B.
1421410	7	19	theme	P-2	1109:1111	arg1	chromatography					1113:1126	Bio-Gel P-2 chromatography	1101:1126	Bio-Gel P-2 chromatography	1101:1126	The reduced radiolabeled products were fractionated by Bio-Gel P-2 chromatography, and their structures were investigated by comparison with standards, by monosaccharide quantification, and by neuraminidases of known specificities.
1421410	5	20	theme	composition	827:837	arg1	Analysis					802:809	Analysis	802:809	Analysis of carbohydrate composition and treatment with N-glycanase	802:868	Analysis of carbohydrate composition and treatment with N-glycanase showed that the Asn-linked unit of glycophorin A was not affected.
1421410	7	21	theme	reduced	1050:1056	arg1	products					1071:1078	The reduced radiolabeled products	1046:1078	The reduced radiolabeled products	1046:1078	The reduced radiolabeled products were fractionated by Bio-Gel P-2 chromatography, and their structures were investigated by comparison with standards, by monosaccharide quantification, and by neuraminidases of known specificities.
1421410	8	22	theme	truncated	1352:1360	arg1	forms					1362:1366	intact and truncated forms	1341:1366	intact and truncated forms of trisaccharide and tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3- (NeuNAc alpha 2,6)GalNAc usually present in glycophorins A and B	1341:1537	The results show that Tn glycophorins from both donors contain intact and truncated forms of trisaccharide and tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3- (NeuNAc alpha 2,6)GalNAc usually present in glycophorins A and B.
1421410	9	23	theme	truncated	1544:1552	arg1	forms					1554:1558	The truncated forms	1540:1558	The truncated forms	1540:1558	The truncated forms include the protein O-linked monosaccharide, GalNAc and disaccharide, NeuNAc alpha 2,6GalNAc (major isomer).
1421410	4	24	theme	individuals	725:735	arg1	erythrocytes					696:707	Tn erythrocytes	693:707	Tn erythrocytes of two affected individuals	693:735	In this report we examine oligosaccharides of glycophorins A and B purified from Tn erythrocytes of two affected individuals to establish how N- and O-linked saccharides differ from normal.
1421410	12	25	theme	sialosyl	2250:2257	arg1	transferase					2259:2269	a specific GalNAc protein alpha 2,6 sialosyl transferase	2214:2269	a specific GalNAc protein alpha 2,6 sialosyl transferase in Tn hematopoietic precursor cells	2214:2305	The data are consistent with alterations in UDPGal:GalNAc beta 1,3galactosyl transferase that may have multiple molecular origins and with induction of a specific GalNAc protein alpha 2,6 sialosyl transferase in Tn hematopoietic precursor cells.
1421410	12	26	from	alterations	2091:2101	arg1	UDPGal					2106:2111	UDPGal	2106:2111	UDPGal:GalNAc beta 1,3galactosyl transferase that may have multiple molecular origins	2106:2190	The data are consistent with alterations in UDPGal:GalNAc beta 1,3galactosyl transferase that may have multiple molecular origins and with induction of a specific GalNAc protein alpha 2,6 sialosyl transferase in Tn hematopoietic precursor cells.
1421410	1	27	theme	polyagglutinability	130:148	arg1	condition					174:182	an acquired condition	162:182	an acquired condition where erythrocytes express Tn neo-antigen and become susceptible to hemagglutination by the naturally occurring anti-Tn present in normal sera	162:325	Tn polyagglutinability syndrome is an acquired condition where erythrocytes express Tn neo-antigen and become susceptible to hemagglutination by the naturally occurring anti-Tn present in normal sera.
1421410	1	27	theme	polyagglutinability	130:148	arg1	syndrome					150:157	Tn polyagglutinability syndrome	127:157	Tn polyagglutinability syndrome	127:157	Tn polyagglutinability syndrome is an acquired condition where erythrocytes express Tn neo-antigen and become susceptible to hemagglutination by the naturally occurring anti-Tn present in normal sera.
1421410	12	28	theme	GalNAc	2113:2118	arg1	transferase					2139:2149	GalNAc beta 1,3galactosyl transferase	2113:2149	UDPGal:GalNAc beta 1,3galactosyl transferase that may have multiple molecular origins	2106:2190	The data are consistent with alterations in UDPGal:GalNAc beta 1,3galactosyl transferase that may have multiple molecular origins and with induction of a specific GalNAc protein alpha 2,6 sialosyl transferase in Tn hematopoietic precursor cells.
1421410	2	29	theme	Tn	513:514	arg1	sialosyl-Tn					525:535	sialosyl-Tn	525:535	sialosyl-Tn	525:535	Early studies had indicated that O-linked N-acetyl galactosamine was the sole serologic Tn determinant, but more recently O-linked NeuNAc alpha 2, 6GalNAc also has been implicated as a Tn antigen (sialosyl-Tn).
1421410	2	29	theme	Tn	513:514	arg1	6GalNAc					475:481	O-linked NeuNAc alpha 2, 6GalNAc	450:481	6GalNAc	475:481	Early studies had indicated that O-linked N-acetyl galactosamine was the sole serologic Tn determinant, but more recently O-linked NeuNAc alpha 2, 6GalNAc also has been implicated as a Tn antigen (sialosyl-Tn).
1421410	2	29	theme	Tn	513:514	arg1	antigen					516:522	a Tn antigen	511:522	a Tn antigen (sialosyl-Tn)	511:536	Early studies had indicated that O-linked N-acetyl galactosamine was the sole serologic Tn determinant, but more recently O-linked NeuNAc alpha 2, 6GalNAc also has been implicated as a Tn antigen (sialosyl-Tn).
1421410	10	30	theme	Tn	1727:1728	arg1	erythrocytes					1730:1741	Tn erythrocytes	1727:1741	Tn erythrocytes	1727:1741	The presence of intact glycans in the total population of Tn erythrocytes was confirmed by their susceptibility to T activation after treatment with neuraminidase.
1421410	8	31	from	donors	1326:1331	arg1	glycophorins					1303:1314	Tn glycophorins	1300:1314	Tn glycophorins from both donors	1300:1331	The results show that Tn glycophorins from both donors contain intact and truncated forms of trisaccharide and tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3- (NeuNAc alpha 2,6)GalNAc usually present in glycophorins A and B.
1421410	5	32	theme	glycophorin	905:915	arg1	A					917:917	glycophorin A	905:917	glycophorin A	905:917	Analysis of carbohydrate composition and treatment with N-glycanase showed that the Asn-linked unit of glycophorin A was not affected.
1421410	10	33	with	treatment	1803:1811	arg1	neuraminidase					1818:1830	neuraminidase	1818:1830	neuraminidase	1818:1830	The presence of intact glycans in the total population of Tn erythrocytes was confirmed by their susceptibility to T activation after treatment with neuraminidase.
1421410	8	34	theme	NeuNAc	1405:1410	arg1	1,3GalNAc					1430:1438	tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3-	1389:1472	1,3GalNAc	1430:1438	The results show that Tn glycophorins from both donors contain intact and truncated forms of trisaccharide and tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3- (NeuNAc alpha 2,6)GalNAc usually present in glycophorins A and B.
1421410	8	34	theme	NeuNAc	1405:1410	arg1	alpha					1482:1486	NeuNAc alpha 2,6	1475:1490	NeuNAc alpha 2,6	1475:1490	The results show that Tn glycophorins from both donors contain intact and truncated forms of trisaccharide and tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3- (NeuNAc alpha 2,6)GalNAc usually present in glycophorins A and B.
1421410	1	35	theme	acquired	165:172	arg1	condition					174:182	an acquired condition	162:182	an acquired condition where erythrocytes express Tn neo-antigen and become susceptible to hemagglutination by the naturally occurring anti-Tn present in normal sera	162:325	Tn polyagglutinability syndrome is an acquired condition where erythrocytes express Tn neo-antigen and become susceptible to hemagglutination by the naturally occurring anti-Tn present in normal sera.
1421410	1	35	theme	acquired	165:172	arg1	syndrome					150:157	Tn polyagglutinability syndrome	127:157	Tn polyagglutinability syndrome	127:157	Tn polyagglutinability syndrome is an acquired condition where erythrocytes express Tn neo-antigen and become susceptible to hemagglutination by the naturally occurring anti-Tn present in normal sera.
1421410	6	36	theme	sodium	1026:1031	arg1	borohydride					1033:1043	tritiated sodium borohydride	1016:1043	tritiated sodium borohydride	1016:1043	O-linked oligosaccharides were obtained by beta-elimination in the presence of tritiated sodium borohydride.
1421410	4	37	theme	O-linked	761:768	arg1	saccharides					770:780	O-linked saccharides	761:780	O-linked saccharides	761:780	In this report we examine oligosaccharides of glycophorins A and B purified from Tn erythrocytes of two affected individuals to establish how N- and O-linked saccharides differ from normal.
1421410	12	38	theme	2,6	2246:2248	arg1	transferase					2259:2269	a specific GalNAc protein alpha 2,6 sialosyl transferase	2214:2269	a specific GalNAc protein alpha 2,6 sialosyl transferase in Tn hematopoietic precursor cells	2214:2305	The data are consistent with alterations in UDPGal:GalNAc beta 1,3galactosyl transferase that may have multiple molecular origins and with induction of a specific GalNAc protein alpha 2,6 sialosyl transferase in Tn hematopoietic precursor cells.
1421410	7	39	theme	specificities	1263:1275	arg1	neuraminidases					1239:1252	neuraminidases	1239:1252	neuraminidases of known specificities	1239:1275	The reduced radiolabeled products were fractionated by Bio-Gel P-2 chromatography, and their structures were investigated by comparison with standards, by monosaccharide quantification, and by neuraminidases of known specificities.
1421410	12	40	theme	precursor	2291:2299	arg1	cells					2301:2305	Tn hematopoietic precursor cells	2274:2305	Tn hematopoietic precursor cells	2274:2305	The data are consistent with alterations in UDPGal:GalNAc beta 1,3galactosyl transferase that may have multiple molecular origins and with induction of a specific GalNAc protein alpha 2,6 sialosyl transferase in Tn hematopoietic precursor cells.
1421410	8	41	theme	1,3GalNAc	1430:1438	arg1	GalNAc					1492:1497	tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3- (NeuNAc alpha 2,6)GalNAc	1389:1497	tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3- (NeuNAc alpha 2,6)GalNAc	1389:1497	The results show that Tn glycophorins from both donors contain intact and truncated forms of trisaccharide and tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3- (NeuNAc alpha 2,6)GalNAc usually present in glycophorins A and B.
1421410	0	42	theme	Tn	94:95	arg1	syndrome					117:124	the Tn polyagglutinability syndrome	90:124	the Tn polyagglutinability syndrome	90:124	O-linked oligosaccharides of glycophorins A and B in erythrocytes of two individuals with the Tn polyagglutinability syndrome.
1421410	8	43	theme	NeuNAc	1444:1449	arg1	beta					1464:1467	tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3-	1389:1472	beta	1464:1467	The results show that Tn glycophorins from both donors contain intact and truncated forms of trisaccharide and tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3- (NeuNAc alpha 2,6)GalNAc usually present in glycophorins A and B.
1421410	2	44	theme	Tn	416:417	arg1	determinant					419:429	the sole serologic Tn determinant	397:429	the sole serologic Tn determinant	397:429	Early studies had indicated that O-linked N-acetyl galactosamine was the sole serologic Tn determinant, but more recently O-linked NeuNAc alpha 2, 6GalNAc also has been implicated as a Tn antigen (sialosyl-Tn).
1421410	2	44	theme	Tn	416:417	arg1	galactosamine					379:391	O-linked N-acetyl galactosamine	361:391	O-linked N-acetyl galactosamine	361:391	Early studies had indicated that O-linked N-acetyl galactosamine was the sole serologic Tn determinant, but more recently O-linked NeuNAc alpha 2, 6GalNAc also has been implicated as a Tn antigen (sialosyl-Tn).
1421410	5	45	theme	carbohydrate	814:825	arg1	composition					827:837	carbohydrate composition	814:837	carbohydrate composition	814:837	Analysis of carbohydrate composition and treatment with N-glycanase showed that the Asn-linked unit of glycophorin A was not affected.
1421410	1	46	theme	present	304:310	arg1	anti-Tn					296:302	the naturally occurring anti-Tn	272:302	the naturally occurring anti-Tn present in normal sera	272:325	Tn polyagglutinability syndrome is an acquired condition where erythrocytes express Tn neo-antigen and become susceptible to hemagglutination by the naturally occurring anti-Tn present in normal sera.
1421410	9	47	theme	NeuNAc	1630:1635	arg1	isomer					1660:1665	major isomer	1654:1665	major isomer	1654:1665	The truncated forms include the protein O-linked monosaccharide, GalNAc and disaccharide, NeuNAc alpha 2,6GalNAc (major isomer).
1421410	9	47	theme	NeuNAc	1630:1635	arg1	monosaccharide					1589:1602	the protein O-linked monosaccharide	1568:1602	the protein O-linked monosaccharide	1568:1602	The truncated forms include the protein O-linked monosaccharide, GalNAc and disaccharide, NeuNAc alpha 2,6GalNAc (major isomer).
1421410	9	47	theme	NeuNAc	1630:1635	arg1	2,6GalNAc					1643:1651	NeuNAc alpha 2,6GalNAc	1630:1651	NeuNAc alpha 2,6GalNAc (major isomer)	1630:1666	The truncated forms include the protein O-linked monosaccharide, GalNAc and disaccharide, NeuNAc alpha 2,6GalNAc (major isomer).
1421410	2	48	theme	alpha	466:470	arg1	antigen					516:522	a Tn antigen	511:522	a Tn antigen (sialosyl-Tn)	511:536	Early studies had indicated that O-linked N-acetyl galactosamine was the sole serologic Tn determinant, but more recently O-linked NeuNAc alpha 2, 6GalNAc also has been implicated as a Tn antigen (sialosyl-Tn).
1421410	2	48	theme	alpha	466:470	arg1	6GalNAc					475:481	O-linked NeuNAc alpha 2, 6GalNAc	450:481	6GalNAc	475:481	Early studies had indicated that O-linked N-acetyl galactosamine was the sole serologic Tn determinant, but more recently O-linked NeuNAc alpha 2, 6GalNAc also has been implicated as a Tn antigen (sialosyl-Tn).
1421410	10	49	theme	glycans	1692:1698	arg1	presence					1673:1680	The presence	1669:1680	The presence of intact glycans in the total population of Tn erythrocytes	1669:1741	The presence of intact glycans in the total population of Tn erythrocytes was confirmed by their susceptibility to T activation after treatment with neuraminidase.
1421410	8	50	theme	2,3Gal	1457:1462	arg1	beta					1464:1467	tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3-	1389:1472	beta	1464:1467	The results show that Tn glycophorins from both donors contain intact and truncated forms of trisaccharide and tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3- (NeuNAc alpha 2,6)GalNAc usually present in glycophorins A and B.
1421410	2	51	theme	O-linked	450:457	arg1	antigen					516:522	a Tn antigen	511:522	a Tn antigen (sialosyl-Tn)	511:536	Early studies had indicated that O-linked N-acetyl galactosamine was the sole serologic Tn determinant, but more recently O-linked NeuNAc alpha 2, 6GalNAc also has been implicated as a Tn antigen (sialosyl-Tn).
1421410	2	51	theme	O-linked	450:457	arg1	6GalNAc					475:481	O-linked NeuNAc alpha 2, 6GalNAc	450:481	6GalNAc	475:481	Early studies had indicated that O-linked N-acetyl galactosamine was the sole serologic Tn determinant, but more recently O-linked NeuNAc alpha 2, 6GalNAc also has been implicated as a Tn antigen (sialosyl-Tn).
1421410	1	52	theme	normal	315:320	arg1	sera					322:325	normal sera	315:325	normal sera	315:325	Tn polyagglutinability syndrome is an acquired condition where erythrocytes express Tn neo-antigen and become susceptible to hemagglutination by the naturally occurring anti-Tn present in normal sera.
1421410	5	53	with	treatment	843:851	arg1	N-glycanase					858:868	N-glycanase	858:868	N-glycanase	858:868	Analysis of carbohydrate composition and treatment with N-glycanase showed that the Asn-linked unit of glycophorin A was not affected.
1421410	7	54	theme	monosaccharide	1201:1214	arg1	quantification					1216:1229	monosaccharide quantification	1201:1229	monosaccharide quantification	1201:1229	The reduced radiolabeled products were fractionated by Bio-Gel P-2 chromatography, and their structures were investigated by comparison with standards, by monosaccharide quantification, and by neuraminidases of known specificities.
1421410	8	55	dep	glycophorins	1518:1529	arg1	glycophorins					1518:1529	glycophorins A and B	1518:1537	glycophorins A and B	1518:1537	The results show that Tn glycophorins from both donors contain intact and truncated forms of trisaccharide and tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3- (NeuNAc alpha 2,6)GalNAc usually present in glycophorins A and B.
1421410	8	55	dep	glycophorins	1518:1529	arg1	B					1537:1537	B	1537:1537	B	1537:1537	The results show that Tn glycophorins from both donors contain intact and truncated forms of trisaccharide and tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3- (NeuNAc alpha 2,6)GalNAc usually present in glycophorins A and B.
1421410	8	55	dep	glycophorins	1518:1529	arg1	A					1531:1531	A	1531:1531	A	1531:1531	The results show that Tn glycophorins from both donors contain intact and truncated forms of trisaccharide and tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3- (NeuNAc alpha 2,6)GalNAc usually present in glycophorins A and B.
1421410	9	56	theme	major	1654:1658	arg1	isomer					1660:1665	major isomer	1654:1665	major isomer	1654:1665	The truncated forms include the protein O-linked monosaccharide, GalNAc and disaccharide, NeuNAc alpha 2,6GalNAc (major isomer).
1421410	9	56	theme	major	1654:1658	arg1	2,6GalNAc					1643:1651	NeuNAc alpha 2,6GalNAc	1630:1651	NeuNAc alpha 2,6GalNAc (major isomer)	1630:1666	The truncated forms include the protein O-linked monosaccharide, GalNAc and disaccharide, NeuNAc alpha 2,6GalNAc (major isomer).
1421410	8	57	theme	NeuNAc	1475:1480	arg1	1,3GalNAc					1430:1438	tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3-	1389:1472	1,3GalNAc	1430:1438	The results show that Tn glycophorins from both donors contain intact and truncated forms of trisaccharide and tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3- (NeuNAc alpha 2,6)GalNAc usually present in glycophorins A and B.
1421410	8	57	theme	NeuNAc	1475:1480	arg1	alpha					1482:1486	NeuNAc alpha 2,6	1475:1490	NeuNAc alpha 2,6	1475:1490	The results show that Tn glycophorins from both donors contain intact and truncated forms of trisaccharide and tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3- (NeuNAc alpha 2,6)GalNAc usually present in glycophorins A and B.
1421410	2	58	theme	N-acetyl	370:377	arg1	determinant					419:429	the sole serologic Tn determinant	397:429	the sole serologic Tn determinant	397:429	Early studies had indicated that O-linked N-acetyl galactosamine was the sole serologic Tn determinant, but more recently O-linked NeuNAc alpha 2, 6GalNAc also has been implicated as a Tn antigen (sialosyl-Tn).
1421410	2	58	theme	N-acetyl	370:377	arg1	galactosamine					379:391	O-linked N-acetyl galactosamine	361:391	O-linked N-acetyl galactosamine	361:391	Early studies had indicated that O-linked N-acetyl galactosamine was the sole serologic Tn determinant, but more recently O-linked NeuNAc alpha 2, 6GalNAc also has been implicated as a Tn antigen (sialosyl-Tn).
1421410	8	59	attach	present	1507:1513	arg1	glycophorins					1518:1529	glycophorins A and B	1518:1537	glycophorins A and B	1518:1537	The results show that Tn glycophorins from both donors contain intact and truncated forms of trisaccharide and tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3- (NeuNAc alpha 2,6)GalNAc usually present in glycophorins A and B.
1421410	8	59	attach	present	1507:1513	arg1	B					1537:1537	B	1537:1537	B	1537:1537	The results show that Tn glycophorins from both donors contain intact and truncated forms of trisaccharide and tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3- (NeuNAc alpha 2,6)GalNAc usually present in glycophorins A and B.
1421410	8	59	attach	present	1507:1513	arg2	trisaccharide					1371:1383	trisaccharide	1371:1383	trisaccharide	1371:1383	The results show that Tn glycophorins from both donors contain intact and truncated forms of trisaccharide and tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3- (NeuNAc alpha 2,6)GalNAc usually present in glycophorins A and B.
1421410	8	59	attach	present	1507:1513	arg1	A					1531:1531	A	1531:1531	A	1531:1531	The results show that Tn glycophorins from both donors contain intact and truncated forms of trisaccharide and tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3- (NeuNAc alpha 2,6)GalNAc usually present in glycophorins A and B.
1421410	11	60	theme	that	2034:2037	arg1	amount					1977:1982	the amount	1973:1982	the amount of the disaccharide	1973:2002	The proportion of the four species was not identical in glycophorins of these two donors but, in both, the truncated units predominated and the amount of the disaccharide was approximately one half of that of the monosaccharide.
1421410	11	60	theme	that	2034:2037	arg1	disaccharide					1991:2002	the disaccharide	1987:2002	the disaccharide	1987:2002	The proportion of the four species was not identical in glycophorins of these two donors but, in both, the truncated units predominated and the amount of the disaccharide was approximately one half of that of the monosaccharide.
1421410	11	60	theme	that	2034:2037	arg1	half					2026:2029	approximately one half	2008:2029	approximately one half of that of the monosaccharide	2008:2059	The proportion of the four species was not identical in glycophorins of these two donors but, in both, the truncated units predominated and the amount of the disaccharide was approximately one half of that of the monosaccharide.
1421410	9	61	theme	protein	1572:1578	arg1	2,6GalNAc					1643:1651	NeuNAc alpha 2,6GalNAc	1630:1651	NeuNAc alpha 2,6GalNAc (major isomer)	1630:1666	The truncated forms include the protein O-linked monosaccharide, GalNAc and disaccharide, NeuNAc alpha 2,6GalNAc (major isomer).
1421410	9	61	theme	protein	1572:1578	arg1	monosaccharide					1589:1602	the protein O-linked monosaccharide	1568:1602	the protein O-linked monosaccharide	1568:1602	The truncated forms include the protein O-linked monosaccharide, GalNAc and disaccharide, NeuNAc alpha 2,6GalNAc (major isomer).
1421410	8	62	theme	GalNAc	1492:1497	arg1	forms					1362:1366	intact and truncated forms	1341:1366	intact and truncated forms of trisaccharide and tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3- (NeuNAc alpha 2,6)GalNAc usually present in glycophorins A and B	1341:1537	The results show that Tn glycophorins from both donors contain intact and truncated forms of trisaccharide and tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3- (NeuNAc alpha 2,6)GalNAc usually present in glycophorins A and B.
1421410	2	63	theme	sole	401:404	arg1	determinant					419:429	the sole serologic Tn determinant	397:429	the sole serologic Tn determinant	397:429	Early studies had indicated that O-linked N-acetyl galactosamine was the sole serologic Tn determinant, but more recently O-linked NeuNAc alpha 2, 6GalNAc also has been implicated as a Tn antigen (sialosyl-Tn).
1421410	2	63	theme	sole	401:404	arg1	galactosamine					379:391	O-linked N-acetyl galactosamine	361:391	O-linked N-acetyl galactosamine	361:391	Early studies had indicated that O-linked N-acetyl galactosamine was the sole serologic Tn determinant, but more recently O-linked NeuNAc alpha 2, 6GalNAc also has been implicated as a Tn antigen (sialosyl-Tn).
1421410	6	64	theme	O-linked	937:944	arg1	oligosaccharides					946:961	O-linked oligosaccharides	937:961	O-linked oligosaccharides	937:961	O-linked oligosaccharides were obtained by beta-elimination in the presence of tritiated sodium borohydride.
1421410	4	65	dep	glycophorins	658:669	arg1	A					671:671	A	671:671	A	671:671	In this report we examine oligosaccharides of glycophorins A and B purified from Tn erythrocytes of two affected individuals to establish how N- and O-linked saccharides differ from normal.
1421410	4	65	dep	glycophorins	658:669	arg1	glycophorins					658:669	glycophorins A and B	658:677	glycophorins A and B purified from Tn erythrocytes of two affected individuals	658:735	In this report we examine oligosaccharides of glycophorins A and B purified from Tn erythrocytes of two affected individuals to establish how N- and O-linked saccharides differ from normal.
1421410	4	65	dep	glycophorins	658:669	arg1	B					677:677	B	677:677	B	677:677	In this report we examine oligosaccharides of glycophorins A and B purified from Tn erythrocytes of two affected individuals to establish how N- and O-linked saccharides differ from normal.
1421410	8	66	from	present	1507:1513	arg1	glycophorins					1518:1529	glycophorins A and B	1518:1537	glycophorins A and B	1518:1537	The results show that Tn glycophorins from both donors contain intact and truncated forms of trisaccharide and tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3- (NeuNAc alpha 2,6)GalNAc usually present in glycophorins A and B.
1421410	8	66	from	present	1507:1513	arg1	B					1537:1537	B	1537:1537	B	1537:1537	The results show that Tn glycophorins from both donors contain intact and truncated forms of trisaccharide and tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3- (NeuNAc alpha 2,6)GalNAc usually present in glycophorins A and B.
1421410	8	66	from	present	1507:1513	arg1	A					1531:1531	A	1531:1531	A	1531:1531	The results show that Tn glycophorins from both donors contain intact and truncated forms of trisaccharide and tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3- (NeuNAc alpha 2,6)GalNAc usually present in glycophorins A and B.
1421410	11	67	theme	donors	1915:1920	arg1	glycophorins					1889:1900	glycophorins	1889:1900	glycophorins of these two donors	1889:1920	The proportion of the four species was not identical in glycophorins of these two donors but, in both, the truncated units predominated and the amount of the disaccharide was approximately one half of that of the monosaccharide.
1421410	2	68	link	O-linked	361:368	arg1	determinant					419:429	the sole serologic Tn determinant	397:429	the sole serologic Tn determinant	397:429	Early studies had indicated that O-linked N-acetyl galactosamine was the sole serologic Tn determinant, but more recently O-linked NeuNAc alpha 2, 6GalNAc also has been implicated as a Tn antigen (sialosyl-Tn).
1421410	2	68	link	O-linked	361:368	arg1	galactosamine					379:391	O-linked N-acetyl galactosamine	361:391	O-linked N-acetyl galactosamine	361:391	Early studies had indicated that O-linked N-acetyl galactosamine was the sole serologic Tn determinant, but more recently O-linked NeuNAc alpha 2, 6GalNAc also has been implicated as a Tn antigen (sialosyl-Tn).
1421410	12	69	theme	GalNAc	2225:2230	arg1	transferase					2259:2269	a specific GalNAc protein alpha 2,6 sialosyl transferase	2214:2269	a specific GalNAc protein alpha 2,6 sialosyl transferase in Tn hematopoietic precursor cells	2214:2305	The data are consistent with alterations in UDPGal:GalNAc beta 1,3galactosyl transferase that may have multiple molecular origins and with induction of a specific GalNAc protein alpha 2,6 sialosyl transferase in Tn hematopoietic precursor cells.
1421410	1	70	theme	occurring	286:294	arg1	anti-Tn					296:302	the naturally occurring anti-Tn	272:302	the naturally occurring anti-Tn present in normal sera	272:325	Tn polyagglutinability syndrome is an acquired condition where erythrocytes express Tn neo-antigen and become susceptible to hemagglutination by the naturally occurring anti-Tn present in normal sera.
1421410	9	71	theme	O-linked	1580:1587	arg1	2,6GalNAc					1643:1651	NeuNAc alpha 2,6GalNAc	1630:1651	NeuNAc alpha 2,6GalNAc (major isomer)	1630:1666	The truncated forms include the protein O-linked monosaccharide, GalNAc and disaccharide, NeuNAc alpha 2,6GalNAc (major isomer).
1421410	9	71	theme	O-linked	1580:1587	arg1	monosaccharide					1589:1602	the protein O-linked monosaccharide	1568:1602	the protein O-linked monosaccharide	1568:1602	The truncated forms include the protein O-linked monosaccharide, GalNAc and disaccharide, NeuNAc alpha 2,6GalNAc (major isomer).
1421410	4	72	theme	glycophorins	658:669	arg1	oligosaccharides					638:653	oligosaccharides	638:653	oligosaccharides of glycophorins A and B purified from Tn erythrocytes of two affected individuals	638:735	In this report we examine oligosaccharides of glycophorins A and B purified from Tn erythrocytes of two affected individuals to establish how N- and O-linked saccharides differ from normal.
1421410	1	73	from	present	304:310	arg1	sera					322:325	normal sera	315:325	normal sera	315:325	Tn polyagglutinability syndrome is an acquired condition where erythrocytes express Tn neo-antigen and become susceptible to hemagglutination by the naturally occurring anti-Tn present in normal sera.
1421410	3	74	theme	studies	562:568	arg1	none					548:551	none	548:551	none of these studies	548:568	However, none of these studies were performed on purified glycoproteins.
1421410	12	75	from	transferase	2259:2269	arg1	cells					2301:2305	Tn hematopoietic precursor cells	2274:2305	Tn hematopoietic precursor cells	2274:2305	The data are consistent with alterations in UDPGal:GalNAc beta 1,3galactosyl transferase that may have multiple molecular origins and with induction of a specific GalNAc protein alpha 2,6 sialosyl transferase in Tn hematopoietic precursor cells.
1421410	5	76	theme	Asn-linked	886:895	arg1	unit					897:900	the Asn-linked unit	882:900	the Asn-linked unit of glycophorin A	882:917	Analysis of carbohydrate composition and treatment with N-glycanase showed that the Asn-linked unit of glycophorin A was not affected.
1421410	12	77	contain	have	2160:2163	arg1	transferase					2139:2149	GalNAc beta 1,3galactosyl transferase	2113:2149	UDPGal:GalNAc beta 1,3galactosyl transferase that may have multiple molecular origins	2106:2190	The data are consistent with alterations in UDPGal:GalNAc beta 1,3galactosyl transferase that may have multiple molecular origins and with induction of a specific GalNAc protein alpha 2,6 sialosyl transferase in Tn hematopoietic precursor cells.
1421410	12	77	contain	have	2160:2163	arg2	origins					2184:2190	multiple molecular origins	2165:2190	multiple molecular origins	2165:2190	The data are consistent with alterations in UDPGal:GalNAc beta 1,3galactosyl transferase that may have multiple molecular origins and with induction of a specific GalNAc protein alpha 2,6 sialosyl transferase in Tn hematopoietic precursor cells.
1421410	12	78	theme	multiple	2165:2172	arg1	origins					2184:2190	multiple molecular origins	2165:2190	multiple molecular origins	2165:2190	The data are consistent with alterations in UDPGal:GalNAc beta 1,3galactosyl transferase that may have multiple molecular origins and with induction of a specific GalNAc protein alpha 2,6 sialosyl transferase in Tn hematopoietic precursor cells.
1421410	11	79	theme	species	1860:1866	arg1	identical					1876:1884	identical	1876:1884	identical	1876:1884	The proportion of the four species was not identical in glycophorins of these two donors but, in both, the truncated units predominated and the amount of the disaccharide was approximately one half of that of the monosaccharide.
1421410	11	79	theme	species	1860:1866	arg1	proportion					1837:1846	The proportion	1833:1846	The proportion of the four species	1833:1866	The proportion of the four species was not identical in glycophorins of these two donors but, in both, the truncated units predominated and the amount of the disaccharide was approximately one half of that of the monosaccharide.
1421410	2	80	theme	Early	328:332	arg1	studies					334:340	Early studies	328:340	Early studies	328:340	Early studies had indicated that O-linked N-acetyl galactosamine was the sole serologic Tn determinant, but more recently O-linked NeuNAc alpha 2, 6GalNAc also has been implicated as a Tn antigen (sialosyl-Tn).
1421410	5	81	theme	treatment	843:851	arg1	Analysis					802:809	Analysis	802:809	Analysis of carbohydrate composition and treatment with N-glycanase	802:868	Analysis of carbohydrate composition and treatment with N-glycanase showed that the Asn-linked unit of glycophorin A was not affected.
1421410	8	82	theme	present	1507:1513	arg1	trisaccharide					1371:1383	trisaccharide	1371:1383	trisaccharide	1371:1383	The results show that Tn glycophorins from both donors contain intact and truncated forms of trisaccharide and tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3- (NeuNAc alpha 2,6)GalNAc usually present in glycophorins A and B.
1421410	8	83	theme	tetrasaccharide	1389:1403	arg1	1,3GalNAc					1430:1438	tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3-	1389:1472	1,3GalNAc	1430:1438	The results show that Tn glycophorins from both donors contain intact and truncated forms of trisaccharide and tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3- (NeuNAc alpha 2,6)GalNAc usually present in glycophorins A and B.
1421410	8	83	theme	tetrasaccharide	1389:1403	arg1	alpha					1482:1486	NeuNAc alpha 2,6	1475:1490	NeuNAc alpha 2,6	1475:1490	The results show that Tn glycophorins from both donors contain intact and truncated forms of trisaccharide and tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3- (NeuNAc alpha 2,6)GalNAc usually present in glycophorins A and B.
1421410	12	84	theme	beta	2120:2123	arg1	transferase					2139:2149	GalNAc beta 1,3galactosyl transferase	2113:2149	UDPGal:GalNAc beta 1,3galactosyl transferase that may have multiple molecular origins	2106:2190	The data are consistent with alterations in UDPGal:GalNAc beta 1,3galactosyl transferase that may have multiple molecular origins and with induction of a specific GalNAc protein alpha 2,6 sialosyl transferase in Tn hematopoietic precursor cells.
1421410	7	85	theme	Bio-Gel	1101:1107	arg1	chromatography					1113:1126	Bio-Gel P-2 chromatography	1101:1126	Bio-Gel P-2 chromatography	1101:1126	The reduced radiolabeled products were fractionated by Bio-Gel P-2 chromatography, and their structures were investigated by comparison with standards, by monosaccharide quantification, and by neuraminidases of known specificities.
1421410	3	86	theme	purified	588:595	arg1	glycoproteins					597:609	purified glycoproteins	588:609	purified glycoproteins	588:609	However, none of these studies were performed on purified glycoproteins.
1421410	13	87	theme	further	2357:2363	arg1	study					2365:2369	further study	2357:2369	further study	2357:2369	The molecular basis for these alterations awaits further study.
1421410	7	88	theme	radiolabeled	1058:1069	arg1	products					1071:1078	The reduced radiolabeled products	1046:1078	The reduced radiolabeled products	1046:1078	The reduced radiolabeled products were fractionated by Bio-Gel P-2 chromatography, and their structures were investigated by comparison with standards, by monosaccharide quantification, and by neuraminidases of known specificities.
1421410	13	89	theme	molecular	2312:2320	arg1	basis					2322:2326	The molecular basis	2308:2326	The molecular basis for these alterations	2308:2348	The molecular basis for these alterations awaits further study.
1421410	1	90	theme	Tn	127:128	arg1	condition					174:182	an acquired condition	162:182	an acquired condition where erythrocytes express Tn neo-antigen and become susceptible to hemagglutination by the naturally occurring anti-Tn present in normal sera	162:325	Tn polyagglutinability syndrome is an acquired condition where erythrocytes express Tn neo-antigen and become susceptible to hemagglutination by the naturally occurring anti-Tn present in normal sera.
1421410	1	90	theme	Tn	127:128	arg1	syndrome					150:157	Tn polyagglutinability syndrome	127:157	Tn polyagglutinability syndrome	127:157	Tn polyagglutinability syndrome is an acquired condition where erythrocytes express Tn neo-antigen and become susceptible to hemagglutination by the naturally occurring anti-Tn present in normal sera.
1421410	8	91	theme	2,3Gal	1418:1423	arg1	1,3GalNAc					1430:1438	tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3-	1389:1472	1,3GalNAc	1430:1438	The results show that Tn glycophorins from both donors contain intact and truncated forms of trisaccharide and tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3- (NeuNAc alpha 2,6)GalNAc usually present in glycophorins A and B.
1421410	8	91	theme	2,3Gal	1418:1423	arg1	alpha					1482:1486	NeuNAc alpha 2,6	1475:1490	NeuNAc alpha 2,6	1475:1490	The results show that Tn glycophorins from both donors contain intact and truncated forms of trisaccharide and tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3- (NeuNAc alpha 2,6)GalNAc usually present in glycophorins A and B.
1421410	11	92	from	both	1930:1933	arg1	identical					1876:1884	identical	1876:1884	identical	1876:1884	The proportion of the four species was not identical in glycophorins of these two donors but, in both, the truncated units predominated and the amount of the disaccharide was approximately one half of that of the monosaccharide.
1421410	4	93	theme	affected	716:723	arg1	individuals					725:735	two affected individuals	712:735	two affected individuals	712:735	In this report we examine oligosaccharides of glycophorins A and B purified from Tn erythrocytes of two affected individuals to establish how N- and O-linked saccharides differ from normal.
1421410	8	94	from	glycophorins	1518:1529	arg1	present					1507:1513	present	1507:1513	present	1507:1513	The results show that Tn glycophorins from both donors contain intact and truncated forms of trisaccharide and tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3- (NeuNAc alpha 2,6)GalNAc usually present in glycophorins A and B.
1421410	12	95	theme	1,3galactosyl	2125:2137	arg1	transferase					2139:2149	GalNAc beta 1,3galactosyl transferase	2113:2149	UDPGal:GalNAc beta 1,3galactosyl transferase that may have multiple molecular origins	2106:2190	The data are consistent with alterations in UDPGal:GalNAc beta 1,3galactosyl transferase that may have multiple molecular origins and with induction of a specific GalNAc protein alpha 2,6 sialosyl transferase in Tn hematopoietic precursor cells.
1421410	8	96	theme	trisaccharide	1371:1383	arg1	forms					1362:1366	intact and truncated forms	1341:1366	intact and truncated forms of trisaccharide and tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3- (NeuNAc alpha 2,6)GalNAc usually present in glycophorins A and B	1341:1537	The results show that Tn glycophorins from both donors contain intact and truncated forms of trisaccharide and tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3- (NeuNAc alpha 2,6)GalNAc usually present in glycophorins A and B.
1421410	0	97	theme	individuals	73:83	arg1	erythrocytes					53:64	erythrocytes	53:64	erythrocytes of two individuals with the Tn polyagglutinability syndrome	53:124	O-linked oligosaccharides of glycophorins A and B in erythrocytes of two individuals with the Tn polyagglutinability syndrome.
1421410	5	98	theme	A	917:917	arg1	unit					897:900	the Asn-linked unit	882:900	the Asn-linked unit of glycophorin A	882:917	Analysis of carbohydrate composition and treatment with N-glycanase showed that the Asn-linked unit of glycophorin A was not affected.
1421410	6	99	theme	borohydride	1033:1043	arg1	presence					1004:1011	the presence	1000:1011	the presence of tritiated sodium borohydride	1000:1043	O-linked oligosaccharides were obtained by beta-elimination in the presence of tritiated sodium borohydride.
1421410	0	100	from	oligosaccharides	9:24	arg1	erythrocytes					53:64	erythrocytes	53:64	erythrocytes of two individuals with the Tn polyagglutinability syndrome	53:124	O-linked oligosaccharides of glycophorins A and B in erythrocytes of two individuals with the Tn polyagglutinability syndrome.
1421410	4	101	theme	Tn	693:694	arg1	erythrocytes					696:707	Tn erythrocytes	693:707	Tn erythrocytes of two affected individuals	693:735	In this report we examine oligosaccharides of glycophorins A and B purified from Tn erythrocytes of two affected individuals to establish how N- and O-linked saccharides differ from normal.
1421410	7	102	theme	known	1257:1261	arg1	specificities					1263:1275	known specificities	1257:1275	known specificities	1257:1275	The reduced radiolabeled products were fractionated by Bio-Gel P-2 chromatography, and their structures were investigated by comparison with standards, by monosaccharide quantification, and by neuraminidases of known specificities.
1421410	6	103	theme	tritiated	1016:1024	arg1	borohydride					1033:1043	tritiated sodium borohydride	1016:1043	tritiated sodium borohydride	1016:1043	O-linked oligosaccharides were obtained by beta-elimination in the presence of tritiated sodium borohydride.
1421410	12	104	theme	transferase	2259:2269	arg1	induction					2201:2209	induction	2201:2209	induction of a specific GalNAc protein alpha 2,6 sialosyl transferase in Tn hematopoietic precursor cells	2201:2305	The data are consistent with alterations in UDPGal:GalNAc beta 1,3galactosyl transferase that may have multiple molecular origins and with induction of a specific GalNAc protein alpha 2,6 sialosyl transferase in Tn hematopoietic precursor cells.
1421410	8	105	theme	alpha	1412:1416	arg1	1,3GalNAc					1430:1438	tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3-	1389:1472	1,3GalNAc	1430:1438	The results show that Tn glycophorins from both donors contain intact and truncated forms of trisaccharide and tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3- (NeuNAc alpha 2,6)GalNAc usually present in glycophorins A and B.
1421410	8	105	theme	alpha	1412:1416	arg1	alpha					1482:1486	NeuNAc alpha 2,6	1475:1490	NeuNAc alpha 2,6	1475:1490	The results show that Tn glycophorins from both donors contain intact and truncated forms of trisaccharide and tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3- (NeuNAc alpha 2,6)GalNAc usually present in glycophorins A and B.
1421410	0	106	theme	polyagglutinability	97:115	arg1	syndrome					117:124	the Tn polyagglutinability syndrome	90:124	the Tn polyagglutinability syndrome	90:124	O-linked oligosaccharides of glycophorins A and B in erythrocytes of two individuals with the Tn polyagglutinability syndrome.
1421410	5	107	link	Asn-linked	886:895	arg1	unit					897:900	the Asn-linked unit	882:900	the Asn-linked unit of glycophorin A	882:917	Analysis of carbohydrate composition and treatment with N-glycanase showed that the Asn-linked unit of glycophorin A was not affected.
1421410	11	108	from	glycophorins	1889:1900	arg1	identical					1876:1884	identical	1876:1884	identical	1876:1884	The proportion of the four species was not identical in glycophorins of these two donors but, in both, the truncated units predominated and the amount of the disaccharide was approximately one half of that of the monosaccharide.
1421410	11	108	from	glycophorins	1889:1900	arg1	proportion					1837:1846	The proportion	1833:1846	The proportion of the four species	1833:1866	The proportion of the four species was not identical in glycophorins of these two donors but, in both, the truncated units predominated and the amount of the disaccharide was approximately one half of that of the monosaccharide.
1421410	8	109	theme	beta	1425:1428	arg1	1,3GalNAc					1430:1438	tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3-	1389:1472	1,3GalNAc	1430:1438	The results show that Tn glycophorins from both donors contain intact and truncated forms of trisaccharide and tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3- (NeuNAc alpha 2,6)GalNAc usually present in glycophorins A and B.
1421410	8	109	theme	beta	1425:1428	arg1	alpha					1482:1486	NeuNAc alpha 2,6	1475:1490	NeuNAc alpha 2,6	1475:1490	The results show that Tn glycophorins from both donors contain intact and truncated forms of trisaccharide and tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3- (NeuNAc alpha 2,6)GalNAc usually present in glycophorins A and B.
1421410	11	110	theme	truncated	1940:1948	arg1	units					1950:1954	the truncated units	1936:1954	the truncated units	1936:1954	The proportion of the four species was not identical in glycophorins of these two donors but, in both, the truncated units predominated and the amount of the disaccharide was approximately one half of that of the monosaccharide.
1421410	12	111	theme	protein	2232:2238	arg1	transferase					2259:2269	a specific GalNAc protein alpha 2,6 sialosyl transferase	2214:2269	a specific GalNAc protein alpha 2,6 sialosyl transferase in Tn hematopoietic precursor cells	2214:2305	The data are consistent with alterations in UDPGal:GalNAc beta 1,3galactosyl transferase that may have multiple molecular origins and with induction of a specific GalNAc protein alpha 2,6 sialosyl transferase in Tn hematopoietic precursor cells.
1421410	2	112	theme	serologic	406:414	arg1	determinant					419:429	the sole serologic Tn determinant	397:429	the sole serologic Tn determinant	397:429	Early studies had indicated that O-linked N-acetyl galactosamine was the sole serologic Tn determinant, but more recently O-linked NeuNAc alpha 2, 6GalNAc also has been implicated as a Tn antigen (sialosyl-Tn).
1421410	2	112	theme	serologic	406:414	arg1	galactosamine					379:391	O-linked N-acetyl galactosamine	361:391	O-linked N-acetyl galactosamine	361:391	Early studies had indicated that O-linked N-acetyl galactosamine was the sole serologic Tn determinant, but more recently O-linked NeuNAc alpha 2, 6GalNAc also has been implicated as a Tn antigen (sialosyl-Tn).
1421410	0	113	theme	glycophorins	29:40	arg1	oligosaccharides					9:24	O-linked oligosaccharides	0:24	O-linked oligosaccharides of glycophorins A and B in erythrocytes of two individuals with the Tn polyagglutinability syndrome	0:124	O-linked oligosaccharides of glycophorins A and B in erythrocytes of two individuals with the Tn polyagglutinability syndrome.
1421410	9	114	link	O-linked	1580:1587	arg1	2,6GalNAc					1643:1651	NeuNAc alpha 2,6GalNAc	1630:1651	NeuNAc alpha 2,6GalNAc (major isomer)	1630:1666	The truncated forms include the protein O-linked monosaccharide, GalNAc and disaccharide, NeuNAc alpha 2,6GalNAc (major isomer).
1421410	9	114	link	O-linked	1580:1587	arg1	monosaccharide					1589:1602	the protein O-linked monosaccharide	1568:1602	the protein O-linked monosaccharide	1568:1602	The truncated forms include the protein O-linked monosaccharide, GalNAc and disaccharide, NeuNAc alpha 2,6GalNAc (major isomer).
1421410	9	115	theme	alpha	1637:1641	arg1	isomer					1660:1665	major isomer	1654:1665	major isomer	1654:1665	The truncated forms include the protein O-linked monosaccharide, GalNAc and disaccharide, NeuNAc alpha 2,6GalNAc (major isomer).
1421410	9	115	theme	alpha	1637:1641	arg1	monosaccharide					1589:1602	the protein O-linked monosaccharide	1568:1602	the protein O-linked monosaccharide	1568:1602	The truncated forms include the protein O-linked monosaccharide, GalNAc and disaccharide, NeuNAc alpha 2,6GalNAc (major isomer).
1421410	9	115	theme	alpha	1637:1641	arg1	2,6GalNAc					1643:1651	NeuNAc alpha 2,6GalNAc	1630:1651	NeuNAc alpha 2,6GalNAc (major isomer)	1630:1666	The truncated forms include the protein O-linked monosaccharide, GalNAc and disaccharide, NeuNAc alpha 2,6GalNAc (major isomer).
1421410	10	116	attach	presence	1673:1680	arg1	population					1713:1722	the total population	1703:1722	the total population of Tn erythrocytes	1703:1741	The presence of intact glycans in the total population of Tn erythrocytes was confirmed by their susceptibility to T activation after treatment with neuraminidase.
1421410	10	116	attach	presence	1673:1680	arg2	glycans					1692:1698	intact glycans	1685:1698	intact glycans	1685:1698	The presence of intact glycans in the total population of Tn erythrocytes was confirmed by their susceptibility to T activation after treatment with neuraminidase.
1421410	2	117	theme	NeuNAc	459:464	arg1	antigen					516:522	a Tn antigen	511:522	a Tn antigen (sialosyl-Tn)	511:536	Early studies had indicated that O-linked N-acetyl galactosamine was the sole serologic Tn determinant, but more recently O-linked NeuNAc alpha 2, 6GalNAc also has been implicated as a Tn antigen (sialosyl-Tn).
1421410	2	117	theme	NeuNAc	459:464	arg1	6GalNAc					475:481	O-linked NeuNAc alpha 2, 6GalNAc	450:481	6GalNAc	475:481	Early studies had indicated that O-linked N-acetyl galactosamine was the sole serologic Tn determinant, but more recently O-linked NeuNAc alpha 2, 6GalNAc also has been implicated as a Tn antigen (sialosyl-Tn).
1421410	12	118	theme	hematopoietic	2277:2289	arg1	cells					2301:2305	Tn hematopoietic precursor cells	2274:2305	Tn hematopoietic precursor cells	2274:2305	The data are consistent with alterations in UDPGal:GalNAc beta 1,3galactosyl transferase that may have multiple molecular origins and with induction of a specific GalNAc protein alpha 2,6 sialosyl transferase in Tn hematopoietic precursor cells.
1421410	8	119	theme	alpha	1451:1455	arg1	beta					1464:1467	tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3-	1389:1472	beta	1464:1467	The results show that Tn glycophorins from both donors contain intact and truncated forms of trisaccharide and tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3- (NeuNAc alpha 2,6)GalNAc usually present in glycophorins A and B.
1421410	10	120	theme	T	1784:1784	arg1	activation					1786:1795	T activation	1784:1795	T activation	1784:1795	The presence of intact glycans in the total population of Tn erythrocytes was confirmed by their susceptibility to T activation after treatment with neuraminidase.
1421410	12	121	from	cells	2301:2305	arg1	induction					2201:2209	induction	2201:2209	induction of a specific GalNAc protein alpha 2,6 sialosyl transferase in Tn hematopoietic precursor cells	2201:2305	The data are consistent with alterations in UDPGal:GalNAc beta 1,3galactosyl transferase that may have multiple molecular origins and with induction of a specific GalNAc protein alpha 2,6 sialosyl transferase in Tn hematopoietic precursor cells.
1421410	8	122	theme	beta	1464:1467	arg1	GalNAc					1492:1497	tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3- (NeuNAc alpha 2,6)GalNAc	1389:1497	tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3- (NeuNAc alpha 2,6)GalNAc	1389:1497	The results show that Tn glycophorins from both donors contain intact and truncated forms of trisaccharide and tetrasaccharide NeuNAc alpha 2,3Gal beta 1,3GalNAc and NeuNAc alpha 2,3Gal beta 1,3- (NeuNAc alpha 2,6)GalNAc usually present in glycophorins A and B.
1421410	10	123	theme	total	1707:1711	arg1	population					1713:1722	the total population	1703:1722	the total population of Tn erythrocytes	1703:1741	The presence of intact glycans in the total population of Tn erythrocytes was confirmed by their susceptibility to T activation after treatment with neuraminidase.
1421410	12	124	theme	specific	2216:2223	arg1	transferase					2259:2269	a specific GalNAc protein alpha 2,6 sialosyl transferase	2214:2269	a specific GalNAc protein alpha 2,6 sialosyl transferase in Tn hematopoietic precursor cells	2214:2305	The data are consistent with alterations in UDPGal:GalNAc beta 1,3galactosyl transferase that may have multiple molecular origins and with induction of a specific GalNAc protein alpha 2,6 sialosyl transferase in Tn hematopoietic precursor cells.
1421410	2	125	theme	O-linked	361:368	arg1	determinant					419:429	the sole serologic Tn determinant	397:429	the sole serologic Tn determinant	397:429	Early studies had indicated that O-linked N-acetyl galactosamine was the sole serologic Tn determinant, but more recently O-linked NeuNAc alpha 2, 6GalNAc also has been implicated as a Tn antigen (sialosyl-Tn).
1421410	2	125	theme	O-linked	361:368	arg1	galactosamine					379:391	O-linked N-acetyl galactosamine	361:391	O-linked N-acetyl galactosamine	361:391	Early studies had indicated that O-linked N-acetyl galactosamine was the sole serologic Tn determinant, but more recently O-linked NeuNAc alpha 2, 6GalNAc also has been implicated as a Tn antigen (sialosyl-Tn).
1421410	0	126	dep	glycophorins	29:40	arg1	glycophorins					29:40	glycophorins A and B	29:48	glycophorins A and B	29:48	O-linked oligosaccharides of glycophorins A and B in erythrocytes of two individuals with the Tn polyagglutinability syndrome.
1421410	0	126	dep	glycophorins	29:40	arg1	B					48:48	B	48:48	B	48:48	O-linked oligosaccharides of glycophorins A and B in erythrocytes of two individuals with the Tn polyagglutinability syndrome.
1421410	0	126	dep	glycophorins	29:40	arg1	A					42:42	A	42:42	A	42:42	O-linked oligosaccharides of glycophorins A and B in erythrocytes of two individuals with the Tn polyagglutinability syndrome.
1421410	11	127	theme	disaccharide	1991:2002	arg1	amount					1977:1982	the amount	1973:1982	the amount of the disaccharide	1973:2002	The proportion of the four species was not identical in glycophorins of these two donors but, in both, the truncated units predominated and the amount of the disaccharide was approximately one half of that of the monosaccharide.
1421410	11	127	theme	disaccharide	1991:2002	arg1	disaccharide					1991:2002	the disaccharide	1987:2002	the disaccharide	1987:2002	The proportion of the four species was not identical in glycophorins of these two donors but, in both, the truncated units predominated and the amount of the disaccharide was approximately one half of that of the monosaccharide.
1421410	11	127	theme	disaccharide	1991:2002	arg1	half					2026:2029	approximately one half	2008:2029	approximately one half of that of the monosaccharide	2008:2059	The proportion of the four species was not identical in glycophorins of these two donors but, in both, the truncated units predominated and the amount of the disaccharide was approximately one half of that of the monosaccharide.
1421410	4	128	link	O-linked	761:768	arg1	saccharides					770:780	O-linked saccharides	761:780	O-linked saccharides	761:780	In this report we examine oligosaccharides of glycophorins A and B purified from Tn erythrocytes of two affected individuals to establish how N- and O-linked saccharides differ from normal.
1421410	12	129	theme	Tn	2274:2275	arg1	cells					2301:2305	Tn hematopoietic precursor cells	2274:2305	Tn hematopoietic precursor cells	2274:2305	The data are consistent with alterations in UDPGal:GalNAc beta 1,3galactosyl transferase that may have multiple molecular origins and with induction of a specific GalNAc protein alpha 2,6 sialosyl transferase in Tn hematopoietic precursor cells.
1421410	2	130	link	O-linked	450:457	arg1	antigen					516:522	a Tn antigen	511:522	a Tn antigen (sialosyl-Tn)	511:536	Early studies had indicated that O-linked N-acetyl galactosamine was the sole serologic Tn determinant, but more recently O-linked NeuNAc alpha 2, 6GalNAc also has been implicated as a Tn antigen (sialosyl-Tn).
1421410	2	130	link	O-linked	450:457	arg1	6GalNAc					475:481	O-linked NeuNAc alpha 2, 6GalNAc	450:481	6GalNAc	475:481	Early studies had indicated that O-linked N-acetyl galactosamine was the sole serologic Tn determinant, but more recently O-linked NeuNAc alpha 2, 6GalNAc also has been implicated as a Tn antigen (sialosyl-Tn).
1421410	10	131	theme	erythrocytes	1730:1741	arg1	population					1713:1722	the total population	1703:1722	the total population of Tn erythrocytes	1703:1741	The presence of intact glycans in the total population of Tn erythrocytes was confirmed by their susceptibility to T activation after treatment with neuraminidase.
1421410	12	132	from	induction	2201:2209	arg1	cells					2301:2305	Tn hematopoietic precursor cells	2274:2305	Tn hematopoietic precursor cells	2274:2305	The data are consistent with alterations in UDPGal:GalNAc beta 1,3galactosyl transferase that may have multiple molecular origins and with induction of a specific GalNAc protein alpha 2,6 sialosyl transferase in Tn hematopoietic precursor cells.
3305497	12	0	theme	junction	2113:2120	arg1	region					2122:2127	the unique junction region	2102:2127	the unique junction region	2102:2127	The results suggest that the unique junction region may be characteristic of the Dantu phenotype.
3305497	12	0	theme	junction	2113:2120	arg1	characteristic					2136:2149	characteristic	2136:2149	characteristic of the Dantu phenotype	2136:2172	The results suggest that the unique junction region may be characteristic of the Dantu phenotype.
3305497	7	1	theme	delta-glycophorin	1303:1319	arg1	delta-glycophorin					1303:1319	delta-glycophorin	1303:1319	delta-glycophorin	1303:1319	Sequence analyses of a mixture of chymotryptic peptides of a CNBr fragment of the variant glycophorin identified the sequence Val-His-Arg-Phe-Thr-Val-Pro-Glu-Ile-Thr-Leu-Ile-Ile that contains the junction point of delta- and alpha-glycophorins spanning residues 33-38/39 of delta-glycophorin and residues 71/72-77 of alpha-glycophorin.
3305497	7	1	theme	delta-glycophorin	1303:1319	arg1	33-38/39					1291:1298	33-38/39	1291:1298	33-38/39	1291:1298	Sequence analyses of a mixture of chymotryptic peptides of a CNBr fragment of the variant glycophorin identified the sequence Val-His-Arg-Phe-Thr-Val-Pro-Glu-Ile-Thr-Leu-Ile-Ile that contains the junction point of delta- and alpha-glycophorins spanning residues 33-38/39 of delta-glycophorin and residues 71/72-77 of alpha-glycophorin.
3305497	4	2	theme	smaller	543:549	arg1	size					551:554	a smaller size	541:554	a smaller size	541:554	The variant glycophorin is of a smaller size, does not bind to Lens culinaris lectin agarose, and lacks residues approximately 40-60 of alpha-glycophorin and its single asparagine-linked carbohydrate; it contains approximately 2 less O-glycosidically bound units whose structures are identical to those found in alpha-glycophorins.
3305497	4	3	link	asparagine-linked	680:696	arg1	carbohydrate					698:709	its single asparagine-linked carbohydrate	669:709	its single asparagine-linked carbohydrate	669:709	The variant glycophorin is of a smaller size, does not bind to Lens culinaris lectin agarose, and lacks residues approximately 40-60 of alpha-glycophorin and its single asparagine-linked carbohydrate; it contains approximately 2 less O-glycosidically bound units whose structures are identical to those found in alpha-glycophorins.
3305497	7	4	theme	variant	1111:1117	arg1	glycophorin					1119:1129	the variant glycophorin	1107:1129	the variant glycophorin	1107:1129	Sequence analyses of a mixture of chymotryptic peptides of a CNBr fragment of the variant glycophorin identified the sequence Val-His-Arg-Phe-Thr-Val-Pro-Glu-Ile-Thr-Leu-Ile-Ile that contains the junction point of delta- and alpha-glycophorins spanning residues 33-38/39 of delta-glycophorin and residues 71/72-77 of alpha-glycophorin.
3305497	2	5	theme	glycophorin	286:296	arg1	alpha-glycophorin					267:283	a normal alpha-glycophorin	258:283	a normal alpha-glycophorin (glycophorin A)	258:299	Immunoblots indicated that erythrocytes of each individual contained a complement of a normal alpha-glycophorin (glycophorin A) and a variant N-glycophorin.
3305497	2	5	theme	glycophorin	286:296	arg1	A					298:298	glycophorin A	286:298	glycophorin A	286:298	Immunoblots indicated that erythrocytes of each individual contained a complement of a normal alpha-glycophorin (glycophorin A) and a variant N-glycophorin.
3305497	9	6	theme	variant	1532:1538	arg1	glycophorin					1546:1556	the variant Dantu glycophorin	1528:1556	the variant Dantu glycophorin when compared to alpha-glycophorin	1528:1591	The quantity of the variant Dantu glycophorin when compared to alpha-glycophorin differed in the two individuals, the ratio being 2/1 in one individual's cells and 0.5/1 in the other's.
3305497	11	7	theme	delta-alpha	1861:1871	arg1	glycophorin					1882:1892	a (delta-alpha) variant glycophorin	1858:1892	a (delta-alpha) variant glycophorin	1858:1892	Together, the evidence indicates that both donors' erythrocytes contain a (delta-alpha) variant glycophorin, whose amino terminus originates from delta-s-glycophorin and the carboxyl end from alpha-glycophorin with a junction point around residues 39 of delta- and 71 of alpha-glycophorins.
3305497	7	8	theme	CNBr	1090:1093	arg1	fragment					1095:1102	a CNBr fragment	1088:1102	a CNBr fragment of the variant glycophorin	1088:1129	Sequence analyses of a mixture of chymotryptic peptides of a CNBr fragment of the variant glycophorin identified the sequence Val-His-Arg-Phe-Thr-Val-Pro-Glu-Ile-Thr-Leu-Ile-Ile that contains the junction point of delta- and alpha-glycophorins spanning residues 33-38/39 of delta-glycophorin and residues 71/72-77 of alpha-glycophorin.
3305497	9	9	theme	glycophorin	1546:1556	arg1	quantity					1516:1523	The quantity	1512:1523	The quantity of the variant Dantu glycophorin when compared to alpha-glycophorin	1512:1591	The quantity of the variant Dantu glycophorin when compared to alpha-glycophorin differed in the two individuals, the ratio being 2/1 in one individual's cells and 0.5/1 in the other's.
3305497	4	10	theme	culinaris	579:587	arg1	agarose					596:602	Lens culinaris lectin agarose	574:602	Lens culinaris lectin agarose	574:602	The variant glycophorin is of a smaller size, does not bind to Lens culinaris lectin agarose, and lacks residues approximately 40-60 of alpha-glycophorin and its single asparagine-linked carbohydrate; it contains approximately 2 less O-glycosidically bound units whose structures are identical to those found in alpha-glycophorins.
3305497	6	11	theme	carboxyl-terminal	956:972	arg1	region					974:979	the carboxyl-terminal region	952:979	the carboxyl-terminal region	952:979	The variant is related to alpha-glycophorin in the carboxyl-terminal region as shown by reaction with a specific antiserum.
3305497	8	12	theme	Sequence	1365:1372	arg1	analysis					1374:1381	Sequence analysis	1365:1381	Sequence analysis of a mixture of CNBr fragments	1365:1412	Sequence analysis of a mixture of CNBr fragments allowed us to conclude that the variant originates from delta-s- rather than delta-S-glycophorin.
3305497	7	13	theme	chymotryptic	1063:1074	arg1	peptides					1076:1083	chymotryptic peptides	1063:1083	chymotryptic peptides of a CNBr fragment of the variant glycophorin	1063:1129	Sequence analyses of a mixture of chymotryptic peptides of a CNBr fragment of the variant glycophorin identified the sequence Val-His-Arg-Phe-Thr-Val-Pro-Glu-Ile-Thr-Leu-Ile-Ile that contains the junction point of delta- and alpha-glycophorins spanning residues 33-38/39 of delta-glycophorin and residues 71/72-77 of alpha-glycophorin.
3305497	11	14	theme	delta-	2040:2045	arg1	delta-					2040:2045	delta-	2040:2045	delta-	2040:2045	Together, the evidence indicates that both donors' erythrocytes contain a (delta-alpha) variant glycophorin, whose amino terminus originates from delta-s-glycophorin and the carboxyl end from alpha-glycophorin with a junction point around residues 39 of delta- and 71 of alpha-glycophorins.
3305497	11	14	theme	delta-	2040:2045	arg1	39					2034:2035	39	2034:2035	39	2034:2035	Together, the evidence indicates that both donors' erythrocytes contain a (delta-alpha) variant glycophorin, whose amino terminus originates from delta-s-glycophorin and the carboxyl end from alpha-glycophorin with a junction point around residues 39 of delta- and 71 of alpha-glycophorins.
3305497	11	15	theme	variant	1874:1880	arg1	glycophorin					1882:1892	a (delta-alpha) variant glycophorin	1858:1892	a (delta-alpha) variant glycophorin	1858:1892	Together, the evidence indicates that both donors' erythrocytes contain a (delta-alpha) variant glycophorin, whose amino terminus originates from delta-s-glycophorin and the carboxyl end from alpha-glycophorin with a junction point around residues 39 of delta- and 71 of alpha-glycophorins.
3305497	7	16	theme	mixture	1052:1058	arg1	analyses					1038:1045	Sequence analyses	1029:1045	Sequence analyses of a mixture of chymotryptic peptides of a CNBr fragment of the variant glycophorin	1029:1129	Sequence analyses of a mixture of chymotryptic peptides of a CNBr fragment of the variant glycophorin identified the sequence Val-His-Arg-Phe-Thr-Val-Pro-Glu-Ile-Thr-Leu-Ile-Ile that contains the junction point of delta- and alpha-glycophorins spanning residues 33-38/39 of delta-glycophorin and residues 71/72-77 of alpha-glycophorin.
3305497	6	17	with	reaction	993:1000	arg1	antiserum					1018:1026	a specific antiserum	1007:1026	a specific antiserum	1007:1026	The variant is related to alpha-glycophorin in the carboxyl-terminal region as shown by reaction with a specific antiserum.
3305497	8	18	theme	mixture	1388:1394	arg1	analysis					1374:1381	Sequence analysis	1365:1381	Sequence analysis of a mixture of CNBr fragments	1365:1412	Sequence analysis of a mixture of CNBr fragments allowed us to conclude that the variant originates from delta-s- rather than delta-S-glycophorin.
3305497	11	19	theme	alpha-glycophorins	2057:2074	arg1	71					2051:2052	71	2051:2052	71	2051:2052	Together, the evidence indicates that both donors' erythrocytes contain a (delta-alpha) variant glycophorin, whose amino terminus originates from delta-s-glycophorin and the carboxyl end from alpha-glycophorin with a junction point around residues 39 of delta- and 71 of alpha-glycophorins.
3305497	11	19	theme	alpha-glycophorins	2057:2074	arg1	alpha-glycophorins					2057:2074	alpha-glycophorins	2057:2074	alpha-glycophorins	2057:2074	Together, the evidence indicates that both donors' erythrocytes contain a (delta-alpha) variant glycophorin, whose amino terminus originates from delta-s-glycophorin and the carboxyl end from alpha-glycophorin with a junction point around residues 39 of delta- and 71 of alpha-glycophorins.
3305497	1	20	theme	blood	137:141	arg1	phenotype					149:157	the Dantu blood group phenotype	127:157	the Dantu blood group phenotype	127:157	Glycophorins of erythrocytes of two unrelated individuals who exhibit the Dantu blood group phenotype were studied.
3305497	4	21	theme	asparagine-linked	680:696	arg1	carbohydrate					698:709	its single asparagine-linked carbohydrate	669:709	its single asparagine-linked carbohydrate	669:709	The variant glycophorin is of a smaller size, does not bind to Lens culinaris lectin agarose, and lacks residues approximately 40-60 of alpha-glycophorin and its single asparagine-linked carbohydrate; it contains approximately 2 less O-glycosidically bound units whose structures are identical to those found in alpha-glycophorins.
3305497	3	22	theme	glycophorin	349:359	arg1	delta-Glycophorin					330:346	delta-Glycophorin	330:346	delta-Glycophorin (glycophorin B)	330:362	delta-Glycophorin (glycophorin B) was present in one donor's cells but not the other's; the s and N phenotypes of the latter's erythrocytes may derive from the variant glycophorin.
3305497	3	22	theme	glycophorin	349:359	arg1	B					361:361	glycophorin B	349:361	glycophorin B	349:361	delta-Glycophorin (glycophorin B) was present in one donor's cells but not the other's; the s and N phenotypes of the latter's erythrocytes may derive from the variant glycophorin.
3305497	8	23	theme	CNBr	1399:1402	arg1	fragments					1404:1412	CNBr fragments	1399:1412	CNBr fragments	1399:1412	Sequence analysis of a mixture of CNBr fragments allowed us to conclude that the variant originates from delta-s- rather than delta-S-glycophorin.
3305497	6	24	theme	specific	1009:1016	arg1	antiserum					1018:1026	a specific antiserum	1007:1026	a specific antiserum	1007:1026	The variant is related to alpha-glycophorin in the carboxyl-terminal region as shown by reaction with a specific antiserum.
3305497	4	25	theme	alpha-glycophorin	647:663	arg1	carbohydrate					698:709	its single asparagine-linked carbohydrate	669:709	its single asparagine-linked carbohydrate	669:709	The variant glycophorin is of a smaller size, does not bind to Lens culinaris lectin agarose, and lacks residues approximately 40-60 of alpha-glycophorin and its single asparagine-linked carbohydrate; it contains approximately 2 less O-glycosidically bound units whose structures are identical to those found in alpha-glycophorins.
3305497	4	25	theme	alpha-glycophorin	647:663	arg1	alpha-glycophorin					647:663	alpha-glycophorin	647:663	alpha-glycophorin	647:663	The variant glycophorin is of a smaller size, does not bind to Lens culinaris lectin agarose, and lacks residues approximately 40-60 of alpha-glycophorin and its single asparagine-linked carbohydrate; it contains approximately 2 less O-glycosidically bound units whose structures are identical to those found in alpha-glycophorins.
3305497	4	25	theme	alpha-glycophorin	647:663	arg1	residues					615:622	residues approximately 40-60	615:642	residues approximately 40-60 of alpha-glycophorin and its single asparagine-linked carbohydrate	615:709	The variant glycophorin is of a smaller size, does not bind to Lens culinaris lectin agarose, and lacks residues approximately 40-60 of alpha-glycophorin and its single asparagine-linked carbohydrate; it contains approximately 2 less O-glycosidically bound units whose structures are identical to those found in alpha-glycophorins.
3305497	7	26	theme	residues	1282:1289	arg1	point					1234:1238	the junction point	1221:1238	the junction point of delta- and alpha-glycophorins spanning residues 33-38/39 of delta-glycophorin and residues 71/72-77 of alpha-glycophorin	1221:1362	Sequence analyses of a mixture of chymotryptic peptides of a CNBr fragment of the variant glycophorin identified the sequence Val-His-Arg-Phe-Thr-Val-Pro-Glu-Ile-Thr-Leu-Ile-Ile that contains the junction point of delta- and alpha-glycophorins spanning residues 33-38/39 of delta-glycophorin and residues 71/72-77 of alpha-glycophorin.
3305497	2	27	theme	alpha-glycophorin	267:283	arg1	complement					244:253	a complement	242:253	a complement of a normal alpha-glycophorin (glycophorin A)	242:299	Immunoblots indicated that erythrocytes of each individual contained a complement of a normal alpha-glycophorin (glycophorin A) and a variant N-glycophorin.
3305497	2	27	theme	alpha-glycophorin	267:283	arg1	N-glycophorin					315:327	a variant N-glycophorin	305:327	a variant N-glycophorin	305:327	Immunoblots indicated that erythrocytes of each individual contained a complement of a normal alpha-glycophorin (glycophorin A) and a variant N-glycophorin.
3305497	7	28	theme	alpha-glycophorins	1254:1271	arg1	residues					1282:1289	delta- and alpha-glycophorins spanning residues	1243:1289	delta- and alpha-glycophorins spanning residues	1243:1289	Sequence analyses of a mixture of chymotryptic peptides of a CNBr fragment of the variant glycophorin identified the sequence Val-His-Arg-Phe-Thr-Val-Pro-Glu-Ile-Thr-Leu-Ile-Ile that contains the junction point of delta- and alpha-glycophorins spanning residues 33-38/39 of delta-glycophorin and residues 71/72-77 of alpha-glycophorin.
3305497	7	28	theme	alpha-glycophorins	1254:1271	arg1	alpha-glycophorin					1346:1362	alpha-glycophorin	1346:1362	alpha-glycophorin	1346:1362	Sequence analyses of a mixture of chymotryptic peptides of a CNBr fragment of the variant glycophorin identified the sequence Val-His-Arg-Phe-Thr-Val-Pro-Glu-Ile-Thr-Leu-Ile-Ile that contains the junction point of delta- and alpha-glycophorins spanning residues 33-38/39 of delta-glycophorin and residues 71/72-77 of alpha-glycophorin.
3305497	12	29	theme	Dantu	2158:2162	arg1	phenotype					2164:2172	the Dantu phenotype	2154:2172	the Dantu phenotype	2154:2172	The results suggest that the unique junction region may be characteristic of the Dantu phenotype.
3305497	9	30	dep	differed	1593:1600	arg1	0.5/1					1676:1680	0.5/1	1676:1680	0.5/1 in the other's	1676:1695	The quantity of the variant Dantu glycophorin when compared to alpha-glycophorin differed in the two individuals, the ratio being 2/1 in one individual's cells and 0.5/1 in the other's.
3305497	9	30	dep	differed	1593:1600	arg1	2/1					1642:1644	2/1	1642:1644	2/1 in one individual's cells	1642:1670	The quantity of the variant Dantu glycophorin when compared to alpha-glycophorin differed in the two individuals, the ratio being 2/1 in one individual's cells and 0.5/1 in the other's.
3305497	9	30	dep	differed	1593:1600	arg1	ratio					1630:1634	the ratio	1626:1634	the ratio	1626:1634	The quantity of the variant Dantu glycophorin when compared to alpha-glycophorin differed in the two individuals, the ratio being 2/1 in one individual's cells and 0.5/1 in the other's.
3305497	7	31	theme	delta-	1243:1248	arg1	residues					1282:1289	delta- and alpha-glycophorins spanning residues	1243:1289	delta- and alpha-glycophorins spanning residues	1243:1289	Sequence analyses of a mixture of chymotryptic peptides of a CNBr fragment of the variant glycophorin identified the sequence Val-His-Arg-Phe-Thr-Val-Pro-Glu-Ile-Thr-Leu-Ile-Ile that contains the junction point of delta- and alpha-glycophorins spanning residues 33-38/39 of delta-glycophorin and residues 71/72-77 of alpha-glycophorin.
3305497	7	31	theme	delta-	1243:1248	arg1	alpha-glycophorin					1346:1362	alpha-glycophorin	1346:1362	alpha-glycophorin	1346:1362	Sequence analyses of a mixture of chymotryptic peptides of a CNBr fragment of the variant glycophorin identified the sequence Val-His-Arg-Phe-Thr-Val-Pro-Glu-Ile-Thr-Leu-Ile-Ile that contains the junction point of delta- and alpha-glycophorins spanning residues 33-38/39 of delta-glycophorin and residues 71/72-77 of alpha-glycophorin.
3305497	0	32	theme	Membrane	0:7	arg1	glycophorins					9:20	Membrane glycophorins	0:20	Membrane glycophorins of Dantu blood group erythrocytes	0:54	Membrane glycophorins of Dantu blood group erythrocytes.
3305497	1	33	theme	unrelated	93:101	arg1	individuals					103:113	two unrelated individuals	89:113	two unrelated individuals who exhibit the Dantu blood group phenotype	89:157	Glycophorins of erythrocytes of two unrelated individuals who exhibit the Dantu blood group phenotype were studied.
3305497	3	34	theme	one	379:381	arg1	cells					391:395	one donor's cells	379:395	one donor's cells but not the other's	379:415	delta-Glycophorin (glycophorin B) was present in one donor's cells but not the other's; the s and N phenotypes of the latter's erythrocytes may derive from the variant glycophorin.
3305497	4	35	theme	variant	515:521	arg1	glycophorin					523:533	The variant glycophorin	511:533	The variant glycophorin	511:533	The variant glycophorin is of a smaller size, does not bind to Lens culinaris lectin agarose, and lacks residues approximately 40-60 of alpha-glycophorin and its single asparagine-linked carbohydrate; it contains approximately 2 less O-glycosidically bound units whose structures are identical to those found in alpha-glycophorins.
3305497	10	36	theme	different	1745:1753	arg1	varieties					1755:1763	different varieties	1745:1763	different varieties of Dantu phenotypes	1745:1783	This may reflect that the two donors belong to different varieties of Dantu phenotypes.
3305497	10	36	theme	different	1745:1753	arg1	phenotypes					1774:1783	Dantu phenotypes	1768:1783	Dantu phenotypes	1768:1783	This may reflect that the two donors belong to different varieties of Dantu phenotypes.
3305497	9	37	from	0.5/1	1676:1680	arg1	cells					1666:1670	one individual's cells	1649:1670	one individual's cells	1649:1670	The quantity of the variant Dantu glycophorin when compared to alpha-glycophorin differed in the two individuals, the ratio being 2/1 in one individual's cells and 0.5/1 in the other's.
3305497	9	37	from	0.5/1	1676:1680	arg1	's					1694:1695	the other's	1685:1695	the other's	1685:1695	The quantity of the variant Dantu glycophorin when compared to alpha-glycophorin differed in the two individuals, the ratio being 2/1 in one individual's cells and 0.5/1 in the other's.
3305497	0	38	theme	blood	31:35	arg1	erythrocytes					43:54	Dantu blood group erythrocytes	25:54	Dantu blood group erythrocytes	25:54	Membrane glycophorins of Dantu blood group erythrocytes.
3305497	6	39	from	alpha-glycophorin	931:947	arg1	region					974:979	the carboxyl-terminal region	952:979	the carboxyl-terminal region	952:979	The variant is related to alpha-glycophorin in the carboxyl-terminal region as shown by reaction with a specific antiserum.
3305497	10	40	theme	phenotypes	1774:1783	arg1	varieties					1755:1763	different varieties	1745:1763	different varieties of Dantu phenotypes	1745:1783	This may reflect that the two donors belong to different varieties of Dantu phenotypes.
3305497	10	40	theme	phenotypes	1774:1783	arg1	phenotypes					1774:1783	Dantu phenotypes	1768:1783	Dantu phenotypes	1768:1783	This may reflect that the two donors belong to different varieties of Dantu phenotypes.
3305497	7	41	theme	sequence	1146:1153	arg1	Val-His-Arg-Phe-Thr-Val-Pro-Glu-Ile-Thr-Leu-Ile-Ile					1155:1205	the sequence Val-His-Arg-Phe-Thr-Val-Pro-Glu-Ile-Thr-Leu-Ile-Ile	1142:1205	the sequence Val-His-Arg-Phe-Thr-Val-Pro-Glu-Ile-Thr-Leu-Ile-Ile that contains the junction point of delta- and alpha-glycophorins spanning residues 33-38/39 of delta-glycophorin and residues 71/72-77 of alpha-glycophorin	1142:1362	Sequence analyses of a mixture of chymotryptic peptides of a CNBr fragment of the variant glycophorin identified the sequence Val-His-Arg-Phe-Thr-Val-Pro-Glu-Ile-Thr-Leu-Ile-Ile that contains the junction point of delta- and alpha-glycophorins spanning residues 33-38/39 of delta-glycophorin and residues 71/72-77 of alpha-glycophorin.
3305497	9	42	theme	other	1689:1693	arg1	's					1694:1695	the other's	1685:1695	the other's	1685:1695	The quantity of the variant Dantu glycophorin when compared to alpha-glycophorin differed in the two individuals, the ratio being 2/1 in one individual's cells and 0.5/1 in the other's.
3305497	11	43	theme	amino	1901:1905	arg1	terminus					1907:1914	terminus	1907:1914	terminus	1907:1914	Together, the evidence indicates that both donors' erythrocytes contain a (delta-alpha) variant glycophorin, whose amino terminus originates from delta-s-glycophorin and the carboxyl end from alpha-glycophorin with a junction point around residues 39 of delta- and 71 of alpha-glycophorins.
3305497	2	44	contain	contained	232:240	arg2	N-glycophorin					315:327	a variant N-glycophorin	305:327	a variant N-glycophorin	305:327	Immunoblots indicated that erythrocytes of each individual contained a complement of a normal alpha-glycophorin (glycophorin A) and a variant N-glycophorin.
3305497	2	44	contain	contained	232:240	arg1	erythrocytes					200:211	erythrocytes	200:211	erythrocytes of each individual	200:230	Immunoblots indicated that erythrocytes of each individual contained a complement of a normal alpha-glycophorin (glycophorin A) and a variant N-glycophorin.
3305497	2	44	contain	contained	232:240	arg2	complement					244:253	a complement	242:253	a complement of a normal alpha-glycophorin (glycophorin A)	242:299	Immunoblots indicated that erythrocytes of each individual contained a complement of a normal alpha-glycophorin (glycophorin A) and a variant N-glycophorin.
3305497	7	45	theme	alpha-glycophorin	1346:1362	arg1	residues					1325:1332	residues	1325:1332	residues	1325:1332	Sequence analyses of a mixture of chymotryptic peptides of a CNBr fragment of the variant glycophorin identified the sequence Val-His-Arg-Phe-Thr-Val-Pro-Glu-Ile-Thr-Leu-Ile-Ile that contains the junction point of delta- and alpha-glycophorins spanning residues 33-38/39 of delta-glycophorin and residues 71/72-77 of alpha-glycophorin.
3305497	7	45	theme	alpha-glycophorin	1346:1362	arg1	residues					1282:1289	delta- and alpha-glycophorins spanning residues	1243:1289	delta- and alpha-glycophorins spanning residues	1243:1289	Sequence analyses of a mixture of chymotryptic peptides of a CNBr fragment of the variant glycophorin identified the sequence Val-His-Arg-Phe-Thr-Val-Pro-Glu-Ile-Thr-Leu-Ile-Ile that contains the junction point of delta- and alpha-glycophorins spanning residues 33-38/39 of delta-glycophorin and residues 71/72-77 of alpha-glycophorin.
3305497	7	45	theme	alpha-glycophorin	1346:1362	arg1	alpha-glycophorin					1346:1362	alpha-glycophorin	1346:1362	alpha-glycophorin	1346:1362	Sequence analyses of a mixture of chymotryptic peptides of a CNBr fragment of the variant glycophorin identified the sequence Val-His-Arg-Phe-Thr-Val-Pro-Glu-Ile-Thr-Leu-Ile-Ile that contains the junction point of delta- and alpha-glycophorins spanning residues 33-38/39 of delta-glycophorin and residues 71/72-77 of alpha-glycophorin.
3305497	3	46	theme	N	428:428	arg1	phenotypes					430:439	the s and N phenotypes	418:439	the s and N phenotypes of the latter's erythrocytes	418:468	delta-Glycophorin (glycophorin B) was present in one donor's cells but not the other's; the s and N phenotypes of the latter's erythrocytes may derive from the variant glycophorin.
3305497	4	47	located	found	814:818	arg1	alpha-glycophorins					823:840	alpha-glycophorins	823:840	alpha-glycophorins	823:840	The variant glycophorin is of a smaller size, does not bind to Lens culinaris lectin agarose, and lacks residues approximately 40-60 of alpha-glycophorin and its single asparagine-linked carbohydrate; it contains approximately 2 less O-glycosidically bound units whose structures are identical to those found in alpha-glycophorins.
3305497	4	47	located	found	814:818	arg2	those					808:812	those	808:812	those	808:812	The variant glycophorin is of a smaller size, does not bind to Lens culinaris lectin agarose, and lacks residues approximately 40-60 of alpha-glycophorin and its single asparagine-linked carbohydrate; it contains approximately 2 less O-glycosidically bound units whose structures are identical to those found in alpha-glycophorins.
3305497	7	48	theme	glycophorin	1119:1129	arg1	fragment					1095:1102	a CNBr fragment	1088:1102	a CNBr fragment of the variant glycophorin	1088:1129	Sequence analyses of a mixture of chymotryptic peptides of a CNBr fragment of the variant glycophorin identified the sequence Val-His-Arg-Phe-Thr-Val-Pro-Glu-Ile-Thr-Leu-Ile-Ile that contains the junction point of delta- and alpha-glycophorins spanning residues 33-38/39 of delta-glycophorin and residues 71/72-77 of alpha-glycophorin.
3305497	12	49	theme	unique	2106:2111	arg1	region					2122:2127	the unique junction region	2102:2127	the unique junction region	2102:2127	The results suggest that the unique junction region may be characteristic of the Dantu phenotype.
3305497	12	49	theme	unique	2106:2111	arg1	characteristic					2136:2149	characteristic	2136:2149	characteristic of the Dantu phenotype	2136:2172	The results suggest that the unique junction region may be characteristic of the Dantu phenotype.
3305497	11	50	contain	contain	1850:1856	arg2	glycophorin					1882:1892	a (delta-alpha) variant glycophorin	1858:1892	a (delta-alpha) variant glycophorin	1858:1892	Together, the evidence indicates that both donors' erythrocytes contain a (delta-alpha) variant glycophorin, whose amino terminus originates from delta-s-glycophorin and the carboxyl end from alpha-glycophorin with a junction point around residues 39 of delta- and 71 of alpha-glycophorins.
3305497	11	50	contain	contain	1850:1856	arg1	erythrocytes					1837:1848	both donors' erythrocytes	1824:1848	both donors' erythrocytes	1824:1848	Together, the evidence indicates that both donors' erythrocytes contain a (delta-alpha) variant glycophorin, whose amino terminus originates from delta-s-glycophorin and the carboxyl end from alpha-glycophorin with a junction point around residues 39 of delta- and 71 of alpha-glycophorins.
3305497	7	51	theme	fragment	1095:1102	arg1	peptides					1076:1083	chymotryptic peptides	1063:1083	chymotryptic peptides of a CNBr fragment of the variant glycophorin	1063:1129	Sequence analyses of a mixture of chymotryptic peptides of a CNBr fragment of the variant glycophorin identified the sequence Val-His-Arg-Phe-Thr-Val-Pro-Glu-Ile-Thr-Leu-Ile-Ile that contains the junction point of delta- and alpha-glycophorins spanning residues 33-38/39 of delta-glycophorin and residues 71/72-77 of alpha-glycophorin.
3305497	3	52	theme	variant	490:496	arg1	glycophorin					498:508	the variant glycophorin	486:508	the variant glycophorin	486:508	delta-Glycophorin (glycophorin B) was present in one donor's cells but not the other's; the s and N phenotypes of the latter's erythrocytes may derive from the variant glycophorin.
3305497	4	53	dep	units	768:772	arg1	bound					762:766	bound	762:766	bound	762:766	The variant glycophorin is of a smaller size, does not bind to Lens culinaris lectin agarose, and lacks residues approximately 40-60 of alpha-glycophorin and its single asparagine-linked carbohydrate; it contains approximately 2 less O-glycosidically bound units whose structures are identical to those found in alpha-glycophorins.
3305497	11	54	dep	residues	2025:2032	arg1	delta-					2040:2045	delta-	2040:2045	delta-	2040:2045	Together, the evidence indicates that both donors' erythrocytes contain a (delta-alpha) variant glycophorin, whose amino terminus originates from delta-s-glycophorin and the carboxyl end from alpha-glycophorin with a junction point around residues 39 of delta- and 71 of alpha-glycophorins.
3305497	11	54	dep	residues	2025:2032	arg1	39					2034:2035	39	2034:2035	39	2034:2035	Together, the evidence indicates that both donors' erythrocytes contain a (delta-alpha) variant glycophorin, whose amino terminus originates from delta-s-glycophorin and the carboxyl end from alpha-glycophorin with a junction point around residues 39 of delta- and 71 of alpha-glycophorins.
3305497	0	55	theme	erythrocytes	43:54	arg1	glycophorins					9:20	Membrane glycophorins	0:20	Membrane glycophorins of Dantu blood group erythrocytes	0:54	Membrane glycophorins of Dantu blood group erythrocytes.
3305497	7	56	contain	contains	1212:1219	arg1	Val-His-Arg-Phe-Thr-Val-Pro-Glu-Ile-Thr-Leu-Ile-Ile					1155:1205	the sequence Val-His-Arg-Phe-Thr-Val-Pro-Glu-Ile-Thr-Leu-Ile-Ile	1142:1205	the sequence Val-His-Arg-Phe-Thr-Val-Pro-Glu-Ile-Thr-Leu-Ile-Ile that contains the junction point of delta- and alpha-glycophorins spanning residues 33-38/39 of delta-glycophorin and residues 71/72-77 of alpha-glycophorin	1142:1362	Sequence analyses of a mixture of chymotryptic peptides of a CNBr fragment of the variant glycophorin identified the sequence Val-His-Arg-Phe-Thr-Val-Pro-Glu-Ile-Thr-Leu-Ile-Ile that contains the junction point of delta- and alpha-glycophorins spanning residues 33-38/39 of delta-glycophorin and residues 71/72-77 of alpha-glycophorin.
3305497	7	56	contain	contains	1212:1219	arg2	point					1234:1238	the junction point	1221:1238	the junction point of delta- and alpha-glycophorins spanning residues 33-38/39 of delta-glycophorin and residues 71/72-77 of alpha-glycophorin	1221:1362	Sequence analyses of a mixture of chymotryptic peptides of a CNBr fragment of the variant glycophorin identified the sequence Val-His-Arg-Phe-Thr-Val-Pro-Glu-Ile-Thr-Leu-Ile-Ile that contains the junction point of delta- and alpha-glycophorins spanning residues 33-38/39 of delta-glycophorin and residues 71/72-77 of alpha-glycophorin.
3305497	9	57	theme	Dantu	1540:1544	arg1	glycophorin					1546:1556	the variant Dantu glycophorin	1528:1556	the variant Dantu glycophorin when compared to alpha-glycophorin	1528:1591	The quantity of the variant Dantu glycophorin when compared to alpha-glycophorin differed in the two individuals, the ratio being 2/1 in one individual's cells and 0.5/1 in the other's.
3305497	4	58	contain	contains	715:722	arg1	it					712:713	it	712:713	it	712:713	The variant glycophorin is of a smaller size, does not bind to Lens culinaris lectin agarose, and lacks residues approximately 40-60 of alpha-glycophorin and its single asparagine-linked carbohydrate; it contains approximately 2 less O-glycosidically bound units whose structures are identical to those found in alpha-glycophorins.
3305497	4	58	contain	contains	715:722	arg2	units					768:772	approximately 2 less O-glycosidically bound units whose structures are identical to those found in alpha-glycophorins	724:840	approximately 2 less O-glycosidically bound units whose structures are identical to those found in alpha-glycophorins	724:840	The variant glycophorin is of a smaller size, does not bind to Lens culinaris lectin agarose, and lacks residues approximately 40-60 of alpha-glycophorin and its single asparagine-linked carbohydrate; it contains approximately 2 less O-glycosidically bound units whose structures are identical to those found in alpha-glycophorins.
3305497	7	59	theme	peptides	1076:1083	arg1	mixture					1052:1058	a mixture	1050:1058	a mixture of chymotryptic peptides of a CNBr fragment of the variant glycophorin	1050:1129	Sequence analyses of a mixture of chymotryptic peptides of a CNBr fragment of the variant glycophorin identified the sequence Val-His-Arg-Phe-Thr-Val-Pro-Glu-Ile-Thr-Leu-Ile-Ile that contains the junction point of delta- and alpha-glycophorins spanning residues 33-38/39 of delta-glycophorin and residues 71/72-77 of alpha-glycophorin.
3305497	2	60	theme	variant	307:313	arg1	N-glycophorin					315:327	a variant N-glycophorin	305:327	a variant N-glycophorin	305:327	Immunoblots indicated that erythrocytes of each individual contained a complement of a normal alpha-glycophorin (glycophorin A) and a variant N-glycophorin.
3305497	4	61	theme	Lens	574:577	arg1	agarose					596:602	Lens culinaris lectin agarose	574:602	Lens culinaris lectin agarose	574:602	The variant glycophorin is of a smaller size, does not bind to Lens culinaris lectin agarose, and lacks residues approximately 40-60 of alpha-glycophorin and its single asparagine-linked carbohydrate; it contains approximately 2 less O-glycosidically bound units whose structures are identical to those found in alpha-glycophorins.
3305497	3	62	theme	erythrocytes	457:468	arg1	phenotypes					430:439	the s and N phenotypes	418:439	the s and N phenotypes of the latter's erythrocytes	418:468	delta-Glycophorin (glycophorin B) was present in one donor's cells but not the other's; the s and N phenotypes of the latter's erythrocytes may derive from the variant glycophorin.
3305497	4	63	dep	bound	762:766	arg1	2					738:738	2	738:738	2	738:738	The variant glycophorin is of a smaller size, does not bind to Lens culinaris lectin agarose, and lacks residues approximately 40-60 of alpha-glycophorin and its single asparagine-linked carbohydrate; it contains approximately 2 less O-glycosidically bound units whose structures are identical to those found in alpha-glycophorins.
3305497	4	64	theme	lectin	589:594	arg1	agarose					596:602	Lens culinaris lectin agarose	574:602	Lens culinaris lectin agarose	574:602	The variant glycophorin is of a smaller size, does not bind to Lens culinaris lectin agarose, and lacks residues approximately 40-60 of alpha-glycophorin and its single asparagine-linked carbohydrate; it contains approximately 2 less O-glycosidically bound units whose structures are identical to those found in alpha-glycophorins.
3305497	7	65	theme	Sequence	1029:1036	arg1	analyses					1038:1045	Sequence analyses	1029:1045	Sequence analyses of a mixture of chymotryptic peptides of a CNBr fragment of the variant glycophorin	1029:1129	Sequence analyses of a mixture of chymotryptic peptides of a CNBr fragment of the variant glycophorin identified the sequence Val-His-Arg-Phe-Thr-Val-Pro-Glu-Ile-Thr-Leu-Ile-Ile that contains the junction point of delta- and alpha-glycophorins spanning residues 33-38/39 of delta-glycophorin and residues 71/72-77 of alpha-glycophorin.
3305497	11	66	with	alpha-glycophorin	1978:1994	arg1	point					2012:2016	a junction point	2001:2016	a junction point around residues 39 of delta- and 71 of alpha-glycophorins	2001:2074	Together, the evidence indicates that both donors' erythrocytes contain a (delta-alpha) variant glycophorin, whose amino terminus originates from delta-s-glycophorin and the carboxyl end from alpha-glycophorin with a junction point around residues 39 of delta- and 71 of alpha-glycophorins.
3305497	1	67	theme	Dantu	131:135	arg1	phenotype					149:157	the Dantu blood group phenotype	127:157	the Dantu blood group phenotype	127:157	Glycophorins of erythrocytes of two unrelated individuals who exhibit the Dantu blood group phenotype were studied.
3305497	4	68	theme	single	673:678	arg1	carbohydrate					698:709	its single asparagine-linked carbohydrate	669:709	its single asparagine-linked carbohydrate	669:709	The variant glycophorin is of a smaller size, does not bind to Lens culinaris lectin agarose, and lacks residues approximately 40-60 of alpha-glycophorin and its single asparagine-linked carbohydrate; it contains approximately 2 less O-glycosidically bound units whose structures are identical to those found in alpha-glycophorins.
3305497	2	69	theme	normal	260:265	arg1	alpha-glycophorin					267:283	a normal alpha-glycophorin	258:283	a normal alpha-glycophorin (glycophorin A)	258:299	Immunoblots indicated that erythrocytes of each individual contained a complement of a normal alpha-glycophorin (glycophorin A) and a variant N-glycophorin.
3305497	2	69	theme	normal	260:265	arg1	A					298:298	glycophorin A	286:298	glycophorin A	286:298	Immunoblots indicated that erythrocytes of each individual contained a complement of a normal alpha-glycophorin (glycophorin A) and a variant N-glycophorin.
3305497	1	70	theme	group	143:147	arg1	phenotype					149:157	the Dantu blood group phenotype	127:157	the Dantu blood group phenotype	127:157	Glycophorins of erythrocytes of two unrelated individuals who exhibit the Dantu blood group phenotype were studied.
3305497	7	71	theme	spanning	1273:1280	arg1	residues					1282:1289	delta- and alpha-glycophorins spanning residues	1243:1289	delta- and alpha-glycophorins spanning residues	1243:1289	Sequence analyses of a mixture of chymotryptic peptides of a CNBr fragment of the variant glycophorin identified the sequence Val-His-Arg-Phe-Thr-Val-Pro-Glu-Ile-Thr-Leu-Ile-Ile that contains the junction point of delta- and alpha-glycophorins spanning residues 33-38/39 of delta-glycophorin and residues 71/72-77 of alpha-glycophorin.
3305497	7	71	theme	spanning	1273:1280	arg1	alpha-glycophorin					1346:1362	alpha-glycophorin	1346:1362	alpha-glycophorin	1346:1362	Sequence analyses of a mixture of chymotryptic peptides of a CNBr fragment of the variant glycophorin identified the sequence Val-His-Arg-Phe-Thr-Val-Pro-Glu-Ile-Thr-Leu-Ile-Ile that contains the junction point of delta- and alpha-glycophorins spanning residues 33-38/39 of delta-glycophorin and residues 71/72-77 of alpha-glycophorin.
3305497	5	72	theme	delta-glycophorin	886:902	arg1	characteristic					868:881	characteristic	868:881	characteristic	868:881	All these properties are characteristic of delta-glycophorin.
3305497	8	73	theme	fragments	1404:1412	arg1	mixture					1388:1394	a mixture	1386:1394	a mixture of CNBr fragments	1386:1412	Sequence analysis of a mixture of CNBr fragments allowed us to conclude that the variant originates from delta-s- rather than delta-S-glycophorin.
3305497	9	74	from	2/1	1642:1644	arg1	cells					1666:1670	one individual's cells	1649:1670	one individual's cells	1649:1670	The quantity of the variant Dantu glycophorin when compared to alpha-glycophorin differed in the two individuals, the ratio being 2/1 in one individual's cells and 0.5/1 in the other's.
3305497	9	74	from	2/1	1642:1644	arg1	's					1694:1695	the other's	1685:1695	the other's	1685:1695	The quantity of the variant Dantu glycophorin when compared to alpha-glycophorin differed in the two individuals, the ratio being 2/1 in one individual's cells and 0.5/1 in the other's.
3305497	1	75	theme	erythrocytes	73:84	arg1	Glycophorins					57:68	Glycophorins	57:68	Glycophorins of erythrocytes of two unrelated individuals who exhibit the Dantu blood group phenotype	57:157	Glycophorins of erythrocytes of two unrelated individuals who exhibit the Dantu blood group phenotype were studied.
3305497	3	76	theme	s	422:422	arg1	phenotypes					430:439	the s and N phenotypes	418:439	the s and N phenotypes of the latter's erythrocytes	418:468	delta-Glycophorin (glycophorin B) was present in one donor's cells but not the other's; the s and N phenotypes of the latter's erythrocytes may derive from the variant glycophorin.
3305497	7	77	theme	junction	1225:1232	arg1	point					1234:1238	the junction point	1221:1238	the junction point of delta- and alpha-glycophorins spanning residues 33-38/39 of delta-glycophorin and residues 71/72-77 of alpha-glycophorin	1221:1362	Sequence analyses of a mixture of chymotryptic peptides of a CNBr fragment of the variant glycophorin identified the sequence Val-His-Arg-Phe-Thr-Val-Pro-Glu-Ile-Thr-Leu-Ile-Ile that contains the junction point of delta- and alpha-glycophorins spanning residues 33-38/39 of delta-glycophorin and residues 71/72-77 of alpha-glycophorin.
3305497	4	78	theme	carbohydrate	698:709	arg1	carbohydrate					698:709	its single asparagine-linked carbohydrate	669:709	its single asparagine-linked carbohydrate	669:709	The variant glycophorin is of a smaller size, does not bind to Lens culinaris lectin agarose, and lacks residues approximately 40-60 of alpha-glycophorin and its single asparagine-linked carbohydrate; it contains approximately 2 less O-glycosidically bound units whose structures are identical to those found in alpha-glycophorins.
3305497	4	78	theme	carbohydrate	698:709	arg1	alpha-glycophorin					647:663	alpha-glycophorin	647:663	alpha-glycophorin	647:663	The variant glycophorin is of a smaller size, does not bind to Lens culinaris lectin agarose, and lacks residues approximately 40-60 of alpha-glycophorin and its single asparagine-linked carbohydrate; it contains approximately 2 less O-glycosidically bound units whose structures are identical to those found in alpha-glycophorins.
3305497	4	78	theme	carbohydrate	698:709	arg1	residues					615:622	residues approximately 40-60	615:642	residues approximately 40-60 of alpha-glycophorin and its single asparagine-linked carbohydrate	615:709	The variant glycophorin is of a smaller size, does not bind to Lens culinaris lectin agarose, and lacks residues approximately 40-60 of alpha-glycophorin and its single asparagine-linked carbohydrate; it contains approximately 2 less O-glycosidically bound units whose structures are identical to those found in alpha-glycophorins.
3305497	0	79	theme	Dantu	25:29	arg1	erythrocytes					43:54	Dantu blood group erythrocytes	25:54	Dantu blood group erythrocytes	25:54	Membrane glycophorins of Dantu blood group erythrocytes.
3305497	1	80	theme	individuals	103:113	arg1	erythrocytes					73:84	erythrocytes	73:84	erythrocytes of two unrelated individuals who exhibit the Dantu blood group phenotype	73:157	Glycophorins of erythrocytes of two unrelated individuals who exhibit the Dantu blood group phenotype were studied.
3305497	7	81	dep	residues	1282:1289	arg1	delta-glycophorin					1303:1319	delta-glycophorin	1303:1319	delta-glycophorin	1303:1319	Sequence analyses of a mixture of chymotryptic peptides of a CNBr fragment of the variant glycophorin identified the sequence Val-His-Arg-Phe-Thr-Val-Pro-Glu-Ile-Thr-Leu-Ile-Ile that contains the junction point of delta- and alpha-glycophorins spanning residues 33-38/39 of delta-glycophorin and residues 71/72-77 of alpha-glycophorin.
3305497	7	81	dep	residues	1282:1289	arg1	71/72-77					1334:1341	71/72-77	1334:1341	71/72-77	1334:1341	Sequence analyses of a mixture of chymotryptic peptides of a CNBr fragment of the variant glycophorin identified the sequence Val-His-Arg-Phe-Thr-Val-Pro-Glu-Ile-Thr-Leu-Ile-Ile that contains the junction point of delta- and alpha-glycophorins spanning residues 33-38/39 of delta-glycophorin and residues 71/72-77 of alpha-glycophorin.
3305497	7	81	dep	residues	1282:1289	arg1	33-38/39					1291:1298	33-38/39	1291:1298	33-38/39	1291:1298	Sequence analyses of a mixture of chymotryptic peptides of a CNBr fragment of the variant glycophorin identified the sequence Val-His-Arg-Phe-Thr-Val-Pro-Glu-Ile-Thr-Leu-Ile-Ile that contains the junction point of delta- and alpha-glycophorins spanning residues 33-38/39 of delta-glycophorin and residues 71/72-77 of alpha-glycophorin.
3305497	0	82	theme	group	37:41	arg1	erythrocytes					43:54	Dantu blood group erythrocytes	25:54	Dantu blood group erythrocytes	25:54	Membrane glycophorins of Dantu blood group erythrocytes.
3305497	3	83	theme	other	409:413	arg1	's					414:415	the other's	405:415	one donor's cells but not the other's	379:415	delta-Glycophorin (glycophorin B) was present in one donor's cells but not the other's; the s and N phenotypes of the latter's erythrocytes may derive from the variant glycophorin.
3305497	11	84	theme	junction	2003:2010	arg1	point					2012:2016	a junction point	2001:2016	a junction point around residues 39 of delta- and 71 of alpha-glycophorins	2001:2074	Together, the evidence indicates that both donors' erythrocytes contain a (delta-alpha) variant glycophorin, whose amino terminus originates from delta-s-glycophorin and the carboxyl end from alpha-glycophorin with a junction point around residues 39 of delta- and 71 of alpha-glycophorins.
3305497	2	85	theme	individual	221:230	arg1	erythrocytes					200:211	erythrocytes	200:211	erythrocytes of each individual	200:230	Immunoblots indicated that erythrocytes of each individual contained a complement of a normal alpha-glycophorin (glycophorin A) and a variant N-glycophorin.
3305497	10	86	theme	Dantu	1768:1772	arg1	phenotypes					1774:1783	Dantu phenotypes	1768:1783	Dantu phenotypes	1768:1783	This may reflect that the two donors belong to different varieties of Dantu phenotypes.
3305497	7	87	theme	residues	1325:1332	arg1	point					1234:1238	the junction point	1221:1238	the junction point of delta- and alpha-glycophorins spanning residues 33-38/39 of delta-glycophorin and residues 71/72-77 of alpha-glycophorin	1221:1362	Sequence analyses of a mixture of chymotryptic peptides of a CNBr fragment of the variant glycophorin identified the sequence Val-His-Arg-Phe-Thr-Val-Pro-Glu-Ile-Thr-Leu-Ile-Ile that contains the junction point of delta- and alpha-glycophorins spanning residues 33-38/39 of delta-glycophorin and residues 71/72-77 of alpha-glycophorin.
3305497	12	88	theme	phenotype	2164:2172	arg1	region					2122:2127	the unique junction region	2102:2127	the unique junction region	2102:2127	The results suggest that the unique junction region may be characteristic of the Dantu phenotype.
3305497	12	88	theme	phenotype	2164:2172	arg1	characteristic					2136:2149	characteristic	2136:2149	characteristic of the Dantu phenotype	2136:2172	The results suggest that the unique junction region may be characteristic of the Dantu phenotype.
3305497	11	89	theme	carboxyl	1960:1967	arg1	end					1969:1971	the carboxyl end	1956:1971	the carboxyl end	1956:1971	Together, the evidence indicates that both donors' erythrocytes contain a (delta-alpha) variant glycophorin, whose amino terminus originates from delta-s-glycophorin and the carboxyl end from alpha-glycophorin with a junction point around residues 39 of delta- and 71 of alpha-glycophorins.
3624241	3	0	theme	following	590:598	arg1	structures					606:615	the following novel structures	586:615	the following novel structures	586:615	Methylation analysis, fast atom bombardment-mass spectrometry, and enzymatic degradation were used to elucidate the following novel structures: formula; see text: These results suggest that O-linked oligosaccharides with a disialosyl group, NeuNAc alpha 2----8NeuNAc alpha 2----, may be present in various tissues.
3624241	1	1	link	O-linked	107:114	arg1	oligosaccharides					116:131	The O-linked oligosaccharides	103:131	The O-linked oligosaccharides attached to human erythrocyte glycophorins	103:174	The O-linked oligosaccharides attached to human erythrocyte glycophorins were extensively characterized.
3624241	3	2	theme	novel	600:604	arg1	structures					606:615	the following novel structures	586:615	the following novel structures	586:615	Methylation analysis, fast atom bombardment-mass spectrometry, and enzymatic degradation were used to elucidate the following novel structures: formula; see text: These results suggest that O-linked oligosaccharides with a disialosyl group, NeuNAc alpha 2----8NeuNAc alpha 2----, may be present in various tissues.
3624241	3	3	dep	used	568:571	arg1	see					627:629	see	627:629	see text	627:634	Methylation analysis, fast atom bombardment-mass spectrometry, and enzymatic degradation were used to elucidate the following novel structures: formula; see text: These results suggest that O-linked oligosaccharides with a disialosyl group, NeuNAc alpha 2----8NeuNAc alpha 2----, may be present in various tissues.
3624241	3	3	dep	used	568:571	arg1	formula					618:624	formula	618:624	formula; see text: These results suggest that O-linked oligosaccharides with a disialosyl group, NeuNAc alpha 2----8NeuNAc alpha 2----, may be present in various tissues	618:786	Methylation analysis, fast atom bombardment-mass spectrometry, and enzymatic degradation were used to elucidate the following novel structures: formula; see text: These results suggest that O-linked oligosaccharides with a disialosyl group, NeuNAc alpha 2----8NeuNAc alpha 2----, may be present in various tissues.
3624241	3	4	theme	O-linked	664:671	arg1	oligosaccharides					673:688	O-linked oligosaccharides	664:688	O-linked oligosaccharides with a disialosyl group	664:712	Methylation analysis, fast atom bombardment-mass spectrometry, and enzymatic degradation were used to elucidate the following novel structures: formula; see text: These results suggest that O-linked oligosaccharides with a disialosyl group, NeuNAc alpha 2----8NeuNAc alpha 2----, may be present in various tissues.
3624241	3	4	theme	O-linked	664:671	arg1	2----					747:751	NeuNAc alpha 2----8NeuNAc alpha 2----	715:751	NeuNAc alpha 2----8NeuNAc alpha 2----	715:751	Methylation analysis, fast atom bombardment-mass spectrometry, and enzymatic degradation were used to elucidate the following novel structures: formula; see text: These results suggest that O-linked oligosaccharides with a disialosyl group, NeuNAc alpha 2----8NeuNAc alpha 2----, may be present in various tissues.
3624241	3	5	with	oligosaccharides	673:688	arg1	group					708:712	a disialosyl group	695:712	a disialosyl group	695:712	Methylation analysis, fast atom bombardment-mass spectrometry, and enzymatic degradation were used to elucidate the following novel structures: formula; see text: These results suggest that O-linked oligosaccharides with a disialosyl group, NeuNAc alpha 2----8NeuNAc alpha 2----, may be present in various tissues.
3624241	3	6	attach	present	761:767	arg1	tissues					780:786	various tissues	772:786	various tissues	772:786	Methylation analysis, fast atom bombardment-mass spectrometry, and enzymatic degradation were used to elucidate the following novel structures: formula; see text: These results suggest that O-linked oligosaccharides with a disialosyl group, NeuNAc alpha 2----8NeuNAc alpha 2----, may be present in various tissues.
3624241	3	6	attach	present	761:767	arg2	2----					747:751	NeuNAc alpha 2----8NeuNAc alpha 2----	715:751	NeuNAc alpha 2----8NeuNAc alpha 2----	715:751	Methylation analysis, fast atom bombardment-mass spectrometry, and enzymatic degradation were used to elucidate the following novel structures: formula; see text: These results suggest that O-linked oligosaccharides with a disialosyl group, NeuNAc alpha 2----8NeuNAc alpha 2----, may be present in various tissues.
3624241	3	6	attach	present	761:767	arg2	oligosaccharides					673:688	O-linked oligosaccharides	664:688	O-linked oligosaccharides with a disialosyl group	664:712	Methylation analysis, fast atom bombardment-mass spectrometry, and enzymatic degradation were used to elucidate the following novel structures: formula; see text: These results suggest that O-linked oligosaccharides with a disialosyl group, NeuNAc alpha 2----8NeuNAc alpha 2----, may be present in various tissues.
3624241	3	7	from	present	761:767	arg1	tissues					780:786	various tissues	772:786	various tissues	772:786	Methylation analysis, fast atom bombardment-mass spectrometry, and enzymatic degradation were used to elucidate the following novel structures: formula; see text: These results suggest that O-linked oligosaccharides with a disialosyl group, NeuNAc alpha 2----8NeuNAc alpha 2----, may be present in various tissues.
3624241	2	8	gly	monosialylated	348:361	arg1	trisaccharide					363:375	monosialylated trisaccharide	348:375	monosialylated trisaccharide	348:375	In addition to the previously described disialylated tetrasaccharide, NeuNAc alpha 2----3Gal beta 1----3 (Neu-NAc alpha 2----6)GalNAcOH and monosialylated trisaccharide, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, novel trisialylated oligosaccharides were isolated.
3624241	3	9	theme	atom	501:504	arg1	spectrometry					523:534	fast atom bombardment-mass spectrometry	496:534	fast atom bombardment-mass spectrometry	496:534	Methylation analysis, fast atom bombardment-mass spectrometry, and enzymatic degradation were used to elucidate the following novel structures: formula; see text: These results suggest that O-linked oligosaccharides with a disialosyl group, NeuNAc alpha 2----8NeuNAc alpha 2----, may be present in various tissues.
3624241	1	10	theme	O-linked	107:114	arg1	oligosaccharides					116:131	The O-linked oligosaccharides	103:131	The O-linked oligosaccharides attached to human erythrocyte glycophorins	103:174	The O-linked oligosaccharides attached to human erythrocyte glycophorins were extensively characterized.
3624241	3	11	theme	bombardment-mass	506:521	arg1	spectrometry					523:534	fast atom bombardment-mass spectrometry	496:534	fast atom bombardment-mass spectrometry	496:534	Methylation analysis, fast atom bombardment-mass spectrometry, and enzymatic degradation were used to elucidate the following novel structures: formula; see text: These results suggest that O-linked oligosaccharides with a disialosyl group, NeuNAc alpha 2----8NeuNAc alpha 2----, may be present in various tissues.
3624241	0	12	theme	sialylated	20:29	arg1	oligosaccharides					40:55	novel sialylated O-linked oligosaccharides	14:55	novel sialylated O-linked oligosaccharides	14:55	Structures of novel sialylated O-linked oligosaccharides isolated from human erythrocyte glycophorins.
3624241	0	13	link	O-linked	31:38	arg1	oligosaccharides					40:55	novel sialylated O-linked oligosaccharides	14:55	novel sialylated O-linked oligosaccharides	14:55	Structures of novel sialylated O-linked oligosaccharides isolated from human erythrocyte glycophorins.
3624241	2	14	theme	monosialylated	348:361	arg1	trisaccharide					363:375	monosialylated trisaccharide	348:375	monosialylated trisaccharide	348:375	In addition to the previously described disialylated tetrasaccharide, NeuNAc alpha 2----3Gal beta 1----3 (Neu-NAc alpha 2----6)GalNAcOH and monosialylated trisaccharide, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, novel trisialylated oligosaccharides were isolated.
3624241	0	15	theme	novel	14:18	arg1	oligosaccharides					40:55	novel sialylated O-linked oligosaccharides	14:55	novel sialylated O-linked oligosaccharides	14:55	Structures of novel sialylated O-linked oligosaccharides isolated from human erythrocyte glycophorins.
3624241	2	16	gly	trisialylated	428:440	arg1	oligosaccharides					442:457	novel trisialylated oligosaccharides	422:457	novel trisialylated oligosaccharides	422:457	In addition to the previously described disialylated tetrasaccharide, NeuNAc alpha 2----3Gal beta 1----3 (Neu-NAc alpha 2----6)GalNAcOH and monosialylated trisaccharide, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, novel trisialylated oligosaccharides were isolated.
3624241	3	17	theme	2----8NeuNAc	728:739	arg1	oligosaccharides					673:688	O-linked oligosaccharides	664:688	O-linked oligosaccharides with a disialosyl group	664:712	Methylation analysis, fast atom bombardment-mass spectrometry, and enzymatic degradation were used to elucidate the following novel structures: formula; see text: These results suggest that O-linked oligosaccharides with a disialosyl group, NeuNAc alpha 2----8NeuNAc alpha 2----, may be present in various tissues.
3624241	3	17	theme	2----8NeuNAc	728:739	arg1	2----					747:751	NeuNAc alpha 2----8NeuNAc alpha 2----	715:751	NeuNAc alpha 2----8NeuNAc alpha 2----	715:751	Methylation analysis, fast atom bombardment-mass spectrometry, and enzymatic degradation were used to elucidate the following novel structures: formula; see text: These results suggest that O-linked oligosaccharides with a disialosyl group, NeuNAc alpha 2----8NeuNAc alpha 2----, may be present in various tissues.
3624241	0	18	theme	oligosaccharides	40:55	arg1	Structures					0:9	Structures	0:9	Structures of novel sialylated O-linked oligosaccharides	0:55	Structures of novel sialylated O-linked oligosaccharides isolated from human erythrocyte glycophorins.
3624241	2	19	theme	2----3Gal	391:399	arg1	beta					401:404	NeuNAc alpha 2----3Gal beta 1----3GalNAcOH	378:419	NeuNAc alpha 2----3Gal beta 1----3GalNAcOH	378:419	In addition to the previously described disialylated tetrasaccharide, NeuNAc alpha 2----3Gal beta 1----3 (Neu-NAc alpha 2----6)GalNAcOH and monosialylated trisaccharide, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, novel trisialylated oligosaccharides were isolated.
3624241	3	20	theme	alpha	741:745	arg1	oligosaccharides					673:688	O-linked oligosaccharides	664:688	O-linked oligosaccharides with a disialosyl group	664:712	Methylation analysis, fast atom bombardment-mass spectrometry, and enzymatic degradation were used to elucidate the following novel structures: formula; see text: These results suggest that O-linked oligosaccharides with a disialosyl group, NeuNAc alpha 2----8NeuNAc alpha 2----, may be present in various tissues.
3624241	3	20	theme	alpha	741:745	arg1	2----					747:751	NeuNAc alpha 2----8NeuNAc alpha 2----	715:751	NeuNAc alpha 2----8NeuNAc alpha 2----	715:751	Methylation analysis, fast atom bombardment-mass spectrometry, and enzymatic degradation were used to elucidate the following novel structures: formula; see text: These results suggest that O-linked oligosaccharides with a disialosyl group, NeuNAc alpha 2----8NeuNAc alpha 2----, may be present in various tissues.
3624241	2	21	theme	2----3Gal	291:299	arg1	alpha					322:326	Neu-NAc alpha 2----6	314:333	Neu-NAc alpha 2----6	314:333	In addition to the previously described disialylated tetrasaccharide, NeuNAc alpha 2----3Gal beta 1----3 (Neu-NAc alpha 2----6)GalNAcOH and monosialylated trisaccharide, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, novel trisialylated oligosaccharides were isolated.
3624241	2	21	theme	2----3Gal	291:299	arg1	beta					301:304	NeuNAc alpha 2----3Gal beta 1----3	278:311	NeuNAc alpha 2----3Gal beta 1----3 (Neu-NAc alpha 2----6)GalNAcOH	278:342	In addition to the previously described disialylated tetrasaccharide, NeuNAc alpha 2----3Gal beta 1----3 (Neu-NAc alpha 2----6)GalNAcOH and monosialylated trisaccharide, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, novel trisialylated oligosaccharides were isolated.
3624241	0	22	theme	O-linked	31:38	arg1	oligosaccharides					40:55	novel sialylated O-linked oligosaccharides	14:55	novel sialylated O-linked oligosaccharides	14:55	Structures of novel sialylated O-linked oligosaccharides isolated from human erythrocyte glycophorins.
3624241	3	23	link	O-linked	664:671	arg1	oligosaccharides					673:688	O-linked oligosaccharides	664:688	O-linked oligosaccharides with a disialosyl group	664:712	Methylation analysis, fast atom bombardment-mass spectrometry, and enzymatic degradation were used to elucidate the following novel structures: formula; see text: These results suggest that O-linked oligosaccharides with a disialosyl group, NeuNAc alpha 2----8NeuNAc alpha 2----, may be present in various tissues.
3624241	3	23	link	O-linked	664:671	arg1	2----					747:751	NeuNAc alpha 2----8NeuNAc alpha 2----	715:751	NeuNAc alpha 2----8NeuNAc alpha 2----	715:751	Methylation analysis, fast atom bombardment-mass spectrometry, and enzymatic degradation were used to elucidate the following novel structures: formula; see text: These results suggest that O-linked oligosaccharides with a disialosyl group, NeuNAc alpha 2----8NeuNAc alpha 2----, may be present in various tissues.
3624241	3	24	theme	NeuNAc	715:720	arg1	oligosaccharides					673:688	O-linked oligosaccharides	664:688	O-linked oligosaccharides with a disialosyl group	664:712	Methylation analysis, fast atom bombardment-mass spectrometry, and enzymatic degradation were used to elucidate the following novel structures: formula; see text: These results suggest that O-linked oligosaccharides with a disialosyl group, NeuNAc alpha 2----8NeuNAc alpha 2----, may be present in various tissues.
3624241	3	24	theme	NeuNAc	715:720	arg1	2----					747:751	NeuNAc alpha 2----8NeuNAc alpha 2----	715:751	NeuNAc alpha 2----8NeuNAc alpha 2----	715:751	Methylation analysis, fast atom bombardment-mass spectrometry, and enzymatic degradation were used to elucidate the following novel structures: formula; see text: These results suggest that O-linked oligosaccharides with a disialosyl group, NeuNAc alpha 2----8NeuNAc alpha 2----, may be present in various tissues.
3624241	2	25	theme	alpha	285:289	arg1	alpha					322:326	Neu-NAc alpha 2----6	314:333	Neu-NAc alpha 2----6	314:333	In addition to the previously described disialylated tetrasaccharide, NeuNAc alpha 2----3Gal beta 1----3 (Neu-NAc alpha 2----6)GalNAcOH and monosialylated trisaccharide, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, novel trisialylated oligosaccharides were isolated.
3624241	2	25	theme	alpha	285:289	arg1	beta					301:304	NeuNAc alpha 2----3Gal beta 1----3	278:311	NeuNAc alpha 2----3Gal beta 1----3 (Neu-NAc alpha 2----6)GalNAcOH	278:342	In addition to the previously described disialylated tetrasaccharide, NeuNAc alpha 2----3Gal beta 1----3 (Neu-NAc alpha 2----6)GalNAcOH and monosialylated trisaccharide, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, novel trisialylated oligosaccharides were isolated.
3624241	3	26	located	present	761:767	arg1	tissues					780:786	various tissues	772:786	various tissues	772:786	Methylation analysis, fast atom bombardment-mass spectrometry, and enzymatic degradation were used to elucidate the following novel structures: formula; see text: These results suggest that O-linked oligosaccharides with a disialosyl group, NeuNAc alpha 2----8NeuNAc alpha 2----, may be present in various tissues.
3624241	3	26	located	present	761:767	arg2	2----					747:751	NeuNAc alpha 2----8NeuNAc alpha 2----	715:751	NeuNAc alpha 2----8NeuNAc alpha 2----	715:751	Methylation analysis, fast atom bombardment-mass spectrometry, and enzymatic degradation were used to elucidate the following novel structures: formula; see text: These results suggest that O-linked oligosaccharides with a disialosyl group, NeuNAc alpha 2----8NeuNAc alpha 2----, may be present in various tissues.
3624241	3	26	located	present	761:767	arg2	oligosaccharides					673:688	O-linked oligosaccharides	664:688	O-linked oligosaccharides with a disialosyl group	664:712	Methylation analysis, fast atom bombardment-mass spectrometry, and enzymatic degradation were used to elucidate the following novel structures: formula; see text: These results suggest that O-linked oligosaccharides with a disialosyl group, NeuNAc alpha 2----8NeuNAc alpha 2----, may be present in various tissues.
3624241	3	27	theme	Methylation	474:484	arg1	analysis					486:493	Methylation analysis	474:493	Methylation analysis	474:493	Methylation analysis, fast atom bombardment-mass spectrometry, and enzymatic degradation were used to elucidate the following novel structures: formula; see text: These results suggest that O-linked oligosaccharides with a disialosyl group, NeuNAc alpha 2----8NeuNAc alpha 2----, may be present in various tissues.
3624241	3	28	theme	fast	496:499	arg1	spectrometry					523:534	fast atom bombardment-mass spectrometry	496:534	fast atom bombardment-mass spectrometry	496:534	Methylation analysis, fast atom bombardment-mass spectrometry, and enzymatic degradation were used to elucidate the following novel structures: formula; see text: These results suggest that O-linked oligosaccharides with a disialosyl group, NeuNAc alpha 2----8NeuNAc alpha 2----, may be present in various tissues.
3624241	3	29	theme	alpha	722:726	arg1	oligosaccharides					673:688	O-linked oligosaccharides	664:688	O-linked oligosaccharides with a disialosyl group	664:712	Methylation analysis, fast atom bombardment-mass spectrometry, and enzymatic degradation were used to elucidate the following novel structures: formula; see text: These results suggest that O-linked oligosaccharides with a disialosyl group, NeuNAc alpha 2----8NeuNAc alpha 2----, may be present in various tissues.
3624241	3	29	theme	alpha	722:726	arg1	2----					747:751	NeuNAc alpha 2----8NeuNAc alpha 2----	715:751	NeuNAc alpha 2----8NeuNAc alpha 2----	715:751	Methylation analysis, fast atom bombardment-mass spectrometry, and enzymatic degradation were used to elucidate the following novel structures: formula; see text: These results suggest that O-linked oligosaccharides with a disialosyl group, NeuNAc alpha 2----8NeuNAc alpha 2----, may be present in various tissues.
3624241	2	30	theme	NeuNAc	278:283	arg1	alpha					322:326	Neu-NAc alpha 2----6	314:333	Neu-NAc alpha 2----6	314:333	In addition to the previously described disialylated tetrasaccharide, NeuNAc alpha 2----3Gal beta 1----3 (Neu-NAc alpha 2----6)GalNAcOH and monosialylated trisaccharide, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, novel trisialylated oligosaccharides were isolated.
3624241	2	30	theme	NeuNAc	278:283	arg1	beta					301:304	NeuNAc alpha 2----3Gal beta 1----3	278:311	NeuNAc alpha 2----3Gal beta 1----3 (Neu-NAc alpha 2----6)GalNAcOH	278:342	In addition to the previously described disialylated tetrasaccharide, NeuNAc alpha 2----3Gal beta 1----3 (Neu-NAc alpha 2----6)GalNAcOH and monosialylated trisaccharide, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, novel trisialylated oligosaccharides were isolated.
3624241	3	31	from	tissues	780:786	arg1	present					761:767	present	761:767	present	761:767	Methylation analysis, fast atom bombardment-mass spectrometry, and enzymatic degradation were used to elucidate the following novel structures: formula; see text: These results suggest that O-linked oligosaccharides with a disialosyl group, NeuNAc alpha 2----8NeuNAc alpha 2----, may be present in various tissues.
3624241	1	32	attach	attached	133:140	arg2	oligosaccharides					116:131	The O-linked oligosaccharides	103:131	The O-linked oligosaccharides attached to human erythrocyte glycophorins	103:174	The O-linked oligosaccharides attached to human erythrocyte glycophorins were extensively characterized.
3624241	1	32	attach	attached	133:140	arg1	glycophorins					163:174	human erythrocyte glycophorins	145:174	human erythrocyte glycophorins	145:174	The O-linked oligosaccharides attached to human erythrocyte glycophorins were extensively characterized.
3624241	0	33	gly	sialylated	20:29	arg1	oligosaccharides					40:55	novel sialylated O-linked oligosaccharides	14:55	novel sialylated O-linked oligosaccharides	14:55	Structures of novel sialylated O-linked oligosaccharides isolated from human erythrocyte glycophorins.
3624241	1	34	theme	human	145:149	arg1	glycophorins					163:174	human erythrocyte glycophorins	145:174	human erythrocyte glycophorins	145:174	The O-linked oligosaccharides attached to human erythrocyte glycophorins were extensively characterized.
3624241	2	35	gly	disialylated	248:259	arg1	tetrasaccharide					261:275	the previously described disialylated tetrasaccharide	223:275	the previously described disialylated tetrasaccharide	223:275	In addition to the previously described disialylated tetrasaccharide, NeuNAc alpha 2----3Gal beta 1----3 (Neu-NAc alpha 2----6)GalNAcOH and monosialylated trisaccharide, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, novel trisialylated oligosaccharides were isolated.
3624241	3	36	theme	disialosyl	697:706	arg1	group					708:712	a disialosyl group	695:712	a disialosyl group	695:712	Methylation analysis, fast atom bombardment-mass spectrometry, and enzymatic degradation were used to elucidate the following novel structures: formula; see text: These results suggest that O-linked oligosaccharides with a disialosyl group, NeuNAc alpha 2----8NeuNAc alpha 2----, may be present in various tissues.
3624241	2	37	theme	disialylated	248:259	arg1	tetrasaccharide					261:275	the previously described disialylated tetrasaccharide	223:275	the previously described disialylated tetrasaccharide	223:275	In addition to the previously described disialylated tetrasaccharide, NeuNAc alpha 2----3Gal beta 1----3 (Neu-NAc alpha 2----6)GalNAcOH and monosialylated trisaccharide, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, novel trisialylated oligosaccharides were isolated.
3624241	2	38	theme	Neu-NAc	314:320	arg1	alpha					322:326	Neu-NAc alpha 2----6	314:333	Neu-NAc alpha 2----6	314:333	In addition to the previously described disialylated tetrasaccharide, NeuNAc alpha 2----3Gal beta 1----3 (Neu-NAc alpha 2----6)GalNAcOH and monosialylated trisaccharide, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, novel trisialylated oligosaccharides were isolated.
3624241	2	38	theme	Neu-NAc	314:320	arg1	beta					301:304	NeuNAc alpha 2----3Gal beta 1----3	278:311	NeuNAc alpha 2----3Gal beta 1----3 (Neu-NAc alpha 2----6)GalNAcOH	278:342	In addition to the previously described disialylated tetrasaccharide, NeuNAc alpha 2----3Gal beta 1----3 (Neu-NAc alpha 2----6)GalNAcOH and monosialylated trisaccharide, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, novel trisialylated oligosaccharides were isolated.
3624241	3	39	used	used	568:571	arg2	analysis					486:493	Methylation analysis	474:493	Methylation analysis	474:493	Methylation analysis, fast atom bombardment-mass spectrometry, and enzymatic degradation were used to elucidate the following novel structures: formula; see text: These results suggest that O-linked oligosaccharides with a disialosyl group, NeuNAc alpha 2----8NeuNAc alpha 2----, may be present in various tissues.
3624241	3	39	used	used	568:571	arg2	degradation					551:561	enzymatic degradation	541:561	enzymatic degradation	541:561	Methylation analysis, fast atom bombardment-mass spectrometry, and enzymatic degradation were used to elucidate the following novel structures: formula; see text: These results suggest that O-linked oligosaccharides with a disialosyl group, NeuNAc alpha 2----8NeuNAc alpha 2----, may be present in various tissues.
3624241	3	39	used	used	568:571	arg2	spectrometry					523:534	fast atom bombardment-mass spectrometry	496:534	fast atom bombardment-mass spectrometry	496:534	Methylation analysis, fast atom bombardment-mass spectrometry, and enzymatic degradation were used to elucidate the following novel structures: formula; see text: These results suggest that O-linked oligosaccharides with a disialosyl group, NeuNAc alpha 2----8NeuNAc alpha 2----, may be present in various tissues.
3624241	1	40	theme	erythrocyte	151:161	arg1	glycophorins					163:174	human erythrocyte glycophorins	145:174	human erythrocyte glycophorins	145:174	The O-linked oligosaccharides attached to human erythrocyte glycophorins were extensively characterized.
3624241	2	41	theme	described	238:246	arg1	tetrasaccharide					261:275	the previously described disialylated tetrasaccharide	223:275	the previously described disialylated tetrasaccharide	223:275	In addition to the previously described disialylated tetrasaccharide, NeuNAc alpha 2----3Gal beta 1----3 (Neu-NAc alpha 2----6)GalNAcOH and monosialylated trisaccharide, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, novel trisialylated oligosaccharides were isolated.
3624241	2	42	theme	NeuNAc	378:383	arg1	beta					401:404	NeuNAc alpha 2----3Gal beta 1----3GalNAcOH	378:419	NeuNAc alpha 2----3Gal beta 1----3GalNAcOH	378:419	In addition to the previously described disialylated tetrasaccharide, NeuNAc alpha 2----3Gal beta 1----3 (Neu-NAc alpha 2----6)GalNAcOH and monosialylated trisaccharide, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, novel trisialylated oligosaccharides were isolated.
3624241	2	43	theme	alpha	385:389	arg1	beta					401:404	NeuNAc alpha 2----3Gal beta 1----3GalNAcOH	378:419	NeuNAc alpha 2----3Gal beta 1----3GalNAcOH	378:419	In addition to the previously described disialylated tetrasaccharide, NeuNAc alpha 2----3Gal beta 1----3 (Neu-NAc alpha 2----6)GalNAcOH and monosialylated trisaccharide, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, novel trisialylated oligosaccharides were isolated.
3624241	0	44	theme	erythrocyte	77:87	arg1	glycophorins					89:100	human erythrocyte glycophorins	71:100	human erythrocyte glycophorins	71:100	Structures of novel sialylated O-linked oligosaccharides isolated from human erythrocyte glycophorins.
3624241	3	45	theme	enzymatic	541:549	arg1	degradation					551:561	enzymatic degradation	541:561	enzymatic degradation	541:561	Methylation analysis, fast atom bombardment-mass spectrometry, and enzymatic degradation were used to elucidate the following novel structures: formula; see text: These results suggest that O-linked oligosaccharides with a disialosyl group, NeuNAc alpha 2----8NeuNAc alpha 2----, may be present in various tissues.
3624241	2	46	theme	trisialylated	428:440	arg1	oligosaccharides					442:457	novel trisialylated oligosaccharides	422:457	novel trisialylated oligosaccharides	422:457	In addition to the previously described disialylated tetrasaccharide, NeuNAc alpha 2----3Gal beta 1----3 (Neu-NAc alpha 2----6)GalNAcOH and monosialylated trisaccharide, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, novel trisialylated oligosaccharides were isolated.
3624241	0	47	theme	human	71:75	arg1	glycophorins					89:100	human erythrocyte glycophorins	71:100	human erythrocyte glycophorins	71:100	Structures of novel sialylated O-linked oligosaccharides isolated from human erythrocyte glycophorins.
3624241	3	48	theme	various	772:778	arg1	tissues					780:786	various tissues	772:786	various tissues	772:786	Methylation analysis, fast atom bombardment-mass spectrometry, and enzymatic degradation were used to elucidate the following novel structures: formula; see text: These results suggest that O-linked oligosaccharides with a disialosyl group, NeuNAc alpha 2----8NeuNAc alpha 2----, may be present in various tissues.
3624241	2	49	theme	beta	301:304	arg1	GalNAcOH					335:342	NeuNAc alpha 2----3Gal beta 1----3 (Neu-NAc alpha 2----6)GalNAcOH	278:342	NeuNAc alpha 2----3Gal beta 1----3 (Neu-NAc alpha 2----6)GalNAcOH	278:342	In addition to the previously described disialylated tetrasaccharide, NeuNAc alpha 2----3Gal beta 1----3 (Neu-NAc alpha 2----6)GalNAcOH and monosialylated trisaccharide, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, novel trisialylated oligosaccharides were isolated.
3624241	2	50	theme	novel	422:426	arg1	oligosaccharides					442:457	novel trisialylated oligosaccharides	422:457	novel trisialylated oligosaccharides	422:457	In addition to the previously described disialylated tetrasaccharide, NeuNAc alpha 2----3Gal beta 1----3 (Neu-NAc alpha 2----6)GalNAcOH and monosialylated trisaccharide, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, novel trisialylated oligosaccharides were isolated.
7215351	0	0	theme	secretory	76:84	arg1	immunoglobulins					86:100	secretory immunoglobulins	76:100	secretory immunoglobulins from human milk	76:116	Heterogeneity of the glycans O-glycosidically linked to the hinge region of secretory immunoglobulins from human milk.
7215351	5	1	theme	mass	936:939	arg1	spectrometry					941:952	mass spectrometry	936:952	mass spectrometry	936:952	The complete structure of four of these oligosaccharides was determined by methanolysis, methylation and mass spectrometry.
7215351	1	2	theme	2SO4	225:228	arg1	concentration					230:242	(NH4)2SO4 concentration	220:242	(NH4)2SO4 concentration	220:242	Pure secretory immunoglobulin A was isolated from human milk by fractionation in gradients of pH and (NH4)2SO4 concentration followed by gel filtration.
7215351	3	3	theme	0.2:0.5:2.5:2:1	655:669	arg1	ratio					646:650	the molar ratio	636:650	the molar ratio of 0.2:0.5:2.5:2:1	636:669	The mixture of O-glycosidically linked oligosaccharides contained N-acetylneuraminic acid (NeuAc), fucose (Fuc), galactose (Gal), N-acetylglucosamine (GlcNAc) and N-acetylgalactosamine (GalNAc) in the molar ratio of 0.2:0.5:2.5:2:1 respectively.
7215351	1	4	theme	concentration	230:242	arg1	gradients					200:208	gradients	200:208	gradients of pH and (NH4)2SO4 concentration followed by gel filtration	200:269	Pure secretory immunoglobulin A was isolated from human milk by fractionation in gradients of pH and (NH4)2SO4 concentration followed by gel filtration.
7215351	2	5	link	linked	325:330	arg1	oligosaccharides					332:347	all the O-glycosidically linked oligosaccharides	300:347	all the O-glycosidically linked oligosaccharides	300:347	The hinge region containing all the O-glycosidically linked oligosaccharides was isolated en bloc after trypsin and pepsin hydrolysis and separated by gel filtration.
7215351	4	6	theme	ion-exchange	768:779	arg1	chromatography					781:794	ion-exchange chromatography	768:794	ion-exchange chromatography	768:794	After beta-elimination several oligosaccharides were separated by a combination of ion-exchange chromatography and gel-filtration chromatography.
7215351	6	7	theme	serine	1426:1431	arg1	residues					1433:1440	serine residues	1426:1440	serine residues of the hinge region from myeloma serum immunoglobulin A1	1426:1497	These oligosaccharides are more complex and heterogenous than the oligosaccharides linked to serine residues of the hinge region from myeloma serum immunoglobulin A1.
7215351	6	7	theme	serine	1426:1431	arg1	region					1455:1460	the hinge region	1445:1460	the hinge region from myeloma serum immunoglobulin A1	1445:1497	These oligosaccharides are more complex and heterogenous than the oligosaccharides linked to serine residues of the hinge region from myeloma serum immunoglobulin A1.
7215351	0	8	theme	immunoglobulins	86:100	arg1	region					66:71	the hinge region	56:71	the hinge region of secretory immunoglobulins from human milk	56:116	Heterogeneity of the glycans O-glycosidically linked to the hinge region of secretory immunoglobulins from human milk.
7215351	3	9	contain	contained	495:503	arg2	acid					524:527	N-acetylneuraminic acid	505:527	N-acetylneuraminic acid (NeuAc)	505:535	The mixture of O-glycosidically linked oligosaccharides contained N-acetylneuraminic acid (NeuAc), fucose (Fuc), galactose (Gal), N-acetylglucosamine (GlcNAc) and N-acetylgalactosamine (GalNAc) in the molar ratio of 0.2:0.5:2.5:2:1 respectively.
7215351	3	9	contain	contained	495:503	arg2	mixture					443:449	The mixture	439:449	The mixture of O-glycosidically linked oligosaccharides	439:493	The mixture of O-glycosidically linked oligosaccharides contained N-acetylneuraminic acid (NeuAc), fucose (Fuc), galactose (Gal), N-acetylglucosamine (GlcNAc) and N-acetylgalactosamine (GalNAc) in the molar ratio of 0.2:0.5:2.5:2:1 respectively.
7215351	3	9	contain	contained	495:503	arg2	fucose					538:543	fucose	538:543	fucose (Fuc)	538:549	The mixture of O-glycosidically linked oligosaccharides contained N-acetylneuraminic acid (NeuAc), fucose (Fuc), galactose (Gal), N-acetylglucosamine (GlcNAc) and N-acetylgalactosamine (GalNAc) in the molar ratio of 0.2:0.5:2.5:2:1 respectively.
7215351	3	9	contain	contained	495:503	arg2	NeuAc					530:534	NeuAc	530:534	NeuAc	530:534	The mixture of O-glycosidically linked oligosaccharides contained N-acetylneuraminic acid (NeuAc), fucose (Fuc), galactose (Gal), N-acetylglucosamine (GlcNAc) and N-acetylgalactosamine (GalNAc) in the molar ratio of 0.2:0.5:2.5:2:1 respectively.
7215351	3	9	contain	contained	495:503	arg1	mixture					443:449	The mixture	439:449	The mixture of O-glycosidically linked oligosaccharides	439:493	The mixture of O-glycosidically linked oligosaccharides contained N-acetylneuraminic acid (NeuAc), fucose (Fuc), galactose (Gal), N-acetylglucosamine (GlcNAc) and N-acetylgalactosamine (GalNAc) in the molar ratio of 0.2:0.5:2.5:2:1 respectively.
7215351	3	9	contain	contained	495:503	arg1	ratio					646:650	the molar ratio	636:650	the molar ratio of 0.2:0.5:2.5:2:1	636:669	The mixture of O-glycosidically linked oligosaccharides contained N-acetylneuraminic acid (NeuAc), fucose (Fuc), galactose (Gal), N-acetylglucosamine (GlcNAc) and N-acetylgalactosamine (GalNAc) in the molar ratio of 0.2:0.5:2.5:2:1 respectively.
7215351	3	10	link	linked	471:476	arg1	oligosaccharides					478:493	O-glycosidically linked oligosaccharides	454:493	O-glycosidically linked oligosaccharides	454:493	The mixture of O-glycosidically linked oligosaccharides contained N-acetylneuraminic acid (NeuAc), fucose (Fuc), galactose (Gal), N-acetylglucosamine (GlcNAc) and N-acetylgalactosamine (GalNAc) in the molar ratio of 0.2:0.5:2.5:2:1 respectively.
7215351	4	11	theme	several	708:714	arg1	oligosaccharides					716:731	several oligosaccharides	708:731	several oligosaccharides	708:731	After beta-elimination several oligosaccharides were separated by a combination of ion-exchange chromatography and gel-filtration chromatography.
7215351	6	12	theme	immunoglobulin	1481:1494	arg1	A1					1496:1497	myeloma serum immunoglobulin A1	1467:1497	myeloma serum immunoglobulin A1	1467:1497	These oligosaccharides are more complex and heterogenous than the oligosaccharides linked to serine residues of the hinge region from myeloma serum immunoglobulin A1.
7215351	2	13	dep	bloc	365:368	arg1	pepsin					388:393	pepsin	388:393	pepsin	388:393	The hinge region containing all the O-glycosidically linked oligosaccharides was isolated en bloc after trypsin and pepsin hydrolysis and separated by gel filtration.
7215351	2	13	dep	bloc	365:368	arg1	trypsin					376:382	trypsin	376:382	trypsin	376:382	The hinge region containing all the O-glycosidically linked oligosaccharides was isolated en bloc after trypsin and pepsin hydrolysis and separated by gel filtration.
7215351	1	14	theme	human	169:173	arg1	milk					175:178	human milk	169:178	human milk	169:178	Pure secretory immunoglobulin A was isolated from human milk by fractionation in gradients of pH and (NH4)2SO4 concentration followed by gel filtration.
7215351	0	15	theme	human	107:111	arg1	milk					113:116	human milk	107:116	human milk	107:116	Heterogeneity of the glycans O-glycosidically linked to the hinge region of secretory immunoglobulins from human milk.
7215351	4	16	theme	chromatography	781:794	arg1	combination					753:763	a combination	751:763	a combination of ion-exchange chromatography and gel-filtration chromatography	751:828	After beta-elimination several oligosaccharides were separated by a combination of ion-exchange chromatography and gel-filtration chromatography.
7215351	5	17	theme	complete	835:842	arg1	structure					844:852	The complete structure	831:852	The complete structure of four of these oligosaccharides	831:886	The complete structure of four of these oligosaccharides was determined by methanolysis, methylation and mass spectrometry.
7215351	1	18	attach	isolated	155:162	arg2	A					149:149	Pure secretory immunoglobulin A	119:149	Pure secretory immunoglobulin A	119:149	Pure secretory immunoglobulin A was isolated from human milk by fractionation in gradients of pH and (NH4)2SO4 concentration followed by gel filtration.
7215351	1	18	attach	isolated	155:162	arg1	milk					175:178	human milk	169:178	human milk	169:178	Pure secretory immunoglobulin A was isolated from human milk by fractionation in gradients of pH and (NH4)2SO4 concentration followed by gel filtration.
7215351	0	19	attach	linked	46:51	arg2	Heterogeneity					0:12	Heterogeneity	0:12	Heterogeneity of the glycans	0:27	Heterogeneity of the glycans O-glycosidically linked to the hinge region of secretory immunoglobulins from human milk.
7215351	0	19	attach	linked	46:51	arg1	region					66:71	the hinge region	56:71	the hinge region of secretory immunoglobulins from human milk	56:116	Heterogeneity of the glycans O-glycosidically linked to the hinge region of secretory immunoglobulins from human milk.
7215351	1	20	theme	gel	256:258	arg1	filtration					260:269	gel filtration	256:269	gel filtration	256:269	Pure secretory immunoglobulin A was isolated from human milk by fractionation in gradients of pH and (NH4)2SO4 concentration followed by gel filtration.
7215351	6	21	from	residues	1433:1440	arg1	A1					1496:1497	myeloma serum immunoglobulin A1	1467:1497	myeloma serum immunoglobulin A1	1467:1497	These oligosaccharides are more complex and heterogenous than the oligosaccharides linked to serine residues of the hinge region from myeloma serum immunoglobulin A1.
7215351	6	22	from	A1	1496:1497	arg1	residues					1433:1440	serine residues	1426:1440	serine residues of the hinge region from myeloma serum immunoglobulin A1	1426:1497	These oligosaccharides are more complex and heterogenous than the oligosaccharides linked to serine residues of the hinge region from myeloma serum immunoglobulin A1.
7215351	6	22	from	A1	1496:1497	arg1	region					1455:1460	the hinge region	1445:1460	the hinge region from myeloma serum immunoglobulin A1	1445:1497	These oligosaccharides are more complex and heterogenous than the oligosaccharides linked to serine residues of the hinge region from myeloma serum immunoglobulin A1.
7215351	0	23	theme	glycans	21:27	arg1	Heterogeneity					0:12	Heterogeneity	0:12	Heterogeneity of the glycans	0:27	Heterogeneity of the glycans O-glycosidically linked to the hinge region of secretory immunoglobulins from human milk.
7215351	2	24	theme	gel	423:425	arg1	filtration					427:436	gel filtration	423:436	gel filtration	423:436	The hinge region containing all the O-glycosidically linked oligosaccharides was isolated en bloc after trypsin and pepsin hydrolysis and separated by gel filtration.
7215351	2	25	theme	hinge	276:280	arg1	region					282:287	The hinge region	272:287	The hinge region containing all the O-glycosidically linked oligosaccharides	272:347	The hinge region containing all the O-glycosidically linked oligosaccharides was isolated en bloc after trypsin and pepsin hydrolysis and separated by gel filtration.
7215351	3	26	theme	linked	471:476	arg1	oligosaccharides					478:493	O-glycosidically linked oligosaccharides	454:493	O-glycosidically linked oligosaccharides	454:493	The mixture of O-glycosidically linked oligosaccharides contained N-acetylneuraminic acid (NeuAc), fucose (Fuc), galactose (Gal), N-acetylglucosamine (GlcNAc) and N-acetylgalactosamine (GalNAc) in the molar ratio of 0.2:0.5:2.5:2:1 respectively.
7215351	2	27	theme	linked	325:330	arg1	oligosaccharides					332:347	all the O-glycosidically linked oligosaccharides	300:347	all the O-glycosidically linked oligosaccharides	300:347	The hinge region containing all the O-glycosidically linked oligosaccharides was isolated en bloc after trypsin and pepsin hydrolysis and separated by gel filtration.
7215351	6	28	theme	serum	1475:1479	arg1	A1					1496:1497	myeloma serum immunoglobulin A1	1467:1497	myeloma serum immunoglobulin A1	1467:1497	These oligosaccharides are more complex and heterogenous than the oligosaccharides linked to serine residues of the hinge region from myeloma serum immunoglobulin A1.
7215351	0	29	gly	Heterogeneity	0:12	arg1	glycans					21:27	the glycans	17:27	the glycans	17:27	Heterogeneity of the glycans O-glycosidically linked to the hinge region of secretory immunoglobulins from human milk.
7215351	5	30	theme	oligosaccharides	871:886	arg1	oligosaccharides					871:886	these oligosaccharides	865:886	these oligosaccharides	865:886	The complete structure of four of these oligosaccharides was determined by methanolysis, methylation and mass spectrometry.
7215351	5	30	theme	oligosaccharides	871:886	arg1	four					857:860	four	857:860	four	857:860	The complete structure of four of these oligosaccharides was determined by methanolysis, methylation and mass spectrometry.
7215351	0	31	from	region	66:71	arg1	milk					113:116	human milk	107:116	human milk	107:116	Heterogeneity of the glycans O-glycosidically linked to the hinge region of secretory immunoglobulins from human milk.
7215351	6	32	theme	hinge	1449:1453	arg1	region					1455:1460	the hinge region	1445:1460	the hinge region from myeloma serum immunoglobulin A1	1445:1497	These oligosaccharides are more complex and heterogenous than the oligosaccharides linked to serine residues of the hinge region from myeloma serum immunoglobulin A1.
7215351	1	33	theme	pH	213:214	arg1	gradients					200:208	gradients	200:208	gradients of pH and (NH4)2SO4 concentration followed by gel filtration	200:269	Pure secretory immunoglobulin A was isolated from human milk by fractionation in gradients of pH and (NH4)2SO4 concentration followed by gel filtration.
7215351	6	34	theme	myeloma	1467:1473	arg1	A1					1496:1497	myeloma serum immunoglobulin A1	1467:1497	myeloma serum immunoglobulin A1	1467:1497	These oligosaccharides are more complex and heterogenous than the oligosaccharides linked to serine residues of the hinge region from myeloma serum immunoglobulin A1.
7215351	3	35	theme	N-acetylneuraminic	505:522	arg1	NeuAc					530:534	NeuAc	530:534	NeuAc	530:534	The mixture of O-glycosidically linked oligosaccharides contained N-acetylneuraminic acid (NeuAc), fucose (Fuc), galactose (Gal), N-acetylglucosamine (GlcNAc) and N-acetylgalactosamine (GalNAc) in the molar ratio of 0.2:0.5:2.5:2:1 respectively.
7215351	3	35	theme	N-acetylneuraminic	505:522	arg1	fucose					538:543	fucose	538:543	fucose (Fuc)	538:549	The mixture of O-glycosidically linked oligosaccharides contained N-acetylneuraminic acid (NeuAc), fucose (Fuc), galactose (Gal), N-acetylglucosamine (GlcNAc) and N-acetylgalactosamine (GalNAc) in the molar ratio of 0.2:0.5:2.5:2:1 respectively.
7215351	3	35	theme	N-acetylneuraminic	505:522	arg1	acid					524:527	N-acetylneuraminic acid	505:527	N-acetylneuraminic acid (NeuAc)	505:535	The mixture of O-glycosidically linked oligosaccharides contained N-acetylneuraminic acid (NeuAc), fucose (Fuc), galactose (Gal), N-acetylglucosamine (GlcNAc) and N-acetylgalactosamine (GalNAc) in the molar ratio of 0.2:0.5:2.5:2:1 respectively.
7215351	2	36	contain	containing	289:298	arg1	region					282:287	The hinge region	272:287	The hinge region containing all the O-glycosidically linked oligosaccharides	272:347	The hinge region containing all the O-glycosidically linked oligosaccharides was isolated en bloc after trypsin and pepsin hydrolysis and separated by gel filtration.
7215351	2	36	contain	containing	289:298	arg2	oligosaccharides					332:347	all the O-glycosidically linked oligosaccharides	300:347	all the O-glycosidically linked oligosaccharides	300:347	The hinge region containing all the O-glycosidically linked oligosaccharides was isolated en bloc after trypsin and pepsin hydrolysis and separated by gel filtration.
7215351	0	37	from	milk	113:116	arg1	region					66:71	the hinge region	56:71	the hinge region of secretory immunoglobulins from human milk	56:116	Heterogeneity of the glycans O-glycosidically linked to the hinge region of secretory immunoglobulins from human milk.
7215351	0	37	from	milk	113:116	arg1	immunoglobulins					86:100	secretory immunoglobulins	76:100	secretory immunoglobulins from human milk	76:116	Heterogeneity of the glycans O-glycosidically linked to the hinge region of secretory immunoglobulins from human milk.
7215351	1	38	theme	Pure	119:122	arg1	A					149:149	Pure secretory immunoglobulin A	119:149	Pure secretory immunoglobulin A	119:149	Pure secretory immunoglobulin A was isolated from human milk by fractionation in gradients of pH and (NH4)2SO4 concentration followed by gel filtration.
7215351	4	39	theme	chromatography	815:828	arg1	combination					753:763	a combination	751:763	a combination of ion-exchange chromatography and gel-filtration chromatography	751:828	After beta-elimination several oligosaccharides were separated by a combination of ion-exchange chromatography and gel-filtration chromatography.
7215351	2	40	dep	trypsin	376:382	arg1	hydrolysis					395:404	hydrolysis	395:404	hydrolysis	395:404	The hinge region containing all the O-glycosidically linked oligosaccharides was isolated en bloc after trypsin and pepsin hydrolysis and separated by gel filtration.
7215351	6	41	theme	region	1455:1460	arg1	residues					1433:1440	serine residues	1426:1440	serine residues of the hinge region from myeloma serum immunoglobulin A1	1426:1497	These oligosaccharides are more complex and heterogenous than the oligosaccharides linked to serine residues of the hinge region from myeloma serum immunoglobulin A1.
7215351	6	41	theme	region	1455:1460	arg1	region					1455:1460	the hinge region	1445:1460	the hinge region from myeloma serum immunoglobulin A1	1445:1497	These oligosaccharides are more complex and heterogenous than the oligosaccharides linked to serine residues of the hinge region from myeloma serum immunoglobulin A1.
7215351	1	42	theme	secretory	124:132	arg1	A					149:149	Pure secretory immunoglobulin A	119:149	Pure secretory immunoglobulin A	119:149	Pure secretory immunoglobulin A was isolated from human milk by fractionation in gradients of pH and (NH4)2SO4 concentration followed by gel filtration.
7215351	4	43	theme	gel-filtration	800:813	arg1	chromatography					815:828	gel-filtration chromatography	800:828	gel-filtration chromatography	800:828	After beta-elimination several oligosaccharides were separated by a combination of ion-exchange chromatography and gel-filtration chromatography.
7215351	1	44	theme	immunoglobulin	134:147	arg1	A					149:149	Pure secretory immunoglobulin A	119:149	Pure secretory immunoglobulin A	119:149	Pure secretory immunoglobulin A was isolated from human milk by fractionation in gradients of pH and (NH4)2SO4 concentration followed by gel filtration.
7215351	3	45	theme	oligosaccharides	478:493	arg1	mixture					443:449	The mixture	439:449	The mixture of O-glycosidically linked oligosaccharides	439:493	The mixture of O-glycosidically linked oligosaccharides contained N-acetylneuraminic acid (NeuAc), fucose (Fuc), galactose (Gal), N-acetylglucosamine (GlcNAc) and N-acetylgalactosamine (GalNAc) in the molar ratio of 0.2:0.5:2.5:2:1 respectively.
7215351	3	46	theme	molar	640:644	arg1	ratio					646:650	the molar ratio	636:650	the molar ratio of 0.2:0.5:2.5:2:1	636:669	The mixture of O-glycosidically linked oligosaccharides contained N-acetylneuraminic acid (NeuAc), fucose (Fuc), galactose (Gal), N-acetylglucosamine (GlcNAc) and N-acetylgalactosamine (GalNAc) in the molar ratio of 0.2:0.5:2.5:2:1 respectively.
7215351	1	47	from	fractionation	183:195	arg1	gradients					200:208	gradients	200:208	gradients of pH and (NH4)2SO4 concentration followed by gel filtration	200:269	Pure secretory immunoglobulin A was isolated from human milk by fractionation in gradients of pH and (NH4)2SO4 concentration followed by gel filtration.
7215351	1	48	theme	NH4	221:223	arg1	concentration					230:242	(NH4)2SO4 concentration	220:242	(NH4)2SO4 concentration	220:242	Pure secretory immunoglobulin A was isolated from human milk by fractionation in gradients of pH and (NH4)2SO4 concentration followed by gel filtration.
7215351	0	49	theme	hinge	60:64	arg1	region					66:71	the hinge region	56:71	the hinge region of secretory immunoglobulins from human milk	56:116	Heterogeneity of the glycans O-glycosidically linked to the hinge region of secretory immunoglobulins from human milk.
7215351	5	50	theme	four	857:860	arg1	structure					844:852	The complete structure	831:852	The complete structure of four of these oligosaccharides	831:886	The complete structure of four of these oligosaccharides was determined by methanolysis, methylation and mass spectrometry.
7215351	6	51	attach	linked	1416:1421	arg1	residues					1433:1440	serine residues	1426:1440	serine residues of the hinge region from myeloma serum immunoglobulin A1	1426:1497	These oligosaccharides are more complex and heterogenous than the oligosaccharides linked to serine residues of the hinge region from myeloma serum immunoglobulin A1.
7215351	6	51	attach	linked	1416:1421	arg2	oligosaccharides					1399:1414	the oligosaccharides	1395:1414	the oligosaccharides linked to serine residues of the hinge region from myeloma serum immunoglobulin A1	1395:1497	These oligosaccharides are more complex and heterogenous than the oligosaccharides linked to serine residues of the hinge region from myeloma serum immunoglobulin A1.
7215351	6	51	attach	linked	1416:1421	arg1	region					1455:1460	the hinge region	1445:1460	the hinge region from myeloma serum immunoglobulin A1	1445:1497	These oligosaccharides are more complex and heterogenous than the oligosaccharides linked to serine residues of the hinge region from myeloma serum immunoglobulin A1.
7215351	2	52	theme	en	362:363	arg1	bloc					365:368	en bloc	362:368	en bloc	362:368	The hinge region containing all the O-glycosidically linked oligosaccharides was isolated en bloc after trypsin and pepsin hydrolysis and separated by gel filtration.
1280920	6	0	gly	desialylation	670:682	arg1	components					752:761	middle size P2 components	737:761	middle size P2 components	737:761	The desialylation of the other components indicated the largest P1 and middle size P2 components possibly corresponded to a disialylated structure, NeuAc alpha 2,3Gal beta 1,3(NeuAc alpha 2,6)GalNAc-PA, and a monosialylated component, NeuAc alpha 2,3Gal beta 1,3GalNAc-PA, respectively.
1280920	6	0	gly	desialylation	670:682	arg1	components					697:706	the other components	687:706	the other components indicated the largest P1	687:731	The desialylation of the other components indicated the largest P1 and middle size P2 components possibly corresponded to a disialylated structure, NeuAc alpha 2,3Gal beta 1,3(NeuAc alpha 2,6)GalNAc-PA, and a monosialylated component, NeuAc alpha 2,3Gal beta 1,3GalNAc-PA, respectively.
1280920	9	1	from	control	1193:1199	arg1	%					1144:1144	%	1144:1144	%	1144:1144	The relative content (%) of P1-P4 (glycoform) in IgA1 from the healthy control was 10.1 +/- 3.3, 48.2 +/- 4.6, 7.0 +/- 2.6, and 34.7 +/- 4.5.
1280920	9	1	from	control	1193:1199	arg1	IgA1					1171:1174	IgA1	1171:1174	IgA1 from the healthy control	1171:1199	The relative content (%) of P1-P4 (glycoform) in IgA1 from the healthy control was 10.1 +/- 3.3, 48.2 +/- 4.6, 7.0 +/- 2.6, and 34.7 +/- 4.5.
1280920	9	1	from	control	1193:1199	arg1	10.1					1205:1208	10.1	1205:1208	10.1	1205:1208	The relative content (%) of P1-P4 (glycoform) in IgA1 from the healthy control was 10.1 +/- 3.3, 48.2 +/- 4.6, 7.0 +/- 2.6, and 34.7 +/- 4.5.
1280920	9	1	from	control	1193:1199	arg1	content					1135:1141	The relative content	1122:1141	The relative content (%) of P1-P4 (glycoform) in IgA1 from the healthy control	1122:1199	The relative content (%) of P1-P4 (glycoform) in IgA1 from the healthy control was 10.1 +/- 3.3, 48.2 +/- 4.6, 7.0 +/- 2.6, and 34.7 +/- 4.5.
1280920	6	2	theme	beta	920:923	arg1	1,3GalNAc-PA					925:936	NeuAc alpha 2,3Gal beta 1,3GalNAc-PA	901:936	NeuAc alpha 2,3Gal beta 1,3GalNAc-PA	901:936	The desialylation of the other components indicated the largest P1 and middle size P2 components possibly corresponded to a disialylated structure, NeuAc alpha 2,3Gal beta 1,3(NeuAc alpha 2,6)GalNAc-PA, and a monosialylated component, NeuAc alpha 2,3Gal beta 1,3GalNAc-PA, respectively.
1280920	6	2	theme	beta	920:923	arg1	component					890:898	a monosialylated component	873:898	a monosialylated component	873:898	The desialylation of the other components indicated the largest P1 and middle size P2 components possibly corresponded to a disialylated structure, NeuAc alpha 2,3Gal beta 1,3(NeuAc alpha 2,6)GalNAc-PA, and a monosialylated component, NeuAc alpha 2,3Gal beta 1,3GalNAc-PA, respectively.
1280920	12	3	dep	5:24:3:68	1552:1560	arg1	II					1568:1569	Type II	1563:1569	Type II	1563:1569	The relative content of these component could be classed as 2:8:0:90 (Type I, only one case designated as Kita), 5:24:3:68 (Type II, seven cases), and 9:41:5:45 (Type III, four cases).
1280920	12	3	dep	5:24:3:68	1552:1560	arg1	cases					1578:1582	seven cases	1572:1582	seven cases	1572:1582	The relative content of these component could be classed as 2:8:0:90 (Type I, only one case designated as Kita), 5:24:3:68 (Type II, seven cases), and 9:41:5:45 (Type III, four cases).
1280920	5	4	theme	neutral	525:531	arg1	component					533:541	The neutral component	521:541	The neutral component (P4) among them	521:557	The neutral component (P4) among them was identified as Gal beta 1,3GalNAc-PA by cochromatography with an authentic standard pyridylamino sugar.
1280920	5	4	theme	neutral	525:531	arg1	1,3GalNAc-PA					586:597	Gal beta 1,3GalNAc-PA	577:597	Gal beta 1,3GalNAc-PA	577:597	The neutral component (P4) among them was identified as Gal beta 1,3GalNAc-PA by cochromatography with an authentic standard pyridylamino sugar.
1280920	5	4	theme	neutral	525:531	arg1	P4					544:545	P4	544:545	P4	544:545	The neutral component (P4) among them was identified as Gal beta 1,3GalNAc-PA by cochromatography with an authentic standard pyridylamino sugar.
1280920	6	5	theme	alpha	907:911	arg1	1,3GalNAc-PA					925:936	NeuAc alpha 2,3Gal beta 1,3GalNAc-PA	901:936	NeuAc alpha 2,3Gal beta 1,3GalNAc-PA	901:936	The desialylation of the other components indicated the largest P1 and middle size P2 components possibly corresponded to a disialylated structure, NeuAc alpha 2,3Gal beta 1,3(NeuAc alpha 2,6)GalNAc-PA, and a monosialylated component, NeuAc alpha 2,3Gal beta 1,3GalNAc-PA, respectively.
1280920	6	5	theme	alpha	907:911	arg1	component					890:898	a monosialylated component	873:898	a monosialylated component	873:898	The desialylation of the other components indicated the largest P1 and middle size P2 components possibly corresponded to a disialylated structure, NeuAc alpha 2,3Gal beta 1,3(NeuAc alpha 2,6)GalNAc-PA, and a monosialylated component, NeuAc alpha 2,3Gal beta 1,3GalNAc-PA, respectively.
1280920	6	6	theme	beta	833:836	arg1	GalNAc-PA					858:866	NeuAc alpha 2,3Gal beta 1,3(NeuAc alpha 2,6)GalNAc-PA	814:866	NeuAc alpha 2,3Gal beta 1,3(NeuAc alpha 2,6)GalNAc-PA	814:866	The desialylation of the other components indicated the largest P1 and middle size P2 components possibly corresponded to a disialylated structure, NeuAc alpha 2,3Gal beta 1,3(NeuAc alpha 2,6)GalNAc-PA, and a monosialylated component, NeuAc alpha 2,3Gal beta 1,3GalNAc-PA, respectively.
1280920	9	7	from	content	1135:1141	arg1	control					1193:1199	the healthy control	1181:1199	the healthy control	1181:1199	The relative content (%) of P1-P4 (glycoform) in IgA1 from the healthy control was 10.1 +/- 3.3, 48.2 +/- 4.6, 7.0 +/- 2.6, and 34.7 +/- 4.5.
1280920	9	7	from	content	1135:1141	arg1	IgA1					1171:1174	IgA1	1171:1174	IgA1 from the healthy control	1171:1199	The relative content (%) of P1-P4 (glycoform) in IgA1 from the healthy control was 10.1 +/- 3.3, 48.2 +/- 4.6, 7.0 +/- 2.6, and 34.7 +/- 4.5.
1280920	6	8	theme	alpha	820:824	arg1	beta					833:836	NeuAc alpha 2,3Gal beta 1,3	814:840	NeuAc alpha 2,3Gal beta 1,3(NeuAc alpha 2,6)GalNAc-PA	814:866	The desialylation of the other components indicated the largest P1 and middle size P2 components possibly corresponded to a disialylated structure, NeuAc alpha 2,3Gal beta 1,3(NeuAc alpha 2,6)GalNAc-PA, and a monosialylated component, NeuAc alpha 2,3Gal beta 1,3GalNAc-PA, respectively.
1280920	6	8	theme	alpha	820:824	arg1	alpha					848:852	NeuAc alpha 2,6	842:856	NeuAc alpha 2,6	842:856	The desialylation of the other components indicated the largest P1 and middle size P2 components possibly corresponded to a disialylated structure, NeuAc alpha 2,3Gal beta 1,3(NeuAc alpha 2,6)GalNAc-PA, and a monosialylated component, NeuAc alpha 2,3Gal beta 1,3GalNAc-PA, respectively.
1280920	1	9	theme	O-glycan	196:203	arg1	glycoform					183:191	the glycoform	179:191	the glycoform of O-glycan from human myeloma immunoglobulin A1	179:240	A comparative study was made on the glycoform of O-glycan from human myeloma immunoglobulin A1.
1280920	0	10	theme	oligosaccharides	129:144	arg1	pyridylamination					109:124	pyridylamination	109:124	pyridylamination of oligosaccharides	109:144	Analysis of glycoform of O-glycan from human myeloma immunoglobulin A1 by gas-phase hydrazinolysis following pyridylamination of oligosaccharides.
1280920	1	11	theme	human	210:214	arg1	A1					239:240	human myeloma immunoglobulin A1	210:240	human myeloma immunoglobulin A1	210:240	A comparative study was made on the glycoform of O-glycan from human myeloma immunoglobulin A1.
1280920	12	12	theme	Type	1509:1512	arg1	case					1526:1529	only one case	1517:1529	only one case designated as Kita	1517:1548	The relative content of these component could be classed as 2:8:0:90 (Type I, only one case designated as Kita), 5:24:3:68 (Type II, seven cases), and 9:41:5:45 (Type III, four cases).
1280920	12	12	theme	Type	1509:1512	arg1	I					1514:1514	Type I	1509:1514	Type I	1509:1514	The relative content of these component could be classed as 2:8:0:90 (Type I, only one case designated as Kita), 5:24:3:68 (Type II, seven cases), and 9:41:5:45 (Type III, four cases).
1280920	11	13	theme	distinct	1394:1401	arg1	glycoforms					1383:1392	glycoforms	1383:1392	glycoforms distinct from those of the healthy controls	1383:1436	Analysis of IgA1 myeloma protein indicated glycoforms distinct from those of the healthy controls.
1280920	1	14	theme	immunoglobulin	224:237	arg1	A1					239:240	human myeloma immunoglobulin A1	210:240	human myeloma immunoglobulin A1	210:240	A comparative study was made on the glycoform of O-glycan from human myeloma immunoglobulin A1.
1280920	5	15	theme	Gal	577:579	arg1	component					533:541	The neutral component	521:541	The neutral component (P4) among them	521:557	The neutral component (P4) among them was identified as Gal beta 1,3GalNAc-PA by cochromatography with an authentic standard pyridylamino sugar.
1280920	5	15	theme	Gal	577:579	arg1	1,3GalNAc-PA					586:597	Gal beta 1,3GalNAc-PA	577:597	Gal beta 1,3GalNAc-PA	577:597	The neutral component (P4) among them was identified as Gal beta 1,3GalNAc-PA by cochromatography with an authentic standard pyridylamino sugar.
1280920	6	16	theme	NeuAc	842:846	arg1	beta					833:836	NeuAc alpha 2,3Gal beta 1,3	814:840	NeuAc alpha 2,3Gal beta 1,3(NeuAc alpha 2,6)GalNAc-PA	814:866	The desialylation of the other components indicated the largest P1 and middle size P2 components possibly corresponded to a disialylated structure, NeuAc alpha 2,3Gal beta 1,3(NeuAc alpha 2,6)GalNAc-PA, and a monosialylated component, NeuAc alpha 2,3Gal beta 1,3GalNAc-PA, respectively.
1280920	6	16	theme	NeuAc	842:846	arg1	alpha					848:852	NeuAc alpha 2,6	842:856	NeuAc alpha 2,6	842:856	The desialylation of the other components indicated the largest P1 and middle size P2 components possibly corresponded to a disialylated structure, NeuAc alpha 2,3Gal beta 1,3(NeuAc alpha 2,6)GalNAc-PA, and a monosialylated component, NeuAc alpha 2,3Gal beta 1,3GalNAc-PA, respectively.
1280920	6	17	theme	other	691:695	arg1	components					697:706	the other components	687:706	the other components indicated the largest P1	687:731	The desialylation of the other components indicated the largest P1 and middle size P2 components possibly corresponded to a disialylated structure, NeuAc alpha 2,3Gal beta 1,3(NeuAc alpha 2,6)GalNAc-PA, and a monosialylated component, NeuAc alpha 2,3Gal beta 1,3GalNAc-PA, respectively.
1280920	6	18	theme	largest	722:728	arg1	P1					730:731	the largest P1	718:731	the largest P1	718:731	The desialylation of the other components indicated the largest P1 and middle size P2 components possibly corresponded to a disialylated structure, NeuAc alpha 2,3Gal beta 1,3(NeuAc alpha 2,6)GalNAc-PA, and a monosialylated component, NeuAc alpha 2,3Gal beta 1,3GalNAc-PA, respectively.
1280920	13	19	theme	IgA1	1646:1649	arg1	protein					1659:1665	IgA1 myeloma protein	1646:1665	IgA1 myeloma protein	1646:1665	Thus, the results for IgA1 myeloma protein indicate that at least three glycoforms of O-glycan are possible for the IgA1 hinge structure.
1280920	10	20	gly	glycoform	1268:1276	arg1	O-glycan					1281:1288	O-glycan	1281:1288	O-glycan	1281:1288	The glycoform of O-glycan on IgA1 thus appears the same for any individual.
1280920	10	20	gly	glycoform	1268:1276	arg2	IgA1					1293:1296	IgA1	1293:1296	IgA1	1293:1296	The glycoform of O-glycan on IgA1 thus appears the same for any individual.
1280920	4	21	theme	major	467:471	arg1	P1-P4					499:503	P1-P4	499:503	P1-P4	499:503	Four major pyridylamino derivatives (P1-P4) were obtained.
1280920	4	21	theme	major	467:471	arg1	derivatives					486:496	Four major pyridylamino derivatives	462:496	Four major pyridylamino derivatives (P1-P4)	462:504	Four major pyridylamino derivatives (P1-P4) were obtained.
1280920	11	22	theme	myeloma	1357:1363	arg1	protein					1365:1371	IgA1 myeloma protein	1352:1371	IgA1 myeloma protein	1352:1371	Analysis of IgA1 myeloma protein indicated glycoforms distinct from those of the healthy controls.
1280920	0	23	theme	immunoglobulin	53:66	arg1	A1					68:69	human myeloma immunoglobulin A1	39:69	human myeloma immunoglobulin A1	39:69	Analysis of glycoform of O-glycan from human myeloma immunoglobulin A1 by gas-phase hydrazinolysis following pyridylamination of oligosaccharides.
1280920	0	24	from	glycoform	12:20	arg1	A1					68:69	human myeloma immunoglobulin A1	39:69	human myeloma immunoglobulin A1	39:69	Analysis of glycoform of O-glycan from human myeloma immunoglobulin A1 by gas-phase hydrazinolysis following pyridylamination of oligosaccharides.
1280920	11	25	theme	healthy	1421:1427	arg1	controls					1429:1436	the healthy controls	1417:1436	the healthy controls	1417:1436	Analysis of IgA1 myeloma protein indicated glycoforms distinct from those of the healthy controls.
1280920	12	26	theme	Type	1563:1566	arg1	II					1568:1569	Type II	1563:1569	Type II	1563:1569	The relative content of these component could be classed as 2:8:0:90 (Type I, only one case designated as Kita), 5:24:3:68 (Type II, seven cases), and 9:41:5:45 (Type III, four cases).
1280920	12	26	theme	Type	1563:1566	arg1	cases					1578:1582	seven cases	1572:1582	seven cases	1572:1582	The relative content of these component could be classed as 2:8:0:90 (Type I, only one case designated as Kita), 5:24:3:68 (Type II, seven cases), and 9:41:5:45 (Type III, four cases).
1280920	13	27	theme	O-glycan	1710:1717	arg1	glycoforms					1696:1705	at least three glycoforms	1681:1705	at least three glycoforms of O-glycan	1681:1717	Thus, the results for IgA1 myeloma protein indicate that at least three glycoforms of O-glycan are possible for the IgA1 hinge structure.
1280920	5	28	theme	standard	637:644	arg1	sugar					659:663	an authentic standard pyridylamino sugar	624:663	an authentic standard pyridylamino sugar	624:663	The neutral component (P4) among them was identified as Gal beta 1,3GalNAc-PA by cochromatography with an authentic standard pyridylamino sugar.
1280920	6	29	gly	disialylated	790:801	arg1	structure					803:811	a disialylated structure	788:811	a disialylated structure	788:811	The desialylation of the other components indicated the largest P1 and middle size P2 components possibly corresponded to a disialylated structure, NeuAc alpha 2,3Gal beta 1,3(NeuAc alpha 2,6)GalNAc-PA, and a monosialylated component, NeuAc alpha 2,3Gal beta 1,3GalNAc-PA, respectively.
1280920	6	30	theme	size	744:747	arg1	components					752:761	middle size P2 components	737:761	middle size P2 components	737:761	The desialylation of the other components indicated the largest P1 and middle size P2 components possibly corresponded to a disialylated structure, NeuAc alpha 2,3Gal beta 1,3(NeuAc alpha 2,6)GalNAc-PA, and a monosialylated component, NeuAc alpha 2,3Gal beta 1,3GalNAc-PA, respectively.
1280920	8	31	theme	relative	1072:1079	arg1	content					1081:1087	relative content	1072:1087	relative content (P1:P2: P3:P:4)	1072:1103	Four similar components were also detected in bovine fetuin whose relative content (P1:P2: P3:P:4) was 16:43:19:22.
1280920	7	32	theme	structural	957:966	arg1	incomplete					994:1003	incomplete	994:1003	incomplete	994:1003	The structural assignment of P3 is still incomplete.
1280920	7	32	theme	structural	957:966	arg1	assignment					968:977	The structural assignment	953:977	The structural assignment of P3	953:983	The structural assignment of P3 is still incomplete.
1280920	1	33	theme	comparative	149:159	arg1	study					161:165	A comparative study	147:165	A comparative study	147:165	A comparative study was made on the glycoform of O-glycan from human myeloma immunoglobulin A1.
1280920	3	34	theme	analytical	402:411	arg1	method					413:418	a two-dimensional analytical method	384:418	a two-dimensional analytical method of gel filtration and reverse-phase HPLC	384:459	The released oligosaccharide was pyridylaminated and separated by a two-dimensional analytical method of gel filtration and reverse-phase HPLC.
1280920	11	35	theme	protein	1365:1371	arg1	Analysis					1340:1347	Analysis	1340:1347	Analysis of IgA1 myeloma protein	1340:1371	Analysis of IgA1 myeloma protein indicated glycoforms distinct from those of the healthy controls.
1280920	0	36	theme	glycoform	12:20	arg1	Analysis					0:7	Analysis	0:7	Analysis of glycoform of O-glycan from human myeloma immunoglobulin A1 by gas-phase hydrazinolysis	0:97	Analysis of glycoform of O-glycan from human myeloma immunoglobulin A1 by gas-phase hydrazinolysis following pyridylamination of oligosaccharides.
1280920	3	37	theme	reverse-phase	442:454	arg1	HPLC					456:459	reverse-phase HPLC	442:459	reverse-phase HPLC	442:459	The released oligosaccharide was pyridylaminated and separated by a two-dimensional analytical method of gel filtration and reverse-phase HPLC.
1280920	11	38	theme	IgA1	1352:1355	arg1	protein					1365:1371	IgA1 myeloma protein	1352:1371	IgA1 myeloma protein	1352:1371	Analysis of IgA1 myeloma protein indicated glycoforms distinct from those of the healthy controls.
1280920	0	39	theme	O-glycan	25:32	arg1	glycoform					12:20	glycoform	12:20	glycoform of O-glycan from human myeloma immunoglobulin A1	12:69	Analysis of glycoform of O-glycan from human myeloma immunoglobulin A1 by gas-phase hydrazinolysis following pyridylamination of oligosaccharides.
1280920	10	40	from	glycoform	1268:1276	arg1	IgA1					1293:1296	IgA1	1293:1296	IgA1	1293:1296	The glycoform of O-glycan on IgA1 thus appears the same for any individual.
1280920	3	41	theme	filtration	427:436	arg1	method					413:418	a two-dimensional analytical method	384:418	a two-dimensional analytical method of gel filtration and reverse-phase HPLC	384:459	The released oligosaccharide was pyridylaminated and separated by a two-dimensional analytical method of gel filtration and reverse-phase HPLC.
1280920	0	42	theme	human	39:43	arg1	A1					68:69	human myeloma immunoglobulin A1	39:69	human myeloma immunoglobulin A1	39:69	Analysis of glycoform of O-glycan from human myeloma immunoglobulin A1 by gas-phase hydrazinolysis following pyridylamination of oligosaccharides.
1280920	13	43	theme	IgA1	1740:1743	arg1	structure					1751:1759	the IgA1 hinge structure	1736:1759	the IgA1 hinge structure	1736:1759	Thus, the results for IgA1 myeloma protein indicate that at least three glycoforms of O-glycan are possible for the IgA1 hinge structure.
1280920	9	44	theme	relative	1126:1133	arg1	%					1144:1144	%	1144:1144	%	1144:1144	The relative content (%) of P1-P4 (glycoform) in IgA1 from the healthy control was 10.1 +/- 3.3, 48.2 +/- 4.6, 7.0 +/- 2.6, and 34.7 +/- 4.5.
1280920	9	44	theme	relative	1126:1133	arg1	10.1					1205:1208	10.1	1205:1208	10.1	1205:1208	The relative content (%) of P1-P4 (glycoform) in IgA1 from the healthy control was 10.1 +/- 3.3, 48.2 +/- 4.6, 7.0 +/- 2.6, and 34.7 +/- 4.5.
1280920	9	44	theme	relative	1126:1133	arg1	content					1135:1141	The relative content	1122:1141	The relative content (%) of P1-P4 (glycoform) in IgA1 from the healthy control	1122:1199	The relative content (%) of P1-P4 (glycoform) in IgA1 from the healthy control was 10.1 +/- 3.3, 48.2 +/- 4.6, 7.0 +/- 2.6, and 34.7 +/- 4.5.
1280920	8	45	dep	P1	1090:1091	arg1	P:4					1100:1102	P:4	1100:1102	P:4	1100:1102	Four similar components were also detected in bovine fetuin whose relative content (P1:P2: P3:P:4) was 16:43:19:22.
1280920	8	45	dep	P1	1090:1091	arg1	P3					1097:1098	P3	1097:1098	P1:P2: P3:P:4	1090:1102	Four similar components were also detected in bovine fetuin whose relative content (P1:P2: P3:P:4) was 16:43:19:22.
1280920	8	45	dep	P1	1090:1091	arg1	P2					1093:1094	P2	1093:1094	P1:P2: P3:P:4	1090:1102	Four similar components were also detected in bovine fetuin whose relative content (P1:P2: P3:P:4) was 16:43:19:22.
1280920	8	46	dep	content	1081:1087	arg1	P1					1090:1091	P1	1090:1091	P1:P2: P3:P:4	1090:1102	Four similar components were also detected in bovine fetuin whose relative content (P1:P2: P3:P:4) was 16:43:19:22.
1280920	1	47	gly	glycoform	183:191	arg1	O-glycan					196:203	O-glycan	196:203	O-glycan	196:203	A comparative study was made on the glycoform of O-glycan from human myeloma immunoglobulin A1.
1280920	6	48	theme	components	752:761	arg1	desialylation					670:682	The desialylation	666:682	The desialylation of the other components indicated the largest P1 and middle size P2 components	666:761	The desialylation of the other components indicated the largest P1 and middle size P2 components possibly corresponded to a disialylated structure, NeuAc alpha 2,3Gal beta 1,3(NeuAc alpha 2,6)GalNAc-PA, and a monosialylated component, NeuAc alpha 2,3Gal beta 1,3GalNAc-PA, respectively.
1280920	13	49	theme	hinge	1745:1749	arg1	structure					1751:1759	the IgA1 hinge structure	1736:1759	the IgA1 hinge structure	1736:1759	Thus, the results for IgA1 myeloma protein indicate that at least three glycoforms of O-glycan are possible for the IgA1 hinge structure.
1280920	9	50	theme	P1-P4	1150:1154	arg1	%					1144:1144	%	1144:1144	%	1144:1144	The relative content (%) of P1-P4 (glycoform) in IgA1 from the healthy control was 10.1 +/- 3.3, 48.2 +/- 4.6, 7.0 +/- 2.6, and 34.7 +/- 4.5.
1280920	9	50	theme	P1-P4	1150:1154	arg1	10.1					1205:1208	10.1	1205:1208	10.1	1205:1208	The relative content (%) of P1-P4 (glycoform) in IgA1 from the healthy control was 10.1 +/- 3.3, 48.2 +/- 4.6, 7.0 +/- 2.6, and 34.7 +/- 4.5.
1280920	9	50	theme	P1-P4	1150:1154	arg1	content					1135:1141	The relative content	1122:1141	The relative content (%) of P1-P4 (glycoform) in IgA1 from the healthy control	1122:1199	The relative content (%) of P1-P4 (glycoform) in IgA1 from the healthy control was 10.1 +/- 3.3, 48.2 +/- 4.6, 7.0 +/- 2.6, and 34.7 +/- 4.5.
1280920	2	51	theme	hinge	303:307	arg1	portion					309:315	its hinge portion	299:315	its hinge portion	299:315	By gas-phase hydrazinolysis, O-glycan was released from its hinge portion.
1280920	6	52	theme	2,3Gal	913:918	arg1	1,3GalNAc-PA					925:936	NeuAc alpha 2,3Gal beta 1,3GalNAc-PA	901:936	NeuAc alpha 2,3Gal beta 1,3GalNAc-PA	901:936	The desialylation of the other components indicated the largest P1 and middle size P2 components possibly corresponded to a disialylated structure, NeuAc alpha 2,3Gal beta 1,3(NeuAc alpha 2,6)GalNAc-PA, and a monosialylated component, NeuAc alpha 2,3Gal beta 1,3GalNAc-PA, respectively.
1280920	6	52	theme	2,3Gal	913:918	arg1	component					890:898	a monosialylated component	873:898	a monosialylated component	873:898	The desialylation of the other components indicated the largest P1 and middle size P2 components possibly corresponded to a disialylated structure, NeuAc alpha 2,3Gal beta 1,3(NeuAc alpha 2,6)GalNAc-PA, and a monosialylated component, NeuAc alpha 2,3Gal beta 1,3GalNAc-PA, respectively.
1280920	8	53	theme	similar	1011:1017	arg1	components					1019:1028	Four similar components	1006:1028	Four similar components	1006:1028	Four similar components were also detected in bovine fetuin whose relative content (P1:P2: P3:P:4) was 16:43:19:22.
1280920	8	54	located	detected	1040:1047	arg1	fetuin					1059:1064	bovine fetuin	1052:1064	bovine fetuin whose relative content (P1:P2: P3:P:4) was 16:43:19:22	1052:1119	Four similar components were also detected in bovine fetuin whose relative content (P1:P2: P3:P:4) was 16:43:19:22.
1280920	8	54	located	detected	1040:1047	arg2	components					1019:1028	Four similar components	1006:1028	Four similar components	1006:1028	Four similar components were also detected in bovine fetuin whose relative content (P1:P2: P3:P:4) was 16:43:19:22.
1280920	10	55	theme	O-glycan	1281:1288	arg1	glycoform					1268:1276	The glycoform	1264:1276	The glycoform of O-glycan on IgA1	1264:1296	The glycoform of O-glycan on IgA1 thus appears the same for any individual.
1280920	6	56	theme	NeuAc	901:905	arg1	1,3GalNAc-PA					925:936	NeuAc alpha 2,3Gal beta 1,3GalNAc-PA	901:936	NeuAc alpha 2,3Gal beta 1,3GalNAc-PA	901:936	The desialylation of the other components indicated the largest P1 and middle size P2 components possibly corresponded to a disialylated structure, NeuAc alpha 2,3Gal beta 1,3(NeuAc alpha 2,6)GalNAc-PA, and a monosialylated component, NeuAc alpha 2,3Gal beta 1,3GalNAc-PA, respectively.
1280920	6	56	theme	NeuAc	901:905	arg1	component					890:898	a monosialylated component	873:898	a monosialylated component	873:898	The desialylation of the other components indicated the largest P1 and middle size P2 components possibly corresponded to a disialylated structure, NeuAc alpha 2,3Gal beta 1,3(NeuAc alpha 2,6)GalNAc-PA, and a monosialylated component, NeuAc alpha 2,3Gal beta 1,3GalNAc-PA, respectively.
1280920	12	57	dep	2:8:0:90	1499:1506	arg1	case					1526:1529	only one case	1517:1529	only one case designated as Kita	1517:1548	The relative content of these component could be classed as 2:8:0:90 (Type I, only one case designated as Kita), 5:24:3:68 (Type II, seven cases), and 9:41:5:45 (Type III, four cases).
1280920	12	57	dep	2:8:0:90	1499:1506	arg1	I					1514:1514	Type I	1509:1514	Type I	1509:1514	The relative content of these component could be classed as 2:8:0:90 (Type I, only one case designated as Kita), 5:24:3:68 (Type II, seven cases), and 9:41:5:45 (Type III, four cases).
1280920	6	58	theme	2,3Gal	826:831	arg1	beta					833:836	NeuAc alpha 2,3Gal beta 1,3	814:840	NeuAc alpha 2,3Gal beta 1,3(NeuAc alpha 2,6)GalNAc-PA	814:866	The desialylation of the other components indicated the largest P1 and middle size P2 components possibly corresponded to a disialylated structure, NeuAc alpha 2,3Gal beta 1,3(NeuAc alpha 2,6)GalNAc-PA, and a monosialylated component, NeuAc alpha 2,3Gal beta 1,3GalNAc-PA, respectively.
1280920	6	58	theme	2,3Gal	826:831	arg1	alpha					848:852	NeuAc alpha 2,6	842:856	NeuAc alpha 2,6	842:856	The desialylation of the other components indicated the largest P1 and middle size P2 components possibly corresponded to a disialylated structure, NeuAc alpha 2,3Gal beta 1,3(NeuAc alpha 2,6)GalNAc-PA, and a monosialylated component, NeuAc alpha 2,3Gal beta 1,3GalNAc-PA, respectively.
1280920	5	59	with	cochromatography	602:617	arg1	sugar					659:663	an authentic standard pyridylamino sugar	624:663	an authentic standard pyridylamino sugar	624:663	The neutral component (P4) among them was identified as Gal beta 1,3GalNAc-PA by cochromatography with an authentic standard pyridylamino sugar.
1280920	6	60	theme	NeuAc	814:818	arg1	beta					833:836	NeuAc alpha 2,3Gal beta 1,3	814:840	NeuAc alpha 2,3Gal beta 1,3(NeuAc alpha 2,6)GalNAc-PA	814:866	The desialylation of the other components indicated the largest P1 and middle size P2 components possibly corresponded to a disialylated structure, NeuAc alpha 2,3Gal beta 1,3(NeuAc alpha 2,6)GalNAc-PA, and a monosialylated component, NeuAc alpha 2,3Gal beta 1,3GalNAc-PA, respectively.
1280920	6	60	theme	NeuAc	814:818	arg1	alpha					848:852	NeuAc alpha 2,6	842:856	NeuAc alpha 2,6	842:856	The desialylation of the other components indicated the largest P1 and middle size P2 components possibly corresponded to a disialylated structure, NeuAc alpha 2,3Gal beta 1,3(NeuAc alpha 2,6)GalNAc-PA, and a monosialylated component, NeuAc alpha 2,3Gal beta 1,3GalNAc-PA, respectively.
1280920	9	61	theme	healthy	1185:1191	arg1	control					1193:1199	the healthy control	1181:1199	the healthy control	1181:1199	The relative content (%) of P1-P4 (glycoform) in IgA1 from the healthy control was 10.1 +/- 3.3, 48.2 +/- 4.6, 7.0 +/- 2.6, and 34.7 +/- 4.5.
1280920	2	62	theme	gas-phase	246:254	arg1	hydrazinolysis					256:269	gas-phase hydrazinolysis	246:269	gas-phase hydrazinolysis	246:269	By gas-phase hydrazinolysis, O-glycan was released from its hinge portion.
1280920	1	63	theme	myeloma	216:222	arg1	A1					239:240	human myeloma immunoglobulin A1	210:240	human myeloma immunoglobulin A1	210:240	A comparative study was made on the glycoform of O-glycan from human myeloma immunoglobulin A1.
1280920	0	64	from	A1	68:69	arg1	glycoform					12:20	glycoform	12:20	glycoform of O-glycan from human myeloma immunoglobulin A1	12:69	Analysis of glycoform of O-glycan from human myeloma immunoglobulin A1 by gas-phase hydrazinolysis following pyridylamination of oligosaccharides.
1280920	0	64	from	A1	68:69	arg1	O-glycan					25:32	O-glycan	25:32	O-glycan from human myeloma immunoglobulin A1	25:69	Analysis of glycoform of O-glycan from human myeloma immunoglobulin A1 by gas-phase hydrazinolysis following pyridylamination of oligosaccharides.
1280920	2	65	attach	released	285:292	arg2	O-glycan					272:279	O-glycan	272:279	O-glycan	272:279	By gas-phase hydrazinolysis, O-glycan was released from its hinge portion.
1280920	2	65	attach	released	285:292	arg1	portion					309:315	its hinge portion	299:315	its hinge portion	299:315	By gas-phase hydrazinolysis, O-glycan was released from its hinge portion.
1280920	3	66	theme	released	322:329	arg1	oligosaccharide					331:345	The released oligosaccharide	318:345	The released oligosaccharide	318:345	The released oligosaccharide was pyridylaminated and separated by a two-dimensional analytical method of gel filtration and reverse-phase HPLC.
1280920	12	67	dep	9:41:5:45	1590:1598	arg1	Type					1601:1604	Type III	1601:1608	Type III	1601:1608	The relative content of these component could be classed as 2:8:0:90 (Type I, only one case designated as Kita), 5:24:3:68 (Type II, seven cases), and 9:41:5:45 (Type III, four cases).
1280920	12	67	dep	9:41:5:45	1590:1598	arg1	cases					1616:1620	four cases	1611:1620	four cases	1611:1620	The relative content of these component could be classed as 2:8:0:90 (Type I, only one case designated as Kita), 5:24:3:68 (Type II, seven cases), and 9:41:5:45 (Type III, four cases).
1280920	1	68	from	A1	239:240	arg1	glycoform					183:191	the glycoform	179:191	the glycoform of O-glycan from human myeloma immunoglobulin A1	179:240	A comparative study was made on the glycoform of O-glycan from human myeloma immunoglobulin A1.
1280920	5	69	theme	beta	581:584	arg1	component					533:541	The neutral component	521:541	The neutral component (P4) among them	521:557	The neutral component (P4) among them was identified as Gal beta 1,3GalNAc-PA by cochromatography with an authentic standard pyridylamino sugar.
1280920	5	69	theme	beta	581:584	arg1	1,3GalNAc-PA					586:597	Gal beta 1,3GalNAc-PA	577:597	Gal beta 1,3GalNAc-PA	577:597	The neutral component (P4) among them was identified as Gal beta 1,3GalNAc-PA by cochromatography with an authentic standard pyridylamino sugar.
1280920	4	70	theme	pyridylamino	473:484	arg1	P1-P4					499:503	P1-P4	499:503	P1-P4	499:503	Four major pyridylamino derivatives (P1-P4) were obtained.
1280920	4	70	theme	pyridylamino	473:484	arg1	derivatives					486:496	Four major pyridylamino derivatives	462:496	Four major pyridylamino derivatives (P1-P4)	462:504	Four major pyridylamino derivatives (P1-P4) were obtained.
1280920	12	71	theme	component	1469:1477	arg1	2:8:0:90					1499:1506	2:8:0:90	1499:1506	2:8:0:90	1499:1506	The relative content of these component could be classed as 2:8:0:90 (Type I, only one case designated as Kita), 5:24:3:68 (Type II, seven cases), and 9:41:5:45 (Type III, four cases).
1280920	12	71	theme	component	1469:1477	arg1	9:41:5:45					1590:1598	9:41:5:45	1590:1598	9:41:5:45	1590:1598	The relative content of these component could be classed as 2:8:0:90 (Type I, only one case designated as Kita), 5:24:3:68 (Type II, seven cases), and 9:41:5:45 (Type III, four cases).
1280920	12	71	theme	component	1469:1477	arg1	5:24:3:68					1552:1560	5:24:3:68	1552:1560	5:24:3:68	1552:1560	The relative content of these component could be classed as 2:8:0:90 (Type I, only one case designated as Kita), 5:24:3:68 (Type II, seven cases), and 9:41:5:45 (Type III, four cases).
1280920	12	71	theme	component	1469:1477	arg1	content					1452:1458	The relative content	1439:1458	The relative content of these component	1439:1477	The relative content of these component could be classed as 2:8:0:90 (Type I, only one case designated as Kita), 5:24:3:68 (Type II, seven cases), and 9:41:5:45 (Type III, four cases).
1280920	0	72	theme	gas-phase	74:82	arg1	hydrazinolysis					84:97	gas-phase hydrazinolysis	74:97	gas-phase hydrazinolysis	74:97	Analysis of glycoform of O-glycan from human myeloma immunoglobulin A1 by gas-phase hydrazinolysis following pyridylamination of oligosaccharides.
1280920	8	73	theme	bovine	1052:1057	arg1	fetuin					1059:1064	bovine fetuin	1052:1064	bovine fetuin whose relative content (P1:P2: P3:P:4) was 16:43:19:22	1052:1119	Four similar components were also detected in bovine fetuin whose relative content (P1:P2: P3:P:4) was 16:43:19:22.
1280920	5	74	theme	authentic	627:635	arg1	sugar					659:663	an authentic standard pyridylamino sugar	624:663	an authentic standard pyridylamino sugar	624:663	The neutral component (P4) among them was identified as Gal beta 1,3GalNAc-PA by cochromatography with an authentic standard pyridylamino sugar.
1280920	11	75	from	those	1408:1412	arg1	distinct					1394:1401	distinct	1394:1401	distinct	1394:1401	Analysis of IgA1 myeloma protein indicated glycoforms distinct from those of the healthy controls.
1280920	12	76	theme	relative	1443:1450	arg1	2:8:0:90					1499:1506	2:8:0:90	1499:1506	2:8:0:90	1499:1506	The relative content of these component could be classed as 2:8:0:90 (Type I, only one case designated as Kita), 5:24:3:68 (Type II, seven cases), and 9:41:5:45 (Type III, four cases).
1280920	12	76	theme	relative	1443:1450	arg1	9:41:5:45					1590:1598	9:41:5:45	1590:1598	9:41:5:45	1590:1598	The relative content of these component could be classed as 2:8:0:90 (Type I, only one case designated as Kita), 5:24:3:68 (Type II, seven cases), and 9:41:5:45 (Type III, four cases).
1280920	12	76	theme	relative	1443:1450	arg1	5:24:3:68					1552:1560	5:24:3:68	1552:1560	5:24:3:68	1552:1560	The relative content of these component could be classed as 2:8:0:90 (Type I, only one case designated as Kita), 5:24:3:68 (Type II, seven cases), and 9:41:5:45 (Type III, four cases).
1280920	12	76	theme	relative	1443:1450	arg1	content					1452:1458	The relative content	1439:1458	The relative content of these component	1439:1477	The relative content of these component could be classed as 2:8:0:90 (Type I, only one case designated as Kita), 5:24:3:68 (Type II, seven cases), and 9:41:5:45 (Type III, four cases).
1280920	3	77	theme	two-dimensional	386:400	arg1	method					413:418	a two-dimensional analytical method	384:418	a two-dimensional analytical method of gel filtration and reverse-phase HPLC	384:459	The released oligosaccharide was pyridylaminated and separated by a two-dimensional analytical method of gel filtration and reverse-phase HPLC.
1280920	6	78	theme	P2	749:750	arg1	components					752:761	middle size P2 components	737:761	middle size P2 components	737:761	The desialylation of the other components indicated the largest P1 and middle size P2 components possibly corresponded to a disialylated structure, NeuAc alpha 2,3Gal beta 1,3(NeuAc alpha 2,6)GalNAc-PA, and a monosialylated component, NeuAc alpha 2,3Gal beta 1,3GalNAc-PA, respectively.
1280920	13	79	gly	glycoforms	1696:1705	arg1	O-glycan					1710:1717	O-glycan	1710:1717	O-glycan	1710:1717	Thus, the results for IgA1 myeloma protein indicate that at least three glycoforms of O-glycan are possible for the IgA1 hinge structure.
1280920	5	80	theme	pyridylamino	646:657	arg1	sugar					659:663	an authentic standard pyridylamino sugar	624:663	an authentic standard pyridylamino sugar	624:663	The neutral component (P4) among them was identified as Gal beta 1,3GalNAc-PA by cochromatography with an authentic standard pyridylamino sugar.
1280920	14	81	theme	healthy	1807:1813	arg1	controls					1815:1822	the healthy controls	1803:1822	the healthy controls	1803:1822	However, only one glycoform was found in the healthy controls.
1280920	6	82	theme	middle	737:742	arg1	components					752:761	middle size P2 components	737:761	middle size P2 components	737:761	The desialylation of the other components indicated the largest P1 and middle size P2 components possibly corresponded to a disialylated structure, NeuAc alpha 2,3Gal beta 1,3(NeuAc alpha 2,6)GalNAc-PA, and a monosialylated component, NeuAc alpha 2,3Gal beta 1,3GalNAc-PA, respectively.
1280920	6	83	theme	components	697:706	arg1	desialylation					670:682	The desialylation	666:682	The desialylation of the other components indicated the largest P1 and middle size P2 components	666:761	The desialylation of the other components indicated the largest P1 and middle size P2 components possibly corresponded to a disialylated structure, NeuAc alpha 2,3Gal beta 1,3(NeuAc alpha 2,6)GalNAc-PA, and a monosialylated component, NeuAc alpha 2,3Gal beta 1,3GalNAc-PA, respectively.
1280920	3	84	theme	gel	423:425	arg1	filtration					427:436	gel filtration	423:436	gel filtration	423:436	The released oligosaccharide was pyridylaminated and separated by a two-dimensional analytical method of gel filtration and reverse-phase HPLC.
1280920	6	85	gly	monosialylated	875:888	arg1	1,3GalNAc-PA					925:936	NeuAc alpha 2,3Gal beta 1,3GalNAc-PA	901:936	NeuAc alpha 2,3Gal beta 1,3GalNAc-PA	901:936	The desialylation of the other components indicated the largest P1 and middle size P2 components possibly corresponded to a disialylated structure, NeuAc alpha 2,3Gal beta 1,3(NeuAc alpha 2,6)GalNAc-PA, and a monosialylated component, NeuAc alpha 2,3Gal beta 1,3GalNAc-PA, respectively.
1280920	6	85	gly	monosialylated	875:888	arg1	component					890:898	a monosialylated component	873:898	a monosialylated component	873:898	The desialylation of the other components indicated the largest P1 and middle size P2 components possibly corresponded to a disialylated structure, NeuAc alpha 2,3Gal beta 1,3(NeuAc alpha 2,6)GalNAc-PA, and a monosialylated component, NeuAc alpha 2,3Gal beta 1,3GalNAc-PA, respectively.
1280920	7	86	theme	P3	982:983	arg1	incomplete					994:1003	incomplete	994:1003	incomplete	994:1003	The structural assignment of P3 is still incomplete.
1280920	7	86	theme	P3	982:983	arg1	assignment					968:977	The structural assignment	953:977	The structural assignment of P3	953:983	The structural assignment of P3 is still incomplete.
1280920	13	87	theme	myeloma	1651:1657	arg1	protein					1659:1665	IgA1 myeloma protein	1646:1665	IgA1 myeloma protein	1646:1665	Thus, the results for IgA1 myeloma protein indicate that at least three glycoforms of O-glycan are possible for the IgA1 hinge structure.
1280920	6	88	theme	monosialylated	875:888	arg1	1,3GalNAc-PA					925:936	NeuAc alpha 2,3Gal beta 1,3GalNAc-PA	901:936	NeuAc alpha 2,3Gal beta 1,3GalNAc-PA	901:936	The desialylation of the other components indicated the largest P1 and middle size P2 components possibly corresponded to a disialylated structure, NeuAc alpha 2,3Gal beta 1,3(NeuAc alpha 2,6)GalNAc-PA, and a monosialylated component, NeuAc alpha 2,3Gal beta 1,3GalNAc-PA, respectively.
1280920	6	88	theme	monosialylated	875:888	arg1	component					890:898	a monosialylated component	873:898	a monosialylated component	873:898	The desialylation of the other components indicated the largest P1 and middle size P2 components possibly corresponded to a disialylated structure, NeuAc alpha 2,3Gal beta 1,3(NeuAc alpha 2,6)GalNAc-PA, and a monosialylated component, NeuAc alpha 2,3Gal beta 1,3GalNAc-PA, respectively.
1280920	3	89	theme	HPLC	456:459	arg1	method					413:418	a two-dimensional analytical method	384:418	a two-dimensional analytical method of gel filtration and reverse-phase HPLC	384:459	The released oligosaccharide was pyridylaminated and separated by a two-dimensional analytical method of gel filtration and reverse-phase HPLC.
1280920	0	90	theme	myeloma	45:51	arg1	A1					68:69	human myeloma immunoglobulin A1	39:69	human myeloma immunoglobulin A1	39:69	Analysis of glycoform of O-glycan from human myeloma immunoglobulin A1 by gas-phase hydrazinolysis following pyridylamination of oligosaccharides.
1280920	0	91	gly	glycoform	12:20	arg1	O-glycan					25:32	O-glycan	25:32	O-glycan from human myeloma immunoglobulin A1	25:69	Analysis of glycoform of O-glycan from human myeloma immunoglobulin A1 by gas-phase hydrazinolysis following pyridylamination of oligosaccharides.
1280920	6	92	theme	disialylated	790:801	arg1	structure					803:811	a disialylated structure	788:811	a disialylated structure	788:811	The desialylation of the other components indicated the largest P1 and middle size P2 components possibly corresponded to a disialylated structure, NeuAc alpha 2,3Gal beta 1,3(NeuAc alpha 2,6)GalNAc-PA, and a monosialylated component, NeuAc alpha 2,3Gal beta 1,3GalNAc-PA, respectively.
1280920	14	93	located	found	1794:1798	arg2	glycoform					1780:1788	only one glycoform	1771:1788	only one glycoform	1771:1788	However, only one glycoform was found in the healthy controls.
1280920	14	93	located	found	1794:1798	arg1	controls					1815:1822	the healthy controls	1803:1822	the healthy controls	1803:1822	However, only one glycoform was found in the healthy controls.
8122360	7	0	theme	intracellular	1524:1536	arg1	domains					1550:1556	their intracellular phosphatase domains	1518:1556	their intracellular phosphatase domains	1518:1556	Since CD45 glycoproteins are thought to play an important regulatory role in cell-to-cell interactions owing to their variable extracellular region and because they may regulate membrane signaling through their intracellular phosphatase domains, we suggest that these altered CD45 molecules may present an abnormal signal for natural ligands such as the B-cell-specific surface receptor CD22, thus perturbing the normal immune response in HIV-1-infected individuals.
8122360	6	1	theme	PNA	1094:1096	arg1	lectin					1098:1103	PNA lectin	1094:1103	PNA lectin which recognizes nonsialylated terminal Gal beta 1-->3GalNAc	1094:1164	Concerning the latter, PNA lectin which recognizes nonsialylated terminal Gal beta 1-->3GalNAc might precipitate up to 75% of the total tyrosine phosphatase activity displayed by CD45 molecules from one latently HIV-1-infected CEM cell line.
8122360	3	2	theme	altered	686:692	arg1	patterns					708:715	altered glycosylation patterns	686:715	altered glycosylation patterns	686:715	In the present study, we show that HIV-1-infected lymphocytes of the CEM cell line (either latent or virus-producing) and HIV-1-infected CD4+ lymphocytes have several membrane proteins with altered glycosylation patterns.
8122360	6	3	theme	CEM	1298:1300	arg1	line					1307:1310	one latently HIV-1-infected CEM cell line	1270:1310	one latently HIV-1-infected CEM cell line	1270:1310	Concerning the latter, PNA lectin which recognizes nonsialylated terminal Gal beta 1-->3GalNAc might precipitate up to 75% of the total tyrosine phosphatase activity displayed by CD45 molecules from one latently HIV-1-infected CEM cell line.
8122360	2	4	from	description	203:213	arg1	functions					279:287	T cell functions	272:287	T cell functions	272:287	Despite description of the virus cytopathicity and numerous modifications in T cell functions, such as perturbation of antigen receptor signaling, CD4 downregulation, and induction of apoptosis, the precise mechanisms underlying the disruption of normal immune responses have not yet been elucidated.
8122360	4	5	theme	terminal	902:909	arg1	Gal					911:913	a terminal Gal	900:913	a terminal Gal beta 1-->4GlcNAc	900:930	Using lectins with specificity for different carbohydrate moieties, we could demonstrate the presence of two exposed nonsialylated disaccharides: a terminal Gal beta 1-->3GalNAc and a terminal Gal beta 1-->4GlcNAc.
8122360	2	6	theme	cytopathicity	228:240	arg1	description					203:213	description	203:213	description of the virus cytopathicity	203:240	Despite description of the virus cytopathicity and numerous modifications in T cell functions, such as perturbation of antigen receptor signaling, CD4 downregulation, and induction of apoptosis, the precise mechanisms underlying the disruption of normal immune responses have not yet been elucidated.
8122360	2	6	theme	cytopathicity	228:240	arg1	perturbation					298:309	perturbation	298:309	perturbation of antigen receptor signaling	298:339	Despite description of the virus cytopathicity and numerous modifications in T cell functions, such as perturbation of antigen receptor signaling, CD4 downregulation, and induction of apoptosis, the precise mechanisms underlying the disruption of normal immune responses have not yet been elucidated.
8122360	2	6	theme	cytopathicity	228:240	arg1	modifications					255:267	numerous modifications	246:267	numerous modifications in T cell functions, such as perturbation of antigen receptor signaling, CD4 downregulation, and induction of apoptosis	246:387	Despite description of the virus cytopathicity and numerous modifications in T cell functions, such as perturbation of antigen receptor signaling, CD4 downregulation, and induction of apoptosis, the precise mechanisms underlying the disruption of normal immune responses have not yet been elucidated.
8122360	7	7	theme	membrane	1491:1498	arg1	signaling					1500:1508	membrane signaling	1491:1508	membrane signaling	1491:1508	Since CD45 glycoproteins are thought to play an important regulatory role in cell-to-cell interactions owing to their variable extracellular region and because they may regulate membrane signaling through their intracellular phosphatase domains, we suggest that these altered CD45 molecules may present an abnormal signal for natural ligands such as the B-cell-specific surface receptor CD22, thus perturbing the normal immune response in HIV-1-infected individuals.
8122360	4	8	theme	terminal	866:873	arg1	Gal					875:877	a terminal Gal	864:877	a terminal Gal beta 1-->3GalNAc	864:894	Using lectins with specificity for different carbohydrate moieties, we could demonstrate the presence of two exposed nonsialylated disaccharides: a terminal Gal beta 1-->3GalNAc and a terminal Gal beta 1-->4GlcNAc.
8122360	7	9	theme	extracellular	1440:1452	arg1	region					1454:1459	their variable extracellular region	1425:1459	their variable extracellular region	1425:1459	Since CD45 glycoproteins are thought to play an important regulatory role in cell-to-cell interactions owing to their variable extracellular region and because they may regulate membrane signaling through their intracellular phosphatase domains, we suggest that these altered CD45 molecules may present an abnormal signal for natural ligands such as the B-cell-specific surface receptor CD22, thus perturbing the normal immune response in HIV-1-infected individuals.
8122360	0	10	theme	Altered	0:6	arg1	sialylation					8:18	Altered sialylation	0:18	Altered sialylation of CD45 in HIV-1-infected T lymphocytes	0:58	Altered sialylation of CD45 in HIV-1-infected T lymphocytes.
8122360	3	11	with	proteins	672:679	arg1	patterns					708:715	altered glycosylation patterns	686:715	altered glycosylation patterns	686:715	In the present study, we show that HIV-1-infected lymphocytes of the CEM cell line (either latent or virus-producing) and HIV-1-infected CD4+ lymphocytes have several membrane proteins with altered glycosylation patterns.
8122360	4	12	theme	beta	879:882	arg1	disaccharides					849:861	two exposed nonsialylated disaccharides	823:861	two exposed nonsialylated disaccharides: a terminal Gal beta 1-->3GalNAc and a terminal Gal beta 1-->4GlcNAc	823:930	Using lectins with specificity for different carbohydrate moieties, we could demonstrate the presence of two exposed nonsialylated disaccharides: a terminal Gal beta 1-->3GalNAc and a terminal Gal beta 1-->4GlcNAc.
8122360	4	12	theme	beta	879:882	arg1	1-->3GalNAc					884:894	a terminal Gal beta 1-->3GalNAc	864:894	a terminal Gal beta 1-->3GalNAc	864:894	Using lectins with specificity for different carbohydrate moieties, we could demonstrate the presence of two exposed nonsialylated disaccharides: a terminal Gal beta 1-->3GalNAc and a terminal Gal beta 1-->4GlcNAc.
8122360	4	13	with	lectins	724:730	arg1	specificity					737:747	specificity	737:747	specificity for different carbohydrate moieties	737:783	Using lectins with specificity for different carbohydrate moieties, we could demonstrate the presence of two exposed nonsialylated disaccharides: a terminal Gal beta 1-->3GalNAc and a terminal Gal beta 1-->4GlcNAc.
8122360	6	14	theme	CD45	1250:1253	arg1	molecules					1255:1263	CD45 molecules	1250:1263	CD45 molecules from one latently HIV-1-infected CEM cell line	1250:1310	Concerning the latter, PNA lectin which recognizes nonsialylated terminal Gal beta 1-->3GalNAc might precipitate up to 75% of the total tyrosine phosphatase activity displayed by CD45 molecules from one latently HIV-1-infected CEM cell line.
8122360	2	15	theme	antigen	314:320	arg1	signaling					331:339	antigen receptor signaling	314:339	antigen receptor signaling	314:339	Despite description of the virus cytopathicity and numerous modifications in T cell functions, such as perturbation of antigen receptor signaling, CD4 downregulation, and induction of apoptosis, the precise mechanisms underlying the disruption of normal immune responses have not yet been elucidated.
8122360	7	16	theme	receptor	1691:1698	arg1	CD22					1700:1703	the B-cell-specific surface receptor CD22	1663:1703	the B-cell-specific surface receptor CD22	1663:1703	Since CD45 glycoproteins are thought to play an important regulatory role in cell-to-cell interactions owing to their variable extracellular region and because they may regulate membrane signaling through their intracellular phosphatase domains, we suggest that these altered CD45 molecules may present an abnormal signal for natural ligands such as the B-cell-specific surface receptor CD22, thus perturbing the normal immune response in HIV-1-infected individuals.
8122360	4	17	dep	disaccharides	849:861	arg1	1-->4GlcNAc					920:930	a terminal Gal beta 1-->4GlcNAc	900:930	a terminal Gal beta 1-->4GlcNAc	900:930	Using lectins with specificity for different carbohydrate moieties, we could demonstrate the presence of two exposed nonsialylated disaccharides: a terminal Gal beta 1-->3GalNAc and a terminal Gal beta 1-->4GlcNAc.
8122360	4	17	dep	disaccharides	849:861	arg1	disaccharides					849:861	two exposed nonsialylated disaccharides	823:861	two exposed nonsialylated disaccharides: a terminal Gal beta 1-->3GalNAc and a terminal Gal beta 1-->4GlcNAc	823:930	Using lectins with specificity for different carbohydrate moieties, we could demonstrate the presence of two exposed nonsialylated disaccharides: a terminal Gal beta 1-->3GalNAc and a terminal Gal beta 1-->4GlcNAc.
8122360	4	17	dep	disaccharides	849:861	arg1	1-->3GalNAc					884:894	a terminal Gal beta 1-->3GalNAc	864:894	a terminal Gal beta 1-->3GalNAc	864:894	Using lectins with specificity for different carbohydrate moieties, we could demonstrate the presence of two exposed nonsialylated disaccharides: a terminal Gal beta 1-->3GalNAc and a terminal Gal beta 1-->4GlcNAc.
8122360	7	18	theme	B-cell-specific	1667:1681	arg1	CD22					1700:1703	the B-cell-specific surface receptor CD22	1663:1703	the B-cell-specific surface receptor CD22	1663:1703	Since CD45 glycoproteins are thought to play an important regulatory role in cell-to-cell interactions owing to their variable extracellular region and because they may regulate membrane signaling through their intracellular phosphatase domains, we suggest that these altered CD45 molecules may present an abnormal signal for natural ligands such as the B-cell-specific surface receptor CD22, thus perturbing the normal immune response in HIV-1-infected individuals.
8122360	7	19	theme	cell-to-cell	1390:1401	arg1	interactions					1403:1414	cell-to-cell interactions	1390:1414	cell-to-cell interactions owing to their variable extracellular region	1390:1459	Since CD45 glycoproteins are thought to play an important regulatory role in cell-to-cell interactions owing to their variable extracellular region and because they may regulate membrane signaling through their intracellular phosphatase domains, we suggest that these altered CD45 molecules may present an abnormal signal for natural ligands such as the B-cell-specific surface receptor CD22, thus perturbing the normal immune response in HIV-1-infected individuals.
8122360	3	20	contain	have	650:653	arg1	lymphocytes					546:556	HIV-1-infected lymphocytes	531:556	HIV-1-infected lymphocytes of the CEM cell line (either latent or virus-producing) and HIV-1-infected CD4+ lymphocytes	531:648	In the present study, we show that HIV-1-infected lymphocytes of the CEM cell line (either latent or virus-producing) and HIV-1-infected CD4+ lymphocytes have several membrane proteins with altered glycosylation patterns.
8122360	3	20	contain	have	650:653	arg2	proteins					672:679	several membrane proteins	655:679	several membrane proteins with altered glycosylation patterns	655:715	In the present study, we show that HIV-1-infected lymphocytes of the CEM cell line (either latent or virus-producing) and HIV-1-infected CD4+ lymphocytes have several membrane proteins with altered glycosylation patterns.
8122360	4	21	theme	beta	915:918	arg1	1-->4GlcNAc					920:930	a terminal Gal beta 1-->4GlcNAc	900:930	a terminal Gal beta 1-->4GlcNAc	900:930	Using lectins with specificity for different carbohydrate moieties, we could demonstrate the presence of two exposed nonsialylated disaccharides: a terminal Gal beta 1-->3GalNAc and a terminal Gal beta 1-->4GlcNAc.
8122360	4	21	theme	beta	915:918	arg1	disaccharides					849:861	two exposed nonsialylated disaccharides	823:861	two exposed nonsialylated disaccharides: a terminal Gal beta 1-->3GalNAc and a terminal Gal beta 1-->4GlcNAc	823:930	Using lectins with specificity for different carbohydrate moieties, we could demonstrate the presence of two exposed nonsialylated disaccharides: a terminal Gal beta 1-->3GalNAc and a terminal Gal beta 1-->4GlcNAc.
8122360	6	22	theme	activity	1228:1235	arg1	activity					1228:1235	the total tyrosine phosphatase activity	1197:1235	the total tyrosine phosphatase activity displayed by CD45 molecules from one latently HIV-1-infected CEM cell line	1197:1310	Concerning the latter, PNA lectin which recognizes nonsialylated terminal Gal beta 1-->3GalNAc might precipitate up to 75% of the total tyrosine phosphatase activity displayed by CD45 molecules from one latently HIV-1-infected CEM cell line.
8122360	6	22	theme	activity	1228:1235	arg1	%					1192:1192	up to 75%	1184:1192	up to 75% of the total tyrosine phosphatase activity displayed by CD45 molecules from one latently HIV-1-infected CEM cell line	1184:1310	Concerning the latter, PNA lectin which recognizes nonsialylated terminal Gal beta 1-->3GalNAc might precipitate up to 75% of the total tyrosine phosphatase activity displayed by CD45 molecules from one latently HIV-1-infected CEM cell line.
8122360	2	23	theme	virus	222:226	arg1	cytopathicity					228:240	the virus cytopathicity	218:240	the virus cytopathicity	218:240	Despite description of the virus cytopathicity and numerous modifications in T cell functions, such as perturbation of antigen receptor signaling, CD4 downregulation, and induction of apoptosis, the precise mechanisms underlying the disruption of normal immune responses have not yet been elucidated.
8122360	1	24	theme	profound	124:131	arg1	dysregulation					133:145	profound dysregulation	124:145	profound dysregulation of normal T lymphocyte properties by the virus	124:192	Immunodeficiency caused by HIV infection probably results from profound dysregulation of normal T lymphocyte properties by the virus.
8122360	7	25	theme	important	1361:1369	arg1	role					1382:1385	an important regulatory role	1358:1385	an important regulatory role	1358:1385	Since CD45 glycoproteins are thought to play an important regulatory role in cell-to-cell interactions owing to their variable extracellular region and because they may regulate membrane signaling through their intracellular phosphatase domains, we suggest that these altered CD45 molecules may present an abnormal signal for natural ligands such as the B-cell-specific surface receptor CD22, thus perturbing the normal immune response in HIV-1-infected individuals.
8122360	6	26	theme	tyrosine	1207:1214	arg1	activity					1228:1235	the total tyrosine phosphatase activity	1197:1235	the total tyrosine phosphatase activity displayed by CD45 molecules from one latently HIV-1-infected CEM cell line	1197:1310	Concerning the latter, PNA lectin which recognizes nonsialylated terminal Gal beta 1-->3GalNAc might precipitate up to 75% of the total tyrosine phosphatase activity displayed by CD45 molecules from one latently HIV-1-infected CEM cell line.
8122360	5	27	theme	carbohydrate	1048:1059	arg1	moieties					1061:1068	O-linked carbohydrate moieties	1039:1068	O-linked carbohydrate moieties	1039:1068	In particular, CD45, one of the major T cell glycoproteins, appeared to be partially sialylated on N- and O-linked carbohydrate moieties.
8122360	2	28	theme	T	272:272	arg1	functions					279:287	T cell functions	272:287	T cell functions	272:287	Despite description of the virus cytopathicity and numerous modifications in T cell functions, such as perturbation of antigen receptor signaling, CD4 downregulation, and induction of apoptosis, the precise mechanisms underlying the disruption of normal immune responses have not yet been elucidated.
8122360	1	29	theme	T	157:157	arg1	properties					170:179	normal T lymphocyte properties	150:179	normal T lymphocyte properties	150:179	Immunodeficiency caused by HIV infection probably results from profound dysregulation of normal T lymphocyte properties by the virus.
8122360	7	30	theme	abnormal	1619:1626	arg1	signal					1628:1633	an abnormal signal	1616:1633	an abnormal signal for natural ligands such as the B-cell-specific surface receptor CD22	1616:1703	Since CD45 glycoproteins are thought to play an important regulatory role in cell-to-cell interactions owing to their variable extracellular region and because they may regulate membrane signaling through their intracellular phosphatase domains, we suggest that these altered CD45 molecules may present an abnormal signal for natural ligands such as the B-cell-specific surface receptor CD22, thus perturbing the normal immune response in HIV-1-infected individuals.
8122360	5	31	gly	glycoproteins	978:990	arg1	glycoproteins					978:990	the major T cell glycoproteins	961:990	the major T cell glycoproteins	961:990	In particular, CD45, one of the major T cell glycoproteins, appeared to be partially sialylated on N- and O-linked carbohydrate moieties.
8122360	1	32	theme	properties	170:179	arg1	dysregulation					133:145	profound dysregulation	124:145	profound dysregulation of normal T lymphocyte properties by the virus	124:192	Immunodeficiency caused by HIV infection probably results from profound dysregulation of normal T lymphocyte properties by the virus.
8122360	7	33	theme	regulatory	1371:1380	arg1	role					1382:1385	an important regulatory role	1358:1385	an important regulatory role	1358:1385	Since CD45 glycoproteins are thought to play an important regulatory role in cell-to-cell interactions owing to their variable extracellular region and because they may regulate membrane signaling through their intracellular phosphatase domains, we suggest that these altered CD45 molecules may present an abnormal signal for natural ligands such as the B-cell-specific surface receptor CD22, thus perturbing the normal immune response in HIV-1-infected individuals.
8122360	5	34	theme	T	971:971	arg1	glycoproteins					978:990	the major T cell glycoproteins	961:990	the major T cell glycoproteins	961:990	In particular, CD45, one of the major T cell glycoproteins, appeared to be partially sialylated on N- and O-linked carbohydrate moieties.
8122360	7	35	theme	immune	1733:1738	arg1	response					1740:1747	the normal immune response	1722:1747	the normal immune response in HIV-1-infected individuals	1722:1777	Since CD45 glycoproteins are thought to play an important regulatory role in cell-to-cell interactions owing to their variable extracellular region and because they may regulate membrane signaling through their intracellular phosphatase domains, we suggest that these altered CD45 molecules may present an abnormal signal for natural ligands such as the B-cell-specific surface receptor CD22, thus perturbing the normal immune response in HIV-1-infected individuals.
8122360	2	36	theme	precise	394:400	arg1	mechanisms					402:411	the precise mechanisms	390:411	the precise mechanisms underlying the disruption of normal immune responses	390:464	Despite description of the virus cytopathicity and numerous modifications in T cell functions, such as perturbation of antigen receptor signaling, CD4 downregulation, and induction of apoptosis, the precise mechanisms underlying the disruption of normal immune responses have not yet been elucidated.
8122360	5	37	theme	glycoproteins	978:990	arg1	CD45					948:951	CD45	948:951	CD45	948:951	In particular, CD45, one of the major T cell glycoproteins, appeared to be partially sialylated on N- and O-linked carbohydrate moieties.
8122360	5	37	theme	glycoproteins	978:990	arg1	one					954:956	one	954:956	one	954:956	In particular, CD45, one of the major T cell glycoproteins, appeared to be partially sialylated on N- and O-linked carbohydrate moieties.
8122360	5	37	theme	glycoproteins	978:990	arg1	glycoproteins					978:990	the major T cell glycoproteins	961:990	the major T cell glycoproteins	961:990	In particular, CD45, one of the major T cell glycoproteins, appeared to be partially sialylated on N- and O-linked carbohydrate moieties.
8122360	2	38	theme	responses	456:464	arg1	disruption					428:437	the disruption	424:437	the disruption of normal immune responses	424:464	Despite description of the virus cytopathicity and numerous modifications in T cell functions, such as perturbation of antigen receptor signaling, CD4 downregulation, and induction of apoptosis, the precise mechanisms underlying the disruption of normal immune responses have not yet been elucidated.
8122360	4	39	theme	different	753:761	arg1	moieties					776:783	different carbohydrate moieties	753:783	different carbohydrate moieties	753:783	Using lectins with specificity for different carbohydrate moieties, we could demonstrate the presence of two exposed nonsialylated disaccharides: a terminal Gal beta 1-->3GalNAc and a terminal Gal beta 1-->4GlcNAc.
8122360	4	40	gly	nonsialylated	835:847	arg1	1-->4GlcNAc					920:930	a terminal Gal beta 1-->4GlcNAc	900:930	a terminal Gal beta 1-->4GlcNAc	900:930	Using lectins with specificity for different carbohydrate moieties, we could demonstrate the presence of two exposed nonsialylated disaccharides: a terminal Gal beta 1-->3GalNAc and a terminal Gal beta 1-->4GlcNAc.
8122360	4	40	gly	nonsialylated	835:847	arg1	disaccharides					849:861	two exposed nonsialylated disaccharides	823:861	two exposed nonsialylated disaccharides: a terminal Gal beta 1-->3GalNAc and a terminal Gal beta 1-->4GlcNAc	823:930	Using lectins with specificity for different carbohydrate moieties, we could demonstrate the presence of two exposed nonsialylated disaccharides: a terminal Gal beta 1-->3GalNAc and a terminal Gal beta 1-->4GlcNAc.
8122360	4	40	gly	nonsialylated	835:847	arg1	1-->3GalNAc					884:894	a terminal Gal beta 1-->3GalNAc	864:894	a terminal Gal beta 1-->3GalNAc	864:894	Using lectins with specificity for different carbohydrate moieties, we could demonstrate the presence of two exposed nonsialylated disaccharides: a terminal Gal beta 1-->3GalNAc and a terminal Gal beta 1-->4GlcNAc.
8122360	7	41	gly	glycoproteins	1324:1336	arg1	glycoproteins					1324:1336	CD45 glycoproteins	1319:1336	CD45 glycoproteins	1319:1336	Since CD45 glycoproteins are thought to play an important regulatory role in cell-to-cell interactions owing to their variable extracellular region and because they may regulate membrane signaling through their intracellular phosphatase domains, we suggest that these altered CD45 molecules may present an abnormal signal for natural ligands such as the B-cell-specific surface receptor CD22, thus perturbing the normal immune response in HIV-1-infected individuals.
8122360	2	42	theme	normal	442:447	arg1	responses					456:464	normal immune responses	442:464	normal immune responses	442:464	Despite description of the virus cytopathicity and numerous modifications in T cell functions, such as perturbation of antigen receptor signaling, CD4 downregulation, and induction of apoptosis, the precise mechanisms underlying the disruption of normal immune responses have not yet been elucidated.
8122360	7	43	theme	CD45	1319:1322	arg1	glycoproteins					1324:1336	CD45 glycoproteins	1319:1336	CD45 glycoproteins	1319:1336	Since CD45 glycoproteins are thought to play an important regulatory role in cell-to-cell interactions owing to their variable extracellular region and because they may regulate membrane signaling through their intracellular phosphatase domains, we suggest that these altered CD45 molecules may present an abnormal signal for natural ligands such as the B-cell-specific surface receptor CD22, thus perturbing the normal immune response in HIV-1-infected individuals.
8122360	4	44	theme	nonsialylated	835:847	arg1	1-->4GlcNAc					920:930	a terminal Gal beta 1-->4GlcNAc	900:930	a terminal Gal beta 1-->4GlcNAc	900:930	Using lectins with specificity for different carbohydrate moieties, we could demonstrate the presence of two exposed nonsialylated disaccharides: a terminal Gal beta 1-->3GalNAc and a terminal Gal beta 1-->4GlcNAc.
8122360	4	44	theme	nonsialylated	835:847	arg1	disaccharides					849:861	two exposed nonsialylated disaccharides	823:861	two exposed nonsialylated disaccharides: a terminal Gal beta 1-->3GalNAc and a terminal Gal beta 1-->4GlcNAc	823:930	Using lectins with specificity for different carbohydrate moieties, we could demonstrate the presence of two exposed nonsialylated disaccharides: a terminal Gal beta 1-->3GalNAc and a terminal Gal beta 1-->4GlcNAc.
8122360	4	44	theme	nonsialylated	835:847	arg1	1-->3GalNAc					884:894	a terminal Gal beta 1-->3GalNAc	864:894	a terminal Gal beta 1-->3GalNAc	864:894	Using lectins with specificity for different carbohydrate moieties, we could demonstrate the presence of two exposed nonsialylated disaccharides: a terminal Gal beta 1-->3GalNAc and a terminal Gal beta 1-->4GlcNAc.
8122360	0	45	gly	sialylation	8:18	arg1	CD45					23:26	CD45	23:26	CD45	23:26	Altered sialylation of CD45 in HIV-1-infected T lymphocytes.
8122360	0	45	gly	sialylation	8:18	arg1	lymphocytes					48:58	HIV-1-infected T lymphocytes	31:58	HIV-1-infected T lymphocytes	31:58	Altered sialylation of CD45 in HIV-1-infected T lymphocytes.
8122360	3	46	theme	CD4+	633:636	arg1	lymphocytes					638:648	HIV-1-infected CD4+ lymphocytes	618:648	HIV-1-infected CD4+ lymphocytes	618:648	In the present study, we show that HIV-1-infected lymphocytes of the CEM cell line (either latent or virus-producing) and HIV-1-infected CD4+ lymphocytes have several membrane proteins with altered glycosylation patterns.
8122360	0	47	theme	T	46:46	arg1	lymphocytes					48:58	HIV-1-infected T lymphocytes	31:58	HIV-1-infected T lymphocytes	31:58	Altered sialylation of CD45 in HIV-1-infected T lymphocytes.
8122360	6	48	theme	terminal	1136:1143	arg1	1-->3GalNAc					1154:1164	nonsialylated terminal Gal beta 1-->3GalNAc	1122:1164	nonsialylated terminal Gal beta 1-->3GalNAc	1122:1164	Concerning the latter, PNA lectin which recognizes nonsialylated terminal Gal beta 1-->3GalNAc might precipitate up to 75% of the total tyrosine phosphatase activity displayed by CD45 molecules from one latently HIV-1-infected CEM cell line.
8122360	7	49	theme	phosphatase	1538:1548	arg1	domains					1550:1556	their intracellular phosphatase domains	1518:1556	their intracellular phosphatase domains	1518:1556	Since CD45 glycoproteins are thought to play an important regulatory role in cell-to-cell interactions owing to their variable extracellular region and because they may regulate membrane signaling through their intracellular phosphatase domains, we suggest that these altered CD45 molecules may present an abnormal signal for natural ligands such as the B-cell-specific surface receptor CD22, thus perturbing the normal immune response in HIV-1-infected individuals.
8122360	3	50	theme	membrane	663:670	arg1	proteins					672:679	several membrane proteins	655:679	several membrane proteins with altered glycosylation patterns	655:715	In the present study, we show that HIV-1-infected lymphocytes of the CEM cell line (either latent or virus-producing) and HIV-1-infected CD4+ lymphocytes have several membrane proteins with altered glycosylation patterns.
8122360	6	51	theme	cell	1302:1305	arg1	line					1307:1310	one latently HIV-1-infected CEM cell line	1270:1310	one latently HIV-1-infected CEM cell line	1270:1310	Concerning the latter, PNA lectin which recognizes nonsialylated terminal Gal beta 1-->3GalNAc might precipitate up to 75% of the total tyrosine phosphatase activity displayed by CD45 molecules from one latently HIV-1-infected CEM cell line.
8122360	3	52	theme	present	503:509	arg1	study					511:515	the present study	499:515	the present study	499:515	In the present study, we show that HIV-1-infected lymphocytes of the CEM cell line (either latent or virus-producing) and HIV-1-infected CD4+ lymphocytes have several membrane proteins with altered glycosylation patterns.
8122360	3	53	theme	glycosylation	694:706	arg1	patterns					708:715	altered glycosylation patterns	686:715	altered glycosylation patterns	686:715	In the present study, we show that HIV-1-infected lymphocytes of the CEM cell line (either latent or virus-producing) and HIV-1-infected CD4+ lymphocytes have several membrane proteins with altered glycosylation patterns.
8122360	6	54	theme	HIV-1-infected	1283:1296	arg1	line					1307:1310	one latently HIV-1-infected CEM cell line	1270:1310	one latently HIV-1-infected CEM cell line	1270:1310	Concerning the latter, PNA lectin which recognizes nonsialylated terminal Gal beta 1-->3GalNAc might precipitate up to 75% of the total tyrosine phosphatase activity displayed by CD45 molecules from one latently HIV-1-infected CEM cell line.
8122360	3	55	theme	HIV-1-infected	531:544	arg1	lymphocytes					546:556	HIV-1-infected lymphocytes	531:556	HIV-1-infected lymphocytes of the CEM cell line (either latent or virus-producing) and HIV-1-infected CD4+ lymphocytes	531:648	In the present study, we show that HIV-1-infected lymphocytes of the CEM cell line (either latent or virus-producing) and HIV-1-infected CD4+ lymphocytes have several membrane proteins with altered glycosylation patterns.
8122360	3	56	theme	CEM	565:567	arg1	line					574:577	the CEM cell line	561:577	the CEM cell line (either latent or virus-producing)	561:612	In the present study, we show that HIV-1-infected lymphocytes of the CEM cell line (either latent or virus-producing) and HIV-1-infected CD4+ lymphocytes have several membrane proteins with altered glycosylation patterns.
8122360	3	57	dep	line	574:577	arg1	virus-producing					597:611	virus-producing	597:611	virus-producing	597:611	In the present study, we show that HIV-1-infected lymphocytes of the CEM cell line (either latent or virus-producing) and HIV-1-infected CD4+ lymphocytes have several membrane proteins with altered glycosylation patterns.
8122360	3	57	dep	line	574:577	arg1	latent					587:592	latent	587:592	latent	587:592	In the present study, we show that HIV-1-infected lymphocytes of the CEM cell line (either latent or virus-producing) and HIV-1-infected CD4+ lymphocytes have several membrane proteins with altered glycosylation patterns.
8122360	2	58	theme	receptor	322:329	arg1	signaling					331:339	antigen receptor signaling	314:339	antigen receptor signaling	314:339	Despite description of the virus cytopathicity and numerous modifications in T cell functions, such as perturbation of antigen receptor signaling, CD4 downregulation, and induction of apoptosis, the precise mechanisms underlying the disruption of normal immune responses have not yet been elucidated.
8122360	7	59	theme	surface	1683:1689	arg1	CD22					1700:1703	the B-cell-specific surface receptor CD22	1663:1703	the B-cell-specific surface receptor CD22	1663:1703	Since CD45 glycoproteins are thought to play an important regulatory role in cell-to-cell interactions owing to their variable extracellular region and because they may regulate membrane signaling through their intracellular phosphatase domains, we suggest that these altered CD45 molecules may present an abnormal signal for natural ligands such as the B-cell-specific surface receptor CD22, thus perturbing the normal immune response in HIV-1-infected individuals.
8122360	4	60	theme	Gal	875:877	arg1	disaccharides					849:861	two exposed nonsialylated disaccharides	823:861	two exposed nonsialylated disaccharides: a terminal Gal beta 1-->3GalNAc and a terminal Gal beta 1-->4GlcNAc	823:930	Using lectins with specificity for different carbohydrate moieties, we could demonstrate the presence of two exposed nonsialylated disaccharides: a terminal Gal beta 1-->3GalNAc and a terminal Gal beta 1-->4GlcNAc.
8122360	4	60	theme	Gal	875:877	arg1	1-->3GalNAc					884:894	a terminal Gal beta 1-->3GalNAc	864:894	a terminal Gal beta 1-->3GalNAc	864:894	Using lectins with specificity for different carbohydrate moieties, we could demonstrate the presence of two exposed nonsialylated disaccharides: a terminal Gal beta 1-->3GalNAc and a terminal Gal beta 1-->4GlcNAc.
8122360	7	61	theme	variable	1431:1438	arg1	region					1454:1459	their variable extracellular region	1425:1459	their variable extracellular region	1425:1459	Since CD45 glycoproteins are thought to play an important regulatory role in cell-to-cell interactions owing to their variable extracellular region and because they may regulate membrane signaling through their intracellular phosphatase domains, we suggest that these altered CD45 molecules may present an abnormal signal for natural ligands such as the B-cell-specific surface receptor CD22, thus perturbing the normal immune response in HIV-1-infected individuals.
8122360	3	62	theme	cell	569:572	arg1	line					574:577	the CEM cell line	561:577	the CEM cell line (either latent or virus-producing)	561:612	In the present study, we show that HIV-1-infected lymphocytes of the CEM cell line (either latent or virus-producing) and HIV-1-infected CD4+ lymphocytes have several membrane proteins with altered glycosylation patterns.
8122360	6	63	theme	beta	1149:1152	arg1	1-->3GalNAc					1154:1164	nonsialylated terminal Gal beta 1-->3GalNAc	1122:1164	nonsialylated terminal Gal beta 1-->3GalNAc	1122:1164	Concerning the latter, PNA lectin which recognizes nonsialylated terminal Gal beta 1-->3GalNAc might precipitate up to 75% of the total tyrosine phosphatase activity displayed by CD45 molecules from one latently HIV-1-infected CEM cell line.
8122360	2	64	theme	numerous	246:253	arg1	perturbation					298:309	perturbation	298:309	perturbation of antigen receptor signaling	298:339	Despite description of the virus cytopathicity and numerous modifications in T cell functions, such as perturbation of antigen receptor signaling, CD4 downregulation, and induction of apoptosis, the precise mechanisms underlying the disruption of normal immune responses have not yet been elucidated.
8122360	2	64	theme	numerous	246:253	arg1	modifications					255:267	numerous modifications	246:267	numerous modifications in T cell functions, such as perturbation of antigen receptor signaling, CD4 downregulation, and induction of apoptosis	246:387	Despite description of the virus cytopathicity and numerous modifications in T cell functions, such as perturbation of antigen receptor signaling, CD4 downregulation, and induction of apoptosis, the precise mechanisms underlying the disruption of normal immune responses have not yet been elucidated.
8122360	6	65	dep	75	1190:1191	arg1	to					1187:1188	to	1187:1188	to	1187:1188	Concerning the latter, PNA lectin which recognizes nonsialylated terminal Gal beta 1-->3GalNAc might precipitate up to 75% of the total tyrosine phosphatase activity displayed by CD45 molecules from one latently HIV-1-infected CEM cell line.
8122360	3	66	theme	line	574:577	arg1	lymphocytes					546:556	HIV-1-infected lymphocytes	531:556	HIV-1-infected lymphocytes of the CEM cell line (either latent or virus-producing) and HIV-1-infected CD4+ lymphocytes	531:648	In the present study, we show that HIV-1-infected lymphocytes of the CEM cell line (either latent or virus-producing) and HIV-1-infected CD4+ lymphocytes have several membrane proteins with altered glycosylation patterns.
8122360	7	67	theme	natural	1639:1645	arg1	CD22					1700:1703	the B-cell-specific surface receptor CD22	1663:1703	the B-cell-specific surface receptor CD22	1663:1703	Since CD45 glycoproteins are thought to play an important regulatory role in cell-to-cell interactions owing to their variable extracellular region and because they may regulate membrane signaling through their intracellular phosphatase domains, we suggest that these altered CD45 molecules may present an abnormal signal for natural ligands such as the B-cell-specific surface receptor CD22, thus perturbing the normal immune response in HIV-1-infected individuals.
8122360	7	67	theme	natural	1639:1645	arg1	ligands					1647:1653	natural ligands	1639:1653	natural ligands such as the B-cell-specific surface receptor CD22	1639:1703	Since CD45 glycoproteins are thought to play an important regulatory role in cell-to-cell interactions owing to their variable extracellular region and because they may regulate membrane signaling through their intracellular phosphatase domains, we suggest that these altered CD45 molecules may present an abnormal signal for natural ligands such as the B-cell-specific surface receptor CD22, thus perturbing the normal immune response in HIV-1-infected individuals.
8122360	4	68	theme	Gal	911:913	arg1	1-->4GlcNAc					920:930	a terminal Gal beta 1-->4GlcNAc	900:930	a terminal Gal beta 1-->4GlcNAc	900:930	Using lectins with specificity for different carbohydrate moieties, we could demonstrate the presence of two exposed nonsialylated disaccharides: a terminal Gal beta 1-->3GalNAc and a terminal Gal beta 1-->4GlcNAc.
8122360	4	68	theme	Gal	911:913	arg1	disaccharides					849:861	two exposed nonsialylated disaccharides	823:861	two exposed nonsialylated disaccharides: a terminal Gal beta 1-->3GalNAc and a terminal Gal beta 1-->4GlcNAc	823:930	Using lectins with specificity for different carbohydrate moieties, we could demonstrate the presence of two exposed nonsialylated disaccharides: a terminal Gal beta 1-->3GalNAc and a terminal Gal beta 1-->4GlcNAc.
8122360	6	69	theme	phosphatase	1216:1226	arg1	activity					1228:1235	the total tyrosine phosphatase activity	1197:1235	the total tyrosine phosphatase activity displayed by CD45 molecules from one latently HIV-1-infected CEM cell line	1197:1310	Concerning the latter, PNA lectin which recognizes nonsialylated terminal Gal beta 1-->3GalNAc might precipitate up to 75% of the total tyrosine phosphatase activity displayed by CD45 molecules from one latently HIV-1-infected CEM cell line.
8122360	5	70	theme	O-linked	1039:1046	arg1	moieties					1061:1068	O-linked carbohydrate moieties	1039:1068	O-linked carbohydrate moieties	1039:1068	In particular, CD45, one of the major T cell glycoproteins, appeared to be partially sialylated on N- and O-linked carbohydrate moieties.
8122360	2	71	theme	cell	274:277	arg1	functions					279:287	T cell functions	272:287	T cell functions	272:287	Despite description of the virus cytopathicity and numerous modifications in T cell functions, such as perturbation of antigen receptor signaling, CD4 downregulation, and induction of apoptosis, the precise mechanisms underlying the disruption of normal immune responses have not yet been elucidated.
8122360	6	72	theme	total	1201:1205	arg1	activity					1228:1235	the total tyrosine phosphatase activity	1197:1235	the total tyrosine phosphatase activity displayed by CD45 molecules from one latently HIV-1-infected CEM cell line	1197:1310	Concerning the latter, PNA lectin which recognizes nonsialylated terminal Gal beta 1-->3GalNAc might precipitate up to 75% of the total tyrosine phosphatase activity displayed by CD45 molecules from one latently HIV-1-infected CEM cell line.
8122360	1	73	theme	normal	150:155	arg1	properties					170:179	normal T lymphocyte properties	150:179	normal T lymphocyte properties	150:179	Immunodeficiency caused by HIV infection probably results from profound dysregulation of normal T lymphocyte properties by the virus.
8122360	5	74	link	O-linked	1039:1046	arg1	moieties					1061:1068	O-linked carbohydrate moieties	1039:1068	O-linked carbohydrate moieties	1039:1068	In particular, CD45, one of the major T cell glycoproteins, appeared to be partially sialylated on N- and O-linked carbohydrate moieties.
8122360	7	75	from	response	1740:1747	arg1	individuals					1767:1777	HIV-1-infected individuals	1752:1777	HIV-1-infected individuals	1752:1777	Since CD45 glycoproteins are thought to play an important regulatory role in cell-to-cell interactions owing to their variable extracellular region and because they may regulate membrane signaling through their intracellular phosphatase domains, we suggest that these altered CD45 molecules may present an abnormal signal for natural ligands such as the B-cell-specific surface receptor CD22, thus perturbing the normal immune response in HIV-1-infected individuals.
8122360	1	76	theme	lymphocyte	159:168	arg1	properties					170:179	normal T lymphocyte properties	150:179	normal T lymphocyte properties	150:179	Immunodeficiency caused by HIV infection probably results from profound dysregulation of normal T lymphocyte properties by the virus.
8122360	0	77	from	sialylation	8:18	arg1	lymphocytes					48:58	HIV-1-infected T lymphocytes	31:58	HIV-1-infected T lymphocytes	31:58	Altered sialylation of CD45 in HIV-1-infected T lymphocytes.
8122360	5	78	theme	major	965:969	arg1	glycoproteins					978:990	the major T cell glycoproteins	961:990	the major T cell glycoproteins	961:990	In particular, CD45, one of the major T cell glycoproteins, appeared to be partially sialylated on N- and O-linked carbohydrate moieties.
8122360	7	79	theme	HIV-1-infected	1752:1765	arg1	individuals					1767:1777	HIV-1-infected individuals	1752:1777	HIV-1-infected individuals	1752:1777	Since CD45 glycoproteins are thought to play an important regulatory role in cell-to-cell interactions owing to their variable extracellular region and because they may regulate membrane signaling through their intracellular phosphatase domains, we suggest that these altered CD45 molecules may present an abnormal signal for natural ligands such as the B-cell-specific surface receptor CD22, thus perturbing the normal immune response in HIV-1-infected individuals.
8122360	7	80	theme	CD45	1589:1592	arg1	molecules					1594:1602	these altered CD45 molecules	1575:1602	these altered CD45 molecules	1575:1602	Since CD45 glycoproteins are thought to play an important regulatory role in cell-to-cell interactions owing to their variable extracellular region and because they may regulate membrane signaling through their intracellular phosphatase domains, we suggest that these altered CD45 molecules may present an abnormal signal for natural ligands such as the B-cell-specific surface receptor CD22, thus perturbing the normal immune response in HIV-1-infected individuals.
8122360	5	81	theme	cell	973:976	arg1	glycoproteins					978:990	the major T cell glycoproteins	961:990	the major T cell glycoproteins	961:990	In particular, CD45, one of the major T cell glycoproteins, appeared to be partially sialylated on N- and O-linked carbohydrate moieties.
8122360	1	82	theme	HIV	88:90	arg1	infection					92:100	HIV infection	88:100	HIV infection	88:100	Immunodeficiency caused by HIV infection probably results from profound dysregulation of normal T lymphocyte properties by the virus.
8122360	7	83	theme	normal	1726:1731	arg1	response					1740:1747	the normal immune response	1722:1747	the normal immune response in HIV-1-infected individuals	1722:1777	Since CD45 glycoproteins are thought to play an important regulatory role in cell-to-cell interactions owing to their variable extracellular region and because they may regulate membrane signaling through their intracellular phosphatase domains, we suggest that these altered CD45 molecules may present an abnormal signal for natural ligands such as the B-cell-specific surface receptor CD22, thus perturbing the normal immune response in HIV-1-infected individuals.
8122360	2	84	theme	immune	449:454	arg1	responses					456:464	normal immune responses	442:464	normal immune responses	442:464	Despite description of the virus cytopathicity and numerous modifications in T cell functions, such as perturbation of antigen receptor signaling, CD4 downregulation, and induction of apoptosis, the precise mechanisms underlying the disruption of normal immune responses have not yet been elucidated.
8122360	6	85	gly	nonsialylated	1122:1134	arg1	1-->3GalNAc					1154:1164	nonsialylated terminal Gal beta 1-->3GalNAc	1122:1164	nonsialylated terminal Gal beta 1-->3GalNAc	1122:1164	Concerning the latter, PNA lectin which recognizes nonsialylated terminal Gal beta 1-->3GalNAc might precipitate up to 75% of the total tyrosine phosphatase activity displayed by CD45 molecules from one latently HIV-1-infected CEM cell line.
8122360	2	86	theme	apoptosis	379:387	arg1	induction					366:374	induction	366:374	induction of apoptosis	366:387	Despite description of the virus cytopathicity and numerous modifications in T cell functions, such as perturbation of antigen receptor signaling, CD4 downregulation, and induction of apoptosis, the precise mechanisms underlying the disruption of normal immune responses have not yet been elucidated.
8122360	0	87	theme	CD45	23:26	arg1	sialylation					8:18	Altered sialylation	0:18	Altered sialylation of CD45 in HIV-1-infected T lymphocytes	0:58	Altered sialylation of CD45 in HIV-1-infected T lymphocytes.
8122360	2	88	from	modifications	255:267	arg1	functions					279:287	T cell functions	272:287	T cell functions	272:287	Despite description of the virus cytopathicity and numerous modifications in T cell functions, such as perturbation of antigen receptor signaling, CD4 downregulation, and induction of apoptosis, the precise mechanisms underlying the disruption of normal immune responses have not yet been elucidated.
8122360	3	89	theme	lymphocytes	638:648	arg1	lymphocytes					546:556	HIV-1-infected lymphocytes	531:556	HIV-1-infected lymphocytes of the CEM cell line (either latent or virus-producing) and HIV-1-infected CD4+ lymphocytes	531:648	In the present study, we show that HIV-1-infected lymphocytes of the CEM cell line (either latent or virus-producing) and HIV-1-infected CD4+ lymphocytes have several membrane proteins with altered glycosylation patterns.
8122360	4	90	theme	carbohydrate	763:774	arg1	moieties					776:783	different carbohydrate moieties	753:783	different carbohydrate moieties	753:783	Using lectins with specificity for different carbohydrate moieties, we could demonstrate the presence of two exposed nonsialylated disaccharides: a terminal Gal beta 1-->3GalNAc and a terminal Gal beta 1-->4GlcNAc.
8122360	0	91	theme	HIV-1-infected	31:44	arg1	lymphocytes					48:58	HIV-1-infected T lymphocytes	31:58	HIV-1-infected T lymphocytes	31:58	Altered sialylation of CD45 in HIV-1-infected T lymphocytes.
8122360	7	92	theme	altered	1581:1587	arg1	molecules					1594:1602	these altered CD45 molecules	1575:1602	these altered CD45 molecules	1575:1602	Since CD45 glycoproteins are thought to play an important regulatory role in cell-to-cell interactions owing to their variable extracellular region and because they may regulate membrane signaling through their intracellular phosphatase domains, we suggest that these altered CD45 molecules may present an abnormal signal for natural ligands such as the B-cell-specific surface receptor CD22, thus perturbing the normal immune response in HIV-1-infected individuals.
8122360	3	93	theme	HIV-1-infected	618:631	arg1	lymphocytes					638:648	HIV-1-infected CD4+ lymphocytes	618:648	HIV-1-infected CD4+ lymphocytes	618:648	In the present study, we show that HIV-1-infected lymphocytes of the CEM cell line (either latent or virus-producing) and HIV-1-infected CD4+ lymphocytes have several membrane proteins with altered glycosylation patterns.
8122360	4	94	theme	exposed	827:833	arg1	1-->4GlcNAc					920:930	a terminal Gal beta 1-->4GlcNAc	900:930	a terminal Gal beta 1-->4GlcNAc	900:930	Using lectins with specificity for different carbohydrate moieties, we could demonstrate the presence of two exposed nonsialylated disaccharides: a terminal Gal beta 1-->3GalNAc and a terminal Gal beta 1-->4GlcNAc.
8122360	4	94	theme	exposed	827:833	arg1	disaccharides					849:861	two exposed nonsialylated disaccharides	823:861	two exposed nonsialylated disaccharides: a terminal Gal beta 1-->3GalNAc and a terminal Gal beta 1-->4GlcNAc	823:930	Using lectins with specificity for different carbohydrate moieties, we could demonstrate the presence of two exposed nonsialylated disaccharides: a terminal Gal beta 1-->3GalNAc and a terminal Gal beta 1-->4GlcNAc.
8122360	4	94	theme	exposed	827:833	arg1	1-->3GalNAc					884:894	a terminal Gal beta 1-->3GalNAc	864:894	a terminal Gal beta 1-->3GalNAc	864:894	Using lectins with specificity for different carbohydrate moieties, we could demonstrate the presence of two exposed nonsialylated disaccharides: a terminal Gal beta 1-->3GalNAc and a terminal Gal beta 1-->4GlcNAc.
8122360	6	95	from	line	1307:1310	arg1	molecules					1255:1263	CD45 molecules	1250:1263	CD45 molecules from one latently HIV-1-infected CEM cell line	1250:1310	Concerning the latter, PNA lectin which recognizes nonsialylated terminal Gal beta 1-->3GalNAc might precipitate up to 75% of the total tyrosine phosphatase activity displayed by CD45 molecules from one latently HIV-1-infected CEM cell line.
8122360	7	96	dep	thought	1342:1348	arg1	regulate					1482:1489	regulate	1482:1489	may regulate membrane signaling through their intracellular phosphatase domains	1478:1556	Since CD45 glycoproteins are thought to play an important regulatory role in cell-to-cell interactions owing to their variable extracellular region and because they may regulate membrane signaling through their intracellular phosphatase domains, we suggest that these altered CD45 molecules may present an abnormal signal for natural ligands such as the B-cell-specific surface receptor CD22, thus perturbing the normal immune response in HIV-1-infected individuals.
8122360	6	97	theme	Gal	1145:1147	arg1	1-->3GalNAc					1154:1164	nonsialylated terminal Gal beta 1-->3GalNAc	1122:1164	nonsialylated terminal Gal beta 1-->3GalNAc	1122:1164	Concerning the latter, PNA lectin which recognizes nonsialylated terminal Gal beta 1-->3GalNAc might precipitate up to 75% of the total tyrosine phosphatase activity displayed by CD45 molecules from one latently HIV-1-infected CEM cell line.
8122360	4	98	theme	disaccharides	849:861	arg1	presence					811:818	the presence	807:818	the presence of two exposed nonsialylated disaccharides: a terminal Gal beta 1-->3GalNAc and a terminal Gal beta 1-->4GlcNAc	807:930	Using lectins with specificity for different carbohydrate moieties, we could demonstrate the presence of two exposed nonsialylated disaccharides: a terminal Gal beta 1-->3GalNAc and a terminal Gal beta 1-->4GlcNAc.
8122360	2	99	theme	CD4	342:344	arg1	downregulation					346:359	CD4 downregulation	342:359	CD4 downregulation	342:359	Despite description of the virus cytopathicity and numerous modifications in T cell functions, such as perturbation of antigen receptor signaling, CD4 downregulation, and induction of apoptosis, the precise mechanisms underlying the disruption of normal immune responses have not yet been elucidated.
8122360	6	100	theme	nonsialylated	1122:1134	arg1	1-->3GalNAc					1154:1164	nonsialylated terminal Gal beta 1-->3GalNAc	1122:1164	nonsialylated terminal Gal beta 1-->3GalNAc	1122:1164	Concerning the latter, PNA lectin which recognizes nonsialylated terminal Gal beta 1-->3GalNAc might precipitate up to 75% of the total tyrosine phosphatase activity displayed by CD45 molecules from one latently HIV-1-infected CEM cell line.
8122360	3	101	theme	several	655:661	arg1	proteins					672:679	several membrane proteins	655:679	several membrane proteins with altered glycosylation patterns	655:715	In the present study, we show that HIV-1-infected lymphocytes of the CEM cell line (either latent or virus-producing) and HIV-1-infected CD4+ lymphocytes have several membrane proteins with altered glycosylation patterns.
8122360	2	102	theme	signaling	331:339	arg1	perturbation					298:309	perturbation	298:309	perturbation of antigen receptor signaling	298:339	Despite description of the virus cytopathicity and numerous modifications in T cell functions, such as perturbation of antigen receptor signaling, CD4 downregulation, and induction of apoptosis, the precise mechanisms underlying the disruption of normal immune responses have not yet been elucidated.
8122360	5	103	gly	sialylated	1018:1027	arg1	glycoproteins					978:990	the major T cell glycoproteins	961:990	the major T cell glycoproteins	961:990	In particular, CD45, one of the major T cell glycoproteins, appeared to be partially sialylated on N- and O-linked carbohydrate moieties.
8122360	5	103	gly	sialylated	1018:1027	arg1	one					954:956	one	954:956	one	954:956	In particular, CD45, one of the major T cell glycoproteins, appeared to be partially sialylated on N- and O-linked carbohydrate moieties.
8122360	5	103	gly	sialylated	1018:1027	arg1	CD45					948:951	CD45	948:951	CD45	948:951	In particular, CD45, one of the major T cell glycoproteins, appeared to be partially sialylated on N- and O-linked carbohydrate moieties.
2943741	4	0	theme	beta	921:924	arg1	1----3GalNAcOH					759:772	GalNAcOH, Gal beta 1----3GalNAcOH	740:772	GalNAcOH, Gal beta 1----3GalNAcOH	740:772	Oligosaccharides from K562 cells were found to be GalNAcOH, Gal beta 1----3GalNAcOH, NeuNAc alpha 2----6GalNAcOH, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH.
2943741	4	0	theme	beta	921:924	arg1	GalNAcOH					953:960	NeuNAc alpha 2----6GalNAcOH, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH	775:960	NeuNAc alpha 2----6GalNAcOH, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH	775:960	Oligosaccharides from K562 cells were found to be GalNAcOH, Gal beta 1----3GalNAcOH, NeuNAc alpha 2----6GalNAcOH, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH.
2943741	5	1	theme	2----3	1213:1218	arg1	beta					1188:1191	Gal beta 1----4GlcNAc beta 1----6	1166:1198	Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH	1166:1243	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	5	1	theme	2----3	1213:1218	arg1	beta					1224:1227	NeuNAc alpha 2----3)Gal beta 1----3	1200:1234	NeuNAc alpha 2----3)Gal beta 1----3	1200:1234	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	2	2	from	cells	350:354	arg1	immunoprecipitation					325:343	specific immunoprecipitation	316:343	specific immunoprecipitation from cells which were metabolically labeled with [3H]glucosamine	316:408	Leukosialin was isolated by specific immunoprecipitation from cells which were metabolically labeled with [3H]glucosamine, and glycopeptides were isolated after Pronase digestion.
2943741	5	3	theme	Gal	1220:1222	arg1	beta					1188:1191	Gal beta 1----4GlcNAc beta 1----6	1166:1198	Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH	1166:1243	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	5	3	theme	Gal	1220:1222	arg1	beta					1224:1227	NeuNAc alpha 2----3)Gal beta 1----3	1200:1234	NeuNAc alpha 2----3)Gal beta 1----3	1200:1234	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	5	4	theme	alpha	1207:1211	arg1	beta					1188:1191	Gal beta 1----4GlcNAc beta 1----6	1166:1198	Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH	1166:1243	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	5	4	theme	alpha	1207:1211	arg1	beta					1224:1227	NeuNAc alpha 2----3)Gal beta 1----3	1200:1234	NeuNAc alpha 2----3)Gal beta 1----3	1200:1234	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	5	5	from	cells	1020:1024	arg1	oligosaccharides					982:997	oligosaccharides	982:997	oligosaccharides from HL-60 and HSB-2 cells	982:1024	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	4	6	theme	alpha	905:909	arg1	beta					921:924	NeuNAc alpha 2----3Gal beta 1----3	898:931	NeuNAc alpha 2----3Gal beta 1----3	898:931	Oligosaccharides from K562 cells were found to be GalNAcOH, Gal beta 1----3GalNAcOH, NeuNAc alpha 2----6GalNAcOH, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH.
2943741	0	7	attach	present	51:57	arg2	variations					11:20	Structural variations	0:20	Structural variations of O-linked oligosaccharides	0:49	Structural variations of O-linked oligosaccharides present in leukosialin isolated from erythroid, myeloid, and T-lymphoid cell lines.
2943741	0	7	attach	present	51:57	arg1	leukosialin					62:72	leukosialin	62:72	leukosialin isolated from erythroid, myeloid, and T-lymphoid cell lines	62:132	Structural variations of O-linked oligosaccharides present in leukosialin isolated from erythroid, myeloid, and T-lymphoid cell lines.
2943741	1	8	theme	K562	204:207	arg1	lines					267:271	K562 erythroid, HL-60 promyelocytic, and HSB-2 T-lymphoid cell lines	204:271	K562 erythroid, HL-60 promyelocytic, and HSB-2 T-lymphoid cell lines	204:271	Structures of O-linked oligosaccharides of leukosialin isolated from K562 erythroid, HL-60 promyelocytic, and HSB-2 T-lymphoid cell lines were examined.
2943741	4	9	theme	K562	712:715	arg1	cells					717:721	K562 cells	712:721	K562 cells	712:721	Oligosaccharides from K562 cells were found to be GalNAcOH, Gal beta 1----3GalNAcOH, NeuNAc alpha 2----6GalNAcOH, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH.
2943741	0	10	theme	cell	123:126	arg1	lines					128:132	erythroid, myeloid, and T-lymphoid cell lines	88:132	erythroid, myeloid, and T-lymphoid cell lines	88:132	Structural variations of O-linked oligosaccharides present in leukosialin isolated from erythroid, myeloid, and T-lymphoid cell lines.
2943741	5	11	theme	alpha	1094:1098	arg1	beta					1128:1131	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	1087:1138	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH	1087:1163	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	5	11	theme	alpha	1094:1098	arg1	beta					1144:1147	Gal beta 1----3	1140:1154	Gal beta 1----3	1140:1154	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	3	12	theme	exoglycosidase	619:632	arg1	digestion					634:642	specific exoglycosidase digestion	610:642	specific exoglycosidase digestion	610:642	O-Linked oligosaccharides were released by alkaline borohydride treatment, and the structures of purified oligosaccharides were elucidated by specific exoglycosidase digestion, Smith degradation, and methylation anaylsis.
2943741	6	13	theme	cell	1497:1500	arg1	line					1502:1505	each erythroid or myeloid (and T-lymphoid) cell line	1454:1505	each erythroid or myeloid (and T-lymphoid) cell line	1454:1505	These results clearly indicate that leukosialin can be differently glycosylated with O-linked chains, and each erythroid or myeloid (and T-lymphoid) cell line expresses a characteristic set of O-linked oligosaccharides which differ in core structures as well as in sialylation.
2943741	5	14	theme	beta	1110:1113	arg1	beta					1128:1131	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	1087:1138	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH	1087:1163	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	5	14	theme	beta	1110:1113	arg1	beta					1144:1147	Gal beta 1----3	1140:1154	Gal beta 1----3	1140:1154	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	6	15	theme	O-linked	1433:1440	arg1	chains					1442:1447	O-linked chains	1433:1447	O-linked chains	1433:1447	These results clearly indicate that leukosialin can be differently glycosylated with O-linked chains, and each erythroid or myeloid (and T-lymphoid) cell line expresses a characteristic set of O-linked oligosaccharides which differ in core structures as well as in sialylation.
2943741	1	16	theme	promyelocytic	226:238	arg1	HL-60					220:224	HL-60 promyelocytic	220:238	HL-60 promyelocytic	220:238	Structures of O-linked oligosaccharides of leukosialin isolated from K562 erythroid, HL-60 promyelocytic, and HSB-2 T-lymphoid cell lines were examined.
2943741	4	17	theme	NeuNAc	775:780	arg1	alpha					782:786	NeuNAc alpha 2----6GalNAcOH	775:801	NeuNAc alpha 2----6GalNAcOH	775:801	Oligosaccharides from K562 cells were found to be GalNAcOH, Gal beta 1----3GalNAcOH, NeuNAc alpha 2----6GalNAcOH, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH.
2943741	4	17	theme	NeuNAc	775:780	arg1	alpha					940:944	NeuNAc alpha 2----6	933:951	NeuNAc alpha 2----6	933:951	Oligosaccharides from K562 cells were found to be GalNAcOH, Gal beta 1----3GalNAcOH, NeuNAc alpha 2----6GalNAcOH, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH.
2943741	4	17	theme	NeuNAc	775:780	arg1	alpha					871:875	NeuNAc alpha 2----6	864:882	NeuNAc alpha 2----6	864:882	Oligosaccharides from K562 cells were found to be GalNAcOH, Gal beta 1----3GalNAcOH, NeuNAc alpha 2----6GalNAcOH, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH.
2943741	5	18	theme	beta	1066:1069	arg1	GalNAcOH					1338:1345	NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH	1043:1345	NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH	1043:1345	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	6	19	theme	core	1583:1586	arg1	structures					1588:1597	core structures	1583:1597	core structures	1583:1597	These results clearly indicate that leukosialin can be differently glycosylated with O-linked chains, and each erythroid or myeloid (and T-lymphoid) cell line expresses a characteristic set of O-linked oligosaccharides which differ in core structures as well as in sialylation.
2943741	5	20	theme	beta	1273:1276	arg1	beta					1326:1329	NeuNAc alpha 2----3Gal beta 1----3	1303:1336	NeuNAc alpha 2----3Gal beta 1----3	1303:1336	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	5	20	theme	beta	1273:1276	arg1	beta					1291:1294	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	1250:1301	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)	1250:1337	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	4	21	theme	Gal	750:752	arg1	1----3GalNAcOH					759:772	GalNAcOH, Gal beta 1----3GalNAcOH	740:772	GalNAcOH, Gal beta 1----3GalNAcOH	740:772	Oligosaccharides from K562 cells were found to be GalNAcOH, Gal beta 1----3GalNAcOH, NeuNAc alpha 2----6GalNAcOH, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH.
2943741	4	21	theme	Gal	750:752	arg1	GalNAcOH					953:960	NeuNAc alpha 2----6GalNAcOH, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH	775:960	NeuNAc alpha 2----6GalNAcOH, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH	775:960	Oligosaccharides from K562 cells were found to be GalNAcOH, Gal beta 1----3GalNAcOH, NeuNAc alpha 2----6GalNAcOH, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH.
2943741	5	22	theme	beta	1291:1294	arg1	GalNAcOH					1338:1345	NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH	1043:1345	NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH	1043:1345	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	6	23	theme	oligosaccharides	1550:1565	arg1	set					1534:1536	a characteristic set	1517:1536	a characteristic set of O-linked oligosaccharides which differ in core structures as well as in sialylation	1517:1623	These results clearly indicate that leukosialin can be differently glycosylated with O-linked chains, and each erythroid or myeloid (and T-lymphoid) cell line expresses a characteristic set of O-linked oligosaccharides which differ in core structures as well as in sialylation.
2943741	6	23	theme	oligosaccharides	1550:1565	arg1	oligosaccharides					1550:1565	O-linked oligosaccharides	1541:1565	O-linked oligosaccharides which differ in core structures as well as in sialylation	1541:1623	These results clearly indicate that leukosialin can be differently glycosylated with O-linked chains, and each erythroid or myeloid (and T-lymphoid) cell line expresses a characteristic set of O-linked oligosaccharides which differ in core structures as well as in sialylation.
2943741	1	24	theme	O-linked	149:156	arg1	oligosaccharides					158:173	O-linked oligosaccharides	149:173	O-linked oligosaccharides of leukosialin isolated from K562 erythroid, HL-60 promyelocytic, and HSB-2 T-lymphoid cell lines	149:271	Structures of O-linked oligosaccharides of leukosialin isolated from K562 erythroid, HL-60 promyelocytic, and HSB-2 T-lymphoid cell lines were examined.
2943741	0	25	theme	erythroid	88:96	arg1	lines					128:132	erythroid, myeloid, and T-lymphoid cell lines	88:132	erythroid, myeloid, and T-lymphoid cell lines	88:132	Structural variations of O-linked oligosaccharides present in leukosialin isolated from erythroid, myeloid, and T-lymphoid cell lines.
2943741	5	26	theme	alpha	1257:1261	arg1	beta					1326:1329	NeuNAc alpha 2----3Gal beta 1----3	1303:1336	NeuNAc alpha 2----3Gal beta 1----3	1303:1336	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	5	26	theme	alpha	1257:1261	arg1	beta					1291:1294	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	1250:1301	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)	1250:1337	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	0	27	theme	myeloid	99:105	arg1	lines					128:132	erythroid, myeloid, and T-lymphoid cell lines	88:132	erythroid, myeloid, and T-lymphoid cell lines	88:132	Structural variations of O-linked oligosaccharides present in leukosialin isolated from erythroid, myeloid, and T-lymphoid cell lines.
2943741	5	28	theme	beta	1128:1131	arg1	GalNAcOH					1156:1163	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH	1087:1163	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH	1087:1163	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	5	29	theme	HL-60	1004:1008	arg1	cells					1020:1024	HL-60 and HSB-2 cells	1004:1024	HL-60 and HSB-2 cells	1004:1024	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	4	30	theme	Gal	848:850	arg1	beta					852:855	Gal beta 1----3	848:862	Gal beta 1----3	848:862	Oligosaccharides from K562 cells were found to be GalNAcOH, Gal beta 1----3GalNAcOH, NeuNAc alpha 2----6GalNAcOH, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH.
2943741	3	31	theme	O-Linked	468:475	arg1	oligosaccharides					477:492	O-Linked oligosaccharides	468:492	O-Linked oligosaccharides	468:492	O-Linked oligosaccharides were released by alkaline borohydride treatment, and the structures of purified oligosaccharides were elucidated by specific exoglycosidase digestion, Smith degradation, and methylation anaylsis.
2943741	5	32	located	found	1031:1035	arg2	oligosaccharides					982:997	oligosaccharides	982:997	oligosaccharides from HL-60 and HSB-2 cells	982:1024	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	5	32	located	found	1031:1035	arg1	hand					976:979	the other hand	966:979	the other hand	966:979	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	5	33	theme	HSB-2	1014:1018	arg1	cells					1020:1024	HL-60 and HSB-2 cells	1004:1024	HL-60 and HSB-2 cells	1004:1024	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	4	34	theme	NeuNAc	804:809	arg1	beta					827:830	NeuNAc alpha 2----3Gal beta 1----3GalNAcOH	804:845	NeuNAc alpha 2----3Gal beta 1----3GalNAcOH	804:845	Oligosaccharides from K562 cells were found to be GalNAcOH, Gal beta 1----3GalNAcOH, NeuNAc alpha 2----6GalNAcOH, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH.
2943741	0	35	theme	Structural	0:9	arg1	variations					11:20	Structural variations	0:20	Structural variations of O-linked oligosaccharides	0:49	Structural variations of O-linked oligosaccharides present in leukosialin isolated from erythroid, myeloid, and T-lymphoid cell lines.
2943741	5	36	theme	beta	1188:1191	arg1	GalNAcOH					1236:1243	Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH	1166:1243	Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH	1166:1243	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	4	37	theme	2----3Gal	817:825	arg1	beta					827:830	NeuNAc alpha 2----3Gal beta 1----3GalNAcOH	804:845	NeuNAc alpha 2----3Gal beta 1----3GalNAcOH	804:845	Oligosaccharides from K562 cells were found to be GalNAcOH, Gal beta 1----3GalNAcOH, NeuNAc alpha 2----6GalNAcOH, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH.
2943741	2	38	theme	Pronase	449:455	arg1	digestion					457:465	Pronase digestion	449:465	Pronase digestion	449:465	Leukosialin was isolated by specific immunoprecipitation from cells which were metabolically labeled with [3H]glucosamine, and glycopeptides were isolated after Pronase digestion.
2943741	5	39	theme	alpha	1310:1314	arg1	beta					1326:1329	NeuNAc alpha 2----3Gal beta 1----3	1303:1336	NeuNAc alpha 2----3Gal beta 1----3	1303:1336	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	5	39	theme	alpha	1310:1314	arg1	beta					1291:1294	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	1250:1301	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)	1250:1337	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	0	40	theme	oligosaccharides	34:49	arg1	variations					11:20	Structural variations	0:20	Structural variations of O-linked oligosaccharides	0:49	Structural variations of O-linked oligosaccharides present in leukosialin isolated from erythroid, myeloid, and T-lymphoid cell lines.
2943741	5	41	theme	NeuNAc	1043:1048	arg1	beta					1066:1069	NeuNAc alpha 2----3Gal beta 1----3GalNAcOH	1043:1084	NeuNAc alpha 2----3Gal beta 1----3GalNAcOH	1043:1084	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	0	42	attach	isolated	74:81	arg2	leukosialin					62:72	leukosialin	62:72	leukosialin isolated from erythroid, myeloid, and T-lymphoid cell lines	62:132	Structural variations of O-linked oligosaccharides present in leukosialin isolated from erythroid, myeloid, and T-lymphoid cell lines.
2943741	0	42	attach	isolated	74:81	arg1	lines					128:132	erythroid, myeloid, and T-lymphoid cell lines	88:132	erythroid, myeloid, and T-lymphoid cell lines	88:132	Structural variations of O-linked oligosaccharides present in leukosialin isolated from erythroid, myeloid, and T-lymphoid cell lines.
2943741	4	43	theme	GalNAcOH	884:891	arg1	1----3GalNAcOH					759:772	GalNAcOH, Gal beta 1----3GalNAcOH	740:772	GalNAcOH, Gal beta 1----3GalNAcOH	740:772	Oligosaccharides from K562 cells were found to be GalNAcOH, Gal beta 1----3GalNAcOH, NeuNAc alpha 2----6GalNAcOH, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH.
2943741	4	43	theme	GalNAcOH	884:891	arg1	GalNAcOH					953:960	NeuNAc alpha 2----6GalNAcOH, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH	775:960	NeuNAc alpha 2----6GalNAcOH, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH	775:960	Oligosaccharides from K562 cells were found to be GalNAcOH, Gal beta 1----3GalNAcOH, NeuNAc alpha 2----6GalNAcOH, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH.
2943741	5	44	theme	beta	1170:1173	arg1	beta					1224:1227	NeuNAc alpha 2----3)Gal beta 1----3	1200:1234	NeuNAc alpha 2----3)Gal beta 1----3	1200:1234	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	5	44	theme	beta	1170:1173	arg1	beta					1188:1191	Gal beta 1----4GlcNAc beta 1----6	1166:1198	Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH	1166:1243	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	5	45	theme	2----3Gal	1056:1064	arg1	beta					1066:1069	NeuNAc alpha 2----3Gal beta 1----3GalNAcOH	1043:1084	NeuNAc alpha 2----3Gal beta 1----3GalNAcOH	1043:1084	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	3	46	theme	borohydride	520:530	arg1	treatment					532:540	alkaline borohydride treatment	511:540	alkaline borohydride treatment	511:540	O-Linked oligosaccharides were released by alkaline borohydride treatment, and the structures of purified oligosaccharides were elucidated by specific exoglycosidase digestion, Smith degradation, and methylation anaylsis.
2943741	6	47	theme	characteristic	1519:1532	arg1	set					1534:1536	a characteristic set	1517:1536	a characteristic set of O-linked oligosaccharides which differ in core structures as well as in sialylation	1517:1623	These results clearly indicate that leukosialin can be differently glycosylated with O-linked chains, and each erythroid or myeloid (and T-lymphoid) cell line expresses a characteristic set of O-linked oligosaccharides which differ in core structures as well as in sialylation.
2943741	6	47	theme	characteristic	1519:1532	arg1	oligosaccharides					1550:1565	O-linked oligosaccharides	1541:1565	O-linked oligosaccharides which differ in core structures as well as in sialylation	1541:1623	These results clearly indicate that leukosialin can be differently glycosylated with O-linked chains, and each erythroid or myeloid (and T-lymphoid) cell line expresses a characteristic set of O-linked oligosaccharides which differ in core structures as well as in sialylation.
2943741	4	48	theme	NeuNAc	864:869	arg1	alpha					782:786	NeuNAc alpha 2----6GalNAcOH	775:801	NeuNAc alpha 2----6GalNAcOH	775:801	Oligosaccharides from K562 cells were found to be GalNAcOH, Gal beta 1----3GalNAcOH, NeuNAc alpha 2----6GalNAcOH, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH.
2943741	4	48	theme	NeuNAc	864:869	arg1	alpha					871:875	NeuNAc alpha 2----6	864:882	NeuNAc alpha 2----6	864:882	Oligosaccharides from K562 cells were found to be GalNAcOH, Gal beta 1----3GalNAcOH, NeuNAc alpha 2----6GalNAcOH, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH.
2943741	6	49	theme	myeloid	1472:1478	arg1	line					1502:1505	each erythroid or myeloid (and T-lymphoid) cell line	1454:1505	each erythroid or myeloid (and T-lymphoid) cell line	1454:1505	These results clearly indicate that leukosialin can be differently glycosylated with O-linked chains, and each erythroid or myeloid (and T-lymphoid) cell line expresses a characteristic set of O-linked oligosaccharides which differ in core structures as well as in sialylation.
2943741	6	50	theme	erythroid	1459:1467	arg1	line					1502:1505	each erythroid or myeloid (and T-lymphoid) cell line	1454:1505	each erythroid or myeloid (and T-lymphoid) cell line	1454:1505	These results clearly indicate that leukosialin can be differently glycosylated with O-linked chains, and each erythroid or myeloid (and T-lymphoid) cell line expresses a characteristic set of O-linked oligosaccharides which differ in core structures as well as in sialylation.
2943741	1	51	theme	cell	262:265	arg1	lines					267:271	K562 erythroid, HL-60 promyelocytic, and HSB-2 T-lymphoid cell lines	204:271	K562 erythroid, HL-60 promyelocytic, and HSB-2 T-lymphoid cell lines	204:271	Structures of O-linked oligosaccharides of leukosialin isolated from K562 erythroid, HL-60 promyelocytic, and HSB-2 T-lymphoid cell lines were examined.
2943741	4	52	theme	2----3Gal	911:919	arg1	beta					921:924	NeuNAc alpha 2----3Gal beta 1----3	898:931	NeuNAc alpha 2----3Gal beta 1----3	898:931	Oligosaccharides from K562 cells were found to be GalNAcOH, Gal beta 1----3GalNAcOH, NeuNAc alpha 2----6GalNAcOH, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH.
2943741	0	53	link	O-linked	25:32	arg1	oligosaccharides					34:49	O-linked oligosaccharides	25:49	O-linked oligosaccharides	25:49	Structural variations of O-linked oligosaccharides present in leukosialin isolated from erythroid, myeloid, and T-lymphoid cell lines.
2943741	3	54	theme	oligosaccharides	574:589	arg1	structures					551:560	the structures	547:560	the structures of purified oligosaccharides	547:589	O-Linked oligosaccharides were released by alkaline borohydride treatment, and the structures of purified oligosaccharides were elucidated by specific exoglycosidase digestion, Smith degradation, and methylation anaylsis.
2943741	1	55	theme	leukosialin	178:188	arg1	oligosaccharides					158:173	O-linked oligosaccharides	149:173	O-linked oligosaccharides of leukosialin isolated from K562 erythroid, HL-60 promyelocytic, and HSB-2 T-lymphoid cell lines	149:271	Structures of O-linked oligosaccharides of leukosialin isolated from K562 erythroid, HL-60 promyelocytic, and HSB-2 T-lymphoid cell lines were examined.
2943741	4	56	theme	NeuNAc	898:903	arg1	beta					921:924	NeuNAc alpha 2----3Gal beta 1----3	898:931	NeuNAc alpha 2----3Gal beta 1----3	898:931	Oligosaccharides from K562 cells were found to be GalNAcOH, Gal beta 1----3GalNAcOH, NeuNAc alpha 2----6GalNAcOH, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH.
2943741	2	57	theme	specific	316:323	arg1	immunoprecipitation					325:343	specific immunoprecipitation	316:343	specific immunoprecipitation from cells which were metabolically labeled with [3H]glucosamine	316:408	Leukosialin was isolated by specific immunoprecipitation from cells which were metabolically labeled with [3H]glucosamine, and glycopeptides were isolated after Pronase digestion.
2943741	4	58	from	cells	717:721	arg1	Oligosaccharides					690:705	Oligosaccharides	690:705	Oligosaccharides from K562 cells	690:721	Oligosaccharides from K562 cells were found to be GalNAcOH, Gal beta 1----3GalNAcOH, NeuNAc alpha 2----6GalNAcOH, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH.
2943741	1	59	theme	erythroid	209:217	arg1	lines					267:271	K562 erythroid, HL-60 promyelocytic, and HSB-2 T-lymphoid cell lines	204:271	K562 erythroid, HL-60 promyelocytic, and HSB-2 T-lymphoid cell lines	204:271	Structures of O-linked oligosaccharides of leukosialin isolated from K562 erythroid, HL-60 promyelocytic, and HSB-2 T-lymphoid cell lines were examined.
2943741	5	60	theme	2----3Gal	1100:1108	arg1	beta					1128:1131	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	1087:1138	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH	1087:1163	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	5	60	theme	2----3Gal	1100:1108	arg1	beta					1144:1147	Gal beta 1----3	1140:1154	Gal beta 1----3	1140:1154	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	1	61	theme	HL-60	220:224	arg1	lines					267:271	K562 erythroid, HL-60 promyelocytic, and HSB-2 T-lymphoid cell lines	204:271	K562 erythroid, HL-60 promyelocytic, and HSB-2 T-lymphoid cell lines	204:271	Structures of O-linked oligosaccharides of leukosialin isolated from K562 erythroid, HL-60 promyelocytic, and HSB-2 T-lymphoid cell lines were examined.
2943741	6	62	link	O-linked	1433:1440	arg1	chains					1442:1447	O-linked chains	1433:1447	O-linked chains	1433:1447	These results clearly indicate that leukosialin can be differently glycosylated with O-linked chains, and each erythroid or myeloid (and T-lymphoid) cell line expresses a characteristic set of O-linked oligosaccharides which differ in core structures as well as in sialylation.
2943741	5	63	theme	1----4GlcNAc	1115:1126	arg1	beta					1128:1131	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	1087:1138	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH	1087:1163	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	5	63	theme	1----4GlcNAc	1115:1126	arg1	beta					1144:1147	Gal beta 1----3	1140:1154	Gal beta 1----3	1140:1154	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	3	64	theme	Smith	645:649	arg1	degradation					651:661	Smith degradation	645:661	Smith degradation	645:661	O-Linked oligosaccharides were released by alkaline borohydride treatment, and the structures of purified oligosaccharides were elucidated by specific exoglycosidase digestion, Smith degradation, and methylation anaylsis.
2943741	4	65	theme	NeuNAc	933:938	arg1	alpha					782:786	NeuNAc alpha 2----6GalNAcOH	775:801	NeuNAc alpha 2----6GalNAcOH	775:801	Oligosaccharides from K562 cells were found to be GalNAcOH, Gal beta 1----3GalNAcOH, NeuNAc alpha 2----6GalNAcOH, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH.
2943741	4	65	theme	NeuNAc	933:938	arg1	alpha					940:944	NeuNAc alpha 2----6	933:951	NeuNAc alpha 2----6	933:951	Oligosaccharides from K562 cells were found to be GalNAcOH, Gal beta 1----3GalNAcOH, NeuNAc alpha 2----6GalNAcOH, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH.
2943741	5	66	theme	2----3Gal	1263:1271	arg1	beta					1326:1329	NeuNAc alpha 2----3Gal beta 1----3	1303:1336	NeuNAc alpha 2----3Gal beta 1----3	1303:1336	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	5	66	theme	2----3Gal	1263:1271	arg1	beta					1291:1294	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	1250:1301	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)	1250:1337	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	3	67	theme	specific	610:617	arg1	digestion					634:642	specific exoglycosidase digestion	610:642	specific exoglycosidase digestion	610:642	O-Linked oligosaccharides were released by alkaline borohydride treatment, and the structures of purified oligosaccharides were elucidated by specific exoglycosidase digestion, Smith degradation, and methylation anaylsis.
2943741	4	68	theme	alpha	782:786	arg1	1----3GalNAcOH					759:772	GalNAcOH, Gal beta 1----3GalNAcOH	740:772	GalNAcOH, Gal beta 1----3GalNAcOH	740:772	Oligosaccharides from K562 cells were found to be GalNAcOH, Gal beta 1----3GalNAcOH, NeuNAc alpha 2----6GalNAcOH, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH.
2943741	4	68	theme	alpha	782:786	arg1	GalNAcOH					953:960	NeuNAc alpha 2----6GalNAcOH, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH	775:960	NeuNAc alpha 2----6GalNAcOH, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH	775:960	Oligosaccharides from K562 cells were found to be GalNAcOH, Gal beta 1----3GalNAcOH, NeuNAc alpha 2----6GalNAcOH, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH.
2943741	5	69	theme	1----4GlcNAc	1278:1289	arg1	beta					1326:1329	NeuNAc alpha 2----3Gal beta 1----3	1303:1336	NeuNAc alpha 2----3Gal beta 1----3	1303:1336	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	5	69	theme	1----4GlcNAc	1278:1289	arg1	beta					1291:1294	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	1250:1301	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)	1250:1337	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	5	70	theme	NeuNAc	1087:1092	arg1	beta					1128:1131	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	1087:1138	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH	1087:1163	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	5	70	theme	NeuNAc	1087:1092	arg1	beta					1144:1147	Gal beta 1----3	1140:1154	Gal beta 1----3	1140:1154	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	3	71	theme	methylation	668:678	arg1	anaylsis					680:687	methylation anaylsis	668:687	methylation anaylsis	668:687	O-Linked oligosaccharides were released by alkaline borohydride treatment, and the structures of purified oligosaccharides were elucidated by specific exoglycosidase digestion, Smith degradation, and methylation anaylsis.
2943741	6	72	theme	O-linked	1541:1548	arg1	oligosaccharides					1550:1565	O-linked oligosaccharides	1541:1565	O-linked oligosaccharides which differ in core structures as well as in sialylation	1541:1623	These results clearly indicate that leukosialin can be differently glycosylated with O-linked chains, and each erythroid or myeloid (and T-lymphoid) cell line expresses a characteristic set of O-linked oligosaccharides which differ in core structures as well as in sialylation.
2943741	1	73	theme	oligosaccharides	158:173	arg1	Structures					135:144	Structures	135:144	Structures of O-linked oligosaccharides of leukosialin isolated from K562 erythroid, HL-60 promyelocytic, and HSB-2 T-lymphoid cell lines	135:271	Structures of O-linked oligosaccharides of leukosialin isolated from K562 erythroid, HL-60 promyelocytic, and HSB-2 T-lymphoid cell lines were examined.
2943741	4	74	theme	beta	754:757	arg1	1----3GalNAcOH					759:772	GalNAcOH, Gal beta 1----3GalNAcOH	740:772	GalNAcOH, Gal beta 1----3GalNAcOH	740:772	Oligosaccharides from K562 cells were found to be GalNAcOH, Gal beta 1----3GalNAcOH, NeuNAc alpha 2----6GalNAcOH, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH.
2943741	4	74	theme	beta	754:757	arg1	GalNAcOH					953:960	NeuNAc alpha 2----6GalNAcOH, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH	775:960	NeuNAc alpha 2----6GalNAcOH, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH	775:960	Oligosaccharides from K562 cells were found to be GalNAcOH, Gal beta 1----3GalNAcOH, NeuNAc alpha 2----6GalNAcOH, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH.
2943741	5	75	theme	NeuNAc	1250:1255	arg1	beta					1326:1329	NeuNAc alpha 2----3Gal beta 1----3	1303:1336	NeuNAc alpha 2----3Gal beta 1----3	1303:1336	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	5	75	theme	NeuNAc	1250:1255	arg1	beta					1291:1294	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	1250:1301	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)	1250:1337	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	5	76	theme	GalNAcOH	1156:1163	arg1	GalNAcOH					1338:1345	NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH	1043:1345	NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH	1043:1345	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	6	77	gly	glycosylated	1415:1426	arg1	leukosialin					1384:1394	leukosialin	1384:1394	leukosialin	1384:1394	These results clearly indicate that leukosialin can be differently glycosylated with O-linked chains, and each erythroid or myeloid (and T-lymphoid) cell line expresses a characteristic set of O-linked oligosaccharides which differ in core structures as well as in sialylation.
2943741	4	78	theme	beta	827:830	arg1	1----3GalNAcOH					759:772	GalNAcOH, Gal beta 1----3GalNAcOH	740:772	GalNAcOH, Gal beta 1----3GalNAcOH	740:772	Oligosaccharides from K562 cells were found to be GalNAcOH, Gal beta 1----3GalNAcOH, NeuNAc alpha 2----6GalNAcOH, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH.
2943741	4	78	theme	beta	827:830	arg1	GalNAcOH					953:960	NeuNAc alpha 2----6GalNAcOH, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH	775:960	NeuNAc alpha 2----6GalNAcOH, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH	775:960	Oligosaccharides from K562 cells were found to be GalNAcOH, Gal beta 1----3GalNAcOH, NeuNAc alpha 2----6GalNAcOH, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH.
2943741	5	79	theme	2----3Gal	1316:1324	arg1	beta					1326:1329	NeuNAc alpha 2----3Gal beta 1----3	1303:1336	NeuNAc alpha 2----3Gal beta 1----3	1303:1336	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	5	79	theme	2----3Gal	1316:1324	arg1	beta					1291:1294	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	1250:1301	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)	1250:1337	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	0	80	theme	T-lymphoid	112:121	arg1	lines					128:132	erythroid, myeloid, and T-lymphoid cell lines	88:132	erythroid, myeloid, and T-lymphoid cell lines	88:132	Structural variations of O-linked oligosaccharides present in leukosialin isolated from erythroid, myeloid, and T-lymphoid cell lines.
2943741	2	81	gly	glycopeptides	415:427	arg2	glycopeptides					415:427	glycopeptides	415:427	glycopeptides	415:427	Leukosialin was isolated by specific immunoprecipitation from cells which were metabolically labeled with [3H]glucosamine, and glycopeptides were isolated after Pronase digestion.
2943741	5	82	theme	Gal	1140:1142	arg1	beta					1128:1131	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	1087:1138	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH	1087:1163	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	5	82	theme	Gal	1140:1142	arg1	beta					1144:1147	Gal beta 1----3	1140:1154	Gal beta 1----3	1140:1154	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	5	83	theme	other	970:974	arg1	hand					976:979	the other hand	966:979	the other hand	966:979	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	0	84	theme	O-linked	25:32	arg1	oligosaccharides					34:49	O-linked oligosaccharides	25:49	O-linked oligosaccharides	25:49	Structural variations of O-linked oligosaccharides present in leukosialin isolated from erythroid, myeloid, and T-lymphoid cell lines.
2943741	1	85	attach	isolated	190:197	arg2	leukosialin					178:188	leukosialin	178:188	leukosialin isolated from K562 erythroid, HL-60 promyelocytic, and HSB-2 T-lymphoid cell lines	178:271	Structures of O-linked oligosaccharides of leukosialin isolated from K562 erythroid, HL-60 promyelocytic, and HSB-2 T-lymphoid cell lines were examined.
2943741	1	85	attach	isolated	190:197	arg1	lines					267:271	K562 erythroid, HL-60 promyelocytic, and HSB-2 T-lymphoid cell lines	204:271	K562 erythroid, HL-60 promyelocytic, and HSB-2 T-lymphoid cell lines	204:271	Structures of O-linked oligosaccharides of leukosialin isolated from K562 erythroid, HL-60 promyelocytic, and HSB-2 T-lymphoid cell lines were examined.
2943741	4	86	theme	alpha	811:815	arg1	beta					827:830	NeuNAc alpha 2----3Gal beta 1----3GalNAcOH	804:845	NeuNAc alpha 2----3Gal beta 1----3GalNAcOH	804:845	Oligosaccharides from K562 cells were found to be GalNAcOH, Gal beta 1----3GalNAcOH, NeuNAc alpha 2----6GalNAcOH, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH.
2943741	5	87	theme	NeuNAc	1303:1308	arg1	beta					1326:1329	NeuNAc alpha 2----3Gal beta 1----3	1303:1336	NeuNAc alpha 2----3Gal beta 1----3	1303:1336	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	5	87	theme	NeuNAc	1303:1308	arg1	beta					1291:1294	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	1250:1301	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)	1250:1337	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	3	88	theme	alkaline	511:518	arg1	treatment					532:540	alkaline borohydride treatment	511:540	alkaline borohydride treatment	511:540	O-Linked oligosaccharides were released by alkaline borohydride treatment, and the structures of purified oligosaccharides were elucidated by specific exoglycosidase digestion, Smith degradation, and methylation anaylsis.
2943741	5	89	theme	NeuNAc	1200:1205	arg1	beta					1188:1191	Gal beta 1----4GlcNAc beta 1----6	1166:1198	Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH	1166:1243	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	5	89	theme	NeuNAc	1200:1205	arg1	beta					1224:1227	NeuNAc alpha 2----3)Gal beta 1----3	1200:1234	NeuNAc alpha 2----3)Gal beta 1----3	1200:1234	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	6	90	link	O-linked	1541:1548	arg1	oligosaccharides					1550:1565	O-linked oligosaccharides	1541:1565	O-linked oligosaccharides which differ in core structures as well as in sialylation	1541:1623	These results clearly indicate that leukosialin can be differently glycosylated with O-linked chains, and each erythroid or myeloid (and T-lymphoid) cell line expresses a characteristic set of O-linked oligosaccharides which differ in core structures as well as in sialylation.
2943741	1	91	link	O-linked	149:156	arg1	oligosaccharides					158:173	O-linked oligosaccharides	149:173	O-linked oligosaccharides of leukosialin isolated from K562 erythroid, HL-60 promyelocytic, and HSB-2 T-lymphoid cell lines	149:271	Structures of O-linked oligosaccharides of leukosialin isolated from K562 erythroid, HL-60 promyelocytic, and HSB-2 T-lymphoid cell lines were examined.
2943741	5	92	theme	Gal	1166:1168	arg1	beta					1224:1227	NeuNAc alpha 2----3)Gal beta 1----3	1200:1234	NeuNAc alpha 2----3)Gal beta 1----3	1200:1234	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	5	92	theme	Gal	1166:1168	arg1	beta					1188:1191	Gal beta 1----4GlcNAc beta 1----6	1166:1198	Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH	1166:1243	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	5	93	theme	alpha	1050:1054	arg1	beta					1066:1069	NeuNAc alpha 2----3Gal beta 1----3GalNAcOH	1043:1084	NeuNAc alpha 2----3Gal beta 1----3GalNAcOH	1043:1084	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	6	94	theme	T-lymphoid	1485:1494	arg1	line					1502:1505	each erythroid or myeloid (and T-lymphoid) cell line	1454:1505	each erythroid or myeloid (and T-lymphoid) cell line	1454:1505	These results clearly indicate that leukosialin can be differently glycosylated with O-linked chains, and each erythroid or myeloid (and T-lymphoid) cell line expresses a characteristic set of O-linked oligosaccharides which differ in core structures as well as in sialylation.
2943741	5	95	theme	1----4GlcNAc	1175:1186	arg1	beta					1224:1227	NeuNAc alpha 2----3)Gal beta 1----3	1200:1234	NeuNAc alpha 2----3)Gal beta 1----3	1200:1234	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	5	95	theme	1----4GlcNAc	1175:1186	arg1	beta					1188:1191	Gal beta 1----4GlcNAc beta 1----6	1166:1198	Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH	1166:1243	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
2943741	4	96	theme	beta	852:855	arg1	1----3GalNAcOH					759:772	GalNAcOH, Gal beta 1----3GalNAcOH	740:772	GalNAcOH, Gal beta 1----3GalNAcOH	740:772	Oligosaccharides from K562 cells were found to be GalNAcOH, Gal beta 1----3GalNAcOH, NeuNAc alpha 2----6GalNAcOH, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH.
2943741	4	96	theme	beta	852:855	arg1	GalNAcOH					953:960	NeuNAc alpha 2----6GalNAcOH, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH	775:960	NeuNAc alpha 2----6GalNAcOH, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH	775:960	Oligosaccharides from K562 cells were found to be GalNAcOH, Gal beta 1----3GalNAcOH, NeuNAc alpha 2----6GalNAcOH, NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)GalNAcOH.
2943741	1	97	theme	T-lymphoid	251:260	arg1	lines					267:271	K562 erythroid, HL-60 promyelocytic, and HSB-2 T-lymphoid cell lines	204:271	K562 erythroid, HL-60 promyelocytic, and HSB-2 T-lymphoid cell lines	204:271	Structures of O-linked oligosaccharides of leukosialin isolated from K562 erythroid, HL-60 promyelocytic, and HSB-2 T-lymphoid cell lines were examined.
2943741	3	98	theme	purified	565:572	arg1	oligosaccharides					574:589	purified oligosaccharides	565:589	purified oligosaccharides	565:589	O-Linked oligosaccharides were released by alkaline borohydride treatment, and the structures of purified oligosaccharides were elucidated by specific exoglycosidase digestion, Smith degradation, and methylation anaylsis.
2943741	5	99	theme	GalNAcOH	1236:1243	arg1	GalNAcOH					1338:1345	NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH	1043:1345	NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH	1043:1345	On the other hand, oligosaccharides from HL-60 and HSB-2 cells were found to be NeuNAc alpha 2----3Gal beta 1----3GalNAcOH, NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(Gal beta 1----3)GalNAcOH, Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3)Gal beta 1----3)GalNAcOH, and NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6(NeuNAc alpha 2----3Gal beta 1----3)GalNAcOH.
9530955	2	0	with	preparation	380:390	arg1	weights					407:413	molecular weights	397:413	molecular weights ranging from about 0.9 to 1.3 x 10(6)	397:451	Sedimentation equilibrium analysis and gel filtration using polysaccharide or protein standards revealed a polydisperse preparation with molecular weights ranging from about 0.9 to 1.3 x 10(6).
9530955	6	1	theme	carbohydrate	1088:1099	arg1	content					1101:1107	the total carbohydrate content	1078:1107	the total carbohydrate content of these preparations	1078:1129	The buoyant densities of epitectin purified from urine and H.Ep.2 cells were found to be 1.39-1.40 g ml(-1), suggesting that the total carbohydrate content of these preparations is not significantly different.
9530955	6	1	theme	carbohydrate	1088:1099	arg1	different					1152:1160	different	1152:1160	different	1152:1160	The buoyant densities of epitectin purified from urine and H.Ep.2 cells were found to be 1.39-1.40 g ml(-1), suggesting that the total carbohydrate content of these preparations is not significantly different.
9530955	1	2	gly	glycoprotein	159:170	arg1	epitectin					173:181	epitectin	173:181	epitectin	173:181	The MUC1 glycoprotein, epitectin, a component of the human bladder epithelium, was purified from human urine.
9530955	1	2	gly	glycoprotein	159:170	arg1	glycoprotein					159:170	The MUC1 glycoprotein	150:170	The MUC1 glycoprotein	150:170	The MUC1 glycoprotein, epitectin, a component of the human bladder epithelium, was purified from human urine.
9530955	10	3	theme	different	1655:1663	arg1	proportions					1665:1675	different proportions	1655:1675	different proportions	1655:1675	The two sources of epitectin, in vitro labeled on sialic acid, were found to have the same sialyl oligosaccharides but in different proportions.
9530955	2	4	theme	Sedimentation	260:272	arg1	analysis					286:293	Sedimentation equilibrium analysis	260:293	Sedimentation equilibrium analysis	260:293	Sedimentation equilibrium analysis and gel filtration using polysaccharide or protein standards revealed a polydisperse preparation with molecular weights ranging from about 0.9 to 1.3 x 10(6).
9530955	1	5	theme	human	247:251	arg1	urine					253:257	human urine	247:257	human urine	247:257	The MUC1 glycoprotein, epitectin, a component of the human bladder epithelium, was purified from human urine.
9530955	12	6	theme	view	2063:2066	arg1	view					2040:2043	view	2040:2043	view of the prevailing view that MUC1 glycoproteins of cancer cells are underglycosylated compared to those produced by non-malignant cells	2040:2178	The remarkable similarities in the total carbohydrate content, the carbohydrate composition and structures of saccharides between epitectin from urine, a non-malignant source, and H.Ep.2 cells is surprising in view of the prevailing view that MUC1 glycoproteins of cancer cells are underglycosylated compared to those produced by non-malignant cells.
9530955	11	7	from	presence	1763:1770	arg1	epitectin					1799:1807	epitectin	1799:1807	epitectin	1799:1807	Metabolic labeling and N-glycanase susceptibility experiments firmly established the presence of N-linked saccharides in epitectin as minor components.
9530955	11	8	theme	N-linked	1775:1782	arg1	saccharides					1784:1794	N-linked saccharides	1775:1794	N-linked saccharides	1775:1794	Metabolic labeling and N-glycanase susceptibility experiments firmly established the presence of N-linked saccharides in epitectin as minor components.
9530955	2	9	theme	gel	299:301	arg1	filtration					303:312	gel filtration	299:312	gel filtration	299:312	Sedimentation equilibrium analysis and gel filtration using polysaccharide or protein standards revealed a polydisperse preparation with molecular weights ranging from about 0.9 to 1.3 x 10(6).
9530955	5	10	theme	H.Ep.2	891:896	arg1	epitectin					898:906	metabolically labeled H.Ep.2 epitectin	869:906	metabolically labeled H.Ep.2 epitectin	869:906	Chemical and enzymic deglycosylation of [125I]-labeled urine epitectin and metabolically labeled H.Ep.2 epitectin resulted in extremely polydisperse products.
9530955	3	11	theme	native	480:485	arg1	state					487:491	the native state	476:491	the native state	476:491	This suggests that in the native state epitectin exists as aggregates of three or four monomer units of 350-400 kDa.
9530955	5	12	theme	-labeled	840:847	arg1	epitectin					855:863	[125I]-labeled urine epitectin	834:863	[125I]-labeled urine epitectin	834:863	Chemical and enzymic deglycosylation of [125I]-labeled urine epitectin and metabolically labeled H.Ep.2 epitectin resulted in extremely polydisperse products.
9530955	12	13	theme	saccharides	1940:1950	arg1	cells					2017:2021	H.Ep.2 cells	2010:2021	H.Ep.2 cells	2010:2021	The remarkable similarities in the total carbohydrate content, the carbohydrate composition and structures of saccharides between epitectin from urine, a non-malignant source, and H.Ep.2 cells is surprising in view of the prevailing view that MUC1 glycoproteins of cancer cells are underglycosylated compared to those produced by non-malignant cells.
9530955	12	13	theme	saccharides	1940:1950	arg1	structures					1926:1935	structures	1926:1935	structures	1926:1935	The remarkable similarities in the total carbohydrate content, the carbohydrate composition and structures of saccharides between epitectin from urine, a non-malignant source, and H.Ep.2 cells is surprising in view of the prevailing view that MUC1 glycoproteins of cancer cells are underglycosylated compared to those produced by non-malignant cells.
9530955	12	13	theme	saccharides	1940:1950	arg1	content					1884:1890	the total carbohydrate content	1861:1890	the total carbohydrate content	1861:1890	The remarkable similarities in the total carbohydrate content, the carbohydrate composition and structures of saccharides between epitectin from urine, a non-malignant source, and H.Ep.2 cells is surprising in view of the prevailing view that MUC1 glycoproteins of cancer cells are underglycosylated compared to those produced by non-malignant cells.
9530955	12	13	theme	saccharides	1940:1950	arg1	source					1998:2003	a non-malignant source	1982:2003	a non-malignant source	1982:2003	The remarkable similarities in the total carbohydrate content, the carbohydrate composition and structures of saccharides between epitectin from urine, a non-malignant source, and H.Ep.2 cells is surprising in view of the prevailing view that MUC1 glycoproteins of cancer cells are underglycosylated compared to those produced by non-malignant cells.
9530955	12	13	theme	saccharides	1940:1950	arg1	composition					1910:1920	carbohydrate composition	1897:1920	carbohydrate composition	1897:1920	The remarkable similarities in the total carbohydrate content, the carbohydrate composition and structures of saccharides between epitectin from urine, a non-malignant source, and H.Ep.2 cells is surprising in view of the prevailing view that MUC1 glycoproteins of cancer cells are underglycosylated compared to those produced by non-malignant cells.
9530955	12	14	from	similarities	1845:1856	arg1	composition					1910:1920	carbohydrate composition	1897:1920	carbohydrate composition	1897:1920	The remarkable similarities in the total carbohydrate content, the carbohydrate composition and structures of saccharides between epitectin from urine, a non-malignant source, and H.Ep.2 cells is surprising in view of the prevailing view that MUC1 glycoproteins of cancer cells are underglycosylated compared to those produced by non-malignant cells.
9530955	12	14	from	similarities	1845:1856	arg1	content					1884:1890	the total carbohydrate content	1861:1890	the total carbohydrate content	1861:1890	The remarkable similarities in the total carbohydrate content, the carbohydrate composition and structures of saccharides between epitectin from urine, a non-malignant source, and H.Ep.2 cells is surprising in view of the prevailing view that MUC1 glycoproteins of cancer cells are underglycosylated compared to those produced by non-malignant cells.
9530955	12	14	from	similarities	1845:1856	arg1	cells					2017:2021	H.Ep.2 cells	2010:2021	H.Ep.2 cells	2010:2021	The remarkable similarities in the total carbohydrate content, the carbohydrate composition and structures of saccharides between epitectin from urine, a non-malignant source, and H.Ep.2 cells is surprising in view of the prevailing view that MUC1 glycoproteins of cancer cells are underglycosylated compared to those produced by non-malignant cells.
9530955	12	14	from	similarities	1845:1856	arg1	source					1998:2003	a non-malignant source	1982:2003	a non-malignant source	1982:2003	The remarkable similarities in the total carbohydrate content, the carbohydrate composition and structures of saccharides between epitectin from urine, a non-malignant source, and H.Ep.2 cells is surprising in view of the prevailing view that MUC1 glycoproteins of cancer cells are underglycosylated compared to those produced by non-malignant cells.
9530955	8	15	theme	-->	1425:1427	arg1	structures					1333:1342	three common structures	1320:1342	three common structures	1320:1342	The neutral saccharides from both sources contain three common structures, namely Gal1 --> 3GalNAc, GlcNAc1 --> 6 (Gal1 --> 3) GalNAc and Gal1 --> 4GlcNAc --> 6 (Gal1 --> 3)GalNAc.
9530955	8	15	theme	-->	1425:1427	arg1	GalNAc					1443:1448	Gal1 --> 4GlcNAc --> 6 (Gal1 --> 3)GalNAc	1408:1448	Gal1 --> 4GlcNAc --> 6 (Gal1 --> 3)GalNAc	1408:1448	The neutral saccharides from both sources contain three common structures, namely Gal1 --> 3GalNAc, GlcNAc1 --> 6 (Gal1 --> 3) GalNAc and Gal1 --> 4GlcNAc --> 6 (Gal1 --> 3)GalNAc.
9530955	12	16	theme	cells	2102:2106	arg1	glycoproteins					2078:2090	MUC1 glycoproteins	2073:2090	MUC1 glycoproteins of cancer cells	2073:2106	The remarkable similarities in the total carbohydrate content, the carbohydrate composition and structures of saccharides between epitectin from urine, a non-malignant source, and H.Ep.2 cells is surprising in view of the prevailing view that MUC1 glycoproteins of cancer cells are underglycosylated compared to those produced by non-malignant cells.
9530955	0	17	theme	major	118:122	arg1	alditols					140:147	the major oligosaccharide alditols	114:147	the major oligosaccharide alditols	114:147	Purification and characterization of the MUC1 mucin-type glycoprotein, epitectin, from human urine: structures of the major oligosaccharide alditols.
9530955	3	18	theme	kDa	566:568	arg1	units					549:553	three or four monomer units	527:553	three or four monomer units of 350-400 kDa	527:568	This suggests that in the native state epitectin exists as aggregates of three or four monomer units of 350-400 kDa.
9530955	5	19	theme	epitectin	855:863	arg1	deglycosylation					815:829	Chemical and enzymic deglycosylation	794:829	Chemical and enzymic deglycosylation of [125I]-labeled urine epitectin and metabolically labeled H.Ep.2 epitectin	794:906	Chemical and enzymic deglycosylation of [125I]-labeled urine epitectin and metabolically labeled H.Ep.2 epitectin resulted in extremely polydisperse products.
9530955	4	20	theme	hydrophobic	672:682	arg1	interactions					684:695	hydrophobic interactions	672:695	hydrophobic interactions	672:695	Epitectin was found to have significant affinity to hexyl-, octyl- or phenyl agarose indicating that hydrophobic interactions and possibly carbohydrate-carbohydrate interactions may be responsible for the self-association.
9530955	0	21	theme	alditols	140:147	arg1	structures					100:109	structures	100:109	Purification and characterization of the MUC1 mucin-type glycoprotein, epitectin, from human urine: structures of the major oligosaccharide alditols.	0:148	Purification and characterization of the MUC1 mucin-type glycoprotein, epitectin, from human urine: structures of the major oligosaccharide alditols.
9530955	12	22	gly	glycoproteins	2078:2090	arg1	glycoproteins					2078:2090	MUC1 glycoproteins	2073:2090	MUC1 glycoproteins of cancer cells	2073:2106	The remarkable similarities in the total carbohydrate content, the carbohydrate composition and structures of saccharides between epitectin from urine, a non-malignant source, and H.Ep.2 cells is surprising in view of the prevailing view that MUC1 glycoproteins of cancer cells are underglycosylated compared to those produced by non-malignant cells.
9530955	6	23	theme	buoyant	957:963	arg1	ml					1054:1055	1.39-1.40 g ml	1042:1055	1.39-1.40 g ml(-1)	1042:1059	The buoyant densities of epitectin purified from urine and H.Ep.2 cells were found to be 1.39-1.40 g ml(-1), suggesting that the total carbohydrate content of these preparations is not significantly different.
9530955	6	23	theme	buoyant	957:963	arg1	densities					965:973	The buoyant densities	953:973	The buoyant densities of epitectin purified from urine and H.Ep.2 cells	953:1023	The buoyant densities of epitectin purified from urine and H.Ep.2 cells were found to be 1.39-1.40 g ml(-1), suggesting that the total carbohydrate content of these preparations is not significantly different.
9530955	8	24	theme	-->	1437:1439	arg1	-->					1425:1427	Gal1 --> 4GlcNAc --> 6	1408:1429	Gal1 --> 4GlcNAc --> 6 (Gal1 --> 3)GalNAc	1408:1448	The neutral saccharides from both sources contain three common structures, namely Gal1 --> 3GalNAc, GlcNAc1 --> 6 (Gal1 --> 3) GalNAc and Gal1 --> 4GlcNAc --> 6 (Gal1 --> 3)GalNAc.
9530955	8	24	theme	-->	1437:1439	arg1	Gal1					1432:1435	Gal1 --> 3	1432:1441	Gal1 --> 3	1432:1441	The neutral saccharides from both sources contain three common structures, namely Gal1 --> 3GalNAc, GlcNAc1 --> 6 (Gal1 --> 3) GalNAc and Gal1 --> 4GlcNAc --> 6 (Gal1 --> 3)GalNAc.
9530955	8	25	theme	common	1326:1331	arg1	GalNAc					1397:1402	GlcNAc1 --> 6 (Gal1 --> 3) GalNAc	1370:1402	GlcNAc1 --> 6 (Gal1 --> 3) GalNAc	1370:1402	The neutral saccharides from both sources contain three common structures, namely Gal1 --> 3GalNAc, GlcNAc1 --> 6 (Gal1 --> 3) GalNAc and Gal1 --> 4GlcNAc --> 6 (Gal1 --> 3)GalNAc.
9530955	8	25	theme	common	1326:1331	arg1	3GalNAc					1361:1367	Gal1 --> 3GalNAc	1352:1367	Gal1 --> 3GalNAc	1352:1367	The neutral saccharides from both sources contain three common structures, namely Gal1 --> 3GalNAc, GlcNAc1 --> 6 (Gal1 --> 3) GalNAc and Gal1 --> 4GlcNAc --> 6 (Gal1 --> 3)GalNAc.
9530955	8	25	theme	common	1326:1331	arg1	structures					1333:1342	three common structures	1320:1342	three common structures	1320:1342	The neutral saccharides from both sources contain three common structures, namely Gal1 --> 3GalNAc, GlcNAc1 --> 6 (Gal1 --> 3) GalNAc and Gal1 --> 4GlcNAc --> 6 (Gal1 --> 3)GalNAc.
9530955	8	25	theme	common	1326:1331	arg1	GalNAc					1443:1448	Gal1 --> 4GlcNAc --> 6 (Gal1 --> 3)GalNAc	1408:1448	Gal1 --> 4GlcNAc --> 6 (Gal1 --> 3)GalNAc	1408:1448	The neutral saccharides from both sources contain three common structures, namely Gal1 --> 3GalNAc, GlcNAc1 --> 6 (Gal1 --> 3) GalNAc and Gal1 --> 4GlcNAc --> 6 (Gal1 --> 3)GalNAc.
9530955	11	26	theme	N-glycanase	1701:1711	arg1	susceptibility					1713:1726	N-glycanase susceptibility	1701:1726	N-glycanase susceptibility	1701:1726	Metabolic labeling and N-glycanase susceptibility experiments firmly established the presence of N-linked saccharides in epitectin as minor components.
9530955	12	27	theme	MUC1	2073:2076	arg1	glycoproteins					2078:2090	MUC1 glycoproteins	2073:2090	MUC1 glycoproteins of cancer cells	2073:2106	The remarkable similarities in the total carbohydrate content, the carbohydrate composition and structures of saccharides between epitectin from urine, a non-malignant source, and H.Ep.2 cells is surprising in view of the prevailing view that MUC1 glycoproteins of cancer cells are underglycosylated compared to those produced by non-malignant cells.
9530955	4	28	theme	phenyl	641:646	arg1	agarose					648:654	phenyl agarose	641:654	phenyl agarose indicating that hydrophobic interactions and possibly carbohydrate-carbohydrate interactions may be responsible for the self-association	641:791	Epitectin was found to have significant affinity to hexyl-, octyl- or phenyl agarose indicating that hydrophobic interactions and possibly carbohydrate-carbohydrate interactions may be responsible for the self-association.
9530955	11	29	theme	labeling	1688:1695	arg1	experiments					1728:1738	Metabolic labeling and N-glycanase susceptibility experiments	1678:1738	Metabolic labeling and N-glycanase susceptibility experiments	1678:1738	Metabolic labeling and N-glycanase susceptibility experiments firmly established the presence of N-linked saccharides in epitectin as minor components.
9530955	12	30	from	view	2040:2043	arg1	similarities					1845:1856	The remarkable similarities	1830:1856	The remarkable similarities in the total carbohydrate content, the carbohydrate composition and structures of saccharides between epitectin from urine, a non-malignant source, and H.Ep.2 cells	1830:2021	The remarkable similarities in the total carbohydrate content, the carbohydrate composition and structures of saccharides between epitectin from urine, a non-malignant source, and H.Ep.2 cells is surprising in view of the prevailing view that MUC1 glycoproteins of cancer cells are underglycosylated compared to those produced by non-malignant cells.
9530955	12	30	from	view	2040:2043	arg1	surprising					2026:2035	surprising	2026:2035	surprising	2026:2035	The remarkable similarities in the total carbohydrate content, the carbohydrate composition and structures of saccharides between epitectin from urine, a non-malignant source, and H.Ep.2 cells is surprising in view of the prevailing view that MUC1 glycoproteins of cancer cells are underglycosylated compared to those produced by non-malignant cells.
9530955	9	31	theme	urine	1470:1474	arg1	epitectin					1476:1484	urine epitectin	1470:1484	urine epitectin	1470:1484	The sialic acid of urine epitectin consisted entirely of N-acetylneuraminic acid.
9530955	8	32	theme	Gal1	1352:1355	arg1	3GalNAc					1361:1367	Gal1 --> 3GalNAc	1352:1367	Gal1 --> 3GalNAc	1352:1367	The neutral saccharides from both sources contain three common structures, namely Gal1 --> 3GalNAc, GlcNAc1 --> 6 (Gal1 --> 3) GalNAc and Gal1 --> 4GlcNAc --> 6 (Gal1 --> 3)GalNAc.
9530955	8	32	theme	Gal1	1352:1355	arg1	structures					1333:1342	three common structures	1320:1342	three common structures	1320:1342	The neutral saccharides from both sources contain three common structures, namely Gal1 --> 3GalNAc, GlcNAc1 --> 6 (Gal1 --> 3) GalNAc and Gal1 --> 4GlcNAc --> 6 (Gal1 --> 3)GalNAc.
9530955	12	33	theme	carbohydrate	1897:1908	arg1	composition					1910:1920	carbohydrate composition	1897:1920	carbohydrate composition	1897:1920	The remarkable similarities in the total carbohydrate content, the carbohydrate composition and structures of saccharides between epitectin from urine, a non-malignant source, and H.Ep.2 cells is surprising in view of the prevailing view that MUC1 glycoproteins of cancer cells are underglycosylated compared to those produced by non-malignant cells.
9530955	1	34	theme	MUC1	154:157	arg1	epitectin					173:181	epitectin	173:181	epitectin	173:181	The MUC1 glycoprotein, epitectin, a component of the human bladder epithelium, was purified from human urine.
9530955	1	34	theme	MUC1	154:157	arg1	glycoprotein					159:170	The MUC1 glycoprotein	150:170	The MUC1 glycoprotein	150:170	The MUC1 glycoprotein, epitectin, a component of the human bladder epithelium, was purified from human urine.
9530955	0	35	theme	human	87:91	arg1	urine					93:97	human urine	87:97	human urine	87:97	Purification and characterization of the MUC1 mucin-type glycoprotein, epitectin, from human urine: structures of the major oligosaccharide alditols.
9530955	6	36	theme	H.Ep.2	1012:1017	arg1	cells					1019:1023	H.Ep.2 cells	1012:1023	H.Ep.2 cells	1012:1023	The buoyant densities of epitectin purified from urine and H.Ep.2 cells were found to be 1.39-1.40 g ml(-1), suggesting that the total carbohydrate content of these preparations is not significantly different.
9530955	8	37	theme	GlcNAc1	1370:1376	arg1	-->					1378:1380	GlcNAc1 --> 6	1370:1382	GlcNAc1 --> 6 (Gal1 --> 3) GalNAc	1370:1402	The neutral saccharides from both sources contain three common structures, namely Gal1 --> 3GalNAc, GlcNAc1 --> 6 (Gal1 --> 3) GalNAc and Gal1 --> 4GlcNAc --> 6 (Gal1 --> 3)GalNAc.
9530955	8	37	theme	GlcNAc1	1370:1376	arg1	Gal1					1385:1388	Gal1 --> 3	1385:1394	Gal1 --> 3	1385:1394	The neutral saccharides from both sources contain three common structures, namely Gal1 --> 3GalNAc, GlcNAc1 --> 6 (Gal1 --> 3) GalNAc and Gal1 --> 4GlcNAc --> 6 (Gal1 --> 3)GalNAc.
9530955	12	38	theme	carbohydrate	1871:1882	arg1	content					1884:1890	the total carbohydrate content	1861:1890	the total carbohydrate content	1861:1890	The remarkable similarities in the total carbohydrate content, the carbohydrate composition and structures of saccharides between epitectin from urine, a non-malignant source, and H.Ep.2 cells is surprising in view of the prevailing view that MUC1 glycoproteins of cancer cells are underglycosylated compared to those produced by non-malignant cells.
9530955	4	39	theme	carbohydrate-carbohydrate	710:734	arg1	interactions					736:747	carbohydrate-carbohydrate interactions	710:747	carbohydrate-carbohydrate interactions	710:747	Epitectin was found to have significant affinity to hexyl-, octyl- or phenyl agarose indicating that hydrophobic interactions and possibly carbohydrate-carbohydrate interactions may be responsible for the self-association.
9530955	7	40	theme	epitectin	1191:1199	arg1	saccharides					1176:1186	The O-linked saccharides	1163:1186	The O-linked saccharides of epitectin	1163:1199	The O-linked saccharides of epitectin were fractionated by HPLC and analyzed by permethylation and FAB-MS.
9530955	10	41	theme	same	1619:1622	arg1	oligosaccharides					1631:1646	the same sialyl oligosaccharides	1615:1646	the same sialyl oligosaccharides	1615:1646	The two sources of epitectin, in vitro labeled on sialic acid, were found to have the same sialyl oligosaccharides but in different proportions.
9530955	5	42	gly	deglycosylation	815:829	arg1	epitectin					898:906	metabolically labeled H.Ep.2 epitectin	869:906	metabolically labeled H.Ep.2 epitectin	869:906	Chemical and enzymic deglycosylation of [125I]-labeled urine epitectin and metabolically labeled H.Ep.2 epitectin resulted in extremely polydisperse products.
9530955	5	42	gly	deglycosylation	815:829	arg1	epitectin					855:863	[125I]-labeled urine epitectin	834:863	[125I]-labeled urine epitectin	834:863	Chemical and enzymic deglycosylation of [125I]-labeled urine epitectin and metabolically labeled H.Ep.2 epitectin resulted in extremely polydisperse products.
9530955	12	43	from	urine	1975:1979	arg1	epitectin					1960:1968	epitectin	1960:1968	epitectin from urine	1960:1979	The remarkable similarities in the total carbohydrate content, the carbohydrate composition and structures of saccharides between epitectin from urine, a non-malignant source, and H.Ep.2 cells is surprising in view of the prevailing view that MUC1 glycoproteins of cancer cells are underglycosylated compared to those produced by non-malignant cells.
9530955	4	44	contain	have	594:597	arg1	Epitectin					571:579	Epitectin	571:579	Epitectin	571:579	Epitectin was found to have significant affinity to hexyl-, octyl- or phenyl agarose indicating that hydrophobic interactions and possibly carbohydrate-carbohydrate interactions may be responsible for the self-association.
9530955	4	44	contain	have	594:597	arg2	affinity					611:618	significant affinity	599:618	significant affinity to hexyl-, octyl- or phenyl agarose indicating that hydrophobic interactions and possibly carbohydrate-carbohydrate interactions may be responsible for the self-association	599:791	Epitectin was found to have significant affinity to hexyl-, octyl- or phenyl agarose indicating that hydrophobic interactions and possibly carbohydrate-carbohydrate interactions may be responsible for the self-association.
9530955	2	45	dep	0.9	434:436	arg1	6					450:450	6	450:450	6	450:450	Sedimentation equilibrium analysis and gel filtration using polysaccharide or protein standards revealed a polydisperse preparation with molecular weights ranging from about 0.9 to 1.3 x 10(6).
9530955	2	45	dep	0.9	434:436	arg1	to					438:439	to	438:439	to	438:439	Sedimentation equilibrium analysis and gel filtration using polysaccharide or protein standards revealed a polydisperse preparation with molecular weights ranging from about 0.9 to 1.3 x 10(6).
9530955	2	45	dep	0.9	434:436	arg1	10					447:448	10	447:448	10	447:448	Sedimentation equilibrium analysis and gel filtration using polysaccharide or protein standards revealed a polydisperse preparation with molecular weights ranging from about 0.9 to 1.3 x 10(6).
9530955	2	45	dep	0.9	434:436	arg1	1.3					441:443	1.3	441:443	1.3	441:443	Sedimentation equilibrium analysis and gel filtration using polysaccharide or protein standards revealed a polydisperse preparation with molecular weights ranging from about 0.9 to 1.3 x 10(6).
9530955	2	46	theme	protein	338:344	arg1	standards					346:354	polysaccharide or protein standards	320:354	standards	346:354	Sedimentation equilibrium analysis and gel filtration using polysaccharide or protein standards revealed a polydisperse preparation with molecular weights ranging from about 0.9 to 1.3 x 10(6).
9530955	0	47	theme	mucin-type	46:55	arg1	epitectin					71:79	epitectin	71:79	epitectin	71:79	Purification and characterization of the MUC1 mucin-type glycoprotein, epitectin, from human urine: structures of the major oligosaccharide alditols.
9530955	0	47	theme	mucin-type	46:55	arg1	glycoprotein					57:68	the MUC1 mucin-type glycoprotein	37:68	the MUC1 mucin-type glycoprotein	37:68	Purification and characterization of the MUC1 mucin-type glycoprotein, epitectin, from human urine: structures of the major oligosaccharide alditols.
9530955	11	48	theme	Metabolic	1678:1686	arg1	labeling					1688:1695	Metabolic labeling	1678:1695	Metabolic labeling	1678:1695	Metabolic labeling and N-glycanase susceptibility experiments firmly established the presence of N-linked saccharides in epitectin as minor components.
9530955	8	49	theme	Gal1	1408:1411	arg1	-->					1425:1427	Gal1 --> 4GlcNAc --> 6	1408:1429	Gal1 --> 4GlcNAc --> 6 (Gal1 --> 3)GalNAc	1408:1448	The neutral saccharides from both sources contain three common structures, namely Gal1 --> 3GalNAc, GlcNAc1 --> 6 (Gal1 --> 3) GalNAc and Gal1 --> 4GlcNAc --> 6 (Gal1 --> 3)GalNAc.
9530955	8	49	theme	Gal1	1408:1411	arg1	Gal1					1432:1435	Gal1 --> 3	1432:1441	Gal1 --> 3	1432:1441	The neutral saccharides from both sources contain three common structures, namely Gal1 --> 3GalNAc, GlcNAc1 --> 6 (Gal1 --> 3) GalNAc and Gal1 --> 4GlcNAc --> 6 (Gal1 --> 3)GalNAc.
9530955	2	50	theme	polysaccharide	320:333	arg1	standards					346:354	polysaccharide or protein standards	320:354	standards	346:354	Sedimentation equilibrium analysis and gel filtration using polysaccharide or protein standards revealed a polydisperse preparation with molecular weights ranging from about 0.9 to 1.3 x 10(6).
9530955	1	51	theme	human	203:207	arg1	epithelium					217:226	the human bladder epithelium	199:226	the human bladder epithelium	199:226	The MUC1 glycoprotein, epitectin, a component of the human bladder epithelium, was purified from human urine.
9530955	8	52	theme	4GlcNAc	1417:1423	arg1	-->					1425:1427	Gal1 --> 4GlcNAc --> 6	1408:1429	Gal1 --> 4GlcNAc --> 6 (Gal1 --> 3)GalNAc	1408:1448	The neutral saccharides from both sources contain three common structures, namely Gal1 --> 3GalNAc, GlcNAc1 --> 6 (Gal1 --> 3) GalNAc and Gal1 --> 4GlcNAc --> 6 (Gal1 --> 3)GalNAc.
9530955	8	52	theme	4GlcNAc	1417:1423	arg1	Gal1					1432:1435	Gal1 --> 3	1432:1441	Gal1 --> 3	1432:1441	The neutral saccharides from both sources contain three common structures, namely Gal1 --> 3GalNAc, GlcNAc1 --> 6 (Gal1 --> 3) GalNAc and Gal1 --> 4GlcNAc --> 6 (Gal1 --> 3)GalNAc.
9530955	2	53	theme	polydisperse	367:378	arg1	preparation					380:390	a polydisperse preparation	365:390	a polydisperse preparation with molecular weights ranging from about 0.9 to 1.3 x 10(6)	365:451	Sedimentation equilibrium analysis and gel filtration using polysaccharide or protein standards revealed a polydisperse preparation with molecular weights ranging from about 0.9 to 1.3 x 10(6).
9530955	1	54	theme	epithelium	217:226	arg1	epitectin					173:181	epitectin	173:181	epitectin	173:181	The MUC1 glycoprotein, epitectin, a component of the human bladder epithelium, was purified from human urine.
9530955	1	54	theme	epithelium	217:226	arg1	component					186:194	a component	184:194	a component of the human bladder epithelium	184:226	The MUC1 glycoprotein, epitectin, a component of the human bladder epithelium, was purified from human urine.
9530955	5	55	theme	Chemical	794:801	arg1	deglycosylation					815:829	Chemical and enzymic deglycosylation	794:829	Chemical and enzymic deglycosylation of [125I]-labeled urine epitectin and metabolically labeled H.Ep.2 epitectin	794:906	Chemical and enzymic deglycosylation of [125I]-labeled urine epitectin and metabolically labeled H.Ep.2 epitectin resulted in extremely polydisperse products.
9530955	12	56	from	surprising	2026:2035	arg1	view					2040:2043	view	2040:2043	view of the prevailing view that MUC1 glycoproteins of cancer cells are underglycosylated compared to those produced by non-malignant cells	2040:2178	The remarkable similarities in the total carbohydrate content, the carbohydrate composition and structures of saccharides between epitectin from urine, a non-malignant source, and H.Ep.2 cells is surprising in view of the prevailing view that MUC1 glycoproteins of cancer cells are underglycosylated compared to those produced by non-malignant cells.
9530955	0	57	gly	glycoprotein	57:68	arg1	epitectin					71:79	epitectin	71:79	epitectin	71:79	Purification and characterization of the MUC1 mucin-type glycoprotein, epitectin, from human urine: structures of the major oligosaccharide alditols.
9530955	0	57	gly	glycoprotein	57:68	arg1	glycoprotein					57:68	the MUC1 mucin-type glycoprotein	37:68	the MUC1 mucin-type glycoprotein	37:68	Purification and characterization of the MUC1 mucin-type glycoprotein, epitectin, from human urine: structures of the major oligosaccharide alditols.
9530955	6	58	theme	total	1082:1086	arg1	content					1101:1107	the total carbohydrate content	1078:1107	the total carbohydrate content of these preparations	1078:1129	The buoyant densities of epitectin purified from urine and H.Ep.2 cells were found to be 1.39-1.40 g ml(-1), suggesting that the total carbohydrate content of these preparations is not significantly different.
9530955	6	58	theme	total	1082:1086	arg1	different					1152:1160	different	1152:1160	different	1152:1160	The buoyant densities of epitectin purified from urine and H.Ep.2 cells were found to be 1.39-1.40 g ml(-1), suggesting that the total carbohydrate content of these preparations is not significantly different.
9530955	2	59	theme	equilibrium	274:284	arg1	analysis					286:293	Sedimentation equilibrium analysis	260:293	Sedimentation equilibrium analysis	260:293	Sedimentation equilibrium analysis and gel filtration using polysaccharide or protein standards revealed a polydisperse preparation with molecular weights ranging from about 0.9 to 1.3 x 10(6).
9530955	12	60	theme	non-malignant	1984:1996	arg1	source					1998:2003	a non-malignant source	1982:2003	a non-malignant source	1982:2003	The remarkable similarities in the total carbohydrate content, the carbohydrate composition and structures of saccharides between epitectin from urine, a non-malignant source, and H.Ep.2 cells is surprising in view of the prevailing view that MUC1 glycoproteins of cancer cells are underglycosylated compared to those produced by non-malignant cells.
9530955	10	61	contain	have	1610:1613	arg2	oligosaccharides					1631:1646	the same sialyl oligosaccharides	1615:1646	the same sialyl oligosaccharides	1615:1646	The two sources of epitectin, in vitro labeled on sialic acid, were found to have the same sialyl oligosaccharides but in different proportions.
9530955	10	61	contain	have	1610:1613	arg1	sources					1541:1547	The two sources	1533:1547	The two sources	1533:1547	The two sources of epitectin, in vitro labeled on sialic acid, were found to have the same sialyl oligosaccharides but in different proportions.
9530955	5	62	theme	labeled	883:889	arg1	epitectin					898:906	metabolically labeled H.Ep.2 epitectin	869:906	metabolically labeled H.Ep.2 epitectin	869:906	Chemical and enzymic deglycosylation of [125I]-labeled urine epitectin and metabolically labeled H.Ep.2 epitectin resulted in extremely polydisperse products.
9530955	10	63	theme	epitectin	1552:1560	arg1	sources					1541:1547	The two sources	1533:1547	The two sources	1533:1547	The two sources of epitectin, in vitro labeled on sialic acid, were found to have the same sialyl oligosaccharides but in different proportions.
9530955	11	64	theme	saccharides	1784:1794	arg1	presence					1763:1770	the presence	1759:1770	the presence of N-linked saccharides in epitectin	1759:1807	Metabolic labeling and N-glycanase susceptibility experiments firmly established the presence of N-linked saccharides in epitectin as minor components.
9530955	11	64	theme	saccharides	1784:1794	arg1	components					1818:1827	minor components	1812:1827	minor components	1812:1827	Metabolic labeling and N-glycanase susceptibility experiments firmly established the presence of N-linked saccharides in epitectin as minor components.
9530955	3	65	theme	monomer	541:547	arg1	units					549:553	three or four monomer units	527:553	three or four monomer units of 350-400 kDa	527:568	This suggests that in the native state epitectin exists as aggregates of three or four monomer units of 350-400 kDa.
9530955	8	66	theme	neutral	1274:1280	arg1	saccharides					1282:1292	The neutral saccharides	1270:1292	The neutral saccharides from both sources	1270:1310	The neutral saccharides from both sources contain three common structures, namely Gal1 --> 3GalNAc, GlcNAc1 --> 6 (Gal1 --> 3) GalNAc and Gal1 --> 4GlcNAc --> 6 (Gal1 --> 3)GalNAc.
9530955	10	67	theme	sialic	1583:1588	arg1	acid					1590:1593	sialic acid	1583:1593	sialic acid	1583:1593	The two sources of epitectin, in vitro labeled on sialic acid, were found to have the same sialyl oligosaccharides but in different proportions.
9530955	0	68	theme	oligosaccharide	124:138	arg1	alditols					140:147	the major oligosaccharide alditols	114:147	the major oligosaccharide alditols	114:147	Purification and characterization of the MUC1 mucin-type glycoprotein, epitectin, from human urine: structures of the major oligosaccharide alditols.
9530955	12	69	gly	underglycosylated	2112:2128	arg1	glycoproteins					2078:2090	MUC1 glycoproteins	2073:2090	MUC1 glycoproteins of cancer cells	2073:2106	The remarkable similarities in the total carbohydrate content, the carbohydrate composition and structures of saccharides between epitectin from urine, a non-malignant source, and H.Ep.2 cells is surprising in view of the prevailing view that MUC1 glycoproteins of cancer cells are underglycosylated compared to those produced by non-malignant cells.
9530955	5	70	theme	urine	849:853	arg1	epitectin					855:863	[125I]-labeled urine epitectin	834:863	[125I]-labeled urine epitectin	834:863	Chemical and enzymic deglycosylation of [125I]-labeled urine epitectin and metabolically labeled H.Ep.2 epitectin resulted in extremely polydisperse products.
9530955	6	71	theme	epitectin	978:986	arg1	ml					1054:1055	1.39-1.40 g ml	1042:1055	1.39-1.40 g ml(-1)	1042:1059	The buoyant densities of epitectin purified from urine and H.Ep.2 cells were found to be 1.39-1.40 g ml(-1), suggesting that the total carbohydrate content of these preparations is not significantly different.
9530955	6	71	theme	epitectin	978:986	arg1	densities					965:973	The buoyant densities	953:973	The buoyant densities of epitectin purified from urine and H.Ep.2 cells	953:1023	The buoyant densities of epitectin purified from urine and H.Ep.2 cells were found to be 1.39-1.40 g ml(-1), suggesting that the total carbohydrate content of these preparations is not significantly different.
9530955	4	72	theme	significant	599:609	arg1	affinity					611:618	significant affinity	599:618	significant affinity to hexyl-, octyl- or phenyl agarose indicating that hydrophobic interactions and possibly carbohydrate-carbohydrate interactions may be responsible for the self-association	599:791	Epitectin was found to have significant affinity to hexyl-, octyl- or phenyl agarose indicating that hydrophobic interactions and possibly carbohydrate-carbohydrate interactions may be responsible for the self-association.
9530955	12	73	dep	composition	1910:1920	arg1	the					1893:1895	the	1893:1895	the	1893:1895	The remarkable similarities in the total carbohydrate content, the carbohydrate composition and structures of saccharides between epitectin from urine, a non-malignant source, and H.Ep.2 cells is surprising in view of the prevailing view that MUC1 glycoproteins of cancer cells are underglycosylated compared to those produced by non-malignant cells.
9530955	11	74	theme	minor	1812:1816	arg1	components					1818:1827	minor components	1812:1827	minor components	1812:1827	Metabolic labeling and N-glycanase susceptibility experiments firmly established the presence of N-linked saccharides in epitectin as minor components.
9530955	11	74	theme	minor	1812:1816	arg1	presence					1763:1770	the presence	1759:1770	the presence of N-linked saccharides in epitectin	1759:1807	Metabolic labeling and N-glycanase susceptibility experiments firmly established the presence of N-linked saccharides in epitectin as minor components.
9530955	3	75	theme	units	549:553	arg1	aggregates					513:522	aggregates	513:522	aggregates of three or four monomer units of 350-400 kDa	513:568	This suggests that in the native state epitectin exists as aggregates of three or four monomer units of 350-400 kDa.
9530955	5	76	theme	polydisperse	930:941	arg1	products					943:950	extremely polydisperse products	920:950	extremely polydisperse products	920:950	Chemical and enzymic deglycosylation of [125I]-labeled urine epitectin and metabolically labeled H.Ep.2 epitectin resulted in extremely polydisperse products.
9530955	12	77	theme	prevailing	2052:2061	arg1	view					2063:2066	the prevailing view that MUC1 glycoproteins of cancer cells are underglycosylated compared to those produced by non-malignant cells	2048:2178	the prevailing view that MUC1 glycoproteins of cancer cells are underglycosylated compared to those produced by non-malignant cells	2048:2178	The remarkable similarities in the total carbohydrate content, the carbohydrate composition and structures of saccharides between epitectin from urine, a non-malignant source, and H.Ep.2 cells is surprising in view of the prevailing view that MUC1 glycoproteins of cancer cells are underglycosylated compared to those produced by non-malignant cells.
9530955	7	78	link	O-linked	1167:1174	arg1	saccharides					1176:1186	The O-linked saccharides	1163:1186	The O-linked saccharides of epitectin	1163:1199	The O-linked saccharides of epitectin were fractionated by HPLC and analyzed by permethylation and FAB-MS.
9530955	9	79	theme	sialic	1455:1460	arg1	acid					1462:1465	The sialic acid	1451:1465	The sialic acid of urine epitectin	1451:1484	The sialic acid of urine epitectin consisted entirely of N-acetylneuraminic acid.
9530955	6	80	theme	g	1052:1052	arg1	-1					1057:1058	-1	1057:1058	-1	1057:1058	The buoyant densities of epitectin purified from urine and H.Ep.2 cells were found to be 1.39-1.40 g ml(-1), suggesting that the total carbohydrate content of these preparations is not significantly different.
9530955	6	80	theme	g	1052:1052	arg1	ml					1054:1055	1.39-1.40 g ml	1042:1055	1.39-1.40 g ml(-1)	1042:1059	The buoyant densities of epitectin purified from urine and H.Ep.2 cells were found to be 1.39-1.40 g ml(-1), suggesting that the total carbohydrate content of these preparations is not significantly different.
9530955	6	80	theme	g	1052:1052	arg1	densities					965:973	The buoyant densities	953:973	The buoyant densities of epitectin purified from urine and H.Ep.2 cells	953:1023	The buoyant densities of epitectin purified from urine and H.Ep.2 cells were found to be 1.39-1.40 g ml(-1), suggesting that the total carbohydrate content of these preparations is not significantly different.
9530955	8	81	contain	contain	1312:1318	arg2	GalNAc					1443:1448	Gal1 --> 4GlcNAc --> 6 (Gal1 --> 3)GalNAc	1408:1448	Gal1 --> 4GlcNAc --> 6 (Gal1 --> 3)GalNAc	1408:1448	The neutral saccharides from both sources contain three common structures, namely Gal1 --> 3GalNAc, GlcNAc1 --> 6 (Gal1 --> 3) GalNAc and Gal1 --> 4GlcNAc --> 6 (Gal1 --> 3)GalNAc.
9530955	8	81	contain	contain	1312:1318	arg1	saccharides					1282:1292	The neutral saccharides	1270:1292	The neutral saccharides from both sources	1270:1310	The neutral saccharides from both sources contain three common structures, namely Gal1 --> 3GalNAc, GlcNAc1 --> 6 (Gal1 --> 3) GalNAc and Gal1 --> 4GlcNAc --> 6 (Gal1 --> 3)GalNAc.
9530955	8	81	contain	contain	1312:1318	arg2	GalNAc					1397:1402	GlcNAc1 --> 6 (Gal1 --> 3) GalNAc	1370:1402	GlcNAc1 --> 6 (Gal1 --> 3) GalNAc	1370:1402	The neutral saccharides from both sources contain three common structures, namely Gal1 --> 3GalNAc, GlcNAc1 --> 6 (Gal1 --> 3) GalNAc and Gal1 --> 4GlcNAc --> 6 (Gal1 --> 3)GalNAc.
9530955	8	81	contain	contain	1312:1318	arg2	structures					1333:1342	three common structures	1320:1342	three common structures	1320:1342	The neutral saccharides from both sources contain three common structures, namely Gal1 --> 3GalNAc, GlcNAc1 --> 6 (Gal1 --> 3) GalNAc and Gal1 --> 4GlcNAc --> 6 (Gal1 --> 3)GalNAc.
9530955	8	81	contain	contain	1312:1318	arg2	3GalNAc					1361:1367	Gal1 --> 3GalNAc	1352:1367	Gal1 --> 3GalNAc	1352:1367	The neutral saccharides from both sources contain three common structures, namely Gal1 --> 3GalNAc, GlcNAc1 --> 6 (Gal1 --> 3) GalNAc and Gal1 --> 4GlcNAc --> 6 (Gal1 --> 3)GalNAc.
9530955	0	82	from	urine	93:97	arg1	characterization					17:32	characterization	17:32	characterization	17:32	Purification and characterization of the MUC1 mucin-type glycoprotein, epitectin, from human urine: structures of the major oligosaccharide alditols.
9530955	0	82	from	urine	93:97	arg1	Purification					0:11	Purification	0:11	Purification	0:11	Purification and characterization of the MUC1 mucin-type glycoprotein, epitectin, from human urine: structures of the major oligosaccharide alditols.
9530955	11	83	theme	susceptibility	1713:1726	arg1	experiments					1728:1738	Metabolic labeling and N-glycanase susceptibility experiments	1678:1738	Metabolic labeling and N-glycanase susceptibility experiments	1678:1738	Metabolic labeling and N-glycanase susceptibility experiments firmly established the presence of N-linked saccharides in epitectin as minor components.
9530955	5	84	theme	epitectin	898:906	arg1	deglycosylation					815:829	Chemical and enzymic deglycosylation	794:829	Chemical and enzymic deglycosylation of [125I]-labeled urine epitectin and metabolically labeled H.Ep.2 epitectin	794:906	Chemical and enzymic deglycosylation of [125I]-labeled urine epitectin and metabolically labeled H.Ep.2 epitectin resulted in extremely polydisperse products.
9530955	11	85	link	N-linked	1775:1782	arg1	saccharides					1784:1794	N-linked saccharides	1775:1794	N-linked saccharides	1775:1794	Metabolic labeling and N-glycanase susceptibility experiments firmly established the presence of N-linked saccharides in epitectin as minor components.
9530955	9	86	theme	epitectin	1476:1484	arg1	acid					1462:1465	The sialic acid	1451:1465	The sialic acid of urine epitectin	1451:1484	The sialic acid of urine epitectin consisted entirely of N-acetylneuraminic acid.
9530955	8	87	theme	-->	1357:1359	arg1	3GalNAc					1361:1367	Gal1 --> 3GalNAc	1352:1367	Gal1 --> 3GalNAc	1352:1367	The neutral saccharides from both sources contain three common structures, namely Gal1 --> 3GalNAc, GlcNAc1 --> 6 (Gal1 --> 3) GalNAc and Gal1 --> 4GlcNAc --> 6 (Gal1 --> 3)GalNAc.
9530955	8	87	theme	-->	1357:1359	arg1	structures					1333:1342	three common structures	1320:1342	three common structures	1320:1342	The neutral saccharides from both sources contain three common structures, namely Gal1 --> 3GalNAc, GlcNAc1 --> 6 (Gal1 --> 3) GalNAc and Gal1 --> 4GlcNAc --> 6 (Gal1 --> 3)GalNAc.
9530955	8	88	from	sources	1304:1310	arg1	saccharides					1282:1292	The neutral saccharides	1270:1292	The neutral saccharides from both sources	1270:1310	The neutral saccharides from both sources contain three common structures, namely Gal1 --> 3GalNAc, GlcNAc1 --> 6 (Gal1 --> 3) GalNAc and Gal1 --> 4GlcNAc --> 6 (Gal1 --> 3)GalNAc.
9530955	9	89	theme	N-acetylneuraminic	1508:1525	arg1	acid					1527:1530	N-acetylneuraminic acid	1508:1530	N-acetylneuraminic acid	1508:1530	The sialic acid of urine epitectin consisted entirely of N-acetylneuraminic acid.
9530955	2	90	theme	molecular	397:405	arg1	weights					407:413	molecular weights	397:413	molecular weights ranging from about 0.9 to 1.3 x 10(6)	397:451	Sedimentation equilibrium analysis and gel filtration using polysaccharide or protein standards revealed a polydisperse preparation with molecular weights ranging from about 0.9 to 1.3 x 10(6).
9530955	5	91	theme	enzymic	807:813	arg1	deglycosylation					815:829	Chemical and enzymic deglycosylation	794:829	Chemical and enzymic deglycosylation of [125I]-labeled urine epitectin and metabolically labeled H.Ep.2 epitectin	794:906	Chemical and enzymic deglycosylation of [125I]-labeled urine epitectin and metabolically labeled H.Ep.2 epitectin resulted in extremely polydisperse products.
9530955	8	92	theme	-->	1378:1380	arg1	GalNAc					1397:1402	GlcNAc1 --> 6 (Gal1 --> 3) GalNAc	1370:1402	GlcNAc1 --> 6 (Gal1 --> 3) GalNAc	1370:1402	The neutral saccharides from both sources contain three common structures, namely Gal1 --> 3GalNAc, GlcNAc1 --> 6 (Gal1 --> 3) GalNAc and Gal1 --> 4GlcNAc --> 6 (Gal1 --> 3)GalNAc.
9530955	8	92	theme	-->	1378:1380	arg1	structures					1333:1342	three common structures	1320:1342	three common structures	1320:1342	The neutral saccharides from both sources contain three common structures, namely Gal1 --> 3GalNAc, GlcNAc1 --> 6 (Gal1 --> 3) GalNAc and Gal1 --> 4GlcNAc --> 6 (Gal1 --> 3)GalNAc.
9530955	7	93	theme	O-linked	1167:1174	arg1	saccharides					1176:1186	The O-linked saccharides	1163:1186	The O-linked saccharides of epitectin	1163:1199	The O-linked saccharides of epitectin were fractionated by HPLC and analyzed by permethylation and FAB-MS.
9530955	12	94	theme	non-malignant	2160:2172	arg1	cells					2174:2178	non-malignant cells	2160:2178	non-malignant cells	2160:2178	The remarkable similarities in the total carbohydrate content, the carbohydrate composition and structures of saccharides between epitectin from urine, a non-malignant source, and H.Ep.2 cells is surprising in view of the prevailing view that MUC1 glycoproteins of cancer cells are underglycosylated compared to those produced by non-malignant cells.
9530955	11	95	attach	presence	1763:1770	arg1	epitectin					1799:1807	epitectin	1799:1807	epitectin	1799:1807	Metabolic labeling and N-glycanase susceptibility experiments firmly established the presence of N-linked saccharides in epitectin as minor components.
9530955	11	95	attach	presence	1763:1770	arg2	saccharides					1784:1794	N-linked saccharides	1775:1794	N-linked saccharides	1775:1794	Metabolic labeling and N-glycanase susceptibility experiments firmly established the presence of N-linked saccharides in epitectin as minor components.
9530955	0	96	theme	MUC1	41:44	arg1	epitectin					71:79	epitectin	71:79	epitectin	71:79	Purification and characterization of the MUC1 mucin-type glycoprotein, epitectin, from human urine: structures of the major oligosaccharide alditols.
9530955	0	96	theme	MUC1	41:44	arg1	glycoprotein					57:68	the MUC1 mucin-type glycoprotein	37:68	the MUC1 mucin-type glycoprotein	37:68	Purification and characterization of the MUC1 mucin-type glycoprotein, epitectin, from human urine: structures of the major oligosaccharide alditols.
9530955	12	97	theme	total	1865:1869	arg1	content					1884:1890	the total carbohydrate content	1861:1890	the total carbohydrate content	1861:1890	The remarkable similarities in the total carbohydrate content, the carbohydrate composition and structures of saccharides between epitectin from urine, a non-malignant source, and H.Ep.2 cells is surprising in view of the prevailing view that MUC1 glycoproteins of cancer cells are underglycosylated compared to those produced by non-malignant cells.
9530955	8	98	theme	-->	1390:1392	arg1	-->					1378:1380	GlcNAc1 --> 6	1370:1382	GlcNAc1 --> 6 (Gal1 --> 3) GalNAc	1370:1402	The neutral saccharides from both sources contain three common structures, namely Gal1 --> 3GalNAc, GlcNAc1 --> 6 (Gal1 --> 3) GalNAc and Gal1 --> 4GlcNAc --> 6 (Gal1 --> 3)GalNAc.
9530955	8	98	theme	-->	1390:1392	arg1	Gal1					1385:1388	Gal1 --> 3	1385:1394	Gal1 --> 3	1385:1394	The neutral saccharides from both sources contain three common structures, namely Gal1 --> 3GalNAc, GlcNAc1 --> 6 (Gal1 --> 3) GalNAc and Gal1 --> 4GlcNAc --> 6 (Gal1 --> 3)GalNAc.
9530955	0	99	theme	glycoprotein	57:68	arg1	characterization					17:32	characterization	17:32	characterization	17:32	Purification and characterization of the MUC1 mucin-type glycoprotein, epitectin, from human urine: structures of the major oligosaccharide alditols.
9530955	0	99	theme	glycoprotein	57:68	arg1	Purification					0:11	Purification	0:11	Purification	0:11	Purification and characterization of the MUC1 mucin-type glycoprotein, epitectin, from human urine: structures of the major oligosaccharide alditols.
9530955	12	100	theme	H.Ep.2	2010:2015	arg1	cells					2017:2021	H.Ep.2 cells	2010:2021	H.Ep.2 cells	2010:2021	The remarkable similarities in the total carbohydrate content, the carbohydrate composition and structures of saccharides between epitectin from urine, a non-malignant source, and H.Ep.2 cells is surprising in view of the prevailing view that MUC1 glycoproteins of cancer cells are underglycosylated compared to those produced by non-malignant cells.
9530955	0	101	dep	Purification	0:11	arg1	structures					100:109	structures	100:109	Purification and characterization of the MUC1 mucin-type glycoprotein, epitectin, from human urine: structures of the major oligosaccharide alditols.	0:148	Purification and characterization of the MUC1 mucin-type glycoprotein, epitectin, from human urine: structures of the major oligosaccharide alditols.
9530955	12	102	theme	remarkable	1834:1843	arg1	similarities					1845:1856	The remarkable similarities	1830:1856	The remarkable similarities in the total carbohydrate content, the carbohydrate composition and structures of saccharides between epitectin from urine, a non-malignant source, and H.Ep.2 cells	1830:2021	The remarkable similarities in the total carbohydrate content, the carbohydrate composition and structures of saccharides between epitectin from urine, a non-malignant source, and H.Ep.2 cells is surprising in view of the prevailing view that MUC1 glycoproteins of cancer cells are underglycosylated compared to those produced by non-malignant cells.
9530955	12	102	theme	remarkable	1834:1843	arg1	surprising					2026:2035	surprising	2026:2035	surprising	2026:2035	The remarkable similarities in the total carbohydrate content, the carbohydrate composition and structures of saccharides between epitectin from urine, a non-malignant source, and H.Ep.2 cells is surprising in view of the prevailing view that MUC1 glycoproteins of cancer cells are underglycosylated compared to those produced by non-malignant cells.
9530955	6	103	theme	preparations	1118:1129	arg1	content					1101:1107	the total carbohydrate content	1078:1107	the total carbohydrate content of these preparations	1078:1129	The buoyant densities of epitectin purified from urine and H.Ep.2 cells were found to be 1.39-1.40 g ml(-1), suggesting that the total carbohydrate content of these preparations is not significantly different.
9530955	6	103	theme	preparations	1118:1129	arg1	different					1152:1160	different	1152:1160	different	1152:1160	The buoyant densities of epitectin purified from urine and H.Ep.2 cells were found to be 1.39-1.40 g ml(-1), suggesting that the total carbohydrate content of these preparations is not significantly different.
9530955	10	104	theme	sialyl	1624:1629	arg1	oligosaccharides					1631:1646	the same sialyl oligosaccharides	1615:1646	the same sialyl oligosaccharides	1615:1646	The two sources of epitectin, in vitro labeled on sialic acid, were found to have the same sialyl oligosaccharides but in different proportions.
9530955	1	105	theme	bladder	209:215	arg1	epithelium					217:226	the human bladder epithelium	199:226	the human bladder epithelium	199:226	The MUC1 glycoprotein, epitectin, a component of the human bladder epithelium, was purified from human urine.
9530955	12	106	theme	cancer	2095:2100	arg1	cells					2102:2106	cancer cells	2095:2106	cancer cells	2095:2106	The remarkable similarities in the total carbohydrate content, the carbohydrate composition and structures of saccharides between epitectin from urine, a non-malignant source, and H.Ep.2 cells is surprising in view of the prevailing view that MUC1 glycoproteins of cancer cells are underglycosylated compared to those produced by non-malignant cells.
9530955	8	107	theme	-->	1413:1415	arg1	-->					1425:1427	Gal1 --> 4GlcNAc --> 6	1408:1429	Gal1 --> 4GlcNAc --> 6 (Gal1 --> 3)GalNAc	1408:1448	The neutral saccharides from both sources contain three common structures, namely Gal1 --> 3GalNAc, GlcNAc1 --> 6 (Gal1 --> 3) GalNAc and Gal1 --> 4GlcNAc --> 6 (Gal1 --> 3)GalNAc.
9530955	8	107	theme	-->	1413:1415	arg1	Gal1					1432:1435	Gal1 --> 3	1432:1441	Gal1 --> 3	1432:1441	The neutral saccharides from both sources contain three common structures, namely Gal1 --> 3GalNAc, GlcNAc1 --> 6 (Gal1 --> 3) GalNAc and Gal1 --> 4GlcNAc --> 6 (Gal1 --> 3)GalNAc.
8969192	6	0	theme	disialo	1217:1223	arg1	species					1233:1239	disialo, core 2 species	1217:1239	disialo, core 2 species	1217:1239	MUC-1 from T47D had rather a simple glycosylation pattern, with NeuAcalpha2-3Galbeta1-3GalNAc-ol, Galbeta1-3GalNAc-ol, and GalNAc-ol predominating; in contrast, MUC-1 from MTSV1-7 had more complex structures, including a number of disialo, core 2 species, i.e. NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-3]GalNAc- ol and NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-4GlcNAcbet a1-3Galbeta1-3]GalNAc-ol.
8969192	2	1	theme	corresponding	322:334	arg1	tissues					343:349	corresponding normal tissues	322:349	corresponding normal tissues	322:349	MUC-1 mucin is considered to be aberrantly glycosylated in breast, ovary, and other carcinomas in comparison with mucin from corresponding normal tissues.
8969192	8	2	theme	breast	1694:1699	arg1	lines					1713:1717	breast cancer cell lines	1694:1717	breast cancer cell lines	1694:1717	We conclude that MUC-1 from breast cancer cell lines has simpler, and fewer, carbohydrate chains than MUC-1 from normal breast epithelial cells, and that these differences, combined or separately, explain the differential tumor specificity of some MUC-1 antibodies and T cells.
8969192	4	3	theme	oligosaccharide	799:813	arg1	profiles					815:822	more complex oligosaccharide profiles	786:822	more complex oligosaccharide profiles	786:822	Analysis by high pH anion chromatography showed that the normal cell lines had a higher ratio of GlcN/GalN and more complex oligosaccharide profiles than the cancer cell lines.
8969192	0	4	link	O-linked	14:21	arg1	chains					36:41	O-linked carbohydrate chains	14:41	O-linked carbohydrate chains in MUC-1	14:50	Comparison of O-linked carbohydrate chains in MUC-1 mucin from normal breast epithelial cell lines and breast carcinoma cell lines.
8969192	5	5	from	T47D	930:933	arg1	oligosaccharides					896:911	the oligosaccharides	892:911	the oligosaccharides from MTSV1-7 and T47D MUC-1	892:939	Structural analyses were carried out on the oligosaccharides from MTSV1-7 and T47D MUC-1, and the following structures were proposed.
8969192	3	6	theme	cell	528:531	arg1	lines					533:537	[3H]GlcN-labeled breast epithelial cell lines	493:537	[3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk	493:610	In order to clarify these differences in glycosylation, we have compared the O-linked carbohydrate chains from MUC-1 immunoprecipitated from [3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk, with three breast cancer cell lines (MCF-7, BT-20, and T47D).
8969192	3	6	theme	cell	528:531	arg1	MTSV1-7					549:555	MTSV1-7	549:555	MTSV1-7	549:555	In order to clarify these differences in glycosylation, we have compared the O-linked carbohydrate chains from MUC-1 immunoprecipitated from [3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk, with three breast cancer cell lines (MCF-7, BT-20, and T47D).
8969192	3	6	theme	cell	528:531	arg1	HB-2					562:565	HB-2	562:565	HB-2	562:565	In order to clarify these differences in glycosylation, we have compared the O-linked carbohydrate chains from MUC-1 immunoprecipitated from [3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk, with three breast cancer cell lines (MCF-7, BT-20, and T47D).
8969192	3	6	theme	cell	528:531	arg1	MMSV1-1					540:546	MMSV1-1	540:546	MMSV1-1	540:546	In order to clarify these differences in glycosylation, we have compared the O-linked carbohydrate chains from MUC-1 immunoprecipitated from [3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk, with three breast cancer cell lines (MCF-7, BT-20, and T47D).
8969192	5	7	from	MTSV1-7	918:924	arg1	oligosaccharides					896:911	the oligosaccharides	892:911	the oligosaccharides from MTSV1-7 and T47D MUC-1	892:939	Structural analyses were carried out on the oligosaccharides from MTSV1-7 and T47D MUC-1, and the following structures were proposed.
8969192	1	8	theme	glycan	167:172	arg1	chains					174:179	fewer glycan chains	161:179	fewer glycan chains in tumor cells	161:194	Demonstration of simpler and fewer glycan chains in tumor cells.
8969192	4	9	theme	GlcN/GalN	772:780	arg1	ratio					763:767	a higher ratio	754:767	a higher ratio of GlcN/GalN and more complex oligosaccharide profiles	754:822	Analysis by high pH anion chromatography showed that the normal cell lines had a higher ratio of GlcN/GalN and more complex oligosaccharide profiles than the cancer cell lines.
8969192	8	10	theme	antibodies	1920:1929	arg1	specificity					1894:1904	the differential tumor specificity	1871:1904	the differential tumor specificity of some MUC-1 antibodies and T cells	1871:1941	We conclude that MUC-1 from breast cancer cell lines has simpler, and fewer, carbohydrate chains than MUC-1 from normal breast epithelial cells, and that these differences, combined or separately, explain the differential tumor specificity of some MUC-1 antibodies and T cells.
8969192	8	11	theme	differential	1875:1886	arg1	specificity					1894:1904	the differential tumor specificity	1871:1904	the differential tumor specificity of some MUC-1 antibodies and T cells	1871:1941	We conclude that MUC-1 from breast cancer cell lines has simpler, and fewer, carbohydrate chains than MUC-1 from normal breast epithelial cells, and that these differences, combined or separately, explain the differential tumor specificity of some MUC-1 antibodies and T cells.
8969192	7	12	from	analysis	1486:1493	arg1	MUC-1					1536:1540	MUC-1	1536:1540	MUC-1	1536:1540	Double-labeling experiments with [3H]GlcN and 14C-aminoacids and analysis of GalNAc or GalNAc-ol:protein ratios in MUC-1 showed that there was also a significant difference in the degree of glycosylation of the mucin between the two cell types.
8969192	7	13	theme	cell	1654:1657	arg1	types					1659:1663	the two cell types	1646:1663	the two cell types	1646:1663	Double-labeling experiments with [3H]GlcN and 14C-aminoacids and analysis of GalNAc or GalNAc-ol:protein ratios in MUC-1 showed that there was also a significant difference in the degree of glycosylation of the mucin between the two cell types.
8969192	2	14	from	tissues	343:349	arg1	mucin					311:315	mucin	311:315	mucin from corresponding normal tissues	311:349	MUC-1 mucin is considered to be aberrantly glycosylated in breast, ovary, and other carcinomas in comparison with mucin from corresponding normal tissues.
8969192	6	15	theme	-3Galbeta1-3	1296:1307	arg1	ol					1317:1318	NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-3]GalNAc- ol	1247:1318	NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-3]GalNAc- ol	1247:1318	MUC-1 from T47D had rather a simple glycosylation pattern, with NeuAcalpha2-3Galbeta1-3GalNAc-ol, Galbeta1-3GalNAc-ol, and GalNAc-ol predominating; in contrast, MUC-1 from MTSV1-7 had more complex structures, including a number of disialo, core 2 species, i.e. NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-3]GalNAc- ol and NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-4GlcNAcbet a1-3Galbeta1-3]GalNAc-ol.
8969192	8	16	theme	fewer	1736:1740	arg1	chains					1756:1761	simpler, and fewer, carbohydrate chains	1723:1761	simpler, and fewer, carbohydrate chains	1723:1761	We conclude that MUC-1 from breast cancer cell lines has simpler, and fewer, carbohydrate chains than MUC-1 from normal breast epithelial cells, and that these differences, combined or separately, explain the differential tumor specificity of some MUC-1 antibodies and T cells.
8969192	7	17	from	GalNAc	1498:1503	arg1	MUC-1					1536:1540	MUC-1	1536:1540	MUC-1	1536:1540	Double-labeling experiments with [3H]GlcN and 14C-aminoacids and analysis of GalNAc or GalNAc-ol:protein ratios in MUC-1 showed that there was also a significant difference in the degree of glycosylation of the mucin between the two cell types.
8969192	6	18	theme	complex	1175:1181	arg1	structures					1183:1192	more complex structures	1170:1192	more complex structures	1170:1192	MUC-1 from T47D had rather a simple glycosylation pattern, with NeuAcalpha2-3Galbeta1-3GalNAc-ol, Galbeta1-3GalNAc-ol, and GalNAc-ol predominating; in contrast, MUC-1 from MTSV1-7 had more complex structures, including a number of disialo, core 2 species, i.e. NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-3]GalNAc- ol and NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-4GlcNAcbet a1-3Galbeta1-3]GalNAc-ol.
8969192	6	18	theme	complex	1175:1181	arg1	number					1207:1212	a number	1205:1212	a number of disialo, core 2 species, i.e. NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-3]GalNAc- ol and NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-4GlcNAcbet a1-3Galbeta1-3]GalNAc-ol	1205:1418	MUC-1 from T47D had rather a simple glycosylation pattern, with NeuAcalpha2-3Galbeta1-3GalNAc-ol, Galbeta1-3GalNAc-ol, and GalNAc-ol predominating; in contrast, MUC-1 from MTSV1-7 had more complex structures, including a number of disialo, core 2 species, i.e. NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-3]GalNAc- ol and NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-4GlcNAcbet a1-3Galbeta1-3]GalNAc-ol.
8969192	5	19	dep	MTSV1-7	918:924	arg1	MUC-1					935:939	MUC-1	935:939	MUC-1	935:939	Structural analyses were carried out on the oligosaccharides from MTSV1-7 and T47D MUC-1, and the following structures were proposed.
8969192	7	20	with	experiments	1437:1447	arg1	14C-aminoacids					1467:1480	14C-aminoacids	1467:1480	14C-aminoacids	1467:1480	Double-labeling experiments with [3H]GlcN and 14C-aminoacids and analysis of GalNAc or GalNAc-ol:protein ratios in MUC-1 showed that there was also a significant difference in the degree of glycosylation of the mucin between the two cell types.
8969192	7	20	with	experiments	1437:1447	arg1	GlcN					1458:1461	GlcN	1458:1461	GlcN	1458:1461	Double-labeling experiments with [3H]GlcN and 14C-aminoacids and analysis of GalNAc or GalNAc-ol:protein ratios in MUC-1 showed that there was also a significant difference in the degree of glycosylation of the mucin between the two cell types.
8969192	8	21	theme	carbohydrate	1743:1754	arg1	chains					1756:1761	simpler, and fewer, carbohydrate chains	1723:1761	simpler, and fewer, carbohydrate chains	1723:1761	We conclude that MUC-1 from breast cancer cell lines has simpler, and fewer, carbohydrate chains than MUC-1 from normal breast epithelial cells, and that these differences, combined or separately, explain the differential tumor specificity of some MUC-1 antibodies and T cells.
8969192	7	22	theme	mucin	1632:1636	arg1	glycosylation					1611:1623	glycosylation	1611:1623	glycosylation of the mucin	1611:1636	Double-labeling experiments with [3H]GlcN and 14C-aminoacids and analysis of GalNAc or GalNAc-ol:protein ratios in MUC-1 showed that there was also a significant difference in the degree of glycosylation of the mucin between the two cell types.
8969192	6	23	theme	species	1233:1239	arg1	number					1207:1212	a number	1205:1212	a number of disialo, core 2 species, i.e. NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-3]GalNAc- ol and NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-4GlcNAcbet a1-3Galbeta1-3]GalNAc-ol	1205:1418	MUC-1 from T47D had rather a simple glycosylation pattern, with NeuAcalpha2-3Galbeta1-3GalNAc-ol, Galbeta1-3GalNAc-ol, and GalNAc-ol predominating; in contrast, MUC-1 from MTSV1-7 had more complex structures, including a number of disialo, core 2 species, i.e. NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-3]GalNAc- ol and NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-4GlcNAcbet a1-3Galbeta1-3]GalNAc-ol.
8969192	4	24	theme	cancer	833:838	arg1	lines					845:849	the cancer cell lines	829:849	the cancer cell lines	829:849	Analysis by high pH anion chromatography showed that the normal cell lines had a higher ratio of GlcN/GalN and more complex oligosaccharide profiles than the cancer cell lines.
8969192	8	25	from	cells	1804:1808	arg1	MUC-1					1768:1772	MUC-1	1768:1772	MUC-1 from normal breast epithelial cells	1768:1808	We conclude that MUC-1 from breast cancer cell lines has simpler, and fewer, carbohydrate chains than MUC-1 from normal breast epithelial cells, and that these differences, combined or separately, explain the differential tumor specificity of some MUC-1 antibodies and T cells.
8969192	6	26	from	MTSV1-7	1158:1164	arg1	MUC-1					1147:1151	MUC-1	1147:1151	MUC-1 from MTSV1-7	1147:1164	MUC-1 from T47D had rather a simple glycosylation pattern, with NeuAcalpha2-3Galbeta1-3GalNAc-ol, Galbeta1-3GalNAc-ol, and GalNAc-ol predominating; in contrast, MUC-1 from MTSV1-7 had more complex structures, including a number of disialo, core 2 species, i.e. NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-3]GalNAc- ol and NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-4GlcNAcbet a1-3Galbeta1-3]GalNAc-ol.
8969192	8	27	theme	T	1935:1935	arg1	cells					1937:1941	T cells	1935:1941	T cells	1935:1941	We conclude that MUC-1 from breast cancer cell lines has simpler, and fewer, carbohydrate chains than MUC-1 from normal breast epithelial cells, and that these differences, combined or separately, explain the differential tumor specificity of some MUC-1 antibodies and T cells.
8969192	1	28	from	chains	174:179	arg1	cells					190:194	tumor cells	184:194	tumor cells	184:194	Demonstration of simpler and fewer glycan chains in tumor cells.
8969192	5	29	theme	Structural	852:861	arg1	analyses					863:870	Structural analyses	852:870	Structural analyses	852:870	Structural analyses were carried out on the oligosaccharides from MTSV1-7 and T47D MUC-1, and the following structures were proposed.
8969192	7	30	from	experiments	1437:1447	arg1	MUC-1					1536:1540	MUC-1	1536:1540	MUC-1	1536:1540	Double-labeling experiments with [3H]GlcN and 14C-aminoacids and analysis of GalNAc or GalNAc-ol:protein ratios in MUC-1 showed that there was also a significant difference in the degree of glycosylation of the mucin between the two cell types.
8969192	8	31	theme	breast	1786:1791	arg1	cells					1804:1808	normal breast epithelial cells	1779:1808	normal breast epithelial cells	1779:1808	We conclude that MUC-1 from breast cancer cell lines has simpler, and fewer, carbohydrate chains than MUC-1 from normal breast epithelial cells, and that these differences, combined or separately, explain the differential tumor specificity of some MUC-1 antibodies and T cells.
8969192	3	32	attach	derived	568:574	arg1	cells					581:585	cells	581:585	cells cultured from human milk	581:610	In order to clarify these differences in glycosylation, we have compared the O-linked carbohydrate chains from MUC-1 immunoprecipitated from [3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk, with three breast cancer cell lines (MCF-7, BT-20, and T47D).
8969192	3	32	attach	derived	568:574	arg2	MTSV1-7					549:555	MTSV1-7	549:555	MTSV1-7	549:555	In order to clarify these differences in glycosylation, we have compared the O-linked carbohydrate chains from MUC-1 immunoprecipitated from [3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk, with three breast cancer cell lines (MCF-7, BT-20, and T47D).
8969192	3	32	attach	derived	568:574	arg2	MMSV1-1					540:546	MMSV1-1	540:546	MMSV1-1	540:546	In order to clarify these differences in glycosylation, we have compared the O-linked carbohydrate chains from MUC-1 immunoprecipitated from [3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk, with three breast cancer cell lines (MCF-7, BT-20, and T47D).
8969192	3	32	attach	derived	568:574	arg2	HB-2					562:565	HB-2	562:565	HB-2	562:565	In order to clarify these differences in glycosylation, we have compared the O-linked carbohydrate chains from MUC-1 immunoprecipitated from [3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk, with three breast cancer cell lines (MCF-7, BT-20, and T47D).
8969192	3	32	attach	derived	568:574	arg2	lines					533:537	[3H]GlcN-labeled breast epithelial cell lines	493:537	[3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk	493:610	In order to clarify these differences in glycosylation, we have compared the O-linked carbohydrate chains from MUC-1 immunoprecipitated from [3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk, with three breast cancer cell lines (MCF-7, BT-20, and T47D).
8969192	4	33	contain	had	750:752	arg1	lines					744:748	the normal cell lines	728:748	the normal cell lines	728:748	Analysis by high pH anion chromatography showed that the normal cell lines had a higher ratio of GlcN/GalN and more complex oligosaccharide profiles than the cancer cell lines.
8969192	4	33	contain	had	750:752	arg2	ratio					763:767	a higher ratio	754:767	a higher ratio of GlcN/GalN and more complex oligosaccharide profiles	754:822	Analysis by high pH anion chromatography showed that the normal cell lines had a higher ratio of GlcN/GalN and more complex oligosaccharide profiles than the cancer cell lines.
8969192	0	34	theme	breast	70:75	arg1	lines					93:97	normal breast epithelial cell lines	63:97	normal breast epithelial cell lines	63:97	Comparison of O-linked carbohydrate chains in MUC-1 mucin from normal breast epithelial cell lines and breast carcinoma cell lines.
8969192	0	35	from	Comparison	0:9	arg1	MUC-1					46:50	MUC-1	46:50	MUC-1	46:50	Comparison of O-linked carbohydrate chains in MUC-1 mucin from normal breast epithelial cell lines and breast carcinoma cell lines.
8969192	4	36	theme	pH	692:693	arg1	chromatography					701:714	high pH anion chromatography	687:714	high pH anion chromatography	687:714	Analysis by high pH anion chromatography showed that the normal cell lines had a higher ratio of GlcN/GalN and more complex oligosaccharide profiles than the cancer cell lines.
8969192	0	37	theme	cell	88:91	arg1	lines					93:97	normal breast epithelial cell lines	63:97	normal breast epithelial cell lines	63:97	Comparison of O-linked carbohydrate chains in MUC-1 mucin from normal breast epithelial cell lines and breast carcinoma cell lines.
8969192	1	38	from	Demonstration	132:144	arg1	cells					190:194	tumor cells	184:194	tumor cells	184:194	Demonstration of simpler and fewer glycan chains in tumor cells.
8969192	0	39	from	MUC-1	46:50	arg1	Comparison					0:9	Comparison	0:9	Comparison of O-linked carbohydrate chains in MUC-1	0:50	Comparison of O-linked carbohydrate chains in MUC-1 mucin from normal breast epithelial cell lines and breast carcinoma cell lines.
8969192	6	40	theme	GalNAc-	1309:1315	arg1	ol					1317:1318	NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-3]GalNAc- ol	1247:1318	NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-3]GalNAc- ol	1247:1318	MUC-1 from T47D had rather a simple glycosylation pattern, with NeuAcalpha2-3Galbeta1-3GalNAc-ol, Galbeta1-3GalNAc-ol, and GalNAc-ol predominating; in contrast, MUC-1 from MTSV1-7 had more complex structures, including a number of disialo, core 2 species, i.e. NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-3]GalNAc- ol and NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-4GlcNAcbet a1-3Galbeta1-3]GalNAc-ol.
8969192	0	41	from	chains	36:41	arg1	MUC-1					46:50	MUC-1	46:50	MUC-1	46:50	Comparison of O-linked carbohydrate chains in MUC-1 mucin from normal breast epithelial cell lines and breast carcinoma cell lines.
8969192	3	42	dep	lines	643:647	arg1	MCF-7					650:654	MCF-7	650:654	MCF-7	650:654	In order to clarify these differences in glycosylation, we have compared the O-linked carbohydrate chains from MUC-1 immunoprecipitated from [3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk, with three breast cancer cell lines (MCF-7, BT-20, and T47D).
8969192	3	42	dep	lines	643:647	arg1	lines					643:647	three breast cancer cell lines	618:647	three breast cancer cell lines (MCF-7, BT-20, and T47D)	618:672	In order to clarify these differences in glycosylation, we have compared the O-linked carbohydrate chains from MUC-1 immunoprecipitated from [3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk, with three breast cancer cell lines (MCF-7, BT-20, and T47D).
8969192	3	42	dep	lines	643:647	arg1	BT-20					657:661	BT-20	657:661	BT-20	657:661	In order to clarify these differences in glycosylation, we have compared the O-linked carbohydrate chains from MUC-1 immunoprecipitated from [3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk, with three breast cancer cell lines (MCF-7, BT-20, and T47D).
8969192	3	42	dep	lines	643:647	arg1	T47D					668:671	T47D	668:671	T47D	668:671	In order to clarify these differences in glycosylation, we have compared the O-linked carbohydrate chains from MUC-1 immunoprecipitated from [3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk, with three breast cancer cell lines (MCF-7, BT-20, and T47D).
8969192	6	43	contain	had	1166:1168	arg1	MUC-1					1147:1151	MUC-1	1147:1151	MUC-1 from MTSV1-7	1147:1164	MUC-1 from T47D had rather a simple glycosylation pattern, with NeuAcalpha2-3Galbeta1-3GalNAc-ol, Galbeta1-3GalNAc-ol, and GalNAc-ol predominating; in contrast, MUC-1 from MTSV1-7 had more complex structures, including a number of disialo, core 2 species, i.e. NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-3]GalNAc- ol and NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-4GlcNAcbet a1-3Galbeta1-3]GalNAc-ol.
8969192	6	43	contain	had	1166:1168	arg2	structures					1183:1192	more complex structures	1170:1192	more complex structures	1170:1192	MUC-1 from T47D had rather a simple glycosylation pattern, with NeuAcalpha2-3Galbeta1-3GalNAc-ol, Galbeta1-3GalNAc-ol, and GalNAc-ol predominating; in contrast, MUC-1 from MTSV1-7 had more complex structures, including a number of disialo, core 2 species, i.e. NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-3]GalNAc- ol and NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-4GlcNAcbet a1-3Galbeta1-3]GalNAc-ol.
8969192	6	43	contain	had	1166:1168	arg2	number					1207:1212	a number	1205:1212	a number of disialo, core 2 species, i.e. NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-3]GalNAc- ol and NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-4GlcNAcbet a1-3Galbeta1-3]GalNAc-ol	1205:1418	MUC-1 from T47D had rather a simple glycosylation pattern, with NeuAcalpha2-3Galbeta1-3GalNAc-ol, Galbeta1-3GalNAc-ol, and GalNAc-ol predominating; in contrast, MUC-1 from MTSV1-7 had more complex structures, including a number of disialo, core 2 species, i.e. NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-3]GalNAc- ol and NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-4GlcNAcbet a1-3Galbeta1-3]GalNAc-ol.
8969192	3	44	theme	carbohydrate	438:449	arg1	chains					451:456	the O-linked carbohydrate chains	425:456	the O-linked carbohydrate chains from MUC-1 immunoprecipitated from [3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk	425:610	In order to clarify these differences in glycosylation, we have compared the O-linked carbohydrate chains from MUC-1 immunoprecipitated from [3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk, with three breast cancer cell lines (MCF-7, BT-20, and T47D).
8969192	0	45	theme	O-linked	14:21	arg1	chains					36:41	O-linked carbohydrate chains	14:41	O-linked carbohydrate chains in MUC-1	14:50	Comparison of O-linked carbohydrate chains in MUC-1 mucin from normal breast epithelial cell lines and breast carcinoma cell lines.
8969192	0	46	theme	chains	36:41	arg1	Comparison					0:9	Comparison	0:9	Comparison of O-linked carbohydrate chains in MUC-1	0:50	Comparison of O-linked carbohydrate chains in MUC-1 mucin from normal breast epithelial cell lines and breast carcinoma cell lines.
8969192	7	47	from	difference	1583:1592	arg1	degree					1601:1606	the degree	1597:1606	the degree of glycosylation of the mucin	1597:1636	Double-labeling experiments with [3H]GlcN and 14C-aminoacids and analysis of GalNAc or GalNAc-ol:protein ratios in MUC-1 showed that there was also a significant difference in the degree of glycosylation of the mucin between the two cell types.
8969192	5	48	theme	following	950:958	arg1	structures					960:969	the following structures	946:969	the following structures	946:969	Structural analyses were carried out on the oligosaccharides from MTSV1-7 and T47D MUC-1, and the following structures were proposed.
8969192	3	49	theme	cell	638:641	arg1	MCF-7					650:654	MCF-7	650:654	MCF-7	650:654	In order to clarify these differences in glycosylation, we have compared the O-linked carbohydrate chains from MUC-1 immunoprecipitated from [3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk, with three breast cancer cell lines (MCF-7, BT-20, and T47D).
8969192	3	49	theme	cell	638:641	arg1	lines					643:647	three breast cancer cell lines	618:647	three breast cancer cell lines (MCF-7, BT-20, and T47D)	618:672	In order to clarify these differences in glycosylation, we have compared the O-linked carbohydrate chains from MUC-1 immunoprecipitated from [3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk, with three breast cancer cell lines (MCF-7, BT-20, and T47D).
8969192	3	49	theme	cell	638:641	arg1	BT-20					657:661	BT-20	657:661	BT-20	657:661	In order to clarify these differences in glycosylation, we have compared the O-linked carbohydrate chains from MUC-1 immunoprecipitated from [3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk, with three breast cancer cell lines (MCF-7, BT-20, and T47D).
8969192	3	49	theme	cell	638:641	arg1	T47D					668:671	T47D	668:671	T47D	668:671	In order to clarify these differences in glycosylation, we have compared the O-linked carbohydrate chains from MUC-1 immunoprecipitated from [3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk, with three breast cancer cell lines (MCF-7, BT-20, and T47D).
8969192	8	50	from	lines	1713:1717	arg1	MUC-1					1683:1687	MUC-1	1683:1687	MUC-1 from breast cancer cell lines	1683:1717	We conclude that MUC-1 from breast cancer cell lines has simpler, and fewer, carbohydrate chains than MUC-1 from normal breast epithelial cells, and that these differences, combined or separately, explain the differential tumor specificity of some MUC-1 antibodies and T cells.
8969192	7	51	theme	protein	1518:1524	arg1	ratios					1526:1531	GalNAc-ol:protein ratios	1508:1531	GalNAc-ol:protein ratios in MUC-1	1508:1540	Double-labeling experiments with [3H]GlcN and 14C-aminoacids and analysis of GalNAc or GalNAc-ol:protein ratios in MUC-1 showed that there was also a significant difference in the degree of glycosylation of the mucin between the two cell types.
8969192	3	52	theme	breast	624:629	arg1	MCF-7					650:654	MCF-7	650:654	MCF-7	650:654	In order to clarify these differences in glycosylation, we have compared the O-linked carbohydrate chains from MUC-1 immunoprecipitated from [3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk, with three breast cancer cell lines (MCF-7, BT-20, and T47D).
8969192	3	52	theme	breast	624:629	arg1	lines					643:647	three breast cancer cell lines	618:647	three breast cancer cell lines (MCF-7, BT-20, and T47D)	618:672	In order to clarify these differences in glycosylation, we have compared the O-linked carbohydrate chains from MUC-1 immunoprecipitated from [3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk, with three breast cancer cell lines (MCF-7, BT-20, and T47D).
8969192	3	52	theme	breast	624:629	arg1	BT-20					657:661	BT-20	657:661	BT-20	657:661	In order to clarify these differences in glycosylation, we have compared the O-linked carbohydrate chains from MUC-1 immunoprecipitated from [3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk, with three breast cancer cell lines (MCF-7, BT-20, and T47D).
8969192	3	52	theme	breast	624:629	arg1	T47D					668:671	T47D	668:671	T47D	668:671	In order to clarify these differences in glycosylation, we have compared the O-linked carbohydrate chains from MUC-1 immunoprecipitated from [3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk, with three breast cancer cell lines (MCF-7, BT-20, and T47D).
8969192	4	53	theme	normal	732:737	arg1	lines					744:748	the normal cell lines	728:748	the normal cell lines	728:748	Analysis by high pH anion chromatography showed that the normal cell lines had a higher ratio of GlcN/GalN and more complex oligosaccharide profiles than the cancer cell lines.
8969192	3	54	theme	GlcN-labeled	497:508	arg1	lines					533:537	[3H]GlcN-labeled breast epithelial cell lines	493:537	[3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk	493:610	In order to clarify these differences in glycosylation, we have compared the O-linked carbohydrate chains from MUC-1 immunoprecipitated from [3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk, with three breast cancer cell lines (MCF-7, BT-20, and T47D).
8969192	3	54	theme	GlcN-labeled	497:508	arg1	MTSV1-7					549:555	MTSV1-7	549:555	MTSV1-7	549:555	In order to clarify these differences in glycosylation, we have compared the O-linked carbohydrate chains from MUC-1 immunoprecipitated from [3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk, with three breast cancer cell lines (MCF-7, BT-20, and T47D).
8969192	3	54	theme	GlcN-labeled	497:508	arg1	HB-2					562:565	HB-2	562:565	HB-2	562:565	In order to clarify these differences in glycosylation, we have compared the O-linked carbohydrate chains from MUC-1 immunoprecipitated from [3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk, with three breast cancer cell lines (MCF-7, BT-20, and T47D).
8969192	3	54	theme	GlcN-labeled	497:508	arg1	MMSV1-1					540:546	MMSV1-1	540:546	MMSV1-1	540:546	In order to clarify these differences in glycosylation, we have compared the O-linked carbohydrate chains from MUC-1 immunoprecipitated from [3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk, with three breast cancer cell lines (MCF-7, BT-20, and T47D).
8969192	7	55	from	ratios	1526:1531	arg1	MUC-1					1536:1540	MUC-1	1536:1540	MUC-1	1536:1540	Double-labeling experiments with [3H]GlcN and 14C-aminoacids and analysis of GalNAc or GalNAc-ol:protein ratios in MUC-1 showed that there was also a significant difference in the degree of glycosylation of the mucin between the two cell types.
8969192	7	56	theme	GalNAc-ol	1508:1516	arg1	ratios					1526:1531	GalNAc-ol:protein ratios	1508:1531	GalNAc-ol:protein ratios in MUC-1	1508:1540	Double-labeling experiments with [3H]GlcN and 14C-aminoacids and analysis of GalNAc or GalNAc-ol:protein ratios in MUC-1 showed that there was also a significant difference in the degree of glycosylation of the mucin between the two cell types.
8969192	6	57	theme	simple	1015:1020	arg1	pattern					1036:1042	a simple glycosylation pattern	1013:1042	a simple glycosylation pattern	1013:1042	MUC-1 from T47D had rather a simple glycosylation pattern, with NeuAcalpha2-3Galbeta1-3GalNAc-ol, Galbeta1-3GalNAc-ol, and GalNAc-ol predominating; in contrast, MUC-1 from MTSV1-7 had more complex structures, including a number of disialo, core 2 species, i.e. NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-3]GalNAc- ol and NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-4GlcNAcbet a1-3Galbeta1-3]GalNAc-ol.
8969192	6	58	theme	a1-3Galbeta1-3	1395:1408	arg1	GalNAc-ol					1410:1418	NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-4GlcNAcbet a1-3Galbeta1-3]GalNAc-ol	1324:1418	NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-4GlcNAcbet a1-3Galbeta1-3]GalNAc-ol	1324:1418	MUC-1 from T47D had rather a simple glycosylation pattern, with NeuAcalpha2-3Galbeta1-3GalNAc-ol, Galbeta1-3GalNAc-ol, and GalNAc-ol predominating; in contrast, MUC-1 from MTSV1-7 had more complex structures, including a number of disialo, core 2 species, i.e. NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-3]GalNAc- ol and NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-4GlcNAcbet a1-3Galbeta1-3]GalNAc-ol.
8969192	2	59	theme	normal	336:341	arg1	tissues					343:349	corresponding normal tissues	322:349	corresponding normal tissues	322:349	MUC-1 mucin is considered to be aberrantly glycosylated in breast, ovary, and other carcinomas in comparison with mucin from corresponding normal tissues.
8969192	7	60	from	MUC-1	1536:1540	arg1	experiments					1437:1447	Double-labeling experiments	1421:1447	Double-labeling experiments with [3H]GlcN and 14C-aminoacids	1421:1480	Double-labeling experiments with [3H]GlcN and 14C-aminoacids and analysis of GalNAc or GalNAc-ol:protein ratios in MUC-1 showed that there was also a significant difference in the degree of glycosylation of the mucin between the two cell types.
8969192	7	60	from	MUC-1	1536:1540	arg1	analysis					1486:1493	analysis	1486:1493	analysis of GalNAc or GalNAc-ol:protein ratios in MUC-1	1486:1540	Double-labeling experiments with [3H]GlcN and 14C-aminoacids and analysis of GalNAc or GalNAc-ol:protein ratios in MUC-1 showed that there was also a significant difference in the degree of glycosylation of the mucin between the two cell types.
8969192	7	61	theme	GalNAc	1498:1503	arg1	experiments					1437:1447	Double-labeling experiments	1421:1447	Double-labeling experiments with [3H]GlcN and 14C-aminoacids	1421:1480	Double-labeling experiments with [3H]GlcN and 14C-aminoacids and analysis of GalNAc or GalNAc-ol:protein ratios in MUC-1 showed that there was also a significant difference in the degree of glycosylation of the mucin between the two cell types.
8969192	7	61	theme	GalNAc	1498:1503	arg1	analysis					1486:1493	analysis	1486:1493	analysis of GalNAc or GalNAc-ol:protein ratios in MUC-1	1486:1540	Double-labeling experiments with [3H]GlcN and 14C-aminoacids and analysis of GalNAc or GalNAc-ol:protein ratios in MUC-1 showed that there was also a significant difference in the degree of glycosylation of the mucin between the two cell types.
8969192	3	62	link	O-linked	429:436	arg1	chains					451:456	the O-linked carbohydrate chains	425:456	the O-linked carbohydrate chains from MUC-1 immunoprecipitated from [3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk	425:610	In order to clarify these differences in glycosylation, we have compared the O-linked carbohydrate chains from MUC-1 immunoprecipitated from [3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk, with three breast cancer cell lines (MCF-7, BT-20, and T47D).
8969192	8	63	theme	cell	1708:1711	arg1	lines					1713:1717	breast cancer cell lines	1694:1717	breast cancer cell lines	1694:1717	We conclude that MUC-1 from breast cancer cell lines has simpler, and fewer, carbohydrate chains than MUC-1 from normal breast epithelial cells, and that these differences, combined or separately, explain the differential tumor specificity of some MUC-1 antibodies and T cells.
8969192	4	64	theme	complex	791:797	arg1	profiles					815:822	more complex oligosaccharide profiles	786:822	more complex oligosaccharide profiles	786:822	Analysis by high pH anion chromatography showed that the normal cell lines had a higher ratio of GlcN/GalN and more complex oligosaccharide profiles than the cancer cell lines.
8969192	6	65	from	T47D	997:1000	arg1	MUC-1					986:990	MUC-1	986:990	MUC-1 from T47D	986:1000	MUC-1 from T47D had rather a simple glycosylation pattern, with NeuAcalpha2-3Galbeta1-3GalNAc-ol, Galbeta1-3GalNAc-ol, and GalNAc-ol predominating; in contrast, MUC-1 from MTSV1-7 had more complex structures, including a number of disialo, core 2 species, i.e. NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-3]GalNAc- ol and NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-4GlcNAcbet a1-3Galbeta1-3]GalNAc-ol.
8969192	3	66	theme	epithelial	517:526	arg1	lines					533:537	[3H]GlcN-labeled breast epithelial cell lines	493:537	[3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk	493:610	In order to clarify these differences in glycosylation, we have compared the O-linked carbohydrate chains from MUC-1 immunoprecipitated from [3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk, with three breast cancer cell lines (MCF-7, BT-20, and T47D).
8969192	3	66	theme	epithelial	517:526	arg1	MTSV1-7					549:555	MTSV1-7	549:555	MTSV1-7	549:555	In order to clarify these differences in glycosylation, we have compared the O-linked carbohydrate chains from MUC-1 immunoprecipitated from [3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk, with three breast cancer cell lines (MCF-7, BT-20, and T47D).
8969192	3	66	theme	epithelial	517:526	arg1	HB-2					562:565	HB-2	562:565	HB-2	562:565	In order to clarify these differences in glycosylation, we have compared the O-linked carbohydrate chains from MUC-1 immunoprecipitated from [3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk, with three breast cancer cell lines (MCF-7, BT-20, and T47D).
8969192	3	66	theme	epithelial	517:526	arg1	MMSV1-1					540:546	MMSV1-1	540:546	MMSV1-1	540:546	In order to clarify these differences in glycosylation, we have compared the O-linked carbohydrate chains from MUC-1 immunoprecipitated from [3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk, with three breast cancer cell lines (MCF-7, BT-20, and T47D).
8969192	8	67	theme	cancer	1701:1706	arg1	lines					1713:1717	breast cancer cell lines	1694:1717	breast cancer cell lines	1694:1717	We conclude that MUC-1 from breast cancer cell lines has simpler, and fewer, carbohydrate chains than MUC-1 from normal breast epithelial cells, and that these differences, combined or separately, explain the differential tumor specificity of some MUC-1 antibodies and T cells.
8969192	1	68	theme	fewer	161:165	arg1	chains					174:179	fewer glycan chains	161:179	fewer glycan chains in tumor cells	161:194	Demonstration of simpler and fewer glycan chains in tumor cells.
8969192	6	69	dep	disialo	1217:1223	arg1	core					1226:1229	core 2	1226:1231	core 2	1226:1231	MUC-1 from T47D had rather a simple glycosylation pattern, with NeuAcalpha2-3Galbeta1-3GalNAc-ol, Galbeta1-3GalNAc-ol, and GalNAc-ol predominating; in contrast, MUC-1 from MTSV1-7 had more complex structures, including a number of disialo, core 2 species, i.e. NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-3]GalNAc- ol and NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-4GlcNAcbet a1-3Galbeta1-3]GalNAc-ol.
8969192	4	70	theme	higher	756:761	arg1	ratio					763:767	a higher ratio	754:767	a higher ratio of GlcN/GalN and more complex oligosaccharide profiles	754:822	Analysis by high pH anion chromatography showed that the normal cell lines had a higher ratio of GlcN/GalN and more complex oligosaccharide profiles than the cancer cell lines.
8969192	6	71	theme	GalNAc-ol	1109:1117	arg1	predominating					1119:1131	GalNAc-ol predominating	1109:1131	GalNAc-ol predominating	1109:1131	MUC-1 from T47D had rather a simple glycosylation pattern, with NeuAcalpha2-3Galbeta1-3GalNAc-ol, Galbeta1-3GalNAc-ol, and GalNAc-ol predominating; in contrast, MUC-1 from MTSV1-7 had more complex structures, including a number of disialo, core 2 species, i.e. NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-3]GalNAc- ol and NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-4GlcNAcbet a1-3Galbeta1-3]GalNAc-ol.
8969192	2	72	gly	glycosylated	240:251	arg1	ovary					264:268	ovary	264:268	ovary	264:268	MUC-1 mucin is considered to be aberrantly glycosylated in breast, ovary, and other carcinomas in comparison with mucin from corresponding normal tissues.
8969192	2	72	gly	glycosylated	240:251	arg2	mucin					203:207	MUC-1 mucin	197:207	MUC-1 mucin	197:207	MUC-1 mucin is considered to be aberrantly glycosylated in breast, ovary, and other carcinomas in comparison with mucin from corresponding normal tissues.
8969192	2	72	gly	glycosylated	240:251	arg1	mucin					203:207	MUC-1 mucin	197:207	MUC-1 mucin	197:207	MUC-1 mucin is considered to be aberrantly glycosylated in breast, ovary, and other carcinomas in comparison with mucin from corresponding normal tissues.
8969192	2	72	gly	glycosylated	240:251	arg1	carcinomas					281:290	other carcinomas	275:290	other carcinomas in comparison with mucin from corresponding normal tissues	275:349	MUC-1 mucin is considered to be aberrantly glycosylated in breast, ovary, and other carcinomas in comparison with mucin from corresponding normal tissues.
8969192	2	72	gly	glycosylated	240:251	arg1	breast					256:261	breast	256:261	breast	256:261	MUC-1 mucin is considered to be aberrantly glycosylated in breast, ovary, and other carcinomas in comparison with mucin from corresponding normal tissues.
8969192	6	73	theme	-3Galbeta1-4GlcNAcbet	1373:1393	arg1	GalNAc-ol					1410:1418	NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-4GlcNAcbet a1-3Galbeta1-3]GalNAc-ol	1324:1418	NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-4GlcNAcbet a1-3Galbeta1-3]GalNAc-ol	1324:1418	MUC-1 from T47D had rather a simple glycosylation pattern, with NeuAcalpha2-3Galbeta1-3GalNAc-ol, Galbeta1-3GalNAc-ol, and GalNAc-ol predominating; in contrast, MUC-1 from MTSV1-7 had more complex structures, including a number of disialo, core 2 species, i.e. NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-3]GalNAc- ol and NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-4GlcNAcbet a1-3Galbeta1-3]GalNAc-ol.
8969192	8	74	theme	tumor	1888:1892	arg1	specificity					1894:1904	the differential tumor specificity	1871:1904	the differential tumor specificity of some MUC-1 antibodies and T cells	1871:1941	We conclude that MUC-1 from breast cancer cell lines has simpler, and fewer, carbohydrate chains than MUC-1 from normal breast epithelial cells, and that these differences, combined or separately, explain the differential tumor specificity of some MUC-1 antibodies and T cells.
8969192	3	75	from	MUC-1	463:467	arg1	chains					451:456	the O-linked carbohydrate chains	425:456	the O-linked carbohydrate chains from MUC-1 immunoprecipitated from [3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk	425:610	In order to clarify these differences in glycosylation, we have compared the O-linked carbohydrate chains from MUC-1 immunoprecipitated from [3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk, with three breast cancer cell lines (MCF-7, BT-20, and T47D).
8969192	2	76	theme	MUC-1	197:201	arg1	mucin					203:207	MUC-1 mucin	197:207	MUC-1 mucin	197:207	MUC-1 mucin is considered to be aberrantly glycosylated in breast, ovary, and other carcinomas in comparison with mucin from corresponding normal tissues.
8969192	0	77	theme	cell	120:123	arg1	lines					125:129	breast carcinoma cell lines	103:129	breast carcinoma cell lines	103:129	Comparison of O-linked carbohydrate chains in MUC-1 mucin from normal breast epithelial cell lines and breast carcinoma cell lines.
8969192	2	78	theme	other	275:279	arg1	carcinomas					281:290	other carcinomas	275:290	other carcinomas in comparison with mucin from corresponding normal tissues	275:349	MUC-1 mucin is considered to be aberrantly glycosylated in breast, ovary, and other carcinomas in comparison with mucin from corresponding normal tissues.
8969192	8	79	theme	simpler	1723:1729	arg1	chains					1756:1761	simpler, and fewer, carbohydrate chains	1723:1761	simpler, and fewer, carbohydrate chains	1723:1761	We conclude that MUC-1 from breast cancer cell lines has simpler, and fewer, carbohydrate chains than MUC-1 from normal breast epithelial cells, and that these differences, combined or separately, explain the differential tumor specificity of some MUC-1 antibodies and T cells.
8969192	1	80	theme	tumor	184:188	arg1	cells					190:194	tumor cells	184:194	tumor cells	184:194	Demonstration of simpler and fewer glycan chains in tumor cells.
8969192	4	81	theme	cell	840:843	arg1	lines					845:849	the cancer cell lines	829:849	the cancer cell lines	829:849	Analysis by high pH anion chromatography showed that the normal cell lines had a higher ratio of GlcN/GalN and more complex oligosaccharide profiles than the cancer cell lines.
8969192	7	82	theme	Double-labeling	1421:1435	arg1	experiments					1437:1447	Double-labeling experiments	1421:1447	Double-labeling experiments with [3H]GlcN and 14C-aminoacids	1421:1480	Double-labeling experiments with [3H]GlcN and 14C-aminoacids and analysis of GalNAc or GalNAc-ol:protein ratios in MUC-1 showed that there was also a significant difference in the degree of glycosylation of the mucin between the two cell types.
8969192	6	83	theme	NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2	1247:1294	arg1	ol					1317:1318	NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-3]GalNAc- ol	1247:1318	NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-3]GalNAc- ol	1247:1318	MUC-1 from T47D had rather a simple glycosylation pattern, with NeuAcalpha2-3Galbeta1-3GalNAc-ol, Galbeta1-3GalNAc-ol, and GalNAc-ol predominating; in contrast, MUC-1 from MTSV1-7 had more complex structures, including a number of disialo, core 2 species, i.e. NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-3]GalNAc- ol and NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-4GlcNAcbet a1-3Galbeta1-3]GalNAc-ol.
8969192	6	84	contain	had	1002:1004	arg2	pattern					1036:1042	a simple glycosylation pattern	1013:1042	a simple glycosylation pattern	1013:1042	MUC-1 from T47D had rather a simple glycosylation pattern, with NeuAcalpha2-3Galbeta1-3GalNAc-ol, Galbeta1-3GalNAc-ol, and GalNAc-ol predominating; in contrast, MUC-1 from MTSV1-7 had more complex structures, including a number of disialo, core 2 species, i.e. NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-3]GalNAc- ol and NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-4GlcNAcbet a1-3Galbeta1-3]GalNAc-ol.
8969192	6	84	contain	had	1002:1004	arg1	MUC-1					986:990	MUC-1	986:990	MUC-1 from T47D	986:1000	MUC-1 from T47D had rather a simple glycosylation pattern, with NeuAcalpha2-3Galbeta1-3GalNAc-ol, Galbeta1-3GalNAc-ol, and GalNAc-ol predominating; in contrast, MUC-1 from MTSV1-7 had more complex structures, including a number of disialo, core 2 species, i.e. NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-3]GalNAc- ol and NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-4GlcNAcbet a1-3Galbeta1-3]GalNAc-ol.
8969192	7	85	theme	glycosylation	1611:1623	arg1	degree					1601:1606	the degree	1597:1606	the degree of glycosylation of the mucin	1597:1636	Double-labeling experiments with [3H]GlcN and 14C-aminoacids and analysis of GalNAc or GalNAc-ol:protein ratios in MUC-1 showed that there was also a significant difference in the degree of glycosylation of the mucin between the two cell types.
8969192	4	86	theme	profiles	815:822	arg1	ratio					763:767	a higher ratio	754:767	a higher ratio of GlcN/GalN and more complex oligosaccharide profiles	754:822	Analysis by high pH anion chromatography showed that the normal cell lines had a higher ratio of GlcN/GalN and more complex oligosaccharide profiles than the cancer cell lines.
8969192	8	87	theme	cells	1937:1941	arg1	specificity					1894:1904	the differential tumor specificity	1871:1904	the differential tumor specificity of some MUC-1 antibodies and T cells	1871:1941	We conclude that MUC-1 from breast cancer cell lines has simpler, and fewer, carbohydrate chains than MUC-1 from normal breast epithelial cells, and that these differences, combined or separately, explain the differential tumor specificity of some MUC-1 antibodies and T cells.
8969192	3	88	dep	lines	533:537	arg1	lines					533:537	[3H]GlcN-labeled breast epithelial cell lines	493:537	[3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk	493:610	In order to clarify these differences in glycosylation, we have compared the O-linked carbohydrate chains from MUC-1 immunoprecipitated from [3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk, with three breast cancer cell lines (MCF-7, BT-20, and T47D).
8969192	3	88	dep	lines	533:537	arg1	MTSV1-7					549:555	MTSV1-7	549:555	MTSV1-7	549:555	In order to clarify these differences in glycosylation, we have compared the O-linked carbohydrate chains from MUC-1 immunoprecipitated from [3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk, with three breast cancer cell lines (MCF-7, BT-20, and T47D).
8969192	3	88	dep	lines	533:537	arg1	HB-2					562:565	HB-2	562:565	HB-2	562:565	In order to clarify these differences in glycosylation, we have compared the O-linked carbohydrate chains from MUC-1 immunoprecipitated from [3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk, with three breast cancer cell lines (MCF-7, BT-20, and T47D).
8969192	3	88	dep	lines	533:537	arg1	MMSV1-1					540:546	MMSV1-1	540:546	MMSV1-1	540:546	In order to clarify these differences in glycosylation, we have compared the O-linked carbohydrate chains from MUC-1 immunoprecipitated from [3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk, with three breast cancer cell lines (MCF-7, BT-20, and T47D).
8969192	2	89	from	breast	256:261	arg1	comparison					295:304	comparison	295:304	comparison with mucin from corresponding normal tissues	295:349	MUC-1 mucin is considered to be aberrantly glycosylated in breast, ovary, and other carcinomas in comparison with mucin from corresponding normal tissues.
8969192	0	90	theme	normal	63:68	arg1	lines					93:97	normal breast epithelial cell lines	63:97	normal breast epithelial cell lines	63:97	Comparison of O-linked carbohydrate chains in MUC-1 mucin from normal breast epithelial cell lines and breast carcinoma cell lines.
8969192	2	91	from	ovary	264:268	arg1	comparison					295:304	comparison	295:304	comparison with mucin from corresponding normal tissues	295:349	MUC-1 mucin is considered to be aberrantly glycosylated in breast, ovary, and other carcinomas in comparison with mucin from corresponding normal tissues.
8969192	0	92	theme	epithelial	77:86	arg1	lines					93:97	normal breast epithelial cell lines	63:97	normal breast epithelial cell lines	63:97	Comparison of O-linked carbohydrate chains in MUC-1 mucin from normal breast epithelial cell lines and breast carcinoma cell lines.
8969192	3	93	from	differences	378:388	arg1	glycosylation					393:405	glycosylation	393:405	glycosylation	393:405	In order to clarify these differences in glycosylation, we have compared the O-linked carbohydrate chains from MUC-1 immunoprecipitated from [3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk, with three breast cancer cell lines (MCF-7, BT-20, and T47D).
8969192	6	94	dep	ol	1317:1318	arg1	i.e.					1242:1245	i.e.	1242:1245	i.e.	1242:1245	MUC-1 from T47D had rather a simple glycosylation pattern, with NeuAcalpha2-3Galbeta1-3GalNAc-ol, Galbeta1-3GalNAc-ol, and GalNAc-ol predominating; in contrast, MUC-1 from MTSV1-7 had more complex structures, including a number of disialo, core 2 species, i.e. NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-3]GalNAc- ol and NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-4GlcNAcbet a1-3Galbeta1-3]GalNAc-ol.
8969192	8	95	theme	normal	1779:1784	arg1	cells					1804:1808	normal breast epithelial cells	1779:1808	normal breast epithelial cells	1779:1808	We conclude that MUC-1 from breast cancer cell lines has simpler, and fewer, carbohydrate chains than MUC-1 from normal breast epithelial cells, and that these differences, combined or separately, explain the differential tumor specificity of some MUC-1 antibodies and T cells.
8969192	1	96	theme	simpler	149:155	arg1	chains					174:179	fewer glycan chains	161:179	fewer glycan chains in tumor cells	161:194	Demonstration of simpler and fewer glycan chains in tumor cells.
8969192	1	96	theme	simpler	149:155	arg1	Demonstration					132:144	Demonstration	132:144	Demonstration of simpler	132:155	Demonstration of simpler and fewer glycan chains in tumor cells.
8969192	7	97	theme	significant	1571:1581	arg1	difference					1583:1592	a significant difference	1569:1592	a significant difference in the degree of glycosylation of the mucin between the two cell types	1569:1663	Double-labeling experiments with [3H]GlcN and 14C-aminoacids and analysis of GalNAc or GalNAc-ol:protein ratios in MUC-1 showed that there was also a significant difference in the degree of glycosylation of the mucin between the two cell types.
8969192	0	98	theme	carcinoma	110:118	arg1	lines					125:129	breast carcinoma cell lines	103:129	breast carcinoma cell lines	103:129	Comparison of O-linked carbohydrate chains in MUC-1 mucin from normal breast epithelial cell lines and breast carcinoma cell lines.
8969192	6	99	theme	NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2	1324:1371	arg1	GalNAc-ol					1410:1418	NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-4GlcNAcbet a1-3Galbeta1-3]GalNAc-ol	1324:1418	NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-4GlcNAcbet a1-3Galbeta1-3]GalNAc-ol	1324:1418	MUC-1 from T47D had rather a simple glycosylation pattern, with NeuAcalpha2-3Galbeta1-3GalNAc-ol, Galbeta1-3GalNAc-ol, and GalNAc-ol predominating; in contrast, MUC-1 from MTSV1-7 had more complex structures, including a number of disialo, core 2 species, i.e. NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-3]GalNAc- ol and NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-4GlcNAcbet a1-3Galbeta1-3]GalNAc-ol.
8969192	8	100	theme	epithelial	1793:1802	arg1	cells					1804:1808	normal breast epithelial cells	1779:1808	normal breast epithelial cells	1779:1808	We conclude that MUC-1 from breast cancer cell lines has simpler, and fewer, carbohydrate chains than MUC-1 from normal breast epithelial cells, and that these differences, combined or separately, explain the differential tumor specificity of some MUC-1 antibodies and T cells.
8969192	2	101	from	carcinomas	281:290	arg1	comparison					295:304	comparison	295:304	comparison with mucin from corresponding normal tissues	295:349	MUC-1 mucin is considered to be aberrantly glycosylated in breast, ovary, and other carcinomas in comparison with mucin from corresponding normal tissues.
8969192	3	102	dep	clarify	364:370	arg1	to					361:362	to	361:362	to	361:362	In order to clarify these differences in glycosylation, we have compared the O-linked carbohydrate chains from MUC-1 immunoprecipitated from [3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk, with three breast cancer cell lines (MCF-7, BT-20, and T47D).
8969192	4	103	theme	high	687:690	arg1	chromatography					701:714	high pH anion chromatography	687:714	high pH anion chromatography	687:714	Analysis by high pH anion chromatography showed that the normal cell lines had a higher ratio of GlcN/GalN and more complex oligosaccharide profiles than the cancer cell lines.
8969192	0	104	theme	breast	103:108	arg1	lines					125:129	breast carcinoma cell lines	103:129	breast carcinoma cell lines	103:129	Comparison of O-linked carbohydrate chains in MUC-1 mucin from normal breast epithelial cell lines and breast carcinoma cell lines.
8969192	8	105	contain	has	1719:1721	arg1	MUC-1					1683:1687	MUC-1	1683:1687	MUC-1 from breast cancer cell lines	1683:1717	We conclude that MUC-1 from breast cancer cell lines has simpler, and fewer, carbohydrate chains than MUC-1 from normal breast epithelial cells, and that these differences, combined or separately, explain the differential tumor specificity of some MUC-1 antibodies and T cells.
8969192	8	105	contain	has	1719:1721	arg2	chains					1756:1761	simpler, and fewer, carbohydrate chains	1723:1761	simpler, and fewer, carbohydrate chains	1723:1761	We conclude that MUC-1 from breast cancer cell lines has simpler, and fewer, carbohydrate chains than MUC-1 from normal breast epithelial cells, and that these differences, combined or separately, explain the differential tumor specificity of some MUC-1 antibodies and T cells.
8969192	4	106	theme	anion	695:699	arg1	chromatography					701:714	high pH anion chromatography	687:714	high pH anion chromatography	687:714	Analysis by high pH anion chromatography showed that the normal cell lines had a higher ratio of GlcN/GalN and more complex oligosaccharide profiles than the cancer cell lines.
8969192	8	107	theme	MUC-1	1914:1918	arg1	antibodies					1920:1929	MUC-1 antibodies	1914:1929	MUC-1 antibodies	1914:1929	We conclude that MUC-1 from breast cancer cell lines has simpler, and fewer, carbohydrate chains than MUC-1 from normal breast epithelial cells, and that these differences, combined or separately, explain the differential tumor specificity of some MUC-1 antibodies and T cells.
8969192	0	108	theme	carbohydrate	23:34	arg1	chains					36:41	O-linked carbohydrate chains	14:41	O-linked carbohydrate chains in MUC-1	14:50	Comparison of O-linked carbohydrate chains in MUC-1 mucin from normal breast epithelial cell lines and breast carcinoma cell lines.
8969192	8	109	dep	antibodies	1920:1929	arg1	some					1909:1912	some	1909:1912	some	1909:1912	We conclude that MUC-1 from breast cancer cell lines has simpler, and fewer, carbohydrate chains than MUC-1 from normal breast epithelial cells, and that these differences, combined or separately, explain the differential tumor specificity of some MUC-1 antibodies and T cells.
8969192	2	110	with	comparison	295:304	arg1	mucin					311:315	mucin	311:315	mucin from corresponding normal tissues	311:349	MUC-1 mucin is considered to be aberrantly glycosylated in breast, ovary, and other carcinomas in comparison with mucin from corresponding normal tissues.
8969192	3	111	theme	human	601:605	arg1	milk					607:610	human milk	601:610	human milk	601:610	In order to clarify these differences in glycosylation, we have compared the O-linked carbohydrate chains from MUC-1 immunoprecipitated from [3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk, with three breast cancer cell lines (MCF-7, BT-20, and T47D).
8969192	4	112	theme	cell	739:742	arg1	lines					744:748	the normal cell lines	728:748	the normal cell lines	728:748	Analysis by high pH anion chromatography showed that the normal cell lines had a higher ratio of GlcN/GalN and more complex oligosaccharide profiles than the cancer cell lines.
8969192	3	113	theme	O-linked	429:436	arg1	chains					451:456	the O-linked carbohydrate chains	425:456	the O-linked carbohydrate chains from MUC-1 immunoprecipitated from [3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk	425:610	In order to clarify these differences in glycosylation, we have compared the O-linked carbohydrate chains from MUC-1 immunoprecipitated from [3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk, with three breast cancer cell lines (MCF-7, BT-20, and T47D).
8969192	3	114	theme	cancer	631:636	arg1	MCF-7					650:654	MCF-7	650:654	MCF-7	650:654	In order to clarify these differences in glycosylation, we have compared the O-linked carbohydrate chains from MUC-1 immunoprecipitated from [3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk, with three breast cancer cell lines (MCF-7, BT-20, and T47D).
8969192	3	114	theme	cancer	631:636	arg1	lines					643:647	three breast cancer cell lines	618:647	three breast cancer cell lines (MCF-7, BT-20, and T47D)	618:672	In order to clarify these differences in glycosylation, we have compared the O-linked carbohydrate chains from MUC-1 immunoprecipitated from [3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk, with three breast cancer cell lines (MCF-7, BT-20, and T47D).
8969192	3	114	theme	cancer	631:636	arg1	BT-20					657:661	BT-20	657:661	BT-20	657:661	In order to clarify these differences in glycosylation, we have compared the O-linked carbohydrate chains from MUC-1 immunoprecipitated from [3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk, with three breast cancer cell lines (MCF-7, BT-20, and T47D).
8969192	3	114	theme	cancer	631:636	arg1	T47D					668:671	T47D	668:671	T47D	668:671	In order to clarify these differences in glycosylation, we have compared the O-linked carbohydrate chains from MUC-1 immunoprecipitated from [3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk, with three breast cancer cell lines (MCF-7, BT-20, and T47D).
8969192	7	115	gly	glycosylation	1611:1623	arg1	mucin					1632:1636	the mucin	1628:1636	the mucin	1628:1636	Double-labeling experiments with [3H]GlcN and 14C-aminoacids and analysis of GalNAc or GalNAc-ol:protein ratios in MUC-1 showed that there was also a significant difference in the degree of glycosylation of the mucin between the two cell types.
8969192	7	116	with	analysis	1486:1493	arg1	14C-aminoacids					1467:1480	14C-aminoacids	1467:1480	14C-aminoacids	1467:1480	Double-labeling experiments with [3H]GlcN and 14C-aminoacids and analysis of GalNAc or GalNAc-ol:protein ratios in MUC-1 showed that there was also a significant difference in the degree of glycosylation of the mucin between the two cell types.
8969192	7	116	with	analysis	1486:1493	arg1	GlcN					1458:1461	GlcN	1458:1461	GlcN	1458:1461	Double-labeling experiments with [3H]GlcN and 14C-aminoacids and analysis of GalNAc or GalNAc-ol:protein ratios in MUC-1 showed that there was also a significant difference in the degree of glycosylation of the mucin between the two cell types.
8969192	7	117	theme	ratios	1526:1531	arg1	experiments					1437:1447	Double-labeling experiments	1421:1447	Double-labeling experiments with [3H]GlcN and 14C-aminoacids	1421:1480	Double-labeling experiments with [3H]GlcN and 14C-aminoacids and analysis of GalNAc or GalNAc-ol:protein ratios in MUC-1 showed that there was also a significant difference in the degree of glycosylation of the mucin between the two cell types.
8969192	7	117	theme	ratios	1526:1531	arg1	analysis					1486:1493	analysis	1486:1493	analysis of GalNAc or GalNAc-ol:protein ratios in MUC-1	1486:1540	Double-labeling experiments with [3H]GlcN and 14C-aminoacids and analysis of GalNAc or GalNAc-ol:protein ratios in MUC-1 showed that there was also a significant difference in the degree of glycosylation of the mucin between the two cell types.
8969192	6	118	theme	glycosylation	1022:1034	arg1	pattern					1036:1042	a simple glycosylation pattern	1013:1042	a simple glycosylation pattern	1013:1042	MUC-1 from T47D had rather a simple glycosylation pattern, with NeuAcalpha2-3Galbeta1-3GalNAc-ol, Galbeta1-3GalNAc-ol, and GalNAc-ol predominating; in contrast, MUC-1 from MTSV1-7 had more complex structures, including a number of disialo, core 2 species, i.e. NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-3]GalNAc- ol and NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-4GlcNAcbet a1-3Galbeta1-3]GalNAc-ol.
8969192	3	119	theme	breast	510:515	arg1	lines					533:537	[3H]GlcN-labeled breast epithelial cell lines	493:537	[3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk	493:610	In order to clarify these differences in glycosylation, we have compared the O-linked carbohydrate chains from MUC-1 immunoprecipitated from [3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk, with three breast cancer cell lines (MCF-7, BT-20, and T47D).
8969192	3	119	theme	breast	510:515	arg1	MTSV1-7					549:555	MTSV1-7	549:555	MTSV1-7	549:555	In order to clarify these differences in glycosylation, we have compared the O-linked carbohydrate chains from MUC-1 immunoprecipitated from [3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk, with three breast cancer cell lines (MCF-7, BT-20, and T47D).
8969192	3	119	theme	breast	510:515	arg1	HB-2					562:565	HB-2	562:565	HB-2	562:565	In order to clarify these differences in glycosylation, we have compared the O-linked carbohydrate chains from MUC-1 immunoprecipitated from [3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk, with three breast cancer cell lines (MCF-7, BT-20, and T47D).
8969192	3	119	theme	breast	510:515	arg1	MMSV1-1					540:546	MMSV1-1	540:546	MMSV1-1	540:546	In order to clarify these differences in glycosylation, we have compared the O-linked carbohydrate chains from MUC-1 immunoprecipitated from [3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk, with three breast cancer cell lines (MCF-7, BT-20, and T47D).
7107587	3	0	theme	parent	247:252	arg1	molecule					254:261	the parent molecule	243:261	the parent molecule	243:261	All the carbohydrate on the parent molecule could be accounted for on the B beta and gamma chains.
7107587	6	1	theme	1H-NMR	527:532	arg1	consistent					587:596	consistent	587:596	consistent	587:596	The 300-MHz 1H-NMR spectra of glycopeptides from all three sources were consistent with biantennary type oligosaccharide chains.
7107587	6	1	theme	1H-NMR	527:532	arg1	spectra					534:540	The 300-MHz 1H-NMR spectra	515:540	The 300-MHz 1H-NMR spectra of glycopeptides from all three sources	515:580	The 300-MHz 1H-NMR spectra of glycopeptides from all three sources were consistent with biantennary type oligosaccharide chains.
7107587	2	2	theme	chains	196:201	arg1	composition					134:144	The carbohydrate composition	117:144	The carbohydrate composition of fibrinogen and constituent S-carboxymethylated chains	117:201	The carbohydrate composition of fibrinogen and constituent S-carboxymethylated chains was determined.
7107587	2	3	theme	constituent	164:174	arg1	chains					196:201	constituent S-carboxymethylated chains	164:201	constituent S-carboxymethylated chains	164:201	The carbohydrate composition of fibrinogen and constituent S-carboxymethylated chains was determined.
7107587	4	4	theme	carbohydrate	362:373	arg1	devoid					352:357	devoid	352:357	devoid	352:357	The A alpha chain was found to be devoid of carbohydrate.
7107587	4	4	theme	carbohydrate	362:373	arg1	chain					330:334	The A alpha chain	318:334	The A alpha chain	318:334	The A alpha chain was found to be devoid of carbohydrate.
7107587	6	5	theme	type	615:618	arg1	chains					636:641	biantennary type oligosaccharide chains	603:641	biantennary type oligosaccharide chains	603:641	The 300-MHz 1H-NMR spectra of glycopeptides from all three sources were consistent with biantennary type oligosaccharide chains.
7107587	6	6	with	consistent	587:596	arg1	chains					636:641	biantennary type oligosaccharide chains	603:641	biantennary type oligosaccharide chains	603:641	The 300-MHz 1H-NMR spectra of glycopeptides from all three sources were consistent with biantennary type oligosaccharide chains.
7107587	12	7	from	chromatography	1230:1243	arg1	A-Sepharose					1282:1292	concanavalin A-Sepharose	1269:1292	concanavalin A-Sepharose	1269:1292	Affinity chromatography of the glycopeptides on concanavalin A-Sepharose also showed that the glycopeptides from fibrinogen are greater than 95% biantennary oligosaccharide chains.
7107587	12	8	theme	biantennary	1366:1376	arg1	chains					1394:1399	greater than 95% biantennary oligosaccharide chains	1349:1399	greater than 95% biantennary oligosaccharide chains	1349:1399	Affinity chromatography of the glycopeptides on concanavalin A-Sepharose also showed that the glycopeptides from fibrinogen are greater than 95% biantennary oligosaccharide chains.
7107587	12	8	theme	biantennary	1366:1376	arg1	glycopeptides					1315:1327	the glycopeptides	1311:1327	the glycopeptides from fibrinogen	1311:1343	Affinity chromatography of the glycopeptides on concanavalin A-Sepharose also showed that the glycopeptides from fibrinogen are greater than 95% biantennary oligosaccharide chains.
7107587	9	9	theme	biantennary	1032:1042	arg1	type					1044:1047	the biantennary type	1028:1047	the biantennary type	1028:1047	Our results indicate that fibrinogen glycopeptides are of the biantennary type, and are in complete agreement with the previously reported peak assignments (Vliegenthart, J. F. G., van Halbeek, H., and Dorland, L. (1981) Pure Appl.
7107587	5	10	theme	subsequent	471:480	arg1	chromatography					482:495	subsequent chromatography	471:495	subsequent chromatography on Sephadex G-50	471:512	Glycopeptides were prepared from fibrinogen, B beta, and gamma chains by pronase digestion and subsequent chromatography on Sephadex G-50.
7107587	3	11	theme	B	293:293	arg1	beta					295:298	B beta	293:298	B beta	293:298	All the carbohydrate on the parent molecule could be accounted for on the B beta and gamma chains.
7107587	7	12	theme	1H-NMR	730:735	arg1	spectroscopy					737:748	300-MHz 1H-NMR spectroscopy	722:748	300-MHz 1H-NMR spectroscopy	722:748	The glycopeptides resulting from exoglycosidase digestions were examined with 300-MHz 1H-NMR spectroscopy, and the changes in the signals caused by selective removal of sugar residues were studied.
7107587	3	13	from	carbohydrate	227:238	arg1	molecule					254:261	the parent molecule	243:261	the parent molecule	243:261	All the carbohydrate on the parent molecule could be accounted for on the B beta and gamma chains.
7107587	9	14	theme	complete	1061:1068	arg1	agreement					1070:1078	complete agreement	1061:1078	complete agreement with the previously reported peak assignments (Vliegenthart, J. F. G., van Halbeek, H., and Dorland, L. (1981) Pure Appl	1061:1199	Our results indicate that fibrinogen glycopeptides are of the biantennary type, and are in complete agreement with the previously reported peak assignments (Vliegenthart, J. F. G., van Halbeek, H., and Dorland, L. (1981) Pure Appl.
7107587	12	15	from	fibrinogen	1334:1343	arg1	chains					1394:1399	greater than 95% biantennary oligosaccharide chains	1349:1399	greater than 95% biantennary oligosaccharide chains	1349:1399	Affinity chromatography of the glycopeptides on concanavalin A-Sepharose also showed that the glycopeptides from fibrinogen are greater than 95% biantennary oligosaccharide chains.
7107587	12	15	from	fibrinogen	1334:1343	arg1	glycopeptides					1315:1327	the glycopeptides	1311:1327	the glycopeptides from fibrinogen	1311:1343	Affinity chromatography of the glycopeptides on concanavalin A-Sepharose also showed that the glycopeptides from fibrinogen are greater than 95% biantennary oligosaccharide chains.
7107587	7	16	theme	exoglycosidase	677:690	arg1	digestions					692:701	exoglycosidase digestions	677:701	exoglycosidase digestions	677:701	The glycopeptides resulting from exoglycosidase digestions were examined with 300-MHz 1H-NMR spectroscopy, and the changes in the signals caused by selective removal of sugar residues were studied.
7107587	13	17	theme	alditol	1568:1574	arg1	acetates					1576:1583	derived partially methylated alditol acetates	1539:1583	derived partially methylated alditol acetates	1539:1583	Based on carbohydrate composition, 1H-NMR spectroscopy, sequential exoglycosidase digestion, and gas chromatography-mass spectrometry of derived partially methylated alditol acetates, we propose that fibrinogen contains four oligosaccharide chains of the structure shown below.
7107587	11	18	dep	53	1209:1210	arg1	45-77					1213:1217	45-77	1213:1217	45-77	1213:1217	53, 45-77).
7107587	14	19	dep	formula	1681:1687	arg1	see					1690:1692	see	1690:1692	see text	1690:1697	(formula, see text)
7107587	9	20	theme	peak	1109:1112	arg1	G.					1147:1148	G.	1147:1148	G.	1147:1148	Our results indicate that fibrinogen glycopeptides are of the biantennary type, and are in complete agreement with the previously reported peak assignments (Vliegenthart, J. F. G., van Halbeek, H., and Dorland, L. (1981) Pure Appl.
7107587	9	20	theme	peak	1109:1112	arg1	assignments					1114:1124	the previously reported peak assignments	1085:1124	the previously reported peak assignments (Vliegenthart, J. F. G., van Halbeek, H., and Dorland, L. (1981) Pure Appl	1085:1199	Our results indicate that fibrinogen glycopeptides are of the biantennary type, and are in complete agreement with the previously reported peak assignments (Vliegenthart, J. F. G., van Halbeek, H., and Dorland, L. (1981) Pure Appl.
7107587	9	20	theme	peak	1109:1112	arg1	H.					1164:1165	H.	1164:1165	H.	1164:1165	Our results indicate that fibrinogen glycopeptides are of the biantennary type, and are in complete agreement with the previously reported peak assignments (Vliegenthart, J. F. G., van Halbeek, H., and Dorland, L. (1981) Pure Appl.
7107587	9	20	theme	peak	1109:1112	arg1	Dorland					1172:1178	Dorland	1172:1178	Dorland	1172:1178	Our results indicate that fibrinogen glycopeptides are of the biantennary type, and are in complete agreement with the previously reported peak assignments (Vliegenthart, J. F. G., van Halbeek, H., and Dorland, L. (1981) Pure Appl.
7107587	9	21	with	agreement	1070:1078	arg1	G.					1147:1148	G.	1147:1148	G.	1147:1148	Our results indicate that fibrinogen glycopeptides are of the biantennary type, and are in complete agreement with the previously reported peak assignments (Vliegenthart, J. F. G., van Halbeek, H., and Dorland, L. (1981) Pure Appl.
7107587	9	21	with	agreement	1070:1078	arg1	assignments					1114:1124	the previously reported peak assignments	1085:1124	the previously reported peak assignments (Vliegenthart, J. F. G., van Halbeek, H., and Dorland, L. (1981) Pure Appl	1085:1199	Our results indicate that fibrinogen glycopeptides are of the biantennary type, and are in complete agreement with the previously reported peak assignments (Vliegenthart, J. F. G., van Halbeek, H., and Dorland, L. (1981) Pure Appl.
7107587	9	21	with	agreement	1070:1078	arg1	H.					1164:1165	H.	1164:1165	H.	1164:1165	Our results indicate that fibrinogen glycopeptides are of the biantennary type, and are in complete agreement with the previously reported peak assignments (Vliegenthart, J. F. G., van Halbeek, H., and Dorland, L. (1981) Pure Appl.
7107587	9	21	with	agreement	1070:1078	arg1	Dorland					1172:1178	Dorland	1172:1178	Dorland	1172:1178	Our results indicate that fibrinogen glycopeptides are of the biantennary type, and are in complete agreement with the previously reported peak assignments (Vliegenthart, J. F. G., van Halbeek, H., and Dorland, L. (1981) Pure Appl.
7107587	1	22	theme	1H-NMR	59:64	arg1	Use					44:46	Use	44:46	Use of 300-MHz 1H-NMR	44:64	Use of 300-MHz 1H-NMR to characterize glycosidase-treated glycopeptides.
7107587	13	23	theme	gas	1499:1501	arg1	spectrometry					1523:1534	gas chromatography-mass spectrometry	1499:1534	gas chromatography-mass spectrometry	1499:1534	Based on carbohydrate composition, 1H-NMR spectroscopy, sequential exoglycosidase digestion, and gas chromatography-mass spectrometry of derived partially methylated alditol acetates, we propose that fibrinogen contains four oligosaccharide chains of the structure shown below.
7107587	4	24	theme	A	322:322	arg1	devoid					352:357	devoid	352:357	devoid	352:357	The A alpha chain was found to be devoid of carbohydrate.
7107587	4	24	theme	A	322:322	arg1	chain					330:334	The A alpha chain	318:334	The A alpha chain	318:334	The A alpha chain was found to be devoid of carbohydrate.
7107587	9	25	theme	fibrinogen	996:1005	arg1	glycopeptides					1007:1019	fibrinogen glycopeptides	996:1019	fibrinogen glycopeptides	996:1019	Our results indicate that fibrinogen glycopeptides are of the biantennary type, and are in complete agreement with the previously reported peak assignments (Vliegenthart, J. F. G., van Halbeek, H., and Dorland, L. (1981) Pure Appl.
7107587	0	26	theme	Carbohydrate	0:11	arg1	structure					13:21	Carbohydrate structure	0:21	Carbohydrate structure of human fibrinogen	0:41	Carbohydrate structure of human fibrinogen.
7107587	8	27	theme	independent	940:950	arg1	unit					935:938	the corresponding monosaccharide unit	902:938	the corresponding monosaccharide unit independent of previous work	902:967	This technique enabled us to assign each anomeric proton to the corresponding monosaccharide unit independent of previous work.
7107587	13	28	link	derived	1539:1545	arg1	acetates					1576:1583	derived partially methylated alditol acetates	1539:1583	derived partially methylated alditol acetates	1539:1583	Based on carbohydrate composition, 1H-NMR spectroscopy, sequential exoglycosidase digestion, and gas chromatography-mass spectrometry of derived partially methylated alditol acetates, we propose that fibrinogen contains four oligosaccharide chains of the structure shown below.
7107587	13	29	theme	exoglycosidase	1469:1482	arg1	digestion					1484:1492	sequential exoglycosidase digestion	1458:1492	sequential exoglycosidase digestion	1458:1492	Based on carbohydrate composition, 1H-NMR spectroscopy, sequential exoglycosidase digestion, and gas chromatography-mass spectrometry of derived partially methylated alditol acetates, we propose that fibrinogen contains four oligosaccharide chains of the structure shown below.
7107587	8	30	theme	previous	955:962	arg1	work					964:967	previous work	955:967	previous work	955:967	This technique enabled us to assign each anomeric proton to the corresponding monosaccharide unit independent of previous work.
7107587	13	31	contain	contains	1613:1620	arg2	chains					1643:1648	four oligosaccharide chains	1622:1648	four oligosaccharide chains of the structure shown below	1622:1677	Based on carbohydrate composition, 1H-NMR spectroscopy, sequential exoglycosidase digestion, and gas chromatography-mass spectrometry of derived partially methylated alditol acetates, we propose that fibrinogen contains four oligosaccharide chains of the structure shown below.
7107587	13	31	contain	contains	1613:1620	arg1	fibrinogen					1602:1611	fibrinogen	1602:1611	fibrinogen	1602:1611	Based on carbohydrate composition, 1H-NMR spectroscopy, sequential exoglycosidase digestion, and gas chromatography-mass spectrometry of derived partially methylated alditol acetates, we propose that fibrinogen contains four oligosaccharide chains of the structure shown below.
7107587	7	32	theme	sugar	813:817	arg1	residues					819:826	sugar residues	813:826	sugar residues	813:826	The glycopeptides resulting from exoglycosidase digestions were examined with 300-MHz 1H-NMR spectroscopy, and the changes in the signals caused by selective removal of sugar residues were studied.
7107587	0	33	theme	fibrinogen	32:41	arg1	structure					13:21	Carbohydrate structure	0:21	Carbohydrate structure of human fibrinogen	0:41	Carbohydrate structure of human fibrinogen.
7107587	5	34	from	chromatography	482:495	arg1	G-50					509:512	Sephadex G-50	500:512	Sephadex G-50	500:512	Glycopeptides were prepared from fibrinogen, B beta, and gamma chains by pronase digestion and subsequent chromatography on Sephadex G-50.
7107587	13	35	theme	structure	1657:1665	arg1	chains					1643:1648	four oligosaccharide chains	1622:1648	four oligosaccharide chains of the structure shown below	1622:1677	Based on carbohydrate composition, 1H-NMR spectroscopy, sequential exoglycosidase digestion, and gas chromatography-mass spectrometry of derived partially methylated alditol acetates, we propose that fibrinogen contains four oligosaccharide chains of the structure shown below.
7107587	13	36	theme	1H-NMR	1437:1442	arg1	spectroscopy					1444:1455	1H-NMR spectroscopy	1437:1455	1H-NMR spectroscopy	1437:1455	Based on carbohydrate composition, 1H-NMR spectroscopy, sequential exoglycosidase digestion, and gas chromatography-mass spectrometry of derived partially methylated alditol acetates, we propose that fibrinogen contains four oligosaccharide chains of the structure shown below.
7107587	6	37	from	sources	574:580	arg1	consistent					587:596	consistent	587:596	consistent	587:596	The 300-MHz 1H-NMR spectra of glycopeptides from all three sources were consistent with biantennary type oligosaccharide chains.
7107587	6	37	from	sources	574:580	arg1	glycopeptides					545:557	glycopeptides	545:557	glycopeptides from all three sources	545:580	The 300-MHz 1H-NMR spectra of glycopeptides from all three sources were consistent with biantennary type oligosaccharide chains.
7107587	6	37	from	sources	574:580	arg1	spectra					534:540	The 300-MHz 1H-NMR spectra	515:540	The 300-MHz 1H-NMR spectra of glycopeptides from all three sources	515:580	The 300-MHz 1H-NMR spectra of glycopeptides from all three sources were consistent with biantennary type oligosaccharide chains.
7107587	9	38	dep	assignments	1114:1124	arg1	1981					1185:1188	1981	1185:1188	1981	1185:1188	Our results indicate that fibrinogen glycopeptides are of the biantennary type, and are in complete agreement with the previously reported peak assignments (Vliegenthart, J. F. G., van Halbeek, H., and Dorland, L. (1981) Pure Appl.
7107587	9	38	dep	assignments	1114:1124	arg1	G.					1147:1148	G.	1147:1148	G.	1147:1148	Our results indicate that fibrinogen glycopeptides are of the biantennary type, and are in complete agreement with the previously reported peak assignments (Vliegenthart, J. F. G., van Halbeek, H., and Dorland, L. (1981) Pure Appl.
7107587	9	38	dep	assignments	1114:1124	arg1	assignments					1114:1124	the previously reported peak assignments	1085:1124	the previously reported peak assignments (Vliegenthart, J. F. G., van Halbeek, H., and Dorland, L. (1981) Pure Appl	1085:1199	Our results indicate that fibrinogen glycopeptides are of the biantennary type, and are in complete agreement with the previously reported peak assignments (Vliegenthart, J. F. G., van Halbeek, H., and Dorland, L. (1981) Pure Appl.
7107587	9	38	dep	assignments	1114:1124	arg1	Dorland					1172:1178	Dorland	1172:1178	Dorland	1172:1178	Our results indicate that fibrinogen glycopeptides are of the biantennary type, and are in complete agreement with the previously reported peak assignments (Vliegenthart, J. F. G., van Halbeek, H., and Dorland, L. (1981) Pure Appl.
7107587	9	38	dep	assignments	1114:1124	arg1	L					1181:1181	L	1181:1181	L	1181:1181	Our results indicate that fibrinogen glycopeptides are of the biantennary type, and are in complete agreement with the previously reported peak assignments (Vliegenthart, J. F. G., van Halbeek, H., and Dorland, L. (1981) Pure Appl.
7107587	9	38	dep	assignments	1114:1124	arg1	H.					1164:1165	H.	1164:1165	H.	1164:1165	Our results indicate that fibrinogen glycopeptides are of the biantennary type, and are in complete agreement with the previously reported peak assignments (Vliegenthart, J. F. G., van Halbeek, H., and Dorland, L. (1981) Pure Appl.
7107587	9	38	dep	assignments	1114:1124	arg1	J.					1141:1142	J.	1141:1142	J.	1141:1142	Our results indicate that fibrinogen glycopeptides are of the biantennary type, and are in complete agreement with the previously reported peak assignments (Vliegenthart, J. F. G., van Halbeek, H., and Dorland, L. (1981) Pure Appl.
7107587	9	39	dep	G.	1147:1148	arg1	Appl					1196:1199	Appl	1196:1199	Appl	1196:1199	Our results indicate that fibrinogen glycopeptides are of the biantennary type, and are in complete agreement with the previously reported peak assignments (Vliegenthart, J. F. G., van Halbeek, H., and Dorland, L. (1981) Pure Appl.
7107587	12	40	gly	glycopeptides	1252:1264	arg2	glycopeptides					1252:1264	the glycopeptides	1248:1264	the glycopeptides	1248:1264	Affinity chromatography of the glycopeptides on concanavalin A-Sepharose also showed that the glycopeptides from fibrinogen are greater than 95% biantennary oligosaccharide chains.
7107587	5	41	theme	pronase	449:455	arg1	digestion					457:465	pronase digestion	449:465	pronase digestion	449:465	Glycopeptides were prepared from fibrinogen, B beta, and gamma chains by pronase digestion and subsequent chromatography on Sephadex G-50.
7107587	9	42	gly	glycopeptides	1007:1019	arg2	glycopeptides					1007:1019	fibrinogen glycopeptides	996:1019	fibrinogen glycopeptides	996:1019	Our results indicate that fibrinogen glycopeptides are of the biantennary type, and are in complete agreement with the previously reported peak assignments (Vliegenthart, J. F. G., van Halbeek, H., and Dorland, L. (1981) Pure Appl.
7107587	6	43	theme	glycopeptides	545:557	arg1	consistent					587:596	consistent	587:596	consistent	587:596	The 300-MHz 1H-NMR spectra of glycopeptides from all three sources were consistent with biantennary type oligosaccharide chains.
7107587	6	43	theme	glycopeptides	545:557	arg1	spectra					534:540	The 300-MHz 1H-NMR spectra	515:540	The 300-MHz 1H-NMR spectra of glycopeptides from all three sources	515:580	The 300-MHz 1H-NMR spectra of glycopeptides from all three sources were consistent with biantennary type oligosaccharide chains.
7107587	12	44	dep	chains	1394:1399	arg1	%					1364:1364	%	1364:1364	%	1364:1364	Affinity chromatography of the glycopeptides on concanavalin A-Sepharose also showed that the glycopeptides from fibrinogen are greater than 95% biantennary oligosaccharide chains.
7107587	2	45	theme	carbohydrate	121:132	arg1	composition					134:144	The carbohydrate composition	117:144	The carbohydrate composition of fibrinogen and constituent S-carboxymethylated chains	117:201	The carbohydrate composition of fibrinogen and constituent S-carboxymethylated chains was determined.
7107587	13	46	theme	oligosaccharide	1627:1641	arg1	chains					1643:1648	four oligosaccharide chains	1622:1648	four oligosaccharide chains of the structure shown below	1622:1677	Based on carbohydrate composition, 1H-NMR spectroscopy, sequential exoglycosidase digestion, and gas chromatography-mass spectrometry of derived partially methylated alditol acetates, we propose that fibrinogen contains four oligosaccharide chains of the structure shown below.
7107587	12	47	theme	oligosaccharide	1378:1392	arg1	chains					1394:1399	greater than 95% biantennary oligosaccharide chains	1349:1399	greater than 95% biantennary oligosaccharide chains	1349:1399	Affinity chromatography of the glycopeptides on concanavalin A-Sepharose also showed that the glycopeptides from fibrinogen are greater than 95% biantennary oligosaccharide chains.
7107587	12	47	theme	oligosaccharide	1378:1392	arg1	glycopeptides					1315:1327	the glycopeptides	1311:1327	the glycopeptides from fibrinogen	1311:1343	Affinity chromatography of the glycopeptides on concanavalin A-Sepharose also showed that the glycopeptides from fibrinogen are greater than 95% biantennary oligosaccharide chains.
7107587	7	48	gly	glycopeptides	648:660	arg2	glycopeptides					648:660	The glycopeptides	644:660	The glycopeptides resulting from exoglycosidase digestions	644:701	The glycopeptides resulting from exoglycosidase digestions were examined with 300-MHz 1H-NMR spectroscopy, and the changes in the signals caused by selective removal of sugar residues were studied.
7107587	6	49	theme	300-MHz	519:525	arg1	consistent					587:596	consistent	587:596	consistent	587:596	The 300-MHz 1H-NMR spectra of glycopeptides from all three sources were consistent with biantennary type oligosaccharide chains.
7107587	6	49	theme	300-MHz	519:525	arg1	spectra					534:540	The 300-MHz 1H-NMR spectra	515:540	The 300-MHz 1H-NMR spectra of glycopeptides from all three sources	515:580	The 300-MHz 1H-NMR spectra of glycopeptides from all three sources were consistent with biantennary type oligosaccharide chains.
7107587	2	50	theme	S-carboxymethylated	176:194	arg1	chains					196:201	constituent S-carboxymethylated chains	164:201	constituent S-carboxymethylated chains	164:201	The carbohydrate composition of fibrinogen and constituent S-carboxymethylated chains was determined.
7107587	5	51	theme	Sephadex	500:507	arg1	G-50					509:512	Sephadex G-50	500:512	Sephadex G-50	500:512	Glycopeptides were prepared from fibrinogen, B beta, and gamma chains by pronase digestion and subsequent chromatography on Sephadex G-50.
7107587	6	52	from	spectra	534:540	arg1	sources					574:580	all three sources	564:580	all three sources	564:580	The 300-MHz 1H-NMR spectra of glycopeptides from all three sources were consistent with biantennary type oligosaccharide chains.
7107587	6	53	theme	oligosaccharide	620:634	arg1	chains					636:641	biantennary type oligosaccharide chains	603:641	biantennary type oligosaccharide chains	603:641	The 300-MHz 1H-NMR spectra of glycopeptides from all three sources were consistent with biantennary type oligosaccharide chains.
7107587	6	54	theme	biantennary	603:613	arg1	chains					636:641	biantennary type oligosaccharide chains	603:641	biantennary type oligosaccharide chains	603:641	The 300-MHz 1H-NMR spectra of glycopeptides from all three sources were consistent with biantennary type oligosaccharide chains.
7107587	7	55	from	changes	759:765	arg1	signals					774:780	the signals	770:780	the signals caused by selective removal of sugar residues	770:826	The glycopeptides resulting from exoglycosidase digestions were examined with 300-MHz 1H-NMR spectroscopy, and the changes in the signals caused by selective removal of sugar residues were studied.
7107587	13	56	theme	acetates	1576:1583	arg1	composition					1424:1434	carbohydrate composition	1411:1434	carbohydrate composition	1411:1434	Based on carbohydrate composition, 1H-NMR spectroscopy, sequential exoglycosidase digestion, and gas chromatography-mass spectrometry of derived partially methylated alditol acetates, we propose that fibrinogen contains four oligosaccharide chains of the structure shown below.
7107587	13	56	theme	acetates	1576:1583	arg1	spectroscopy					1444:1455	1H-NMR spectroscopy	1437:1455	1H-NMR spectroscopy	1437:1455	Based on carbohydrate composition, 1H-NMR spectroscopy, sequential exoglycosidase digestion, and gas chromatography-mass spectrometry of derived partially methylated alditol acetates, we propose that fibrinogen contains four oligosaccharide chains of the structure shown below.
7107587	13	56	theme	acetates	1576:1583	arg1	spectrometry					1523:1534	gas chromatography-mass spectrometry	1499:1534	gas chromatography-mass spectrometry	1499:1534	Based on carbohydrate composition, 1H-NMR spectroscopy, sequential exoglycosidase digestion, and gas chromatography-mass spectrometry of derived partially methylated alditol acetates, we propose that fibrinogen contains four oligosaccharide chains of the structure shown below.
7107587	13	56	theme	acetates	1576:1583	arg1	digestion					1484:1492	sequential exoglycosidase digestion	1458:1492	sequential exoglycosidase digestion	1458:1492	Based on carbohydrate composition, 1H-NMR spectroscopy, sequential exoglycosidase digestion, and gas chromatography-mass spectrometry of derived partially methylated alditol acetates, we propose that fibrinogen contains four oligosaccharide chains of the structure shown below.
7107587	3	57	theme	beta	295:298	arg1	chains					310:315	the B beta and gamma chains	289:315	the B beta and gamma chains	289:315	All the carbohydrate on the parent molecule could be accounted for on the B beta and gamma chains.
7107587	7	58	theme	300-MHz	722:728	arg1	spectroscopy					737:748	300-MHz 1H-NMR spectroscopy	722:748	300-MHz 1H-NMR spectroscopy	722:748	The glycopeptides resulting from exoglycosidase digestions were examined with 300-MHz 1H-NMR spectroscopy, and the changes in the signals caused by selective removal of sugar residues were studied.
7107587	13	59	theme	derived	1539:1545	arg1	acetates					1576:1583	derived partially methylated alditol acetates	1539:1583	derived partially methylated alditol acetates	1539:1583	Based on carbohydrate composition, 1H-NMR spectroscopy, sequential exoglycosidase digestion, and gas chromatography-mass spectrometry of derived partially methylated alditol acetates, we propose that fibrinogen contains four oligosaccharide chains of the structure shown below.
7107587	13	60	theme	methylated	1557:1566	arg1	acetates					1576:1583	derived partially methylated alditol acetates	1539:1583	derived partially methylated alditol acetates	1539:1583	Based on carbohydrate composition, 1H-NMR spectroscopy, sequential exoglycosidase digestion, and gas chromatography-mass spectrometry of derived partially methylated alditol acetates, we propose that fibrinogen contains four oligosaccharide chains of the structure shown below.
7107587	6	61	gly	glycopeptides	545:557	arg2	glycopeptides					545:557	glycopeptides	545:557	glycopeptides from all three sources	545:580	The 300-MHz 1H-NMR spectra of glycopeptides from all three sources were consistent with biantennary type oligosaccharide chains.
7107587	6	61	gly	glycopeptides	545:557	arg1	sources					574:580	all three sources	564:580	all three sources	564:580	The 300-MHz 1H-NMR spectra of glycopeptides from all three sources were consistent with biantennary type oligosaccharide chains.
7107587	3	62	theme	gamma	304:308	arg1	chains					310:315	the B beta and gamma chains	289:315	the B beta and gamma chains	289:315	All the carbohydrate on the parent molecule could be accounted for on the B beta and gamma chains.
7107587	9	63	theme	reported	1100:1107	arg1	G.					1147:1148	G.	1147:1148	G.	1147:1148	Our results indicate that fibrinogen glycopeptides are of the biantennary type, and are in complete agreement with the previously reported peak assignments (Vliegenthart, J. F. G., van Halbeek, H., and Dorland, L. (1981) Pure Appl.
7107587	9	63	theme	reported	1100:1107	arg1	assignments					1114:1124	the previously reported peak assignments	1085:1124	the previously reported peak assignments (Vliegenthart, J. F. G., van Halbeek, H., and Dorland, L. (1981) Pure Appl	1085:1199	Our results indicate that fibrinogen glycopeptides are of the biantennary type, and are in complete agreement with the previously reported peak assignments (Vliegenthart, J. F. G., van Halbeek, H., and Dorland, L. (1981) Pure Appl.
7107587	9	63	theme	reported	1100:1107	arg1	H.					1164:1165	H.	1164:1165	H.	1164:1165	Our results indicate that fibrinogen glycopeptides are of the biantennary type, and are in complete agreement with the previously reported peak assignments (Vliegenthart, J. F. G., van Halbeek, H., and Dorland, L. (1981) Pure Appl.
7107587	9	63	theme	reported	1100:1107	arg1	Dorland					1172:1178	Dorland	1172:1178	Dorland	1172:1178	Our results indicate that fibrinogen glycopeptides are of the biantennary type, and are in complete agreement with the previously reported peak assignments (Vliegenthart, J. F. G., van Halbeek, H., and Dorland, L. (1981) Pure Appl.
7107587	1	64	gly	glycopeptides	102:114	arg2	glycopeptides					102:114	glycosidase-treated glycopeptides	82:114	glycosidase-treated glycopeptides	82:114	Use of 300-MHz 1H-NMR to characterize glycosidase-treated glycopeptides.
7107587	1	65	theme	300-MHz	51:57	arg1	1H-NMR					59:64	300-MHz 1H-NMR	51:64	300-MHz 1H-NMR	51:64	Use of 300-MHz 1H-NMR to characterize glycosidase-treated glycopeptides.
7107587	8	66	theme	anomeric	883:890	arg1	proton					892:897	each anomeric proton	878:897	each anomeric proton	878:897	This technique enabled us to assign each anomeric proton to the corresponding monosaccharide unit independent of previous work.
7107587	12	67	gly	glycopeptides	1315:1327	arg1	fibrinogen					1334:1343	fibrinogen	1334:1343	fibrinogen	1334:1343	Affinity chromatography of the glycopeptides on concanavalin A-Sepharose also showed that the glycopeptides from fibrinogen are greater than 95% biantennary oligosaccharide chains.
7107587	12	67	gly	glycopeptides	1315:1327	arg2	chains					1394:1399	greater than 95% biantennary oligosaccharide chains	1349:1399	greater than 95% biantennary oligosaccharide chains	1349:1399	Affinity chromatography of the glycopeptides on concanavalin A-Sepharose also showed that the glycopeptides from fibrinogen are greater than 95% biantennary oligosaccharide chains.
7107587	12	67	gly	glycopeptides	1315:1327	arg2	glycopeptides					1315:1327	the glycopeptides	1311:1327	the glycopeptides from fibrinogen	1311:1343	Affinity chromatography of the glycopeptides on concanavalin A-Sepharose also showed that the glycopeptides from fibrinogen are greater than 95% biantennary oligosaccharide chains.
7107587	9	68	with	type	1044:1047	arg1	G.					1147:1148	G.	1147:1148	G.	1147:1148	Our results indicate that fibrinogen glycopeptides are of the biantennary type, and are in complete agreement with the previously reported peak assignments (Vliegenthart, J. F. G., van Halbeek, H., and Dorland, L. (1981) Pure Appl.
7107587	9	68	with	type	1044:1047	arg1	assignments					1114:1124	the previously reported peak assignments	1085:1124	the previously reported peak assignments (Vliegenthart, J. F. G., van Halbeek, H., and Dorland, L. (1981) Pure Appl	1085:1199	Our results indicate that fibrinogen glycopeptides are of the biantennary type, and are in complete agreement with the previously reported peak assignments (Vliegenthart, J. F. G., van Halbeek, H., and Dorland, L. (1981) Pure Appl.
7107587	9	68	with	type	1044:1047	arg1	H.					1164:1165	H.	1164:1165	H.	1164:1165	Our results indicate that fibrinogen glycopeptides are of the biantennary type, and are in complete agreement with the previously reported peak assignments (Vliegenthart, J. F. G., van Halbeek, H., and Dorland, L. (1981) Pure Appl.
7107587	9	68	with	type	1044:1047	arg1	Dorland					1172:1178	Dorland	1172:1178	Dorland	1172:1178	Our results indicate that fibrinogen glycopeptides are of the biantennary type, and are in complete agreement with the previously reported peak assignments (Vliegenthart, J. F. G., van Halbeek, H., and Dorland, L. (1981) Pure Appl.
7107587	12	69	theme	concanavalin	1269:1280	arg1	A-Sepharose					1282:1292	concanavalin A-Sepharose	1269:1292	concanavalin A-Sepharose	1269:1292	Affinity chromatography of the glycopeptides on concanavalin A-Sepharose also showed that the glycopeptides from fibrinogen are greater than 95% biantennary oligosaccharide chains.
7107587	7	70	theme	selective	792:800	arg1	removal					802:808	selective removal	792:808	selective removal of sugar residues	792:826	The glycopeptides resulting from exoglycosidase digestions were examined with 300-MHz 1H-NMR spectroscopy, and the changes in the signals caused by selective removal of sugar residues were studied.
7107587	13	71	theme	chromatography-mass	1503:1521	arg1	spectrometry					1523:1534	gas chromatography-mass spectrometry	1499:1534	gas chromatography-mass spectrometry	1499:1534	Based on carbohydrate composition, 1H-NMR spectroscopy, sequential exoglycosidase digestion, and gas chromatography-mass spectrometry of derived partially methylated alditol acetates, we propose that fibrinogen contains four oligosaccharide chains of the structure shown below.
7107587	1	72	theme	glycosidase-treated	82:100	arg1	glycopeptides					102:114	glycosidase-treated glycopeptides	82:114	glycosidase-treated glycopeptides	82:114	Use of 300-MHz 1H-NMR to characterize glycosidase-treated glycopeptides.
7107587	8	73	theme	corresponding	906:918	arg1	unit					935:938	the corresponding monosaccharide unit	902:938	the corresponding monosaccharide unit independent of previous work	902:967	This technique enabled us to assign each anomeric proton to the corresponding monosaccharide unit independent of previous work.
7107587	0	74	theme	human	26:30	arg1	fibrinogen					32:41	human fibrinogen	26:41	human fibrinogen	26:41	Carbohydrate structure of human fibrinogen.
7107587	12	75	theme	glycopeptides	1252:1264	arg1	chromatography					1230:1243	Affinity chromatography	1221:1243	Affinity chromatography of the glycopeptides on concanavalin A-Sepharose	1221:1292	Affinity chromatography of the glycopeptides on concanavalin A-Sepharose also showed that the glycopeptides from fibrinogen are greater than 95% biantennary oligosaccharide chains.
7107587	7	76	theme	residues	819:826	arg1	removal					802:808	selective removal	792:808	selective removal of sugar residues	792:826	The glycopeptides resulting from exoglycosidase digestions were examined with 300-MHz 1H-NMR spectroscopy, and the changes in the signals caused by selective removal of sugar residues were studied.
7107587	5	77	from	digestion	457:465	arg1	G-50					509:512	Sephadex G-50	500:512	Sephadex G-50	500:512	Glycopeptides were prepared from fibrinogen, B beta, and gamma chains by pronase digestion and subsequent chromatography on Sephadex G-50.
7107587	8	78	theme	work	964:967	arg1	independent					940:950	independent	940:950	independent	940:950	This technique enabled us to assign each anomeric proton to the corresponding monosaccharide unit independent of previous work.
7107587	12	79	dep	%	1364:1364	arg1	95					1362:1363	95	1362:1363	95	1362:1363	Affinity chromatography of the glycopeptides on concanavalin A-Sepharose also showed that the glycopeptides from fibrinogen are greater than 95% biantennary oligosaccharide chains.
7107587	5	80	theme	gamma	433:437	arg1	chains					439:444	gamma chains	433:444	gamma chains	433:444	Glycopeptides were prepared from fibrinogen, B beta, and gamma chains by pronase digestion and subsequent chromatography on Sephadex G-50.
7107587	12	81	theme	Affinity	1221:1228	arg1	chromatography					1230:1243	Affinity chromatography	1221:1243	Affinity chromatography of the glycopeptides on concanavalin A-Sepharose	1221:1292	Affinity chromatography of the glycopeptides on concanavalin A-Sepharose also showed that the glycopeptides from fibrinogen are greater than 95% biantennary oligosaccharide chains.
7107587	13	82	theme	sequential	1458:1467	arg1	digestion					1484:1492	sequential exoglycosidase digestion	1458:1492	sequential exoglycosidase digestion	1458:1492	Based on carbohydrate composition, 1H-NMR spectroscopy, sequential exoglycosidase digestion, and gas chromatography-mass spectrometry of derived partially methylated alditol acetates, we propose that fibrinogen contains four oligosaccharide chains of the structure shown below.
7107587	8	83	theme	monosaccharide	920:933	arg1	unit					935:938	the corresponding monosaccharide unit	902:938	the corresponding monosaccharide unit independent of previous work	902:967	This technique enabled us to assign each anomeric proton to the corresponding monosaccharide unit independent of previous work.
7107587	4	84	theme	alpha	324:328	arg1	devoid					352:357	devoid	352:357	devoid	352:357	The A alpha chain was found to be devoid of carbohydrate.
7107587	4	84	theme	alpha	324:328	arg1	chain					330:334	The A alpha chain	318:334	The A alpha chain	318:334	The A alpha chain was found to be devoid of carbohydrate.
7107587	2	85	theme	fibrinogen	149:158	arg1	composition					134:144	The carbohydrate composition	117:144	The carbohydrate composition of fibrinogen and constituent S-carboxymethylated chains	117:201	The carbohydrate composition of fibrinogen and constituent S-carboxymethylated chains was determined.
7107587	13	86	theme	carbohydrate	1411:1422	arg1	composition					1424:1434	carbohydrate composition	1411:1434	carbohydrate composition	1411:1434	Based on carbohydrate composition, 1H-NMR spectroscopy, sequential exoglycosidase digestion, and gas chromatography-mass spectrometry of derived partially methylated alditol acetates, we propose that fibrinogen contains four oligosaccharide chains of the structure shown below.
7107587	5	87	theme	B	421:421	arg1	beta					423:426	B beta	421:426	B beta	421:426	Glycopeptides were prepared from fibrinogen, B beta, and gamma chains by pronase digestion and subsequent chromatography on Sephadex G-50.
7309709	5	0	theme	sugar	623:627	arg1	chains					629:634	the asparagine-linked sugar chains	601:634	the asparagine-linked sugar chains of human prothrombin	601:655	By the combination of sequential exoglycosidase digestion and methylation analysis, the structures of the asparagine-linked sugar chains of human prothrombin were confirmed to be as follows: (sequence in text).
7309709	0	1	theme	prothrombin	62:72	arg1	moiety					46:51	the carbohydrate moiety	29:51	the carbohydrate moiety of human prothrombin	29:72	Studies on the structures of the carbohydrate moiety of human prothrombin.
7309709	0	2	from	Studies	0:6	arg1	structures					15:24	the structures	11:24	the structures of the carbohydrate moiety of human prothrombin	11:72	Studies on the structures of the carbohydrate moiety of human prothrombin.
7309709	5	3	theme	analysis	573:580	arg1	combination					506:516	the combination	502:516	the combination of sequential exoglycosidase digestion and methylation analysis	502:580	By the combination of sequential exoglycosidase digestion and methylation analysis, the structures of the asparagine-linked sugar chains of human prothrombin were confirmed to be as follows: (sequence in text).
7309709	4	4	theme	sialidase	464:472	arg1	digestion					474:482	sialidase digestion	464:482	sialidase digestion	464:482	The neutral oligosaccharides obtained from all acidic oligosaccharides by sialidase digestion are identical.
7309709	2	5	from	moiety	256:261	arg1	oligosaccharides					218:233	radioactive oligosaccharides	206:233	radioactive oligosaccharides from the polypeptide moiety	206:261	The sugar chains were quantitatively liberated as radioactive oligosaccharides from the polypeptide moiety by hydrazinolysis followed by N-acetylation and Nab3H4 reduction.
7309709	0	6	theme	human	56:60	arg1	prothrombin					62:72	human prothrombin	56:72	human prothrombin	56:72	Studies on the structures of the carbohydrate moiety of human prothrombin.
7309709	1	7	theme	Human	75:79	arg1	prothrombin					81:91	Human prothrombin	75:91	Human prothrombin	75:91	Human prothrombin contains three asparagine-linked sugar chains in one molecule.
7309709	5	8	link	asparagine-linked	605:621	arg1	chains					629:634	the asparagine-linked sugar chains	601:634	the asparagine-linked sugar chains of human prothrombin	601:655	By the combination of sequential exoglycosidase digestion and methylation analysis, the structures of the asparagine-linked sugar chains of human prothrombin were confirmed to be as follows: (sequence in text).
7309709	4	9	theme	acidic	437:442	arg1	oligosaccharides					444:459	all acidic oligosaccharides	433:459	all acidic oligosaccharides	433:459	The neutral oligosaccharides obtained from all acidic oligosaccharides by sialidase digestion are identical.
7309709	5	10	theme	exoglycosidase	532:545	arg1	digestion					547:555	sequential exoglycosidase digestion	521:555	sequential exoglycosidase digestion	521:555	By the combination of sequential exoglycosidase digestion and methylation analysis, the structures of the asparagine-linked sugar chains of human prothrombin were confirmed to be as follows: (sequence in text).
7309709	5	11	theme	digestion	547:555	arg1	combination					506:516	the combination	502:516	the combination of sequential exoglycosidase digestion and methylation analysis	502:580	By the combination of sequential exoglycosidase digestion and methylation analysis, the structures of the asparagine-linked sugar chains of human prothrombin were confirmed to be as follows: (sequence in text).
7309709	5	12	from	sequence	691:698	arg1	text					703:706	text	703:706	text	703:706	By the combination of sequential exoglycosidase digestion and methylation analysis, the structures of the asparagine-linked sugar chains of human prothrombin were confirmed to be as follows: (sequence in text).
7309709	5	13	theme	methylation	561:571	arg1	analysis					573:580	methylation analysis	561:580	methylation analysis	561:580	By the combination of sequential exoglycosidase digestion and methylation analysis, the structures of the asparagine-linked sugar chains of human prothrombin were confirmed to be as follows: (sequence in text).
7309709	2	14	theme	polypeptide	244:254	arg1	moiety					256:261	the polypeptide moiety	240:261	the polypeptide moiety	240:261	The sugar chains were quantitatively liberated as radioactive oligosaccharides from the polypeptide moiety by hydrazinolysis followed by N-acetylation and Nab3H4 reduction.
7309709	5	15	theme	chains	629:634	arg1	structures					587:596	the structures	583:596	the structures of the asparagine-linked sugar chains of human prothrombin	583:655	By the combination of sequential exoglycosidase digestion and methylation analysis, the structures of the asparagine-linked sugar chains of human prothrombin were confirmed to be as follows: (sequence in text).
7309709	0	16	theme	moiety	46:51	arg1	structures					15:24	the structures	11:24	the structures of the carbohydrate moiety of human prothrombin	11:72	Studies on the structures of the carbohydrate moiety of human prothrombin.
7309709	1	17	contain	contains	93:100	arg1	prothrombin					81:91	Human prothrombin	75:91	Human prothrombin	75:91	Human prothrombin contains three asparagine-linked sugar chains in one molecule.
7309709	1	17	contain	contains	93:100	arg2	prothrombin					81:91	Human prothrombin	75:91	Human prothrombin	75:91	Human prothrombin contains three asparagine-linked sugar chains in one molecule.
7309709	1	17	contain	contains	93:100	arg1	molecule					146:153	one molecule	142:153	one molecule	142:153	Human prothrombin contains three asparagine-linked sugar chains in one molecule.
7309709	1	17	contain	contains	93:100	arg2	chains					132:137	three asparagine-linked sugar chains	102:137	three asparagine-linked sugar chains	102:137	Human prothrombin contains three asparagine-linked sugar chains in one molecule.
7309709	2	18	theme	sugar	160:164	arg1	chains					166:171	The sugar chains	156:171	The sugar chains	156:171	The sugar chains were quantitatively liberated as radioactive oligosaccharides from the polypeptide moiety by hydrazinolysis followed by N-acetylation and Nab3H4 reduction.
7309709	1	19	theme	asparagine-linked	108:124	arg1	chains					132:137	three asparagine-linked sugar chains	102:137	three asparagine-linked sugar chains	102:137	Human prothrombin contains three asparagine-linked sugar chains in one molecule.
7309709	0	20	theme	carbohydrate	33:44	arg1	moiety					46:51	the carbohydrate moiety	29:51	the carbohydrate moiety of human prothrombin	29:72	Studies on the structures of the carbohydrate moiety of human prothrombin.
7309709	5	21	theme	human	639:643	arg1	prothrombin					645:655	human prothrombin	639:655	human prothrombin	639:655	By the combination of sequential exoglycosidase digestion and methylation analysis, the structures of the asparagine-linked sugar chains of human prothrombin were confirmed to be as follows: (sequence in text).
7309709	1	22	theme	sugar	126:130	arg1	chains					132:137	three asparagine-linked sugar chains	102:137	three asparagine-linked sugar chains	102:137	Human prothrombin contains three asparagine-linked sugar chains in one molecule.
7309709	1	23	link	asparagine-linked	108:124	arg1	chains					132:137	three asparagine-linked sugar chains	102:137	three asparagine-linked sugar chains	102:137	Human prothrombin contains three asparagine-linked sugar chains in one molecule.
7309709	2	24	theme	radioactive	206:216	arg1	oligosaccharides					218:233	radioactive oligosaccharides	206:233	radioactive oligosaccharides from the polypeptide moiety	206:261	The sugar chains were quantitatively liberated as radioactive oligosaccharides from the polypeptide moiety by hydrazinolysis followed by N-acetylation and Nab3H4 reduction.
7309709	4	25	theme	neutral	394:400	arg1	identical					488:496	identical	488:496	identical	488:496	The neutral oligosaccharides obtained from all acidic oligosaccharides by sialidase digestion are identical.
7309709	4	25	theme	neutral	394:400	arg1	oligosaccharides					402:417	The neutral oligosaccharides	390:417	The neutral oligosaccharides obtained from all acidic oligosaccharides by sialidase digestion	390:482	The neutral oligosaccharides obtained from all acidic oligosaccharides by sialidase digestion are identical.
7309709	5	26	theme	prothrombin	645:655	arg1	chains					629:634	the asparagine-linked sugar chains	601:634	the asparagine-linked sugar chains of human prothrombin	601:655	By the combination of sequential exoglycosidase digestion and methylation analysis, the structures of the asparagine-linked sugar chains of human prothrombin were confirmed to be as follows: (sequence in text).
7309709	3	27	contain	contain	357:363	arg1	All					329:331	All	329:331	All	329:331	All of the oligosaccharides contain N-acetylneuraminic acid.
7309709	3	27	contain	contain	357:363	arg1	oligosaccharides					340:355	the oligosaccharides	336:355	the oligosaccharides	336:355	All of the oligosaccharides contain N-acetylneuraminic acid.
7309709	3	27	contain	contain	357:363	arg2	acid					384:387	N-acetylneuraminic acid	365:387	N-acetylneuraminic acid	365:387	All of the oligosaccharides contain N-acetylneuraminic acid.
7309709	3	28	theme	N-acetylneuraminic	365:382	arg1	acid					384:387	N-acetylneuraminic acid	365:387	N-acetylneuraminic acid	365:387	All of the oligosaccharides contain N-acetylneuraminic acid.
7309709	5	29	theme	sequential	521:530	arg1	digestion					547:555	sequential exoglycosidase digestion	521:555	sequential exoglycosidase digestion	521:555	By the combination of sequential exoglycosidase digestion and methylation analysis, the structures of the asparagine-linked sugar chains of human prothrombin were confirmed to be as follows: (sequence in text).
7309709	5	30	theme	asparagine-linked	605:621	arg1	chains					629:634	the asparagine-linked sugar chains	601:634	the asparagine-linked sugar chains of human prothrombin	601:655	By the combination of sequential exoglycosidase digestion and methylation analysis, the structures of the asparagine-linked sugar chains of human prothrombin were confirmed to be as follows: (sequence in text).
7309709	2	31	dep	N-acetylation	293:305	arg1	reduction					318:326	reduction	318:326	reduction	318:326	The sugar chains were quantitatively liberated as radioactive oligosaccharides from the polypeptide moiety by hydrazinolysis followed by N-acetylation and Nab3H4 reduction.
7462199	0	0	theme	human	80:84	arg1	plasma					86:91	human plasma	80:91	human plasma	80:91	Structural studies of the sugar chains of cold-insoluble globulin isolated from human plasma.
7462199	4	1	theme	oligosaccharides	518:533	arg1	%					497:497	More than 90%	485:497	More than 90% of the radioactive oligosaccharides	485:533	More than 90% of the radioactive oligosaccharides contain N-acetylneuraminic acid, and could be separated into two acidic oligosaccharides, A-1 and A-2.
7462199	4	1	theme	oligosaccharides	518:533	arg1	oligosaccharides					518:533	the radioactive oligosaccharides	502:533	the radioactive oligosaccharides	502:533	More than 90% of the radioactive oligosaccharides contain N-acetylneuraminic acid, and could be separated into two acidic oligosaccharides, A-1 and A-2.
7462199	5	2	theme	2Man	798:801	arg1	alpha					803:807	2Man alpha 1	798:809	2Man alpha 1	798:809	By sequential exoglycosidase digestion in combination with methylation studies, their structures were elucidated as Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6 (NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2 Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc.
7462199	5	3	dep	6	1061:1061	arg1	leads					1078:1082	leads	1078:1082	leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2 Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc	1078:1208	By sequential exoglycosidase digestion in combination with methylation studies, their structures were elucidated as Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6 (NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2 Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc.
7462199	5	4	theme	methylation	697:707	arg1	studies					709:715	methylation studies	697:715	methylation studies	697:715	By sequential exoglycosidase digestion in combination with methylation studies, their structures were elucidated as Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6 (NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2 Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc.
7462199	5	5	dep	Man	1134:1136	arg1	leads					1146:1150	leads	1146:1150	leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc	1146:1208	By sequential exoglycosidase digestion in combination with methylation studies, their structures were elucidated as Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6 (NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2 Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc.
7462199	1	6	theme	human	170:174	arg1	plasma					176:181	human plasma	170:181	human plasma	170:181	The asparagine-linked sugar chains of cold-insoluble globulin isolated from human plasma were released as oligosaccharides from the polypeptide moiety by hydrazinolysis.
7462199	3	7	theme	radioactive	367:377	arg1	oligosaccharides					379:394	radioactive oligosaccharides	367:394	radioactive oligosaccharides	367:394	The yield of radioactive oligosaccharides indicated that the glycoprotein has four asparagine-linked sugar chains in one molecule.
7462199	4	8	theme	N-acetylneuraminic	543:560	arg1	acid					562:565	N-acetylneuraminic acid	543:565	N-acetylneuraminic acid	543:565	More than 90% of the radioactive oligosaccharides contain N-acetylneuraminic acid, and could be separated into two acidic oligosaccharides, A-1 and A-2.
7462199	4	9	contain	contain	535:541	arg2	acid					562:565	N-acetylneuraminic acid	543:565	N-acetylneuraminic acid	543:565	More than 90% of the radioactive oligosaccharides contain N-acetylneuraminic acid, and could be separated into two acidic oligosaccharides, A-1 and A-2.
7462199	4	9	contain	contain	535:541	arg1	%					497:497	More than 90%	485:497	More than 90% of the radioactive oligosaccharides	485:533	More than 90% of the radioactive oligosaccharides contain N-acetylneuraminic acid, and could be separated into two acidic oligosaccharides, A-1 and A-2.
7462199	4	9	contain	contain	535:541	arg1	oligosaccharides					518:533	the radioactive oligosaccharides	502:533	the radioactive oligosaccharides	502:533	More than 90% of the radioactive oligosaccharides contain N-acetylneuraminic acid, and could be separated into two acidic oligosaccharides, A-1 and A-2.
7462199	3	10	contain	has	428:430	arg2	chains					461:466	four asparagine-linked sugar chains	432:466	four asparagine-linked sugar chains	432:466	The yield of radioactive oligosaccharides indicated that the glycoprotein has four asparagine-linked sugar chains in one molecule.
7462199	3	10	contain	has	428:430	arg1	glycoprotein					415:426	the glycoprotein	411:426	the glycoprotein	411:426	The yield of radioactive oligosaccharides indicated that the glycoprotein has four asparagine-linked sugar chains in one molecule.
7462199	5	11	theme	Man	915:917	arg1	beta					919:922	Man beta 1	915:924	3) Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc	912:965	By sequential exoglycosidase digestion in combination with methylation studies, their structures were elucidated as Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6 (NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2 Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc.
7462199	3	12	theme	oligosaccharides	379:394	arg1	yield					358:362	The yield	354:362	The yield of radioactive oligosaccharides	354:394	The yield of radioactive oligosaccharides indicated that the glycoprotein has four asparagine-linked sugar chains in one molecule.
7462199	1	13	attach	isolated	156:163	arg1	plasma					176:181	human plasma	170:181	human plasma	170:181	The asparagine-linked sugar chains of cold-insoluble globulin isolated from human plasma were released as oligosaccharides from the polypeptide moiety by hydrazinolysis.
7462199	1	13	attach	isolated	156:163	arg2	globulin					147:154	cold-insoluble globulin	132:154	cold-insoluble globulin isolated from human plasma	132:181	The asparagine-linked sugar chains of cold-insoluble globulin isolated from human plasma were released as oligosaccharides from the polypeptide moiety by hydrazinolysis.
7462199	5	14	dep	beta	919:922	arg1	3					912:912	3	912:912	3	912:912	By sequential exoglycosidase digestion in combination with methylation studies, their structures were elucidated as Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6 (NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2 Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc.
7462199	5	14	dep	beta	919:922	arg1	leads					985:989	leads	985:989	leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6 (NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2 Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc	985:1208	By sequential exoglycosidase digestion in combination with methylation studies, their structures were elucidated as Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6 (NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2 Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc.
7462199	5	14	dep	beta	919:922	arg1	leads					926:930	leads	926:930	leads to 4GlcNAc beta 1 leads to 4GlcNAc	926:965	By sequential exoglycosidase digestion in combination with methylation studies, their structures were elucidated as Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6 (NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2 Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc.
7462199	5	15	theme	6Gal	1087:1090	arg1	beta					1092:1095	6Gal beta 1	1087:1097	6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2 Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc	1087:1208	By sequential exoglycosidase digestion in combination with methylation studies, their structures were elucidated as Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6 (NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2 Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc.
7462199	5	16	theme	4GlcNAc	774:780	arg1	beta					782:785	4GlcNAc beta 1	774:787	4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6 (NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2 Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc	774:1208	By sequential exoglycosidase digestion in combination with methylation studies, their structures were elucidated as Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6 (NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2 Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc.
7462199	3	17	gly	glycoprotein	415:426	arg1	glycoprotein					415:426	the glycoprotein	411:426	the glycoprotein	411:426	The yield of radioactive oligosaccharides indicated that the glycoprotein has four asparagine-linked sugar chains in one molecule.
7462199	5	18	theme	sequential	641:650	arg1	digestion					667:675	sequential exoglycosidase digestion	641:675	sequential exoglycosidase digestion in combination with methylation studies	641:715	By sequential exoglycosidase digestion in combination with methylation studies, their structures were elucidated as Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6 (NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2 Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc.
7462199	5	19	theme	-Man	1157:1160	arg1	beta					1162:1165	3)-Man beta 1	1155:1167	3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc	1155:1208	By sequential exoglycosidase digestion in combination with methylation studies, their structures were elucidated as Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6 (NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2 Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc.
7462199	4	20	theme	radioactive	506:516	arg1	oligosaccharides					518:533	the radioactive oligosaccharides	502:533	the radioactive oligosaccharides	502:533	More than 90% of the radioactive oligosaccharides contain N-acetylneuraminic acid, and could be separated into two acidic oligosaccharides, A-1 and A-2.
7462199	3	21	theme	asparagine-linked	437:453	arg1	chains					461:466	four asparagine-linked sugar chains	432:466	four asparagine-linked sugar chains	432:466	The yield of radioactive oligosaccharides indicated that the glycoprotein has four asparagine-linked sugar chains in one molecule.
7462199	5	22	theme	NeuAc	1064:1068	arg1	alpha					1070:1074	NeuAc alpha 2	1064:1076	NeuAc alpha 2	1064:1076	By sequential exoglycosidase digestion in combination with methylation studies, their structures were elucidated as Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6 (NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2 Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc.
7462199	0	23	theme	Structural	0:9	arg1	studies					11:17	Structural studies	0:17	Structural studies of the sugar chains of cold-insoluble globulin	0:64	Structural studies of the sugar chains of cold-insoluble globulin isolated from human plasma.
7462199	5	24	theme	exoglycosidase	652:665	arg1	digestion					667:675	sequential exoglycosidase digestion	641:675	sequential exoglycosidase digestion in combination with methylation studies	641:715	By sequential exoglycosidase digestion in combination with methylation studies, their structures were elucidated as Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6 (NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2 Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc.
7462199	5	25	theme	NeuAc	822:826	arg1	alpha					828:832	NeuAc alpha 2	822:834	NeuAc alpha 2	822:834	By sequential exoglycosidase digestion in combination with methylation studies, their structures were elucidated as Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6 (NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2 Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc.
7462199	5	26	dep	beta	1186:1189	arg1	leads					1193:1197	leads	1193:1197	leads to 4GlcNAc	1193:1208	By sequential exoglycosidase digestion in combination with methylation studies, their structures were elucidated as Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6 (NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2 Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc.
7462199	5	27	dep	beta	943:946	arg1	leads					950:954	leads	950:954	leads to 4GlcNAc	950:965	By sequential exoglycosidase digestion in combination with methylation studies, their structures were elucidated as Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6 (NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2 Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc.
7462199	4	28	theme	acidic	600:605	arg1	A-1					625:627	A-1	625:627	A-1	625:627	More than 90% of the radioactive oligosaccharides contain N-acetylneuraminic acid, and could be separated into two acidic oligosaccharides, A-1 and A-2.
7462199	4	28	theme	acidic	600:605	arg1	oligosaccharides					607:622	two acidic oligosaccharides	596:622	two acidic oligosaccharides	596:622	More than 90% of the radioactive oligosaccharides contain N-acetylneuraminic acid, and could be separated into two acidic oligosaccharides, A-1 and A-2.
7462199	4	28	theme	acidic	600:605	arg1	A-2					633:635	A-2	633:635	A-2	633:635	More than 90% of the radioactive oligosaccharides contain N-acetylneuraminic acid, and could be separated into two acidic oligosaccharides, A-1 and A-2.
7462199	5	29	theme	Gal	754:756	arg1	beta					758:761	Gal beta 1	754:763	Gal beta 1	754:763	By sequential exoglycosidase digestion in combination with methylation studies, their structures were elucidated as Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6 (NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2 Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc.
7462199	5	30	dep	leads	1099:1103	arg1	leads					1123:1127	leads	1123:1127	leads to 2 Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc	1123:1208	By sequential exoglycosidase digestion in combination with methylation studies, their structures were elucidated as Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6 (NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2 Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc.
7462199	1	31	theme	asparagine-linked	98:114	arg1	chains					122:127	The asparagine-linked sugar chains	94:127	The asparagine-linked sugar chains of cold-insoluble globulin isolated from human plasma	94:181	The asparagine-linked sugar chains of cold-insoluble globulin isolated from human plasma were released as oligosaccharides from the polypeptide moiety by hydrazinolysis.
7462199	1	31	theme	asparagine-linked	98:114	arg1	oligosaccharides					200:215	oligosaccharides	200:215	oligosaccharides from the polypeptide moiety	200:243	The asparagine-linked sugar chains of cold-insoluble globulin isolated from human plasma were released as oligosaccharides from the polypeptide moiety by hydrazinolysis.
7462199	5	32	theme	4GlcNAc	866:872	arg1	beta					874:877	4GlcNAc beta 1	866:879	4GlcNAc beta 1	866:879	By sequential exoglycosidase digestion in combination with methylation studies, their structures were elucidated as Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6 (NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2 Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc.
7462199	0	33	theme	chains	32:37	arg1	studies					11:17	Structural studies	0:17	Structural studies of the sugar chains of cold-insoluble globulin	0:64	Structural studies of the sugar chains of cold-insoluble globulin isolated from human plasma.
7462199	5	34	from	digestion	667:675	arg1	combination					680:690	combination	680:690	combination with methylation studies	680:715	By sequential exoglycosidase digestion in combination with methylation studies, their structures were elucidated as Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6 (NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2 Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc.
7462199	5	35	theme	6Gal	994:997	arg1	beta					999:1002	6Gal beta 1	994:1004	6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6 (NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2 Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc	994:1208	By sequential exoglycosidase digestion in combination with methylation studies, their structures were elucidated as Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6 (NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2 Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc.
7462199	5	36	with	combination	680:690	arg1	studies					709:715	methylation studies	697:715	methylation studies	697:715	By sequential exoglycosidase digestion in combination with methylation studies, their structures were elucidated as Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6 (NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2 Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc.
7462199	3	37	theme	sugar	455:459	arg1	chains					461:466	four asparagine-linked sugar chains	432:466	four asparagine-linked sugar chains	432:466	The yield of radioactive oligosaccharides indicated that the glycoprotein has four asparagine-linked sugar chains in one molecule.
7462199	0	38	theme	sugar	26:30	arg1	chains					32:37	the sugar chains	22:37	the sugar chains of cold-insoluble globulin	22:64	Structural studies of the sugar chains of cold-insoluble globulin isolated from human plasma.
7462199	5	39	dep	beta	1092:1095	arg1	leads					1099:1103	leads	1099:1103	leads to 4GlcNAc beta 1	1099:1121	By sequential exoglycosidase digestion in combination with methylation studies, their structures were elucidated as Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6 (NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2 Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc.
7462199	5	40	dep	beta	1162:1165	arg1	leads					1169:1173	leads	1169:1173	leads to 4GlcNAc beta 1 leads to 4GlcNAc	1169:1208	By sequential exoglycosidase digestion in combination with methylation studies, their structures were elucidated as Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6 (NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2 Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc.
7462199	5	40	dep	beta	1162:1165	arg1	3					1155:1155	3	1155:1155	3	1155:1155	By sequential exoglycosidase digestion in combination with methylation studies, their structures were elucidated as Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6 (NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2 Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc.
7462199	1	41	theme	polypeptide	226:236	arg1	moiety					238:243	the polypeptide moiety	222:243	the polypeptide moiety	222:243	The asparagine-linked sugar chains of cold-insoluble globulin isolated from human plasma were released as oligosaccharides from the polypeptide moiety by hydrazinolysis.
7462199	0	42	theme	cold-insoluble	42:55	arg1	globulin					57:64	cold-insoluble globulin	42:64	cold-insoluble globulin	42:64	Structural studies of the sugar chains of cold-insoluble globulin isolated from human plasma.
7462199	0	43	theme	globulin	57:64	arg1	chains					32:37	the sugar chains	22:37	the sugar chains of cold-insoluble globulin	22:64	Structural studies of the sugar chains of cold-insoluble globulin isolated from human plasma.
7462199	3	44	link	asparagine-linked	437:453	arg1	chains					461:466	four asparagine-linked sugar chains	432:466	four asparagine-linked sugar chains	432:466	The yield of radioactive oligosaccharides indicated that the glycoprotein has four asparagine-linked sugar chains in one molecule.
7462199	5	45	theme	4GlcNAc	1015:1021	arg1	beta					1023:1026	4GlcNAc beta 1	1015:1028	4GlcNAc beta 1	1015:1028	By sequential exoglycosidase digestion in combination with methylation studies, their structures were elucidated as Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6 (NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2 Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc.
7462199	1	46	theme	sugar	116:120	arg1	chains					122:127	The asparagine-linked sugar chains	94:127	The asparagine-linked sugar chains of cold-insoluble globulin isolated from human plasma	94:181	The asparagine-linked sugar chains of cold-insoluble globulin isolated from human plasma were released as oligosaccharides from the polypeptide moiety by hydrazinolysis.
7462199	1	46	theme	sugar	116:120	arg1	oligosaccharides					200:215	oligosaccharides	200:215	oligosaccharides from the polypeptide moiety	200:243	The asparagine-linked sugar chains of cold-insoluble globulin isolated from human plasma were released as oligosaccharides from the polypeptide moiety by hydrazinolysis.
7462199	5	47	theme	2Man	1039:1042	arg1	alpha					1044:1048	2Man alpha 1	1039:1050	2Man alpha 1	1039:1050	By sequential exoglycosidase digestion in combination with methylation studies, their structures were elucidated as Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6 (NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2 Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc.
7462199	5	48	dep	beta	850:853	arg1	leads					903:907	leads	903:907	leads to 3) Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6 (NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2 Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc	903:1208	By sequential exoglycosidase digestion in combination with methylation studies, their structures were elucidated as Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6 (NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2 Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc.
7462199	5	48	dep	beta	850:853	arg1	leads					881:885	leads	881:885	leads to 2Man alpha 1	881:901	By sequential exoglycosidase digestion in combination with methylation studies, their structures were elucidated as Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6 (NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2 Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc.
7462199	5	48	dep	beta	850:853	arg1	leads					857:861	leads	857:861	leads to 4GlcNAc beta 1	857:879	By sequential exoglycosidase digestion in combination with methylation studies, their structures were elucidated as Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6 (NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2 Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc.
7462199	5	49	dep	beta	782:785	arg1	leads					811:815	leads	811:815	leads to 6	811:820	By sequential exoglycosidase digestion in combination with methylation studies, their structures were elucidated as Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6 (NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2 Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc.
7462199	5	49	dep	beta	782:785	arg1	leads					789:793	leads	789:793	leads to 2Man alpha 1	789:809	By sequential exoglycosidase digestion in combination with methylation studies, their structures were elucidated as Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6 (NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2 Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc.
7462199	5	49	dep	beta	782:785	arg1	leads					836:840	leads	836:840	leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6 (NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2 Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc	836:1208	By sequential exoglycosidase digestion in combination with methylation studies, their structures were elucidated as Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6 (NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2 Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc.
7462199	5	50	theme	NeuAc	971:975	arg1	alpha					977:981	NeuAc alpha 2	971:983	NeuAc alpha 2	971:983	By sequential exoglycosidase digestion in combination with methylation studies, their structures were elucidated as Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6 (NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2 Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc.
7462199	5	51	theme	2Man	890:893	arg1	alpha					895:899	2Man alpha 1	890:901	2Man alpha 1	890:901	By sequential exoglycosidase digestion in combination with methylation studies, their structures were elucidated as Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6 (NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2 Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc.
7462199	1	52	from	moiety	238:243	arg1	chains					122:127	The asparagine-linked sugar chains	94:127	The asparagine-linked sugar chains of cold-insoluble globulin isolated from human plasma	94:181	The asparagine-linked sugar chains of cold-insoluble globulin isolated from human plasma were released as oligosaccharides from the polypeptide moiety by hydrazinolysis.
7462199	1	52	from	moiety	238:243	arg1	oligosaccharides					200:215	oligosaccharides	200:215	oligosaccharides from the polypeptide moiety	200:243	The asparagine-linked sugar chains of cold-insoluble globulin isolated from human plasma were released as oligosaccharides from the polypeptide moiety by hydrazinolysis.
7462199	5	53	dep	beta	999:1002	arg1	leads					1052:1056	leads	1052:1056	leads to 6 (NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2 Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc	1052:1208	By sequential exoglycosidase digestion in combination with methylation studies, their structures were elucidated as Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6 (NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2 Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc.
7462199	5	53	dep	beta	999:1002	arg1	leads					1030:1034	leads	1030:1034	leads to 2Man alpha 1	1030:1050	By sequential exoglycosidase digestion in combination with methylation studies, their structures were elucidated as Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6 (NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2 Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc.
7462199	5	53	dep	beta	999:1002	arg1	leads					1006:1010	leads	1006:1010	leads to 4GlcNAc beta 1	1006:1028	By sequential exoglycosidase digestion in combination with methylation studies, their structures were elucidated as Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6 (NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2 Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc.
7462199	5	54	theme	4GlcNAc	935:941	arg1	beta					943:946	4GlcNAc beta 1	935:948	4GlcNAc beta 1 leads to 4GlcNAc	935:965	By sequential exoglycosidase digestion in combination with methylation studies, their structures were elucidated as Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6 (NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2 Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc.
7462199	1	55	theme	cold-insoluble	132:145	arg1	globulin					147:154	cold-insoluble globulin	132:154	cold-insoluble globulin isolated from human plasma	132:181	The asparagine-linked sugar chains of cold-insoluble globulin isolated from human plasma were released as oligosaccharides from the polypeptide moiety by hydrazinolysis.
7462199	5	56	theme	6Gal	845:848	arg1	beta					850:853	6Gal beta 1	845:855	6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6 (NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2 Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc	845:1208	By sequential exoglycosidase digestion in combination with methylation studies, their structures were elucidated as Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6 (NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2 Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc.
7462199	1	57	theme	globulin	147:154	arg1	chains					122:127	The asparagine-linked sugar chains	94:127	The asparagine-linked sugar chains of cold-insoluble globulin isolated from human plasma	94:181	The asparagine-linked sugar chains of cold-insoluble globulin isolated from human plasma were released as oligosaccharides from the polypeptide moiety by hydrazinolysis.
7462199	1	57	theme	globulin	147:154	arg1	oligosaccharides					200:215	oligosaccharides	200:215	oligosaccharides from the polypeptide moiety	200:243	The asparagine-linked sugar chains of cold-insoluble globulin isolated from human plasma were released as oligosaccharides from the polypeptide moiety by hydrazinolysis.
7462199	1	58	link	asparagine-linked	98:114	arg1	chains					122:127	The asparagine-linked sugar chains	94:127	The asparagine-linked sugar chains of cold-insoluble globulin isolated from human plasma	94:181	The asparagine-linked sugar chains of cold-insoluble globulin isolated from human plasma were released as oligosaccharides from the polypeptide moiety by hydrazinolysis.
7462199	1	58	link	asparagine-linked	98:114	arg1	oligosaccharides					200:215	oligosaccharides	200:215	oligosaccharides from the polypeptide moiety	200:243	The asparagine-linked sugar chains of cold-insoluble globulin isolated from human plasma were released as oligosaccharides from the polypeptide moiety by hydrazinolysis.
7462199	5	59	theme	4GlcNAc	1178:1184	arg1	beta					1186:1189	4GlcNAc beta 1	1178:1191	4GlcNAc beta 1 leads to 4GlcNAc	1178:1208	By sequential exoglycosidase digestion in combination with methylation studies, their structures were elucidated as Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6 (NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2 Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc.
7462199	5	60	theme	4GlcNAc	1108:1114	arg1	beta					1116:1119	4GlcNAc beta 1	1108:1121	4GlcNAc beta 1	1108:1121	By sequential exoglycosidase digestion in combination with methylation studies, their structures were elucidated as Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6 (NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2 Man alpha 1 leads to 3)-Man beta 1 leads to 4GlcNAc beta 1 leads to 4GlcNAc.
2390069	3	0	theme	human	376:380	arg1	lactotransferrin					387:402	human milk lactotransferrin	376:402	human milk lactotransferrin	376:402	A comparative analysis of the molar carbohydrate compositions of human leucocyte lactotransferrin and human milk lactotransferrin reveals that the glycans of leucocyte lactotransferrin differ essentially by the absence of fucose residues.
2390069	3	1	theme	milk	382:385	arg1	lactotransferrin					387:402	human milk lactotransferrin	376:402	human milk lactotransferrin	376:402	A comparative analysis of the molar carbohydrate compositions of human leucocyte lactotransferrin and human milk lactotransferrin reveals that the glycans of leucocyte lactotransferrin differ essentially by the absence of fucose residues.
2390069	4	2	theme	alditols	627:634	arg1	spectrometry					595:606	400 MHz 1H-n.m.r. spectrometry	577:606	400 MHz 1H-n.m.r. spectrometry of oligosaccharide alditols released from human leucocyte lactotransferrin	577:681	Structural analysis combining methylation-mass spectrometry and 400 MHz 1H-n.m.r. spectrometry of oligosaccharide alditols released from human leucocyte lactotransferrin shows the presence of two disialylated and non-fucosylated biantennary glycans of the N-acetyl-lactosaminic type.
2390069	4	2	theme	alditols	627:634	arg1	spectrometry					560:571	methylation-mass spectrometry	543:571	methylation-mass spectrometry	543:571	Structural analysis combining methylation-mass spectrometry and 400 MHz 1H-n.m.r. spectrometry of oligosaccharide alditols released from human leucocyte lactotransferrin shows the presence of two disialylated and non-fucosylated biantennary glycans of the N-acetyl-lactosaminic type.
2390069	4	3	theme	Structural	513:522	arg1	analysis					524:531	Structural analysis	513:531	Structural analysis combining methylation-mass spectrometry and 400 MHz 1H-n.m.r. spectrometry of oligosaccharide alditols released from human leucocyte lactotransferrin	513:681	Structural analysis combining methylation-mass spectrometry and 400 MHz 1H-n.m.r. spectrometry of oligosaccharide alditols released from human leucocyte lactotransferrin shows the presence of two disialylated and non-fucosylated biantennary glycans of the N-acetyl-lactosaminic type.
2390069	4	4	gly	non-fucosylated	726:740	arg1	glycans					754:760	two disialylated and non-fucosylated biantennary glycans	705:760	two disialylated and non-fucosylated biantennary glycans of the N-acetyl-lactosaminic type	705:794	Structural analysis combining methylation-mass spectrometry and 400 MHz 1H-n.m.r. spectrometry of oligosaccharide alditols released from human leucocyte lactotransferrin shows the presence of two disialylated and non-fucosylated biantennary glycans of the N-acetyl-lactosaminic type.
2390069	5	5	theme	leucocyte	884:892	arg1	lactotransferrin					894:909	the leucocyte lactotransferrin	880:909	the leucocyte lactotransferrin	880:909	These results question a previously proposed mechanism for hyposideraemia in which the leucocyte lactotransferrin was involved and in which the fucose residues played a key role.
2390069	4	6	theme	oligosaccharide	611:625	arg1	alditols					627:634	oligosaccharide alditols	611:634	oligosaccharide alditols released from human leucocyte lactotransferrin	611:681	Structural analysis combining methylation-mass spectrometry and 400 MHz 1H-n.m.r. spectrometry of oligosaccharide alditols released from human leucocyte lactotransferrin shows the presence of two disialylated and non-fucosylated biantennary glycans of the N-acetyl-lactosaminic type.
2390069	4	7	attach	released	636:643	arg2	alditols					627:634	oligosaccharide alditols	611:634	oligosaccharide alditols released from human leucocyte lactotransferrin	611:681	Structural analysis combining methylation-mass spectrometry and 400 MHz 1H-n.m.r. spectrometry of oligosaccharide alditols released from human leucocyte lactotransferrin shows the presence of two disialylated and non-fucosylated biantennary glycans of the N-acetyl-lactosaminic type.
2390069	4	7	attach	released	636:643	arg1	lactotransferrin					666:681	human leucocyte lactotransferrin	650:681	human leucocyte lactotransferrin	650:681	Structural analysis combining methylation-mass spectrometry and 400 MHz 1H-n.m.r. spectrometry of oligosaccharide alditols released from human leucocyte lactotransferrin shows the presence of two disialylated and non-fucosylated biantennary glycans of the N-acetyl-lactosaminic type.
2390069	4	8	theme	disialylated	709:720	arg1	glycans					754:760	two disialylated and non-fucosylated biantennary glycans	705:760	two disialylated and non-fucosylated biantennary glycans of the N-acetyl-lactosaminic type	705:794	Structural analysis combining methylation-mass spectrometry and 400 MHz 1H-n.m.r. spectrometry of oligosaccharide alditols released from human leucocyte lactotransferrin shows the presence of two disialylated and non-fucosylated biantennary glycans of the N-acetyl-lactosaminic type.
2390069	4	9	theme	1H-n.m.r.	585:593	arg1	spectrometry					595:606	400 MHz 1H-n.m.r. spectrometry	577:606	400 MHz 1H-n.m.r. spectrometry of oligosaccharide alditols released from human leucocyte lactotransferrin	577:681	Structural analysis combining methylation-mass spectrometry and 400 MHz 1H-n.m.r. spectrometry of oligosaccharide alditols released from human leucocyte lactotransferrin shows the presence of two disialylated and non-fucosylated biantennary glycans of the N-acetyl-lactosaminic type.
2390069	5	10	theme	key	966:968	arg1	role					970:973	a key role	964:973	a key role	964:973	These results question a previously proposed mechanism for hyposideraemia in which the leucocyte lactotransferrin was involved and in which the fucose residues played a key role.
2390069	4	11	theme	MHz	581:583	arg1	spectrometry					595:606	400 MHz 1H-n.m.r. spectrometry	577:606	400 MHz 1H-n.m.r. spectrometry of oligosaccharide alditols released from human leucocyte lactotransferrin	577:681	Structural analysis combining methylation-mass spectrometry and 400 MHz 1H-n.m.r. spectrometry of oligosaccharide alditols released from human leucocyte lactotransferrin shows the presence of two disialylated and non-fucosylated biantennary glycans of the N-acetyl-lactosaminic type.
2390069	3	12	theme	comparative	276:286	arg1	analysis					288:295	A comparative analysis	274:295	A comparative analysis of the molar carbohydrate compositions of human leucocyte lactotransferrin and human milk lactotransferrin	274:402	A comparative analysis of the molar carbohydrate compositions of human leucocyte lactotransferrin and human milk lactotransferrin reveals that the glycans of leucocyte lactotransferrin differ essentially by the absence of fucose residues.
2390069	1	13	theme	fucose	88:93	arg1	residues					95:102	fucose residues	88:102	fucose residues	88:102	Absence of fucose residues questions the proposed mechanism of hyposideraemia.
2390069	3	14	theme	fucose	496:501	arg1	residues					503:510	fucose residues	496:510	fucose residues	496:510	A comparative analysis of the molar carbohydrate compositions of human leucocyte lactotransferrin and human milk lactotransferrin reveals that the glycans of leucocyte lactotransferrin differ essentially by the absence of fucose residues.
2390069	0	15	theme	Primary	0:6	arg1	structure					8:16	Primary structure	0:16	Primary structure of glycans	0:27	Primary structure of glycans isolated from human leucocyte lactotransferrin.
2390069	4	16	gly	disialylated	709:720	arg1	glycans					754:760	two disialylated and non-fucosylated biantennary glycans	705:760	two disialylated and non-fucosylated biantennary glycans of the N-acetyl-lactosaminic type	705:794	Structural analysis combining methylation-mass spectrometry and 400 MHz 1H-n.m.r. spectrometry of oligosaccharide alditols released from human leucocyte lactotransferrin shows the presence of two disialylated and non-fucosylated biantennary glycans of the N-acetyl-lactosaminic type.
2390069	1	17	theme	residues	95:102	arg1	Absence					77:83	Absence	77:83	Absence of fucose residues	77:102	Absence of fucose residues questions the proposed mechanism of hyposideraemia.
2390069	3	18	theme	residues	503:510	arg1	absence					485:491	the absence	481:491	the absence of fucose residues	481:510	A comparative analysis of the molar carbohydrate compositions of human leucocyte lactotransferrin and human milk lactotransferrin reveals that the glycans of leucocyte lactotransferrin differ essentially by the absence of fucose residues.
2390069	3	19	theme	leucocyte	432:440	arg1	lactotransferrin					442:457	leucocyte lactotransferrin	432:457	leucocyte lactotransferrin	432:457	A comparative analysis of the molar carbohydrate compositions of human leucocyte lactotransferrin and human milk lactotransferrin reveals that the glycans of leucocyte lactotransferrin differ essentially by the absence of fucose residues.
2390069	3	20	theme	compositions	323:334	arg1	analysis					288:295	A comparative analysis	274:295	A comparative analysis of the molar carbohydrate compositions of human leucocyte lactotransferrin and human milk lactotransferrin	274:402	A comparative analysis of the molar carbohydrate compositions of human leucocyte lactotransferrin and human milk lactotransferrin reveals that the glycans of leucocyte lactotransferrin differ essentially by the absence of fucose residues.
2390069	4	21	theme	N-acetyl-lactosaminic	769:789	arg1	type					791:794	the N-acetyl-lactosaminic type	765:794	the N-acetyl-lactosaminic type	765:794	Structural analysis combining methylation-mass spectrometry and 400 MHz 1H-n.m.r. spectrometry of oligosaccharide alditols released from human leucocyte lactotransferrin shows the presence of two disialylated and non-fucosylated biantennary glycans of the N-acetyl-lactosaminic type.
2390069	3	22	theme	lactotransferrin	442:457	arg1	glycans					421:427	the glycans	417:427	the glycans of leucocyte lactotransferrin	417:457	A comparative analysis of the molar carbohydrate compositions of human leucocyte lactotransferrin and human milk lactotransferrin reveals that the glycans of leucocyte lactotransferrin differ essentially by the absence of fucose residues.
2390069	5	23	theme	fucose	941:946	arg1	residues					948:955	the fucose residues	937:955	the fucose residues	937:955	These results question a previously proposed mechanism for hyposideraemia in which the leucocyte lactotransferrin was involved and in which the fucose residues played a key role.
2390069	3	24	theme	molar	304:308	arg1	compositions					323:334	the molar carbohydrate compositions	300:334	the molar carbohydrate compositions of human leucocyte lactotransferrin and human milk lactotransferrin	300:402	A comparative analysis of the molar carbohydrate compositions of human leucocyte lactotransferrin and human milk lactotransferrin reveals that the glycans of leucocyte lactotransferrin differ essentially by the absence of fucose residues.
2390069	3	25	theme	carbohydrate	310:321	arg1	compositions					323:334	the molar carbohydrate compositions	300:334	the molar carbohydrate compositions of human leucocyte lactotransferrin and human milk lactotransferrin	300:402	A comparative analysis of the molar carbohydrate compositions of human leucocyte lactotransferrin and human milk lactotransferrin reveals that the glycans of leucocyte lactotransferrin differ essentially by the absence of fucose residues.
2390069	0	26	theme	glycans	21:27	arg1	structure					8:16	Primary structure	0:16	Primary structure of glycans	0:27	Primary structure of glycans isolated from human leucocyte lactotransferrin.
2390069	4	27	theme	type	791:794	arg1	glycans					754:760	two disialylated and non-fucosylated biantennary glycans	705:760	two disialylated and non-fucosylated biantennary glycans of the N-acetyl-lactosaminic type	705:794	Structural analysis combining methylation-mass spectrometry and 400 MHz 1H-n.m.r. spectrometry of oligosaccharide alditols released from human leucocyte lactotransferrin shows the presence of two disialylated and non-fucosylated biantennary glycans of the N-acetyl-lactosaminic type.
2390069	0	28	theme	leucocyte	49:57	arg1	lactotransferrin					59:74	human leucocyte lactotransferrin	43:74	human leucocyte lactotransferrin	43:74	Primary structure of glycans isolated from human leucocyte lactotransferrin.
2390069	3	29	theme	lactotransferrin	355:370	arg1	compositions					323:334	the molar carbohydrate compositions	300:334	the molar carbohydrate compositions of human leucocyte lactotransferrin and human milk lactotransferrin	300:402	A comparative analysis of the molar carbohydrate compositions of human leucocyte lactotransferrin and human milk lactotransferrin reveals that the glycans of leucocyte lactotransferrin differ essentially by the absence of fucose residues.
2390069	4	30	theme	methylation-mass	543:558	arg1	spectrometry					560:571	methylation-mass spectrometry	543:571	methylation-mass spectrometry	543:571	Structural analysis combining methylation-mass spectrometry and 400 MHz 1H-n.m.r. spectrometry of oligosaccharide alditols released from human leucocyte lactotransferrin shows the presence of two disialylated and non-fucosylated biantennary glycans of the N-acetyl-lactosaminic type.
2390069	1	31	theme	proposed	118:125	arg1	mechanism					127:135	the proposed mechanism	114:135	the proposed mechanism of hyposideraemia	114:153	Absence of fucose residues questions the proposed mechanism of hyposideraemia.
2390069	0	32	theme	human	43:47	arg1	lactotransferrin					59:74	human leucocyte lactotransferrin	43:74	human leucocyte lactotransferrin	43:74	Primary structure of glycans isolated from human leucocyte lactotransferrin.
2390069	4	33	theme	leucocyte	656:664	arg1	lactotransferrin					666:681	human leucocyte lactotransferrin	650:681	human leucocyte lactotransferrin	650:681	Structural analysis combining methylation-mass spectrometry and 400 MHz 1H-n.m.r. spectrometry of oligosaccharide alditols released from human leucocyte lactotransferrin shows the presence of two disialylated and non-fucosylated biantennary glycans of the N-acetyl-lactosaminic type.
2390069	5	34	theme	proposed	833:840	arg1	mechanism					842:850	a previously proposed mechanism	820:850	a previously proposed mechanism for hyposideraemia in which the leucocyte lactotransferrin was involved and in which the fucose residues played a key role	820:973	These results question a previously proposed mechanism for hyposideraemia in which the leucocyte lactotransferrin was involved and in which the fucose residues played a key role.
2390069	2	35	theme	immuno-affinity	242:256	arg1	chromatography					258:271	immuno-affinity chromatography	242:271	immuno-affinity chromatography	242:271	Lactotransferrin was highly purified from lysates of human neutrophilic leucocytes by immuno-affinity chromatography.
2390069	4	36	theme	human	650:654	arg1	lactotransferrin					666:681	human leucocyte lactotransferrin	650:681	human leucocyte lactotransferrin	650:681	Structural analysis combining methylation-mass spectrometry and 400 MHz 1H-n.m.r. spectrometry of oligosaccharide alditols released from human leucocyte lactotransferrin shows the presence of two disialylated and non-fucosylated biantennary glycans of the N-acetyl-lactosaminic type.
2390069	3	37	theme	human	339:343	arg1	lactotransferrin					355:370	human leucocyte lactotransferrin	339:370	human leucocyte lactotransferrin	339:370	A comparative analysis of the molar carbohydrate compositions of human leucocyte lactotransferrin and human milk lactotransferrin reveals that the glycans of leucocyte lactotransferrin differ essentially by the absence of fucose residues.
2390069	2	38	theme	leucocytes	228:237	arg1	lysates					198:204	lysates	198:204	lysates of human neutrophilic leucocytes	198:237	Lactotransferrin was highly purified from lysates of human neutrophilic leucocytes by immuno-affinity chromatography.
2390069	4	39	theme	biantennary	742:752	arg1	glycans					754:760	two disialylated and non-fucosylated biantennary glycans	705:760	two disialylated and non-fucosylated biantennary glycans of the N-acetyl-lactosaminic type	705:794	Structural analysis combining methylation-mass spectrometry and 400 MHz 1H-n.m.r. spectrometry of oligosaccharide alditols released from human leucocyte lactotransferrin shows the presence of two disialylated and non-fucosylated biantennary glycans of the N-acetyl-lactosaminic type.
2390069	3	40	theme	leucocyte	345:353	arg1	lactotransferrin					355:370	human leucocyte lactotransferrin	339:370	human leucocyte lactotransferrin	339:370	A comparative analysis of the molar carbohydrate compositions of human leucocyte lactotransferrin and human milk lactotransferrin reveals that the glycans of leucocyte lactotransferrin differ essentially by the absence of fucose residues.
2390069	2	41	theme	neutrophilic	215:226	arg1	leucocytes					228:237	human neutrophilic leucocytes	209:237	human neutrophilic leucocytes	209:237	Lactotransferrin was highly purified from lysates of human neutrophilic leucocytes by immuno-affinity chromatography.
2390069	1	42	theme	hyposideraemia	140:153	arg1	mechanism					127:135	the proposed mechanism	114:135	the proposed mechanism of hyposideraemia	114:153	Absence of fucose residues questions the proposed mechanism of hyposideraemia.
2390069	4	43	theme	non-fucosylated	726:740	arg1	glycans					754:760	two disialylated and non-fucosylated biantennary glycans	705:760	two disialylated and non-fucosylated biantennary glycans of the N-acetyl-lactosaminic type	705:794	Structural analysis combining methylation-mass spectrometry and 400 MHz 1H-n.m.r. spectrometry of oligosaccharide alditols released from human leucocyte lactotransferrin shows the presence of two disialylated and non-fucosylated biantennary glycans of the N-acetyl-lactosaminic type.
2390069	3	44	theme	lactotransferrin	387:402	arg1	compositions					323:334	the molar carbohydrate compositions	300:334	the molar carbohydrate compositions of human leucocyte lactotransferrin and human milk lactotransferrin	300:402	A comparative analysis of the molar carbohydrate compositions of human leucocyte lactotransferrin and human milk lactotransferrin reveals that the glycans of leucocyte lactotransferrin differ essentially by the absence of fucose residues.
2390069	2	45	theme	human	209:213	arg1	leucocytes					228:237	human neutrophilic leucocytes	209:237	human neutrophilic leucocytes	209:237	Lactotransferrin was highly purified from lysates of human neutrophilic leucocytes by immuno-affinity chromatography.
2390069	4	46	theme	glycans	754:760	arg1	presence					693:700	the presence	689:700	the presence of two disialylated and non-fucosylated biantennary glycans of the N-acetyl-lactosaminic type	689:794	Structural analysis combining methylation-mass spectrometry and 400 MHz 1H-n.m.r. spectrometry of oligosaccharide alditols released from human leucocyte lactotransferrin shows the presence of two disialylated and non-fucosylated biantennary glycans of the N-acetyl-lactosaminic type.
10679288	6	0	with	comparison	656:665	arg1	structures					685:694	the N-glycan structures	672:694	the N-glycan structures of osteopontins obtained from other sources (kidney tissues, macrophages, urinary stones, human milk, etc.)	672:802	The result should permit future comparison with the N-glycan structures of osteopontins obtained from other sources (kidney tissues, macrophages, urinary stones, human milk, etc.).
10679288	3	1	theme	mapping	476:482	arg1	technique					484:492	a multidimensional mapping technique	457:492	a multidimensional mapping technique on HPLC columns	457:508	The derivatized N-glycans were separated and structurally identified by a multidimensional mapping technique on HPLC columns.
10679288	2	2	with	aminated	354:361	arg1	2-aminopyridine					368:382	2-aminopyridine	368:382	2-aminopyridine	368:382	Asn-linked glycan portion was released from 100 microg of osteopontin by digestion with glycoamidase A (from sweet almond), and the reducing ends of the N-glycans were reductively aminated with 2-aminopyridine.
10679288	2	3	from	almond	289:294	arg1	A					275:275	glycoamidase A	262:275	glycoamidase A (from sweet almond)	262:295	Asn-linked glycan portion was released from 100 microg of osteopontin by digestion with glycoamidase A (from sweet almond), and the reducing ends of the N-glycans were reductively aminated with 2-aminopyridine.
10679288	1	4	theme	lumbar	131:136	arg1	bone					125:128	human bone	119:128	human bone (lumbar vertabrate)	119:148	N-Glycan structures of osteopontin (a bone matrix protein) from human bone (lumbar vertabrate) are reported in detail.
10679288	1	4	theme	lumbar	131:136	arg1	vertabrate					138:147	lumbar vertabrate	131:147	lumbar vertabrate	131:147	N-Glycan structures of osteopontin (a bone matrix protein) from human bone (lumbar vertabrate) are reported in detail.
10679288	2	5	attach	released	204:211	arg1	microg					222:227	100 microg	218:227	100 microg of osteopontin	218:242	Asn-linked glycan portion was released from 100 microg of osteopontin by digestion with glycoamidase A (from sweet almond), and the reducing ends of the N-glycans were reductively aminated with 2-aminopyridine.
10679288	2	5	attach	released	204:211	arg2	portion					192:198	Asn-linked glycan portion	174:198	Asn-linked glycan portion	174:198	Asn-linked glycan portion was released from 100 microg of osteopontin by digestion with glycoamidase A (from sweet almond), and the reducing ends of the N-glycans were reductively aminated with 2-aminopyridine.
10679288	3	6	from	technique	484:492	arg1	columns					502:508	HPLC columns	497:508	HPLC columns	497:508	The derivatized N-glycans were separated and structurally identified by a multidimensional mapping technique on HPLC columns.
10679288	2	7	theme	glycoamidase	262:273	arg1	A					275:275	glycoamidase A	262:275	glycoamidase A (from sweet almond)	262:295	Asn-linked glycan portion was released from 100 microg of osteopontin by digestion with glycoamidase A (from sweet almond), and the reducing ends of the N-glycans were reductively aminated with 2-aminopyridine.
10679288	0	8	from	bone	49:52	arg1	structures					9:18	N-Glycan structures	0:18	N-Glycan structures of an osteopontin from human bone	0:52	N-Glycan structures of an osteopontin from human bone.
10679288	5	9	theme	proposed	587:594	arg1	structures					596:605	The proposed structures	583:605	The proposed structures	583:605	The proposed structures are shown below.
10679288	1	10	theme	N-Glycan	55:62	arg1	structures					64:73	N-Glycan structures	55:73	N-Glycan structures of osteopontin (a bone matrix protein) from human bone (lumbar vertabrate)	55:148	N-Glycan structures of osteopontin (a bone matrix protein) from human bone (lumbar vertabrate) are reported in detail.
10679288	6	11	theme	osteopontins	699:710	arg1	structures					685:694	the N-glycan structures	672:694	the N-glycan structures of osteopontins obtained from other sources (kidney tissues, macrophages, urinary stones, human milk, etc.)	672:802	The result should permit future comparison with the N-glycan structures of osteopontins obtained from other sources (kidney tissues, macrophages, urinary stones, human milk, etc.).
10679288	4	12	theme	mass	564:567	arg1	spectrometry					569:580	mass spectrometry	564:580	mass spectrometry	564:580	Two major N-glycan structures were also confirmed by mass spectrometry.
10679288	1	13	from	bone	125:128	arg1	structures					64:73	N-Glycan structures	55:73	N-Glycan structures of osteopontin (a bone matrix protein) from human bone (lumbar vertabrate)	55:148	N-Glycan structures of osteopontin (a bone matrix protein) from human bone (lumbar vertabrate) are reported in detail.
10679288	3	14	theme	derivatized	389:399	arg1	N-glycans					401:409	The derivatized N-glycans	385:409	The derivatized N-glycans	385:409	The derivatized N-glycans were separated and structurally identified by a multidimensional mapping technique on HPLC columns.
10679288	2	15	theme	osteopontin	232:242	arg1	microg					222:227	100 microg	218:227	100 microg of osteopontin	218:242	Asn-linked glycan portion was released from 100 microg of osteopontin by digestion with glycoamidase A (from sweet almond), and the reducing ends of the N-glycans were reductively aminated with 2-aminopyridine.
10679288	2	16	theme	N-glycans	327:335	arg1	aminated					354:361	aminated	354:361	aminated	354:361	Asn-linked glycan portion was released from 100 microg of osteopontin by digestion with glycoamidase A (from sweet almond), and the reducing ends of the N-glycans were reductively aminated with 2-aminopyridine.
10679288	2	16	theme	N-glycans	327:335	arg1	ends					315:318	the reducing ends	302:318	the reducing ends of the N-glycans	302:335	Asn-linked glycan portion was released from 100 microg of osteopontin by digestion with glycoamidase A (from sweet almond), and the reducing ends of the N-glycans were reductively aminated with 2-aminopyridine.
10679288	3	17	theme	HPLC	497:500	arg1	columns					502:508	HPLC columns	497:508	HPLC columns	497:508	The derivatized N-glycans were separated and structurally identified by a multidimensional mapping technique on HPLC columns.
10679288	6	18	theme	urinary	770:776	arg1	stones					778:783	urinary stones	770:783	urinary stones	770:783	The result should permit future comparison with the N-glycan structures of osteopontins obtained from other sources (kidney tissues, macrophages, urinary stones, human milk, etc.).
10679288	6	18	theme	urinary	770:776	arg1	tissues					748:754	kidney tissues	741:754	kidney tissues	741:754	The result should permit future comparison with the N-glycan structures of osteopontins obtained from other sources (kidney tissues, macrophages, urinary stones, human milk, etc.).
10679288	1	19	theme	osteopontin	78:88	arg1	structures					64:73	N-Glycan structures	55:73	N-Glycan structures of osteopontin (a bone matrix protein) from human bone (lumbar vertabrate)	55:148	N-Glycan structures of osteopontin (a bone matrix protein) from human bone (lumbar vertabrate) are reported in detail.
10679288	6	20	theme	N-glycan	676:683	arg1	structures					685:694	the N-glycan structures	672:694	the N-glycan structures of osteopontins obtained from other sources (kidney tissues, macrophages, urinary stones, human milk, etc.)	672:802	The result should permit future comparison with the N-glycan structures of osteopontins obtained from other sources (kidney tissues, macrophages, urinary stones, human milk, etc.).
10679288	0	21	theme	N-Glycan	0:7	arg1	structures					9:18	N-Glycan structures	0:18	N-Glycan structures of an osteopontin from human bone	0:52	N-Glycan structures of an osteopontin from human bone.
10679288	4	22	theme	N-glycan	521:528	arg1	structures					530:539	Two major N-glycan structures	511:539	Two major N-glycan structures	511:539	Two major N-glycan structures were also confirmed by mass spectrometry.
10679288	1	23	theme	bone	93:96	arg1	protein					105:111	a bone matrix protein	91:111	a bone matrix protein	91:111	N-Glycan structures of osteopontin (a bone matrix protein) from human bone (lumbar vertabrate) are reported in detail.
10679288	1	23	theme	bone	93:96	arg1	osteopontin					78:88	osteopontin	78:88	osteopontin (a bone matrix protein)	78:112	N-Glycan structures of osteopontin (a bone matrix protein) from human bone (lumbar vertabrate) are reported in detail.
10679288	6	24	theme	future	649:654	arg1	comparison					656:665	future comparison	649:665	future comparison with the N-glycan structures of osteopontins obtained from other sources (kidney tissues, macrophages, urinary stones, human milk, etc.)	649:802	The result should permit future comparison with the N-glycan structures of osteopontins obtained from other sources (kidney tissues, macrophages, urinary stones, human milk, etc.).
10679288	2	25	link	Asn-linked	174:183	arg1	portion					192:198	Asn-linked glycan portion	174:198	Asn-linked glycan portion	174:198	Asn-linked glycan portion was released from 100 microg of osteopontin by digestion with glycoamidase A (from sweet almond), and the reducing ends of the N-glycans were reductively aminated with 2-aminopyridine.
10679288	0	26	theme	osteopontin	26:36	arg1	structures					9:18	N-Glycan structures	0:18	N-Glycan structures of an osteopontin from human bone	0:52	N-Glycan structures of an osteopontin from human bone.
10679288	6	27	theme	human	786:790	arg1	tissues					748:754	kidney tissues	741:754	kidney tissues	741:754	The result should permit future comparison with the N-glycan structures of osteopontins obtained from other sources (kidney tissues, macrophages, urinary stones, human milk, etc.).
10679288	6	27	theme	human	786:790	arg1	milk					792:795	human milk	786:795	human milk	786:795	The result should permit future comparison with the N-glycan structures of osteopontins obtained from other sources (kidney tissues, macrophages, urinary stones, human milk, etc.).
10679288	1	28	theme	matrix	98:103	arg1	protein					105:111	a bone matrix protein	91:111	a bone matrix protein	91:111	N-Glycan structures of osteopontin (a bone matrix protein) from human bone (lumbar vertabrate) are reported in detail.
10679288	1	28	theme	matrix	98:103	arg1	osteopontin					78:88	osteopontin	78:88	osteopontin (a bone matrix protein)	78:112	N-Glycan structures of osteopontin (a bone matrix protein) from human bone (lumbar vertabrate) are reported in detail.
10679288	0	29	theme	human	43:47	arg1	bone					49:52	human bone	43:52	human bone	43:52	N-Glycan structures of an osteopontin from human bone.
10679288	4	30	theme	major	515:519	arg1	structures					530:539	Two major N-glycan structures	511:539	Two major N-glycan structures	511:539	Two major N-glycan structures were also confirmed by mass spectrometry.
10679288	2	31	theme	Asn-linked	174:183	arg1	portion					192:198	Asn-linked glycan portion	174:198	Asn-linked glycan portion	174:198	Asn-linked glycan portion was released from 100 microg of osteopontin by digestion with glycoamidase A (from sweet almond), and the reducing ends of the N-glycans were reductively aminated with 2-aminopyridine.
10679288	2	32	theme	glycan	185:190	arg1	portion					192:198	Asn-linked glycan portion	174:198	Asn-linked glycan portion	174:198	Asn-linked glycan portion was released from 100 microg of osteopontin by digestion with glycoamidase A (from sweet almond), and the reducing ends of the N-glycans were reductively aminated with 2-aminopyridine.
10679288	6	33	theme	kidney	741:746	arg1	milk					792:795	human milk	786:795	human milk	786:795	The result should permit future comparison with the N-glycan structures of osteopontins obtained from other sources (kidney tissues, macrophages, urinary stones, human milk, etc.).
10679288	6	33	theme	kidney	741:746	arg1	macrophages					757:767	macrophages	757:767	macrophages	757:767	The result should permit future comparison with the N-glycan structures of osteopontins obtained from other sources (kidney tissues, macrophages, urinary stones, human milk, etc.).
10679288	6	33	theme	kidney	741:746	arg1	stones					778:783	urinary stones	770:783	urinary stones	770:783	The result should permit future comparison with the N-glycan structures of osteopontins obtained from other sources (kidney tissues, macrophages, urinary stones, human milk, etc.).
10679288	6	33	theme	kidney	741:746	arg1	tissues					748:754	kidney tissues	741:754	kidney tissues	741:754	The result should permit future comparison with the N-glycan structures of osteopontins obtained from other sources (kidney tissues, macrophages, urinary stones, human milk, etc.).
10679288	6	33	theme	kidney	741:746	arg1	etc					798:800	etc	798:800	etc	798:800	The result should permit future comparison with the N-glycan structures of osteopontins obtained from other sources (kidney tissues, macrophages, urinary stones, human milk, etc.).
10679288	3	34	theme	multidimensional	459:474	arg1	technique					484:492	a multidimensional mapping technique	457:492	a multidimensional mapping technique on HPLC columns	457:508	The derivatized N-glycans were separated and structurally identified by a multidimensional mapping technique on HPLC columns.
10679288	2	35	theme	sweet	283:287	arg1	almond					289:294	sweet almond	283:294	sweet almond	283:294	Asn-linked glycan portion was released from 100 microg of osteopontin by digestion with glycoamidase A (from sweet almond), and the reducing ends of the N-glycans were reductively aminated with 2-aminopyridine.
10679288	6	36	dep	sources	732:738	arg1	milk					792:795	human milk	786:795	human milk	786:795	The result should permit future comparison with the N-glycan structures of osteopontins obtained from other sources (kidney tissues, macrophages, urinary stones, human milk, etc.).
10679288	6	36	dep	sources	732:738	arg1	macrophages					757:767	macrophages	757:767	macrophages	757:767	The result should permit future comparison with the N-glycan structures of osteopontins obtained from other sources (kidney tissues, macrophages, urinary stones, human milk, etc.).
10679288	6	36	dep	sources	732:738	arg1	stones					778:783	urinary stones	770:783	urinary stones	770:783	The result should permit future comparison with the N-glycan structures of osteopontins obtained from other sources (kidney tissues, macrophages, urinary stones, human milk, etc.).
10679288	6	36	dep	sources	732:738	arg1	tissues					748:754	kidney tissues	741:754	kidney tissues	741:754	The result should permit future comparison with the N-glycan structures of osteopontins obtained from other sources (kidney tissues, macrophages, urinary stones, human milk, etc.).
10679288	6	36	dep	sources	732:738	arg1	etc					798:800	etc	798:800	etc	798:800	The result should permit future comparison with the N-glycan structures of osteopontins obtained from other sources (kidney tissues, macrophages, urinary stones, human milk, etc.).
10679288	6	37	theme	other	726:730	arg1	sources					732:738	other sources	726:738	other sources (kidney tissues, macrophages, urinary stones, human milk, etc.)	726:802	The result should permit future comparison with the N-glycan structures of osteopontins obtained from other sources (kidney tissues, macrophages, urinary stones, human milk, etc.).
10679288	1	38	theme	human	119:123	arg1	bone					125:128	human bone	119:128	human bone (lumbar vertabrate)	119:148	N-Glycan structures of osteopontin (a bone matrix protein) from human bone (lumbar vertabrate) are reported in detail.
10679288	1	38	theme	human	119:123	arg1	vertabrate					138:147	lumbar vertabrate	131:147	lumbar vertabrate	131:147	N-Glycan structures of osteopontin (a bone matrix protein) from human bone (lumbar vertabrate) are reported in detail.
10679288	2	39	theme	reducing	306:313	arg1	aminated					354:361	aminated	354:361	aminated	354:361	Asn-linked glycan portion was released from 100 microg of osteopontin by digestion with glycoamidase A (from sweet almond), and the reducing ends of the N-glycans were reductively aminated with 2-aminopyridine.
10679288	2	39	theme	reducing	306:313	arg1	ends					315:318	the reducing ends	302:318	the reducing ends of the N-glycans	302:335	Asn-linked glycan portion was released from 100 microg of osteopontin by digestion with glycoamidase A (from sweet almond), and the reducing ends of the N-glycans were reductively aminated with 2-aminopyridine.
10679288	2	40	with	digestion	247:255	arg1	A					275:275	glycoamidase A	262:275	glycoamidase A (from sweet almond)	262:295	Asn-linked glycan portion was released from 100 microg of osteopontin by digestion with glycoamidase A (from sweet almond), and the reducing ends of the N-glycans were reductively aminated with 2-aminopyridine.
2535488	0	0	theme	von	82:84	arg1	factor					97:102	human von Willebrand factor	76:102	human von Willebrand factor	76:102	Primary structure of the major O-glycosidically linked carbohydrate unit of human von Willebrand factor.
2535488	1	1	theme	human	155:159	arg1	vWF					184:186	vWF	184:186	vWF	184:186	A reduced tetrasaccharide chain was obtained from human von Willebrand factor (vWF) by mild alkaline borohydride treatment.
2535488	1	1	theme	human	155:159	arg1	factor					176:181	human von Willebrand factor	155:181	human von Willebrand factor (vWF)	155:187	A reduced tetrasaccharide chain was obtained from human von Willebrand factor (vWF) by mild alkaline borohydride treatment.
2535488	0	2	theme	human	76:80	arg1	factor					97:102	human von Willebrand factor	76:102	human von Willebrand factor	76:102	Primary structure of the major O-glycosidically linked carbohydrate unit of human von Willebrand factor.
2535488	2	3	theme	Lens	375:378	arg1	agglutinin					390:399	Lens culinaris agglutinin	375:399	Lens culinaris agglutinin	375:399	The purification of this O-glycosidically-linked oligosaccharide was achieved by serial affinity chromatography on immobilized concanavalin A and Lens culinaris agglutinin and finally gel filtration.
2535488	0	4	theme	factor	97:102	arg1	unit					68:71	the major O-glycosidically linked carbohydrate unit	21:71	the major O-glycosidically linked carbohydrate unit of human von Willebrand factor	21:102	Primary structure of the major O-glycosidically linked carbohydrate unit of human von Willebrand factor.
2535488	2	5	theme	serial	310:315	arg1	chromatography					326:339	serial affinity chromatography	310:339	serial affinity chromatography on immobilized concanavalin A and Lens culinaris agglutinin	310:399	The purification of this O-glycosidically-linked oligosaccharide was achieved by serial affinity chromatography on immobilized concanavalin A and Lens culinaris agglutinin and finally gel filtration.
2535488	2	6	link	O-glycosidically-linked	254:276	arg1	oligosaccharide					278:292	this O-glycosidically-linked oligosaccharide	249:292	this O-glycosidically-linked oligosaccharide	249:292	The purification of this O-glycosidically-linked oligosaccharide was achieved by serial affinity chromatography on immobilized concanavalin A and Lens culinaris agglutinin and finally gel filtration.
2535488	0	7	theme	Willebrand	86:95	arg1	factor					97:102	human von Willebrand factor	76:102	human von Willebrand factor	76:102	Primary structure of the major O-glycosidically linked carbohydrate unit of human von Willebrand factor.
2535488	3	8	theme	Gal	553:555	arg1	GalNAc-ol					584:592	: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol	535:592	: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol	535:592	Its structure was determined by a combination of methylation studies and 500 MHz 1H-NMR spectroscopy to be: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol.
2535488	2	9	theme	culinaris	380:388	arg1	agglutinin					390:399	Lens culinaris agglutinin	375:399	Lens culinaris agglutinin	375:399	The purification of this O-glycosidically-linked oligosaccharide was achieved by serial affinity chromatography on immobilized concanavalin A and Lens culinaris agglutinin and finally gel filtration.
2535488	3	10	theme	1H-NMR	510:515	arg1	spectroscopy					517:528	500 MHz 1H-NMR spectroscopy	502:528	500 MHz 1H-NMR spectroscopy	502:528	Its structure was determined by a combination of methylation studies and 500 MHz 1H-NMR spectroscopy to be: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol.
2535488	3	11	theme	spectroscopy	517:528	arg1	combination					463:473	a combination	461:473	a combination of methylation studies and 500 MHz 1H-NMR spectroscopy to be: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol	461:592	Its structure was determined by a combination of methylation studies and 500 MHz 1H-NMR spectroscopy to be: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol.
2535488	3	12	theme	alpha	543:547	arg1	Gal					553:555	NeuAc(alpha 2-3)Gal	537:555	: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol	535:592	Its structure was determined by a combination of methylation studies and 500 MHz 1H-NMR spectroscopy to be: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol.
2535488	1	13	theme	Willebrand	165:174	arg1	vWF					184:186	vWF	184:186	vWF	184:186	A reduced tetrasaccharide chain was obtained from human von Willebrand factor (vWF) by mild alkaline borohydride treatment.
2535488	1	13	theme	Willebrand	165:174	arg1	factor					176:181	human von Willebrand factor	155:181	human von Willebrand factor (vWF)	155:187	A reduced tetrasaccharide chain was obtained from human von Willebrand factor (vWF) by mild alkaline borohydride treatment.
2535488	2	14	theme	oligosaccharide	278:292	arg1	purification					233:244	The purification	229:244	The purification of this O-glycosidically-linked oligosaccharide	229:292	The purification of this O-glycosidically-linked oligosaccharide was achieved by serial affinity chromatography on immobilized concanavalin A and Lens culinaris agglutinin and finally gel filtration.
2535488	0	15	link	linked	48:53	arg1	unit					68:71	the major O-glycosidically linked carbohydrate unit	21:71	the major O-glycosidically linked carbohydrate unit of human von Willebrand factor	21:102	Primary structure of the major O-glycosidically linked carbohydrate unit of human von Willebrand factor.
2535488	2	16	theme	gel	413:415	arg1	filtration					417:426	gel filtration	413:426	gel filtration	413:426	The purification of this O-glycosidically-linked oligosaccharide was achieved by serial affinity chromatography on immobilized concanavalin A and Lens culinaris agglutinin and finally gel filtration.
2535488	0	17	theme	Primary	0:6	arg1	structure					8:16	Primary structure	0:16	Primary structure of the major O-glycosidically linked carbohydrate unit of human von Willebrand factor	0:102	Primary structure of the major O-glycosidically linked carbohydrate unit of human von Willebrand factor.
2535488	3	18	theme	beta	557:560	arg1	alpha					573:577	alpha 2-6	573:581	alpha 2-6	573:581	Its structure was determined by a combination of methylation studies and 500 MHz 1H-NMR spectroscopy to be: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol.
2535488	3	18	theme	beta	557:560	arg1	[NeuAc					566:571	beta 1-3)[NeuAc	557:571	beta 1-3)[NeuAc(alpha 2-6)	557:582	Its structure was determined by a combination of methylation studies and 500 MHz 1H-NMR spectroscopy to be: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol.
2535488	3	19	dep	Gal	553:555	arg1	alpha					573:577	alpha 2-6	573:581	alpha 2-6	573:581	Its structure was determined by a combination of methylation studies and 500 MHz 1H-NMR spectroscopy to be: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol.
2535488	3	19	dep	Gal	553:555	arg1	[NeuAc					566:571	beta 1-3)[NeuAc	557:571	beta 1-3)[NeuAc(alpha 2-6)	557:582	Its structure was determined by a combination of methylation studies and 500 MHz 1H-NMR spectroscopy to be: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol.
2535488	2	20	theme	affinity	317:324	arg1	chromatography					326:339	serial affinity chromatography	310:339	serial affinity chromatography on immobilized concanavalin A and Lens culinaris agglutinin	310:399	The purification of this O-glycosidically-linked oligosaccharide was achieved by serial affinity chromatography on immobilized concanavalin A and Lens culinaris agglutinin and finally gel filtration.
2535488	1	21	theme	von	161:163	arg1	vWF					184:186	vWF	184:186	vWF	184:186	A reduced tetrasaccharide chain was obtained from human von Willebrand factor (vWF) by mild alkaline borohydride treatment.
2535488	1	21	theme	von	161:163	arg1	factor					176:181	human von Willebrand factor	155:181	human von Willebrand factor (vWF)	155:187	A reduced tetrasaccharide chain was obtained from human von Willebrand factor (vWF) by mild alkaline borohydride treatment.
2535488	3	22	theme	500	502:504	arg1	MHz					506:508	MHz	506:508	MHz	506:508	Its structure was determined by a combination of methylation studies and 500 MHz 1H-NMR spectroscopy to be: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol.
2535488	3	23	theme	methylation	478:488	arg1	studies					490:496	methylation studies	478:496	methylation studies	478:496	Its structure was determined by a combination of methylation studies and 500 MHz 1H-NMR spectroscopy to be: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol.
2535488	1	24	theme	mild	192:195	arg1	treatment					218:226	mild alkaline borohydride treatment	192:226	mild alkaline borohydride treatment	192:226	A reduced tetrasaccharide chain was obtained from human von Willebrand factor (vWF) by mild alkaline borohydride treatment.
2535488	0	25	theme	major	25:29	arg1	unit					68:71	the major O-glycosidically linked carbohydrate unit	21:71	the major O-glycosidically linked carbohydrate unit of human von Willebrand factor	21:102	Primary structure of the major O-glycosidically linked carbohydrate unit of human von Willebrand factor.
2535488	1	26	theme	alkaline	197:204	arg1	treatment					218:226	mild alkaline borohydride treatment	192:226	mild alkaline borohydride treatment	192:226	A reduced tetrasaccharide chain was obtained from human von Willebrand factor (vWF) by mild alkaline borohydride treatment.
2535488	0	27	theme	carbohydrate	55:66	arg1	unit					68:71	the major O-glycosidically linked carbohydrate unit	21:71	the major O-glycosidically linked carbohydrate unit of human von Willebrand factor	21:102	Primary structure of the major O-glycosidically linked carbohydrate unit of human von Willebrand factor.
2535488	3	28	theme	studies	490:496	arg1	combination					463:473	a combination	461:473	a combination of methylation studies and 500 MHz 1H-NMR spectroscopy to be: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol	461:592	Its structure was determined by a combination of methylation studies and 500 MHz 1H-NMR spectroscopy to be: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol.
2535488	1	29	theme	reduced	107:113	arg1	chain					131:135	A reduced tetrasaccharide chain	105:135	A reduced tetrasaccharide chain	105:135	A reduced tetrasaccharide chain was obtained from human von Willebrand factor (vWF) by mild alkaline borohydride treatment.
2535488	0	30	theme	linked	48:53	arg1	unit					68:71	the major O-glycosidically linked carbohydrate unit	21:71	the major O-glycosidically linked carbohydrate unit of human von Willebrand factor	21:102	Primary structure of the major O-glycosidically linked carbohydrate unit of human von Willebrand factor.
2535488	1	31	theme	tetrasaccharide	115:129	arg1	chain					131:135	A reduced tetrasaccharide chain	105:135	A reduced tetrasaccharide chain	105:135	A reduced tetrasaccharide chain was obtained from human von Willebrand factor (vWF) by mild alkaline borohydride treatment.
2535488	2	32	theme	O-glycosidically-linked	254:276	arg1	oligosaccharide					278:292	this O-glycosidically-linked oligosaccharide	249:292	this O-glycosidically-linked oligosaccharide	249:292	The purification of this O-glycosidically-linked oligosaccharide was achieved by serial affinity chromatography on immobilized concanavalin A and Lens culinaris agglutinin and finally gel filtration.
2535488	2	33	from	filtration	417:426	arg1	A					369:369	immobilized concanavalin A	344:369	immobilized concanavalin A	344:369	The purification of this O-glycosidically-linked oligosaccharide was achieved by serial affinity chromatography on immobilized concanavalin A and Lens culinaris agglutinin and finally gel filtration.
2535488	2	33	from	filtration	417:426	arg1	agglutinin					390:399	Lens culinaris agglutinin	375:399	Lens culinaris agglutinin	375:399	The purification of this O-glycosidically-linked oligosaccharide was achieved by serial affinity chromatography on immobilized concanavalin A and Lens culinaris agglutinin and finally gel filtration.
2535488	2	34	theme	concanavalin	356:367	arg1	A					369:369	immobilized concanavalin A	344:369	immobilized concanavalin A	344:369	The purification of this O-glycosidically-linked oligosaccharide was achieved by serial affinity chromatography on immobilized concanavalin A and Lens culinaris agglutinin and finally gel filtration.
2535488	1	35	theme	borohydride	206:216	arg1	treatment					218:226	mild alkaline borohydride treatment	192:226	mild alkaline borohydride treatment	192:226	A reduced tetrasaccharide chain was obtained from human von Willebrand factor (vWF) by mild alkaline borohydride treatment.
2535488	3	36	theme	2-3	549:551	arg1	Gal					553:555	NeuAc(alpha 2-3)Gal	537:555	: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol	535:592	Its structure was determined by a combination of methylation studies and 500 MHz 1H-NMR spectroscopy to be: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol.
2535488	2	37	theme	immobilized	344:354	arg1	A					369:369	immobilized concanavalin A	344:369	immobilized concanavalin A	344:369	The purification of this O-glycosidically-linked oligosaccharide was achieved by serial affinity chromatography on immobilized concanavalin A and Lens culinaris agglutinin and finally gel filtration.
2535488	3	38	theme	MHz	506:508	arg1	spectroscopy					517:528	500 MHz 1H-NMR spectroscopy	502:528	500 MHz 1H-NMR spectroscopy	502:528	Its structure was determined by a combination of methylation studies and 500 MHz 1H-NMR spectroscopy to be: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol.
2535488	2	39	from	chromatography	326:339	arg1	A					369:369	immobilized concanavalin A	344:369	immobilized concanavalin A	344:369	The purification of this O-glycosidically-linked oligosaccharide was achieved by serial affinity chromatography on immobilized concanavalin A and Lens culinaris agglutinin and finally gel filtration.
2535488	2	39	from	chromatography	326:339	arg1	agglutinin					390:399	Lens culinaris agglutinin	375:399	Lens culinaris agglutinin	375:399	The purification of this O-glycosidically-linked oligosaccharide was achieved by serial affinity chromatography on immobilized concanavalin A and Lens culinaris agglutinin and finally gel filtration.
2535488	3	40	theme	NeuAc	537:541	arg1	Gal					553:555	NeuAc(alpha 2-3)Gal	537:555	: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol	535:592	Its structure was determined by a combination of methylation studies and 500 MHz 1H-NMR spectroscopy to be: NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol.
2535488	0	41	theme	unit	68:71	arg1	structure					8:16	Primary structure	0:16	Primary structure of the major O-glycosidically linked carbohydrate unit of human von Willebrand factor	0:102	Primary structure of the major O-glycosidically linked carbohydrate unit of human von Willebrand factor.
6714238	0	0	theme	sialidosis	78:87	arg1	urine					107:111	sialidosis (mucolipidosis I) urine	78:111	sialidosis (mucolipidosis I) urine	78:111	The structure of sialyl-glycopeptides of the O-glycosidic type, isolated from sialidosis (mucolipidosis I) urine.
6714238	2	1	theme	methylation	521:531	arg1	studies					533:539	methylation studies	521:539	methylation studies	521:539	Their structures were determined by a combination of carbohydrate and amino acid analysis, dansylation, periodate oxidation, methylation studies, enzymatic hydrolysis and 1H-NMR spectroscopy, to be as follows: (formula; see text) wherein R = peptide linked through -Thr-, -Ser-Thr- or -Thr-Ser-.
6714238	1	2	theme	linked	166:171	arg1	chain					189:193	an O-glycosidically linked tetrasaccharide chain	146:193	an O-glycosidically linked tetrasaccharide chain	146:193	Sialyl-glycopeptides containing an O-glycosidically linked tetrasaccharide chain were obtained from the urine of a patient suffering from mucolipidosis I. Isolation of these compounds was achieved by gel filtration, ion-exchange chromatography and preparative paper chromatography.
6714238	1	3	theme	I.	266:267	arg1	Isolation					269:277	mucolipidosis I. Isolation	252:277	mucolipidosis I. Isolation of these compounds	252:296	Sialyl-glycopeptides containing an O-glycosidically linked tetrasaccharide chain were obtained from the urine of a patient suffering from mucolipidosis I. Isolation of these compounds was achieved by gel filtration, ion-exchange chromatography and preparative paper chromatography.
6714238	1	4	theme	preparative	362:372	arg1	chromatography					380:393	preparative paper chromatography	362:393	preparative paper chromatography	362:393	Sialyl-glycopeptides containing an O-glycosidically linked tetrasaccharide chain were obtained from the urine of a patient suffering from mucolipidosis I. Isolation of these compounds was achieved by gel filtration, ion-exchange chromatography and preparative paper chromatography.
6714238	4	5	theme	existence	862:870	arg1	possibility					843:853	The possibility	839:853	The possibility of the existence of a human endo-alpha-N-acetylgalactosaminidase	839:918	The possibility of the existence of a human endo-alpha-N-acetylgalactosaminidase is discussed.
6714238	1	6	theme	tetrasaccharide	173:187	arg1	chain					189:193	an O-glycosidically linked tetrasaccharide chain	146:193	an O-glycosidically linked tetrasaccharide chain	146:193	Sialyl-glycopeptides containing an O-glycosidically linked tetrasaccharide chain were obtained from the urine of a patient suffering from mucolipidosis I. Isolation of these compounds was achieved by gel filtration, ion-exchange chromatography and preparative paper chromatography.
6714238	0	7	theme	mucolipidosis	90:102	arg1	urine					107:111	sialidosis (mucolipidosis I) urine	78:111	sialidosis (mucolipidosis I) urine	78:111	The structure of sialyl-glycopeptides of the O-glycosidic type, isolated from sialidosis (mucolipidosis I) urine.
6714238	1	8	theme	paper	374:378	arg1	chromatography					380:393	preparative paper chromatography	362:393	preparative paper chromatography	362:393	Sialyl-glycopeptides containing an O-glycosidically linked tetrasaccharide chain were obtained from the urine of a patient suffering from mucolipidosis I. Isolation of these compounds was achieved by gel filtration, ion-exchange chromatography and preparative paper chromatography.
6714238	4	9	theme	endo-alpha-N-acetylgalactosaminidase	883:918	arg1	existence					862:870	the existence	858:870	the existence of a human endo-alpha-N-acetylgalactosaminidase	858:918	The possibility of the existence of a human endo-alpha-N-acetylgalactosaminidase is discussed.
6714238	3	10	theme	sialidase	817:825	arg1	deficiency					827:836	a general "glycoprotein-specific" sialidase deficiency	783:836	a general "glycoprotein-specific" sialidase deficiency	783:836	The finding of these glycopeptides in urine shows that mucolipidosis I is characterized by a general "glycoprotein-specific" sialidase deficiency.
6714238	4	11	theme	human	877:881	arg1	endo-alpha-N-acetylgalactosaminidase					883:918	a human endo-alpha-N-acetylgalactosaminidase	875:918	a human endo-alpha-N-acetylgalactosaminidase	875:918	The possibility of the existence of a human endo-alpha-N-acetylgalactosaminidase is discussed.
6714238	2	12	theme	hydrolysis	552:561	arg1	combination					434:444	a combination	432:444	a combination of carbohydrate and amino acid analysis, dansylation, periodate oxidation, methylation studies, enzymatic hydrolysis and 1H-NMR spectroscopy	432:585	Their structures were determined by a combination of carbohydrate and amino acid analysis, dansylation, periodate oxidation, methylation studies, enzymatic hydrolysis and 1H-NMR spectroscopy, to be as follows: (formula; see text) wherein R = peptide linked through -Thr-, -Ser-Thr- or -Thr-Ser-.
6714238	0	13	theme	I	104:104	arg1	urine					107:111	sialidosis (mucolipidosis I) urine	78:111	sialidosis (mucolipidosis I) urine	78:111	The structure of sialyl-glycopeptides of the O-glycosidic type, isolated from sialidosis (mucolipidosis I) urine.
6714238	2	14	dep	see	616:618	arg1	formula					607:613	formula	607:613	formula	607:613	Their structures were determined by a combination of carbohydrate and amino acid analysis, dansylation, periodate oxidation, methylation studies, enzymatic hydrolysis and 1H-NMR spectroscopy, to be as follows: (formula; see text) wherein R = peptide linked through -Thr-, -Ser-Thr- or -Thr-Ser-.
6714238	3	15	theme	glycopeptides	713:725	arg1	finding					696:702	The finding	692:702	The finding of these glycopeptides in urine	692:734	The finding of these glycopeptides in urine shows that mucolipidosis I is characterized by a general "glycoprotein-specific" sialidase deficiency.
6714238	2	16	theme	wherein	626:632	arg1	R					634:634	(formula; see text) wherein R	606:634	(formula; see text) wherein R	606:634	Their structures were determined by a combination of carbohydrate and amino acid analysis, dansylation, periodate oxidation, methylation studies, enzymatic hydrolysis and 1H-NMR spectroscopy, to be as follows: (formula; see text) wherein R = peptide linked through -Thr-, -Ser-Thr- or -Thr-Ser-.
6714238	2	17	theme	analysis	477:484	arg1	combination					434:444	a combination	432:444	a combination of carbohydrate and amino acid analysis, dansylation, periodate oxidation, methylation studies, enzymatic hydrolysis and 1H-NMR spectroscopy	432:585	Their structures were determined by a combination of carbohydrate and amino acid analysis, dansylation, periodate oxidation, methylation studies, enzymatic hydrolysis and 1H-NMR spectroscopy, to be as follows: (formula; see text) wherein R = peptide linked through -Thr-, -Ser-Thr- or -Thr-Ser-.
6714238	1	18	theme	compounds	288:296	arg1	Isolation					269:277	mucolipidosis I. Isolation	252:277	mucolipidosis I. Isolation of these compounds	252:296	Sialyl-glycopeptides containing an O-glycosidically linked tetrasaccharide chain were obtained from the urine of a patient suffering from mucolipidosis I. Isolation of these compounds was achieved by gel filtration, ion-exchange chromatography and preparative paper chromatography.
6714238	0	19	theme	sialyl-glycopeptides	17:36	arg1	structure					4:12	The structure	0:12	The structure of sialyl-glycopeptides of the O-glycosidic type, isolated from sialidosis (mucolipidosis I) urine.	0:112	The structure of sialyl-glycopeptides of the O-glycosidic type, isolated from sialidosis (mucolipidosis I) urine.
6714238	1	20	link	linked	166:171	arg1	chain					189:193	an O-glycosidically linked tetrasaccharide chain	146:193	an O-glycosidically linked tetrasaccharide chain	146:193	Sialyl-glycopeptides containing an O-glycosidically linked tetrasaccharide chain were obtained from the urine of a patient suffering from mucolipidosis I. Isolation of these compounds was achieved by gel filtration, ion-exchange chromatography and preparative paper chromatography.
6714238	2	21	theme	amino	466:470	arg1	analysis					477:484	carbohydrate and amino acid analysis	449:484	analysis	477:484	Their structures were determined by a combination of carbohydrate and amino acid analysis, dansylation, periodate oxidation, methylation studies, enzymatic hydrolysis and 1H-NMR spectroscopy, to be as follows: (formula; see text) wherein R = peptide linked through -Thr-, -Ser-Thr- or -Thr-Ser-.
6714238	3	22	gly	glycopeptides	713:725	arg2	glycopeptides					713:725	these glycopeptides	707:725	these glycopeptides	707:725	The finding of these glycopeptides in urine shows that mucolipidosis I is characterized by a general "glycoprotein-specific" sialidase deficiency.
6714238	2	23	theme	carbohydrate	449:460	arg1	analysis					477:484	carbohydrate and amino acid analysis	449:484	analysis	477:484	Their structures were determined by a combination of carbohydrate and amino acid analysis, dansylation, periodate oxidation, methylation studies, enzymatic hydrolysis and 1H-NMR spectroscopy, to be as follows: (formula; see text) wherein R = peptide linked through -Thr-, -Ser-Thr- or -Thr-Ser-.
6714238	2	24	theme	oxidation	510:518	arg1	combination					434:444	a combination	432:444	a combination of carbohydrate and amino acid analysis, dansylation, periodate oxidation, methylation studies, enzymatic hydrolysis and 1H-NMR spectroscopy	432:585	Their structures were determined by a combination of carbohydrate and amino acid analysis, dansylation, periodate oxidation, methylation studies, enzymatic hydrolysis and 1H-NMR spectroscopy, to be as follows: (formula; see text) wherein R = peptide linked through -Thr-, -Ser-Thr- or -Thr-Ser-.
6714238	2	25	theme	periodate	500:508	arg1	oxidation					510:518	periodate oxidation	500:518	periodate oxidation	500:518	Their structures were determined by a combination of carbohydrate and amino acid analysis, dansylation, periodate oxidation, methylation studies, enzymatic hydrolysis and 1H-NMR spectroscopy, to be as follows: (formula; see text) wherein R = peptide linked through -Thr-, -Ser-Thr- or -Thr-Ser-.
6714238	1	26	theme	gel	314:316	arg1	filtration					318:327	gel filtration	314:327	gel filtration	314:327	Sialyl-glycopeptides containing an O-glycosidically linked tetrasaccharide chain were obtained from the urine of a patient suffering from mucolipidosis I. Isolation of these compounds was achieved by gel filtration, ion-exchange chromatography and preparative paper chromatography.
6714238	1	27	gly	Sialyl-glycopeptides	114:133	arg2	Sialyl-glycopeptides					114:133	Sialyl-glycopeptides	114:133	Sialyl-glycopeptides containing an O-glycosidically linked tetrasaccharide chain	114:193	Sialyl-glycopeptides containing an O-glycosidically linked tetrasaccharide chain were obtained from the urine of a patient suffering from mucolipidosis I. Isolation of these compounds was achieved by gel filtration, ion-exchange chromatography and preparative paper chromatography.
6714238	2	28	theme	acid	472:475	arg1	analysis					477:484	carbohydrate and amino acid analysis	449:484	analysis	477:484	Their structures were determined by a combination of carbohydrate and amino acid analysis, dansylation, periodate oxidation, methylation studies, enzymatic hydrolysis and 1H-NMR spectroscopy, to be as follows: (formula; see text) wherein R = peptide linked through -Thr-, -Ser-Thr- or -Thr-Ser-.
6714238	2	29	theme	spectroscopy	574:585	arg1	combination					434:444	a combination	432:444	a combination of carbohydrate and amino acid analysis, dansylation, periodate oxidation, methylation studies, enzymatic hydrolysis and 1H-NMR spectroscopy	432:585	Their structures were determined by a combination of carbohydrate and amino acid analysis, dansylation, periodate oxidation, methylation studies, enzymatic hydrolysis and 1H-NMR spectroscopy, to be as follows: (formula; see text) wherein R = peptide linked through -Thr-, -Ser-Thr- or -Thr-Ser-.
6714238	2	30	theme	enzymatic	542:550	arg1	hydrolysis					552:561	enzymatic hydrolysis	542:561	enzymatic hydrolysis	542:561	Their structures were determined by a combination of carbohydrate and amino acid analysis, dansylation, periodate oxidation, methylation studies, enzymatic hydrolysis and 1H-NMR spectroscopy, to be as follows: (formula; see text) wherein R = peptide linked through -Thr-, -Ser-Thr- or -Thr-Ser-.
6714238	0	31	theme	type	58:61	arg1	sialyl-glycopeptides					17:36	sialyl-glycopeptides	17:36	sialyl-glycopeptides	17:36	The structure of sialyl-glycopeptides of the O-glycosidic type, isolated from sialidosis (mucolipidosis I) urine.
6714238	2	32	theme	1H-NMR	567:572	arg1	spectroscopy					574:585	1H-NMR spectroscopy	567:585	1H-NMR spectroscopy	567:585	Their structures were determined by a combination of carbohydrate and amino acid analysis, dansylation, periodate oxidation, methylation studies, enzymatic hydrolysis and 1H-NMR spectroscopy, to be as follows: (formula; see text) wherein R = peptide linked through -Thr-, -Ser-Thr- or -Thr-Ser-.
6714238	0	33	attach	isolated	64:71	arg1	urine					107:111	sialidosis (mucolipidosis I) urine	78:111	sialidosis (mucolipidosis I) urine	78:111	The structure of sialyl-glycopeptides of the O-glycosidic type, isolated from sialidosis (mucolipidosis I) urine.
6714238	0	33	attach	isolated	64:71	arg2	sialyl-glycopeptides					17:36	sialyl-glycopeptides	17:36	sialyl-glycopeptides	17:36	The structure of sialyl-glycopeptides of the O-glycosidic type, isolated from sialidosis (mucolipidosis I) urine.
6714238	0	34	theme	O-glycosidic	45:56	arg1	type					58:61	the O-glycosidic type	41:61	the O-glycosidic type	41:61	The structure of sialyl-glycopeptides of the O-glycosidic type, isolated from sialidosis (mucolipidosis I) urine.
6714238	2	35	theme	dansylation	487:497	arg1	combination					434:444	a combination	432:444	a combination of carbohydrate and amino acid analysis, dansylation, periodate oxidation, methylation studies, enzymatic hydrolysis and 1H-NMR spectroscopy	432:585	Their structures were determined by a combination of carbohydrate and amino acid analysis, dansylation, periodate oxidation, methylation studies, enzymatic hydrolysis and 1H-NMR spectroscopy, to be as follows: (formula; see text) wherein R = peptide linked through -Thr-, -Ser-Thr- or -Thr-Ser-.
6714238	0	36	gly	sialyl-glycopeptides	17:36	arg2	sialyl-glycopeptides					17:36	sialyl-glycopeptides	17:36	sialyl-glycopeptides	17:36	The structure of sialyl-glycopeptides of the O-glycosidic type, isolated from sialidosis (mucolipidosis I) urine.
6714238	0	36	gly	sialyl-glycopeptides	17:36	arg1	type					58:61	the O-glycosidic type	41:61	the O-glycosidic type	41:61	The structure of sialyl-glycopeptides of the O-glycosidic type, isolated from sialidosis (mucolipidosis I) urine.
6714238	1	37	theme	ion-exchange	330:341	arg1	chromatography					343:356	ion-exchange chromatography	330:356	ion-exchange chromatography	330:356	Sialyl-glycopeptides containing an O-glycosidically linked tetrasaccharide chain were obtained from the urine of a patient suffering from mucolipidosis I. Isolation of these compounds was achieved by gel filtration, ion-exchange chromatography and preparative paper chromatography.
6714238	3	38	from	finding	696:702	arg1	urine					730:734	urine	730:734	urine	730:734	The finding of these glycopeptides in urine shows that mucolipidosis I is characterized by a general "glycoprotein-specific" sialidase deficiency.
6714238	1	39	theme	patient	229:235	arg1	urine					218:222	the urine	214:222	the urine of a patient suffering from mucolipidosis I. Isolation of these compounds was achieved by gel filtration, ion-exchange chromatography and preparative paper chromatography	214:393	Sialyl-glycopeptides containing an O-glycosidically linked tetrasaccharide chain were obtained from the urine of a patient suffering from mucolipidosis I. Isolation of these compounds was achieved by gel filtration, ion-exchange chromatography and preparative paper chromatography.
6714238	3	40	theme	"	815:815	arg1	deficiency					827:836	a general "glycoprotein-specific" sialidase deficiency	783:836	a general "glycoprotein-specific" sialidase deficiency	783:836	The finding of these glycopeptides in urine shows that mucolipidosis I is characterized by a general "glycoprotein-specific" sialidase deficiency.
6714238	3	41	theme	general	785:791	arg1	deficiency					827:836	a general "glycoprotein-specific" sialidase deficiency	783:836	a general "glycoprotein-specific" sialidase deficiency	783:836	The finding of these glycopeptides in urine shows that mucolipidosis I is characterized by a general "glycoprotein-specific" sialidase deficiency.
6714238	2	42	theme	studies	533:539	arg1	combination					434:444	a combination	432:444	a combination of carbohydrate and amino acid analysis, dansylation, periodate oxidation, methylation studies, enzymatic hydrolysis and 1H-NMR spectroscopy	432:585	Their structures were determined by a combination of carbohydrate and amino acid analysis, dansylation, periodate oxidation, methylation studies, enzymatic hydrolysis and 1H-NMR spectroscopy, to be as follows: (formula; see text) wherein R = peptide linked through -Thr-, -Ser-Thr- or -Thr-Ser-.
6714238	1	43	contain	containing	135:144	arg1	Sialyl-glycopeptides					114:133	Sialyl-glycopeptides	114:133	Sialyl-glycopeptides containing an O-glycosidically linked tetrasaccharide chain	114:193	Sialyl-glycopeptides containing an O-glycosidically linked tetrasaccharide chain were obtained from the urine of a patient suffering from mucolipidosis I. Isolation of these compounds was achieved by gel filtration, ion-exchange chromatography and preparative paper chromatography.
6714238	1	43	contain	containing	135:144	arg2	chain					189:193	an O-glycosidically linked tetrasaccharide chain	146:193	an O-glycosidically linked tetrasaccharide chain	146:193	Sialyl-glycopeptides containing an O-glycosidically linked tetrasaccharide chain were obtained from the urine of a patient suffering from mucolipidosis I. Isolation of these compounds was achieved by gel filtration, ion-exchange chromatography and preparative paper chromatography.
6714238	2	44	dep	R	634:634	arg1	see					616:618	see	616:618	see text	616:623	Their structures were determined by a combination of carbohydrate and amino acid analysis, dansylation, periodate oxidation, methylation studies, enzymatic hydrolysis and 1H-NMR spectroscopy, to be as follows: (formula; see text) wherein R = peptide linked through -Thr-, -Ser-Thr- or -Thr-Ser-.
6714238	3	45	theme	glycoprotein-specific	794:814	arg1	deficiency					827:836	a general "glycoprotein-specific" sialidase deficiency	783:836	a general "glycoprotein-specific" sialidase deficiency	783:836	The finding of these glycopeptides in urine shows that mucolipidosis I is characterized by a general "glycoprotein-specific" sialidase deficiency.
6714238	1	46	theme	mucolipidosis	252:264	arg1	Isolation					269:277	mucolipidosis I. Isolation	252:277	mucolipidosis I. Isolation of these compounds	252:296	Sialyl-glycopeptides containing an O-glycosidically linked tetrasaccharide chain were obtained from the urine of a patient suffering from mucolipidosis I. Isolation of these compounds was achieved by gel filtration, ion-exchange chromatography and preparative paper chromatography.
11805077	5	0	theme	H-nuclear	800:808	arg1	resonance					819:827	(1)H-nuclear magnetic resonance	797:827	(1)H-nuclear magnetic resonance	797:827	The linkage position and branch-location of the sulfate group in the tetraantennary oligosaccharide were analyzed by (1)H-nuclear magnetic resonance.
11805077	5	1	theme	linkage	684:690	arg1	position					692:699	linkage position	684:699	linkage position	684:699	The linkage position and branch-location of the sulfate group in the tetraantennary oligosaccharide were analyzed by (1)H-nuclear magnetic resonance.
11805077	5	2	theme	magnetic	810:817	arg1	resonance					819:827	(1)H-nuclear magnetic resonance	797:827	(1)H-nuclear magnetic resonance	797:827	The linkage position and branch-location of the sulfate group in the tetraantennary oligosaccharide were analyzed by (1)H-nuclear magnetic resonance.
11805077	0	3	from	analysis	11:18	arg1	erythropoietin					61:74	erythropoietin	61:74	erythropoietin	61:74	Structural analysis of sulfated N-linked oligosaccharides in erythropoietin.
11805077	5	4	dep	resonance	819:827	arg1	1					798:798	1	798:798	1	798:798	The linkage position and branch-location of the sulfate group in the tetraantennary oligosaccharide were analyzed by (1)H-nuclear magnetic resonance.
11805077	1	5	theme	structural	269:278	arg1	analysis					280:287	the structural analysis	265:287	the structural analysis of carbohydrates in glycoproteins	265:321	We previously demonstrated that high-performance liquid chromatography with electrospray ionization mass spectrometry (LC/MS) equipped with a graphitized carbon column (GCC) is useful for the structural analysis of carbohydrates in glycoproteins.
11805077	2	6	link	N-linked	355:362	arg1	oligosaccharides					364:379	sulfated N-linked oligosaccharides	346:379	sulfated N-linked oligosaccharides	346:379	Using LC/MS with GCC, sulfated N-linked oligosaccharides were found in erythropoietin (EPO) expressed in baby hamster kidney cells.
11805077	3	7	from	EPO	523:525	arg1	part					478:481	a part	476:481	a part of the N-linked oligosaccharides in the EPO	476:525	Sulfation occurs in a part of the N-linked oligosaccharides in the EPO.
11805077	0	8	from	erythropoietin	61:74	arg1	analysis					11:18	Structural analysis	0:18	Structural analysis of sulfated N-linked oligosaccharides in erythropoietin	0:74	Structural analysis of sulfated N-linked oligosaccharides in erythropoietin.
11805077	5	9	from	branch-location	705:719	arg1	oligosaccharide					764:778	the tetraantennary oligosaccharide	745:778	the tetraantennary oligosaccharide	745:778	The linkage position and branch-location of the sulfate group in the tetraantennary oligosaccharide were analyzed by (1)H-nuclear magnetic resonance.
11805077	3	10	theme	N-linked	490:497	arg1	oligosaccharides					499:514	the N-linked oligosaccharides	486:514	the N-linked oligosaccharides in the EPO	486:525	Sulfation occurs in a part of the N-linked oligosaccharides in the EPO.
11805077	1	11	from	glycoproteins	309:321	arg1	analysis					280:287	the structural analysis	265:287	the structural analysis of carbohydrates in glycoproteins	265:321	We previously demonstrated that high-performance liquid chromatography with electrospray ionization mass spectrometry (LC/MS) equipped with a graphitized carbon column (GCC) is useful for the structural analysis of carbohydrates in glycoproteins.
11805077	4	12	theme	exoglycosidase	619:632	arg1	digestion					634:642	exoglycosidase digestion	619:642	exoglycosidase digestion followed by sugar mapping by LC/MS	619:677	Sulfated monosaccharide residue in the sulfated N-linked oligosaccharide was determined by exoglycosidase digestion followed by sugar mapping by LC/MS.
11805077	0	13	from	oligosaccharides	41:56	arg1	erythropoietin					61:74	erythropoietin	61:74	erythropoietin	61:74	Structural analysis of sulfated N-linked oligosaccharides in erythropoietin.
11805077	1	14	with	chromatography	133:146	arg1	LC/MS					196:200	electrospray ionization mass spectrometry (LC/MS)	153:201	electrospray ionization mass spectrometry (LC/MS) equipped with a graphitized carbon column (GCC)	153:249	We previously demonstrated that high-performance liquid chromatography with electrospray ionization mass spectrometry (LC/MS) equipped with a graphitized carbon column (GCC) is useful for the structural analysis of carbohydrates in glycoproteins.
11805077	1	15	from	carbohydrates	292:304	arg1	glycoproteins					309:321	glycoproteins	309:321	glycoproteins	309:321	We previously demonstrated that high-performance liquid chromatography with electrospray ionization mass spectrometry (LC/MS) equipped with a graphitized carbon column (GCC) is useful for the structural analysis of carbohydrates in glycoproteins.
11805077	4	16	theme	N-linked	576:583	arg1	oligosaccharide					585:599	the sulfated N-linked oligosaccharide	563:599	the sulfated N-linked oligosaccharide	563:599	Sulfated monosaccharide residue in the sulfated N-linked oligosaccharide was determined by exoglycosidase digestion followed by sugar mapping by LC/MS.
11805077	0	17	theme	Structural	0:9	arg1	analysis					11:18	Structural analysis	0:18	Structural analysis of sulfated N-linked oligosaccharides in erythropoietin	0:74	Structural analysis of sulfated N-linked oligosaccharides in erythropoietin.
11805077	1	18	theme	carbohydrates	292:304	arg1	analysis					280:287	the structural analysis	265:287	the structural analysis of carbohydrates in glycoproteins	265:321	We previously demonstrated that high-performance liquid chromatography with electrospray ionization mass spectrometry (LC/MS) equipped with a graphitized carbon column (GCC) is useful for the structural analysis of carbohydrates in glycoproteins.
11805077	3	19	from	oligosaccharides	499:514	arg1	EPO					523:525	the EPO	519:525	the EPO	519:525	Sulfation occurs in a part of the N-linked oligosaccharides in the EPO.
11805077	1	20	theme	high-performance	109:124	arg1	chromatography					133:146	high-performance liquid chromatography	109:146	high-performance liquid chromatography with electrospray ionization mass spectrometry (LC/MS) equipped with a graphitized carbon column (GCC)	109:249	We previously demonstrated that high-performance liquid chromatography with electrospray ionization mass spectrometry (LC/MS) equipped with a graphitized carbon column (GCC) is useful for the structural analysis of carbohydrates in glycoproteins.
11805077	1	21	theme	graphitized	219:229	arg1	column					238:243	a graphitized carbon column	217:243	a graphitized carbon column (GCC)	217:249	We previously demonstrated that high-performance liquid chromatography with electrospray ionization mass spectrometry (LC/MS) equipped with a graphitized carbon column (GCC) is useful for the structural analysis of carbohydrates in glycoproteins.
11805077	1	21	theme	graphitized	219:229	arg1	GCC					246:248	GCC	246:248	GCC	246:248	We previously demonstrated that high-performance liquid chromatography with electrospray ionization mass spectrometry (LC/MS) equipped with a graphitized carbon column (GCC) is useful for the structural analysis of carbohydrates in glycoproteins.
11805077	0	22	theme	sulfated	23:30	arg1	oligosaccharides					41:56	sulfated N-linked oligosaccharides	23:56	sulfated N-linked oligosaccharides in erythropoietin	23:74	Structural analysis of sulfated N-linked oligosaccharides in erythropoietin.
11805077	4	23	theme	sulfated	567:574	arg1	oligosaccharide					585:599	the sulfated N-linked oligosaccharide	563:599	the sulfated N-linked oligosaccharide	563:599	Sulfated monosaccharide residue in the sulfated N-linked oligosaccharide was determined by exoglycosidase digestion followed by sugar mapping by LC/MS.
11805077	1	24	from	analysis	280:287	arg1	glycoproteins					309:321	glycoproteins	309:321	glycoproteins	309:321	We previously demonstrated that high-performance liquid chromatography with electrospray ionization mass spectrometry (LC/MS) equipped with a graphitized carbon column (GCC) is useful for the structural analysis of carbohydrates in glycoproteins.
11805077	0	25	link	N-linked	32:39	arg1	oligosaccharides					41:56	sulfated N-linked oligosaccharides	23:56	sulfated N-linked oligosaccharides in erythropoietin	23:74	Structural analysis of sulfated N-linked oligosaccharides in erythropoietin.
11805077	1	26	theme	liquid	126:131	arg1	chromatography					133:146	high-performance liquid chromatography	109:146	high-performance liquid chromatography with electrospray ionization mass spectrometry (LC/MS) equipped with a graphitized carbon column (GCC)	109:249	We previously demonstrated that high-performance liquid chromatography with electrospray ionization mass spectrometry (LC/MS) equipped with a graphitized carbon column (GCC) is useful for the structural analysis of carbohydrates in glycoproteins.
11805077	1	27	theme	carbon	231:236	arg1	column					238:243	a graphitized carbon column	217:243	a graphitized carbon column (GCC)	217:249	We previously demonstrated that high-performance liquid chromatography with electrospray ionization mass spectrometry (LC/MS) equipped with a graphitized carbon column (GCC) is useful for the structural analysis of carbohydrates in glycoproteins.
11805077	1	27	theme	carbon	231:236	arg1	GCC					246:248	GCC	246:248	GCC	246:248	We previously demonstrated that high-performance liquid chromatography with electrospray ionization mass spectrometry (LC/MS) equipped with a graphitized carbon column (GCC) is useful for the structural analysis of carbohydrates in glycoproteins.
11805077	5	28	dep	position	692:699	arg1	The					680:682	The	680:682	The	680:682	The linkage position and branch-location of the sulfate group in the tetraantennary oligosaccharide were analyzed by (1)H-nuclear magnetic resonance.
11805077	2	29	theme	hamster	434:440	arg1	cells					449:453	baby hamster kidney cells	429:453	baby hamster kidney cells	429:453	Using LC/MS with GCC, sulfated N-linked oligosaccharides were found in erythropoietin (EPO) expressed in baby hamster kidney cells.
11805077	0	30	theme	oligosaccharides	41:56	arg1	analysis					11:18	Structural analysis	0:18	Structural analysis of sulfated N-linked oligosaccharides in erythropoietin	0:74	Structural analysis of sulfated N-linked oligosaccharides in erythropoietin.
11805077	2	31	theme	N-linked	355:362	arg1	oligosaccharides					364:379	sulfated N-linked oligosaccharides	346:379	sulfated N-linked oligosaccharides	346:379	Using LC/MS with GCC, sulfated N-linked oligosaccharides were found in erythropoietin (EPO) expressed in baby hamster kidney cells.
11805077	5	32	theme	tetraantennary	749:762	arg1	oligosaccharide					764:778	the tetraantennary oligosaccharide	745:778	the tetraantennary oligosaccharide	745:778	The linkage position and branch-location of the sulfate group in the tetraantennary oligosaccharide were analyzed by (1)H-nuclear magnetic resonance.
11805077	6	33	theme	located	899:905	arg1	position					880:887	the C-6 position	872:887	the C-6 position of GlcNAc located in the GlcNAcbeta1-4Manalpha1-3 branch	872:944	It was suggested that sulfation occurs on the C-6 position of GlcNAc located in the GlcNAcbeta1-4Manalpha1-3 branch.
11805077	2	34	theme	baby	429:432	arg1	cells					449:453	baby hamster kidney cells	429:453	baby hamster kidney cells	429:453	Using LC/MS with GCC, sulfated N-linked oligosaccharides were found in erythropoietin (EPO) expressed in baby hamster kidney cells.
11805077	0	35	theme	N-linked	32:39	arg1	oligosaccharides					41:56	sulfated N-linked oligosaccharides	23:56	sulfated N-linked oligosaccharides in erythropoietin	23:74	Structural analysis of sulfated N-linked oligosaccharides in erythropoietin.
11805077	6	36	theme	GlcNAc	892:897	arg1	position					880:887	the C-6 position	872:887	the C-6 position of GlcNAc located in the GlcNAcbeta1-4Manalpha1-3 branch	872:944	It was suggested that sulfation occurs on the C-6 position of GlcNAc located in the GlcNAcbeta1-4Manalpha1-3 branch.
11805077	4	37	theme	Sulfated	528:535	arg1	residue					552:558	Sulfated monosaccharide residue	528:558	Sulfated monosaccharide residue in the sulfated N-linked oligosaccharide	528:599	Sulfated monosaccharide residue in the sulfated N-linked oligosaccharide was determined by exoglycosidase digestion followed by sugar mapping by LC/MS.
11805077	6	38	from	branch	939:944	arg1	located					899:905	located	899:905	located	899:905	It was suggested that sulfation occurs on the C-6 position of GlcNAc located in the GlcNAcbeta1-4Manalpha1-3 branch.
11805077	4	39	from	residue	552:558	arg1	oligosaccharide					585:599	the sulfated N-linked oligosaccharide	563:599	the sulfated N-linked oligosaccharide	563:599	Sulfated monosaccharide residue in the sulfated N-linked oligosaccharide was determined by exoglycosidase digestion followed by sugar mapping by LC/MS.
11805077	4	40	theme	monosaccharide	537:550	arg1	residue					552:558	Sulfated monosaccharide residue	528:558	Sulfated monosaccharide residue in the sulfated N-linked oligosaccharide	528:599	Sulfated monosaccharide residue in the sulfated N-linked oligosaccharide was determined by exoglycosidase digestion followed by sugar mapping by LC/MS.
11805077	6	41	theme	GlcNAcbeta1-4Manalpha1-3	914:937	arg1	branch					939:944	the GlcNAcbeta1-4Manalpha1-3 branch	910:944	the GlcNAcbeta1-4Manalpha1-3 branch	910:944	It was suggested that sulfation occurs on the C-6 position of GlcNAc located in the GlcNAcbeta1-4Manalpha1-3 branch.
11805077	3	42	theme	oligosaccharides	499:514	arg1	part					478:481	a part	476:481	a part of the N-linked oligosaccharides in the EPO	476:525	Sulfation occurs in a part of the N-linked oligosaccharides in the EPO.
11805077	2	43	located	found	386:390	arg2	oligosaccharides					364:379	sulfated N-linked oligosaccharides	346:379	sulfated N-linked oligosaccharides	346:379	Using LC/MS with GCC, sulfated N-linked oligosaccharides were found in erythropoietin (EPO) expressed in baby hamster kidney cells.
11805077	2	43	located	found	386:390	arg1	EPO					411:413	EPO	411:413	EPO	411:413	Using LC/MS with GCC, sulfated N-linked oligosaccharides were found in erythropoietin (EPO) expressed in baby hamster kidney cells.
11805077	2	43	located	found	386:390	arg1	erythropoietin					395:408	erythropoietin	395:408	erythropoietin (EPO) expressed in baby hamster kidney cells	395:453	Using LC/MS with GCC, sulfated N-linked oligosaccharides were found in erythropoietin (EPO) expressed in baby hamster kidney cells.
11805077	3	44	link	N-linked	490:497	arg1	oligosaccharides					499:514	the N-linked oligosaccharides	486:514	the N-linked oligosaccharides in the EPO	486:525	Sulfation occurs in a part of the N-linked oligosaccharides in the EPO.
11805077	3	45	from	part	478:481	arg1	EPO					523:525	the EPO	519:525	the EPO	519:525	Sulfation occurs in a part of the N-linked oligosaccharides in the EPO.
11805077	1	46	theme	electrospray	153:164	arg1	LC/MS					196:200	electrospray ionization mass spectrometry (LC/MS)	153:201	electrospray ionization mass spectrometry (LC/MS) equipped with a graphitized carbon column (GCC)	153:249	We previously demonstrated that high-performance liquid chromatography with electrospray ionization mass spectrometry (LC/MS) equipped with a graphitized carbon column (GCC) is useful for the structural analysis of carbohydrates in glycoproteins.
11805077	5	47	from	position	692:699	arg1	oligosaccharide					764:778	the tetraantennary oligosaccharide	745:778	the tetraantennary oligosaccharide	745:778	The linkage position and branch-location of the sulfate group in the tetraantennary oligosaccharide were analyzed by (1)H-nuclear magnetic resonance.
11805077	5	48	theme	sulfate	728:734	arg1	group					736:740	the sulfate group	724:740	the sulfate group	724:740	The linkage position and branch-location of the sulfate group in the tetraantennary oligosaccharide were analyzed by (1)H-nuclear magnetic resonance.
11805077	6	49	theme	C-6	876:878	arg1	position					880:887	the C-6 position	872:887	the C-6 position of GlcNAc located in the GlcNAcbeta1-4Manalpha1-3 branch	872:944	It was suggested that sulfation occurs on the C-6 position of GlcNAc located in the GlcNAcbeta1-4Manalpha1-3 branch.
11805077	1	50	gly	glycoproteins	309:321	arg1	glycoproteins					309:321	glycoproteins	309:321	glycoproteins	309:321	We previously demonstrated that high-performance liquid chromatography with electrospray ionization mass spectrometry (LC/MS) equipped with a graphitized carbon column (GCC) is useful for the structural analysis of carbohydrates in glycoproteins.
11805077	1	51	theme	ionization	166:175	arg1	LC/MS					196:200	electrospray ionization mass spectrometry (LC/MS)	153:201	electrospray ionization mass spectrometry (LC/MS) equipped with a graphitized carbon column (GCC)	153:249	We previously demonstrated that high-performance liquid chromatography with electrospray ionization mass spectrometry (LC/MS) equipped with a graphitized carbon column (GCC) is useful for the structural analysis of carbohydrates in glycoproteins.
11805077	5	52	theme	group	736:740	arg1	position					692:699	linkage position	684:699	linkage position	684:699	The linkage position and branch-location of the sulfate group in the tetraantennary oligosaccharide were analyzed by (1)H-nuclear magnetic resonance.
11805077	5	52	theme	group	736:740	arg1	branch-location					705:719	branch-location	705:719	branch-location	705:719	The linkage position and branch-location of the sulfate group in the tetraantennary oligosaccharide were analyzed by (1)H-nuclear magnetic resonance.
11805077	1	53	theme	mass	177:180	arg1	LC/MS					196:200	electrospray ionization mass spectrometry (LC/MS)	153:201	electrospray ionization mass spectrometry (LC/MS) equipped with a graphitized carbon column (GCC)	153:249	We previously demonstrated that high-performance liquid chromatography with electrospray ionization mass spectrometry (LC/MS) equipped with a graphitized carbon column (GCC) is useful for the structural analysis of carbohydrates in glycoproteins.
11805077	2	54	theme	sulfated	346:353	arg1	oligosaccharides					364:379	sulfated N-linked oligosaccharides	346:379	sulfated N-linked oligosaccharides	346:379	Using LC/MS with GCC, sulfated N-linked oligosaccharides were found in erythropoietin (EPO) expressed in baby hamster kidney cells.
11805077	2	55	theme	kidney	442:447	arg1	cells					449:453	baby hamster kidney cells	429:453	baby hamster kidney cells	429:453	Using LC/MS with GCC, sulfated N-linked oligosaccharides were found in erythropoietin (EPO) expressed in baby hamster kidney cells.
11805077	1	56	theme	spectrometry	182:193	arg1	LC/MS					196:200	electrospray ionization mass spectrometry (LC/MS)	153:201	electrospray ionization mass spectrometry (LC/MS) equipped with a graphitized carbon column (GCC)	153:249	We previously demonstrated that high-performance liquid chromatography with electrospray ionization mass spectrometry (LC/MS) equipped with a graphitized carbon column (GCC) is useful for the structural analysis of carbohydrates in glycoproteins.
11805077	6	57	from	located	899:905	arg1	branch					939:944	the GlcNAcbeta1-4Manalpha1-3 branch	910:944	the GlcNAcbeta1-4Manalpha1-3 branch	910:944	It was suggested that sulfation occurs on the C-6 position of GlcNAc located in the GlcNAcbeta1-4Manalpha1-3 branch.
11805077	4	58	link	N-linked	576:583	arg1	oligosaccharide					585:599	the sulfated N-linked oligosaccharide	563:599	the sulfated N-linked oligosaccharide	563:599	Sulfated monosaccharide residue in the sulfated N-linked oligosaccharide was determined by exoglycosidase digestion followed by sugar mapping by LC/MS.
11805077	4	59	theme	sugar	656:660	arg1	mapping					662:668	sugar mapping	656:668	sugar mapping	656:668	Sulfated monosaccharide residue in the sulfated N-linked oligosaccharide was determined by exoglycosidase digestion followed by sugar mapping by LC/MS.
3571205	3	0	from	chromatography	729:742	arg1	column					756:761	a Mono Q column	747:761	a Mono Q column	747:761	The structures of the two major oligosaccharide-alditols separated by ion-exchange chromatography on a Mono Q column were investigated by means of methylation analysis, glycosidase digestion, and Smith periodate degradation, and they were assigned as typical di- and trisialylated complex-type oligosaccharide-alditols with two and three peripheral chains consisting of Gal-GlcNAc sequences, respectively.
3571205	3	1	theme	Mono	749:752	arg1	column					756:761	a Mono Q column	747:761	a Mono Q column	747:761	The structures of the two major oligosaccharide-alditols separated by ion-exchange chromatography on a Mono Q column were investigated by means of methylation analysis, glycosidase digestion, and Smith periodate degradation, and they were assigned as typical di- and trisialylated complex-type oligosaccharide-alditols with two and three peripheral chains consisting of Gal-GlcNAc sequences, respectively.
3571205	3	2	theme	periodate	848:856	arg1	degradation					858:868	Smith periodate degradation	842:868	Smith periodate degradation	842:868	The structures of the two major oligosaccharide-alditols separated by ion-exchange chromatography on a Mono Q column were investigated by means of methylation analysis, glycosidase digestion, and Smith periodate degradation, and they were assigned as typical di- and trisialylated complex-type oligosaccharide-alditols with two and three peripheral chains consisting of Gal-GlcNAc sequences, respectively.
3571205	0	3	theme	Asn-linked	84:93	arg1	chains					101:106	the major Asn-linked sugar chains	74:106	the major Asn-linked sugar chains	74:106	The carbohydrate moiety of human platelet glycocalicin: the structures of the major Asn-linked sugar chains.
3571205	3	4	with	di-	905:907	arg1	chains					995:1000	two and three peripheral chains	970:1000	two and three peripheral chains consisting of Gal-GlcNAc sequences, respectively	970:1049	The structures of the two major oligosaccharide-alditols separated by ion-exchange chromatography on a Mono Q column were investigated by means of methylation analysis, glycosidase digestion, and Smith periodate degradation, and they were assigned as typical di- and trisialylated complex-type oligosaccharide-alditols with two and three peripheral chains consisting of Gal-GlcNAc sequences, respectively.
3571205	3	5	theme	methylation	793:803	arg1	analysis					805:812	methylation analysis	793:812	methylation analysis	793:812	The structures of the two major oligosaccharide-alditols separated by ion-exchange chromatography on a Mono Q column were investigated by means of methylation analysis, glycosidase digestion, and Smith periodate degradation, and they were assigned as typical di- and trisialylated complex-type oligosaccharide-alditols with two and three peripheral chains consisting of Gal-GlcNAc sequences, respectively.
3571205	3	6	theme	Gal-GlcNAc	1016:1025	arg1	sequences					1027:1035	Gal-GlcNAc sequences	1016:1035	Gal-GlcNAc sequences	1016:1035	The structures of the two major oligosaccharide-alditols separated by ion-exchange chromatography on a Mono Q column were investigated by means of methylation analysis, glycosidase digestion, and Smith periodate degradation, and they were assigned as typical di- and trisialylated complex-type oligosaccharide-alditols with two and three peripheral chains consisting of Gal-GlcNAc sequences, respectively.
3571205	0	7	theme	major	78:82	arg1	chains					101:106	the major Asn-linked sugar chains	74:106	the major Asn-linked sugar chains	74:106	The carbohydrate moiety of human platelet glycocalicin: the structures of the major Asn-linked sugar chains.
3571205	1	8	theme	wheat	341:345	arg1	agglutinin-Sepharose					352:371	wheat germ agglutinin-Sepharose and Mono Q. Asparagine-linked (N-linked) oligosaccharides	341:429	agglutinin-Sepharose	352:371	Glycocalicin, a predominant glycoprotein on the human platelet surface, has been purified from a platelet suspension by means of sonication, ammonium sulfate precipitation and acid treatment followed by chromatography on columns of wheat germ agglutinin-Sepharose and Mono Q. Asparagine-linked (N-linked) oligosaccharides were released by hydrazinolysis, and then N-acetylated and reduced with NaBH4 or NaB3H4.
3571205	3	9	theme	complex-type	927:938	arg1	they					875:878	they	875:878	they	875:878	The structures of the two major oligosaccharide-alditols separated by ion-exchange chromatography on a Mono Q column were investigated by means of methylation analysis, glycosidase digestion, and Smith periodate degradation, and they were assigned as typical di- and trisialylated complex-type oligosaccharide-alditols with two and three peripheral chains consisting of Gal-GlcNAc sequences, respectively.
3571205	3	9	theme	complex-type	927:938	arg1	oligosaccharide-alditols					940:963	trisialylated complex-type oligosaccharide-alditols	913:963	trisialylated complex-type oligosaccharide-alditols with two and three peripheral chains consisting of Gal-GlcNAc sequences, respectively	913:1049	The structures of the two major oligosaccharide-alditols separated by ion-exchange chromatography on a Mono Q column were investigated by means of methylation analysis, glycosidase digestion, and Smith periodate degradation, and they were assigned as typical di- and trisialylated complex-type oligosaccharide-alditols with two and three peripheral chains consisting of Gal-GlcNAc sequences, respectively.
3571205	3	10	theme	Smith	842:846	arg1	degradation					858:868	Smith periodate degradation	842:868	Smith periodate degradation	842:868	The structures of the two major oligosaccharide-alditols separated by ion-exchange chromatography on a Mono Q column were investigated by means of methylation analysis, glycosidase digestion, and Smith periodate degradation, and they were assigned as typical di- and trisialylated complex-type oligosaccharide-alditols with two and three peripheral chains consisting of Gal-GlcNAc sequences, respectively.
3571205	0	11	theme	chains	101:106	arg1	structures					60:69	the structures	56:69	The carbohydrate moiety of human platelet glycocalicin: the structures of the major Asn-linked sugar chains.	0:107	The carbohydrate moiety of human platelet glycocalicin: the structures of the major Asn-linked sugar chains.
3571205	1	12	theme	germ	347:350	arg1	agglutinin-Sepharose					352:371	wheat germ agglutinin-Sepharose and Mono Q. Asparagine-linked (N-linked) oligosaccharides	341:429	agglutinin-Sepharose	352:371	Glycocalicin, a predominant glycoprotein on the human platelet surface, has been purified from a platelet suspension by means of sonication, ammonium sulfate precipitation and acid treatment followed by chromatography on columns of wheat germ agglutinin-Sepharose and Mono Q. Asparagine-linked (N-linked) oligosaccharides were released by hydrazinolysis, and then N-acetylated and reduced with NaBH4 or NaB3H4.
3571205	1	13	from	glycoprotein	137:148	arg1	surface					172:178	the human platelet surface	153:178	the human platelet surface	153:178	Glycocalicin, a predominant glycoprotein on the human platelet surface, has been purified from a platelet suspension by means of sonication, ammonium sulfate precipitation and acid treatment followed by chromatography on columns of wheat germ agglutinin-Sepharose and Mono Q. Asparagine-linked (N-linked) oligosaccharides were released by hydrazinolysis, and then N-acetylated and reduced with NaBH4 or NaB3H4.
3571205	1	14	theme	human	157:161	arg1	surface					172:178	the human platelet surface	153:178	the human platelet surface	153:178	Glycocalicin, a predominant glycoprotein on the human platelet surface, has been purified from a platelet suspension by means of sonication, ammonium sulfate precipitation and acid treatment followed by chromatography on columns of wheat germ agglutinin-Sepharose and Mono Q. Asparagine-linked (N-linked) oligosaccharides were released by hydrazinolysis, and then N-acetylated and reduced with NaBH4 or NaB3H4.
3571205	0	15	theme	sugar	95:99	arg1	chains					101:106	the major Asn-linked sugar chains	74:106	the major Asn-linked sugar chains	74:106	The carbohydrate moiety of human platelet glycocalicin: the structures of the major Asn-linked sugar chains.
3571205	1	16	theme	agglutinin-Sepharose	352:371	arg1	columns					330:336	columns	330:336	columns of wheat germ agglutinin-Sepharose and Mono Q. Asparagine-linked (N-linked) oligosaccharides	330:429	Glycocalicin, a predominant glycoprotein on the human platelet surface, has been purified from a platelet suspension by means of sonication, ammonium sulfate precipitation and acid treatment followed by chromatography on columns of wheat germ agglutinin-Sepharose and Mono Q. Asparagine-linked (N-linked) oligosaccharides were released by hydrazinolysis, and then N-acetylated and reduced with NaBH4 or NaB3H4.
3571205	2	17	theme	lectin	630:635	arg1	columns					637:643	immobilized lectin columns	618:643	immobilized lectin columns	618:643	The released carbohydrate chains were found to be of the complex-type from their interaction with immobilized lectin columns.
3571205	2	18	with	interaction	601:611	arg1	columns					637:643	immobilized lectin columns	618:643	immobilized lectin columns	618:643	The released carbohydrate chains were found to be of the complex-type from their interaction with immobilized lectin columns.
3571205	1	19	theme	platelet	163:170	arg1	surface					172:178	the human platelet surface	153:178	the human platelet surface	153:178	Glycocalicin, a predominant glycoprotein on the human platelet surface, has been purified from a platelet suspension by means of sonication, ammonium sulfate precipitation and acid treatment followed by chromatography on columns of wheat germ agglutinin-Sepharose and Mono Q. Asparagine-linked (N-linked) oligosaccharides were released by hydrazinolysis, and then N-acetylated and reduced with NaBH4 or NaB3H4.
3571205	0	20	theme	carbohydrate	4:15	arg1	moiety					17:22	The carbohydrate moiety	0:22	The carbohydrate moiety of human platelet glycocalicin: the structures of the major Asn-linked sugar chains.	0:107	The carbohydrate moiety of human platelet glycocalicin: the structures of the major Asn-linked sugar chains.
3571205	2	21	theme	immobilized	618:628	arg1	columns					637:643	immobilized lectin columns	618:643	immobilized lectin columns	618:643	The released carbohydrate chains were found to be of the complex-type from their interaction with immobilized lectin columns.
3571205	3	22	theme	Q	754:754	arg1	column					756:761	a Mono Q column	747:761	a Mono Q column	747:761	The structures of the two major oligosaccharide-alditols separated by ion-exchange chromatography on a Mono Q column were investigated by means of methylation analysis, glycosidase digestion, and Smith periodate degradation, and they were assigned as typical di- and trisialylated complex-type oligosaccharide-alditols with two and three peripheral chains consisting of Gal-GlcNAc sequences, respectively.
3571205	1	23	theme	ammonium	250:257	arg1	precipitation					267:279	ammonium sulfate precipitation	250:279	ammonium sulfate precipitation	250:279	Glycocalicin, a predominant glycoprotein on the human platelet surface, has been purified from a platelet suspension by means of sonication, ammonium sulfate precipitation and acid treatment followed by chromatography on columns of wheat germ agglutinin-Sepharose and Mono Q. Asparagine-linked (N-linked) oligosaccharides were released by hydrazinolysis, and then N-acetylated and reduced with NaBH4 or NaB3H4.
3571205	1	24	dep	sonication	238:247	arg1	released					436:443	released	436:443	were released by hydrazinolysis	431:461	Glycocalicin, a predominant glycoprotein on the human platelet surface, has been purified from a platelet suspension by means of sonication, ammonium sulfate precipitation and acid treatment followed by chromatography on columns of wheat germ agglutinin-Sepharose and Mono Q. Asparagine-linked (N-linked) oligosaccharides were released by hydrazinolysis, and then N-acetylated and reduced with NaBH4 or NaB3H4.
3571205	1	24	dep	sonication	238:247	arg1	N-acetylated					473:484	N-acetylated	473:484	N-acetylated	473:484	Glycocalicin, a predominant glycoprotein on the human platelet surface, has been purified from a platelet suspension by means of sonication, ammonium sulfate precipitation and acid treatment followed by chromatography on columns of wheat germ agglutinin-Sepharose and Mono Q. Asparagine-linked (N-linked) oligosaccharides were released by hydrazinolysis, and then N-acetylated and reduced with NaBH4 or NaB3H4.
3571205	1	25	theme	sulfate	259:265	arg1	precipitation					267:279	ammonium sulfate precipitation	250:279	ammonium sulfate precipitation	250:279	Glycocalicin, a predominant glycoprotein on the human platelet surface, has been purified from a platelet suspension by means of sonication, ammonium sulfate precipitation and acid treatment followed by chromatography on columns of wheat germ agglutinin-Sepharose and Mono Q. Asparagine-linked (N-linked) oligosaccharides were released by hydrazinolysis, and then N-acetylated and reduced with NaBH4 or NaB3H4.
3571205	2	26	from	interaction	601:611	arg1	complex-type					577:588	the complex-type	573:588	the complex-type	573:588	The released carbohydrate chains were found to be of the complex-type from their interaction with immobilized lectin columns.
3571205	1	27	theme	Mono	377:380	arg1	oligosaccharides					414:429	wheat germ agglutinin-Sepharose and Mono Q. Asparagine-linked (N-linked) oligosaccharides	341:429	oligosaccharides	414:429	Glycocalicin, a predominant glycoprotein on the human platelet surface, has been purified from a platelet suspension by means of sonication, ammonium sulfate precipitation and acid treatment followed by chromatography on columns of wheat germ agglutinin-Sepharose and Mono Q. Asparagine-linked (N-linked) oligosaccharides were released by hydrazinolysis, and then N-acetylated and reduced with NaBH4 or NaB3H4.
3571205	0	28	theme	platelet	33:40	arg1	glycocalicin					42:53	human platelet glycocalicin	27:53	human platelet glycocalicin	27:53	The carbohydrate moiety of human platelet glycocalicin: the structures of the major Asn-linked sugar chains.
3571205	1	29	theme	Q.	382:383	arg1	oligosaccharides					414:429	wheat germ agglutinin-Sepharose and Mono Q. Asparagine-linked (N-linked) oligosaccharides	341:429	oligosaccharides	414:429	Glycocalicin, a predominant glycoprotein on the human platelet surface, has been purified from a platelet suspension by means of sonication, ammonium sulfate precipitation and acid treatment followed by chromatography on columns of wheat germ agglutinin-Sepharose and Mono Q. Asparagine-linked (N-linked) oligosaccharides were released by hydrazinolysis, and then N-acetylated and reduced with NaBH4 or NaB3H4.
3571205	0	30	theme	human	27:31	arg1	glycocalicin					42:53	human platelet glycocalicin	27:53	human platelet glycocalicin	27:53	The carbohydrate moiety of human platelet glycocalicin: the structures of the major Asn-linked sugar chains.
3571205	1	31	theme	acid	285:288	arg1	treatment					290:298	acid treatment	285:298	acid treatment	285:298	Glycocalicin, a predominant glycoprotein on the human platelet surface, has been purified from a platelet suspension by means of sonication, ammonium sulfate precipitation and acid treatment followed by chromatography on columns of wheat germ agglutinin-Sepharose and Mono Q. Asparagine-linked (N-linked) oligosaccharides were released by hydrazinolysis, and then N-acetylated and reduced with NaBH4 or NaB3H4.
3571205	2	32	theme	carbohydrate	533:544	arg1	chains					546:551	The released carbohydrate chains	520:551	The released carbohydrate chains	520:551	The released carbohydrate chains were found to be of the complex-type from their interaction with immobilized lectin columns.
3571205	1	33	theme	Asparagine-linked	385:401	arg1	oligosaccharides					414:429	wheat germ agglutinin-Sepharose and Mono Q. Asparagine-linked (N-linked) oligosaccharides	341:429	oligosaccharides	414:429	Glycocalicin, a predominant glycoprotein on the human platelet surface, has been purified from a platelet suspension by means of sonication, ammonium sulfate precipitation and acid treatment followed by chromatography on columns of wheat germ agglutinin-Sepharose and Mono Q. Asparagine-linked (N-linked) oligosaccharides were released by hydrazinolysis, and then N-acetylated and reduced with NaBH4 or NaB3H4.
3571205	1	34	from	chromatography	312:325	arg1	columns					330:336	columns	330:336	columns of wheat germ agglutinin-Sepharose and Mono Q. Asparagine-linked (N-linked) oligosaccharides	330:429	Glycocalicin, a predominant glycoprotein on the human platelet surface, has been purified from a platelet suspension by means of sonication, ammonium sulfate precipitation and acid treatment followed by chromatography on columns of wheat germ agglutinin-Sepharose and Mono Q. Asparagine-linked (N-linked) oligosaccharides were released by hydrazinolysis, and then N-acetylated and reduced with NaBH4 or NaB3H4.
3571205	2	35	theme	released	524:531	arg1	chains					546:551	The released carbohydrate chains	520:551	The released carbohydrate chains	520:551	The released carbohydrate chains were found to be of the complex-type from their interaction with immobilized lectin columns.
3571205	1	36	gly	glycoprotein	137:148	arg1	glycoprotein					137:148	a predominant glycoprotein	123:148	a predominant glycoprotein on the human platelet surface	123:178	Glycocalicin, a predominant glycoprotein on the human platelet surface, has been purified from a platelet suspension by means of sonication, ammonium sulfate precipitation and acid treatment followed by chromatography on columns of wheat germ agglutinin-Sepharose and Mono Q. Asparagine-linked (N-linked) oligosaccharides were released by hydrazinolysis, and then N-acetylated and reduced with NaBH4 or NaB3H4.
3571205	1	36	gly	glycoprotein	137:148	arg1	Glycocalicin					109:120	Glycocalicin	109:120	Glycocalicin	109:120	Glycocalicin, a predominant glycoprotein on the human platelet surface, has been purified from a platelet suspension by means of sonication, ammonium sulfate precipitation and acid treatment followed by chromatography on columns of wheat germ agglutinin-Sepharose and Mono Q. Asparagine-linked (N-linked) oligosaccharides were released by hydrazinolysis, and then N-acetylated and reduced with NaBH4 or NaB3H4.
3571205	0	37	theme	glycocalicin	42:53	arg1	moiety					17:22	The carbohydrate moiety	0:22	The carbohydrate moiety of human platelet glycocalicin: the structures of the major Asn-linked sugar chains.	0:107	The carbohydrate moiety of human platelet glycocalicin: the structures of the major Asn-linked sugar chains.
3571205	1	38	theme	N-linked	404:411	arg1	oligosaccharides					414:429	wheat germ agglutinin-Sepharose and Mono Q. Asparagine-linked (N-linked) oligosaccharides	341:429	oligosaccharides	414:429	Glycocalicin, a predominant glycoprotein on the human platelet surface, has been purified from a platelet suspension by means of sonication, ammonium sulfate precipitation and acid treatment followed by chromatography on columns of wheat germ agglutinin-Sepharose and Mono Q. Asparagine-linked (N-linked) oligosaccharides were released by hydrazinolysis, and then N-acetylated and reduced with NaBH4 or NaB3H4.
3571205	3	39	theme	peripheral	984:993	arg1	chains					995:1000	two and three peripheral chains	970:1000	two and three peripheral chains consisting of Gal-GlcNAc sequences, respectively	970:1049	The structures of the two major oligosaccharide-alditols separated by ion-exchange chromatography on a Mono Q column were investigated by means of methylation analysis, glycosidase digestion, and Smith periodate degradation, and they were assigned as typical di- and trisialylated complex-type oligosaccharide-alditols with two and three peripheral chains consisting of Gal-GlcNAc sequences, respectively.
3571205	3	40	theme	oligosaccharide-alditols	678:701	arg1	structures					650:659	The structures	646:659	The structures of the two major oligosaccharide-alditols separated by ion-exchange chromatography on a Mono Q column	646:761	The structures of the two major oligosaccharide-alditols separated by ion-exchange chromatography on a Mono Q column were investigated by means of methylation analysis, glycosidase digestion, and Smith periodate degradation, and they were assigned as typical di- and trisialylated complex-type oligosaccharide-alditols with two and three peripheral chains consisting of Gal-GlcNAc sequences, respectively.
3571205	3	41	theme	trisialylated	913:925	arg1	they					875:878	they	875:878	they	875:878	The structures of the two major oligosaccharide-alditols separated by ion-exchange chromatography on a Mono Q column were investigated by means of methylation analysis, glycosidase digestion, and Smith periodate degradation, and they were assigned as typical di- and trisialylated complex-type oligosaccharide-alditols with two and three peripheral chains consisting of Gal-GlcNAc sequences, respectively.
3571205	3	41	theme	trisialylated	913:925	arg1	oligosaccharide-alditols					940:963	trisialylated complex-type oligosaccharide-alditols	913:963	trisialylated complex-type oligosaccharide-alditols with two and three peripheral chains consisting of Gal-GlcNAc sequences, respectively	913:1049	The structures of the two major oligosaccharide-alditols separated by ion-exchange chromatography on a Mono Q column were investigated by means of methylation analysis, glycosidase digestion, and Smith periodate degradation, and they were assigned as typical di- and trisialylated complex-type oligosaccharide-alditols with two and three peripheral chains consisting of Gal-GlcNAc sequences, respectively.
3571205	3	42	gly	trisialylated	913:925	arg1	they					875:878	they	875:878	they	875:878	The structures of the two major oligosaccharide-alditols separated by ion-exchange chromatography on a Mono Q column were investigated by means of methylation analysis, glycosidase digestion, and Smith periodate degradation, and they were assigned as typical di- and trisialylated complex-type oligosaccharide-alditols with two and three peripheral chains consisting of Gal-GlcNAc sequences, respectively.
3571205	3	42	gly	trisialylated	913:925	arg1	oligosaccharide-alditols					940:963	trisialylated complex-type oligosaccharide-alditols	913:963	trisialylated complex-type oligosaccharide-alditols with two and three peripheral chains consisting of Gal-GlcNAc sequences, respectively	913:1049	The structures of the two major oligosaccharide-alditols separated by ion-exchange chromatography on a Mono Q column were investigated by means of methylation analysis, glycosidase digestion, and Smith periodate degradation, and they were assigned as typical di- and trisialylated complex-type oligosaccharide-alditols with two and three peripheral chains consisting of Gal-GlcNAc sequences, respectively.
3571205	1	43	theme	oligosaccharides	414:429	arg1	columns					330:336	columns	330:336	columns of wheat germ agglutinin-Sepharose and Mono Q. Asparagine-linked (N-linked) oligosaccharides	330:429	Glycocalicin, a predominant glycoprotein on the human platelet surface, has been purified from a platelet suspension by means of sonication, ammonium sulfate precipitation and acid treatment followed by chromatography on columns of wheat germ agglutinin-Sepharose and Mono Q. Asparagine-linked (N-linked) oligosaccharides were released by hydrazinolysis, and then N-acetylated and reduced with NaBH4 or NaB3H4.
3571205	0	44	dep	moiety	17:22	arg1	structures					60:69	the structures	56:69	The carbohydrate moiety of human platelet glycocalicin: the structures of the major Asn-linked sugar chains.	0:107	The carbohydrate moiety of human platelet glycocalicin: the structures of the major Asn-linked sugar chains.
3571205	1	45	link	N-linked	404:411	arg1	oligosaccharides					414:429	wheat germ agglutinin-Sepharose and Mono Q. Asparagine-linked (N-linked) oligosaccharides	341:429	oligosaccharides	414:429	Glycocalicin, a predominant glycoprotein on the human platelet surface, has been purified from a platelet suspension by means of sonication, ammonium sulfate precipitation and acid treatment followed by chromatography on columns of wheat germ agglutinin-Sepharose and Mono Q. Asparagine-linked (N-linked) oligosaccharides were released by hydrazinolysis, and then N-acetylated and reduced with NaBH4 or NaB3H4.
3571205	1	46	theme	platelet	206:213	arg1	suspension					215:224	a platelet suspension	204:224	a platelet suspension	204:224	Glycocalicin, a predominant glycoprotein on the human platelet surface, has been purified from a platelet suspension by means of sonication, ammonium sulfate precipitation and acid treatment followed by chromatography on columns of wheat germ agglutinin-Sepharose and Mono Q. Asparagine-linked (N-linked) oligosaccharides were released by hydrazinolysis, and then N-acetylated and reduced with NaBH4 or NaB3H4.
3571205	3	47	with	oligosaccharide-alditols	940:963	arg1	chains					995:1000	two and three peripheral chains	970:1000	two and three peripheral chains consisting of Gal-GlcNAc sequences, respectively	970:1049	The structures of the two major oligosaccharide-alditols separated by ion-exchange chromatography on a Mono Q column were investigated by means of methylation analysis, glycosidase digestion, and Smith periodate degradation, and they were assigned as typical di- and trisialylated complex-type oligosaccharide-alditols with two and three peripheral chains consisting of Gal-GlcNAc sequences, respectively.
3571205	3	48	theme	typical	897:903	arg1	they					875:878	they	875:878	they	875:878	The structures of the two major oligosaccharide-alditols separated by ion-exchange chromatography on a Mono Q column were investigated by means of methylation analysis, glycosidase digestion, and Smith periodate degradation, and they were assigned as typical di- and trisialylated complex-type oligosaccharide-alditols with two and three peripheral chains consisting of Gal-GlcNAc sequences, respectively.
3571205	3	48	theme	typical	897:903	arg1	di-					905:907	typical di-	897:907	typical di-	897:907	The structures of the two major oligosaccharide-alditols separated by ion-exchange chromatography on a Mono Q column were investigated by means of methylation analysis, glycosidase digestion, and Smith periodate degradation, and they were assigned as typical di- and trisialylated complex-type oligosaccharide-alditols with two and three peripheral chains consisting of Gal-GlcNAc sequences, respectively.
3571205	1	49	theme	predominant	125:135	arg1	glycoprotein					137:148	a predominant glycoprotein	123:148	a predominant glycoprotein on the human platelet surface	123:178	Glycocalicin, a predominant glycoprotein on the human platelet surface, has been purified from a platelet suspension by means of sonication, ammonium sulfate precipitation and acid treatment followed by chromatography on columns of wheat germ agglutinin-Sepharose and Mono Q. Asparagine-linked (N-linked) oligosaccharides were released by hydrazinolysis, and then N-acetylated and reduced with NaBH4 or NaB3H4.
3571205	1	49	theme	predominant	125:135	arg1	Glycocalicin					109:120	Glycocalicin	109:120	Glycocalicin	109:120	Glycocalicin, a predominant glycoprotein on the human platelet surface, has been purified from a platelet suspension by means of sonication, ammonium sulfate precipitation and acid treatment followed by chromatography on columns of wheat germ agglutinin-Sepharose and Mono Q. Asparagine-linked (N-linked) oligosaccharides were released by hydrazinolysis, and then N-acetylated and reduced with NaBH4 or NaB3H4.
3571205	3	50	theme	major	672:676	arg1	oligosaccharide-alditols					678:701	the two major oligosaccharide-alditols	664:701	the two major oligosaccharide-alditols separated by ion-exchange chromatography on a Mono Q column	664:761	The structures of the two major oligosaccharide-alditols separated by ion-exchange chromatography on a Mono Q column were investigated by means of methylation analysis, glycosidase digestion, and Smith periodate degradation, and they were assigned as typical di- and trisialylated complex-type oligosaccharide-alditols with two and three peripheral chains consisting of Gal-GlcNAc sequences, respectively.
3571205	3	51	theme	ion-exchange	716:727	arg1	chromatography					729:742	ion-exchange chromatography	716:742	ion-exchange chromatography on a Mono Q column	716:761	The structures of the two major oligosaccharide-alditols separated by ion-exchange chromatography on a Mono Q column were investigated by means of methylation analysis, glycosidase digestion, and Smith periodate degradation, and they were assigned as typical di- and trisialylated complex-type oligosaccharide-alditols with two and three peripheral chains consisting of Gal-GlcNAc sequences, respectively.
3571205	0	52	link	Asn-linked	84:93	arg1	chains					101:106	the major Asn-linked sugar chains	74:106	the major Asn-linked sugar chains	74:106	The carbohydrate moiety of human platelet glycocalicin: the structures of the major Asn-linked sugar chains.
3571205	1	53	link	Asparagine-linked	385:401	arg1	oligosaccharides					414:429	wheat germ agglutinin-Sepharose and Mono Q. Asparagine-linked (N-linked) oligosaccharides	341:429	oligosaccharides	414:429	Glycocalicin, a predominant glycoprotein on the human platelet surface, has been purified from a platelet suspension by means of sonication, ammonium sulfate precipitation and acid treatment followed by chromatography on columns of wheat germ agglutinin-Sepharose and Mono Q. Asparagine-linked (N-linked) oligosaccharides were released by hydrazinolysis, and then N-acetylated and reduced with NaBH4 or NaB3H4.
3571205	3	54	theme	glycosidase	815:825	arg1	digestion					827:835	glycosidase digestion	815:835	glycosidase digestion	815:835	The structures of the two major oligosaccharide-alditols separated by ion-exchange chromatography on a Mono Q column were investigated by means of methylation analysis, glycosidase digestion, and Smith periodate degradation, and they were assigned as typical di- and trisialylated complex-type oligosaccharide-alditols with two and three peripheral chains consisting of Gal-GlcNAc sequences, respectively.
9425062	13	0	theme	heavy	1619:1623	arg1	chain					1625:1629	heavy chain 2	1619:1631	heavy chain 2	1619:1631	In heavy chain 1 the two disulfide bonds are formed between Cys210 and Cys213 and between Cys234 and Cys506, and in heavy chain 2, between Cys207 and Cys210 and between Cys596 and Cys597.
9425062	6	1	theme	heavy	709:713	arg1	chains					715:720	the heavy chains	705:720	the heavy chains	705:720	The aim of this study was to complete the primary structure by characterizing additional covalent posttranslational modifications of the heavy chains.
9425062	2	2	theme	unknown	339:345	arg1	function					347:354	unknown function	339:354	unknown function	339:354	The protein is composed of a light inhibitory chain called bikunin and two heavy chains of unknown function.
9425062	1	3	from	concentrations	216:229	arg1	plasma					240:245	human plasma	234:245	human plasma	234:245	Inter-alpha-inhibitor (IalphaI) is a serine proteinase inhibitor found in high concentrations in human plasma.
9425062	2	4	theme	light	277:281	arg1	chain					294:298	a light inhibitory chain	275:298	a light inhibitory chain called bikunin	275:313	The protein is composed of a light inhibitory chain called bikunin and two heavy chains of unknown function.
9425062	8	5	theme	oligosaccharides	1085:1100	arg1	cluster					1060:1066	a cluster	1058:1066	a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2	1058:1155	In addition, the IalphaI heavy chains carried several O-linked glycans located on Thr619 of heavy chain 1 and a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2.
9425062	8	5	theme	oligosaccharides	1085:1100	arg1	chain					1046:1050	heavy chain 1	1040:1052	heavy chain 1	1040:1052	In addition, the IalphaI heavy chains carried several O-linked glycans located on Thr619 of heavy chain 1 and a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2.
9425062	6	6	theme	posttranslational	670:686	arg1	modifications					688:700	additional covalent posttranslational modifications	650:700	additional covalent posttranslational modifications of the heavy chains	650:720	The aim of this study was to complete the primary structure by characterizing additional covalent posttranslational modifications of the heavy chains.
9425062	1	7	theme	serine	174:179	arg1	inhibitor					192:200	a serine proteinase inhibitor	172:200	a serine proteinase inhibitor found in high concentrations in human plasma	172:245	Inter-alpha-inhibitor (IalphaI) is a serine proteinase inhibitor found in high concentrations in human plasma.
9425062	1	7	theme	serine	174:179	arg1	Inter-alpha-inhibitor					137:157	Inter-alpha-inhibitor	137:157	Inter-alpha-inhibitor (IalphaI)	137:167	Inter-alpha-inhibitor (IalphaI) is a serine proteinase inhibitor found in high concentrations in human plasma.
9425062	8	8	theme	chain	1046:1050	arg1	Thr619					1030:1035	Thr619	1030:1035	Thr619 of heavy chain 1 and a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2	1030:1155	In addition, the IalphaI heavy chains carried several O-linked glycans located on Thr619 of heavy chain 1 and a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2.
9425062	6	9	theme	additional	650:659	arg1	modifications					688:700	additional covalent posttranslational modifications	650:700	additional covalent posttranslational modifications of the heavy chains	650:720	The aim of this study was to complete the primary structure by characterizing additional covalent posttranslational modifications of the heavy chains.
9425062	11	10	theme	heavy	1369:1373	arg1	chain					1375:1379	heavy chain 1	1369:1381	heavy chain 1	1369:1381	The unpaired Cys residue residing on heavy chain 1, Cys26, appears to be modified by dihexosylation.
9425062	11	10	theme	heavy	1369:1373	arg1	Cys26					1384:1388	Cys26	1384:1388	Cys26	1384:1388	The unpaired Cys residue residing on heavy chain 1, Cys26, appears to be modified by dihexosylation.
9425062	8	11	from	oligosaccharides	1085:1100	arg1	Thr637					1133:1138	Thr637	1133:1138	Thr637	1133:1138	In addition, the IalphaI heavy chains carried several O-linked glycans located on Thr619 of heavy chain 1 and a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2.
9425062	8	11	from	oligosaccharides	1085:1100	arg1	Ser619					1113:1118	Ser619	1113:1118	Ser619	1113:1118	In addition, the IalphaI heavy chains carried several O-linked glycans located on Thr619 of heavy chain 1 and a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2.
9425062	8	11	from	oligosaccharides	1085:1100	arg1	Thr612					1105:1110	Thr612	1105:1110	Thr612	1105:1110	In addition, the IalphaI heavy chains carried several O-linked glycans located on Thr619 of heavy chain 1 and a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2.
9425062	8	11	from	oligosaccharides	1085:1100	arg1	Thr621					1121:1126	Thr621	1121:1126	Thr621	1121:1126	In addition, the IalphaI heavy chains carried several O-linked glycans located on Thr619 of heavy chain 1 and a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2.
9425062	8	12	theme	cluster	1060:1066	arg1	Thr619					1030:1035	Thr619	1030:1035	Thr619 of heavy chain 1 and a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2	1030:1155	In addition, the IalphaI heavy chains carried several O-linked glycans located on Thr619 of heavy chain 1 and a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2.
9425062	8	13	from	Thr612	1105:1110	arg1	cluster					1060:1066	a cluster	1058:1066	a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2	1058:1155	In addition, the IalphaI heavy chains carried several O-linked glycans located on Thr619 of heavy chain 1 and a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2.
9425062	8	13	from	Thr612	1105:1110	arg1	chain					1046:1050	heavy chain 1	1040:1052	heavy chain 1	1040:1052	In addition, the IalphaI heavy chains carried several O-linked glycans located on Thr619 of heavy chain 1 and a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2.
9425062	7	14	theme	-GlcNAc2-Man-	913:925	arg1	Man-GlcNAc-Gal-SA					927:943	(Asn)-GlcNAc2-Man-(Man-GlcNAc-Gal-SA)2	908:945	(Asn)-GlcNAc2-Man-(Man-GlcNAc-Gal-SA)2	908:945	Analysis revealed three N-linked oligosaccharides located on Asn251 and Asn554 of heavy chain 1 and on Asn64 of heavy chain 2: all these were complex biantennary structures composed of (Asn)-GlcNAc2-Man-(Man-GlcNAc-Gal-SA)2.
9425062	7	15	theme	biantennary	873:883	arg1	structures					885:894	complex biantennary structures	865:894	complex biantennary structures composed of (Asn)-GlcNAc2-Man-(Man-GlcNAc-Gal-SA)2	865:945	Analysis revealed three N-linked oligosaccharides located on Asn251 and Asn554 of heavy chain 1 and on Asn64 of heavy chain 2: all these were complex biantennary structures composed of (Asn)-GlcNAc2-Man-(Man-GlcNAc-Gal-SA)2.
9425062	7	16	theme	Asn	909:911	arg1	Man-GlcNAc-Gal-SA					927:943	(Asn)-GlcNAc2-Man-(Man-GlcNAc-Gal-SA)2	908:945	(Asn)-GlcNAc2-Man-(Man-GlcNAc-Gal-SA)2	908:945	Analysis revealed three N-linked oligosaccharides located on Asn251 and Asn554 of heavy chain 1 and on Asn64 of heavy chain 2: all these were complex biantennary structures composed of (Asn)-GlcNAc2-Man-(Man-GlcNAc-Gal-SA)2.
9425062	8	17	from	Thr621	1121:1126	arg1	cluster					1060:1066	a cluster	1058:1066	a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2	1058:1155	In addition, the IalphaI heavy chains carried several O-linked glycans located on Thr619 of heavy chain 1 and a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2.
9425062	8	17	from	Thr621	1121:1126	arg1	chain					1046:1050	heavy chain 1	1040:1052	heavy chain 1	1040:1052	In addition, the IalphaI heavy chains carried several O-linked glycans located on Thr619 of heavy chain 1 and a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2.
9425062	8	18	theme	chain	1149:1153	arg1	Thr637					1133:1138	Thr637	1133:1138	Thr637	1133:1138	In addition, the IalphaI heavy chains carried several O-linked glycans located on Thr619 of heavy chain 1 and a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2.
9425062	8	18	theme	chain	1149:1153	arg1	Ser619					1113:1118	Ser619	1113:1118	Ser619	1113:1118	In addition, the IalphaI heavy chains carried several O-linked glycans located on Thr619 of heavy chain 1 and a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2.
9425062	8	18	theme	chain	1149:1153	arg1	Thr612					1105:1110	Thr612	1105:1110	Thr612	1105:1110	In addition, the IalphaI heavy chains carried several O-linked glycans located on Thr619 of heavy chain 1 and a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2.
9425062	8	18	theme	chain	1149:1153	arg1	Thr621					1121:1126	Thr621	1121:1126	Thr621	1121:1126	In addition, the IalphaI heavy chains carried several O-linked glycans located on Thr619 of heavy chain 1 and a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2.
9425062	0	19	theme	glycans	82:88	arg1	bridges					104:110	disulfide bridges	94:110	disulfide bridges in heavy chains 1 and 2	94:134	Posttranslational modifications of human inter-alpha-inhibitor: identification of glycans and disulfide bridges in heavy chains 1 and 2.
9425062	0	19	theme	glycans	82:88	arg1	identification					64:77	identification	64:77	identification of glycans	64:88	Posttranslational modifications of human inter-alpha-inhibitor: identification of glycans and disulfide bridges in heavy chains 1 and 2.
9425062	8	20	from	Ser619	1113:1118	arg1	cluster					1060:1066	a cluster	1058:1066	a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2	1058:1155	In addition, the IalphaI heavy chains carried several O-linked glycans located on Thr619 of heavy chain 1 and a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2.
9425062	8	20	from	Ser619	1113:1118	arg1	chain					1046:1050	heavy chain 1	1040:1052	heavy chain 1	1040:1052	In addition, the IalphaI heavy chains carried several O-linked glycans located on Thr619 of heavy chain 1 and a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2.
9425062	9	21	dep	short	1184:1188	arg1	Ser/Thr					1191:1197	Ser/Thr	1191:1197	Ser/Thr	1191:1197	The oligosaccharides were short (Ser/Thr)-GalNAc-Gal-SA trisaccharides.
9425062	0	22	theme	disulfide	94:102	arg1	bridges					104:110	disulfide bridges	94:110	disulfide bridges in heavy chains 1 and 2	94:134	Posttranslational modifications of human inter-alpha-inhibitor: identification of glycans and disulfide bridges in heavy chains 1 and 2.
9425062	11	23	theme	unpaired	1336:1343	arg1	residue					1349:1355	The unpaired Cys residue	1332:1355	The unpaired Cys residue residing on heavy chain 1, Cys26,	1332:1389	The unpaired Cys residue residing on heavy chain 1, Cys26, appears to be modified by dihexosylation.
9425062	7	24	theme	heavy	835:839	arg1	chain					841:845	heavy chain 2	835:847	heavy chain 2	835:847	Analysis revealed three N-linked oligosaccharides located on Asn251 and Asn554 of heavy chain 1 and on Asn64 of heavy chain 2: all these were complex biantennary structures composed of (Asn)-GlcNAc2-Man-(Man-GlcNAc-Gal-SA)2.
9425062	0	25	dep	chains	121:126	arg1	2					134:134	2	134:134	2	134:134	Posttranslational modifications of human inter-alpha-inhibitor: identification of glycans and disulfide bridges in heavy chains 1 and 2.
9425062	0	25	dep	chains	121:126	arg1	1					128:128	1	128:128	1	128:128	Posttranslational modifications of human inter-alpha-inhibitor: identification of glycans and disulfide bridges in heavy chains 1 and 2.
9425062	12	26	theme	intrachain	1473:1482	arg1	bridges					1494:1500	intrachain disulfide bridges	1473:1500	intrachain disulfide bridges	1473:1500	The other Cys residues exclusively form intrachain disulfide bridges.
9425062	0	27	from	identification	64:77	arg1	chains					121:126	heavy chains 1 and 2	115:134	heavy chains 1 and 2	115:134	Posttranslational modifications of human inter-alpha-inhibitor: identification of glycans and disulfide bridges in heavy chains 1 and 2.
9425062	13	28	theme	heavy	1506:1510	arg1	chain					1512:1516	heavy chain 1	1506:1518	heavy chain 1	1506:1518	In heavy chain 1 the two disulfide bonds are formed between Cys210 and Cys213 and between Cys234 and Cys506, and in heavy chain 2, between Cys207 and Cys210 and between Cys596 and Cys597.
9425062	3	29	theme	carbohydrate	417:428	arg1	[Enghild					441:448	a carbohydrate cross-link [Enghild	415:448	a carbohydrate cross-link [Enghild	415:448	The three polypeptide chains are covalently assembled via a carbohydrate cross-link [Enghild, J. J., Salvesen, G., Hefta, S. A., Thogersen, I. B., Rutherfurd, S., & Pizzo, S. V. (1991) J. Biol.
9425062	3	29	theme	carbohydrate	417:428	arg1	G.					468:469	G.	468:469	G.	468:469	The three polypeptide chains are covalently assembled via a carbohydrate cross-link [Enghild, J. J., Salvesen, G., Hefta, S. A., Thogersen, I. B., Rutherfurd, S., & Pizzo, S. V. (1991) J. Biol.
9425062	0	30	theme	Posttranslational	0:16	arg1	modifications					18:30	Posttranslational modifications	0:30	Posttranslational modifications of human inter-alpha-inhibitor: identification of glycans and disulfide bridges in heavy chains 1 and 2.	0:135	Posttranslational modifications of human inter-alpha-inhibitor: identification of glycans and disulfide bridges in heavy chains 1 and 2.
9425062	12	31	theme	Cys	1443:1445	arg1	residues					1447:1454	The other Cys residues	1433:1454	The other Cys residues	1433:1454	The other Cys residues exclusively form intrachain disulfide bridges.
9425062	10	32	theme	IalphaI	1234:1240	arg1	chains					1248:1253	The IalphaI heavy chains	1230:1253	The IalphaI heavy chains	1230:1253	The IalphaI heavy chains contain nine Cys residues, of which eight are involved in disulfide bridges.
9425062	10	33	theme	disulfide	1313:1321	arg1	bridges					1323:1329	disulfide bridges	1313:1329	disulfide bridges	1313:1329	The IalphaI heavy chains contain nine Cys residues, of which eight are involved in disulfide bridges.
9425062	0	34	theme	inter-alpha-inhibitor	41:61	arg1	modifications					18:30	Posttranslational modifications	0:30	Posttranslational modifications of human inter-alpha-inhibitor: identification of glycans and disulfide bridges in heavy chains 1 and 2.	0:135	Posttranslational modifications of human inter-alpha-inhibitor: identification of glycans and disulfide bridges in heavy chains 1 and 2.
9425062	14	35	theme	acid	1812:1815	arg1	residues					1817:1824	only two amino acid residues	1797:1824	only two amino acid residues apart	1797:1830	Interestingly, three of these four disulfides are formed between Cys residues that are either adjacent or only two amino acid residues apart.
9425062	2	36	theme	heavy	323:327	arg1	chains					329:334	two heavy chains	319:334	two heavy chains of unknown function	319:354	The protein is composed of a light inhibitory chain called bikunin and two heavy chains of unknown function.
9425062	8	37	theme	heavy	973:977	arg1	chains					979:984	the IalphaI heavy chains	961:984	the IalphaI heavy chains	961:984	In addition, the IalphaI heavy chains carried several O-linked glycans located on Thr619 of heavy chain 1 and a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2.
9425062	7	38	theme	heavy	805:809	arg1	chain					811:815	heavy chain 1	805:817	heavy chain 1	805:817	Analysis revealed three N-linked oligosaccharides located on Asn251 and Asn554 of heavy chain 1 and on Asn64 of heavy chain 2: all these were complex biantennary structures composed of (Asn)-GlcNAc2-Man-(Man-GlcNAc-Gal-SA)2.
9425062	6	39	theme	study	588:592	arg1	aim					576:578	The aim	572:578	The aim of this study	572:592	The aim of this study was to complete the primary structure by characterizing additional covalent posttranslational modifications of the heavy chains.
9425062	2	40	theme	function	347:354	arg1	chains					329:334	two heavy chains	319:334	two heavy chains of unknown function	319:354	The protein is composed of a light inhibitory chain called bikunin and two heavy chains of unknown function.
9425062	2	40	theme	function	347:354	arg1	chain					294:298	a light inhibitory chain	275:298	a light inhibitory chain called bikunin	275:313	The protein is composed of a light inhibitory chain called bikunin and two heavy chains of unknown function.
9425062	8	41	theme	O-linked	1002:1009	arg1	glycans					1011:1017	several O-linked glycans	994:1017	several O-linked glycans located on Thr619 of heavy chain 1 and a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2	994:1155	In addition, the IalphaI heavy chains carried several O-linked glycans located on Thr619 of heavy chain 1 and a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2.
9425062	8	42	from	chain	1046:1050	arg1	Thr637					1133:1138	Thr637	1133:1138	Thr637	1133:1138	In addition, the IalphaI heavy chains carried several O-linked glycans located on Thr619 of heavy chain 1 and a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2.
9425062	8	42	from	chain	1046:1050	arg1	Ser619					1113:1118	Ser619	1113:1118	Ser619	1113:1118	In addition, the IalphaI heavy chains carried several O-linked glycans located on Thr619 of heavy chain 1 and a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2.
9425062	8	42	from	chain	1046:1050	arg1	Thr612					1105:1110	Thr612	1105:1110	Thr612	1105:1110	In addition, the IalphaI heavy chains carried several O-linked glycans located on Thr619 of heavy chain 1 and a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2.
9425062	8	42	from	chain	1046:1050	arg1	Thr621					1121:1126	Thr621	1121:1126	Thr621	1121:1126	In addition, the IalphaI heavy chains carried several O-linked glycans located on Thr619 of heavy chain 1 and a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2.
9425062	2	43	theme	inhibitory	283:292	arg1	chain					294:298	a light inhibitory chain	275:298	a light inhibitory chain called bikunin	275:313	The protein is composed of a light inhibitory chain called bikunin and two heavy chains of unknown function.
9425062	10	44	contain	contain	1255:1261	arg1	chains					1248:1253	The IalphaI heavy chains	1230:1253	The IalphaI heavy chains	1230:1253	The IalphaI heavy chains contain nine Cys residues, of which eight are involved in disulfide bridges.
9425062	10	44	contain	contain	1255:1261	arg2	residues					1272:1279	nine Cys residues	1263:1279	nine Cys residues	1263:1279	The IalphaI heavy chains contain nine Cys residues, of which eight are involved in disulfide bridges.
9425062	8	45	theme	located	1019:1025	arg1	glycans					1011:1017	several O-linked glycans	994:1017	several O-linked glycans located on Thr619 of heavy chain 1 and a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2	994:1155	In addition, the IalphaI heavy chains carried several O-linked glycans located on Thr619 of heavy chain 1 and a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2.
9425062	7	46	link	N-linked	747:754	arg1	oligosaccharides					756:771	three N-linked oligosaccharides	741:771	three N-linked oligosaccharides located on Asn251 and Asn554 of heavy chain 1 and on Asn64 of heavy chain 2	741:847	Analysis revealed three N-linked oligosaccharides located on Asn251 and Asn554 of heavy chain 1 and on Asn64 of heavy chain 2: all these were complex biantennary structures composed of (Asn)-GlcNAc2-Man-(Man-GlcNAc-Gal-SA)2.
9425062	14	47	dep	either	1778:1783	arg1	adjacent					1785:1792	adjacent	1785:1792	adjacent	1785:1792	Interestingly, three of these four disulfides are formed between Cys residues that are either adjacent or only two amino acid residues apart.
9425062	7	48	theme	located	773:779	arg1	oligosaccharides					756:771	three N-linked oligosaccharides	741:771	three N-linked oligosaccharides located on Asn251 and Asn554 of heavy chain 1 and on Asn64 of heavy chain 2	741:847	Analysis revealed three N-linked oligosaccharides located on Asn251 and Asn554 of heavy chain 1 and on Asn64 of heavy chain 2: all these were complex biantennary structures composed of (Asn)-GlcNAc2-Man-(Man-GlcNAc-Gal-SA)2.
9425062	8	49	from	cluster	1060:1066	arg1	Thr637					1133:1138	Thr637	1133:1138	Thr637	1133:1138	In addition, the IalphaI heavy chains carried several O-linked glycans located on Thr619 of heavy chain 1 and a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2.
9425062	8	49	from	cluster	1060:1066	arg1	Ser619					1113:1118	Ser619	1113:1118	Ser619	1113:1118	In addition, the IalphaI heavy chains carried several O-linked glycans located on Thr619 of heavy chain 1 and a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2.
9425062	8	49	from	cluster	1060:1066	arg1	Thr612					1105:1110	Thr612	1105:1110	Thr612	1105:1110	In addition, the IalphaI heavy chains carried several O-linked glycans located on Thr619 of heavy chain 1 and a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2.
9425062	8	49	from	cluster	1060:1066	arg1	Thr621					1121:1126	Thr621	1121:1126	Thr621	1121:1126	In addition, the IalphaI heavy chains carried several O-linked glycans located on Thr619 of heavy chain 1 and a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2.
9425062	8	50	theme	O-linked	1076:1083	arg1	oligosaccharides					1085:1100	four O-linked oligosaccharides	1071:1100	four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2	1071:1155	In addition, the IalphaI heavy chains carried several O-linked glycans located on Thr619 of heavy chain 1 and a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2.
9425062	6	51	theme	covalent	661:668	arg1	modifications					688:700	additional covalent posttranslational modifications	650:700	additional covalent posttranslational modifications of the heavy chains	650:720	The aim of this study was to complete the primary structure by characterizing additional covalent posttranslational modifications of the heavy chains.
9425062	7	52	theme	N-linked	747:754	arg1	oligosaccharides					756:771	three N-linked oligosaccharides	741:771	three N-linked oligosaccharides located on Asn251 and Asn554 of heavy chain 1 and on Asn64 of heavy chain 2	741:847	Analysis revealed three N-linked oligosaccharides located on Asn251 and Asn554 of heavy chain 1 and on Asn64 of heavy chain 2: all these were complex biantennary structures composed of (Asn)-GlcNAc2-Man-(Man-GlcNAc-Gal-SA)2.
9425062	1	53	theme	proteinase	181:190	arg1	inhibitor					192:200	a serine proteinase inhibitor	172:200	a serine proteinase inhibitor found in high concentrations in human plasma	172:245	Inter-alpha-inhibitor (IalphaI) is a serine proteinase inhibitor found in high concentrations in human plasma.
9425062	1	53	theme	proteinase	181:190	arg1	Inter-alpha-inhibitor					137:157	Inter-alpha-inhibitor	137:157	Inter-alpha-inhibitor (IalphaI)	137:167	Inter-alpha-inhibitor (IalphaI) is a serine proteinase inhibitor found in high concentrations in human plasma.
9425062	8	54	theme	heavy	1040:1044	arg1	chain					1046:1050	heavy chain 1	1040:1052	heavy chain 1	1040:1052	In addition, the IalphaI heavy chains carried several O-linked glycans located on Thr619 of heavy chain 1 and a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2.
9425062	10	55	theme	heavy	1242:1246	arg1	chains					1248:1253	The IalphaI heavy chains	1230:1253	The IalphaI heavy chains	1230:1253	The IalphaI heavy chains contain nine Cys residues, of which eight are involved in disulfide bridges.
9425062	8	56	contain	carried	986:992	arg3	addition					951:958	addition	951:958	addition	951:958	In addition, the IalphaI heavy chains carried several O-linked glycans located on Thr619 of heavy chain 1 and a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2.
9425062	8	56	contain	carried	986:992	arg2	glycans					1011:1017	several O-linked glycans	994:1017	several O-linked glycans located on Thr619 of heavy chain 1 and a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2	994:1155	In addition, the IalphaI heavy chains carried several O-linked glycans located on Thr619 of heavy chain 1 and a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2.
9425062	8	56	contain	carried	986:992	arg1	chains					979:984	the IalphaI heavy chains	961:984	the IalphaI heavy chains	961:984	In addition, the IalphaI heavy chains carried several O-linked glycans located on Thr619 of heavy chain 1 and a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2.
9425062	0	57	from	bridges	104:110	arg1	chains					121:126	heavy chains 1 and 2	115:134	heavy chains 1 and 2	115:134	Posttranslational modifications of human inter-alpha-inhibitor: identification of glycans and disulfide bridges in heavy chains 1 and 2.
9425062	1	58	theme	high	211:214	arg1	concentrations					216:229	high concentrations	211:229	high concentrations in human plasma	211:245	Inter-alpha-inhibitor (IalphaI) is a serine proteinase inhibitor found in high concentrations in human plasma.
9425062	8	59	link	O-linked	1002:1009	arg1	glycans					1011:1017	several O-linked glycans	994:1017	several O-linked glycans located on Thr619 of heavy chain 1 and a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2	994:1155	In addition, the IalphaI heavy chains carried several O-linked glycans located on Thr619 of heavy chain 1 and a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2.
9425062	1	60	located	found	202:206	arg2	Inter-alpha-inhibitor					137:157	Inter-alpha-inhibitor	137:157	Inter-alpha-inhibitor (IalphaI)	137:167	Inter-alpha-inhibitor (IalphaI) is a serine proteinase inhibitor found in high concentrations in human plasma.
9425062	1	60	located	found	202:206	arg2	inhibitor					192:200	a serine proteinase inhibitor	172:200	a serine proteinase inhibitor found in high concentrations in human plasma	172:245	Inter-alpha-inhibitor (IalphaI) is a serine proteinase inhibitor found in high concentrations in human plasma.
9425062	1	60	located	found	202:206	arg1	concentrations					216:229	high concentrations	211:229	high concentrations in human plasma	211:245	Inter-alpha-inhibitor (IalphaI) is a serine proteinase inhibitor found in high concentrations in human plasma.
9425062	11	61	mod	modified	1405:1412	arg3	dihexosylation					1417:1430	dihexosylation	1417:1430	dihexosylation	1417:1430	The unpaired Cys residue residing on heavy chain 1, Cys26, appears to be modified by dihexosylation.
9425062	11	61	mod	modified	1405:1412	arg1	residue					1349:1355	The unpaired Cys residue	1332:1355	The unpaired Cys residue residing on heavy chain 1, Cys26,	1332:1389	The unpaired Cys residue residing on heavy chain 1, Cys26, appears to be modified by dihexosylation.
9425062	7	62	theme	complex	865:871	arg1	structures					885:894	complex biantennary structures	865:894	complex biantennary structures composed of (Asn)-GlcNAc2-Man-(Man-GlcNAc-Gal-SA)2	865:945	Analysis revealed three N-linked oligosaccharides located on Asn251 and Asn554 of heavy chain 1 and on Asn64 of heavy chain 2: all these were complex biantennary structures composed of (Asn)-GlcNAc2-Man-(Man-GlcNAc-Gal-SA)2.
9425062	8	63	theme	heavy	1143:1147	arg1	chain					1149:1153	heavy chain 2	1143:1155	heavy chain 2	1143:1155	In addition, the IalphaI heavy chains carried several O-linked glycans located on Thr619 of heavy chain 1 and a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2.
9425062	11	64	theme	Cys	1345:1347	arg1	residue					1349:1355	The unpaired Cys residue	1332:1355	The unpaired Cys residue residing on heavy chain 1, Cys26,	1332:1389	The unpaired Cys residue residing on heavy chain 1, Cys26, appears to be modified by dihexosylation.
9425062	10	65	theme	Cys	1268:1270	arg1	residues					1272:1279	nine Cys residues	1263:1279	nine Cys residues	1263:1279	The IalphaI heavy chains contain nine Cys residues, of which eight are involved in disulfide bridges.
9425062	0	66	theme	heavy	115:119	arg1	chains					121:126	heavy chains 1 and 2	115:134	heavy chains 1 and 2	115:134	Posttranslational modifications of human inter-alpha-inhibitor: identification of glycans and disulfide bridges in heavy chains 1 and 2.
9425062	8	67	from	Thr637	1133:1138	arg1	cluster					1060:1066	a cluster	1058:1066	a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2	1058:1155	In addition, the IalphaI heavy chains carried several O-linked glycans located on Thr619 of heavy chain 1 and a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2.
9425062	8	67	from	Thr637	1133:1138	arg1	chain					1046:1050	heavy chain 1	1040:1052	heavy chain 1	1040:1052	In addition, the IalphaI heavy chains carried several O-linked glycans located on Thr619 of heavy chain 1 and a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2.
9425062	13	68	theme	disulfide	1528:1536	arg1	bonds					1538:1542	the two disulfide bonds	1520:1542	the two disulfide bonds	1520:1542	In heavy chain 1 the two disulfide bonds are formed between Cys210 and Cys213 and between Cys234 and Cys506, and in heavy chain 2, between Cys207 and Cys210 and between Cys596 and Cys597.
9425062	7	69	theme	chain	841:845	arg1	Asn64					826:830	Asn64	826:830	Asn64 of heavy chain 2	826:847	Analysis revealed three N-linked oligosaccharides located on Asn251 and Asn554 of heavy chain 1 and on Asn64 of heavy chain 2: all these were complex biantennary structures composed of (Asn)-GlcNAc2-Man-(Man-GlcNAc-Gal-SA)2.
9425062	12	70	theme	disulfide	1484:1492	arg1	bridges					1494:1500	intrachain disulfide bridges	1473:1500	intrachain disulfide bridges	1473:1500	The other Cys residues exclusively form intrachain disulfide bridges.
9425062	3	71	theme	cross-link	430:439	arg1	[Enghild					441:448	a carbohydrate cross-link [Enghild	415:448	a carbohydrate cross-link [Enghild	415:448	The three polypeptide chains are covalently assembled via a carbohydrate cross-link [Enghild, J. J., Salvesen, G., Hefta, S. A., Thogersen, I. B., Rutherfurd, S., & Pizzo, S. V. (1991) J. Biol.
9425062	3	71	theme	cross-link	430:439	arg1	G.					468:469	G.	468:469	G.	468:469	The three polypeptide chains are covalently assembled via a carbohydrate cross-link [Enghild, J. J., Salvesen, G., Hefta, S. A., Thogersen, I. B., Rutherfurd, S., & Pizzo, S. V. (1991) J. Biol.
9425062	0	72	theme	human	35:39	arg1	inter-alpha-inhibitor					41:61	human inter-alpha-inhibitor	35:61	human inter-alpha-inhibitor	35:61	Posttranslational modifications of human inter-alpha-inhibitor: identification of glycans and disulfide bridges in heavy chains 1 and 2.
9425062	12	73	theme	other	1437:1441	arg1	residues					1447:1454	The other Cys residues	1433:1454	The other Cys residues	1433:1454	The other Cys residues exclusively form intrachain disulfide bridges.
9425062	3	74	theme	polypeptide	367:377	arg1	chains					379:384	The three polypeptide chains	357:384	The three polypeptide chains	357:384	The three polypeptide chains are covalently assembled via a carbohydrate cross-link [Enghild, J. J., Salvesen, G., Hefta, S. A., Thogersen, I. B., Rutherfurd, S., & Pizzo, S. V. (1991) J. Biol.
9425062	9	75	theme	short	1184:1188	arg1	trisaccharides					1214:1227	short (Ser/Thr)-GalNAc-Gal-SA trisaccharides	1184:1227	short (Ser/Thr)-GalNAc-Gal-SA trisaccharides	1184:1227	The oligosaccharides were short (Ser/Thr)-GalNAc-Gal-SA trisaccharides.
9425062	9	75	theme	short	1184:1188	arg1	oligosaccharides					1162:1177	The oligosaccharides	1158:1177	The oligosaccharides	1158:1177	The oligosaccharides were short (Ser/Thr)-GalNAc-Gal-SA trisaccharides.
9425062	14	76	theme	Cys	1756:1758	arg1	residues					1760:1767	Cys residues	1756:1767	Cys residues that are either adjacent or only two amino acid residues apart	1756:1830	Interestingly, three of these four disulfides are formed between Cys residues that are either adjacent or only two amino acid residues apart.
9425062	8	77	theme	IalphaI	965:971	arg1	chains					979:984	the IalphaI heavy chains	961:984	the IalphaI heavy chains	961:984	In addition, the IalphaI heavy chains carried several O-linked glycans located on Thr619 of heavy chain 1 and a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2.
9425062	8	78	link	O-linked	1076:1083	arg1	oligosaccharides					1085:1100	four O-linked oligosaccharides	1071:1100	four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2	1071:1155	In addition, the IalphaI heavy chains carried several O-linked glycans located on Thr619 of heavy chain 1 and a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2.
9425062	6	79	theme	primary	614:620	arg1	structure					622:630	the primary structure	610:630	the primary structure	610:630	The aim of this study was to complete the primary structure by characterizing additional covalent posttranslational modifications of the heavy chains.
9425062	7	80	theme	chain	811:815	arg1	Asn251					784:789	Asn251	784:789	Asn251	784:789	Analysis revealed three N-linked oligosaccharides located on Asn251 and Asn554 of heavy chain 1 and on Asn64 of heavy chain 2: all these were complex biantennary structures composed of (Asn)-GlcNAc2-Man-(Man-GlcNAc-Gal-SA)2.
9425062	9	81	theme	-GalNAc-Gal-SA	1199:1212	arg1	trisaccharides					1214:1227	short (Ser/Thr)-GalNAc-Gal-SA trisaccharides	1184:1227	short (Ser/Thr)-GalNAc-Gal-SA trisaccharides	1184:1227	The oligosaccharides were short (Ser/Thr)-GalNAc-Gal-SA trisaccharides.
9425062	9	81	theme	-GalNAc-Gal-SA	1199:1212	arg1	oligosaccharides					1162:1177	The oligosaccharides	1158:1177	The oligosaccharides	1158:1177	The oligosaccharides were short (Ser/Thr)-GalNAc-Gal-SA trisaccharides.
9425062	14	82	theme	disulfides	1726:1735	arg1	disulfides					1726:1735	these four disulfides	1715:1735	these four disulfides	1715:1735	Interestingly, three of these four disulfides are formed between Cys residues that are either adjacent or only two amino acid residues apart.
9425062	14	82	theme	disulfides	1726:1735	arg1	three					1706:1710	three	1706:1710	three	1706:1710	Interestingly, three of these four disulfides are formed between Cys residues that are either adjacent or only two amino acid residues apart.
9425062	14	83	theme	amino	1806:1810	arg1	residues					1817:1824	only two amino acid residues	1797:1824	only two amino acid residues apart	1797:1830	Interestingly, three of these four disulfides are formed between Cys residues that are either adjacent or only two amino acid residues apart.
9425062	1	84	theme	human	234:238	arg1	plasma					240:245	human plasma	234:245	human plasma	234:245	Inter-alpha-inhibitor (IalphaI) is a serine proteinase inhibitor found in high concentrations in human plasma.
9425062	8	85	theme	several	994:1000	arg1	glycans					1011:1017	several O-linked glycans	994:1017	several O-linked glycans located on Thr619 of heavy chain 1 and a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2	994:1155	In addition, the IalphaI heavy chains carried several O-linked glycans located on Thr619 of heavy chain 1 and a cluster of four O-linked oligosaccharides on Thr612, Ser619, Thr621, and Thr637 of heavy chain 2.
9425062	6	86	theme	chains	715:720	arg1	modifications					688:700	additional covalent posttranslational modifications	650:700	additional covalent posttranslational modifications of the heavy chains	650:720	The aim of this study was to complete the primary structure by characterizing additional covalent posttranslational modifications of the heavy chains.
9425062	0	87	dep	modifications	18:30	arg1	bridges					104:110	disulfide bridges	94:110	disulfide bridges in heavy chains 1 and 2	94:134	Posttranslational modifications of human inter-alpha-inhibitor: identification of glycans and disulfide bridges in heavy chains 1 and 2.
9425062	0	87	dep	modifications	18:30	arg1	identification					64:77	identification	64:77	identification of glycans	64:88	Posttranslational modifications of human inter-alpha-inhibitor: identification of glycans and disulfide bridges in heavy chains 1 and 2.
9425062	3	88	dep	G.	468:469	arg1	Biol					545:548	Biol	545:548	Biol	545:548	The three polypeptide chains are covalently assembled via a carbohydrate cross-link [Enghild, J. J., Salvesen, G., Hefta, S. A., Thogersen, I. B., Rutherfurd, S., & Pizzo, S. V. (1991) J. Biol.
10211705	1	0	theme	human	175:179	arg1	IgA1					187:190	human serum IgA1	175:190	human serum IgA1	175:190	Glycopeptides containing the N-linked oligosaccharide from human serum IgA1 were analyzed by matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOFMS).
10211705	4	1	theme	galactosylated	773:786	arg1	chain					804:808	a fully galactosylated bianntena sugar chain	765:808	a fully galactosylated bianntena sugar chain with or without a bisecting N-acetylglucosamine (GlcNAc) residue	765:873	GP1 was composed of two major components having a fully galactosylated bianntena sugar chain with or without a bisecting N-acetylglucosamine (GlcNAc) residue.
10211705	0	2	theme	A1	88:89	arg1	oligosaccharide					54:68	N-linked oligosaccharide	45:68	N-linked oligosaccharide of immunoglobulin A1 from normal human serum	45:113	Evidence for a site-specific fucosylation of N-linked oligosaccharide of immunoglobulin A1 from normal human serum.
10211705	1	3	contain	containing	130:139	arg1	Glycopeptides					116:128	Glycopeptides	116:128	Glycopeptides containing the N-linked oligosaccharide from human serum IgA1	116:190	Glycopeptides containing the N-linked oligosaccharide from human serum IgA1 were analyzed by matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOFMS).
10211705	1	3	contain	containing	130:139	arg2	oligosaccharide					154:168	the N-linked oligosaccharide	141:168	the N-linked oligosaccharide from human serum IgA1	141:190	Glycopeptides containing the N-linked oligosaccharide from human serum IgA1 were analyzed by matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOFMS).
10211705	4	4	theme	GlcNAc	859:864	arg1	residue					867:873	a bisecting N-acetylglucosamine (GlcNAc) residue	826:873	a bisecting N-acetylglucosamine (GlcNAc) residue	826:873	GP1 was composed of two major components having a fully galactosylated bianntena sugar chain with or without a bisecting N-acetylglucosamine (GlcNAc) residue.
10211705	5	5	theme	other	883:887	arg1	hand					889:892	the other hand	879:892	the other hand	879:892	On the other hand, the GP2 fraction corresponded to the glycopeptides having a fully galactosylated and fucosylated bianntena sugar chain partly bearing a bisecting GlcNAc residue.
10211705	1	6	theme	serum	181:185	arg1	IgA1					187:190	human serum IgA1	175:190	human serum IgA1	175:190	Glycopeptides containing the N-linked oligosaccharide from human serum IgA1 were analyzed by matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOFMS).
10211705	3	7	gly	glycopeptide	612:623	arg2	glycopeptide					612:623	the glycopeptide	608:623	the glycopeptide	608:623	The structure of the attached sugar chain was deduced from the mass number of the glycopeptide and confirmed by a two-dimensional mapping technique for a pyridylaminated oligosaccharide.
10211705	0	8	theme	human	103:107	arg1	serum					109:113	normal human serum	96:113	normal human serum	96:113	Evidence for a site-specific fucosylation of N-linked oligosaccharide of immunoglobulin A1 from normal human serum.
10211705	6	9	gly	fucosylation	1081:1092	arg1	oligosaccharide					1110:1124	the N-linked oligosaccharide	1097:1124	the N-linked oligosaccharide	1097:1124	Thus, the site-specific fucosylation of the N-linked oligosaccharide on the tailpiece of the alpha1 chain became evident for normal human serum IgA1.
10211705	6	9	gly	fucosylation	1081:1092	arg1	tailpiece					1133:1141	the tailpiece	1129:1141	the tailpiece of the alpha1 chain	1129:1161	Thus, the site-specific fucosylation of the N-linked oligosaccharide on the tailpiece of the alpha1 chain became evident for normal human serum IgA1.
10211705	3	10	theme	sugar	560:564	arg1	chain					566:570	the attached sugar chain	547:570	the attached sugar chain	547:570	The structure of the attached sugar chain was deduced from the mass number of the glycopeptide and confirmed by a two-dimensional mapping technique for a pyridylaminated oligosaccharide.
10211705	6	11	theme	normal	1182:1187	arg1	IgA1					1201:1204	normal human serum IgA1	1182:1204	normal human serum IgA1	1182:1204	Thus, the site-specific fucosylation of the N-linked oligosaccharide on the tailpiece of the alpha1 chain became evident for normal human serum IgA1.
10211705	3	12	theme	two-dimensional	644:658	arg1	technique					668:676	a two-dimensional mapping technique	642:676	a two-dimensional mapping technique for a pyridylaminated oligosaccharide	642:714	The structure of the attached sugar chain was deduced from the mass number of the glycopeptide and confirmed by a two-dimensional mapping technique for a pyridylaminated oligosaccharide.
10211705	0	13	theme	normal	96:101	arg1	serum					109:113	normal human serum	96:113	normal human serum	96:113	Evidence for a site-specific fucosylation of N-linked oligosaccharide of immunoglobulin A1 from normal human serum.
10211705	6	14	theme	alpha1	1150:1155	arg1	chain					1157:1161	the alpha1 chain	1146:1161	the alpha1 chain	1146:1161	Thus, the site-specific fucosylation of the N-linked oligosaccharide on the tailpiece of the alpha1 chain became evident for normal human serum IgA1.
10211705	4	15	theme	major	741:745	arg1	components					747:756	two major components	737:756	two major components having a fully galactosylated bianntena sugar chain with or without a bisecting N-acetylglucosamine (GlcNAc) residue	737:873	GP1 was composed of two major components having a fully galactosylated bianntena sugar chain with or without a bisecting N-acetylglucosamine (GlcNAc) residue.
10211705	6	16	theme	oligosaccharide	1110:1124	arg1	fucosylation					1081:1092	the site-specific fucosylation	1063:1092	the site-specific fucosylation of the N-linked oligosaccharide on the tailpiece of the alpha1 chain	1063:1161	Thus, the site-specific fucosylation of the N-linked oligosaccharide on the tailpiece of the alpha1 chain became evident for normal human serum IgA1.
10211705	2	17	gly	glycopeptides	305:317	arg2	glycopeptides					305:317	Two glycopeptides	301:317	Two glycopeptides	301:317	Two glycopeptides, GP1 and GP2, prepared from the endoproteinase Asp-N digest of the IgA1 heavy chain, were derived from the CH2 domain (N-glycan site at Asn263) and the tailpiece portion (N-glycan site at Asn459), respectively.
10211705	2	17	gly	glycopeptides	305:317	arg2	GP2					328:330	GP2	328:330	GP2	328:330	Two glycopeptides, GP1 and GP2, prepared from the endoproteinase Asp-N digest of the IgA1 heavy chain, were derived from the CH2 domain (N-glycan site at Asn263) and the tailpiece portion (N-glycan site at Asn459), respectively.
10211705	2	17	gly	glycopeptides	305:317	arg2	GP1					320:322	GP1	320:322	GP1	320:322	Two glycopeptides, GP1 and GP2, prepared from the endoproteinase Asp-N digest of the IgA1 heavy chain, were derived from the CH2 domain (N-glycan site at Asn263) and the tailpiece portion (N-glycan site at Asn459), respectively.
10211705	2	18	from	Asn263	455:460	arg1	site					447:450	N-glycan site	438:450	N-glycan site	438:450	Two glycopeptides, GP1 and GP2, prepared from the endoproteinase Asp-N digest of the IgA1 heavy chain, were derived from the CH2 domain (N-glycan site at Asn263) and the tailpiece portion (N-glycan site at Asn459), respectively.
10211705	4	19	theme	bisecting	828:836	arg1	residue					867:873	a bisecting N-acetylglucosamine (GlcNAc) residue	826:873	a bisecting N-acetylglucosamine (GlcNAc) residue	826:873	GP1 was composed of two major components having a fully galactosylated bianntena sugar chain with or without a bisecting N-acetylglucosamine (GlcNAc) residue.
10211705	2	20	theme	CH2	426:428	arg1	domain					430:435	the CH2 domain	422:435	the CH2 domain (N-glycan site at Asn263)	422:461	Two glycopeptides, GP1 and GP2, prepared from the endoproteinase Asp-N digest of the IgA1 heavy chain, were derived from the CH2 domain (N-glycan site at Asn263) and the tailpiece portion (N-glycan site at Asn459), respectively.
10211705	5	21	theme	GP2	899:901	arg1	fraction					903:910	the GP2 fraction	895:910	the GP2 fraction	895:910	On the other hand, the GP2 fraction corresponded to the glycopeptides having a fully galactosylated and fucosylated bianntena sugar chain partly bearing a bisecting GlcNAc residue.
10211705	6	22	theme	site-specific	1067:1079	arg1	fucosylation					1081:1092	the site-specific fucosylation	1063:1092	the site-specific fucosylation of the N-linked oligosaccharide on the tailpiece of the alpha1 chain	1063:1161	Thus, the site-specific fucosylation of the N-linked oligosaccharide on the tailpiece of the alpha1 chain became evident for normal human serum IgA1.
10211705	2	23	theme	tailpiece	471:479	arg1	portion					481:487	the tailpiece portion	467:487	the tailpiece portion (N-glycan site at Asn459)	467:513	Two glycopeptides, GP1 and GP2, prepared from the endoproteinase Asp-N digest of the IgA1 heavy chain, were derived from the CH2 domain (N-glycan site at Asn263) and the tailpiece portion (N-glycan site at Asn459), respectively.
10211705	5	24	theme	galactosylated	961:974	arg1	chain					1008:1012	a fully galactosylated and fucosylated bianntena sugar chain	953:1012	a fully galactosylated and fucosylated bianntena sugar chain partly bearing a bisecting GlcNAc residue	953:1054	On the other hand, the GP2 fraction corresponded to the glycopeptides having a fully galactosylated and fucosylated bianntena sugar chain partly bearing a bisecting GlcNAc residue.
10211705	5	25	gly	glycopeptides	932:944	arg2	glycopeptides					932:944	the glycopeptides	928:944	the glycopeptides having a fully galactosylated and fucosylated bianntena sugar chain partly bearing a bisecting GlcNAc residue	928:1054	On the other hand, the GP2 fraction corresponded to the glycopeptides having a fully galactosylated and fucosylated bianntena sugar chain partly bearing a bisecting GlcNAc residue.
10211705	0	26	from	fucosylation	29:40	arg1	serum					109:113	normal human serum	96:113	normal human serum	96:113	Evidence for a site-specific fucosylation of N-linked oligosaccharide of immunoglobulin A1 from normal human serum.
10211705	0	27	link	N-linked	45:52	arg1	oligosaccharide					54:68	N-linked oligosaccharide	45:68	N-linked oligosaccharide of immunoglobulin A1 from normal human serum	45:113	Evidence for a site-specific fucosylation of N-linked oligosaccharide of immunoglobulin A1 from normal human serum.
10211705	6	28	theme	chain	1157:1161	arg1	tailpiece					1133:1141	the tailpiece	1129:1141	the tailpiece of the alpha1 chain	1129:1161	Thus, the site-specific fucosylation of the N-linked oligosaccharide on the tailpiece of the alpha1 chain became evident for normal human serum IgA1.
10211705	5	29	contain	having	946:951	arg1	glycopeptides					932:944	the glycopeptides	928:944	the glycopeptides having a fully galactosylated and fucosylated bianntena sugar chain partly bearing a bisecting GlcNAc residue	928:1054	On the other hand, the GP2 fraction corresponded to the glycopeptides having a fully galactosylated and fucosylated bianntena sugar chain partly bearing a bisecting GlcNAc residue.
10211705	5	29	contain	having	946:951	arg2	chain					1008:1012	a fully galactosylated and fucosylated bianntena sugar chain	953:1012	a fully galactosylated and fucosylated bianntena sugar chain partly bearing a bisecting GlcNAc residue	953:1054	On the other hand, the GP2 fraction corresponded to the glycopeptides having a fully galactosylated and fucosylated bianntena sugar chain partly bearing a bisecting GlcNAc residue.
10211705	3	30	theme	mapping	660:666	arg1	technique					668:676	a two-dimensional mapping technique	642:676	a two-dimensional mapping technique for a pyridylaminated oligosaccharide	642:714	The structure of the attached sugar chain was deduced from the mass number of the glycopeptide and confirmed by a two-dimensional mapping technique for a pyridylaminated oligosaccharide.
10211705	6	31	theme	serum	1195:1199	arg1	IgA1					1201:1204	normal human serum IgA1	1182:1204	normal human serum IgA1	1182:1204	Thus, the site-specific fucosylation of the N-linked oligosaccharide on the tailpiece of the alpha1 chain became evident for normal human serum IgA1.
10211705	4	32	theme	N-acetylglucosamine	838:856	arg1	residue					867:873	a bisecting N-acetylglucosamine (GlcNAc) residue	826:873	a bisecting N-acetylglucosamine (GlcNAc) residue	826:873	GP1 was composed of two major components having a fully galactosylated bianntena sugar chain with or without a bisecting N-acetylglucosamine (GlcNAc) residue.
10211705	3	33	theme	mass	593:596	arg1	number					598:603	the mass number	589:603	the mass number of the glycopeptide	589:623	The structure of the attached sugar chain was deduced from the mass number of the glycopeptide and confirmed by a two-dimensional mapping technique for a pyridylaminated oligosaccharide.
10211705	2	34	theme	chain	397:401	arg1	digest					372:377	the endoproteinase Asp-N digest	347:377	the endoproteinase Asp-N digest of the IgA1 heavy chain	347:401	Two glycopeptides, GP1 and GP2, prepared from the endoproteinase Asp-N digest of the IgA1 heavy chain, were derived from the CH2 domain (N-glycan site at Asn263) and the tailpiece portion (N-glycan site at Asn459), respectively.
10211705	0	35	theme	site-specific	15:27	arg1	fucosylation					29:40	a site-specific fucosylation	13:40	a site-specific fucosylation of N-linked oligosaccharide of immunoglobulin A1 from normal human serum	13:113	Evidence for a site-specific fucosylation of N-linked oligosaccharide of immunoglobulin A1 from normal human serum.
10211705	5	36	theme	bianntena	992:1000	arg1	chain					1008:1012	a fully galactosylated and fucosylated bianntena sugar chain	953:1012	a fully galactosylated and fucosylated bianntena sugar chain partly bearing a bisecting GlcNAc residue	953:1054	On the other hand, the GP2 fraction corresponded to the glycopeptides having a fully galactosylated and fucosylated bianntena sugar chain partly bearing a bisecting GlcNAc residue.
10211705	3	37	theme	chain	566:570	arg1	structure					534:542	The structure	530:542	The structure of the attached sugar chain	530:570	The structure of the attached sugar chain was deduced from the mass number of the glycopeptide and confirmed by a two-dimensional mapping technique for a pyridylaminated oligosaccharide.
10211705	1	38	theme	matrix-assisted	209:223	arg1	spectrometry					273:284	matrix-assisted laser desorption ionization time-of-flight mass spectrometry	209:284	matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOFMS)	209:298	Glycopeptides containing the N-linked oligosaccharide from human serum IgA1 were analyzed by matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOFMS).
10211705	1	38	theme	matrix-assisted	209:223	arg1	MALDI-TOFMS					287:297	MALDI-TOFMS	287:297	MALDI-TOFMS	287:297	Glycopeptides containing the N-linked oligosaccharide from human serum IgA1 were analyzed by matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOFMS).
10211705	3	39	theme	attached	551:558	arg1	chain					566:570	the attached sugar chain	547:570	the attached sugar chain	547:570	The structure of the attached sugar chain was deduced from the mass number of the glycopeptide and confirmed by a two-dimensional mapping technique for a pyridylaminated oligosaccharide.
10211705	3	40	theme	glycopeptide	612:623	arg1	number					598:603	the mass number	589:603	the mass number of the glycopeptide	589:623	The structure of the attached sugar chain was deduced from the mass number of the glycopeptide and confirmed by a two-dimensional mapping technique for a pyridylaminated oligosaccharide.
10211705	1	41	theme	laser	225:229	arg1	spectrometry					273:284	matrix-assisted laser desorption ionization time-of-flight mass spectrometry	209:284	matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOFMS)	209:298	Glycopeptides containing the N-linked oligosaccharide from human serum IgA1 were analyzed by matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOFMS).
10211705	1	41	theme	laser	225:229	arg1	MALDI-TOFMS					287:297	MALDI-TOFMS	287:297	MALDI-TOFMS	287:297	Glycopeptides containing the N-linked oligosaccharide from human serum IgA1 were analyzed by matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOFMS).
10211705	5	42	gly	fucosylated	980:990	arg1	chain					1008:1012	a fully galactosylated and fucosylated bianntena sugar chain	953:1012	a fully galactosylated and fucosylated bianntena sugar chain partly bearing a bisecting GlcNAc residue	953:1054	On the other hand, the GP2 fraction corresponded to the glycopeptides having a fully galactosylated and fucosylated bianntena sugar chain partly bearing a bisecting GlcNAc residue.
10211705	6	43	theme	human	1189:1193	arg1	IgA1					1201:1204	normal human serum IgA1	1182:1204	normal human serum IgA1	1182:1204	Thus, the site-specific fucosylation of the N-linked oligosaccharide on the tailpiece of the alpha1 chain became evident for normal human serum IgA1.
10211705	1	44	theme	desorption	231:240	arg1	spectrometry					273:284	matrix-assisted laser desorption ionization time-of-flight mass spectrometry	209:284	matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOFMS)	209:298	Glycopeptides containing the N-linked oligosaccharide from human serum IgA1 were analyzed by matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOFMS).
10211705	1	44	theme	desorption	231:240	arg1	MALDI-TOFMS					287:297	MALDI-TOFMS	287:297	MALDI-TOFMS	287:297	Glycopeptides containing the N-linked oligosaccharide from human serum IgA1 were analyzed by matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOFMS).
10211705	4	45	contain	having	758:763	arg1	components					747:756	two major components	737:756	two major components having a fully galactosylated bianntena sugar chain with or without a bisecting N-acetylglucosamine (GlcNAc) residue	737:873	GP1 was composed of two major components having a fully galactosylated bianntena sugar chain with or without a bisecting N-acetylglucosamine (GlcNAc) residue.
10211705	4	45	contain	having	758:763	arg2	chain					804:808	a fully galactosylated bianntena sugar chain	765:808	a fully galactosylated bianntena sugar chain with or without a bisecting N-acetylglucosamine (GlcNAc) residue	765:873	GP1 was composed of two major components having a fully galactosylated bianntena sugar chain with or without a bisecting N-acetylglucosamine (GlcNAc) residue.
10211705	2	46	theme	N-glycan	438:445	arg1	site					447:450	N-glycan site	438:450	N-glycan site	438:450	Two glycopeptides, GP1 and GP2, prepared from the endoproteinase Asp-N digest of the IgA1 heavy chain, were derived from the CH2 domain (N-glycan site at Asn263) and the tailpiece portion (N-glycan site at Asn459), respectively.
10211705	1	47	theme	ionization	242:251	arg1	spectrometry					273:284	matrix-assisted laser desorption ionization time-of-flight mass spectrometry	209:284	matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOFMS)	209:298	Glycopeptides containing the N-linked oligosaccharide from human serum IgA1 were analyzed by matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOFMS).
10211705	1	47	theme	ionization	242:251	arg1	MALDI-TOFMS					287:297	MALDI-TOFMS	287:297	MALDI-TOFMS	287:297	Glycopeptides containing the N-linked oligosaccharide from human serum IgA1 were analyzed by matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOFMS).
10211705	0	48	theme	oligosaccharide	54:68	arg1	fucosylation					29:40	a site-specific fucosylation	13:40	a site-specific fucosylation of N-linked oligosaccharide of immunoglobulin A1 from normal human serum	13:113	Evidence for a site-specific fucosylation of N-linked oligosaccharide of immunoglobulin A1 from normal human serum.
10211705	2	49	theme	N-glycan	490:497	arg1	site					499:502	N-glycan site	490:502	N-glycan site	490:502	Two glycopeptides, GP1 and GP2, prepared from the endoproteinase Asp-N digest of the IgA1 heavy chain, were derived from the CH2 domain (N-glycan site at Asn263) and the tailpiece portion (N-glycan site at Asn459), respectively.
10211705	2	50	dep	portion	481:487	arg1	site					499:502	N-glycan site	490:502	N-glycan site	490:502	Two glycopeptides, GP1 and GP2, prepared from the endoproteinase Asp-N digest of the IgA1 heavy chain, were derived from the CH2 domain (N-glycan site at Asn263) and the tailpiece portion (N-glycan site at Asn459), respectively.
10211705	5	51	theme	GlcNAc	1041:1046	arg1	residue					1048:1054	a bisecting GlcNAc residue	1029:1054	a bisecting GlcNAc residue	1029:1054	On the other hand, the GP2 fraction corresponded to the glycopeptides having a fully galactosylated and fucosylated bianntena sugar chain partly bearing a bisecting GlcNAc residue.
10211705	2	52	dep	domain	430:435	arg1	site					447:450	N-glycan site	438:450	N-glycan site	438:450	Two glycopeptides, GP1 and GP2, prepared from the endoproteinase Asp-N digest of the IgA1 heavy chain, were derived from the CH2 domain (N-glycan site at Asn263) and the tailpiece portion (N-glycan site at Asn459), respectively.
10211705	3	53	theme	pyridylaminated	684:698	arg1	oligosaccharide					700:714	a pyridylaminated oligosaccharide	682:714	a pyridylaminated oligosaccharide	682:714	The structure of the attached sugar chain was deduced from the mass number of the glycopeptide and confirmed by a two-dimensional mapping technique for a pyridylaminated oligosaccharide.
10211705	0	54	theme	N-linked	45:52	arg1	oligosaccharide					54:68	N-linked oligosaccharide	45:68	N-linked oligosaccharide of immunoglobulin A1 from normal human serum	45:113	Evidence for a site-specific fucosylation of N-linked oligosaccharide of immunoglobulin A1 from normal human serum.
10211705	1	55	link	N-linked	145:152	arg1	oligosaccharide					154:168	the N-linked oligosaccharide	141:168	the N-linked oligosaccharide from human serum IgA1	141:190	Glycopeptides containing the N-linked oligosaccharide from human serum IgA1 were analyzed by matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOFMS).
10211705	5	56	theme	bisecting	1031:1039	arg1	residue					1048:1054	a bisecting GlcNAc residue	1029:1054	a bisecting GlcNAc residue	1029:1054	On the other hand, the GP2 fraction corresponded to the glycopeptides having a fully galactosylated and fucosylated bianntena sugar chain partly bearing a bisecting GlcNAc residue.
10211705	2	57	attach	derived	409:415	arg2	glycopeptides					305:317	Two glycopeptides	301:317	Two glycopeptides	301:317	Two glycopeptides, GP1 and GP2, prepared from the endoproteinase Asp-N digest of the IgA1 heavy chain, were derived from the CH2 domain (N-glycan site at Asn263) and the tailpiece portion (N-glycan site at Asn459), respectively.
10211705	2	57	attach	derived	409:415	arg2	GP2					328:330	GP2	328:330	GP2	328:330	Two glycopeptides, GP1 and GP2, prepared from the endoproteinase Asp-N digest of the IgA1 heavy chain, were derived from the CH2 domain (N-glycan site at Asn263) and the tailpiece portion (N-glycan site at Asn459), respectively.
10211705	2	57	attach	derived	409:415	arg2	GP1					320:322	GP1	320:322	GP1	320:322	Two glycopeptides, GP1 and GP2, prepared from the endoproteinase Asp-N digest of the IgA1 heavy chain, were derived from the CH2 domain (N-glycan site at Asn263) and the tailpiece portion (N-glycan site at Asn459), respectively.
10211705	2	57	attach	derived	409:415	arg1	portion					481:487	the tailpiece portion	467:487	the tailpiece portion (N-glycan site at Asn459)	467:513	Two glycopeptides, GP1 and GP2, prepared from the endoproteinase Asp-N digest of the IgA1 heavy chain, were derived from the CH2 domain (N-glycan site at Asn263) and the tailpiece portion (N-glycan site at Asn459), respectively.
10211705	2	57	attach	derived	409:415	arg1	domain					430:435	the CH2 domain	422:435	the CH2 domain (N-glycan site at Asn263)	422:461	Two glycopeptides, GP1 and GP2, prepared from the endoproteinase Asp-N digest of the IgA1 heavy chain, were derived from the CH2 domain (N-glycan site at Asn263) and the tailpiece portion (N-glycan site at Asn459), respectively.
10211705	2	58	theme	Asp-N	366:370	arg1	digest					372:377	the endoproteinase Asp-N digest	347:377	the endoproteinase Asp-N digest of the IgA1 heavy chain	347:401	Two glycopeptides, GP1 and GP2, prepared from the endoproteinase Asp-N digest of the IgA1 heavy chain, were derived from the CH2 domain (N-glycan site at Asn263) and the tailpiece portion (N-glycan site at Asn459), respectively.
10211705	5	59	theme	sugar	1002:1006	arg1	chain					1008:1012	a fully galactosylated and fucosylated bianntena sugar chain	953:1012	a fully galactosylated and fucosylated bianntena sugar chain partly bearing a bisecting GlcNAc residue	953:1054	On the other hand, the GP2 fraction corresponded to the glycopeptides having a fully galactosylated and fucosylated bianntena sugar chain partly bearing a bisecting GlcNAc residue.
10211705	0	60	from	serum	109:113	arg1	fucosylation					29:40	a site-specific fucosylation	13:40	a site-specific fucosylation of N-linked oligosaccharide of immunoglobulin A1 from normal human serum	13:113	Evidence for a site-specific fucosylation of N-linked oligosaccharide of immunoglobulin A1 from normal human serum.
10211705	0	60	from	serum	109:113	arg1	oligosaccharide					54:68	N-linked oligosaccharide	45:68	N-linked oligosaccharide of immunoglobulin A1 from normal human serum	45:113	Evidence for a site-specific fucosylation of N-linked oligosaccharide of immunoglobulin A1 from normal human serum.
10211705	0	61	gly	fucosylation	29:40	arg1	oligosaccharide					54:68	N-linked oligosaccharide	45:68	N-linked oligosaccharide of immunoglobulin A1 from normal human serum	45:113	Evidence for a site-specific fucosylation of N-linked oligosaccharide of immunoglobulin A1 from normal human serum.
10211705	2	62	theme	endoproteinase	351:364	arg1	digest					372:377	the endoproteinase Asp-N digest	347:377	the endoproteinase Asp-N digest of the IgA1 heavy chain	347:401	Two glycopeptides, GP1 and GP2, prepared from the endoproteinase Asp-N digest of the IgA1 heavy chain, were derived from the CH2 domain (N-glycan site at Asn263) and the tailpiece portion (N-glycan site at Asn459), respectively.
10211705	1	63	theme	time-of-flight	253:266	arg1	spectrometry					273:284	matrix-assisted laser desorption ionization time-of-flight mass spectrometry	209:284	matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOFMS)	209:298	Glycopeptides containing the N-linked oligosaccharide from human serum IgA1 were analyzed by matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOFMS).
10211705	1	63	theme	time-of-flight	253:266	arg1	MALDI-TOFMS					287:297	MALDI-TOFMS	287:297	MALDI-TOFMS	287:297	Glycopeptides containing the N-linked oligosaccharide from human serum IgA1 were analyzed by matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOFMS).
10211705	6	64	link	N-linked	1101:1108	arg1	oligosaccharide					1110:1124	the N-linked oligosaccharide	1097:1124	the N-linked oligosaccharide	1097:1124	Thus, the site-specific fucosylation of the N-linked oligosaccharide on the tailpiece of the alpha1 chain became evident for normal human serum IgA1.
10211705	5	65	theme	fucosylated	980:990	arg1	chain					1008:1012	a fully galactosylated and fucosylated bianntena sugar chain	953:1012	a fully galactosylated and fucosylated bianntena sugar chain partly bearing a bisecting GlcNAc residue	953:1054	On the other hand, the GP2 fraction corresponded to the glycopeptides having a fully galactosylated and fucosylated bianntena sugar chain partly bearing a bisecting GlcNAc residue.
10211705	1	66	theme	N-linked	145:152	arg1	oligosaccharide					154:168	the N-linked oligosaccharide	141:168	the N-linked oligosaccharide from human serum IgA1	141:190	Glycopeptides containing the N-linked oligosaccharide from human serum IgA1 were analyzed by matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOFMS).
10211705	1	67	theme	mass	268:271	arg1	spectrometry					273:284	matrix-assisted laser desorption ionization time-of-flight mass spectrometry	209:284	matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOFMS)	209:298	Glycopeptides containing the N-linked oligosaccharide from human serum IgA1 were analyzed by matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOFMS).
10211705	1	67	theme	mass	268:271	arg1	MALDI-TOFMS					287:297	MALDI-TOFMS	287:297	MALDI-TOFMS	287:297	Glycopeptides containing the N-linked oligosaccharide from human serum IgA1 were analyzed by matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOFMS).
10211705	0	68	theme	immunoglobulin	73:86	arg1	A1					88:89	immunoglobulin A1	73:89	immunoglobulin A1	73:89	Evidence for a site-specific fucosylation of N-linked oligosaccharide of immunoglobulin A1 from normal human serum.
10211705	2	69	from	Asn459	507:512	arg1	site					499:502	N-glycan site	490:502	N-glycan site	490:502	Two glycopeptides, GP1 and GP2, prepared from the endoproteinase Asp-N digest of the IgA1 heavy chain, were derived from the CH2 domain (N-glycan site at Asn263) and the tailpiece portion (N-glycan site at Asn459), respectively.
10211705	4	70	theme	sugar	798:802	arg1	chain					804:808	a fully galactosylated bianntena sugar chain	765:808	a fully galactosylated bianntena sugar chain with or without a bisecting N-acetylglucosamine (GlcNAc) residue	765:873	GP1 was composed of two major components having a fully galactosylated bianntena sugar chain with or without a bisecting N-acetylglucosamine (GlcNAc) residue.
10211705	6	71	from	fucosylation	1081:1092	arg1	tailpiece					1133:1141	the tailpiece	1129:1141	the tailpiece of the alpha1 chain	1129:1161	Thus, the site-specific fucosylation of the N-linked oligosaccharide on the tailpiece of the alpha1 chain became evident for normal human serum IgA1.
10211705	2	72	theme	heavy	391:395	arg1	chain					397:401	the IgA1 heavy chain	382:401	the IgA1 heavy chain	382:401	Two glycopeptides, GP1 and GP2, prepared from the endoproteinase Asp-N digest of the IgA1 heavy chain, were derived from the CH2 domain (N-glycan site at Asn263) and the tailpiece portion (N-glycan site at Asn459), respectively.
10211705	6	73	theme	N-linked	1101:1108	arg1	oligosaccharide					1110:1124	the N-linked oligosaccharide	1097:1124	the N-linked oligosaccharide	1097:1124	Thus, the site-specific fucosylation of the N-linked oligosaccharide on the tailpiece of the alpha1 chain became evident for normal human serum IgA1.
10211705	4	74	theme	bianntena	788:796	arg1	chain					804:808	a fully galactosylated bianntena sugar chain	765:808	a fully galactosylated bianntena sugar chain with or without a bisecting N-acetylglucosamine (GlcNAc) residue	765:873	GP1 was composed of two major components having a fully galactosylated bianntena sugar chain with or without a bisecting N-acetylglucosamine (GlcNAc) residue.
10211705	1	75	from	IgA1	187:190	arg1	oligosaccharide					154:168	the N-linked oligosaccharide	141:168	the N-linked oligosaccharide from human serum IgA1	141:190	Glycopeptides containing the N-linked oligosaccharide from human serum IgA1 were analyzed by matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOFMS).
10211705	2	76	theme	IgA1	386:389	arg1	chain					397:401	the IgA1 heavy chain	382:401	the IgA1 heavy chain	382:401	Two glycopeptides, GP1 and GP2, prepared from the endoproteinase Asp-N digest of the IgA1 heavy chain, were derived from the CH2 domain (N-glycan site at Asn263) and the tailpiece portion (N-glycan site at Asn459), respectively.
8174273	1	0	with	individuals	237:247	arg1	cirrhosis					281:289	liver cirrhosis	275:289	liver cirrhosis	275:289	The asparagine-linked sugar chains in serum transferrin purified from patients with hepatocellular carcinoma (n = 13), healthy individuals (n = 5) and patients with liver cirrhosis (n = 6) were compared.
8174273	1	0	with	individuals	237:247	arg1	carcinoma					209:217	hepatocellular carcinoma	194:217	hepatocellular carcinoma	194:217	The asparagine-linked sugar chains in serum transferrin purified from patients with hepatocellular carcinoma (n = 13), healthy individuals (n = 5) and patients with liver cirrhosis (n = 6) were compared.
8174273	2	1	theme	Sugar	314:318	arg1	chains					320:325	Sugar chains	314:325	Sugar chains released with N-glycanase from desialylated and pepsin-digested transferrin	314:401	Sugar chains released with N-glycanase from desialylated and pepsin-digested transferrin were derivatized by reductive pyridylamination.
8174273	0	2	link	asparagine-linked	14:30	arg1	glycosylation					32:44	asparagine-linked glycosylation	14:44	asparagine-linked glycosylation	14:44	Alteration of asparagine-linked glycosylation in serum transferrin of patients with hepatocellular carcinoma.
8174273	3	3	theme	1-4GlcNAc	939:947	arg1	alpha					1020:1024	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3	989:1028	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3	989:1028	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	3	theme	1-4GlcNAc	939:947	arg1	alpha					961:965	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6	930:969	an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients	830:1110	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	3	theme	1-4GlcNAc	939:947	arg1	beta					978:981	GlcNAc beta 1-4	971:985	GlcNAc beta 1-4	971:985	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	4	theme	1-2Man	732:737	arg1	chain					624:628	a biantennary complex-type sugar chain	591:628	a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients	591:824	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	4	theme	1-2Man	732:737	arg1	alpha					739:743	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3	708:747	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3	708:747	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	5	with	combination	525:535	arg1	digestion					557:565	exoglycosidase digestion	542:565	exoglycosidase digestion	542:565	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	6	theme	1-4GlcNAc	717:725	arg1	chain					624:628	a biantennary complex-type sugar chain	591:628	a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients	591:824	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	6	theme	1-4GlcNAc	717:725	arg1	alpha					739:743	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3	708:747	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3	708:747	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	7	theme	exoglycosidase	542:555	arg1	digestion					557:565	exoglycosidase digestion	542:565	exoglycosidase digestion	542:565	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	8	theme	Man	750:752	arg1	beta					769:772	a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4	591:776	a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients	591:824	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	8	theme	Man	750:752	arg1	alpha					782:786	Fuc alpha 1-6	778:790	Fuc alpha 1-6	778:790	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	9	dep	chain	624:628	arg1	1-6					704:706	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6	667:706	a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients	591:824	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	10	theme	cancer	1096:1101	arg1	patients					1103:1110	the 13 cancer patients	1089:1110	the 13 cancer patients	1089:1110	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	11	from	patients	817:824	arg1	increase					579:586	an increase	576:586	an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients	576:824	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	11	from	patients	817:824	arg1	increase					833:840	an increase	830:840	an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients	830:1110	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	4	12	theme	alpha	1251:1255	arg1	glycoprotein					1262:1273	alpha 2-HS glycoprotein	1251:1273	alpha 2-HS glycoprotein	1251:1273	Further, the fucosylated alteration of the sugar chain was detected also in alpha 1-antitrypsin, hemopexin, alpha 1-acid glycoprotein and alpha 2-HS glycoprotein from one of the patients with increased fucosylated transferrin.
8174273	4	12	theme	alpha	1251:1255	arg1	1-antitrypsin					1195:1207	alpha 1-antitrypsin	1189:1207	alpha 1-antitrypsin	1189:1207	Further, the fucosylated alteration of the sugar chain was detected also in alpha 1-antitrypsin, hemopexin, alpha 1-acid glycoprotein and alpha 2-HS glycoprotein from one of the patients with increased fucosylated transferrin.
8174273	3	13	theme	chain	624:628	arg1	beta					769:772	a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4	591:776	a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients	591:824	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	13	theme	chain	624:628	arg1	alpha					782:786	Fuc alpha 1-6	778:790	Fuc alpha 1-6	778:790	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	4	14	theme	2-HS	1257:1260	arg1	glycoprotein					1262:1273	alpha 2-HS glycoprotein	1251:1273	alpha 2-HS glycoprotein	1251:1273	Further, the fucosylated alteration of the sugar chain was detected also in alpha 1-antitrypsin, hemopexin, alpha 1-acid glycoprotein and alpha 2-HS glycoprotein from one of the patients with increased fucosylated transferrin.
8174273	4	14	theme	2-HS	1257:1260	arg1	1-antitrypsin					1195:1207	alpha 1-antitrypsin	1189:1207	alpha 1-antitrypsin	1189:1207	Further, the fucosylated alteration of the sugar chain was detected also in alpha 1-antitrypsin, hemopexin, alpha 1-acid glycoprotein and alpha 2-HS glycoprotein from one of the patients with increased fucosylated transferrin.
8174273	3	15	theme	1-4GlcNAc	759:767	arg1	beta					769:772	a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4	591:776	a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients	591:824	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	15	theme	1-4GlcNAc	759:767	arg1	alpha					782:786	Fuc alpha 1-6	778:790	Fuc alpha 1-6	778:790	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	16	theme	complex-type	605:616	arg1	chain					624:628	a biantennary complex-type sugar chain	591:628	a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients	591:824	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	16	theme	complex-type	605:616	arg1	alpha					739:743	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3	708:747	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3	708:747	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	17	gly	fucosylated	866:876	arg1	core					890:893	a fucosylated trimannosyl core	864:893	a fucosylated trimannosyl core	864:893	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	18	from	increase	579:586	arg1	patients					817:824	7 of 13 cancer patients	802:824	7 of 13 cancer patients	802:824	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	18	from	increase	579:586	arg1	patients					1103:1110	the 13 cancer patients	1089:1110	the 13 cancer patients	1089:1110	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	18	from	increase	579:586	arg1	one					1082:1084	one	1082:1084	one	1082:1084	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	19	theme	trimannosyl	649:659	arg1	core					661:664	a fucosylated trimannosyl core	635:664	a fucosylated trimannosyl core	635:664	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	20	theme	GlcNAc	971:976	arg1	alpha					961:965	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6	930:969	an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients	830:1110	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	20	theme	GlcNAc	971:976	arg1	beta					978:981	GlcNAc beta 1-4	971:985	GlcNAc beta 1-4	971:985	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	21	theme	Fuc	778:780	arg1	beta					769:772	a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4	591:776	a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients	591:824	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	21	theme	Fuc	778:780	arg1	alpha					782:786	Fuc alpha 1-6	778:790	Fuc alpha 1-6	778:790	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	0	22	theme	patients	70:77	arg1	transferrin					55:65	serum transferrin	49:65	serum transferrin of patients with hepatocellular carcinoma	49:107	Alteration of asparagine-linked glycosylation in serum transferrin of patients with hepatocellular carcinoma.
8174273	0	23	theme	hepatocellular	84:97	arg1	carcinoma					99:107	hepatocellular carcinoma	84:107	hepatocellular carcinoma	84:107	Alteration of asparagine-linked glycosylation in serum transferrin of patients with hepatocellular carcinoma.
8174273	3	24	theme	beta	1008:1011	arg1	alpha					1020:1024	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3	989:1028	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3	989:1028	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	24	theme	beta	1008:1011	arg1	alpha					961:965	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6	930:969	an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients	830:1110	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	0	25	from	Alteration	0:9	arg1	transferrin					55:65	serum transferrin	49:65	serum transferrin of patients with hepatocellular carcinoma	49:107	Alteration of asparagine-linked glycosylation in serum transferrin of patients with hepatocellular carcinoma.
8174273	3	26	theme	GlcNAc	792:797	arg1	increase					579:586	an increase	576:586	an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients	576:824	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	26	theme	GlcNAc	792:797	arg1	increase					833:840	an increase	830:840	an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients	830:1110	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	27	theme	beta	993:996	arg1	alpha					1020:1024	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3	989:1028	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3	989:1028	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	27	theme	beta	993:996	arg1	alpha					961:965	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6	930:969	an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients	830:1110	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	2	28	gly	desialylated	358:369	arg1	transferrin					391:401	desialylated and pepsin-digested transferrin	358:401	desialylated and pepsin-digested transferrin	358:401	Sugar chains released with N-glycanase from desialylated and pepsin-digested transferrin were derivatized by reductive pyridylamination.
8174273	4	29	theme	fucosylated	1126:1136	arg1	alteration					1138:1147	the fucosylated alteration	1122:1147	the fucosylated alteration of the sugar chain	1122:1166	Further, the fucosylated alteration of the sugar chain was detected also in alpha 1-antitrypsin, hemopexin, alpha 1-acid glycoprotein and alpha 2-HS glycoprotein from one of the patients with increased fucosylated transferrin.
8174273	3	30	with	chain	624:628	arg1	core					661:664	a fucosylated trimannosyl core	635:664	a fucosylated trimannosyl core	635:664	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	31	theme	sugar	847:851	arg1	chain					853:857	a sugar chain	845:857	a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine	845:927	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	4	32	gly	glycoprotein	1234:1245	arg1	1-antitrypsin					1195:1207	alpha 1-antitrypsin	1189:1207	alpha 1-antitrypsin	1189:1207	Further, the fucosylated alteration of the sugar chain was detected also in alpha 1-antitrypsin, hemopexin, alpha 1-acid glycoprotein and alpha 2-HS glycoprotein from one of the patients with increased fucosylated transferrin.
8174273	4	32	gly	glycoprotein	1234:1245	arg1	glycoprotein					1234:1245	alpha 1-acid glycoprotein	1221:1245	alpha 1-acid glycoprotein	1221:1245	Further, the fucosylated alteration of the sugar chain was detected also in alpha 1-antitrypsin, hemopexin, alpha 1-acid glycoprotein and alpha 2-HS glycoprotein from one of the patients with increased fucosylated transferrin.
8174273	1	33	from	chains	138:143	arg1	transferrin					154:164	serum transferrin	148:164	serum transferrin purified from patients with hepatocellular carcinoma (n = 13), healthy individuals (n = 5) and patients with liver cirrhosis (n = 6)	148:297	The asparagine-linked sugar chains in serum transferrin purified from patients with hepatocellular carcinoma (n = 13), healthy individuals (n = 5) and patients with liver cirrhosis (n = 6) were compared.
8174273	2	34	theme	reductive	423:431	arg1	pyridylamination					433:448	reductive pyridylamination	423:448	reductive pyridylamination	423:448	Sugar chains released with N-glycanase from desialylated and pepsin-digested transferrin were derivatized by reductive pyridylamination.
8174273	3	35	from	GlcNAc	792:797	arg1	patients					817:824	7 of 13 cancer patients	802:824	7 of 13 cancer patients	802:824	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	0	36	theme	asparagine-linked	14:30	arg1	glycosylation					32:44	asparagine-linked glycosylation	14:44	asparagine-linked glycosylation	14:44	Alteration of asparagine-linked glycosylation in serum transferrin of patients with hepatocellular carcinoma.
8174273	1	37	theme	liver	275:279	arg1	cirrhosis					281:289	liver cirrhosis	275:289	liver cirrhosis	275:289	The asparagine-linked sugar chains in serum transferrin purified from patients with hepatocellular carcinoma (n = 13), healthy individuals (n = 5) and patients with liver cirrhosis (n = 6) were compared.
8174273	3	38	theme	beta	1049:1052	arg1	GlcNAc					1072:1077	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc	930:1077	an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients	830:1110	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	1	39	theme	sugar	132:136	arg1	chains					138:143	The asparagine-linked sugar chains	110:143	The asparagine-linked sugar chains in serum transferrin purified from patients with hepatocellular carcinoma (n = 13), healthy individuals (n = 5) and patients with liver cirrhosis (n = 6)	110:297	The asparagine-linked sugar chains in serum transferrin purified from patients with hepatocellular carcinoma (n = 13), healthy individuals (n = 5) and patients with liver cirrhosis (n = 6) were compared.
8174273	3	40	theme	fucosylated	866:876	arg1	core					890:893	a fucosylated trimannosyl core	864:893	a fucosylated trimannosyl core	864:893	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	41	theme	beta	671:674	arg1	1-6					704:706	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6	667:706	a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients	591:824	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	42	theme	beta	1034:1037	arg1	beta					1049:1052	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4	930:1056	an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients	830:1110	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	42	theme	beta	1034:1037	arg1	alpha					1062:1066	Fuc alpha 1-6	1058:1070	Fuc alpha 1-6	1058:1070	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	43	theme	high	483:486	arg1	chromatography					507:520	high performance liquid chromatography	483:520	high performance liquid chromatography in combination with exoglycosidase digestion	483:565	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	1	44	theme	=	294:294	arg1	n					292:292	n = 6	292:296	n = 6	292:296	The asparagine-linked sugar chains in serum transferrin purified from patients with hepatocellular carcinoma (n = 13), healthy individuals (n = 5) and patients with liver cirrhosis (n = 6) were compared.
8174273	1	44	theme	=	294:294	arg1	patients					261:268	patients	261:268	patients with liver cirrhosis (n = 6)	261:297	The asparagine-linked sugar chains in serum transferrin purified from patients with hepatocellular carcinoma (n = 13), healthy individuals (n = 5) and patients with liver cirrhosis (n = 6) were compared.
8174273	3	45	theme	bisecting	899:907	arg1	N-acetylglucosamine					909:927	bisecting N-acetylglucosamine	899:927	bisecting N-acetylglucosamine	899:927	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	46	theme	alpha	698:702	arg1	1-6					704:706	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6	667:706	a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients	591:824	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	47	theme	chains	473:478	arg1	Analysis					451:458	Analysis	451:458	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion	451:565	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	1	48	theme	healthy	229:235	arg1	n					250:250	n = 5	250:254	n = 5	250:254	The asparagine-linked sugar chains in serum transferrin purified from patients with hepatocellular carcinoma (n = 13), healthy individuals (n = 5) and patients with liver cirrhosis (n = 6) were compared.
8174273	1	48	theme	healthy	229:235	arg1	individuals					237:247	healthy individuals	229:247	healthy individuals (n = 5)	229:255	The asparagine-linked sugar chains in serum transferrin purified from patients with hepatocellular carcinoma (n = 13), healthy individuals (n = 5) and patients with liver cirrhosis (n = 6) were compared.
8174273	3	49	theme	beta	949:952	arg1	alpha					1020:1024	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3	989:1028	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3	989:1028	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	49	theme	beta	949:952	arg1	alpha					961:965	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6	930:969	an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients	830:1110	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	49	theme	beta	949:952	arg1	beta					978:981	GlcNAc beta 1-4	971:985	GlcNAc beta 1-4	971:985	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	1	50	link	asparagine-linked	114:130	arg1	chains					138:143	The asparagine-linked sugar chains	110:143	The asparagine-linked sugar chains in serum transferrin purified from patients with hepatocellular carcinoma (n = 13), healthy individuals (n = 5) and patients with liver cirrhosis (n = 6)	110:297	The asparagine-linked sugar chains in serum transferrin purified from patients with hepatocellular carcinoma (n = 13), healthy individuals (n = 5) and patients with liver cirrhosis (n = 6) were compared.
8174273	3	51	theme	beta	686:689	arg1	1-6					704:706	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6	667:706	a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients	591:824	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	4	52	gly	fucosylated	1126:1136	arg1	alteration					1138:1147	the fucosylated alteration	1122:1147	the fucosylated alteration of the sugar chain	1122:1166	Further, the fucosylated alteration of the sugar chain was detected also in alpha 1-antitrypsin, hemopexin, alpha 1-acid glycoprotein and alpha 2-HS glycoprotein from one of the patients with increased fucosylated transferrin.
8174273	2	53	attach	released	327:334	arg1	transferrin					391:401	desialylated and pepsin-digested transferrin	358:401	desialylated and pepsin-digested transferrin	358:401	Sugar chains released with N-glycanase from desialylated and pepsin-digested transferrin were derivatized by reductive pyridylamination.
8174273	2	53	attach	released	327:334	arg2	chains					320:325	Sugar chains	314:325	Sugar chains released with N-glycanase from desialylated and pepsin-digested transferrin	314:401	Sugar chains released with N-glycanase from desialylated and pepsin-digested transferrin were derivatized by reductive pyridylamination.
8174273	3	54	theme	beta	934:937	arg1	alpha					1020:1024	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3	989:1028	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3	989:1028	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	54	theme	beta	934:937	arg1	alpha					961:965	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6	930:969	an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients	830:1110	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	54	theme	beta	934:937	arg1	beta					978:981	GlcNAc beta 1-4	971:985	GlcNAc beta 1-4	971:985	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	55	theme	beta	712:715	arg1	chain					624:628	a biantennary complex-type sugar chain	591:628	a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients	591:824	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	55	theme	beta	712:715	arg1	alpha					739:743	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3	708:747	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3	708:747	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	4	56	gly	glycoprotein	1262:1273	arg1	glycoprotein					1262:1273	alpha 2-HS glycoprotein	1251:1273	alpha 2-HS glycoprotein	1251:1273	Further, the fucosylated alteration of the sugar chain was detected also in alpha 1-antitrypsin, hemopexin, alpha 1-acid glycoprotein and alpha 2-HS glycoprotein from one of the patients with increased fucosylated transferrin.
8174273	4	56	gly	glycoprotein	1262:1273	arg1	1-antitrypsin					1195:1207	alpha 1-antitrypsin	1189:1207	alpha 1-antitrypsin	1189:1207	Further, the fucosylated alteration of the sugar chain was detected also in alpha 1-antitrypsin, hemopexin, alpha 1-acid glycoprotein and alpha 2-HS glycoprotein from one of the patients with increased fucosylated transferrin.
8174273	3	57	theme	liquid	500:505	arg1	chromatography					507:520	high performance liquid chromatography	483:520	high performance liquid chromatography in combination with exoglycosidase digestion	483:565	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	1	58	theme	=	252:252	arg1	n					250:250	n = 5	250:254	n = 5	250:254	The asparagine-linked sugar chains in serum transferrin purified from patients with hepatocellular carcinoma (n = 13), healthy individuals (n = 5) and patients with liver cirrhosis (n = 6) were compared.
8174273	1	58	theme	=	252:252	arg1	individuals					237:247	healthy individuals	229:247	healthy individuals (n = 5)	229:255	The asparagine-linked sugar chains in serum transferrin purified from patients with hepatocellular carcinoma (n = 13), healthy individuals (n = 5) and patients with liver cirrhosis (n = 6) were compared.
8174273	3	59	theme	1-4GlcNAc	998:1006	arg1	alpha					1020:1024	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3	989:1028	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3	989:1028	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	59	theme	1-4GlcNAc	998:1006	arg1	alpha					961:965	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6	930:969	an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients	830:1110	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	4	60	theme	1-acid	1227:1232	arg1	1-antitrypsin					1195:1207	alpha 1-antitrypsin	1189:1207	alpha 1-antitrypsin	1189:1207	Further, the fucosylated alteration of the sugar chain was detected also in alpha 1-antitrypsin, hemopexin, alpha 1-acid glycoprotein and alpha 2-HS glycoprotein from one of the patients with increased fucosylated transferrin.
8174273	4	60	theme	1-acid	1227:1232	arg1	glycoprotein					1234:1245	alpha 1-acid glycoprotein	1221:1245	alpha 1-acid glycoprotein	1221:1245	Further, the fucosylated alteration of the sugar chain was detected also in alpha 1-antitrypsin, hemopexin, alpha 1-acid glycoprotein and alpha 2-HS glycoprotein from one of the patients with increased fucosylated transferrin.
8174273	3	61	from	chromatography	507:520	arg1	combination					525:535	combination	525:535	combination with exoglycosidase digestion	525:565	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	62	theme	alpha	961:965	arg1	beta					1049:1052	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4	930:1056	an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients	830:1110	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	62	theme	alpha	961:965	arg1	alpha					1062:1066	Fuc alpha 1-6	1058:1070	Fuc alpha 1-6	1058:1070	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	63	from	increase	833:840	arg1	patients					817:824	7 of 13 cancer patients	802:824	7 of 13 cancer patients	802:824	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	63	from	increase	833:840	arg1	patients					1103:1110	the 13 cancer patients	1089:1110	the 13 cancer patients	1089:1110	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	63	from	increase	833:840	arg1	one					1082:1084	one	1082:1084	one	1082:1084	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	4	64	theme	alpha	1189:1193	arg1	hemopexin					1210:1218	hemopexin	1210:1218	hemopexin	1210:1218	Further, the fucosylated alteration of the sugar chain was detected also in alpha 1-antitrypsin, hemopexin, alpha 1-acid glycoprotein and alpha 2-HS glycoprotein from one of the patients with increased fucosylated transferrin.
8174273	4	64	theme	alpha	1189:1193	arg1	1-antitrypsin					1195:1207	alpha 1-antitrypsin	1189:1207	alpha 1-antitrypsin	1189:1207	Further, the fucosylated alteration of the sugar chain was detected also in alpha 1-antitrypsin, hemopexin, alpha 1-acid glycoprotein and alpha 2-HS glycoprotein from one of the patients with increased fucosylated transferrin.
8174273	4	64	theme	alpha	1189:1193	arg1	glycoprotein					1262:1273	alpha 2-HS glycoprotein	1251:1273	alpha 2-HS glycoprotein	1251:1273	Further, the fucosylated alteration of the sugar chain was detected also in alpha 1-antitrypsin, hemopexin, alpha 1-acid glycoprotein and alpha 2-HS glycoprotein from one of the patients with increased fucosylated transferrin.
8174273	4	64	theme	alpha	1189:1193	arg1	glycoprotein					1234:1245	alpha 1-acid glycoprotein	1221:1245	alpha 1-acid glycoprotein	1221:1245	Further, the fucosylated alteration of the sugar chain was detected also in alpha 1-antitrypsin, hemopexin, alpha 1-acid glycoprotein and alpha 2-HS glycoprotein from one of the patients with increased fucosylated transferrin.
8174273	0	65	with	patients	70:77	arg1	carcinoma					99:107	hepatocellular carcinoma	84:107	hepatocellular carcinoma	84:107	Alteration of asparagine-linked glycosylation in serum transferrin of patients with hepatocellular carcinoma.
8174273	1	66	theme	hepatocellular	194:207	arg1	carcinoma					209:217	hepatocellular carcinoma	194:217	hepatocellular carcinoma	194:217	The asparagine-linked sugar chains in serum transferrin purified from patients with hepatocellular carcinoma (n = 13), healthy individuals (n = 5) and patients with liver cirrhosis (n = 6) were compared.
8174273	3	67	gly	fucosylated	637:647	arg1	core					661:664	a fucosylated trimannosyl core	635:664	a fucosylated trimannosyl core	635:664	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	68	theme	beta	727:730	arg1	chain					624:628	a biantennary complex-type sugar chain	591:628	a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients	591:824	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	68	theme	beta	727:730	arg1	alpha					739:743	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3	708:747	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3	708:747	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	1	69	with	patients	261:268	arg1	cirrhosis					281:289	liver cirrhosis	275:289	liver cirrhosis	275:289	The asparagine-linked sugar chains in serum transferrin purified from patients with hepatocellular carcinoma (n = 13), healthy individuals (n = 5) and patients with liver cirrhosis (n = 6) were compared.
8174273	1	69	with	patients	261:268	arg1	carcinoma					209:217	hepatocellular carcinoma	194:217	hepatocellular carcinoma	194:217	The asparagine-linked sugar chains in serum transferrin purified from patients with hepatocellular carcinoma (n = 13), healthy individuals (n = 5) and patients with liver cirrhosis (n = 6) were compared.
8174273	4	70	from	one	1280:1282	arg1	glycoprotein					1262:1273	alpha 2-HS glycoprotein	1251:1273	alpha 2-HS glycoprotein	1251:1273	Further, the fucosylated alteration of the sugar chain was detected also in alpha 1-antitrypsin, hemopexin, alpha 1-acid glycoprotein and alpha 2-HS glycoprotein from one of the patients with increased fucosylated transferrin.
8174273	4	70	from	one	1280:1282	arg1	1-antitrypsin					1195:1207	alpha 1-antitrypsin	1189:1207	alpha 1-antitrypsin	1189:1207	Further, the fucosylated alteration of the sugar chain was detected also in alpha 1-antitrypsin, hemopexin, alpha 1-acid glycoprotein and alpha 2-HS glycoprotein from one of the patients with increased fucosylated transferrin.
8174273	4	70	from	one	1280:1282	arg1	glycoprotein					1234:1245	alpha 1-acid glycoprotein	1221:1245	alpha 1-acid glycoprotein	1221:1245	Further, the fucosylated alteration of the sugar chain was detected also in alpha 1-antitrypsin, hemopexin, alpha 1-acid glycoprotein and alpha 2-HS glycoprotein from one of the patients with increased fucosylated transferrin.
8174273	3	71	theme	beta	754:757	arg1	beta					769:772	a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4	591:776	a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients	591:824	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	71	theme	beta	754:757	arg1	alpha					782:786	Fuc alpha 1-6	778:790	Fuc alpha 1-6	778:790	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	4	72	gly	fucosylated	1315:1325	arg1	transferrin					1327:1337	increased fucosylated transferrin	1305:1337	increased fucosylated transferrin	1305:1337	Further, the fucosylated alteration of the sugar chain was detected also in alpha 1-antitrypsin, hemopexin, alpha 1-acid glycoprotein and alpha 2-HS glycoprotein from one of the patients with increased fucosylated transferrin.
8174273	1	73	theme	=	222:222	arg1	n					220:220	n = 13	220:225	n = 13	220:225	The asparagine-linked sugar chains in serum transferrin purified from patients with hepatocellular carcinoma (n = 13), healthy individuals (n = 5) and patients with liver cirrhosis (n = 6) were compared.
8174273	1	73	theme	=	222:222	arg1	patients					180:187	patients	180:187	patients with hepatocellular carcinoma (n = 13)	180:226	The asparagine-linked sugar chains in serum transferrin purified from patients with hepatocellular carcinoma (n = 13), healthy individuals (n = 5) and patients with liver cirrhosis (n = 6) were compared.
8174273	3	74	theme	patients	1103:1110	arg1	patients					1103:1110	the 13 cancer patients	1089:1110	the 13 cancer patients	1089:1110	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	74	theme	patients	1103:1110	arg1	one					1082:1084	one	1082:1084	one	1082:1084	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	75	theme	sugar	618:622	arg1	chain					624:628	a biantennary complex-type sugar chain	591:628	a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients	591:824	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	75	theme	sugar	618:622	arg1	alpha					739:743	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3	708:747	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3	708:747	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	76	theme	biantennary	593:603	arg1	chain					624:628	a biantennary complex-type sugar chain	591:628	a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients	591:824	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	76	theme	biantennary	593:603	arg1	alpha					739:743	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3	708:747	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3	708:747	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	77	theme	beta	769:772	arg1	GlcNAc					792:797	a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc	591:797	a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients	591:824	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	78	with	chain	853:857	arg1	core					890:893	a fucosylated trimannosyl core	864:893	a fucosylated trimannosyl core	864:893	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	78	with	chain	853:857	arg1	N-acetylglucosamine					909:927	bisecting N-acetylglucosamine	899:927	bisecting N-acetylglucosamine	899:927	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	79	theme	fucosylated	637:647	arg1	core					661:664	a fucosylated trimannosyl core	635:664	a fucosylated trimannosyl core	635:664	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	1	80	theme	serum	148:152	arg1	transferrin					154:164	serum transferrin	148:164	serum transferrin purified from patients with hepatocellular carcinoma (n = 13), healthy individuals (n = 5) and patients with liver cirrhosis (n = 6)	148:297	The asparagine-linked sugar chains in serum transferrin purified from patients with hepatocellular carcinoma (n = 13), healthy individuals (n = 5) and patients with liver cirrhosis (n = 6) were compared.
8174273	3	81	theme	cancer	810:815	arg1	patients					817:824	7 of 13 cancer patients	802:824	7 of 13 cancer patients	802:824	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	4	82	theme	fucosylated	1315:1325	arg1	transferrin					1327:1337	increased fucosylated transferrin	1305:1337	increased fucosylated transferrin	1305:1337	Further, the fucosylated alteration of the sugar chain was detected also in alpha 1-antitrypsin, hemopexin, alpha 1-acid glycoprotein and alpha 2-HS glycoprotein from one of the patients with increased fucosylated transferrin.
8174273	1	83	with	patients	180:187	arg1	cirrhosis					281:289	liver cirrhosis	275:289	liver cirrhosis	275:289	The asparagine-linked sugar chains in serum transferrin purified from patients with hepatocellular carcinoma (n = 13), healthy individuals (n = 5) and patients with liver cirrhosis (n = 6) were compared.
8174273	1	83	with	patients	180:187	arg1	carcinoma					209:217	hepatocellular carcinoma	194:217	hepatocellular carcinoma	194:217	The asparagine-linked sugar chains in serum transferrin purified from patients with hepatocellular carcinoma (n = 13), healthy individuals (n = 5) and patients with liver cirrhosis (n = 6) were compared.
8174273	4	84	theme	chain	1162:1166	arg1	alteration					1138:1147	the fucosylated alteration	1122:1147	the fucosylated alteration of the sugar chain	1122:1166	Further, the fucosylated alteration of the sugar chain was detected also in alpha 1-antitrypsin, hemopexin, alpha 1-acid glycoprotein and alpha 2-HS glycoprotein from one of the patients with increased fucosylated transferrin.
8174273	4	85	theme	patients	1291:1298	arg1	one					1280:1282	one	1280:1282	one	1280:1282	Further, the fucosylated alteration of the sugar chain was detected also in alpha 1-antitrypsin, hemopexin, alpha 1-acid glycoprotein and alpha 2-HS glycoprotein from one of the patients with increased fucosylated transferrin.
8174273	4	85	theme	patients	1291:1298	arg1	patients					1291:1298	the patients	1287:1298	the patients with increased fucosylated transferrin	1287:1337	Further, the fucosylated alteration of the sugar chain was detected also in alpha 1-antitrypsin, hemopexin, alpha 1-acid glycoprotein and alpha 2-HS glycoprotein from one of the patients with increased fucosylated transferrin.
8174273	3	86	theme	Gal	989:991	arg1	alpha					1020:1024	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3	989:1028	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3	989:1028	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	86	theme	Gal	989:991	arg1	alpha					961:965	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6	930:969	an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients	830:1110	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	4	87	theme	increased	1305:1313	arg1	transferrin					1327:1337	increased fucosylated transferrin	1305:1337	increased fucosylated transferrin	1305:1337	Further, the fucosylated alteration of the sugar chain was detected also in alpha 1-antitrypsin, hemopexin, alpha 1-acid glycoprotein and alpha 2-HS glycoprotein from one of the patients with increased fucosylated transferrin.
8174273	2	88	theme	desialylated	358:369	arg1	transferrin					391:401	desialylated and pepsin-digested transferrin	358:401	desialylated and pepsin-digested transferrin	358:401	Sugar chains released with N-glycanase from desialylated and pepsin-digested transferrin were derivatized by reductive pyridylamination.
8174273	3	89	theme	1-2Man	1013:1018	arg1	alpha					1020:1024	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3	989:1028	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3	989:1028	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	89	theme	1-2Man	1013:1018	arg1	alpha					961:965	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6	930:969	an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients	830:1110	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	90	dep	increase	833:840	arg1	GlcNAc					1072:1077	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc	930:1077	an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients	830:1110	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	91	theme	chain	853:857	arg1	increase					579:586	an increase	576:586	an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients	576:824	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	91	theme	chain	853:857	arg1	increase					833:840	an increase	830:840	an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients	830:1110	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	4	92	theme	sugar	1156:1160	arg1	chain					1162:1166	the sugar chain	1152:1166	the sugar chain	1152:1166	Further, the fucosylated alteration of the sugar chain was detected also in alpha 1-antitrypsin, hemopexin, alpha 1-acid glycoprotein and alpha 2-HS glycoprotein from one of the patients with increased fucosylated transferrin.
8174273	0	93	theme	glycosylation	32:44	arg1	Alteration					0:9	Alteration	0:9	Alteration of asparagine-linked glycosylation in serum transferrin of patients with hepatocellular carcinoma	0:107	Alteration of asparagine-linked glycosylation in serum transferrin of patients with hepatocellular carcinoma.
8174273	3	94	theme	1-4GlcNAc	1039:1047	arg1	beta					1049:1052	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4	930:1056	an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients	830:1110	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	94	theme	1-4GlcNAc	1039:1047	arg1	alpha					1062:1066	Fuc alpha 1-6	1058:1070	Fuc alpha 1-6	1058:1070	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	1	95	theme	asparagine-linked	114:130	arg1	chains					138:143	The asparagine-linked sugar chains	110:143	The asparagine-linked sugar chains in serum transferrin purified from patients with hepatocellular carcinoma (n = 13), healthy individuals (n = 5) and patients with liver cirrhosis (n = 6)	110:297	The asparagine-linked sugar chains in serum transferrin purified from patients with hepatocellular carcinoma (n = 13), healthy individuals (n = 5) and patients with liver cirrhosis (n = 6) were compared.
8174273	3	96	theme	Gal	667:669	arg1	1-6					704:706	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6	667:706	a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients	591:824	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	97	theme	sugar	467:471	arg1	chains					473:478	the sugar chains	463:478	the sugar chains	463:478	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	0	98	theme	serum	49:53	arg1	transferrin					55:65	serum transferrin	49:65	serum transferrin of patients with hepatocellular carcinoma	49:107	Alteration of asparagine-linked glycosylation in serum transferrin of patients with hepatocellular carcinoma.
8174273	3	99	theme	Man	1030:1032	arg1	beta					1049:1052	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4	930:1056	an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients	830:1110	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	99	theme	Man	1030:1032	arg1	alpha					1062:1066	Fuc alpha 1-6	1058:1070	Fuc alpha 1-6	1058:1070	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	100	theme	trimannosyl	878:888	arg1	core					890:893	a fucosylated trimannosyl core	864:893	a fucosylated trimannosyl core	864:893	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	2	101	theme	pepsin-digested	375:389	arg1	transferrin					391:401	desialylated and pepsin-digested transferrin	358:401	desialylated and pepsin-digested transferrin	358:401	Sugar chains released with N-glycanase from desialylated and pepsin-digested transferrin were derivatized by reductive pyridylamination.
8174273	3	102	theme	Fuc	1058:1060	arg1	beta					1049:1052	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4	930:1056	an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients	830:1110	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	102	theme	Fuc	1058:1060	arg1	alpha					1062:1066	Fuc alpha 1-6	1058:1070	Fuc alpha 1-6	1058:1070	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	103	theme	Gal	930:932	arg1	alpha					1020:1024	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3	989:1028	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3	989:1028	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	103	theme	Gal	930:932	arg1	alpha					961:965	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6	930:969	an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients	830:1110	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	103	theme	Gal	930:932	arg1	beta					978:981	GlcNAc beta 1-4	971:985	GlcNAc beta 1-4	971:985	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	4	104	theme	alpha	1221:1225	arg1	1-antitrypsin					1195:1207	alpha 1-antitrypsin	1189:1207	alpha 1-antitrypsin	1189:1207	Further, the fucosylated alteration of the sugar chain was detected also in alpha 1-antitrypsin, hemopexin, alpha 1-acid glycoprotein and alpha 2-HS glycoprotein from one of the patients with increased fucosylated transferrin.
8174273	4	104	theme	alpha	1221:1225	arg1	glycoprotein					1234:1245	alpha 1-acid glycoprotein	1221:1245	alpha 1-acid glycoprotein	1221:1245	Further, the fucosylated alteration of the sugar chain was detected also in alpha 1-antitrypsin, hemopexin, alpha 1-acid glycoprotein and alpha 2-HS glycoprotein from one of the patients with increased fucosylated transferrin.
8174273	3	105	theme	1-2Man	691:696	arg1	1-6					704:706	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6	667:706	a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients	591:824	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	106	theme	performance	488:498	arg1	chromatography					507:520	high performance liquid chromatography	483:520	high performance liquid chromatography in combination with exoglycosidase digestion	483:565	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	107	theme	1-4GlcNAc	676:684	arg1	1-6					704:706	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6	667:706	a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients	591:824	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	108	theme	1-2Man	954:959	arg1	alpha					1020:1024	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3	989:1028	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3	989:1028	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	108	theme	1-2Man	954:959	arg1	alpha					961:965	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6	930:969	an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients	830:1110	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	108	theme	1-2Man	954:959	arg1	beta					978:981	GlcNAc beta 1-4	971:985	GlcNAc beta 1-4	971:985	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	4	109	located	detected	1172:1179	arg2	alteration					1138:1147	the fucosylated alteration	1122:1147	the fucosylated alteration of the sugar chain	1122:1166	Further, the fucosylated alteration of the sugar chain was detected also in alpha 1-antitrypsin, hemopexin, alpha 1-acid glycoprotein and alpha 2-HS glycoprotein from one of the patients with increased fucosylated transferrin.
8174273	4	109	located	detected	1172:1179	arg1	hemopexin					1210:1218	hemopexin	1210:1218	hemopexin	1210:1218	Further, the fucosylated alteration of the sugar chain was detected also in alpha 1-antitrypsin, hemopexin, alpha 1-acid glycoprotein and alpha 2-HS glycoprotein from one of the patients with increased fucosylated transferrin.
8174273	4	109	located	detected	1172:1179	arg1	1-antitrypsin					1195:1207	alpha 1-antitrypsin	1189:1207	alpha 1-antitrypsin	1189:1207	Further, the fucosylated alteration of the sugar chain was detected also in alpha 1-antitrypsin, hemopexin, alpha 1-acid glycoprotein and alpha 2-HS glycoprotein from one of the patients with increased fucosylated transferrin.
8174273	4	109	located	detected	1172:1179	arg1	glycoprotein					1262:1273	alpha 2-HS glycoprotein	1251:1273	alpha 2-HS glycoprotein	1251:1273	Further, the fucosylated alteration of the sugar chain was detected also in alpha 1-antitrypsin, hemopexin, alpha 1-acid glycoprotein and alpha 2-HS glycoprotein from one of the patients with increased fucosylated transferrin.
8174273	4	109	located	detected	1172:1179	arg1	glycoprotein					1234:1245	alpha 1-acid glycoprotein	1221:1245	alpha 1-acid glycoprotein	1221:1245	Further, the fucosylated alteration of the sugar chain was detected also in alpha 1-antitrypsin, hemopexin, alpha 1-acid glycoprotein and alpha 2-HS glycoprotein from one of the patients with increased fucosylated transferrin.
8174273	3	110	theme	Gal	708:710	arg1	chain					624:628	a biantennary complex-type sugar chain	591:628	a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients	591:824	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	3	110	theme	Gal	708:710	arg1	alpha					739:743	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3	708:747	Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3	708:747	Analysis of the sugar chains by high performance liquid chromatography in combination with exoglycosidase digestion revealed an increase of a biantennary complex-type sugar chain with a fucosylated trimannosyl core; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3) Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in 7 of 13 cancer patients and an increase of a sugar chain with a fucosylated trimannosyl core and bisecting N-acetylglucosamine; Gal beta 1-4GlcNAc beta 1-2Man alpha 1-6(GlcNAc beta 1-4) (Gal beta 1-4GlcNAc beta 1-2Man alpha 1-3)Man beta 1-4GlcNAc beta 1-4(Fuc alpha 1-6)GlcNAc in one of the 13 cancer patients.
8174273	4	111	with	patients	1291:1298	arg1	transferrin					1327:1337	increased fucosylated transferrin	1305:1337	increased fucosylated transferrin	1305:1337	Further, the fucosylated alteration of the sugar chain was detected also in alpha 1-antitrypsin, hemopexin, alpha 1-acid glycoprotein and alpha 2-HS glycoprotein from one of the patients with increased fucosylated transferrin.
11067851	2	0	with	length	325:330	arg1	Cys					347:349	conserved Cys and Trp residues	337:366	Cys	347:349	Some of these functions have been localized to the three thrombospondin type 1 repeats (TSRs), modules of approximately 60 amino acids in length with conserved Cys and Trp residues.
11067851	2	0	with	length	325:330	arg1	residues					359:366	conserved Cys and Trp residues	337:366	residues	359:366	Some of these functions have been localized to the three thrombospondin type 1 repeats (TSRs), modules of approximately 60 amino acids in length with conserved Cys and Trp residues.
11067851	8	1	contain	carry	1113:1117	arg1	Thr-432					1068:1074	Thr-432	1068:1074	Thr-432	1068:1074	By using a novel mass spectrometric approach, it was found that Ser-377, Thr-432, and Thr-489 in the motif CSX(S/T)CG carry the O-linked disaccharide Glc-Fuc-O-Ser/Thr.
11067851	8	1	contain	carry	1113:1117	arg1	Thr-489					1081:1087	Thr-489	1081:1087	Thr-489	1081:1087	By using a novel mass spectrometric approach, it was found that Ser-377, Thr-432, and Thr-489 in the motif CSX(S/T)CG carry the O-linked disaccharide Glc-Fuc-O-Ser/Thr.
11067851	8	1	contain	carry	1113:1117	arg1	Ser-377					1059:1065	Ser-377	1059:1065	Ser-377	1059:1065	By using a novel mass spectrometric approach, it was found that Ser-377, Thr-432, and Thr-489 in the motif CSX(S/T)CG carry the O-linked disaccharide Glc-Fuc-O-Ser/Thr.
11067851	8	1	contain	carry	1113:1117	arg2	disaccharide					1132:1143	the O-linked disaccharide	1119:1143	the O-linked disaccharide Glc-Fuc-O-Ser/Thr	1119:1161	By using a novel mass spectrometric approach, it was found that Ser-377, Thr-432, and Thr-489 in the motif CSX(S/T)CG carry the O-linked disaccharide Glc-Fuc-O-Ser/Thr.
11067851	9	2	theme	first	1176:1180	arg1	protein					1182:1188	the first protein	1172:1188	the first protein in which such a disaccharide has been identified, although protein O-fucosylation is well described in epidermal growth factor-like modules	1172:1328	This is the first protein in which such a disaccharide has been identified, although protein O-fucosylation is well described in epidermal growth factor-like modules.
11067851	9	2	theme	first	1176:1180	arg1	This					1164:1167	This	1164:1167	This	1164:1167	This is the first protein in which such a disaccharide has been identified, although protein O-fucosylation is well described in epidermal growth factor-like modules.
11067851	2	3	theme	amino	310:314	arg1	acids					316:320	approximately 60 amino acids	293:320	approximately 60 amino acids	293:320	Some of these functions have been localized to the three thrombospondin type 1 repeats (TSRs), modules of approximately 60 amino acids in length with conserved Cys and Trp residues.
11067851	4	4	theme	residue	535:541	arg1	attachment					503:512	the attachment	499:512	the attachment of an alpha-mannosyl residue to the C-2 atom of the first tryptophan	499:581	This modification involves the attachment of an alpha-mannosyl residue to the C-2 atom of the first tryptophan.
11067851	8	5	from	Thr-432	1068:1074	arg1	CG					1110:1111	the motif CSX(S/T)CG	1092:1111	the motif CSX(S/T)CG	1092:1111	By using a novel mass spectrometric approach, it was found that Ser-377, Thr-432, and Thr-489 in the motif CSX(S/T)CG carry the O-linked disaccharide Glc-Fuc-O-Ser/Thr.
11067851	6	6	theme	such	831:834	arg1	cells					836:840	such cells	831:840	such cells	831:840	Mannosylation also occurred in recombinant, baculovirally expressed TSR modules from Sf9 and "High Five" cells, contradictory to earlier reports that such cells do not carry out this reaction.
11067851	5	7	theme	human	596:600	arg1	TSP-1					611:615	human platelet TSP-1	596:615	human platelet TSP-1	596:615	Analysis of human platelet TSP-1 revealed that Trp-368, -420, -423, and -480 are C-mannosylated.
11067851	1	8	theme	cell	150:153	arg1	adhesion					155:162	cell adhesion	150:162	cell adhesion	150:162	Thrombospondin-1 (TSP-1) is a multidomain protein that has been implicated in cell adhesion, motility, and growth.
11067851	4	9	theme	alpha-mannosyl	520:533	arg1	residue					535:541	an alpha-mannosyl residue	517:541	an alpha-mannosyl residue	517:541	This modification involves the attachment of an alpha-mannosyl residue to the C-2 atom of the first tryptophan.
11067851	8	10	link	O-linked	1123:1130	arg1	disaccharide					1132:1143	the O-linked disaccharide	1119:1143	the O-linked disaccharide Glc-Fuc-O-Ser/Thr	1119:1161	By using a novel mass spectrometric approach, it was found that Ser-377, Thr-432, and Thr-489 in the motif CSX(S/T)CG carry the O-linked disaccharide Glc-Fuc-O-Ser/Thr.
11067851	5	11	theme	platelet	602:609	arg1	TSP-1					611:615	human platelet TSP-1	596:615	human platelet TSP-1	596:615	Analysis of human platelet TSP-1 revealed that Trp-368, -420, -423, and -480 are C-mannosylated.
11067851	10	12	theme	TSP-1	1431:1435	arg1	interaction					1416:1426	the interaction	1412:1426	the interaction of TSP-1 with glycosaminoglycans or other cellular receptors	1412:1487	Both C- and O-glycosylations take place on residues that have been implicated in the interaction of TSP-1 with glycosaminoglycans or other cellular receptors.
11067851	2	13	theme	type	259:262	arg1	TSRs					275:278	TSRs	275:278	TSRs	275:278	Some of these functions have been localized to the three thrombospondin type 1 repeats (TSRs), modules of approximately 60 amino acids in length with conserved Cys and Trp residues.
11067851	2	13	theme	type	259:262	arg1	modules					282:288	modules	282:288	modules of approximately 60 amino acids	282:320	Some of these functions have been localized to the three thrombospondin type 1 repeats (TSRs), modules of approximately 60 amino acids in length with conserved Cys and Trp residues.
11067851	2	13	theme	type	259:262	arg1	repeats					266:272	the three thrombospondin type 1 repeats	234:272	the three thrombospondin type 1 repeats (TSRs)	234:279	Some of these functions have been localized to the three thrombospondin type 1 repeats (TSRs), modules of approximately 60 amino acids in length with conserved Cys and Trp residues.
11067851	6	14	theme	TSR	749:751	arg1	modules					753:759	recombinant, baculovirally expressed TSR modules	712:759	recombinant, baculovirally expressed TSR modules from Sf9 and "High Five" cells, contradictory to earlier reports that such cells do not carry out this reaction	712:871	Mannosylation also occurred in recombinant, baculovirally expressed TSR modules from Sf9 and "High Five" cells, contradictory to earlier reports that such cells do not carry out this reaction.
11067851	4	15	attach	attachment	503:512	arg1	atom					554:557	the C-2 atom	546:557	the C-2 atom of the first tryptophan	546:581	This modification involves the attachment of an alpha-mannosyl residue to the C-2 atom of the first tryptophan.
11067851	4	15	attach	attachment	503:512	arg2	residue					535:541	an alpha-mannosyl residue	517:541	an alpha-mannosyl residue	517:541	This modification involves the attachment of an alpha-mannosyl residue to the C-2 atom of the first tryptophan.
11067851	6	16	dep	recombinant	712:722	arg1	expressed					739:747	expressed	739:747	expressed	739:747	Mannosylation also occurred in recombinant, baculovirally expressed TSR modules from Sf9 and "High Five" cells, contradictory to earlier reports that such cells do not carry out this reaction.
11067851	6	17	theme	earlier	810:816	arg1	reports					818:824	earlier reports	810:824	earlier reports that such cells do not carry out this reaction	810:871	Mannosylation also occurred in recombinant, baculovirally expressed TSR modules from Sf9 and "High Five" cells, contradictory to earlier reports that such cells do not carry out this reaction.
11067851	7	18	theme	glycosylation	980:992	arg1	form					964:967	a second form	955:967	a second form of unusual glycosylation	955:992	In the course of these studies it was appreciated that the TSRs in TSP-1 undergo a second form of unusual glycosylation.
11067851	2	19	theme	thrombospondin	244:257	arg1	TSRs					275:278	TSRs	275:278	TSRs	275:278	Some of these functions have been localized to the three thrombospondin type 1 repeats (TSRs), modules of approximately 60 amino acids in length with conserved Cys and Trp residues.
11067851	2	19	theme	thrombospondin	244:257	arg1	modules					282:288	modules	282:288	modules of approximately 60 amino acids	282:320	Some of these functions have been localized to the three thrombospondin type 1 repeats (TSRs), modules of approximately 60 amino acids in length with conserved Cys and Trp residues.
11067851	2	19	theme	thrombospondin	244:257	arg1	repeats					266:272	the three thrombospondin type 1 repeats	234:272	the three thrombospondin type 1 repeats (TSRs)	234:279	Some of these functions have been localized to the three thrombospondin type 1 repeats (TSRs), modules of approximately 60 amino acids in length with conserved Cys and Trp residues.
11067851	9	20	theme	growth	1303:1308	arg1	modules					1322:1328	epidermal growth factor-like modules	1293:1328	epidermal growth factor-like modules	1293:1328	This is the first protein in which such a disaccharide has been identified, although protein O-fucosylation is well described in epidermal growth factor-like modules.
11067851	8	21	theme	CSX	1102:1104	arg1	CG					1110:1111	the motif CSX(S/T)CG	1092:1111	the motif CSX(S/T)CG	1092:1111	By using a novel mass spectrometric approach, it was found that Ser-377, Thr-432, and Thr-489 in the motif CSX(S/T)CG carry the O-linked disaccharide Glc-Fuc-O-Ser/Thr.
11067851	8	22	from	Thr-489	1081:1087	arg1	CG					1110:1111	the motif CSX(S/T)CG	1092:1111	the motif CSX(S/T)CG	1092:1111	By using a novel mass spectrometric approach, it was found that Ser-377, Thr-432, and Thr-489 in the motif CSX(S/T)CG carry the O-linked disaccharide Glc-Fuc-O-Ser/Thr.
11067851	7	23	from	TSRs	933:936	arg1	TSP-1					941:945	TSP-1	941:945	TSP-1	941:945	In the course of these studies it was appreciated that the TSRs in TSP-1 undergo a second form of unusual glycosylation.
11067851	2	24	theme	conserved	337:345	arg1	Cys					347:349	conserved Cys and Trp residues	337:366	Cys	347:349	Some of these functions have been localized to the three thrombospondin type 1 repeats (TSRs), modules of approximately 60 amino acids in length with conserved Cys and Trp residues.
11067851	10	25	theme	cellular	1470:1477	arg1	receptors					1479:1487	other cellular receptors	1464:1487	other cellular receptors	1464:1487	Both C- and O-glycosylations take place on residues that have been implicated in the interaction of TSP-1 with glycosaminoglycans or other cellular receptors.
11067851	6	26	theme	contradictory	793:805	arg1	cells					786:790	Sf9 and "High Five" cells	766:790	cells	786:790	Mannosylation also occurred in recombinant, baculovirally expressed TSR modules from Sf9 and "High Five" cells, contradictory to earlier reports that such cells do not carry out this reaction.
11067851	10	27	with	interaction	1416:1426	arg1	glycosaminoglycans					1442:1459	glycosaminoglycans	1442:1459	glycosaminoglycans	1442:1459	Both C- and O-glycosylations take place on residues that have been implicated in the interaction of TSP-1 with glycosaminoglycans or other cellular receptors.
11067851	10	27	with	interaction	1416:1426	arg1	receptors					1479:1487	other cellular receptors	1464:1487	other cellular receptors	1464:1487	Both C- and O-glycosylations take place on residues that have been implicated in the interaction of TSP-1 with glycosaminoglycans or other cellular receptors.
11067851	8	28	theme	S/T	1106:1108	arg1	CG					1110:1111	the motif CSX(S/T)CG	1092:1111	the motif CSX(S/T)CG	1092:1111	By using a novel mass spectrometric approach, it was found that Ser-377, Thr-432, and Thr-489 in the motif CSX(S/T)CG carry the O-linked disaccharide Glc-Fuc-O-Ser/Thr.
11067851	10	29	theme	other	1464:1468	arg1	receptors					1479:1487	other cellular receptors	1464:1487	other cellular receptors	1464:1487	Both C- and O-glycosylations take place on residues that have been implicated in the interaction of TSP-1 with glycosaminoglycans or other cellular receptors.
11067851	7	30	theme	unusual	972:978	arg1	glycosylation					980:992	unusual glycosylation	972:992	unusual glycosylation	972:992	In the course of these studies it was appreciated that the TSRs in TSP-1 undergo a second form of unusual glycosylation.
11067851	6	31	theme	recombinant	712:722	arg1	modules					753:759	recombinant, baculovirally expressed TSR modules	712:759	recombinant, baculovirally expressed TSR modules from Sf9 and "High Five" cells, contradictory to earlier reports that such cells do not carry out this reaction	712:871	Mannosylation also occurred in recombinant, baculovirally expressed TSR modules from Sf9 and "High Five" cells, contradictory to earlier reports that such cells do not carry out this reaction.
11067851	3	32	theme	Trp	373:375	arg1	residues					377:384	The Trp residues	369:384	The Trp residues	369:384	The Trp residues occur in WXXW patterns, which are the recognition motifs for protein C-mannosylation.
11067851	7	33	theme	second	957:962	arg1	form					964:967	a second form	955:967	a second form of unusual glycosylation	955:992	In the course of these studies it was appreciated that the TSRs in TSP-1 undergo a second form of unusual glycosylation.
11067851	5	34	gly	C-mannosylated	665:678	arg1	Trp-368					631:637	Trp-368	631:637	Trp-368	631:637	Analysis of human platelet TSP-1 revealed that Trp-368, -420, -423, and -480 are C-mannosylated.
11067851	5	34	gly	C-mannosylated	665:678	arg1	-423					646:649	-423	646:649	-423	646:649	Analysis of human platelet TSP-1 revealed that Trp-368, -420, -423, and -480 are C-mannosylated.
11067851	5	34	gly	C-mannosylated	665:678	arg1	-480					656:659	-480	656:659	-480	656:659	Analysis of human platelet TSP-1 revealed that Trp-368, -420, -423, and -480 are C-mannosylated.
11067851	5	34	gly	C-mannosylated	665:678	arg1	-420					640:643	-420	640:643	-420	640:643	Analysis of human platelet TSP-1 revealed that Trp-368, -420, -423, and -480 are C-mannosylated.
11067851	4	35	theme	tryptophan	572:581	arg1	atom					554:557	the C-2 atom	546:557	the C-2 atom of the first tryptophan	546:581	This modification involves the attachment of an alpha-mannosyl residue to the C-2 atom of the first tryptophan.
11067851	6	36	from	cells	786:790	arg1	modules					753:759	recombinant, baculovirally expressed TSR modules	712:759	recombinant, baculovirally expressed TSR modules from Sf9 and "High Five" cells, contradictory to earlier reports that such cells do not carry out this reaction	712:871	Mannosylation also occurred in recombinant, baculovirally expressed TSR modules from Sf9 and "High Five" cells, contradictory to earlier reports that such cells do not carry out this reaction.
11067851	8	37	from	Ser-377	1059:1065	arg1	CG					1110:1111	the motif CSX(S/T)CG	1092:1111	the motif CSX(S/T)CG	1092:1111	By using a novel mass spectrometric approach, it was found that Ser-377, Thr-432, and Thr-489 in the motif CSX(S/T)CG carry the O-linked disaccharide Glc-Fuc-O-Ser/Thr.
11067851	4	38	theme	first	566:570	arg1	tryptophan					572:581	the first tryptophan	562:581	the first tryptophan	562:581	This modification involves the attachment of an alpha-mannosyl residue to the C-2 atom of the first tryptophan.
11067851	0	39	theme	thrombospondin	42:55	arg1	module					64:69	the thrombospondin type 1 module	38:69	the thrombospondin type 1 module	38:69	C-mannosylation and O-fucosylation of the thrombospondin type 1 module.
11067851	8	40	theme	O-linked	1123:1130	arg1	disaccharide					1132:1143	the O-linked disaccharide	1119:1143	the O-linked disaccharide Glc-Fuc-O-Ser/Thr	1119:1161	By using a novel mass spectrometric approach, it was found that Ser-377, Thr-432, and Thr-489 in the motif CSX(S/T)CG carry the O-linked disaccharide Glc-Fuc-O-Ser/Thr.
11067851	0	41	gly	C-mannosylation	0:14	arg1	module					64:69	the thrombospondin type 1 module	38:69	the thrombospondin type 1 module	38:69	C-mannosylation and O-fucosylation of the thrombospondin type 1 module.
11067851	9	42	theme	factor-like	1310:1320	arg1	modules					1322:1328	epidermal growth factor-like modules	1293:1328	epidermal growth factor-like modules	1293:1328	This is the first protein in which such a disaccharide has been identified, although protein O-fucosylation is well described in epidermal growth factor-like modules.
11067851	2	43	theme	Trp	355:357	arg1	residues					359:366	conserved Cys and Trp residues	337:366	residues	359:366	Some of these functions have been localized to the three thrombospondin type 1 repeats (TSRs), modules of approximately 60 amino acids in length with conserved Cys and Trp residues.
11067851	6	44	theme	"	784:784	arg1	cells					786:790	Sf9 and "High Five" cells	766:790	cells	786:790	Mannosylation also occurred in recombinant, baculovirally expressed TSR modules from Sf9 and "High Five" cells, contradictory to earlier reports that such cells do not carry out this reaction.
11067851	3	45	theme	WXXW	395:398	arg1	patterns					400:407	WXXW patterns	395:407	WXXW patterns	395:407	The Trp residues occur in WXXW patterns, which are the recognition motifs for protein C-mannosylation.
11067851	3	45	theme	WXXW	395:398	arg1	motifs					436:441	the recognition motifs	420:441	the recognition motifs for protein C-mannosylation	420:469	The Trp residues occur in WXXW patterns, which are the recognition motifs for protein C-mannosylation.
11067851	9	46	theme	epidermal	1293:1301	arg1	modules					1322:1328	epidermal growth factor-like modules	1293:1328	epidermal growth factor-like modules	1293:1328	This is the first protein in which such a disaccharide has been identified, although protein O-fucosylation is well described in epidermal growth factor-like modules.
11067851	8	47	theme	mass	1012:1015	arg1	approach					1031:1038	a novel mass spectrometric approach	1004:1038	a novel mass spectrometric approach	1004:1038	By using a novel mass spectrometric approach, it was found that Ser-377, Thr-432, and Thr-489 in the motif CSX(S/T)CG carry the O-linked disaccharide Glc-Fuc-O-Ser/Thr.
11067851	0	48	gly	O-fucosylation	20:33	arg1	module					64:69	the thrombospondin type 1 module	38:69	the thrombospondin type 1 module	38:69	C-mannosylation and O-fucosylation of the thrombospondin type 1 module.
11067851	1	49	theme	multidomain	102:112	arg1	Thrombospondin-1					72:87	Thrombospondin-1	72:87	Thrombospondin-1 (TSP-1)	72:95	Thrombospondin-1 (TSP-1) is a multidomain protein that has been implicated in cell adhesion, motility, and growth.
11067851	1	49	theme	multidomain	102:112	arg1	protein					114:120	a multidomain protein	100:120	a multidomain protein that has been implicated in cell adhesion, motility, and growth	100:184	Thrombospondin-1 (TSP-1) is a multidomain protein that has been implicated in cell adhesion, motility, and growth.
11067851	0	50	theme	type	57:60	arg1	module					64:69	the thrombospondin type 1 module	38:69	the thrombospondin type 1 module	38:69	C-mannosylation and O-fucosylation of the thrombospondin type 1 module.
11067851	6	51	theme	High	775:778	arg1	cells					786:790	Sf9 and "High Five" cells	766:790	cells	786:790	Mannosylation also occurred in recombinant, baculovirally expressed TSR modules from Sf9 and "High Five" cells, contradictory to earlier reports that such cells do not carry out this reaction.
11067851	3	52	theme	recognition	424:434	arg1	patterns					400:407	WXXW patterns	395:407	WXXW patterns	395:407	The Trp residues occur in WXXW patterns, which are the recognition motifs for protein C-mannosylation.
11067851	3	52	theme	recognition	424:434	arg1	motifs					436:441	the recognition motifs	420:441	the recognition motifs for protein C-mannosylation	420:469	The Trp residues occur in WXXW patterns, which are the recognition motifs for protein C-mannosylation.
11067851	8	53	theme	novel	1006:1010	arg1	approach					1031:1038	a novel mass spectrometric approach	1004:1038	a novel mass spectrometric approach	1004:1038	By using a novel mass spectrometric approach, it was found that Ser-377, Thr-432, and Thr-489 in the motif CSX(S/T)CG carry the O-linked disaccharide Glc-Fuc-O-Ser/Thr.
11067851	6	54	contain	carry	849:853	arg2	reports					818:824	earlier reports	810:824	earlier reports that such cells do not carry out this reaction	810:871	Mannosylation also occurred in recombinant, baculovirally expressed TSR modules from Sf9 and "High Five" cells, contradictory to earlier reports that such cells do not carry out this reaction.
11067851	6	54	contain	carry	849:853	arg1	cells					836:840	such cells	831:840	such cells	831:840	Mannosylation also occurred in recombinant, baculovirally expressed TSR modules from Sf9 and "High Five" cells, contradictory to earlier reports that such cells do not carry out this reaction.
11067851	6	54	contain	carry	849:853	arg2	reaction					864:871	this reaction	859:871	this reaction	859:871	Mannosylation also occurred in recombinant, baculovirally expressed TSR modules from Sf9 and "High Five" cells, contradictory to earlier reports that such cells do not carry out this reaction.
11067851	8	55	theme	Glc-Fuc-O-Ser/Thr	1145:1161	arg1	disaccharide					1132:1143	the O-linked disaccharide	1119:1143	the O-linked disaccharide Glc-Fuc-O-Ser/Thr	1119:1161	By using a novel mass spectrometric approach, it was found that Ser-377, Thr-432, and Thr-489 in the motif CSX(S/T)CG carry the O-linked disaccharide Glc-Fuc-O-Ser/Thr.
11067851	4	56	theme	C-2	550:552	arg1	atom					554:557	the C-2 atom	546:557	the C-2 atom of the first tryptophan	546:581	This modification involves the attachment of an alpha-mannosyl residue to the C-2 atom of the first tryptophan.
11067851	8	57	theme	spectrometric	1017:1029	arg1	approach					1031:1038	a novel mass spectrometric approach	1004:1038	a novel mass spectrometric approach	1004:1038	By using a novel mass spectrometric approach, it was found that Ser-377, Thr-432, and Thr-489 in the motif CSX(S/T)CG carry the O-linked disaccharide Glc-Fuc-O-Ser/Thr.
11067851	6	58	theme	Sf9	766:768	arg1	cells					786:790	Sf9 and "High Five" cells	766:790	cells	786:790	Mannosylation also occurred in recombinant, baculovirally expressed TSR modules from Sf9 and "High Five" cells, contradictory to earlier reports that such cells do not carry out this reaction.
11067851	7	59	theme	studies	897:903	arg1	course					881:886	the course	877:886	the course of these studies	877:903	In the course of these studies it was appreciated that the TSRs in TSP-1 undergo a second form of unusual glycosylation.
11067851	3	60	theme	protein	447:453	arg1	C-mannosylation					455:469	protein C-mannosylation	447:469	protein C-mannosylation	447:469	The Trp residues occur in WXXW patterns, which are the recognition motifs for protein C-mannosylation.
11067851	8	61	theme	motif	1096:1100	arg1	CG					1110:1111	the motif CSX(S/T)CG	1092:1111	the motif CSX(S/T)CG	1092:1111	By using a novel mass spectrometric approach, it was found that Ser-377, Thr-432, and Thr-489 in the motif CSX(S/T)CG carry the O-linked disaccharide Glc-Fuc-O-Ser/Thr.
11067851	5	62	theme	TSP-1	611:615	arg1	Analysis					584:591	Analysis	584:591	Analysis of human platelet TSP-1	584:615	Analysis of human platelet TSP-1 revealed that Trp-368, -420, -423, and -480 are C-mannosylated.
11067851	0	63	theme	module	64:69	arg1	O-fucosylation					20:33	O-fucosylation	20:33	O-fucosylation	20:33	C-mannosylation and O-fucosylation of the thrombospondin type 1 module.
11067851	0	63	theme	module	64:69	arg1	C-mannosylation					0:14	C-mannosylation	0:14	C-mannosylation	0:14	C-mannosylation and O-fucosylation of the thrombospondin type 1 module.
11067851	9	64	gly	O-fucosylation	1257:1270	arg1	modules					1322:1328	epidermal growth factor-like modules	1293:1328	epidermal growth factor-like modules	1293:1328	This is the first protein in which such a disaccharide has been identified, although protein O-fucosylation is well described in epidermal growth factor-like modules.
11067851	2	65	theme	acids	316:320	arg1	modules					282:288	modules	282:288	modules of approximately 60 amino acids	282:320	Some of these functions have been localized to the three thrombospondin type 1 repeats (TSRs), modules of approximately 60 amino acids in length with conserved Cys and Trp residues.
11067851	2	65	theme	acids	316:320	arg1	repeats					266:272	the three thrombospondin type 1 repeats	234:272	the three thrombospondin type 1 repeats (TSRs)	234:279	Some of these functions have been localized to the three thrombospondin type 1 repeats (TSRs), modules of approximately 60 amino acids in length with conserved Cys and Trp residues.
11067851	9	66	theme	protein	1249:1255	arg1	O-fucosylation					1257:1270	protein O-fucosylation	1249:1270	protein O-fucosylation	1249:1270	This is the first protein in which such a disaccharide has been identified, although protein O-fucosylation is well described in epidermal growth factor-like modules.
11067851	2	67	located	localized	221:229	arg2	Some					187:190	Some	187:190	Some	187:190	Some of these functions have been localized to the three thrombospondin type 1 repeats (TSRs), modules of approximately 60 amino acids in length with conserved Cys and Trp residues.
11067851	2	67	located	localized	221:229	arg1	length					325:330	length	325:330	length with conserved Cys and Trp residues	325:366	Some of these functions have been localized to the three thrombospondin type 1 repeats (TSRs), modules of approximately 60 amino acids in length with conserved Cys and Trp residues.
11067851	2	67	located	localized	221:229	arg2	functions					201:209	these functions	195:209	these functions	195:209	Some of these functions have been localized to the three thrombospondin type 1 repeats (TSRs), modules of approximately 60 amino acids in length with conserved Cys and Trp residues.
1872845	6	0	from	chains	963:968	arg1	oligosaccharides					988:1003	its Asn-linked oligosaccharides	973:1003	its Asn-linked oligosaccharides	973:1003	Our results indicate that vWF itself contains UEA-I reactive sugar chains in its Asn-linked oligosaccharides.
1872845	6	1	theme	sugar	957:961	arg1	chains					963:968	UEA-I reactive sugar chains	942:968	UEA-I reactive sugar chains in its Asn-linked oligosaccharides	942:1003	Our results indicate that vWF itself contains UEA-I reactive sugar chains in its Asn-linked oligosaccharides.
1872845	1	2	theme	polyvinylidene	152:165	arg1	membrane					178:185	a polyvinylidene difluoride membrane	150:185	a polyvinylidene difluoride membrane	150:185	Human von Willebrand factor (vWF) immobilized on a polyvinylidene difluoride membrane was subjected to binding assay with a series of horseradish peroxidase-conjugated lectins.
1872845	1	3	theme	lectins	269:275	arg1	series					225:230	a series	223:230	a series of horseradish peroxidase-conjugated lectins	223:275	Human von Willebrand factor (vWF) immobilized on a polyvinylidene difluoride membrane was subjected to binding assay with a series of horseradish peroxidase-conjugated lectins.
1872845	6	4	theme	reactive	948:955	arg1	chains					963:968	UEA-I reactive sugar chains	942:968	UEA-I reactive sugar chains in its Asn-linked oligosaccharides	942:1003	Our results indicate that vWF itself contains UEA-I reactive sugar chains in its Asn-linked oligosaccharides.
1872845	1	5	theme	difluoride	167:176	arg1	membrane					178:185	a polyvinylidene difluoride membrane	150:185	a polyvinylidene difluoride membrane	150:185	Human von Willebrand factor (vWF) immobilized on a polyvinylidene difluoride membrane was subjected to binding assay with a series of horseradish peroxidase-conjugated lectins.
1872845	6	6	theme	UEA-I	942:946	arg1	chains					963:968	UEA-I reactive sugar chains	942:968	UEA-I reactive sugar chains in its Asn-linked oligosaccharides	942:1003	Our results indicate that vWF itself contains UEA-I reactive sugar chains in its Asn-linked oligosaccharides.
1872845	2	7	theme	concanavalin	308:319	arg1	agglutinin					368:377	wheat germ agglutinin	357:377	wheat germ agglutinin	357:377	The protein was reactive with concanavalin A, Ricinus communis agglutinin 120, wheat germ agglutinin and Ulex europaeus agglutinin I (UEA-I) but not with peanut agglutinin before sialidase treatment.
1872845	2	7	theme	concanavalin	308:319	arg1	europaeus					388:396	Ulex europaeus	383:396	Ulex europaeus	383:396	The protein was reactive with concanavalin A, Ricinus communis agglutinin 120, wheat germ agglutinin and Ulex europaeus agglutinin I (UEA-I) but not with peanut agglutinin before sialidase treatment.
1872845	2	7	theme	concanavalin	308:319	arg1	agglutinin					341:350	Ricinus communis agglutinin 120	324:354	Ricinus communis agglutinin 120	324:354	The protein was reactive with concanavalin A, Ricinus communis agglutinin 120, wheat germ agglutinin and Ulex europaeus agglutinin I (UEA-I) but not with peanut agglutinin before sialidase treatment.
1872845	2	7	theme	concanavalin	308:319	arg1	A					321:321	concanavalin A	308:321	concanavalin A	308:321	The protein was reactive with concanavalin A, Ricinus communis agglutinin 120, wheat germ agglutinin and Ulex europaeus agglutinin I (UEA-I) but not with peanut agglutinin before sialidase treatment.
1872845	2	8	theme	communis	332:339	arg1	agglutinin					341:350	Ricinus communis agglutinin 120	324:354	Ricinus communis agglutinin 120	324:354	The protein was reactive with concanavalin A, Ricinus communis agglutinin 120, wheat germ agglutinin and Ulex europaeus agglutinin I (UEA-I) but not with peanut agglutinin before sialidase treatment.
1872845	2	8	theme	communis	332:339	arg1	A					321:321	concanavalin A	308:321	concanavalin A	308:321	The protein was reactive with concanavalin A, Ricinus communis agglutinin 120, wheat germ agglutinin and Ulex europaeus agglutinin I (UEA-I) but not with peanut agglutinin before sialidase treatment.
1872845	2	8	theme	communis	332:339	arg1	UEA-I					412:416	UEA-I	412:416	UEA-I	412:416	The protein was reactive with concanavalin A, Ricinus communis agglutinin 120, wheat germ agglutinin and Ulex europaeus agglutinin I (UEA-I) but not with peanut agglutinin before sialidase treatment.
1872845	4	9	with	reactivity	585:594	arg1	UEA-I					601:605	UEA-I	601:605	UEA-I	601:605	The reactivity with UEA-I was greatly decreased after digestion of the protein with either alpha-L-fucosidase or peptide-N-glycosidase F, but no significant decrease was observed after mild alkaline treatment or delipidation.
1872845	4	10	theme	significant	726:736	arg1	decrease					738:745	no significant decrease	723:745	no significant decrease	723:745	The reactivity with UEA-I was greatly decreased after digestion of the protein with either alpha-L-fucosidase or peptide-N-glycosidase F, but no significant decrease was observed after mild alkaline treatment or delipidation.
1872845	5	11	theme	human	871:875	arg1	cells					889:893	human endothelial cells	871:893	human endothelial cells	871:893	vWF and UEA-I have been independently used as a good marker for human endothelial cells.
1872845	4	12	theme	protein	652:658	arg1	digestion					635:643	digestion	635:643	digestion of the protein with either alpha-L-fucosidase or peptide-N-glycosidase F	635:716	The reactivity with UEA-I was greatly decreased after digestion of the protein with either alpha-L-fucosidase or peptide-N-glycosidase F, but no significant decrease was observed after mild alkaline treatment or delipidation.
1872845	4	13	theme	peptide-N-glycosidase	694:714	arg1	F					716:716	peptide-N-glycosidase F	694:716	peptide-N-glycosidase F	694:716	The reactivity with UEA-I was greatly decreased after digestion of the protein with either alpha-L-fucosidase or peptide-N-glycosidase F, but no significant decrease was observed after mild alkaline treatment or delipidation.
1872845	2	14	theme	sialidase	457:465	arg1	treatment					467:475	sialidase treatment	457:475	sialidase treatment	457:475	The protein was reactive with concanavalin A, Ricinus communis agglutinin 120, wheat germ agglutinin and Ulex europaeus agglutinin I (UEA-I) but not with peanut agglutinin before sialidase treatment.
1872845	3	15	with	consistent	502:511	arg1	structure					544:552	the major oligosaccharide structure	518:552	the major oligosaccharide structure reported except for UEA-I	518:578	These reactivities were consistent with the major oligosaccharide structure reported except for UEA-I.
1872845	1	16	theme	Human	101:105	arg1	vWF					130:132	vWF	130:132	vWF	130:132	Human von Willebrand factor (vWF) immobilized on a polyvinylidene difluoride membrane was subjected to binding assay with a series of horseradish peroxidase-conjugated lectins.
1872845	1	16	theme	Human	101:105	arg1	factor					122:127	Human von Willebrand factor	101:127	Human von Willebrand factor (vWF) immobilized on a polyvinylidene difluoride membrane	101:185	Human von Willebrand factor (vWF) immobilized on a polyvinylidene difluoride membrane was subjected to binding assay with a series of horseradish peroxidase-conjugated lectins.
1872845	0	17	theme	Carbohydrate	0:11	arg1	analysis					13:20	Carbohydrate analysis	0:20	Carbohydrate analysis of human von Willebrand factor with horseradish peroxidase-conjugated lectins.	0:99	Carbohydrate analysis of human von Willebrand factor with horseradish peroxidase-conjugated lectins.
1872845	1	18	theme	von	107:109	arg1	vWF					130:132	vWF	130:132	vWF	130:132	Human von Willebrand factor (vWF) immobilized on a polyvinylidene difluoride membrane was subjected to binding assay with a series of horseradish peroxidase-conjugated lectins.
1872845	1	18	theme	von	107:109	arg1	factor					122:127	Human von Willebrand factor	101:127	Human von Willebrand factor (vWF) immobilized on a polyvinylidene difluoride membrane	101:185	Human von Willebrand factor (vWF) immobilized on a polyvinylidene difluoride membrane was subjected to binding assay with a series of horseradish peroxidase-conjugated lectins.
1872845	0	19	theme	human	25:29	arg1	factor					46:51	human von Willebrand factor	25:51	human von Willebrand factor	25:51	Carbohydrate analysis of human von Willebrand factor with horseradish peroxidase-conjugated lectins.
1872845	4	20	theme	alkaline	771:778	arg1	treatment					780:788	mild alkaline treatment	766:788	mild alkaline treatment	766:788	The reactivity with UEA-I was greatly decreased after digestion of the protein with either alpha-L-fucosidase or peptide-N-glycosidase F, but no significant decrease was observed after mild alkaline treatment or delipidation.
1872845	5	21	used	used	845:848	arg2	UEA-I					815:819	UEA-I	815:819	UEA-I	815:819	vWF and UEA-I have been independently used as a good marker for human endothelial cells.
1872845	5	21	used	used	845:848	arg2	marker					860:865	a good marker	853:865	a good marker for human endothelial cells	853:893	vWF and UEA-I have been independently used as a good marker for human endothelial cells.
1872845	5	21	used	used	845:848	arg2	vWF					807:809	vWF	807:809	vWF	807:809	vWF and UEA-I have been independently used as a good marker for human endothelial cells.
1872845	1	22	theme	Willebrand	111:120	arg1	vWF					130:132	vWF	130:132	vWF	130:132	Human von Willebrand factor (vWF) immobilized on a polyvinylidene difluoride membrane was subjected to binding assay with a series of horseradish peroxidase-conjugated lectins.
1872845	1	22	theme	Willebrand	111:120	arg1	factor					122:127	Human von Willebrand factor	101:127	Human von Willebrand factor (vWF) immobilized on a polyvinylidene difluoride membrane	101:185	Human von Willebrand factor (vWF) immobilized on a polyvinylidene difluoride membrane was subjected to binding assay with a series of horseradish peroxidase-conjugated lectins.
1872845	1	23	theme	binding	204:210	arg1	assay					212:216	binding assay	204:216	binding assay	204:216	Human von Willebrand factor (vWF) immobilized on a polyvinylidene difluoride membrane was subjected to binding assay with a series of horseradish peroxidase-conjugated lectins.
1872845	2	24	theme	Ricinus	324:330	arg1	agglutinin					341:350	Ricinus communis agglutinin 120	324:354	Ricinus communis agglutinin 120	324:354	The protein was reactive with concanavalin A, Ricinus communis agglutinin 120, wheat germ agglutinin and Ulex europaeus agglutinin I (UEA-I) but not with peanut agglutinin before sialidase treatment.
1872845	2	24	theme	Ricinus	324:330	arg1	A					321:321	concanavalin A	308:321	concanavalin A	308:321	The protein was reactive with concanavalin A, Ricinus communis agglutinin 120, wheat germ agglutinin and Ulex europaeus agglutinin I (UEA-I) but not with peanut agglutinin before sialidase treatment.
1872845	2	24	theme	Ricinus	324:330	arg1	UEA-I					412:416	UEA-I	412:416	UEA-I	412:416	The protein was reactive with concanavalin A, Ricinus communis agglutinin 120, wheat germ agglutinin and Ulex europaeus agglutinin I (UEA-I) but not with peanut agglutinin before sialidase treatment.
1872845	2	25	theme	germ	363:366	arg1	agglutinin					368:377	wheat germ agglutinin	357:377	wheat germ agglutinin	357:377	The protein was reactive with concanavalin A, Ricinus communis agglutinin 120, wheat germ agglutinin and Ulex europaeus agglutinin I (UEA-I) but not with peanut agglutinin before sialidase treatment.
1872845	2	25	theme	germ	363:366	arg1	A					321:321	concanavalin A	308:321	concanavalin A	308:321	The protein was reactive with concanavalin A, Ricinus communis agglutinin 120, wheat germ agglutinin and Ulex europaeus agglutinin I (UEA-I) but not with peanut agglutinin before sialidase treatment.
1872845	3	26	theme	oligosaccharide	528:542	arg1	structure					544:552	the major oligosaccharide structure	518:552	the major oligosaccharide structure reported except for UEA-I	518:578	These reactivities were consistent with the major oligosaccharide structure reported except for UEA-I.
1872845	0	27	theme	Willebrand	35:44	arg1	factor					46:51	human von Willebrand factor	25:51	human von Willebrand factor	25:51	Carbohydrate analysis of human von Willebrand factor with horseradish peroxidase-conjugated lectins.
1872845	2	28	dep	agglutinin	341:350	arg1	agglutinin					398:407	agglutinin I	398:409	agglutinin I	398:409	The protein was reactive with concanavalin A, Ricinus communis agglutinin 120, wheat germ agglutinin and Ulex europaeus agglutinin I (UEA-I) but not with peanut agglutinin before sialidase treatment.
1872845	5	29	theme	endothelial	877:887	arg1	cells					889:893	human endothelial cells	871:893	human endothelial cells	871:893	vWF and UEA-I have been independently used as a good marker for human endothelial cells.
1872845	0	30	theme	von	31:33	arg1	factor					46:51	human von Willebrand factor	25:51	human von Willebrand factor	25:51	Carbohydrate analysis of human von Willebrand factor with horseradish peroxidase-conjugated lectins.
1872845	2	31	theme	peanut	432:437	arg1	agglutinin					439:448	peanut agglutinin	432:448	peanut agglutinin before sialidase treatment	432:475	The protein was reactive with concanavalin A, Ricinus communis agglutinin 120, wheat germ agglutinin and Ulex europaeus agglutinin I (UEA-I) but not with peanut agglutinin before sialidase treatment.
1872845	5	32	theme	good	855:858	arg1	vWF					807:809	vWF	807:809	vWF	807:809	vWF and UEA-I have been independently used as a good marker for human endothelial cells.
1872845	5	32	theme	good	855:858	arg1	UEA-I					815:819	UEA-I	815:819	UEA-I	815:819	vWF and UEA-I have been independently used as a good marker for human endothelial cells.
1872845	5	32	theme	good	855:858	arg1	marker					860:865	a good marker	853:865	a good marker for human endothelial cells	853:893	vWF and UEA-I have been independently used as a good marker for human endothelial cells.
1872845	6	33	theme	Asn-linked	977:986	arg1	oligosaccharides					988:1003	its Asn-linked oligosaccharides	973:1003	its Asn-linked oligosaccharides	973:1003	Our results indicate that vWF itself contains UEA-I reactive sugar chains in its Asn-linked oligosaccharides.
1872845	4	34	with	digestion	635:643	arg1	alpha-L-fucosidase					672:689	alpha-L-fucosidase	672:689	alpha-L-fucosidase	672:689	The reactivity with UEA-I was greatly decreased after digestion of the protein with either alpha-L-fucosidase or peptide-N-glycosidase F, but no significant decrease was observed after mild alkaline treatment or delipidation.
1872845	4	34	with	digestion	635:643	arg1	F					716:716	peptide-N-glycosidase F	694:716	peptide-N-glycosidase F	694:716	The reactivity with UEA-I was greatly decreased after digestion of the protein with either alpha-L-fucosidase or peptide-N-glycosidase F, but no significant decrease was observed after mild alkaline treatment or delipidation.
1872845	2	35	theme	wheat	357:361	arg1	agglutinin					368:377	wheat germ agglutinin	357:377	wheat germ agglutinin	357:377	The protein was reactive with concanavalin A, Ricinus communis agglutinin 120, wheat germ agglutinin and Ulex europaeus agglutinin I (UEA-I) but not with peanut agglutinin before sialidase treatment.
1872845	2	35	theme	wheat	357:361	arg1	A					321:321	concanavalin A	308:321	concanavalin A	308:321	The protein was reactive with concanavalin A, Ricinus communis agglutinin 120, wheat germ agglutinin and Ulex europaeus agglutinin I (UEA-I) but not with peanut agglutinin before sialidase treatment.
1872845	0	36	theme	factor	46:51	arg1	analysis					13:20	Carbohydrate analysis	0:20	Carbohydrate analysis of human von Willebrand factor with horseradish peroxidase-conjugated lectins.	0:99	Carbohydrate analysis of human von Willebrand factor with horseradish peroxidase-conjugated lectins.
1872845	0	37	with	analysis	13:20	arg1	lectins					92:98	horseradish peroxidase-conjugated lectins	58:98	horseradish peroxidase-conjugated lectins	58:98	Carbohydrate analysis of human von Willebrand factor with horseradish peroxidase-conjugated lectins.
1872845	3	38	theme	major	522:526	arg1	structure					544:552	the major oligosaccharide structure	518:552	the major oligosaccharide structure reported except for UEA-I	518:578	These reactivities were consistent with the major oligosaccharide structure reported except for UEA-I.
1872845	4	39	theme	mild	766:769	arg1	treatment					780:788	mild alkaline treatment	766:788	mild alkaline treatment	766:788	The reactivity with UEA-I was greatly decreased after digestion of the protein with either alpha-L-fucosidase or peptide-N-glycosidase F, but no significant decrease was observed after mild alkaline treatment or delipidation.
1872845	2	40	with	reactive	294:301	arg1	agglutinin					439:448	peanut agglutinin	432:448	peanut agglutinin before sialidase treatment	432:475	The protein was reactive with concanavalin A, Ricinus communis agglutinin 120, wheat germ agglutinin and Ulex europaeus agglutinin I (UEA-I) but not with peanut agglutinin before sialidase treatment.
1872845	2	40	with	reactive	294:301	arg1	agglutinin					368:377	wheat germ agglutinin	357:377	wheat germ agglutinin	357:377	The protein was reactive with concanavalin A, Ricinus communis agglutinin 120, wheat germ agglutinin and Ulex europaeus agglutinin I (UEA-I) but not with peanut agglutinin before sialidase treatment.
1872845	2	40	with	reactive	294:301	arg1	europaeus					388:396	Ulex europaeus	383:396	Ulex europaeus	383:396	The protein was reactive with concanavalin A, Ricinus communis agglutinin 120, wheat germ agglutinin and Ulex europaeus agglutinin I (UEA-I) but not with peanut agglutinin before sialidase treatment.
1872845	2	40	with	reactive	294:301	arg1	agglutinin					341:350	Ricinus communis agglutinin 120	324:354	Ricinus communis agglutinin 120	324:354	The protein was reactive with concanavalin A, Ricinus communis agglutinin 120, wheat germ agglutinin and Ulex europaeus agglutinin I (UEA-I) but not with peanut agglutinin before sialidase treatment.
1872845	2	40	with	reactive	294:301	arg1	A					321:321	concanavalin A	308:321	concanavalin A	308:321	The protein was reactive with concanavalin A, Ricinus communis agglutinin 120, wheat germ agglutinin and Ulex europaeus agglutinin I (UEA-I) but not with peanut agglutinin before sialidase treatment.
1872845	0	41	theme	peroxidase-conjugated	70:90	arg1	lectins					92:98	horseradish peroxidase-conjugated lectins	58:98	horseradish peroxidase-conjugated lectins	58:98	Carbohydrate analysis of human von Willebrand factor with horseradish peroxidase-conjugated lectins.
1872845	6	42	contain	contains	933:940	arg2	chains					963:968	UEA-I reactive sugar chains	942:968	UEA-I reactive sugar chains in its Asn-linked oligosaccharides	942:1003	Our results indicate that vWF itself contains UEA-I reactive sugar chains in its Asn-linked oligosaccharides.
1872845	6	42	contain	contains	933:940	arg1	vWF					922:924	vWF itself	922:931	vWF itself	922:931	Our results indicate that vWF itself contains UEA-I reactive sugar chains in its Asn-linked oligosaccharides.
1872845	2	43	theme	Ulex	383:386	arg1	europaeus					388:396	Ulex europaeus	383:396	Ulex europaeus	383:396	The protein was reactive with concanavalin A, Ricinus communis agglutinin 120, wheat germ agglutinin and Ulex europaeus agglutinin I (UEA-I) but not with peanut agglutinin before sialidase treatment.
1872845	2	43	theme	Ulex	383:386	arg1	A					321:321	concanavalin A	308:321	concanavalin A	308:321	The protein was reactive with concanavalin A, Ricinus communis agglutinin 120, wheat germ agglutinin and Ulex europaeus agglutinin I (UEA-I) but not with peanut agglutinin before sialidase treatment.
1872845	1	44	theme	horseradish	235:245	arg1	lectins					269:275	horseradish peroxidase-conjugated lectins	235:275	horseradish peroxidase-conjugated lectins	235:275	Human von Willebrand factor (vWF) immobilized on a polyvinylidene difluoride membrane was subjected to binding assay with a series of horseradish peroxidase-conjugated lectins.
1872845	0	45	theme	horseradish	58:68	arg1	lectins					92:98	horseradish peroxidase-conjugated lectins	58:98	horseradish peroxidase-conjugated lectins	58:98	Carbohydrate analysis of human von Willebrand factor with horseradish peroxidase-conjugated lectins.
1872845	6	46	link	Asn-linked	977:986	arg1	oligosaccharides					988:1003	its Asn-linked oligosaccharides	973:1003	its Asn-linked oligosaccharides	973:1003	Our results indicate that vWF itself contains UEA-I reactive sugar chains in its Asn-linked oligosaccharides.
1872845	1	47	theme	peroxidase-conjugated	247:267	arg1	lectins					269:275	horseradish peroxidase-conjugated lectins	235:275	horseradish peroxidase-conjugated lectins	235:275	Human von Willebrand factor (vWF) immobilized on a polyvinylidene difluoride membrane was subjected to binding assay with a series of horseradish peroxidase-conjugated lectins.
447737	4	0	theme	sugar	644:648	arg1	units					650:654	the various sugar units	632:654	the various sugar units	632:654	The positions of links between the various sugar units were studied by methylation analyses of: secretory component, periodate-oxidized and reduced secretory component, the fragment produced by base-borohydride treatment, and the pronase glycopeptide after treatment with specific glycosidases.
447737	0	1	theme	human	69:73	arg1	milk					75:78	human milk	69:78	human milk	69:78	Structure of the carbohydrate chain of free secretory component from human milk.
447737	5	2	attach	released	903:910	arg1	glycopeptide					921:932	the glycopeptide	917:932	the glycopeptide	917:932	Sugars released from the glycopeptide by various glycosidases were also quantitated.
447737	5	2	attach	released	903:910	arg2	Sugars					896:901	Sugars	896:901	Sugars released from the glycopeptide by various glycosidases	896:956	Sugars released from the glycopeptide by various glycosidases were also quantitated.
447737	3	3	gly	glycopeptide	361:372	arg2	glycopeptide					361:372	glycopeptide	361:372	glycopeptide	361:372	In the glycopeptide produced by pronase digestion, aspartic acid was the only amino acid present in molar quantities after amino acid analysis, which suggests that the carbohydrate moiety is linked to the polypeptide chain at asparagine residues.
447737	1	4	theme	%	142:142	arg1	carbohydrate					144:155	23.4% carbohydrate	138:155	23.4% carbohydrate	138:155	Secretory component from human milk was found to contain 23.4% carbohydrate, which includes galactose, mannose, fucose, glucosamine, and sialic acid.
447737	1	5	theme	sialic	218:223	arg1	acid					225:228	sialic acid	218:228	sialic acid	218:228	Secretory component from human milk was found to contain 23.4% carbohydrate, which includes galactose, mannose, fucose, glucosamine, and sialic acid.
447737	5	6	theme	various	937:943	arg1	glycosidases					945:956	various glycosidases	937:956	various glycosidases	937:956	Sugars released from the glycopeptide by various glycosidases were also quantitated.
447737	4	7	theme	pronase	831:837	arg1	analyses					684:691	methylation analyses	672:691	methylation analyses of: secretory component, periodate-oxidized and reduced secretory component, the fragment produced by base-borohydride treatment, and the pronase glycopeptide	672:850	The positions of links between the various sugar units were studied by methylation analyses of: secretory component, periodate-oxidized and reduced secretory component, the fragment produced by base-borohydride treatment, and the pronase glycopeptide after treatment with specific glycosidases.
447737	4	7	theme	pronase	831:837	arg1	glycopeptide					839:850	the pronase glycopeptide	827:850	the pronase glycopeptide	827:850	The positions of links between the various sugar units were studied by methylation analyses of: secretory component, periodate-oxidized and reduced secretory component, the fragment produced by base-borohydride treatment, and the pronase glycopeptide after treatment with specific glycosidases.
447737	3	8	from	quantities	460:469	arg1	present					443:449	present	443:449	present	443:449	In the glycopeptide produced by pronase digestion, aspartic acid was the only amino acid present in molar quantities after amino acid analysis, which suggests that the carbohydrate moiety is linked to the polypeptide chain at asparagine residues.
447737	4	9	theme	secretory	697:705	arg1	component					707:715	secretory component	697:715	secretory component	697:715	The positions of links between the various sugar units were studied by methylation analyses of: secretory component, periodate-oxidized and reduced secretory component, the fragment produced by base-borohydride treatment, and the pronase glycopeptide after treatment with specific glycosidases.
447737	4	9	theme	secretory	697:705	arg1	analyses					684:691	methylation analyses	672:691	methylation analyses of: secretory component, periodate-oxidized and reduced secretory component, the fragment produced by base-borohydride treatment, and the pronase glycopeptide	672:850	The positions of links between the various sugar units were studied by methylation analyses of: secretory component, periodate-oxidized and reduced secretory component, the fragment produced by base-borohydride treatment, and the pronase glycopeptide after treatment with specific glycosidases.
447737	6	10	theme	component	1094:1102	arg1	chain					1075:1079	the carbohydrate chain	1058:1079	the carbohydrate chain of secretory component	1058:1102	From the results of these studies a branched chain structure was assigned to the carbohydrate chain of secretory component.
447737	3	11	from	residues	591:598	arg1	chain					571:575	the polypeptide chain	555:575	the polypeptide chain at asparagine residues	555:598	In the glycopeptide produced by pronase digestion, aspartic acid was the only amino acid present in molar quantities after amino acid analysis, which suggests that the carbohydrate moiety is linked to the polypeptide chain at asparagine residues.
447737	4	12	theme	base-borohydride	795:810	arg1	treatment					812:820	base-borohydride treatment	795:820	base-borohydride treatment	795:820	The positions of links between the various sugar units were studied by methylation analyses of: secretory component, periodate-oxidized and reduced secretory component, the fragment produced by base-borohydride treatment, and the pronase glycopeptide after treatment with specific glycosidases.
447737	3	13	theme	amino	477:481	arg1	analysis					488:495	amino acid analysis	477:495	amino acid analysis	477:495	In the glycopeptide produced by pronase digestion, aspartic acid was the only amino acid present in molar quantities after amino acid analysis, which suggests that the carbohydrate moiety is linked to the polypeptide chain at asparagine residues.
447737	4	14	theme	links	618:622	arg1	positions					605:613	The positions	601:613	The positions of links between the various sugar units	601:654	The positions of links between the various sugar units were studied by methylation analyses of: secretory component, periodate-oxidized and reduced secretory component, the fragment produced by base-borohydride treatment, and the pronase glycopeptide after treatment with specific glycosidases.
447737	5	15	gly	glycopeptide	921:932	arg2	glycopeptide					921:932	the glycopeptide	917:932	the glycopeptide	917:932	Sugars released from the glycopeptide by various glycosidases were also quantitated.
447737	1	16	contain	contain	130:136	arg2	carbohydrate					144:155	23.4% carbohydrate	138:155	23.4% carbohydrate	138:155	Secretory component from human milk was found to contain 23.4% carbohydrate, which includes galactose, mannose, fucose, glucosamine, and sialic acid.
447737	1	16	contain	contain	130:136	arg1	component					91:99	Secretory component	81:99	Secretory component from human milk	81:115	Secretory component from human milk was found to contain 23.4% carbohydrate, which includes galactose, mannose, fucose, glucosamine, and sialic acid.
447737	2	17	theme	Secretory	231:239	arg1	component					241:249	Secretory component	231:249	Secretory component	231:249	Secretory component could be degraded by pronase or base-borohydride to yield the same, single type of carbohydrate chain.
447737	6	18	theme	carbohydrate	1062:1073	arg1	chain					1075:1079	the carbohydrate chain	1058:1079	the carbohydrate chain of secretory component	1058:1102	From the results of these studies a branched chain structure was assigned to the carbohydrate chain of secretory component.
447737	2	19	theme	chain	347:351	arg1	type					326:329	the same, single type	309:329	type	326:329	Secretory component could be degraded by pronase or base-borohydride to yield the same, single type of carbohydrate chain.
447737	0	20	from	chain	30:34	arg1	milk					75:78	human milk	69:78	human milk	69:78	Structure of the carbohydrate chain of free secretory component from human milk.
447737	2	21	theme	carbohydrate	334:345	arg1	chain					347:351	carbohydrate chain	334:351	carbohydrate chain	334:351	Secretory component could be degraded by pronase or base-borohydride to yield the same, single type of carbohydrate chain.
447737	3	22	from	acid	438:441	arg1	glycopeptide					361:372	glycopeptide	361:372	glycopeptide	361:372	In the glycopeptide produced by pronase digestion, aspartic acid was the only amino acid present in molar quantities after amino acid analysis, which suggests that the carbohydrate moiety is linked to the polypeptide chain at asparagine residues.
447737	1	23	theme	Secretory	81:89	arg1	component					91:99	Secretory component	81:99	Secretory component from human milk	81:115	Secretory component from human milk was found to contain 23.4% carbohydrate, which includes galactose, mannose, fucose, glucosamine, and sialic acid.
447737	3	24	theme	pronase	386:392	arg1	digestion					394:402	pronase digestion	386:402	pronase digestion	386:402	In the glycopeptide produced by pronase digestion, aspartic acid was the only amino acid present in molar quantities after amino acid analysis, which suggests that the carbohydrate moiety is linked to the polypeptide chain at asparagine residues.
447737	0	25	theme	carbohydrate	17:28	arg1	chain					30:34	the carbohydrate chain	13:34	the carbohydrate chain of free secretory component from human milk	13:78	Structure of the carbohydrate chain of free secretory component from human milk.
447737	1	26	from	milk	112:115	arg1	component					91:99	Secretory component	81:99	Secretory component from human milk	81:115	Secretory component from human milk was found to contain 23.4% carbohydrate, which includes galactose, mannose, fucose, glucosamine, and sialic acid.
447737	4	27	theme	methylation	672:682	arg1	component					707:715	secretory component	697:715	secretory component	697:715	The positions of links between the various sugar units were studied by methylation analyses of: secretory component, periodate-oxidized and reduced secretory component, the fragment produced by base-borohydride treatment, and the pronase glycopeptide after treatment with specific glycosidases.
447737	4	27	theme	methylation	672:682	arg1	component					759:767	periodate-oxidized and reduced secretory component	718:767	periodate-oxidized and reduced secretory component	718:767	The positions of links between the various sugar units were studied by methylation analyses of: secretory component, periodate-oxidized and reduced secretory component, the fragment produced by base-borohydride treatment, and the pronase glycopeptide after treatment with specific glycosidases.
447737	4	27	theme	methylation	672:682	arg1	fragment					774:781	the fragment	770:781	the fragment produced by base-borohydride treatment	770:820	The positions of links between the various sugar units were studied by methylation analyses of: secretory component, periodate-oxidized and reduced secretory component, the fragment produced by base-borohydride treatment, and the pronase glycopeptide after treatment with specific glycosidases.
447737	4	27	theme	methylation	672:682	arg1	analyses					684:691	methylation analyses	672:691	methylation analyses of: secretory component, periodate-oxidized and reduced secretory component, the fragment produced by base-borohydride treatment, and the pronase glycopeptide	672:850	The positions of links between the various sugar units were studied by methylation analyses of: secretory component, periodate-oxidized and reduced secretory component, the fragment produced by base-borohydride treatment, and the pronase glycopeptide after treatment with specific glycosidases.
447737	4	27	theme	methylation	672:682	arg1	glycopeptide					839:850	the pronase glycopeptide	827:850	the pronase glycopeptide	827:850	The positions of links between the various sugar units were studied by methylation analyses of: secretory component, periodate-oxidized and reduced secretory component, the fragment produced by base-borohydride treatment, and the pronase glycopeptide after treatment with specific glycosidases.
447737	3	28	dep	acid	438:441	arg1	suggests					504:511	suggests	504:511	suggests that the carbohydrate moiety is linked to the polypeptide chain at asparagine residues	504:598	In the glycopeptide produced by pronase digestion, aspartic acid was the only amino acid present in molar quantities after amino acid analysis, which suggests that the carbohydrate moiety is linked to the polypeptide chain at asparagine residues.
447737	0	29	from	milk	75:78	arg1	component					54:62	free secretory component	39:62	free secretory component from human milk	39:78	Structure of the carbohydrate chain of free secretory component from human milk.
447737	0	29	from	milk	75:78	arg1	chain					30:34	the carbohydrate chain	13:34	the carbohydrate chain of free secretory component from human milk	13:78	Structure of the carbohydrate chain of free secretory component from human milk.
447737	2	30	theme	same	313:316	arg1	type					326:329	the same, single type	309:329	type	326:329	Secretory component could be degraded by pronase or base-borohydride to yield the same, single type of carbohydrate chain.
447737	4	31	with	treatment	858:866	arg1	glycosidases					882:893	specific glycosidases	873:893	specific glycosidases	873:893	The positions of links between the various sugar units were studied by methylation analyses of: secretory component, periodate-oxidized and reduced secretory component, the fragment produced by base-borohydride treatment, and the pronase glycopeptide after treatment with specific glycosidases.
447737	6	32	theme	chain	1026:1030	arg1	structure					1032:1040	a branched chain structure	1015:1040	a branched chain structure	1015:1040	From the results of these studies a branched chain structure was assigned to the carbohydrate chain of secretory component.
447737	6	33	theme	branched	1017:1024	arg1	structure					1032:1040	a branched chain structure	1015:1040	a branched chain structure	1015:1040	From the results of these studies a branched chain structure was assigned to the carbohydrate chain of secretory component.
447737	4	34	gly	glycopeptide	839:850	arg2	glycopeptide					839:850	the pronase glycopeptide	827:850	the pronase glycopeptide	827:850	The positions of links between the various sugar units were studied by methylation analyses of: secretory component, periodate-oxidized and reduced secretory component, the fragment produced by base-borohydride treatment, and the pronase glycopeptide after treatment with specific glycosidases.
447737	4	34	gly	glycopeptide	839:850	arg2	analyses					684:691	methylation analyses	672:691	methylation analyses of: secretory component, periodate-oxidized and reduced secretory component, the fragment produced by base-borohydride treatment, and the pronase glycopeptide	672:850	The positions of links between the various sugar units were studied by methylation analyses of: secretory component, periodate-oxidized and reduced secretory component, the fragment produced by base-borohydride treatment, and the pronase glycopeptide after treatment with specific glycosidases.
447737	3	35	theme	aspartic	405:412	arg1	acid					438:441	the only amino acid	423:441	the only amino acid present in molar quantities	423:469	In the glycopeptide produced by pronase digestion, aspartic acid was the only amino acid present in molar quantities after amino acid analysis, which suggests that the carbohydrate moiety is linked to the polypeptide chain at asparagine residues.
447737	3	35	theme	aspartic	405:412	arg1	acid					414:417	aspartic acid	405:417	aspartic acid	405:417	In the glycopeptide produced by pronase digestion, aspartic acid was the only amino acid present in molar quantities after amino acid analysis, which suggests that the carbohydrate moiety is linked to the polypeptide chain at asparagine residues.
447737	0	36	theme	chain	30:34	arg1	Structure					0:8	Structure	0:8	Structure of the carbohydrate chain of free secretory component from human milk	0:78	Structure of the carbohydrate chain of free secretory component from human milk.
447737	0	37	theme	secretory	44:52	arg1	component					54:62	free secretory component	39:62	free secretory component from human milk	39:78	Structure of the carbohydrate chain of free secretory component from human milk.
447737	3	38	theme	asparagine	580:589	arg1	residues					591:598	asparagine residues	580:598	asparagine residues	580:598	In the glycopeptide produced by pronase digestion, aspartic acid was the only amino acid present in molar quantities after amino acid analysis, which suggests that the carbohydrate moiety is linked to the polypeptide chain at asparagine residues.
447737	3	39	theme	carbohydrate	522:533	arg1	moiety					535:540	the carbohydrate moiety	518:540	the carbohydrate moiety	518:540	In the glycopeptide produced by pronase digestion, aspartic acid was the only amino acid present in molar quantities after amino acid analysis, which suggests that the carbohydrate moiety is linked to the polypeptide chain at asparagine residues.
447737	1	40	theme	human	106:110	arg1	milk					112:115	human milk	106:115	human milk	106:115	Secretory component from human milk was found to contain 23.4% carbohydrate, which includes galactose, mannose, fucose, glucosamine, and sialic acid.
447737	0	41	theme	free	39:42	arg1	component					54:62	free secretory component	39:62	free secretory component from human milk	39:78	Structure of the carbohydrate chain of free secretory component from human milk.
447737	3	42	theme	molar	454:458	arg1	quantities					460:469	molar quantities	454:469	molar quantities	454:469	In the glycopeptide produced by pronase digestion, aspartic acid was the only amino acid present in molar quantities after amino acid analysis, which suggests that the carbohydrate moiety is linked to the polypeptide chain at asparagine residues.
447737	3	43	theme	present	443:449	arg1	acid					438:441	the only amino acid	423:441	the only amino acid present in molar quantities	423:469	In the glycopeptide produced by pronase digestion, aspartic acid was the only amino acid present in molar quantities after amino acid analysis, which suggests that the carbohydrate moiety is linked to the polypeptide chain at asparagine residues.
447737	3	43	theme	present	443:449	arg1	acid					414:417	aspartic acid	405:417	aspartic acid	405:417	In the glycopeptide produced by pronase digestion, aspartic acid was the only amino acid present in molar quantities after amino acid analysis, which suggests that the carbohydrate moiety is linked to the polypeptide chain at asparagine residues.
447737	3	44	from	present	443:449	arg1	quantities					460:469	molar quantities	454:469	molar quantities	454:469	In the glycopeptide produced by pronase digestion, aspartic acid was the only amino acid present in molar quantities after amino acid analysis, which suggests that the carbohydrate moiety is linked to the polypeptide chain at asparagine residues.
447737	4	45	theme	specific	873:880	arg1	glycosidases					882:893	specific glycosidases	873:893	specific glycosidases	873:893	The positions of links between the various sugar units were studied by methylation analyses of: secretory component, periodate-oxidized and reduced secretory component, the fragment produced by base-borohydride treatment, and the pronase glycopeptide after treatment with specific glycosidases.
447737	4	46	theme	reduced	741:747	arg1	component					759:767	periodate-oxidized and reduced secretory component	718:767	periodate-oxidized and reduced secretory component	718:767	The positions of links between the various sugar units were studied by methylation analyses of: secretory component, periodate-oxidized and reduced secretory component, the fragment produced by base-borohydride treatment, and the pronase glycopeptide after treatment with specific glycosidases.
447737	4	46	theme	reduced	741:747	arg1	analyses					684:691	methylation analyses	672:691	methylation analyses of: secretory component, periodate-oxidized and reduced secretory component, the fragment produced by base-borohydride treatment, and the pronase glycopeptide	672:850	The positions of links between the various sugar units were studied by methylation analyses of: secretory component, periodate-oxidized and reduced secretory component, the fragment produced by base-borohydride treatment, and the pronase glycopeptide after treatment with specific glycosidases.
447737	3	47	theme	polypeptide	559:569	arg1	chain					571:575	the polypeptide chain	555:575	the polypeptide chain at asparagine residues	555:598	In the glycopeptide produced by pronase digestion, aspartic acid was the only amino acid present in molar quantities after amino acid analysis, which suggests that the carbohydrate moiety is linked to the polypeptide chain at asparagine residues.
447737	3	48	theme	only	427:430	arg1	acid					438:441	the only amino acid	423:441	the only amino acid present in molar quantities	423:469	In the glycopeptide produced by pronase digestion, aspartic acid was the only amino acid present in molar quantities after amino acid analysis, which suggests that the carbohydrate moiety is linked to the polypeptide chain at asparagine residues.
447737	3	48	theme	only	427:430	arg1	acid					414:417	aspartic acid	405:417	aspartic acid	405:417	In the glycopeptide produced by pronase digestion, aspartic acid was the only amino acid present in molar quantities after amino acid analysis, which suggests that the carbohydrate moiety is linked to the polypeptide chain at asparagine residues.
447737	4	49	theme	various	636:642	arg1	units					650:654	the various sugar units	632:654	the various sugar units	632:654	The positions of links between the various sugar units were studied by methylation analyses of: secretory component, periodate-oxidized and reduced secretory component, the fragment produced by base-borohydride treatment, and the pronase glycopeptide after treatment with specific glycosidases.
447737	6	50	theme	studies	1007:1013	arg1	results					990:996	the results	986:996	the results of these studies	986:1013	From the results of these studies a branched chain structure was assigned to the carbohydrate chain of secretory component.
447737	3	51	theme	acid	483:486	arg1	analysis					488:495	amino acid analysis	477:495	amino acid analysis	477:495	In the glycopeptide produced by pronase digestion, aspartic acid was the only amino acid present in molar quantities after amino acid analysis, which suggests that the carbohydrate moiety is linked to the polypeptide chain at asparagine residues.
447737	4	52	theme	periodate-oxidized	718:735	arg1	component					759:767	periodate-oxidized and reduced secretory component	718:767	periodate-oxidized and reduced secretory component	718:767	The positions of links between the various sugar units were studied by methylation analyses of: secretory component, periodate-oxidized and reduced secretory component, the fragment produced by base-borohydride treatment, and the pronase glycopeptide after treatment with specific glycosidases.
447737	4	52	theme	periodate-oxidized	718:735	arg1	analyses					684:691	methylation analyses	672:691	methylation analyses of: secretory component, periodate-oxidized and reduced secretory component, the fragment produced by base-borohydride treatment, and the pronase glycopeptide	672:850	The positions of links between the various sugar units were studied by methylation analyses of: secretory component, periodate-oxidized and reduced secretory component, the fragment produced by base-borohydride treatment, and the pronase glycopeptide after treatment with specific glycosidases.
447737	3	53	attach	present	443:449	arg2	acid					414:417	aspartic acid	405:417	aspartic acid	405:417	In the glycopeptide produced by pronase digestion, aspartic acid was the only amino acid present in molar quantities after amino acid analysis, which suggests that the carbohydrate moiety is linked to the polypeptide chain at asparagine residues.
447737	3	53	attach	present	443:449	arg1	quantities					460:469	molar quantities	454:469	molar quantities	454:469	In the glycopeptide produced by pronase digestion, aspartic acid was the only amino acid present in molar quantities after amino acid analysis, which suggests that the carbohydrate moiety is linked to the polypeptide chain at asparagine residues.
447737	3	53	attach	present	443:449	arg2	acid					438:441	the only amino acid	423:441	the only amino acid present in molar quantities	423:469	In the glycopeptide produced by pronase digestion, aspartic acid was the only amino acid present in molar quantities after amino acid analysis, which suggests that the carbohydrate moiety is linked to the polypeptide chain at asparagine residues.
447737	3	54	theme	amino	432:436	arg1	acid					438:441	the only amino acid	423:441	the only amino acid present in molar quantities	423:469	In the glycopeptide produced by pronase digestion, aspartic acid was the only amino acid present in molar quantities after amino acid analysis, which suggests that the carbohydrate moiety is linked to the polypeptide chain at asparagine residues.
447737	3	54	theme	amino	432:436	arg1	acid					414:417	aspartic acid	405:417	aspartic acid	405:417	In the glycopeptide produced by pronase digestion, aspartic acid was the only amino acid present in molar quantities after amino acid analysis, which suggests that the carbohydrate moiety is linked to the polypeptide chain at asparagine residues.
447737	4	55	dep	analyses	684:691	arg1	component					707:715	secretory component	697:715	secretory component	697:715	The positions of links between the various sugar units were studied by methylation analyses of: secretory component, periodate-oxidized and reduced secretory component, the fragment produced by base-borohydride treatment, and the pronase glycopeptide after treatment with specific glycosidases.
447737	4	55	dep	analyses	684:691	arg1	component					759:767	periodate-oxidized and reduced secretory component	718:767	periodate-oxidized and reduced secretory component	718:767	The positions of links between the various sugar units were studied by methylation analyses of: secretory component, periodate-oxidized and reduced secretory component, the fragment produced by base-borohydride treatment, and the pronase glycopeptide after treatment with specific glycosidases.
447737	4	55	dep	analyses	684:691	arg1	fragment					774:781	the fragment	770:781	the fragment produced by base-borohydride treatment	770:820	The positions of links between the various sugar units were studied by methylation analyses of: secretory component, periodate-oxidized and reduced secretory component, the fragment produced by base-borohydride treatment, and the pronase glycopeptide after treatment with specific glycosidases.
447737	4	55	dep	analyses	684:691	arg1	analyses					684:691	methylation analyses	672:691	methylation analyses of: secretory component, periodate-oxidized and reduced secretory component, the fragment produced by base-borohydride treatment, and the pronase glycopeptide	672:850	The positions of links between the various sugar units were studied by methylation analyses of: secretory component, periodate-oxidized and reduced secretory component, the fragment produced by base-borohydride treatment, and the pronase glycopeptide after treatment with specific glycosidases.
447737	4	55	dep	analyses	684:691	arg1	glycopeptide					839:850	the pronase glycopeptide	827:850	the pronase glycopeptide	827:850	The positions of links between the various sugar units were studied by methylation analyses of: secretory component, periodate-oxidized and reduced secretory component, the fragment produced by base-borohydride treatment, and the pronase glycopeptide after treatment with specific glycosidases.
447737	6	56	theme	secretory	1084:1092	arg1	component					1094:1102	secretory component	1084:1102	secretory component	1084:1102	From the results of these studies a branched chain structure was assigned to the carbohydrate chain of secretory component.
447737	0	57	theme	component	54:62	arg1	chain					30:34	the carbohydrate chain	13:34	the carbohydrate chain of free secretory component from human milk	13:78	Structure of the carbohydrate chain of free secretory component from human milk.
447737	4	58	theme	secretory	749:757	arg1	component					759:767	periodate-oxidized and reduced secretory component	718:767	periodate-oxidized and reduced secretory component	718:767	The positions of links between the various sugar units were studied by methylation analyses of: secretory component, periodate-oxidized and reduced secretory component, the fragment produced by base-borohydride treatment, and the pronase glycopeptide after treatment with specific glycosidases.
447737	4	58	theme	secretory	749:757	arg1	analyses					684:691	methylation analyses	672:691	methylation analyses of: secretory component, periodate-oxidized and reduced secretory component, the fragment produced by base-borohydride treatment, and the pronase glycopeptide	672:850	The positions of links between the various sugar units were studied by methylation analyses of: secretory component, periodate-oxidized and reduced secretory component, the fragment produced by base-borohydride treatment, and the pronase glycopeptide after treatment with specific glycosidases.
447737	2	59	theme	single	319:324	arg1	type					326:329	the same, single type	309:329	type	326:329	Secretory component could be degraded by pronase or base-borohydride to yield the same, single type of carbohydrate chain.
447737	3	60	attach	linked	545:550	arg2	moiety					535:540	the carbohydrate moiety	518:540	the carbohydrate moiety	518:540	In the glycopeptide produced by pronase digestion, aspartic acid was the only amino acid present in molar quantities after amino acid analysis, which suggests that the carbohydrate moiety is linked to the polypeptide chain at asparagine residues.
447737	3	60	attach	linked	545:550	arg1	chain					571:575	the polypeptide chain	555:575	the polypeptide chain at asparagine residues	555:598	In the glycopeptide produced by pronase digestion, aspartic acid was the only amino acid present in molar quantities after amino acid analysis, which suggests that the carbohydrate moiety is linked to the polypeptide chain at asparagine residues.
6277894	12	0	theme	beta	1764:1767	arg1	GalNAcol					1786:1793	GlcNAc beta 1-6(Gal beta 1-3)GalNAcol	1757:1793	Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol	1713:1793	Two structures are consistent with the data obtained for A3: Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol and/or Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNac beta 1-6(Fuc alpha 1-2Gal beta 1-3)GalNacol.
6277894	10	1	theme	GalNAcol	1386:1393	arg1	GalNAcol					1386:1393	GalNAcol	1386:1393	GalNAcol	1386:1393	Enzymatic hydrolysis of the Gal beta 1-3GalNAcol linkage required prior removal of the Gal beta 1-4GlcNAc beta 1-unit attached to 0-6 of GalNAcol.
6277894	10	1	theme	GalNAcol	1386:1393	arg1	0-6					1379:1381	0-6	1379:1381	0-6	1379:1381	Enzymatic hydrolysis of the Gal beta 1-3GalNAcol linkage required prior removal of the Gal beta 1-4GlcNAc beta 1-unit attached to 0-6 of GalNAcol.
6277894	11	2	theme	beta	1495:1498	arg1	GalNacol					1517:1524	Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNacol	1457:1524	Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNacol	1457:1524	The data for A2 indicated a mixture of two oligosaccharides, Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNacol and Fuc alpha 1-2Gal beta 1-4GlcNac beta 1-6(Gal beta 1-3)-GalNacol, in an approximate molar ratio of 3 to 4:1, respectively.
6277894	11	2	theme	beta	1495:1498	arg1	oligosaccharides					1439:1454	two oligosaccharides	1435:1454	two oligosaccharides	1435:1454	The data for A2 indicated a mixture of two oligosaccharides, Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNacol and Fuc alpha 1-2Gal beta 1-4GlcNac beta 1-6(Gal beta 1-3)-GalNacol, in an approximate molar ratio of 3 to 4:1, respectively.
6277894	12	3	theme	alpha	1745:1749	arg1	1-3,4					1751:1755	Fuc alpha 1-3,4	1741:1755	Fuc alpha 1-3,4	1741:1755	Two structures are consistent with the data obtained for A3: Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol and/or Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNac beta 1-6(Fuc alpha 1-2Gal beta 1-3)GalNacol.
6277894	12	3	theme	alpha	1745:1749	arg1	beta					1730:1733	Fuc alpha 1-2Gal beta 1-4,3	1713:1739	Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol	1713:1793	Two structures are consistent with the data obtained for A3: Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol and/or Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNac beta 1-6(Fuc alpha 1-2Gal beta 1-3)GalNacol.
6277894	8	4	from	submaxillary	1037:1048	arg1	regions					1116:1122	their carbohydrate-to-protein linkage regions	1078:1122	their carbohydrate-to-protein linkage regions	1078:1122	The proposed structure, Gal beta 1-4GlcNAc beta 1-6(Gal beta 1-3)GalNAcol, has previously been found in human gastric, submaxillary, and ovarian cyst mucins in their carbohydrate-to-protein linkage regions.
6277894	8	5	theme	ovarian	1055:1061	arg1	mucins					1068:1073	human gastric, submaxillary, and ovarian cyst mucins	1022:1073	mucins	1068:1073	The proposed structure, Gal beta 1-4GlcNAc beta 1-6(Gal beta 1-3)GalNAcol, has previously been found in human gastric, submaxillary, and ovarian cyst mucins in their carbohydrate-to-protein linkage regions.
6277894	10	6	theme	beta	1281:1284	arg1	linkage					1298:1304	the Gal beta 1-3GalNAcol linkage	1273:1304	the Gal beta 1-3GalNAcol linkage	1273:1304	Enzymatic hydrolysis of the Gal beta 1-3GalNAcol linkage required prior removal of the Gal beta 1-4GlcNAc beta 1-unit attached to 0-6 of GalNAcol.
6277894	13	7	theme	oligosaccharides	1987:2002	arg1	tetrasaccharide					1936:1950	the "core" tetrasaccharide	1925:1950	the "core" tetrasaccharide of the larger human cervical mucin oligosaccharides A2 and A3	1925:2012	The results indicate that A1 represents the "core" tetrasaccharide of the larger human cervical mucin oligosaccharides A2 and A3.
6277894	12	8	theme	alpha	1717:1721	arg1	beta					1866:1869	Fuc alpha 1-2Gal beta 1-3	1849:1873	Fuc alpha 1-2Gal beta 1-3	1849:1873	Two structures are consistent with the data obtained for A3: Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol and/or Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNac beta 1-6(Fuc alpha 1-2Gal beta 1-3)GalNacol.
6277894	12	8	theme	alpha	1717:1721	arg1	1-3,4					1751:1755	Fuc alpha 1-3,4	1741:1755	Fuc alpha 1-3,4	1741:1755	Two structures are consistent with the data obtained for A3: Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol and/or Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNac beta 1-6(Fuc alpha 1-2Gal beta 1-3)GalNacol.
6277894	12	8	theme	alpha	1717:1721	arg1	beta					1730:1733	Fuc alpha 1-2Gal beta 1-4,3	1713:1739	Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol	1713:1793	Two structures are consistent with the data obtained for A3: Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol and/or Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNac beta 1-6(Fuc alpha 1-2Gal beta 1-3)GalNacol.
6277894	7	9	contain	contain	785:791	arg2	component					807:815	more than one component	793:815	more than one component	793:815	A1 was shown to contain more than one component, but structural analyses clearly demonstrated the presence of one predominant (75%) tetrasaccharide.
6277894	7	9	contain	contain	785:791	arg1	A1					769:770	A1	769:770	A1	769:770	A1 was shown to contain more than one component, but structural analyses clearly demonstrated the presence of one predominant (75%) tetrasaccharide.
6277894	8	10	theme	human	1022:1026	arg1	submaxillary					1037:1048	human gastric, submaxillary, and ovarian cyst mucins	1022:1073	submaxillary	1037:1048	The proposed structure, Gal beta 1-4GlcNAc beta 1-6(Gal beta 1-3)GalNAcol, has previously been found in human gastric, submaxillary, and ovarian cyst mucins in their carbohydrate-to-protein linkage regions.
6277894	12	11	theme	beta	1806:1809	arg1	GalNacol					1875:1882	A3: Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol and/or Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNac beta 1-6(Fuc alpha 1-2Gal beta 1-3)GalNacol	1709:1882	A3: Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol and/or Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNac beta 1-6(Fuc alpha 1-2Gal beta 1-3)GalNacol	1709:1882	Two structures are consistent with the data obtained for A3: Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol and/or Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNac beta 1-6(Fuc alpha 1-2Gal beta 1-3)GalNacol.
6277894	1	12	theme	reduced	222:228	arg1	oligosaccharides					264:279	reduced neutral, sialylated, and sulfated oligosaccharides	222:279	reduced neutral, sialylated, and sulfated oligosaccharides	222:279	It was previously shown that alkaline borohydride treatment of human midcycle cervical mucin releases a heterogeneous population of reduced neutral, sialylated, and sulfated oligosaccharides (Yurewicz, E. C., and Moghissi, K. S. (1981) J. Biol.
6277894	13	13	theme	"	1934:1934	arg1	tetrasaccharide					1936:1950	the "core" tetrasaccharide	1925:1950	the "core" tetrasaccharide of the larger human cervical mucin oligosaccharides A2 and A3	1925:2012	The results indicate that A1 represents the "core" tetrasaccharide of the larger human cervical mucin oligosaccharides A2 and A3.
6277894	8	14	theme	linkage	1108:1114	arg1	regions					1116:1122	their carbohydrate-to-protein linkage regions	1078:1122	their carbohydrate-to-protein linkage regions	1078:1122	The proposed structure, Gal beta 1-4GlcNAc beta 1-6(Gal beta 1-3)GalNAcol, has previously been found in human gastric, submaxillary, and ovarian cyst mucins in their carbohydrate-to-protein linkage regions.
6277894	8	15	from	mucins	1068:1073	arg1	regions					1116:1122	their carbohydrate-to-protein linkage regions	1078:1122	their carbohydrate-to-protein linkage regions	1078:1122	The proposed structure, Gal beta 1-4GlcNAc beta 1-6(Gal beta 1-3)GalNAcol, has previously been found in human gastric, submaxillary, and ovarian cyst mucins in their carbohydrate-to-protein linkage regions.
6277894	13	16	theme	cervical	1972:1979	arg1	oligosaccharides					1987:2002	the larger human cervical mucin oligosaccharides A2 and A3	1955:2012	the larger human cervical mucin oligosaccharides A2 and A3	1955:2012	The results indicate that A1 represents the "core" tetrasaccharide of the larger human cervical mucin oligosaccharides A2 and A3.
6277894	13	16	theme	cervical	1972:1979	arg1	A3					2011:2012	A3	2011:2012	A3	2011:2012	The results indicate that A1 represents the "core" tetrasaccharide of the larger human cervical mucin oligosaccharides A2 and A3.
6277894	13	16	theme	cervical	1972:1979	arg1	A2					2004:2005	A2	2004:2005	A2	2004:2005	The results indicate that A1 represents the "core" tetrasaccharide of the larger human cervical mucin oligosaccharides A2 and A3.
6277894	11	17	theme	Fuc	1472:1474	arg1	1-3,4					1482:1486	Fuc alpha 1-3,4	1472:1486	Fuc alpha 1-3,4	1472:1486	The data for A2 indicated a mixture of two oligosaccharides, Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNacol and Fuc alpha 1-2Gal beta 1-4GlcNac beta 1-6(Gal beta 1-3)-GalNacol, in an approximate molar ratio of 3 to 4:1, respectively.
6277894	11	17	theme	Fuc	1472:1474	arg1	1-4,3					1466:1470	beta 1-4,3	1461:1470	Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNacol	1457:1524	The data for A2 indicated a mixture of two oligosaccharides, Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNacol and Fuc alpha 1-2Gal beta 1-4GlcNac beta 1-6(Gal beta 1-3)-GalNacol, in an approximate molar ratio of 3 to 4:1, respectively.
6277894	1	18	theme	borohydride	128:138	arg1	treatment					140:148	alkaline borohydride treatment	119:148	alkaline borohydride treatment of human midcycle cervical mucin	119:181	It was previously shown that alkaline borohydride treatment of human midcycle cervical mucin releases a heterogeneous population of reduced neutral, sialylated, and sulfated oligosaccharides (Yurewicz, E. C., and Moghissi, K. S. (1981) J. Biol.
6277894	4	19	theme	neutral	372:378	arg1	oligosaccharides					380:395	Three major neutral oligosaccharides	360:395	Three major neutral oligosaccharides	360:395	Three major neutral oligosaccharides were isolated with approximate compositions of Fuc:Gal:GlcNAc:N-acetylgalactosaminitol (GalNAcol) = 0:2:1:1 (A1), 1:2:1:1 (A2), and 2:2:1:1 (A3).
6277894	11	20	theme	beta	1547:1550	arg1	beta					1575:1578	Gal beta 1-3	1571:1582	Gal beta 1-3	1571:1582	The data for A2 indicated a mixture of two oligosaccharides, Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNacol and Fuc alpha 1-2Gal beta 1-4GlcNac beta 1-6(Gal beta 1-3)-GalNacol, in an approximate molar ratio of 3 to 4:1, respectively.
6277894	11	20	theme	beta	1547:1550	arg1	beta					1562:1565	Fuc alpha 1-2Gal beta 1-4GlcNac beta 1-6	1530:1569	Fuc alpha 1-2Gal beta 1-4GlcNac beta 1-6(Gal beta 1-3)-GalNacol	1530:1592	The data for A2 indicated a mixture of two oligosaccharides, Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNacol and Fuc alpha 1-2Gal beta 1-4GlcNac beta 1-6(Gal beta 1-3)-GalNacol, in an approximate molar ratio of 3 to 4:1, respectively.
6277894	11	21	theme	alpha	1534:1538	arg1	beta					1575:1578	Gal beta 1-3	1571:1582	Gal beta 1-3	1571:1582	The data for A2 indicated a mixture of two oligosaccharides, Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNacol and Fuc alpha 1-2Gal beta 1-4GlcNac beta 1-6(Gal beta 1-3)-GalNacol, in an approximate molar ratio of 3 to 4:1, respectively.
6277894	11	21	theme	alpha	1534:1538	arg1	beta					1562:1565	Fuc alpha 1-2Gal beta 1-4GlcNac beta 1-6	1530:1569	Fuc alpha 1-2Gal beta 1-4GlcNac beta 1-6(Gal beta 1-3)-GalNacol	1530:1592	The data for A2 indicated a mixture of two oligosaccharides, Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNacol and Fuc alpha 1-2Gal beta 1-4GlcNac beta 1-6(Gal beta 1-3)-GalNacol, in an approximate molar ratio of 3 to 4:1, respectively.
6277894	0	22	theme	cervical	74:81	arg1	mucin					83:87	human midcycle cervical mucin	59:87	human midcycle cervical mucin	59:87	Structural characterization of neutral oligosaccharides of human midcycle cervical mucin.
6277894	1	23	theme	midcycle	159:166	arg1	mucin					177:181	human midcycle cervical mucin	153:181	human midcycle cervical mucin	153:181	It was previously shown that alkaline borohydride treatment of human midcycle cervical mucin releases a heterogeneous population of reduced neutral, sialylated, and sulfated oligosaccharides (Yurewicz, E. C., and Moghissi, K. S. (1981) J. Biol.
6277894	4	24	theme	GlcNAc	452:457	arg1	compositions					428:439	approximate compositions	416:439	approximate compositions of Fuc:Gal:GlcNAc:N-acetylgalactosaminitol (GalNAcol) = 0:2:1:1 (A1), 1:2:1:1 (A2), and 2:2:1:1 (A3)	416:540	Three major neutral oligosaccharides were isolated with approximate compositions of Fuc:Gal:GlcNAc:N-acetylgalactosaminitol (GalNAcol) = 0:2:1:1 (A1), 1:2:1:1 (A2), and 2:2:1:1 (A3).
6277894	10	25	theme	prior	1315:1319	arg1	removal					1321:1327	prior removal	1315:1327	prior removal of the Gal beta 1-4GlcNAc beta 1-unit attached to 0-6 of GalNAcol	1315:1393	Enzymatic hydrolysis of the Gal beta 1-3GalNAcol linkage required prior removal of the Gal beta 1-4GlcNAc beta 1-unit attached to 0-6 of GalNAcol.
6277894	1	26	theme	mucin	177:181	arg1	treatment					140:148	alkaline borohydride treatment	119:148	alkaline borohydride treatment of human midcycle cervical mucin	119:181	It was previously shown that alkaline borohydride treatment of human midcycle cervical mucin releases a heterogeneous population of reduced neutral, sialylated, and sulfated oligosaccharides (Yurewicz, E. C., and Moghissi, K. S. (1981) J. Biol.
6277894	10	27	theme	linkage	1298:1304	arg1	hydrolysis					1259:1268	Enzymatic hydrolysis	1249:1268	Enzymatic hydrolysis of the Gal beta 1-3GalNAcol linkage	1249:1304	Enzymatic hydrolysis of the Gal beta 1-3GalNAcol linkage required prior removal of the Gal beta 1-4GlcNAc beta 1-unit attached to 0-6 of GalNAcol.
6277894	11	28	theme	beta	1562:1565	arg1	oligosaccharides					1439:1454	two oligosaccharides	1435:1454	two oligosaccharides	1435:1454	The data for A2 indicated a mixture of two oligosaccharides, Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNacol and Fuc alpha 1-2Gal beta 1-4GlcNac beta 1-6(Gal beta 1-3)-GalNacol, in an approximate molar ratio of 3 to 4:1, respectively.
6277894	11	28	theme	beta	1562:1565	arg1	-GalNacol					1584:1592	Fuc alpha 1-2Gal beta 1-4GlcNac beta 1-6(Gal beta 1-3)-GalNacol	1530:1592	Fuc alpha 1-2Gal beta 1-4GlcNac beta 1-6(Gal beta 1-3)-GalNacol	1530:1592	The data for A2 indicated a mixture of two oligosaccharides, Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNacol and Fuc alpha 1-2Gal beta 1-4GlcNac beta 1-6(Gal beta 1-3)-GalNacol, in an approximate molar ratio of 3 to 4:1, respectively.
6277894	5	29	theme	cervical	592:599	arg1	chains					623:628	human cervical mucin oligosaccharide chains	586:628	human cervical mucin oligosaccharide chains	586:628	They comprised roughly 21%, 13%, and 8% of human cervical mucin oligosaccharide chains, respectively.
6277894	9	30	theme	Aspergillus	1149:1159	arg1	niger					1161:1165	Aspergillus niger	1149:1165	Aspergillus niger	1149:1165	beta-Galactosidase from Aspergillus niger selectively cleaved the Gal beta 1-4GlcNAc linkage in the intact tetrasaccharide.
6277894	4	31	theme	Fuc	444:446	arg1	compositions					428:439	approximate compositions	416:439	approximate compositions of Fuc:Gal:GlcNAc:N-acetylgalactosaminitol (GalNAcol) = 0:2:1:1 (A1), 1:2:1:1 (A2), and 2:2:1:1 (A3)	416:540	Three major neutral oligosaccharides were isolated with approximate compositions of Fuc:Gal:GlcNAc:N-acetylgalactosaminitol (GalNAcol) = 0:2:1:1 (A1), 1:2:1:1 (A2), and 2:2:1:1 (A3).
6277894	10	32	theme	Gal	1336:1338	arg1	beta					1355:1358	the Gal beta 1-4GlcNAc beta 1-unit	1332:1365	the Gal beta 1-4GlcNAc beta 1-unit attached to 0-6 of GalNAcol	1332:1393	Enzymatic hydrolysis of the Gal beta 1-3GalNAcol linkage required prior removal of the Gal beta 1-4GlcNAc beta 1-unit attached to 0-6 of GalNAcol.
6277894	5	33	theme	oligosaccharide	607:621	arg1	chains					623:628	human cervical mucin oligosaccharide chains	586:628	human cervical mucin oligosaccharide chains	586:628	They comprised roughly 21%, 13%, and 8% of human cervical mucin oligosaccharide chains, respectively.
6277894	6	34	with	methylation	710:720	arg1	glycosidases					755:766	glycosidases	755:766	glycosidases	755:766	In the present report, each was analyzed by periodate oxidation, methylation, and sequential degradation with glycosidases.
6277894	4	35	theme	Gal	448:450	arg1	compositions					428:439	approximate compositions	416:439	approximate compositions of Fuc:Gal:GlcNAc:N-acetylgalactosaminitol (GalNAcol) = 0:2:1:1 (A1), 1:2:1:1 (A2), and 2:2:1:1 (A3)	416:540	Three major neutral oligosaccharides were isolated with approximate compositions of Fuc:Gal:GlcNAc:N-acetylgalactosaminitol (GalNAcol) = 0:2:1:1 (A1), 1:2:1:1 (A2), and 2:2:1:1 (A3).
6277894	11	36	theme	molar	1613:1617	arg1	ratio					1619:1623	an approximate molar ratio	1598:1623	an approximate molar ratio of 3 to 4:1	1598:1635	The data for A2 indicated a mixture of two oligosaccharides, Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNacol and Fuc alpha 1-2Gal beta 1-4GlcNac beta 1-6(Gal beta 1-3)-GalNacol, in an approximate molar ratio of 3 to 4:1, respectively.
6277894	0	37	theme	mucin	83:87	arg1	oligosaccharides					39:54	neutral oligosaccharides	31:54	neutral oligosaccharides of human midcycle cervical mucin	31:87	Structural characterization of neutral oligosaccharides of human midcycle cervical mucin.
6277894	0	38	theme	Structural	0:9	arg1	characterization					11:26	Structural characterization	0:26	Structural characterization of neutral oligosaccharides of human midcycle cervical mucin.	0:88	Structural characterization of neutral oligosaccharides of human midcycle cervical mucin.
6277894	10	39	theme	1-unit	1360:1365	arg1	beta					1355:1358	the Gal beta 1-4GlcNAc beta 1-unit	1332:1365	the Gal beta 1-4GlcNAc beta 1-unit attached to 0-6 of GalNAcol	1332:1393	Enzymatic hydrolysis of the Gal beta 1-3GalNAcol linkage required prior removal of the Gal beta 1-4GlcNAc beta 1-unit attached to 0-6 of GalNAcol.
6277894	9	40	theme	beta	1195:1198	arg1	linkage					1210:1216	the Gal beta 1-4GlcNAc linkage	1187:1216	the Gal beta 1-4GlcNAc linkage in the intact tetrasaccharide	1187:1246	beta-Galactosidase from Aspergillus niger selectively cleaved the Gal beta 1-4GlcNAc linkage in the intact tetrasaccharide.
6277894	6	41	theme	sequential	727:736	arg1	degradation					738:748	sequential degradation	727:748	sequential degradation with glycosidases	727:766	In the present report, each was analyzed by periodate oxidation, methylation, and sequential degradation with glycosidases.
6277894	10	42	theme	1-4GlcNAc	1345:1353	arg1	beta					1355:1358	the Gal beta 1-4GlcNAc beta 1-unit	1332:1365	the Gal beta 1-4GlcNAc beta 1-unit attached to 0-6 of GalNAcol	1332:1393	Enzymatic hydrolysis of the Gal beta 1-3GalNAcol linkage required prior removal of the Gal beta 1-4GlcNAc beta 1-unit attached to 0-6 of GalNAcol.
6277894	12	43	theme	alpha	1853:1857	arg1	beta					1730:1733	Fuc alpha 1-2Gal beta 1-4,3	1713:1739	Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol	1713:1793	Two structures are consistent with the data obtained for A3: Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol and/or Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNac beta 1-6(Fuc alpha 1-2Gal beta 1-3)GalNacol.
6277894	12	43	theme	alpha	1853:1857	arg1	beta					1866:1869	Fuc alpha 1-2Gal beta 1-3	1849:1873	Fuc alpha 1-2Gal beta 1-3	1849:1873	Two structures are consistent with the data obtained for A3: Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol and/or Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNac beta 1-6(Fuc alpha 1-2Gal beta 1-3)GalNacol.
6277894	0	44	theme	oligosaccharides	39:54	arg1	characterization					11:26	Structural characterization	0:26	Structural characterization of neutral oligosaccharides of human midcycle cervical mucin.	0:88	Structural characterization of neutral oligosaccharides of human midcycle cervical mucin.
6277894	8	45	theme	Gal	942:944	arg1	beta					961:964	Gal beta 1-4GlcNAc beta 1-6	942:968	Gal beta 1-4GlcNAc beta 1-6(Gal beta 1-3)GalNAcol	942:990	The proposed structure, Gal beta 1-4GlcNAc beta 1-6(Gal beta 1-3)GalNAcol, has previously been found in human gastric, submaxillary, and ovarian cyst mucins in their carbohydrate-to-protein linkage regions.
6277894	8	45	theme	Gal	942:944	arg1	beta					974:977	Gal beta 1-3	970:981	Gal beta 1-3	970:981	The proposed structure, Gal beta 1-4GlcNAc beta 1-6(Gal beta 1-3)GalNAcol, has previously been found in human gastric, submaxillary, and ovarian cyst mucins in their carbohydrate-to-protein linkage regions.
6277894	6	46	with	oxidation	699:707	arg1	glycosidases					755:766	glycosidases	755:766	glycosidases	755:766	In the present report, each was analyzed by periodate oxidation, methylation, and sequential degradation with glycosidases.
6277894	11	47	theme	Gal	1504:1506	arg1	beta					1508:1511	Gal beta 1-3	1504:1515	Gal beta 1-3	1504:1515	The data for A2 indicated a mixture of two oligosaccharides, Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNacol and Fuc alpha 1-2Gal beta 1-4GlcNac beta 1-6(Gal beta 1-3)-GalNacol, in an approximate molar ratio of 3 to 4:1, respectively.
6277894	11	47	theme	Gal	1504:1506	arg1	beta					1495:1498	Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6	1457:1502	Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNacol	1457:1524	The data for A2 indicated a mixture of two oligosaccharides, Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNacol and Fuc alpha 1-2Gal beta 1-4GlcNac beta 1-6(Gal beta 1-3)-GalNacol, in an approximate molar ratio of 3 to 4:1, respectively.
6277894	1	48	dep	releases	183:190	arg1	1981					320:323	1981	320:323	1981	320:323	It was previously shown that alkaline borohydride treatment of human midcycle cervical mucin releases a heterogeneous population of reduced neutral, sialylated, and sulfated oligosaccharides (Yurewicz, E. C., and Moghissi, K. S. (1981) J. Biol.
6277894	1	48	dep	releases	183:190	arg1	K.					313:314	K.	313:314	K.	313:314	It was previously shown that alkaline borohydride treatment of human midcycle cervical mucin releases a heterogeneous population of reduced neutral, sialylated, and sulfated oligosaccharides (Yurewicz, E. C., and Moghissi, K. S. (1981) J. Biol.
6277894	1	48	dep	releases	183:190	arg1	Yurewicz					282:289	Yurewicz	282:289	Yurewicz	282:289	It was previously shown that alkaline borohydride treatment of human midcycle cervical mucin releases a heterogeneous population of reduced neutral, sialylated, and sulfated oligosaccharides (Yurewicz, E. C., and Moghissi, K. S. (1981) J. Biol.
6277894	1	48	dep	releases	183:190	arg1	C.					295:296	C.	295:296	C.	295:296	It was previously shown that alkaline borohydride treatment of human midcycle cervical mucin releases a heterogeneous population of reduced neutral, sialylated, and sulfated oligosaccharides (Yurewicz, E. C., and Moghissi, K. S. (1981) J. Biol.
6277894	1	48	dep	releases	183:190	arg1	S					316:316	S	316:316	S	316:316	It was previously shown that alkaline borohydride treatment of human midcycle cervical mucin releases a heterogeneous population of reduced neutral, sialylated, and sulfated oligosaccharides (Yurewicz, E. C., and Moghissi, K. S. (1981) J. Biol.
6277894	11	49	theme	oligosaccharides	1439:1454	arg1	mixture					1424:1430	a mixture	1422:1430	a mixture of two oligosaccharides, Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNacol and Fuc alpha 1-2Gal beta 1-4GlcNac beta 1-6(Gal beta 1-3)-GalNacol,	1422:1593	The data for A2 indicated a mixture of two oligosaccharides, Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNacol and Fuc alpha 1-2Gal beta 1-4GlcNac beta 1-6(Gal beta 1-3)-GalNacol, in an approximate molar ratio of 3 to 4:1, respectively.
6277894	0	50	theme	human	59:63	arg1	mucin					83:87	human midcycle cervical mucin	59:87	human midcycle cervical mucin	59:87	Structural characterization of neutral oligosaccharides of human midcycle cervical mucin.
6277894	8	51	theme	1-4GlcNAc	951:959	arg1	beta					961:964	Gal beta 1-4GlcNAc beta 1-6	942:968	Gal beta 1-4GlcNAc beta 1-6(Gal beta 1-3)GalNAcol	942:990	The proposed structure, Gal beta 1-4GlcNAc beta 1-6(Gal beta 1-3)GalNAcol, has previously been found in human gastric, submaxillary, and ovarian cyst mucins in their carbohydrate-to-protein linkage regions.
6277894	8	51	theme	1-4GlcNAc	951:959	arg1	beta					974:977	Gal beta 1-3	970:981	Gal beta 1-3	970:981	The proposed structure, Gal beta 1-4GlcNAc beta 1-6(Gal beta 1-3)GalNAcol, has previously been found in human gastric, submaxillary, and ovarian cyst mucins in their carbohydrate-to-protein linkage regions.
6277894	4	52	theme	=	495:495	arg1	A1					506:507	A1	506:507	A1	506:507	Three major neutral oligosaccharides were isolated with approximate compositions of Fuc:Gal:GlcNAc:N-acetylgalactosaminitol (GalNAcol) = 0:2:1:1 (A1), 1:2:1:1 (A2), and 2:2:1:1 (A3).
6277894	4	52	theme	=	495:495	arg1	0:2:1:1					497:503	N-acetylgalactosaminitol (GalNAcol) = 0:2:1:1	459:503	N-acetylgalactosaminitol (GalNAcol) = 0:2:1:1 (A1)	459:508	Three major neutral oligosaccharides were isolated with approximate compositions of Fuc:Gal:GlcNAc:N-acetylgalactosaminitol (GalNAcol) = 0:2:1:1 (A1), 1:2:1:1 (A2), and 2:2:1:1 (A3).
6277894	11	53	theme	Fuc	1530:1532	arg1	beta					1575:1578	Gal beta 1-3	1571:1582	Gal beta 1-3	1571:1582	The data for A2 indicated a mixture of two oligosaccharides, Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNacol and Fuc alpha 1-2Gal beta 1-4GlcNac beta 1-6(Gal beta 1-3)-GalNacol, in an approximate molar ratio of 3 to 4:1, respectively.
6277894	11	53	theme	Fuc	1530:1532	arg1	beta					1562:1565	Fuc alpha 1-2Gal beta 1-4GlcNac beta 1-6	1530:1569	Fuc alpha 1-2Gal beta 1-4GlcNac beta 1-6(Gal beta 1-3)-GalNacol	1530:1592	The data for A2 indicated a mixture of two oligosaccharides, Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNacol and Fuc alpha 1-2Gal beta 1-4GlcNac beta 1-6(Gal beta 1-3)-GalNacol, in an approximate molar ratio of 3 to 4:1, respectively.
6277894	12	54	theme	Fuc	1849:1851	arg1	beta					1730:1733	Fuc alpha 1-2Gal beta 1-4,3	1713:1739	Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol	1713:1793	Two structures are consistent with the data obtained for A3: Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol and/or Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNac beta 1-6(Fuc alpha 1-2Gal beta 1-3)GalNacol.
6277894	12	54	theme	Fuc	1849:1851	arg1	beta					1866:1869	Fuc alpha 1-2Gal beta 1-3	1849:1873	Fuc alpha 1-2Gal beta 1-3	1849:1873	Two structures are consistent with the data obtained for A3: Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol and/or Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNac beta 1-6(Fuc alpha 1-2Gal beta 1-3)GalNacol.
6277894	10	55	attach	attached	1367:1374	arg1	GalNAcol					1386:1393	GalNAcol	1386:1393	GalNAcol	1386:1393	Enzymatic hydrolysis of the Gal beta 1-3GalNAcol linkage required prior removal of the Gal beta 1-4GlcNAc beta 1-unit attached to 0-6 of GalNAcol.
6277894	10	55	attach	attached	1367:1374	arg1	0-6					1379:1381	0-6	1379:1381	0-6	1379:1381	Enzymatic hydrolysis of the Gal beta 1-3GalNAcol linkage required prior removal of the Gal beta 1-4GlcNAc beta 1-unit attached to 0-6 of GalNAcol.
6277894	10	55	attach	attached	1367:1374	arg2	beta					1355:1358	the Gal beta 1-4GlcNAc beta 1-unit	1332:1365	the Gal beta 1-4GlcNAc beta 1-unit attached to 0-6 of GalNAcol	1332:1393	Enzymatic hydrolysis of the Gal beta 1-3GalNAcol linkage required prior removal of the Gal beta 1-4GlcNAc beta 1-unit attached to 0-6 of GalNAcol.
6277894	1	56	theme	sialylated	239:248	arg1	oligosaccharides					264:279	reduced neutral, sialylated, and sulfated oligosaccharides	222:279	reduced neutral, sialylated, and sulfated oligosaccharides	222:279	It was previously shown that alkaline borohydride treatment of human midcycle cervical mucin releases a heterogeneous population of reduced neutral, sialylated, and sulfated oligosaccharides (Yurewicz, E. C., and Moghissi, K. S. (1981) J. Biol.
6277894	6	57	theme	periodate	689:697	arg1	oxidation					699:707	periodate oxidation	689:707	periodate oxidation	689:707	In the present report, each was analyzed by periodate oxidation, methylation, and sequential degradation with glycosidases.
6277894	11	58	theme	1-4,3	1466:1470	arg1	beta					1508:1511	Gal beta 1-3	1504:1515	Gal beta 1-3	1504:1515	The data for A2 indicated a mixture of two oligosaccharides, Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNacol and Fuc alpha 1-2Gal beta 1-4GlcNac beta 1-6(Gal beta 1-3)-GalNacol, in an approximate molar ratio of 3 to 4:1, respectively.
6277894	11	58	theme	1-4,3	1466:1470	arg1	beta					1495:1498	Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6	1457:1502	Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNacol	1457:1524	The data for A2 indicated a mixture of two oligosaccharides, Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNacol and Fuc alpha 1-2Gal beta 1-4GlcNac beta 1-6(Gal beta 1-3)-GalNacol, in an approximate molar ratio of 3 to 4:1, respectively.
6277894	8	59	theme	Gal	970:972	arg1	beta					961:964	Gal beta 1-4GlcNAc beta 1-6	942:968	Gal beta 1-4GlcNAc beta 1-6(Gal beta 1-3)GalNAcol	942:990	The proposed structure, Gal beta 1-4GlcNAc beta 1-6(Gal beta 1-3)GalNAcol, has previously been found in human gastric, submaxillary, and ovarian cyst mucins in their carbohydrate-to-protein linkage regions.
6277894	8	59	theme	Gal	970:972	arg1	beta					974:977	Gal beta 1-3	970:981	Gal beta 1-3	970:981	The proposed structure, Gal beta 1-4GlcNAc beta 1-6(Gal beta 1-3)GalNAcol, has previously been found in human gastric, submaxillary, and ovarian cyst mucins in their carbohydrate-to-protein linkage regions.
6277894	6	60	with	degradation	738:748	arg1	glycosidases					755:766	glycosidases	755:766	glycosidases	755:766	In the present report, each was analyzed by periodate oxidation, methylation, and sequential degradation with glycosidases.
6277894	4	61	theme	2:2:1:1	529:535	arg1	compositions					428:439	approximate compositions	416:439	approximate compositions of Fuc:Gal:GlcNAc:N-acetylgalactosaminitol (GalNAcol) = 0:2:1:1 (A1), 1:2:1:1 (A2), and 2:2:1:1 (A3)	416:540	Three major neutral oligosaccharides were isolated with approximate compositions of Fuc:Gal:GlcNAc:N-acetylgalactosaminitol (GalNAcol) = 0:2:1:1 (A1), 1:2:1:1 (A2), and 2:2:1:1 (A3).
6277894	11	62	theme	Gal	1457:1459	arg1	beta					1508:1511	Gal beta 1-3	1504:1515	Gal beta 1-3	1504:1515	The data for A2 indicated a mixture of two oligosaccharides, Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNacol and Fuc alpha 1-2Gal beta 1-4GlcNac beta 1-6(Gal beta 1-3)-GalNacol, in an approximate molar ratio of 3 to 4:1, respectively.
6277894	11	62	theme	Gal	1457:1459	arg1	beta					1495:1498	Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6	1457:1502	Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNacol	1457:1524	The data for A2 indicated a mixture of two oligosaccharides, Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNacol and Fuc alpha 1-2Gal beta 1-4GlcNac beta 1-6(Gal beta 1-3)-GalNacol, in an approximate molar ratio of 3 to 4:1, respectively.
6277894	1	63	theme	oligosaccharides	264:279	arg1	population					208:217	a heterogeneous population	192:217	a heterogeneous population of reduced neutral, sialylated, and sulfated oligosaccharides	192:279	It was previously shown that alkaline borohydride treatment of human midcycle cervical mucin releases a heterogeneous population of reduced neutral, sialylated, and sulfated oligosaccharides (Yurewicz, E. C., and Moghissi, K. S. (1981) J. Biol.
6277894	12	64	theme	GlcNAc	1757:1762	arg1	beta					1777:1780	Gal beta 1-3	1773:1784	Gal beta 1-3	1773:1784	Two structures are consistent with the data obtained for A3: Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol and/or Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNac beta 1-6(Fuc alpha 1-2Gal beta 1-3)GalNacol.
6277894	12	64	theme	GlcNAc	1757:1762	arg1	beta					1764:1767	GlcNAc beta 1-6	1757:1771	Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol	1713:1793	Two structures are consistent with the data obtained for A3: Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol and/or Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNac beta 1-6(Fuc alpha 1-2Gal beta 1-3)GalNacol.
6277894	4	65	theme	1:2:1:1	511:517	arg1	compositions					428:439	approximate compositions	416:439	approximate compositions of Fuc:Gal:GlcNAc:N-acetylgalactosaminitol (GalNAcol) = 0:2:1:1 (A1), 1:2:1:1 (A2), and 2:2:1:1 (A3)	416:540	Three major neutral oligosaccharides were isolated with approximate compositions of Fuc:Gal:GlcNAc:N-acetylgalactosaminitol (GalNAcol) = 0:2:1:1 (A1), 1:2:1:1 (A2), and 2:2:1:1 (A3).
6277894	10	66	theme	Gal	1277:1279	arg1	linkage					1298:1304	the Gal beta 1-3GalNAcol linkage	1273:1304	the Gal beta 1-3GalNAcol linkage	1273:1304	Enzymatic hydrolysis of the Gal beta 1-3GalNAcol linkage required prior removal of the Gal beta 1-4GlcNAc beta 1-unit attached to 0-6 of GalNAcol.
6277894	10	67	theme	Enzymatic	1249:1257	arg1	hydrolysis					1259:1268	Enzymatic hydrolysis	1249:1268	Enzymatic hydrolysis of the Gal beta 1-3GalNAcol linkage	1249:1304	Enzymatic hydrolysis of the Gal beta 1-3GalNAcol linkage required prior removal of the Gal beta 1-4GlcNAc beta 1-unit attached to 0-6 of GalNAcol.
6277894	4	68	theme	major	366:370	arg1	oligosaccharides					380:395	Three major neutral oligosaccharides	360:395	Three major neutral oligosaccharides	360:395	Three major neutral oligosaccharides were isolated with approximate compositions of Fuc:Gal:GlcNAc:N-acetylgalactosaminitol (GalNAcol) = 0:2:1:1 (A1), 1:2:1:1 (A2), and 2:2:1:1 (A3).
6277894	13	69	theme	mucin	1981:1985	arg1	oligosaccharides					1987:2002	the larger human cervical mucin oligosaccharides A2 and A3	1955:2012	the larger human cervical mucin oligosaccharides A2 and A3	1955:2012	The results indicate that A1 represents the "core" tetrasaccharide of the larger human cervical mucin oligosaccharides A2 and A3.
6277894	13	69	theme	mucin	1981:1985	arg1	A3					2011:2012	A3	2011:2012	A3	2011:2012	The results indicate that A1 represents the "core" tetrasaccharide of the larger human cervical mucin oligosaccharides A2 and A3.
6277894	13	69	theme	mucin	1981:1985	arg1	A2					2004:2005	A2	2004:2005	A2	2004:2005	The results indicate that A1 represents the "core" tetrasaccharide of the larger human cervical mucin oligosaccharides A2 and A3.
6277894	12	70	theme	Fuc	1741:1743	arg1	1-3,4					1751:1755	Fuc alpha 1-3,4	1741:1755	Fuc alpha 1-3,4	1741:1755	Two structures are consistent with the data obtained for A3: Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol and/or Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNac beta 1-6(Fuc alpha 1-2Gal beta 1-3)GalNacol.
6277894	12	70	theme	Fuc	1741:1743	arg1	beta					1730:1733	Fuc alpha 1-2Gal beta 1-4,3	1713:1739	Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol	1713:1793	Two structures are consistent with the data obtained for A3: Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol and/or Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNac beta 1-6(Fuc alpha 1-2Gal beta 1-3)GalNacol.
6277894	12	71	theme	Fuc	1817:1819	arg1	1-3,4					1827:1831	Fuc alpha 1-3,4	1817:1831	Fuc alpha 1-3,4	1817:1831	Two structures are consistent with the data obtained for A3: Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol and/or Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNac beta 1-6(Fuc alpha 1-2Gal beta 1-3)GalNacol.
6277894	12	71	theme	Fuc	1817:1819	arg1	beta					1806:1809	Gal beta 1-4,3	1802:1815	Gal beta 1-4,3(Fuc alpha 1-3,4)	1802:1832	Two structures are consistent with the data obtained for A3: Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol and/or Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNac beta 1-6(Fuc alpha 1-2Gal beta 1-3)GalNacol.
6277894	11	72	theme	GlcNAc	1488:1493	arg1	beta					1508:1511	Gal beta 1-3	1504:1515	Gal beta 1-3	1504:1515	The data for A2 indicated a mixture of two oligosaccharides, Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNacol and Fuc alpha 1-2Gal beta 1-4GlcNac beta 1-6(Gal beta 1-3)-GalNacol, in an approximate molar ratio of 3 to 4:1, respectively.
6277894	11	72	theme	GlcNAc	1488:1493	arg1	beta					1495:1498	Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6	1457:1502	Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNacol	1457:1524	The data for A2 indicated a mixture of two oligosaccharides, Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNacol and Fuc alpha 1-2Gal beta 1-4GlcNac beta 1-6(Gal beta 1-3)-GalNacol, in an approximate molar ratio of 3 to 4:1, respectively.
6277894	6	73	theme	present	652:658	arg1	report					660:665	the present report	648:665	the present report	648:665	In the present report, each was analyzed by periodate oxidation, methylation, and sequential degradation with glycosidases.
6277894	1	74	theme	heterogeneous	194:206	arg1	population					208:217	a heterogeneous population	192:217	a heterogeneous population of reduced neutral, sialylated, and sulfated oligosaccharides	192:279	It was previously shown that alkaline borohydride treatment of human midcycle cervical mucin releases a heterogeneous population of reduced neutral, sialylated, and sulfated oligosaccharides (Yurewicz, E. C., and Moghissi, K. S. (1981) J. Biol.
6277894	12	75	theme	Fuc	1713:1715	arg1	beta					1866:1869	Fuc alpha 1-2Gal beta 1-3	1849:1873	Fuc alpha 1-2Gal beta 1-3	1849:1873	Two structures are consistent with the data obtained for A3: Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol and/or Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNac beta 1-6(Fuc alpha 1-2Gal beta 1-3)GalNacol.
6277894	12	75	theme	Fuc	1713:1715	arg1	1-3,4					1751:1755	Fuc alpha 1-3,4	1741:1755	Fuc alpha 1-3,4	1741:1755	Two structures are consistent with the data obtained for A3: Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol and/or Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNac beta 1-6(Fuc alpha 1-2Gal beta 1-3)GalNacol.
6277894	12	75	theme	Fuc	1713:1715	arg1	beta					1730:1733	Fuc alpha 1-2Gal beta 1-4,3	1713:1739	Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol	1713:1793	Two structures are consistent with the data obtained for A3: Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol and/or Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNac beta 1-6(Fuc alpha 1-2Gal beta 1-3)GalNacol.
6277894	8	76	theme	cyst	1063:1066	arg1	mucins					1068:1073	human gastric, submaxillary, and ovarian cyst mucins	1022:1073	mucins	1068:1073	The proposed structure, Gal beta 1-4GlcNAc beta 1-6(Gal beta 1-3)GalNAcol, has previously been found in human gastric, submaxillary, and ovarian cyst mucins in their carbohydrate-to-protein linkage regions.
6277894	13	77	dep	oligosaccharides	1987:2002	arg1	oligosaccharides					1987:2002	the larger human cervical mucin oligosaccharides A2 and A3	1955:2012	the larger human cervical mucin oligosaccharides A2 and A3	1955:2012	The results indicate that A1 represents the "core" tetrasaccharide of the larger human cervical mucin oligosaccharides A2 and A3.
6277894	13	77	dep	oligosaccharides	1987:2002	arg1	A3					2011:2012	A3	2011:2012	A3	2011:2012	The results indicate that A1 represents the "core" tetrasaccharide of the larger human cervical mucin oligosaccharides A2 and A3.
6277894	13	77	dep	oligosaccharides	1987:2002	arg1	A2					2004:2005	A2	2004:2005	A2	2004:2005	The results indicate that A1 represents the "core" tetrasaccharide of the larger human cervical mucin oligosaccharides A2 and A3.
6277894	9	78	from	niger	1161:1165	arg1	beta-Galactosidase					1125:1142	beta-Galactosidase	1125:1142	beta-Galactosidase from Aspergillus niger	1125:1165	beta-Galactosidase from Aspergillus niger selectively cleaved the Gal beta 1-4GlcNAc linkage in the intact tetrasaccharide.
6277894	4	79	theme	approximate	416:426	arg1	compositions					428:439	approximate compositions	416:439	approximate compositions of Fuc:Gal:GlcNAc:N-acetylgalactosaminitol (GalNAcol) = 0:2:1:1 (A1), 1:2:1:1 (A2), and 2:2:1:1 (A3)	416:540	Three major neutral oligosaccharides were isolated with approximate compositions of Fuc:Gal:GlcNAc:N-acetylgalactosaminitol (GalNAcol) = 0:2:1:1 (A1), 1:2:1:1 (A2), and 2:2:1:1 (A3).
6277894	12	80	theme	Gal	1802:1804	arg1	1-3,4					1827:1831	Fuc alpha 1-3,4	1817:1831	Fuc alpha 1-3,4	1817:1831	Two structures are consistent with the data obtained for A3: Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol and/or Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNac beta 1-6(Fuc alpha 1-2Gal beta 1-3)GalNacol.
6277894	12	80	theme	Gal	1802:1804	arg1	beta					1806:1809	Gal beta 1-4,3	1802:1815	Gal beta 1-4,3(Fuc alpha 1-3,4)	1802:1832	Two structures are consistent with the data obtained for A3: Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol and/or Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNac beta 1-6(Fuc alpha 1-2Gal beta 1-3)GalNacol.
6277894	7	81	theme	tetrasaccharide	901:915	arg1	presence					867:874	the presence	863:874	the presence of one predominant (75%) tetrasaccharide	863:915	A1 was shown to contain more than one component, but structural analyses clearly demonstrated the presence of one predominant (75%) tetrasaccharide.
6277894	1	82	theme	neutral	230:236	arg1	oligosaccharides					264:279	reduced neutral, sialylated, and sulfated oligosaccharides	222:279	reduced neutral, sialylated, and sulfated oligosaccharides	222:279	It was previously shown that alkaline borohydride treatment of human midcycle cervical mucin releases a heterogeneous population of reduced neutral, sialylated, and sulfated oligosaccharides (Yurewicz, E. C., and Moghissi, K. S. (1981) J. Biol.
6277894	8	83	theme	gastric	1028:1034	arg1	submaxillary					1037:1048	human gastric, submaxillary, and ovarian cyst mucins	1022:1073	submaxillary	1037:1048	The proposed structure, Gal beta 1-4GlcNAc beta 1-6(Gal beta 1-3)GalNAcol, has previously been found in human gastric, submaxillary, and ovarian cyst mucins in their carbohydrate-to-protein linkage regions.
6277894	12	84	theme	beta	1730:1733	arg1	GalNacol					1875:1882	A3: Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol and/or Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNac beta 1-6(Fuc alpha 1-2Gal beta 1-3)GalNacol	1709:1882	A3: Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol and/or Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNac beta 1-6(Fuc alpha 1-2Gal beta 1-3)GalNacol	1709:1882	Two structures are consistent with the data obtained for A3: Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol and/or Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNac beta 1-6(Fuc alpha 1-2Gal beta 1-3)GalNacol.
6277894	8	85	theme	carbohydrate-to-protein	1084:1106	arg1	regions					1116:1122	their carbohydrate-to-protein linkage regions	1078:1122	their carbohydrate-to-protein linkage regions	1078:1122	The proposed structure, Gal beta 1-4GlcNAc beta 1-6(Gal beta 1-3)GalNAcol, has previously been found in human gastric, submaxillary, and ovarian cyst mucins in their carbohydrate-to-protein linkage regions.
6277894	11	86	theme	approximate	1601:1611	arg1	ratio					1619:1623	an approximate molar ratio	1598:1623	an approximate molar ratio of 3 to 4:1	1598:1635	The data for A2 indicated a mixture of two oligosaccharides, Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNacol and Fuc alpha 1-2Gal beta 1-4GlcNac beta 1-6(Gal beta 1-3)-GalNacol, in an approximate molar ratio of 3 to 4:1, respectively.
6277894	7	87	theme	predominant	883:893	arg1	tetrasaccharide					901:915	one predominant (75%) tetrasaccharide	879:915	one predominant (75%) tetrasaccharide	879:915	A1 was shown to contain more than one component, but structural analyses clearly demonstrated the presence of one predominant (75%) tetrasaccharide.
6277894	1	88	theme	alkaline	119:126	arg1	treatment					140:148	alkaline borohydride treatment	119:148	alkaline borohydride treatment of human midcycle cervical mucin	119:181	It was previously shown that alkaline borohydride treatment of human midcycle cervical mucin releases a heterogeneous population of reduced neutral, sialylated, and sulfated oligosaccharides (Yurewicz, E. C., and Moghissi, K. S. (1981) J. Biol.
6277894	12	89	theme	A3	1709:1710	arg1	GalNacol					1875:1882	A3: Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol and/or Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNac beta 1-6(Fuc alpha 1-2Gal beta 1-3)GalNacol	1709:1882	A3: Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol and/or Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNac beta 1-6(Fuc alpha 1-2Gal beta 1-3)GalNacol	1709:1882	Two structures are consistent with the data obtained for A3: Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol and/or Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNac beta 1-6(Fuc alpha 1-2Gal beta 1-3)GalNacol.
6277894	1	90	dep	Yurewicz	282:289	arg1	Biol					329:332	Biol	329:332	Biol	329:332	It was previously shown that alkaline borohydride treatment of human midcycle cervical mucin releases a heterogeneous population of reduced neutral, sialylated, and sulfated oligosaccharides (Yurewicz, E. C., and Moghissi, K. S. (1981) J. Biol.
6277894	7	91	theme	structural	822:831	arg1	analyses					833:840	structural analyses	822:840	structural analyses	822:840	A1 was shown to contain more than one component, but structural analyses clearly demonstrated the presence of one predominant (75%) tetrasaccharide.
6277894	11	92	theme	1-4GlcNac	1552:1560	arg1	beta					1575:1578	Gal beta 1-3	1571:1582	Gal beta 1-3	1571:1582	The data for A2 indicated a mixture of two oligosaccharides, Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNacol and Fuc alpha 1-2Gal beta 1-4GlcNac beta 1-6(Gal beta 1-3)-GalNacol, in an approximate molar ratio of 3 to 4:1, respectively.
6277894	11	92	theme	1-4GlcNac	1552:1560	arg1	beta					1562:1565	Fuc alpha 1-2Gal beta 1-4GlcNac beta 1-6	1530:1569	Fuc alpha 1-2Gal beta 1-4GlcNac beta 1-6(Gal beta 1-3)-GalNacol	1530:1592	The data for A2 indicated a mixture of two oligosaccharides, Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNacol and Fuc alpha 1-2Gal beta 1-4GlcNac beta 1-6(Gal beta 1-3)-GalNacol, in an approximate molar ratio of 3 to 4:1, respectively.
6277894	5	93	theme	chains	623:628	arg1	%					573:573	13%	571:573	13%	571:573	They comprised roughly 21%, 13%, and 8% of human cervical mucin oligosaccharide chains, respectively.
6277894	5	93	theme	chains	623:628	arg1	%					581:581	8%	580:581	8% of human cervical mucin oligosaccharide chains	580:628	They comprised roughly 21%, 13%, and 8% of human cervical mucin oligosaccharide chains, respectively.
6277894	5	93	theme	chains	623:628	arg1	chains					623:628	human cervical mucin oligosaccharide chains	586:628	human cervical mucin oligosaccharide chains	586:628	They comprised roughly 21%, 13%, and 8% of human cervical mucin oligosaccharide chains, respectively.
6277894	5	93	theme	chains	623:628	arg1	%					568:568	21%	566:568	21%	566:568	They comprised roughly 21%, 13%, and 8% of human cervical mucin oligosaccharide chains, respectively.
6277894	1	94	theme	human	153:157	arg1	mucin					177:181	human midcycle cervical mucin	153:181	human midcycle cervical mucin	153:181	It was previously shown that alkaline borohydride treatment of human midcycle cervical mucin releases a heterogeneous population of reduced neutral, sialylated, and sulfated oligosaccharides (Yurewicz, E. C., and Moghissi, K. S. (1981) J. Biol.
6277894	12	95	theme	1-2Gal	1723:1728	arg1	beta					1866:1869	Fuc alpha 1-2Gal beta 1-3	1849:1873	Fuc alpha 1-2Gal beta 1-3	1849:1873	Two structures are consistent with the data obtained for A3: Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol and/or Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNac beta 1-6(Fuc alpha 1-2Gal beta 1-3)GalNacol.
6277894	12	95	theme	1-2Gal	1723:1728	arg1	1-3,4					1751:1755	Fuc alpha 1-3,4	1741:1755	Fuc alpha 1-3,4	1741:1755	Two structures are consistent with the data obtained for A3: Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol and/or Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNac beta 1-6(Fuc alpha 1-2Gal beta 1-3)GalNacol.
6277894	12	95	theme	1-2Gal	1723:1728	arg1	beta					1730:1733	Fuc alpha 1-2Gal beta 1-4,3	1713:1739	Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol	1713:1793	Two structures are consistent with the data obtained for A3: Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol and/or Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNac beta 1-6(Fuc alpha 1-2Gal beta 1-3)GalNacol.
6277894	11	96	theme	1-2Gal	1540:1545	arg1	beta					1575:1578	Gal beta 1-3	1571:1582	Gal beta 1-3	1571:1582	The data for A2 indicated a mixture of two oligosaccharides, Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNacol and Fuc alpha 1-2Gal beta 1-4GlcNac beta 1-6(Gal beta 1-3)-GalNacol, in an approximate molar ratio of 3 to 4:1, respectively.
6277894	11	96	theme	1-2Gal	1540:1545	arg1	beta					1562:1565	Fuc alpha 1-2Gal beta 1-4GlcNac beta 1-6	1530:1569	Fuc alpha 1-2Gal beta 1-4GlcNac beta 1-6(Gal beta 1-3)-GalNacol	1530:1592	The data for A2 indicated a mixture of two oligosaccharides, Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNacol and Fuc alpha 1-2Gal beta 1-4GlcNac beta 1-6(Gal beta 1-3)-GalNacol, in an approximate molar ratio of 3 to 4:1, respectively.
6277894	1	97	theme	cervical	168:175	arg1	mucin					177:181	human midcycle cervical mucin	153:181	human midcycle cervical mucin	153:181	It was previously shown that alkaline borohydride treatment of human midcycle cervical mucin releases a heterogeneous population of reduced neutral, sialylated, and sulfated oligosaccharides (Yurewicz, E. C., and Moghissi, K. S. (1981) J. Biol.
6277894	3	98	dep	256	341:343	arg1	11895-11905					346:356	11895-11905	346:356	11895-11905	346:356	256, 11895-11905).
6277894	12	99	theme	Gal	1773:1775	arg1	beta					1777:1780	Gal beta 1-3	1773:1784	Gal beta 1-3	1773:1784	Two structures are consistent with the data obtained for A3: Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol and/or Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNac beta 1-6(Fuc alpha 1-2Gal beta 1-3)GalNacol.
6277894	12	99	theme	Gal	1773:1775	arg1	beta					1764:1767	GlcNAc beta 1-6	1757:1771	Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol	1713:1793	Two structures are consistent with the data obtained for A3: Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol and/or Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNac beta 1-6(Fuc alpha 1-2Gal beta 1-3)GalNacol.
6277894	11	100	theme	Gal	1571:1573	arg1	beta					1575:1578	Gal beta 1-3	1571:1582	Gal beta 1-3	1571:1582	The data for A2 indicated a mixture of two oligosaccharides, Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNacol and Fuc alpha 1-2Gal beta 1-4GlcNac beta 1-6(Gal beta 1-3)-GalNacol, in an approximate molar ratio of 3 to 4:1, respectively.
6277894	11	100	theme	Gal	1571:1573	arg1	beta					1562:1565	Fuc alpha 1-2Gal beta 1-4GlcNac beta 1-6	1530:1569	Fuc alpha 1-2Gal beta 1-4GlcNac beta 1-6(Gal beta 1-3)-GalNacol	1530:1592	The data for A2 indicated a mixture of two oligosaccharides, Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNacol and Fuc alpha 1-2Gal beta 1-4GlcNac beta 1-6(Gal beta 1-3)-GalNacol, in an approximate molar ratio of 3 to 4:1, respectively.
6277894	5	101	theme	human	586:590	arg1	chains					623:628	human cervical mucin oligosaccharide chains	586:628	human cervical mucin oligosaccharide chains	586:628	They comprised roughly 21%, 13%, and 8% of human cervical mucin oligosaccharide chains, respectively.
6277894	9	102	from	linkage	1210:1216	arg1	tetrasaccharide					1232:1246	the intact tetrasaccharide	1221:1246	the intact tetrasaccharide	1221:1246	beta-Galactosidase from Aspergillus niger selectively cleaved the Gal beta 1-4GlcNAc linkage in the intact tetrasaccharide.
6277894	1	103	gly	sialylated	239:248	arg1	oligosaccharides					264:279	reduced neutral, sialylated, and sulfated oligosaccharides	222:279	reduced neutral, sialylated, and sulfated oligosaccharides	222:279	It was previously shown that alkaline borohydride treatment of human midcycle cervical mucin releases a heterogeneous population of reduced neutral, sialylated, and sulfated oligosaccharides (Yurewicz, E. C., and Moghissi, K. S. (1981) J. Biol.
6277894	12	104	with	consistent	1671:1680	arg1	data					1691:1694	the data	1687:1694	the data obtained for A3: Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol and/or Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNac beta 1-6(Fuc alpha 1-2Gal beta 1-3)GalNacol	1687:1882	Two structures are consistent with the data obtained for A3: Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol and/or Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNac beta 1-6(Fuc alpha 1-2Gal beta 1-3)GalNacol.
6277894	10	105	theme	1-3GalNAcol	1286:1296	arg1	linkage					1298:1304	the Gal beta 1-3GalNAcol linkage	1273:1304	the Gal beta 1-3GalNAcol linkage	1273:1304	Enzymatic hydrolysis of the Gal beta 1-3GalNAcol linkage required prior removal of the Gal beta 1-4GlcNAc beta 1-unit attached to 0-6 of GalNAcol.
6277894	5	106	theme	mucin	601:605	arg1	chains					623:628	human cervical mucin oligosaccharide chains	586:628	human cervical mucin oligosaccharide chains	586:628	They comprised roughly 21%, 13%, and 8% of human cervical mucin oligosaccharide chains, respectively.
6277894	13	107	theme	larger	1959:1964	arg1	oligosaccharides					1987:2002	the larger human cervical mucin oligosaccharides A2 and A3	1955:2012	the larger human cervical mucin oligosaccharides A2 and A3	1955:2012	The results indicate that A1 represents the "core" tetrasaccharide of the larger human cervical mucin oligosaccharides A2 and A3.
6277894	13	107	theme	larger	1959:1964	arg1	A3					2011:2012	A3	2011:2012	A3	2011:2012	The results indicate that A1 represents the "core" tetrasaccharide of the larger human cervical mucin oligosaccharides A2 and A3.
6277894	13	107	theme	larger	1959:1964	arg1	A2					2004:2005	A2	2004:2005	A2	2004:2005	The results indicate that A1 represents the "core" tetrasaccharide of the larger human cervical mucin oligosaccharides A2 and A3.
6277894	8	108	theme	proposed	922:929	arg1	structure					931:939	The proposed structure	918:939	The proposed structure	918:939	The proposed structure, Gal beta 1-4GlcNAc beta 1-6(Gal beta 1-3)GalNAcol, has previously been found in human gastric, submaxillary, and ovarian cyst mucins in their carbohydrate-to-protein linkage regions.
6277894	8	108	theme	proposed	922:929	arg1	GalNAcol					983:990	Gal beta 1-4GlcNAc beta 1-6(Gal beta 1-3)GalNAcol	942:990	Gal beta 1-4GlcNAc beta 1-6(Gal beta 1-3)GalNAcol	942:990	The proposed structure, Gal beta 1-4GlcNAc beta 1-6(Gal beta 1-3)GalNAcol, has previously been found in human gastric, submaxillary, and ovarian cyst mucins in their carbohydrate-to-protein linkage regions.
6277894	12	109	dep	beta	1730:1733	arg1	GalNAcol					1786:1793	GlcNAc beta 1-6(Gal beta 1-3)GalNAcol	1757:1793	Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol	1713:1793	Two structures are consistent with the data obtained for A3: Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol and/or Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNac beta 1-6(Fuc alpha 1-2Gal beta 1-3)GalNacol.
6277894	12	109	dep	beta	1730:1733	arg1	beta					1840:1843	GlcNac beta 1-6	1833:1847	GlcNac beta 1-6	1833:1847	Two structures are consistent with the data obtained for A3: Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol and/or Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNac beta 1-6(Fuc alpha 1-2Gal beta 1-3)GalNacol.
6277894	0	110	theme	neutral	31:37	arg1	oligosaccharides					39:54	neutral oligosaccharides	31:54	neutral oligosaccharides of human midcycle cervical mucin	31:87	Structural characterization of neutral oligosaccharides of human midcycle cervical mucin.
6277894	9	111	theme	Gal	1191:1193	arg1	linkage					1210:1216	the Gal beta 1-4GlcNAc linkage	1187:1216	the Gal beta 1-4GlcNAc linkage in the intact tetrasaccharide	1187:1246	beta-Galactosidase from Aspergillus niger selectively cleaved the Gal beta 1-4GlcNAc linkage in the intact tetrasaccharide.
6277894	10	112	theme	beta	1355:1358	arg1	removal					1321:1327	prior removal	1315:1327	prior removal of the Gal beta 1-4GlcNAc beta 1-unit attached to 0-6 of GalNAcol	1315:1393	Enzymatic hydrolysis of the Gal beta 1-3GalNAcol linkage required prior removal of the Gal beta 1-4GlcNAc beta 1-unit attached to 0-6 of GalNAcol.
6277894	9	113	theme	1-4GlcNAc	1200:1208	arg1	linkage					1210:1216	the Gal beta 1-4GlcNAc linkage	1187:1216	the Gal beta 1-4GlcNAc linkage in the intact tetrasaccharide	1187:1246	beta-Galactosidase from Aspergillus niger selectively cleaved the Gal beta 1-4GlcNAc linkage in the intact tetrasaccharide.
6277894	8	114	theme	beta	946:949	arg1	beta					961:964	Gal beta 1-4GlcNAc beta 1-6	942:968	Gal beta 1-4GlcNAc beta 1-6(Gal beta 1-3)GalNAcol	942:990	The proposed structure, Gal beta 1-4GlcNAc beta 1-6(Gal beta 1-3)GalNAcol, has previously been found in human gastric, submaxillary, and ovarian cyst mucins in their carbohydrate-to-protein linkage regions.
6277894	8	114	theme	beta	946:949	arg1	beta					974:977	Gal beta 1-3	970:981	Gal beta 1-3	970:981	The proposed structure, Gal beta 1-4GlcNAc beta 1-6(Gal beta 1-3)GalNAcol, has previously been found in human gastric, submaxillary, and ovarian cyst mucins in their carbohydrate-to-protein linkage regions.
6277894	13	115	theme	human	1966:1970	arg1	oligosaccharides					1987:2002	the larger human cervical mucin oligosaccharides A2 and A3	1955:2012	the larger human cervical mucin oligosaccharides A2 and A3	1955:2012	The results indicate that A1 represents the "core" tetrasaccharide of the larger human cervical mucin oligosaccharides A2 and A3.
6277894	13	115	theme	human	1966:1970	arg1	A3					2011:2012	A3	2011:2012	A3	2011:2012	The results indicate that A1 represents the "core" tetrasaccharide of the larger human cervical mucin oligosaccharides A2 and A3.
6277894	13	115	theme	human	1966:1970	arg1	A2					2004:2005	A2	2004:2005	A2	2004:2005	The results indicate that A1 represents the "core" tetrasaccharide of the larger human cervical mucin oligosaccharides A2 and A3.
6277894	10	116	theme	beta	1340:1343	arg1	beta					1355:1358	the Gal beta 1-4GlcNAc beta 1-unit	1332:1365	the Gal beta 1-4GlcNAc beta 1-unit attached to 0-6 of GalNAcol	1332:1393	Enzymatic hydrolysis of the Gal beta 1-3GalNAcol linkage required prior removal of the Gal beta 1-4GlcNAc beta 1-unit attached to 0-6 of GalNAcol.
6277894	8	117	located	found	1013:1017	arg2	structure					931:939	The proposed structure	918:939	The proposed structure	918:939	The proposed structure, Gal beta 1-4GlcNAc beta 1-6(Gal beta 1-3)GalNAcol, has previously been found in human gastric, submaxillary, and ovarian cyst mucins in their carbohydrate-to-protein linkage regions.
6277894	8	117	located	found	1013:1017	arg1	mucins					1068:1073	human gastric, submaxillary, and ovarian cyst mucins	1022:1073	mucins	1068:1073	The proposed structure, Gal beta 1-4GlcNAc beta 1-6(Gal beta 1-3)GalNAcol, has previously been found in human gastric, submaxillary, and ovarian cyst mucins in their carbohydrate-to-protein linkage regions.
6277894	8	117	located	found	1013:1017	arg1	submaxillary					1037:1048	human gastric, submaxillary, and ovarian cyst mucins	1022:1073	submaxillary	1037:1048	The proposed structure, Gal beta 1-4GlcNAc beta 1-6(Gal beta 1-3)GalNAcol, has previously been found in human gastric, submaxillary, and ovarian cyst mucins in their carbohydrate-to-protein linkage regions.
6277894	8	117	located	found	1013:1017	arg2	GalNAcol					983:990	Gal beta 1-4GlcNAc beta 1-6(Gal beta 1-3)GalNAcol	942:990	Gal beta 1-4GlcNAc beta 1-6(Gal beta 1-3)GalNAcol	942:990	The proposed structure, Gal beta 1-4GlcNAc beta 1-6(Gal beta 1-3)GalNAcol, has previously been found in human gastric, submaxillary, and ovarian cyst mucins in their carbohydrate-to-protein linkage regions.
6277894	0	118	theme	midcycle	65:72	arg1	mucin					83:87	human midcycle cervical mucin	59:87	human midcycle cervical mucin	59:87	Structural characterization of neutral oligosaccharides of human midcycle cervical mucin.
6277894	8	119	theme	beta	961:964	arg1	structure					931:939	The proposed structure	918:939	The proposed structure	918:939	The proposed structure, Gal beta 1-4GlcNAc beta 1-6(Gal beta 1-3)GalNAcol, has previously been found in human gastric, submaxillary, and ovarian cyst mucins in their carbohydrate-to-protein linkage regions.
6277894	8	119	theme	beta	961:964	arg1	GalNAcol					983:990	Gal beta 1-4GlcNAc beta 1-6(Gal beta 1-3)GalNAcol	942:990	Gal beta 1-4GlcNAc beta 1-6(Gal beta 1-3)GalNAcol	942:990	The proposed structure, Gal beta 1-4GlcNAc beta 1-6(Gal beta 1-3)GalNAcol, has previously been found in human gastric, submaxillary, and ovarian cyst mucins in their carbohydrate-to-protein linkage regions.
6277894	4	120	theme	0:2:1:1	497:503	arg1	compositions					428:439	approximate compositions	416:439	approximate compositions of Fuc:Gal:GlcNAc:N-acetylgalactosaminitol (GalNAcol) = 0:2:1:1 (A1), 1:2:1:1 (A2), and 2:2:1:1 (A3)	416:540	Three major neutral oligosaccharides were isolated with approximate compositions of Fuc:Gal:GlcNAc:N-acetylgalactosaminitol (GalNAcol) = 0:2:1:1 (A1), 1:2:1:1 (A2), and 2:2:1:1 (A3).
6277894	12	121	theme	1-2Gal	1859:1864	arg1	beta					1730:1733	Fuc alpha 1-2Gal beta 1-4,3	1713:1739	Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol	1713:1793	Two structures are consistent with the data obtained for A3: Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol and/or Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNac beta 1-6(Fuc alpha 1-2Gal beta 1-3)GalNacol.
6277894	12	121	theme	1-2Gal	1859:1864	arg1	beta					1866:1869	Fuc alpha 1-2Gal beta 1-3	1849:1873	Fuc alpha 1-2Gal beta 1-3	1849:1873	Two structures are consistent with the data obtained for A3: Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol and/or Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNac beta 1-6(Fuc alpha 1-2Gal beta 1-3)GalNacol.
6277894	11	122	theme	3	1628:1628	arg1	ratio					1619:1623	an approximate molar ratio	1598:1623	an approximate molar ratio of 3 to 4:1	1598:1635	The data for A2 indicated a mixture of two oligosaccharides, Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNacol and Fuc alpha 1-2Gal beta 1-4GlcNac beta 1-6(Gal beta 1-3)-GalNacol, in an approximate molar ratio of 3 to 4:1, respectively.
6277894	9	123	theme	intact	1225:1230	arg1	tetrasaccharide					1232:1246	the intact tetrasaccharide	1221:1246	the intact tetrasaccharide	1221:1246	beta-Galactosidase from Aspergillus niger selectively cleaved the Gal beta 1-4GlcNAc linkage in the intact tetrasaccharide.
6277894	12	124	theme	GlcNac	1833:1838	arg1	beta					1840:1843	GlcNac beta 1-6	1833:1847	GlcNac beta 1-6	1833:1847	Two structures are consistent with the data obtained for A3: Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol and/or Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNac beta 1-6(Fuc alpha 1-2Gal beta 1-3)GalNacol.
6277894	11	125	theme	beta	1461:1464	arg1	1-3,4					1482:1486	Fuc alpha 1-3,4	1472:1486	Fuc alpha 1-3,4	1472:1486	The data for A2 indicated a mixture of two oligosaccharides, Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNacol and Fuc alpha 1-2Gal beta 1-4GlcNac beta 1-6(Gal beta 1-3)-GalNacol, in an approximate molar ratio of 3 to 4:1, respectively.
6277894	11	125	theme	beta	1461:1464	arg1	1-4,3					1466:1470	beta 1-4,3	1461:1470	Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNacol	1457:1524	The data for A2 indicated a mixture of two oligosaccharides, Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNacol and Fuc alpha 1-2Gal beta 1-4GlcNac beta 1-6(Gal beta 1-3)-GalNacol, in an approximate molar ratio of 3 to 4:1, respectively.
6277894	12	126	theme	alpha	1821:1825	arg1	1-3,4					1827:1831	Fuc alpha 1-3,4	1817:1831	Fuc alpha 1-3,4	1817:1831	Two structures are consistent with the data obtained for A3: Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol and/or Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNac beta 1-6(Fuc alpha 1-2Gal beta 1-3)GalNacol.
6277894	12	126	theme	alpha	1821:1825	arg1	beta					1806:1809	Gal beta 1-4,3	1802:1815	Gal beta 1-4,3(Fuc alpha 1-3,4)	1802:1832	Two structures are consistent with the data obtained for A3: Fuc alpha 1-2Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNAcol and/or Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNac beta 1-6(Fuc alpha 1-2Gal beta 1-3)GalNacol.
6277894	11	127	theme	alpha	1476:1480	arg1	1-3,4					1482:1486	Fuc alpha 1-3,4	1472:1486	Fuc alpha 1-3,4	1472:1486	The data for A2 indicated a mixture of two oligosaccharides, Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNacol and Fuc alpha 1-2Gal beta 1-4GlcNac beta 1-6(Gal beta 1-3)-GalNacol, in an approximate molar ratio of 3 to 4:1, respectively.
6277894	11	127	theme	alpha	1476:1480	arg1	1-4,3					1466:1470	beta 1-4,3	1461:1470	Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNacol	1457:1524	The data for A2 indicated a mixture of two oligosaccharides, Gal beta 1-4,3(Fuc alpha 1-3,4)GlcNAc beta 1-6(Gal beta 1-3)GalNacol and Fuc alpha 1-2Gal beta 1-4GlcNac beta 1-6(Gal beta 1-3)-GalNacol, in an approximate molar ratio of 3 to 4:1, respectively.
6277894	13	128	theme	core	1930:1933	arg1	tetrasaccharide					1936:1950	the "core" tetrasaccharide	1925:1950	the "core" tetrasaccharide of the larger human cervical mucin oligosaccharides A2 and A3	1925:2012	The results indicate that A1 represents the "core" tetrasaccharide of the larger human cervical mucin oligosaccharides A2 and A3.
6277894	1	129	theme	sulfated	255:262	arg1	oligosaccharides					264:279	reduced neutral, sialylated, and sulfated oligosaccharides	222:279	reduced neutral, sialylated, and sulfated oligosaccharides	222:279	It was previously shown that alkaline borohydride treatment of human midcycle cervical mucin releases a heterogeneous population of reduced neutral, sialylated, and sulfated oligosaccharides (Yurewicz, E. C., and Moghissi, K. S. (1981) J. Biol.
3029097	4	0	theme	sequential	748:757	arg1	separation					759:768	sequential separation	748:768	sequential separation	748:768	From this fraction, five short chain monosulfated oligosaccharides (S-I to S-V) were purified by sequential separation by SynChroprep AX300 anion exchange high pressure liquid chromatography, gel filtration on Bio-Gel P-2, and high voltage paper electrophoresis.
3029097	4	1	from	filtration	847:856	arg1	P-2					869:871	Bio-Gel P-2	861:871	Bio-Gel P-2	861:871	From this fraction, five short chain monosulfated oligosaccharides (S-I to S-V) were purified by sequential separation by SynChroprep AX300 anion exchange high pressure liquid chromatography, gel filtration on Bio-Gel P-2, and high voltage paper electrophoresis.
3029097	1	2	theme	tracheobronchial	180:195	arg1	glycoproteins					204:216	highly anionic tracheobronchial mucous glycoproteins	165:216	highly anionic tracheobronchial mucous glycoproteins	165:216	The structure of five sulfated oligosaccharide units of highly anionic tracheobronchial mucous glycoproteins, isolated from a cystic fibrosis patient's sputum, were established.
3029097	5	3	theme	affinity	1035:1042	arg1	chromatography					1044:1057	lectin affinity chromatography	1028:1057	lectin affinity chromatography	1028:1057	Based on the results of carbohydrate composition, sequential exoglycosidase degradation, permethylation analysis, lectin affinity chromatography, and periodate oxidation, the following structures (where GalNAcol is N-acetylgalactosaminitol) were proposed for these oligosaccharides.
3029097	1	4	gly	glycoproteins	204:216	arg1	glycoproteins					204:216	highly anionic tracheobronchial mucous glycoproteins	165:216	highly anionic tracheobronchial mucous glycoproteins	165:216	The structure of five sulfated oligosaccharide units of highly anionic tracheobronchial mucous glycoproteins, isolated from a cystic fibrosis patient's sputum, were established.
3029097	1	5	theme	mucous	197:202	arg1	glycoproteins					204:216	highly anionic tracheobronchial mucous glycoproteins	165:216	highly anionic tracheobronchial mucous glycoproteins	165:216	The structure of five sulfated oligosaccharide units of highly anionic tracheobronchial mucous glycoproteins, isolated from a cystic fibrosis patient's sputum, were established.
3029097	4	6	theme	exchange	797:804	arg1	chromatography					827:840	SynChroprep AX300 anion exchange high pressure liquid chromatography	773:840	SynChroprep AX300 anion exchange high pressure liquid chromatography	773:840	From this fraction, five short chain monosulfated oligosaccharides (S-I to S-V) were purified by sequential separation by SynChroprep AX300 anion exchange high pressure liquid chromatography, gel filtration on Bio-Gel P-2, and high voltage paper electrophoresis.
3029097	4	7	dep	S-V	726:728	arg1	to					723:724	to	723:724	to	723:724	From this fraction, five short chain monosulfated oligosaccharides (S-I to S-V) were purified by sequential separation by SynChroprep AX300 anion exchange high pressure liquid chromatography, gel filtration on Bio-Gel P-2, and high voltage paper electrophoresis.
3029097	3	8	theme	heterogeneous	586:598	arg1	mixture					600:606	a heterogeneous mixture	584:606	a heterogeneous mixture of sulfated oligosaccharides	584:635	Following the removal of acidic oligosaccharides possessing N-acetylneuraminic acid and L-fucose by lectin affinity chromatography a heterogeneous mixture of sulfated oligosaccharides was obtained.
3029097	4	9	theme	high	806:809	arg1	chromatography					827:840	SynChroprep AX300 anion exchange high pressure liquid chromatography	773:840	SynChroprep AX300 anion exchange high pressure liquid chromatography	773:840	From this fraction, five short chain monosulfated oligosaccharides (S-I to S-V) were purified by sequential separation by SynChroprep AX300 anion exchange high pressure liquid chromatography, gel filtration on Bio-Gel P-2, and high voltage paper electrophoresis.
3029097	3	10	theme	oligosaccharides	620:635	arg1	mixture					600:606	a heterogeneous mixture	584:606	a heterogeneous mixture of sulfated oligosaccharides	584:635	Following the removal of acidic oligosaccharides possessing N-acetylneuraminic acid and L-fucose by lectin affinity chromatography a heterogeneous mixture of sulfated oligosaccharides was obtained.
3029097	4	11	theme	chain	682:686	arg1	oligosaccharides					701:716	five short chain monosulfated oligosaccharides	671:716	five short chain monosulfated oligosaccharides (S-I to S-V)	671:729	From this fraction, five short chain monosulfated oligosaccharides (S-I to S-V) were purified by sequential separation by SynChroprep AX300 anion exchange high pressure liquid chromatography, gel filtration on Bio-Gel P-2, and high voltage paper electrophoresis.
3029097	4	11	theme	chain	682:686	arg1	S-V					726:728	S-I to S-V	719:728	S-I to S-V	719:728	From this fraction, five short chain monosulfated oligosaccharides (S-I to S-V) were purified by sequential separation by SynChroprep AX300 anion exchange high pressure liquid chromatography, gel filtration on Bio-Gel P-2, and high voltage paper electrophoresis.
3029097	4	12	theme	liquid	820:825	arg1	chromatography					827:840	SynChroprep AX300 anion exchange high pressure liquid chromatography	773:840	SynChroprep AX300 anion exchange high pressure liquid chromatography	773:840	From this fraction, five short chain monosulfated oligosaccharides (S-I to S-V) were purified by sequential separation by SynChroprep AX300 anion exchange high pressure liquid chromatography, gel filtration on Bio-Gel P-2, and high voltage paper electrophoresis.
3029097	4	13	from	chromatography	827:840	arg1	P-2					869:871	Bio-Gel P-2	861:871	Bio-Gel P-2	861:871	From this fraction, five short chain monosulfated oligosaccharides (S-I to S-V) were purified by sequential separation by SynChroprep AX300 anion exchange high pressure liquid chromatography, gel filtration on Bio-Gel P-2, and high voltage paper electrophoresis.
3029097	2	14	theme	acidic	379:384	arg1	oligosaccharides					386:401	the acidic oligosaccharides	375:401	the acidic oligosaccharides (63%)	375:407	Reduced oligosaccharides (84%) were released under alkaline borohydride conditions, and the acidic oligosaccharides (63%) were isolated by Dowex 1-X2 chromatography.
3029097	2	14	theme	acidic	379:384	arg1	%					406:406	63%	404:406	63%	404:406	Reduced oligosaccharides (84%) were released under alkaline borohydride conditions, and the acidic oligosaccharides (63%) were isolated by Dowex 1-X2 chromatography.
3029097	3	15	theme	N-acetylneuraminic	513:530	arg1	acid					532:535	N-acetylneuraminic acid	513:535	N-acetylneuraminic acid	513:535	Following the removal of acidic oligosaccharides possessing N-acetylneuraminic acid and L-fucose by lectin affinity chromatography a heterogeneous mixture of sulfated oligosaccharides was obtained.
3029097	3	16	contain	possessing	502:511	arg2	acid					532:535	N-acetylneuraminic acid	513:535	N-acetylneuraminic acid	513:535	Following the removal of acidic oligosaccharides possessing N-acetylneuraminic acid and L-fucose by lectin affinity chromatography a heterogeneous mixture of sulfated oligosaccharides was obtained.
3029097	3	16	contain	possessing	502:511	arg2	L-fucose					541:548	L-fucose	541:548	L-fucose	541:548	Following the removal of acidic oligosaccharides possessing N-acetylneuraminic acid and L-fucose by lectin affinity chromatography a heterogeneous mixture of sulfated oligosaccharides was obtained.
3029097	3	16	contain	possessing	502:511	arg1	oligosaccharides					485:500	acidic oligosaccharides	478:500	acidic oligosaccharides possessing N-acetylneuraminic acid and L-fucose	478:548	Following the removal of acidic oligosaccharides possessing N-acetylneuraminic acid and L-fucose by lectin affinity chromatography a heterogeneous mixture of sulfated oligosaccharides was obtained.
3029097	2	17	theme	Dowex	426:430	arg1	chromatography					437:450	Dowex 1-X2 chromatography	426:450	Dowex 1-X2 chromatography	426:450	Reduced oligosaccharides (84%) were released under alkaline borohydride conditions, and the acidic oligosaccharides (63%) were isolated by Dowex 1-X2 chromatography.
3029097	0	18	gly	glycoproteins	94:106	arg1	glycoproteins					94:106	tracheobronchial mucus glycoproteins	71:106	tracheobronchial mucus glycoproteins	71:106	Structure determination of five sulfated oligosaccharides derived from tracheobronchial mucus glycoproteins.
3029097	1	19	theme	glycoproteins	204:216	arg1	units					156:160	five sulfated oligosaccharide units	126:160	five sulfated oligosaccharide units	126:160	The structure of five sulfated oligosaccharide units of highly anionic tracheobronchial mucous glycoproteins, isolated from a cystic fibrosis patient's sputum, were established.
3029097	4	20	from	electrophoresis	897:911	arg1	P-2					869:871	Bio-Gel P-2	861:871	Bio-Gel P-2	861:871	From this fraction, five short chain monosulfated oligosaccharides (S-I to S-V) were purified by sequential separation by SynChroprep AX300 anion exchange high pressure liquid chromatography, gel filtration on Bio-Gel P-2, and high voltage paper electrophoresis.
3029097	4	21	theme	paper	891:895	arg1	electrophoresis					897:911	high voltage paper electrophoresis	878:911	high voltage paper electrophoresis	878:911	From this fraction, five short chain monosulfated oligosaccharides (S-I to S-V) were purified by sequential separation by SynChroprep AX300 anion exchange high pressure liquid chromatography, gel filtration on Bio-Gel P-2, and high voltage paper electrophoresis.
3029097	4	22	theme	monosulfated	688:699	arg1	oligosaccharides					701:716	five short chain monosulfated oligosaccharides	671:716	five short chain monosulfated oligosaccharides (S-I to S-V)	671:729	From this fraction, five short chain monosulfated oligosaccharides (S-I to S-V) were purified by sequential separation by SynChroprep AX300 anion exchange high pressure liquid chromatography, gel filtration on Bio-Gel P-2, and high voltage paper electrophoresis.
3029097	4	22	theme	monosulfated	688:699	arg1	S-V					726:728	S-I to S-V	719:728	S-I to S-V	719:728	From this fraction, five short chain monosulfated oligosaccharides (S-I to S-V) were purified by sequential separation by SynChroprep AX300 anion exchange high pressure liquid chromatography, gel filtration on Bio-Gel P-2, and high voltage paper electrophoresis.
3029097	5	23	theme	periodate	1064:1072	arg1	oxidation					1074:1082	periodate oxidation	1064:1082	periodate oxidation	1064:1082	Based on the results of carbohydrate composition, sequential exoglycosidase degradation, permethylation analysis, lectin affinity chromatography, and periodate oxidation, the following structures (where GalNAcol is N-acetylgalactosaminitol) were proposed for these oligosaccharides.
3029097	4	24	theme	S-I	719:721	arg1	oligosaccharides					701:716	five short chain monosulfated oligosaccharides	671:716	five short chain monosulfated oligosaccharides (S-I to S-V)	671:729	From this fraction, five short chain monosulfated oligosaccharides (S-I to S-V) were purified by sequential separation by SynChroprep AX300 anion exchange high pressure liquid chromatography, gel filtration on Bio-Gel P-2, and high voltage paper electrophoresis.
3029097	4	24	theme	S-I	719:721	arg1	S-V					726:728	S-I to S-V	719:728	S-I to S-V	719:728	From this fraction, five short chain monosulfated oligosaccharides (S-I to S-V) were purified by sequential separation by SynChroprep AX300 anion exchange high pressure liquid chromatography, gel filtration on Bio-Gel P-2, and high voltage paper electrophoresis.
3029097	3	25	theme	affinity	560:567	arg1	chromatography					569:582	lectin affinity chromatography	553:582	lectin affinity chromatography	553:582	Following the removal of acidic oligosaccharides possessing N-acetylneuraminic acid and L-fucose by lectin affinity chromatography a heterogeneous mixture of sulfated oligosaccharides was obtained.
3029097	2	26	theme	alkaline	338:345	arg1	conditions					359:368	alkaline borohydride conditions	338:368	alkaline borohydride conditions	338:368	Reduced oligosaccharides (84%) were released under alkaline borohydride conditions, and the acidic oligosaccharides (63%) were isolated by Dowex 1-X2 chromatography.
3029097	0	27	theme	Structure	0:8	arg1	determination					10:22	Structure determination	0:22	Structure determination of five sulfated oligosaccharides	0:56	Structure determination of five sulfated oligosaccharides derived from tracheobronchial mucus glycoproteins.
3029097	4	28	theme	SynChroprep	773:783	arg1	chromatography					827:840	SynChroprep AX300 anion exchange high pressure liquid chromatography	773:840	SynChroprep AX300 anion exchange high pressure liquid chromatography	773:840	From this fraction, five short chain monosulfated oligosaccharides (S-I to S-V) were purified by sequential separation by SynChroprep AX300 anion exchange high pressure liquid chromatography, gel filtration on Bio-Gel P-2, and high voltage paper electrophoresis.
3029097	4	29	theme	anion	791:795	arg1	chromatography					827:840	SynChroprep AX300 anion exchange high pressure liquid chromatography	773:840	SynChroprep AX300 anion exchange high pressure liquid chromatography	773:840	From this fraction, five short chain monosulfated oligosaccharides (S-I to S-V) were purified by sequential separation by SynChroprep AX300 anion exchange high pressure liquid chromatography, gel filtration on Bio-Gel P-2, and high voltage paper electrophoresis.
3029097	5	30	theme	sequential	964:973	arg1	degradation					990:1000	sequential exoglycosidase degradation	964:1000	sequential exoglycosidase degradation	964:1000	Based on the results of carbohydrate composition, sequential exoglycosidase degradation, permethylation analysis, lectin affinity chromatography, and periodate oxidation, the following structures (where GalNAcol is N-acetylgalactosaminitol) were proposed for these oligosaccharides.
3029097	3	31	theme	oligosaccharides	485:500	arg1	removal					467:473	the removal	463:473	the removal of acidic oligosaccharides possessing N-acetylneuraminic acid and L-fucose by lectin affinity chromatography	463:582	Following the removal of acidic oligosaccharides possessing N-acetylneuraminic acid and L-fucose by lectin affinity chromatography a heterogeneous mixture of sulfated oligosaccharides was obtained.
3029097	5	32	theme	permethylation	1003:1016	arg1	analysis					1018:1025	permethylation analysis	1003:1025	permethylation analysis	1003:1025	Based on the results of carbohydrate composition, sequential exoglycosidase degradation, permethylation analysis, lectin affinity chromatography, and periodate oxidation, the following structures (where GalNAcol is N-acetylgalactosaminitol) were proposed for these oligosaccharides.
3029097	4	33	theme	pressure	811:818	arg1	chromatography					827:840	SynChroprep AX300 anion exchange high pressure liquid chromatography	773:840	SynChroprep AX300 anion exchange high pressure liquid chromatography	773:840	From this fraction, five short chain monosulfated oligosaccharides (S-I to S-V) were purified by sequential separation by SynChroprep AX300 anion exchange high pressure liquid chromatography, gel filtration on Bio-Gel P-2, and high voltage paper electrophoresis.
3029097	2	34	theme	1-X2	432:435	arg1	chromatography					437:450	Dowex 1-X2 chromatography	426:450	Dowex 1-X2 chromatography	426:450	Reduced oligosaccharides (84%) were released under alkaline borohydride conditions, and the acidic oligosaccharides (63%) were isolated by Dowex 1-X2 chromatography.
3029097	4	35	theme	gel	843:845	arg1	filtration					847:856	gel filtration	843:856	gel filtration on Bio-Gel P-2	843:871	From this fraction, five short chain monosulfated oligosaccharides (S-I to S-V) were purified by sequential separation by SynChroprep AX300 anion exchange high pressure liquid chromatography, gel filtration on Bio-Gel P-2, and high voltage paper electrophoresis.
3029097	3	36	theme	sulfated	611:618	arg1	oligosaccharides					620:635	sulfated oligosaccharides	611:635	sulfated oligosaccharides	611:635	Following the removal of acidic oligosaccharides possessing N-acetylneuraminic acid and L-fucose by lectin affinity chromatography a heterogeneous mixture of sulfated oligosaccharides was obtained.
3029097	1	37	theme	cystic	235:240	arg1	sputum					261:266	a cystic fibrosis patient's sputum	233:266	a cystic fibrosis patient's sputum	233:266	The structure of five sulfated oligosaccharide units of highly anionic tracheobronchial mucous glycoproteins, isolated from a cystic fibrosis patient's sputum, were established.
3029097	0	38	theme	oligosaccharides	41:56	arg1	determination					10:22	Structure determination	0:22	Structure determination of five sulfated oligosaccharides	0:56	Structure determination of five sulfated oligosaccharides derived from tracheobronchial mucus glycoproteins.
3029097	5	39	theme	chromatography	1044:1057	arg1	results					927:933	the results	923:933	the results of carbohydrate composition, sequential exoglycosidase degradation, permethylation analysis, lectin affinity chromatography, and periodate oxidation	923:1082	Based on the results of carbohydrate composition, sequential exoglycosidase degradation, permethylation analysis, lectin affinity chromatography, and periodate oxidation, the following structures (where GalNAcol is N-acetylgalactosaminitol) were proposed for these oligosaccharides.
3029097	1	40	theme	fibrosis	242:249	arg1	sputum					261:266	a cystic fibrosis patient's sputum	233:266	a cystic fibrosis patient's sputum	233:266	The structure of five sulfated oligosaccharide units of highly anionic tracheobronchial mucous glycoproteins, isolated from a cystic fibrosis patient's sputum, were established.
3029097	0	41	theme	sulfated	32:39	arg1	oligosaccharides					41:56	five sulfated oligosaccharides	27:56	five sulfated oligosaccharides	27:56	Structure determination of five sulfated oligosaccharides derived from tracheobronchial mucus glycoproteins.
3029097	5	42	theme	degradation	990:1000	arg1	results					927:933	the results	923:933	the results of carbohydrate composition, sequential exoglycosidase degradation, permethylation analysis, lectin affinity chromatography, and periodate oxidation	923:1082	Based on the results of carbohydrate composition, sequential exoglycosidase degradation, permethylation analysis, lectin affinity chromatography, and periodate oxidation, the following structures (where GalNAcol is N-acetylgalactosaminitol) were proposed for these oligosaccharides.
3029097	5	43	theme	carbohydrate	938:949	arg1	composition					951:961	carbohydrate composition	938:961	carbohydrate composition	938:961	Based on the results of carbohydrate composition, sequential exoglycosidase degradation, permethylation analysis, lectin affinity chromatography, and periodate oxidation, the following structures (where GalNAcol is N-acetylgalactosaminitol) were proposed for these oligosaccharides.
3029097	4	44	theme	voltage	883:889	arg1	electrophoresis					897:911	high voltage paper electrophoresis	878:911	high voltage paper electrophoresis	878:911	From this fraction, five short chain monosulfated oligosaccharides (S-I to S-V) were purified by sequential separation by SynChroprep AX300 anion exchange high pressure liquid chromatography, gel filtration on Bio-Gel P-2, and high voltage paper electrophoresis.
3029097	1	45	theme	sulfated	131:138	arg1	units					156:160	five sulfated oligosaccharide units	126:160	five sulfated oligosaccharide units	126:160	The structure of five sulfated oligosaccharide units of highly anionic tracheobronchial mucous glycoproteins, isolated from a cystic fibrosis patient's sputum, were established.
3029097	4	46	theme	high	878:881	arg1	electrophoresis					897:911	high voltage paper electrophoresis	878:911	high voltage paper electrophoresis	878:911	From this fraction, five short chain monosulfated oligosaccharides (S-I to S-V) were purified by sequential separation by SynChroprep AX300 anion exchange high pressure liquid chromatography, gel filtration on Bio-Gel P-2, and high voltage paper electrophoresis.
3029097	1	47	theme	oligosaccharide	140:154	arg1	units					156:160	five sulfated oligosaccharide units	126:160	five sulfated oligosaccharide units	126:160	The structure of five sulfated oligosaccharide units of highly anionic tracheobronchial mucous glycoproteins, isolated from a cystic fibrosis patient's sputum, were established.
3029097	5	48	theme	following	1089:1097	arg1	structures					1099:1108	the following structures	1085:1108	the following structures (where GalNAcol is N-acetylgalactosaminitol)	1085:1153	Based on the results of carbohydrate composition, sequential exoglycosidase degradation, permethylation analysis, lectin affinity chromatography, and periodate oxidation, the following structures (where GalNAcol is N-acetylgalactosaminitol) were proposed for these oligosaccharides.
3029097	5	49	theme	analysis	1018:1025	arg1	results					927:933	the results	923:933	the results of carbohydrate composition, sequential exoglycosidase degradation, permethylation analysis, lectin affinity chromatography, and periodate oxidation	923:1082	Based on the results of carbohydrate composition, sequential exoglycosidase degradation, permethylation analysis, lectin affinity chromatography, and periodate oxidation, the following structures (where GalNAcol is N-acetylgalactosaminitol) were proposed for these oligosaccharides.
3029097	5	50	theme	oxidation	1074:1082	arg1	results					927:933	the results	923:933	the results of carbohydrate composition, sequential exoglycosidase degradation, permethylation analysis, lectin affinity chromatography, and periodate oxidation	923:1082	Based on the results of carbohydrate composition, sequential exoglycosidase degradation, permethylation analysis, lectin affinity chromatography, and periodate oxidation, the following structures (where GalNAcol is N-acetylgalactosaminitol) were proposed for these oligosaccharides.
3029097	1	51	theme	units	156:160	arg1	structure					113:121	The structure	109:121	The structure of five sulfated oligosaccharide units of highly anionic tracheobronchial mucous glycoproteins, isolated from a cystic fibrosis patient's sputum,	109:267	The structure of five sulfated oligosaccharide units of highly anionic tracheobronchial mucous glycoproteins, isolated from a cystic fibrosis patient's sputum, were established.
3029097	5	52	theme	lectin	1028:1033	arg1	chromatography					1044:1057	lectin affinity chromatography	1028:1057	lectin affinity chromatography	1028:1057	Based on the results of carbohydrate composition, sequential exoglycosidase degradation, permethylation analysis, lectin affinity chromatography, and periodate oxidation, the following structures (where GalNAcol is N-acetylgalactosaminitol) were proposed for these oligosaccharides.
3029097	5	53	theme	exoglycosidase	975:988	arg1	degradation					990:1000	sequential exoglycosidase degradation	964:1000	sequential exoglycosidase degradation	964:1000	Based on the results of carbohydrate composition, sequential exoglycosidase degradation, permethylation analysis, lectin affinity chromatography, and periodate oxidation, the following structures (where GalNAcol is N-acetylgalactosaminitol) were proposed for these oligosaccharides.
3029097	2	54	theme	Reduced	287:293	arg1	%					315:315	84%	313:315	84%	313:315	Reduced oligosaccharides (84%) were released under alkaline borohydride conditions, and the acidic oligosaccharides (63%) were isolated by Dowex 1-X2 chromatography.
3029097	2	54	theme	Reduced	287:293	arg1	oligosaccharides					295:310	Reduced oligosaccharides	287:310	Reduced oligosaccharides (84%)	287:316	Reduced oligosaccharides (84%) were released under alkaline borohydride conditions, and the acidic oligosaccharides (63%) were isolated by Dowex 1-X2 chromatography.
3029097	2	55	theme	borohydride	347:357	arg1	conditions					359:368	alkaline borohydride conditions	338:368	alkaline borohydride conditions	338:368	Reduced oligosaccharides (84%) were released under alkaline borohydride conditions, and the acidic oligosaccharides (63%) were isolated by Dowex 1-X2 chromatography.
3029097	0	56	theme	mucus	88:92	arg1	glycoproteins					94:106	tracheobronchial mucus glycoproteins	71:106	tracheobronchial mucus glycoproteins	71:106	Structure determination of five sulfated oligosaccharides derived from tracheobronchial mucus glycoproteins.
3029097	5	57	theme	composition	951:961	arg1	results					927:933	the results	923:933	the results of carbohydrate composition, sequential exoglycosidase degradation, permethylation analysis, lectin affinity chromatography, and periodate oxidation	923:1082	Based on the results of carbohydrate composition, sequential exoglycosidase degradation, permethylation analysis, lectin affinity chromatography, and periodate oxidation, the following structures (where GalNAcol is N-acetylgalactosaminitol) were proposed for these oligosaccharides.
3029097	3	58	theme	acidic	478:483	arg1	oligosaccharides					485:500	acidic oligosaccharides	478:500	acidic oligosaccharides possessing N-acetylneuraminic acid and L-fucose	478:548	Following the removal of acidic oligosaccharides possessing N-acetylneuraminic acid and L-fucose by lectin affinity chromatography a heterogeneous mixture of sulfated oligosaccharides was obtained.
3029097	3	59	theme	lectin	553:558	arg1	chromatography					569:582	lectin affinity chromatography	553:582	lectin affinity chromatography	553:582	Following the removal of acidic oligosaccharides possessing N-acetylneuraminic acid and L-fucose by lectin affinity chromatography a heterogeneous mixture of sulfated oligosaccharides was obtained.
3029097	4	60	theme	short	676:680	arg1	oligosaccharides					701:716	five short chain monosulfated oligosaccharides	671:716	five short chain monosulfated oligosaccharides (S-I to S-V)	671:729	From this fraction, five short chain monosulfated oligosaccharides (S-I to S-V) were purified by sequential separation by SynChroprep AX300 anion exchange high pressure liquid chromatography, gel filtration on Bio-Gel P-2, and high voltage paper electrophoresis.
3029097	4	60	theme	short	676:680	arg1	S-V					726:728	S-I to S-V	719:728	S-I to S-V	719:728	From this fraction, five short chain monosulfated oligosaccharides (S-I to S-V) were purified by sequential separation by SynChroprep AX300 anion exchange high pressure liquid chromatography, gel filtration on Bio-Gel P-2, and high voltage paper electrophoresis.
3029097	0	61	theme	tracheobronchial	71:86	arg1	glycoproteins					94:106	tracheobronchial mucus glycoproteins	71:106	tracheobronchial mucus glycoproteins	71:106	Structure determination of five sulfated oligosaccharides derived from tracheobronchial mucus glycoproteins.
3029097	4	62	theme	Bio-Gel	861:867	arg1	P-2					869:871	Bio-Gel P-2	861:871	Bio-Gel P-2	861:871	From this fraction, five short chain monosulfated oligosaccharides (S-I to S-V) were purified by sequential separation by SynChroprep AX300 anion exchange high pressure liquid chromatography, gel filtration on Bio-Gel P-2, and high voltage paper electrophoresis.
3029097	1	63	theme	anionic	172:178	arg1	glycoproteins					204:216	highly anionic tracheobronchial mucous glycoproteins	165:216	highly anionic tracheobronchial mucous glycoproteins	165:216	The structure of five sulfated oligosaccharide units of highly anionic tracheobronchial mucous glycoproteins, isolated from a cystic fibrosis patient's sputum, were established.
9677337	4	0	theme	biantennary	713:723	arg1	structure					725:733	predominantly biantennary structure	699:733	predominantly biantennary structure linked to asparagine residues at positions 256 and 559 respectively	699:801	H1 carries two complex-type N-glycans of predominantly biantennary structure linked to asparagine residues at positions 256 and 559 respectively.
9677337	5	1	theme	complex-type	859:870	arg1	oligosaccharides					821:836	the oligosaccharides	817:836	the oligosaccharides attached to H2	817:851	In contrast, the oligosaccharides attached to H2 are a complex-type N-glycan in the N-terminal region of the protein (Asn64) and three to four type-1 core-structure O-glycans mono- or di-sialylated, clustered in the C-terminal region.
9677337	5	1	theme	complex-type	859:870	arg1	N-glycan					872:879	a complex-type N-glycan	857:879	a complex-type N-glycan	857:879	In contrast, the oligosaccharides attached to H2 are a complex-type N-glycan in the N-terminal region of the protein (Asn64) and three to four type-1 core-structure O-glycans mono- or di-sialylated, clustered in the C-terminal region.
9677337	5	2	theme	mono-	979:983	arg1	region					899:904	the N-terminal region	884:904	the N-terminal region of the protein (Asn64) and three to four type-1 core-structure O-glycans mono- or di-sialylated	884:1000	In contrast, the oligosaccharides attached to H2 are a complex-type N-glycan in the N-terminal region of the protein (Asn64) and three to four type-1 core-structure O-glycans mono- or di-sialylated, clustered in the C-terminal region.
9677337	7	3	theme	biological	1138:1147	arg1	implications					1149:1160	The biological implications	1134:1160	The biological implications	1134:1160	The biological implications of this hypothesis, notably for the biosynthetic pathway of IalphaI, are discussed.
9677337	2	4	theme	specific	347:354	arg1	properties					356:365	specific properties	347:365	specific properties	347:365	It consists of three polypeptide chains covalently linked by a glycosaminoglycan chain: a light chain named bikunin carrying the anti-proteinase activity and two heavy chains, H1 and H2, which exhibit specific properties, e.g. they interact with hyaluronan thus stabilizing the extracellular matrix.
9677337	2	5	contain	carrying	262:269	arg2	activity					291:298	anti-proteinase activity	275:298	anti-proteinase activity	275:298	It consists of three polypeptide chains covalently linked by a glycosaminoglycan chain: a light chain named bikunin carrying the anti-proteinase activity and two heavy chains, H1 and H2, which exhibit specific properties, e.g. they interact with hyaluronan thus stabilizing the extracellular matrix.
9677337	2	5	contain	carrying	262:269	arg2	H1					322:323	H1	322:323	H1	322:323	It consists of three polypeptide chains covalently linked by a glycosaminoglycan chain: a light chain named bikunin carrying the anti-proteinase activity and two heavy chains, H1 and H2, which exhibit specific properties, e.g. they interact with hyaluronan thus stabilizing the extracellular matrix.
9677337	2	5	contain	carrying	262:269	arg2	chains					314:319	two heavy chains	304:319	two heavy chains	304:319	It consists of three polypeptide chains covalently linked by a glycosaminoglycan chain: a light chain named bikunin carrying the anti-proteinase activity and two heavy chains, H1 and H2, which exhibit specific properties, e.g. they interact with hyaluronan thus stabilizing the extracellular matrix.
9677337	2	5	contain	carrying	262:269	arg1	bikunin					254:260	bikunin	254:260	bikunin carrying the anti-proteinase activity and two heavy chains, H1 and H2, which exhibit specific properties, e.g. they interact with hyaluronan thus stabilizing the extracellular matrix	254:443	It consists of three polypeptide chains covalently linked by a glycosaminoglycan chain: a light chain named bikunin carrying the anti-proteinase activity and two heavy chains, H1 and H2, which exhibit specific properties, e.g. they interact with hyaluronan thus stabilizing the extracellular matrix.
9677337	2	5	contain	carrying	262:269	arg2	H2					329:330	H2	329:330	H2	329:330	It consists of three polypeptide chains covalently linked by a glycosaminoglycan chain: a light chain named bikunin carrying the anti-proteinase activity and two heavy chains, H1 and H2, which exhibit specific properties, e.g. they interact with hyaluronan thus stabilizing the extracellular matrix.
9677337	3	6	theme	heavy	644:648	arg1	chains					650:655	both heavy chains	639:655	both heavy chains	639:655	In this study, using matrix-assisted laser desorption ionization-time-of-flight MS and amino acid sequencing of tryptic peptides, we provide a detailed analysis of the glycosylation pattern of both heavy chains.
9677337	2	7	theme	heavy	308:312	arg1	H2					329:330	H2	329:330	H2	329:330	It consists of three polypeptide chains covalently linked by a glycosaminoglycan chain: a light chain named bikunin carrying the anti-proteinase activity and two heavy chains, H1 and H2, which exhibit specific properties, e.g. they interact with hyaluronan thus stabilizing the extracellular matrix.
9677337	2	7	theme	heavy	308:312	arg1	H1					322:323	H1	322:323	H1	322:323	It consists of three polypeptide chains covalently linked by a glycosaminoglycan chain: a light chain named bikunin carrying the anti-proteinase activity and two heavy chains, H1 and H2, which exhibit specific properties, e.g. they interact with hyaluronan thus stabilizing the extracellular matrix.
9677337	2	7	theme	heavy	308:312	arg1	chains					314:319	two heavy chains	304:319	two heavy chains	304:319	It consists of three polypeptide chains covalently linked by a glycosaminoglycan chain: a light chain named bikunin carrying the anti-proteinase activity and two heavy chains, H1 and H2, which exhibit specific properties, e.g. they interact with hyaluronan thus stabilizing the extracellular matrix.
9677337	4	8	theme	complex-type	673:684	arg1	N-glycans					686:694	two complex-type N-glycans	669:694	two complex-type N-glycans of predominantly biantennary structure linked to asparagine residues at positions 256 and 559 respectively	669:801	H1 carries two complex-type N-glycans of predominantly biantennary structure linked to asparagine residues at positions 256 and 559 respectively.
9677337	7	9	theme	IalphaI	1222:1228	arg1	pathway					1211:1217	the biosynthetic pathway	1194:1217	the biosynthetic pathway of IalphaI	1194:1228	The biological implications of this hypothesis, notably for the biosynthetic pathway of IalphaI, are discussed.
9677337	2	10	theme	polypeptide	167:177	arg1	chains					179:184	three polypeptide chains	161:184	three polypeptide chains covalently linked by a glycosaminoglycan chain	161:231	It consists of three polypeptide chains covalently linked by a glycosaminoglycan chain: a light chain named bikunin carrying the anti-proteinase activity and two heavy chains, H1 and H2, which exhibit specific properties, e.g. they interact with hyaluronan thus stabilizing the extracellular matrix.
9677337	5	11	dep	four	942:945	arg1	to					939:940	to	939:940	to	939:940	In contrast, the oligosaccharides attached to H2 are a complex-type N-glycan in the N-terminal region of the protein (Asn64) and three to four type-1 core-structure O-glycans mono- or di-sialylated, clustered in the C-terminal region.
9677337	5	12	theme	di-sialylated	988:1000	arg1	region					899:904	the N-terminal region	884:904	the N-terminal region of the protein (Asn64) and three to four type-1 core-structure O-glycans mono- or di-sialylated	884:1000	In contrast, the oligosaccharides attached to H2 are a complex-type N-glycan in the N-terminal region of the protein (Asn64) and three to four type-1 core-structure O-glycans mono- or di-sialylated, clustered in the C-terminal region.
9677337	4	13	dep	positions	768:776	arg1	559					786:788	559	786:788	559	786:788	H1 carries two complex-type N-glycans of predominantly biantennary structure linked to asparagine residues at positions 256 and 559 respectively.
9677337	4	13	dep	positions	768:776	arg1	256					778:780	256	778:780	256	778:780	H1 carries two complex-type N-glycans of predominantly biantennary structure linked to asparagine residues at positions 256 and 559 respectively.
9677337	4	14	theme	structure	725:733	arg1	N-glycans					686:694	two complex-type N-glycans	669:694	two complex-type N-glycans of predominantly biantennary structure linked to asparagine residues at positions 256 and 559 respectively	669:801	H1 carries two complex-type N-glycans of predominantly biantennary structure linked to asparagine residues at positions 256 and 559 respectively.
9677337	3	15	theme	ionization-time-of-flight	500:524	arg1	MS					526:527	matrix-assisted laser desorption ionization-time-of-flight MS	467:527	matrix-assisted laser desorption ionization-time-of-flight MS	467:527	In this study, using matrix-assisted laser desorption ionization-time-of-flight MS and amino acid sequencing of tryptic peptides, we provide a detailed analysis of the glycosylation pattern of both heavy chains.
9677337	2	16	dep	carrying	262:269	arg1	interact					378:385	interact	378:385	interact with hyaluronan thus stabilizing the extracellular matrix	378:443	It consists of three polypeptide chains covalently linked by a glycosaminoglycan chain: a light chain named bikunin carrying the anti-proteinase activity and two heavy chains, H1 and H2, which exhibit specific properties, e.g. they interact with hyaluronan thus stabilizing the extracellular matrix.
9677337	3	17	theme	tryptic	558:564	arg1	peptides					566:573	tryptic peptides	558:573	tryptic peptides	558:573	In this study, using matrix-assisted laser desorption ionization-time-of-flight MS and amino acid sequencing of tryptic peptides, we provide a detailed analysis of the glycosylation pattern of both heavy chains.
9677337	6	18	theme	recognition	1091:1101	arg1	O-glycans					1061:1069	these O-glycans	1055:1069	these O-glycans	1055:1069	We propose that these O-glycans might function as a recognition signal for the H2 heavy chain.
9677337	6	18	theme	recognition	1091:1101	arg1	signal					1103:1108	a recognition signal	1089:1108	a recognition signal for the H2 heavy chain	1089:1131	We propose that these O-glycans might function as a recognition signal for the H2 heavy chain.
9677337	4	19	attach	linked	735:740	arg1	residues					756:763	asparagine residues	745:763	asparagine residues at positions 256 and 559 respectively	745:801	H1 carries two complex-type N-glycans of predominantly biantennary structure linked to asparagine residues at positions 256 and 559 respectively.
9677337	4	19	attach	linked	735:740	arg2	structure					725:733	predominantly biantennary structure	699:733	predominantly biantennary structure linked to asparagine residues at positions 256 and 559 respectively	699:801	H1 carries two complex-type N-glycans of predominantly biantennary structure linked to asparagine residues at positions 256 and 559 respectively.
9677337	5	20	theme	C-terminal	1020:1029	arg1	region					1031:1036	the C-terminal region	1016:1036	the C-terminal region	1016:1036	In contrast, the oligosaccharides attached to H2 are a complex-type N-glycan in the N-terminal region of the protein (Asn64) and three to four type-1 core-structure O-glycans mono- or di-sialylated, clustered in the C-terminal region.
9677337	5	21	theme	type-1	947:952	arg1	O-glycans					969:977	three to four type-1 core-structure O-glycans	933:977	three to four type-1 core-structure O-glycans	933:977	In contrast, the oligosaccharides attached to H2 are a complex-type N-glycan in the N-terminal region of the protein (Asn64) and three to four type-1 core-structure O-glycans mono- or di-sialylated, clustered in the C-terminal region.
9677337	0	22	theme	Glycosylation	0:12	arg1	pattern					14:20	Glycosylation pattern	0:20	Glycosylation pattern of human inter-alpha-inhibitor heavy chains	0:64	Glycosylation pattern of human inter-alpha-inhibitor heavy chains.
9677337	5	23	attach	attached	838:845	arg1	H2					850:851	H2	850:851	H2	850:851	In contrast, the oligosaccharides attached to H2 are a complex-type N-glycan in the N-terminal region of the protein (Asn64) and three to four type-1 core-structure O-glycans mono- or di-sialylated, clustered in the C-terminal region.
9677337	5	23	attach	attached	838:845	arg2	N-glycan					872:879	a complex-type N-glycan	857:879	a complex-type N-glycan	857:879	In contrast, the oligosaccharides attached to H2 are a complex-type N-glycan in the N-terminal region of the protein (Asn64) and three to four type-1 core-structure O-glycans mono- or di-sialylated, clustered in the C-terminal region.
9677337	5	23	attach	attached	838:845	arg2	oligosaccharides					821:836	the oligosaccharides	817:836	the oligosaccharides attached to H2	817:851	In contrast, the oligosaccharides attached to H2 are a complex-type N-glycan in the N-terminal region of the protein (Asn64) and three to four type-1 core-structure O-glycans mono- or di-sialylated, clustered in the C-terminal region.
9677337	3	24	theme	detailed	589:596	arg1	analysis					598:605	a detailed analysis	587:605	a detailed analysis of the glycosylation pattern of both heavy chains	587:655	In this study, using matrix-assisted laser desorption ionization-time-of-flight MS and amino acid sequencing of tryptic peptides, we provide a detailed analysis of the glycosylation pattern of both heavy chains.
9677337	0	25	theme	human	25:29	arg1	chains					59:64	human inter-alpha-inhibitor heavy chains	25:64	human inter-alpha-inhibitor heavy chains	25:64	Glycosylation pattern of human inter-alpha-inhibitor heavy chains.
9677337	2	26	dep	consists	149:156	arg1	chain					242:246	a light chain	234:246	a light chain named bikunin carrying the anti-proteinase activity and two heavy chains, H1 and H2, which exhibit specific properties, e.g. they interact with hyaluronan thus stabilizing the extracellular matrix	234:443	It consists of three polypeptide chains covalently linked by a glycosaminoglycan chain: a light chain named bikunin carrying the anti-proteinase activity and two heavy chains, H1 and H2, which exhibit specific properties, e.g. they interact with hyaluronan thus stabilizing the extracellular matrix.
9677337	4	27	from	positions	768:776	arg1	residues					756:763	asparagine residues	745:763	asparagine residues at positions 256 and 559 respectively	745:801	H1 carries two complex-type N-glycans of predominantly biantennary structure linked to asparagine residues at positions 256 and 559 respectively.
9677337	5	28	theme	O-glycans	969:977	arg1	region					899:904	the N-terminal region	884:904	the N-terminal region of the protein (Asn64) and three to four type-1 core-structure O-glycans mono- or di-sialylated	884:1000	In contrast, the oligosaccharides attached to H2 are a complex-type N-glycan in the N-terminal region of the protein (Asn64) and three to four type-1 core-structure O-glycans mono- or di-sialylated, clustered in the C-terminal region.
9677337	3	29	gly	glycosylation	614:626	arg1	chains					650:655	both heavy chains	639:655	both heavy chains	639:655	In this study, using matrix-assisted laser desorption ionization-time-of-flight MS and amino acid sequencing of tryptic peptides, we provide a detailed analysis of the glycosylation pattern of both heavy chains.
9677337	5	30	theme	core-structure	954:967	arg1	O-glycans					969:977	three to four type-1 core-structure O-glycans	933:977	three to four type-1 core-structure O-glycans	933:977	In contrast, the oligosaccharides attached to H2 are a complex-type N-glycan in the N-terminal region of the protein (Asn64) and three to four type-1 core-structure O-glycans mono- or di-sialylated, clustered in the C-terminal region.
9677337	1	31	theme	plasma	110:115	arg1	inhibitor					135:143	a plasma serine-proteinase inhibitor	108:143	a plasma serine-proteinase inhibitor	108:143	Human inter-alpha-inhibitor (IalphaI) is a plasma serine-proteinase inhibitor.
9677337	1	31	theme	plasma	110:115	arg1	inter-alpha-inhibitor					73:93	Human inter-alpha-inhibitor	67:93	Human inter-alpha-inhibitor (IalphaI)	67:103	Human inter-alpha-inhibitor (IalphaI) is a plasma serine-proteinase inhibitor.
9677337	3	32	theme	matrix-assisted	467:481	arg1	MS					526:527	matrix-assisted laser desorption ionization-time-of-flight MS	467:527	matrix-assisted laser desorption ionization-time-of-flight MS	467:527	In this study, using matrix-assisted laser desorption ionization-time-of-flight MS and amino acid sequencing of tryptic peptides, we provide a detailed analysis of the glycosylation pattern of both heavy chains.
9677337	0	33	theme	heavy	53:57	arg1	chains					59:64	human inter-alpha-inhibitor heavy chains	25:64	human inter-alpha-inhibitor heavy chains	25:64	Glycosylation pattern of human inter-alpha-inhibitor heavy chains.
9677337	7	34	theme	biosynthetic	1198:1209	arg1	pathway					1211:1217	the biosynthetic pathway	1194:1217	the biosynthetic pathway of IalphaI	1194:1228	The biological implications of this hypothesis, notably for the biosynthetic pathway of IalphaI, are discussed.
9677337	4	35	contain	carries	661:667	arg1	H1					658:659	H1	658:659	H1	658:659	H1 carries two complex-type N-glycans of predominantly biantennary structure linked to asparagine residues at positions 256 and 559 respectively.
9677337	4	35	contain	carries	661:667	arg2	N-glycans					686:694	two complex-type N-glycans	669:694	two complex-type N-glycans of predominantly biantennary structure linked to asparagine residues at positions 256 and 559 respectively	669:801	H1 carries two complex-type N-glycans of predominantly biantennary structure linked to asparagine residues at positions 256 and 559 respectively.
9677337	0	36	theme	inter-alpha-inhibitor	31:51	arg1	chains					59:64	human inter-alpha-inhibitor heavy chains	25:64	human inter-alpha-inhibitor heavy chains	25:64	Glycosylation pattern of human inter-alpha-inhibitor heavy chains.
9677337	7	37	theme	hypothesis	1170:1179	arg1	implications					1149:1160	The biological implications	1134:1160	The biological implications	1134:1160	The biological implications of this hypothesis, notably for the biosynthetic pathway of IalphaI, are discussed.
9677337	3	38	theme	chains	650:655	arg1	pattern					628:634	the glycosylation pattern	610:634	the glycosylation pattern of both heavy chains	610:655	In this study, using matrix-assisted laser desorption ionization-time-of-flight MS and amino acid sequencing of tryptic peptides, we provide a detailed analysis of the glycosylation pattern of both heavy chains.
9677337	3	39	theme	glycosylation	614:626	arg1	pattern					628:634	the glycosylation pattern	610:634	the glycosylation pattern of both heavy chains	610:655	In this study, using matrix-assisted laser desorption ionization-time-of-flight MS and amino acid sequencing of tryptic peptides, we provide a detailed analysis of the glycosylation pattern of both heavy chains.
9677337	5	40	theme	protein	913:919	arg1	region					899:904	the N-terminal region	884:904	the N-terminal region of the protein (Asn64) and three to four type-1 core-structure O-glycans mono- or di-sialylated	884:1000	In contrast, the oligosaccharides attached to H2 are a complex-type N-glycan in the N-terminal region of the protein (Asn64) and three to four type-1 core-structure O-glycans mono- or di-sialylated, clustered in the C-terminal region.
9677337	2	41	theme	light	236:240	arg1	chain					242:246	a light chain	234:246	a light chain named bikunin carrying the anti-proteinase activity and two heavy chains, H1 and H2, which exhibit specific properties, e.g. they interact with hyaluronan thus stabilizing the extracellular matrix	234:443	It consists of three polypeptide chains covalently linked by a glycosaminoglycan chain: a light chain named bikunin carrying the anti-proteinase activity and two heavy chains, H1 and H2, which exhibit specific properties, e.g. they interact with hyaluronan thus stabilizing the extracellular matrix.
9677337	6	42	theme	heavy	1121:1125	arg1	chain					1127:1131	the H2 heavy chain	1114:1131	the H2 heavy chain	1114:1131	We propose that these O-glycans might function as a recognition signal for the H2 heavy chain.
9677337	1	43	theme	serine-proteinase	117:133	arg1	inhibitor					135:143	a plasma serine-proteinase inhibitor	108:143	a plasma serine-proteinase inhibitor	108:143	Human inter-alpha-inhibitor (IalphaI) is a plasma serine-proteinase inhibitor.
9677337	1	43	theme	serine-proteinase	117:133	arg1	inter-alpha-inhibitor					73:93	Human inter-alpha-inhibitor	67:93	Human inter-alpha-inhibitor (IalphaI)	67:103	Human inter-alpha-inhibitor (IalphaI) is a plasma serine-proteinase inhibitor.
9677337	0	44	theme	chains	59:64	arg1	pattern					14:20	Glycosylation pattern	0:20	Glycosylation pattern of human inter-alpha-inhibitor heavy chains	0:64	Glycosylation pattern of human inter-alpha-inhibitor heavy chains.
9677337	3	45	theme	amino	533:537	arg1	sequencing					544:553	amino acid sequencing	533:553	amino acid sequencing of tryptic peptides	533:573	In this study, using matrix-assisted laser desorption ionization-time-of-flight MS and amino acid sequencing of tryptic peptides, we provide a detailed analysis of the glycosylation pattern of both heavy chains.
9677337	4	46	theme	asparagine	745:754	arg1	residues					756:763	asparagine residues	745:763	asparagine residues at positions 256 and 559 respectively	745:801	H1 carries two complex-type N-glycans of predominantly biantennary structure linked to asparagine residues at positions 256 and 559 respectively.
9677337	2	47	theme	anti-proteinase	275:289	arg1	activity					291:298	anti-proteinase activity	275:298	anti-proteinase activity	275:298	It consists of three polypeptide chains covalently linked by a glycosaminoglycan chain: a light chain named bikunin carrying the anti-proteinase activity and two heavy chains, H1 and H2, which exhibit specific properties, e.g. they interact with hyaluronan thus stabilizing the extracellular matrix.
9677337	5	48	from	N-glycan	872:879	arg1	region					899:904	the N-terminal region	884:904	the N-terminal region of the protein (Asn64) and three to four type-1 core-structure O-glycans mono- or di-sialylated	884:1000	In contrast, the oligosaccharides attached to H2 are a complex-type N-glycan in the N-terminal region of the protein (Asn64) and three to four type-1 core-structure O-glycans mono- or di-sialylated, clustered in the C-terminal region.
9677337	5	48	from	N-glycan	872:879	arg1	contrast					807:814	contrast	807:814	contrast	807:814	In contrast, the oligosaccharides attached to H2 are a complex-type N-glycan in the N-terminal region of the protein (Asn64) and three to four type-1 core-structure O-glycans mono- or di-sialylated, clustered in the C-terminal region.
9677337	3	49	theme	laser	483:487	arg1	MS					526:527	matrix-assisted laser desorption ionization-time-of-flight MS	467:527	matrix-assisted laser desorption ionization-time-of-flight MS	467:527	In this study, using matrix-assisted laser desorption ionization-time-of-flight MS and amino acid sequencing of tryptic peptides, we provide a detailed analysis of the glycosylation pattern of both heavy chains.
9677337	2	50	theme	glycosaminoglycan	209:225	arg1	chain					227:231	a glycosaminoglycan chain	207:231	a glycosaminoglycan chain	207:231	It consists of three polypeptide chains covalently linked by a glycosaminoglycan chain: a light chain named bikunin carrying the anti-proteinase activity and two heavy chains, H1 and H2, which exhibit specific properties, e.g. they interact with hyaluronan thus stabilizing the extracellular matrix.
9677337	1	51	theme	Human	67:71	arg1	IalphaI					96:102	IalphaI	96:102	IalphaI	96:102	Human inter-alpha-inhibitor (IalphaI) is a plasma serine-proteinase inhibitor.
9677337	1	51	theme	Human	67:71	arg1	inter-alpha-inhibitor					73:93	Human inter-alpha-inhibitor	67:93	Human inter-alpha-inhibitor (IalphaI)	67:103	Human inter-alpha-inhibitor (IalphaI) is a plasma serine-proteinase inhibitor.
9677337	1	51	theme	Human	67:71	arg1	inhibitor					135:143	a plasma serine-proteinase inhibitor	108:143	a plasma serine-proteinase inhibitor	108:143	Human inter-alpha-inhibitor (IalphaI) is a plasma serine-proteinase inhibitor.
9677337	5	52	theme	N-terminal	888:897	arg1	region					899:904	the N-terminal region	884:904	the N-terminal region of the protein (Asn64) and three to four type-1 core-structure O-glycans mono- or di-sialylated	884:1000	In contrast, the oligosaccharides attached to H2 are a complex-type N-glycan in the N-terminal region of the protein (Asn64) and three to four type-1 core-structure O-glycans mono- or di-sialylated, clustered in the C-terminal region.
9677337	3	53	theme	desorption	489:498	arg1	MS					526:527	matrix-assisted laser desorption ionization-time-of-flight MS	467:527	matrix-assisted laser desorption ionization-time-of-flight MS	467:527	In this study, using matrix-assisted laser desorption ionization-time-of-flight MS and amino acid sequencing of tryptic peptides, we provide a detailed analysis of the glycosylation pattern of both heavy chains.
9677337	5	54	gly	di-sialylated	988:1000	arg1	region					899:904	the N-terminal region	884:904	the N-terminal region of the protein (Asn64) and three to four type-1 core-structure O-glycans mono- or di-sialylated	884:1000	In contrast, the oligosaccharides attached to H2 are a complex-type N-glycan in the N-terminal region of the protein (Asn64) and three to four type-1 core-structure O-glycans mono- or di-sialylated, clustered in the C-terminal region.
9677337	6	55	theme	H2	1118:1119	arg1	chain					1127:1131	the H2 heavy chain	1114:1131	the H2 heavy chain	1114:1131	We propose that these O-glycans might function as a recognition signal for the H2 heavy chain.
9677337	3	56	theme	pattern	628:634	arg1	analysis					598:605	a detailed analysis	587:605	a detailed analysis of the glycosylation pattern of both heavy chains	587:655	In this study, using matrix-assisted laser desorption ionization-time-of-flight MS and amino acid sequencing of tryptic peptides, we provide a detailed analysis of the glycosylation pattern of both heavy chains.
9677337	2	57	theme	extracellular	424:436	arg1	matrix					438:443	the extracellular matrix	420:443	the extracellular matrix	420:443	It consists of three polypeptide chains covalently linked by a glycosaminoglycan chain: a light chain named bikunin carrying the anti-proteinase activity and two heavy chains, H1 and H2, which exhibit specific properties, e.g. they interact with hyaluronan thus stabilizing the extracellular matrix.
9677337	3	58	theme	acid	539:542	arg1	sequencing					544:553	amino acid sequencing	533:553	amino acid sequencing of tryptic peptides	533:573	In this study, using matrix-assisted laser desorption ionization-time-of-flight MS and amino acid sequencing of tryptic peptides, we provide a detailed analysis of the glycosylation pattern of both heavy chains.
9677337	3	59	theme	peptides	566:573	arg1	MS					526:527	matrix-assisted laser desorption ionization-time-of-flight MS	467:527	matrix-assisted laser desorption ionization-time-of-flight MS	467:527	In this study, using matrix-assisted laser desorption ionization-time-of-flight MS and amino acid sequencing of tryptic peptides, we provide a detailed analysis of the glycosylation pattern of both heavy chains.
9677337	3	59	theme	peptides	566:573	arg1	sequencing					544:553	amino acid sequencing	533:553	amino acid sequencing of tryptic peptides	533:573	In this study, using matrix-assisted laser desorption ionization-time-of-flight MS and amino acid sequencing of tryptic peptides, we provide a detailed analysis of the glycosylation pattern of both heavy chains.
9677337	2	60	dep	activity	291:298	arg1	the					271:273	the	271:273	the	271:273	It consists of three polypeptide chains covalently linked by a glycosaminoglycan chain: a light chain named bikunin carrying the anti-proteinase activity and two heavy chains, H1 and H2, which exhibit specific properties, e.g. they interact with hyaluronan thus stabilizing the extracellular matrix.
6547160	12	0	from	three	1914:1918	arg1	Lymphocytes					1897:1907	Lymphocytes	1897:1907	Lymphocytes from three of these patients	1897:1936	Lymphocytes from three of these patients displayed an abnormal 125I-component of apparent mol wt 135,000.
6547160	2	1	with	labeling	406:413	arg1	methionine					425:434	[35S]methionine	420:434	[35S]methionine	420:434	The glycoprotein nature of gpL115 is demonstrated through labeling in carbohydrate moieties by [3H]NaBH4 and its synthesis by lymphocytes through labeling with [35S]methionine.
6547160	9	2	theme	desialylated	1632:1643	arg1	species					1645:1651	partially desialylated species	1622:1651	partially desialylated species of decreasing electrophoretic mobility	1622:1690	On treatment with limiting sialidase concentrations, gpL115 of normal lymphocytes is transformed into a series of partially desialylated species of decreasing electrophoretic mobility.
6547160	4	3	theme	disaccharide	674:685	arg1	1-3GalNAc					696:704	the disaccharide Gal beta 1-3GalNAc	670:704	the disaccharide Gal beta 1-3GalNAc	670:704	When tested on peanut lectin, which shows specificity for the disaccharide Gal beta 1-3GalNAc, gpL115 is nonadherent and sialidase-treated gpL115 is adherent, indicating the presence of the sequence sialic acid-Gal beta 1-3GalNAc, which is characteristic for O-linked (mucin-type, acidic-type) carbohydrates.
6547160	2	4	theme	gpL115	287:292	arg1	nature					277:282	The glycoprotein nature	260:282	The glycoprotein nature of gpL115	260:292	The glycoprotein nature of gpL115 is demonstrated through labeling in carbohydrate moieties by [3H]NaBH4 and its synthesis by lymphocytes through labeling with [35S]methionine.
6547160	4	5	theme	beta	691:694	arg1	1-3GalNAc					696:704	the disaccharide Gal beta 1-3GalNAc	670:704	the disaccharide Gal beta 1-3GalNAc	670:704	When tested on peanut lectin, which shows specificity for the disaccharide Gal beta 1-3GalNAc, gpL115 is nonadherent and sialidase-treated gpL115 is adherent, indicating the presence of the sequence sialic acid-Gal beta 1-3GalNAc, which is characteristic for O-linked (mucin-type, acidic-type) carbohydrates.
6547160	2	6	theme	carbohydrate	330:341	arg1	moieties					343:350	carbohydrate moieties	330:350	carbohydrate moieties	330:350	The glycoprotein nature of gpL115 is demonstrated through labeling in carbohydrate moieties by [3H]NaBH4 and its synthesis by lymphocytes through labeling with [35S]methionine.
6547160	1	7	theme	X-chromosome-linked	192:210	arg1	6					256:256	6	256:256	6	256:256	gpL115 is a lymphocyte surface component that is deficient in patients with the X-chromosome-linked immune deficiency Wiskott-Aldrich syndrome (6).
6547160	1	7	theme	X-chromosome-linked	192:210	arg1	syndrome					246:253	the X-chromosome-linked immune deficiency Wiskott-Aldrich syndrome	188:253	the X-chromosome-linked immune deficiency Wiskott-Aldrich syndrome (6)	188:257	gpL115 is a lymphocyte surface component that is deficient in patients with the X-chromosome-linked immune deficiency Wiskott-Aldrich syndrome (6).
6547160	2	8	gly	glycoprotein	264:275	arg1	glycoprotein					264:275	The glycoprotein nature	260:282	The glycoprotein nature of gpL115	260:292	The glycoprotein nature of gpL115 is demonstrated through labeling in carbohydrate moieties by [3H]NaBH4 and its synthesis by lymphocytes through labeling with [35S]methionine.
6547160	9	9	theme	limiting	1526:1533	arg1	concentrations					1545:1558	limiting sialidase concentrations	1526:1558	limiting sialidase concentrations	1526:1558	On treatment with limiting sialidase concentrations, gpL115 of normal lymphocytes is transformed into a series of partially desialylated species of decreasing electrophoretic mobility.
6547160	8	10	theme	carbohydrate	1494:1505	arg1	quantities					1471:1480	significant quantities	1459:1480	significant quantities of O-linked carbohydrate	1459:1505	Cumulatively, these findings indicate that gpL115 , like glycophorin of erythrocytes and GPIb of platelets, is a sialoglyco protein with significant quantities of O-linked carbohydrate.
6547160	4	11	link	O-linked	871:878	arg1	carbohydrates					906:918	O-linked (mucin-type, acidic-type) carbohydrates	871:918	O-linked (mucin-type, acidic-type) carbohydrates	871:918	When tested on peanut lectin, which shows specificity for the disaccharide Gal beta 1-3GalNAc, gpL115 is nonadherent and sialidase-treated gpL115 is adherent, indicating the presence of the sequence sialic acid-Gal beta 1-3GalNAc, which is characteristic for O-linked (mucin-type, acidic-type) carbohydrates.
6547160	7	12	theme	gpL115	1182:1187	arg1	Sialidase-treatment					1159:1177	Sialidase-treatment	1159:1177	Sialidase-treatment of gpL115	1159:1187	Sialidase-treatment of gpL115 significantly alters its physical properties, reducing its electrophoretic mobility and changing its behavior on isoelectrofocusing.
6547160	1	13	theme	lymphocyte	124:133	arg1	deficient					161:169	deficient	161:169	deficient	161:169	gpL115 is a lymphocyte surface component that is deficient in patients with the X-chromosome-linked immune deficiency Wiskott-Aldrich syndrome (6).
6547160	1	13	theme	lymphocyte	124:133	arg1	component					143:151	a lymphocyte surface component	122:151	a lymphocyte surface component that is deficient in patients with the X-chromosome-linked immune deficiency Wiskott-Aldrich syndrome (6)	122:257	gpL115 is a lymphocyte surface component that is deficient in patients with the X-chromosome-linked immune deficiency Wiskott-Aldrich syndrome (6).
6547160	1	13	theme	lymphocyte	124:133	arg1	gpL115					112:117	gpL115	112:117	gpL115	112:117	gpL115 is a lymphocyte surface component that is deficient in patients with the X-chromosome-linked immune deficiency Wiskott-Aldrich syndrome (6).
6547160	11	14	from	deficient	1862:1870	arg1	gpL115					1888:1893	125I-labeled gpL115	1875:1893	125I-labeled gpL115	1875:1893	Lymphocytes of eight Wiskott-Aldrich syndrome patients were found to be deficient in 125I-labeled gpL115 .
6547160	9	15	theme	normal	1571:1576	arg1	lymphocytes					1578:1588	normal lymphocytes	1571:1588	normal lymphocytes	1571:1588	On treatment with limiting sialidase concentrations, gpL115 of normal lymphocytes is transformed into a series of partially desialylated species of decreasing electrophoretic mobility.
6547160	0	16	from	syndrome	102:109	arg1	sialoglycoprotein					47:63	a human lymphocyte surface sialoglycoprotein	20:63	a human lymphocyte surface sialoglycoprotein that is defective in Wiskott-Aldrich syndrome	20:109	Characterization of a human lymphocyte surface sialoglycoprotein that is defective in Wiskott-Aldrich syndrome.
6547160	0	16	from	syndrome	102:109	arg1	defective					73:81	defective	73:81	defective	73:81	Characterization of a human lymphocyte surface sialoglycoprotein that is defective in Wiskott-Aldrich syndrome.
6547160	1	17	from	patients	174:181	arg1	gpL115					112:117	gpL115	112:117	gpL115	112:117	gpL115 is a lymphocyte surface component that is deficient in patients with the X-chromosome-linked immune deficiency Wiskott-Aldrich syndrome (6).
6547160	1	17	from	patients	174:181	arg1	component					143:151	a lymphocyte surface component	122:151	a lymphocyte surface component that is deficient in patients with the X-chromosome-linked immune deficiency Wiskott-Aldrich syndrome (6)	122:257	gpL115 is a lymphocyte surface component that is deficient in patients with the X-chromosome-linked immune deficiency Wiskott-Aldrich syndrome (6).
6547160	1	17	from	patients	174:181	arg1	deficient					161:169	deficient	161:169	deficient	161:169	gpL115 is a lymphocyte surface component that is deficient in patients with the X-chromosome-linked immune deficiency Wiskott-Aldrich syndrome (6).
6547160	4	18	dep	carbohydrates	906:918	arg1	acidic-type					893:903	acidic-type	893:903	acidic-type	893:903	When tested on peanut lectin, which shows specificity for the disaccharide Gal beta 1-3GalNAc, gpL115 is nonadherent and sialidase-treated gpL115 is adherent, indicating the presence of the sequence sialic acid-Gal beta 1-3GalNAc, which is characteristic for O-linked (mucin-type, acidic-type) carbohydrates.
6547160	4	18	dep	carbohydrates	906:918	arg1	mucin-type					881:890	mucin-type	881:890	mucin-type	881:890	When tested on peanut lectin, which shows specificity for the disaccharide Gal beta 1-3GalNAc, gpL115 is nonadherent and sialidase-treated gpL115 is adherent, indicating the presence of the sequence sialic acid-Gal beta 1-3GalNAc, which is characteristic for O-linked (mucin-type, acidic-type) carbohydrates.
6547160	1	19	from	deficient	161:169	arg1	patients					174:181	patients	174:181	patients with the X-chromosome-linked immune deficiency Wiskott-Aldrich syndrome (6)	174:257	gpL115 is a lymphocyte surface component that is deficient in patients with the X-chromosome-linked immune deficiency Wiskott-Aldrich syndrome (6).
6547160	5	20	theme	surface	923:929	arg1	glycoprotein					931:942	A surface glycoprotein	921:942	A surface glycoprotein with all the above characteristics	921:977	A surface glycoprotein with all the above characteristics was found on the lymphoblastoid cell line CEM.
6547160	7	21	dep	alters	1203:1208	arg1	changing					1277:1284	changing	1277:1284	changing its behavior on isoelectrofocusing	1277:1319	Sialidase-treatment of gpL115 significantly alters its physical properties, reducing its electrophoretic mobility and changing its behavior on isoelectrofocusing.
6547160	7	21	dep	alters	1203:1208	arg1	reducing					1235:1242	reducing	1235:1242	reducing its electrophoretic mobility	1235:1271	Sialidase-treatment of gpL115 significantly alters its physical properties, reducing its electrophoretic mobility and changing its behavior on isoelectrofocusing.
6547160	8	22	theme	erythrocytes	1394:1405	arg1	GPIb					1411:1414	GPIb	1411:1414	GPIb of platelets	1411:1427	Cumulatively, these findings indicate that gpL115 , like glycophorin of erythrocytes and GPIb of platelets, is a sialoglyco protein with significant quantities of O-linked carbohydrate.
6547160	8	22	theme	erythrocytes	1394:1405	arg1	glycophorin					1379:1389	glycophorin	1379:1389	glycophorin of erythrocytes	1379:1405	Cumulatively, these findings indicate that gpL115 , like glycophorin of erythrocytes and GPIb of platelets, is a sialoglyco protein with significant quantities of O-linked carbohydrate.
6547160	11	23	theme	125I-labeled	1875:1886	arg1	gpL115					1888:1893	125I-labeled gpL115	1875:1893	125I-labeled gpL115	1875:1893	Lymphocytes of eight Wiskott-Aldrich syndrome patients were found to be deficient in 125I-labeled gpL115 .
6547160	5	24	theme	cell	1011:1014	arg1	CEM					1021:1023	the lymphoblastoid cell line CEM	992:1023	the lymphoblastoid cell line CEM	992:1023	A surface glycoprotein with all the above characteristics was found on the lymphoblastoid cell line CEM.
6547160	5	25	with	glycoprotein	931:942	arg1	characteristics					963:977	all the above characteristics	949:977	all the above characteristics	949:977	A surface glycoprotein with all the above characteristics was found on the lymphoblastoid cell line CEM.
6547160	8	26	theme	platelets	1419:1427	arg1	GPIb					1411:1414	GPIb	1411:1414	GPIb of platelets	1411:1427	Cumulatively, these findings indicate that gpL115 , like glycophorin of erythrocytes and GPIb of platelets, is a sialoglyco protein with significant quantities of O-linked carbohydrate.
6547160	8	26	theme	platelets	1419:1427	arg1	glycophorin					1379:1389	glycophorin	1379:1389	glycophorin of erythrocytes	1379:1405	Cumulatively, these findings indicate that gpL115 , like glycophorin of erythrocytes and GPIb of platelets, is a sialoglyco protein with significant quantities of O-linked carbohydrate.
6547160	3	27	theme	Native	437:442	arg1	gpL115					444:449	Native gpL115	437:449	Native gpL115	437:449	Native gpL115 adheres to wheat germ lectin-Sepharose and sialidase-treated gpL115 does not adhere, indicating that native gpL115 adheres via clusters of sialic acid residues.
6547160	9	28	theme	species	1645:1651	arg1	series					1612:1617	a series	1610:1617	a series of partially desialylated species of decreasing electrophoretic mobility	1610:1690	On treatment with limiting sialidase concentrations, gpL115 of normal lymphocytes is transformed into a series of partially desialylated species of decreasing electrophoretic mobility.
6547160	6	29	theme	monoclonal	1075:1084	arg1	L10					1095:1097	the monoclonal antibody L10	1071:1097	the monoclonal antibody L10	1071:1097	CEM cells were used as immunogen to generate the monoclonal antibody L10, an IgG1, which binds native and sialidase-treated gpL115 .
6547160	6	29	theme	monoclonal	1075:1084	arg1	IgG1					1103:1106	an IgG1	1100:1106	an IgG1	1100:1106	CEM cells were used as immunogen to generate the monoclonal antibody L10, an IgG1, which binds native and sialidase-treated gpL115 .
6547160	12	30	theme	wt	1991:1992	arg1	125I-component					1960:1973	an abnormal 125I-component	1948:1973	an abnormal 125I-component of apparent mol wt 135,000	1948:2000	Lymphocytes from three of these patients displayed an abnormal 125I-component of apparent mol wt 135,000.
6547160	3	31	theme	wheat	462:466	arg1	lectin-Sepharose					473:488	wheat germ lectin-Sepharose	462:488	wheat germ lectin-Sepharose	462:488	Native gpL115 adheres to wheat germ lectin-Sepharose and sialidase-treated gpL115 does not adhere, indicating that native gpL115 adheres via clusters of sialic acid residues.
6547160	8	32	theme	sialoglyco	1435:1444	arg1	protein					1446:1452	a sialoglyco protein	1433:1452	a sialoglyco protein with significant quantities of O-linked carbohydrate	1433:1505	Cumulatively, these findings indicate that gpL115 , like glycophorin of erythrocytes and GPIb of platelets, is a sialoglyco protein with significant quantities of O-linked carbohydrate.
6547160	8	32	theme	sialoglyco	1435:1444	arg1	gpL115					1365:1370	gpL115	1365:1370	gpL115	1365:1370	Cumulatively, these findings indicate that gpL115 , like glycophorin of erythrocytes and GPIb of platelets, is a sialoglyco protein with significant quantities of O-linked carbohydrate.
6547160	10	33	theme	syndrome	1771:1778	arg1	patients					1780:1787	some Wiskott-Aldrich syndrome patients	1750:1787	some Wiskott-Aldrich syndrome patients	1750:1787	This finding resembles the situation with lymphocytes of some Wiskott-Aldrich syndrome patients.
6547160	0	34	theme	lymphocyte	28:37	arg1	sialoglycoprotein					47:63	a human lymphocyte surface sialoglycoprotein	20:63	a human lymphocyte surface sialoglycoprotein that is defective in Wiskott-Aldrich syndrome	20:109	Characterization of a human lymphocyte surface sialoglycoprotein that is defective in Wiskott-Aldrich syndrome.
6547160	0	34	theme	lymphocyte	28:37	arg1	defective					73:81	defective	73:81	defective	73:81	Characterization of a human lymphocyte surface sialoglycoprotein that is defective in Wiskott-Aldrich syndrome.
6547160	9	35	gly	desialylated	1632:1643	arg1	species					1645:1651	partially desialylated species	1622:1651	partially desialylated species of decreasing electrophoretic mobility	1622:1690	On treatment with limiting sialidase concentrations, gpL115 of normal lymphocytes is transformed into a series of partially desialylated species of decreasing electrophoretic mobility.
6547160	0	36	theme	sialoglycoprotein	47:63	arg1	Characterization					0:15	Characterization	0:15	Characterization of a human lymphocyte surface sialoglycoprotein that is defective in Wiskott-Aldrich syndrome.	0:110	Characterization of a human lymphocyte surface sialoglycoprotein that is defective in Wiskott-Aldrich syndrome.
6547160	5	37	located	found	983:987	arg1	CEM					1021:1023	the lymphoblastoid cell line CEM	992:1023	the lymphoblastoid cell line CEM	992:1023	A surface glycoprotein with all the above characteristics was found on the lymphoblastoid cell line CEM.
6547160	5	37	located	found	983:987	arg2	glycoprotein					931:942	A surface glycoprotein	921:942	A surface glycoprotein with all the above characteristics	921:977	A surface glycoprotein with all the above characteristics was found on the lymphoblastoid cell line CEM.
6547160	12	38	theme	abnormal	1951:1958	arg1	125I-component					1960:1973	an abnormal 125I-component	1948:1973	an abnormal 125I-component of apparent mol wt 135,000	1948:2000	Lymphocytes from three of these patients displayed an abnormal 125I-component of apparent mol wt 135,000.
6547160	4	39	theme	sialic	811:816	arg1	characteristic					852:865	characteristic	852:865	characteristic	852:865	When tested on peanut lectin, which shows specificity for the disaccharide Gal beta 1-3GalNAc, gpL115 is nonadherent and sialidase-treated gpL115 is adherent, indicating the presence of the sequence sialic acid-Gal beta 1-3GalNAc, which is characteristic for O-linked (mucin-type, acidic-type) carbohydrates.
6547160	4	39	theme	sialic	811:816	arg1	1-3GalNAc					832:840	the sequence sialic acid-Gal beta 1-3GalNAc	798:840	the sequence sialic acid-Gal beta 1-3GalNAc	798:840	When tested on peanut lectin, which shows specificity for the disaccharide Gal beta 1-3GalNAc, gpL115 is nonadherent and sialidase-treated gpL115 is adherent, indicating the presence of the sequence sialic acid-Gal beta 1-3GalNAc, which is characteristic for O-linked (mucin-type, acidic-type) carbohydrates.
6547160	3	40	theme	sialidase-treated	494:510	arg1	gpL115					512:517	sialidase-treated gpL115	494:517	sialidase-treated gpL115	494:517	Native gpL115 adheres to wheat germ lectin-Sepharose and sialidase-treated gpL115 does not adhere, indicating that native gpL115 adheres via clusters of sialic acid residues.
6547160	12	41	theme	apparent	1978:1985	arg1	wt					1991:1992	apparent mol wt 135,000	1978:2000	apparent mol wt 135,000	1978:2000	Lymphocytes from three of these patients displayed an abnormal 125I-component of apparent mol wt 135,000.
6547160	2	42	theme	[35S	420:423	arg1	methionine					425:434	[35S]methionine	420:434	[35S]methionine	420:434	The glycoprotein nature of gpL115 is demonstrated through labeling in carbohydrate moieties by [3H]NaBH4 and its synthesis by lymphocytes through labeling with [35S]methionine.
6547160	8	43	theme	O-linked	1485:1492	arg1	carbohydrate					1494:1505	O-linked carbohydrate	1485:1505	O-linked carbohydrate	1485:1505	Cumulatively, these findings indicate that gpL115 , like glycophorin of erythrocytes and GPIb of platelets, is a sialoglyco protein with significant quantities of O-linked carbohydrate.
6547160	10	44	with	situation	1720:1728	arg1	lymphocytes					1735:1745	lymphocytes	1735:1745	lymphocytes of some Wiskott-Aldrich syndrome patients	1735:1787	This finding resembles the situation with lymphocytes of some Wiskott-Aldrich syndrome patients.
6547160	7	45	from	behavior	1290:1297	arg1	isoelectrofocusing					1302:1319	isoelectrofocusing	1302:1319	isoelectrofocusing	1302:1319	Sialidase-treatment of gpL115 significantly alters its physical properties, reducing its electrophoretic mobility and changing its behavior on isoelectrofocusing.
6547160	3	46	theme	native	552:557	arg1	gpL115					559:564	native gpL115	552:564	native gpL115	552:564	Native gpL115 adheres to wheat germ lectin-Sepharose and sialidase-treated gpL115 does not adhere, indicating that native gpL115 adheres via clusters of sialic acid residues.
6547160	8	47	link	O-linked	1485:1492	arg1	carbohydrate					1494:1505	O-linked carbohydrate	1485:1505	O-linked carbohydrate	1485:1505	Cumulatively, these findings indicate that gpL115 , like glycophorin of erythrocytes and GPIb of platelets, is a sialoglyco protein with significant quantities of O-linked carbohydrate.
6547160	7	48	theme	electrophoretic	1248:1262	arg1	mobility					1264:1271	its electrophoretic mobility	1244:1271	its electrophoretic mobility	1244:1271	Sialidase-treatment of gpL115 significantly alters its physical properties, reducing its electrophoretic mobility and changing its behavior on isoelectrofocusing.
6547160	6	49	used	used	1041:1044	arg2	immunogen					1049:1057	immunogen	1049:1057	immunogen	1049:1057	CEM cells were used as immunogen to generate the monoclonal antibody L10, an IgG1, which binds native and sialidase-treated gpL115 .
6547160	6	49	used	used	1041:1044	arg2	cells					1030:1034	CEM cells	1026:1034	CEM cells	1026:1034	CEM cells were used as immunogen to generate the monoclonal antibody L10, an IgG1, which binds native and sialidase-treated gpL115 .
6547160	3	50	theme	sialic	590:595	arg1	residues					602:609	sialic acid residues	590:609	sialic acid residues	590:609	Native gpL115 adheres to wheat germ lectin-Sepharose and sialidase-treated gpL115 does not adhere, indicating that native gpL115 adheres via clusters of sialic acid residues.
6547160	4	51	theme	O-linked	871:878	arg1	carbohydrates					906:918	O-linked (mucin-type, acidic-type) carbohydrates	871:918	O-linked (mucin-type, acidic-type) carbohydrates	871:918	When tested on peanut lectin, which shows specificity for the disaccharide Gal beta 1-3GalNAc, gpL115 is nonadherent and sialidase-treated gpL115 is adherent, indicating the presence of the sequence sialic acid-Gal beta 1-3GalNAc, which is characteristic for O-linked (mucin-type, acidic-type) carbohydrates.
6547160	4	52	theme	Gal	687:689	arg1	1-3GalNAc					696:704	the disaccharide Gal beta 1-3GalNAc	670:704	the disaccharide Gal beta 1-3GalNAc	670:704	When tested on peanut lectin, which shows specificity for the disaccharide Gal beta 1-3GalNAc, gpL115 is nonadherent and sialidase-treated gpL115 is adherent, indicating the presence of the sequence sialic acid-Gal beta 1-3GalNAc, which is characteristic for O-linked (mucin-type, acidic-type) carbohydrates.
6547160	8	53	with	protein	1446:1452	arg1	quantities					1471:1480	significant quantities	1459:1480	significant quantities of O-linked carbohydrate	1459:1505	Cumulatively, these findings indicate that gpL115 , like glycophorin of erythrocytes and GPIb of platelets, is a sialoglyco protein with significant quantities of O-linked carbohydrate.
6547160	1	54	theme	immune	212:217	arg1	6					256:256	6	256:256	6	256:256	gpL115 is a lymphocyte surface component that is deficient in patients with the X-chromosome-linked immune deficiency Wiskott-Aldrich syndrome (6).
6547160	1	54	theme	immune	212:217	arg1	syndrome					246:253	the X-chromosome-linked immune deficiency Wiskott-Aldrich syndrome	188:253	the X-chromosome-linked immune deficiency Wiskott-Aldrich syndrome (6)	188:257	gpL115 is a lymphocyte surface component that is deficient in patients with the X-chromosome-linked immune deficiency Wiskott-Aldrich syndrome (6).
6547160	3	55	theme	acid	597:600	arg1	residues					602:609	sialic acid residues	590:609	sialic acid residues	590:609	Native gpL115 adheres to wheat germ lectin-Sepharose and sialidase-treated gpL115 does not adhere, indicating that native gpL115 adheres via clusters of sialic acid residues.
6547160	5	56	gly	glycoprotein	931:942	arg1	glycoprotein					931:942	A surface glycoprotein	921:942	A surface glycoprotein with all the above characteristics	921:977	A surface glycoprotein with all the above characteristics was found on the lymphoblastoid cell line CEM.
6547160	9	57	theme	sialidase	1535:1543	arg1	concentrations					1545:1558	limiting sialidase concentrations	1526:1558	limiting sialidase concentrations	1526:1558	On treatment with limiting sialidase concentrations, gpL115 of normal lymphocytes is transformed into a series of partially desialylated species of decreasing electrophoretic mobility.
6547160	0	58	from	defective	73:81	arg1	syndrome					102:109	Wiskott-Aldrich syndrome	86:109	Wiskott-Aldrich syndrome	86:109	Characterization of a human lymphocyte surface sialoglycoprotein that is defective in Wiskott-Aldrich syndrome.
6547160	3	59	theme	residues	602:609	arg1	clusters					578:585	clusters	578:585	clusters of sialic acid residues	578:609	Native gpL115 adheres to wheat germ lectin-Sepharose and sialidase-treated gpL115 does not adhere, indicating that native gpL115 adheres via clusters of sialic acid residues.
6547160	12	60	theme	mol	1987:1989	arg1	wt					1991:1992	apparent mol wt 135,000	1978:2000	apparent mol wt 135,000	1978:2000	Lymphocytes from three of these patients displayed an abnormal 125I-component of apparent mol wt 135,000.
6547160	11	61	theme	Wiskott-Aldrich	1811:1825	arg1	patients					1836:1843	eight Wiskott-Aldrich syndrome patients	1805:1843	eight Wiskott-Aldrich syndrome patients	1805:1843	Lymphocytes of eight Wiskott-Aldrich syndrome patients were found to be deficient in 125I-labeled gpL115 .
6547160	1	62	theme	surface	135:141	arg1	deficient					161:169	deficient	161:169	deficient	161:169	gpL115 is a lymphocyte surface component that is deficient in patients with the X-chromosome-linked immune deficiency Wiskott-Aldrich syndrome (6).
6547160	1	62	theme	surface	135:141	arg1	component					143:151	a lymphocyte surface component	122:151	a lymphocyte surface component that is deficient in patients with the X-chromosome-linked immune deficiency Wiskott-Aldrich syndrome (6)	122:257	gpL115 is a lymphocyte surface component that is deficient in patients with the X-chromosome-linked immune deficiency Wiskott-Aldrich syndrome (6).
6547160	1	62	theme	surface	135:141	arg1	gpL115					112:117	gpL115	112:117	gpL115	112:117	gpL115 is a lymphocyte surface component that is deficient in patients with the X-chromosome-linked immune deficiency Wiskott-Aldrich syndrome (6).
6547160	4	63	theme	sialidase-treated	733:749	arg1	gpL115					751:756	sialidase-treated gpL115	733:756	sialidase-treated gpL115	733:756	When tested on peanut lectin, which shows specificity for the disaccharide Gal beta 1-3GalNAc, gpL115 is nonadherent and sialidase-treated gpL115 is adherent, indicating the presence of the sequence sialic acid-Gal beta 1-3GalNAc, which is characteristic for O-linked (mucin-type, acidic-type) carbohydrates.
6547160	2	64	theme	glycoprotein	264:275	arg1	nature					277:282	The glycoprotein nature	260:282	The glycoprotein nature of gpL115	260:292	The glycoprotein nature of gpL115 is demonstrated through labeling in carbohydrate moieties by [3H]NaBH4 and its synthesis by lymphocytes through labeling with [35S]methionine.
6547160	9	65	theme	lymphocytes	1578:1588	arg1	gpL115					1561:1566	gpL115	1561:1566	gpL115 of normal lymphocytes	1561:1588	On treatment with limiting sialidase concentrations, gpL115 of normal lymphocytes is transformed into a series of partially desialylated species of decreasing electrophoretic mobility.
6547160	0	66	theme	Wiskott-Aldrich	86:100	arg1	syndrome					102:109	Wiskott-Aldrich syndrome	86:109	Wiskott-Aldrich syndrome	86:109	Characterization of a human lymphocyte surface sialoglycoprotein that is defective in Wiskott-Aldrich syndrome.
6547160	2	67	from	labeling	318:325	arg1	moieties					343:350	carbohydrate moieties	330:350	carbohydrate moieties	330:350	The glycoprotein nature of gpL115 is demonstrated through labeling in carbohydrate moieties by [3H]NaBH4 and its synthesis by lymphocytes through labeling with [35S]methionine.
6547160	6	68	theme	CEM	1026:1028	arg1	immunogen					1049:1057	immunogen	1049:1057	immunogen	1049:1057	CEM cells were used as immunogen to generate the monoclonal antibody L10, an IgG1, which binds native and sialidase-treated gpL115 .
6547160	6	68	theme	CEM	1026:1028	arg1	cells					1030:1034	CEM cells	1026:1034	CEM cells	1026:1034	CEM cells were used as immunogen to generate the monoclonal antibody L10, an IgG1, which binds native and sialidase-treated gpL115 .
6547160	11	69	from	gpL115	1888:1893	arg1	deficient					1862:1870	deficient	1862:1870	deficient	1862:1870	Lymphocytes of eight Wiskott-Aldrich syndrome patients were found to be deficient in 125I-labeled gpL115 .
6547160	8	70	theme	significant	1459:1469	arg1	quantities					1471:1480	significant quantities	1459:1480	significant quantities of O-linked carbohydrate	1459:1505	Cumulatively, these findings indicate that gpL115 , like glycophorin of erythrocytes and GPIb of platelets, is a sialoglyco protein with significant quantities of O-linked carbohydrate.
6547160	7	71	theme	physical	1214:1221	arg1	properties					1223:1232	its physical properties	1210:1232	its physical properties	1210:1232	Sialidase-treatment of gpL115 significantly alters its physical properties, reducing its electrophoretic mobility and changing its behavior on isoelectrofocusing.
6547160	1	72	theme	deficiency	219:228	arg1	6					256:256	6	256:256	6	256:256	gpL115 is a lymphocyte surface component that is deficient in patients with the X-chromosome-linked immune deficiency Wiskott-Aldrich syndrome (6).
6547160	1	72	theme	deficiency	219:228	arg1	syndrome					246:253	the X-chromosome-linked immune deficiency Wiskott-Aldrich syndrome	188:253	the X-chromosome-linked immune deficiency Wiskott-Aldrich syndrome (6)	188:257	gpL115 is a lymphocyte surface component that is deficient in patients with the X-chromosome-linked immune deficiency Wiskott-Aldrich syndrome (6).
6547160	5	73	theme	lymphoblastoid	996:1009	arg1	CEM					1021:1023	the lymphoblastoid cell line CEM	992:1023	the lymphoblastoid cell line CEM	992:1023	A surface glycoprotein with all the above characteristics was found on the lymphoblastoid cell line CEM.
6547160	1	74	link	X-chromosome-linked	192:210	arg1	6					256:256	6	256:256	6	256:256	gpL115 is a lymphocyte surface component that is deficient in patients with the X-chromosome-linked immune deficiency Wiskott-Aldrich syndrome (6).
6547160	1	74	link	X-chromosome-linked	192:210	arg1	syndrome					246:253	the X-chromosome-linked immune deficiency Wiskott-Aldrich syndrome	188:253	the X-chromosome-linked immune deficiency Wiskott-Aldrich syndrome (6)	188:257	gpL115 is a lymphocyte surface component that is deficient in patients with the X-chromosome-linked immune deficiency Wiskott-Aldrich syndrome (6).
6547160	5	75	theme	above	957:961	arg1	characteristics					963:977	all the above characteristics	949:977	all the above characteristics	949:977	A surface glycoprotein with all the above characteristics was found on the lymphoblastoid cell line CEM.
6547160	6	76	theme	antibody	1086:1093	arg1	L10					1095:1097	the monoclonal antibody L10	1071:1097	the monoclonal antibody L10	1071:1097	CEM cells were used as immunogen to generate the monoclonal antibody L10, an IgG1, which binds native and sialidase-treated gpL115 .
6547160	6	76	theme	antibody	1086:1093	arg1	IgG1					1103:1106	an IgG1	1100:1106	an IgG1	1100:1106	CEM cells were used as immunogen to generate the monoclonal antibody L10, an IgG1, which binds native and sialidase-treated gpL115 .
6547160	11	77	theme	patients	1836:1843	arg1	Lymphocytes					1790:1800	Lymphocytes	1790:1800	Lymphocytes of eight Wiskott-Aldrich syndrome patients	1790:1843	Lymphocytes of eight Wiskott-Aldrich syndrome patients were found to be deficient in 125I-labeled gpL115 .
6547160	0	78	theme	human	22:26	arg1	sialoglycoprotein					47:63	a human lymphocyte surface sialoglycoprotein	20:63	a human lymphocyte surface sialoglycoprotein that is defective in Wiskott-Aldrich syndrome	20:109	Characterization of a human lymphocyte surface sialoglycoprotein that is defective in Wiskott-Aldrich syndrome.
6547160	0	78	theme	human	22:26	arg1	defective					73:81	defective	73:81	defective	73:81	Characterization of a human lymphocyte surface sialoglycoprotein that is defective in Wiskott-Aldrich syndrome.
6547160	4	79	theme	beta	827:830	arg1	characteristic					852:865	characteristic	852:865	characteristic	852:865	When tested on peanut lectin, which shows specificity for the disaccharide Gal beta 1-3GalNAc, gpL115 is nonadherent and sialidase-treated gpL115 is adherent, indicating the presence of the sequence sialic acid-Gal beta 1-3GalNAc, which is characteristic for O-linked (mucin-type, acidic-type) carbohydrates.
6547160	4	79	theme	beta	827:830	arg1	1-3GalNAc					832:840	the sequence sialic acid-Gal beta 1-3GalNAc	798:840	the sequence sialic acid-Gal beta 1-3GalNAc	798:840	When tested on peanut lectin, which shows specificity for the disaccharide Gal beta 1-3GalNAc, gpL115 is nonadherent and sialidase-treated gpL115 is adherent, indicating the presence of the sequence sialic acid-Gal beta 1-3GalNAc, which is characteristic for O-linked (mucin-type, acidic-type) carbohydrates.
6547160	10	80	theme	Wiskott-Aldrich	1755:1769	arg1	patients					1780:1787	some Wiskott-Aldrich syndrome patients	1750:1787	some Wiskott-Aldrich syndrome patients	1750:1787	This finding resembles the situation with lymphocytes of some Wiskott-Aldrich syndrome patients.
6547160	10	81	theme	patients	1780:1787	arg1	lymphocytes					1735:1745	lymphocytes	1735:1745	lymphocytes of some Wiskott-Aldrich syndrome patients	1735:1787	This finding resembles the situation with lymphocytes of some Wiskott-Aldrich syndrome patients.
6547160	0	82	theme	surface	39:45	arg1	sialoglycoprotein					47:63	a human lymphocyte surface sialoglycoprotein	20:63	a human lymphocyte surface sialoglycoprotein that is defective in Wiskott-Aldrich syndrome	20:109	Characterization of a human lymphocyte surface sialoglycoprotein that is defective in Wiskott-Aldrich syndrome.
6547160	0	82	theme	surface	39:45	arg1	defective					73:81	defective	73:81	defective	73:81	Characterization of a human lymphocyte surface sialoglycoprotein that is defective in Wiskott-Aldrich syndrome.
6547160	1	83	theme	Wiskott-Aldrich	230:244	arg1	6					256:256	6	256:256	6	256:256	gpL115 is a lymphocyte surface component that is deficient in patients with the X-chromosome-linked immune deficiency Wiskott-Aldrich syndrome (6).
6547160	1	83	theme	Wiskott-Aldrich	230:244	arg1	syndrome					246:253	the X-chromosome-linked immune deficiency Wiskott-Aldrich syndrome	188:253	the X-chromosome-linked immune deficiency Wiskott-Aldrich syndrome (6)	188:257	gpL115 is a lymphocyte surface component that is deficient in patients with the X-chromosome-linked immune deficiency Wiskott-Aldrich syndrome (6).
6547160	9	84	theme	electrophoretic	1667:1681	arg1	mobility					1683:1690	electrophoretic mobility	1667:1690	electrophoretic mobility	1667:1690	On treatment with limiting sialidase concentrations, gpL115 of normal lymphocytes is transformed into a series of partially desialylated species of decreasing electrophoretic mobility.
6547160	4	85	theme	1-3GalNAc	832:840	arg1	presence					786:793	the presence	782:793	the presence of the sequence sialic acid-Gal beta 1-3GalNAc, which is characteristic for O-linked (mucin-type, acidic-type) carbohydrates	782:918	When tested on peanut lectin, which shows specificity for the disaccharide Gal beta 1-3GalNAc, gpL115 is nonadherent and sialidase-treated gpL115 is adherent, indicating the presence of the sequence sialic acid-Gal beta 1-3GalNAc, which is characteristic for O-linked (mucin-type, acidic-type) carbohydrates.
6547160	3	86	theme	germ	468:471	arg1	lectin-Sepharose					473:488	wheat germ lectin-Sepharose	462:488	wheat germ lectin-Sepharose	462:488	Native gpL115 adheres to wheat germ lectin-Sepharose and sialidase-treated gpL115 does not adhere, indicating that native gpL115 adheres via clusters of sialic acid residues.
6547160	12	87	theme	patients	1929:1936	arg1	three					1914:1918	three	1914:1918	three	1914:1918	Lymphocytes from three of these patients displayed an abnormal 125I-component of apparent mol wt 135,000.
6547160	12	87	theme	patients	1929:1936	arg1	patients					1929:1936	these patients	1923:1936	these patients	1923:1936	Lymphocytes from three of these patients displayed an abnormal 125I-component of apparent mol wt 135,000.
6547160	6	88	theme	sialidase-treated	1132:1148	arg1	gpL115					1150:1155	native and sialidase-treated gpL115	1121:1155	native and sialidase-treated gpL115	1121:1155	CEM cells were used as immunogen to generate the monoclonal antibody L10, an IgG1, which binds native and sialidase-treated gpL115 .
6547160	9	89	with	treatment	1511:1519	arg1	concentrations					1545:1558	limiting sialidase concentrations	1526:1558	limiting sialidase concentrations	1526:1558	On treatment with limiting sialidase concentrations, gpL115 of normal lymphocytes is transformed into a series of partially desialylated species of decreasing electrophoretic mobility.
6547160	1	90	with	patients	174:181	arg1	6					256:256	6	256:256	6	256:256	gpL115 is a lymphocyte surface component that is deficient in patients with the X-chromosome-linked immune deficiency Wiskott-Aldrich syndrome (6).
6547160	1	90	with	patients	174:181	arg1	syndrome					246:253	the X-chromosome-linked immune deficiency Wiskott-Aldrich syndrome	188:253	the X-chromosome-linked immune deficiency Wiskott-Aldrich syndrome (6)	188:257	gpL115 is a lymphocyte surface component that is deficient in patients with the X-chromosome-linked immune deficiency Wiskott-Aldrich syndrome (6).
6547160	5	91	theme	line	1016:1019	arg1	CEM					1021:1023	the lymphoblastoid cell line CEM	992:1023	the lymphoblastoid cell line CEM	992:1023	A surface glycoprotein with all the above characteristics was found on the lymphoblastoid cell line CEM.
6547160	6	92	theme	native	1121:1126	arg1	gpL115					1150:1155	native and sialidase-treated gpL115	1121:1155	native and sialidase-treated gpL115	1121:1155	CEM cells were used as immunogen to generate the monoclonal antibody L10, an IgG1, which binds native and sialidase-treated gpL115 .
6547160	4	93	theme	peanut	627:632	arg1	lectin					634:639	peanut lectin	627:639	peanut lectin	627:639	When tested on peanut lectin, which shows specificity for the disaccharide Gal beta 1-3GalNAc, gpL115 is nonadherent and sialidase-treated gpL115 is adherent, indicating the presence of the sequence sialic acid-Gal beta 1-3GalNAc, which is characteristic for O-linked (mucin-type, acidic-type) carbohydrates.
6547160	11	94	theme	syndrome	1827:1834	arg1	patients					1836:1843	eight Wiskott-Aldrich syndrome patients	1805:1843	eight Wiskott-Aldrich syndrome patients	1805:1843	Lymphocytes of eight Wiskott-Aldrich syndrome patients were found to be deficient in 125I-labeled gpL115 .
6547160	4	95	theme	sequence	802:809	arg1	characteristic					852:865	characteristic	852:865	characteristic	852:865	When tested on peanut lectin, which shows specificity for the disaccharide Gal beta 1-3GalNAc, gpL115 is nonadherent and sialidase-treated gpL115 is adherent, indicating the presence of the sequence sialic acid-Gal beta 1-3GalNAc, which is characteristic for O-linked (mucin-type, acidic-type) carbohydrates.
6547160	4	95	theme	sequence	802:809	arg1	1-3GalNAc					832:840	the sequence sialic acid-Gal beta 1-3GalNAc	798:840	the sequence sialic acid-Gal beta 1-3GalNAc	798:840	When tested on peanut lectin, which shows specificity for the disaccharide Gal beta 1-3GalNAc, gpL115 is nonadherent and sialidase-treated gpL115 is adherent, indicating the presence of the sequence sialic acid-Gal beta 1-3GalNAc, which is characteristic for O-linked (mucin-type, acidic-type) carbohydrates.
6547160	0	96	gly	sialoglycoprotein	47:63	arg1	sialoglycoprotein					47:63	a human lymphocyte surface sialoglycoprotein	20:63	a human lymphocyte surface sialoglycoprotein that is defective in Wiskott-Aldrich syndrome	20:109	Characterization of a human lymphocyte surface sialoglycoprotein that is defective in Wiskott-Aldrich syndrome.
6547160	0	96	gly	sialoglycoprotein	47:63	arg1	defective					73:81	defective	73:81	defective	73:81	Characterization of a human lymphocyte surface sialoglycoprotein that is defective in Wiskott-Aldrich syndrome.
6547160	4	97	theme	acid-Gal	818:825	arg1	characteristic					852:865	characteristic	852:865	characteristic	852:865	When tested on peanut lectin, which shows specificity for the disaccharide Gal beta 1-3GalNAc, gpL115 is nonadherent and sialidase-treated gpL115 is adherent, indicating the presence of the sequence sialic acid-Gal beta 1-3GalNAc, which is characteristic for O-linked (mucin-type, acidic-type) carbohydrates.
6547160	4	97	theme	acid-Gal	818:825	arg1	1-3GalNAc					832:840	the sequence sialic acid-Gal beta 1-3GalNAc	798:840	the sequence sialic acid-Gal beta 1-3GalNAc	798:840	When tested on peanut lectin, which shows specificity for the disaccharide Gal beta 1-3GalNAc, gpL115 is nonadherent and sialidase-treated gpL115 is adherent, indicating the presence of the sequence sialic acid-Gal beta 1-3GalNAc, which is characteristic for O-linked (mucin-type, acidic-type) carbohydrates.
8627329	5	0	theme	lectin	652:657	arg1	blotting					659:666	lectin blotting	652:666	lectin blotting	652:666	Addition during biosynthesis of O-linked glycans was evaluated, and structures were characterized by lectin blotting and glycosidase digestion.
8627329	1	1	theme	common	144:149	arg1	receptor					185:192	the 75-kDa neurotrophin receptor	161:192	the 75-kDa neurotrophin receptor (NTR)	161:198	Four neurotrophic factors, important for survival and function of neurons, bind a common receptor, the 75-kDa neurotrophin receptor (NTR).
8627329	1	1	theme	common	144:149	arg1	receptor					151:158	a common receptor	142:158	a common receptor	142:158	Four neurotrophic factors, important for survival and function of neurons, bind a common receptor, the 75-kDa neurotrophin receptor (NTR).
8627329	0	2	from	oligosaccharide	9:23	arg1	receptor					52:59	the 75-kDa neurotrophin receptor	28:59	the 75-kDa neurotrophin receptor	28:59	O-linked oligosaccharide on the 75-kDa neurotrophin receptor.
8627329	9	3	theme	nerve	1184:1188	arg1	factor					1197:1202	nerve growth factor	1184:1202	nerve growth factor	1184:1202	Modification of the O-linked oligosaccharide produced small, possibly significant effects on the binding constant of NTR for nerve growth factor.
8627329	8	4	theme	Gal	1039:1041	arg1	1-3GalNAc					1048:1056	the structure (NeuNAc)(1-2-) Gal beta 1-3GalNAc	1010:1056	the structure (NeuNAc)(1-2-) Gal beta 1-3GalNAc	1010:1056	NTR O-linked glycans synthesized by cultured cells had the structure (NeuNAc)(1-2-) Gal beta 1-3GalNAc.
8627329	4	5	theme	extracellular	495:507	arg1	domains					509:515	the extracellular domains	491:515	the extracellular domains	491:515	To investigate the structure and function of O-glycosylation on NTR, we produced the extracellular domains by expression in mammalian cells.
8627329	8	6	theme	beta	1043:1046	arg1	1-3GalNAc					1048:1056	the structure (NeuNAc)(1-2-) Gal beta 1-3GalNAc	1010:1056	the structure (NeuNAc)(1-2-) Gal beta 1-3GalNAc	1010:1056	NTR O-linked glycans synthesized by cultured cells had the structure (NeuNAc)(1-2-) Gal beta 1-3GalNAc.
8627329	9	7	theme	growth	1190:1195	arg1	factor					1197:1202	nerve growth factor	1184:1202	nerve growth factor	1184:1202	Modification of the O-linked oligosaccharide produced small, possibly significant effects on the binding constant of NTR for nerve growth factor.
8627329	6	8	from	Effects	695:701	arg1	constant					787:794	the equilibrium binding constant	763:794	the equilibrium binding constant	763:794	Effects of disialylation, deglycosylation, and lectin attachment on the equilibrium binding constant were measured.
8627329	3	9	theme	intracellular	340:352	arg1	sequences					354:362	intracellular sequences	340:362	intracellular sequences	340:362	This peptide, the transmembrane helix, and intracellular sequences are highly conserved in vertebrate evolution.
8627329	5	10	theme	glycosidase	672:682	arg1	digestion					684:692	glycosidase digestion	672:692	glycosidase digestion	672:692	Addition during biosynthesis of O-linked glycans was evaluated, and structures were characterized by lectin blotting and glycosidase digestion.
8627329	1	11	theme	neurotrophic	67:78	arg1	factors					80:86	Four neurotrophic factors	62:86	Four neurotrophic factors	62:86	Four neurotrophic factors, important for survival and function of neurons, bind a common receptor, the 75-kDa neurotrophin receptor (NTR).
8627329	7	12	theme	large	880:884	arg1	effect					886:891	a large effect	878:891	a large effect	878:891	Addition of O-linked glycans during biosynthesis was found to have a large effect on NTR structure assessed by mobility in polyacrylamide gels.
8627329	8	13	contain	had	1006:1008	arg2	1-3GalNAc					1048:1056	the structure (NeuNAc)(1-2-) Gal beta 1-3GalNAc	1010:1056	the structure (NeuNAc)(1-2-) Gal beta 1-3GalNAc	1010:1056	NTR O-linked glycans synthesized by cultured cells had the structure (NeuNAc)(1-2-) Gal beta 1-3GalNAc.
8627329	8	13	contain	had	1006:1008	arg1	glycans					968:974	NTR O-linked glycans	955:974	NTR O-linked glycans synthesized by cultured cells	955:1004	NTR O-linked glycans synthesized by cultured cells had the structure (NeuNAc)(1-2-) Gal beta 1-3GalNAc.
8627329	10	14	theme	ligand	1288:1293	arg1	binding					1295:1301	ligand binding	1288:1301	ligand binding	1288:1301	The results are discussed in reference to a potential role for the stalk region in ligand binding and signaling.
8627329	0	15	link	O-linked	0:7	arg1	oligosaccharide					9:23	O-linked oligosaccharide	0:23	O-linked oligosaccharide on the 75-kDa neurotrophin receptor	0:59	O-linked oligosaccharide on the 75-kDa neurotrophin receptor.
8627329	2	16	theme	NTR	265:267	arg1	NTR					265:267	NTR	265:267	NTR	265:267	An O-glycosylated peptide connects the ligand-binding domain of NTR to its transmembrane helix.
8627329	2	16	theme	NTR	265:267	arg1	domain					255:260	the ligand-binding domain	236:260	the ligand-binding domain of NTR	236:267	An O-glycosylated peptide connects the ligand-binding domain of NTR to its transmembrane helix.
8627329	6	17	theme	deglycosylation	721:735	arg1	Effects					695:701	Effects	695:701	Effects of disialylation, deglycosylation, and lectin attachment on the equilibrium binding constant	695:794	Effects of disialylation, deglycosylation, and lectin attachment on the equilibrium binding constant were measured.
8627329	0	18	theme	neurotrophin	39:50	arg1	receptor					52:59	the 75-kDa neurotrophin receptor	28:59	the 75-kDa neurotrophin receptor	28:59	O-linked oligosaccharide on the 75-kDa neurotrophin receptor.
8627329	9	19	theme	oligosaccharide	1088:1102	arg1	Modification					1059:1070	Modification	1059:1070	Modification of the O-linked oligosaccharide	1059:1102	Modification of the O-linked oligosaccharide produced small, possibly significant effects on the binding constant of NTR for nerve growth factor.
8627329	9	20	link	O-linked	1079:1086	arg1	oligosaccharide					1088:1102	the O-linked oligosaccharide	1075:1102	the O-linked oligosaccharide	1075:1102	Modification of the O-linked oligosaccharide produced small, possibly significant effects on the binding constant of NTR for nerve growth factor.
8627329	1	21	theme	important	89:97	arg1	factors					80:86	Four neurotrophic factors	62:86	Four neurotrophic factors	62:86	Four neurotrophic factors, important for survival and function of neurons, bind a common receptor, the 75-kDa neurotrophin receptor (NTR).
8627329	6	22	theme	disialylation	706:718	arg1	Effects					695:701	Effects	695:701	Effects of disialylation, deglycosylation, and lectin attachment on the equilibrium binding constant	695:794	Effects of disialylation, deglycosylation, and lectin attachment on the equilibrium binding constant were measured.
8627329	1	23	theme	75-kDa	165:170	arg1	NTR					195:197	NTR	195:197	NTR	195:197	Four neurotrophic factors, important for survival and function of neurons, bind a common receptor, the 75-kDa neurotrophin receptor (NTR).
8627329	1	23	theme	75-kDa	165:170	arg1	receptor					185:192	the 75-kDa neurotrophin receptor	161:192	the 75-kDa neurotrophin receptor (NTR)	161:198	Four neurotrophic factors, important for survival and function of neurons, bind a common receptor, the 75-kDa neurotrophin receptor (NTR).
8627329	1	23	theme	75-kDa	165:170	arg1	receptor					151:158	a common receptor	142:158	a common receptor	142:158	Four neurotrophic factors, important for survival and function of neurons, bind a common receptor, the 75-kDa neurotrophin receptor (NTR).
8627329	0	24	theme	O-linked	0:7	arg1	oligosaccharide					9:23	O-linked oligosaccharide	0:23	O-linked oligosaccharide on the 75-kDa neurotrophin receptor	0:59	O-linked oligosaccharide on the 75-kDa neurotrophin receptor.
8627329	7	25	theme	glycans	832:838	arg1	Addition					811:818	Addition	811:818	Addition of O-linked glycans during biosynthesis	811:858	Addition of O-linked glycans during biosynthesis was found to have a large effect on NTR structure assessed by mobility in polyacrylamide gels.
8627329	5	26	theme	O-linked	583:590	arg1	glycans					592:598	O-linked glycans	583:598	O-linked glycans	583:598	Addition during biosynthesis of O-linked glycans was evaluated, and structures were characterized by lectin blotting and glycosidase digestion.
8627329	9	27	theme	small	1113:1117	arg1	effects					1141:1147	small, possibly significant effects	1113:1147	small, possibly significant effects	1113:1147	Modification of the O-linked oligosaccharide produced small, possibly significant effects on the binding constant of NTR for nerve growth factor.
8627329	1	28	theme	neurotrophin	172:183	arg1	NTR					195:197	NTR	195:197	NTR	195:197	Four neurotrophic factors, important for survival and function of neurons, bind a common receptor, the 75-kDa neurotrophin receptor (NTR).
8627329	1	28	theme	neurotrophin	172:183	arg1	receptor					185:192	the 75-kDa neurotrophin receptor	161:192	the 75-kDa neurotrophin receptor (NTR)	161:198	Four neurotrophic factors, important for survival and function of neurons, bind a common receptor, the 75-kDa neurotrophin receptor (NTR).
8627329	1	28	theme	neurotrophin	172:183	arg1	receptor					151:158	a common receptor	142:158	a common receptor	142:158	Four neurotrophic factors, important for survival and function of neurons, bind a common receptor, the 75-kDa neurotrophin receptor (NTR).
8627329	5	29	theme	glycans	592:598	arg1	biosynthesis					567:578	biosynthesis	567:578	biosynthesis of O-linked glycans	567:598	Addition during biosynthesis of O-linked glycans was evaluated, and structures were characterized by lectin blotting and glycosidase digestion.
8627329	10	30	theme	stalk	1272:1276	arg1	region					1278:1283	the stalk region	1268:1283	the stalk region	1268:1283	The results are discussed in reference to a potential role for the stalk region in ligand binding and signaling.
8627329	7	31	link	O-linked	823:830	arg1	glycans					832:838	O-linked glycans	823:838	O-linked glycans	823:838	Addition of O-linked glycans during biosynthesis was found to have a large effect on NTR structure assessed by mobility in polyacrylamide gels.
8627329	8	32	theme	O-linked	959:966	arg1	glycans					968:974	NTR O-linked glycans	955:974	NTR O-linked glycans synthesized by cultured cells	955:1004	NTR O-linked glycans synthesized by cultured cells had the structure (NeuNAc)(1-2-) Gal beta 1-3GalNAc.
8627329	10	33	theme	potential	1249:1257	arg1	role					1259:1262	a potential role	1247:1262	a potential role for the stalk region in ligand binding and signaling	1247:1315	The results are discussed in reference to a potential role for the stalk region in ligand binding and signaling.
8627329	2	34	theme	transmembrane	276:288	arg1	helix					290:294	its transmembrane helix	272:294	its transmembrane helix	272:294	An O-glycosylated peptide connects the ligand-binding domain of NTR to its transmembrane helix.
8627329	2	35	gly	O-glycosylated	204:217	arg1	peptide					219:225	An O-glycosylated peptide	201:225	An O-glycosylated peptide	201:225	An O-glycosylated peptide connects the ligand-binding domain of NTR to its transmembrane helix.
8627329	7	36	theme	O-linked	823:830	arg1	glycans					832:838	O-linked glycans	823:838	O-linked glycans	823:838	Addition of O-linked glycans during biosynthesis was found to have a large effect on NTR structure assessed by mobility in polyacrylamide gels.
8627329	4	37	from	function	443:450	arg1	NTR					474:476	NTR	474:476	NTR	474:476	To investigate the structure and function of O-glycosylation on NTR, we produced the extracellular domains by expression in mammalian cells.
8627329	10	38	from	role	1259:1262	arg1	signaling					1307:1315	signaling	1307:1315	signaling	1307:1315	The results are discussed in reference to a potential role for the stalk region in ligand binding and signaling.
8627329	10	38	from	role	1259:1262	arg1	binding					1295:1301	ligand binding	1288:1301	ligand binding	1288:1301	The results are discussed in reference to a potential role for the stalk region in ligand binding and signaling.
8627329	0	39	theme	75-kDa	32:37	arg1	receptor					52:59	the 75-kDa neurotrophin receptor	28:59	the 75-kDa neurotrophin receptor	28:59	O-linked oligosaccharide on the 75-kDa neurotrophin receptor.
8627329	4	40	theme	O-glycosylation	455:469	arg1	function					443:450	function	443:450	function	443:450	To investigate the structure and function of O-glycosylation on NTR, we produced the extracellular domains by expression in mammalian cells.
8627329	4	40	theme	O-glycosylation	455:469	arg1	structure					429:437	structure	429:437	structure	429:437	To investigate the structure and function of O-glycosylation on NTR, we produced the extracellular domains by expression in mammalian cells.
8627329	2	41	theme	O-glycosylated	204:217	arg1	peptide					219:225	An O-glycosylated peptide	201:225	An O-glycosylated peptide	201:225	An O-glycosylated peptide connects the ligand-binding domain of NTR to its transmembrane helix.
8627329	4	42	from	expression	520:529	arg1	cells					544:548	mammalian cells	534:548	mammalian cells	534:548	To investigate the structure and function of O-glycosylation on NTR, we produced the extracellular domains by expression in mammalian cells.
8627329	9	43	dep	small	1113:1117	arg1	significant					1129:1139	significant	1129:1139	significant	1129:1139	Modification of the O-linked oligosaccharide produced small, possibly significant effects on the binding constant of NTR for nerve growth factor.
8627329	4	44	from	structure	429:437	arg1	NTR					474:476	NTR	474:476	NTR	474:476	To investigate the structure and function of O-glycosylation on NTR, we produced the extracellular domains by expression in mammalian cells.
8627329	6	45	theme	binding	779:785	arg1	constant					787:794	the equilibrium binding constant	763:794	the equilibrium binding constant	763:794	Effects of disialylation, deglycosylation, and lectin attachment on the equilibrium binding constant were measured.
8627329	3	46	theme	vertebrate	388:397	arg1	evolution					399:407	vertebrate evolution	388:407	vertebrate evolution	388:407	This peptide, the transmembrane helix, and intracellular sequences are highly conserved in vertebrate evolution.
8627329	4	47	theme	mammalian	534:542	arg1	cells					544:548	mammalian cells	534:548	mammalian cells	534:548	To investigate the structure and function of O-glycosylation on NTR, we produced the extracellular domains by expression in mammalian cells.
8627329	7	48	contain	have	873:876	arg2	effect					886:891	a large effect	878:891	a large effect	878:891	Addition of O-linked glycans during biosynthesis was found to have a large effect on NTR structure assessed by mobility in polyacrylamide gels.
8627329	7	48	contain	have	873:876	arg1	Addition					811:818	Addition	811:818	Addition of O-linked glycans during biosynthesis	811:858	Addition of O-linked glycans during biosynthesis was found to have a large effect on NTR structure assessed by mobility in polyacrylamide gels.
8627329	6	49	gly	deglycosylation	721:735	arg1	equilibrium					767:777	the equilibrium binding constant	763:794	the equilibrium binding constant	763:794	Effects of disialylation, deglycosylation, and lectin attachment on the equilibrium binding constant were measured.
8627329	6	49	gly	deglycosylation	721:735	arg1	binding					779:785	the equilibrium binding constant	763:794	the equilibrium binding constant	763:794	Effects of disialylation, deglycosylation, and lectin attachment on the equilibrium binding constant were measured.
8627329	6	50	theme	equilibrium	767:777	arg1	constant					787:794	the equilibrium binding constant	763:794	the equilibrium binding constant	763:794	Effects of disialylation, deglycosylation, and lectin attachment on the equilibrium binding constant were measured.
8627329	9	51	theme	O-linked	1079:1086	arg1	oligosaccharide					1088:1102	the O-linked oligosaccharide	1075:1102	the O-linked oligosaccharide	1075:1102	Modification of the O-linked oligosaccharide produced small, possibly significant effects on the binding constant of NTR for nerve growth factor.
8627329	9	52	theme	NTR	1176:1178	arg1	constant					1164:1171	the binding constant	1152:1171	the binding constant of NTR for nerve growth factor	1152:1202	Modification of the O-linked oligosaccharide produced small, possibly significant effects on the binding constant of NTR for nerve growth factor.
8627329	8	53	theme	cultured	991:998	arg1	cells					1000:1004	cultured cells	991:1004	cultured cells	991:1004	NTR O-linked glycans synthesized by cultured cells had the structure (NeuNAc)(1-2-) Gal beta 1-3GalNAc.
8627329	9	54	theme	binding	1156:1162	arg1	constant					1164:1171	the binding constant	1152:1171	the binding constant of NTR for nerve growth factor	1152:1202	Modification of the O-linked oligosaccharide produced small, possibly significant effects on the binding constant of NTR for nerve growth factor.
8627329	1	55	theme	neurons	128:134	arg1	function					116:123	function	116:123	function	116:123	Four neurotrophic factors, important for survival and function of neurons, bind a common receptor, the 75-kDa neurotrophin receptor (NTR).
8627329	1	55	theme	neurons	128:134	arg1	survival					103:110	survival	103:110	survival	103:110	Four neurotrophic factors, important for survival and function of neurons, bind a common receptor, the 75-kDa neurotrophin receptor (NTR).
8627329	7	56	theme	polyacrylamide	934:947	arg1	gels					949:952	polyacrylamide gels	934:952	polyacrylamide gels	934:952	Addition of O-linked glycans during biosynthesis was found to have a large effect on NTR structure assessed by mobility in polyacrylamide gels.
8627329	4	57	dep	structure	429:437	arg1	the					425:427	the	425:427	the	425:427	To investigate the structure and function of O-glycosylation on NTR, we produced the extracellular domains by expression in mammalian cells.
8627329	6	58	gly	disialylation	706:718	arg1	equilibrium					767:777	the equilibrium binding constant	763:794	the equilibrium binding constant	763:794	Effects of disialylation, deglycosylation, and lectin attachment on the equilibrium binding constant were measured.
8627329	6	58	gly	disialylation	706:718	arg1	binding					779:785	the equilibrium binding constant	763:794	the equilibrium binding constant	763:794	Effects of disialylation, deglycosylation, and lectin attachment on the equilibrium binding constant were measured.
8627329	2	59	theme	ligand-binding	240:253	arg1	NTR					265:267	NTR	265:267	NTR	265:267	An O-glycosylated peptide connects the ligand-binding domain of NTR to its transmembrane helix.
8627329	2	59	theme	ligand-binding	240:253	arg1	domain					255:260	the ligand-binding domain	236:260	the ligand-binding domain of NTR	236:267	An O-glycosylated peptide connects the ligand-binding domain of NTR to its transmembrane helix.
8627329	8	60	link	O-linked	959:966	arg1	glycans					968:974	NTR O-linked glycans	955:974	NTR O-linked glycans synthesized by cultured cells	955:1004	NTR O-linked glycans synthesized by cultured cells had the structure (NeuNAc)(1-2-) Gal beta 1-3GalNAc.
8627329	7	61	theme	NTR	896:898	arg1	structure					900:908	NTR structure	896:908	NTR structure assessed by mobility in polyacrylamide gels	896:952	Addition of O-linked glycans during biosynthesis was found to have a large effect on NTR structure assessed by mobility in polyacrylamide gels.
8627329	6	62	theme	attachment	749:758	arg1	Effects					695:701	Effects	695:701	Effects of disialylation, deglycosylation, and lectin attachment on the equilibrium binding constant	695:794	Effects of disialylation, deglycosylation, and lectin attachment on the equilibrium binding constant were measured.
8627329	3	63	theme	transmembrane	315:327	arg1	helix					329:333	the transmembrane helix	311:333	the transmembrane helix	311:333	This peptide, the transmembrane helix, and intracellular sequences are highly conserved in vertebrate evolution.
8627329	6	64	theme	lectin	742:747	arg1	attachment					749:758	lectin attachment	742:758	lectin attachment	742:758	Effects of disialylation, deglycosylation, and lectin attachment on the equilibrium binding constant were measured.
8627329	5	65	link	O-linked	583:590	arg1	glycans					592:598	O-linked glycans	583:598	O-linked glycans	583:598	Addition during biosynthesis of O-linked glycans was evaluated, and structures were characterized by lectin blotting and glycosidase digestion.
8627329	8	66	dep	Gal	1039:1041	arg1	NeuNAc					1025:1030	NeuNAc	1025:1030	NeuNAc	1025:1030	NTR O-linked glycans synthesized by cultured cells had the structure (NeuNAc)(1-2-) Gal beta 1-3GalNAc.
8627329	8	66	dep	Gal	1039:1041	arg1	structure					1014:1022	structure	1014:1022	structure (NeuNAc)	1014:1031	NTR O-linked glycans synthesized by cultured cells had the structure (NeuNAc)(1-2-) Gal beta 1-3GalNAc.
7430095	3	0	dep	beta	978:981	arg1	leads					1031:1035	leads	1031:1035	leads to 3	1031:1040	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	3	0	dep	beta	978:981	arg1	leads					1009:1013	leads	1009:1013	leads to 2Man alpha 1	1009:1029	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	3	0	dep	beta	978:981	arg1	leads					985:989	leads	985:989	leads to 4GlcNAc beta 1	985:1007	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	3	1	dep	6	948:948	arg1	leads					1080:1084	leads	1080:1084	leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc	1080:1144	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	3	1	dep	6	948:948	arg1	leads					1058:1062	leads	1058:1062	leads to 4	1058:1067	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	3	1	dep	6	948:948	arg1	leads					964:968	leads	964:968	leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3	964:1040	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	3	2	theme	exoglycosidase	482:495	arg1	digestion					497:505	sequential exoglycosidase digestion	471:505	sequential exoglycosidase digestion in combination with methylation study and periodate oxidation	471:567	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	3	3	theme	GlcNAc	753:758	arg1	beta					760:763	GlcNAc beta 1	753:765	GlcNAc beta 1 leads to 4	753:776	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	3	4	dep	beta	633:636	arg1	beta					760:763	GlcNAc beta 1	753:765	GlcNAc beta 1 leads to 4	753:776	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	3	4	dep	beta	633:636	arg1	leads					640:644	leads	640:644	leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)	640:749	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	0	5	theme	A	79:79	arg1	chains					42:47	the asparagine-linked sugar chains	14:47	the asparagine-linked sugar chains of glycophorin A. Glycophorin A isolated from human erythrocytes	14:112	Structures of the asparagine-linked sugar chains of glycophorin A. Glycophorin A isolated from human erythrocytes contains one asparagine-linked sugar chain in one molecule.
7430095	3	6	theme	2Man	649:652	arg1	alpha					654:658	2Man alpha 1	649:660	2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)	649:749	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	3	7	theme	NeuAc	858:862	arg1	alpha					864:868	NeuAc alpha 2	858:870	NeuAc alpha 2	858:870	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	0	8	link	asparagine-linked	18:34	arg1	chains					42:47	the asparagine-linked sugar chains	14:47	the asparagine-linked sugar chains of glycophorin A. Glycophorin A isolated from human erythrocytes	14:112	Structures of the asparagine-linked sugar chains of glycophorin A. Glycophorin A isolated from human erythrocytes contains one asparagine-linked sugar chain in one molecule.
7430095	3	9	with	combination	510:520	arg1	study					539:543	methylation study	527:543	methylation study	527:543	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	3	9	with	combination	510:520	arg1	oxidation					559:567	periodate oxidation	549:567	periodate oxidation	549:567	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	0	10	theme	human	95:99	arg1	erythrocytes					101:112	human erythrocytes	95:112	human erythrocytes	95:112	Structures of the asparagine-linked sugar chains of glycophorin A. Glycophorin A isolated from human erythrocytes contains one asparagine-linked sugar chain in one molecule.
7430095	3	11	from	digestion	497:505	arg1	combination					510:520	combination	510:520	combination with methylation study and periodate oxidation	510:567	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	3	12	dep	beta	782:785	arg1	leads					789:793	leads	789:793	leads to 4GlcNAc beta 1	789:811	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	3	13	theme	2Man	724:727	arg1	alpha					729:733	2Man alpha 1	724:735	2Man alpha 1	724:735	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	3	14	theme	4GlcNAc	798:804	arg1	beta					806:809	4GlcNAc beta 1	798:811	4GlcNAc beta 1	798:811	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	3	15	theme	GlcNAc	1044:1049	arg1	beta					1051:1054	GlcNAc beta 1	1044:1056	GlcNAc beta 1	1044:1056	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	3	16	theme	major	408:412	arg1	oligosaccharides					421:436	the major acidic oligosaccharides	404:436	the major acidic oligosaccharides (A-1 and A-2)	404:450	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	3	16	theme	major	408:412	arg1	A-2					447:449	A-2	447:449	A-2	447:449	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	3	16	theme	major	408:412	arg1	A-1					439:441	A-1	439:441	A-1	439:441	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	3	17	theme	oligosaccharides	421:436	arg1	structures					390:399	Complete structures	381:399	Complete structures of the major acidic oligosaccharides (A-1 and A-2)	381:450	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	3	17	theme	oligosaccharides	421:436	arg1	follows					572:578	follows	572:578	follows	572:578	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	3	18	theme	6Gal	973:976	arg1	beta					978:981	6Gal beta 1	973:983	6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3	973:1040	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	3	19	theme	methylation	527:537	arg1	study					539:543	methylation study	527:543	methylation study	527:543	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	0	20	link	asparagine-linked	127:143	arg1	chain					151:155	one asparagine-linked sugar chain	123:155	one asparagine-linked sugar chain in one molecule	123:171	Structures of the asparagine-linked sugar chains of glycophorin A. Glycophorin A isolated from human erythrocytes contains one asparagine-linked sugar chain in one molecule.
7430095	1	21	theme	sugar	179:183	arg1	chain					185:189	This sugar chain	174:189	This sugar chain	174:189	This sugar chain was successfully released as an oligosaccharide fraction by hydrazinolysis.
7430095	1	21	theme	sugar	179:183	arg1	fraction					239:246	an oligosaccharide fraction	220:246	an oligosaccharide fraction	220:246	This sugar chain was successfully released as an oligosaccharide fraction by hydrazinolysis.
7430095	3	22	theme	2Man	926:929	arg1	alpha					931:935	2Man alpha 1	926:937	2Man alpha 1	926:937	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	2	23	theme	paper	358:362	arg1	electrophoresis					364:378	paper electrophoresis	358:378	paper electrophoresis	358:378	The oligosaccharide fraction was separated into four components (N, A-1, A-2', and A-2) by paper electrophoresis.
7430095	3	24	dep	GlcNAc	847:852	arg1	leads					836:840	leads	836:840	leads to 6	836:845	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	3	25	theme	Complete	381:388	arg1	structures					390:399	Complete structures	381:399	Complete structures of the major acidic oligosaccharides (A-1 and A-2)	381:450	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	3	25	theme	Complete	381:388	arg1	follows					572:578	follows	572:578	follows	572:578	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	3	26	theme	Man	1069:1071	arg1	beta					1073:1076	Man beta 1	1069:1078	Man beta 1	1069:1078	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	3	27	theme	Man	778:780	arg1	beta					782:785	4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1	625:787	4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1	625:811	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	3	28	theme	4GlcNAc	625:631	arg1	beta					633:636	4GlcNAc beta 1	625:638	4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1	625:811	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	0	29	theme	asparagine-linked	18:34	arg1	chains					42:47	the asparagine-linked sugar chains	14:47	the asparagine-linked sugar chains of glycophorin A. Glycophorin A isolated from human erythrocytes	14:112	Structures of the asparagine-linked sugar chains of glycophorin A. Glycophorin A isolated from human erythrocytes contains one asparagine-linked sugar chain in one molecule.
7430095	3	30	dep	alpha	654:658	arg1	leads					662:666	leads	662:666	leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)	662:749	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	0	31	theme	asparagine-linked	127:143	arg1	chain					151:155	one asparagine-linked sugar chain	123:155	one asparagine-linked sugar chain in one molecule	123:171	Structures of the asparagine-linked sugar chains of glycophorin A. Glycophorin A isolated from human erythrocytes contains one asparagine-linked sugar chain in one molecule.
7430095	3	32	theme	periodate	549:557	arg1	oxidation					559:567	periodate oxidation	549:567	periodate oxidation	549:567	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	3	33	theme	Fuc	824:826	arg1	alpha					828:832	Fuc alpha 1	824:834	Fuc alpha 1	824:834	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	3	34	theme	NeuAc	950:954	arg1	alpha					956:960	NeuAc alpha 2	950:962	NeuAc alpha 2	950:962	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	3	35	dep	GlcNAc	1139:1144	arg1	leads					1127:1131	leads	1127:1131	leads to 6	1127:1136	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	3	36	theme	sequential	471:480	arg1	digestion					497:505	sequential exoglycosidase digestion	471:505	sequential exoglycosidase digestion in combination with methylation study and periodate oxidation	471:567	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	3	37	dep	follows	572:578	arg1	leads					616:620	leads	616:620	leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1	616:811	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	3	38	dep	beta	1097:1100	arg1	leads					1104:1108	leads	1104:1108	leads to 4(Fuc alpha 1 leads to 6) GlcNAc	1104:1144	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	0	39	theme	chains	42:47	arg1	Structures					0:9	Structures	0:9	Structures of the asparagine-linked sugar chains of glycophorin A. Glycophorin A isolated from human erythrocytes	0:112	Structures of the asparagine-linked sugar chains of glycophorin A. Glycophorin A isolated from human erythrocytes contains one asparagine-linked sugar chain in one molecule.
7430095	3	40	theme	[Gal	676:679	arg1	beta					681:684	6(3) [Gal beta 1	671:686	6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)	671:749	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	3	41	theme	6Gal	881:884	arg1	beta					886:889	6Gal beta 1	881:891	6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc	881:1144	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	3	42	theme	Fuc	1115:1117	arg1	alpha					1119:1123	Fuc alpha 1	1115:1125	Fuc alpha 1	1115:1125	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	3	43	theme	acidic	414:419	arg1	oligosaccharides					421:436	the major acidic oligosaccharides	404:436	the major acidic oligosaccharides (A-1 and A-2)	404:450	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	3	43	theme	acidic	414:419	arg1	A-2					447:449	A-2	447:449	A-2	447:449	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	3	43	theme	acidic	414:419	arg1	A-1					439:441	A-1	439:441	A-1	439:441	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	0	44	theme	sugar	36:40	arg1	chains					42:47	the asparagine-linked sugar chains	14:47	the asparagine-linked sugar chains of glycophorin A. Glycophorin A isolated from human erythrocytes	14:112	Structures of the asparagine-linked sugar chains of glycophorin A. Glycophorin A isolated from human erythrocytes contains one asparagine-linked sugar chain in one molecule.
7430095	3	45	theme	4GlcNAc	697:703	arg1	beta					705:708	4GlcNAc beta 1	697:710	4GlcNAc beta 1	697:710	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	0	46	theme	sugar	145:149	arg1	chain					151:155	one asparagine-linked sugar chain	123:155	one asparagine-linked sugar chain in one molecule	123:171	Structures of the asparagine-linked sugar chains of glycophorin A. Glycophorin A isolated from human erythrocytes contains one asparagine-linked sugar chain in one molecule.
7430095	3	47	dep	beta	760:763	arg1	leads					767:771	leads	767:771	leads to 4	767:776	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	0	48	theme	glycophorin	52:62	arg1	A					79:79	glycophorin A. Glycophorin A	52:79	glycophorin A. Glycophorin A isolated from human erythrocytes	52:112	Structures of the asparagine-linked sugar chains of glycophorin A. Glycophorin A isolated from human erythrocytes contains one asparagine-linked sugar chain in one molecule.
7430095	3	49	dep	beta	886:889	arg1	leads					939:943	leads	939:943	leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc	939:1144	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	3	49	dep	beta	886:889	arg1	leads					917:921	leads	917:921	leads to 2Man alpha 1	917:937	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	3	49	dep	beta	886:889	arg1	leads					893:897	leads	893:897	leads to 4GlcNAc beta 1	893:915	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	3	50	dep	oligosaccharides	421:436	arg1	oligosaccharides					421:436	the major acidic oligosaccharides	404:436	the major acidic oligosaccharides (A-1 and A-2)	404:450	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	3	50	dep	oligosaccharides	421:436	arg1	A-2					447:449	A-2	447:449	A-2	447:449	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	3	50	dep	oligosaccharides	421:436	arg1	A-1					439:441	A-1	439:441	A-1	439:441	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	0	51	contain	contains	114:121	arg1	Structures					0:9	Structures	0:9	Structures of the asparagine-linked sugar chains of glycophorin A. Glycophorin A isolated from human erythrocytes	0:112	Structures of the asparagine-linked sugar chains of glycophorin A. Glycophorin A isolated from human erythrocytes contains one asparagine-linked sugar chain in one molecule.
7430095	0	51	contain	contains	114:121	arg2	chain					151:155	one asparagine-linked sugar chain	123:155	one asparagine-linked sugar chain in one molecule	123:171	Structures of the asparagine-linked sugar chains of glycophorin A. Glycophorin A isolated from human erythrocytes contains one asparagine-linked sugar chain in one molecule.
7430095	4	52	dep	acid	1201:1204	arg1	N-acetylglucosamine					1215:1233	N-acetylglucosamine	1215:1233	N-acetylglucosamine	1215:1233	The abbreviations used are: NeuAc, N-acetylneuraminic acid; GlcNAc, N-acetylglucosamine; Fuc, fucose.
7430095	4	52	dep	acid	1201:1204	arg1	GlcNAc					1207:1212	GlcNAc	1207:1212	GlcNAc	1207:1212	The abbreviations used are: NeuAc, N-acetylneuraminic acid; GlcNAc, N-acetylglucosamine; Fuc, fucose.
7430095	4	52	dep	acid	1201:1204	arg1	fucose					1241:1246	fucose	1241:1246	fucose	1241:1246	The abbreviations used are: NeuAc, N-acetylneuraminic acid; GlcNAc, N-acetylglucosamine; Fuc, fucose.
7430095	3	53	theme	NeuAc	581:585	arg1	alpha					587:591	NeuAc alpha 2	581:593	NeuAc alpha 2	581:593	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	2	54	dep	components	320:329	arg1	A-2					340:342	A-2'	340:343	A-2'	340:343	The oligosaccharide fraction was separated into four components (N, A-1, A-2', and A-2) by paper electrophoresis.
7430095	2	54	dep	components	320:329	arg1	N					332:332	N	332:332	N	332:332	The oligosaccharide fraction was separated into four components (N, A-1, A-2', and A-2) by paper electrophoresis.
7430095	2	54	dep	components	320:329	arg1	A-1					335:337	A-1	335:337	A-1	335:337	The oligosaccharide fraction was separated into four components (N, A-1, A-2', and A-2) by paper electrophoresis.
7430095	2	54	dep	components	320:329	arg1	A-2					350:352	A-2	350:352	A-2	350:352	The oligosaccharide fraction was separated into four components (N, A-1, A-2', and A-2) by paper electrophoresis.
7430095	2	54	dep	components	320:329	arg1	components					320:329	four components	315:329	four components (N, A-1, A-2', and A-2)	315:353	The oligosaccharide fraction was separated into four components (N, A-1, A-2', and A-2) by paper electrophoresis.
7430095	3	55	theme	6Gal	604:607	arg1	beta					609:612	6Gal beta 1	604:614	6Gal beta 1	604:614	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	0	56	attach	isolated	81:88	arg1	erythrocytes					101:112	human erythrocytes	95:112	human erythrocytes	95:112	Structures of the asparagine-linked sugar chains of glycophorin A. Glycophorin A isolated from human erythrocytes contains one asparagine-linked sugar chain in one molecule.
7430095	0	56	attach	isolated	81:88	arg2	A					79:79	glycophorin A. Glycophorin A	52:79	glycophorin A. Glycophorin A isolated from human erythrocytes	52:112	Structures of the asparagine-linked sugar chains of glycophorin A. Glycophorin A isolated from human erythrocytes contains one asparagine-linked sugar chain in one molecule.
7430095	3	57	theme	2Man	1018:1021	arg1	alpha					1023:1027	2Man alpha 1	1018:1029	2Man alpha 1	1018:1029	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	4	58	theme	N-acetylneuraminic	1182:1199	arg1	NeuAc					1175:1179	NeuAc	1175:1179	NeuAc	1175:1179	The abbreviations used are: NeuAc, N-acetylneuraminic acid; GlcNAc, N-acetylglucosamine; Fuc, fucose.
7430095	4	58	theme	N-acetylneuraminic	1182:1199	arg1	acid					1201:1204	N-acetylneuraminic acid	1182:1204	N-acetylneuraminic acid; GlcNAc, N-acetylglucosamine; Fuc, fucose	1182:1246	The abbreviations used are: NeuAc, N-acetylneuraminic acid; GlcNAc, N-acetylglucosamine; Fuc, fucose.
7430095	1	59	theme	oligosaccharide	223:237	arg1	chain					185:189	This sugar chain	174:189	This sugar chain	174:189	This sugar chain was successfully released as an oligosaccharide fraction by hydrazinolysis.
7430095	1	59	theme	oligosaccharide	223:237	arg1	fraction					239:246	an oligosaccharide fraction	220:246	an oligosaccharide fraction	220:246	This sugar chain was successfully released as an oligosaccharide fraction by hydrazinolysis.
7430095	3	60	theme	4GlcNAc	902:908	arg1	beta					910:913	4GlcNAc beta 1	902:915	4GlcNAc beta 1	902:915	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	3	61	theme	beta	633:636	arg1	beta					782:785	4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1	625:787	4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1	625:811	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	2	62	theme	oligosaccharide	271:285	arg1	fraction					287:294	The oligosaccharide fraction	267:294	The oligosaccharide fraction	267:294	The oligosaccharide fraction was separated into four components (N, A-1, A-2', and A-2) by paper electrophoresis.
7430095	4	63	dep	GlcNAc	1207:1212	arg1	Fuc					1236:1238	Fuc	1236:1238	Fuc	1236:1238	The abbreviations used are: NeuAc, N-acetylneuraminic acid; GlcNAc, N-acetylglucosamine; Fuc, fucose.
7430095	0	64	theme	Glycophorin	67:77	arg1	A					79:79	glycophorin A. Glycophorin A	52:79	glycophorin A. Glycophorin A isolated from human erythrocytes	52:112	Structures of the asparagine-linked sugar chains of glycophorin A. Glycophorin A isolated from human erythrocytes contains one asparagine-linked sugar chain in one molecule.
7430095	3	65	theme	4GlcNAc	1089:1095	arg1	beta					1097:1100	4GlcNAc beta 1	1089:1102	4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc	1089:1144	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	3	66	theme	4GlcNAc	994:1000	arg1	beta					1002:1005	4GlcNAc beta 1	994:1007	4GlcNAc beta 1	994:1007	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	0	67	theme	A.	64:65	arg1	A					79:79	glycophorin A. Glycophorin A	52:79	glycophorin A. Glycophorin A isolated from human erythrocytes	52:112	Structures of the asparagine-linked sugar chains of glycophorin A. Glycophorin A isolated from human erythrocytes contains one asparagine-linked sugar chain in one molecule.
7430095	3	68	dep	beta	681:684	arg1	leads					712:716	leads	712:716	leads to to 2Man alpha 1	712:735	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	3	68	dep	beta	681:684	arg1	leads					688:692	leads	688:692	leads to 4GlcNAc beta 1	688:710	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	3	68	dep	beta	681:684	arg1	leads					737:741	leads	737:741	leads to 3(6)	737:749	Complete structures of the major acidic oligosaccharides (A-1 and A-2) were elucidated by sequential exoglycosidase digestion in combination with methylation study and periodate oxidation as follows: NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(3) [Gal beta 1 leads to 4GlcNAc beta 1 leads to to 2Man alpha 1 leads to 3(6)] (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6)GlcNAc and NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 6(NeuAc alpha 2 leads to 6Gal beta 1 leads to 4GlcNAc beta 1 leads to 2Man alpha 1 leads to 3) (GlcNAc beta 1 leads to 4)Man beta 1 leads to 4GlcNAc beta 1 leads to 4(Fuc alpha 1 leads to 6) GlcNAc.
7430095	0	69	from	chain	151:155	arg1	molecule					164:171	one molecule	160:171	one molecule	160:171	Structures of the asparagine-linked sugar chains of glycophorin A. Glycophorin A isolated from human erythrocytes contains one asparagine-linked sugar chain in one molecule.
3191509	5	0	theme	trioxide	1039:1046	arg1	oxidation					1048:1056	chromium trioxide oxidation	1030:1056	chromium trioxide oxidation	1030:1056	Two ubiquitous (FW2, FW3) and three novel oligosaccharide alditols (FW5) were characterized by f.a.b.- and e.i.-m.s., combined with methylation analysis and chromium trioxide oxidation.
3191509	6	1	theme	terminal	1221:1228	arg1	residue					1230:1236	the reducing terminal residue	1208:1236	the reducing terminal residue	1208:1236	The OC 125 epitope on mucin-carried O-glycans was destroyed during reductive cleavage of the saccharides, indicating a conformational involvement of the reducing terminal residue and its mode of conjugation to the protein.
3191509	2	2	gly	glycoproteins	280:292	arg1	glycoproteins					280:292	smaller-sized glycoproteins	266:292	smaller-sized glycoproteins	266:292	phenol and separated from the bulk of smaller-sized glycoproteins by exclusion on Sephacryl S400.
3191509	2	3	theme	Sephacryl	310:318	arg1	S400					320:323	Sephacryl S400	310:323	Sephacryl S400	310:323	phenol and separated from the bulk of smaller-sized glycoproteins by exclusion on Sephacryl S400.
3191509	7	4	theme	terminal	1428:1435	arg1	groups					1444:1449	terminal sialyl groups	1428:1449	terminal sialyl groups	1428:1449	Exoglycosidase treatment of the mucin-bound antigen revealed that the epitope structure of OC 125 includes terminal beta-D-galactosyl groups, and terminal sialyl groups that are almost inaccessible to Vibrio cholerae sialidase digestion.
3191509	7	5	theme	sialyl	1437:1442	arg1	groups					1444:1449	terminal sialyl groups	1428:1449	terminal sialyl groups	1428:1449	Exoglycosidase treatment of the mucin-bound antigen revealed that the epitope structure of OC 125 includes terminal beta-D-galactosyl groups, and terminal sialyl groups that are almost inaccessible to Vibrio cholerae sialidase digestion.
3191509	0	6	from	studies	11:17	arg1	antigens					45:52	oncofetal carbohydrate antigens	22:52	oncofetal carbohydrate antigens (Ca 19-9, Ca 50, and Ca 125)	22:81	Structural studies on oncofetal carbohydrate antigens (Ca 19-9, Ca 50, and Ca 125) carried by O-linked sialyloligosaccharides on human amniotic mucins.
3191509	4	7	theme	alditols	773:780	arg1	purification					745:756	purification	745:756	purification of the derived alditols by gel-permeation chromatography on Bio-Gel P-4 or high performance liquid chromatography	745:870	The structures of the respective mucin-linked saccharides responsible for Ca 50-, Ca 19-9-, and Lea-related antigenic activities were analyzed before or after reductive beta-elimination from sialylglycoproteins, and purification of the derived alditols by gel-permeation chromatography on Bio-Gel P-4 or high performance liquid chromatography.
3191509	4	7	theme	alditols	773:780	arg1	beta-elimination					698:713	reductive beta-elimination	688:713	reductive beta-elimination from sialylglycoproteins	688:738	The structures of the respective mucin-linked saccharides responsible for Ca 50-, Ca 19-9-, and Lea-related antigenic activities were analyzed before or after reductive beta-elimination from sialylglycoproteins, and purification of the derived alditols by gel-permeation chromatography on Bio-Gel P-4 or high performance liquid chromatography.
3191509	1	8	theme	45	219:220	arg1	%					221:221	%	221:221	%	221:221	Mucins were extracted from human amniotic fluid in the presence of 45% vol.
3191509	6	9	theme	reductive	1126:1134	arg1	cleavage					1136:1143	reductive cleavage	1126:1143	reductive cleavage of the saccharides	1126:1162	The OC 125 epitope on mucin-carried O-glycans was destroyed during reductive cleavage of the saccharides, indicating a conformational involvement of the reducing terminal residue and its mode of conjugation to the protein.
3191509	7	10	theme	OC	1373:1374	arg1	structure					1360:1368	the epitope structure	1348:1368	the epitope structure of OC 125	1348:1378	Exoglycosidase treatment of the mucin-bound antigen revealed that the epitope structure of OC 125 includes terminal beta-D-galactosyl groups, and terminal sialyl groups that are almost inaccessible to Vibrio cholerae sialidase digestion.
3191509	1	11	theme	%	221:221	arg1	vol					223:225	45% vol	219:225	45% vol	219:225	Mucins were extracted from human amniotic fluid in the presence of 45% vol.
3191509	3	12	dep	antibodies	466:475	arg1	H					511:511	49 H 8	508:513	49 H 8	508:513	The mucin-fraction FW, which still contained a minute proportion of mannose, strongly expressed oncofetal antigens recognized by monoclonal antibodies C 50, NS 19-9, OC 125, Leu M1, 49 H 8, and 115 C 2.
3191509	3	12	dep	antibodies	466:475	arg1	C					477:477	C 50	477:480	C 50	477:480	The mucin-fraction FW, which still contained a minute proportion of mannose, strongly expressed oncofetal antigens recognized by monoclonal antibodies C 50, NS 19-9, OC 125, Leu M1, 49 H 8, and 115 C 2.
3191509	3	12	dep	antibodies	466:475	arg1	M1					504:505	Leu M1	500:505	Leu M1	500:505	The mucin-fraction FW, which still contained a minute proportion of mannose, strongly expressed oncofetal antigens recognized by monoclonal antibodies C 50, NS 19-9, OC 125, Leu M1, 49 H 8, and 115 C 2.
3191509	3	12	dep	antibodies	466:475	arg1	19-9					486:489	NS 19-9	483:489	NS 19-9	483:489	The mucin-fraction FW, which still contained a minute proportion of mannose, strongly expressed oncofetal antigens recognized by monoclonal antibodies C 50, NS 19-9, OC 125, Leu M1, 49 H 8, and 115 C 2.
3191509	3	12	dep	antibodies	466:475	arg1	C					524:524	115 C 2	520:526	115 C 2	520:526	The mucin-fraction FW, which still contained a minute proportion of mannose, strongly expressed oncofetal antigens recognized by monoclonal antibodies C 50, NS 19-9, OC 125, Leu M1, 49 H 8, and 115 C 2.
3191509	3	12	dep	antibodies	466:475	arg1	OC					492:493	OC 125	492:497	OC 125	492:497	The mucin-fraction FW, which still contained a minute proportion of mannose, strongly expressed oncofetal antigens recognized by monoclonal antibodies C 50, NS 19-9, OC 125, Leu M1, 49 H 8, and 115 C 2.
3191509	3	12	dep	antibodies	466:475	arg1	antibodies					466:475	monoclonal antibodies C 50, NS 19-9, OC 125, Leu M1, 49 H 8, and 115 C 2	455:526	monoclonal antibodies C 50, NS 19-9, OC 125, Leu M1, 49 H 8, and 115 C 2	455:526	The mucin-fraction FW, which still contained a minute proportion of mannose, strongly expressed oncofetal antigens recognized by monoclonal antibodies C 50, NS 19-9, OC 125, Leu M1, 49 H 8, and 115 C 2.
3191509	7	13	theme	beta-D-galactosyl	1398:1414	arg1	groups					1416:1421	terminal beta-D-galactosyl groups	1389:1421	terminal beta-D-galactosyl groups	1389:1421	Exoglycosidase treatment of the mucin-bound antigen revealed that the epitope structure of OC 125 includes terminal beta-D-galactosyl groups, and terminal sialyl groups that are almost inaccessible to Vibrio cholerae sialidase digestion.
3191509	4	14	theme	gel-permeation	785:798	arg1	chromatography					800:813	gel-permeation chromatography	785:813	gel-permeation chromatography on Bio-Gel P-4	785:828	The structures of the respective mucin-linked saccharides responsible for Ca 50-, Ca 19-9-, and Lea-related antigenic activities were analyzed before or after reductive beta-elimination from sialylglycoproteins, and purification of the derived alditols by gel-permeation chromatography on Bio-Gel P-4 or high performance liquid chromatography.
3191509	2	15	from	exclusion	297:305	arg1	S400					320:323	Sephacryl S400	310:323	Sephacryl S400	310:323	phenol and separated from the bulk of smaller-sized glycoproteins by exclusion on Sephacryl S400.
3191509	4	16	theme	Ca	603:604	arg1	50-					606:608	Ca 50-	603:608	Ca 50-	603:608	The structures of the respective mucin-linked saccharides responsible for Ca 50-, Ca 19-9-, and Lea-related antigenic activities were analyzed before or after reductive beta-elimination from sialylglycoproteins, and purification of the derived alditols by gel-permeation chromatography on Bio-Gel P-4 or high performance liquid chromatography.
3191509	0	17	link	O-linked	94:101	arg1	sialyloligosaccharides					103:124	O-linked sialyloligosaccharides	94:124	O-linked sialyloligosaccharides on human amniotic mucins	94:149	Structural studies on oncofetal carbohydrate antigens (Ca 19-9, Ca 50, and Ca 125) carried by O-linked sialyloligosaccharides on human amniotic mucins.
3191509	1	18	theme	vol	223:225	arg1	presence					207:214	the presence	203:214	the presence of 45% vol	203:225	Mucins were extracted from human amniotic fluid in the presence of 45% vol.
3191509	5	19	theme	methylation	1005:1015	arg1	analysis					1017:1024	methylation analysis	1005:1024	methylation analysis	1005:1024	Two ubiquitous (FW2, FW3) and three novel oligosaccharide alditols (FW5) were characterized by f.a.b.- and e.i.-m.s., combined with methylation analysis and chromium trioxide oxidation.
3191509	3	20	contain	contained	361:369	arg1	FW					345:346	The mucin-fraction FW	326:346	The mucin-fraction FW	326:346	The mucin-fraction FW, which still contained a minute proportion of mannose, strongly expressed oncofetal antigens recognized by monoclonal antibodies C 50, NS 19-9, OC 125, Leu M1, 49 H 8, and 115 C 2.
3191509	3	20	contain	contained	361:369	arg2	proportion					380:389	a minute proportion	371:389	a minute proportion of mannose	371:400	The mucin-fraction FW, which still contained a minute proportion of mannose, strongly expressed oncofetal antigens recognized by monoclonal antibodies C 50, NS 19-9, OC 125, Leu M1, 49 H 8, and 115 C 2.
3191509	3	21	theme	NS	483:484	arg1	19-9					486:489	NS 19-9	483:489	NS 19-9	483:489	The mucin-fraction FW, which still contained a minute proportion of mannose, strongly expressed oncofetal antigens recognized by monoclonal antibodies C 50, NS 19-9, OC 125, Leu M1, 49 H 8, and 115 C 2.
3191509	4	22	theme	mucin-linked	562:573	arg1	saccharides					575:585	the respective mucin-linked saccharides	547:585	the respective mucin-linked saccharides responsible for Ca 50-, Ca 19-9-, and Lea-related antigenic activities	547:656	The structures of the respective mucin-linked saccharides responsible for Ca 50-, Ca 19-9-, and Lea-related antigenic activities were analyzed before or after reductive beta-elimination from sialylglycoproteins, and purification of the derived alditols by gel-permeation chromatography on Bio-Gel P-4 or high performance liquid chromatography.
3191509	0	23	from	sialyloligosaccharides	103:124	arg1	mucins					144:149	human amniotic mucins	129:149	human amniotic mucins	129:149	Structural studies on oncofetal carbohydrate antigens (Ca 19-9, Ca 50, and Ca 125) carried by O-linked sialyloligosaccharides on human amniotic mucins.
3191509	6	24	theme	conformational	1178:1191	arg1	involvement					1193:1203	a conformational involvement	1176:1203	a conformational involvement of the reducing terminal residue	1176:1236	The OC 125 epitope on mucin-carried O-glycans was destroyed during reductive cleavage of the saccharides, indicating a conformational involvement of the reducing terminal residue and its mode of conjugation to the protein.
3191509	4	25	gly	sialylglycoproteins	720:738	arg1	sialylglycoproteins					720:738	sialylglycoproteins	720:738	sialylglycoproteins	720:738	The structures of the respective mucin-linked saccharides responsible for Ca 50-, Ca 19-9-, and Lea-related antigenic activities were analyzed before or after reductive beta-elimination from sialylglycoproteins, and purification of the derived alditols by gel-permeation chromatography on Bio-Gel P-4 or high performance liquid chromatography.
3191509	3	26	theme	mannose	394:400	arg1	proportion					380:389	a minute proportion	371:389	a minute proportion of mannose	371:400	The mucin-fraction FW, which still contained a minute proportion of mannose, strongly expressed oncofetal antigens recognized by monoclonal antibodies C 50, NS 19-9, OC 125, Leu M1, 49 H 8, and 115 C 2.
3191509	7	27	theme	terminal	1389:1396	arg1	groups					1416:1421	terminal beta-D-galactosyl groups	1389:1421	terminal beta-D-galactosyl groups	1389:1421	Exoglycosidase treatment of the mucin-bound antigen revealed that the epitope structure of OC 125 includes terminal beta-D-galactosyl groups, and terminal sialyl groups that are almost inaccessible to Vibrio cholerae sialidase digestion.
3191509	4	28	theme	derived	765:771	arg1	alditols					773:780	the derived alditols	761:780	the derived alditols	761:780	The structures of the respective mucin-linked saccharides responsible for Ca 50-, Ca 19-9-, and Lea-related antigenic activities were analyzed before or after reductive beta-elimination from sialylglycoproteins, and purification of the derived alditols by gel-permeation chromatography on Bio-Gel P-4 or high performance liquid chromatography.
3191509	3	29	theme	Leu	500:502	arg1	antibodies					466:475	monoclonal antibodies C 50, NS 19-9, OC 125, Leu M1, 49 H 8, and 115 C 2	455:526	monoclonal antibodies C 50, NS 19-9, OC 125, Leu M1, 49 H 8, and 115 C 2	455:526	The mucin-fraction FW, which still contained a minute proportion of mannose, strongly expressed oncofetal antigens recognized by monoclonal antibodies C 50, NS 19-9, OC 125, Leu M1, 49 H 8, and 115 C 2.
3191509	3	29	theme	Leu	500:502	arg1	M1					504:505	Leu M1	500:505	Leu M1	500:505	The mucin-fraction FW, which still contained a minute proportion of mannose, strongly expressed oncofetal antigens recognized by monoclonal antibodies C 50, NS 19-9, OC 125, Leu M1, 49 H 8, and 115 C 2.
3191509	3	30	theme	minute	373:378	arg1	proportion					380:389	a minute proportion	371:389	a minute proportion of mannose	371:400	The mucin-fraction FW, which still contained a minute proportion of mannose, strongly expressed oncofetal antigens recognized by monoclonal antibodies C 50, NS 19-9, OC 125, Leu M1, 49 H 8, and 115 C 2.
3191509	0	31	theme	Structural	0:9	arg1	studies					11:17	Structural studies	0:17	Structural studies on oncofetal carbohydrate antigens (Ca 19-9, Ca 50, and Ca 125)	0:81	Structural studies on oncofetal carbohydrate antigens (Ca 19-9, Ca 50, and Ca 125) carried by O-linked sialyloligosaccharides on human amniotic mucins.
3191509	4	32	theme	Ca	611:612	arg1	19-9-					614:618	Ca 19-9-	611:618	Ca 19-9-	611:618	The structures of the respective mucin-linked saccharides responsible for Ca 50-, Ca 19-9-, and Lea-related antigenic activities were analyzed before or after reductive beta-elimination from sialylglycoproteins, and purification of the derived alditols by gel-permeation chromatography on Bio-Gel P-4 or high performance liquid chromatography.
3191509	7	33	theme	epitope	1352:1358	arg1	structure					1360:1368	the epitope structure	1348:1368	the epitope structure of OC 125	1348:1378	Exoglycosidase treatment of the mucin-bound antigen revealed that the epitope structure of OC 125 includes terminal beta-D-galactosyl groups, and terminal sialyl groups that are almost inaccessible to Vibrio cholerae sialidase digestion.
3191509	4	34	theme	respective	551:560	arg1	saccharides					575:585	the respective mucin-linked saccharides	547:585	the respective mucin-linked saccharides responsible for Ca 50-, Ca 19-9-, and Lea-related antigenic activities	547:656	The structures of the respective mucin-linked saccharides responsible for Ca 50-, Ca 19-9-, and Lea-related antigenic activities were analyzed before or after reductive beta-elimination from sialylglycoproteins, and purification of the derived alditols by gel-permeation chromatography on Bio-Gel P-4 or high performance liquid chromatography.
3191509	0	35	theme	oncofetal	22:30	arg1	antigens					45:52	oncofetal carbohydrate antigens	22:52	oncofetal carbohydrate antigens (Ca 19-9, Ca 50, and Ca 125)	22:81	Structural studies on oncofetal carbohydrate antigens (Ca 19-9, Ca 50, and Ca 125) carried by O-linked sialyloligosaccharides on human amniotic mucins.
3191509	4	36	theme	performance	838:848	arg1	chromatography					857:870	high performance liquid chromatography	833:870	high performance liquid chromatography	833:870	The structures of the respective mucin-linked saccharides responsible for Ca 50-, Ca 19-9-, and Lea-related antigenic activities were analyzed before or after reductive beta-elimination from sialylglycoproteins, and purification of the derived alditols by gel-permeation chromatography on Bio-Gel P-4 or high performance liquid chromatography.
3191509	6	37	theme	reducing	1212:1219	arg1	residue					1230:1236	the reducing terminal residue	1208:1236	the reducing terminal residue	1208:1236	The OC 125 epitope on mucin-carried O-glycans was destroyed during reductive cleavage of the saccharides, indicating a conformational involvement of the reducing terminal residue and its mode of conjugation to the protein.
3191509	4	38	theme	antigenic	637:645	arg1	activities					647:656	Lea-related antigenic activities	625:656	Lea-related antigenic activities	625:656	The structures of the respective mucin-linked saccharides responsible for Ca 50-, Ca 19-9-, and Lea-related antigenic activities were analyzed before or after reductive beta-elimination from sialylglycoproteins, and purification of the derived alditols by gel-permeation chromatography on Bio-Gel P-4 or high performance liquid chromatography.
3191509	7	39	theme	mucin-bound	1314:1324	arg1	antigen					1326:1332	the mucin-bound antigen	1310:1332	the mucin-bound antigen	1310:1332	Exoglycosidase treatment of the mucin-bound antigen revealed that the epitope structure of OC 125 includes terminal beta-D-galactosyl groups, and terminal sialyl groups that are almost inaccessible to Vibrio cholerae sialidase digestion.
3191509	3	40	theme	mucin-fraction	330:343	arg1	FW					345:346	The mucin-fraction FW	326:346	The mucin-fraction FW	326:346	The mucin-fraction FW, which still contained a minute proportion of mannose, strongly expressed oncofetal antigens recognized by monoclonal antibodies C 50, NS 19-9, OC 125, Leu M1, 49 H 8, and 115 C 2.
3191509	4	41	theme	high	833:836	arg1	chromatography					857:870	high performance liquid chromatography	833:870	high performance liquid chromatography	833:870	The structures of the respective mucin-linked saccharides responsible for Ca 50-, Ca 19-9-, and Lea-related antigenic activities were analyzed before or after reductive beta-elimination from sialylglycoproteins, and purification of the derived alditols by gel-permeation chromatography on Bio-Gel P-4 or high performance liquid chromatography.
3191509	4	42	from	chromatography	857:870	arg1	P-4					826:828	Bio-Gel P-4	818:828	Bio-Gel P-4	818:828	The structures of the respective mucin-linked saccharides responsible for Ca 50-, Ca 19-9-, and Lea-related antigenic activities were analyzed before or after reductive beta-elimination from sialylglycoproteins, and purification of the derived alditols by gel-permeation chromatography on Bio-Gel P-4 or high performance liquid chromatography.
3191509	4	43	theme	Lea-related	625:635	arg1	activities					647:656	Lea-related antigenic activities	625:656	Lea-related antigenic activities	625:656	The structures of the respective mucin-linked saccharides responsible for Ca 50-, Ca 19-9-, and Lea-related antigenic activities were analyzed before or after reductive beta-elimination from sialylglycoproteins, and purification of the derived alditols by gel-permeation chromatography on Bio-Gel P-4 or high performance liquid chromatography.
3191509	6	44	from	epitope	1070:1076	arg1	O-glycans					1095:1103	mucin-carried O-glycans	1081:1103	mucin-carried O-glycans	1081:1103	The OC 125 epitope on mucin-carried O-glycans was destroyed during reductive cleavage of the saccharides, indicating a conformational involvement of the reducing terminal residue and its mode of conjugation to the protein.
3191509	3	45	theme	oncofetal	422:430	arg1	antigens					432:439	oncofetal antigens	422:439	oncofetal antigens recognized by monoclonal antibodies C 50, NS 19-9, OC 125, Leu M1, 49 H 8, and 115 C 2	422:526	The mucin-fraction FW, which still contained a minute proportion of mannose, strongly expressed oncofetal antigens recognized by monoclonal antibodies C 50, NS 19-9, OC 125, Leu M1, 49 H 8, and 115 C 2.
3191509	4	46	link	derived	765:771	arg1	alditols					773:780	the derived alditols	761:780	the derived alditols	761:780	The structures of the respective mucin-linked saccharides responsible for Ca 50-, Ca 19-9-, and Lea-related antigenic activities were analyzed before or after reductive beta-elimination from sialylglycoproteins, and purification of the derived alditols by gel-permeation chromatography on Bio-Gel P-4 or high performance liquid chromatography.
3191509	0	47	theme	O-linked	94:101	arg1	sialyloligosaccharides					103:124	O-linked sialyloligosaccharides	94:124	O-linked sialyloligosaccharides on human amniotic mucins	94:149	Structural studies on oncofetal carbohydrate antigens (Ca 19-9, Ca 50, and Ca 125) carried by O-linked sialyloligosaccharides on human amniotic mucins.
3191509	7	48	theme	cholerae	1490:1497	arg1	digestion					1509:1517	Vibrio cholerae sialidase digestion	1483:1517	Vibrio cholerae sialidase digestion	1483:1517	Exoglycosidase treatment of the mucin-bound antigen revealed that the epitope structure of OC 125 includes terminal beta-D-galactosyl groups, and terminal sialyl groups that are almost inaccessible to Vibrio cholerae sialidase digestion.
3191509	4	49	link	mucin-linked	562:573	arg1	saccharides					575:585	the respective mucin-linked saccharides	547:585	the respective mucin-linked saccharides responsible for Ca 50-, Ca 19-9-, and Lea-related antigenic activities	547:656	The structures of the respective mucin-linked saccharides responsible for Ca 50-, Ca 19-9-, and Lea-related antigenic activities were analyzed before or after reductive beta-elimination from sialylglycoproteins, and purification of the derived alditols by gel-permeation chromatography on Bio-Gel P-4 or high performance liquid chromatography.
3191509	1	50	theme	human	179:183	arg1	fluid					194:198	human amniotic fluid	179:198	human amniotic fluid	179:198	Mucins were extracted from human amniotic fluid in the presence of 45% vol.
3191509	0	51	theme	carbohydrate	32:43	arg1	antigens					45:52	oncofetal carbohydrate antigens	22:52	oncofetal carbohydrate antigens (Ca 19-9, Ca 50, and Ca 125)	22:81	Structural studies on oncofetal carbohydrate antigens (Ca 19-9, Ca 50, and Ca 125) carried by O-linked sialyloligosaccharides on human amniotic mucins.
3191509	4	52	theme	liquid	850:855	arg1	chromatography					857:870	high performance liquid chromatography	833:870	high performance liquid chromatography	833:870	The structures of the respective mucin-linked saccharides responsible for Ca 50-, Ca 19-9-, and Lea-related antigenic activities were analyzed before or after reductive beta-elimination from sialylglycoproteins, and purification of the derived alditols by gel-permeation chromatography on Bio-Gel P-4 or high performance liquid chromatography.
3191509	6	53	theme	conjugation	1254:1264	arg1	mode					1246:1249	its mode	1242:1249	its mode of conjugation to the protein	1242:1279	The OC 125 epitope on mucin-carried O-glycans was destroyed during reductive cleavage of the saccharides, indicating a conformational involvement of the reducing terminal residue and its mode of conjugation to the protein.
3191509	6	53	theme	conjugation	1254:1264	arg1	involvement					1193:1203	a conformational involvement	1176:1203	a conformational involvement of the reducing terminal residue	1176:1236	The OC 125 epitope on mucin-carried O-glycans was destroyed during reductive cleavage of the saccharides, indicating a conformational involvement of the reducing terminal residue and its mode of conjugation to the protein.
3191509	6	54	theme	saccharides	1152:1162	arg1	cleavage					1136:1143	reductive cleavage	1126:1143	reductive cleavage of the saccharides	1126:1162	The OC 125 epitope on mucin-carried O-glycans was destroyed during reductive cleavage of the saccharides, indicating a conformational involvement of the reducing terminal residue and its mode of conjugation to the protein.
3191509	1	55	theme	amniotic	185:192	arg1	fluid					194:198	human amniotic fluid	179:198	human amniotic fluid	179:198	Mucins were extracted from human amniotic fluid in the presence of 45% vol.
3191509	0	56	theme	Ca	55:56	arg1	19-9					58:61	Ca 19-9	55:61	Ca 19-9	55:61	Structural studies on oncofetal carbohydrate antigens (Ca 19-9, Ca 50, and Ca 125) carried by O-linked sialyloligosaccharides on human amniotic mucins.
3191509	4	57	theme	Bio-Gel	818:824	arg1	P-4					826:828	Bio-Gel P-4	818:828	Bio-Gel P-4	818:828	The structures of the respective mucin-linked saccharides responsible for Ca 50-, Ca 19-9-, and Lea-related antigenic activities were analyzed before or after reductive beta-elimination from sialylglycoproteins, and purification of the derived alditols by gel-permeation chromatography on Bio-Gel P-4 or high performance liquid chromatography.
3191509	0	58	dep	antigens	45:52	arg1	Ca					64:65	Ca 50	64:68	Ca 50	64:68	Structural studies on oncofetal carbohydrate antigens (Ca 19-9, Ca 50, and Ca 125) carried by O-linked sialyloligosaccharides on human amniotic mucins.
3191509	0	58	dep	antigens	45:52	arg1	19-9					58:61	Ca 19-9	55:61	Ca 19-9	55:61	Structural studies on oncofetal carbohydrate antigens (Ca 19-9, Ca 50, and Ca 125) carried by O-linked sialyloligosaccharides on human amniotic mucins.
3191509	0	58	dep	antigens	45:52	arg1	Ca					75:76	Ca 125	75:80	Ca 125	75:80	Structural studies on oncofetal carbohydrate antigens (Ca 19-9, Ca 50, and Ca 125) carried by O-linked sialyloligosaccharides on human amniotic mucins.
3191509	5	59	theme	chromium	1030:1037	arg1	oxidation					1048:1056	chromium trioxide oxidation	1030:1056	chromium trioxide oxidation	1030:1056	Two ubiquitous (FW2, FW3) and three novel oligosaccharide alditols (FW5) were characterized by f.a.b.- and e.i.-m.s., combined with methylation analysis and chromium trioxide oxidation.
3191509	4	60	from	sialylglycoproteins	720:738	arg1	purification					745:756	purification	745:756	purification of the derived alditols by gel-permeation chromatography on Bio-Gel P-4 or high performance liquid chromatography	745:870	The structures of the respective mucin-linked saccharides responsible for Ca 50-, Ca 19-9-, and Lea-related antigenic activities were analyzed before or after reductive beta-elimination from sialylglycoproteins, and purification of the derived alditols by gel-permeation chromatography on Bio-Gel P-4 or high performance liquid chromatography.
3191509	4	60	from	sialylglycoproteins	720:738	arg1	beta-elimination					698:713	reductive beta-elimination	688:713	reductive beta-elimination from sialylglycoproteins	688:738	The structures of the respective mucin-linked saccharides responsible for Ca 50-, Ca 19-9-, and Lea-related antigenic activities were analyzed before or after reductive beta-elimination from sialylglycoproteins, and purification of the derived alditols by gel-permeation chromatography on Bio-Gel P-4 or high performance liquid chromatography.
3191509	3	61	theme	monoclonal	455:464	arg1	H					511:511	49 H 8	508:513	49 H 8	508:513	The mucin-fraction FW, which still contained a minute proportion of mannose, strongly expressed oncofetal antigens recognized by monoclonal antibodies C 50, NS 19-9, OC 125, Leu M1, 49 H 8, and 115 C 2.
3191509	3	61	theme	monoclonal	455:464	arg1	C					477:477	C 50	477:480	C 50	477:480	The mucin-fraction FW, which still contained a minute proportion of mannose, strongly expressed oncofetal antigens recognized by monoclonal antibodies C 50, NS 19-9, OC 125, Leu M1, 49 H 8, and 115 C 2.
3191509	3	61	theme	monoclonal	455:464	arg1	M1					504:505	Leu M1	500:505	Leu M1	500:505	The mucin-fraction FW, which still contained a minute proportion of mannose, strongly expressed oncofetal antigens recognized by monoclonal antibodies C 50, NS 19-9, OC 125, Leu M1, 49 H 8, and 115 C 2.
3191509	3	61	theme	monoclonal	455:464	arg1	C					524:524	115 C 2	520:526	115 C 2	520:526	The mucin-fraction FW, which still contained a minute proportion of mannose, strongly expressed oncofetal antigens recognized by monoclonal antibodies C 50, NS 19-9, OC 125, Leu M1, 49 H 8, and 115 C 2.
3191509	3	61	theme	monoclonal	455:464	arg1	OC					492:493	OC 125	492:497	OC 125	492:497	The mucin-fraction FW, which still contained a minute proportion of mannose, strongly expressed oncofetal antigens recognized by monoclonal antibodies C 50, NS 19-9, OC 125, Leu M1, 49 H 8, and 115 C 2.
3191509	3	61	theme	monoclonal	455:464	arg1	antibodies					466:475	monoclonal antibodies C 50, NS 19-9, OC 125, Leu M1, 49 H 8, and 115 C 2	455:526	monoclonal antibodies C 50, NS 19-9, OC 125, Leu M1, 49 H 8, and 115 C 2	455:526	The mucin-fraction FW, which still contained a minute proportion of mannose, strongly expressed oncofetal antigens recognized by monoclonal antibodies C 50, NS 19-9, OC 125, Leu M1, 49 H 8, and 115 C 2.
3191509	5	62	theme	oligosaccharide	915:929	arg1	FW5					941:943	FW5	941:943	FW5	941:943	Two ubiquitous (FW2, FW3) and three novel oligosaccharide alditols (FW5) were characterized by f.a.b.- and e.i.-m.s., combined with methylation analysis and chromium trioxide oxidation.
3191509	5	62	theme	oligosaccharide	915:929	arg1	alditols					931:938	novel oligosaccharide alditols	909:938	three novel oligosaccharide alditols (FW5)	903:944	Two ubiquitous (FW2, FW3) and three novel oligosaccharide alditols (FW5) were characterized by f.a.b.- and e.i.-m.s., combined with methylation analysis and chromium trioxide oxidation.
3191509	0	63	theme	amniotic	135:142	arg1	mucins					144:149	human amniotic mucins	129:149	human amniotic mucins	129:149	Structural studies on oncofetal carbohydrate antigens (Ca 19-9, Ca 50, and Ca 125) carried by O-linked sialyloligosaccharides on human amniotic mucins.
3191509	7	64	theme	Exoglycosidase	1282:1295	arg1	treatment					1297:1305	Exoglycosidase treatment	1282:1305	Exoglycosidase treatment of the mucin-bound antigen	1282:1332	Exoglycosidase treatment of the mucin-bound antigen revealed that the epitope structure of OC 125 includes terminal beta-D-galactosyl groups, and terminal sialyl groups that are almost inaccessible to Vibrio cholerae sialidase digestion.
3191509	3	65	theme	115	520:522	arg1	antibodies					466:475	monoclonal antibodies C 50, NS 19-9, OC 125, Leu M1, 49 H 8, and 115 C 2	455:526	monoclonal antibodies C 50, NS 19-9, OC 125, Leu M1, 49 H 8, and 115 C 2	455:526	The mucin-fraction FW, which still contained a minute proportion of mannose, strongly expressed oncofetal antigens recognized by monoclonal antibodies C 50, NS 19-9, OC 125, Leu M1, 49 H 8, and 115 C 2.
3191509	3	65	theme	115	520:522	arg1	C					524:524	115 C 2	520:526	115 C 2	520:526	The mucin-fraction FW, which still contained a minute proportion of mannose, strongly expressed oncofetal antigens recognized by monoclonal antibodies C 50, NS 19-9, OC 125, Leu M1, 49 H 8, and 115 C 2.
3191509	7	66	theme	antigen	1326:1332	arg1	treatment					1297:1305	Exoglycosidase treatment	1282:1305	Exoglycosidase treatment of the mucin-bound antigen	1282:1332	Exoglycosidase treatment of the mucin-bound antigen revealed that the epitope structure of OC 125 includes terminal beta-D-galactosyl groups, and terminal sialyl groups that are almost inaccessible to Vibrio cholerae sialidase digestion.
3191509	2	67	theme	glycoproteins	280:292	arg1	bulk					258:261	the bulk	254:261	the bulk of smaller-sized glycoproteins	254:292	phenol and separated from the bulk of smaller-sized glycoproteins by exclusion on Sephacryl S400.
3191509	6	68	theme	OC	1063:1064	arg1	epitope					1070:1076	The OC 125 epitope	1059:1076	The OC 125 epitope on mucin-carried O-glycans	1059:1103	The OC 125 epitope on mucin-carried O-glycans was destroyed during reductive cleavage of the saccharides, indicating a conformational involvement of the reducing terminal residue and its mode of conjugation to the protein.
3191509	0	69	theme	human	129:133	arg1	mucins					144:149	human amniotic mucins	129:149	human amniotic mucins	129:149	Structural studies on oncofetal carbohydrate antigens (Ca 19-9, Ca 50, and Ca 125) carried by O-linked sialyloligosaccharides on human amniotic mucins.
3191509	5	70	dep	ubiquitous	877:886	arg1	FW3					894:896	FW3	894:896	FW3	894:896	Two ubiquitous (FW2, FW3) and three novel oligosaccharide alditols (FW5) were characterized by f.a.b.- and e.i.-m.s., combined with methylation analysis and chromium trioxide oxidation.
3191509	5	70	dep	ubiquitous	877:886	arg1	FW2					889:891	FW2	889:891	FW2	889:891	Two ubiquitous (FW2, FW3) and three novel oligosaccharide alditols (FW5) were characterized by f.a.b.- and e.i.-m.s., combined with methylation analysis and chromium trioxide oxidation.
3191509	2	71	theme	smaller-sized	266:278	arg1	glycoproteins					280:292	smaller-sized glycoproteins	266:292	smaller-sized glycoproteins	266:292	phenol and separated from the bulk of smaller-sized glycoproteins by exclusion on Sephacryl S400.
3191509	6	72	theme	residue	1230:1236	arg1	mode					1246:1249	its mode	1242:1249	its mode of conjugation to the protein	1242:1279	The OC 125 epitope on mucin-carried O-glycans was destroyed during reductive cleavage of the saccharides, indicating a conformational involvement of the reducing terminal residue and its mode of conjugation to the protein.
3191509	6	72	theme	residue	1230:1236	arg1	involvement					1193:1203	a conformational involvement	1176:1203	a conformational involvement of the reducing terminal residue	1176:1236	The OC 125 epitope on mucin-carried O-glycans was destroyed during reductive cleavage of the saccharides, indicating a conformational involvement of the reducing terminal residue and its mode of conjugation to the protein.
3191509	5	73	dep	three	903:907	arg1	FW5					941:943	FW5	941:943	FW5	941:943	Two ubiquitous (FW2, FW3) and three novel oligosaccharide alditols (FW5) were characterized by f.a.b.- and e.i.-m.s., combined with methylation analysis and chromium trioxide oxidation.
3191509	5	73	dep	three	903:907	arg1	alditols					931:938	novel oligosaccharide alditols	909:938	three novel oligosaccharide alditols (FW5)	903:944	Two ubiquitous (FW2, FW3) and three novel oligosaccharide alditols (FW5) were characterized by f.a.b.- and e.i.-m.s., combined with methylation analysis and chromium trioxide oxidation.
3191509	5	74	theme	novel	909:913	arg1	FW5					941:943	FW5	941:943	FW5	941:943	Two ubiquitous (FW2, FW3) and three novel oligosaccharide alditols (FW5) were characterized by f.a.b.- and e.i.-m.s., combined with methylation analysis and chromium trioxide oxidation.
3191509	5	74	theme	novel	909:913	arg1	alditols					931:938	novel oligosaccharide alditols	909:938	three novel oligosaccharide alditols (FW5)	903:944	Two ubiquitous (FW2, FW3) and three novel oligosaccharide alditols (FW5) were characterized by f.a.b.- and e.i.-m.s., combined with methylation analysis and chromium trioxide oxidation.
3191509	4	75	theme	responsible	587:597	arg1	saccharides					575:585	the respective mucin-linked saccharides	547:585	the respective mucin-linked saccharides responsible for Ca 50-, Ca 19-9-, and Lea-related antigenic activities	547:656	The structures of the respective mucin-linked saccharides responsible for Ca 50-, Ca 19-9-, and Lea-related antigenic activities were analyzed before or after reductive beta-elimination from sialylglycoproteins, and purification of the derived alditols by gel-permeation chromatography on Bio-Gel P-4 or high performance liquid chromatography.
3191509	6	76	theme	mucin-carried	1081:1093	arg1	O-glycans					1095:1103	mucin-carried O-glycans	1081:1103	mucin-carried O-glycans	1081:1103	The OC 125 epitope on mucin-carried O-glycans was destroyed during reductive cleavage of the saccharides, indicating a conformational involvement of the reducing terminal residue and its mode of conjugation to the protein.
3191509	7	77	theme	sialidase	1499:1507	arg1	digestion					1509:1517	Vibrio cholerae sialidase digestion	1483:1517	Vibrio cholerae sialidase digestion	1483:1517	Exoglycosidase treatment of the mucin-bound antigen revealed that the epitope structure of OC 125 includes terminal beta-D-galactosyl groups, and terminal sialyl groups that are almost inaccessible to Vibrio cholerae sialidase digestion.
3191509	4	78	from	chromatography	800:813	arg1	P-4					826:828	Bio-Gel P-4	818:828	Bio-Gel P-4	818:828	The structures of the respective mucin-linked saccharides responsible for Ca 50-, Ca 19-9-, and Lea-related antigenic activities were analyzed before or after reductive beta-elimination from sialylglycoproteins, and purification of the derived alditols by gel-permeation chromatography on Bio-Gel P-4 or high performance liquid chromatography.
3191509	4	79	theme	reductive	688:696	arg1	beta-elimination					698:713	reductive beta-elimination	688:713	reductive beta-elimination from sialylglycoproteins	688:738	The structures of the respective mucin-linked saccharides responsible for Ca 50-, Ca 19-9-, and Lea-related antigenic activities were analyzed before or after reductive beta-elimination from sialylglycoproteins, and purification of the derived alditols by gel-permeation chromatography on Bio-Gel P-4 or high performance liquid chromatography.
3191509	4	80	theme	saccharides	575:585	arg1	structures					533:542	The structures	529:542	The structures of the respective mucin-linked saccharides responsible for Ca 50-, Ca 19-9-, and Lea-related antigenic activities	529:656	The structures of the respective mucin-linked saccharides responsible for Ca 50-, Ca 19-9-, and Lea-related antigenic activities were analyzed before or after reductive beta-elimination from sialylglycoproteins, and purification of the derived alditols by gel-permeation chromatography on Bio-Gel P-4 or high performance liquid chromatography.
3191509	7	81	theme	Vibrio	1483:1488	arg1	cholerae					1490:1497	Vibrio cholerae	1483:1497	Vibrio cholerae sialidase digestion	1483:1517	Exoglycosidase treatment of the mucin-bound antigen revealed that the epitope structure of OC 125 includes terminal beta-D-galactosyl groups, and terminal sialyl groups that are almost inaccessible to Vibrio cholerae sialidase digestion.
1730235	8	0	theme	blood-group-A	1091:1103	arg1	determinants					1105:1116	blood-group-A determinants	1091:1116	blood-group-A determinants in the small intestine	1091:1139	The other strain (GOT-BW) expressed blood-group-A determinants in the small intestine.
1730235	6	1	theme	beta	806:809	arg1	2					787:787	2	787:787	2	787:787	Blood-group-H types 1 (Fuc alpha 1-2Gal beta 1-3GlcNAc) and 2(Fuc alpha 1-2Gal beta 1-4GlcNAc) were found in the small and large intestines of both strains, although type-1 predominated.
1730235	6	1	theme	beta	806:809	arg1	1-4GlcNAc					811:819	Fuc alpha 1-2Gal beta 1-4GlcNAc	789:819	Fuc alpha 1-2Gal beta 1-4GlcNAc	789:819	Blood-group-H types 1 (Fuc alpha 1-2Gal beta 1-3GlcNAc) and 2(Fuc alpha 1-2Gal beta 1-4GlcNAc) were found in the small and large intestines of both strains, although type-1 predominated.
1730235	6	2	theme	strains	875:881	arg1	intestines					856:865	the small and large intestines	836:865	the small and large intestines of both strains	836:881	Blood-group-H types 1 (Fuc alpha 1-2Gal beta 1-3GlcNAc) and 2(Fuc alpha 1-2Gal beta 1-4GlcNAc) were found in the small and large intestines of both strains, although type-1 predominated.
1730235	6	3	theme	alpha	793:797	arg1	2					787:787	2	787:787	2	787:787	Blood-group-H types 1 (Fuc alpha 1-2Gal beta 1-3GlcNAc) and 2(Fuc alpha 1-2Gal beta 1-4GlcNAc) were found in the small and large intestines of both strains, although type-1 predominated.
1730235	6	3	theme	alpha	793:797	arg1	1-4GlcNAc					811:819	Fuc alpha 1-2Gal beta 1-4GlcNAc	789:819	Fuc alpha 1-2Gal beta 1-4GlcNAc	789:819	Blood-group-H types 1 (Fuc alpha 1-2Gal beta 1-3GlcNAc) and 2(Fuc alpha 1-2Gal beta 1-4GlcNAc) were found in the small and large intestines of both strains, although type-1 predominated.
1730235	1	4	theme	small	260:264	arg1	intestine					276:284	the small and large intestine	256:284	the small and large intestine of two inbred strains of rat	256:313	The N-linked type of glycans were prepared as their glycopeptides after pronase digestion of the epithelial cells from the small and large intestine of two inbred strains of rat.
1730235	8	5	theme	small	1125:1129	arg1	intestine					1131:1139	the small intestine	1121:1139	the small intestine	1121:1139	The other strain (GOT-BW) expressed blood-group-A determinants in the small intestine.
1730235	0	6	link	N-linked	0:7	arg1	glycopeptides					9:21	N-linked glycopeptides	0:21	N-linked glycopeptides with blood group determinants	0:51	N-linked glycopeptides with blood group determinants lacking neuraminic acid from the epithelial cells of rat small and large intestine.
1730235	4	7	theme	neuraminic	652:661	arg1	residues					668:675	neuraminic acid residues	652:675	neuraminic acid residues	652:675	The terminal parts were, in contrast to most N-linked glycans, devoid of neuraminic acid residues.
1730235	3	8	theme	tetraantennary	533:546	arg1	types					548:552	the triantennary and tetraantennary types	512:552	the triantennary and tetraantennary types with intersected GlcNAc	512:576	The glycopeptides were of the triantennary and tetraantennary types with intersected GlcNAc.
1730235	6	9	theme	large	850:854	arg1	intestines					856:865	the small and large intestines	836:865	the small and large intestines of both strains	836:881	Blood-group-H types 1 (Fuc alpha 1-2Gal beta 1-3GlcNAc) and 2(Fuc alpha 1-2Gal beta 1-4GlcNAc) were found in the small and large intestines of both strains, although type-1 predominated.
1730235	4	10	theme	residues	668:675	arg1	devoid					642:647	devoid	642:647	devoid	642:647	The terminal parts were, in contrast to most N-linked glycans, devoid of neuraminic acid residues.
1730235	4	10	theme	residues	668:675	arg1	parts					592:596	The terminal parts	579:596	The terminal parts	579:596	The terminal parts were, in contrast to most N-linked glycans, devoid of neuraminic acid residues.
1730235	9	11	theme	acid	1165:1168	arg1	residues					1170:1177	neuraminic acid residues	1154:1177	neuraminic acid residues	1154:1177	The lack of neuraminic acid residues in the small and large intestine and of blood-group-B activity in the large intestine differed from that found in glycosphingolipids obtained from the same organs.
1730235	7	12	from	glycopeptides	967:979	arg1	intestine					994:1002	the small intestine	984:1002	the small intestine	984:1002	One rat strain (GOT-W) did not express blood-group-A glycopeptides in the small intestine, but the large intestine from the same strain did.
1730235	0	13	theme	intestine	126:134	arg1	cells					97:101	the epithelial cells	82:101	the epithelial cells of rat small and large intestine	82:134	N-linked glycopeptides with blood group determinants lacking neuraminic acid from the epithelial cells of rat small and large intestine.
1730235	9	14	theme	small	1186:1190	arg1	intestine					1202:1210	the small and large intestine	1182:1210	the small and large intestine	1182:1210	The lack of neuraminic acid residues in the small and large intestine and of blood-group-B activity in the large intestine differed from that found in glycosphingolipids obtained from the same organs.
1730235	1	15	theme	pronase	209:215	arg1	digestion					217:225	pronase digestion	209:225	pronase digestion of the epithelial cells from the small and large intestine of two inbred strains of rat	209:313	The N-linked type of glycans were prepared as their glycopeptides after pronase digestion of the epithelial cells from the small and large intestine of two inbred strains of rat.
1730235	9	16	theme	large	1196:1200	arg1	intestine					1202:1210	the small and large intestine	1182:1210	the small and large intestine	1182:1210	The lack of neuraminic acid residues in the small and large intestine and of blood-group-B activity in the large intestine differed from that found in glycosphingolipids obtained from the same organs.
1730235	0	17	from	cells	97:101	arg1	acid					72:75	neuraminic acid	61:75	neuraminic acid from the epithelial cells of rat small and large intestine	61:134	N-linked glycopeptides with blood group determinants lacking neuraminic acid from the epithelial cells of rat small and large intestine.
1730235	1	18	theme	rat	311:313	arg1	strains					300:306	two inbred strains	289:306	two inbred strains of rat	289:313	The N-linked type of glycans were prepared as their glycopeptides after pronase digestion of the epithelial cells from the small and large intestine of two inbred strains of rat.
1730235	1	19	theme	N-linked	141:148	arg1	glycopeptides					189:201	their glycopeptides	183:201	their glycopeptides	183:201	The N-linked type of glycans were prepared as their glycopeptides after pronase digestion of the epithelial cells from the small and large intestine of two inbred strains of rat.
1730235	1	19	theme	N-linked	141:148	arg1	glycans					158:164	The N-linked type of glycans	137:164	The N-linked type of glycans	137:164	The N-linked type of glycans were prepared as their glycopeptides after pronase digestion of the epithelial cells from the small and large intestine of two inbred strains of rat.
1730235	1	20	theme	of	155:156	arg1	glycopeptides					189:201	their glycopeptides	183:201	their glycopeptides	183:201	The N-linked type of glycans were prepared as their glycopeptides after pronase digestion of the epithelial cells from the small and large intestine of two inbred strains of rat.
1730235	1	20	theme	of	155:156	arg1	glycans					158:164	The N-linked type of glycans	137:164	The N-linked type of glycans	137:164	The N-linked type of glycans were prepared as their glycopeptides after pronase digestion of the epithelial cells from the small and large intestine of two inbred strains of rat.
1730235	9	21	theme	large	1249:1253	arg1	intestine					1255:1263	the large intestine	1245:1263	the large intestine	1245:1263	The lack of neuraminic acid residues in the small and large intestine and of blood-group-B activity in the large intestine differed from that found in glycosphingolipids obtained from the same organs.
1730235	2	22	theme	blood-group	377:387	arg1	activity					389:396	blood-group activity	377:396	blood-group activity	377:396	These glycopeptides were analysed for sugar composition, for blood-group activity, by 1H-NMR spectroscopy, and after permethylation by electron-impact mass spectrometry.
1730235	0	23	theme	rat	106:108	arg1	intestine					126:134	rat small and large intestine	106:134	rat small and large intestine	106:134	N-linked glycopeptides with blood group determinants lacking neuraminic acid from the epithelial cells of rat small and large intestine.
1730235	3	24	gly	glycopeptides	490:502	arg2	glycopeptides					490:502	The glycopeptides	486:502	The glycopeptides	486:502	The glycopeptides were of the triantennary and tetraantennary types with intersected GlcNAc.
1730235	0	25	theme	N-linked	0:7	arg1	glycopeptides					9:21	N-linked glycopeptides	0:21	N-linked glycopeptides with blood group determinants	0:51	N-linked glycopeptides with blood group determinants lacking neuraminic acid from the epithelial cells of rat small and large intestine.
1730235	1	26	from	intestine	276:284	arg1	digestion					217:225	pronase digestion	209:225	pronase digestion of the epithelial cells from the small and large intestine of two inbred strains of rat	209:313	The N-linked type of glycans were prepared as their glycopeptides after pronase digestion of the epithelial cells from the small and large intestine of two inbred strains of rat.
1730235	1	26	from	intestine	276:284	arg1	cells					245:249	the epithelial cells	230:249	the epithelial cells from the small and large intestine of two inbred strains of rat	230:313	The N-linked type of glycans were prepared as their glycopeptides after pronase digestion of the epithelial cells from the small and large intestine of two inbred strains of rat.
1730235	7	27	from	strain	1043:1048	arg1	intestine					1019:1027	the large intestine	1009:1027	the large intestine from the same strain	1009:1048	One rat strain (GOT-W) did not express blood-group-A glycopeptides in the small intestine, but the large intestine from the same strain did.
1730235	2	28	theme	1H-NMR	402:407	arg1	spectroscopy					409:420	1H-NMR spectroscopy	402:420	1H-NMR spectroscopy	402:420	These glycopeptides were analysed for sugar composition, for blood-group activity, by 1H-NMR spectroscopy, and after permethylation by electron-impact mass spectrometry.
1730235	2	29	theme	mass	467:470	arg1	spectrometry					472:483	electron-impact mass spectrometry	451:483	electron-impact mass spectrometry	451:483	These glycopeptides were analysed for sugar composition, for blood-group activity, by 1H-NMR spectroscopy, and after permethylation by electron-impact mass spectrometry.
1730235	0	30	theme	group	34:38	arg1	determinants					40:51	blood group determinants	28:51	blood group determinants	28:51	N-linked glycopeptides with blood group determinants lacking neuraminic acid from the epithelial cells of rat small and large intestine.
1730235	0	31	gly	glycopeptides	9:21	arg2	glycopeptides					9:21	N-linked glycopeptides	0:21	N-linked glycopeptides with blood group determinants	0:51	N-linked glycopeptides with blood group determinants lacking neuraminic acid from the epithelial cells of rat small and large intestine.
1730235	6	32	theme	beta	767:770	arg1	1					747:747	1	747:747	1	747:747	Blood-group-H types 1 (Fuc alpha 1-2Gal beta 1-3GlcNAc) and 2(Fuc alpha 1-2Gal beta 1-4GlcNAc) were found in the small and large intestines of both strains, although type-1 predominated.
1730235	6	32	theme	beta	767:770	arg1	1-3GlcNAc					772:780	Fuc alpha 1-2Gal beta 1-3GlcNAc	750:780	Fuc alpha 1-2Gal beta 1-3GlcNAc	750:780	Blood-group-H types 1 (Fuc alpha 1-2Gal beta 1-3GlcNAc) and 2(Fuc alpha 1-2Gal beta 1-4GlcNAc) were found in the small and large intestines of both strains, although type-1 predominated.
1730235	1	33	theme	strains	300:306	arg1	intestine					276:284	the small and large intestine	256:284	the small and large intestine of two inbred strains of rat	256:313	The N-linked type of glycans were prepared as their glycopeptides after pronase digestion of the epithelial cells from the small and large intestine of two inbred strains of rat.
1730235	9	34	theme	blood-group-B	1219:1231	arg1	activity					1233:1240	blood-group-B activity	1219:1240	blood-group-B activity in the large intestine	1219:1263	The lack of neuraminic acid residues in the small and large intestine and of blood-group-B activity in the large intestine differed from that found in glycosphingolipids obtained from the same organs.
1730235	7	35	gly	glycopeptides	967:979	arg2	glycopeptides					967:979	blood-group-A glycopeptides	953:979	blood-group-A glycopeptides in the small intestine	953:1002	One rat strain (GOT-W) did not express blood-group-A glycopeptides in the small intestine, but the large intestine from the same strain did.
1730235	6	36	theme	alpha	754:758	arg1	1					747:747	1	747:747	1	747:747	Blood-group-H types 1 (Fuc alpha 1-2Gal beta 1-3GlcNAc) and 2(Fuc alpha 1-2Gal beta 1-4GlcNAc) were found in the small and large intestines of both strains, although type-1 predominated.
1730235	6	36	theme	alpha	754:758	arg1	1-3GlcNAc					772:780	Fuc alpha 1-2Gal beta 1-3GlcNAc	750:780	Fuc alpha 1-2Gal beta 1-3GlcNAc	750:780	Blood-group-H types 1 (Fuc alpha 1-2Gal beta 1-3GlcNAc) and 2(Fuc alpha 1-2Gal beta 1-4GlcNAc) were found in the small and large intestines of both strains, although type-1 predominated.
1730235	2	37	theme	sugar	354:358	arg1	composition					360:370	sugar composition	354:370	sugar composition	354:370	These glycopeptides were analysed for sugar composition, for blood-group activity, by 1H-NMR spectroscopy, and after permethylation by electron-impact mass spectrometry.
1730235	3	38	with	types	548:552	arg1	GlcNAc					571:576	intersected GlcNAc	559:576	intersected GlcNAc	559:576	The glycopeptides were of the triantennary and tetraantennary types with intersected GlcNAc.
1730235	1	39	theme	cells	245:249	arg1	digestion					217:225	pronase digestion	209:225	pronase digestion of the epithelial cells from the small and large intestine of two inbred strains of rat	209:313	The N-linked type of glycans were prepared as their glycopeptides after pronase digestion of the epithelial cells from the small and large intestine of two inbred strains of rat.
1730235	4	40	theme	terminal	583:590	arg1	devoid					642:647	devoid	642:647	devoid	642:647	The terminal parts were, in contrast to most N-linked glycans, devoid of neuraminic acid residues.
1730235	4	40	theme	terminal	583:590	arg1	parts					592:596	The terminal parts	579:596	The terminal parts	579:596	The terminal parts were, in contrast to most N-linked glycans, devoid of neuraminic acid residues.
1730235	6	41	theme	1-2Gal	799:804	arg1	2					787:787	2	787:787	2	787:787	Blood-group-H types 1 (Fuc alpha 1-2Gal beta 1-3GlcNAc) and 2(Fuc alpha 1-2Gal beta 1-4GlcNAc) were found in the small and large intestines of both strains, although type-1 predominated.
1730235	6	41	theme	1-2Gal	799:804	arg1	1-4GlcNAc					811:819	Fuc alpha 1-2Gal beta 1-4GlcNAc	789:819	Fuc alpha 1-2Gal beta 1-4GlcNAc	789:819	Blood-group-H types 1 (Fuc alpha 1-2Gal beta 1-3GlcNAc) and 2(Fuc alpha 1-2Gal beta 1-4GlcNAc) were found in the small and large intestines of both strains, although type-1 predominated.
1730235	1	42	gly	glycopeptides	189:201	arg2	glycans					158:164	The N-linked type of glycans	137:164	The N-linked type of glycans	137:164	The N-linked type of glycans were prepared as their glycopeptides after pronase digestion of the epithelial cells from the small and large intestine of two inbred strains of rat.
1730235	1	42	gly	glycopeptides	189:201	arg2	glycopeptides					189:201	their glycopeptides	183:201	their glycopeptides	183:201	The N-linked type of glycans were prepared as their glycopeptides after pronase digestion of the epithelial cells from the small and large intestine of two inbred strains of rat.
1730235	6	43	theme	Fuc	789:791	arg1	2					787:787	2	787:787	2	787:787	Blood-group-H types 1 (Fuc alpha 1-2Gal beta 1-3GlcNAc) and 2(Fuc alpha 1-2Gal beta 1-4GlcNAc) were found in the small and large intestines of both strains, although type-1 predominated.
1730235	6	43	theme	Fuc	789:791	arg1	1-4GlcNAc					811:819	Fuc alpha 1-2Gal beta 1-4GlcNAc	789:819	Fuc alpha 1-2Gal beta 1-4GlcNAc	789:819	Blood-group-H types 1 (Fuc alpha 1-2Gal beta 1-3GlcNAc) and 2(Fuc alpha 1-2Gal beta 1-4GlcNAc) were found in the small and large intestines of both strains, although type-1 predominated.
1730235	7	44	theme	same	1038:1041	arg1	strain					1043:1048	the same strain	1034:1048	the same strain	1034:1048	One rat strain (GOT-W) did not express blood-group-A glycopeptides in the small intestine, but the large intestine from the same strain did.
1730235	9	45	theme	neuraminic	1154:1163	arg1	residues					1170:1177	neuraminic acid residues	1154:1177	neuraminic acid residues	1154:1177	The lack of neuraminic acid residues in the small and large intestine and of blood-group-B activity in the large intestine differed from that found in glycosphingolipids obtained from the same organs.
1730235	4	46	theme	acid	663:666	arg1	residues					668:675	neuraminic acid residues	652:675	neuraminic acid residues	652:675	The terminal parts were, in contrast to most N-linked glycans, devoid of neuraminic acid residues.
1730235	5	47	theme	blood-group	701:711	arg1	determinants					713:724	blood-group determinants	701:724	blood-group determinants	701:724	Instead they contained blood-group determinants.
1730235	9	48	theme	residues	1170:1177	arg1	lack					1146:1149	The lack	1142:1149	The lack of neuraminic acid residues in the small and large intestine and of blood-group-B activity in the large intestine	1142:1263	The lack of neuraminic acid residues in the small and large intestine and of blood-group-B activity in the large intestine differed from that found in glycosphingolipids obtained from the same organs.
1730235	3	49	theme	intersected	559:569	arg1	GlcNAc					571:576	intersected GlcNAc	559:576	intersected GlcNAc	559:576	The glycopeptides were of the triantennary and tetraantennary types with intersected GlcNAc.
1730235	9	50	from	intestine	1255:1263	arg1	lack					1146:1149	The lack	1142:1149	The lack of neuraminic acid residues in the small and large intestine and of blood-group-B activity in the large intestine	1142:1263	The lack of neuraminic acid residues in the small and large intestine and of blood-group-B activity in the large intestine differed from that found in glycosphingolipids obtained from the same organs.
1730235	0	51	with	glycopeptides	9:21	arg1	determinants					40:51	blood group determinants	28:51	blood group determinants	28:51	N-linked glycopeptides with blood group determinants lacking neuraminic acid from the epithelial cells of rat small and large intestine.
1730235	4	52	theme	N-linked	624:631	arg1	glycans					633:639	most N-linked glycans	619:639	most N-linked glycans	619:639	The terminal parts were, in contrast to most N-linked glycans, devoid of neuraminic acid residues.
1730235	7	53	theme	large	1013:1017	arg1	intestine					1019:1027	the large intestine	1009:1027	the large intestine from the same strain	1009:1048	One rat strain (GOT-W) did not express blood-group-A glycopeptides in the small intestine, but the large intestine from the same strain did.
1730235	7	54	theme	small	988:992	arg1	intestine					994:1002	the small intestine	984:1002	the small intestine	984:1002	One rat strain (GOT-W) did not express blood-group-A glycopeptides in the small intestine, but the large intestine from the same strain did.
1730235	9	55	from	activity	1233:1240	arg1	intestine					1255:1263	the large intestine	1245:1263	the large intestine	1245:1263	The lack of neuraminic acid residues in the small and large intestine and of blood-group-B activity in the large intestine differed from that found in glycosphingolipids obtained from the same organs.
1730235	0	56	theme	large	120:124	arg1	intestine					126:134	rat small and large intestine	106:134	rat small and large intestine	106:134	N-linked glycopeptides with blood group determinants lacking neuraminic acid from the epithelial cells of rat small and large intestine.
1730235	6	57	located	found	827:831	arg2	types					741:745	Blood-group-H types 1 (Fuc alpha 1-2Gal beta 1-3GlcNAc) and 2(Fuc alpha 1-2Gal beta 1-4GlcNAc)	727:820	Blood-group-H types 1 (Fuc alpha 1-2Gal beta 1-3GlcNAc) and 2(Fuc alpha 1-2Gal beta 1-4GlcNAc)	727:820	Blood-group-H types 1 (Fuc alpha 1-2Gal beta 1-3GlcNAc) and 2(Fuc alpha 1-2Gal beta 1-4GlcNAc) were found in the small and large intestines of both strains, although type-1 predominated.
1730235	6	57	located	found	827:831	arg1	intestines					856:865	the small and large intestines	836:865	the small and large intestines of both strains	836:881	Blood-group-H types 1 (Fuc alpha 1-2Gal beta 1-3GlcNAc) and 2(Fuc alpha 1-2Gal beta 1-4GlcNAc) were found in the small and large intestines of both strains, although type-1 predominated.
1730235	1	58	from	digestion	217:225	arg1	intestine					276:284	the small and large intestine	256:284	the small and large intestine of two inbred strains of rat	256:313	The N-linked type of glycans were prepared as their glycopeptides after pronase digestion of the epithelial cells from the small and large intestine of two inbred strains of rat.
1730235	7	59	theme	blood-group-A	953:965	arg1	glycopeptides					967:979	blood-group-A glycopeptides	953:979	blood-group-A glycopeptides in the small intestine	953:1002	One rat strain (GOT-W) did not express blood-group-A glycopeptides in the small intestine, but the large intestine from the same strain did.
1730235	4	60	link	N-linked	624:631	arg1	glycans					633:639	most N-linked glycans	619:639	most N-linked glycans	619:639	The terminal parts were, in contrast to most N-linked glycans, devoid of neuraminic acid residues.
1730235	9	61	from	lack	1146:1149	arg1	intestine					1255:1263	the large intestine	1245:1263	the large intestine	1245:1263	The lack of neuraminic acid residues in the small and large intestine and of blood-group-B activity in the large intestine differed from that found in glycosphingolipids obtained from the same organs.
1730235	9	61	from	lack	1146:1149	arg1	intestine					1202:1210	the small and large intestine	1182:1210	the small and large intestine	1182:1210	The lack of neuraminic acid residues in the small and large intestine and of blood-group-B activity in the large intestine differed from that found in glycosphingolipids obtained from the same organs.
1730235	0	62	theme	epithelial	86:95	arg1	cells					97:101	the epithelial cells	82:101	the epithelial cells of rat small and large intestine	82:134	N-linked glycopeptides with blood group determinants lacking neuraminic acid from the epithelial cells of rat small and large intestine.
1730235	9	63	theme	activity	1233:1240	arg1	lack					1146:1149	The lack	1142:1149	The lack of neuraminic acid residues in the small and large intestine and of blood-group-B activity in the large intestine	1142:1263	The lack of neuraminic acid residues in the small and large intestine and of blood-group-B activity in the large intestine differed from that found in glycosphingolipids obtained from the same organs.
1730235	1	64	theme	type	150:153	arg1	glycopeptides					189:201	their glycopeptides	183:201	their glycopeptides	183:201	The N-linked type of glycans were prepared as their glycopeptides after pronase digestion of the epithelial cells from the small and large intestine of two inbred strains of rat.
1730235	1	64	theme	type	150:153	arg1	glycans					158:164	The N-linked type of glycans	137:164	The N-linked type of glycans	137:164	The N-linked type of glycans were prepared as their glycopeptides after pronase digestion of the epithelial cells from the small and large intestine of two inbred strains of rat.
1730235	6	65	theme	Blood-group-H	727:739	arg1	types					741:745	Blood-group-H types 1 (Fuc alpha 1-2Gal beta 1-3GlcNAc) and 2(Fuc alpha 1-2Gal beta 1-4GlcNAc)	727:820	Blood-group-H types 1 (Fuc alpha 1-2Gal beta 1-3GlcNAc) and 2(Fuc alpha 1-2Gal beta 1-4GlcNAc)	727:820	Blood-group-H types 1 (Fuc alpha 1-2Gal beta 1-3GlcNAc) and 2(Fuc alpha 1-2Gal beta 1-4GlcNAc) were found in the small and large intestines of both strains, although type-1 predominated.
1730235	0	66	theme	small	110:114	arg1	intestine					126:134	rat small and large intestine	106:134	rat small and large intestine	106:134	N-linked glycopeptides with blood group determinants lacking neuraminic acid from the epithelial cells of rat small and large intestine.
1730235	7	67	theme	rat	918:920	arg1	GOT-W					930:934	GOT-W	930:934	GOT-W	930:934	One rat strain (GOT-W) did not express blood-group-A glycopeptides in the small intestine, but the large intestine from the same strain did.
1730235	7	67	theme	rat	918:920	arg1	strain					922:927	One rat strain	914:927	One rat strain (GOT-W)	914:935	One rat strain (GOT-W) did not express blood-group-A glycopeptides in the small intestine, but the large intestine from the same strain did.
1730235	0	68	theme	blood	28:32	arg1	determinants					40:51	blood group determinants	28:51	blood group determinants	28:51	N-linked glycopeptides with blood group determinants lacking neuraminic acid from the epithelial cells of rat small and large intestine.
1730235	1	69	theme	large	270:274	arg1	intestine					276:284	the small and large intestine	256:284	the small and large intestine of two inbred strains of rat	256:313	The N-linked type of glycans were prepared as their glycopeptides after pronase digestion of the epithelial cells from the small and large intestine of two inbred strains of rat.
1730235	6	70	theme	small	840:844	arg1	intestines					856:865	the small and large intestines	836:865	the small and large intestines of both strains	836:881	Blood-group-H types 1 (Fuc alpha 1-2Gal beta 1-3GlcNAc) and 2(Fuc alpha 1-2Gal beta 1-4GlcNAc) were found in the small and large intestines of both strains, although type-1 predominated.
1730235	2	71	theme	electron-impact	451:465	arg1	spectrometry					472:483	electron-impact mass spectrometry	451:483	electron-impact mass spectrometry	451:483	These glycopeptides were analysed for sugar composition, for blood-group activity, by 1H-NMR spectroscopy, and after permethylation by electron-impact mass spectrometry.
1730235	5	72	contain	contained	691:699	arg1	they					686:689	they	686:689	they	686:689	Instead they contained blood-group determinants.
1730235	5	72	contain	contained	691:699	arg2	determinants					713:724	blood-group determinants	701:724	blood-group determinants	701:724	Instead they contained blood-group determinants.
1730235	1	73	link	N-linked	141:148	arg1	glycopeptides					189:201	their glycopeptides	183:201	their glycopeptides	183:201	The N-linked type of glycans were prepared as their glycopeptides after pronase digestion of the epithelial cells from the small and large intestine of two inbred strains of rat.
1730235	1	73	link	N-linked	141:148	arg1	glycans					158:164	The N-linked type of glycans	137:164	The N-linked type of glycans	137:164	The N-linked type of glycans were prepared as their glycopeptides after pronase digestion of the epithelial cells from the small and large intestine of two inbred strains of rat.
1730235	0	74	theme	neuraminic	61:70	arg1	acid					72:75	neuraminic acid	61:75	neuraminic acid from the epithelial cells of rat small and large intestine	61:134	N-linked glycopeptides with blood group determinants lacking neuraminic acid from the epithelial cells of rat small and large intestine.
1730235	1	75	theme	inbred	293:298	arg1	strains					300:306	two inbred strains	289:306	two inbred strains of rat	289:313	The N-linked type of glycans were prepared as their glycopeptides after pronase digestion of the epithelial cells from the small and large intestine of two inbred strains of rat.
1730235	8	76	theme	other	1059:1063	arg1	GOT-BW					1073:1078	GOT-BW	1073:1078	GOT-BW	1073:1078	The other strain (GOT-BW) expressed blood-group-A determinants in the small intestine.
1730235	8	76	theme	other	1059:1063	arg1	strain					1065:1070	The other strain	1055:1070	The other strain (GOT-BW)	1055:1079	The other strain (GOT-BW) expressed blood-group-A determinants in the small intestine.
1730235	4	77	dep	glycans	633:639	arg1	contrast					607:614	contrast	607:614	contrast	607:614	The terminal parts were, in contrast to most N-linked glycans, devoid of neuraminic acid residues.
1730235	2	78	gly	glycopeptides	322:334	arg2	glycopeptides					322:334	These glycopeptides	316:334	These glycopeptides	316:334	These glycopeptides were analysed for sugar composition, for blood-group activity, by 1H-NMR spectroscopy, and after permethylation by electron-impact mass spectrometry.
1730235	6	79	theme	1-2Gal	760:765	arg1	1					747:747	1	747:747	1	747:747	Blood-group-H types 1 (Fuc alpha 1-2Gal beta 1-3GlcNAc) and 2(Fuc alpha 1-2Gal beta 1-4GlcNAc) were found in the small and large intestines of both strains, although type-1 predominated.
1730235	6	79	theme	1-2Gal	760:765	arg1	1-3GlcNAc					772:780	Fuc alpha 1-2Gal beta 1-3GlcNAc	750:780	Fuc alpha 1-2Gal beta 1-3GlcNAc	750:780	Blood-group-H types 1 (Fuc alpha 1-2Gal beta 1-3GlcNAc) and 2(Fuc alpha 1-2Gal beta 1-4GlcNAc) were found in the small and large intestines of both strains, although type-1 predominated.
1730235	9	80	theme	same	1330:1333	arg1	organs					1335:1340	the same organs	1326:1340	the same organs	1326:1340	The lack of neuraminic acid residues in the small and large intestine and of blood-group-B activity in the large intestine differed from that found in glycosphingolipids obtained from the same organs.
1730235	6	81	dep	types	741:745	arg1	2					787:787	2	787:787	2	787:787	Blood-group-H types 1 (Fuc alpha 1-2Gal beta 1-3GlcNAc) and 2(Fuc alpha 1-2Gal beta 1-4GlcNAc) were found in the small and large intestines of both strains, although type-1 predominated.
1730235	6	81	dep	types	741:745	arg1	1-4GlcNAc					811:819	Fuc alpha 1-2Gal beta 1-4GlcNAc	789:819	Fuc alpha 1-2Gal beta 1-4GlcNAc	789:819	Blood-group-H types 1 (Fuc alpha 1-2Gal beta 1-3GlcNAc) and 2(Fuc alpha 1-2Gal beta 1-4GlcNAc) were found in the small and large intestines of both strains, although type-1 predominated.
1730235	6	81	dep	types	741:745	arg1	1					747:747	1	747:747	1	747:747	Blood-group-H types 1 (Fuc alpha 1-2Gal beta 1-3GlcNAc) and 2(Fuc alpha 1-2Gal beta 1-4GlcNAc) were found in the small and large intestines of both strains, although type-1 predominated.
1730235	6	81	dep	types	741:745	arg1	1-3GlcNAc					772:780	Fuc alpha 1-2Gal beta 1-3GlcNAc	750:780	Fuc alpha 1-2Gal beta 1-3GlcNAc	750:780	Blood-group-H types 1 (Fuc alpha 1-2Gal beta 1-3GlcNAc) and 2(Fuc alpha 1-2Gal beta 1-4GlcNAc) were found in the small and large intestines of both strains, although type-1 predominated.
1730235	6	82	theme	Fuc	750:752	arg1	1					747:747	1	747:747	1	747:747	Blood-group-H types 1 (Fuc alpha 1-2Gal beta 1-3GlcNAc) and 2(Fuc alpha 1-2Gal beta 1-4GlcNAc) were found in the small and large intestines of both strains, although type-1 predominated.
1730235	6	82	theme	Fuc	750:752	arg1	1-3GlcNAc					772:780	Fuc alpha 1-2Gal beta 1-3GlcNAc	750:780	Fuc alpha 1-2Gal beta 1-3GlcNAc	750:780	Blood-group-H types 1 (Fuc alpha 1-2Gal beta 1-3GlcNAc) and 2(Fuc alpha 1-2Gal beta 1-4GlcNAc) were found in the small and large intestines of both strains, although type-1 predominated.
1730235	8	83	from	determinants	1105:1116	arg1	intestine					1131:1139	the small intestine	1121:1139	the small intestine	1121:1139	The other strain (GOT-BW) expressed blood-group-A determinants in the small intestine.
1730235	4	84	theme	most	619:622	arg1	glycans					633:639	most N-linked glycans	619:639	most N-linked glycans	619:639	The terminal parts were, in contrast to most N-linked glycans, devoid of neuraminic acid residues.
1730235	3	85	theme	triantennary	516:527	arg1	types					548:552	the triantennary and tetraantennary types	512:552	the triantennary and tetraantennary types with intersected GlcNAc	512:576	The glycopeptides were of the triantennary and tetraantennary types with intersected GlcNAc.
1730235	1	86	theme	epithelial	234:243	arg1	cells					245:249	the epithelial cells	230:249	the epithelial cells from the small and large intestine of two inbred strains of rat	230:313	The N-linked type of glycans were prepared as their glycopeptides after pronase digestion of the epithelial cells from the small and large intestine of two inbred strains of rat.
2511201	4	0	contain	contain	816:822	arg1	Z					788:788	protein Z	780:788	protein Z	780:788	We report here that human factors VII and IX and protein Z and bovine protein Z also contain such carbohydrate moieties linked to a serine residue at the same position found in bovine factors VII and IX.
2511201	4	0	contain	contain	816:822	arg2	moieties					842:849	such carbohydrate moieties	824:849	such carbohydrate moieties linked to a serine residue at the same position found in bovine factors VII and IX	824:932	We report here that human factors VII and IX and protein Z and bovine protein Z also contain such carbohydrate moieties linked to a serine residue at the same position found in bovine factors VII and IX.
2511201	4	0	contain	contain	816:822	arg1	IX					773:774	IX	773:774	IX	773:774	We report here that human factors VII and IX and protein Z and bovine protein Z also contain such carbohydrate moieties linked to a serine residue at the same position found in bovine factors VII and IX.
2511201	4	0	contain	contain	816:822	arg1	Z					809:809	bovine protein Z	794:809	bovine protein Z	794:809	We report here that human factors VII and IX and protein Z and bovine protein Z also contain such carbohydrate moieties linked to a serine residue at the same position found in bovine factors VII and IX.
2511201	4	0	contain	contain	816:822	arg1	VII					765:767	human factors VII	751:767	human factors VII	751:767	We report here that human factors VII and IX and protein Z and bovine protein Z also contain such carbohydrate moieties linked to a serine residue at the same position found in bovine factors VII and IX.
2511201	11	1	theme	Z	1968:1968	arg1	VII					1945:1947	human factors VII	1931:1947	human factors VII	1931:1947	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	11	1	theme	Z	1968:1968	arg1	domains					1920:1926	the first epidermal growth factor-like domains	1881:1926	the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown	1881:2114	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	11	1	theme	Z	1968:1968	arg1	IX					1953:1954	IX	1953:1954	IX	1953:1954	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	11	1	theme	Z	1968:1968	arg1	Z					1968:1968	protein Z	1960:1968	protein Z	1960:1968	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	0	2	theme	factor-like	148:158	arg1	domain					160:165	the first epidermal growth factor-like domain	121:165	the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z	121:228	Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc) O-glycosidically linked to a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z.
2511201	0	2	theme	factor-like	148:158	arg1	factors					176:182	human factors	170:182	human factors VII and IX and protein Z and bovine protein Z	170:228	Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc) O-glycosidically linked to a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z.
2511201	5	3	theme	spectrometric	1083:1095	arg1	analysis					1097:1104	mass spectrometric analysis	1078:1104	mass spectrometric analysis	1078:1104	A glycopeptide derived from each of these proteins was subjected to amino acid sequence and component sugar analyses and fast atom bombardment mass spectrometric analysis.
2511201	11	4	theme	trisaccharide	1716:1728	arg1	chain					1736:1740	the trisaccharide sugar chain	1712:1740	the trisaccharide sugar chain previously discovered in bovine factors VII and IX	1712:1791	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	8	5	theme	factor	1353:1358	arg1	VII					1360:1362	human factor VII	1347:1362	human factor VII	1347:1362	In contrast, human factor VII and protein Z yielded two different glycopeptides which contained Glc and Xyl at molar ratios of 1:1 and 1:2, respectively, suggesting microheterogeneity of these O-linked sugar chains.
2511201	11	6	theme	bovine	1767:1772	arg1	VII					1782:1784	bovine factors VII	1767:1784	bovine factors VII	1767:1784	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	4	7	theme	bovine	794:799	arg1	Z					809:809	bovine protein Z	794:809	bovine protein Z	794:809	We report here that human factors VII and IX and protein Z and bovine protein Z also contain such carbohydrate moieties linked to a serine residue at the same position found in bovine factors VII and IX.
2511201	9	8	contain	contained	1580:1588	arg2	mol					1592:1594	1 mol	1590:1594	1 mol of Glc	1590:1601	Bovine protein Z glycopeptide contained 1 mol of Glc and 2 mol of Xyl.
2511201	9	8	contain	contained	1580:1588	arg2	mol					1609:1611	2 mol	1607:1611	2 mol of Xyl	1607:1618	Bovine protein Z glycopeptide contained 1 mol of Glc and 2 mol of Xyl.
2511201	9	8	contain	contained	1580:1588	arg1	glycopeptide					1567:1578	Bovine protein Z glycopeptide	1550:1578	Bovine protein Z glycopeptide	1550:1578	Bovine protein Z glycopeptide contained 1 mol of Glc and 2 mol of Xyl.
2511201	0	9	theme	factors	176:182	arg1	domain					160:165	the first epidermal growth factor-like domain	121:165	the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z	121:228	Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc) O-glycosidically linked to a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z.
2511201	0	9	theme	factors	176:182	arg1	factors					176:182	human factors	170:182	human factors VII and IX and protein Z and bovine protein Z	170:228	Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc) O-glycosidically linked to a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z.
2511201	5	10	theme	fast	1056:1059	arg1	bombardment					1066:1076	fast atom bombardment	1056:1076	fast atom bombardment	1056:1076	A glycopeptide derived from each of these proteins was subjected to amino acid sequence and component sugar analyses and fast atom bombardment mass spectrometric analysis.
2511201	6	11	dep	mol	1190:1192	arg1	each					1194:1197	each	1194:1197	each	1194:1197	The results indicate that the glycopeptide derived from human factor IX contains 1 mol each of Glc and Xyl.
2511201	9	12	theme	Z	1565:1565	arg1	glycopeptide					1567:1578	Bovine protein Z glycopeptide	1550:1578	Bovine protein Z glycopeptide	1550:1578	Bovine protein Z glycopeptide contained 1 mol of Glc and 2 mol of Xyl.
2511201	8	13	theme	sugar	1536:1540	arg1	chains					1542:1547	these O-linked sugar chains	1521:1547	these O-linked sugar chains	1521:1547	In contrast, human factor VII and protein Z yielded two different glycopeptides which contained Glc and Xyl at molar ratios of 1:1 and 1:2, respectively, suggesting microheterogeneity of these O-linked sugar chains.
2511201	0	14	dep	factors	176:182	arg1	Z					207:207	protein Z	199:207	protein Z	199:207	Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc) O-glycosidically linked to a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z.
2511201	0	14	dep	factors	176:182	arg1	VII					184:186	VII	184:186	VII	184:186	Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc) O-glycosidically linked to a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z.
2511201	0	14	dep	factors	176:182	arg1	Z					228:228	bovine protein Z	213:228	bovine protein Z	213:228	Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc) O-glycosidically linked to a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z.
2511201	0	14	dep	factors	176:182	arg1	factors					176:182	human factors	170:182	human factors VII and IX and protein Z and bovine protein Z	170:228	Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc) O-glycosidically linked to a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z.
2511201	0	14	dep	factors	176:182	arg1	IX					192:193	IX	192:193	IX	192:193	Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc) O-glycosidically linked to a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z.
2511201	1	15	theme	growth	331:336	arg1	domains					350:356	the first epidermal growth factor-like domains	311:356	the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem	311:573	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	15	theme	growth	331:336	arg1	factors					386:392	bovine blood coagulation factors	361:392	bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem	361:573	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	5	16	dep	sequence	1014:1021	arg1	analysis					1097:1104	mass spectrometric analysis	1078:1104	mass spectrometric analysis	1078:1104	A glycopeptide derived from each of these proteins was subjected to amino acid sequence and component sugar analyses and fast atom bombardment mass spectrometric analysis.
2511201	11	17	theme	IX	1953:1954	arg1	VII					1945:1947	human factors VII	1931:1947	human factors VII	1931:1947	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	11	17	theme	IX	1953:1954	arg1	domains					1920:1926	the first epidermal growth factor-like domains	1881:1926	the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown	1881:2114	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	11	17	theme	IX	1953:1954	arg1	IX					1953:1954	IX	1953:1954	IX	1953:1954	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	11	17	theme	IX	1953:1954	arg1	Z					1968:1968	protein Z	1960:1968	protein Z	1960:1968	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	11	18	theme	factor-like	1908:1918	arg1	VII					1945:1947	human factors VII	1931:1947	human factors VII	1931:1947	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	11	18	theme	factor-like	1908:1918	arg1	domains					1920:1926	the first epidermal growth factor-like domains	1881:1926	the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown	1881:2114	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	11	18	theme	factor-like	1908:1918	arg1	IX					1953:1954	IX	1953:1954	IX	1953:1954	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	11	18	theme	factor-like	1908:1918	arg1	Z					1968:1968	protein Z	1960:1968	protein Z	1960:1968	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	9	19	theme	Glc	1599:1601	arg1	mol					1609:1611	2 mol	1607:1611	2 mol of Xyl	1607:1618	Bovine protein Z glycopeptide contained 1 mol of Glc and 2 mol of Xyl.
2511201	9	19	theme	Glc	1599:1601	arg1	mol					1592:1594	1 mol	1590:1594	1 mol of Glc	1590:1601	Bovine protein Z glycopeptide contained 1 mol of Glc and 2 mol of Xyl.
2511201	9	20	gly	glycopeptide	1567:1578	arg2	glycopeptide					1567:1578	Bovine protein Z glycopeptide	1550:1578	Bovine protein Z glycopeptide	1550:1578	Bovine protein Z glycopeptide contained 1 mol of Glc and 2 mol of Xyl.
2511201	1	21	theme	bovine	361:366	arg1	Sueyoshi					475:482	Sueyoshi	475:482	Sueyoshi	475:482	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	21	theme	bovine	361:366	arg1	VII					394:396	VII (Ser-52)	394:405	VII (Ser-52)	394:405	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	21	theme	bovine	361:366	arg1	Kawabata					434:441	Kawabata	434:441	Kawabata	434:441	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	21	theme	bovine	361:366	arg1	H.					459:460	H.	459:460	H.	459:460	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	21	theme	bovine	361:366	arg1	Ikenaka					545:551	Ikenaka	545:551	Ikenaka	545:551	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	21	theme	bovine	361:366	arg1	Iwanaga					501:507	Iwanaga	501:507	Iwanaga	501:507	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	21	theme	bovine	361:366	arg1	T.					521:522	T.	521:522	T.	521:522	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	21	theme	bovine	361:366	arg1	S.					430:431	S.	430:431	S.	430:431	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	21	theme	bovine	361:366	arg1	Takeya					463:468	Takeya	463:468	Takeya	463:468	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	21	theme	bovine	361:366	arg1	T.					497:498	T.	497:498	T.	497:498	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	21	theme	bovine	361:366	arg1	T.					485:486	T.	485:486	T.	485:486	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	21	theme	bovine	361:366	arg1	Shimonishi					525:534	Shimonishi	525:534	Shimonishi	525:534	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	21	theme	bovine	361:366	arg1	S.					444:445	S.	444:445	S.	444:445	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	21	theme	bovine	361:366	arg1	Miyata					489:494	Miyata	489:494	Miyata	489:494	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	21	theme	bovine	361:366	arg1	T					554:554	T	554:554	T	554:554	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	21	theme	bovine	361:366	arg1	S.					510:511	S.	510:511	S.	510:511	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	21	theme	bovine	361:366	arg1	factors					386:392	bovine blood coagulation factors	361:392	bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem	361:573	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	21	theme	bovine	361:366	arg1	Nishimura					448:456	Nishimura	448:456	Nishimura	448:456	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	21	theme	bovine	361:366	arg1	H.					471:472	H.	471:472	H.	471:472	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	21	theme	bovine	361:366	arg1	Takao					514:518	Takao	514:518	Takao	514:518	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	21	theme	bovine	361:366	arg1	Y.					537:538	Y.	537:538	Y.	537:538	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	5	22	attach	derived	950:956	arg2	glycopeptide					937:948	A glycopeptide	935:948	A glycopeptide derived from each of these proteins	935:984	A glycopeptide derived from each of these proteins was subjected to amino acid sequence and component sugar analyses and fast atom bombardment mass spectrometric analysis.
2511201	5	22	attach	derived	950:956	arg1	each					963:966	each	963:966	each	963:966	A glycopeptide derived from each of these proteins was subjected to amino acid sequence and component sugar analyses and fast atom bombardment mass spectrometric analysis.
2511201	5	22	attach	derived	950:956	arg1	proteins					977:984	these proteins	971:984	these proteins	971:984	A glycopeptide derived from each of these proteins was subjected to amino acid sequence and component sugar analyses and fast atom bombardment mass spectrometric analysis.
2511201	3	23	theme	sugar	603:607	arg1	chain					609:613	The sugar chain	599:613	The sugar chain identified in these clotting factors	599:650	The sugar chain identified in these clotting factors consists of 1 mol of hexose (glucose (Glc] and 2 mol of pentose (xylose (Xyl].
2511201	0	24	theme	epidermal	131:139	arg1	domain					160:165	the first epidermal growth factor-like domain	121:165	the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z	121:228	Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc) O-glycosidically linked to a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z.
2511201	0	24	theme	epidermal	131:139	arg1	factors					176:182	human factors	170:182	human factors VII and IX and protein Z and bovine protein Z	170:228	Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc) O-glycosidically linked to a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z.
2511201	1	25	theme	coagulation	374:384	arg1	Sueyoshi					475:482	Sueyoshi	475:482	Sueyoshi	475:482	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	25	theme	coagulation	374:384	arg1	VII					394:396	VII (Ser-52)	394:405	VII (Ser-52)	394:405	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	25	theme	coagulation	374:384	arg1	Kawabata					434:441	Kawabata	434:441	Kawabata	434:441	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	25	theme	coagulation	374:384	arg1	H.					459:460	H.	459:460	H.	459:460	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	25	theme	coagulation	374:384	arg1	Ikenaka					545:551	Ikenaka	545:551	Ikenaka	545:551	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	25	theme	coagulation	374:384	arg1	Iwanaga					501:507	Iwanaga	501:507	Iwanaga	501:507	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	25	theme	coagulation	374:384	arg1	T.					521:522	T.	521:522	T.	521:522	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	25	theme	coagulation	374:384	arg1	S.					430:431	S.	430:431	S.	430:431	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	25	theme	coagulation	374:384	arg1	Takeya					463:468	Takeya	463:468	Takeya	463:468	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	25	theme	coagulation	374:384	arg1	T.					497:498	T.	497:498	T.	497:498	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	25	theme	coagulation	374:384	arg1	T.					485:486	T.	485:486	T.	485:486	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	25	theme	coagulation	374:384	arg1	Shimonishi					525:534	Shimonishi	525:534	Shimonishi	525:534	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	25	theme	coagulation	374:384	arg1	S.					444:445	S.	444:445	S.	444:445	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	25	theme	coagulation	374:384	arg1	Miyata					489:494	Miyata	489:494	Miyata	489:494	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	25	theme	coagulation	374:384	arg1	T					554:554	T	554:554	T	554:554	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	25	theme	coagulation	374:384	arg1	S.					510:511	S.	510:511	S.	510:511	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	25	theme	coagulation	374:384	arg1	factors					386:392	bovine blood coagulation factors	361:392	bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem	361:573	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	25	theme	coagulation	374:384	arg1	Nishimura					448:456	Nishimura	448:456	Nishimura	448:456	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	25	theme	coagulation	374:384	arg1	H.					471:472	H.	471:472	H.	471:472	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	25	theme	coagulation	374:384	arg1	Takao					514:518	Takao	514:518	Takao	514:518	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	25	theme	coagulation	374:384	arg1	Y.					537:538	Y.	537:538	Y.	537:538	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	11	26	theme	biological	2065:2074	arg1	activities					2076:2085	the biological activities	2061:2085	the biological activities of these proteins	2061:2103	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	10	27	theme	sugar	1627:1631	arg1	compositions					1633:1644	These sugar compositions	1621:1644	These sugar compositions	1621:1644	These sugar compositions were confirmed by analyses of the intact proteins.
2511201	6	28	theme	Xyl	1210:1212	arg1	mol					1190:1192	1 mol	1188:1192	1 mol each of Glc and Xyl	1188:1212	The results indicate that the glycopeptide derived from human factor IX contains 1 mol each of Glc and Xyl.
2511201	11	29	theme	proteins	2096:2103	arg1	activities					2076:2085	the biological activities	2061:2085	the biological activities of these proteins	2061:2103	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	4	30	theme	carbohydrate	829:840	arg1	moieties					842:849	such carbohydrate moieties	824:849	such carbohydrate moieties linked to a serine residue at the same position found in bovine factors VII and IX	824:932	We report here that human factors VII and IX and protein Z and bovine protein Z also contain such carbohydrate moieties linked to a serine residue at the same position found in bovine factors VII and IX.
2511201	1	31	theme	serine	293:298	arg1	residue					300:306	a serine residue	291:306	a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem	291:573	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	0	32	theme	protein	199:205	arg1	Z					207:207	protein Z	199:207	protein Z	199:207	Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc) O-glycosidically linked to a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z.
2511201	0	32	theme	protein	199:205	arg1	factors					176:182	human factors	170:182	human factors VII and IX and protein Z and bovine protein Z	170:228	Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc) O-glycosidically linked to a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z.
2511201	8	33	link	O-linked	1527:1534	arg1	chains					1542:1547	these O-linked sugar chains	1521:1547	these O-linked sugar chains	1521:1547	In contrast, human factor VII and protein Z yielded two different glycopeptides which contained Glc and Xyl at molar ratios of 1:1 and 1:2, respectively, suggesting microheterogeneity of these O-linked sugar chains.
2511201	11	34	theme	Xyl-Glc-Ser	1856:1866	arg1	structure					1868:1876	a Xyl-Glc-Ser structure	1854:1876	a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown	1854:2114	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	11	35	dep	Z.	2008:2009	arg1	contribute					2047:2056	contribute	2047:2056	contribute to the biological activities of these proteins is unknown	2047:2114	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	8	36	theme	1:1	1461:1463	arg1	ratios					1451:1456	molar ratios	1445:1456	molar ratios of 1:1 and 1:2	1445:1471	In contrast, human factor VII and protein Z yielded two different glycopeptides which contained Glc and Xyl at molar ratios of 1:1 and 1:2, respectively, suggesting microheterogeneity of these O-linked sugar chains.
2511201	3	37	dep	glucose	681:687	arg1	Xyl					725:727	Xyl	725:727	Xyl	725:727	The sugar chain identified in these clotting factors consists of 1 mol of hexose (glucose (Glc] and 2 mol of pentose (xylose (Xyl].
2511201	1	38	theme	first	315:319	arg1	domains					350:356	the first epidermal growth factor-like domains	311:356	the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem	311:573	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	38	theme	first	315:319	arg1	factors					386:392	bovine blood coagulation factors	361:392	bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem	361:573	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	8	39	theme	1:2	1469:1471	arg1	ratios					1451:1456	molar ratios	1445:1456	molar ratios of 1:1 and 1:2	1445:1471	In contrast, human factor VII and protein Z yielded two different glycopeptides which contained Glc and Xyl at molar ratios of 1:1 and 1:2, respectively, suggesting microheterogeneity of these O-linked sugar chains.
2511201	4	40	from	position	890:897	arg1	residue					870:876	a serine residue	861:876	a serine residue at the same position found in bovine factors VII and IX	861:932	We report here that human factors VII and IX and protein Z and bovine protein Z also contain such carbohydrate moieties linked to a serine residue at the same position found in bovine factors VII and IX.
2511201	3	41	theme	hexose	673:678	arg1	mol					666:668	1 mol	664:668	1 mol of hexose (glucose (Glc] and 2 mol of pentose (xylose (Xyl]	664:728	The sugar chain identified in these clotting factors consists of 1 mol of hexose (glucose (Glc] and 2 mol of pentose (xylose (Xyl].
2511201	11	42	theme	first	1885:1889	arg1	VII					1945:1947	human factors VII	1931:1947	human factors VII	1931:1947	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	11	42	theme	first	1885:1889	arg1	domains					1920:1926	the first epidermal growth factor-like domains	1881:1926	the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown	1881:2114	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	11	42	theme	first	1885:1889	arg1	IX					1953:1954	IX	1953:1954	IX	1953:1954	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	11	42	theme	first	1885:1889	arg1	Z					1968:1968	protein Z	1960:1968	protein Z	1960:1968	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	11	43	theme	bovine	1993:1998	arg1	Z.					2008:2009	bovine protein Z.	1993:2009	bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown	1993:2114	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	9	44	theme	Bovine	1550:1555	arg1	glycopeptide					1567:1578	Bovine protein Z glycopeptide	1550:1578	Bovine protein Z glycopeptide	1550:1578	Bovine protein Z glycopeptide contained 1 mol of Glc and 2 mol of Xyl.
2511201	1	45	from	residue	300:306	arg1	domains					350:356	the first epidermal growth factor-like domains	311:356	the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem	311:573	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	45	from	residue	300:306	arg1	factors					386:392	bovine blood coagulation factors	361:392	bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem	361:573	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	5	46	gly	glycopeptide	937:948	arg2	glycopeptide					937:948	A glycopeptide	935:948	A glycopeptide derived from each of these proteins	935:984	A glycopeptide derived from each of these proteins was subjected to amino acid sequence and component sugar analyses and fast atom bombardment mass spectrometric analysis.
2511201	5	47	theme	sugar	1037:1041	arg1	analyses					1043:1050	component sugar analyses	1027:1050	component sugar analyses	1027:1050	A glycopeptide derived from each of these proteins was subjected to amino acid sequence and component sugar analyses and fast atom bombardment mass spectrometric analysis.
2511201	11	48	theme	Xyl2-Glc-Ser	1837:1848	arg1	existence					1822:1830	the existence	1818:1830	the existence of a Xyl2-Glc-Ser	1818:1848	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	11	48	theme	Xyl2-Glc-Ser	1837:1848	arg1	structure					1868:1876	a Xyl-Glc-Ser structure	1854:1876	a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown	1854:2114	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	11	49	theme	VII	1945:1947	arg1	VII					1945:1947	human factors VII	1931:1947	human factors VII	1931:1947	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	11	49	theme	VII	1945:1947	arg1	domains					1920:1926	the first epidermal growth factor-like domains	1881:1926	the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown	1881:2114	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	11	49	theme	VII	1945:1947	arg1	IX					1953:1954	IX	1953:1954	IX	1953:1954	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	11	49	theme	VII	1945:1947	arg1	Z					1968:1968	protein Z	1960:1968	protein Z	1960:1968	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	4	50	theme	factors	915:921	arg1	VII					923:925	bovine factors VII	908:925	bovine factors VII	908:925	We report here that human factors VII and IX and protein Z and bovine protein Z also contain such carbohydrate moieties linked to a serine residue at the same position found in bovine factors VII and IX.
2511201	3	51	theme	mol	701:703	arg1	xylose					717:722	2 mol of pentose (xylose	699:722	2 mol of pentose (xylose	699:722	The sugar chain identified in these clotting factors consists of 1 mol of hexose (glucose (Glc] and 2 mol of pentose (xylose (Xyl].
2511201	3	51	theme	mol	701:703	arg1	hexose					673:678	hexose	673:678	hexose (glucose (Glc] and 2 mol of pentose (xylose (Xyl]	673:728	The sugar chain identified in these clotting factors consists of 1 mol of hexose (glucose (Glc] and 2 mol of pentose (xylose (Xyl].
2511201	8	52	gly	microheterogeneity	1499:1516	arg1	chains					1542:1547	these O-linked sugar chains	1521:1547	these O-linked sugar chains	1521:1547	In contrast, human factor VII and protein Z yielded two different glycopeptides which contained Glc and Xyl at molar ratios of 1:1 and 1:2, respectively, suggesting microheterogeneity of these O-linked sugar chains.
2511201	0	53	from	residue	110:116	arg1	domain					160:165	the first epidermal growth factor-like domain	121:165	the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z	121:228	Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc) O-glycosidically linked to a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z.
2511201	0	53	from	residue	110:116	arg1	factors					176:182	human factors	170:182	human factors VII and IX and protein Z and bovine protein Z	170:228	Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc) O-glycosidically linked to a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z.
2511201	5	54	theme	acid	1009:1012	arg1	sequence					1014:1021	amino acid sequence	1003:1021	amino acid sequence	1003:1021	A glycopeptide derived from each of these proteins was subjected to amino acid sequence and component sugar analyses and fast atom bombardment mass spectrometric analysis.
2511201	0	55	attach	linked	91:96	arg1	residue					110:116	a serine residue	101:116	a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z	101:228	Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc) O-glycosidically linked to a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z.
2511201	0	55	attach	linked	91:96	arg2	Identification					0:13	Identification	0:13	Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc)	0:72	Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc) O-glycosidically linked to a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z.
2511201	11	56	theme	protein	1960:1966	arg1	Z					1968:1968	protein Z	1960:1968	protein Z	1960:1968	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	8	57	contain	contained	1420:1428	arg2	Xyl					1438:1440	Xyl	1438:1440	Xyl	1438:1440	In contrast, human factor VII and protein Z yielded two different glycopeptides which contained Glc and Xyl at molar ratios of 1:1 and 1:2, respectively, suggesting microheterogeneity of these O-linked sugar chains.
2511201	8	57	contain	contained	1420:1428	arg1	ratios					1451:1456	molar ratios	1445:1456	molar ratios of 1:1 and 1:2	1445:1471	In contrast, human factor VII and protein Z yielded two different glycopeptides which contained Glc and Xyl at molar ratios of 1:1 and 1:2, respectively, suggesting microheterogeneity of these O-linked sugar chains.
2511201	8	57	contain	contained	1420:1428	arg1	glycopeptides					1400:1412	two different glycopeptides	1386:1412	two different glycopeptides which contained Glc and Xyl at molar ratios of 1:1 and 1:2, respectively	1386:1485	In contrast, human factor VII and protein Z yielded two different glycopeptides which contained Glc and Xyl at molar ratios of 1:1 and 1:2, respectively, suggesting microheterogeneity of these O-linked sugar chains.
2511201	8	57	contain	contained	1420:1428	arg2	glycopeptides					1400:1412	two different glycopeptides	1386:1412	two different glycopeptides which contained Glc and Xyl at molar ratios of 1:1 and 1:2, respectively	1386:1485	In contrast, human factor VII and protein Z yielded two different glycopeptides which contained Glc and Xyl at molar ratios of 1:1 and 1:2, respectively, suggesting microheterogeneity of these O-linked sugar chains.
2511201	8	57	contain	contained	1420:1428	arg2	Glc					1430:1432	Glc	1430:1432	Glc	1430:1432	In contrast, human factor VII and protein Z yielded two different glycopeptides which contained Glc and Xyl at molar ratios of 1:1 and 1:2, respectively, suggesting microheterogeneity of these O-linked sugar chains.
2511201	11	58	from	structure	1868:1876	arg1	VII					1945:1947	human factors VII	1931:1947	human factors VII	1931:1947	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	11	58	from	structure	1868:1876	arg1	domains					1920:1926	the first epidermal growth factor-like domains	1881:1926	the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown	1881:2114	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	11	58	from	structure	1868:1876	arg1	IX					1953:1954	IX	1953:1954	IX	1953:1954	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	11	58	from	structure	1868:1876	arg1	Z					1968:1968	protein Z	1960:1968	protein Z	1960:1968	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	4	59	theme	human	751:755	arg1	VII					765:767	human factors VII	751:767	human factors VII	751:767	We report here that human factors VII and IX and protein Z and bovine protein Z also contain such carbohydrate moieties linked to a serine residue at the same position found in bovine factors VII and IX.
2511201	1	60	dep	factors	386:392	arg1	VII					394:396	VII (Ser-52)	394:405	VII (Ser-52)	394:405	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	60	dep	factors	386:392	arg1	1988					558:561	1988	558:561	1988	558:561	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	60	dep	factors	386:392	arg1	Y.					537:538	Y.	537:538	Y.	537:538	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	60	dep	factors	386:392	arg1	factors					386:392	bovine blood coagulation factors	361:392	bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem	361:573	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	0	61	theme	human	170:174	arg1	Z					207:207	protein Z	199:207	protein Z	199:207	Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc) O-glycosidically linked to a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z.
2511201	0	61	theme	human	170:174	arg1	VII					184:186	VII	184:186	VII	184:186	Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc) O-glycosidically linked to a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z.
2511201	0	61	theme	human	170:174	arg1	Z					228:228	bovine protein Z	213:228	bovine protein Z	213:228	Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc) O-glycosidically linked to a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z.
2511201	0	61	theme	human	170:174	arg1	factors					176:182	human factors	170:182	human factors VII and IX and protein Z and bovine protein Z	170:228	Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc) O-glycosidically linked to a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z.
2511201	0	61	theme	human	170:174	arg1	IX					192:193	IX	192:193	IX	192:193	Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc) O-glycosidically linked to a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z.
2511201	11	62	theme	sugar	1730:1734	arg1	chain					1736:1740	the trisaccharide sugar chain	1712:1740	the trisaccharide sugar chain previously discovered in bovine factors VII and IX	1712:1791	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	3	63	theme	pentose	708:714	arg1	xylose					717:722	2 mol of pentose (xylose	699:722	2 mol of pentose (xylose	699:722	The sugar chain identified in these clotting factors consists of 1 mol of hexose (glucose (Glc] and 2 mol of pentose (xylose (Xyl].
2511201	3	63	theme	pentose	708:714	arg1	hexose					673:678	hexose	673:678	hexose (glucose (Glc] and 2 mol of pentose (xylose (Xyl]	673:728	The sugar chain identified in these clotting factors consists of 1 mol of hexose (glucose (Glc] and 2 mol of pentose (xylose (Xyl].
2511201	4	64	theme	protein	801:807	arg1	Z					809:809	bovine protein Z	794:809	bovine protein Z	794:809	We report here that human factors VII and IX and protein Z and bovine protein Z also contain such carbohydrate moieties linked to a serine residue at the same position found in bovine factors VII and IX.
2511201	11	65	theme	human	1931:1935	arg1	VII					1945:1947	human factors VII	1931:1947	human factors VII	1931:1947	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	8	66	theme	O-linked	1527:1534	arg1	chains					1542:1547	these O-linked sugar chains	1521:1547	these O-linked sugar chains	1521:1547	In contrast, human factor VII and protein Z yielded two different glycopeptides which contained Glc and Xyl at molar ratios of 1:1 and 1:2, respectively, suggesting microheterogeneity of these O-linked sugar chains.
2511201	8	67	theme	human	1347:1351	arg1	VII					1360:1362	human factor VII	1347:1362	human factor VII	1347:1362	In contrast, human factor VII and protein Z yielded two different glycopeptides which contained Glc and Xyl at molar ratios of 1:1 and 1:2, respectively, suggesting microheterogeneity of these O-linked sugar chains.
2511201	11	68	theme	factors	1774:1780	arg1	VII					1782:1784	bovine factors VII	1767:1784	bovine factors VII	1767:1784	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	9	69	theme	protein	1557:1563	arg1	glycopeptide					1567:1578	Bovine protein Z glycopeptide	1550:1578	Bovine protein Z glycopeptide	1550:1578	Bovine protein Z glycopeptide contained 1 mol of Glc and 2 mol of Xyl.
2511201	8	70	theme	chains	1542:1547	arg1	microheterogeneity					1499:1516	microheterogeneity	1499:1516	microheterogeneity of these O-linked sugar chains	1499:1547	In contrast, human factor VII and protein Z yielded two different glycopeptides which contained Glc and Xyl at molar ratios of 1:1 and 1:2, respectively, suggesting microheterogeneity of these O-linked sugar chains.
2511201	5	71	theme	atom	1061:1064	arg1	bombardment					1066:1076	fast atom bombardment	1056:1076	fast atom bombardment	1056:1076	A glycopeptide derived from each of these proteins was subjected to amino acid sequence and component sugar analyses and fast atom bombardment mass spectrometric analysis.
2511201	4	72	theme	protein	780:786	arg1	Z					788:788	protein Z	780:788	protein Z	780:788	We report here that human factors VII and IX and protein Z and bovine protein Z also contain such carbohydrate moieties linked to a serine residue at the same position found in bovine factors VII and IX.
2511201	0	73	theme	serine	103:108	arg1	residue					110:116	a serine residue	101:116	a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z	101:228	Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc) O-glycosidically linked to a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z.
2511201	5	74	theme	mass	1078:1081	arg1	analysis					1097:1104	mass spectrometric analysis	1078:1104	mass spectrometric analysis	1078:1104	A glycopeptide derived from each of these proteins was subjected to amino acid sequence and component sugar analyses and fast atom bombardment mass spectrometric analysis.
2511201	1	75	attach	linked	281:286	arg2	trisaccharide					267:279	a unique trisaccharide	258:279	a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem	258:573	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	75	attach	linked	281:286	arg1	residue					300:306	a serine residue	291:306	a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem	291:573	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	8	76	theme	protein	1368:1374	arg1	Z					1376:1376	protein Z	1368:1376	protein Z	1368:1376	In contrast, human factor VII and protein Z yielded two different glycopeptides which contained Glc and Xyl at molar ratios of 1:1 and 1:2, respectively, suggesting microheterogeneity of these O-linked sugar chains.
2511201	11	77	theme	growth	1901:1906	arg1	VII					1945:1947	human factors VII	1931:1947	human factors VII	1931:1947	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	11	77	theme	growth	1901:1906	arg1	domains					1920:1926	the first epidermal growth factor-like domains	1881:1926	the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown	1881:2114	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	11	77	theme	growth	1901:1906	arg1	IX					1953:1954	IX	1953:1954	IX	1953:1954	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	11	77	theme	growth	1901:1906	arg1	Z					1968:1968	protein Z	1960:1968	protein Z	1960:1968	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	1	78	theme	factor-like	338:348	arg1	domains					350:356	the first epidermal growth factor-like domains	311:356	the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem	311:573	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	78	theme	factor-like	338:348	arg1	factors					386:392	bovine blood coagulation factors	361:392	bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem	361:573	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	6	79	theme	factor	1169:1174	arg1	IX					1176:1177	human factor IX	1163:1177	human factor IX	1163:1177	The results indicate that the glycopeptide derived from human factor IX contains 1 mol each of Glc and Xyl.
2511201	11	80	theme	carbohydrate	2025:2036	arg1	moieties					2038:2045	these carbohydrate moieties	2019:2045	these carbohydrate moieties	2019:2045	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	11	81	theme	epidermal	1891:1899	arg1	VII					1945:1947	human factors VII	1931:1947	human factors VII	1931:1947	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	11	81	theme	epidermal	1891:1899	arg1	domains					1920:1926	the first epidermal growth factor-like domains	1881:1926	the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown	1881:2114	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	11	81	theme	epidermal	1891:1899	arg1	IX					1953:1954	IX	1953:1954	IX	1953:1954	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	11	81	theme	epidermal	1891:1899	arg1	Z					1968:1968	protein Z	1960:1968	protein Z	1960:1968	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	0	82	theme	first	125:129	arg1	domain					160:165	the first epidermal growth factor-like domain	121:165	the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z	121:228	Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc) O-glycosidically linked to a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z.
2511201	0	82	theme	first	125:129	arg1	factors					176:182	human factors	170:182	human factors VII and IX and protein Z and bovine protein Z	170:228	Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc) O-glycosidically linked to a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z.
2511201	8	83	theme	different	1390:1398	arg1	glycopeptides					1400:1412	two different glycopeptides	1386:1412	two different glycopeptides which contained Glc and Xyl at molar ratios of 1:1 and 1:2, respectively	1386:1485	In contrast, human factor VII and protein Z yielded two different glycopeptides which contained Glc and Xyl at molar ratios of 1:1 and 1:2, respectively, suggesting microheterogeneity of these O-linked sugar chains.
2511201	7	84	theme	disaccharide	1240:1251	arg1	end					1228:1230	The reducing end	1215:1230	The reducing end of this disaccharide	1215:1251	The reducing end of this disaccharide was identified as Glc by analyzing the disaccharide generated by hydrazinolysis.
2511201	7	84	theme	disaccharide	1240:1251	arg1	Glc					1271:1273	Glc	1271:1273	Glc	1271:1273	The reducing end of this disaccharide was identified as Glc by analyzing the disaccharide generated by hydrazinolysis.
2511201	4	85	theme	serine	863:868	arg1	residue					870:876	a serine residue	861:876	a serine residue at the same position found in bovine factors VII and IX	861:932	We report here that human factors VII and IX and protein Z and bovine protein Z also contain such carbohydrate moieties linked to a serine residue at the same position found in bovine factors VII and IX.
2511201	6	86	theme	Glc	1202:1204	arg1	mol					1190:1192	1 mol	1188:1192	1 mol each of Glc and Xyl	1188:1212	The results indicate that the glycopeptide derived from human factor IX contains 1 mol each of Glc and Xyl.
2511201	0	87	theme	growth	141:146	arg1	domain					160:165	the first epidermal growth factor-like domain	121:165	the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z	121:228	Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc) O-glycosidically linked to a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z.
2511201	0	87	theme	growth	141:146	arg1	factors					176:182	human factors	170:182	human factors VII and IX and protein Z and bovine protein Z	170:228	Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc) O-glycosidically linked to a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z.
2511201	1	88	theme	blood	368:372	arg1	Sueyoshi					475:482	Sueyoshi	475:482	Sueyoshi	475:482	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	88	theme	blood	368:372	arg1	VII					394:396	VII (Ser-52)	394:405	VII (Ser-52)	394:405	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	88	theme	blood	368:372	arg1	Kawabata					434:441	Kawabata	434:441	Kawabata	434:441	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	88	theme	blood	368:372	arg1	H.					459:460	H.	459:460	H.	459:460	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	88	theme	blood	368:372	arg1	Ikenaka					545:551	Ikenaka	545:551	Ikenaka	545:551	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	88	theme	blood	368:372	arg1	Iwanaga					501:507	Iwanaga	501:507	Iwanaga	501:507	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	88	theme	blood	368:372	arg1	T.					521:522	T.	521:522	T.	521:522	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	88	theme	blood	368:372	arg1	S.					430:431	S.	430:431	S.	430:431	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	88	theme	blood	368:372	arg1	Takeya					463:468	Takeya	463:468	Takeya	463:468	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	88	theme	blood	368:372	arg1	T.					497:498	T.	497:498	T.	497:498	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	88	theme	blood	368:372	arg1	T.					485:486	T.	485:486	T.	485:486	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	88	theme	blood	368:372	arg1	Shimonishi					525:534	Shimonishi	525:534	Shimonishi	525:534	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	88	theme	blood	368:372	arg1	S.					444:445	S.	444:445	S.	444:445	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	88	theme	blood	368:372	arg1	Miyata					489:494	Miyata	489:494	Miyata	489:494	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	88	theme	blood	368:372	arg1	T					554:554	T	554:554	T	554:554	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	88	theme	blood	368:372	arg1	S.					510:511	S.	510:511	S.	510:511	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	88	theme	blood	368:372	arg1	factors					386:392	bovine blood coagulation factors	361:392	bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem	361:573	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	88	theme	blood	368:372	arg1	Nishimura					448:456	Nishimura	448:456	Nishimura	448:456	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	88	theme	blood	368:372	arg1	H.					471:472	H.	471:472	H.	471:472	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	88	theme	blood	368:372	arg1	Takao					514:518	Takao	514:518	Takao	514:518	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	88	theme	blood	368:372	arg1	Y.					537:538	Y.	537:538	Y.	537:538	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	6	89	attach	derived	1150:1156	arg2	glycopeptide					1137:1148	the glycopeptide	1133:1148	the glycopeptide derived from human factor IX	1133:1177	The results indicate that the glycopeptide derived from human factor IX contains 1 mol each of Glc and Xyl.
2511201	6	89	attach	derived	1150:1156	arg1	IX					1176:1177	human factor IX	1163:1177	human factor IX	1163:1177	The results indicate that the glycopeptide derived from human factor IX contains 1 mol each of Glc and Xyl.
2511201	4	90	theme	such	824:827	arg1	moieties					842:849	such carbohydrate moieties	824:849	such carbohydrate moieties linked to a serine residue at the same position found in bovine factors VII and IX	824:932	We report here that human factors VII and IX and protein Z and bovine protein Z also contain such carbohydrate moieties linked to a serine residue at the same position found in bovine factors VII and IX.
2511201	0	91	theme	trisaccharide	49:61	arg1	Identification					0:13	Identification	0:13	Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc)	0:72	Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc) O-glycosidically linked to a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z.
2511201	1	92	theme	factors	386:392	arg1	domains					350:356	the first epidermal growth factor-like domains	311:356	the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem	311:573	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	92	theme	factors	386:392	arg1	factors					386:392	bovine blood coagulation factors	361:392	bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem	361:573	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	10	93	theme	proteins	1687:1694	arg1	analyses					1664:1671	analyses	1664:1671	analyses of the intact proteins	1664:1694	These sugar compositions were confirmed by analyses of the intact proteins.
2511201	7	94	theme	reducing	1219:1226	arg1	end					1228:1230	The reducing end	1215:1230	The reducing end of this disaccharide	1215:1251	The reducing end of this disaccharide was identified as Glc by analyzing the disaccharide generated by hydrazinolysis.
2511201	7	94	theme	reducing	1219:1226	arg1	Glc					1271:1273	Glc	1271:1273	Glc	1271:1273	The reducing end of this disaccharide was identified as Glc by analyzing the disaccharide generated by hydrazinolysis.
2511201	8	95	gly	glycopeptides	1400:1412	arg2	glycopeptides					1400:1412	two different glycopeptides	1386:1412	two different glycopeptides which contained Glc and Xyl at molar ratios of 1:1 and 1:2, respectively	1386:1485	In contrast, human factor VII and protein Z yielded two different glycopeptides which contained Glc and Xyl at molar ratios of 1:1 and 1:2, respectively, suggesting microheterogeneity of these O-linked sugar chains.
2511201	9	96	theme	Xyl	1616:1618	arg1	mol					1609:1611	2 mol	1607:1611	2 mol of Xyl	1607:1618	Bovine protein Z glycopeptide contained 1 mol of Glc and 2 mol of Xyl.
2511201	9	96	theme	Xyl	1616:1618	arg1	mol					1592:1594	1 mol	1590:1594	1 mol of Glc	1590:1601	Bovine protein Z glycopeptide contained 1 mol of Glc and 2 mol of Xyl.
2511201	3	97	theme	clotting	635:642	arg1	factors					644:650	these clotting factors	629:650	these clotting factors	629:650	The sugar chain identified in these clotting factors consists of 1 mol of hexose (glucose (Glc] and 2 mol of pentose (xylose (Xyl].
2511201	8	98	theme	molar	1445:1449	arg1	ratios					1451:1456	molar ratios	1445:1456	molar ratios of 1:1 and 1:2	1445:1471	In contrast, human factor VII and protein Z yielded two different glycopeptides which contained Glc and Xyl at molar ratios of 1:1 and 1:2, respectively, suggesting microheterogeneity of these O-linked sugar chains.
2511201	4	99	theme	bovine	908:913	arg1	VII					923:925	bovine factors VII	908:925	bovine factors VII	908:925	We report here that human factors VII and IX and protein Z and bovine protein Z also contain such carbohydrate moieties linked to a serine residue at the same position found in bovine factors VII and IX.
2511201	10	100	theme	intact	1680:1685	arg1	proteins					1687:1694	the intact proteins	1676:1694	the intact proteins	1676:1694	These sugar compositions were confirmed by analyses of the intact proteins.
2511201	11	101	theme	protein	2000:2006	arg1	Z.					2008:2009	bovine protein Z.	1993:2009	bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown	1993:2114	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	1	102	theme	epidermal	321:329	arg1	domains					350:356	the first epidermal growth factor-like domains	311:356	the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem	311:573	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	1	102	theme	epidermal	321:329	arg1	factors					386:392	bovine blood coagulation factors	361:392	bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem	361:573	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	6	103	contain	contains	1179:1186	arg2	mol					1190:1192	1 mol	1188:1192	1 mol each of Glc and Xyl	1188:1212	The results indicate that the glycopeptide derived from human factor IX contains 1 mol each of Glc and Xyl.
2511201	6	103	contain	contains	1179:1186	arg1	glycopeptide					1137:1148	the glycopeptide	1133:1148	the glycopeptide derived from human factor IX	1133:1177	The results indicate that the glycopeptide derived from human factor IX contains 1 mol each of Glc and Xyl.
2511201	0	104	theme	bovine	213:218	arg1	Z					228:228	bovine protein Z	213:228	bovine protein Z	213:228	Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc) O-glycosidically linked to a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z.
2511201	0	104	theme	bovine	213:218	arg1	factors					176:182	human factors	170:182	human factors VII and IX and protein Z and bovine protein Z	170:228	Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc) O-glycosidically linked to a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z.
2511201	4	105	located	found	899:903	arg1	IX					931:932	IX	931:932	IX	931:932	We report here that human factors VII and IX and protein Z and bovine protein Z also contain such carbohydrate moieties linked to a serine residue at the same position found in bovine factors VII and IX.
2511201	4	105	located	found	899:903	arg1	VII					923:925	bovine factors VII	908:925	bovine factors VII	908:925	We report here that human factors VII and IX and protein Z and bovine protein Z also contain such carbohydrate moieties linked to a serine residue at the same position found in bovine factors VII and IX.
2511201	4	105	located	found	899:903	arg2	position					890:897	the same position	881:897	the same position found in bovine factors VII and IX	881:932	We report here that human factors VII and IX and protein Z and bovine protein Z also contain such carbohydrate moieties linked to a serine residue at the same position found in bovine factors VII and IX.
2511201	4	106	theme	same	885:888	arg1	position					890:897	the same position	881:897	the same position found in bovine factors VII and IX	881:932	We report here that human factors VII and IX and protein Z and bovine protein Z also contain such carbohydrate moieties linked to a serine residue at the same position found in bovine factors VII and IX.
2511201	0	107	theme	disaccharide	20:31	arg1	Identification					0:13	Identification	0:13	Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc)	0:72	Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc) O-glycosidically linked to a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z.
2511201	5	108	theme	component	1027:1035	arg1	analyses					1043:1050	component sugar analyses	1027:1050	component sugar analyses	1027:1050	A glycopeptide derived from each of these proteins was subjected to amino acid sequence and component sugar analyses and fast atom bombardment mass spectrometric analysis.
2511201	1	109	theme	unique	260:265	arg1	trisaccharide					267:279	a unique trisaccharide	258:279	a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem	258:573	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	6	110	gly	glycopeptide	1137:1148	arg2	glycopeptide					1137:1148	the glycopeptide	1133:1148	the glycopeptide derived from human factor IX	1133:1177	The results indicate that the glycopeptide derived from human factor IX contains 1 mol each of Glc and Xyl.
2511201	11	111	from	existence	1822:1830	arg1	VII					1945:1947	human factors VII	1931:1947	human factors VII	1931:1947	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	11	111	from	existence	1822:1830	arg1	domains					1920:1926	the first epidermal growth factor-like domains	1881:1926	the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown	1881:2114	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	11	111	from	existence	1822:1830	arg1	IX					1953:1954	IX	1953:1954	IX	1953:1954	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	11	111	from	existence	1822:1830	arg1	Z					1968:1968	protein Z	1960:1968	protein Z	1960:1968	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
2511201	6	112	theme	human	1163:1167	arg1	IX					1176:1177	human factor IX	1163:1177	human factor IX	1163:1177	The results indicate that the glycopeptide derived from human factor IX contains 1 mol each of Glc and Xyl.
2511201	1	113	dep	Y.	537:538	arg1	Biochem					567:573	Biochem	567:573	Biochem	567:573	We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem.
2511201	0	114	theme	protein	220:226	arg1	Z					228:228	bovine protein Z	213:228	bovine protein Z	213:228	Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc) O-glycosidically linked to a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z.
2511201	0	114	theme	protein	220:226	arg1	factors					176:182	human factors	170:182	human factors VII and IX and protein Z and bovine protein Z	170:228	Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc) O-glycosidically linked to a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z.
2511201	4	115	theme	factors	757:763	arg1	VII					765:767	human factors VII	751:767	human factors VII	751:767	We report here that human factors VII and IX and protein Z and bovine protein Z also contain such carbohydrate moieties linked to a serine residue at the same position found in bovine factors VII and IX.
2511201	5	116	theme	amino	1003:1007	arg1	sequence					1014:1021	amino acid sequence	1003:1021	amino acid sequence	1003:1021	A glycopeptide derived from each of these proteins was subjected to amino acid sequence and component sugar analyses and fast atom bombardment mass spectrometric analysis.
2511201	4	117	attach	linked	851:856	arg1	residue					870:876	a serine residue	861:876	a serine residue at the same position found in bovine factors VII and IX	861:932	We report here that human factors VII and IX and protein Z and bovine protein Z also contain such carbohydrate moieties linked to a serine residue at the same position found in bovine factors VII and IX.
2511201	4	117	attach	linked	851:856	arg2	moieties					842:849	such carbohydrate moieties	824:849	such carbohydrate moieties linked to a serine residue at the same position found in bovine factors VII and IX	824:932	We report here that human factors VII and IX and protein Z and bovine protein Z also contain such carbohydrate moieties linked to a serine residue at the same position found in bovine factors VII and IX.
2511201	3	118	theme	of	705:706	arg1	xylose					717:722	2 mol of pentose (xylose	699:722	2 mol of pentose (xylose	699:722	The sugar chain identified in these clotting factors consists of 1 mol of hexose (glucose (Glc] and 2 mol of pentose (xylose (Xyl].
2511201	3	118	theme	of	705:706	arg1	hexose					673:678	hexose	673:678	hexose (glucose (Glc] and 2 mol of pentose (xylose (Xyl]	673:728	The sugar chain identified in these clotting factors consists of 1 mol of hexose (glucose (Glc] and 2 mol of pentose (xylose (Xyl].
2511201	11	119	theme	factors	1937:1943	arg1	VII					1945:1947	human factors VII	1931:1947	human factors VII	1931:1947	In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.
7944531	0	0	theme	localised	76:84	arg1	N-acetyl-glucosaminyltransferase					86:117	Golgi localised N-acetyl-glucosaminyltransferase II	70:120	Golgi localised N-acetyl-glucosaminyltransferase II	70:120	Carbohydrate deficient glycoprotein syndrome type II: a deficiency in Golgi localised N-acetyl-glucosaminyltransferase II.
7944531	4	1	theme	type	485:488	arg1	patients					492:499	type I patients	485:499	type I patients	485:499	Compared with type I patients they have a more severe psychomotor retardation but no peripheral neuropathy nor cerebellar hypoplasia.
7944531	7	2	theme	N-acetylglucosaminyltransferase	1008:1038	arg1	activity					979:986	A profoundly deficient activity	956:986	A profoundly deficient activity of the Golgi enzyme N-acetylglucosaminyltransferase II (EC 2.4.1.143)	956:1056	A profoundly deficient activity of the Golgi enzyme N-acetylglucosaminyltransferase II (EC 2.4.1.143) was demonstrated in fibroblasts.
7944531	0	3	theme	Golgi	70:74	arg1	N-acetyl-glucosaminyltransferase					86:117	Golgi localised N-acetyl-glucosaminyltransferase II	70:120	Golgi localised N-acetyl-glucosaminyltransferase II	70:120	Carbohydrate deficient glycoprotein syndrome type II: a deficiency in Golgi localised N-acetyl-glucosaminyltransferase II.
7944531	4	4	theme	peripheral	556:565	arg1	neuropathy					567:576	peripheral neuropathy	556:576	peripheral neuropathy	556:576	Compared with type I patients they have a more severe psychomotor retardation but no peripheral neuropathy nor cerebellar hypoplasia.
7944531	6	5	contain	contained	787:795	arg1	disialotransferrin					735:752	The serum disialotransferrin	725:752	The serum disialotransferrin	725:752	The serum disialotransferrin, studied in the present patient, contained two moles of truncated monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc (beta 1-->4)GlcNAc-Asn per mole of transferrin.
7944531	6	5	contain	contained	787:795	arg2	moles					801:805	two moles	797:805	two moles of truncated monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc (beta 1-->4)GlcNAc-Asn per mole of transferrin	797:953	The serum disialotransferrin, studied in the present patient, contained two moles of truncated monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc (beta 1-->4)GlcNAc-Asn per mole of transferrin.
7944531	4	6	dep	have	506:509	arg1	Compared					471:478	Compared	471:478	Compared with type I patients	471:499	Compared with type I patients they have a more severe psychomotor retardation but no peripheral neuropathy nor cerebellar hypoplasia.
7944531	6	7	theme	Sialyl-Gal-GlcNAc-Man	834:854	arg1	GlcNAc					901:906	monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc	820:906	truncated monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc (beta 1-->4)GlcNAc-Asn	810:929	The serum disialotransferrin, studied in the present patient, contained two moles of truncated monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc (beta 1-->4)GlcNAc-Asn per mole of transferrin.
7944531	6	7	theme	Sialyl-Gal-GlcNAc-Man	834:854	arg1	1-->4					914:918	beta 1-->4	909:918	beta 1-->4	909:918	The serum disialotransferrin, studied in the present patient, contained two moles of truncated monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc (beta 1-->4)GlcNAc-Asn per mole of transferrin.
7944531	4	8	theme	cerebellar	582:591	arg1	hypoplasia					593:602	cerebellar hypoplasia	582:602	cerebellar hypoplasia	582:602	Compared with type I patients they have a more severe psychomotor retardation but no peripheral neuropathy nor cerebellar hypoplasia.
7944531	6	9	theme	beta	890:893	arg1	GlcNAc					901:906	monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc	820:906	truncated monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc (beta 1-->4)GlcNAc-Asn	810:929	The serum disialotransferrin, studied in the present patient, contained two moles of truncated monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc (beta 1-->4)GlcNAc-Asn per mole of transferrin.
7944531	6	9	theme	beta	890:893	arg1	1-->4					914:918	beta 1-->4	909:918	beta 1-->4	909:918	The serum disialotransferrin, studied in the present patient, contained two moles of truncated monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc (beta 1-->4)GlcNAc-Asn per mole of transferrin.
7944531	6	10	theme	monoantennary	820:832	arg1	GlcNAc					901:906	monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc	820:906	truncated monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc (beta 1-->4)GlcNAc-Asn	810:929	The serum disialotransferrin, studied in the present patient, contained two moles of truncated monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc (beta 1-->4)GlcNAc-Asn per mole of transferrin.
7944531	6	10	theme	monoantennary	820:832	arg1	1-->4					914:918	beta 1-->4	909:918	beta 1-->4	909:918	The serum disialotransferrin, studied in the present patient, contained two moles of truncated monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc (beta 1-->4)GlcNAc-Asn per mole of transferrin.
7944531	6	11	theme	serum	729:733	arg1	disialotransferrin					735:752	The serum disialotransferrin	725:752	The serum disialotransferrin	725:752	The serum disialotransferrin, studied in the present patient, contained two moles of truncated monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc (beta 1-->4)GlcNAc-Asn per mole of transferrin.
7944531	5	12	theme	transferrin	615:625	arg1	pattern					635:641	The serum transferrin isoform pattern	605:641	The serum transferrin isoform pattern obtained by isoelectric focusing	605:674	The serum transferrin isoform pattern obtained by isoelectric focusing showed disialotransferrin as the major fraction.
7944531	5	13	theme	serum	609:613	arg1	pattern					635:641	The serum transferrin isoform pattern	605:641	The serum transferrin isoform pattern obtained by isoelectric focusing	605:674	The serum transferrin isoform pattern obtained by isoelectric focusing showed disialotransferrin as the major fraction.
7944531	4	14	contain	have	506:509	arg2	retardation					537:547	a more severe psychomotor retardation	511:547	a more severe psychomotor retardation but no peripheral neuropathy nor cerebellar hypoplasia	511:602	Compared with type I patients they have a more severe psychomotor retardation but no peripheral neuropathy nor cerebellar hypoplasia.
7944531	4	14	contain	have	506:509	arg2	neuropathy					567:576	peripheral neuropathy	556:576	peripheral neuropathy	556:576	Compared with type I patients they have a more severe psychomotor retardation but no peripheral neuropathy nor cerebellar hypoplasia.
7944531	4	14	contain	have	506:509	arg1	they					501:504	they	501:504	they	501:504	Compared with type I patients they have a more severe psychomotor retardation but no peripheral neuropathy nor cerebellar hypoplasia.
7944531	6	15	theme	Man	886:888	arg1	GlcNAc					901:906	monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc	820:906	truncated monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc (beta 1-->4)GlcNAc-Asn	810:929	The serum disialotransferrin, studied in the present patient, contained two moles of truncated monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc (beta 1-->4)GlcNAc-Asn per mole of transferrin.
7944531	6	15	theme	Man	886:888	arg1	1-->4					914:918	beta 1-->4	909:918	beta 1-->4	909:918	The serum disialotransferrin, studied in the present patient, contained two moles of truncated monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc (beta 1-->4)GlcNAc-Asn per mole of transferrin.
7944531	5	16	theme	isoform	627:633	arg1	pattern					635:641	The serum transferrin isoform pattern	605:641	The serum transferrin isoform pattern obtained by isoelectric focusing	605:674	The serum transferrin isoform pattern obtained by isoelectric focusing showed disialotransferrin as the major fraction.
7944531	7	17	theme	deficient	969:977	arg1	activity					979:986	A profoundly deficient activity	956:986	A profoundly deficient activity of the Golgi enzyme N-acetylglucosaminyltransferase II (EC 2.4.1.143)	956:1056	A profoundly deficient activity of the Golgi enzyme N-acetylglucosaminyltransferase II (EC 2.4.1.143) was demonstrated in fibroblasts.
7944531	0	18	theme	deficient	13:21	arg1	type					45:48	Carbohydrate deficient glycoprotein syndrome type II	0:51	Carbohydrate deficient glycoprotein syndrome type II: a deficiency in Golgi localised N-acetyl-glucosaminyltransferase II.	0:121	Carbohydrate deficient glycoprotein syndrome type II: a deficiency in Golgi localised N-acetyl-glucosaminyltransferase II.
7944531	6	19	theme	transferrin	943:953	arg1	mole					935:938	mole	935:938	mole of transferrin	935:953	The serum disialotransferrin, studied in the present patient, contained two moles of truncated monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc (beta 1-->4)GlcNAc-Asn per mole of transferrin.
7944531	6	20	theme	alpha	856:860	arg1	GlcNAc					901:906	monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc	820:906	truncated monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc (beta 1-->4)GlcNAc-Asn	810:929	The serum disialotransferrin, studied in the present patient, contained two moles of truncated monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc (beta 1-->4)GlcNAc-Asn per mole of transferrin.
7944531	6	20	theme	alpha	856:860	arg1	1-->4					914:918	beta 1-->4	909:918	beta 1-->4	909:918	The serum disialotransferrin, studied in the present patient, contained two moles of truncated monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc (beta 1-->4)GlcNAc-Asn per mole of transferrin.
7944531	1	21	theme	genetic	195:201	arg1	disorders					217:225	genetic multisystemic disorders	195:225	genetic multisystemic disorders with severe nervous system involvement	195:264	The carbohydrate deficient glycoprotein (CDG) syndromes are a family of genetic multisystemic disorders with severe nervous system involvement.
7944531	0	22	theme	syndrome	36:43	arg1	type					45:48	Carbohydrate deficient glycoprotein syndrome type II	0:51	Carbohydrate deficient glycoprotein syndrome type II: a deficiency in Golgi localised N-acetyl-glucosaminyltransferase II.	0:121	Carbohydrate deficient glycoprotein syndrome type II: a deficiency in Golgi localised N-acetyl-glucosaminyltransferase II.
7944531	4	23	theme	psychomotor	525:535	arg1	retardation					537:547	a more severe psychomotor retardation	511:547	a more severe psychomotor retardation but no peripheral neuropathy nor cerebellar hypoplasia	511:602	Compared with type I patients they have a more severe psychomotor retardation but no peripheral neuropathy nor cerebellar hypoplasia.
7944531	6	24	theme	truncated	810:818	arg1	GlcNAc-Asn					920:929	truncated monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc (beta 1-->4)GlcNAc-Asn	810:929	truncated monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc (beta 1-->4)GlcNAc-Asn	810:929	The serum disialotransferrin, studied in the present patient, contained two moles of truncated monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc (beta 1-->4)GlcNAc-Asn per mole of transferrin.
7944531	1	25	theme	multisystemic	203:215	arg1	disorders					217:225	genetic multisystemic disorders	195:225	genetic multisystemic disorders with severe nervous system involvement	195:264	The carbohydrate deficient glycoprotein (CDG) syndromes are a family of genetic multisystemic disorders with severe nervous system involvement.
7944531	0	26	theme	glycoprotein	23:34	arg1	type					45:48	Carbohydrate deficient glycoprotein syndrome type II	0:51	Carbohydrate deficient glycoprotein syndrome type II: a deficiency in Golgi localised N-acetyl-glucosaminyltransferase II.	0:121	Carbohydrate deficient glycoprotein syndrome type II: a deficiency in Golgi localised N-acetyl-glucosaminyltransferase II.
7944531	2	27	theme	CDG	300:302	arg1	syndrome					304:311	a CDG syndrome	298:311	a CDG syndrome that differs from the classical picture but is very similar to a patient reported in 1991	298:401	This report is on a child with a CDG syndrome that differs from the classical picture but is very similar to a patient reported in 1991.
7944531	2	27	theme	CDG	300:302	arg1	similar					365:371	similar	365:371	similar	365:371	This report is on a child with a CDG syndrome that differs from the classical picture but is very similar to a patient reported in 1991.
7944531	6	28	theme	GlcNAc	901:906	arg1	GlcNAc-Asn					920:929	truncated monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc (beta 1-->4)GlcNAc-Asn	810:929	truncated monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc (beta 1-->4)GlcNAc-Asn	810:929	The serum disialotransferrin, studied in the present patient, contained two moles of truncated monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc (beta 1-->4)GlcNAc-Asn per mole of transferrin.
7944531	1	29	theme	disorders	217:225	arg1	syndromes					169:177	The carbohydrate deficient glycoprotein (CDG) syndromes	123:177	The carbohydrate deficient glycoprotein (CDG) syndromes	123:177	The carbohydrate deficient glycoprotein (CDG) syndromes are a family of genetic multisystemic disorders with severe nervous system involvement.
7944531	1	29	theme	disorders	217:225	arg1	family					185:190	a family	183:190	a family of genetic multisystemic disorders with severe nervous system involvement	183:264	The carbohydrate deficient glycoprotein (CDG) syndromes are a family of genetic multisystemic disorders with severe nervous system involvement.
7944531	2	30	theme	classical	335:343	arg1	picture					345:351	the classical picture	331:351	the classical picture	331:351	This report is on a child with a CDG syndrome that differs from the classical picture but is very similar to a patient reported in 1991.
7944531	6	31	theme	1-->6	879:883	arg1	GlcNAc					901:906	monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc	820:906	truncated monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc (beta 1-->4)GlcNAc-Asn	810:929	The serum disialotransferrin, studied in the present patient, contained two moles of truncated monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc (beta 1-->4)GlcNAc-Asn per mole of transferrin.
7944531	6	31	theme	1-->6	879:883	arg1	1-->4					914:918	beta 1-->4	909:918	beta 1-->4	909:918	The serum disialotransferrin, studied in the present patient, contained two moles of truncated monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc (beta 1-->4)GlcNAc-Asn per mole of transferrin.
7944531	6	32	theme	GlcNAc-Asn	920:929	arg1	moles					801:805	two moles	797:805	two moles of truncated monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc (beta 1-->4)GlcNAc-Asn per mole of transferrin	797:953	The serum disialotransferrin, studied in the present patient, contained two moles of truncated monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc (beta 1-->4)GlcNAc-Asn per mole of transferrin.
7944531	1	33	gly	glycoprotein	150:161	arg1	glycoprotein					150:161	carbohydrate deficient glycoprotein	127:161	The carbohydrate deficient glycoprotein (CDG) syndromes	123:177	The carbohydrate deficient glycoprotein (CDG) syndromes are a family of genetic multisystemic disorders with severe nervous system involvement.
7944531	1	33	gly	glycoprotein	150:161	arg1	CDG					164:166	CDG	164:166	CDG	164:166	The carbohydrate deficient glycoprotein (CDG) syndromes are a family of genetic multisystemic disorders with severe nervous system involvement.
7944531	6	34	theme	alpha	873:877	arg1	GlcNAc					901:906	monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc	820:906	truncated monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc (beta 1-->4)GlcNAc-Asn	810:929	The serum disialotransferrin, studied in the present patient, contained two moles of truncated monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc (beta 1-->4)GlcNAc-Asn per mole of transferrin.
7944531	6	34	theme	alpha	873:877	arg1	1-->4					914:918	beta 1-->4	909:918	beta 1-->4	909:918	The serum disialotransferrin, studied in the present patient, contained two moles of truncated monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc (beta 1-->4)GlcNAc-Asn per mole of transferrin.
7944531	1	35	theme	severe	232:237	arg1	involvement					254:264	severe nervous system involvement	232:264	severe nervous system involvement	232:264	The carbohydrate deficient glycoprotein (CDG) syndromes are a family of genetic multisystemic disorders with severe nervous system involvement.
7944531	0	36	from	deficiency	56:65	arg1	N-acetyl-glucosaminyltransferase					86:117	Golgi localised N-acetyl-glucosaminyltransferase II	70:120	Golgi localised N-acetyl-glucosaminyltransferase II	70:120	Carbohydrate deficient glycoprotein syndrome type II: a deficiency in Golgi localised N-acetyl-glucosaminyltransferase II.
7944531	0	37	gly	glycoprotein	23:34	arg1	glycoprotein					23:34	Carbohydrate deficient glycoprotein syndrome type II	0:51	Carbohydrate deficient glycoprotein syndrome type II: a deficiency in Golgi localised N-acetyl-glucosaminyltransferase II.	0:121	Carbohydrate deficient glycoprotein syndrome type II: a deficiency in Golgi localised N-acetyl-glucosaminyltransferase II.
7944531	7	38	theme	Golgi	995:999	arg1	N-acetylglucosaminyltransferase					1008:1038	the Golgi enzyme N-acetylglucosaminyltransferase II	991:1041	the Golgi enzyme N-acetylglucosaminyltransferase II (EC 2.4.1.143)	991:1056	A profoundly deficient activity of the Golgi enzyme N-acetylglucosaminyltransferase II (EC 2.4.1.143) was demonstrated in fibroblasts.
7944531	7	38	theme	Golgi	995:999	arg1	EC					1044:1045	EC 2.4.1.143	1044:1055	EC 2.4.1.143	1044:1055	A profoundly deficient activity of the Golgi enzyme N-acetylglucosaminyltransferase II (EC 2.4.1.143) was demonstrated in fibroblasts.
7944531	1	39	theme	carbohydrate	127:138	arg1	glycoprotein					150:161	carbohydrate deficient glycoprotein	127:161	The carbohydrate deficient glycoprotein (CDG) syndromes	123:177	The carbohydrate deficient glycoprotein (CDG) syndromes are a family of genetic multisystemic disorders with severe nervous system involvement.
7944531	1	39	theme	carbohydrate	127:138	arg1	CDG					164:166	CDG	164:166	CDG	164:166	The carbohydrate deficient glycoprotein (CDG) syndromes are a family of genetic multisystemic disorders with severe nervous system involvement.
7944531	1	40	with	disorders	217:225	arg1	involvement					254:264	severe nervous system involvement	232:264	severe nervous system involvement	232:264	The carbohydrate deficient glycoprotein (CDG) syndromes are a family of genetic multisystemic disorders with severe nervous system involvement.
7944531	4	41	theme	severe	518:523	arg1	retardation					537:547	a more severe psychomotor retardation	511:547	a more severe psychomotor retardation but no peripheral neuropathy nor cerebellar hypoplasia	511:602	Compared with type I patients they have a more severe psychomotor retardation but no peripheral neuropathy nor cerebellar hypoplasia.
7944531	6	42	theme	[Man	868:871	arg1	GlcNAc					901:906	monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc	820:906	truncated monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc (beta 1-->4)GlcNAc-Asn	810:929	The serum disialotransferrin, studied in the present patient, contained two moles of truncated monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc (beta 1-->4)GlcNAc-Asn per mole of transferrin.
7944531	6	42	theme	[Man	868:871	arg1	1-->4					914:918	beta 1-->4	909:918	beta 1-->4	909:918	The serum disialotransferrin, studied in the present patient, contained two moles of truncated monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc (beta 1-->4)GlcNAc-Asn per mole of transferrin.
7944531	0	43	dep	type	45:48	arg1	deficiency					56:65	a deficiency	54:65	Carbohydrate deficient glycoprotein syndrome type II: a deficiency in Golgi localised N-acetyl-glucosaminyltransferase II.	0:121	Carbohydrate deficient glycoprotein syndrome type II: a deficiency in Golgi localised N-acetyl-glucosaminyltransferase II.
7944531	6	44	theme	present	770:776	arg1	patient					778:784	the present patient	766:784	the present patient	766:784	The serum disialotransferrin, studied in the present patient, contained two moles of truncated monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc (beta 1-->4)GlcNAc-Asn per mole of transferrin.
7944531	1	45	theme	deficient	140:148	arg1	glycoprotein					150:161	carbohydrate deficient glycoprotein	127:161	The carbohydrate deficient glycoprotein (CDG) syndromes	123:177	The carbohydrate deficient glycoprotein (CDG) syndromes are a family of genetic multisystemic disorders with severe nervous system involvement.
7944531	1	45	theme	deficient	140:148	arg1	CDG					164:166	CDG	164:166	CDG	164:166	The carbohydrate deficient glycoprotein (CDG) syndromes are a family of genetic multisystemic disorders with severe nervous system involvement.
7944531	6	46	theme	beta	909:912	arg1	GlcNAc					901:906	monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc	820:906	truncated monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc (beta 1-->4)GlcNAc-Asn	810:929	The serum disialotransferrin, studied in the present patient, contained two moles of truncated monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc (beta 1-->4)GlcNAc-Asn per mole of transferrin.
7944531	6	46	theme	beta	909:912	arg1	1-->4					914:918	beta 1-->4	909:918	beta 1-->4	909:918	The serum disialotransferrin, studied in the present patient, contained two moles of truncated monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc (beta 1-->4)GlcNAc-Asn per mole of transferrin.
7944531	7	47	theme	enzyme	1001:1006	arg1	N-acetylglucosaminyltransferase					1008:1038	the Golgi enzyme N-acetylglucosaminyltransferase II	991:1041	the Golgi enzyme N-acetylglucosaminyltransferase II (EC 2.4.1.143)	991:1056	A profoundly deficient activity of the Golgi enzyme N-acetylglucosaminyltransferase II (EC 2.4.1.143) was demonstrated in fibroblasts.
7944531	7	47	theme	enzyme	1001:1006	arg1	EC					1044:1045	EC 2.4.1.143	1044:1055	EC 2.4.1.143	1044:1055	A profoundly deficient activity of the Golgi enzyme N-acetylglucosaminyltransferase II (EC 2.4.1.143) was demonstrated in fibroblasts.
7944531	1	48	theme	glycoprotein	150:161	arg1	syndromes					169:177	The carbohydrate deficient glycoprotein (CDG) syndromes	123:177	The carbohydrate deficient glycoprotein (CDG) syndromes	123:177	The carbohydrate deficient glycoprotein (CDG) syndromes are a family of genetic multisystemic disorders with severe nervous system involvement.
7944531	1	48	theme	glycoprotein	150:161	arg1	family					185:190	a family	183:190	a family of genetic multisystemic disorders with severe nervous system involvement	183:264	The carbohydrate deficient glycoprotein (CDG) syndromes are a family of genetic multisystemic disorders with severe nervous system involvement.
7944531	2	49	with	child	287:291	arg1	syndrome					304:311	a CDG syndrome	298:311	a CDG syndrome that differs from the classical picture but is very similar to a patient reported in 1991	298:401	This report is on a child with a CDG syndrome that differs from the classical picture but is very similar to a patient reported in 1991.
7944531	2	49	with	child	287:291	arg1	similar					365:371	similar	365:371	similar	365:371	This report is on a child with a CDG syndrome that differs from the classical picture but is very similar to a patient reported in 1991.
7944531	5	50	theme	major	709:713	arg1	disialotransferrin					683:700	disialotransferrin	683:700	disialotransferrin	683:700	The serum transferrin isoform pattern obtained by isoelectric focusing showed disialotransferrin as the major fraction.
7944531	5	50	theme	major	709:713	arg1	fraction					715:722	the major fraction	705:722	the major fraction	705:722	The serum transferrin isoform pattern obtained by isoelectric focusing showed disialotransferrin as the major fraction.
7944531	6	51	theme	1-->3	862:866	arg1	GlcNAc					901:906	monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc	820:906	truncated monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc (beta 1-->4)GlcNAc-Asn	810:929	The serum disialotransferrin, studied in the present patient, contained two moles of truncated monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc (beta 1-->4)GlcNAc-Asn per mole of transferrin.
7944531	6	51	theme	1-->3	862:866	arg1	1-->4					914:918	beta 1-->4	909:918	beta 1-->4	909:918	The serum disialotransferrin, studied in the present patient, contained two moles of truncated monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc (beta 1-->4)GlcNAc-Asn per mole of transferrin.
7944531	1	52	theme	system	247:252	arg1	involvement					254:264	severe nervous system involvement	232:264	severe nervous system involvement	232:264	The carbohydrate deficient glycoprotein (CDG) syndromes are a family of genetic multisystemic disorders with severe nervous system involvement.
7944531	3	53	theme	CDG	449:451	arg1	type					462:465	CDG syndrome type II	449:468	CDG syndrome type II	449:468	Both these patients are therefore designated CDG syndrome type II.
7944531	3	54	theme	syndrome	453:460	arg1	type					462:465	CDG syndrome type II	449:468	CDG syndrome type II	449:468	Both these patients are therefore designated CDG syndrome type II.
7944531	6	55	theme	1-->4	895:899	arg1	GlcNAc					901:906	monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc	820:906	truncated monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc (beta 1-->4)GlcNAc-Asn	810:929	The serum disialotransferrin, studied in the present patient, contained two moles of truncated monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc (beta 1-->4)GlcNAc-Asn per mole of transferrin.
7944531	6	55	theme	1-->4	895:899	arg1	1-->4					914:918	beta 1-->4	909:918	beta 1-->4	909:918	The serum disialotransferrin, studied in the present patient, contained two moles of truncated monoantennary Sialyl-Gal-GlcNAc-Man(alpha 1-->3)[Man(alpha 1-->6)]Man(beta 1-->4)GlcNAc (beta 1-->4)GlcNAc-Asn per mole of transferrin.
7944531	4	56	theme	I	490:490	arg1	patients					492:499	type I patients	485:499	type I patients	485:499	Compared with type I patients they have a more severe psychomotor retardation but no peripheral neuropathy nor cerebellar hypoplasia.
7944531	1	57	theme	nervous	239:245	arg1	involvement					254:264	severe nervous system involvement	232:264	severe nervous system involvement	232:264	The carbohydrate deficient glycoprotein (CDG) syndromes are a family of genetic multisystemic disorders with severe nervous system involvement.
2403553	11	0	contain	contain	1642:1648	arg2	oligosaccharides					1699:1714	both complex-type and high mannose-type N-linked oligosaccharides	1650:1714	both complex-type and high mannose-type N-linked oligosaccharides	1650:1714	In addition, the receptors from all three cell lines contain both complex-type and high mannose-type N-linked oligosaccharides.
2403553	11	0	contain	contain	1642:1648	arg2	receptors					1606:1614	the receptors	1602:1614	the receptors from all three cell lines	1602:1640	In addition, the receptors from all three cell lines contain both complex-type and high mannose-type N-linked oligosaccharides.
2403553	11	0	contain	contain	1642:1648	arg1	addition					1592:1599	addition	1592:1599	addition	1592:1599	In addition, the receptors from all three cell lines contain both complex-type and high mannose-type N-linked oligosaccharides.
2403553	11	0	contain	contain	1642:1648	arg1	receptors					1606:1614	the receptors	1602:1614	the receptors from all three cell lines	1602:1640	In addition, the receptors from all three cell lines contain both complex-type and high mannose-type N-linked oligosaccharides.
2403553	13	1	theme	blood	2006:2010	arg1	antigens					2020:2027	blood group A antigens	2006:2027	blood group A antigens	2006:2027	These results are interesting since both A431 and BeWo cells, but not K562 cells, are positive for blood group A antigens.
2403553	7	2	theme	released	825:832	arg1	glycopeptides					847:859	glycopeptides	847:859	glycopeptides	847:859	The released radiolabeled glycopeptides and oligosaccharides were separated by a variety of chromatographic techniques, and their structures were analyzed.
2403553	4	3	theme	human	436:440	arg1	lines--K562					447:457	Three different human cell lines--K562	420:457	Three different human cell lines--K562	420:457	Three different human cell lines--K562, A431, and BeWo--were grown in media containing either [2-3H] mannose or [6-3H]glucosamine.
2403553	10	4	from	A431	1396:1399	arg1	oligosaccharides					1339:1354	the O-linked oligosaccharides	1326:1354	the O-linked oligosaccharides in the transferring receptors from both A431 and BeWo cell lines	1326:1419	In contrast, the O-linked oligosaccharides in the transferring receptors from both A431 and BeWo cell lines are not as highly sialylated and were identified as both the neutral disaccharide galactose-N-acetylgalactosamine and the neutral monosaccharide N-acetylgalactosamine.
2403553	10	4	from	A431	1396:1399	arg1	N-acetylgalactosamine					1566:1586	the neutral monosaccharide N-acetylgalactosamine	1539:1586	the neutral monosaccharide N-acetylgalactosamine	1539:1586	In contrast, the O-linked oligosaccharides in the transferring receptors from both A431 and BeWo cell lines are not as highly sialylated and were identified as both the neutral disaccharide galactose-N-acetylgalactosamine and the neutral monosaccharide N-acetylgalactosamine.
2403553	10	4	from	A431	1396:1399	arg1	galactose-N-acetylgalactosamine					1503:1533	the neutral disaccharide galactose-N-acetylgalactosamine	1478:1533	the neutral disaccharide galactose-N-acetylgalactosamine	1478:1533	In contrast, the O-linked oligosaccharides in the transferring receptors from both A431 and BeWo cell lines are not as highly sialylated and were identified as both the neutral disaccharide galactose-N-acetylgalactosamine and the neutral monosaccharide N-acetylgalactosamine.
2403553	10	4	from	A431	1396:1399	arg1	receptors					1376:1384	the transferring receptors	1359:1384	the transferring receptors from both A431 and BeWo cell lines	1359:1419	In contrast, the O-linked oligosaccharides in the transferring receptors from both A431 and BeWo cell lines are not as highly sialylated and were identified as both the neutral disaccharide galactose-N-acetylgalactosamine and the neutral monosaccharide N-acetylgalactosamine.
2403553	13	5	theme	K562	1977:1980	arg1	cells					1982:1986	K562 cells	1977:1986	K562 cells	1977:1986	These results are interesting since both A431 and BeWo cells, but not K562 cells, are positive for blood group A antigens.
2403553	12	6	contain	have	1773:1776	arg2	properties					1778:1787	properties	1778:1787	properties of blood group A antigens	1778:1813	The complex-type chains in the receptor from A431 cells have properties of blood group A antigens, whereas oligosaccharides in receptors from both BeWo and K562 cells lack these properties.
2403553	12	6	contain	have	1773:1776	arg1	chains					1734:1739	The complex-type chains	1717:1739	The complex-type chains in the receptor from A431 cells	1717:1771	The complex-type chains in the receptor from A431 cells have properties of blood group A antigens, whereas oligosaccharides in receptors from both BeWo and K562 cells lack these properties.
2403553	3	7	link	O-linked	393:400	arg1	oligosaccharides					402:417	these O-linked oligosaccharides	387:417	these O-linked oligosaccharides	387:417	This report describes the isolation and characterization of these O-linked oligosaccharides.
2403553	12	8	from	chains	1734:1739	arg1	receptor					1748:1755	the receptor	1744:1755	the receptor from A431 cells	1744:1771	The complex-type chains in the receptor from A431 cells have properties of blood group A antigens, whereas oligosaccharides in receptors from both BeWo and K562 cells lack these properties.
2403553	12	8	from	chains	1734:1739	arg1	cells					1767:1771	A431 cells	1762:1771	A431 cells	1762:1771	The complex-type chains in the receptor from A431 cells have properties of blood group A antigens, whereas oligosaccharides in receptors from both BeWo and K562 cells lack these properties.
2403553	10	9	from	lines	1415:1419	arg1	oligosaccharides					1339:1354	the O-linked oligosaccharides	1326:1354	the O-linked oligosaccharides in the transferring receptors from both A431 and BeWo cell lines	1326:1419	In contrast, the O-linked oligosaccharides in the transferring receptors from both A431 and BeWo cell lines are not as highly sialylated and were identified as both the neutral disaccharide galactose-N-acetylgalactosamine and the neutral monosaccharide N-acetylgalactosamine.
2403553	10	9	from	lines	1415:1419	arg1	N-acetylgalactosamine					1566:1586	the neutral monosaccharide N-acetylgalactosamine	1539:1586	the neutral monosaccharide N-acetylgalactosamine	1539:1586	In contrast, the O-linked oligosaccharides in the transferring receptors from both A431 and BeWo cell lines are not as highly sialylated and were identified as both the neutral disaccharide galactose-N-acetylgalactosamine and the neutral monosaccharide N-acetylgalactosamine.
2403553	10	9	from	lines	1415:1419	arg1	galactose-N-acetylgalactosamine					1503:1533	the neutral disaccharide galactose-N-acetylgalactosamine	1478:1533	the neutral disaccharide galactose-N-acetylgalactosamine	1478:1533	In contrast, the O-linked oligosaccharides in the transferring receptors from both A431 and BeWo cell lines are not as highly sialylated and were identified as both the neutral disaccharide galactose-N-acetylgalactosamine and the neutral monosaccharide N-acetylgalactosamine.
2403553	10	9	from	lines	1415:1419	arg1	receptors					1376:1384	the transferring receptors	1359:1384	the transferring receptors from both A431 and BeWo cell lines	1359:1419	In contrast, the O-linked oligosaccharides in the transferring receptors from both A431 and BeWo cell lines are not as highly sialylated and were identified as both the neutral disaccharide galactose-N-acetylgalactosamine and the neutral monosaccharide N-acetylgalactosamine.
2403553	5	10	theme	gel	710:712	arg1	electrophoresis					714:728	sodium dodecyl sulfate-polyacrylamide gel electrophoresis	672:728	sodium dodecyl sulfate-polyacrylamide gel electrophoresis	672:728	The newly synthesized and radiolabeled transferrin receptors were purified by immunoprecipitation from cell extracts and sodium dodecyl sulfate-polyacrylamide gel electrophoresis.
2403553	14	11	theme	transferrin	2075:2085	arg1	receptor					2087:2094	the human transferrin receptor	2065:2094	the human transferrin receptor	2065:2094	Thus, our results demonstrate that the human transferrin receptor contains O-linked oligosaccharides and that there are differences in the structures of both the O-linked and complex-type N-linked oligosaccharides on the receptors synthesized by different cell types.
2403553	12	12	theme	antigens	1806:1813	arg1	properties					1778:1787	properties	1778:1787	properties of blood group A antigens	1778:1813	The complex-type chains in the receptor from A431 cells have properties of blood group A antigens, whereas oligosaccharides in receptors from both BeWo and K562 cells lack these properties.
2403553	0	13	link	O-linked	36:43	arg1	oligosaccharides					45:60	O-linked oligosaccharides	36:60	O-linked oligosaccharides	36:60	Human transferrin receptor contains O-linked oligosaccharides.
2403553	8	14	theme	base/borohydride	1102:1117	arg1	treatment					1119:1127	mild base/borohydride treatment	1097:1127	mild base/borohydride treatment	1097:1127	The transferrin receptor from all three cell types contains O-linked oligosaccharides that are released from peptide by mild base/borohydride treatment.
2403553	2	15	link	O-linked	300:307	arg1	oligosaccharides					309:324	O-linked oligosaccharides	300:324	O-linked oligosaccharides	300:324	During our studies on the structures of the N-linked oligosaccharides of the receptor, we discovered that the receptor contains O-linked oligosaccharides.
2403553	13	16	theme	group	2012:2016	arg1	antigens					2020:2027	blood group A antigens	2006:2027	blood group A antigens	2006:2027	These results are interesting since both A431 and BeWo cells, but not K562 cells, are positive for blood group A antigens.
2403553	10	17	theme	BeWo	1405:1408	arg1	lines					1415:1419	both A431 and BeWo cell lines	1391:1419	lines	1415:1419	In contrast, the O-linked oligosaccharides in the transferring receptors from both A431 and BeWo cell lines are not as highly sialylated and were identified as both the neutral disaccharide galactose-N-acetylgalactosamine and the neutral monosaccharide N-acetylgalactosamine.
2403553	10	18	from	oligosaccharides	1339:1354	arg1	lines					1415:1419	both A431 and BeWo cell lines	1391:1419	lines	1415:1419	In contrast, the O-linked oligosaccharides in the transferring receptors from both A431 and BeWo cell lines are not as highly sialylated and were identified as both the neutral disaccharide galactose-N-acetylgalactosamine and the neutral monosaccharide N-acetylgalactosamine.
2403553	10	18	from	oligosaccharides	1339:1354	arg1	receptors					1376:1384	the transferring receptors	1359:1384	the transferring receptors from both A431 and BeWo cell lines	1359:1419	In contrast, the O-linked oligosaccharides in the transferring receptors from both A431 and BeWo cell lines are not as highly sialylated and were identified as both the neutral disaccharide galactose-N-acetylgalactosamine and the neutral monosaccharide N-acetylgalactosamine.
2403553	10	18	from	oligosaccharides	1339:1354	arg1	A431					1396:1399	both A431 and BeWo cell lines	1391:1419	A431	1396:1399	In contrast, the O-linked oligosaccharides in the transferring receptors from both A431 and BeWo cell lines are not as highly sialylated and were identified as both the neutral disaccharide galactose-N-acetylgalactosamine and the neutral monosaccharide N-acetylgalactosamine.
2403553	9	19	contain	contains	1159:1166	arg2	structure					1249:1257	a core structure	1242:1257	a core structure of the disaccharide galactose-N-acetyl-galactosamine	1242:1310	The receptor from K562 cells contains at least one O-linked oligosaccharide having two sialic acid residues and a core structure of the disaccharide galactose-N-acetyl-galactosamine.
2403553	9	19	contain	contains	1159:1166	arg1	receptor					1134:1141	The receptor	1130:1141	The receptor from K562 cells	1130:1157	The receptor from K562 cells contains at least one O-linked oligosaccharide having two sialic acid residues and a core structure of the disaccharide galactose-N-acetyl-galactosamine.
2403553	9	19	contain	contains	1159:1166	arg2	oligosaccharide					1190:1204	at least one O-linked oligosaccharide	1168:1204	at least one O-linked oligosaccharide having two sialic acid residues	1168:1236	The receptor from K562 cells contains at least one O-linked oligosaccharide having two sialic acid residues and a core structure of the disaccharide galactose-N-acetyl-galactosamine.
2403553	14	20	from	differences	2150:2160	arg1	structures					2169:2178	the structures	2165:2178	the structures of both the O-linked and complex-type N-linked oligosaccharides on the receptors synthesized by different cell types	2165:2295	Thus, our results demonstrate that the human transferrin receptor contains O-linked oligosaccharides and that there are differences in the structures of both the O-linked and complex-type N-linked oligosaccharides on the receptors synthesized by different cell types.
2403553	10	21	gly	sialylated	1439:1448	arg1	oligosaccharides					1339:1354	the O-linked oligosaccharides	1326:1354	the O-linked oligosaccharides in the transferring receptors from both A431 and BeWo cell lines	1326:1419	In contrast, the O-linked oligosaccharides in the transferring receptors from both A431 and BeWo cell lines are not as highly sialylated and were identified as both the neutral disaccharide galactose-N-acetylgalactosamine and the neutral monosaccharide N-acetylgalactosamine.
2403553	10	21	gly	sialylated	1439:1448	arg1	N-acetylgalactosamine					1566:1586	the neutral monosaccharide N-acetylgalactosamine	1539:1586	the neutral monosaccharide N-acetylgalactosamine	1539:1586	In contrast, the O-linked oligosaccharides in the transferring receptors from both A431 and BeWo cell lines are not as highly sialylated and were identified as both the neutral disaccharide galactose-N-acetylgalactosamine and the neutral monosaccharide N-acetylgalactosamine.
2403553	10	21	gly	sialylated	1439:1448	arg1	galactose-N-acetylgalactosamine					1503:1533	the neutral disaccharide galactose-N-acetylgalactosamine	1478:1533	the neutral disaccharide galactose-N-acetylgalactosamine	1478:1533	In contrast, the O-linked oligosaccharides in the transferring receptors from both A431 and BeWo cell lines are not as highly sialylated and were identified as both the neutral disaccharide galactose-N-acetylgalactosamine and the neutral monosaccharide N-acetylgalactosamine.
2403553	9	22	link	O-linked	1181:1188	arg1	oligosaccharide					1190:1204	at least one O-linked oligosaccharide	1168:1204	at least one O-linked oligosaccharide having two sialic acid residues	1168:1236	The receptor from K562 cells contains at least one O-linked oligosaccharide having two sialic acid residues and a core structure of the disaccharide galactose-N-acetyl-galactosamine.
2403553	9	23	theme	K562	1148:1151	arg1	cells					1153:1157	K562 cells	1148:1157	K562 cells	1148:1157	The receptor from K562 cells contains at least one O-linked oligosaccharide having two sialic acid residues and a core structure of the disaccharide galactose-N-acetyl-galactosamine.
2403553	9	24	contain	having	1206:1211	arg2	residues					1229:1236	two sialic acid residues	1213:1236	two sialic acid residues	1213:1236	The receptor from K562 cells contains at least one O-linked oligosaccharide having two sialic acid residues and a core structure of the disaccharide galactose-N-acetyl-galactosamine.
2403553	9	24	contain	having	1206:1211	arg1	oligosaccharide					1190:1204	at least one O-linked oligosaccharide	1168:1204	at least one O-linked oligosaccharide having two sialic acid residues	1168:1236	The receptor from K562 cells contains at least one O-linked oligosaccharide having two sialic acid residues and a core structure of the disaccharide galactose-N-acetyl-galactosamine.
2403553	2	25	theme	oligosaccharides	225:240	arg1	structures					198:207	the structures	194:207	the structures of the N-linked oligosaccharides of the receptor	194:256	During our studies on the structures of the N-linked oligosaccharides of the receptor, we discovered that the receptor contains O-linked oligosaccharides.
2403553	5	26	theme	transferrin	590:600	arg1	receptors					602:610	radiolabeled transferrin receptors	577:610	radiolabeled transferrin receptors	577:610	The newly synthesized and radiolabeled transferrin receptors were purified by immunoprecipitation from cell extracts and sodium dodecyl sulfate-polyacrylamide gel electrophoresis.
2403553	12	27	theme	group	1798:1802	arg1	antigens					1806:1813	blood group A antigens	1792:1813	blood group A antigens	1792:1813	The complex-type chains in the receptor from A431 cells have properties of blood group A antigens, whereas oligosaccharides in receptors from both BeWo and K562 cells lack these properties.
2403553	8	28	theme	mild	1097:1100	arg1	treatment					1119:1127	mild base/borohydride treatment	1097:1127	mild base/borohydride treatment	1097:1127	The transferrin receptor from all three cell types contains O-linked oligosaccharides that are released from peptide by mild base/borohydride treatment.
2403553	11	29	link	N-linked	1690:1697	arg1	oligosaccharides					1699:1714	both complex-type and high mannose-type N-linked oligosaccharides	1650:1714	both complex-type and high mannose-type N-linked oligosaccharides	1650:1714	In addition, the receptors from all three cell lines contain both complex-type and high mannose-type N-linked oligosaccharides.
2403553	12	30	from	cells	1878:1882	arg1	receptors					1844:1852	receptors	1844:1852	receptors from both BeWo and K562 cells	1844:1882	The complex-type chains in the receptor from A431 cells have properties of blood group A antigens, whereas oligosaccharides in receptors from both BeWo and K562 cells lack these properties.
2403553	12	30	from	cells	1878:1882	arg1	oligosaccharides					1824:1839	oligosaccharides	1824:1839	oligosaccharides in receptors from both BeWo and K562 cells	1824:1882	The complex-type chains in the receptor from A431 cells have properties of blood group A antigens, whereas oligosaccharides in receptors from both BeWo and K562 cells lack these properties.
2403553	1	31	theme	different	150:158	arg1	lines					165:169	three different cell lines	144:169	three different cell lines	144:169	We have investigated the oligosaccharides in the human transferrin receptor from three different cell lines.
2403553	12	32	theme	A431	1762:1765	arg1	cells					1767:1771	A431 cells	1762:1771	A431 cells	1762:1771	The complex-type chains in the receptor from A431 cells have properties of blood group A antigens, whereas oligosaccharides in receptors from both BeWo and K562 cells lack these properties.
2403553	11	33	theme	mannose-type	1677:1688	arg1	oligosaccharides					1699:1714	both complex-type and high mannose-type N-linked oligosaccharides	1650:1714	both complex-type and high mannose-type N-linked oligosaccharides	1650:1714	In addition, the receptors from all three cell lines contain both complex-type and high mannose-type N-linked oligosaccharides.
2403553	14	34	contain	contains	2096:2103	arg1	receptor					2087:2094	the human transferrin receptor	2065:2094	the human transferrin receptor	2065:2094	Thus, our results demonstrate that the human transferrin receptor contains O-linked oligosaccharides and that there are differences in the structures of both the O-linked and complex-type N-linked oligosaccharides on the receptors synthesized by different cell types.
2403553	14	34	contain	contains	2096:2103	arg2	oligosaccharides					2114:2129	O-linked oligosaccharides	2105:2129	O-linked oligosaccharides	2105:2129	Thus, our results demonstrate that the human transferrin receptor contains O-linked oligosaccharides and that there are differences in the structures of both the O-linked and complex-type N-linked oligosaccharides on the receptors synthesized by different cell types.
2403553	14	35	link	O-linked	2192:2199	arg1	oligosaccharides					2227:2242	both the O-linked and complex-type N-linked oligosaccharides	2183:2242	oligosaccharides	2227:2242	Thus, our results demonstrate that the human transferrin receptor contains O-linked oligosaccharides and that there are differences in the structures of both the O-linked and complex-type N-linked oligosaccharides on the receptors synthesized by different cell types.
2403553	9	36	theme	O-linked	1181:1188	arg1	oligosaccharide					1190:1204	at least one O-linked oligosaccharide	1168:1204	at least one O-linked oligosaccharide having two sialic acid residues	1168:1236	The receptor from K562 cells contains at least one O-linked oligosaccharide having two sialic acid residues and a core structure of the disaccharide galactose-N-acetyl-galactosamine.
2403553	8	37	link	O-linked	1037:1044	arg1	oligosaccharides					1046:1061	O-linked oligosaccharides	1037:1061	O-linked oligosaccharides that are released from peptide by mild base/borohydride treatment	1037:1127	The transferrin receptor from all three cell types contains O-linked oligosaccharides that are released from peptide by mild base/borohydride treatment.
2403553	10	38	theme	cell	1410:1413	arg1	lines					1415:1419	both A431 and BeWo cell lines	1391:1419	lines	1415:1419	In contrast, the O-linked oligosaccharides in the transferring receptors from both A431 and BeWo cell lines are not as highly sialylated and were identified as both the neutral disaccharide galactose-N-acetylgalactosamine and the neutral monosaccharide N-acetylgalactosamine.
2403553	14	39	theme	complex-type	2205:2216	arg1	oligosaccharides					2227:2242	both the O-linked and complex-type N-linked oligosaccharides	2183:2242	oligosaccharides	2227:2242	Thus, our results demonstrate that the human transferrin receptor contains O-linked oligosaccharides and that there are differences in the structures of both the O-linked and complex-type N-linked oligosaccharides on the receptors synthesized by different cell types.
2403553	9	40	theme	sialic	1217:1222	arg1	residues					1229:1236	two sialic acid residues	1213:1236	two sialic acid residues	1213:1236	The receptor from K562 cells contains at least one O-linked oligosaccharide having two sialic acid residues and a core structure of the disaccharide galactose-N-acetyl-galactosamine.
2403553	14	41	theme	O-linked	2192:2199	arg1	oligosaccharides					2227:2242	both the O-linked and complex-type N-linked oligosaccharides	2183:2242	oligosaccharides	2227:2242	Thus, our results demonstrate that the human transferrin receptor contains O-linked oligosaccharides and that there are differences in the structures of both the O-linked and complex-type N-linked oligosaccharides on the receptors synthesized by different cell types.
2403553	0	42	theme	Human	0:4	arg1	receptor					18:25	Human transferrin receptor	0:25	Human transferrin receptor	0:25	Human transferrin receptor contains O-linked oligosaccharides.
2403553	7	43	theme	chromatographic	913:927	arg1	techniques					929:938	chromatographic techniques	913:938	chromatographic techniques	913:938	The released radiolabeled glycopeptides and oligosaccharides were separated by a variety of chromatographic techniques, and their structures were analyzed.
2403553	8	44	theme	cell	1017:1020	arg1	types					1022:1026	all three cell types	1007:1026	all three cell types	1007:1026	The transferrin receptor from all three cell types contains O-linked oligosaccharides that are released from peptide by mild base/borohydride treatment.
2403553	3	45	theme	oligosaccharides	402:417	arg1	isolation					353:361	isolation	353:361	isolation	353:361	This report describes the isolation and characterization of these O-linked oligosaccharides.
2403553	3	45	theme	oligosaccharides	402:417	arg1	characterization					367:382	characterization	367:382	characterization	367:382	This report describes the isolation and characterization of these O-linked oligosaccharides.
2403553	14	46	theme	cell	2286:2289	arg1	types					2291:2295	different cell types	2276:2295	different cell types	2276:2295	Thus, our results demonstrate that the human transferrin receptor contains O-linked oligosaccharides and that there are differences in the structures of both the O-linked and complex-type N-linked oligosaccharides on the receptors synthesized by different cell types.
2403553	9	47	from	cells	1153:1157	arg1	receptor					1134:1141	The receptor	1130:1141	The receptor from K562 cells	1130:1157	The receptor from K562 cells contains at least one O-linked oligosaccharide having two sialic acid residues and a core structure of the disaccharide galactose-N-acetyl-galactosamine.
2403553	13	48	theme	A	2018:2018	arg1	antigens					2020:2027	blood group A antigens	2006:2027	blood group A antigens	2006:2027	These results are interesting since both A431 and BeWo cells, but not K562 cells, are positive for blood group A antigens.
2403553	2	49	contain	contains	291:298	arg1	receptor					282:289	the receptor	278:289	the receptor	278:289	During our studies on the structures of the N-linked oligosaccharides of the receptor, we discovered that the receptor contains O-linked oligosaccharides.
2403553	2	49	contain	contains	291:298	arg2	oligosaccharides					309:324	O-linked oligosaccharides	300:324	O-linked oligosaccharides	300:324	During our studies on the structures of the N-linked oligosaccharides of the receptor, we discovered that the receptor contains O-linked oligosaccharides.
2403553	1	50	theme	transferrin	118:128	arg1	receptor					130:137	the human transferrin receptor	108:137	the human transferrin receptor	108:137	We have investigated the oligosaccharides in the human transferrin receptor from three different cell lines.
2403553	1	51	theme	cell	160:163	arg1	lines					165:169	three different cell lines	144:169	three different cell lines	144:169	We have investigated the oligosaccharides in the human transferrin receptor from three different cell lines.
2403553	2	52	link	N-linked	216:223	arg1	oligosaccharides					225:240	the N-linked oligosaccharides	212:240	the N-linked oligosaccharides of the receptor	212:256	During our studies on the structures of the N-linked oligosaccharides of the receptor, we discovered that the receptor contains O-linked oligosaccharides.
2403553	0	53	theme	O-linked	36:43	arg1	oligosaccharides					45:60	O-linked oligosaccharides	36:60	O-linked oligosaccharides	36:60	Human transferrin receptor contains O-linked oligosaccharides.
2403553	10	54	theme	disaccharide	1490:1501	arg1	oligosaccharides					1339:1354	the O-linked oligosaccharides	1326:1354	the O-linked oligosaccharides in the transferring receptors from both A431 and BeWo cell lines	1326:1419	In contrast, the O-linked oligosaccharides in the transferring receptors from both A431 and BeWo cell lines are not as highly sialylated and were identified as both the neutral disaccharide galactose-N-acetylgalactosamine and the neutral monosaccharide N-acetylgalactosamine.
2403553	10	54	theme	disaccharide	1490:1501	arg1	galactose-N-acetylgalactosamine					1503:1533	the neutral disaccharide galactose-N-acetylgalactosamine	1478:1533	the neutral disaccharide galactose-N-acetylgalactosamine	1478:1533	In contrast, the O-linked oligosaccharides in the transferring receptors from both A431 and BeWo cell lines are not as highly sialylated and were identified as both the neutral disaccharide galactose-N-acetylgalactosamine and the neutral monosaccharide N-acetylgalactosamine.
2403553	12	55	dep	have	1773:1776	arg1	whereas					1816:1822	whereas	1816:1822	whereas	1816:1822	The complex-type chains in the receptor from A431 cells have properties of blood group A antigens, whereas oligosaccharides in receptors from both BeWo and K562 cells lack these properties.
2403553	9	56	theme	galactose-N-acetyl-galactosamine	1279:1310	arg1	oligosaccharide					1190:1204	at least one O-linked oligosaccharide	1168:1204	at least one O-linked oligosaccharide having two sialic acid residues	1168:1236	The receptor from K562 cells contains at least one O-linked oligosaccharide having two sialic acid residues and a core structure of the disaccharide galactose-N-acetyl-galactosamine.
2403553	9	56	theme	galactose-N-acetyl-galactosamine	1279:1310	arg1	structure					1249:1257	a core structure	1242:1257	a core structure of the disaccharide galactose-N-acetyl-galactosamine	1242:1310	The receptor from K562 cells contains at least one O-linked oligosaccharide having two sialic acid residues and a core structure of the disaccharide galactose-N-acetyl-galactosamine.
2403553	14	57	from	receptors	2251:2259	arg1	structures					2169:2178	the structures	2165:2178	the structures of both the O-linked and complex-type N-linked oligosaccharides on the receptors synthesized by different cell types	2165:2295	Thus, our results demonstrate that the human transferrin receptor contains O-linked oligosaccharides and that there are differences in the structures of both the O-linked and complex-type N-linked oligosaccharides on the receptors synthesized by different cell types.
2403553	10	58	theme	neutral	1543:1549	arg1	oligosaccharides					1339:1354	the O-linked oligosaccharides	1326:1354	the O-linked oligosaccharides in the transferring receptors from both A431 and BeWo cell lines	1326:1419	In contrast, the O-linked oligosaccharides in the transferring receptors from both A431 and BeWo cell lines are not as highly sialylated and were identified as both the neutral disaccharide galactose-N-acetylgalactosamine and the neutral monosaccharide N-acetylgalactosamine.
2403553	10	58	theme	neutral	1543:1549	arg1	N-acetylgalactosamine					1566:1586	the neutral monosaccharide N-acetylgalactosamine	1539:1586	the neutral monosaccharide N-acetylgalactosamine	1539:1586	In contrast, the O-linked oligosaccharides in the transferring receptors from both A431 and BeWo cell lines are not as highly sialylated and were identified as both the neutral disaccharide galactose-N-acetylgalactosamine and the neutral monosaccharide N-acetylgalactosamine.
2403553	10	59	theme	O-linked	1330:1337	arg1	oligosaccharides					1339:1354	the O-linked oligosaccharides	1326:1354	the O-linked oligosaccharides in the transferring receptors from both A431 and BeWo cell lines	1326:1419	In contrast, the O-linked oligosaccharides in the transferring receptors from both A431 and BeWo cell lines are not as highly sialylated and were identified as both the neutral disaccharide galactose-N-acetylgalactosamine and the neutral monosaccharide N-acetylgalactosamine.
2403553	10	59	theme	O-linked	1330:1337	arg1	N-acetylgalactosamine					1566:1586	the neutral monosaccharide N-acetylgalactosamine	1539:1586	the neutral monosaccharide N-acetylgalactosamine	1539:1586	In contrast, the O-linked oligosaccharides in the transferring receptors from both A431 and BeWo cell lines are not as highly sialylated and were identified as both the neutral disaccharide galactose-N-acetylgalactosamine and the neutral monosaccharide N-acetylgalactosamine.
2403553	10	59	theme	O-linked	1330:1337	arg1	galactose-N-acetylgalactosamine					1503:1533	the neutral disaccharide galactose-N-acetylgalactosamine	1478:1533	the neutral disaccharide galactose-N-acetylgalactosamine	1478:1533	In contrast, the O-linked oligosaccharides in the transferring receptors from both A431 and BeWo cell lines are not as highly sialylated and were identified as both the neutral disaccharide galactose-N-acetylgalactosamine and the neutral monosaccharide N-acetylgalactosamine.
2403553	11	60	from	lines	1636:1640	arg1	receptors					1606:1614	the receptors	1602:1614	the receptors from all three cell lines	1602:1640	In addition, the receptors from all three cell lines contain both complex-type and high mannose-type N-linked oligosaccharides.
2403553	8	61	contain	contains	1028:1035	arg1	receptor					993:1000	The transferrin receptor	977:1000	The transferrin receptor from all three cell types	977:1026	The transferrin receptor from all three cell types contains O-linked oligosaccharides that are released from peptide by mild base/borohydride treatment.
2403553	8	61	contain	contains	1028:1035	arg2	oligosaccharides					1046:1061	O-linked oligosaccharides	1037:1061	O-linked oligosaccharides that are released from peptide by mild base/borohydride treatment	1037:1127	The transferrin receptor from all three cell types contains O-linked oligosaccharides that are released from peptide by mild base/borohydride treatment.
2403553	1	62	from	oligosaccharides	88:103	arg1	receptor					130:137	the human transferrin receptor	108:137	the human transferrin receptor	108:137	We have investigated the oligosaccharides in the human transferrin receptor from three different cell lines.
2403553	4	63	theme	cell	442:445	arg1	lines--K562					447:457	Three different human cell lines--K562	420:457	Three different human cell lines--K562	420:457	Three different human cell lines--K562, A431, and BeWo--were grown in media containing either [2-3H] mannose or [6-3H]glucosamine.
2403553	2	64	theme	O-linked	300:307	arg1	oligosaccharides					309:324	O-linked oligosaccharides	300:324	O-linked oligosaccharides	300:324	During our studies on the structures of the N-linked oligosaccharides of the receptor, we discovered that the receptor contains O-linked oligosaccharides.
2403553	10	65	theme	transferring	1363:1374	arg1	receptors					1376:1384	the transferring receptors	1359:1384	the transferring receptors from both A431 and BeWo cell lines	1359:1419	In contrast, the O-linked oligosaccharides in the transferring receptors from both A431 and BeWo cell lines are not as highly sialylated and were identified as both the neutral disaccharide galactose-N-acetylgalactosamine and the neutral monosaccharide N-acetylgalactosamine.
2403553	14	66	theme	O-linked	2105:2112	arg1	oligosaccharides					2114:2129	O-linked oligosaccharides	2105:2129	O-linked oligosaccharides	2105:2129	Thus, our results demonstrate that the human transferrin receptor contains O-linked oligosaccharides and that there are differences in the structures of both the O-linked and complex-type N-linked oligosaccharides on the receptors synthesized by different cell types.
2403553	13	67	theme	BeWo	1957:1960	arg1	cells					1962:1966	BeWo cells	1957:1966	BeWo cells	1957:1966	These results are interesting since both A431 and BeWo cells, but not K562 cells, are positive for blood group A antigens.
2403553	5	68	theme	sulfate-polyacrylamide	687:708	arg1	electrophoresis					714:728	sodium dodecyl sulfate-polyacrylamide gel electrophoresis	672:728	sodium dodecyl sulfate-polyacrylamide gel electrophoresis	672:728	The newly synthesized and radiolabeled transferrin receptors were purified by immunoprecipitation from cell extracts and sodium dodecyl sulfate-polyacrylamide gel electrophoresis.
2403553	0	69	contain	contains	27:34	arg1	receptor					18:25	Human transferrin receptor	0:25	Human transferrin receptor	0:25	Human transferrin receptor contains O-linked oligosaccharides.
2403553	0	69	contain	contains	27:34	arg2	oligosaccharides					45:60	O-linked oligosaccharides	36:60	O-linked oligosaccharides	36:60	Human transferrin receptor contains O-linked oligosaccharides.
2403553	4	70	theme	different	426:434	arg1	lines--K562					447:457	Three different human cell lines--K562	420:457	Three different human cell lines--K562	420:457	Three different human cell lines--K562, A431, and BeWo--were grown in media containing either [2-3H] mannose or [6-3H]glucosamine.
2403553	14	71	theme	human	2069:2073	arg1	receptor					2087:2094	the human transferrin receptor	2065:2094	the human transferrin receptor	2065:2094	Thus, our results demonstrate that the human transferrin receptor contains O-linked oligosaccharides and that there are differences in the structures of both the O-linked and complex-type N-linked oligosaccharides on the receptors synthesized by different cell types.
2403553	9	72	theme	disaccharide	1266:1277	arg1	galactose-N-acetyl-galactosamine					1279:1310	the disaccharide galactose-N-acetyl-galactosamine	1262:1310	the disaccharide galactose-N-acetyl-galactosamine	1262:1310	The receptor from K562 cells contains at least one O-linked oligosaccharide having two sialic acid residues and a core structure of the disaccharide galactose-N-acetyl-galactosamine.
2403553	2	73	theme	receptor	249:256	arg1	oligosaccharides					225:240	the N-linked oligosaccharides	212:240	the N-linked oligosaccharides of the receptor	212:256	During our studies on the structures of the N-linked oligosaccharides of the receptor, we discovered that the receptor contains O-linked oligosaccharides.
2403553	8	74	attach	released	1072:1079	arg1	peptide					1086:1092	peptide	1086:1092	peptide	1086:1092	The transferrin receptor from all three cell types contains O-linked oligosaccharides that are released from peptide by mild base/borohydride treatment.
2403553	8	74	attach	released	1072:1079	arg2	oligosaccharides					1046:1061	O-linked oligosaccharides	1037:1061	O-linked oligosaccharides that are released from peptide by mild base/borohydride treatment	1037:1127	The transferrin receptor from all three cell types contains O-linked oligosaccharides that are released from peptide by mild base/borohydride treatment.
2403553	5	75	theme	radiolabeled	577:588	arg1	receptors					602:610	radiolabeled transferrin receptors	577:610	radiolabeled transferrin receptors	577:610	The newly synthesized and radiolabeled transferrin receptors were purified by immunoprecipitation from cell extracts and sodium dodecyl sulfate-polyacrylamide gel electrophoresis.
2403553	12	76	theme	A	1804:1804	arg1	antigens					1806:1813	blood group A antigens	1792:1813	blood group A antigens	1792:1813	The complex-type chains in the receptor from A431 cells have properties of blood group A antigens, whereas oligosaccharides in receptors from both BeWo and K562 cells lack these properties.
2403553	11	77	theme	N-linked	1690:1697	arg1	oligosaccharides					1699:1714	both complex-type and high mannose-type N-linked oligosaccharides	1650:1714	both complex-type and high mannose-type N-linked oligosaccharides	1650:1714	In addition, the receptors from all three cell lines contain both complex-type and high mannose-type N-linked oligosaccharides.
2403553	8	78	from	types	1022:1026	arg1	receptor					993:1000	The transferrin receptor	977:1000	The transferrin receptor from all three cell types	977:1026	The transferrin receptor from all three cell types contains O-linked oligosaccharides that are released from peptide by mild base/borohydride treatment.
2403553	11	79	theme	high	1672:1675	arg1	oligosaccharides					1699:1714	both complex-type and high mannose-type N-linked oligosaccharides	1650:1714	both complex-type and high mannose-type N-linked oligosaccharides	1650:1714	In addition, the receptors from all three cell lines contain both complex-type and high mannose-type N-linked oligosaccharides.
2403553	5	80	from	extracts	659:666	arg1	immunoprecipitation					629:647	immunoprecipitation	629:647	immunoprecipitation from cell extracts	629:666	The newly synthesized and radiolabeled transferrin receptors were purified by immunoprecipitation from cell extracts and sodium dodecyl sulfate-polyacrylamide gel electrophoresis.
2403553	5	80	from	extracts	659:666	arg1	electrophoresis					714:728	sodium dodecyl sulfate-polyacrylamide gel electrophoresis	672:728	sodium dodecyl sulfate-polyacrylamide gel electrophoresis	672:728	The newly synthesized and radiolabeled transferrin receptors were purified by immunoprecipitation from cell extracts and sodium dodecyl sulfate-polyacrylamide gel electrophoresis.
2403553	14	81	dep	oligosaccharides	2227:2242	arg1	both					2183:2186	both	2183:2186	both	2183:2186	Thus, our results demonstrate that the human transferrin receptor contains O-linked oligosaccharides and that there are differences in the structures of both the O-linked and complex-type N-linked oligosaccharides on the receptors synthesized by different cell types.
2403553	14	82	link	N-linked	2218:2225	arg1	oligosaccharides					2227:2242	both the O-linked and complex-type N-linked oligosaccharides	2183:2242	oligosaccharides	2227:2242	Thus, our results demonstrate that the human transferrin receptor contains O-linked oligosaccharides and that there are differences in the structures of both the O-linked and complex-type N-linked oligosaccharides on the receptors synthesized by different cell types.
2403553	12	83	from	cells	1767:1771	arg1	receptor					1748:1755	the receptor	1744:1755	the receptor from A431 cells	1744:1771	The complex-type chains in the receptor from A431 cells have properties of blood group A antigens, whereas oligosaccharides in receptors from both BeWo and K562 cells lack these properties.
2403553	12	83	from	cells	1767:1771	arg1	chains					1734:1739	The complex-type chains	1717:1739	The complex-type chains in the receptor from A431 cells	1717:1771	The complex-type chains in the receptor from A431 cells have properties of blood group A antigens, whereas oligosaccharides in receptors from both BeWo and K562 cells lack these properties.
2403553	5	84	theme	cell	654:657	arg1	extracts					659:666	cell extracts	654:666	cell extracts	654:666	The newly synthesized and radiolabeled transferrin receptors were purified by immunoprecipitation from cell extracts and sodium dodecyl sulfate-polyacrylamide gel electrophoresis.
2403553	14	85	theme	N-linked	2218:2225	arg1	oligosaccharides					2227:2242	both the O-linked and complex-type N-linked oligosaccharides	2183:2242	oligosaccharides	2227:2242	Thus, our results demonstrate that the human transferrin receptor contains O-linked oligosaccharides and that there are differences in the structures of both the O-linked and complex-type N-linked oligosaccharides on the receptors synthesized by different cell types.
2403553	3	86	theme	O-linked	393:400	arg1	oligosaccharides					402:417	these O-linked oligosaccharides	387:417	these O-linked oligosaccharides	387:417	This report describes the isolation and characterization of these O-linked oligosaccharides.
2403553	6	87	theme	mild	798:801	arg1	base/borohydride					803:818	mild base/borohydride	798:818	mild base/borohydride	798:818	The receptor was proteolytically digested or treated directly with mild base/borohydride.
2403553	11	88	theme	cell	1631:1634	arg1	lines					1636:1640	all three cell lines	1621:1640	all three cell lines	1621:1640	In addition, the receptors from all three cell lines contain both complex-type and high mannose-type N-linked oligosaccharides.
2403553	1	89	from	lines	165:169	arg1	oligosaccharides					88:103	the oligosaccharides	84:103	the oligosaccharides in the human transferrin receptor from three different cell lines	84:169	We have investigated the oligosaccharides in the human transferrin receptor from three different cell lines.
2403553	8	90	theme	transferrin	981:991	arg1	receptor					993:1000	The transferrin receptor	977:1000	The transferrin receptor from all three cell types	977:1026	The transferrin receptor from all three cell types contains O-linked oligosaccharides that are released from peptide by mild base/borohydride treatment.
2403553	9	91	theme	acid	1224:1227	arg1	residues					1229:1236	two sialic acid residues	1213:1236	two sialic acid residues	1213:1236	The receptor from K562 cells contains at least one O-linked oligosaccharide having two sialic acid residues and a core structure of the disaccharide galactose-N-acetyl-galactosamine.
2403553	0	92	theme	transferrin	6:16	arg1	receptor					18:25	Human transferrin receptor	0:25	Human transferrin receptor	0:25	Human transferrin receptor contains O-linked oligosaccharides.
2403553	14	93	from	structures	2169:2178	arg1	receptors					2251:2259	the receptors	2247:2259	the receptors synthesized by different cell types	2247:2295	Thus, our results demonstrate that the human transferrin receptor contains O-linked oligosaccharides and that there are differences in the structures of both the O-linked and complex-type N-linked oligosaccharides on the receptors synthesized by different cell types.
2403553	12	94	theme	K562	1873:1876	arg1	cells					1878:1882	both BeWo and K562 cells	1859:1882	cells	1878:1882	The complex-type chains in the receptor from A431 cells have properties of blood group A antigens, whereas oligosaccharides in receptors from both BeWo and K562 cells lack these properties.
2403553	7	95	gly	glycopeptides	847:859	arg2	glycopeptides					847:859	glycopeptides	847:859	glycopeptides	847:859	The released radiolabeled glycopeptides and oligosaccharides were separated by a variety of chromatographic techniques, and their structures were analyzed.
2403553	11	96	theme	complex-type	1655:1666	arg1	oligosaccharides					1699:1714	both complex-type and high mannose-type N-linked oligosaccharides	1650:1714	both complex-type and high mannose-type N-linked oligosaccharides	1650:1714	In addition, the receptors from all three cell lines contain both complex-type and high mannose-type N-linked oligosaccharides.
2403553	7	97	theme	techniques	929:938	arg1	variety					902:908	a variety	900:908	a variety of chromatographic techniques	900:938	The released radiolabeled glycopeptides and oligosaccharides were separated by a variety of chromatographic techniques, and their structures were analyzed.
2403553	7	97	theme	techniques	929:938	arg1	techniques					929:938	chromatographic techniques	913:938	chromatographic techniques	913:938	The released radiolabeled glycopeptides and oligosaccharides were separated by a variety of chromatographic techniques, and their structures were analyzed.
2403553	12	98	from	oligosaccharides	1824:1839	arg1	receptors					1844:1852	receptors	1844:1852	receptors from both BeWo and K562 cells	1844:1882	The complex-type chains in the receptor from A431 cells have properties of blood group A antigens, whereas oligosaccharides in receptors from both BeWo and K562 cells lack these properties.
2403553	12	98	from	oligosaccharides	1824:1839	arg1	cells					1878:1882	both BeWo and K562 cells	1859:1882	cells	1878:1882	The complex-type chains in the receptor from A431 cells have properties of blood group A antigens, whereas oligosaccharides in receptors from both BeWo and K562 cells lack these properties.
2403553	1	99	theme	human	112:116	arg1	receptor					130:137	the human transferrin receptor	108:137	the human transferrin receptor	108:137	We have investigated the oligosaccharides in the human transferrin receptor from three different cell lines.
2403553	14	100	theme	different	2276:2284	arg1	types					2291:2295	different cell types	2276:2295	different cell types	2276:2295	Thus, our results demonstrate that the human transferrin receptor contains O-linked oligosaccharides and that there are differences in the structures of both the O-linked and complex-type N-linked oligosaccharides on the receptors synthesized by different cell types.
2403553	9	101	theme	core	1244:1247	arg1	structure					1249:1257	a core structure	1242:1257	a core structure of the disaccharide galactose-N-acetyl-galactosamine	1242:1310	The receptor from K562 cells contains at least one O-linked oligosaccharide having two sialic acid residues and a core structure of the disaccharide galactose-N-acetyl-galactosamine.
2403553	4	102	contain	containing	496:505	arg2	glucosamine					538:548	glucosamine	538:548	glucosamine	538:548	Three different human cell lines--K562, A431, and BeWo--were grown in media containing either [2-3H] mannose or [6-3H]glucosamine.
2403553	4	102	contain	containing	496:505	arg2	mannose					521:527	mannose	521:527	mannose	521:527	Three different human cell lines--K562, A431, and BeWo--were grown in media containing either [2-3H] mannose or [6-3H]glucosamine.
2403553	4	102	contain	containing	496:505	arg1	media					490:494	media	490:494	media containing either [2-3H] mannose or [6-3H]glucosamine	490:548	Three different human cell lines--K562, A431, and BeWo--were grown in media containing either [2-3H] mannose or [6-3H]glucosamine.
2403553	12	103	theme	BeWo	1864:1867	arg1	cells					1878:1882	both BeWo and K562 cells	1859:1882	cells	1878:1882	The complex-type chains in the receptor from A431 cells have properties of blood group A antigens, whereas oligosaccharides in receptors from both BeWo and K562 cells lack these properties.
2403553	10	104	link	O-linked	1330:1337	arg1	oligosaccharides					1339:1354	the O-linked oligosaccharides	1326:1354	the O-linked oligosaccharides in the transferring receptors from both A431 and BeWo cell lines	1326:1419	In contrast, the O-linked oligosaccharides in the transferring receptors from both A431 and BeWo cell lines are not as highly sialylated and were identified as both the neutral disaccharide galactose-N-acetylgalactosamine and the neutral monosaccharide N-acetylgalactosamine.
2403553	10	104	link	O-linked	1330:1337	arg1	N-acetylgalactosamine					1566:1586	the neutral monosaccharide N-acetylgalactosamine	1539:1586	the neutral monosaccharide N-acetylgalactosamine	1539:1586	In contrast, the O-linked oligosaccharides in the transferring receptors from both A431 and BeWo cell lines are not as highly sialylated and were identified as both the neutral disaccharide galactose-N-acetylgalactosamine and the neutral monosaccharide N-acetylgalactosamine.
2403553	10	104	link	O-linked	1330:1337	arg1	galactose-N-acetylgalactosamine					1503:1533	the neutral disaccharide galactose-N-acetylgalactosamine	1478:1533	the neutral disaccharide galactose-N-acetylgalactosamine	1478:1533	In contrast, the O-linked oligosaccharides in the transferring receptors from both A431 and BeWo cell lines are not as highly sialylated and were identified as both the neutral disaccharide galactose-N-acetylgalactosamine and the neutral monosaccharide N-acetylgalactosamine.
2403553	7	105	theme	radiolabeled	834:845	arg1	glycopeptides					847:859	glycopeptides	847:859	glycopeptides	847:859	The released radiolabeled glycopeptides and oligosaccharides were separated by a variety of chromatographic techniques, and their structures were analyzed.
2403553	12	106	theme	blood	1792:1796	arg1	antigens					1806:1813	blood group A antigens	1792:1813	blood group A antigens	1792:1813	The complex-type chains in the receptor from A431 cells have properties of blood group A antigens, whereas oligosaccharides in receptors from both BeWo and K562 cells lack these properties.
2403553	12	107	theme	complex-type	1721:1732	arg1	chains					1734:1739	The complex-type chains	1717:1739	The complex-type chains in the receptor from A431 cells	1717:1771	The complex-type chains in the receptor from A431 cells have properties of blood group A antigens, whereas oligosaccharides in receptors from both BeWo and K562 cells lack these properties.
2403553	8	108	theme	O-linked	1037:1044	arg1	oligosaccharides					1046:1061	O-linked oligosaccharides	1037:1061	O-linked oligosaccharides that are released from peptide by mild base/borohydride treatment	1037:1127	The transferrin receptor from all three cell types contains O-linked oligosaccharides that are released from peptide by mild base/borohydride treatment.
2403553	2	109	theme	N-linked	216:223	arg1	oligosaccharides					225:240	the N-linked oligosaccharides	212:240	the N-linked oligosaccharides of the receptor	212:256	During our studies on the structures of the N-linked oligosaccharides of the receptor, we discovered that the receptor contains O-linked oligosaccharides.
2403553	10	110	theme	neutral	1482:1488	arg1	oligosaccharides					1339:1354	the O-linked oligosaccharides	1326:1354	the O-linked oligosaccharides in the transferring receptors from both A431 and BeWo cell lines	1326:1419	In contrast, the O-linked oligosaccharides in the transferring receptors from both A431 and BeWo cell lines are not as highly sialylated and were identified as both the neutral disaccharide galactose-N-acetylgalactosamine and the neutral monosaccharide N-acetylgalactosamine.
2403553	10	110	theme	neutral	1482:1488	arg1	galactose-N-acetylgalactosamine					1503:1533	the neutral disaccharide galactose-N-acetylgalactosamine	1478:1533	the neutral disaccharide galactose-N-acetylgalactosamine	1478:1533	In contrast, the O-linked oligosaccharides in the transferring receptors from both A431 and BeWo cell lines are not as highly sialylated and were identified as both the neutral disaccharide galactose-N-acetylgalactosamine and the neutral monosaccharide N-acetylgalactosamine.
2403553	14	111	from	oligosaccharides	2227:2242	arg1	receptors					2251:2259	the receptors	2247:2259	the receptors synthesized by different cell types	2247:2295	Thus, our results demonstrate that the human transferrin receptor contains O-linked oligosaccharides and that there are differences in the structures of both the O-linked and complex-type N-linked oligosaccharides on the receptors synthesized by different cell types.
2403553	14	112	theme	oligosaccharides	2227:2242	arg1	structures					2169:2178	the structures	2165:2178	the structures of both the O-linked and complex-type N-linked oligosaccharides on the receptors synthesized by different cell types	2165:2295	Thus, our results demonstrate that the human transferrin receptor contains O-linked oligosaccharides and that there are differences in the structures of both the O-linked and complex-type N-linked oligosaccharides on the receptors synthesized by different cell types.
2403553	10	113	theme	monosaccharide	1551:1564	arg1	oligosaccharides					1339:1354	the O-linked oligosaccharides	1326:1354	the O-linked oligosaccharides in the transferring receptors from both A431 and BeWo cell lines	1326:1419	In contrast, the O-linked oligosaccharides in the transferring receptors from both A431 and BeWo cell lines are not as highly sialylated and were identified as both the neutral disaccharide galactose-N-acetylgalactosamine and the neutral monosaccharide N-acetylgalactosamine.
2403553	10	113	theme	monosaccharide	1551:1564	arg1	N-acetylgalactosamine					1566:1586	the neutral monosaccharide N-acetylgalactosamine	1539:1586	the neutral monosaccharide N-acetylgalactosamine	1539:1586	In contrast, the O-linked oligosaccharides in the transferring receptors from both A431 and BeWo cell lines are not as highly sialylated and were identified as both the neutral disaccharide galactose-N-acetylgalactosamine and the neutral monosaccharide N-acetylgalactosamine.
2403553	2	114	from	studies	183:189	arg1	structures					198:207	the structures	194:207	the structures of the N-linked oligosaccharides of the receptor	194:256	During our studies on the structures of the N-linked oligosaccharides of the receptor, we discovered that the receptor contains O-linked oligosaccharides.
2403553	14	115	link	O-linked	2105:2112	arg1	oligosaccharides					2114:2129	O-linked oligosaccharides	2105:2129	O-linked oligosaccharides	2105:2129	Thus, our results demonstrate that the human transferrin receptor contains O-linked oligosaccharides and that there are differences in the structures of both the O-linked and complex-type N-linked oligosaccharides on the receptors synthesized by different cell types.
1694784	0	0	theme	protein	83:89	arg1	HC					91:92	human protein HC	77:92	human protein HC	77:92	Location and characterization of the three carbohydrate prosthetic groups of human protein HC.
1694784	6	1	theme	Q3	806:807	arg1	compositions					783:794	The sugar compositions	773:794	The sugar compositions of Q2 and Q3 oligosaccharides	773:824	The sugar compositions of Q2 and Q3 oligosaccharides are compatible with that of the complex kind.
1694784	6	1	theme	Q3	806:807	arg1	compatible					830:839	compatible	830:839	compatible	830:839	The sugar compositions of Q2 and Q3 oligosaccharides are compatible with that of the complex kind.
1694784	3	2	attach	N-linkages	463:472	arg2	residues					490:497	asparagine residues	479:497	asparagine residues at positions 17 and 96	479:520	The second and third carbohydrate prosthetic groups form N-linkages with asparagine residues at positions 17 and 96.
1694784	3	2	attach	N-linkages	463:472	arg1	groups					451:456	The second and third carbohydrate prosthetic groups	406:456	The second and third carbohydrate prosthetic groups	406:456	The second and third carbohydrate prosthetic groups form N-linkages with asparagine residues at positions 17 and 96.
1694784	1	3	theme	chymotryptic	162:173	arg1	Q3					196:197	Q3	196:197	Q3	196:197	Three different carbohydrate prosthetic groups associated to three chymotryptic peptides, Q1, Q2 and Q3, were isolated from the reduced and carboxymethylated human protein HC.
1694784	1	3	theme	chymotryptic	162:173	arg1	Q2					189:190	Q2	189:190	Q2	189:190	Three different carbohydrate prosthetic groups associated to three chymotryptic peptides, Q1, Q2 and Q3, were isolated from the reduced and carboxymethylated human protein HC.
1694784	1	3	theme	chymotryptic	162:173	arg1	Q1					185:186	Q1	185:186	Q1	185:186	Three different carbohydrate prosthetic groups associated to three chymotryptic peptides, Q1, Q2 and Q3, were isolated from the reduced and carboxymethylated human protein HC.
1694784	1	3	theme	chymotryptic	162:173	arg1	peptides					175:182	three chymotryptic peptides	156:182	three chymotryptic peptides	156:182	Three different carbohydrate prosthetic groups associated to three chymotryptic peptides, Q1, Q2 and Q3, were isolated from the reduced and carboxymethylated human protein HC.
1694784	0	4	theme	human	77:81	arg1	HC					91:92	human protein HC	77:92	human protein HC	77:92	Location and characterization of the three carbohydrate prosthetic groups of human protein HC.
1694784	6	5	with	compatible	830:839	arg1	that					846:849	that	846:849	that	846:849	The sugar compositions of Q2 and Q3 oligosaccharides are compatible with that of the complex kind.
1694784	1	6	theme	carboxymethylated	235:251	arg1	HC					267:268	the reduced and carboxymethylated human protein HC	219:268	the reduced and carboxymethylated human protein HC	219:268	Three different carbohydrate prosthetic groups associated to three chymotryptic peptides, Q1, Q2 and Q3, were isolated from the reduced and carboxymethylated human protein HC.
1694784	6	7	theme	Q2	799:800	arg1	compositions					783:794	The sugar compositions	773:794	The sugar compositions of Q2 and Q3 oligosaccharides	773:824	The sugar compositions of Q2 and Q3 oligosaccharides are compatible with that of the complex kind.
1694784	6	7	theme	Q2	799:800	arg1	compatible					830:839	compatible	830:839	compatible	830:839	The sugar compositions of Q2 and Q3 oligosaccharides are compatible with that of the complex kind.
1694784	3	8	from	positions	502:510	arg1	residues					490:497	asparagine residues	479:497	asparagine residues at positions 17 and 96	479:520	The second and third carbohydrate prosthetic groups form N-linkages with asparagine residues at positions 17 and 96.
1694784	2	9	theme	first	275:279	arg1	oligosaccharide					281:295	The first oligosaccharide	271:295	The first oligosaccharide	271:295	The first oligosaccharide forms an O-glycosidic linkage with a threonine residue at position 5 in the polypeptide chain of protein HC.
1694784	4	10	attach	present	540:546	arg1	Q1					551:552	Q1	551:552	Q1	551:552	Oligosaccharides present in Q1 contain 1 residue of NANA, 2 of GalNAc and 1 of Gal corresponding to the following structure: -O-GalNAc-GalNAc-Gal-NANA.
1694784	4	10	attach	present	540:546	arg2	Oligosaccharides					523:538	Oligosaccharides	523:538	Oligosaccharides present in Q1	523:552	Oligosaccharides present in Q1 contain 1 residue of NANA, 2 of GalNAc and 1 of Gal corresponding to the following structure: -O-GalNAc-GalNAc-Gal-NANA.
1694784	1	11	theme	human	253:257	arg1	HC					267:268	the reduced and carboxymethylated human protein HC	219:268	the reduced and carboxymethylated human protein HC	219:268	Three different carbohydrate prosthetic groups associated to three chymotryptic peptides, Q1, Q2 and Q3, were isolated from the reduced and carboxymethylated human protein HC.
1694784	0	12	theme	HC	91:92	arg1	groups					67:72	the three carbohydrate prosthetic groups	33:72	the three carbohydrate prosthetic groups of human protein HC	33:92	Location and characterization of the three carbohydrate prosthetic groups of human protein HC.
1694784	0	12	theme	HC	91:92	arg1	HC					91:92	human protein HC	77:92	human protein HC	77:92	Location and characterization of the three carbohydrate prosthetic groups of human protein HC.
1694784	1	13	theme	protein	259:265	arg1	HC					267:268	the reduced and carboxymethylated human protein HC	219:268	the reduced and carboxymethylated human protein HC	219:268	Three different carbohydrate prosthetic groups associated to three chymotryptic peptides, Q1, Q2 and Q3, were isolated from the reduced and carboxymethylated human protein HC.
1694784	7	14	attach	present	903:909	arg1	Q3					925:926	Q3	925:926	Q3	925:926	The amount of oligosaccharides present in Q1, Q2 and Q3 corresponded respectively to 3.0%, 12.2% and 7.3% of the weight of protein HC.
1694784	7	14	attach	present	903:909	arg2	oligosaccharides					886:901	oligosaccharides	886:901	oligosaccharides present in Q1, Q2 and Q3	886:926	The amount of oligosaccharides present in Q1, Q2 and Q3 corresponded respectively to 3.0%, 12.2% and 7.3% of the weight of protein HC.
1694784	7	14	attach	present	903:909	arg1	Q2					918:919	Q2	918:919	Q2	918:919	The amount of oligosaccharides present in Q1, Q2 and Q3 corresponded respectively to 3.0%, 12.2% and 7.3% of the weight of protein HC.
1694784	7	14	attach	present	903:909	arg1	Q1					914:915	Q1	914:915	Q1	914:915	The amount of oligosaccharides present in Q1, Q2 and Q3 corresponded respectively to 3.0%, 12.2% and 7.3% of the weight of protein HC.
1694784	2	15	theme	threonine	334:342	arg1	residue					344:350	a threonine residue	332:350	a threonine residue at position 5 in the polypeptide chain of protein HC	332:403	The first oligosaccharide forms an O-glycosidic linkage with a threonine residue at position 5 in the polypeptide chain of protein HC.
1694784	7	16	from	present	903:909	arg1	Q3					925:926	Q3	925:926	Q3	925:926	The amount of oligosaccharides present in Q1, Q2 and Q3 corresponded respectively to 3.0%, 12.2% and 7.3% of the weight of protein HC.
1694784	7	16	from	present	903:909	arg1	Q2					918:919	Q2	918:919	Q2	918:919	The amount of oligosaccharides present in Q1, Q2 and Q3 corresponded respectively to 3.0%, 12.2% and 7.3% of the weight of protein HC.
1694784	7	16	from	present	903:909	arg1	Q1					914:915	Q1	914:915	Q1	914:915	The amount of oligosaccharides present in Q1, Q2 and Q3 corresponded respectively to 3.0%, 12.2% and 7.3% of the weight of protein HC.
1694784	8	17	theme	plasma	1083:1088	arg1	HC					1098:1099	urinary and plasma protein HC	1071:1099	HC	1098:1099	No difference was found between the carbohydrate composition of urinary and plasma protein HC.
1694784	4	18	theme	NANA	575:578	arg1	NANA					575:578	NANA	575:578	NANA	575:578	Oligosaccharides present in Q1 contain 1 residue of NANA, 2 of GalNAc and 1 of Gal corresponding to the following structure: -O-GalNAc-GalNAc-Gal-NANA.
1694784	4	18	theme	NANA	575:578	arg1	residue					564:570	1 residue	562:570	1 residue of NANA	562:578	Oligosaccharides present in Q1 contain 1 residue of NANA, 2 of GalNAc and 1 of Gal corresponding to the following structure: -O-GalNAc-GalNAc-Gal-NANA.
1694784	2	19	attach	linkage	319:325	arg2	residue					344:350	a threonine residue	332:350	a threonine residue at position 5 in the polypeptide chain of protein HC	332:403	The first oligosaccharide forms an O-glycosidic linkage with a threonine residue at position 5 in the polypeptide chain of protein HC.
1694784	2	19	attach	linkage	319:325	arg1	oligosaccharide					281:295	The first oligosaccharide	271:295	The first oligosaccharide	271:295	The first oligosaccharide forms an O-glycosidic linkage with a threonine residue at position 5 in the polypeptide chain of protein HC.
1694784	3	20	theme	asparagine	479:488	arg1	residues					490:497	asparagine residues	479:497	asparagine residues at positions 17 and 96	479:520	The second and third carbohydrate prosthetic groups form N-linkages with asparagine residues at positions 17 and 96.
1694784	2	21	theme	polypeptide	373:383	arg1	chain					385:389	the polypeptide chain	369:389	the polypeptide chain of protein HC	369:403	The first oligosaccharide forms an O-glycosidic linkage with a threonine residue at position 5 in the polypeptide chain of protein HC.
1694784	2	22	from	residue	344:350	arg1	chain					385:389	the polypeptide chain	369:389	the polypeptide chain of protein HC	369:403	The first oligosaccharide forms an O-glycosidic linkage with a threonine residue at position 5 in the polypeptide chain of protein HC.
1694784	2	23	theme	O-glycosidic	306:317	arg1	linkage					319:325	an O-glycosidic linkage	303:325	an O-glycosidic linkage with a threonine residue at position 5 in the polypeptide chain of protein HC	303:403	The first oligosaccharide forms an O-glycosidic linkage with a threonine residue at position 5 in the polypeptide chain of protein HC.
1694784	8	24	theme	HC	1098:1099	arg1	composition					1056:1066	the carbohydrate composition	1039:1066	the carbohydrate composition of urinary and plasma protein HC	1039:1099	No difference was found between the carbohydrate composition of urinary and plasma protein HC.
1694784	3	25	theme	second	410:415	arg1	groups					451:456	The second and third carbohydrate prosthetic groups	406:456	The second and third carbohydrate prosthetic groups	406:456	The second and third carbohydrate prosthetic groups form N-linkages with asparagine residues at positions 17 and 96.
1694784	4	26	from	Q1	551:552	arg1	present					540:546	present	540:546	present	540:546	Oligosaccharides present in Q1 contain 1 residue of NANA, 2 of GalNAc and 1 of Gal corresponding to the following structure: -O-GalNAc-GalNAc-Gal-NANA.
1694784	6	27	theme	complex	858:864	arg1	kind					866:869	the complex kind	854:869	the complex kind	854:869	The sugar compositions of Q2 and Q3 oligosaccharides are compatible with that of the complex kind.
1694784	2	28	from	position	355:362	arg1	residue					344:350	a threonine residue	332:350	a threonine residue at position 5 in the polypeptide chain of protein HC	332:403	The first oligosaccharide forms an O-glycosidic linkage with a threonine residue at position 5 in the polypeptide chain of protein HC.
1694784	7	29	from	Q3	925:926	arg1	present					903:909	present	903:909	present	903:909	The amount of oligosaccharides present in Q1, Q2 and Q3 corresponded respectively to 3.0%, 12.2% and 7.3% of the weight of protein HC.
1694784	1	30	theme	different	101:109	arg1	groups					135:140	Three different carbohydrate prosthetic groups	95:140	Three different carbohydrate prosthetic groups associated to three chymotryptic peptides, Q1, Q2 and Q3,	95:198	Three different carbohydrate prosthetic groups associated to three chymotryptic peptides, Q1, Q2 and Q3, were isolated from the reduced and carboxymethylated human protein HC.
1694784	2	31	theme	HC	402:403	arg1	chain					385:389	the polypeptide chain	369:389	the polypeptide chain of protein HC	369:403	The first oligosaccharide forms an O-glycosidic linkage with a threonine residue at position 5 in the polypeptide chain of protein HC.
1694784	4	32	from	present	540:546	arg1	Q1					551:552	Q1	551:552	Q1	551:552	Oligosaccharides present in Q1 contain 1 residue of NANA, 2 of GalNAc and 1 of Gal corresponding to the following structure: -O-GalNAc-GalNAc-Gal-NANA.
1694784	5	33	contain	contains	678:685	arg2	Man					717:719	9 GlcNAc, 2 Gal and 3 Man	695:719	Man	717:719	Q2 contains 3 NANA, 9 GlcNAc, 2 Gal and 3 Man, and Q3 contains 2 NANA, 5 GlcNAc, 1 Gal and 2 Man.
1694784	5	33	contain	contains	678:685	arg2	NANA					689:692	3 NANA	687:692	3 NANA	687:692	Q2 contains 3 NANA, 9 GlcNAc, 2 Gal and 3 Man, and Q3 contains 2 NANA, 5 GlcNAc, 1 Gal and 2 Man.
1694784	5	33	contain	contains	678:685	arg1	Q2					675:676	Q2	675:676	Q2	675:676	Q2 contains 3 NANA, 9 GlcNAc, 2 Gal and 3 Man, and Q3 contains 2 NANA, 5 GlcNAc, 1 Gal and 2 Man.
1694784	5	33	contain	contains	678:685	arg2	Gal					707:709	9 GlcNAc, 2 Gal and 3 Man	695:719	Gal	707:709	Q2 contains 3 NANA, 9 GlcNAc, 2 Gal and 3 Man, and Q3 contains 2 NANA, 5 GlcNAc, 1 Gal and 2 Man.
1694784	2	34	with	linkage	319:325	arg1	residue					344:350	a threonine residue	332:350	a threonine residue at position 5 in the polypeptide chain of protein HC	332:403	The first oligosaccharide forms an O-glycosidic linkage with a threonine residue at position 5 in the polypeptide chain of protein HC.
1694784	4	35	theme	following	627:635	arg1	structure					637:645	the following structure	623:645	the following structure: -O-GalNAc-GalNAc-Gal-NANA	623:672	Oligosaccharides present in Q1 contain 1 residue of NANA, 2 of GalNAc and 1 of Gal corresponding to the following structure: -O-GalNAc-GalNAc-Gal-NANA.
1694784	2	36	theme	protein	394:400	arg1	HC					402:403	protein HC	394:403	protein HC	394:403	The first oligosaccharide forms an O-glycosidic linkage with a threonine residue at position 5 in the polypeptide chain of protein HC.
1694784	7	37	theme	protein	995:1001	arg1	weight					985:990	the weight	981:990	the weight of protein HC	981:1004	The amount of oligosaccharides present in Q1, Q2 and Q3 corresponded respectively to 3.0%, 12.2% and 7.3% of the weight of protein HC.
1694784	6	38	dep	Q2	799:800	arg1	oligosaccharides					809:824	oligosaccharides	809:824	oligosaccharides	809:824	The sugar compositions of Q2 and Q3 oligosaccharides are compatible with that of the complex kind.
1694784	5	39	theme	GlcNAc	697:702	arg1	NANA					689:692	3 NANA	687:692	3 NANA	687:692	Q2 contains 3 NANA, 9 GlcNAc, 2 Gal and 3 Man, and Q3 contains 2 NANA, 5 GlcNAc, 1 Gal and 2 Man.
1694784	5	39	theme	GlcNAc	697:702	arg1	Gal					707:709	9 GlcNAc, 2 Gal and 3 Man	695:719	Gal	707:709	Q2 contains 3 NANA, 9 GlcNAc, 2 Gal and 3 Man, and Q3 contains 2 NANA, 5 GlcNAc, 1 Gal and 2 Man.
1694784	1	40	attach	isolated	205:212	arg1	HC					267:268	the reduced and carboxymethylated human protein HC	219:268	the reduced and carboxymethylated human protein HC	219:268	Three different carbohydrate prosthetic groups associated to three chymotryptic peptides, Q1, Q2 and Q3, were isolated from the reduced and carboxymethylated human protein HC.
1694784	1	40	attach	isolated	205:212	arg2	groups					135:140	Three different carbohydrate prosthetic groups	95:140	Three different carbohydrate prosthetic groups associated to three chymotryptic peptides, Q1, Q2 and Q3,	95:198	Three different carbohydrate prosthetic groups associated to three chymotryptic peptides, Q1, Q2 and Q3, were isolated from the reduced and carboxymethylated human protein HC.
1694784	3	41	theme	prosthetic	440:449	arg1	groups					451:456	The second and third carbohydrate prosthetic groups	406:456	The second and third carbohydrate prosthetic groups	406:456	The second and third carbohydrate prosthetic groups form N-linkages with asparagine residues at positions 17 and 96.
1694784	0	42	theme	prosthetic	56:65	arg1	groups					67:72	the three carbohydrate prosthetic groups	33:72	the three carbohydrate prosthetic groups of human protein HC	33:92	Location and characterization of the three carbohydrate prosthetic groups of human protein HC.
1694784	0	42	theme	prosthetic	56:65	arg1	HC					91:92	human protein HC	77:92	human protein HC	77:92	Location and characterization of the three carbohydrate prosthetic groups of human protein HC.
1694784	8	43	theme	carbohydrate	1043:1054	arg1	composition					1056:1066	the carbohydrate composition	1039:1066	the carbohydrate composition of urinary and plasma protein HC	1039:1099	No difference was found between the carbohydrate composition of urinary and plasma protein HC.
1694784	8	44	theme	protein	1090:1096	arg1	HC					1098:1099	urinary and plasma protein HC	1071:1099	HC	1098:1099	No difference was found between the carbohydrate composition of urinary and plasma protein HC.
1694784	6	45	theme	sugar	777:781	arg1	compositions					783:794	The sugar compositions	773:794	The sugar compositions of Q2 and Q3 oligosaccharides	773:824	The sugar compositions of Q2 and Q3 oligosaccharides are compatible with that of the complex kind.
1694784	6	45	theme	sugar	777:781	arg1	compatible					830:839	compatible	830:839	compatible	830:839	The sugar compositions of Q2 and Q3 oligosaccharides are compatible with that of the complex kind.
1694784	1	46	theme	carbohydrate	111:122	arg1	groups					135:140	Three different carbohydrate prosthetic groups	95:140	Three different carbohydrate prosthetic groups associated to three chymotryptic peptides, Q1, Q2 and Q3,	95:198	Three different carbohydrate prosthetic groups associated to three chymotryptic peptides, Q1, Q2 and Q3, were isolated from the reduced and carboxymethylated human protein HC.
1694784	0	47	theme	carbohydrate	43:54	arg1	groups					67:72	the three carbohydrate prosthetic groups	33:72	the three carbohydrate prosthetic groups of human protein HC	33:92	Location and characterization of the three carbohydrate prosthetic groups of human protein HC.
1694784	0	47	theme	carbohydrate	43:54	arg1	HC					91:92	human protein HC	77:92	human protein HC	77:92	Location and characterization of the three carbohydrate prosthetic groups of human protein HC.
1694784	4	48	theme	present	540:546	arg1	Oligosaccharides					523:538	Oligosaccharides	523:538	Oligosaccharides present in Q1	523:552	Oligosaccharides present in Q1 contain 1 residue of NANA, 2 of GalNAc and 1 of Gal corresponding to the following structure: -O-GalNAc-GalNAc-Gal-NANA.
1694784	5	49	contain	contains	729:736	arg1	Q3					726:727	Q3	726:727	Q3	726:727	Q2 contains 3 NANA, 9 GlcNAc, 2 Gal and 3 Man, and Q3 contains 2 NANA, 5 GlcNAc, 1 Gal and 2 Man.
1694784	5	49	contain	contains	729:736	arg2	GlcNAc					748:753	5 GlcNAc	746:753	5 GlcNAc	746:753	Q2 contains 3 NANA, 9 GlcNAc, 2 Gal and 3 Man, and Q3 contains 2 NANA, 5 GlcNAc, 1 Gal and 2 Man.
1694784	5	49	contain	contains	729:736	arg2	NANA					740:743	2 NANA	738:743	2 NANA	738:743	Q2 contains 3 NANA, 9 GlcNAc, 2 Gal and 3 Man, and Q3 contains 2 NANA, 5 GlcNAc, 1 Gal and 2 Man.
1694784	5	49	contain	contains	729:736	arg2	Man					768:770	2 Man	766:770	2 Man	766:770	Q2 contains 3 NANA, 9 GlcNAc, 2 Gal and 3 Man, and Q3 contains 2 NANA, 5 GlcNAc, 1 Gal and 2 Man.
1694784	5	49	contain	contains	729:736	arg2	Gal					758:760	1 Gal	756:760	1 Gal	756:760	Q2 contains 3 NANA, 9 GlcNAc, 2 Gal and 3 Man, and Q3 contains 2 NANA, 5 GlcNAc, 1 Gal and 2 Man.
1694784	7	50	theme	oligosaccharides	886:901	arg1	amount					876:881	The amount	872:881	The amount of oligosaccharides present in Q1, Q2 and Q3	872:926	The amount of oligosaccharides present in Q1, Q2 and Q3 corresponded respectively to 3.0%, 12.2% and 7.3% of the weight of protein HC.
1694784	7	50	theme	oligosaccharides	886:901	arg1	oligosaccharides					886:901	oligosaccharides	886:901	oligosaccharides present in Q1, Q2 and Q3	886:926	The amount of oligosaccharides present in Q1, Q2 and Q3 corresponded respectively to 3.0%, 12.2% and 7.3% of the weight of protein HC.
1694784	1	51	theme	prosthetic	124:133	arg1	groups					135:140	Three different carbohydrate prosthetic groups	95:140	Three different carbohydrate prosthetic groups associated to three chymotryptic peptides, Q1, Q2 and Q3,	95:198	Three different carbohydrate prosthetic groups associated to three chymotryptic peptides, Q1, Q2 and Q3, were isolated from the reduced and carboxymethylated human protein HC.
1694784	7	52	theme	weight	985:990	arg1	%					960:960	3.0%	957:960	3.0%	957:960	The amount of oligosaccharides present in Q1, Q2 and Q3 corresponded respectively to 3.0%, 12.2% and 7.3% of the weight of protein HC.
1694784	7	52	theme	weight	985:990	arg1	%					967:967	12.2%	963:967	12.2%	963:967	The amount of oligosaccharides present in Q1, Q2 and Q3 corresponded respectively to 3.0%, 12.2% and 7.3% of the weight of protein HC.
1694784	7	52	theme	weight	985:990	arg1	%					976:976	7.3%	973:976	7.3%	973:976	The amount of oligosaccharides present in Q1, Q2 and Q3 corresponded respectively to 3.0%, 12.2% and 7.3% of the weight of protein HC.
1694784	7	52	theme	weight	985:990	arg1	weight					985:990	the weight	981:990	the weight of protein HC	981:1004	The amount of oligosaccharides present in Q1, Q2 and Q3 corresponded respectively to 3.0%, 12.2% and 7.3% of the weight of protein HC.
1694784	4	53	dep	structure	637:645	arg1	-O-GalNAc-GalNAc-Gal-NANA					648:672	-O-GalNAc-GalNAc-Gal-NANA	648:672	the following structure: -O-GalNAc-GalNAc-Gal-NANA	623:672	Oligosaccharides present in Q1 contain 1 residue of NANA, 2 of GalNAc and 1 of Gal corresponding to the following structure: -O-GalNAc-GalNAc-Gal-NANA.
1694784	7	54	theme	present	903:909	arg1	oligosaccharides					886:901	oligosaccharides	886:901	oligosaccharides present in Q1, Q2 and Q3	886:926	The amount of oligosaccharides present in Q1, Q2 and Q3 corresponded respectively to 3.0%, 12.2% and 7.3% of the weight of protein HC.
1694784	8	55	theme	urinary	1071:1077	arg1	HC					1098:1099	urinary and plasma protein HC	1071:1099	HC	1098:1099	No difference was found between the carbohydrate composition of urinary and plasma protein HC.
1694784	7	56	from	Q2	918:919	arg1	present					903:909	present	903:909	present	903:909	The amount of oligosaccharides present in Q1, Q2 and Q3 corresponded respectively to 3.0%, 12.2% and 7.3% of the weight of protein HC.
1694784	4	57	theme	Gal	602:604	arg1	Gal					602:604	Gal	602:604	Gal	602:604	Oligosaccharides present in Q1 contain 1 residue of NANA, 2 of GalNAc and 1 of Gal corresponding to the following structure: -O-GalNAc-GalNAc-Gal-NANA.
1694784	4	57	theme	Gal	602:604	arg1	GalNAc					586:591	GalNAc	586:591	GalNAc	586:591	Oligosaccharides present in Q1 contain 1 residue of NANA, 2 of GalNAc and 1 of Gal corresponding to the following structure: -O-GalNAc-GalNAc-Gal-NANA.
1694784	4	57	theme	Gal	602:604	arg1	2					581:581	2	581:581	2	581:581	Oligosaccharides present in Q1 contain 1 residue of NANA, 2 of GalNAc and 1 of Gal corresponding to the following structure: -O-GalNAc-GalNAc-Gal-NANA.
1694784	3	58	theme	carbohydrate	427:438	arg1	groups					451:456	The second and third carbohydrate prosthetic groups	406:456	The second and third carbohydrate prosthetic groups	406:456	The second and third carbohydrate prosthetic groups form N-linkages with asparagine residues at positions 17 and 96.
1694784	3	59	theme	third	421:425	arg1	groups					451:456	The second and third carbohydrate prosthetic groups	406:456	The second and third carbohydrate prosthetic groups	406:456	The second and third carbohydrate prosthetic groups form N-linkages with asparagine residues at positions 17 and 96.
1694784	0	60	theme	groups	67:72	arg1	characterization					13:28	characterization	13:28	characterization	13:28	Location and characterization of the three carbohydrate prosthetic groups of human protein HC.
1694784	0	60	theme	groups	67:72	arg1	Location					0:7	Location	0:7	Location	0:7	Location and characterization of the three carbohydrate prosthetic groups of human protein HC.
1694784	7	61	from	Q1	914:915	arg1	present					903:909	present	903:909	present	903:909	The amount of oligosaccharides present in Q1, Q2 and Q3 corresponded respectively to 3.0%, 12.2% and 7.3% of the weight of protein HC.
1694784	4	62	theme	GalNAc	586:591	arg1	Gal					602:604	Gal	602:604	Gal	602:604	Oligosaccharides present in Q1 contain 1 residue of NANA, 2 of GalNAc and 1 of Gal corresponding to the following structure: -O-GalNAc-GalNAc-Gal-NANA.
1694784	4	62	theme	GalNAc	586:591	arg1	GalNAc					586:591	GalNAc	586:591	GalNAc	586:591	Oligosaccharides present in Q1 contain 1 residue of NANA, 2 of GalNAc and 1 of Gal corresponding to the following structure: -O-GalNAc-GalNAc-Gal-NANA.
1694784	4	62	theme	GalNAc	586:591	arg1	2					581:581	2	581:581	2	581:581	Oligosaccharides present in Q1 contain 1 residue of NANA, 2 of GalNAc and 1 of Gal corresponding to the following structure: -O-GalNAc-GalNAc-Gal-NANA.
1694784	4	63	contain	contain	554:560	arg1	Oligosaccharides					523:538	Oligosaccharides	523:538	Oligosaccharides present in Q1	523:552	Oligosaccharides present in Q1 contain 1 residue of NANA, 2 of GalNAc and 1 of Gal corresponding to the following structure: -O-GalNAc-GalNAc-Gal-NANA.
1694784	4	63	contain	contain	554:560	arg2	residue					564:570	1 residue	562:570	1 residue of NANA	562:578	Oligosaccharides present in Q1 contain 1 residue of NANA, 2 of GalNAc and 1 of Gal corresponding to the following structure: -O-GalNAc-GalNAc-Gal-NANA.
1694784	4	63	contain	contain	554:560	arg2	NANA					575:578	NANA	575:578	NANA	575:578	Oligosaccharides present in Q1 contain 1 residue of NANA, 2 of GalNAc and 1 of Gal corresponding to the following structure: -O-GalNAc-GalNAc-Gal-NANA.
1694784	1	64	theme	reduced	223:229	arg1	HC					267:268	the reduced and carboxymethylated human protein HC	219:268	the reduced and carboxymethylated human protein HC	219:268	Three different carbohydrate prosthetic groups associated to three chymotryptic peptides, Q1, Q2 and Q3, were isolated from the reduced and carboxymethylated human protein HC.
6406478	2	0	link	Ser/Thr-linked	332:345	arg1	oligosaccharides					358:373	Ser/Thr-linked (O-linked) oligosaccharides	332:373	Ser/Thr-linked (O-linked) oligosaccharides	332:373	Ser/Thr-linked (O-linked) oligosaccharides were released by alkaline borohydride treatment, and fractionated by high performance liquid chromatography with an anion-exchange resin.
6406478	3	1	theme	major	532:536	arg1	alditol					554:560	a major oligosaccharide alditol	530:560	a major oligosaccharide alditol separated by high performance liquid chromatography	530:612	The structure of a major oligosaccharide alditol separated by high performance liquid chromatography was investigated by a combination of compositional analyses, methylation and glycosidase treatments, and proposed to be a hexasaccharide alditol, NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6(NeuAc alpha 2-3Gal beta 1-3) N-acetylgalactosaminitol.
6406478	3	2	theme	NeuAc	760:764	arg1	2-3Gal					772:777	NeuAc alpha 2-3Gal	760:777	NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6(NeuAc alpha 2-3Gal beta 1-3)	760:830	The structure of a major oligosaccharide alditol separated by high performance liquid chromatography was investigated by a combination of compositional analyses, methylation and glycosidase treatments, and proposed to be a hexasaccharide alditol, NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6(NeuAc alpha 2-3Gal beta 1-3) N-acetylgalactosaminitol.
6406478	3	3	theme	hexasaccharide	736:749	arg1	N-acetylgalactosaminitol					832:855	a hexasaccharide alditol, NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6(NeuAc alpha 2-3Gal beta 1-3) N-acetylgalactosaminitol	734:855	N-acetylgalactosaminitol	832:855	The structure of a major oligosaccharide alditol separated by high performance liquid chromatography was investigated by a combination of compositional analyses, methylation and glycosidase treatments, and proposed to be a hexasaccharide alditol, NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6(NeuAc alpha 2-3Gal beta 1-3) N-acetylgalactosaminitol.
6406478	3	3	theme	hexasaccharide	736:749	arg1	structure					517:525	The structure	513:525	The structure of a major oligosaccharide alditol separated by high performance liquid chromatography	513:612	The structure of a major oligosaccharide alditol separated by high performance liquid chromatography was investigated by a combination of compositional analyses, methylation and glycosidase treatments, and proposed to be a hexasaccharide alditol, NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6(NeuAc alpha 2-3Gal beta 1-3) N-acetylgalactosaminitol.
6406478	3	4	theme	oligosaccharide	538:552	arg1	alditol					554:560	a major oligosaccharide alditol	530:560	a major oligosaccharide alditol separated by high performance liquid chromatography	530:612	The structure of a major oligosaccharide alditol separated by high performance liquid chromatography was investigated by a combination of compositional analyses, methylation and glycosidase treatments, and proposed to be a hexasaccharide alditol, NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6(NeuAc alpha 2-3Gal beta 1-3) N-acetylgalactosaminitol.
6406478	2	5	link	O-linked	348:355	arg1	oligosaccharides					358:373	Ser/Thr-linked (O-linked) oligosaccharides	332:373	Ser/Thr-linked (O-linked) oligosaccharides	332:373	Ser/Thr-linked (O-linked) oligosaccharides were released by alkaline borohydride treatment, and fractionated by high performance liquid chromatography with an anion-exchange resin.
6406478	3	6	theme	performance	580:590	arg1	chromatography					599:612	high performance liquid chromatography	575:612	high performance liquid chromatography	575:612	The structure of a major oligosaccharide alditol separated by high performance liquid chromatography was investigated by a combination of compositional analyses, methylation and glycosidase treatments, and proposed to be a hexasaccharide alditol, NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6(NeuAc alpha 2-3Gal beta 1-3) N-acetylgalactosaminitol.
6406478	1	7	gly	glycoprotein	84:95	arg1	Glycocalicin					56:67	Glycocalicin	56:67	Glycocalicin	56:67	Glycocalicin, a predominant glycoprotein on the human platelet surface, has been purified from a platelet suspension by sonication, ammonium sulfate precipitation and acid treatment followed by chromatography on columns of wheat germ agglutinin-Sepharose and Sephacryl S-300.
6406478	1	7	gly	glycoprotein	84:95	arg1	glycoprotein					84:95	a predominant glycoprotein	70:95	a predominant glycoprotein on the human platelet surface	70:125	Glycocalicin, a predominant glycoprotein on the human platelet surface, has been purified from a platelet suspension by sonication, ammonium sulfate precipitation and acid treatment followed by chromatography on columns of wheat germ agglutinin-Sepharose and Sephacryl S-300.
6406478	3	8	theme	beta	779:782	arg1	beta					794:797	NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6	760:801	NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6(NeuAc alpha 2-3Gal beta 1-3)	760:830	The structure of a major oligosaccharide alditol separated by high performance liquid chromatography was investigated by a combination of compositional analyses, methylation and glycosidase treatments, and proposed to be a hexasaccharide alditol, NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6(NeuAc alpha 2-3Gal beta 1-3) N-acetylgalactosaminitol.
6406478	3	8	theme	beta	779:782	arg1	beta					822:825	NeuAc alpha 2-3Gal beta 1-3	803:829	NeuAc alpha 2-3Gal beta 1-3	803:829	The structure of a major oligosaccharide alditol separated by high performance liquid chromatography was investigated by a combination of compositional analyses, methylation and glycosidase treatments, and proposed to be a hexasaccharide alditol, NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6(NeuAc alpha 2-3Gal beta 1-3) N-acetylgalactosaminitol.
6406478	3	9	theme	liquid	592:597	arg1	chromatography					599:612	high performance liquid chromatography	575:612	high performance liquid chromatography	575:612	The structure of a major oligosaccharide alditol separated by high performance liquid chromatography was investigated by a combination of compositional analyses, methylation and glycosidase treatments, and proposed to be a hexasaccharide alditol, NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6(NeuAc alpha 2-3Gal beta 1-3) N-acetylgalactosaminitol.
6406478	3	10	theme	1-4GlcNAc	784:792	arg1	beta					794:797	NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6	760:801	NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6(NeuAc alpha 2-3Gal beta 1-3)	760:830	The structure of a major oligosaccharide alditol separated by high performance liquid chromatography was investigated by a combination of compositional analyses, methylation and glycosidase treatments, and proposed to be a hexasaccharide alditol, NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6(NeuAc alpha 2-3Gal beta 1-3) N-acetylgalactosaminitol.
6406478	3	10	theme	1-4GlcNAc	784:792	arg1	beta					822:825	NeuAc alpha 2-3Gal beta 1-3	803:829	NeuAc alpha 2-3Gal beta 1-3	803:829	The structure of a major oligosaccharide alditol separated by high performance liquid chromatography was investigated by a combination of compositional analyses, methylation and glycosidase treatments, and proposed to be a hexasaccharide alditol, NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6(NeuAc alpha 2-3Gal beta 1-3) N-acetylgalactosaminitol.
6406478	1	11	theme	platelet	153:160	arg1	suspension					162:171	a platelet suspension	151:171	a platelet suspension	151:171	Glycocalicin, a predominant glycoprotein on the human platelet surface, has been purified from a platelet suspension by sonication, ammonium sulfate precipitation and acid treatment followed by chromatography on columns of wheat germ agglutinin-Sepharose and Sephacryl S-300.
6406478	3	12	theme	alpha	766:770	arg1	2-3Gal					772:777	NeuAc alpha 2-3Gal	760:777	NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6(NeuAc alpha 2-3Gal beta 1-3)	760:830	The structure of a major oligosaccharide alditol separated by high performance liquid chromatography was investigated by a combination of compositional analyses, methylation and glycosidase treatments, and proposed to be a hexasaccharide alditol, NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6(NeuAc alpha 2-3Gal beta 1-3) N-acetylgalactosaminitol.
6406478	1	13	theme	predominant	72:82	arg1	Glycocalicin					56:67	Glycocalicin	56:67	Glycocalicin	56:67	Glycocalicin, a predominant glycoprotein on the human platelet surface, has been purified from a platelet suspension by sonication, ammonium sulfate precipitation and acid treatment followed by chromatography on columns of wheat germ agglutinin-Sepharose and Sephacryl S-300.
6406478	1	13	theme	predominant	72:82	arg1	glycoprotein					84:95	a predominant glycoprotein	70:95	a predominant glycoprotein on the human platelet surface	70:125	Glycocalicin, a predominant glycoprotein on the human platelet surface, has been purified from a platelet suspension by sonication, ammonium sulfate precipitation and acid treatment followed by chromatography on columns of wheat germ agglutinin-Sepharose and Sephacryl S-300.
6406478	3	14	theme	alpha	809:813	arg1	beta					794:797	NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6	760:801	NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6(NeuAc alpha 2-3Gal beta 1-3)	760:830	The structure of a major oligosaccharide alditol separated by high performance liquid chromatography was investigated by a combination of compositional analyses, methylation and glycosidase treatments, and proposed to be a hexasaccharide alditol, NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6(NeuAc alpha 2-3Gal beta 1-3) N-acetylgalactosaminitol.
6406478	3	14	theme	alpha	809:813	arg1	beta					822:825	NeuAc alpha 2-3Gal beta 1-3	803:829	NeuAc alpha 2-3Gal beta 1-3	803:829	The structure of a major oligosaccharide alditol separated by high performance liquid chromatography was investigated by a combination of compositional analyses, methylation and glycosidase treatments, and proposed to be a hexasaccharide alditol, NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6(NeuAc alpha 2-3Gal beta 1-3) N-acetylgalactosaminitol.
6406478	0	15	theme	carbohydrate	4:15	arg1	moiety					17:22	The carbohydrate moiety	0:22	The carbohydrate moiety of human platelet glycocalicin	0:53	The carbohydrate moiety of human platelet glycocalicin.
6406478	3	16	theme	2-3Gal	772:777	arg1	beta					794:797	NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6	760:801	NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6(NeuAc alpha 2-3Gal beta 1-3)	760:830	The structure of a major oligosaccharide alditol separated by high performance liquid chromatography was investigated by a combination of compositional analyses, methylation and glycosidase treatments, and proposed to be a hexasaccharide alditol, NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6(NeuAc alpha 2-3Gal beta 1-3) N-acetylgalactosaminitol.
6406478	3	16	theme	2-3Gal	772:777	arg1	beta					822:825	NeuAc alpha 2-3Gal beta 1-3	803:829	NeuAc alpha 2-3Gal beta 1-3	803:829	The structure of a major oligosaccharide alditol separated by high performance liquid chromatography was investigated by a combination of compositional analyses, methylation and glycosidase treatments, and proposed to be a hexasaccharide alditol, NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6(NeuAc alpha 2-3Gal beta 1-3) N-acetylgalactosaminitol.
6406478	2	17	theme	borohydride	401:411	arg1	treatment					413:421	alkaline borohydride treatment	392:421	alkaline borohydride treatment	392:421	Ser/Thr-linked (O-linked) oligosaccharides were released by alkaline borohydride treatment, and fractionated by high performance liquid chromatography with an anion-exchange resin.
6406478	4	18	from	intermediates	910:922	arg1	pathway					944:950	the biosynthetic pathway	927:950	the biosynthetic pathway of the major hexasaccharide	927:978	We also found some sugar units which appeared to be intermediates in the biosynthetic pathway of the major hexasaccharide.
6406478	2	19	theme	alkaline	392:399	arg1	treatment					413:421	alkaline borohydride treatment	392:421	alkaline borohydride treatment	392:421	Ser/Thr-linked (O-linked) oligosaccharides were released by alkaline borohydride treatment, and fractionated by high performance liquid chromatography with an anion-exchange resin.
6406478	2	20	theme	liquid	461:466	arg1	chromatography					468:481	high performance liquid chromatography	444:481	high performance liquid chromatography with an anion-exchange resin	444:510	Ser/Thr-linked (O-linked) oligosaccharides were released by alkaline borohydride treatment, and fractionated by high performance liquid chromatography with an anion-exchange resin.
6406478	1	21	theme	wheat	279:283	arg1	agglutinin-Sepharose					290:309	wheat germ agglutinin-Sepharose	279:309	wheat germ agglutinin-Sepharose	279:309	Glycocalicin, a predominant glycoprotein on the human platelet surface, has been purified from a platelet suspension by sonication, ammonium sulfate precipitation and acid treatment followed by chromatography on columns of wheat germ agglutinin-Sepharose and Sephacryl S-300.
6406478	4	22	theme	hexasaccharide	965:978	arg1	pathway					944:950	the biosynthetic pathway	927:950	the biosynthetic pathway of the major hexasaccharide	927:978	We also found some sugar units which appeared to be intermediates in the biosynthetic pathway of the major hexasaccharide.
6406478	2	23	theme	high	444:447	arg1	chromatography					468:481	high performance liquid chromatography	444:481	high performance liquid chromatography with an anion-exchange resin	444:510	Ser/Thr-linked (O-linked) oligosaccharides were released by alkaline borohydride treatment, and fractionated by high performance liquid chromatography with an anion-exchange resin.
6406478	2	24	theme	performance	449:459	arg1	chromatography					468:481	high performance liquid chromatography	444:481	high performance liquid chromatography with an anion-exchange resin	444:510	Ser/Thr-linked (O-linked) oligosaccharides were released by alkaline borohydride treatment, and fractionated by high performance liquid chromatography with an anion-exchange resin.
6406478	1	25	theme	germ	285:288	arg1	agglutinin-Sepharose					290:309	wheat germ agglutinin-Sepharose	279:309	wheat germ agglutinin-Sepharose	279:309	Glycocalicin, a predominant glycoprotein on the human platelet surface, has been purified from a platelet suspension by sonication, ammonium sulfate precipitation and acid treatment followed by chromatography on columns of wheat germ agglutinin-Sepharose and Sephacryl S-300.
6406478	4	26	theme	major	959:963	arg1	hexasaccharide					965:978	the major hexasaccharide	955:978	the major hexasaccharide	955:978	We also found some sugar units which appeared to be intermediates in the biosynthetic pathway of the major hexasaccharide.
6406478	1	27	theme	human	104:108	arg1	surface					119:125	the human platelet surface	100:125	the human platelet surface	100:125	Glycocalicin, a predominant glycoprotein on the human platelet surface, has been purified from a platelet suspension by sonication, ammonium sulfate precipitation and acid treatment followed by chromatography on columns of wheat germ agglutinin-Sepharose and Sephacryl S-300.
6406478	1	28	theme	ammonium	188:195	arg1	precipitation					205:217	ammonium sulfate precipitation	188:217	ammonium sulfate precipitation	188:217	Glycocalicin, a predominant glycoprotein on the human platelet surface, has been purified from a platelet suspension by sonication, ammonium sulfate precipitation and acid treatment followed by chromatography on columns of wheat germ agglutinin-Sepharose and Sephacryl S-300.
6406478	0	29	theme	platelet	33:40	arg1	glycocalicin					42:53	human platelet glycocalicin	27:53	human platelet glycocalicin	27:53	The carbohydrate moiety of human platelet glycocalicin.
6406478	1	30	theme	agglutinin-Sepharose	290:309	arg1	columns					268:274	columns	268:274	columns of wheat germ agglutinin-Sepharose and Sephacryl S-300	268:329	Glycocalicin, a predominant glycoprotein on the human platelet surface, has been purified from a platelet suspension by sonication, ammonium sulfate precipitation and acid treatment followed by chromatography on columns of wheat germ agglutinin-Sepharose and Sephacryl S-300.
6406478	3	31	dep	N-acetylgalactosaminitol	832:855	arg1	beta					794:797	NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6	760:801	NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6(NeuAc alpha 2-3Gal beta 1-3)	760:830	The structure of a major oligosaccharide alditol separated by high performance liquid chromatography was investigated by a combination of compositional analyses, methylation and glycosidase treatments, and proposed to be a hexasaccharide alditol, NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6(NeuAc alpha 2-3Gal beta 1-3) N-acetylgalactosaminitol.
6406478	3	31	dep	N-acetylgalactosaminitol	832:855	arg1	beta					822:825	NeuAc alpha 2-3Gal beta 1-3	803:829	NeuAc alpha 2-3Gal beta 1-3	803:829	The structure of a major oligosaccharide alditol separated by high performance liquid chromatography was investigated by a combination of compositional analyses, methylation and glycosidase treatments, and proposed to be a hexasaccharide alditol, NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6(NeuAc alpha 2-3Gal beta 1-3) N-acetylgalactosaminitol.
6406478	1	32	theme	sulfate	197:203	arg1	precipitation					205:217	ammonium sulfate precipitation	188:217	ammonium sulfate precipitation	188:217	Glycocalicin, a predominant glycoprotein on the human platelet surface, has been purified from a platelet suspension by sonication, ammonium sulfate precipitation and acid treatment followed by chromatography on columns of wheat germ agglutinin-Sepharose and Sephacryl S-300.
6406478	0	33	theme	human	27:31	arg1	glycocalicin					42:53	human platelet glycocalicin	27:53	human platelet glycocalicin	27:53	The carbohydrate moiety of human platelet glycocalicin.
6406478	1	34	from	chromatography	250:263	arg1	columns					268:274	columns	268:274	columns of wheat germ agglutinin-Sepharose and Sephacryl S-300	268:329	Glycocalicin, a predominant glycoprotein on the human platelet surface, has been purified from a platelet suspension by sonication, ammonium sulfate precipitation and acid treatment followed by chromatography on columns of wheat germ agglutinin-Sepharose and Sephacryl S-300.
6406478	3	35	theme	glycosidase	691:701	arg1	treatments					703:712	glycosidase treatments	691:712	glycosidase treatments	691:712	The structure of a major oligosaccharide alditol separated by high performance liquid chromatography was investigated by a combination of compositional analyses, methylation and glycosidase treatments, and proposed to be a hexasaccharide alditol, NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6(NeuAc alpha 2-3Gal beta 1-3) N-acetylgalactosaminitol.
6406478	3	35	theme	glycosidase	691:701	arg1	analyses					665:672	compositional analyses	651:672	compositional analyses	651:672	The structure of a major oligosaccharide alditol separated by high performance liquid chromatography was investigated by a combination of compositional analyses, methylation and glycosidase treatments, and proposed to be a hexasaccharide alditol, NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6(NeuAc alpha 2-3Gal beta 1-3) N-acetylgalactosaminitol.
6406478	3	36	theme	compositional	651:663	arg1	methylation					675:685	methylation	675:685	methylation	675:685	The structure of a major oligosaccharide alditol separated by high performance liquid chromatography was investigated by a combination of compositional analyses, methylation and glycosidase treatments, and proposed to be a hexasaccharide alditol, NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6(NeuAc alpha 2-3Gal beta 1-3) N-acetylgalactosaminitol.
6406478	3	36	theme	compositional	651:663	arg1	treatments					703:712	glycosidase treatments	691:712	glycosidase treatments	691:712	The structure of a major oligosaccharide alditol separated by high performance liquid chromatography was investigated by a combination of compositional analyses, methylation and glycosidase treatments, and proposed to be a hexasaccharide alditol, NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6(NeuAc alpha 2-3Gal beta 1-3) N-acetylgalactosaminitol.
6406478	3	36	theme	compositional	651:663	arg1	analyses					665:672	compositional analyses	651:672	compositional analyses	651:672	The structure of a major oligosaccharide alditol separated by high performance liquid chromatography was investigated by a combination of compositional analyses, methylation and glycosidase treatments, and proposed to be a hexasaccharide alditol, NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6(NeuAc alpha 2-3Gal beta 1-3) N-acetylgalactosaminitol.
6406478	2	37	theme	anion-exchange	491:504	arg1	resin					506:510	an anion-exchange resin	488:510	an anion-exchange resin	488:510	Ser/Thr-linked (O-linked) oligosaccharides were released by alkaline borohydride treatment, and fractionated by high performance liquid chromatography with an anion-exchange resin.
6406478	1	38	theme	Sephacryl	315:323	arg1	S-300					325:329	Sephacryl S-300	315:329	Sephacryl S-300	315:329	Glycocalicin, a predominant glycoprotein on the human platelet surface, has been purified from a platelet suspension by sonication, ammonium sulfate precipitation and acid treatment followed by chromatography on columns of wheat germ agglutinin-Sepharose and Sephacryl S-300.
6406478	3	39	theme	NeuAc	803:807	arg1	beta					794:797	NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6	760:801	NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6(NeuAc alpha 2-3Gal beta 1-3)	760:830	The structure of a major oligosaccharide alditol separated by high performance liquid chromatography was investigated by a combination of compositional analyses, methylation and glycosidase treatments, and proposed to be a hexasaccharide alditol, NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6(NeuAc alpha 2-3Gal beta 1-3) N-acetylgalactosaminitol.
6406478	3	39	theme	NeuAc	803:807	arg1	beta					822:825	NeuAc alpha 2-3Gal beta 1-3	803:829	NeuAc alpha 2-3Gal beta 1-3	803:829	The structure of a major oligosaccharide alditol separated by high performance liquid chromatography was investigated by a combination of compositional analyses, methylation and glycosidase treatments, and proposed to be a hexasaccharide alditol, NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6(NeuAc alpha 2-3Gal beta 1-3) N-acetylgalactosaminitol.
6406478	4	40	theme	sugar	877:881	arg1	units					883:887	some sugar units	872:887	some sugar units which appeared to be intermediates in the biosynthetic pathway of the major hexasaccharide	872:978	We also found some sugar units which appeared to be intermediates in the biosynthetic pathway of the major hexasaccharide.
6406478	1	41	theme	platelet	110:117	arg1	surface					119:125	the human platelet surface	100:125	the human platelet surface	100:125	Glycocalicin, a predominant glycoprotein on the human platelet surface, has been purified from a platelet suspension by sonication, ammonium sulfate precipitation and acid treatment followed by chromatography on columns of wheat germ agglutinin-Sepharose and Sephacryl S-300.
6406478	0	42	theme	glycocalicin	42:53	arg1	moiety					17:22	The carbohydrate moiety	0:22	The carbohydrate moiety of human platelet glycocalicin	0:53	The carbohydrate moiety of human platelet glycocalicin.
6406478	1	43	theme	S-300	325:329	arg1	columns					268:274	columns	268:274	columns of wheat germ agglutinin-Sepharose and Sephacryl S-300	268:329	Glycocalicin, a predominant glycoprotein on the human platelet surface, has been purified from a platelet suspension by sonication, ammonium sulfate precipitation and acid treatment followed by chromatography on columns of wheat germ agglutinin-Sepharose and Sephacryl S-300.
6406478	4	44	theme	biosynthetic	931:942	arg1	pathway					944:950	the biosynthetic pathway	927:950	the biosynthetic pathway of the major hexasaccharide	927:978	We also found some sugar units which appeared to be intermediates in the biosynthetic pathway of the major hexasaccharide.
6406478	2	45	theme	O-linked	348:355	arg1	oligosaccharides					358:373	Ser/Thr-linked (O-linked) oligosaccharides	332:373	Ser/Thr-linked (O-linked) oligosaccharides	332:373	Ser/Thr-linked (O-linked) oligosaccharides were released by alkaline borohydride treatment, and fractionated by high performance liquid chromatography with an anion-exchange resin.
6406478	3	46	theme	2-3Gal	815:820	arg1	beta					794:797	NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6	760:801	NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6(NeuAc alpha 2-3Gal beta 1-3)	760:830	The structure of a major oligosaccharide alditol separated by high performance liquid chromatography was investigated by a combination of compositional analyses, methylation and glycosidase treatments, and proposed to be a hexasaccharide alditol, NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6(NeuAc alpha 2-3Gal beta 1-3) N-acetylgalactosaminitol.
6406478	3	46	theme	2-3Gal	815:820	arg1	beta					822:825	NeuAc alpha 2-3Gal beta 1-3	803:829	NeuAc alpha 2-3Gal beta 1-3	803:829	The structure of a major oligosaccharide alditol separated by high performance liquid chromatography was investigated by a combination of compositional analyses, methylation and glycosidase treatments, and proposed to be a hexasaccharide alditol, NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6(NeuAc alpha 2-3Gal beta 1-3) N-acetylgalactosaminitol.
6406478	2	47	with	chromatography	468:481	arg1	resin					506:510	an anion-exchange resin	488:510	an anion-exchange resin	488:510	Ser/Thr-linked (O-linked) oligosaccharides were released by alkaline borohydride treatment, and fractionated by high performance liquid chromatography with an anion-exchange resin.
6406478	3	48	theme	analyses	665:672	arg1	combination					636:646	a combination	634:646	a combination of compositional analyses, methylation and glycosidase treatments	634:712	The structure of a major oligosaccharide alditol separated by high performance liquid chromatography was investigated by a combination of compositional analyses, methylation and glycosidase treatments, and proposed to be a hexasaccharide alditol, NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6(NeuAc alpha 2-3Gal beta 1-3) N-acetylgalactosaminitol.
6406478	3	49	theme	high	575:578	arg1	chromatography					599:612	high performance liquid chromatography	575:612	high performance liquid chromatography	575:612	The structure of a major oligosaccharide alditol separated by high performance liquid chromatography was investigated by a combination of compositional analyses, methylation and glycosidase treatments, and proposed to be a hexasaccharide alditol, NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6(NeuAc alpha 2-3Gal beta 1-3) N-acetylgalactosaminitol.
6406478	2	50	theme	Ser/Thr-linked	332:345	arg1	oligosaccharides					358:373	Ser/Thr-linked (O-linked) oligosaccharides	332:373	Ser/Thr-linked (O-linked) oligosaccharides	332:373	Ser/Thr-linked (O-linked) oligosaccharides were released by alkaline borohydride treatment, and fractionated by high performance liquid chromatography with an anion-exchange resin.
6406478	1	51	from	glycoprotein	84:95	arg1	surface					119:125	the human platelet surface	100:125	the human platelet surface	100:125	Glycocalicin, a predominant glycoprotein on the human platelet surface, has been purified from a platelet suspension by sonication, ammonium sulfate precipitation and acid treatment followed by chromatography on columns of wheat germ agglutinin-Sepharose and Sephacryl S-300.
6406478	1	52	theme	acid	223:226	arg1	treatment					228:236	acid treatment	223:236	acid treatment	223:236	Glycocalicin, a predominant glycoprotein on the human platelet surface, has been purified from a platelet suspension by sonication, ammonium sulfate precipitation and acid treatment followed by chromatography on columns of wheat germ agglutinin-Sepharose and Sephacryl S-300.
6406478	3	53	theme	alditol	751:757	arg1	N-acetylgalactosaminitol					832:855	a hexasaccharide alditol, NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6(NeuAc alpha 2-3Gal beta 1-3) N-acetylgalactosaminitol	734:855	N-acetylgalactosaminitol	832:855	The structure of a major oligosaccharide alditol separated by high performance liquid chromatography was investigated by a combination of compositional analyses, methylation and glycosidase treatments, and proposed to be a hexasaccharide alditol, NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6(NeuAc alpha 2-3Gal beta 1-3) N-acetylgalactosaminitol.
6406478	3	53	theme	alditol	751:757	arg1	structure					517:525	The structure	513:525	The structure of a major oligosaccharide alditol separated by high performance liquid chromatography	513:612	The structure of a major oligosaccharide alditol separated by high performance liquid chromatography was investigated by a combination of compositional analyses, methylation and glycosidase treatments, and proposed to be a hexasaccharide alditol, NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6(NeuAc alpha 2-3Gal beta 1-3) N-acetylgalactosaminitol.
6406478	3	54	theme	alditol	554:560	arg1	structure					517:525	The structure	513:525	The structure of a major oligosaccharide alditol separated by high performance liquid chromatography	513:612	The structure of a major oligosaccharide alditol separated by high performance liquid chromatography was investigated by a combination of compositional analyses, methylation and glycosidase treatments, and proposed to be a hexasaccharide alditol, NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6(NeuAc alpha 2-3Gal beta 1-3) N-acetylgalactosaminitol.
6406478	3	54	theme	alditol	554:560	arg1	N-acetylgalactosaminitol					832:855	a hexasaccharide alditol, NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6(NeuAc alpha 2-3Gal beta 1-3) N-acetylgalactosaminitol	734:855	N-acetylgalactosaminitol	832:855	The structure of a major oligosaccharide alditol separated by high performance liquid chromatography was investigated by a combination of compositional analyses, methylation and glycosidase treatments, and proposed to be a hexasaccharide alditol, NeuAc alpha 2-3Gal beta 1-4GlcNAc beta 1-6(NeuAc alpha 2-3Gal beta 1-3) N-acetylgalactosaminitol.
2271582	4	0	theme	major	1093:1097	arg1	glycoproteins					1109:1121	two major intrinsic glycoproteins	1089:1121	two major intrinsic glycoproteins of human erythrocytes	1089:1143	These structural features of the sugar moiety of glucose transporter are quite different from those of two major intrinsic glycoproteins of human erythrocytes, glycophorin A and band 3.
2271582	4	0	theme	major	1093:1097	arg1	band					1164:1167	band 3	1164:1169	band 3	1164:1169	These structural features of the sugar moiety of glucose transporter are quite different from those of two major intrinsic glycoproteins of human erythrocytes, glycophorin A and band 3.
2271582	4	0	theme	major	1093:1097	arg1	A					1158:1158	glycophorin A	1146:1158	glycophorin A	1146:1158	These structural features of the sugar moiety of glucose transporter are quite different from those of two major intrinsic glycoproteins of human erythrocytes, glycophorin A and band 3.
2271582	3	1	theme	1----4GlcNAc	814:825	arg1	1----6					853:858	Fuc alpha 1----6	843:858	Fuc alpha 1----6	843:858	Structural study of each oligosaccharide by exo- and endoglycosidase digestion and methylation analysis indicated that the glycoprotein contains a high-mannose-type oligosaccharide, Man9.GlcNAc.GlcNAc, and biantennary complex-type oligosaccharides with Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc as their cores and the poly-N-acetyllactosamine composed of about 16 N-acetyllactosaminyl units as their outer chains.
2271582	3	1	theme	1----4GlcNAc	814:825	arg1	beta					827:830	Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4	741:837	Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc	741:865	Structural study of each oligosaccharide by exo- and endoglycosidase digestion and methylation analysis indicated that the glycoprotein contains a high-mannose-type oligosaccharide, Man9.GlcNAc.GlcNAc, and biantennary complex-type oligosaccharides with Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc as their cores and the poly-N-acetyllactosamine composed of about 16 N-acetyllactosaminyl units as their outer chains.
2271582	4	2	gly	glycoproteins	1109:1121	arg1	glycoproteins					1109:1121	two major intrinsic glycoproteins	1089:1121	two major intrinsic glycoproteins of human erythrocytes	1089:1143	These structural features of the sugar moiety of glucose transporter are quite different from those of two major intrinsic glycoproteins of human erythrocytes, glycophorin A and band 3.
2271582	4	2	gly	glycoproteins	1109:1121	arg1	band					1164:1167	band 3	1164:1169	band 3	1164:1169	These structural features of the sugar moiety of glucose transporter are quite different from those of two major intrinsic glycoproteins of human erythrocytes, glycophorin A and band 3.
2271582	4	2	gly	glycoproteins	1109:1121	arg1	A					1158:1158	glycophorin A	1146:1158	glycophorin A	1146:1158	These structural features of the sugar moiety of glucose transporter are quite different from those of two major intrinsic glycoproteins of human erythrocytes, glycophorin A and band 3.
2271582	2	3	theme	Bio-Gel	427:433	arg1	chromatography					446:459	Bio-Gel P-4 column chromatography	427:459	Bio-Gel P-4 column chromatography	427:459	They were converted to radioactive oligosaccharides by NaB3H4 reduction after N-acetylation and fractionated by anion-exchange column chromatography and Bio-Gel P-4 column chromatography after sialidase treatment.
2271582	0	4	theme	human	76:80	arg1	erythrocytes					82:93	human erythrocytes	76:93	human erythrocytes	76:93	Structures of the asparagine-linked sugar chain of glucose transporter from human erythrocytes.
2271582	3	5	theme	Man	800:802	arg1	1----6					853:858	Fuc alpha 1----6	843:858	Fuc alpha 1----6	843:858	Structural study of each oligosaccharide by exo- and endoglycosidase digestion and methylation analysis indicated that the glycoprotein contains a high-mannose-type oligosaccharide, Man9.GlcNAc.GlcNAc, and biantennary complex-type oligosaccharides with Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc as their cores and the poly-N-acetyllactosamine composed of about 16 N-acetyllactosaminyl units as their outer chains.
2271582	3	5	theme	Man	800:802	arg1	beta					827:830	Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4	741:837	Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc	741:865	Structural study of each oligosaccharide by exo- and endoglycosidase digestion and methylation analysis indicated that the glycoprotein contains a high-mannose-type oligosaccharide, Man9.GlcNAc.GlcNAc, and biantennary complex-type oligosaccharides with Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc as their cores and the poly-N-acetyllactosamine composed of about 16 N-acetyllactosaminyl units as their outer chains.
2271582	0	6	link	asparagine-linked	18:34	arg1	chain					42:46	the asparagine-linked sugar chain	14:46	the asparagine-linked sugar chain of glucose transporter from human erythrocytes	14:93	Structures of the asparagine-linked sugar chain of glucose transporter from human erythrocytes.
2271582	4	7	theme	human	1126:1130	arg1	erythrocytes					1132:1143	human erythrocytes	1126:1143	human erythrocytes	1126:1143	These structural features of the sugar moiety of glucose transporter are quite different from those of two major intrinsic glycoproteins of human erythrocytes, glycophorin A and band 3.
2271582	3	8	theme	N-acetyllactosaminyl	936:955	arg1	units					957:961	about 16 N-acetyllactosaminyl units	927:961	about 16 N-acetyllactosaminyl units	927:961	Structural study of each oligosaccharide by exo- and endoglycosidase digestion and methylation analysis indicated that the glycoprotein contains a high-mannose-type oligosaccharide, Man9.GlcNAc.GlcNAc, and biantennary complex-type oligosaccharides with Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc as their cores and the poly-N-acetyllactosamine composed of about 16 N-acetyllactosaminyl units as their outer chains.
2271582	3	9	with	oligosaccharides	719:734	arg1	GlcNAc					860:865	Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc	741:865	Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc	741:865	Structural study of each oligosaccharide by exo- and endoglycosidase digestion and methylation analysis indicated that the glycoprotein contains a high-mannose-type oligosaccharide, Man9.GlcNAc.GlcNAc, and biantennary complex-type oligosaccharides with Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc as their cores and the poly-N-acetyllactosamine composed of about 16 N-acetyllactosaminyl units as their outer chains.
2271582	3	10	contain	contains	624:631	arg1	glycoprotein					611:622	the glycoprotein	607:622	the glycoprotein	607:622	Structural study of each oligosaccharide by exo- and endoglycosidase digestion and methylation analysis indicated that the glycoprotein contains a high-mannose-type oligosaccharide, Man9.GlcNAc.GlcNAc, and biantennary complex-type oligosaccharides with Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc as their cores and the poly-N-acetyllactosamine composed of about 16 N-acetyllactosaminyl units as their outer chains.
2271582	3	10	contain	contains	624:631	arg2	Man9.GlcNAc.GlcNAc					670:687	Man9.GlcNAc.GlcNAc	670:687	Man9.GlcNAc.GlcNAc	670:687	Structural study of each oligosaccharide by exo- and endoglycosidase digestion and methylation analysis indicated that the glycoprotein contains a high-mannose-type oligosaccharide, Man9.GlcNAc.GlcNAc, and biantennary complex-type oligosaccharides with Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc as their cores and the poly-N-acetyllactosamine composed of about 16 N-acetyllactosaminyl units as their outer chains.
2271582	3	10	contain	contains	624:631	arg2	oligosaccharide					653:667	a high-mannose-type oligosaccharide	633:667	a high-mannose-type oligosaccharide	633:667	Structural study of each oligosaccharide by exo- and endoglycosidase digestion and methylation analysis indicated that the glycoprotein contains a high-mannose-type oligosaccharide, Man9.GlcNAc.GlcNAc, and biantennary complex-type oligosaccharides with Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc as their cores and the poly-N-acetyllactosamine composed of about 16 N-acetyllactosaminyl units as their outer chains.
2271582	3	10	contain	contains	624:631	arg2	oligosaccharides					719:734	biantennary complex-type oligosaccharides	694:734	biantennary complex-type oligosaccharides with Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc as their cores and the poly-N-acetyllactosamine composed of about 16 N-acetyllactosaminyl units as their outer chains	694:983	Structural study of each oligosaccharide by exo- and endoglycosidase digestion and methylation analysis indicated that the glycoprotein contains a high-mannose-type oligosaccharide, Man9.GlcNAc.GlcNAc, and biantennary complex-type oligosaccharides with Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc as their cores and the poly-N-acetyllactosamine composed of about 16 N-acetyllactosaminyl units as their outer chains.
2271582	4	11	theme	structural	992:1001	arg1	features					1003:1010	These structural features	986:1010	These structural features of the sugar moiety of glucose transporter	986:1053	These structural features of the sugar moiety of glucose transporter are quite different from those of two major intrinsic glycoproteins of human erythrocytes, glycophorin A and band 3.
2271582	2	12	theme	NaB3H4	329:334	arg1	reduction					336:344	NaB3H4 reduction	329:344	NaB3H4 reduction after N-acetylation	329:364	They were converted to radioactive oligosaccharides by NaB3H4 reduction after N-acetylation and fractionated by anion-exchange column chromatography and Bio-Gel P-4 column chromatography after sialidase treatment.
2271582	4	13	theme	intrinsic	1099:1107	arg1	glycoproteins					1109:1121	two major intrinsic glycoproteins	1089:1121	two major intrinsic glycoproteins of human erythrocytes	1089:1143	These structural features of the sugar moiety of glucose transporter are quite different from those of two major intrinsic glycoproteins of human erythrocytes, glycophorin A and band 3.
2271582	4	13	theme	intrinsic	1099:1107	arg1	band					1164:1167	band 3	1164:1169	band 3	1164:1169	These structural features of the sugar moiety of glucose transporter are quite different from those of two major intrinsic glycoproteins of human erythrocytes, glycophorin A and band 3.
2271582	4	13	theme	intrinsic	1099:1107	arg1	A					1158:1158	glycophorin A	1146:1158	glycophorin A	1146:1158	These structural features of the sugar moiety of glucose transporter are quite different from those of two major intrinsic glycoproteins of human erythrocytes, glycophorin A and band 3.
2271582	3	14	gly	glycoprotein	611:622	arg1	glycoprotein					611:622	the glycoprotein	607:622	the glycoprotein	607:622	Structural study of each oligosaccharide by exo- and endoglycosidase digestion and methylation analysis indicated that the glycoprotein contains a high-mannose-type oligosaccharide, Man9.GlcNAc.GlcNAc, and biantennary complex-type oligosaccharides with Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc as their cores and the poly-N-acetyllactosamine composed of about 16 N-acetyllactosaminyl units as their outer chains.
2271582	4	15	theme	moiety	1025:1030	arg1	features					1003:1010	These structural features	986:1010	These structural features of the sugar moiety of glucose transporter	986:1053	These structural features of the sugar moiety of glucose transporter are quite different from those of two major intrinsic glycoproteins of human erythrocytes, glycophorin A and band 3.
2271582	3	16	theme	Structural	488:497	arg1	study					499:503	Structural study	488:503	Structural study of each oligosaccharide by exo- and endoglycosidase digestion and methylation analysis	488:590	Structural study of each oligosaccharide by exo- and endoglycosidase digestion and methylation analysis indicated that the glycoprotein contains a high-mannose-type oligosaccharide, Man9.GlcNAc.GlcNAc, and biantennary complex-type oligosaccharides with Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc as their cores and the poly-N-acetyllactosamine composed of about 16 N-acetyllactosaminyl units as their outer chains.
2271582	0	17	from	chain	42:46	arg1	erythrocytes					82:93	human erythrocytes	76:93	human erythrocytes	76:93	Structures of the asparagine-linked sugar chain of glucose transporter from human erythrocytes.
2271582	2	18	theme	sialidase	467:475	arg1	treatment					477:485	sialidase treatment	467:485	sialidase treatment	467:485	They were converted to radioactive oligosaccharides by NaB3H4 reduction after N-acetylation and fractionated by anion-exchange column chromatography and Bio-Gel P-4 column chromatography after sialidase treatment.
2271582	4	19	theme	glucose	1035:1041	arg1	transporter					1043:1053	glucose transporter	1035:1053	glucose transporter	1035:1053	These structural features of the sugar moiety of glucose transporter are quite different from those of two major intrinsic glycoproteins of human erythrocytes, glycophorin A and band 3.
2271582	3	20	theme	biantennary	694:704	arg1	oligosaccharides					719:734	biantennary complex-type oligosaccharides	694:734	biantennary complex-type oligosaccharides with Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc as their cores and the poly-N-acetyllactosamine composed of about 16 N-acetyllactosaminyl units as their outer chains	694:983	Structural study of each oligosaccharide by exo- and endoglycosidase digestion and methylation analysis indicated that the glycoprotein contains a high-mannose-type oligosaccharide, Man9.GlcNAc.GlcNAc, and biantennary complex-type oligosaccharides with Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc as their cores and the poly-N-acetyllactosamine composed of about 16 N-acetyllactosaminyl units as their outer chains.
2271582	3	21	theme	beta	804:807	arg1	1----6					853:858	Fuc alpha 1----6	843:858	Fuc alpha 1----6	843:858	Structural study of each oligosaccharide by exo- and endoglycosidase digestion and methylation analysis indicated that the glycoprotein contains a high-mannose-type oligosaccharide, Man9.GlcNAc.GlcNAc, and biantennary complex-type oligosaccharides with Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc as their cores and the poly-N-acetyllactosamine composed of about 16 N-acetyllactosaminyl units as their outer chains.
2271582	3	21	theme	beta	804:807	arg1	beta					827:830	Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4	741:837	Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc	741:865	Structural study of each oligosaccharide by exo- and endoglycosidase digestion and methylation analysis indicated that the glycoprotein contains a high-mannose-type oligosaccharide, Man9.GlcNAc.GlcNAc, and biantennary complex-type oligosaccharides with Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc as their cores and the poly-N-acetyllactosamine composed of about 16 N-acetyllactosaminyl units as their outer chains.
2271582	4	22	theme	erythrocytes	1132:1143	arg1	glycoproteins					1109:1121	two major intrinsic glycoproteins	1089:1121	two major intrinsic glycoproteins of human erythrocytes	1089:1143	These structural features of the sugar moiety of glucose transporter are quite different from those of two major intrinsic glycoproteins of human erythrocytes, glycophorin A and band 3.
2271582	4	22	theme	erythrocytes	1132:1143	arg1	band					1164:1167	band 3	1164:1169	band 3	1164:1169	These structural features of the sugar moiety of glucose transporter are quite different from those of two major intrinsic glycoproteins of human erythrocytes, glycophorin A and band 3.
2271582	4	22	theme	erythrocytes	1132:1143	arg1	A					1158:1158	glycophorin A	1146:1158	glycophorin A	1146:1158	These structural features of the sugar moiety of glucose transporter are quite different from those of two major intrinsic glycoproteins of human erythrocytes, glycophorin A and band 3.
2271582	1	23	from	chain	124:128	arg1	erythrocytes					164:175	human erythrocytes	158:175	human erythrocytes	158:175	The asparagine-linked sugar chain of glucose transporter from human erythrocytes was quantitatively released as oligosaccharides from the polypeptide backbone by hydrazinolysis.
2271582	3	24	theme	complex-type	706:717	arg1	oligosaccharides					719:734	biantennary complex-type oligosaccharides	694:734	biantennary complex-type oligosaccharides with Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc as their cores and the poly-N-acetyllactosamine composed of about 16 N-acetyllactosaminyl units as their outer chains	694:983	Structural study of each oligosaccharide by exo- and endoglycosidase digestion and methylation analysis indicated that the glycoprotein contains a high-mannose-type oligosaccharide, Man9.GlcNAc.GlcNAc, and biantennary complex-type oligosaccharides with Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc as their cores and the poly-N-acetyllactosamine composed of about 16 N-acetyllactosaminyl units as their outer chains.
2271582	3	25	theme	oligosaccharide	513:527	arg1	study					499:503	Structural study	488:503	Structural study of each oligosaccharide by exo- and endoglycosidase digestion and methylation analysis	488:590	Structural study of each oligosaccharide by exo- and endoglycosidase digestion and methylation analysis indicated that the glycoprotein contains a high-mannose-type oligosaccharide, Man9.GlcNAc.GlcNAc, and biantennary complex-type oligosaccharides with Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc as their cores and the poly-N-acetyllactosamine composed of about 16 N-acetyllactosaminyl units as their outer chains.
2271582	0	26	theme	asparagine-linked	18:34	arg1	chain					42:46	the asparagine-linked sugar chain	14:46	the asparagine-linked sugar chain of glucose transporter from human erythrocytes	14:93	Structures of the asparagine-linked sugar chain of glucose transporter from human erythrocytes.
2271582	1	27	theme	asparagine-linked	100:116	arg1	chain					124:128	The asparagine-linked sugar chain	96:128	The asparagine-linked sugar chain of glucose transporter from human erythrocytes	96:175	The asparagine-linked sugar chain of glucose transporter from human erythrocytes was quantitatively released as oligosaccharides from the polypeptide backbone by hydrazinolysis.
2271582	1	27	theme	asparagine-linked	100:116	arg1	oligosaccharides					208:223	oligosaccharides	208:223	oligosaccharides from the polypeptide backbone	208:253	The asparagine-linked sugar chain of glucose transporter from human erythrocytes was quantitatively released as oligosaccharides from the polypeptide backbone by hydrazinolysis.
2271582	1	28	from	erythrocytes	164:175	arg1	chain					124:128	The asparagine-linked sugar chain	96:128	The asparagine-linked sugar chain of glucose transporter from human erythrocytes	96:175	The asparagine-linked sugar chain of glucose transporter from human erythrocytes was quantitatively released as oligosaccharides from the polypeptide backbone by hydrazinolysis.
2271582	1	28	from	erythrocytes	164:175	arg1	transporter					141:151	glucose transporter	133:151	glucose transporter from human erythrocytes	133:175	The asparagine-linked sugar chain of glucose transporter from human erythrocytes was quantitatively released as oligosaccharides from the polypeptide backbone by hydrazinolysis.
2271582	1	28	from	erythrocytes	164:175	arg1	oligosaccharides					208:223	oligosaccharides	208:223	oligosaccharides from the polypeptide backbone	208:253	The asparagine-linked sugar chain of glucose transporter from human erythrocytes was quantitatively released as oligosaccharides from the polypeptide backbone by hydrazinolysis.
2271582	4	29	theme	glycophorin	1146:1156	arg1	glycoproteins					1109:1121	two major intrinsic glycoproteins	1089:1121	two major intrinsic glycoproteins of human erythrocytes	1089:1143	These structural features of the sugar moiety of glucose transporter are quite different from those of two major intrinsic glycoproteins of human erythrocytes, glycophorin A and band 3.
2271582	4	29	theme	glycophorin	1146:1156	arg1	A					1158:1158	glycophorin A	1146:1158	glycophorin A	1146:1158	These structural features of the sugar moiety of glucose transporter are quite different from those of two major intrinsic glycoproteins of human erythrocytes, glycophorin A and band 3.
2271582	3	30	theme	Fuc	843:845	arg1	1----6					853:858	Fuc alpha 1----6	843:858	Fuc alpha 1----6	843:858	Structural study of each oligosaccharide by exo- and endoglycosidase digestion and methylation analysis indicated that the glycoprotein contains a high-mannose-type oligosaccharide, Man9.GlcNAc.GlcNAc, and biantennary complex-type oligosaccharides with Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc as their cores and the poly-N-acetyllactosamine composed of about 16 N-acetyllactosaminyl units as their outer chains.
2271582	3	30	theme	Fuc	843:845	arg1	beta					827:830	Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4	741:837	Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc	741:865	Structural study of each oligosaccharide by exo- and endoglycosidase digestion and methylation analysis indicated that the glycoprotein contains a high-mannose-type oligosaccharide, Man9.GlcNAc.GlcNAc, and biantennary complex-type oligosaccharides with Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc as their cores and the poly-N-acetyllactosamine composed of about 16 N-acetyllactosaminyl units as their outer chains.
2271582	3	31	theme	high-mannose-type	635:651	arg1	oligosaccharide					653:667	a high-mannose-type oligosaccharide	633:667	a high-mannose-type oligosaccharide	633:667	Structural study of each oligosaccharide by exo- and endoglycosidase digestion and methylation analysis indicated that the glycoprotein contains a high-mannose-type oligosaccharide, Man9.GlcNAc.GlcNAc, and biantennary complex-type oligosaccharides with Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc as their cores and the poly-N-acetyllactosamine composed of about 16 N-acetyllactosaminyl units as their outer chains.
2271582	0	32	from	erythrocytes	82:93	arg1	chain					42:46	the asparagine-linked sugar chain	14:46	the asparagine-linked sugar chain of glucose transporter from human erythrocytes	14:93	Structures of the asparagine-linked sugar chain of glucose transporter from human erythrocytes.
2271582	0	32	from	erythrocytes	82:93	arg1	transporter					59:69	glucose transporter	51:69	glucose transporter from human erythrocytes	51:93	Structures of the asparagine-linked sugar chain of glucose transporter from human erythrocytes.
2271582	1	33	theme	sugar	118:122	arg1	chain					124:128	The asparagine-linked sugar chain	96:128	The asparagine-linked sugar chain of glucose transporter from human erythrocytes	96:175	The asparagine-linked sugar chain of glucose transporter from human erythrocytes was quantitatively released as oligosaccharides from the polypeptide backbone by hydrazinolysis.
2271582	1	33	theme	sugar	118:122	arg1	oligosaccharides					208:223	oligosaccharides	208:223	oligosaccharides from the polypeptide backbone	208:253	The asparagine-linked sugar chain of glucose transporter from human erythrocytes was quantitatively released as oligosaccharides from the polypeptide backbone by hydrazinolysis.
2271582	3	34	with	Man9.GlcNAc.GlcNAc	670:687	arg1	GlcNAc					860:865	Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc	741:865	Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc	741:865	Structural study of each oligosaccharide by exo- and endoglycosidase digestion and methylation analysis indicated that the glycoprotein contains a high-mannose-type oligosaccharide, Man9.GlcNAc.GlcNAc, and biantennary complex-type oligosaccharides with Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc as their cores and the poly-N-acetyllactosamine composed of about 16 N-acetyllactosaminyl units as their outer chains.
2271582	0	35	theme	chain	42:46	arg1	Structures					0:9	Structures	0:9	Structures of the asparagine-linked sugar chain of glucose transporter from human erythrocytes	0:93	Structures of the asparagine-linked sugar chain of glucose transporter from human erythrocytes.
2271582	3	36	theme	alpha	847:851	arg1	1----6					853:858	Fuc alpha 1----6	843:858	Fuc alpha 1----6	843:858	Structural study of each oligosaccharide by exo- and endoglycosidase digestion and methylation analysis indicated that the glycoprotein contains a high-mannose-type oligosaccharide, Man9.GlcNAc.GlcNAc, and biantennary complex-type oligosaccharides with Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc as their cores and the poly-N-acetyllactosamine composed of about 16 N-acetyllactosaminyl units as their outer chains.
2271582	3	36	theme	alpha	847:851	arg1	beta					827:830	Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4	741:837	Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc	741:865	Structural study of each oligosaccharide by exo- and endoglycosidase digestion and methylation analysis indicated that the glycoprotein contains a high-mannose-type oligosaccharide, Man9.GlcNAc.GlcNAc, and biantennary complex-type oligosaccharides with Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc as their cores and the poly-N-acetyllactosamine composed of about 16 N-acetyllactosaminyl units as their outer chains.
2271582	4	37	theme	transporter	1043:1053	arg1	moiety					1025:1030	the sugar moiety	1015:1030	the sugar moiety of glucose transporter	1015:1053	These structural features of the sugar moiety of glucose transporter are quite different from those of two major intrinsic glycoproteins of human erythrocytes, glycophorin A and band 3.
2271582	3	38	theme	Man	741:743	arg1	alpha					786:790	Man alpha 1----3	782:797	Man alpha 1----3	782:797	Structural study of each oligosaccharide by exo- and endoglycosidase digestion and methylation analysis indicated that the glycoprotein contains a high-mannose-type oligosaccharide, Man9.GlcNAc.GlcNAc, and biantennary complex-type oligosaccharides with Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc as their cores and the poly-N-acetyllactosamine composed of about 16 N-acetyllactosaminyl units as their outer chains.
2271582	3	38	theme	Man	741:743	arg1	beta					769:772	GlcNAc beta 1----4	762:779	GlcNAc beta 1----4	762:779	Structural study of each oligosaccharide by exo- and endoglycosidase digestion and methylation analysis indicated that the glycoprotein contains a high-mannose-type oligosaccharide, Man9.GlcNAc.GlcNAc, and biantennary complex-type oligosaccharides with Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc as their cores and the poly-N-acetyllactosamine composed of about 16 N-acetyllactosaminyl units as their outer chains.
2271582	3	38	theme	Man	741:743	arg1	alpha					745:749	Man alpha 1----6	741:756	Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc	741:865	Structural study of each oligosaccharide by exo- and endoglycosidase digestion and methylation analysis indicated that the glycoprotein contains a high-mannose-type oligosaccharide, Man9.GlcNAc.GlcNAc, and biantennary complex-type oligosaccharides with Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc as their cores and the poly-N-acetyllactosamine composed of about 16 N-acetyllactosaminyl units as their outer chains.
2271582	1	39	theme	polypeptide	234:244	arg1	backbone					246:253	the polypeptide backbone	230:253	the polypeptide backbone	230:253	The asparagine-linked sugar chain of glucose transporter from human erythrocytes was quantitatively released as oligosaccharides from the polypeptide backbone by hydrazinolysis.
2271582	0	40	theme	sugar	36:40	arg1	chain					42:46	the asparagine-linked sugar chain	14:46	the asparagine-linked sugar chain of glucose transporter from human erythrocytes	14:93	Structures of the asparagine-linked sugar chain of glucose transporter from human erythrocytes.
2271582	3	41	with	oligosaccharide	653:667	arg1	GlcNAc					860:865	Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc	741:865	Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc	741:865	Structural study of each oligosaccharide by exo- and endoglycosidase digestion and methylation analysis indicated that the glycoprotein contains a high-mannose-type oligosaccharide, Man9.GlcNAc.GlcNAc, and biantennary complex-type oligosaccharides with Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc as their cores and the poly-N-acetyllactosamine composed of about 16 N-acetyllactosaminyl units as their outer chains.
2271582	3	42	theme	alpha	745:749	arg1	1----6					853:858	Fuc alpha 1----6	843:858	Fuc alpha 1----6	843:858	Structural study of each oligosaccharide by exo- and endoglycosidase digestion and methylation analysis indicated that the glycoprotein contains a high-mannose-type oligosaccharide, Man9.GlcNAc.GlcNAc, and biantennary complex-type oligosaccharides with Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc as their cores and the poly-N-acetyllactosamine composed of about 16 N-acetyllactosaminyl units as their outer chains.
2271582	3	42	theme	alpha	745:749	arg1	beta					827:830	Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4	741:837	Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc	741:865	Structural study of each oligosaccharide by exo- and endoglycosidase digestion and methylation analysis indicated that the glycoprotein contains a high-mannose-type oligosaccharide, Man9.GlcNAc.GlcNAc, and biantennary complex-type oligosaccharides with Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc as their cores and the poly-N-acetyllactosamine composed of about 16 N-acetyllactosaminyl units as their outer chains.
2271582	3	43	theme	endoglycosidase	541:555	arg1	digestion					557:565	endoglycosidase digestion	541:565	endoglycosidase digestion	541:565	Structural study of each oligosaccharide by exo- and endoglycosidase digestion and methylation analysis indicated that the glycoprotein contains a high-mannose-type oligosaccharide, Man9.GlcNAc.GlcNAc, and biantennary complex-type oligosaccharides with Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc as their cores and the poly-N-acetyllactosamine composed of about 16 N-acetyllactosaminyl units as their outer chains.
2271582	0	44	theme	glucose	51:57	arg1	transporter					59:69	glucose transporter	51:69	glucose transporter from human erythrocytes	51:93	Structures of the asparagine-linked sugar chain of glucose transporter from human erythrocytes.
2271582	1	45	from	backbone	246:253	arg1	chain					124:128	The asparagine-linked sugar chain	96:128	The asparagine-linked sugar chain of glucose transporter from human erythrocytes	96:175	The asparagine-linked sugar chain of glucose transporter from human erythrocytes was quantitatively released as oligosaccharides from the polypeptide backbone by hydrazinolysis.
2271582	1	45	from	backbone	246:253	arg1	oligosaccharides					208:223	oligosaccharides	208:223	oligosaccharides from the polypeptide backbone	208:253	The asparagine-linked sugar chain of glucose transporter from human erythrocytes was quantitatively released as oligosaccharides from the polypeptide backbone by hydrazinolysis.
2271582	2	46	theme	P-4	435:437	arg1	chromatography					446:459	Bio-Gel P-4 column chromatography	427:459	Bio-Gel P-4 column chromatography	427:459	They were converted to radioactive oligosaccharides by NaB3H4 reduction after N-acetylation and fractionated by anion-exchange column chromatography and Bio-Gel P-4 column chromatography after sialidase treatment.
2271582	3	47	theme	methylation	571:581	arg1	analysis					583:590	methylation analysis	571:590	methylation analysis	571:590	Structural study of each oligosaccharide by exo- and endoglycosidase digestion and methylation analysis indicated that the glycoprotein contains a high-mannose-type oligosaccharide, Man9.GlcNAc.GlcNAc, and biantennary complex-type oligosaccharides with Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc as their cores and the poly-N-acetyllactosamine composed of about 16 N-acetyllactosaminyl units as their outer chains.
2271582	2	48	theme	column	401:406	arg1	chromatography					408:421	anion-exchange column chromatography	386:421	anion-exchange column chromatography	386:421	They were converted to radioactive oligosaccharides by NaB3H4 reduction after N-acetylation and fractionated by anion-exchange column chromatography and Bio-Gel P-4 column chromatography after sialidase treatment.
2271582	4	49	theme	sugar	1019:1023	arg1	moiety					1025:1030	the sugar moiety	1015:1030	the sugar moiety of glucose transporter	1015:1053	These structural features of the sugar moiety of glucose transporter are quite different from those of two major intrinsic glycoproteins of human erythrocytes, glycophorin A and band 3.
2271582	2	50	theme	radioactive	297:307	arg1	oligosaccharides					309:324	radioactive oligosaccharides	297:324	radioactive oligosaccharides	297:324	They were converted to radioactive oligosaccharides by NaB3H4 reduction after N-acetylation and fractionated by anion-exchange column chromatography and Bio-Gel P-4 column chromatography after sialidase treatment.
2271582	1	51	theme	glucose	133:139	arg1	transporter					141:151	glucose transporter	133:151	glucose transporter from human erythrocytes	133:175	The asparagine-linked sugar chain of glucose transporter from human erythrocytes was quantitatively released as oligosaccharides from the polypeptide backbone by hydrazinolysis.
2271582	3	52	theme	outer	972:976	arg1	chains					978:983	their outer chains	966:983	their outer chains	966:983	Structural study of each oligosaccharide by exo- and endoglycosidase digestion and methylation analysis indicated that the glycoprotein contains a high-mannose-type oligosaccharide, Man9.GlcNAc.GlcNAc, and biantennary complex-type oligosaccharides with Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc as their cores and the poly-N-acetyllactosamine composed of about 16 N-acetyllactosaminyl units as their outer chains.
2271582	3	53	theme	Man	782:784	arg1	alpha					786:790	Man alpha 1----3	782:797	Man alpha 1----3	782:797	Structural study of each oligosaccharide by exo- and endoglycosidase digestion and methylation analysis indicated that the glycoprotein contains a high-mannose-type oligosaccharide, Man9.GlcNAc.GlcNAc, and biantennary complex-type oligosaccharides with Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc as their cores and the poly-N-acetyllactosamine composed of about 16 N-acetyllactosaminyl units as their outer chains.
2271582	3	53	theme	Man	782:784	arg1	alpha					745:749	Man alpha 1----6	741:756	Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc	741:865	Structural study of each oligosaccharide by exo- and endoglycosidase digestion and methylation analysis indicated that the glycoprotein contains a high-mannose-type oligosaccharide, Man9.GlcNAc.GlcNAc, and biantennary complex-type oligosaccharides with Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc as their cores and the poly-N-acetyllactosamine composed of about 16 N-acetyllactosaminyl units as their outer chains.
2271582	3	54	theme	GlcNAc	762:767	arg1	beta					769:772	GlcNAc beta 1----4	762:779	GlcNAc beta 1----4	762:779	Structural study of each oligosaccharide by exo- and endoglycosidase digestion and methylation analysis indicated that the glycoprotein contains a high-mannose-type oligosaccharide, Man9.GlcNAc.GlcNAc, and biantennary complex-type oligosaccharides with Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc as their cores and the poly-N-acetyllactosamine composed of about 16 N-acetyllactosaminyl units as their outer chains.
2271582	3	54	theme	GlcNAc	762:767	arg1	alpha					745:749	Man alpha 1----6	741:756	Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc	741:865	Structural study of each oligosaccharide by exo- and endoglycosidase digestion and methylation analysis indicated that the glycoprotein contains a high-mannose-type oligosaccharide, Man9.GlcNAc.GlcNAc, and biantennary complex-type oligosaccharides with Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc as their cores and the poly-N-acetyllactosamine composed of about 16 N-acetyllactosaminyl units as their outer chains.
2271582	1	55	theme	transporter	141:151	arg1	chain					124:128	The asparagine-linked sugar chain	96:128	The asparagine-linked sugar chain of glucose transporter from human erythrocytes	96:175	The asparagine-linked sugar chain of glucose transporter from human erythrocytes was quantitatively released as oligosaccharides from the polypeptide backbone by hydrazinolysis.
2271582	1	55	theme	transporter	141:151	arg1	oligosaccharides					208:223	oligosaccharides	208:223	oligosaccharides from the polypeptide backbone	208:253	The asparagine-linked sugar chain of glucose transporter from human erythrocytes was quantitatively released as oligosaccharides from the polypeptide backbone by hydrazinolysis.
2271582	2	56	theme	anion-exchange	386:399	arg1	chromatography					408:421	anion-exchange column chromatography	386:421	anion-exchange column chromatography	386:421	They were converted to radioactive oligosaccharides by NaB3H4 reduction after N-acetylation and fractionated by anion-exchange column chromatography and Bio-Gel P-4 column chromatography after sialidase treatment.
2271582	1	57	link	asparagine-linked	100:116	arg1	chain					124:128	The asparagine-linked sugar chain	96:128	The asparagine-linked sugar chain of glucose transporter from human erythrocytes	96:175	The asparagine-linked sugar chain of glucose transporter from human erythrocytes was quantitatively released as oligosaccharides from the polypeptide backbone by hydrazinolysis.
2271582	1	57	link	asparagine-linked	100:116	arg1	oligosaccharides					208:223	oligosaccharides	208:223	oligosaccharides from the polypeptide backbone	208:253	The asparagine-linked sugar chain of glucose transporter from human erythrocytes was quantitatively released as oligosaccharides from the polypeptide backbone by hydrazinolysis.
2271582	2	58	theme	column	439:444	arg1	chromatography					446:459	Bio-Gel P-4 column chromatography	427:459	Bio-Gel P-4 column chromatography	427:459	They were converted to radioactive oligosaccharides by NaB3H4 reduction after N-acetylation and fractionated by anion-exchange column chromatography and Bio-Gel P-4 column chromatography after sialidase treatment.
2271582	0	59	theme	transporter	59:69	arg1	chain					42:46	the asparagine-linked sugar chain	14:46	the asparagine-linked sugar chain of glucose transporter from human erythrocytes	14:93	Structures of the asparagine-linked sugar chain of glucose transporter from human erythrocytes.
2271582	3	60	theme	beta	809:812	arg1	1----6					853:858	Fuc alpha 1----6	843:858	Fuc alpha 1----6	843:858	Structural study of each oligosaccharide by exo- and endoglycosidase digestion and methylation analysis indicated that the glycoprotein contains a high-mannose-type oligosaccharide, Man9.GlcNAc.GlcNAc, and biantennary complex-type oligosaccharides with Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc as their cores and the poly-N-acetyllactosamine composed of about 16 N-acetyllactosaminyl units as their outer chains.
2271582	3	60	theme	beta	809:812	arg1	beta					827:830	Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4	741:837	Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc	741:865	Structural study of each oligosaccharide by exo- and endoglycosidase digestion and methylation analysis indicated that the glycoprotein contains a high-mannose-type oligosaccharide, Man9.GlcNAc.GlcNAc, and biantennary complex-type oligosaccharides with Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc as their cores and the poly-N-acetyllactosamine composed of about 16 N-acetyllactosaminyl units as their outer chains.
2271582	4	61	from	those	1080:1084	arg1	different					1065:1073	different	1065:1073	different	1065:1073	These structural features of the sugar moiety of glucose transporter are quite different from those of two major intrinsic glycoproteins of human erythrocytes, glycophorin A and band 3.
2271582	1	62	theme	human	158:162	arg1	erythrocytes					164:175	human erythrocytes	158:175	human erythrocytes	158:175	The asparagine-linked sugar chain of glucose transporter from human erythrocytes was quantitatively released as oligosaccharides from the polypeptide backbone by hydrazinolysis.
2271582	3	63	theme	beta	827:830	arg1	GlcNAc					860:865	Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc	741:865	Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc	741:865	Structural study of each oligosaccharide by exo- and endoglycosidase digestion and methylation analysis indicated that the glycoprotein contains a high-mannose-type oligosaccharide, Man9.GlcNAc.GlcNAc, and biantennary complex-type oligosaccharides with Man alpha 1----6(+/- GlcNAc beta 1----4)(Man alpha 1----3) Man beta beta 1----4GlcNAc beta 1----4(+/- Fuc alpha 1----6)GlcNAc as their cores and the poly-N-acetyllactosamine composed of about 16 N-acetyllactosaminyl units as their outer chains.
7686446	3	0	theme	1-->2Man	1071:1078	arg1	alpha					1080:1084	1-->2Man alpha 1-->6	1071:1090	Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)	1027:1157	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	6	1	theme	inverse	1717:1723	arg1	proportion					1725:1734	inverse proportion	1717:1734	inverse proportion to the gestation period	1717:1758	Fucosylation of AFP produced in fetal liver increased in inverse proportion to the gestation period, in weeks, indicating that fucosylation of AFP in HCC may be related to the dedifferentiation of human hepatocytes through malignant transformation.
7686446	3	2	theme	chain	660:664	arg1	beta					1002:1005	Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2	885:1020	beta	1002:1005	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	2	theme	chain	660:664	arg1	beta					864:867	Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2	730:882	beta	864:867	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	2	theme	chain	660:664	arg1	structures					666:675	the whole sugar chain structures	644:675	the whole sugar chain structures of human cord serum AFP	644:699	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	2	theme	chain	660:664	arg1	follows					721:727	follows	721:727	follows	721:727	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	2	theme	chain	660:664	arg1	beta					1066:1069	Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta	1027:1069	Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)	1027:1157	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	5	3	theme	additional	1599:1608	arg1	fucosylation					1610:1621	additional fucosylation	1599:1621	additional fucosylation of the proximal N-acetylglucosamine	1599:1657	In contrast, the sugar chain structure of HCC highly specific AFP isoform was found to comprise a monosialyl-biantennary sugar chain with additional fucosylation of the proximal N-acetylglucosamine.
7686446	4	4	dep	1-->4GlcNAcOT	1241:1253	arg1	GlcNAcOT					1353:1360	GlcNAcOT	1353:1360	GlcNAcOT	1353:1360	R1 and R2 denote GlcNAc beta 1-->4GlcNAcOT (subscript OT represents an NaB3H4-reduced oligosaccharide) and GlcNAc beta 1-->4(Fuc alpha 1-->6)GlcNAcOT, respectively, and the ratio between R1 and R2 in the respective fractions was approximately 19:1.
7686446	3	5	theme	beta	954:957	arg1	beta					906:909	Gal beta 1-->4GlcNAc beta	885:909	Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)	885:997	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	5	theme	beta	954:957	arg1	1-->3					992:996	Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3	932:996	Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3	932:996	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	6	theme	AFP	697:699	arg1	beta					1002:1005	Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2	885:1020	beta	1002:1005	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	6	theme	AFP	697:699	arg1	beta					864:867	Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2	730:882	beta	864:867	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	6	theme	AFP	697:699	arg1	structures					666:675	the whole sugar chain structures	644:675	the whole sugar chain structures of human cord serum AFP	644:699	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	6	theme	AFP	697:699	arg1	follows					721:727	follows	721:727	follows	721:727	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	6	theme	AFP	697:699	arg1	beta					1066:1069	Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta	1027:1069	Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)	1027:1157	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	7	theme	Neu5Ac	1092:1097	arg1	beta					1132:1135	Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta	1092:1135	Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3	1092:1156	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	8	theme	alpha	939:943	arg1	beta					954:957	Neu5Ac alpha 2-->6Gal beta 1	932:959	Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3	932:996	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	9	theme	cord	686:689	arg1	AFP					697:699	human cord serum AFP	680:699	human cord serum AFP	680:699	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	10	theme	1-->2Man	977:984	arg1	beta					906:909	Gal beta 1-->4GlcNAc beta	885:909	Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)	885:997	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	10	theme	1-->2Man	977:984	arg1	1-->3					992:996	Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3	932:996	Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3	932:996	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	11	theme	beta	1162:1165	arg1	1-->4R1					1167:1173	Man beta 1-->4R1	1158:1173	Man beta 1-->4R1	1158:1173	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	4	12	theme	beta	1236:1239	arg1	1-->4GlcNAcOT					1241:1253	GlcNAc beta 1-->4GlcNAcOT	1229:1253	GlcNAc beta 1-->4GlcNAcOT (subscript OT represents an NaB3H4-reduced oligosaccharide)	1229:1313	R1 and R2 denote GlcNAc beta 1-->4GlcNAcOT (subscript OT represents an NaB3H4-reduced oligosaccharide) and GlcNAc beta 1-->4(Fuc alpha 1-->6)GlcNAcOT, respectively, and the ratio between R1 and R2 in the respective fractions was approximately 19:1.
7686446	4	12	theme	beta	1236:1239	arg1	OT					1266:1267	subscript OT	1256:1267	subscript OT represents an NaB3H4-reduced oligosaccharide	1256:1312	R1 and R2 denote GlcNAc beta 1-->4GlcNAcOT (subscript OT represents an NaB3H4-reduced oligosaccharide) and GlcNAc beta 1-->4(Fuc alpha 1-->6)GlcNAcOT, respectively, and the ratio between R1 and R2 in the respective fractions was approximately 19:1.
7686446	3	13	theme	beta	1115:1118	arg1	beta					1132:1135	Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta	1092:1135	Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3	1092:1156	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	2	14	theme	liver	545:549	arg1	diseases					551:558	benign liver diseases	538:558	benign liver diseases	538:558	AFP produced in HCC and benign liver diseases was separated into several isoforms corresponding to different sugar chain structures by several types of lectin affinity electrophoresis, and the HCC-specific AFP isoform was discriminated from those of benign liver diseases.
7686446	3	15	theme	-->4GlcNAc	961:970	arg1	beta					906:909	Gal beta 1-->4GlcNAc beta	885:909	Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)	885:997	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	15	theme	-->4GlcNAc	961:970	arg1	1-->3					992:996	Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3	932:996	Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3	932:996	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	5	16	theme	specific	1514:1521	arg1	isoform					1527:1533	HCC highly specific AFP isoform	1503:1533	HCC highly specific AFP isoform	1503:1533	In contrast, the sugar chain structure of HCC highly specific AFP isoform was found to comprise a monosialyl-biantennary sugar chain with additional fucosylation of the proximal N-acetylglucosamine.
7686446	4	17	theme	beta	1326:1329	arg1	1-->4					1331:1335	GlcNAc beta 1-->4	1319:1335	GlcNAc beta 1-->4(Fuc alpha 1-->6)	1319:1352	R1 and R2 denote GlcNAc beta 1-->4GlcNAcOT (subscript OT represents an NaB3H4-reduced oligosaccharide) and GlcNAc beta 1-->4(Fuc alpha 1-->6)GlcNAcOT, respectively, and the ratio between R1 and R2 in the respective fractions was approximately 19:1.
7686446	4	17	theme	beta	1326:1329	arg1	alpha					1341:1345	Fuc alpha 1-->6	1337:1351	Fuc alpha 1-->6	1337:1351	R1 and R2 denote GlcNAc beta 1-->4GlcNAcOT (subscript OT represents an NaB3H4-reduced oligosaccharide) and GlcNAc beta 1-->4(Fuc alpha 1-->6)GlcNAcOT, respectively, and the ratio between R1 and R2 in the respective fractions was approximately 19:1.
7686446	5	18	theme	monosialyl-biantennary	1559:1580	arg1	chain					1588:1592	a monosialyl-biantennary sugar chain	1557:1592	a monosialyl-biantennary sugar chain with additional fucosylation of the proximal N-acetylglucosamine	1557:1657	In contrast, the sugar chain structure of HCC highly specific AFP isoform was found to comprise a monosialyl-biantennary sugar chain with additional fucosylation of the proximal N-acetylglucosamine.
7686446	5	19	theme	sugar	1478:1482	arg1	structure					1490:1498	the sugar chain structure	1474:1498	the sugar chain structure of HCC highly specific AFP isoform	1474:1533	In contrast, the sugar chain structure of HCC highly specific AFP isoform was found to comprise a monosialyl-biantennary sugar chain with additional fucosylation of the proximal N-acetylglucosamine.
7686446	3	20	theme	alpha	737:741	arg1	1-->3					854:858	Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3	794:858	Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3	794:858	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	20	theme	alpha	737:741	arg1	beta					864:867	Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2	730:882	beta	864:867	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	20	theme	alpha	737:741	arg1	structures					666:675	the whole sugar chain structures	644:675	the whole sugar chain structures of human cord serum AFP	644:699	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	21	theme	HCC-specific	587:598	arg1	isoform					604:610	HCC-specific AFP isoform	587:610	HCC-specific AFP isoform	587:610	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	4	22	theme	subscript	1256:1264	arg1	1-->4GlcNAcOT					1241:1253	GlcNAc beta 1-->4GlcNAcOT	1229:1253	GlcNAc beta 1-->4GlcNAcOT (subscript OT represents an NaB3H4-reduced oligosaccharide)	1229:1313	R1 and R2 denote GlcNAc beta 1-->4GlcNAcOT (subscript OT represents an NaB3H4-reduced oligosaccharide) and GlcNAc beta 1-->4(Fuc alpha 1-->6)GlcNAcOT, respectively, and the ratio between R1 and R2 in the respective fractions was approximately 19:1.
7686446	4	22	theme	subscript	1256:1264	arg1	OT					1266:1267	subscript OT	1256:1267	subscript OT represents an NaB3H4-reduced oligosaccharide	1256:1312	R1 and R2 denote GlcNAc beta 1-->4GlcNAcOT (subscript OT represents an NaB3H4-reduced oligosaccharide) and GlcNAc beta 1-->4(Fuc alpha 1-->6)GlcNAcOT, respectively, and the ratio between R1 and R2 in the respective fractions was approximately 19:1.
7686446	0	23	theme	hepatocellular	138:151	arg1	carcinomas					153:162	hepatocellular carcinomas	138:162	hepatocellular carcinomas	138:162	Sugar chains of human cord serum alpha-fetoprotein: characteristics of N-linked sugar chains of glycoproteins produced in human liver and hepatocellular carcinomas.
7686446	3	24	theme	-->6Gal	809:815	arg1	beta					834:837	Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta	794:837	Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3	794:858	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	25	theme	81.6:8.9:9.5	1198:1209	arg1	ratio					1189:1193	the ratio	1185:1193	the ratio of 81.6:8.9:9.5	1185:1209	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	26	theme	beta	768:771	arg1	1-->3					854:858	Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3	794:858	Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3	794:858	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	26	theme	beta	768:771	arg1	beta					864:867	Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2	730:882	beta	864:867	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	26	theme	beta	768:771	arg1	structures					666:675	the whole sugar chain structures	644:675	the whole sugar chain structures of human cord serum AFP	644:699	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	27	theme	alpha	801:805	arg1	beta					834:837	Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta	794:837	Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3	794:858	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	2	28	theme	AFP	494:496	arg1	isoform					498:504	the HCC-specific AFP isoform	477:504	the HCC-specific AFP isoform	477:504	AFP produced in HCC and benign liver diseases was separated into several isoforms corresponding to different sugar chain structures by several types of lectin affinity electrophoresis, and the HCC-specific AFP isoform was discriminated from those of benign liver diseases.
7686446	3	29	theme	beta	751:754	arg1	1-->3					854:858	Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3	794:858	Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3	794:858	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	29	theme	beta	751:754	arg1	beta					864:867	Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2	730:882	beta	864:867	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	29	theme	beta	751:754	arg1	structures					666:675	the whole sugar chain structures	644:675	the whole sugar chain structures of human cord serum AFP	644:699	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	30	theme	isoform	604:610	arg1	isoform					604:610	HCC-specific AFP isoform	587:610	HCC-specific AFP isoform	587:610	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	30	theme	isoform	604:610	arg1	amount					577:582	a small amount	569:582	a small amount of HCC-specific AFP isoform	569:610	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	31	theme	1-->2Man	839:846	arg1	1-->3					854:858	Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3	794:858	Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3	794:858	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	31	theme	1-->2Man	839:846	arg1	beta					864:867	Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2	730:882	beta	864:867	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	6	32	theme	AFP	1803:1805	arg1	fucosylation					1787:1798	fucosylation	1787:1798	fucosylation of AFP in HCC	1787:1812	Fucosylation of AFP produced in fetal liver increased in inverse proportion to the gestation period, in weeks, indicating that fucosylation of AFP in HCC may be related to the dedifferentiation of human hepatocytes through malignant transformation.
7686446	0	33	theme	N-linked	71:78	arg1	chains					86:91	N-linked sugar chains	71:91	N-linked sugar chains of glycoproteins produced in human liver and hepatocellular carcinomas	71:162	Sugar chains of human cord serum alpha-fetoprotein: characteristics of N-linked sugar chains of glycoproteins produced in human liver and hepatocellular carcinomas.
7686446	3	34	theme	Man	998:1000	arg1	structures					666:675	the whole sugar chain structures	644:675	the whole sugar chain structures of human cord serum AFP	644:699	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	34	theme	Man	998:1000	arg1	beta					1002:1005	Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2	885:1020	beta	1002:1005	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	1	35	theme	Human	165:169	arg1	AFP					196:198	AFP	196:198	AFP	196:198	Human serum alpha-fetoprotein (AFP) is elevated in not only hepatocellular carcinoma (HCC) but also benign liver diseases.
7686446	1	35	theme	Human	165:169	arg1	alpha-fetoprotein					177:193	Human serum alpha-fetoprotein	165:193	Human serum alpha-fetoprotein (AFP)	165:199	Human serum alpha-fetoprotein (AFP) is elevated in not only hepatocellular carcinoma (HCC) but also benign liver diseases.
7686446	3	36	theme	1-->4GlcNAc	822:832	arg1	beta					834:837	Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta	794:837	Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3	794:858	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	4	37	from	ratio	1385:1389	arg1	fractions					1427:1435	the respective fractions	1412:1435	the respective fractions	1412:1435	R1 and R2 denote GlcNAc beta 1-->4GlcNAcOT (subscript OT represents an NaB3H4-reduced oligosaccharide) and GlcNAc beta 1-->4(Fuc alpha 1-->6)GlcNAcOT, respectively, and the ratio between R1 and R2 in the respective fractions was approximately 19:1.
7686446	3	38	theme	alpha	782:786	arg1	1-->3					854:858	Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3	794:858	Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3	794:858	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	38	theme	alpha	782:786	arg1	beta					864:867	Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2	730:882	beta	864:867	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	38	theme	alpha	782:786	arg1	structures					666:675	the whole sugar chain structures	644:675	the whole sugar chain structures of human cord serum AFP	644:699	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	0	39	theme	chains	86:91	arg1	characteristics					52:66	characteristics	52:66	Sugar chains of human cord serum alpha-fetoprotein: characteristics of N-linked sugar chains of glycoproteins produced in human liver and hepatocellular carcinomas.	0:163	Sugar chains of human cord serum alpha-fetoprotein: characteristics of N-linked sugar chains of glycoproteins produced in human liver and hepatocellular carcinomas.
7686446	3	40	theme	Man	860:862	arg1	1-->3					854:858	Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3	794:858	Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3	794:858	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	40	theme	Man	860:862	arg1	beta					864:867	Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2	730:882	beta	864:867	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	40	theme	Man	860:862	arg1	structures					666:675	the whole sugar chain structures	644:675	the whole sugar chain structures of human cord serum AFP	644:699	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	5	41	theme	isoform	1527:1533	arg1	structure					1490:1498	the sugar chain structure	1474:1498	the sugar chain structure of HCC highly specific AFP isoform	1474:1533	In contrast, the sugar chain structure of HCC highly specific AFP isoform was found to comprise a monosialyl-biantennary sugar chain with additional fucosylation of the proximal N-acetylglucosamine.
7686446	0	42	theme	glycoproteins	96:108	arg1	chains					86:91	N-linked sugar chains	71:91	N-linked sugar chains of glycoproteins produced in human liver and hepatocellular carcinomas	71:162	Sugar chains of human cord serum alpha-fetoprotein: characteristics of N-linked sugar chains of glycoproteins produced in human liver and hepatocellular carcinomas.
7686446	3	43	dep	beta	1002:1005	arg1	1-->4R1					1007:1013	1-->4R1	1007:1013	1-->4R1	1007:1013	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	6	44	theme	human	1857:1861	arg1	hepatocytes					1863:1873	human hepatocytes	1857:1873	human hepatocytes	1857:1873	Fucosylation of AFP produced in fetal liver increased in inverse proportion to the gestation period, in weeks, indicating that fucosylation of AFP in HCC may be related to the dedifferentiation of human hepatocytes through malignant transformation.
7686446	0	45	theme	Sugar	0:4	arg1	chains					6:11	Sugar chains	0:11	Sugar chains of human cord serum alpha-fetoprotein: characteristics of N-linked sugar chains of glycoproteins produced in human liver and hepatocellular carcinomas.	0:163	Sugar chains of human cord serum alpha-fetoprotein: characteristics of N-linked sugar chains of glycoproteins produced in human liver and hepatocellular carcinomas.
7686446	2	46	theme	several	423:429	arg1	types					431:435	several types	423:435	several types of lectin affinity electrophoresis	423:470	AFP produced in HCC and benign liver diseases was separated into several isoforms corresponding to different sugar chain structures by several types of lectin affinity electrophoresis, and the HCC-specific AFP isoform was discriminated from those of benign liver diseases.
7686446	5	47	theme	AFP	1523:1525	arg1	isoform					1527:1533	HCC highly specific AFP isoform	1503:1533	HCC highly specific AFP isoform	1503:1533	In contrast, the sugar chain structure of HCC highly specific AFP isoform was found to comprise a monosialyl-biantennary sugar chain with additional fucosylation of the proximal N-acetylglucosamine.
7686446	1	48	theme	liver	272:276	arg1	diseases					278:285	benign liver diseases	265:285	not only hepatocellular carcinoma (HCC) but also benign liver diseases	216:285	Human serum alpha-fetoprotein (AFP) is elevated in not only hepatocellular carcinoma (HCC) but also benign liver diseases.
7686446	3	49	theme	alpha	1034:1038	arg1	structures					666:675	the whole sugar chain structures	644:675	the whole sugar chain structures of human cord serum AFP	644:699	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	49	theme	alpha	1034:1038	arg1	beta					1066:1069	Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta	1027:1069	Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)	1027:1157	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	6	50	theme	AFP	1676:1678	arg1	Fucosylation					1660:1671	Fucosylation	1660:1671	Fucosylation of AFP produced in fetal liver	1660:1702	Fucosylation of AFP produced in fetal liver increased in inverse proportion to the gestation period, in weeks, indicating that fucosylation of AFP in HCC may be related to the dedifferentiation of human hepatocytes through malignant transformation.
7686446	2	51	theme	sugar	397:401	arg1	structures					409:418	different sugar chain structures	387:418	different sugar chain structures by several types of lectin affinity electrophoresis	387:470	AFP produced in HCC and benign liver diseases was separated into several isoforms corresponding to different sugar chain structures by several types of lectin affinity electrophoresis, and the HCC-specific AFP isoform was discriminated from those of benign liver diseases.
7686446	0	52	theme	cord	22:25	arg1	alpha-fetoprotein					33:49	human cord serum alpha-fetoprotein	16:49	human cord serum alpha-fetoprotein	16:49	Sugar chains of human cord serum alpha-fetoprotein: characteristics of N-linked sugar chains of glycoproteins produced in human liver and hepatocellular carcinomas.
7686446	3	53	theme	1-->4GlcNAc	894:904	arg1	beta					906:909	Gal beta 1-->4GlcNAc beta	885:909	Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)	885:997	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	53	theme	1-->4GlcNAc	894:904	arg1	1-->3					992:996	Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3	932:996	Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3	932:996	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	2	54	theme	affinity	447:454	arg1	electrophoresis					456:470	lectin affinity electrophoresis	440:470	lectin affinity electrophoresis	440:470	AFP produced in HCC and benign liver diseases was separated into several isoforms corresponding to different sugar chain structures by several types of lectin affinity electrophoresis, and the HCC-specific AFP isoform was discriminated from those of benign liver diseases.
7686446	3	55	theme	cord	628:631	arg1	AFP					639:641	cord serum AFP	628:641	cord serum AFP	628:641	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	2	56	theme	liver	319:323	arg1	diseases					325:332	benign liver diseases	312:332	benign liver diseases	312:332	AFP produced in HCC and benign liver diseases was separated into several isoforms corresponding to different sugar chain structures by several types of lectin affinity electrophoresis, and the HCC-specific AFP isoform was discriminated from those of benign liver diseases.
7686446	0	57	theme	alpha-fetoprotein	33:49	arg1	chains					6:11	Sugar chains	0:11	Sugar chains of human cord serum alpha-fetoprotein: characteristics of N-linked sugar chains of glycoproteins produced in human liver and hepatocellular carcinomas.	0:163	Sugar chains of human cord serum alpha-fetoprotein: characteristics of N-linked sugar chains of glycoproteins produced in human liver and hepatocellular carcinomas.
7686446	3	58	theme	Gal	885:887	arg1	beta					906:909	Gal beta 1-->4GlcNAc beta	885:909	Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)	885:997	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	58	theme	Gal	885:887	arg1	1-->3					992:996	Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3	932:996	Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3	932:996	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	59	theme	sugar	654:658	arg1	beta					1002:1005	Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2	885:1020	beta	1002:1005	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	59	theme	sugar	654:658	arg1	beta					864:867	Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2	730:882	beta	864:867	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	59	theme	sugar	654:658	arg1	structures					666:675	the whole sugar chain structures	644:675	the whole sugar chain structures of human cord serum AFP	644:699	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	59	theme	sugar	654:658	arg1	follows					721:727	follows	721:727	follows	721:727	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	59	theme	sugar	654:658	arg1	beta					1066:1069	Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta	1027:1069	Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)	1027:1157	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	4	60	theme	respective	1416:1425	arg1	fractions					1427:1435	the respective fractions	1412:1435	the respective fractions	1412:1435	R1 and R2 denote GlcNAc beta 1-->4GlcNAcOT (subscript OT represents an NaB3H4-reduced oligosaccharide) and GlcNAc beta 1-->4(Fuc alpha 1-->6)GlcNAcOT, respectively, and the ratio between R1 and R2 in the respective fractions was approximately 19:1.
7686446	3	61	theme	beta	1049:1052	arg1	structures					666:675	the whole sugar chain structures	644:675	the whole sugar chain structures of human cord serum AFP	644:699	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	61	theme	beta	1049:1052	arg1	beta					1066:1069	Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta	1027:1069	Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)	1027:1157	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	5	62	theme	sugar	1582:1586	arg1	chain					1588:1592	a monosialyl-biantennary sugar chain	1557:1592	a monosialyl-biantennary sugar chain with additional fucosylation of the proximal N-acetylglucosamine	1557:1657	In contrast, the sugar chain structure of HCC highly specific AFP isoform was found to comprise a monosialyl-biantennary sugar chain with additional fucosylation of the proximal N-acetylglucosamine.
7686446	1	63	theme	hepatocellular	225:238	arg1	HCC					251:253	HCC	251:253	HCC	251:253	Human serum alpha-fetoprotein (AFP) is elevated in not only hepatocellular carcinoma (HCC) but also benign liver diseases.
7686446	1	63	theme	hepatocellular	225:238	arg1	carcinoma					240:248	hepatocellular carcinoma	225:248	not only hepatocellular carcinoma (HCC) but also benign liver diseases	216:285	Human serum alpha-fetoprotein (AFP) is elevated in not only hepatocellular carcinoma (HCC) but also benign liver diseases.
7686446	4	64	dep	OT	1266:1267	arg1	represents					1269:1278	represents	1269:1278	represents an NaB3H4-reduced oligosaccharide	1269:1312	R1 and R2 denote GlcNAc beta 1-->4GlcNAcOT (subscript OT represents an NaB3H4-reduced oligosaccharide) and GlcNAc beta 1-->4(Fuc alpha 1-->6)GlcNAcOT, respectively, and the ratio between R1 and R2 in the respective fractions was approximately 19:1.
7686446	4	65	theme	Fuc	1337:1339	arg1	1-->4					1331:1335	GlcNAc beta 1-->4	1319:1335	GlcNAc beta 1-->4(Fuc alpha 1-->6)	1319:1352	R1 and R2 denote GlcNAc beta 1-->4GlcNAcOT (subscript OT represents an NaB3H4-reduced oligosaccharide) and GlcNAc beta 1-->4(Fuc alpha 1-->6)GlcNAcOT, respectively, and the ratio between R1 and R2 in the respective fractions was approximately 19:1.
7686446	4	65	theme	Fuc	1337:1339	arg1	alpha					1341:1345	Fuc alpha 1-->6	1337:1351	Fuc alpha 1-->6	1337:1351	R1 and R2 denote GlcNAc beta 1-->4GlcNAcOT (subscript OT represents an NaB3H4-reduced oligosaccharide) and GlcNAc beta 1-->4(Fuc alpha 1-->6)GlcNAcOT, respectively, and the ratio between R1 and R2 in the respective fractions was approximately 19:1.
7686446	3	66	theme	1-->2Man	911:918	arg1	alpha					920:924	1-->2Man alpha 1-->6	911:930	Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)	885:997	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	67	theme	human	680:684	arg1	AFP					697:699	human cord serum AFP	680:699	human cord serum AFP	680:699	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	68	theme	2-->6Gal	945:952	arg1	beta					954:957	Neu5Ac alpha 2-->6Gal beta 1	932:959	Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3	932:996	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	4	69	theme	GlcNAc	1229:1234	arg1	1-->4GlcNAcOT					1241:1253	GlcNAc beta 1-->4GlcNAcOT	1229:1253	GlcNAc beta 1-->4GlcNAcOT (subscript OT represents an NaB3H4-reduced oligosaccharide)	1229:1313	R1 and R2 denote GlcNAc beta 1-->4GlcNAcOT (subscript OT represents an NaB3H4-reduced oligosaccharide) and GlcNAc beta 1-->4(Fuc alpha 1-->6)GlcNAcOT, respectively, and the ratio between R1 and R2 in the respective fractions was approximately 19:1.
7686446	4	69	theme	GlcNAc	1229:1234	arg1	OT					1266:1267	subscript OT	1256:1267	subscript OT represents an NaB3H4-reduced oligosaccharide	1256:1312	R1 and R2 denote GlcNAc beta 1-->4GlcNAcOT (subscript OT represents an NaB3H4-reduced oligosaccharide) and GlcNAc beta 1-->4(Fuc alpha 1-->6)GlcNAcOT, respectively, and the ratio between R1 and R2 in the respective fractions was approximately 19:1.
7686446	3	70	dep	beta	1132:1135	arg1	alpha					1146:1150	1-->2Man alpha 1-->3	1137:1156	Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3	1092:1156	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	71	theme	-->6Gal	1107:1113	arg1	beta					1132:1135	Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta	1092:1135	Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3	1092:1156	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	0	72	link	N-linked	71:78	arg1	chains					86:91	N-linked sugar chains	71:91	N-linked sugar chains of glycoproteins produced in human liver and hepatocellular carcinomas	71:162	Sugar chains of human cord serum alpha-fetoprotein: characteristics of N-linked sugar chains of glycoproteins produced in human liver and hepatocellular carcinomas.
7686446	3	73	theme	Neu5Ac	932:937	arg1	beta					954:957	Neu5Ac alpha 2-->6Gal beta 1	932:959	Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3	932:996	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	5	74	with	chain	1588:1592	arg1	fucosylation					1610:1621	additional fucosylation	1599:1621	additional fucosylation of the proximal N-acetylglucosamine	1599:1657	In contrast, the sugar chain structure of HCC highly specific AFP isoform was found to comprise a monosialyl-biantennary sugar chain with additional fucosylation of the proximal N-acetylglucosamine.
7686446	1	75	theme	serum	171:175	arg1	AFP					196:198	AFP	196:198	AFP	196:198	Human serum alpha-fetoprotein (AFP) is elevated in not only hepatocellular carcinoma (HCC) but also benign liver diseases.
7686446	1	75	theme	serum	171:175	arg1	alpha-fetoprotein					177:193	Human serum alpha-fetoprotein	165:193	Human serum alpha-fetoprotein (AFP)	165:199	Human serum alpha-fetoprotein (AFP) is elevated in not only hepatocellular carcinoma (HCC) but also benign liver diseases.
7686446	3	76	theme	alpha	1099:1103	arg1	beta					1132:1135	Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta	1092:1135	Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3	1092:1156	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	77	theme	beta	972:975	arg1	beta					906:909	Gal beta 1-->4GlcNAc beta	885:909	Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)	885:997	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	77	theme	beta	972:975	arg1	1-->3					992:996	Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3	932:996	Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3	932:996	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	5	78	theme	HCC	1503:1505	arg1	isoform					1527:1533	HCC highly specific AFP isoform	1503:1533	HCC highly specific AFP isoform	1503:1533	In contrast, the sugar chain structure of HCC highly specific AFP isoform was found to comprise a monosialyl-biantennary sugar chain with additional fucosylation of the proximal N-acetylglucosamine.
7686446	3	79	theme	serum	691:695	arg1	AFP					697:699	human cord serum AFP	680:699	human cord serum AFP	680:699	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	5	80	theme	N-acetylglucosamine	1639:1657	arg1	fucosylation					1610:1621	additional fucosylation	1599:1621	additional fucosylation of the proximal N-acetylglucosamine	1599:1657	In contrast, the sugar chain structure of HCC highly specific AFP isoform was found to comprise a monosialyl-biantennary sugar chain with additional fucosylation of the proximal N-acetylglucosamine.
7686446	3	81	dep	beta	906:909	arg1	alpha					920:924	1-->2Man alpha 1-->6	911:930	Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)	885:997	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	82	theme	1-->2Man	1137:1144	arg1	alpha					1146:1150	1-->2Man alpha 1-->3	1137:1156	Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3	1092:1156	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	0	83	theme	human	122:126	arg1	liver					128:132	human liver	122:132	human liver	122:132	Sugar chains of human cord serum alpha-fetoprotein: characteristics of N-linked sugar chains of glycoproteins produced in human liver and hepatocellular carcinomas.
7686446	3	84	theme	1-->4GlcNAc	1120:1130	arg1	beta					1132:1135	Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta	1092:1135	Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3	1092:1156	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	2	85	theme	benign	538:543	arg1	diseases					551:558	benign liver diseases	538:558	benign liver diseases	538:558	AFP produced in HCC and benign liver diseases was separated into several isoforms corresponding to different sugar chain structures by several types of lectin affinity electrophoresis, and the HCC-specific AFP isoform was discriminated from those of benign liver diseases.
7686446	4	86	theme	NaB3H4-reduced	1283:1296	arg1	oligosaccharide					1298:1312	an NaB3H4-reduced oligosaccharide	1280:1312	an NaB3H4-reduced oligosaccharide	1280:1312	R1 and R2 denote GlcNAc beta 1-->4GlcNAcOT (subscript OT represents an NaB3H4-reduced oligosaccharide) and GlcNAc beta 1-->4(Fuc alpha 1-->6)GlcNAcOT, respectively, and the ratio between R1 and R2 in the respective fractions was approximately 19:1.
7686446	3	87	theme	Man	1158:1160	arg1	1-->4R1					1167:1173	Man beta 1-->4R1	1158:1173	Man beta 1-->4R1	1158:1173	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	5	88	theme	chain	1484:1488	arg1	structure					1490:1498	the sugar chain structure	1474:1498	the sugar chain structure of HCC highly specific AFP isoform	1474:1533	In contrast, the sugar chain structure of HCC highly specific AFP isoform was found to comprise a monosialyl-biantennary sugar chain with additional fucosylation of the proximal N-acetylglucosamine.
7686446	3	89	theme	2-->Gal	743:749	arg1	1-->3					854:858	Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3	794:858	Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3	794:858	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	89	theme	2-->Gal	743:749	arg1	beta					864:867	Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2	730:882	beta	864:867	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	89	theme	2-->Gal	743:749	arg1	structures					666:675	the whole sugar chain structures	644:675	the whole sugar chain structures of human cord serum AFP	644:699	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	90	dep	beta	1066:1069	arg1	beta					1132:1135	Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta	1092:1135	Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3	1092:1156	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	90	dep	beta	1066:1069	arg1	alpha					1080:1084	1-->2Man alpha 1-->6	1071:1090	Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)	1027:1157	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	91	theme	small	571:575	arg1	isoform					604:610	HCC-specific AFP isoform	587:610	HCC-specific AFP isoform	587:610	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	91	theme	small	571:575	arg1	amount					577:582	a small amount	569:582	a small amount of HCC-specific AFP isoform	569:610	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	6	92	gly	fucosylation	1787:1798	arg1	AFP					1803:1805	AFP	1803:1805	AFP in HCC	1803:1812	Fucosylation of AFP produced in fetal liver increased in inverse proportion to the gestation period, in weeks, indicating that fucosylation of AFP in HCC may be related to the dedifferentiation of human hepatocytes through malignant transformation.
7686446	3	93	theme	Neu5Ac	730:735	arg1	1-->3					854:858	Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3	794:858	Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3	794:858	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	93	theme	Neu5Ac	730:735	arg1	beta					864:867	Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2	730:882	beta	864:867	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	93	theme	Neu5Ac	730:735	arg1	structures					666:675	the whole sugar chain structures	644:675	the whole sugar chain structures of human cord serum AFP	644:699	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	94	dep	beta	864:867	arg1	1-->4R1					869:875	1-->4R1	869:875	1-->4R1	869:875	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	95	theme	beta	817:820	arg1	beta					834:837	Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta	794:837	Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3	794:858	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	6	96	from	AFP	1803:1805	arg1	HCC					1810:1812	HCC	1810:1812	HCC	1810:1812	Fucosylation of AFP produced in fetal liver increased in inverse proportion to the gestation period, in weeks, indicating that fucosylation of AFP in HCC may be related to the dedifferentiation of human hepatocytes through malignant transformation.
7686446	3	97	theme	1-->2Man	773:780	arg1	1-->3					854:858	Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3	794:858	Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3	794:858	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	97	theme	1-->2Man	773:780	arg1	beta					864:867	Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2	730:882	beta	864:867	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	97	theme	1-->2Man	773:780	arg1	structures					666:675	the whole sugar chain structures	644:675	the whole sugar chain structures of human cord serum AFP	644:699	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	98	theme	AFP	600:602	arg1	isoform					604:610	HCC-specific AFP isoform	587:610	HCC-specific AFP isoform	587:610	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	99	from	1-->4R1	1167:1173	arg1	ratio					1189:1193	the ratio	1185:1193	the ratio of 81.6:8.9:9.5	1185:1209	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	2	100	theme	HCC-specific	481:492	arg1	isoform					498:504	the HCC-specific AFP isoform	477:504	the HCC-specific AFP isoform	477:504	AFP produced in HCC and benign liver diseases was separated into several isoforms corresponding to different sugar chain structures by several types of lectin affinity electrophoresis, and the HCC-specific AFP isoform was discriminated from those of benign liver diseases.
7686446	6	101	from	HCC	1810:1812	arg1	fucosylation					1787:1798	fucosylation	1787:1798	fucosylation of AFP in HCC	1787:1812	Fucosylation of AFP produced in fetal liver increased in inverse proportion to the gestation period, in weeks, indicating that fucosylation of AFP in HCC may be related to the dedifferentiation of human hepatocytes through malignant transformation.
7686446	3	102	theme	1-->4GlcNAc	756:766	arg1	1-->3					854:858	Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3	794:858	Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3	794:858	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	102	theme	1-->4GlcNAc	756:766	arg1	beta					864:867	Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2	730:882	beta	864:867	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	102	theme	1-->4GlcNAc	756:766	arg1	structures					666:675	the whole sugar chain structures	644:675	the whole sugar chain structures of human cord serum AFP	644:699	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	0	103	theme	sugar	80:84	arg1	chains					86:91	N-linked sugar chains	71:91	N-linked sugar chains of glycoproteins produced in human liver and hepatocellular carcinomas	71:162	Sugar chains of human cord serum alpha-fetoprotein: characteristics of N-linked sugar chains of glycoproteins produced in human liver and hepatocellular carcinomas.
7686446	3	104	from	R2	1179:1180	arg1	ratio					1189:1193	the ratio	1185:1193	the ratio of 81.6:8.9:9.5	1185:1209	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	105	theme	alpha	848:852	arg1	1-->3					854:858	Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3	794:858	Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3	794:858	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	105	theme	alpha	848:852	arg1	beta					864:867	Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2	730:882	beta	864:867	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	6	106	gly	Fucosylation	1660:1671	arg1	AFP					1676:1678	AFP	1676:1678	AFP produced in fetal liver	1676:1702	Fucosylation of AFP produced in fetal liver increased in inverse proportion to the gestation period, in weeks, indicating that fucosylation of AFP in HCC may be related to the dedifferentiation of human hepatocytes through malignant transformation.
7686446	3	107	theme	Neu5Ac	794:799	arg1	beta					834:837	Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta	794:837	Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3	794:858	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	108	dep	follows	721:727	arg1	R2					1179:1180	R2	1179:1180	R2	1179:1180	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	108	dep	follows	721:727	arg1	1-->4R1					1167:1173	Man beta 1-->4R1	1158:1173	Man beta 1-->4R1	1158:1173	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	109	theme	alpha	986:990	arg1	beta					906:909	Gal beta 1-->4GlcNAc beta	885:909	Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)	885:997	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	109	theme	alpha	986:990	arg1	1-->3					992:996	Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3	932:996	Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3	932:996	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	110	theme	beta	834:837	arg1	1-->3					854:858	Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3	794:858	Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3	794:858	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	110	theme	beta	834:837	arg1	beta					864:867	Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2	730:882	beta	864:867	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	6	111	from	fucosylation	1787:1798	arg1	HCC					1810:1812	HCC	1810:1812	HCC	1810:1812	Fucosylation of AFP produced in fetal liver increased in inverse proportion to the gestation period, in weeks, indicating that fucosylation of AFP in HCC may be related to the dedifferentiation of human hepatocytes through malignant transformation.
7686446	6	112	theme	malignant	1883:1891	arg1	transformation					1893:1906	malignant transformation	1883:1906	malignant transformation	1883:1906	Fucosylation of AFP produced in fetal liver increased in inverse proportion to the gestation period, in weeks, indicating that fucosylation of AFP in HCC may be related to the dedifferentiation of human hepatocytes through malignant transformation.
7686446	3	113	theme	1-->6	788:792	arg1	1-->3					854:858	Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3	794:858	Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3	794:858	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	113	theme	1-->6	788:792	arg1	beta					864:867	Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2	730:882	beta	864:867	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	113	theme	1-->6	788:792	arg1	structures					666:675	the whole sugar chain structures	644:675	the whole sugar chain structures of human cord serum AFP	644:699	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	4	114	theme	GlcNAc	1319:1324	arg1	1-->4					1331:1335	GlcNAc beta 1-->4	1319:1335	GlcNAc beta 1-->4(Fuc alpha 1-->6)	1319:1352	R1 and R2 denote GlcNAc beta 1-->4GlcNAcOT (subscript OT represents an NaB3H4-reduced oligosaccharide) and GlcNAc beta 1-->4(Fuc alpha 1-->6)GlcNAcOT, respectively, and the ratio between R1 and R2 in the respective fractions was approximately 19:1.
7686446	4	114	theme	GlcNAc	1319:1324	arg1	alpha					1341:1345	Fuc alpha 1-->6	1337:1351	Fuc alpha 1-->6	1337:1351	R1 and R2 denote GlcNAc beta 1-->4GlcNAcOT (subscript OT represents an NaB3H4-reduced oligosaccharide) and GlcNAc beta 1-->4(Fuc alpha 1-->6)GlcNAcOT, respectively, and the ratio between R1 and R2 in the respective fractions was approximately 19:1.
7686446	6	115	theme	hepatocytes	1863:1873	arg1	dedifferentiation					1836:1852	the dedifferentiation	1832:1852	the dedifferentiation of human hepatocytes through malignant transformation	1832:1906	Fucosylation of AFP produced in fetal liver increased in inverse proportion to the gestation period, in weeks, indicating that fucosylation of AFP in HCC may be related to the dedifferentiation of human hepatocytes through malignant transformation.
7686446	6	116	theme	fetal	1692:1696	arg1	liver					1698:1702	fetal liver	1692:1702	fetal liver	1692:1702	Fucosylation of AFP produced in fetal liver increased in inverse proportion to the gestation period, in weeks, indicating that fucosylation of AFP in HCC may be related to the dedifferentiation of human hepatocytes through malignant transformation.
7686446	2	117	theme	several	353:359	arg1	isoforms					361:368	several isoforms	353:368	several isoforms corresponding to different sugar chain structures by several types of lectin affinity electrophoresis	353:470	AFP produced in HCC and benign liver diseases was separated into several isoforms corresponding to different sugar chain structures by several types of lectin affinity electrophoresis, and the HCC-specific AFP isoform was discriminated from those of benign liver diseases.
7686446	0	118	theme	human	16:20	arg1	alpha-fetoprotein					33:49	human cord serum alpha-fetoprotein	16:49	human cord serum alpha-fetoprotein	16:49	Sugar chains of human cord serum alpha-fetoprotein: characteristics of N-linked sugar chains of glycoproteins produced in human liver and hepatocellular carcinomas.
7686446	1	119	theme	benign	265:270	arg1	diseases					278:285	benign liver diseases	265:285	not only hepatocellular carcinoma (HCC) but also benign liver diseases	216:285	Human serum alpha-fetoprotein (AFP) is elevated in not only hepatocellular carcinoma (HCC) but also benign liver diseases.
7686446	3	120	theme	Neu5Ac	1027:1032	arg1	structures					666:675	the whole sugar chain structures	644:675	the whole sugar chain structures of human cord serum AFP	644:699	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	120	theme	Neu5Ac	1027:1032	arg1	beta					1066:1069	Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta	1027:1069	Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)	1027:1157	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	0	121	gly	glycoproteins	96:108	arg1	glycoproteins					96:108	glycoproteins	96:108	glycoproteins produced in human liver and hepatocellular carcinomas	96:162	Sugar chains of human cord serum alpha-fetoprotein: characteristics of N-linked sugar chains of glycoproteins produced in human liver and hepatocellular carcinomas.
7686446	5	122	gly	fucosylation	1610:1621	arg1	N-acetylglucosamine					1639:1657	the proximal N-acetylglucosamine	1626:1657	the proximal N-acetylglucosamine	1626:1657	In contrast, the sugar chain structure of HCC highly specific AFP isoform was found to comprise a monosialyl-biantennary sugar chain with additional fucosylation of the proximal N-acetylglucosamine.
7686446	5	122	gly	fucosylation	1610:1621	arg1	chain					1588:1592	a monosialyl-biantennary sugar chain	1557:1592	a monosialyl-biantennary sugar chain with additional fucosylation of the proximal N-acetylglucosamine	1557:1657	In contrast, the sugar chain structure of HCC highly specific AFP isoform was found to comprise a monosialyl-biantennary sugar chain with additional fucosylation of the proximal N-acetylglucosamine.
7686446	3	123	theme	serum	633:637	arg1	AFP					639:641	cord serum AFP	628:641	cord serum AFP	628:641	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	2	124	theme	chain	403:407	arg1	structures					409:418	different sugar chain structures	387:418	different sugar chain structures by several types of lectin affinity electrophoresis	387:470	AFP produced in HCC and benign liver diseases was separated into several isoforms corresponding to different sugar chain structures by several types of lectin affinity electrophoresis, and the HCC-specific AFP isoform was discriminated from those of benign liver diseases.
7686446	0	125	theme	serum	27:31	arg1	alpha-fetoprotein					33:49	human cord serum alpha-fetoprotein	16:49	human cord serum alpha-fetoprotein	16:49	Sugar chains of human cord serum alpha-fetoprotein: characteristics of N-linked sugar chains of glycoproteins produced in human liver and hepatocellular carcinomas.
7686446	2	126	theme	electrophoresis	456:470	arg1	types					431:435	several types	423:435	several types of lectin affinity electrophoresis	423:470	AFP produced in HCC and benign liver diseases was separated into several isoforms corresponding to different sugar chain structures by several types of lectin affinity electrophoresis, and the HCC-specific AFP isoform was discriminated from those of benign liver diseases.
7686446	2	127	theme	different	387:395	arg1	structures					409:418	different sugar chain structures	387:418	different sugar chain structures by several types of lectin affinity electrophoresis	387:470	AFP produced in HCC and benign liver diseases was separated into several isoforms corresponding to different sugar chain structures by several types of lectin affinity electrophoresis, and the HCC-specific AFP isoform was discriminated from those of benign liver diseases.
7686446	3	128	theme	1-->4GlcNAc	1054:1064	arg1	structures					666:675	the whole sugar chain structures	644:675	the whole sugar chain structures of human cord serum AFP	644:699	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	128	theme	1-->4GlcNAc	1054:1064	arg1	beta					1066:1069	Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta	1027:1069	Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)	1027:1157	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	129	theme	beta	906:909	arg1	structures					666:675	the whole sugar chain structures	644:675	the whole sugar chain structures of human cord serum AFP	644:699	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	129	theme	beta	906:909	arg1	beta					1002:1005	Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2	885:1020	beta	1002:1005	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	2	130	theme	lectin	440:445	arg1	electrophoresis					456:470	lectin affinity electrophoresis	440:470	lectin affinity electrophoresis	440:470	AFP produced in HCC and benign liver diseases was separated into several isoforms corresponding to different sugar chain structures by several types of lectin affinity electrophoresis, and the HCC-specific AFP isoform was discriminated from those of benign liver diseases.
7686446	3	131	theme	whole	648:652	arg1	beta					1002:1005	Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2	885:1020	beta	1002:1005	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	131	theme	whole	648:652	arg1	beta					864:867	Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2	730:882	beta	864:867	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	131	theme	whole	648:652	arg1	structures					666:675	the whole sugar chain structures	644:675	the whole sugar chain structures of human cord serum AFP	644:699	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	131	theme	whole	648:652	arg1	follows					721:727	follows	721:727	follows	721:727	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	131	theme	whole	648:652	arg1	beta					1066:1069	Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta	1027:1069	Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)	1027:1157	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	2	132	theme	benign	312:317	arg1	diseases					325:332	benign liver diseases	312:332	benign liver diseases	312:332	AFP produced in HCC and benign liver diseases was separated into several isoforms corresponding to different sugar chain structures by several types of lectin affinity electrophoresis, and the HCC-specific AFP isoform was discriminated from those of benign liver diseases.
7686446	3	133	located	detected	616:623	arg2	isoform					604:610	HCC-specific AFP isoform	587:610	HCC-specific AFP isoform	587:610	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	133	located	detected	616:623	arg1	AFP					639:641	cord serum AFP	628:641	cord serum AFP	628:641	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	133	located	detected	616:623	arg2	amount					577:582	a small amount	569:582	a small amount of HCC-specific AFP isoform	569:610	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	134	theme	2-->3Gal	1040:1047	arg1	structures					666:675	the whole sugar chain structures	644:675	the whole sugar chain structures of human cord serum AFP	644:699	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	134	theme	2-->3Gal	1040:1047	arg1	beta					1066:1069	Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta	1027:1069	Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)	1027:1157	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	135	theme	beta	889:892	arg1	beta					906:909	Gal beta 1-->4GlcNAc beta	885:909	Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)	885:997	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	3	135	theme	beta	889:892	arg1	1-->3					992:996	Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3	932:996	Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3	932:996	Because a small amount of HCC-specific AFP isoform was detected in cord serum AFP, the whole sugar chain structures of human cord serum AFP were determined, as follows: Neu5Ac alpha 2-->Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2-->6Gal beta 1 -->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2, and Neu5Ac alpha 2-->3Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->6(Neu5Ac alpha 2 -->6Gal beta 1-->4GlcNAc beta 1-->2Man alpha 1-->3)Man beta 1-->4R1 and R2 in the ratio of 81.6:8.9:9.5.
7686446	6	136	theme	gestation	1743:1751	arg1	period					1753:1758	the gestation period	1739:1758	the gestation period	1739:1758	Fucosylation of AFP produced in fetal liver increased in inverse proportion to the gestation period, in weeks, indicating that fucosylation of AFP in HCC may be related to the dedifferentiation of human hepatocytes through malignant transformation.
7686446	5	137	located	found	1539:1543	arg2	structure					1490:1498	the sugar chain structure	1474:1498	the sugar chain structure of HCC highly specific AFP isoform	1474:1533	In contrast, the sugar chain structure of HCC highly specific AFP isoform was found to comprise a monosialyl-biantennary sugar chain with additional fucosylation of the proximal N-acetylglucosamine.
7686446	5	137	located	found	1539:1543	arg1	contrast					1464:1471	contrast	1464:1471	contrast	1464:1471	In contrast, the sugar chain structure of HCC highly specific AFP isoform was found to comprise a monosialyl-biantennary sugar chain with additional fucosylation of the proximal N-acetylglucosamine.
7686446	5	138	theme	proximal	1630:1637	arg1	N-acetylglucosamine					1639:1657	the proximal N-acetylglucosamine	1626:1657	the proximal N-acetylglucosamine	1626:1657	In contrast, the sugar chain structure of HCC highly specific AFP isoform was found to comprise a monosialyl-biantennary sugar chain with additional fucosylation of the proximal N-acetylglucosamine.
7686446	0	139	dep	chains	6:11	arg1	characteristics					52:66	characteristics	52:66	Sugar chains of human cord serum alpha-fetoprotein: characteristics of N-linked sugar chains of glycoproteins produced in human liver and hepatocellular carcinomas.	0:163	Sugar chains of human cord serum alpha-fetoprotein: characteristics of N-linked sugar chains of glycoproteins produced in human liver and hepatocellular carcinomas.
3139301	0	0	theme	regulation	100:109	arg1	mechanisms					70:79	mechanisms	70:79	mechanisms of transcriptional regulation	70:109	O-glycosylation of eukaryotic transcription factors: implications for mechanisms of transcriptional regulation.
3139301	5	1	theme	polypeptide	770:780	arg1	species					782:788	the polypeptide species	766:788	the polypeptide species within a particular family of closely related RNA polymerase II factors	766:860	In some cases, only a subset of the polypeptide species within a particular family of closely related RNA polymerase II factors appears to be glycosylated.
3139301	5	2	theme	polymerase	840:849	arg1	factors					854:860	closely related RNA polymerase II factors	820:860	closely related RNA polymerase II factors	820:860	In some cases, only a subset of the polypeptide species within a particular family of closely related RNA polymerase II factors appears to be glycosylated.
3139301	6	3	theme	activation	1017:1026	arg1	regulation					987:996	regulation	987:996	regulation	987:996	Our findings raise the possibility that O-linked GlcNAc residues play a role in the mechanism or regulation of transcriptional activation of RNA polymerase II.
3139301	6	3	theme	activation	1017:1026	arg1	mechanism					974:982	mechanism	974:982	mechanism	974:982	Our findings raise the possibility that O-linked GlcNAc residues play a role in the mechanism or regulation of transcriptional activation of RNA polymerase II.
3139301	0	4	theme	transcriptional	84:98	arg1	regulation					100:109	transcriptional regulation	84:109	transcriptional regulation	84:109	O-glycosylation of eukaryotic transcription factors: implications for mechanisms of transcriptional regulation.
3139301	4	5	theme	other	548:552	arg1	factors					586:592	many other RNA polymerase II transcription factors	543:592	many other RNA polymerase II transcription factors	543:592	Furthermore, many other RNA polymerase II transcription factors also bear terminal GlcNAc residues, whereas most nuclear proteins, including RNA polymerase I and III transcription factors tested, do not.
3139301	2	6	dep	polymerase	286:295	arg1	Sp1					321:323	transcription factor Sp1	300:323	the human RNA polymerase II transcription factor Sp1	272:323	Here we show that the human RNA polymerase II transcription factor Sp1 bears multiple O-linked N-acetylglucosamine (GlcNAc) monosaccharide residues.
3139301	4	7	theme	GlcNAc	613:618	arg1	residues					620:627	terminal GlcNAc residues	604:627	terminal GlcNAc residues	604:627	Furthermore, many other RNA polymerase II transcription factors also bear terminal GlcNAc residues, whereas most nuclear proteins, including RNA polymerase I and III transcription factors tested, do not.
3139301	4	8	theme	many	543:546	arg1	factors					586:592	many other RNA polymerase II transcription factors	543:592	many other RNA polymerase II transcription factors	543:592	Furthermore, many other RNA polymerase II transcription factors also bear terminal GlcNAc residues, whereas most nuclear proteins, including RNA polymerase I and III transcription factors tested, do not.
3139301	5	9	gly	glycosylated	876:887	arg1	subset					756:761	only a subset	749:761	only a subset of the polypeptide species within a particular family of closely related RNA polymerase II factors	749:860	In some cases, only a subset of the polypeptide species within a particular family of closely related RNA polymerase II factors appears to be glycosylated.
3139301	4	10	dep	bear	599:602	arg1	whereas					630:636	whereas	630:636	whereas	630:636	Furthermore, many other RNA polymerase II transcription factors also bear terminal GlcNAc residues, whereas most nuclear proteins, including RNA polymerase I and III transcription factors tested, do not.
3139301	2	11	theme	RNA	282:284	arg1	polymerase					286:295	the human RNA polymerase II transcription factor Sp1	272:323	the human RNA polymerase II transcription factor Sp1	272:323	Here we show that the human RNA polymerase II transcription factor Sp1 bears multiple O-linked N-acetylglucosamine (GlcNAc) monosaccharide residues.
3139301	2	12	theme	human	276:280	arg1	polymerase					286:295	the human RNA polymerase II transcription factor Sp1	272:323	the human RNA polymerase II transcription factor Sp1	272:323	Here we show that the human RNA polymerase II transcription factor Sp1 bears multiple O-linked N-acetylglucosamine (GlcNAc) monosaccharide residues.
3139301	1	13	theme	cell	192:195	arg1	surface					197:203	the cell surface	188:203	the cell surface	188:203	Glycosylation is often regarded as being restricted to proteins confined to the cell surface or within the lumen of intracellular organelles.
3139301	3	14	theme	lectin	407:412	arg1	agglutinin					425:434	The lectin wheat germ agglutinin	403:434	The lectin wheat germ agglutinin	403:434	The lectin wheat germ agglutinin specifically inhibits the transcriptional activation but not the DNA binding function of Sp1.
3139301	5	15	theme	species	782:788	arg1	subset					756:761	only a subset	749:761	only a subset of the polypeptide species within a particular family of closely related RNA polymerase II factors	749:860	In some cases, only a subset of the polypeptide species within a particular family of closely related RNA polymerase II factors appears to be glycosylated.
3139301	4	16	contain	bear	599:602	arg2	residues					620:627	terminal GlcNAc residues	604:627	terminal GlcNAc residues	604:627	Furthermore, many other RNA polymerase II transcription factors also bear terminal GlcNAc residues, whereas most nuclear proteins, including RNA polymerase I and III transcription factors tested, do not.
3139301	4	16	contain	bear	599:602	arg1	factors					586:592	many other RNA polymerase II transcription factors	543:592	many other RNA polymerase II transcription factors	543:592	Furthermore, many other RNA polymerase II transcription factors also bear terminal GlcNAc residues, whereas most nuclear proteins, including RNA polymerase I and III transcription factors tested, do not.
3139301	3	17	theme	wheat	414:418	arg1	agglutinin					425:434	The lectin wheat germ agglutinin	403:434	The lectin wheat germ agglutinin	403:434	The lectin wheat germ agglutinin specifically inhibits the transcriptional activation but not the DNA binding function of Sp1.
3139301	3	18	theme	transcriptional	462:476	arg1	activation					478:487	the transcriptional activation	458:487	the transcriptional activation but not the DNA binding function of Sp1	458:527	The lectin wheat germ agglutinin specifically inhibits the transcriptional activation but not the DNA binding function of Sp1.
3139301	0	19	theme	transcription	30:42	arg1	factors					44:50	eukaryotic transcription factors	19:50	eukaryotic transcription factors	19:50	O-glycosylation of eukaryotic transcription factors: implications for mechanisms of transcriptional regulation.
3139301	2	20	theme	factor	314:319	arg1	Sp1					321:323	transcription factor Sp1	300:323	the human RNA polymerase II transcription factor Sp1	272:323	Here we show that the human RNA polymerase II transcription factor Sp1 bears multiple O-linked N-acetylglucosamine (GlcNAc) monosaccharide residues.
3139301	3	21	theme	DNA	501:503	arg1	function					513:520	the DNA binding function	497:520	the transcriptional activation but not the DNA binding function of Sp1	458:527	The lectin wheat germ agglutinin specifically inhibits the transcriptional activation but not the DNA binding function of Sp1.
3139301	0	22	theme	eukaryotic	19:28	arg1	factors					44:50	eukaryotic transcription factors	19:50	eukaryotic transcription factors	19:50	O-glycosylation of eukaryotic transcription factors: implications for mechanisms of transcriptional regulation.
3139301	4	23	theme	terminal	604:611	arg1	residues					620:627	terminal GlcNAc residues	604:627	terminal GlcNAc residues	604:627	Furthermore, many other RNA polymerase II transcription factors also bear terminal GlcNAc residues, whereas most nuclear proteins, including RNA polymerase I and III transcription factors tested, do not.
3139301	4	24	theme	nuclear	643:649	arg1	polymerase					675:684	RNA polymerase I	671:686	RNA polymerase I	671:686	Furthermore, many other RNA polymerase II transcription factors also bear terminal GlcNAc residues, whereas most nuclear proteins, including RNA polymerase I and III transcription factors tested, do not.
3139301	4	24	theme	nuclear	643:649	arg1	proteins					651:658	most nuclear proteins	638:658	most nuclear proteins	638:658	Furthermore, many other RNA polymerase II transcription factors also bear terminal GlcNAc residues, whereas most nuclear proteins, including RNA polymerase I and III transcription factors tested, do not.
3139301	4	24	theme	nuclear	643:649	arg1	factors					710:716	III transcription factors	692:716	III transcription factors tested	692:723	Furthermore, many other RNA polymerase II transcription factors also bear terminal GlcNAc residues, whereas most nuclear proteins, including RNA polymerase I and III transcription factors tested, do not.
3139301	2	25	theme	transcription	300:312	arg1	Sp1					321:323	transcription factor Sp1	300:323	the human RNA polymerase II transcription factor Sp1	272:323	Here we show that the human RNA polymerase II transcription factor Sp1 bears multiple O-linked N-acetylglucosamine (GlcNAc) monosaccharide residues.
3139301	6	26	theme	O-linked	930:937	arg1	residues					946:953	O-linked GlcNAc residues	930:953	O-linked GlcNAc residues	930:953	Our findings raise the possibility that O-linked GlcNAc residues play a role in the mechanism or regulation of transcriptional activation of RNA polymerase II.
3139301	3	27	theme	binding	505:511	arg1	function					513:520	the DNA binding function	497:520	the transcriptional activation but not the DNA binding function of Sp1	458:527	The lectin wheat germ agglutinin specifically inhibits the transcriptional activation but not the DNA binding function of Sp1.
3139301	0	28	gly	O-glycosylation	0:14	arg1	factors					44:50	eukaryotic transcription factors	19:50	eukaryotic transcription factors	19:50	O-glycosylation of eukaryotic transcription factors: implications for mechanisms of transcriptional regulation.
3139301	4	29	theme	transcription	696:708	arg1	factors					710:716	III transcription factors	692:716	III transcription factors tested	692:723	Furthermore, many other RNA polymerase II transcription factors also bear terminal GlcNAc residues, whereas most nuclear proteins, including RNA polymerase I and III transcription factors tested, do not.
3139301	5	30	theme	factors	854:860	arg1	family					810:815	a particular family	797:815	a particular family of closely related RNA polymerase II factors	797:860	In some cases, only a subset of the polypeptide species within a particular family of closely related RNA polymerase II factors appears to be glycosylated.
3139301	0	31	theme	factors	44:50	arg1	O-glycosylation					0:14	O-glycosylation	0:14	O-glycosylation of eukaryotic transcription factors: implications for mechanisms of transcriptional regulation.	0:110	O-glycosylation of eukaryotic transcription factors: implications for mechanisms of transcriptional regulation.
3139301	4	32	theme	polymerase	558:567	arg1	factors					586:592	many other RNA polymerase II transcription factors	543:592	many other RNA polymerase II transcription factors	543:592	Furthermore, many other RNA polymerase II transcription factors also bear terminal GlcNAc residues, whereas most nuclear proteins, including RNA polymerase I and III transcription factors tested, do not.
3139301	6	33	theme	transcriptional	1001:1015	arg1	activation					1017:1026	transcriptional activation	1001:1026	transcriptional activation of RNA polymerase II	1001:1047	Our findings raise the possibility that O-linked GlcNAc residues play a role in the mechanism or regulation of transcriptional activation of RNA polymerase II.
3139301	5	34	theme	related	828:834	arg1	factors					854:860	closely related RNA polymerase II factors	820:860	closely related RNA polymerase II factors	820:860	In some cases, only a subset of the polypeptide species within a particular family of closely related RNA polymerase II factors appears to be glycosylated.
3139301	3	35	theme	germ	420:423	arg1	agglutinin					425:434	The lectin wheat germ agglutinin	403:434	The lectin wheat germ agglutinin	403:434	The lectin wheat germ agglutinin specifically inhibits the transcriptional activation but not the DNA binding function of Sp1.
3139301	4	36	theme	RNA	554:556	arg1	factors					586:592	many other RNA polymerase II transcription factors	543:592	many other RNA polymerase II transcription factors	543:592	Furthermore, many other RNA polymerase II transcription factors also bear terminal GlcNAc residues, whereas most nuclear proteins, including RNA polymerase I and III transcription factors tested, do not.
3139301	3	37	theme	Sp1	525:527	arg1	function					513:520	the DNA binding function	497:520	the transcriptional activation but not the DNA binding function of Sp1	458:527	The lectin wheat germ agglutinin specifically inhibits the transcriptional activation but not the DNA binding function of Sp1.
3139301	4	38	theme	most	638:641	arg1	polymerase					675:684	RNA polymerase I	671:686	RNA polymerase I	671:686	Furthermore, many other RNA polymerase II transcription factors also bear terminal GlcNAc residues, whereas most nuclear proteins, including RNA polymerase I and III transcription factors tested, do not.
3139301	4	38	theme	most	638:641	arg1	proteins					651:658	most nuclear proteins	638:658	most nuclear proteins	638:658	Furthermore, many other RNA polymerase II transcription factors also bear terminal GlcNAc residues, whereas most nuclear proteins, including RNA polymerase I and III transcription factors tested, do not.
3139301	4	38	theme	most	638:641	arg1	factors					710:716	III transcription factors	692:716	III transcription factors tested	692:723	Furthermore, many other RNA polymerase II transcription factors also bear terminal GlcNAc residues, whereas most nuclear proteins, including RNA polymerase I and III transcription factors tested, do not.
3139301	4	39	theme	transcription	572:584	arg1	factors					586:592	many other RNA polymerase II transcription factors	543:592	many other RNA polymerase II transcription factors	543:592	Furthermore, many other RNA polymerase II transcription factors also bear terminal GlcNAc residues, whereas most nuclear proteins, including RNA polymerase I and III transcription factors tested, do not.
3139301	6	40	theme	GlcNAc	939:944	arg1	residues					946:953	O-linked GlcNAc residues	930:953	O-linked GlcNAc residues	930:953	Our findings raise the possibility that O-linked GlcNAc residues play a role in the mechanism or regulation of transcriptional activation of RNA polymerase II.
3139301	2	41	theme	N-acetylglucosamine	349:367	arg1	residues					393:400	multiple O-linked N-acetylglucosamine (GlcNAc) monosaccharide residues	331:400	multiple O-linked N-acetylglucosamine (GlcNAc) monosaccharide residues	331:400	Here we show that the human RNA polymerase II transcription factor Sp1 bears multiple O-linked N-acetylglucosamine (GlcNAc) monosaccharide residues.
3139301	2	42	contain	bears	325:329	arg1	polymerase					286:295	the human RNA polymerase II transcription factor Sp1	272:323	the human RNA polymerase II transcription factor Sp1	272:323	Here we show that the human RNA polymerase II transcription factor Sp1 bears multiple O-linked N-acetylglucosamine (GlcNAc) monosaccharide residues.
3139301	2	42	contain	bears	325:329	arg2	residues					393:400	multiple O-linked N-acetylglucosamine (GlcNAc) monosaccharide residues	331:400	multiple O-linked N-acetylglucosamine (GlcNAc) monosaccharide residues	331:400	Here we show that the human RNA polymerase II transcription factor Sp1 bears multiple O-linked N-acetylglucosamine (GlcNAc) monosaccharide residues.
3139301	6	43	theme	polymerase	1035:1044	arg1	activation					1017:1026	transcriptional activation	1001:1026	transcriptional activation of RNA polymerase II	1001:1047	Our findings raise the possibility that O-linked GlcNAc residues play a role in the mechanism or regulation of transcriptional activation of RNA polymerase II.
3139301	2	44	theme	O-linked	340:347	arg1	N-acetylglucosamine					349:367	O-linked N-acetylglucosamine	340:367	multiple O-linked N-acetylglucosamine (GlcNAc) monosaccharide residues	331:400	Here we show that the human RNA polymerase II transcription factor Sp1 bears multiple O-linked N-acetylglucosamine (GlcNAc) monosaccharide residues.
3139301	2	44	theme	O-linked	340:347	arg1	GlcNAc					370:375	GlcNAc	370:375	GlcNAc	370:375	Here we show that the human RNA polymerase II transcription factor Sp1 bears multiple O-linked N-acetylglucosamine (GlcNAc) monosaccharide residues.
3139301	1	45	theme	intracellular	228:240	arg1	organelles					242:251	intracellular organelles	228:251	intracellular organelles	228:251	Glycosylation is often regarded as being restricted to proteins confined to the cell surface or within the lumen of intracellular organelles.
3139301	5	46	theme	RNA	836:838	arg1	polymerase					840:849	RNA polymerase II	836:852	closely related RNA polymerase II factors	820:860	In some cases, only a subset of the polypeptide species within a particular family of closely related RNA polymerase II factors appears to be glycosylated.
3139301	2	47	theme	multiple	331:338	arg1	residues					393:400	multiple O-linked N-acetylglucosamine (GlcNAc) monosaccharide residues	331:400	multiple O-linked N-acetylglucosamine (GlcNAc) monosaccharide residues	331:400	Here we show that the human RNA polymerase II transcription factor Sp1 bears multiple O-linked N-acetylglucosamine (GlcNAc) monosaccharide residues.
3139301	1	48	theme	organelles	242:251	arg1	lumen					219:223	the lumen	215:223	the lumen of intracellular organelles	215:251	Glycosylation is often regarded as being restricted to proteins confined to the cell surface or within the lumen of intracellular organelles.
3139301	6	49	dep	mechanism	974:982	arg1	the					970:972	the	970:972	the	970:972	Our findings raise the possibility that O-linked GlcNAc residues play a role in the mechanism or regulation of transcriptional activation of RNA polymerase II.
3139301	4	50	theme	RNA	671:673	arg1	polymerase					675:684	RNA polymerase I	671:686	RNA polymerase I	671:686	Furthermore, many other RNA polymerase II transcription factors also bear terminal GlcNAc residues, whereas most nuclear proteins, including RNA polymerase I and III transcription factors tested, do not.
3139301	6	51	theme	RNA	1031:1033	arg1	polymerase					1035:1044	RNA polymerase II	1031:1047	RNA polymerase II	1031:1047	Our findings raise the possibility that O-linked GlcNAc residues play a role in the mechanism or regulation of transcriptional activation of RNA polymerase II.
3139301	5	52	theme	particular	799:808	arg1	family					810:815	a particular family	797:815	a particular family of closely related RNA polymerase II factors	797:860	In some cases, only a subset of the polypeptide species within a particular family of closely related RNA polymerase II factors appears to be glycosylated.
3139301	2	53	link	O-linked	340:347	arg1	N-acetylglucosamine					349:367	O-linked N-acetylglucosamine	340:367	multiple O-linked N-acetylglucosamine (GlcNAc) monosaccharide residues	331:400	Here we show that the human RNA polymerase II transcription factor Sp1 bears multiple O-linked N-acetylglucosamine (GlcNAc) monosaccharide residues.
3139301	2	53	link	O-linked	340:347	arg1	GlcNAc					370:375	GlcNAc	370:375	GlcNAc	370:375	Here we show that the human RNA polymerase II transcription factor Sp1 bears multiple O-linked N-acetylglucosamine (GlcNAc) monosaccharide residues.
3139301	0	54	dep	O-glycosylation	0:14	arg1	implications					53:64	implications	53:64	O-glycosylation of eukaryotic transcription factors: implications for mechanisms of transcriptional regulation.	0:110	O-glycosylation of eukaryotic transcription factors: implications for mechanisms of transcriptional regulation.
3139301	2	55	theme	monosaccharide	378:391	arg1	residues					393:400	multiple O-linked N-acetylglucosamine (GlcNAc) monosaccharide residues	331:400	multiple O-linked N-acetylglucosamine (GlcNAc) monosaccharide residues	331:400	Here we show that the human RNA polymerase II transcription factor Sp1 bears multiple O-linked N-acetylglucosamine (GlcNAc) monosaccharide residues.
3139301	6	56	link	O-linked	930:937	arg1	residues					946:953	O-linked GlcNAc residues	930:953	O-linked GlcNAc residues	930:953	Our findings raise the possibility that O-linked GlcNAc residues play a role in the mechanism or regulation of transcriptional activation of RNA polymerase II.
8404896	13	0	theme	own	1608:1610	arg1	transferase					1621:1631	its own O-GlcNAc transferase	1604:1631	its own O-GlcNAc transferase	1604:1631	Probing with a synthetic pentapeptide, we could show that P. falciparum expresses its own O-GlcNAc transferase during intraerythrocytic development.
8404896	11	1	theme	reducing	1400:1407	arg1	terminus					1409:1416	its reducing terminus	1396:1416	its reducing terminus	1396:1416	At least one O-glycan found in P. falciparum-infected erythrocytes contains GlcNAc at its reducing terminus.
8404896	7	2	theme	2-4-times	745:753	arg1	O-glycans					768:776	2-4-times more labeled O-glycans	745:776	2-4-times more labeled O-glycans	745:776	2-4-times more labeled O-glycans were obtained from infected erythrocytes compared to the same number of uninfected ones, consistent with additional biosynthesis by the parasite.
8404896	7	3	theme	ones	861:864	arg1	number					840:845	the same number	831:845	the same number of uninfected ones	831:864	2-4-times more labeled O-glycans were obtained from infected erythrocytes compared to the same number of uninfected ones, consistent with additional biosynthesis by the parasite.
8404896	7	4	theme	labeled	760:766	arg1	O-glycans					768:776	2-4-times more labeled O-glycans	745:776	2-4-times more labeled O-glycans	745:776	2-4-times more labeled O-glycans were obtained from infected erythrocytes compared to the same number of uninfected ones, consistent with additional biosynthesis by the parasite.
8404896	13	5	theme	synthetic	1537:1545	arg1	pentapeptide					1547:1558	a synthetic pentapeptide	1535:1558	a synthetic pentapeptide	1535:1558	Probing with a synthetic pentapeptide, we could show that P. falciparum expresses its own O-GlcNAc transferase during intraerythrocytic development.
8404896	13	6	theme	intraerythrocytic	1640:1656	arg1	development					1658:1668	intraerythrocytic development	1640:1668	intraerythrocytic development	1640:1668	Probing with a synthetic pentapeptide, we could show that P. falciparum expresses its own O-GlcNAc transferase during intraerythrocytic development.
8404896	5	7	theme	metabolically	441:453	arg1	O-glycans					475:483	Non-labeled and metabolically glucosamine-labeled O-glycans	425:483	Non-labeled and metabolically glucosamine-labeled O-glycans	425:483	Non-labeled and metabolically glucosamine-labeled O-glycans were obtained from the protein fraction of infected or uninfected erythrocytes by beta elimination.
8404896	15	8	from	function	1757:1764	arg1	falciparum					1784:1793	P. falciparum	1781:1793	P. falciparum	1781:1793	The localization and function of O-GlcNAc in P. falciparum remains to be elucidated.
8404896	0	9	from	Studies	0:6	arg1	O-glycans					11:19	O-glycans	11:19	O-glycans of Plasmodium-falciparum-infected human erythrocytes	11:72	Studies on O-glycans of Plasmodium-falciparum-infected human erythrocytes.
8404896	9	10	theme	red	1160:1162	arg1	cells					1164:1168	P. falciparum-infected red cells	1137:1168	P. falciparum-infected red cells	1137:1168	According to preliminary alditol analyses, the O-glycans of P. falciparum-infected red cells do not contain GalNAc at their reducing terminus.
8404896	5	11	theme	infected	528:535	arg1	erythrocytes					551:562	infected or uninfected erythrocytes	528:562	infected or uninfected erythrocytes	528:562	Non-labeled and metabolically glucosamine-labeled O-glycans were obtained from the protein fraction of infected or uninfected erythrocytes by beta elimination.
8404896	5	12	theme	glucosamine-labeled	455:473	arg1	O-glycans					475:483	Non-labeled and metabolically glucosamine-labeled O-glycans	425:483	Non-labeled and metabolically glucosamine-labeled O-glycans	425:483	Non-labeled and metabolically glucosamine-labeled O-glycans were obtained from the protein fraction of infected or uninfected erythrocytes by beta elimination.
8404896	6	13	theme	sodium	635:640	arg1	borohydride					642:652	sodium borohydride	635:652	sodium borohydride	635:652	Additional label was introduced by reduction with sodium borohydride, or by the attachment of radioactive Gal to peripheral GlcNAc using galactosyltransferase.
8404896	2	14	theme	protein	181:187	arg1	glycosylation					189:201	protein glycosylation	181:201	protein glycosylation	181:201	O-Glycosylation is the major form of protein glycosylation in human erythrocytes infected with the asexual intraerythrocytic stage of the malaria parasite.
8404896	8	15	theme	uninfected	1056:1065	arg1	cell					1071:1074	the uninfected red cell	1052:1074	the uninfected red cell	1052:1074	Our analysis of these O-glycans showed no significant qualitative divergence between the O-glycans of the infected and those of the uninfected red cell.
8404896	15	16	theme	O-GlcNAc	1769:1776	arg1	function					1757:1764	function	1757:1764	function	1757:1764	The localization and function of O-GlcNAc in P. falciparum remains to be elucidated.
8404896	15	16	theme	O-GlcNAc	1769:1776	arg1	localization					1740:1751	localization	1740:1751	localization	1740:1751	The localization and function of O-GlcNAc in P. falciparum remains to be elucidated.
8404896	7	17	theme	uninfected	850:859	arg1	ones					861:864	uninfected ones	850:864	uninfected ones	850:864	2-4-times more labeled O-glycans were obtained from infected erythrocytes compared to the same number of uninfected ones, consistent with additional biosynthesis by the parasite.
8404896	9	18	theme	preliminary	1090:1100	arg1	analyses					1110:1117	preliminary alditol analyses	1090:1117	preliminary alditol analyses	1090:1117	According to preliminary alditol analyses, the O-glycans of P. falciparum-infected red cells do not contain GalNAc at their reducing terminus.
8404896	8	19	theme	qualitative	978:988	arg1	divergence					990:999	no significant qualitative divergence	963:999	no significant qualitative divergence between the O-glycans of the infected and those of the uninfected red cell	963:1074	Our analysis of these O-glycans showed no significant qualitative divergence between the O-glycans of the infected and those of the uninfected red cell.
8404896	4	20	dep	falciparum-infected	376:394	arg1	P.					373:374	P. falciparum-infected and uninfected erythrocytes	373:422	P.	373:374	This study compares aspects of O-glycosylation in P. falciparum-infected and uninfected erythrocytes.
8404896	12	21	theme	Gel-filtration	1419:1432	arg1	results					1434:1440	Gel-filtration results	1419:1440	Gel-filtration results	1419:1440	Gel-filtration results had suggested the presence of O-GlcNAc on proteins in the infected erythrocyte.
8404896	9	22	theme	alditol	1102:1108	arg1	analyses					1110:1117	preliminary alditol analyses	1090:1117	preliminary alditol analyses	1090:1117	According to preliminary alditol analyses, the O-glycans of P. falciparum-infected red cells do not contain GalNAc at their reducing terminus.
8404896	3	23	theme	Plasmodium	300:309	arg1	falciparum					311:320	Plasmodium falciparum	300:320	Plasmodium falciparum.	300:321	Plasmodium falciparum.
8404896	4	24	theme	O-glycosylation	354:368	arg1	aspects					343:349	aspects	343:349	aspects of O-glycosylation in P. falciparum-infected and uninfected erythrocytes	343:422	This study compares aspects of O-glycosylation in P. falciparum-infected and uninfected erythrocytes.
8404896	12	25	from	presence	1460:1467	arg1	proteins					1484:1491	proteins	1484:1491	proteins in the infected erythrocyte	1484:1519	Gel-filtration results had suggested the presence of O-GlcNAc on proteins in the infected erythrocyte.
8404896	6	26	theme	using	716:720	arg1	galactosyltransferase					722:742	peripheral GlcNAc using galactosyltransferase	698:742	peripheral GlcNAc using galactosyltransferase	698:742	Additional label was introduced by reduction with sodium borohydride, or by the attachment of radioactive Gal to peripheral GlcNAc using galactosyltransferase.
8404896	2	27	theme	major	167:171	arg1	form					173:176	the major form	163:176	the major form of protein glycosylation in human erythrocytes infected with the asexual intraerythrocytic stage of the malaria parasite	163:297	O-Glycosylation is the major form of protein glycosylation in human erythrocytes infected with the asexual intraerythrocytic stage of the malaria parasite.
8404896	2	27	theme	major	167:171	arg1	O-Glycosylation					144:158	O-Glycosylation	144:158	O-Glycosylation	144:158	O-Glycosylation is the major form of protein glycosylation in human erythrocytes infected with the asexual intraerythrocytic stage of the malaria parasite.
8404896	12	28	theme	infected	1500:1507	arg1	erythrocyte					1509:1519	the infected erythrocyte	1496:1519	the infected erythrocyte	1496:1519	Gel-filtration results had suggested the presence of O-GlcNAc on proteins in the infected erythrocyte.
8404896	4	29	from	aspects	343:349	arg1	falciparum-infected					376:394	falciparum-infected	376:394	falciparum-infected	376:394	This study compares aspects of O-glycosylation in P. falciparum-infected and uninfected erythrocytes.
8404896	4	29	from	aspects	343:349	arg1	erythrocytes					411:422	P. falciparum-infected and uninfected erythrocytes	373:422	erythrocytes	411:422	This study compares aspects of O-glycosylation in P. falciparum-infected and uninfected erythrocytes.
8404896	6	30	theme	GlcNAc	709:714	arg1	galactosyltransferase					722:742	peripheral GlcNAc using galactosyltransferase	698:742	peripheral GlcNAc using galactosyltransferase	698:742	Additional label was introduced by reduction with sodium borohydride, or by the attachment of radioactive Gal to peripheral GlcNAc using galactosyltransferase.
8404896	5	31	theme	beta	567:570	arg1	elimination					572:582	beta elimination	567:582	beta elimination	567:582	Non-labeled and metabolically glucosamine-labeled O-glycans were obtained from the protein fraction of infected or uninfected erythrocytes by beta elimination.
8404896	6	32	theme	peripheral	698:707	arg1	galactosyltransferase					722:742	peripheral GlcNAc using galactosyltransferase	698:742	peripheral GlcNAc using galactosyltransferase	698:742	Additional label was introduced by reduction with sodium borohydride, or by the attachment of radioactive Gal to peripheral GlcNAc using galactosyltransferase.
8404896	6	33	dep	Additional	585:594	arg1	label					596:600	label	596:600	label	596:600	Additional label was introduced by reduction with sodium borohydride, or by the attachment of radioactive Gal to peripheral GlcNAc using galactosyltransferase.
8404896	1	34	theme	malaria	125:131	arg1	parasites					133:141	malaria parasites	125:141	malaria parasites	125:141	Evidence for O-GlcNAc and O-GlcNAc-transferase in malaria parasites.
8404896	6	35	with	reduction	620:628	arg1	borohydride					642:652	sodium borohydride	635:652	sodium borohydride	635:652	Additional label was introduced by reduction with sodium borohydride, or by the attachment of radioactive Gal to peripheral GlcNAc using galactosyltransferase.
8404896	15	36	dep	localization	1740:1751	arg1	The					1736:1738	The	1736:1738	The	1736:1738	The localization and function of O-GlcNAc in P. falciparum remains to be elucidated.
8404896	11	37	theme	P.	1341:1342	arg1	erythrocytes					1364:1375	P. falciparum-infected erythrocytes	1341:1375	P. falciparum-infected erythrocytes	1341:1375	At least one O-glycan found in P. falciparum-infected erythrocytes contains GlcNAc at its reducing terminus.
8404896	7	38	theme	same	835:838	arg1	number					840:845	the same number	831:845	the same number of uninfected ones	831:864	2-4-times more labeled O-glycans were obtained from infected erythrocytes compared to the same number of uninfected ones, consistent with additional biosynthesis by the parasite.
8404896	6	39	theme	Gal	691:693	arg1	attachment					665:674	the attachment	661:674	the attachment of radioactive Gal to peripheral GlcNAc using galactosyltransferase	661:742	Additional label was introduced by reduction with sodium borohydride, or by the attachment of radioactive Gal to peripheral GlcNAc using galactosyltransferase.
8404896	8	40	theme	those	1043:1047	arg1	O-glycans					1013:1021	the O-glycans	1009:1021	the O-glycans of the infected and those of the uninfected red cell	1009:1074	Our analysis of these O-glycans showed no significant qualitative divergence between the O-glycans of the infected and those of the uninfected red cell.
8404896	2	41	from	form	173:176	arg1	erythrocytes					212:223	human erythrocytes	206:223	human erythrocytes infected with the asexual intraerythrocytic stage of the malaria parasite	206:297	O-Glycosylation is the major form of protein glycosylation in human erythrocytes infected with the asexual intraerythrocytic stage of the malaria parasite.
8404896	5	42	theme	Non-labeled	425:435	arg1	O-glycans					475:483	Non-labeled and metabolically glucosamine-labeled O-glycans	425:483	Non-labeled and metabolically glucosamine-labeled O-glycans	425:483	Non-labeled and metabolically glucosamine-labeled O-glycans were obtained from the protein fraction of infected or uninfected erythrocytes by beta elimination.
8404896	2	43	theme	human	206:210	arg1	erythrocytes					212:223	human erythrocytes	206:223	human erythrocytes infected with the asexual intraerythrocytic stage of the malaria parasite	206:297	O-Glycosylation is the major form of protein glycosylation in human erythrocytes infected with the asexual intraerythrocytic stage of the malaria parasite.
8404896	11	44	located	found	1332:1336	arg1	erythrocytes					1364:1375	P. falciparum-infected erythrocytes	1341:1375	P. falciparum-infected erythrocytes	1341:1375	At least one O-glycan found in P. falciparum-infected erythrocytes contains GlcNAc at its reducing terminus.
8404896	11	44	located	found	1332:1336	arg2	O-glycan					1323:1330	At least one O-glycan	1310:1330	At least one O-glycan found in P. falciparum-infected erythrocytes	1310:1375	At least one O-glycan found in P. falciparum-infected erythrocytes contains GlcNAc at its reducing terminus.
8404896	0	45	theme	Plasmodium-falciparum-infected	24:53	arg1	erythrocytes					61:72	Plasmodium-falciparum-infected human erythrocytes	24:72	Plasmodium-falciparum-infected human erythrocytes	24:72	Studies on O-glycans of Plasmodium-falciparum-infected human erythrocytes.
8404896	6	46	theme	radioactive	679:689	arg1	Gal					691:693	radioactive Gal	679:693	radioactive Gal	679:693	Additional label was introduced by reduction with sodium borohydride, or by the attachment of radioactive Gal to peripheral GlcNAc using galactosyltransferase.
8404896	5	47	theme	erythrocytes	551:562	arg1	fraction					516:523	the protein fraction	504:523	the protein fraction of infected or uninfected erythrocytes	504:562	Non-labeled and metabolically glucosamine-labeled O-glycans were obtained from the protein fraction of infected or uninfected erythrocytes by beta elimination.
8404896	8	48	theme	red	1067:1069	arg1	cell					1071:1074	the uninfected red cell	1052:1074	the uninfected red cell	1052:1074	Our analysis of these O-glycans showed no significant qualitative divergence between the O-glycans of the infected and those of the uninfected red cell.
8404896	13	49	theme	O-GlcNAc	1612:1619	arg1	transferase					1621:1631	its own O-GlcNAc transferase	1604:1631	its own O-GlcNAc transferase	1604:1631	Probing with a synthetic pentapeptide, we could show that P. falciparum expresses its own O-GlcNAc transferase during intraerythrocytic development.
8404896	9	50	theme	falciparum-infected	1140:1158	arg1	cells					1164:1168	P. falciparum-infected red cells	1137:1168	P. falciparum-infected red cells	1137:1168	According to preliminary alditol analyses, the O-glycans of P. falciparum-infected red cells do not contain GalNAc at their reducing terminus.
8404896	2	51	theme	glycosylation	189:201	arg1	form					173:176	the major form	163:176	the major form of protein glycosylation in human erythrocytes infected with the asexual intraerythrocytic stage of the malaria parasite	163:297	O-Glycosylation is the major form of protein glycosylation in human erythrocytes infected with the asexual intraerythrocytic stage of the malaria parasite.
8404896	2	51	theme	glycosylation	189:201	arg1	O-Glycosylation					144:158	O-Glycosylation	144:158	O-Glycosylation	144:158	O-Glycosylation is the major form of protein glycosylation in human erythrocytes infected with the asexual intraerythrocytic stage of the malaria parasite.
8404896	15	52	from	localization	1740:1751	arg1	falciparum					1784:1793	P. falciparum	1781:1793	P. falciparum	1781:1793	The localization and function of O-GlcNAc in P. falciparum remains to be elucidated.
8404896	4	53	theme	uninfected	400:409	arg1	erythrocytes					411:422	P. falciparum-infected and uninfected erythrocytes	373:422	erythrocytes	411:422	This study compares aspects of O-glycosylation in P. falciparum-infected and uninfected erythrocytes.
8404896	0	54	theme	erythrocytes	61:72	arg1	O-glycans					11:19	O-glycans	11:19	O-glycans of Plasmodium-falciparum-infected human erythrocytes	11:72	Studies on O-glycans of Plasmodium-falciparum-infected human erythrocytes.
8404896	8	55	theme	significant	966:976	arg1	divergence					990:999	no significant qualitative divergence	963:999	no significant qualitative divergence between the O-glycans of the infected and those of the uninfected red cell	963:1074	Our analysis of these O-glycans showed no significant qualitative divergence between the O-glycans of the infected and those of the uninfected red cell.
8404896	2	56	theme	asexual	243:249	arg1	stage					269:273	the asexual intraerythrocytic stage	239:273	the asexual intraerythrocytic stage of the malaria parasite	239:297	O-Glycosylation is the major form of protein glycosylation in human erythrocytes infected with the asexual intraerythrocytic stage of the malaria parasite.
8404896	2	57	theme	intraerythrocytic	251:267	arg1	stage					269:273	the asexual intraerythrocytic stage	239:273	the asexual intraerythrocytic stage of the malaria parasite	239:297	O-Glycosylation is the major form of protein glycosylation in human erythrocytes infected with the asexual intraerythrocytic stage of the malaria parasite.
8404896	6	58	attach	attachment	665:674	arg1	galactosyltransferase					722:742	peripheral GlcNAc using galactosyltransferase	698:742	peripheral GlcNAc using galactosyltransferase	698:742	Additional label was introduced by reduction with sodium borohydride, or by the attachment of radioactive Gal to peripheral GlcNAc using galactosyltransferase.
8404896	6	58	attach	attachment	665:674	arg2	Gal					691:693	radioactive Gal	679:693	radioactive Gal	679:693	Additional label was introduced by reduction with sodium borohydride, or by the attachment of radioactive Gal to peripheral GlcNAc using galactosyltransferase.
8404896	9	59	theme	P.	1137:1138	arg1	cells					1164:1168	P. falciparum-infected red cells	1137:1168	P. falciparum-infected red cells	1137:1168	According to preliminary alditol analyses, the O-glycans of P. falciparum-infected red cells do not contain GalNAc at their reducing terminus.
8404896	9	60	theme	cells	1164:1168	arg1	O-glycans					1124:1132	the O-glycans	1120:1132	the O-glycans of P. falciparum-infected red cells	1120:1168	According to preliminary alditol analyses, the O-glycans of P. falciparum-infected red cells do not contain GalNAc at their reducing terminus.
8404896	12	61	from	proteins	1484:1491	arg1	erythrocyte					1509:1519	the infected erythrocyte	1496:1519	the infected erythrocyte	1496:1519	Gel-filtration results had suggested the presence of O-GlcNAc on proteins in the infected erythrocyte.
8404896	9	62	contain	contain	1177:1183	arg1	terminus					1210:1217	their reducing terminus	1195:1217	their reducing terminus	1195:1217	According to preliminary alditol analyses, the O-glycans of P. falciparum-infected red cells do not contain GalNAc at their reducing terminus.
8404896	9	62	contain	contain	1177:1183	arg1	O-glycans					1124:1132	the O-glycans	1120:1132	the O-glycans of P. falciparum-infected red cells	1120:1168	According to preliminary alditol analyses, the O-glycans of P. falciparum-infected red cells do not contain GalNAc at their reducing terminus.
8404896	9	62	contain	contain	1177:1183	arg2	O-glycans					1124:1132	the O-glycans	1120:1132	the O-glycans of P. falciparum-infected red cells	1120:1168	According to preliminary alditol analyses, the O-glycans of P. falciparum-infected red cells do not contain GalNAc at their reducing terminus.
8404896	9	62	contain	contain	1177:1183	arg2	GalNAc					1185:1190	GalNAc	1185:1190	GalNAc	1185:1190	According to preliminary alditol analyses, the O-glycans of P. falciparum-infected red cells do not contain GalNAc at their reducing terminus.
8404896	11	63	theme	falciparum-infected	1344:1362	arg1	erythrocytes					1364:1375	P. falciparum-infected erythrocytes	1341:1375	P. falciparum-infected erythrocytes	1341:1375	At least one O-glycan found in P. falciparum-infected erythrocytes contains GlcNAc at its reducing terminus.
8404896	12	64	theme	O-GlcNAc	1472:1479	arg1	presence					1460:1467	the presence	1456:1467	the presence of O-GlcNAc on proteins in the infected erythrocyte	1456:1519	Gel-filtration results had suggested the presence of O-GlcNAc on proteins in the infected erythrocyte.
8404896	0	65	theme	human	55:59	arg1	erythrocytes					61:72	Plasmodium-falciparum-infected human erythrocytes	24:72	Plasmodium-falciparum-infected human erythrocytes	24:72	Studies on O-glycans of Plasmodium-falciparum-infected human erythrocytes.
8404896	5	66	theme	uninfected	540:549	arg1	erythrocytes					551:562	infected or uninfected erythrocytes	528:562	infected or uninfected erythrocytes	528:562	Non-labeled and metabolically glucosamine-labeled O-glycans were obtained from the protein fraction of infected or uninfected erythrocytes by beta elimination.
8404896	7	67	theme	additional	883:892	arg1	biosynthesis					894:905	additional biosynthesis	883:905	additional biosynthesis by the parasite	883:921	2-4-times more labeled O-glycans were obtained from infected erythrocytes compared to the same number of uninfected ones, consistent with additional biosynthesis by the parasite.
8404896	7	68	with	consistent	867:876	arg1	biosynthesis					894:905	additional biosynthesis	883:905	additional biosynthesis by the parasite	883:921	2-4-times more labeled O-glycans were obtained from infected erythrocytes compared to the same number of uninfected ones, consistent with additional biosynthesis by the parasite.
8404896	11	69	contain	contains	1377:1384	arg2	GlcNAc					1386:1391	GlcNAc	1386:1391	GlcNAc	1386:1391	At least one O-glycan found in P. falciparum-infected erythrocytes contains GlcNAc at its reducing terminus.
8404896	11	69	contain	contains	1377:1384	arg2	O-glycan					1323:1330	At least one O-glycan	1310:1330	At least one O-glycan found in P. falciparum-infected erythrocytes	1310:1375	At least one O-glycan found in P. falciparum-infected erythrocytes contains GlcNAc at its reducing terminus.
8404896	11	69	contain	contains	1377:1384	arg1	O-glycan					1323:1330	At least one O-glycan	1310:1330	At least one O-glycan found in P. falciparum-infected erythrocytes	1310:1375	At least one O-glycan found in P. falciparum-infected erythrocytes contains GlcNAc at its reducing terminus.
8404896	11	69	contain	contains	1377:1384	arg1	terminus					1409:1416	its reducing terminus	1396:1416	its reducing terminus	1396:1416	At least one O-glycan found in P. falciparum-infected erythrocytes contains GlcNAc at its reducing terminus.
8404896	1	70	from	O-GlcNAc-transferase	101:120	arg1	parasites					133:141	malaria parasites	125:141	malaria parasites	125:141	Evidence for O-GlcNAc and O-GlcNAc-transferase in malaria parasites.
8404896	8	71	theme	infected	1030:1037	arg1	O-glycans					1013:1021	the O-glycans	1009:1021	the O-glycans of the infected and those of the uninfected red cell	1009:1074	Our analysis of these O-glycans showed no significant qualitative divergence between the O-glycans of the infected and those of the uninfected red cell.
8404896	7	72	theme	infected	797:804	arg1	erythrocytes					806:817	infected erythrocytes	797:817	infected erythrocytes	797:817	2-4-times more labeled O-glycans were obtained from infected erythrocytes compared to the same number of uninfected ones, consistent with additional biosynthesis by the parasite.
8404896	2	73	theme	parasite	290:297	arg1	stage					269:273	the asexual intraerythrocytic stage	239:273	the asexual intraerythrocytic stage of the malaria parasite	239:297	O-Glycosylation is the major form of protein glycosylation in human erythrocytes infected with the asexual intraerythrocytic stage of the malaria parasite.
8404896	1	74	from	O-GlcNAc	88:95	arg1	parasites					133:141	malaria parasites	125:141	malaria parasites	125:141	Evidence for O-GlcNAc and O-GlcNAc-transferase in malaria parasites.
8404896	8	75	theme	O-glycans	946:954	arg1	analysis					928:935	Our analysis	924:935	Our analysis of these O-glycans	924:954	Our analysis of these O-glycans showed no significant qualitative divergence between the O-glycans of the infected and those of the uninfected red cell.
8404896	12	76	attach	presence	1460:1467	arg1	proteins					1484:1491	proteins	1484:1491	proteins in the infected erythrocyte	1484:1519	Gel-filtration results had suggested the presence of O-GlcNAc on proteins in the infected erythrocyte.
8404896	12	76	attach	presence	1460:1467	arg2	O-GlcNAc					1472:1479	O-GlcNAc	1472:1479	O-GlcNAc	1472:1479	Gel-filtration results had suggested the presence of O-GlcNAc on proteins in the infected erythrocyte.
8404896	9	77	theme	reducing	1201:1208	arg1	terminus					1210:1217	their reducing terminus	1195:1217	their reducing terminus	1195:1217	According to preliminary alditol analyses, the O-glycans of P. falciparum-infected red cells do not contain GalNAc at their reducing terminus.
8404896	2	78	theme	malaria	282:288	arg1	parasite					290:297	the malaria parasite	278:297	the malaria parasite	278:297	O-Glycosylation is the major form of protein glycosylation in human erythrocytes infected with the asexual intraerythrocytic stage of the malaria parasite.
8404896	5	79	theme	protein	508:514	arg1	fraction					516:523	the protein fraction	504:523	the protein fraction of infected or uninfected erythrocytes	504:562	Non-labeled and metabolically glucosamine-labeled O-glycans were obtained from the protein fraction of infected or uninfected erythrocytes by beta elimination.
8810905	4	0	theme	peptide	881:887	arg1	isolation					889:897	peptide isolation	881:897	peptide isolation	881:897	In this paper, we have (1) excluded the possibility that (C2-Man-)Trp arose artificially under the acidic conditions previously employed for protein and peptide isolation and analysis, by maintaining the pH > 5 throughout these procedures, (2) demonstrated the occurrence of (C2-Man-)Trp in the intact protein, by NMR spectroscopy, (3) showed that (C2-Man-)Trp is not unique for RNase 2 from urine but that it is also present in the enzyme isolated from erythrocytes, and (4) found also that high-molecular mass isoforms of urinary RNase 2 are C-mannosylated.
8810905	3	1	theme	intact	607:612	arg1	protein					614:620	the intact protein	603:620	the intact protein	603:620	The evidence for the occurrence of C2-alpha-mannosyltryptophan [(C2-Man-)Trp] in the intact protein relied exclusively on the detection of the same phenylthiohydantoin derivatives during Edman degradation.
8810905	5	2	dep	N-	1444:1445	arg1	addition					1417:1424	addition	1417:1424	addition	1417:1424	These observations firmly establish C-mannosylation as a novel way of post-translationally attaching carbohydrate to protein, in addition to the well-known N- and O-glycosylations.
8810905	4	3	from	occurrence	989:998	arg1	protein					1030:1036	the intact protein	1019:1036	the intact protein	1019:1036	In this paper, we have (1) excluded the possibility that (C2-Man-)Trp arose artificially under the acidic conditions previously employed for protein and peptide isolation and analysis, by maintaining the pH > 5 throughout these procedures, (2) demonstrated the occurrence of (C2-Man-)Trp in the intact protein, by NMR spectroscopy, (3) showed that (C2-Man-)Trp is not unique for RNase 2 from urine but that it is also present in the enzyme isolated from erythrocytes, and (4) found also that high-molecular mass isoforms of urinary RNase 2 are C-mannosylated.
8810905	4	4	theme	C2-Man-	786:792	arg1	Trp					794:796	(C2-Man-)Trp	785:796	(C2-Man-)Trp	785:796	In this paper, we have (1) excluded the possibility that (C2-Man-)Trp arose artificially under the acidic conditions previously employed for protein and peptide isolation and analysis, by maintaining the pH > 5 throughout these procedures, (2) demonstrated the occurrence of (C2-Man-)Trp in the intact protein, by NMR spectroscopy, (3) showed that (C2-Man-)Trp is not unique for RNase 2 from urine but that it is also present in the enzyme isolated from erythrocytes, and (4) found also that high-molecular mass isoforms of urinary RNase 2 are C-mannosylated.
8810905	6	5	theme	different	1620:1628	arg1	conformation					1630:1641	a different conformation	1618:1641	a different conformation than in the glycopeptide or denatured protein, due to protein-carbohydrate interactions	1618:1729	Furthermore, the NMR data, in combination with molecular dynamics calculations, indicate that in the native protein the mannopyranosyl residue is in a different conformation than in the glycopeptide or denatured protein, due to protein-carbohydrate interactions.
8810905	0	6	theme	tryptophan	87:96	arg1	isoforms					130:137	its isoforms	126:137	its isoforms	126:137	Spectroscopic and protein chemical analyses demonstrate the presence of C-mannosylated tryptophan in intact human RNase 2 and its isoforms.
8810905	0	6	theme	tryptophan	87:96	arg1	presence					60:67	the presence	56:67	the presence of C-mannosylated tryptophan in intact human RNase 2	56:120	Spectroscopic and protein chemical analyses demonstrate the presence of C-mannosylated tryptophan in intact human RNase 2 and its isoforms.
8810905	1	7	dep	J.	262:263	arg1	Biochemistry					280:291	Biochemistry	280:291	Biochemistry	280:291	Recently, the C-mannosylation of a specific tryptophan residue in RNase 2 from human urine has been reported [Hofsteenge, J., et al. (1994) Biochemistry 33, 13524-13530; de Beer, T., et al. (1995) Biochemistry 34, 11785-11789].
8810905	1	7	dep	J.	262:263	arg1	al					326:327	et al	323:327	et al	323:327	Recently, the C-mannosylation of a specific tryptophan residue in RNase 2 from human urine has been reported [Hofsteenge, J., et al. (1994) Biochemistry 33, 13524-13530; de Beer, T., et al. (1995) Biochemistry 34, 11785-11789].
8810905	1	7	dep	J.	262:263	arg1	T.					319:320	T.	319:320	T.	319:320	Recently, the C-mannosylation of a specific tryptophan residue in RNase 2 from human urine has been reported [Hofsteenge, J., et al. (1994) Biochemistry 33, 13524-13530; de Beer, T., et al. (1995) Biochemistry 34, 11785-11789].
8810905	1	7	dep	J.	262:263	arg1	Biochemistry					337:348	Biochemistry	337:348	Biochemistry	337:348	Recently, the C-mannosylation of a specific tryptophan residue in RNase 2 from human urine has been reported [Hofsteenge, J., et al. (1994) Biochemistry 33, 13524-13530; de Beer, T., et al. (1995) Biochemistry 34, 11785-11789].
8810905	2	8	theme	fragments	511:519	arg1	analysis					491:498	mass spectrometric and NMR spectroscopic analysis	450:498	mass spectrometric and NMR spectroscopic analysis of peptide fragments	450:519	In those studies, identification of this unusual modification was accomplished by mass spectrometric and NMR spectroscopic analysis of peptide fragments.
8810905	4	9	dep	showed	1064:1069	arg1	3					1061:1061	3	1061:1061	3	1061:1061	In this paper, we have (1) excluded the possibility that (C2-Man-)Trp arose artificially under the acidic conditions previously employed for protein and peptide isolation and analysis, by maintaining the pH > 5 throughout these procedures, (2) demonstrated the occurrence of (C2-Man-)Trp in the intact protein, by NMR spectroscopy, (3) showed that (C2-Man-)Trp is not unique for RNase 2 from urine but that it is also present in the enzyme isolated from erythrocytes, and (4) found also that high-molecular mass isoforms of urinary RNase 2 are C-mannosylated.
8810905	4	9	dep	showed	1064:1069	arg1	demonstrated					972:983	demonstrated	972:983	demonstrated	972:983	In this paper, we have (1) excluded the possibility that (C2-Man-)Trp arose artificially under the acidic conditions previously employed for protein and peptide isolation and analysis, by maintaining the pH > 5 throughout these procedures, (2) demonstrated the occurrence of (C2-Man-)Trp in the intact protein, by NMR spectroscopy, (3) showed that (C2-Man-)Trp is not unique for RNase 2 from urine but that it is also present in the enzyme isolated from erythrocytes, and (4) found also that high-molecular mass isoforms of urinary RNase 2 are C-mannosylated.
8810905	4	9	dep	showed	1064:1069	arg1	2					969:969	2	969:969	2	969:969	In this paper, we have (1) excluded the possibility that (C2-Man-)Trp arose artificially under the acidic conditions previously employed for protein and peptide isolation and analysis, by maintaining the pH > 5 throughout these procedures, (2) demonstrated the occurrence of (C2-Man-)Trp in the intact protein, by NMR spectroscopy, (3) showed that (C2-Man-)Trp is not unique for RNase 2 from urine but that it is also present in the enzyme isolated from erythrocytes, and (4) found also that high-molecular mass isoforms of urinary RNase 2 are C-mannosylated.
8810905	0	10	theme	human	108:112	arg1	RNase					114:118	intact human RNase 2	101:120	intact human RNase 2	101:120	Spectroscopic and protein chemical analyses demonstrate the presence of C-mannosylated tryptophan in intact human RNase 2 and its isoforms.
8810905	6	11	theme	dynamics	1526:1533	arg1	calculations					1535:1546	molecular dynamics calculations	1516:1546	molecular dynamics calculations	1516:1546	Furthermore, the NMR data, in combination with molecular dynamics calculations, indicate that in the native protein the mannopyranosyl residue is in a different conformation than in the glycopeptide or denatured protein, due to protein-carbohydrate interactions.
8810905	2	12	theme	peptide	503:509	arg1	fragments					511:519	peptide fragments	503:519	peptide fragments	503:519	In those studies, identification of this unusual modification was accomplished by mass spectrometric and NMR spectroscopic analysis of peptide fragments.
8810905	1	13	from	C-mannosylation	154:168	arg1	RNase					206:210	RNase 2	206:212	RNase 2 from human urine	206:229	Recently, the C-mannosylation of a specific tryptophan residue in RNase 2 from human urine has been reported [Hofsteenge, J., et al. (1994) Biochemistry 33, 13524-13530; de Beer, T., et al. (1995) Biochemistry 34, 11785-11789].
8810905	4	14	attach	isolated	1168:1175	arg1	erythrocytes					1182:1193	erythrocytes	1182:1193	erythrocytes	1182:1193	In this paper, we have (1) excluded the possibility that (C2-Man-)Trp arose artificially under the acidic conditions previously employed for protein and peptide isolation and analysis, by maintaining the pH > 5 throughout these procedures, (2) demonstrated the occurrence of (C2-Man-)Trp in the intact protein, by NMR spectroscopy, (3) showed that (C2-Man-)Trp is not unique for RNase 2 from urine but that it is also present in the enzyme isolated from erythrocytes, and (4) found also that high-molecular mass isoforms of urinary RNase 2 are C-mannosylated.
8810905	4	14	attach	isolated	1168:1175	arg2	enzyme					1161:1166	the enzyme	1157:1166	the enzyme isolated from erythrocytes	1157:1193	In this paper, we have (1) excluded the possibility that (C2-Man-)Trp arose artificially under the acidic conditions previously employed for protein and peptide isolation and analysis, by maintaining the pH > 5 throughout these procedures, (2) demonstrated the occurrence of (C2-Man-)Trp in the intact protein, by NMR spectroscopy, (3) showed that (C2-Man-)Trp is not unique for RNase 2 from urine but that it is also present in the enzyme isolated from erythrocytes, and (4) found also that high-molecular mass isoforms of urinary RNase 2 are C-mannosylated.
8810905	6	15	theme	native	1570:1575	arg1	protein					1577:1583	the native protein	1566:1583	the native protein	1566:1583	Furthermore, the NMR data, in combination with molecular dynamics calculations, indicate that in the native protein the mannopyranosyl residue is in a different conformation than in the glycopeptide or denatured protein, due to protein-carbohydrate interactions.
8810905	0	16	theme	intact	101:106	arg1	RNase					114:118	intact human RNase 2	101:120	intact human RNase 2	101:120	Spectroscopic and protein chemical analyses demonstrate the presence of C-mannosylated tryptophan in intact human RNase 2 and its isoforms.
8810905	0	17	from	presence	60:67	arg1	RNase					114:118	intact human RNase 2	101:120	intact human RNase 2	101:120	Spectroscopic and protein chemical analyses demonstrate the presence of C-mannosylated tryptophan in intact human RNase 2 and its isoforms.
8810905	4	18	gly	C-mannosylated	1272:1285	arg1	isoforms					1240:1247	high-molecular mass isoforms	1220:1247	high-molecular mass isoforms of urinary RNase 2	1220:1266	In this paper, we have (1) excluded the possibility that (C2-Man-)Trp arose artificially under the acidic conditions previously employed for protein and peptide isolation and analysis, by maintaining the pH > 5 throughout these procedures, (2) demonstrated the occurrence of (C2-Man-)Trp in the intact protein, by NMR spectroscopy, (3) showed that (C2-Man-)Trp is not unique for RNase 2 from urine but that it is also present in the enzyme isolated from erythrocytes, and (4) found also that high-molecular mass isoforms of urinary RNase 2 are C-mannosylated.
8810905	0	19	gly	C-mannosylated	72:85	arg1	tryptophan					87:96	C-mannosylated tryptophan	72:96	C-mannosylated tryptophan	72:96	Spectroscopic and protein chemical analyses demonstrate the presence of C-mannosylated tryptophan in intact human RNase 2 and its isoforms.
8810905	2	20	theme	unusual	409:415	arg1	modification					417:428	this unusual modification	404:428	this unusual modification	404:428	In those studies, identification of this unusual modification was accomplished by mass spectrometric and NMR spectroscopic analysis of peptide fragments.
8810905	6	21	with	combination	1499:1509	arg1	calculations					1535:1546	molecular dynamics calculations	1516:1546	molecular dynamics calculations	1516:1546	Furthermore, the NMR data, in combination with molecular dynamics calculations, indicate that in the native protein the mannopyranosyl residue is in a different conformation than in the glycopeptide or denatured protein, due to protein-carbohydrate interactions.
8810905	6	22	theme	denatured	1671:1679	arg1	protein					1681:1687	the glycopeptide or denatured protein	1651:1687	the glycopeptide or denatured protein	1651:1687	Furthermore, the NMR data, in combination with molecular dynamics calculations, indicate that in the native protein the mannopyranosyl residue is in a different conformation than in the glycopeptide or denatured protein, due to protein-carbohydrate interactions.
8810905	6	23	theme	due	1690:1692	arg1	protein					1681:1687	the glycopeptide or denatured protein	1651:1687	the glycopeptide or denatured protein	1651:1687	Furthermore, the NMR data, in combination with molecular dynamics calculations, indicate that in the native protein the mannopyranosyl residue is in a different conformation than in the glycopeptide or denatured protein, due to protein-carbohydrate interactions.
8810905	6	24	theme	protein-carbohydrate	1697:1716	arg1	interactions					1718:1729	protein-carbohydrate interactions	1697:1729	protein-carbohydrate interactions	1697:1729	Furthermore, the NMR data, in combination with molecular dynamics calculations, indicate that in the native protein the mannopyranosyl residue is in a different conformation than in the glycopeptide or denatured protein, due to protein-carbohydrate interactions.
8810905	4	25	dep	excluded	755:762	arg1	1					752:752	1	752:752	1	752:752	In this paper, we have (1) excluded the possibility that (C2-Man-)Trp arose artificially under the acidic conditions previously employed for protein and peptide isolation and analysis, by maintaining the pH > 5 throughout these procedures, (2) demonstrated the occurrence of (C2-Man-)Trp in the intact protein, by NMR spectroscopy, (3) showed that (C2-Man-)Trp is not unique for RNase 2 from urine but that it is also present in the enzyme isolated from erythrocytes, and (4) found also that high-molecular mass isoforms of urinary RNase 2 are C-mannosylated.
8810905	4	26	from	urine	1120:1124	arg1	RNase					1107:1111	RNase 2	1107:1113	RNase 2 from urine	1107:1124	In this paper, we have (1) excluded the possibility that (C2-Man-)Trp arose artificially under the acidic conditions previously employed for protein and peptide isolation and analysis, by maintaining the pH > 5 throughout these procedures, (2) demonstrated the occurrence of (C2-Man-)Trp in the intact protein, by NMR spectroscopy, (3) showed that (C2-Man-)Trp is not unique for RNase 2 from urine but that it is also present in the enzyme isolated from erythrocytes, and (4) found also that high-molecular mass isoforms of urinary RNase 2 are C-mannosylated.
8810905	1	27	theme	human	219:223	arg1	urine					225:229	human urine	219:229	human urine	219:229	Recently, the C-mannosylation of a specific tryptophan residue in RNase 2 from human urine has been reported [Hofsteenge, J., et al. (1994) Biochemistry 33, 13524-13530; de Beer, T., et al. (1995) Biochemistry 34, 11785-11789].
8810905	6	28	gly	glycopeptide	1655:1666	arg2	glycopeptide					1655:1666	glycopeptide	1655:1666	glycopeptide	1655:1666	Furthermore, the NMR data, in combination with molecular dynamics calculations, indicate that in the native protein the mannopyranosyl residue is in a different conformation than in the glycopeptide or denatured protein, due to protein-carbohydrate interactions.
8810905	4	29	theme	RNase	1260:1264	arg1	isoforms					1240:1247	high-molecular mass isoforms	1220:1247	high-molecular mass isoforms of urinary RNase 2	1220:1266	In this paper, we have (1) excluded the possibility that (C2-Man-)Trp arose artificially under the acidic conditions previously employed for protein and peptide isolation and analysis, by maintaining the pH > 5 throughout these procedures, (2) demonstrated the occurrence of (C2-Man-)Trp in the intact protein, by NMR spectroscopy, (3) showed that (C2-Man-)Trp is not unique for RNase 2 from urine but that it is also present in the enzyme isolated from erythrocytes, and (4) found also that high-molecular mass isoforms of urinary RNase 2 are C-mannosylated.
8810905	5	30	theme	attaching	1379:1387	arg1	carbohydrate					1389:1400	post-translationally attaching carbohydrate	1358:1400	post-translationally attaching carbohydrate	1358:1400	These observations firmly establish C-mannosylation as a novel way of post-translationally attaching carbohydrate to protein, in addition to the well-known N- and O-glycosylations.
8810905	4	31	attach	present	1146:1152	arg2	it					1135:1136	it	1135:1136	it	1135:1136	In this paper, we have (1) excluded the possibility that (C2-Man-)Trp arose artificially under the acidic conditions previously employed for protein and peptide isolation and analysis, by maintaining the pH > 5 throughout these procedures, (2) demonstrated the occurrence of (C2-Man-)Trp in the intact protein, by NMR spectroscopy, (3) showed that (C2-Man-)Trp is not unique for RNase 2 from urine but that it is also present in the enzyme isolated from erythrocytes, and (4) found also that high-molecular mass isoforms of urinary RNase 2 are C-mannosylated.
8810905	4	31	attach	present	1146:1152	arg1	enzyme					1161:1166	the enzyme	1157:1166	the enzyme isolated from erythrocytes	1157:1193	In this paper, we have (1) excluded the possibility that (C2-Man-)Trp arose artificially under the acidic conditions previously employed for protein and peptide isolation and analysis, by maintaining the pH > 5 throughout these procedures, (2) demonstrated the occurrence of (C2-Man-)Trp in the intact protein, by NMR spectroscopy, (3) showed that (C2-Man-)Trp is not unique for RNase 2 from urine but that it is also present in the enzyme isolated from erythrocytes, and (4) found also that high-molecular mass isoforms of urinary RNase 2 are C-mannosylated.
8810905	4	32	theme	C2-Man-	1004:1010	arg1	Trp					1012:1014	(C2-Man-)Trp	1003:1014	(C2-Man-)Trp	1003:1014	In this paper, we have (1) excluded the possibility that (C2-Man-)Trp arose artificially under the acidic conditions previously employed for protein and peptide isolation and analysis, by maintaining the pH > 5 throughout these procedures, (2) demonstrated the occurrence of (C2-Man-)Trp in the intact protein, by NMR spectroscopy, (3) showed that (C2-Man-)Trp is not unique for RNase 2 from urine but that it is also present in the enzyme isolated from erythrocytes, and (4) found also that high-molecular mass isoforms of urinary RNase 2 are C-mannosylated.
8810905	1	33	theme	specific	175:182	arg1	residue					195:201	a specific tryptophan residue	173:201	a specific tryptophan residue in RNase 2 from human urine	173:229	Recently, the C-mannosylation of a specific tryptophan residue in RNase 2 from human urine has been reported [Hofsteenge, J., et al. (1994) Biochemistry 33, 13524-13530; de Beer, T., et al. (1995) Biochemistry 34, 11785-11789].
8810905	0	34	theme	Spectroscopic	0:12	arg1	analyses					35:42	Spectroscopic and protein chemical analyses	0:42	Spectroscopic and protein chemical analyses	0:42	Spectroscopic and protein chemical analyses demonstrate the presence of C-mannosylated tryptophan in intact human RNase 2 and its isoforms.
8810905	4	35	located	present	1146:1152	arg2	it					1135:1136	it	1135:1136	it	1135:1136	In this paper, we have (1) excluded the possibility that (C2-Man-)Trp arose artificially under the acidic conditions previously employed for protein and peptide isolation and analysis, by maintaining the pH > 5 throughout these procedures, (2) demonstrated the occurrence of (C2-Man-)Trp in the intact protein, by NMR spectroscopy, (3) showed that (C2-Man-)Trp is not unique for RNase 2 from urine but that it is also present in the enzyme isolated from erythrocytes, and (4) found also that high-molecular mass isoforms of urinary RNase 2 are C-mannosylated.
8810905	4	35	located	present	1146:1152	arg1	enzyme					1161:1166	the enzyme	1157:1166	the enzyme isolated from erythrocytes	1157:1193	In this paper, we have (1) excluded the possibility that (C2-Man-)Trp arose artificially under the acidic conditions previously employed for protein and peptide isolation and analysis, by maintaining the pH > 5 throughout these procedures, (2) demonstrated the occurrence of (C2-Man-)Trp in the intact protein, by NMR spectroscopy, (3) showed that (C2-Man-)Trp is not unique for RNase 2 from urine but that it is also present in the enzyme isolated from erythrocytes, and (4) found also that high-molecular mass isoforms of urinary RNase 2 are C-mannosylated.
8810905	5	36	theme	novel	1345:1349	arg1	C-mannosylation					1324:1338	C-mannosylation	1324:1338	C-mannosylation	1324:1338	These observations firmly establish C-mannosylation as a novel way of post-translationally attaching carbohydrate to protein, in addition to the well-known N- and O-glycosylations.
8810905	5	36	theme	novel	1345:1349	arg1	way					1351:1353	a novel way	1343:1353	a novel way of post-translationally attaching carbohydrate to protein	1343:1411	These observations firmly establish C-mannosylation as a novel way of post-translationally attaching carbohydrate to protein, in addition to the well-known N- and O-glycosylations.
8810905	1	37	theme	tryptophan	184:193	arg1	residue					195:201	a specific tryptophan residue	173:201	a specific tryptophan residue in RNase 2 from human urine	173:229	Recently, the C-mannosylation of a specific tryptophan residue in RNase 2 from human urine has been reported [Hofsteenge, J., et al. (1994) Biochemistry 33, 13524-13530; de Beer, T., et al. (1995) Biochemistry 34, 11785-11789].
8810905	0	38	theme	chemical	26:33	arg1	analyses					35:42	Spectroscopic and protein chemical analyses	0:42	Spectroscopic and protein chemical analyses	0:42	Spectroscopic and protein chemical analyses demonstrate the presence of C-mannosylated tryptophan in intact human RNase 2 and its isoforms.
8810905	6	39	theme	mannopyranosyl	1589:1602	arg1	residue					1604:1610	the mannopyranosyl residue	1585:1610	the mannopyranosyl residue	1585:1610	Furthermore, the NMR data, in combination with molecular dynamics calculations, indicate that in the native protein the mannopyranosyl residue is in a different conformation than in the glycopeptide or denatured protein, due to protein-carbohydrate interactions.
8810905	2	40	theme	spectrometric	455:467	arg1	analysis					491:498	mass spectrometric and NMR spectroscopic analysis	450:498	mass spectrometric and NMR spectroscopic analysis of peptide fragments	450:519	In those studies, identification of this unusual modification was accomplished by mass spectrometric and NMR spectroscopic analysis of peptide fragments.
8810905	0	41	attach	presence	60:67	arg1	RNase					114:118	intact human RNase 2	101:120	intact human RNase 2	101:120	Spectroscopic and protein chemical analyses demonstrate the presence of C-mannosylated tryptophan in intact human RNase 2 and its isoforms.
8810905	0	41	attach	presence	60:67	arg2	tryptophan					87:96	C-mannosylated tryptophan	72:96	C-mannosylated tryptophan	72:96	Spectroscopic and protein chemical analyses demonstrate the presence of C-mannosylated tryptophan in intact human RNase 2 and its isoforms.
8810905	1	42	theme	residue	195:201	arg1	C-mannosylation					154:168	the C-mannosylation	150:168	the C-mannosylation of a specific tryptophan residue in RNase 2 from human urine	150:229	Recently, the C-mannosylation of a specific tryptophan residue in RNase 2 from human urine has been reported [Hofsteenge, J., et al. (1994) Biochemistry 33, 13524-13530; de Beer, T., et al. (1995) Biochemistry 34, 11785-11789].
8810905	0	43	theme	protein	18:24	arg1	analyses					35:42	Spectroscopic and protein chemical analyses	0:42	Spectroscopic and protein chemical analyses	0:42	Spectroscopic and protein chemical analyses demonstrate the presence of C-mannosylated tryptophan in intact human RNase 2 and its isoforms.
8810905	4	44	theme	NMR	1042:1044	arg1	spectroscopy					1046:1057	NMR spectroscopy	1042:1057	NMR spectroscopy	1042:1057	In this paper, we have (1) excluded the possibility that (C2-Man-)Trp arose artificially under the acidic conditions previously employed for protein and peptide isolation and analysis, by maintaining the pH > 5 throughout these procedures, (2) demonstrated the occurrence of (C2-Man-)Trp in the intact protein, by NMR spectroscopy, (3) showed that (C2-Man-)Trp is not unique for RNase 2 from urine but that it is also present in the enzyme isolated from erythrocytes, and (4) found also that high-molecular mass isoforms of urinary RNase 2 are C-mannosylated.
8810905	3	45	theme	C2-alpha-mannosyltryptophan	557:583	arg1	occurrence					543:552	the occurrence	539:552	the occurrence of C2-alpha-mannosyltryptophan [(C2-Man-)Trp] in the intact protein	539:620	The evidence for the occurrence of C2-alpha-mannosyltryptophan [(C2-Man-)Trp] in the intact protein relied exclusively on the detection of the same phenylthiohydantoin derivatives during Edman degradation.
8810905	4	46	theme	mass	1235:1238	arg1	isoforms					1240:1247	high-molecular mass isoforms	1220:1247	high-molecular mass isoforms of urinary RNase 2	1220:1266	In this paper, we have (1) excluded the possibility that (C2-Man-)Trp arose artificially under the acidic conditions previously employed for protein and peptide isolation and analysis, by maintaining the pH > 5 throughout these procedures, (2) demonstrated the occurrence of (C2-Man-)Trp in the intact protein, by NMR spectroscopy, (3) showed that (C2-Man-)Trp is not unique for RNase 2 from urine but that it is also present in the enzyme isolated from erythrocytes, and (4) found also that high-molecular mass isoforms of urinary RNase 2 are C-mannosylated.
8810905	4	47	from	enzyme	1161:1166	arg1	present					1146:1152	present	1146:1152	present	1146:1152	In this paper, we have (1) excluded the possibility that (C2-Man-)Trp arose artificially under the acidic conditions previously employed for protein and peptide isolation and analysis, by maintaining the pH > 5 throughout these procedures, (2) demonstrated the occurrence of (C2-Man-)Trp in the intact protein, by NMR spectroscopy, (3) showed that (C2-Man-)Trp is not unique for RNase 2 from urine but that it is also present in the enzyme isolated from erythrocytes, and (4) found also that high-molecular mass isoforms of urinary RNase 2 are C-mannosylated.
8810905	4	48	theme	acidic	827:832	arg1	conditions					834:843	the acidic conditions	823:843	the acidic conditions previously employed for protein and peptide isolation and analysis, by maintaining the pH > 5 throughout these procedures, (2) demonstrated the occurrence of (C2-Man-)Trp in the intact protein, by NMR spectroscopy, (3) showed that (C2-Man-)Trp is not unique for RNase 2 from urine but that it is also present in the enzyme isolated from erythrocytes, and (4) found also that high-molecular mass isoforms of urinary RNase 2 are C-mannosylated	823:1285	In this paper, we have (1) excluded the possibility that (C2-Man-)Trp arose artificially under the acidic conditions previously employed for protein and peptide isolation and analysis, by maintaining the pH > 5 throughout these procedures, (2) demonstrated the occurrence of (C2-Man-)Trp in the intact protein, by NMR spectroscopy, (3) showed that (C2-Man-)Trp is not unique for RNase 2 from urine but that it is also present in the enzyme isolated from erythrocytes, and (4) found also that high-molecular mass isoforms of urinary RNase 2 are C-mannosylated.
8810905	4	49	theme	urinary	1252:1258	arg1	RNase					1260:1264	urinary RNase 2	1252:1266	urinary RNase 2	1252:1266	In this paper, we have (1) excluded the possibility that (C2-Man-)Trp arose artificially under the acidic conditions previously employed for protein and peptide isolation and analysis, by maintaining the pH > 5 throughout these procedures, (2) demonstrated the occurrence of (C2-Man-)Trp in the intact protein, by NMR spectroscopy, (3) showed that (C2-Man-)Trp is not unique for RNase 2 from urine but that it is also present in the enzyme isolated from erythrocytes, and (4) found also that high-molecular mass isoforms of urinary RNase 2 are C-mannosylated.
8810905	3	50	theme	derivatives	690:700	arg1	detection					648:656	the detection	644:656	the detection of the same phenylthiohydantoin derivatives during Edman degradation	644:725	The evidence for the occurrence of C2-alpha-mannosyltryptophan [(C2-Man-)Trp] in the intact protein relied exclusively on the detection of the same phenylthiohydantoin derivatives during Edman degradation.
8810905	4	51	dep	found	1204:1208	arg1	4					1201:1201	4	1201:1201	4	1201:1201	In this paper, we have (1) excluded the possibility that (C2-Man-)Trp arose artificially under the acidic conditions previously employed for protein and peptide isolation and analysis, by maintaining the pH > 5 throughout these procedures, (2) demonstrated the occurrence of (C2-Man-)Trp in the intact protein, by NMR spectroscopy, (3) showed that (C2-Man-)Trp is not unique for RNase 2 from urine but that it is also present in the enzyme isolated from erythrocytes, and (4) found also that high-molecular mass isoforms of urinary RNase 2 are C-mannosylated.
8810905	6	52	theme	NMR	1486:1488	arg1	data					1490:1493	the NMR data	1482:1493	the NMR data	1482:1493	Furthermore, the NMR data, in combination with molecular dynamics calculations, indicate that in the native protein the mannopyranosyl residue is in a different conformation than in the glycopeptide or denatured protein, due to protein-carbohydrate interactions.
8810905	4	53	theme	pH	932:933	arg1	>					935:935	the pH > 5	928:937	the pH > 5	928:937	In this paper, we have (1) excluded the possibility that (C2-Man-)Trp arose artificially under the acidic conditions previously employed for protein and peptide isolation and analysis, by maintaining the pH > 5 throughout these procedures, (2) demonstrated the occurrence of (C2-Man-)Trp in the intact protein, by NMR spectroscopy, (3) showed that (C2-Man-)Trp is not unique for RNase 2 from urine but that it is also present in the enzyme isolated from erythrocytes, and (4) found also that high-molecular mass isoforms of urinary RNase 2 are C-mannosylated.
8810905	1	54	from	RNase	206:210	arg1	C-mannosylation					154:168	the C-mannosylation	150:168	the C-mannosylation of a specific tryptophan residue in RNase 2 from human urine	150:229	Recently, the C-mannosylation of a specific tryptophan residue in RNase 2 from human urine has been reported [Hofsteenge, J., et al. (1994) Biochemistry 33, 13524-13530; de Beer, T., et al. (1995) Biochemistry 34, 11785-11789].
8810905	6	55	theme	glycopeptide	1655:1666	arg1	protein					1681:1687	the glycopeptide or denatured protein	1651:1687	the glycopeptide or denatured protein	1651:1687	Furthermore, the NMR data, in combination with molecular dynamics calculations, indicate that in the native protein the mannopyranosyl residue is in a different conformation than in the glycopeptide or denatured protein, due to protein-carbohydrate interactions.
8810905	3	56	from	occurrence	543:552	arg1	protein					614:620	the intact protein	603:620	the intact protein	603:620	The evidence for the occurrence of C2-alpha-mannosyltryptophan [(C2-Man-)Trp] in the intact protein relied exclusively on the detection of the same phenylthiohydantoin derivatives during Edman degradation.
8810905	1	57	from	urine	225:229	arg1	RNase					206:210	RNase 2	206:212	RNase 2 from human urine	206:229	Recently, the C-mannosylation of a specific tryptophan residue in RNase 2 from human urine has been reported [Hofsteenge, J., et al. (1994) Biochemistry 33, 13524-13530; de Beer, T., et al. (1995) Biochemistry 34, 11785-11789].
8810905	1	57	from	urine	225:229	arg1	residue					195:201	a specific tryptophan residue	173:201	a specific tryptophan residue in RNase 2 from human urine	173:229	Recently, the C-mannosylation of a specific tryptophan residue in RNase 2 from human urine has been reported [Hofsteenge, J., et al. (1994) Biochemistry 33, 13524-13530; de Beer, T., et al. (1995) Biochemistry 34, 11785-11789].
8810905	4	58	theme	high-molecular	1220:1233	arg1	isoforms					1240:1247	high-molecular mass isoforms	1220:1247	high-molecular mass isoforms of urinary RNase 2	1220:1266	In this paper, we have (1) excluded the possibility that (C2-Man-)Trp arose artificially under the acidic conditions previously employed for protein and peptide isolation and analysis, by maintaining the pH > 5 throughout these procedures, (2) demonstrated the occurrence of (C2-Man-)Trp in the intact protein, by NMR spectroscopy, (3) showed that (C2-Man-)Trp is not unique for RNase 2 from urine but that it is also present in the enzyme isolated from erythrocytes, and (4) found also that high-molecular mass isoforms of urinary RNase 2 are C-mannosylated.
8810905	4	59	from	present	1146:1152	arg1	enzyme					1161:1166	the enzyme	1157:1166	the enzyme isolated from erythrocytes	1157:1193	In this paper, we have (1) excluded the possibility that (C2-Man-)Trp arose artificially under the acidic conditions previously employed for protein and peptide isolation and analysis, by maintaining the pH > 5 throughout these procedures, (2) demonstrated the occurrence of (C2-Man-)Trp in the intact protein, by NMR spectroscopy, (3) showed that (C2-Man-)Trp is not unique for RNase 2 from urine but that it is also present in the enzyme isolated from erythrocytes, and (4) found also that high-molecular mass isoforms of urinary RNase 2 are C-mannosylated.
8810905	3	60	theme	same	665:668	arg1	derivatives					690:700	the same phenylthiohydantoin derivatives	661:700	the same phenylthiohydantoin derivatives	661:700	The evidence for the occurrence of C2-alpha-mannosyltryptophan [(C2-Man-)Trp] in the intact protein relied exclusively on the detection of the same phenylthiohydantoin derivatives during Edman degradation.
8810905	2	61	theme	spectroscopic	477:489	arg1	analysis					491:498	mass spectrometric and NMR spectroscopic analysis	450:498	mass spectrometric and NMR spectroscopic analysis of peptide fragments	450:519	In those studies, identification of this unusual modification was accomplished by mass spectrometric and NMR spectroscopic analysis of peptide fragments.
8810905	1	62	from	residue	195:201	arg1	urine					225:229	human urine	219:229	human urine	219:229	Recently, the C-mannosylation of a specific tryptophan residue in RNase 2 from human urine has been reported [Hofsteenge, J., et al. (1994) Biochemistry 33, 13524-13530; de Beer, T., et al. (1995) Biochemistry 34, 11785-11789].
8810905	1	62	from	residue	195:201	arg1	RNase					206:210	RNase 2	206:212	RNase 2 from human urine	206:229	Recently, the C-mannosylation of a specific tryptophan residue in RNase 2 from human urine has been reported [Hofsteenge, J., et al. (1994) Biochemistry 33, 13524-13530; de Beer, T., et al. (1995) Biochemistry 34, 11785-11789].
8810905	5	63	theme	well-known	1433:1442	arg1	N-					1444:1445	the well-known N-	1429:1445	the well-known N-	1429:1445	These observations firmly establish C-mannosylation as a novel way of post-translationally attaching carbohydrate to protein, in addition to the well-known N- and O-glycosylations.
8810905	3	64	theme	phenylthiohydantoin	670:688	arg1	derivatives					690:700	the same phenylthiohydantoin derivatives	661:700	the same phenylthiohydantoin derivatives	661:700	The evidence for the occurrence of C2-alpha-mannosyltryptophan [(C2-Man-)Trp] in the intact protein relied exclusively on the detection of the same phenylthiohydantoin derivatives during Edman degradation.
8810905	1	65	gly	C-mannosylation	154:168	arg1	residue					195:201	a specific tryptophan residue	173:201	a specific tryptophan residue in RNase 2 from human urine	173:229	Recently, the C-mannosylation of a specific tryptophan residue in RNase 2 from human urine has been reported [Hofsteenge, J., et al. (1994) Biochemistry 33, 13524-13530; de Beer, T., et al. (1995) Biochemistry 34, 11785-11789].
8810905	4	66	theme	C2-Man-	1077:1083	arg1	Trp					1085:1087	(C2-Man-)Trp	1076:1087	(C2-Man-)Trp	1076:1087	In this paper, we have (1) excluded the possibility that (C2-Man-)Trp arose artificially under the acidic conditions previously employed for protein and peptide isolation and analysis, by maintaining the pH > 5 throughout these procedures, (2) demonstrated the occurrence of (C2-Man-)Trp in the intact protein, by NMR spectroscopy, (3) showed that (C2-Man-)Trp is not unique for RNase 2 from urine but that it is also present in the enzyme isolated from erythrocytes, and (4) found also that high-molecular mass isoforms of urinary RNase 2 are C-mannosylated.
8810905	6	67	from	conformation	1630:1641	arg1	protein					1681:1687	the glycopeptide or denatured protein	1651:1687	the glycopeptide or denatured protein	1651:1687	Furthermore, the NMR data, in combination with molecular dynamics calculations, indicate that in the native protein the mannopyranosyl residue is in a different conformation than in the glycopeptide or denatured protein, due to protein-carbohydrate interactions.
8810905	6	67	from	conformation	1630:1641	arg1	protein					1577:1583	the native protein	1566:1583	the native protein	1566:1583	Furthermore, the NMR data, in combination with molecular dynamics calculations, indicate that in the native protein the mannopyranosyl residue is in a different conformation than in the glycopeptide or denatured protein, due to protein-carbohydrate interactions.
8810905	0	68	from	isoforms	130:137	arg1	RNase					114:118	intact human RNase 2	101:120	intact human RNase 2	101:120	Spectroscopic and protein chemical analyses demonstrate the presence of C-mannosylated tryptophan in intact human RNase 2 and its isoforms.
8810905	0	69	theme	C-mannosylated	72:85	arg1	tryptophan					87:96	C-mannosylated tryptophan	72:96	C-mannosylated tryptophan	72:96	Spectroscopic and protein chemical analyses demonstrate the presence of C-mannosylated tryptophan in intact human RNase 2 and its isoforms.
8810905	3	70	theme	C2-Man-	587:593	arg1	C2-alpha-mannosyltryptophan					557:583	C2-alpha-mannosyltryptophan	557:583	C2-alpha-mannosyltryptophan [(C2-Man-)Trp]	557:598	The evidence for the occurrence of C2-alpha-mannosyltryptophan [(C2-Man-)Trp] in the intact protein relied exclusively on the detection of the same phenylthiohydantoin derivatives during Edman degradation.
8810905	3	70	theme	C2-Man-	587:593	arg1	Trp					595:597	(C2-Man-)Trp	586:597	(C2-Man-)Trp	586:597	The evidence for the occurrence of C2-alpha-mannosyltryptophan [(C2-Man-)Trp] in the intact protein relied exclusively on the detection of the same phenylthiohydantoin derivatives during Edman degradation.
8810905	4	71	theme	Trp	1012:1014	arg1	occurrence					989:998	the occurrence	985:998	the occurrence of (C2-Man-)Trp in the intact protein	985:1036	In this paper, we have (1) excluded the possibility that (C2-Man-)Trp arose artificially under the acidic conditions previously employed for protein and peptide isolation and analysis, by maintaining the pH > 5 throughout these procedures, (2) demonstrated the occurrence of (C2-Man-)Trp in the intact protein, by NMR spectroscopy, (3) showed that (C2-Man-)Trp is not unique for RNase 2 from urine but that it is also present in the enzyme isolated from erythrocytes, and (4) found also that high-molecular mass isoforms of urinary RNase 2 are C-mannosylated.
8810905	6	72	theme	molecular	1516:1524	arg1	calculations					1535:1546	molecular dynamics calculations	1516:1546	molecular dynamics calculations	1516:1546	Furthermore, the NMR data, in combination with molecular dynamics calculations, indicate that in the native protein the mannopyranosyl residue is in a different conformation than in the glycopeptide or denatured protein, due to protein-carbohydrate interactions.
8810905	3	73	theme	Edman	709:713	arg1	degradation					715:725	Edman degradation	709:725	Edman degradation	709:725	The evidence for the occurrence of C2-alpha-mannosyltryptophan [(C2-Man-)Trp] in the intact protein relied exclusively on the detection of the same phenylthiohydantoin derivatives during Edman degradation.
8810905	5	74	theme	carbohydrate	1389:1400	arg1	C-mannosylation					1324:1338	C-mannosylation	1324:1338	C-mannosylation	1324:1338	These observations firmly establish C-mannosylation as a novel way of post-translationally attaching carbohydrate to protein, in addition to the well-known N- and O-glycosylations.
8810905	5	74	theme	carbohydrate	1389:1400	arg1	way					1351:1353	a novel way	1343:1353	a novel way of post-translationally attaching carbohydrate to protein	1343:1411	These observations firmly establish C-mannosylation as a novel way of post-translationally attaching carbohydrate to protein, in addition to the well-known N- and O-glycosylations.
8810905	6	75	from	data	1490:1493	arg1	combination					1499:1509	combination	1499:1509	combination with molecular dynamics calculations	1499:1546	Furthermore, the NMR data, in combination with molecular dynamics calculations, indicate that in the native protein the mannopyranosyl residue is in a different conformation than in the glycopeptide or denatured protein, due to protein-carbohydrate interactions.
8810905	4	76	theme	intact	1023:1028	arg1	protein					1030:1036	the intact protein	1019:1036	the intact protein	1019:1036	In this paper, we have (1) excluded the possibility that (C2-Man-)Trp arose artificially under the acidic conditions previously employed for protein and peptide isolation and analysis, by maintaining the pH > 5 throughout these procedures, (2) demonstrated the occurrence of (C2-Man-)Trp in the intact protein, by NMR spectroscopy, (3) showed that (C2-Man-)Trp is not unique for RNase 2 from urine but that it is also present in the enzyme isolated from erythrocytes, and (4) found also that high-molecular mass isoforms of urinary RNase 2 are C-mannosylated.
8810905	2	77	theme	modification	417:428	arg1	identification					386:399	identification	386:399	identification of this unusual modification	386:428	In those studies, identification of this unusual modification was accomplished by mass spectrometric and NMR spectroscopic analysis of peptide fragments.
10207176	5	0	theme	B-lymphoblastoid	719:734	arg1	cells					736:740	human B-lymphoblastoid cells	713:740	human B-lymphoblastoid cells	713:740	Furthermore, human B-lymphoblastoid cells, which secrete IL-12, were found to contain an enzyme that carries out the C-mannosylation reaction.
10207176	7	1	theme	second	936:941	arg1	report					943:948	only the second report	927:948	only the second report on a C-mannosylated protein	927:976	This is only the second report on a C-mannosylated protein.
10207176	7	1	theme	second	936:941	arg1	This					919:922	This	919:922	This	919:922	This is only the second report on a C-mannosylated protein.
10207176	0	2	theme	protein	75:81	arg1	interleukin-12					18:31	Recombinant human interleukin-12	0:31	Recombinant human interleukin-12	0:31	Recombinant human interleukin-12 is the second example of a C-mannosylated protein.
10207176	0	2	theme	protein	75:81	arg1	example					47:53	the second example	36:53	the second example of a C-mannosylated protein	36:81	Recombinant human interleukin-12 is the second example of a C-mannosylated protein.
10207176	2	3	attach	attachment	320:329	arg2	residue					345:351	a mannosyl residue	334:351	a mannosyl residue	334:351	In human RNase 2 this is the recognition motif for a new, recently discovered posttranslational modification, i.e., the C-glycosidic attachment of a mannosyl residue to the side chain of tryptophan.
10207176	2	3	attach	attachment	320:329	arg1	chain					365:369	the side chain	356:369	the side chain of tryptophan	356:383	In human RNase 2 this is the recognition motif for a new, recently discovered posttranslational modification, i.e., the C-glycosidic attachment of a mannosyl residue to the side chain of tryptophan.
10207176	3	4	dep	C-mannosylated	533:546	arg1	partially					522:530	partially	522:530	partially	522:530	Analysis of C-terminal peptides of recombinant IL-12 (rHuIL-12) by mass spectrometry and NMR spectroscopy revealed that Trp-319beta is (partially) C-mannosylated.
10207176	8	5	theme	recognition	1100:1110	arg1	motif					1112:1116	the recognition motif	1096:1116	the recognition motif	1096:1116	However, the occurrence of the C-mannosyltransferase activity in a variety of cells and tissues, and the presence of the recognition motif in many proteins indicate that more C-mannosylated proteins may be found.
10207176	3	6	theme	NMR	475:477	arg1	spectroscopy					479:490	NMR spectroscopy	475:490	NMR spectroscopy	475:490	Analysis of C-terminal peptides of recombinant IL-12 (rHuIL-12) by mass spectrometry and NMR spectroscopy revealed that Trp-319beta is (partially) C-mannosylated.
10207176	4	7	theme	synthetic	622:630	arg1	peptide					632:638	a synthetic peptide	620:638	a synthetic peptide derived from the same region of the protein	620:682	This finding was extended by in vitro mannosylation experiments, using a synthetic peptide derived from the same region of the protein as an acceptor.
10207176	4	7	theme	synthetic	622:630	arg1	acceptor					690:697	an acceptor	687:697	an acceptor	687:697	This finding was extended by in vitro mannosylation experiments, using a synthetic peptide derived from the same region of the protein as an acceptor.
10207176	0	8	gly	C-mannosylated	60:73	arg1	protein					75:81	a C-mannosylated protein	58:81	a C-mannosylated protein	58:81	Recombinant human interleukin-12 is the second example of a C-mannosylated protein.
10207176	6	9	gly	C-mannosylated	895:908	arg1	IL-12					874:878	nonrecombinant IL-12	859:878	nonrecombinant IL-12	859:878	This shows that nonrecombinant IL-12 is potentially C-mannosylated as well.
10207176	4	10	theme	same	657:660	arg1	region					662:667	the same region	653:667	the same region of the protein	653:682	This finding was extended by in vitro mannosylation experiments, using a synthetic peptide derived from the same region of the protein as an acceptor.
10207176	2	11	theme	C-glycosidic	307:318	arg1	modification					283:294	a new, recently discovered posttranslational modification	238:294	a new, recently discovered posttranslational modification	238:294	In human RNase 2 this is the recognition motif for a new, recently discovered posttranslational modification, i.e., the C-glycosidic attachment of a mannosyl residue to the side chain of tryptophan.
10207176	2	11	theme	C-glycosidic	307:318	arg1	attachment					320:329	the C-glycosidic attachment	303:329	the C-glycosidic attachment of a mannosyl residue to the side chain of tryptophan	303:383	In human RNase 2 this is the recognition motif for a new, recently discovered posttranslational modification, i.e., the C-glycosidic attachment of a mannosyl residue to the side chain of tryptophan.
10207176	4	12	theme	mannosylation	587:599	arg1	experiments					601:611	in vitro mannosylation experiments	578:611	in vitro mannosylation experiments	578:611	This finding was extended by in vitro mannosylation experiments, using a synthetic peptide derived from the same region of the protein as an acceptor.
10207176	2	13	theme	new	240:242	arg1	modification					283:294	a new, recently discovered posttranslational modification	238:294	a new, recently discovered posttranslational modification	238:294	In human RNase 2 this is the recognition motif for a new, recently discovered posttranslational modification, i.e., the C-glycosidic attachment of a mannosyl residue to the side chain of tryptophan.
10207176	2	13	theme	new	240:242	arg1	attachment					320:329	the C-glycosidic attachment	303:329	the C-glycosidic attachment of a mannosyl residue to the side chain of tryptophan	303:383	In human RNase 2 this is the recognition motif for a new, recently discovered posttranslational modification, i.e., the C-glycosidic attachment of a mannosyl residue to the side chain of tryptophan.
10207176	2	14	theme	side	360:363	arg1	chain					365:369	the side chain	356:369	the side chain of tryptophan	356:383	In human RNase 2 this is the recognition motif for a new, recently discovered posttranslational modification, i.e., the C-glycosidic attachment of a mannosyl residue to the side chain of tryptophan.
10207176	8	15	theme	motif	1112:1116	arg1	presence					1084:1091	the presence	1080:1091	the presence of the recognition motif in many proteins	1080:1133	However, the occurrence of the C-mannosyltransferase activity in a variety of cells and tissues, and the presence of the recognition motif in many proteins indicate that more C-mannosylated proteins may be found.
10207176	8	15	theme	motif	1112:1116	arg1	occurrence					992:1001	the occurrence	988:1001	the occurrence of the C-mannosyltransferase activity in a variety of cells and tissues	988:1073	However, the occurrence of the C-mannosyltransferase activity in a variety of cells and tissues, and the presence of the recognition motif in many proteins indicate that more C-mannosylated proteins may be found.
10207176	1	16	contain	contains	131:138	arg2	beta-chain					88:97	The beta-chain	84:97	The beta-chain of human interleukin 12 (IL-12)	84:129	The beta-chain of human interleukin 12 (IL-12) contains at position 319-322, the sequence Trp-x-x-Trp.
10207176	1	16	contain	contains	131:138	arg1	Trp-x-x-Trp					174:184	the sequence Trp-x-x-Trp	161:184	the sequence Trp-x-x-Trp	161:184	The beta-chain of human interleukin 12 (IL-12) contains at position 319-322, the sequence Trp-x-x-Trp.
10207176	1	16	contain	contains	131:138	arg1	position					143:150	position 319-322	143:158	position 319-322	143:158	The beta-chain of human interleukin 12 (IL-12) contains at position 319-322, the sequence Trp-x-x-Trp.
10207176	8	17	theme	C-mannosylated	1154:1167	arg1	proteins					1169:1176	more C-mannosylated proteins	1149:1176	more C-mannosylated proteins	1149:1176	However, the occurrence of the C-mannosyltransferase activity in a variety of cells and tissues, and the presence of the recognition motif in many proteins indicate that more C-mannosylated proteins may be found.
10207176	8	18	theme	many	1121:1124	arg1	proteins					1126:1133	many proteins	1121:1133	many proteins	1121:1133	However, the occurrence of the C-mannosyltransferase activity in a variety of cells and tissues, and the presence of the recognition motif in many proteins indicate that more C-mannosylated proteins may be found.
10207176	3	19	theme	peptides	409:416	arg1	Analysis					386:393	Analysis	386:393	Analysis of C-terminal peptides of recombinant IL-12 (rHuIL-12) by mass spectrometry and NMR spectroscopy	386:490	Analysis of C-terminal peptides of recombinant IL-12 (rHuIL-12) by mass spectrometry and NMR spectroscopy revealed that Trp-319beta is (partially) C-mannosylated.
10207176	0	20	theme	human	12:16	arg1	interleukin-12					18:31	Recombinant human interleukin-12	0:31	Recombinant human interleukin-12	0:31	Recombinant human interleukin-12 is the second example of a C-mannosylated protein.
10207176	0	20	theme	human	12:16	arg1	example					47:53	the second example	36:53	the second example of a C-mannosylated protein	36:81	Recombinant human interleukin-12 is the second example of a C-mannosylated protein.
10207176	8	21	theme	activity	1032:1039	arg1	presence					1084:1091	the presence	1080:1091	the presence of the recognition motif in many proteins	1080:1133	However, the occurrence of the C-mannosyltransferase activity in a variety of cells and tissues, and the presence of the recognition motif in many proteins indicate that more C-mannosylated proteins may be found.
10207176	8	21	theme	activity	1032:1039	arg1	occurrence					992:1001	the occurrence	988:1001	the occurrence of the C-mannosyltransferase activity in a variety of cells and tissues	988:1073	However, the occurrence of the C-mannosyltransferase activity in a variety of cells and tissues, and the presence of the recognition motif in many proteins indicate that more C-mannosylated proteins may be found.
10207176	8	22	gly	C-mannosylated	1154:1167	arg1	proteins					1169:1176	more C-mannosylated proteins	1149:1176	more C-mannosylated proteins	1149:1176	However, the occurrence of the C-mannosyltransferase activity in a variety of cells and tissues, and the presence of the recognition motif in many proteins indicate that more C-mannosylated proteins may be found.
10207176	6	23	theme	nonrecombinant	859:872	arg1	IL-12					874:878	nonrecombinant IL-12	859:878	nonrecombinant IL-12	859:878	This shows that nonrecombinant IL-12 is potentially C-mannosylated as well.
10207176	7	24	from	report	943:948	arg1	protein					970:976	a C-mannosylated protein	953:976	a C-mannosylated protein	953:976	This is only the second report on a C-mannosylated protein.
10207176	0	25	theme	Recombinant	0:10	arg1	interleukin-12					18:31	Recombinant human interleukin-12	0:31	Recombinant human interleukin-12	0:31	Recombinant human interleukin-12 is the second example of a C-mannosylated protein.
10207176	0	25	theme	Recombinant	0:10	arg1	example					47:53	the second example	36:53	the second example of a C-mannosylated protein	36:81	Recombinant human interleukin-12 is the second example of a C-mannosylated protein.
10207176	8	26	from	occurrence	992:1001	arg1	variety					1046:1052	a variety	1044:1052	a variety of cells and tissues	1044:1073	However, the occurrence of the C-mannosyltransferase activity in a variety of cells and tissues, and the presence of the recognition motif in many proteins indicate that more C-mannosylated proteins may be found.
10207176	8	26	from	occurrence	992:1001	arg1	tissues					1067:1073	tissues	1067:1073	tissues	1067:1073	However, the occurrence of the C-mannosyltransferase activity in a variety of cells and tissues, and the presence of the recognition motif in many proteins indicate that more C-mannosylated proteins may be found.
10207176	8	26	from	occurrence	992:1001	arg1	proteins					1126:1133	many proteins	1121:1133	many proteins	1121:1133	However, the occurrence of the C-mannosyltransferase activity in a variety of cells and tissues, and the presence of the recognition motif in many proteins indicate that more C-mannosylated proteins may be found.
10207176	8	26	from	occurrence	992:1001	arg1	cells					1057:1061	cells	1057:1061	cells	1057:1061	However, the occurrence of the C-mannosyltransferase activity in a variety of cells and tissues, and the presence of the recognition motif in many proteins indicate that more C-mannosylated proteins may be found.
10207176	8	27	theme	C-mannosyltransferase	1010:1030	arg1	activity					1032:1039	the C-mannosyltransferase activity	1006:1039	the C-mannosyltransferase activity	1006:1039	However, the occurrence of the C-mannosyltransferase activity in a variety of cells and tissues, and the presence of the recognition motif in many proteins indicate that more C-mannosylated proteins may be found.
10207176	3	28	gly	C-mannosylated	533:546	arg1	Trp-319beta					506:516	Trp-319beta	506:516	Trp-319beta	506:516	Analysis of C-terminal peptides of recombinant IL-12 (rHuIL-12) by mass spectrometry and NMR spectroscopy revealed that Trp-319beta is (partially) C-mannosylated.
10207176	2	29	theme	residue	345:351	arg1	modification					283:294	a new, recently discovered posttranslational modification	238:294	a new, recently discovered posttranslational modification	238:294	In human RNase 2 this is the recognition motif for a new, recently discovered posttranslational modification, i.e., the C-glycosidic attachment of a mannosyl residue to the side chain of tryptophan.
10207176	2	29	theme	residue	345:351	arg1	attachment					320:329	the C-glycosidic attachment	303:329	the C-glycosidic attachment of a mannosyl residue to the side chain of tryptophan	303:383	In human RNase 2 this is the recognition motif for a new, recently discovered posttranslational modification, i.e., the C-glycosidic attachment of a mannosyl residue to the side chain of tryptophan.
10207176	5	30	contain	contain	778:784	arg2	enzyme					789:794	an enzyme	786:794	an enzyme that carries out the C-mannosylation reaction	786:840	Furthermore, human B-lymphoblastoid cells, which secrete IL-12, were found to contain an enzyme that carries out the C-mannosylation reaction.
10207176	5	30	contain	contain	778:784	arg1	cells					736:740	human B-lymphoblastoid cells	713:740	human B-lymphoblastoid cells	713:740	Furthermore, human B-lymphoblastoid cells, which secrete IL-12, were found to contain an enzyme that carries out the C-mannosylation reaction.
10207176	2	31	theme	posttranslational	265:281	arg1	modification					283:294	a new, recently discovered posttranslational modification	238:294	a new, recently discovered posttranslational modification	238:294	In human RNase 2 this is the recognition motif for a new, recently discovered posttranslational modification, i.e., the C-glycosidic attachment of a mannosyl residue to the side chain of tryptophan.
10207176	2	31	theme	posttranslational	265:281	arg1	attachment					320:329	the C-glycosidic attachment	303:329	the C-glycosidic attachment of a mannosyl residue to the side chain of tryptophan	303:383	In human RNase 2 this is the recognition motif for a new, recently discovered posttranslational modification, i.e., the C-glycosidic attachment of a mannosyl residue to the side chain of tryptophan.
10207176	3	32	theme	IL-12	433:437	arg1	peptides					409:416	C-terminal peptides	398:416	C-terminal peptides of recombinant IL-12 (rHuIL-12)	398:448	Analysis of C-terminal peptides of recombinant IL-12 (rHuIL-12) by mass spectrometry and NMR spectroscopy revealed that Trp-319beta is (partially) C-mannosylated.
10207176	2	33	theme	mannosyl	336:343	arg1	residue					345:351	a mannosyl residue	334:351	a mannosyl residue	334:351	In human RNase 2 this is the recognition motif for a new, recently discovered posttranslational modification, i.e., the C-glycosidic attachment of a mannosyl residue to the side chain of tryptophan.
10207176	1	34	theme	human	102:106	arg1	interleukin					108:118	human interleukin 12	102:121	human interleukin 12 (IL-12)	102:129	The beta-chain of human interleukin 12 (IL-12) contains at position 319-322, the sequence Trp-x-x-Trp.
10207176	1	34	theme	human	102:106	arg1	IL-12					124:128	IL-12	124:128	IL-12	124:128	The beta-chain of human interleukin 12 (IL-12) contains at position 319-322, the sequence Trp-x-x-Trp.
10207176	2	35	theme	tryptophan	374:383	arg1	chain					365:369	the side chain	356:369	the side chain of tryptophan	356:383	In human RNase 2 this is the recognition motif for a new, recently discovered posttranslational modification, i.e., the C-glycosidic attachment of a mannosyl residue to the side chain of tryptophan.
10207176	0	36	theme	second	40:45	arg1	interleukin-12					18:31	Recombinant human interleukin-12	0:31	Recombinant human interleukin-12	0:31	Recombinant human interleukin-12 is the second example of a C-mannosylated protein.
10207176	0	36	theme	second	40:45	arg1	example					47:53	the second example	36:53	the second example of a C-mannosylated protein	36:81	Recombinant human interleukin-12 is the second example of a C-mannosylated protein.
10207176	8	37	attach	presence	1084:1091	arg1	tissues					1067:1073	tissues	1067:1073	tissues	1067:1073	However, the occurrence of the C-mannosyltransferase activity in a variety of cells and tissues, and the presence of the recognition motif in many proteins indicate that more C-mannosylated proteins may be found.
10207176	8	37	attach	presence	1084:1091	arg2	activity					1032:1039	the C-mannosyltransferase activity	1006:1039	the C-mannosyltransferase activity	1006:1039	However, the occurrence of the C-mannosyltransferase activity in a variety of cells and tissues, and the presence of the recognition motif in many proteins indicate that more C-mannosylated proteins may be found.
10207176	8	37	attach	presence	1084:1091	arg1	variety					1046:1052	a variety	1044:1052	a variety of cells and tissues	1044:1073	However, the occurrence of the C-mannosyltransferase activity in a variety of cells and tissues, and the presence of the recognition motif in many proteins indicate that more C-mannosylated proteins may be found.
10207176	8	37	attach	presence	1084:1091	arg2	motif					1112:1116	the recognition motif	1096:1116	the recognition motif	1096:1116	However, the occurrence of the C-mannosyltransferase activity in a variety of cells and tissues, and the presence of the recognition motif in many proteins indicate that more C-mannosylated proteins may be found.
10207176	8	37	attach	presence	1084:1091	arg1	proteins					1126:1133	many proteins	1121:1133	many proteins	1121:1133	However, the occurrence of the C-mannosyltransferase activity in a variety of cells and tissues, and the presence of the recognition motif in many proteins indicate that more C-mannosylated proteins may be found.
10207176	8	37	attach	presence	1084:1091	arg1	cells					1057:1061	cells	1057:1061	cells	1057:1061	However, the occurrence of the C-mannosyltransferase activity in a variety of cells and tissues, and the presence of the recognition motif in many proteins indicate that more C-mannosylated proteins may be found.
10207176	8	38	from	presence	1084:1091	arg1	variety					1046:1052	a variety	1044:1052	a variety of cells and tissues	1044:1073	However, the occurrence of the C-mannosyltransferase activity in a variety of cells and tissues, and the presence of the recognition motif in many proteins indicate that more C-mannosylated proteins may be found.
10207176	8	38	from	presence	1084:1091	arg1	tissues					1067:1073	tissues	1067:1073	tissues	1067:1073	However, the occurrence of the C-mannosyltransferase activity in a variety of cells and tissues, and the presence of the recognition motif in many proteins indicate that more C-mannosylated proteins may be found.
10207176	8	38	from	presence	1084:1091	arg1	proteins					1126:1133	many proteins	1121:1133	many proteins	1121:1133	However, the occurrence of the C-mannosyltransferase activity in a variety of cells and tissues, and the presence of the recognition motif in many proteins indicate that more C-mannosylated proteins may be found.
10207176	8	38	from	presence	1084:1091	arg1	cells					1057:1061	cells	1057:1061	cells	1057:1061	However, the occurrence of the C-mannosyltransferase activity in a variety of cells and tissues, and the presence of the recognition motif in many proteins indicate that more C-mannosylated proteins may be found.
10207176	2	39	from	motif	228:232	arg1	RNase					196:200	human RNase 2	190:202	human RNase 2	190:202	In human RNase 2 this is the recognition motif for a new, recently discovered posttranslational modification, i.e., the C-glycosidic attachment of a mannosyl residue to the side chain of tryptophan.
10207176	3	40	theme	C-terminal	398:407	arg1	peptides					409:416	C-terminal peptides	398:416	C-terminal peptides of recombinant IL-12 (rHuIL-12)	398:448	Analysis of C-terminal peptides of recombinant IL-12 (rHuIL-12) by mass spectrometry and NMR spectroscopy revealed that Trp-319beta is (partially) C-mannosylated.
10207176	3	41	theme	recombinant	421:431	arg1	rHuIL-12					440:447	rHuIL-12	440:447	rHuIL-12	440:447	Analysis of C-terminal peptides of recombinant IL-12 (rHuIL-12) by mass spectrometry and NMR spectroscopy revealed that Trp-319beta is (partially) C-mannosylated.
10207176	3	41	theme	recombinant	421:431	arg1	IL-12					433:437	recombinant IL-12	421:437	recombinant IL-12 (rHuIL-12)	421:448	Analysis of C-terminal peptides of recombinant IL-12 (rHuIL-12) by mass spectrometry and NMR spectroscopy revealed that Trp-319beta is (partially) C-mannosylated.
10207176	4	42	attach	derived	640:646	arg2	peptide					632:638	a synthetic peptide	620:638	a synthetic peptide derived from the same region of the protein	620:682	This finding was extended by in vitro mannosylation experiments, using a synthetic peptide derived from the same region of the protein as an acceptor.
10207176	4	42	attach	derived	640:646	arg1	region					662:667	the same region	653:667	the same region of the protein	653:682	This finding was extended by in vitro mannosylation experiments, using a synthetic peptide derived from the same region of the protein as an acceptor.
10207176	4	42	attach	derived	640:646	arg2	acceptor					690:697	an acceptor	687:697	an acceptor	687:697	This finding was extended by in vitro mannosylation experiments, using a synthetic peptide derived from the same region of the protein as an acceptor.
10207176	1	43	theme	sequence	165:172	arg1	Trp-x-x-Trp					174:184	the sequence Trp-x-x-Trp	161:184	the sequence Trp-x-x-Trp	161:184	The beta-chain of human interleukin 12 (IL-12) contains at position 319-322, the sequence Trp-x-x-Trp.
10207176	1	43	theme	sequence	165:172	arg1	position					143:150	position 319-322	143:158	position 319-322	143:158	The beta-chain of human interleukin 12 (IL-12) contains at position 319-322, the sequence Trp-x-x-Trp.
10207176	1	44	theme	interleukin	108:118	arg1	beta-chain					88:97	The beta-chain	84:97	The beta-chain of human interleukin 12 (IL-12)	84:129	The beta-chain of human interleukin 12 (IL-12) contains at position 319-322, the sequence Trp-x-x-Trp.
10207176	7	45	gly	C-mannosylated	955:968	arg1	protein					970:976	a C-mannosylated protein	953:976	a C-mannosylated protein	953:976	This is only the second report on a C-mannosylated protein.
10207176	8	46	theme	cells	1057:1061	arg1	variety					1046:1052	a variety	1044:1052	a variety of cells and tissues	1044:1073	However, the occurrence of the C-mannosyltransferase activity in a variety of cells and tissues, and the presence of the recognition motif in many proteins indicate that more C-mannosylated proteins may be found.
10207176	8	46	theme	cells	1057:1061	arg1	tissues					1067:1073	tissues	1067:1073	tissues	1067:1073	However, the occurrence of the C-mannosyltransferase activity in a variety of cells and tissues, and the presence of the recognition motif in many proteins indicate that more C-mannosylated proteins may be found.
10207176	8	46	theme	cells	1057:1061	arg1	cells					1057:1061	cells	1057:1061	cells	1057:1061	However, the occurrence of the C-mannosyltransferase activity in a variety of cells and tissues, and the presence of the recognition motif in many proteins indicate that more C-mannosylated proteins may be found.
10207176	2	47	theme	human	190:194	arg1	RNase					196:200	human RNase 2	190:202	human RNase 2	190:202	In human RNase 2 this is the recognition motif for a new, recently discovered posttranslational modification, i.e., the C-glycosidic attachment of a mannosyl residue to the side chain of tryptophan.
10207176	3	48	theme	mass	453:456	arg1	spectrometry					458:469	mass spectrometry	453:469	mass spectrometry	453:469	Analysis of C-terminal peptides of recombinant IL-12 (rHuIL-12) by mass spectrometry and NMR spectroscopy revealed that Trp-319beta is (partially) C-mannosylated.
10207176	4	49	dep	in	578:579	arg1	vitro					581:585	vitro	581:585	vitro	581:585	This finding was extended by in vitro mannosylation experiments, using a synthetic peptide derived from the same region of the protein as an acceptor.
10207176	7	50	theme	C-mannosylated	955:968	arg1	protein					970:976	a C-mannosylated protein	953:976	a C-mannosylated protein	953:976	This is only the second report on a C-mannosylated protein.
10207176	5	51	theme	C-mannosylation	817:831	arg1	reaction					833:840	the C-mannosylation reaction	813:840	the C-mannosylation reaction	813:840	Furthermore, human B-lymphoblastoid cells, which secrete IL-12, were found to contain an enzyme that carries out the C-mannosylation reaction.
10207176	8	52	theme	tissues	1067:1073	arg1	variety					1046:1052	a variety	1044:1052	a variety of cells and tissues	1044:1073	However, the occurrence of the C-mannosyltransferase activity in a variety of cells and tissues, and the presence of the recognition motif in many proteins indicate that more C-mannosylated proteins may be found.
10207176	8	52	theme	tissues	1067:1073	arg1	tissues					1067:1073	tissues	1067:1073	tissues	1067:1073	However, the occurrence of the C-mannosyltransferase activity in a variety of cells and tissues, and the presence of the recognition motif in many proteins indicate that more C-mannosylated proteins may be found.
10207176	8	52	theme	tissues	1067:1073	arg1	cells					1057:1061	cells	1057:1061	cells	1057:1061	However, the occurrence of the C-mannosyltransferase activity in a variety of cells and tissues, and the presence of the recognition motif in many proteins indicate that more C-mannosylated proteins may be found.
10207176	4	53	theme	protein	676:682	arg1	region					662:667	the same region	653:667	the same region of the protein	653:682	This finding was extended by in vitro mannosylation experiments, using a synthetic peptide derived from the same region of the protein as an acceptor.
10207176	0	54	theme	C-mannosylated	60:73	arg1	protein					75:81	a C-mannosylated protein	58:81	a C-mannosylated protein	58:81	Recombinant human interleukin-12 is the second example of a C-mannosylated protein.
10207176	2	55	theme	recognition	216:226	arg1	this					204:207	this	204:207	this	204:207	In human RNase 2 this is the recognition motif for a new, recently discovered posttranslational modification, i.e., the C-glycosidic attachment of a mannosyl residue to the side chain of tryptophan.
10207176	2	55	theme	recognition	216:226	arg1	motif					228:232	the recognition motif	212:232	the recognition motif for a new, recently discovered posttranslational modification, i.e., the C-glycosidic attachment of a mannosyl residue to the side chain of tryptophan	212:383	In human RNase 2 this is the recognition motif for a new, recently discovered posttranslational modification, i.e., the C-glycosidic attachment of a mannosyl residue to the side chain of tryptophan.
10207176	2	56	dep	new	240:242	arg1	discovered					254:263	discovered	254:263	discovered	254:263	In human RNase 2 this is the recognition motif for a new, recently discovered posttranslational modification, i.e., the C-glycosidic attachment of a mannosyl residue to the side chain of tryptophan.
10207176	5	57	theme	human	713:717	arg1	cells					736:740	human B-lymphoblastoid cells	713:740	human B-lymphoblastoid cells	713:740	Furthermore, human B-lymphoblastoid cells, which secrete IL-12, were found to contain an enzyme that carries out the C-mannosylation reaction.
10207176	4	58	theme	in	578:579	arg1	experiments					601:611	in vitro mannosylation experiments	578:611	in vitro mannosylation experiments	578:611	This finding was extended by in vitro mannosylation experiments, using a synthetic peptide derived from the same region of the protein as an acceptor.
6833285	4	0	theme	chain	471:475	arg1	moiety					456:461	the polypeptide moiety	440:461	the polypeptide moiety of this chain	440:475	Employing automated Edman degradation, the polypeptide moiety of this chain was shown to consist of 27 amino acid residues with an unequal distribution of the neutral and charged amino acid residues.
6833285	5	1	theme	first	605:609	arg1	whereas					638:644	whereas	638:644	whereas	638:644	The first 20 residues are uncharged, whereas the carboxyl-terminal heptapeptide contains all charged residues.
6833285	5	1	theme	first	605:609	arg1	uncharged					627:635	uncharged	627:635	uncharged	627:635	The first 20 residues are uncharged, whereas the carboxyl-terminal heptapeptide contains all charged residues.
6833285	5	1	theme	first	605:609	arg1	residues					614:621	The first 20 residues	601:621	The first 20 residues	601:621	The first 20 residues are uncharged, whereas the carboxyl-terminal heptapeptide contains all charged residues.
6833285	10	2	dep	47	1164:1165	arg1	45-148					1168:1173	45-148	1168:1173	45-148	1168:1173	47, 45-148) predicts that the B-chain has two beta-turns.
6833285	9	3	theme	polypeptide	1059:1069	arg1	chain					1071:1075	the polypeptide chain	1055:1075	the polypeptide chain	1055:1075	Evaluation of the polypeptide chain by the procedure of Chou and Fasman (Chou, P.Y., and Fasman, G.D. (1979) Adv. Enzymol.
6833285	12	4	theme	second	1369:1374	arg1	beta-turn					1376:1384	The second beta-turn	1365:1384	The second beta-turn	1365:1384	The second beta-turn probably includes the Cys residue which links the B- to the A-chain.
6833285	11	5	theme	carbohydrate	1235:1246	arg1	unit					1248:1251	the carbohydrate unit	1231:1251	the carbohydrate unit which is linked to the Ser residue located in the first beta-turn	1231:1317	Thereby, the carbohydrate unit which is linked to the Ser residue located in the first beta-turn appears to be directed away from the protein.
6833285	7	6	theme	B-chain	934:940	arg1	structure					917:925	The structure	913:925	The structure of the B-chain	913:940	The structure of the B-chain was found to be as follows.
6833285	4	7	theme	unequal	532:538	arg1	distribution					540:551	an unequal distribution	529:551	an unequal distribution of the neutral and charged amino acid residues	529:598	Employing automated Edman degradation, the polypeptide moiety of this chain was shown to consist of 27 amino acid residues with an unequal distribution of the neutral and charged amino acid residues.
6833285	5	8	theme	charged	694:700	arg1	residues					702:709	all charged residues	690:709	all charged residues	690:709	The first 20 residues are uncharged, whereas the carboxyl-terminal heptapeptide contains all charged residues.
6833285	13	9	theme	short	1542:1546	arg1	region					1562:1567	a short alpha-helical region	1540:1567	a short alpha-helical region	1540:1567	In agreement with the CD analysis, the B-chain lacks beta-conformation but possesses a short alpha-helical region.
6833285	11	10	from	beta-turn	1309:1317	arg1	located					1288:1294	located	1288:1294	located	1288:1294	Thereby, the carbohydrate unit which is linked to the Ser residue located in the first beta-turn appears to be directed away from the protein.
6833285	0	11	gly	2HS-glycoprotein	54:69	arg1	2HS-glycoprotein					54:69	human plasma alpha 2HS-glycoprotein	35:69	human plasma alpha 2HS-glycoprotein	35:69	Characterization of the B-chain of human plasma alpha 2HS-glycoprotein.
6833285	13	12	theme	alpha-helical	1548:1560	arg1	region					1562:1567	a short alpha-helical region	1540:1567	a short alpha-helical region	1540:1567	In agreement with the CD analysis, the B-chain lacks beta-conformation but possesses a short alpha-helical region.
6833285	9	13	theme	Fasman	1106:1111	arg1	procedure					1084:1092	the procedure	1080:1092	the procedure of Chou and Fasman (Chou, P.Y., and Fasman, G.D. (1979) Adv. Enzymol	1080:1161	Evaluation of the polypeptide chain by the procedure of Chou and Fasman (Chou, P.Y., and Fasman, G.D. (1979) Adv. Enzymol.
6833285	5	14	contain	contains	681:688	arg1	heptapeptide					668:679	the carboxyl-terminal heptapeptide	646:679	the carboxyl-terminal heptapeptide	646:679	The first 20 residues are uncharged, whereas the carboxyl-terminal heptapeptide contains all charged residues.
6833285	5	14	contain	contains	681:688	arg2	residues					702:709	all charged residues	690:709	all charged residues	690:709	The first 20 residues are uncharged, whereas the carboxyl-terminal heptapeptide contains all charged residues.
6833285	11	15	theme	located	1288:1294	arg1	residue					1280:1286	the Ser residue	1272:1286	the Ser residue located in the first beta-turn	1272:1317	Thereby, the carbohydrate unit which is linked to the Ser residue located in the first beta-turn appears to be directed away from the protein.
6833285	5	16	dep	uncharged	627:635	arg1	whereas					638:644	whereas	638:644	whereas	638:644	The first 20 residues are uncharged, whereas the carboxyl-terminal heptapeptide contains all charged residues.
6833285	5	16	dep	uncharged	627:635	arg1	uncharged					627:635	uncharged	627:635	uncharged	627:635	The first 20 residues are uncharged, whereas the carboxyl-terminal heptapeptide contains all charged residues.
6833285	5	16	dep	uncharged	627:635	arg1	residues					614:621	The first 20 residues	601:621	The first 20 residues	601:621	The first 20 residues are uncharged, whereas the carboxyl-terminal heptapeptide contains all charged residues.
6833285	2	17	theme	alpha	148:152	arg1	protein					194:200	a normal human plasma protein	172:200	a normal human plasma protein	172:200	alpha 2HS-Glycoprotein, a normal human plasma protein, was recently shown to consist of two polypeptide chains.
6833285	2	17	theme	alpha	148:152	arg1	2HS-Glycoprotein					154:169	alpha 2HS-Glycoprotein	148:169	alpha 2HS-Glycoprotein	148:169	alpha 2HS-Glycoprotein, a normal human plasma protein, was recently shown to consist of two polypeptide chains.
6833285	6	18	attach	linked	883:888	arg2	trisaccharide					788:800	a trisaccharide	786:800	a trisaccharide consisting of sialic acid, galactose, and N-acetylgalactosamine O-glycosidically linked to serine (residue 6)	786:910	Utilizing 500-MHz 1H-NMR spectroscopy, the carbohydrate unit proved to be a trisaccharide consisting of sialic acid, galactose, and N-acetylgalactosamine O-glycosidically linked to serine (residue 6).
6833285	6	18	attach	linked	883:888	arg1	residue					901:907	residue 6	901:909	residue 6	901:909	Utilizing 500-MHz 1H-NMR spectroscopy, the carbohydrate unit proved to be a trisaccharide consisting of sialic acid, galactose, and N-acetylgalactosamine O-glycosidically linked to serine (residue 6).
6833285	6	18	attach	linked	883:888	arg1	serine					893:898	serine	893:898	serine (residue 6)	893:910	Utilizing 500-MHz 1H-NMR spectroscopy, the carbohydrate unit proved to be a trisaccharide consisting of sialic acid, galactose, and N-acetylgalactosamine O-glycosidically linked to serine (residue 6).
6833285	6	18	attach	linked	883:888	arg2	unit					768:771	the carbohydrate unit	751:771	the carbohydrate unit	751:771	Utilizing 500-MHz 1H-NMR spectroscopy, the carbohydrate unit proved to be a trisaccharide consisting of sialic acid, galactose, and N-acetylgalactosamine O-glycosidically linked to serine (residue 6).
6833285	13	19	with	agreement	1458:1466	arg1	analysis					1480:1487	the CD analysis	1473:1487	the CD analysis	1473:1487	In agreement with the CD analysis, the B-chain lacks beta-conformation but possesses a short alpha-helical region.
6833285	13	20	theme	CD	1477:1478	arg1	analysis					1480:1487	the CD analysis	1473:1487	the CD analysis	1473:1487	In agreement with the CD analysis, the B-chain lacks beta-conformation but possesses a short alpha-helical region.
6833285	1	21	theme	complete	76:83	arg1	sequence					96:103	The complete amino acid sequence	72:103	The complete amino acid sequence	72:103	The complete amino acid sequence and primary structure of its heteroglycan.
6833285	11	22	theme	Ser	1276:1278	arg1	residue					1280:1286	the Ser residue	1272:1286	the Ser residue located in the first beta-turn	1272:1317	Thereby, the carbohydrate unit which is linked to the Ser residue located in the first beta-turn appears to be directed away from the protein.
6833285	8	23	theme	molecular	1000:1008	arg1	3386					1035:1038	3386	1035:1038	3386	1035:1038	(formula; see text) Thus, the molecular weight of the B-chain is 3386.
6833285	8	23	theme	molecular	1000:1008	arg1	weight					1010:1015	the molecular weight	996:1015	the molecular weight of the B-chain	996:1030	(formula; see text) Thus, the molecular weight of the B-chain is 3386.
6833285	1	24	theme	amino	85:89	arg1	sequence					96:103	The complete amino acid sequence	72:103	The complete amino acid sequence	72:103	The complete amino acid sequence and primary structure of its heteroglycan.
6833285	4	25	theme	polypeptide	444:454	arg1	moiety					456:461	the polypeptide moiety	440:461	the polypeptide moiety of this chain	440:475	Employing automated Edman degradation, the polypeptide moiety of this chain was shown to consist of 27 amino acid residues with an unequal distribution of the neutral and charged amino acid residues.
6833285	3	26	theme	B-chain	392:398	arg1	structure					375:383	the complete primary structure	354:383	the complete primary structure of the B-chain	354:398	In the present study, we have separated these two chains from one another and have elucidated the complete primary structure of the B-chain.
6833285	3	27	theme	complete	358:365	arg1	structure					375:383	the complete primary structure	354:383	the complete primary structure of the B-chain	354:398	In the present study, we have separated these two chains from one another and have elucidated the complete primary structure of the B-chain.
6833285	6	28	theme	carbohydrate	755:766	arg1	unit					768:771	the carbohydrate unit	751:771	the carbohydrate unit	751:771	Utilizing 500-MHz 1H-NMR spectroscopy, the carbohydrate unit proved to be a trisaccharide consisting of sialic acid, galactose, and N-acetylgalactosamine O-glycosidically linked to serine (residue 6).
6833285	6	28	theme	carbohydrate	755:766	arg1	trisaccharide					788:800	a trisaccharide	786:800	a trisaccharide consisting of sialic acid, galactose, and N-acetylgalactosamine O-glycosidically linked to serine (residue 6)	786:910	Utilizing 500-MHz 1H-NMR spectroscopy, the carbohydrate unit proved to be a trisaccharide consisting of sialic acid, galactose, and N-acetylgalactosamine O-glycosidically linked to serine (residue 6).
6833285	1	29	theme	acid	91:94	arg1	sequence					96:103	The complete amino acid sequence	72:103	The complete amino acid sequence	72:103	The complete amino acid sequence and primary structure of its heteroglycan.
6833285	4	30	theme	Edman	421:425	arg1	degradation					427:437	automated Edman degradation	411:437	automated Edman degradation	411:437	Employing automated Edman degradation, the polypeptide moiety of this chain was shown to consist of 27 amino acid residues with an unequal distribution of the neutral and charged amino acid residues.
6833285	0	31	theme	B-chain	24:30	arg1	Characterization					0:15	Characterization	0:15	Characterization of the B-chain of human plasma alpha 2HS-glycoprotein.	0:70	Characterization of the B-chain of human plasma alpha 2HS-glycoprotein.
6833285	4	32	theme	acid	510:513	arg1	residues					515:522	27 amino acid residues	501:522	27 amino acid residues	501:522	Employing automated Edman degradation, the polypeptide moiety of this chain was shown to consist of 27 amino acid residues with an unequal distribution of the neutral and charged amino acid residues.
6833285	5	33	theme	carboxyl-terminal	650:666	arg1	heptapeptide					668:679	the carboxyl-terminal heptapeptide	646:679	the carboxyl-terminal heptapeptide	646:679	The first 20 residues are uncharged, whereas the carboxyl-terminal heptapeptide contains all charged residues.
6833285	9	34	theme	Chou	1097:1100	arg1	procedure					1084:1092	the procedure	1080:1092	the procedure of Chou and Fasman (Chou, P.Y., and Fasman, G.D. (1979) Adv. Enzymol	1080:1161	Evaluation of the polypeptide chain by the procedure of Chou and Fasman (Chou, P.Y., and Fasman, G.D. (1979) Adv. Enzymol.
6833285	4	35	theme	residues	591:598	arg1	distribution					540:551	an unequal distribution	529:551	an unequal distribution of the neutral and charged amino acid residues	529:598	Employing automated Edman degradation, the polypeptide moiety of this chain was shown to consist of 27 amino acid residues with an unequal distribution of the neutral and charged amino acid residues.
6833285	10	36	contain	has	1202:1204	arg1	B-chain					1194:1200	the B-chain	1190:1200	the B-chain	1190:1200	47, 45-148) predicts that the B-chain has two beta-turns.
6833285	10	36	contain	has	1202:1204	arg2	beta-turns					1210:1219	two beta-turns	1206:1219	two beta-turns	1206:1219	47, 45-148) predicts that the B-chain has two beta-turns.
6833285	3	37	theme	present	267:273	arg1	study					275:279	the present study	263:279	the present study	263:279	In the present study, we have separated these two chains from one another and have elucidated the complete primary structure of the B-chain.
6833285	2	38	theme	human	181:185	arg1	protein					194:200	a normal human plasma protein	172:200	a normal human plasma protein	172:200	alpha 2HS-Glycoprotein, a normal human plasma protein, was recently shown to consist of two polypeptide chains.
6833285	2	38	theme	human	181:185	arg1	2HS-Glycoprotein					154:169	alpha 2HS-Glycoprotein	148:169	alpha 2HS-Glycoprotein	148:169	alpha 2HS-Glycoprotein, a normal human plasma protein, was recently shown to consist of two polypeptide chains.
6833285	4	39	theme	acid	586:589	arg1	residues					591:598	the neutral and charged amino acid residues	556:598	the neutral and charged amino acid residues	556:598	Employing automated Edman degradation, the polypeptide moiety of this chain was shown to consist of 27 amino acid residues with an unequal distribution of the neutral and charged amino acid residues.
6833285	0	40	theme	human	35:39	arg1	2HS-glycoprotein					54:69	human plasma alpha 2HS-glycoprotein	35:69	human plasma alpha 2HS-glycoprotein	35:69	Characterization of the B-chain of human plasma alpha 2HS-glycoprotein.
6833285	8	41	theme	B-chain	1024:1030	arg1	3386					1035:1038	3386	1035:1038	3386	1035:1038	(formula; see text) Thus, the molecular weight of the B-chain is 3386.
6833285	8	41	theme	B-chain	1024:1030	arg1	weight					1010:1015	the molecular weight	996:1015	the molecular weight of the B-chain	996:1030	(formula; see text) Thus, the molecular weight of the B-chain is 3386.
6833285	2	42	theme	normal	174:179	arg1	protein					194:200	a normal human plasma protein	172:200	a normal human plasma protein	172:200	alpha 2HS-Glycoprotein, a normal human plasma protein, was recently shown to consist of two polypeptide chains.
6833285	2	42	theme	normal	174:179	arg1	2HS-Glycoprotein					154:169	alpha 2HS-Glycoprotein	148:169	alpha 2HS-Glycoprotein	148:169	alpha 2HS-Glycoprotein, a normal human plasma protein, was recently shown to consist of two polypeptide chains.
6833285	11	43	theme	first	1303:1307	arg1	beta-turn					1309:1317	the first beta-turn	1299:1317	the first beta-turn	1299:1317	Thereby, the carbohydrate unit which is linked to the Ser residue located in the first beta-turn appears to be directed away from the protein.
6833285	8	44	dep	3386	1035:1038	arg1	see					980:982	see	980:982	see text	980:987	(formula; see text) Thus, the molecular weight of the B-chain is 3386.
6833285	8	44	dep	3386	1035:1038	arg1	formula					971:977	formula	971:977	formula; see text	971:987	(formula; see text) Thus, the molecular weight of the B-chain is 3386.
6833285	3	45	theme	primary	367:373	arg1	structure					375:383	the complete primary structure	354:383	the complete primary structure of the B-chain	354:398	In the present study, we have separated these two chains from one another and have elucidated the complete primary structure of the B-chain.
6833285	0	46	theme	2HS-glycoprotein	54:69	arg1	B-chain					24:30	the B-chain	20:30	the B-chain of human plasma alpha 2HS-glycoprotein	20:69	Characterization of the B-chain of human plasma alpha 2HS-glycoprotein.
6833285	11	47	attach	linked	1262:1267	arg1	residue					1280:1286	the Ser residue	1272:1286	the Ser residue located in the first beta-turn	1272:1317	Thereby, the carbohydrate unit which is linked to the Ser residue located in the first beta-turn appears to be directed away from the protein.
6833285	11	47	attach	linked	1262:1267	arg2	unit					1248:1251	the carbohydrate unit	1231:1251	the carbohydrate unit which is linked to the Ser residue located in the first beta-turn	1231:1317	Thereby, the carbohydrate unit which is linked to the Ser residue located in the first beta-turn appears to be directed away from the protein.
6833285	1	48	theme	primary	109:115	arg1	structure					117:125	primary structure	109:125	primary structure	109:125	The complete amino acid sequence and primary structure of its heteroglycan.
6833285	0	49	theme	plasma	41:46	arg1	2HS-glycoprotein					54:69	human plasma alpha 2HS-glycoprotein	35:69	human plasma alpha 2HS-glycoprotein	35:69	Characterization of the B-chain of human plasma alpha 2HS-glycoprotein.
6833285	4	50	theme	amino	504:508	arg1	residues					515:522	27 amino acid residues	501:522	27 amino acid residues	501:522	Employing automated Edman degradation, the polypeptide moiety of this chain was shown to consist of 27 amino acid residues with an unequal distribution of the neutral and charged amino acid residues.
6833285	3	51	dep	one	322:324	arg1	another					326:332	another	326:332	another	326:332	In the present study, we have separated these two chains from one another and have elucidated the complete primary structure of the B-chain.
6833285	6	52	theme	1H-NMR	730:735	arg1	spectroscopy					737:748	500-MHz 1H-NMR spectroscopy	722:748	500-MHz 1H-NMR spectroscopy	722:748	Utilizing 500-MHz 1H-NMR spectroscopy, the carbohydrate unit proved to be a trisaccharide consisting of sialic acid, galactose, and N-acetylgalactosamine O-glycosidically linked to serine (residue 6).
6833285	6	53	theme	sialic	816:821	arg1	acid					823:826	sialic acid	816:826	sialic acid	816:826	Utilizing 500-MHz 1H-NMR spectroscopy, the carbohydrate unit proved to be a trisaccharide consisting of sialic acid, galactose, and N-acetylgalactosamine O-glycosidically linked to serine (residue 6).
6833285	6	54	theme	500-MHz	722:728	arg1	spectroscopy					737:748	500-MHz 1H-NMR spectroscopy	722:748	500-MHz 1H-NMR spectroscopy	722:748	Utilizing 500-MHz 1H-NMR spectroscopy, the carbohydrate unit proved to be a trisaccharide consisting of sialic acid, galactose, and N-acetylgalactosamine O-glycosidically linked to serine (residue 6).
6833285	9	55	theme	chain	1071:1075	arg1	Evaluation					1041:1050	Evaluation	1041:1050	Evaluation of the polypeptide chain by the procedure of Chou and Fasman (Chou, P.Y., and Fasman, G.D. (1979) Adv. Enzymol.	1041:1162	Evaluation of the polypeptide chain by the procedure of Chou and Fasman (Chou, P.Y., and Fasman, G.D. (1979) Adv. Enzymol.
6833285	4	56	theme	automated	411:419	arg1	degradation					427:437	automated Edman degradation	411:437	automated Edman degradation	411:437	Employing automated Edman degradation, the polypeptide moiety of this chain was shown to consist of 27 amino acid residues with an unequal distribution of the neutral and charged amino acid residues.
6833285	2	57	theme	polypeptide	240:250	arg1	chains					252:257	two polypeptide chains	236:257	two polypeptide chains	236:257	alpha 2HS-Glycoprotein, a normal human plasma protein, was recently shown to consist of two polypeptide chains.
6833285	13	58	contain	possesses	1530:1538	arg2	region					1562:1567	a short alpha-helical region	1540:1567	a short alpha-helical region	1540:1567	In agreement with the CD analysis, the B-chain lacks beta-conformation but possesses a short alpha-helical region.
6833285	13	58	contain	possesses	1530:1538	arg1	B-chain					1494:1500	the B-chain	1490:1500	the B-chain	1490:1500	In agreement with the CD analysis, the B-chain lacks beta-conformation but possesses a short alpha-helical region.
6833285	9	59	dep	Chou	1097:1100	arg1	Enzymol					1155:1161	Enzymol	1155:1161	Enzymol	1155:1161	Evaluation of the polypeptide chain by the procedure of Chou and Fasman (Chou, P.Y., and Fasman, G.D. (1979) Adv. Enzymol.
6833285	4	60	theme	neutral	560:566	arg1	residues					591:598	the neutral and charged amino acid residues	556:598	the neutral and charged amino acid residues	556:598	Employing automated Edman degradation, the polypeptide moiety of this chain was shown to consist of 27 amino acid residues with an unequal distribution of the neutral and charged amino acid residues.
6833285	2	61	theme	plasma	187:192	arg1	protein					194:200	a normal human plasma protein	172:200	a normal human plasma protein	172:200	alpha 2HS-Glycoprotein, a normal human plasma protein, was recently shown to consist of two polypeptide chains.
6833285	2	61	theme	plasma	187:192	arg1	2HS-Glycoprotein					154:169	alpha 2HS-Glycoprotein	148:169	alpha 2HS-Glycoprotein	148:169	alpha 2HS-Glycoprotein, a normal human plasma protein, was recently shown to consist of two polypeptide chains.
6833285	11	62	from	located	1288:1294	arg1	beta-turn					1309:1317	the first beta-turn	1299:1317	the first beta-turn	1299:1317	Thereby, the carbohydrate unit which is linked to the Ser residue located in the first beta-turn appears to be directed away from the protein.
6833285	12	63	attach	links	1426:1430	arg2	residue					1412:1418	the Cys residue	1404:1418	the Cys residue which links the B- to the A-chain	1404:1452	The second beta-turn probably includes the Cys residue which links the B- to the A-chain.
6833285	12	63	attach	links	1426:1430	arg1	A-chain					1446:1452	the A-chain	1442:1452	the A-chain	1442:1452	The second beta-turn probably includes the Cys residue which links the B- to the A-chain.
6833285	1	64	theme	heteroglycan	134:145	arg1	sequence					96:103	The complete amino acid sequence	72:103	The complete amino acid sequence	72:103	The complete amino acid sequence and primary structure of its heteroglycan.
6833285	1	64	theme	heteroglycan	134:145	arg1	structure					117:125	primary structure	109:125	primary structure	109:125	The complete amino acid sequence and primary structure of its heteroglycan.
6833285	4	65	theme	amino	580:584	arg1	residues					591:598	the neutral and charged amino acid residues	556:598	the neutral and charged amino acid residues	556:598	Employing automated Edman degradation, the polypeptide moiety of this chain was shown to consist of 27 amino acid residues with an unequal distribution of the neutral and charged amino acid residues.
6833285	0	66	theme	alpha	48:52	arg1	2HS-glycoprotein					54:69	human plasma alpha 2HS-glycoprotein	35:69	human plasma alpha 2HS-glycoprotein	35:69	Characterization of the B-chain of human plasma alpha 2HS-glycoprotein.
6833285	12	67	theme	Cys	1408:1410	arg1	residue					1412:1418	the Cys residue	1404:1418	the Cys residue which links the B- to the A-chain	1404:1452	The second beta-turn probably includes the Cys residue which links the B- to the A-chain.
6833285	9	68	dep	P.Y.	1120:1123	arg1	1979					1144:1147	1979	1144:1147	1979	1144:1147	Evaluation of the polypeptide chain by the procedure of Chou and Fasman (Chou, P.Y., and Fasman, G.D. (1979) Adv. Enzymol.
6833285	4	69	theme	charged	572:578	arg1	residues					591:598	the neutral and charged amino acid residues	556:598	the neutral and charged amino acid residues	556:598	Employing automated Edman degradation, the polypeptide moiety of this chain was shown to consist of 27 amino acid residues with an unequal distribution of the neutral and charged amino acid residues.
10861392	0	0	theme	fusion	78:83	arg1	protein					85:91	a recombinant fusion protein	64:91	a recombinant fusion protein expressed in BHK cells	64:114	Metabolic shifts do not influence the glycosylation patterns of a recombinant fusion protein expressed in BHK cells.
10861392	5	1	theme	significant	687:697	arg1	differences					699:709	No significant differences	684:709	No significant differences in the oligosaccharide structures	684:743	No significant differences in the oligosaccharide structures were detected from the IgG-IL2 fusion protein preparations obtained by growing cells under the different metabolic states.
10861392	7	2	theme	oligosaccharide	1095:1109	arg1	present					1131:1137	present	1131:1137	present	1131:1137	Although the O-linked oligosaccharide structures that are present in the IL2 moiety of the protein were studied with less detail, the data obtained from the hydrazinolysis procedure point to the presence of the classical NeuAcalpha2-3Galbeta1-3GalNAc structure.
10861392	7	2	theme	oligosaccharide	1095:1109	arg1	structures					1111:1120	the O-linked oligosaccharide structures	1082:1120	the O-linked oligosaccharide structures that are present in the IL2 moiety of the protein	1082:1170	Although the O-linked oligosaccharide structures that are present in the IL2 moiety of the protein were studied with less detail, the data obtained from the hydrazinolysis procedure point to the presence of the classical NeuAcalpha2-3Galbeta1-3GalNAc structure.
10861392	8	3	link	N-linked	1465:1472	arg1	oligosaccharides					1474:1489	N-linked oligosaccharides	1465:1489	N-linked oligosaccharides	1465:1489	Here, it is shown that under different defined cellular metabolic states, the quality of a recombinant product in terms of O- and N-linked oligosaccharides is stable, even after a prolonged cultivation period.
10861392	1	4	theme	human	143:147	arg1	protein					164:170	a human IgG-IL2 fusion protein	141:170	a human IgG-IL2 fusion protein	141:170	BHK-21 cells expressing a human IgG-IL2 fusion protein, with potential application in tumor-targeted therapy, were grown under different nutrient conditions in a continuous system for a time period of 80 days.
10861392	4	5	theme	growth	541:546	arg1	conditions					548:557	metabolically shifted growth conditions	519:557	metabolically shifted growth conditions	519:557	Cell-specific productivity was maintained under metabolically shifted growth conditions and at the same time an almost identical intracellular ATP content, obtained by in vivo (31)P NMR experiments, was observed.
10861392	0	6	theme	recombinant	66:76	arg1	protein					85:91	a recombinant fusion protein	64:91	a recombinant fusion protein expressed in BHK cells	64:114	Metabolic shifts do not influence the glycosylation patterns of a recombinant fusion protein expressed in BHK cells.
10861392	1	7	theme	days	321:324	arg1	period					308:313	a time period	301:313	a time period of 80 days	301:324	BHK-21 cells expressing a human IgG-IL2 fusion protein, with potential application in tumor-targeted therapy, were grown under different nutrient conditions in a continuous system for a time period of 80 days.
10861392	9	8	theme	ATP	1580:1582	arg1	levels					1584:1589	unaffected intracellular ATP levels	1555:1589	unaffected intracellular ATP levels under the different metabolic states	1555:1626	Moreover, unaffected intracellular ATP levels under the different metabolic states were observed.
10861392	1	9	theme	IgG-IL2	149:155	arg1	protein					164:170	a human IgG-IL2 fusion protein	141:170	a human IgG-IL2 fusion protein	141:170	BHK-21 cells expressing a human IgG-IL2 fusion protein, with potential application in tumor-targeted therapy, were grown under different nutrient conditions in a continuous system for a time period of 80 days.
10861392	1	10	theme	different	244:252	arg1	conditions					263:272	different nutrient conditions	244:272	different nutrient conditions	244:272	BHK-21 cells expressing a human IgG-IL2 fusion protein, with potential application in tumor-targeted therapy, were grown under different nutrient conditions in a continuous system for a time period of 80 days.
10861392	8	11	theme	oligosaccharides	1474:1489	arg1	terms					1449:1453	terms	1449:1453	terms of O- and N-linked oligosaccharides	1449:1489	Here, it is shown that under different defined cellular metabolic states, the quality of a recombinant product in terms of O- and N-linked oligosaccharides is stable, even after a prolonged cultivation period.
10861392	7	12	attach	present	1131:1137	arg2	structures					1111:1120	the O-linked oligosaccharide structures	1082:1120	the O-linked oligosaccharide structures that are present in the IL2 moiety of the protein	1082:1170	Although the O-linked oligosaccharide structures that are present in the IL2 moiety of the protein were studied with less detail, the data obtained from the hydrazinolysis procedure point to the presence of the classical NeuAcalpha2-3Galbeta1-3GalNAc structure.
10861392	7	12	attach	present	1131:1137	arg1	moiety					1150:1155	the IL2 moiety	1142:1155	the IL2 moiety of the protein	1142:1170	Although the O-linked oligosaccharide structures that are present in the IL2 moiety of the protein were studied with less detail, the data obtained from the hydrazinolysis procedure point to the presence of the classical NeuAcalpha2-3Galbeta1-3GalNAc structure.
10861392	7	12	attach	present	1131:1137	arg2	present					1131:1137	present	1131:1137	present	1131:1137	Although the O-linked oligosaccharide structures that are present in the IL2 moiety of the protein were studied with less detail, the data obtained from the hydrazinolysis procedure point to the presence of the classical NeuAcalpha2-3Galbeta1-3GalNAc structure.
10861392	6	13	link	alpha1-6-linked	982:996	arg1	fucose					998:1003	core alpha1-6-linked fucose	977:1003	core alpha1-6-linked fucose	977:1003	By using oligosaccharide mapping and MALDI/TOF-MS, only neutral diantennary oligosaccharides with or without core alpha1-6-linked fucose were detected that carried no, one or two beta1-4-linked galactose.
10861392	9	14	theme	unaffected	1555:1564	arg1	levels					1584:1589	unaffected intracellular ATP levels	1555:1589	unaffected intracellular ATP levels under the different metabolic states	1555:1626	Moreover, unaffected intracellular ATP levels under the different metabolic states were observed.
10861392	1	15	theme	nutrient	254:261	arg1	conditions					263:272	different nutrient conditions	244:272	different nutrient conditions	244:272	BHK-21 cells expressing a human IgG-IL2 fusion protein, with potential application in tumor-targeted therapy, were grown under different nutrient conditions in a continuous system for a time period of 80 days.
10861392	0	16	theme	protein	85:91	arg1	patterns					52:59	the glycosylation patterns	34:59	the glycosylation patterns of a recombinant fusion protein expressed in BHK cells	34:114	Metabolic shifts do not influence the glycosylation patterns of a recombinant fusion protein expressed in BHK cells.
10861392	7	17	theme	O-linked	1086:1093	arg1	present					1131:1137	present	1131:1137	present	1131:1137	Although the O-linked oligosaccharide structures that are present in the IL2 moiety of the protein were studied with less detail, the data obtained from the hydrazinolysis procedure point to the presence of the classical NeuAcalpha2-3Galbeta1-3GalNAc structure.
10861392	7	17	theme	O-linked	1086:1093	arg1	structures					1111:1120	the O-linked oligosaccharide structures	1082:1120	the O-linked oligosaccharide structures that are present in the IL2 moiety of the protein	1082:1170	Although the O-linked oligosaccharide structures that are present in the IL2 moiety of the protein were studied with less detail, the data obtained from the hydrazinolysis procedure point to the presence of the classical NeuAcalpha2-3Galbeta1-3GalNAc structure.
10861392	5	18	theme	different	840:848	arg1	states					860:865	the different metabolic states	836:865	the different metabolic states	836:865	No significant differences in the oligosaccharide structures were detected from the IgG-IL2 fusion protein preparations obtained by growing cells under the different metabolic states.
10861392	7	19	theme	hydrazinolysis	1230:1243	arg1	procedure					1245:1253	the hydrazinolysis procedure	1226:1253	the hydrazinolysis procedure	1226:1253	Although the O-linked oligosaccharide structures that are present in the IL2 moiety of the protein were studied with less detail, the data obtained from the hydrazinolysis procedure point to the presence of the classical NeuAcalpha2-3Galbeta1-3GalNAc structure.
10861392	0	20	theme	BHK	106:108	arg1	cells					110:114	BHK cells	106:114	BHK cells	106:114	Metabolic shifts do not influence the glycosylation patterns of a recombinant fusion protein expressed in BHK cells.
10861392	7	21	link	O-linked	1086:1093	arg1	present					1131:1137	present	1131:1137	present	1131:1137	Although the O-linked oligosaccharide structures that are present in the IL2 moiety of the protein were studied with less detail, the data obtained from the hydrazinolysis procedure point to the presence of the classical NeuAcalpha2-3Galbeta1-3GalNAc structure.
10861392	7	21	link	O-linked	1086:1093	arg1	structures					1111:1120	the O-linked oligosaccharide structures	1082:1120	the O-linked oligosaccharide structures that are present in the IL2 moiety of the protein	1082:1170	Although the O-linked oligosaccharide structures that are present in the IL2 moiety of the protein were studied with less detail, the data obtained from the hydrazinolysis procedure point to the presence of the classical NeuAcalpha2-3Galbeta1-3GalNAc structure.
10861392	4	22	dep	in	639:640	arg1	vivo					642:645	vivo	642:645	vivo	642:645	Cell-specific productivity was maintained under metabolically shifted growth conditions and at the same time an almost identical intracellular ATP content, obtained by in vivo (31)P NMR experiments, was observed.
10861392	4	22	dep	in	639:640	arg1	31					648:649	31	648:649	31	648:649	Cell-specific productivity was maintained under metabolically shifted growth conditions and at the same time an almost identical intracellular ATP content, obtained by in vivo (31)P NMR experiments, was observed.
10861392	1	23	theme	fusion	157:162	arg1	protein					164:170	a human IgG-IL2 fusion protein	141:170	a human IgG-IL2 fusion protein	141:170	BHK-21 cells expressing a human IgG-IL2 fusion protein, with potential application in tumor-targeted therapy, were grown under different nutrient conditions in a continuous system for a time period of 80 days.
10861392	7	24	theme	protein	1164:1170	arg1	moiety					1150:1155	the IL2 moiety	1142:1155	the IL2 moiety of the protein	1142:1170	Although the O-linked oligosaccharide structures that are present in the IL2 moiety of the protein were studied with less detail, the data obtained from the hydrazinolysis procedure point to the presence of the classical NeuAcalpha2-3Galbeta1-3GalNAc structure.
10861392	5	25	theme	metabolic	850:858	arg1	states					860:865	the different metabolic states	836:865	the different metabolic states	836:865	No significant differences in the oligosaccharide structures were detected from the IgG-IL2 fusion protein preparations obtained by growing cells under the different metabolic states.
10861392	4	26	theme	Cell-specific	471:483	arg1	productivity					485:496	Cell-specific productivity	471:496	Cell-specific productivity	471:496	Cell-specific productivity was maintained under metabolically shifted growth conditions and at the same time an almost identical intracellular ATP content, obtained by in vivo (31)P NMR experiments, was observed.
10861392	8	27	theme	defined	1374:1380	arg1	states					1401:1406	different defined cellular metabolic states	1364:1406	different defined cellular metabolic states	1364:1406	Here, it is shown that under different defined cellular metabolic states, the quality of a recombinant product in terms of O- and N-linked oligosaccharides is stable, even after a prolonged cultivation period.
10861392	3	28	theme	mM	379:380	arg1	concentrations					383:396	2 mM) concentrations	377:396	2 mM) concentrations	377:396	2 mM) concentrations, a shift toward an energetically more efficient metabolism was observed.
10861392	3	28	theme	mM	379:380	arg1	shift					401:405	a shift	399:405	a shift toward an energetically more efficient metabolism	399:455	2 mM) concentrations, a shift toward an energetically more efficient metabolism was observed.
10861392	7	29	theme	less	1190:1193	arg1	detail					1195:1200	less detail	1190:1200	less detail	1190:1200	Although the O-linked oligosaccharide structures that are present in the IL2 moiety of the protein were studied with less detail, the data obtained from the hydrazinolysis procedure point to the presence of the classical NeuAcalpha2-3Galbeta1-3GalNAc structure.
10861392	8	30	theme	prolonged	1515:1523	arg1	period					1537:1542	a prolonged cultivation period	1513:1542	a prolonged cultivation period	1513:1542	Here, it is shown that under different defined cellular metabolic states, the quality of a recombinant product in terms of O- and N-linked oligosaccharides is stable, even after a prolonged cultivation period.
10861392	7	31	from	moiety	1150:1155	arg1	present					1131:1137	present	1131:1137	present	1131:1137	Although the O-linked oligosaccharide structures that are present in the IL2 moiety of the protein were studied with less detail, the data obtained from the hydrazinolysis procedure point to the presence of the classical NeuAcalpha2-3Galbeta1-3GalNAc structure.
10861392	7	31	from	moiety	1150:1155	arg1	structures					1111:1120	the O-linked oligosaccharide structures	1082:1120	the O-linked oligosaccharide structures that are present in the IL2 moiety of the protein	1082:1170	Although the O-linked oligosaccharide structures that are present in the IL2 moiety of the protein were studied with less detail, the data obtained from the hydrazinolysis procedure point to the presence of the classical NeuAcalpha2-3Galbeta1-3GalNAc structure.
10861392	9	32	theme	intracellular	1566:1578	arg1	levels					1584:1589	unaffected intracellular ATP levels	1555:1589	unaffected intracellular ATP levels under the different metabolic states	1555:1626	Moreover, unaffected intracellular ATP levels under the different metabolic states were observed.
10861392	0	33	theme	Metabolic	0:8	arg1	shifts					10:15	Metabolic shifts	0:15	Metabolic shifts	0:15	Metabolic shifts do not influence the glycosylation patterns of a recombinant fusion protein expressed in BHK cells.
10861392	6	34	theme	diantennary	932:942	arg1	oligosaccharides					944:959	only neutral diantennary oligosaccharides	919:959	only neutral diantennary oligosaccharides with or without core alpha1-6-linked fucose	919:1003	By using oligosaccharide mapping and MALDI/TOF-MS, only neutral diantennary oligosaccharides with or without core alpha1-6-linked fucose were detected that carried no, one or two beta1-4-linked galactose.
10861392	6	35	theme	oligosaccharide	877:891	arg1	mapping					893:899	oligosaccharide mapping	877:899	oligosaccharide mapping	877:899	By using oligosaccharide mapping and MALDI/TOF-MS, only neutral diantennary oligosaccharides with or without core alpha1-6-linked fucose were detected that carried no, one or two beta1-4-linked galactose.
10861392	8	36	from	quality	1413:1419	arg1	terms					1449:1453	terms	1449:1453	terms of O- and N-linked oligosaccharides	1449:1489	Here, it is shown that under different defined cellular metabolic states, the quality of a recombinant product in terms of O- and N-linked oligosaccharides is stable, even after a prolonged cultivation period.
10861392	2	37	theme	<	348:348	arg1	mM					354:355	< 0.5 mM	348:355	< 0.5 mM	348:355	At very low-glucose (< 0.5 mM) or glutamine (< 0.
10861392	2	37	theme	<	348:348	arg1	low-glucose					335:345	low-glucose	335:345	low-glucose	335:345	At very low-glucose (< 0.5 mM) or glutamine (< 0.
10861392	6	38	theme	neutral	924:930	arg1	oligosaccharides					944:959	only neutral diantennary oligosaccharides	919:959	only neutral diantennary oligosaccharides with or without core alpha1-6-linked fucose	919:1003	By using oligosaccharide mapping and MALDI/TOF-MS, only neutral diantennary oligosaccharides with or without core alpha1-6-linked fucose were detected that carried no, one or two beta1-4-linked galactose.
10861392	8	39	theme	cellular	1382:1389	arg1	states					1401:1406	different defined cellular metabolic states	1364:1406	different defined cellular metabolic states	1364:1406	Here, it is shown that under different defined cellular metabolic states, the quality of a recombinant product in terms of O- and N-linked oligosaccharides is stable, even after a prolonged cultivation period.
10861392	6	40	dep	galactose	1062:1070	arg1	beta1-4-linked					1047:1060	beta1-4-linked	1047:1060	beta1-4-linked	1047:1060	By using oligosaccharide mapping and MALDI/TOF-MS, only neutral diantennary oligosaccharides with or without core alpha1-6-linked fucose were detected that carried no, one or two beta1-4-linked galactose.
10861392	1	41	theme	potential	178:186	arg1	application					188:198	potential application	178:198	potential application in tumor-targeted therapy	178:224	BHK-21 cells expressing a human IgG-IL2 fusion protein, with potential application in tumor-targeted therapy, were grown under different nutrient conditions in a continuous system for a time period of 80 days.
10861392	7	42	theme	IL2	1146:1148	arg1	moiety					1150:1155	the IL2 moiety	1142:1155	the IL2 moiety of the protein	1142:1170	Although the O-linked oligosaccharide structures that are present in the IL2 moiety of the protein were studied with less detail, the data obtained from the hydrazinolysis procedure point to the presence of the classical NeuAcalpha2-3Galbeta1-3GalNAc structure.
10861392	1	43	theme	continuous	279:288	arg1	system					290:295	a continuous system	277:295	a continuous system for a time period of 80 days	277:324	BHK-21 cells expressing a human IgG-IL2 fusion protein, with potential application in tumor-targeted therapy, were grown under different nutrient conditions in a continuous system for a time period of 80 days.
10861392	8	44	theme	different	1364:1372	arg1	states					1401:1406	different defined cellular metabolic states	1364:1406	different defined cellular metabolic states	1364:1406	Here, it is shown that under different defined cellular metabolic states, the quality of a recombinant product in terms of O- and N-linked oligosaccharides is stable, even after a prolonged cultivation period.
10861392	3	45	theme	efficient	436:444	arg1	metabolism					446:455	an energetically more efficient metabolism	414:455	an energetically more efficient metabolism	414:455	2 mM) concentrations, a shift toward an energetically more efficient metabolism was observed.
10861392	5	46	theme	fusion	776:781	arg1	preparations					791:802	the IgG-IL2 fusion protein preparations	764:802	the IgG-IL2 fusion protein preparations obtained by growing cells under the different metabolic states	764:865	No significant differences in the oligosaccharide structures were detected from the IgG-IL2 fusion protein preparations obtained by growing cells under the different metabolic states.
10861392	8	47	theme	cultivation	1525:1535	arg1	period					1537:1542	a prolonged cultivation period	1513:1542	a prolonged cultivation period	1513:1542	Here, it is shown that under different defined cellular metabolic states, the quality of a recombinant product in terms of O- and N-linked oligosaccharides is stable, even after a prolonged cultivation period.
10861392	5	48	theme	protein	783:789	arg1	preparations					791:802	the IgG-IL2 fusion protein preparations	764:802	the IgG-IL2 fusion protein preparations obtained by growing cells under the different metabolic states	764:865	No significant differences in the oligosaccharide structures were detected from the IgG-IL2 fusion protein preparations obtained by growing cells under the different metabolic states.
10861392	2	49	dep	glutamine	361:369	arg1	<					372:372	< 0	372:374	< 0	372:374	At very low-glucose (< 0.5 mM) or glutamine (< 0.
10861392	7	50	theme	classical	1284:1292	arg1	structure					1324:1332	the classical NeuAcalpha2-3Galbeta1-3GalNAc structure	1280:1332	the classical NeuAcalpha2-3Galbeta1-3GalNAc structure	1280:1332	Although the O-linked oligosaccharide structures that are present in the IL2 moiety of the protein were studied with less detail, the data obtained from the hydrazinolysis procedure point to the presence of the classical NeuAcalpha2-3Galbeta1-3GalNAc structure.
10861392	4	51	theme	intracellular	600:612	arg1	content					618:624	an almost identical intracellular ATP content	580:624	an almost identical intracellular ATP content	580:624	Cell-specific productivity was maintained under metabolically shifted growth conditions and at the same time an almost identical intracellular ATP content, obtained by in vivo (31)P NMR experiments, was observed.
10861392	7	52	theme	NeuAcalpha2-3Galbeta1-3GalNAc	1294:1322	arg1	structure					1324:1332	the classical NeuAcalpha2-3Galbeta1-3GalNAc structure	1280:1332	the classical NeuAcalpha2-3Galbeta1-3GalNAc structure	1280:1332	Although the O-linked oligosaccharide structures that are present in the IL2 moiety of the protein were studied with less detail, the data obtained from the hydrazinolysis procedure point to the presence of the classical NeuAcalpha2-3Galbeta1-3GalNAc structure.
10861392	4	53	theme	shifted	533:539	arg1	conditions					548:557	metabolically shifted growth conditions	519:557	metabolically shifted growth conditions	519:557	Cell-specific productivity was maintained under metabolically shifted growth conditions and at the same time an almost identical intracellular ATP content, obtained by in vivo (31)P NMR experiments, was observed.
10861392	8	54	theme	product	1438:1444	arg1	stable					1494:1499	stable	1494:1499	stable	1494:1499	Here, it is shown that under different defined cellular metabolic states, the quality of a recombinant product in terms of O- and N-linked oligosaccharides is stable, even after a prolonged cultivation period.
10861392	8	54	theme	product	1438:1444	arg1	quality					1413:1419	the quality	1409:1419	the quality of a recombinant product in terms of O- and N-linked oligosaccharides	1409:1489	Here, it is shown that under different defined cellular metabolic states, the quality of a recombinant product in terms of O- and N-linked oligosaccharides is stable, even after a prolonged cultivation period.
10861392	6	55	dep	beta1-4-linked	1047:1060	arg1	one					1036:1038	one	1036:1038	one	1036:1038	By using oligosaccharide mapping and MALDI/TOF-MS, only neutral diantennary oligosaccharides with or without core alpha1-6-linked fucose were detected that carried no, one or two beta1-4-linked galactose.
10861392	6	55	dep	beta1-4-linked	1047:1060	arg1	two					1043:1045	two	1043:1045	two	1043:1045	By using oligosaccharide mapping and MALDI/TOF-MS, only neutral diantennary oligosaccharides with or without core alpha1-6-linked fucose were detected that carried no, one or two beta1-4-linked galactose.
10861392	9	56	theme	metabolic	1611:1619	arg1	states					1621:1626	the different metabolic states	1597:1626	the different metabolic states	1597:1626	Moreover, unaffected intracellular ATP levels under the different metabolic states were observed.
10861392	1	57	theme	tumor-targeted	203:216	arg1	therapy					218:224	tumor-targeted therapy	203:224	tumor-targeted therapy	203:224	BHK-21 cells expressing a human IgG-IL2 fusion protein, with potential application in tumor-targeted therapy, were grown under different nutrient conditions in a continuous system for a time period of 80 days.
10861392	5	58	theme	oligosaccharide	718:732	arg1	structures					734:743	the oligosaccharide structures	714:743	the oligosaccharide structures	714:743	No significant differences in the oligosaccharide structures were detected from the IgG-IL2 fusion protein preparations obtained by growing cells under the different metabolic states.
10861392	7	59	located	present	1131:1137	arg2	structures					1111:1120	the O-linked oligosaccharide structures	1082:1120	the O-linked oligosaccharide structures that are present in the IL2 moiety of the protein	1082:1170	Although the O-linked oligosaccharide structures that are present in the IL2 moiety of the protein were studied with less detail, the data obtained from the hydrazinolysis procedure point to the presence of the classical NeuAcalpha2-3Galbeta1-3GalNAc structure.
10861392	7	59	located	present	1131:1137	arg1	moiety					1150:1155	the IL2 moiety	1142:1155	the IL2 moiety of the protein	1142:1170	Although the O-linked oligosaccharide structures that are present in the IL2 moiety of the protein were studied with less detail, the data obtained from the hydrazinolysis procedure point to the presence of the classical NeuAcalpha2-3Galbeta1-3GalNAc structure.
10861392	7	59	located	present	1131:1137	arg2	present					1131:1137	present	1131:1137	present	1131:1137	Although the O-linked oligosaccharide structures that are present in the IL2 moiety of the protein were studied with less detail, the data obtained from the hydrazinolysis procedure point to the presence of the classical NeuAcalpha2-3Galbeta1-3GalNAc structure.
10861392	8	60	theme	recombinant	1426:1436	arg1	product					1438:1444	a recombinant product	1424:1444	a recombinant product	1424:1444	Here, it is shown that under different defined cellular metabolic states, the quality of a recombinant product in terms of O- and N-linked oligosaccharides is stable, even after a prolonged cultivation period.
10861392	8	61	theme	metabolic	1391:1399	arg1	states					1401:1406	different defined cellular metabolic states	1364:1406	different defined cellular metabolic states	1364:1406	Here, it is shown that under different defined cellular metabolic states, the quality of a recombinant product in terms of O- and N-linked oligosaccharides is stable, even after a prolonged cultivation period.
10861392	6	62	contain	carried	1024:1030	arg1	that					1019:1022	that	1019:1022	that	1019:1022	By using oligosaccharide mapping and MALDI/TOF-MS, only neutral diantennary oligosaccharides with or without core alpha1-6-linked fucose were detected that carried no, one or two beta1-4-linked galactose.
10861392	6	62	contain	carried	1024:1030	arg2	galactose					1062:1070	no, one or two beta1-4-linked galactose	1032:1070	no, one or two beta1-4-linked galactose	1032:1070	By using oligosaccharide mapping and MALDI/TOF-MS, only neutral diantennary oligosaccharides with or without core alpha1-6-linked fucose were detected that carried no, one or two beta1-4-linked galactose.
10861392	0	63	theme	glycosylation	38:50	arg1	patterns					52:59	the glycosylation patterns	34:59	the glycosylation patterns of a recombinant fusion protein expressed in BHK cells	34:114	Metabolic shifts do not influence the glycosylation patterns of a recombinant fusion protein expressed in BHK cells.
10861392	1	64	theme	time	303:306	arg1	period					308:313	a time period	301:313	a time period of 80 days	301:324	BHK-21 cells expressing a human IgG-IL2 fusion protein, with potential application in tumor-targeted therapy, were grown under different nutrient conditions in a continuous system for a time period of 80 days.
10861392	7	65	from	present	1131:1137	arg1	moiety					1150:1155	the IL2 moiety	1142:1155	the IL2 moiety of the protein	1142:1170	Although the O-linked oligosaccharide structures that are present in the IL2 moiety of the protein were studied with less detail, the data obtained from the hydrazinolysis procedure point to the presence of the classical NeuAcalpha2-3Galbeta1-3GalNAc structure.
10861392	7	66	theme	structure	1324:1332	arg1	presence					1268:1275	the presence	1264:1275	the presence of the classical NeuAcalpha2-3Galbeta1-3GalNAc structure	1264:1332	Although the O-linked oligosaccharide structures that are present in the IL2 moiety of the protein were studied with less detail, the data obtained from the hydrazinolysis procedure point to the presence of the classical NeuAcalpha2-3Galbeta1-3GalNAc structure.
10861392	4	67	located	observed	674:681	arg2	content					618:624	an almost identical intracellular ATP content	580:624	an almost identical intracellular ATP content	580:624	Cell-specific productivity was maintained under metabolically shifted growth conditions and at the same time an almost identical intracellular ATP content, obtained by in vivo (31)P NMR experiments, was observed.
10861392	4	67	located	observed	674:681	arg1	time					575:578	the same time	566:578	the same time	566:578	Cell-specific productivity was maintained under metabolically shifted growth conditions and at the same time an almost identical intracellular ATP content, obtained by in vivo (31)P NMR experiments, was observed.
10861392	5	68	from	differences	699:709	arg1	structures					734:743	the oligosaccharide structures	714:743	the oligosaccharide structures	714:743	No significant differences in the oligosaccharide structures were detected from the IgG-IL2 fusion protein preparations obtained by growing cells under the different metabolic states.
10861392	1	69	from	application	188:198	arg1	therapy					218:224	tumor-targeted therapy	203:224	tumor-targeted therapy	203:224	BHK-21 cells expressing a human IgG-IL2 fusion protein, with potential application in tumor-targeted therapy, were grown under different nutrient conditions in a continuous system for a time period of 80 days.
10861392	1	70	theme	BHK-21	117:122	arg1	cells					124:128	BHK-21 cells	117:128	BHK-21 cells expressing a human IgG-IL2 fusion protein, with potential application in tumor-targeted therapy,	117:225	BHK-21 cells expressing a human IgG-IL2 fusion protein, with potential application in tumor-targeted therapy, were grown under different nutrient conditions in a continuous system for a time period of 80 days.
10861392	1	71	with	protein	164:170	arg1	application					188:198	potential application	178:198	potential application in tumor-targeted therapy	178:224	BHK-21 cells expressing a human IgG-IL2 fusion protein, with potential application in tumor-targeted therapy, were grown under different nutrient conditions in a continuous system for a time period of 80 days.
10861392	8	72	theme	O-	1458:1459	arg1	terms					1449:1453	terms	1449:1453	terms of O- and N-linked oligosaccharides	1449:1489	Here, it is shown that under different defined cellular metabolic states, the quality of a recombinant product in terms of O- and N-linked oligosaccharides is stable, even after a prolonged cultivation period.
10861392	9	73	theme	different	1601:1609	arg1	states					1621:1626	the different metabolic states	1597:1626	the different metabolic states	1597:1626	Moreover, unaffected intracellular ATP levels under the different metabolic states were observed.
10861392	4	74	theme	P	651:651	arg1	experiments					657:667	in vivo (31)P NMR experiments	639:667	in vivo (31)P NMR experiments	639:667	Cell-specific productivity was maintained under metabolically shifted growth conditions and at the same time an almost identical intracellular ATP content, obtained by in vivo (31)P NMR experiments, was observed.
10861392	4	75	theme	NMR	653:655	arg1	experiments					657:667	in vivo (31)P NMR experiments	639:667	in vivo (31)P NMR experiments	639:667	Cell-specific productivity was maintained under metabolically shifted growth conditions and at the same time an almost identical intracellular ATP content, obtained by in vivo (31)P NMR experiments, was observed.
10861392	4	76	theme	identical	590:598	arg1	content					618:624	an almost identical intracellular ATP content	580:624	an almost identical intracellular ATP content	580:624	Cell-specific productivity was maintained under metabolically shifted growth conditions and at the same time an almost identical intracellular ATP content, obtained by in vivo (31)P NMR experiments, was observed.
10861392	0	77	gly	glycosylation	38:50	arg1	protein					85:91	a recombinant fusion protein	64:91	a recombinant fusion protein expressed in BHK cells	64:114	Metabolic shifts do not influence the glycosylation patterns of a recombinant fusion protein expressed in BHK cells.
10861392	5	78	theme	IgG-IL2	768:774	arg1	preparations					791:802	the IgG-IL2 fusion protein preparations	764:802	the IgG-IL2 fusion protein preparations obtained by growing cells under the different metabolic states	764:865	No significant differences in the oligosaccharide structures were detected from the IgG-IL2 fusion protein preparations obtained by growing cells under the different metabolic states.
10861392	4	79	theme	in	639:640	arg1	experiments					657:667	in vivo (31)P NMR experiments	639:667	in vivo (31)P NMR experiments	639:667	Cell-specific productivity was maintained under metabolically shifted growth conditions and at the same time an almost identical intracellular ATP content, obtained by in vivo (31)P NMR experiments, was observed.
10861392	4	80	theme	ATP	614:616	arg1	content					618:624	an almost identical intracellular ATP content	580:624	an almost identical intracellular ATP content	580:624	Cell-specific productivity was maintained under metabolically shifted growth conditions and at the same time an almost identical intracellular ATP content, obtained by in vivo (31)P NMR experiments, was observed.
10861392	6	81	theme	alpha1-6-linked	982:996	arg1	fucose					998:1003	core alpha1-6-linked fucose	977:1003	core alpha1-6-linked fucose	977:1003	By using oligosaccharide mapping and MALDI/TOF-MS, only neutral diantennary oligosaccharides with or without core alpha1-6-linked fucose were detected that carried no, one or two beta1-4-linked galactose.
10861392	8	82	theme	N-linked	1465:1472	arg1	oligosaccharides					1474:1489	N-linked oligosaccharides	1465:1489	N-linked oligosaccharides	1465:1489	Here, it is shown that under different defined cellular metabolic states, the quality of a recombinant product in terms of O- and N-linked oligosaccharides is stable, even after a prolonged cultivation period.
10861392	6	83	theme	core	977:980	arg1	fucose					998:1003	core alpha1-6-linked fucose	977:1003	core alpha1-6-linked fucose	977:1003	By using oligosaccharide mapping and MALDI/TOF-MS, only neutral diantennary oligosaccharides with or without core alpha1-6-linked fucose were detected that carried no, one or two beta1-4-linked galactose.
10861392	4	84	theme	same	570:573	arg1	time					575:578	the same time	566:578	the same time	566:578	Cell-specific productivity was maintained under metabolically shifted growth conditions and at the same time an almost identical intracellular ATP content, obtained by in vivo (31)P NMR experiments, was observed.
10026155	5	0	theme	HNK-1	720:724	arg1	antibody					737:744	an HNK-1 monoclonal antibody	717:744	an HNK-1 monoclonal antibody	717:744	These sugar chains could bind to an HNK-1 monoclonal antibody.
10026155	3	1	contain	containing	374:383	arg2	end					419:421	a reducing end	408:421	a reducing end	408:421	Two fractions containing pyridylaminated Xyl as a reducing end were collected.
10026155	3	1	contain	containing	374:383	arg1	fractions					364:372	Two fractions	360:372	Two fractions containing pyridylaminated Xyl as a reducing end	360:421	Two fractions containing pyridylaminated Xyl as a reducing end were collected.
10026155	3	1	contain	containing	374:383	arg2	Xyl					401:403	pyridylaminated Xyl	385:403	pyridylaminated Xyl	385:403	Two fractions containing pyridylaminated Xyl as a reducing end were collected.
10026155	5	2	theme	monoclonal	726:735	arg1	antibody					737:744	an HNK-1 monoclonal antibody	717:744	an HNK-1 monoclonal antibody	717:744	These sugar chains could bind to an HNK-1 monoclonal antibody.
10026155	1	3	theme	reducing	181:188	arg1	end					190:192	a reducing end	179:192	a reducing end linked to human urinary soluble thrombomodulin	179:239	O-linked sugar chains with xylose as a reducing end linked to human urinary soluble thrombomodulin were studied.
10026155	4	4	theme	two-dimensional	500:514	arg1	mapping					522:528	two-dimensional sugar mapping	500:528	two-dimensional sugar mapping combined with exoglycosidase digestions	500:568	Their structures were determined by partial acid hydrolysis, two-dimensional sugar mapping combined with exoglycosidase digestions, methylation analysis, mass spectrometry, and NMR as SO4-3GlcAbeta1-3Galbeta1-3(+/-Siaalpha2-6)Galbeta1+ ++-4Xyl.
10026155	3	5	theme	reducing	410:417	arg1	end					419:421	a reducing end	408:421	a reducing end	408:421	Two fractions containing pyridylaminated Xyl as a reducing end were collected.
10026155	3	5	theme	reducing	410:417	arg1	Xyl					401:403	pyridylaminated Xyl	385:403	pyridylaminated Xyl	385:403	Two fractions containing pyridylaminated Xyl as a reducing end were collected.
10026155	5	6	theme	sugar	690:694	arg1	chains					696:701	These sugar chains	684:701	These sugar chains	684:701	These sugar chains could bind to an HNK-1 monoclonal antibody.
10026155	4	7	theme	sugar	516:520	arg1	mapping					522:528	two-dimensional sugar mapping	500:528	two-dimensional sugar mapping combined with exoglycosidase digestions	500:568	Their structures were determined by partial acid hydrolysis, two-dimensional sugar mapping combined with exoglycosidase digestions, methylation analysis, mass spectrometry, and NMR as SO4-3GlcAbeta1-3Galbeta1-3(+/-Siaalpha2-6)Galbeta1+ ++-4Xyl.
10026155	4	8	theme	Galbeta1+	665:673	arg1	structures					445:454	Their structures	439:454	Their structures	439:454	Their structures were determined by partial acid hydrolysis, two-dimensional sugar mapping combined with exoglycosidase digestions, methylation analysis, mass spectrometry, and NMR as SO4-3GlcAbeta1-3Galbeta1-3(+/-Siaalpha2-6)Galbeta1+ ++-4Xyl.
10026155	4	8	theme	Galbeta1+	665:673	arg1	++-4Xyl					675:681	SO4-3GlcAbeta1-3Galbeta1-3(+/-Siaalpha2-6)Galbeta1+ ++-4Xyl	623:681	SO4-3GlcAbeta1-3Galbeta1-3(+/-Siaalpha2-6)Galbeta1+ ++-4Xyl	623:681	Their structures were determined by partial acid hydrolysis, two-dimensional sugar mapping combined with exoglycosidase digestions, methylation analysis, mass spectrometry, and NMR as SO4-3GlcAbeta1-3Galbeta1-3(+/-Siaalpha2-6)Galbeta1+ ++-4Xyl.
10026155	1	9	with	chains	157:162	arg1	xylose					169:174	xylose	169:174	xylose	169:174	O-linked sugar chains with xylose as a reducing end linked to human urinary soluble thrombomodulin were studied.
10026155	6	10	theme	first	774:778	arg1	This					747:750	This	747:750	This	747:750	This is believed to be the first example of a proteoglycan linkage tetrasaccharide with glucuronic acid 3-sulfate and sialic acid.
10026155	6	10	theme	first	774:778	arg1	example					780:786	the first example	770:786	the first example of a proteoglycan linkage tetrasaccharide with glucuronic acid 3-sulfate and sialic acid	770:875	This is believed to be the first example of a proteoglycan linkage tetrasaccharide with glucuronic acid 3-sulfate and sialic acid.
10026155	0	11	theme	Galbeta1-4Xyl	127:139	arg1	tetrasaccharides					27:42	Novel proteoglycan linkage tetrasaccharides	0:42	Novel proteoglycan linkage tetrasaccharides	0:42	Novel proteoglycan linkage tetrasaccharides of human urinary soluble thrombomodulin, SO4-3GlcAbeta1-3Galbeta1-3(+/-Siaalpha2-6)Galbeta1-4Xyl.
10026155	0	12	theme	proteoglycan	6:17	arg1	tetrasaccharides					27:42	Novel proteoglycan linkage tetrasaccharides	0:42	Novel proteoglycan linkage tetrasaccharides	0:42	Novel proteoglycan linkage tetrasaccharides of human urinary soluble thrombomodulin, SO4-3GlcAbeta1-3Galbeta1-3(+/-Siaalpha2-6)Galbeta1-4Xyl.
10026155	4	13	theme	exoglycosidase	544:557	arg1	digestions					559:568	exoglycosidase digestions	544:568	exoglycosidase digestions	544:568	Their structures were determined by partial acid hydrolysis, two-dimensional sugar mapping combined with exoglycosidase digestions, methylation analysis, mass spectrometry, and NMR as SO4-3GlcAbeta1-3Galbeta1-3(+/-Siaalpha2-6)Galbeta1+ ++-4Xyl.
10026155	6	14	theme	sialic	865:870	arg1	acid					872:875	sialic acid	865:875	sialic acid	865:875	This is believed to be the first example of a proteoglycan linkage tetrasaccharide with glucuronic acid 3-sulfate and sialic acid.
10026155	0	15	theme	Novel	0:4	arg1	tetrasaccharides					27:42	Novel proteoglycan linkage tetrasaccharides	0:42	Novel proteoglycan linkage tetrasaccharides	0:42	Novel proteoglycan linkage tetrasaccharides of human urinary soluble thrombomodulin, SO4-3GlcAbeta1-3Galbeta1-3(+/-Siaalpha2-6)Galbeta1-4Xyl.
10026155	1	16	theme	human	204:208	arg1	thrombomodulin					226:239	human urinary soluble thrombomodulin	204:239	human urinary soluble thrombomodulin	204:239	O-linked sugar chains with xylose as a reducing end linked to human urinary soluble thrombomodulin were studied.
10026155	6	17	theme	3-sulfate	851:859	arg1	acid					846:849	glucuronic acid 3-sulfate	835:859	glucuronic acid 3-sulfate	835:859	This is believed to be the first example of a proteoglycan linkage tetrasaccharide with glucuronic acid 3-sulfate and sialic acid.
10026155	1	18	theme	urinary	210:216	arg1	thrombomodulin					226:239	human urinary soluble thrombomodulin	204:239	human urinary soluble thrombomodulin	204:239	O-linked sugar chains with xylose as a reducing end linked to human urinary soluble thrombomodulin were studied.
10026155	0	19	theme	linkage	19:25	arg1	tetrasaccharides					27:42	Novel proteoglycan linkage tetrasaccharides	0:42	Novel proteoglycan linkage tetrasaccharides	0:42	Novel proteoglycan linkage tetrasaccharides of human urinary soluble thrombomodulin, SO4-3GlcAbeta1-3Galbeta1-3(+/-Siaalpha2-6)Galbeta1-4Xyl.
10026155	1	20	attach	linked	194:199	arg2	end					190:192	a reducing end	179:192	a reducing end linked to human urinary soluble thrombomodulin	179:239	O-linked sugar chains with xylose as a reducing end linked to human urinary soluble thrombomodulin were studied.
10026155	1	20	attach	linked	194:199	arg1	thrombomodulin					226:239	human urinary soluble thrombomodulin	204:239	human urinary soluble thrombomodulin	204:239	O-linked sugar chains with xylose as a reducing end linked to human urinary soluble thrombomodulin were studied.
10026155	1	21	theme	soluble	218:224	arg1	thrombomodulin					226:239	human urinary soluble thrombomodulin	204:239	human urinary soluble thrombomodulin	204:239	O-linked sugar chains with xylose as a reducing end linked to human urinary soluble thrombomodulin were studied.
10026155	0	22	theme	human	47:51	arg1	thrombomodulin					69:82	human urinary soluble thrombomodulin	47:82	human urinary soluble thrombomodulin	47:82	Novel proteoglycan linkage tetrasaccharides of human urinary soluble thrombomodulin, SO4-3GlcAbeta1-3Galbeta1-3(+/-Siaalpha2-6)Galbeta1-4Xyl.
10026155	6	23	with	example	780:786	arg1	acid					872:875	sialic acid	865:875	sialic acid	865:875	This is believed to be the first example of a proteoglycan linkage tetrasaccharide with glucuronic acid 3-sulfate and sialic acid.
10026155	6	23	with	example	780:786	arg1	acid					846:849	glucuronic acid 3-sulfate	835:859	glucuronic acid 3-sulfate	835:859	This is believed to be the first example of a proteoglycan linkage tetrasaccharide with glucuronic acid 3-sulfate and sialic acid.
10026155	2	24	theme	Sugar	255:259	arg1	chains					261:266	Sugar chains	255:266	Sugar chains	255:266	Sugar chains were liberated by hydrazinolysis followed by N-acetylation and tagged with 2-aminopyridine.
10026155	0	25	theme	soluble	61:67	arg1	thrombomodulin					69:82	human urinary soluble thrombomodulin	47:82	human urinary soluble thrombomodulin	47:82	Novel proteoglycan linkage tetrasaccharides of human urinary soluble thrombomodulin, SO4-3GlcAbeta1-3Galbeta1-3(+/-Siaalpha2-6)Galbeta1-4Xyl.
10026155	4	26	theme	mass	593:596	arg1	spectrometry					598:609	mass spectrometry	593:609	mass spectrometry	593:609	Their structures were determined by partial acid hydrolysis, two-dimensional sugar mapping combined with exoglycosidase digestions, methylation analysis, mass spectrometry, and NMR as SO4-3GlcAbeta1-3Galbeta1-3(+/-Siaalpha2-6)Galbeta1+ ++-4Xyl.
10026155	0	27	theme	thrombomodulin	69:82	arg1	tetrasaccharides					27:42	Novel proteoglycan linkage tetrasaccharides	0:42	Novel proteoglycan linkage tetrasaccharides	0:42	Novel proteoglycan linkage tetrasaccharides of human urinary soluble thrombomodulin, SO4-3GlcAbeta1-3Galbeta1-3(+/-Siaalpha2-6)Galbeta1-4Xyl.
10026155	6	28	theme	glucuronic	835:844	arg1	acid					846:849	glucuronic acid 3-sulfate	835:859	glucuronic acid 3-sulfate	835:859	This is believed to be the first example of a proteoglycan linkage tetrasaccharide with glucuronic acid 3-sulfate and sialic acid.
10026155	1	29	theme	O-linked	142:149	arg1	chains					157:162	O-linked sugar chains	142:162	O-linked sugar chains with xylose as a reducing end linked to human urinary soluble thrombomodulin	142:239	O-linked sugar chains with xylose as a reducing end linked to human urinary soluble thrombomodulin were studied.
10026155	0	30	theme	urinary	53:59	arg1	thrombomodulin					69:82	human urinary soluble thrombomodulin	47:82	human urinary soluble thrombomodulin	47:82	Novel proteoglycan linkage tetrasaccharides of human urinary soluble thrombomodulin, SO4-3GlcAbeta1-3Galbeta1-3(+/-Siaalpha2-6)Galbeta1-4Xyl.
10026155	4	31	theme	partial	475:481	arg1	hydrolysis					488:497	partial acid hydrolysis	475:497	partial acid hydrolysis	475:497	Their structures were determined by partial acid hydrolysis, two-dimensional sugar mapping combined with exoglycosidase digestions, methylation analysis, mass spectrometry, and NMR as SO4-3GlcAbeta1-3Galbeta1-3(+/-Siaalpha2-6)Galbeta1+ ++-4Xyl.
10026155	1	32	theme	sugar	151:155	arg1	chains					157:162	O-linked sugar chains	142:162	O-linked sugar chains with xylose as a reducing end linked to human urinary soluble thrombomodulin	142:239	O-linked sugar chains with xylose as a reducing end linked to human urinary soluble thrombomodulin were studied.
10026155	1	33	link	O-linked	142:149	arg1	chains					157:162	O-linked sugar chains	142:162	O-linked sugar chains with xylose as a reducing end linked to human urinary soluble thrombomodulin	142:239	O-linked sugar chains with xylose as a reducing end linked to human urinary soluble thrombomodulin were studied.
10026155	6	34	theme	tetrasaccharide	814:828	arg1	This					747:750	This	747:750	This	747:750	This is believed to be the first example of a proteoglycan linkage tetrasaccharide with glucuronic acid 3-sulfate and sialic acid.
10026155	6	34	theme	tetrasaccharide	814:828	arg1	example					780:786	the first example	770:786	the first example of a proteoglycan linkage tetrasaccharide with glucuronic acid 3-sulfate and sialic acid	770:875	This is believed to be the first example of a proteoglycan linkage tetrasaccharide with glucuronic acid 3-sulfate and sialic acid.
10026155	6	35	theme	linkage	806:812	arg1	tetrasaccharide					814:828	a proteoglycan linkage tetrasaccharide	791:828	a proteoglycan linkage tetrasaccharide	791:828	This is believed to be the first example of a proteoglycan linkage tetrasaccharide with glucuronic acid 3-sulfate and sialic acid.
10026155	4	36	theme	acid	483:486	arg1	hydrolysis					488:497	partial acid hydrolysis	475:497	partial acid hydrolysis	475:497	Their structures were determined by partial acid hydrolysis, two-dimensional sugar mapping combined with exoglycosidase digestions, methylation analysis, mass spectrometry, and NMR as SO4-3GlcAbeta1-3Galbeta1-3(+/-Siaalpha2-6)Galbeta1+ ++-4Xyl.
10026155	6	37	theme	proteoglycan	793:804	arg1	tetrasaccharide					814:828	a proteoglycan linkage tetrasaccharide	791:828	a proteoglycan linkage tetrasaccharide	791:828	This is believed to be the first example of a proteoglycan linkage tetrasaccharide with glucuronic acid 3-sulfate and sialic acid.
10026155	3	38	theme	pyridylaminated	385:399	arg1	end					419:421	a reducing end	408:421	a reducing end	408:421	Two fractions containing pyridylaminated Xyl as a reducing end were collected.
10026155	3	38	theme	pyridylaminated	385:399	arg1	Xyl					401:403	pyridylaminated Xyl	385:403	pyridylaminated Xyl	385:403	Two fractions containing pyridylaminated Xyl as a reducing end were collected.
10026155	4	39	theme	methylation	571:581	arg1	analysis					583:590	methylation analysis	571:590	methylation analysis	571:590	Their structures were determined by partial acid hydrolysis, two-dimensional sugar mapping combined with exoglycosidase digestions, methylation analysis, mass spectrometry, and NMR as SO4-3GlcAbeta1-3Galbeta1-3(+/-Siaalpha2-6)Galbeta1+ ++-4Xyl.
3197039	0	0	theme	assigned	78:85	arg1	spectra					97:103	fully assigned 1H-n.m.r. spectra	72:103	fully assigned 1H-n.m.r. spectra for solutions in non-aqueous solvents	72:141	The determination of the structure of blood group oligosaccharides from fully assigned 1H-n.m.r. spectra for solutions in non-aqueous solvents.
3197039	4	1	theme	n.O.e.	978:983	arg1	values					985:990	either negative or positive n.O.e. values	950:990	either negative or positive n.O.e. values	950:990	Although the rotational correlation times (tau c) of these oligosaccharides are similar to the reciprocal of the spectrometer frequency, either negative or positive n.O.e. values were measurable for both oligosaccharides in all three solvents in one-dimensional difference spectroscopy by taking advantage of the dependence of tau c on the solvent viscosity and, thus, on sample temperature.
3197039	1	2	theme	assigned	154:161	arg1	spectra					173:179	The fully assigned 1H-n.m.r. spectra	144:179	The fully assigned 1H-n.m.r. spectra of a blood group A tetrasaccharide and of a blood group H hexasaccharide in dimethyl sulfoxide and in pyridine by use of two-dimensional COSY and homonuclear Hartmann-Hann coherence transfer methods	144:378	The fully assigned 1H-n.m.r. spectra of a blood group A tetrasaccharide and of a blood group H hexasaccharide in dimethyl sulfoxide and in pyridine by use of two-dimensional COSY and homonuclear Hartmann-Hann coherence transfer methods are reported.
3197039	1	3	theme	H	237:237	arg1	hexasaccharide					239:252	a blood group H hexasaccharide	223:252	a blood group H hexasaccharide in dimethyl sulfoxide and in pyridine by use of two-dimensional COSY and homonuclear Hartmann-Hann coherence transfer methods	223:378	The fully assigned 1H-n.m.r. spectra of a blood group A tetrasaccharide and of a blood group H hexasaccharide in dimethyl sulfoxide and in pyridine by use of two-dimensional COSY and homonuclear Hartmann-Hann coherence transfer methods are reported.
3197039	4	4	theme	positive	969:976	arg1	values					985:990	either negative or positive n.O.e. values	950:990	either negative or positive n.O.e. values	950:990	Although the rotational correlation times (tau c) of these oligosaccharides are similar to the reciprocal of the spectrometer frequency, either negative or positive n.O.e. values were measurable for both oligosaccharides in all three solvents in one-dimensional difference spectroscopy by taking advantage of the dependence of tau c on the solvent viscosity and, thus, on sample temperature.
3197039	1	5	theme	homonuclear	327:337	arg1	methods					372:378	two-dimensional COSY and homonuclear Hartmann-Hann coherence transfer methods	302:378	methods	372:378	The fully assigned 1H-n.m.r. spectra of a blood group A tetrasaccharide and of a blood group H hexasaccharide in dimethyl sulfoxide and in pyridine by use of two-dimensional COSY and homonuclear Hartmann-Hann coherence transfer methods are reported.
3197039	4	6	theme	c	1144:1144	arg1	dependence					1126:1135	the dependence	1122:1135	the dependence of tau c on the solvent viscosity and, thus, on sample temperature	1122:1202	Although the rotational correlation times (tau c) of these oligosaccharides are similar to the reciprocal of the spectrometer frequency, either negative or positive n.O.e. values were measurable for both oligosaccharides in all three solvents in one-dimensional difference spectroscopy by taking advantage of the dependence of tau c on the solvent viscosity and, thus, on sample temperature.
3197039	4	7	from	solvents	1047:1054	arg1	measurable					997:1006	measurable	997:1006	measurable	997:1006	Although the rotational correlation times (tau c) of these oligosaccharides are similar to the reciprocal of the spectrometer frequency, either negative or positive n.O.e. values were measurable for both oligosaccharides in all three solvents in one-dimensional difference spectroscopy by taking advantage of the dependence of tau c on the solvent viscosity and, thus, on sample temperature.
3197039	4	7	from	solvents	1047:1054	arg1	spectroscopy					1086:1097	one-dimensional difference spectroscopy	1059:1097	one-dimensional difference spectroscopy	1059:1097	Although the rotational correlation times (tau c) of these oligosaccharides are similar to the reciprocal of the spectrometer frequency, either negative or positive n.O.e. values were measurable for both oligosaccharides in all three solvents in one-dimensional difference spectroscopy by taking advantage of the dependence of tau c on the solvent viscosity and, thus, on sample temperature.
3197039	1	8	theme	1H-n.m.r.	163:171	arg1	spectra					173:179	The fully assigned 1H-n.m.r. spectra	144:179	The fully assigned 1H-n.m.r. spectra of a blood group A tetrasaccharide and of a blood group H hexasaccharide in dimethyl sulfoxide and in pyridine by use of two-dimensional COSY and homonuclear Hartmann-Hann coherence transfer methods	144:378	The fully assigned 1H-n.m.r. spectra of a blood group A tetrasaccharide and of a blood group H hexasaccharide in dimethyl sulfoxide and in pyridine by use of two-dimensional COSY and homonuclear Hartmann-Hann coherence transfer methods are reported.
3197039	4	9	theme	one-dimensional	1059:1073	arg1	spectroscopy					1086:1097	one-dimensional difference spectroscopy	1059:1097	one-dimensional difference spectroscopy	1059:1097	Although the rotational correlation times (tau c) of these oligosaccharides are similar to the reciprocal of the spectrometer frequency, either negative or positive n.O.e. values were measurable for both oligosaccharides in all three solvents in one-dimensional difference spectroscopy by taking advantage of the dependence of tau c on the solvent viscosity and, thus, on sample temperature.
3197039	1	10	theme	hexasaccharide	239:252	arg1	spectra					173:179	The fully assigned 1H-n.m.r. spectra	144:179	The fully assigned 1H-n.m.r. spectra of a blood group A tetrasaccharide and of a blood group H hexasaccharide in dimethyl sulfoxide and in pyridine by use of two-dimensional COSY and homonuclear Hartmann-Hann coherence transfer methods	144:378	The fully assigned 1H-n.m.r. spectra of a blood group A tetrasaccharide and of a blood group H hexasaccharide in dimethyl sulfoxide and in pyridine by use of two-dimensional COSY and homonuclear Hartmann-Hann coherence transfer methods are reported.
3197039	4	11	theme	frequency	939:947	arg1	reciprocal					908:917	reciprocal	908:917	reciprocal	908:917	Although the rotational correlation times (tau c) of these oligosaccharides are similar to the reciprocal of the spectrometer frequency, either negative or positive n.O.e. values were measurable for both oligosaccharides in all three solvents in one-dimensional difference spectroscopy by taking advantage of the dependence of tau c on the solvent viscosity and, thus, on sample temperature.
3197039	1	12	theme	Hartmann-Hann	339:351	arg1	methods					372:378	two-dimensional COSY and homonuclear Hartmann-Hann coherence transfer methods	302:378	methods	372:378	The fully assigned 1H-n.m.r. spectra of a blood group A tetrasaccharide and of a blood group H hexasaccharide in dimethyl sulfoxide and in pyridine by use of two-dimensional COSY and homonuclear Hartmann-Hann coherence transfer methods are reported.
3197039	0	13	theme	1H-n.m.r.	87:95	arg1	spectra					97:103	fully assigned 1H-n.m.r. spectra	72:103	fully assigned 1H-n.m.r. spectra for solutions in non-aqueous solvents	72:141	The determination of the structure of blood group oligosaccharides from fully assigned 1H-n.m.r. spectra for solutions in non-aqueous solvents.
3197039	1	14	theme	coherence	353:361	arg1	methods					372:378	two-dimensional COSY and homonuclear Hartmann-Hann coherence transfer methods	302:378	methods	372:378	The fully assigned 1H-n.m.r. spectra of a blood group A tetrasaccharide and of a blood group H hexasaccharide in dimethyl sulfoxide and in pyridine by use of two-dimensional COSY and homonuclear Hartmann-Hann coherence transfer methods are reported.
3197039	3	15	theme	relative	502:509	arg1	different					566:574	different	566:574	different	566:574	Since the relative proton chemical shifts in the three solvents are quite different, resonances which overlap or are strongly coupled for one solvent may be well resolved for another, thus providing an extension of the method of complete proton assignments for determination of the structure of complex oligosaccharides.
3197039	3	15	theme	relative	502:509	arg1	shifts					527:532	the relative proton chemical shifts	498:532	the relative proton chemical shifts in the three solvents	498:554	Since the relative proton chemical shifts in the three solvents are quite different, resonances which overlap or are strongly coupled for one solvent may be well resolved for another, thus providing an extension of the method of complete proton assignments for determination of the structure of complex oligosaccharides.
3197039	4	16	theme	tau	1140:1142	arg1	c					1144:1144	tau c	1140:1144	tau c	1140:1144	Although the rotational correlation times (tau c) of these oligosaccharides are similar to the reciprocal of the spectrometer frequency, either negative or positive n.O.e. values were measurable for both oligosaccharides in all three solvents in one-dimensional difference spectroscopy by taking advantage of the dependence of tau c on the solvent viscosity and, thus, on sample temperature.
3197039	1	17	theme	dimethyl	257:264	arg1	sulfoxide					266:274	dimethyl sulfoxide	257:274	dimethyl sulfoxide	257:274	The fully assigned 1H-n.m.r. spectra of a blood group A tetrasaccharide and of a blood group H hexasaccharide in dimethyl sulfoxide and in pyridine by use of two-dimensional COSY and homonuclear Hartmann-Hann coherence transfer methods are reported.
3197039	1	18	theme	transfer	363:370	arg1	methods					372:378	two-dimensional COSY and homonuclear Hartmann-Hann coherence transfer methods	302:378	methods	372:378	The fully assigned 1H-n.m.r. spectra of a blood group A tetrasaccharide and of a blood group H hexasaccharide in dimethyl sulfoxide and in pyridine by use of two-dimensional COSY and homonuclear Hartmann-Hann coherence transfer methods are reported.
3197039	2	19	theme	both	419:422	arg1	spectra					408:414	The 1H-n.m.r. spectra	394:414	The 1H-n.m.r. spectra of both of these compounds in deuterium oxide	394:460	The 1H-n.m.r. spectra of both of these compounds in deuterium oxide had been previously assigned.
3197039	2	20	theme	1H-n.m.r.	398:406	arg1	spectra					408:414	The 1H-n.m.r. spectra	394:414	The 1H-n.m.r. spectra of both of these compounds in deuterium oxide	394:460	The 1H-n.m.r. spectra of both of these compounds in deuterium oxide had been previously assigned.
3197039	1	21	theme	methods	372:378	arg1	use					295:297	use	295:297	use of two-dimensional COSY and homonuclear Hartmann-Hann coherence transfer methods	295:378	The fully assigned 1H-n.m.r. spectra of a blood group A tetrasaccharide and of a blood group H hexasaccharide in dimethyl sulfoxide and in pyridine by use of two-dimensional COSY and homonuclear Hartmann-Hann coherence transfer methods are reported.
3197039	1	22	from	pyridine	283:290	arg1	spectra					173:179	The fully assigned 1H-n.m.r. spectra	144:179	The fully assigned 1H-n.m.r. spectra of a blood group A tetrasaccharide and of a blood group H hexasaccharide in dimethyl sulfoxide and in pyridine by use of two-dimensional COSY and homonuclear Hartmann-Hann coherence transfer methods	144:378	The fully assigned 1H-n.m.r. spectra of a blood group A tetrasaccharide and of a blood group H hexasaccharide in dimethyl sulfoxide and in pyridine by use of two-dimensional COSY and homonuclear Hartmann-Hann coherence transfer methods are reported.
3197039	5	23	theme	same	1323:1326	arg1	ring					1339:1342	the same pyranoside ring	1319:1342	the same pyranoside ring	1319:1342	Whereas n.O.e. depend strongly on temperature and solvent viscosity, the ratios of the effects between protons on the same pyranoside ring and those on different rings were observed to be similar, suggesting that the oligosaccharide conformations are not strongly dependent on solvent or temperature.
3197039	2	24	theme	deuterium	446:454	arg1	oxide					456:460	deuterium oxide	446:460	deuterium oxide	446:460	The 1H-n.m.r. spectra of both of these compounds in deuterium oxide had been previously assigned.
3197039	1	25	from	sulfoxide	266:274	arg1	spectra					173:179	The fully assigned 1H-n.m.r. spectra	144:179	The fully assigned 1H-n.m.r. spectra of a blood group A tetrasaccharide and of a blood group H hexasaccharide in dimethyl sulfoxide and in pyridine by use of two-dimensional COSY and homonuclear Hartmann-Hann coherence transfer methods	144:378	The fully assigned 1H-n.m.r. spectra of a blood group A tetrasaccharide and of a blood group H hexasaccharide in dimethyl sulfoxide and in pyridine by use of two-dimensional COSY and homonuclear Hartmann-Hann coherence transfer methods are reported.
3197039	4	26	theme	sample	1185:1190	arg1	temperature					1192:1202	sample temperature	1185:1202	sample temperature	1185:1202	Although the rotational correlation times (tau c) of these oligosaccharides are similar to the reciprocal of the spectrometer frequency, either negative or positive n.O.e. values were measurable for both oligosaccharides in all three solvents in one-dimensional difference spectroscopy by taking advantage of the dependence of tau c on the solvent viscosity and, thus, on sample temperature.
3197039	5	27	from	ratios	1278:1283	arg1	ring					1339:1342	the same pyranoside ring	1319:1342	the same pyranoside ring	1319:1342	Whereas n.O.e. depend strongly on temperature and solvent viscosity, the ratios of the effects between protons on the same pyranoside ring and those on different rings were observed to be similar, suggesting that the oligosaccharide conformations are not strongly dependent on solvent or temperature.
3197039	3	28	theme	method	711:716	arg1	extension					694:702	an extension	691:702	an extension of the method of complete proton assignments for determination of the structure of complex oligosaccharides	691:810	Since the relative proton chemical shifts in the three solvents are quite different, resonances which overlap or are strongly coupled for one solvent may be well resolved for another, thus providing an extension of the method of complete proton assignments for determination of the structure of complex oligosaccharides.
3197039	5	29	from	ring	1339:1342	arg1	similar					1393:1399	similar	1393:1399	similar	1393:1399	Whereas n.O.e. depend strongly on temperature and solvent viscosity, the ratios of the effects between protons on the same pyranoside ring and those on different rings were observed to be similar, suggesting that the oligosaccharide conformations are not strongly dependent on solvent or temperature.
3197039	5	29	from	ring	1339:1342	arg1	ratios					1278:1283	the ratios	1274:1283	the ratios of the effects between protons on the same pyranoside ring	1274:1342	Whereas n.O.e. depend strongly on temperature and solvent viscosity, the ratios of the effects between protons on the same pyranoside ring and those on different rings were observed to be similar, suggesting that the oligosaccharide conformations are not strongly dependent on solvent or temperature.
3197039	3	30	theme	proton	730:735	arg1	assignments					737:747	complete proton assignments	721:747	complete proton assignments	721:747	Since the relative proton chemical shifts in the three solvents are quite different, resonances which overlap or are strongly coupled for one solvent may be well resolved for another, thus providing an extension of the method of complete proton assignments for determination of the structure of complex oligosaccharides.
3197039	1	31	theme	blood	186:190	arg1	tetrasaccharide					200:214	a blood group A tetrasaccharide	184:214	a blood group A tetrasaccharide	184:214	The fully assigned 1H-n.m.r. spectra of a blood group A tetrasaccharide and of a blood group H hexasaccharide in dimethyl sulfoxide and in pyridine by use of two-dimensional COSY and homonuclear Hartmann-Hann coherence transfer methods are reported.
3197039	3	32	theme	assignments	737:747	arg1	method					711:716	the method	707:716	the method of complete proton assignments for determination of the structure of complex oligosaccharides	707:810	Since the relative proton chemical shifts in the three solvents are quite different, resonances which overlap or are strongly coupled for one solvent may be well resolved for another, thus providing an extension of the method of complete proton assignments for determination of the structure of complex oligosaccharides.
3197039	0	33	theme	non-aqueous	122:132	arg1	solvents					134:141	non-aqueous solvents	122:141	non-aqueous solvents	122:141	The determination of the structure of blood group oligosaccharides from fully assigned 1H-n.m.r. spectra for solutions in non-aqueous solvents.
3197039	3	34	from	shifts	527:532	arg1	solvents					547:554	the three solvents	537:554	the three solvents	537:554	Since the relative proton chemical shifts in the three solvents are quite different, resonances which overlap or are strongly coupled for one solvent may be well resolved for another, thus providing an extension of the method of complete proton assignments for determination of the structure of complex oligosaccharides.
3197039	5	35	theme	effects	1292:1298	arg1	similar					1393:1399	similar	1393:1399	similar	1393:1399	Whereas n.O.e. depend strongly on temperature and solvent viscosity, the ratios of the effects between protons on the same pyranoside ring and those on different rings were observed to be similar, suggesting that the oligosaccharide conformations are not strongly dependent on solvent or temperature.
3197039	5	35	theme	effects	1292:1298	arg1	ratios					1278:1283	the ratios	1274:1283	the ratios of the effects between protons on the same pyranoside ring	1274:1342	Whereas n.O.e. depend strongly on temperature and solvent viscosity, the ratios of the effects between protons on the same pyranoside ring and those on different rings were observed to be similar, suggesting that the oligosaccharide conformations are not strongly dependent on solvent or temperature.
3197039	1	36	theme	group	192:196	arg1	tetrasaccharide					200:214	a blood group A tetrasaccharide	184:214	a blood group A tetrasaccharide	184:214	The fully assigned 1H-n.m.r. spectra of a blood group A tetrasaccharide and of a blood group H hexasaccharide in dimethyl sulfoxide and in pyridine by use of two-dimensional COSY and homonuclear Hartmann-Hann coherence transfer methods are reported.
3197039	3	37	theme	proton	511:516	arg1	different					566:574	different	566:574	different	566:574	Since the relative proton chemical shifts in the three solvents are quite different, resonances which overlap or are strongly coupled for one solvent may be well resolved for another, thus providing an extension of the method of complete proton assignments for determination of the structure of complex oligosaccharides.
3197039	3	37	theme	proton	511:516	arg1	shifts					527:532	the relative proton chemical shifts	498:532	the relative proton chemical shifts in the three solvents	498:554	Since the relative proton chemical shifts in the three solvents are quite different, resonances which overlap or are strongly coupled for one solvent may be well resolved for another, thus providing an extension of the method of complete proton assignments for determination of the structure of complex oligosaccharides.
3197039	4	38	theme	dependence	1126:1135	arg1	advantage					1109:1117	advantage	1109:1117	advantage of the dependence of tau c on the solvent viscosity and, thus, on sample temperature	1109:1202	Although the rotational correlation times (tau c) of these oligosaccharides are similar to the reciprocal of the spectrometer frequency, either negative or positive n.O.e. values were measurable for both oligosaccharides in all three solvents in one-dimensional difference spectroscopy by taking advantage of the dependence of tau c on the solvent viscosity and, thus, on sample temperature.
3197039	1	39	theme	A	198:198	arg1	tetrasaccharide					200:214	a blood group A tetrasaccharide	184:214	a blood group A tetrasaccharide	184:214	The fully assigned 1H-n.m.r. spectra of a blood group A tetrasaccharide and of a blood group H hexasaccharide in dimethyl sulfoxide and in pyridine by use of two-dimensional COSY and homonuclear Hartmann-Hann coherence transfer methods are reported.
3197039	3	40	theme	complete	721:728	arg1	assignments					737:747	complete proton assignments	721:747	complete proton assignments	721:747	Since the relative proton chemical shifts in the three solvents are quite different, resonances which overlap or are strongly coupled for one solvent may be well resolved for another, thus providing an extension of the method of complete proton assignments for determination of the structure of complex oligosaccharides.
3197039	4	41	theme	spectrometer	926:937	arg1	frequency					939:947	the spectrometer frequency	922:947	the spectrometer frequency	922:947	Although the rotational correlation times (tau c) of these oligosaccharides are similar to the reciprocal of the spectrometer frequency, either negative or positive n.O.e. values were measurable for both oligosaccharides in all three solvents in one-dimensional difference spectroscopy by taking advantage of the dependence of tau c on the solvent viscosity and, thus, on sample temperature.
3197039	5	42	theme	solvent	1255:1261	arg1	viscosity					1263:1271	solvent viscosity	1255:1271	solvent viscosity	1255:1271	Whereas n.O.e. depend strongly on temperature and solvent viscosity, the ratios of the effects between protons on the same pyranoside ring and those on different rings were observed to be similar, suggesting that the oligosaccharide conformations are not strongly dependent on solvent or temperature.
3197039	1	43	theme	tetrasaccharide	200:214	arg1	spectra					173:179	The fully assigned 1H-n.m.r. spectra	144:179	The fully assigned 1H-n.m.r. spectra of a blood group A tetrasaccharide and of a blood group H hexasaccharide in dimethyl sulfoxide and in pyridine by use of two-dimensional COSY and homonuclear Hartmann-Hann coherence transfer methods	144:378	The fully assigned 1H-n.m.r. spectra of a blood group A tetrasaccharide and of a blood group H hexasaccharide in dimethyl sulfoxide and in pyridine by use of two-dimensional COSY and homonuclear Hartmann-Hann coherence transfer methods are reported.
3197039	0	44	theme	structure	25:33	arg1	determination					4:16	The determination	0:16	The determination of the structure of blood group	0:48	The determination of the structure of blood group oligosaccharides from fully assigned 1H-n.m.r. spectra for solutions in non-aqueous solvents.
3197039	1	45	from	hexasaccharide	239:252	arg1	sulfoxide					266:274	dimethyl sulfoxide	257:274	dimethyl sulfoxide	257:274	The fully assigned 1H-n.m.r. spectra of a blood group A tetrasaccharide and of a blood group H hexasaccharide in dimethyl sulfoxide and in pyridine by use of two-dimensional COSY and homonuclear Hartmann-Hann coherence transfer methods are reported.
3197039	1	45	from	hexasaccharide	239:252	arg1	pyridine					283:290	pyridine	283:290	pyridine by use of two-dimensional COSY and homonuclear Hartmann-Hann coherence transfer methods	283:378	The fully assigned 1H-n.m.r. spectra of a blood group A tetrasaccharide and of a blood group H hexasaccharide in dimethyl sulfoxide and in pyridine by use of two-dimensional COSY and homonuclear Hartmann-Hann coherence transfer methods are reported.
3197039	5	46	theme	oligosaccharide	1422:1436	arg1	conformations					1438:1450	the oligosaccharide conformations	1418:1450	the oligosaccharide conformations	1418:1450	Whereas n.O.e. depend strongly on temperature and solvent viscosity, the ratios of the effects between protons on the same pyranoside ring and those on different rings were observed to be similar, suggesting that the oligosaccharide conformations are not strongly dependent on solvent or temperature.
3197039	5	46	theme	oligosaccharide	1422:1436	arg1	dependent					1469:1477	dependent	1469:1477	dependent	1469:1477	Whereas n.O.e. depend strongly on temperature and solvent viscosity, the ratios of the effects between protons on the same pyranoside ring and those on different rings were observed to be similar, suggesting that the oligosaccharide conformations are not strongly dependent on solvent or temperature.
3197039	3	47	theme	structure	774:782	arg1	determination					753:765	determination	753:765	determination of the structure of complex oligosaccharides	753:810	Since the relative proton chemical shifts in the three solvents are quite different, resonances which overlap or are strongly coupled for one solvent may be well resolved for another, thus providing an extension of the method of complete proton assignments for determination of the structure of complex oligosaccharides.
3197039	5	48	theme	different	1357:1365	arg1	rings					1367:1371	different rings	1357:1371	different rings	1357:1371	Whereas n.O.e. depend strongly on temperature and solvent viscosity, the ratios of the effects between protons on the same pyranoside ring and those on different rings were observed to be similar, suggesting that the oligosaccharide conformations are not strongly dependent on solvent or temperature.
3197039	0	49	theme	group	44:48	arg1	structure					25:33	the structure	21:33	the structure of blood group	21:48	The determination of the structure of blood group oligosaccharides from fully assigned 1H-n.m.r. spectra for solutions in non-aqueous solvents.
3197039	4	50	from	measurable	997:1006	arg1	solvents					1047:1054	all three solvents	1037:1054	all three solvents in one-dimensional difference spectroscopy	1037:1097	Although the rotational correlation times (tau c) of these oligosaccharides are similar to the reciprocal of the spectrometer frequency, either negative or positive n.O.e. values were measurable for both oligosaccharides in all three solvents in one-dimensional difference spectroscopy by taking advantage of the dependence of tau c on the solvent viscosity and, thus, on sample temperature.
3197039	4	51	theme	rotational	826:835	arg1	similar					893:899	similar	893:899	similar	893:899	Although the rotational correlation times (tau c) of these oligosaccharides are similar to the reciprocal of the spectrometer frequency, either negative or positive n.O.e. values were measurable for both oligosaccharides in all three solvents in one-dimensional difference spectroscopy by taking advantage of the dependence of tau c on the solvent viscosity and, thus, on sample temperature.
3197039	4	51	theme	rotational	826:835	arg1	times					849:853	the rotational correlation times	822:853	the rotational correlation times (tau c) of these oligosaccharides	822:887	Although the rotational correlation times (tau c) of these oligosaccharides are similar to the reciprocal of the spectrometer frequency, either negative or positive n.O.e. values were measurable for both oligosaccharides in all three solvents in one-dimensional difference spectroscopy by taking advantage of the dependence of tau c on the solvent viscosity and, thus, on sample temperature.
3197039	4	51	theme	rotational	826:835	arg1	c					860:860	tau c	856:860	tau c	856:860	Although the rotational correlation times (tau c) of these oligosaccharides are similar to the reciprocal of the spectrometer frequency, either negative or positive n.O.e. values were measurable for both oligosaccharides in all three solvents in one-dimensional difference spectroscopy by taking advantage of the dependence of tau c on the solvent viscosity and, thus, on sample temperature.
3197039	0	52	theme	blood	38:42	arg1	group					44:48	blood group	38:48	blood group	38:48	The determination of the structure of blood group oligosaccharides from fully assigned 1H-n.m.r. spectra for solutions in non-aqueous solvents.
3197039	4	53	theme	oligosaccharides	872:887	arg1	similar					893:899	similar	893:899	similar	893:899	Although the rotational correlation times (tau c) of these oligosaccharides are similar to the reciprocal of the spectrometer frequency, either negative or positive n.O.e. values were measurable for both oligosaccharides in all three solvents in one-dimensional difference spectroscopy by taking advantage of the dependence of tau c on the solvent viscosity and, thus, on sample temperature.
3197039	4	53	theme	oligosaccharides	872:887	arg1	times					849:853	the rotational correlation times	822:853	the rotational correlation times (tau c) of these oligosaccharides	822:887	Although the rotational correlation times (tau c) of these oligosaccharides are similar to the reciprocal of the spectrometer frequency, either negative or positive n.O.e. values were measurable for both oligosaccharides in all three solvents in one-dimensional difference spectroscopy by taking advantage of the dependence of tau c on the solvent viscosity and, thus, on sample temperature.
3197039	4	53	theme	oligosaccharides	872:887	arg1	c					860:860	tau c	856:860	tau c	856:860	Although the rotational correlation times (tau c) of these oligosaccharides are similar to the reciprocal of the spectrometer frequency, either negative or positive n.O.e. values were measurable for both oligosaccharides in all three solvents in one-dimensional difference spectroscopy by taking advantage of the dependence of tau c on the solvent viscosity and, thus, on sample temperature.
3197039	0	54	from	solutions	109:117	arg1	solvents					134:141	non-aqueous solvents	122:141	non-aqueous solvents	122:141	The determination of the structure of blood group oligosaccharides from fully assigned 1H-n.m.r. spectra for solutions in non-aqueous solvents.
3197039	4	55	theme	correlation	837:847	arg1	similar					893:899	similar	893:899	similar	893:899	Although the rotational correlation times (tau c) of these oligosaccharides are similar to the reciprocal of the spectrometer frequency, either negative or positive n.O.e. values were measurable for both oligosaccharides in all three solvents in one-dimensional difference spectroscopy by taking advantage of the dependence of tau c on the solvent viscosity and, thus, on sample temperature.
3197039	4	55	theme	correlation	837:847	arg1	times					849:853	the rotational correlation times	822:853	the rotational correlation times (tau c) of these oligosaccharides	822:887	Although the rotational correlation times (tau c) of these oligosaccharides are similar to the reciprocal of the spectrometer frequency, either negative or positive n.O.e. values were measurable for both oligosaccharides in all three solvents in one-dimensional difference spectroscopy by taking advantage of the dependence of tau c on the solvent viscosity and, thus, on sample temperature.
3197039	4	55	theme	correlation	837:847	arg1	c					860:860	tau c	856:860	tau c	856:860	Although the rotational correlation times (tau c) of these oligosaccharides are similar to the reciprocal of the spectrometer frequency, either negative or positive n.O.e. values were measurable for both oligosaccharides in all three solvents in one-dimensional difference spectroscopy by taking advantage of the dependence of tau c on the solvent viscosity and, thus, on sample temperature.
3197039	5	56	from	effects	1292:1298	arg1	ring					1339:1342	the same pyranoside ring	1319:1342	the same pyranoside ring	1319:1342	Whereas n.O.e. depend strongly on temperature and solvent viscosity, the ratios of the effects between protons on the same pyranoside ring and those on different rings were observed to be similar, suggesting that the oligosaccharide conformations are not strongly dependent on solvent or temperature.
3197039	1	57	theme	two-dimensional	302:316	arg1	COSY					318:321	two-dimensional COSY and homonuclear Hartmann-Hann coherence transfer methods	302:378	COSY	318:321	The fully assigned 1H-n.m.r. spectra of a blood group A tetrasaccharide and of a blood group H hexasaccharide in dimethyl sulfoxide and in pyridine by use of two-dimensional COSY and homonuclear Hartmann-Hann coherence transfer methods are reported.
3197039	4	58	theme	difference	1075:1084	arg1	spectroscopy					1086:1097	one-dimensional difference spectroscopy	1059:1097	one-dimensional difference spectroscopy	1059:1097	Although the rotational correlation times (tau c) of these oligosaccharides are similar to the reciprocal of the spectrometer frequency, either negative or positive n.O.e. values were measurable for both oligosaccharides in all three solvents in one-dimensional difference spectroscopy by taking advantage of the dependence of tau c on the solvent viscosity and, thus, on sample temperature.
3197039	3	59	theme	complex	787:793	arg1	oligosaccharides					795:810	complex oligosaccharides	787:810	complex oligosaccharides	787:810	Since the relative proton chemical shifts in the three solvents are quite different, resonances which overlap or are strongly coupled for one solvent may be well resolved for another, thus providing an extension of the method of complete proton assignments for determination of the structure of complex oligosaccharides.
3197039	4	60	theme	solvent	1153:1159	arg1	viscosity					1161:1169	the solvent viscosity	1149:1169	the solvent viscosity	1149:1169	Although the rotational correlation times (tau c) of these oligosaccharides are similar to the reciprocal of the spectrometer frequency, either negative or positive n.O.e. values were measurable for both oligosaccharides in all three solvents in one-dimensional difference spectroscopy by taking advantage of the dependence of tau c on the solvent viscosity and, thus, on sample temperature.
3197039	5	61	theme	pyranoside	1328:1337	arg1	ring					1339:1342	the same pyranoside ring	1319:1342	the same pyranoside ring	1319:1342	Whereas n.O.e. depend strongly on temperature and solvent viscosity, the ratios of the effects between protons on the same pyranoside ring and those on different rings were observed to be similar, suggesting that the oligosaccharide conformations are not strongly dependent on solvent or temperature.
3197039	3	62	theme	oligosaccharides	795:810	arg1	structure					774:782	the structure	770:782	the structure of complex oligosaccharides	770:810	Since the relative proton chemical shifts in the three solvents are quite different, resonances which overlap or are strongly coupled for one solvent may be well resolved for another, thus providing an extension of the method of complete proton assignments for determination of the structure of complex oligosaccharides.
3197039	2	63	from	spectra	408:414	arg1	oxide					456:460	deuterium oxide	446:460	deuterium oxide	446:460	The 1H-n.m.r. spectra of both of these compounds in deuterium oxide had been previously assigned.
3197039	3	64	theme	chemical	518:525	arg1	different					566:574	different	566:574	different	566:574	Since the relative proton chemical shifts in the three solvents are quite different, resonances which overlap or are strongly coupled for one solvent may be well resolved for another, thus providing an extension of the method of complete proton assignments for determination of the structure of complex oligosaccharides.
3197039	3	64	theme	chemical	518:525	arg1	shifts					527:532	the relative proton chemical shifts	498:532	the relative proton chemical shifts in the three solvents	498:554	Since the relative proton chemical shifts in the three solvents are quite different, resonances which overlap or are strongly coupled for one solvent may be well resolved for another, thus providing an extension of the method of complete proton assignments for determination of the structure of complex oligosaccharides.
3197039	1	65	theme	blood	225:229	arg1	hexasaccharide					239:252	a blood group H hexasaccharide	223:252	a blood group H hexasaccharide in dimethyl sulfoxide and in pyridine by use of two-dimensional COSY and homonuclear Hartmann-Hann coherence transfer methods	223:378	The fully assigned 1H-n.m.r. spectra of a blood group A tetrasaccharide and of a blood group H hexasaccharide in dimethyl sulfoxide and in pyridine by use of two-dimensional COSY and homonuclear Hartmann-Hann coherence transfer methods are reported.
3197039	4	66	theme	negative	957:964	arg1	values					985:990	either negative or positive n.O.e. values	950:990	either negative or positive n.O.e. values	950:990	Although the rotational correlation times (tau c) of these oligosaccharides are similar to the reciprocal of the spectrometer frequency, either negative or positive n.O.e. values were measurable for both oligosaccharides in all three solvents in one-dimensional difference spectroscopy by taking advantage of the dependence of tau c on the solvent viscosity and, thus, on sample temperature.
3197039	1	67	theme	COSY	318:321	arg1	use					295:297	use	295:297	use of two-dimensional COSY and homonuclear Hartmann-Hann coherence transfer methods	295:378	The fully assigned 1H-n.m.r. spectra of a blood group A tetrasaccharide and of a blood group H hexasaccharide in dimethyl sulfoxide and in pyridine by use of two-dimensional COSY and homonuclear Hartmann-Hann coherence transfer methods are reported.
3197039	1	68	from	spectra	173:179	arg1	sulfoxide					266:274	dimethyl sulfoxide	257:274	dimethyl sulfoxide	257:274	The fully assigned 1H-n.m.r. spectra of a blood group A tetrasaccharide and of a blood group H hexasaccharide in dimethyl sulfoxide and in pyridine by use of two-dimensional COSY and homonuclear Hartmann-Hann coherence transfer methods are reported.
3197039	1	68	from	spectra	173:179	arg1	pyridine					283:290	pyridine	283:290	pyridine by use of two-dimensional COSY and homonuclear Hartmann-Hann coherence transfer methods	283:378	The fully assigned 1H-n.m.r. spectra of a blood group A tetrasaccharide and of a blood group H hexasaccharide in dimethyl sulfoxide and in pyridine by use of two-dimensional COSY and homonuclear Hartmann-Hann coherence transfer methods are reported.
3197039	1	69	theme	group	231:235	arg1	hexasaccharide					239:252	a blood group H hexasaccharide	223:252	a blood group H hexasaccharide in dimethyl sulfoxide and in pyridine by use of two-dimensional COSY and homonuclear Hartmann-Hann coherence transfer methods	223:378	The fully assigned 1H-n.m.r. spectra of a blood group A tetrasaccharide and of a blood group H hexasaccharide in dimethyl sulfoxide and in pyridine by use of two-dimensional COSY and homonuclear Hartmann-Hann coherence transfer methods are reported.
1639758	3	0	theme	glycoprotein	555:566	arg1	separation					537:546	electrophoretic separation	521:546	electrophoretic separation of the glycoprotein	521:566	After electrophoretic separation of the glycoprotein, oligosaccharides were released by the use of a gas-phase hydrazinolysis apparatus.
1639758	4	1	theme	water	824:828	arg1	removal					813:819	removal	813:819	removal of water in a P2O5 desiccator	813:849	In the first method, the gel was stained with Coomassie Blue and the glycoprotein together with the gel was directly subjected to gas-phase hydrazinolysis after removal of water in a P2O5 desiccator.
1639758	6	2	theme	second	1019:1024	arg1	method					1026:1031	the second method	1015:1031	the second method	1015:1031	In the second method, the glycoprotein was electroblotted onto an Immobilon transfer membrane and was visualized by staining with Coomassie Blue.
1639758	2	3	with	incubation	448:457	arg1	oxidase					476:482	D-galactose oxidase	464:482	D-galactose oxidase	464:482	Asialo-alpha 1-acid glycoprotein, which was tritiated at the nonreducing terminal D-galactopyranosyl residue by reduction with sodium borotritide after incubation with D-galactose oxidase, was used as a model compound.
1639758	6	4	theme	Blue	1152:1155	arg1	Coomassie					1142:1150	Coomassie Blue	1142:1155	Coomassie Blue	1142:1155	In the second method, the glycoprotein was electroblotted onto an Immobilon transfer membrane and was visualized by staining with Coomassie Blue.
1639758	8	5	from	%	1366:1366	arg1	case					1302:1305	this case	1297:1305	this case	1297:1305	In this case, the recovery of released oligosaccharides was 15.2 +/- 1.0%.
1639758	5	6	theme	micrograms	1000:1009	arg1	range					982:986	the range	978:986	the range of 3.5-28.5 micrograms	978:1009	The recovery of released oligosaccharides was 25.9 +/- 2.4%, based on the amount of the glycoprotein loaded on the gel within the range of 3.5-28.5 micrograms.
1639758	2	7	gly	glycoprotein	316:327	arg1	glycoprotein					316:327	Asialo-alpha 1-acid glycoprotein	296:327	Asialo-alpha 1-acid glycoprotein	296:327	Asialo-alpha 1-acid glycoprotein, which was tritiated at the nonreducing terminal D-galactopyranosyl residue by reduction with sodium borotritide after incubation with D-galactose oxidase, was used as a model compound.
1639758	2	7	gly	glycoprotein	316:327	arg1	compound					505:512	a model compound	497:512	a model compound	497:512	Asialo-alpha 1-acid glycoprotein, which was tritiated at the nonreducing terminal D-galactopyranosyl residue by reduction with sodium borotritide after incubation with D-galactose oxidase, was used as a model compound.
1639758	1	8	gly	glycoproteins	199:211	arg1	glycoproteins					199:211	glycoproteins	199:211	glycoproteins separated by SDS-polyacrylamide gel electrophoresis (SDS-PAGE)	199:274	A simple method for the release of oligosaccharides from glycoproteins separated by SDS-polyacrylamide gel electrophoresis (SDS-PAGE) has been developed.
1639758	4	9	from	water	824:828	arg1	desiccator					840:849	a P2O5 desiccator	833:849	a P2O5 desiccator	833:849	In the first method, the gel was stained with Coomassie Blue and the glycoprotein together with the gel was directly subjected to gas-phase hydrazinolysis after removal of water in a P2O5 desiccator.
1639758	4	10	theme	gas-phase	782:790	arg1	hydrazinolysis					792:805	gas-phase hydrazinolysis	782:805	gas-phase hydrazinolysis after removal of water in a P2O5 desiccator	782:849	In the first method, the gel was stained with Coomassie Blue and the glycoprotein together with the gel was directly subjected to gas-phase hydrazinolysis after removal of water in a P2O5 desiccator.
1639758	8	11	theme	oligosaccharides	1333:1348	arg1	recovery					1312:1319	the recovery	1308:1319	the recovery of released oligosaccharides	1308:1348	In this case, the recovery of released oligosaccharides was 15.2 +/- 1.0%.
1639758	8	11	theme	oligosaccharides	1333:1348	arg1	%					1366:1366	15.2 +/- 1.0%	1354:1366	15.2 +/- 1.0%	1354:1366	In this case, the recovery of released oligosaccharides was 15.2 +/- 1.0%.
1639758	7	12	theme	gas-phase	1268:1276	arg1	hydrazinolysis					1278:1291	gas-phase hydrazinolysis	1268:1291	gas-phase hydrazinolysis	1268:1291	A small piece of the membrane with the corresponding band was cut out, dried in a desiccator and subjected to gas-phase hydrazinolysis.
1639758	0	13	theme	gel	121:123	arg1	electrophoresis					125:139	SDS-polyacrylamide gel electrophoresis	102:139	SDS-polyacrylamide gel electrophoresis	102:139	A simple method for the release of asparagine-linked oligosaccharides from a glycoprotein purified by SDS-polyacrylamide gel electrophoresis.
1639758	2	14	used	used	489:492	arg2	compound					505:512	a model compound	497:512	a model compound	497:512	Asialo-alpha 1-acid glycoprotein, which was tritiated at the nonreducing terminal D-galactopyranosyl residue by reduction with sodium borotritide after incubation with D-galactose oxidase, was used as a model compound.
1639758	2	14	used	used	489:492	arg2	glycoprotein					316:327	Asialo-alpha 1-acid glycoprotein	296:327	Asialo-alpha 1-acid glycoprotein	296:327	Asialo-alpha 1-acid glycoprotein, which was tritiated at the nonreducing terminal D-galactopyranosyl residue by reduction with sodium borotritide after incubation with D-galactose oxidase, was used as a model compound.
1639758	4	15	from	removal	813:819	arg1	desiccator					840:849	a P2O5 desiccator	833:849	a P2O5 desiccator	833:849	In the first method, the gel was stained with Coomassie Blue and the glycoprotein together with the gel was directly subjected to gas-phase hydrazinolysis after removal of water in a P2O5 desiccator.
1639758	2	16	theme	1-acid	309:314	arg1	glycoprotein					316:327	Asialo-alpha 1-acid glycoprotein	296:327	Asialo-alpha 1-acid glycoprotein	296:327	Asialo-alpha 1-acid glycoprotein, which was tritiated at the nonreducing terminal D-galactopyranosyl residue by reduction with sodium borotritide after incubation with D-galactose oxidase, was used as a model compound.
1639758	2	16	theme	1-acid	309:314	arg1	compound					505:512	a model compound	497:512	a model compound	497:512	Asialo-alpha 1-acid glycoprotein, which was tritiated at the nonreducing terminal D-galactopyranosyl residue by reduction with sodium borotritide after incubation with D-galactose oxidase, was used as a model compound.
1639758	4	17	theme	Blue	708:711	arg1	Coomassie					698:706	Coomassie Blue	698:711	Coomassie Blue	698:711	In the first method, the gel was stained with Coomassie Blue and the glycoprotein together with the gel was directly subjected to gas-phase hydrazinolysis after removal of water in a P2O5 desiccator.
1639758	0	18	theme	SDS-polyacrylamide	102:119	arg1	electrophoresis					125:139	SDS-polyacrylamide gel electrophoresis	102:139	SDS-polyacrylamide gel electrophoresis	102:139	A simple method for the release of asparagine-linked oligosaccharides from a glycoprotein purified by SDS-polyacrylamide gel electrophoresis.
1639758	0	19	link	asparagine-linked	35:51	arg1	oligosaccharides					53:68	asparagine-linked oligosaccharides	35:68	asparagine-linked oligosaccharides	35:68	A simple method for the release of asparagine-linked oligosaccharides from a glycoprotein purified by SDS-polyacrylamide gel electrophoresis.
1639758	0	20	gly	glycoprotein	77:88	arg1	glycoprotein					77:88	a glycoprotein	75:88	a glycoprotein	75:88	A simple method for the release of asparagine-linked oligosaccharides from a glycoprotein purified by SDS-polyacrylamide gel electrophoresis.
1639758	1	21	theme	oligosaccharides	177:192	arg1	release					166:172	the release	162:172	the release of oligosaccharides from glycoproteins separated by SDS-polyacrylamide gel electrophoresis (SDS-PAGE)	162:274	A simple method for the release of oligosaccharides from glycoproteins separated by SDS-polyacrylamide gel electrophoresis (SDS-PAGE) has been developed.
1639758	0	22	theme	simple	2:7	arg1	method					9:14	A simple method	0:14	A simple method for the release of asparagine-linked oligosaccharides from a glycoprotein	0:88	A simple method for the release of asparagine-linked oligosaccharides from a glycoprotein purified by SDS-polyacrylamide gel electrophoresis.
1639758	2	23	from	residue	397:403	arg1	tritiated					340:348	tritiated	340:348	tritiated	340:348	Asialo-alpha 1-acid glycoprotein, which was tritiated at the nonreducing terminal D-galactopyranosyl residue by reduction with sodium borotritide after incubation with D-galactose oxidase, was used as a model compound.
1639758	3	24	theme	gas-phase	616:624	arg1	apparatus					641:649	a gas-phase hydrazinolysis apparatus	614:649	a gas-phase hydrazinolysis apparatus	614:649	After electrophoretic separation of the glycoprotein, oligosaccharides were released by the use of a gas-phase hydrazinolysis apparatus.
1639758	6	25	theme	transfer	1088:1095	arg1	membrane					1097:1104	an Immobilon transfer membrane	1075:1104	an Immobilon transfer membrane	1075:1104	In the second method, the glycoprotein was electroblotted onto an Immobilon transfer membrane and was visualized by staining with Coomassie Blue.
1639758	3	26	theme	hydrazinolysis	626:639	arg1	apparatus					641:649	a gas-phase hydrazinolysis apparatus	614:649	a gas-phase hydrazinolysis apparatus	614:649	After electrophoretic separation of the glycoprotein, oligosaccharides were released by the use of a gas-phase hydrazinolysis apparatus.
1639758	2	27	theme	sodium	423:428	arg1	borotritide					430:440	sodium borotritide	423:440	sodium borotritide	423:440	Asialo-alpha 1-acid glycoprotein, which was tritiated at the nonreducing terminal D-galactopyranosyl residue by reduction with sodium borotritide after incubation with D-galactose oxidase, was used as a model compound.
1639758	4	28	theme	first	659:663	arg1	method					665:670	the first method	655:670	the first method	655:670	In the first method, the gel was stained with Coomassie Blue and the glycoprotein together with the gel was directly subjected to gas-phase hydrazinolysis after removal of water in a P2O5 desiccator.
1639758	5	29	gly	glycoprotein	940:951	arg1	glycoprotein					940:951	the glycoprotein	936:951	the glycoprotein loaded on the gel within the range of 3.5-28.5 micrograms	936:1009	The recovery of released oligosaccharides was 25.9 +/- 2.4%, based on the amount of the glycoprotein loaded on the gel within the range of 3.5-28.5 micrograms.
1639758	9	30	from	glycoproteins	1486:1498	arg1	isolation					1451:1459	the isolation	1447:1459	the isolation of oligosaccharides from glycoproteins separated by SDS-PAGE	1447:1520	These procedures, particularly the first one, should be widely applicable for the isolation of oligosaccharides from glycoproteins separated by SDS-PAGE.
1639758	9	30	from	glycoproteins	1486:1498	arg1	oligosaccharides					1464:1479	oligosaccharides	1464:1479	oligosaccharides from glycoproteins separated by SDS-PAGE	1464:1520	These procedures, particularly the first one, should be widely applicable for the isolation of oligosaccharides from glycoproteins separated by SDS-PAGE.
1639758	5	31	theme	oligosaccharides	877:892	arg1	recovery					856:863	The recovery	852:863	The recovery of released oligosaccharides	852:892	The recovery of released oligosaccharides was 25.9 +/- 2.4%, based on the amount of the glycoprotein loaded on the gel within the range of 3.5-28.5 micrograms.
1639758	5	31	theme	oligosaccharides	877:892	arg1	%					910:910	25.9 +/- 2.4%	898:910	25.9 +/- 2.4%	898:910	The recovery of released oligosaccharides was 25.9 +/- 2.4%, based on the amount of the glycoprotein loaded on the gel within the range of 3.5-28.5 micrograms.
1639758	4	32	from	desiccator	840:849	arg1	removal					813:819	removal	813:819	removal of water in a P2O5 desiccator	813:849	In the first method, the gel was stained with Coomassie Blue and the glycoprotein together with the gel was directly subjected to gas-phase hydrazinolysis after removal of water in a P2O5 desiccator.
1639758	7	33	with	piece	1166:1170	arg1	band					1211:1214	the corresponding band	1193:1214	the corresponding band	1193:1214	A small piece of the membrane with the corresponding band was cut out, dried in a desiccator and subjected to gas-phase hydrazinolysis.
1639758	0	34	from	glycoprotein	77:88	arg1	release					24:30	the release	20:30	the release of asparagine-linked oligosaccharides from a glycoprotein	20:88	A simple method for the release of asparagine-linked oligosaccharides from a glycoprotein purified by SDS-polyacrylamide gel electrophoresis.
1639758	5	35	theme	glycoprotein	940:951	arg1	amount					926:931	the amount	922:931	the amount of the glycoprotein loaded on the gel within the range of 3.5-28.5 micrograms	922:1009	The recovery of released oligosaccharides was 25.9 +/- 2.4%, based on the amount of the glycoprotein loaded on the gel within the range of 3.5-28.5 micrograms.
1639758	5	35	theme	glycoprotein	940:951	arg1	glycoprotein					940:951	the glycoprotein	936:951	the glycoprotein loaded on the gel within the range of 3.5-28.5 micrograms	936:1009	The recovery of released oligosaccharides was 25.9 +/- 2.4%, based on the amount of the glycoprotein loaded on the gel within the range of 3.5-28.5 micrograms.
1639758	1	36	theme	SDS-polyacrylamide	226:243	arg1	SDS-PAGE					266:273	SDS-PAGE	266:273	SDS-PAGE	266:273	A simple method for the release of oligosaccharides from glycoproteins separated by SDS-polyacrylamide gel electrophoresis (SDS-PAGE) has been developed.
1639758	1	36	theme	SDS-polyacrylamide	226:243	arg1	electrophoresis					249:263	SDS-polyacrylamide gel electrophoresis	226:263	SDS-polyacrylamide gel electrophoresis (SDS-PAGE)	226:274	A simple method for the release of oligosaccharides from glycoproteins separated by SDS-polyacrylamide gel electrophoresis (SDS-PAGE) has been developed.
1639758	6	37	theme	Immobilon	1078:1086	arg1	membrane					1097:1104	an Immobilon transfer membrane	1075:1104	an Immobilon transfer membrane	1075:1104	In the second method, the glycoprotein was electroblotted onto an Immobilon transfer membrane and was visualized by staining with Coomassie Blue.
1639758	2	38	theme	D-galactose	464:474	arg1	oxidase					476:482	D-galactose oxidase	464:482	D-galactose oxidase	464:482	Asialo-alpha 1-acid glycoprotein, which was tritiated at the nonreducing terminal D-galactopyranosyl residue by reduction with sodium borotritide after incubation with D-galactose oxidase, was used as a model compound.
1639758	1	39	theme	gel	245:247	arg1	SDS-PAGE					266:273	SDS-PAGE	266:273	SDS-PAGE	266:273	A simple method for the release of oligosaccharides from glycoproteins separated by SDS-polyacrylamide gel electrophoresis (SDS-PAGE) has been developed.
1639758	1	39	theme	gel	245:247	arg1	electrophoresis					249:263	SDS-polyacrylamide gel electrophoresis	226:263	SDS-polyacrylamide gel electrophoresis (SDS-PAGE)	226:274	A simple method for the release of oligosaccharides from glycoproteins separated by SDS-polyacrylamide gel electrophoresis (SDS-PAGE) has been developed.
1639758	0	40	theme	asparagine-linked	35:51	arg1	oligosaccharides					53:68	asparagine-linked oligosaccharides	35:68	asparagine-linked oligosaccharides	35:68	A simple method for the release of asparagine-linked oligosaccharides from a glycoprotein purified by SDS-polyacrylamide gel electrophoresis.
1639758	3	41	gly	glycoprotein	555:566	arg1	glycoprotein					555:566	the glycoprotein	551:566	the glycoprotein	551:566	After electrophoretic separation of the glycoprotein, oligosaccharides were released by the use of a gas-phase hydrazinolysis apparatus.
1639758	4	42	gly	glycoprotein	721:732	arg1	glycoprotein					721:732	the glycoprotein	717:732	the glycoprotein together with the gel	717:754	In the first method, the gel was stained with Coomassie Blue and the glycoprotein together with the gel was directly subjected to gas-phase hydrazinolysis after removal of water in a P2O5 desiccator.
1639758	3	43	theme	apparatus	641:649	arg1	use					607:609	the use	603:609	the use of a gas-phase hydrazinolysis apparatus	603:649	After electrophoretic separation of the glycoprotein, oligosaccharides were released by the use of a gas-phase hydrazinolysis apparatus.
1639758	2	44	theme	D-galactopyranosyl	378:395	arg1	residue					397:403	the nonreducing terminal D-galactopyranosyl residue	353:403	the nonreducing terminal D-galactopyranosyl residue by reduction with sodium borotritide	353:440	Asialo-alpha 1-acid glycoprotein, which was tritiated at the nonreducing terminal D-galactopyranosyl residue by reduction with sodium borotritide after incubation with D-galactose oxidase, was used as a model compound.
1639758	2	45	theme	model	499:503	arg1	glycoprotein					316:327	Asialo-alpha 1-acid glycoprotein	296:327	Asialo-alpha 1-acid glycoprotein	296:327	Asialo-alpha 1-acid glycoprotein, which was tritiated at the nonreducing terminal D-galactopyranosyl residue by reduction with sodium borotritide after incubation with D-galactose oxidase, was used as a model compound.
1639758	2	45	theme	model	499:503	arg1	compound					505:512	a model compound	497:512	a model compound	497:512	Asialo-alpha 1-acid glycoprotein, which was tritiated at the nonreducing terminal D-galactopyranosyl residue by reduction with sodium borotritide after incubation with D-galactose oxidase, was used as a model compound.
1639758	9	46	gly	glycoproteins	1486:1498	arg1	glycoproteins					1486:1498	glycoproteins	1486:1498	glycoproteins separated by SDS-PAGE	1486:1520	These procedures, particularly the first one, should be widely applicable for the isolation of oligosaccharides from glycoproteins separated by SDS-PAGE.
1639758	2	47	theme	terminal	369:376	arg1	residue					397:403	the nonreducing terminal D-galactopyranosyl residue	353:403	the nonreducing terminal D-galactopyranosyl residue by reduction with sodium borotritide	353:440	Asialo-alpha 1-acid glycoprotein, which was tritiated at the nonreducing terminal D-galactopyranosyl residue by reduction with sodium borotritide after incubation with D-galactose oxidase, was used as a model compound.
1639758	6	48	gly	glycoprotein	1038:1049	arg1	glycoprotein					1038:1049	the glycoprotein	1034:1049	the glycoprotein	1034:1049	In the second method, the glycoprotein was electroblotted onto an Immobilon transfer membrane and was visualized by staining with Coomassie Blue.
1639758	7	49	theme	small	1160:1164	arg1	piece					1166:1170	A small piece	1158:1170	A small piece of the membrane with the corresponding band	1158:1214	A small piece of the membrane with the corresponding band was cut out, dried in a desiccator and subjected to gas-phase hydrazinolysis.
1639758	4	50	theme	P2O5	835:838	arg1	desiccator					840:849	a P2O5 desiccator	833:849	a P2O5 desiccator	833:849	In the first method, the gel was stained with Coomassie Blue and the glycoprotein together with the gel was directly subjected to gas-phase hydrazinolysis after removal of water in a P2O5 desiccator.
1639758	9	51	from	isolation	1451:1459	arg1	glycoproteins					1486:1498	glycoproteins	1486:1498	glycoproteins separated by SDS-PAGE	1486:1520	These procedures, particularly the first one, should be widely applicable for the isolation of oligosaccharides from glycoproteins separated by SDS-PAGE.
1639758	2	52	theme	nonreducing	357:367	arg1	residue					397:403	the nonreducing terminal D-galactopyranosyl residue	353:403	the nonreducing terminal D-galactopyranosyl residue by reduction with sodium borotritide	353:440	Asialo-alpha 1-acid glycoprotein, which was tritiated at the nonreducing terminal D-galactopyranosyl residue by reduction with sodium borotritide after incubation with D-galactose oxidase, was used as a model compound.
1639758	2	53	theme	Asialo-alpha	296:307	arg1	glycoprotein					316:327	Asialo-alpha 1-acid glycoprotein	296:327	Asialo-alpha 1-acid glycoprotein	296:327	Asialo-alpha 1-acid glycoprotein, which was tritiated at the nonreducing terminal D-galactopyranosyl residue by reduction with sodium borotritide after incubation with D-galactose oxidase, was used as a model compound.
1639758	2	53	theme	Asialo-alpha	296:307	arg1	compound					505:512	a model compound	497:512	a model compound	497:512	Asialo-alpha 1-acid glycoprotein, which was tritiated at the nonreducing terminal D-galactopyranosyl residue by reduction with sodium borotritide after incubation with D-galactose oxidase, was used as a model compound.
1639758	1	54	theme	simple	144:149	arg1	method					151:156	A simple method	142:156	A simple method for the release of oligosaccharides from glycoproteins separated by SDS-polyacrylamide gel electrophoresis (SDS-PAGE)	142:274	A simple method for the release of oligosaccharides from glycoproteins separated by SDS-polyacrylamide gel electrophoresis (SDS-PAGE) has been developed.
1639758	8	55	theme	released	1324:1331	arg1	oligosaccharides					1333:1348	released oligosaccharides	1324:1348	released oligosaccharides	1324:1348	In this case, the recovery of released oligosaccharides was 15.2 +/- 1.0%.
1639758	3	56	theme	electrophoretic	521:535	arg1	separation					537:546	electrophoretic separation	521:546	electrophoretic separation of the glycoprotein	521:566	After electrophoretic separation of the glycoprotein, oligosaccharides were released by the use of a gas-phase hydrazinolysis apparatus.
1639758	9	57	theme	oligosaccharides	1464:1479	arg1	isolation					1451:1459	the isolation	1447:1459	the isolation of oligosaccharides from glycoproteins separated by SDS-PAGE	1447:1520	These procedures, particularly the first one, should be widely applicable for the isolation of oligosaccharides from glycoproteins separated by SDS-PAGE.
1639758	2	58	with	reduction	408:416	arg1	borotritide					430:440	sodium borotritide	423:440	sodium borotritide	423:440	Asialo-alpha 1-acid glycoprotein, which was tritiated at the nonreducing terminal D-galactopyranosyl residue by reduction with sodium borotritide after incubation with D-galactose oxidase, was used as a model compound.
1639758	1	59	from	glycoproteins	199:211	arg1	release					166:172	the release	162:172	the release of oligosaccharides from glycoproteins separated by SDS-polyacrylamide gel electrophoresis (SDS-PAGE)	162:274	A simple method for the release of oligosaccharides from glycoproteins separated by SDS-polyacrylamide gel electrophoresis (SDS-PAGE) has been developed.
1639758	0	60	theme	oligosaccharides	53:68	arg1	release					24:30	the release	20:30	the release of asparagine-linked oligosaccharides from a glycoprotein	20:88	A simple method for the release of asparagine-linked oligosaccharides from a glycoprotein purified by SDS-polyacrylamide gel electrophoresis.
1639758	7	61	theme	corresponding	1197:1209	arg1	band					1211:1214	the corresponding band	1193:1214	the corresponding band	1193:1214	A small piece of the membrane with the corresponding band was cut out, dried in a desiccator and subjected to gas-phase hydrazinolysis.
1639758	5	62	theme	released	868:875	arg1	oligosaccharides					877:892	released oligosaccharides	868:892	released oligosaccharides	868:892	The recovery of released oligosaccharides was 25.9 +/- 2.4%, based on the amount of the glycoprotein loaded on the gel within the range of 3.5-28.5 micrograms.
1639758	7	63	theme	membrane	1179:1186	arg1	piece					1166:1170	A small piece	1158:1170	A small piece of the membrane with the corresponding band	1158:1214	A small piece of the membrane with the corresponding band was cut out, dried in a desiccator and subjected to gas-phase hydrazinolysis.
2387072	4	0	theme	triantennary	1017:1028	arg1	type					1030:1033	the di and triantennary type	1006:1033	the di and triantennary type containing sialic acid linked alpha 2----3 and alpha 2----6 to galactose in an approximate molar ratio of 3:2 and 2:1	1006:1151	The glycopeptides from both sources were of the di and triantennary type containing sialic acid linked alpha 2----3 and alpha 2----6 to galactose in an approximate molar ratio of 3:2 and 2:1, from CF and Control, respectively.
2387072	5	1	gly	glycopeptides	1486:1498	arg2	glycopeptides					1486:1498	the peripheral membrane glycopeptides	1462:1498	the peripheral membrane glycopeptides	1462:1498	Glycopeptides derived from a glycoprotein, fibronectin, secreted from CF fibroblasts were also examined by 1H-NMR spectroscopy and showed no evidence of fucosyl residues linked alpha 1----3 to branch N-acetylglucosamine and a lesser percentage of core fucose than found in the peripheral membrane glycopeptides.
2387072	3	2	theme	different	714:722	arg1	features					724:731	two different features	710:731	two different features	710:731	The CF derived glycopeptides had two different features when compared to those from Controls (1) an increased number of fucosyl residues linked alpha 1----6 to the N-acetylglucosamine attached to asparagine and (2) fucosyl residues linked alpha 1----3 to a branch N-acetylglucosamine.
2387072	3	3	attach	linked	909:914	arg2	residues					900:907	fucosyl residues	892:907	fucosyl residues	892:907	The CF derived glycopeptides had two different features when compared to those from Controls (1) an increased number of fucosyl residues linked alpha 1----6 to the N-acetylglucosamine attached to asparagine and (2) fucosyl residues linked alpha 1----3 to a branch N-acetylglucosamine.
2387072	3	3	attach	linked	909:914	arg1	N-acetylglucosamine					941:959	a branch N-acetylglucosamine	932:959	a branch N-acetylglucosamine	932:959	The CF derived glycopeptides had two different features when compared to those from Controls (1) an increased number of fucosyl residues linked alpha 1----6 to the N-acetylglucosamine attached to asparagine and (2) fucosyl residues linked alpha 1----3 to a branch N-acetylglucosamine.
2387072	5	4	theme	alpha	1366:1370	arg1	1----3					1372:1377	alpha 1----3	1366:1377	alpha 1----3	1366:1377	Glycopeptides derived from a glycoprotein, fibronectin, secreted from CF fibroblasts were also examined by 1H-NMR spectroscopy and showed no evidence of fucosyl residues linked alpha 1----3 to branch N-acetylglucosamine and a lesser percentage of core fucose than found in the peripheral membrane glycopeptides.
2387072	2	5	dep	digested	603:610	arg1	purified					623:630	purified	623:630	purified	623:630	To further define these results, the membrane glycopeptides which bound to immobilized lentil lectin and thereby enriched in fucosyl residues linked alpha 1----6 to N-acetylglucosamine attached to asparagine, were Pronase digested, partially purified and examined by 500-MHz 1H-NMR spectroscopy.
2387072	2	6	attach	linked	523:528	arg1	N-acetylglucosamine					546:564	N-acetylglucosamine	546:564	N-acetylglucosamine attached to asparagine	546:587	To further define these results, the membrane glycopeptides which bound to immobilized lentil lectin and thereby enriched in fucosyl residues linked alpha 1----6 to N-acetylglucosamine attached to asparagine, were Pronase digested, partially purified and examined by 500-MHz 1H-NMR spectroscopy.
2387072	2	6	attach	linked	523:528	arg2	residues					514:521	fucosyl residues	506:521	fucosyl residues linked alpha 1----6 to N-acetylglucosamine attached to asparagine	506:587	To further define these results, the membrane glycopeptides which bound to immobilized lentil lectin and thereby enriched in fucosyl residues linked alpha 1----6 to N-acetylglucosamine attached to asparagine, were Pronase digested, partially purified and examined by 500-MHz 1H-NMR spectroscopy.
2387072	1	7	theme	patients	210:217	arg1	fibroblasts					189:199	skin fibroblasts	184:199	skin fibroblasts of seven patients with cystic fibrosis (CF)	184:243	Glycopeptides derived from peripheral membrane glycoproteins of skin fibroblasts of seven patients with cystic fibrosis (CF) had an increase in fucosyl residues when compared with those of seven age, race and sex matched controls (Pediatr Res 1985;19:368-374).
2387072	2	8	theme	alpha	530:534	arg1	1----6					536:541	alpha 1----6	530:541	alpha 1----6	530:541	To further define these results, the membrane glycopeptides which bound to immobilized lentil lectin and thereby enriched in fucosyl residues linked alpha 1----6 to N-acetylglucosamine attached to asparagine, were Pronase digested, partially purified and examined by 500-MHz 1H-NMR spectroscopy.
2387072	1	9	theme	cystic	224:229	arg1	CF					241:242	CF	241:242	CF	241:242	Glycopeptides derived from peripheral membrane glycoproteins of skin fibroblasts of seven patients with cystic fibrosis (CF) had an increase in fucosyl residues when compared with those of seven age, race and sex matched controls (Pediatr Res 1985;19:368-374).
2387072	1	9	theme	cystic	224:229	arg1	fibrosis					231:238	cystic fibrosis	224:238	cystic fibrosis (CF)	224:243	Glycopeptides derived from peripheral membrane glycoproteins of skin fibroblasts of seven patients with cystic fibrosis (CF) had an increase in fucosyl residues when compared with those of seven age, race and sex matched controls (Pediatr Res 1985;19:368-374).
2387072	1	10	contain	had	245:247	arg1	Glycopeptides					120:132	Glycopeptides	120:132	Glycopeptides derived from peripheral membrane glycoproteins of skin fibroblasts of seven patients with cystic fibrosis (CF)	120:243	Glycopeptides derived from peripheral membrane glycoproteins of skin fibroblasts of seven patients with cystic fibrosis (CF) had an increase in fucosyl residues when compared with those of seven age, race and sex matched controls (Pediatr Res 1985;19:368-374).
2387072	1	10	contain	had	245:247	arg2	increase					252:259	an increase	249:259	an increase in fucosyl residues	249:279	Glycopeptides derived from peripheral membrane glycoproteins of skin fibroblasts of seven patients with cystic fibrosis (CF) had an increase in fucosyl residues when compared with those of seven age, race and sex matched controls (Pediatr Res 1985;19:368-374).
2387072	6	11	theme	membrane	1576:1583	arg1	glycoproteins					1585:1597	the CF peripheral membrane glycoproteins	1558:1597	the CF peripheral membrane glycoproteins	1558:1597	These results define further the altered fucosylation of the CF peripheral membrane glycoproteins.
2387072	5	12	attach	derived	1203:1209	arg1	glycoprotein					1218:1229	a glycoprotein	1216:1229	a glycoprotein	1216:1229	Glycopeptides derived from a glycoprotein, fibronectin, secreted from CF fibroblasts were also examined by 1H-NMR spectroscopy and showed no evidence of fucosyl residues linked alpha 1----3 to branch N-acetylglucosamine and a lesser percentage of core fucose than found in the peripheral membrane glycopeptides.
2387072	5	12	attach	derived	1203:1209	arg2	Glycopeptides					1189:1201	Glycopeptides	1189:1201	Glycopeptides derived from a glycoprotein, fibronectin, secreted from CF fibroblasts	1189:1272	Glycopeptides derived from a glycoprotein, fibronectin, secreted from CF fibroblasts were also examined by 1H-NMR spectroscopy and showed no evidence of fucosyl residues linked alpha 1----3 to branch N-acetylglucosamine and a lesser percentage of core fucose than found in the peripheral membrane glycopeptides.
2387072	5	12	attach	derived	1203:1209	arg1	fibronectin					1232:1242	fibronectin	1232:1242	fibronectin	1232:1242	Glycopeptides derived from a glycoprotein, fibronectin, secreted from CF fibroblasts were also examined by 1H-NMR spectroscopy and showed no evidence of fucosyl residues linked alpha 1----3 to branch N-acetylglucosamine and a lesser percentage of core fucose than found in the peripheral membrane glycopeptides.
2387072	6	13	theme	CF	1562:1563	arg1	glycoproteins					1585:1597	the CF peripheral membrane glycoproteins	1558:1597	the CF peripheral membrane glycoproteins	1558:1597	These results define further the altered fucosylation of the CF peripheral membrane glycoproteins.
2387072	0	14	from	fibroblasts	107:117	arg1	glycoprotein					73:84	a secreted glycoprotein	62:84	membrane glycoproteins but not a secreted glycoprotein from cystic fibrosis fibroblasts	31:117	Additional fucosyl residues on membrane glycoproteins but not a secreted glycoprotein from cystic fibrosis fibroblasts.
2387072	3	15	theme	increased	777:785	arg1	number					787:792	an increased number	774:792	an increased number of fucosyl residues	774:812	The CF derived glycopeptides had two different features when compared to those from Controls (1) an increased number of fucosyl residues linked alpha 1----6 to the N-acetylglucosamine attached to asparagine and (2) fucosyl residues linked alpha 1----3 to a branch N-acetylglucosamine.
2387072	1	16	theme	peripheral	147:156	arg1	glycoproteins					167:179	peripheral membrane glycoproteins	147:179	peripheral membrane glycoproteins of skin fibroblasts of seven patients with cystic fibrosis (CF)	147:243	Glycopeptides derived from peripheral membrane glycoproteins of skin fibroblasts of seven patients with cystic fibrosis (CF) had an increase in fucosyl residues when compared with those of seven age, race and sex matched controls (Pediatr Res 1985;19:368-374).
2387072	3	17	theme	alpha	821:825	arg1	1----6					827:832	alpha 1----6	821:832	alpha 1----6	821:832	The CF derived glycopeptides had two different features when compared to those from Controls (1) an increased number of fucosyl residues linked alpha 1----6 to the N-acetylglucosamine attached to asparagine and (2) fucosyl residues linked alpha 1----3 to a branch N-acetylglucosamine.
2387072	4	18	theme	molar	1126:1130	arg1	ratio					1132:1136	an approximate molar ratio	1111:1136	an approximate molar ratio of 3:2 and 2:1	1111:1151	The glycopeptides from both sources were of the di and triantennary type containing sialic acid linked alpha 2----3 and alpha 2----6 to galactose in an approximate molar ratio of 3:2 and 2:1, from CF and Control, respectively.
2387072	3	19	dep	linked	909:914	arg1	2					889:889	2	889:889	2	889:889	The CF derived glycopeptides had two different features when compared to those from Controls (1) an increased number of fucosyl residues linked alpha 1----6 to the N-acetylglucosamine attached to asparagine and (2) fucosyl residues linked alpha 1----3 to a branch N-acetylglucosamine.
2387072	2	20	theme	immobilized	456:466	arg1	lectin					475:480	immobilized lentil lectin	456:480	immobilized lentil lectin	456:480	To further define these results, the membrane glycopeptides which bound to immobilized lentil lectin and thereby enriched in fucosyl residues linked alpha 1----6 to N-acetylglucosamine attached to asparagine, were Pronase digested, partially purified and examined by 500-MHz 1H-NMR spectroscopy.
2387072	0	21	from	residues	19:26	arg1	glycoprotein					73:84	a secreted glycoprotein	62:84	membrane glycoproteins but not a secreted glycoprotein from cystic fibrosis fibroblasts	31:117	Additional fucosyl residues on membrane glycoproteins but not a secreted glycoprotein from cystic fibrosis fibroblasts.
2387072	0	21	from	residues	19:26	arg1	glycoproteins					40:52	membrane glycoproteins	31:52	membrane glycoproteins but not a secreted glycoprotein from cystic fibrosis fibroblasts	31:117	Additional fucosyl residues on membrane glycoproteins but not a secreted glycoprotein from cystic fibrosis fibroblasts.
2387072	3	22	theme	residues	805:812	arg1	number					787:792	an increased number	774:792	an increased number of fucosyl residues	774:812	The CF derived glycopeptides had two different features when compared to those from Controls (1) an increased number of fucosyl residues linked alpha 1----6 to the N-acetylglucosamine attached to asparagine and (2) fucosyl residues linked alpha 1----3 to a branch N-acetylglucosamine.
2387072	4	23	attach	linked	1058:1063	arg2	acid					1053:1056	sialic acid	1046:1056	sialic acid linked alpha 2----3 and alpha 2----6 to galactose in an approximate molar ratio of 3:2 and 2:1	1046:1151	The glycopeptides from both sources were of the di and triantennary type containing sialic acid linked alpha 2----3 and alpha 2----6 to galactose in an approximate molar ratio of 3:2 and 2:1, from CF and Control, respectively.
2387072	4	23	attach	linked	1058:1063	arg1	galactose					1098:1106	galactose	1098:1106	galactose in an approximate molar ratio of 3:2 and 2:1	1098:1151	The glycopeptides from both sources were of the di and triantennary type containing sialic acid linked alpha 2----3 and alpha 2----6 to galactose in an approximate molar ratio of 3:2 and 2:1, from CF and Control, respectively.
2387072	1	24	theme	skin	184:187	arg1	fibroblasts					189:199	skin fibroblasts	184:199	skin fibroblasts of seven patients with cystic fibrosis (CF)	184:243	Glycopeptides derived from peripheral membrane glycoproteins of skin fibroblasts of seven patients with cystic fibrosis (CF) had an increase in fucosyl residues when compared with those of seven age, race and sex matched controls (Pediatr Res 1985;19:368-374).
2387072	1	25	dep	compared	286:293	arg1	Res					359:361	Res	359:361	Res	359:361	Glycopeptides derived from peripheral membrane glycoproteins of skin fibroblasts of seven patients with cystic fibrosis (CF) had an increase in fucosyl residues when compared with those of seven age, race and sex matched controls (Pediatr Res 1985;19:368-374).
2387072	0	26	theme	cystic	91:96	arg1	fibrosis					98:105	cystic fibrosis	91:105	cystic fibrosis fibroblasts	91:117	Additional fucosyl residues on membrane glycoproteins but not a secreted glycoprotein from cystic fibrosis fibroblasts.
2387072	4	27	gly	glycopeptides	966:978	arg2	glycopeptides					966:978	The glycopeptides	962:978	The glycopeptides from both sources	962:996	The glycopeptides from both sources were of the di and triantennary type containing sialic acid linked alpha 2----3 and alpha 2----6 to galactose in an approximate molar ratio of 3:2 and 2:1, from CF and Control, respectively.
2387072	4	27	gly	glycopeptides	966:978	arg1	sources					990:996	both sources	985:996	both sources	985:996	The glycopeptides from both sources were of the di and triantennary type containing sialic acid linked alpha 2----3 and alpha 2----6 to galactose in an approximate molar ratio of 3:2 and 2:1, from CF and Control, respectively.
2387072	5	28	theme	core	1436:1439	arg1	fucose					1441:1446	core fucose	1436:1446	core fucose	1436:1446	Glycopeptides derived from a glycoprotein, fibronectin, secreted from CF fibroblasts were also examined by 1H-NMR spectroscopy and showed no evidence of fucosyl residues linked alpha 1----3 to branch N-acetylglucosamine and a lesser percentage of core fucose than found in the peripheral membrane glycopeptides.
2387072	0	29	theme	Additional	0:9	arg1	residues					19:26	Additional fucosyl residues	0:26	Additional fucosyl residues on membrane glycoproteins but not a secreted glycoprotein from cystic fibrosis fibroblasts	0:117	Additional fucosyl residues on membrane glycoproteins but not a secreted glycoprotein from cystic fibrosis fibroblasts.
2387072	4	30	from	Control	1166:1172	arg1	type					1030:1033	the di and triantennary type	1006:1033	the di and triantennary type containing sialic acid linked alpha 2----3 and alpha 2----6 to galactose in an approximate molar ratio of 3:2 and 2:1	1006:1151	The glycopeptides from both sources were of the di and triantennary type containing sialic acid linked alpha 2----3 and alpha 2----6 to galactose in an approximate molar ratio of 3:2 and 2:1, from CF and Control, respectively.
2387072	2	31	theme	500-MHz	648:654	arg1	spectroscopy					663:674	500-MHz 1H-NMR spectroscopy	648:674	500-MHz 1H-NMR spectroscopy	648:674	To further define these results, the membrane glycopeptides which bound to immobilized lentil lectin and thereby enriched in fucosyl residues linked alpha 1----6 to N-acetylglucosamine attached to asparagine, were Pronase digested, partially purified and examined by 500-MHz 1H-NMR spectroscopy.
2387072	3	32	dep	derived	684:690	arg1	CF					681:682	CF	681:682	CF	681:682	The CF derived glycopeptides had two different features when compared to those from Controls (1) an increased number of fucosyl residues linked alpha 1----6 to the N-acetylglucosamine attached to asparagine and (2) fucosyl residues linked alpha 1----3 to a branch N-acetylglucosamine.
2387072	4	33	from	CF	1159:1160	arg1	type					1030:1033	the di and triantennary type	1006:1033	the di and triantennary type containing sialic acid linked alpha 2----3 and alpha 2----6 to galactose in an approximate molar ratio of 3:2 and 2:1	1006:1151	The glycopeptides from both sources were of the di and triantennary type containing sialic acid linked alpha 2----3 and alpha 2----6 to galactose in an approximate molar ratio of 3:2 and 2:1, from CF and Control, respectively.
2387072	3	34	theme	fucosyl	892:898	arg1	residues					900:907	fucosyl residues	892:907	fucosyl residues	892:907	The CF derived glycopeptides had two different features when compared to those from Controls (1) an increased number of fucosyl residues linked alpha 1----6 to the N-acetylglucosamine attached to asparagine and (2) fucosyl residues linked alpha 1----3 to a branch N-acetylglucosamine.
2387072	0	35	theme	membrane	31:38	arg1	glycoproteins					40:52	membrane glycoproteins	31:52	membrane glycoproteins but not a secreted glycoprotein from cystic fibrosis fibroblasts	31:117	Additional fucosyl residues on membrane glycoproteins but not a secreted glycoprotein from cystic fibrosis fibroblasts.
2387072	5	36	theme	peripheral	1466:1475	arg1	glycopeptides					1486:1498	the peripheral membrane glycopeptides	1462:1498	the peripheral membrane glycopeptides	1462:1498	Glycopeptides derived from a glycoprotein, fibronectin, secreted from CF fibroblasts were also examined by 1H-NMR spectroscopy and showed no evidence of fucosyl residues linked alpha 1----3 to branch N-acetylglucosamine and a lesser percentage of core fucose than found in the peripheral membrane glycopeptides.
2387072	5	37	theme	fucosyl	1342:1348	arg1	residues					1350:1357	fucosyl residues	1342:1357	fucosyl residues linked alpha 1----3 to branch N-acetylglucosamine and a lesser percentage of core fucose	1342:1446	Glycopeptides derived from a glycoprotein, fibronectin, secreted from CF fibroblasts were also examined by 1H-NMR spectroscopy and showed no evidence of fucosyl residues linked alpha 1----3 to branch N-acetylglucosamine and a lesser percentage of core fucose than found in the peripheral membrane glycopeptides.
2387072	6	38	gly	glycoproteins	1585:1597	arg1	glycoproteins					1585:1597	the CF peripheral membrane glycoproteins	1558:1597	the CF peripheral membrane glycoproteins	1558:1597	These results define further the altered fucosylation of the CF peripheral membrane glycoproteins.
2387072	1	39	with	patients	210:217	arg1	CF					241:242	CF	241:242	CF	241:242	Glycopeptides derived from peripheral membrane glycoproteins of skin fibroblasts of seven patients with cystic fibrosis (CF) had an increase in fucosyl residues when compared with those of seven age, race and sex matched controls (Pediatr Res 1985;19:368-374).
2387072	1	39	with	patients	210:217	arg1	fibrosis					231:238	cystic fibrosis	224:238	cystic fibrosis (CF)	224:243	Glycopeptides derived from peripheral membrane glycoproteins of skin fibroblasts of seven patients with cystic fibrosis (CF) had an increase in fucosyl residues when compared with those of seven age, race and sex matched controls (Pediatr Res 1985;19:368-374).
2387072	2	40	gly	glycopeptides	427:439	arg2	glycopeptides					427:439	the membrane glycopeptides	414:439	the membrane glycopeptides	414:439	To further define these results, the membrane glycopeptides which bound to immobilized lentil lectin and thereby enriched in fucosyl residues linked alpha 1----6 to N-acetylglucosamine attached to asparagine, were Pronase digested, partially purified and examined by 500-MHz 1H-NMR spectroscopy.
2387072	6	41	theme	altered	1534:1540	arg1	fucosylation					1542:1553	the altered fucosylation	1530:1553	the altered fucosylation of the CF peripheral membrane glycoproteins	1530:1597	These results define further the altered fucosylation of the CF peripheral membrane glycoproteins.
2387072	6	42	gly	fucosylation	1542:1553	arg1	glycoproteins					1585:1597	the CF peripheral membrane glycoproteins	1558:1597	the CF peripheral membrane glycoproteins	1558:1597	These results define further the altered fucosylation of the CF peripheral membrane glycoproteins.
2387072	0	43	gly	glycoproteins	40:52	arg1	glycoproteins					40:52	membrane glycoproteins	31:52	membrane glycoproteins but not a secreted glycoprotein from cystic fibrosis fibroblasts	31:117	Additional fucosyl residues on membrane glycoproteins but not a secreted glycoprotein from cystic fibrosis fibroblasts.
2387072	5	44	gly	glycoprotein	1218:1229	arg1	glycoprotein					1218:1229	a glycoprotein	1216:1229	a glycoprotein	1216:1229	Glycopeptides derived from a glycoprotein, fibronectin, secreted from CF fibroblasts were also examined by 1H-NMR spectroscopy and showed no evidence of fucosyl residues linked alpha 1----3 to branch N-acetylglucosamine and a lesser percentage of core fucose than found in the peripheral membrane glycopeptides.
2387072	5	44	gly	glycoprotein	1218:1229	arg1	fibronectin					1232:1242	fibronectin	1232:1242	fibronectin	1232:1242	Glycopeptides derived from a glycoprotein, fibronectin, secreted from CF fibroblasts were also examined by 1H-NMR spectroscopy and showed no evidence of fucosyl residues linked alpha 1----3 to branch N-acetylglucosamine and a lesser percentage of core fucose than found in the peripheral membrane glycopeptides.
2387072	4	45	theme	sialic	1046:1051	arg1	acid					1053:1056	sialic acid	1046:1056	sialic acid linked alpha 2----3 and alpha 2----6 to galactose in an approximate molar ratio of 3:2 and 2:1	1046:1151	The glycopeptides from both sources were of the di and triantennary type containing sialic acid linked alpha 2----3 and alpha 2----6 to galactose in an approximate molar ratio of 3:2 and 2:1, from CF and Control, respectively.
2387072	4	46	contain	containing	1035:1044	arg1	type					1030:1033	the di and triantennary type	1006:1033	the di and triantennary type containing sialic acid linked alpha 2----3 and alpha 2----6 to galactose in an approximate molar ratio of 3:2 and 2:1	1006:1151	The glycopeptides from both sources were of the di and triantennary type containing sialic acid linked alpha 2----3 and alpha 2----6 to galactose in an approximate molar ratio of 3:2 and 2:1, from CF and Control, respectively.
2387072	4	46	contain	containing	1035:1044	arg2	acid					1053:1056	sialic acid	1046:1056	sialic acid linked alpha 2----3 and alpha 2----6 to galactose in an approximate molar ratio of 3:2 and 2:1	1046:1151	The glycopeptides from both sources were of the di and triantennary type containing sialic acid linked alpha 2----3 and alpha 2----6 to galactose in an approximate molar ratio of 3:2 and 2:1, from CF and Control, respectively.
2387072	1	47	theme	fucosyl	264:270	arg1	residues					272:279	fucosyl residues	264:279	fucosyl residues	264:279	Glycopeptides derived from peripheral membrane glycoproteins of skin fibroblasts of seven patients with cystic fibrosis (CF) had an increase in fucosyl residues when compared with those of seven age, race and sex matched controls (Pediatr Res 1985;19:368-374).
2387072	5	48	theme	lesser	1415:1420	arg1	percentage					1422:1431	a lesser percentage	1413:1431	a lesser percentage of core fucose	1413:1446	Glycopeptides derived from a glycoprotein, fibronectin, secreted from CF fibroblasts were also examined by 1H-NMR spectroscopy and showed no evidence of fucosyl residues linked alpha 1----3 to branch N-acetylglucosamine and a lesser percentage of core fucose than found in the peripheral membrane glycopeptides.
2387072	2	49	attach	attached	566:573	arg2	N-acetylglucosamine					546:564	N-acetylglucosamine	546:564	N-acetylglucosamine attached to asparagine	546:587	To further define these results, the membrane glycopeptides which bound to immobilized lentil lectin and thereby enriched in fucosyl residues linked alpha 1----6 to N-acetylglucosamine attached to asparagine, were Pronase digested, partially purified and examined by 500-MHz 1H-NMR spectroscopy.
2387072	2	49	attach	attached	566:573	arg1	asparagine					578:587	asparagine	578:587	asparagine	578:587	To further define these results, the membrane glycopeptides which bound to immobilized lentil lectin and thereby enriched in fucosyl residues linked alpha 1----6 to N-acetylglucosamine attached to asparagine, were Pronase digested, partially purified and examined by 500-MHz 1H-NMR spectroscopy.
2387072	1	50	theme	fibroblasts	189:199	arg1	glycoproteins					167:179	peripheral membrane glycoproteins	147:179	peripheral membrane glycoproteins of skin fibroblasts of seven patients with cystic fibrosis (CF)	147:243	Glycopeptides derived from peripheral membrane glycoproteins of skin fibroblasts of seven patients with cystic fibrosis (CF) had an increase in fucosyl residues when compared with those of seven age, race and sex matched controls (Pediatr Res 1985;19:368-374).
2387072	4	51	theme	approximate	1114:1124	arg1	ratio					1132:1136	an approximate molar ratio	1111:1136	an approximate molar ratio of 3:2 and 2:1	1111:1151	The glycopeptides from both sources were of the di and triantennary type containing sialic acid linked alpha 2----3 and alpha 2----6 to galactose in an approximate molar ratio of 3:2 and 2:1, from CF and Control, respectively.
2387072	4	52	theme	alpha	1082:1086	arg1	2----6					1088:1093	alpha 2----6	1082:1093	alpha 2----6	1082:1093	The glycopeptides from both sources were of the di and triantennary type containing sialic acid linked alpha 2----3 and alpha 2----6 to galactose in an approximate molar ratio of 3:2 and 2:1, from CF and Control, respectively.
2387072	5	53	theme	branch	1382:1387	arg1	N-acetylglucosamine					1389:1407	branch N-acetylglucosamine	1382:1407	branch N-acetylglucosamine	1382:1407	Glycopeptides derived from a glycoprotein, fibronectin, secreted from CF fibroblasts were also examined by 1H-NMR spectroscopy and showed no evidence of fucosyl residues linked alpha 1----3 to branch N-acetylglucosamine and a lesser percentage of core fucose than found in the peripheral membrane glycopeptides.
2387072	3	54	link	derived	684:690	arg1	glycopeptides					692:704	The CF derived glycopeptides	677:704	The CF derived glycopeptides	677:704	The CF derived glycopeptides had two different features when compared to those from Controls (1) an increased number of fucosyl residues linked alpha 1----6 to the N-acetylglucosamine attached to asparagine and (2) fucosyl residues linked alpha 1----3 to a branch N-acetylglucosamine.
2387072	1	55	from	increase	252:259	arg1	residues					272:279	fucosyl residues	264:279	fucosyl residues	264:279	Glycopeptides derived from peripheral membrane glycoproteins of skin fibroblasts of seven patients with cystic fibrosis (CF) had an increase in fucosyl residues when compared with those of seven age, race and sex matched controls (Pediatr Res 1985;19:368-374).
2387072	4	56	from	galactose	1098:1106	arg1	ratio					1132:1136	an approximate molar ratio	1111:1136	an approximate molar ratio of 3:2 and 2:1	1111:1151	The glycopeptides from both sources were of the di and triantennary type containing sialic acid linked alpha 2----3 and alpha 2----6 to galactose in an approximate molar ratio of 3:2 and 2:1, from CF and Control, respectively.
2387072	2	57	theme	fucosyl	506:512	arg1	residues					514:521	fucosyl residues	506:521	fucosyl residues linked alpha 1----6 to N-acetylglucosamine attached to asparagine	506:587	To further define these results, the membrane glycopeptides which bound to immobilized lentil lectin and thereby enriched in fucosyl residues linked alpha 1----6 to N-acetylglucosamine attached to asparagine, were Pronase digested, partially purified and examined by 500-MHz 1H-NMR spectroscopy.
2387072	4	58	theme	2:1	1149:1151	arg1	ratio					1132:1136	an approximate molar ratio	1111:1136	an approximate molar ratio of 3:2 and 2:1	1111:1151	The glycopeptides from both sources were of the di and triantennary type containing sialic acid linked alpha 2----3 and alpha 2----6 to galactose in an approximate molar ratio of 3:2 and 2:1, from CF and Control, respectively.
2387072	1	59	gly	glycoproteins	167:179	arg1	glycoproteins					167:179	peripheral membrane glycoproteins	147:179	peripheral membrane glycoproteins of skin fibroblasts of seven patients with cystic fibrosis (CF)	147:243	Glycopeptides derived from peripheral membrane glycoproteins of skin fibroblasts of seven patients with cystic fibrosis (CF) had an increase in fucosyl residues when compared with those of seven age, race and sex matched controls (Pediatr Res 1985;19:368-374).
2387072	3	60	attach	attached	861:868	arg2	N-acetylglucosamine					841:859	the N-acetylglucosamine	837:859	the N-acetylglucosamine attached to asparagine	837:882	The CF derived glycopeptides had two different features when compared to those from Controls (1) an increased number of fucosyl residues linked alpha 1----6 to the N-acetylglucosamine attached to asparagine and (2) fucosyl residues linked alpha 1----3 to a branch N-acetylglucosamine.
2387072	3	60	attach	attached	861:868	arg1	asparagine					873:882	asparagine	873:882	asparagine	873:882	The CF derived glycopeptides had two different features when compared to those from Controls (1) an increased number of fucosyl residues linked alpha 1----6 to the N-acetylglucosamine attached to asparagine and (2) fucosyl residues linked alpha 1----3 to a branch N-acetylglucosamine.
2387072	6	61	theme	peripheral	1565:1574	arg1	glycoproteins					1585:1597	the CF peripheral membrane glycoproteins	1558:1597	the CF peripheral membrane glycoproteins	1558:1597	These results define further the altered fucosylation of the CF peripheral membrane glycoproteins.
2387072	1	62	theme	matched	333:339	arg1	controls					341:348	matched controls	333:348	matched controls	333:348	Glycopeptides derived from peripheral membrane glycoproteins of skin fibroblasts of seven patients with cystic fibrosis (CF) had an increase in fucosyl residues when compared with those of seven age, race and sex matched controls (Pediatr Res 1985;19:368-374).
2387072	3	63	contain	had	706:708	arg2	features					724:731	two different features	710:731	two different features	710:731	The CF derived glycopeptides had two different features when compared to those from Controls (1) an increased number of fucosyl residues linked alpha 1----6 to the N-acetylglucosamine attached to asparagine and (2) fucosyl residues linked alpha 1----3 to a branch N-acetylglucosamine.
2387072	3	63	contain	had	706:708	arg1	glycopeptides					692:704	The CF derived glycopeptides	677:704	The CF derived glycopeptides	677:704	The CF derived glycopeptides had two different features when compared to those from Controls (1) an increased number of fucosyl residues linked alpha 1----6 to the N-acetylglucosamine attached to asparagine and (2) fucosyl residues linked alpha 1----3 to a branch N-acetylglucosamine.
2387072	0	64	theme	secreted	64:71	arg1	glycoprotein					73:84	a secreted glycoprotein	62:84	membrane glycoproteins but not a secreted glycoprotein from cystic fibrosis fibroblasts	31:117	Additional fucosyl residues on membrane glycoproteins but not a secreted glycoprotein from cystic fibrosis fibroblasts.
2387072	3	65	dep	linked	814:819	arg1	1					771:771	1	771:771	1	771:771	The CF derived glycopeptides had two different features when compared to those from Controls (1) an increased number of fucosyl residues linked alpha 1----6 to the N-acetylglucosamine attached to asparagine and (2) fucosyl residues linked alpha 1----3 to a branch N-acetylglucosamine.
2387072	1	66	theme	membrane	158:165	arg1	glycoproteins					167:179	peripheral membrane glycoproteins	147:179	peripheral membrane glycoproteins of skin fibroblasts of seven patients with cystic fibrosis (CF)	147:243	Glycopeptides derived from peripheral membrane glycoproteins of skin fibroblasts of seven patients with cystic fibrosis (CF) had an increase in fucosyl residues when compared with those of seven age, race and sex matched controls (Pediatr Res 1985;19:368-374).
2387072	2	67	theme	lentil	468:473	arg1	lectin					475:480	immobilized lentil lectin	456:480	immobilized lentil lectin	456:480	To further define these results, the membrane glycopeptides which bound to immobilized lentil lectin and thereby enriched in fucosyl residues linked alpha 1----6 to N-acetylglucosamine attached to asparagine, were Pronase digested, partially purified and examined by 500-MHz 1H-NMR spectroscopy.
2387072	4	68	theme	3:2	1141:1143	arg1	ratio					1132:1136	an approximate molar ratio	1111:1136	an approximate molar ratio of 3:2 and 2:1	1111:1151	The glycopeptides from both sources were of the di and triantennary type containing sialic acid linked alpha 2----3 and alpha 2----6 to galactose in an approximate molar ratio of 3:2 and 2:1, from CF and Control, respectively.
2387072	5	69	attach	linked	1359:1364	arg1	percentage					1422:1431	a lesser percentage	1413:1431	a lesser percentage of core fucose	1413:1446	Glycopeptides derived from a glycoprotein, fibronectin, secreted from CF fibroblasts were also examined by 1H-NMR spectroscopy and showed no evidence of fucosyl residues linked alpha 1----3 to branch N-acetylglucosamine and a lesser percentage of core fucose than found in the peripheral membrane glycopeptides.
2387072	5	69	attach	linked	1359:1364	arg2	residues					1350:1357	fucosyl residues	1342:1357	fucosyl residues linked alpha 1----3 to branch N-acetylglucosamine and a lesser percentage of core fucose	1342:1446	Glycopeptides derived from a glycoprotein, fibronectin, secreted from CF fibroblasts were also examined by 1H-NMR spectroscopy and showed no evidence of fucosyl residues linked alpha 1----3 to branch N-acetylglucosamine and a lesser percentage of core fucose than found in the peripheral membrane glycopeptides.
2387072	5	69	attach	linked	1359:1364	arg1	N-acetylglucosamine					1389:1407	branch N-acetylglucosamine	1382:1407	branch N-acetylglucosamine	1382:1407	Glycopeptides derived from a glycoprotein, fibronectin, secreted from CF fibroblasts were also examined by 1H-NMR spectroscopy and showed no evidence of fucosyl residues linked alpha 1----3 to branch N-acetylglucosamine and a lesser percentage of core fucose than found in the peripheral membrane glycopeptides.
2387072	3	70	attach	linked	814:819	arg2	number					787:792	an increased number	774:792	an increased number of fucosyl residues	774:812	The CF derived glycopeptides had two different features when compared to those from Controls (1) an increased number of fucosyl residues linked alpha 1----6 to the N-acetylglucosamine attached to asparagine and (2) fucosyl residues linked alpha 1----3 to a branch N-acetylglucosamine.
2387072	3	70	attach	linked	814:819	arg1	N-acetylglucosamine					841:859	the N-acetylglucosamine	837:859	the N-acetylglucosamine attached to asparagine	837:882	The CF derived glycopeptides had two different features when compared to those from Controls (1) an increased number of fucosyl residues linked alpha 1----6 to the N-acetylglucosamine attached to asparagine and (2) fucosyl residues linked alpha 1----3 to a branch N-acetylglucosamine.
2387072	0	71	theme	fibrosis	98:105	arg1	fibroblasts					107:117	cystic fibrosis fibroblasts	91:117	cystic fibrosis fibroblasts	91:117	Additional fucosyl residues on membrane glycoproteins but not a secreted glycoprotein from cystic fibrosis fibroblasts.
2387072	3	72	dep	those	750:754	arg1	linked					909:914	linked	909:914	linked alpha 1----3 to a branch N-acetylglucosamine	909:959	The CF derived glycopeptides had two different features when compared to those from Controls (1) an increased number of fucosyl residues linked alpha 1----6 to the N-acetylglucosamine attached to asparagine and (2) fucosyl residues linked alpha 1----3 to a branch N-acetylglucosamine.
2387072	3	72	dep	those	750:754	arg1	linked					814:819	linked	814:819	linked alpha 1----6 to the N-acetylglucosamine attached to asparagine	814:882	The CF derived glycopeptides had two different features when compared to those from Controls (1) an increased number of fucosyl residues linked alpha 1----6 to the N-acetylglucosamine attached to asparagine and (2) fucosyl residues linked alpha 1----3 to a branch N-acetylglucosamine.
2387072	1	73	dep	age	315:317	arg1	controls					341:348	matched controls	333:348	matched controls	333:348	Glycopeptides derived from peripheral membrane glycoproteins of skin fibroblasts of seven patients with cystic fibrosis (CF) had an increase in fucosyl residues when compared with those of seven age, race and sex matched controls (Pediatr Res 1985;19:368-374).
2387072	3	74	theme	fucosyl	797:803	arg1	residues					805:812	fucosyl residues	797:812	fucosyl residues	797:812	The CF derived glycopeptides had two different features when compared to those from Controls (1) an increased number of fucosyl residues linked alpha 1----6 to the N-acetylglucosamine attached to asparagine and (2) fucosyl residues linked alpha 1----3 to a branch N-acetylglucosamine.
2387072	0	75	gly	glycoprotein	73:84	arg1	glycoprotein					73:84	a secreted glycoprotein	62:84	membrane glycoproteins but not a secreted glycoprotein from cystic fibrosis fibroblasts	31:117	Additional fucosyl residues on membrane glycoproteins but not a secreted glycoprotein from cystic fibrosis fibroblasts.
2387072	5	76	theme	1H-NMR	1296:1301	arg1	spectroscopy					1303:1314	1H-NMR spectroscopy	1296:1314	1H-NMR spectroscopy	1296:1314	Glycopeptides derived from a glycoprotein, fibronectin, secreted from CF fibroblasts were also examined by 1H-NMR spectroscopy and showed no evidence of fucosyl residues linked alpha 1----3 to branch N-acetylglucosamine and a lesser percentage of core fucose than found in the peripheral membrane glycopeptides.
2387072	0	77	theme	fucosyl	11:17	arg1	residues					19:26	Additional fucosyl residues	0:26	Additional fucosyl residues on membrane glycoproteins but not a secreted glycoprotein from cystic fibrosis fibroblasts	0:117	Additional fucosyl residues on membrane glycoproteins but not a secreted glycoprotein from cystic fibrosis fibroblasts.
2387072	5	78	theme	fucose	1441:1446	arg1	percentage					1422:1431	a lesser percentage	1413:1431	a lesser percentage of core fucose	1413:1446	Glycopeptides derived from a glycoprotein, fibronectin, secreted from CF fibroblasts were also examined by 1H-NMR spectroscopy and showed no evidence of fucosyl residues linked alpha 1----3 to branch N-acetylglucosamine and a lesser percentage of core fucose than found in the peripheral membrane glycopeptides.
2387072	5	78	theme	fucose	1441:1446	arg1	N-acetylglucosamine					1389:1407	branch N-acetylglucosamine	1382:1407	branch N-acetylglucosamine	1382:1407	Glycopeptides derived from a glycoprotein, fibronectin, secreted from CF fibroblasts were also examined by 1H-NMR spectroscopy and showed no evidence of fucosyl residues linked alpha 1----3 to branch N-acetylglucosamine and a lesser percentage of core fucose than found in the peripheral membrane glycopeptides.
2387072	2	79	theme	1H-NMR	656:661	arg1	spectroscopy					663:674	500-MHz 1H-NMR spectroscopy	648:674	500-MHz 1H-NMR spectroscopy	648:674	To further define these results, the membrane glycopeptides which bound to immobilized lentil lectin and thereby enriched in fucosyl residues linked alpha 1----6 to N-acetylglucosamine attached to asparagine, were Pronase digested, partially purified and examined by 500-MHz 1H-NMR spectroscopy.
2387072	5	80	theme	CF	1259:1260	arg1	fibroblasts					1262:1272	CF fibroblasts	1259:1272	CF fibroblasts	1259:1272	Glycopeptides derived from a glycoprotein, fibronectin, secreted from CF fibroblasts were also examined by 1H-NMR spectroscopy and showed no evidence of fucosyl residues linked alpha 1----3 to branch N-acetylglucosamine and a lesser percentage of core fucose than found in the peripheral membrane glycopeptides.
2387072	6	81	theme	glycoproteins	1585:1597	arg1	fucosylation					1542:1553	the altered fucosylation	1530:1553	the altered fucosylation of the CF peripheral membrane glycoproteins	1530:1597	These results define further the altered fucosylation of the CF peripheral membrane glycoproteins.
2387072	1	82	attach	derived	134:140	arg2	Glycopeptides					120:132	Glycopeptides	120:132	Glycopeptides derived from peripheral membrane glycoproteins of skin fibroblasts of seven patients with cystic fibrosis (CF)	120:243	Glycopeptides derived from peripheral membrane glycoproteins of skin fibroblasts of seven patients with cystic fibrosis (CF) had an increase in fucosyl residues when compared with those of seven age, race and sex matched controls (Pediatr Res 1985;19:368-374).
2387072	1	82	attach	derived	134:140	arg1	glycoproteins					167:179	peripheral membrane glycoproteins	147:179	peripheral membrane glycoproteins of skin fibroblasts of seven patients with cystic fibrosis (CF)	147:243	Glycopeptides derived from peripheral membrane glycoproteins of skin fibroblasts of seven patients with cystic fibrosis (CF) had an increase in fucosyl residues when compared with those of seven age, race and sex matched controls (Pediatr Res 1985;19:368-374).
2387072	3	83	theme	alpha	916:920	arg1	1----3					922:927	alpha 1----3	916:927	alpha 1----3	916:927	The CF derived glycopeptides had two different features when compared to those from Controls (1) an increased number of fucosyl residues linked alpha 1----6 to the N-acetylglucosamine attached to asparagine and (2) fucosyl residues linked alpha 1----3 to a branch N-acetylglucosamine.
2387072	4	84	theme	di	1010:1011	arg1	type					1030:1033	the di and triantennary type	1006:1033	the di and triantennary type containing sialic acid linked alpha 2----3 and alpha 2----6 to galactose in an approximate molar ratio of 3:2 and 2:1	1006:1151	The glycopeptides from both sources were of the di and triantennary type containing sialic acid linked alpha 2----3 and alpha 2----6 to galactose in an approximate molar ratio of 3:2 and 2:1, from CF and Control, respectively.
2387072	3	85	gly	glycopeptides	692:704	arg2	glycopeptides					692:704	The CF derived glycopeptides	677:704	The CF derived glycopeptides	677:704	The CF derived glycopeptides had two different features when compared to those from Controls (1) an increased number of fucosyl residues linked alpha 1----6 to the N-acetylglucosamine attached to asparagine and (2) fucosyl residues linked alpha 1----3 to a branch N-acetylglucosamine.
2387072	4	86	from	sources	990:996	arg1	glycopeptides					966:978	The glycopeptides	962:978	The glycopeptides from both sources	962:996	The glycopeptides from both sources were of the di and triantennary type containing sialic acid linked alpha 2----3 and alpha 2----6 to galactose in an approximate molar ratio of 3:2 and 2:1, from CF and Control, respectively.
2387072	3	87	theme	branch	934:939	arg1	N-acetylglucosamine					941:959	a branch N-acetylglucosamine	932:959	a branch N-acetylglucosamine	932:959	The CF derived glycopeptides had two different features when compared to those from Controls (1) an increased number of fucosyl residues linked alpha 1----6 to the N-acetylglucosamine attached to asparagine and (2) fucosyl residues linked alpha 1----3 to a branch N-acetylglucosamine.
2387072	2	88	theme	membrane	418:425	arg1	glycopeptides					427:439	the membrane glycopeptides	414:439	the membrane glycopeptides	414:439	To further define these results, the membrane glycopeptides which bound to immobilized lentil lectin and thereby enriched in fucosyl residues linked alpha 1----6 to N-acetylglucosamine attached to asparagine, were Pronase digested, partially purified and examined by 500-MHz 1H-NMR spectroscopy.
2387072	5	89	theme	membrane	1477:1484	arg1	glycopeptides					1486:1498	the peripheral membrane glycopeptides	1462:1498	the peripheral membrane glycopeptides	1462:1498	Glycopeptides derived from a glycoprotein, fibronectin, secreted from CF fibroblasts were also examined by 1H-NMR spectroscopy and showed no evidence of fucosyl residues linked alpha 1----3 to branch N-acetylglucosamine and a lesser percentage of core fucose than found in the peripheral membrane glycopeptides.
2387072	5	90	theme	residues	1350:1357	arg1	evidence					1330:1337	no evidence	1327:1337	no evidence of fucosyl residues linked alpha 1----3 to branch N-acetylglucosamine and a lesser percentage of core fucose	1327:1446	Glycopeptides derived from a glycoprotein, fibronectin, secreted from CF fibroblasts were also examined by 1H-NMR spectroscopy and showed no evidence of fucosyl residues linked alpha 1----3 to branch N-acetylglucosamine and a lesser percentage of core fucose than found in the peripheral membrane glycopeptides.
2387072	4	91	theme	alpha	1065:1069	arg1	2----3					1071:1076	alpha 2----3	1065:1076	alpha 2----3	1065:1076	The glycopeptides from both sources were of the di and triantennary type containing sialic acid linked alpha 2----3 and alpha 2----6 to galactose in an approximate molar ratio of 3:2 and 2:1, from CF and Control, respectively.
2387072	3	92	theme	derived	684:690	arg1	glycopeptides					692:704	The CF derived glycopeptides	677:704	The CF derived glycopeptides	677:704	The CF derived glycopeptides had two different features when compared to those from Controls (1) an increased number of fucosyl residues linked alpha 1----6 to the N-acetylglucosamine attached to asparagine and (2) fucosyl residues linked alpha 1----3 to a branch N-acetylglucosamine.
7511099	3	0	theme	antenna	1225:1231	arg1	galactose					1202:1210	the galactose	1198:1210	the galactose of the other antenna	1198:1231	Desialylated AFP with the terminal galactose of the Man alpha 1-->6 antenna with or without the galactose of the other arm also had a migration of AFP-P4, and other hydrolytic intermediates without the terminal galactose of the Man alpha 1-->6 arm with and without the galactose of the other antenna had mobilities of AFP-P3s and AFP-P3, respectively.
7511099	2	1	theme	1-->6	681:685	arg1	arm					687:689	the Mannose (Man) alpha 1-->6 arm	657:689	the Mannose (Man) alpha 1-->6 arm	657:689	By means of neuraminidase and/or beta-galactosidase treatment, AFP-P2 was identified as alpha 2-->6 disialo-AFP, AFP-P3 as having biantennary structures with alpha 2-->6 monosialylated galactose of the Mannose (Man) alpha 1-->6 arm, AFP-P4 as having alpha 2-->6 monosialylated galactose of the Man alpha 1-->3 arm, and AFP-P5 as disialo-AFP with alpha 2-->3 sialylated galactose of the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna.
7511099	2	1	theme	1-->6	681:685	arg1	AFP-P4					692:697	AFP-P4	692:697	AFP-P4	692:697	By means of neuraminidase and/or beta-galactosidase treatment, AFP-P2 was identified as alpha 2-->6 disialo-AFP, AFP-P3 as having biantennary structures with alpha 2-->6 monosialylated galactose of the Mannose (Man) alpha 1-->6 arm, AFP-P4 as having alpha 2-->6 monosialylated galactose of the Man alpha 1-->3 arm, and AFP-P5 as disialo-AFP with alpha 2-->3 sialylated galactose of the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna.
7511099	2	2	theme	2-->6	884:888	arg1	galactose					901:909	the alpha 2-->6 sialylated galactose	874:909	the alpha 2-->6 sialylated galactose of the other antenna	874:930	By means of neuraminidase and/or beta-galactosidase treatment, AFP-P2 was identified as alpha 2-->6 disialo-AFP, AFP-P3 as having biantennary structures with alpha 2-->6 monosialylated galactose of the Mannose (Man) alpha 1-->6 arm, AFP-P4 as having alpha 2-->6 monosialylated galactose of the Man alpha 1-->3 arm, and AFP-P5 as disialo-AFP with alpha 2-->3 sialylated galactose of the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna.
7511099	4	3	theme	electrophoreses	1345:1359	arg1	system					1303:1308	the present system	1291:1308	the present system of two-dimensional lectin affinity electrophoreses	1291:1359	Thus, the present system of two-dimensional lectin affinity electrophoreses would provide a model for the determination of the sugar chain structure of glycoproteins.
7511099	2	4	gly	monosialylated	721:734	arg1	galactose					736:744	alpha 2-->6 monosialylated galactose	709:744	alpha 2-->6 monosialylated galactose of the Man alpha 1-->3 arm	709:771	By means of neuraminidase and/or beta-galactosidase treatment, AFP-P2 was identified as alpha 2-->6 disialo-AFP, AFP-P3 as having biantennary structures with alpha 2-->6 monosialylated galactose of the Mannose (Man) alpha 1-->6 arm, AFP-P4 as having alpha 2-->6 monosialylated galactose of the Man alpha 1-->3 arm, and AFP-P5 as disialo-AFP with alpha 2-->3 sialylated galactose of the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna.
7511099	2	5	theme	alpha	709:713	arg1	galactose					736:744	alpha 2-->6 monosialylated galactose	709:744	alpha 2-->6 monosialylated galactose of the Man alpha 1-->3 arm	709:771	By means of neuraminidase and/or beta-galactosidase treatment, AFP-P2 was identified as alpha 2-->6 disialo-AFP, AFP-P3 as having biantennary structures with alpha 2-->6 monosialylated galactose of the Mannose (Man) alpha 1-->6 arm, AFP-P4 as having alpha 2-->6 monosialylated galactose of the Man alpha 1-->3 arm, and AFP-P5 as disialo-AFP with alpha 2-->3 sialylated galactose of the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna.
7511099	1	6	theme	cord	219:222	arg1	blood					224:228	cord blood	219:228	cord blood	219:228	Erythroagglutinating phytohemagglutinin (E-PHA)-dependent isoforms of human alpha-fetoprotein (AFP) from cord blood were analyzed for their carbohydrate structures by two-dimensional electrophoresis with E-PHA combined with extended agarose gel electrophoresis or with affinity electrophoresis with concanavalin A or Allomyrina dichtoma lectin.
7511099	3	7	theme	AFP-P3s	1251:1257	arg1	mobilities					1237:1246	mobilities	1237:1246	mobilities of AFP-P3s and AFP-P3	1237:1268	Desialylated AFP with the terminal galactose of the Man alpha 1-->6 antenna with or without the galactose of the other arm also had a migration of AFP-P4, and other hydrolytic intermediates without the terminal galactose of the Man alpha 1-->6 arm with and without the galactose of the other antenna had mobilities of AFP-P3s and AFP-P3, respectively.
7511099	2	8	theme	2-->3	811:815	arg1	galactose					828:836	alpha 2-->3 sialylated galactose	805:836	alpha 2-->3 sialylated galactose of the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna	805:930	By means of neuraminidase and/or beta-galactosidase treatment, AFP-P2 was identified as alpha 2-->6 disialo-AFP, AFP-P3 as having biantennary structures with alpha 2-->6 monosialylated galactose of the Mannose (Man) alpha 1-->6 arm, AFP-P4 as having alpha 2-->6 monosialylated galactose of the Man alpha 1-->3 arm, and AFP-P5 as disialo-AFP with alpha 2-->3 sialylated galactose of the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna.
7511099	4	9	theme	structure	1424:1432	arg1	determination					1391:1403	the determination	1387:1403	the determination of the sugar chain structure of glycoproteins	1387:1449	Thus, the present system of two-dimensional lectin affinity electrophoreses would provide a model for the determination of the sugar chain structure of glycoproteins.
7511099	2	10	theme	alpha	849:853	arg1	antenna					861:867	the Man alpha 1-->6 antenna	841:867	the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna	841:930	By means of neuraminidase and/or beta-galactosidase treatment, AFP-P2 was identified as alpha 2-->6 disialo-AFP, AFP-P3 as having biantennary structures with alpha 2-->6 monosialylated galactose of the Mannose (Man) alpha 1-->6 arm, AFP-P4 as having alpha 2-->6 monosialylated galactose of the Man alpha 1-->3 arm, and AFP-P5 as disialo-AFP with alpha 2-->3 sialylated galactose of the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna.
7511099	4	11	theme	glycoproteins	1437:1449	arg1	structure					1424:1432	the sugar chain structure	1408:1432	the sugar chain structure of glycoproteins	1408:1449	Thus, the present system of two-dimensional lectin affinity electrophoreses would provide a model for the determination of the sugar chain structure of glycoproteins.
7511099	2	12	with	antenna	861:867	arg1	galactose					901:909	the alpha 2-->6 sialylated galactose	874:909	the alpha 2-->6 sialylated galactose of the other antenna	874:930	By means of neuraminidase and/or beta-galactosidase treatment, AFP-P2 was identified as alpha 2-->6 disialo-AFP, AFP-P3 as having biantennary structures with alpha 2-->6 monosialylated galactose of the Mannose (Man) alpha 1-->6 arm, AFP-P4 as having alpha 2-->6 monosialylated galactose of the Man alpha 1-->3 arm, and AFP-P5 as disialo-AFP with alpha 2-->3 sialylated galactose of the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna.
7511099	1	13	theme	carbohydrate	254:265	arg1	structures					267:276	their carbohydrate structures	248:276	their carbohydrate structures	248:276	Erythroagglutinating phytohemagglutinin (E-PHA)-dependent isoforms of human alpha-fetoprotein (AFP) from cord blood were analyzed for their carbohydrate structures by two-dimensional electrophoresis with E-PHA combined with extended agarose gel electrophoresis or with affinity electrophoresis with concanavalin A or Allomyrina dichtoma lectin.
7511099	3	14	theme	AFP-P3	1263:1268	arg1	mobilities					1237:1246	mobilities	1237:1246	mobilities of AFP-P3s and AFP-P3	1237:1268	Desialylated AFP with the terminal galactose of the Man alpha 1-->6 antenna with or without the galactose of the other arm also had a migration of AFP-P4, and other hydrolytic intermediates without the terminal galactose of the Man alpha 1-->6 arm with and without the galactose of the other antenna had mobilities of AFP-P3s and AFP-P3, respectively.
7511099	4	15	theme	sugar	1412:1416	arg1	structure					1424:1432	the sugar chain structure	1408:1432	the sugar chain structure of glycoproteins	1408:1449	Thus, the present system of two-dimensional lectin affinity electrophoreses would provide a model for the determination of the sugar chain structure of glycoproteins.
7511099	2	16	theme	arm	769:771	arg1	galactose					736:744	alpha 2-->6 monosialylated galactose	709:744	alpha 2-->6 monosialylated galactose of the Man alpha 1-->3 arm	709:771	By means of neuraminidase and/or beta-galactosidase treatment, AFP-P2 was identified as alpha 2-->6 disialo-AFP, AFP-P3 as having biantennary structures with alpha 2-->6 monosialylated galactose of the Mannose (Man) alpha 1-->6 arm, AFP-P4 as having alpha 2-->6 monosialylated galactose of the Man alpha 1-->3 arm, and AFP-P5 as disialo-AFP with alpha 2-->3 sialylated galactose of the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna.
7511099	1	17	from	blood	224:228	arg1	AFP					209:211	AFP	209:211	AFP	209:211	Erythroagglutinating phytohemagglutinin (E-PHA)-dependent isoforms of human alpha-fetoprotein (AFP) from cord blood were analyzed for their carbohydrate structures by two-dimensional electrophoresis with E-PHA combined with extended agarose gel electrophoresis or with affinity electrophoresis with concanavalin A or Allomyrina dichtoma lectin.
7511099	1	17	from	blood	224:228	arg1	isoforms					172:179	Erythroagglutinating phytohemagglutinin (E-PHA)-dependent isoforms	114:179	Erythroagglutinating phytohemagglutinin (E-PHA)-dependent isoforms of human alpha-fetoprotein (AFP) from cord blood	114:228	Erythroagglutinating phytohemagglutinin (E-PHA)-dependent isoforms of human alpha-fetoprotein (AFP) from cord blood were analyzed for their carbohydrate structures by two-dimensional electrophoresis with E-PHA combined with extended agarose gel electrophoresis or with affinity electrophoresis with concanavalin A or Allomyrina dichtoma lectin.
7511099	1	17	from	blood	224:228	arg1	alpha-fetoprotein					190:206	human alpha-fetoprotein	184:206	human alpha-fetoprotein (AFP) from cord blood	184:228	Erythroagglutinating phytohemagglutinin (E-PHA)-dependent isoforms of human alpha-fetoprotein (AFP) from cord blood were analyzed for their carbohydrate structures by two-dimensional electrophoresis with E-PHA combined with extended agarose gel electrophoresis or with affinity electrophoresis with concanavalin A or Allomyrina dichtoma lectin.
7511099	1	18	theme	human	184:188	arg1	AFP					209:211	AFP	209:211	AFP	209:211	Erythroagglutinating phytohemagglutinin (E-PHA)-dependent isoforms of human alpha-fetoprotein (AFP) from cord blood were analyzed for their carbohydrate structures by two-dimensional electrophoresis with E-PHA combined with extended agarose gel electrophoresis or with affinity electrophoresis with concanavalin A or Allomyrina dichtoma lectin.
7511099	1	18	theme	human	184:188	arg1	alpha-fetoprotein					190:206	human alpha-fetoprotein	184:206	human alpha-fetoprotein (AFP) from cord blood	184:228	Erythroagglutinating phytohemagglutinin (E-PHA)-dependent isoforms of human alpha-fetoprotein (AFP) from cord blood were analyzed for their carbohydrate structures by two-dimensional electrophoresis with E-PHA combined with extended agarose gel electrophoresis or with affinity electrophoresis with concanavalin A or Allomyrina dichtoma lectin.
7511099	2	19	theme	biantennary	589:599	arg1	structures					601:610	biantennary structures	589:610	biantennary structures	589:610	By means of neuraminidase and/or beta-galactosidase treatment, AFP-P2 was identified as alpha 2-->6 disialo-AFP, AFP-P3 as having biantennary structures with alpha 2-->6 monosialylated galactose of the Mannose (Man) alpha 1-->6 arm, AFP-P4 as having alpha 2-->6 monosialylated galactose of the Man alpha 1-->3 arm, and AFP-P5 as disialo-AFP with alpha 2-->3 sialylated galactose of the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna.
7511099	0	20	theme	affinity	88:95	arg1	electrophoresis					97:111	two-dimensional lectin affinity electrophoresis	65:111	two-dimensional lectin affinity electrophoresis	65:111	Characterization of E-PHA-reactive alpha-fetoprotein isoforms by two-dimensional lectin affinity electrophoresis.
7511099	3	21	theme	Desialylated	933:944	arg1	AFP					946:948	Desialylated AFP	933:948	Desialylated AFP with the terminal galactose of the Man alpha 1-->6 antenna with or without the galactose of the other arm	933:1054	Desialylated AFP with the terminal galactose of the Man alpha 1-->6 antenna with or without the galactose of the other arm also had a migration of AFP-P4, and other hydrolytic intermediates without the terminal galactose of the Man alpha 1-->6 arm with and without the galactose of the other antenna had mobilities of AFP-P3s and AFP-P3, respectively.
7511099	1	22	theme	Allomyrina	431:440	arg1	lectin					451:456	Allomyrina dichtoma lectin	431:456	Allomyrina dichtoma lectin	431:456	Erythroagglutinating phytohemagglutinin (E-PHA)-dependent isoforms of human alpha-fetoprotein (AFP) from cord blood were analyzed for their carbohydrate structures by two-dimensional electrophoresis with E-PHA combined with extended agarose gel electrophoresis or with affinity electrophoresis with concanavalin A or Allomyrina dichtoma lectin.
7511099	3	23	theme	other	1092:1096	arg1	intermediates					1109:1121	other hydrolytic intermediates	1092:1121	other hydrolytic intermediates without the terminal galactose of the Man alpha 1-->6 arm with and without the galactose of the other antenna	1092:1231	Desialylated AFP with the terminal galactose of the Man alpha 1-->6 antenna with or without the galactose of the other arm also had a migration of AFP-P4, and other hydrolytic intermediates without the terminal galactose of the Man alpha 1-->6 arm with and without the galactose of the other antenna had mobilities of AFP-P3s and AFP-P3, respectively.
7511099	2	24	theme	2-->6	715:719	arg1	galactose					736:744	alpha 2-->6 monosialylated galactose	709:744	alpha 2-->6 monosialylated galactose of the Man alpha 1-->3 arm	709:771	By means of neuraminidase and/or beta-galactosidase treatment, AFP-P2 was identified as alpha 2-->6 disialo-AFP, AFP-P3 as having biantennary structures with alpha 2-->6 monosialylated galactose of the Mannose (Man) alpha 1-->6 arm, AFP-P4 as having alpha 2-->6 monosialylated galactose of the Man alpha 1-->3 arm, and AFP-P5 as disialo-AFP with alpha 2-->3 sialylated galactose of the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna.
7511099	1	25	theme	Erythroagglutinating	114:133	arg1	isoforms					172:179	Erythroagglutinating phytohemagglutinin (E-PHA)-dependent isoforms	114:179	Erythroagglutinating phytohemagglutinin (E-PHA)-dependent isoforms of human alpha-fetoprotein (AFP) from cord blood	114:228	Erythroagglutinating phytohemagglutinin (E-PHA)-dependent isoforms of human alpha-fetoprotein (AFP) from cord blood were analyzed for their carbohydrate structures by two-dimensional electrophoresis with E-PHA combined with extended agarose gel electrophoresis or with affinity electrophoresis with concanavalin A or Allomyrina dichtoma lectin.
7511099	3	26	theme	terminal	959:966	arg1	galactose					968:976	the terminal galactose	955:976	the terminal galactose of the Man alpha 1-->6 antenna	955:1007	Desialylated AFP with the terminal galactose of the Man alpha 1-->6 antenna with or without the galactose of the other arm also had a migration of AFP-P4, and other hydrolytic intermediates without the terminal galactose of the Man alpha 1-->6 arm with and without the galactose of the other antenna had mobilities of AFP-P3s and AFP-P3, respectively.
7511099	2	27	theme	alpha	757:761	arg1	arm					769:771	the Man alpha 1-->3 arm	749:771	the Man alpha 1-->3 arm	749:771	By means of neuraminidase and/or beta-galactosidase treatment, AFP-P2 was identified as alpha 2-->6 disialo-AFP, AFP-P3 as having biantennary structures with alpha 2-->6 monosialylated galactose of the Mannose (Man) alpha 1-->6 arm, AFP-P4 as having alpha 2-->6 monosialylated galactose of the Man alpha 1-->3 arm, and AFP-P5 as disialo-AFP with alpha 2-->3 sialylated galactose of the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna.
7511099	1	28	theme	extended	338:345	arg1	electrophoresis					359:373	extended agarose gel electrophoresis	338:373	extended agarose gel electrophoresis	338:373	Erythroagglutinating phytohemagglutinin (E-PHA)-dependent isoforms of human alpha-fetoprotein (AFP) from cord blood were analyzed for their carbohydrate structures by two-dimensional electrophoresis with E-PHA combined with extended agarose gel electrophoresis or with affinity electrophoresis with concanavalin A or Allomyrina dichtoma lectin.
7511099	3	29	theme	1-->6	995:999	arg1	antenna					1001:1007	the Man alpha 1-->6 antenna	981:1007	the Man alpha 1-->6 antenna	981:1007	Desialylated AFP with the terminal galactose of the Man alpha 1-->6 antenna with or without the galactose of the other arm also had a migration of AFP-P4, and other hydrolytic intermediates without the terminal galactose of the Man alpha 1-->6 arm with and without the galactose of the other antenna had mobilities of AFP-P3s and AFP-P3, respectively.
7511099	0	30	theme	E-PHA-reactive	20:33	arg1	alpha-fetoprotein					35:51	E-PHA-reactive alpha-fetoprotein	20:51	E-PHA-reactive alpha-fetoprotein	20:51	Characterization of E-PHA-reactive alpha-fetoprotein isoforms by two-dimensional lectin affinity electrophoresis.
7511099	1	31	theme	gel	355:357	arg1	electrophoresis					359:373	extended agarose gel electrophoresis	338:373	extended agarose gel electrophoresis	338:373	Erythroagglutinating phytohemagglutinin (E-PHA)-dependent isoforms of human alpha-fetoprotein (AFP) from cord blood were analyzed for their carbohydrate structures by two-dimensional electrophoresis with E-PHA combined with extended agarose gel electrophoresis or with affinity electrophoresis with concanavalin A or Allomyrina dichtoma lectin.
7511099	3	32	theme	alpha	1165:1169	arg1	arm					1177:1179	the Man alpha 1-->6 arm	1157:1179	the Man alpha 1-->6 arm	1157:1179	Desialylated AFP with the terminal galactose of the Man alpha 1-->6 antenna with or without the galactose of the other arm also had a migration of AFP-P4, and other hydrolytic intermediates without the terminal galactose of the Man alpha 1-->6 arm with and without the galactose of the other antenna had mobilities of AFP-P3s and AFP-P3, respectively.
7511099	3	33	theme	Man	985:987	arg1	antenna					1001:1007	the Man alpha 1-->6 antenna	981:1007	the Man alpha 1-->6 antenna	981:1007	Desialylated AFP with the terminal galactose of the Man alpha 1-->6 antenna with or without the galactose of the other arm also had a migration of AFP-P4, and other hydrolytic intermediates without the terminal galactose of the Man alpha 1-->6 arm with and without the galactose of the other antenna had mobilities of AFP-P3s and AFP-P3, respectively.
7511099	2	34	theme	2-->6	553:557	arg1	AFP-P2					522:527	AFP-P2	522:527	AFP-P2	522:527	By means of neuraminidase and/or beta-galactosidase treatment, AFP-P2 was identified as alpha 2-->6 disialo-AFP, AFP-P3 as having biantennary structures with alpha 2-->6 monosialylated galactose of the Mannose (Man) alpha 1-->6 arm, AFP-P4 as having alpha 2-->6 monosialylated galactose of the Man alpha 1-->3 arm, and AFP-P5 as disialo-AFP with alpha 2-->3 sialylated galactose of the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna.
7511099	2	34	theme	2-->6	553:557	arg1	disialo-AFP					559:569	alpha 2-->6 disialo-AFP	547:569	alpha 2-->6 disialo-AFP	547:569	By means of neuraminidase and/or beta-galactosidase treatment, AFP-P2 was identified as alpha 2-->6 disialo-AFP, AFP-P3 as having biantennary structures with alpha 2-->6 monosialylated galactose of the Mannose (Man) alpha 1-->6 arm, AFP-P4 as having alpha 2-->6 monosialylated galactose of the Man alpha 1-->3 arm, and AFP-P5 as disialo-AFP with alpha 2-->3 sialylated galactose of the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna.
7511099	4	35	theme	two-dimensional	1313:1327	arg1	electrophoreses					1345:1359	two-dimensional lectin affinity electrophoreses	1313:1359	two-dimensional lectin affinity electrophoreses	1313:1359	Thus, the present system of two-dimensional lectin affinity electrophoreses would provide a model for the determination of the sugar chain structure of glycoproteins.
7511099	0	36	theme	two-dimensional	65:79	arg1	electrophoresis					97:111	two-dimensional lectin affinity electrophoresis	65:111	two-dimensional lectin affinity electrophoresis	65:111	Characterization of E-PHA-reactive alpha-fetoprotein isoforms by two-dimensional lectin affinity electrophoresis.
7511099	1	37	theme	affinity	383:390	arg1	electrophoresis					392:406	affinity electrophoresis	383:406	affinity electrophoresis	383:406	Erythroagglutinating phytohemagglutinin (E-PHA)-dependent isoforms of human alpha-fetoprotein (AFP) from cord blood were analyzed for their carbohydrate structures by two-dimensional electrophoresis with E-PHA combined with extended agarose gel electrophoresis or with affinity electrophoresis with concanavalin A or Allomyrina dichtoma lectin.
7511099	2	38	theme	alpha	878:882	arg1	galactose					901:909	the alpha 2-->6 sialylated galactose	874:909	the alpha 2-->6 sialylated galactose of the other antenna	874:930	By means of neuraminidase and/or beta-galactosidase treatment, AFP-P2 was identified as alpha 2-->6 disialo-AFP, AFP-P3 as having biantennary structures with alpha 2-->6 monosialylated galactose of the Mannose (Man) alpha 1-->6 arm, AFP-P4 as having alpha 2-->6 monosialylated galactose of the Man alpha 1-->3 arm, and AFP-P5 as disialo-AFP with alpha 2-->3 sialylated galactose of the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna.
7511099	4	39	gly	glycoproteins	1437:1449	arg1	glycoproteins					1437:1449	glycoproteins	1437:1449	glycoproteins	1437:1449	Thus, the present system of two-dimensional lectin affinity electrophoreses would provide a model for the determination of the sugar chain structure of glycoproteins.
7511099	3	40	theme	arm	1177:1179	arg1	galactose					1144:1152	the terminal galactose	1131:1152	the terminal galactose of the Man alpha 1-->6 arm	1131:1179	Desialylated AFP with the terminal galactose of the Man alpha 1-->6 antenna with or without the galactose of the other arm also had a migration of AFP-P4, and other hydrolytic intermediates without the terminal galactose of the Man alpha 1-->6 arm with and without the galactose of the other antenna had mobilities of AFP-P3s and AFP-P3, respectively.
7511099	2	41	theme	antenna	924:930	arg1	galactose					901:909	the alpha 2-->6 sialylated galactose	874:909	the alpha 2-->6 sialylated galactose of the other antenna	874:930	By means of neuraminidase and/or beta-galactosidase treatment, AFP-P2 was identified as alpha 2-->6 disialo-AFP, AFP-P3 as having biantennary structures with alpha 2-->6 monosialylated galactose of the Mannose (Man) alpha 1-->6 arm, AFP-P4 as having alpha 2-->6 monosialylated galactose of the Man alpha 1-->3 arm, and AFP-P5 as disialo-AFP with alpha 2-->3 sialylated galactose of the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna.
7511099	2	42	dep	neuraminidase	471:483	arg1	treatment					511:519	treatment	511:519	treatment	511:519	By means of neuraminidase and/or beta-galactosidase treatment, AFP-P2 was identified as alpha 2-->6 disialo-AFP, AFP-P3 as having biantennary structures with alpha 2-->6 monosialylated galactose of the Mannose (Man) alpha 1-->6 arm, AFP-P4 as having alpha 2-->6 monosialylated galactose of the Man alpha 1-->3 arm, and AFP-P5 as disialo-AFP with alpha 2-->3 sialylated galactose of the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna.
7511099	1	43	theme	two-dimensional	281:295	arg1	electrophoresis					297:311	two-dimensional electrophoresis	281:311	two-dimensional electrophoresis with E-PHA combined with extended agarose gel electrophoresis or with affinity electrophoresis with concanavalin A or Allomyrina dichtoma lectin	281:456	Erythroagglutinating phytohemagglutinin (E-PHA)-dependent isoforms of human alpha-fetoprotein (AFP) from cord blood were analyzed for their carbohydrate structures by two-dimensional electrophoresis with E-PHA combined with extended agarose gel electrophoresis or with affinity electrophoresis with concanavalin A or Allomyrina dichtoma lectin.
7511099	3	44	with	AFP	946:948	arg1	galactose					968:976	the terminal galactose	955:976	the terminal galactose of the Man alpha 1-->6 antenna	955:1007	Desialylated AFP with the terminal galactose of the Man alpha 1-->6 antenna with or without the galactose of the other arm also had a migration of AFP-P4, and other hydrolytic intermediates without the terminal galactose of the Man alpha 1-->6 arm with and without the galactose of the other antenna had mobilities of AFP-P3s and AFP-P3, respectively.
7511099	2	45	theme	arm	687:689	arg1	galactose					644:652	galactose	644:652	galactose of the Mannose (Man) alpha 1-->6 arm, AFP-P4	644:697	By means of neuraminidase and/or beta-galactosidase treatment, AFP-P2 was identified as alpha 2-->6 disialo-AFP, AFP-P3 as having biantennary structures with alpha 2-->6 monosialylated galactose of the Mannose (Man) alpha 1-->6 arm, AFP-P4 as having alpha 2-->6 monosialylated galactose of the Man alpha 1-->3 arm, and AFP-P5 as disialo-AFP with alpha 2-->3 sialylated galactose of the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna.
7511099	2	46	theme	sialylated	890:899	arg1	galactose					901:909	the alpha 2-->6 sialylated galactose	874:909	the alpha 2-->6 sialylated galactose of the other antenna	874:930	By means of neuraminidase and/or beta-galactosidase treatment, AFP-P2 was identified as alpha 2-->6 disialo-AFP, AFP-P3 as having biantennary structures with alpha 2-->6 monosialylated galactose of the Mannose (Man) alpha 1-->6 arm, AFP-P4 as having alpha 2-->6 monosialylated galactose of the Man alpha 1-->3 arm, and AFP-P5 as disialo-AFP with alpha 2-->3 sialylated galactose of the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna.
7511099	2	47	theme	alpha	675:679	arg1	arm					687:689	the Mannose (Man) alpha 1-->6 arm	657:689	the Mannose (Man) alpha 1-->6 arm	657:689	By means of neuraminidase and/or beta-galactosidase treatment, AFP-P2 was identified as alpha 2-->6 disialo-AFP, AFP-P3 as having biantennary structures with alpha 2-->6 monosialylated galactose of the Mannose (Man) alpha 1-->6 arm, AFP-P4 as having alpha 2-->6 monosialylated galactose of the Man alpha 1-->3 arm, and AFP-P5 as disialo-AFP with alpha 2-->3 sialylated galactose of the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna.
7511099	2	47	theme	alpha	675:679	arg1	AFP-P4					692:697	AFP-P4	692:697	AFP-P4	692:697	By means of neuraminidase and/or beta-galactosidase treatment, AFP-P2 was identified as alpha 2-->6 disialo-AFP, AFP-P3 as having biantennary structures with alpha 2-->6 monosialylated galactose of the Mannose (Man) alpha 1-->6 arm, AFP-P4 as having alpha 2-->6 monosialylated galactose of the Man alpha 1-->3 arm, and AFP-P5 as disialo-AFP with alpha 2-->3 sialylated galactose of the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna.
7511099	3	48	theme	arm	1052:1054	arg1	galactose					1029:1037	the galactose	1025:1037	the galactose of the other arm	1025:1054	Desialylated AFP with the terminal galactose of the Man alpha 1-->6 antenna with or without the galactose of the other arm also had a migration of AFP-P4, and other hydrolytic intermediates without the terminal galactose of the Man alpha 1-->6 arm with and without the galactose of the other antenna had mobilities of AFP-P3s and AFP-P3, respectively.
7511099	4	49	theme	affinity	1336:1343	arg1	electrophoreses					1345:1359	two-dimensional lectin affinity electrophoreses	1313:1359	two-dimensional lectin affinity electrophoreses	1313:1359	Thus, the present system of two-dimensional lectin affinity electrophoreses would provide a model for the determination of the sugar chain structure of glycoproteins.
7511099	3	50	theme	other	1219:1223	arg1	antenna					1225:1231	the other antenna	1215:1231	the other antenna	1215:1231	Desialylated AFP with the terminal galactose of the Man alpha 1-->6 antenna with or without the galactose of the other arm also had a migration of AFP-P4, and other hydrolytic intermediates without the terminal galactose of the Man alpha 1-->6 arm with and without the galactose of the other antenna had mobilities of AFP-P3s and AFP-P3, respectively.
7511099	3	51	theme	AFP-P4	1080:1085	arg1	migration					1067:1075	a migration	1065:1075	a migration of AFP-P4	1065:1085	Desialylated AFP with the terminal galactose of the Man alpha 1-->6 antenna with or without the galactose of the other arm also had a migration of AFP-P4, and other hydrolytic intermediates without the terminal galactose of the Man alpha 1-->6 arm with and without the galactose of the other antenna had mobilities of AFP-P3s and AFP-P3, respectively.
7511099	2	52	theme	sialylated	817:826	arg1	galactose					828:836	alpha 2-->3 sialylated galactose	805:836	alpha 2-->3 sialylated galactose of the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna	805:930	By means of neuraminidase and/or beta-galactosidase treatment, AFP-P2 was identified as alpha 2-->6 disialo-AFP, AFP-P3 as having biantennary structures with alpha 2-->6 monosialylated galactose of the Mannose (Man) alpha 1-->6 arm, AFP-P4 as having alpha 2-->6 monosialylated galactose of the Man alpha 1-->3 arm, and AFP-P5 as disialo-AFP with alpha 2-->3 sialylated galactose of the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna.
7511099	2	53	theme	1-->6	855:859	arg1	antenna					861:867	the Man alpha 1-->6 antenna	841:867	the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna	841:930	By means of neuraminidase and/or beta-galactosidase treatment, AFP-P2 was identified as alpha 2-->6 disialo-AFP, AFP-P3 as having biantennary structures with alpha 2-->6 monosialylated galactose of the Mannose (Man) alpha 1-->6 arm, AFP-P4 as having alpha 2-->6 monosialylated galactose of the Man alpha 1-->3 arm, and AFP-P5 as disialo-AFP with alpha 2-->3 sialylated galactose of the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna.
7511099	4	54	theme	chain	1418:1422	arg1	structure					1424:1432	the sugar chain structure	1408:1432	the sugar chain structure of glycoproteins	1408:1449	Thus, the present system of two-dimensional lectin affinity electrophoreses would provide a model for the determination of the sugar chain structure of glycoproteins.
7511099	2	55	theme	Man	845:847	arg1	antenna					861:867	the Man alpha 1-->6 antenna	841:867	the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna	841:930	By means of neuraminidase and/or beta-galactosidase treatment, AFP-P2 was identified as alpha 2-->6 disialo-AFP, AFP-P3 as having biantennary structures with alpha 2-->6 monosialylated galactose of the Mannose (Man) alpha 1-->6 arm, AFP-P4 as having alpha 2-->6 monosialylated galactose of the Man alpha 1-->3 arm, and AFP-P5 as disialo-AFP with alpha 2-->3 sialylated galactose of the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna.
7511099	2	56	gly	sialylated	890:899	arg1	galactose					901:909	the alpha 2-->6 sialylated galactose	874:909	the alpha 2-->6 sialylated galactose of the other antenna	874:930	By means of neuraminidase and/or beta-galactosidase treatment, AFP-P2 was identified as alpha 2-->6 disialo-AFP, AFP-P3 as having biantennary structures with alpha 2-->6 monosialylated galactose of the Mannose (Man) alpha 1-->6 arm, AFP-P4 as having alpha 2-->6 monosialylated galactose of the Man alpha 1-->3 arm, and AFP-P5 as disialo-AFP with alpha 2-->3 sialylated galactose of the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna.
7511099	1	57	theme	-dependent	161:170	arg1	isoforms					172:179	Erythroagglutinating phytohemagglutinin (E-PHA)-dependent isoforms	114:179	Erythroagglutinating phytohemagglutinin (E-PHA)-dependent isoforms of human alpha-fetoprotein (AFP) from cord blood	114:228	Erythroagglutinating phytohemagglutinin (E-PHA)-dependent isoforms of human alpha-fetoprotein (AFP) from cord blood were analyzed for their carbohydrate structures by two-dimensional electrophoresis with E-PHA combined with extended agarose gel electrophoresis or with affinity electrophoresis with concanavalin A or Allomyrina dichtoma lectin.
7511099	2	58	theme	Man	670:672	arg1	arm					687:689	the Mannose (Man) alpha 1-->6 arm	657:689	the Mannose (Man) alpha 1-->6 arm	657:689	By means of neuraminidase and/or beta-galactosidase treatment, AFP-P2 was identified as alpha 2-->6 disialo-AFP, AFP-P3 as having biantennary structures with alpha 2-->6 monosialylated galactose of the Mannose (Man) alpha 1-->6 arm, AFP-P4 as having alpha 2-->6 monosialylated galactose of the Man alpha 1-->3 arm, and AFP-P5 as disialo-AFP with alpha 2-->3 sialylated galactose of the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna.
7511099	2	58	theme	Man	670:672	arg1	AFP-P4					692:697	AFP-P4	692:697	AFP-P4	692:697	By means of neuraminidase and/or beta-galactosidase treatment, AFP-P2 was identified as alpha 2-->6 disialo-AFP, AFP-P3 as having biantennary structures with alpha 2-->6 monosialylated galactose of the Mannose (Man) alpha 1-->6 arm, AFP-P4 as having alpha 2-->6 monosialylated galactose of the Man alpha 1-->3 arm, and AFP-P5 as disialo-AFP with alpha 2-->3 sialylated galactose of the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna.
7511099	3	59	contain	had	1233:1235	arg2	mobilities					1237:1246	mobilities	1237:1246	mobilities of AFP-P3s and AFP-P3	1237:1268	Desialylated AFP with the terminal galactose of the Man alpha 1-->6 antenna with or without the galactose of the other arm also had a migration of AFP-P4, and other hydrolytic intermediates without the terminal galactose of the Man alpha 1-->6 arm with and without the galactose of the other antenna had mobilities of AFP-P3s and AFP-P3, respectively.
7511099	3	59	contain	had	1233:1235	arg1	intermediates					1109:1121	other hydrolytic intermediates	1092:1121	other hydrolytic intermediates without the terminal galactose of the Man alpha 1-->6 arm with and without the galactose of the other antenna	1092:1231	Desialylated AFP with the terminal galactose of the Man alpha 1-->6 antenna with or without the galactose of the other arm also had a migration of AFP-P4, and other hydrolytic intermediates without the terminal galactose of the Man alpha 1-->6 arm with and without the galactose of the other antenna had mobilities of AFP-P3s and AFP-P3, respectively.
7511099	2	60	theme	Mannose	661:667	arg1	arm					687:689	the Mannose (Man) alpha 1-->6 arm	657:689	the Mannose (Man) alpha 1-->6 arm	657:689	By means of neuraminidase and/or beta-galactosidase treatment, AFP-P2 was identified as alpha 2-->6 disialo-AFP, AFP-P3 as having biantennary structures with alpha 2-->6 monosialylated galactose of the Mannose (Man) alpha 1-->6 arm, AFP-P4 as having alpha 2-->6 monosialylated galactose of the Man alpha 1-->3 arm, and AFP-P5 as disialo-AFP with alpha 2-->3 sialylated galactose of the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna.
7511099	2	60	theme	Mannose	661:667	arg1	AFP-P4					692:697	AFP-P4	692:697	AFP-P4	692:697	By means of neuraminidase and/or beta-galactosidase treatment, AFP-P2 was identified as alpha 2-->6 disialo-AFP, AFP-P3 as having biantennary structures with alpha 2-->6 monosialylated galactose of the Mannose (Man) alpha 1-->6 arm, AFP-P4 as having alpha 2-->6 monosialylated galactose of the Man alpha 1-->3 arm, and AFP-P5 as disialo-AFP with alpha 2-->3 sialylated galactose of the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna.
7511099	2	61	theme	alpha	805:809	arg1	galactose					828:836	alpha 2-->3 sialylated galactose	805:836	alpha 2-->3 sialylated galactose of the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna	805:930	By means of neuraminidase and/or beta-galactosidase treatment, AFP-P2 was identified as alpha 2-->6 disialo-AFP, AFP-P3 as having biantennary structures with alpha 2-->6 monosialylated galactose of the Mannose (Man) alpha 1-->6 arm, AFP-P4 as having alpha 2-->6 monosialylated galactose of the Man alpha 1-->3 arm, and AFP-P5 as disialo-AFP with alpha 2-->3 sialylated galactose of the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna.
7511099	1	62	theme	alpha-fetoprotein	190:206	arg1	isoforms					172:179	Erythroagglutinating phytohemagglutinin (E-PHA)-dependent isoforms	114:179	Erythroagglutinating phytohemagglutinin (E-PHA)-dependent isoforms of human alpha-fetoprotein (AFP) from cord blood	114:228	Erythroagglutinating phytohemagglutinin (E-PHA)-dependent isoforms of human alpha-fetoprotein (AFP) from cord blood were analyzed for their carbohydrate structures by two-dimensional electrophoresis with E-PHA combined with extended agarose gel electrophoresis or with affinity electrophoresis with concanavalin A or Allomyrina dichtoma lectin.
7511099	3	63	gly	Desialylated	933:944	arg1	AFP					946:948	Desialylated AFP	933:948	Desialylated AFP with the terminal galactose of the Man alpha 1-->6 antenna with or without the galactose of the other arm	933:1054	Desialylated AFP with the terminal galactose of the Man alpha 1-->6 antenna with or without the galactose of the other arm also had a migration of AFP-P4, and other hydrolytic intermediates without the terminal galactose of the Man alpha 1-->6 arm with and without the galactose of the other antenna had mobilities of AFP-P3s and AFP-P3, respectively.
7511099	1	64	theme	concanavalin	413:424	arg1	A					426:426	concanavalin A	413:426	concanavalin A	413:426	Erythroagglutinating phytohemagglutinin (E-PHA)-dependent isoforms of human alpha-fetoprotein (AFP) from cord blood were analyzed for their carbohydrate structures by two-dimensional electrophoresis with E-PHA combined with extended agarose gel electrophoresis or with affinity electrophoresis with concanavalin A or Allomyrina dichtoma lectin.
7511099	3	65	theme	hydrolytic	1098:1107	arg1	intermediates					1109:1121	other hydrolytic intermediates	1092:1121	other hydrolytic intermediates without the terminal galactose of the Man alpha 1-->6 arm with and without the galactose of the other antenna	1092:1231	Desialylated AFP with the terminal galactose of the Man alpha 1-->6 antenna with or without the galactose of the other arm also had a migration of AFP-P4, and other hydrolytic intermediates without the terminal galactose of the Man alpha 1-->6 arm with and without the galactose of the other antenna had mobilities of AFP-P3s and AFP-P3, respectively.
7511099	2	66	gly	monosialylated	629:642	arg1	AFP-P3					572:577	AFP-P3	572:577	AFP-P3 as having biantennary structures with alpha 2-->6 monosialylated galactose of the Mannose (Man) alpha 1-->6 arm, AFP-P4 as having alpha 2-->6 monosialylated galactose of the Man alpha 1-->3 arm	572:771	By means of neuraminidase and/or beta-galactosidase treatment, AFP-P2 was identified as alpha 2-->6 disialo-AFP, AFP-P3 as having biantennary structures with alpha 2-->6 monosialylated galactose of the Mannose (Man) alpha 1-->6 arm, AFP-P4 as having alpha 2-->6 monosialylated galactose of the Man alpha 1-->3 arm, and AFP-P5 as disialo-AFP with alpha 2-->3 sialylated galactose of the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna.
7511099	2	66	gly	monosialylated	629:642	arg1	AFP-P2					522:527	AFP-P2	522:527	AFP-P2	522:527	By means of neuraminidase and/or beta-galactosidase treatment, AFP-P2 was identified as alpha 2-->6 disialo-AFP, AFP-P3 as having biantennary structures with alpha 2-->6 monosialylated galactose of the Mannose (Man) alpha 1-->6 arm, AFP-P4 as having alpha 2-->6 monosialylated galactose of the Man alpha 1-->3 arm, and AFP-P5 as disialo-AFP with alpha 2-->3 sialylated galactose of the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna.
7511099	2	67	theme	alpha	617:621	arg1	2-->6					623:627	alpha 2-->6	617:627	alpha 2-->6	617:627	By means of neuraminidase and/or beta-galactosidase treatment, AFP-P2 was identified as alpha 2-->6 disialo-AFP, AFP-P3 as having biantennary structures with alpha 2-->6 monosialylated galactose of the Mannose (Man) alpha 1-->6 arm, AFP-P4 as having alpha 2-->6 monosialylated galactose of the Man alpha 1-->3 arm, and AFP-P5 as disialo-AFP with alpha 2-->3 sialylated galactose of the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna.
7511099	2	68	theme	monosialylated	721:734	arg1	galactose					736:744	alpha 2-->6 monosialylated galactose	709:744	alpha 2-->6 monosialylated galactose of the Man alpha 1-->3 arm	709:771	By means of neuraminidase and/or beta-galactosidase treatment, AFP-P2 was identified as alpha 2-->6 disialo-AFP, AFP-P3 as having biantennary structures with alpha 2-->6 monosialylated galactose of the Mannose (Man) alpha 1-->6 arm, AFP-P4 as having alpha 2-->6 monosialylated galactose of the Man alpha 1-->3 arm, and AFP-P5 as disialo-AFP with alpha 2-->3 sialylated galactose of the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna.
7511099	1	69	theme	dichtoma	442:449	arg1	lectin					451:456	Allomyrina dichtoma lectin	431:456	Allomyrina dichtoma lectin	431:456	Erythroagglutinating phytohemagglutinin (E-PHA)-dependent isoforms of human alpha-fetoprotein (AFP) from cord blood were analyzed for their carbohydrate structures by two-dimensional electrophoresis with E-PHA combined with extended agarose gel electrophoresis or with affinity electrophoresis with concanavalin A or Allomyrina dichtoma lectin.
7511099	3	70	contain	had	1061:1063	arg1	AFP					946:948	Desialylated AFP	933:948	Desialylated AFP with the terminal galactose of the Man alpha 1-->6 antenna with or without the galactose of the other arm	933:1054	Desialylated AFP with the terminal galactose of the Man alpha 1-->6 antenna with or without the galactose of the other arm also had a migration of AFP-P4, and other hydrolytic intermediates without the terminal galactose of the Man alpha 1-->6 arm with and without the galactose of the other antenna had mobilities of AFP-P3s and AFP-P3, respectively.
7511099	3	70	contain	had	1061:1063	arg2	migration					1067:1075	a migration	1065:1075	a migration of AFP-P4	1065:1085	Desialylated AFP with the terminal galactose of the Man alpha 1-->6 antenna with or without the galactose of the other arm also had a migration of AFP-P4, and other hydrolytic intermediates without the terminal galactose of the Man alpha 1-->6 arm with and without the galactose of the other antenna had mobilities of AFP-P3s and AFP-P3, respectively.
7511099	2	71	theme	1-->3	763:767	arg1	arm					769:771	the Man alpha 1-->3 arm	749:771	the Man alpha 1-->3 arm	749:771	By means of neuraminidase and/or beta-galactosidase treatment, AFP-P2 was identified as alpha 2-->6 disialo-AFP, AFP-P3 as having biantennary structures with alpha 2-->6 monosialylated galactose of the Mannose (Man) alpha 1-->6 arm, AFP-P4 as having alpha 2-->6 monosialylated galactose of the Man alpha 1-->3 arm, and AFP-P5 as disialo-AFP with alpha 2-->3 sialylated galactose of the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna.
7511099	2	72	gly	sialylated	817:826	arg1	galactose					828:836	alpha 2-->3 sialylated galactose	805:836	alpha 2-->3 sialylated galactose of the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna	805:930	By means of neuraminidase and/or beta-galactosidase treatment, AFP-P2 was identified as alpha 2-->6 disialo-AFP, AFP-P3 as having biantennary structures with alpha 2-->6 monosialylated galactose of the Mannose (Man) alpha 1-->6 arm, AFP-P4 as having alpha 2-->6 monosialylated galactose of the Man alpha 1-->3 arm, and AFP-P5 as disialo-AFP with alpha 2-->3 sialylated galactose of the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna.
7511099	2	73	theme	Man	753:755	arg1	arm					769:771	the Man alpha 1-->3 arm	749:771	the Man alpha 1-->3 arm	749:771	By means of neuraminidase and/or beta-galactosidase treatment, AFP-P2 was identified as alpha 2-->6 disialo-AFP, AFP-P3 as having biantennary structures with alpha 2-->6 monosialylated galactose of the Mannose (Man) alpha 1-->6 arm, AFP-P4 as having alpha 2-->6 monosialylated galactose of the Man alpha 1-->3 arm, and AFP-P5 as disialo-AFP with alpha 2-->3 sialylated galactose of the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna.
7511099	3	74	theme	terminal	1135:1142	arg1	galactose					1144:1152	the terminal galactose	1131:1152	the terminal galactose of the Man alpha 1-->6 arm	1131:1179	Desialylated AFP with the terminal galactose of the Man alpha 1-->6 antenna with or without the galactose of the other arm also had a migration of AFP-P4, and other hydrolytic intermediates without the terminal galactose of the Man alpha 1-->6 arm with and without the galactose of the other antenna had mobilities of AFP-P3s and AFP-P3, respectively.
7511099	0	75	theme	alpha-fetoprotein	35:51	arg1	Characterization					0:15	Characterization	0:15	Characterization of E-PHA-reactive alpha-fetoprotein	0:51	Characterization of E-PHA-reactive alpha-fetoprotein isoforms by two-dimensional lectin affinity electrophoresis.
7511099	1	76	theme	agarose	347:353	arg1	electrophoresis					359:373	extended agarose gel electrophoresis	338:373	extended agarose gel electrophoresis	338:373	Erythroagglutinating phytohemagglutinin (E-PHA)-dependent isoforms of human alpha-fetoprotein (AFP) from cord blood were analyzed for their carbohydrate structures by two-dimensional electrophoresis with E-PHA combined with extended agarose gel electrophoresis or with affinity electrophoresis with concanavalin A or Allomyrina dichtoma lectin.
7511099	3	77	theme	Man	1161:1163	arg1	arm					1177:1179	the Man alpha 1-->6 arm	1157:1179	the Man alpha 1-->6 arm	1157:1179	Desialylated AFP with the terminal galactose of the Man alpha 1-->6 antenna with or without the galactose of the other arm also had a migration of AFP-P4, and other hydrolytic intermediates without the terminal galactose of the Man alpha 1-->6 arm with and without the galactose of the other antenna had mobilities of AFP-P3s and AFP-P3, respectively.
7511099	1	78	from	isoforms	172:179	arg1	blood					224:228	cord blood	219:228	cord blood	219:228	Erythroagglutinating phytohemagglutinin (E-PHA)-dependent isoforms of human alpha-fetoprotein (AFP) from cord blood were analyzed for their carbohydrate structures by two-dimensional electrophoresis with E-PHA combined with extended agarose gel electrophoresis or with affinity electrophoresis with concanavalin A or Allomyrina dichtoma lectin.
7511099	3	79	theme	antenna	1001:1007	arg1	galactose					968:976	the terminal galactose	955:976	the terminal galactose of the Man alpha 1-->6 antenna	955:1007	Desialylated AFP with the terminal galactose of the Man alpha 1-->6 antenna with or without the galactose of the other arm also had a migration of AFP-P4, and other hydrolytic intermediates without the terminal galactose of the Man alpha 1-->6 arm with and without the galactose of the other antenna had mobilities of AFP-P3s and AFP-P3, respectively.
7511099	1	80	with	electrophoresis	297:311	arg1	E-PHA					318:322	E-PHA	318:322	E-PHA combined with extended agarose gel electrophoresis or with affinity electrophoresis with concanavalin A or Allomyrina dichtoma lectin	318:456	Erythroagglutinating phytohemagglutinin (E-PHA)-dependent isoforms of human alpha-fetoprotein (AFP) from cord blood were analyzed for their carbohydrate structures by two-dimensional electrophoresis with E-PHA combined with extended agarose gel electrophoresis or with affinity electrophoresis with concanavalin A or Allomyrina dichtoma lectin.
7511099	2	81	with	disialo-AFP	788:798	arg1	galactose					828:836	alpha 2-->3 sialylated galactose	805:836	alpha 2-->3 sialylated galactose of the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna	805:930	By means of neuraminidase and/or beta-galactosidase treatment, AFP-P2 was identified as alpha 2-->6 disialo-AFP, AFP-P3 as having biantennary structures with alpha 2-->6 monosialylated galactose of the Mannose (Man) alpha 1-->6 arm, AFP-P4 as having alpha 2-->6 monosialylated galactose of the Man alpha 1-->3 arm, and AFP-P5 as disialo-AFP with alpha 2-->3 sialylated galactose of the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna.
7511099	3	82	theme	alpha	989:993	arg1	antenna					1001:1007	the Man alpha 1-->6 antenna	981:1007	the Man alpha 1-->6 antenna	981:1007	Desialylated AFP with the terminal galactose of the Man alpha 1-->6 antenna with or without the galactose of the other arm also had a migration of AFP-P4, and other hydrolytic intermediates without the terminal galactose of the Man alpha 1-->6 arm with and without the galactose of the other antenna had mobilities of AFP-P3s and AFP-P3, respectively.
7511099	4	83	theme	lectin	1329:1334	arg1	electrophoreses					1345:1359	two-dimensional lectin affinity electrophoreses	1313:1359	two-dimensional lectin affinity electrophoreses	1313:1359	Thus, the present system of two-dimensional lectin affinity electrophoreses would provide a model for the determination of the sugar chain structure of glycoproteins.
7511099	0	84	theme	lectin	81:86	arg1	electrophoresis					97:111	two-dimensional lectin affinity electrophoresis	65:111	two-dimensional lectin affinity electrophoresis	65:111	Characterization of E-PHA-reactive alpha-fetoprotein isoforms by two-dimensional lectin affinity electrophoresis.
7511099	2	85	theme	alpha	547:551	arg1	AFP-P2					522:527	AFP-P2	522:527	AFP-P2	522:527	By means of neuraminidase and/or beta-galactosidase treatment, AFP-P2 was identified as alpha 2-->6 disialo-AFP, AFP-P3 as having biantennary structures with alpha 2-->6 monosialylated galactose of the Mannose (Man) alpha 1-->6 arm, AFP-P4 as having alpha 2-->6 monosialylated galactose of the Man alpha 1-->3 arm, and AFP-P5 as disialo-AFP with alpha 2-->3 sialylated galactose of the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna.
7511099	2	85	theme	alpha	547:551	arg1	disialo-AFP					559:569	alpha 2-->6 disialo-AFP	547:569	alpha 2-->6 disialo-AFP	547:569	By means of neuraminidase and/or beta-galactosidase treatment, AFP-P2 was identified as alpha 2-->6 disialo-AFP, AFP-P3 as having biantennary structures with alpha 2-->6 monosialylated galactose of the Mannose (Man) alpha 1-->6 arm, AFP-P4 as having alpha 2-->6 monosialylated galactose of the Man alpha 1-->3 arm, and AFP-P5 as disialo-AFP with alpha 2-->3 sialylated galactose of the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna.
7511099	3	86	theme	1-->6	1171:1175	arg1	arm					1177:1179	the Man alpha 1-->6 arm	1157:1179	the Man alpha 1-->6 arm	1157:1179	Desialylated AFP with the terminal galactose of the Man alpha 1-->6 antenna with or without the galactose of the other arm also had a migration of AFP-P4, and other hydrolytic intermediates without the terminal galactose of the Man alpha 1-->6 arm with and without the galactose of the other antenna had mobilities of AFP-P3s and AFP-P3, respectively.
7511099	4	87	theme	present	1295:1301	arg1	system					1303:1308	the present system	1291:1308	the present system of two-dimensional lectin affinity electrophoreses	1291:1359	Thus, the present system of two-dimensional lectin affinity electrophoreses would provide a model for the determination of the sugar chain structure of glycoproteins.
7511099	3	88	theme	other	1046:1050	arg1	arm					1052:1054	the other arm	1042:1054	the other arm	1042:1054	Desialylated AFP with the terminal galactose of the Man alpha 1-->6 antenna with or without the galactose of the other arm also had a migration of AFP-P4, and other hydrolytic intermediates without the terminal galactose of the Man alpha 1-->6 arm with and without the galactose of the other antenna had mobilities of AFP-P3s and AFP-P3, respectively.
7511099	2	89	theme	antenna	861:867	arg1	galactose					828:836	alpha 2-->3 sialylated galactose	805:836	alpha 2-->3 sialylated galactose of the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna	805:930	By means of neuraminidase and/or beta-galactosidase treatment, AFP-P2 was identified as alpha 2-->6 disialo-AFP, AFP-P3 as having biantennary structures with alpha 2-->6 monosialylated galactose of the Mannose (Man) alpha 1-->6 arm, AFP-P4 as having alpha 2-->6 monosialylated galactose of the Man alpha 1-->3 arm, and AFP-P5 as disialo-AFP with alpha 2-->3 sialylated galactose of the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna.
7511099	2	90	theme	other	918:922	arg1	antenna					924:930	the other antenna	914:930	the other antenna	914:930	By means of neuraminidase and/or beta-galactosidase treatment, AFP-P2 was identified as alpha 2-->6 disialo-AFP, AFP-P3 as having biantennary structures with alpha 2-->6 monosialylated galactose of the Mannose (Man) alpha 1-->6 arm, AFP-P4 as having alpha 2-->6 monosialylated galactose of the Man alpha 1-->3 arm, and AFP-P5 as disialo-AFP with alpha 2-->3 sialylated galactose of the Man alpha 1-->6 antenna with the alpha 2-->6 sialylated galactose of the other antenna.
2775488	4	0	theme	R	1013:1013	arg1	B2					1021:1022	R = Ser B2	1013:1022	Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro	721:1046	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	3	1	theme	500	569:571	arg1	MHz					573:575	MHz	573:575	MHz	573:575	Structural determination was done using one- and two-dimensional 500 MHz 1H-NMR spectroscopy and FAB mass spectrometry of native and derivatized glycopeptides.
2775488	4	2	theme	alpha	923:927	arg1	beta					982:985	Neu5Ac alpha 2-3-Gal beta 1-3	961:989	Neu5Ac alpha 2-3-Gal beta 1-3	961:989	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	4	2	theme	alpha	923:927	arg1	beta					951:954	Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6	721:958	Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro	721:1046	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	1	3	theme	aged	278:281	arg1	patients					268:275	two patients	264:275	two patients	264:275	Glycopeptides have been isolated from the urine of two patients, aged 5 and 6, with a new lysosomal storage disease characterized by a deficiency in alpha-N-acetylgalactosaminidase activity.
2775488	0	4	theme	type	102:105	arg1	glycopeptides					68:80	sialic-acid-containing glycopeptides	45:80	sialic-acid-containing glycopeptides of the O-glycosidic type	45:105	Isolation and structural characterization of sialic-acid-containing glycopeptides of the O-glycosidic type from the urine of two patients with an hereditary deficiency in alpha-N-acetylgalactosaminidase activity.
2775488	0	5	from	urine	116:120	arg1	Isolation					0:8	Isolation	0:8	Isolation	0:8	Isolation and structural characterization of sialic-acid-containing glycopeptides of the O-glycosidic type from the urine of two patients with an hereditary deficiency in alpha-N-acetylgalactosaminidase activity.
2775488	0	5	from	urine	116:120	arg1	characterization					25:40	structural characterization	14:40	structural characterization	14:40	Isolation and structural characterization of sialic-acid-containing glycopeptides of the O-glycosidic type from the urine of two patients with an hereditary deficiency in alpha-N-acetylgalactosaminidase activity.
2775488	4	6	theme	=	1038:1038	arg1	Thr-Pro					1040:1046	R = Thr-Pro	1036:1046	Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro	721:1046	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	3	7	theme	MHz	573:575	arg1	spectroscopy					584:595	500 MHz 1H-NMR spectroscopy	569:595	500 MHz 1H-NMR spectroscopy	569:595	Structural determination was done using one- and two-dimensional 500 MHz 1H-NMR spectroscopy and FAB mass spectrometry of native and derivatized glycopeptides.
2775488	4	8	theme	1-4GlcNAc	941:949	arg1	beta					982:985	Neu5Ac alpha 2-3-Gal beta 1-3	961:989	Neu5Ac alpha 2-3-Gal beta 1-3	961:989	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	4	8	theme	1-4GlcNAc	941:949	arg1	beta					951:954	Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6	721:958	Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro	721:1046	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	4	9	theme	=	1026:1026	arg1	B3					1032:1033	R = Thr B3	1024:1033	Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro	721:1046	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	4	10	theme	1-R	827:829	arg1	A1					831:832	Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1	721:832	Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro	721:1046	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	3	11	theme	mass	605:608	arg1	spectrometry					610:621	FAB mass spectrometry	601:621	FAB mass spectrometry	601:621	Structural determination was done using one- and two-dimensional 500 MHz 1H-NMR spectroscopy and FAB mass spectrometry of native and derivatized glycopeptides.
2775488	4	12	theme	beta	936:939	arg1	beta					982:985	Neu5Ac alpha 2-3-Gal beta 1-3	961:989	Neu5Ac alpha 2-3-Gal beta 1-3	961:989	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	4	12	theme	beta	936:939	arg1	beta					951:954	Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6	721:958	Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro	721:1046	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	4	13	theme	following	668:676	arg1	structures					678:687	The following structures	664:687	The following structures	664:687	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	1	14	theme	alpha-N-acetylgalactosaminidase	362:392	arg1	activity					394:401	alpha-N-acetylgalactosaminidase activity	362:401	alpha-N-acetylgalactosaminidase activity	362:401	Glycopeptides have been isolated from the urine of two patients, aged 5 and 6, with a new lysosomal storage disease characterized by a deficiency in alpha-N-acetylgalactosaminidase activity.
2775488	4	15	dep	inferred	694:701	arg1	B1					1009:1010	Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1	721:1010	Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro	721:1046	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	4	16	theme	alpha	774:778	arg1	beta					787:790	(3) Neu5Ac alpha 2-3Gal beta 1-3	763:794	(3) Neu5Ac alpha 2-3Gal beta 1-3	763:794	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	4	17	theme	GalNAc	992:997	arg1	B1					1009:1010	Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1	721:1010	Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro	721:1046	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	0	18	from	deficiency	157:166	arg1	activity					203:210	alpha-N-acetylgalactosaminidase activity	171:210	alpha-N-acetylgalactosaminidase activity	171:210	Isolation and structural characterization of sialic-acid-containing glycopeptides of the O-glycosidic type from the urine of two patients with an hereditary deficiency in alpha-N-acetylgalactosaminidase activity.
2775488	2	19	gly	glycopeptides	423:435	arg2	glycopeptides					423:435	these glycopeptides	417:435	these glycopeptides	417:435	Isolation of these glycopeptides was achieved using gel filtration and ion-exchange chromatography.
2775488	1	20	from	deficiency	348:357	arg1	activity					394:401	alpha-N-acetylgalactosaminidase activity	362:401	alpha-N-acetylgalactosaminidase activity	362:401	Glycopeptides have been isolated from the urine of two patients, aged 5 and 6, with a new lysosomal storage disease characterized by a deficiency in alpha-N-acetylgalactosaminidase activity.
2775488	4	21	theme	Thr	1028:1030	arg1	B3					1032:1033	R = Thr B3	1024:1033	Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro	721:1046	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	3	22	theme	FAB	601:603	arg1	spectrometry					610:621	FAB mass spectrometry	601:621	FAB mass spectrometry	601:621	Structural determination was done using one- and two-dimensional 500 MHz 1H-NMR spectroscopy and FAB mass spectrometry of native and derivatized glycopeptides.
2775488	4	23	theme	1-R	1005:1007	arg1	B1					1009:1010	Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1	721:1010	Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro	721:1046	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	2	24	theme	glycopeptides	423:435	arg1	Isolation					404:412	Isolation	404:412	Isolation of these glycopeptides	404:435	Isolation of these glycopeptides was achieved using gel filtration and ion-exchange chromatography.
2775488	4	25	theme	A	734:734	arg1	A1					831:832	Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1	721:832	Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro	721:1046	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	4	26	theme	alpha	999:1003	arg1	B1					1009:1010	Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1	721:1010	Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro	721:1046	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	4	27	theme	Glycopeptide	871:882	arg1	B					884:884	Thr-Pro Glycopeptide B	863:884	Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)	863:910	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	4	27	theme	Glycopeptide	871:882	arg1	urine					901:905	up to 80 mg/l urine	887:905	up to 80 mg/l urine	887:905	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	4	27	theme	Glycopeptide	871:882	arg1	4					909:909	4	909:909	4	909:909	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	3	28	theme	derivatized	637:647	arg1	glycopeptides					649:661	native and derivatized glycopeptides	626:661	native and derivatized glycopeptides	626:661	Structural determination was done using one- and two-dimensional 500 MHz 1H-NMR spectroscopy and FAB mass spectrometry of native and derivatized glycopeptides.
2775488	4	29	theme	2-3-Gal	974:980	arg1	beta					982:985	Neu5Ac alpha 2-3-Gal beta 1-3	961:989	Neu5Ac alpha 2-3-Gal beta 1-3	961:989	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	4	29	theme	2-3-Gal	974:980	arg1	beta					951:954	Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6	721:958	Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro	721:1046	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	4	30	theme	Ser	839:841	arg1	A2					843:844	Ser A2	839:844	Ser A2	839:844	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	2	31	theme	ion-exchange	475:486	arg1	chromatography					488:501	ion-exchange chromatography	475:501	ion-exchange chromatography	475:501	Isolation of these glycopeptides was achieved using gel filtration and ion-exchange chromatography.
2775488	4	32	theme	alpha	821:825	arg1	A1					831:832	Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1	721:832	Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro	721:1046	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	4	33	theme	Neu5Ac	767:772	arg1	beta					787:790	(3) Neu5Ac alpha 2-3Gal beta 1-3	763:794	(3) Neu5Ac alpha 2-3Gal beta 1-3	763:794	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	4	34	theme	alpha	968:972	arg1	beta					982:985	Neu5Ac alpha 2-3-Gal beta 1-3	961:989	Neu5Ac alpha 2-3-Gal beta 1-3	961:989	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	4	34	theme	alpha	968:972	arg1	beta					951:954	Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6	721:958	Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro	721:1046	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	4	35	dep	140	743:745	arg1	to					740:741	to	740:741	to	740:741	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	0	36	theme	structural	14:23	arg1	characterization					25:40	structural characterization	14:40	structural characterization	14:40	Isolation and structural characterization of sialic-acid-containing glycopeptides of the O-glycosidic type from the urine of two patients with an hereditary deficiency in alpha-N-acetylgalactosaminidase activity.
2775488	4	37	dep	B1	1009:1010	arg1	B3					1032:1033	R = Thr B3	1024:1033	Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro	721:1046	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	4	37	dep	B1	1009:1010	arg1	B2					1021:1022	R = Ser B2	1013:1022	Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro	721:1046	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	4	37	dep	B1	1009:1010	arg1	Thr-Pro					1040:1046	R = Thr-Pro	1036:1046	Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro	721:1046	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	0	38	theme	patients	129:136	arg1	urine					116:120	the urine	112:120	the urine of two patients with an hereditary deficiency in alpha-N-acetylgalactosaminidase activity	112:210	Isolation and structural characterization of sialic-acid-containing glycopeptides of the O-glycosidic type from the urine of two patients with an hereditary deficiency in alpha-N-acetylgalactosaminidase activity.
2775488	3	39	theme	native	626:631	arg1	glycopeptides					649:661	native and derivatized glycopeptides	626:661	native and derivatized glycopeptides	626:661	Structural determination was done using one- and two-dimensional 500 MHz 1H-NMR spectroscopy and FAB mass spectrometry of native and derivatized glycopeptides.
2775488	2	40	theme	gel	456:458	arg1	filtration					460:469	gel filtration	456:469	gel filtration	456:469	Isolation of these glycopeptides was achieved using gel filtration and ion-exchange chromatography.
2775488	0	41	theme	sialic-acid-containing	45:66	arg1	glycopeptides					68:80	sialic-acid-containing glycopeptides	45:80	sialic-acid-containing glycopeptides of the O-glycosidic type	45:105	Isolation and structural characterization of sialic-acid-containing glycopeptides of the O-glycosidic type from the urine of two patients with an hereditary deficiency in alpha-N-acetylgalactosaminidase activity.
2775488	1	42	theme	new	299:301	arg1	disease					321:327	a new lysosomal storage disease	297:327	a new lysosomal storage disease characterized by a deficiency in alpha-N-acetylgalactosaminidase activity	297:401	Glycopeptides have been isolated from the urine of two patients, aged 5 and 6, with a new lysosomal storage disease characterized by a deficiency in alpha-N-acetylgalactosaminidase activity.
2775488	0	43	theme	hereditary	146:155	arg1	deficiency					157:166	an hereditary deficiency	143:166	an hereditary deficiency in alpha-N-acetylgalactosaminidase activity	143:210	Isolation and structural characterization of sialic-acid-containing glycopeptides of the O-glycosidic type from the urine of two patients with an hereditary deficiency in alpha-N-acetylgalactosaminidase activity.
2775488	4	44	theme	Glycopeptide	721:732	arg1	urine					752:756	up to 140 mg/l urine	737:756	up to 140 mg/l urine	737:756	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	4	44	theme	Glycopeptide	721:732	arg1	alpha					804:808	Neu5Ac alpha 2-6	797:812	Neu5Ac alpha 2-6	797:812	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	4	44	theme	Glycopeptide	721:732	arg1	A					734:734	Glycopeptide A	721:734	Glycopeptide A (up to 140 mg/l urine) (1)	721:761	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	4	44	theme	Glycopeptide	721:732	arg1	1					760:760	1	760:760	1	760:760	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	4	45	theme	GalNAc	814:819	arg1	A1					831:832	Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1	721:832	Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro	721:1046	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	4	46	theme	mg/l	896:899	arg1	B					884:884	Thr-Pro Glycopeptide B	863:884	Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)	863:910	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	4	46	theme	mg/l	896:899	arg1	urine					901:905	up to 80 mg/l urine	887:905	up to 80 mg/l urine	887:905	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	3	47	theme	Structural	504:513	arg1	determination					515:527	Structural determination	504:527	Structural determination	504:527	Structural determination was done using one- and two-dimensional 500 MHz 1H-NMR spectroscopy and FAB mass spectrometry of native and derivatized glycopeptides.
2775488	4	48	theme	mg/l	747:750	arg1	urine					752:756	up to 140 mg/l urine	737:756	up to 140 mg/l urine	737:756	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	4	48	theme	mg/l	747:750	arg1	A					734:734	Glycopeptide A	721:734	Glycopeptide A (up to 140 mg/l urine) (1)	721:761	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	1	49	theme	lysosomal	303:311	arg1	disease					321:327	a new lysosomal storage disease	297:327	a new lysosomal storage disease characterized by a deficiency in alpha-N-acetylgalactosaminidase activity	297:401	Glycopeptides have been isolated from the urine of two patients, aged 5 and 6, with a new lysosomal storage disease characterized by a deficiency in alpha-N-acetylgalactosaminidase activity.
2775488	4	50	theme	Thr-Pro	863:869	arg1	B					884:884	Thr-Pro Glycopeptide B	863:884	Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)	863:910	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	4	50	theme	Thr-Pro	863:869	arg1	urine					901:905	up to 80 mg/l urine	887:905	up to 80 mg/l urine	887:905	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	4	50	theme	Thr-Pro	863:869	arg1	4					909:909	4	909:909	4	909:909	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	4	51	theme	Neu5Ac	916:921	arg1	beta					982:985	Neu5Ac alpha 2-3-Gal beta 1-3	961:989	Neu5Ac alpha 2-3-Gal beta 1-3	961:989	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	4	51	theme	Neu5Ac	916:921	arg1	beta					951:954	Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6	721:958	Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro	721:1046	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	3	52	gly	glycopeptides	649:661	arg2	glycopeptides					649:661	native and derivatized glycopeptides	626:661	native and derivatized glycopeptides	626:661	Structural determination was done using one- and two-dimensional 500 MHz 1H-NMR spectroscopy and FAB mass spectrometry of native and derivatized glycopeptides.
2775488	1	53	theme	storage	313:319	arg1	disease					321:327	a new lysosomal storage disease	297:327	a new lysosomal storage disease characterized by a deficiency in alpha-N-acetylgalactosaminidase activity	297:401	Glycopeptides have been isolated from the urine of two patients, aged 5 and 6, with a new lysosomal storage disease characterized by a deficiency in alpha-N-acetylgalactosaminidase activity.
2775488	4	54	theme	Thr	851:853	arg1	A3					855:856	Thr A3	851:856	Thr A3	851:856	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	3	55	theme	glycopeptides	649:661	arg1	spectrometry					610:621	FAB mass spectrometry	601:621	FAB mass spectrometry	601:621	Structural determination was done using one- and two-dimensional 500 MHz 1H-NMR spectroscopy and FAB mass spectrometry of native and derivatized glycopeptides.
2775488	3	55	theme	glycopeptides	649:661	arg1	spectroscopy					584:595	500 MHz 1H-NMR spectroscopy	569:595	500 MHz 1H-NMR spectroscopy	569:595	Structural determination was done using one- and two-dimensional 500 MHz 1H-NMR spectroscopy and FAB mass spectrometry of native and derivatized glycopeptides.
2775488	4	56	theme	Ser	1017:1019	arg1	B2					1021:1022	R = Ser B2	1013:1022	Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro	721:1046	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	0	57	theme	glycopeptides	68:80	arg1	Isolation					0:8	Isolation	0:8	Isolation	0:8	Isolation and structural characterization of sialic-acid-containing glycopeptides of the O-glycosidic type from the urine of two patients with an hereditary deficiency in alpha-N-acetylgalactosaminidase activity.
2775488	0	57	theme	glycopeptides	68:80	arg1	characterization					25:40	structural characterization	14:40	structural characterization	14:40	Isolation and structural characterization of sialic-acid-containing glycopeptides of the O-glycosidic type from the urine of two patients with an hereditary deficiency in alpha-N-acetylgalactosaminidase activity.
2775488	4	58	theme	A1	831:832	arg1	beta					982:985	Neu5Ac alpha 2-3-Gal beta 1-3	961:989	Neu5Ac alpha 2-3-Gal beta 1-3	961:989	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	4	58	theme	A1	831:832	arg1	beta					951:954	Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6	721:958	Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro	721:1046	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	4	59	theme	R	1024:1024	arg1	B3					1032:1033	R = Thr B3	1024:1033	Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro	721:1046	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	3	60	theme	two-dimensional	553:567	arg1	spectroscopy					584:595	500 MHz 1H-NMR spectroscopy	569:595	500 MHz 1H-NMR spectroscopy	569:595	Structural determination was done using one- and two-dimensional 500 MHz 1H-NMR spectroscopy and FAB mass spectrometry of native and derivatized glycopeptides.
2775488	4	61	dep	beta	787:790	arg1	3					764:764	3	764:764	3	764:764	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	1	62	attach	isolated	237:244	arg2	Glycopeptides					213:225	Glycopeptides	213:225	Glycopeptides	213:225	Glycopeptides have been isolated from the urine of two patients, aged 5 and 6, with a new lysosomal storage disease characterized by a deficiency in alpha-N-acetylgalactosaminidase activity.
2775488	1	62	attach	isolated	237:244	arg1	urine					255:259	the urine	251:259	the urine of two patients, aged 5 and 6, with a new lysosomal storage disease characterized by a deficiency in alpha-N-acetylgalactosaminidase activity	251:401	Glycopeptides have been isolated from the urine of two patients, aged 5 and 6, with a new lysosomal storage disease characterized by a deficiency in alpha-N-acetylgalactosaminidase activity.
2775488	4	63	theme	Neu5Ac	797:802	arg1	alpha					804:808	Neu5Ac alpha 2-6	797:812	Neu5Ac alpha 2-6	797:812	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	4	63	theme	Neu5Ac	797:802	arg1	A					734:734	Glycopeptide A	721:734	Glycopeptide A (up to 140 mg/l urine) (1)	721:761	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	4	64	theme	R	1036:1036	arg1	Thr-Pro					1040:1046	R = Thr-Pro	1036:1046	Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro	721:1046	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	4	65	theme	beta	951:954	arg1	B1					1009:1010	Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1	721:1010	Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro	721:1046	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	0	66	theme	alpha-N-acetylgalactosaminidase	171:201	arg1	activity					203:210	alpha-N-acetylgalactosaminidase activity	171:210	alpha-N-acetylgalactosaminidase activity	171:210	Isolation and structural characterization of sialic-acid-containing glycopeptides of the O-glycosidic type from the urine of two patients with an hereditary deficiency in alpha-N-acetylgalactosaminidase activity.
2775488	1	67	dep	aged	278:281	arg1	5					283:283	5	283:283	5	283:283	Glycopeptides have been isolated from the urine of two patients, aged 5 and 6, with a new lysosomal storage disease characterized by a deficiency in alpha-N-acetylgalactosaminidase activity.
2775488	1	67	dep	aged	278:281	arg1	6					289:289	6	289:289	6	289:289	Glycopeptides have been isolated from the urine of two patients, aged 5 and 6, with a new lysosomal storage disease characterized by a deficiency in alpha-N-acetylgalactosaminidase activity.
2775488	4	68	theme	2-3Gal	780:785	arg1	beta					787:790	(3) Neu5Ac alpha 2-3Gal beta 1-3	763:794	(3) Neu5Ac alpha 2-3Gal beta 1-3	763:794	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	1	69	with	patients	268:275	arg1	disease					321:327	a new lysosomal storage disease	297:327	a new lysosomal storage disease characterized by a deficiency in alpha-N-acetylgalactosaminidase activity	297:401	Glycopeptides have been isolated from the urine of two patients, aged 5 and 6, with a new lysosomal storage disease characterized by a deficiency in alpha-N-acetylgalactosaminidase activity.
2775488	3	70	theme	one-	544:547	arg1	spectroscopy					584:595	500 MHz 1H-NMR spectroscopy	569:595	500 MHz 1H-NMR spectroscopy	569:595	Structural determination was done using one- and two-dimensional 500 MHz 1H-NMR spectroscopy and FAB mass spectrometry of native and derivatized glycopeptides.
2775488	4	71	theme	Neu5Ac	961:966	arg1	beta					982:985	Neu5Ac alpha 2-3-Gal beta 1-3	961:989	Neu5Ac alpha 2-3-Gal beta 1-3	961:989	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	4	71	theme	Neu5Ac	961:966	arg1	beta					951:954	Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6	721:958	Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro	721:1046	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	0	72	theme	O-glycosidic	89:100	arg1	type					102:105	the O-glycosidic type	85:105	the O-glycosidic type	85:105	Isolation and structural characterization of sialic-acid-containing glycopeptides of the O-glycosidic type from the urine of two patients with an hereditary deficiency in alpha-N-acetylgalactosaminidase activity.
2775488	4	73	dep	80	893:894	arg1	to					890:891	to	890:891	to	890:891	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	0	74	gly	glycopeptides	68:80	arg1	type					102:105	the O-glycosidic type	85:105	the O-glycosidic type	85:105	Isolation and structural characterization of sialic-acid-containing glycopeptides of the O-glycosidic type from the urine of two patients with an hereditary deficiency in alpha-N-acetylgalactosaminidase activity.
2775488	0	74	gly	glycopeptides	68:80	arg2	glycopeptides					68:80	sialic-acid-containing glycopeptides	45:80	sialic-acid-containing glycopeptides of the O-glycosidic type	45:105	Isolation and structural characterization of sialic-acid-containing glycopeptides of the O-glycosidic type from the urine of two patients with an hereditary deficiency in alpha-N-acetylgalactosaminidase activity.
2775488	3	75	theme	1H-NMR	577:582	arg1	spectroscopy					584:595	500 MHz 1H-NMR spectroscopy	569:595	500 MHz 1H-NMR spectroscopy	569:595	Structural determination was done using one- and two-dimensional 500 MHz 1H-NMR spectroscopy and FAB mass spectrometry of native and derivatized glycopeptides.
2775488	0	76	with	patients	129:136	arg1	deficiency					157:166	an hereditary deficiency	143:166	an hereditary deficiency in alpha-N-acetylgalactosaminidase activity	143:210	Isolation and structural characterization of sialic-acid-containing glycopeptides of the O-glycosidic type from the urine of two patients with an hereditary deficiency in alpha-N-acetylgalactosaminidase activity.
2775488	1	77	theme	patients	268:275	arg1	urine					255:259	the urine	251:259	the urine of two patients, aged 5 and 6, with a new lysosomal storage disease characterized by a deficiency in alpha-N-acetylgalactosaminidase activity	251:401	Glycopeptides have been isolated from the urine of two patients, aged 5 and 6, with a new lysosomal storage disease characterized by a deficiency in alpha-N-acetylgalactosaminidase activity.
2775488	4	78	dep	A1	831:832	arg1	=					837:837	=	837:837	= Ser A2	837:844	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	4	79	theme	=	1015:1015	arg1	B2					1021:1022	R = Ser B2	1013:1022	Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro	721:1046	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	4	80	theme	beta	787:790	arg1	A1					831:832	Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1	721:832	Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro	721:1046	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	4	81	theme	2-3Gal	929:934	arg1	beta					982:985	Neu5Ac alpha 2-3-Gal beta 1-3	961:989	Neu5Ac alpha 2-3-Gal beta 1-3	961:989	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2775488	4	81	theme	2-3Gal	929:934	arg1	beta					951:954	Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6	721:958	Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro	721:1046	The following structures were inferred as being present: Glycopeptide A (up to 140 mg/l urine) (1)-(3) Neu5Ac alpha 2-3Gal beta 1-3 (Neu5Ac alpha 2-6)GalNAc alpha 1-R A1: R = Ser A2: R = Thr A3: R = Thr-Pro Glycopeptide B (up to 80 mg/l urine) (4)-(6) Neu5Ac alpha 2-3Gal beta 1-4GlcNAc beta 1-6 (Neu5Ac alpha 2-3-Gal beta 1-3) GalNAc alpha 1-R B1: R = Ser B2:R = Thr B3: R = Thr-Pro
2971663	4	0	theme	resting	930:936	arg1	cells					938:942	resting cells	930:942	resting cells	930:942	The radical shift in the biosynthetic pathway of O-glycans in activated T-lymphocytes compared to resting cells is apparently caused by a decrease of alpha 2----6 sialyltransferase activity and by the parallel dramatic stimulation of the beta 1----6GlcNAc-transferase.
2971663	2	1	from	changes	425:431	arg1	structures					453:462	the carbohydrate structures	436:462	the carbohydrate structures	436:462	Both forms of the sialoglycoprotein were identified as leukosialin by a monospecific antiserum, and the differences in molecular weight were found to be due to changes in the carbohydrate structures.
2971663	5	2	theme	coordinate	1166:1175	arg1	responsible					1221:1231	responsible	1221:1231	responsible	1221:1231	Since both enzymes compete for the same precursor substrate, the coordinate changes in their activities are most likely responsible for the complete change of the carbohydrate structures on leukosialin during the activation of human T-lymphocytes.
2971663	5	2	theme	coordinate	1166:1175	arg1	changes					1177:1183	the coordinate changes	1162:1183	the coordinate changes in their activities	1162:1203	Since both enzymes compete for the same precursor substrate, the coordinate changes in their activities are most likely responsible for the complete change of the carbohydrate structures on leukosialin during the activation of human T-lymphocytes.
2971663	5	3	theme	structures	1277:1286	arg1	change					1250:1255	the complete change	1237:1255	the complete change of the carbohydrate structures on leukosialin during the activation of human T-lymphocytes	1237:1346	Since both enzymes compete for the same precursor substrate, the coordinate changes in their activities are most likely responsible for the complete change of the carbohydrate structures on leukosialin during the activation of human T-lymphocytes.
2971663	4	4	theme	dramatic	1042:1049	arg1	stimulation					1051:1061	the parallel dramatic stimulation	1029:1061	the parallel dramatic stimulation of the beta 1----6GlcNAc-transferase	1029:1098	The radical shift in the biosynthetic pathway of O-glycans in activated T-lymphocytes compared to resting cells is apparently caused by a decrease of alpha 2----6 sialyltransferase activity and by the parallel dramatic stimulation of the beta 1----6GlcNAc-transferase.
2971663	3	5	theme	alpha	735:739	arg1	beta					751:754	NeuNAc alpha 2----3Gal beta 1----3	728:761	NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6)	728:815	Our results suggest that resting T-lymphocytes express on leukosialin the disialotetrasaccharides NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)Gal-NAc-Ser/Thr, whereas activated human T-cells carry on leukosialin exclusively the more complex structures NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6)GalNAc-Ser/Thr.
2971663	3	5	theme	alpha	735:739	arg1	beta					804:807	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	763:814	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	763:814	Our results suggest that resting T-lymphocytes express on leukosialin the disialotetrasaccharides NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)Gal-NAc-Ser/Thr, whereas activated human T-cells carry on leukosialin exclusively the more complex structures NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6)GalNAc-Ser/Thr.
2971663	4	6	theme	activity	1013:1020	arg1	decrease					970:977	a decrease	968:977	a decrease of alpha 2----6 sialyltransferase activity	968:1020	The radical shift in the biosynthetic pathway of O-glycans in activated T-lymphocytes compared to resting cells is apparently caused by a decrease of alpha 2----6 sialyltransferase activity and by the parallel dramatic stimulation of the beta 1----6GlcNAc-transferase.
2971663	3	7	theme	2----3Gal	741:749	arg1	beta					751:754	NeuNAc alpha 2----3Gal beta 1----3	728:761	NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6)	728:815	Our results suggest that resting T-lymphocytes express on leukosialin the disialotetrasaccharides NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)Gal-NAc-Ser/Thr, whereas activated human T-cells carry on leukosialin exclusively the more complex structures NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6)GalNAc-Ser/Thr.
2971663	3	7	theme	2----3Gal	741:749	arg1	beta					804:807	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	763:814	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	763:814	Our results suggest that resting T-lymphocytes express on leukosialin the disialotetrasaccharides NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)Gal-NAc-Ser/Thr, whereas activated human T-cells carry on leukosialin exclusively the more complex structures NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6)GalNAc-Ser/Thr.
2971663	3	8	theme	beta	586:589	arg1	Gal-NAc-Ser/Thr					618:632	the disialotetrasaccharides NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)Gal-NAc-Ser/Thr	535:632	leukosialin the disialotetrasaccharides NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)Gal-NAc-Ser/Thr	523:632	Our results suggest that resting T-lymphocytes express on leukosialin the disialotetrasaccharides NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)Gal-NAc-Ser/Thr, whereas activated human T-cells carry on leukosialin exclusively the more complex structures NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6)GalNAc-Ser/Thr.
2971663	1	9	from	increase	182:189	arg1	weight					213:218	apparent molecular weight	194:218	apparent molecular weight of the major cell-surface sialoglycoprotein	194:262	The activation of human T-lymphocytes by anti-CD3 antibodies and interleukin-2 results in a marked increase in apparent molecular weight of the major cell-surface sialoglycoprotein.
2971663	3	10	dep	leukosialin	523:533	arg1	Gal-NAc-Ser/Thr					618:632	the disialotetrasaccharides NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)Gal-NAc-Ser/Thr	535:632	leukosialin the disialotetrasaccharides NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)Gal-NAc-Ser/Thr	523:632	Our results suggest that resting T-lymphocytes express on leukosialin the disialotetrasaccharides NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)Gal-NAc-Ser/Thr, whereas activated human T-cells carry on leukosialin exclusively the more complex structures NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6)GalNAc-Ser/Thr.
2971663	3	11	theme	alpha	770:774	arg1	beta					804:807	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	763:814	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	763:814	Our results suggest that resting T-lymphocytes express on leukosialin the disialotetrasaccharides NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)Gal-NAc-Ser/Thr, whereas activated human T-cells carry on leukosialin exclusively the more complex structures NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6)GalNAc-Ser/Thr.
2971663	3	11	theme	alpha	770:774	arg1	beta					751:754	NeuNAc alpha 2----3Gal beta 1----3	728:761	NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6)	728:815	Our results suggest that resting T-lymphocytes express on leukosialin the disialotetrasaccharides NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)Gal-NAc-Ser/Thr, whereas activated human T-cells carry on leukosialin exclusively the more complex structures NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6)GalNAc-Ser/Thr.
2971663	5	12	theme	human	1328:1332	arg1	T-lymphocytes					1334:1346	human T-lymphocytes	1328:1346	human T-lymphocytes	1328:1346	Since both enzymes compete for the same precursor substrate, the coordinate changes in their activities are most likely responsible for the complete change of the carbohydrate structures on leukosialin during the activation of human T-lymphocytes.
2971663	2	13	gly	sialoglycoprotein	283:299	arg1	sialoglycoprotein					283:299	the sialoglycoprotein	279:299	the sialoglycoprotein	279:299	Both forms of the sialoglycoprotein were identified as leukosialin by a monospecific antiserum, and the differences in molecular weight were found to be due to changes in the carbohydrate structures.
2971663	0	14	from	changes	49:55	arg1	biosynthesis					69:80	O-glycan biosynthesis	60:80	O-glycan biosynthesis	60:80	Human T-lymphocyte activation is associated with changes in O-glycan biosynthesis.
2971663	4	15	theme	activated	894:902	arg1	T-lymphocytes					904:916	activated T-lymphocytes	894:916	activated T-lymphocytes	894:916	The radical shift in the biosynthetic pathway of O-glycans in activated T-lymphocytes compared to resting cells is apparently caused by a decrease of alpha 2----6 sialyltransferase activity and by the parallel dramatic stimulation of the beta 1----6GlcNAc-transferase.
2971663	1	16	gly	sialoglycoprotein	246:262	arg1	sialoglycoprotein					246:262	the major cell-surface sialoglycoprotein	223:262	the major cell-surface sialoglycoprotein	223:262	The activation of human T-lymphocytes by anti-CD3 antibodies and interleukin-2 results in a marked increase in apparent molecular weight of the major cell-surface sialoglycoprotein.
2971663	3	17	theme	alpha	570:574	arg1	beta					586:589	disialotetrasaccharides NeuNAc alpha 2----3Gal beta 1----3	539:596	leukosialin the disialotetrasaccharides NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)Gal-NAc-Ser/Thr	523:632	Our results suggest that resting T-lymphocytes express on leukosialin the disialotetrasaccharides NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)Gal-NAc-Ser/Thr, whereas activated human T-cells carry on leukosialin exclusively the more complex structures NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6)GalNAc-Ser/Thr.
2971663	3	17	theme	alpha	570:574	arg1	alpha					605:609	NeuNAc alpha 2----6	598:616	NeuNAc alpha 2----6	598:616	Our results suggest that resting T-lymphocytes express on leukosialin the disialotetrasaccharides NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)Gal-NAc-Ser/Thr, whereas activated human T-cells carry on leukosialin exclusively the more complex structures NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6)GalNAc-Ser/Thr.
2971663	1	18	theme	marked	175:180	arg1	increase					182:189	a marked increase	173:189	a marked increase in apparent molecular weight of the major cell-surface sialoglycoprotein	173:262	The activation of human T-lymphocytes by anti-CD3 antibodies and interleukin-2 results in a marked increase in apparent molecular weight of the major cell-surface sialoglycoprotein.
2971663	2	19	theme	sialoglycoprotein	283:299	arg1	forms					270:274	Both forms	265:274	Both forms of the sialoglycoprotein	265:299	Both forms of the sialoglycoprotein were identified as leukosialin by a monospecific antiserum, and the differences in molecular weight were found to be due to changes in the carbohydrate structures.
2971663	2	19	theme	sialoglycoprotein	283:299	arg1	leukosialin					320:330	leukosialin	320:330	leukosialin	320:330	Both forms of the sialoglycoprotein were identified as leukosialin by a monospecific antiserum, and the differences in molecular weight were found to be due to changes in the carbohydrate structures.
2971663	0	20	theme	T-lymphocyte	6:17	arg1	activation					19:28	Human T-lymphocyte activation	0:28	Human T-lymphocyte activation	0:28	Human T-lymphocyte activation is associated with changes in O-glycan biosynthesis.
2971663	3	21	theme	NeuNAc	763:768	arg1	beta					804:807	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	763:814	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	763:814	Our results suggest that resting T-lymphocytes express on leukosialin the disialotetrasaccharides NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)Gal-NAc-Ser/Thr, whereas activated human T-cells carry on leukosialin exclusively the more complex structures NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6)GalNAc-Ser/Thr.
2971663	3	21	theme	NeuNAc	763:768	arg1	beta					751:754	NeuNAc alpha 2----3Gal beta 1----3	728:761	NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6)	728:815	Our results suggest that resting T-lymphocytes express on leukosialin the disialotetrasaccharides NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)Gal-NAc-Ser/Thr, whereas activated human T-cells carry on leukosialin exclusively the more complex structures NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6)GalNAc-Ser/Thr.
2971663	5	22	from	change	1250:1255	arg1	leukosialin					1291:1301	leukosialin	1291:1301	leukosialin during the activation of human T-lymphocytes	1291:1346	Since both enzymes compete for the same precursor substrate, the coordinate changes in their activities are most likely responsible for the complete change of the carbohydrate structures on leukosialin during the activation of human T-lymphocytes.
2971663	2	23	from	differences	369:379	arg1	weight					394:399	molecular weight	384:399	molecular weight	384:399	Both forms of the sialoglycoprotein were identified as leukosialin by a monospecific antiserum, and the differences in molecular weight were found to be due to changes in the carbohydrate structures.
2971663	2	24	theme	monospecific	337:348	arg1	antiserum					350:358	a monospecific antiserum	335:358	a monospecific antiserum	335:358	Both forms of the sialoglycoprotein were identified as leukosialin by a monospecific antiserum, and the differences in molecular weight were found to be due to changes in the carbohydrate structures.
2971663	3	25	theme	2----3Gal	776:784	arg1	beta					804:807	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	763:814	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	763:814	Our results suggest that resting T-lymphocytes express on leukosialin the disialotetrasaccharides NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)Gal-NAc-Ser/Thr, whereas activated human T-cells carry on leukosialin exclusively the more complex structures NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6)GalNAc-Ser/Thr.
2971663	3	25	theme	2----3Gal	776:784	arg1	beta					751:754	NeuNAc alpha 2----3Gal beta 1----3	728:761	NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6)	728:815	Our results suggest that resting T-lymphocytes express on leukosialin the disialotetrasaccharides NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)Gal-NAc-Ser/Thr, whereas activated human T-cells carry on leukosialin exclusively the more complex structures NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6)GalNAc-Ser/Thr.
2971663	0	26	theme	Human	0:4	arg1	activation					19:28	Human T-lymphocyte activation	0:28	Human T-lymphocyte activation	0:28	Human T-lymphocyte activation is associated with changes in O-glycan biosynthesis.
2971663	3	27	theme	NeuNAc	598:603	arg1	beta					586:589	disialotetrasaccharides NeuNAc alpha 2----3Gal beta 1----3	539:596	leukosialin the disialotetrasaccharides NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)Gal-NAc-Ser/Thr	523:632	Our results suggest that resting T-lymphocytes express on leukosialin the disialotetrasaccharides NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)Gal-NAc-Ser/Thr, whereas activated human T-cells carry on leukosialin exclusively the more complex structures NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6)GalNAc-Ser/Thr.
2971663	3	27	theme	NeuNAc	598:603	arg1	alpha					605:609	NeuNAc alpha 2----6	598:616	NeuNAc alpha 2----6	598:616	Our results suggest that resting T-lymphocytes express on leukosialin the disialotetrasaccharides NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)Gal-NAc-Ser/Thr, whereas activated human T-cells carry on leukosialin exclusively the more complex structures NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6)GalNAc-Ser/Thr.
2971663	5	28	theme	same	1136:1139	arg1	substrate					1151:1159	the same precursor substrate	1132:1159	the same precursor substrate	1132:1159	Since both enzymes compete for the same precursor substrate, the coordinate changes in their activities are most likely responsible for the complete change of the carbohydrate structures on leukosialin during the activation of human T-lymphocytes.
2971663	1	29	theme	apparent	194:201	arg1	weight					213:218	apparent molecular weight	194:218	apparent molecular weight of the major cell-surface sialoglycoprotein	194:262	The activation of human T-lymphocytes by anti-CD3 antibodies and interleukin-2 results in a marked increase in apparent molecular weight of the major cell-surface sialoglycoprotein.
2971663	2	30	theme	carbohydrate	440:451	arg1	structures					453:462	the carbohydrate structures	436:462	the carbohydrate structures	436:462	Both forms of the sialoglycoprotein were identified as leukosialin by a monospecific antiserum, and the differences in molecular weight were found to be due to changes in the carbohydrate structures.
2971663	5	31	from	leukosialin	1291:1301	arg1	change					1250:1255	the complete change	1237:1255	the complete change of the carbohydrate structures on leukosialin during the activation of human T-lymphocytes	1237:1346	Since both enzymes compete for the same precursor substrate, the coordinate changes in their activities are most likely responsible for the complete change of the carbohydrate structures on leukosialin during the activation of human T-lymphocytes.
2971663	1	32	theme	human	101:105	arg1	T-lymphocytes					107:119	human T-lymphocytes	101:119	human T-lymphocytes	101:119	The activation of human T-lymphocytes by anti-CD3 antibodies and interleukin-2 results in a marked increase in apparent molecular weight of the major cell-surface sialoglycoprotein.
2971663	1	33	theme	molecular	203:211	arg1	weight					213:218	apparent molecular weight	194:218	apparent molecular weight of the major cell-surface sialoglycoprotein	194:262	The activation of human T-lymphocytes by anti-CD3 antibodies and interleukin-2 results in a marked increase in apparent molecular weight of the major cell-surface sialoglycoprotein.
2971663	5	34	from	changes	1177:1183	arg1	activities					1194:1203	their activities	1188:1203	their activities	1188:1203	Since both enzymes compete for the same precursor substrate, the coordinate changes in their activities are most likely responsible for the complete change of the carbohydrate structures on leukosialin during the activation of human T-lymphocytes.
2971663	3	35	theme	beta	786:789	arg1	beta					804:807	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	763:814	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	763:814	Our results suggest that resting T-lymphocytes express on leukosialin the disialotetrasaccharides NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)Gal-NAc-Ser/Thr, whereas activated human T-cells carry on leukosialin exclusively the more complex structures NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6)GalNAc-Ser/Thr.
2971663	3	35	theme	beta	786:789	arg1	beta					751:754	NeuNAc alpha 2----3Gal beta 1----3	728:761	NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6)	728:815	Our results suggest that resting T-lymphocytes express on leukosialin the disialotetrasaccharides NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)Gal-NAc-Ser/Thr, whereas activated human T-cells carry on leukosialin exclusively the more complex structures NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6)GalNAc-Ser/Thr.
2971663	3	36	dep	express	512:518	arg1	whereas					635:641	whereas	635:641	whereas	635:641	Our results suggest that resting T-lymphocytes express on leukosialin the disialotetrasaccharides NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)Gal-NAc-Ser/Thr, whereas activated human T-cells carry on leukosialin exclusively the more complex structures NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6)GalNAc-Ser/Thr.
2971663	5	37	theme	precursor	1141:1149	arg1	substrate					1151:1159	the same precursor substrate	1132:1159	the same precursor substrate	1132:1159	Since both enzymes compete for the same precursor substrate, the coordinate changes in their activities are most likely responsible for the complete change of the carbohydrate structures on leukosialin during the activation of human T-lymphocytes.
2971663	1	38	theme	T-lymphocytes	107:119	arg1	activation					87:96	The activation	83:96	The activation of human T-lymphocytes by anti-CD3 antibodies and interleukin-2	83:160	The activation of human T-lymphocytes by anti-CD3 antibodies and interleukin-2 results in a marked increase in apparent molecular weight of the major cell-surface sialoglycoprotein.
2971663	5	39	theme	carbohydrate	1264:1275	arg1	structures					1277:1286	the carbohydrate structures	1260:1286	the carbohydrate structures on leukosialin during the activation of human T-lymphocytes	1260:1346	Since both enzymes compete for the same precursor substrate, the coordinate changes in their activities are most likely responsible for the complete change of the carbohydrate structures on leukosialin during the activation of human T-lymphocytes.
2971663	3	40	theme	1----4GlcNAc	791:802	arg1	beta					804:807	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	763:814	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	763:814	Our results suggest that resting T-lymphocytes express on leukosialin the disialotetrasaccharides NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)Gal-NAc-Ser/Thr, whereas activated human T-cells carry on leukosialin exclusively the more complex structures NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6)GalNAc-Ser/Thr.
2971663	3	40	theme	1----4GlcNAc	791:802	arg1	beta					751:754	NeuNAc alpha 2----3Gal beta 1----3	728:761	NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6)	728:815	Our results suggest that resting T-lymphocytes express on leukosialin the disialotetrasaccharides NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)Gal-NAc-Ser/Thr, whereas activated human T-cells carry on leukosialin exclusively the more complex structures NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6)GalNAc-Ser/Thr.
2971663	4	41	theme	2----6	988:993	arg1	activity					1013:1020	alpha 2----6 sialyltransferase activity	982:1020	alpha 2----6 sialyltransferase activity	982:1020	The radical shift in the biosynthetic pathway of O-glycans in activated T-lymphocytes compared to resting cells is apparently caused by a decrease of alpha 2----6 sialyltransferase activity and by the parallel dramatic stimulation of the beta 1----6GlcNAc-transferase.
2971663	4	42	theme	alpha	982:986	arg1	activity					1013:1020	alpha 2----6 sialyltransferase activity	982:1020	alpha 2----6 sialyltransferase activity	982:1020	The radical shift in the biosynthetic pathway of O-glycans in activated T-lymphocytes compared to resting cells is apparently caused by a decrease of alpha 2----6 sialyltransferase activity and by the parallel dramatic stimulation of the beta 1----6GlcNAc-transferase.
2971663	5	43	from	structures	1277:1286	arg1	leukosialin					1291:1301	leukosialin	1291:1301	leukosialin during the activation of human T-lymphocytes	1291:1346	Since both enzymes compete for the same precursor substrate, the coordinate changes in their activities are most likely responsible for the complete change of the carbohydrate structures on leukosialin during the activation of human T-lymphocytes.
2971663	4	44	theme	biosynthetic	857:868	arg1	pathway					870:876	the biosynthetic pathway	853:876	the biosynthetic pathway of O-glycans in activated T-lymphocytes	853:916	The radical shift in the biosynthetic pathway of O-glycans in activated T-lymphocytes compared to resting cells is apparently caused by a decrease of alpha 2----6 sialyltransferase activity and by the parallel dramatic stimulation of the beta 1----6GlcNAc-transferase.
2971663	5	45	theme	complete	1241:1248	arg1	change					1250:1255	the complete change	1237:1255	the complete change of the carbohydrate structures on leukosialin during the activation of human T-lymphocytes	1237:1346	Since both enzymes compete for the same precursor substrate, the coordinate changes in their activities are most likely responsible for the complete change of the carbohydrate structures on leukosialin during the activation of human T-lymphocytes.
2971663	4	46	theme	1----6GlcNAc-transferase	1075:1098	arg1	stimulation					1051:1061	the parallel dramatic stimulation	1029:1061	the parallel dramatic stimulation of the beta 1----6GlcNAc-transferase	1029:1098	The radical shift in the biosynthetic pathway of O-glycans in activated T-lymphocytes compared to resting cells is apparently caused by a decrease of alpha 2----6 sialyltransferase activity and by the parallel dramatic stimulation of the beta 1----6GlcNAc-transferase.
2971663	4	47	theme	O-glycans	881:889	arg1	pathway					870:876	the biosynthetic pathway	853:876	the biosynthetic pathway of O-glycans in activated T-lymphocytes	853:916	The radical shift in the biosynthetic pathway of O-glycans in activated T-lymphocytes compared to resting cells is apparently caused by a decrease of alpha 2----6 sialyltransferase activity and by the parallel dramatic stimulation of the beta 1----6GlcNAc-transferase.
2971663	4	48	theme	beta	1070:1073	arg1	1----6GlcNAc-transferase					1075:1098	the beta 1----6GlcNAc-transferase	1066:1098	the beta 1----6GlcNAc-transferase	1066:1098	The radical shift in the biosynthetic pathway of O-glycans in activated T-lymphocytes compared to resting cells is apparently caused by a decrease of alpha 2----6 sialyltransferase activity and by the parallel dramatic stimulation of the beta 1----6GlcNAc-transferase.
2971663	4	49	from	pathway	870:876	arg1	T-lymphocytes					904:916	activated T-lymphocytes	894:916	activated T-lymphocytes	894:916	The radical shift in the biosynthetic pathway of O-glycans in activated T-lymphocytes compared to resting cells is apparently caused by a decrease of alpha 2----6 sialyltransferase activity and by the parallel dramatic stimulation of the beta 1----6GlcNAc-transferase.
2971663	1	50	theme	anti-CD3	124:131	arg1	antibodies					133:142	anti-CD3 antibodies	124:142	anti-CD3 antibodies	124:142	The activation of human T-lymphocytes by anti-CD3 antibodies and interleukin-2 results in a marked increase in apparent molecular weight of the major cell-surface sialoglycoprotein.
2971663	3	51	theme	GalNAc-Ser/Thr	816:829	arg1	structures					717:726	the more complex structures	700:726	the more complex structures NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6)GalNAc-Ser/Thr	700:829	Our results suggest that resting T-lymphocytes express on leukosialin the disialotetrasaccharides NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)Gal-NAc-Ser/Thr, whereas activated human T-cells carry on leukosialin exclusively the more complex structures NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6)GalNAc-Ser/Thr.
2971663	3	52	theme	NeuNAc	728:733	arg1	beta					751:754	NeuNAc alpha 2----3Gal beta 1----3	728:761	NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6)	728:815	Our results suggest that resting T-lymphocytes express on leukosialin the disialotetrasaccharides NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)Gal-NAc-Ser/Thr, whereas activated human T-cells carry on leukosialin exclusively the more complex structures NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6)GalNAc-Ser/Thr.
2971663	3	52	theme	NeuNAc	728:733	arg1	beta					804:807	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	763:814	NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6	763:814	Our results suggest that resting T-lymphocytes express on leukosialin the disialotetrasaccharides NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)Gal-NAc-Ser/Thr, whereas activated human T-cells carry on leukosialin exclusively the more complex structures NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6)GalNAc-Ser/Thr.
2971663	3	53	theme	resting	490:496	arg1	T-lymphocytes					498:510	resting T-lymphocytes	490:510	resting T-lymphocytes	490:510	Our results suggest that resting T-lymphocytes express on leukosialin the disialotetrasaccharides NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)Gal-NAc-Ser/Thr, whereas activated human T-cells carry on leukosialin exclusively the more complex structures NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6)GalNAc-Ser/Thr.
2971663	1	54	theme	major	227:231	arg1	sialoglycoprotein					246:262	the major cell-surface sialoglycoprotein	223:262	the major cell-surface sialoglycoprotein	223:262	The activation of human T-lymphocytes by anti-CD3 antibodies and interleukin-2 results in a marked increase in apparent molecular weight of the major cell-surface sialoglycoprotein.
2971663	3	55	theme	2----3Gal	576:584	arg1	beta					586:589	disialotetrasaccharides NeuNAc alpha 2----3Gal beta 1----3	539:596	leukosialin the disialotetrasaccharides NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)Gal-NAc-Ser/Thr	523:632	Our results suggest that resting T-lymphocytes express on leukosialin the disialotetrasaccharides NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)Gal-NAc-Ser/Thr, whereas activated human T-cells carry on leukosialin exclusively the more complex structures NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6)GalNAc-Ser/Thr.
2971663	3	55	theme	2----3Gal	576:584	arg1	alpha					605:609	NeuNAc alpha 2----6	598:616	NeuNAc alpha 2----6	598:616	Our results suggest that resting T-lymphocytes express on leukosialin the disialotetrasaccharides NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)Gal-NAc-Ser/Thr, whereas activated human T-cells carry on leukosialin exclusively the more complex structures NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6)GalNAc-Ser/Thr.
2971663	4	56	theme	radical	836:842	arg1	shift					844:848	The radical shift	832:848	The radical shift in the biosynthetic pathway of O-glycans in activated T-lymphocytes compared to resting cells	832:942	The radical shift in the biosynthetic pathway of O-glycans in activated T-lymphocytes compared to resting cells is apparently caused by a decrease of alpha 2----6 sialyltransferase activity and by the parallel dramatic stimulation of the beta 1----6GlcNAc-transferase.
2971663	3	57	theme	NeuNAc	563:568	arg1	beta					586:589	disialotetrasaccharides NeuNAc alpha 2----3Gal beta 1----3	539:596	leukosialin the disialotetrasaccharides NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)Gal-NAc-Ser/Thr	523:632	Our results suggest that resting T-lymphocytes express on leukosialin the disialotetrasaccharides NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)Gal-NAc-Ser/Thr, whereas activated human T-cells carry on leukosialin exclusively the more complex structures NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6)GalNAc-Ser/Thr.
2971663	3	57	theme	NeuNAc	563:568	arg1	alpha					605:609	NeuNAc alpha 2----6	598:616	NeuNAc alpha 2----6	598:616	Our results suggest that resting T-lymphocytes express on leukosialin the disialotetrasaccharides NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)Gal-NAc-Ser/Thr, whereas activated human T-cells carry on leukosialin exclusively the more complex structures NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6)GalNAc-Ser/Thr.
2971663	1	58	theme	cell-surface	233:244	arg1	sialoglycoprotein					246:262	the major cell-surface sialoglycoprotein	223:262	the major cell-surface sialoglycoprotein	223:262	The activation of human T-lymphocytes by anti-CD3 antibodies and interleukin-2 results in a marked increase in apparent molecular weight of the major cell-surface sialoglycoprotein.
2971663	4	59	theme	parallel	1033:1040	arg1	stimulation					1051:1061	the parallel dramatic stimulation	1029:1061	the parallel dramatic stimulation of the beta 1----6GlcNAc-transferase	1029:1098	The radical shift in the biosynthetic pathway of O-glycans in activated T-lymphocytes compared to resting cells is apparently caused by a decrease of alpha 2----6 sialyltransferase activity and by the parallel dramatic stimulation of the beta 1----6GlcNAc-transferase.
2971663	3	60	theme	complex	709:715	arg1	structures					717:726	the more complex structures	700:726	the more complex structures NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6)GalNAc-Ser/Thr	700:829	Our results suggest that resting T-lymphocytes express on leukosialin the disialotetrasaccharides NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)Gal-NAc-Ser/Thr, whereas activated human T-cells carry on leukosialin exclusively the more complex structures NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6)GalNAc-Ser/Thr.
2971663	3	61	theme	activated	643:651	arg1	T-cells					659:665	activated human T-cells	643:665	activated human T-cells	643:665	Our results suggest that resting T-lymphocytes express on leukosialin the disialotetrasaccharides NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)Gal-NAc-Ser/Thr, whereas activated human T-cells carry on leukosialin exclusively the more complex structures NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6)GalNAc-Ser/Thr.
2971663	3	62	theme	disialotetrasaccharides	539:561	arg1	beta					586:589	disialotetrasaccharides NeuNAc alpha 2----3Gal beta 1----3	539:596	leukosialin the disialotetrasaccharides NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)Gal-NAc-Ser/Thr	523:632	Our results suggest that resting T-lymphocytes express on leukosialin the disialotetrasaccharides NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)Gal-NAc-Ser/Thr, whereas activated human T-cells carry on leukosialin exclusively the more complex structures NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6)GalNAc-Ser/Thr.
2971663	3	62	theme	disialotetrasaccharides	539:561	arg1	alpha					605:609	NeuNAc alpha 2----6	598:616	NeuNAc alpha 2----6	598:616	Our results suggest that resting T-lymphocytes express on leukosialin the disialotetrasaccharides NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)Gal-NAc-Ser/Thr, whereas activated human T-cells carry on leukosialin exclusively the more complex structures NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6)GalNAc-Ser/Thr.
2971663	1	63	theme	sialoglycoprotein	246:262	arg1	weight					213:218	apparent molecular weight	194:218	apparent molecular weight of the major cell-surface sialoglycoprotein	194:262	The activation of human T-lymphocytes by anti-CD3 antibodies and interleukin-2 results in a marked increase in apparent molecular weight of the major cell-surface sialoglycoprotein.
2971663	0	64	theme	O-glycan	60:67	arg1	biosynthesis					69:80	O-glycan biosynthesis	60:80	O-glycan biosynthesis	60:80	Human T-lymphocyte activation is associated with changes in O-glycan biosynthesis.
2971663	3	65	theme	human	653:657	arg1	T-cells					659:665	activated human T-cells	643:665	activated human T-cells	643:665	Our results suggest that resting T-lymphocytes express on leukosialin the disialotetrasaccharides NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----6)Gal-NAc-Ser/Thr, whereas activated human T-cells carry on leukosialin exclusively the more complex structures NeuNAc alpha 2----3Gal beta 1----3(NeuNAc alpha 2----3Gal beta 1----4GlcNAc beta 1----6)GalNAc-Ser/Thr.
2971663	4	66	from	shift	844:848	arg1	pathway					870:876	the biosynthetic pathway	853:876	the biosynthetic pathway of O-glycans in activated T-lymphocytes	853:916	The radical shift in the biosynthetic pathway of O-glycans in activated T-lymphocytes compared to resting cells is apparently caused by a decrease of alpha 2----6 sialyltransferase activity and by the parallel dramatic stimulation of the beta 1----6GlcNAc-transferase.
2971663	2	67	theme	molecular	384:392	arg1	weight					394:399	molecular weight	384:399	molecular weight	384:399	Both forms of the sialoglycoprotein were identified as leukosialin by a monospecific antiserum, and the differences in molecular weight were found to be due to changes in the carbohydrate structures.
2971663	5	68	theme	T-lymphocytes	1334:1346	arg1	activation					1314:1323	the activation	1310:1323	the activation of human T-lymphocytes	1310:1346	Since both enzymes compete for the same precursor substrate, the coordinate changes in their activities are most likely responsible for the complete change of the carbohydrate structures on leukosialin during the activation of human T-lymphocytes.
2971663	4	69	theme	sialyltransferase	995:1011	arg1	activity					1013:1020	alpha 2----6 sialyltransferase activity	982:1020	alpha 2----6 sialyltransferase activity	982:1020	The radical shift in the biosynthetic pathway of O-glycans in activated T-lymphocytes compared to resting cells is apparently caused by a decrease of alpha 2----6 sialyltransferase activity and by the parallel dramatic stimulation of the beta 1----6GlcNAc-transferase.
1872812	2	0	theme	%	347:347	arg1	galactose					349:357	20% galactose	345:357	20% galactose	345:357	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	2	0	theme	%	347:347	arg1	acid					339:342	23% N-acetylneuraminic acid	316:342	23% N-acetylneuraminic acid	316:342	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	6	1	theme	major	1159:1163	arg1	portion					1165:1171	the major portion	1155:1171	the major portion of the carbohydrate moiety	1155:1198	C.d. shows that native galactoglycoprotein and all derivatives in aqueous buffer are predominantly random coil, suggesting that removal of a large number of electrostatic net charges, as well as the major portion of the carbohydrate moiety, does not alter the secondary structure of the polypeptide chain.
1872812	7	2	theme	electron	1387:1394	arg1	microscopy					1396:1405	electron microscopy	1387:1405	electron microscopy	1387:1405	Examination of the size and conformation of tungsten-shadowed galactoglycoprotein and asialo and agalacto derivatives by electron microscopy shows the size and conformation of all three preparations to be similar, with only minor differences in particle length and width.
1872812	7	3	theme	derivatives	1372:1382	arg1	size					1285:1288	size	1285:1288	size	1285:1288	Examination of the size and conformation of tungsten-shadowed galactoglycoprotein and asialo and agalacto derivatives by electron microscopy shows the size and conformation of all three preparations to be similar, with only minor differences in particle length and width.
1872812	7	3	theme	derivatives	1372:1382	arg1	conformation					1294:1305	conformation	1294:1305	conformation	1294:1305	Examination of the size and conformation of tungsten-shadowed galactoglycoprotein and asialo and agalacto derivatives by electron microscopy shows the size and conformation of all three preparations to be similar, with only minor differences in particle length and width.
1872812	6	4	theme	moiety	1193:1198	arg1	portion					1165:1171	the major portion	1155:1171	the major portion of the carbohydrate moiety	1155:1198	C.d. shows that native galactoglycoprotein and all derivatives in aqueous buffer are predominantly random coil, suggesting that removal of a large number of electrostatic net charges, as well as the major portion of the carbohydrate moiety, does not alter the secondary structure of the polypeptide chain.
1872812	6	4	theme	moiety	1193:1198	arg1	charges					1135:1141	electrostatic net charges	1117:1141	electrostatic net charges	1117:1141	C.d. shows that native galactoglycoprotein and all derivatives in aqueous buffer are predominantly random coil, suggesting that removal of a large number of electrostatic net charges, as well as the major portion of the carbohydrate moiety, does not alter the secondary structure of the polypeptide chain.
1872812	6	5	from	galactoglycoprotein	983:1001	arg1	buffer					1034:1039	aqueous buffer	1026:1039	aqueous buffer	1026:1039	C.d. shows that native galactoglycoprotein and all derivatives in aqueous buffer are predominantly random coil, suggesting that removal of a large number of electrostatic net charges, as well as the major portion of the carbohydrate moiety, does not alter the secondary structure of the polypeptide chain.
1872812	2	6	theme	plasma	282:287	arg1	Galactoglycoprotein					244:262	Galactoglycoprotein	244:262	Galactoglycoprotein	244:262	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	2	6	theme	plasma	282:287	arg1	carbohydrate					302:313	a unique human plasma protein [76% carbohydrate	267:313	a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine)	267:436	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	2	7	theme	[Schmid	565:571	arg1	Binette					597:603	Binette	597:603	Binette	597:603	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	2	7	theme	[Schmid	565:571	arg1	serine					535:540	serine	535:540	serine	535:540	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	6	8	theme	number	1107:1112	arg1	removal					1088:1094	removal	1088:1094	removal of a large number of electrostatic net charges, as well as the major portion of the carbohydrate moiety,	1088:1199	C.d. shows that native galactoglycoprotein and all derivatives in aqueous buffer are predominantly random coil, suggesting that removal of a large number of electrostatic net charges, as well as the major portion of the carbohydrate moiety, does not alter the secondary structure of the polypeptide chain.
1872812	2	9	theme	23	316:317	arg1	%					318:318	%	318:318	%	318:318	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	5	10	theme	acid	820:823	arg1	residues					789:796	sequential residues	778:796	sequential residues of N-acetylneuraminic acid, galactose, N-acetylglucosamine, a second galactose and N-acetylgalactosamine	778:901	Highly purified exoglycosidases with well-defined specificities were used to prepare five derivatives of galactoglycoprotein in which sequential residues of N-acetylneuraminic acid, galactose, N-acetylglucosamine, a second galactose and N-acetylgalactosamine were removed with 83% of the total carbohydrate cleaved.
1872812	5	10	theme	acid	820:823	arg1	acid					820:823	N-acetylneuraminic acid	801:823	N-acetylneuraminic acid	801:823	Highly purified exoglycosidases with well-defined specificities were used to prepare five derivatives of galactoglycoprotein in which sequential residues of N-acetylneuraminic acid, galactose, N-acetylglucosamine, a second galactose and N-acetylgalactosamine were removed with 83% of the total carbohydrate cleaved.
1872812	2	11	theme	residues	510:517	arg1	chain					480:484	a single polypeptide chain	459:484	a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol	459:618	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	2	11	theme	residues	510:517	arg1	polypeptide					446:456	24% polypeptide	442:456	24% polypeptide	442:456	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	7	12	gly	galactoglycoprotein	1328:1346	arg1	galactoglycoprotein					1328:1346	galactoglycoprotein	1328:1346	galactoglycoprotein	1328:1346	Examination of the size and conformation of tungsten-shadowed galactoglycoprotein and asialo and agalacto derivatives by electron microscopy shows the size and conformation of all three preparations to be similar, with only minor differences in particle length and width.
1872812	2	13	theme	amino	499:503	arg1	residues					510:517	about 200 amino acid residues	489:517	about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol	489:618	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	7	14	theme	tungsten-shadowed	1310:1326	arg1	derivatives					1372:1382	tungsten-shadowed galactoglycoprotein and asialo and agalacto derivatives	1310:1382	tungsten-shadowed galactoglycoprotein and asialo and agalacto derivatives	1310:1382	Examination of the size and conformation of tungsten-shadowed galactoglycoprotein and asialo and agalacto derivatives by electron microscopy shows the size and conformation of all three preparations to be similar, with only minor differences in particle length and width.
1872812	2	15	gly	Galactoglycoprotein	244:262	arg1	Galactoglycoprotein					244:262	Galactoglycoprotein	244:262	Galactoglycoprotein	244:262	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	2	15	gly	Galactoglycoprotein	244:262	arg1	carbohydrate					302:313	a unique human plasma protein [76% carbohydrate	267:313	a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine)	267:436	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	6	16	theme	polypeptide	1247:1257	arg1	chain					1259:1263	the polypeptide chain	1243:1263	the polypeptide chain	1243:1263	C.d. shows that native galactoglycoprotein and all derivatives in aqueous buffer are predominantly random coil, suggesting that removal of a large number of electrostatic net charges, as well as the major portion of the carbohydrate moiety, does not alter the secondary structure of the polypeptide chain.
1872812	5	17	theme	sequential	778:787	arg1	residues					789:796	sequential residues	778:796	sequential residues of N-acetylneuraminic acid, galactose, N-acetylglucosamine, a second galactose and N-acetylgalactosamine	778:901	Highly purified exoglycosidases with well-defined specificities were used to prepare five derivatives of galactoglycoprotein in which sequential residues of N-acetylneuraminic acid, galactose, N-acetylglucosamine, a second galactose and N-acetylgalactosamine were removed with 83% of the total carbohydrate cleaved.
1872812	5	17	theme	sequential	778:787	arg1	acid					820:823	N-acetylneuraminic acid	801:823	N-acetylneuraminic acid	801:823	Highly purified exoglycosidases with well-defined specificities were used to prepare five derivatives of galactoglycoprotein in which sequential residues of N-acetylneuraminic acid, galactose, N-acetylglucosamine, a second galactose and N-acetylgalactosamine were removed with 83% of the total carbohydrate cleaved.
1872812	7	18	theme	conformation	1294:1305	arg1	Examination					1266:1276	Examination	1266:1276	Examination of the size and conformation of tungsten-shadowed galactoglycoprotein and asialo and agalacto derivatives by electron microscopy	1266:1405	Examination of the size and conformation of tungsten-shadowed galactoglycoprotein and asialo and agalacto derivatives by electron microscopy shows the size and conformation of all three preparations to be similar, with only minor differences in particle length and width.
1872812	2	19	dep	Binette	597:603	arg1	Biol					615:618	Biol	615:618	Biol	615:618	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	7	20	theme	size	1285:1288	arg1	Examination					1266:1276	Examination	1266:1276	Examination of the size and conformation of tungsten-shadowed galactoglycoprotein and asialo and agalacto derivatives by electron microscopy	1266:1405	Examination of the size and conformation of tungsten-shadowed galactoglycoprotein and asialo and agalacto derivatives by electron microscopy shows the size and conformation of all three preparations to be similar, with only minor differences in particle length and width.
1872812	6	21	theme	secondary	1220:1228	arg1	structure					1230:1238	the secondary structure	1216:1238	the secondary structure of the polypeptide chain	1216:1263	C.d. shows that native galactoglycoprotein and all derivatives in aqueous buffer are predominantly random coil, suggesting that removal of a large number of electrostatic net charges, as well as the major portion of the carbohydrate moiety, does not alter the secondary structure of the polypeptide chain.
1872812	6	22	theme	charges	1135:1141	arg1	number					1107:1112	a large number	1099:1112	a large number of electrostatic net charges, as well as the major portion of the carbohydrate moiety,	1099:1199	C.d. shows that native galactoglycoprotein and all derivatives in aqueous buffer are predominantly random coil, suggesting that removal of a large number of electrostatic net charges, as well as the major portion of the carbohydrate moiety, does not alter the secondary structure of the polypeptide chain.
1872812	2	23	theme	single	461:466	arg1	chain					480:484	a single polypeptide chain	459:484	a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol	459:618	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	2	23	theme	single	461:466	arg1	polypeptide					446:456	24% polypeptide	442:456	24% polypeptide	442:456	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	5	24	theme	well-defined	681:692	arg1	specificities					694:706	well-defined specificities	681:706	well-defined specificities	681:706	Highly purified exoglycosidases with well-defined specificities were used to prepare five derivatives of galactoglycoprotein in which sequential residues of N-acetylneuraminic acid, galactose, N-acetylglucosamine, a second galactose and N-acetylgalactosamine were removed with 83% of the total carbohydrate cleaved.
1872812	2	25	theme	unique	269:274	arg1	Galactoglycoprotein					244:262	Galactoglycoprotein	244:262	Galactoglycoprotein	244:262	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	2	25	theme	unique	269:274	arg1	carbohydrate					302:313	a unique human plasma protein [76% carbohydrate	267:313	a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine)	267:436	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	0	26	theme	human	72:76	arg1	plasma					78:83	human plasma	72:83	human plasma	72:83	The effect of the carbohydrate moiety upon the size and conformation of human plasma galactoglycoprotein as judged by electron microscopy and circular dichroism.
1872812	2	27	theme	1	372:372	arg1	%					373:373	%	373:373	%	373:373	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	6	28	theme	aqueous	1026:1032	arg1	buffer					1034:1039	aqueous buffer	1026:1039	aqueous buffer	1026:1039	C.d. shows that native galactoglycoprotein and all derivatives in aqueous buffer are predominantly random coil, suggesting that removal of a large number of electrostatic net charges, as well as the major portion of the carbohydrate moiety, does not alter the secondary structure of the polypeptide chain.
1872812	2	29	from	serine	535:540	arg1	high					527:530	high	527:530	high	527:530	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	2	30	theme	29	386:387	arg1	%					388:388	%	388:388	%	388:388	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	6	31	theme	electrostatic	1117:1129	arg1	charges					1135:1141	electrostatic net charges	1117:1141	electrostatic net charges	1117:1141	C.d. shows that native galactoglycoprotein and all derivatives in aqueous buffer are predominantly random coil, suggesting that removal of a large number of electrostatic net charges, as well as the major portion of the carbohydrate moiety, does not alter the secondary structure of the polypeptide chain.
1872812	2	32	theme	%	444:444	arg1	chain					480:484	a single polypeptide chain	459:484	a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol	459:618	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	2	32	theme	%	444:444	arg1	polypeptide					446:456	24% polypeptide	442:456	24% polypeptide	442:456	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	2	33	from	threonine	546:554	arg1	high					527:530	high	527:530	high	527:530	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	0	34	theme	carbohydrate	18:29	arg1	moiety					31:36	the carbohydrate moiety	14:36	the carbohydrate moiety	14:36	The effect of the carbohydrate moiety upon the size and conformation of human plasma galactoglycoprotein as judged by electron microscopy and circular dichroism.
1872812	6	35	theme	native	976:981	arg1	coil					1066:1069	random coil	1059:1069	random coil	1059:1069	C.d. shows that native galactoglycoprotein and all derivatives in aqueous buffer are predominantly random coil, suggesting that removal of a large number of electrostatic net charges, as well as the major portion of the carbohydrate moiety, does not alter the secondary structure of the polypeptide chain.
1872812	6	35	theme	native	976:981	arg1	galactoglycoprotein					983:1001	native galactoglycoprotein	976:1001	native galactoglycoprotein	976:1001	C.d. shows that native galactoglycoprotein and all derivatives in aqueous buffer are predominantly random coil, suggesting that removal of a large number of electrostatic net charges, as well as the major portion of the carbohydrate moiety, does not alter the secondary structure of the polypeptide chain.
1872812	6	35	theme	native	976:981	arg1	derivatives					1011:1021	all derivatives	1007:1021	all derivatives in aqueous buffer	1007:1039	C.d. shows that native galactoglycoprotein and all derivatives in aqueous buffer are predominantly random coil, suggesting that removal of a large number of electrostatic net charges, as well as the major portion of the carbohydrate moiety, does not alter the secondary structure of the polypeptide chain.
1872812	2	36	theme	20	345:346	arg1	%					347:347	%	347:347	%	347:347	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	1	37	gly	glycoprotein	186:197	arg1	glycoprotein					186:197	a glycoprotein	184:197	a glycoprotein	184:197	Structural studies of a glycoprotein after stepwise enzymic carbohydrate removal.
1872812	1	38	theme	carbohydrate	222:233	arg1	removal					235:241	stepwise enzymic carbohydrate removal	205:241	stepwise enzymic carbohydrate removal	205:241	Structural studies of a glycoprotein after stepwise enzymic carbohydrate removal.
1872812	7	39	theme	preparations	1452:1463	arg1	size					1417:1420	size	1417:1420	size	1417:1420	Examination of the size and conformation of tungsten-shadowed galactoglycoprotein and asialo and agalacto derivatives by electron microscopy shows the size and conformation of all three preparations to be similar, with only minor differences in particle length and width.
1872812	7	39	theme	preparations	1452:1463	arg1	conformation					1426:1437	conformation	1426:1437	conformation	1426:1437	Examination of the size and conformation of tungsten-shadowed galactoglycoprotein and asialo and agalacto derivatives by electron microscopy shows the size and conformation of all three preparations to be similar, with only minor differences in particle length and width.
1872812	5	40	theme	total	932:936	arg1	carbohydrate					938:949	the total carbohydrate	928:949	the total carbohydrate cleaved	928:957	Highly purified exoglycosidases with well-defined specificities were used to prepare five derivatives of galactoglycoprotein in which sequential residues of N-acetylneuraminic acid, galactose, N-acetylglucosamine, a second galactose and N-acetylgalactosamine were removed with 83% of the total carbohydrate cleaved.
1872812	2	41	theme	3	360:360	arg1	%					361:361	%	361:361	%	361:361	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	5	42	used	used	713:716	arg2	exoglycosidases					660:674	Highly purified exoglycosidases	644:674	Highly purified exoglycosidases with well-defined specificities	644:706	Highly purified exoglycosidases with well-defined specificities were used to prepare five derivatives of galactoglycoprotein in which sequential residues of N-acetylneuraminic acid, galactose, N-acetylglucosamine, a second galactose and N-acetylgalactosamine were removed with 83% of the total carbohydrate cleaved.
1872812	6	43	theme	random	1059:1064	arg1	coil					1066:1069	random coil	1059:1069	random coil	1059:1069	C.d. shows that native galactoglycoprotein and all derivatives in aqueous buffer are predominantly random coil, suggesting that removal of a large number of electrostatic net charges, as well as the major portion of the carbohydrate moiety, does not alter the secondary structure of the polypeptide chain.
1872812	6	43	theme	random	1059:1064	arg1	galactoglycoprotein					983:1001	native galactoglycoprotein	976:1001	native galactoglycoprotein	976:1001	C.d. shows that native galactoglycoprotein and all derivatives in aqueous buffer are predominantly random coil, suggesting that removal of a large number of electrostatic net charges, as well as the major portion of the carbohydrate moiety, does not alter the secondary structure of the polypeptide chain.
1872812	6	43	theme	random	1059:1064	arg1	derivatives					1011:1021	all derivatives	1007:1021	all derivatives in aqueous buffer	1007:1039	C.d. shows that native galactoglycoprotein and all derivatives in aqueous buffer are predominantly random coil, suggesting that removal of a large number of electrostatic net charges, as well as the major portion of the carbohydrate moiety, does not alter the secondary structure of the polypeptide chain.
1872812	7	44	dep	size	1285:1288	arg1	the					1281:1283	the	1281:1283	the	1281:1283	Examination of the size and conformation of tungsten-shadowed galactoglycoprotein and asialo and agalacto derivatives by electron microscopy shows the size and conformation of all three preparations to be similar, with only minor differences in particle length and width.
1872812	6	45	from	derivatives	1011:1021	arg1	buffer					1034:1039	aqueous buffer	1026:1039	aqueous buffer	1026:1039	C.d. shows that native galactoglycoprotein and all derivatives in aqueous buffer are predominantly random coil, suggesting that removal of a large number of electrostatic net charges, as well as the major portion of the carbohydrate moiety, does not alter the secondary structure of the polypeptide chain.
1872812	2	46	theme	%	300:300	arg1	Galactoglycoprotein					244:262	Galactoglycoprotein	244:262	Galactoglycoprotein	244:262	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	2	46	theme	%	300:300	arg1	carbohydrate					302:313	a unique human plasma protein [76% carbohydrate	267:313	a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine)	267:436	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	6	47	theme	net	1131:1133	arg1	charges					1135:1141	electrostatic net charges	1117:1141	electrostatic net charges	1117:1141	C.d. shows that native galactoglycoprotein and all derivatives in aqueous buffer are predominantly random coil, suggesting that removal of a large number of electrostatic net charges, as well as the major portion of the carbohydrate moiety, does not alter the secondary structure of the polypeptide chain.
1872812	2	48	from	high	527:530	arg1	threonine					546:554	threonine	546:554	threonine	546:554	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	2	48	from	high	527:530	arg1	Binette					597:603	Binette	597:603	Binette	597:603	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	2	48	from	high	527:530	arg1	serine					535:540	serine	535:540	serine	535:540	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	2	49	theme	protein	289:295	arg1	Galactoglycoprotein					244:262	Galactoglycoprotein	244:262	Galactoglycoprotein	244:262	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	2	49	theme	protein	289:295	arg1	carbohydrate					302:313	a unique human plasma protein [76% carbohydrate	267:313	a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine)	267:436	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	1	50	theme	Structural	162:171	arg1	studies					173:179	Structural studies	162:179	Structural studies of a glycoprotein	162:197	Structural studies of a glycoprotein after stepwise enzymic carbohydrate removal.
1872812	5	51	gly	galactoglycoprotein	749:767	arg1	galactoglycoprotein					749:767	galactoglycoprotein	749:767	galactoglycoprotein	749:767	Highly purified exoglycosidases with well-defined specificities were used to prepare five derivatives of galactoglycoprotein in which sequential residues of N-acetylneuraminic acid, galactose, N-acetylglucosamine, a second galactose and N-acetylgalactosamine were removed with 83% of the total carbohydrate cleaved.
1872812	6	52	theme	carbohydrate	1180:1191	arg1	moiety					1193:1198	the carbohydrate moiety	1176:1198	the carbohydrate moiety	1176:1198	C.d. shows that native galactoglycoprotein and all derivatives in aqueous buffer are predominantly random coil, suggesting that removal of a large number of electrostatic net charges, as well as the major portion of the carbohydrate moiety, does not alter the secondary structure of the polypeptide chain.
1872812	2	53	theme	%	318:318	arg1	N-acetylgalactosamine					390:410	29% N-acetylgalactosamine	386:410	29% N-acetylgalactosamine	386:410	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	2	53	theme	%	318:318	arg1	galactose					349:357	20% galactose	345:357	20% galactose	345:357	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	2	53	theme	%	318:318	arg1	N-acetylglucosamine					417:435	N-acetylglucosamine	417:435	N-acetylglucosamine	417:435	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	2	53	theme	%	318:318	arg1	fucose					375:380	1% fucose	372:380	1% fucose	372:380	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	2	53	theme	%	318:318	arg1	acid					339:342	23% N-acetylneuraminic acid	316:342	23% N-acetylneuraminic acid	316:342	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	2	53	theme	%	318:318	arg1	mannose					363:369	3% mannose	360:369	3% mannose	360:369	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	5	54	theme	N-acetylneuraminic	801:818	arg1	galactose					867:875	a second galactose	858:875	a second galactose	858:875	Highly purified exoglycosidases with well-defined specificities were used to prepare five derivatives of galactoglycoprotein in which sequential residues of N-acetylneuraminic acid, galactose, N-acetylglucosamine, a second galactose and N-acetylgalactosamine were removed with 83% of the total carbohydrate cleaved.
1872812	5	54	theme	N-acetylneuraminic	801:818	arg1	N-acetylgalactosamine					881:901	N-acetylgalactosamine	881:901	N-acetylgalactosamine	881:901	Highly purified exoglycosidases with well-defined specificities were used to prepare five derivatives of galactoglycoprotein in which sequential residues of N-acetylneuraminic acid, galactose, N-acetylglucosamine, a second galactose and N-acetylgalactosamine were removed with 83% of the total carbohydrate cleaved.
1872812	5	54	theme	N-acetylneuraminic	801:818	arg1	N-acetylglucosamine					837:855	N-acetylglucosamine	837:855	N-acetylglucosamine	837:855	Highly purified exoglycosidases with well-defined specificities were used to prepare five derivatives of galactoglycoprotein in which sequential residues of N-acetylneuraminic acid, galactose, N-acetylglucosamine, a second galactose and N-acetylgalactosamine were removed with 83% of the total carbohydrate cleaved.
1872812	5	54	theme	N-acetylneuraminic	801:818	arg1	galactose					826:834	galactose	826:834	galactose	826:834	Highly purified exoglycosidases with well-defined specificities were used to prepare five derivatives of galactoglycoprotein in which sequential residues of N-acetylneuraminic acid, galactose, N-acetylglucosamine, a second galactose and N-acetylgalactosamine were removed with 83% of the total carbohydrate cleaved.
1872812	5	54	theme	N-acetylneuraminic	801:818	arg1	acid					820:823	N-acetylneuraminic acid	801:823	N-acetylneuraminic acid	801:823	Highly purified exoglycosidases with well-defined specificities were used to prepare five derivatives of galactoglycoprotein in which sequential residues of N-acetylneuraminic acid, galactose, N-acetylglucosamine, a second galactose and N-acetylgalactosamine were removed with 83% of the total carbohydrate cleaved.
1872812	7	55	theme	agalacto	1363:1370	arg1	derivatives					1372:1382	tungsten-shadowed galactoglycoprotein and asialo and agalacto derivatives	1310:1382	tungsten-shadowed galactoglycoprotein and asialo and agalacto derivatives	1310:1382	Examination of the size and conformation of tungsten-shadowed galactoglycoprotein and asialo and agalacto derivatives by electron microscopy shows the size and conformation of all three preparations to be similar, with only minor differences in particle length and width.
1872812	5	56	theme	galactoglycoprotein	749:767	arg1	derivatives					734:744	five derivatives	729:744	five derivatives of galactoglycoprotein in which sequential residues of N-acetylneuraminic acid, galactose, N-acetylglucosamine, a second galactose and N-acetylgalactosamine were removed with 83% of the total carbohydrate cleaved	729:957	Highly purified exoglycosidases with well-defined specificities were used to prepare five derivatives of galactoglycoprotein in which sequential residues of N-acetylneuraminic acid, galactose, N-acetylglucosamine, a second galactose and N-acetylgalactosamine were removed with 83% of the total carbohydrate cleaved.
1872812	6	57	theme	large	1101:1105	arg1	number					1107:1112	a large number	1099:1112	a large number of electrostatic net charges, as well as the major portion of the carbohydrate moiety,	1099:1199	C.d. shows that native galactoglycoprotein and all derivatives in aqueous buffer are predominantly random coil, suggesting that removal of a large number of electrostatic net charges, as well as the major portion of the carbohydrate moiety, does not alter the secondary structure of the polypeptide chain.
1872812	2	58	theme	acid	505:508	arg1	residues					510:517	about 200 amino acid residues	489:517	about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol	489:618	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	7	59	theme	asialo	1352:1357	arg1	derivatives					1372:1382	tungsten-shadowed galactoglycoprotein and asialo and agalacto derivatives	1310:1382	tungsten-shadowed galactoglycoprotein and asialo and agalacto derivatives	1310:1382	Examination of the size and conformation of tungsten-shadowed galactoglycoprotein and asialo and agalacto derivatives by electron microscopy shows the size and conformation of all three preparations to be similar, with only minor differences in particle length and width.
1872812	6	60	theme	chain	1259:1263	arg1	structure					1230:1238	the secondary structure	1216:1238	the secondary structure of the polypeptide chain	1216:1263	C.d. shows that native galactoglycoprotein and all derivatives in aqueous buffer are predominantly random coil, suggesting that removal of a large number of electrostatic net charges, as well as the major portion of the carbohydrate moiety, does not alter the secondary structure of the polypeptide chain.
1872812	1	61	theme	stepwise	205:212	arg1	removal					235:241	stepwise enzymic carbohydrate removal	205:241	stepwise enzymic carbohydrate removal	205:241	Structural studies of a glycoprotein after stepwise enzymic carbohydrate removal.
1872812	6	62	theme	portion	1165:1171	arg1	number					1107:1112	a large number	1099:1112	a large number of electrostatic net charges, as well as the major portion of the carbohydrate moiety,	1099:1199	C.d. shows that native galactoglycoprotein and all derivatives in aqueous buffer are predominantly random coil, suggesting that removal of a large number of electrostatic net charges, as well as the major portion of the carbohydrate moiety, does not alter the secondary structure of the polypeptide chain.
1872812	0	63	theme	circular	142:149	arg1	dichroism					151:159	circular dichroism	142:159	circular dichroism	142:159	The effect of the carbohydrate moiety upon the size and conformation of human plasma galactoglycoprotein as judged by electron microscopy and circular dichroism.
1872812	2	64	dep	carbohydrate	302:313	arg1	N-acetylgalactosamine					390:410	29% N-acetylgalactosamine	386:410	29% N-acetylgalactosamine	386:410	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	2	64	dep	carbohydrate	302:313	arg1	galactose					349:357	20% galactose	345:357	20% galactose	345:357	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	2	64	dep	carbohydrate	302:313	arg1	N-acetylglucosamine					417:435	N-acetylglucosamine	417:435	N-acetylglucosamine	417:435	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	2	64	dep	carbohydrate	302:313	arg1	fucose					375:380	1% fucose	372:380	1% fucose	372:380	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	2	64	dep	carbohydrate	302:313	arg1	acid					339:342	23% N-acetylneuraminic acid	316:342	23% N-acetylneuraminic acid	316:342	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	2	64	dep	carbohydrate	302:313	arg1	mannose					363:369	3% mannose	360:369	3% mannose	360:369	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	2	65	theme	human	276:280	arg1	Galactoglycoprotein					244:262	Galactoglycoprotein	244:262	Galactoglycoprotein	244:262	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	2	65	theme	human	276:280	arg1	carbohydrate					302:313	a unique human plasma protein [76% carbohydrate	267:313	a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine)	267:436	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	5	66	theme	second	860:865	arg1	acid					820:823	N-acetylneuraminic acid	801:823	N-acetylneuraminic acid	801:823	Highly purified exoglycosidases with well-defined specificities were used to prepare five derivatives of galactoglycoprotein in which sequential residues of N-acetylneuraminic acid, galactose, N-acetylglucosamine, a second galactose and N-acetylgalactosamine were removed with 83% of the total carbohydrate cleaved.
1872812	5	66	theme	second	860:865	arg1	galactose					867:875	a second galactose	858:875	a second galactose	858:875	Highly purified exoglycosidases with well-defined specificities were used to prepare five derivatives of galactoglycoprotein in which sequential residues of N-acetylneuraminic acid, galactose, N-acetylglucosamine, a second galactose and N-acetylgalactosamine were removed with 83% of the total carbohydrate cleaved.
1872812	5	67	theme	purified	651:658	arg1	exoglycosidases					660:674	Highly purified exoglycosidases	644:674	Highly purified exoglycosidases with well-defined specificities	644:706	Highly purified exoglycosidases with well-defined specificities were used to prepare five derivatives of galactoglycoprotein in which sequential residues of N-acetylneuraminic acid, galactose, N-acetylglucosamine, a second galactose and N-acetylgalactosamine were removed with 83% of the total carbohydrate cleaved.
1872812	1	68	theme	glycoprotein	186:197	arg1	studies					173:179	Structural studies	162:179	Structural studies of a glycoprotein	162:197	Structural studies of a glycoprotein after stepwise enzymic carbohydrate removal.
1872812	5	69	with	exoglycosidases	660:674	arg1	specificities					694:706	well-defined specificities	681:706	well-defined specificities	681:706	Highly purified exoglycosidases with well-defined specificities were used to prepare five derivatives of galactoglycoprotein in which sequential residues of N-acetylneuraminic acid, galactose, N-acetylglucosamine, a second galactose and N-acetylgalactosamine were removed with 83% of the total carbohydrate cleaved.
1872812	7	70	theme	particle	1511:1518	arg1	length					1520:1525	particle length	1511:1525	particle length	1511:1525	Examination of the size and conformation of tungsten-shadowed galactoglycoprotein and asialo and agalacto derivatives by electron microscopy shows the size and conformation of all three preparations to be similar, with only minor differences in particle length and width.
1872812	0	71	theme	plasma	78:83	arg1	conformation					56:67	conformation	56:67	conformation	56:67	The effect of the carbohydrate moiety upon the size and conformation of human plasma galactoglycoprotein as judged by electron microscopy and circular dichroism.
1872812	0	71	theme	plasma	78:83	arg1	size					47:50	size	47:50	size	47:50	The effect of the carbohydrate moiety upon the size and conformation of human plasma galactoglycoprotein as judged by electron microscopy and circular dichroism.
1872812	2	72	theme	polypeptide	468:478	arg1	chain					480:484	a single polypeptide chain	459:484	a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol	459:618	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	2	72	theme	polypeptide	468:478	arg1	polypeptide					446:456	24% polypeptide	442:456	24% polypeptide	442:456	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	2	73	theme	%	361:361	arg1	mannose					363:369	3% mannose	360:369	3% mannose	360:369	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	2	73	theme	%	361:361	arg1	acid					339:342	23% N-acetylneuraminic acid	316:342	23% N-acetylneuraminic acid	316:342	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	7	74	from	differences	1496:1506	arg1	width					1531:1535	width	1531:1535	width	1531:1535	Examination of the size and conformation of tungsten-shadowed galactoglycoprotein and asialo and agalacto derivatives by electron microscopy shows the size and conformation of all three preparations to be similar, with only minor differences in particle length and width.
1872812	7	74	from	differences	1496:1506	arg1	length					1520:1525	particle length	1511:1525	particle length	1511:1525	Examination of the size and conformation of tungsten-shadowed galactoglycoprotein and asialo and agalacto derivatives by electron microscopy shows the size and conformation of all three preparations to be similar, with only minor differences in particle length and width.
1872812	0	75	gly	galactoglycoprotein	85:103	arg1	galactoglycoprotein					85:103	galactoglycoprotein	85:103	galactoglycoprotein as judged by electron microscopy and circular dichroism	85:159	The effect of the carbohydrate moiety upon the size and conformation of human plasma galactoglycoprotein as judged by electron microscopy and circular dichroism.
1872812	2	76	theme	%	388:388	arg1	N-acetylgalactosamine					390:410	29% N-acetylgalactosamine	386:410	29% N-acetylgalactosamine	386:410	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	2	76	theme	%	388:388	arg1	acid					339:342	23% N-acetylneuraminic acid	316:342	23% N-acetylneuraminic acid	316:342	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	0	77	theme	moiety	31:36	arg1	effect					4:9	The effect	0:9	The effect of the carbohydrate moiety upon the size and conformation of human plasma	0:83	The effect of the carbohydrate moiety upon the size and conformation of human plasma galactoglycoprotein as judged by electron microscopy and circular dichroism.
1872812	7	78	theme	minor	1490:1494	arg1	differences					1496:1506	only minor differences	1485:1506	only minor differences in particle length and width	1485:1535	Examination of the size and conformation of tungsten-shadowed galactoglycoprotein and asialo and agalacto derivatives by electron microscopy shows the size and conformation of all three preparations to be similar, with only minor differences in particle length and width.
1872812	2	79	theme	24	442:443	arg1	%					444:444	%	444:444	%	444:444	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	6	80	gly	galactoglycoprotein	983:1001	arg1	coil					1066:1069	random coil	1059:1069	random coil	1059:1069	C.d. shows that native galactoglycoprotein and all derivatives in aqueous buffer are predominantly random coil, suggesting that removal of a large number of electrostatic net charges, as well as the major portion of the carbohydrate moiety, does not alter the secondary structure of the polypeptide chain.
1872812	6	80	gly	galactoglycoprotein	983:1001	arg1	galactoglycoprotein					983:1001	native galactoglycoprotein	976:1001	native galactoglycoprotein	976:1001	C.d. shows that native galactoglycoprotein and all derivatives in aqueous buffer are predominantly random coil, suggesting that removal of a large number of electrostatic net charges, as well as the major portion of the carbohydrate moiety, does not alter the secondary structure of the polypeptide chain.
1872812	6	80	gly	galactoglycoprotein	983:1001	arg1	derivatives					1011:1021	all derivatives	1007:1021	all derivatives in aqueous buffer	1007:1039	C.d. shows that native galactoglycoprotein and all derivatives in aqueous buffer are predominantly random coil, suggesting that removal of a large number of electrostatic net charges, as well as the major portion of the carbohydrate moiety, does not alter the secondary structure of the polypeptide chain.
1872812	2	81	theme	%	373:373	arg1	fucose					375:380	1% fucose	372:380	1% fucose	372:380	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	2	81	theme	%	373:373	arg1	acid					339:342	23% N-acetylneuraminic acid	316:342	23% N-acetylneuraminic acid	316:342	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	0	82	theme	electron	118:125	arg1	microscopy					127:136	electron microscopy	118:136	electron microscopy	118:136	The effect of the carbohydrate moiety upon the size and conformation of human plasma galactoglycoprotein as judged by electron microscopy and circular dichroism.
1872812	1	83	dep	studies	173:179	arg1	removal					235:241	stepwise enzymic carbohydrate removal	205:241	stepwise enzymic carbohydrate removal	205:241	Structural studies of a glycoprotein after stepwise enzymic carbohydrate removal.
1872812	7	84	theme	galactoglycoprotein	1328:1346	arg1	derivatives					1372:1382	tungsten-shadowed galactoglycoprotein and asialo and agalacto derivatives	1310:1382	tungsten-shadowed galactoglycoprotein and asialo and agalacto derivatives	1310:1382	Examination of the size and conformation of tungsten-shadowed galactoglycoprotein and asialo and agalacto derivatives by electron microscopy shows the size and conformation of all three preparations to be similar, with only minor differences in particle length and width.
1872812	2	85	theme	N-acetylneuraminic	320:337	arg1	N-acetylgalactosamine					390:410	29% N-acetylgalactosamine	386:410	29% N-acetylgalactosamine	386:410	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	2	85	theme	N-acetylneuraminic	320:337	arg1	galactose					349:357	20% galactose	345:357	20% galactose	345:357	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	2	85	theme	N-acetylneuraminic	320:337	arg1	N-acetylglucosamine					417:435	N-acetylglucosamine	417:435	N-acetylglucosamine	417:435	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	2	85	theme	N-acetylneuraminic	320:337	arg1	fucose					375:380	1% fucose	372:380	1% fucose	372:380	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	2	85	theme	N-acetylneuraminic	320:337	arg1	acid					339:342	23% N-acetylneuraminic acid	316:342	23% N-acetylneuraminic acid	316:342	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	2	85	theme	N-acetylneuraminic	320:337	arg1	mannose					363:369	3% mannose	360:369	3% mannose	360:369	Galactoglycoprotein is a unique human plasma protein [76% carbohydrate (23% N-acetylneuraminic acid, 20% galactose, 3% mannose, 1% fucose and 29% N-acetylgalactosamine plus N-acetylglucosamine) and 24% polypeptide, a single polypeptide chain of about 200 amino acid residues that is high in serine and threonine content] [Schmid, Mao, Kimura, Hayashi & Binette (1980) J. Biol.
1872812	1	86	theme	enzymic	214:220	arg1	removal					235:241	stepwise enzymic carbohydrate removal	205:241	stepwise enzymic carbohydrate removal	205:241	Structural studies of a glycoprotein after stepwise enzymic carbohydrate removal.
1872812	5	87	theme	carbohydrate	938:949	arg1	carbohydrate					938:949	the total carbohydrate	928:949	the total carbohydrate cleaved	928:957	Highly purified exoglycosidases with well-defined specificities were used to prepare five derivatives of galactoglycoprotein in which sequential residues of N-acetylneuraminic acid, galactose, N-acetylglucosamine, a second galactose and N-acetylgalactosamine were removed with 83% of the total carbohydrate cleaved.
1872812	5	87	theme	carbohydrate	938:949	arg1	%					923:923	83%	921:923	83% of the total carbohydrate cleaved	921:957	Highly purified exoglycosidases with well-defined specificities were used to prepare five derivatives of galactoglycoprotein in which sequential residues of N-acetylneuraminic acid, galactose, N-acetylglucosamine, a second galactose and N-acetylgalactosamine were removed with 83% of the total carbohydrate cleaved.
6725284	6	0	dep	hexasaccharide	814:827	arg1	see					840:842	see	840:842	see text	840:847	The structure of the predominant glycan, a hexasaccharide: (formula; see text) and that of a tetrasaccharide: NeuAc alpha(2----3)Gal beta(1----3)[NeuAc alpha (2----6)]GalNAc-ol, were determined.
6725284	1	1	theme	=	162:162	arg1	Mr					159:160	Mr = 81,000	159:169	Mr = 81,000	159:169	Human plasma galactoglycoprotein (Mr = 81,000) which was recently identified and characterized (Schmid, K., Mao, S. K. Y., Kimura, A., Hayashi, S., and Binette , J. P. (1980) J. Biol.
6725284	1	1	theme	=	162:162	arg1	galactoglycoprotein					138:156	Human plasma galactoglycoprotein	125:156	Human plasma galactoglycoprotein (Mr = 81,000) which was recently identified and characterized (Schmid, K., Mao, S. K. Y., Kimura, A., Hayashi, S., and Binette , J. P. (1980) J. Biol	125:306	Human plasma galactoglycoprotein (Mr = 81,000) which was recently identified and characterized (Schmid, K., Mao, S. K. Y., Kimura, A., Hayashi, S., and Binette , J. P. (1980) J. Biol.
6725284	8	2	gly	glycopeptide	1219:1230	arg2	glycopeptide					1219:1230	the desialyzed resulting glycopeptide fraction	1194:1239	the desialyzed resulting glycopeptide fraction on concanavalin A-Sepharose	1194:1267	For the isolation of its N-glycosidic oligosaccharide chains, the protein was exhaustively digested with proteases followed by chromatography of the desialyzed resulting glycopeptide fraction on concanavalin A-Sepharose.
6725284	5	3	theme	NMR	753:755	arg1	spectroscopy					757:768	500-MHz 1H NMR spectroscopy	742:768	500-MHz 1H NMR spectroscopy	742:768	For the study of the O-glycosidic oligosaccharide chains, the protein was subjected to beta-elimination and the resulting oligosaccharide preparations were analyzed by 500-MHz 1H NMR spectroscopy.
6725284	4	4	theme	primary	510:516	arg1	structure					518:526	the primary structure	506:526	the primary structure of the oligosaccharide units of this protein	506:571	The aim of the present investigation was to elucidate the primary structure of the oligosaccharide units of this protein.
6725284	9	5	theme	obtained	1305:1312	arg1	preparations					1314:1325	the obtained preparations	1301:1325	the obtained preparations	1301:1325	500-MHz 1H NMR spectroscopy of the obtained preparations revealed the presence of 3 diantennary N-glycosidic chains that are extended with a Fuc residue at the Asn-linked GlcNAc.
6725284	0	6	theme	1H	104:105	arg1	spectroscopy					111:122	500-megahertz 1H NMR spectroscopy	90:122	500-megahertz 1H NMR spectroscopy	90:122	The structure of the carbohydrate units of human plasma galactoglycoprotein determined by 500-megahertz 1H NMR spectroscopy.
6725284	5	7	theme	oligosaccharide	608:622	arg1	chains					624:629	the O-glycosidic oligosaccharide chains	591:629	the O-glycosidic oligosaccharide chains	591:629	For the study of the O-glycosidic oligosaccharide chains, the protein was subjected to beta-elimination and the resulting oligosaccharide preparations were analyzed by 500-MHz 1H NMR spectroscopy.
6725284	6	8	theme	[NeuAc	916:921	arg1	alpha					923:927	1----3)[NeuAc alpha (2----6)	909:936	1----3)[NeuAc alpha (2----6)	909:936	The structure of the predominant glycan, a hexasaccharide: (formula; see text) and that of a tetrasaccharide: NeuAc alpha(2----3)Gal beta(1----3)[NeuAc alpha (2----6)]GalNAc-ol, were determined.
6725284	6	8	theme	[NeuAc	916:921	arg1	beta					904:907	NeuAc alpha(2----3)Gal beta	881:907	a tetrasaccharide: NeuAc alpha(2----3)Gal beta(1----3)[NeuAc alpha (2----6)]GalNAc-ol	862:946	The structure of the predominant glycan, a hexasaccharide: (formula; see text) and that of a tetrasaccharide: NeuAc alpha(2----3)Gal beta(1----3)[NeuAc alpha (2----6)]GalNAc-ol, were determined.
6725284	0	9	theme	500-megahertz	90:102	arg1	spectroscopy					111:122	500-megahertz 1H NMR spectroscopy	90:122	500-megahertz 1H NMR spectroscopy	90:122	The structure of the carbohydrate units of human plasma galactoglycoprotein determined by 500-megahertz 1H NMR spectroscopy.
6725284	6	10	dep	see	840:842	arg1	formula					831:837	formula	831:837	formula	831:837	The structure of the predominant glycan, a hexasaccharide: (formula; see text) and that of a tetrasaccharide: NeuAc alpha(2----3)Gal beta(1----3)[NeuAc alpha (2----6)]GalNAc-ol, were determined.
6725284	9	11	theme	chains	1379:1384	arg1	presence					1340:1347	the presence	1336:1347	the presence of 3 diantennary N-glycosidic chains that are extended with a Fuc residue at the Asn-linked GlcNAc	1336:1446	500-MHz 1H NMR spectroscopy of the obtained preparations revealed the presence of 3 diantennary N-glycosidic chains that are extended with a Fuc residue at the Asn-linked GlcNAc.
6725284	0	12	gly	galactoglycoprotein	56:74	arg1	galactoglycoprotein					56:74	galactoglycoprotein	56:74	galactoglycoprotein determined by 500-megahertz 1H NMR spectroscopy	56:122	The structure of the carbohydrate units of human plasma galactoglycoprotein determined by 500-megahertz 1H NMR spectroscopy.
6725284	6	13	theme	beta	904:907	arg1	GalNAc-ol					938:946	a tetrasaccharide: NeuAc alpha(2----3)Gal beta(1----3)[NeuAc alpha (2----6)]GalNAc-ol	862:946	a tetrasaccharide: NeuAc alpha(2----3)Gal beta(1----3)[NeuAc alpha (2----6)]GalNAc-ol	862:946	The structure of the predominant glycan, a hexasaccharide: (formula; see text) and that of a tetrasaccharide: NeuAc alpha(2----3)Gal beta(1----3)[NeuAc alpha (2----6)]GalNAc-ol, were determined.
6725284	5	14	theme	1H	750:751	arg1	spectroscopy					757:768	500-MHz 1H NMR spectroscopy	742:768	500-MHz 1H NMR spectroscopy	742:768	For the study of the O-glycosidic oligosaccharide chains, the protein was subjected to beta-elimination and the resulting oligosaccharide preparations were analyzed by 500-MHz 1H NMR spectroscopy.
6725284	6	15	theme	2----3	893:898	arg1	alpha					923:927	1----3)[NeuAc alpha (2----6)	909:936	1----3)[NeuAc alpha (2----6)	909:936	The structure of the predominant glycan, a hexasaccharide: (formula; see text) and that of a tetrasaccharide: NeuAc alpha(2----3)Gal beta(1----3)[NeuAc alpha (2----6)]GalNAc-ol, were determined.
6725284	6	15	theme	2----3	893:898	arg1	beta					904:907	NeuAc alpha(2----3)Gal beta	881:907	a tetrasaccharide: NeuAc alpha(2----3)Gal beta(1----3)[NeuAc alpha (2----6)]GalNAc-ol	862:946	The structure of the predominant glycan, a hexasaccharide: (formula; see text) and that of a tetrasaccharide: NeuAc alpha(2----3)Gal beta(1----3)[NeuAc alpha (2----6)]GalNAc-ol, were determined.
6725284	6	16	theme	alpha	887:891	arg1	alpha					923:927	1----3)[NeuAc alpha (2----6)	909:936	1----3)[NeuAc alpha (2----6)	909:936	The structure of the predominant glycan, a hexasaccharide: (formula; see text) and that of a tetrasaccharide: NeuAc alpha(2----3)Gal beta(1----3)[NeuAc alpha (2----6)]GalNAc-ol, were determined.
6725284	6	16	theme	alpha	887:891	arg1	beta					904:907	NeuAc alpha(2----3)Gal beta	881:907	a tetrasaccharide: NeuAc alpha(2----3)Gal beta(1----3)[NeuAc alpha (2----6)]GalNAc-ol	862:946	The structure of the predominant glycan, a hexasaccharide: (formula; see text) and that of a tetrasaccharide: NeuAc alpha(2----3)Gal beta(1----3)[NeuAc alpha (2----6)]GalNAc-ol, were determined.
6725284	9	17	theme	Fuc	1411:1413	arg1	residue					1415:1421	a Fuc residue	1409:1421	a Fuc residue at the Asn-linked GlcNAc	1409:1446	500-MHz 1H NMR spectroscopy of the obtained preparations revealed the presence of 3 diantennary N-glycosidic chains that are extended with a Fuc residue at the Asn-linked GlcNAc.
6725284	9	18	theme	500-MHz	1270:1276	arg1	spectroscopy					1285:1296	500-MHz 1H NMR spectroscopy	1270:1296	500-MHz 1H NMR spectroscopy of the obtained preparations	1270:1325	500-MHz 1H NMR spectroscopy of the obtained preparations revealed the presence of 3 diantennary N-glycosidic chains that are extended with a Fuc residue at the Asn-linked GlcNAc.
6725284	4	19	theme	investigation	475:487	arg1	aim					456:458	The aim	452:458	The aim of the present investigation	452:487	The aim of the present investigation was to elucidate the primary structure of the oligosaccharide units of this protein.
6725284	0	20	theme	NMR	107:109	arg1	spectroscopy					111:122	500-megahertz 1H NMR spectroscopy	90:122	500-megahertz 1H NMR spectroscopy	90:122	The structure of the carbohydrate units of human plasma galactoglycoprotein determined by 500-megahertz 1H NMR spectroscopy.
6725284	5	21	theme	500-MHz	742:748	arg1	spectroscopy					757:768	500-MHz 1H NMR spectroscopy	742:768	500-MHz 1H NMR spectroscopy	742:768	For the study of the O-glycosidic oligosaccharide chains, the protein was subjected to beta-elimination and the resulting oligosaccharide preparations were analyzed by 500-MHz 1H NMR spectroscopy.
6725284	9	22	theme	preparations	1314:1325	arg1	spectroscopy					1285:1296	500-MHz 1H NMR spectroscopy	1270:1296	500-MHz 1H NMR spectroscopy of the obtained preparations	1270:1325	500-MHz 1H NMR spectroscopy of the obtained preparations revealed the presence of 3 diantennary N-glycosidic chains that are extended with a Fuc residue at the Asn-linked GlcNAc.
6725284	9	23	from	GlcNAc	1441:1446	arg1	residue					1415:1421	a Fuc residue	1409:1421	a Fuc residue at the Asn-linked GlcNAc	1409:1446	500-MHz 1H NMR spectroscopy of the obtained preparations revealed the presence of 3 diantennary N-glycosidic chains that are extended with a Fuc residue at the Asn-linked GlcNAc.
6725284	4	24	theme	present	467:473	arg1	investigation					475:487	the present investigation	463:487	the present investigation	463:487	The aim of the present investigation was to elucidate the primary structure of the oligosaccharide units of this protein.
6725284	8	25	theme	oligosaccharide	1087:1101	arg1	chains					1103:1108	its N-glycosidic oligosaccharide chains	1070:1108	its N-glycosidic oligosaccharide chains	1070:1108	For the isolation of its N-glycosidic oligosaccharide chains, the protein was exhaustively digested with proteases followed by chromatography of the desialyzed resulting glycopeptide fraction on concanavalin A-Sepharose.
6725284	6	26	theme	predominant	792:802	arg1	glycan					804:809	the predominant glycan	788:809	the predominant glycan	788:809	The structure of the predominant glycan, a hexasaccharide: (formula; see text) and that of a tetrasaccharide: NeuAc alpha(2----3)Gal beta(1----3)[NeuAc alpha (2----6)]GalNAc-ol, were determined.
6725284	6	26	theme	predominant	792:802	arg1	hexasaccharide					814:827	a hexasaccharide	812:827	a hexasaccharide: (formula; see text)	812:848	The structure of the predominant glycan, a hexasaccharide: (formula; see text) and that of a tetrasaccharide: NeuAc alpha(2----3)Gal beta(1----3)[NeuAc alpha (2----6)]GalNAc-ol, were determined.
6725284	6	26	theme	predominant	792:802	arg1	that					854:857	that	854:857	that	854:857	The structure of the predominant glycan, a hexasaccharide: (formula; see text) and that of a tetrasaccharide: NeuAc alpha(2----3)Gal beta(1----3)[NeuAc alpha (2----6)]GalNAc-ol, were determined.
6725284	5	27	theme	oligosaccharide	696:710	arg1	preparations					712:723	the resulting oligosaccharide preparations	682:723	the resulting oligosaccharide preparations	682:723	For the study of the O-glycosidic oligosaccharide chains, the protein was subjected to beta-elimination and the resulting oligosaccharide preparations were analyzed by 500-MHz 1H NMR spectroscopy.
6725284	6	28	theme	tetrasaccharide	864:878	arg1	GalNAc-ol					938:946	a tetrasaccharide: NeuAc alpha(2----3)Gal beta(1----3)[NeuAc alpha (2----6)]GalNAc-ol	862:946	a tetrasaccharide: NeuAc alpha(2----3)Gal beta(1----3)[NeuAc alpha (2----6)]GalNAc-ol	862:946	The structure of the predominant glycan, a hexasaccharide: (formula; see text) and that of a tetrasaccharide: NeuAc alpha(2----3)Gal beta(1----3)[NeuAc alpha (2----6)]GalNAc-ol, were determined.
6725284	6	29	theme	NeuAc	881:885	arg1	alpha					923:927	1----3)[NeuAc alpha (2----6)	909:936	1----3)[NeuAc alpha (2----6)	909:936	The structure of the predominant glycan, a hexasaccharide: (formula; see text) and that of a tetrasaccharide: NeuAc alpha(2----3)Gal beta(1----3)[NeuAc alpha (2----6)]GalNAc-ol, were determined.
6725284	6	29	theme	NeuAc	881:885	arg1	beta					904:907	NeuAc alpha(2----3)Gal beta	881:907	a tetrasaccharide: NeuAc alpha(2----3)Gal beta(1----3)[NeuAc alpha (2----6)]GalNAc-ol	862:946	The structure of the predominant glycan, a hexasaccharide: (formula; see text) and that of a tetrasaccharide: NeuAc alpha(2----3)Gal beta(1----3)[NeuAc alpha (2----6)]GalNAc-ol, were determined.
6725284	9	30	theme	Asn-linked	1430:1439	arg1	GlcNAc					1441:1446	the Asn-linked GlcNAc	1426:1446	the Asn-linked GlcNAc	1426:1446	500-MHz 1H NMR spectroscopy of the obtained preparations revealed the presence of 3 diantennary N-glycosidic chains that are extended with a Fuc residue at the Asn-linked GlcNAc.
6725284	0	31	dep	galactoglycoprotein	56:74	arg1	determined					76:85	determined	76:85	galactoglycoprotein determined by 500-megahertz 1H NMR spectroscopy	56:122	The structure of the carbohydrate units of human plasma galactoglycoprotein determined by 500-megahertz 1H NMR spectroscopy.
6725284	9	32	theme	NMR	1281:1283	arg1	spectroscopy					1285:1296	500-MHz 1H NMR spectroscopy	1270:1296	500-MHz 1H NMR spectroscopy of the obtained preparations	1270:1325	500-MHz 1H NMR spectroscopy of the obtained preparations revealed the presence of 3 diantennary N-glycosidic chains that are extended with a Fuc residue at the Asn-linked GlcNAc.
6725284	6	33	theme	glycan	804:809	arg1	structure					775:783	The structure	771:783	The structure of the predominant glycan, a hexasaccharide: (formula; see text) and that of a tetrasaccharide: NeuAc alpha(2----3)Gal beta(1----3)[NeuAc alpha (2----6)]GalNAc-ol,	771:947	The structure of the predominant glycan, a hexasaccharide: (formula; see text) and that of a tetrasaccharide: NeuAc alpha(2----3)Gal beta(1----3)[NeuAc alpha (2----6)]GalNAc-ol, were determined.
6725284	1	34	dep	K.	229:230	arg1	P					290:290	P	290:290	Schmid, K., Mao, S. K. Y., Kimura, A., Hayashi, S., and Binette , J. P. (1980) J. Biol	221:306	Human plasma galactoglycoprotein (Mr = 81,000) which was recently identified and characterized (Schmid, K., Mao, S. K. Y., Kimura, A., Hayashi, S., and Binette , J. P. (1980) J. Biol.
6725284	1	34	dep	K.	229:230	arg1	Biol					303:306	Biol	303:306	Biol	303:306	Human plasma galactoglycoprotein (Mr = 81,000) which was recently identified and characterized (Schmid, K., Mao, S. K. Y., Kimura, A., Hayashi, S., and Binette , J. P. (1980) J. Biol.
6725284	4	35	theme	protein	565:571	arg1	units					551:555	the oligosaccharide units	531:555	the oligosaccharide units of this protein	531:571	The aim of the present investigation was to elucidate the primary structure of the oligosaccharide units of this protein.
6725284	8	36	from	fraction	1232:1239	arg1	A-Sepharose					1257:1267	concanavalin A-Sepharose	1244:1267	concanavalin A-Sepharose	1244:1267	For the isolation of its N-glycosidic oligosaccharide chains, the protein was exhaustively digested with proteases followed by chromatography of the desialyzed resulting glycopeptide fraction on concanavalin A-Sepharose.
6725284	8	37	theme	concanavalin	1244:1255	arg1	A-Sepharose					1257:1267	concanavalin A-Sepharose	1244:1267	concanavalin A-Sepharose	1244:1267	For the isolation of its N-glycosidic oligosaccharide chains, the protein was exhaustively digested with proteases followed by chromatography of the desialyzed resulting glycopeptide fraction on concanavalin A-Sepharose.
6725284	0	38	theme	units	34:38	arg1	structure					4:12	The structure	0:12	The structure of the carbohydrate units of human plasma	0:54	The structure of the carbohydrate units of human plasma galactoglycoprotein determined by 500-megahertz 1H NMR spectroscopy.
6725284	3	39	theme	carbohydrate	370:381	arg1	GalNAc					432:437	GalNAc	432:437	GalNAc	432:437	255, 3221-3226) was found to possess an unusually high carbohydrate content (76%) comprised of NeuAc, Gal, Man, Fuc, GalNAc, and GlcNAc.
6725284	3	39	theme	carbohydrate	370:381	arg1	%					394:394	76%	392:394	76%	392:394	255, 3221-3226) was found to possess an unusually high carbohydrate content (76%) comprised of NeuAc, Gal, Man, Fuc, GalNAc, and GlcNAc.
6725284	3	39	theme	carbohydrate	370:381	arg1	Gal					417:419	Gal	417:419	Gal	417:419	255, 3221-3226) was found to possess an unusually high carbohydrate content (76%) comprised of NeuAc, Gal, Man, Fuc, GalNAc, and GlcNAc.
6725284	3	39	theme	carbohydrate	370:381	arg1	Man					422:424	Man	422:424	Man	422:424	255, 3221-3226) was found to possess an unusually high carbohydrate content (76%) comprised of NeuAc, Gal, Man, Fuc, GalNAc, and GlcNAc.
6725284	3	39	theme	carbohydrate	370:381	arg1	GlcNAc					444:449	GlcNAc	444:449	GlcNAc	444:449	255, 3221-3226) was found to possess an unusually high carbohydrate content (76%) comprised of NeuAc, Gal, Man, Fuc, GalNAc, and GlcNAc.
6725284	3	39	theme	carbohydrate	370:381	arg1	Fuc					427:429	Fuc	427:429	Fuc	427:429	255, 3221-3226) was found to possess an unusually high carbohydrate content (76%) comprised of NeuAc, Gal, Man, Fuc, GalNAc, and GlcNAc.
6725284	3	39	theme	carbohydrate	370:381	arg1	content					383:389	an unusually high carbohydrate content	352:389	an unusually high carbohydrate content (76%) comprised of NeuAc	352:414	255, 3221-3226) was found to possess an unusually high carbohydrate content (76%) comprised of NeuAc, Gal, Man, Fuc, GalNAc, and GlcNAc.
6725284	1	40	gly	galactoglycoprotein	138:156	arg1	Mr					159:160	Mr = 81,000	159:169	Mr = 81,000	159:169	Human plasma galactoglycoprotein (Mr = 81,000) which was recently identified and characterized (Schmid, K., Mao, S. K. Y., Kimura, A., Hayashi, S., and Binette , J. P. (1980) J. Biol.
6725284	1	40	gly	galactoglycoprotein	138:156	arg1	galactoglycoprotein					138:156	Human plasma galactoglycoprotein	125:156	Human plasma galactoglycoprotein (Mr = 81,000) which was recently identified and characterized (Schmid, K., Mao, S. K. Y., Kimura, A., Hayashi, S., and Binette , J. P. (1980) J. Biol	125:306	Human plasma galactoglycoprotein (Mr = 81,000) which was recently identified and characterized (Schmid, K., Mao, S. K. Y., Kimura, A., Hayashi, S., and Binette , J. P. (1980) J. Biol.
6725284	3	41	dep	255	315:317	arg1	3221-3226					320:328	3221-3226	320:328	3221-3226	320:328	255, 3221-3226) was found to possess an unusually high carbohydrate content (76%) comprised of NeuAc, Gal, Man, Fuc, GalNAc, and GlcNAc.
6725284	9	42	theme	1H	1278:1279	arg1	spectroscopy					1285:1296	500-MHz 1H NMR spectroscopy	1270:1296	500-MHz 1H NMR spectroscopy of the obtained preparations	1270:1325	500-MHz 1H NMR spectroscopy of the obtained preparations revealed the presence of 3 diantennary N-glycosidic chains that are extended with a Fuc residue at the Asn-linked GlcNAc.
6725284	0	43	theme	carbohydrate	21:32	arg1	units					34:38	the carbohydrate units	17:38	the carbohydrate units of human plasma	17:54	The structure of the carbohydrate units of human plasma galactoglycoprotein determined by 500-megahertz 1H NMR spectroscopy.
6725284	5	44	theme	O-glycosidic	595:606	arg1	chains					624:629	the O-glycosidic oligosaccharide chains	591:629	the O-glycosidic oligosaccharide chains	591:629	For the study of the O-glycosidic oligosaccharide chains, the protein was subjected to beta-elimination and the resulting oligosaccharide preparations were analyzed by 500-MHz 1H NMR spectroscopy.
6725284	3	45	contain	possess	344:350	arg1	255					315:317	255	315:317	255	315:317	255, 3221-3226) was found to possess an unusually high carbohydrate content (76%) comprised of NeuAc, Gal, Man, Fuc, GalNAc, and GlcNAc.
6725284	3	45	contain	possess	344:350	arg2	GlcNAc					444:449	GlcNAc	444:449	GlcNAc	444:449	255, 3221-3226) was found to possess an unusually high carbohydrate content (76%) comprised of NeuAc, Gal, Man, Fuc, GalNAc, and GlcNAc.
6725284	3	45	contain	possess	344:350	arg2	content					383:389	an unusually high carbohydrate content	352:389	an unusually high carbohydrate content (76%) comprised of NeuAc	352:414	255, 3221-3226) was found to possess an unusually high carbohydrate content (76%) comprised of NeuAc, Gal, Man, Fuc, GalNAc, and GlcNAc.
6725284	3	45	contain	possess	344:350	arg2	Fuc					427:429	Fuc	427:429	Fuc	427:429	255, 3221-3226) was found to possess an unusually high carbohydrate content (76%) comprised of NeuAc, Gal, Man, Fuc, GalNAc, and GlcNAc.
6725284	3	45	contain	possess	344:350	arg2	%					394:394	76%	392:394	76%	392:394	255, 3221-3226) was found to possess an unusually high carbohydrate content (76%) comprised of NeuAc, Gal, Man, Fuc, GalNAc, and GlcNAc.
6725284	3	45	contain	possess	344:350	arg2	Gal					417:419	Gal	417:419	Gal	417:419	255, 3221-3226) was found to possess an unusually high carbohydrate content (76%) comprised of NeuAc, Gal, Man, Fuc, GalNAc, and GlcNAc.
6725284	3	45	contain	possess	344:350	arg2	GalNAc					432:437	GalNAc	432:437	GalNAc	432:437	255, 3221-3226) was found to possess an unusually high carbohydrate content (76%) comprised of NeuAc, Gal, Man, Fuc, GalNAc, and GlcNAc.
6725284	3	45	contain	possess	344:350	arg2	Man					422:424	Man	422:424	Man	422:424	255, 3221-3226) was found to possess an unusually high carbohydrate content (76%) comprised of NeuAc, Gal, Man, Fuc, GalNAc, and GlcNAc.
6725284	8	46	theme	N-glycosidic	1074:1085	arg1	chains					1103:1108	its N-glycosidic oligosaccharide chains	1070:1108	its N-glycosidic oligosaccharide chains	1070:1108	For the isolation of its N-glycosidic oligosaccharide chains, the protein was exhaustively digested with proteases followed by chromatography of the desialyzed resulting glycopeptide fraction on concanavalin A-Sepharose.
6725284	0	47	theme	human	43:47	arg1	plasma					49:54	human plasma	43:54	human plasma	43:54	The structure of the carbohydrate units of human plasma galactoglycoprotein determined by 500-megahertz 1H NMR spectroscopy.
6725284	8	48	theme	resulting	1209:1217	arg1	fraction					1232:1239	the desialyzed resulting glycopeptide fraction	1194:1239	the desialyzed resulting glycopeptide fraction on concanavalin A-Sepharose	1194:1267	For the isolation of its N-glycosidic oligosaccharide chains, the protein was exhaustively digested with proteases followed by chromatography of the desialyzed resulting glycopeptide fraction on concanavalin A-Sepharose.
6725284	3	49	theme	high	365:368	arg1	GalNAc					432:437	GalNAc	432:437	GalNAc	432:437	255, 3221-3226) was found to possess an unusually high carbohydrate content (76%) comprised of NeuAc, Gal, Man, Fuc, GalNAc, and GlcNAc.
6725284	3	49	theme	high	365:368	arg1	%					394:394	76%	392:394	76%	392:394	255, 3221-3226) was found to possess an unusually high carbohydrate content (76%) comprised of NeuAc, Gal, Man, Fuc, GalNAc, and GlcNAc.
6725284	3	49	theme	high	365:368	arg1	Gal					417:419	Gal	417:419	Gal	417:419	255, 3221-3226) was found to possess an unusually high carbohydrate content (76%) comprised of NeuAc, Gal, Man, Fuc, GalNAc, and GlcNAc.
6725284	3	49	theme	high	365:368	arg1	Man					422:424	Man	422:424	Man	422:424	255, 3221-3226) was found to possess an unusually high carbohydrate content (76%) comprised of NeuAc, Gal, Man, Fuc, GalNAc, and GlcNAc.
6725284	3	49	theme	high	365:368	arg1	GlcNAc					444:449	GlcNAc	444:449	GlcNAc	444:449	255, 3221-3226) was found to possess an unusually high carbohydrate content (76%) comprised of NeuAc, Gal, Man, Fuc, GalNAc, and GlcNAc.
6725284	3	49	theme	high	365:368	arg1	Fuc					427:429	Fuc	427:429	Fuc	427:429	255, 3221-3226) was found to possess an unusually high carbohydrate content (76%) comprised of NeuAc, Gal, Man, Fuc, GalNAc, and GlcNAc.
6725284	3	49	theme	high	365:368	arg1	content					383:389	an unusually high carbohydrate content	352:389	an unusually high carbohydrate content (76%) comprised of NeuAc	352:414	255, 3221-3226) was found to possess an unusually high carbohydrate content (76%) comprised of NeuAc, Gal, Man, Fuc, GalNAc, and GlcNAc.
6725284	5	50	theme	chains	624:629	arg1	study					582:586	the study	578:586	the study of the O-glycosidic oligosaccharide chains	578:629	For the study of the O-glycosidic oligosaccharide chains, the protein was subjected to beta-elimination and the resulting oligosaccharide preparations were analyzed by 500-MHz 1H NMR spectroscopy.
6725284	9	51	theme	diantennary	1354:1364	arg1	chains					1379:1384	3 diantennary N-glycosidic chains	1352:1384	3 diantennary N-glycosidic chains that are extended with a Fuc residue at the Asn-linked GlcNAc	1352:1446	500-MHz 1H NMR spectroscopy of the obtained preparations revealed the presence of 3 diantennary N-glycosidic chains that are extended with a Fuc residue at the Asn-linked GlcNAc.
6725284	9	52	theme	N-glycosidic	1366:1377	arg1	chains					1379:1384	3 diantennary N-glycosidic chains	1352:1384	3 diantennary N-glycosidic chains that are extended with a Fuc residue at the Asn-linked GlcNAc	1352:1446	500-MHz 1H NMR spectroscopy of the obtained preparations revealed the presence of 3 diantennary N-glycosidic chains that are extended with a Fuc residue at the Asn-linked GlcNAc.
6725284	8	53	theme	desialyzed	1198:1207	arg1	fraction					1232:1239	the desialyzed resulting glycopeptide fraction	1194:1239	the desialyzed resulting glycopeptide fraction on concanavalin A-Sepharose	1194:1267	For the isolation of its N-glycosidic oligosaccharide chains, the protein was exhaustively digested with proteases followed by chromatography of the desialyzed resulting glycopeptide fraction on concanavalin A-Sepharose.
6725284	1	54	theme	Human	125:129	arg1	Mr					159:160	Mr = 81,000	159:169	Mr = 81,000	159:169	Human plasma galactoglycoprotein (Mr = 81,000) which was recently identified and characterized (Schmid, K., Mao, S. K. Y., Kimura, A., Hayashi, S., and Binette , J. P. (1980) J. Biol.
6725284	1	54	theme	Human	125:129	arg1	galactoglycoprotein					138:156	Human plasma galactoglycoprotein	125:156	Human plasma galactoglycoprotein (Mr = 81,000) which was recently identified and characterized (Schmid, K., Mao, S. K. Y., Kimura, A., Hayashi, S., and Binette , J. P. (1980) J. Biol	125:306	Human plasma galactoglycoprotein (Mr = 81,000) which was recently identified and characterized (Schmid, K., Mao, S. K. Y., Kimura, A., Hayashi, S., and Binette , J. P. (1980) J. Biol.
6725284	8	55	theme	fraction	1232:1239	arg1	chromatography					1176:1189	chromatography	1176:1189	chromatography of the desialyzed resulting glycopeptide fraction on concanavalin A-Sepharose	1176:1267	For the isolation of its N-glycosidic oligosaccharide chains, the protein was exhaustively digested with proteases followed by chromatography of the desialyzed resulting glycopeptide fraction on concanavalin A-Sepharose.
6725284	4	56	theme	units	551:555	arg1	structure					518:526	the primary structure	506:526	the primary structure of the oligosaccharide units of this protein	506:571	The aim of the present investigation was to elucidate the primary structure of the oligosaccharide units of this protein.
6725284	8	57	theme	glycopeptide	1219:1230	arg1	fraction					1232:1239	the desialyzed resulting glycopeptide fraction	1194:1239	the desialyzed resulting glycopeptide fraction on concanavalin A-Sepharose	1194:1267	For the isolation of its N-glycosidic oligosaccharide chains, the protein was exhaustively digested with proteases followed by chromatography of the desialyzed resulting glycopeptide fraction on concanavalin A-Sepharose.
6725284	7	58	contain	possesses	978:986	arg2	hexasaccharides					1005:1019	approximately 40 hexasaccharides	988:1019	approximately 40 hexasaccharides	988:1019	The protein possesses approximately 40 hexasaccharides and 3 tetrasaccharides/mol.
6725284	7	58	contain	possesses	978:986	arg2	tetrasaccharides/mol					1027:1046	3 tetrasaccharides/mol	1025:1046	3 tetrasaccharides/mol	1025:1046	The protein possesses approximately 40 hexasaccharides and 3 tetrasaccharides/mol.
6725284	7	58	contain	possesses	978:986	arg1	protein					970:976	The protein	966:976	The protein	966:976	The protein possesses approximately 40 hexasaccharides and 3 tetrasaccharides/mol.
6725284	4	59	theme	oligosaccharide	535:549	arg1	units					551:555	the oligosaccharide units	531:555	the oligosaccharide units of this protein	531:571	The aim of the present investigation was to elucidate the primary structure of the oligosaccharide units of this protein.
6725284	1	60	theme	plasma	131:136	arg1	Mr					159:160	Mr = 81,000	159:169	Mr = 81,000	159:169	Human plasma galactoglycoprotein (Mr = 81,000) which was recently identified and characterized (Schmid, K., Mao, S. K. Y., Kimura, A., Hayashi, S., and Binette , J. P. (1980) J. Biol.
6725284	1	60	theme	plasma	131:136	arg1	galactoglycoprotein					138:156	Human plasma galactoglycoprotein	125:156	Human plasma galactoglycoprotein (Mr = 81,000) which was recently identified and characterized (Schmid, K., Mao, S. K. Y., Kimura, A., Hayashi, S., and Binette , J. P. (1980) J. Biol	125:306	Human plasma galactoglycoprotein (Mr = 81,000) which was recently identified and characterized (Schmid, K., Mao, S. K. Y., Kimura, A., Hayashi, S., and Binette , J. P. (1980) J. Biol.
6725284	9	61	link	Asn-linked	1430:1439	arg1	GlcNAc					1441:1446	the Asn-linked GlcNAc	1426:1446	the Asn-linked GlcNAc	1426:1446	500-MHz 1H NMR spectroscopy of the obtained preparations revealed the presence of 3 diantennary N-glycosidic chains that are extended with a Fuc residue at the Asn-linked GlcNAc.
6725284	1	62	dep	identified	191:200	arg1	K.					229:230	K.	229:230	K.	229:230	Human plasma galactoglycoprotein (Mr = 81,000) which was recently identified and characterized (Schmid, K., Mao, S. K. Y., Kimura, A., Hayashi, S., and Binette , J. P. (1980) J. Biol.
6725284	1	62	dep	identified	191:200	arg1	J.					287:288	J.	287:288	J.	287:288	Human plasma galactoglycoprotein (Mr = 81,000) which was recently identified and characterized (Schmid, K., Mao, S. K. Y., Kimura, A., Hayashi, S., and Binette , J. P. (1980) J. Biol.
6725284	1	62	dep	identified	191:200	arg1	Kimura					248:253	Kimura	248:253	Kimura	248:253	Human plasma galactoglycoprotein (Mr = 81,000) which was recently identified and characterized (Schmid, K., Mao, S. K. Y., Kimura, A., Hayashi, S., and Binette , J. P. (1980) J. Biol.
6725284	1	62	dep	identified	191:200	arg1	S.					269:270	S.	269:270	S.	269:270	Human plasma galactoglycoprotein (Mr = 81,000) which was recently identified and characterized (Schmid, K., Mao, S. K. Y., Kimura, A., Hayashi, S., and Binette , J. P. (1980) J. Biol.
6725284	1	62	dep	identified	191:200	arg1	S.					238:239	S.	238:239	S.	238:239	Human plasma galactoglycoprotein (Mr = 81,000) which was recently identified and characterized (Schmid, K., Mao, S. K. Y., Kimura, A., Hayashi, S., and Binette , J. P. (1980) J. Biol.
6725284	1	62	dep	identified	191:200	arg1	1980					294:297	1980	294:297	1980	294:297	Human plasma galactoglycoprotein (Mr = 81,000) which was recently identified and characterized (Schmid, K., Mao, S. K. Y., Kimura, A., Hayashi, S., and Binette , J. P. (1980) J. Biol.
6725284	1	62	dep	identified	191:200	arg1	A.					256:257	A.	256:257	A.	256:257	Human plasma galactoglycoprotein (Mr = 81,000) which was recently identified and characterized (Schmid, K., Mao, S. K. Y., Kimura, A., Hayashi, S., and Binette , J. P. (1980) J. Biol.
6725284	6	63	theme	Gal	900:902	arg1	alpha					923:927	1----3)[NeuAc alpha (2----6)	909:936	1----3)[NeuAc alpha (2----6)	909:936	The structure of the predominant glycan, a hexasaccharide: (formula; see text) and that of a tetrasaccharide: NeuAc alpha(2----3)Gal beta(1----3)[NeuAc alpha (2----6)]GalNAc-ol, were determined.
6725284	6	63	theme	Gal	900:902	arg1	beta					904:907	NeuAc alpha(2----3)Gal beta	881:907	a tetrasaccharide: NeuAc alpha(2----3)Gal beta(1----3)[NeuAc alpha (2----6)]GalNAc-ol	862:946	The structure of the predominant glycan, a hexasaccharide: (formula; see text) and that of a tetrasaccharide: NeuAc alpha(2----3)Gal beta(1----3)[NeuAc alpha (2----6)]GalNAc-ol, were determined.
6725284	5	64	theme	resulting	686:694	arg1	preparations					712:723	the resulting oligosaccharide preparations	682:723	the resulting oligosaccharide preparations	682:723	For the study of the O-glycosidic oligosaccharide chains, the protein was subjected to beta-elimination and the resulting oligosaccharide preparations were analyzed by 500-MHz 1H NMR spectroscopy.
6725284	8	65	from	A-Sepharose	1257:1267	arg1	chromatography					1176:1189	chromatography	1176:1189	chromatography of the desialyzed resulting glycopeptide fraction on concanavalin A-Sepharose	1176:1267	For the isolation of its N-glycosidic oligosaccharide chains, the protein was exhaustively digested with proteases followed by chromatography of the desialyzed resulting glycopeptide fraction on concanavalin A-Sepharose.
6725284	0	66	theme	plasma	49:54	arg1	units					34:38	the carbohydrate units	17:38	the carbohydrate units of human plasma	17:54	The structure of the carbohydrate units of human plasma galactoglycoprotein determined by 500-megahertz 1H NMR spectroscopy.
6725284	8	67	theme	chains	1103:1108	arg1	isolation					1057:1065	the isolation	1053:1065	the isolation of its N-glycosidic oligosaccharide chains	1053:1108	For the isolation of its N-glycosidic oligosaccharide chains, the protein was exhaustively digested with proteases followed by chromatography of the desialyzed resulting glycopeptide fraction on concanavalin A-Sepharose.
6725284	8	68	from	chromatography	1176:1189	arg1	A-Sepharose					1257:1267	concanavalin A-Sepharose	1244:1267	concanavalin A-Sepharose	1244:1267	For the isolation of its N-glycosidic oligosaccharide chains, the protein was exhaustively digested with proteases followed by chromatography of the desialyzed resulting glycopeptide fraction on concanavalin A-Sepharose.
32578997	6	0	from	Cys29	953:957	arg1	rhEPO					972:976	rhEPO	972:976	rhEPO	972:976	Here, cysteine aminoethylation using 2-bromoethylamine was applied as an alternative alkylation strategy to introduce artificial tryptic cleavage sites at Cys29 and Cys33 in rhEPO.
32578997	8	1	theme	alkylation	1193:1202	arg1	step					1204:1207	the alkylation step	1189:1207	the alkylation step in a conventional workflow	1189:1234	The new trypsin-based workflow was easily implemented by adapting the alkylation step in a conventional workflow and was directly compared to an established approach using GluC.
32578997	5	2	theme	sole	662:665	arg1	protease					667:674	as the sole protease	655:674	as the sole protease	655:674	The use of trypsin, the gold standard protease in proteomics, as the sole protease for rhEPO is compromised, as no natural tryptic cleavage site is located between the glycosylation sites Asn24 and Asn38.
32578997	5	2	theme	sole	662:665	arg1	trypsin					604:610	trypsin	604:610	trypsin	604:610	The use of trypsin, the gold standard protease in proteomics, as the sole protease for rhEPO is compromised, as no natural tryptic cleavage site is located between the glycosylation sites Asn24 and Asn38.
32578997	1	3	theme	important	172:180	arg1	erythropoietin					143:156	Recombinant human erythropoietin	125:156	Recombinant human erythropoietin (rhEPO)	125:164	Recombinant human erythropoietin (rhEPO) is an important biopharmaceutical for which glycosylation is a critical quality attribute.
32578997	1	3	theme	important	172:180	arg1	biopharmaceutical					182:198	an important biopharmaceutical	169:198	an important biopharmaceutical for which glycosylation is a critical quality attribute	169:254	Recombinant human erythropoietin (rhEPO) is an important biopharmaceutical for which glycosylation is a critical quality attribute.
32578997	10	4	theme	specific	1576:1583	arg1	sites					1585:1589	specific sites	1576:1589	specific sites in parallel to the site-specific glycosylation analysis of rhEPO	1576:1654	Furthermore, the method allows for the monitoring of additional attributes, such as oxidation and deamidation at specific sites in parallel to the site-specific glycosylation analysis of rhEPO.
32578997	9	5	dep	method	1309:1314	arg1	shows					1316:1320	shows	1316:1320	shows an improved specificity	1316:1344	The new method shows an improved specificity, a significantly reduced chromatogram complexity, allows for shorter analysis times, and simplifies data evaluation.
32578997	0	6	theme	Erythropoietin	95:108	arg1	Analysis					65:72	the Site-Specific Glycosylation Analysis	33:72	the Site-Specific Glycosylation Analysis of Recombinant Human Erythropoietin using Trypsin	33:122	Cysteine Aminoethylation Enables the Site-Specific Glycosylation Analysis of Recombinant Human Erythropoietin using Trypsin.
32578997	6	7	theme	cleavage	935:942	arg1	sites					944:948	artificial tryptic cleavage sites	916:948	artificial tryptic cleavage sites	916:948	Here, cysteine aminoethylation using 2-bromoethylamine was applied as an alternative alkylation strategy to introduce artificial tryptic cleavage sites at Cys29 and Cys33 in rhEPO.
32578997	7	8	theme	glyco	984:988	arg1	peptides					990:997	The (glyco)peptides	979:997	The (glyco)peptides resulting from a subsequent digestion using trypsin	979:1049	The (glyco)peptides resulting from a subsequent digestion using trypsin were analyzed by reverse-phase liquid chromatography-mass spectrometry.
32578997	5	9	theme	standard	622:629	arg1	protease					631:638	the gold standard protease	613:638	the gold standard protease in proteomics	613:652	The use of trypsin, the gold standard protease in proteomics, as the sole protease for rhEPO is compromised, as no natural tryptic cleavage site is located between the glycosylation sites Asn24 and Asn38.
32578997	5	9	theme	standard	622:629	arg1	trypsin					604:610	trypsin	604:610	trypsin	604:610	The use of trypsin, the gold standard protease in proteomics, as the sole protease for rhEPO is compromised, as no natural tryptic cleavage site is located between the glycosylation sites Asn24 and Asn38.
32578997	5	10	gly	glycosylation	761:773	arg2	Asn24					781:785	Asn24	781:785	Asn24	781:785	The use of trypsin, the gold standard protease in proteomics, as the sole protease for rhEPO is compromised, as no natural tryptic cleavage site is located between the glycosylation sites Asn24 and Asn38.
32578997	5	10	gly	glycosylation	761:773	arg2	sites					775:779	the glycosylation sites Asn24 and Asn38	757:795	the glycosylation sites Asn24 and Asn38	757:795	The use of trypsin, the gold standard protease in proteomics, as the sole protease for rhEPO is compromised, as no natural tryptic cleavage site is located between the glycosylation sites Asn24 and Asn38.
32578997	5	10	gly	glycosylation	761:773	arg2	Asn38					791:795	Asn38	791:795	Asn38	791:795	The use of trypsin, the gold standard protease in proteomics, as the sole protease for rhEPO is compromised, as no natural tryptic cleavage site is located between the glycosylation sites Asn24 and Asn38.
32578997	10	11	theme	glycosylation	1624:1636	arg1	analysis					1638:1645	the site-specific glycosylation analysis	1606:1645	the site-specific glycosylation analysis of rhEPO	1606:1654	Furthermore, the method allows for the monitoring of additional attributes, such as oxidation and deamidation at specific sites in parallel to the site-specific glycosylation analysis of rhEPO.
32578997	6	12	theme	tryptic	927:933	arg1	sites					944:948	artificial tryptic cleavage sites	916:948	artificial tryptic cleavage sites	916:948	Here, cysteine aminoethylation using 2-bromoethylamine was applied as an alternative alkylation strategy to introduce artificial tryptic cleavage sites at Cys29 and Cys33 in rhEPO.
32578997	6	13	theme	cysteine	804:811	arg1	aminoethylation					813:827	cysteine aminoethylation	804:827	cysteine aminoethylation using 2-bromoethylamine	804:851	Here, cysteine aminoethylation using 2-bromoethylamine was applied as an alternative alkylation strategy to introduce artificial tryptic cleavage sites at Cys29 and Cys33 in rhEPO.
32578997	6	13	theme	cysteine	804:811	arg1	strategy					894:901	an alternative alkylation strategy	868:901	an alternative alkylation strategy to introduce artificial tryptic cleavage sites at Cys29 and Cys33 in rhEPO	868:976	Here, cysteine aminoethylation using 2-bromoethylamine was applied as an alternative alkylation strategy to introduce artificial tryptic cleavage sites at Cys29 and Cys33 in rhEPO.
32578997	2	14	theme	in-depth	313:320	arg1	characterization					322:337	the in-depth characterization	309:337	the in-depth characterization of rhEPO glycosylation	309:360	Therefore, robust analytical methods are needed for the in-depth characterization of rhEPO glycosylation.
32578997	8	15	theme	conventional	1214:1225	arg1	workflow					1227:1234	a conventional workflow	1212:1234	a conventional workflow	1212:1234	The new trypsin-based workflow was easily implemented by adapting the alkylation step in a conventional workflow and was directly compared to an established approach using GluC.
32578997	6	16	theme	artificial	916:925	arg1	sites					944:948	artificial tryptic cleavage sites	916:948	artificial tryptic cleavage sites	916:948	Here, cysteine aminoethylation using 2-bromoethylamine was applied as an alternative alkylation strategy to introduce artificial tryptic cleavage sites at Cys29 and Cys33 in rhEPO.
32578997	3	17	gly	glycosylation	436:448	arg1	rhEPO					462:466	rhEPO	462:466	rhEPO	462:466	Currently, the protease GluC is widely established for the site-specific glycosylation analysis of rhEPO.
32578997	9	18	theme	reduced	1363:1369	arg1	complexity					1384:1393	a significantly reduced chromatogram complexity	1347:1393	a significantly reduced chromatogram complexity	1347:1393	The new method shows an improved specificity, a significantly reduced chromatogram complexity, allows for shorter analysis times, and simplifies data evaluation.
32578997	9	18	theme	reduced	1363:1369	arg1	method					1309:1314	The new method	1301:1314	The new method shows an improved specificity	1301:1344	The new method shows an improved specificity, a significantly reduced chromatogram complexity, allows for shorter analysis times, and simplifies data evaluation.
32578997	0	19	theme	Glycosylation	51:63	arg1	Analysis					65:72	the Site-Specific Glycosylation Analysis	33:72	the Site-Specific Glycosylation Analysis of Recombinant Human Erythropoietin using Trypsin	33:122	Cysteine Aminoethylation Enables the Site-Specific Glycosylation Analysis of Recombinant Human Erythropoietin using Trypsin.
32578997	0	20	theme	Cysteine	0:7	arg1	Aminoethylation					9:23	Cysteine Aminoethylation	0:23	Cysteine Aminoethylation	0:23	Cysteine Aminoethylation Enables the Site-Specific Glycosylation Analysis of Recombinant Human Erythropoietin using Trypsin.
32578997	10	21	theme	site-specific	1610:1622	arg1	analysis					1638:1645	the site-specific glycosylation analysis	1606:1645	the site-specific glycosylation analysis of rhEPO	1606:1654	Furthermore, the method allows for the monitoring of additional attributes, such as oxidation and deamidation at specific sites in parallel to the site-specific glycosylation analysis of rhEPO.
32578997	3	22	theme	site-specific	422:434	arg1	analysis					450:457	the site-specific glycosylation analysis	418:457	the site-specific glycosylation analysis of rhEPO	418:466	Currently, the protease GluC is widely established for the site-specific glycosylation analysis of rhEPO.
32578997	9	23	theme	chromatogram	1371:1382	arg1	complexity					1384:1393	a significantly reduced chromatogram complexity	1347:1393	a significantly reduced chromatogram complexity	1347:1393	The new method shows an improved specificity, a significantly reduced chromatogram complexity, allows for shorter analysis times, and simplifies data evaluation.
32578997	9	23	theme	chromatogram	1371:1382	arg1	method					1309:1314	The new method	1301:1314	The new method shows an improved specificity	1301:1344	The new method shows an improved specificity, a significantly reduced chromatogram complexity, allows for shorter analysis times, and simplifies data evaluation.
32578997	5	24	theme	trypsin	604:610	arg1	use					597:599	The use	593:599	The use of trypsin, the gold standard protease in proteomics, as the sole protease for rhEPO	593:684	The use of trypsin, the gold standard protease in proteomics, as the sole protease for rhEPO is compromised, as no natural tryptic cleavage site is located between the glycosylation sites Asn24 and Asn38.
32578997	3	25	theme	glycosylation	436:448	arg1	analysis					450:457	the site-specific glycosylation analysis	418:457	the site-specific glycosylation analysis of rhEPO	418:466	Currently, the protease GluC is widely established for the site-specific glycosylation analysis of rhEPO.
32578997	2	26	theme	glycosylation	348:360	arg1	characterization					322:337	the in-depth characterization	309:337	the in-depth characterization of rhEPO glycosylation	309:360	Therefore, robust analytical methods are needed for the in-depth characterization of rhEPO glycosylation.
32578997	10	27	from	sites	1585:1589	arg1	parallel					1594:1601	parallel	1594:1601	parallel to the site-specific glycosylation analysis of rhEPO	1594:1654	Furthermore, the method allows for the monitoring of additional attributes, such as oxidation and deamidation at specific sites in parallel to the site-specific glycosylation analysis of rhEPO.
32578997	10	27	from	sites	1585:1589	arg1	deamidation					1561:1571	deamidation	1561:1571	deamidation	1561:1571	Furthermore, the method allows for the monitoring of additional attributes, such as oxidation and deamidation at specific sites in parallel to the site-specific glycosylation analysis of rhEPO.
32578997	10	27	from	sites	1585:1589	arg1	oxidation					1547:1555	oxidation	1547:1555	oxidation	1547:1555	Furthermore, the method allows for the monitoring of additional attributes, such as oxidation and deamidation at specific sites in parallel to the site-specific glycosylation analysis of rhEPO.
32578997	10	28	theme	rhEPO	1650:1654	arg1	analysis					1638:1645	the site-specific glycosylation analysis	1606:1645	the site-specific glycosylation analysis of rhEPO	1606:1654	Furthermore, the method allows for the monitoring of additional attributes, such as oxidation and deamidation at specific sites in parallel to the site-specific glycosylation analysis of rhEPO.
32578997	4	29	theme	peptides	583:590	arg1	specificity					523:533	its specificity	519:533	its specificity	519:533	However, this enzyme shows disadvantages, such as its specificity and the characteristics of the resulting (glyco)peptides.
32578997	4	29	theme	peptides	583:590	arg1	characteristics					543:557	the characteristics	539:557	the characteristics of the resulting (glyco)peptides	539:590	However, this enzyme shows disadvantages, such as its specificity and the characteristics of the resulting (glyco)peptides.
32578997	5	30	dep	sites	775:779	arg1	sites					775:779	the glycosylation sites Asn24 and Asn38	757:795	the glycosylation sites Asn24 and Asn38	757:795	The use of trypsin, the gold standard protease in proteomics, as the sole protease for rhEPO is compromised, as no natural tryptic cleavage site is located between the glycosylation sites Asn24 and Asn38.
32578997	5	30	dep	sites	775:779	arg1	Asn38					791:795	Asn38	791:795	Asn38	791:795	The use of trypsin, the gold standard protease in proteomics, as the sole protease for rhEPO is compromised, as no natural tryptic cleavage site is located between the glycosylation sites Asn24 and Asn38.
32578997	5	30	dep	sites	775:779	arg1	Asn24					781:785	Asn24	781:785	Asn24	781:785	The use of trypsin, the gold standard protease in proteomics, as the sole protease for rhEPO is compromised, as no natural tryptic cleavage site is located between the glycosylation sites Asn24 and Asn38.
32578997	2	31	theme	rhEPO	342:346	arg1	glycosylation					348:360	rhEPO glycosylation	342:360	rhEPO glycosylation	342:360	Therefore, robust analytical methods are needed for the in-depth characterization of rhEPO glycosylation.
32578997	7	32	theme	reverse-phase	1068:1080	arg1	spectrometry					1109:1120	reverse-phase liquid chromatography-mass spectrometry	1068:1120	reverse-phase liquid chromatography-mass spectrometry	1068:1120	The (glyco)peptides resulting from a subsequent digestion using trypsin were analyzed by reverse-phase liquid chromatography-mass spectrometry.
32578997	5	33	theme	natural	708:714	arg1	site					733:736	no natural tryptic cleavage site	705:736	no natural tryptic cleavage site	705:736	The use of trypsin, the gold standard protease in proteomics, as the sole protease for rhEPO is compromised, as no natural tryptic cleavage site is located between the glycosylation sites Asn24 and Asn38.
32578997	1	34	theme	human	137:141	arg1	rhEPO					159:163	rhEPO	159:163	rhEPO	159:163	Recombinant human erythropoietin (rhEPO) is an important biopharmaceutical for which glycosylation is a critical quality attribute.
32578997	1	34	theme	human	137:141	arg1	erythropoietin					143:156	Recombinant human erythropoietin	125:156	Recombinant human erythropoietin (rhEPO)	125:164	Recombinant human erythropoietin (rhEPO) is an important biopharmaceutical for which glycosylation is a critical quality attribute.
32578997	1	34	theme	human	137:141	arg1	biopharmaceutical					182:198	an important biopharmaceutical	169:198	an important biopharmaceutical for which glycosylation is a critical quality attribute	169:254	Recombinant human erythropoietin (rhEPO) is an important biopharmaceutical for which glycosylation is a critical quality attribute.
32578997	1	35	theme	critical	229:236	arg1	glycosylation					210:222	glycosylation	210:222	glycosylation	210:222	Recombinant human erythropoietin (rhEPO) is an important biopharmaceutical for which glycosylation is a critical quality attribute.
32578997	1	35	theme	critical	229:236	arg1	attribute					246:254	a critical quality attribute	227:254	a critical quality attribute	227:254	Recombinant human erythropoietin (rhEPO) is an important biopharmaceutical for which glycosylation is a critical quality attribute.
32578997	3	36	theme	rhEPO	462:466	arg1	analysis					450:457	the site-specific glycosylation analysis	418:457	the site-specific glycosylation analysis of rhEPO	418:466	Currently, the protease GluC is widely established for the site-specific glycosylation analysis of rhEPO.
32578997	5	37	theme	tryptic	716:722	arg1	site					733:736	no natural tryptic cleavage site	705:736	no natural tryptic cleavage site	705:736	The use of trypsin, the gold standard protease in proteomics, as the sole protease for rhEPO is compromised, as no natural tryptic cleavage site is located between the glycosylation sites Asn24 and Asn38.
32578997	6	38	theme	alkylation	883:892	arg1	aminoethylation					813:827	cysteine aminoethylation	804:827	cysteine aminoethylation using 2-bromoethylamine	804:851	Here, cysteine aminoethylation using 2-bromoethylamine was applied as an alternative alkylation strategy to introduce artificial tryptic cleavage sites at Cys29 and Cys33 in rhEPO.
32578997	6	38	theme	alkylation	883:892	arg1	strategy					894:901	an alternative alkylation strategy	868:901	an alternative alkylation strategy to introduce artificial tryptic cleavage sites at Cys29 and Cys33 in rhEPO	868:976	Here, cysteine aminoethylation using 2-bromoethylamine was applied as an alternative alkylation strategy to introduce artificial tryptic cleavage sites at Cys29 and Cys33 in rhEPO.
32578997	2	39	theme	robust	268:273	arg1	methods					286:292	robust analytical methods	268:292	robust analytical methods	268:292	Therefore, robust analytical methods are needed for the in-depth characterization of rhEPO glycosylation.
32578997	1	40	theme	quality	238:244	arg1	glycosylation					210:222	glycosylation	210:222	glycosylation	210:222	Recombinant human erythropoietin (rhEPO) is an important biopharmaceutical for which glycosylation is a critical quality attribute.
32578997	1	40	theme	quality	238:244	arg1	attribute					246:254	a critical quality attribute	227:254	a critical quality attribute	227:254	Recombinant human erythropoietin (rhEPO) is an important biopharmaceutical for which glycosylation is a critical quality attribute.
32578997	0	41	theme	Site-Specific	37:49	arg1	Analysis					65:72	the Site-Specific Glycosylation Analysis	33:72	the Site-Specific Glycosylation Analysis of Recombinant Human Erythropoietin using Trypsin	33:122	Cysteine Aminoethylation Enables the Site-Specific Glycosylation Analysis of Recombinant Human Erythropoietin using Trypsin.
32578997	9	42	theme	shorter	1407:1413	arg1	times					1424:1428	shorter analysis times	1407:1428	shorter analysis times	1407:1428	The new method shows an improved specificity, a significantly reduced chromatogram complexity, allows for shorter analysis times, and simplifies data evaluation.
32578997	5	43	theme	cleavage	724:731	arg1	site					733:736	no natural tryptic cleavage site	705:736	no natural tryptic cleavage site	705:736	The use of trypsin, the gold standard protease in proteomics, as the sole protease for rhEPO is compromised, as no natural tryptic cleavage site is located between the glycosylation sites Asn24 and Asn38.
32578997	6	44	theme	alternative	871:881	arg1	aminoethylation					813:827	cysteine aminoethylation	804:827	cysteine aminoethylation using 2-bromoethylamine	804:851	Here, cysteine aminoethylation using 2-bromoethylamine was applied as an alternative alkylation strategy to introduce artificial tryptic cleavage sites at Cys29 and Cys33 in rhEPO.
32578997	6	44	theme	alternative	871:881	arg1	strategy					894:901	an alternative alkylation strategy	868:901	an alternative alkylation strategy to introduce artificial tryptic cleavage sites at Cys29 and Cys33 in rhEPO	868:976	Here, cysteine aminoethylation using 2-bromoethylamine was applied as an alternative alkylation strategy to introduce artificial tryptic cleavage sites at Cys29 and Cys33 in rhEPO.
32578997	10	45	gly	glycosylation	1624:1636	arg1	rhEPO					1650:1654	rhEPO	1650:1654	rhEPO	1650:1654	Furthermore, the method allows for the monitoring of additional attributes, such as oxidation and deamidation at specific sites in parallel to the site-specific glycosylation analysis of rhEPO.
32578997	8	46	theme	established	1268:1278	arg1	approach					1280:1287	an established approach	1265:1287	an established approach using GluC	1265:1298	The new trypsin-based workflow was easily implemented by adapting the alkylation step in a conventional workflow and was directly compared to an established approach using GluC.
32578997	4	47	theme	resulting	566:574	arg1	peptides					583:590	the resulting (glyco)peptides	562:590	the resulting (glyco)peptides	562:590	However, this enzyme shows disadvantages, such as its specificity and the characteristics of the resulting (glyco)peptides.
32578997	6	48	from	Cys33	963:967	arg1	rhEPO					972:976	rhEPO	972:976	rhEPO	972:976	Here, cysteine aminoethylation using 2-bromoethylamine was applied as an alternative alkylation strategy to introduce artificial tryptic cleavage sites at Cys29 and Cys33 in rhEPO.
32578997	3	49	theme	protease	378:385	arg1	GluC					387:390	the protease GluC	374:390	the protease GluC	374:390	Currently, the protease GluC is widely established for the site-specific glycosylation analysis of rhEPO.
32578997	7	50	theme	liquid	1082:1087	arg1	spectrometry					1109:1120	reverse-phase liquid chromatography-mass spectrometry	1068:1120	reverse-phase liquid chromatography-mass spectrometry	1068:1120	The (glyco)peptides resulting from a subsequent digestion using trypsin were analyzed by reverse-phase liquid chromatography-mass spectrometry.
32578997	7	51	theme	chromatography-mass	1089:1107	arg1	spectrometry					1109:1120	reverse-phase liquid chromatography-mass spectrometry	1068:1120	reverse-phase liquid chromatography-mass spectrometry	1068:1120	The (glyco)peptides resulting from a subsequent digestion using trypsin were analyzed by reverse-phase liquid chromatography-mass spectrometry.
32578997	10	52	theme	additional	1516:1525	arg1	deamidation					1561:1571	deamidation	1561:1571	deamidation	1561:1571	Furthermore, the method allows for the monitoring of additional attributes, such as oxidation and deamidation at specific sites in parallel to the site-specific glycosylation analysis of rhEPO.
32578997	10	52	theme	additional	1516:1525	arg1	oxidation					1547:1555	oxidation	1547:1555	oxidation	1547:1555	Furthermore, the method allows for the monitoring of additional attributes, such as oxidation and deamidation at specific sites in parallel to the site-specific glycosylation analysis of rhEPO.
32578997	10	52	theme	additional	1516:1525	arg1	attributes					1527:1536	additional attributes	1516:1536	additional attributes	1516:1536	Furthermore, the method allows for the monitoring of additional attributes, such as oxidation and deamidation at specific sites in parallel to the site-specific glycosylation analysis of rhEPO.
32578997	9	53	theme	improved	1325:1332	arg1	specificity					1334:1344	an improved specificity	1322:1344	an improved specificity	1322:1344	The new method shows an improved specificity, a significantly reduced chromatogram complexity, allows for shorter analysis times, and simplifies data evaluation.
32578997	4	54	theme	glyco	577:581	arg1	peptides					583:590	the resulting (glyco)peptides	562:590	the resulting (glyco)peptides	562:590	However, this enzyme shows disadvantages, such as its specificity and the characteristics of the resulting (glyco)peptides.
32578997	8	55	theme	trypsin-based	1131:1143	arg1	workflow					1145:1152	The new trypsin-based workflow	1123:1152	The new trypsin-based workflow	1123:1152	The new trypsin-based workflow was easily implemented by adapting the alkylation step in a conventional workflow and was directly compared to an established approach using GluC.
32578997	9	56	theme	new	1305:1307	arg1	complexity					1384:1393	a significantly reduced chromatogram complexity	1347:1393	a significantly reduced chromatogram complexity	1347:1393	The new method shows an improved specificity, a significantly reduced chromatogram complexity, allows for shorter analysis times, and simplifies data evaluation.
32578997	9	56	theme	new	1305:1307	arg1	method					1309:1314	The new method	1301:1314	The new method shows an improved specificity	1301:1344	The new method shows an improved specificity, a significantly reduced chromatogram complexity, allows for shorter analysis times, and simplifies data evaluation.
32578997	5	57	theme	glycosylation	761:773	arg1	sites					775:779	the glycosylation sites Asn24 and Asn38	757:795	the glycosylation sites Asn24 and Asn38	757:795	The use of trypsin, the gold standard protease in proteomics, as the sole protease for rhEPO is compromised, as no natural tryptic cleavage site is located between the glycosylation sites Asn24 and Asn38.
32578997	5	57	theme	glycosylation	761:773	arg1	Asn38					791:795	Asn38	791:795	Asn38	791:795	The use of trypsin, the gold standard protease in proteomics, as the sole protease for rhEPO is compromised, as no natural tryptic cleavage site is located between the glycosylation sites Asn24 and Asn38.
32578997	5	57	theme	glycosylation	761:773	arg1	Asn24					781:785	Asn24	781:785	Asn24	781:785	The use of trypsin, the gold standard protease in proteomics, as the sole protease for rhEPO is compromised, as no natural tryptic cleavage site is located between the glycosylation sites Asn24 and Asn38.
32578997	1	58	theme	Recombinant	125:135	arg1	rhEPO					159:163	rhEPO	159:163	rhEPO	159:163	Recombinant human erythropoietin (rhEPO) is an important biopharmaceutical for which glycosylation is a critical quality attribute.
32578997	1	58	theme	Recombinant	125:135	arg1	erythropoietin					143:156	Recombinant human erythropoietin	125:156	Recombinant human erythropoietin (rhEPO)	125:164	Recombinant human erythropoietin (rhEPO) is an important biopharmaceutical for which glycosylation is a critical quality attribute.
32578997	1	58	theme	Recombinant	125:135	arg1	biopharmaceutical					182:198	an important biopharmaceutical	169:198	an important biopharmaceutical for which glycosylation is a critical quality attribute	169:254	Recombinant human erythropoietin (rhEPO) is an important biopharmaceutical for which glycosylation is a critical quality attribute.
32578997	7	59	theme	subsequent	1016:1025	arg1	digestion					1027:1035	a subsequent digestion	1014:1035	a subsequent digestion using trypsin	1014:1049	The (glyco)peptides resulting from a subsequent digestion using trypsin were analyzed by reverse-phase liquid chromatography-mass spectrometry.
32578997	10	60	theme	attributes	1527:1536	arg1	monitoring					1502:1511	the monitoring	1498:1511	the monitoring of additional attributes, such as oxidation and deamidation at specific sites in parallel to the site-specific glycosylation analysis of rhEPO	1498:1654	Furthermore, the method allows for the monitoring of additional attributes, such as oxidation and deamidation at specific sites in parallel to the site-specific glycosylation analysis of rhEPO.
32578997	0	61	theme	Human	89:93	arg1	Erythropoietin					95:108	Recombinant Human Erythropoietin	77:108	Recombinant Human Erythropoietin using Trypsin	77:122	Cysteine Aminoethylation Enables the Site-Specific Glycosylation Analysis of Recombinant Human Erythropoietin using Trypsin.
32578997	8	62	from	step	1204:1207	arg1	workflow					1227:1234	a conventional workflow	1212:1234	a conventional workflow	1212:1234	The new trypsin-based workflow was easily implemented by adapting the alkylation step in a conventional workflow and was directly compared to an established approach using GluC.
32578997	5	63	from	protease	631:638	arg1	proteomics					643:652	proteomics	643:652	proteomics	643:652	The use of trypsin, the gold standard protease in proteomics, as the sole protease for rhEPO is compromised, as no natural tryptic cleavage site is located between the glycosylation sites Asn24 and Asn38.
32578997	9	64	theme	data	1446:1449	arg1	evaluation					1451:1460	data evaluation	1446:1460	data evaluation	1446:1460	The new method shows an improved specificity, a significantly reduced chromatogram complexity, allows for shorter analysis times, and simplifies data evaluation.
32578997	0	65	theme	Recombinant	77:87	arg1	Erythropoietin					95:108	Recombinant Human Erythropoietin	77:108	Recombinant Human Erythropoietin using Trypsin	77:122	Cysteine Aminoethylation Enables the Site-Specific Glycosylation Analysis of Recombinant Human Erythropoietin using Trypsin.
32578997	2	66	theme	analytical	275:284	arg1	methods					286:292	robust analytical methods	268:292	robust analytical methods	268:292	Therefore, robust analytical methods are needed for the in-depth characterization of rhEPO glycosylation.
32578997	8	67	theme	new	1127:1129	arg1	workflow					1145:1152	The new trypsin-based workflow	1123:1152	The new trypsin-based workflow	1123:1152	The new trypsin-based workflow was easily implemented by adapting the alkylation step in a conventional workflow and was directly compared to an established approach using GluC.
32578997	9	68	theme	analysis	1415:1422	arg1	times					1424:1428	shorter analysis times	1407:1428	shorter analysis times	1407:1428	The new method shows an improved specificity, a significantly reduced chromatogram complexity, allows for shorter analysis times, and simplifies data evaluation.
8999954	5	0	theme	human	776:780	arg1	MCF-7					803:807	MCF-7	803:807	MCF-7	803:807	Wheat germ agglutinin-Sepharose affinity chromatography also readily detected terminal GlcNAc residues on subpopulations of ER purified from calf uterus, from human breast cancer cells (MCF-7), or from mER produced by in vitro translation.
8999954	5	0	theme	human	776:780	arg1	cells					796:800	human breast cancer cells	776:800	human breast cancer cells (MCF-7)	776:808	Wheat germ agglutinin-Sepharose affinity chromatography also readily detected terminal GlcNAc residues on subpopulations of ER purified from calf uterus, from human breast cancer cells (MCF-7), or from mER produced by in vitro translation.
8999954	5	1	theme	affinity	649:656	arg1	chromatography					658:671	Wheat germ agglutinin-Sepharose affinity chromatography	617:671	Wheat germ agglutinin-Sepharose affinity chromatography	617:671	Wheat germ agglutinin-Sepharose affinity chromatography also readily detected terminal GlcNAc residues on subpopulations of ER purified from calf uterus, from human breast cancer cells (MCF-7), or from mER produced by in vitro translation.
8999954	1	2	theme	Ser	164:166	arg1	-O-phosphorylation					172:189	Ser(Thr)-O-phosphorylation	164:189	Ser(Thr)-O-phosphorylation	164:189	Estrogen receptors (ER) are ligand-inducible transcription factors regulated by Ser(Thr)-O-phosphorylation.
8999954	4	3	theme	milk	556:559	arg1	galactosyltransferase					561:581	bovine milk galactosyltransferase	549:581	bovine milk galactosyltransferase	549:581	O-GlcNAc moieties were detected on insect cell-expressed, mouse ER (mER) by probing with bovine milk galactosyltransferase, followed by structural analysis.
8999954	5	4	theme	breast	782:787	arg1	MCF-7					803:807	MCF-7	803:807	MCF-7	803:807	Wheat germ agglutinin-Sepharose affinity chromatography also readily detected terminal GlcNAc residues on subpopulations of ER purified from calf uterus, from human breast cancer cells (MCF-7), or from mER produced by in vitro translation.
8999954	5	4	theme	breast	782:787	arg1	cells					796:800	human breast cancer cells	776:800	human breast cancer cells (MCF-7)	776:808	Wheat germ agglutinin-Sepharose affinity chromatography also readily detected terminal GlcNAc residues on subpopulations of ER purified from calf uterus, from human breast cancer cells (MCF-7), or from mER produced by in vitro translation.
8999954	7	5	theme	carboxyl-terminal	1084:1100	arg1	domain					1104:1109	the carboxyl-terminal F domain	1080:1109	the carboxyl-terminal F domain	1080:1109	Site mapping of insect cell expressed mER localized one major site of O-GlcNAc addition to Thr-575, within a PEST region of the carboxyl-terminal F domain.
8999954	2	6	mod	modified	280:287	arg3	moieties					330:337	Ser(Thr)-O-linked N-acetylglucosamine moieties	292:337	Ser(Thr)-O-linked N-acetylglucosamine moieties (O-GlcNAc)	292:348	Many transcription factors and eukaryotic RNA polymerase II itself are also dynamically modified by Ser(Thr)-O-linked N-acetylglucosamine moieties (O-GlcNAc).
8999954	2	6	mod	modified	280:287	arg1	polymerase					238:247	eukaryotic RNA polymerase II	223:250	eukaryotic RNA polymerase II	223:250	Many transcription factors and eukaryotic RNA polymerase II itself are also dynamically modified by Ser(Thr)-O-linked N-acetylglucosamine moieties (O-GlcNAc).
8999954	2	6	mod	modified	280:287	arg3	O-GlcNAc					340:347	O-GlcNAc	340:347	O-GlcNAc	340:347	Many transcription factors and eukaryotic RNA polymerase II itself are also dynamically modified by Ser(Thr)-O-linked N-acetylglucosamine moieties (O-GlcNAc).
8999954	2	6	mod	modified	280:287	arg1	factors					211:217	Many transcription factors	192:217	Many transcription factors	192:217	Many transcription factors and eukaryotic RNA polymerase II itself are also dynamically modified by Ser(Thr)-O-linked N-acetylglucosamine moieties (O-GlcNAc).
8999954	4	7	located	detected	483:490	arg1	cell-expressed					502:515	insect cell-expressed	495:515	insect cell-expressed	495:515	O-GlcNAc moieties were detected on insect cell-expressed, mouse ER (mER) by probing with bovine milk galactosyltransferase, followed by structural analysis.
8999954	4	7	located	detected	483:490	arg1	ER					524:525	mouse ER	518:525	mouse ER (mER)	518:531	O-GlcNAc moieties were detected on insect cell-expressed, mouse ER (mER) by probing with bovine milk galactosyltransferase, followed by structural analysis.
8999954	4	7	located	detected	483:490	arg2	moieties					469:476	O-GlcNAc moieties	460:476	O-GlcNAc moieties	460:476	O-GlcNAc moieties were detected on insect cell-expressed, mouse ER (mER) by probing with bovine milk galactosyltransferase, followed by structural analysis.
8999954	4	8	theme	bovine	549:554	arg1	galactosyltransferase					561:581	bovine milk galactosyltransferase	549:581	bovine milk galactosyltransferase	549:581	O-GlcNAc moieties were detected on insect cell-expressed, mouse ER (mER) by probing with bovine milk galactosyltransferase, followed by structural analysis.
8999954	2	9	theme	Ser	292:294	arg1	O-GlcNAc					340:347	O-GlcNAc	340:347	O-GlcNAc	340:347	Many transcription factors and eukaryotic RNA polymerase II itself are also dynamically modified by Ser(Thr)-O-linked N-acetylglucosamine moieties (O-GlcNAc).
8999954	2	9	theme	Ser	292:294	arg1	moieties					330:337	Ser(Thr)-O-linked N-acetylglucosamine moieties	292:337	Ser(Thr)-O-linked N-acetylglucosamine moieties (O-GlcNAc)	292:348	Many transcription factors and eukaryotic RNA polymerase II itself are also dynamically modified by Ser(Thr)-O-linked N-acetylglucosamine moieties (O-GlcNAc).
8999954	5	10	theme	calf	758:761	arg1	uterus					763:768	calf uterus	758:768	calf uterus	758:768	Wheat germ agglutinin-Sepharose affinity chromatography also readily detected terminal GlcNAc residues on subpopulations of ER purified from calf uterus, from human breast cancer cells (MCF-7), or from mER produced by in vitro translation.
8999954	4	11	theme	O-GlcNAc	460:467	arg1	moieties					469:476	O-GlcNAc moieties	460:476	O-GlcNAc moieties	460:476	O-GlcNAc moieties were detected on insect cell-expressed, mouse ER (mER) by probing with bovine milk galactosyltransferase, followed by structural analysis.
8999954	3	12	theme	receptors	424:432	arg1	subpopulations					371:384	subpopulations	371:384	subpopulations of murine, bovine, and human estrogen receptors	371:432	Here we report that subpopulations of murine, bovine, and human estrogen receptors are modified by O-GlcNAc.
8999954	7	13	theme	domain	1104:1109	arg1	region					1070:1075	a PEST region	1063:1075	a PEST region of the carboxyl-terminal F domain	1063:1109	Site mapping of insect cell expressed mER localized one major site of O-GlcNAc addition to Thr-575, within a PEST region of the carboxyl-terminal F domain.
8999954	9	14	theme	saccharide	1279:1288	arg1	modification					1290:1301	This dynamic saccharide modification	1266:1301	This dynamic saccharide modification	1266:1301	This dynamic saccharide modification, like phosphorylation, may play a role in modulating the dimerization, stability, or transactivation functions of estrogen receptors.
8999954	5	15	theme	Wheat	617:621	arg1	germ					623:626	Wheat germ	617:626	Wheat germ agglutinin-Sepharose affinity chromatography	617:671	Wheat germ agglutinin-Sepharose affinity chromatography also readily detected terminal GlcNAc residues on subpopulations of ER purified from calf uterus, from human breast cancer cells (MCF-7), or from mER produced by in vitro translation.
8999954	8	16	theme	native	1254:1259	arg1	mER					1261:1263	native mER	1254:1263	native mER	1254:1263	Based upon their relative resistance to both hexosaminidase and to in vitro galactosylation, O-GlcNAc moieties appear to be largely buried on native mER.
8999954	1	17	theme	Estrogen	84:91	arg1	factors					143:149	ligand-inducible transcription factors	112:149	ligand-inducible transcription factors regulated by Ser(Thr)-O-phosphorylation	112:189	Estrogen receptors (ER) are ligand-inducible transcription factors regulated by Ser(Thr)-O-phosphorylation.
8999954	1	17	theme	Estrogen	84:91	arg1	ER					104:105	ER	104:105	ER	104:105	Estrogen receptors (ER) are ligand-inducible transcription factors regulated by Ser(Thr)-O-phosphorylation.
8999954	1	17	theme	Estrogen	84:91	arg1	receptors					93:101	Estrogen receptors	84:101	Estrogen receptors (ER)	84:106	Estrogen receptors (ER) are ligand-inducible transcription factors regulated by Ser(Thr)-O-phosphorylation.
8999954	6	18	theme	receptors	931:939	arg1	populations					907:917	these populations	901:917	these populations of estrogen receptors	901:939	These data suggest that greater than 10% of these populations of estrogen receptors bear O-GlcNAc.
8999954	5	19	theme	germ	623:626	arg1	chromatography					658:671	Wheat germ agglutinin-Sepharose affinity chromatography	617:671	Wheat germ agglutinin-Sepharose affinity chromatography	617:671	Wheat germ agglutinin-Sepharose affinity chromatography also readily detected terminal GlcNAc residues on subpopulations of ER purified from calf uterus, from human breast cancer cells (MCF-7), or from mER produced by in vitro translation.
8999954	4	20	dep	detected	483:490	arg1	followed					584:591	followed	584:591	followed by structural analysis	584:614	O-GlcNAc moieties were detected on insect cell-expressed, mouse ER (mER) by probing with bovine milk galactosyltransferase, followed by structural analysis.
8999954	2	21	theme	N-acetylglucosamine	310:328	arg1	O-GlcNAc					340:347	O-GlcNAc	340:347	O-GlcNAc	340:347	Many transcription factors and eukaryotic RNA polymerase II itself are also dynamically modified by Ser(Thr)-O-linked N-acetylglucosamine moieties (O-GlcNAc).
8999954	2	21	theme	N-acetylglucosamine	310:328	arg1	moieties					330:337	Ser(Thr)-O-linked N-acetylglucosamine moieties	292:337	Ser(Thr)-O-linked N-acetylglucosamine moieties (O-GlcNAc)	292:348	Many transcription factors and eukaryotic RNA polymerase II itself are also dynamically modified by Ser(Thr)-O-linked N-acetylglucosamine moieties (O-GlcNAc).
8999954	9	22	theme	dynamic	1271:1277	arg1	modification					1290:1301	This dynamic saccharide modification	1266:1301	This dynamic saccharide modification	1266:1301	This dynamic saccharide modification, like phosphorylation, may play a role in modulating the dimerization, stability, or transactivation functions of estrogen receptors.
8999954	3	23	theme	human	409:413	arg1	receptors					424:432	murine, bovine, and human estrogen receptors	389:432	murine, bovine, and human estrogen receptors	389:432	Here we report that subpopulations of murine, bovine, and human estrogen receptors are modified by O-GlcNAc.
8999954	3	24	theme	murine	389:394	arg1	receptors					424:432	murine, bovine, and human estrogen receptors	389:432	murine, bovine, and human estrogen receptors	389:432	Here we report that subpopulations of murine, bovine, and human estrogen receptors are modified by O-GlcNAc.
8999954	0	25	mod	modified	42:49	arg3	N-acetylglucosamine					63:81	O-linked N-acetylglucosamine	54:81	O-linked N-acetylglucosamine	54:81	A subpopulation of estrogen receptors are modified by O-linked N-acetylglucosamine.
8999954	0	25	mod	modified	42:49	arg1	subpopulation					2:14	A subpopulation	0:14	A subpopulation of estrogen receptors	0:36	A subpopulation of estrogen receptors are modified by O-linked N-acetylglucosamine.
8999954	5	26	theme	agglutinin-Sepharose	628:647	arg1	chromatography					658:671	Wheat germ agglutinin-Sepharose affinity chromatography	617:671	Wheat germ agglutinin-Sepharose affinity chromatography	617:671	Wheat germ agglutinin-Sepharose affinity chromatography also readily detected terminal GlcNAc residues on subpopulations of ER purified from calf uterus, from human breast cancer cells (MCF-7), or from mER produced by in vitro translation.
8999954	2	27	theme	-O-linked	300:308	arg1	O-GlcNAc					340:347	O-GlcNAc	340:347	O-GlcNAc	340:347	Many transcription factors and eukaryotic RNA polymerase II itself are also dynamically modified by Ser(Thr)-O-linked N-acetylglucosamine moieties (O-GlcNAc).
8999954	2	27	theme	-O-linked	300:308	arg1	moieties					330:337	Ser(Thr)-O-linked N-acetylglucosamine moieties	292:337	Ser(Thr)-O-linked N-acetylglucosamine moieties (O-GlcNAc)	292:348	Many transcription factors and eukaryotic RNA polymerase II itself are also dynamically modified by Ser(Thr)-O-linked N-acetylglucosamine moieties (O-GlcNAc).
8999954	3	28	theme	estrogen	415:422	arg1	receptors					424:432	murine, bovine, and human estrogen receptors	389:432	murine, bovine, and human estrogen receptors	389:432	Here we report that subpopulations of murine, bovine, and human estrogen receptors are modified by O-GlcNAc.
8999954	0	29	theme	estrogen	19:26	arg1	receptors					28:36	estrogen receptors	19:36	estrogen receptors	19:36	A subpopulation of estrogen receptors are modified by O-linked N-acetylglucosamine.
8999954	8	30	theme	relative	1129:1136	arg1	resistance					1138:1147	their relative resistance	1123:1147	their relative resistance to both hexosaminidase and to in vitro galactosylation	1123:1202	Based upon their relative resistance to both hexosaminidase and to in vitro galactosylation, O-GlcNAc moieties appear to be largely buried on native mER.
8999954	9	31	theme	transactivation	1388:1402	arg1	functions					1404:1412	transactivation functions	1388:1412	transactivation functions	1388:1412	This dynamic saccharide modification, like phosphorylation, may play a role in modulating the dimerization, stability, or transactivation functions of estrogen receptors.
8999954	8	32	theme	in	1179:1180	arg1	galactosylation					1188:1202	in vitro galactosylation	1179:1202	in vitro galactosylation	1179:1202	Based upon their relative resistance to both hexosaminidase and to in vitro galactosylation, O-GlcNAc moieties appear to be largely buried on native mER.
8999954	7	33	theme	PEST	1065:1068	arg1	region					1070:1075	a PEST region	1063:1075	a PEST region of the carboxyl-terminal F domain	1063:1109	Site mapping of insect cell expressed mER localized one major site of O-GlcNAc addition to Thr-575, within a PEST region of the carboxyl-terminal F domain.
8999954	9	34	theme	receptors	1426:1434	arg1	stability					1374:1382	stability	1374:1382	stability	1374:1382	This dynamic saccharide modification, like phosphorylation, may play a role in modulating the dimerization, stability, or transactivation functions of estrogen receptors.
8999954	9	34	theme	receptors	1426:1434	arg1	dimerization					1360:1371	dimerization	1360:1371	dimerization	1360:1371	This dynamic saccharide modification, like phosphorylation, may play a role in modulating the dimerization, stability, or transactivation functions of estrogen receptors.
8999954	9	34	theme	receptors	1426:1434	arg1	functions					1404:1412	transactivation functions	1388:1412	transactivation functions	1388:1412	This dynamic saccharide modification, like phosphorylation, may play a role in modulating the dimerization, stability, or transactivation functions of estrogen receptors.
8999954	7	35	theme	expressed	984:992	arg1	mER					994:996	insect cell expressed mER	972:996	insect cell expressed mER	972:996	Site mapping of insect cell expressed mER localized one major site of O-GlcNAc addition to Thr-575, within a PEST region of the carboxyl-terminal F domain.
8999954	5	36	theme	cancer	789:794	arg1	MCF-7					803:807	MCF-7	803:807	MCF-7	803:807	Wheat germ agglutinin-Sepharose affinity chromatography also readily detected terminal GlcNAc residues on subpopulations of ER purified from calf uterus, from human breast cancer cells (MCF-7), or from mER produced by in vitro translation.
8999954	5	36	theme	cancer	789:794	arg1	cells					796:800	human breast cancer cells	776:800	human breast cancer cells (MCF-7)	776:808	Wheat germ agglutinin-Sepharose affinity chromatography also readily detected terminal GlcNAc residues on subpopulations of ER purified from calf uterus, from human breast cancer cells (MCF-7), or from mER produced by in vitro translation.
8999954	3	37	mod	modified	438:445	arg1	subpopulations					371:384	subpopulations	371:384	subpopulations of murine, bovine, and human estrogen receptors	371:432	Here we report that subpopulations of murine, bovine, and human estrogen receptors are modified by O-GlcNAc.
8999954	3	37	mod	modified	438:445	arg3	O-GlcNAc					450:457	O-GlcNAc	450:457	O-GlcNAc	450:457	Here we report that subpopulations of murine, bovine, and human estrogen receptors are modified by O-GlcNAc.
8999954	7	38	theme	O-GlcNAc	1026:1033	arg1	addition					1035:1042	O-GlcNAc addition	1026:1042	O-GlcNAc addition	1026:1042	Site mapping of insect cell expressed mER localized one major site of O-GlcNAc addition to Thr-575, within a PEST region of the carboxyl-terminal F domain.
8999954	8	39	dep	in	1179:1180	arg1	vitro					1182:1186	vitro	1182:1186	vitro	1182:1186	Based upon their relative resistance to both hexosaminidase and to in vitro galactosylation, O-GlcNAc moieties appear to be largely buried on native mER.
8999954	9	40	theme	estrogen	1417:1424	arg1	receptors					1426:1434	estrogen receptors	1417:1434	estrogen receptors	1417:1434	This dynamic saccharide modification, like phosphorylation, may play a role in modulating the dimerization, stability, or transactivation functions of estrogen receptors.
8999954	0	41	theme	receptors	28:36	arg1	subpopulation					2:14	A subpopulation	0:14	A subpopulation of estrogen receptors	0:36	A subpopulation of estrogen receptors are modified by O-linked N-acetylglucosamine.
8999954	6	42	theme	estrogen	922:929	arg1	receptors					931:939	estrogen receptors	922:939	estrogen receptors	922:939	These data suggest that greater than 10% of these populations of estrogen receptors bear O-GlcNAc.
8999954	5	43	theme	ER	741:742	arg1	subpopulations					723:736	subpopulations	723:736	subpopulations of ER purified from calf uterus, from human breast cancer cells (MCF-7), or from mER produced by in vitro translation	723:854	Wheat germ agglutinin-Sepharose affinity chromatography also readily detected terminal GlcNAc residues on subpopulations of ER purified from calf uterus, from human breast cancer cells (MCF-7), or from mER produced by in vitro translation.
8999954	6	44	contain	bear	941:944	arg2	O-GlcNAc					946:953	O-GlcNAc	946:953	O-GlcNAc	946:953	These data suggest that greater than 10% of these populations of estrogen receptors bear O-GlcNAc.
8999954	6	44	contain	bear	941:944	arg1	%					896:896	greater than 10%	881:896	greater than 10% of these populations of estrogen receptors	881:939	These data suggest that greater than 10% of these populations of estrogen receptors bear O-GlcNAc.
8999954	6	44	contain	bear	941:944	arg1	populations					907:917	these populations	901:917	these populations of estrogen receptors	901:939	These data suggest that greater than 10% of these populations of estrogen receptors bear O-GlcNAc.
8999954	7	45	theme	mER	994:996	arg1	mapping					961:967	Site mapping	956:967	Site mapping of insect cell expressed mER	956:996	Site mapping of insect cell expressed mER localized one major site of O-GlcNAc addition to Thr-575, within a PEST region of the carboxyl-terminal F domain.
8999954	5	46	theme	in	835:836	arg1	translation					844:854	in vitro translation	835:854	in vitro translation	835:854	Wheat germ agglutinin-Sepharose affinity chromatography also readily detected terminal GlcNAc residues on subpopulations of ER purified from calf uterus, from human breast cancer cells (MCF-7), or from mER produced by in vitro translation.
8999954	7	47	theme	F	1102:1102	arg1	domain					1104:1109	the carboxyl-terminal F domain	1080:1109	the carboxyl-terminal F domain	1080:1109	Site mapping of insect cell expressed mER localized one major site of O-GlcNAc addition to Thr-575, within a PEST region of the carboxyl-terminal F domain.
8999954	4	48	theme	mouse	518:522	arg1	mER					528:530	mER	528:530	mER	528:530	O-GlcNAc moieties were detected on insect cell-expressed, mouse ER (mER) by probing with bovine milk galactosyltransferase, followed by structural analysis.
8999954	4	48	theme	mouse	518:522	arg1	cell-expressed					502:515	insect cell-expressed	495:515	insect cell-expressed	495:515	O-GlcNAc moieties were detected on insect cell-expressed, mouse ER (mER) by probing with bovine milk galactosyltransferase, followed by structural analysis.
8999954	4	48	theme	mouse	518:522	arg1	ER					524:525	mouse ER	518:525	mouse ER (mER)	518:531	O-GlcNAc moieties were detected on insect cell-expressed, mouse ER (mER) by probing with bovine milk galactosyltransferase, followed by structural analysis.
8999954	2	49	theme	RNA	234:236	arg1	polymerase					238:247	eukaryotic RNA polymerase II	223:250	eukaryotic RNA polymerase II	223:250	Many transcription factors and eukaryotic RNA polymerase II itself are also dynamically modified by Ser(Thr)-O-linked N-acetylglucosamine moieties (O-GlcNAc).
8999954	7	50	theme	addition	1035:1042	arg1	site					1018:1021	one major site	1008:1021	one major site of O-GlcNAc addition	1008:1042	Site mapping of insect cell expressed mER localized one major site of O-GlcNAc addition to Thr-575, within a PEST region of the carboxyl-terminal F domain.
8999954	7	50	theme	addition	1035:1042	arg1	addition					1035:1042	O-GlcNAc addition	1026:1042	O-GlcNAc addition	1026:1042	Site mapping of insect cell expressed mER localized one major site of O-GlcNAc addition to Thr-575, within a PEST region of the carboxyl-terminal F domain.
8999954	3	51	theme	bovine	397:402	arg1	receptors					424:432	murine, bovine, and human estrogen receptors	389:432	murine, bovine, and human estrogen receptors	389:432	Here we report that subpopulations of murine, bovine, and human estrogen receptors are modified by O-GlcNAc.
8999954	6	52	theme	populations	907:917	arg1	%					896:896	greater than 10%	881:896	greater than 10% of these populations of estrogen receptors	881:939	These data suggest that greater than 10% of these populations of estrogen receptors bear O-GlcNAc.
8999954	6	52	theme	populations	907:917	arg1	populations					907:917	these populations	901:917	these populations of estrogen receptors	901:939	These data suggest that greater than 10% of these populations of estrogen receptors bear O-GlcNAc.
8999954	5	53	theme	terminal	695:702	arg1	residues					711:718	terminal GlcNAc residues	695:718	terminal GlcNAc residues	695:718	Wheat germ agglutinin-Sepharose affinity chromatography also readily detected terminal GlcNAc residues on subpopulations of ER purified from calf uterus, from human breast cancer cells (MCF-7), or from mER produced by in vitro translation.
8999954	2	54	theme	eukaryotic	223:232	arg1	polymerase					238:247	eukaryotic RNA polymerase II	223:250	eukaryotic RNA polymerase II	223:250	Many transcription factors and eukaryotic RNA polymerase II itself are also dynamically modified by Ser(Thr)-O-linked N-acetylglucosamine moieties (O-GlcNAc).
8999954	7	55	theme	cell	979:982	arg1	mER					994:996	insect cell expressed mER	972:996	insect cell expressed mER	972:996	Site mapping of insect cell expressed mER localized one major site of O-GlcNAc addition to Thr-575, within a PEST region of the carboxyl-terminal F domain.
8999954	1	56	theme	ligand-inducible	112:127	arg1	factors					143:149	ligand-inducible transcription factors	112:149	ligand-inducible transcription factors regulated by Ser(Thr)-O-phosphorylation	112:189	Estrogen receptors (ER) are ligand-inducible transcription factors regulated by Ser(Thr)-O-phosphorylation.
8999954	1	56	theme	ligand-inducible	112:127	arg1	receptors					93:101	Estrogen receptors	84:101	Estrogen receptors (ER)	84:106	Estrogen receptors (ER) are ligand-inducible transcription factors regulated by Ser(Thr)-O-phosphorylation.
8999954	2	57	link	-O-linked	300:308	arg1	O-GlcNAc					340:347	O-GlcNAc	340:347	O-GlcNAc	340:347	Many transcription factors and eukaryotic RNA polymerase II itself are also dynamically modified by Ser(Thr)-O-linked N-acetylglucosamine moieties (O-GlcNAc).
8999954	2	57	link	-O-linked	300:308	arg1	moieties					330:337	Ser(Thr)-O-linked N-acetylglucosamine moieties	292:337	Ser(Thr)-O-linked N-acetylglucosamine moieties (O-GlcNAc)	292:348	Many transcription factors and eukaryotic RNA polymerase II itself are also dynamically modified by Ser(Thr)-O-linked N-acetylglucosamine moieties (O-GlcNAc).
8999954	5	58	theme	GlcNAc	704:709	arg1	residues					711:718	terminal GlcNAc residues	695:718	terminal GlcNAc residues	695:718	Wheat germ agglutinin-Sepharose affinity chromatography also readily detected terminal GlcNAc residues on subpopulations of ER purified from calf uterus, from human breast cancer cells (MCF-7), or from mER produced by in vitro translation.
8999954	0	59	link	O-linked	54:61	arg1	N-acetylglucosamine					63:81	O-linked N-acetylglucosamine	54:81	O-linked N-acetylglucosamine	54:81	A subpopulation of estrogen receptors are modified by O-linked N-acetylglucosamine.
8999954	1	60	theme	transcription	129:141	arg1	factors					143:149	ligand-inducible transcription factors	112:149	ligand-inducible transcription factors regulated by Ser(Thr)-O-phosphorylation	112:189	Estrogen receptors (ER) are ligand-inducible transcription factors regulated by Ser(Thr)-O-phosphorylation.
8999954	1	60	theme	transcription	129:141	arg1	receptors					93:101	Estrogen receptors	84:101	Estrogen receptors (ER)	84:106	Estrogen receptors (ER) are ligand-inducible transcription factors regulated by Ser(Thr)-O-phosphorylation.
8999954	7	61	theme	major	1012:1016	arg1	site					1018:1021	one major site	1008:1021	one major site of O-GlcNAc addition	1008:1042	Site mapping of insect cell expressed mER localized one major site of O-GlcNAc addition to Thr-575, within a PEST region of the carboxyl-terminal F domain.
8999954	7	61	theme	major	1012:1016	arg1	addition					1035:1042	O-GlcNAc addition	1026:1042	O-GlcNAc addition	1026:1042	Site mapping of insect cell expressed mER localized one major site of O-GlcNAc addition to Thr-575, within a PEST region of the carboxyl-terminal F domain.
8999954	2	62	theme	transcription	197:209	arg1	factors					211:217	Many transcription factors	192:217	Many transcription factors	192:217	Many transcription factors and eukaryotic RNA polymerase II itself are also dynamically modified by Ser(Thr)-O-linked N-acetylglucosamine moieties (O-GlcNAc).
8999954	5	63	dep	in	835:836	arg1	vitro					838:842	vitro	838:842	vitro	838:842	Wheat germ agglutinin-Sepharose affinity chromatography also readily detected terminal GlcNAc residues on subpopulations of ER purified from calf uterus, from human breast cancer cells (MCF-7), or from mER produced by in vitro translation.
8999954	2	64	theme	Many	192:195	arg1	factors					211:217	Many transcription factors	192:217	Many transcription factors	192:217	Many transcription factors and eukaryotic RNA polymerase II itself are also dynamically modified by Ser(Thr)-O-linked N-acetylglucosamine moieties (O-GlcNAc).
8999954	7	65	theme	insect	972:977	arg1	mER					994:996	insect cell expressed mER	972:996	insect cell expressed mER	972:996	Site mapping of insect cell expressed mER localized one major site of O-GlcNAc addition to Thr-575, within a PEST region of the carboxyl-terminal F domain.
8999954	9	66	dep	dimerization	1360:1371	arg1	the					1356:1358	the	1356:1358	the	1356:1358	This dynamic saccharide modification, like phosphorylation, may play a role in modulating the dimerization, stability, or transactivation functions of estrogen receptors.
8999954	0	67	theme	O-linked	54:61	arg1	N-acetylglucosamine					63:81	O-linked N-acetylglucosamine	54:81	O-linked N-acetylglucosamine	54:81	A subpopulation of estrogen receptors are modified by O-linked N-acetylglucosamine.
8999954	4	68	theme	insect	495:500	arg1	cell-expressed					502:515	insect cell-expressed	495:515	insect cell-expressed	495:515	O-GlcNAc moieties were detected on insect cell-expressed, mouse ER (mER) by probing with bovine milk galactosyltransferase, followed by structural analysis.
8999954	4	68	theme	insect	495:500	arg1	ER					524:525	mouse ER	518:525	mouse ER (mER)	518:531	O-GlcNAc moieties were detected on insect cell-expressed, mouse ER (mER) by probing with bovine milk galactosyltransferase, followed by structural analysis.
8999954	7	69	theme	Site	956:959	arg1	mapping					961:967	Site mapping	956:967	Site mapping of insect cell expressed mER	956:996	Site mapping of insect cell expressed mER localized one major site of O-GlcNAc addition to Thr-575, within a PEST region of the carboxyl-terminal F domain.
8999954	8	70	theme	O-GlcNAc	1205:1212	arg1	moieties					1214:1221	O-GlcNAc moieties	1205:1221	O-GlcNAc moieties	1205:1221	Based upon their relative resistance to both hexosaminidase and to in vitro galactosylation, O-GlcNAc moieties appear to be largely buried on native mER.
8999954	4	71	theme	structural	596:605	arg1	analysis					607:614	structural analysis	596:614	structural analysis	596:614	O-GlcNAc moieties were detected on insect cell-expressed, mouse ER (mER) by probing with bovine milk galactosyltransferase, followed by structural analysis.
2474541	8	0	theme	Bio-Gel	1254:1260	arg1	columns					1266:1272	Bio-Gel P-2 columns	1254:1272	Bio-Gel P-2 columns	1254:1272	On Bio-Gel P-2 columns, the beta-eliminated carbohydrate co-eluted with authentic N-acetylglucosaminitol.
2474541	9	1	theme	N-acetylglucosamine	1426:1444	arg1	N-acetylglucosamine					1426:1444	N-acetylglucosamine	1426:1444	N-acetylglucosamine O-glycosidically linked to the polypeptide chain	1426:1493	The results indicate that cytokeratin 13 contains single residues of N-acetylglucosamine O-glycosidically linked to the polypeptide chain.
2474541	9	1	theme	N-acetylglucosamine	1426:1444	arg1	residues					1414:1421	single residues	1407:1421	single residues of N-acetylglucosamine O-glycosidically linked to the polypeptide chain	1407:1493	The results indicate that cytokeratin 13 contains single residues of N-acetylglucosamine O-glycosidically linked to the polypeptide chain.
2474541	5	2	theme	ion-exchange	800:811	arg1	chromatography					813:826	ion-exchange chromatography	800:826	ion-exchange chromatography	800:826	Acid hydrolysis followed by paper and ion-exchange chromatography showed that the radioactivity in electrophoretically purified cytokeratin 13 was still present as glucosamine.
2474541	7	3	theme	O-glycosidic	1229:1240	arg1	linkage					1242:1248	an O-glycosidic linkage	1226:1248	an O-glycosidic linkage	1226:1248	The labeled carbohydrate was released by alkaline borohydride treatment and was bound by a phenylboronic acid column, indicating an O-glycosidic linkage.
2474541	1	4	theme	metabolic	185:193	arg1	labeling					195:202	metabolic labeling	185:202	metabolic labeling with [3H]glucosamine	185:223	The glycosylation of human cytokeratins was investigated in cultured human keratinocytes and A431 cells by metabolic labeling with [3H]glucosamine.
2474541	9	5	contain	contains	1398:1405	arg2	residues					1414:1421	single residues	1407:1421	single residues of N-acetylglucosamine O-glycosidically linked to the polypeptide chain	1407:1493	The results indicate that cytokeratin 13 contains single residues of N-acetylglucosamine O-glycosidically linked to the polypeptide chain.
2474541	9	5	contain	contains	1398:1405	arg1	cytokeratin					1383:1393	cytokeratin 13	1383:1396	cytokeratin 13	1383:1396	The results indicate that cytokeratin 13 contains single residues of N-acetylglucosamine O-glycosidically linked to the polypeptide chain.
2474541	9	5	contain	contains	1398:1405	arg2	N-acetylglucosamine					1426:1444	N-acetylglucosamine	1426:1444	N-acetylglucosamine O-glycosidically linked to the polypeptide chain	1426:1493	The results indicate that cytokeratin 13 contains single residues of N-acetylglucosamine O-glycosidically linked to the polypeptide chain.
2474541	2	6	theme	vitamin	308:314	arg1	cytokeratin					396:406	cytokeratin 13	396:409	cytokeratin 13	396:409	In the presence of tunicamycin, keratinocytes incorporated [3H]glucosamine into a vitamin A-regulated acidic 53-kDa component of the cytoskeleton which was identified as cytokeratin 13 by one- and two-dimensional immunoblotting with specific monoclonal antibodies.
2474541	2	6	theme	vitamin	308:314	arg1	component					342:350	a vitamin A-regulated acidic 53-kDa component	306:350	a vitamin A-regulated acidic 53-kDa component of the cytoskeleton which was identified as cytokeratin 13 by one- and two-dimensional immunoblotting with specific monoclonal antibodies	306:488	In the presence of tunicamycin, keratinocytes incorporated [3H]glucosamine into a vitamin A-regulated acidic 53-kDa component of the cytoskeleton which was identified as cytokeratin 13 by one- and two-dimensional immunoblotting with specific monoclonal antibodies.
2474541	5	7	theme	Acid	762:765	arg1	hydrolysis					767:776	Acid hydrolysis	762:776	Acid hydrolysis followed by paper and ion-exchange chromatography	762:826	Acid hydrolysis followed by paper and ion-exchange chromatography showed that the radioactivity in electrophoretically purified cytokeratin 13 was still present as glucosamine.
2474541	2	8	with	immunoblotting	439:452	arg1	antibodies					479:488	specific monoclonal antibodies	459:488	specific monoclonal antibodies	459:488	In the presence of tunicamycin, keratinocytes incorporated [3H]glucosamine into a vitamin A-regulated acidic 53-kDa component of the cytoskeleton which was identified as cytokeratin 13 by one- and two-dimensional immunoblotting with specific monoclonal antibodies.
2474541	4	9	link	N-linked	735:742	arg1	oligosaccharides					744:759	N-linked oligosaccharides	735:759	N-linked oligosaccharides	735:759	Its labeling was resistant to tunicamycin, suggesting that [3H]glucosamine had not been incorporated into N-linked oligosaccharides.
2474541	3	10	theme	KB	582:583	arg1	cells					585:589	KB cells	582:589	KB cells	582:589	This cytoskeletal component was also labeled with [3H]glucosamine in A431 cells but not in KB cells, which do not express cytokeratin 13.
2474541	6	11	theme	N-acetylglucosamine	1067:1085	arg1	residues					1087:1094	terminal N-acetylglucosamine residues	1058:1094	terminal N-acetylglucosamine residues	1058:1094	Radioactivity was completely removed by treatment with beta-N-acetylglucosaminidase, suggesting that it was present in terminal N-acetylglucosamine residues.
2474541	6	12	with	treatment	979:987	arg1	beta-N-acetylglucosaminidase					994:1021	beta-N-acetylglucosaminidase	994:1021	beta-N-acetylglucosaminidase	994:1021	Radioactivity was completely removed by treatment with beta-N-acetylglucosaminidase, suggesting that it was present in terminal N-acetylglucosamine residues.
2474541	6	13	from	residues	1087:1094	arg1	present					1047:1053	present	1047:1053	present	1047:1053	Radioactivity was completely removed by treatment with beta-N-acetylglucosaminidase, suggesting that it was present in terminal N-acetylglucosamine residues.
2474541	7	14	theme	acid	1202:1205	arg1	column					1207:1212	a phenylboronic acid column	1186:1212	a phenylboronic acid column	1186:1212	The labeled carbohydrate was released by alkaline borohydride treatment and was bound by a phenylboronic acid column, indicating an O-glycosidic linkage.
2474541	5	15	from	radioactivity	844:856	arg1	cytokeratin					890:900	electrophoretically purified cytokeratin 13	861:903	electrophoretically purified cytokeratin 13	861:903	Acid hydrolysis followed by paper and ion-exchange chromatography showed that the radioactivity in electrophoretically purified cytokeratin 13 was still present as glucosamine.
2474541	0	16	contain	contains	15:22	arg1	Cytokeratin					0:10	Cytokeratin 13	0:13	Cytokeratin 13	0:13	Cytokeratin 13 contains O-glycosidically linked N-acetylglucosamine residues.
2474541	0	16	contain	contains	15:22	arg2	residues					68:75	O-glycosidically linked N-acetylglucosamine residues	24:75	O-glycosidically linked N-acetylglucosamine residues	24:75	Cytokeratin 13 contains O-glycosidically linked N-acetylglucosamine residues.
2474541	1	17	theme	human	99:103	arg1	cytokeratins					105:116	human cytokeratins	99:116	human cytokeratins	99:116	The glycosylation of human cytokeratins was investigated in cultured human keratinocytes and A431 cells by metabolic labeling with [3H]glucosamine.
2474541	9	18	attach	linked	1463:1468	arg2	N-acetylglucosamine					1426:1444	N-acetylglucosamine	1426:1444	N-acetylglucosamine O-glycosidically linked to the polypeptide chain	1426:1493	The results indicate that cytokeratin 13 contains single residues of N-acetylglucosamine O-glycosidically linked to the polypeptide chain.
2474541	9	18	attach	linked	1463:1468	arg1	chain					1489:1493	the polypeptide chain	1473:1493	the polypeptide chain	1473:1493	The results indicate that cytokeratin 13 contains single residues of N-acetylglucosamine O-glycosidically linked to the polypeptide chain.
2474541	2	19	theme	one-	414:417	arg1	immunoblotting					439:452	one- and two-dimensional immunoblotting	414:452	one- and two-dimensional immunoblotting with specific monoclonal antibodies	414:488	In the presence of tunicamycin, keratinocytes incorporated [3H]glucosamine into a vitamin A-regulated acidic 53-kDa component of the cytoskeleton which was identified as cytokeratin 13 by one- and two-dimensional immunoblotting with specific monoclonal antibodies.
2474541	1	20	theme	cytokeratins	105:116	arg1	glycosylation					82:94	The glycosylation	78:94	The glycosylation of human cytokeratins	78:116	The glycosylation of human cytokeratins was investigated in cultured human keratinocytes and A431 cells by metabolic labeling with [3H]glucosamine.
2474541	6	21	located	present	1047:1053	arg2	it					1040:1041	it	1040:1041	it	1040:1041	Radioactivity was completely removed by treatment with beta-N-acetylglucosaminidase, suggesting that it was present in terminal N-acetylglucosamine residues.
2474541	6	21	located	present	1047:1053	arg1	residues					1087:1094	terminal N-acetylglucosamine residues	1058:1094	terminal N-acetylglucosamine residues	1058:1094	Radioactivity was completely removed by treatment with beta-N-acetylglucosaminidase, suggesting that it was present in terminal N-acetylglucosamine residues.
2474541	8	22	theme	beta-eliminated	1279:1293	arg1	carbohydrate					1295:1306	the beta-eliminated carbohydrate	1275:1306	the beta-eliminated carbohydrate	1275:1306	On Bio-Gel P-2 columns, the beta-eliminated carbohydrate co-eluted with authentic N-acetylglucosaminitol.
2474541	6	23	theme	terminal	1058:1065	arg1	residues					1087:1094	terminal N-acetylglucosamine residues	1058:1094	terminal N-acetylglucosamine residues	1058:1094	Radioactivity was completely removed by treatment with beta-N-acetylglucosaminidase, suggesting that it was present in terminal N-acetylglucosamine residues.
2474541	7	24	theme	phenylboronic	1188:1200	arg1	column					1207:1212	a phenylboronic acid column	1186:1212	a phenylboronic acid column	1186:1212	The labeled carbohydrate was released by alkaline borohydride treatment and was bound by a phenylboronic acid column, indicating an O-glycosidic linkage.
2474541	2	25	theme	53-kDa	335:340	arg1	cytokeratin					396:406	cytokeratin 13	396:409	cytokeratin 13	396:409	In the presence of tunicamycin, keratinocytes incorporated [3H]glucosamine into a vitamin A-regulated acidic 53-kDa component of the cytoskeleton which was identified as cytokeratin 13 by one- and two-dimensional immunoblotting with specific monoclonal antibodies.
2474541	2	25	theme	53-kDa	335:340	arg1	component					342:350	a vitamin A-regulated acidic 53-kDa component	306:350	a vitamin A-regulated acidic 53-kDa component of the cytoskeleton which was identified as cytokeratin 13 by one- and two-dimensional immunoblotting with specific monoclonal antibodies	306:488	In the presence of tunicamycin, keratinocytes incorporated [3H]glucosamine into a vitamin A-regulated acidic 53-kDa component of the cytoskeleton which was identified as cytokeratin 13 by one- and two-dimensional immunoblotting with specific monoclonal antibodies.
2474541	6	26	from	present	1047:1053	arg1	residues					1087:1094	terminal N-acetylglucosamine residues	1058:1094	terminal N-acetylglucosamine residues	1058:1094	Radioactivity was completely removed by treatment with beta-N-acetylglucosaminidase, suggesting that it was present in terminal N-acetylglucosamine residues.
2474541	0	27	link	linked	41:46	arg1	residues					68:75	O-glycosidically linked N-acetylglucosamine residues	24:75	O-glycosidically linked N-acetylglucosamine residues	24:75	Cytokeratin 13 contains O-glycosidically linked N-acetylglucosamine residues.
2474541	2	28	theme	acidic	328:333	arg1	cytokeratin					396:406	cytokeratin 13	396:409	cytokeratin 13	396:409	In the presence of tunicamycin, keratinocytes incorporated [3H]glucosamine into a vitamin A-regulated acidic 53-kDa component of the cytoskeleton which was identified as cytokeratin 13 by one- and two-dimensional immunoblotting with specific monoclonal antibodies.
2474541	2	28	theme	acidic	328:333	arg1	component					342:350	a vitamin A-regulated acidic 53-kDa component	306:350	a vitamin A-regulated acidic 53-kDa component of the cytoskeleton which was identified as cytokeratin 13 by one- and two-dimensional immunoblotting with specific monoclonal antibodies	306:488	In the presence of tunicamycin, keratinocytes incorporated [3H]glucosamine into a vitamin A-regulated acidic 53-kDa component of the cytoskeleton which was identified as cytokeratin 13 by one- and two-dimensional immunoblotting with specific monoclonal antibodies.
2474541	2	29	theme	specific	459:466	arg1	antibodies					479:488	specific monoclonal antibodies	459:488	specific monoclonal antibodies	459:488	In the presence of tunicamycin, keratinocytes incorporated [3H]glucosamine into a vitamin A-regulated acidic 53-kDa component of the cytoskeleton which was identified as cytokeratin 13 by one- and two-dimensional immunoblotting with specific monoclonal antibodies.
2474541	2	30	theme	monoclonal	468:477	arg1	antibodies					479:488	specific monoclonal antibodies	459:488	specific monoclonal antibodies	459:488	In the presence of tunicamycin, keratinocytes incorporated [3H]glucosamine into a vitamin A-regulated acidic 53-kDa component of the cytoskeleton which was identified as cytokeratin 13 by one- and two-dimensional immunoblotting with specific monoclonal antibodies.
2474541	2	31	theme	A-regulated	316:326	arg1	cytokeratin					396:406	cytokeratin 13	396:409	cytokeratin 13	396:409	In the presence of tunicamycin, keratinocytes incorporated [3H]glucosamine into a vitamin A-regulated acidic 53-kDa component of the cytoskeleton which was identified as cytokeratin 13 by one- and two-dimensional immunoblotting with specific monoclonal antibodies.
2474541	2	31	theme	A-regulated	316:326	arg1	component					342:350	a vitamin A-regulated acidic 53-kDa component	306:350	a vitamin A-regulated acidic 53-kDa component of the cytoskeleton which was identified as cytokeratin 13 by one- and two-dimensional immunoblotting with specific monoclonal antibodies	306:488	In the presence of tunicamycin, keratinocytes incorporated [3H]glucosamine into a vitamin A-regulated acidic 53-kDa component of the cytoskeleton which was identified as cytokeratin 13 by one- and two-dimensional immunoblotting with specific monoclonal antibodies.
2474541	3	32	theme	A431	560:563	arg1	cells					565:569	A431 cells	560:569	A431 cells	560:569	This cytoskeletal component was also labeled with [3H]glucosamine in A431 cells but not in KB cells, which do not express cytokeratin 13.
2474541	0	33	theme	N-acetylglucosamine	48:66	arg1	residues					68:75	O-glycosidically linked N-acetylglucosamine residues	24:75	O-glycosidically linked N-acetylglucosamine residues	24:75	Cytokeratin 13 contains O-glycosidically linked N-acetylglucosamine residues.
2474541	2	34	theme	cytoskeleton	359:370	arg1	cytokeratin					396:406	cytokeratin 13	396:409	cytokeratin 13	396:409	In the presence of tunicamycin, keratinocytes incorporated [3H]glucosamine into a vitamin A-regulated acidic 53-kDa component of the cytoskeleton which was identified as cytokeratin 13 by one- and two-dimensional immunoblotting with specific monoclonal antibodies.
2474541	2	34	theme	cytoskeleton	359:370	arg1	component					342:350	a vitamin A-regulated acidic 53-kDa component	306:350	a vitamin A-regulated acidic 53-kDa component of the cytoskeleton which was identified as cytokeratin 13 by one- and two-dimensional immunoblotting with specific monoclonal antibodies	306:488	In the presence of tunicamycin, keratinocytes incorporated [3H]glucosamine into a vitamin A-regulated acidic 53-kDa component of the cytoskeleton which was identified as cytokeratin 13 by one- and two-dimensional immunoblotting with specific monoclonal antibodies.
2474541	3	35	theme	cytoskeletal	496:507	arg1	component					509:517	This cytoskeletal component	491:517	This cytoskeletal component	491:517	This cytoskeletal component was also labeled with [3H]glucosamine in A431 cells but not in KB cells, which do not express cytokeratin 13.
2474541	0	36	theme	linked	41:46	arg1	residues					68:75	O-glycosidically linked N-acetylglucosamine residues	24:75	O-glycosidically linked N-acetylglucosamine residues	24:75	Cytokeratin 13 contains O-glycosidically linked N-acetylglucosamine residues.
2474541	8	37	theme	authentic	1323:1331	arg1	N-acetylglucosaminitol					1333:1354	authentic N-acetylglucosaminitol	1323:1354	authentic N-acetylglucosaminitol	1323:1354	On Bio-Gel P-2 columns, the beta-eliminated carbohydrate co-eluted with authentic N-acetylglucosaminitol.
2474541	2	38	theme	two-dimensional	423:437	arg1	immunoblotting					439:452	one- and two-dimensional immunoblotting	414:452	one- and two-dimensional immunoblotting with specific monoclonal antibodies	414:488	In the presence of tunicamycin, keratinocytes incorporated [3H]glucosamine into a vitamin A-regulated acidic 53-kDa component of the cytoskeleton which was identified as cytokeratin 13 by one- and two-dimensional immunoblotting with specific monoclonal antibodies.
2474541	7	39	theme	borohydride	1147:1157	arg1	treatment					1159:1167	alkaline borohydride treatment	1138:1167	alkaline borohydride treatment	1138:1167	The labeled carbohydrate was released by alkaline borohydride treatment and was bound by a phenylboronic acid column, indicating an O-glycosidic linkage.
2474541	9	40	theme	polypeptide	1477:1487	arg1	chain					1489:1493	the polypeptide chain	1473:1493	the polypeptide chain	1473:1493	The results indicate that cytokeratin 13 contains single residues of N-acetylglucosamine O-glycosidically linked to the polypeptide chain.
2474541	1	41	theme	cultured	138:145	arg1	keratinocytes					153:165	cultured human keratinocytes	138:165	cultured human keratinocytes	138:165	The glycosylation of human cytokeratins was investigated in cultured human keratinocytes and A431 cells by metabolic labeling with [3H]glucosamine.
2474541	7	42	theme	labeled	1101:1107	arg1	carbohydrate					1109:1120	The labeled carbohydrate	1097:1120	The labeled carbohydrate	1097:1120	The labeled carbohydrate was released by alkaline borohydride treatment and was bound by a phenylboronic acid column, indicating an O-glycosidic linkage.
2474541	1	43	theme	human	147:151	arg1	keratinocytes					153:165	cultured human keratinocytes	138:165	cultured human keratinocytes	138:165	The glycosylation of human cytokeratins was investigated in cultured human keratinocytes and A431 cells by metabolic labeling with [3H]glucosamine.
2474541	6	44	attach	present	1047:1053	arg2	it					1040:1041	it	1040:1041	it	1040:1041	Radioactivity was completely removed by treatment with beta-N-acetylglucosaminidase, suggesting that it was present in terminal N-acetylglucosamine residues.
2474541	6	44	attach	present	1047:1053	arg1	residues					1087:1094	terminal N-acetylglucosamine residues	1058:1094	terminal N-acetylglucosamine residues	1058:1094	Radioactivity was completely removed by treatment with beta-N-acetylglucosaminidase, suggesting that it was present in terminal N-acetylglucosamine residues.
2474541	1	45	with	labeling	195:202	arg1	glucosamine					213:223	[3H]glucosamine	209:223	[3H]glucosamine	209:223	The glycosylation of human cytokeratins was investigated in cultured human keratinocytes and A431 cells by metabolic labeling with [3H]glucosamine.
2474541	7	46	theme	alkaline	1138:1145	arg1	treatment					1159:1167	alkaline borohydride treatment	1138:1167	alkaline borohydride treatment	1138:1167	The labeled carbohydrate was released by alkaline borohydride treatment and was bound by a phenylboronic acid column, indicating an O-glycosidic linkage.
2474541	9	47	theme	single	1407:1412	arg1	N-acetylglucosamine					1426:1444	N-acetylglucosamine	1426:1444	N-acetylglucosamine O-glycosidically linked to the polypeptide chain	1426:1493	The results indicate that cytokeratin 13 contains single residues of N-acetylglucosamine O-glycosidically linked to the polypeptide chain.
2474541	9	47	theme	single	1407:1412	arg1	residues					1414:1421	single residues	1407:1421	single residues of N-acetylglucosamine O-glycosidically linked to the polypeptide chain	1407:1493	The results indicate that cytokeratin 13 contains single residues of N-acetylglucosamine O-glycosidically linked to the polypeptide chain.
2474541	4	48	theme	N-linked	735:742	arg1	oligosaccharides					744:759	N-linked oligosaccharides	735:759	N-linked oligosaccharides	735:759	Its labeling was resistant to tunicamycin, suggesting that [3H]glucosamine had not been incorporated into N-linked oligosaccharides.
2474541	1	49	gly	glycosylation	82:94	arg1	keratinocytes					153:165	cultured human keratinocytes	138:165	cultured human keratinocytes	138:165	The glycosylation of human cytokeratins was investigated in cultured human keratinocytes and A431 cells by metabolic labeling with [3H]glucosamine.
2474541	1	49	gly	glycosylation	82:94	arg1	cells					176:180	A431 cells	171:180	A431 cells	171:180	The glycosylation of human cytokeratins was investigated in cultured human keratinocytes and A431 cells by metabolic labeling with [3H]glucosamine.
2474541	1	49	gly	glycosylation	82:94	arg1	cytokeratins					105:116	human cytokeratins	99:116	human cytokeratins	99:116	The glycosylation of human cytokeratins was investigated in cultured human keratinocytes and A431 cells by metabolic labeling with [3H]glucosamine.
2474541	2	50	dep	tunicamycin	245:255	arg1	presence					233:240	presence	233:240	presence	233:240	In the presence of tunicamycin, keratinocytes incorporated [3H]glucosamine into a vitamin A-regulated acidic 53-kDa component of the cytoskeleton which was identified as cytokeratin 13 by one- and two-dimensional immunoblotting with specific monoclonal antibodies.
2474541	2	50	dep	tunicamycin	245:255	arg1	the					229:231	the	229:231	the	229:231	In the presence of tunicamycin, keratinocytes incorporated [3H]glucosamine into a vitamin A-regulated acidic 53-kDa component of the cytoskeleton which was identified as cytokeratin 13 by one- and two-dimensional immunoblotting with specific monoclonal antibodies.
2474541	1	51	theme	A431	171:174	arg1	cells					176:180	A431 cells	171:180	A431 cells	171:180	The glycosylation of human cytokeratins was investigated in cultured human keratinocytes and A431 cells by metabolic labeling with [3H]glucosamine.
2474541	5	52	theme	purified	881:888	arg1	cytokeratin					890:900	electrophoretically purified cytokeratin 13	861:903	electrophoretically purified cytokeratin 13	861:903	Acid hydrolysis followed by paper and ion-exchange chromatography showed that the radioactivity in electrophoretically purified cytokeratin 13 was still present as glucosamine.
2474541	8	53	theme	P-2	1262:1264	arg1	columns					1266:1272	Bio-Gel P-2 columns	1254:1272	Bio-Gel P-2 columns	1254:1272	On Bio-Gel P-2 columns, the beta-eliminated carbohydrate co-eluted with authentic N-acetylglucosaminitol.
1647397	2	0	theme	Indirect	606:613	arg1	immunofluorescence					615:632	Indirect immunofluorescence	606:632	Indirect immunofluorescence	606:632	The enzyme, purified 3400-fold from mitotic cell extracts by (NH4)2SO4 precipitation, DEAE chromatography, and immunoaffinity chromatography on immobilized anti-p65 IgG, was inhibited by Zn2- and Na3VO4 but not NaF or beta-glycerophosphate; 32P-labeled poly(Glu, Tyr) was more efficiently dephosphorylated than phosphorylated histone or phosphorylase a. Indirect immunofluorescence showed most of the phosphatase to be localized in the nucleus of interphase cells, with a fine, granular distribution unaltered by detergent extraction; in mitotic cells, p65 was localized on chromosomes.
1647397	1	1	theme	human	164:168	arg1	factor					188:193	human M phase-promoting factor	164:193	human M phase-promoting factor	164:193	Histochemical staining of immunoprecipitates of p65, a component of human M phase-promoting factor, identified the molecule as having phosphatase activity.
1647397	5	2	theme	proteins	1211:1218	arg1	proteins					1211:1218	other nuclear proteins	1197:1218	other nuclear proteins	1197:1218	Alkaline hydrolysis of blotted protein prevented WGA binding, indicating that phosphatase p65, like a small group of other nuclear proteins, contains O-linked carbohydrate terminating in N-acetylglucosamine.
1647397	5	2	theme	proteins	1211:1218	arg1	group					1188:1192	a small group	1180:1192	a small group of other nuclear proteins	1180:1218	Alkaline hydrolysis of blotted protein prevented WGA binding, indicating that phosphatase p65, like a small group of other nuclear proteins, contains O-linked carbohydrate terminating in N-acetylglucosamine.
1647397	2	3	theme	anti-p65	408:415	arg1	IgG					417:419	immobilized anti-p65 IgG	396:419	immobilized anti-p65 IgG	396:419	The enzyme, purified 3400-fold from mitotic cell extracts by (NH4)2SO4 precipitation, DEAE chromatography, and immunoaffinity chromatography on immobilized anti-p65 IgG, was inhibited by Zn2- and Na3VO4 but not NaF or beta-glycerophosphate; 32P-labeled poly(Glu, Tyr) was more efficiently dephosphorylated than phosphorylated histone or phosphorylase a. Indirect immunofluorescence showed most of the phosphatase to be localized in the nucleus of interphase cells, with a fine, granular distribution unaltered by detergent extraction; in mitotic cells, p65 was localized on chromosomes.
1647397	0	4	from	localization	8:19	arg1	cells					89:93	human cells	83:93	human cells	83:93	Nuclear localization of an O-glycosylated protein phosphotyrosine phosphatase from human cells.
1647397	1	5	theme	M	170:170	arg1	factor					188:193	human M phase-promoting factor	164:193	human M phase-promoting factor	164:193	Histochemical staining of immunoprecipitates of p65, a component of human M phase-promoting factor, identified the molecule as having phosphatase activity.
1647397	3	6	theme	fractions	860:868	arg1	ELISA					839:843	ELISA	839:843	ELISA of subcellular fractions	839:868	ELISA of subcellular fractions confirmed this localization.
1647397	5	7	link	O-linked	1230:1237	arg1	carbohydrate					1239:1250	O-linked carbohydrate	1230:1250	O-linked carbohydrate terminating in N-acetylglucosamine	1230:1285	Alkaline hydrolysis of blotted protein prevented WGA binding, indicating that phosphatase p65, like a small group of other nuclear proteins, contains O-linked carbohydrate terminating in N-acetylglucosamine.
1647397	4	8	theme	germ	955:958	arg1	WGA					972:974	WGA	972:974	WGA	972:974	Immunoreactive p65 was recovered from immobilized wheat germ agglutinin (WGA) upon elution with N-acetylglucosamine; similarly, WGA recognized immunoaffinity-purified p65 on blots.
1647397	4	8	theme	germ	955:958	arg1	agglutinin					960:969	immobilized wheat germ agglutinin	937:969	immobilized wheat germ agglutinin (WGA)	937:975	Immunoreactive p65 was recovered from immobilized wheat germ agglutinin (WGA) upon elution with N-acetylglucosamine; similarly, WGA recognized immunoaffinity-purified p65 on blots.
1647397	2	9	located	localized	813:821	arg2	p65					805:807	p65	805:807	p65	805:807	The enzyme, purified 3400-fold from mitotic cell extracts by (NH4)2SO4 precipitation, DEAE chromatography, and immunoaffinity chromatography on immobilized anti-p65 IgG, was inhibited by Zn2- and Na3VO4 but not NaF or beta-glycerophosphate; 32P-labeled poly(Glu, Tyr) was more efficiently dephosphorylated than phosphorylated histone or phosphorylase a. Indirect immunofluorescence showed most of the phosphatase to be localized in the nucleus of interphase cells, with a fine, granular distribution unaltered by detergent extraction; in mitotic cells, p65 was localized on chromosomes.
1647397	2	9	located	localized	813:821	arg1	cells					798:802	mitotic cells	790:802	mitotic cells	790:802	The enzyme, purified 3400-fold from mitotic cell extracts by (NH4)2SO4 precipitation, DEAE chromatography, and immunoaffinity chromatography on immobilized anti-p65 IgG, was inhibited by Zn2- and Na3VO4 but not NaF or beta-glycerophosphate; 32P-labeled poly(Glu, Tyr) was more efficiently dephosphorylated than phosphorylated histone or phosphorylase a. Indirect immunofluorescence showed most of the phosphatase to be localized in the nucleus of interphase cells, with a fine, granular distribution unaltered by detergent extraction; in mitotic cells, p65 was localized on chromosomes.
1647397	2	9	located	localized	813:821	arg1	chromosomes					826:836	chromosomes	826:836	chromosomes	826:836	The enzyme, purified 3400-fold from mitotic cell extracts by (NH4)2SO4 precipitation, DEAE chromatography, and immunoaffinity chromatography on immobilized anti-p65 IgG, was inhibited by Zn2- and Na3VO4 but not NaF or beta-glycerophosphate; 32P-labeled poly(Glu, Tyr) was more efficiently dephosphorylated than phosphorylated histone or phosphorylase a. Indirect immunofluorescence showed most of the phosphatase to be localized in the nucleus of interphase cells, with a fine, granular distribution unaltered by detergent extraction; in mitotic cells, p65 was localized on chromosomes.
1647397	2	10	theme	cell	296:299	arg1	extracts					301:308	mitotic cell extracts	288:308	mitotic cell extracts	288:308	The enzyme, purified 3400-fold from mitotic cell extracts by (NH4)2SO4 precipitation, DEAE chromatography, and immunoaffinity chromatography on immobilized anti-p65 IgG, was inhibited by Zn2- and Na3VO4 but not NaF or beta-glycerophosphate; 32P-labeled poly(Glu, Tyr) was more efficiently dephosphorylated than phosphorylated histone or phosphorylase a. Indirect immunofluorescence showed most of the phosphatase to be localized in the nucleus of interphase cells, with a fine, granular distribution unaltered by detergent extraction; in mitotic cells, p65 was localized on chromosomes.
1647397	5	11	theme	O-linked	1230:1237	arg1	carbohydrate					1239:1250	O-linked carbohydrate	1230:1250	O-linked carbohydrate terminating in N-acetylglucosamine	1230:1285	Alkaline hydrolysis of blotted protein prevented WGA binding, indicating that phosphatase p65, like a small group of other nuclear proteins, contains O-linked carbohydrate terminating in N-acetylglucosamine.
1647397	5	12	theme	WGA	1129:1131	arg1	binding					1133:1139	WGA binding	1129:1139	WGA binding	1129:1139	Alkaline hydrolysis of blotted protein prevented WGA binding, indicating that phosphatase p65, like a small group of other nuclear proteins, contains O-linked carbohydrate terminating in N-acetylglucosamine.
1647397	2	13	theme	mitotic	288:294	arg1	extracts					301:308	mitotic cell extracts	288:308	mitotic cell extracts	288:308	The enzyme, purified 3400-fold from mitotic cell extracts by (NH4)2SO4 precipitation, DEAE chromatography, and immunoaffinity chromatography on immobilized anti-p65 IgG, was inhibited by Zn2- and Na3VO4 but not NaF or beta-glycerophosphate; 32P-labeled poly(Glu, Tyr) was more efficiently dephosphorylated than phosphorylated histone or phosphorylase a. Indirect immunofluorescence showed most of the phosphatase to be localized in the nucleus of interphase cells, with a fine, granular distribution unaltered by detergent extraction; in mitotic cells, p65 was localized on chromosomes.
1647397	2	14	theme	unaltered	752:760	arg1	distribution					739:750	a fine, granular distribution	722:750	a fine, granular distribution unaltered by detergent extraction	722:784	The enzyme, purified 3400-fold from mitotic cell extracts by (NH4)2SO4 precipitation, DEAE chromatography, and immunoaffinity chromatography on immobilized anti-p65 IgG, was inhibited by Zn2- and Na3VO4 but not NaF or beta-glycerophosphate; 32P-labeled poly(Glu, Tyr) was more efficiently dephosphorylated than phosphorylated histone or phosphorylase a. Indirect immunofluorescence showed most of the phosphatase to be localized in the nucleus of interphase cells, with a fine, granular distribution unaltered by detergent extraction; in mitotic cells, p65 was localized on chromosomes.
1647397	1	15	theme	phase-promoting	172:186	arg1	factor					188:193	human M phase-promoting factor	164:193	human M phase-promoting factor	164:193	Histochemical staining of immunoprecipitates of p65, a component of human M phase-promoting factor, identified the molecule as having phosphatase activity.
1647397	5	16	contain	contains	1221:1228	arg2	carbohydrate					1239:1250	O-linked carbohydrate	1230:1250	O-linked carbohydrate terminating in N-acetylglucosamine	1230:1285	Alkaline hydrolysis of blotted protein prevented WGA binding, indicating that phosphatase p65, like a small group of other nuclear proteins, contains O-linked carbohydrate terminating in N-acetylglucosamine.
1647397	5	16	contain	contains	1221:1228	arg1	p65					1170:1172	phosphatase p65	1158:1172	phosphatase p65	1158:1172	Alkaline hydrolysis of blotted protein prevented WGA binding, indicating that phosphatase p65, like a small group of other nuclear proteins, contains O-linked carbohydrate terminating in N-acetylglucosamine.
1647397	2	17	dep	immunofluorescence	615:632	arg1	a.					603:604	a.	603:604	a.	603:604	The enzyme, purified 3400-fold from mitotic cell extracts by (NH4)2SO4 precipitation, DEAE chromatography, and immunoaffinity chromatography on immobilized anti-p65 IgG, was inhibited by Zn2- and Na3VO4 but not NaF or beta-glycerophosphate; 32P-labeled poly(Glu, Tyr) was more efficiently dephosphorylated than phosphorylated histone or phosphorylase a. Indirect immunofluorescence showed most of the phosphatase to be localized in the nucleus of interphase cells, with a fine, granular distribution unaltered by detergent extraction; in mitotic cells, p65 was localized on chromosomes.
1647397	1	18	theme	factor	188:193	arg1	p65					144:146	p65	144:146	p65	144:146	Histochemical staining of immunoprecipitates of p65, a component of human M phase-promoting factor, identified the molecule as having phosphatase activity.
1647397	1	18	theme	factor	188:193	arg1	component					151:159	a component	149:159	a component of human M phase-promoting factor	149:193	Histochemical staining of immunoprecipitates of p65, a component of human M phase-promoting factor, identified the molecule as having phosphatase activity.
1647397	1	19	theme	Histochemical	96:108	arg1	staining					110:117	Histochemical staining	96:117	Histochemical staining of immunoprecipitates of p65, a component of human M phase-promoting factor,	96:194	Histochemical staining of immunoprecipitates of p65, a component of human M phase-promoting factor, identified the molecule as having phosphatase activity.
1647397	2	20	dep	fine	724:727	arg1	granular					730:737	granular	730:737	granular	730:737	The enzyme, purified 3400-fold from mitotic cell extracts by (NH4)2SO4 precipitation, DEAE chromatography, and immunoaffinity chromatography on immobilized anti-p65 IgG, was inhibited by Zn2- and Na3VO4 but not NaF or beta-glycerophosphate; 32P-labeled poly(Glu, Tyr) was more efficiently dephosphorylated than phosphorylated histone or phosphorylase a. Indirect immunofluorescence showed most of the phosphatase to be localized in the nucleus of interphase cells, with a fine, granular distribution unaltered by detergent extraction; in mitotic cells, p65 was localized on chromosomes.
1647397	0	21	theme	Nuclear	0:6	arg1	localization					8:19	Nuclear localization	0:19	Nuclear localization of an O-glycosylated protein phosphotyrosine phosphatase from human cells	0:93	Nuclear localization of an O-glycosylated protein phosphotyrosine phosphatase from human cells.
1647397	4	22	with	elution	982:988	arg1	N-acetylglucosamine					995:1013	N-acetylglucosamine	995:1013	N-acetylglucosamine	995:1013	Immunoreactive p65 was recovered from immobilized wheat germ agglutinin (WGA) upon elution with N-acetylglucosamine; similarly, WGA recognized immunoaffinity-purified p65 on blots.
1647397	2	23	theme	NH4	314:316	arg1	precipitation					323:335	(NH4)2SO4 precipitation	313:335	(NH4)2SO4 precipitation	313:335	The enzyme, purified 3400-fold from mitotic cell extracts by (NH4)2SO4 precipitation, DEAE chromatography, and immunoaffinity chromatography on immobilized anti-p65 IgG, was inhibited by Zn2- and Na3VO4 but not NaF or beta-glycerophosphate; 32P-labeled poly(Glu, Tyr) was more efficiently dephosphorylated than phosphorylated histone or phosphorylase a. Indirect immunofluorescence showed most of the phosphatase to be localized in the nucleus of interphase cells, with a fine, granular distribution unaltered by detergent extraction; in mitotic cells, p65 was localized on chromosomes.
1647397	5	24	theme	phosphatase	1158:1168	arg1	p65					1170:1172	phosphatase p65	1158:1172	phosphatase p65	1158:1172	Alkaline hydrolysis of blotted protein prevented WGA binding, indicating that phosphatase p65, like a small group of other nuclear proteins, contains O-linked carbohydrate terminating in N-acetylglucosamine.
1647397	2	25	located	localized	671:679	arg2	phosphatase					653:663	the phosphatase to be localized in the nucleus of interphase cells, with a fine, granular distribution unaltered by detergent extraction	649:784	the phosphatase to be localized in the nucleus of interphase cells, with a fine, granular distribution unaltered by detergent extraction	649:784	The enzyme, purified 3400-fold from mitotic cell extracts by (NH4)2SO4 precipitation, DEAE chromatography, and immunoaffinity chromatography on immobilized anti-p65 IgG, was inhibited by Zn2- and Na3VO4 but not NaF or beta-glycerophosphate; 32P-labeled poly(Glu, Tyr) was more efficiently dephosphorylated than phosphorylated histone or phosphorylase a. Indirect immunofluorescence showed most of the phosphatase to be localized in the nucleus of interphase cells, with a fine, granular distribution unaltered by detergent extraction; in mitotic cells, p65 was localized on chromosomes.
1647397	2	25	located	localized	671:679	arg1	nucleus					688:694	the nucleus	684:694	the nucleus of interphase cells	684:714	The enzyme, purified 3400-fold from mitotic cell extracts by (NH4)2SO4 precipitation, DEAE chromatography, and immunoaffinity chromatography on immobilized anti-p65 IgG, was inhibited by Zn2- and Na3VO4 but not NaF or beta-glycerophosphate; 32P-labeled poly(Glu, Tyr) was more efficiently dephosphorylated than phosphorylated histone or phosphorylase a. Indirect immunofluorescence showed most of the phosphatase to be localized in the nucleus of interphase cells, with a fine, granular distribution unaltered by detergent extraction; in mitotic cells, p65 was localized on chromosomes.
1647397	4	26	theme	immunoaffinity-purified	1042:1064	arg1	p65					1066:1068	immunoaffinity-purified p65	1042:1068	immunoaffinity-purified p65	1042:1068	Immunoreactive p65 was recovered from immobilized wheat germ agglutinin (WGA) upon elution with N-acetylglucosamine; similarly, WGA recognized immunoaffinity-purified p65 on blots.
1647397	5	27	theme	other	1197:1201	arg1	proteins					1211:1218	other nuclear proteins	1197:1218	other nuclear proteins	1197:1218	Alkaline hydrolysis of blotted protein prevented WGA binding, indicating that phosphatase p65, like a small group of other nuclear proteins, contains O-linked carbohydrate terminating in N-acetylglucosamine.
1647397	1	28	theme	immunoprecipitates	122:139	arg1	staining					110:117	Histochemical staining	96:117	Histochemical staining of immunoprecipitates of p65, a component of human M phase-promoting factor,	96:194	Histochemical staining of immunoprecipitates of p65, a component of human M phase-promoting factor, identified the molecule as having phosphatase activity.
1647397	0	29	theme	protein	42:48	arg1	phosphatase					66:76	an O-glycosylated protein phosphotyrosine phosphatase	24:76	an O-glycosylated protein phosphotyrosine phosphatase from human cells	24:93	Nuclear localization of an O-glycosylated protein phosphotyrosine phosphatase from human cells.
1647397	5	30	theme	nuclear	1203:1209	arg1	proteins					1211:1218	other nuclear proteins	1197:1218	other nuclear proteins	1197:1218	Alkaline hydrolysis of blotted protein prevented WGA binding, indicating that phosphatase p65, like a small group of other nuclear proteins, contains O-linked carbohydrate terminating in N-acetylglucosamine.
1647397	4	31	theme	wheat	949:953	arg1	WGA					972:974	WGA	972:974	WGA	972:974	Immunoreactive p65 was recovered from immobilized wheat germ agglutinin (WGA) upon elution with N-acetylglucosamine; similarly, WGA recognized immunoaffinity-purified p65 on blots.
1647397	4	31	theme	wheat	949:953	arg1	agglutinin					960:969	immobilized wheat germ agglutinin	937:969	immobilized wheat germ agglutinin (WGA)	937:975	Immunoreactive p65 was recovered from immobilized wheat germ agglutinin (WGA) upon elution with N-acetylglucosamine; similarly, WGA recognized immunoaffinity-purified p65 on blots.
1647397	0	32	from	cells	89:93	arg1	localization					8:19	Nuclear localization	0:19	Nuclear localization of an O-glycosylated protein phosphotyrosine phosphatase from human cells	0:93	Nuclear localization of an O-glycosylated protein phosphotyrosine phosphatase from human cells.
1647397	0	32	from	cells	89:93	arg1	phosphatase					66:76	an O-glycosylated protein phosphotyrosine phosphatase	24:76	an O-glycosylated protein phosphotyrosine phosphatase from human cells	24:93	Nuclear localization of an O-glycosylated protein phosphotyrosine phosphatase from human cells.
1647397	2	33	theme	detergent	765:773	arg1	extraction					775:784	detergent extraction	765:784	detergent extraction	765:784	The enzyme, purified 3400-fold from mitotic cell extracts by (NH4)2SO4 precipitation, DEAE chromatography, and immunoaffinity chromatography on immobilized anti-p65 IgG, was inhibited by Zn2- and Na3VO4 but not NaF or beta-glycerophosphate; 32P-labeled poly(Glu, Tyr) was more efficiently dephosphorylated than phosphorylated histone or phosphorylase a. Indirect immunofluorescence showed most of the phosphatase to be localized in the nucleus of interphase cells, with a fine, granular distribution unaltered by detergent extraction; in mitotic cells, p65 was localized on chromosomes.
1647397	0	34	theme	O-glycosylated	27:40	arg1	phosphatase					66:76	an O-glycosylated protein phosphotyrosine phosphatase	24:76	an O-glycosylated protein phosphotyrosine phosphatase from human cells	24:93	Nuclear localization of an O-glycosylated protein phosphotyrosine phosphatase from human cells.
1647397	4	35	theme	immobilized	937:947	arg1	WGA					972:974	WGA	972:974	WGA	972:974	Immunoreactive p65 was recovered from immobilized wheat germ agglutinin (WGA) upon elution with N-acetylglucosamine; similarly, WGA recognized immunoaffinity-purified p65 on blots.
1647397	4	35	theme	immobilized	937:947	arg1	agglutinin					960:969	immobilized wheat germ agglutinin	937:969	immobilized wheat germ agglutinin (WGA)	937:975	Immunoreactive p65 was recovered from immobilized wheat germ agglutinin (WGA) upon elution with N-acetylglucosamine; similarly, WGA recognized immunoaffinity-purified p65 on blots.
1647397	5	36	theme	blotted	1103:1109	arg1	protein					1111:1117	blotted protein	1103:1117	blotted protein	1103:1117	Alkaline hydrolysis of blotted protein prevented WGA binding, indicating that phosphatase p65, like a small group of other nuclear proteins, contains O-linked carbohydrate terminating in N-acetylglucosamine.
1647397	0	37	theme	phosphatase	66:76	arg1	localization					8:19	Nuclear localization	0:19	Nuclear localization of an O-glycosylated protein phosphotyrosine phosphatase from human cells	0:93	Nuclear localization of an O-glycosylated protein phosphotyrosine phosphatase from human cells.
1647397	4	38	theme	Immunoreactive	899:912	arg1	p65					914:916	Immunoreactive p65	899:916	Immunoreactive p65	899:916	Immunoreactive p65 was recovered from immobilized wheat germ agglutinin (WGA) upon elution with N-acetylglucosamine; similarly, WGA recognized immunoaffinity-purified p65 on blots.
1647397	5	39	theme	protein	1111:1117	arg1	hydrolysis					1089:1098	Alkaline hydrolysis	1080:1098	Alkaline hydrolysis of blotted protein	1080:1117	Alkaline hydrolysis of blotted protein prevented WGA binding, indicating that phosphatase p65, like a small group of other nuclear proteins, contains O-linked carbohydrate terminating in N-acetylglucosamine.
1647397	2	40	theme	cells	710:714	arg1	nucleus					688:694	the nucleus	684:694	the nucleus of interphase cells	684:714	The enzyme, purified 3400-fold from mitotic cell extracts by (NH4)2SO4 precipitation, DEAE chromatography, and immunoaffinity chromatography on immobilized anti-p65 IgG, was inhibited by Zn2- and Na3VO4 but not NaF or beta-glycerophosphate; 32P-labeled poly(Glu, Tyr) was more efficiently dephosphorylated than phosphorylated histone or phosphorylase a. Indirect immunofluorescence showed most of the phosphatase to be localized in the nucleus of interphase cells, with a fine, granular distribution unaltered by detergent extraction; in mitotic cells, p65 was localized on chromosomes.
1647397	2	41	theme	DEAE	338:341	arg1	chromatography					343:356	DEAE chromatography	338:356	DEAE chromatography	338:356	The enzyme, purified 3400-fold from mitotic cell extracts by (NH4)2SO4 precipitation, DEAE chromatography, and immunoaffinity chromatography on immobilized anti-p65 IgG, was inhibited by Zn2- and Na3VO4 but not NaF or beta-glycerophosphate; 32P-labeled poly(Glu, Tyr) was more efficiently dephosphorylated than phosphorylated histone or phosphorylase a. Indirect immunofluorescence showed most of the phosphatase to be localized in the nucleus of interphase cells, with a fine, granular distribution unaltered by detergent extraction; in mitotic cells, p65 was localized on chromosomes.
1647397	0	42	theme	phosphotyrosine	50:64	arg1	phosphatase					66:76	an O-glycosylated protein phosphotyrosine phosphatase	24:76	an O-glycosylated protein phosphotyrosine phosphatase from human cells	24:93	Nuclear localization of an O-glycosylated protein phosphotyrosine phosphatase from human cells.
1647397	2	43	theme	phosphorylated	563:576	arg1	histone					578:584	phosphorylated histone	563:584	phosphorylated histone	563:584	The enzyme, purified 3400-fold from mitotic cell extracts by (NH4)2SO4 precipitation, DEAE chromatography, and immunoaffinity chromatography on immobilized anti-p65 IgG, was inhibited by Zn2- and Na3VO4 but not NaF or beta-glycerophosphate; 32P-labeled poly(Glu, Tyr) was more efficiently dephosphorylated than phosphorylated histone or phosphorylase a. Indirect immunofluorescence showed most of the phosphatase to be localized in the nucleus of interphase cells, with a fine, granular distribution unaltered by detergent extraction; in mitotic cells, p65 was localized on chromosomes.
1647397	2	44	theme	interphase	699:708	arg1	cells					710:714	interphase cells	699:714	interphase cells	699:714	The enzyme, purified 3400-fold from mitotic cell extracts by (NH4)2SO4 precipitation, DEAE chromatography, and immunoaffinity chromatography on immobilized anti-p65 IgG, was inhibited by Zn2- and Na3VO4 but not NaF or beta-glycerophosphate; 32P-labeled poly(Glu, Tyr) was more efficiently dephosphorylated than phosphorylated histone or phosphorylase a. Indirect immunofluorescence showed most of the phosphatase to be localized in the nucleus of interphase cells, with a fine, granular distribution unaltered by detergent extraction; in mitotic cells, p65 was localized on chromosomes.
1647397	1	45	theme	p65	144:146	arg1	immunoprecipitates					122:139	immunoprecipitates	122:139	immunoprecipitates of p65, a component of human M phase-promoting factor,	122:194	Histochemical staining of immunoprecipitates of p65, a component of human M phase-promoting factor, identified the molecule as having phosphatase activity.
1647397	5	46	theme	small	1182:1186	arg1	proteins					1211:1218	other nuclear proteins	1197:1218	other nuclear proteins	1197:1218	Alkaline hydrolysis of blotted protein prevented WGA binding, indicating that phosphatase p65, like a small group of other nuclear proteins, contains O-linked carbohydrate terminating in N-acetylglucosamine.
1647397	5	46	theme	small	1182:1186	arg1	group					1188:1192	a small group	1180:1192	a small group of other nuclear proteins	1180:1218	Alkaline hydrolysis of blotted protein prevented WGA binding, indicating that phosphatase p65, like a small group of other nuclear proteins, contains O-linked carbohydrate terminating in N-acetylglucosamine.
1647397	0	47	gly	O-glycosylated	27:40	arg1	phosphatase					66:76	an O-glycosylated protein phosphotyrosine phosphatase	24:76	an O-glycosylated protein phosphotyrosine phosphatase from human cells	24:93	Nuclear localization of an O-glycosylated protein phosphotyrosine phosphatase from human cells.
1647397	3	48	theme	subcellular	848:858	arg1	fractions					860:868	subcellular fractions	848:868	subcellular fractions	848:868	ELISA of subcellular fractions confirmed this localization.
1647397	1	49	theme	phosphatase	230:240	arg1	activity					242:249	phosphatase activity	230:249	phosphatase activity	230:249	Histochemical staining of immunoprecipitates of p65, a component of human M phase-promoting factor, identified the molecule as having phosphatase activity.
1647397	2	50	theme	immobilized	396:406	arg1	IgG					417:419	immobilized anti-p65 IgG	396:419	immobilized anti-p65 IgG	396:419	The enzyme, purified 3400-fold from mitotic cell extracts by (NH4)2SO4 precipitation, DEAE chromatography, and immunoaffinity chromatography on immobilized anti-p65 IgG, was inhibited by Zn2- and Na3VO4 but not NaF or beta-glycerophosphate; 32P-labeled poly(Glu, Tyr) was more efficiently dephosphorylated than phosphorylated histone or phosphorylase a. Indirect immunofluorescence showed most of the phosphatase to be localized in the nucleus of interphase cells, with a fine, granular distribution unaltered by detergent extraction; in mitotic cells, p65 was localized on chromosomes.
1647397	2	51	theme	2SO4	318:321	arg1	precipitation					323:335	(NH4)2SO4 precipitation	313:335	(NH4)2SO4 precipitation	313:335	The enzyme, purified 3400-fold from mitotic cell extracts by (NH4)2SO4 precipitation, DEAE chromatography, and immunoaffinity chromatography on immobilized anti-p65 IgG, was inhibited by Zn2- and Na3VO4 but not NaF or beta-glycerophosphate; 32P-labeled poly(Glu, Tyr) was more efficiently dephosphorylated than phosphorylated histone or phosphorylase a. Indirect immunofluorescence showed most of the phosphatase to be localized in the nucleus of interphase cells, with a fine, granular distribution unaltered by detergent extraction; in mitotic cells, p65 was localized on chromosomes.
1647397	0	52	theme	human	83:87	arg1	cells					89:93	human cells	83:93	human cells	83:93	Nuclear localization of an O-glycosylated protein phosphotyrosine phosphatase from human cells.
1647397	5	53	theme	Alkaline	1080:1087	arg1	hydrolysis					1089:1098	Alkaline hydrolysis	1080:1098	Alkaline hydrolysis of blotted protein	1080:1117	Alkaline hydrolysis of blotted protein prevented WGA binding, indicating that phosphatase p65, like a small group of other nuclear proteins, contains O-linked carbohydrate terminating in N-acetylglucosamine.
1647397	2	54	theme	fine	724:727	arg1	distribution					739:750	a fine, granular distribution	722:750	a fine, granular distribution unaltered by detergent extraction	722:784	The enzyme, purified 3400-fold from mitotic cell extracts by (NH4)2SO4 precipitation, DEAE chromatography, and immunoaffinity chromatography on immobilized anti-p65 IgG, was inhibited by Zn2- and Na3VO4 but not NaF or beta-glycerophosphate; 32P-labeled poly(Glu, Tyr) was more efficiently dephosphorylated than phosphorylated histone or phosphorylase a. Indirect immunofluorescence showed most of the phosphatase to be localized in the nucleus of interphase cells, with a fine, granular distribution unaltered by detergent extraction; in mitotic cells, p65 was localized on chromosomes.
1647397	2	55	theme	immunoaffinity	363:376	arg1	chromatography					378:391	immunoaffinity chromatography	363:391	immunoaffinity chromatography	363:391	The enzyme, purified 3400-fold from mitotic cell extracts by (NH4)2SO4 precipitation, DEAE chromatography, and immunoaffinity chromatography on immobilized anti-p65 IgG, was inhibited by Zn2- and Na3VO4 but not NaF or beta-glycerophosphate; 32P-labeled poly(Glu, Tyr) was more efficiently dephosphorylated than phosphorylated histone or phosphorylase a. Indirect immunofluorescence showed most of the phosphatase to be localized in the nucleus of interphase cells, with a fine, granular distribution unaltered by detergent extraction; in mitotic cells, p65 was localized on chromosomes.
1647397	2	56	theme	mitotic	790:796	arg1	cells					798:802	mitotic cells	790:802	mitotic cells	790:802	The enzyme, purified 3400-fold from mitotic cell extracts by (NH4)2SO4 precipitation, DEAE chromatography, and immunoaffinity chromatography on immobilized anti-p65 IgG, was inhibited by Zn2- and Na3VO4 but not NaF or beta-glycerophosphate; 32P-labeled poly(Glu, Tyr) was more efficiently dephosphorylated than phosphorylated histone or phosphorylase a. Indirect immunofluorescence showed most of the phosphatase to be localized in the nucleus of interphase cells, with a fine, granular distribution unaltered by detergent extraction; in mitotic cells, p65 was localized on chromosomes.
1647397	2	57	theme	32P-labeled	493:503	arg1	poly					505:508	32P-labeled poly	493:508	32P-labeled poly(Glu, Tyr)	493:518	The enzyme, purified 3400-fold from mitotic cell extracts by (NH4)2SO4 precipitation, DEAE chromatography, and immunoaffinity chromatography on immobilized anti-p65 IgG, was inhibited by Zn2- and Na3VO4 but not NaF or beta-glycerophosphate; 32P-labeled poly(Glu, Tyr) was more efficiently dephosphorylated than phosphorylated histone or phosphorylase a. Indirect immunofluorescence showed most of the phosphatase to be localized in the nucleus of interphase cells, with a fine, granular distribution unaltered by detergent extraction; in mitotic cells, p65 was localized on chromosomes.
1647397	2	57	theme	32P-labeled	493:503	arg1	Tyr					515:517	Tyr	515:517	Tyr	515:517	The enzyme, purified 3400-fold from mitotic cell extracts by (NH4)2SO4 precipitation, DEAE chromatography, and immunoaffinity chromatography on immobilized anti-p65 IgG, was inhibited by Zn2- and Na3VO4 but not NaF or beta-glycerophosphate; 32P-labeled poly(Glu, Tyr) was more efficiently dephosphorylated than phosphorylated histone or phosphorylase a. Indirect immunofluorescence showed most of the phosphatase to be localized in the nucleus of interphase cells, with a fine, granular distribution unaltered by detergent extraction; in mitotic cells, p65 was localized on chromosomes.
3117790	8	0	theme	amino	1095:1099	arg1	acids					1101:1105	the last 117 amino acids	1082:1105	the last 117 amino acids of the carboxy terminus of Band 4.1	1082:1141	One of the sites of O-GlcNAc addition has been localized to the last 117 amino acids of the carboxy terminus of Band 4.1.
3117790	5	1	theme	techniques	663:672	arg1	techniques					663:672	chemical and enzymatic techniques	640:672	chemical and enzymatic techniques	640:672	The proportion of the incorporated label found on O-GlcNAc was determined by a variety of chemical and enzymatic techniques.
3117790	5	1	theme	techniques	663:672	arg1	variety					629:635	a variety	627:635	a variety of chemical and enzymatic techniques	627:672	The proportion of the incorporated label found on O-GlcNAc was determined by a variety of chemical and enzymatic techniques.
3117790	4	2	theme	bovine	492:497	arg1	galactosyltransferase					504:524	bovine milk galactosyltransferase	492:524	bovine milk galactosyltransferase	492:524	Intact or permeabilized erythrocytes, as well as subcellular fractions, were labeled with bovine milk galactosyltransferase and UDP-[3H] galactose.
3117790	3	3	theme	O-GlcNAc	326:333	arg1	moieties					335:342	O-GlcNAc moieties	326:342	O-GlcNAc moieties	326:342	Here we demonstrate that O-GlcNAc moieties are also added to human erythrocyte cytoplasmic proteins.
3117790	2	4	theme	protein-saccharide	115:132	arg1	linkage					134:140	the novel protein-saccharide linkage	105:140	the novel protein-saccharide linkage	105:140	Previously we reported that the novel protein-saccharide linkage, O-linked N-acetylglucosamine (GlcNAc), is found in abundance on proteins associated with the cytoplasmic and nucleoplasmic faces of the nuclear pore complex.
3117790	2	4	theme	protein-saccharide	115:132	arg1	N-acetylglucosamine					152:170	O-linked N-acetylglucosamine	143:170	O-linked N-acetylglucosamine (GlcNAc)	143:179	Previously we reported that the novel protein-saccharide linkage, O-linked N-acetylglucosamine (GlcNAc), is found in abundance on proteins associated with the cytoplasmic and nucleoplasmic faces of the nuclear pore complex.
3117790	4	5	theme	UDP-[3H	530:536	arg1	galactose					539:547	UDP-[3H] galactose	530:547	UDP-[3H] galactose	530:547	Intact or permeabilized erythrocytes, as well as subcellular fractions, were labeled with bovine milk galactosyltransferase and UDP-[3H] galactose.
3117790	7	6	theme	inner	935:939	arg1	surface					941:947	the inner surface	931:947	the inner surface of the plasma membrane	931:970	In addition, we have determined that Band 4.1, a protein which serves as a bridge joining the cytoskeleton to the inner surface of the plasma membrane in erythrocytes, also contains O-GlcNAc moieties.
3117790	4	7	theme	Intact	402:407	arg1	erythrocytes					426:437	Intact or permeabilized erythrocytes	402:437	Intact or permeabilized erythrocytes	402:437	Intact or permeabilized erythrocytes, as well as subcellular fractions, were labeled with bovine milk galactosyltransferase and UDP-[3H] galactose.
3117790	2	8	theme	complex	292:298	arg1	faces					266:270	the cytoplasmic and nucleoplasmic faces	232:270	the cytoplasmic and nucleoplasmic faces of the nuclear pore complex	232:298	Previously we reported that the novel protein-saccharide linkage, O-linked N-acetylglucosamine (GlcNAc), is found in abundance on proteins associated with the cytoplasmic and nucleoplasmic faces of the nuclear pore complex.
3117790	3	9	theme	human	362:366	arg1	proteins					392:399	human erythrocyte cytoplasmic proteins	362:399	human erythrocyte cytoplasmic proteins	362:399	Here we demonstrate that O-GlcNAc moieties are also added to human erythrocyte cytoplasmic proteins.
3117790	6	10	theme	unidentified	792:803	arg1	protein					812:818	an as yet unidentified 65-kDa protein	782:818	an as yet unidentified 65-kDa protein	782:818	The bulk of the O-GlcNAc residues are found in the cytoplasm of erythrocytes, the majority of which are on an as yet unidentified 65-kDa protein.
3117790	2	11	theme	pore	287:290	arg1	complex					292:298	the nuclear pore complex	275:298	the nuclear pore complex	275:298	Previously we reported that the novel protein-saccharide linkage, O-linked N-acetylglucosamine (GlcNAc), is found in abundance on proteins associated with the cytoplasmic and nucleoplasmic faces of the nuclear pore complex.
3117790	7	12	contain	contains	994:1001	arg1	Band					858:861	Band 4.1	858:865	Band 4.1	858:865	In addition, we have determined that Band 4.1, a protein which serves as a bridge joining the cytoskeleton to the inner surface of the plasma membrane in erythrocytes, also contains O-GlcNAc moieties.
3117790	7	12	contain	contains	994:1001	arg2	moieties					1012:1019	O-GlcNAc moieties	1003:1019	O-GlcNAc moieties	1003:1019	In addition, we have determined that Band 4.1, a protein which serves as a bridge joining the cytoskeleton to the inner surface of the plasma membrane in erythrocytes, also contains O-GlcNAc moieties.
3117790	7	12	contain	contains	994:1001	arg1	protein					870:876	a protein	868:876	a protein which serves as a bridge joining the cytoskeleton to the inner surface of the plasma membrane in erythrocytes	868:986	In addition, we have determined that Band 4.1, a protein which serves as a bridge joining the cytoskeleton to the inner surface of the plasma membrane in erythrocytes, also contains O-GlcNAc moieties.
3117790	8	13	theme	carboxy	1114:1120	arg1	terminus					1122:1129	the carboxy terminus	1110:1129	the carboxy terminus of Band 4.1	1110:1141	One of the sites of O-GlcNAc addition has been localized to the last 117 amino acids of the carboxy terminus of Band 4.1.
3117790	4	14	theme	permeabilized	412:424	arg1	erythrocytes					426:437	Intact or permeabilized erythrocytes	402:437	Intact or permeabilized erythrocytes	402:437	Intact or permeabilized erythrocytes, as well as subcellular fractions, were labeled with bovine milk galactosyltransferase and UDP-[3H] galactose.
3117790	2	15	theme	nuclear	279:285	arg1	complex					292:298	the nuclear pore complex	275:298	the nuclear pore complex	275:298	Previously we reported that the novel protein-saccharide linkage, O-linked N-acetylglucosamine (GlcNAc), is found in abundance on proteins associated with the cytoplasmic and nucleoplasmic faces of the nuclear pore complex.
3117790	8	16	theme	Band	1134:1137	arg1	terminus					1122:1129	the carboxy terminus	1110:1129	the carboxy terminus of Band 4.1	1110:1141	One of the sites of O-GlcNAc addition has been localized to the last 117 amino acids of the carboxy terminus of Band 4.1.
3117790	4	17	theme	milk	499:502	arg1	galactosyltransferase					504:524	bovine milk galactosyltransferase	492:524	bovine milk galactosyltransferase	492:524	Intact or permeabilized erythrocytes, as well as subcellular fractions, were labeled with bovine milk galactosyltransferase and UDP-[3H] galactose.
3117790	5	18	theme	chemical	640:647	arg1	techniques					663:672	chemical and enzymatic techniques	640:672	chemical and enzymatic techniques	640:672	The proportion of the incorporated label found on O-GlcNAc was determined by a variety of chemical and enzymatic techniques.
3117790	7	19	theme	plasma	956:961	arg1	membrane					963:970	the plasma membrane	952:970	the plasma membrane	952:970	In addition, we have determined that Band 4.1, a protein which serves as a bridge joining the cytoskeleton to the inner surface of the plasma membrane in erythrocytes, also contains O-GlcNAc moieties.
3117790	2	20	theme	O-linked	143:150	arg1	linkage					134:140	the novel protein-saccharide linkage	105:140	the novel protein-saccharide linkage	105:140	Previously we reported that the novel protein-saccharide linkage, O-linked N-acetylglucosamine (GlcNAc), is found in abundance on proteins associated with the cytoplasmic and nucleoplasmic faces of the nuclear pore complex.
3117790	2	20	theme	O-linked	143:150	arg1	N-acetylglucosamine					152:170	O-linked N-acetylglucosamine	143:170	O-linked N-acetylglucosamine (GlcNAc)	143:179	Previously we reported that the novel protein-saccharide linkage, O-linked N-acetylglucosamine (GlcNAc), is found in abundance on proteins associated with the cytoplasmic and nucleoplasmic faces of the nuclear pore complex.
3117790	2	20	theme	O-linked	143:150	arg1	GlcNAc					173:178	GlcNAc	173:178	GlcNAc	173:178	Previously we reported that the novel protein-saccharide linkage, O-linked N-acetylglucosamine (GlcNAc), is found in abundance on proteins associated with the cytoplasmic and nucleoplasmic faces of the nuclear pore complex.
3117790	5	21	dep	the	568:570	arg1	label					585:589	label	585:589	label	585:589	The proportion of the incorporated label found on O-GlcNAc was determined by a variety of chemical and enzymatic techniques.
3117790	8	22	theme	terminus	1122:1129	arg1	acids					1101:1105	the last 117 amino acids	1082:1105	the last 117 amino acids of the carboxy terminus of Band 4.1	1082:1141	One of the sites of O-GlcNAc addition has been localized to the last 117 amino acids of the carboxy terminus of Band 4.1.
3117790	5	23	theme	enzymatic	653:661	arg1	techniques					663:672	chemical and enzymatic techniques	640:672	chemical and enzymatic techniques	640:672	The proportion of the incorporated label found on O-GlcNAc was determined by a variety of chemical and enzymatic techniques.
3117790	6	24	theme	residues	700:707	arg1	bulk					679:682	The bulk	675:682	The bulk of the O-GlcNAc residues	675:707	The bulk of the O-GlcNAc residues are found in the cytoplasm of erythrocytes, the majority of which are on an as yet unidentified 65-kDa protein.
3117790	4	25	theme	subcellular	451:461	arg1	fractions					463:471	subcellular fractions	451:471	subcellular fractions	451:471	Intact or permeabilized erythrocytes, as well as subcellular fractions, were labeled with bovine milk galactosyltransferase and UDP-[3H] galactose.
3117790	3	26	theme	erythrocyte	368:378	arg1	proteins					392:399	human erythrocyte cytoplasmic proteins	362:399	human erythrocyte cytoplasmic proteins	362:399	Here we demonstrate that O-GlcNAc moieties are also added to human erythrocyte cytoplasmic proteins.
3117790	0	27	contain	contain	13:19	arg1	Erythrocytes					0:11	Erythrocytes	0:11	Erythrocytes	0:11	Erythrocytes contain cytoplasmic glycoproteins.
3117790	0	27	contain	contain	13:19	arg2	glycoproteins					33:45	cytoplasmic glycoproteins	21:45	cytoplasmic glycoproteins	21:45	Erythrocytes contain cytoplasmic glycoproteins.
3117790	6	28	theme	O-GlcNAc	691:698	arg1	residues					700:707	the O-GlcNAc residues	687:707	the O-GlcNAc residues	687:707	The bulk of the O-GlcNAc residues are found in the cytoplasm of erythrocytes, the majority of which are on an as yet unidentified 65-kDa protein.
3117790	1	29	dep	GlcNAc	57:62	arg1	Band					67:70	Band 4.1	67:74	Band 4.1	67:74	O-linked GlcNAc on Band 4.1.
3117790	0	30	theme	cytoplasmic	21:31	arg1	glycoproteins					33:45	cytoplasmic glycoproteins	21:45	cytoplasmic glycoproteins	21:45	Erythrocytes contain cytoplasmic glycoproteins.
3117790	8	31	theme	sites	1033:1037	arg1	One					1022:1024	One	1022:1024	One	1022:1024	One of the sites of O-GlcNAc addition has been localized to the last 117 amino acids of the carboxy terminus of Band 4.1.
3117790	8	31	theme	sites	1033:1037	arg1	sites					1033:1037	the sites	1029:1037	the sites of O-GlcNAc addition	1029:1058	One of the sites of O-GlcNAc addition has been localized to the last 117 amino acids of the carboxy terminus of Band 4.1.
3117790	8	31	theme	sites	1033:1037	arg1	addition					1051:1058	O-GlcNAc addition	1042:1058	O-GlcNAc addition	1042:1058	One of the sites of O-GlcNAc addition has been localized to the last 117 amino acids of the carboxy terminus of Band 4.1.
3117790	2	32	located	found	185:189	arg1	abundance					194:202	abundance	194:202	abundance	194:202	Previously we reported that the novel protein-saccharide linkage, O-linked N-acetylglucosamine (GlcNAc), is found in abundance on proteins associated with the cytoplasmic and nucleoplasmic faces of the nuclear pore complex.
3117790	2	32	located	found	185:189	arg2	N-acetylglucosamine					152:170	O-linked N-acetylglucosamine	143:170	O-linked N-acetylglucosamine (GlcNAc)	143:179	Previously we reported that the novel protein-saccharide linkage, O-linked N-acetylglucosamine (GlcNAc), is found in abundance on proteins associated with the cytoplasmic and nucleoplasmic faces of the nuclear pore complex.
3117790	2	32	located	found	185:189	arg1	proteins					207:214	proteins	207:214	proteins associated with the cytoplasmic and nucleoplasmic faces of the nuclear pore complex	207:298	Previously we reported that the novel protein-saccharide linkage, O-linked N-acetylglucosamine (GlcNAc), is found in abundance on proteins associated with the cytoplasmic and nucleoplasmic faces of the nuclear pore complex.
3117790	2	32	located	found	185:189	arg2	linkage					134:140	the novel protein-saccharide linkage	105:140	the novel protein-saccharide linkage	105:140	Previously we reported that the novel protein-saccharide linkage, O-linked N-acetylglucosamine (GlcNAc), is found in abundance on proteins associated with the cytoplasmic and nucleoplasmic faces of the nuclear pore complex.
3117790	8	33	theme	addition	1051:1058	arg1	sites					1033:1037	the sites	1029:1037	the sites of O-GlcNAc addition	1029:1058	One of the sites of O-GlcNAc addition has been localized to the last 117 amino acids of the carboxy terminus of Band 4.1.
3117790	8	33	theme	addition	1051:1058	arg1	addition					1051:1058	O-GlcNAc addition	1042:1058	O-GlcNAc addition	1042:1058	One of the sites of O-GlcNAc addition has been localized to the last 117 amino acids of the carboxy terminus of Band 4.1.
3117790	1	34	link	O-linked	48:55	arg1	GlcNAc					57:62	O-linked GlcNAc	48:62	O-linked GlcNAc	48:62	O-linked GlcNAc on Band 4.1.
3117790	2	35	theme	cytoplasmic	236:246	arg1	faces					266:270	the cytoplasmic and nucleoplasmic faces	232:270	the cytoplasmic and nucleoplasmic faces of the nuclear pore complex	232:298	Previously we reported that the novel protein-saccharide linkage, O-linked N-acetylglucosamine (GlcNAc), is found in abundance on proteins associated with the cytoplasmic and nucleoplasmic faces of the nuclear pore complex.
3117790	5	36	located	found	591:595	arg1	O-GlcNAc					600:607	O-GlcNAc	600:607	O-GlcNAc	600:607	The proportion of the incorporated label found on O-GlcNAc was determined by a variety of chemical and enzymatic techniques.
3117790	5	36	located	found	591:595	arg2	the					568:570	the	568:570	the	568:570	The proportion of the incorporated label found on O-GlcNAc was determined by a variety of chemical and enzymatic techniques.
3117790	8	37	theme	O-GlcNAc	1042:1049	arg1	addition					1051:1058	O-GlcNAc addition	1042:1058	O-GlcNAc addition	1042:1058	One of the sites of O-GlcNAc addition has been localized to the last 117 amino acids of the carboxy terminus of Band 4.1.
3117790	7	38	theme	O-GlcNAc	1003:1010	arg1	moieties					1012:1019	O-GlcNAc moieties	1003:1019	O-GlcNAc moieties	1003:1019	In addition, we have determined that Band 4.1, a protein which serves as a bridge joining the cytoskeleton to the inner surface of the plasma membrane in erythrocytes, also contains O-GlcNAc moieties.
3117790	5	39	theme	the	568:570	arg1	proportion					554:563	The proportion	550:563	The proportion of the incorporated label found on O-GlcNAc	550:607	The proportion of the incorporated label found on O-GlcNAc was determined by a variety of chemical and enzymatic techniques.
3117790	2	40	theme	novel	109:113	arg1	linkage					134:140	the novel protein-saccharide linkage	105:140	the novel protein-saccharide linkage	105:140	Previously we reported that the novel protein-saccharide linkage, O-linked N-acetylglucosamine (GlcNAc), is found in abundance on proteins associated with the cytoplasmic and nucleoplasmic faces of the nuclear pore complex.
3117790	2	40	theme	novel	109:113	arg1	N-acetylglucosamine					152:170	O-linked N-acetylglucosamine	143:170	O-linked N-acetylglucosamine (GlcNAc)	143:179	Previously we reported that the novel protein-saccharide linkage, O-linked N-acetylglucosamine (GlcNAc), is found in abundance on proteins associated with the cytoplasmic and nucleoplasmic faces of the nuclear pore complex.
3117790	0	41	gly	glycoproteins	33:45	arg1	glycoproteins					33:45	cytoplasmic glycoproteins	21:45	cytoplasmic glycoproteins	21:45	Erythrocytes contain cytoplasmic glycoproteins.
3117790	7	42	theme	membrane	963:970	arg1	surface					941:947	the inner surface	931:947	the inner surface of the plasma membrane	931:970	In addition, we have determined that Band 4.1, a protein which serves as a bridge joining the cytoskeleton to the inner surface of the plasma membrane in erythrocytes, also contains O-GlcNAc moieties.
3117790	6	43	theme	65-kDa	805:810	arg1	protein					812:818	an as yet unidentified 65-kDa protein	782:818	an as yet unidentified 65-kDa protein	782:818	The bulk of the O-GlcNAc residues are found in the cytoplasm of erythrocytes, the majority of which are on an as yet unidentified 65-kDa protein.
3117790	1	44	theme	O-linked	48:55	arg1	GlcNAc					57:62	O-linked GlcNAc	48:62	O-linked GlcNAc	48:62	O-linked GlcNAc on Band 4.1.
3117790	8	45	theme	last	1086:1089	arg1	acids					1101:1105	the last 117 amino acids	1082:1105	the last 117 amino acids of the carboxy terminus of Band 4.1	1082:1141	One of the sites of O-GlcNAc addition has been localized to the last 117 amino acids of the carboxy terminus of Band 4.1.
3117790	2	46	theme	nucleoplasmic	252:264	arg1	faces					266:270	the cytoplasmic and nucleoplasmic faces	232:270	the cytoplasmic and nucleoplasmic faces of the nuclear pore complex	232:298	Previously we reported that the novel protein-saccharide linkage, O-linked N-acetylglucosamine (GlcNAc), is found in abundance on proteins associated with the cytoplasmic and nucleoplasmic faces of the nuclear pore complex.
3117790	6	47	theme	erythrocytes	739:750	arg1	majority					757:764	the majority	753:764	the majority	753:764	The bulk of the O-GlcNAc residues are found in the cytoplasm of erythrocytes, the majority of which are on an as yet unidentified 65-kDa protein.
3117790	6	47	theme	erythrocytes	739:750	arg1	cytoplasm					726:734	the cytoplasm	722:734	the cytoplasm of erythrocytes, the majority of which are on an as yet unidentified 65-kDa protein	722:818	The bulk of the O-GlcNAc residues are found in the cytoplasm of erythrocytes, the majority of which are on an as yet unidentified 65-kDa protein.
3117790	7	48	from	cytoskeleton	915:926	arg1	erythrocytes					975:986	erythrocytes	975:986	erythrocytes	975:986	In addition, we have determined that Band 4.1, a protein which serves as a bridge joining the cytoskeleton to the inner surface of the plasma membrane in erythrocytes, also contains O-GlcNAc moieties.
3117790	3	49	theme	cytoplasmic	380:390	arg1	proteins					392:399	human erythrocyte cytoplasmic proteins	362:399	human erythrocyte cytoplasmic proteins	362:399	Here we demonstrate that O-GlcNAc moieties are also added to human erythrocyte cytoplasmic proteins.
3117790	6	50	located	found	713:717	arg2	bulk					679:682	The bulk	675:682	The bulk of the O-GlcNAc residues	675:707	The bulk of the O-GlcNAc residues are found in the cytoplasm of erythrocytes, the majority of which are on an as yet unidentified 65-kDa protein.
3117790	6	50	located	found	713:717	arg1	cytoplasm					726:734	the cytoplasm	722:734	the cytoplasm of erythrocytes, the majority of which are on an as yet unidentified 65-kDa protein	722:818	The bulk of the O-GlcNAc residues are found in the cytoplasm of erythrocytes, the majority of which are on an as yet unidentified 65-kDa protein.
3117790	2	51	link	O-linked	143:150	arg1	linkage					134:140	the novel protein-saccharide linkage	105:140	the novel protein-saccharide linkage	105:140	Previously we reported that the novel protein-saccharide linkage, O-linked N-acetylglucosamine (GlcNAc), is found in abundance on proteins associated with the cytoplasmic and nucleoplasmic faces of the nuclear pore complex.
3117790	2	51	link	O-linked	143:150	arg1	N-acetylglucosamine					152:170	O-linked N-acetylglucosamine	143:170	O-linked N-acetylglucosamine (GlcNAc)	143:179	Previously we reported that the novel protein-saccharide linkage, O-linked N-acetylglucosamine (GlcNAc), is found in abundance on proteins associated with the cytoplasmic and nucleoplasmic faces of the nuclear pore complex.
3117790	2	51	link	O-linked	143:150	arg1	GlcNAc					173:178	GlcNAc	173:178	GlcNAc	173:178	Previously we reported that the novel protein-saccharide linkage, O-linked N-acetylglucosamine (GlcNAc), is found in abundance on proteins associated with the cytoplasmic and nucleoplasmic faces of the nuclear pore complex.
32938750	1	0	theme	regulatory	252:261	arg1	O-GlcNAcylation					81:95	O-GlcNAcylation	81:95	O-GlcNAcylation	81:95	O-GlcNAcylation, the addition of a single N-acetylglucosamine residue to serine and threonine residues of cytoplasmic, nuclear, or mitochondrial proteins, is a widespread regulatory posttranslational modification.
32938750	1	0	theme	regulatory	252:261	arg1	modification					281:292	a widespread regulatory posttranslational modification	239:292	a widespread regulatory posttranslational modification	239:292	O-GlcNAcylation, the addition of a single N-acetylglucosamine residue to serine and threonine residues of cytoplasmic, nuclear, or mitochondrial proteins, is a widespread regulatory posttranslational modification.
32938750	1	1	theme	posttranslational	263:279	arg1	O-GlcNAcylation					81:95	O-GlcNAcylation	81:95	O-GlcNAcylation	81:95	O-GlcNAcylation, the addition of a single N-acetylglucosamine residue to serine and threonine residues of cytoplasmic, nuclear, or mitochondrial proteins, is a widespread regulatory posttranslational modification.
32938750	1	1	theme	posttranslational	263:279	arg1	modification					281:292	a widespread regulatory posttranslational modification	239:292	a widespread regulatory posttranslational modification	239:292	O-GlcNAcylation, the addition of a single N-acetylglucosamine residue to serine and threonine residues of cytoplasmic, nuclear, or mitochondrial proteins, is a widespread regulatory posttranslational modification.
32938750	4	2	from	analysis	915:922	arg1	peptides					955:962	O-GlcNAc-modified peptides	937:962	O-GlcNAc-modified peptides	937:962	This article summarizes methods for O-GlcNAc enrichment, key mass spectrometry instrumentation advancements, particularly those that allow modification site localization, and software tools that allow analysis of data from O-GlcNAc-modified peptides.
32938750	4	3	theme	key	771:773	arg1	spectrometry					780:791	key mass spectrometry	771:791	key mass spectrometry instrumentation advancements	771:820	This article summarizes methods for O-GlcNAc enrichment, key mass spectrometry instrumentation advancements, particularly those that allow modification site localization, and software tools that allow analysis of data from O-GlcNAc-modified peptides.
32938750	4	4	theme	data	927:930	arg1	analysis					915:922	analysis	915:922	analysis of data from O-GlcNAc-modified peptides	915:962	This article summarizes methods for O-GlcNAc enrichment, key mass spectrometry instrumentation advancements, particularly those that allow modification site localization, and software tools that allow analysis of data from O-GlcNAc-modified peptides.
32938750	4	5	theme	instrumentation	793:807	arg1	advancements					809:820	key mass spectrometry instrumentation advancements	771:820	key mass spectrometry instrumentation advancements	771:820	This article summarizes methods for O-GlcNAc enrichment, key mass spectrometry instrumentation advancements, particularly those that allow modification site localization, and software tools that allow analysis of data from O-GlcNAc-modified peptides.
32938750	4	5	theme	instrumentation	793:807	arg1	those					836:840	those	836:840	those	836:840	This article summarizes methods for O-GlcNAc enrichment, key mass spectrometry instrumentation advancements, particularly those that allow modification site localization, and software tools that allow analysis of data from O-GlcNAc-modified peptides.
32938750	4	6	theme	software	889:896	arg1	tools					898:902	software tools	889:902	software tools	889:902	This article summarizes methods for O-GlcNAc enrichment, key mass spectrometry instrumentation advancements, particularly those that allow modification site localization, and software tools that allow analysis of data from O-GlcNAc-modified peptides.
32938750	3	7	theme	O-GlcNAcylation	542:556	arg1	function					530:537	the function	526:537	the function of O-GlcNAcylation	526:556	Although the modification was first detected over 35 years ago, research into the function of O-GlcNAcylation has accelerated dramatically in the last 10 years owing to the development of new enrichment and mass spectrometry techniques that facilitate its analysis.
32938750	1	8	theme	cytoplasmic	187:197	arg1	proteins					226:233	cytoplasmic, nuclear, or mitochondrial proteins	187:233	cytoplasmic, nuclear, or mitochondrial proteins	187:233	O-GlcNAcylation, the addition of a single N-acetylglucosamine residue to serine and threonine residues of cytoplasmic, nuclear, or mitochondrial proteins, is a widespread regulatory posttranslational modification.
32938750	2	9	theme	nutritional	329:339	arg1	status					341:346	nutritional status	329:346	nutritional status	329:346	It is involved in the response to nutritional status and stress, and its dysregulation is associated with diseases ranging from Alzheimer's to diabetes.
32938750	3	10	theme	last	594:597	arg1	10 years					599:606	the last 10 years	590:606	the last 10 years owing to the development of new enrichment and mass spectrometry techniques that facilitate its analysis	590:711	Although the modification was first detected over 35 years ago, research into the function of O-GlcNAcylation has accelerated dramatically in the last 10 years owing to the development of new enrichment and mass spectrometry techniques that facilitate its analysis.
32938750	1	11	theme	nuclear	200:206	arg1	proteins					226:233	cytoplasmic, nuclear, or mitochondrial proteins	187:233	cytoplasmic, nuclear, or mitochondrial proteins	187:233	O-GlcNAcylation, the addition of a single N-acetylglucosamine residue to serine and threonine residues of cytoplasmic, nuclear, or mitochondrial proteins, is a widespread regulatory posttranslational modification.
32938750	1	12	dep	serine	154:159	arg1	residues					175:182	residues	175:182	residues	175:182	O-GlcNAcylation, the addition of a single N-acetylglucosamine residue to serine and threonine residues of cytoplasmic, nuclear, or mitochondrial proteins, is a widespread regulatory posttranslational modification.
32938750	3	13	theme	spectrometry	660:671	arg1	techniques					673:682	new enrichment and mass spectrometry techniques	636:682	new enrichment and mass spectrometry techniques that facilitate its analysis	636:711	Although the modification was first detected over 35 years ago, research into the function of O-GlcNAcylation has accelerated dramatically in the last 10 years owing to the development of new enrichment and mass spectrometry techniques that facilitate its analysis.
32938750	4	14	theme	mass	775:778	arg1	spectrometry					780:791	key mass spectrometry	771:791	key mass spectrometry instrumentation advancements	771:820	This article summarizes methods for O-GlcNAc enrichment, key mass spectrometry instrumentation advancements, particularly those that allow modification site localization, and software tools that allow analysis of data from O-GlcNAc-modified peptides.
32938750	3	15	theme	techniques	673:682	arg1	development					621:631	the development	617:631	the development of new enrichment and mass spectrometry techniques that facilitate its analysis	617:711	Although the modification was first detected over 35 years ago, research into the function of O-GlcNAcylation has accelerated dramatically in the last 10 years owing to the development of new enrichment and mass spectrometry techniques that facilitate its analysis.
32938750	1	16	theme	mitochondrial	212:224	arg1	proteins					226:233	cytoplasmic, nuclear, or mitochondrial proteins	187:233	cytoplasmic, nuclear, or mitochondrial proteins	187:233	O-GlcNAcylation, the addition of a single N-acetylglucosamine residue to serine and threonine residues of cytoplasmic, nuclear, or mitochondrial proteins, is a widespread regulatory posttranslational modification.
32938750	4	17	theme	site	866:869	arg1	localization					871:882	modification site localization	853:882	modification site localization	853:882	This article summarizes methods for O-GlcNAc enrichment, key mass spectrometry instrumentation advancements, particularly those that allow modification site localization, and software tools that allow analysis of data from O-GlcNAc-modified peptides.
32938750	1	18	theme	proteins	226:233	arg1	threonine					165:173	threonine	165:173	threonine	165:173	O-GlcNAcylation, the addition of a single N-acetylglucosamine residue to serine and threonine residues of cytoplasmic, nuclear, or mitochondrial proteins, is a widespread regulatory posttranslational modification.
32938750	1	18	theme	proteins	226:233	arg1	serine					154:159	serine	154:159	serine	154:159	O-GlcNAcylation, the addition of a single N-acetylglucosamine residue to serine and threonine residues of cytoplasmic, nuclear, or mitochondrial proteins, is a widespread regulatory posttranslational modification.
32938750	0	19	theme	Modification	61:72	arg1	Sites					74:78	N-Acetylglucosamine Modification Sites	41:78	N-Acetylglucosamine Modification Sites	41:78	Methods for Enrichment and Assignment of N-Acetylglucosamine Modification Sites.
32938750	3	20	theme	mass	655:658	arg1	spectrometry					660:671	mass spectrometry	655:671	mass spectrometry	655:671	Although the modification was first detected over 35 years ago, research into the function of O-GlcNAcylation has accelerated dramatically in the last 10 years owing to the development of new enrichment and mass spectrometry techniques that facilitate its analysis.
32938750	1	21	theme	single	116:121	arg1	residue					143:149	a single N-acetylglucosamine residue	114:149	a single N-acetylglucosamine residue	114:149	O-GlcNAcylation, the addition of a single N-acetylglucosamine residue to serine and threonine residues of cytoplasmic, nuclear, or mitochondrial proteins, is a widespread regulatory posttranslational modification.
32938750	0	22	theme	N-Acetylglucosamine	41:59	arg1	Sites					74:78	N-Acetylglucosamine Modification Sites	41:78	N-Acetylglucosamine Modification Sites	41:78	Methods for Enrichment and Assignment of N-Acetylglucosamine Modification Sites.
32938750	4	23	theme	O-GlcNAc-modified	937:953	arg1	peptides					955:962	O-GlcNAc-modified peptides	937:962	O-GlcNAc-modified peptides	937:962	This article summarizes methods for O-GlcNAc enrichment, key mass spectrometry instrumentation advancements, particularly those that allow modification site localization, and software tools that allow analysis of data from O-GlcNAc-modified peptides.
32938750	1	24	theme	N-acetylglucosamine	123:141	arg1	residue					143:149	a single N-acetylglucosamine residue	114:149	a single N-acetylglucosamine residue	114:149	O-GlcNAcylation, the addition of a single N-acetylglucosamine residue to serine and threonine residues of cytoplasmic, nuclear, or mitochondrial proteins, is a widespread regulatory posttranslational modification.
32938750	3	25	theme	new	636:638	arg1	techniques					673:682	new enrichment and mass spectrometry techniques	636:682	new enrichment and mass spectrometry techniques that facilitate its analysis	636:711	Although the modification was first detected over 35 years ago, research into the function of O-GlcNAcylation has accelerated dramatically in the last 10 years owing to the development of new enrichment and mass spectrometry techniques that facilitate its analysis.
32938750	1	26	theme	residue	143:149	arg1	O-GlcNAcylation					81:95	O-GlcNAcylation	81:95	O-GlcNAcylation	81:95	O-GlcNAcylation, the addition of a single N-acetylglucosamine residue to serine and threonine residues of cytoplasmic, nuclear, or mitochondrial proteins, is a widespread regulatory posttranslational modification.
32938750	1	26	theme	residue	143:149	arg1	addition					102:109	the addition	98:109	the addition of a single N-acetylglucosamine residue to serine and threonine residues of cytoplasmic, nuclear, or mitochondrial proteins	98:233	O-GlcNAcylation, the addition of a single N-acetylglucosamine residue to serine and threonine residues of cytoplasmic, nuclear, or mitochondrial proteins, is a widespread regulatory posttranslational modification.
32938750	4	27	theme	spectrometry	780:791	arg1	advancements					809:820	key mass spectrometry instrumentation advancements	771:820	key mass spectrometry instrumentation advancements	771:820	This article summarizes methods for O-GlcNAc enrichment, key mass spectrometry instrumentation advancements, particularly those that allow modification site localization, and software tools that allow analysis of data from O-GlcNAc-modified peptides.
32938750	4	27	theme	spectrometry	780:791	arg1	those					836:840	those	836:840	those	836:840	This article summarizes methods for O-GlcNAc enrichment, key mass spectrometry instrumentation advancements, particularly those that allow modification site localization, and software tools that allow analysis of data from O-GlcNAc-modified peptides.
32938750	4	28	from	peptides	955:962	arg1	data					927:930	data	927:930	data from O-GlcNAc-modified peptides	927:962	This article summarizes methods for O-GlcNAc enrichment, key mass spectrometry instrumentation advancements, particularly those that allow modification site localization, and software tools that allow analysis of data from O-GlcNAc-modified peptides.
32938750	4	28	from	peptides	955:962	arg1	analysis					915:922	analysis	915:922	analysis of data from O-GlcNAc-modified peptides	915:962	This article summarizes methods for O-GlcNAc enrichment, key mass spectrometry instrumentation advancements, particularly those that allow modification site localization, and software tools that allow analysis of data from O-GlcNAc-modified peptides.
32938750	3	29	theme	enrichment	640:649	arg1	techniques					673:682	new enrichment and mass spectrometry techniques	636:682	new enrichment and mass spectrometry techniques that facilitate its analysis	636:711	Although the modification was first detected over 35 years ago, research into the function of O-GlcNAcylation has accelerated dramatically in the last 10 years owing to the development of new enrichment and mass spectrometry techniques that facilitate its analysis.
32938750	4	30	theme	O-GlcNAc	750:757	arg1	enrichment					759:768	O-GlcNAc enrichment	750:768	O-GlcNAc enrichment	750:768	This article summarizes methods for O-GlcNAc enrichment, key mass spectrometry instrumentation advancements, particularly those that allow modification site localization, and software tools that allow analysis of data from O-GlcNAc-modified peptides.
32938750	4	31	theme	modification	853:864	arg1	localization					871:882	modification site localization	853:882	modification site localization	853:882	This article summarizes methods for O-GlcNAc enrichment, key mass spectrometry instrumentation advancements, particularly those that allow modification site localization, and software tools that allow analysis of data from O-GlcNAc-modified peptides.
32938750	0	32	theme	Sites	74:78	arg1	Enrichment					12:21	Enrichment	12:21	Enrichment	12:21	Methods for Enrichment and Assignment of N-Acetylglucosamine Modification Sites.
32938750	0	32	theme	Sites	74:78	arg1	Assignment					27:36	Assignment	27:36	Assignment	27:36	Methods for Enrichment and Assignment of N-Acetylglucosamine Modification Sites.
32938750	1	33	theme	widespread	241:250	arg1	O-GlcNAcylation					81:95	O-GlcNAcylation	81:95	O-GlcNAcylation	81:95	O-GlcNAcylation, the addition of a single N-acetylglucosamine residue to serine and threonine residues of cytoplasmic, nuclear, or mitochondrial proteins, is a widespread regulatory posttranslational modification.
32938750	1	33	theme	widespread	241:250	arg1	modification					281:292	a widespread regulatory posttranslational modification	239:292	a widespread regulatory posttranslational modification	239:292	O-GlcNAcylation, the addition of a single N-acetylglucosamine residue to serine and threonine residues of cytoplasmic, nuclear, or mitochondrial proteins, is a widespread regulatory posttranslational modification.
31373491	5	0	theme	conserved	686:694	arg1	residues					706:713	conserved aspartate residues	686:713	conserved aspartate residues in the tetratricopeptide repeat (TPR) lumen of OGT	686:764	Here we use protein microarray technology and proteome-wide glycosylation profiling to show that conserved aspartate residues in the tetratricopeptide repeat (TPR) lumen of OGT drive substrate selection.
31373491	7	1	theme	substrate	1040:1048	arg1	residues					1078:1085	substrate side chains five to fifteen residues C-terminal	1040:1096	substrate side chains five to fifteen residues C-terminal	1040:1096	Our findings support a model where sites of glycosylation for many OGT substrates are determined by TPR domain contacts to substrate side chains five to fifteen residues C-terminal to the glycosite.
31373491	0	2	theme	Substrate	71:79	arg1	Selection					81:89	O-GlcNAc Transferase Substrate Selection	50:89	O-GlcNAc Transferase Substrate Selection	50:89	Aspartate Residues Far from the Active Site Drive O-GlcNAc Transferase Substrate Selection.
31373491	1	3	located	found	148:152	arg1	proteins					181:188	nuclear and cytoplasmic proteins	157:188	nuclear and cytoplasmic proteins in all metazoans	157:205	O-GlcNAc is an abundant post-translational modification found on nuclear and cytoplasmic proteins in all metazoans.
31373491	1	3	located	found	148:152	arg2	O-GlcNAc					92:99	O-GlcNAc	92:99	O-GlcNAc	92:99	O-GlcNAc is an abundant post-translational modification found on nuclear and cytoplasmic proteins in all metazoans.
31373491	1	3	located	found	148:152	arg2	modification					135:146	an abundant post-translational modification	104:146	an abundant post-translational modification found on nuclear and cytoplasmic proteins in all metazoans	104:205	O-GlcNAc is an abundant post-translational modification found on nuclear and cytoplasmic proteins in all metazoans.
31373491	5	4	theme	aspartate	696:704	arg1	residues					706:713	conserved aspartate residues	686:713	conserved aspartate residues in the tetratricopeptide repeat (TPR) lumen of OGT	686:764	Here we use protein microarray technology and proteome-wide glycosylation profiling to show that conserved aspartate residues in the tetratricopeptide repeat (TPR) lumen of OGT drive substrate selection.
31373491	7	5	theme	domain	1021:1026	arg1	contacts					1028:1035	TPR domain contacts	1017:1035	TPR domain contacts to substrate side chains five to fifteen residues C-terminal to the glycosite	1017:1113	Our findings support a model where sites of glycosylation for many OGT substrates are determined by TPR domain contacts to substrate side chains five to fifteen residues C-terminal to the glycosite.
31373491	1	6	theme	cytoplasmic	169:179	arg1	proteins					181:188	nuclear and cytoplasmic proteins	157:188	nuclear and cytoplasmic proteins in all metazoans	157:205	O-GlcNAc is an abundant post-translational modification found on nuclear and cytoplasmic proteins in all metazoans.
31373491	5	7	theme	OGT	762:764	arg1	lumen					753:757	the tetratricopeptide repeat (TPR) lumen	718:757	the tetratricopeptide repeat (TPR) lumen of OGT	718:764	Here we use protein microarray technology and proteome-wide glycosylation profiling to show that conserved aspartate residues in the tetratricopeptide repeat (TPR) lumen of OGT drive substrate selection.
31373491	3	8	theme	O-GlcNAc	374:381	arg1	OGT					396:398	OGT	396:398	OGT	396:398	A single essential enzyme, O-GlcNAc transferase (OGT), is responsible for all nucleocytoplasmic O-GlcNAcylation.
31373491	3	8	theme	O-GlcNAc	374:381	arg1	enzyme					366:371	A single essential enzyme	347:371	A single essential enzyme	347:371	A single essential enzyme, O-GlcNAc transferase (OGT), is responsible for all nucleocytoplasmic O-GlcNAcylation.
31373491	3	8	theme	O-GlcNAc	374:381	arg1	transferase					383:393	O-GlcNAc transferase	374:393	O-GlcNAc transferase (OGT)	374:399	A single essential enzyme, O-GlcNAc transferase (OGT), is responsible for all nucleocytoplasmic O-GlcNAcylation.
31373491	5	9	theme	proteome-wide	635:647	arg1	profiling					663:671	proteome-wide glycosylation profiling	635:671	proteome-wide glycosylation profiling	635:671	Here we use protein microarray technology and proteome-wide glycosylation profiling to show that conserved aspartate residues in the tetratricopeptide repeat (TPR) lumen of OGT drive substrate selection.
31373491	4	10	dep	Understanding	460:472	arg1	chooses					490:496	chooses	490:496	chooses its substrates	490:511	Understanding how this enzyme chooses its substrates is critical for understanding, and potentially manipulating, its functions.
31373491	3	11	theme	essential	356:364	arg1	enzyme					366:371	A single essential enzyme	347:371	A single essential enzyme	347:371	A single essential enzyme, O-GlcNAc transferase (OGT), is responsible for all nucleocytoplasmic O-GlcNAcylation.
31373491	3	11	theme	essential	356:364	arg1	transferase					383:393	O-GlcNAc transferase	374:393	O-GlcNAc transferase (OGT)	374:399	A single essential enzyme, O-GlcNAc transferase (OGT), is responsible for all nucleocytoplasmic O-GlcNAcylation.
31373491	3	11	theme	essential	356:364	arg1	responsible					405:415	responsible	405:415	responsible	405:415	A single essential enzyme, O-GlcNAc transferase (OGT), is responsible for all nucleocytoplasmic O-GlcNAcylation.
31373491	7	12	gly	glycosite	1105:1113	arg2	glycosite					1105:1113	the glycosite	1101:1113	the glycosite	1101:1113	Our findings support a model where sites of glycosylation for many OGT substrates are determined by TPR domain contacts to substrate side chains five to fifteen residues C-terminal to the glycosite.
31373491	5	13	theme	glycosylation	649:661	arg1	profiling					663:671	proteome-wide glycosylation profiling	635:671	proteome-wide glycosylation profiling	635:671	Here we use protein microarray technology and proteome-wide glycosylation profiling to show that conserved aspartate residues in the tetratricopeptide repeat (TPR) lumen of OGT drive substrate selection.
31373491	2	14	theme	O-GlcNAc	287:294	arg1	levels					296:301	elevated O-GlcNAc levels	278:301	elevated O-GlcNAc levels	278:301	This modification regulates a wide variety of cellular processes, and elevated O-GlcNAc levels have been implicated in cancer progression.
31373491	8	15	theme	biological	1261:1270	arg1	functions					1272:1280	biological functions	1261:1280	biological functions	1261:1280	In addition to guiding design of inhibitors that target OGT's TPR domain, this information will inform efforts to engineer substrates to explore biological functions.
31373491	6	16	theme	substrate	836:844	arg1	selectivity					846:856	substrate selectivity	836:856	substrate selectivity	836:856	Changing these residues to alanines alters substrate selectivity and unexpectedly increases rates of protein glycosylation.
31373491	2	17	theme	elevated	278:285	arg1	levels					296:301	elevated O-GlcNAc levels	278:301	elevated O-GlcNAc levels	278:301	This modification regulates a wide variety of cellular processes, and elevated O-GlcNAc levels have been implicated in cancer progression.
31373491	5	18	theme	substrate	772:780	arg1	selection					782:790	substrate selection	772:790	substrate selection	772:790	Here we use protein microarray technology and proteome-wide glycosylation profiling to show that conserved aspartate residues in the tetratricopeptide repeat (TPR) lumen of OGT drive substrate selection.
31373491	2	19	theme	cancer	327:332	arg1	progression					334:344	cancer progression	327:344	cancer progression	327:344	This modification regulates a wide variety of cellular processes, and elevated O-GlcNAc levels have been implicated in cancer progression.
31373491	7	20	dep	residues	1078:1085	arg1	to					1067:1068	to	1067:1068	to	1067:1068	Our findings support a model where sites of glycosylation for many OGT substrates are determined by TPR domain contacts to substrate side chains five to fifteen residues C-terminal to the glycosite.
31373491	0	21	theme	Aspartate	0:8	arg1	Residues					10:17	Aspartate Residues	0:17	Aspartate Residues Far from the Active Site	0:42	Aspartate Residues Far from the Active Site Drive O-GlcNAc Transferase Substrate Selection.
31373491	5	22	theme	protein	601:607	arg1	technology					620:629	protein microarray technology	601:629	protein microarray technology	601:629	Here we use protein microarray technology and proteome-wide glycosylation profiling to show that conserved aspartate residues in the tetratricopeptide repeat (TPR) lumen of OGT drive substrate selection.
31373491	3	23	theme	nucleocytoplasmic	425:441	arg1	O-GlcNAcylation					443:457	all nucleocytoplasmic O-GlcNAcylation	421:457	all nucleocytoplasmic O-GlcNAcylation	421:457	A single essential enzyme, O-GlcNAc transferase (OGT), is responsible for all nucleocytoplasmic O-GlcNAcylation.
31373491	7	24	theme	OGT	984:986	arg1	substrates					988:997	many OGT substrates	979:997	many OGT substrates	979:997	Our findings support a model where sites of glycosylation for many OGT substrates are determined by TPR domain contacts to substrate side chains five to fifteen residues C-terminal to the glycosite.
31373491	5	25	theme	microarray	609:618	arg1	technology					620:629	protein microarray technology	601:629	protein microarray technology	601:629	Here we use protein microarray technology and proteome-wide glycosylation profiling to show that conserved aspartate residues in the tetratricopeptide repeat (TPR) lumen of OGT drive substrate selection.
31373491	7	26	theme	TPR	1017:1019	arg1	contacts					1028:1035	TPR domain contacts	1017:1035	TPR domain contacts to substrate side chains five to fifteen residues C-terminal to the glycosite	1017:1113	Our findings support a model where sites of glycosylation for many OGT substrates are determined by TPR domain contacts to substrate side chains five to fifteen residues C-terminal to the glycosite.
31373491	0	27	theme	Active	32:37	arg1	Site					39:42	the Active Site	28:42	the Active Site	28:42	Aspartate Residues Far from the Active Site Drive O-GlcNAc Transferase Substrate Selection.
31373491	8	28	theme	inhibitors	1149:1158	arg1	design					1139:1144	design	1139:1144	design of inhibitors that target OGT's TPR domain	1139:1187	In addition to guiding design of inhibitors that target OGT's TPR domain, this information will inform efforts to engineer substrates to explore biological functions.
31373491	5	29	from	residues	706:713	arg1	lumen					753:757	the tetratricopeptide repeat (TPR) lumen	718:757	the tetratricopeptide repeat (TPR) lumen of OGT	718:764	Here we use protein microarray technology and proteome-wide glycosylation profiling to show that conserved aspartate residues in the tetratricopeptide repeat (TPR) lumen of OGT drive substrate selection.
31373491	3	30	theme	single	349:354	arg1	enzyme					366:371	A single essential enzyme	347:371	A single essential enzyme	347:371	A single essential enzyme, O-GlcNAc transferase (OGT), is responsible for all nucleocytoplasmic O-GlcNAcylation.
31373491	3	30	theme	single	349:354	arg1	transferase					383:393	O-GlcNAc transferase	374:393	O-GlcNAc transferase (OGT)	374:399	A single essential enzyme, O-GlcNAc transferase (OGT), is responsible for all nucleocytoplasmic O-GlcNAcylation.
31373491	3	30	theme	single	349:354	arg1	responsible					405:415	responsible	405:415	responsible	405:415	A single essential enzyme, O-GlcNAc transferase (OGT), is responsible for all nucleocytoplasmic O-GlcNAcylation.
31373491	2	31	theme	wide	238:241	arg1	variety					243:249	a wide variety	236:249	a wide variety of cellular processes	236:271	This modification regulates a wide variety of cellular processes, and elevated O-GlcNAc levels have been implicated in cancer progression.
31373491	2	31	theme	wide	238:241	arg1	processes					263:271	cellular processes	254:271	cellular processes	254:271	This modification regulates a wide variety of cellular processes, and elevated O-GlcNAc levels have been implicated in cancer progression.
31373491	7	32	theme	C-terminal	1087:1096	arg1	residues					1078:1085	substrate side chains five to fifteen residues C-terminal	1040:1096	substrate side chains five to fifteen residues C-terminal	1040:1096	Our findings support a model where sites of glycosylation for many OGT substrates are determined by TPR domain contacts to substrate side chains five to fifteen residues C-terminal to the glycosite.
31373491	1	33	theme	abundant	107:114	arg1	modification					135:146	an abundant post-translational modification	104:146	an abundant post-translational modification found on nuclear and cytoplasmic proteins in all metazoans	104:205	O-GlcNAc is an abundant post-translational modification found on nuclear and cytoplasmic proteins in all metazoans.
31373491	1	33	theme	abundant	107:114	arg1	O-GlcNAc					92:99	O-GlcNAc	92:99	O-GlcNAc	92:99	O-GlcNAc is an abundant post-translational modification found on nuclear and cytoplasmic proteins in all metazoans.
31373491	8	34	dep	guiding	1131:1137	arg1	addition					1119:1126	addition	1119:1126	addition	1119:1126	In addition to guiding design of inhibitors that target OGT's TPR domain, this information will inform efforts to engineer substrates to explore biological functions.
31373491	5	35	theme	tetratricopeptide	722:738	arg1	repeat					740:745	tetratricopeptide repeat	722:745	the tetratricopeptide repeat (TPR) lumen of OGT	718:764	Here we use protein microarray technology and proteome-wide glycosylation profiling to show that conserved aspartate residues in the tetratricopeptide repeat (TPR) lumen of OGT drive substrate selection.
31373491	5	35	theme	tetratricopeptide	722:738	arg1	TPR					748:750	TPR	748:750	TPR	748:750	Here we use protein microarray technology and proteome-wide glycosylation profiling to show that conserved aspartate residues in the tetratricopeptide repeat (TPR) lumen of OGT drive substrate selection.
31373491	6	36	theme	glycosylation	902:914	arg1	rates					885:889	rates	885:889	rates of protein glycosylation	885:914	Changing these residues to alanines alters substrate selectivity and unexpectedly increases rates of protein glycosylation.
31373491	1	37	theme	post-translational	116:133	arg1	modification					135:146	an abundant post-translational modification	104:146	an abundant post-translational modification found on nuclear and cytoplasmic proteins in all metazoans	104:205	O-GlcNAc is an abundant post-translational modification found on nuclear and cytoplasmic proteins in all metazoans.
31373491	1	37	theme	post-translational	116:133	arg1	O-GlcNAc					92:99	O-GlcNAc	92:99	O-GlcNAc	92:99	O-GlcNAc is an abundant post-translational modification found on nuclear and cytoplasmic proteins in all metazoans.
31373491	5	38	theme	repeat	740:745	arg1	lumen					753:757	the tetratricopeptide repeat (TPR) lumen	718:757	the tetratricopeptide repeat (TPR) lumen of OGT	718:764	Here we use protein microarray technology and proteome-wide glycosylation profiling to show that conserved aspartate residues in the tetratricopeptide repeat (TPR) lumen of OGT drive substrate selection.
31373491	6	39	theme	protein	894:900	arg1	glycosylation					902:914	protein glycosylation	894:914	protein glycosylation	894:914	Changing these residues to alanines alters substrate selectivity and unexpectedly increases rates of protein glycosylation.
31373491	7	40	theme	many	979:982	arg1	substrates					988:997	many OGT substrates	979:997	many OGT substrates	979:997	Our findings support a model where sites of glycosylation for many OGT substrates are determined by TPR domain contacts to substrate side chains five to fifteen residues C-terminal to the glycosite.
31373491	7	41	gly	glycosylation	961:973	arg2	glycosylation					961:973	glycosylation	961:973	glycosylation	961:973	Our findings support a model where sites of glycosylation for many OGT substrates are determined by TPR domain contacts to substrate side chains five to fifteen residues C-terminal to the glycosite.
31373491	7	41	gly	glycosylation	961:973	arg2	sites					952:956	sites	952:956	sites of glycosylation for many OGT substrates	952:997	Our findings support a model where sites of glycosylation for many OGT substrates are determined by TPR domain contacts to substrate side chains five to fifteen residues C-terminal to the glycosite.
31373491	7	42	theme	side	1050:1053	arg1	residues					1078:1085	substrate side chains five to fifteen residues C-terminal	1040:1096	substrate side chains five to fifteen residues C-terminal	1040:1096	Our findings support a model where sites of glycosylation for many OGT substrates are determined by TPR domain contacts to substrate side chains five to fifteen residues C-terminal to the glycosite.
31373491	8	43	theme	TPR	1178:1180	arg1	domain					1182:1187	OGT's TPR domain	1172:1187	OGT's TPR domain	1172:1187	In addition to guiding design of inhibitors that target OGT's TPR domain, this information will inform efforts to engineer substrates to explore biological functions.
31373491	0	44	theme	Transferase	59:69	arg1	Selection					81:89	O-GlcNAc Transferase Substrate Selection	50:89	O-GlcNAc Transferase Substrate Selection	50:89	Aspartate Residues Far from the Active Site Drive O-GlcNAc Transferase Substrate Selection.
31373491	2	45	theme	processes	263:271	arg1	variety					243:249	a wide variety	236:249	a wide variety of cellular processes	236:271	This modification regulates a wide variety of cellular processes, and elevated O-GlcNAc levels have been implicated in cancer progression.
31373491	2	45	theme	processes	263:271	arg1	processes					263:271	cellular processes	254:271	cellular processes	254:271	This modification regulates a wide variety of cellular processes, and elevated O-GlcNAc levels have been implicated in cancer progression.
31373491	7	46	theme	chains	1055:1060	arg1	residues					1078:1085	substrate side chains five to fifteen residues C-terminal	1040:1096	substrate side chains five to fifteen residues C-terminal	1040:1096	Our findings support a model where sites of glycosylation for many OGT substrates are determined by TPR domain contacts to substrate side chains five to fifteen residues C-terminal to the glycosite.
31373491	7	47	theme	glycosylation	961:973	arg1	glycosylation					961:973	glycosylation	961:973	glycosylation	961:973	Our findings support a model where sites of glycosylation for many OGT substrates are determined by TPR domain contacts to substrate side chains five to fifteen residues C-terminal to the glycosite.
31373491	7	47	theme	glycosylation	961:973	arg1	sites					952:956	sites	952:956	sites of glycosylation for many OGT substrates	952:997	Our findings support a model where sites of glycosylation for many OGT substrates are determined by TPR domain contacts to substrate side chains five to fifteen residues C-terminal to the glycosite.
31373491	0	48	theme	O-GlcNAc	50:57	arg1	Transferase					59:69	O-GlcNAc Transferase	50:69	O-GlcNAc Transferase Substrate Selection	50:89	Aspartate Residues Far from the Active Site Drive O-GlcNAc Transferase Substrate Selection.
31373491	2	49	theme	cellular	254:261	arg1	processes					263:271	cellular processes	254:271	cellular processes	254:271	This modification regulates a wide variety of cellular processes, and elevated O-GlcNAc levels have been implicated in cancer progression.
31373491	1	50	from	proteins	181:188	arg1	metazoans					197:205	all metazoans	193:205	all metazoans	193:205	O-GlcNAc is an abundant post-translational modification found on nuclear and cytoplasmic proteins in all metazoans.
31373491	1	51	theme	nuclear	157:163	arg1	proteins					181:188	nuclear and cytoplasmic proteins	157:188	nuclear and cytoplasmic proteins in all metazoans	157:205	O-GlcNAc is an abundant post-translational modification found on nuclear and cytoplasmic proteins in all metazoans.
31492838	0	0	theme	embryonic	108:116	arg1	cells					123:127	mouse embryonic stem cells	102:127	mouse embryonic stem cells	102:127	Next-generation unnatural monosaccharides reveal that ESRRB O-GlcNAcylation regulates pluripotency of mouse embryonic stem cells.
31492838	7	1	theme	transcription	1232:1244	arg1	activity					1246:1253	its transcription activity	1228:1253	its transcription activity	1228:1253	Mechanistically, ESRRB is O-GlcNAcylated by O-GlcNAc transferase at serine 25, which stabilizes ESRRB, promotes its transcription activity and facilitates its interactions with two master pluripotency regulators, OCT4 and NANOG.
31492838	1	2	theme	glycan	276:281	arg1	imaging					283:289	glycan imaging	276:289	glycan imaging	276:289	Unnatural monosaccharides such as azidosugars that can be metabolically incorporated into cellular glycans are currently used as a major tool for glycan imaging and glycoproteomic profiling.
31492838	0	3	theme	mouse	102:106	arg1	cells					123:127	mouse embryonic stem cells	102:127	mouse embryonic stem cells	102:127	Next-generation unnatural monosaccharides reveal that ESRRB O-GlcNAcylation regulates pluripotency of mouse embryonic stem cells.
31492838	5	4	theme	embryonic	899:907	arg1	cells					914:918	mouse embryonic stem cells	893:918	mouse embryonic stem cells (mESCs)	893:926	Applying 1,3-Pr2GalNAz in mouse embryonic stem cells (mESCs), we identify ESRRB, a critical transcription factor for pluripotency, as an O-GlcNAcylated protein.
31492838	5	4	theme	embryonic	899:907	arg1	mESCs					921:925	mESCs	921:925	mESCs	921:925	Applying 1,3-Pr2GalNAz in mouse embryonic stem cells (mESCs), we identify ESRRB, a critical transcription factor for pluripotency, as an O-GlcNAcylated protein.
31492838	7	5	from	serine	1184:1189	arg1	transferase					1169:1179	O-GlcNAc transferase	1160:1179	O-GlcNAc transferase	1160:1179	Mechanistically, ESRRB is O-GlcNAcylated by O-GlcNAc transferase at serine 25, which stabilizes ESRRB, promotes its transcription activity and facilitates its interactions with two master pluripotency regulators, OCT4 and NANOG.
31492838	0	6	theme	cells	123:127	arg1	pluripotency					86:97	pluripotency	86:97	pluripotency of mouse embryonic stem cells	86:127	Next-generation unnatural monosaccharides reveal that ESRRB O-GlcNAcylation regulates pluripotency of mouse embryonic stem cells.
31492838	2	7	theme	common	326:331	arg1	practice					333:340	a common practice	324:340	a common practice to enhance membrane permeability and cellular uptake	324:393	As a common practice to enhance membrane permeability and cellular uptake, the unnatural sugars are per-O-acetylated, which, however, can induce a long-overlooked side reaction, non-enzymatic S-glycosylation.
31492838	0	8	theme	stem	118:121	arg1	cells					123:127	mouse embryonic stem cells	102:127	mouse embryonic stem cells	102:127	Next-generation unnatural monosaccharides reveal that ESRRB O-GlcNAcylation regulates pluripotency of mouse embryonic stem cells.
31492838	1	9	theme	glycoproteomic	295:308	arg1	profiling					310:318	glycoproteomic profiling	295:318	glycoproteomic profiling	295:318	Unnatural monosaccharides such as azidosugars that can be metabolically incorporated into cellular glycans are currently used as a major tool for glycan imaging and glycoproteomic profiling.
31492838	4	10	theme	protein	807:813	arg1	O-GlcNAcylation					815:829	protein O-GlcNAcylation	807:829	protein O-GlcNAcylation	807:829	Both 1,3-di-O-acetylated GalNAz (1,3-Ac2GalNAz) and 1,3-di-O-propionylated GalNAz (1,3-Pr2GalNAz) exhibit high efficiency for labeling protein O-GlcNAcylation with no artificial S-glycosylation.
31492838	5	11	theme	critical	950:957	arg1	factor					973:978	a critical transcription factor	948:978	a critical transcription factor for pluripotency	948:995	Applying 1,3-Pr2GalNAz in mouse embryonic stem cells (mESCs), we identify ESRRB, a critical transcription factor for pluripotency, as an O-GlcNAcylated protein.
31492838	5	11	theme	critical	950:957	arg1	ESRRB					941:945	ESRRB	941:945	ESRRB	941:945	Applying 1,3-Pr2GalNAz in mouse embryonic stem cells (mESCs), we identify ESRRB, a critical transcription factor for pluripotency, as an O-GlcNAcylated protein.
31492838	2	12	theme	non-enzymatic	499:511	arg1	reaction					489:496	a long-overlooked side reaction	466:496	a long-overlooked side reaction	466:496	As a common practice to enhance membrane permeability and cellular uptake, the unnatural sugars are per-O-acetylated, which, however, can induce a long-overlooked side reaction, non-enzymatic S-glycosylation.
31492838	2	12	theme	non-enzymatic	499:511	arg1	S-glycosylation					513:527	non-enzymatic S-glycosylation	499:527	non-enzymatic S-glycosylation	499:527	As a common practice to enhance membrane permeability and cellular uptake, the unnatural sugars are per-O-acetylated, which, however, can induce a long-overlooked side reaction, non-enzymatic S-glycosylation.
31492838	7	13	theme	pluripotency	1304:1315	arg1	OCT4					1329:1332	OCT4	1329:1332	OCT4	1329:1332	Mechanistically, ESRRB is O-GlcNAcylated by O-GlcNAc transferase at serine 25, which stabilizes ESRRB, promotes its transcription activity and facilitates its interactions with two master pluripotency regulators, OCT4 and NANOG.
31492838	7	13	theme	pluripotency	1304:1315	arg1	regulators					1317:1326	two master pluripotency regulators	1293:1326	two master pluripotency regulators	1293:1326	Mechanistically, ESRRB is O-GlcNAcylated by O-GlcNAc transferase at serine 25, which stabilizes ESRRB, promotes its transcription activity and facilitates its interactions with two master pluripotency regulators, OCT4 and NANOG.
31492838	7	13	theme	pluripotency	1304:1315	arg1	NANOG					1338:1342	NANOG	1338:1342	NANOG	1338:1342	Mechanistically, ESRRB is O-GlcNAcylated by O-GlcNAc transferase at serine 25, which stabilizes ESRRB, promotes its transcription activity and facilitates its interactions with two master pluripotency regulators, OCT4 and NANOG.
31492838	5	14	theme	transcription	959:971	arg1	factor					973:978	a critical transcription factor	948:978	a critical transcription factor for pluripotency	948:995	Applying 1,3-Pr2GalNAz in mouse embryonic stem cells (mESCs), we identify ESRRB, a critical transcription factor for pluripotency, as an O-GlcNAcylated protein.
31492838	5	14	theme	transcription	959:971	arg1	ESRRB					941:945	ESRRB	941:945	ESRRB	941:945	Applying 1,3-Pr2GalNAz in mouse embryonic stem cells (mESCs), we identify ESRRB, a critical transcription factor for pluripotency, as an O-GlcNAcylated protein.
31492838	0	15	theme	unnatural	16:24	arg1	monosaccharides					26:40	Next-generation unnatural monosaccharides	0:40	Next-generation unnatural monosaccharides	0:40	Next-generation unnatural monosaccharides reveal that ESRRB O-GlcNAcylation regulates pluripotency of mouse embryonic stem cells.
31492838	5	16	theme	mouse	893:897	arg1	cells					914:918	mouse embryonic stem cells	893:918	mouse embryonic stem cells (mESCs)	893:926	Applying 1,3-Pr2GalNAz in mouse embryonic stem cells (mESCs), we identify ESRRB, a critical transcription factor for pluripotency, as an O-GlcNAcylated protein.
31492838	5	16	theme	mouse	893:897	arg1	mESCs					921:925	mESCs	921:925	mESCs	921:925	Applying 1,3-Pr2GalNAz in mouse embryonic stem cells (mESCs), we identify ESRRB, a critical transcription factor for pluripotency, as an O-GlcNAcylated protein.
31492838	4	17	theme	artificial	839:848	arg1	S-glycosylation					850:864	no artificial S-glycosylation	836:864	no artificial S-glycosylation	836:864	Both 1,3-di-O-acetylated GalNAz (1,3-Ac2GalNAz) and 1,3-di-O-propionylated GalNAz (1,3-Pr2GalNAz) exhibit high efficiency for labeling protein O-GlcNAcylation with no artificial S-glycosylation.
31492838	7	18	theme	master	1297:1302	arg1	OCT4					1329:1332	OCT4	1329:1332	OCT4	1329:1332	Mechanistically, ESRRB is O-GlcNAcylated by O-GlcNAc transferase at serine 25, which stabilizes ESRRB, promotes its transcription activity and facilitates its interactions with two master pluripotency regulators, OCT4 and NANOG.
31492838	7	18	theme	master	1297:1302	arg1	regulators					1317:1326	two master pluripotency regulators	1293:1326	two master pluripotency regulators	1293:1326	Mechanistically, ESRRB is O-GlcNAcylated by O-GlcNAc transferase at serine 25, which stabilizes ESRRB, promotes its transcription activity and facilitates its interactions with two master pluripotency regulators, OCT4 and NANOG.
31492838	7	18	theme	master	1297:1302	arg1	NANOG					1338:1342	NANOG	1338:1342	NANOG	1338:1342	Mechanistically, ESRRB is O-GlcNAcylated by O-GlcNAc transferase at serine 25, which stabilizes ESRRB, promotes its transcription activity and facilitates its interactions with two master pluripotency regulators, OCT4 and NANOG.
31492838	1	19	theme	cellular	220:227	arg1	glycans					229:235	cellular glycans	220:235	cellular glycans	220:235	Unnatural monosaccharides such as azidosugars that can be metabolically incorporated into cellular glycans are currently used as a major tool for glycan imaging and glycoproteomic profiling.
31492838	0	20	theme	Next-generation	0:14	arg1	monosaccharides					26:40	Next-generation unnatural monosaccharides	0:40	Next-generation unnatural monosaccharides	0:40	Next-generation unnatural monosaccharides reveal that ESRRB O-GlcNAcylation regulates pluripotency of mouse embryonic stem cells.
31492838	3	21	theme	chemical	622:629	arg1	reporters					631:639	next-generation chemical reporters	606:639	next-generation chemical reporters for metabolic glycan labeling	606:669	Herein, we develop 1,3-di-esterified N-azidoacetylgalactosamine (GalNAz) as next-generation chemical reporters for metabolic glycan labeling.
31492838	3	21	theme	chemical	622:629	arg1	N-azidoacetylgalactosamine					567:592	1,3-di-esterified N-azidoacetylgalactosamine	549:592	1,3-di-esterified N-azidoacetylgalactosamine (GalNAz)	549:601	Herein, we develop 1,3-di-esterified N-azidoacetylgalactosamine (GalNAz) as next-generation chemical reporters for metabolic glycan labeling.
31492838	3	22	theme	next-generation	606:620	arg1	reporters					631:639	next-generation chemical reporters	606:639	next-generation chemical reporters for metabolic glycan labeling	606:669	Herein, we develop 1,3-di-esterified N-azidoacetylgalactosamine (GalNAz) as next-generation chemical reporters for metabolic glycan labeling.
31492838	3	22	theme	next-generation	606:620	arg1	N-azidoacetylgalactosamine					567:592	1,3-di-esterified N-azidoacetylgalactosamine	549:592	1,3-di-esterified N-azidoacetylgalactosamine (GalNAz)	549:601	Herein, we develop 1,3-di-esterified N-azidoacetylgalactosamine (GalNAz) as next-generation chemical reporters for metabolic glycan labeling.
31492838	1	23	theme	Unnatural	130:138	arg1	tool					267:270	a major tool	259:270	a major tool for glycan imaging and glycoproteomic profiling	259:318	Unnatural monosaccharides such as azidosugars that can be metabolically incorporated into cellular glycans are currently used as a major tool for glycan imaging and glycoproteomic profiling.
31492838	1	23	theme	Unnatural	130:138	arg1	monosaccharides					140:154	Unnatural monosaccharides	130:154	Unnatural monosaccharides such as azidosugars that can be metabolically incorporated into cellular glycans	130:235	Unnatural monosaccharides such as azidosugars that can be metabolically incorporated into cellular glycans are currently used as a major tool for glycan imaging and glycoproteomic profiling.
31492838	1	23	theme	Unnatural	130:138	arg1	azidosugars					164:174	azidosugars	164:174	azidosugars that can be metabolically incorporated into cellular glycans	164:235	Unnatural monosaccharides such as azidosugars that can be metabolically incorporated into cellular glycans are currently used as a major tool for glycan imaging and glycoproteomic profiling.
31492838	3	24	theme	1,3-di-esterified	549:565	arg1	reporters					631:639	next-generation chemical reporters	606:639	next-generation chemical reporters for metabolic glycan labeling	606:669	Herein, we develop 1,3-di-esterified N-azidoacetylgalactosamine (GalNAz) as next-generation chemical reporters for metabolic glycan labeling.
31492838	3	24	theme	1,3-di-esterified	549:565	arg1	GalNAz					595:600	GalNAz	595:600	GalNAz	595:600	Herein, we develop 1,3-di-esterified N-azidoacetylgalactosamine (GalNAz) as next-generation chemical reporters for metabolic glycan labeling.
31492838	3	24	theme	1,3-di-esterified	549:565	arg1	N-azidoacetylgalactosamine					567:592	1,3-di-esterified N-azidoacetylgalactosamine	549:592	1,3-di-esterified N-azidoacetylgalactosamine (GalNAz)	549:601	Herein, we develop 1,3-di-esterified N-azidoacetylgalactosamine (GalNAz) as next-generation chemical reporters for metabolic glycan labeling.
31492838	0	25	theme	ESRRB	54:58	arg1	O-GlcNAcylation					60:74	ESRRB O-GlcNAcylation	54:74	ESRRB O-GlcNAcylation	54:74	Next-generation unnatural monosaccharides reveal that ESRRB O-GlcNAcylation regulates pluripotency of mouse embryonic stem cells.
31492838	4	26	theme	1,3-di-O-propionylated	724:745	arg1	1,3-Pr2GalNAz					755:767	1,3-Pr2GalNAz	755:767	1,3-Pr2GalNAz	755:767	Both 1,3-di-O-acetylated GalNAz (1,3-Ac2GalNAz) and 1,3-di-O-propionylated GalNAz (1,3-Pr2GalNAz) exhibit high efficiency for labeling protein O-GlcNAcylation with no artificial S-glycosylation.
31492838	4	26	theme	1,3-di-O-propionylated	724:745	arg1	GalNAz					747:752	1,3-di-O-propionylated GalNAz	724:752	1,3-di-O-propionylated GalNAz (1,3-Pr2GalNAz)	724:768	Both 1,3-di-O-acetylated GalNAz (1,3-Ac2GalNAz) and 1,3-di-O-propionylated GalNAz (1,3-Pr2GalNAz) exhibit high efficiency for labeling protein O-GlcNAcylation with no artificial S-glycosylation.
31492838	4	27	theme	high	778:781	arg1	efficiency					783:792	high efficiency	778:792	high efficiency for labeling protein O-GlcNAcylation with no artificial S-glycosylation	778:864	Both 1,3-di-O-acetylated GalNAz (1,3-Ac2GalNAz) and 1,3-di-O-propionylated GalNAz (1,3-Pr2GalNAz) exhibit high efficiency for labeling protein O-GlcNAcylation with no artificial S-glycosylation.
31492838	5	28	theme	stem	909:912	arg1	cells					914:918	mouse embryonic stem cells	893:918	mouse embryonic stem cells (mESCs)	893:926	Applying 1,3-Pr2GalNAz in mouse embryonic stem cells (mESCs), we identify ESRRB, a critical transcription factor for pluripotency, as an O-GlcNAcylated protein.
31492838	5	28	theme	stem	909:912	arg1	mESCs					921:925	mESCs	921:925	mESCs	921:925	Applying 1,3-Pr2GalNAz in mouse embryonic stem cells (mESCs), we identify ESRRB, a critical transcription factor for pluripotency, as an O-GlcNAcylated protein.
31492838	1	29	used	used	251:254	arg2	monosaccharides					140:154	Unnatural monosaccharides	130:154	Unnatural monosaccharides such as azidosugars that can be metabolically incorporated into cellular glycans	130:235	Unnatural monosaccharides such as azidosugars that can be metabolically incorporated into cellular glycans are currently used as a major tool for glycan imaging and glycoproteomic profiling.
31492838	1	29	used	used	251:254	arg2	azidosugars					164:174	azidosugars	164:174	azidosugars that can be metabolically incorporated into cellular glycans	164:235	Unnatural monosaccharides such as azidosugars that can be metabolically incorporated into cellular glycans are currently used as a major tool for glycan imaging and glycoproteomic profiling.
31492838	1	29	used	used	251:254	arg2	tool					267:270	a major tool	259:270	a major tool for glycan imaging and glycoproteomic profiling	259:318	Unnatural monosaccharides such as azidosugars that can be metabolically incorporated into cellular glycans are currently used as a major tool for glycan imaging and glycoproteomic profiling.
31492838	6	30	theme	ESRRB	1041:1045	arg1	O-GlcNAcylation					1047:1061	ESRRB O-GlcNAcylation	1041:1061	ESRRB O-GlcNAcylation	1041:1061	We show that ESRRB O-GlcNAcylation is important for mESC self-renewal and pluripotency.
31492838	7	31	theme	O-GlcNAc	1160:1167	arg1	transferase					1169:1179	O-GlcNAc transferase	1160:1179	O-GlcNAc transferase	1160:1179	Mechanistically, ESRRB is O-GlcNAcylated by O-GlcNAc transferase at serine 25, which stabilizes ESRRB, promotes its transcription activity and facilitates its interactions with two master pluripotency regulators, OCT4 and NANOG.
31492838	3	32	theme	metabolic	645:653	arg1	labeling					662:669	metabolic glycan labeling	645:669	metabolic glycan labeling	645:669	Herein, we develop 1,3-di-esterified N-azidoacetylgalactosamine (GalNAz) as next-generation chemical reporters for metabolic glycan labeling.
31492838	2	33	theme	cellular	379:386	arg1	uptake					388:393	cellular uptake	379:393	cellular uptake	379:393	As a common practice to enhance membrane permeability and cellular uptake, the unnatural sugars are per-O-acetylated, which, however, can induce a long-overlooked side reaction, non-enzymatic S-glycosylation.
31492838	2	34	theme	side	484:487	arg1	reaction					489:496	a long-overlooked side reaction	466:496	a long-overlooked side reaction	466:496	As a common practice to enhance membrane permeability and cellular uptake, the unnatural sugars are per-O-acetylated, which, however, can induce a long-overlooked side reaction, non-enzymatic S-glycosylation.
31492838	2	34	theme	side	484:487	arg1	S-glycosylation					513:527	non-enzymatic S-glycosylation	499:527	non-enzymatic S-glycosylation	499:527	As a common practice to enhance membrane permeability and cellular uptake, the unnatural sugars are per-O-acetylated, which, however, can induce a long-overlooked side reaction, non-enzymatic S-glycosylation.
31492838	3	35	theme	glycan	655:660	arg1	labeling					662:669	metabolic glycan labeling	645:669	metabolic glycan labeling	645:669	Herein, we develop 1,3-di-esterified N-azidoacetylgalactosamine (GalNAz) as next-generation chemical reporters for metabolic glycan labeling.
31492838	4	36	theme	1,3-di-O-acetylated	677:695	arg1	1,3-Ac2GalNAz					705:717	1,3-Ac2GalNAz	705:717	1,3-Ac2GalNAz	705:717	Both 1,3-di-O-acetylated GalNAz (1,3-Ac2GalNAz) and 1,3-di-O-propionylated GalNAz (1,3-Pr2GalNAz) exhibit high efficiency for labeling protein O-GlcNAcylation with no artificial S-glycosylation.
31492838	4	36	theme	1,3-di-O-acetylated	677:695	arg1	GalNAz					697:702	1,3-di-O-acetylated GalNAz	677:702	1,3-di-O-acetylated GalNAz (1,3-Ac2GalNAz)	677:718	Both 1,3-di-O-acetylated GalNAz (1,3-Ac2GalNAz) and 1,3-di-O-propionylated GalNAz (1,3-Pr2GalNAz) exhibit high efficiency for labeling protein O-GlcNAcylation with no artificial S-glycosylation.
31492838	7	37	with	interactions	1275:1286	arg1	OCT4					1329:1332	OCT4	1329:1332	OCT4	1329:1332	Mechanistically, ESRRB is O-GlcNAcylated by O-GlcNAc transferase at serine 25, which stabilizes ESRRB, promotes its transcription activity and facilitates its interactions with two master pluripotency regulators, OCT4 and NANOG.
31492838	7	37	with	interactions	1275:1286	arg1	regulators					1317:1326	two master pluripotency regulators	1293:1326	two master pluripotency regulators	1293:1326	Mechanistically, ESRRB is O-GlcNAcylated by O-GlcNAc transferase at serine 25, which stabilizes ESRRB, promotes its transcription activity and facilitates its interactions with two master pluripotency regulators, OCT4 and NANOG.
31492838	7	37	with	interactions	1275:1286	arg1	NANOG					1338:1342	NANOG	1338:1342	NANOG	1338:1342	Mechanistically, ESRRB is O-GlcNAcylated by O-GlcNAc transferase at serine 25, which stabilizes ESRRB, promotes its transcription activity and facilitates its interactions with two master pluripotency regulators, OCT4 and NANOG.
31492838	5	38	theme	O-GlcNAcylated	1004:1017	arg1	protein					1019:1025	an O-GlcNAcylated protein	1001:1025	an O-GlcNAcylated protein	1001:1025	Applying 1,3-Pr2GalNAz in mouse embryonic stem cells (mESCs), we identify ESRRB, a critical transcription factor for pluripotency, as an O-GlcNAcylated protein.
31492838	5	38	theme	O-GlcNAcylated	1004:1017	arg1	ESRRB					941:945	ESRRB	941:945	ESRRB	941:945	Applying 1,3-Pr2GalNAz in mouse embryonic stem cells (mESCs), we identify ESRRB, a critical transcription factor for pluripotency, as an O-GlcNAcylated protein.
31492838	2	39	theme	membrane	353:360	arg1	permeability					362:373	membrane permeability	353:373	membrane permeability	353:373	As a common practice to enhance membrane permeability and cellular uptake, the unnatural sugars are per-O-acetylated, which, however, can induce a long-overlooked side reaction, non-enzymatic S-glycosylation.
31492838	1	40	theme	major	261:265	arg1	tool					267:270	a major tool	259:270	a major tool for glycan imaging and glycoproteomic profiling	259:318	Unnatural monosaccharides such as azidosugars that can be metabolically incorporated into cellular glycans are currently used as a major tool for glycan imaging and glycoproteomic profiling.
31492838	1	40	theme	major	261:265	arg1	monosaccharides					140:154	Unnatural monosaccharides	130:154	Unnatural monosaccharides such as azidosugars that can be metabolically incorporated into cellular glycans	130:235	Unnatural monosaccharides such as azidosugars that can be metabolically incorporated into cellular glycans are currently used as a major tool for glycan imaging and glycoproteomic profiling.
31492838	1	40	theme	major	261:265	arg1	azidosugars					164:174	azidosugars	164:174	azidosugars that can be metabolically incorporated into cellular glycans	164:235	Unnatural monosaccharides such as azidosugars that can be metabolically incorporated into cellular glycans are currently used as a major tool for glycan imaging and glycoproteomic profiling.
31492838	5	41	from	1,3-Pr2GalNAz	876:888	arg1	cells					914:918	mouse embryonic stem cells	893:918	mouse embryonic stem cells (mESCs)	893:926	Applying 1,3-Pr2GalNAz in mouse embryonic stem cells (mESCs), we identify ESRRB, a critical transcription factor for pluripotency, as an O-GlcNAcylated protein.
31492838	5	41	from	1,3-Pr2GalNAz	876:888	arg1	mESCs					921:925	mESCs	921:925	mESCs	921:925	Applying 1,3-Pr2GalNAz in mouse embryonic stem cells (mESCs), we identify ESRRB, a critical transcription factor for pluripotency, as an O-GlcNAcylated protein.
31492838	2	42	theme	unnatural	400:408	arg1	per-O-acetylated					421:436	per-O-acetylated	421:436	per-O-acetylated	421:436	As a common practice to enhance membrane permeability and cellular uptake, the unnatural sugars are per-O-acetylated, which, however, can induce a long-overlooked side reaction, non-enzymatic S-glycosylation.
31492838	2	42	theme	unnatural	400:408	arg1	sugars					410:415	the unnatural sugars	396:415	the unnatural sugars	396:415	As a common practice to enhance membrane permeability and cellular uptake, the unnatural sugars are per-O-acetylated, which, however, can induce a long-overlooked side reaction, non-enzymatic S-glycosylation.
31492838	2	43	theme	long-overlooked	468:482	arg1	reaction					489:496	a long-overlooked side reaction	466:496	a long-overlooked side reaction	466:496	As a common practice to enhance membrane permeability and cellular uptake, the unnatural sugars are per-O-acetylated, which, however, can induce a long-overlooked side reaction, non-enzymatic S-glycosylation.
31492838	2	43	theme	long-overlooked	468:482	arg1	S-glycosylation					513:527	non-enzymatic S-glycosylation	499:527	non-enzymatic S-glycosylation	499:527	As a common practice to enhance membrane permeability and cellular uptake, the unnatural sugars are per-O-acetylated, which, however, can induce a long-overlooked side reaction, non-enzymatic S-glycosylation.
32574038	8	0	theme	galactosyltransferase	1256:1276	arg1	promiscuity					1237:1247	the promiscuity	1233:1247	the promiscuity of the galactosyltransferase	1233:1276	Moreover, because of the promiscuity of the galactosyltransferase, 18 unique O-glucosylated peptides were identified on the EGF domain from nine proteins.
32574038	9	1	theme	current	1470:1476	arg1	method					1478:1483	the current method	1466:1483	the current method without any sample restrictions	1466:1515	Considering that effective and approachable methods are critical to advance glycoscience research, the current method without any sample restrictions can be widely applied for global analysis of protein O-GlcNAcylation in different samples.
32574038	1	2	theme	protein	170:176	arg1	O-GlcNAcylation					98:112	O-GlcNAcylation	98:112	O-GlcNAcylation	98:112	O-GlcNAcylation has gradually been recognized as a critically important protein post-translational modification in mammalian cells.
32574038	1	2	theme	protein	170:176	arg1	modification					197:208	a critically important protein post-translational modification	147:208	a critically important protein post-translational modification in mammalian cells	147:227	O-GlcNAcylation has gradually been recognized as a critically important protein post-translational modification in mammalian cells.
32574038	0	3	theme	Protein	73:79	arg1	O-GlcNAcylation					81:95	Profiling Protein O-GlcNAcylation	63:95	Profiling Protein O-GlcNAcylation	63:95	A Chemoenzymatic Method Based on Easily Accessible Enzymes for Profiling Protein O-GlcNAcylation.
32574038	4	4	theme	chemoenzymatic	565:578	arg1	method					580:585	a novel chemoenzymatic method	557:585	a novel chemoenzymatic method based on a wild-type galactosyltransferase and uridine diphosphate galactose (UDP-Gal) for global and site-specific analysis of protein O-GlcNAcylation	557:737	Here, we developed a novel chemoenzymatic method based on a wild-type galactosyltransferase and uridine diphosphate galactose (UDP-Gal) for global and site-specific analysis of protein O-GlcNAcylation.
32574038	1	5	theme	post-translational	178:195	arg1	O-GlcNAcylation					98:112	O-GlcNAcylation	98:112	O-GlcNAcylation	98:112	O-GlcNAcylation has gradually been recognized as a critically important protein post-translational modification in mammalian cells.
32574038	1	5	theme	post-translational	178:195	arg1	modification					197:208	a critically important protein post-translational modification	147:208	a critically important protein post-translational modification in mammalian cells	147:227	O-GlcNAcylation has gradually been recognized as a critically important protein post-translational modification in mammalian cells.
32574038	7	6	theme	triplicate	984:993	arg1	experiments					995:1005	Biological triplicate experiments	973:1005	Biological triplicate experiments	973:1005	Biological triplicate experiments were performed to validate the effectiveness and the reproducibility of this method, and the results are comparable with the previous chemoenzymatic method using the engineered enzyme and click chemistry.
32574038	4	7	theme	diphosphate	642:652	arg1	UDP-Gal					665:671	UDP-Gal	665:671	UDP-Gal	665:671	Here, we developed a novel chemoenzymatic method based on a wild-type galactosyltransferase and uridine diphosphate galactose (UDP-Gal) for global and site-specific analysis of protein O-GlcNAcylation.
32574038	4	7	theme	diphosphate	642:652	arg1	galactose					654:662	uridine diphosphate galactose	634:662	uridine diphosphate galactose (UDP-Gal)	634:672	Here, we developed a novel chemoenzymatic method based on a wild-type galactosyltransferase and uridine diphosphate galactose (UDP-Gal) for global and site-specific analysis of protein O-GlcNAcylation.
32574038	5	8	theme	O-GlcNAcylated	817:830	arg1	peptides					832:839	O-GlcNAcylated peptides	817:839	O-GlcNAcylated peptides	817:839	This method integrates enzymatic reactions and hydrazide chemistry to enrich O-GlcNAcylated peptides.
32574038	4	9	theme	novel	559:563	arg1	method					580:585	a novel chemoenzymatic method	557:585	a novel chemoenzymatic method based on a wild-type galactosyltransferase and uridine diphosphate galactose (UDP-Gal) for global and site-specific analysis of protein O-GlcNAcylation	557:737	Here, we developed a novel chemoenzymatic method based on a wild-type galactosyltransferase and uridine diphosphate galactose (UDP-Gal) for global and site-specific analysis of protein O-GlcNAcylation.
32574038	2	10	theme	cell	325:328	arg1	signaling					330:338	cell signaling	325:338	cell signaling	325:338	Besides regulation of gene expression, its crosstalk with protein phosphorylation is vital for cell signaling.
32574038	9	11	from	samples	1599:1605	arg1	analysis					1550:1557	global analysis	1543:1557	global analysis of protein O-GlcNAcylation in different samples	1543:1605	Considering that effective and approachable methods are critical to advance glycoscience research, the current method without any sample restrictions can be widely applied for global analysis of protein O-GlcNAcylation in different samples.
32574038	9	12	theme	glycoscience	1443:1454	arg1	research					1456:1463	glycoscience research	1443:1463	glycoscience research	1443:1463	Considering that effective and approachable methods are critical to advance glycoscience research, the current method without any sample restrictions can be widely applied for global analysis of protein O-GlcNAcylation in different samples.
32574038	8	13	theme	unique	1282:1287	arg1	peptides					1304:1311	18 unique O-glucosylated peptides	1279:1311	18 unique O-glucosylated peptides	1279:1311	Moreover, because of the promiscuity of the galactosyltransferase, 18 unique O-glucosylated peptides were identified on the EGF domain from nine proteins.
32574038	8	14	from	proteins	1357:1364	arg1	domain					1340:1345	the EGF domain	1332:1345	the EGF domain from nine proteins	1332:1364	Moreover, because of the promiscuity of the galactosyltransferase, 18 unique O-glucosylated peptides were identified on the EGF domain from nine proteins.
32574038	4	15	theme	site-specific	689:701	arg1	analysis					703:710	global and site-specific analysis	678:710	global and site-specific analysis of protein O-GlcNAcylation	678:737	Here, we developed a novel chemoenzymatic method based on a wild-type galactosyltransferase and uridine diphosphate galactose (UDP-Gal) for global and site-specific analysis of protein O-GlcNAcylation.
32574038	7	16	dep	effectiveness	1038:1050	arg1	the					1034:1036	the	1034:1036	the	1034:1036	Biological triplicate experiments were performed to validate the effectiveness and the reproducibility of this method, and the results are comparable with the previous chemoenzymatic method using the engineered enzyme and click chemistry.
32574038	1	17	theme	mammalian	213:221	arg1	cells					223:227	mammalian cells	213:227	mammalian cells	213:227	O-GlcNAcylation has gradually been recognized as a critically important protein post-translational modification in mammalian cells.
32574038	9	18	theme	different	1589:1597	arg1	samples					1599:1605	different samples	1589:1605	different samples	1589:1605	Considering that effective and approachable methods are critical to advance glycoscience research, the current method without any sample restrictions can be widely applied for global analysis of protein O-GlcNAcylation in different samples.
32574038	3	19	theme	O-GlcNAcylation	391:405	arg1	analysis					379:386	comprehensive analysis	365:386	comprehensive analysis of O-GlcNAcylation	365:405	Despite its importance, comprehensive analysis of O-GlcNAcylation is extraordinarily challenging due to the low abundances of many O-GlcNAcylated proteins and the complexity of biological samples.
32574038	4	20	theme	O-GlcNAcylation	723:737	arg1	analysis					703:710	global and site-specific analysis	678:710	global and site-specific analysis of protein O-GlcNAcylation	678:737	Here, we developed a novel chemoenzymatic method based on a wild-type galactosyltransferase and uridine diphosphate galactose (UDP-Gal) for global and site-specific analysis of protein O-GlcNAcylation.
32574038	0	21	theme	Chemoenzymatic	2:15	arg1	Method					17:22	A Chemoenzymatic Method	0:22	A Chemoenzymatic Method	0:22	A Chemoenzymatic Method Based on Easily Accessible Enzymes for Profiling Protein O-GlcNAcylation.
32574038	9	22	theme	sample	1497:1502	arg1	restrictions					1504:1515	any sample restrictions	1493:1515	any sample restrictions	1493:1515	Considering that effective and approachable methods are critical to advance glycoscience research, the current method without any sample restrictions can be widely applied for global analysis of protein O-GlcNAcylation in different samples.
32574038	0	23	theme	Profiling	63:71	arg1	O-GlcNAcylation					81:95	Profiling Protein O-GlcNAcylation	63:95	Profiling Protein O-GlcNAcylation	63:95	A Chemoenzymatic Method Based on Easily Accessible Enzymes for Profiling Protein O-GlcNAcylation.
32574038	7	24	theme	engineered	1173:1182	arg1	chemistry					1201:1209	the engineered enzyme and click chemistry	1169:1209	the engineered enzyme and click chemistry	1169:1209	Biological triplicate experiments were performed to validate the effectiveness and the reproducibility of this method, and the results are comparable with the previous chemoenzymatic method using the engineered enzyme and click chemistry.
32574038	3	25	theme	O-GlcNAcylated	472:485	arg1	proteins					487:494	many O-GlcNAcylated proteins	467:494	many O-GlcNAcylated proteins	467:494	Despite its importance, comprehensive analysis of O-GlcNAcylation is extraordinarily challenging due to the low abundances of many O-GlcNAcylated proteins and the complexity of biological samples.
32574038	7	26	theme	click	1195:1199	arg1	chemistry					1201:1209	the engineered enzyme and click chemistry	1169:1209	the engineered enzyme and click chemistry	1169:1209	Biological triplicate experiments were performed to validate the effectiveness and the reproducibility of this method, and the results are comparable with the previous chemoenzymatic method using the engineered enzyme and click chemistry.
32574038	3	27	theme	proteins	487:494	arg1	abundances					453:462	the low abundances	445:462	the low abundances of many O-GlcNAcylated proteins	445:494	Despite its importance, comprehensive analysis of O-GlcNAcylation is extraordinarily challenging due to the low abundances of many O-GlcNAcylated proteins and the complexity of biological samples.
32574038	3	27	theme	proteins	487:494	arg1	complexity					504:513	the complexity	500:513	the complexity of biological samples	500:535	Despite its importance, comprehensive analysis of O-GlcNAcylation is extraordinarily challenging due to the low abundances of many O-GlcNAcylated proteins and the complexity of biological samples.
32574038	8	28	theme	EGF	1336:1338	arg1	domain					1340:1345	the EGF domain	1332:1345	the EGF domain from nine proteins	1332:1364	Moreover, because of the promiscuity of the galactosyltransferase, 18 unique O-glucosylated peptides were identified on the EGF domain from nine proteins.
32574038	4	29	theme	wild-type	598:606	arg1	galactosyltransferase					608:628	a wild-type galactosyltransferase	596:628	a wild-type galactosyltransferase	596:628	Here, we developed a novel chemoenzymatic method based on a wild-type galactosyltransferase and uridine diphosphate galactose (UDP-Gal) for global and site-specific analysis of protein O-GlcNAcylation.
32574038	5	30	theme	hydrazide	787:795	arg1	chemistry					797:805	hydrazide chemistry	787:805	hydrazide chemistry	787:805	This method integrates enzymatic reactions and hydrazide chemistry to enrich O-GlcNAcylated peptides.
32574038	7	31	theme	method	1084:1089	arg1	reproducibility					1060:1074	the reproducibility	1056:1074	the reproducibility	1056:1074	Biological triplicate experiments were performed to validate the effectiveness and the reproducibility of this method, and the results are comparable with the previous chemoenzymatic method using the engineered enzyme and click chemistry.
32574038	7	31	theme	method	1084:1089	arg1	effectiveness					1038:1050	effectiveness	1038:1050	effectiveness	1038:1050	Biological triplicate experiments were performed to validate the effectiveness and the reproducibility of this method, and the results are comparable with the previous chemoenzymatic method using the engineered enzyme and click chemistry.
32574038	9	32	from	analysis	1550:1557	arg1	samples					1599:1605	different samples	1589:1605	different samples	1589:1605	Considering that effective and approachable methods are critical to advance glycoscience research, the current method without any sample restrictions can be widely applied for global analysis of protein O-GlcNAcylation in different samples.
32574038	3	33	theme	biological	518:527	arg1	samples					529:535	biological samples	518:535	biological samples	518:535	Despite its importance, comprehensive analysis of O-GlcNAcylation is extraordinarily challenging due to the low abundances of many O-GlcNAcylated proteins and the complexity of biological samples.
32574038	4	34	theme	uridine	634:640	arg1	UDP-Gal					665:671	UDP-Gal	665:671	UDP-Gal	665:671	Here, we developed a novel chemoenzymatic method based on a wild-type galactosyltransferase and uridine diphosphate galactose (UDP-Gal) for global and site-specific analysis of protein O-GlcNAcylation.
32574038	4	34	theme	uridine	634:640	arg1	galactose					654:662	uridine diphosphate galactose	634:662	uridine diphosphate galactose (UDP-Gal)	634:672	Here, we developed a novel chemoenzymatic method based on a wild-type galactosyltransferase and uridine diphosphate galactose (UDP-Gal) for global and site-specific analysis of protein O-GlcNAcylation.
32574038	9	35	theme	effective	1384:1392	arg1	methods					1411:1417	effective and approachable methods	1384:1417	effective and approachable methods	1384:1417	Considering that effective and approachable methods are critical to advance glycoscience research, the current method without any sample restrictions can be widely applied for global analysis of protein O-GlcNAcylation in different samples.
32574038	3	36	theme	samples	529:535	arg1	abundances					453:462	the low abundances	445:462	the low abundances of many O-GlcNAcylated proteins	445:494	Despite its importance, comprehensive analysis of O-GlcNAcylation is extraordinarily challenging due to the low abundances of many O-GlcNAcylated proteins and the complexity of biological samples.
32574038	3	36	theme	samples	529:535	arg1	complexity					504:513	the complexity	500:513	the complexity of biological samples	500:535	Despite its importance, comprehensive analysis of O-GlcNAcylation is extraordinarily challenging due to the low abundances of many O-GlcNAcylated proteins and the complexity of biological samples.
32574038	7	37	theme	Biological	973:982	arg1	experiments					995:1005	Biological triplicate experiments	973:1005	Biological triplicate experiments	973:1005	Biological triplicate experiments were performed to validate the effectiveness and the reproducibility of this method, and the results are comparable with the previous chemoenzymatic method using the engineered enzyme and click chemistry.
32574038	7	38	theme	enzyme	1184:1189	arg1	chemistry					1201:1209	the engineered enzyme and click chemistry	1169:1209	the engineered enzyme and click chemistry	1169:1209	Biological triplicate experiments were performed to validate the effectiveness and the reproducibility of this method, and the results are comparable with the previous chemoenzymatic method using the engineered enzyme and click chemistry.
32574038	4	39	theme	protein	715:721	arg1	O-GlcNAcylation					723:737	protein O-GlcNAcylation	715:737	protein O-GlcNAcylation	715:737	Here, we developed a novel chemoenzymatic method based on a wild-type galactosyltransferase and uridine diphosphate galactose (UDP-Gal) for global and site-specific analysis of protein O-GlcNAcylation.
32574038	3	40	theme	many	467:470	arg1	proteins					487:494	many O-GlcNAcylated proteins	467:494	many O-GlcNAcylated proteins	467:494	Despite its importance, comprehensive analysis of O-GlcNAcylation is extraordinarily challenging due to the low abundances of many O-GlcNAcylated proteins and the complexity of biological samples.
32574038	9	41	theme	protein	1562:1568	arg1	O-GlcNAcylation					1570:1584	protein O-GlcNAcylation	1562:1584	protein O-GlcNAcylation in different samples	1562:1605	Considering that effective and approachable methods are critical to advance glycoscience research, the current method without any sample restrictions can be widely applied for global analysis of protein O-GlcNAcylation in different samples.
32574038	7	42	theme	previous	1132:1139	arg1	method					1156:1161	the previous chemoenzymatic method	1128:1161	the previous chemoenzymatic method using the engineered enzyme and click chemistry	1128:1209	Biological triplicate experiments were performed to validate the effectiveness and the reproducibility of this method, and the results are comparable with the previous chemoenzymatic method using the engineered enzyme and click chemistry.
32574038	3	43	theme	low	449:451	arg1	abundances					453:462	the low abundances	445:462	the low abundances of many O-GlcNAcylated proteins	445:494	Despite its importance, comprehensive analysis of O-GlcNAcylation is extraordinarily challenging due to the low abundances of many O-GlcNAcylated proteins and the complexity of biological samples.
32574038	2	44	with	crosstalk	273:281	arg1	phosphorylation					296:310	protein phosphorylation	288:310	protein phosphorylation	288:310	Besides regulation of gene expression, its crosstalk with protein phosphorylation is vital for cell signaling.
32574038	6	45	theme	chemistry	953:961	arg1	reagents					963:970	click chemistry reagents	947:970	click chemistry reagents	947:970	All reagents used are more easily accessible and cost-effective as compared to the engineered enzyme and click chemistry reagents.
32574038	2	46	theme	expression	257:266	arg1	regulation					238:247	regulation	238:247	regulation of gene expression	238:266	Besides regulation of gene expression, its crosstalk with protein phosphorylation is vital for cell signaling.
32574038	7	47	theme	chemoenzymatic	1141:1154	arg1	method					1156:1161	the previous chemoenzymatic method	1128:1161	the previous chemoenzymatic method using the engineered enzyme and click chemistry	1128:1209	Biological triplicate experiments were performed to validate the effectiveness and the reproducibility of this method, and the results are comparable with the previous chemoenzymatic method using the engineered enzyme and click chemistry.
32574038	0	48	theme	Accessible	40:49	arg1	Enzymes					51:57	Easily Accessible Enzymes	33:57	Easily Accessible Enzymes for Profiling Protein O-GlcNAcylation	33:95	A Chemoenzymatic Method Based on Easily Accessible Enzymes for Profiling Protein O-GlcNAcylation.
32574038	5	49	theme	enzymatic	763:771	arg1	reactions					773:781	enzymatic reactions	763:781	enzymatic reactions	763:781	This method integrates enzymatic reactions and hydrazide chemistry to enrich O-GlcNAcylated peptides.
32574038	6	50	theme	click	947:951	arg1	reagents					963:970	click chemistry reagents	947:970	click chemistry reagents	947:970	All reagents used are more easily accessible and cost-effective as compared to the engineered enzyme and click chemistry reagents.
32574038	2	51	theme	gene	252:255	arg1	expression					257:266	gene expression	252:266	gene expression	252:266	Besides regulation of gene expression, its crosstalk with protein phosphorylation is vital for cell signaling.
32574038	9	52	theme	approachable	1398:1409	arg1	methods					1411:1417	effective and approachable methods	1384:1417	effective and approachable methods	1384:1417	Considering that effective and approachable methods are critical to advance glycoscience research, the current method without any sample restrictions can be widely applied for global analysis of protein O-GlcNAcylation in different samples.
32574038	8	53	theme	O-glucosylated	1289:1302	arg1	peptides					1304:1311	18 unique O-glucosylated peptides	1279:1311	18 unique O-glucosylated peptides	1279:1311	Moreover, because of the promiscuity of the galactosyltransferase, 18 unique O-glucosylated peptides were identified on the EGF domain from nine proteins.
32574038	2	54	theme	protein	288:294	arg1	phosphorylation					296:310	protein phosphorylation	288:310	protein phosphorylation	288:310	Besides regulation of gene expression, its crosstalk with protein phosphorylation is vital for cell signaling.
32574038	3	55	theme	comprehensive	365:377	arg1	analysis					379:386	comprehensive analysis	365:386	comprehensive analysis of O-GlcNAcylation	365:405	Despite its importance, comprehensive analysis of O-GlcNAcylation is extraordinarily challenging due to the low abundances of many O-GlcNAcylated proteins and the complexity of biological samples.
32574038	6	56	theme	engineered	925:934	arg1	enzyme					936:941	the engineered enzyme	921:941	the engineered enzyme	921:941	All reagents used are more easily accessible and cost-effective as compared to the engineered enzyme and click chemistry reagents.
32574038	9	57	theme	global	1543:1548	arg1	analysis					1550:1557	global analysis	1543:1557	global analysis of protein O-GlcNAcylation in different samples	1543:1605	Considering that effective and approachable methods are critical to advance glycoscience research, the current method without any sample restrictions can be widely applied for global analysis of protein O-GlcNAcylation in different samples.
32574038	9	58	theme	O-GlcNAcylation	1570:1584	arg1	analysis					1550:1557	global analysis	1543:1557	global analysis of protein O-GlcNAcylation in different samples	1543:1605	Considering that effective and approachable methods are critical to advance glycoscience research, the current method without any sample restrictions can be widely applied for global analysis of protein O-GlcNAcylation in different samples.
32574038	7	59	with	comparable	1112:1121	arg1	method					1156:1161	the previous chemoenzymatic method	1128:1161	the previous chemoenzymatic method using the engineered enzyme and click chemistry	1128:1209	Biological triplicate experiments were performed to validate the effectiveness and the reproducibility of this method, and the results are comparable with the previous chemoenzymatic method using the engineered enzyme and click chemistry.
32574038	1	60	from	modification	197:208	arg1	cells					223:227	mammalian cells	213:227	mammalian cells	213:227	O-GlcNAcylation has gradually been recognized as a critically important protein post-translational modification in mammalian cells.
32574038	1	61	theme	important	160:168	arg1	O-GlcNAcylation					98:112	O-GlcNAcylation	98:112	O-GlcNAcylation	98:112	O-GlcNAcylation has gradually been recognized as a critically important protein post-translational modification in mammalian cells.
32574038	1	61	theme	important	160:168	arg1	modification					197:208	a critically important protein post-translational modification	147:208	a critically important protein post-translational modification in mammalian cells	147:227	O-GlcNAcylation has gradually been recognized as a critically important protein post-translational modification in mammalian cells.
32574038	9	62	from	O-GlcNAcylation	1570:1584	arg1	samples					1599:1605	different samples	1589:1605	different samples	1589:1605	Considering that effective and approachable methods are critical to advance glycoscience research, the current method without any sample restrictions can be widely applied for global analysis of protein O-GlcNAcylation in different samples.
32574038	4	63	theme	global	678:683	arg1	analysis					703:710	global and site-specific analysis	678:710	global and site-specific analysis of protein O-GlcNAcylation	678:737	Here, we developed a novel chemoenzymatic method based on a wild-type galactosyltransferase and uridine diphosphate galactose (UDP-Gal) for global and site-specific analysis of protein O-GlcNAcylation.
34846842	0	0	theme	Reversible	86:95	arg1	Chemistry					107:115	Reversible Hydrazide Chemistry	86:115	Reversible Hydrazide Chemistry	86:115	Highly Efficient Enrichment of O-GlcNAc Glycopeptides Based on Chemical Oxidation and Reversible Hydrazide Chemistry.
34846842	1	1	theme	stoichiometry	325:337	arg1	result					307:312	a result	305:312	a result of the low stoichiometry and limited enrichment efficiency	305:371	Protein O-GlcNAcylation has been implicated in a broad range of cellular processes, while the functional research is still lagging behind other post-translational modification (PTMs), as a result of the low stoichiometry and limited enrichment efficiency.
34846842	1	1	theme	stoichiometry	325:337	arg1	modification					281:292	other post-translational modification	256:292	other post-translational modification (PTMs)	256:299	Protein O-GlcNAcylation has been implicated in a broad range of cellular processes, while the functional research is still lagging behind other post-translational modification (PTMs), as a result of the low stoichiometry and limited enrichment efficiency.
34846842	4	2	gly	glycopeptides	659:671	arg2	glycopeptides					659:671	The labeled O-GlcNAc glycopeptides	638:671	The labeled O-GlcNAc glycopeptides	638:671	The labeled O-GlcNAc glycopeptides could be efficiently enriched based on the equilibrium between the hydrazine and oxime bonds.
34846842	1	3	theme	broad	167:171	arg1	range					173:177	a broad range	165:177	a broad range of cellular processes	165:199	Protein O-GlcNAcylation has been implicated in a broad range of cellular processes, while the functional research is still lagging behind other post-translational modification (PTMs), as a result of the low stoichiometry and limited enrichment efficiency.
34846842	1	4	theme	other	256:260	arg1	result					307:312	a result	305:312	a result of the low stoichiometry and limited enrichment efficiency	305:371	Protein O-GlcNAcylation has been implicated in a broad range of cellular processes, while the functional research is still lagging behind other post-translational modification (PTMs), as a result of the low stoichiometry and limited enrichment efficiency.
34846842	1	4	theme	other	256:260	arg1	PTMs					295:298	PTMs	295:298	PTMs	295:298	Protein O-GlcNAcylation has been implicated in a broad range of cellular processes, while the functional research is still lagging behind other post-translational modification (PTMs), as a result of the low stoichiometry and limited enrichment efficiency.
34846842	1	4	theme	other	256:260	arg1	modification					281:292	other post-translational modification	256:292	other post-translational modification (PTMs)	256:299	Protein O-GlcNAcylation has been implicated in a broad range of cellular processes, while the functional research is still lagging behind other post-translational modification (PTMs), as a result of the low stoichiometry and limited enrichment efficiency.
34846842	5	5	theme	glycopeptide	791:802	arg1	enrichment					804:813	the glycopeptide enrichment	787:813	the glycopeptide enrichment	787:813	Good specificity of the glycopeptide enrichment was observed from the mixtures of glycopeptide and non-glycopeptides using the CHO-GlcNAc method.
34846842	1	6	theme	post-translational	262:279	arg1	result					307:312	a result	305:312	a result of the low stoichiometry and limited enrichment efficiency	305:371	Protein O-GlcNAcylation has been implicated in a broad range of cellular processes, while the functional research is still lagging behind other post-translational modification (PTMs), as a result of the low stoichiometry and limited enrichment efficiency.
34846842	1	6	theme	post-translational	262:279	arg1	PTMs					295:298	PTMs	295:298	PTMs	295:298	Protein O-GlcNAcylation has been implicated in a broad range of cellular processes, while the functional research is still lagging behind other post-translational modification (PTMs), as a result of the low stoichiometry and limited enrichment efficiency.
34846842	1	6	theme	post-translational	262:279	arg1	modification					281:292	other post-translational modification	256:292	other post-translational modification (PTMs)	256:299	Protein O-GlcNAcylation has been implicated in a broad range of cellular processes, while the functional research is still lagging behind other post-translational modification (PTMs), as a result of the low stoichiometry and limited enrichment efficiency.
34846842	1	7	theme	limited	343:349	arg1	efficiency					362:371	limited enrichment efficiency	343:371	limited enrichment efficiency	343:371	Protein O-GlcNAcylation has been implicated in a broad range of cellular processes, while the functional research is still lagging behind other post-translational modification (PTMs), as a result of the low stoichiometry and limited enrichment efficiency.
34846842	6	8	theme	proteins	1222:1229	arg1	O-GlcNAcylation					1188:1202	O-GlcNAcylation	1188:1202	O-GlcNAcylation	1188:1202	Then, it was applied to analyze O-GlcNAcylation in the nucleus of HeLa cells, and 829 potential O-GlcNAcylation sites on 274 glycoproteins were identified, including the two readers of m6A (YTHDF1 and YTHDF3), which could provide clues for the mechanism of crosstalk between O-GlcNAcylation and other PTMs of proteins and RNA.
34846842	6	8	theme	proteins	1222:1229	arg1	PTMs					1214:1217	other PTMs	1208:1217	other PTMs	1208:1217	Then, it was applied to analyze O-GlcNAcylation in the nucleus of HeLa cells, and 829 potential O-GlcNAcylation sites on 274 glycoproteins were identified, including the two readers of m6A (YTHDF1 and YTHDF3), which could provide clues for the mechanism of crosstalk between O-GlcNAcylation and other PTMs of proteins and RNA.
34846842	6	9	theme	potential	999:1007	arg1	sites					1025:1029	829 potential O-GlcNAcylation sites	995:1029	829 potential O-GlcNAcylation sites on 274 glycoproteins	995:1050	Then, it was applied to analyze O-GlcNAcylation in the nucleus of HeLa cells, and 829 potential O-GlcNAcylation sites on 274 glycoproteins were identified, including the two readers of m6A (YTHDF1 and YTHDF3), which could provide clues for the mechanism of crosstalk between O-GlcNAcylation and other PTMs of proteins and RNA.
34846842	0	10	theme	Hydrazide	97:105	arg1	Chemistry					107:115	Reversible Hydrazide Chemistry	86:115	Reversible Hydrazide Chemistry	86:115	Highly Efficient Enrichment of O-GlcNAc Glycopeptides Based on Chemical Oxidation and Reversible Hydrazide Chemistry.
34846842	1	11	theme	enrichment	351:360	arg1	efficiency					362:371	limited enrichment efficiency	343:371	limited enrichment efficiency	343:371	Protein O-GlcNAcylation has been implicated in a broad range of cellular processes, while the functional research is still lagging behind other post-translational modification (PTMs), as a result of the low stoichiometry and limited enrichment efficiency.
34846842	6	12	theme	crosstalk	1170:1178	arg1	mechanism					1157:1165	the mechanism	1153:1165	the mechanism of crosstalk between O-GlcNAcylation and other PTMs of proteins and RNA	1153:1237	Then, it was applied to analyze O-GlcNAcylation in the nucleus of HeLa cells, and 829 potential O-GlcNAcylation sites on 274 glycoproteins were identified, including the two readers of m6A (YTHDF1 and YTHDF3), which could provide clues for the mechanism of crosstalk between O-GlcNAcylation and other PTMs of proteins and RNA.
34846842	6	13	theme	other	1208:1212	arg1	PTMs					1214:1217	other PTMs	1208:1217	other PTMs	1208:1217	Then, it was applied to analyze O-GlcNAcylation in the nucleus of HeLa cells, and 829 potential O-GlcNAcylation sites on 274 glycoproteins were identified, including the two readers of m6A (YTHDF1 and YTHDF3), which could provide clues for the mechanism of crosstalk between O-GlcNAcylation and other PTMs of proteins and RNA.
34846842	3	14	theme	Gal	549:551	arg1	moiety					553:558	a Gal moiety	547:558	a Gal moiety	547:558	In this strategy, the O-GlcNAc glycopeptides were first enzymatically labeled with a Gal moiety, followed by chemical oxidation to efficiently introduce the aldehyde groups.
34846842	5	15	gly	glycopeptide	791:802	arg2	glycopeptide					791:802	the glycopeptide enrichment	787:813	the glycopeptide enrichment	787:813	Good specificity of the glycopeptide enrichment was observed from the mixtures of glycopeptide and non-glycopeptides using the CHO-GlcNAc method.
34846842	1	16	theme	efficiency	362:371	arg1	result					307:312	a result	305:312	a result of the low stoichiometry and limited enrichment efficiency	305:371	Protein O-GlcNAcylation has been implicated in a broad range of cellular processes, while the functional research is still lagging behind other post-translational modification (PTMs), as a result of the low stoichiometry and limited enrichment efficiency.
34846842	1	16	theme	efficiency	362:371	arg1	modification					281:292	other post-translational modification	256:292	other post-translational modification (PTMs)	256:299	Protein O-GlcNAcylation has been implicated in a broad range of cellular processes, while the functional research is still lagging behind other post-translational modification (PTMs), as a result of the low stoichiometry and limited enrichment efficiency.
34846842	7	17	theme	proteomic	1292:1300	arg1	analysis					1302:1309	the proteomic analysis	1288:1309	the proteomic analysis of O-GlcNAcylation	1288:1328	Thus, this method could be a versatile tool for the proteomic analysis of O-GlcNAcylation.
34846842	6	18	theme	m6A	1098:1100	arg1	readers					1087:1093	the two readers	1079:1093	the two readers of m6A (YTHDF1 and YTHDF3), which could provide clues for the mechanism of crosstalk between O-GlcNAcylation and other PTMs of proteins and RNA	1079:1237	Then, it was applied to analyze O-GlcNAcylation in the nucleus of HeLa cells, and 829 potential O-GlcNAcylation sites on 274 glycoproteins were identified, including the two readers of m6A (YTHDF1 and YTHDF3), which could provide clues for the mechanism of crosstalk between O-GlcNAcylation and other PTMs of proteins and RNA.
34846842	6	19	theme	829	995:997	arg1	sites					1025:1029	829 potential O-GlcNAcylation sites	995:1029	829 potential O-GlcNAcylation sites on 274 glycoproteins	995:1050	Then, it was applied to analyze O-GlcNAcylation in the nucleus of HeLa cells, and 829 potential O-GlcNAcylation sites on 274 glycoproteins were identified, including the two readers of m6A (YTHDF1 and YTHDF3), which could provide clues for the mechanism of crosstalk between O-GlcNAcylation and other PTMs of proteins and RNA.
34846842	5	20	gly	glycopeptide	849:860	arg2	glycopeptide					849:860	glycopeptide	849:860	glycopeptide	849:860	Good specificity of the glycopeptide enrichment was observed from the mixtures of glycopeptide and non-glycopeptides using the CHO-GlcNAc method.
34846842	3	21	gly	glycopeptides	495:507	arg2	glycopeptides					495:507	the O-GlcNAc glycopeptides	482:507	the O-GlcNAc glycopeptides	482:507	In this strategy, the O-GlcNAc glycopeptides were first enzymatically labeled with a Gal moiety, followed by chemical oxidation to efficiently introduce the aldehyde groups.
34846842	1	22	theme	cellular	182:189	arg1	processes					191:199	cellular processes	182:199	cellular processes	182:199	Protein O-GlcNAcylation has been implicated in a broad range of cellular processes, while the functional research is still lagging behind other post-translational modification (PTMs), as a result of the low stoichiometry and limited enrichment efficiency.
34846842	0	23	theme	Efficient	7:15	arg1	Enrichment					17:26	Highly Efficient Enrichment	0:26	Highly Efficient Enrichment of O-GlcNAc Glycopeptides	0:52	Highly Efficient Enrichment of O-GlcNAc Glycopeptides Based on Chemical Oxidation and Reversible Hydrazide Chemistry.
34846842	6	24	from	sites	1025:1029	arg1	glycoproteins					1038:1050	274 glycoproteins	1034:1050	274 glycoproteins	1034:1050	Then, it was applied to analyze O-GlcNAcylation in the nucleus of HeLa cells, and 829 potential O-GlcNAcylation sites on 274 glycoproteins were identified, including the two readers of m6A (YTHDF1 and YTHDF3), which could provide clues for the mechanism of crosstalk between O-GlcNAcylation and other PTMs of proteins and RNA.
34846842	4	25	theme	oxime	754:758	arg1	bonds					760:764	the hydrazine and oxime bonds	736:764	the hydrazine and oxime bonds	736:764	The labeled O-GlcNAc glycopeptides could be efficiently enriched based on the equilibrium between the hydrazine and oxime bonds.
34846842	1	26	theme	processes	191:199	arg1	range					173:177	a broad range	165:177	a broad range of cellular processes	165:199	Protein O-GlcNAcylation has been implicated in a broad range of cellular processes, while the functional research is still lagging behind other post-translational modification (PTMs), as a result of the low stoichiometry and limited enrichment efficiency.
34846842	2	27	theme	O-GlcNAc	430:437	arg1	enrichment					452:461	O-GlcNAc glycopeptide enrichment	430:461	O-GlcNAc glycopeptide enrichment	430:461	Herein, a strategy, named CHO-GlcNAc, was developed for O-GlcNAc glycopeptide enrichment.
34846842	5	28	gly	non-glycopeptides	866:882	arg2	non-glycopeptides					866:882	non-glycopeptides	866:882	non-glycopeptides	866:882	Good specificity of the glycopeptide enrichment was observed from the mixtures of glycopeptide and non-glycopeptides using the CHO-GlcNAc method.
34846842	7	29	theme	versatile	1269:1277	arg1	tool					1279:1282	a versatile tool	1267:1282	a versatile tool for the proteomic analysis of O-GlcNAcylation	1267:1328	Thus, this method could be a versatile tool for the proteomic analysis of O-GlcNAcylation.
34846842	7	29	theme	versatile	1269:1277	arg1	method					1251:1256	this method	1246:1256	this method	1246:1256	Thus, this method could be a versatile tool for the proteomic analysis of O-GlcNAcylation.
34846842	5	30	theme	non-glycopeptides	866:882	arg1	mixtures					837:844	the mixtures	833:844	the mixtures of glycopeptide and non-glycopeptides	833:882	Good specificity of the glycopeptide enrichment was observed from the mixtures of glycopeptide and non-glycopeptides using the CHO-GlcNAc method.
34846842	6	31	dep	m6A	1098:1100	arg1	YTHDF3					1114:1119	YTHDF3	1114:1119	YTHDF3	1114:1119	Then, it was applied to analyze O-GlcNAcylation in the nucleus of HeLa cells, and 829 potential O-GlcNAcylation sites on 274 glycoproteins were identified, including the two readers of m6A (YTHDF1 and YTHDF3), which could provide clues for the mechanism of crosstalk between O-GlcNAcylation and other PTMs of proteins and RNA.
34846842	6	31	dep	m6A	1098:1100	arg1	YTHDF1					1103:1108	YTHDF1	1103:1108	YTHDF1	1103:1108	Then, it was applied to analyze O-GlcNAcylation in the nucleus of HeLa cells, and 829 potential O-GlcNAcylation sites on 274 glycoproteins were identified, including the two readers of m6A (YTHDF1 and YTHDF3), which could provide clues for the mechanism of crosstalk between O-GlcNAcylation and other PTMs of proteins and RNA.
34846842	5	32	theme	glycopeptide	849:860	arg1	mixtures					837:844	the mixtures	833:844	the mixtures of glycopeptide and non-glycopeptides	833:882	Good specificity of the glycopeptide enrichment was observed from the mixtures of glycopeptide and non-glycopeptides using the CHO-GlcNAc method.
34846842	6	33	theme	cells	984:988	arg1	nucleus					968:974	the nucleus	964:974	the nucleus of HeLa cells	964:988	Then, it was applied to analyze O-GlcNAcylation in the nucleus of HeLa cells, and 829 potential O-GlcNAcylation sites on 274 glycoproteins were identified, including the two readers of m6A (YTHDF1 and YTHDF3), which could provide clues for the mechanism of crosstalk between O-GlcNAcylation and other PTMs of proteins and RNA.
34846842	1	34	gly	O-GlcNAcylation	126:140	arg1	range					173:177	a broad range	165:177	a broad range of cellular processes	165:199	Protein O-GlcNAcylation has been implicated in a broad range of cellular processes, while the functional research is still lagging behind other post-translational modification (PTMs), as a result of the low stoichiometry and limited enrichment efficiency.
34846842	1	35	theme	Protein	118:124	arg1	O-GlcNAcylation					126:140	Protein O-GlcNAcylation	118:140	Protein O-GlcNAcylation	118:140	Protein O-GlcNAcylation has been implicated in a broad range of cellular processes, while the functional research is still lagging behind other post-translational modification (PTMs), as a result of the low stoichiometry and limited enrichment efficiency.
34846842	0	36	theme	Glycopeptides	40:52	arg1	Enrichment					17:26	Highly Efficient Enrichment	0:26	Highly Efficient Enrichment of O-GlcNAc Glycopeptides	0:52	Highly Efficient Enrichment of O-GlcNAc Glycopeptides Based on Chemical Oxidation and Reversible Hydrazide Chemistry.
34846842	6	37	theme	HeLa	979:982	arg1	cells					984:988	HeLa cells	979:988	HeLa cells	979:988	Then, it was applied to analyze O-GlcNAcylation in the nucleus of HeLa cells, and 829 potential O-GlcNAcylation sites on 274 glycoproteins were identified, including the two readers of m6A (YTHDF1 and YTHDF3), which could provide clues for the mechanism of crosstalk between O-GlcNAcylation and other PTMs of proteins and RNA.
34846842	4	38	theme	O-GlcNAc	650:657	arg1	glycopeptides					659:671	The labeled O-GlcNAc glycopeptides	638:671	The labeled O-GlcNAc glycopeptides	638:671	The labeled O-GlcNAc glycopeptides could be efficiently enriched based on the equilibrium between the hydrazine and oxime bonds.
34846842	6	39	theme	RNA	1235:1237	arg1	O-GlcNAcylation					1188:1202	O-GlcNAcylation	1188:1202	O-GlcNAcylation	1188:1202	Then, it was applied to analyze O-GlcNAcylation in the nucleus of HeLa cells, and 829 potential O-GlcNAcylation sites on 274 glycoproteins were identified, including the two readers of m6A (YTHDF1 and YTHDF3), which could provide clues for the mechanism of crosstalk between O-GlcNAcylation and other PTMs of proteins and RNA.
34846842	6	39	theme	RNA	1235:1237	arg1	PTMs					1214:1217	other PTMs	1208:1217	other PTMs	1208:1217	Then, it was applied to analyze O-GlcNAcylation in the nucleus of HeLa cells, and 829 potential O-GlcNAcylation sites on 274 glycoproteins were identified, including the two readers of m6A (YTHDF1 and YTHDF3), which could provide clues for the mechanism of crosstalk between O-GlcNAcylation and other PTMs of proteins and RNA.
34846842	1	40	theme	functional	212:221	arg1	research					223:230	the functional research	208:230	the functional research	208:230	Protein O-GlcNAcylation has been implicated in a broad range of cellular processes, while the functional research is still lagging behind other post-translational modification (PTMs), as a result of the low stoichiometry and limited enrichment efficiency.
34846842	0	41	theme	O-GlcNAc	31:38	arg1	Glycopeptides					40:52	O-GlcNAc Glycopeptides	31:52	O-GlcNAc Glycopeptides	31:52	Highly Efficient Enrichment of O-GlcNAc Glycopeptides Based on Chemical Oxidation and Reversible Hydrazide Chemistry.
34846842	5	42	theme	enrichment	804:813	arg1	specificity					772:782	Good specificity	767:782	Good specificity of the glycopeptide enrichment	767:813	Good specificity of the glycopeptide enrichment was observed from the mixtures of glycopeptide and non-glycopeptides using the CHO-GlcNAc method.
34846842	6	43	theme	O-GlcNAcylation	1009:1023	arg1	sites					1025:1029	829 potential O-GlcNAcylation sites	995:1029	829 potential O-GlcNAcylation sites on 274 glycoproteins	995:1050	Then, it was applied to analyze O-GlcNAcylation in the nucleus of HeLa cells, and 829 potential O-GlcNAcylation sites on 274 glycoproteins were identified, including the two readers of m6A (YTHDF1 and YTHDF3), which could provide clues for the mechanism of crosstalk between O-GlcNAcylation and other PTMs of proteins and RNA.
34846842	4	44	theme	labeled	642:648	arg1	glycopeptides					659:671	The labeled O-GlcNAc glycopeptides	638:671	The labeled O-GlcNAc glycopeptides	638:671	The labeled O-GlcNAc glycopeptides could be efficiently enriched based on the equilibrium between the hydrazine and oxime bonds.
34846842	3	45	theme	chemical	573:580	arg1	oxidation					582:590	chemical oxidation	573:590	chemical oxidation	573:590	In this strategy, the O-GlcNAc glycopeptides were first enzymatically labeled with a Gal moiety, followed by chemical oxidation to efficiently introduce the aldehyde groups.
34846842	7	46	theme	O-GlcNAcylation	1314:1328	arg1	analysis					1302:1309	the proteomic analysis	1288:1309	the proteomic analysis of O-GlcNAcylation	1288:1328	Thus, this method could be a versatile tool for the proteomic analysis of O-GlcNAcylation.
34846842	3	47	theme	O-GlcNAc	486:493	arg1	glycopeptides					495:507	the O-GlcNAc glycopeptides	482:507	the O-GlcNAc glycopeptides	482:507	In this strategy, the O-GlcNAc glycopeptides were first enzymatically labeled with a Gal moiety, followed by chemical oxidation to efficiently introduce the aldehyde groups.
34846842	3	48	theme	aldehyde	621:628	arg1	groups					630:635	the aldehyde groups	617:635	the aldehyde groups	617:635	In this strategy, the O-GlcNAc glycopeptides were first enzymatically labeled with a Gal moiety, followed by chemical oxidation to efficiently introduce the aldehyde groups.
34846842	4	49	theme	hydrazine	740:748	arg1	bonds					760:764	the hydrazine and oxime bonds	736:764	the hydrazine and oxime bonds	736:764	The labeled O-GlcNAc glycopeptides could be efficiently enriched based on the equilibrium between the hydrazine and oxime bonds.
34846842	2	50	gly	glycopeptide	439:450	arg2	glycopeptide					439:450	O-GlcNAc glycopeptide enrichment	430:461	O-GlcNAc glycopeptide enrichment	430:461	Herein, a strategy, named CHO-GlcNAc, was developed for O-GlcNAc glycopeptide enrichment.
34846842	6	51	gly	glycoproteins	1038:1050	arg1	glycoproteins					1038:1050	274 glycoproteins	1034:1050	274 glycoproteins	1034:1050	Then, it was applied to analyze O-GlcNAcylation in the nucleus of HeLa cells, and 829 potential O-GlcNAcylation sites on 274 glycoproteins were identified, including the two readers of m6A (YTHDF1 and YTHDF3), which could provide clues for the mechanism of crosstalk between O-GlcNAcylation and other PTMs of proteins and RNA.
34846842	5	52	theme	Good	767:770	arg1	specificity					772:782	Good specificity	767:782	Good specificity of the glycopeptide enrichment	767:813	Good specificity of the glycopeptide enrichment was observed from the mixtures of glycopeptide and non-glycopeptides using the CHO-GlcNAc method.
34846842	5	53	theme	CHO-GlcNAc	894:903	arg1	method					905:910	the CHO-GlcNAc method	890:910	the CHO-GlcNAc method	890:910	Good specificity of the glycopeptide enrichment was observed from the mixtures of glycopeptide and non-glycopeptides using the CHO-GlcNAc method.
34846842	6	54	theme	274	1034:1036	arg1	glycoproteins					1038:1050	274 glycoproteins	1034:1050	274 glycoproteins	1034:1050	Then, it was applied to analyze O-GlcNAcylation in the nucleus of HeLa cells, and 829 potential O-GlcNAcylation sites on 274 glycoproteins were identified, including the two readers of m6A (YTHDF1 and YTHDF3), which could provide clues for the mechanism of crosstalk between O-GlcNAcylation and other PTMs of proteins and RNA.
34846842	0	55	theme	Chemical	63:70	arg1	Oxidation					72:80	Chemical Oxidation	63:80	Chemical Oxidation	63:80	Highly Efficient Enrichment of O-GlcNAc Glycopeptides Based on Chemical Oxidation and Reversible Hydrazide Chemistry.
34846842	1	56	theme	low	321:323	arg1	stoichiometry					325:337	the low stoichiometry	317:337	the low stoichiometry	317:337	Protein O-GlcNAcylation has been implicated in a broad range of cellular processes, while the functional research is still lagging behind other post-translational modification (PTMs), as a result of the low stoichiometry and limited enrichment efficiency.
34846842	2	57	theme	glycopeptide	439:450	arg1	enrichment					452:461	O-GlcNAc glycopeptide enrichment	430:461	O-GlcNAc glycopeptide enrichment	430:461	Herein, a strategy, named CHO-GlcNAc, was developed for O-GlcNAc glycopeptide enrichment.
7867791	5	0	theme	bisecting	933:941	arg1	N-acetylglucosamine					943:961	bisecting N-acetylglucosamine	933:961	bisecting N-acetylglucosamine	933:961	Analysis of a second transferrin preparation containing both asialo- and sialo-transferrin revealed another major glycan species derived from the sialylated transferrin variant which is galactosylated and lacks bisecting N-acetylglucosamine and fucose.
7867791	4	1	theme	major	582:586	arg1	oligosaccharide					650:664	a complex-type agalactodiantennary oligosaccharide	615:664	a complex-type agalactodiantennary oligosaccharide with bisecting N-acetylglucosamine and proximal fucose	615:719	The major structure turned out to be a complex-type agalactodiantennary oligosaccharide with bisecting N-acetylglucosamine and proximal fucose.
7867791	4	1	theme	major	582:586	arg1	structure					588:596	The major structure	578:596	The major structure	578:596	The major structure turned out to be a complex-type agalactodiantennary oligosaccharide with bisecting N-acetylglucosamine and proximal fucose.
7867791	5	2	theme	major	830:834	arg1	species					843:849	another major glycan species	822:849	another major glycan species derived from the sialylated transferrin variant which is galactosylated and lacks bisecting N-acetylglucosamine and fucose	822:972	Analysis of a second transferrin preparation containing both asialo- and sialo-transferrin revealed another major glycan species derived from the sialylated transferrin variant which is galactosylated and lacks bisecting N-acetylglucosamine and fucose.
7867791	3	3	theme	high-pH	384:390	arg1	chromatography					407:420	high-pH anion-exchange chromatography	384:420	high-pH anion-exchange chromatography	384:420	For carbohydrate structural analysis, high-pH anion-exchange chromatography, methylation analysis, liquid secondary ion- and matrix-assisted laser desorption/ ionization mass spectrometry of the permethylated derivatives were used.
7867791	4	4	theme	proximal	705:712	arg1	fucose					714:719	proximal fucose	705:719	proximal fucose	705:719	The major structure turned out to be a complex-type agalactodiantennary oligosaccharide with bisecting N-acetylglucosamine and proximal fucose.
7867791	3	5	theme	matrix-assisted	471:485	arg1	spectrometry					521:532	matrix-assisted laser desorption/ ionization mass spectrometry	471:532	matrix-assisted laser desorption/ ionization mass spectrometry	471:532	For carbohydrate structural analysis, high-pH anion-exchange chromatography, methylation analysis, liquid secondary ion- and matrix-assisted laser desorption/ ionization mass spectrometry of the permethylated derivatives were used.
7867791	5	6	theme	second	736:741	arg1	preparation					755:765	a second transferrin preparation	734:765	a second transferrin preparation containing both asialo- and sialo-transferrin	734:811	Analysis of a second transferrin preparation containing both asialo- and sialo-transferrin revealed another major glycan species derived from the sialylated transferrin variant which is galactosylated and lacks bisecting N-acetylglucosamine and fucose.
7867791	2	7	theme	proteins	336:343	arg1	glycosylation					273:285	'brain-type' glycosylation	260:285	'brain-type' glycosylation of intrathecally synthesized cerebrospinal fluid proteins	260:343	Investigation of the structural characteristics of its oligosaccharides support our hypothesis of 'brain-type' glycosylation of intrathecally synthesized cerebrospinal fluid proteins.
7867791	5	8	theme	preparation	755:765	arg1	Analysis					722:729	Analysis	722:729	Analysis of a second transferrin preparation containing both asialo- and sialo-transferrin	722:811	Analysis of a second transferrin preparation containing both asialo- and sialo-transferrin revealed another major glycan species derived from the sialylated transferrin variant which is galactosylated and lacks bisecting N-acetylglucosamine and fucose.
7867791	5	9	theme	transferrin	743:753	arg1	preparation					755:765	a second transferrin preparation	734:765	a second transferrin preparation containing both asialo- and sialo-transferrin	734:811	Analysis of a second transferrin preparation containing both asialo- and sialo-transferrin revealed another major glycan species derived from the sialylated transferrin variant which is galactosylated and lacks bisecting N-acetylglucosamine and fucose.
7867791	2	10	theme	fluid	330:334	arg1	proteins					336:343	intrathecally synthesized cerebrospinal fluid proteins	290:343	intrathecally synthesized cerebrospinal fluid proteins	290:343	Investigation of the structural characteristics of its oligosaccharides support our hypothesis of 'brain-type' glycosylation of intrathecally synthesized cerebrospinal fluid proteins.
7867791	3	11	theme	methylation	423:433	arg1	analysis					435:442	methylation analysis	423:442	methylation analysis	423:442	For carbohydrate structural analysis, high-pH anion-exchange chromatography, methylation analysis, liquid secondary ion- and matrix-assisted laser desorption/ ionization mass spectrometry of the permethylated derivatives were used.
7867791	3	12	theme	desorption/	493:503	arg1	spectrometry					521:532	matrix-assisted laser desorption/ ionization mass spectrometry	471:532	matrix-assisted laser desorption/ ionization mass spectrometry	471:532	For carbohydrate structural analysis, high-pH anion-exchange chromatography, methylation analysis, liquid secondary ion- and matrix-assisted laser desorption/ ionization mass spectrometry of the permethylated derivatives were used.
7867791	2	13	theme	cerebrospinal	316:328	arg1	proteins					336:343	intrathecally synthesized cerebrospinal fluid proteins	290:343	intrathecally synthesized cerebrospinal fluid proteins	290:343	Investigation of the structural characteristics of its oligosaccharides support our hypothesis of 'brain-type' glycosylation of intrathecally synthesized cerebrospinal fluid proteins.
7867791	0	14	theme	Brain-type	1:10	arg1	N-glycosylation					13:27	'Brain-type' N-glycosylation	0:27	'Brain-type' N-glycosylation of asialo-transferrin from human cerebrospinal fluid	0:80	'Brain-type' N-glycosylation of asialo-transferrin from human cerebrospinal fluid.
7867791	3	15	theme	liquid	445:450	arg1	ion-					462:465	liquid secondary ion-	445:465	liquid secondary ion-	445:465	For carbohydrate structural analysis, high-pH anion-exchange chromatography, methylation analysis, liquid secondary ion- and matrix-assisted laser desorption/ ionization mass spectrometry of the permethylated derivatives were used.
7867791	4	16	with	oligosaccharide	650:664	arg1	N-acetylglucosamine					681:699	bisecting N-acetylglucosamine	671:699	bisecting N-acetylglucosamine	671:699	The major structure turned out to be a complex-type agalactodiantennary oligosaccharide with bisecting N-acetylglucosamine and proximal fucose.
7867791	4	16	with	oligosaccharide	650:664	arg1	fucose					714:719	proximal fucose	705:719	proximal fucose	705:719	The major structure turned out to be a complex-type agalactodiantennary oligosaccharide with bisecting N-acetylglucosamine and proximal fucose.
7867791	3	17	theme	mass	516:519	arg1	spectrometry					521:532	matrix-assisted laser desorption/ ionization mass spectrometry	471:532	matrix-assisted laser desorption/ ionization mass spectrometry	471:532	For carbohydrate structural analysis, high-pH anion-exchange chromatography, methylation analysis, liquid secondary ion- and matrix-assisted laser desorption/ ionization mass spectrometry of the permethylated derivatives were used.
7867791	4	18	theme	bisecting	671:679	arg1	N-acetylglucosamine					681:699	bisecting N-acetylglucosamine	671:699	bisecting N-acetylglucosamine	671:699	The major structure turned out to be a complex-type agalactodiantennary oligosaccharide with bisecting N-acetylglucosamine and proximal fucose.
7867791	1	19	theme	human	107:111	arg1	fluid					127:131	human cerebrospinal fluid	107:131	human cerebrospinal fluid	107:131	Asialo-transferrin from human cerebrospinal fluid was purified to homogeneity.
7867791	2	20	gly	glycosylation	273:285	arg1	proteins					336:343	intrathecally synthesized cerebrospinal fluid proteins	290:343	intrathecally synthesized cerebrospinal fluid proteins	290:343	Investigation of the structural characteristics of its oligosaccharides support our hypothesis of 'brain-type' glycosylation of intrathecally synthesized cerebrospinal fluid proteins.
7867791	3	21	used	used	572:575	arg2	analysis					435:442	methylation analysis	423:442	methylation analysis	423:442	For carbohydrate structural analysis, high-pH anion-exchange chromatography, methylation analysis, liquid secondary ion- and matrix-assisted laser desorption/ ionization mass spectrometry of the permethylated derivatives were used.
7867791	3	21	used	used	572:575	arg2	chromatography					407:420	high-pH anion-exchange chromatography	384:420	high-pH anion-exchange chromatography	384:420	For carbohydrate structural analysis, high-pH anion-exchange chromatography, methylation analysis, liquid secondary ion- and matrix-assisted laser desorption/ ionization mass spectrometry of the permethylated derivatives were used.
7867791	3	21	used	used	572:575	arg2	spectrometry					521:532	matrix-assisted laser desorption/ ionization mass spectrometry	471:532	matrix-assisted laser desorption/ ionization mass spectrometry	471:532	For carbohydrate structural analysis, high-pH anion-exchange chromatography, methylation analysis, liquid secondary ion- and matrix-assisted laser desorption/ ionization mass spectrometry of the permethylated derivatives were used.
7867791	3	21	used	used	572:575	arg2	ion-					462:465	liquid secondary ion-	445:465	liquid secondary ion-	445:465	For carbohydrate structural analysis, high-pH anion-exchange chromatography, methylation analysis, liquid secondary ion- and matrix-assisted laser desorption/ ionization mass spectrometry of the permethylated derivatives were used.
7867791	3	22	theme	secondary	452:460	arg1	ion-					462:465	liquid secondary ion-	445:465	liquid secondary ion-	445:465	For carbohydrate structural analysis, high-pH anion-exchange chromatography, methylation analysis, liquid secondary ion- and matrix-assisted laser desorption/ ionization mass spectrometry of the permethylated derivatives were used.
7867791	5	23	attach	derived	851:857	arg1	variant					891:897	the sialylated transferrin variant	864:897	the sialylated transferrin variant which is galactosylated and lacks bisecting N-acetylglucosamine and fucose	864:972	Analysis of a second transferrin preparation containing both asialo- and sialo-transferrin revealed another major glycan species derived from the sialylated transferrin variant which is galactosylated and lacks bisecting N-acetylglucosamine and fucose.
7867791	5	23	attach	derived	851:857	arg2	species					843:849	another major glycan species	822:849	another major glycan species derived from the sialylated transferrin variant which is galactosylated and lacks bisecting N-acetylglucosamine and fucose	822:972	Analysis of a second transferrin preparation containing both asialo- and sialo-transferrin revealed another major glycan species derived from the sialylated transferrin variant which is galactosylated and lacks bisecting N-acetylglucosamine and fucose.
7867791	0	24	theme	asialo-transferrin	32:49	arg1	N-glycosylation					13:27	'Brain-type' N-glycosylation	0:27	'Brain-type' N-glycosylation of asialo-transferrin from human cerebrospinal fluid	0:80	'Brain-type' N-glycosylation of asialo-transferrin from human cerebrospinal fluid.
7867791	5	25	theme	sialylated	868:877	arg1	variant					891:897	the sialylated transferrin variant	864:897	the sialylated transferrin variant which is galactosylated and lacks bisecting N-acetylglucosamine and fucose	864:972	Analysis of a second transferrin preparation containing both asialo- and sialo-transferrin revealed another major glycan species derived from the sialylated transferrin variant which is galactosylated and lacks bisecting N-acetylglucosamine and fucose.
7867791	1	26	theme	cerebrospinal	113:125	arg1	fluid					127:131	human cerebrospinal fluid	107:131	human cerebrospinal fluid	107:131	Asialo-transferrin from human cerebrospinal fluid was purified to homogeneity.
7867791	3	27	theme	permethylated	541:553	arg1	derivatives					555:565	the permethylated derivatives	537:565	the permethylated derivatives	537:565	For carbohydrate structural analysis, high-pH anion-exchange chromatography, methylation analysis, liquid secondary ion- and matrix-assisted laser desorption/ ionization mass spectrometry of the permethylated derivatives were used.
7867791	3	28	theme	ionization	505:514	arg1	spectrometry					521:532	matrix-assisted laser desorption/ ionization mass spectrometry	471:532	matrix-assisted laser desorption/ ionization mass spectrometry	471:532	For carbohydrate structural analysis, high-pH anion-exchange chromatography, methylation analysis, liquid secondary ion- and matrix-assisted laser desorption/ ionization mass spectrometry of the permethylated derivatives were used.
7867791	4	29	theme	complex-type	617:628	arg1	oligosaccharide					650:664	a complex-type agalactodiantennary oligosaccharide	615:664	a complex-type agalactodiantennary oligosaccharide with bisecting N-acetylglucosamine and proximal fucose	615:719	The major structure turned out to be a complex-type agalactodiantennary oligosaccharide with bisecting N-acetylglucosamine and proximal fucose.
7867791	4	29	theme	complex-type	617:628	arg1	structure					588:596	The major structure	578:596	The major structure	578:596	The major structure turned out to be a complex-type agalactodiantennary oligosaccharide with bisecting N-acetylglucosamine and proximal fucose.
7867791	5	30	theme	transferrin	879:889	arg1	variant					891:897	the sialylated transferrin variant	864:897	the sialylated transferrin variant which is galactosylated and lacks bisecting N-acetylglucosamine and fucose	864:972	Analysis of a second transferrin preparation containing both asialo- and sialo-transferrin revealed another major glycan species derived from the sialylated transferrin variant which is galactosylated and lacks bisecting N-acetylglucosamine and fucose.
7867791	2	31	theme	characteristics	194:208	arg1	Investigation					162:174	Investigation	162:174	Investigation of the structural characteristics of its oligosaccharides	162:232	Investigation of the structural characteristics of its oligosaccharides support our hypothesis of 'brain-type' glycosylation of intrathecally synthesized cerebrospinal fluid proteins.
7867791	2	32	theme	brain-type	261:270	arg1	glycosylation					273:285	'brain-type' glycosylation	260:285	'brain-type' glycosylation of intrathecally synthesized cerebrospinal fluid proteins	260:343	Investigation of the structural characteristics of its oligosaccharides support our hypothesis of 'brain-type' glycosylation of intrathecally synthesized cerebrospinal fluid proteins.
7867791	3	33	theme	derivatives	555:565	arg1	ion-					462:465	liquid secondary ion-	445:465	liquid secondary ion-	445:465	For carbohydrate structural analysis, high-pH anion-exchange chromatography, methylation analysis, liquid secondary ion- and matrix-assisted laser desorption/ ionization mass spectrometry of the permethylated derivatives were used.
7867791	3	33	theme	derivatives	555:565	arg1	chromatography					407:420	high-pH anion-exchange chromatography	384:420	high-pH anion-exchange chromatography	384:420	For carbohydrate structural analysis, high-pH anion-exchange chromatography, methylation analysis, liquid secondary ion- and matrix-assisted laser desorption/ ionization mass spectrometry of the permethylated derivatives were used.
7867791	3	33	theme	derivatives	555:565	arg1	analysis					435:442	methylation analysis	423:442	methylation analysis	423:442	For carbohydrate structural analysis, high-pH anion-exchange chromatography, methylation analysis, liquid secondary ion- and matrix-assisted laser desorption/ ionization mass spectrometry of the permethylated derivatives were used.
7867791	3	33	theme	derivatives	555:565	arg1	spectrometry					521:532	matrix-assisted laser desorption/ ionization mass spectrometry	471:532	matrix-assisted laser desorption/ ionization mass spectrometry	471:532	For carbohydrate structural analysis, high-pH anion-exchange chromatography, methylation analysis, liquid secondary ion- and matrix-assisted laser desorption/ ionization mass spectrometry of the permethylated derivatives were used.
7867791	0	34	theme	human	56:60	arg1	fluid					76:80	human cerebrospinal fluid	56:80	human cerebrospinal fluid	56:80	'Brain-type' N-glycosylation of asialo-transferrin from human cerebrospinal fluid.
7867791	3	35	theme	structural	363:372	arg1	analysis					374:381	carbohydrate structural analysis	350:381	carbohydrate structural analysis	350:381	For carbohydrate structural analysis, high-pH anion-exchange chromatography, methylation analysis, liquid secondary ion- and matrix-assisted laser desorption/ ionization mass spectrometry of the permethylated derivatives were used.
7867791	2	36	theme	structural	183:192	arg1	characteristics					194:208	the structural characteristics	179:208	the structural characteristics of its oligosaccharides	179:232	Investigation of the structural characteristics of its oligosaccharides support our hypothesis of 'brain-type' glycosylation of intrathecally synthesized cerebrospinal fluid proteins.
7867791	3	37	theme	laser	487:491	arg1	spectrometry					521:532	matrix-assisted laser desorption/ ionization mass spectrometry	471:532	matrix-assisted laser desorption/ ionization mass spectrometry	471:532	For carbohydrate structural analysis, high-pH anion-exchange chromatography, methylation analysis, liquid secondary ion- and matrix-assisted laser desorption/ ionization mass spectrometry of the permethylated derivatives were used.
7867791	5	38	theme	glycan	836:841	arg1	species					843:849	another major glycan species	822:849	another major glycan species derived from the sialylated transferrin variant which is galactosylated and lacks bisecting N-acetylglucosamine and fucose	822:972	Analysis of a second transferrin preparation containing both asialo- and sialo-transferrin revealed another major glycan species derived from the sialylated transferrin variant which is galactosylated and lacks bisecting N-acetylglucosamine and fucose.
7867791	0	39	gly	N-glycosylation	13:27	arg1	asialo-transferrin					32:49	asialo-transferrin	32:49	asialo-transferrin	32:49	'Brain-type' N-glycosylation of asialo-transferrin from human cerebrospinal fluid.
7867791	0	40	from	fluid	76:80	arg1	N-glycosylation					13:27	'Brain-type' N-glycosylation	0:27	'Brain-type' N-glycosylation of asialo-transferrin from human cerebrospinal fluid	0:80	'Brain-type' N-glycosylation of asialo-transferrin from human cerebrospinal fluid.
7867791	4	41	theme	agalactodiantennary	630:648	arg1	oligosaccharide					650:664	a complex-type agalactodiantennary oligosaccharide	615:664	a complex-type agalactodiantennary oligosaccharide with bisecting N-acetylglucosamine and proximal fucose	615:719	The major structure turned out to be a complex-type agalactodiantennary oligosaccharide with bisecting N-acetylglucosamine and proximal fucose.
7867791	4	41	theme	agalactodiantennary	630:648	arg1	structure					588:596	The major structure	578:596	The major structure	578:596	The major structure turned out to be a complex-type agalactodiantennary oligosaccharide with bisecting N-acetylglucosamine and proximal fucose.
7867791	2	42	theme	synthesized	304:314	arg1	proteins					336:343	intrathecally synthesized cerebrospinal fluid proteins	290:343	intrathecally synthesized cerebrospinal fluid proteins	290:343	Investigation of the structural characteristics of its oligosaccharides support our hypothesis of 'brain-type' glycosylation of intrathecally synthesized cerebrospinal fluid proteins.
7867791	1	43	from	fluid	127:131	arg1	Asialo-transferrin					83:100	Asialo-transferrin	83:100	Asialo-transferrin from human cerebrospinal fluid	83:131	Asialo-transferrin from human cerebrospinal fluid was purified to homogeneity.
7867791	3	44	theme	carbohydrate	350:361	arg1	analysis					374:381	carbohydrate structural analysis	350:381	carbohydrate structural analysis	350:381	For carbohydrate structural analysis, high-pH anion-exchange chromatography, methylation analysis, liquid secondary ion- and matrix-assisted laser desorption/ ionization mass spectrometry of the permethylated derivatives were used.
7867791	5	45	contain	containing	767:776	arg1	preparation					755:765	a second transferrin preparation	734:765	a second transferrin preparation containing both asialo- and sialo-transferrin	734:811	Analysis of a second transferrin preparation containing both asialo- and sialo-transferrin revealed another major glycan species derived from the sialylated transferrin variant which is galactosylated and lacks bisecting N-acetylglucosamine and fucose.
7867791	5	45	contain	containing	767:776	arg2	asialo-					783:789	asialo-	783:789	asialo-	783:789	Analysis of a second transferrin preparation containing both asialo- and sialo-transferrin revealed another major glycan species derived from the sialylated transferrin variant which is galactosylated and lacks bisecting N-acetylglucosamine and fucose.
7867791	5	45	contain	containing	767:776	arg2	sialo-transferrin					795:811	sialo-transferrin	795:811	sialo-transferrin	795:811	Analysis of a second transferrin preparation containing both asialo- and sialo-transferrin revealed another major glycan species derived from the sialylated transferrin variant which is galactosylated and lacks bisecting N-acetylglucosamine and fucose.
7867791	5	46	gly	sialylated	868:877	arg1	variant					891:897	the sialylated transferrin variant	864:897	the sialylated transferrin variant which is galactosylated and lacks bisecting N-acetylglucosamine and fucose	864:972	Analysis of a second transferrin preparation containing both asialo- and sialo-transferrin revealed another major glycan species derived from the sialylated transferrin variant which is galactosylated and lacks bisecting N-acetylglucosamine and fucose.
7867791	3	47	theme	anion-exchange	392:405	arg1	chromatography					407:420	high-pH anion-exchange chromatography	384:420	high-pH anion-exchange chromatography	384:420	For carbohydrate structural analysis, high-pH anion-exchange chromatography, methylation analysis, liquid secondary ion- and matrix-assisted laser desorption/ ionization mass spectrometry of the permethylated derivatives were used.
7867791	2	48	theme	oligosaccharides	217:232	arg1	characteristics					194:208	the structural characteristics	179:208	the structural characteristics of its oligosaccharides	179:232	Investigation of the structural characteristics of its oligosaccharides support our hypothesis of 'brain-type' glycosylation of intrathecally synthesized cerebrospinal fluid proteins.
7867791	0	49	theme	cerebrospinal	62:74	arg1	fluid					76:80	human cerebrospinal fluid	56:80	human cerebrospinal fluid	56:80	'Brain-type' N-glycosylation of asialo-transferrin from human cerebrospinal fluid.
7867791	2	50	theme	glycosylation	273:285	arg1	hypothesis					246:255	our hypothesis	242:255	our hypothesis of 'brain-type' glycosylation of intrathecally synthesized cerebrospinal fluid proteins	242:343	Investigation of the structural characteristics of its oligosaccharides support our hypothesis of 'brain-type' glycosylation of intrathecally synthesized cerebrospinal fluid proteins.
11168369	1	0	theme	Jews	293:296	arg1	family					273:278	a family	271:278	a family of Sephardic Jews from Kenitra (Morocco)	271:319	Albumin Kenitra is a new type of genetic variant of human serum albumin that has been found in two members of a family of Sephardic Jews from Kenitra (Morocco).
11168369	1	1	from	family	273:278	arg1	Morocco					312:318	Morocco	312:318	Morocco	312:318	Albumin Kenitra is a new type of genetic variant of human serum albumin that has been found in two members of a family of Sephardic Jews from Kenitra (Morocco).
11168369	6	2	theme	albumin	1227:1233	arg1	Kenitra					1235:1241	albumin Kenitra	1227:1241	albumin Kenitra	1227:1241	Mass spectrometric analyses revealed that the four additional cysteine residues of the variant form two new S-S bridges and showed that albumin Kenitra is partially O-glycosylated by a monosialylated HexHexNAc structure.
11168369	4	3	theme	Albumin	676:682	arg1	Kenitra					684:690	Albumin Kenitra	676:690	Albumin Kenitra	676:690	Albumin Kenitra is peculiar because it has an elongated polypeptide chain, 601 residues instead of 585, and its sequence is modified beginning from residue 575.
11168369	7	4	theme	fragment	1413:1420	arg1	analysis					1389:1396	amino-acid sequence analysis	1369:1396	amino-acid sequence analysis of the tryptic fragment 592-597	1369:1428	This oligosaccharide chain has been located to Thr596 by amino-acid sequence analysis of the tryptic fragment 592-597.
11168369	1	5	theme	albumin	225:231	arg1	variant					202:208	genetic variant	194:208	genetic variant of human serum albumin that has been found in two members of a family of Sephardic Jews from Kenitra (Morocco)	194:319	Albumin Kenitra is a new type of genetic variant of human serum albumin that has been found in two members of a family of Sephardic Jews from Kenitra (Morocco).
11168369	0	6	theme	extended	64:71	arg1	mutant					92:97	an extended and O-glycosylated mutant	61:97	an extended and O-glycosylated mutant of human serum albumin with two additional disulfide bridges	61:158	A nucleotide insertion and frameshift cause albumin Kénitra, an extended and O-glycosylated mutant of human serum albumin with two additional disulfide bridges.
11168369	0	6	theme	extended	64:71	arg1	Kénitra					52:58	albumin Kénitra	44:58	albumin Kénitra	44:58	A nucleotide insertion and frameshift cause albumin Kénitra, an extended and O-glycosylated mutant of human serum albumin with two additional disulfide bridges.
11168369	3	7	theme	sequence	657:664	arg1	analysis					666:673	sequence analysis	657:673	sequence analysis	657:673	The CNBr peptides of the variant were purified by reverse-phase high performance liquid chromatography and submitted to sequence analysis.
11168369	5	8	theme	genomic	970:976	arg1	sequence					978:985	the genomic sequence	966:985	the genomic sequence	966:985	DNA structural studies showed that the variant is caused by a single-base insertion, an adenine at nucleotide position 15 970 in the genomic sequence, which leads to a frameshift with the subsequent translation to the first termination codon of exon 15.
11168369	0	9	theme	O-glycosylated	77:90	arg1	mutant					92:97	an extended and O-glycosylated mutant	61:97	an extended and O-glycosylated mutant of human serum albumin with two additional disulfide bridges	61:158	A nucleotide insertion and frameshift cause albumin Kénitra, an extended and O-glycosylated mutant of human serum albumin with two additional disulfide bridges.
11168369	0	9	theme	O-glycosylated	77:90	arg1	Kénitra					52:58	albumin Kénitra	44:58	albumin Kénitra	44:58	A nucleotide insertion and frameshift cause albumin Kénitra, an extended and O-glycosylated mutant of human serum albumin with two additional disulfide bridges.
11168369	5	10	theme	subsequent	1025:1034	arg1	translation					1036:1046	the subsequent translation	1021:1046	the subsequent translation to the first termination codon of exon 15	1021:1088	DNA structural studies showed that the variant is caused by a single-base insertion, an adenine at nucleotide position 15 970 in the genomic sequence, which leads to a frameshift with the subsequent translation to the first termination codon of exon 15.
11168369	4	11	theme	polypeptide	732:742	arg1	chain					744:748	an elongated polypeptide chain	719:748	an elongated polypeptide chain	719:748	Albumin Kenitra is peculiar because it has an elongated polypeptide chain, 601 residues instead of 585, and its sequence is modified beginning from residue 575.
11168369	4	11	theme	polypeptide	732:742	arg1	residues					755:762	601 residues	751:762	601 residues	751:762	Albumin Kenitra is peculiar because it has an elongated polypeptide chain, 601 residues instead of 585, and its sequence is modified beginning from residue 575.
11168369	1	12	located	found	247:251	arg1	members					260:266	two members	256:266	two members of a family of Sephardic Jews from Kenitra (Morocco)	256:319	Albumin Kenitra is a new type of genetic variant of human serum albumin that has been found in two members of a family of Sephardic Jews from Kenitra (Morocco).
11168369	1	12	located	found	247:251	arg2	albumin					225:231	human serum albumin	213:231	human serum albumin that has been found in two members of a family of Sephardic Jews from Kenitra (Morocco)	213:319	Albumin Kenitra is a new type of genetic variant of human serum albumin that has been found in two members of a family of Sephardic Jews from Kenitra (Morocco).
11168369	6	13	theme	monosialylated	1276:1289	arg1	structure					1301:1309	a monosialylated HexHexNAc structure	1274:1309	a monosialylated HexHexNAc structure	1274:1309	Mass spectrometric analyses revealed that the four additional cysteine residues of the variant form two new S-S bridges and showed that albumin Kenitra is partially O-glycosylated by a monosialylated HexHexNAc structure.
11168369	0	14	theme	human	102:106	arg1	albumin					114:120	human serum albumin	102:120	human serum albumin	102:120	A nucleotide insertion and frameshift cause albumin Kénitra, an extended and O-glycosylated mutant of human serum albumin with two additional disulfide bridges.
11168369	6	15	theme	S-S	1199:1201	arg1	bridges					1203:1209	two new S-S bridges	1191:1209	two new S-S bridges	1191:1209	Mass spectrometric analyses revealed that the four additional cysteine residues of the variant form two new S-S bridges and showed that albumin Kenitra is partially O-glycosylated by a monosialylated HexHexNAc structure.
11168369	4	16	theme	601	751:753	arg1	chain					744:748	an elongated polypeptide chain	719:748	an elongated polypeptide chain	719:748	Albumin Kenitra is peculiar because it has an elongated polypeptide chain, 601 residues instead of 585, and its sequence is modified beginning from residue 575.
11168369	4	16	theme	601	751:753	arg1	residues					755:762	601 residues	751:762	601 residues	751:762	Albumin Kenitra is peculiar because it has an elongated polypeptide chain, 601 residues instead of 585, and its sequence is modified beginning from residue 575.
11168369	5	17	from	970	959:961	arg1	sequence					978:985	the genomic sequence	966:985	the genomic sequence	966:985	DNA structural studies showed that the variant is caused by a single-base insertion, an adenine at nucleotide position 15 970 in the genomic sequence, which leads to a frameshift with the subsequent translation to the first termination codon of exon 15.
11168369	1	18	theme	Albumin	161:167	arg1	type					186:189	a new type	180:189	a new type of genetic variant of human serum albumin that has been found in two members of a family of Sephardic Jews from Kenitra (Morocco)	180:319	Albumin Kenitra is a new type of genetic variant of human serum albumin that has been found in two members of a family of Sephardic Jews from Kenitra (Morocco).
11168369	1	18	theme	Albumin	161:167	arg1	Kenitra					169:175	Albumin Kenitra	161:175	Albumin Kenitra	161:175	Albumin Kenitra is a new type of genetic variant of human serum albumin that has been found in two members of a family of Sephardic Jews from Kenitra (Morocco).
11168369	6	19	theme	HexHexNAc	1291:1299	arg1	structure					1301:1309	a monosialylated HexHexNAc structure	1274:1309	a monosialylated HexHexNAc structure	1274:1309	Mass spectrometric analyses revealed that the four additional cysteine residues of the variant form two new S-S bridges and showed that albumin Kenitra is partially O-glycosylated by a monosialylated HexHexNAc structure.
11168369	5	20	theme	first	1055:1059	arg1	codon					1073:1077	the first termination codon	1051:1077	the first termination codon of exon 15	1051:1088	DNA structural studies showed that the variant is caused by a single-base insertion, an adenine at nucleotide position 15 970 in the genomic sequence, which leads to a frameshift with the subsequent translation to the first termination codon of exon 15.
11168369	6	21	theme	spectrometric	1096:1108	arg1	analyses					1110:1117	Mass spectrometric analyses	1091:1117	Mass spectrometric analyses	1091:1117	Mass spectrometric analyses revealed that the four additional cysteine residues of the variant form two new S-S bridges and showed that albumin Kenitra is partially O-glycosylated by a monosialylated HexHexNAc structure.
11168369	0	22	theme	nucleotide	2:11	arg1	insertion					13:21	A nucleotide insertion	0:21	A nucleotide insertion	0:21	A nucleotide insertion and frameshift cause albumin Kénitra, an extended and O-glycosylated mutant of human serum albumin with two additional disulfide bridges.
11168369	6	23	theme	Mass	1091:1094	arg1	analyses					1110:1117	Mass spectrometric analyses	1091:1117	Mass spectrometric analyses	1091:1117	Mass spectrometric analyses revealed that the four additional cysteine residues of the variant form two new S-S bridges and showed that albumin Kenitra is partially O-glycosylated by a monosialylated HexHexNAc structure.
11168369	0	24	gly	O-glycosylated	77:90	arg1	mutant					92:97	an extended and O-glycosylated mutant	61:97	an extended and O-glycosylated mutant of human serum albumin with two additional disulfide bridges	61:158	A nucleotide insertion and frameshift cause albumin Kénitra, an extended and O-glycosylated mutant of human serum albumin with two additional disulfide bridges.
11168369	0	24	gly	O-glycosylated	77:90	arg1	Kénitra					52:58	albumin Kénitra	44:58	albumin Kénitra	44:58	A nucleotide insertion and frameshift cause albumin Kénitra, an extended and O-glycosylated mutant of human serum albumin with two additional disulfide bridges.
11168369	5	25	from	position	947:954	arg1	insertion					911:919	a single-base insertion	897:919	a single-base insertion	897:919	DNA structural studies showed that the variant is caused by a single-base insertion, an adenine at nucleotide position 15 970 in the genomic sequence, which leads to a frameshift with the subsequent translation to the first termination codon of exon 15.
11168369	5	25	from	position	947:954	arg1	adenine					925:931	an adenine	922:931	an adenine at nucleotide position 15 970 in the genomic sequence, which leads to a frameshift with the subsequent translation to the first termination codon of exon 15	922:1088	DNA structural studies showed that the variant is caused by a single-base insertion, an adenine at nucleotide position 15 970 in the genomic sequence, which leads to a frameshift with the subsequent translation to the first termination codon of exon 15.
11168369	2	26	theme	slow-migrating	326:339	arg1	variant					341:347	The slow-migrating variant	322:347	The slow-migrating variant	322:347	The slow-migrating variant and the normal protein were isolated by anion-exchange chromatography and, after treatment with CNBr, the digests were analyzed by two-dimensional electrophoresis in a polyacrylamide gel.
11168369	2	27	theme	anion-exchange	389:402	arg1	chromatography					404:417	anion-exchange chromatography	389:417	anion-exchange chromatography	389:417	The slow-migrating variant and the normal protein were isolated by anion-exchange chromatography and, after treatment with CNBr, the digests were analyzed by two-dimensional electrophoresis in a polyacrylamide gel.
11168369	0	28	with	mutant	92:97	arg1	bridges					152:158	two additional disulfide bridges	127:158	two additional disulfide bridges	127:158	A nucleotide insertion and frameshift cause albumin Kénitra, an extended and O-glycosylated mutant of human serum albumin with two additional disulfide bridges.
11168369	5	29	theme	DNA	837:839	arg1	studies					852:858	DNA structural studies	837:858	DNA structural studies	837:858	DNA structural studies showed that the variant is caused by a single-base insertion, an adenine at nucleotide position 15 970 in the genomic sequence, which leads to a frameshift with the subsequent translation to the first termination codon of exon 15.
11168369	7	30	theme	oligosaccharide	1317:1331	arg1	chain					1333:1337	This oligosaccharide chain	1312:1337	This oligosaccharide chain	1312:1337	This oligosaccharide chain has been located to Thr596 by amino-acid sequence analysis of the tryptic fragment 592-597.
11168369	0	31	theme	albumin	114:120	arg1	mutant					92:97	an extended and O-glycosylated mutant	61:97	an extended and O-glycosylated mutant of human serum albumin with two additional disulfide bridges	61:158	A nucleotide insertion and frameshift cause albumin Kénitra, an extended and O-glycosylated mutant of human serum albumin with two additional disulfide bridges.
11168369	0	31	theme	albumin	114:120	arg1	Kénitra					52:58	albumin Kénitra	44:58	albumin Kénitra	44:58	A nucleotide insertion and frameshift cause albumin Kénitra, an extended and O-glycosylated mutant of human serum albumin with two additional disulfide bridges.
11168369	4	32	theme	elongated	722:730	arg1	chain					744:748	an elongated polypeptide chain	719:748	an elongated polypeptide chain	719:748	Albumin Kenitra is peculiar because it has an elongated polypeptide chain, 601 residues instead of 585, and its sequence is modified beginning from residue 575.
11168369	4	32	theme	elongated	722:730	arg1	residues					755:762	601 residues	751:762	601 residues	751:762	Albumin Kenitra is peculiar because it has an elongated polypeptide chain, 601 residues instead of 585, and its sequence is modified beginning from residue 575.
11168369	1	33	theme	new	182:184	arg1	type					186:189	a new type	180:189	a new type of genetic variant of human serum albumin that has been found in two members of a family of Sephardic Jews from Kenitra (Morocco)	180:319	Albumin Kenitra is a new type of genetic variant of human serum albumin that has been found in two members of a family of Sephardic Jews from Kenitra (Morocco).
11168369	1	33	theme	new	182:184	arg1	Kenitra					169:175	Albumin Kenitra	161:175	Albumin Kenitra	161:175	Albumin Kenitra is a new type of genetic variant of human serum albumin that has been found in two members of a family of Sephardic Jews from Kenitra (Morocco).
11168369	1	34	from	Morocco	312:318	arg1	family					273:278	a family	271:278	a family of Sephardic Jews from Kenitra (Morocco)	271:319	Albumin Kenitra is a new type of genetic variant of human serum albumin that has been found in two members of a family of Sephardic Jews from Kenitra (Morocco).
11168369	1	34	from	Morocco	312:318	arg1	Jews					293:296	Sephardic Jews	283:296	Sephardic Jews from Kenitra (Morocco)	283:319	Albumin Kenitra is a new type of genetic variant of human serum albumin that has been found in two members of a family of Sephardic Jews from Kenitra (Morocco).
11168369	5	35	theme	termination	1061:1071	arg1	codon					1073:1077	the first termination codon	1051:1077	the first termination codon of exon 15	1051:1088	DNA structural studies showed that the variant is caused by a single-base insertion, an adenine at nucleotide position 15 970 in the genomic sequence, which leads to a frameshift with the subsequent translation to the first termination codon of exon 15.
11168369	0	36	theme	serum	108:112	arg1	albumin					114:120	human serum albumin	102:120	human serum albumin	102:120	A nucleotide insertion and frameshift cause albumin Kénitra, an extended and O-glycosylated mutant of human serum albumin with two additional disulfide bridges.
11168369	3	37	theme	performance	606:616	arg1	chromatography					625:638	reverse-phase high performance liquid chromatography	587:638	reverse-phase high performance liquid chromatography	587:638	The CNBr peptides of the variant were purified by reverse-phase high performance liquid chromatography and submitted to sequence analysis.
11168369	6	38	gly	monosialylated	1276:1289	arg1	structure					1301:1309	a monosialylated HexHexNAc structure	1274:1309	a monosialylated HexHexNAc structure	1274:1309	Mass spectrometric analyses revealed that the four additional cysteine residues of the variant form two new S-S bridges and showed that albumin Kenitra is partially O-glycosylated by a monosialylated HexHexNAc structure.
11168369	4	39	contain	has	715:717	arg2	residues					755:762	601 residues	751:762	601 residues	751:762	Albumin Kenitra is peculiar because it has an elongated polypeptide chain, 601 residues instead of 585, and its sequence is modified beginning from residue 575.
11168369	4	39	contain	has	715:717	arg1	it					712:713	it	712:713	it	712:713	Albumin Kenitra is peculiar because it has an elongated polypeptide chain, 601 residues instead of 585, and its sequence is modified beginning from residue 575.
11168369	4	39	contain	has	715:717	arg2	585					775:777	585	775:777	an elongated polypeptide chain, 601 residues instead of 585	719:777	Albumin Kenitra is peculiar because it has an elongated polypeptide chain, 601 residues instead of 585, and its sequence is modified beginning from residue 575.
11168369	4	39	contain	has	715:717	arg2	chain					744:748	an elongated polypeptide chain	719:748	an elongated polypeptide chain	719:748	Albumin Kenitra is peculiar because it has an elongated polypeptide chain, 601 residues instead of 585, and its sequence is modified beginning from residue 575.
11168369	3	40	theme	liquid	618:623	arg1	chromatography					625:638	reverse-phase high performance liquid chromatography	587:638	reverse-phase high performance liquid chromatography	587:638	The CNBr peptides of the variant were purified by reverse-phase high performance liquid chromatography and submitted to sequence analysis.
11168369	6	41	theme	variant	1178:1184	arg1	residues					1162:1169	the four additional cysteine residues	1133:1169	the four additional cysteine residues of the variant	1133:1184	Mass spectrometric analyses revealed that the four additional cysteine residues of the variant form two new S-S bridges and showed that albumin Kenitra is partially O-glycosylated by a monosialylated HexHexNAc structure.
11168369	6	41	theme	variant	1178:1184	arg1	variant					1178:1184	the variant	1174:1184	the variant	1174:1184	Mass spectrometric analyses revealed that the four additional cysteine residues of the variant form two new S-S bridges and showed that albumin Kenitra is partially O-glycosylated by a monosialylated HexHexNAc structure.
11168369	5	42	with	frameshift	1005:1014	arg1	translation					1036:1046	the subsequent translation	1021:1046	the subsequent translation to the first termination codon of exon 15	1021:1088	DNA structural studies showed that the variant is caused by a single-base insertion, an adenine at nucleotide position 15 970 in the genomic sequence, which leads to a frameshift with the subsequent translation to the first termination codon of exon 15.
11168369	2	43	theme	normal	357:362	arg1	protein					364:370	the normal protein	353:370	the normal protein	353:370	The slow-migrating variant and the normal protein were isolated by anion-exchange chromatography and, after treatment with CNBr, the digests were analyzed by two-dimensional electrophoresis in a polyacrylamide gel.
11168369	5	44	theme	exon	1082:1085	arg1	codon					1073:1077	the first termination codon	1051:1077	the first termination codon of exon 15	1051:1088	DNA structural studies showed that the variant is caused by a single-base insertion, an adenine at nucleotide position 15 970 in the genomic sequence, which leads to a frameshift with the subsequent translation to the first termination codon of exon 15.
11168369	2	45	theme	two-dimensional	480:494	arg1	electrophoresis					496:510	two-dimensional electrophoresis	480:510	two-dimensional electrophoresis	480:510	The slow-migrating variant and the normal protein were isolated by anion-exchange chromatography and, after treatment with CNBr, the digests were analyzed by two-dimensional electrophoresis in a polyacrylamide gel.
11168369	3	46	theme	reverse-phase	587:599	arg1	chromatography					625:638	reverse-phase high performance liquid chromatography	587:638	reverse-phase high performance liquid chromatography	587:638	The CNBr peptides of the variant were purified by reverse-phase high performance liquid chromatography and submitted to sequence analysis.
11168369	7	47	theme	tryptic	1405:1411	arg1	fragment					1413:1420	the tryptic fragment 592-597	1401:1428	the tryptic fragment 592-597	1401:1428	This oligosaccharide chain has been located to Thr596 by amino-acid sequence analysis of the tryptic fragment 592-597.
11168369	1	48	theme	genetic	194:200	arg1	variant					202:208	genetic variant	194:208	genetic variant of human serum albumin that has been found in two members of a family of Sephardic Jews from Kenitra (Morocco)	194:319	Albumin Kenitra is a new type of genetic variant of human serum albumin that has been found in two members of a family of Sephardic Jews from Kenitra (Morocco).
11168369	0	49	theme	disulfide	142:150	arg1	bridges					152:158	two additional disulfide bridges	127:158	two additional disulfide bridges	127:158	A nucleotide insertion and frameshift cause albumin Kénitra, an extended and O-glycosylated mutant of human serum albumin with two additional disulfide bridges.
11168369	3	50	theme	high	601:604	arg1	chromatography					625:638	reverse-phase high performance liquid chromatography	587:638	reverse-phase high performance liquid chromatography	587:638	The CNBr peptides of the variant were purified by reverse-phase high performance liquid chromatography and submitted to sequence analysis.
11168369	3	51	theme	CNBr	541:544	arg1	peptides					546:553	The CNBr peptides	537:553	The CNBr peptides of the variant	537:568	The CNBr peptides of the variant were purified by reverse-phase high performance liquid chromatography and submitted to sequence analysis.
11168369	0	52	theme	albumin	44:50	arg1	mutant					92:97	an extended and O-glycosylated mutant	61:97	an extended and O-glycosylated mutant of human serum albumin with two additional disulfide bridges	61:158	A nucleotide insertion and frameshift cause albumin Kénitra, an extended and O-glycosylated mutant of human serum albumin with two additional disulfide bridges.
11168369	0	52	theme	albumin	44:50	arg1	Kénitra					52:58	albumin Kénitra	44:58	albumin Kénitra	44:58	A nucleotide insertion and frameshift cause albumin Kénitra, an extended and O-glycosylated mutant of human serum albumin with two additional disulfide bridges.
11168369	1	53	theme	family	273:278	arg1	members					260:266	two members	256:266	two members of a family of Sephardic Jews from Kenitra (Morocco)	256:319	Albumin Kenitra is a new type of genetic variant of human serum albumin that has been found in two members of a family of Sephardic Jews from Kenitra (Morocco).
11168369	0	54	theme	additional	131:140	arg1	bridges					152:158	two additional disulfide bridges	127:158	two additional disulfide bridges	127:158	A nucleotide insertion and frameshift cause albumin Kénitra, an extended and O-glycosylated mutant of human serum albumin with two additional disulfide bridges.
11168369	6	55	theme	new	1195:1197	arg1	bridges					1203:1209	two new S-S bridges	1191:1209	two new S-S bridges	1191:1209	Mass spectrometric analyses revealed that the four additional cysteine residues of the variant form two new S-S bridges and showed that albumin Kenitra is partially O-glycosylated by a monosialylated HexHexNAc structure.
11168369	7	56	theme	sequence	1380:1387	arg1	analysis					1389:1396	amino-acid sequence analysis	1369:1396	amino-acid sequence analysis of the tryptic fragment 592-597	1369:1428	This oligosaccharide chain has been located to Thr596 by amino-acid sequence analysis of the tryptic fragment 592-597.
11168369	6	57	theme	cysteine	1153:1160	arg1	residues					1162:1169	the four additional cysteine residues	1133:1169	the four additional cysteine residues of the variant	1133:1184	Mass spectrometric analyses revealed that the four additional cysteine residues of the variant form two new S-S bridges and showed that albumin Kenitra is partially O-glycosylated by a monosialylated HexHexNAc structure.
11168369	6	57	theme	cysteine	1153:1160	arg1	variant					1178:1184	the variant	1174:1184	the variant	1174:1184	Mass spectrometric analyses revealed that the four additional cysteine residues of the variant form two new S-S bridges and showed that albumin Kenitra is partially O-glycosylated by a monosialylated HexHexNAc structure.
11168369	5	58	theme	nucleotide	936:945	arg1	position					947:954	nucleotide position 15	936:957	nucleotide position 15	936:957	DNA structural studies showed that the variant is caused by a single-base insertion, an adenine at nucleotide position 15 970 in the genomic sequence, which leads to a frameshift with the subsequent translation to the first termination codon of exon 15.
11168369	7	59	theme	amino-acid	1369:1378	arg1	analysis					1389:1396	amino-acid sequence analysis	1369:1396	amino-acid sequence analysis of the tryptic fragment 592-597	1369:1428	This oligosaccharide chain has been located to Thr596 by amino-acid sequence analysis of the tryptic fragment 592-597.
11168369	6	60	gly	O-glycosylated	1256:1269	arg1	Kenitra					1235:1241	albumin Kenitra	1227:1241	albumin Kenitra	1227:1241	Mass spectrometric analyses revealed that the four additional cysteine residues of the variant form two new S-S bridges and showed that albumin Kenitra is partially O-glycosylated by a monosialylated HexHexNAc structure.
11168369	5	61	theme	single-base	899:909	arg1	insertion					911:919	a single-base insertion	897:919	a single-base insertion	897:919	DNA structural studies showed that the variant is caused by a single-base insertion, an adenine at nucleotide position 15 970 in the genomic sequence, which leads to a frameshift with the subsequent translation to the first termination codon of exon 15.
11168369	5	61	theme	single-base	899:909	arg1	adenine					925:931	an adenine	922:931	an adenine at nucleotide position 15 970 in the genomic sequence, which leads to a frameshift with the subsequent translation to the first termination codon of exon 15	922:1088	DNA structural studies showed that the variant is caused by a single-base insertion, an adenine at nucleotide position 15 970 in the genomic sequence, which leads to a frameshift with the subsequent translation to the first termination codon of exon 15.
11168369	1	62	theme	variant	202:208	arg1	type					186:189	a new type	180:189	a new type of genetic variant of human serum albumin that has been found in two members of a family of Sephardic Jews from Kenitra (Morocco)	180:319	Albumin Kenitra is a new type of genetic variant of human serum albumin that has been found in two members of a family of Sephardic Jews from Kenitra (Morocco).
11168369	1	62	theme	variant	202:208	arg1	Kenitra					169:175	Albumin Kenitra	161:175	Albumin Kenitra	161:175	Albumin Kenitra is a new type of genetic variant of human serum albumin that has been found in two members of a family of Sephardic Jews from Kenitra (Morocco).
11168369	2	63	theme	polyacrylamide	517:530	arg1	gel					532:534	a polyacrylamide gel	515:534	a polyacrylamide gel	515:534	The slow-migrating variant and the normal protein were isolated by anion-exchange chromatography and, after treatment with CNBr, the digests were analyzed by two-dimensional electrophoresis in a polyacrylamide gel.
11168369	6	64	theme	additional	1142:1151	arg1	residues					1162:1169	the four additional cysteine residues	1133:1169	the four additional cysteine residues of the variant	1133:1184	Mass spectrometric analyses revealed that the four additional cysteine residues of the variant form two new S-S bridges and showed that albumin Kenitra is partially O-glycosylated by a monosialylated HexHexNAc structure.
11168369	6	64	theme	additional	1142:1151	arg1	variant					1178:1184	the variant	1174:1184	the variant	1174:1184	Mass spectrometric analyses revealed that the four additional cysteine residues of the variant form two new S-S bridges and showed that albumin Kenitra is partially O-glycosylated by a monosialylated HexHexNAc structure.
11168369	5	65	dep	position	947:954	arg1	970					959:961	970	959:961	970	959:961	DNA structural studies showed that the variant is caused by a single-base insertion, an adenine at nucleotide position 15 970 in the genomic sequence, which leads to a frameshift with the subsequent translation to the first termination codon of exon 15.
11168369	3	66	theme	variant	562:568	arg1	peptides					546:553	The CNBr peptides	537:553	The CNBr peptides of the variant	537:568	The CNBr peptides of the variant were purified by reverse-phase high performance liquid chromatography and submitted to sequence analysis.
11168369	5	67	theme	structural	841:850	arg1	studies					852:858	DNA structural studies	837:858	DNA structural studies	837:858	DNA structural studies showed that the variant is caused by a single-base insertion, an adenine at nucleotide position 15 970 in the genomic sequence, which leads to a frameshift with the subsequent translation to the first termination codon of exon 15.
11168369	1	68	theme	human	213:217	arg1	albumin					225:231	human serum albumin	213:231	human serum albumin that has been found in two members of a family of Sephardic Jews from Kenitra (Morocco)	213:319	Albumin Kenitra is a new type of genetic variant of human serum albumin that has been found in two members of a family of Sephardic Jews from Kenitra (Morocco).
11168369	1	69	theme	Sephardic	283:291	arg1	Jews					293:296	Sephardic Jews	283:296	Sephardic Jews from Kenitra (Morocco)	283:319	Albumin Kenitra is a new type of genetic variant of human serum albumin that has been found in two members of a family of Sephardic Jews from Kenitra (Morocco).
11168369	2	70	with	treatment	430:438	arg1	CNBr					445:448	CNBr	445:448	CNBr	445:448	The slow-migrating variant and the normal protein were isolated by anion-exchange chromatography and, after treatment with CNBr, the digests were analyzed by two-dimensional electrophoresis in a polyacrylamide gel.
11168369	1	71	theme	serum	219:223	arg1	albumin					225:231	human serum albumin	213:231	human serum albumin that has been found in two members of a family of Sephardic Jews from Kenitra (Morocco)	213:319	Albumin Kenitra is a new type of genetic variant of human serum albumin that has been found in two members of a family of Sephardic Jews from Kenitra (Morocco).
6593222	3	0	theme	19-9	693:696	arg1	sialyl-oligosaccharide					705:726	The Ca 19-9 active sialyl-oligosaccharide	686:726	The Ca 19-9 active sialyl-oligosaccharide	686:726	The Ca 19-9 active sialyl-oligosaccharide was cleaved from the proteins by mild alkaline borohydride treatment and was shown to chromatograph on gradient elution from DEAE-Sephadex with the fraction of monosialylated saccharide alditols (MS-SP).
6593222	1	1	from	amounts	352:358	arg1	19-9					179:182	The monoclonal antibody-defined, tumor-associated antigen Ca 19-9	118:182	The monoclonal antibody-defined, tumor-associated antigen Ca 19-9	118:182	The monoclonal antibody-defined, tumor-associated antigen Ca 19-9, chemically identical with the sialylated Lewisa-carbohydrate determinant of a monoganglioside and a mucin, was demonstrated by radioimmunoassay to be present in large amounts as component of fucose-rich sialoglycoproteins, which had been extracted from human seminal plasma of healthy donors.
6593222	1	1	from	amounts	352:358	arg1	present					335:341	present	335:341	present	335:341	The monoclonal antibody-defined, tumor-associated antigen Ca 19-9, chemically identical with the sialylated Lewisa-carbohydrate determinant of a monoganglioside and a mucin, was demonstrated by radioimmunoassay to be present in large amounts as component of fucose-rich sialoglycoproteins, which had been extracted from human seminal plasma of healthy donors.
6593222	1	2	theme	donors	470:475	arg1	plasma					452:457	human seminal plasma	438:457	human seminal plasma of healthy donors	438:475	The monoclonal antibody-defined, tumor-associated antigen Ca 19-9, chemically identical with the sialylated Lewisa-carbohydrate determinant of a monoganglioside and a mucin, was demonstrated by radioimmunoassay to be present in large amounts as component of fucose-rich sialoglycoproteins, which had been extracted from human seminal plasma of healthy donors.
6593222	1	3	theme	human	438:442	arg1	plasma					452:457	human seminal plasma	438:457	human seminal plasma of healthy donors	438:475	The monoclonal antibody-defined, tumor-associated antigen Ca 19-9, chemically identical with the sialylated Lewisa-carbohydrate determinant of a monoganglioside and a mucin, was demonstrated by radioimmunoassay to be present in large amounts as component of fucose-rich sialoglycoproteins, which had been extracted from human seminal plasma of healthy donors.
6593222	6	4	theme	direct	1595:1600	arg1	EI					1608:1609	direct probe EI	1595:1609	direct probe EI	1595:1609	The presented data and the fragmentation pattern obtained on direct probe EI and FAB+ mass spectrometry of the permethylated asialo derivative are in accordance with the structure of a sialylated pentasaccharide alditol (formula; see text).
6593222	5	5	theme	fraction	1274:1281	arg1	MS-SP					1283:1287	fraction MS-SP	1274:1287	fraction MS-SP	1274:1287	A methylation analysis of the sialylated saccharide alditol in fraction MS-SP, which had been purified by high-pressure liquid chromatography, revealed the presence of terminal, non-reducing L-fucose, 3-O-substituted D-galactose, 3,4 di-O-substituted N-acetyl-D-glucosamine and 3-O-substituted N-acetyl-D-galactosaminitol.
6593222	6	6	gly	sialylated	1719:1728	arg1	alditol					1746:1752	a sialylated pentasaccharide alditol	1717:1752	a sialylated pentasaccharide alditol (formula; see text)	1717:1772	The presented data and the fragmentation pattern obtained on direct probe EI and FAB+ mass spectrometry of the permethylated asialo derivative are in accordance with the structure of a sialylated pentasaccharide alditol (formula; see text).
6593222	1	7	gly	sialylated	215:224	arg1	determinant					246:256	the sialylated Lewisa-carbohydrate determinant	211:256	the sialylated Lewisa-carbohydrate determinant of a monoganglioside and a mucin	211:289	The monoclonal antibody-defined, tumor-associated antigen Ca 19-9, chemically identical with the sialylated Lewisa-carbohydrate determinant of a monoganglioside and a mucin, was demonstrated by radioimmunoassay to be present in large amounts as component of fucose-rich sialoglycoproteins, which had been extracted from human seminal plasma of healthy donors.
6593222	1	8	theme	identical	196:204	arg1	19-9					179:182	The monoclonal antibody-defined, tumor-associated antigen Ca 19-9	118:182	The monoclonal antibody-defined, tumor-associated antigen Ca 19-9	118:182	The monoclonal antibody-defined, tumor-associated antigen Ca 19-9, chemically identical with the sialylated Lewisa-carbohydrate determinant of a monoganglioside and a mucin, was demonstrated by radioimmunoassay to be present in large amounts as component of fucose-rich sialoglycoproteins, which had been extracted from human seminal plasma of healthy donors.
6593222	1	8	theme	identical	196:204	arg1	present					335:341	present	335:341	present	335:341	The monoclonal antibody-defined, tumor-associated antigen Ca 19-9, chemically identical with the sialylated Lewisa-carbohydrate determinant of a monoganglioside and a mucin, was demonstrated by radioimmunoassay to be present in large amounts as component of fucose-rich sialoglycoproteins, which had been extracted from human seminal plasma of healthy donors.
6593222	3	9	theme	alkaline	766:773	arg1	treatment					787:795	mild alkaline borohydride treatment	761:795	mild alkaline borohydride treatment	761:795	The Ca 19-9 active sialyl-oligosaccharide was cleaved from the proteins by mild alkaline borohydride treatment and was shown to chromatograph on gradient elution from DEAE-Sephadex with the fraction of monosialylated saccharide alditols (MS-SP).
6593222	1	10	attach	present	335:341	arg2	19-9					179:182	The monoclonal antibody-defined, tumor-associated antigen Ca 19-9	118:182	The monoclonal antibody-defined, tumor-associated antigen Ca 19-9	118:182	The monoclonal antibody-defined, tumor-associated antigen Ca 19-9, chemically identical with the sialylated Lewisa-carbohydrate determinant of a monoganglioside and a mucin, was demonstrated by radioimmunoassay to be present in large amounts as component of fucose-rich sialoglycoproteins, which had been extracted from human seminal plasma of healthy donors.
6593222	1	10	attach	present	335:341	arg2	present					335:341	present	335:341	present	335:341	The monoclonal antibody-defined, tumor-associated antigen Ca 19-9, chemically identical with the sialylated Lewisa-carbohydrate determinant of a monoganglioside and a mucin, was demonstrated by radioimmunoassay to be present in large amounts as component of fucose-rich sialoglycoproteins, which had been extracted from human seminal plasma of healthy donors.
6593222	1	10	attach	present	335:341	arg1	amounts					352:358	large amounts	346:358	large amounts as component of fucose-rich sialoglycoproteins, which had been extracted from human seminal plasma of healthy donors	346:475	The monoclonal antibody-defined, tumor-associated antigen Ca 19-9, chemically identical with the sialylated Lewisa-carbohydrate determinant of a monoganglioside and a mucin, was demonstrated by radioimmunoassay to be present in large amounts as component of fucose-rich sialoglycoproteins, which had been extracted from human seminal plasma of healthy donors.
6593222	6	11	theme	asialo	1659:1664	arg1	derivative					1666:1675	the permethylated asialo derivative	1641:1675	the permethylated asialo derivative	1641:1675	The presented data and the fragmentation pattern obtained on direct probe EI and FAB+ mass spectrometry of the permethylated asialo derivative are in accordance with the structure of a sialylated pentasaccharide alditol (formula; see text).
6593222	6	12	theme	sialylated	1719:1728	arg1	alditol					1746:1752	a sialylated pentasaccharide alditol	1717:1752	a sialylated pentasaccharide alditol (formula; see text)	1717:1772	The presented data and the fragmentation pattern obtained on direct probe EI and FAB+ mass spectrometry of the permethylated asialo derivative are in accordance with the structure of a sialylated pentasaccharide alditol (formula; see text).
6593222	1	13	theme	Lewisa-carbohydrate	226:244	arg1	determinant					246:256	the sialylated Lewisa-carbohydrate determinant	211:256	the sialylated Lewisa-carbohydrate determinant of a monoganglioside and a mucin	211:289	The monoclonal antibody-defined, tumor-associated antigen Ca 19-9, chemically identical with the sialylated Lewisa-carbohydrate determinant of a monoganglioside and a mucin, was demonstrated by radioimmunoassay to be present in large amounts as component of fucose-rich sialoglycoproteins, which had been extracted from human seminal plasma of healthy donors.
6593222	4	14	theme	major	961:965	arg1	alditol					978:984	the major saccharide alditol	957:984	the major saccharide alditol in this fraction	957:1001	The asialo derivative of the major saccharide alditol in this fraction was composed of L-fucose, D-galactose, N-acetyl-D-glucosamine and N-acetyl-D-galactosaminitol in the molar proportions 1:2:1:1 and chromatographed on Bio-Gel P2 according to approximately seven hexose units.
6593222	6	15	theme	fragmentation	1561:1573	arg1	pattern					1575:1581	the fragmentation pattern	1557:1581	the fragmentation pattern	1557:1581	The presented data and the fragmentation pattern obtained on direct probe EI and FAB+ mass spectrometry of the permethylated asialo derivative are in accordance with the structure of a sialylated pentasaccharide alditol (formula; see text).
6593222	6	16	theme	alditol	1746:1752	arg1	structure					1704:1712	the structure	1700:1712	the structure of a sialylated pentasaccharide alditol (formula; see text)	1700:1772	The presented data and the fragmentation pattern obtained on direct probe EI and FAB+ mass spectrometry of the permethylated asialo derivative are in accordance with the structure of a sialylated pentasaccharide alditol (formula; see text).
6593222	4	17	from	N-acetyl-D-galactosaminitol	1069:1095	arg1	proportions					1110:1120	the molar proportions	1100:1120	the molar proportions 1:2:1:1 and chromatographed on Bio-Gel P2 according to approximately seven hexose units	1100:1208	The asialo derivative of the major saccharide alditol in this fraction was composed of L-fucose, D-galactose, N-acetyl-D-glucosamine and N-acetyl-D-galactosaminitol in the molar proportions 1:2:1:1 and chromatographed on Bio-Gel P2 according to approximately seven hexose units.
6593222	2	18	from	plasma	642:647	arg1	absent					624:629	absent	624:629	absent	624:629	The carbohydrate antigen of these glycoproteins (m greater than 205 kDa and m 115 kDa), which are presumably secreted by the prostatic gland, was absent in seminal plasma from blood-group-Lewis-negative men.
6593222	2	18	from	plasma	642:647	arg1	antigen					495:501	The carbohydrate antigen	478:501	The carbohydrate antigen	478:501	The carbohydrate antigen of these glycoproteins (m greater than 205 kDa and m 115 kDa), which are presumably secreted by the prostatic gland, was absent in seminal plasma from blood-group-Lewis-negative men.
6593222	1	19	theme	seminal	444:450	arg1	plasma					452:457	human seminal plasma	438:457	human seminal plasma of healthy donors	438:475	The monoclonal antibody-defined, tumor-associated antigen Ca 19-9, chemically identical with the sialylated Lewisa-carbohydrate determinant of a monoganglioside and a mucin, was demonstrated by radioimmunoassay to be present in large amounts as component of fucose-rich sialoglycoproteins, which had been extracted from human seminal plasma of healthy donors.
6593222	3	20	with	DEAE-Sephadex	853:865	arg1	fraction					876:883	the fraction	872:883	the fraction of monosialylated saccharide alditols (MS-SP)	872:929	The Ca 19-9 active sialyl-oligosaccharide was cleaved from the proteins by mild alkaline borohydride treatment and was shown to chromatograph on gradient elution from DEAE-Sephadex with the fraction of monosialylated saccharide alditols (MS-SP).
6593222	1	21	theme	antibody-defined	133:148	arg1	19-9					179:182	The monoclonal antibody-defined, tumor-associated antigen Ca 19-9	118:182	The monoclonal antibody-defined, tumor-associated antigen Ca 19-9	118:182	The monoclonal antibody-defined, tumor-associated antigen Ca 19-9, chemically identical with the sialylated Lewisa-carbohydrate determinant of a monoganglioside and a mucin, was demonstrated by radioimmunoassay to be present in large amounts as component of fucose-rich sialoglycoproteins, which had been extracted from human seminal plasma of healthy donors.
6593222	1	21	theme	antibody-defined	133:148	arg1	present					335:341	present	335:341	present	335:341	The monoclonal antibody-defined, tumor-associated antigen Ca 19-9, chemically identical with the sialylated Lewisa-carbohydrate determinant of a monoganglioside and a mucin, was demonstrated by radioimmunoassay to be present in large amounts as component of fucose-rich sialoglycoproteins, which had been extracted from human seminal plasma of healthy donors.
6593222	4	22	theme	asialo	936:941	arg1	derivative					943:952	The asialo derivative	932:952	The asialo derivative of the major saccharide alditol in this fraction	932:1001	The asialo derivative of the major saccharide alditol in this fraction was composed of L-fucose, D-galactose, N-acetyl-D-glucosamine and N-acetyl-D-galactosaminitol in the molar proportions 1:2:1:1 and chromatographed on Bio-Gel P2 according to approximately seven hexose units.
6593222	0	23	theme	human	62:66	arg1	glycoproteins					83:95	human seminal-plasma glycoproteins	62:95	human seminal-plasma glycoproteins from healthy donors	62:115	Structure of tumor-associated carbohydrate antigen Ca 19-9 on human seminal-plasma glycoproteins from healthy donors.
6593222	1	24	theme	Ca	176:177	arg1	19-9					179:182	The monoclonal antibody-defined, tumor-associated antigen Ca 19-9	118:182	The monoclonal antibody-defined, tumor-associated antigen Ca 19-9	118:182	The monoclonal antibody-defined, tumor-associated antigen Ca 19-9, chemically identical with the sialylated Lewisa-carbohydrate determinant of a monoganglioside and a mucin, was demonstrated by radioimmunoassay to be present in large amounts as component of fucose-rich sialoglycoproteins, which had been extracted from human seminal plasma of healthy donors.
6593222	1	24	theme	Ca	176:177	arg1	present					335:341	present	335:341	present	335:341	The monoclonal antibody-defined, tumor-associated antigen Ca 19-9, chemically identical with the sialylated Lewisa-carbohydrate determinant of a monoganglioside and a mucin, was demonstrated by radioimmunoassay to be present in large amounts as component of fucose-rich sialoglycoproteins, which had been extracted from human seminal plasma of healthy donors.
6593222	5	25	theme	high-pressure	1317:1329	arg1	chromatography					1338:1351	high-pressure liquid chromatography	1317:1351	high-pressure liquid chromatography	1317:1351	A methylation analysis of the sialylated saccharide alditol in fraction MS-SP, which had been purified by high-pressure liquid chromatography, revealed the presence of terminal, non-reducing L-fucose, 3-O-substituted D-galactose, 3,4 di-O-substituted N-acetyl-D-glucosamine and 3-O-substituted N-acetyl-D-galactosaminitol.
6593222	2	26	dep	antigen	495:501	arg1	m					527:527	m	527:527	m greater than 205 kDa and m 115 kDa	527:562	The carbohydrate antigen of these glycoproteins (m greater than 205 kDa and m 115 kDa), which are presumably secreted by the prostatic gland, was absent in seminal plasma from blood-group-Lewis-negative men.
6593222	3	27	theme	saccharide	903:912	arg1	alditols					914:921	monosialylated saccharide alditols	888:921	monosialylated saccharide alditols (MS-SP)	888:929	The Ca 19-9 active sialyl-oligosaccharide was cleaved from the proteins by mild alkaline borohydride treatment and was shown to chromatograph on gradient elution from DEAE-Sephadex with the fraction of monosialylated saccharide alditols (MS-SP).
6593222	3	27	theme	saccharide	903:912	arg1	MS-SP					924:928	MS-SP	924:928	MS-SP	924:928	The Ca 19-9 active sialyl-oligosaccharide was cleaved from the proteins by mild alkaline borohydride treatment and was shown to chromatograph on gradient elution from DEAE-Sephadex with the fraction of monosialylated saccharide alditols (MS-SP).
6593222	2	28	theme	m	554:554	arg1	kDa					560:562	m 115 kDa	554:562	m 115 kDa	554:562	The carbohydrate antigen of these glycoproteins (m greater than 205 kDa and m 115 kDa), which are presumably secreted by the prostatic gland, was absent in seminal plasma from blood-group-Lewis-negative men.
6593222	0	29	from	Structure	0:8	arg1	glycoproteins					83:95	human seminal-plasma glycoproteins	62:95	human seminal-plasma glycoproteins from healthy donors	62:115	Structure of tumor-associated carbohydrate antigen Ca 19-9 on human seminal-plasma glycoproteins from healthy donors.
6593222	0	30	theme	healthy	102:108	arg1	donors					110:115	healthy donors	102:115	healthy donors	102:115	Structure of tumor-associated carbohydrate antigen Ca 19-9 on human seminal-plasma glycoproteins from healthy donors.
6593222	1	31	theme	sialoglycoproteins	388:405	arg1	component					363:371	component	363:371	component of fucose-rich sialoglycoproteins, which had been extracted from human seminal plasma of healthy donors	363:475	The monoclonal antibody-defined, tumor-associated antigen Ca 19-9, chemically identical with the sialylated Lewisa-carbohydrate determinant of a monoganglioside and a mucin, was demonstrated by radioimmunoassay to be present in large amounts as component of fucose-rich sialoglycoproteins, which had been extracted from human seminal plasma of healthy donors.
6593222	2	32	theme	seminal	634:640	arg1	plasma					642:647	seminal plasma	634:647	seminal plasma from blood-group-Lewis-negative men	634:683	The carbohydrate antigen of these glycoproteins (m greater than 205 kDa and m 115 kDa), which are presumably secreted by the prostatic gland, was absent in seminal plasma from blood-group-Lewis-negative men.
6593222	6	33	dep	see	1764:1766	arg1	formula					1755:1761	formula	1755:1761	formula	1755:1761	The presented data and the fragmentation pattern obtained on direct probe EI and FAB+ mass spectrometry of the permethylated asialo derivative are in accordance with the structure of a sialylated pentasaccharide alditol (formula; see text).
6593222	2	34	theme	carbohydrate	482:493	arg1	absent					624:629	absent	624:629	absent	624:629	The carbohydrate antigen of these glycoproteins (m greater than 205 kDa and m 115 kDa), which are presumably secreted by the prostatic gland, was absent in seminal plasma from blood-group-Lewis-negative men.
6593222	2	34	theme	carbohydrate	482:493	arg1	antigen					495:501	The carbohydrate antigen	478:501	The carbohydrate antigen	478:501	The carbohydrate antigen of these glycoproteins (m greater than 205 kDa and m 115 kDa), which are presumably secreted by the prostatic gland, was absent in seminal plasma from blood-group-Lewis-negative men.
6593222	5	35	theme	alditol	1263:1269	arg1	analysis					1225:1232	A methylation analysis	1211:1232	A methylation analysis	1211:1232	A methylation analysis of the sialylated saccharide alditol in fraction MS-SP, which had been purified by high-pressure liquid chromatography, revealed the presence of terminal, non-reducing L-fucose, 3-O-substituted D-galactose, 3,4 di-O-substituted N-acetyl-D-glucosamine and 3-O-substituted N-acetyl-D-galactosaminitol.
6593222	1	36	located	present	335:341	arg2	19-9					179:182	The monoclonal antibody-defined, tumor-associated antigen Ca 19-9	118:182	The monoclonal antibody-defined, tumor-associated antigen Ca 19-9	118:182	The monoclonal antibody-defined, tumor-associated antigen Ca 19-9, chemically identical with the sialylated Lewisa-carbohydrate determinant of a monoganglioside and a mucin, was demonstrated by radioimmunoassay to be present in large amounts as component of fucose-rich sialoglycoproteins, which had been extracted from human seminal plasma of healthy donors.
6593222	1	36	located	present	335:341	arg2	present					335:341	present	335:341	present	335:341	The monoclonal antibody-defined, tumor-associated antigen Ca 19-9, chemically identical with the sialylated Lewisa-carbohydrate determinant of a monoganglioside and a mucin, was demonstrated by radioimmunoassay to be present in large amounts as component of fucose-rich sialoglycoproteins, which had been extracted from human seminal plasma of healthy donors.
6593222	1	36	located	present	335:341	arg1	amounts					352:358	large amounts	346:358	large amounts as component of fucose-rich sialoglycoproteins, which had been extracted from human seminal plasma of healthy donors	346:475	The monoclonal antibody-defined, tumor-associated antigen Ca 19-9, chemically identical with the sialylated Lewisa-carbohydrate determinant of a monoganglioside and a mucin, was demonstrated by radioimmunoassay to be present in large amounts as component of fucose-rich sialoglycoproteins, which had been extracted from human seminal plasma of healthy donors.
6593222	5	37	theme	terminal	1379:1386	arg1	N-acetyl-D-glucosamine					1462:1483	3,4 di-O-substituted N-acetyl-D-glucosamine	1441:1483	3,4 di-O-substituted N-acetyl-D-glucosamine	1441:1483	A methylation analysis of the sialylated saccharide alditol in fraction MS-SP, which had been purified by high-pressure liquid chromatography, revealed the presence of terminal, non-reducing L-fucose, 3-O-substituted D-galactose, 3,4 di-O-substituted N-acetyl-D-glucosamine and 3-O-substituted N-acetyl-D-galactosaminitol.
6593222	5	37	theme	terminal	1379:1386	arg1	N-acetyl-D-galactosaminitol					1505:1531	3-O-substituted N-acetyl-D-galactosaminitol	1489:1531	3-O-substituted N-acetyl-D-galactosaminitol	1489:1531	A methylation analysis of the sialylated saccharide alditol in fraction MS-SP, which had been purified by high-pressure liquid chromatography, revealed the presence of terminal, non-reducing L-fucose, 3-O-substituted D-galactose, 3,4 di-O-substituted N-acetyl-D-glucosamine and 3-O-substituted N-acetyl-D-galactosaminitol.
6593222	5	37	theme	terminal	1379:1386	arg1	L-fucose					1402:1409	terminal, non-reducing L-fucose	1379:1409	L-fucose	1402:1409	A methylation analysis of the sialylated saccharide alditol in fraction MS-SP, which had been purified by high-pressure liquid chromatography, revealed the presence of terminal, non-reducing L-fucose, 3-O-substituted D-galactose, 3,4 di-O-substituted N-acetyl-D-glucosamine and 3-O-substituted N-acetyl-D-galactosaminitol.
6593222	5	37	theme	terminal	1379:1386	arg1	D-galactose					1428:1438	3-O-substituted D-galactose	1412:1438	3-O-substituted D-galactose	1412:1438	A methylation analysis of the sialylated saccharide alditol in fraction MS-SP, which had been purified by high-pressure liquid chromatography, revealed the presence of terminal, non-reducing L-fucose, 3-O-substituted D-galactose, 3,4 di-O-substituted N-acetyl-D-glucosamine and 3-O-substituted N-acetyl-D-galactosaminitol.
6593222	0	38	theme	tumor-associated	13:28	arg1	19-9					54:57	tumor-associated carbohydrate antigen Ca 19-9	13:57	tumor-associated carbohydrate antigen Ca 19-9	13:57	Structure of tumor-associated carbohydrate antigen Ca 19-9 on human seminal-plasma glycoproteins from healthy donors.
6593222	5	39	theme	saccharide	1252:1261	arg1	alditol					1263:1269	the sialylated saccharide alditol	1237:1269	the sialylated saccharide alditol in fraction MS-SP	1237:1287	A methylation analysis of the sialylated saccharide alditol in fraction MS-SP, which had been purified by high-pressure liquid chromatography, revealed the presence of terminal, non-reducing L-fucose, 3-O-substituted D-galactose, 3,4 di-O-substituted N-acetyl-D-glucosamine and 3-O-substituted N-acetyl-D-galactosaminitol.
6593222	2	40	theme	glycoproteins	512:524	arg1	absent					624:629	absent	624:629	absent	624:629	The carbohydrate antigen of these glycoproteins (m greater than 205 kDa and m 115 kDa), which are presumably secreted by the prostatic gland, was absent in seminal plasma from blood-group-Lewis-negative men.
6593222	2	40	theme	glycoproteins	512:524	arg1	antigen					495:501	The carbohydrate antigen	478:501	The carbohydrate antigen	478:501	The carbohydrate antigen of these glycoproteins (m greater than 205 kDa and m 115 kDa), which are presumably secreted by the prostatic gland, was absent in seminal plasma from blood-group-Lewis-negative men.
6593222	3	41	from	DEAE-Sephadex	853:865	arg1	elution					840:846	gradient elution	831:846	gradient elution from DEAE-Sephadex with the fraction of monosialylated saccharide alditols (MS-SP)	831:929	The Ca 19-9 active sialyl-oligosaccharide was cleaved from the proteins by mild alkaline borohydride treatment and was shown to chromatograph on gradient elution from DEAE-Sephadex with the fraction of monosialylated saccharide alditols (MS-SP).
6593222	5	42	theme	non-reducing	1389:1400	arg1	N-acetyl-D-glucosamine					1462:1483	3,4 di-O-substituted N-acetyl-D-glucosamine	1441:1483	3,4 di-O-substituted N-acetyl-D-glucosamine	1441:1483	A methylation analysis of the sialylated saccharide alditol in fraction MS-SP, which had been purified by high-pressure liquid chromatography, revealed the presence of terminal, non-reducing L-fucose, 3-O-substituted D-galactose, 3,4 di-O-substituted N-acetyl-D-glucosamine and 3-O-substituted N-acetyl-D-galactosaminitol.
6593222	5	42	theme	non-reducing	1389:1400	arg1	N-acetyl-D-galactosaminitol					1505:1531	3-O-substituted N-acetyl-D-galactosaminitol	1489:1531	3-O-substituted N-acetyl-D-galactosaminitol	1489:1531	A methylation analysis of the sialylated saccharide alditol in fraction MS-SP, which had been purified by high-pressure liquid chromatography, revealed the presence of terminal, non-reducing L-fucose, 3-O-substituted D-galactose, 3,4 di-O-substituted N-acetyl-D-glucosamine and 3-O-substituted N-acetyl-D-galactosaminitol.
6593222	5	42	theme	non-reducing	1389:1400	arg1	L-fucose					1402:1409	terminal, non-reducing L-fucose	1379:1409	L-fucose	1402:1409	A methylation analysis of the sialylated saccharide alditol in fraction MS-SP, which had been purified by high-pressure liquid chromatography, revealed the presence of terminal, non-reducing L-fucose, 3-O-substituted D-galactose, 3,4 di-O-substituted N-acetyl-D-glucosamine and 3-O-substituted N-acetyl-D-galactosaminitol.
6593222	5	42	theme	non-reducing	1389:1400	arg1	D-galactose					1428:1438	3-O-substituted D-galactose	1412:1438	3-O-substituted D-galactose	1412:1438	A methylation analysis of the sialylated saccharide alditol in fraction MS-SP, which had been purified by high-pressure liquid chromatography, revealed the presence of terminal, non-reducing L-fucose, 3-O-substituted D-galactose, 3,4 di-O-substituted N-acetyl-D-glucosamine and 3-O-substituted N-acetyl-D-galactosaminitol.
6593222	0	43	theme	antigen	43:49	arg1	19-9					54:57	tumor-associated carbohydrate antigen Ca 19-9	13:57	tumor-associated carbohydrate antigen Ca 19-9	13:57	Structure of tumor-associated carbohydrate antigen Ca 19-9 on human seminal-plasma glycoproteins from healthy donors.
6593222	2	44	gly	glycoproteins	512:524	arg1	glycoproteins					512:524	these glycoproteins	506:524	these glycoproteins	506:524	The carbohydrate antigen of these glycoproteins (m greater than 205 kDa and m 115 kDa), which are presumably secreted by the prostatic gland, was absent in seminal plasma from blood-group-Lewis-negative men.
6593222	5	45	theme	3-O-substituted	1489:1503	arg1	N-acetyl-D-galactosaminitol					1505:1531	3-O-substituted N-acetyl-D-galactosaminitol	1489:1531	3-O-substituted N-acetyl-D-galactosaminitol	1489:1531	A methylation analysis of the sialylated saccharide alditol in fraction MS-SP, which had been purified by high-pressure liquid chromatography, revealed the presence of terminal, non-reducing L-fucose, 3-O-substituted D-galactose, 3,4 di-O-substituted N-acetyl-D-glucosamine and 3-O-substituted N-acetyl-D-galactosaminitol.
6593222	5	45	theme	3-O-substituted	1489:1503	arg1	L-fucose					1402:1409	terminal, non-reducing L-fucose	1379:1409	L-fucose	1402:1409	A methylation analysis of the sialylated saccharide alditol in fraction MS-SP, which had been purified by high-pressure liquid chromatography, revealed the presence of terminal, non-reducing L-fucose, 3-O-substituted D-galactose, 3,4 di-O-substituted N-acetyl-D-glucosamine and 3-O-substituted N-acetyl-D-galactosaminitol.
6593222	0	46	theme	19-9	54:57	arg1	Structure					0:8	Structure	0:8	Structure of tumor-associated carbohydrate antigen Ca 19-9 on human seminal-plasma glycoproteins from healthy donors.	0:116	Structure of tumor-associated carbohydrate antigen Ca 19-9 on human seminal-plasma glycoproteins from healthy donors.
6593222	1	47	theme	large	346:350	arg1	amounts					352:358	large amounts	346:358	large amounts as component of fucose-rich sialoglycoproteins, which had been extracted from human seminal plasma of healthy donors	346:475	The monoclonal antibody-defined, tumor-associated antigen Ca 19-9, chemically identical with the sialylated Lewisa-carbohydrate determinant of a monoganglioside and a mucin, was demonstrated by radioimmunoassay to be present in large amounts as component of fucose-rich sialoglycoproteins, which had been extracted from human seminal plasma of healthy donors.
6593222	5	48	from	alditol	1263:1269	arg1	MS-SP					1283:1287	fraction MS-SP	1274:1287	fraction MS-SP	1274:1287	A methylation analysis of the sialylated saccharide alditol in fraction MS-SP, which had been purified by high-pressure liquid chromatography, revealed the presence of terminal, non-reducing L-fucose, 3-O-substituted D-galactose, 3,4 di-O-substituted N-acetyl-D-glucosamine and 3-O-substituted N-acetyl-D-galactosaminitol.
6593222	2	49	from	absent	624:629	arg1	plasma					642:647	seminal plasma	634:647	seminal plasma from blood-group-Lewis-negative men	634:683	The carbohydrate antigen of these glycoproteins (m greater than 205 kDa and m 115 kDa), which are presumably secreted by the prostatic gland, was absent in seminal plasma from blood-group-Lewis-negative men.
6593222	3	50	theme	Ca	690:691	arg1	19-9					693:696	The Ca 19-9	686:696	The Ca 19-9 active sialyl-oligosaccharide	686:726	The Ca 19-9 active sialyl-oligosaccharide was cleaved from the proteins by mild alkaline borohydride treatment and was shown to chromatograph on gradient elution from DEAE-Sephadex with the fraction of monosialylated saccharide alditols (MS-SP).
6593222	6	51	theme	mass	1620:1623	arg1	spectrometry					1625:1636	FAB+ mass spectrometry	1615:1636	FAB+ mass spectrometry	1615:1636	The presented data and the fragmentation pattern obtained on direct probe EI and FAB+ mass spectrometry of the permethylated asialo derivative are in accordance with the structure of a sialylated pentasaccharide alditol (formula; see text).
6593222	1	52	with	identical	196:204	arg1	determinant					246:256	the sialylated Lewisa-carbohydrate determinant	211:256	the sialylated Lewisa-carbohydrate determinant of a monoganglioside and a mucin	211:289	The monoclonal antibody-defined, tumor-associated antigen Ca 19-9, chemically identical with the sialylated Lewisa-carbohydrate determinant of a monoganglioside and a mucin, was demonstrated by radioimmunoassay to be present in large amounts as component of fucose-rich sialoglycoproteins, which had been extracted from human seminal plasma of healthy donors.
6593222	4	53	theme	Bio-Gel	1153:1159	arg1	P2					1161:1162	Bio-Gel P2	1153:1162	Bio-Gel P2	1153:1162	The asialo derivative of the major saccharide alditol in this fraction was composed of L-fucose, D-galactose, N-acetyl-D-glucosamine and N-acetyl-D-galactosaminitol in the molar proportions 1:2:1:1 and chromatographed on Bio-Gel P2 according to approximately seven hexose units.
6593222	5	54	theme	3,4	1441:1443	arg1	N-acetyl-D-glucosamine					1462:1483	3,4 di-O-substituted N-acetyl-D-glucosamine	1441:1483	3,4 di-O-substituted N-acetyl-D-glucosamine	1441:1483	A methylation analysis of the sialylated saccharide alditol in fraction MS-SP, which had been purified by high-pressure liquid chromatography, revealed the presence of terminal, non-reducing L-fucose, 3-O-substituted D-galactose, 3,4 di-O-substituted N-acetyl-D-glucosamine and 3-O-substituted N-acetyl-D-galactosaminitol.
6593222	5	54	theme	3,4	1441:1443	arg1	L-fucose					1402:1409	terminal, non-reducing L-fucose	1379:1409	L-fucose	1402:1409	A methylation analysis of the sialylated saccharide alditol in fraction MS-SP, which had been purified by high-pressure liquid chromatography, revealed the presence of terminal, non-reducing L-fucose, 3-O-substituted D-galactose, 3,4 di-O-substituted N-acetyl-D-glucosamine and 3-O-substituted N-acetyl-D-galactosaminitol.
6593222	4	55	theme	molar	1104:1108	arg1	proportions					1110:1120	the molar proportions	1100:1120	the molar proportions 1:2:1:1 and chromatographed on Bio-Gel P2 according to approximately seven hexose units	1100:1208	The asialo derivative of the major saccharide alditol in this fraction was composed of L-fucose, D-galactose, N-acetyl-D-glucosamine and N-acetyl-D-galactosaminitol in the molar proportions 1:2:1:1 and chromatographed on Bio-Gel P2 according to approximately seven hexose units.
6593222	4	56	from	D-galactose	1029:1039	arg1	proportions					1110:1120	the molar proportions	1100:1120	the molar proportions 1:2:1:1 and chromatographed on Bio-Gel P2 according to approximately seven hexose units	1100:1208	The asialo derivative of the major saccharide alditol in this fraction was composed of L-fucose, D-galactose, N-acetyl-D-glucosamine and N-acetyl-D-galactosaminitol in the molar proportions 1:2:1:1 and chromatographed on Bio-Gel P2 according to approximately seven hexose units.
6593222	5	57	from	analysis	1225:1232	arg1	MS-SP					1283:1287	fraction MS-SP	1274:1287	fraction MS-SP	1274:1287	A methylation analysis of the sialylated saccharide alditol in fraction MS-SP, which had been purified by high-pressure liquid chromatography, revealed the presence of terminal, non-reducing L-fucose, 3-O-substituted D-galactose, 3,4 di-O-substituted N-acetyl-D-glucosamine and 3-O-substituted N-acetyl-D-galactosaminitol.
6593222	6	58	theme	probe	1602:1606	arg1	EI					1608:1609	direct probe EI	1595:1609	direct probe EI	1595:1609	The presented data and the fragmentation pattern obtained on direct probe EI and FAB+ mass spectrometry of the permethylated asialo derivative are in accordance with the structure of a sialylated pentasaccharide alditol (formula; see text).
6593222	1	59	theme	mucin	285:289	arg1	determinant					246:256	the sialylated Lewisa-carbohydrate determinant	211:256	the sialylated Lewisa-carbohydrate determinant of a monoganglioside and a mucin	211:289	The monoclonal antibody-defined, tumor-associated antigen Ca 19-9, chemically identical with the sialylated Lewisa-carbohydrate determinant of a monoganglioside and a mucin, was demonstrated by radioimmunoassay to be present in large amounts as component of fucose-rich sialoglycoproteins, which had been extracted from human seminal plasma of healthy donors.
6593222	2	60	theme	prostatic	603:611	arg1	gland					613:617	the prostatic gland	599:617	the prostatic gland	599:617	The carbohydrate antigen of these glycoproteins (m greater than 205 kDa and m 115 kDa), which are presumably secreted by the prostatic gland, was absent in seminal plasma from blood-group-Lewis-negative men.
6593222	3	61	theme	active	698:703	arg1	sialyl-oligosaccharide					705:726	The Ca 19-9 active sialyl-oligosaccharide	686:726	The Ca 19-9 active sialyl-oligosaccharide	686:726	The Ca 19-9 active sialyl-oligosaccharide was cleaved from the proteins by mild alkaline borohydride treatment and was shown to chromatograph on gradient elution from DEAE-Sephadex with the fraction of monosialylated saccharide alditols (MS-SP).
6593222	1	62	from	present	335:341	arg1	amounts					352:358	large amounts	346:358	large amounts as component of fucose-rich sialoglycoproteins, which had been extracted from human seminal plasma of healthy donors	346:475	The monoclonal antibody-defined, tumor-associated antigen Ca 19-9, chemically identical with the sialylated Lewisa-carbohydrate determinant of a monoganglioside and a mucin, was demonstrated by radioimmunoassay to be present in large amounts as component of fucose-rich sialoglycoproteins, which had been extracted from human seminal plasma of healthy donors.
6593222	4	63	from	alditol	978:984	arg1	fraction					994:1001	this fraction	989:1001	this fraction	989:1001	The asialo derivative of the major saccharide alditol in this fraction was composed of L-fucose, D-galactose, N-acetyl-D-glucosamine and N-acetyl-D-galactosaminitol in the molar proportions 1:2:1:1 and chromatographed on Bio-Gel P2 according to approximately seven hexose units.
6593222	4	64	theme	hexose	1197:1202	arg1	units					1204:1208	approximately seven hexose units	1177:1208	approximately seven hexose units	1177:1208	The asialo derivative of the major saccharide alditol in this fraction was composed of L-fucose, D-galactose, N-acetyl-D-glucosamine and N-acetyl-D-galactosaminitol in the molar proportions 1:2:1:1 and chromatographed on Bio-Gel P2 according to approximately seven hexose units.
6593222	6	65	theme	derivative	1666:1675	arg1	EI					1608:1609	direct probe EI	1595:1609	direct probe EI	1595:1609	The presented data and the fragmentation pattern obtained on direct probe EI and FAB+ mass spectrometry of the permethylated asialo derivative are in accordance with the structure of a sialylated pentasaccharide alditol (formula; see text).
6593222	6	65	theme	derivative	1666:1675	arg1	spectrometry					1625:1636	FAB+ mass spectrometry	1615:1636	FAB+ mass spectrometry	1615:1636	The presented data and the fragmentation pattern obtained on direct probe EI and FAB+ mass spectrometry of the permethylated asialo derivative are in accordance with the structure of a sialylated pentasaccharide alditol (formula; see text).
6593222	3	66	theme	borohydride	775:785	arg1	treatment					787:795	mild alkaline borohydride treatment	761:795	mild alkaline borohydride treatment	761:795	The Ca 19-9 active sialyl-oligosaccharide was cleaved from the proteins by mild alkaline borohydride treatment and was shown to chromatograph on gradient elution from DEAE-Sephadex with the fraction of monosialylated saccharide alditols (MS-SP).
6593222	5	67	from	MS-SP	1283:1287	arg1	analysis					1225:1232	A methylation analysis	1211:1232	A methylation analysis	1211:1232	A methylation analysis of the sialylated saccharide alditol in fraction MS-SP, which had been purified by high-pressure liquid chromatography, revealed the presence of terminal, non-reducing L-fucose, 3-O-substituted D-galactose, 3,4 di-O-substituted N-acetyl-D-glucosamine and 3-O-substituted N-acetyl-D-galactosaminitol.
6593222	1	68	gly	sialoglycoproteins	388:405	arg1	sialoglycoproteins					388:405	fucose-rich sialoglycoproteins	376:405	fucose-rich sialoglycoproteins	376:405	The monoclonal antibody-defined, tumor-associated antigen Ca 19-9, chemically identical with the sialylated Lewisa-carbohydrate determinant of a monoganglioside and a mucin, was demonstrated by radioimmunoassay to be present in large amounts as component of fucose-rich sialoglycoproteins, which had been extracted from human seminal plasma of healthy donors.
6593222	1	69	theme	sialylated	215:224	arg1	determinant					246:256	the sialylated Lewisa-carbohydrate determinant	211:256	the sialylated Lewisa-carbohydrate determinant of a monoganglioside and a mucin	211:289	The monoclonal antibody-defined, tumor-associated antigen Ca 19-9, chemically identical with the sialylated Lewisa-carbohydrate determinant of a monoganglioside and a mucin, was demonstrated by radioimmunoassay to be present in large amounts as component of fucose-rich sialoglycoproteins, which had been extracted from human seminal plasma of healthy donors.
6593222	3	70	theme	mild	761:764	arg1	treatment					787:795	mild alkaline borohydride treatment	761:795	mild alkaline borohydride treatment	761:795	The Ca 19-9 active sialyl-oligosaccharide was cleaved from the proteins by mild alkaline borohydride treatment and was shown to chromatograph on gradient elution from DEAE-Sephadex with the fraction of monosialylated saccharide alditols (MS-SP).
6593222	6	71	dep	alditol	1746:1752	arg1	see					1764:1766	see	1764:1766	see text	1764:1771	The presented data and the fragmentation pattern obtained on direct probe EI and FAB+ mass spectrometry of the permethylated asialo derivative are in accordance with the structure of a sialylated pentasaccharide alditol (formula; see text).
6593222	2	72	theme	115	556:558	arg1	kDa					560:562	m 115 kDa	554:562	m 115 kDa	554:562	The carbohydrate antigen of these glycoproteins (m greater than 205 kDa and m 115 kDa), which are presumably secreted by the prostatic gland, was absent in seminal plasma from blood-group-Lewis-negative men.
6593222	5	73	gly	sialylated	1241:1250	arg1	alditol					1263:1269	the sialylated saccharide alditol	1237:1269	the sialylated saccharide alditol in fraction MS-SP	1237:1287	A methylation analysis of the sialylated saccharide alditol in fraction MS-SP, which had been purified by high-pressure liquid chromatography, revealed the presence of terminal, non-reducing L-fucose, 3-O-substituted D-galactose, 3,4 di-O-substituted N-acetyl-D-glucosamine and 3-O-substituted N-acetyl-D-galactosaminitol.
6593222	4	74	theme	alditol	978:984	arg1	derivative					943:952	The asialo derivative	932:952	The asialo derivative of the major saccharide alditol in this fraction	932:1001	The asialo derivative of the major saccharide alditol in this fraction was composed of L-fucose, D-galactose, N-acetyl-D-glucosamine and N-acetyl-D-galactosaminitol in the molar proportions 1:2:1:1 and chromatographed on Bio-Gel P2 according to approximately seven hexose units.
6593222	4	75	from	derivative	943:952	arg1	fraction					994:1001	this fraction	989:1001	this fraction	989:1001	The asialo derivative of the major saccharide alditol in this fraction was composed of L-fucose, D-galactose, N-acetyl-D-glucosamine and N-acetyl-D-galactosaminitol in the molar proportions 1:2:1:1 and chromatographed on Bio-Gel P2 according to approximately seven hexose units.
6593222	6	76	theme	pentasaccharide	1730:1744	arg1	alditol					1746:1752	a sialylated pentasaccharide alditol	1717:1752	a sialylated pentasaccharide alditol (formula; see text)	1717:1772	The presented data and the fragmentation pattern obtained on direct probe EI and FAB+ mass spectrometry of the permethylated asialo derivative are in accordance with the structure of a sialylated pentasaccharide alditol (formula; see text).
6593222	1	77	theme	monoclonal	122:131	arg1	19-9					179:182	The monoclonal antibody-defined, tumor-associated antigen Ca 19-9	118:182	The monoclonal antibody-defined, tumor-associated antigen Ca 19-9	118:182	The monoclonal antibody-defined, tumor-associated antigen Ca 19-9, chemically identical with the sialylated Lewisa-carbohydrate determinant of a monoganglioside and a mucin, was demonstrated by radioimmunoassay to be present in large amounts as component of fucose-rich sialoglycoproteins, which had been extracted from human seminal plasma of healthy donors.
6593222	1	77	theme	monoclonal	122:131	arg1	present					335:341	present	335:341	present	335:341	The monoclonal antibody-defined, tumor-associated antigen Ca 19-9, chemically identical with the sialylated Lewisa-carbohydrate determinant of a monoganglioside and a mucin, was demonstrated by radioimmunoassay to be present in large amounts as component of fucose-rich sialoglycoproteins, which had been extracted from human seminal plasma of healthy donors.
6593222	3	78	theme	monosialylated	888:901	arg1	alditols					914:921	monosialylated saccharide alditols	888:921	monosialylated saccharide alditols (MS-SP)	888:929	The Ca 19-9 active sialyl-oligosaccharide was cleaved from the proteins by mild alkaline borohydride treatment and was shown to chromatograph on gradient elution from DEAE-Sephadex with the fraction of monosialylated saccharide alditols (MS-SP).
6593222	3	78	theme	monosialylated	888:901	arg1	MS-SP					924:928	MS-SP	924:928	MS-SP	924:928	The Ca 19-9 active sialyl-oligosaccharide was cleaved from the proteins by mild alkaline borohydride treatment and was shown to chromatograph on gradient elution from DEAE-Sephadex with the fraction of monosialylated saccharide alditols (MS-SP).
6593222	0	79	from	donors	110:115	arg1	glycoproteins					83:95	human seminal-plasma glycoproteins	62:95	human seminal-plasma glycoproteins from healthy donors	62:115	Structure of tumor-associated carbohydrate antigen Ca 19-9 on human seminal-plasma glycoproteins from healthy donors.
6593222	6	80	theme	permethylated	1645:1657	arg1	derivative					1666:1675	the permethylated asialo derivative	1641:1675	the permethylated asialo derivative	1641:1675	The presented data and the fragmentation pattern obtained on direct probe EI and FAB+ mass spectrometry of the permethylated asialo derivative are in accordance with the structure of a sialylated pentasaccharide alditol (formula; see text).
6593222	3	81	theme	gradient	831:838	arg1	elution					840:846	gradient elution	831:846	gradient elution from DEAE-Sephadex with the fraction of monosialylated saccharide alditols (MS-SP)	831:929	The Ca 19-9 active sialyl-oligosaccharide was cleaved from the proteins by mild alkaline borohydride treatment and was shown to chromatograph on gradient elution from DEAE-Sephadex with the fraction of monosialylated saccharide alditols (MS-SP).
6593222	0	82	theme	seminal-plasma	68:81	arg1	glycoproteins					83:95	human seminal-plasma glycoproteins	62:95	human seminal-plasma glycoproteins from healthy donors	62:115	Structure of tumor-associated carbohydrate antigen Ca 19-9 on human seminal-plasma glycoproteins from healthy donors.
6593222	1	83	theme	healthy	462:468	arg1	donors					470:475	healthy donors	462:475	healthy donors	462:475	The monoclonal antibody-defined, tumor-associated antigen Ca 19-9, chemically identical with the sialylated Lewisa-carbohydrate determinant of a monoganglioside and a mucin, was demonstrated by radioimmunoassay to be present in large amounts as component of fucose-rich sialoglycoproteins, which had been extracted from human seminal plasma of healthy donors.
6593222	1	84	theme	antigen	168:174	arg1	19-9					179:182	The monoclonal antibody-defined, tumor-associated antigen Ca 19-9	118:182	The monoclonal antibody-defined, tumor-associated antigen Ca 19-9	118:182	The monoclonal antibody-defined, tumor-associated antigen Ca 19-9, chemically identical with the sialylated Lewisa-carbohydrate determinant of a monoganglioside and a mucin, was demonstrated by radioimmunoassay to be present in large amounts as component of fucose-rich sialoglycoproteins, which had been extracted from human seminal plasma of healthy donors.
6593222	1	84	theme	antigen	168:174	arg1	present					335:341	present	335:341	present	335:341	The monoclonal antibody-defined, tumor-associated antigen Ca 19-9, chemically identical with the sialylated Lewisa-carbohydrate determinant of a monoganglioside and a mucin, was demonstrated by radioimmunoassay to be present in large amounts as component of fucose-rich sialoglycoproteins, which had been extracted from human seminal plasma of healthy donors.
6593222	2	85	from	men	681:683	arg1	plasma					642:647	seminal plasma	634:647	seminal plasma from blood-group-Lewis-negative men	634:683	The carbohydrate antigen of these glycoproteins (m greater than 205 kDa and m 115 kDa), which are presumably secreted by the prostatic gland, was absent in seminal plasma from blood-group-Lewis-negative men.
6593222	2	86	theme	blood-group-Lewis-negative	654:679	arg1	men					681:683	blood-group-Lewis-negative men	654:683	blood-group-Lewis-negative men	654:683	The carbohydrate antigen of these glycoproteins (m greater than 205 kDa and m 115 kDa), which are presumably secreted by the prostatic gland, was absent in seminal plasma from blood-group-Lewis-negative men.
6593222	5	87	theme	liquid	1331:1336	arg1	chromatography					1338:1351	high-pressure liquid chromatography	1317:1351	high-pressure liquid chromatography	1317:1351	A methylation analysis of the sialylated saccharide alditol in fraction MS-SP, which had been purified by high-pressure liquid chromatography, revealed the presence of terminal, non-reducing L-fucose, 3-O-substituted D-galactose, 3,4 di-O-substituted N-acetyl-D-glucosamine and 3-O-substituted N-acetyl-D-galactosaminitol.
6593222	1	88	theme	fucose-rich	376:386	arg1	sialoglycoproteins					388:405	fucose-rich sialoglycoproteins	376:405	fucose-rich sialoglycoproteins	376:405	The monoclonal antibody-defined, tumor-associated antigen Ca 19-9, chemically identical with the sialylated Lewisa-carbohydrate determinant of a monoganglioside and a mucin, was demonstrated by radioimmunoassay to be present in large amounts as component of fucose-rich sialoglycoproteins, which had been extracted from human seminal plasma of healthy donors.
6593222	4	89	dep	proportions	1110:1120	arg1	chromatographed					1134:1148	chromatographed	1134:1148	chromatographed on Bio-Gel P2 according to approximately seven hexose units	1134:1208	The asialo derivative of the major saccharide alditol in this fraction was composed of L-fucose, D-galactose, N-acetyl-D-glucosamine and N-acetyl-D-galactosaminitol in the molar proportions 1:2:1:1 and chromatographed on Bio-Gel P2 according to approximately seven hexose units.
6593222	4	89	dep	proportions	1110:1120	arg1	1:2:1:1					1122:1128	1:2:1:1	1122:1128	1:2:1:1	1122:1128	The asialo derivative of the major saccharide alditol in this fraction was composed of L-fucose, D-galactose, N-acetyl-D-glucosamine and N-acetyl-D-galactosaminitol in the molar proportions 1:2:1:1 and chromatographed on Bio-Gel P2 according to approximately seven hexose units.
6593222	3	90	theme	alditols	914:921	arg1	fraction					876:883	the fraction	872:883	the fraction of monosialylated saccharide alditols (MS-SP)	872:929	The Ca 19-9 active sialyl-oligosaccharide was cleaved from the proteins by mild alkaline borohydride treatment and was shown to chromatograph on gradient elution from DEAE-Sephadex with the fraction of monosialylated saccharide alditols (MS-SP).
6593222	4	91	theme	saccharide	967:976	arg1	alditol					978:984	the major saccharide alditol	957:984	the major saccharide alditol in this fraction	957:1001	The asialo derivative of the major saccharide alditol in this fraction was composed of L-fucose, D-galactose, N-acetyl-D-glucosamine and N-acetyl-D-galactosaminitol in the molar proportions 1:2:1:1 and chromatographed on Bio-Gel P2 according to approximately seven hexose units.
6593222	5	92	theme	L-fucose	1402:1409	arg1	presence					1367:1374	the presence	1363:1374	the presence of terminal, non-reducing L-fucose, 3-O-substituted D-galactose, 3,4 di-O-substituted N-acetyl-D-glucosamine and 3-O-substituted N-acetyl-D-galactosaminitol	1363:1531	A methylation analysis of the sialylated saccharide alditol in fraction MS-SP, which had been purified by high-pressure liquid chromatography, revealed the presence of terminal, non-reducing L-fucose, 3-O-substituted D-galactose, 3,4 di-O-substituted N-acetyl-D-glucosamine and 3-O-substituted N-acetyl-D-galactosaminitol.
6593222	0	93	gly	glycoproteins	83:95	arg1	glycoproteins					83:95	human seminal-plasma glycoproteins	62:95	human seminal-plasma glycoproteins from healthy donors	62:115	Structure of tumor-associated carbohydrate antigen Ca 19-9 on human seminal-plasma glycoproteins from healthy donors.
6593222	3	94	gly	monosialylated	888:901	arg1	alditols					914:921	monosialylated saccharide alditols	888:921	monosialylated saccharide alditols (MS-SP)	888:929	The Ca 19-9 active sialyl-oligosaccharide was cleaved from the proteins by mild alkaline borohydride treatment and was shown to chromatograph on gradient elution from DEAE-Sephadex with the fraction of monosialylated saccharide alditols (MS-SP).
6593222	3	94	gly	monosialylated	888:901	arg1	MS-SP					924:928	MS-SP	924:928	MS-SP	924:928	The Ca 19-9 active sialyl-oligosaccharide was cleaved from the proteins by mild alkaline borohydride treatment and was shown to chromatograph on gradient elution from DEAE-Sephadex with the fraction of monosialylated saccharide alditols (MS-SP).
6593222	1	95	dep	antibody-defined	133:148	arg1	tumor-associated					151:166	tumor-associated	151:166	tumor-associated	151:166	The monoclonal antibody-defined, tumor-associated antigen Ca 19-9, chemically identical with the sialylated Lewisa-carbohydrate determinant of a monoganglioside and a mucin, was demonstrated by radioimmunoassay to be present in large amounts as component of fucose-rich sialoglycoproteins, which had been extracted from human seminal plasma of healthy donors.
6593222	5	96	theme	3-O-substituted	1412:1426	arg1	L-fucose					1402:1409	terminal, non-reducing L-fucose	1379:1409	L-fucose	1402:1409	A methylation analysis of the sialylated saccharide alditol in fraction MS-SP, which had been purified by high-pressure liquid chromatography, revealed the presence of terminal, non-reducing L-fucose, 3-O-substituted D-galactose, 3,4 di-O-substituted N-acetyl-D-glucosamine and 3-O-substituted N-acetyl-D-galactosaminitol.
6593222	5	96	theme	3-O-substituted	1412:1426	arg1	D-galactose					1428:1438	3-O-substituted D-galactose	1412:1438	3-O-substituted D-galactose	1412:1438	A methylation analysis of the sialylated saccharide alditol in fraction MS-SP, which had been purified by high-pressure liquid chromatography, revealed the presence of terminal, non-reducing L-fucose, 3-O-substituted D-galactose, 3,4 di-O-substituted N-acetyl-D-glucosamine and 3-O-substituted N-acetyl-D-galactosaminitol.
6593222	0	97	theme	carbohydrate	30:41	arg1	19-9					54:57	tumor-associated carbohydrate antigen Ca 19-9	13:57	tumor-associated carbohydrate antigen Ca 19-9	13:57	Structure of tumor-associated carbohydrate antigen Ca 19-9 on human seminal-plasma glycoproteins from healthy donors.
6593222	5	98	theme	sialylated	1241:1250	arg1	alditol					1263:1269	the sialylated saccharide alditol	1237:1269	the sialylated saccharide alditol in fraction MS-SP	1237:1287	A methylation analysis of the sialylated saccharide alditol in fraction MS-SP, which had been purified by high-pressure liquid chromatography, revealed the presence of terminal, non-reducing L-fucose, 3-O-substituted D-galactose, 3,4 di-O-substituted N-acetyl-D-glucosamine and 3-O-substituted N-acetyl-D-galactosaminitol.
6593222	0	99	theme	Ca	51:52	arg1	19-9					54:57	tumor-associated carbohydrate antigen Ca 19-9	13:57	tumor-associated carbohydrate antigen Ca 19-9	13:57	Structure of tumor-associated carbohydrate antigen Ca 19-9 on human seminal-plasma glycoproteins from healthy donors.
6593222	4	100	from	N-acetyl-D-glucosamine	1042:1063	arg1	proportions					1110:1120	the molar proportions	1100:1120	the molar proportions 1:2:1:1 and chromatographed on Bio-Gel P2 according to approximately seven hexose units	1100:1208	The asialo derivative of the major saccharide alditol in this fraction was composed of L-fucose, D-galactose, N-acetyl-D-glucosamine and N-acetyl-D-galactosaminitol in the molar proportions 1:2:1:1 and chromatographed on Bio-Gel P2 according to approximately seven hexose units.
6593222	6	101	theme	presented	1538:1546	arg1	data					1548:1551	The presented data	1534:1551	The presented data	1534:1551	The presented data and the fragmentation pattern obtained on direct probe EI and FAB+ mass spectrometry of the permethylated asialo derivative are in accordance with the structure of a sialylated pentasaccharide alditol (formula; see text).
6593222	5	102	theme	methylation	1213:1223	arg1	analysis					1225:1232	A methylation analysis	1211:1232	A methylation analysis	1211:1232	A methylation analysis of the sialylated saccharide alditol in fraction MS-SP, which had been purified by high-pressure liquid chromatography, revealed the presence of terminal, non-reducing L-fucose, 3-O-substituted D-galactose, 3,4 di-O-substituted N-acetyl-D-glucosamine and 3-O-substituted N-acetyl-D-galactosaminitol.
6593222	2	103	dep	m	527:527	arg1	kDa					546:548	greater than 205 kDa	529:548	greater than 205 kDa	529:548	The carbohydrate antigen of these glycoproteins (m greater than 205 kDa and m 115 kDa), which are presumably secreted by the prostatic gland, was absent in seminal plasma from blood-group-Lewis-negative men.
6593222	2	103	dep	m	527:527	arg1	kDa					560:562	m 115 kDa	554:562	m 115 kDa	554:562	The carbohydrate antigen of these glycoproteins (m greater than 205 kDa and m 115 kDa), which are presumably secreted by the prostatic gland, was absent in seminal plasma from blood-group-Lewis-negative men.
6593222	4	104	from	L-fucose	1019:1026	arg1	proportions					1110:1120	the molar proportions	1100:1120	the molar proportions 1:2:1:1 and chromatographed on Bio-Gel P2 according to approximately seven hexose units	1100:1208	The asialo derivative of the major saccharide alditol in this fraction was composed of L-fucose, D-galactose, N-acetyl-D-glucosamine and N-acetyl-D-galactosaminitol in the molar proportions 1:2:1:1 and chromatographed on Bio-Gel P2 according to approximately seven hexose units.
6593222	6	105	theme	FAB+	1615:1618	arg1	spectrometry					1625:1636	FAB+ mass spectrometry	1615:1636	FAB+ mass spectrometry	1615:1636	The presented data and the fragmentation pattern obtained on direct probe EI and FAB+ mass spectrometry of the permethylated asialo derivative are in accordance with the structure of a sialylated pentasaccharide alditol (formula; see text).
6593222	1	106	theme	monoganglioside	263:277	arg1	determinant					246:256	the sialylated Lewisa-carbohydrate determinant	211:256	the sialylated Lewisa-carbohydrate determinant of a monoganglioside and a mucin	211:289	The monoclonal antibody-defined, tumor-associated antigen Ca 19-9, chemically identical with the sialylated Lewisa-carbohydrate determinant of a monoganglioside and a mucin, was demonstrated by radioimmunoassay to be present in large amounts as component of fucose-rich sialoglycoproteins, which had been extracted from human seminal plasma of healthy donors.
6593222	5	107	theme	di-O-substituted	1445:1460	arg1	N-acetyl-D-glucosamine					1462:1483	3,4 di-O-substituted N-acetyl-D-glucosamine	1441:1483	3,4 di-O-substituted N-acetyl-D-glucosamine	1441:1483	A methylation analysis of the sialylated saccharide alditol in fraction MS-SP, which had been purified by high-pressure liquid chromatography, revealed the presence of terminal, non-reducing L-fucose, 3-O-substituted D-galactose, 3,4 di-O-substituted N-acetyl-D-glucosamine and 3-O-substituted N-acetyl-D-galactosaminitol.
6593222	5	107	theme	di-O-substituted	1445:1460	arg1	L-fucose					1402:1409	terminal, non-reducing L-fucose	1379:1409	L-fucose	1402:1409	A methylation analysis of the sialylated saccharide alditol in fraction MS-SP, which had been purified by high-pressure liquid chromatography, revealed the presence of terminal, non-reducing L-fucose, 3-O-substituted D-galactose, 3,4 di-O-substituted N-acetyl-D-glucosamine and 3-O-substituted N-acetyl-D-galactosaminitol.
6593222	4	108	from	fraction	994:1001	arg1	derivative					943:952	The asialo derivative	932:952	The asialo derivative of the major saccharide alditol in this fraction	932:1001	The asialo derivative of the major saccharide alditol in this fraction was composed of L-fucose, D-galactose, N-acetyl-D-glucosamine and N-acetyl-D-galactosaminitol in the molar proportions 1:2:1:1 and chromatographed on Bio-Gel P2 according to approximately seven hexose units.
33618028	13	0	theme	intact	1832:1837	arg1	profile					1854:1860	the intact PSA proteoform profile	1828:1860	the intact PSA proteoform profile	1828:1860	However, a comprehensive analysis of the intact PSA proteoform profile is still lacking.
33618028	6	1	theme	electrophoresis-electrospray	826:853	arg1	spectrometry					871:882	capillary electrophoresis-electrospray ionization-mass spectrometry	816:882	capillary electrophoresis-electrospray ionization-mass spectrometry	816:882	For this purpose, we developed an intact protein assay to analyze PSA by capillary electrophoresis-electrospray ionization-mass spectrometry after affinity purification from patients' urine.
33618028	12	2	theme	current	1773:1779	arg1	test					1785:1788	the current PSA test	1769:1788	the current PSA test	1769:1788	SIGNIFICANCE: The detection of clinically relevant prostate cancer requires a more specific and sensitive biomarker and, in this case, several PSA proteoforms may be able to aid or improve the current PSA test.
33618028	12	3	from	case	1709:1712	arg1	able					1746:1749	able	1746:1749	able	1746:1749	SIGNIFICANCE: The detection of clinically relevant prostate cancer requires a more specific and sensitive biomarker and, in this case, several PSA proteoforms may be able to aid or improve the current PSA test.
33618028	4	4	theme	prostate	604:611	arg1	cancer					613:618	prostate cancer	604:618	prostate cancer	604:618	In order to improve early detection and diagnosis, several studies have investigated whether different PSA proteoforms are correlated to prostate cancer.
33618028	11	5	theme	urinary	1567:1573	arg1	PSA					1575:1577	urinary PSA	1567:1577	urinary PSA	1567:1577	This combined approach revealed complimentary information on both levels, demonstrating the benefit of using two orthogonal techniques to provide a thorough profile of urinary PSA.
33618028	14	6	from	present	1924:1930	arg1	urine					1935:1939	urine	1935:1939	urine	1935:1939	This study investigated the PSA proteoforms present in urine and, in particular, determined the relative contribution of cleaved PSA and non-cleaved PSA forms to the total glycosylation profile.
33618028	8	7	theme	di-	1023:1025	arg1	N-glycans					1066:1074	tri-, di-, mono- and non-sialylated complex-type N-glycans	1017:1074	tri-, di-, mono- and non-sialylated complex-type N-glycans	1017:1074	In regard to glycosylation, tri-, di-, mono- and non-sialylated complex-type N-glycans were found on non-cleaved PSA, as well as the non-glycosylated variant.
33618028	16	8	gly	glycosylation	2206:2218	arg1	approach					2253:2260	a bottom-up approach	2241:2260	a bottom-up approach to provide complementary information	2241:2297	Furthermore, its glycosylation was also assessed in a bottom-up approach to provide complementary information.
33618028	13	9	theme	comprehensive	1802:1814	arg1	analysis					1816:1823	a comprehensive analysis	1800:1823	a comprehensive analysis of the intact PSA proteoform profile	1800:1860	However, a comprehensive analysis of the intact PSA proteoform profile is still lacking.
33618028	2	10	theme	elevated	285:292	arg1	concentrations					300:313	elevated serum concentrations	285:313	elevated serum concentrations of prostate-specific antigen (PSA)	285:348	The current diagnostic approach uses elevated serum concentrations of prostate-specific antigen (PSA) as an indicator of risk.
33618028	2	10	theme	elevated	285:292	arg1	indicator					356:364	an indicator	353:364	an indicator of risk	353:372	The current diagnostic approach uses elevated serum concentrations of prostate-specific antigen (PSA) as an indicator of risk.
33618028	14	11	from	urine	1935:1939	arg1	present					1924:1930	present	1924:1930	present	1924:1930	This study investigated the PSA proteoforms present in urine and, in particular, determined the relative contribution of cleaved PSA and non-cleaved PSA forms to the total glycosylation profile.
33618028	11	12	theme	combined	1404:1411	arg1	approach					1413:1420	This combined approach	1399:1420	This combined approach	1399:1420	This combined approach revealed complimentary information on both levels, demonstrating the benefit of using two orthogonal techniques to provide a thorough profile of urinary PSA.
33618028	8	13	theme	mono-	1028:1032	arg1	N-glycans					1066:1074	tri-, di-, mono- and non-sialylated complex-type N-glycans	1017:1074	tri-, di-, mono- and non-sialylated complex-type N-glycans	1017:1074	In regard to glycosylation, tri-, di-, mono- and non-sialylated complex-type N-glycans were found on non-cleaved PSA, as well as the non-glycosylated variant.
33618028	8	14	located	found	1081:1085	arg2	N-glycans					1066:1074	tri-, di-, mono- and non-sialylated complex-type N-glycans	1017:1074	tri-, di-, mono- and non-sialylated complex-type N-glycans	1017:1074	In regard to glycosylation, tri-, di-, mono- and non-sialylated complex-type N-glycans were found on non-cleaved PSA, as well as the non-glycosylated variant.
33618028	8	14	located	found	1081:1085	arg1	variant					1139:1145	the non-glycosylated variant	1118:1145	the non-glycosylated variant	1118:1145	In regard to glycosylation, tri-, di-, mono- and non-sialylated complex-type N-glycans were found on non-cleaved PSA, as well as the non-glycosylated variant.
33618028	8	14	located	found	1081:1085	arg1	regard					992:997	regard	992:997	regard to glycosylation	992:1014	In regard to glycosylation, tri-, di-, mono- and non-sialylated complex-type N-glycans were found on non-cleaved PSA, as well as the non-glycosylated variant.
33618028	8	14	located	found	1081:1085	arg1	PSA					1102:1104	non-cleaved PSA	1090:1104	non-cleaved PSA	1090:1104	In regard to glycosylation, tri-, di-, mono- and non-sialylated complex-type N-glycans were found on non-cleaved PSA, as well as the non-glycosylated variant.
33618028	9	15	theme	inter-day	1241:1249	arg1	variability					1251:1261	an inter-day variability	1238:1261	an inter-day variability of 15%	1238:1268	The performance of the intact protein assay was assessed using a pooled sample, obtaining an inter-day variability of 15%.
33618028	1	16	theme	patients	199:206	arg1	cancers					239:245	missing significant cancers	219:245	the overdiagnosis and overtreatment of patients as well as missing significant cancers	160:245	Early detection of prostate cancer may lead to the overdiagnosis and overtreatment of patients as well as missing significant cancers.
33618028	1	16	theme	patients	199:206	arg1	overtreatment					182:194	overtreatment	182:194	overtreatment	182:194	Early detection of prostate cancer may lead to the overdiagnosis and overtreatment of patients as well as missing significant cancers.
33618028	1	16	theme	patients	199:206	arg1	overdiagnosis					164:176	overdiagnosis	164:176	overdiagnosis	164:176	Early detection of prostate cancer may lead to the overdiagnosis and overtreatment of patients as well as missing significant cancers.
33618028	8	17	theme	non-sialylated	1038:1051	arg1	N-glycans					1066:1074	tri-, di-, mono- and non-sialylated complex-type N-glycans	1017:1074	tri-, di-, mono- and non-sialylated complex-type N-glycans	1017:1074	In regard to glycosylation, tri-, di-, mono- and non-sialylated complex-type N-glycans were found on non-cleaved PSA, as well as the non-glycosylated variant.
33618028	2	18	theme	prostate-specific	318:334	arg1	antigen					336:342	prostate-specific antigen	318:342	prostate-specific antigen (PSA)	318:348	The current diagnostic approach uses elevated serum concentrations of prostate-specific antigen (PSA) as an indicator of risk.
33618028	2	18	theme	prostate-specific	318:334	arg1	PSA					345:347	PSA	345:347	PSA	345:347	The current diagnostic approach uses elevated serum concentrations of prostate-specific antigen (PSA) as an indicator of risk.
33618028	9	19	theme	%	1268:1268	arg1	variability					1251:1261	an inter-day variability	1238:1261	an inter-day variability of 15%	1238:1268	The performance of the intact protein assay was assessed using a pooled sample, obtaining an inter-day variability of 15%.
33618028	1	20	theme	missing	219:225	arg1	cancers					239:245	missing significant cancers	219:245	the overdiagnosis and overtreatment of patients as well as missing significant cancers	160:245	Early detection of prostate cancer may lead to the overdiagnosis and overtreatment of patients as well as missing significant cancers.
33618028	5	21	theme	PSA	700:702	arg1	proteoforms					704:714	PSA proteoforms	700:714	PSA proteoforms from biofluids	700:729	Until now, studies and methodologies for the comprehensive characterization of PSA proteoforms from biofluids are scarce.
33618028	1	22	theme	prostate	132:139	arg1	cancer					141:146	prostate cancer	132:146	prostate cancer	132:146	Early detection of prostate cancer may lead to the overdiagnosis and overtreatment of patients as well as missing significant cancers.
33618028	9	23	dep	sample	1220:1225	arg1	obtaining					1228:1236	obtaining	1228:1236	obtaining an inter-day variability of 15%	1228:1268	The performance of the intact protein assay was assessed using a pooled sample, obtaining an inter-day variability of 15%.
33618028	12	24	theme	prostate	1631:1638	arg1	cancer					1640:1645	clinically relevant prostate cancer	1611:1645	clinically relevant prostate cancer	1611:1645	SIGNIFICANCE: The detection of clinically relevant prostate cancer requires a more specific and sensitive biomarker and, in this case, several PSA proteoforms may be able to aid or improve the current PSA test.
33618028	17	25	theme	important	2336:2344	arg1	basis					2346:2350	an important basis	2333:2350	an important basis for future characterization and biomarker studies	2333:2400	Overall, these results represent an important basis for future characterization and biomarker studies.
33618028	6	26	theme	capillary	816:824	arg1	spectrometry					871:882	capillary electrophoresis-electrospray ionization-mass spectrometry	816:882	capillary electrophoresis-electrospray ionization-mass spectrometry	816:882	For this purpose, we developed an intact protein assay to analyze PSA by capillary electrophoresis-electrospray ionization-mass spectrometry after affinity purification from patients' urine.
33618028	16	27	theme	complementary	2273:2285	arg1	information					2287:2297	complementary information	2273:2297	complementary information	2273:2297	Furthermore, its glycosylation was also assessed in a bottom-up approach to provide complementary information.
33618028	0	28	theme	capillary	66:74	arg1	electrophoresis					76:90	capillary electrophoresis	66:90	capillary electrophoresis	66:90	Profiling the proteoforms of urinary prostate-specific antigen by capillary electrophoresis - mass spectrometry.
33618028	2	29	theme	current	252:258	arg1	approach					271:278	The current diagnostic approach	248:278	The current diagnostic approach	248:278	The current diagnostic approach uses elevated serum concentrations of prostate-specific antigen (PSA) as an indicator of risk.
33618028	12	30	theme	several	1715:1721	arg1	proteoforms					1727:1737	several PSA proteoforms	1715:1737	several PSA proteoforms	1715:1737	SIGNIFICANCE: The detection of clinically relevant prostate cancer requires a more specific and sensitive biomarker and, in this case, several PSA proteoforms may be able to aid or improve the current PSA test.
33618028	10	31	gly	glycopeptide	1375:1386	arg2	glycopeptide					1375:1386	glycopeptide analysis	1375:1395	glycopeptide analysis	1375:1395	Furthermore, urinary patient samples were analyzed by intact protein analysis and a bottom-up approach (glycopeptide analysis).
33618028	10	32	theme	urinary	1284:1290	arg1	samples					1300:1306	urinary patient samples	1284:1306	urinary patient samples	1284:1306	Furthermore, urinary patient samples were analyzed by intact protein analysis and a bottom-up approach (glycopeptide analysis).
33618028	11	33	theme	thorough	1547:1554	arg1	profile					1556:1562	a thorough profile	1545:1562	a thorough profile of urinary PSA	1545:1577	This combined approach revealed complimentary information on both levels, demonstrating the benefit of using two orthogonal techniques to provide a thorough profile of urinary PSA.
33618028	10	34	theme	protein	1332:1338	arg1	analysis					1340:1347	intact protein analysis	1325:1347	intact protein analysis	1325:1347	Furthermore, urinary patient samples were analyzed by intact protein analysis and a bottom-up approach (glycopeptide analysis).
33618028	16	35	theme	bottom-up	2243:2251	arg1	approach					2253:2260	a bottom-up approach	2241:2260	a bottom-up approach to provide complementary information	2241:2297	Furthermore, its glycosylation was also assessed in a bottom-up approach to provide complementary information.
33618028	3	36	theme	poor	433:436	arg1	specificity					438:448	poor specificity	433:448	poor specificity	433:448	However, this test has been widely criticized as it shows poor specificity and sensitivity.
33618028	8	37	theme	non-cleaved	1090:1100	arg1	PSA					1102:1104	non-cleaved PSA	1090:1104	non-cleaved PSA	1090:1104	In regard to glycosylation, tri-, di-, mono- and non-sialylated complex-type N-glycans were found on non-cleaved PSA, as well as the non-glycosylated variant.
33618028	8	38	gly	non-glycosylated	1122:1137	arg1	variant					1139:1145	the non-glycosylated variant	1118:1145	the non-glycosylated variant	1118:1145	In regard to glycosylation, tri-, di-, mono- and non-sialylated complex-type N-glycans were found on non-cleaved PSA, as well as the non-glycosylated variant.
33618028	7	39	theme	cleavage	970:977	arg1	variants					979:986	six proteolytic cleavage variants	954:986	six proteolytic cleavage variants	954:986	Here, we determined six proteolytic cleavage variants.
33618028	14	40	theme	cleaved	2001:2007	arg1	PSA					2009:2011	cleaved PSA	2001:2011	cleaved PSA	2001:2011	This study investigated the PSA proteoforms present in urine and, in particular, determined the relative contribution of cleaved PSA and non-cleaved PSA forms to the total glycosylation profile.
33618028	12	41	theme	sensitive	1676:1684	arg1	biomarker					1686:1694	a more specific and sensitive biomarker	1656:1694	a more specific and sensitive biomarker	1656:1694	SIGNIFICANCE: The detection of clinically relevant prostate cancer requires a more specific and sensitive biomarker and, in this case, several PSA proteoforms may be able to aid or improve the current PSA test.
33618028	13	42	theme	proteoform	1843:1852	arg1	profile					1854:1860	the intact PSA proteoform profile	1828:1860	the intact PSA proteoform profile	1828:1860	However, a comprehensive analysis of the intact PSA proteoform profile is still lacking.
33618028	4	43	theme	PSA	570:572	arg1	proteoforms					574:584	different PSA proteoforms	560:584	different PSA proteoforms	560:584	In order to improve early detection and diagnosis, several studies have investigated whether different PSA proteoforms are correlated to prostate cancer.
33618028	10	44	theme	intact	1325:1330	arg1	analysis					1340:1347	intact protein analysis	1325:1347	intact protein analysis	1325:1347	Furthermore, urinary patient samples were analyzed by intact protein analysis and a bottom-up approach (glycopeptide analysis).
33618028	0	45	theme	urinary	29:35	arg1	antigen					55:61	urinary prostate-specific antigen	29:61	urinary prostate-specific antigen	29:61	Profiling the proteoforms of urinary prostate-specific antigen by capillary electrophoresis - mass spectrometry.
33618028	15	46	theme	sample	2136:2141	arg1	treatment					2143:2151	further sample treatment	2128:2151	further sample treatment	2128:2151	Importantly, intact protein analysis did not require further sample treatment before being measured by CE-ESI-MS.
33618028	4	47	theme	several	518:524	arg1	studies					526:532	several studies	518:532	several studies	518:532	In order to improve early detection and diagnosis, several studies have investigated whether different PSA proteoforms are correlated to prostate cancer.
33618028	14	48	theme	glycosylation	2052:2064	arg1	profile					2066:2072	the total glycosylation profile	2042:2072	the total glycosylation profile	2042:2072	This study investigated the PSA proteoforms present in urine and, in particular, determined the relative contribution of cleaved PSA and non-cleaved PSA forms to the total glycosylation profile.
33618028	0	49	theme	antigen	55:61	arg1	proteoforms					14:24	the proteoforms	10:24	the proteoforms of urinary prostate-specific antigen	10:61	Profiling the proteoforms of urinary prostate-specific antigen by capillary electrophoresis - mass spectrometry.
33618028	6	50	theme	affinity	890:897	arg1	purification					899:910	affinity purification	890:910	affinity purification from patients' urine	890:931	For this purpose, we developed an intact protein assay to analyze PSA by capillary electrophoresis-electrospray ionization-mass spectrometry after affinity purification from patients' urine.
33618028	6	51	dep	patients	917:924	arg1	urine					927:931	urine	927:931	patients' urine	917:931	For this purpose, we developed an intact protein assay to analyze PSA by capillary electrophoresis-electrospray ionization-mass spectrometry after affinity purification from patients' urine.
33618028	9	52	theme	protein	1178:1184	arg1	assay					1186:1190	the intact protein assay	1167:1190	the intact protein assay	1167:1190	The performance of the intact protein assay was assessed using a pooled sample, obtaining an inter-day variability of 15%.
33618028	7	53	theme	proteolytic	958:968	arg1	variants					979:986	six proteolytic cleavage variants	954:986	six proteolytic cleavage variants	954:986	Here, we determined six proteolytic cleavage variants.
33618028	1	54	theme	significant	227:237	arg1	cancers					239:245	missing significant cancers	219:245	the overdiagnosis and overtreatment of patients as well as missing significant cancers	160:245	Early detection of prostate cancer may lead to the overdiagnosis and overtreatment of patients as well as missing significant cancers.
33618028	15	55	theme	protein	2095:2101	arg1	analysis					2103:2110	intact protein analysis	2088:2110	intact protein analysis	2088:2110	Importantly, intact protein analysis did not require further sample treatment before being measured by CE-ESI-MS.
33618028	17	56	theme	biomarker	2384:2392	arg1	studies					2394:2400	biomarker studies	2384:2400	biomarker studies	2384:2400	Overall, these results represent an important basis for future characterization and biomarker studies.
33618028	10	57	theme	glycopeptide	1375:1386	arg1	approach					1365:1372	a bottom-up approach	1353:1372	a bottom-up approach (glycopeptide analysis)	1353:1396	Furthermore, urinary patient samples were analyzed by intact protein analysis and a bottom-up approach (glycopeptide analysis).
33618028	10	57	theme	glycopeptide	1375:1386	arg1	analysis					1388:1395	glycopeptide analysis	1375:1395	glycopeptide analysis	1375:1395	Furthermore, urinary patient samples were analyzed by intact protein analysis and a bottom-up approach (glycopeptide analysis).
33618028	2	58	theme	risk	369:372	arg1	concentrations					300:313	elevated serum concentrations	285:313	elevated serum concentrations of prostate-specific antigen (PSA)	285:348	The current diagnostic approach uses elevated serum concentrations of prostate-specific antigen (PSA) as an indicator of risk.
33618028	2	58	theme	risk	369:372	arg1	indicator					356:364	an indicator	353:364	an indicator of risk	353:372	The current diagnostic approach uses elevated serum concentrations of prostate-specific antigen (PSA) as an indicator of risk.
33618028	12	59	theme	PSA	1781:1783	arg1	test					1785:1788	the current PSA test	1769:1788	the current PSA test	1769:1788	SIGNIFICANCE: The detection of clinically relevant prostate cancer requires a more specific and sensitive biomarker and, in this case, several PSA proteoforms may be able to aid or improve the current PSA test.
33618028	5	60	theme	comprehensive	666:678	arg1	characterization					680:695	the comprehensive characterization	662:695	the comprehensive characterization of PSA proteoforms from biofluids	662:729	Until now, studies and methodologies for the comprehensive characterization of PSA proteoforms from biofluids are scarce.
33618028	9	61	theme	pooled	1213:1218	arg1	sample					1220:1225	a pooled sample	1211:1225	a pooled sample	1211:1225	The performance of the intact protein assay was assessed using a pooled sample, obtaining an inter-day variability of 15%.
33618028	5	62	from	biofluids	721:729	arg1	proteoforms					704:714	PSA proteoforms	700:714	PSA proteoforms from biofluids	700:729	Until now, studies and methodologies for the comprehensive characterization of PSA proteoforms from biofluids are scarce.
33618028	5	62	from	biofluids	721:729	arg1	characterization					680:695	the comprehensive characterization	662:695	the comprehensive characterization of PSA proteoforms from biofluids	662:729	Until now, studies and methodologies for the comprehensive characterization of PSA proteoforms from biofluids are scarce.
33618028	14	63	attach	present	1924:1930	arg2	proteoforms					1912:1922	the PSA proteoforms	1904:1922	the PSA proteoforms present in urine	1904:1939	This study investigated the PSA proteoforms present in urine and, in particular, determined the relative contribution of cleaved PSA and non-cleaved PSA forms to the total glycosylation profile.
33618028	14	63	attach	present	1924:1930	arg1	urine					1935:1939	urine	1935:1939	urine	1935:1939	This study investigated the PSA proteoforms present in urine and, in particular, determined the relative contribution of cleaved PSA and non-cleaved PSA forms to the total glycosylation profile.
33618028	11	64	theme	complimentary	1431:1443	arg1	information					1445:1455	complimentary information	1431:1455	complimentary information on both levels	1431:1470	This combined approach revealed complimentary information on both levels, demonstrating the benefit of using two orthogonal techniques to provide a thorough profile of urinary PSA.
33618028	11	65	theme	PSA	1575:1577	arg1	profile					1556:1562	a thorough profile	1545:1562	a thorough profile of urinary PSA	1545:1577	This combined approach revealed complimentary information on both levels, demonstrating the benefit of using two orthogonal techniques to provide a thorough profile of urinary PSA.
33618028	2	66	theme	serum	294:298	arg1	concentrations					300:313	elevated serum concentrations	285:313	elevated serum concentrations of prostate-specific antigen (PSA)	285:348	The current diagnostic approach uses elevated serum concentrations of prostate-specific antigen (PSA) as an indicator of risk.
33618028	2	66	theme	serum	294:298	arg1	indicator					356:364	an indicator	353:364	an indicator of risk	353:372	The current diagnostic approach uses elevated serum concentrations of prostate-specific antigen (PSA) as an indicator of risk.
33618028	14	67	theme	present	1924:1930	arg1	proteoforms					1912:1922	the PSA proteoforms	1904:1922	the PSA proteoforms present in urine	1904:1939	This study investigated the PSA proteoforms present in urine and, in particular, determined the relative contribution of cleaved PSA and non-cleaved PSA forms to the total glycosylation profile.
33618028	8	68	theme	complex-type	1053:1064	arg1	N-glycans					1066:1074	tri-, di-, mono- and non-sialylated complex-type N-glycans	1017:1074	tri-, di-, mono- and non-sialylated complex-type N-glycans	1017:1074	In regard to glycosylation, tri-, di-, mono- and non-sialylated complex-type N-glycans were found on non-cleaved PSA, as well as the non-glycosylated variant.
33618028	6	69	theme	protein	784:790	arg1	assay					792:796	an intact protein assay	774:796	an intact protein assay to analyze PSA by capillary electrophoresis-electrospray ionization-mass spectrometry after affinity purification from patients' urine	774:931	For this purpose, we developed an intact protein assay to analyze PSA by capillary electrophoresis-electrospray ionization-mass spectrometry after affinity purification from patients' urine.
33618028	2	70	theme	antigen	336:342	arg1	concentrations					300:313	elevated serum concentrations	285:313	elevated serum concentrations of prostate-specific antigen (PSA)	285:348	The current diagnostic approach uses elevated serum concentrations of prostate-specific antigen (PSA) as an indicator of risk.
33618028	2	70	theme	antigen	336:342	arg1	indicator					356:364	an indicator	353:364	an indicator of risk	353:372	The current diagnostic approach uses elevated serum concentrations of prostate-specific antigen (PSA) as an indicator of risk.
33618028	14	71	theme	PSA	1908:1910	arg1	proteoforms					1912:1922	the PSA proteoforms	1904:1922	the PSA proteoforms present in urine	1904:1939	This study investigated the PSA proteoforms present in urine and, in particular, determined the relative contribution of cleaved PSA and non-cleaved PSA forms to the total glycosylation profile.
33618028	12	72	theme	specific	1663:1670	arg1	biomarker					1686:1694	a more specific and sensitive biomarker	1656:1694	a more specific and sensitive biomarker	1656:1694	SIGNIFICANCE: The detection of clinically relevant prostate cancer requires a more specific and sensitive biomarker and, in this case, several PSA proteoforms may be able to aid or improve the current PSA test.
33618028	9	73	theme	intact	1171:1176	arg1	assay					1186:1190	the intact protein assay	1167:1190	the intact protein assay	1167:1190	The performance of the intact protein assay was assessed using a pooled sample, obtaining an inter-day variability of 15%.
33618028	11	74	from	information	1445:1455	arg1	levels					1465:1470	both levels	1460:1470	both levels	1460:1470	This combined approach revealed complimentary information on both levels, demonstrating the benefit of using two orthogonal techniques to provide a thorough profile of urinary PSA.
33618028	12	75	theme	relevant	1622:1629	arg1	cancer					1640:1645	clinically relevant prostate cancer	1611:1645	clinically relevant prostate cancer	1611:1645	SIGNIFICANCE: The detection of clinically relevant prostate cancer requires a more specific and sensitive biomarker and, in this case, several PSA proteoforms may be able to aid or improve the current PSA test.
33618028	12	76	from	able	1746:1749	arg1	case					1709:1712	this case	1704:1712	this case	1704:1712	SIGNIFICANCE: The detection of clinically relevant prostate cancer requires a more specific and sensitive biomarker and, in this case, several PSA proteoforms may be able to aid or improve the current PSA test.
33618028	8	77	gly	non-sialylated	1038:1051	arg1	N-glycans					1066:1074	tri-, di-, mono- and non-sialylated complex-type N-glycans	1017:1074	tri-, di-, mono- and non-sialylated complex-type N-glycans	1017:1074	In regard to glycosylation, tri-, di-, mono- and non-sialylated complex-type N-glycans were found on non-cleaved PSA, as well as the non-glycosylated variant.
33618028	12	78	theme	cancer	1640:1645	arg1	detection					1598:1606	The detection	1594:1606	The detection of clinically relevant prostate cancer	1594:1645	SIGNIFICANCE: The detection of clinically relevant prostate cancer requires a more specific and sensitive biomarker and, in this case, several PSA proteoforms may be able to aid or improve the current PSA test.
33618028	5	79	theme	proteoforms	704:714	arg1	characterization					680:695	the comprehensive characterization	662:695	the comprehensive characterization of PSA proteoforms from biofluids	662:729	Until now, studies and methodologies for the comprehensive characterization of PSA proteoforms from biofluids are scarce.
33618028	1	80	theme	cancer	141:146	arg1	detection					119:127	Early detection	113:127	Early detection of prostate cancer	113:146	Early detection of prostate cancer may lead to the overdiagnosis and overtreatment of patients as well as missing significant cancers.
33618028	11	81	theme	orthogonal	1512:1521	arg1	techniques					1523:1532	two orthogonal techniques	1508:1532	two orthogonal techniques	1508:1532	This combined approach revealed complimentary information on both levels, demonstrating the benefit of using two orthogonal techniques to provide a thorough profile of urinary PSA.
33618028	2	82	theme	diagnostic	260:269	arg1	approach					271:278	The current diagnostic approach	248:278	The current diagnostic approach	248:278	The current diagnostic approach uses elevated serum concentrations of prostate-specific antigen (PSA) as an indicator of risk.
33618028	10	83	theme	patient	1292:1298	arg1	samples					1300:1306	urinary patient samples	1284:1306	urinary patient samples	1284:1306	Furthermore, urinary patient samples were analyzed by intact protein analysis and a bottom-up approach (glycopeptide analysis).
33618028	0	84	theme	mass	94:97	arg1	spectrometry					99:110	mass spectrometry	94:110	mass spectrometry	94:110	Profiling the proteoforms of urinary prostate-specific antigen by capillary electrophoresis - mass spectrometry.
33618028	15	85	theme	further	2128:2134	arg1	treatment					2143:2151	further sample treatment	2128:2151	further sample treatment	2128:2151	Importantly, intact protein analysis did not require further sample treatment before being measured by CE-ESI-MS.
33618028	14	86	theme	forms	2033:2037	arg1	contribution					1985:1996	the relative contribution	1972:1996	the relative contribution of cleaved PSA and non-cleaved PSA forms to the total glycosylation profile	1972:2072	This study investigated the PSA proteoforms present in urine and, in particular, determined the relative contribution of cleaved PSA and non-cleaved PSA forms to the total glycosylation profile.
33618028	12	87	theme	PSA	1723:1725	arg1	proteoforms					1727:1737	several PSA proteoforms	1715:1737	several PSA proteoforms	1715:1737	SIGNIFICANCE: The detection of clinically relevant prostate cancer requires a more specific and sensitive biomarker and, in this case, several PSA proteoforms may be able to aid or improve the current PSA test.
33618028	14	88	theme	PSA	2029:2031	arg1	forms					2033:2037	non-cleaved PSA forms	2017:2037	non-cleaved PSA forms	2017:2037	This study investigated the PSA proteoforms present in urine and, in particular, determined the relative contribution of cleaved PSA and non-cleaved PSA forms to the total glycosylation profile.
33618028	14	89	theme	non-cleaved	2017:2027	arg1	forms					2033:2037	non-cleaved PSA forms	2017:2037	non-cleaved PSA forms	2017:2037	This study investigated the PSA proteoforms present in urine and, in particular, determined the relative contribution of cleaved PSA and non-cleaved PSA forms to the total glycosylation profile.
33618028	4	90	theme	early	487:491	arg1	detection					493:501	early detection	487:501	early detection	487:501	In order to improve early detection and diagnosis, several studies have investigated whether different PSA proteoforms are correlated to prostate cancer.
33618028	14	91	theme	PSA	2009:2011	arg1	contribution					1985:1996	the relative contribution	1972:1996	the relative contribution of cleaved PSA and non-cleaved PSA forms to the total glycosylation profile	1972:2072	This study investigated the PSA proteoforms present in urine and, in particular, determined the relative contribution of cleaved PSA and non-cleaved PSA forms to the total glycosylation profile.
33618028	4	92	theme	different	560:568	arg1	proteoforms					574:584	different PSA proteoforms	560:584	different PSA proteoforms	560:584	In order to improve early detection and diagnosis, several studies have investigated whether different PSA proteoforms are correlated to prostate cancer.
33618028	1	93	dep	overdiagnosis	164:176	arg1	the					160:162	the	160:162	the	160:162	Early detection of prostate cancer may lead to the overdiagnosis and overtreatment of patients as well as missing significant cancers.
33618028	13	94	theme	PSA	1839:1841	arg1	profile					1854:1860	the intact PSA proteoform profile	1828:1860	the intact PSA proteoform profile	1828:1860	However, a comprehensive analysis of the intact PSA proteoform profile is still lacking.
33618028	1	95	theme	Early	113:117	arg1	detection					119:127	Early detection	113:127	Early detection of prostate cancer	113:146	Early detection of prostate cancer may lead to the overdiagnosis and overtreatment of patients as well as missing significant cancers.
33618028	13	96	theme	profile	1854:1860	arg1	analysis					1816:1823	a comprehensive analysis	1800:1823	a comprehensive analysis of the intact PSA proteoform profile	1800:1860	However, a comprehensive analysis of the intact PSA proteoform profile is still lacking.
33618028	0	97	theme	prostate-specific	37:53	arg1	antigen					55:61	urinary prostate-specific antigen	29:61	urinary prostate-specific antigen	29:61	Profiling the proteoforms of urinary prostate-specific antigen by capillary electrophoresis - mass spectrometry.
33618028	8	98	theme	non-glycosylated	1122:1137	arg1	variant					1139:1145	the non-glycosylated variant	1118:1145	the non-glycosylated variant	1118:1145	In regard to glycosylation, tri-, di-, mono- and non-sialylated complex-type N-glycans were found on non-cleaved PSA, as well as the non-glycosylated variant.
33618028	14	99	theme	relative	1976:1983	arg1	contribution					1985:1996	the relative contribution	1972:1996	the relative contribution of cleaved PSA and non-cleaved PSA forms to the total glycosylation profile	1972:2072	This study investigated the PSA proteoforms present in urine and, in particular, determined the relative contribution of cleaved PSA and non-cleaved PSA forms to the total glycosylation profile.
33618028	14	100	dep	investigated	1891:1902	arg1	determined					1961:1970	determined	1961:1970	determined the relative contribution of cleaved PSA and non-cleaved PSA forms to the total glycosylation profile	1961:2072	This study investigated the PSA proteoforms present in urine and, in particular, determined the relative contribution of cleaved PSA and non-cleaved PSA forms to the total glycosylation profile.
33618028	6	101	theme	intact	777:782	arg1	assay					792:796	an intact protein assay	774:796	an intact protein assay to analyze PSA by capillary electrophoresis-electrospray ionization-mass spectrometry after affinity purification from patients' urine	774:931	For this purpose, we developed an intact protein assay to analyze PSA by capillary electrophoresis-electrospray ionization-mass spectrometry after affinity purification from patients' urine.
33618028	5	102	from	characterization	680:695	arg1	biofluids					721:729	biofluids	721:729	biofluids	721:729	Until now, studies and methodologies for the comprehensive characterization of PSA proteoforms from biofluids are scarce.
33618028	8	103	theme	tri-	1017:1020	arg1	N-glycans					1066:1074	tri-, di-, mono- and non-sialylated complex-type N-glycans	1017:1074	tri-, di-, mono- and non-sialylated complex-type N-glycans	1017:1074	In regard to glycosylation, tri-, di-, mono- and non-sialylated complex-type N-glycans were found on non-cleaved PSA, as well as the non-glycosylated variant.
33618028	14	104	theme	total	2046:2050	arg1	profile					2066:2072	the total glycosylation profile	2042:2072	the total glycosylation profile	2042:2072	This study investigated the PSA proteoforms present in urine and, in particular, determined the relative contribution of cleaved PSA and non-cleaved PSA forms to the total glycosylation profile.
33618028	10	105	theme	bottom-up	1355:1363	arg1	approach					1365:1372	a bottom-up approach	1353:1372	a bottom-up approach (glycopeptide analysis)	1353:1396	Furthermore, urinary patient samples were analyzed by intact protein analysis and a bottom-up approach (glycopeptide analysis).
33618028	10	105	theme	bottom-up	1355:1363	arg1	analysis					1388:1395	glycopeptide analysis	1375:1395	glycopeptide analysis	1375:1395	Furthermore, urinary patient samples were analyzed by intact protein analysis and a bottom-up approach (glycopeptide analysis).
33618028	17	106	theme	future	2356:2361	arg1	characterization					2363:2378	future characterization	2356:2378	future characterization	2356:2378	Overall, these results represent an important basis for future characterization and biomarker studies.
33618028	9	107	theme	assay	1186:1190	arg1	performance					1152:1162	The performance	1148:1162	The performance of the intact protein assay	1148:1190	The performance of the intact protein assay was assessed using a pooled sample, obtaining an inter-day variability of 15%.
33618028	6	108	theme	ionization-mass	855:869	arg1	spectrometry					871:882	capillary electrophoresis-electrospray ionization-mass spectrometry	816:882	capillary electrophoresis-electrospray ionization-mass spectrometry	816:882	For this purpose, we developed an intact protein assay to analyze PSA by capillary electrophoresis-electrospray ionization-mass spectrometry after affinity purification from patients' urine.
33618028	15	109	theme	intact	2088:2093	arg1	analysis					2103:2110	intact protein analysis	2088:2110	intact protein analysis	2088:2110	Importantly, intact protein analysis did not require further sample treatment before being measured by CE-ESI-MS.
8323280	8	0	theme	Man	1850:1852	arg1	beta					1871:1874	[Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta	1769:1874	[Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta 1-->4GlcNAc-->Asn	1769:1892	The interaction between desialylated rhLT and uromodulin was inhibited by N,N'-diacetylchitobiose and [Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta 1-->4GlcNAc-->Asn.
8323280	8	0	theme	Man	1850:1852	arg1	1-->3					1844:1848	Man alpha 1-->2Man alpha 1-->3	1819:1848	Man alpha 1-->2Man alpha 1-->3	1819:1848	The interaction between desialylated rhLT and uromodulin was inhibited by N,N'-diacetylchitobiose and [Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta 1-->4GlcNAc-->Asn.
8323280	3	1	from	oligosaccharides	617:632	arg1	C					665:665	100 degrees C	653:665	100 degrees C	653:665	The N-linked sugar chains of Tr-45 were released quantitatively as oligosaccharides on hydrazinolysis (100 degrees C, 8 h), followed by N-acetylation.
8323280	3	1	from	oligosaccharides	617:632	arg1	hydrazinolysis					637:650	hydrazinolysis	637:650	hydrazinolysis (100 degrees C, 8 h)	637:671	The N-linked sugar chains of Tr-45 were released quantitatively as oligosaccharides on hydrazinolysis (100 degrees C, 8 h), followed by N-acetylation.
8323280	0	2	theme	clearance	159:167	arg1	velocity					169:176	clearance velocity	159:176	clearance velocity	159:176	N-linked sugar chain structure of recombinant human lymphotoxin produced by CHO cells: the functional role of carbohydrate as to its lectin-like character and clearance velocity.
8323280	2	3	theme	reverse	530:536	arg1	HPLC					544:547	reverse phase HPLC	530:547	reverse phase HPLC	530:547	A peptide N-glycosylated at Asn62 (Tr-45) and one partially O-glycosylated at Thr7 (Tr-14) on cleavage with trypsin were separated by reverse phase HPLC.
8323280	8	4	theme	Man	1802:1804	arg1	alpha					1774:1778	[Man alpha 1-->6	1769:1784	[Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta 1-->4GlcNAc-->Asn	1769:1892	The interaction between desialylated rhLT and uromodulin was inhibited by N,N'-diacetylchitobiose and [Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta 1-->4GlcNAc-->Asn.
8323280	8	4	theme	Man	1802:1804	arg1	1-->6					1812:1816	Man alpha 1-->3)Man alpha 1-->6	1786:1816	Man alpha 1-->3)Man alpha 1-->6	1786:1816	The interaction between desialylated rhLT and uromodulin was inhibited by N,N'-diacetylchitobiose and [Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta 1-->4GlcNAc-->Asn.
8323280	6	5	theme	filtration	1491:1500	arg1	system					1502:1507	the filtration system	1487:1507	the filtration system of the kidney	1487:1521	The clearance velocity from the bloodstream dramatically increased with desialylation, and rhLT tends to have accumulated in the kidney, indicating that there may exist other mechanisms for clearance from the circulation besides the galactose-binding protein in hepatocytes and the filtration system of the kidney.
8323280	5	6	theme	acid	1148:1151	arg1	residues					1153:1160	Their sialic acid residues	1135:1160	Their sialic acid residues	1135:1160	Their sialic acid residues occur only as the Neu5Ac alpha 2-->3Gal group.
8323280	0	7	link	N-linked	0:7	arg1	chain					15:19	N-linked sugar chain	0:19	N-linked sugar chain structure of recombinant human lymphotoxin produced by CHO cells: the functional role of carbohydrate as to its lectin-like character and clearance velocity.	0:177	N-linked sugar chain structure of recombinant human lymphotoxin produced by CHO cells: the functional role of carbohydrate as to its lectin-like character and clearance velocity.
8323280	3	8	theme	degrees	657:663	arg1	C					665:665	100 degrees C	653:665	100 degrees C	653:665	The N-linked sugar chains of Tr-45 were released quantitatively as oligosaccharides on hydrazinolysis (100 degrees C, 8 h), followed by N-acetylation.
8323280	3	8	theme	degrees	657:663	arg1	hydrazinolysis					637:650	hydrazinolysis	637:650	hydrazinolysis (100 degrees C, 8 h)	637:671	The N-linked sugar chains of Tr-45 were released quantitatively as oligosaccharides on hydrazinolysis (100 degrees C, 8 h), followed by N-acetylation.
8323280	4	9	theme	branched	1052:1059	arg1	chains					1095:1100	C-2,6 branched tetraantennary complex-type sugar chains	1046:1100	C-2,6 branched tetraantennary complex-type sugar chains with a fucosylated mannose core	1046:1132	After being reduced with either NaB3H4 or NaB2H4, their structures were determined by a combination of serial lectin affinity chromatography, exoglycosidase digestion, and methylation analysis: 82.7% of the sugar chains occur as biantennary complex-type sugar chains, the remainder being C-2 and C-2,4/C-2,6 branched triantennary, and C-2,4 and C-2,6 branched tetraantennary complex-type sugar chains with a fucosylated mannose core.
8323280	1	10	theme	Recombinant	179:189	arg1	lymphotoxin					197:207	Recombinant human lymphotoxin	179:207	Recombinant human lymphotoxin (rhLT) produced by CHO cells transfected with human LT genomic DNA	179:274	Recombinant human lymphotoxin (rhLT) produced by CHO cells transfected with human LT genomic DNA was purified to homogeneity, but approximately 5% of the molecules were devoid of the last two amino terminal residues.
8323280	1	10	theme	Recombinant	179:189	arg1	rhLT					210:213	rhLT	210:213	rhLT	210:213	Recombinant human lymphotoxin (rhLT) produced by CHO cells transfected with human LT genomic DNA was purified to homogeneity, but approximately 5% of the molecules were devoid of the last two amino terminal residues.
8323280	4	11	theme	exoglycosidase	843:856	arg1	digestion					858:866	exoglycosidase digestion	843:866	exoglycosidase digestion	843:866	After being reduced with either NaB3H4 or NaB2H4, their structures were determined by a combination of serial lectin affinity chromatography, exoglycosidase digestion, and methylation analysis: 82.7% of the sugar chains occur as biantennary complex-type sugar chains, the remainder being C-2 and C-2,4/C-2,6 branched triantennary, and C-2,4 and C-2,6 branched tetraantennary complex-type sugar chains with a fucosylated mannose core.
8323280	8	12	theme	alpha	1823:1827	arg1	beta					1871:1874	[Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta	1769:1874	[Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta 1-->4GlcNAc-->Asn	1769:1892	The interaction between desialylated rhLT and uromodulin was inhibited by N,N'-diacetylchitobiose and [Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta 1-->4GlcNAc-->Asn.
8323280	8	12	theme	alpha	1823:1827	arg1	1-->3					1844:1848	Man alpha 1-->2Man alpha 1-->3	1819:1848	Man alpha 1-->2Man alpha 1-->3	1819:1848	The interaction between desialylated rhLT and uromodulin was inhibited by N,N'-diacetylchitobiose and [Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta 1-->4GlcNAc-->Asn.
8323280	6	13	theme	galactose-binding	1442:1458	arg1	protein					1460:1466	the galactose-binding protein	1438:1466	the galactose-binding protein in hepatocytes and the filtration system of the kidney	1438:1521	The clearance velocity from the bloodstream dramatically increased with desialylation, and rhLT tends to have accumulated in the kidney, indicating that there may exist other mechanisms for clearance from the circulation besides the galactose-binding protein in hepatocytes and the filtration system of the kidney.
8323280	8	14	theme	alpha	1838:1842	arg1	beta					1871:1874	[Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta	1769:1874	[Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta 1-->4GlcNAc-->Asn	1769:1892	The interaction between desialylated rhLT and uromodulin was inhibited by N,N'-diacetylchitobiose and [Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta 1-->4GlcNAc-->Asn.
8323280	8	14	theme	alpha	1838:1842	arg1	1-->3					1844:1848	Man alpha 1-->2Man alpha 1-->3	1819:1848	Man alpha 1-->2Man alpha 1-->3	1819:1848	The interaction between desialylated rhLT and uromodulin was inhibited by N,N'-diacetylchitobiose and [Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta 1-->4GlcNAc-->Asn.
8323280	4	15	theme	lectin	811:816	arg1	chromatography					827:840	serial lectin affinity chromatography	804:840	serial lectin affinity chromatography	804:840	After being reduced with either NaB3H4 or NaB2H4, their structures were determined by a combination of serial lectin affinity chromatography, exoglycosidase digestion, and methylation analysis: 82.7% of the sugar chains occur as biantennary complex-type sugar chains, the remainder being C-2 and C-2,4/C-2,6 branched triantennary, and C-2,4 and C-2,6 branched tetraantennary complex-type sugar chains with a fucosylated mannose core.
8323280	2	16	from	one	442:444	arg1	N-glycosylated					406:419	N-glycosylated	406:419	N-glycosylated	406:419	A peptide N-glycosylated at Asn62 (Tr-45) and one partially O-glycosylated at Thr7 (Tr-14) on cleavage with trypsin were separated by reverse phase HPLC.
8323280	7	17	theme	lectin-like	1551:1561	arg1	character					1571:1579	a lectin-like binding character	1549:1579	a lectin-like binding character	1549:1579	Desialylated rhLT showed a lectin-like binding character to uromodulin similar to that of tumor necrosis factor, although intact rhLT did not.
8323280	4	18	theme	chromatography	827:840	arg1	combination					789:799	a combination	787:799	a combination of serial lectin affinity chromatography, exoglycosidase digestion, and methylation analysis	787:892	After being reduced with either NaB3H4 or NaB2H4, their structures were determined by a combination of serial lectin affinity chromatography, exoglycosidase digestion, and methylation analysis: 82.7% of the sugar chains occur as biantennary complex-type sugar chains, the remainder being C-2 and C-2,4/C-2,6 branched triantennary, and C-2,4 and C-2,6 branched tetraantennary complex-type sugar chains with a fucosylated mannose core.
8323280	4	19	theme	mannose	1121:1127	arg1	core					1129:1132	a fucosylated mannose core	1107:1132	a fucosylated mannose core	1107:1132	After being reduced with either NaB3H4 or NaB2H4, their structures were determined by a combination of serial lectin affinity chromatography, exoglycosidase digestion, and methylation analysis: 82.7% of the sugar chains occur as biantennary complex-type sugar chains, the remainder being C-2 and C-2,4/C-2,6 branched triantennary, and C-2,4 and C-2,6 branched tetraantennary complex-type sugar chains with a fucosylated mannose core.
8323280	8	20	theme	beta	1854:1857	arg1	beta					1871:1874	[Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta	1769:1874	[Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta 1-->4GlcNAc-->Asn	1769:1892	The interaction between desialylated rhLT and uromodulin was inhibited by N,N'-diacetylchitobiose and [Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta 1-->4GlcNAc-->Asn.
8323280	8	20	theme	beta	1854:1857	arg1	1-->3					1844:1848	Man alpha 1-->2Man alpha 1-->3	1819:1848	Man alpha 1-->2Man alpha 1-->3	1819:1848	The interaction between desialylated rhLT and uromodulin was inhibited by N,N'-diacetylchitobiose and [Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta 1-->4GlcNAc-->Asn.
8323280	1	21	theme	terminal	377:384	arg1	residues					386:393	the last two amino terminal residues	358:393	the last two amino terminal residues	358:393	Recombinant human lymphotoxin (rhLT) produced by CHO cells transfected with human LT genomic DNA was purified to homogeneity, but approximately 5% of the molecules were devoid of the last two amino terminal residues.
8323280	3	22	theme	sugar	563:567	arg1	chains					569:574	The N-linked sugar chains	550:574	The N-linked sugar chains of Tr-45	550:583	The N-linked sugar chains of Tr-45 were released quantitatively as oligosaccharides on hydrazinolysis (100 degrees C, 8 h), followed by N-acetylation.
8323280	3	22	theme	sugar	563:567	arg1	oligosaccharides					617:632	oligosaccharides	617:632	oligosaccharides on hydrazinolysis (100 degrees C, 8 h), followed by N-acetylation	617:698	The N-linked sugar chains of Tr-45 were released quantitatively as oligosaccharides on hydrazinolysis (100 degrees C, 8 h), followed by N-acetylation.
8323280	6	23	theme	kidney	1516:1521	arg1	system					1502:1507	the filtration system	1487:1507	the filtration system of the kidney	1487:1521	The clearance velocity from the bloodstream dramatically increased with desialylation, and rhLT tends to have accumulated in the kidney, indicating that there may exist other mechanisms for clearance from the circulation besides the galactose-binding protein in hepatocytes and the filtration system of the kidney.
8323280	6	23	theme	kidney	1516:1521	arg1	hepatocytes					1471:1481	hepatocytes	1471:1481	hepatocytes	1471:1481	The clearance velocity from the bloodstream dramatically increased with desialylation, and rhLT tends to have accumulated in the kidney, indicating that there may exist other mechanisms for clearance from the circulation besides the galactose-binding protein in hepatocytes and the filtration system of the kidney.
8323280	2	24	from	Thr7	474:477	arg1	O-glycosylated					456:469	O-glycosylated	456:469	O-glycosylated	456:469	A peptide N-glycosylated at Asn62 (Tr-45) and one partially O-glycosylated at Thr7 (Tr-14) on cleavage with trypsin were separated by reverse phase HPLC.
8323280	4	25	theme	complex-type	1076:1087	arg1	chains					1095:1100	C-2,6 branched tetraantennary complex-type sugar chains	1046:1100	C-2,6 branched tetraantennary complex-type sugar chains with a fucosylated mannose core	1046:1132	After being reduced with either NaB3H4 or NaB2H4, their structures were determined by a combination of serial lectin affinity chromatography, exoglycosidase digestion, and methylation analysis: 82.7% of the sugar chains occur as biantennary complex-type sugar chains, the remainder being C-2 and C-2,4/C-2,6 branched triantennary, and C-2,4 and C-2,6 branched tetraantennary complex-type sugar chains with a fucosylated mannose core.
8323280	8	26	theme	beta	1871:1874	arg1	1-->4GlcNAc-->Asn					1876:1892	[Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta 1-->4GlcNAc-->Asn	1769:1892	[Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta 1-->4GlcNAc-->Asn	1769:1892	The interaction between desialylated rhLT and uromodulin was inhibited by N,N'-diacetylchitobiose and [Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta 1-->4GlcNAc-->Asn.
8323280	7	27	theme	Desialylated	1524:1535	arg1	rhLT					1537:1540	Desialylated rhLT	1524:1540	Desialylated rhLT	1524:1540	Desialylated rhLT showed a lectin-like binding character to uromodulin similar to that of tumor necrosis factor, although intact rhLT did not.
8323280	8	28	gly	desialylated	1691:1702	arg1	rhLT					1704:1707	desialylated rhLT	1691:1707	desialylated rhLT	1691:1707	The interaction between desialylated rhLT and uromodulin was inhibited by N,N'-diacetylchitobiose and [Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta 1-->4GlcNAc-->Asn.
8323280	5	29	theme	Neu5Ac	1180:1185	arg1	group					1202:1206	the Neu5Ac alpha 2-->3Gal group	1176:1206	the Neu5Ac alpha 2-->3Gal group	1176:1206	Their sialic acid residues occur only as the Neu5Ac alpha 2-->3Gal group.
8323280	0	30	theme	CHO	76:78	arg1	cells					80:84	CHO cells	76:84	CHO cells	76:84	N-linked sugar chain structure of recombinant human lymphotoxin produced by CHO cells: the functional role of carbohydrate as to its lectin-like character and clearance velocity.
8323280	4	31	theme	methylation	873:883	arg1	analysis					885:892	methylation analysis	873:892	methylation analysis	873:892	After being reduced with either NaB3H4 or NaB2H4, their structures were determined by a combination of serial lectin affinity chromatography, exoglycosidase digestion, and methylation analysis: 82.7% of the sugar chains occur as biantennary complex-type sugar chains, the remainder being C-2 and C-2,4/C-2,6 branched triantennary, and C-2,4 and C-2,6 branched tetraantennary complex-type sugar chains with a fucosylated mannose core.
8323280	2	32	from	peptide	398:404	arg1	cleavage					490:497	cleavage	490:497	cleavage	490:497	A peptide N-glycosylated at Asn62 (Tr-45) and one partially O-glycosylated at Thr7 (Tr-14) on cleavage with trypsin were separated by reverse phase HPLC.
8323280	5	33	theme	2-->3Gal	1193:1200	arg1	group					1202:1206	the Neu5Ac alpha 2-->3Gal group	1176:1206	the Neu5Ac alpha 2-->3Gal group	1176:1206	Their sialic acid residues occur only as the Neu5Ac alpha 2-->3Gal group.
8323280	8	34	theme	alpha	1774:1778	arg1	beta					1871:1874	[Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta	1769:1874	[Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta 1-->4GlcNAc-->Asn	1769:1892	The interaction between desialylated rhLT and uromodulin was inhibited by N,N'-diacetylchitobiose and [Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta 1-->4GlcNAc-->Asn.
8323280	8	34	theme	alpha	1774:1778	arg1	1-->3					1844:1848	Man alpha 1-->2Man alpha 1-->3	1819:1848	Man alpha 1-->2Man alpha 1-->3	1819:1848	The interaction between desialylated rhLT and uromodulin was inhibited by N,N'-diacetylchitobiose and [Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta 1-->4GlcNAc-->Asn.
8323280	9	35	theme	rhLT	1949:1952	arg1	rhLT					1949:1952	rhLT	1949:1952	rhLT	1949:1952	These results indicate that the lectin-like domain of rhLT is exposed on its desialylation.
8323280	9	35	theme	rhLT	1949:1952	arg1	domain					1939:1944	the lectin-like domain	1923:1944	the lectin-like domain of rhLT	1923:1952	These results indicate that the lectin-like domain of rhLT is exposed on its desialylation.
8323280	1	36	theme	human	255:259	arg1	DNA					272:274	human LT genomic DNA	255:274	human LT genomic DNA	255:274	Recombinant human lymphotoxin (rhLT) produced by CHO cells transfected with human LT genomic DNA was purified to homogeneity, but approximately 5% of the molecules were devoid of the last two amino terminal residues.
8323280	1	37	theme	molecules	333:341	arg1	%					324:324	approximately 5%	309:324	approximately 5% of the molecules	309:341	Recombinant human lymphotoxin (rhLT) produced by CHO cells transfected with human LT genomic DNA was purified to homogeneity, but approximately 5% of the molecules were devoid of the last two amino terminal residues.
8323280	1	37	theme	molecules	333:341	arg1	molecules					333:341	the molecules	329:341	the molecules	329:341	Recombinant human lymphotoxin (rhLT) produced by CHO cells transfected with human LT genomic DNA was purified to homogeneity, but approximately 5% of the molecules were devoid of the last two amino terminal residues.
8323280	4	38	with	remainder	973:981	arg1	core					1129:1132	a fucosylated mannose core	1107:1132	a fucosylated mannose core	1107:1132	After being reduced with either NaB3H4 or NaB2H4, their structures were determined by a combination of serial lectin affinity chromatography, exoglycosidase digestion, and methylation analysis: 82.7% of the sugar chains occur as biantennary complex-type sugar chains, the remainder being C-2 and C-2,4/C-2,6 branched triantennary, and C-2,4 and C-2,6 branched tetraantennary complex-type sugar chains with a fucosylated mannose core.
8323280	4	39	theme	complex-type	942:953	arg1	chains					961:966	biantennary complex-type sugar chains	930:966	biantennary complex-type sugar chains	930:966	After being reduced with either NaB3H4 or NaB2H4, their structures were determined by a combination of serial lectin affinity chromatography, exoglycosidase digestion, and methylation analysis: 82.7% of the sugar chains occur as biantennary complex-type sugar chains, the remainder being C-2 and C-2,4/C-2,6 branched triantennary, and C-2,4 and C-2,6 branched tetraantennary complex-type sugar chains with a fucosylated mannose core.
8323280	0	40	theme	N-linked	0:7	arg1	chain					15:19	N-linked sugar chain	0:19	N-linked sugar chain structure of recombinant human lymphotoxin produced by CHO cells: the functional role of carbohydrate as to its lectin-like character and clearance velocity.	0:177	N-linked sugar chain structure of recombinant human lymphotoxin produced by CHO cells: the functional role of carbohydrate as to its lectin-like character and clearance velocity.
8323280	1	41	theme	LT	261:262	arg1	DNA					272:274	human LT genomic DNA	255:274	human LT genomic DNA	255:274	Recombinant human lymphotoxin (rhLT) produced by CHO cells transfected with human LT genomic DNA was purified to homogeneity, but approximately 5% of the molecules were devoid of the last two amino terminal residues.
8323280	8	42	theme	alpha	1790:1794	arg1	alpha					1774:1778	[Man alpha 1-->6	1769:1784	[Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta 1-->4GlcNAc-->Asn	1769:1892	The interaction between desialylated rhLT and uromodulin was inhibited by N,N'-diacetylchitobiose and [Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta 1-->4GlcNAc-->Asn.
8323280	8	42	theme	alpha	1790:1794	arg1	1-->6					1812:1816	Man alpha 1-->3)Man alpha 1-->6	1786:1816	Man alpha 1-->3)Man alpha 1-->6	1786:1816	The interaction between desialylated rhLT and uromodulin was inhibited by N,N'-diacetylchitobiose and [Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta 1-->4GlcNAc-->Asn.
8323280	7	43	theme	tumor	1614:1618	arg1	factor					1629:1634	tumor necrosis factor	1614:1634	tumor necrosis factor	1614:1634	Desialylated rhLT showed a lectin-like binding character to uromodulin similar to that of tumor necrosis factor, although intact rhLT did not.
8323280	3	44	link	N-linked	554:561	arg1	chains					569:574	The N-linked sugar chains	550:574	The N-linked sugar chains of Tr-45	550:583	The N-linked sugar chains of Tr-45 were released quantitatively as oligosaccharides on hydrazinolysis (100 degrees C, 8 h), followed by N-acetylation.
8323280	3	44	link	N-linked	554:561	arg1	oligosaccharides					617:632	oligosaccharides	617:632	oligosaccharides on hydrazinolysis (100 degrees C, 8 h), followed by N-acetylation	617:698	The N-linked sugar chains of Tr-45 were released quantitatively as oligosaccharides on hydrazinolysis (100 degrees C, 8 h), followed by N-acetylation.
8323280	0	45	theme	chain	15:19	arg1	structure					21:29	N-linked sugar chain structure	0:29	N-linked sugar chain structure of recombinant human lymphotoxin produced by CHO cells: the functional role of carbohydrate as to its lectin-like character and clearance velocity.	0:177	N-linked sugar chain structure of recombinant human lymphotoxin produced by CHO cells: the functional role of carbohydrate as to its lectin-like character and clearance velocity.
8323280	6	46	from	protein	1460:1466	arg1	system					1502:1507	the filtration system	1487:1507	the filtration system of the kidney	1487:1521	The clearance velocity from the bloodstream dramatically increased with desialylation, and rhLT tends to have accumulated in the kidney, indicating that there may exist other mechanisms for clearance from the circulation besides the galactose-binding protein in hepatocytes and the filtration system of the kidney.
8323280	6	46	from	protein	1460:1466	arg1	hepatocytes					1471:1481	hepatocytes	1471:1481	hepatocytes	1471:1481	The clearance velocity from the bloodstream dramatically increased with desialylation, and rhLT tends to have accumulated in the kidney, indicating that there may exist other mechanisms for clearance from the circulation besides the galactose-binding protein in hepatocytes and the filtration system of the kidney.
8323280	4	47	theme	chains	914:919	arg1	%					899:899	82.7%	895:899	82.7% of the sugar chains	895:919	After being reduced with either NaB3H4 or NaB2H4, their structures were determined by a combination of serial lectin affinity chromatography, exoglycosidase digestion, and methylation analysis: 82.7% of the sugar chains occur as biantennary complex-type sugar chains, the remainder being C-2 and C-2,4/C-2,6 branched triantennary, and C-2,4 and C-2,6 branched tetraantennary complex-type sugar chains with a fucosylated mannose core.
8323280	4	47	theme	chains	914:919	arg1	chains					914:919	the sugar chains	904:919	the sugar chains	904:919	After being reduced with either NaB3H4 or NaB2H4, their structures were determined by a combination of serial lectin affinity chromatography, exoglycosidase digestion, and methylation analysis: 82.7% of the sugar chains occur as biantennary complex-type sugar chains, the remainder being C-2 and C-2,4/C-2,6 branched triantennary, and C-2,4 and C-2,6 branched tetraantennary complex-type sugar chains with a fucosylated mannose core.
8323280	0	48	theme	human	46:50	arg1	lymphotoxin					52:62	recombinant human lymphotoxin	34:62	recombinant human lymphotoxin produced by CHO cells	34:84	N-linked sugar chain structure of recombinant human lymphotoxin produced by CHO cells: the functional role of carbohydrate as to its lectin-like character and clearance velocity.
8323280	6	49	from	bloodstream	1241:1251	arg1	velocity					1223:1230	The clearance velocity	1209:1230	The clearance velocity from the bloodstream	1209:1251	The clearance velocity from the bloodstream dramatically increased with desialylation, and rhLT tends to have accumulated in the kidney, indicating that there may exist other mechanisms for clearance from the circulation besides the galactose-binding protein in hepatocytes and the filtration system of the kidney.
8323280	6	50	from	circulation	1418:1428	arg1	clearance					1399:1407	clearance	1399:1407	clearance from the circulation	1399:1428	The clearance velocity from the bloodstream dramatically increased with desialylation, and rhLT tends to have accumulated in the kidney, indicating that there may exist other mechanisms for clearance from the circulation besides the galactose-binding protein in hepatocytes and the filtration system of the kidney.
8323280	2	51	gly	N-glycosylated	406:419	arg1	peptide					398:404	A peptide	396:404	A peptide N-glycosylated at Asn62 (Tr-45) and one partially O-glycosylated at Thr7 (Tr-14) on cleavage with trypsin	396:510	A peptide N-glycosylated at Asn62 (Tr-45) and one partially O-glycosylated at Thr7 (Tr-14) on cleavage with trypsin were separated by reverse phase HPLC.
8323280	2	51	gly	N-glycosylated	406:419	arg2	Tr-45					431:435	Tr-45	431:435	Tr-45	431:435	A peptide N-glycosylated at Asn62 (Tr-45) and one partially O-glycosylated at Thr7 (Tr-14) on cleavage with trypsin were separated by reverse phase HPLC.
8323280	2	51	gly	N-glycosylated	406:419	arg2	Asn62					424:428	Asn62	424:428	Asn62	424:428	A peptide N-glycosylated at Asn62 (Tr-45) and one partially O-glycosylated at Thr7 (Tr-14) on cleavage with trypsin were separated by reverse phase HPLC.
8323280	2	51	gly	N-glycosylated	406:419	arg1	Tr-14					480:484	Tr-14	480:484	Tr-14	480:484	A peptide N-glycosylated at Asn62 (Tr-45) and one partially O-glycosylated at Thr7 (Tr-14) on cleavage with trypsin were separated by reverse phase HPLC.
8323280	2	51	gly	N-glycosylated	406:419	arg2	one					442:444	one	442:444	one	442:444	A peptide N-glycosylated at Asn62 (Tr-45) and one partially O-glycosylated at Thr7 (Tr-14) on cleavage with trypsin were separated by reverse phase HPLC.
8323280	4	52	theme	branched	1009:1016	arg1	triantennary					1018:1029	C-2,4/C-2,6 branched triantennary	997:1029	C-2,4/C-2,6 branched triantennary	997:1029	After being reduced with either NaB3H4 or NaB2H4, their structures were determined by a combination of serial lectin affinity chromatography, exoglycosidase digestion, and methylation analysis: 82.7% of the sugar chains occur as biantennary complex-type sugar chains, the remainder being C-2 and C-2,4/C-2,6 branched triantennary, and C-2,4 and C-2,6 branched tetraantennary complex-type sugar chains with a fucosylated mannose core.
8323280	1	53	theme	genomic	264:270	arg1	DNA					272:274	human LT genomic DNA	255:274	human LT genomic DNA	255:274	Recombinant human lymphotoxin (rhLT) produced by CHO cells transfected with human LT genomic DNA was purified to homogeneity, but approximately 5% of the molecules were devoid of the last two amino terminal residues.
8323280	6	54	theme	clearance	1213:1221	arg1	velocity					1223:1230	The clearance velocity	1209:1230	The clearance velocity from the bloodstream	1209:1251	The clearance velocity from the bloodstream dramatically increased with desialylation, and rhLT tends to have accumulated in the kidney, indicating that there may exist other mechanisms for clearance from the circulation besides the galactose-binding protein in hepatocytes and the filtration system of the kidney.
8323280	2	55	theme	phase	538:542	arg1	HPLC					544:547	reverse phase HPLC	530:547	reverse phase HPLC	530:547	A peptide N-glycosylated at Asn62 (Tr-45) and one partially O-glycosylated at Thr7 (Tr-14) on cleavage with trypsin were separated by reverse phase HPLC.
8323280	4	56	with	chains	961:966	arg1	core					1129:1132	a fucosylated mannose core	1107:1132	a fucosylated mannose core	1107:1132	After being reduced with either NaB3H4 or NaB2H4, their structures were determined by a combination of serial lectin affinity chromatography, exoglycosidase digestion, and methylation analysis: 82.7% of the sugar chains occur as biantennary complex-type sugar chains, the remainder being C-2 and C-2,4/C-2,6 branched triantennary, and C-2,4 and C-2,6 branched tetraantennary complex-type sugar chains with a fucosylated mannose core.
8323280	8	57	theme	alpha	1806:1810	arg1	alpha					1774:1778	[Man alpha 1-->6	1769:1784	[Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta 1-->4GlcNAc-->Asn	1769:1892	The interaction between desialylated rhLT and uromodulin was inhibited by N,N'-diacetylchitobiose and [Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta 1-->4GlcNAc-->Asn.
8323280	8	57	theme	alpha	1806:1810	arg1	1-->6					1812:1816	Man alpha 1-->3)Man alpha 1-->6	1786:1816	Man alpha 1-->3)Man alpha 1-->6	1786:1816	The interaction between desialylated rhLT and uromodulin was inhibited by N,N'-diacetylchitobiose and [Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta 1-->4GlcNAc-->Asn.
8323280	6	58	theme	other	1378:1382	arg1	mechanisms					1384:1393	other mechanisms	1378:1393	other mechanisms for clearance from the circulation	1378:1428	The clearance velocity from the bloodstream dramatically increased with desialylation, and rhLT tends to have accumulated in the kidney, indicating that there may exist other mechanisms for clearance from the circulation besides the galactose-binding protein in hepatocytes and the filtration system of the kidney.
8323280	5	59	theme	sialic	1141:1146	arg1	residues					1153:1160	Their sialic acid residues	1135:1160	Their sialic acid residues	1135:1160	Their sialic acid residues occur only as the Neu5Ac alpha 2-->3Gal group.
8323280	4	60	with	chains	1095:1100	arg1	core					1129:1132	a fucosylated mannose core	1107:1132	a fucosylated mannose core	1107:1132	After being reduced with either NaB3H4 or NaB2H4, their structures were determined by a combination of serial lectin affinity chromatography, exoglycosidase digestion, and methylation analysis: 82.7% of the sugar chains occur as biantennary complex-type sugar chains, the remainder being C-2 and C-2,4/C-2,6 branched triantennary, and C-2,4 and C-2,6 branched tetraantennary complex-type sugar chains with a fucosylated mannose core.
8323280	4	61	theme	C-2,6	1046:1050	arg1	chains					1095:1100	C-2,6 branched tetraantennary complex-type sugar chains	1046:1100	C-2,6 branched tetraantennary complex-type sugar chains with a fucosylated mannose core	1046:1132	After being reduced with either NaB3H4 or NaB2H4, their structures were determined by a combination of serial lectin affinity chromatography, exoglycosidase digestion, and methylation analysis: 82.7% of the sugar chains occur as biantennary complex-type sugar chains, the remainder being C-2 and C-2,4/C-2,6 branched triantennary, and C-2,4 and C-2,6 branched tetraantennary complex-type sugar chains with a fucosylated mannose core.
8323280	4	62	theme	tetraantennary	1061:1074	arg1	chains					1095:1100	C-2,6 branched tetraantennary complex-type sugar chains	1046:1100	C-2,6 branched tetraantennary complex-type sugar chains with a fucosylated mannose core	1046:1132	After being reduced with either NaB3H4 or NaB2H4, their structures were determined by a combination of serial lectin affinity chromatography, exoglycosidase digestion, and methylation analysis: 82.7% of the sugar chains occur as biantennary complex-type sugar chains, the remainder being C-2 and C-2,4/C-2,6 branched triantennary, and C-2,4 and C-2,6 branched tetraantennary complex-type sugar chains with a fucosylated mannose core.
8323280	8	63	theme	Man	1819:1821	arg1	beta					1871:1874	[Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta	1769:1874	[Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta 1-->4GlcNAc-->Asn	1769:1892	The interaction between desialylated rhLT and uromodulin was inhibited by N,N'-diacetylchitobiose and [Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta 1-->4GlcNAc-->Asn.
8323280	8	63	theme	Man	1819:1821	arg1	1-->3					1844:1848	Man alpha 1-->2Man alpha 1-->3	1819:1848	Man alpha 1-->2Man alpha 1-->3	1819:1848	The interaction between desialylated rhLT and uromodulin was inhibited by N,N'-diacetylchitobiose and [Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta 1-->4GlcNAc-->Asn.
8323280	7	64	theme	similar	1595:1601	arg1	uromodulin					1584:1593	uromodulin	1584:1593	uromodulin similar to that of tumor necrosis factor	1584:1634	Desialylated rhLT showed a lectin-like binding character to uromodulin similar to that of tumor necrosis factor, although intact rhLT did not.
8323280	7	65	gly	Desialylated	1524:1535	arg1	rhLT					1537:1540	Desialylated rhLT	1524:1540	Desialylated rhLT	1524:1540	Desialylated rhLT showed a lectin-like binding character to uromodulin similar to that of tumor necrosis factor, although intact rhLT did not.
8323280	0	66	theme	carbohydrate	110:121	arg1	role					102:105	the functional role	87:105	N-linked sugar chain structure of recombinant human lymphotoxin produced by CHO cells: the functional role of carbohydrate as to its lectin-like character and clearance velocity.	0:177	N-linked sugar chain structure of recombinant human lymphotoxin produced by CHO cells: the functional role of carbohydrate as to its lectin-like character and clearance velocity.
8323280	1	67	theme	human	191:195	arg1	lymphotoxin					197:207	Recombinant human lymphotoxin	179:207	Recombinant human lymphotoxin (rhLT) produced by CHO cells transfected with human LT genomic DNA	179:274	Recombinant human lymphotoxin (rhLT) produced by CHO cells transfected with human LT genomic DNA was purified to homogeneity, but approximately 5% of the molecules were devoid of the last two amino terminal residues.
8323280	1	67	theme	human	191:195	arg1	rhLT					210:213	rhLT	210:213	rhLT	210:213	Recombinant human lymphotoxin (rhLT) produced by CHO cells transfected with human LT genomic DNA was purified to homogeneity, but approximately 5% of the molecules were devoid of the last two amino terminal residues.
8323280	7	68	theme	binding	1563:1569	arg1	character					1571:1579	a lectin-like binding character	1549:1579	a lectin-like binding character	1549:1579	Desialylated rhLT showed a lectin-like binding character to uromodulin similar to that of tumor necrosis factor, although intact rhLT did not.
8323280	4	69	theme	digestion	858:866	arg1	combination					789:799	a combination	787:799	a combination of serial lectin affinity chromatography, exoglycosidase digestion, and methylation analysis	787:892	After being reduced with either NaB3H4 or NaB2H4, their structures were determined by a combination of serial lectin affinity chromatography, exoglycosidase digestion, and methylation analysis: 82.7% of the sugar chains occur as biantennary complex-type sugar chains, the remainder being C-2 and C-2,4/C-2,6 branched triantennary, and C-2,4 and C-2,6 branched tetraantennary complex-type sugar chains with a fucosylated mannose core.
8323280	4	70	theme	fucosylated	1109:1119	arg1	core					1129:1132	a fucosylated mannose core	1107:1132	a fucosylated mannose core	1107:1132	After being reduced with either NaB3H4 or NaB2H4, their structures were determined by a combination of serial lectin affinity chromatography, exoglycosidase digestion, and methylation analysis: 82.7% of the sugar chains occur as biantennary complex-type sugar chains, the remainder being C-2 and C-2,4/C-2,6 branched triantennary, and C-2,4 and C-2,6 branched tetraantennary complex-type sugar chains with a fucosylated mannose core.
8323280	0	71	theme	lectin-like	133:143	arg1	character					145:153	its lectin-like character	129:153	its lectin-like character	129:153	N-linked sugar chain structure of recombinant human lymphotoxin produced by CHO cells: the functional role of carbohydrate as to its lectin-like character and clearance velocity.
8323280	1	72	theme	last	362:365	arg1	residues					386:393	the last two amino terminal residues	358:393	the last two amino terminal residues	358:393	Recombinant human lymphotoxin (rhLT) produced by CHO cells transfected with human LT genomic DNA was purified to homogeneity, but approximately 5% of the molecules were devoid of the last two amino terminal residues.
8323280	4	73	theme	serial	804:809	arg1	chromatography					827:840	serial lectin affinity chromatography	804:840	serial lectin affinity chromatography	804:840	After being reduced with either NaB3H4 or NaB2H4, their structures were determined by a combination of serial lectin affinity chromatography, exoglycosidase digestion, and methylation analysis: 82.7% of the sugar chains occur as biantennary complex-type sugar chains, the remainder being C-2 and C-2,4/C-2,6 branched triantennary, and C-2,4 and C-2,6 branched tetraantennary complex-type sugar chains with a fucosylated mannose core.
8323280	8	74	theme	1-->4GlcNAc	1859:1869	arg1	beta					1871:1874	[Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta	1769:1874	[Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta 1-->4GlcNAc-->Asn	1769:1892	The interaction between desialylated rhLT and uromodulin was inhibited by N,N'-diacetylchitobiose and [Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta 1-->4GlcNAc-->Asn.
8323280	8	74	theme	1-->4GlcNAc	1859:1869	arg1	1-->3					1844:1848	Man alpha 1-->2Man alpha 1-->3	1819:1848	Man alpha 1-->2Man alpha 1-->3	1819:1848	The interaction between desialylated rhLT and uromodulin was inhibited by N,N'-diacetylchitobiose and [Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta 1-->4GlcNAc-->Asn.
8323280	1	75	theme	amino	371:375	arg1	residues					386:393	the last two amino terminal residues	358:393	the last two amino terminal residues	358:393	Recombinant human lymphotoxin (rhLT) produced by CHO cells transfected with human LT genomic DNA was purified to homogeneity, but approximately 5% of the molecules were devoid of the last two amino terminal residues.
8323280	3	76	theme	N-linked	554:561	arg1	chains					569:574	The N-linked sugar chains	550:574	The N-linked sugar chains of Tr-45	550:583	The N-linked sugar chains of Tr-45 were released quantitatively as oligosaccharides on hydrazinolysis (100 degrees C, 8 h), followed by N-acetylation.
8323280	3	76	theme	N-linked	554:561	arg1	oligosaccharides					617:632	oligosaccharides	617:632	oligosaccharides on hydrazinolysis (100 degrees C, 8 h), followed by N-acetylation	617:698	The N-linked sugar chains of Tr-45 were released quantitatively as oligosaccharides on hydrazinolysis (100 degrees C, 8 h), followed by N-acetylation.
8323280	2	77	with	peptide	398:404	arg1	trypsin					504:510	trypsin	504:510	trypsin	504:510	A peptide N-glycosylated at Asn62 (Tr-45) and one partially O-glycosylated at Thr7 (Tr-14) on cleavage with trypsin were separated by reverse phase HPLC.
8323280	4	78	theme	affinity	818:825	arg1	chromatography					827:840	serial lectin affinity chromatography	804:840	serial lectin affinity chromatography	804:840	After being reduced with either NaB3H4 or NaB2H4, their structures were determined by a combination of serial lectin affinity chromatography, exoglycosidase digestion, and methylation analysis: 82.7% of the sugar chains occur as biantennary complex-type sugar chains, the remainder being C-2 and C-2,4/C-2,6 branched triantennary, and C-2,4 and C-2,6 branched tetraantennary complex-type sugar chains with a fucosylated mannose core.
8323280	4	79	theme	sugar	1089:1093	arg1	chains					1095:1100	C-2,6 branched tetraantennary complex-type sugar chains	1046:1100	C-2,6 branched tetraantennary complex-type sugar chains with a fucosylated mannose core	1046:1132	After being reduced with either NaB3H4 or NaB2H4, their structures were determined by a combination of serial lectin affinity chromatography, exoglycosidase digestion, and methylation analysis: 82.7% of the sugar chains occur as biantennary complex-type sugar chains, the remainder being C-2 and C-2,4/C-2,6 branched triantennary, and C-2,4 and C-2,6 branched tetraantennary complex-type sugar chains with a fucosylated mannose core.
8323280	1	80	theme	residues	386:393	arg1	devoid					348:353	devoid	348:353	devoid	348:353	Recombinant human lymphotoxin (rhLT) produced by CHO cells transfected with human LT genomic DNA was purified to homogeneity, but approximately 5% of the molecules were devoid of the last two amino terminal residues.
8323280	9	81	theme	lectin-like	1927:1937	arg1	rhLT					1949:1952	rhLT	1949:1952	rhLT	1949:1952	These results indicate that the lectin-like domain of rhLT is exposed on its desialylation.
8323280	9	81	theme	lectin-like	1927:1937	arg1	domain					1939:1944	the lectin-like domain	1923:1944	the lectin-like domain of rhLT	1923:1952	These results indicate that the lectin-like domain of rhLT is exposed on its desialylation.
8323280	5	82	theme	alpha	1187:1191	arg1	group					1202:1206	the Neu5Ac alpha 2-->3Gal group	1176:1206	the Neu5Ac alpha 2-->3Gal group	1176:1206	Their sialic acid residues occur only as the Neu5Ac alpha 2-->3Gal group.
8323280	8	83	theme	1-->3	1796:1800	arg1	alpha					1774:1778	[Man alpha 1-->6	1769:1784	[Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta 1-->4GlcNAc-->Asn	1769:1892	The interaction between desialylated rhLT and uromodulin was inhibited by N,N'-diacetylchitobiose and [Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta 1-->4GlcNAc-->Asn.
8323280	8	83	theme	1-->3	1796:1800	arg1	1-->6					1812:1816	Man alpha 1-->3)Man alpha 1-->6	1786:1816	Man alpha 1-->3)Man alpha 1-->6	1786:1816	The interaction between desialylated rhLT and uromodulin was inhibited by N,N'-diacetylchitobiose and [Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta 1-->4GlcNAc-->Asn.
8323280	2	84	from	Asn62	424:428	arg1	N-glycosylated					406:419	N-glycosylated	406:419	N-glycosylated	406:419	A peptide N-glycosylated at Asn62 (Tr-45) and one partially O-glycosylated at Thr7 (Tr-14) on cleavage with trypsin were separated by reverse phase HPLC.
8323280	8	85	theme	desialylated	1691:1702	arg1	rhLT					1704:1707	desialylated rhLT	1691:1707	desialylated rhLT	1691:1707	The interaction between desialylated rhLT and uromodulin was inhibited by N,N'-diacetylchitobiose and [Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta 1-->4GlcNAc-->Asn.
8323280	8	86	theme	[Man	1769:1772	arg1	alpha					1774:1778	[Man alpha 1-->6	1769:1784	[Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta 1-->4GlcNAc-->Asn	1769:1892	The interaction between desialylated rhLT and uromodulin was inhibited by N,N'-diacetylchitobiose and [Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta 1-->4GlcNAc-->Asn.
8323280	8	86	theme	[Man	1769:1772	arg1	1-->6					1812:1816	Man alpha 1-->3)Man alpha 1-->6	1786:1816	Man alpha 1-->3)Man alpha 1-->6	1786:1816	The interaction between desialylated rhLT and uromodulin was inhibited by N,N'-diacetylchitobiose and [Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta 1-->4GlcNAc-->Asn.
8323280	2	87	gly	O-glycosylated	456:469	arg2	Thr7					474:477	Thr7	474:477	Thr7	474:477	A peptide N-glycosylated at Asn62 (Tr-45) and one partially O-glycosylated at Thr7 (Tr-14) on cleavage with trypsin were separated by reverse phase HPLC.
8323280	7	88	theme	intact	1646:1651	arg1	rhLT					1653:1656	intact rhLT	1646:1656	intact rhLT	1646:1656	Desialylated rhLT showed a lectin-like binding character to uromodulin similar to that of tumor necrosis factor, although intact rhLT did not.
8323280	4	89	theme	analysis	885:892	arg1	combination					789:799	a combination	787:799	a combination of serial lectin affinity chromatography, exoglycosidase digestion, and methylation analysis	787:892	After being reduced with either NaB3H4 or NaB2H4, their structures were determined by a combination of serial lectin affinity chromatography, exoglycosidase digestion, and methylation analysis: 82.7% of the sugar chains occur as biantennary complex-type sugar chains, the remainder being C-2 and C-2,4/C-2,6 branched triantennary, and C-2,4 and C-2,6 branched tetraantennary complex-type sugar chains with a fucosylated mannose core.
8323280	0	90	theme	sugar	9:13	arg1	chain					15:19	N-linked sugar chain	0:19	N-linked sugar chain structure of recombinant human lymphotoxin produced by CHO cells: the functional role of carbohydrate as to its lectin-like character and clearance velocity.	0:177	N-linked sugar chain structure of recombinant human lymphotoxin produced by CHO cells: the functional role of carbohydrate as to its lectin-like character and clearance velocity.
8323280	2	91	dep	N-glycosylated	406:419	arg1	O-glycosylated					456:469	O-glycosylated	456:469	O-glycosylated	456:469	A peptide N-glycosylated at Asn62 (Tr-45) and one partially O-glycosylated at Thr7 (Tr-14) on cleavage with trypsin were separated by reverse phase HPLC.
8323280	4	92	theme	biantennary	930:940	arg1	chains					961:966	biantennary complex-type sugar chains	930:966	biantennary complex-type sugar chains	930:966	After being reduced with either NaB3H4 or NaB2H4, their structures were determined by a combination of serial lectin affinity chromatography, exoglycosidase digestion, and methylation analysis: 82.7% of the sugar chains occur as biantennary complex-type sugar chains, the remainder being C-2 and C-2,4/C-2,6 branched triantennary, and C-2,4 and C-2,6 branched tetraantennary complex-type sugar chains with a fucosylated mannose core.
8323280	4	93	gly	fucosylated	1109:1119	arg1	core					1129:1132	a fucosylated mannose core	1107:1132	a fucosylated mannose core	1107:1132	After being reduced with either NaB3H4 or NaB2H4, their structures were determined by a combination of serial lectin affinity chromatography, exoglycosidase digestion, and methylation analysis: 82.7% of the sugar chains occur as biantennary complex-type sugar chains, the remainder being C-2 and C-2,4/C-2,6 branched triantennary, and C-2,4 and C-2,6 branched tetraantennary complex-type sugar chains with a fucosylated mannose core.
8323280	8	94	theme	Man	1786:1788	arg1	alpha					1774:1778	[Man alpha 1-->6	1769:1784	[Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta 1-->4GlcNAc-->Asn	1769:1892	The interaction between desialylated rhLT and uromodulin was inhibited by N,N'-diacetylchitobiose and [Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta 1-->4GlcNAc-->Asn.
8323280	8	94	theme	Man	1786:1788	arg1	1-->6					1812:1816	Man alpha 1-->3)Man alpha 1-->6	1786:1816	Man alpha 1-->3)Man alpha 1-->6	1786:1816	The interaction between desialylated rhLT and uromodulin was inhibited by N,N'-diacetylchitobiose and [Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta 1-->4GlcNAc-->Asn.
8323280	7	95	theme	necrosis	1620:1627	arg1	factor					1629:1634	tumor necrosis factor	1614:1634	tumor necrosis factor	1614:1634	Desialylated rhLT showed a lectin-like binding character to uromodulin similar to that of tumor necrosis factor, although intact rhLT did not.
8323280	4	96	theme	sugar	955:959	arg1	chains					961:966	biantennary complex-type sugar chains	930:966	biantennary complex-type sugar chains	930:966	After being reduced with either NaB3H4 or NaB2H4, their structures were determined by a combination of serial lectin affinity chromatography, exoglycosidase digestion, and methylation analysis: 82.7% of the sugar chains occur as biantennary complex-type sugar chains, the remainder being C-2 and C-2,4/C-2,6 branched triantennary, and C-2,4 and C-2,6 branched tetraantennary complex-type sugar chains with a fucosylated mannose core.
8323280	3	97	theme	Tr-45	579:583	arg1	chains					569:574	The N-linked sugar chains	550:574	The N-linked sugar chains of Tr-45	550:583	The N-linked sugar chains of Tr-45 were released quantitatively as oligosaccharides on hydrazinolysis (100 degrees C, 8 h), followed by N-acetylation.
8323280	3	97	theme	Tr-45	579:583	arg1	oligosaccharides					617:632	oligosaccharides	617:632	oligosaccharides on hydrazinolysis (100 degrees C, 8 h), followed by N-acetylation	617:698	The N-linked sugar chains of Tr-45 were released quantitatively as oligosaccharides on hydrazinolysis (100 degrees C, 8 h), followed by N-acetylation.
8323280	0	98	theme	recombinant	34:44	arg1	lymphotoxin					52:62	recombinant human lymphotoxin	34:62	recombinant human lymphotoxin produced by CHO cells	34:84	N-linked sugar chain structure of recombinant human lymphotoxin produced by CHO cells: the functional role of carbohydrate as to its lectin-like character and clearance velocity.
8323280	8	99	theme	1-->2Man	1829:1836	arg1	beta					1871:1874	[Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta	1769:1874	[Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta 1-->4GlcNAc-->Asn	1769:1892	The interaction between desialylated rhLT and uromodulin was inhibited by N,N'-diacetylchitobiose and [Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta 1-->4GlcNAc-->Asn.
8323280	8	99	theme	1-->2Man	1829:1836	arg1	1-->3					1844:1848	Man alpha 1-->2Man alpha 1-->3	1819:1848	Man alpha 1-->2Man alpha 1-->3	1819:1848	The interaction between desialylated rhLT and uromodulin was inhibited by N,N'-diacetylchitobiose and [Man alpha 1-->6(Man alpha 1-->3)Man alpha 1-->6](Man alpha 1-->2Man alpha 1-->3)Man beta 1-->4GlcNAc beta 1-->4GlcNAc-->Asn.
8323280	4	100	theme	sugar	908:912	arg1	chains					914:919	the sugar chains	904:919	the sugar chains	904:919	After being reduced with either NaB3H4 or NaB2H4, their structures were determined by a combination of serial lectin affinity chromatography, exoglycosidase digestion, and methylation analysis: 82.7% of the sugar chains occur as biantennary complex-type sugar chains, the remainder being C-2 and C-2,4/C-2,6 branched triantennary, and C-2,4 and C-2,6 branched tetraantennary complex-type sugar chains with a fucosylated mannose core.
8323280	0	101	theme	functional	91:100	arg1	role					102:105	the functional role	87:105	N-linked sugar chain structure of recombinant human lymphotoxin produced by CHO cells: the functional role of carbohydrate as to its lectin-like character and clearance velocity.	0:177	N-linked sugar chain structure of recombinant human lymphotoxin produced by CHO cells: the functional role of carbohydrate as to its lectin-like character and clearance velocity.
8323280	0	102	theme	lymphotoxin	52:62	arg1	structure					21:29	N-linked sugar chain structure	0:29	N-linked sugar chain structure of recombinant human lymphotoxin produced by CHO cells: the functional role of carbohydrate as to its lectin-like character and clearance velocity.	0:177	N-linked sugar chain structure of recombinant human lymphotoxin produced by CHO cells: the functional role of carbohydrate as to its lectin-like character and clearance velocity.
8323280	3	103	dep	C	665:665	arg1	h					670:670	8 h	668:670	8 h	668:670	The N-linked sugar chains of Tr-45 were released quantitatively as oligosaccharides on hydrazinolysis (100 degrees C, 8 h), followed by N-acetylation.
8323280	0	104	dep	structure	21:29	arg1	role					102:105	the functional role	87:105	N-linked sugar chain structure of recombinant human lymphotoxin produced by CHO cells: the functional role of carbohydrate as to its lectin-like character and clearance velocity.	0:177	N-linked sugar chain structure of recombinant human lymphotoxin produced by CHO cells: the functional role of carbohydrate as to its lectin-like character and clearance velocity.
8323280	4	105	theme	C-2,4/C-2,6	997:1007	arg1	triantennary					1018:1029	C-2,4/C-2,6 branched triantennary	997:1029	C-2,4/C-2,6 branched triantennary	997:1029	After being reduced with either NaB3H4 or NaB2H4, their structures were determined by a combination of serial lectin affinity chromatography, exoglycosidase digestion, and methylation analysis: 82.7% of the sugar chains occur as biantennary complex-type sugar chains, the remainder being C-2 and C-2,4/C-2,6 branched triantennary, and C-2,4 and C-2,6 branched tetraantennary complex-type sugar chains with a fucosylated mannose core.
8323280	2	106	theme	N-glycosylated	406:419	arg1	peptide					398:404	A peptide	396:404	A peptide N-glycosylated at Asn62 (Tr-45) and one partially O-glycosylated at Thr7 (Tr-14) on cleavage with trypsin	396:510	A peptide N-glycosylated at Asn62 (Tr-45) and one partially O-glycosylated at Thr7 (Tr-14) on cleavage with trypsin were separated by reverse phase HPLC.
8323280	2	106	theme	N-glycosylated	406:419	arg1	Tr-14					480:484	Tr-14	480:484	Tr-14	480:484	A peptide N-glycosylated at Asn62 (Tr-45) and one partially O-glycosylated at Thr7 (Tr-14) on cleavage with trypsin were separated by reverse phase HPLC.
8323280	1	107	theme	CHO	228:230	arg1	cells					232:236	CHO cells	228:236	CHO cells transfected with human LT genomic DNA	228:274	Recombinant human lymphotoxin (rhLT) produced by CHO cells transfected with human LT genomic DNA was purified to homogeneity, but approximately 5% of the molecules were devoid of the last two amino terminal residues.
3661998	0	0	theme	exoglycosidases	85:99	arg1	combination					54:64	a combination	52:64	a combination of glycopeptidase, exoglycosidases, and high-performance liquid chromatography	52:143	Structural analysis of N-linked oligosaccharides by a combination of glycopeptidase, exoglycosidases, and high-performance liquid chromatography.
3661998	2	1	theme	exoglycosidase	682:695	arg1	digestion					697:705	sequential exoglycosidase digestion	671:705	sequential exoglycosidase digestion	671:705	The method involves four steps: preparation of carbohydrate chains from glycopeptides by N-oligosaccharide glycopeptidase digestion; derivatization of the reducing ends of carbohydrate chains with a fluorescent reagent, 2-aminopyridine, by using sodium cyanoborohydride; separation of oligosaccharide derivatives by reverse-phase high-performance liquid chromatography; and structural analysis of oligosaccharides by sequential exoglycosidase digestion.
3661998	5	2	theme	oligosaccharides	993:1008	arg1	structures					979:988	the structures	975:988	the structures of oligosaccharides in the myeloma IgG protein, Yot	975:1040	The method was applied to elucidate the structures of oligosaccharides in the myeloma IgG protein, Yot.
3661998	2	3	theme	sequential	671:680	arg1	digestion					697:705	sequential exoglycosidase digestion	671:705	sequential exoglycosidase digestion	671:705	The method involves four steps: preparation of carbohydrate chains from glycopeptides by N-oligosaccharide glycopeptidase digestion; derivatization of the reducing ends of carbohydrate chains with a fluorescent reagent, 2-aminopyridine, by using sodium cyanoborohydride; separation of oligosaccharide derivatives by reverse-phase high-performance liquid chromatography; and structural analysis of oligosaccharides by sequential exoglycosidase digestion.
3661998	0	4	link	N-linked	23:30	arg1	oligosaccharides					32:47	N-linked oligosaccharides	23:47	N-linked oligosaccharides	23:47	Structural analysis of N-linked oligosaccharides by a combination of glycopeptidase, exoglycosidases, and high-performance liquid chromatography.
3661998	2	5	theme	reverse-phase	570:582	arg1	chromatography					608:621	reverse-phase high-performance liquid chromatography	570:621	reverse-phase high-performance liquid chromatography	570:621	The method involves four steps: preparation of carbohydrate chains from glycopeptides by N-oligosaccharide glycopeptidase digestion; derivatization of the reducing ends of carbohydrate chains with a fluorescent reagent, 2-aminopyridine, by using sodium cyanoborohydride; separation of oligosaccharide derivatives by reverse-phase high-performance liquid chromatography; and structural analysis of oligosaccharides by sequential exoglycosidase digestion.
3661998	4	6	theme	elution	884:890	arg1	position					892:899	its elution position	880:899	its elution position	880:899	The structure of an unknown oligosaccharide can be characterized by comparison of its elution position with those of the standard compounds.
3661998	2	7	from	glycopeptides	326:338	arg1	preparation					286:296	preparation	286:296	four steps: preparation of carbohydrate chains from glycopeptides by N-oligosaccharide glycopeptidase digestion; derivatization of the reducing ends of carbohydrate chains with a fluorescent reagent, 2-aminopyridine,	274:489	The method involves four steps: preparation of carbohydrate chains from glycopeptides by N-oligosaccharide glycopeptidase digestion; derivatization of the reducing ends of carbohydrate chains with a fluorescent reagent, 2-aminopyridine, by using sodium cyanoborohydride; separation of oligosaccharide derivatives by reverse-phase high-performance liquid chromatography; and structural analysis of oligosaccharides by sequential exoglycosidase digestion.
3661998	2	7	from	glycopeptides	326:338	arg1	chains					314:319	carbohydrate chains	301:319	carbohydrate chains from glycopeptides	301:338	The method involves four steps: preparation of carbohydrate chains from glycopeptides by N-oligosaccharide glycopeptidase digestion; derivatization of the reducing ends of carbohydrate chains with a fluorescent reagent, 2-aminopyridine, by using sodium cyanoborohydride; separation of oligosaccharide derivatives by reverse-phase high-performance liquid chromatography; and structural analysis of oligosaccharides by sequential exoglycosidase digestion.
3661998	2	8	with	chains	439:444	arg1	2-aminopyridine					474:488	2-aminopyridine	474:488	2-aminopyridine	474:488	The method involves four steps: preparation of carbohydrate chains from glycopeptides by N-oligosaccharide glycopeptidase digestion; derivatization of the reducing ends of carbohydrate chains with a fluorescent reagent, 2-aminopyridine, by using sodium cyanoborohydride; separation of oligosaccharide derivatives by reverse-phase high-performance liquid chromatography; and structural analysis of oligosaccharides by sequential exoglycosidase digestion.
3661998	2	8	with	chains	439:444	arg1	reagent					465:471	a fluorescent reagent	451:471	a fluorescent reagent	451:471	The method involves four steps: preparation of carbohydrate chains from glycopeptides by N-oligosaccharide glycopeptidase digestion; derivatization of the reducing ends of carbohydrate chains with a fluorescent reagent, 2-aminopyridine, by using sodium cyanoborohydride; separation of oligosaccharide derivatives by reverse-phase high-performance liquid chromatography; and structural analysis of oligosaccharides by sequential exoglycosidase digestion.
3661998	2	9	theme	oligosaccharides	651:666	arg1	separation					525:534	separation	525:534	separation of oligosaccharide derivatives by reverse-phase high-performance liquid chromatography	525:621	The method involves four steps: preparation of carbohydrate chains from glycopeptides by N-oligosaccharide glycopeptidase digestion; derivatization of the reducing ends of carbohydrate chains with a fluorescent reagent, 2-aminopyridine, by using sodium cyanoborohydride; separation of oligosaccharide derivatives by reverse-phase high-performance liquid chromatography; and structural analysis of oligosaccharides by sequential exoglycosidase digestion.
3661998	2	9	theme	oligosaccharides	651:666	arg1	cyanoborohydride					507:522	sodium cyanoborohydride	500:522	sodium cyanoborohydride	500:522	The method involves four steps: preparation of carbohydrate chains from glycopeptides by N-oligosaccharide glycopeptidase digestion; derivatization of the reducing ends of carbohydrate chains with a fluorescent reagent, 2-aminopyridine, by using sodium cyanoborohydride; separation of oligosaccharide derivatives by reverse-phase high-performance liquid chromatography; and structural analysis of oligosaccharides by sequential exoglycosidase digestion.
3661998	2	9	theme	oligosaccharides	651:666	arg1	analysis					639:646	structural analysis	628:646	structural analysis of oligosaccharides by sequential exoglycosidase digestion	628:705	The method involves four steps: preparation of carbohydrate chains from glycopeptides by N-oligosaccharide glycopeptidase digestion; derivatization of the reducing ends of carbohydrate chains with a fluorescent reagent, 2-aminopyridine, by using sodium cyanoborohydride; separation of oligosaccharide derivatives by reverse-phase high-performance liquid chromatography; and structural analysis of oligosaccharides by sequential exoglycosidase digestion.
3661998	5	10	from	structures	979:988	arg1	Yot					1038:1040	Yot	1038:1040	Yot	1038:1040	The method was applied to elucidate the structures of oligosaccharides in the myeloma IgG protein, Yot.
3661998	5	10	from	structures	979:988	arg1	protein					1029:1035	the myeloma IgG protein	1013:1035	the myeloma IgG protein	1013:1035	The method was applied to elucidate the structures of oligosaccharides in the myeloma IgG protein, Yot.
3661998	0	11	theme	liquid	123:128	arg1	chromatography					130:143	high-performance liquid chromatography	106:143	high-performance liquid chromatography	106:143	Structural analysis of N-linked oligosaccharides by a combination of glycopeptidase, exoglycosidases, and high-performance liquid chromatography.
3661998	5	12	theme	IgG	1025:1027	arg1	Yot					1038:1040	Yot	1038:1040	Yot	1038:1040	The method was applied to elucidate the structures of oligosaccharides in the myeloma IgG protein, Yot.
3661998	5	12	theme	IgG	1025:1027	arg1	protein					1029:1035	the myeloma IgG protein	1013:1035	the myeloma IgG protein	1013:1035	The method was applied to elucidate the structures of oligosaccharides in the myeloma IgG protein, Yot.
3661998	1	13	theme	rapid	171:175	arg1	method					177:182	A simple, sensitive, and rapid method	146:182	A simple, sensitive, and rapid method for the analysis of structures of N-linked carbohydrates	146:239	A simple, sensitive, and rapid method for the analysis of structures of N-linked carbohydrates is reported.
3661998	0	14	theme	high-performance	106:121	arg1	chromatography					130:143	high-performance liquid chromatography	106:143	high-performance liquid chromatography	106:143	Structural analysis of N-linked oligosaccharides by a combination of glycopeptidase, exoglycosidases, and high-performance liquid chromatography.
3661998	2	15	theme	ends	418:421	arg1	derivatization					387:400	derivatization	387:400	four steps: preparation of carbohydrate chains from glycopeptides by N-oligosaccharide glycopeptidase digestion; derivatization of the reducing ends of carbohydrate chains with a fluorescent reagent, 2-aminopyridine,	274:489	The method involves four steps: preparation of carbohydrate chains from glycopeptides by N-oligosaccharide glycopeptidase digestion; derivatization of the reducing ends of carbohydrate chains with a fluorescent reagent, 2-aminopyridine, by using sodium cyanoborohydride; separation of oligosaccharide derivatives by reverse-phase high-performance liquid chromatography; and structural analysis of oligosaccharides by sequential exoglycosidase digestion.
3661998	2	16	theme	reducing	409:416	arg1	ends					418:421	the reducing ends	405:421	the reducing ends of carbohydrate chains with a fluorescent reagent, 2-aminopyridine,	405:489	The method involves four steps: preparation of carbohydrate chains from glycopeptides by N-oligosaccharide glycopeptidase digestion; derivatization of the reducing ends of carbohydrate chains with a fluorescent reagent, 2-aminopyridine, by using sodium cyanoborohydride; separation of oligosaccharide derivatives by reverse-phase high-performance liquid chromatography; and structural analysis of oligosaccharides by sequential exoglycosidase digestion.
3661998	0	17	theme	Structural	0:9	arg1	analysis					11:18	Structural analysis	0:18	Structural analysis of N-linked oligosaccharides by a combination of glycopeptidase, exoglycosidases, and high-performance liquid chromatography.	0:144	Structural analysis of N-linked oligosaccharides by a combination of glycopeptidase, exoglycosidases, and high-performance liquid chromatography.
3661998	3	18	theme	derivatives	761:771	arg1	positions					720:728	The elution positions	708:728	The elution positions of 50 standard oligosaccharide derivatives	708:771	The elution positions of 50 standard oligosaccharide derivatives were determined by HPLC.
3661998	1	19	link	N-linked	218:225	arg1	carbohydrates					227:239	N-linked carbohydrates	218:239	N-linked carbohydrates	218:239	A simple, sensitive, and rapid method for the analysis of structures of N-linked carbohydrates is reported.
3661998	2	20	theme	chains	314:319	arg1	preparation					286:296	preparation	286:296	four steps: preparation of carbohydrate chains from glycopeptides by N-oligosaccharide glycopeptidase digestion; derivatization of the reducing ends of carbohydrate chains with a fluorescent reagent, 2-aminopyridine,	274:489	The method involves four steps: preparation of carbohydrate chains from glycopeptides by N-oligosaccharide glycopeptidase digestion; derivatization of the reducing ends of carbohydrate chains with a fluorescent reagent, 2-aminopyridine, by using sodium cyanoborohydride; separation of oligosaccharide derivatives by reverse-phase high-performance liquid chromatography; and structural analysis of oligosaccharides by sequential exoglycosidase digestion.
3661998	3	21	theme	standard	736:743	arg1	derivatives					761:771	50 standard oligosaccharide derivatives	733:771	50 standard oligosaccharide derivatives	733:771	The elution positions of 50 standard oligosaccharide derivatives were determined by HPLC.
3661998	0	22	theme	N-linked	23:30	arg1	oligosaccharides					32:47	N-linked oligosaccharides	23:47	N-linked oligosaccharides	23:47	Structural analysis of N-linked oligosaccharides by a combination of glycopeptidase, exoglycosidases, and high-performance liquid chromatography.
3661998	4	23	theme	oligosaccharide	826:840	arg1	structure					802:810	The structure	798:810	The structure of an unknown oligosaccharide	798:840	The structure of an unknown oligosaccharide can be characterized by comparison of its elution position with those of the standard compounds.
3661998	2	24	theme	carbohydrate	301:312	arg1	chains					314:319	carbohydrate chains	301:319	carbohydrate chains from glycopeptides	301:338	The method involves four steps: preparation of carbohydrate chains from glycopeptides by N-oligosaccharide glycopeptidase digestion; derivatization of the reducing ends of carbohydrate chains with a fluorescent reagent, 2-aminopyridine, by using sodium cyanoborohydride; separation of oligosaccharide derivatives by reverse-phase high-performance liquid chromatography; and structural analysis of oligosaccharides by sequential exoglycosidase digestion.
3661998	2	25	theme	fluorescent	453:463	arg1	2-aminopyridine					474:488	2-aminopyridine	474:488	2-aminopyridine	474:488	The method involves four steps: preparation of carbohydrate chains from glycopeptides by N-oligosaccharide glycopeptidase digestion; derivatization of the reducing ends of carbohydrate chains with a fluorescent reagent, 2-aminopyridine, by using sodium cyanoborohydride; separation of oligosaccharide derivatives by reverse-phase high-performance liquid chromatography; and structural analysis of oligosaccharides by sequential exoglycosidase digestion.
3661998	2	25	theme	fluorescent	453:463	arg1	reagent					465:471	a fluorescent reagent	451:471	a fluorescent reagent	451:471	The method involves four steps: preparation of carbohydrate chains from glycopeptides by N-oligosaccharide glycopeptidase digestion; derivatization of the reducing ends of carbohydrate chains with a fluorescent reagent, 2-aminopyridine, by using sodium cyanoborohydride; separation of oligosaccharide derivatives by reverse-phase high-performance liquid chromatography; and structural analysis of oligosaccharides by sequential exoglycosidase digestion.
3661998	4	26	with	comparison	866:875	arg1	those					906:910	those	906:910	those	906:910	The structure of an unknown oligosaccharide can be characterized by comparison of its elution position with those of the standard compounds.
3661998	0	27	theme	chromatography	130:143	arg1	combination					54:64	a combination	52:64	a combination of glycopeptidase, exoglycosidases, and high-performance liquid chromatography	52:143	Structural analysis of N-linked oligosaccharides by a combination of glycopeptidase, exoglycosidases, and high-performance liquid chromatography.
3661998	2	28	theme	sodium	500:505	arg1	cyanoborohydride					507:522	sodium cyanoborohydride	500:522	sodium cyanoborohydride	500:522	The method involves four steps: preparation of carbohydrate chains from glycopeptides by N-oligosaccharide glycopeptidase digestion; derivatization of the reducing ends of carbohydrate chains with a fluorescent reagent, 2-aminopyridine, by using sodium cyanoborohydride; separation of oligosaccharide derivatives by reverse-phase high-performance liquid chromatography; and structural analysis of oligosaccharides by sequential exoglycosidase digestion.
3661998	5	29	theme	myeloma	1017:1023	arg1	Yot					1038:1040	Yot	1038:1040	Yot	1038:1040	The method was applied to elucidate the structures of oligosaccharides in the myeloma IgG protein, Yot.
3661998	5	29	theme	myeloma	1017:1023	arg1	protein					1029:1035	the myeloma IgG protein	1013:1035	the myeloma IgG protein	1013:1035	The method was applied to elucidate the structures of oligosaccharides in the myeloma IgG protein, Yot.
3661998	2	30	theme	liquid	601:606	arg1	chromatography					608:621	reverse-phase high-performance liquid chromatography	570:621	reverse-phase high-performance liquid chromatography	570:621	The method involves four steps: preparation of carbohydrate chains from glycopeptides by N-oligosaccharide glycopeptidase digestion; derivatization of the reducing ends of carbohydrate chains with a fluorescent reagent, 2-aminopyridine, by using sodium cyanoborohydride; separation of oligosaccharide derivatives by reverse-phase high-performance liquid chromatography; and structural analysis of oligosaccharides by sequential exoglycosidase digestion.
3661998	2	31	theme	chains	439:444	arg1	ends					418:421	the reducing ends	405:421	the reducing ends of carbohydrate chains with a fluorescent reagent, 2-aminopyridine,	405:489	The method involves four steps: preparation of carbohydrate chains from glycopeptides by N-oligosaccharide glycopeptidase digestion; derivatization of the reducing ends of carbohydrate chains with a fluorescent reagent, 2-aminopyridine, by using sodium cyanoborohydride; separation of oligosaccharide derivatives by reverse-phase high-performance liquid chromatography; and structural analysis of oligosaccharides by sequential exoglycosidase digestion.
3661998	1	32	theme	structures	204:213	arg1	analysis					192:199	the analysis	188:199	the analysis of structures of N-linked carbohydrates	188:239	A simple, sensitive, and rapid method for the analysis of structures of N-linked carbohydrates is reported.
3661998	0	33	theme	oligosaccharides	32:47	arg1	analysis					11:18	Structural analysis	0:18	Structural analysis of N-linked oligosaccharides by a combination of glycopeptidase, exoglycosidases, and high-performance liquid chromatography.	0:144	Structural analysis of N-linked oligosaccharides by a combination of glycopeptidase, exoglycosidases, and high-performance liquid chromatography.
3661998	2	34	theme	high-performance	584:599	arg1	chromatography					608:621	reverse-phase high-performance liquid chromatography	570:621	reverse-phase high-performance liquid chromatography	570:621	The method involves four steps: preparation of carbohydrate chains from glycopeptides by N-oligosaccharide glycopeptidase digestion; derivatization of the reducing ends of carbohydrate chains with a fluorescent reagent, 2-aminopyridine, by using sodium cyanoborohydride; separation of oligosaccharide derivatives by reverse-phase high-performance liquid chromatography; and structural analysis of oligosaccharides by sequential exoglycosidase digestion.
3661998	2	35	theme	oligosaccharide	539:553	arg1	derivatives					555:565	oligosaccharide derivatives	539:565	oligosaccharide derivatives	539:565	The method involves four steps: preparation of carbohydrate chains from glycopeptides by N-oligosaccharide glycopeptidase digestion; derivatization of the reducing ends of carbohydrate chains with a fluorescent reagent, 2-aminopyridine, by using sodium cyanoborohydride; separation of oligosaccharide derivatives by reverse-phase high-performance liquid chromatography; and structural analysis of oligosaccharides by sequential exoglycosidase digestion.
3661998	2	36	theme	derivatives	555:565	arg1	separation					525:534	separation	525:534	separation of oligosaccharide derivatives by reverse-phase high-performance liquid chromatography	525:621	The method involves four steps: preparation of carbohydrate chains from glycopeptides by N-oligosaccharide glycopeptidase digestion; derivatization of the reducing ends of carbohydrate chains with a fluorescent reagent, 2-aminopyridine, by using sodium cyanoborohydride; separation of oligosaccharide derivatives by reverse-phase high-performance liquid chromatography; and structural analysis of oligosaccharides by sequential exoglycosidase digestion.
3661998	2	36	theme	derivatives	555:565	arg1	cyanoborohydride					507:522	sodium cyanoborohydride	500:522	sodium cyanoborohydride	500:522	The method involves four steps: preparation of carbohydrate chains from glycopeptides by N-oligosaccharide glycopeptidase digestion; derivatization of the reducing ends of carbohydrate chains with a fluorescent reagent, 2-aminopyridine, by using sodium cyanoborohydride; separation of oligosaccharide derivatives by reverse-phase high-performance liquid chromatography; and structural analysis of oligosaccharides by sequential exoglycosidase digestion.
3661998	2	36	theme	derivatives	555:565	arg1	analysis					639:646	structural analysis	628:646	structural analysis of oligosaccharides by sequential exoglycosidase digestion	628:705	The method involves four steps: preparation of carbohydrate chains from glycopeptides by N-oligosaccharide glycopeptidase digestion; derivatization of the reducing ends of carbohydrate chains with a fluorescent reagent, 2-aminopyridine, by using sodium cyanoborohydride; separation of oligosaccharide derivatives by reverse-phase high-performance liquid chromatography; and structural analysis of oligosaccharides by sequential exoglycosidase digestion.
3661998	2	37	theme	structural	628:637	arg1	analysis					639:646	structural analysis	628:646	structural analysis of oligosaccharides by sequential exoglycosidase digestion	628:705	The method involves four steps: preparation of carbohydrate chains from glycopeptides by N-oligosaccharide glycopeptidase digestion; derivatization of the reducing ends of carbohydrate chains with a fluorescent reagent, 2-aminopyridine, by using sodium cyanoborohydride; separation of oligosaccharide derivatives by reverse-phase high-performance liquid chromatography; and structural analysis of oligosaccharides by sequential exoglycosidase digestion.
3661998	2	38	theme	glycopeptidase	361:374	arg1	digestion					376:384	N-oligosaccharide glycopeptidase digestion	343:384	N-oligosaccharide glycopeptidase digestion	343:384	The method involves four steps: preparation of carbohydrate chains from glycopeptides by N-oligosaccharide glycopeptidase digestion; derivatization of the reducing ends of carbohydrate chains with a fluorescent reagent, 2-aminopyridine, by using sodium cyanoborohydride; separation of oligosaccharide derivatives by reverse-phase high-performance liquid chromatography; and structural analysis of oligosaccharides by sequential exoglycosidase digestion.
3661998	4	39	theme	standard	919:926	arg1	compounds					928:936	the standard compounds	915:936	the standard compounds	915:936	The structure of an unknown oligosaccharide can be characterized by comparison of its elution position with those of the standard compounds.
3661998	2	40	theme	N-oligosaccharide	343:359	arg1	digestion					376:384	N-oligosaccharide glycopeptidase digestion	343:384	N-oligosaccharide glycopeptidase digestion	343:384	The method involves four steps: preparation of carbohydrate chains from glycopeptides by N-oligosaccharide glycopeptidase digestion; derivatization of the reducing ends of carbohydrate chains with a fluorescent reagent, 2-aminopyridine, by using sodium cyanoborohydride; separation of oligosaccharide derivatives by reverse-phase high-performance liquid chromatography; and structural analysis of oligosaccharides by sequential exoglycosidase digestion.
3661998	2	41	gly	glycopeptides	326:338	arg2	glycopeptides					326:338	glycopeptides	326:338	glycopeptides	326:338	The method involves four steps: preparation of carbohydrate chains from glycopeptides by N-oligosaccharide glycopeptidase digestion; derivatization of the reducing ends of carbohydrate chains with a fluorescent reagent, 2-aminopyridine, by using sodium cyanoborohydride; separation of oligosaccharide derivatives by reverse-phase high-performance liquid chromatography; and structural analysis of oligosaccharides by sequential exoglycosidase digestion.
3661998	4	42	theme	position	892:899	arg1	comparison					866:875	comparison	866:875	comparison of its elution position with those of the standard compounds	866:936	The structure of an unknown oligosaccharide can be characterized by comparison of its elution position with those of the standard compounds.
3661998	4	43	theme	unknown	818:824	arg1	oligosaccharide					826:840	an unknown oligosaccharide	815:840	an unknown oligosaccharide	815:840	The structure of an unknown oligosaccharide can be characterized by comparison of its elution position with those of the standard compounds.
3661998	1	44	theme	N-linked	218:225	arg1	carbohydrates					227:239	N-linked carbohydrates	218:239	N-linked carbohydrates	218:239	A simple, sensitive, and rapid method for the analysis of structures of N-linked carbohydrates is reported.
3661998	3	45	theme	oligosaccharide	745:759	arg1	derivatives					761:771	50 standard oligosaccharide derivatives	733:771	50 standard oligosaccharide derivatives	733:771	The elution positions of 50 standard oligosaccharide derivatives were determined by HPLC.
3661998	3	46	theme	elution	712:718	arg1	positions					720:728	The elution positions	708:728	The elution positions of 50 standard oligosaccharide derivatives	708:771	The elution positions of 50 standard oligosaccharide derivatives were determined by HPLC.
3661998	1	47	theme	simple	148:153	arg1	method					177:182	A simple, sensitive, and rapid method	146:182	A simple, sensitive, and rapid method for the analysis of structures of N-linked carbohydrates	146:239	A simple, sensitive, and rapid method for the analysis of structures of N-linked carbohydrates is reported.
3661998	2	48	from	preparation	286:296	arg1	glycopeptides					326:338	glycopeptides	326:338	glycopeptides	326:338	The method involves four steps: preparation of carbohydrate chains from glycopeptides by N-oligosaccharide glycopeptidase digestion; derivatization of the reducing ends of carbohydrate chains with a fluorescent reagent, 2-aminopyridine, by using sodium cyanoborohydride; separation of oligosaccharide derivatives by reverse-phase high-performance liquid chromatography; and structural analysis of oligosaccharides by sequential exoglycosidase digestion.
3661998	1	49	theme	carbohydrates	227:239	arg1	structures					204:213	structures	204:213	structures of N-linked carbohydrates	204:239	A simple, sensitive, and rapid method for the analysis of structures of N-linked carbohydrates is reported.
3661998	0	50	theme	glycopeptidase	69:82	arg1	combination					54:64	a combination	52:64	a combination of glycopeptidase, exoglycosidases, and high-performance liquid chromatography	52:143	Structural analysis of N-linked oligosaccharides by a combination of glycopeptidase, exoglycosidases, and high-performance liquid chromatography.
3661998	2	51	theme	carbohydrate	426:437	arg1	chains					439:444	carbohydrate chains	426:444	carbohydrate chains with a fluorescent reagent, 2-aminopyridine,	426:489	The method involves four steps: preparation of carbohydrate chains from glycopeptides by N-oligosaccharide glycopeptidase digestion; derivatization of the reducing ends of carbohydrate chains with a fluorescent reagent, 2-aminopyridine, by using sodium cyanoborohydride; separation of oligosaccharide derivatives by reverse-phase high-performance liquid chromatography; and structural analysis of oligosaccharides by sequential exoglycosidase digestion.
3661998	2	52	dep	steps	279:283	arg1	preparation					286:296	preparation	286:296	four steps: preparation of carbohydrate chains from glycopeptides by N-oligosaccharide glycopeptidase digestion; derivatization of the reducing ends of carbohydrate chains with a fluorescent reagent, 2-aminopyridine,	274:489	The method involves four steps: preparation of carbohydrate chains from glycopeptides by N-oligosaccharide glycopeptidase digestion; derivatization of the reducing ends of carbohydrate chains with a fluorescent reagent, 2-aminopyridine, by using sodium cyanoborohydride; separation of oligosaccharide derivatives by reverse-phase high-performance liquid chromatography; and structural analysis of oligosaccharides by sequential exoglycosidase digestion.
3661998	2	52	dep	steps	279:283	arg1	derivatization					387:400	derivatization	387:400	four steps: preparation of carbohydrate chains from glycopeptides by N-oligosaccharide glycopeptidase digestion; derivatization of the reducing ends of carbohydrate chains with a fluorescent reagent, 2-aminopyridine,	274:489	The method involves four steps: preparation of carbohydrate chains from glycopeptides by N-oligosaccharide glycopeptidase digestion; derivatization of the reducing ends of carbohydrate chains with a fluorescent reagent, 2-aminopyridine, by using sodium cyanoborohydride; separation of oligosaccharide derivatives by reverse-phase high-performance liquid chromatography; and structural analysis of oligosaccharides by sequential exoglycosidase digestion.
3661998	1	53	theme	sensitive	156:164	arg1	method					177:182	A simple, sensitive, and rapid method	146:182	A simple, sensitive, and rapid method for the analysis of structures of N-linked carbohydrates	146:239	A simple, sensitive, and rapid method for the analysis of structures of N-linked carbohydrates is reported.
11738084	0	0	theme	human	67:71	arg1	albumin					79:85	human serum albumin	67:85	human serum albumin	67:85	The glycan structure of albumin Redhill, a glycosylated variant of human serum albumin.
11738084	6	1	theme	albumin	817:823	arg1	variants					825:832	glycosylated albumin variants	804:832	glycosylated albumin variants	804:832	The structure is principally the same as that of glycans bound to two other types of glycosylated albumin variants.
11738084	7	2	theme	fatty	878:882	arg1	properties					897:906	the fatty acid binding properties	874:906	the fatty acid binding properties of albumin	874:917	Glycosylation can affect, for example, the fatty acid binding properties of albumin.
11738084	3	3	theme	array	466:470	arg1	method					481:486	a reagent array analysis method	456:486	a reagent array analysis method	456:486	The oligosaccharide was released from the protein using anhydrous hydrazine, and its structure was investigated using neuraminidase and a reagent array analysis method, which is based on the use of specific exoglycosidases.
11738084	5	4	theme	glycan	687:692	arg1	%					677:677	11 mol%	671:677	11 mol%	671:677	However, a minor part (11 mol%) of the glycan was without sialic acid.
11738084	5	4	theme	glycan	687:692	arg1	part					665:668	a minor part	657:668	a minor part (11 mol%) of the glycan	657:692	However, a minor part (11 mol%) of the glycan was without sialic acid.
11738084	6	5	theme	glycosylated	804:815	arg1	variants					825:832	glycosylated albumin variants	804:832	glycosylated albumin variants	804:832	The structure is principally the same as that of glycans bound to two other types of glycosylated albumin variants.
11738084	1	6	gly	glycosylated	154:165	arg1	variants					167:174	glycosylated variants	154:174	glycosylated variants of the protein	154:189	Although human serum albumin is synthesized without carbohydrate, glycosylated variants of the protein can be found.
11738084	3	7	theme	analysis	472:479	arg1	method					481:486	a reagent array analysis method	456:486	a reagent array analysis method	456:486	The oligosaccharide was released from the protein using anhydrous hydrazine, and its structure was investigated using neuraminidase and a reagent array analysis method, which is based on the use of specific exoglycosidases.
11738084	0	8	theme	albumin	79:85	arg1	variant					56:62	a glycosylated variant	41:62	a glycosylated variant of human serum albumin	41:85	The glycan structure of albumin Redhill, a glycosylated variant of human serum albumin.
11738084	0	9	dep	Redhill	32:38	arg1	structure					11:19	The glycan structure	0:19	The glycan structure of albumin	0:30	The glycan structure of albumin Redhill, a glycosylated variant of human serum albumin.
11738084	0	9	dep	Redhill	32:38	arg1	variant					56:62	a glycosylated variant	41:62	a glycosylated variant of human serum albumin	41:85	The glycan structure of albumin Redhill, a glycosylated variant of human serum albumin.
11738084	0	10	gly	glycosylated	43:54	arg1	variant					56:62	a glycosylated variant	41:62	a glycosylated variant of human serum albumin	41:85	The glycan structure of albumin Redhill, a glycosylated variant of human serum albumin.
11738084	6	11	gly	glycosylated	804:815	arg1	variants					825:832	glycosylated albumin variants	804:832	glycosylated albumin variants	804:832	The structure is principally the same as that of glycans bound to two other types of glycosylated albumin variants.
11738084	0	12	theme	serum	73:77	arg1	albumin					79:85	human serum albumin	67:85	human serum albumin	67:85	The glycan structure of albumin Redhill, a glycosylated variant of human serum albumin.
11738084	8	13	theme	present	931:937	arg1	information					939:949	the present information	927:949	the present information	927:949	Taking the present information into account, it is apparent that different effects on binding are caused not by different glycan structures but by different locations of attachment, with the possible addition of local conformational changes in the protein molecule.
11738084	8	14	from	effects	995:1001	arg1	binding					1006:1012	binding	1006:1012	binding	1006:1012	Taking the present information into account, it is apparent that different effects on binding are caused not by different glycan structures but by different locations of attachment, with the possible addition of local conformational changes in the protein molecule.
11738084	5	15	theme	mol	674:676	arg1	%					677:677	11 mol%	671:677	11 mol%	671:677	However, a minor part (11 mol%) of the glycan was without sialic acid.
11738084	5	15	theme	mol	674:676	arg1	part					665:668	a minor part	657:668	a minor part (11 mol%) of the glycan	657:692	However, a minor part (11 mol%) of the glycan was without sialic acid.
11738084	6	16	theme	other	789:793	arg1	types					795:799	two other types	785:799	two other types of glycosylated albumin variants	785:832	The structure is principally the same as that of glycans bound to two other types of glycosylated albumin variants.
11738084	8	17	from	molecule	1176:1183	arg1	addition					1120:1127	the possible addition	1107:1127	the possible addition of local conformational changes in the protein molecule	1107:1183	Taking the present information into account, it is apparent that different effects on binding are caused not by different glycan structures but by different locations of attachment, with the possible addition of local conformational changes in the protein molecule.
11738084	1	18	theme	glycosylated	154:165	arg1	variants					167:174	glycosylated variants	154:174	glycosylated variants of the protein	154:189	Although human serum albumin is synthesized without carbohydrate, glycosylated variants of the protein can be found.
11738084	4	19	gly	disialylated	573:584	arg1	oligosaccharide					611:625	a disialylated biantennary complex type oligosaccharide	571:625	a disialylated biantennary complex type oligosaccharide N-linked to 318 Asn	571:645	The glycan was shown to be a disialylated biantennary complex type oligosaccharide N-linked to 318 Asn.
11738084	4	19	gly	disialylated	573:584	arg1	glycan					548:553	The glycan	544:553	The glycan	544:553	The glycan was shown to be a disialylated biantennary complex type oligosaccharide N-linked to 318 Asn.
11738084	2	20	theme	glycan	245:250	arg1	structure					228:236	the structure	224:236	the structure of the glycan bound to the double-mutant albumin Redhill (-1 Arg, 320 Ala-->Thr)	224:317	We have determined the structure of the glycan bound to the double-mutant albumin Redhill (-1 Arg, 320 Ala-->Thr).
11738084	4	21	theme	type	606:609	arg1	oligosaccharide					611:625	a disialylated biantennary complex type oligosaccharide	571:625	a disialylated biantennary complex type oligosaccharide N-linked to 318 Asn	571:645	The glycan was shown to be a disialylated biantennary complex type oligosaccharide N-linked to 318 Asn.
11738084	4	21	theme	type	606:609	arg1	glycan					548:553	The glycan	544:553	The glycan	544:553	The glycan was shown to be a disialylated biantennary complex type oligosaccharide N-linked to 318 Asn.
11738084	0	22	theme	glycan	4:9	arg1	structure					11:19	The glycan structure	0:19	The glycan structure of albumin	0:30	The glycan structure of albumin Redhill, a glycosylated variant of human serum albumin.
11738084	8	23	theme	conformational	1138:1151	arg1	changes					1153:1159	local conformational changes	1132:1159	local conformational changes in the protein molecule	1132:1183	Taking the present information into account, it is apparent that different effects on binding are caused not by different glycan structures but by different locations of attachment, with the possible addition of local conformational changes in the protein molecule.
11738084	8	24	theme	different	985:993	arg1	effects					995:1001	different effects	985:1001	different effects on binding	985:1012	Taking the present information into account, it is apparent that different effects on binding are caused not by different glycan structures but by different locations of attachment, with the possible addition of local conformational changes in the protein molecule.
11738084	3	25	theme	specific	518:525	arg1	exoglycosidases					527:541	specific exoglycosidases	518:541	specific exoglycosidases	518:541	The oligosaccharide was released from the protein using anhydrous hydrazine, and its structure was investigated using neuraminidase and a reagent array analysis method, which is based on the use of specific exoglycosidases.
11738084	8	26	theme	different	1032:1040	arg1	structures					1049:1058	different glycan structures	1032:1058	different glycan structures	1032:1058	Taking the present information into account, it is apparent that different effects on binding are caused not by different glycan structures but by different locations of attachment, with the possible addition of local conformational changes in the protein molecule.
11738084	4	27	theme	N-linked	627:634	arg1	oligosaccharide					611:625	a disialylated biantennary complex type oligosaccharide	571:625	a disialylated biantennary complex type oligosaccharide N-linked to 318 Asn	571:645	The glycan was shown to be a disialylated biantennary complex type oligosaccharide N-linked to 318 Asn.
11738084	4	27	theme	N-linked	627:634	arg1	glycan					548:553	The glycan	544:553	The glycan	544:553	The glycan was shown to be a disialylated biantennary complex type oligosaccharide N-linked to 318 Asn.
11738084	8	28	theme	attachment	1090:1099	arg1	locations					1077:1085	different locations	1067:1085	different locations of attachment	1067:1099	Taking the present information into account, it is apparent that different effects on binding are caused not by different glycan structures but by different locations of attachment, with the possible addition of local conformational changes in the protein molecule.
11738084	2	29	theme	albumin	279:285	arg1	Redhill					287:293	the double-mutant albumin Redhill	261:293	the double-mutant albumin Redhill (-1 Arg, 320 Ala-->Thr)	261:317	We have determined the structure of the glycan bound to the double-mutant albumin Redhill (-1 Arg, 320 Ala-->Thr).
11738084	1	30	theme	protein	183:189	arg1	variants					167:174	glycosylated variants	154:174	glycosylated variants of the protein	154:189	Although human serum albumin is synthesized without carbohydrate, glycosylated variants of the protein can be found.
11738084	7	31	theme	binding	889:895	arg1	properties					897:906	the fatty acid binding properties	874:906	the fatty acid binding properties of albumin	874:917	Glycosylation can affect, for example, the fatty acid binding properties of albumin.
11738084	2	32	theme	double-mutant	265:277	arg1	Redhill					287:293	the double-mutant albumin Redhill	261:293	the double-mutant albumin Redhill (-1 Arg, 320 Ala-->Thr)	261:317	We have determined the structure of the glycan bound to the double-mutant albumin Redhill (-1 Arg, 320 Ala-->Thr).
11738084	8	33	theme	changes	1153:1159	arg1	addition					1120:1127	the possible addition	1107:1127	the possible addition of local conformational changes in the protein molecule	1107:1183	Taking the present information into account, it is apparent that different effects on binding are caused not by different glycan structures but by different locations of attachment, with the possible addition of local conformational changes in the protein molecule.
11738084	3	34	theme	reagent	458:464	arg1	method					481:486	a reagent array analysis method	456:486	a reagent array analysis method	456:486	The oligosaccharide was released from the protein using anhydrous hydrazine, and its structure was investigated using neuraminidase and a reagent array analysis method, which is based on the use of specific exoglycosidases.
11738084	5	35	theme	minor	659:663	arg1	%					677:677	11 mol%	671:677	11 mol%	671:677	However, a minor part (11 mol%) of the glycan was without sialic acid.
11738084	5	35	theme	minor	659:663	arg1	part					665:668	a minor part	657:668	a minor part (11 mol%) of the glycan	657:692	However, a minor part (11 mol%) of the glycan was without sialic acid.
11738084	8	36	theme	protein	1168:1174	arg1	molecule					1176:1183	the protein molecule	1164:1183	the protein molecule	1164:1183	Taking the present information into account, it is apparent that different effects on binding are caused not by different glycan structures but by different locations of attachment, with the possible addition of local conformational changes in the protein molecule.
11738084	8	37	theme	local	1132:1136	arg1	changes					1153:1159	local conformational changes	1132:1159	local conformational changes in the protein molecule	1132:1183	Taking the present information into account, it is apparent that different effects on binding are caused not by different glycan structures but by different locations of attachment, with the possible addition of local conformational changes in the protein molecule.
11738084	4	38	theme	complex	598:604	arg1	oligosaccharide					611:625	a disialylated biantennary complex type oligosaccharide	571:625	a disialylated biantennary complex type oligosaccharide N-linked to 318 Asn	571:645	The glycan was shown to be a disialylated biantennary complex type oligosaccharide N-linked to 318 Asn.
11738084	4	38	theme	complex	598:604	arg1	glycan					548:553	The glycan	544:553	The glycan	544:553	The glycan was shown to be a disialylated biantennary complex type oligosaccharide N-linked to 318 Asn.
11738084	0	39	theme	albumin	24:30	arg1	structure					11:19	The glycan structure	0:19	The glycan structure of albumin	0:30	The glycan structure of albumin Redhill, a glycosylated variant of human serum albumin.
11738084	3	40	theme	anhydrous	376:384	arg1	hydrazine					386:394	anhydrous hydrazine	376:394	anhydrous hydrazine	376:394	The oligosaccharide was released from the protein using anhydrous hydrazine, and its structure was investigated using neuraminidase and a reagent array analysis method, which is based on the use of specific exoglycosidases.
11738084	4	41	link	N-linked	627:634	arg1	oligosaccharide					611:625	a disialylated biantennary complex type oligosaccharide	571:625	a disialylated biantennary complex type oligosaccharide N-linked to 318 Asn	571:645	The glycan was shown to be a disialylated biantennary complex type oligosaccharide N-linked to 318 Asn.
11738084	4	41	link	N-linked	627:634	arg1	glycan					548:553	The glycan	544:553	The glycan	544:553	The glycan was shown to be a disialylated biantennary complex type oligosaccharide N-linked to 318 Asn.
11738084	7	42	theme	albumin	911:917	arg1	properties					897:906	the fatty acid binding properties	874:906	the fatty acid binding properties of albumin	874:917	Glycosylation can affect, for example, the fatty acid binding properties of albumin.
11738084	4	43	theme	biantennary	586:596	arg1	oligosaccharide					611:625	a disialylated biantennary complex type oligosaccharide	571:625	a disialylated biantennary complex type oligosaccharide N-linked to 318 Asn	571:645	The glycan was shown to be a disialylated biantennary complex type oligosaccharide N-linked to 318 Asn.
11738084	4	43	theme	biantennary	586:596	arg1	glycan					548:553	The glycan	544:553	The glycan	544:553	The glycan was shown to be a disialylated biantennary complex type oligosaccharide N-linked to 318 Asn.
11738084	5	44	theme	sialic	706:711	arg1	acid					713:716	sialic acid	706:716	sialic acid	706:716	However, a minor part (11 mol%) of the glycan was without sialic acid.
11738084	3	45	theme	exoglycosidases	527:541	arg1	use					511:513	the use	507:513	the use of specific exoglycosidases	507:541	The oligosaccharide was released from the protein using anhydrous hydrazine, and its structure was investigated using neuraminidase and a reagent array analysis method, which is based on the use of specific exoglycosidases.
11738084	1	46	theme	human	97:101	arg1	albumin					109:115	human serum albumin	97:115	human serum albumin	97:115	Although human serum albumin is synthesized without carbohydrate, glycosylated variants of the protein can be found.
11738084	1	47	theme	serum	103:107	arg1	albumin					109:115	human serum albumin	97:115	human serum albumin	97:115	Although human serum albumin is synthesized without carbohydrate, glycosylated variants of the protein can be found.
11738084	3	48	attach	released	344:351	arg2	oligosaccharide					324:338	The oligosaccharide	320:338	The oligosaccharide	320:338	The oligosaccharide was released from the protein using anhydrous hydrazine, and its structure was investigated using neuraminidase and a reagent array analysis method, which is based on the use of specific exoglycosidases.
11738084	3	48	attach	released	344:351	arg1	protein					362:368	the protein	358:368	the protein using anhydrous hydrazine	358:394	The oligosaccharide was released from the protein using anhydrous hydrazine, and its structure was investigated using neuraminidase and a reagent array analysis method, which is based on the use of specific exoglycosidases.
11738084	8	49	from	addition	1120:1127	arg1	molecule					1176:1183	the protein molecule	1164:1183	the protein molecule	1164:1183	Taking the present information into account, it is apparent that different effects on binding are caused not by different glycan structures but by different locations of attachment, with the possible addition of local conformational changes in the protein molecule.
11738084	8	50	from	changes	1153:1159	arg1	molecule					1176:1183	the protein molecule	1164:1183	the protein molecule	1164:1183	Taking the present information into account, it is apparent that different effects on binding are caused not by different glycan structures but by different locations of attachment, with the possible addition of local conformational changes in the protein molecule.
11738084	8	51	theme	different	1067:1075	arg1	locations					1077:1085	different locations	1067:1085	different locations of attachment	1067:1099	Taking the present information into account, it is apparent that different effects on binding are caused not by different glycan structures but by different locations of attachment, with the possible addition of local conformational changes in the protein molecule.
11738084	7	52	theme	acid	884:887	arg1	properties					897:906	the fatty acid binding properties	874:906	the fatty acid binding properties of albumin	874:917	Glycosylation can affect, for example, the fatty acid binding properties of albumin.
11738084	2	53	dep	Redhill	287:293	arg1	Arg					299:301	-1 Arg	296:301	-1 Arg	296:301	We have determined the structure of the glycan bound to the double-mutant albumin Redhill (-1 Arg, 320 Ala-->Thr).
11738084	2	53	dep	Redhill	287:293	arg1	Ala-->Thr					308:316	320 Ala-->Thr	304:316	320 Ala-->Thr	304:316	We have determined the structure of the glycan bound to the double-mutant albumin Redhill (-1 Arg, 320 Ala-->Thr).
11738084	8	54	theme	possible	1111:1118	arg1	addition					1120:1127	the possible addition	1107:1127	the possible addition of local conformational changes in the protein molecule	1107:1183	Taking the present information into account, it is apparent that different effects on binding are caused not by different glycan structures but by different locations of attachment, with the possible addition of local conformational changes in the protein molecule.
11738084	4	55	theme	disialylated	573:584	arg1	oligosaccharide					611:625	a disialylated biantennary complex type oligosaccharide	571:625	a disialylated biantennary complex type oligosaccharide N-linked to 318 Asn	571:645	The glycan was shown to be a disialylated biantennary complex type oligosaccharide N-linked to 318 Asn.
11738084	4	55	theme	disialylated	573:584	arg1	glycan					548:553	The glycan	544:553	The glycan	544:553	The glycan was shown to be a disialylated biantennary complex type oligosaccharide N-linked to 318 Asn.
11738084	0	56	theme	glycosylated	43:54	arg1	variant					56:62	a glycosylated variant	41:62	a glycosylated variant of human serum albumin	41:85	The glycan structure of albumin Redhill, a glycosylated variant of human serum albumin.
11738084	6	57	theme	variants	825:832	arg1	types					795:799	two other types	785:799	two other types of glycosylated albumin variants	785:832	The structure is principally the same as that of glycans bound to two other types of glycosylated albumin variants.
11738084	8	58	theme	glycan	1042:1047	arg1	structures					1049:1058	different glycan structures	1032:1058	different glycan structures	1032:1058	Taking the present information into account, it is apparent that different effects on binding are caused not by different glycan structures but by different locations of attachment, with the possible addition of local conformational changes in the protein molecule.
30407017	4	0	theme	oxonium	575:581	arg1	ions					583:586	glycan oxonium ions	568:586	glycan oxonium ions	568:586	Unexpectedly, glycan oxonium ions indicated the presence of O-acetyl, and even O-diacetyl-sialic acids.
30407017	5	1	theme	core	701:704	arg1	structures					708:717	core 1 structures	701:717	core 1 structures	701:717	B and Y fragment ions revealed that (i) in core 1 structures the Gal residue featured the O-acetyl-sialic acid, when there was only one in the glycan; (ii) several glycopeptides featured core 1 glycans with disialic acids, in certain instances O-acetylated; (iii) the disialic acid was linked to the GalNAc residue whatever the degree of O-acetylation; (iv) core 2 isomers with a single O-acetyl-sialic acid were chromatographically resolved.
30407017	1	2	theme	electron-transfer/higher-energy	203:233	arg1	EThcD					259:263	EThcD	259:263	EThcD	259:263	A relatively novel activation technique, electron-transfer/higher-energy collision dissociation (EThcD) was used in the LC-MS/MS analysis of tryptic glycopeptides enriched with wheat germ agglutinin from human urine samples.
30407017	1	2	theme	electron-transfer/higher-energy	203:233	arg1	dissociation					245:256	electron-transfer/higher-energy collision dissociation	203:256	electron-transfer/higher-energy collision dissociation (EThcD)	203:264	A relatively novel activation technique, electron-transfer/higher-energy collision dissociation (EThcD) was used in the LC-MS/MS analysis of tryptic glycopeptides enriched with wheat germ agglutinin from human urine samples.
30407017	1	2	theme	electron-transfer/higher-energy	203:233	arg1	technique					192:200	A relatively novel activation technique	162:200	A relatively novel activation technique	162:200	A relatively novel activation technique, electron-transfer/higher-energy collision dissociation (EThcD) was used in the LC-MS/MS analysis of tryptic glycopeptides enriched with wheat germ agglutinin from human urine samples.
30407017	1	3	theme	glycopeptides	311:323	arg1	analysis					291:298	the LC-MS/MS analysis	278:298	the LC-MS/MS analysis of tryptic glycopeptides enriched with wheat germ agglutinin from human urine samples	278:384	A relatively novel activation technique, electron-transfer/higher-energy collision dissociation (EThcD) was used in the LC-MS/MS analysis of tryptic glycopeptides enriched with wheat germ agglutinin from human urine samples.
30407017	3	4	from	information	489:499	arg1	peptide					513:519	the peptide	509:519	the peptide modified	509:528	EThcD in a single spectrum provided information on both the peptide modified and the glycan carried.
30407017	3	4	from	information	489:499	arg1	glycan					538:543	the glycan	534:543	the glycan carried	534:551	EThcD in a single spectrum provided information on both the peptide modified and the glycan carried.
30407017	5	5	theme	fragment	666:673	arg1	ions					675:678	fragment ions	666:678	fragment ions	666:678	B and Y fragment ions revealed that (i) in core 1 structures the Gal residue featured the O-acetyl-sialic acid, when there was only one in the glycan; (ii) several glycopeptides featured core 1 glycans with disialic acids, in certain instances O-acetylated; (iii) the disialic acid was linked to the GalNAc residue whatever the degree of O-acetylation; (iv) core 2 isomers with a single O-acetyl-sialic acid were chromatographically resolved.
30407017	1	6	theme	collision	235:243	arg1	EThcD					259:263	EThcD	259:263	EThcD	259:263	A relatively novel activation technique, electron-transfer/higher-energy collision dissociation (EThcD) was used in the LC-MS/MS analysis of tryptic glycopeptides enriched with wheat germ agglutinin from human urine samples.
30407017	1	6	theme	collision	235:243	arg1	dissociation					245:256	electron-transfer/higher-energy collision dissociation	203:256	electron-transfer/higher-energy collision dissociation (EThcD)	203:264	A relatively novel activation technique, electron-transfer/higher-energy collision dissociation (EThcD) was used in the LC-MS/MS analysis of tryptic glycopeptides enriched with wheat germ agglutinin from human urine samples.
30407017	1	6	theme	collision	235:243	arg1	technique					192:200	A relatively novel activation technique	162:200	A relatively novel activation technique	162:200	A relatively novel activation technique, electron-transfer/higher-energy collision dissociation (EThcD) was used in the LC-MS/MS analysis of tryptic glycopeptides enriched with wheat germ agglutinin from human urine samples.
30407017	8	7	theme	first	1369:1373	arg1	this					1357:1360	this	1357:1360	this	1357:1360	We believe this is the first study when such structures were characterized from a very complex mixture and were linked not only to a specific protein, but also the sites of modifications have been determined.
30407017	8	7	theme	first	1369:1373	arg1	study					1375:1379	the first study	1365:1379	the first study when such structures were characterized from a very complex mixture and were linked not only to a specific protein	1365:1494	We believe this is the first study when such structures were characterized from a very complex mixture and were linked not only to a specific protein, but also the sites of modifications have been determined.
30407017	8	8	dep	protein	1488:1494	arg1	only					1469:1472	only	1469:1472	only	1469:1472	We believe this is the first study when such structures were characterized from a very complex mixture and were linked not only to a specific protein, but also the sites of modifications have been determined.
30407017	0	9	theme	Collision	138:146	arg1	Dissociation					148:159	Electron-Transfer/Higher-Energy Collision Dissociation	106:159	Electron-Transfer/Higher-Energy Collision Dissociation	106:159	Extended Sialylated O-Glycan Repertoire of Human Urinary Glycoproteins Discovered and Characterized Using Electron-Transfer/Higher-Energy Collision Dissociation.
30407017	8	10	theme	modifications	1519:1531	arg1	modifications					1519:1531	modifications	1519:1531	modifications	1519:1531	We believe this is the first study when such structures were characterized from a very complex mixture and were linked not only to a specific protein, but also the sites of modifications have been determined.
30407017	8	10	theme	modifications	1519:1531	arg1	sites					1510:1514	the sites	1506:1514	the sites of modifications	1506:1531	We believe this is the first study when such structures were characterized from a very complex mixture and were linked not only to a specific protein, but also the sites of modifications have been determined.
30407017	5	11	dep	featured	836:843	arg1	ii					810:811	ii	810:811	ii	810:811	B and Y fragment ions revealed that (i) in core 1 structures the Gal residue featured the O-acetyl-sialic acid, when there was only one in the glycan; (ii) several glycopeptides featured core 1 glycans with disialic acids, in certain instances O-acetylated; (iii) the disialic acid was linked to the GalNAc residue whatever the degree of O-acetylation; (iv) core 2 isomers with a single O-acetyl-sialic acid were chromatographically resolved.
30407017	5	12	theme	GalNAc	958:963	arg1	residue					965:971	the GalNAc residue	954:971	the GalNAc residue whatever the degree of O-acetylation; (iv) core 2 isomers with a single O-acetyl-sialic acid were chromatographically resolved	954:1098	B and Y fragment ions revealed that (i) in core 1 structures the Gal residue featured the O-acetyl-sialic acid, when there was only one in the glycan; (ii) several glycopeptides featured core 1 glycans with disialic acids, in certain instances O-acetylated; (iii) the disialic acid was linked to the GalNAc residue whatever the degree of O-acetylation; (iv) core 2 isomers with a single O-acetyl-sialic acid were chromatographically resolved.
30407017	5	13	dep	B	658:658	arg1	ions					675:678	fragment ions	666:678	fragment ions	666:678	B and Y fragment ions revealed that (i) in core 1 structures the Gal residue featured the O-acetyl-sialic acid, when there was only one in the glycan; (ii) several glycopeptides featured core 1 glycans with disialic acids, in certain instances O-acetylated; (iii) the disialic acid was linked to the GalNAc residue whatever the degree of O-acetylation; (iv) core 2 isomers with a single O-acetyl-sialic acid were chromatographically resolved.
30407017	0	14	theme	Electron-Transfer/Higher-Energy	106:136	arg1	Dissociation					148:159	Electron-Transfer/Higher-Energy Collision Dissociation	106:159	Electron-Transfer/Higher-Energy Collision Dissociation	106:159	Extended Sialylated O-Glycan Repertoire of Human Urinary Glycoproteins Discovered and Characterized Using Electron-Transfer/Higher-Energy Collision Dissociation.
30407017	3	15	from	EThcD	453:457	arg1	spectrum					471:478	a single spectrum	462:478	a single spectrum	462:478	EThcD in a single spectrum provided information on both the peptide modified and the glycan carried.
30407017	1	16	from	samples	378:384	arg1	agglutinin					350:359	wheat germ agglutinin	339:359	wheat germ agglutinin from human urine samples	339:384	A relatively novel activation technique, electron-transfer/higher-energy collision dissociation (EThcD) was used in the LC-MS/MS analysis of tryptic glycopeptides enriched with wheat germ agglutinin from human urine samples.
30407017	2	17	theme	mucin-type	425:434	arg1	O-glycopeptides					436:450	mucin-type O-glycopeptides	425:450	mucin-type O-glycopeptides	425:450	We focused on the characterization of mucin-type O-glycopeptides.
30407017	1	18	theme	wheat	339:343	arg1	agglutinin					350:359	wheat germ agglutinin	339:359	wheat germ agglutinin from human urine samples	339:384	A relatively novel activation technique, electron-transfer/higher-energy collision dissociation (EThcD) was used in the LC-MS/MS analysis of tryptic glycopeptides enriched with wheat germ agglutinin from human urine samples.
30407017	5	19	theme	several	814:820	arg1	glycopeptides					822:834	several glycopeptides	814:834	several glycopeptides	814:834	B and Y fragment ions revealed that (i) in core 1 structures the Gal residue featured the O-acetyl-sialic acid, when there was only one in the glycan; (ii) several glycopeptides featured core 1 glycans with disialic acids, in certain instances O-acetylated; (iii) the disialic acid was linked to the GalNAc residue whatever the degree of O-acetylation; (iv) core 2 isomers with a single O-acetyl-sialic acid were chromatographically resolved.
30407017	4	20	theme	glycan	568:573	arg1	ions					583:586	glycan oxonium ions	568:586	glycan oxonium ions	568:586	Unexpectedly, glycan oxonium ions indicated the presence of O-acetyl, and even O-diacetyl-sialic acids.
30407017	6	21	theme	O-acetylation	1265:1277	arg1	stages					1255:1260	different stages	1245:1260	different stages of O-acetylation	1245:1277	Glycan fragmentation also helped to decipher additional core 2 oligosaccharides: a LacdiNAc-like structure, glycans carrying sialyl LewisX/A at different stages of O-acetylation, and blood antigens.
30407017	3	22	theme	single	464:469	arg1	spectrum					471:478	a single spectrum	462:478	a single spectrum	462:478	EThcD in a single spectrum provided information on both the peptide modified and the glycan carried.
30407017	0	23	theme	Sialylated	9:18	arg1	Repertoire					29:38	Extended Sialylated O-Glycan Repertoire	0:38	Extended Sialylated O-Glycan Repertoire of Human Urinary Glycoproteins	0:69	Extended Sialylated O-Glycan Repertoire of Human Urinary Glycoproteins Discovered and Characterized Using Electron-Transfer/Higher-Energy Collision Dissociation.
30407017	0	23	theme	Sialylated	9:18	arg1	Glycoproteins					57:69	Human Urinary Glycoproteins	43:69	Human Urinary Glycoproteins	43:69	Extended Sialylated O-Glycan Repertoire of Human Urinary Glycoproteins Discovered and Characterized Using Electron-Transfer/Higher-Energy Collision Dissociation.
30407017	4	24	theme	O-diacetyl-sialic	633:649	arg1	acids					651:655	O-diacetyl-sialic acids	633:655	O-diacetyl-sialic acids	633:655	Unexpectedly, glycan oxonium ions indicated the presence of O-acetyl, and even O-diacetyl-sialic acids.
30407017	1	25	gly	glycopeptides	311:323	arg2	glycopeptides					311:323	tryptic glycopeptides	303:323	tryptic glycopeptides enriched with wheat germ agglutinin from human urine samples	303:384	A relatively novel activation technique, electron-transfer/higher-energy collision dissociation (EThcD) was used in the LC-MS/MS analysis of tryptic glycopeptides enriched with wheat germ agglutinin from human urine samples.
30407017	5	26	with	isomers	1023:1029	arg1	acid					1061:1064	a single O-acetyl-sialic acid	1036:1064	a single O-acetyl-sialic acid	1036:1064	B and Y fragment ions revealed that (i) in core 1 structures the Gal residue featured the O-acetyl-sialic acid, when there was only one in the glycan; (ii) several glycopeptides featured core 1 glycans with disialic acids, in certain instances O-acetylated; (iii) the disialic acid was linked to the GalNAc residue whatever the degree of O-acetylation; (iv) core 2 isomers with a single O-acetyl-sialic acid were chromatographically resolved.
30407017	5	27	theme	certain	884:890	arg1	instances					892:900	certain instances	884:900	certain instances O-acetylated	884:913	B and Y fragment ions revealed that (i) in core 1 structures the Gal residue featured the O-acetyl-sialic acid, when there was only one in the glycan; (ii) several glycopeptides featured core 1 glycans with disialic acids, in certain instances O-acetylated; (iii) the disialic acid was linked to the GalNAc residue whatever the degree of O-acetylation; (iv) core 2 isomers with a single O-acetyl-sialic acid were chromatographically resolved.
30407017	0	28	theme	Extended	0:7	arg1	Repertoire					29:38	Extended Sialylated O-Glycan Repertoire	0:38	Extended Sialylated O-Glycan Repertoire of Human Urinary Glycoproteins	0:69	Extended Sialylated O-Glycan Repertoire of Human Urinary Glycoproteins Discovered and Characterized Using Electron-Transfer/Higher-Energy Collision Dissociation.
30407017	0	28	theme	Extended	0:7	arg1	Glycoproteins					57:69	Human Urinary Glycoproteins	43:69	Human Urinary Glycoproteins	43:69	Extended Sialylated O-Glycan Repertoire of Human Urinary Glycoproteins Discovered and Characterized Using Electron-Transfer/Higher-Energy Collision Dissociation.
30407017	1	29	theme	germ	345:348	arg1	agglutinin					350:359	wheat germ agglutinin	339:359	wheat germ agglutinin from human urine samples	339:384	A relatively novel activation technique, electron-transfer/higher-energy collision dissociation (EThcD) was used in the LC-MS/MS analysis of tryptic glycopeptides enriched with wheat germ agglutinin from human urine samples.
30407017	6	30	theme	core	1157:1160	arg1	oligosaccharides					1164:1179	additional core 2 oligosaccharides	1146:1179	additional core 2 oligosaccharides	1146:1179	Glycan fragmentation also helped to decipher additional core 2 oligosaccharides: a LacdiNAc-like structure, glycans carrying sialyl LewisX/A at different stages of O-acetylation, and blood antigens.
30407017	8	31	theme	complex	1433:1439	arg1	mixture					1441:1447	a very complex mixture	1426:1447	a very complex mixture	1426:1447	We believe this is the first study when such structures were characterized from a very complex mixture and were linked not only to a specific protein, but also the sites of modifications have been determined.
30407017	5	32	theme	core	845:848	arg1	glycans					852:858	core 1 glycans	845:858	core 1 glycans with disialic acids	845:878	B and Y fragment ions revealed that (i) in core 1 structures the Gal residue featured the O-acetyl-sialic acid, when there was only one in the glycan; (ii) several glycopeptides featured core 1 glycans with disialic acids, in certain instances O-acetylated; (iii) the disialic acid was linked to the GalNAc residue whatever the degree of O-acetylation; (iv) core 2 isomers with a single O-acetyl-sialic acid were chromatographically resolved.
30407017	2	33	gly	O-glycopeptides	436:450	arg2	O-glycopeptides					436:450	mucin-type O-glycopeptides	425:450	mucin-type O-glycopeptides	425:450	We focused on the characterization of mucin-type O-glycopeptides.
30407017	6	34	theme	sialyl	1226:1231	arg1	LewisX/A					1233:1240	sialyl LewisX/A	1226:1240	sialyl LewisX/A	1226:1240	Glycan fragmentation also helped to decipher additional core 2 oligosaccharides: a LacdiNAc-like structure, glycans carrying sialyl LewisX/A at different stages of O-acetylation, and blood antigens.
30407017	6	35	theme	additional	1146:1155	arg1	oligosaccharides					1164:1179	additional core 2 oligosaccharides	1146:1179	additional core 2 oligosaccharides	1146:1179	Glycan fragmentation also helped to decipher additional core 2 oligosaccharides: a LacdiNAc-like structure, glycans carrying sialyl LewisX/A at different stages of O-acetylation, and blood antigens.
30407017	8	36	theme	such	1386:1389	arg1	structures					1391:1400	such structures	1386:1400	such structures	1386:1400	We believe this is the first study when such structures were characterized from a very complex mixture and were linked not only to a specific protein, but also the sites of modifications have been determined.
30407017	7	37	theme	core	1308:1311	arg1	structure					1315:1323	A sialo core 3 structure	1300:1323	A sialo core 3 structure	1300:1323	A sialo core 3 structure was also identified.
30407017	0	38	theme	O-Glycan	20:27	arg1	Repertoire					29:38	Extended Sialylated O-Glycan Repertoire	0:38	Extended Sialylated O-Glycan Repertoire of Human Urinary Glycoproteins	0:69	Extended Sialylated O-Glycan Repertoire of Human Urinary Glycoproteins Discovered and Characterized Using Electron-Transfer/Higher-Energy Collision Dissociation.
30407017	0	38	theme	O-Glycan	20:27	arg1	Glycoproteins					57:69	Human Urinary Glycoproteins	43:69	Human Urinary Glycoproteins	43:69	Extended Sialylated O-Glycan Repertoire of Human Urinary Glycoproteins Discovered and Characterized Using Electron-Transfer/Higher-Energy Collision Dissociation.
30407017	5	39	theme	single	1038:1043	arg1	acid					1061:1064	a single O-acetyl-sialic acid	1036:1064	a single O-acetyl-sialic acid	1036:1064	B and Y fragment ions revealed that (i) in core 1 structures the Gal residue featured the O-acetyl-sialic acid, when there was only one in the glycan; (ii) several glycopeptides featured core 1 glycans with disialic acids, in certain instances O-acetylated; (iii) the disialic acid was linked to the GalNAc residue whatever the degree of O-acetylation; (iv) core 2 isomers with a single O-acetyl-sialic acid were chromatographically resolved.
30407017	5	40	dep	linked	944:949	arg1	iii					917:919	iii	917:919	iii	917:919	B and Y fragment ions revealed that (i) in core 1 structures the Gal residue featured the O-acetyl-sialic acid, when there was only one in the glycan; (ii) several glycopeptides featured core 1 glycans with disialic acids, in certain instances O-acetylated; (iii) the disialic acid was linked to the GalNAc residue whatever the degree of O-acetylation; (iv) core 2 isomers with a single O-acetyl-sialic acid were chromatographically resolved.
30407017	6	41	theme	Glycan	1101:1106	arg1	fragmentation					1108:1120	Glycan fragmentation	1101:1120	Glycan fragmentation	1101:1120	Glycan fragmentation also helped to decipher additional core 2 oligosaccharides: a LacdiNAc-like structure, glycans carrying sialyl LewisX/A at different stages of O-acetylation, and blood antigens.
30407017	0	42	theme	Human	43:47	arg1	Glycoproteins					57:69	Human Urinary Glycoproteins	43:69	Human Urinary Glycoproteins	43:69	Extended Sialylated O-Glycan Repertoire of Human Urinary Glycoproteins Discovered and Characterized Using Electron-Transfer/Higher-Energy Collision Dissociation.
30407017	1	43	theme	human	366:370	arg1	samples					378:384	human urine samples	366:384	human urine samples	366:384	A relatively novel activation technique, electron-transfer/higher-energy collision dissociation (EThcD) was used in the LC-MS/MS analysis of tryptic glycopeptides enriched with wheat germ agglutinin from human urine samples.
30407017	5	44	with	glycans	852:858	arg1	acids					874:878	disialic acids	865:878	disialic acids	865:878	B and Y fragment ions revealed that (i) in core 1 structures the Gal residue featured the O-acetyl-sialic acid, when there was only one in the glycan; (ii) several glycopeptides featured core 1 glycans with disialic acids, in certain instances O-acetylated; (iii) the disialic acid was linked to the GalNAc residue whatever the degree of O-acetylation; (iv) core 2 isomers with a single O-acetyl-sialic acid were chromatographically resolved.
30407017	5	45	theme	O-acetyl-sialic	1045:1059	arg1	acid					1061:1064	a single O-acetyl-sialic acid	1036:1064	a single O-acetyl-sialic acid	1036:1064	B and Y fragment ions revealed that (i) in core 1 structures the Gal residue featured the O-acetyl-sialic acid, when there was only one in the glycan; (ii) several glycopeptides featured core 1 glycans with disialic acids, in certain instances O-acetylated; (iii) the disialic acid was linked to the GalNAc residue whatever the degree of O-acetylation; (iv) core 2 isomers with a single O-acetyl-sialic acid were chromatographically resolved.
30407017	6	46	theme	different	1245:1253	arg1	stages					1255:1260	different stages	1245:1260	different stages of O-acetylation	1245:1277	Glycan fragmentation also helped to decipher additional core 2 oligosaccharides: a LacdiNAc-like structure, glycans carrying sialyl LewisX/A at different stages of O-acetylation, and blood antigens.
30407017	5	47	theme	disialic	865:872	arg1	acids					874:878	disialic acids	865:878	disialic acids	865:878	B and Y fragment ions revealed that (i) in core 1 structures the Gal residue featured the O-acetyl-sialic acid, when there was only one in the glycan; (ii) several glycopeptides featured core 1 glycans with disialic acids, in certain instances O-acetylated; (iii) the disialic acid was linked to the GalNAc residue whatever the degree of O-acetylation; (iv) core 2 isomers with a single O-acetyl-sialic acid were chromatographically resolved.
30407017	1	48	theme	urine	372:376	arg1	samples					378:384	human urine samples	366:384	human urine samples	366:384	A relatively novel activation technique, electron-transfer/higher-energy collision dissociation (EThcD) was used in the LC-MS/MS analysis of tryptic glycopeptides enriched with wheat germ agglutinin from human urine samples.
30407017	5	49	gly	glycopeptides	822:834	arg2	glycopeptides					822:834	several glycopeptides	814:834	several glycopeptides	814:834	B and Y fragment ions revealed that (i) in core 1 structures the Gal residue featured the O-acetyl-sialic acid, when there was only one in the glycan; (ii) several glycopeptides featured core 1 glycans with disialic acids, in certain instances O-acetylated; (iii) the disialic acid was linked to the GalNAc residue whatever the degree of O-acetylation; (iv) core 2 isomers with a single O-acetyl-sialic acid were chromatographically resolved.
30407017	6	50	contain	carrying	1217:1224	arg1	glycans					1209:1215	glycans	1209:1215	glycans carrying sialyl LewisX/A at different stages of O-acetylation	1209:1277	Glycan fragmentation also helped to decipher additional core 2 oligosaccharides: a LacdiNAc-like structure, glycans carrying sialyl LewisX/A at different stages of O-acetylation, and blood antigens.
30407017	6	50	contain	carrying	1217:1224	arg2	LewisX/A					1233:1240	sialyl LewisX/A	1226:1240	sialyl LewisX/A	1226:1240	Glycan fragmentation also helped to decipher additional core 2 oligosaccharides: a LacdiNAc-like structure, glycans carrying sialyl LewisX/A at different stages of O-acetylation, and blood antigens.
30407017	6	50	contain	carrying	1217:1224	arg1	structure					1198:1206	a LacdiNAc-like structure	1182:1206	a LacdiNAc-like structure	1182:1206	Glycan fragmentation also helped to decipher additional core 2 oligosaccharides: a LacdiNAc-like structure, glycans carrying sialyl LewisX/A at different stages of O-acetylation, and blood antigens.
30407017	0	51	theme	Glycoproteins	57:69	arg1	Repertoire					29:38	Extended Sialylated O-Glycan Repertoire	0:38	Extended Sialylated O-Glycan Repertoire of Human Urinary Glycoproteins	0:69	Extended Sialylated O-Glycan Repertoire of Human Urinary Glycoproteins Discovered and Characterized Using Electron-Transfer/Higher-Energy Collision Dissociation.
30407017	0	51	theme	Glycoproteins	57:69	arg1	Glycoproteins					57:69	Human Urinary Glycoproteins	43:69	Human Urinary Glycoproteins	43:69	Extended Sialylated O-Glycan Repertoire of Human Urinary Glycoproteins Discovered and Characterized Using Electron-Transfer/Higher-Energy Collision Dissociation.
30407017	5	52	attach	linked	944:949	arg2	acid					935:938	the disialic acid	922:938	the disialic acid	922:938	B and Y fragment ions revealed that (i) in core 1 structures the Gal residue featured the O-acetyl-sialic acid, when there was only one in the glycan; (ii) several glycopeptides featured core 1 glycans with disialic acids, in certain instances O-acetylated; (iii) the disialic acid was linked to the GalNAc residue whatever the degree of O-acetylation; (iv) core 2 isomers with a single O-acetyl-sialic acid were chromatographically resolved.
30407017	5	52	attach	linked	944:949	arg1	residue					965:971	the GalNAc residue	954:971	the GalNAc residue whatever the degree of O-acetylation; (iv) core 2 isomers with a single O-acetyl-sialic acid were chromatographically resolved	954:1098	B and Y fragment ions revealed that (i) in core 1 structures the Gal residue featured the O-acetyl-sialic acid, when there was only one in the glycan; (ii) several glycopeptides featured core 1 glycans with disialic acids, in certain instances O-acetylated; (iii) the disialic acid was linked to the GalNAc residue whatever the degree of O-acetylation; (iv) core 2 isomers with a single O-acetyl-sialic acid were chromatographically resolved.
30407017	5	53	theme	Gal	723:725	arg1	residue					727:733	the Gal residue	719:733	the Gal residue	719:733	B and Y fragment ions revealed that (i) in core 1 structures the Gal residue featured the O-acetyl-sialic acid, when there was only one in the glycan; (ii) several glycopeptides featured core 1 glycans with disialic acids, in certain instances O-acetylated; (iii) the disialic acid was linked to the GalNAc residue whatever the degree of O-acetylation; (iv) core 2 isomers with a single O-acetyl-sialic acid were chromatographically resolved.
30407017	1	54	used	used	270:273	arg2	dissociation					245:256	electron-transfer/higher-energy collision dissociation	203:256	electron-transfer/higher-energy collision dissociation (EThcD)	203:264	A relatively novel activation technique, electron-transfer/higher-energy collision dissociation (EThcD) was used in the LC-MS/MS analysis of tryptic glycopeptides enriched with wheat germ agglutinin from human urine samples.
30407017	1	54	used	used	270:273	arg2	technique					192:200	A relatively novel activation technique	162:200	A relatively novel activation technique	162:200	A relatively novel activation technique, electron-transfer/higher-energy collision dissociation (EThcD) was used in the LC-MS/MS analysis of tryptic glycopeptides enriched with wheat germ agglutinin from human urine samples.
30407017	0	55	theme	Urinary	49:55	arg1	Glycoproteins					57:69	Human Urinary Glycoproteins	43:69	Human Urinary Glycoproteins	43:69	Extended Sialylated O-Glycan Repertoire of Human Urinary Glycoproteins Discovered and Characterized Using Electron-Transfer/Higher-Energy Collision Dissociation.
30407017	5	56	theme	O-acetyl-sialic	748:762	arg1	acid					764:767	the O-acetyl-sialic acid	744:767	the O-acetyl-sialic acid	744:767	B and Y fragment ions revealed that (i) in core 1 structures the Gal residue featured the O-acetyl-sialic acid, when there was only one in the glycan; (ii) several glycopeptides featured core 1 glycans with disialic acids, in certain instances O-acetylated; (iii) the disialic acid was linked to the GalNAc residue whatever the degree of O-acetylation; (iv) core 2 isomers with a single O-acetyl-sialic acid were chromatographically resolved.
30407017	5	57	theme	core	1016:1019	arg1	isomers					1023:1029	(iv) core 2 isomers	1011:1029	(iv) core 2 isomers with a single O-acetyl-sialic acid	1011:1064	B and Y fragment ions revealed that (i) in core 1 structures the Gal residue featured the O-acetyl-sialic acid, when there was only one in the glycan; (ii) several glycopeptides featured core 1 glycans with disialic acids, in certain instances O-acetylated; (iii) the disialic acid was linked to the GalNAc residue whatever the degree of O-acetylation; (iv) core 2 isomers with a single O-acetyl-sialic acid were chromatographically resolved.
30407017	6	58	theme	blood	1284:1288	arg1	antigens					1290:1297	blood antigens	1284:1297	blood antigens	1284:1297	Glycan fragmentation also helped to decipher additional core 2 oligosaccharides: a LacdiNAc-like structure, glycans carrying sialyl LewisX/A at different stages of O-acetylation, and blood antigens.
30407017	4	59	theme	O-acetyl	614:621	arg1	presence					602:609	the presence	598:609	the presence of O-acetyl	598:621	Unexpectedly, glycan oxonium ions indicated the presence of O-acetyl, and even O-diacetyl-sialic acids.
30407017	1	60	theme	novel	175:179	arg1	dissociation					245:256	electron-transfer/higher-energy collision dissociation	203:256	electron-transfer/higher-energy collision dissociation (EThcD)	203:264	A relatively novel activation technique, electron-transfer/higher-energy collision dissociation (EThcD) was used in the LC-MS/MS analysis of tryptic glycopeptides enriched with wheat germ agglutinin from human urine samples.
30407017	1	60	theme	novel	175:179	arg1	technique					192:200	A relatively novel activation technique	162:200	A relatively novel activation technique	162:200	A relatively novel activation technique, electron-transfer/higher-energy collision dissociation (EThcD) was used in the LC-MS/MS analysis of tryptic glycopeptides enriched with wheat germ agglutinin from human urine samples.
30407017	1	61	theme	LC-MS/MS	282:289	arg1	analysis					291:298	the LC-MS/MS analysis	278:298	the LC-MS/MS analysis of tryptic glycopeptides enriched with wheat germ agglutinin from human urine samples	278:384	A relatively novel activation technique, electron-transfer/higher-energy collision dissociation (EThcD) was used in the LC-MS/MS analysis of tryptic glycopeptides enriched with wheat germ agglutinin from human urine samples.
30407017	6	62	theme	LacdiNAc-like	1184:1196	arg1	glycans					1209:1215	glycans	1209:1215	glycans carrying sialyl LewisX/A at different stages of O-acetylation	1209:1277	Glycan fragmentation also helped to decipher additional core 2 oligosaccharides: a LacdiNAc-like structure, glycans carrying sialyl LewisX/A at different stages of O-acetylation, and blood antigens.
30407017	6	62	theme	LacdiNAc-like	1184:1196	arg1	structure					1198:1206	a LacdiNAc-like structure	1182:1206	a LacdiNAc-like structure	1182:1206	Glycan fragmentation also helped to decipher additional core 2 oligosaccharides: a LacdiNAc-like structure, glycans carrying sialyl LewisX/A at different stages of O-acetylation, and blood antigens.
30407017	1	63	theme	activation	181:190	arg1	dissociation					245:256	electron-transfer/higher-energy collision dissociation	203:256	electron-transfer/higher-energy collision dissociation (EThcD)	203:264	A relatively novel activation technique, electron-transfer/higher-energy collision dissociation (EThcD) was used in the LC-MS/MS analysis of tryptic glycopeptides enriched with wheat germ agglutinin from human urine samples.
30407017	1	63	theme	activation	181:190	arg1	technique					192:200	A relatively novel activation technique	162:200	A relatively novel activation technique	162:200	A relatively novel activation technique, electron-transfer/higher-energy collision dissociation (EThcD) was used in the LC-MS/MS analysis of tryptic glycopeptides enriched with wheat germ agglutinin from human urine samples.
30407017	5	64	theme	disialic	926:933	arg1	acid					935:938	the disialic acid	922:938	the disialic acid	922:938	B and Y fragment ions revealed that (i) in core 1 structures the Gal residue featured the O-acetyl-sialic acid, when there was only one in the glycan; (ii) several glycopeptides featured core 1 glycans with disialic acids, in certain instances O-acetylated; (iii) the disialic acid was linked to the GalNAc residue whatever the degree of O-acetylation; (iv) core 2 isomers with a single O-acetyl-sialic acid were chromatographically resolved.
30407017	7	65	theme	sialo	1302:1306	arg1	structure					1315:1323	A sialo core 3 structure	1300:1323	A sialo core 3 structure	1300:1323	A sialo core 3 structure was also identified.
30407017	5	66	theme	O-acetylation	996:1008	arg1	degree					986:991	the degree	982:991	the degree of O-acetylation	982:1008	B and Y fragment ions revealed that (i) in core 1 structures the Gal residue featured the O-acetyl-sialic acid, when there was only one in the glycan; (ii) several glycopeptides featured core 1 glycans with disialic acids, in certain instances O-acetylated; (iii) the disialic acid was linked to the GalNAc residue whatever the degree of O-acetylation; (iv) core 2 isomers with a single O-acetyl-sialic acid were chromatographically resolved.
30407017	5	67	theme	O-acetylated	902:913	arg1	instances					892:900	certain instances	884:900	certain instances O-acetylated	884:913	B and Y fragment ions revealed that (i) in core 1 structures the Gal residue featured the O-acetyl-sialic acid, when there was only one in the glycan; (ii) several glycopeptides featured core 1 glycans with disialic acids, in certain instances O-acetylated; (iii) the disialic acid was linked to the GalNAc residue whatever the degree of O-acetylation; (iv) core 2 isomers with a single O-acetyl-sialic acid were chromatographically resolved.
30407017	5	68	dep	featured	735:742	arg1	i					695:695	i	695:695	i	695:695	B and Y fragment ions revealed that (i) in core 1 structures the Gal residue featured the O-acetyl-sialic acid, when there was only one in the glycan; (ii) several glycopeptides featured core 1 glycans with disialic acids, in certain instances O-acetylated; (iii) the disialic acid was linked to the GalNAc residue whatever the degree of O-acetylation; (iv) core 2 isomers with a single O-acetyl-sialic acid were chromatographically resolved.
30407017	8	69	theme	specific	1479:1486	arg1	protein					1488:1494	a specific protein	1477:1494	a specific protein	1477:1494	We believe this is the first study when such structures were characterized from a very complex mixture and were linked not only to a specific protein, but also the sites of modifications have been determined.
30407017	6	70	dep	helped	1127:1132	arg1	glycans					1209:1215	glycans	1209:1215	glycans carrying sialyl LewisX/A at different stages of O-acetylation	1209:1277	Glycan fragmentation also helped to decipher additional core 2 oligosaccharides: a LacdiNAc-like structure, glycans carrying sialyl LewisX/A at different stages of O-acetylation, and blood antigens.
30407017	6	70	dep	helped	1127:1132	arg1	structure					1198:1206	a LacdiNAc-like structure	1182:1206	a LacdiNAc-like structure	1182:1206	Glycan fragmentation also helped to decipher additional core 2 oligosaccharides: a LacdiNAc-like structure, glycans carrying sialyl LewisX/A at different stages of O-acetylation, and blood antigens.
30407017	6	70	dep	helped	1127:1132	arg1	antigens					1290:1297	blood antigens	1284:1297	blood antigens	1284:1297	Glycan fragmentation also helped to decipher additional core 2 oligosaccharides: a LacdiNAc-like structure, glycans carrying sialyl LewisX/A at different stages of O-acetylation, and blood antigens.
30407017	2	71	theme	O-glycopeptides	436:450	arg1	characterization					405:420	the characterization	401:420	the characterization of mucin-type O-glycopeptides	401:450	We focused on the characterization of mucin-type O-glycopeptides.
30407017	8	72	attach	linked	1458:1463	arg1	protein					1488:1494	a specific protein	1477:1494	a specific protein	1477:1494	We believe this is the first study when such structures were characterized from a very complex mixture and were linked not only to a specific protein, but also the sites of modifications have been determined.
30407017	8	72	attach	linked	1458:1463	arg2	structures					1391:1400	such structures	1386:1400	such structures	1386:1400	We believe this is the first study when such structures were characterized from a very complex mixture and were linked not only to a specific protein, but also the sites of modifications have been determined.
30407017	1	73	theme	tryptic	303:309	arg1	glycopeptides					311:323	tryptic glycopeptides	303:323	tryptic glycopeptides enriched with wheat germ agglutinin from human urine samples	303:384	A relatively novel activation technique, electron-transfer/higher-energy collision dissociation (EThcD) was used in the LC-MS/MS analysis of tryptic glycopeptides enriched with wheat germ agglutinin from human urine samples.
10766826	4	0	theme	structure	782:790	arg1	Determination					747:759	Determination	747:759	Determination of the x-ray crystal structure of a myeloperoxidase-bromide complex (r = 0.243, free r = 0.296)	747:855	Determination of the x-ray crystal structure of a myeloperoxidase-bromide complex (r = 0.243, free r = 0.296) has shown that this chloride ion can be replaced by bromide.
10766826	2	1	theme	heme	482:485	arg1	rings					461:465	pyrrole rings A and C	453:473	pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A	453:613	Results confirm that the heme is covalently attached to the protein via two ester linkages between the carboxyl groups of Glu(242) and Asp(94) and modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A.
10766826	2	1	theme	heme	482:485	arg1	C					473:473	C	473:473	C	473:473	Results confirm that the heme is covalently attached to the protein via two ester linkages between the carboxyl groups of Glu(242) and Asp(94) and modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A.
10766826	2	1	theme	heme	482:485	arg1	A					467:467	A	467:467	A	467:467	Results confirm that the heme is covalently attached to the protein via two ester linkages between the carboxyl groups of Glu(242) and Asp(94) and modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A.
10766826	3	2	contain	containing	713:722	arg2	336					741:743	336	741:743	336	741:743	In the native enzyme a bound chloride ion has been identified at the amino terminus of the helix containing the proximal His(336).
10766826	3	2	contain	containing	713:722	arg2	His					737:739	the proximal His	724:739	the proximal His(336)	724:744	In the native enzyme a bound chloride ion has been identified at the amino terminus of the helix containing the proximal His(336).
10766826	3	2	contain	containing	713:722	arg1	helix					707:711	the helix	703:711	the helix containing the proximal His(336)	703:744	In the native enzyme a bound chloride ion has been identified at the amino terminus of the helix containing the proximal His(336).
10766826	1	3	theme	myeloperoxidase	152:166	arg1	structure					133:141	The x-ray crystal structure	115:141	The x-ray crystal structure of human myeloperoxidase	115:166	The x-ray crystal structure of human myeloperoxidase has been extended to 1.8 A resolution, using x-ray data recorded at -180 degrees C (r = 0.197, free r = 0.239).
10766826	3	4	theme	native	623:628	arg1	enzyme					630:635	the native enzyme	619:635	the native enzyme	619:635	In the native enzyme a bound chloride ion has been identified at the amino terminus of the helix containing the proximal His(336).
10766826	3	5	theme	chloride	645:652	arg1	ion					654:656	a bound chloride ion	637:656	a bound chloride ion	637:656	In the native enzyme a bound chloride ion has been identified at the amino terminus of the helix containing the proximal His(336).
10766826	0	6	theme	myeloperoxidase	78:92	arg1	myeloperoxidase					78:92	human myeloperoxidase	72:92	human myeloperoxidase	72:92	X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 A resolution.
10766826	0	6	theme	myeloperoxidase	78:92	arg1	sites					63:67	halide-binding sites	48:67	halide-binding sites of human myeloperoxidase	48:92	X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 A resolution.
10766826	4	7	dep	=	848:848	arg1	r					830:830	r	830:830	r = 0.243	830:838	Determination of the x-ray crystal structure of a myeloperoxidase-bromide complex (r = 0.243, free r = 0.296) has shown that this chloride ion can be replaced by bromide.
10766826	6	8	theme	distal	1136:1141	arg1	cavity					1143:1148	the distal cavity	1132:1148	the distal cavity	1132:1148	The bromide-binding site in the distal cavity appears to be the halide-binding site responsible for shifts in the Soret band of the absorption spectrum of myeloperoxidase.
10766826	1	9	theme	degrees	241:247	arg1	C					249:249	-180 degrees C	236:249	-180 degrees C	236:249	The x-ray crystal structure of human myeloperoxidase has been extended to 1.8 A resolution, using x-ray data recorded at -180 degrees C (r = 0.197, free r = 0.239).
10766826	0	10	theme	A	101:101	arg1	resolution					103:112	1.8 A resolution	97:112	1.8 A resolution	97:112	X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 A resolution.
10766826	1	11	dep	=	254:254	arg1	0.197					256:260	0.197	256:260	0.197	256:260	The x-ray crystal structure of human myeloperoxidase has been extended to 1.8 A resolution, using x-ray data recorded at -180 degrees C (r = 0.197, free r = 0.239).
10766826	6	12	theme	halide-binding	1168:1181	arg1	site					1183:1186	the halide-binding site	1164:1186	the halide-binding site responsible for shifts in the Soret band of the absorption spectrum of myeloperoxidase	1164:1273	The bromide-binding site in the distal cavity appears to be the halide-binding site responsible for shifts in the Soret band of the absorption spectrum of myeloperoxidase.
10766826	6	12	theme	halide-binding	1168:1181	arg1	site					1124:1127	The bromide-binding site	1104:1127	The bromide-binding site in the distal cavity	1104:1148	The bromide-binding site in the distal cavity appears to be the halide-binding site responsible for shifts in the Soret band of the absorption spectrum of myeloperoxidase.
10766826	3	13	theme	amino	685:689	arg1	terminus					691:698	the amino terminus	681:698	the amino terminus of the helix containing the proximal His(336)	681:744	In the native enzyme a bound chloride ion has been identified at the amino terminus of the helix containing the proximal His(336).
10766826	5	14	theme	partial	951:957	arg1	occupancy					959:967	partial occupancy	951:967	partial occupancy	951:967	Bromide is also seen to bind, at partial occupancy, in the distal heme cavity, in close proximity to the distal His(95), where it replaces the water molecule hydrogen bonded to Gln(91).
10766826	1	15	dep	=	270:270	arg1	r					252:252	r	252:252	r = 0.197	252:260	The x-ray crystal structure of human myeloperoxidase has been extended to 1.8 A resolution, using x-ray data recorded at -180 degrees C (r = 0.197, free r = 0.239).
10766826	5	16	theme	distal	977:982	arg1	cavity					989:994	the distal heme cavity	973:994	the distal heme cavity	973:994	Bromide is also seen to bind, at partial occupancy, in the distal heme cavity, in close proximity to the distal His(95), where it replaces the water molecule hydrogen bonded to Gln(91).
10766826	2	17	theme	ion	510:512	arg1	linkage					514:520	a sulfonium ion linkage	498:520	a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A	498:613	Results confirm that the heme is covalently attached to the protein via two ester linkages between the carboxyl groups of Glu(242) and Asp(94) and modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A.
10766826	3	18	theme	proximal	728:735	arg1	His					737:739	the proximal His	724:739	the proximal His(336)	724:744	In the native enzyme a bound chloride ion has been identified at the amino terminus of the helix containing the proximal His(336).
10766826	3	18	theme	proximal	728:735	arg1	336					741:743	336	741:743	336	741:743	In the native enzyme a bound chloride ion has been identified at the amino terminus of the helix containing the proximal His(336).
10766826	3	19	theme	bound	639:643	arg1	ion					654:656	a bound chloride ion	637:656	a bound chloride ion	637:656	In the native enzyme a bound chloride ion has been identified at the amino terminus of the helix containing the proximal His(336).
10766826	2	20	from	groups	392:397	arg1	rings					461:465	pyrrole rings A and C	453:473	pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A	453:613	Results confirm that the heme is covalently attached to the protein via two ester linkages between the carboxyl groups of Glu(242) and Asp(94) and modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A.
10766826	2	20	from	groups	392:397	arg1	C					473:473	C	473:473	C	473:473	Results confirm that the heme is covalently attached to the protein via two ester linkages between the carboxyl groups of Glu(242) and Asp(94) and modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A.
10766826	2	20	from	groups	392:397	arg1	A					467:467	A	467:467	A	467:467	Results confirm that the heme is covalently attached to the protein via two ester linkages between the carboxyl groups of Glu(242) and Asp(94) and modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A.
10766826	2	21	theme	sulfonium	500:508	arg1	linkage					514:520	a sulfonium ion linkage	498:520	a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A	498:613	Results confirm that the heme is covalently attached to the protein via two ester linkages between the carboxyl groups of Glu(242) and Asp(94) and modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A.
10766826	2	22	theme	group	591:595	arg1	Met					549:551	Met(243)	549:556	Met(243)	549:556	Results confirm that the heme is covalently attached to the protein via two ester linkages between the carboxyl groups of Glu(242) and Asp(94) and modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A.
10766826	2	22	theme	group	591:595	arg1	beta-carbon					566:576	the beta-carbon	562:576	the beta-carbon of the vinyl group on pyrrole ring A	562:613	Results confirm that the heme is covalently attached to the protein via two ester linkages between the carboxyl groups of Glu(242) and Asp(94) and modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A.
10766826	7	23	from	site	1492:1495	arg1	compound					1430:1437	compound I	1430:1439	compound I	1430:1439	It is proposed that halide binding to this site inhibits the enzyme by effectively competing with H(2)O(2) for access to the distal histidine, whereas in compound I, the same site may be the halide substrate-binding site.
10766826	4	24	theme	myeloperoxidase-bromide	797:819	arg1	complex					821:827	a myeloperoxidase-bromide complex	795:827	a myeloperoxidase-bromide complex (r = 0.243, free r = 0.296)	795:855	Determination of the x-ray crystal structure of a myeloperoxidase-bromide complex (r = 0.243, free r = 0.296) has shown that this chloride ion can be replaced by bromide.
10766826	7	25	theme	halide	1467:1472	arg1	site					1451:1454	the same site	1442:1454	the same site	1442:1454	It is proposed that halide binding to this site inhibits the enzyme by effectively competing with H(2)O(2) for access to the distal histidine, whereas in compound I, the same site may be the halide substrate-binding site.
10766826	7	25	theme	halide	1467:1472	arg1	site					1492:1495	the halide substrate-binding site	1463:1495	the halide substrate-binding site	1463:1495	It is proposed that halide binding to this site inhibits the enzyme by effectively competing with H(2)O(2) for access to the distal histidine, whereas in compound I, the same site may be the halide substrate-binding site.
10766826	2	26	theme	carboxyl	383:390	arg1	Asp					415:417	Asp(94)	415:421	Asp(94)	415:421	Results confirm that the heme is covalently attached to the protein via two ester linkages between the carboxyl groups of Glu(242) and Asp(94) and modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A.
10766826	2	26	theme	carboxyl	383:390	arg1	Glu					402:404	Glu(242)	402:409	Glu(242)	402:409	Results confirm that the heme is covalently attached to the protein via two ester linkages between the carboxyl groups of Glu(242) and Asp(94) and modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A.
10766826	2	26	theme	carboxyl	383:390	arg1	groups					392:397	the carboxyl groups	379:397	the carboxyl groups of Glu(242) and Asp(94)	379:421	Results confirm that the heme is covalently attached to the protein via two ester linkages between the carboxyl groups of Glu(242) and Asp(94) and modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A.
10766826	2	27	theme	vinyl	585:589	arg1	group					591:595	the vinyl group	581:595	the vinyl group on pyrrole ring A	581:613	Results confirm that the heme is covalently attached to the protein via two ester linkages between the carboxyl groups of Glu(242) and Asp(94) and modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A.
10766826	2	28	from	Met	549:551	arg1	A					613:613	pyrrole ring A	600:613	pyrrole ring A	600:613	Results confirm that the heme is covalently attached to the protein via two ester linkages between the carboxyl groups of Glu(242) and Asp(94) and modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A.
10766826	0	29	theme	crystal	6:12	arg1	structure					14:22	X-ray crystal structure	0:22	X-ray crystal structure	0:22	X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 A resolution.
10766826	4	30	theme	crystal	774:780	arg1	structure					782:790	the x-ray crystal structure	764:790	the x-ray crystal structure of a myeloperoxidase-bromide complex (r = 0.243, free r = 0.296)	764:855	Determination of the x-ray crystal structure of a myeloperoxidase-bromide complex (r = 0.243, free r = 0.296) has shown that this chloride ion can be replaced by bromide.
10766826	2	31	theme	Asp	415:417	arg1	groups					443:448	modified methyl groups	427:448	modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A	427:613	Results confirm that the heme is covalently attached to the protein via two ester linkages between the carboxyl groups of Glu(242) and Asp(94) and modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A.
10766826	2	31	theme	Asp	415:417	arg1	Asp					415:417	Asp(94)	415:421	Asp(94)	415:421	Results confirm that the heme is covalently attached to the protein via two ester linkages between the carboxyl groups of Glu(242) and Asp(94) and modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A.
10766826	2	31	theme	Asp	415:417	arg1	Glu					402:404	Glu(242)	402:409	Glu(242)	402:409	Results confirm that the heme is covalently attached to the protein via two ester linkages between the carboxyl groups of Glu(242) and Asp(94) and modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A.
10766826	2	31	theme	Asp	415:417	arg1	groups					392:397	the carboxyl groups	379:397	the carboxyl groups of Glu(242) and Asp(94)	379:421	Results confirm that the heme is covalently attached to the protein via two ester linkages between the carboxyl groups of Glu(242) and Asp(94) and modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A.
10766826	3	32	theme	helix	707:711	arg1	terminus					691:698	the amino terminus	681:698	the amino terminus of the helix containing the proximal His(336)	681:744	In the native enzyme a bound chloride ion has been identified at the amino terminus of the helix containing the proximal His(336).
10766826	0	33	theme	X-ray	0:4	arg1	structure					14:22	X-ray crystal structure	0:22	X-ray crystal structure	0:22	X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 A resolution.
10766826	2	34	theme	sulfur	534:539	arg1	atom					541:544	the sulfur atom	530:544	the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A	530:613	Results confirm that the heme is covalently attached to the protein via two ester linkages between the carboxyl groups of Glu(242) and Asp(94) and modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A.
10766826	5	35	theme	distal	1023:1028	arg1	His					1030:1032	the distal His(95)	1019:1036	the distal His(95)	1019:1036	Bromide is also seen to bind, at partial occupancy, in the distal heme cavity, in close proximity to the distal His(95), where it replaces the water molecule hydrogen bonded to Gln(91).
10766826	6	36	theme	absorption	1236:1245	arg1	spectrum					1247:1254	the absorption spectrum	1232:1254	the absorption spectrum of myeloperoxidase	1232:1273	The bromide-binding site in the distal cavity appears to be the halide-binding site responsible for shifts in the Soret band of the absorption spectrum of myeloperoxidase.
10766826	6	37	theme	bromide-binding	1108:1122	arg1	site					1183:1186	the halide-binding site	1164:1186	the halide-binding site responsible for shifts in the Soret band of the absorption spectrum of myeloperoxidase	1164:1273	The bromide-binding site in the distal cavity appears to be the halide-binding site responsible for shifts in the Soret band of the absorption spectrum of myeloperoxidase.
10766826	6	37	theme	bromide-binding	1108:1122	arg1	site					1124:1127	The bromide-binding site	1104:1127	The bromide-binding site in the distal cavity	1104:1148	The bromide-binding site in the distal cavity appears to be the halide-binding site responsible for shifts in the Soret band of the absorption spectrum of myeloperoxidase.
10766826	1	38	theme	=	254:254	arg1	r					252:252	r	252:252	r = 0.197	252:260	The x-ray crystal structure of human myeloperoxidase has been extended to 1.8 A resolution, using x-ray data recorded at -180 degrees C (r = 0.197, free r = 0.239).
10766826	6	39	from	shifts	1204:1209	arg1	band					1224:1227	the Soret band	1214:1227	the Soret band of the absorption spectrum of myeloperoxidase	1214:1273	The bromide-binding site in the distal cavity appears to be the halide-binding site responsible for shifts in the Soret band of the absorption spectrum of myeloperoxidase.
10766826	2	40	theme	ester	356:360	arg1	linkages					362:369	two ester linkages	352:369	two ester linkages between the carboxyl groups of Glu(242) and Asp(94) and modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A	352:613	Results confirm that the heme is covalently attached to the protein via two ester linkages between the carboxyl groups of Glu(242) and Asp(94) and modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A.
10766826	2	41	theme	beta-carbon	566:576	arg1	atom					541:544	the sulfur atom	530:544	the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A	530:613	Results confirm that the heme is covalently attached to the protein via two ester linkages between the carboxyl groups of Glu(242) and Asp(94) and modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A.
10766826	7	42	theme	same	1446:1449	arg1	site					1451:1454	the same site	1442:1454	the same site	1442:1454	It is proposed that halide binding to this site inhibits the enzyme by effectively competing with H(2)O(2) for access to the distal histidine, whereas in compound I, the same site may be the halide substrate-binding site.
10766826	7	42	theme	same	1446:1449	arg1	site					1492:1495	the halide substrate-binding site	1463:1495	the halide substrate-binding site	1463:1495	It is proposed that halide binding to this site inhibits the enzyme by effectively competing with H(2)O(2) for access to the distal histidine, whereas in compound I, the same site may be the halide substrate-binding site.
10766826	4	43	theme	chloride	877:884	arg1	ion					886:888	this chloride ion	872:888	this chloride ion	872:888	Determination of the x-ray crystal structure of a myeloperoxidase-bromide complex (r = 0.243, free r = 0.296) has shown that this chloride ion can be replaced by bromide.
10766826	2	44	theme	ring	608:611	arg1	A					613:613	pyrrole ring A	600:613	pyrrole ring A	600:613	Results confirm that the heme is covalently attached to the protein via two ester linkages between the carboxyl groups of Glu(242) and Asp(94) and modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A.
10766826	4	45	theme	x-ray	768:772	arg1	structure					782:790	the x-ray crystal structure	764:790	the x-ray crystal structure of a myeloperoxidase-bromide complex (r = 0.243, free r = 0.296)	764:855	Determination of the x-ray crystal structure of a myeloperoxidase-bromide complex (r = 0.243, free r = 0.296) has shown that this chloride ion can be replaced by bromide.
10766826	6	46	theme	Soret	1218:1222	arg1	band					1224:1227	the Soret band	1214:1227	the Soret band of the absorption spectrum of myeloperoxidase	1214:1273	The bromide-binding site in the distal cavity appears to be the halide-binding site responsible for shifts in the Soret band of the absorption spectrum of myeloperoxidase.
10766826	2	47	theme	methyl	436:441	arg1	groups					443:448	modified methyl groups	427:448	modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A	427:613	Results confirm that the heme is covalently attached to the protein via two ester linkages between the carboxyl groups of Glu(242) and Asp(94) and modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A.
10766826	2	47	theme	methyl	436:441	arg1	Asp					415:417	Asp(94)	415:421	Asp(94)	415:421	Results confirm that the heme is covalently attached to the protein via two ester linkages between the carboxyl groups of Glu(242) and Asp(94) and modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A.
10766826	2	47	theme	methyl	436:441	arg1	Glu					402:404	Glu(242)	402:409	Glu(242)	402:409	Results confirm that the heme is covalently attached to the protein via two ester linkages between the carboxyl groups of Glu(242) and Asp(94) and modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A.
10766826	6	48	theme	responsible	1188:1198	arg1	site					1183:1186	the halide-binding site	1164:1186	the halide-binding site responsible for shifts in the Soret band of the absorption spectrum of myeloperoxidase	1164:1273	The bromide-binding site in the distal cavity appears to be the halide-binding site responsible for shifts in the Soret band of the absorption spectrum of myeloperoxidase.
10766826	6	48	theme	responsible	1188:1198	arg1	site					1124:1127	The bromide-binding site	1104:1127	The bromide-binding site in the distal cavity	1104:1148	The bromide-binding site in the distal cavity appears to be the halide-binding site responsible for shifts in the Soret band of the absorption spectrum of myeloperoxidase.
10766826	2	49	theme	pyrrole	600:606	arg1	A					613:613	pyrrole ring A	600:613	pyrrole ring A	600:613	Results confirm that the heme is covalently attached to the protein via two ester linkages between the carboxyl groups of Glu(242) and Asp(94) and modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A.
10766826	2	50	theme	Glu	402:404	arg1	groups					443:448	modified methyl groups	427:448	modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A	427:613	Results confirm that the heme is covalently attached to the protein via two ester linkages between the carboxyl groups of Glu(242) and Asp(94) and modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A.
10766826	2	50	theme	Glu	402:404	arg1	Asp					415:417	Asp(94)	415:421	Asp(94)	415:421	Results confirm that the heme is covalently attached to the protein via two ester linkages between the carboxyl groups of Glu(242) and Asp(94) and modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A.
10766826	2	50	theme	Glu	402:404	arg1	Glu					402:404	Glu(242)	402:409	Glu(242)	402:409	Results confirm that the heme is covalently attached to the protein via two ester linkages between the carboxyl groups of Glu(242) and Asp(94) and modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A.
10766826	2	50	theme	Glu	402:404	arg1	groups					392:397	the carboxyl groups	379:397	the carboxyl groups of Glu(242) and Asp(94)	379:421	Results confirm that the heme is covalently attached to the protein via two ester linkages between the carboxyl groups of Glu(242) and Asp(94) and modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A.
10766826	1	51	theme	free	263:266	arg1	r					268:268	free r	263:268	free r	263:268	The x-ray crystal structure of human myeloperoxidase has been extended to 1.8 A resolution, using x-ray data recorded at -180 degrees C (r = 0.197, free r = 0.239).
10766826	2	52	theme	modified	427:434	arg1	groups					443:448	modified methyl groups	427:448	modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A	427:613	Results confirm that the heme is covalently attached to the protein via two ester linkages between the carboxyl groups of Glu(242) and Asp(94) and modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A.
10766826	2	52	theme	modified	427:434	arg1	Asp					415:417	Asp(94)	415:421	Asp(94)	415:421	Results confirm that the heme is covalently attached to the protein via two ester linkages between the carboxyl groups of Glu(242) and Asp(94) and modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A.
10766826	2	52	theme	modified	427:434	arg1	Glu					402:404	Glu(242)	402:409	Glu(242)	402:409	Results confirm that the heme is covalently attached to the protein via two ester linkages between the carboxyl groups of Glu(242) and Asp(94) and modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A.
10766826	7	53	theme	H	1374:1374	arg1	O					1378:1378	H(2)O(2)	1374:1381	H(2)O(2)	1374:1381	It is proposed that halide binding to this site inhibits the enzyme by effectively competing with H(2)O(2) for access to the distal histidine, whereas in compound I, the same site may be the halide substrate-binding site.
10766826	2	54	from	beta-carbon	566:576	arg1	A					613:613	pyrrole ring A	600:613	pyrrole ring A	600:613	Results confirm that the heme is covalently attached to the protein via two ester linkages between the carboxyl groups of Glu(242) and Asp(94) and modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A.
10766826	0	55	theme	sites	63:67	arg1	structure					14:22	X-ray crystal structure	0:22	X-ray crystal structure	0:22	X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 A resolution.
10766826	0	55	theme	sites	63:67	arg1	characterization					28:43	characterization	28:43	characterization	28:43	X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 A resolution.
10766826	7	56	theme	halide	1296:1301	arg1	binding					1303:1309	halide binding	1296:1309	halide binding to this site	1296:1322	It is proposed that halide binding to this site inhibits the enzyme by effectively competing with H(2)O(2) for access to the distal histidine, whereas in compound I, the same site may be the halide substrate-binding site.
10766826	7	57	theme	substrate-binding	1474:1490	arg1	site					1451:1454	the same site	1442:1454	the same site	1442:1454	It is proposed that halide binding to this site inhibits the enzyme by effectively competing with H(2)O(2) for access to the distal histidine, whereas in compound I, the same site may be the halide substrate-binding site.
10766826	7	57	theme	substrate-binding	1474:1490	arg1	site					1492:1495	the halide substrate-binding site	1463:1495	the halide substrate-binding site	1463:1495	It is proposed that halide binding to this site inhibits the enzyme by effectively competing with H(2)O(2) for access to the distal histidine, whereas in compound I, the same site may be the halide substrate-binding site.
10766826	6	58	from	site	1124:1127	arg1	cavity					1143:1148	the distal cavity	1132:1148	the distal cavity	1132:1148	The bromide-binding site in the distal cavity appears to be the halide-binding site responsible for shifts in the Soret band of the absorption spectrum of myeloperoxidase.
10766826	4	59	dep	complex	821:827	arg1	=					848:848	=	848:848	=	848:848	Determination of the x-ray crystal structure of a myeloperoxidase-bromide complex (r = 0.243, free r = 0.296) has shown that this chloride ion can be replaced by bromide.
10766826	5	60	theme	bonded	1085:1090	arg1	hydrogen					1076:1083	the water molecule hydrogen	1057:1083	the water molecule hydrogen bonded to Gln(91)	1057:1101	Bromide is also seen to bind, at partial occupancy, in the distal heme cavity, in close proximity to the distal His(95), where it replaces the water molecule hydrogen bonded to Gln(91).
10766826	5	61	theme	heme	984:987	arg1	cavity					989:994	the distal heme cavity	973:994	the distal heme cavity	973:994	Bromide is also seen to bind, at partial occupancy, in the distal heme cavity, in close proximity to the distal His(95), where it replaces the water molecule hydrogen bonded to Gln(91).
10766826	0	62	theme	halide-binding	48:61	arg1	myeloperoxidase					78:92	human myeloperoxidase	72:92	human myeloperoxidase	72:92	X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 A resolution.
10766826	0	62	theme	halide-binding	48:61	arg1	sites					63:67	halide-binding sites	48:67	halide-binding sites of human myeloperoxidase	48:92	X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 A resolution.
10766826	7	63	theme	distal	1401:1406	arg1	histidine					1408:1416	the distal histidine	1397:1416	the distal histidine	1397:1416	It is proposed that halide binding to this site inhibits the enzyme by effectively competing with H(2)O(2) for access to the distal histidine, whereas in compound I, the same site may be the halide substrate-binding site.
10766826	2	64	from	group	591:595	arg1	A					613:613	pyrrole ring A	600:613	pyrrole ring A	600:613	Results confirm that the heme is covalently attached to the protein via two ester linkages between the carboxyl groups of Glu(242) and Asp(94) and modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A.
10766826	6	65	theme	myeloperoxidase	1259:1273	arg1	spectrum					1247:1254	the absorption spectrum	1232:1254	the absorption spectrum of myeloperoxidase	1232:1273	The bromide-binding site in the distal cavity appears to be the halide-binding site responsible for shifts in the Soret band of the absorption spectrum of myeloperoxidase.
10766826	1	66	theme	x-ray	119:123	arg1	structure					133:141	The x-ray crystal structure	115:141	The x-ray crystal structure of human myeloperoxidase	115:166	The x-ray crystal structure of human myeloperoxidase has been extended to 1.8 A resolution, using x-ray data recorded at -180 degrees C (r = 0.197, free r = 0.239).
10766826	5	67	theme	close	1000:1004	arg1	proximity					1006:1014	close proximity	1000:1014	close proximity to the distal His(95), where it replaces the water molecule hydrogen bonded to Gln(91)	1000:1101	Bromide is also seen to bind, at partial occupancy, in the distal heme cavity, in close proximity to the distal His(95), where it replaces the water molecule hydrogen bonded to Gln(91).
10766826	0	68	from	resolution	103:112	arg1	structure					14:22	X-ray crystal structure	0:22	X-ray crystal structure	0:22	X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 A resolution.
10766826	0	68	from	resolution	103:112	arg1	characterization					28:43	characterization	28:43	characterization	28:43	X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 A resolution.
10766826	2	69	theme	Met	549:551	arg1	atom					541:544	the sulfur atom	530:544	the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A	530:613	Results confirm that the heme is covalently attached to the protein via two ester linkages between the carboxyl groups of Glu(242) and Asp(94) and modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A.
10766826	1	70	theme	crystal	125:131	arg1	structure					133:141	The x-ray crystal structure	115:141	The x-ray crystal structure of human myeloperoxidase	115:166	The x-ray crystal structure of human myeloperoxidase has been extended to 1.8 A resolution, using x-ray data recorded at -180 degrees C (r = 0.197, free r = 0.239).
10766826	1	71	theme	x-ray	213:217	arg1	data					219:222	x-ray data	213:222	x-ray data recorded at -180 degrees C (r = 0.197, free r = 0.239)	213:277	The x-ray crystal structure of human myeloperoxidase has been extended to 1.8 A resolution, using x-ray data recorded at -180 degrees C (r = 0.197, free r = 0.239).
10766826	2	72	theme	pyrrole	453:459	arg1	rings					461:465	pyrrole rings A and C	453:473	pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A	453:613	Results confirm that the heme is covalently attached to the protein via two ester linkages between the carboxyl groups of Glu(242) and Asp(94) and modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A.
10766826	2	72	theme	pyrrole	453:459	arg1	C					473:473	C	473:473	C	473:473	Results confirm that the heme is covalently attached to the protein via two ester linkages between the carboxyl groups of Glu(242) and Asp(94) and modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A.
10766826	2	72	theme	pyrrole	453:459	arg1	A					467:467	A	467:467	A	467:467	Results confirm that the heme is covalently attached to the protein via two ester linkages between the carboxyl groups of Glu(242) and Asp(94) and modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A.
10766826	5	73	theme	molecule	1067:1074	arg1	hydrogen					1076:1083	the water molecule hydrogen	1057:1083	the water molecule hydrogen bonded to Gln(91)	1057:1101	Bromide is also seen to bind, at partial occupancy, in the distal heme cavity, in close proximity to the distal His(95), where it replaces the water molecule hydrogen bonded to Gln(91).
10766826	6	74	theme	spectrum	1247:1254	arg1	band					1224:1227	the Soret band	1214:1227	the Soret band of the absorption spectrum of myeloperoxidase	1214:1273	The bromide-binding site in the distal cavity appears to be the halide-binding site responsible for shifts in the Soret band of the absorption spectrum of myeloperoxidase.
10766826	2	75	dep	rings	461:465	arg1	rings					461:465	pyrrole rings A and C	453:473	pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A	453:613	Results confirm that the heme is covalently attached to the protein via two ester linkages between the carboxyl groups of Glu(242) and Asp(94) and modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A.
10766826	2	75	dep	rings	461:465	arg1	C					473:473	C	473:473	C	473:473	Results confirm that the heme is covalently attached to the protein via two ester linkages between the carboxyl groups of Glu(242) and Asp(94) and modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A.
10766826	2	75	dep	rings	461:465	arg1	A					467:467	A	467:467	A	467:467	Results confirm that the heme is covalently attached to the protein via two ester linkages between the carboxyl groups of Glu(242) and Asp(94) and modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A.
10766826	0	76	theme	human	72:76	arg1	myeloperoxidase					78:92	human myeloperoxidase	72:92	human myeloperoxidase	72:92	X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 A resolution.
10766826	2	77	attach	attached	324:331	arg2	heme					305:308	the heme	301:308	the heme	301:308	Results confirm that the heme is covalently attached to the protein via two ester linkages between the carboxyl groups of Glu(242) and Asp(94) and modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A.
10766826	2	77	attach	attached	324:331	arg1	protein					340:346	the protein	336:346	the protein	336:346	Results confirm that the heme is covalently attached to the protein via two ester linkages between the carboxyl groups of Glu(242) and Asp(94) and modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A.
10766826	1	78	theme	A	193:193	arg1	resolution					195:204	1.8 A resolution	189:204	1.8 A resolution	189:204	The x-ray crystal structure of human myeloperoxidase has been extended to 1.8 A resolution, using x-ray data recorded at -180 degrees C (r = 0.197, free r = 0.239).
10766826	4	79	theme	complex	821:827	arg1	structure					782:790	the x-ray crystal structure	764:790	the x-ray crystal structure of a myeloperoxidase-bromide complex (r = 0.243, free r = 0.296)	764:855	Determination of the x-ray crystal structure of a myeloperoxidase-bromide complex (r = 0.243, free r = 0.296) has shown that this chloride ion can be replaced by bromide.
10766826	2	80	from	A	613:613	arg1	Met					549:551	Met(243)	549:556	Met(243)	549:556	Results confirm that the heme is covalently attached to the protein via two ester linkages between the carboxyl groups of Glu(242) and Asp(94) and modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A.
10766826	2	80	from	A	613:613	arg1	beta-carbon					566:576	the beta-carbon	562:576	the beta-carbon of the vinyl group on pyrrole ring A	562:613	Results confirm that the heme is covalently attached to the protein via two ester linkages between the carboxyl groups of Glu(242) and Asp(94) and modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A.
10766826	5	81	theme	water	1061:1065	arg1	hydrogen					1076:1083	the water molecule hydrogen	1057:1083	the water molecule hydrogen bonded to Gln(91)	1057:1101	Bromide is also seen to bind, at partial occupancy, in the distal heme cavity, in close proximity to the distal His(95), where it replaces the water molecule hydrogen bonded to Gln(91).
10766826	1	82	theme	human	146:150	arg1	myeloperoxidase					152:166	human myeloperoxidase	146:166	human myeloperoxidase	146:166	The x-ray crystal structure of human myeloperoxidase has been extended to 1.8 A resolution, using x-ray data recorded at -180 degrees C (r = 0.197, free r = 0.239).
10766826	4	83	theme	free	841:844	arg1	r					846:846	free r	841:846	free r	841:846	Determination of the x-ray crystal structure of a myeloperoxidase-bromide complex (r = 0.243, free r = 0.296) has shown that this chloride ion can be replaced by bromide.
10766826	2	84	from	groups	443:448	arg1	rings					461:465	pyrrole rings A and C	453:473	pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A	453:613	Results confirm that the heme is covalently attached to the protein via two ester linkages between the carboxyl groups of Glu(242) and Asp(94) and modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A.
10766826	2	84	from	groups	443:448	arg1	C					473:473	C	473:473	C	473:473	Results confirm that the heme is covalently attached to the protein via two ester linkages between the carboxyl groups of Glu(242) and Asp(94) and modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A.
10766826	2	84	from	groups	443:448	arg1	A					467:467	A	467:467	A	467:467	Results confirm that the heme is covalently attached to the protein via two ester linkages between the carboxyl groups of Glu(242) and Asp(94) and modified methyl groups on pyrrole rings A and C of the heme as well as a sulfonium ion linkage between the sulfur atom of Met(243) and the beta-carbon of the vinyl group on pyrrole ring A.
2808371	5	0	theme	Multiple	878:885	arg1	isoforms					899:906	Multiple protein 4.1 isoforms	878:906	Multiple protein 4.1 isoforms in erythroid and nonerythroid cells including major components of erythrocyte membrane proteins	878:1002	Multiple protein 4.1 isoforms in erythroid and nonerythroid cells including major components of erythrocyte membrane proteins, 4.1a and 4.1b, appear to contain this sequence since most immunochemically reactive proteins were labeled with [3H]galactose, with the exception of several variant polypeptides.
2808371	5	0	theme	Multiple	878:885	arg1	4.1b					1014:1017	4.1b	1014:1017	4.1b	1014:1017	Multiple protein 4.1 isoforms in erythroid and nonerythroid cells including major components of erythrocyte membrane proteins, 4.1a and 4.1b, appear to contain this sequence since most immunochemically reactive proteins were labeled with [3H]galactose, with the exception of several variant polypeptides.
2808371	5	0	theme	Multiple	878:885	arg1	4.1a					1005:1008	4.1a	1005:1008	4.1a	1005:1008	Multiple protein 4.1 isoforms in erythroid and nonerythroid cells including major components of erythrocyte membrane proteins, 4.1a and 4.1b, appear to contain this sequence since most immunochemically reactive proteins were labeled with [3H]galactose, with the exception of several variant polypeptides.
2808371	0	1	from	moiety	25:30	arg1	peptide					44:50	discrete peptide	35:50	discrete peptide of multiple protein 4.1 isoforms	35:83	O-N-acetyl-D-glucosamine moiety on discrete peptide of multiple protein 4.1 isoforms regulated by alternative pathways.
2808371	4	2	from	half	709:712	arg1	domain					778:783	the 22/24-kDa carboxyl-terminal domain	746:783	the 22/24-kDa carboxyl-terminal domain of protein 4.1, which is one of the discrete peptides regulated by alternative RNA splicing	746:875	This sequence corresponds to the carboxyl-terminal half of the 34-amino acid peptide in the 22/24-kDa carboxyl-terminal domain of protein 4.1, which is one of the discrete peptides regulated by alternative RNA splicing.
2808371	4	2	from	half	709:712	arg1	protein					788:794	protein 4.1	788:798	protein 4.1	788:798	This sequence corresponds to the carboxyl-terminal half of the 34-amino acid peptide in the 22/24-kDa carboxyl-terminal domain of protein 4.1, which is one of the discrete peptides regulated by alternative RNA splicing.
2808371	5	3	theme	reactive	1080:1087	arg1	proteins					1089:1096	most immunochemically reactive proteins	1058:1096	most immunochemically reactive proteins	1058:1096	Multiple protein 4.1 isoforms in erythroid and nonerythroid cells including major components of erythrocyte membrane proteins, 4.1a and 4.1b, appear to contain this sequence since most immunochemically reactive proteins were labeled with [3H]galactose, with the exception of several variant polypeptides.
2808371	2	4	theme	proteolytic	319:329	arg1	fragment					331:338	the proteolytic fragment	315:338	the proteolytic fragment containing the O-GlcNAc moiety	315:369	We determined the amino acid sequence of the proteolytic fragment containing the O-GlcNAc moiety after labeling the saccharide with [3H]galactose in the presence of bovine milk galactosyltransferase.
2808371	0	5	theme	alternative	98:108	arg1	pathways					110:117	alternative pathways	98:117	alternative pathways	98:117	O-N-acetyl-D-glucosamine moiety on discrete peptide of multiple protein 4.1 isoforms regulated by alternative pathways.
2808371	1	6	contain	possesses	174:182	arg1	protein					161:167	a cytoplasmic protein	147:167	a cytoplasmic protein that possesses a protein-saccharide modification structure, an O-N-acetyl-D-glucosamine (GlcNAc) moiety	147:271	Erythrocyte protein 4.1 is a cytoplasmic protein that possesses a protein-saccharide modification structure, an O-N-acetyl-D-glucosamine (GlcNAc) moiety.
2808371	1	6	contain	possesses	174:182	arg1	protein					132:138	Erythrocyte protein 4.1	120:142	Erythrocyte protein 4.1	120:142	Erythrocyte protein 4.1 is a cytoplasmic protein that possesses a protein-saccharide modification structure, an O-N-acetyl-D-glucosamine (GlcNAc) moiety.
2808371	1	6	contain	possesses	174:182	arg2	structure					218:226	a protein-saccharide modification structure	184:226	a protein-saccharide modification structure	184:226	Erythrocyte protein 4.1 is a cytoplasmic protein that possesses a protein-saccharide modification structure, an O-N-acetyl-D-glucosamine (GlcNAc) moiety.
2808371	1	6	contain	possesses	174:182	arg2	moiety					266:271	an O-N-acetyl-D-glucosamine (GlcNAc) moiety	229:271	an O-N-acetyl-D-glucosamine (GlcNAc) moiety	229:271	Erythrocyte protein 4.1 is a cytoplasmic protein that possesses a protein-saccharide modification structure, an O-N-acetyl-D-glucosamine (GlcNAc) moiety.
2808371	4	7	theme	RNA	864:866	arg1	splicing					868:875	alternative RNA splicing	852:875	alternative RNA splicing	852:875	This sequence corresponds to the carboxyl-terminal half of the 34-amino acid peptide in the 22/24-kDa carboxyl-terminal domain of protein 4.1, which is one of the discrete peptides regulated by alternative RNA splicing.
2808371	4	8	theme	carboxyl-terminal	691:707	arg1	half					709:712	the carboxyl-terminal half	687:712	the carboxyl-terminal half of the 34-amino acid peptide in the 22/24-kDa carboxyl-terminal domain of protein 4.1, which is one of the discrete peptides regulated by alternative RNA splicing	687:875	This sequence corresponds to the carboxyl-terminal half of the 34-amino acid peptide in the 22/24-kDa carboxyl-terminal domain of protein 4.1, which is one of the discrete peptides regulated by alternative RNA splicing.
2808371	5	9	theme	major	954:958	arg1	components					960:969	major components	954:969	major components of erythrocyte membrane proteins	954:1002	Multiple protein 4.1 isoforms in erythroid and nonerythroid cells including major components of erythrocyte membrane proteins, 4.1a and 4.1b, appear to contain this sequence since most immunochemically reactive proteins were labeled with [3H]galactose, with the exception of several variant polypeptides.
2808371	4	10	theme	peptide	735:741	arg1	half					709:712	the carboxyl-terminal half	687:712	the carboxyl-terminal half of the 34-amino acid peptide in the 22/24-kDa carboxyl-terminal domain of protein 4.1, which is one of the discrete peptides regulated by alternative RNA splicing	687:875	This sequence corresponds to the carboxyl-terminal half of the 34-amino acid peptide in the 22/24-kDa carboxyl-terminal domain of protein 4.1, which is one of the discrete peptides regulated by alternative RNA splicing.
2808371	3	11	theme	following	556:564	arg1	Thr-Ala-Gln-Thr-Ile-Thr-Ser-Glu-Thr-Pro-Ser-Ser-Thr-Thr-Thr-Thr-Gln-Ile-Thr-Lys					576:654	the following sequence: Thr-Ala-Gln-Thr-Ile-Thr-Ser-Glu-Thr-Pro-Ser-Ser-Thr-Thr-Thr-Thr-Gln-Ile-Thr-Lys	552:654	the following sequence: Thr-Ala-Gln-Thr-Ile-Thr-Ser-Glu-Thr-Pro-Ser-Ser-Thr-Thr-Thr-Thr-Gln-Ile-Thr-Lys	552:654	Glycosylation appears to occur on one or more serine or threonine residues in the following sequence: Thr-Ala-Gln-Thr-Ile-Thr-Ser-Glu-Thr-Pro-Ser-Ser-Thr-Thr-Thr-Thr-Gln-Ile-Thr-Lys .
2808371	4	12	theme	protein	788:794	arg1	domain					778:783	the 22/24-kDa carboxyl-terminal domain	746:783	the 22/24-kDa carboxyl-terminal domain of protein 4.1, which is one of the discrete peptides regulated by alternative RNA splicing	746:875	This sequence corresponds to the carboxyl-terminal half of the 34-amino acid peptide in the 22/24-kDa carboxyl-terminal domain of protein 4.1, which is one of the discrete peptides regulated by alternative RNA splicing.
2808371	4	12	theme	protein	788:794	arg1	protein					788:794	protein 4.1	788:798	protein 4.1	788:798	This sequence corresponds to the carboxyl-terminal half of the 34-amino acid peptide in the 22/24-kDa carboxyl-terminal domain of protein 4.1, which is one of the discrete peptides regulated by alternative RNA splicing.
2808371	5	13	theme	erythrocyte	974:984	arg1	proteins					995:1002	erythrocyte membrane proteins	974:1002	erythrocyte membrane proteins	974:1002	Multiple protein 4.1 isoforms in erythroid and nonerythroid cells including major components of erythrocyte membrane proteins, 4.1a and 4.1b, appear to contain this sequence since most immunochemically reactive proteins were labeled with [3H]galactose, with the exception of several variant polypeptides.
2808371	2	14	theme	acid	298:301	arg1	sequence					303:310	the amino acid sequence	288:310	the amino acid sequence of the proteolytic fragment containing the O-GlcNAc moiety	288:369	We determined the amino acid sequence of the proteolytic fragment containing the O-GlcNAc moiety after labeling the saccharide with [3H]galactose in the presence of bovine milk galactosyltransferase.
2808371	4	15	from	domain	778:783	arg1	half					709:712	the carboxyl-terminal half	687:712	the carboxyl-terminal half of the 34-amino acid peptide in the 22/24-kDa carboxyl-terminal domain of protein 4.1, which is one of the discrete peptides regulated by alternative RNA splicing	687:875	This sequence corresponds to the carboxyl-terminal half of the 34-amino acid peptide in the 22/24-kDa carboxyl-terminal domain of protein 4.1, which is one of the discrete peptides regulated by alternative RNA splicing.
2808371	1	16	theme	protein-saccharide	186:203	arg1	moiety					266:271	an O-N-acetyl-D-glucosamine (GlcNAc) moiety	229:271	an O-N-acetyl-D-glucosamine (GlcNAc) moiety	229:271	Erythrocyte protein 4.1 is a cytoplasmic protein that possesses a protein-saccharide modification structure, an O-N-acetyl-D-glucosamine (GlcNAc) moiety.
2808371	1	16	theme	protein-saccharide	186:203	arg1	structure					218:226	a protein-saccharide modification structure	184:226	a protein-saccharide modification structure	184:226	Erythrocyte protein 4.1 is a cytoplasmic protein that possesses a protein-saccharide modification structure, an O-N-acetyl-D-glucosamine (GlcNAc) moiety.
2808371	5	17	theme	erythroid	911:919	arg1	components					960:969	major components	954:969	major components of erythrocyte membrane proteins	954:1002	Multiple protein 4.1 isoforms in erythroid and nonerythroid cells including major components of erythrocyte membrane proteins, 4.1a and 4.1b, appear to contain this sequence since most immunochemically reactive proteins were labeled with [3H]galactose, with the exception of several variant polypeptides.
2808371	5	17	theme	erythroid	911:919	arg1	cells					938:942	erythroid and nonerythroid cells	911:942	erythroid and nonerythroid cells including major components of erythrocyte membrane proteins	911:1002	Multiple protein 4.1 isoforms in erythroid and nonerythroid cells including major components of erythrocyte membrane proteins, 4.1a and 4.1b, appear to contain this sequence since most immunochemically reactive proteins were labeled with [3H]galactose, with the exception of several variant polypeptides.
2808371	1	18	theme	modification	205:216	arg1	moiety					266:271	an O-N-acetyl-D-glucosamine (GlcNAc) moiety	229:271	an O-N-acetyl-D-glucosamine (GlcNAc) moiety	229:271	Erythrocyte protein 4.1 is a cytoplasmic protein that possesses a protein-saccharide modification structure, an O-N-acetyl-D-glucosamine (GlcNAc) moiety.
2808371	1	18	theme	modification	205:216	arg1	structure					218:226	a protein-saccharide modification structure	184:226	a protein-saccharide modification structure	184:226	Erythrocyte protein 4.1 is a cytoplasmic protein that possesses a protein-saccharide modification structure, an O-N-acetyl-D-glucosamine (GlcNAc) moiety.
2808371	0	19	theme	O-N-acetyl-D-glucosamine	0:23	arg1	moiety					25:30	O-N-acetyl-D-glucosamine moiety	0:30	O-N-acetyl-D-glucosamine moiety on discrete peptide of multiple protein 4.1 isoforms	0:83	O-N-acetyl-D-glucosamine moiety on discrete peptide of multiple protein 4.1 isoforms regulated by alternative pathways.
2808371	4	20	theme	peptides	830:837	arg1	peptides					830:837	the discrete peptides	817:837	the discrete peptides regulated by alternative RNA splicing	817:875	This sequence corresponds to the carboxyl-terminal half of the 34-amino acid peptide in the 22/24-kDa carboxyl-terminal domain of protein 4.1, which is one of the discrete peptides regulated by alternative RNA splicing.
2808371	4	20	theme	peptides	830:837	arg1	one					810:812	one	810:812	one	810:812	This sequence corresponds to the carboxyl-terminal half of the 34-amino acid peptide in the 22/24-kDa carboxyl-terminal domain of protein 4.1, which is one of the discrete peptides regulated by alternative RNA splicing.
2808371	0	21	theme	discrete	35:42	arg1	peptide					44:50	discrete peptide	35:50	discrete peptide of multiple protein 4.1 isoforms	35:83	O-N-acetyl-D-glucosamine moiety on discrete peptide of multiple protein 4.1 isoforms regulated by alternative pathways.
2808371	2	22	theme	fragment	331:338	arg1	sequence					303:310	the amino acid sequence	288:310	the amino acid sequence of the proteolytic fragment containing the O-GlcNAc moiety	288:369	We determined the amino acid sequence of the proteolytic fragment containing the O-GlcNAc moiety after labeling the saccharide with [3H]galactose in the presence of bovine milk galactosyltransferase.
2808371	2	23	theme	milk	446:449	arg1	galactosyltransferase					451:471	bovine milk galactosyltransferase	439:471	bovine milk galactosyltransferase	439:471	We determined the amino acid sequence of the proteolytic fragment containing the O-GlcNAc moiety after labeling the saccharide with [3H]galactose in the presence of bovine milk galactosyltransferase.
2808371	2	24	theme	galactosyltransferase	451:471	arg1	presence					427:434	the presence	423:434	the presence of bovine milk galactosyltransferase	423:471	We determined the amino acid sequence of the proteolytic fragment containing the O-GlcNAc moiety after labeling the saccharide with [3H]galactose in the presence of bovine milk galactosyltransferase.
2808371	3	25	dep	serine	520:525	arg1	residues					540:547	residues	540:547	residues	540:547	Glycosylation appears to occur on one or more serine or threonine residues in the following sequence: Thr-Ala-Gln-Thr-Ile-Thr-Ser-Glu-Thr-Pro-Ser-Ser-Thr-Thr-Thr-Thr-Gln-Ile-Thr-Lys .
2808371	1	26	theme	Erythrocyte	120:130	arg1	protein					161:167	a cytoplasmic protein	147:167	a cytoplasmic protein that possesses a protein-saccharide modification structure, an O-N-acetyl-D-glucosamine (GlcNAc) moiety	147:271	Erythrocyte protein 4.1 is a cytoplasmic protein that possesses a protein-saccharide modification structure, an O-N-acetyl-D-glucosamine (GlcNAc) moiety.
2808371	1	26	theme	Erythrocyte	120:130	arg1	protein					132:138	Erythrocyte protein 4.1	120:142	Erythrocyte protein 4.1	120:142	Erythrocyte protein 4.1 is a cytoplasmic protein that possesses a protein-saccharide modification structure, an O-N-acetyl-D-glucosamine (GlcNAc) moiety.
2808371	2	27	theme	bovine	439:444	arg1	galactosyltransferase					451:471	bovine milk galactosyltransferase	439:471	bovine milk galactosyltransferase	439:471	We determined the amino acid sequence of the proteolytic fragment containing the O-GlcNAc moiety after labeling the saccharide with [3H]galactose in the presence of bovine milk galactosyltransferase.
2808371	5	28	theme	protein	887:893	arg1	isoforms					899:906	Multiple protein 4.1 isoforms	878:906	Multiple protein 4.1 isoforms in erythroid and nonerythroid cells including major components of erythrocyte membrane proteins	878:1002	Multiple protein 4.1 isoforms in erythroid and nonerythroid cells including major components of erythrocyte membrane proteins, 4.1a and 4.1b, appear to contain this sequence since most immunochemically reactive proteins were labeled with [3H]galactose, with the exception of several variant polypeptides.
2808371	5	28	theme	protein	887:893	arg1	4.1b					1014:1017	4.1b	1014:1017	4.1b	1014:1017	Multiple protein 4.1 isoforms in erythroid and nonerythroid cells including major components of erythrocyte membrane proteins, 4.1a and 4.1b, appear to contain this sequence since most immunochemically reactive proteins were labeled with [3H]galactose, with the exception of several variant polypeptides.
2808371	5	28	theme	protein	887:893	arg1	4.1a					1005:1008	4.1a	1005:1008	4.1a	1005:1008	Multiple protein 4.1 isoforms in erythroid and nonerythroid cells including major components of erythrocyte membrane proteins, 4.1a and 4.1b, appear to contain this sequence since most immunochemically reactive proteins were labeled with [3H]galactose, with the exception of several variant polypeptides.
2808371	4	29	theme	22/24-kDa	750:758	arg1	domain					778:783	the 22/24-kDa carboxyl-terminal domain	746:783	the 22/24-kDa carboxyl-terminal domain of protein 4.1, which is one of the discrete peptides regulated by alternative RNA splicing	746:875	This sequence corresponds to the carboxyl-terminal half of the 34-amino acid peptide in the 22/24-kDa carboxyl-terminal domain of protein 4.1, which is one of the discrete peptides regulated by alternative RNA splicing.
2808371	4	29	theme	22/24-kDa	750:758	arg1	protein					788:794	protein 4.1	788:798	protein 4.1	788:798	This sequence corresponds to the carboxyl-terminal half of the 34-amino acid peptide in the 22/24-kDa carboxyl-terminal domain of protein 4.1, which is one of the discrete peptides regulated by alternative RNA splicing.
2808371	4	30	from	peptide	735:741	arg1	domain					778:783	the 22/24-kDa carboxyl-terminal domain	746:783	the 22/24-kDa carboxyl-terminal domain of protein 4.1, which is one of the discrete peptides regulated by alternative RNA splicing	746:875	This sequence corresponds to the carboxyl-terminal half of the 34-amino acid peptide in the 22/24-kDa carboxyl-terminal domain of protein 4.1, which is one of the discrete peptides regulated by alternative RNA splicing.
2808371	4	30	from	peptide	735:741	arg1	protein					788:794	protein 4.1	788:798	protein 4.1	788:798	This sequence corresponds to the carboxyl-terminal half of the 34-amino acid peptide in the 22/24-kDa carboxyl-terminal domain of protein 4.1, which is one of the discrete peptides regulated by alternative RNA splicing.
2808371	1	31	theme	O-N-acetyl-D-glucosamine	232:255	arg1	moiety					266:271	an O-N-acetyl-D-glucosamine (GlcNAc) moiety	229:271	an O-N-acetyl-D-glucosamine (GlcNAc) moiety	229:271	Erythrocyte protein 4.1 is a cytoplasmic protein that possesses a protein-saccharide modification structure, an O-N-acetyl-D-glucosamine (GlcNAc) moiety.
2808371	1	31	theme	O-N-acetyl-D-glucosamine	232:255	arg1	structure					218:226	a protein-saccharide modification structure	184:226	a protein-saccharide modification structure	184:226	Erythrocyte protein 4.1 is a cytoplasmic protein that possesses a protein-saccharide modification structure, an O-N-acetyl-D-glucosamine (GlcNAc) moiety.
2808371	5	32	theme	membrane	986:993	arg1	proteins					995:1002	erythrocyte membrane proteins	974:1002	erythrocyte membrane proteins	974:1002	Multiple protein 4.1 isoforms in erythroid and nonerythroid cells including major components of erythrocyte membrane proteins, 4.1a and 4.1b, appear to contain this sequence since most immunochemically reactive proteins were labeled with [3H]galactose, with the exception of several variant polypeptides.
2808371	5	33	theme	proteins	995:1002	arg1	components					960:969	major components	954:969	major components of erythrocyte membrane proteins	954:1002	Multiple protein 4.1 isoforms in erythroid and nonerythroid cells including major components of erythrocyte membrane proteins, 4.1a and 4.1b, appear to contain this sequence since most immunochemically reactive proteins were labeled with [3H]galactose, with the exception of several variant polypeptides.
2808371	5	34	theme	nonerythroid	925:936	arg1	components					960:969	major components	954:969	major components of erythrocyte membrane proteins	954:1002	Multiple protein 4.1 isoforms in erythroid and nonerythroid cells including major components of erythrocyte membrane proteins, 4.1a and 4.1b, appear to contain this sequence since most immunochemically reactive proteins were labeled with [3H]galactose, with the exception of several variant polypeptides.
2808371	5	34	theme	nonerythroid	925:936	arg1	cells					938:942	erythroid and nonerythroid cells	911:942	erythroid and nonerythroid cells including major components of erythrocyte membrane proteins	911:1002	Multiple protein 4.1 isoforms in erythroid and nonerythroid cells including major components of erythrocyte membrane proteins, 4.1a and 4.1b, appear to contain this sequence since most immunochemically reactive proteins were labeled with [3H]galactose, with the exception of several variant polypeptides.
2808371	0	35	theme	protein	64:70	arg1	isoforms					76:83	multiple protein 4.1 isoforms	55:83	multiple protein 4.1 isoforms	55:83	O-N-acetyl-D-glucosamine moiety on discrete peptide of multiple protein 4.1 isoforms regulated by alternative pathways.
2808371	5	36	contain	contain	1030:1036	arg1	isoforms					899:906	Multiple protein 4.1 isoforms	878:906	Multiple protein 4.1 isoforms in erythroid and nonerythroid cells including major components of erythrocyte membrane proteins	878:1002	Multiple protein 4.1 isoforms in erythroid and nonerythroid cells including major components of erythrocyte membrane proteins, 4.1a and 4.1b, appear to contain this sequence since most immunochemically reactive proteins were labeled with [3H]galactose, with the exception of several variant polypeptides.
2808371	5	36	contain	contain	1030:1036	arg2	sequence					1043:1050	this sequence	1038:1050	this sequence	1038:1050	Multiple protein 4.1 isoforms in erythroid and nonerythroid cells including major components of erythrocyte membrane proteins, 4.1a and 4.1b, appear to contain this sequence since most immunochemically reactive proteins were labeled with [3H]galactose, with the exception of several variant polypeptides.
2808371	5	36	contain	contain	1030:1036	arg1	4.1a					1005:1008	4.1a	1005:1008	4.1a	1005:1008	Multiple protein 4.1 isoforms in erythroid and nonerythroid cells including major components of erythrocyte membrane proteins, 4.1a and 4.1b, appear to contain this sequence since most immunochemically reactive proteins were labeled with [3H]galactose, with the exception of several variant polypeptides.
2808371	5	36	contain	contain	1030:1036	arg1	4.1b					1014:1017	4.1b	1014:1017	4.1b	1014:1017	Multiple protein 4.1 isoforms in erythroid and nonerythroid cells including major components of erythrocyte membrane proteins, 4.1a and 4.1b, appear to contain this sequence since most immunochemically reactive proteins were labeled with [3H]galactose, with the exception of several variant polypeptides.
2808371	0	37	theme	multiple	55:62	arg1	isoforms					76:83	multiple protein 4.1 isoforms	55:83	multiple protein 4.1 isoforms	55:83	O-N-acetyl-D-glucosamine moiety on discrete peptide of multiple protein 4.1 isoforms regulated by alternative pathways.
2808371	2	38	contain	containing	340:349	arg1	fragment					331:338	the proteolytic fragment	315:338	the proteolytic fragment containing the O-GlcNAc moiety	315:369	We determined the amino acid sequence of the proteolytic fragment containing the O-GlcNAc moiety after labeling the saccharide with [3H]galactose in the presence of bovine milk galactosyltransferase.
2808371	2	38	contain	containing	340:349	arg2	moiety					364:369	the O-GlcNAc moiety	351:369	the O-GlcNAc moiety	351:369	We determined the amino acid sequence of the proteolytic fragment containing the O-GlcNAc moiety after labeling the saccharide with [3H]galactose in the presence of bovine milk galactosyltransferase.
2808371	2	39	with	saccharide	390:399	arg1	galactose					410:418	[3H]galactose	406:418	[3H]galactose	406:418	We determined the amino acid sequence of the proteolytic fragment containing the O-GlcNAc moiety after labeling the saccharide with [3H]galactose in the presence of bovine milk galactosyltransferase.
2808371	6	40	theme	O-GlcNAc	1264:1271	arg1	linkage					1273:1279	the O-GlcNAc linkage	1260:1279	the O-GlcNAc linkage	1260:1279	These results appear to suggest the functional or biological significance of the O-GlcNAc linkage in protein 4.1.
2808371	5	41	theme	several	1153:1159	arg1	polypeptides					1169:1180	several variant polypeptides	1153:1180	several variant polypeptides	1153:1180	Multiple protein 4.1 isoforms in erythroid and nonerythroid cells including major components of erythrocyte membrane proteins, 4.1a and 4.1b, appear to contain this sequence since most immunochemically reactive proteins were labeled with [3H]galactose, with the exception of several variant polypeptides.
2808371	2	42	theme	amino	292:296	arg1	sequence					303:310	the amino acid sequence	288:310	the amino acid sequence of the proteolytic fragment containing the O-GlcNAc moiety	288:369	We determined the amino acid sequence of the proteolytic fragment containing the O-GlcNAc moiety after labeling the saccharide with [3H]galactose in the presence of bovine milk galactosyltransferase.
2808371	6	43	from	significance	1244:1255	arg1	protein					1284:1290	protein 4.1	1284:1294	protein 4.1	1284:1294	These results appear to suggest the functional or biological significance of the O-GlcNAc linkage in protein 4.1.
2808371	4	44	theme	discrete	821:828	arg1	peptides					830:837	the discrete peptides	817:837	the discrete peptides regulated by alternative RNA splicing	817:875	This sequence corresponds to the carboxyl-terminal half of the 34-amino acid peptide in the 22/24-kDa carboxyl-terminal domain of protein 4.1, which is one of the discrete peptides regulated by alternative RNA splicing.
2808371	4	45	theme	alternative	852:862	arg1	splicing					868:875	alternative RNA splicing	852:875	alternative RNA splicing	852:875	This sequence corresponds to the carboxyl-terminal half of the 34-amino acid peptide in the 22/24-kDa carboxyl-terminal domain of protein 4.1, which is one of the discrete peptides regulated by alternative RNA splicing.
2808371	1	46	theme	GlcNAc	258:263	arg1	moiety					266:271	an O-N-acetyl-D-glucosamine (GlcNAc) moiety	229:271	an O-N-acetyl-D-glucosamine (GlcNAc) moiety	229:271	Erythrocyte protein 4.1 is a cytoplasmic protein that possesses a protein-saccharide modification structure, an O-N-acetyl-D-glucosamine (GlcNAc) moiety.
2808371	1	46	theme	GlcNAc	258:263	arg1	structure					218:226	a protein-saccharide modification structure	184:226	a protein-saccharide modification structure	184:226	Erythrocyte protein 4.1 is a cytoplasmic protein that possesses a protein-saccharide modification structure, an O-N-acetyl-D-glucosamine (GlcNAc) moiety.
2808371	3	47	theme	sequence	566:573	arg1	Thr-Ala-Gln-Thr-Ile-Thr-Ser-Glu-Thr-Pro-Ser-Ser-Thr-Thr-Thr-Thr-Gln-Ile-Thr-Lys					576:654	the following sequence: Thr-Ala-Gln-Thr-Ile-Thr-Ser-Glu-Thr-Pro-Ser-Ser-Thr-Thr-Thr-Thr-Gln-Ile-Thr-Lys	552:654	the following sequence: Thr-Ala-Gln-Thr-Ile-Thr-Ser-Glu-Thr-Pro-Ser-Ser-Thr-Thr-Thr-Thr-Gln-Ile-Thr-Lys	552:654	Glycosylation appears to occur on one or more serine or threonine residues in the following sequence: Thr-Ala-Gln-Thr-Ile-Thr-Ser-Glu-Thr-Pro-Ser-Ser-Thr-Thr-Thr-Thr-Gln-Ile-Thr-Lys .
2808371	5	48	theme	variant	1161:1167	arg1	polypeptides					1169:1180	several variant polypeptides	1153:1180	several variant polypeptides	1153:1180	Multiple protein 4.1 isoforms in erythroid and nonerythroid cells including major components of erythrocyte membrane proteins, 4.1a and 4.1b, appear to contain this sequence since most immunochemically reactive proteins were labeled with [3H]galactose, with the exception of several variant polypeptides.
2808371	2	49	theme	O-GlcNAc	355:362	arg1	moiety					364:369	the O-GlcNAc moiety	351:369	the O-GlcNAc moiety	351:369	We determined the amino acid sequence of the proteolytic fragment containing the O-GlcNAc moiety after labeling the saccharide with [3H]galactose in the presence of bovine milk galactosyltransferase.
2808371	6	50	theme	biological	1233:1242	arg1	significance					1244:1255	the functional or biological significance	1215:1255	the functional or biological significance of the O-GlcNAc linkage in protein 4.1	1215:1294	These results appear to suggest the functional or biological significance of the O-GlcNAc linkage in protein 4.1.
2808371	0	51	theme	isoforms	76:83	arg1	peptide					44:50	discrete peptide	35:50	discrete peptide of multiple protein 4.1 isoforms	35:83	O-N-acetyl-D-glucosamine moiety on discrete peptide of multiple protein 4.1 isoforms regulated by alternative pathways.
2808371	5	52	theme	polypeptides	1169:1180	arg1	exception					1140:1148	the exception	1136:1148	the exception of several variant polypeptides	1136:1180	Multiple protein 4.1 isoforms in erythroid and nonerythroid cells including major components of erythrocyte membrane proteins, 4.1a and 4.1b, appear to contain this sequence since most immunochemically reactive proteins were labeled with [3H]galactose, with the exception of several variant polypeptides.
2808371	1	53	theme	cytoplasmic	149:159	arg1	protein					161:167	a cytoplasmic protein	147:167	a cytoplasmic protein that possesses a protein-saccharide modification structure, an O-N-acetyl-D-glucosamine (GlcNAc) moiety	147:271	Erythrocyte protein 4.1 is a cytoplasmic protein that possesses a protein-saccharide modification structure, an O-N-acetyl-D-glucosamine (GlcNAc) moiety.
2808371	1	53	theme	cytoplasmic	149:159	arg1	protein					132:138	Erythrocyte protein 4.1	120:142	Erythrocyte protein 4.1	120:142	Erythrocyte protein 4.1 is a cytoplasmic protein that possesses a protein-saccharide modification structure, an O-N-acetyl-D-glucosamine (GlcNAc) moiety.
2808371	4	54	theme	carboxyl-terminal	760:776	arg1	domain					778:783	the 22/24-kDa carboxyl-terminal domain	746:783	the 22/24-kDa carboxyl-terminal domain of protein 4.1, which is one of the discrete peptides regulated by alternative RNA splicing	746:875	This sequence corresponds to the carboxyl-terminal half of the 34-amino acid peptide in the 22/24-kDa carboxyl-terminal domain of protein 4.1, which is one of the discrete peptides regulated by alternative RNA splicing.
2808371	4	54	theme	carboxyl-terminal	760:776	arg1	protein					788:794	protein 4.1	788:798	protein 4.1	788:798	This sequence corresponds to the carboxyl-terminal half of the 34-amino acid peptide in the 22/24-kDa carboxyl-terminal domain of protein 4.1, which is one of the discrete peptides regulated by alternative RNA splicing.
2808371	4	55	theme	acid	730:733	arg1	peptide					735:741	the 34-amino acid peptide	717:741	the 34-amino acid peptide in the 22/24-kDa carboxyl-terminal domain of protein 4.1, which is one of the discrete peptides regulated by alternative RNA splicing	717:875	This sequence corresponds to the carboxyl-terminal half of the 34-amino acid peptide in the 22/24-kDa carboxyl-terminal domain of protein 4.1, which is one of the discrete peptides regulated by alternative RNA splicing.
2808371	6	56	theme	functional	1219:1228	arg1	significance					1244:1255	the functional or biological significance	1215:1255	the functional or biological significance of the O-GlcNAc linkage in protein 4.1	1215:1294	These results appear to suggest the functional or biological significance of the O-GlcNAc linkage in protein 4.1.
2808371	5	57	from	isoforms	899:906	arg1	components					960:969	major components	954:969	major components of erythrocyte membrane proteins	954:1002	Multiple protein 4.1 isoforms in erythroid and nonerythroid cells including major components of erythrocyte membrane proteins, 4.1a and 4.1b, appear to contain this sequence since most immunochemically reactive proteins were labeled with [3H]galactose, with the exception of several variant polypeptides.
2808371	5	57	from	isoforms	899:906	arg1	cells					938:942	erythroid and nonerythroid cells	911:942	erythroid and nonerythroid cells including major components of erythrocyte membrane proteins	911:1002	Multiple protein 4.1 isoforms in erythroid and nonerythroid cells including major components of erythrocyte membrane proteins, 4.1a and 4.1b, appear to contain this sequence since most immunochemically reactive proteins were labeled with [3H]galactose, with the exception of several variant polypeptides.
2808371	6	58	theme	linkage	1273:1279	arg1	significance					1244:1255	the functional or biological significance	1215:1255	the functional or biological significance of the O-GlcNAc linkage in protein 4.1	1215:1294	These results appear to suggest the functional or biological significance of the O-GlcNAc linkage in protein 4.1.
2808371	4	59	theme	34-amino	721:728	arg1	peptide					735:741	the 34-amino acid peptide	717:741	the 34-amino acid peptide in the 22/24-kDa carboxyl-terminal domain of protein 4.1, which is one of the discrete peptides regulated by alternative RNA splicing	717:875	This sequence corresponds to the carboxyl-terminal half of the 34-amino acid peptide in the 22/24-kDa carboxyl-terminal domain of protein 4.1, which is one of the discrete peptides regulated by alternative RNA splicing.
6192908	2	0	theme	paper	347:351	arg1	electrophoresis					353:367	paper electrophoresis	347:367	paper electrophoresis	347:367	The oligosaccharides were separated into a neutral and two acidic oligosaccharides by paper electrophoresis.
6192908	1	1	theme	nude	157:160	arg1	mice					162:165	nude mice	157:165	nude mice	157:165	The carbohydrate moiety of alpha-fetoprotein purified from human yolk sac tumors grown in nude mice was quantitatively released from the polypeptide chain as oligosaccharides by hydrazinolysis.
6192908	1	2	theme	alpha-fetoprotein	94:110	arg1	moiety					84:89	The carbohydrate moiety	67:89	The carbohydrate moiety of alpha-fetoprotein purified from human yolk sac tumors grown in nude mice	67:165	The carbohydrate moiety of alpha-fetoprotein purified from human yolk sac tumors grown in nude mice was quantitatively released from the polypeptide chain as oligosaccharides by hydrazinolysis.
6192908	1	3	attach	released	186:193	arg2	moiety					84:89	The carbohydrate moiety	67:89	The carbohydrate moiety of alpha-fetoprotein purified from human yolk sac tumors grown in nude mice	67:165	The carbohydrate moiety of alpha-fetoprotein purified from human yolk sac tumors grown in nude mice was quantitatively released from the polypeptide chain as oligosaccharides by hydrazinolysis.
6192908	1	3	attach	released	186:193	arg1	chain					216:220	the polypeptide chain	200:220	the polypeptide chain as oligosaccharides	200:240	The carbohydrate moiety of alpha-fetoprotein purified from human yolk sac tumors grown in nude mice was quantitatively released from the polypeptide chain as oligosaccharides by hydrazinolysis.
6192908	1	4	theme	human	126:130	arg1	sac					137:139	human yolk sac	126:139	human yolk sac tumors grown in nude mice	126:165	The carbohydrate moiety of alpha-fetoprotein purified from human yolk sac tumors grown in nude mice was quantitatively released from the polypeptide chain as oligosaccharides by hydrazinolysis.
6192908	1	5	theme	carbohydrate	71:82	arg1	moiety					84:89	The carbohydrate moiety	67:89	The carbohydrate moiety of alpha-fetoprotein purified from human yolk sac tumors grown in nude mice	67:165	The carbohydrate moiety of alpha-fetoprotein purified from human yolk sac tumors grown in nude mice was quantitatively released from the polypeptide chain as oligosaccharides by hydrazinolysis.
6192908	1	6	theme	yolk	132:135	arg1	sac					137:139	human yolk sac	126:139	human yolk sac tumors grown in nude mice	126:165	The carbohydrate moiety of alpha-fetoprotein purified from human yolk sac tumors grown in nude mice was quantitatively released from the polypeptide chain as oligosaccharides by hydrazinolysis.
6192908	0	7	theme	Sugar	0:4	arg1	chain					6:10	Sugar chain	0:10	Sugar chain of alpha-fetoprotein	0:31	Sugar chain of alpha-fetoprotein produced in human yolk sac tumor.
6192908	1	8	theme	polypeptide	204:214	arg1	chain					216:220	the polypeptide chain	200:220	the polypeptide chain as oligosaccharides	200:240	The carbohydrate moiety of alpha-fetoprotein purified from human yolk sac tumors grown in nude mice was quantitatively released from the polypeptide chain as oligosaccharides by hydrazinolysis.
6192908	0	9	theme	yolk	51:54	arg1	tumor					60:64	human yolk sac tumor	45:64	human yolk sac tumor	45:64	Sugar chain of alpha-fetoprotein produced in human yolk sac tumor.
6192908	2	10	theme	acidic	320:325	arg1	oligosaccharides					327:342	two acidic oligosaccharides	316:342	two acidic oligosaccharides	316:342	The oligosaccharides were separated into a neutral and two acidic oligosaccharides by paper electrophoresis.
6192908	1	11	theme	sac	137:139	arg1	tumors					141:146	human yolk sac tumors	126:146	human yolk sac tumors grown in nude mice	126:165	The carbohydrate moiety of alpha-fetoprotein purified from human yolk sac tumors grown in nude mice was quantitatively released from the polypeptide chain as oligosaccharides by hydrazinolysis.
6192908	0	12	theme	alpha-fetoprotein	15:31	arg1	chain					6:10	Sugar chain	0:10	Sugar chain of alpha-fetoprotein	0:31	Sugar chain of alpha-fetoprotein produced in human yolk sac tumor.
6192908	0	13	theme	sac	56:58	arg1	tumor					60:64	human yolk sac tumor	45:64	human yolk sac tumor	45:64	Sugar chain of alpha-fetoprotein produced in human yolk sac tumor.
6192908	0	14	theme	human	45:49	arg1	tumor					60:64	human yolk sac tumor	45:64	human yolk sac tumor	45:64	Sugar chain of alpha-fetoprotein produced in human yolk sac tumor.
8329384	1	0	theme	EGF	295:297	arg1	domains					299:305	the N-terminal EGF domains	280:305	the N-terminal EGF domains of several coagulation/fibrinolytic proteins	280:350	O-Linked fucose has been found attached to Thr/Ser residues within the sequence Cys-X-X-Gly-Gly-Thr/Ser-Cys in the N-terminal EGF domains of several coagulation/fibrinolytic proteins.
8329384	1	0	theme	EGF	295:297	arg1	proteins					343:350	several coagulation/fibrinolytic proteins	310:350	several coagulation/fibrinolytic proteins	310:350	O-Linked fucose has been found attached to Thr/Ser residues within the sequence Cys-X-X-Gly-Gly-Thr/Ser-Cys in the N-terminal EGF domains of several coagulation/fibrinolytic proteins.
8329384	5	1	dep	IX	1016:1017	arg1	residues					1019:1026	residues 57-65	1019:1032	factor IX residues 57-65	1009:1032	The involvement of fucose in the carbohydrate-peptide linkage was confirmed by two-dimensional 1H NMR spectroscopic analysis of the glycopeptide containing factor IX residues 57-65.
8329384	6	2	theme	complete	1039:1046	arg1	1-->O-Ser61					1233:1243	NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-Ser61	1172:1243	NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-Ser61	1172:1243	The complete structure of the tetrasaccharide was obtained by methylation analysis and two-dimensional 1H TOCSY and ROESY experiments as NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-Ser61.
8329384	6	2	theme	complete	1039:1046	arg1	structure					1048:1056	The complete structure	1035:1056	The complete structure of the tetrasaccharide	1035:1079	The complete structure of the tetrasaccharide was obtained by methylation analysis and two-dimensional 1H TOCSY and ROESY experiments as NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-Ser61.
8329384	0	3	theme	2-->6	74:78	arg1	beta					102:105	tetrasaccharide NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta	46:105	the tetrasaccharide NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-linked to serine 61 of human factor IX	42:166	Identification and structural analysis of the tetrasaccharide NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-linked to serine 61 of human factor IX.
8329384	0	3	theme	2-->6	74:78	arg1	1-->3					107:111	1-->3	107:111	1-->3	107:111	Identification and structural analysis of the tetrasaccharide NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-linked to serine 61 of human factor IX.
8329384	0	4	theme	1-->O-linked	123:134	arg1	alpha					117:121	the tetrasaccharide NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha	42:121	the tetrasaccharide NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-linked to serine 61 of human factor IX	42:166	Identification and structural analysis of the tetrasaccharide NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-linked to serine 61 of human factor IX.
8329384	2	5	theme	tetrasaccharide	560:574	arg1	presence					546:553	the presence	542:553	the presence of a tetrasaccharide containing one residue each of sialic acid, galactose, N-acetylglucosamine, and fucose	542:661	Carbohydrate composition and mass spectrometric analyses of tryptic and thermolytic peptides containing the corresponding site (Ser-61) in the first EGF domain of human factor IX indicated the presence of a tetrasaccharide containing one residue each of sialic acid, galactose, N-acetylglucosamine, and fucose.
8329384	0	6	theme	beta	84:87	arg1	beta					102:105	tetrasaccharide NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta	46:105	the tetrasaccharide NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-linked to serine 61 of human factor IX	42:166	Identification and structural analysis of the tetrasaccharide NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-linked to serine 61 of human factor IX.
8329384	0	6	theme	beta	84:87	arg1	1-->3					107:111	1-->3	107:111	1-->3	107:111	Identification and structural analysis of the tetrasaccharide NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-linked to serine 61 of human factor IX.
8329384	3	7	theme	Ser-61	668:673	arg1	tetrasaccharide					675:689	The Ser-61 tetrasaccharide	664:689	The Ser-61 tetrasaccharide	664:689	The Ser-61 tetrasaccharide was not susceptible to alpha-fucosidase digestion.
8329384	3	7	theme	Ser-61	668:673	arg1	susceptible					699:709	susceptible	699:709	susceptible	699:709	The Ser-61 tetrasaccharide was not susceptible to alpha-fucosidase digestion.
8329384	4	8	theme	mass	769:772	arg1	analysis					788:795	mass spectrometric analysis	769:795	mass spectrometric analysis	769:795	Fragments generated during mass spectrometric analysis indicated that fucose was the attachment sugar residue.
8329384	6	9	theme	2-->6	1184:1188	arg1	1-->3					1217:1221	1-->3	1217:1221	1-->3	1217:1221	The complete structure of the tetrasaccharide was obtained by methylation analysis and two-dimensional 1H TOCSY and ROESY experiments as NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-Ser61.
8329384	6	9	theme	2-->6	1184:1188	arg1	beta					1212:1215	NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta	1172:1215	NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-Ser61	1172:1243	The complete structure of the tetrasaccharide was obtained by methylation analysis and two-dimensional 1H TOCSY and ROESY experiments as NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-Ser61.
8329384	0	10	theme	Gal	80:82	arg1	beta					102:105	tetrasaccharide NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta	46:105	the tetrasaccharide NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-linked to serine 61 of human factor IX	42:166	Identification and structural analysis of the tetrasaccharide NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-linked to serine 61 of human factor IX.
8329384	0	10	theme	Gal	80:82	arg1	1-->3					107:111	1-->3	107:111	1-->3	107:111	Identification and structural analysis of the tetrasaccharide NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-linked to serine 61 of human factor IX.
8329384	1	11	theme	several	310:316	arg1	proteins					343:350	several coagulation/fibrinolytic proteins	310:350	several coagulation/fibrinolytic proteins	310:350	O-Linked fucose has been found attached to Thr/Ser residues within the sequence Cys-X-X-Gly-Gly-Thr/Ser-Cys in the N-terminal EGF domains of several coagulation/fibrinolytic proteins.
8329384	1	12	from	Cys-X-X-Gly-Gly-Thr/Ser-Cys	249:275	arg1	domains					299:305	the N-terminal EGF domains	280:305	the N-terminal EGF domains of several coagulation/fibrinolytic proteins	280:350	O-Linked fucose has been found attached to Thr/Ser residues within the sequence Cys-X-X-Gly-Gly-Thr/Ser-Cys in the N-terminal EGF domains of several coagulation/fibrinolytic proteins.
8329384	1	12	from	Cys-X-X-Gly-Gly-Thr/Ser-Cys	249:275	arg1	proteins					343:350	several coagulation/fibrinolytic proteins	310:350	several coagulation/fibrinolytic proteins	310:350	O-Linked fucose has been found attached to Thr/Ser residues within the sequence Cys-X-X-Gly-Gly-Thr/Ser-Cys in the N-terminal EGF domains of several coagulation/fibrinolytic proteins.
8329384	5	13	theme	factor	1009:1014	arg1	IX					1016:1017	factor IX	1009:1017	factor IX residues 57-65	1009:1032	The involvement of fucose in the carbohydrate-peptide linkage was confirmed by two-dimensional 1H NMR spectroscopic analysis of the glycopeptide containing factor IX residues 57-65.
8329384	5	14	contain	containing	998:1007	arg1	glycopeptide					985:996	the glycopeptide	981:996	the glycopeptide containing factor IX residues 57-65	981:1032	The involvement of fucose in the carbohydrate-peptide linkage was confirmed by two-dimensional 1H NMR spectroscopic analysis of the glycopeptide containing factor IX residues 57-65.
8329384	5	14	contain	containing	998:1007	arg2	IX					1016:1017	factor IX	1009:1017	factor IX residues 57-65	1009:1032	The involvement of fucose in the carbohydrate-peptide linkage was confirmed by two-dimensional 1H NMR spectroscopic analysis of the glycopeptide containing factor IX residues 57-65.
8329384	0	15	theme	1-->4	89:93	arg1	beta					102:105	tetrasaccharide NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta	46:105	the tetrasaccharide NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-linked to serine 61 of human factor IX	42:166	Identification and structural analysis of the tetrasaccharide NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-linked to serine 61 of human factor IX.
8329384	0	15	theme	1-->4	89:93	arg1	1-->3					107:111	1-->3	107:111	1-->3	107:111	Identification and structural analysis of the tetrasaccharide NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-linked to serine 61 of human factor IX.
8329384	1	16	theme	coagulation/fibrinolytic	318:341	arg1	proteins					343:350	several coagulation/fibrinolytic proteins	310:350	several coagulation/fibrinolytic proteins	310:350	O-Linked fucose has been found attached to Thr/Ser residues within the sequence Cys-X-X-Gly-Gly-Thr/Ser-Cys in the N-terminal EGF domains of several coagulation/fibrinolytic proteins.
8329384	0	17	theme	human	152:156	arg1	IX					165:166	human factor IX	152:166	human factor IX	152:166	Identification and structural analysis of the tetrasaccharide NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-linked to serine 61 of human factor IX.
8329384	2	18	contain	containing	446:455	arg1	peptides					437:444	tryptic and thermolytic peptides	413:444	tryptic and thermolytic peptides containing the corresponding site (Ser-61) in the first EGF domain of human factor IX	413:530	Carbohydrate composition and mass spectrometric analyses of tryptic and thermolytic peptides containing the corresponding site (Ser-61) in the first EGF domain of human factor IX indicated the presence of a tetrasaccharide containing one residue each of sialic acid, galactose, N-acetylglucosamine, and fucose.
8329384	2	18	contain	containing	446:455	arg2	Ser-61					481:486	Ser-61	481:486	Ser-61	481:486	Carbohydrate composition and mass spectrometric analyses of tryptic and thermolytic peptides containing the corresponding site (Ser-61) in the first EGF domain of human factor IX indicated the presence of a tetrasaccharide containing one residue each of sialic acid, galactose, N-acetylglucosamine, and fucose.
8329384	2	18	contain	containing	446:455	arg2	site					475:478	the corresponding site	457:478	the corresponding site (Ser-61)	457:487	Carbohydrate composition and mass spectrometric analyses of tryptic and thermolytic peptides containing the corresponding site (Ser-61) in the first EGF domain of human factor IX indicated the presence of a tetrasaccharide containing one residue each of sialic acid, galactose, N-acetylglucosamine, and fucose.
8329384	6	19	theme	1-->4	1199:1203	arg1	1-->3					1217:1221	1-->3	1217:1221	1-->3	1217:1221	The complete structure of the tetrasaccharide was obtained by methylation analysis and two-dimensional 1H TOCSY and ROESY experiments as NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-Ser61.
8329384	6	19	theme	1-->4	1199:1203	arg1	beta					1212:1215	NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta	1172:1215	NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-Ser61	1172:1243	The complete structure of the tetrasaccharide was obtained by methylation analysis and two-dimensional 1H TOCSY and ROESY experiments as NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-Ser61.
8329384	2	20	theme	mass	382:385	arg1	analyses					401:408	mass spectrometric analyses	382:408	mass spectrometric analyses	382:408	Carbohydrate composition and mass spectrometric analyses of tryptic and thermolytic peptides containing the corresponding site (Ser-61) in the first EGF domain of human factor IX indicated the presence of a tetrasaccharide containing one residue each of sialic acid, galactose, N-acetylglucosamine, and fucose.
8329384	2	21	theme	first	496:500	arg1	IX					529:530	human factor IX	516:530	human factor IX	516:530	Carbohydrate composition and mass spectrometric analyses of tryptic and thermolytic peptides containing the corresponding site (Ser-61) in the first EGF domain of human factor IX indicated the presence of a tetrasaccharide containing one residue each of sialic acid, galactose, N-acetylglucosamine, and fucose.
8329384	2	21	theme	first	496:500	arg1	domain					506:511	the first EGF domain	492:511	the first EGF domain of human factor IX	492:530	Carbohydrate composition and mass spectrometric analyses of tryptic and thermolytic peptides containing the corresponding site (Ser-61) in the first EGF domain of human factor IX indicated the presence of a tetrasaccharide containing one residue each of sialic acid, galactose, N-acetylglucosamine, and fucose.
8329384	1	22	theme	proteins	343:350	arg1	domains					299:305	the N-terminal EGF domains	280:305	the N-terminal EGF domains of several coagulation/fibrinolytic proteins	280:350	O-Linked fucose has been found attached to Thr/Ser residues within the sequence Cys-X-X-Gly-Gly-Thr/Ser-Cys in the N-terminal EGF domains of several coagulation/fibrinolytic proteins.
8329384	1	22	theme	proteins	343:350	arg1	proteins					343:350	several coagulation/fibrinolytic proteins	310:350	several coagulation/fibrinolytic proteins	310:350	O-Linked fucose has been found attached to Thr/Ser residues within the sequence Cys-X-X-Gly-Gly-Thr/Ser-Cys in the N-terminal EGF domains of several coagulation/fibrinolytic proteins.
8329384	2	23	theme	sialic	607:612	arg1	acid					614:617	sialic acid	607:617	sialic acid	607:617	Carbohydrate composition and mass spectrometric analyses of tryptic and thermolytic peptides containing the corresponding site (Ser-61) in the first EGF domain of human factor IX indicated the presence of a tetrasaccharide containing one residue each of sialic acid, galactose, N-acetylglucosamine, and fucose.
8329384	4	24	theme	spectrometric	774:786	arg1	analysis					788:795	mass spectrometric analysis	769:795	mass spectrometric analysis	769:795	Fragments generated during mass spectrometric analysis indicated that fucose was the attachment sugar residue.
8329384	2	25	theme	EGF	502:504	arg1	IX					529:530	human factor IX	516:530	human factor IX	516:530	Carbohydrate composition and mass spectrometric analyses of tryptic and thermolytic peptides containing the corresponding site (Ser-61) in the first EGF domain of human factor IX indicated the presence of a tetrasaccharide containing one residue each of sialic acid, galactose, N-acetylglucosamine, and fucose.
8329384	2	25	theme	EGF	502:504	arg1	domain					506:511	the first EGF domain	492:511	the first EGF domain of human factor IX	492:530	Carbohydrate composition and mass spectrometric analyses of tryptic and thermolytic peptides containing the corresponding site (Ser-61) in the first EGF domain of human factor IX indicated the presence of a tetrasaccharide containing one residue each of sialic acid, galactose, N-acetylglucosamine, and fucose.
8329384	0	26	theme	IX	165:166	arg1	serine					139:144	serine 61	139:147	serine 61 of human factor IX	139:166	Identification and structural analysis of the tetrasaccharide NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-linked to serine 61 of human factor IX.
8329384	6	27	theme	beta	1194:1197	arg1	1-->3					1217:1221	1-->3	1217:1221	1-->3	1217:1221	The complete structure of the tetrasaccharide was obtained by methylation analysis and two-dimensional 1H TOCSY and ROESY experiments as NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-Ser61.
8329384	6	27	theme	beta	1194:1197	arg1	beta					1212:1215	NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta	1172:1215	NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-Ser61	1172:1243	The complete structure of the tetrasaccharide was obtained by methylation analysis and two-dimensional 1H TOCSY and ROESY experiments as NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-Ser61.
8329384	3	28	theme	alpha-fucosidase	714:729	arg1	digestion					731:739	alpha-fucosidase digestion	714:739	alpha-fucosidase digestion	714:739	The Ser-61 tetrasaccharide was not susceptible to alpha-fucosidase digestion.
8329384	2	29	theme	peptides	437:444	arg1	analyses					401:408	mass spectrometric analyses	382:408	mass spectrometric analyses	382:408	Carbohydrate composition and mass spectrometric analyses of tryptic and thermolytic peptides containing the corresponding site (Ser-61) in the first EGF domain of human factor IX indicated the presence of a tetrasaccharide containing one residue each of sialic acid, galactose, N-acetylglucosamine, and fucose.
8329384	2	29	theme	peptides	437:444	arg1	composition					366:376	Carbohydrate composition	353:376	Carbohydrate composition	353:376	Carbohydrate composition and mass spectrometric analyses of tryptic and thermolytic peptides containing the corresponding site (Ser-61) in the first EGF domain of human factor IX indicated the presence of a tetrasaccharide containing one residue each of sialic acid, galactose, N-acetylglucosamine, and fucose.
8329384	1	30	theme	Thr/Ser	212:218	arg1	residues					220:227	Thr/Ser residues	212:227	Thr/Ser residues within the sequence Cys-X-X-Gly-Gly-Thr/Ser-Cys in the N-terminal EGF domains of several coagulation/fibrinolytic proteins	212:350	O-Linked fucose has been found attached to Thr/Ser residues within the sequence Cys-X-X-Gly-Gly-Thr/Ser-Cys in the N-terminal EGF domains of several coagulation/fibrinolytic proteins.
8329384	0	31	theme	factor	158:163	arg1	IX					165:166	human factor IX	152:166	human factor IX	152:166	Identification and structural analysis of the tetrasaccharide NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-linked to serine 61 of human factor IX.
8329384	6	32	theme	Gal	1190:1192	arg1	1-->3					1217:1221	1-->3	1217:1221	1-->3	1217:1221	The complete structure of the tetrasaccharide was obtained by methylation analysis and two-dimensional 1H TOCSY and ROESY experiments as NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-Ser61.
8329384	6	32	theme	Gal	1190:1192	arg1	beta					1212:1215	NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta	1172:1215	NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-Ser61	1172:1243	The complete structure of the tetrasaccharide was obtained by methylation analysis and two-dimensional 1H TOCSY and ROESY experiments as NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-Ser61.
8329384	2	33	theme	Carbohydrate	353:364	arg1	composition					366:376	Carbohydrate composition	353:376	Carbohydrate composition	353:376	Carbohydrate composition and mass spectrometric analyses of tryptic and thermolytic peptides containing the corresponding site (Ser-61) in the first EGF domain of human factor IX indicated the presence of a tetrasaccharide containing one residue each of sialic acid, galactose, N-acetylglucosamine, and fucose.
8329384	2	34	theme	thermolytic	425:435	arg1	peptides					437:444	tryptic and thermolytic peptides	413:444	tryptic and thermolytic peptides containing the corresponding site (Ser-61) in the first EGF domain of human factor IX	413:530	Carbohydrate composition and mass spectrometric analyses of tryptic and thermolytic peptides containing the corresponding site (Ser-61) in the first EGF domain of human factor IX indicated the presence of a tetrasaccharide containing one residue each of sialic acid, galactose, N-acetylglucosamine, and fucose.
8329384	6	35	theme	two-dimensional	1122:1136	arg1	TOCSY					1141:1145	two-dimensional 1H TOCSY and ROESY experiments	1122:1167	TOCSY	1141:1145	The complete structure of the tetrasaccharide was obtained by methylation analysis and two-dimensional 1H TOCSY and ROESY experiments as NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-Ser61.
8329384	0	36	theme	GlcNAc	95:100	arg1	beta					102:105	tetrasaccharide NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta	46:105	the tetrasaccharide NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-linked to serine 61 of human factor IX	42:166	Identification and structural analysis of the tetrasaccharide NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-linked to serine 61 of human factor IX.
8329384	0	36	theme	GlcNAc	95:100	arg1	1-->3					107:111	1-->3	107:111	1-->3	107:111	Identification and structural analysis of the tetrasaccharide NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-linked to serine 61 of human factor IX.
8329384	6	37	theme	Fuc	1223:1225	arg1	1-->O-Ser61					1233:1243	NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-Ser61	1172:1243	NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-Ser61	1172:1243	The complete structure of the tetrasaccharide was obtained by methylation analysis and two-dimensional 1H TOCSY and ROESY experiments as NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-Ser61.
8329384	6	37	theme	Fuc	1223:1225	arg1	structure					1048:1056	The complete structure	1035:1056	The complete structure of the tetrasaccharide	1035:1079	The complete structure of the tetrasaccharide was obtained by methylation analysis and two-dimensional 1H TOCSY and ROESY experiments as NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-Ser61.
8329384	2	38	theme	tryptic	413:419	arg1	peptides					437:444	tryptic and thermolytic peptides	413:444	tryptic and thermolytic peptides containing the corresponding site (Ser-61) in the first EGF domain of human factor IX	413:530	Carbohydrate composition and mass spectrometric analyses of tryptic and thermolytic peptides containing the corresponding site (Ser-61) in the first EGF domain of human factor IX indicated the presence of a tetrasaccharide containing one residue each of sialic acid, galactose, N-acetylglucosamine, and fucose.
8329384	0	39	theme	structural	19:28	arg1	analysis					30:37	structural analysis	19:37	structural analysis	19:37	Identification and structural analysis of the tetrasaccharide NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-linked to serine 61 of human factor IX.
8329384	2	40	theme	IX	529:530	arg1	IX					529:530	human factor IX	516:530	human factor IX	516:530	Carbohydrate composition and mass spectrometric analyses of tryptic and thermolytic peptides containing the corresponding site (Ser-61) in the first EGF domain of human factor IX indicated the presence of a tetrasaccharide containing one residue each of sialic acid, galactose, N-acetylglucosamine, and fucose.
8329384	2	40	theme	IX	529:530	arg1	domain					506:511	the first EGF domain	492:511	the first EGF domain of human factor IX	492:530	Carbohydrate composition and mass spectrometric analyses of tryptic and thermolytic peptides containing the corresponding site (Ser-61) in the first EGF domain of human factor IX indicated the presence of a tetrasaccharide containing one residue each of sialic acid, galactose, N-acetylglucosamine, and fucose.
8329384	6	41	theme	GlcNAc	1205:1210	arg1	1-->3					1217:1221	1-->3	1217:1221	1-->3	1217:1221	The complete structure of the tetrasaccharide was obtained by methylation analysis and two-dimensional 1H TOCSY and ROESY experiments as NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-Ser61.
8329384	6	41	theme	GlcNAc	1205:1210	arg1	beta					1212:1215	NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta	1172:1215	NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-Ser61	1172:1243	The complete structure of the tetrasaccharide was obtained by methylation analysis and two-dimensional 1H TOCSY and ROESY experiments as NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-Ser61.
8329384	5	42	theme	glycopeptide	985:996	arg1	analysis					969:976	two-dimensional 1H NMR spectroscopic analysis	932:976	two-dimensional 1H NMR spectroscopic analysis of the glycopeptide containing factor IX residues 57-65	932:1032	The involvement of fucose in the carbohydrate-peptide linkage was confirmed by two-dimensional 1H NMR spectroscopic analysis of the glycopeptide containing factor IX residues 57-65.
8329384	2	43	theme	corresponding	461:473	arg1	Ser-61					481:486	Ser-61	481:486	Ser-61	481:486	Carbohydrate composition and mass spectrometric analyses of tryptic and thermolytic peptides containing the corresponding site (Ser-61) in the first EGF domain of human factor IX indicated the presence of a tetrasaccharide containing one residue each of sialic acid, galactose, N-acetylglucosamine, and fucose.
8329384	2	43	theme	corresponding	461:473	arg1	site					475:478	the corresponding site	457:478	the corresponding site (Ser-61)	457:487	Carbohydrate composition and mass spectrometric analyses of tryptic and thermolytic peptides containing the corresponding site (Ser-61) in the first EGF domain of human factor IX indicated the presence of a tetrasaccharide containing one residue each of sialic acid, galactose, N-acetylglucosamine, and fucose.
8329384	6	44	theme	alpha	1178:1182	arg1	1-->3					1217:1221	1-->3	1217:1221	1-->3	1217:1221	The complete structure of the tetrasaccharide was obtained by methylation analysis and two-dimensional 1H TOCSY and ROESY experiments as NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-Ser61.
8329384	6	44	theme	alpha	1178:1182	arg1	beta					1212:1215	NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta	1172:1215	NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-Ser61	1172:1243	The complete structure of the tetrasaccharide was obtained by methylation analysis and two-dimensional 1H TOCSY and ROESY experiments as NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-Ser61.
8329384	2	45	theme	factor	522:527	arg1	IX					529:530	human factor IX	516:530	human factor IX	516:530	Carbohydrate composition and mass spectrometric analyses of tryptic and thermolytic peptides containing the corresponding site (Ser-61) in the first EGF domain of human factor IX indicated the presence of a tetrasaccharide containing one residue each of sialic acid, galactose, N-acetylglucosamine, and fucose.
8329384	4	46	theme	attachment	827:836	arg1	fucose					812:817	fucose	812:817	fucose	812:817	Fragments generated during mass spectrometric analysis indicated that fucose was the attachment sugar residue.
8329384	4	46	theme	attachment	827:836	arg1	residue					844:850	the attachment sugar residue	823:850	the attachment sugar residue	823:850	Fragments generated during mass spectrometric analysis indicated that fucose was the attachment sugar residue.
8329384	5	47	theme	carbohydrate-peptide	886:905	arg1	linkage					907:913	the carbohydrate-peptide linkage	882:913	the carbohydrate-peptide linkage	882:913	The involvement of fucose in the carbohydrate-peptide linkage was confirmed by two-dimensional 1H NMR spectroscopic analysis of the glycopeptide containing factor IX residues 57-65.
8329384	5	48	theme	fucose	872:877	arg1	involvement					857:867	The involvement	853:867	The involvement of fucose in the carbohydrate-peptide linkage	853:913	The involvement of fucose in the carbohydrate-peptide linkage was confirmed by two-dimensional 1H NMR spectroscopic analysis of the glycopeptide containing factor IX residues 57-65.
8329384	1	49	theme	sequence	240:247	arg1	Cys-X-X-Gly-Gly-Thr/Ser-Cys					249:275	the sequence Cys-X-X-Gly-Gly-Thr/Ser-Cys	236:275	the sequence Cys-X-X-Gly-Gly-Thr/Ser-Cys in the N-terminal EGF domains of several coagulation/fibrinolytic proteins	236:350	O-Linked fucose has been found attached to Thr/Ser residues within the sequence Cys-X-X-Gly-Gly-Thr/Ser-Cys in the N-terminal EGF domains of several coagulation/fibrinolytic proteins.
8329384	0	50	theme	beta	102:105	arg1	alpha					117:121	the tetrasaccharide NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha	42:121	the tetrasaccharide NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-linked to serine 61 of human factor IX	42:166	Identification and structural analysis of the tetrasaccharide NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-linked to serine 61 of human factor IX.
8329384	6	51	theme	1H	1138:1139	arg1	TOCSY					1141:1145	two-dimensional 1H TOCSY and ROESY experiments	1122:1167	TOCSY	1141:1145	The complete structure of the tetrasaccharide was obtained by methylation analysis and two-dimensional 1H TOCSY and ROESY experiments as NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-Ser61.
8329384	2	52	theme	human	516:520	arg1	IX					529:530	human factor IX	516:530	human factor IX	516:530	Carbohydrate composition and mass spectrometric analyses of tryptic and thermolytic peptides containing the corresponding site (Ser-61) in the first EGF domain of human factor IX indicated the presence of a tetrasaccharide containing one residue each of sialic acid, galactose, N-acetylglucosamine, and fucose.
8329384	2	53	theme	spectrometric	387:399	arg1	analyses					401:408	mass spectrometric analyses	382:408	mass spectrometric analyses	382:408	Carbohydrate composition and mass spectrometric analyses of tryptic and thermolytic peptides containing the corresponding site (Ser-61) in the first EGF domain of human factor IX indicated the presence of a tetrasaccharide containing one residue each of sialic acid, galactose, N-acetylglucosamine, and fucose.
8329384	0	54	theme	NeuAc	62:66	arg1	beta					102:105	tetrasaccharide NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta	46:105	the tetrasaccharide NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-linked to serine 61 of human factor IX	42:166	Identification and structural analysis of the tetrasaccharide NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-linked to serine 61 of human factor IX.
8329384	0	54	theme	NeuAc	62:66	arg1	1-->3					107:111	1-->3	107:111	1-->3	107:111	Identification and structural analysis of the tetrasaccharide NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-linked to serine 61 of human factor IX.
8329384	6	55	theme	alpha	1227:1231	arg1	1-->O-Ser61					1233:1243	NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-Ser61	1172:1243	NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-Ser61	1172:1243	The complete structure of the tetrasaccharide was obtained by methylation analysis and two-dimensional 1H TOCSY and ROESY experiments as NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-Ser61.
8329384	6	55	theme	alpha	1227:1231	arg1	structure					1048:1056	The complete structure	1035:1056	The complete structure of the tetrasaccharide	1035:1079	The complete structure of the tetrasaccharide was obtained by methylation analysis and two-dimensional 1H TOCSY and ROESY experiments as NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-Ser61.
8329384	6	56	theme	NeuAc	1172:1176	arg1	1-->3					1217:1221	1-->3	1217:1221	1-->3	1217:1221	The complete structure of the tetrasaccharide was obtained by methylation analysis and two-dimensional 1H TOCSY and ROESY experiments as NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-Ser61.
8329384	6	56	theme	NeuAc	1172:1176	arg1	beta					1212:1215	NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta	1172:1215	NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-Ser61	1172:1243	The complete structure of the tetrasaccharide was obtained by methylation analysis and two-dimensional 1H TOCSY and ROESY experiments as NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-Ser61.
8329384	5	57	theme	two-dimensional	932:946	arg1	NMR					951:953	two-dimensional 1H NMR	932:953	two-dimensional 1H NMR spectroscopic analysis of the glycopeptide containing factor IX residues 57-65	932:1032	The involvement of fucose in the carbohydrate-peptide linkage was confirmed by two-dimensional 1H NMR spectroscopic analysis of the glycopeptide containing factor IX residues 57-65.
8329384	0	58	theme	tetrasaccharide	46:60	arg1	beta					102:105	tetrasaccharide NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta	46:105	the tetrasaccharide NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-linked to serine 61 of human factor IX	42:166	Identification and structural analysis of the tetrasaccharide NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-linked to serine 61 of human factor IX.
8329384	0	58	theme	tetrasaccharide	46:60	arg1	1-->3					107:111	1-->3	107:111	1-->3	107:111	Identification and structural analysis of the tetrasaccharide NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-linked to serine 61 of human factor IX.
8329384	4	59	theme	sugar	838:842	arg1	fucose					812:817	fucose	812:817	fucose	812:817	Fragments generated during mass spectrometric analysis indicated that fucose was the attachment sugar residue.
8329384	4	59	theme	sugar	838:842	arg1	residue					844:850	the attachment sugar residue	823:850	the attachment sugar residue	823:850	Fragments generated during mass spectrometric analysis indicated that fucose was the attachment sugar residue.
8329384	2	60	dep	residue	591:597	arg1	N-acetylglucosamine					631:649	N-acetylglucosamine	631:649	N-acetylglucosamine	631:649	Carbohydrate composition and mass spectrometric analyses of tryptic and thermolytic peptides containing the corresponding site (Ser-61) in the first EGF domain of human factor IX indicated the presence of a tetrasaccharide containing one residue each of sialic acid, galactose, N-acetylglucosamine, and fucose.
8329384	2	60	dep	residue	591:597	arg1	fucose					656:661	fucose	656:661	fucose	656:661	Carbohydrate composition and mass spectrometric analyses of tryptic and thermolytic peptides containing the corresponding site (Ser-61) in the first EGF domain of human factor IX indicated the presence of a tetrasaccharide containing one residue each of sialic acid, galactose, N-acetylglucosamine, and fucose.
8329384	2	60	dep	residue	591:597	arg1	galactose					620:628	galactose	620:628	galactose	620:628	Carbohydrate composition and mass spectrometric analyses of tryptic and thermolytic peptides containing the corresponding site (Ser-61) in the first EGF domain of human factor IX indicated the presence of a tetrasaccharide containing one residue each of sialic acid, galactose, N-acetylglucosamine, and fucose.
8329384	2	60	dep	residue	591:597	arg1	each					599:602	each	599:602	each	599:602	Carbohydrate composition and mass spectrometric analyses of tryptic and thermolytic peptides containing the corresponding site (Ser-61) in the first EGF domain of human factor IX indicated the presence of a tetrasaccharide containing one residue each of sialic acid, galactose, N-acetylglucosamine, and fucose.
8329384	2	60	dep	residue	591:597	arg1	acid					614:617	sialic acid	607:617	sialic acid	607:617	Carbohydrate composition and mass spectrometric analyses of tryptic and thermolytic peptides containing the corresponding site (Ser-61) in the first EGF domain of human factor IX indicated the presence of a tetrasaccharide containing one residue each of sialic acid, galactose, N-acetylglucosamine, and fucose.
8329384	5	61	theme	1H	948:949	arg1	NMR					951:953	two-dimensional 1H NMR	932:953	two-dimensional 1H NMR spectroscopic analysis of the glycopeptide containing factor IX residues 57-65	932:1032	The involvement of fucose in the carbohydrate-peptide linkage was confirmed by two-dimensional 1H NMR spectroscopic analysis of the glycopeptide containing factor IX residues 57-65.
8329384	6	62	theme	beta	1212:1215	arg1	1-->O-Ser61					1233:1243	NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-Ser61	1172:1243	NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-Ser61	1172:1243	The complete structure of the tetrasaccharide was obtained by methylation analysis and two-dimensional 1H TOCSY and ROESY experiments as NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-Ser61.
8329384	6	62	theme	beta	1212:1215	arg1	structure					1048:1056	The complete structure	1035:1056	The complete structure of the tetrasaccharide	1035:1079	The complete structure of the tetrasaccharide was obtained by methylation analysis and two-dimensional 1H TOCSY and ROESY experiments as NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-Ser61.
8329384	0	63	theme	alpha	117:121	arg1	Identification					0:13	Identification	0:13	Identification	0:13	Identification and structural analysis of the tetrasaccharide NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-linked to serine 61 of human factor IX.
8329384	0	63	theme	alpha	117:121	arg1	analysis					30:37	structural analysis	19:37	structural analysis	19:37	Identification and structural analysis of the tetrasaccharide NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-linked to serine 61 of human factor IX.
8329384	5	64	theme	NMR	951:953	arg1	analysis					969:976	two-dimensional 1H NMR spectroscopic analysis	932:976	two-dimensional 1H NMR spectroscopic analysis of the glycopeptide containing factor IX residues 57-65	932:1032	The involvement of fucose in the carbohydrate-peptide linkage was confirmed by two-dimensional 1H NMR spectroscopic analysis of the glycopeptide containing factor IX residues 57-65.
8329384	2	65	contain	containing	576:585	arg1	tetrasaccharide					560:574	a tetrasaccharide	558:574	a tetrasaccharide containing one residue each of sialic acid, galactose, N-acetylglucosamine, and fucose	558:661	Carbohydrate composition and mass spectrometric analyses of tryptic and thermolytic peptides containing the corresponding site (Ser-61) in the first EGF domain of human factor IX indicated the presence of a tetrasaccharide containing one residue each of sialic acid, galactose, N-acetylglucosamine, and fucose.
8329384	2	65	contain	containing	576:585	arg2	residue					591:597	one residue	587:597	one residue each of sialic acid, galactose, N-acetylglucosamine, and fucose	587:661	Carbohydrate composition and mass spectrometric analyses of tryptic and thermolytic peptides containing the corresponding site (Ser-61) in the first EGF domain of human factor IX indicated the presence of a tetrasaccharide containing one residue each of sialic acid, galactose, N-acetylglucosamine, and fucose.
8329384	6	66	theme	tetrasaccharide	1065:1079	arg1	1-->O-Ser61					1233:1243	NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-Ser61	1172:1243	NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-Ser61	1172:1243	The complete structure of the tetrasaccharide was obtained by methylation analysis and two-dimensional 1H TOCSY and ROESY experiments as NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-Ser61.
8329384	6	66	theme	tetrasaccharide	1065:1079	arg1	structure					1048:1056	The complete structure	1035:1056	The complete structure of the tetrasaccharide	1035:1079	The complete structure of the tetrasaccharide was obtained by methylation analysis and two-dimensional 1H TOCSY and ROESY experiments as NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-Ser61.
8329384	0	67	theme	Fuc	113:115	arg1	alpha					117:121	the tetrasaccharide NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha	42:121	the tetrasaccharide NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-linked to serine 61 of human factor IX	42:166	Identification and structural analysis of the tetrasaccharide NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-linked to serine 61 of human factor IX.
8329384	5	68	from	involvement	857:867	arg1	linkage					907:913	the carbohydrate-peptide linkage	882:913	the carbohydrate-peptide linkage	882:913	The involvement of fucose in the carbohydrate-peptide linkage was confirmed by two-dimensional 1H NMR spectroscopic analysis of the glycopeptide containing factor IX residues 57-65.
8329384	5	69	theme	spectroscopic	955:967	arg1	analysis					969:976	two-dimensional 1H NMR spectroscopic analysis	932:976	two-dimensional 1H NMR spectroscopic analysis of the glycopeptide containing factor IX residues 57-65	932:1032	The involvement of fucose in the carbohydrate-peptide linkage was confirmed by two-dimensional 1H NMR spectroscopic analysis of the glycopeptide containing factor IX residues 57-65.
8329384	1	70	theme	O-Linked	169:176	arg1	fucose					178:183	O-Linked fucose	169:183	O-Linked fucose	169:183	O-Linked fucose has been found attached to Thr/Ser residues within the sequence Cys-X-X-Gly-Gly-Thr/Ser-Cys in the N-terminal EGF domains of several coagulation/fibrinolytic proteins.
8329384	5	71	gly	glycopeptide	985:996	arg2	glycopeptide					985:996	the glycopeptide	981:996	the glycopeptide containing factor IX residues 57-65	981:1032	The involvement of fucose in the carbohydrate-peptide linkage was confirmed by two-dimensional 1H NMR spectroscopic analysis of the glycopeptide containing factor IX residues 57-65.
8329384	1	72	dep	found	194:198	arg1	attached					200:207	attached	200:207	attached to Thr/Ser residues within the sequence Cys-X-X-Gly-Gly-Thr/Ser-Cys in the N-terminal EGF domains of several coagulation/fibrinolytic proteins	200:350	O-Linked fucose has been found attached to Thr/Ser residues within the sequence Cys-X-X-Gly-Gly-Thr/Ser-Cys in the N-terminal EGF domains of several coagulation/fibrinolytic proteins.
8329384	6	73	theme	methylation	1097:1107	arg1	analysis					1109:1116	methylation analysis	1097:1116	methylation analysis	1097:1116	The complete structure of the tetrasaccharide was obtained by methylation analysis and two-dimensional 1H TOCSY and ROESY experiments as NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-Ser61.
8329384	0	74	link	1-->O-linked	123:134	arg1	alpha					117:121	the tetrasaccharide NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha	42:121	the tetrasaccharide NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-linked to serine 61 of human factor IX	42:166	Identification and structural analysis of the tetrasaccharide NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-linked to serine 61 of human factor IX.
8329384	0	75	theme	alpha	68:72	arg1	beta					102:105	tetrasaccharide NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta	46:105	the tetrasaccharide NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-linked to serine 61 of human factor IX	42:166	Identification and structural analysis of the tetrasaccharide NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-linked to serine 61 of human factor IX.
8329384	0	75	theme	alpha	68:72	arg1	1-->3					107:111	1-->3	107:111	1-->3	107:111	Identification and structural analysis of the tetrasaccharide NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-linked to serine 61 of human factor IX.
8329384	1	76	theme	N-terminal	284:293	arg1	domains					299:305	the N-terminal EGF domains	280:305	the N-terminal EGF domains of several coagulation/fibrinolytic proteins	280:350	O-Linked fucose has been found attached to Thr/Ser residues within the sequence Cys-X-X-Gly-Gly-Thr/Ser-Cys in the N-terminal EGF domains of several coagulation/fibrinolytic proteins.
8329384	1	76	theme	N-terminal	284:293	arg1	proteins					343:350	several coagulation/fibrinolytic proteins	310:350	several coagulation/fibrinolytic proteins	310:350	O-Linked fucose has been found attached to Thr/Ser residues within the sequence Cys-X-X-Gly-Gly-Thr/Ser-Cys in the N-terminal EGF domains of several coagulation/fibrinolytic proteins.
8329384	1	77	attach	attached	200:207	arg1	residues					220:227	Thr/Ser residues	212:227	Thr/Ser residues within the sequence Cys-X-X-Gly-Gly-Thr/Ser-Cys in the N-terminal EGF domains of several coagulation/fibrinolytic proteins	212:350	O-Linked fucose has been found attached to Thr/Ser residues within the sequence Cys-X-X-Gly-Gly-Thr/Ser-Cys in the N-terminal EGF domains of several coagulation/fibrinolytic proteins.
8329384	1	77	attach	attached	200:207	arg2	fucose					178:183	O-Linked fucose	169:183	O-Linked fucose	169:183	O-Linked fucose has been found attached to Thr/Ser residues within the sequence Cys-X-X-Gly-Gly-Thr/Ser-Cys in the N-terminal EGF domains of several coagulation/fibrinolytic proteins.
8329384	6	78	theme	ROESY	1151:1155	arg1	experiments					1157:1167	two-dimensional 1H TOCSY and ROESY experiments	1122:1167	experiments	1157:1167	The complete structure of the tetrasaccharide was obtained by methylation analysis and two-dimensional 1H TOCSY and ROESY experiments as NeuAc alpha(2-->6)Gal beta(1-->4)GlcNAc beta(1-->3)Fuc alpha 1-->O-Ser61.
3356193	0	0	theme	porcine	61:67	arg1	N-					4:5	N-	4:5	N-	4:5	The N- and O-linked carbohydrate chains of human, bovine and porcine plasminogen.
3356193	4	1	theme	plasminogen	475:485	arg1	N-glycan					457:464	the N-glycan	453:464	the N-glycan of human plasminogen	453:485	In the N-glycan of human plasminogen the two antennae are sialylated with N-acetylneuraminic acid (NeuAc), whereas in the bovine counterpart both branches carry significant amounts of N-glycolylneuraminic acid (NeuGc).
3356193	5	2	theme	alpha	733:737	arg1	branch					746:751	the Man alpha 1----6 branch	725:751	the Man alpha 1----6 branch	725:751	In porcine plasminogen the sialic acid is mainly NeuAc; the Man alpha 1----6 branch, however, is only partially sialylated.
3356193	7	3	theme	1----3GalNAc	969:980	arg1	core					982:985	an identical Gal beta 1----3GalNAc core	947:985	an identical Gal beta 1----3GalNAc core which is alpha 2----3 sialylated with NeuAc at Gal	947:1036	The O-glycans of the three species possess an identical Gal beta 1----3GalNAc core which is alpha 2----3 sialylated with NeuAc at Gal.
3356193	7	3	theme	1----3GalNAc	969:980	arg1	2----3					1002:1007	alpha 2----3	996:1007	alpha 2----3 sialylated with NeuAc at Gal	996:1036	The O-glycans of the three species possess an identical Gal beta 1----3GalNAc core which is alpha 2----3 sialylated with NeuAc at Gal.
3356193	5	4	theme	1----6	739:744	arg1	branch					746:751	the Man alpha 1----6 branch	725:751	the Man alpha 1----6 branch	725:751	In porcine plasminogen the sialic acid is mainly NeuAc; the Man alpha 1----6 branch, however, is only partially sialylated.
3356193	4	5	dep	sialylated	508:517	arg1	whereas					557:563	whereas	557:563	whereas	557:563	In the N-glycan of human plasminogen the two antennae are sialylated with N-acetylneuraminic acid (NeuAc), whereas in the bovine counterpart both branches carry significant amounts of N-glycolylneuraminic acid (NeuGc).
3356193	10	6	theme	plasminogens	1372:1383	arg1	moiety					1350:1355	the carbohydrate moiety	1333:1355	the carbohydrate moiety of these three plasminogens	1333:1383	This study on the carbohydrate moiety of these three plasminogens reveals species specificity in terms of various types of microheterogeneities.
3356193	10	7	from	specificity	1401:1411	arg1	terms					1416:1420	terms	1416:1420	terms of various types of microheterogeneities	1416:1461	This study on the carbohydrate moiety of these three plasminogens reveals species specificity in terms of various types of microheterogeneities.
3356193	8	8	from	species	1097:1103	arg1	present					1076:1082	present	1076:1082	present	1076:1082	The disialylated form, which is also present in all three species, has an additional NeuAc residue in alpha 2----6 linkage to GalNAc.
3356193	8	8	from	species	1097:1103	arg1	form					1056:1059	The disialylated form	1039:1059	The disialylated form	1039:1059	The disialylated form, which is also present in all three species, has an additional NeuAc residue in alpha 2----6 linkage to GalNAc.
3356193	9	9	from	80:20	1265:1269	arg1	human					1274:1278	human	1274:1278	human	1274:1278	Mono- and disialylated forms occur in different molar ratios in the different plasminogens: 80:20 in human, 70:30 in bovine and 50:50 in porcine.
3356193	4	10	theme	acid	655:658	arg1	amounts					623:629	significant amounts	611:629	significant amounts of N-glycolylneuraminic acid (NeuGc)	611:666	In the N-glycan of human plasminogen the two antennae are sialylated with N-acetylneuraminic acid (NeuAc), whereas in the bovine counterpart both branches carry significant amounts of N-glycolylneuraminic acid (NeuGc).
3356193	4	10	theme	acid	655:658	arg1	acid					655:658	N-glycolylneuraminic acid	634:658	N-glycolylneuraminic acid (NeuGc)	634:666	In the N-glycan of human plasminogen the two antennae are sialylated with N-acetylneuraminic acid (NeuAc), whereas in the bovine counterpart both branches carry significant amounts of N-glycolylneuraminic acid (NeuGc).
3356193	4	10	theme	acid	655:658	arg1	NeuGc					661:665	NeuGc	661:665	NeuGc	661:665	In the N-glycan of human plasminogen the two antennae are sialylated with N-acetylneuraminic acid (NeuAc), whereas in the bovine counterpart both branches carry significant amounts of N-glycolylneuraminic acid (NeuGc).
3356193	7	11	contain	possess	939:945	arg2	2----3					1002:1007	alpha 2----3	996:1007	alpha 2----3 sialylated with NeuAc at Gal	996:1036	The O-glycans of the three species possess an identical Gal beta 1----3GalNAc core which is alpha 2----3 sialylated with NeuAc at Gal.
3356193	7	11	contain	possess	939:945	arg2	core					982:985	an identical Gal beta 1----3GalNAc core	947:985	an identical Gal beta 1----3GalNAc core which is alpha 2----3 sialylated with NeuAc at Gal	947:1036	The O-glycans of the three species possess an identical Gal beta 1----3GalNAc core which is alpha 2----3 sialylated with NeuAc at Gal.
3356193	7	11	contain	possess	939:945	arg1	O-glycans					908:916	The O-glycans	904:916	The O-glycans of the three species	904:937	The O-glycans of the three species possess an identical Gal beta 1----3GalNAc core which is alpha 2----3 sialylated with NeuAc at Gal.
3356193	9	12	theme	different	1211:1219	arg1	ratios					1227:1232	different molar ratios	1211:1232	different molar ratios in the different plasminogens: 80:20 in human, 70:30 in bovine and 50:50 in porcine	1211:1316	Mono- and disialylated forms occur in different molar ratios in the different plasminogens: 80:20 in human, 70:30 in bovine and 50:50 in porcine.
3356193	1	13	dep	sialylation	117:127	arg1	patterns					146:153	patterns	146:153	patterns	146:153	Species specificity in relation to sialylation and fucosylation patterns.
3356193	2	14	theme	1H-NMR	263:268	arg1	spectroscopy					270:281	500-MHz 1H-NMR spectroscopy	255:281	500-MHz 1H-NMR spectroscopy	255:281	The structures of the N- and O-glycans of human, bovine and porcine plasminogen were determined by 500-MHz 1H-NMR spectroscopy.
3356193	8	15	from	residue	1130:1136	arg1	linkage					1154:1160	alpha 2----6 linkage	1141:1160	alpha 2----6 linkage	1141:1160	The disialylated form, which is also present in all three species, has an additional NeuAc residue in alpha 2----6 linkage to GalNAc.
3356193	3	16	dep	one	379:381	arg1	another					383:389	another	383:389	another	383:389	The N-glycans of all three species proved to be of the N-acetyllactosamine type differing from one another with respect to the sialylation and fucosylation patterns.
3356193	2	17	theme	500-MHz	255:261	arg1	spectroscopy					270:281	500-MHz 1H-NMR spectroscopy	255:281	500-MHz 1H-NMR spectroscopy	255:281	The structures of the N- and O-glycans of human, bovine and porcine plasminogen were determined by 500-MHz 1H-NMR spectroscopy.
3356193	9	18	dep	plasminogens	1251:1262	arg1	70:30					1281:1285	70:30	1281:1285	70:30	1281:1285	Mono- and disialylated forms occur in different molar ratios in the different plasminogens: 80:20 in human, 70:30 in bovine and 50:50 in porcine.
3356193	9	18	dep	plasminogens	1251:1262	arg1	80:20					1265:1269	80:20	1265:1269	80:20	1265:1269	Mono- and disialylated forms occur in different molar ratios in the different plasminogens: 80:20 in human, 70:30 in bovine and 50:50 in porcine.
3356193	9	18	dep	plasminogens	1251:1262	arg1	50:50					1301:1305	50:50	1301:1305	50:50	1301:1305	Mono- and disialylated forms occur in different molar ratios in the different plasminogens: 80:20 in human, 70:30 in bovine and 50:50 in porcine.
3356193	3	19	theme	sialylation	411:421	arg1	patterns					440:447	the sialylation and fucosylation patterns	407:447	the sialylation and fucosylation patterns	407:447	The N-glycans of all three species proved to be of the N-acetyllactosamine type differing from one another with respect to the sialylation and fucosylation patterns.
3356193	8	20	located	present	1076:1082	arg2	form					1056:1059	The disialylated form	1039:1059	The disialylated form	1039:1059	The disialylated form, which is also present in all three species, has an additional NeuAc residue in alpha 2----6 linkage to GalNAc.
3356193	8	20	located	present	1076:1082	arg1	species					1097:1103	all three species	1087:1103	all three species	1087:1103	The disialylated form, which is also present in all three species, has an additional NeuAc residue in alpha 2----6 linkage to GalNAc.
3356193	8	20	located	present	1076:1082	arg2	present					1076:1082	present	1076:1082	present	1076:1082	The disialylated form, which is also present in all three species, has an additional NeuAc residue in alpha 2----6 linkage to GalNAc.
3356193	4	21	theme	human	469:473	arg1	plasminogen					475:485	human plasminogen	469:485	human plasminogen	469:485	In the N-glycan of human plasminogen the two antennae are sialylated with N-acetylneuraminic acid (NeuAc), whereas in the bovine counterpart both branches carry significant amounts of N-glycolylneuraminic acid (NeuGc).
3356193	4	22	theme	N-glycolylneuraminic	634:653	arg1	acid					655:658	N-glycolylneuraminic acid	634:658	N-glycolylneuraminic acid (NeuGc)	634:666	In the N-glycan of human plasminogen the two antennae are sialylated with N-acetylneuraminic acid (NeuAc), whereas in the bovine counterpart both branches carry significant amounts of N-glycolylneuraminic acid (NeuGc).
3356193	4	22	theme	N-glycolylneuraminic	634:653	arg1	NeuGc					661:665	NeuGc	661:665	NeuGc	661:665	In the N-glycan of human plasminogen the two antennae are sialylated with N-acetylneuraminic acid (NeuAc), whereas in the bovine counterpart both branches carry significant amounts of N-glycolylneuraminic acid (NeuGc).
3356193	9	23	from	ratios	1227:1232	arg1	plasminogens					1251:1262	the different plasminogens	1237:1262	the different plasminogens: 80:20 in human, 70:30 in bovine and 50:50 in porcine	1237:1316	Mono- and disialylated forms occur in different molar ratios in the different plasminogens: 80:20 in human, 70:30 in bovine and 50:50 in porcine.
3356193	10	24	theme	various	1425:1431	arg1	types					1433:1437	various types	1425:1437	various types of microheterogeneities	1425:1461	This study on the carbohydrate moiety of these three plasminogens reveals species specificity in terms of various types of microheterogeneities.
3356193	3	25	theme	species	311:317	arg1	N-glycans					288:296	The N-glycans	284:296	The N-glycans of all three species	284:317	The N-glycans of all three species proved to be of the N-acetyllactosamine type differing from one another with respect to the sialylation and fucosylation patterns.
3356193	8	26	attach	present	1076:1082	arg2	form					1056:1059	The disialylated form	1039:1059	The disialylated form	1039:1059	The disialylated form, which is also present in all three species, has an additional NeuAc residue in alpha 2----6 linkage to GalNAc.
3356193	8	26	attach	present	1076:1082	arg1	species					1097:1103	all three species	1087:1103	all three species	1087:1103	The disialylated form, which is also present in all three species, has an additional NeuAc residue in alpha 2----6 linkage to GalNAc.
3356193	8	26	attach	present	1076:1082	arg2	present					1076:1082	present	1076:1082	present	1076:1082	The disialylated form, which is also present in all three species, has an additional NeuAc residue in alpha 2----6 linkage to GalNAc.
3356193	9	27	theme	molar	1221:1225	arg1	ratios					1227:1232	different molar ratios	1211:1232	different molar ratios in the different plasminogens: 80:20 in human, 70:30 in bovine and 50:50 in porcine	1211:1316	Mono- and disialylated forms occur in different molar ratios in the different plasminogens: 80:20 in human, 70:30 in bovine and 50:50 in porcine.
3356193	9	28	from	50:50	1301:1305	arg1	porcine					1310:1316	porcine	1310:1316	porcine	1310:1316	Mono- and disialylated forms occur in different molar ratios in the different plasminogens: 80:20 in human, 70:30 in bovine and 50:50 in porcine.
3356193	10	29	from	study	1324:1328	arg1	moiety					1350:1355	the carbohydrate moiety	1333:1355	the carbohydrate moiety of these three plasminogens	1333:1383	This study on the carbohydrate moiety of these three plasminogens reveals species specificity in terms of various types of microheterogeneities.
3356193	8	30	theme	2----6	1147:1152	arg1	linkage					1154:1160	alpha 2----6 linkage	1141:1160	alpha 2----6 linkage	1141:1160	The disialylated form, which is also present in all three species, has an additional NeuAc residue in alpha 2----6 linkage to GalNAc.
3356193	8	31	gly	disialylated	1043:1054	arg1	present					1076:1082	present	1076:1082	present	1076:1082	The disialylated form, which is also present in all three species, has an additional NeuAc residue in alpha 2----6 linkage to GalNAc.
3356193	8	31	gly	disialylated	1043:1054	arg1	form					1056:1059	The disialylated form	1039:1059	The disialylated form	1039:1059	The disialylated form, which is also present in all three species, has an additional NeuAc residue in alpha 2----6 linkage to GalNAc.
3356193	3	32	theme	N-acetyllactosamine	339:357	arg1	type					359:362	the N-acetyllactosamine type	335:362	the N-acetyllactosamine type differing from one another with respect to the sialylation and fucosylation patterns	335:447	The N-glycans of all three species proved to be of the N-acetyllactosamine type differing from one another with respect to the sialylation and fucosylation patterns.
3356193	9	33	theme	different	1241:1249	arg1	plasminogens					1251:1262	the different plasminogens	1237:1262	the different plasminogens: 80:20 in human, 70:30 in bovine and 50:50 in porcine	1237:1316	Mono- and disialylated forms occur in different molar ratios in the different plasminogens: 80:20 in human, 70:30 in bovine and 50:50 in porcine.
3356193	10	34	theme	species	1393:1399	arg1	specificity					1401:1411	species specificity	1393:1411	species specificity in terms of various types of microheterogeneities	1393:1461	This study on the carbohydrate moiety of these three plasminogens reveals species specificity in terms of various types of microheterogeneities.
3356193	10	35	theme	carbohydrate	1337:1348	arg1	moiety					1350:1355	the carbohydrate moiety	1333:1355	the carbohydrate moiety of these three plasminogens	1333:1383	This study on the carbohydrate moiety of these three plasminogens reveals species specificity in terms of various types of microheterogeneities.
3356193	4	36	theme	significant	611:621	arg1	amounts					623:629	significant amounts	611:629	significant amounts of N-glycolylneuraminic acid (NeuGc)	611:666	In the N-glycan of human plasminogen the two antennae are sialylated with N-acetylneuraminic acid (NeuAc), whereas in the bovine counterpart both branches carry significant amounts of N-glycolylneuraminic acid (NeuGc).
3356193	4	36	theme	significant	611:621	arg1	acid					655:658	N-glycolylneuraminic acid	634:658	N-glycolylneuraminic acid (NeuGc)	634:666	In the N-glycan of human plasminogen the two antennae are sialylated with N-acetylneuraminic acid (NeuAc), whereas in the bovine counterpart both branches carry significant amounts of N-glycolylneuraminic acid (NeuGc).
3356193	4	36	theme	significant	611:621	arg1	NeuGc					661:665	NeuGc	661:665	NeuGc	661:665	In the N-glycan of human plasminogen the two antennae are sialylated with N-acetylneuraminic acid (NeuAc), whereas in the bovine counterpart both branches carry significant amounts of N-glycolylneuraminic acid (NeuGc).
3356193	7	37	theme	species	931:937	arg1	O-glycans					908:916	The O-glycans	904:916	The O-glycans of the three species	904:937	The O-glycans of the three species possess an identical Gal beta 1----3GalNAc core which is alpha 2----3 sialylated with NeuAc at Gal.
3356193	5	38	from	NeuAc	718:722	arg1	plasminogen					680:690	porcine plasminogen	672:690	porcine plasminogen	672:690	In porcine plasminogen the sialic acid is mainly NeuAc; the Man alpha 1----6 branch, however, is only partially sialylated.
3356193	6	39	theme	alpha	858:862	arg1	linkage					871:877	alpha 1----6 linkage	858:877	alpha 1----6 linkage to the GlcNAc-1 residue	858:901	In addition, the porcine N-glycan is fucosylated to about 80% in alpha 1----6 linkage to the GlcNAc-1 residue.
3356193	2	40	dep	human	198:202	arg1	plasminogen					224:234	plasminogen	224:234	plasminogen	224:234	The structures of the N- and O-glycans of human, bovine and porcine plasminogen were determined by 500-MHz 1H-NMR spectroscopy.
3356193	8	41	theme	NeuAc	1124:1128	arg1	residue					1130:1136	an additional NeuAc residue	1110:1136	an additional NeuAc residue in alpha 2----6 linkage to GalNAc	1110:1170	The disialylated form, which is also present in all three species, has an additional NeuAc residue in alpha 2----6 linkage to GalNAc.
3356193	7	42	from	Gal	1034:1036	arg1	NeuAc					1025:1029	NeuAc	1025:1029	NeuAc at Gal	1025:1036	The O-glycans of the three species possess an identical Gal beta 1----3GalNAc core which is alpha 2----3 sialylated with NeuAc at Gal.
3356193	5	43	theme	sialic	696:701	arg1	NeuAc					718:722	NeuAc	718:722	NeuAc	718:722	In porcine plasminogen the sialic acid is mainly NeuAc; the Man alpha 1----6 branch, however, is only partially sialylated.
3356193	5	43	theme	sialic	696:701	arg1	acid					703:706	the sialic acid	692:706	the sialic acid	692:706	In porcine plasminogen the sialic acid is mainly NeuAc; the Man alpha 1----6 branch, however, is only partially sialylated.
3356193	0	44	dep	human	43:47	arg1	plasminogen					69:79	plasminogen	69:79	plasminogen	69:79	The N- and O-linked carbohydrate chains of human, bovine and porcine plasminogen.
3356193	3	45	theme	fucosylation	427:438	arg1	patterns					440:447	the sialylation and fucosylation patterns	407:447	the sialylation and fucosylation patterns	407:447	The N-glycans of all three species proved to be of the N-acetyllactosamine type differing from one another with respect to the sialylation and fucosylation patterns.
3356193	0	46	theme	carbohydrate	20:31	arg1	chains					33:38	carbohydrate chains	20:38	carbohydrate chains	20:38	The N- and O-linked carbohydrate chains of human, bovine and porcine plasminogen.
3356193	6	47	theme	GlcNAc-1	886:893	arg1	residue					895:901	the GlcNAc-1 residue	882:901	the GlcNAc-1 residue	882:901	In addition, the porcine N-glycan is fucosylated to about 80% in alpha 1----6 linkage to the GlcNAc-1 residue.
3356193	7	48	theme	alpha	996:1000	arg1	core					982:985	an identical Gal beta 1----3GalNAc core	947:985	an identical Gal beta 1----3GalNAc core which is alpha 2----3 sialylated with NeuAc at Gal	947:1036	The O-glycans of the three species possess an identical Gal beta 1----3GalNAc core which is alpha 2----3 sialylated with NeuAc at Gal.
3356193	7	48	theme	alpha	996:1000	arg1	2----3					1002:1007	alpha 2----3	996:1007	alpha 2----3 sialylated with NeuAc at Gal	996:1036	The O-glycans of the three species possess an identical Gal beta 1----3GalNAc core which is alpha 2----3 sialylated with NeuAc at Gal.
3356193	4	49	contain	carry	605:609	arg2	NeuGc					661:665	NeuGc	661:665	NeuGc	661:665	In the N-glycan of human plasminogen the two antennae are sialylated with N-acetylneuraminic acid (NeuAc), whereas in the bovine counterpart both branches carry significant amounts of N-glycolylneuraminic acid (NeuGc).
3356193	4	49	contain	carry	605:609	arg3	counterpart					579:589	the bovine counterpart	568:589	the bovine counterpart	568:589	In the N-glycan of human plasminogen the two antennae are sialylated with N-acetylneuraminic acid (NeuAc), whereas in the bovine counterpart both branches carry significant amounts of N-glycolylneuraminic acid (NeuGc).
3356193	4	49	contain	carry	605:609	arg2	acid					655:658	N-glycolylneuraminic acid	634:658	N-glycolylneuraminic acid (NeuGc)	634:666	In the N-glycan of human plasminogen the two antennae are sialylated with N-acetylneuraminic acid (NeuAc), whereas in the bovine counterpart both branches carry significant amounts of N-glycolylneuraminic acid (NeuGc).
3356193	4	49	contain	carry	605:609	arg2	amounts					623:629	significant amounts	611:629	significant amounts of N-glycolylneuraminic acid (NeuGc)	611:666	In the N-glycan of human plasminogen the two antennae are sialylated with N-acetylneuraminic acid (NeuAc), whereas in the bovine counterpart both branches carry significant amounts of N-glycolylneuraminic acid (NeuGc).
3356193	4	49	contain	carry	605:609	arg1	branches					596:603	both branches	591:603	both branches	591:603	In the N-glycan of human plasminogen the two antennae are sialylated with N-acetylneuraminic acid (NeuAc), whereas in the bovine counterpart both branches carry significant amounts of N-glycolylneuraminic acid (NeuGc).
3356193	2	50	theme	bovine	205:210	arg1	O-glycans					185:193	O-glycans	185:193	O-glycans	185:193	The structures of the N- and O-glycans of human, bovine and porcine plasminogen were determined by 500-MHz 1H-NMR spectroscopy.
3356193	2	50	theme	bovine	205:210	arg1	N-					178:179	N-	178:179	N-	178:179	The structures of the N- and O-glycans of human, bovine and porcine plasminogen were determined by 500-MHz 1H-NMR spectroscopy.
3356193	7	51	theme	identical	950:958	arg1	core					982:985	an identical Gal beta 1----3GalNAc core	947:985	an identical Gal beta 1----3GalNAc core which is alpha 2----3 sialylated with NeuAc at Gal	947:1036	The O-glycans of the three species possess an identical Gal beta 1----3GalNAc core which is alpha 2----3 sialylated with NeuAc at Gal.
3356193	7	51	theme	identical	950:958	arg1	2----3					1002:1007	alpha 2----3	996:1007	alpha 2----3 sialylated with NeuAc at Gal	996:1036	The O-glycans of the three species possess an identical Gal beta 1----3GalNAc core which is alpha 2----3 sialylated with NeuAc at Gal.
3356193	10	52	theme	microheterogeneities	1442:1461	arg1	types					1433:1437	various types	1425:1437	various types of microheterogeneities	1425:1461	This study on the carbohydrate moiety of these three plasminogens reveals species specificity in terms of various types of microheterogeneities.
3356193	0	53	theme	human	43:47	arg1	N-					4:5	N-	4:5	N-	4:5	The N- and O-linked carbohydrate chains of human, bovine and porcine plasminogen.
3356193	8	54	theme	additional	1113:1122	arg1	residue					1130:1136	an additional NeuAc residue	1110:1136	an additional NeuAc residue in alpha 2----6 linkage to GalNAc	1110:1170	The disialylated form, which is also present in all three species, has an additional NeuAc residue in alpha 2----6 linkage to GalNAc.
3356193	6	55	from	%	853:853	arg1	linkage					871:877	alpha 1----6 linkage	858:877	alpha 1----6 linkage to the GlcNAc-1 residue	858:901	In addition, the porcine N-glycan is fucosylated to about 80% in alpha 1----6 linkage to the GlcNAc-1 residue.
3356193	5	56	gly	sialylated	781:790	arg1	branch					746:751	the Man alpha 1----6 branch	725:751	the Man alpha 1----6 branch	725:751	In porcine plasminogen the sialic acid is mainly NeuAc; the Man alpha 1----6 branch, however, is only partially sialylated.
3356193	7	57	theme	Gal	960:962	arg1	core					982:985	an identical Gal beta 1----3GalNAc core	947:985	an identical Gal beta 1----3GalNAc core which is alpha 2----3 sialylated with NeuAc at Gal	947:1036	The O-glycans of the three species possess an identical Gal beta 1----3GalNAc core which is alpha 2----3 sialylated with NeuAc at Gal.
3356193	7	57	theme	Gal	960:962	arg1	2----3					1002:1007	alpha 2----3	996:1007	alpha 2----3 sialylated with NeuAc at Gal	996:1036	The O-glycans of the three species possess an identical Gal beta 1----3GalNAc core which is alpha 2----3 sialylated with NeuAc at Gal.
3356193	4	58	theme	N-acetylneuraminic	524:541	arg1	NeuAc					549:553	NeuAc	549:553	NeuAc	549:553	In the N-glycan of human plasminogen the two antennae are sialylated with N-acetylneuraminic acid (NeuAc), whereas in the bovine counterpart both branches carry significant amounts of N-glycolylneuraminic acid (NeuGc).
3356193	4	58	theme	N-acetylneuraminic	524:541	arg1	acid					543:546	N-acetylneuraminic acid	524:546	N-acetylneuraminic acid (NeuAc)	524:554	In the N-glycan of human plasminogen the two antennae are sialylated with N-acetylneuraminic acid (NeuAc), whereas in the bovine counterpart both branches carry significant amounts of N-glycolylneuraminic acid (NeuGc).
3356193	9	59	theme	disialylated	1183:1194	arg1	forms					1196:1200	Mono- and disialylated forms	1173:1200	Mono- and disialylated forms	1173:1200	Mono- and disialylated forms occur in different molar ratios in the different plasminogens: 80:20 in human, 70:30 in bovine and 50:50 in porcine.
3356193	10	60	theme	types	1433:1437	arg1	terms					1416:1420	terms	1416:1420	terms of various types of microheterogeneities	1416:1461	This study on the carbohydrate moiety of these three plasminogens reveals species specificity in terms of various types of microheterogeneities.
3356193	2	61	theme	human	198:202	arg1	O-glycans					185:193	O-glycans	185:193	O-glycans	185:193	The structures of the N- and O-glycans of human, bovine and porcine plasminogen were determined by 500-MHz 1H-NMR spectroscopy.
3356193	2	61	theme	human	198:202	arg1	N-					178:179	N-	178:179	N-	178:179	The structures of the N- and O-glycans of human, bovine and porcine plasminogen were determined by 500-MHz 1H-NMR spectroscopy.
3356193	6	62	theme	porcine	810:816	arg1	N-glycan					818:825	the porcine N-glycan	806:825	the porcine N-glycan	806:825	In addition, the porcine N-glycan is fucosylated to about 80% in alpha 1----6 linkage to the GlcNAc-1 residue.
3356193	9	63	from	70:30	1281:1285	arg1	bovine					1290:1295	bovine	1290:1295	bovine	1290:1295	Mono- and disialylated forms occur in different molar ratios in the different plasminogens: 80:20 in human, 70:30 in bovine and 50:50 in porcine.
3356193	7	64	theme	beta	964:967	arg1	core					982:985	an identical Gal beta 1----3GalNAc core	947:985	an identical Gal beta 1----3GalNAc core which is alpha 2----3 sialylated with NeuAc at Gal	947:1036	The O-glycans of the three species possess an identical Gal beta 1----3GalNAc core which is alpha 2----3 sialylated with NeuAc at Gal.
3356193	7	64	theme	beta	964:967	arg1	2----3					1002:1007	alpha 2----3	996:1007	alpha 2----3 sialylated with NeuAc at Gal	996:1036	The O-glycans of the three species possess an identical Gal beta 1----3GalNAc core which is alpha 2----3 sialylated with NeuAc at Gal.
3356193	2	65	theme	O-glycans	185:193	arg1	structures					160:169	The structures	156:169	The structures of the N- and O-glycans of human, bovine and porcine plasminogen	156:234	The structures of the N- and O-glycans of human, bovine and porcine plasminogen were determined by 500-MHz 1H-NMR spectroscopy.
3356193	8	66	contain	has	1106:1108	arg2	residue					1130:1136	an additional NeuAc residue	1110:1136	an additional NeuAc residue in alpha 2----6 linkage to GalNAc	1110:1170	The disialylated form, which is also present in all three species, has an additional NeuAc residue in alpha 2----6 linkage to GalNAc.
3356193	8	66	contain	has	1106:1108	arg1	present					1076:1082	present	1076:1082	present	1076:1082	The disialylated form, which is also present in all three species, has an additional NeuAc residue in alpha 2----6 linkage to GalNAc.
3356193	8	66	contain	has	1106:1108	arg1	form					1056:1059	The disialylated form	1039:1059	The disialylated form	1039:1059	The disialylated form, which is also present in all three species, has an additional NeuAc residue in alpha 2----6 linkage to GalNAc.
3356193	8	67	theme	disialylated	1043:1054	arg1	present					1076:1082	present	1076:1082	present	1076:1082	The disialylated form, which is also present in all three species, has an additional NeuAc residue in alpha 2----6 linkage to GalNAc.
3356193	8	67	theme	disialylated	1043:1054	arg1	form					1056:1059	The disialylated form	1039:1059	The disialylated form	1039:1059	The disialylated form, which is also present in all three species, has an additional NeuAc residue in alpha 2----6 linkage to GalNAc.
3356193	1	68	from	specificity	90:100	arg1	relation					105:112	relation	105:112	relation to sialylation and fucosylation patterns	105:153	Species specificity in relation to sialylation and fucosylation patterns.
3356193	5	69	theme	porcine	672:678	arg1	plasminogen					680:690	porcine plasminogen	672:690	porcine plasminogen	672:690	In porcine plasminogen the sialic acid is mainly NeuAc; the Man alpha 1----6 branch, however, is only partially sialylated.
3356193	9	70	theme	Mono-	1173:1177	arg1	forms					1196:1200	Mono- and disialylated forms	1173:1200	Mono- and disialylated forms	1173:1200	Mono- and disialylated forms occur in different molar ratios in the different plasminogens: 80:20 in human, 70:30 in bovine and 50:50 in porcine.
3356193	9	71	gly	disialylated	1183:1194	arg1	forms					1196:1200	Mono- and disialylated forms	1173:1200	Mono- and disialylated forms	1173:1200	Mono- and disialylated forms occur in different molar ratios in the different plasminogens: 80:20 in human, 70:30 in bovine and 50:50 in porcine.
3356193	6	72	gly	fucosylated	830:840	arg1	N-glycan					818:825	the porcine N-glycan	806:825	the porcine N-glycan	806:825	In addition, the porcine N-glycan is fucosylated to about 80% in alpha 1----6 linkage to the GlcNAc-1 residue.
3356193	4	73	theme	bovine	572:577	arg1	counterpart					579:589	the bovine counterpart	568:589	the bovine counterpart	568:589	In the N-glycan of human plasminogen the two antennae are sialylated with N-acetylneuraminic acid (NeuAc), whereas in the bovine counterpart both branches carry significant amounts of N-glycolylneuraminic acid (NeuGc).
3356193	0	74	theme	bovine	50:55	arg1	N-					4:5	N-	4:5	N-	4:5	The N- and O-linked carbohydrate chains of human, bovine and porcine plasminogen.
3356193	2	75	theme	N-	178:179	arg1	structures					160:169	The structures	156:169	The structures of the N- and O-glycans of human, bovine and porcine plasminogen	156:234	The structures of the N- and O-glycans of human, bovine and porcine plasminogen were determined by 500-MHz 1H-NMR spectroscopy.
3356193	0	76	dep	N-	4:5	arg1	chains					33:38	carbohydrate chains	20:38	carbohydrate chains	20:38	The N- and O-linked carbohydrate chains of human, bovine and porcine plasminogen.
3356193	0	76	dep	N-	4:5	arg1	The					0:2	The	0:2	The	0:2	The N- and O-linked carbohydrate chains of human, bovine and porcine plasminogen.
3356193	4	77	gly	sialylated	508:517	arg1	antennae					495:502	the two antennae	487:502	the two antennae	487:502	In the N-glycan of human plasminogen the two antennae are sialylated with N-acetylneuraminic acid (NeuAc), whereas in the bovine counterpart both branches carry significant amounts of N-glycolylneuraminic acid (NeuGc).
3356193	7	78	gly	sialylated	1009:1018	arg1	core					982:985	an identical Gal beta 1----3GalNAc core	947:985	an identical Gal beta 1----3GalNAc core which is alpha 2----3 sialylated with NeuAc at Gal	947:1036	The O-glycans of the three species possess an identical Gal beta 1----3GalNAc core which is alpha 2----3 sialylated with NeuAc at Gal.
3356193	7	78	gly	sialylated	1009:1018	arg1	2----3					1002:1007	alpha 2----3	996:1007	alpha 2----3 sialylated with NeuAc at Gal	996:1036	The O-glycans of the three species possess an identical Gal beta 1----3GalNAc core which is alpha 2----3 sialylated with NeuAc at Gal.
3356193	8	79	theme	alpha	1141:1145	arg1	linkage					1154:1160	alpha 2----6 linkage	1141:1160	alpha 2----6 linkage	1141:1160	The disialylated form, which is also present in all three species, has an additional NeuAc residue in alpha 2----6 linkage to GalNAc.
3356193	5	80	theme	Man	729:731	arg1	branch					746:751	the Man alpha 1----6 branch	725:751	the Man alpha 1----6 branch	725:751	In porcine plasminogen the sialic acid is mainly NeuAc; the Man alpha 1----6 branch, however, is only partially sialylated.
3356193	6	81	theme	1----6	864:869	arg1	linkage					871:877	alpha 1----6 linkage	858:877	alpha 1----6 linkage to the GlcNAc-1 residue	858:901	In addition, the porcine N-glycan is fucosylated to about 80% in alpha 1----6 linkage to the GlcNAc-1 residue.
3356193	2	82	theme	porcine	216:222	arg1	O-glycans					185:193	O-glycans	185:193	O-glycans	185:193	The structures of the N- and O-glycans of human, bovine and porcine plasminogen were determined by 500-MHz 1H-NMR spectroscopy.
3356193	2	82	theme	porcine	216:222	arg1	N-					178:179	N-	178:179	N-	178:179	The structures of the N- and O-glycans of human, bovine and porcine plasminogen were determined by 500-MHz 1H-NMR spectroscopy.
3356193	8	83	from	present	1076:1082	arg1	species					1097:1103	all three species	1087:1103	all three species	1087:1103	The disialylated form, which is also present in all three species, has an additional NeuAc residue in alpha 2----6 linkage to GalNAc.
2049076	14	0	theme	human	2263:2267	arg1	protein					2279:2285	the only O-glycosylated human IFN-alpha protein	2239:2285	the only O-glycosylated human IFN-alpha protein	2239:2285	As IFN-alpha 2 is the only IFN-alpha species with a threonine residue at position 106, it may represent the only O-glycosylated human IFN-alpha protein.
2049076	3	1	theme	IFN-alpha	492:500	arg1	2a					502:503	IFN-alpha 2a	492:503	IFN-alpha 2a	492:503	N-Terminal amino-acid-sequence analysis identified the subspecies IFN-alpha 2b and/or IFN-alpha 2c, whereas IFN-alpha 2a was not detectable.
2049076	7	2	theme	peptides	1106:1113	arg1	analysis					1082:1089	sequence analysis	1073:1089	sequence analysis of proteolytic peptides	1073:1113	On sequence analysis of proteolytic peptides, Thr-106 was found to be modified.
2049076	7	3	located	found	1128:1132	arg1	analysis					1082:1089	sequence analysis	1073:1089	sequence analysis of proteolytic peptides	1073:1113	On sequence analysis of proteolytic peptides, Thr-106 was found to be modified.
2049076	7	3	located	found	1128:1132	arg2	Thr-106					1116:1122	Thr-106	1116:1122	Thr-106	1116:1122	On sequence analysis of proteolytic peptides, Thr-106 was found to be modified.
2049076	12	4	theme	protein	2066:2072	arg1	proportion					2048:2057	another proportion	2040:2057	another proportion of the protein	2040:2072	In part of the molecules, this core carbohydrate carries (alpha-)N-acetylneuraminic acid, whereas a disaccharide, probably N-acetyl-lactosamine, is bound to Gal-GalNAc in another proportion of the protein.
2049076	6	5	theme	recombinant	870:880	arg1	IFN-alpha					882:890	recombinant IFN-alpha 2	870:892	recombinant IFN-alpha 2	870:892	Secondly, the apparent molecular mass of the natural protein determined by SDS/PAGE was higher than that of recombinant IFN-alpha 2; incubation under mild alkaline conditions known to eliminate O-linked carbohydrates resulted in a reduction of the apparent molecular mass to that of the recombinant protein.
2049076	2	6	theme	total	341:345	arg1	activity					357:364	the total antiviral activity	337:364	the total antiviral activity of leucocyte IFN	337:381	The purified protein had a specific activity of 1.5 x 10(8) i.u./mg; it was estimated to constitute 10-20% of the total antiviral activity of leucocyte IFN.
2049076	12	7	dep	carries	1918:1924	arg1	whereas					1959:1965	whereas	1959:1965	whereas	1959:1965	In part of the molecules, this core carbohydrate carries (alpha-)N-acetylneuraminic acid, whereas a disaccharide, probably N-acetyl-lactosamine, is bound to Gal-GalNAc in another proportion of the protein.
2049076	6	8	theme	apparent	776:783	arg1	mass					795:798	the apparent molecular mass	772:798	the apparent molecular mass of the natural protein determined by SDS/PAGE	772:844	Secondly, the apparent molecular mass of the natural protein determined by SDS/PAGE was higher than that of recombinant IFN-alpha 2; incubation under mild alkaline conditions known to eliminate O-linked carbohydrates resulted in a reduction of the apparent molecular mass to that of the recombinant protein.
2049076	6	8	theme	apparent	776:783	arg1	higher					850:855	higher	850:855	higher	850:855	Secondly, the apparent molecular mass of the natural protein determined by SDS/PAGE was higher than that of recombinant IFN-alpha 2; incubation under mild alkaline conditions known to eliminate O-linked carbohydrates resulted in a reduction of the apparent molecular mass to that of the recombinant protein.
2049076	1	9	theme	leucocyte	159:167	arg1	IFN					169:171	partially purified human leucocyte IFN	134:171	partially purified human leucocyte IFN	134:171	Natural human interferon alpha 2 (IFN-alpha 2) was isolated from a preparation of partially purified human leucocyte IFN by monoclonal-antibody immunoaffinity chromatography.
2049076	11	10	contain	contains	1778:1785	arg2	galactosyl-N-acetylgalactosamine					1804:1835	the disaccharide galactosyl-N-acetylgalactosamine	1787:1835	the disaccharide galactosyl-N-acetylgalactosamine (Gal-GalNAc) linked to Thr-106	1787:1866	The results indicate that natural IFN-alpha 2 contains the disaccharide galactosyl-N-acetylgalactosamine (Gal-GalNAc) linked to Thr-106.
2049076	11	10	contain	contains	1778:1785	arg2	Gal-GalNAc					1838:1847	Gal-GalNAc	1838:1847	Gal-GalNAc	1838:1847	The results indicate that natural IFN-alpha 2 contains the disaccharide galactosyl-N-acetylgalactosamine (Gal-GalNAc) linked to Thr-106.
2049076	11	10	contain	contains	1778:1785	arg1	IFN-alpha					1766:1774	natural IFN-alpha 2	1758:1776	natural IFN-alpha 2	1758:1776	The results indicate that natural IFN-alpha 2 contains the disaccharide galactosyl-N-acetylgalactosamine (Gal-GalNAc) linked to Thr-106.
2049076	10	11	theme	m.s.	1632:1635	arg1	information					1645:1655	m.s. Further information	1632:1655	m.s. Further information on the composition of the glycans	1632:1689	For characterization of the carbohydrate moieties, the protein was treated with neuraminidase and/or O-glycanase and analysed by gel electrophoresis; in addition, glycopeptides obtained by proteinase digestion and separated by h.p.l.c. were characterized by sequence analysis and m.s. Further information on the composition of the glycans was obtained by monosaccharide analysis.
2049076	7	12	theme	sequence	1073:1080	arg1	analysis					1082:1089	sequence analysis	1073:1089	sequence analysis of proteolytic peptides	1073:1113	On sequence analysis of proteolytic peptides, Thr-106 was found to be modified.
2049076	2	13	theme	i.u./mg	287:293	arg1	activity					263:270	a specific activity	252:270	a specific activity of 1.5 x 10(8) i.u./mg	252:293	The purified protein had a specific activity of 1.5 x 10(8) i.u./mg; it was estimated to constitute 10-20% of the total antiviral activity of leucocyte IFN.
2049076	13	14	located	present	2109:2115	arg2	isomers					2097:2103	Further glycosylation isomers	2075:2103	Further glycosylation isomers	2075:2103	Further glycosylation isomers are present in small amounts.
2049076	13	14	located	present	2109:2115	arg1	amounts					2126:2132	small amounts	2120:2132	small amounts	2120:2132	Further glycosylation isomers are present in small amounts.
2049076	6	15	theme	O-linked	956:963	arg1	carbohydrates					965:977	O-linked carbohydrates	956:977	O-linked carbohydrates	956:977	Secondly, the apparent molecular mass of the natural protein determined by SDS/PAGE was higher than that of recombinant IFN-alpha 2; incubation under mild alkaline conditions known to eliminate O-linked carbohydrates resulted in a reduction of the apparent molecular mass to that of the recombinant protein.
2049076	10	16	gly	glycopeptides	1515:1527	arg2	glycopeptides					1515:1527	glycopeptides	1515:1527	glycopeptides obtained by proteinase digestion and separated by h.p.l.c.	1515:1586	For characterization of the carbohydrate moieties, the protein was treated with neuraminidase and/or O-glycanase and analysed by gel electrophoresis; in addition, glycopeptides obtained by proteinase digestion and separated by h.p.l.c. were characterized by sequence analysis and m.s. Further information on the composition of the glycans was obtained by monosaccharide analysis.
2049076	4	17	theme	recombinant	599:609	arg1	equivalent					638:647	its recombinant (Escherichia coli-derived) equivalent	595:647	its recombinant (Escherichia coli-derived) equivalent	595:647	The structure of natural IFN-alpha 2 was found to differ from that of its recombinant (Escherichia coli-derived) equivalent.
2049076	13	18	from	present	2109:2115	arg1	amounts					2126:2132	small amounts	2120:2132	small amounts	2120:2132	Further glycosylation isomers are present in small amounts.
2049076	1	19	theme	immunoaffinity	196:209	arg1	chromatography					211:224	monoclonal-antibody immunoaffinity chromatography	176:224	monoclonal-antibody immunoaffinity chromatography	176:224	Natural human interferon alpha 2 (IFN-alpha 2) was isolated from a preparation of partially purified human leucocyte IFN by monoclonal-antibody immunoaffinity chromatography.
2049076	8	20	theme	IFN-alpha	1198:1206	arg1	Thr-106					1179:1185	Thr-106	1179:1185	Thr-106	1179:1185	These results suggested that Thr-106 of natural IFN-alpha 2 carries O-linked carbohydrates.
2049076	8	20	theme	IFN-alpha	1198:1206	arg1	IFN-alpha					1198:1206	natural IFN-alpha 2	1190:1208	natural IFN-alpha 2	1190:1208	These results suggested that Thr-106 of natural IFN-alpha 2 carries O-linked carbohydrates.
2049076	5	21	dep	hydrophilic	735:745	arg1	expected					752:759	expected	752:759	expected	752:759	First, reverse-phase h.p.l.c. showed that natural IFN-alpha 2 was significantly more hydrophilic then expected.
2049076	8	22	contain	carries	1210:1216	arg1	Thr-106					1179:1185	Thr-106	1179:1185	Thr-106	1179:1185	These results suggested that Thr-106 of natural IFN-alpha 2 carries O-linked carbohydrates.
2049076	8	22	contain	carries	1210:1216	arg1	IFN-alpha					1198:1206	natural IFN-alpha 2	1190:1208	natural IFN-alpha 2	1190:1208	These results suggested that Thr-106 of natural IFN-alpha 2 carries O-linked carbohydrates.
2049076	8	22	contain	carries	1210:1216	arg2	carbohydrates					1227:1239	O-linked carbohydrates	1218:1239	O-linked carbohydrates	1218:1239	These results suggested that Thr-106 of natural IFN-alpha 2 carries O-linked carbohydrates.
2049076	11	23	attach	linked	1850:1855	arg2	Gal-GalNAc					1838:1847	Gal-GalNAc	1838:1847	Gal-GalNAc	1838:1847	The results indicate that natural IFN-alpha 2 contains the disaccharide galactosyl-N-acetylgalactosamine (Gal-GalNAc) linked to Thr-106.
2049076	11	23	attach	linked	1850:1855	arg2	galactosyl-N-acetylgalactosamine					1804:1835	the disaccharide galactosyl-N-acetylgalactosamine	1787:1835	the disaccharide galactosyl-N-acetylgalactosamine (Gal-GalNAc) linked to Thr-106	1787:1866	The results indicate that natural IFN-alpha 2 contains the disaccharide galactosyl-N-acetylgalactosamine (Gal-GalNAc) linked to Thr-106.
2049076	11	23	attach	linked	1850:1855	arg1	Thr-106					1860:1866	Thr-106	1860:1866	Thr-106	1860:1866	The results indicate that natural IFN-alpha 2 contains the disaccharide galactosyl-N-acetylgalactosamine (Gal-GalNAc) linked to Thr-106.
2049076	14	24	theme	O-glycosylated	2248:2261	arg1	protein					2279:2285	the only O-glycosylated human IFN-alpha protein	2239:2285	the only O-glycosylated human IFN-alpha protein	2239:2285	As IFN-alpha 2 is the only IFN-alpha species with a threonine residue at position 106, it may represent the only O-glycosylated human IFN-alpha protein.
2049076	14	25	theme	threonine	2187:2195	arg1	residue					2197:2203	a threonine residue	2185:2203	a threonine residue at position 106	2185:2219	As IFN-alpha 2 is the only IFN-alpha species with a threonine residue at position 106, it may represent the only O-glycosylated human IFN-alpha protein.
2049076	6	26	link	O-linked	956:963	arg1	carbohydrates					965:977	O-linked carbohydrates	956:977	O-linked carbohydrates	956:977	Secondly, the apparent molecular mass of the natural protein determined by SDS/PAGE was higher than that of recombinant IFN-alpha 2; incubation under mild alkaline conditions known to eliminate O-linked carbohydrates resulted in a reduction of the apparent molecular mass to that of the recombinant protein.
2049076	6	27	theme	mild	912:915	arg1	conditions					926:935	mild alkaline conditions	912:935	mild alkaline conditions known to eliminate O-linked carbohydrates	912:977	Secondly, the apparent molecular mass of the natural protein determined by SDS/PAGE was higher than that of recombinant IFN-alpha 2; incubation under mild alkaline conditions known to eliminate O-linked carbohydrates resulted in a reduction of the apparent molecular mass to that of the recombinant protein.
2049076	14	28	from	position	2208:2215	arg1	residue					2197:2203	a threonine residue	2185:2203	a threonine residue at position 106	2185:2219	As IFN-alpha 2 is the only IFN-alpha species with a threonine residue at position 106, it may represent the only O-glycosylated human IFN-alpha protein.
2049076	11	29	theme	disaccharide	1791:1802	arg1	Gal-GalNAc					1838:1847	Gal-GalNAc	1838:1847	Gal-GalNAc	1838:1847	The results indicate that natural IFN-alpha 2 contains the disaccharide galactosyl-N-acetylgalactosamine (Gal-GalNAc) linked to Thr-106.
2049076	11	29	theme	disaccharide	1791:1802	arg1	galactosyl-N-acetylgalactosamine					1804:1835	the disaccharide galactosyl-N-acetylgalactosamine	1787:1835	the disaccharide galactosyl-N-acetylgalactosamine (Gal-GalNAc) linked to Thr-106	1787:1866	The results indicate that natural IFN-alpha 2 contains the disaccharide galactosyl-N-acetylgalactosamine (Gal-GalNAc) linked to Thr-106.
2049076	6	30	theme	apparent	1010:1017	arg1	mass					1029:1032	the apparent molecular mass	1006:1032	the apparent molecular mass to that of the recombinant protein	1006:1067	Secondly, the apparent molecular mass of the natural protein determined by SDS/PAGE was higher than that of recombinant IFN-alpha 2; incubation under mild alkaline conditions known to eliminate O-linked carbohydrates resulted in a reduction of the apparent molecular mass to that of the recombinant protein.
2049076	9	31	theme	natural	1288:1294	arg1	IFN-alpha					1296:1304	natural IFN-alpha 2	1288:1306	natural IFN-alpha 2	1288:1306	Reverse-phase h.p.l.c. as well as SDS/PAGE of natural IFN-alpha 2 showed that glycosylation is heterogeneous.
2049076	1	32	theme	purified	144:151	arg1	IFN					169:171	partially purified human leucocyte IFN	134:171	partially purified human leucocyte IFN	134:171	Natural human interferon alpha 2 (IFN-alpha 2) was isolated from a preparation of partially purified human leucocyte IFN by monoclonal-antibody immunoaffinity chromatography.
2049076	1	33	theme	interferon	66:75	arg1	alpha					77:81	Natural human interferon alpha 2	52:83	Natural human interferon alpha 2 (IFN-alpha 2)	52:97	Natural human interferon alpha 2 (IFN-alpha 2) was isolated from a preparation of partially purified human leucocyte IFN by monoclonal-antibody immunoaffinity chromatography.
2049076	1	33	theme	interferon	66:75	arg1	IFN-alpha					86:94	IFN-alpha 2	86:96	IFN-alpha 2	86:96	Natural human interferon alpha 2 (IFN-alpha 2) was isolated from a preparation of partially purified human leucocyte IFN by monoclonal-antibody immunoaffinity chromatography.
2049076	14	34	theme	only	2157:2160	arg1	species					2172:2178	the only IFN-alpha species	2153:2178	the only IFN-alpha species with a threonine residue at position 106	2153:2219	As IFN-alpha 2 is the only IFN-alpha species with a threonine residue at position 106, it may represent the only O-glycosylated human IFN-alpha protein.
2049076	14	34	theme	only	2157:2160	arg1	IFN-alpha					2138:2146	IFN-alpha 2	2138:2148	IFN-alpha 2	2138:2148	As IFN-alpha 2 is the only IFN-alpha species with a threonine residue at position 106, it may represent the only O-glycosylated human IFN-alpha protein.
2049076	10	35	theme	monosaccharide	1707:1720	arg1	analysis					1722:1729	monosaccharide analysis	1707:1729	monosaccharide analysis	1707:1729	For characterization of the carbohydrate moieties, the protein was treated with neuraminidase and/or O-glycanase and analysed by gel electrophoresis; in addition, glycopeptides obtained by proteinase digestion and separated by h.p.l.c. were characterized by sequence analysis and m.s. Further information on the composition of the glycans was obtained by monosaccharide analysis.
2049076	2	36	theme	activity	357:364	arg1	activity					357:364	the total antiviral activity	337:364	the total antiviral activity of leucocyte IFN	337:381	The purified protein had a specific activity of 1.5 x 10(8) i.u./mg; it was estimated to constitute 10-20% of the total antiviral activity of leucocyte IFN.
2049076	2	36	theme	activity	357:364	arg1	%					332:332	10-20%	327:332	10-20% of the total antiviral activity of leucocyte IFN	327:381	The purified protein had a specific activity of 1.5 x 10(8) i.u./mg; it was estimated to constitute 10-20% of the total antiviral activity of leucocyte IFN.
2049076	12	37	theme	N-acetylneuraminic	1934:1951	arg1	acid					1953:1956	(alpha-)N-acetylneuraminic acid	1926:1956	(alpha-)N-acetylneuraminic acid	1926:1956	In part of the molecules, this core carbohydrate carries (alpha-)N-acetylneuraminic acid, whereas a disaccharide, probably N-acetyl-lactosamine, is bound to Gal-GalNAc in another proportion of the protein.
2049076	10	38	theme	gel	1481:1483	arg1	electrophoresis					1485:1499	gel electrophoresis	1481:1499	gel electrophoresis	1481:1499	For characterization of the carbohydrate moieties, the protein was treated with neuraminidase and/or O-glycanase and analysed by gel electrophoresis; in addition, glycopeptides obtained by proteinase digestion and separated by h.p.l.c. were characterized by sequence analysis and m.s. Further information on the composition of the glycans was obtained by monosaccharide analysis.
2049076	10	39	from	information	1645:1655	arg1	composition					1664:1674	the composition	1660:1674	the composition of the glycans	1660:1689	For characterization of the carbohydrate moieties, the protein was treated with neuraminidase and/or O-glycanase and analysed by gel electrophoresis; in addition, glycopeptides obtained by proteinase digestion and separated by h.p.l.c. were characterized by sequence analysis and m.s. Further information on the composition of the glycans was obtained by monosaccharide analysis.
2049076	3	40	theme	N-Terminal	384:393	arg1	analysis					415:422	N-Terminal amino-acid-sequence analysis	384:422	N-Terminal amino-acid-sequence analysis	384:422	N-Terminal amino-acid-sequence analysis identified the subspecies IFN-alpha 2b and/or IFN-alpha 2c, whereas IFN-alpha 2a was not detectable.
2049076	0	41	theme	Natural	0:6	arg1	interferon-alpha					14:29	Natural human interferon-alpha 2	0:31	Natural human interferon-alpha 2	0:31	Natural human interferon-alpha 2 is O-glycosylated.
2049076	10	42	theme	moieties	1393:1400	arg1	characterization					1356:1371	characterization	1356:1371	characterization of the carbohydrate moieties	1356:1400	For characterization of the carbohydrate moieties, the protein was treated with neuraminidase and/or O-glycanase and analysed by gel electrophoresis; in addition, glycopeptides obtained by proteinase digestion and separated by h.p.l.c. were characterized by sequence analysis and m.s. Further information on the composition of the glycans was obtained by monosaccharide analysis.
2049076	3	43	theme	IFN-alpha	450:458	arg1	2b					460:461	IFN-alpha 2b	450:461	IFN-alpha 2b	450:461	N-Terminal amino-acid-sequence analysis identified the subspecies IFN-alpha 2b and/or IFN-alpha 2c, whereas IFN-alpha 2a was not detectable.
2049076	4	44	theme	natural	542:548	arg1	IFN-alpha					550:558	natural IFN-alpha 2	542:560	natural IFN-alpha 2	542:560	The structure of natural IFN-alpha 2 was found to differ from that of its recombinant (Escherichia coli-derived) equivalent.
2049076	2	45	theme	leucocyte	369:377	arg1	IFN					379:381	leucocyte IFN	369:381	leucocyte IFN	369:381	The purified protein had a specific activity of 1.5 x 10(8) i.u./mg; it was estimated to constitute 10-20% of the total antiviral activity of leucocyte IFN.
2049076	12	46	theme	alpha-	1927:1932	arg1	acid					1953:1956	(alpha-)N-acetylneuraminic acid	1926:1956	(alpha-)N-acetylneuraminic acid	1926:1956	In part of the molecules, this core carbohydrate carries (alpha-)N-acetylneuraminic acid, whereas a disaccharide, probably N-acetyl-lactosamine, is bound to Gal-GalNAc in another proportion of the protein.
2049076	12	47	from	Gal-GalNAc	2026:2035	arg1	proportion					2048:2057	another proportion	2040:2057	another proportion of the protein	2040:2072	In part of the molecules, this core carbohydrate carries (alpha-)N-acetylneuraminic acid, whereas a disaccharide, probably N-acetyl-lactosamine, is bound to Gal-GalNAc in another proportion of the protein.
2049076	6	48	theme	mass	1029:1032	arg1	reduction					993:1001	a reduction	991:1001	a reduction of the apparent molecular mass to that of the recombinant protein	991:1067	Secondly, the apparent molecular mass of the natural protein determined by SDS/PAGE was higher than that of recombinant IFN-alpha 2; incubation under mild alkaline conditions known to eliminate O-linked carbohydrates resulted in a reduction of the apparent molecular mass to that of the recombinant protein.
2049076	13	49	theme	Further	2075:2081	arg1	isomers					2097:2103	Further glycosylation isomers	2075:2103	Further glycosylation isomers	2075:2103	Further glycosylation isomers are present in small amounts.
2049076	12	50	theme	molecules	1884:1892	arg1	part					1872:1875	part	1872:1875	part of the molecules	1872:1892	In part of the molecules, this core carbohydrate carries (alpha-)N-acetylneuraminic acid, whereas a disaccharide, probably N-acetyl-lactosamine, is bound to Gal-GalNAc in another proportion of the protein.
2049076	14	51	gly	O-glycosylated	2248:2261	arg1	protein					2279:2285	the only O-glycosylated human IFN-alpha protein	2239:2285	the only O-glycosylated human IFN-alpha protein	2239:2285	As IFN-alpha 2 is the only IFN-alpha species with a threonine residue at position 106, it may represent the only O-glycosylated human IFN-alpha protein.
2049076	12	52	theme	core	1900:1903	arg1	carbohydrate					1905:1916	this core carbohydrate	1895:1916	this core carbohydrate	1895:1916	In part of the molecules, this core carbohydrate carries (alpha-)N-acetylneuraminic acid, whereas a disaccharide, probably N-acetyl-lactosamine, is bound to Gal-GalNAc in another proportion of the protein.
2049076	6	53	theme	protein	815:821	arg1	mass					795:798	the apparent molecular mass	772:798	the apparent molecular mass of the natural protein determined by SDS/PAGE	772:844	Secondly, the apparent molecular mass of the natural protein determined by SDS/PAGE was higher than that of recombinant IFN-alpha 2; incubation under mild alkaline conditions known to eliminate O-linked carbohydrates resulted in a reduction of the apparent molecular mass to that of the recombinant protein.
2049076	6	53	theme	protein	815:821	arg1	higher					850:855	higher	850:855	higher	850:855	Secondly, the apparent molecular mass of the natural protein determined by SDS/PAGE was higher than that of recombinant IFN-alpha 2; incubation under mild alkaline conditions known to eliminate O-linked carbohydrates resulted in a reduction of the apparent molecular mass to that of the recombinant protein.
2049076	3	54	dep	subspecies	439:448	arg1	2c					480:481	IFN-alpha 2c	470:481	IFN-alpha 2c	470:481	N-Terminal amino-acid-sequence analysis identified the subspecies IFN-alpha 2b and/or IFN-alpha 2c, whereas IFN-alpha 2a was not detectable.
2049076	3	54	dep	subspecies	439:448	arg1	2b					460:461	IFN-alpha 2b	450:461	IFN-alpha 2b	450:461	N-Terminal amino-acid-sequence analysis identified the subspecies IFN-alpha 2b and/or IFN-alpha 2c, whereas IFN-alpha 2a was not detectable.
2049076	11	55	theme	natural	1758:1764	arg1	IFN-alpha					1766:1774	natural IFN-alpha 2	1758:1776	natural IFN-alpha 2	1758:1776	The results indicate that natural IFN-alpha 2 contains the disaccharide galactosyl-N-acetylgalactosamine (Gal-GalNAc) linked to Thr-106.
2049076	4	56	dep	coli-derived	624:635	arg1	Escherichia					612:622	Escherichia coli-derived	612:635	Escherichia coli-derived	612:635	The structure of natural IFN-alpha 2 was found to differ from that of its recombinant (Escherichia coli-derived) equivalent.
2049076	14	57	theme	IFN-alpha	2269:2277	arg1	protein					2279:2285	the only O-glycosylated human IFN-alpha protein	2239:2285	the only O-glycosylated human IFN-alpha protein	2239:2285	As IFN-alpha 2 is the only IFN-alpha species with a threonine residue at position 106, it may represent the only O-glycosylated human IFN-alpha protein.
2049076	12	58	contain	carries	1918:1924	arg1	carbohydrate					1905:1916	this core carbohydrate	1895:1916	this core carbohydrate	1895:1916	In part of the molecules, this core carbohydrate carries (alpha-)N-acetylneuraminic acid, whereas a disaccharide, probably N-acetyl-lactosamine, is bound to Gal-GalNAc in another proportion of the protein.
2049076	12	58	contain	carries	1918:1924	arg3	part					1872:1875	part	1872:1875	part of the molecules	1872:1892	In part of the molecules, this core carbohydrate carries (alpha-)N-acetylneuraminic acid, whereas a disaccharide, probably N-acetyl-lactosamine, is bound to Gal-GalNAc in another proportion of the protein.
2049076	12	58	contain	carries	1918:1924	arg2	acid					1953:1956	(alpha-)N-acetylneuraminic acid	1926:1956	(alpha-)N-acetylneuraminic acid	1926:1956	In part of the molecules, this core carbohydrate carries (alpha-)N-acetylneuraminic acid, whereas a disaccharide, probably N-acetyl-lactosamine, is bound to Gal-GalNAc in another proportion of the protein.
2049076	10	59	theme	sequence	1610:1617	arg1	analysis					1619:1626	sequence analysis	1610:1626	sequence analysis	1610:1626	For characterization of the carbohydrate moieties, the protein was treated with neuraminidase and/or O-glycanase and analysed by gel electrophoresis; in addition, glycopeptides obtained by proteinase digestion and separated by h.p.l.c. were characterized by sequence analysis and m.s. Further information on the composition of the glycans was obtained by monosaccharide analysis.
2049076	7	60	theme	proteolytic	1094:1104	arg1	peptides					1106:1113	proteolytic peptides	1094:1113	proteolytic peptides	1094:1113	On sequence analysis of proteolytic peptides, Thr-106 was found to be modified.
2049076	6	61	theme	molecular	785:793	arg1	mass					795:798	the apparent molecular mass	772:798	the apparent molecular mass of the natural protein determined by SDS/PAGE	772:844	Secondly, the apparent molecular mass of the natural protein determined by SDS/PAGE was higher than that of recombinant IFN-alpha 2; incubation under mild alkaline conditions known to eliminate O-linked carbohydrates resulted in a reduction of the apparent molecular mass to that of the recombinant protein.
2049076	6	61	theme	molecular	785:793	arg1	higher					850:855	higher	850:855	higher	850:855	Secondly, the apparent molecular mass of the natural protein determined by SDS/PAGE was higher than that of recombinant IFN-alpha 2; incubation under mild alkaline conditions known to eliminate O-linked carbohydrates resulted in a reduction of the apparent molecular mass to that of the recombinant protein.
2049076	1	62	theme	human	153:157	arg1	IFN					169:171	partially purified human leucocyte IFN	134:171	partially purified human leucocyte IFN	134:171	Natural human interferon alpha 2 (IFN-alpha 2) was isolated from a preparation of partially purified human leucocyte IFN by monoclonal-antibody immunoaffinity chromatography.
2049076	8	63	theme	O-linked	1218:1225	arg1	carbohydrates					1227:1239	O-linked carbohydrates	1218:1239	O-linked carbohydrates	1218:1239	These results suggested that Thr-106 of natural IFN-alpha 2 carries O-linked carbohydrates.
2049076	10	64	theme	Further	1637:1643	arg1	information					1645:1655	m.s. Further information	1632:1655	m.s. Further information on the composition of the glycans	1632:1689	For characterization of the carbohydrate moieties, the protein was treated with neuraminidase and/or O-glycanase and analysed by gel electrophoresis; in addition, glycopeptides obtained by proteinase digestion and separated by h.p.l.c. were characterized by sequence analysis and m.s. Further information on the composition of the glycans was obtained by monosaccharide analysis.
2049076	1	65	theme	IFN	169:171	arg1	preparation					119:129	a preparation	117:129	a preparation of partially purified human leucocyte IFN	117:171	Natural human interferon alpha 2 (IFN-alpha 2) was isolated from a preparation of partially purified human leucocyte IFN by monoclonal-antibody immunoaffinity chromatography.
2049076	0	66	gly	O-glycosylated	36:49	arg1	interferon-alpha					14:29	Natural human interferon-alpha 2	0:31	Natural human interferon-alpha 2	0:31	Natural human interferon-alpha 2 is O-glycosylated.
2049076	1	67	theme	monoclonal-antibody	176:194	arg1	chromatography					211:224	monoclonal-antibody immunoaffinity chromatography	176:224	monoclonal-antibody immunoaffinity chromatography	176:224	Natural human interferon alpha 2 (IFN-alpha 2) was isolated from a preparation of partially purified human leucocyte IFN by monoclonal-antibody immunoaffinity chromatography.
2049076	5	68	theme	natural	692:698	arg1	IFN-alpha					700:708	natural IFN-alpha 2	692:710	natural IFN-alpha 2	692:710	First, reverse-phase h.p.l.c. showed that natural IFN-alpha 2 was significantly more hydrophilic then expected.
2049076	8	69	theme	natural	1190:1196	arg1	IFN-alpha					1198:1206	natural IFN-alpha 2	1190:1208	natural IFN-alpha 2	1190:1208	These results suggested that Thr-106 of natural IFN-alpha 2 carries O-linked carbohydrates.
2049076	13	70	from	amounts	2126:2132	arg1	present					2109:2115	present	2109:2115	present	2109:2115	Further glycosylation isomers are present in small amounts.
2049076	9	71	theme	Reverse-phase	1242:1254	arg1	h.p.l.c.					1256:1263	Reverse-phase h.p.l.c.	1242:1263	Reverse-phase h.p.l.c. as well as SDS/PAGE of natural IFN-alpha 2	1242:1306	Reverse-phase h.p.l.c. as well as SDS/PAGE of natural IFN-alpha 2 showed that glycosylation is heterogeneous.
2049076	2	72	theme	purified	231:238	arg1	protein					240:246	The purified protein	227:246	The purified protein	227:246	The purified protein had a specific activity of 1.5 x 10(8) i.u./mg; it was estimated to constitute 10-20% of the total antiviral activity of leucocyte IFN.
2049076	6	73	theme	alkaline	917:924	arg1	conditions					926:935	mild alkaline conditions	912:935	mild alkaline conditions known to eliminate O-linked carbohydrates	912:977	Secondly, the apparent molecular mass of the natural protein determined by SDS/PAGE was higher than that of recombinant IFN-alpha 2; incubation under mild alkaline conditions known to eliminate O-linked carbohydrates resulted in a reduction of the apparent molecular mass to that of the recombinant protein.
2049076	5	74	theme	reverse-phase	657:669	arg1	h.p.l.c.					671:678	reverse-phase h.p.l.c.	657:678	reverse-phase h.p.l.c.	657:678	First, reverse-phase h.p.l.c. showed that natural IFN-alpha 2 was significantly more hydrophilic then expected.
2049076	6	75	theme	molecular	1019:1027	arg1	mass					1029:1032	the apparent molecular mass	1006:1032	the apparent molecular mass to that of the recombinant protein	1006:1067	Secondly, the apparent molecular mass of the natural protein determined by SDS/PAGE was higher than that of recombinant IFN-alpha 2; incubation under mild alkaline conditions known to eliminate O-linked carbohydrates resulted in a reduction of the apparent molecular mass to that of the recombinant protein.
2049076	2	76	theme	specific	254:261	arg1	activity					263:270	a specific activity	252:270	a specific activity of 1.5 x 10(8) i.u./mg	252:293	The purified protein had a specific activity of 1.5 x 10(8) i.u./mg; it was estimated to constitute 10-20% of the total antiviral activity of leucocyte IFN.
2049076	2	77	dep	1.5	275:277	arg1	8					284:284	8	284:284	8	284:284	The purified protein had a specific activity of 1.5 x 10(8) i.u./mg; it was estimated to constitute 10-20% of the total antiviral activity of leucocyte IFN.
2049076	9	78	theme	IFN-alpha	1296:1304	arg1	SDS/PAGE					1276:1283	SDS/PAGE	1276:1283	Reverse-phase h.p.l.c. as well as SDS/PAGE of natural IFN-alpha 2	1242:1306	Reverse-phase h.p.l.c. as well as SDS/PAGE of natural IFN-alpha 2 showed that glycosylation is heterogeneous.
2049076	9	78	theme	IFN-alpha	1296:1304	arg1	h.p.l.c.					1256:1263	Reverse-phase h.p.l.c.	1242:1263	Reverse-phase h.p.l.c. as well as SDS/PAGE of natural IFN-alpha 2	1242:1306	Reverse-phase h.p.l.c. as well as SDS/PAGE of natural IFN-alpha 2 showed that glycosylation is heterogeneous.
2049076	1	79	theme	human	60:64	arg1	alpha					77:81	Natural human interferon alpha 2	52:83	Natural human interferon alpha 2 (IFN-alpha 2)	52:97	Natural human interferon alpha 2 (IFN-alpha 2) was isolated from a preparation of partially purified human leucocyte IFN by monoclonal-antibody immunoaffinity chromatography.
2049076	1	79	theme	human	60:64	arg1	IFN-alpha					86:94	IFN-alpha 2	86:96	IFN-alpha 2	86:96	Natural human interferon alpha 2 (IFN-alpha 2) was isolated from a preparation of partially purified human leucocyte IFN by monoclonal-antibody immunoaffinity chromatography.
2049076	14	80	theme	IFN-alpha	2162:2170	arg1	species					2172:2178	the only IFN-alpha species	2153:2178	the only IFN-alpha species with a threonine residue at position 106	2153:2219	As IFN-alpha 2 is the only IFN-alpha species with a threonine residue at position 106, it may represent the only O-glycosylated human IFN-alpha protein.
2049076	14	80	theme	IFN-alpha	2162:2170	arg1	IFN-alpha					2138:2146	IFN-alpha 2	2138:2148	IFN-alpha 2	2138:2148	As IFN-alpha 2 is the only IFN-alpha species with a threonine residue at position 106, it may represent the only O-glycosylated human IFN-alpha protein.
2049076	10	81	dep	glycopeptides	1515:1527	arg1	separated					1566:1574	separated	1566:1574	separated by h.p.l.c.	1566:1586	For characterization of the carbohydrate moieties, the protein was treated with neuraminidase and/or O-glycanase and analysed by gel electrophoresis; in addition, glycopeptides obtained by proteinase digestion and separated by h.p.l.c. were characterized by sequence analysis and m.s. Further information on the composition of the glycans was obtained by monosaccharide analysis.
2049076	10	81	dep	glycopeptides	1515:1527	arg1	obtained					1529:1536	obtained	1529:1536	obtained by proteinase digestion	1529:1560	For characterization of the carbohydrate moieties, the protein was treated with neuraminidase and/or O-glycanase and analysed by gel electrophoresis; in addition, glycopeptides obtained by proteinase digestion and separated by h.p.l.c. were characterized by sequence analysis and m.s. Further information on the composition of the glycans was obtained by monosaccharide analysis.
2049076	10	82	theme	glycans	1683:1689	arg1	composition					1664:1674	the composition	1660:1674	the composition of the glycans	1660:1689	For characterization of the carbohydrate moieties, the protein was treated with neuraminidase and/or O-glycanase and analysed by gel electrophoresis; in addition, glycopeptides obtained by proteinase digestion and separated by h.p.l.c. were characterized by sequence analysis and m.s. Further information on the composition of the glycans was obtained by monosaccharide analysis.
2049076	0	83	theme	human	8:12	arg1	interferon-alpha					14:29	Natural human interferon-alpha 2	0:31	Natural human interferon-alpha 2	0:31	Natural human interferon-alpha 2 is O-glycosylated.
2049076	13	84	theme	small	2120:2124	arg1	amounts					2126:2132	small amounts	2120:2132	small amounts	2120:2132	Further glycosylation isomers are present in small amounts.
2049076	6	85	theme	recombinant	1049:1059	arg1	protein					1061:1067	the recombinant protein	1045:1067	the recombinant protein	1045:1067	Secondly, the apparent molecular mass of the natural protein determined by SDS/PAGE was higher than that of recombinant IFN-alpha 2; incubation under mild alkaline conditions known to eliminate O-linked carbohydrates resulted in a reduction of the apparent molecular mass to that of the recombinant protein.
2049076	13	86	attach	present	2109:2115	arg2	isomers					2097:2103	Further glycosylation isomers	2075:2103	Further glycosylation isomers	2075:2103	Further glycosylation isomers are present in small amounts.
2049076	13	86	attach	present	2109:2115	arg1	amounts					2126:2132	small amounts	2120:2132	small amounts	2120:2132	Further glycosylation isomers are present in small amounts.
2049076	3	87	theme	amino-acid-sequence	395:413	arg1	analysis					415:422	N-Terminal amino-acid-sequence analysis	384:422	N-Terminal amino-acid-sequence analysis	384:422	N-Terminal amino-acid-sequence analysis identified the subspecies IFN-alpha 2b and/or IFN-alpha 2c, whereas IFN-alpha 2a was not detectable.
2049076	4	88	theme	IFN-alpha	550:558	arg1	structure					529:537	The structure	525:537	The structure of natural IFN-alpha 2	525:560	The structure of natural IFN-alpha 2 was found to differ from that of its recombinant (Escherichia coli-derived) equivalent.
2049076	2	89	theme	IFN	379:381	arg1	activity					357:364	the total antiviral activity	337:364	the total antiviral activity of leucocyte IFN	337:381	The purified protein had a specific activity of 1.5 x 10(8) i.u./mg; it was estimated to constitute 10-20% of the total antiviral activity of leucocyte IFN.
2049076	14	90	with	species	2172:2178	arg1	residue					2197:2203	a threonine residue	2185:2203	a threonine residue at position 106	2185:2219	As IFN-alpha 2 is the only IFN-alpha species with a threonine residue at position 106, it may represent the only O-glycosylated human IFN-alpha protein.
2049076	8	91	link	O-linked	1218:1225	arg1	carbohydrates					1227:1239	O-linked carbohydrates	1218:1239	O-linked carbohydrates	1218:1239	These results suggested that Thr-106 of natural IFN-alpha 2 carries O-linked carbohydrates.
2049076	4	92	dep	recombinant	599:609	arg1	coli-derived					624:635	coli-derived	624:635	coli-derived	624:635	The structure of natural IFN-alpha 2 was found to differ from that of its recombinant (Escherichia coli-derived) equivalent.
2049076	10	93	theme	proteinase	1541:1550	arg1	digestion					1552:1560	proteinase digestion	1541:1560	proteinase digestion	1541:1560	For characterization of the carbohydrate moieties, the protein was treated with neuraminidase and/or O-glycanase and analysed by gel electrophoresis; in addition, glycopeptides obtained by proteinase digestion and separated by h.p.l.c. were characterized by sequence analysis and m.s. Further information on the composition of the glycans was obtained by monosaccharide analysis.
2049076	13	94	theme	glycosylation	2083:2095	arg1	isomers					2097:2103	Further glycosylation isomers	2075:2103	Further glycosylation isomers	2075:2103	Further glycosylation isomers are present in small amounts.
2049076	1	95	theme	Natural	52:58	arg1	alpha					77:81	Natural human interferon alpha 2	52:83	Natural human interferon alpha 2 (IFN-alpha 2)	52:97	Natural human interferon alpha 2 (IFN-alpha 2) was isolated from a preparation of partially purified human leucocyte IFN by monoclonal-antibody immunoaffinity chromatography.
2049076	1	95	theme	Natural	52:58	arg1	IFN-alpha					86:94	IFN-alpha 2	86:96	IFN-alpha 2	86:96	Natural human interferon alpha 2 (IFN-alpha 2) was isolated from a preparation of partially purified human leucocyte IFN by monoclonal-antibody immunoaffinity chromatography.
2049076	10	96	theme	carbohydrate	1380:1391	arg1	moieties					1393:1400	the carbohydrate moieties	1376:1400	the carbohydrate moieties	1376:1400	For characterization of the carbohydrate moieties, the protein was treated with neuraminidase and/or O-glycanase and analysed by gel electrophoresis; in addition, glycopeptides obtained by proteinase digestion and separated by h.p.l.c. were characterized by sequence analysis and m.s. Further information on the composition of the glycans was obtained by monosaccharide analysis.
2049076	3	97	theme	IFN-alpha	470:478	arg1	2c					480:481	IFN-alpha 2c	470:481	IFN-alpha 2c	470:481	N-Terminal amino-acid-sequence analysis identified the subspecies IFN-alpha 2b and/or IFN-alpha 2c, whereas IFN-alpha 2a was not detectable.
2049076	6	98	theme	natural	807:813	arg1	protein					815:821	the natural protein	803:821	the natural protein determined by SDS/PAGE	803:844	Secondly, the apparent molecular mass of the natural protein determined by SDS/PAGE was higher than that of recombinant IFN-alpha 2; incubation under mild alkaline conditions known to eliminate O-linked carbohydrates resulted in a reduction of the apparent molecular mass to that of the recombinant protein.
2049076	2	99	theme	antiviral	347:355	arg1	activity					357:364	the total antiviral activity	337:364	the total antiviral activity of leucocyte IFN	337:381	The purified protein had a specific activity of 1.5 x 10(8) i.u./mg; it was estimated to constitute 10-20% of the total antiviral activity of leucocyte IFN.
2049076	1	100	attach	isolated	103:110	arg2	IFN-alpha					86:94	IFN-alpha 2	86:96	IFN-alpha 2	86:96	Natural human interferon alpha 2 (IFN-alpha 2) was isolated from a preparation of partially purified human leucocyte IFN by monoclonal-antibody immunoaffinity chromatography.
2049076	1	100	attach	isolated	103:110	arg1	preparation					119:129	a preparation	117:129	a preparation of partially purified human leucocyte IFN	117:171	Natural human interferon alpha 2 (IFN-alpha 2) was isolated from a preparation of partially purified human leucocyte IFN by monoclonal-antibody immunoaffinity chromatography.
2049076	1	100	attach	isolated	103:110	arg2	alpha					77:81	Natural human interferon alpha 2	52:83	Natural human interferon alpha 2 (IFN-alpha 2)	52:97	Natural human interferon alpha 2 (IFN-alpha 2) was isolated from a preparation of partially purified human leucocyte IFN by monoclonal-antibody immunoaffinity chromatography.
2049076	2	101	contain	had	248:250	arg1	protein					240:246	The purified protein	227:246	The purified protein	227:246	The purified protein had a specific activity of 1.5 x 10(8) i.u./mg; it was estimated to constitute 10-20% of the total antiviral activity of leucocyte IFN.
2049076	2	101	contain	had	248:250	arg2	activity					263:270	a specific activity	252:270	a specific activity of 1.5 x 10(8) i.u./mg	252:293	The purified protein had a specific activity of 1.5 x 10(8) i.u./mg; it was estimated to constitute 10-20% of the total antiviral activity of leucocyte IFN.
18984734	10	0	theme	diabetes	1618:1625	arg1	detection					1605:1613	the early detection	1595:1613	the early detection of diabetes	1595:1625	These data suggest not only that site-specific O-GlcNAc levels reflect the glycemic status of an individual but also that O-GlcNAc site occupancy on erythrocyte proteins may be eventually useful as a diagnostic tool for the early detection of diabetes.
18984734	7	1	theme	normal	1100:1105	arg1	erythrocytes					1107:1118	diabetic and normal erythrocytes	1087:1118	diabetic and normal erythrocytes	1087:1118	Protein expression levels were compared between diabetic and normal erythrocytes.
18984734	4	2	theme	site-specific	768:780	arg1	levels					801:806	site-specific O-GlcNAc occupancy levels	768:806	site-specific O-GlcNAc occupancy levels between normal and diabetic erythrocyte proteins	768:855	The enrichment approach was combined with solid-phase chemical derivatization and isotopic labeling to detect O-GlcNAc modification sites and to compare site-specific O-GlcNAc occupancy levels between normal and diabetic erythrocyte proteins.
18984734	10	3	from	occupancy	1511:1519	arg1	proteins					1536:1543	erythrocyte proteins	1524:1543	erythrocyte proteins	1524:1543	These data suggest not only that site-specific O-GlcNAc levels reflect the glycemic status of an individual but also that O-GlcNAc site occupancy on erythrocyte proteins may be eventually useful as a diagnostic tool for the early detection of diabetes.
18984734	8	4	theme	O-GlcNAc	1133:1140	arg1	sites					1142:1146	Thirty-five O-GlcNAc sites	1121:1146	Thirty-five O-GlcNAc sites	1121:1146	Thirty-five O-GlcNAc sites were reproducibly identified, and their site-specific O-GlcNAc occupancy ratios were calculated.
18984734	4	5	theme	enrichment	619:628	arg1	approach					630:637	The enrichment approach	615:637	The enrichment approach	615:637	The enrichment approach was combined with solid-phase chemical derivatization and isotopic labeling to detect O-GlcNAc modification sites and to compare site-specific O-GlcNAc occupancy levels between normal and diabetic erythrocyte proteins.
18984734	6	6	theme	erythrocyte	1001:1011	arg1	proteins					1013:1020	Twenty-five GlcNAcylated erythrocyte proteins	976:1020	Twenty-five GlcNAcylated erythrocyte proteins	976:1020	Twenty-five GlcNAcylated erythrocyte proteins were identified.
18984734	5	7	dep	cycling	896:902	arg1	removal					918:924	removal	918:924	removal	918:924	RESULTS The enzymes that catalyze the cycling (addition and removal) of O-GlcNAc were detected in human erythrocytes.
18984734	5	7	dep	cycling	896:902	arg1	addition					905:912	addition	905:912	addition	905:912	RESULTS The enzymes that catalyze the cycling (addition and removal) of O-GlcNAc were detected in human erythrocytes.
18984734	7	8	theme	diabetic	1087:1094	arg1	erythrocytes					1107:1118	diabetic and normal erythrocytes	1087:1118	diabetic and normal erythrocytes	1087:1118	Protein expression levels were compared between diabetic and normal erythrocytes.
18984734	2	9	theme	GlcNAcylation	278:290	arg1	extent					268:273	the extent	264:273	the extent of GlcNAcylation on human erythrocyte proteins	264:320	Here, we investigated the extent of GlcNAcylation on human erythrocyte proteins and compared site-specific GlcNAcylation on erythrocyte proteins from diabetic and normal individuals.
18984734	6	10	theme	GlcNAcylated	988:999	arg1	proteins					1013:1020	Twenty-five GlcNAcylated erythrocyte proteins	976:1020	Twenty-five GlcNAcylated erythrocyte proteins	976:1020	Twenty-five GlcNAcylated erythrocyte proteins were identified.
18984734	10	11	theme	early	1599:1603	arg1	detection					1605:1613	the early detection	1595:1613	the early detection of diabetes	1595:1625	These data suggest not only that site-specific O-GlcNAc levels reflect the glycemic status of an individual but also that O-GlcNAc site occupancy on erythrocyte proteins may be eventually useful as a diagnostic tool for the early detection of diabetes.
18984734	9	12	theme	glycemic	1358:1365	arg1	status					1367:1372	glycemic status	1358:1372	glycemic status	1358:1372	CONCLUSIONS GlcNAcylation is differentially regulated at individual sites on erythrocyte proteins in response to glycemic status.
18984734	10	13	theme	glycemic	1450:1457	arg1	status					1459:1464	the glycemic status	1446:1464	the glycemic status of an individual	1446:1481	These data suggest not only that site-specific O-GlcNAc levels reflect the glycemic status of an individual but also that O-GlcNAc site occupancy on erythrocyte proteins may be eventually useful as a diagnostic tool for the early detection of diabetes.
18984734	8	14	theme	Thirty-five	1121:1131	arg1	sites					1142:1146	Thirty-five O-GlcNAc sites	1121:1146	Thirty-five O-GlcNAc sites	1121:1146	Thirty-five O-GlcNAc sites were reproducibly identified, and their site-specific O-GlcNAc occupancy ratios were calculated.
18984734	2	15	theme	site-specific	335:347	arg1	GlcNAcylation					349:361	site-specific GlcNAcylation	335:361	site-specific GlcNAcylation on erythrocyte proteins from diabetic and normal individuals	335:422	Here, we investigated the extent of GlcNAcylation on human erythrocyte proteins and compared site-specific GlcNAcylation on erythrocyte proteins from diabetic and normal individuals.
18984734	8	16	theme	site-specific	1188:1200	arg1	ratios					1221:1226	their site-specific O-GlcNAc occupancy ratios	1182:1226	their site-specific O-GlcNAc occupancy ratios	1182:1226	Thirty-five O-GlcNAc sites were reproducibly identified, and their site-specific O-GlcNAc occupancy ratios were calculated.
18984734	10	17	theme	O-GlcNAc	1422:1429	arg1	levels					1431:1436	site-specific O-GlcNAc levels	1408:1436	site-specific O-GlcNAc levels	1408:1436	These data suggest not only that site-specific O-GlcNAc levels reflect the glycemic status of an individual but also that O-GlcNAc site occupancy on erythrocyte proteins may be eventually useful as a diagnostic tool for the early detection of diabetes.
18984734	1	18	theme	diabetic	164:171	arg1	tissues					173:179	diabetic tissues	164:179	diabetic tissues	164:179	OBJECTIVE O-linked N-acetylglucosamine (O-GlcNAc) is upregulated in diabetic tissues and plays a role in insulin resistance and glucose toxicity.
18984734	3	19	theme	RESEARCH	425:432	arg1	DESIGN					434:439	RESEARCH DESIGN	425:439	RESEARCH DESIGN	425:439	RESEARCH DESIGN AND METHODS GlcNAcylated erythrocyte proteins or GlcNAcylated peptides were tagged and selectively enriched by a chemoenzymatic approach and identified by mass spectrometry.
18984734	7	20	theme	expression	1047:1056	arg1	levels					1058:1063	Protein expression levels	1039:1063	Protein expression levels	1039:1063	Protein expression levels were compared between diabetic and normal erythrocytes.
18984734	10	21	theme	erythrocyte	1524:1534	arg1	proteins					1536:1543	erythrocyte proteins	1524:1543	erythrocyte proteins	1524:1543	These data suggest not only that site-specific O-GlcNAc levels reflect the glycemic status of an individual but also that O-GlcNAc site occupancy on erythrocyte proteins may be eventually useful as a diagnostic tool for the early detection of diabetes.
18984734	3	22	theme	erythrocyte	466:476	arg1	proteins					478:485	RESEARCH DESIGN AND METHODS GlcNAcylated erythrocyte proteins	425:485	RESEARCH DESIGN AND METHODS GlcNAcylated erythrocyte proteins	425:485	RESEARCH DESIGN AND METHODS GlcNAcylated erythrocyte proteins or GlcNAcylated peptides were tagged and selectively enriched by a chemoenzymatic approach and identified by mass spectrometry.
18984734	10	23	theme	individual	1472:1481	arg1	status					1459:1464	the glycemic status	1446:1464	the glycemic status of an individual	1446:1481	These data suggest not only that site-specific O-GlcNAc levels reflect the glycemic status of an individual but also that O-GlcNAc site occupancy on erythrocyte proteins may be eventually useful as a diagnostic tool for the early detection of diabetes.
18984734	8	24	theme	occupancy	1211:1219	arg1	ratios					1221:1226	their site-specific O-GlcNAc occupancy ratios	1182:1226	their site-specific O-GlcNAc occupancy ratios	1182:1226	Thirty-five O-GlcNAc sites were reproducibly identified, and their site-specific O-GlcNAc occupancy ratios were calculated.
18984734	2	25	from	GlcNAcylation	349:361	arg1	proteins					378:385	erythrocyte proteins	366:385	erythrocyte proteins	366:385	Here, we investigated the extent of GlcNAcylation on human erythrocyte proteins and compared site-specific GlcNAcylation on erythrocyte proteins from diabetic and normal individuals.
18984734	2	26	theme	erythrocyte	301:311	arg1	proteins					313:320	human erythrocyte proteins	295:320	human erythrocyte proteins	295:320	Here, we investigated the extent of GlcNAcylation on human erythrocyte proteins and compared site-specific GlcNAcylation on erythrocyte proteins from diabetic and normal individuals.
18984734	6	27	theme	Twenty-five	976:986	arg1	proteins					1013:1020	Twenty-five GlcNAcylated erythrocyte proteins	976:1020	Twenty-five GlcNAcylated erythrocyte proteins	976:1020	Twenty-five GlcNAcylated erythrocyte proteins were identified.
18984734	2	28	theme	diabetic	392:399	arg1	individuals					412:422	diabetic and normal individuals	392:422	diabetic and normal individuals	392:422	Here, we investigated the extent of GlcNAcylation on human erythrocyte proteins and compared site-specific GlcNAcylation on erythrocyte proteins from diabetic and normal individuals.
18984734	0	29	theme	Site-specific	0:12	arg1	GlcNAcylation					14:26	Site-specific GlcNAcylation	0:26	Site-specific GlcNAcylation of human erythrocyte proteins: potential biomarker(s) for diabetes.	0:94	Site-specific GlcNAcylation of human erythrocyte proteins: potential biomarker(s) for diabetes.
18984734	10	30	theme	diagnostic	1575:1584	arg1	tool					1586:1589	a diagnostic tool	1573:1589	a diagnostic tool for the early detection of diabetes	1573:1625	These data suggest not only that site-specific O-GlcNAc levels reflect the glycemic status of an individual but also that O-GlcNAc site occupancy on erythrocyte proteins may be eventually useful as a diagnostic tool for the early detection of diabetes.
18984734	8	31	theme	O-GlcNAc	1202:1209	arg1	ratios					1221:1226	their site-specific O-GlcNAc occupancy ratios	1182:1226	their site-specific O-GlcNAc occupancy ratios	1182:1226	Thirty-five O-GlcNAc sites were reproducibly identified, and their site-specific O-GlcNAc occupancy ratios were calculated.
18984734	4	32	theme	O-GlcNAc	725:732	arg1	sites					747:751	O-GlcNAc modification sites	725:751	O-GlcNAc modification sites	725:751	The enrichment approach was combined with solid-phase chemical derivatization and isotopic labeling to detect O-GlcNAc modification sites and to compare site-specific O-GlcNAc occupancy levels between normal and diabetic erythrocyte proteins.
18984734	2	33	theme	human	295:299	arg1	proteins					313:320	human erythrocyte proteins	295:320	human erythrocyte proteins	295:320	Here, we investigated the extent of GlcNAcylation on human erythrocyte proteins and compared site-specific GlcNAcylation on erythrocyte proteins from diabetic and normal individuals.
18984734	9	34	theme	CONCLUSIONS	1245:1255	arg1	GlcNAcylation					1257:1269	CONCLUSIONS GlcNAcylation	1245:1269	CONCLUSIONS GlcNAcylation	1245:1269	CONCLUSIONS GlcNAcylation is differentially regulated at individual sites on erythrocyte proteins in response to glycemic status.
18984734	3	35	theme	METHODS	445:451	arg1	proteins					478:485	RESEARCH DESIGN AND METHODS GlcNAcylated erythrocyte proteins	425:485	RESEARCH DESIGN AND METHODS GlcNAcylated erythrocyte proteins	425:485	RESEARCH DESIGN AND METHODS GlcNAcylated erythrocyte proteins or GlcNAcylated peptides were tagged and selectively enriched by a chemoenzymatic approach and identified by mass spectrometry.
18984734	0	36	theme	human	31:35	arg1	proteins					49:56	human erythrocyte proteins	31:56	human erythrocyte proteins	31:56	Site-specific GlcNAcylation of human erythrocyte proteins: potential biomarker(s) for diabetes.
18984734	5	37	dep	RESULTS	858:864	arg1	enzymes					870:876	The enzymes	866:876	RESULTS The enzymes that catalyze the cycling (addition and removal) of O-GlcNAc	858:937	RESULTS The enzymes that catalyze the cycling (addition and removal) of O-GlcNAc were detected in human erythrocytes.
18984734	4	38	theme	occupancy	791:799	arg1	levels					801:806	site-specific O-GlcNAc occupancy levels	768:806	site-specific O-GlcNAc occupancy levels between normal and diabetic erythrocyte proteins	768:855	The enrichment approach was combined with solid-phase chemical derivatization and isotopic labeling to detect O-GlcNAc modification sites and to compare site-specific O-GlcNAc occupancy levels between normal and diabetic erythrocyte proteins.
18984734	3	39	theme	mass	596:599	arg1	spectrometry					601:612	mass spectrometry	596:612	mass spectrometry	596:612	RESEARCH DESIGN AND METHODS GlcNAcylated erythrocyte proteins or GlcNAcylated peptides were tagged and selectively enriched by a chemoenzymatic approach and identified by mass spectrometry.
18984734	3	40	theme	GlcNAcylated	490:501	arg1	peptides					503:510	GlcNAcylated peptides	490:510	GlcNAcylated peptides	490:510	RESEARCH DESIGN AND METHODS GlcNAcylated erythrocyte proteins or GlcNAcylated peptides were tagged and selectively enriched by a chemoenzymatic approach and identified by mass spectrometry.
18984734	4	41	theme	normal	816:821	arg1	proteins					848:855	normal and diabetic erythrocyte proteins	816:855	normal and diabetic erythrocyte proteins	816:855	The enrichment approach was combined with solid-phase chemical derivatization and isotopic labeling to detect O-GlcNAc modification sites and to compare site-specific O-GlcNAc occupancy levels between normal and diabetic erythrocyte proteins.
18984734	10	42	theme	site	1506:1509	arg1	occupancy					1511:1519	O-GlcNAc site occupancy	1497:1519	O-GlcNAc site occupancy on erythrocyte proteins	1497:1543	These data suggest not only that site-specific O-GlcNAc levels reflect the glycemic status of an individual but also that O-GlcNAc site occupancy on erythrocyte proteins may be eventually useful as a diagnostic tool for the early detection of diabetes.
18984734	5	43	located	detected	944:951	arg1	erythrocytes					962:973	human erythrocytes	956:973	human erythrocytes	956:973	RESULTS The enzymes that catalyze the cycling (addition and removal) of O-GlcNAc were detected in human erythrocytes.
18984734	5	43	located	detected	944:951	arg2	RESULTS					858:864	RESULTS	858:864	RESULTS The enzymes that catalyze the cycling (addition and removal) of O-GlcNAc	858:937	RESULTS The enzymes that catalyze the cycling (addition and removal) of O-GlcNAc were detected in human erythrocytes.
18984734	1	44	theme	OBJECTIVE	96:104	arg1	O-GlcNAc					136:143	O-GlcNAc	136:143	O-GlcNAc	136:143	OBJECTIVE O-linked N-acetylglucosamine (O-GlcNAc) is upregulated in diabetic tissues and plays a role in insulin resistance and glucose toxicity.
18984734	1	44	theme	OBJECTIVE	96:104	arg1	N-acetylglucosamine					115:133	OBJECTIVE O-linked N-acetylglucosamine	96:133	OBJECTIVE O-linked N-acetylglucosamine (O-GlcNAc)	96:144	OBJECTIVE O-linked N-acetylglucosamine (O-GlcNAc) is upregulated in diabetic tissues and plays a role in insulin resistance and glucose toxicity.
18984734	9	45	from	sites	1313:1317	arg1	proteins					1334:1341	erythrocyte proteins	1322:1341	erythrocyte proteins	1322:1341	CONCLUSIONS GlcNAcylation is differentially regulated at individual sites on erythrocyte proteins in response to glycemic status.
18984734	0	46	theme	proteins	49:56	arg1	GlcNAcylation					14:26	Site-specific GlcNAcylation	0:26	Site-specific GlcNAcylation of human erythrocyte proteins: potential biomarker(s) for diabetes.	0:94	Site-specific GlcNAcylation of human erythrocyte proteins: potential biomarker(s) for diabetes.
18984734	4	47	theme	modification	734:745	arg1	sites					747:751	O-GlcNAc modification sites	725:751	O-GlcNAc modification sites	725:751	The enrichment approach was combined with solid-phase chemical derivatization and isotopic labeling to detect O-GlcNAc modification sites and to compare site-specific O-GlcNAc occupancy levels between normal and diabetic erythrocyte proteins.
18984734	2	48	theme	normal	405:410	arg1	individuals					412:422	diabetic and normal individuals	392:422	diabetic and normal individuals	392:422	Here, we investigated the extent of GlcNAcylation on human erythrocyte proteins and compared site-specific GlcNAcylation on erythrocyte proteins from diabetic and normal individuals.
18984734	0	49	theme	erythrocyte	37:47	arg1	proteins					49:56	human erythrocyte proteins	31:56	human erythrocyte proteins	31:56	Site-specific GlcNAcylation of human erythrocyte proteins: potential biomarker(s) for diabetes.
18984734	1	50	theme	insulin	201:207	arg1	resistance					209:218	insulin resistance	201:218	insulin resistance	201:218	OBJECTIVE O-linked N-acetylglucosamine (O-GlcNAc) is upregulated in diabetic tissues and plays a role in insulin resistance and glucose toxicity.
18984734	0	51	theme	potential	59:67	arg1	s					79:79	potential biomarker(s)	59:80	Site-specific GlcNAcylation of human erythrocyte proteins: potential biomarker(s) for diabetes.	0:94	Site-specific GlcNAcylation of human erythrocyte proteins: potential biomarker(s) for diabetes.
18984734	9	52	gly	GlcNAcylation	1257:1269	arg1	response					1346:1353	response	1346:1353	response to glycemic status	1346:1372	CONCLUSIONS GlcNAcylation is differentially regulated at individual sites on erythrocyte proteins in response to glycemic status.
18984734	9	52	gly	GlcNAcylation	1257:1269	arg1	sites					1313:1317	individual sites	1302:1317	individual sites on erythrocyte proteins	1302:1341	CONCLUSIONS GlcNAcylation is differentially regulated at individual sites on erythrocyte proteins in response to glycemic status.
18984734	3	53	theme	GlcNAcylated	453:464	arg1	proteins					478:485	RESEARCH DESIGN AND METHODS GlcNAcylated erythrocyte proteins	425:485	RESEARCH DESIGN AND METHODS GlcNAcylated erythrocyte proteins	425:485	RESEARCH DESIGN AND METHODS GlcNAcylated erythrocyte proteins or GlcNAcylated peptides were tagged and selectively enriched by a chemoenzymatic approach and identified by mass spectrometry.
18984734	1	54	theme	O-linked	106:113	arg1	O-GlcNAc					136:143	O-GlcNAc	136:143	O-GlcNAc	136:143	OBJECTIVE O-linked N-acetylglucosamine (O-GlcNAc) is upregulated in diabetic tissues and plays a role in insulin resistance and glucose toxicity.
18984734	1	54	theme	O-linked	106:113	arg1	N-acetylglucosamine					115:133	OBJECTIVE O-linked N-acetylglucosamine	96:133	OBJECTIVE O-linked N-acetylglucosamine (O-GlcNAc)	96:144	OBJECTIVE O-linked N-acetylglucosamine (O-GlcNAc) is upregulated in diabetic tissues and plays a role in insulin resistance and glucose toxicity.
18984734	9	55	theme	individual	1302:1311	arg1	sites					1313:1317	individual sites	1302:1317	individual sites on erythrocyte proteins	1302:1341	CONCLUSIONS GlcNAcylation is differentially regulated at individual sites on erythrocyte proteins in response to glycemic status.
18984734	4	56	theme	O-GlcNAc	782:789	arg1	levels					801:806	site-specific O-GlcNAc occupancy levels	768:806	site-specific O-GlcNAc occupancy levels between normal and diabetic erythrocyte proteins	768:855	The enrichment approach was combined with solid-phase chemical derivatization and isotopic labeling to detect O-GlcNAc modification sites and to compare site-specific O-GlcNAc occupancy levels between normal and diabetic erythrocyte proteins.
18984734	10	57	theme	site-specific	1408:1420	arg1	levels					1431:1436	site-specific O-GlcNAc levels	1408:1436	site-specific O-GlcNAc levels	1408:1436	These data suggest not only that site-specific O-GlcNAc levels reflect the glycemic status of an individual but also that O-GlcNAc site occupancy on erythrocyte proteins may be eventually useful as a diagnostic tool for the early detection of diabetes.
18984734	7	58	theme	Protein	1039:1045	arg1	levels					1058:1063	Protein expression levels	1039:1063	Protein expression levels	1039:1063	Protein expression levels were compared between diabetic and normal erythrocytes.
18984734	1	59	link	O-linked	106:113	arg1	O-GlcNAc					136:143	O-GlcNAc	136:143	O-GlcNAc	136:143	OBJECTIVE O-linked N-acetylglucosamine (O-GlcNAc) is upregulated in diabetic tissues and plays a role in insulin resistance and glucose toxicity.
18984734	1	59	link	O-linked	106:113	arg1	N-acetylglucosamine					115:133	OBJECTIVE O-linked N-acetylglucosamine	96:133	OBJECTIVE O-linked N-acetylglucosamine (O-GlcNAc)	96:144	OBJECTIVE O-linked N-acetylglucosamine (O-GlcNAc) is upregulated in diabetic tissues and plays a role in insulin resistance and glucose toxicity.
18984734	5	60	theme	human	956:960	arg1	erythrocytes					962:973	human erythrocytes	956:973	human erythrocytes	956:973	RESULTS The enzymes that catalyze the cycling (addition and removal) of O-GlcNAc were detected in human erythrocytes.
18984734	10	61	theme	O-GlcNAc	1497:1504	arg1	occupancy					1511:1519	O-GlcNAc site occupancy	1497:1519	O-GlcNAc site occupancy on erythrocyte proteins	1497:1543	These data suggest not only that site-specific O-GlcNAc levels reflect the glycemic status of an individual but also that O-GlcNAc site occupancy on erythrocyte proteins may be eventually useful as a diagnostic tool for the early detection of diabetes.
18984734	4	62	theme	erythrocyte	836:846	arg1	proteins					848:855	normal and diabetic erythrocyte proteins	816:855	normal and diabetic erythrocyte proteins	816:855	The enrichment approach was combined with solid-phase chemical derivatization and isotopic labeling to detect O-GlcNAc modification sites and to compare site-specific O-GlcNAc occupancy levels between normal and diabetic erythrocyte proteins.
18984734	4	63	theme	solid-phase	657:667	arg1	derivatization					678:691	solid-phase chemical derivatization	657:691	solid-phase chemical derivatization	657:691	The enrichment approach was combined with solid-phase chemical derivatization and isotopic labeling to detect O-GlcNAc modification sites and to compare site-specific O-GlcNAc occupancy levels between normal and diabetic erythrocyte proteins.
18984734	9	64	theme	erythrocyte	1322:1332	arg1	proteins					1334:1341	erythrocyte proteins	1322:1341	erythrocyte proteins	1322:1341	CONCLUSIONS GlcNAcylation is differentially regulated at individual sites on erythrocyte proteins in response to glycemic status.
18984734	4	65	theme	diabetic	827:834	arg1	proteins					848:855	normal and diabetic erythrocyte proteins	816:855	normal and diabetic erythrocyte proteins	816:855	The enrichment approach was combined with solid-phase chemical derivatization and isotopic labeling to detect O-GlcNAc modification sites and to compare site-specific O-GlcNAc occupancy levels between normal and diabetic erythrocyte proteins.
18984734	3	66	theme	chemoenzymatic	554:567	arg1	approach					569:576	a chemoenzymatic approach	552:576	a chemoenzymatic approach	552:576	RESEARCH DESIGN AND METHODS GlcNAcylated erythrocyte proteins or GlcNAcylated peptides were tagged and selectively enriched by a chemoenzymatic approach and identified by mass spectrometry.
18984734	5	67	theme	O-GlcNAc	930:937	arg1	cycling					896:902	the cycling	892:902	the cycling (addition and removal) of O-GlcNAc	892:937	RESULTS The enzymes that catalyze the cycling (addition and removal) of O-GlcNAc were detected in human erythrocytes.
18984734	0	68	dep	GlcNAcylation	14:26	arg1	s					79:79	potential biomarker(s)	59:80	Site-specific GlcNAcylation of human erythrocyte proteins: potential biomarker(s) for diabetes.	0:94	Site-specific GlcNAcylation of human erythrocyte proteins: potential biomarker(s) for diabetes.
18984734	2	69	from	individuals	412:422	arg1	GlcNAcylation					349:361	site-specific GlcNAcylation	335:361	site-specific GlcNAcylation on erythrocyte proteins from diabetic and normal individuals	335:422	Here, we investigated the extent of GlcNAcylation on human erythrocyte proteins and compared site-specific GlcNAcylation on erythrocyte proteins from diabetic and normal individuals.
18984734	2	70	from	extent	268:273	arg1	proteins					313:320	human erythrocyte proteins	295:320	human erythrocyte proteins	295:320	Here, we investigated the extent of GlcNAcylation on human erythrocyte proteins and compared site-specific GlcNAcylation on erythrocyte proteins from diabetic and normal individuals.
18984734	1	71	theme	glucose	224:230	arg1	toxicity					232:239	glucose toxicity	224:239	glucose toxicity	224:239	OBJECTIVE O-linked N-acetylglucosamine (O-GlcNAc) is upregulated in diabetic tissues and plays a role in insulin resistance and glucose toxicity.
18984734	0	72	theme	biomarker	69:77	arg1	s					79:79	potential biomarker(s)	59:80	Site-specific GlcNAcylation of human erythrocyte proteins: potential biomarker(s) for diabetes.	0:94	Site-specific GlcNAcylation of human erythrocyte proteins: potential biomarker(s) for diabetes.
18984734	3	73	theme	DESIGN	434:439	arg1	proteins					478:485	RESEARCH DESIGN AND METHODS GlcNAcylated erythrocyte proteins	425:485	RESEARCH DESIGN AND METHODS GlcNAcylated erythrocyte proteins	425:485	RESEARCH DESIGN AND METHODS GlcNAcylated erythrocyte proteins or GlcNAcylated peptides were tagged and selectively enriched by a chemoenzymatic approach and identified by mass spectrometry.
18984734	4	74	theme	isotopic	697:704	arg1	labeling					706:713	isotopic labeling	697:713	isotopic labeling	697:713	The enrichment approach was combined with solid-phase chemical derivatization and isotopic labeling to detect O-GlcNAc modification sites and to compare site-specific O-GlcNAc occupancy levels between normal and diabetic erythrocyte proteins.
18984734	2	75	theme	erythrocyte	366:376	arg1	proteins					378:385	erythrocyte proteins	366:385	erythrocyte proteins	366:385	Here, we investigated the extent of GlcNAcylation on human erythrocyte proteins and compared site-specific GlcNAcylation on erythrocyte proteins from diabetic and normal individuals.
18984734	4	76	theme	chemical	669:676	arg1	derivatization					678:691	solid-phase chemical derivatization	657:691	solid-phase chemical derivatization	657:691	The enrichment approach was combined with solid-phase chemical derivatization and isotopic labeling to detect O-GlcNAc modification sites and to compare site-specific O-GlcNAc occupancy levels between normal and diabetic erythrocyte proteins.
11180632	0	0	theme	urine	76:80	arg1	protein					112:118	human urine cerebroside sulfate activator protein	70:118	human urine cerebroside sulfate activator protein	70:118	Structure of the asparagine-linked sugar chains of porcine kidney and human urine cerebroside sulfate activator protein.
11180632	7	1	theme	final	1388:1392	arg1	product					1394:1400	the final product	1384:1400	the final product of intra-lysosomal exoglycosidase digestion	1384:1444	This highly degraded structure probably represents the final product of intra-lysosomal exoglycosidase digestion.
11180632	6	2	from	kidney	1141:1146	arg1	pentasaccharides					1115:1130	The pentasaccharides	1111:1130	The pentasaccharides from pig kidney and human urine protein	1111:1170	The pentasaccharides from pig kidney and human urine protein were shown to be of the asparagine-linked complex type composed of mannose-alpha 1-6-mannose-beta 1-4-N-acetylglucosamine-N-acetylglucosamine(alpha 1-6-fucose).
11180632	2	3	theme	exoglycosidase	371:384	arg1	digestion					386:394	Exhaustive sequential exoglycosidase digestion	349:394	Exhaustive sequential exoglycosidase digestion	349:394	Exhaustive sequential exoglycosidase digestion of the trimethyl-p-aminophenyl derivatives, followed by either matrix-assisted laser desorption/ionization and/or mass spectrometry, was used to define the residues and their linkages.
11180632	9	4	theme	sequencing	1648:1657	arg1	those					1692:1696	those	1692:1696	those	1692:1696	The procedures developed will be useful for sequencing other oligosaccharides including those from other members of the lipid-binding protein class to which cerebroside sulfate activator belongs.
11180632	9	4	theme	sequencing	1648:1657	arg1	oligosaccharides					1665:1680	sequencing other oligosaccharides	1648:1680	sequencing other oligosaccharides including those from other members of the lipid-binding protein class to which cerebroside sulfate activator belongs	1648:1797	The procedures developed will be useful for sequencing other oligosaccharides including those from other members of the lipid-binding protein class to which cerebroside sulfate activator belongs.
11180632	0	5	theme	human	70:74	arg1	protein					112:118	human urine cerebroside sulfate activator protein	70:118	human urine cerebroside sulfate activator protein	70:118	Structure of the asparagine-linked sugar chains of porcine kidney and human urine cerebroside sulfate activator protein.
11180632	0	6	link	asparagine-linked	17:33	arg1	chains					41:46	the asparagine-linked sugar chains	13:46	the asparagine-linked sugar chains of porcine kidney and human urine cerebroside sulfate activator protein	13:118	Structure of the asparagine-linked sugar chains of porcine kidney and human urine cerebroside sulfate activator protein.
11180632	2	7	theme	sequential	360:369	arg1	digestion					386:394	Exhaustive sequential exoglycosidase digestion	349:394	Exhaustive sequential exoglycosidase digestion	349:394	Exhaustive sequential exoglycosidase digestion of the trimethyl-p-aminophenyl derivatives, followed by either matrix-assisted laser desorption/ionization and/or mass spectrometry, was used to define the residues and their linkages.
11180632	9	8	theme	other	1659:1663	arg1	those					1692:1696	those	1692:1696	those	1692:1696	The procedures developed will be useful for sequencing other oligosaccharides including those from other members of the lipid-binding protein class to which cerebroside sulfate activator belongs.
11180632	9	8	theme	other	1659:1663	arg1	oligosaccharides					1665:1680	sequencing other oligosaccharides	1648:1680	sequencing other oligosaccharides including those from other members of the lipid-binding protein class to which cerebroside sulfate activator belongs	1648:1797	The procedures developed will be useful for sequencing other oligosaccharides including those from other members of the lipid-binding protein class to which cerebroside sulfate activator belongs.
11180632	0	9	theme	sulfate	94:100	arg1	protein					112:118	human urine cerebroside sulfate activator protein	70:118	human urine cerebroside sulfate activator protein	70:118	Structure of the asparagine-linked sugar chains of porcine kidney and human urine cerebroside sulfate activator protein.
11180632	2	10	used	used	533:536	arg2	digestion					386:394	Exhaustive sequential exoglycosidase digestion	349:394	Exhaustive sequential exoglycosidase digestion	349:394	Exhaustive sequential exoglycosidase digestion of the trimethyl-p-aminophenyl derivatives, followed by either matrix-assisted laser desorption/ionization and/or mass spectrometry, was used to define the residues and their linkages.
11180632	1	11	from	linkages	159:166	arg1	oligosaccharides					175:190	the oligosaccharides	171:190	the oligosaccharides from pig kidney and human urine cerebroside sulfate activator proteins (saposin B)	171:273	The specific sugar residues and their linkages in the oligosaccharides from pig kidney and human urine cerebroside sulfate activator proteins (saposin B), although previously hypothesized, have been unambiguously characterized.
11180632	1	11	from	linkages	159:166	arg1	proteins					254:261	pig kidney and human urine cerebroside sulfate activator proteins	197:261	pig kidney and human urine cerebroside sulfate activator proteins (saposin B)	197:273	The specific sugar residues and their linkages in the oligosaccharides from pig kidney and human urine cerebroside sulfate activator proteins (saposin B), although previously hypothesized, have been unambiguously characterized.
11180632	1	11	from	linkages	159:166	arg1	B					272:272	saposin B	264:272	saposin B	264:272	The specific sugar residues and their linkages in the oligosaccharides from pig kidney and human urine cerebroside sulfate activator proteins (saposin B), although previously hypothesized, have been unambiguously characterized.
11180632	8	12	theme	conventional	1563:1574	arg1	sequencing					1592:1601	conventional oligosaccharide sequencing	1563:1601	conventional oligosaccharide sequencing	1563:1601	Oligosaccharide sequencing by specific exoglycosidase degradation coupled with mass spectrometry is more rapid than conventional oligosaccharide sequencing.
11180632	1	13	theme	saposin	264:270	arg1	proteins					254:261	pig kidney and human urine cerebroside sulfate activator proteins	197:261	pig kidney and human urine cerebroside sulfate activator proteins (saposin B)	197:273	The specific sugar residues and their linkages in the oligosaccharides from pig kidney and human urine cerebroside sulfate activator proteins (saposin B), although previously hypothesized, have been unambiguously characterized.
11180632	1	13	theme	saposin	264:270	arg1	B					272:272	saposin B	264:272	saposin B	264:272	The specific sugar residues and their linkages in the oligosaccharides from pig kidney and human urine cerebroside sulfate activator proteins (saposin B), although previously hypothesized, have been unambiguously characterized.
11180632	0	14	theme	cerebroside	82:92	arg1	protein					112:118	human urine cerebroside sulfate activator protein	70:118	human urine cerebroside sulfate activator protein	70:118	Structure of the asparagine-linked sugar chains of porcine kidney and human urine cerebroside sulfate activator protein.
11180632	1	15	from	residues	140:147	arg1	oligosaccharides					175:190	the oligosaccharides	171:190	the oligosaccharides from pig kidney and human urine cerebroside sulfate activator proteins (saposin B)	171:273	The specific sugar residues and their linkages in the oligosaccharides from pig kidney and human urine cerebroside sulfate activator proteins (saposin B), although previously hypothesized, have been unambiguously characterized.
11180632	1	15	from	residues	140:147	arg1	proteins					254:261	pig kidney and human urine cerebroside sulfate activator proteins	197:261	pig kidney and human urine cerebroside sulfate activator proteins (saposin B)	197:273	The specific sugar residues and their linkages in the oligosaccharides from pig kidney and human urine cerebroside sulfate activator proteins (saposin B), although previously hypothesized, have been unambiguously characterized.
11180632	1	15	from	residues	140:147	arg1	B					272:272	saposin B	264:272	saposin B	264:272	The specific sugar residues and their linkages in the oligosaccharides from pig kidney and human urine cerebroside sulfate activator proteins (saposin B), although previously hypothesized, have been unambiguously characterized.
11180632	4	16	theme	Reducing	788:795	arg1	termini					797:803	Reducing termini	788:803	Reducing termini	788:803	Reducing termini were converted to the trimethyl-p-aminophenyl derivative and the samples were further purified by normal-phase HPLC.
11180632	6	17	theme	pig	1137:1139	arg1	kidney					1141:1146	pig kidney	1137:1146	pig kidney	1137:1146	The pentasaccharides from pig kidney and human urine protein were shown to be of the asparagine-linked complex type composed of mannose-alpha 1-6-mannose-beta 1-4-N-acetylglucosamine-N-acetylglucosamine(alpha 1-6-fucose).
11180632	0	18	theme	protein	112:118	arg1	chains					41:46	the asparagine-linked sugar chains	13:46	the asparagine-linked sugar chains of porcine kidney and human urine cerebroside sulfate activator protein	13:118	Structure of the asparagine-linked sugar chains of porcine kidney and human urine cerebroside sulfate activator protein.
11180632	9	19	theme	class	1746:1750	arg1	members					1709:1715	other members	1703:1715	other members of the lipid-binding protein class to which cerebroside sulfate activator belongs	1703:1797	The procedures developed will be useful for sequencing other oligosaccharides including those from other members of the lipid-binding protein class to which cerebroside sulfate activator belongs.
11180632	6	20	theme	complex	1214:1220	arg1	type					1222:1225	the asparagine-linked complex type	1192:1225	the asparagine-linked complex type composed of mannose-alpha 1-6-mannose-beta 1-4-N-acetylglucosamine-N-acetylglucosamine(alpha 1-6-fucose)	1192:1330	The pentasaccharides from pig kidney and human urine protein were shown to be of the asparagine-linked complex type composed of mannose-alpha 1-6-mannose-beta 1-4-N-acetylglucosamine-N-acetylglucosamine(alpha 1-6-fucose).
11180632	5	21	theme	mass	1092:1095	arg1	spectrometry					1097:1108	mass spectrometry	1092:1108	mass spectrometry	1092:1108	The derivatized carbohydrates were then treated sequentially with a series of exoglycosidases of defined specificity, and the products of each digestion were examined by mass spectrometry.
11180632	8	22	theme	Oligosaccharide	1447:1461	arg1	sequencing					1463:1472	Oligosaccharide sequencing	1447:1472	Oligosaccharide sequencing by specific exoglycosidase degradation coupled with mass spectrometry	1447:1542	Oligosaccharide sequencing by specific exoglycosidase degradation coupled with mass spectrometry is more rapid than conventional oligosaccharide sequencing.
11180632	0	23	theme	activator	102:110	arg1	protein					112:118	human urine cerebroside sulfate activator protein	70:118	human urine cerebroside sulfate activator protein	70:118	Structure of the asparagine-linked sugar chains of porcine kidney and human urine cerebroside sulfate activator protein.
11180632	6	24	theme	mannose-alpha	1239:1251	arg1	1-6-fucose					1320:1329	alpha 1-6-fucose	1314:1329	alpha 1-6-fucose	1314:1329	The pentasaccharides from pig kidney and human urine protein were shown to be of the asparagine-linked complex type composed of mannose-alpha 1-6-mannose-beta 1-4-N-acetylglucosamine-N-acetylglucosamine(alpha 1-6-fucose).
11180632	6	24	theme	mannose-alpha	1239:1251	arg1	1-4-N-acetylglucosamine-N-acetylglucosamine					1270:1312	mannose-alpha 1-6-mannose-beta 1-4-N-acetylglucosamine-N-acetylglucosamine	1239:1312	mannose-alpha 1-6-mannose-beta 1-4-N-acetylglucosamine-N-acetylglucosamine(alpha 1-6-fucose)	1239:1330	The pentasaccharides from pig kidney and human urine protein were shown to be of the asparagine-linked complex type composed of mannose-alpha 1-6-mannose-beta 1-4-N-acetylglucosamine-N-acetylglucosamine(alpha 1-6-fucose).
11180632	6	25	from	protein	1164:1170	arg1	pentasaccharides					1115:1130	The pentasaccharides	1111:1130	The pentasaccharides from pig kidney and human urine protein	1111:1170	The pentasaccharides from pig kidney and human urine protein were shown to be of the asparagine-linked complex type composed of mannose-alpha 1-6-mannose-beta 1-4-N-acetylglucosamine-N-acetylglucosamine(alpha 1-6-fucose).
11180632	5	26	theme	defined	1019:1025	arg1	specificity					1027:1037	defined specificity	1019:1037	defined specificity	1019:1037	The derivatized carbohydrates were then treated sequentially with a series of exoglycosidases of defined specificity, and the products of each digestion were examined by mass spectrometry.
11180632	6	27	theme	asparagine-linked	1196:1212	arg1	type					1222:1225	the asparagine-linked complex type	1192:1225	the asparagine-linked complex type composed of mannose-alpha 1-6-mannose-beta 1-4-N-acetylglucosamine-N-acetylglucosamine(alpha 1-6-fucose)	1192:1330	The pentasaccharides from pig kidney and human urine protein were shown to be of the asparagine-linked complex type composed of mannose-alpha 1-6-mannose-beta 1-4-N-acetylglucosamine-N-acetylglucosamine(alpha 1-6-fucose).
11180632	2	28	theme	derivatives	427:437	arg1	digestion					386:394	Exhaustive sequential exoglycosidase digestion	349:394	Exhaustive sequential exoglycosidase digestion	349:394	Exhaustive sequential exoglycosidase digestion of the trimethyl-p-aminophenyl derivatives, followed by either matrix-assisted laser desorption/ionization and/or mass spectrometry, was used to define the residues and their linkages.
11180632	2	29	theme	mass	510:513	arg1	spectrometry					515:526	mass spectrometry	510:526	mass spectrometry	510:526	Exhaustive sequential exoglycosidase digestion of the trimethyl-p-aminophenyl derivatives, followed by either matrix-assisted laser desorption/ionization and/or mass spectrometry, was used to define the residues and their linkages.
11180632	4	30	theme	trimethyl-p-aminophenyl	827:849	arg1	derivative					851:860	the trimethyl-p-aminophenyl derivative	823:860	the trimethyl-p-aminophenyl derivative	823:860	Reducing termini were converted to the trimethyl-p-aminophenyl derivative and the samples were further purified by normal-phase HPLC.
11180632	3	31	attach	released	621:628	arg2	oligosaccharides					585:600	The oligosaccharides	581:600	The oligosaccharides	581:600	The oligosaccharides were enzymatically released from the proteins by treatment with peptidyl-N-glycosidase F and separated from the proteins by reversed-phase high-performance liquid chromatography (HPLC).
11180632	3	31	attach	released	621:628	arg1	proteins					639:646	the proteins	635:646	the proteins	635:646	The oligosaccharides were enzymatically released from the proteins by treatment with peptidyl-N-glycosidase F and separated from the proteins by reversed-phase high-performance liquid chromatography (HPLC).
11180632	2	32	theme	trimethyl-p-aminophenyl	403:425	arg1	derivatives					427:437	the trimethyl-p-aminophenyl derivatives	399:437	the trimethyl-p-aminophenyl derivatives	399:437	Exhaustive sequential exoglycosidase digestion of the trimethyl-p-aminophenyl derivatives, followed by either matrix-assisted laser desorption/ionization and/or mass spectrometry, was used to define the residues and their linkages.
11180632	7	33	theme	degraded	1345:1352	arg1	structure					1354:1362	This highly degraded structure	1333:1362	This highly degraded structure	1333:1362	This highly degraded structure probably represents the final product of intra-lysosomal exoglycosidase digestion.
11180632	9	34	theme	sulfate	1773:1779	arg1	activator					1781:1789	cerebroside sulfate activator	1761:1789	cerebroside sulfate activator	1761:1789	The procedures developed will be useful for sequencing other oligosaccharides including those from other members of the lipid-binding protein class to which cerebroside sulfate activator belongs.
11180632	0	35	theme	asparagine-linked	17:33	arg1	chains					41:46	the asparagine-linked sugar chains	13:46	the asparagine-linked sugar chains of porcine kidney and human urine cerebroside sulfate activator protein	13:118	Structure of the asparagine-linked sugar chains of porcine kidney and human urine cerebroside sulfate activator protein.
11180632	8	36	theme	mass	1526:1529	arg1	spectrometry					1531:1542	mass spectrometry	1526:1542	mass spectrometry	1526:1542	Oligosaccharide sequencing by specific exoglycosidase degradation coupled with mass spectrometry is more rapid than conventional oligosaccharide sequencing.
11180632	5	37	theme	digestion	1065:1073	arg1	products					1048:1055	the products	1044:1055	the products of each digestion	1044:1073	The derivatized carbohydrates were then treated sequentially with a series of exoglycosidases of defined specificity, and the products of each digestion were examined by mass spectrometry.
11180632	1	38	theme	pig	197:199	arg1	kidney					201:206	pig kidney	197:206	pig kidney	197:206	The specific sugar residues and their linkages in the oligosaccharides from pig kidney and human urine cerebroside sulfate activator proteins (saposin B), although previously hypothesized, have been unambiguously characterized.
11180632	2	39	theme	laser	475:479	arg1	desorption/ionization					481:501	matrix-assisted laser desorption/ionization	459:501	matrix-assisted laser desorption/ionization	459:501	Exhaustive sequential exoglycosidase digestion of the trimethyl-p-aminophenyl derivatives, followed by either matrix-assisted laser desorption/ionization and/or mass spectrometry, was used to define the residues and their linkages.
11180632	5	40	theme	specificity	1027:1037	arg1	exoglycosidases					1000:1014	exoglycosidases	1000:1014	exoglycosidases of defined specificity	1000:1037	The derivatized carbohydrates were then treated sequentially with a series of exoglycosidases of defined specificity, and the products of each digestion were examined by mass spectrometry.
11180632	1	41	theme	kidney	201:206	arg1	proteins					254:261	pig kidney and human urine cerebroside sulfate activator proteins	197:261	pig kidney and human urine cerebroside sulfate activator proteins (saposin B)	197:273	The specific sugar residues and their linkages in the oligosaccharides from pig kidney and human urine cerebroside sulfate activator proteins (saposin B), although previously hypothesized, have been unambiguously characterized.
11180632	1	41	theme	kidney	201:206	arg1	B					272:272	saposin B	264:272	saposin B	264:272	The specific sugar residues and their linkages in the oligosaccharides from pig kidney and human urine cerebroside sulfate activator proteins (saposin B), although previously hypothesized, have been unambiguously characterized.
11180632	0	42	theme	chains	41:46	arg1	Structure					0:8	Structure	0:8	Structure of the asparagine-linked sugar chains of porcine kidney and human urine cerebroside sulfate activator protein.	0:119	Structure of the asparagine-linked sugar chains of porcine kidney and human urine cerebroside sulfate activator protein.
11180632	1	43	dep	characterized	334:346	arg1	hypothesized					296:307	hypothesized	296:307	hypothesized	296:307	The specific sugar residues and their linkages in the oligosaccharides from pig kidney and human urine cerebroside sulfate activator proteins (saposin B), although previously hypothesized, have been unambiguously characterized.
11180632	1	44	from	proteins	254:261	arg1	oligosaccharides					175:190	the oligosaccharides	171:190	the oligosaccharides from pig kidney and human urine cerebroside sulfate activator proteins (saposin B)	171:273	The specific sugar residues and their linkages in the oligosaccharides from pig kidney and human urine cerebroside sulfate activator proteins (saposin B), although previously hypothesized, have been unambiguously characterized.
11180632	1	44	from	proteins	254:261	arg1	residues					140:147	The specific sugar residues	121:147	The specific sugar residues	121:147	The specific sugar residues and their linkages in the oligosaccharides from pig kidney and human urine cerebroside sulfate activator proteins (saposin B), although previously hypothesized, have been unambiguously characterized.
11180632	1	44	from	proteins	254:261	arg1	linkages					159:166	their linkages	153:166	their linkages	153:166	The specific sugar residues and their linkages in the oligosaccharides from pig kidney and human urine cerebroside sulfate activator proteins (saposin B), although previously hypothesized, have been unambiguously characterized.
11180632	3	45	theme	reversed-phase	726:739	arg1	HPLC					781:784	HPLC	781:784	HPLC	781:784	The oligosaccharides were enzymatically released from the proteins by treatment with peptidyl-N-glycosidase F and separated from the proteins by reversed-phase high-performance liquid chromatography (HPLC).
11180632	3	45	theme	reversed-phase	726:739	arg1	chromatography					765:778	reversed-phase high-performance liquid chromatography	726:778	reversed-phase high-performance liquid chromatography (HPLC)	726:785	The oligosaccharides were enzymatically released from the proteins by treatment with peptidyl-N-glycosidase F and separated from the proteins by reversed-phase high-performance liquid chromatography (HPLC).
11180632	8	46	theme	exoglycosidase	1486:1499	arg1	degradation					1501:1511	specific exoglycosidase degradation	1477:1511	specific exoglycosidase degradation coupled with mass spectrometry	1477:1542	Oligosaccharide sequencing by specific exoglycosidase degradation coupled with mass spectrometry is more rapid than conventional oligosaccharide sequencing.
11180632	0	47	theme	sugar	35:39	arg1	chains					41:46	the asparagine-linked sugar chains	13:46	the asparagine-linked sugar chains of porcine kidney and human urine cerebroside sulfate activator protein	13:118	Structure of the asparagine-linked sugar chains of porcine kidney and human urine cerebroside sulfate activator protein.
11180632	10	48	dep	&	1820:1820	arg1	c					1801:1801	c	1801:1801	c	1801:1801	(c) 2000 John Wiley & Sons, Ltd.
11180632	10	48	dep	&	1820:1820	arg1	Sons					1822:1825	Sons	1822:1825	Sons	1822:1825	(c) 2000 John Wiley & Sons, Ltd.
11180632	3	49	theme	peptidyl-N-glycosidase	666:687	arg1	F					689:689	peptidyl-N-glycosidase F	666:689	peptidyl-N-glycosidase F	666:689	The oligosaccharides were enzymatically released from the proteins by treatment with peptidyl-N-glycosidase F and separated from the proteins by reversed-phase high-performance liquid chromatography (HPLC).
11180632	1	50	theme	human	212:216	arg1	urine					218:222	human urine	212:222	human urine	212:222	The specific sugar residues and their linkages in the oligosaccharides from pig kidney and human urine cerebroside sulfate activator proteins (saposin B), although previously hypothesized, have been unambiguously characterized.
11180632	0	51	theme	porcine	51:57	arg1	kidney					59:64	porcine kidney	51:64	porcine kidney	51:64	Structure of the asparagine-linked sugar chains of porcine kidney and human urine cerebroside sulfate activator protein.
11180632	6	52	theme	urine	1158:1162	arg1	protein					1164:1170	human urine protein	1152:1170	human urine protein	1152:1170	The pentasaccharides from pig kidney and human urine protein were shown to be of the asparagine-linked complex type composed of mannose-alpha 1-6-mannose-beta 1-4-N-acetylglucosamine-N-acetylglucosamine(alpha 1-6-fucose).
11180632	7	53	theme	intra-lysosomal	1405:1419	arg1	digestion					1436:1444	intra-lysosomal exoglycosidase digestion	1405:1444	intra-lysosomal exoglycosidase digestion	1405:1444	This highly degraded structure probably represents the final product of intra-lysosomal exoglycosidase digestion.
11180632	9	54	theme	lipid-binding	1724:1736	arg1	class					1746:1750	the lipid-binding protein class	1720:1750	the lipid-binding protein class to which cerebroside sulfate activator belongs	1720:1797	The procedures developed will be useful for sequencing other oligosaccharides including those from other members of the lipid-binding protein class to which cerebroside sulfate activator belongs.
11180632	2	55	theme	Exhaustive	349:358	arg1	digestion					386:394	Exhaustive sequential exoglycosidase digestion	349:394	Exhaustive sequential exoglycosidase digestion	349:394	Exhaustive sequential exoglycosidase digestion of the trimethyl-p-aminophenyl derivatives, followed by either matrix-assisted laser desorption/ionization and/or mass spectrometry, was used to define the residues and their linkages.
11180632	9	56	theme	cerebroside	1761:1771	arg1	activator					1781:1789	cerebroside sulfate activator	1761:1789	cerebroside sulfate activator	1761:1789	The procedures developed will be useful for sequencing other oligosaccharides including those from other members of the lipid-binding protein class to which cerebroside sulfate activator belongs.
11180632	7	57	theme	digestion	1436:1444	arg1	product					1394:1400	the final product	1384:1400	the final product of intra-lysosomal exoglycosidase digestion	1384:1444	This highly degraded structure probably represents the final product of intra-lysosomal exoglycosidase digestion.
11180632	5	58	theme	derivatized	926:936	arg1	carbohydrates					938:950	The derivatized carbohydrates	922:950	The derivatized carbohydrates	922:950	The derivatized carbohydrates were then treated sequentially with a series of exoglycosidases of defined specificity, and the products of each digestion were examined by mass spectrometry.
11180632	3	59	with	treatment	651:659	arg1	F					689:689	peptidyl-N-glycosidase F	666:689	peptidyl-N-glycosidase F	666:689	The oligosaccharides were enzymatically released from the proteins by treatment with peptidyl-N-glycosidase F and separated from the proteins by reversed-phase high-performance liquid chromatography (HPLC).
11180632	6	60	theme	1-6-mannose-beta	1253:1268	arg1	1-6-fucose					1320:1329	alpha 1-6-fucose	1314:1329	alpha 1-6-fucose	1314:1329	The pentasaccharides from pig kidney and human urine protein were shown to be of the asparagine-linked complex type composed of mannose-alpha 1-6-mannose-beta 1-4-N-acetylglucosamine-N-acetylglucosamine(alpha 1-6-fucose).
11180632	6	60	theme	1-6-mannose-beta	1253:1268	arg1	1-4-N-acetylglucosamine-N-acetylglucosamine					1270:1312	mannose-alpha 1-6-mannose-beta 1-4-N-acetylglucosamine-N-acetylglucosamine	1239:1312	mannose-alpha 1-6-mannose-beta 1-4-N-acetylglucosamine-N-acetylglucosamine(alpha 1-6-fucose)	1239:1330	The pentasaccharides from pig kidney and human urine protein were shown to be of the asparagine-linked complex type composed of mannose-alpha 1-6-mannose-beta 1-4-N-acetylglucosamine-N-acetylglucosamine(alpha 1-6-fucose).
11180632	6	61	link	asparagine-linked	1196:1212	arg1	type					1222:1225	the asparagine-linked complex type	1192:1225	the asparagine-linked complex type composed of mannose-alpha 1-6-mannose-beta 1-4-N-acetylglucosamine-N-acetylglucosamine(alpha 1-6-fucose)	1192:1330	The pentasaccharides from pig kidney and human urine protein were shown to be of the asparagine-linked complex type composed of mannose-alpha 1-6-mannose-beta 1-4-N-acetylglucosamine-N-acetylglucosamine(alpha 1-6-fucose).
11180632	1	62	theme	specific	125:132	arg1	residues					140:147	The specific sugar residues	121:147	The specific sugar residues	121:147	The specific sugar residues and their linkages in the oligosaccharides from pig kidney and human urine cerebroside sulfate activator proteins (saposin B), although previously hypothesized, have been unambiguously characterized.
11180632	6	63	theme	alpha	1314:1318	arg1	1-6-fucose					1320:1329	alpha 1-6-fucose	1314:1329	alpha 1-6-fucose	1314:1329	The pentasaccharides from pig kidney and human urine protein were shown to be of the asparagine-linked complex type composed of mannose-alpha 1-6-mannose-beta 1-4-N-acetylglucosamine-N-acetylglucosamine(alpha 1-6-fucose).
11180632	6	63	theme	alpha	1314:1318	arg1	1-4-N-acetylglucosamine-N-acetylglucosamine					1270:1312	mannose-alpha 1-6-mannose-beta 1-4-N-acetylglucosamine-N-acetylglucosamine	1239:1312	mannose-alpha 1-6-mannose-beta 1-4-N-acetylglucosamine-N-acetylglucosamine(alpha 1-6-fucose)	1239:1330	The pentasaccharides from pig kidney and human urine protein were shown to be of the asparagine-linked complex type composed of mannose-alpha 1-6-mannose-beta 1-4-N-acetylglucosamine-N-acetylglucosamine(alpha 1-6-fucose).
11180632	1	64	theme	urine	218:222	arg1	proteins					254:261	pig kidney and human urine cerebroside sulfate activator proteins	197:261	pig kidney and human urine cerebroside sulfate activator proteins (saposin B)	197:273	The specific sugar residues and their linkages in the oligosaccharides from pig kidney and human urine cerebroside sulfate activator proteins (saposin B), although previously hypothesized, have been unambiguously characterized.
11180632	1	64	theme	urine	218:222	arg1	B					272:272	saposin B	264:272	saposin B	264:272	The specific sugar residues and their linkages in the oligosaccharides from pig kidney and human urine cerebroside sulfate activator proteins (saposin B), although previously hypothesized, have been unambiguously characterized.
11180632	8	65	theme	oligosaccharide	1576:1590	arg1	sequencing					1592:1601	conventional oligosaccharide sequencing	1563:1601	conventional oligosaccharide sequencing	1563:1601	Oligosaccharide sequencing by specific exoglycosidase degradation coupled with mass spectrometry is more rapid than conventional oligosaccharide sequencing.
11180632	3	66	theme	high-performance	741:756	arg1	HPLC					781:784	HPLC	781:784	HPLC	781:784	The oligosaccharides were enzymatically released from the proteins by treatment with peptidyl-N-glycosidase F and separated from the proteins by reversed-phase high-performance liquid chromatography (HPLC).
11180632	3	66	theme	high-performance	741:756	arg1	chromatography					765:778	reversed-phase high-performance liquid chromatography	726:778	reversed-phase high-performance liquid chromatography (HPLC)	726:785	The oligosaccharides were enzymatically released from the proteins by treatment with peptidyl-N-glycosidase F and separated from the proteins by reversed-phase high-performance liquid chromatography (HPLC).
11180632	1	67	theme	sugar	134:138	arg1	residues					140:147	The specific sugar residues	121:147	The specific sugar residues	121:147	The specific sugar residues and their linkages in the oligosaccharides from pig kidney and human urine cerebroside sulfate activator proteins (saposin B), although previously hypothesized, have been unambiguously characterized.
11180632	1	68	theme	cerebroside	224:234	arg1	proteins					254:261	pig kidney and human urine cerebroside sulfate activator proteins	197:261	pig kidney and human urine cerebroside sulfate activator proteins (saposin B)	197:273	The specific sugar residues and their linkages in the oligosaccharides from pig kidney and human urine cerebroside sulfate activator proteins (saposin B), although previously hypothesized, have been unambiguously characterized.
11180632	1	68	theme	cerebroside	224:234	arg1	B					272:272	saposin B	264:272	saposin B	264:272	The specific sugar residues and their linkages in the oligosaccharides from pig kidney and human urine cerebroside sulfate activator proteins (saposin B), although previously hypothesized, have been unambiguously characterized.
11180632	9	69	theme	protein	1738:1744	arg1	class					1746:1750	the lipid-binding protein class	1720:1750	the lipid-binding protein class to which cerebroside sulfate activator belongs	1720:1797	The procedures developed will be useful for sequencing other oligosaccharides including those from other members of the lipid-binding protein class to which cerebroside sulfate activator belongs.
11180632	3	70	theme	liquid	758:763	arg1	HPLC					781:784	HPLC	781:784	HPLC	781:784	The oligosaccharides were enzymatically released from the proteins by treatment with peptidyl-N-glycosidase F and separated from the proteins by reversed-phase high-performance liquid chromatography (HPLC).
11180632	3	70	theme	liquid	758:763	arg1	chromatography					765:778	reversed-phase high-performance liquid chromatography	726:778	reversed-phase high-performance liquid chromatography (HPLC)	726:785	The oligosaccharides were enzymatically released from the proteins by treatment with peptidyl-N-glycosidase F and separated from the proteins by reversed-phase high-performance liquid chromatography (HPLC).
11180632	8	71	theme	specific	1477:1484	arg1	degradation					1501:1511	specific exoglycosidase degradation	1477:1511	specific exoglycosidase degradation coupled with mass spectrometry	1477:1542	Oligosaccharide sequencing by specific exoglycosidase degradation coupled with mass spectrometry is more rapid than conventional oligosaccharide sequencing.
11180632	2	72	theme	matrix-assisted	459:473	arg1	desorption/ionization					481:501	matrix-assisted laser desorption/ionization	459:501	matrix-assisted laser desorption/ionization	459:501	Exhaustive sequential exoglycosidase digestion of the trimethyl-p-aminophenyl derivatives, followed by either matrix-assisted laser desorption/ionization and/or mass spectrometry, was used to define the residues and their linkages.
11180632	5	73	theme	exoglycosidases	1000:1014	arg1	series					990:995	a series	988:995	a series of exoglycosidases of defined specificity	988:1037	The derivatized carbohydrates were then treated sequentially with a series of exoglycosidases of defined specificity, and the products of each digestion were examined by mass spectrometry.
11180632	1	74	theme	sulfate	236:242	arg1	proteins					254:261	pig kidney and human urine cerebroside sulfate activator proteins	197:261	pig kidney and human urine cerebroside sulfate activator proteins (saposin B)	197:273	The specific sugar residues and their linkages in the oligosaccharides from pig kidney and human urine cerebroside sulfate activator proteins (saposin B), although previously hypothesized, have been unambiguously characterized.
11180632	1	74	theme	sulfate	236:242	arg1	B					272:272	saposin B	264:272	saposin B	264:272	The specific sugar residues and their linkages in the oligosaccharides from pig kidney and human urine cerebroside sulfate activator proteins (saposin B), although previously hypothesized, have been unambiguously characterized.
11180632	0	75	theme	kidney	59:64	arg1	chains					41:46	the asparagine-linked sugar chains	13:46	the asparagine-linked sugar chains of porcine kidney and human urine cerebroside sulfate activator protein	13:118	Structure of the asparagine-linked sugar chains of porcine kidney and human urine cerebroside sulfate activator protein.
11180632	9	76	theme	other	1703:1707	arg1	members					1709:1715	other members	1703:1715	other members of the lipid-binding protein class to which cerebroside sulfate activator belongs	1703:1797	The procedures developed will be useful for sequencing other oligosaccharides including those from other members of the lipid-binding protein class to which cerebroside sulfate activator belongs.
11180632	4	77	theme	normal-phase	903:914	arg1	HPLC					916:919	normal-phase HPLC	903:919	normal-phase HPLC	903:919	Reducing termini were converted to the trimethyl-p-aminophenyl derivative and the samples were further purified by normal-phase HPLC.
11180632	6	78	theme	human	1152:1156	arg1	protein					1164:1170	human urine protein	1152:1170	human urine protein	1152:1170	The pentasaccharides from pig kidney and human urine protein were shown to be of the asparagine-linked complex type composed of mannose-alpha 1-6-mannose-beta 1-4-N-acetylglucosamine-N-acetylglucosamine(alpha 1-6-fucose).
11180632	7	79	theme	exoglycosidase	1421:1434	arg1	digestion					1436:1444	intra-lysosomal exoglycosidase digestion	1405:1444	intra-lysosomal exoglycosidase digestion	1405:1444	This highly degraded structure probably represents the final product of intra-lysosomal exoglycosidase digestion.
11180632	1	80	theme	activator	244:252	arg1	proteins					254:261	pig kidney and human urine cerebroside sulfate activator proteins	197:261	pig kidney and human urine cerebroside sulfate activator proteins (saposin B)	197:273	The specific sugar residues and their linkages in the oligosaccharides from pig kidney and human urine cerebroside sulfate activator proteins (saposin B), although previously hypothesized, have been unambiguously characterized.
11180632	1	80	theme	activator	244:252	arg1	B					272:272	saposin B	264:272	saposin B	264:272	The specific sugar residues and their linkages in the oligosaccharides from pig kidney and human urine cerebroside sulfate activator proteins (saposin B), although previously hypothesized, have been unambiguously characterized.
10441114	6	0	theme	semiquantitative	938:953	arg1	technique					1009:1017	the semiquantitative HPLC-electrospray ionization mass spectrometry (ESMS) technique	934:1017	the semiquantitative HPLC-electrospray ionization mass spectrometry (ESMS) technique after exoglycosidase hydrolysis	934:1049	Carbohydrate analyses were performed via the semiquantitative HPLC-electrospray ionization mass spectrometry (ESMS) technique after exoglycosidase hydrolysis.
10441114	5	1	from	T	748:748	arg1	O-glycosylated					730:743	O-glycosylated	730:743	O-glycosylated	730:743	These polypetides are found to be O-glycosylated at T(125) (residue 9) with a glycan structure of the mucin type consisting of galactose N-acetylgalactosamine and N-acetylneuraminic acid residues.
10441114	4	2	theme	noncollagenous	632:645	arg1	collagen					666:673	collagen XVIII	666:679	collagen XVIII	666:679	lacking the last and final three residues of the noncollagenous domain 1 (NC-1) of collagen XVIII, respectively.
10441114	4	2	theme	noncollagenous	632:645	arg1	domain					647:652	noncollagenous domain 1	632:654	the noncollagenous domain 1 (NC-1) of collagen XVIII	628:679	lacking the last and final three residues of the noncollagenous domain 1 (NC-1) of collagen XVIII, respectively.
10441114	4	2	theme	noncollagenous	632:645	arg1	NC-1					657:660	NC-1	657:660	NC-1	657:660	lacking the last and final three residues of the noncollagenous domain 1 (NC-1) of collagen XVIII, respectively.
10441114	8	3	theme	NC-1	1403:1406	arg1	collagen					1418:1425	collagen XVIII	1418:1431	collagen XVIII	1418:1431	The described glycosylated endostatins may represent intermediates in the proteolytic pathway of the NC-1 domain of collagen XVIII resulting in bioactive endostatins.
10441114	8	3	theme	NC-1	1403:1406	arg1	domain					1408:1413	the NC-1 domain	1399:1413	the NC-1 domain of collagen XVIII	1399:1431	The described glycosylated endostatins may represent intermediates in the proteolytic pathway of the NC-1 domain of collagen XVIII resulting in bioactive endostatins.
10441114	7	4	theme	asialoglycoprotein	1146:1163	arg1	structures					1165:1174	sialoglycoprotein (22 000 and 21 841 Da +/- 0.02%) and asialoglycoprotein structures	1091:1174	structures	1165:1174	Circulating endostatins are present as sialoglycoprotein (22 000 and 21 841 Da +/- 0.02%) and asialoglycoprotein structures (21 710 and 21 549 Da +/- 0.02%), while the two completely deglycosylated forms are obtained only after enzymatic incubation.
10441114	8	5	theme	described	1306:1314	arg1	endostatins					1329:1339	The described glycosylated endostatins	1302:1339	The described glycosylated endostatins	1302:1339	The described glycosylated endostatins may represent intermediates in the proteolytic pathway of the NC-1 domain of collagen XVIII resulting in bioactive endostatins.
10441114	5	6	theme	glycan	774:779	arg1	structure					781:789	a glycan structure	772:789	a glycan structure of the mucin type consisting of galactose N-acetylgalactosamine and N-acetylneuraminic acid residues	772:890	These polypetides are found to be O-glycosylated at T(125) (residue 9) with a glycan structure of the mucin type consisting of galactose N-acetylgalactosamine and N-acetylneuraminic acid residues.
10441114	2	7	theme	polyclonal	300:309	arg1	antiserum					318:326	a polyclonal rabbit antiserum	298:326	a polyclonal rabbit antiserum raised against an N-terminal epitope of the polypeptide	298:382	Immunoreactive endostatin was identified by a polyclonal rabbit antiserum raised against an N-terminal epitope of the polypeptide and purified by consecutive chromatographic steps and immunoblotting.
10441114	1	8	theme	drug	197:200	arg1	forms					135:139	Circulating elongated forms	113:139	Circulating elongated forms of the angiogenesis inhibitor and potential anti-cancer drug endostatin	113:211	Circulating elongated forms of the angiogenesis inhibitor and potential anti-cancer drug endostatin were isolated from human blood filtrate.
10441114	6	9	theme	Carbohydrate	893:904	arg1	analyses					906:913	Carbohydrate analyses	893:913	Carbohydrate analyses	893:913	Carbohydrate analyses were performed via the semiquantitative HPLC-electrospray ionization mass spectrometry (ESMS) technique after exoglycosidase hydrolysis.
10441114	2	10	theme	N-terminal	346:355	arg1	epitope					357:363	an N-terminal epitope	343:363	an N-terminal epitope of the polypeptide	343:382	Immunoreactive endostatin was identified by a polyclonal rabbit antiserum raised against an N-terminal epitope of the polypeptide and purified by consecutive chromatographic steps and immunoblotting.
10441114	9	11	theme	C-terminal	1516:1525	arg1	fragments					1527:1535	immunoreactive endostatin-related C-terminal fragments	1482:1535	immunoreactive endostatin-related C-terminal fragments of human collagen XV	1482:1556	Furthermore, immunoreactive endostatin-related C-terminal fragments of human collagen XV are found in the hemofiltrate.
10441114	8	12	theme	glycosylated	1316:1327	arg1	endostatins					1329:1339	The described glycosylated endostatins	1302:1339	The described glycosylated endostatins	1302:1339	The described glycosylated endostatins may represent intermediates in the proteolytic pathway of the NC-1 domain of collagen XVIII resulting in bioactive endostatins.
10441114	14	13	theme	homology	1850:1857	arg1	degree					1840:1845	the high degree	1831:1845	the high degree of homology between collagen XV and collagen XVIII as well as their analoqous proteolytic processing	1831:1946	Due to the high degree of homology between collagen XV and collagen XVIII as well as their analoqous proteolytic processing, functional similarities of collagen XVIII- and XV-related fragments should be revealed in future experiments.
10441114	14	13	theme	homology	1850:1857	arg1	processing					1937:1946	their analoqous proteolytic processing	1909:1946	the high degree of homology between collagen XV and collagen XVIII as well as their analoqous proteolytic processing	1831:1946	Due to the high degree of homology between collagen XV and collagen XVIII as well as their analoqous proteolytic processing, functional similarities of collagen XVIII- and XV-related fragments should be revealed in future experiments.
10441114	14	14	theme	fragments	2007:2015	arg1	similarities					1960:1971	functional similarities	1949:1971	functional similarities of collagen XVIII- and XV-related fragments	1949:2015	Due to the high degree of homology between collagen XV and collagen XVIII as well as their analoqous proteolytic processing, functional similarities of collagen XVIII- and XV-related fragments should be revealed in future experiments.
10441114	7	15	gly	asialoglycoprotein	1146:1163	arg1	asialoglycoprotein					1146:1163	sialoglycoprotein (22 000 and 21 841 Da +/- 0.02%) and asialoglycoprotein structures	1091:1174	asialoglycoprotein	1146:1163	Circulating endostatins are present as sialoglycoprotein (22 000 and 21 841 Da +/- 0.02%) and asialoglycoprotein structures (21 710 and 21 549 Da +/- 0.02%), while the two completely deglycosylated forms are obtained only after enzymatic incubation.
10441114	2	16	theme	Immunoreactive	254:267	arg1	endostatin					269:278	Immunoreactive endostatin	254:278	Immunoreactive endostatin	254:278	Immunoreactive endostatin was identified by a polyclonal rabbit antiserum raised against an N-terminal epitope of the polypeptide and purified by consecutive chromatographic steps and immunoblotting.
10441114	9	17	theme	collagen	1546:1553	arg1	XV					1555:1556	human collagen XV	1540:1556	human collagen XV	1540:1556	Furthermore, immunoreactive endostatin-related C-terminal fragments of human collagen XV are found in the hemofiltrate.
10441114	6	18	theme	spectrometry	989:1000	arg1	technique					1009:1017	the semiquantitative HPLC-electrospray ionization mass spectrometry (ESMS) technique	934:1017	the semiquantitative HPLC-electrospray ionization mass spectrometry (ESMS) technique after exoglycosidase hydrolysis	934:1049	Carbohydrate analyses were performed via the semiquantitative HPLC-electrospray ionization mass spectrometry (ESMS) technique after exoglycosidase hydrolysis.
10441114	5	19	gly	O-glycosylated	730:743	arg2	T					748:748	T	748:748	T(125) (residue 9)	748:765	These polypetides are found to be O-glycosylated at T(125) (residue 9) with a glycan structure of the mucin type consisting of galactose N-acetylgalactosamine and N-acetylneuraminic acid residues.
10441114	5	19	gly	O-glycosylated	730:743	arg1	polypetides					702:712	These polypetides	696:712	These polypetides	696:712	These polypetides are found to be O-glycosylated at T(125) (residue 9) with a glycan structure of the mucin type consisting of galactose N-acetylgalactosamine and N-acetylneuraminic acid residues.
10441114	5	19	gly	O-glycosylated	730:743	arg2	residue					756:762	residue 9	756:764	residue 9	756:764	These polypetides are found to be O-glycosylated at T(125) (residue 9) with a glycan structure of the mucin type consisting of galactose N-acetylgalactosamine and N-acetylneuraminic acid residues.
10441114	5	19	gly	O-glycosylated	730:743	arg2	125					750:752	125	750:752	125	750:752	These polypetides are found to be O-glycosylated at T(125) (residue 9) with a glycan structure of the mucin type consisting of galactose N-acetylgalactosamine and N-acetylneuraminic acid residues.
10441114	13	20	theme	molecular	1782:1790	arg1	mass					1792:1795	a molecular mass	1780:1795	a molecular mass ranging from 16 to 21 kDa	1780:1821	ESMS and immunoblotting analyses reveal three glycosylated polypeptides with a molecular mass ranging from 16 to 21 kDa.
10441114	6	21	theme	ionization	973:982	arg1	spectrometry					989:1000	HPLC-electrospray ionization mass spectrometry	955:1000	the semiquantitative HPLC-electrospray ionization mass spectrometry (ESMS) technique after exoglycosidase hydrolysis	934:1049	Carbohydrate analyses were performed via the semiquantitative HPLC-electrospray ionization mass spectrometry (ESMS) technique after exoglycosidase hydrolysis.
10441114	6	21	theme	ionization	973:982	arg1	ESMS					1003:1006	ESMS	1003:1006	ESMS	1003:1006	Carbohydrate analyses were performed via the semiquantitative HPLC-electrospray ionization mass spectrometry (ESMS) technique after exoglycosidase hydrolysis.
10441114	14	22	theme	collagen	1867:1874	arg1	XV					1876:1877	collagen XV	1867:1877	collagen XV	1867:1877	Due to the high degree of homology between collagen XV and collagen XVIII as well as their analoqous proteolytic processing, functional similarities of collagen XVIII- and XV-related fragments should be revealed in future experiments.
10441114	13	23	gly	glycosylated	1749:1760	arg1	polypeptides					1762:1773	three glycosylated polypeptides	1743:1773	three glycosylated polypeptides	1743:1773	ESMS and immunoblotting analyses reveal three glycosylated polypeptides with a molecular mass ranging from 16 to 21 kDa.
10441114	7	24	theme	deglycosylated	1235:1248	arg1	forms					1250:1254	the two completely deglycosylated forms	1216:1254	the two completely deglycosylated forms	1216:1254	Circulating endostatins are present as sialoglycoprotein (22 000 and 21 841 Da +/- 0.02%) and asialoglycoprotein structures (21 710 and 21 549 Da +/- 0.02%), while the two completely deglycosylated forms are obtained only after enzymatic incubation.
10441114	1	25	theme	inhibitor	161:169	arg1	forms					135:139	Circulating elongated forms	113:139	Circulating elongated forms of the angiogenesis inhibitor and potential anti-cancer drug endostatin	113:211	Circulating elongated forms of the angiogenesis inhibitor and potential anti-cancer drug endostatin were isolated from human blood filtrate.
10441114	8	26	gly	glycosylated	1316:1327	arg1	endostatins					1329:1339	The described glycosylated endostatins	1302:1339	The described glycosylated endostatins	1302:1339	The described glycosylated endostatins may represent intermediates in the proteolytic pathway of the NC-1 domain of collagen XVIII resulting in bioactive endostatins.
10441114	1	27	theme	potential	175:183	arg1	drug					197:200	potential anti-cancer drug	175:200	potential anti-cancer drug	175:200	Circulating elongated forms of the angiogenesis inhibitor and potential anti-cancer drug endostatin were isolated from human blood filtrate.
10441114	8	28	theme	proteolytic	1376:1386	arg1	pathway					1388:1394	the proteolytic pathway	1372:1394	the proteolytic pathway of the NC-1 domain of collagen XVIII resulting in bioactive endostatins	1372:1466	The described glycosylated endostatins may represent intermediates in the proteolytic pathway of the NC-1 domain of collagen XVIII resulting in bioactive endostatins.
10441114	1	29	dep	inhibitor	161:169	arg1	endostatin					202:211	endostatin	202:211	endostatin	202:211	Circulating elongated forms of the angiogenesis inhibitor and potential anti-cancer drug endostatin were isolated from human blood filtrate.
10441114	0	30	theme	collagen	100:107	arg1	forms					19:23	Novel glycosylated forms	0:23	Novel glycosylated forms of human plasma endostatin	0:50	Novel glycosylated forms of human plasma endostatin and circulating endostatin-related fragments of collagen XV.
10441114	0	30	theme	collagen	100:107	arg1	fragments					87:95	circulating endostatin-related fragments	56:95	circulating endostatin-related fragments of collagen XV	56:110	Novel glycosylated forms of human plasma endostatin and circulating endostatin-related fragments of collagen XV.
10441114	12	31	theme	XV	1687:1688	arg1	domain					1695:1700	the collagen XV NC-1 domain	1674:1700	the collagen XV NC-1 domain	1674:1700	of the collagen XV NC-1 domain.
10441114	6	32	theme	exoglycosidase	1025:1038	arg1	hydrolysis					1040:1049	exoglycosidase hydrolysis	1025:1049	exoglycosidase hydrolysis	1025:1049	Carbohydrate analyses were performed via the semiquantitative HPLC-electrospray ionization mass spectrometry (ESMS) technique after exoglycosidase hydrolysis.
10441114	7	33	gly	deglycosylated	1235:1248	arg1	forms					1250:1254	the two completely deglycosylated forms	1216:1254	the two completely deglycosylated forms	1216:1254	Circulating endostatins are present as sialoglycoprotein (22 000 and 21 841 Da +/- 0.02%) and asialoglycoprotein structures (21 710 and 21 549 Da +/- 0.02%), while the two completely deglycosylated forms are obtained only after enzymatic incubation.
10441114	0	34	theme	Novel	0:4	arg1	forms					19:23	Novel glycosylated forms	0:23	Novel glycosylated forms of human plasma endostatin	0:50	Novel glycosylated forms of human plasma endostatin and circulating endostatin-related fragments of collagen XV.
10441114	14	35	theme	high	1835:1838	arg1	degree					1840:1845	the high degree	1831:1845	the high degree of homology between collagen XV and collagen XVIII as well as their analoqous proteolytic processing	1831:1946	Due to the high degree of homology between collagen XV and collagen XVIII as well as their analoqous proteolytic processing, functional similarities of collagen XVIII- and XV-related fragments should be revealed in future experiments.
10441114	3	36	theme	different	525:533	arg1	forms					535:539	different forms	525:539	different forms of endostatin starting with V(117)HLRPAR	525:580	N- and C-terminal sequence analyses of the isolated molecules revealed different forms of endostatin starting with V(117)HLRPAR.
10441114	1	37	theme	Circulating	113:123	arg1	forms					135:139	Circulating elongated forms	113:139	Circulating elongated forms of the angiogenesis inhibitor and potential anti-cancer drug endostatin	113:211	Circulating elongated forms of the angiogenesis inhibitor and potential anti-cancer drug endostatin were isolated from human blood filtrate.
10441114	3	38	theme	C-terminal	461:470	arg1	sequence					472:479	C-terminal sequence	461:479	C-terminal sequence	461:479	N- and C-terminal sequence analyses of the isolated molecules revealed different forms of endostatin starting with V(117)HLRPAR.
10441114	4	39	theme	final	604:608	arg1	residues					616:623	the last and final three residues	591:623	residues	616:623	lacking the last and final three residues of the noncollagenous domain 1 (NC-1) of collagen XVIII, respectively.
10441114	3	40	theme	molecules	506:514	arg1	analyses					481:488	N- and C-terminal sequence analyses	454:488	N- and C-terminal sequence analyses of the isolated molecules	454:514	N- and C-terminal sequence analyses of the isolated molecules revealed different forms of endostatin starting with V(117)HLRPAR.
10441114	5	41	theme	N-acetylneuraminic	859:876	arg1	acid					878:881	N-acetylneuraminic acid	859:881	N-acetylneuraminic acid	859:881	These polypetides are found to be O-glycosylated at T(125) (residue 9) with a glycan structure of the mucin type consisting of galactose N-acetylgalactosamine and N-acetylneuraminic acid residues.
10441114	0	42	theme	human	28:32	arg1	endostatin					41:50	human plasma endostatin	28:50	human plasma endostatin	28:50	Novel glycosylated forms of human plasma endostatin and circulating endostatin-related fragments of collagen XV.
10441114	0	43	gly	glycosylated	6:17	arg1	forms					19:23	Novel glycosylated forms	0:23	Novel glycosylated forms of human plasma endostatin	0:50	Novel glycosylated forms of human plasma endostatin and circulating endostatin-related fragments of collagen XV.
10441114	0	43	gly	glycosylated	6:17	arg1	endostatin					41:50	human plasma endostatin	28:50	human plasma endostatin	28:50	Novel glycosylated forms of human plasma endostatin and circulating endostatin-related fragments of collagen XV.
10441114	0	43	gly	glycosylated	6:17	arg1	collagen					100:107	collagen XV	100:110	collagen XV	100:110	Novel glycosylated forms of human plasma endostatin and circulating endostatin-related fragments of collagen XV.
10441114	5	44	with	O-glycosylated	730:743	arg1	structure					781:789	a glycan structure	772:789	a glycan structure of the mucin type consisting of galactose N-acetylgalactosamine and N-acetylneuraminic acid residues	772:890	These polypetides are found to be O-glycosylated at T(125) (residue 9) with a glycan structure of the mucin type consisting of galactose N-acetylgalactosamine and N-acetylneuraminic acid residues.
10441114	3	45	theme	N-	454:455	arg1	analyses					481:488	N- and C-terminal sequence analyses	454:488	N- and C-terminal sequence analyses of the isolated molecules	454:514	N- and C-terminal sequence analyses of the isolated molecules revealed different forms of endostatin starting with V(117)HLRPAR.
10441114	0	46	theme	circulating	56:66	arg1	fragments					87:95	circulating endostatin-related fragments	56:95	circulating endostatin-related fragments of collagen XV	56:110	Novel glycosylated forms of human plasma endostatin and circulating endostatin-related fragments of collagen XV.
10441114	0	47	theme	endostatin	41:50	arg1	forms					19:23	Novel glycosylated forms	0:23	Novel glycosylated forms of human plasma endostatin	0:50	Novel glycosylated forms of human plasma endostatin and circulating endostatin-related fragments of collagen XV.
10441114	0	47	theme	endostatin	41:50	arg1	fragments					87:95	circulating endostatin-related fragments	56:95	circulating endostatin-related fragments of collagen XV	56:110	Novel glycosylated forms of human plasma endostatin and circulating endostatin-related fragments of collagen XV.
10441114	14	48	theme	collagen	1976:1983	arg1	fragments					2007:2015	collagen XVIII- and XV-related fragments	1976:2015	collagen XVIII- and XV-related fragments	1976:2015	Due to the high degree of homology between collagen XV and collagen XVIII as well as their analoqous proteolytic processing, functional similarities of collagen XVIII- and XV-related fragments should be revealed in future experiments.
10441114	1	49	attach	isolated	218:225	arg1	filtrate					244:251	human blood filtrate	232:251	human blood filtrate	232:251	Circulating elongated forms of the angiogenesis inhibitor and potential anti-cancer drug endostatin were isolated from human blood filtrate.
10441114	1	49	attach	isolated	218:225	arg2	forms					135:139	Circulating elongated forms	113:139	Circulating elongated forms of the angiogenesis inhibitor and potential anti-cancer drug endostatin	113:211	Circulating elongated forms of the angiogenesis inhibitor and potential anti-cancer drug endostatin were isolated from human blood filtrate.
10441114	13	50	dep	21	1816:1817	arg1	to					1813:1814	to	1813:1814	to	1813:1814	ESMS and immunoblotting analyses reveal three glycosylated polypeptides with a molecular mass ranging from 16 to 21 kDa.
10441114	7	51	theme	enzymatic	1280:1288	arg1	incubation					1290:1299	enzymatic incubation	1280:1299	enzymatic incubation	1280:1299	Circulating endostatins are present as sialoglycoprotein (22 000 and 21 841 Da +/- 0.02%) and asialoglycoprotein structures (21 710 and 21 549 Da +/- 0.02%), while the two completely deglycosylated forms are obtained only after enzymatic incubation.
10441114	4	52	theme	domain	647:652	arg1	last					595:598	last	595:598	last	595:598	lacking the last and final three residues of the noncollagenous domain 1 (NC-1) of collagen XVIII, respectively.
10441114	10	53	theme	N-terminal	1620:1629	arg1	sequences					1631:1639	the N-terminal sequences	1616:1639	the N-terminal sequences P(66)HLLPPP	1616:1651	These polypeptides exhibit the N-terminal sequences P(66)HLLPPP.
10441114	2	54	theme	chromatographic	412:426	arg1	steps					428:432	consecutive chromatographic steps	400:432	consecutive chromatographic steps	400:432	Immunoreactive endostatin was identified by a polyclonal rabbit antiserum raised against an N-terminal epitope of the polypeptide and purified by consecutive chromatographic steps and immunoblotting.
10441114	9	55	theme	immunoreactive	1482:1495	arg1	fragments					1527:1535	immunoreactive endostatin-related C-terminal fragments	1482:1535	immunoreactive endostatin-related C-terminal fragments of human collagen XV	1482:1556	Furthermore, immunoreactive endostatin-related C-terminal fragments of human collagen XV are found in the hemofiltrate.
10441114	6	56	theme	HPLC-electrospray	955:971	arg1	spectrometry					989:1000	HPLC-electrospray ionization mass spectrometry	955:1000	the semiquantitative HPLC-electrospray ionization mass spectrometry (ESMS) technique after exoglycosidase hydrolysis	934:1049	Carbohydrate analyses were performed via the semiquantitative HPLC-electrospray ionization mass spectrometry (ESMS) technique after exoglycosidase hydrolysis.
10441114	6	56	theme	HPLC-electrospray	955:971	arg1	ESMS					1003:1006	ESMS	1003:1006	ESMS	1003:1006	Carbohydrate analyses were performed via the semiquantitative HPLC-electrospray ionization mass spectrometry (ESMS) technique after exoglycosidase hydrolysis.
10441114	3	57	theme	V	569:569	arg1	HLRPAR					575:580	V(117)HLRPAR	569:580	V(117)HLRPAR	569:580	N- and C-terminal sequence analyses of the isolated molecules revealed different forms of endostatin starting with V(117)HLRPAR.
10441114	14	58	theme	proteolytic	1925:1935	arg1	processing					1937:1946	their analoqous proteolytic processing	1909:1946	the high degree of homology between collagen XV and collagen XVIII as well as their analoqous proteolytic processing	1831:1946	Due to the high degree of homology between collagen XV and collagen XVIII as well as their analoqous proteolytic processing, functional similarities of collagen XVIII- and XV-related fragments should be revealed in future experiments.
10441114	9	59	theme	XV	1555:1556	arg1	fragments					1527:1535	immunoreactive endostatin-related C-terminal fragments	1482:1535	immunoreactive endostatin-related C-terminal fragments of human collagen XV	1482:1556	Furthermore, immunoreactive endostatin-related C-terminal fragments of human collagen XV are found in the hemofiltrate.
10441114	7	60	dep	sialoglycoprotein	1091:1107	arg1	Da					1195:1196	21 710 and 21 549 Da +/- 0.02%	1177:1206	Da	1195:1196	Circulating endostatins are present as sialoglycoprotein (22 000 and 21 841 Da +/- 0.02%) and asialoglycoprotein structures (21 710 and 21 549 Da +/- 0.02%), while the two completely deglycosylated forms are obtained only after enzymatic incubation.
10441114	7	60	dep	sialoglycoprotein	1091:1107	arg1	000					1113:1115	22 000 and 21 841 Da +/- 0.02%	1110:1139	000	1113:1115	Circulating endostatins are present as sialoglycoprotein (22 000 and 21 841 Da +/- 0.02%) and asialoglycoprotein structures (21 710 and 21 549 Da +/- 0.02%), while the two completely deglycosylated forms are obtained only after enzymatic incubation.
10441114	7	60	dep	sialoglycoprotein	1091:1107	arg1	%					1139:1139	22 000 and 21 841 Da +/- 0.02%	1110:1139	%	1139:1139	Circulating endostatins are present as sialoglycoprotein (22 000 and 21 841 Da +/- 0.02%) and asialoglycoprotein structures (21 710 and 21 549 Da +/- 0.02%), while the two completely deglycosylated forms are obtained only after enzymatic incubation.
10441114	7	60	dep	sialoglycoprotein	1091:1107	arg1	710					1180:1182	21 710 and 21 549 Da +/- 0.02%	1177:1206	710	1180:1182	Circulating endostatins are present as sialoglycoprotein (22 000 and 21 841 Da +/- 0.02%) and asialoglycoprotein structures (21 710 and 21 549 Da +/- 0.02%), while the two completely deglycosylated forms are obtained only after enzymatic incubation.
10441114	7	60	dep	sialoglycoprotein	1091:1107	arg1	%					1206:1206	21 710 and 21 549 Da +/- 0.02%	1177:1206	%	1206:1206	Circulating endostatins are present as sialoglycoprotein (22 000 and 21 841 Da +/- 0.02%) and asialoglycoprotein structures (21 710 and 21 549 Da +/- 0.02%), while the two completely deglycosylated forms are obtained only after enzymatic incubation.
10441114	7	60	dep	sialoglycoprotein	1091:1107	arg1	Da					1128:1129	22 000 and 21 841 Da +/- 0.02%	1110:1139	Da	1128:1129	Circulating endostatins are present as sialoglycoprotein (22 000 and 21 841 Da +/- 0.02%) and asialoglycoprotein structures (21 710 and 21 549 Da +/- 0.02%), while the two completely deglycosylated forms are obtained only after enzymatic incubation.
10441114	2	61	theme	rabbit	311:316	arg1	antiserum					318:326	a polyclonal rabbit antiserum	298:326	a polyclonal rabbit antiserum raised against an N-terminal epitope of the polypeptide	298:382	Immunoreactive endostatin was identified by a polyclonal rabbit antiserum raised against an N-terminal epitope of the polypeptide and purified by consecutive chromatographic steps and immunoblotting.
10441114	14	62	theme	analoqous	1915:1923	arg1	processing					1937:1946	their analoqous proteolytic processing	1909:1946	the high degree of homology between collagen XV and collagen XVIII as well as their analoqous proteolytic processing	1831:1946	Due to the high degree of homology between collagen XV and collagen XVIII as well as their analoqous proteolytic processing, functional similarities of collagen XVIII- and XV-related fragments should be revealed in future experiments.
10441114	1	63	theme	anti-cancer	185:195	arg1	drug					197:200	potential anti-cancer drug	175:200	potential anti-cancer drug	175:200	Circulating elongated forms of the angiogenesis inhibitor and potential anti-cancer drug endostatin were isolated from human blood filtrate.
10441114	9	64	theme	endostatin-related	1497:1514	arg1	fragments					1527:1535	immunoreactive endostatin-related C-terminal fragments	1482:1535	immunoreactive endostatin-related C-terminal fragments of human collagen XV	1482:1556	Furthermore, immunoreactive endostatin-related C-terminal fragments of human collagen XV are found in the hemofiltrate.
10441114	10	65	theme	HLLPPP	1646:1651	arg1	sequences					1631:1639	the N-terminal sequences	1616:1639	the N-terminal sequences P(66)HLLPPP	1616:1651	These polypeptides exhibit the N-terminal sequences P(66)HLLPPP.
10441114	7	66	theme	841	1124:1126	arg1	Da					1128:1129	22 000 and 21 841 Da +/- 0.02%	1110:1139	Da	1128:1129	Circulating endostatins are present as sialoglycoprotein (22 000 and 21 841 Da +/- 0.02%) and asialoglycoprotein structures (21 710 and 21 549 Da +/- 0.02%), while the two completely deglycosylated forms are obtained only after enzymatic incubation.
10441114	14	67	theme	collagen	1883:1890	arg1	XVIII					1892:1896	collagen XVIII	1883:1896	collagen XVIII	1883:1896	Due to the high degree of homology between collagen XV and collagen XVIII as well as their analoqous proteolytic processing, functional similarities of collagen XVIII- and XV-related fragments should be revealed in future experiments.
10441114	1	68	theme	human	232:236	arg1	filtrate					244:251	human blood filtrate	232:251	human blood filtrate	232:251	Circulating elongated forms of the angiogenesis inhibitor and potential anti-cancer drug endostatin were isolated from human blood filtrate.
10441114	9	69	located	found	1562:1566	arg1	hemofiltrate					1575:1586	the hemofiltrate	1571:1586	the hemofiltrate	1571:1586	Furthermore, immunoreactive endostatin-related C-terminal fragments of human collagen XV are found in the hemofiltrate.
10441114	9	69	located	found	1562:1566	arg2	fragments					1527:1535	immunoreactive endostatin-related C-terminal fragments	1482:1535	immunoreactive endostatin-related C-terminal fragments of human collagen XV	1482:1556	Furthermore, immunoreactive endostatin-related C-terminal fragments of human collagen XV are found in the hemofiltrate.
10441114	4	70	theme	collagen	666:673	arg1	collagen					666:673	collagen XVIII	666:679	collagen XVIII	666:679	lacking the last and final three residues of the noncollagenous domain 1 (NC-1) of collagen XVIII, respectively.
10441114	4	70	theme	collagen	666:673	arg1	domain					647:652	noncollagenous domain 1	632:654	the noncollagenous domain 1 (NC-1) of collagen XVIII	628:679	lacking the last and final three residues of the noncollagenous domain 1 (NC-1) of collagen XVIII, respectively.
10441114	4	70	theme	collagen	666:673	arg1	NC-1					657:660	NC-1	657:660	NC-1	657:660	lacking the last and final three residues of the noncollagenous domain 1 (NC-1) of collagen XVIII, respectively.
10441114	1	71	theme	elongated	125:133	arg1	forms					135:139	Circulating elongated forms	113:139	Circulating elongated forms of the angiogenesis inhibitor and potential anti-cancer drug endostatin	113:211	Circulating elongated forms of the angiogenesis inhibitor and potential anti-cancer drug endostatin were isolated from human blood filtrate.
10441114	6	72	theme	mass	984:987	arg1	spectrometry					989:1000	HPLC-electrospray ionization mass spectrometry	955:1000	the semiquantitative HPLC-electrospray ionization mass spectrometry (ESMS) technique after exoglycosidase hydrolysis	934:1049	Carbohydrate analyses were performed via the semiquantitative HPLC-electrospray ionization mass spectrometry (ESMS) technique after exoglycosidase hydrolysis.
10441114	6	72	theme	mass	984:987	arg1	ESMS					1003:1006	ESMS	1003:1006	ESMS	1003:1006	Carbohydrate analyses were performed via the semiquantitative HPLC-electrospray ionization mass spectrometry (ESMS) technique after exoglycosidase hydrolysis.
10441114	7	73	gly	sialoglycoprotein	1091:1107	arg1	sialoglycoprotein					1091:1107	sialoglycoprotein (22 000 and 21 841 Da +/- 0.02%) and asialoglycoprotein structures	1091:1174	sialoglycoprotein	1091:1107	Circulating endostatins are present as sialoglycoprotein (22 000 and 21 841 Da +/- 0.02%) and asialoglycoprotein structures (21 710 and 21 549 Da +/- 0.02%), while the two completely deglycosylated forms are obtained only after enzymatic incubation.
10441114	0	74	theme	endostatin-related	68:85	arg1	fragments					87:95	circulating endostatin-related fragments	56:95	circulating endostatin-related fragments of collagen XV	56:110	Novel glycosylated forms of human plasma endostatin and circulating endostatin-related fragments of collagen XV.
10441114	7	75	theme	Circulating	1052:1062	arg1	endostatins					1064:1074	Circulating endostatins	1052:1074	Circulating endostatins	1052:1074	Circulating endostatins are present as sialoglycoprotein (22 000 and 21 841 Da +/- 0.02%) and asialoglycoprotein structures (21 710 and 21 549 Da +/- 0.02%), while the two completely deglycosylated forms are obtained only after enzymatic incubation.
10441114	1	76	theme	angiogenesis	148:159	arg1	inhibitor					161:169	the angiogenesis inhibitor	144:169	the angiogenesis inhibitor	144:169	Circulating elongated forms of the angiogenesis inhibitor and potential anti-cancer drug endostatin were isolated from human blood filtrate.
10441114	13	77	theme	glycosylated	1749:1760	arg1	polypeptides					1762:1773	three glycosylated polypeptides	1743:1773	three glycosylated polypeptides	1743:1773	ESMS and immunoblotting analyses reveal three glycosylated polypeptides with a molecular mass ranging from 16 to 21 kDa.
10441114	14	78	theme	future	2039:2044	arg1	experiments					2046:2056	future experiments	2039:2056	future experiments	2039:2056	Due to the high degree of homology between collagen XV and collagen XVIII as well as their analoqous proteolytic processing, functional similarities of collagen XVIII- and XV-related fragments should be revealed in future experiments.
10441114	12	79	theme	collagen	1678:1685	arg1	domain					1695:1700	the collagen XV NC-1 domain	1674:1700	the collagen XV NC-1 domain	1674:1700	of the collagen XV NC-1 domain.
10441114	13	80	theme	ESMS	1703:1706	arg1	analyses					1727:1734	ESMS and immunoblotting analyses	1703:1734	ESMS and immunoblotting analyses	1703:1734	ESMS and immunoblotting analyses reveal three glycosylated polypeptides with a molecular mass ranging from 16 to 21 kDa.
10441114	3	81	theme	isolated	497:504	arg1	molecules					506:514	the isolated molecules	493:514	the isolated molecules	493:514	N- and C-terminal sequence analyses of the isolated molecules revealed different forms of endostatin starting with V(117)HLRPAR.
10441114	0	82	theme	glycosylated	6:17	arg1	forms					19:23	Novel glycosylated forms	0:23	Novel glycosylated forms of human plasma endostatin	0:50	Novel glycosylated forms of human plasma endostatin and circulating endostatin-related fragments of collagen XV.
10441114	8	83	from	intermediates	1355:1367	arg1	pathway					1388:1394	the proteolytic pathway	1372:1394	the proteolytic pathway of the NC-1 domain of collagen XVIII resulting in bioactive endostatins	1372:1466	The described glycosylated endostatins may represent intermediates in the proteolytic pathway of the NC-1 domain of collagen XVIII resulting in bioactive endostatins.
10441114	12	84	theme	NC-1	1690:1693	arg1	domain					1695:1700	the collagen XV NC-1 domain	1674:1700	the collagen XV NC-1 domain	1674:1700	of the collagen XV NC-1 domain.
10441114	13	85	theme	immunoblotting	1712:1725	arg1	analyses					1727:1734	ESMS and immunoblotting analyses	1703:1734	ESMS and immunoblotting analyses	1703:1734	ESMS and immunoblotting analyses reveal three glycosylated polypeptides with a molecular mass ranging from 16 to 21 kDa.
10441114	5	86	theme	type	804:807	arg1	structure					781:789	a glycan structure	772:789	a glycan structure of the mucin type consisting of galactose N-acetylgalactosamine and N-acetylneuraminic acid residues	772:890	These polypetides are found to be O-glycosylated at T(125) (residue 9) with a glycan structure of the mucin type consisting of galactose N-acetylgalactosamine and N-acetylneuraminic acid residues.
10441114	5	87	theme	mucin	798:802	arg1	type					804:807	the mucin type	794:807	the mucin type consisting of galactose N-acetylgalactosamine and N-acetylneuraminic acid residues	794:890	These polypetides are found to be O-glycosylated at T(125) (residue 9) with a glycan structure of the mucin type consisting of galactose N-acetylgalactosamine and N-acetylneuraminic acid residues.
10441114	8	88	theme	domain	1408:1413	arg1	pathway					1388:1394	the proteolytic pathway	1372:1394	the proteolytic pathway of the NC-1 domain of collagen XVIII resulting in bioactive endostatins	1372:1466	The described glycosylated endostatins may represent intermediates in the proteolytic pathway of the NC-1 domain of collagen XVIII resulting in bioactive endostatins.
10441114	0	89	theme	plasma	34:39	arg1	endostatin					41:50	human plasma endostatin	28:50	human plasma endostatin	28:50	Novel glycosylated forms of human plasma endostatin and circulating endostatin-related fragments of collagen XV.
10441114	9	90	theme	human	1540:1544	arg1	XV					1555:1556	human collagen XV	1540:1556	human collagen XV	1540:1556	Furthermore, immunoreactive endostatin-related C-terminal fragments of human collagen XV are found in the hemofiltrate.
10441114	14	91	theme	XV-related	1996:2005	arg1	fragments					2007:2015	collagen XVIII- and XV-related fragments	1976:2015	collagen XVIII- and XV-related fragments	1976:2015	Due to the high degree of homology between collagen XV and collagen XVIII as well as their analoqous proteolytic processing, functional similarities of collagen XVIII- and XV-related fragments should be revealed in future experiments.
10441114	3	92	theme	sequence	472:479	arg1	analyses					481:488	N- and C-terminal sequence analyses	454:488	N- and C-terminal sequence analyses of the isolated molecules	454:514	N- and C-terminal sequence analyses of the isolated molecules revealed different forms of endostatin starting with V(117)HLRPAR.
10441114	8	93	theme	collagen	1418:1425	arg1	collagen					1418:1425	collagen XVIII	1418:1431	collagen XVIII	1418:1431	The described glycosylated endostatins may represent intermediates in the proteolytic pathway of the NC-1 domain of collagen XVIII resulting in bioactive endostatins.
10441114	8	93	theme	collagen	1418:1425	arg1	domain					1408:1413	the NC-1 domain	1399:1413	the NC-1 domain of collagen XVIII	1399:1431	The described glycosylated endostatins may represent intermediates in the proteolytic pathway of the NC-1 domain of collagen XVIII resulting in bioactive endostatins.
10441114	14	94	theme	XVIII-	1985:1990	arg1	fragments					2007:2015	collagen XVIII- and XV-related fragments	1976:2015	collagen XVIII- and XV-related fragments	1976:2015	Due to the high degree of homology between collagen XV and collagen XVIII as well as their analoqous proteolytic processing, functional similarities of collagen XVIII- and XV-related fragments should be revealed in future experiments.
10441114	2	95	theme	polypeptide	372:382	arg1	epitope					357:363	an N-terminal epitope	343:363	an N-terminal epitope of the polypeptide	343:382	Immunoreactive endostatin was identified by a polyclonal rabbit antiserum raised against an N-terminal epitope of the polypeptide and purified by consecutive chromatographic steps and immunoblotting.
10441114	8	96	theme	bioactive	1446:1454	arg1	endostatins					1456:1466	bioactive endostatins	1446:1466	bioactive endostatins	1446:1466	The described glycosylated endostatins may represent intermediates in the proteolytic pathway of the NC-1 domain of collagen XVIII resulting in bioactive endostatins.
10441114	3	97	theme	endostatin	544:553	arg1	forms					535:539	different forms	525:539	different forms of endostatin starting with V(117)HLRPAR	525:580	N- and C-terminal sequence analyses of the isolated molecules revealed different forms of endostatin starting with V(117)HLRPAR.
10441114	1	98	theme	blood	238:242	arg1	filtrate					244:251	human blood filtrate	232:251	human blood filtrate	232:251	Circulating elongated forms of the angiogenesis inhibitor and potential anti-cancer drug endostatin were isolated from human blood filtrate.
10441114	14	99	theme	functional	1949:1958	arg1	similarities					1960:1971	functional similarities	1949:1971	functional similarities of collagen XVIII- and XV-related fragments	1949:2015	Due to the high degree of homology between collagen XV and collagen XVIII as well as their analoqous proteolytic processing, functional similarities of collagen XVIII- and XV-related fragments should be revealed in future experiments.
10441114	5	100	dep	galactose	823:831	arg1	N-acetylgalactosamine					833:853	N-acetylgalactosamine	833:853	N-acetylgalactosamine	833:853	These polypetides are found to be O-glycosylated at T(125) (residue 9) with a glycan structure of the mucin type consisting of galactose N-acetylgalactosamine and N-acetylneuraminic acid residues.
10441114	5	100	dep	galactose	823:831	arg1	residues					883:890	residues	883:890	residues	883:890	These polypetides are found to be O-glycosylated at T(125) (residue 9) with a glycan structure of the mucin type consisting of galactose N-acetylgalactosamine and N-acetylneuraminic acid residues.
10441114	11	101	theme	Y	1658:1658	arg1	EKPALH					1663:1668	Y(81)EKPALH	1658:1668	Y(81)EKPALH	1658:1668	and Y(81)EKPALH.
10441114	2	102	theme	consecutive	400:410	arg1	steps					428:432	consecutive chromatographic steps	400:432	consecutive chromatographic steps	400:432	Immunoreactive endostatin was identified by a polyclonal rabbit antiserum raised against an N-terminal epitope of the polypeptide and purified by consecutive chromatographic steps and immunoblotting.
18420577	6	0	theme	stress	1111:1116	arg1	response					1118:1125	stress response	1111:1125	stress response	1111:1125	GlcNAcylation of FoxO provides a new mechanism for direct nutrient control of transcription to regulate metabolism and stress response through control of FoxO1 activity.
18420577	5	1	theme	increased	843:851	arg1	expression					853:862	the paradoxically increased expression	825:862	the paradoxically increased expression of gluconeogenic genes	825:885	Furthermore, O-GlcNAc regulates FoxO1 activation in response to glucose, resulting in the paradoxically increased expression of gluconeogenic genes while concomitantly inducing expression of genes encoding enzymes that detoxify reactive oxygen species.
18420577	2	2	dep	factor	171:176	arg1	FoxO1					178:182	FoxO1	178:182	The transcription factor FoxO1	153:182	The transcription factor FoxO1 activates expression of gluconeogenic, including phosphoenolpyruvate carboxykinase and glucose-6-phosphatase, and also activates the expression of the oxidative stress response enzymes catalase and manganese superoxide dismutase.
18420577	3	3	theme	Hormonal	414:421	arg1	regulation					444:453	Hormonal and stress-dependent regulation	414:453	Hormonal and stress-dependent regulation of FoxO1 via acetylation	414:478	Hormonal and stress-dependent regulation of FoxO1 via acetylation, ubiquitination, and phosphorylation, are well established, but FoxOs have not been studied in the context of the glucose-derived O-linked beta-N-acetylglucosamine (O-GlcNAc) modification.
18420577	6	4	theme	FoxO	1009:1012	arg1	GlcNAcylation					992:1004	GlcNAcylation	992:1004	GlcNAcylation of FoxO	992:1012	GlcNAcylation of FoxO provides a new mechanism for direct nutrient control of transcription to regulate metabolism and stress response through control of FoxO1 activity.
18420577	3	5	theme	beta-N-acetylglucosamine	619:642	arg1	modification					655:666	the glucose-derived O-linked beta-N-acetylglucosamine (O-GlcNAc) modification	590:666	the glucose-derived O-linked beta-N-acetylglucosamine (O-GlcNAc) modification	590:666	Hormonal and stress-dependent regulation of FoxO1 via acetylation, ubiquitination, and phosphorylation, are well established, but FoxOs have not been studied in the context of the glucose-derived O-linked beta-N-acetylglucosamine (O-GlcNAc) modification.
18420577	2	6	theme	enzymes	361:367	arg1	expression					317:326	the expression	313:326	the expression of the oxidative stress response enzymes catalase and manganese superoxide dismutase	313:411	The transcription factor FoxO1 activates expression of gluconeogenic, including phosphoenolpyruvate carboxykinase and glucose-6-phosphatase, and also activates the expression of the oxidative stress response enzymes catalase and manganese superoxide dismutase.
18420577	2	7	theme	transcription	157:169	arg1	factor					171:176	The transcription factor	153:176	The transcription factor FoxO1	153:182	The transcription factor FoxO1 activates expression of gluconeogenic, including phosphoenolpyruvate carboxykinase and glucose-6-phosphatase, and also activates the expression of the oxidative stress response enzymes catalase and manganese superoxide dismutase.
18420577	3	8	theme	glucose-derived	594:608	arg1	modification					655:666	the glucose-derived O-linked beta-N-acetylglucosamine (O-GlcNAc) modification	590:666	the glucose-derived O-linked beta-N-acetylglucosamine (O-GlcNAc) modification	590:666	Hormonal and stress-dependent regulation of FoxO1 via acetylation, ubiquitination, and phosphorylation, are well established, but FoxOs have not been studied in the context of the glucose-derived O-linked beta-N-acetylglucosamine (O-GlcNAc) modification.
18420577	1	9	theme	FoxO	59:62	arg1	proteins					64:71	FoxO proteins	59:71	FoxO proteins	59:71	FoxO proteins are key transcriptional regulators of nutrient homeostasis and stress response.
18420577	1	9	theme	FoxO	59:62	arg1	regulators					97:106	key transcriptional regulators	77:106	key transcriptional regulators of nutrient homeostasis and stress response	77:150	FoxO proteins are key transcriptional regulators of nutrient homeostasis and stress response.
18420577	5	10	from	activation	777:786	arg1	response					791:798	response	791:798	response to glucose	791:809	Furthermore, O-GlcNAc regulates FoxO1 activation in response to glucose, resulting in the paradoxically increased expression of gluconeogenic genes while concomitantly inducing expression of genes encoding enzymes that detoxify reactive oxygen species.
18420577	2	11	theme	superoxide	392:401	arg1	dismutase					403:411	manganese superoxide dismutase	382:411	manganese superoxide dismutase	382:411	The transcription factor FoxO1 activates expression of gluconeogenic, including phosphoenolpyruvate carboxykinase and glucose-6-phosphatase, and also activates the expression of the oxidative stress response enzymes catalase and manganese superoxide dismutase.
18420577	2	11	theme	superoxide	392:401	arg1	enzymes					361:367	the oxidative stress response enzymes	331:367	the oxidative stress response enzymes catalase and manganese superoxide dismutase	331:411	The transcription factor FoxO1 activates expression of gluconeogenic, including phosphoenolpyruvate carboxykinase and glucose-6-phosphatase, and also activates the expression of the oxidative stress response enzymes catalase and manganese superoxide dismutase.
18420577	3	12	link	glucose-derived	594:608	arg1	modification					655:666	the glucose-derived O-linked beta-N-acetylglucosamine (O-GlcNAc) modification	590:666	the glucose-derived O-linked beta-N-acetylglucosamine (O-GlcNAc) modification	590:666	Hormonal and stress-dependent regulation of FoxO1 via acetylation, ubiquitination, and phosphorylation, are well established, but FoxOs have not been studied in the context of the glucose-derived O-linked beta-N-acetylglucosamine (O-GlcNAc) modification.
18420577	4	13	from	O-GlcNAc	687:694	arg1	FoxO1					707:711	hepatic FoxO1	699:711	hepatic FoxO1	699:711	Here we show that O-GlcNAc on hepatic FoxO1 is increased in diabetes.
18420577	1	14	theme	key	77:79	arg1	proteins					64:71	FoxO proteins	59:71	FoxO proteins	59:71	FoxO proteins are key transcriptional regulators of nutrient homeostasis and stress response.
18420577	1	14	theme	key	77:79	arg1	regulators					97:106	key transcriptional regulators	77:106	key transcriptional regulators of nutrient homeostasis and stress response	77:150	FoxO proteins are key transcriptional regulators of nutrient homeostasis and stress response.
18420577	5	15	theme	reactive	967:974	arg1	species					983:989	reactive oxygen species	967:989	reactive oxygen species	967:989	Furthermore, O-GlcNAc regulates FoxO1 activation in response to glucose, resulting in the paradoxically increased expression of gluconeogenic genes while concomitantly inducing expression of genes encoding enzymes that detoxify reactive oxygen species.
18420577	3	16	theme	FoxO1	458:462	arg1	phosphorylation					501:515	phosphorylation	501:515	phosphorylation	501:515	Hormonal and stress-dependent regulation of FoxO1 via acetylation, ubiquitination, and phosphorylation, are well established, but FoxOs have not been studied in the context of the glucose-derived O-linked beta-N-acetylglucosamine (O-GlcNAc) modification.
18420577	3	16	theme	FoxO1	458:462	arg1	regulation					444:453	Hormonal and stress-dependent regulation	414:453	Hormonal and stress-dependent regulation of FoxO1 via acetylation	414:478	Hormonal and stress-dependent regulation of FoxO1 via acetylation, ubiquitination, and phosphorylation, are well established, but FoxOs have not been studied in the context of the glucose-derived O-linked beta-N-acetylglucosamine (O-GlcNAc) modification.
18420577	3	16	theme	FoxO1	458:462	arg1	ubiquitination					481:494	ubiquitination	481:494	ubiquitination	481:494	Hormonal and stress-dependent regulation of FoxO1 via acetylation, ubiquitination, and phosphorylation, are well established, but FoxOs have not been studied in the context of the glucose-derived O-linked beta-N-acetylglucosamine (O-GlcNAc) modification.
18420577	2	17	theme	response	352:359	arg1	catalase					369:376	catalase	369:376	catalase	369:376	The transcription factor FoxO1 activates expression of gluconeogenic, including phosphoenolpyruvate carboxykinase and glucose-6-phosphatase, and also activates the expression of the oxidative stress response enzymes catalase and manganese superoxide dismutase.
18420577	2	17	theme	response	352:359	arg1	dismutase					403:411	manganese superoxide dismutase	382:411	manganese superoxide dismutase	382:411	The transcription factor FoxO1 activates expression of gluconeogenic, including phosphoenolpyruvate carboxykinase and glucose-6-phosphatase, and also activates the expression of the oxidative stress response enzymes catalase and manganese superoxide dismutase.
18420577	2	17	theme	response	352:359	arg1	enzymes					361:367	the oxidative stress response enzymes	331:367	the oxidative stress response enzymes catalase and manganese superoxide dismutase	331:411	The transcription factor FoxO1 activates expression of gluconeogenic, including phosphoenolpyruvate carboxykinase and glucose-6-phosphatase, and also activates the expression of the oxidative stress response enzymes catalase and manganese superoxide dismutase.
18420577	5	18	theme	oxygen	976:981	arg1	species					983:989	reactive oxygen species	967:989	reactive oxygen species	967:989	Furthermore, O-GlcNAc regulates FoxO1 activation in response to glucose, resulting in the paradoxically increased expression of gluconeogenic genes while concomitantly inducing expression of genes encoding enzymes that detoxify reactive oxygen species.
18420577	3	19	theme	stress-dependent	427:442	arg1	regulation					444:453	Hormonal and stress-dependent regulation	414:453	Hormonal and stress-dependent regulation of FoxO1 via acetylation	414:478	Hormonal and stress-dependent regulation of FoxO1 via acetylation, ubiquitination, and phosphorylation, are well established, but FoxOs have not been studied in the context of the glucose-derived O-linked beta-N-acetylglucosamine (O-GlcNAc) modification.
18420577	6	20	theme	transcription	1070:1082	arg1	control					1059:1065	direct nutrient control	1043:1065	direct nutrient control of transcription	1043:1082	GlcNAcylation of FoxO provides a new mechanism for direct nutrient control of transcription to regulate metabolism and stress response through control of FoxO1 activity.
18420577	5	21	theme	FoxO1	771:775	arg1	activation					777:786	FoxO1 activation	771:786	FoxO1 activation	771:786	Furthermore, O-GlcNAc regulates FoxO1 activation in response to glucose, resulting in the paradoxically increased expression of gluconeogenic genes while concomitantly inducing expression of genes encoding enzymes that detoxify reactive oxygen species.
18420577	3	22	theme	modification	655:666	arg1	context					579:585	the context	575:585	the context of the glucose-derived O-linked beta-N-acetylglucosamine (O-GlcNAc) modification	575:666	Hormonal and stress-dependent regulation of FoxO1 via acetylation, ubiquitination, and phosphorylation, are well established, but FoxOs have not been studied in the context of the glucose-derived O-linked beta-N-acetylglucosamine (O-GlcNAc) modification.
18420577	2	23	theme	stress	345:350	arg1	catalase					369:376	catalase	369:376	catalase	369:376	The transcription factor FoxO1 activates expression of gluconeogenic, including phosphoenolpyruvate carboxykinase and glucose-6-phosphatase, and also activates the expression of the oxidative stress response enzymes catalase and manganese superoxide dismutase.
18420577	2	23	theme	stress	345:350	arg1	dismutase					403:411	manganese superoxide dismutase	382:411	manganese superoxide dismutase	382:411	The transcription factor FoxO1 activates expression of gluconeogenic, including phosphoenolpyruvate carboxykinase and glucose-6-phosphatase, and also activates the expression of the oxidative stress response enzymes catalase and manganese superoxide dismutase.
18420577	2	23	theme	stress	345:350	arg1	enzymes					361:367	the oxidative stress response enzymes	331:367	the oxidative stress response enzymes catalase and manganese superoxide dismutase	331:411	The transcription factor FoxO1 activates expression of gluconeogenic, including phosphoenolpyruvate carboxykinase and glucose-6-phosphatase, and also activates the expression of the oxidative stress response enzymes catalase and manganese superoxide dismutase.
18420577	4	24	theme	hepatic	699:705	arg1	FoxO1					707:711	hepatic FoxO1	699:711	hepatic FoxO1	699:711	Here we show that O-GlcNAc on hepatic FoxO1 is increased in diabetes.
18420577	1	25	theme	transcriptional	81:95	arg1	proteins					64:71	FoxO proteins	59:71	FoxO proteins	59:71	FoxO proteins are key transcriptional regulators of nutrient homeostasis and stress response.
18420577	1	25	theme	transcriptional	81:95	arg1	regulators					97:106	key transcriptional regulators	77:106	key transcriptional regulators of nutrient homeostasis and stress response	77:150	FoxO proteins are key transcriptional regulators of nutrient homeostasis and stress response.
18420577	2	26	theme	oxidative	335:343	arg1	catalase					369:376	catalase	369:376	catalase	369:376	The transcription factor FoxO1 activates expression of gluconeogenic, including phosphoenolpyruvate carboxykinase and glucose-6-phosphatase, and also activates the expression of the oxidative stress response enzymes catalase and manganese superoxide dismutase.
18420577	2	26	theme	oxidative	335:343	arg1	dismutase					403:411	manganese superoxide dismutase	382:411	manganese superoxide dismutase	382:411	The transcription factor FoxO1 activates expression of gluconeogenic, including phosphoenolpyruvate carboxykinase and glucose-6-phosphatase, and also activates the expression of the oxidative stress response enzymes catalase and manganese superoxide dismutase.
18420577	2	26	theme	oxidative	335:343	arg1	enzymes					361:367	the oxidative stress response enzymes	331:367	the oxidative stress response enzymes catalase and manganese superoxide dismutase	331:411	The transcription factor FoxO1 activates expression of gluconeogenic, including phosphoenolpyruvate carboxykinase and glucose-6-phosphatase, and also activates the expression of the oxidative stress response enzymes catalase and manganese superoxide dismutase.
18420577	5	27	theme	genes	930:934	arg1	expression					916:925	expression	916:925	expression of genes encoding enzymes that detoxify reactive oxygen species	916:989	Furthermore, O-GlcNAc regulates FoxO1 activation in response to glucose, resulting in the paradoxically increased expression of gluconeogenic genes while concomitantly inducing expression of genes encoding enzymes that detoxify reactive oxygen species.
18420577	2	28	theme	manganese	382:390	arg1	dismutase					403:411	manganese superoxide dismutase	382:411	manganese superoxide dismutase	382:411	The transcription factor FoxO1 activates expression of gluconeogenic, including phosphoenolpyruvate carboxykinase and glucose-6-phosphatase, and also activates the expression of the oxidative stress response enzymes catalase and manganese superoxide dismutase.
18420577	2	28	theme	manganese	382:390	arg1	enzymes					361:367	the oxidative stress response enzymes	331:367	the oxidative stress response enzymes catalase and manganese superoxide dismutase	331:411	The transcription factor FoxO1 activates expression of gluconeogenic, including phosphoenolpyruvate carboxykinase and glucose-6-phosphatase, and also activates the expression of the oxidative stress response enzymes catalase and manganese superoxide dismutase.
18420577	6	29	theme	activity	1152:1159	arg1	control					1135:1141	control	1135:1141	control of FoxO1 activity	1135:1159	GlcNAcylation of FoxO provides a new mechanism for direct nutrient control of transcription to regulate metabolism and stress response through control of FoxO1 activity.
18420577	6	30	theme	nutrient	1050:1057	arg1	control					1059:1065	direct nutrient control	1043:1065	direct nutrient control of transcription	1043:1082	GlcNAcylation of FoxO provides a new mechanism for direct nutrient control of transcription to regulate metabolism and stress response through control of FoxO1 activity.
18420577	6	31	theme	FoxO1	1146:1150	arg1	activity					1152:1159	FoxO1 activity	1146:1159	FoxO1 activity	1146:1159	GlcNAcylation of FoxO provides a new mechanism for direct nutrient control of transcription to regulate metabolism and stress response through control of FoxO1 activity.
18420577	5	32	theme	gluconeogenic	867:879	arg1	genes					881:885	gluconeogenic genes	867:885	gluconeogenic genes	867:885	Furthermore, O-GlcNAc regulates FoxO1 activation in response to glucose, resulting in the paradoxically increased expression of gluconeogenic genes while concomitantly inducing expression of genes encoding enzymes that detoxify reactive oxygen species.
18420577	6	33	theme	direct	1043:1048	arg1	control					1059:1065	direct nutrient control	1043:1065	direct nutrient control of transcription	1043:1082	GlcNAcylation of FoxO provides a new mechanism for direct nutrient control of transcription to regulate metabolism and stress response through control of FoxO1 activity.
18420577	1	34	theme	nutrient	111:118	arg1	homeostasis					120:130	nutrient homeostasis	111:130	nutrient homeostasis	111:130	FoxO proteins are key transcriptional regulators of nutrient homeostasis and stress response.
18420577	5	35	theme	genes	881:885	arg1	expression					853:862	the paradoxically increased expression	825:862	the paradoxically increased expression of gluconeogenic genes	825:885	Furthermore, O-GlcNAc regulates FoxO1 activation in response to glucose, resulting in the paradoxically increased expression of gluconeogenic genes while concomitantly inducing expression of genes encoding enzymes that detoxify reactive oxygen species.
18420577	2	36	theme	phosphoenolpyruvate	233:251	arg1	carboxykinase					253:265	phosphoenolpyruvate carboxykinase	233:265	phosphoenolpyruvate carboxykinase	233:265	The transcription factor FoxO1 activates expression of gluconeogenic, including phosphoenolpyruvate carboxykinase and glucose-6-phosphatase, and also activates the expression of the oxidative stress response enzymes catalase and manganese superoxide dismutase.
18420577	1	37	theme	homeostasis	120:130	arg1	proteins					64:71	FoxO proteins	59:71	FoxO proteins	59:71	FoxO proteins are key transcriptional regulators of nutrient homeostasis and stress response.
18420577	1	37	theme	homeostasis	120:130	arg1	regulators					97:106	key transcriptional regulators	77:106	key transcriptional regulators of nutrient homeostasis and stress response	77:150	FoxO proteins are key transcriptional regulators of nutrient homeostasis and stress response.
18420577	2	38	dep	enzymes	361:367	arg1	catalase					369:376	catalase	369:376	catalase	369:376	The transcription factor FoxO1 activates expression of gluconeogenic, including phosphoenolpyruvate carboxykinase and glucose-6-phosphatase, and also activates the expression of the oxidative stress response enzymes catalase and manganese superoxide dismutase.
18420577	2	38	dep	enzymes	361:367	arg1	dismutase					403:411	manganese superoxide dismutase	382:411	manganese superoxide dismutase	382:411	The transcription factor FoxO1 activates expression of gluconeogenic, including phosphoenolpyruvate carboxykinase and glucose-6-phosphatase, and also activates the expression of the oxidative stress response enzymes catalase and manganese superoxide dismutase.
18420577	2	38	dep	enzymes	361:367	arg1	enzymes					361:367	the oxidative stress response enzymes	331:367	the oxidative stress response enzymes catalase and manganese superoxide dismutase	331:411	The transcription factor FoxO1 activates expression of gluconeogenic, including phosphoenolpyruvate carboxykinase and glucose-6-phosphatase, and also activates the expression of the oxidative stress response enzymes catalase and manganese superoxide dismutase.
18420577	3	39	theme	O-linked	610:617	arg1	beta-N-acetylglucosamine					619:642	O-linked beta-N-acetylglucosamine	610:642	the glucose-derived O-linked beta-N-acetylglucosamine (O-GlcNAc) modification	590:666	Hormonal and stress-dependent regulation of FoxO1 via acetylation, ubiquitination, and phosphorylation, are well established, but FoxOs have not been studied in the context of the glucose-derived O-linked beta-N-acetylglucosamine (O-GlcNAc) modification.
18420577	3	39	theme	O-linked	610:617	arg1	O-GlcNAc					645:652	O-GlcNAc	645:652	O-GlcNAc	645:652	Hormonal and stress-dependent regulation of FoxO1 via acetylation, ubiquitination, and phosphorylation, are well established, but FoxOs have not been studied in the context of the glucose-derived O-linked beta-N-acetylglucosamine (O-GlcNAc) modification.
18420577	2	40	theme	gluconeogenic	208:220	arg1	expression					194:203	expression	194:203	expression of gluconeogenic, including phosphoenolpyruvate carboxykinase and glucose-6-phosphatase	194:291	The transcription factor FoxO1 activates expression of gluconeogenic, including phosphoenolpyruvate carboxykinase and glucose-6-phosphatase, and also activates the expression of the oxidative stress response enzymes catalase and manganese superoxide dismutase.
18420577	1	41	theme	stress	136:141	arg1	response					143:150	stress response	136:150	stress response	136:150	FoxO proteins are key transcriptional regulators of nutrient homeostasis and stress response.
18420577	3	42	link	O-linked	610:617	arg1	beta-N-acetylglucosamine					619:642	O-linked beta-N-acetylglucosamine	610:642	the glucose-derived O-linked beta-N-acetylglucosamine (O-GlcNAc) modification	590:666	Hormonal and stress-dependent regulation of FoxO1 via acetylation, ubiquitination, and phosphorylation, are well established, but FoxOs have not been studied in the context of the glucose-derived O-linked beta-N-acetylglucosamine (O-GlcNAc) modification.
18420577	3	42	link	O-linked	610:617	arg1	O-GlcNAc					645:652	O-GlcNAc	645:652	O-GlcNAc	645:652	Hormonal and stress-dependent regulation of FoxO1 via acetylation, ubiquitination, and phosphorylation, are well established, but FoxOs have not been studied in the context of the glucose-derived O-linked beta-N-acetylglucosamine (O-GlcNAc) modification.
18420577	1	43	theme	response	143:150	arg1	proteins					64:71	FoxO proteins	59:71	FoxO proteins	59:71	FoxO proteins are key transcriptional regulators of nutrient homeostasis and stress response.
18420577	1	43	theme	response	143:150	arg1	regulators					97:106	key transcriptional regulators	77:106	key transcriptional regulators of nutrient homeostasis and stress response	77:150	FoxO proteins are key transcriptional regulators of nutrient homeostasis and stress response.
18420577	6	44	theme	new	1025:1027	arg1	mechanism					1029:1037	a new mechanism	1023:1037	a new mechanism for direct nutrient control of transcription	1023:1082	GlcNAcylation of FoxO provides a new mechanism for direct nutrient control of transcription to regulate metabolism and stress response through control of FoxO1 activity.
18420577	0	45	theme	FoxO	19:22	arg1	activation					24:33	FoxO activation	19:33	FoxO activation	19:33	O-GlcNAc regulates FoxO activation in response to glucose.
34411563	4	0	theme	novel	663:667	arg1	O-glucosyltransferases					677:698	two novel protein O-glucosyltransferases	659:698	two novel protein O-glucosyltransferases	659:698	We recently identified two novel protein O-glucosyltransferases, Protein O-glucosyltransferase 2 (POGLUT2) and 3 (POGLUT3), that modify a small fraction of EGF repeats on Notch.
34411563	4	0	theme	novel	663:667	arg1	O-glucosyltransferase					709:729	Protein O-glucosyltransferase 2	701:731	Protein O-glucosyltransferase 2 (POGLUT2)	701:741	We recently identified two novel protein O-glucosyltransferases, Protein O-glucosyltransferase 2 (POGLUT2) and 3 (POGLUT3), that modify a small fraction of EGF repeats on Notch.
34411563	4	0	theme	novel	663:667	arg1	3					747:747	3	747:747	3	747:747	We recently identified two novel protein O-glucosyltransferases, Protein O-glucosyltransferase 2 (POGLUT2) and 3 (POGLUT3), that modify a small fraction of EGF repeats on Notch.
34411563	9	1	theme	3	1502:1502	arg1	double-knockout					1504:1518	double-knockout	1504:1518	double-knockout	1504:1518	In vitro secretion assays using the N-terminal portion of recombinant FBN1 revealed reduced FBN1 secretion in POGLUT2 knockout, POGLUT3 knockout, and POGLUT2 and 3 double-knockout HEK293T cells compared with wild type.
34411563	4	2	from	repeats	796:802	arg1	Notch					807:811	Notch	807:811	Notch	807:811	We recently identified two novel protein O-glucosyltransferases, Protein O-glucosyltransferase 2 (POGLUT2) and 3 (POGLUT3), that modify a small fraction of EGF repeats on Notch.
34411563	2	3	theme	latent	338:343	arg1	TGF					373:375	TGF	373:375	TGF	373:375	Through protein-protein interactions with latent transforming growth factor (TGF) β-binding protein 1 (LTBP1), microfibrils regulate TGF-β signaling.
34411563	2	3	theme	latent	338:343	arg1	factor					365:370	latent transforming growth factor	338:370	latent transforming growth factor (TGF) β-binding protein 1 (LTBP1)	338:404	Through protein-protein interactions with latent transforming growth factor (TGF) β-binding protein 1 (LTBP1), microfibrils regulate TGF-β signaling.
34411563	2	3	theme	latent	338:343	arg1	LTBP1					399:403	LTBP1	399:403	LTBP1	399:403	Through protein-protein interactions with latent transforming growth factor (TGF) β-binding protein 1 (LTBP1), microfibrils regulate TGF-β signaling.
34411563	10	4	theme	substrate	1718:1726	arg1	proteins					1728:1735	substrate proteins	1718:1735	substrate proteins	1718:1735	These results illustrate that POGLUT2 and 3 function together to O-glucosylate protein substrates and that these modifications play a role in the secretion of substrate proteins.
34411563	9	5	theme	double-knockout	1504:1518	arg1	cells					1528:1532	POGLUT2 knockout, POGLUT3 knockout, and POGLUT2 and 3 double-knockout HEK293T cells	1450:1532	POGLUT2 knockout, POGLUT3 knockout, and POGLUT2 and 3 double-knockout HEK293T cells	1450:1532	In vitro secretion assays using the N-terminal portion of recombinant FBN1 revealed reduced FBN1 secretion in POGLUT2 knockout, POGLUT3 knockout, and POGLUT2 and 3 double-knockout HEK293T cells compared with wild type.
34411563	3	6	theme	growth	480:485	arg1	repeats					505:511	the 47 epidermal growth factor-like (EGF) repeats	463:511	the 47 epidermal growth factor-like (EGF) repeats of FBN1	463:519	Mutations within the 47 epidermal growth factor-like (EGF) repeats of FBN1 cause autosomal dominant disorders including Marfan Syndrome, which is characterized by disrupted TGF-β signaling.
34411563	5	7	from	half	900:903	arg1	FBN1					927:930	FBN1	927:930	FBN1	927:930	Here, using mass spectral analysis, we show that POGLUT2 and POGLUT3 also modify over half of the EGF repeats on FBN1, fibrillin-2 (FBN2), and LTBP1.
34411563	5	7	from	half	900:903	arg1	LTBP1					957:961	LTBP1	957:961	LTBP1	957:961	Here, using mass spectral analysis, we show that POGLUT2 and POGLUT3 also modify over half of the EGF repeats on FBN1, fibrillin-2 (FBN2), and LTBP1.
34411563	5	7	from	half	900:903	arg1	FBN2					946:949	FBN2	946:949	FBN2	946:949	Here, using mass spectral analysis, we show that POGLUT2 and POGLUT3 also modify over half of the EGF repeats on FBN1, fibrillin-2 (FBN2), and LTBP1.
34411563	5	7	from	half	900:903	arg1	fibrillin-2					933:943	fibrillin-2	933:943	fibrillin-2 (FBN2)	933:950	Here, using mass spectral analysis, we show that POGLUT2 and POGLUT3 also modify over half of the EGF repeats on FBN1, fibrillin-2 (FBN2), and LTBP1.
34411563	1	8	theme	proper	226:231	arg1	development					233:243	proper development	226:243	proper development of elastic tissues, including the heart and lungs	226:293	Fibrillin-1 (FBN1) is the major component of extracellular matrix microfibrils, which are required for proper development of elastic tissues, including the heart and lungs.
34411563	9	9	theme	HEK293T	1520:1526	arg1	cells					1528:1532	POGLUT2 knockout, POGLUT3 knockout, and POGLUT2 and 3 double-knockout HEK293T cells	1450:1532	POGLUT2 knockout, POGLUT3 knockout, and POGLUT2 and 3 double-knockout HEK293T cells	1450:1532	In vitro secretion assays using the N-terminal portion of recombinant FBN1 revealed reduced FBN1 secretion in POGLUT2 knockout, POGLUT3 knockout, and POGLUT2 and 3 double-knockout HEK293T cells compared with wild type.
34411563	3	10	theme	factor-like	487:497	arg1	repeats					505:511	the 47 epidermal growth factor-like (EGF) repeats	463:511	the 47 epidermal growth factor-like (EGF) repeats of FBN1	463:519	Mutations within the 47 epidermal growth factor-like (EGF) repeats of FBN1 cause autosomal dominant disorders including Marfan Syndrome, which is characterized by disrupted TGF-β signaling.
34411563	9	11	theme	recombinant	1398:1408	arg1	FBN1					1410:1413	recombinant FBN1	1398:1413	recombinant FBN1	1398:1413	In vitro secretion assays using the N-terminal portion of recombinant FBN1 revealed reduced FBN1 secretion in POGLUT2 knockout, POGLUT3 knockout, and POGLUT2 and 3 double-knockout HEK293T cells compared with wild type.
34411563	8	12	theme	folded	1237:1242	arg1	repeat					1264:1269	a folded versus unfolded EGF repeat	1235:1269	a folded versus unfolded EGF repeat	1235:1269	Like POGLUT1, POGLUT2 and 3 can discern a folded versus unfolded EGF repeat, suggesting POGLUT2 and 3 are involved in a protein folding pathway.
34411563	9	13	theme	FBN1	1432:1435	arg1	secretion					1437:1445	reduced FBN1 secretion	1424:1445	reduced FBN1 secretion	1424:1445	In vitro secretion assays using the N-terminal portion of recombinant FBN1 revealed reduced FBN1 secretion in POGLUT2 knockout, POGLUT3 knockout, and POGLUT2 and 3 double-knockout HEK293T cells compared with wild type.
34411563	9	14	theme	FBN1	1410:1413	arg1	portion					1387:1393	the N-terminal portion	1372:1393	the N-terminal portion of recombinant FBN1	1372:1413	In vitro secretion assays using the N-terminal portion of recombinant FBN1 revealed reduced FBN1 secretion in POGLUT2 knockout, POGLUT3 knockout, and POGLUT2 and 3 double-knockout HEK293T cells compared with wild type.
34411563	3	15	theme	epidermal	470:478	arg1	repeats					505:511	the 47 epidermal growth factor-like (EGF) repeats	463:511	the 47 epidermal growth factor-like (EGF) repeats of FBN1	463:519	Mutations within the 47 epidermal growth factor-like (EGF) repeats of FBN1 cause autosomal dominant disorders including Marfan Syndrome, which is characterized by disrupted TGF-β signaling.
34411563	5	16	from	FBN1	927:930	arg1	half					900:903	half	900:903	half of the EGF repeats on FBN1, fibrillin-2 (FBN2), and LTBP1	900:961	Here, using mass spectral analysis, we show that POGLUT2 and POGLUT3 also modify over half of the EGF repeats on FBN1, fibrillin-2 (FBN2), and LTBP1.
34411563	0	17	from	repeats	47:53	arg1	-2					71:72	-2	71:72	-2	71:72	POGLUT2 and POGLUT3 O-glucosylate multiple EGF repeats in fibrillin-1, -2, and LTBP1 and promote secretion of fibrillin-1.
34411563	0	17	from	repeats	47:53	arg1	LTBP1					79:83	LTBP1	79:83	LTBP1	79:83	POGLUT2 and POGLUT3 O-glucosylate multiple EGF repeats in fibrillin-1, -2, and LTBP1 and promote secretion of fibrillin-1.
34411563	0	17	from	repeats	47:53	arg1	fibrillin-1					58:68	fibrillin-1	58:68	fibrillin-1	58:68	POGLUT2 and POGLUT3 O-glucosylate multiple EGF repeats in fibrillin-1, -2, and LTBP1 and promote secretion of fibrillin-1.
34411563	3	18	theme	EGF	500:502	arg1	repeats					505:511	the 47 epidermal growth factor-like (EGF) repeats	463:511	the 47 epidermal growth factor-like (EGF) repeats of FBN1	463:519	Mutations within the 47 epidermal growth factor-like (EGF) repeats of FBN1 cause autosomal dominant disorders including Marfan Syndrome, which is characterized by disrupted TGF-β signaling.
34411563	6	19	theme	most	970:973	arg1	sites					975:979	most sites	970:979	most sites	970:979	While most sites are modified by both enzymes, some sites show a preference for either POGLUT2 or POGLUT3.
34411563	9	20	theme	In vitro	1340:1347	arg1	assays					1359:1364	In vitro secretion assays	1340:1364	In vitro secretion assays using the N-terminal portion of recombinant FBN1	1340:1413	In vitro secretion assays using the N-terminal portion of recombinant FBN1 revealed reduced FBN1 secretion in POGLUT2 knockout, POGLUT3 knockout, and POGLUT2 and 3 double-knockout HEK293T cells compared with wild type.
34411563	4	21	theme	repeats	796:802	arg1	fraction					780:787	a small fraction	772:787	a small fraction of EGF repeats on Notch	772:811	We recently identified two novel protein O-glucosyltransferases, Protein O-glucosyltransferase 2 (POGLUT2) and 3 (POGLUT3), that modify a small fraction of EGF repeats on Notch.
34411563	5	22	theme	EGF	912:914	arg1	repeats					916:922	the EGF repeats	908:922	the EGF repeats on FBN1, fibrillin-2 (FBN2), and LTBP1	908:961	Here, using mass spectral analysis, we show that POGLUT2 and POGLUT3 also modify over half of the EGF repeats on FBN1, fibrillin-2 (FBN2), and LTBP1.
34411563	5	23	from	repeats	916:922	arg1	FBN1					927:930	FBN1	927:930	FBN1	927:930	Here, using mass spectral analysis, we show that POGLUT2 and POGLUT3 also modify over half of the EGF repeats on FBN1, fibrillin-2 (FBN2), and LTBP1.
34411563	5	23	from	repeats	916:922	arg1	LTBP1					957:961	LTBP1	957:961	LTBP1	957:961	Here, using mass spectral analysis, we show that POGLUT2 and POGLUT3 also modify over half of the EGF repeats on FBN1, fibrillin-2 (FBN2), and LTBP1.
34411563	5	23	from	repeats	916:922	arg1	FBN2					946:949	FBN2	946:949	FBN2	946:949	Here, using mass spectral analysis, we show that POGLUT2 and POGLUT3 also modify over half of the EGF repeats on FBN1, fibrillin-2 (FBN2), and LTBP1.
34411563	5	23	from	repeats	916:922	arg1	fibrillin-2					933:943	fibrillin-2	933:943	fibrillin-2 (FBN2)	933:950	Here, using mass spectral analysis, we show that POGLUT2 and POGLUT3 also modify over half of the EGF repeats on FBN1, fibrillin-2 (FBN2), and LTBP1.
34411563	11	24	theme	disease	1772:1778	arg1	variants					1780:1787	disease variants	1772:1787	disease variants in these proteins	1772:1805	It will be interesting to see how disease variants in these proteins affect their O-glucosylation.
34411563	10	25	theme	O-glucosylate	1624:1636	arg1	substrates					1646:1655	O-glucosylate protein substrates	1624:1655	O-glucosylate protein substrates	1624:1655	These results illustrate that POGLUT2 and 3 function together to O-glucosylate protein substrates and that these modifications play a role in the secretion of substrate proteins.
34411563	1	26	dep	heart	279:283	arg1	the					275:277	the	275:277	the	275:277	Fibrillin-1 (FBN1) is the major component of extracellular matrix microfibrils, which are required for proper development of elastic tissues, including the heart and lungs.
34411563	9	27	theme	wild	1548:1551	arg1	type					1553:1556	wild type	1548:1556	wild type	1548:1556	In vitro secretion assays using the N-terminal portion of recombinant FBN1 revealed reduced FBN1 secretion in POGLUT2 knockout, POGLUT3 knockout, and POGLUT2 and 3 double-knockout HEK293T cells compared with wild type.
34411563	7	28	theme	POGLUT1	1107:1113	arg1	POGLUT3					1083:1089	POGLUT3	1083:1089	POGLUT3	1083:1089	POGLUT2 and POGLUT3 are homologs of POGLUT1, which stabilizes Notch proteins by addition of O-glucose to Notch EGF repeats.
34411563	7	28	theme	POGLUT1	1107:1113	arg1	POGLUT2					1071:1077	POGLUT2	1071:1077	POGLUT2	1071:1077	POGLUT2 and POGLUT3 are homologs of POGLUT1, which stabilizes Notch proteins by addition of O-glucose to Notch EGF repeats.
34411563	7	28	theme	POGLUT1	1107:1113	arg1	homologs					1095:1102	homologs	1095:1102	homologs	1095:1102	POGLUT2 and POGLUT3 are homologs of POGLUT1, which stabilizes Notch proteins by addition of O-glucose to Notch EGF repeats.
34411563	3	29	theme	autosomal	527:535	arg1	disorders					546:554	autosomal dominant disorders	527:554	autosomal dominant disorders including Marfan Syndrome, which is characterized by disrupted TGF-β signaling	527:633	Mutations within the 47 epidermal growth factor-like (EGF) repeats of FBN1 cause autosomal dominant disorders including Marfan Syndrome, which is characterized by disrupted TGF-β signaling.
34411563	3	29	theme	autosomal	527:535	arg1	Syndrome					573:580	Marfan Syndrome	566:580	Marfan Syndrome	566:580	Mutations within the 47 epidermal growth factor-like (EGF) repeats of FBN1 cause autosomal dominant disorders including Marfan Syndrome, which is characterized by disrupted TGF-β signaling.
34411563	4	30	from	Notch	807:811	arg1	fraction					780:787	a small fraction	772:787	a small fraction of EGF repeats on Notch	772:811	We recently identified two novel protein O-glucosyltransferases, Protein O-glucosyltransferase 2 (POGLUT2) and 3 (POGLUT3), that modify a small fraction of EGF repeats on Notch.
34411563	1	31	theme	major	149:153	arg1	component					155:163	the major component	145:163	the major component of extracellular matrix microfibrils, which are required for proper development of elastic tissues, including the heart and lungs	145:293	Fibrillin-1 (FBN1) is the major component of extracellular matrix microfibrils, which are required for proper development of elastic tissues, including the heart and lungs.
34411563	1	31	theme	major	149:153	arg1	Fibrillin-1					123:133	Fibrillin-1	123:133	Fibrillin-1 (FBN1)	123:140	Fibrillin-1 (FBN1) is the major component of extracellular matrix microfibrils, which are required for proper development of elastic tissues, including the heart and lungs.
34411563	0	32	theme	POGLUT2	0:6	arg1	repeats					47:53	POGLUT2 and POGLUT3 O-glucosylate multiple EGF repeats	0:53	POGLUT2 and POGLUT3 O-glucosylate multiple EGF repeats in fibrillin-1, -2, and LTBP1	0:83	POGLUT2 and POGLUT3 O-glucosylate multiple EGF repeats in fibrillin-1, -2, and LTBP1 and promote secretion of fibrillin-1.
34411563	1	33	theme	elastic	248:254	arg1	heart					279:283	heart	279:283	heart	279:283	Fibrillin-1 (FBN1) is the major component of extracellular matrix microfibrils, which are required for proper development of elastic tissues, including the heart and lungs.
34411563	1	33	theme	elastic	248:254	arg1	tissues					256:262	elastic tissues	248:262	elastic tissues	248:262	Fibrillin-1 (FBN1) is the major component of extracellular matrix microfibrils, which are required for proper development of elastic tissues, including the heart and lungs.
34411563	1	33	theme	elastic	248:254	arg1	lungs					289:293	lungs	289:293	lungs	289:293	Fibrillin-1 (FBN1) is the major component of extracellular matrix microfibrils, which are required for proper development of elastic tissues, including the heart and lungs.
34411563	3	34	theme	dominant	537:544	arg1	disorders					546:554	autosomal dominant disorders	527:554	autosomal dominant disorders including Marfan Syndrome, which is characterized by disrupted TGF-β signaling	527:633	Mutations within the 47 epidermal growth factor-like (EGF) repeats of FBN1 cause autosomal dominant disorders including Marfan Syndrome, which is characterized by disrupted TGF-β signaling.
34411563	3	34	theme	dominant	537:544	arg1	Syndrome					573:580	Marfan Syndrome	566:580	Marfan Syndrome	566:580	Mutations within the 47 epidermal growth factor-like (EGF) repeats of FBN1 cause autosomal dominant disorders including Marfan Syndrome, which is characterized by disrupted TGF-β signaling.
34411563	6	35	mod	modified	985:992	arg1	sites					975:979	most sites	970:979	most sites	970:979	While most sites are modified by both enzymes, some sites show a preference for either POGLUT2 or POGLUT3.
34411563	6	35	mod	modified	985:992	arg3	enzymes					1002:1008	both enzymes	997:1008	both enzymes	997:1008	While most sites are modified by both enzymes, some sites show a preference for either POGLUT2 or POGLUT3.
34411563	5	36	theme	mass	826:829	arg1	analysis					840:847	mass spectral analysis	826:847	mass spectral analysis	826:847	Here, using mass spectral analysis, we show that POGLUT2 and POGLUT3 also modify over half of the EGF repeats on FBN1, fibrillin-2 (FBN2), and LTBP1.
34411563	0	37	theme	O-glucosylate	20:32	arg1	repeats					47:53	POGLUT2 and POGLUT3 O-glucosylate multiple EGF repeats	0:53	POGLUT2 and POGLUT3 O-glucosylate multiple EGF repeats in fibrillin-1, -2, and LTBP1	0:83	POGLUT2 and POGLUT3 O-glucosylate multiple EGF repeats in fibrillin-1, -2, and LTBP1 and promote secretion of fibrillin-1.
34411563	1	38	theme	tissues	256:262	arg1	development					233:243	proper development	226:243	proper development of elastic tissues, including the heart and lungs	226:293	Fibrillin-1 (FBN1) is the major component of extracellular matrix microfibrils, which are required for proper development of elastic tissues, including the heart and lungs.
34411563	3	39	theme	FBN1	516:519	arg1	repeats					505:511	the 47 epidermal growth factor-like (EGF) repeats	463:511	the 47 epidermal growth factor-like (EGF) repeats of FBN1	463:519	Mutations within the 47 epidermal growth factor-like (EGF) repeats of FBN1 cause autosomal dominant disorders including Marfan Syndrome, which is characterized by disrupted TGF-β signaling.
34411563	8	40	theme	EGF	1260:1262	arg1	repeat					1264:1269	a folded versus unfolded EGF repeat	1235:1269	a folded versus unfolded EGF repeat	1235:1269	Like POGLUT1, POGLUT2 and 3 can discern a folded versus unfolded EGF repeat, suggesting POGLUT2 and 3 are involved in a protein folding pathway.
34411563	7	41	theme	EGF	1182:1184	arg1	repeats					1186:1192	Notch EGF repeats	1176:1192	Notch EGF repeats	1176:1192	POGLUT2 and POGLUT3 are homologs of POGLUT1, which stabilizes Notch proteins by addition of O-glucose to Notch EGF repeats.
34411563	0	42	theme	POGLUT3	12:18	arg1	repeats					47:53	POGLUT2 and POGLUT3 O-glucosylate multiple EGF repeats	0:53	POGLUT2 and POGLUT3 O-glucosylate multiple EGF repeats in fibrillin-1, -2, and LTBP1	0:83	POGLUT2 and POGLUT3 O-glucosylate multiple EGF repeats in fibrillin-1, -2, and LTBP1 and promote secretion of fibrillin-1.
34411563	3	43	theme	TGF-β	619:623	arg1	signaling					625:633	disrupted TGF-β signaling	609:633	disrupted TGF-β signaling	609:633	Mutations within the 47 epidermal growth factor-like (EGF) repeats of FBN1 cause autosomal dominant disorders including Marfan Syndrome, which is characterized by disrupted TGF-β signaling.
34411563	4	44	theme	protein	669:675	arg1	O-glucosyltransferases					677:698	two novel protein O-glucosyltransferases	659:698	two novel protein O-glucosyltransferases	659:698	We recently identified two novel protein O-glucosyltransferases, Protein O-glucosyltransferase 2 (POGLUT2) and 3 (POGLUT3), that modify a small fraction of EGF repeats on Notch.
34411563	4	44	theme	protein	669:675	arg1	O-glucosyltransferase					709:729	Protein O-glucosyltransferase 2	701:731	Protein O-glucosyltransferase 2 (POGLUT2)	701:741	We recently identified two novel protein O-glucosyltransferases, Protein O-glucosyltransferase 2 (POGLUT2) and 3 (POGLUT3), that modify a small fraction of EGF repeats on Notch.
34411563	4	44	theme	protein	669:675	arg1	3					747:747	3	747:747	3	747:747	We recently identified two novel protein O-glucosyltransferases, Protein O-glucosyltransferase 2 (POGLUT2) and 3 (POGLUT3), that modify a small fraction of EGF repeats on Notch.
34411563	5	45	from	fibrillin-2	933:943	arg1	half					900:903	half	900:903	half of the EGF repeats on FBN1, fibrillin-2 (FBN2), and LTBP1	900:961	Here, using mass spectral analysis, we show that POGLUT2 and POGLUT3 also modify over half of the EGF repeats on FBN1, fibrillin-2 (FBN2), and LTBP1.
34411563	1	46	theme	extracellular	168:180	arg1	microfibrils					189:200	extracellular matrix microfibrils	168:200	extracellular matrix microfibrils	168:200	Fibrillin-1 (FBN1) is the major component of extracellular matrix microfibrils, which are required for proper development of elastic tissues, including the heart and lungs.
34411563	0	47	theme	EGF	43:45	arg1	repeats					47:53	POGLUT2 and POGLUT3 O-glucosylate multiple EGF repeats	0:53	POGLUT2 and POGLUT3 O-glucosylate multiple EGF repeats in fibrillin-1, -2, and LTBP1	0:83	POGLUT2 and POGLUT3 O-glucosylate multiple EGF repeats in fibrillin-1, -2, and LTBP1 and promote secretion of fibrillin-1.
34411563	7	48	theme	Notch	1176:1180	arg1	repeats					1186:1192	Notch EGF repeats	1176:1192	Notch EGF repeats	1176:1192	POGLUT2 and POGLUT3 are homologs of POGLUT1, which stabilizes Notch proteins by addition of O-glucose to Notch EGF repeats.
34411563	9	49	theme	secretion	1349:1357	arg1	assays					1359:1364	In vitro secretion assays	1340:1364	In vitro secretion assays using the N-terminal portion of recombinant FBN1	1340:1413	In vitro secretion assays using the N-terminal portion of recombinant FBN1 revealed reduced FBN1 secretion in POGLUT2 knockout, POGLUT3 knockout, and POGLUT2 and 3 double-knockout HEK293T cells compared with wild type.
34411563	7	50	theme	Notch	1133:1137	arg1	proteins					1139:1146	Notch proteins	1133:1146	Notch proteins	1133:1146	POGLUT2 and POGLUT3 are homologs of POGLUT1, which stabilizes Notch proteins by addition of O-glucose to Notch EGF repeats.
34411563	3	51	theme	Marfan	566:571	arg1	Syndrome					573:580	Marfan Syndrome	566:580	Marfan Syndrome	566:580	Mutations within the 47 epidermal growth factor-like (EGF) repeats of FBN1 cause autosomal dominant disorders including Marfan Syndrome, which is characterized by disrupted TGF-β signaling.
34411563	1	52	theme	matrix	182:187	arg1	microfibrils					189:200	extracellular matrix microfibrils	168:200	extracellular matrix microfibrils	168:200	Fibrillin-1 (FBN1) is the major component of extracellular matrix microfibrils, which are required for proper development of elastic tissues, including the heart and lungs.
34411563	0	53	theme	multiple	34:41	arg1	repeats					47:53	POGLUT2 and POGLUT3 O-glucosylate multiple EGF repeats	0:53	POGLUT2 and POGLUT3 O-glucosylate multiple EGF repeats in fibrillin-1, -2, and LTBP1	0:83	POGLUT2 and POGLUT3 O-glucosylate multiple EGF repeats in fibrillin-1, -2, and LTBP1 and promote secretion of fibrillin-1.
34411563	0	54	theme	fibrillin-1	110:120	arg1	secretion					97:105	secretion	97:105	secretion of fibrillin-1	97:120	POGLUT2 and POGLUT3 O-glucosylate multiple EGF repeats in fibrillin-1, -2, and LTBP1 and promote secretion of fibrillin-1.
34411563	2	55	with	interactions	320:331	arg1	TGF					373:375	TGF	373:375	TGF	373:375	Through protein-protein interactions with latent transforming growth factor (TGF) β-binding protein 1 (LTBP1), microfibrils regulate TGF-β signaling.
34411563	2	55	with	interactions	320:331	arg1	factor					365:370	latent transforming growth factor	338:370	latent transforming growth factor (TGF) β-binding protein 1 (LTBP1)	338:404	Through protein-protein interactions with latent transforming growth factor (TGF) β-binding protein 1 (LTBP1), microfibrils regulate TGF-β signaling.
34411563	2	55	with	interactions	320:331	arg1	LTBP1					399:403	LTBP1	399:403	LTBP1	399:403	Through protein-protein interactions with latent transforming growth factor (TGF) β-binding protein 1 (LTBP1), microfibrils regulate TGF-β signaling.
34411563	4	56	theme	small	774:778	arg1	fraction					780:787	a small fraction	772:787	a small fraction of EGF repeats on Notch	772:811	We recently identified two novel protein O-glucosyltransferases, Protein O-glucosyltransferase 2 (POGLUT2) and 3 (POGLUT3), that modify a small fraction of EGF repeats on Notch.
34411563	11	57	from	variants	1780:1787	arg1	proteins					1798:1805	these proteins	1792:1805	these proteins	1792:1805	It will be interesting to see how disease variants in these proteins affect their O-glucosylation.
34411563	1	58	theme	microfibrils	189:200	arg1	component					155:163	the major component	145:163	the major component of extracellular matrix microfibrils, which are required for proper development of elastic tissues, including the heart and lungs	145:293	Fibrillin-1 (FBN1) is the major component of extracellular matrix microfibrils, which are required for proper development of elastic tissues, including the heart and lungs.
34411563	1	58	theme	microfibrils	189:200	arg1	Fibrillin-1					123:133	Fibrillin-1	123:133	Fibrillin-1 (FBN1)	123:140	Fibrillin-1 (FBN1) is the major component of extracellular matrix microfibrils, which are required for proper development of elastic tissues, including the heart and lungs.
34411563	2	59	theme	TGF-β	429:433	arg1	signaling					435:443	TGF-β signaling	429:443	TGF-β signaling	429:443	Through protein-protein interactions with latent transforming growth factor (TGF) β-binding protein 1 (LTBP1), microfibrils regulate TGF-β signaling.
34411563	5	60	theme	spectral	831:838	arg1	analysis					840:847	mass spectral analysis	826:847	mass spectral analysis	826:847	Here, using mass spectral analysis, we show that POGLUT2 and POGLUT3 also modify over half of the EGF repeats on FBN1, fibrillin-2 (FBN2), and LTBP1.
34411563	3	61	theme	disrupted	609:617	arg1	signaling					625:633	disrupted TGF-β signaling	609:633	disrupted TGF-β signaling	609:633	Mutations within the 47 epidermal growth factor-like (EGF) repeats of FBN1 cause autosomal dominant disorders including Marfan Syndrome, which is characterized by disrupted TGF-β signaling.
34411563	4	62	theme	EGF	792:794	arg1	repeats					796:802	EGF repeats	792:802	EGF repeats on Notch	792:811	We recently identified two novel protein O-glucosyltransferases, Protein O-glucosyltransferase 2 (POGLUT2) and 3 (POGLUT3), that modify a small fraction of EGF repeats on Notch.
34411563	4	63	theme	Protein	701:707	arg1	O-glucosyltransferases					677:698	two novel protein O-glucosyltransferases	659:698	two novel protein O-glucosyltransferases	659:698	We recently identified two novel protein O-glucosyltransferases, Protein O-glucosyltransferase 2 (POGLUT2) and 3 (POGLUT3), that modify a small fraction of EGF repeats on Notch.
34411563	4	63	theme	Protein	701:707	arg1	O-glucosyltransferase					709:729	Protein O-glucosyltransferase 2	701:731	Protein O-glucosyltransferase 2 (POGLUT2)	701:741	We recently identified two novel protein O-glucosyltransferases, Protein O-glucosyltransferase 2 (POGLUT2) and 3 (POGLUT3), that modify a small fraction of EGF repeats on Notch.
34411563	4	63	theme	Protein	701:707	arg1	POGLUT2					734:740	POGLUT2	734:740	POGLUT2	734:740	We recently identified two novel protein O-glucosyltransferases, Protein O-glucosyltransferase 2 (POGLUT2) and 3 (POGLUT3), that modify a small fraction of EGF repeats on Notch.
34411563	10	64	theme	proteins	1728:1735	arg1	secretion					1705:1713	the secretion	1701:1713	the secretion of substrate proteins	1701:1735	These results illustrate that POGLUT2 and 3 function together to O-glucosylate protein substrates and that these modifications play a role in the secretion of substrate proteins.
34411563	8	65	theme	folding	1323:1329	arg1	pathway					1331:1337	a protein folding pathway	1313:1337	a protein folding pathway	1313:1337	Like POGLUT1, POGLUT2 and 3 can discern a folded versus unfolded EGF repeat, suggesting POGLUT2 and 3 are involved in a protein folding pathway.
34411563	9	66	theme	knockout	1476:1483	arg1	cells					1528:1532	POGLUT2 knockout, POGLUT3 knockout, and POGLUT2 and 3 double-knockout HEK293T cells	1450:1532	POGLUT2 knockout, POGLUT3 knockout, and POGLUT2 and 3 double-knockout HEK293T cells	1450:1532	In vitro secretion assays using the N-terminal portion of recombinant FBN1 revealed reduced FBN1 secretion in POGLUT2 knockout, POGLUT3 knockout, and POGLUT2 and 3 double-knockout HEK293T cells compared with wild type.
34411563	4	67	from	fraction	780:787	arg1	Notch					807:811	Notch	807:811	Notch	807:811	We recently identified two novel protein O-glucosyltransferases, Protein O-glucosyltransferase 2 (POGLUT2) and 3 (POGLUT3), that modify a small fraction of EGF repeats on Notch.
34411563	2	68	theme	protein-protein	304:318	arg1	interactions					320:331	protein-protein interactions	304:331	protein-protein interactions with latent transforming growth factor (TGF) β-binding protein 1 (LTBP1)	304:404	Through protein-protein interactions with latent transforming growth factor (TGF) β-binding protein 1 (LTBP1), microfibrils regulate TGF-β signaling.
34411563	10	69	theme	protein	1638:1644	arg1	substrates					1646:1655	O-glucosylate protein substrates	1624:1655	O-glucosylate protein substrates	1624:1655	These results illustrate that POGLUT2 and 3 function together to O-glucosylate protein substrates and that these modifications play a role in the secretion of substrate proteins.
34411563	8	70	theme	protein	1315:1321	arg1	pathway					1331:1337	a protein folding pathway	1313:1337	a protein folding pathway	1313:1337	Like POGLUT1, POGLUT2 and 3 can discern a folded versus unfolded EGF repeat, suggesting POGLUT2 and 3 are involved in a protein folding pathway.
34411563	5	71	theme	repeats	916:922	arg1	half					900:903	half	900:903	half of the EGF repeats on FBN1, fibrillin-2 (FBN2), and LTBP1	900:961	Here, using mass spectral analysis, we show that POGLUT2 and POGLUT3 also modify over half of the EGF repeats on FBN1, fibrillin-2 (FBN2), and LTBP1.
34411563	8	72	theme	unfolded	1251:1258	arg1	repeat					1264:1269	a folded versus unfolded EGF repeat	1235:1269	a folded versus unfolded EGF repeat	1235:1269	Like POGLUT1, POGLUT2 and 3 can discern a folded versus unfolded EGF repeat, suggesting POGLUT2 and 3 are involved in a protein folding pathway.
34411563	9	73	theme	reduced	1424:1430	arg1	secretion					1437:1445	reduced FBN1 secretion	1424:1445	reduced FBN1 secretion	1424:1445	In vitro secretion assays using the N-terminal portion of recombinant FBN1 revealed reduced FBN1 secretion in POGLUT2 knockout, POGLUT3 knockout, and POGLUT2 and 3 double-knockout HEK293T cells compared with wild type.
34411563	2	74	dep	factor	365:370	arg1	protein					388:394	β-binding protein 1	378:396	latent transforming growth factor (TGF) β-binding protein 1 (LTBP1)	338:404	Through protein-protein interactions with latent transforming growth factor (TGF) β-binding protein 1 (LTBP1), microfibrils regulate TGF-β signaling.
34411563	9	75	theme	N-terminal	1376:1385	arg1	portion					1387:1393	the N-terminal portion	1372:1393	the N-terminal portion of recombinant FBN1	1372:1413	In vitro secretion assays using the N-terminal portion of recombinant FBN1 revealed reduced FBN1 secretion in POGLUT2 knockout, POGLUT3 knockout, and POGLUT2 and 3 double-knockout HEK293T cells compared with wild type.
34411563	5	76	from	LTBP1	957:961	arg1	half					900:903	half	900:903	half of the EGF repeats on FBN1, fibrillin-2 (FBN2), and LTBP1	900:961	Here, using mass spectral analysis, we show that POGLUT2 and POGLUT3 also modify over half of the EGF repeats on FBN1, fibrillin-2 (FBN2), and LTBP1.
34411563	2	77	theme	β-binding	378:386	arg1	protein					388:394	β-binding protein 1	378:396	latent transforming growth factor (TGF) β-binding protein 1 (LTBP1)	338:404	Through protein-protein interactions with latent transforming growth factor (TGF) β-binding protein 1 (LTBP1), microfibrils regulate TGF-β signaling.
34411563	9	78	theme	POGLUT2	1490:1496	arg1	cells					1528:1532	POGLUT2 knockout, POGLUT3 knockout, and POGLUT2 and 3 double-knockout HEK293T cells	1450:1532	POGLUT2 knockout, POGLUT3 knockout, and POGLUT2 and 3 double-knockout HEK293T cells	1450:1532	In vitro secretion assays using the N-terminal portion of recombinant FBN1 revealed reduced FBN1 secretion in POGLUT2 knockout, POGLUT3 knockout, and POGLUT2 and 3 double-knockout HEK293T cells compared with wild type.
34411563	2	79	theme	growth	358:363	arg1	TGF					373:375	TGF	373:375	TGF	373:375	Through protein-protein interactions with latent transforming growth factor (TGF) β-binding protein 1 (LTBP1), microfibrils regulate TGF-β signaling.
34411563	2	79	theme	growth	358:363	arg1	factor					365:370	latent transforming growth factor	338:370	latent transforming growth factor (TGF) β-binding protein 1 (LTBP1)	338:404	Through protein-protein interactions with latent transforming growth factor (TGF) β-binding protein 1 (LTBP1), microfibrils regulate TGF-β signaling.
34411563	2	79	theme	growth	358:363	arg1	LTBP1					399:403	LTBP1	399:403	LTBP1	399:403	Through protein-protein interactions with latent transforming growth factor (TGF) β-binding protein 1 (LTBP1), microfibrils regulate TGF-β signaling.
34411563	9	80	theme	knockout	1458:1465	arg1	cells					1528:1532	POGLUT2 knockout, POGLUT3 knockout, and POGLUT2 and 3 double-knockout HEK293T cells	1450:1532	POGLUT2 knockout, POGLUT3 knockout, and POGLUT2 and 3 double-knockout HEK293T cells	1450:1532	In vitro secretion assays using the N-terminal portion of recombinant FBN1 revealed reduced FBN1 secretion in POGLUT2 knockout, POGLUT3 knockout, and POGLUT2 and 3 double-knockout HEK293T cells compared with wild type.
34411563	7	81	theme	O-glucose	1163:1171	arg1	addition					1151:1158	addition	1151:1158	addition of O-glucose to Notch EGF repeats	1151:1192	POGLUT2 and POGLUT3 are homologs of POGLUT1, which stabilizes Notch proteins by addition of O-glucose to Notch EGF repeats.
34411563	2	82	theme	transforming	345:356	arg1	TGF					373:375	TGF	373:375	TGF	373:375	Through protein-protein interactions with latent transforming growth factor (TGF) β-binding protein 1 (LTBP1), microfibrils regulate TGF-β signaling.
34411563	2	82	theme	transforming	345:356	arg1	factor					365:370	latent transforming growth factor	338:370	latent transforming growth factor (TGF) β-binding protein 1 (LTBP1)	338:404	Through protein-protein interactions with latent transforming growth factor (TGF) β-binding protein 1 (LTBP1), microfibrils regulate TGF-β signaling.
34411563	2	82	theme	transforming	345:356	arg1	LTBP1					399:403	LTBP1	399:403	LTBP1	399:403	Through protein-protein interactions with latent transforming growth factor (TGF) β-binding protein 1 (LTBP1), microfibrils regulate TGF-β signaling.
30379171	0	0	theme	post-translational	105:122	arg1	modifications					124:136	protein post-translational modifications	97:136	protein post-translational modifications	97:136	A triarylphosphine-trimethylpiperidine reagent for the one-step derivatization and enrichment of protein post-translational modifications and identification by mass spectrometry.
30379171	2	1	theme	O-GlcNAc	515:522	arg1	peptides					524:531	3293 O-GlcNAc peptides	510:531	3293 O-GlcNAc peptides	510:531	Facile sample recovery, enhanced ionization and fragmentation in MS of the enriched PTM peptides are achieved, which leads to the identification of 3293 O-GlcNAc peptides and the location of 1706 sites in HeLa cells and efficiently expands the current mapping scale.
30379171	2	2	from	identification	492:505	arg1	cells					572:576	HeLa cells	567:576	HeLa cells	567:576	Facile sample recovery, enhanced ionization and fragmentation in MS of the enriched PTM peptides are achieved, which leads to the identification of 3293 O-GlcNAc peptides and the location of 1706 sites in HeLa cells and efficiently expands the current mapping scale.
30379171	1	3	theme	new	191:193	arg1	capable					211:217	capable	211:217	capable	211:217	We report a new reagent that is capable of both chemical derivatization and selective enrichment of azide-labeled PTM peptides for sensitive identification by mass spectrometry (MS).
30379171	1	3	theme	new	191:193	arg1	reagent					195:201	a new reagent	189:201	a new reagent that is capable of both chemical derivatization and selective enrichment of azide-labeled PTM peptides for sensitive identification by mass spectrometry (MS)	189:359	We report a new reagent that is capable of both chemical derivatization and selective enrichment of azide-labeled PTM peptides for sensitive identification by mass spectrometry (MS).
30379171	1	4	theme	PTM	293:295	arg1	peptides					297:304	azide-labeled PTM peptides	279:304	azide-labeled PTM peptides for sensitive identification by mass spectrometry (MS)	279:359	We report a new reagent that is capable of both chemical derivatization and selective enrichment of azide-labeled PTM peptides for sensitive identification by mass spectrometry (MS).
30379171	0	5	theme	protein	97:103	arg1	modifications					124:136	protein post-translational modifications	97:136	protein post-translational modifications	97:136	A triarylphosphine-trimethylpiperidine reagent for the one-step derivatization and enrichment of protein post-translational modifications and identification by mass spectrometry.
30379171	2	6	theme	enhanced	386:393	arg1	ionization					395:404	enhanced ionization	386:404	enhanced ionization	386:404	Facile sample recovery, enhanced ionization and fragmentation in MS of the enriched PTM peptides are achieved, which leads to the identification of 3293 O-GlcNAc peptides and the location of 1706 sites in HeLa cells and efficiently expands the current mapping scale.
30379171	1	7	theme	peptides	297:304	arg1	derivatization					236:249	chemical derivatization	227:249	chemical derivatization	227:249	We report a new reagent that is capable of both chemical derivatization and selective enrichment of azide-labeled PTM peptides for sensitive identification by mass spectrometry (MS).
30379171	1	7	theme	peptides	297:304	arg1	enrichment					265:274	selective enrichment	255:274	selective enrichment of azide-labeled PTM peptides for sensitive identification by mass spectrometry (MS)	255:359	We report a new reagent that is capable of both chemical derivatization and selective enrichment of azide-labeled PTM peptides for sensitive identification by mass spectrometry (MS).
30379171	2	8	theme	mapping	614:620	arg1	scale					622:626	the current mapping scale	602:626	the current mapping scale	602:626	Facile sample recovery, enhanced ionization and fragmentation in MS of the enriched PTM peptides are achieved, which leads to the identification of 3293 O-GlcNAc peptides and the location of 1706 sites in HeLa cells and efficiently expands the current mapping scale.
30379171	0	9	theme	modifications	124:136	arg1	enrichment					83:92	enrichment	83:92	enrichment	83:92	A triarylphosphine-trimethylpiperidine reagent for the one-step derivatization and enrichment of protein post-translational modifications and identification by mass spectrometry.
30379171	0	9	theme	modifications	124:136	arg1	derivatization					64:77	one-step derivatization	55:77	one-step derivatization	55:77	A triarylphosphine-trimethylpiperidine reagent for the one-step derivatization and enrichment of protein post-translational modifications and identification by mass spectrometry.
30379171	2	10	theme	current	606:612	arg1	scale					622:626	the current mapping scale	602:626	the current mapping scale	602:626	Facile sample recovery, enhanced ionization and fragmentation in MS of the enriched PTM peptides are achieved, which leads to the identification of 3293 O-GlcNAc peptides and the location of 1706 sites in HeLa cells and efficiently expands the current mapping scale.
30379171	2	11	theme	ionization	395:404	arg1	peptides					450:457	Facile sample recovery, enhanced ionization and fragmentation in MS of the enriched PTM peptides	362:457	Facile sample recovery, enhanced ionization and fragmentation in MS of the enriched PTM peptides	362:457	Facile sample recovery, enhanced ionization and fragmentation in MS of the enriched PTM peptides are achieved, which leads to the identification of 3293 O-GlcNAc peptides and the location of 1706 sites in HeLa cells and efficiently expands the current mapping scale.
30379171	1	12	theme	sensitive	310:318	arg1	identification					320:333	sensitive identification	310:333	sensitive identification by mass spectrometry (MS)	310:359	We report a new reagent that is capable of both chemical derivatization and selective enrichment of azide-labeled PTM peptides for sensitive identification by mass spectrometry (MS).
30379171	2	13	theme	HeLa	567:570	arg1	cells					572:576	HeLa cells	567:576	HeLa cells	567:576	Facile sample recovery, enhanced ionization and fragmentation in MS of the enriched PTM peptides are achieved, which leads to the identification of 3293 O-GlcNAc peptides and the location of 1706 sites in HeLa cells and efficiently expands the current mapping scale.
30379171	2	14	from	recovery	376:383	arg1	MS					427:428	MS	427:428	MS	427:428	Facile sample recovery, enhanced ionization and fragmentation in MS of the enriched PTM peptides are achieved, which leads to the identification of 3293 O-GlcNAc peptides and the location of 1706 sites in HeLa cells and efficiently expands the current mapping scale.
30379171	2	15	from	ionization	395:404	arg1	MS					427:428	MS	427:428	MS	427:428	Facile sample recovery, enhanced ionization and fragmentation in MS of the enriched PTM peptides are achieved, which leads to the identification of 3293 O-GlcNAc peptides and the location of 1706 sites in HeLa cells and efficiently expands the current mapping scale.
30379171	2	16	from	sites	558:562	arg1	cells					572:576	HeLa cells	567:576	HeLa cells	567:576	Facile sample recovery, enhanced ionization and fragmentation in MS of the enriched PTM peptides are achieved, which leads to the identification of 3293 O-GlcNAc peptides and the location of 1706 sites in HeLa cells and efficiently expands the current mapping scale.
30379171	0	17	theme	triarylphosphine-trimethylpiperidine	2:37	arg1	reagent					39:45	A triarylphosphine-trimethylpiperidine reagent	0:45	A triarylphosphine-trimethylpiperidine reagent for the one-step derivatization and enrichment of protein post-translational modifications	0:136	A triarylphosphine-trimethylpiperidine reagent for the one-step derivatization and enrichment of protein post-translational modifications and identification by mass spectrometry.
30379171	2	18	theme	3293	510:513	arg1	peptides					524:531	3293 O-GlcNAc peptides	510:531	3293 O-GlcNAc peptides	510:531	Facile sample recovery, enhanced ionization and fragmentation in MS of the enriched PTM peptides are achieved, which leads to the identification of 3293 O-GlcNAc peptides and the location of 1706 sites in HeLa cells and efficiently expands the current mapping scale.
30379171	2	19	from	fragmentation	410:422	arg1	MS					427:428	MS	427:428	MS	427:428	Facile sample recovery, enhanced ionization and fragmentation in MS of the enriched PTM peptides are achieved, which leads to the identification of 3293 O-GlcNAc peptides and the location of 1706 sites in HeLa cells and efficiently expands the current mapping scale.
30379171	1	20	theme	mass	338:341	arg1	MS					357:358	MS	357:358	MS	357:358	We report a new reagent that is capable of both chemical derivatization and selective enrichment of azide-labeled PTM peptides for sensitive identification by mass spectrometry (MS).
30379171	1	20	theme	mass	338:341	arg1	spectrometry					343:354	mass spectrometry	338:354	mass spectrometry (MS)	338:359	We report a new reagent that is capable of both chemical derivatization and selective enrichment of azide-labeled PTM peptides for sensitive identification by mass spectrometry (MS).
30379171	0	21	theme	mass	160:163	arg1	spectrometry					165:176	mass spectrometry	160:176	mass spectrometry	160:176	A triarylphosphine-trimethylpiperidine reagent for the one-step derivatization and enrichment of protein post-translational modifications and identification by mass spectrometry.
30379171	1	22	theme	chemical	227:234	arg1	derivatization					236:249	chemical derivatization	227:249	chemical derivatization	227:249	We report a new reagent that is capable of both chemical derivatization and selective enrichment of azide-labeled PTM peptides for sensitive identification by mass spectrometry (MS).
30379171	0	23	theme	one-step	55:62	arg1	derivatization					64:77	one-step derivatization	55:77	one-step derivatization	55:77	A triarylphosphine-trimethylpiperidine reagent for the one-step derivatization and enrichment of protein post-translational modifications and identification by mass spectrometry.
30379171	2	24	theme	PTM	446:448	arg1	recovery					376:383	Facile sample recovery	362:383	Facile sample recovery	362:383	Facile sample recovery, enhanced ionization and fragmentation in MS of the enriched PTM peptides are achieved, which leads to the identification of 3293 O-GlcNAc peptides and the location of 1706 sites in HeLa cells and efficiently expands the current mapping scale.
30379171	2	24	theme	PTM	446:448	arg1	ionization					395:404	enhanced ionization	386:404	enhanced ionization	386:404	Facile sample recovery, enhanced ionization and fragmentation in MS of the enriched PTM peptides are achieved, which leads to the identification of 3293 O-GlcNAc peptides and the location of 1706 sites in HeLa cells and efficiently expands the current mapping scale.
30379171	2	24	theme	PTM	446:448	arg1	fragmentation					410:422	fragmentation	410:422	fragmentation in MS of the enriched PTM	410:448	Facile sample recovery, enhanced ionization and fragmentation in MS of the enriched PTM peptides are achieved, which leads to the identification of 3293 O-GlcNAc peptides and the location of 1706 sites in HeLa cells and efficiently expands the current mapping scale.
30379171	1	25	theme	derivatization	236:249	arg1	capable					211:217	capable	211:217	capable	211:217	We report a new reagent that is capable of both chemical derivatization and selective enrichment of azide-labeled PTM peptides for sensitive identification by mass spectrometry (MS).
30379171	1	25	theme	derivatization	236:249	arg1	reagent					195:201	a new reagent	189:201	a new reagent that is capable of both chemical derivatization and selective enrichment of azide-labeled PTM peptides for sensitive identification by mass spectrometry (MS)	189:359	We report a new reagent that is capable of both chemical derivatization and selective enrichment of azide-labeled PTM peptides for sensitive identification by mass spectrometry (MS).
30379171	2	26	theme	sites	558:562	arg1	location					541:548	the location	537:548	the location of 1706 sites in HeLa cells	537:576	Facile sample recovery, enhanced ionization and fragmentation in MS of the enriched PTM peptides are achieved, which leads to the identification of 3293 O-GlcNAc peptides and the location of 1706 sites in HeLa cells and efficiently expands the current mapping scale.
30379171	2	26	theme	sites	558:562	arg1	identification					492:505	the identification	488:505	the identification of 3293 O-GlcNAc peptides	488:531	Facile sample recovery, enhanced ionization and fragmentation in MS of the enriched PTM peptides are achieved, which leads to the identification of 3293 O-GlcNAc peptides and the location of 1706 sites in HeLa cells and efficiently expands the current mapping scale.
30379171	0	27	dep	derivatization	64:77	arg1	the					51:53	the	51:53	the	51:53	A triarylphosphine-trimethylpiperidine reagent for the one-step derivatization and enrichment of protein post-translational modifications and identification by mass spectrometry.
30379171	2	28	theme	enriched	437:444	arg1	PTM					446:448	the enriched PTM	433:448	the enriched PTM	433:448	Facile sample recovery, enhanced ionization and fragmentation in MS of the enriched PTM peptides are achieved, which leads to the identification of 3293 O-GlcNAc peptides and the location of 1706 sites in HeLa cells and efficiently expands the current mapping scale.
30379171	2	29	from	location	541:548	arg1	cells					572:576	HeLa cells	567:576	HeLa cells	567:576	Facile sample recovery, enhanced ionization and fragmentation in MS of the enriched PTM peptides are achieved, which leads to the identification of 3293 O-GlcNAc peptides and the location of 1706 sites in HeLa cells and efficiently expands the current mapping scale.
30379171	2	30	theme	recovery	376:383	arg1	peptides					450:457	Facile sample recovery, enhanced ionization and fragmentation in MS of the enriched PTM peptides	362:457	Facile sample recovery, enhanced ionization and fragmentation in MS of the enriched PTM peptides	362:457	Facile sample recovery, enhanced ionization and fragmentation in MS of the enriched PTM peptides are achieved, which leads to the identification of 3293 O-GlcNAc peptides and the location of 1706 sites in HeLa cells and efficiently expands the current mapping scale.
30379171	2	31	theme	sample	369:374	arg1	recovery					376:383	Facile sample recovery	362:383	Facile sample recovery	362:383	Facile sample recovery, enhanced ionization and fragmentation in MS of the enriched PTM peptides are achieved, which leads to the identification of 3293 O-GlcNAc peptides and the location of 1706 sites in HeLa cells and efficiently expands the current mapping scale.
30379171	1	32	theme	selective	255:263	arg1	enrichment					265:274	selective enrichment	255:274	selective enrichment of azide-labeled PTM peptides for sensitive identification by mass spectrometry (MS)	255:359	We report a new reagent that is capable of both chemical derivatization and selective enrichment of azide-labeled PTM peptides for sensitive identification by mass spectrometry (MS).
30379171	2	33	theme	Facile	362:367	arg1	recovery					376:383	Facile sample recovery	362:383	Facile sample recovery	362:383	Facile sample recovery, enhanced ionization and fragmentation in MS of the enriched PTM peptides are achieved, which leads to the identification of 3293 O-GlcNAc peptides and the location of 1706 sites in HeLa cells and efficiently expands the current mapping scale.
30379171	1	34	theme	enrichment	265:274	arg1	capable					211:217	capable	211:217	capable	211:217	We report a new reagent that is capable of both chemical derivatization and selective enrichment of azide-labeled PTM peptides for sensitive identification by mass spectrometry (MS).
30379171	1	34	theme	enrichment	265:274	arg1	reagent					195:201	a new reagent	189:201	a new reagent that is capable of both chemical derivatization and selective enrichment of azide-labeled PTM peptides for sensitive identification by mass spectrometry (MS)	189:359	We report a new reagent that is capable of both chemical derivatization and selective enrichment of azide-labeled PTM peptides for sensitive identification by mass spectrometry (MS).
30379171	2	35	theme	fragmentation	410:422	arg1	peptides					450:457	Facile sample recovery, enhanced ionization and fragmentation in MS of the enriched PTM peptides	362:457	Facile sample recovery, enhanced ionization and fragmentation in MS of the enriched PTM peptides	362:457	Facile sample recovery, enhanced ionization and fragmentation in MS of the enriched PTM peptides are achieved, which leads to the identification of 3293 O-GlcNAc peptides and the location of 1706 sites in HeLa cells and efficiently expands the current mapping scale.
30379171	2	36	from	cells	572:576	arg1	location					541:548	the location	537:548	the location of 1706 sites in HeLa cells	537:576	Facile sample recovery, enhanced ionization and fragmentation in MS of the enriched PTM peptides are achieved, which leads to the identification of 3293 O-GlcNAc peptides and the location of 1706 sites in HeLa cells and efficiently expands the current mapping scale.
30379171	2	36	from	cells	572:576	arg1	identification					492:505	the identification	488:505	the identification of 3293 O-GlcNAc peptides	488:531	Facile sample recovery, enhanced ionization and fragmentation in MS of the enriched PTM peptides are achieved, which leads to the identification of 3293 O-GlcNAc peptides and the location of 1706 sites in HeLa cells and efficiently expands the current mapping scale.
30379171	2	37	theme	peptides	524:531	arg1	location					541:548	the location	537:548	the location of 1706 sites in HeLa cells	537:576	Facile sample recovery, enhanced ionization and fragmentation in MS of the enriched PTM peptides are achieved, which leads to the identification of 3293 O-GlcNAc peptides and the location of 1706 sites in HeLa cells and efficiently expands the current mapping scale.
30379171	2	37	theme	peptides	524:531	arg1	identification					492:505	the identification	488:505	the identification of 3293 O-GlcNAc peptides	488:531	Facile sample recovery, enhanced ionization and fragmentation in MS of the enriched PTM peptides are achieved, which leads to the identification of 3293 O-GlcNAc peptides and the location of 1706 sites in HeLa cells and efficiently expands the current mapping scale.
30379171	1	38	theme	azide-labeled	279:291	arg1	peptides					297:304	azide-labeled PTM peptides	279:304	azide-labeled PTM peptides for sensitive identification by mass spectrometry (MS)	279:359	We report a new reagent that is capable of both chemical derivatization and selective enrichment of azide-labeled PTM peptides for sensitive identification by mass spectrometry (MS).
1457416	1	0	theme	A-chain	240:246	arg1	glycans					225:231	the glycans	221:231	the glycans of the A-chain of human plasma alpha 2HS-glycoprotein	221:285	The structure of the glycans of the A-chain of human plasma alpha 2HS-glycoprotein was established from the chemical compositions of its derivatives prepared by sequential enzymatic degradation of the carbohydrate moiety, from the determination of the kind and amount of the monosaccharides liberated after each step of the enzymatic digestion, and from the distinct specificity of the highly purified exoglycosidases.
1457416	4	1	link	1-4-linked	1148:1157	arg1	residues					1169:1176	only beta 1-4-linked galactose residues	1138:1176	only beta 1-4-linked galactose residues	1138:1176	As to the beta-galactosidases, the enzyme isolated from S. pneumoniae cleaves only beta 1-4-linked galactose residues, whereas the bovine testes enzyme acts on both the beta 1-4- and beta 1-3-linked galactose residues.
1457416	1	2	theme	human	251:255	arg1	2HS-glycoprotein					270:285	human plasma alpha 2HS-glycoprotein	251:285	human plasma alpha 2HS-glycoprotein	251:285	The structure of the glycans of the A-chain of human plasma alpha 2HS-glycoprotein was established from the chemical compositions of its derivatives prepared by sequential enzymatic degradation of the carbohydrate moiety, from the determination of the kind and amount of the monosaccharides liberated after each step of the enzymatic digestion, and from the distinct specificity of the highly purified exoglycosidases.
1457416	8	3	theme	biantennary	1697:1707	arg1	N-glycans					1709:1717	two biantennary N-glycans	1693:1717	two biantennary N-glycans	1693:1717	On the basis of these results, the A-chain of alpha 2 HS-glycoprotein was found to possess two biantennary N-glycans and two O-linked trisaccharides.
1457416	2	4	theme	Streptococcus	758:770	arg1	beta-galactosidases					737:755	two beta-galactosidases	733:755	two beta-galactosidases (Streptococcus pneumoniae and bovine testis)	733:800	The exoglycosidases were three sialidases (Vibrio cholerae, fowl plague virus, and Arthrobacter ureafaciens), two beta-galactosidases (Streptococcus pneumoniae and bovine testis), one alpha-N-acetylgalactosaminidase, one beta-N-acetylglucosaminidase, and one alpha-mannosidase.
1457416	2	4	theme	Streptococcus	758:770	arg1	pneumoniae					772:781	Streptococcus pneumoniae	758:781	Streptococcus pneumoniae	758:781	The exoglycosidases were three sialidases (Vibrio cholerae, fowl plague virus, and Arthrobacter ureafaciens), two beta-galactosidases (Streptococcus pneumoniae and bovine testis), one alpha-N-acetylgalactosaminidase, one beta-N-acetylglucosaminidase, and one alpha-mannosidase.
1457416	6	5	with	Man	1477:1479	arg1	activity					1494:1501	greater activity	1486:1501	greater activity for alpha 1-2 and alpha 1-6	1486:1529	Jack bean alpha-mannosidase cleaves alpha 1-2, alpha 1-6, and alpha 1-3 Man with greater activity for alpha 1-2 and alpha 1-6.
1457416	4	6	theme	bovine	1191:1196	arg1	enzyme					1205:1210	the bovine testes enzyme	1187:1210	the bovine testes enzyme	1187:1210	As to the beta-galactosidases, the enzyme isolated from S. pneumoniae cleaves only beta 1-4-linked galactose residues, whereas the bovine testes enzyme acts on both the beta 1-4- and beta 1-3-linked galactose residues.
1457416	1	7	theme	moiety	418:423	arg1	degradation					386:396	sequential enzymatic degradation	365:396	sequential enzymatic degradation of the carbohydrate moiety	365:423	The structure of the glycans of the A-chain of human plasma alpha 2HS-glycoprotein was established from the chemical compositions of its derivatives prepared by sequential enzymatic degradation of the carbohydrate moiety, from the determination of the kind and amount of the monosaccharides liberated after each step of the enzymatic digestion, and from the distinct specificity of the highly purified exoglycosidases.
1457416	4	8	theme	1-4-linked	1148:1157	arg1	residues					1169:1176	only beta 1-4-linked galactose residues	1138:1176	only beta 1-4-linked galactose residues	1138:1176	As to the beta-galactosidases, the enzyme isolated from S. pneumoniae cleaves only beta 1-4-linked galactose residues, whereas the bovine testes enzyme acts on both the beta 1-4- and beta 1-3-linked galactose residues.
1457416	5	9	with	GlcNAc	1359:1364	arg1	activity					1378:1385	higher activity	1371:1385	higher activity	1371:1385	Jack bean beta-N-acetylglucosaminidase cleaves beta 1-2, beta 1-4, and beta 1-6 GlcNAc with higher activity for the beta 1-2.
1457416	0	10	theme	chemical	108:115	arg1	compositions					117:128	the chemical compositions	104:128	the chemical compositions of the derivatives prepared by stepwise degradation with exoglycosidases	104:201	Structure of the N- and O-glycans of the A-chain of human plasma alpha 2HS-glycoprotein as deduced from the chemical compositions of the derivatives prepared by stepwise degradation with exoglycosidases.
1457416	8	11	contain	possess	1685:1691	arg1	A-chain					1637:1643	the A-chain	1633:1643	the A-chain of alpha 2 HS-glycoprotein	1633:1670	On the basis of these results, the A-chain of alpha 2 HS-glycoprotein was found to possess two biantennary N-glycans and two O-linked trisaccharides.
1457416	8	11	contain	possess	1685:1691	arg2	N-glycans					1709:1717	two biantennary N-glycans	1693:1717	two biantennary N-glycans	1693:1717	On the basis of these results, the A-chain of alpha 2 HS-glycoprotein was found to possess two biantennary N-glycans and two O-linked trisaccharides.
1457416	8	11	contain	possess	1685:1691	arg2	trisaccharides					1736:1749	two O-linked trisaccharides	1723:1749	two O-linked trisaccharides	1723:1749	On the basis of these results, the A-chain of alpha 2 HS-glycoprotein was found to possess two biantennary N-glycans and two O-linked trisaccharides.
1457416	0	12	theme	derivatives	137:147	arg1	compositions					117:128	the chemical compositions	104:128	the chemical compositions of the derivatives prepared by stepwise degradation with exoglycosidases	104:201	Structure of the N- and O-glycans of the A-chain of human plasma alpha 2HS-glycoprotein as deduced from the chemical compositions of the derivatives prepared by stepwise degradation with exoglycosidases.
1457416	7	13	link	O-linked	1585:1592	arg1	GalNAc					1594:1599	O-linked GalNAc	1585:1599	O-linked GalNAc	1585:1599	Bovine liver alpha-N-acetylgalactosaminidase cleaves O-linked GalNAc.
1457416	1	14	theme	exoglycosidases	606:620	arg1	specificity					571:581	the distinct specificity	558:581	the distinct specificity of the highly purified exoglycosidases	558:620	The structure of the glycans of the A-chain of human plasma alpha 2HS-glycoprotein was established from the chemical compositions of its derivatives prepared by sequential enzymatic degradation of the carbohydrate moiety, from the determination of the kind and amount of the monosaccharides liberated after each step of the enzymatic digestion, and from the distinct specificity of the highly purified exoglycosidases.
1457416	0	15	theme	A-chain	41:47	arg1	O-glycans					24:32	O-glycans	24:32	O-glycans	24:32	Structure of the N- and O-glycans of the A-chain of human plasma alpha 2HS-glycoprotein as deduced from the chemical compositions of the derivatives prepared by stepwise degradation with exoglycosidases.
1457416	0	15	theme	A-chain	41:47	arg1	N-					17:18	N-	17:18	N-	17:18	Structure of the N- and O-glycans of the A-chain of human plasma alpha 2HS-glycoprotein as deduced from the chemical compositions of the derivatives prepared by stepwise degradation with exoglycosidases.
1457416	3	16	with	sialidases	911:920	arg1	specificities					946:958	different cleavage specificities	927:958	different cleavage specificities	927:958	Utilizing sialidases with different cleavage specificities, the number of alpha 2-3- and alpha 2-6-linked sialic acid residues could be separately determined.
1457416	3	17	theme	different	927:935	arg1	specificities					946:958	different cleavage specificities	927:958	different cleavage specificities	927:958	Utilizing sialidases with different cleavage specificities, the number of alpha 2-3- and alpha 2-6-linked sialic acid residues could be separately determined.
1457416	5	18	theme	beta	1326:1329	arg1	GlcNAc					1359:1364	beta 1-2, beta 1-4, and beta 1-6 GlcNAc	1326:1364	beta 1-2, beta 1-4, and beta 1-6 GlcNAc with higher activity for the beta 1-2	1326:1402	Jack bean beta-N-acetylglucosaminidase cleaves beta 1-2, beta 1-4, and beta 1-6 GlcNAc with higher activity for the beta 1-2.
1457416	0	19	theme	human	52:56	arg1	alpha					65:69	human plasma alpha	52:69	human plasma alpha	52:69	Structure of the N- and O-glycans of the A-chain of human plasma alpha 2HS-glycoprotein as deduced from the chemical compositions of the derivatives prepared by stepwise degradation with exoglycosidases.
1457416	0	20	theme	alpha	65:69	arg1	A-chain					41:47	the A-chain	37:47	the A-chain of human plasma alpha	37:69	Structure of the N- and O-glycans of the A-chain of human plasma alpha 2HS-glycoprotein as deduced from the chemical compositions of the derivatives prepared by stepwise degradation with exoglycosidases.
1457416	0	21	with	degradation	170:180	arg1	exoglycosidases					187:201	exoglycosidases	187:201	exoglycosidases	187:201	Structure of the N- and O-glycans of the A-chain of human plasma alpha 2HS-glycoprotein as deduced from the chemical compositions of the derivatives prepared by stepwise degradation with exoglycosidases.
1457416	1	22	theme	sequential	365:374	arg1	degradation					386:396	sequential enzymatic degradation	365:396	sequential enzymatic degradation of the carbohydrate moiety	365:423	The structure of the glycans of the A-chain of human plasma alpha 2HS-glycoprotein was established from the chemical compositions of its derivatives prepared by sequential enzymatic degradation of the carbohydrate moiety, from the determination of the kind and amount of the monosaccharides liberated after each step of the enzymatic digestion, and from the distinct specificity of the highly purified exoglycosidases.
1457416	4	23	attach	isolated	1102:1109	arg2	enzyme					1095:1100	the enzyme	1091:1100	the enzyme isolated from S. pneumoniae	1091:1128	As to the beta-galactosidases, the enzyme isolated from S. pneumoniae cleaves only beta 1-4-linked galactose residues, whereas the bovine testes enzyme acts on both the beta 1-4- and beta 1-3-linked galactose residues.
1457416	4	23	attach	isolated	1102:1109	arg1	pneumoniae					1119:1128	S. pneumoniae	1116:1128	S. pneumoniae	1116:1128	As to the beta-galactosidases, the enzyme isolated from S. pneumoniae cleaves only beta 1-4-linked galactose residues, whereas the bovine testes enzyme acts on both the beta 1-4- and beta 1-3-linked galactose residues.
1457416	2	24	theme	fowl	683:686	arg1	virus					695:699	fowl plague virus	683:699	fowl plague virus	683:699	The exoglycosidases were three sialidases (Vibrio cholerae, fowl plague virus, and Arthrobacter ureafaciens), two beta-galactosidases (Streptococcus pneumoniae and bovine testis), one alpha-N-acetylgalactosaminidase, one beta-N-acetylglucosaminidase, and one alpha-mannosidase.
1457416	6	25	theme	alpha	1467:1471	arg1	Man					1477:1479	alpha 1-2, alpha 1-6, and alpha 1-3 Man	1441:1479	alpha 1-2, alpha 1-6, and alpha 1-3 Man with greater activity for alpha 1-2 and alpha 1-6	1441:1529	Jack bean alpha-mannosidase cleaves alpha 1-2, alpha 1-6, and alpha 1-3 Man with greater activity for alpha 1-2 and alpha 1-6.
1457416	1	26	theme	plasma	257:262	arg1	2HS-glycoprotein					270:285	human plasma alpha 2HS-glycoprotein	251:285	human plasma alpha 2HS-glycoprotein	251:285	The structure of the glycans of the A-chain of human plasma alpha 2HS-glycoprotein was established from the chemical compositions of its derivatives prepared by sequential enzymatic degradation of the carbohydrate moiety, from the determination of the kind and amount of the monosaccharides liberated after each step of the enzymatic digestion, and from the distinct specificity of the highly purified exoglycosidases.
1457416	4	27	dep	cleaves	1130:1136	arg1	whereas					1179:1185	whereas	1179:1185	whereas	1179:1185	As to the beta-galactosidases, the enzyme isolated from S. pneumoniae cleaves only beta 1-4-linked galactose residues, whereas the bovine testes enzyme acts on both the beta 1-4- and beta 1-3-linked galactose residues.
1457416	0	28	gly	2HS-glycoprotein	71:86	arg1	2HS-glycoprotein					71:86	2HS-glycoprotein	71:86	2HS-glycoprotein as deduced from the chemical compositions of the derivatives prepared by stepwise degradation with exoglycosidases	71:201	Structure of the N- and O-glycans of the A-chain of human plasma alpha 2HS-glycoprotein as deduced from the chemical compositions of the derivatives prepared by stepwise degradation with exoglycosidases.
1457416	4	29	theme	galactose	1259:1267	arg1	residues					1269:1276	1-3-linked galactose residues	1248:1276	1-3-linked galactose residues	1248:1276	As to the beta-galactosidases, the enzyme isolated from S. pneumoniae cleaves only beta 1-4-linked galactose residues, whereas the bovine testes enzyme acts on both the beta 1-4- and beta 1-3-linked galactose residues.
1457416	1	30	theme	distinct	562:569	arg1	specificity					571:581	the distinct specificity	558:581	the distinct specificity of the highly purified exoglycosidases	558:620	The structure of the glycans of the A-chain of human plasma alpha 2HS-glycoprotein was established from the chemical compositions of its derivatives prepared by sequential enzymatic degradation of the carbohydrate moiety, from the determination of the kind and amount of the monosaccharides liberated after each step of the enzymatic digestion, and from the distinct specificity of the highly purified exoglycosidases.
1457416	1	31	theme	2HS-glycoprotein	270:285	arg1	A-chain					240:246	the A-chain	236:246	the A-chain of human plasma alpha 2HS-glycoprotein	236:285	The structure of the glycans of the A-chain of human plasma alpha 2HS-glycoprotein was established from the chemical compositions of its derivatives prepared by sequential enzymatic degradation of the carbohydrate moiety, from the determination of the kind and amount of the monosaccharides liberated after each step of the enzymatic digestion, and from the distinct specificity of the highly purified exoglycosidases.
1457416	6	32	theme	alpha	1452:1456	arg1	Man					1477:1479	alpha 1-2, alpha 1-6, and alpha 1-3 Man	1441:1479	alpha 1-2, alpha 1-6, and alpha 1-3 Man with greater activity for alpha 1-2 and alpha 1-6	1441:1529	Jack bean alpha-mannosidase cleaves alpha 1-2, alpha 1-6, and alpha 1-3 Man with greater activity for alpha 1-2 and alpha 1-6.
1457416	8	33	link	O-linked	1727:1734	arg1	trisaccharides					1736:1749	two O-linked trisaccharides	1723:1749	two O-linked trisaccharides	1723:1749	On the basis of these results, the A-chain of alpha 2 HS-glycoprotein was found to possess two biantennary N-glycans and two O-linked trisaccharides.
1457416	7	34	theme	liver	1539:1543	arg1	alpha-N-acetylgalactosaminidase					1545:1575	Bovine liver alpha-N-acetylgalactosaminidase	1532:1575	Bovine liver alpha-N-acetylgalactosaminidase	1532:1575	Bovine liver alpha-N-acetylgalactosaminidase cleaves O-linked GalNAc.
1457416	3	35	theme	sialic	1007:1012	arg1	residues					1019:1026	alpha 2-3- and alpha 2-6-linked sialic acid residues	975:1026	alpha 2-3- and alpha 2-6-linked sialic acid residues	975:1026	Utilizing sialidases with different cleavage specificities, the number of alpha 2-3- and alpha 2-6-linked sialic acid residues could be separately determined.
1457416	3	36	link	2-6-linked	996:1005	arg1	residues					1019:1026	alpha 2-3- and alpha 2-6-linked sialic acid residues	975:1026	alpha 2-3- and alpha 2-6-linked sialic acid residues	975:1026	Utilizing sialidases with different cleavage specificities, the number of alpha 2-3- and alpha 2-6-linked sialic acid residues could be separately determined.
1457416	3	37	theme	alpha	990:994	arg1	residues					1019:1026	alpha 2-3- and alpha 2-6-linked sialic acid residues	975:1026	alpha 2-3- and alpha 2-6-linked sialic acid residues	975:1026	Utilizing sialidases with different cleavage specificities, the number of alpha 2-3- and alpha 2-6-linked sialic acid residues could be separately determined.
1457416	4	38	theme	beta	1143:1146	arg1	residues					1169:1176	only beta 1-4-linked galactose residues	1138:1176	only beta 1-4-linked galactose residues	1138:1176	As to the beta-galactosidases, the enzyme isolated from S. pneumoniae cleaves only beta 1-4-linked galactose residues, whereas the bovine testes enzyme acts on both the beta 1-4- and beta 1-3-linked galactose residues.
1457416	2	39	dep	sialidases	654:663	arg1	virus					695:699	fowl plague virus	683:699	fowl plague virus	683:699	The exoglycosidases were three sialidases (Vibrio cholerae, fowl plague virus, and Arthrobacter ureafaciens), two beta-galactosidases (Streptococcus pneumoniae and bovine testis), one alpha-N-acetylgalactosaminidase, one beta-N-acetylglucosaminidase, and one alpha-mannosidase.
1457416	2	39	dep	sialidases	654:663	arg1	cholerae					673:680	Vibrio cholerae	666:680	Vibrio cholerae	666:680	The exoglycosidases were three sialidases (Vibrio cholerae, fowl plague virus, and Arthrobacter ureafaciens), two beta-galactosidases (Streptococcus pneumoniae and bovine testis), one alpha-N-acetylgalactosaminidase, one beta-N-acetylglucosaminidase, and one alpha-mannosidase.
1457416	2	39	dep	sialidases	654:663	arg1	ureafaciens					719:729	Arthrobacter ureafaciens	706:729	Arthrobacter ureafaciens	706:729	The exoglycosidases were three sialidases (Vibrio cholerae, fowl plague virus, and Arthrobacter ureafaciens), two beta-galactosidases (Streptococcus pneumoniae and bovine testis), one alpha-N-acetylgalactosaminidase, one beta-N-acetylglucosaminidase, and one alpha-mannosidase.
1457416	5	40	theme	bean	1284:1287	arg1	beta-N-acetylglucosaminidase					1289:1316	Jack bean beta-N-acetylglucosaminidase	1279:1316	Jack bean beta-N-acetylglucosaminidase	1279:1316	Jack bean beta-N-acetylglucosaminidase cleaves beta 1-2, beta 1-4, and beta 1-6 GlcNAc with higher activity for the beta 1-2.
1457416	3	41	theme	residues	1019:1026	arg1	number					965:970	the number	961:970	the number of alpha 2-3- and alpha 2-6-linked sialic acid residues	961:1026	Utilizing sialidases with different cleavage specificities, the number of alpha 2-3- and alpha 2-6-linked sialic acid residues could be separately determined.
1457416	0	42	theme	stepwise	161:168	arg1	degradation					170:180	stepwise degradation	161:180	stepwise degradation with exoglycosidases	161:201	Structure of the N- and O-glycans of the A-chain of human plasma alpha 2HS-glycoprotein as deduced from the chemical compositions of the derivatives prepared by stepwise degradation with exoglycosidases.
1457416	1	43	theme	enzymatic	528:536	arg1	digestion					538:546	the enzymatic digestion	524:546	the enzymatic digestion	524:546	The structure of the glycans of the A-chain of human plasma alpha 2HS-glycoprotein was established from the chemical compositions of its derivatives prepared by sequential enzymatic degradation of the carbohydrate moiety, from the determination of the kind and amount of the monosaccharides liberated after each step of the enzymatic digestion, and from the distinct specificity of the highly purified exoglycosidases.
1457416	6	44	theme	greater	1486:1492	arg1	activity					1494:1501	greater activity	1486:1501	greater activity for alpha 1-2 and alpha 1-6	1486:1529	Jack bean alpha-mannosidase cleaves alpha 1-2, alpha 1-6, and alpha 1-3 Man with greater activity for alpha 1-2 and alpha 1-6.
1457416	8	45	theme	alpha	1648:1652	arg1	HS-glycoprotein					1656:1670	alpha 2 HS-glycoprotein	1648:1670	alpha 2 HS-glycoprotein	1648:1670	On the basis of these results, the A-chain of alpha 2 HS-glycoprotein was found to possess two biantennary N-glycans and two O-linked trisaccharides.
1457416	8	46	theme	HS-glycoprotein	1656:1670	arg1	A-chain					1637:1643	the A-chain	1633:1643	the A-chain of alpha 2 HS-glycoprotein	1633:1670	On the basis of these results, the A-chain of alpha 2 HS-glycoprotein was found to possess two biantennary N-glycans and two O-linked trisaccharides.
1457416	1	47	theme	kind	456:459	arg1	determination					435:447	the determination	431:447	the determination of the kind and amount of the monosaccharides liberated after each step of the enzymatic digestion	431:546	The structure of the glycans of the A-chain of human plasma alpha 2HS-glycoprotein was established from the chemical compositions of its derivatives prepared by sequential enzymatic degradation of the carbohydrate moiety, from the determination of the kind and amount of the monosaccharides liberated after each step of the enzymatic digestion, and from the distinct specificity of the highly purified exoglycosidases.
1457416	8	48	theme	O-linked	1727:1734	arg1	trisaccharides					1736:1749	two O-linked trisaccharides	1723:1749	two O-linked trisaccharides	1723:1749	On the basis of these results, the A-chain of alpha 2 HS-glycoprotein was found to possess two biantennary N-glycans and two O-linked trisaccharides.
1457416	4	49	theme	testes	1198:1203	arg1	enzyme					1205:1210	the bovine testes enzyme	1187:1210	the bovine testes enzyme	1187:1210	As to the beta-galactosidases, the enzyme isolated from S. pneumoniae cleaves only beta 1-4-linked galactose residues, whereas the bovine testes enzyme acts on both the beta 1-4- and beta 1-3-linked galactose residues.
1457416	6	50	theme	bean	1410:1413	arg1	alpha-mannosidase					1415:1431	Jack bean alpha-mannosidase	1405:1431	Jack bean alpha-mannosidase	1405:1431	Jack bean alpha-mannosidase cleaves alpha 1-2, alpha 1-6, and alpha 1-3 Man with greater activity for alpha 1-2 and alpha 1-6.
1457416	1	51	theme	amount	465:470	arg1	determination					435:447	the determination	431:447	the determination of the kind and amount of the monosaccharides liberated after each step of the enzymatic digestion	431:546	The structure of the glycans of the A-chain of human plasma alpha 2HS-glycoprotein was established from the chemical compositions of its derivatives prepared by sequential enzymatic degradation of the carbohydrate moiety, from the determination of the kind and amount of the monosaccharides liberated after each step of the enzymatic digestion, and from the distinct specificity of the highly purified exoglycosidases.
1457416	4	52	theme	galactose	1159:1167	arg1	residues					1169:1176	only beta 1-4-linked galactose residues	1138:1176	only beta 1-4-linked galactose residues	1138:1176	As to the beta-galactosidases, the enzyme isolated from S. pneumoniae cleaves only beta 1-4-linked galactose residues, whereas the bovine testes enzyme acts on both the beta 1-4- and beta 1-3-linked galactose residues.
1457416	4	53	dep	1-4-	1234:1237	arg1	residues					1269:1276	1-3-linked galactose residues	1248:1276	1-3-linked galactose residues	1248:1276	As to the beta-galactosidases, the enzyme isolated from S. pneumoniae cleaves only beta 1-4-linked galactose residues, whereas the bovine testes enzyme acts on both the beta 1-4- and beta 1-3-linked galactose residues.
1457416	2	54	theme	bovine	787:792	arg1	beta-galactosidases					737:755	two beta-galactosidases	733:755	two beta-galactosidases (Streptococcus pneumoniae and bovine testis)	733:800	The exoglycosidases were three sialidases (Vibrio cholerae, fowl plague virus, and Arthrobacter ureafaciens), two beta-galactosidases (Streptococcus pneumoniae and bovine testis), one alpha-N-acetylgalactosaminidase, one beta-N-acetylglucosaminidase, and one alpha-mannosidase.
1457416	2	54	theme	bovine	787:792	arg1	testis					794:799	bovine testis	787:799	bovine testis	787:799	The exoglycosidases were three sialidases (Vibrio cholerae, fowl plague virus, and Arthrobacter ureafaciens), two beta-galactosidases (Streptococcus pneumoniae and bovine testis), one alpha-N-acetylgalactosaminidase, one beta-N-acetylglucosaminidase, and one alpha-mannosidase.
1457416	4	55	theme	beta	1229:1232	arg1	1-4-					1234:1237	the beta 1-4-	1225:1237	the beta 1-4-	1225:1237	As to the beta-galactosidases, the enzyme isolated from S. pneumoniae cleaves only beta 1-4-linked galactose residues, whereas the bovine testes enzyme acts on both the beta 1-4- and beta 1-3-linked galactose residues.
1457416	1	56	theme	carbohydrate	405:416	arg1	moiety					418:423	the carbohydrate moiety	401:423	the carbohydrate moiety	401:423	The structure of the glycans of the A-chain of human plasma alpha 2HS-glycoprotein was established from the chemical compositions of its derivatives prepared by sequential enzymatic degradation of the carbohydrate moiety, from the determination of the kind and amount of the monosaccharides liberated after each step of the enzymatic digestion, and from the distinct specificity of the highly purified exoglycosidases.
1457416	7	57	theme	Bovine	1532:1537	arg1	alpha-N-acetylgalactosaminidase					1545:1575	Bovine liver alpha-N-acetylgalactosaminidase	1532:1575	Bovine liver alpha-N-acetylgalactosaminidase	1532:1575	Bovine liver alpha-N-acetylgalactosaminidase cleaves O-linked GalNAc.
1457416	5	58	theme	beta	1336:1339	arg1	GlcNAc					1359:1364	beta 1-2, beta 1-4, and beta 1-6 GlcNAc	1326:1364	beta 1-2, beta 1-4, and beta 1-6 GlcNAc with higher activity for the beta 1-2	1326:1402	Jack bean beta-N-acetylglucosaminidase cleaves beta 1-2, beta 1-4, and beta 1-6 GlcNAc with higher activity for the beta 1-2.
1457416	1	59	gly	2HS-glycoprotein	270:285	arg1	2HS-glycoprotein					270:285	human plasma alpha 2HS-glycoprotein	251:285	human plasma alpha 2HS-glycoprotein	251:285	The structure of the glycans of the A-chain of human plasma alpha 2HS-glycoprotein was established from the chemical compositions of its derivatives prepared by sequential enzymatic degradation of the carbohydrate moiety, from the determination of the kind and amount of the monosaccharides liberated after each step of the enzymatic digestion, and from the distinct specificity of the highly purified exoglycosidases.
1457416	1	60	dep	kind	456:459	arg1	the					452:454	the	452:454	the	452:454	The structure of the glycans of the A-chain of human plasma alpha 2HS-glycoprotein was established from the chemical compositions of its derivatives prepared by sequential enzymatic degradation of the carbohydrate moiety, from the determination of the kind and amount of the monosaccharides liberated after each step of the enzymatic digestion, and from the distinct specificity of the highly purified exoglycosidases.
1457416	1	61	theme	purified	597:604	arg1	exoglycosidases					606:620	the highly purified exoglycosidases	586:620	the highly purified exoglycosidases	586:620	The structure of the glycans of the A-chain of human plasma alpha 2HS-glycoprotein was established from the chemical compositions of its derivatives prepared by sequential enzymatic degradation of the carbohydrate moiety, from the determination of the kind and amount of the monosaccharides liberated after each step of the enzymatic digestion, and from the distinct specificity of the highly purified exoglycosidases.
1457416	6	62	theme	alpha	1441:1445	arg1	Man					1477:1479	alpha 1-2, alpha 1-6, and alpha 1-3 Man	1441:1479	alpha 1-2, alpha 1-6, and alpha 1-3 Man with greater activity for alpha 1-2 and alpha 1-6	1441:1529	Jack bean alpha-mannosidase cleaves alpha 1-2, alpha 1-6, and alpha 1-3 Man with greater activity for alpha 1-2 and alpha 1-6.
1457416	0	63	theme	plasma	58:63	arg1	alpha					65:69	human plasma alpha	52:69	human plasma alpha	52:69	Structure of the N- and O-glycans of the A-chain of human plasma alpha 2HS-glycoprotein as deduced from the chemical compositions of the derivatives prepared by stepwise degradation with exoglycosidases.
1457416	3	64	theme	cleavage	937:944	arg1	specificities					946:958	different cleavage specificities	927:958	different cleavage specificities	927:958	Utilizing sialidases with different cleavage specificities, the number of alpha 2-3- and alpha 2-6-linked sialic acid residues could be separately determined.
1457416	4	65	link	1-3-linked	1248:1257	arg1	residues					1269:1276	1-3-linked galactose residues	1248:1276	1-3-linked galactose residues	1248:1276	As to the beta-galactosidases, the enzyme isolated from S. pneumoniae cleaves only beta 1-4-linked galactose residues, whereas the bovine testes enzyme acts on both the beta 1-4- and beta 1-3-linked galactose residues.
1457416	8	66	dep	results	1624:1630	arg1	the					1605:1607	the	1605:1607	the	1605:1607	On the basis of these results, the A-chain of alpha 2 HS-glycoprotein was found to possess two biantennary N-glycans and two O-linked trisaccharides.
1457416	8	66	dep	results	1624:1630	arg1	basis					1609:1613	basis	1609:1613	basis	1609:1613	On the basis of these results, the A-chain of alpha 2 HS-glycoprotein was found to possess two biantennary N-glycans and two O-linked trisaccharides.
1457416	6	67	theme	Jack	1405:1408	arg1	alpha-mannosidase					1415:1431	Jack bean alpha-mannosidase	1405:1431	Jack bean alpha-mannosidase	1405:1431	Jack bean alpha-mannosidase cleaves alpha 1-2, alpha 1-6, and alpha 1-3 Man with greater activity for alpha 1-2 and alpha 1-6.
1457416	1	68	theme	derivatives	341:351	arg1	compositions					321:332	the chemical compositions	308:332	the chemical compositions of its derivatives prepared by sequential enzymatic degradation of the carbohydrate moiety	308:423	The structure of the glycans of the A-chain of human plasma alpha 2HS-glycoprotein was established from the chemical compositions of its derivatives prepared by sequential enzymatic degradation of the carbohydrate moiety, from the determination of the kind and amount of the monosaccharides liberated after each step of the enzymatic digestion, and from the distinct specificity of the highly purified exoglycosidases.
1457416	1	69	theme	digestion	538:546	arg1	step					516:519	each step	511:519	each step of the enzymatic digestion	511:546	The structure of the glycans of the A-chain of human plasma alpha 2HS-glycoprotein was established from the chemical compositions of its derivatives prepared by sequential enzymatic degradation of the carbohydrate moiety, from the determination of the kind and amount of the monosaccharides liberated after each step of the enzymatic digestion, and from the distinct specificity of the highly purified exoglycosidases.
1457416	5	70	theme	higher	1371:1376	arg1	activity					1378:1385	higher activity	1371:1385	higher activity	1371:1385	Jack bean beta-N-acetylglucosaminidase cleaves beta 1-2, beta 1-4, and beta 1-6 GlcNAc with higher activity for the beta 1-2.
1457416	2	71	theme	plague	688:693	arg1	virus					695:699	fowl plague virus	683:699	fowl plague virus	683:699	The exoglycosidases were three sialidases (Vibrio cholerae, fowl plague virus, and Arthrobacter ureafaciens), two beta-galactosidases (Streptococcus pneumoniae and bovine testis), one alpha-N-acetylgalactosaminidase, one beta-N-acetylglucosaminidase, and one alpha-mannosidase.
1457416	1	72	theme	enzymatic	376:384	arg1	degradation					386:396	sequential enzymatic degradation	365:396	sequential enzymatic degradation of the carbohydrate moiety	365:423	The structure of the glycans of the A-chain of human plasma alpha 2HS-glycoprotein was established from the chemical compositions of its derivatives prepared by sequential enzymatic degradation of the carbohydrate moiety, from the determination of the kind and amount of the monosaccharides liberated after each step of the enzymatic digestion, and from the distinct specificity of the highly purified exoglycosidases.
1457416	5	73	theme	beta	1350:1353	arg1	GlcNAc					1359:1364	beta 1-2, beta 1-4, and beta 1-6 GlcNAc	1326:1364	beta 1-2, beta 1-4, and beta 1-6 GlcNAc with higher activity for the beta 1-2	1326:1402	Jack bean beta-N-acetylglucosaminidase cleaves beta 1-2, beta 1-4, and beta 1-6 GlcNAc with higher activity for the beta 1-2.
1457416	0	74	theme	N-	17:18	arg1	Structure					0:8	Structure	0:8	Structure of the N- and O-glycans of the A-chain of human plasma alpha	0:69	Structure of the N- and O-glycans of the A-chain of human plasma alpha 2HS-glycoprotein as deduced from the chemical compositions of the derivatives prepared by stepwise degradation with exoglycosidases.
1457416	1	75	theme	alpha	264:268	arg1	2HS-glycoprotein					270:285	human plasma alpha 2HS-glycoprotein	251:285	human plasma alpha 2HS-glycoprotein	251:285	The structure of the glycans of the A-chain of human plasma alpha 2HS-glycoprotein was established from the chemical compositions of its derivatives prepared by sequential enzymatic degradation of the carbohydrate moiety, from the determination of the kind and amount of the monosaccharides liberated after each step of the enzymatic digestion, and from the distinct specificity of the highly purified exoglycosidases.
1457416	0	76	theme	O-glycans	24:32	arg1	Structure					0:8	Structure	0:8	Structure of the N- and O-glycans of the A-chain of human plasma alpha	0:69	Structure of the N- and O-glycans of the A-chain of human plasma alpha 2HS-glycoprotein as deduced from the chemical compositions of the derivatives prepared by stepwise degradation with exoglycosidases.
1457416	7	77	theme	O-linked	1585:1592	arg1	GalNAc					1594:1599	O-linked GalNAc	1585:1599	O-linked GalNAc	1585:1599	Bovine liver alpha-N-acetylgalactosaminidase cleaves O-linked GalNAc.
1457416	3	78	theme	alpha	975:979	arg1	residues					1019:1026	alpha 2-3- and alpha 2-6-linked sialic acid residues	975:1026	alpha 2-3- and alpha 2-6-linked sialic acid residues	975:1026	Utilizing sialidases with different cleavage specificities, the number of alpha 2-3- and alpha 2-6-linked sialic acid residues could be separately determined.
1457416	1	79	theme	glycans	225:231	arg1	structure					208:216	The structure	204:216	The structure of the glycans of the A-chain of human plasma alpha 2HS-glycoprotein	204:285	The structure of the glycans of the A-chain of human plasma alpha 2HS-glycoprotein was established from the chemical compositions of its derivatives prepared by sequential enzymatic degradation of the carbohydrate moiety, from the determination of the kind and amount of the monosaccharides liberated after each step of the enzymatic digestion, and from the distinct specificity of the highly purified exoglycosidases.
1457416	1	80	theme	monosaccharides	479:493	arg1	amount					465:470	amount	465:470	amount	465:470	The structure of the glycans of the A-chain of human plasma alpha 2HS-glycoprotein was established from the chemical compositions of its derivatives prepared by sequential enzymatic degradation of the carbohydrate moiety, from the determination of the kind and amount of the monosaccharides liberated after each step of the enzymatic digestion, and from the distinct specificity of the highly purified exoglycosidases.
1457416	1	80	theme	monosaccharides	479:493	arg1	monosaccharides					479:493	the monosaccharides	475:493	the monosaccharides liberated after each step of the enzymatic digestion	475:546	The structure of the glycans of the A-chain of human plasma alpha 2HS-glycoprotein was established from the chemical compositions of its derivatives prepared by sequential enzymatic degradation of the carbohydrate moiety, from the determination of the kind and amount of the monosaccharides liberated after each step of the enzymatic digestion, and from the distinct specificity of the highly purified exoglycosidases.
1457416	1	80	theme	monosaccharides	479:493	arg1	kind					456:459	kind	456:459	kind	456:459	The structure of the glycans of the A-chain of human plasma alpha 2HS-glycoprotein was established from the chemical compositions of its derivatives prepared by sequential enzymatic degradation of the carbohydrate moiety, from the determination of the kind and amount of the monosaccharides liberated after each step of the enzymatic digestion, and from the distinct specificity of the highly purified exoglycosidases.
1457416	3	81	theme	acid	1014:1017	arg1	residues					1019:1026	alpha 2-3- and alpha 2-6-linked sialic acid residues	975:1026	alpha 2-3- and alpha 2-6-linked sialic acid residues	975:1026	Utilizing sialidases with different cleavage specificities, the number of alpha 2-3- and alpha 2-6-linked sialic acid residues could be separately determined.
1457416	1	82	theme	chemical	312:319	arg1	compositions					321:332	the chemical compositions	308:332	the chemical compositions of its derivatives prepared by sequential enzymatic degradation of the carbohydrate moiety	308:423	The structure of the glycans of the A-chain of human plasma alpha 2HS-glycoprotein was established from the chemical compositions of its derivatives prepared by sequential enzymatic degradation of the carbohydrate moiety, from the determination of the kind and amount of the monosaccharides liberated after each step of the enzymatic digestion, and from the distinct specificity of the highly purified exoglycosidases.
1457416	4	83	theme	1-3-linked	1248:1257	arg1	residues					1269:1276	1-3-linked galactose residues	1248:1276	1-3-linked galactose residues	1248:1276	As to the beta-galactosidases, the enzyme isolated from S. pneumoniae cleaves only beta 1-4-linked galactose residues, whereas the bovine testes enzyme acts on both the beta 1-4- and beta 1-3-linked galactose residues.
1457416	3	84	theme	2-6-linked	996:1005	arg1	residues					1019:1026	alpha 2-3- and alpha 2-6-linked sialic acid residues	975:1026	alpha 2-3- and alpha 2-6-linked sialic acid residues	975:1026	Utilizing sialidases with different cleavage specificities, the number of alpha 2-3- and alpha 2-6-linked sialic acid residues could be separately determined.
1457416	8	85	gly	HS-glycoprotein	1656:1670	arg1	HS-glycoprotein					1656:1670	alpha 2 HS-glycoprotein	1648:1670	alpha 2 HS-glycoprotein	1648:1670	On the basis of these results, the A-chain of alpha 2 HS-glycoprotein was found to possess two biantennary N-glycans and two O-linked trisaccharides.
1457416	2	86	dep	beta-galactosidases	737:755	arg1	beta-galactosidases					737:755	two beta-galactosidases	733:755	two beta-galactosidases (Streptococcus pneumoniae and bovine testis)	733:800	The exoglycosidases were three sialidases (Vibrio cholerae, fowl plague virus, and Arthrobacter ureafaciens), two beta-galactosidases (Streptococcus pneumoniae and bovine testis), one alpha-N-acetylgalactosaminidase, one beta-N-acetylglucosaminidase, and one alpha-mannosidase.
1457416	2	86	dep	beta-galactosidases	737:755	arg1	pneumoniae					772:781	Streptococcus pneumoniae	758:781	Streptococcus pneumoniae	758:781	The exoglycosidases were three sialidases (Vibrio cholerae, fowl plague virus, and Arthrobacter ureafaciens), two beta-galactosidases (Streptococcus pneumoniae and bovine testis), one alpha-N-acetylgalactosaminidase, one beta-N-acetylglucosaminidase, and one alpha-mannosidase.
1457416	2	86	dep	beta-galactosidases	737:755	arg1	testis					794:799	bovine testis	787:799	bovine testis	787:799	The exoglycosidases were three sialidases (Vibrio cholerae, fowl plague virus, and Arthrobacter ureafaciens), two beta-galactosidases (Streptococcus pneumoniae and bovine testis), one alpha-N-acetylgalactosaminidase, one beta-N-acetylglucosaminidase, and one alpha-mannosidase.
1457416	4	87	theme	only	1138:1141	arg1	residues					1169:1176	only beta 1-4-linked galactose residues	1138:1176	only beta 1-4-linked galactose residues	1138:1176	As to the beta-galactosidases, the enzyme isolated from S. pneumoniae cleaves only beta 1-4-linked galactose residues, whereas the bovine testes enzyme acts on both the beta 1-4- and beta 1-3-linked galactose residues.
3935432	8	0	theme	following	1187:1195	arg1	structures					1216:1225	the following major carbohydrate structures	1183:1225	the following major carbohydrate structures	1183:1225	Applying methylation analysis, exoglycosidase digestion and fast atom bombardment mass spectrometry the following major carbohydrate structures were identified: N1, NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol; and N2, NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol.
3935432	7	1	theme	reductive	976:984	arg1	beta-elimination					986:1001	reductive beta-elimination	976:1001	reductive beta-elimination	976:1001	The oligosaccharides were released by reductive beta-elimination and were purified by gel filtration and high-performance liquid chromatography.
3935432	6	2	theme	IL-2	883:886	arg1	protein					888:894	the IL-2 protein	879:894	the IL-2 protein	879:894	Carbohydrates are O-linked to the IL-2 protein via threonine-3 of the polypeptide chain.
3935432	4	3	theme	interleukin-2	587:599	arg1	M					601:601	interleukin-2 M	587:601	interleukin-2 M	587:601	A third component (interleukin-2 M, 14.5 kDa) represents a nonglycosylated form.
3935432	4	3	theme	interleukin-2	587:599	arg1	kDa					609:611	14.5 kDa	604:611	14.5 kDa	604:611	A third component (interleukin-2 M, 14.5 kDa) represents a nonglycosylated form.
3935432	3	4	theme	major	359:363	arg1	N2					407:408	N2	407:408	N2	407:408	Two major polypeptide species (interleukin-2 N1 and N2, 16.5 kDa) were shown to be glycosylated on the basis of [3H]galactose/[3H]glucosamine incorporation and determination of amino sugars after acid hydrolysis.
3935432	3	4	theme	major	359:363	arg1	species					377:383	Two major polypeptide species	355:383	Two major polypeptide species (interleukin-2 N1 and N2, 16.5 kDa)	355:419	Two major polypeptide species (interleukin-2 N1 and N2, 16.5 kDa) were shown to be glycosylated on the basis of [3H]galactose/[3H]glucosamine incorporation and determination of amino sugars after acid hydrolysis.
3935432	3	4	theme	major	359:363	arg1	N1					400:401	N1	400:401	N1	400:401	Two major polypeptide species (interleukin-2 N1 and N2, 16.5 kDa) were shown to be glycosylated on the basis of [3H]galactose/[3H]glucosamine incorporation and determination of amino sugars after acid hydrolysis.
3935432	5	5	theme	amino	653:657	arg1	consistent					724:733	consistent	724:733	consistent	724:733	The amino acid composition and the NH2-terminal sequence of both forms are consistent with the data deduced from the cDNA coding for interleukin-2 after removal of a leader peptide of 20 amino acids.
3935432	5	5	theme	amino	653:657	arg1	composition					664:674	The amino acid composition	649:674	The amino acid composition	649:674	The amino acid composition and the NH2-terminal sequence of both forms are consistent with the data deduced from the cDNA coding for interleukin-2 after removal of a leader peptide of 20 amino acids.
3935432	8	6	theme	carbohydrate	1203:1214	arg1	structures					1216:1225	the following major carbohydrate structures	1183:1225	the following major carbohydrate structures	1183:1225	Applying methylation analysis, exoglycosidase digestion and fast atom bombardment mass spectrometry the following major carbohydrate structures were identified: N1, NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol; and N2, NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol.
3935432	2	7	theme	high-performance	253:268	arg1	chromatography					277:290	reversed-phase high-performance liquid chromatography	238:290	reversed-phase high-performance liquid chromatography	238:290	These forms were (partially) resolved by reversed-phase high-performance liquid chromatography and sodium dodecyl sulfate/polyacrylamide gel electrophoresis.
3935432	5	8	theme	acid	659:662	arg1	consistent					724:733	consistent	724:733	consistent	724:733	The amino acid composition and the NH2-terminal sequence of both forms are consistent with the data deduced from the cDNA coding for interleukin-2 after removal of a leader peptide of 20 amino acids.
3935432	5	8	theme	acid	659:662	arg1	composition					664:674	The amino acid composition	649:674	The amino acid composition	649:674	The amino acid composition and the NH2-terminal sequence of both forms are consistent with the data deduced from the cDNA coding for interleukin-2 after removal of a leader peptide of 20 amino acids.
3935432	3	9	theme	acid	551:554	arg1	hydrolysis					556:565	acid hydrolysis	551:565	acid hydrolysis	551:565	Two major polypeptide species (interleukin-2 N1 and N2, 16.5 kDa) were shown to be glycosylated on the basis of [3H]galactose/[3H]glucosamine incorporation and determination of amino sugars after acid hydrolysis.
3935432	2	10	theme	sulfate/polyacrylamide	311:332	arg1	electrophoresis					338:352	sodium dodecyl sulfate/polyacrylamide gel electrophoresis	296:352	sodium dodecyl sulfate/polyacrylamide gel electrophoresis	296:352	These forms were (partially) resolved by reversed-phase high-performance liquid chromatography and sodium dodecyl sulfate/polyacrylamide gel electrophoresis.
3935432	8	11	theme	fast	1143:1146	arg1	spectrometry					1170:1181	fast atom bombardment mass spectrometry	1143:1181	fast atom bombardment mass spectrometry	1143:1181	Applying methylation analysis, exoglycosidase digestion and fast atom bombardment mass spectrometry the following major carbohydrate structures were identified: N1, NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol; and N2, NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol.
3935432	8	12	theme	major	1197:1201	arg1	structures					1216:1225	the following major carbohydrate structures	1183:1225	the following major carbohydrate structures	1183:1225	Applying methylation analysis, exoglycosidase digestion and fast atom bombardment mass spectrometry the following major carbohydrate structures were identified: N1, NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol; and N2, NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol.
3935432	4	13	dep	component	576:584	arg1	M					601:601	interleukin-2 M	587:601	interleukin-2 M	587:601	A third component (interleukin-2 M, 14.5 kDa) represents a nonglycosylated form.
3935432	4	13	dep	component	576:584	arg1	kDa					609:611	14.5 kDa	604:611	14.5 kDa	604:611	A third component (interleukin-2 M, 14.5 kDa) represents a nonglycosylated form.
3935432	7	14	theme	gel	1024:1026	arg1	filtration					1028:1037	gel filtration	1024:1037	gel filtration	1024:1037	The oligosaccharides were released by reductive beta-elimination and were purified by gel filtration and high-performance liquid chromatography.
3935432	1	15	from	donors	153:158	arg1	lymphocytes					128:138	peripheral blood lymphocytes	111:138	peripheral blood lymphocytes from healthy donors	111:158	Purified human interleukin-2 secreted by peripheral blood lymphocytes from healthy donors was found to exist in several forms.
3935432	2	16	theme	sodium	296:301	arg1	electrophoresis					338:352	sodium dodecyl sulfate/polyacrylamide gel electrophoresis	296:352	sodium dodecyl sulfate/polyacrylamide gel electrophoresis	296:352	These forms were (partially) resolved by reversed-phase high-performance liquid chromatography and sodium dodecyl sulfate/polyacrylamide gel electrophoresis.
3935432	3	17	theme	glucosamine	485:495	arg1	incorporation					497:509	[3H]galactose/[3H]glucosamine incorporation	467:509	[3H]galactose/[3H]glucosamine incorporation	467:509	Two major polypeptide species (interleukin-2 N1 and N2, 16.5 kDa) were shown to be glycosylated on the basis of [3H]galactose/[3H]glucosamine incorporation and determination of amino sugars after acid hydrolysis.
3935432	1	18	theme	Purified	70:77	arg1	interleukin-2					85:97	Purified human interleukin-2	70:97	Purified human interleukin-2 secreted by peripheral blood lymphocytes from healthy donors	70:158	Purified human interleukin-2 secreted by peripheral blood lymphocytes from healthy donors was found to exist in several forms.
3935432	6	19	attach	O-linked	867:874	arg2	Carbohydrates					849:861	Carbohydrates	849:861	Carbohydrates	849:861	Carbohydrates are O-linked to the IL-2 protein via threonine-3 of the polypeptide chain.
3935432	6	19	attach	O-linked	867:874	arg3	threonine-3					900:910	threonine-3	900:910	threonine-3 of the polypeptide chain	900:935	Carbohydrates are O-linked to the IL-2 protein via threonine-3 of the polypeptide chain.
3935432	6	19	attach	O-linked	867:874	arg1	protein					888:894	the IL-2 protein	879:894	the IL-2 protein	879:894	Carbohydrates are O-linked to the IL-2 protein via threonine-3 of the polypeptide chain.
3935432	5	20	theme	acids	842:846	arg1	peptide					822:828	a leader peptide	813:828	a leader peptide of 20 amino acids	813:846	The amino acid composition and the NH2-terminal sequence of both forms are consistent with the data deduced from the cDNA coding for interleukin-2 after removal of a leader peptide of 20 amino acids.
3935432	8	21	theme	alpha	1254:1258	arg1	N1					1244:1245	N1	1244:1245	N1	1244:1245	Applying methylation analysis, exoglycosidase digestion and fast atom bombardment mass spectrometry the following major carbohydrate structures were identified: N1, NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol; and N2, NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol.
3935432	8	21	theme	alpha	1254:1258	arg1	GalNAc-ol					1277:1285	NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol	1248:1285	NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol	1248:1285	Applying methylation analysis, exoglycosidase digestion and fast atom bombardment mass spectrometry the following major carbohydrate structures were identified: N1, NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol; and N2, NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol.
3935432	4	22	gly	nonglycosylated	627:641	arg1	form					643:646	a nonglycosylated form	625:646	a nonglycosylated form	625:646	A third component (interleukin-2 M, 14.5 kDa) represents a nonglycosylated form.
3935432	1	23	theme	human	79:83	arg1	interleukin-2					85:97	Purified human interleukin-2	70:97	Purified human interleukin-2 secreted by peripheral blood lymphocytes from healthy donors	70:158	Purified human interleukin-2 secreted by peripheral blood lymphocytes from healthy donors was found to exist in several forms.
3935432	8	24	theme	methylation	1092:1102	arg1	analysis					1104:1111	methylation analysis	1092:1111	methylation analysis	1092:1111	Applying methylation analysis, exoglycosidase digestion and fast atom bombardment mass spectrometry the following major carbohydrate structures were identified: N1, NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol; and N2, NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol.
3935432	8	25	theme	[NeuAc	1325:1330	arg1	GalNAc-ol					1343:1351	NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol	1296:1351	NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol	1296:1351	Applying methylation analysis, exoglycosidase digestion and fast atom bombardment mass spectrometry the following major carbohydrate structures were identified: N1, NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol; and N2, NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol.
3935432	8	25	theme	[NeuAc	1325:1330	arg1	N2					1292:1293	N2	1292:1293	N2	1292:1293	Applying methylation analysis, exoglycosidase digestion and fast atom bombardment mass spectrometry the following major carbohydrate structures were identified: N1, NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol; and N2, NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol.
3935432	8	25	theme	[NeuAc	1325:1330	arg1	alpha					1332:1336	alpha 2-6)	1332:1341	alpha 2-6)	1332:1341	Applying methylation analysis, exoglycosidase digestion and fast atom bombardment mass spectrometry the following major carbohydrate structures were identified: N1, NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol; and N2, NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol.
3935432	1	26	theme	several	182:188	arg1	forms					190:194	several forms	182:194	several forms	182:194	Purified human interleukin-2 secreted by peripheral blood lymphocytes from healthy donors was found to exist in several forms.
3935432	8	27	theme	exoglycosidase	1114:1127	arg1	digestion					1129:1137	exoglycosidase digestion	1114:1137	exoglycosidase digestion	1114:1137	Applying methylation analysis, exoglycosidase digestion and fast atom bombardment mass spectrometry the following major carbohydrate structures were identified: N1, NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol; and N2, NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol.
3935432	8	28	theme	Gal	1264:1266	arg1	N1					1244:1245	N1	1244:1245	N1	1244:1245	Applying methylation analysis, exoglycosidase digestion and fast atom bombardment mass spectrometry the following major carbohydrate structures were identified: N1, NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol; and N2, NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol.
3935432	8	28	theme	Gal	1264:1266	arg1	GalNAc-ol					1277:1285	NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol	1248:1285	NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol	1248:1285	Applying methylation analysis, exoglycosidase digestion and fast atom bombardment mass spectrometry the following major carbohydrate structures were identified: N1, NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol; and N2, NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol.
3935432	0	29	theme	major	18:22	arg1	carbohydrates					24:36	the major carbohydrates	14:36	the major carbohydrates of natural human interleukin-2	14:67	Structures of the major carbohydrates of natural human interleukin-2.
3935432	3	30	gly	glycosylated	438:449	arg1	determination					515:527	determination	515:527	determination of amino sugars after acid hydrolysis	515:565	Two major polypeptide species (interleukin-2 N1 and N2, 16.5 kDa) were shown to be glycosylated on the basis of [3H]galactose/[3H]glucosamine incorporation and determination of amino sugars after acid hydrolysis.
3935432	3	30	gly	glycosylated	438:449	arg2	N1					400:401	N1	400:401	N1	400:401	Two major polypeptide species (interleukin-2 N1 and N2, 16.5 kDa) were shown to be glycosylated on the basis of [3H]galactose/[3H]glucosamine incorporation and determination of amino sugars after acid hydrolysis.
3935432	3	30	gly	glycosylated	438:449	arg2	basis					458:462	the basis	454:462	the basis of [3H]galactose/[3H]glucosamine incorporation	454:509	Two major polypeptide species (interleukin-2 N1 and N2, 16.5 kDa) were shown to be glycosylated on the basis of [3H]galactose/[3H]glucosamine incorporation and determination of amino sugars after acid hydrolysis.
3935432	3	30	gly	glycosylated	438:449	arg1	N1					400:401	N1	400:401	N1	400:401	Two major polypeptide species (interleukin-2 N1 and N2, 16.5 kDa) were shown to be glycosylated on the basis of [3H]galactose/[3H]glucosamine incorporation and determination of amino sugars after acid hydrolysis.
3935432	3	30	gly	glycosylated	438:449	arg2	determination					515:527	determination	515:527	determination of amino sugars after acid hydrolysis	515:565	Two major polypeptide species (interleukin-2 N1 and N2, 16.5 kDa) were shown to be glycosylated on the basis of [3H]galactose/[3H]glucosamine incorporation and determination of amino sugars after acid hydrolysis.
3935432	3	30	gly	glycosylated	438:449	arg2	species					377:383	Two major polypeptide species	355:383	Two major polypeptide species (interleukin-2 N1 and N2, 16.5 kDa)	355:419	Two major polypeptide species (interleukin-2 N1 and N2, 16.5 kDa) were shown to be glycosylated on the basis of [3H]galactose/[3H]glucosamine incorporation and determination of amino sugars after acid hydrolysis.
3935432	3	30	gly	glycosylated	438:449	arg2	N2					407:408	N2	407:408	N2	407:408	Two major polypeptide species (interleukin-2 N1 and N2, 16.5 kDa) were shown to be glycosylated on the basis of [3H]galactose/[3H]glucosamine incorporation and determination of amino sugars after acid hydrolysis.
3935432	3	30	gly	glycosylated	438:449	arg1	basis					458:462	the basis	454:462	the basis of [3H]galactose/[3H]glucosamine incorporation	454:509	Two major polypeptide species (interleukin-2 N1 and N2, 16.5 kDa) were shown to be glycosylated on the basis of [3H]galactose/[3H]glucosamine incorporation and determination of amino sugars after acid hydrolysis.
3935432	3	30	gly	glycosylated	438:449	arg1	N2					407:408	N2	407:408	N2	407:408	Two major polypeptide species (interleukin-2 N1 and N2, 16.5 kDa) were shown to be glycosylated on the basis of [3H]galactose/[3H]glucosamine incorporation and determination of amino sugars after acid hydrolysis.
3935432	3	30	gly	glycosylated	438:449	arg1	species					377:383	Two major polypeptide species	355:383	Two major polypeptide species (interleukin-2 N1 and N2, 16.5 kDa)	355:419	Two major polypeptide species (interleukin-2 N1 and N2, 16.5 kDa) were shown to be glycosylated on the basis of [3H]galactose/[3H]glucosamine incorporation and determination of amino sugars after acid hydrolysis.
3935432	2	31	theme	gel	334:336	arg1	electrophoresis					338:352	sodium dodecyl sulfate/polyacrylamide gel electrophoresis	296:352	sodium dodecyl sulfate/polyacrylamide gel electrophoresis	296:352	These forms were (partially) resolved by reversed-phase high-performance liquid chromatography and sodium dodecyl sulfate/polyacrylamide gel electrophoresis.
3935432	4	32	theme	nonglycosylated	627:641	arg1	form					643:646	a nonglycosylated form	625:646	a nonglycosylated form	625:646	A third component (interleukin-2 M, 14.5 kDa) represents a nonglycosylated form.
3935432	5	33	theme	leader	815:820	arg1	peptide					822:828	a leader peptide	813:828	a leader peptide of 20 amino acids	813:846	The amino acid composition and the NH2-terminal sequence of both forms are consistent with the data deduced from the cDNA coding for interleukin-2 after removal of a leader peptide of 20 amino acids.
3935432	3	34	theme	sugars	538:543	arg1	determination					515:527	determination	515:527	determination of amino sugars after acid hydrolysis	515:565	Two major polypeptide species (interleukin-2 N1 and N2, 16.5 kDa) were shown to be glycosylated on the basis of [3H]galactose/[3H]glucosamine incorporation and determination of amino sugars after acid hydrolysis.
3935432	3	34	theme	sugars	538:543	arg1	basis					458:462	the basis	454:462	the basis of [3H]galactose/[3H]glucosamine incorporation	454:509	Two major polypeptide species (interleukin-2 N1 and N2, 16.5 kDa) were shown to be glycosylated on the basis of [3H]galactose/[3H]glucosamine incorporation and determination of amino sugars after acid hydrolysis.
3935432	1	35	theme	peripheral	111:120	arg1	lymphocytes					128:138	peripheral blood lymphocytes	111:138	peripheral blood lymphocytes from healthy donors	111:158	Purified human interleukin-2 secreted by peripheral blood lymphocytes from healthy donors was found to exist in several forms.
3935432	4	36	theme	third	570:574	arg1	component					576:584	A third component	568:584	A third component (interleukin-2 M, 14.5 kDa)	568:612	A third component (interleukin-2 M, 14.5 kDa) represents a nonglycosylated form.
3935432	5	37	theme	forms	714:718	arg1	consistent					724:733	consistent	724:733	consistent	724:733	The amino acid composition and the NH2-terminal sequence of both forms are consistent with the data deduced from the cDNA coding for interleukin-2 after removal of a leader peptide of 20 amino acids.
3935432	5	37	theme	forms	714:718	arg1	sequence					697:704	the NH2-terminal sequence	680:704	the NH2-terminal sequence of both forms	680:718	The amino acid composition and the NH2-terminal sequence of both forms are consistent with the data deduced from the cDNA coding for interleukin-2 after removal of a leader peptide of 20 amino acids.
3935432	5	37	theme	forms	714:718	arg1	composition					664:674	The amino acid composition	649:674	The amino acid composition	649:674	The amino acid composition and the NH2-terminal sequence of both forms are consistent with the data deduced from the cDNA coding for interleukin-2 after removal of a leader peptide of 20 amino acids.
3935432	2	38	dep	resolved	226:233	arg1	partially					215:223	partially	215:223	partially	215:223	These forms were (partially) resolved by reversed-phase high-performance liquid chromatography and sodium dodecyl sulfate/polyacrylamide gel electrophoresis.
3935432	0	39	theme	carbohydrates	24:36	arg1	Structures					0:9	Structures	0:9	Structures of the major carbohydrates of natural human interleukin-2	0:67	Structures of the major carbohydrates of natural human interleukin-2.
3935432	8	40	theme	NeuAc	1248:1252	arg1	N1					1244:1245	N1	1244:1245	N1	1244:1245	Applying methylation analysis, exoglycosidase digestion and fast atom bombardment mass spectrometry the following major carbohydrate structures were identified: N1, NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol; and N2, NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol.
3935432	8	40	theme	NeuAc	1248:1252	arg1	GalNAc-ol					1277:1285	NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol	1248:1285	NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol	1248:1285	Applying methylation analysis, exoglycosidase digestion and fast atom bombardment mass spectrometry the following major carbohydrate structures were identified: N1, NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol; and N2, NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol.
3935432	5	41	theme	amino	836:840	arg1	acids					842:846	20 amino acids	833:846	20 amino acids	833:846	The amino acid composition and the NH2-terminal sequence of both forms are consistent with the data deduced from the cDNA coding for interleukin-2 after removal of a leader peptide of 20 amino acids.
3935432	0	42	theme	human	49:53	arg1	interleukin-2					55:67	natural human interleukin-2	41:67	natural human interleukin-2	41:67	Structures of the major carbohydrates of natural human interleukin-2.
3935432	6	43	theme	chain	931:935	arg1	threonine-3					900:910	threonine-3	900:910	threonine-3 of the polypeptide chain	900:935	Carbohydrates are O-linked to the IL-2 protein via threonine-3 of the polypeptide chain.
3935432	7	44	theme	high-performance	1043:1058	arg1	chromatography					1067:1080	high-performance liquid chromatography	1043:1080	high-performance liquid chromatography	1043:1080	The oligosaccharides were released by reductive beta-elimination and were purified by gel filtration and high-performance liquid chromatography.
3935432	8	45	theme	mass	1165:1168	arg1	spectrometry					1170:1181	fast atom bombardment mass spectrometry	1143:1181	fast atom bombardment mass spectrometry	1143:1181	Applying methylation analysis, exoglycosidase digestion and fast atom bombardment mass spectrometry the following major carbohydrate structures were identified: N1, NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol; and N2, NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol.
3935432	5	46	with	consistent	724:733	arg1	data					744:747	the data	740:747	the data deduced from the cDNA coding for interleukin-2 after removal of a leader peptide of 20 amino acids	740:846	The amino acid composition and the NH2-terminal sequence of both forms are consistent with the data deduced from the cDNA coding for interleukin-2 after removal of a leader peptide of 20 amino acids.
3935432	5	47	theme	NH2-terminal	684:695	arg1	consistent					724:733	consistent	724:733	consistent	724:733	The amino acid composition and the NH2-terminal sequence of both forms are consistent with the data deduced from the cDNA coding for interleukin-2 after removal of a leader peptide of 20 amino acids.
3935432	5	47	theme	NH2-terminal	684:695	arg1	sequence					697:704	the NH2-terminal sequence	680:704	the NH2-terminal sequence of both forms	680:718	The amino acid composition and the NH2-terminal sequence of both forms are consistent with the data deduced from the cDNA coding for interleukin-2 after removal of a leader peptide of 20 amino acids.
3935432	1	48	theme	blood	122:126	arg1	lymphocytes					128:138	peripheral blood lymphocytes	111:138	peripheral blood lymphocytes from healthy donors	111:158	Purified human interleukin-2 secreted by peripheral blood lymphocytes from healthy donors was found to exist in several forms.
3935432	0	49	theme	natural	41:47	arg1	interleukin-2					55:67	natural human interleukin-2	41:67	natural human interleukin-2	41:67	Structures of the major carbohydrates of natural human interleukin-2.
3935432	6	50	theme	polypeptide	919:929	arg1	chain					931:935	the polypeptide chain	915:935	the polypeptide chain	915:935	Carbohydrates are O-linked to the IL-2 protein via threonine-3 of the polypeptide chain.
3935432	7	51	theme	liquid	1060:1065	arg1	chromatography					1067:1080	high-performance liquid chromatography	1043:1080	high-performance liquid chromatography	1043:1080	The oligosaccharides were released by reductive beta-elimination and were purified by gel filtration and high-performance liquid chromatography.
3935432	3	52	theme	incorporation	497:509	arg1	determination					515:527	determination	515:527	determination of amino sugars after acid hydrolysis	515:565	Two major polypeptide species (interleukin-2 N1 and N2, 16.5 kDa) were shown to be glycosylated on the basis of [3H]galactose/[3H]glucosamine incorporation and determination of amino sugars after acid hydrolysis.
3935432	3	52	theme	incorporation	497:509	arg1	basis					458:462	the basis	454:462	the basis of [3H]galactose/[3H]glucosamine incorporation	454:509	Two major polypeptide species (interleukin-2 N1 and N2, 16.5 kDa) were shown to be glycosylated on the basis of [3H]galactose/[3H]glucosamine incorporation and determination of amino sugars after acid hydrolysis.
3935432	3	53	dep	N1	400:401	arg1	kDa					416:418	16.5 kDa	411:418	16.5 kDa	411:418	Two major polypeptide species (interleukin-2 N1 and N2, 16.5 kDa) were shown to be glycosylated on the basis of [3H]galactose/[3H]glucosamine incorporation and determination of amino sugars after acid hydrolysis.
3935432	2	54	theme	liquid	270:275	arg1	chromatography					277:290	reversed-phase high-performance liquid chromatography	238:290	reversed-phase high-performance liquid chromatography	238:290	These forms were (partially) resolved by reversed-phase high-performance liquid chromatography and sodium dodecyl sulfate/polyacrylamide gel electrophoresis.
3935432	8	55	theme	beta	1268:1271	arg1	N1					1244:1245	N1	1244:1245	N1	1244:1245	Applying methylation analysis, exoglycosidase digestion and fast atom bombardment mass spectrometry the following major carbohydrate structures were identified: N1, NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol; and N2, NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol.
3935432	8	55	theme	beta	1268:1271	arg1	GalNAc-ol					1277:1285	NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol	1248:1285	NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol	1248:1285	Applying methylation analysis, exoglycosidase digestion and fast atom bombardment mass spectrometry the following major carbohydrate structures were identified: N1, NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol; and N2, NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol.
3935432	3	56	theme	galactose/[3H	471:483	arg1	incorporation					497:509	[3H]galactose/[3H]glucosamine incorporation	467:509	[3H]galactose/[3H]glucosamine incorporation	467:509	Two major polypeptide species (interleukin-2 N1 and N2, 16.5 kDa) were shown to be glycosylated on the basis of [3H]galactose/[3H]glucosamine incorporation and determination of amino sugars after acid hydrolysis.
3935432	8	57	theme	beta	1316:1319	arg1	GalNAc-ol					1343:1351	NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol	1296:1351	NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol	1296:1351	Applying methylation analysis, exoglycosidase digestion and fast atom bombardment mass spectrometry the following major carbohydrate structures were identified: N1, NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol; and N2, NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol.
3935432	8	57	theme	beta	1316:1319	arg1	N2					1292:1293	N2	1292:1293	N2	1292:1293	Applying methylation analysis, exoglycosidase digestion and fast atom bombardment mass spectrometry the following major carbohydrate structures were identified: N1, NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol; and N2, NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol.
3935432	8	57	theme	beta	1316:1319	arg1	alpha					1332:1336	alpha 2-6)	1332:1341	alpha 2-6)	1332:1341	Applying methylation analysis, exoglycosidase digestion and fast atom bombardment mass spectrometry the following major carbohydrate structures were identified: N1, NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol; and N2, NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol.
3935432	2	58	theme	dodecyl	303:309	arg1	electrophoresis					338:352	sodium dodecyl sulfate/polyacrylamide gel electrophoresis	296:352	sodium dodecyl sulfate/polyacrylamide gel electrophoresis	296:352	These forms were (partially) resolved by reversed-phase high-performance liquid chromatography and sodium dodecyl sulfate/polyacrylamide gel electrophoresis.
3935432	8	59	theme	bombardment	1153:1163	arg1	spectrometry					1170:1181	fast atom bombardment mass spectrometry	1143:1181	fast atom bombardment mass spectrometry	1143:1181	Applying methylation analysis, exoglycosidase digestion and fast atom bombardment mass spectrometry the following major carbohydrate structures were identified: N1, NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol; and N2, NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol.
3935432	1	60	theme	healthy	145:151	arg1	donors					153:158	healthy donors	145:158	healthy donors	145:158	Purified human interleukin-2 secreted by peripheral blood lymphocytes from healthy donors was found to exist in several forms.
3935432	8	61	theme	Gal	1312:1314	arg1	GalNAc-ol					1343:1351	NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol	1296:1351	NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol	1296:1351	Applying methylation analysis, exoglycosidase digestion and fast atom bombardment mass spectrometry the following major carbohydrate structures were identified: N1, NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol; and N2, NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol.
3935432	8	61	theme	Gal	1312:1314	arg1	N2					1292:1293	N2	1292:1293	N2	1292:1293	Applying methylation analysis, exoglycosidase digestion and fast atom bombardment mass spectrometry the following major carbohydrate structures were identified: N1, NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol; and N2, NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol.
3935432	8	61	theme	Gal	1312:1314	arg1	alpha					1332:1336	alpha 2-6)	1332:1341	alpha 2-6)	1332:1341	Applying methylation analysis, exoglycosidase digestion and fast atom bombardment mass spectrometry the following major carbohydrate structures were identified: N1, NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol; and N2, NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol.
3935432	8	62	theme	NeuAc	1296:1300	arg1	GalNAc-ol					1343:1351	NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol	1296:1351	NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol	1296:1351	Applying methylation analysis, exoglycosidase digestion and fast atom bombardment mass spectrometry the following major carbohydrate structures were identified: N1, NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol; and N2, NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol.
3935432	8	62	theme	NeuAc	1296:1300	arg1	N2					1292:1293	N2	1292:1293	N2	1292:1293	Applying methylation analysis, exoglycosidase digestion and fast atom bombardment mass spectrometry the following major carbohydrate structures were identified: N1, NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol; and N2, NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol.
3935432	8	62	theme	NeuAc	1296:1300	arg1	alpha					1332:1336	alpha 2-6)	1332:1341	alpha 2-6)	1332:1341	Applying methylation analysis, exoglycosidase digestion and fast atom bombardment mass spectrometry the following major carbohydrate structures were identified: N1, NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol; and N2, NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol.
3935432	3	63	theme	polypeptide	365:375	arg1	N2					407:408	N2	407:408	N2	407:408	Two major polypeptide species (interleukin-2 N1 and N2, 16.5 kDa) were shown to be glycosylated on the basis of [3H]galactose/[3H]glucosamine incorporation and determination of amino sugars after acid hydrolysis.
3935432	3	63	theme	polypeptide	365:375	arg1	species					377:383	Two major polypeptide species	355:383	Two major polypeptide species (interleukin-2 N1 and N2, 16.5 kDa)	355:419	Two major polypeptide species (interleukin-2 N1 and N2, 16.5 kDa) were shown to be glycosylated on the basis of [3H]galactose/[3H]glucosamine incorporation and determination of amino sugars after acid hydrolysis.
3935432	3	63	theme	polypeptide	365:375	arg1	N1					400:401	N1	400:401	N1	400:401	Two major polypeptide species (interleukin-2 N1 and N2, 16.5 kDa) were shown to be glycosylated on the basis of [3H]galactose/[3H]glucosamine incorporation and determination of amino sugars after acid hydrolysis.
3935432	2	64	theme	reversed-phase	238:251	arg1	chromatography					277:290	reversed-phase high-performance liquid chromatography	238:290	reversed-phase high-performance liquid chromatography	238:290	These forms were (partially) resolved by reversed-phase high-performance liquid chromatography and sodium dodecyl sulfate/polyacrylamide gel electrophoresis.
3935432	5	65	theme	peptide	822:828	arg1	removal					802:808	removal	802:808	removal of a leader peptide of 20 amino acids	802:846	The amino acid composition and the NH2-terminal sequence of both forms are consistent with the data deduced from the cDNA coding for interleukin-2 after removal of a leader peptide of 20 amino acids.
3935432	8	66	theme	alpha	1302:1306	arg1	GalNAc-ol					1343:1351	NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol	1296:1351	NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol	1296:1351	Applying methylation analysis, exoglycosidase digestion and fast atom bombardment mass spectrometry the following major carbohydrate structures were identified: N1, NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol; and N2, NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol.
3935432	8	66	theme	alpha	1302:1306	arg1	N2					1292:1293	N2	1292:1293	N2	1292:1293	Applying methylation analysis, exoglycosidase digestion and fast atom bombardment mass spectrometry the following major carbohydrate structures were identified: N1, NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol; and N2, NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol.
3935432	8	66	theme	alpha	1302:1306	arg1	alpha					1332:1336	alpha 2-6)	1332:1341	alpha 2-6)	1332:1341	Applying methylation analysis, exoglycosidase digestion and fast atom bombardment mass spectrometry the following major carbohydrate structures were identified: N1, NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol; and N2, NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol.
3935432	0	67	theme	interleukin-2	55:67	arg1	carbohydrates					24:36	the major carbohydrates	14:36	the major carbohydrates of natural human interleukin-2	14:67	Structures of the major carbohydrates of natural human interleukin-2.
3935432	3	68	theme	amino	532:536	arg1	sugars					538:543	amino sugars	532:543	amino sugars	532:543	Two major polypeptide species (interleukin-2 N1 and N2, 16.5 kDa) were shown to be glycosylated on the basis of [3H]galactose/[3H]glucosamine incorporation and determination of amino sugars after acid hydrolysis.
3935432	8	69	theme	atom	1148:1151	arg1	spectrometry					1170:1181	fast atom bombardment mass spectrometry	1143:1181	fast atom bombardment mass spectrometry	1143:1181	Applying methylation analysis, exoglycosidase digestion and fast atom bombardment mass spectrometry the following major carbohydrate structures were identified: N1, NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol; and N2, NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol.
3935432	8	70	dep	identified	1232:1241	arg1	N1					1244:1245	N1	1244:1245	N1	1244:1245	Applying methylation analysis, exoglycosidase digestion and fast atom bombardment mass spectrometry the following major carbohydrate structures were identified: N1, NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol; and N2, NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol.
3935432	8	70	dep	identified	1232:1241	arg1	GalNAc-ol					1277:1285	NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol	1248:1285	NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol	1248:1285	Applying methylation analysis, exoglycosidase digestion and fast atom bombardment mass spectrometry the following major carbohydrate structures were identified: N1, NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol; and N2, NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol.
3935432	8	70	dep	identified	1232:1241	arg1	GalNAc-ol					1343:1351	NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol	1296:1351	NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol	1296:1351	Applying methylation analysis, exoglycosidase digestion and fast atom bombardment mass spectrometry the following major carbohydrate structures were identified: N1, NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol; and N2, NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol.
3935432	8	70	dep	identified	1232:1241	arg1	Applying					1083:1090	Applying	1083:1090	Applying methylation analysis, exoglycosidase digestion and fast atom bombardment mass spectrometry	1083:1181	Applying methylation analysis, exoglycosidase digestion and fast atom bombardment mass spectrometry the following major carbohydrate structures were identified: N1, NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol; and N2, NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol.
3935432	8	70	dep	identified	1232:1241	arg1	N2					1292:1293	N2	1292:1293	N2	1292:1293	Applying methylation analysis, exoglycosidase digestion and fast atom bombardment mass spectrometry the following major carbohydrate structures were identified: N1, NeuAc(alpha 2-3)Gal(beta 1-3)GalNAc-ol; and N2, NeuAc(alpha 2-3)Gal(beta 1-3)[NeuAc(alpha 2-6)]GalNAc-ol.
10024660	5	0	theme	glycan	864:869	arg1	entities					1033:1040	complex/dibranched, fucosylated/complex/dibranched, monosialylated/complex/dibranched, and monosialylated/fucosylated/dibranched entities	904:1040	complex/dibranched, fucosylated/complex/dibranched, monosialylated/complex/dibranched, and monosialylated/fucosylated/dibranched entities	904:1040	The N- glycan structures were elucidated to be complex/dibranched, fucosylated/complex/dibranched, monosialylated/complex/dibranched, and monosialylated/fucosylated/dibranched entities.
10024660	5	0	theme	glycan	864:869	arg1	structures					871:880	The N- glycan structures	857:880	The N- glycan structures	857:880	The N- glycan structures were elucidated to be complex/dibranched, fucosylated/complex/dibranched, monosialylated/complex/dibranched, and monosialylated/fucosylated/dibranched entities.
10024660	4	1	theme	molecular	663:671	arg1	profile					678:684	The molecular mass profile	659:684	The molecular mass profile of esterified N- glycans present in BSSL	659:725	The molecular mass profile of esterified N- glycans present in BSSL further permitted the more detailed studies through collision-induced dissociation (CID) and sequential exoglycosidase cleavages.
10024660	0	2	from	characterization	11:26	arg1	lipase					85:90	bile salt-stimulated lipase	64:90	bile salt-stimulated lipase	64:90	Structural characterization of the N-linked oligosaccharides in bile salt-stimulated lipase originated from human breast milk.
10024660	3	3	theme	esterified	583:592	arg1	glycans					597:603	the esterified N- glycans	579:603	the esterified N- glycans	579:603	Ion-exchange chromatography with pulsed amperometric detection, together with mass-spectral analysis of the esterified N- glycans, indicated the presence of monosialylated structures.
10024660	0	4	theme	breast	114:119	arg1	milk					121:124	human breast milk	108:124	human breast milk	108:124	Structural characterization of the N-linked oligosaccharides in bile salt-stimulated lipase originated from human breast milk.
10024660	3	5	theme	N-	594:595	arg1	glycans					597:603	the esterified N- glycans	579:603	the esterified N- glycans	579:603	Ion-exchange chromatography with pulsed amperometric detection, together with mass-spectral analysis of the esterified N- glycans, indicated the presence of monosialylated structures.
10024660	1	6	theme	exoglycosidase	262:275	arg1	digestion					277:285	exoglycosidase digestion	262:285	exoglycosidase digestion	262:285	The detailed structures of N- glycans derived from bile salt-stimulated lipase (BSSL) found in human milk were determined by combining exoglycosidase digestion with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry.
10024660	0	7	theme	human	108:112	arg1	milk					121:124	human breast milk	108:124	human breast milk	108:124	Structural characterization of the N-linked oligosaccharides in bile salt-stimulated lipase originated from human breast milk.
10024660	4	8	theme	present	711:717	arg1	glycans					703:709	esterified N- glycans	689:709	esterified N- glycans present in BSSL	689:725	The molecular mass profile of esterified N- glycans present in BSSL further permitted the more detailed studies through collision-induced dissociation (CID) and sequential exoglycosidase cleavages.
10024660	3	9	theme	mass-spectral	553:565	arg1	analysis					567:574	mass-spectral analysis	553:574	mass-spectral analysis of the esterified N- glycans	553:603	Ion-exchange chromatography with pulsed amperometric detection, together with mass-spectral analysis of the esterified N- glycans, indicated the presence of monosialylated structures.
10024660	4	10	theme	collision-induced	779:795	arg1	CID					811:813	CID	811:813	CID	811:813	The molecular mass profile of esterified N- glycans present in BSSL further permitted the more detailed studies through collision-induced dissociation (CID) and sequential exoglycosidase cleavages.
10024660	4	10	theme	collision-induced	779:795	arg1	dissociation					797:808	collision-induced dissociation	779:808	collision-induced dissociation (CID)	779:814	The molecular mass profile of esterified N- glycans present in BSSL further permitted the more detailed studies through collision-induced dissociation (CID) and sequential exoglycosidase cleavages.
10024660	4	11	theme	exoglycosidase	831:844	arg1	cleavages					846:854	sequential exoglycosidase cleavages	820:854	sequential exoglycosidase cleavages	820:854	The molecular mass profile of esterified N- glycans present in BSSL further permitted the more detailed studies through collision-induced dissociation (CID) and sequential exoglycosidase cleavages.
10024660	4	12	theme	detailed	754:761	arg1	studies					763:769	the more detailed studies	745:769	the more detailed studies	745:769	The molecular mass profile of esterified N- glycans present in BSSL further permitted the more detailed studies through collision-induced dissociation (CID) and sequential exoglycosidase cleavages.
10024660	1	13	theme	bile	178:181	arg1	lipase					199:204	bile salt-stimulated lipase	178:204	bile salt-stimulated lipase (BSSL) found in human milk	178:231	The detailed structures of N- glycans derived from bile salt-stimulated lipase (BSSL) found in human milk were determined by combining exoglycosidase digestion with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry.
10024660	1	13	theme	bile	178:181	arg1	BSSL					207:210	BSSL	207:210	BSSL	207:210	The detailed structures of N- glycans derived from bile salt-stimulated lipase (BSSL) found in human milk were determined by combining exoglycosidase digestion with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry.
10024660	4	14	theme	mass	673:676	arg1	profile					678:684	The molecular mass profile	659:684	The molecular mass profile of esterified N- glycans present in BSSL	659:725	The molecular mass profile of esterified N- glycans present in BSSL further permitted the more detailed studies through collision-induced dissociation (CID) and sequential exoglycosidase cleavages.
10024660	1	15	theme	salt-stimulated	183:197	arg1	lipase					199:204	bile salt-stimulated lipase	178:204	bile salt-stimulated lipase (BSSL) found in human milk	178:231	The detailed structures of N- glycans derived from bile salt-stimulated lipase (BSSL) found in human milk were determined by combining exoglycosidase digestion with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry.
10024660	1	15	theme	salt-stimulated	183:197	arg1	BSSL					207:210	BSSL	207:210	BSSL	207:210	The detailed structures of N- glycans derived from bile salt-stimulated lipase (BSSL) found in human milk were determined by combining exoglycosidase digestion with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry.
10024660	5	16	theme	complex/dibranched	904:921	arg1	entities					1033:1040	complex/dibranched, fucosylated/complex/dibranched, monosialylated/complex/dibranched, and monosialylated/fucosylated/dibranched entities	904:1040	complex/dibranched, fucosylated/complex/dibranched, monosialylated/complex/dibranched, and monosialylated/fucosylated/dibranched entities	904:1040	The N- glycan structures were elucidated to be complex/dibranched, fucosylated/complex/dibranched, monosialylated/complex/dibranched, and monosialylated/fucosylated/dibranched entities.
10024660	5	16	theme	complex/dibranched	904:921	arg1	structures					871:880	The N- glycan structures	857:880	The N- glycan structures	857:880	The N- glycan structures were elucidated to be complex/dibranched, fucosylated/complex/dibranched, monosialylated/complex/dibranched, and monosialylated/fucosylated/dibranched entities.
10024660	1	17	attach	derived	165:171	arg1	lipase					199:204	bile salt-stimulated lipase	178:204	bile salt-stimulated lipase (BSSL) found in human milk	178:231	The detailed structures of N- glycans derived from bile salt-stimulated lipase (BSSL) found in human milk were determined by combining exoglycosidase digestion with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry.
10024660	1	17	attach	derived	165:171	arg2	glycans					157:163	N- glycans	154:163	N- glycans derived from bile salt-stimulated lipase (BSSL) found in human milk	154:231	The detailed structures of N- glycans derived from bile salt-stimulated lipase (BSSL) found in human milk were determined by combining exoglycosidase digestion with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry.
10024660	1	17	attach	derived	165:171	arg1	BSSL					207:210	BSSL	207:210	BSSL	207:210	The detailed structures of N- glycans derived from bile salt-stimulated lipase (BSSL) found in human milk were determined by combining exoglycosidase digestion with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry.
10024660	3	18	theme	structures	647:656	arg1	presence					620:627	the presence	616:627	the presence of monosialylated structures	616:656	Ion-exchange chromatography with pulsed amperometric detection, together with mass-spectral analysis of the esterified N- glycans, indicated the presence of monosialylated structures.
10024660	3	19	theme	Ion-exchange	475:486	arg1	chromatography					488:501	Ion-exchange chromatography	475:501	Ion-exchange chromatography with pulsed amperometric detection, together with mass-spectral analysis of the esterified N- glycans,	475:604	Ion-exchange chromatography with pulsed amperometric detection, together with mass-spectral analysis of the esterified N- glycans, indicated the presence of monosialylated structures.
10024660	0	20	theme	Structural	0:9	arg1	characterization					11:26	Structural characterization	0:26	Structural characterization of the N-linked oligosaccharides in bile salt-stimulated lipase	0:90	Structural characterization of the N-linked oligosaccharides in bile salt-stimulated lipase originated from human breast milk.
10024660	4	21	theme	sequential	820:829	arg1	cleavages					846:854	sequential exoglycosidase cleavages	820:854	sequential exoglycosidase cleavages	820:854	The molecular mass profile of esterified N- glycans present in BSSL further permitted the more detailed studies through collision-induced dissociation (CID) and sequential exoglycosidase cleavages.
10024660	5	22	theme	fucosylated/complex/dibranched	924:953	arg1	entities					1033:1040	complex/dibranched, fucosylated/complex/dibranched, monosialylated/complex/dibranched, and monosialylated/fucosylated/dibranched entities	904:1040	complex/dibranched, fucosylated/complex/dibranched, monosialylated/complex/dibranched, and monosialylated/fucosylated/dibranched entities	904:1040	The N- glycan structures were elucidated to be complex/dibranched, fucosylated/complex/dibranched, monosialylated/complex/dibranched, and monosialylated/fucosylated/dibranched entities.
10024660	5	22	theme	fucosylated/complex/dibranched	924:953	arg1	structures					871:880	The N- glycan structures	857:880	The N- glycan structures	857:880	The N- glycan structures were elucidated to be complex/dibranched, fucosylated/complex/dibranched, monosialylated/complex/dibranched, and monosialylated/fucosylated/dibranched entities.
10024660	1	23	theme	matrix-assisted	292:306	arg1	spectrometry					356:367	matrix-assisted laser desorption/ionization time-of-flight mass spectrometry	292:367	matrix-assisted laser desorption/ionization time-of-flight mass spectrometry	292:367	The detailed structures of N- glycans derived from bile salt-stimulated lipase (BSSL) found in human milk were determined by combining exoglycosidase digestion with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry.
10024660	0	24	link	N-linked	35:42	arg1	oligosaccharides					44:59	the N-linked oligosaccharides	31:59	the N-linked oligosaccharides	31:59	Structural characterization of the N-linked oligosaccharides in bile salt-stimulated lipase originated from human breast milk.
10024660	4	25	from	BSSL	722:725	arg1	present					711:717	present	711:717	present	711:717	The molecular mass profile of esterified N- glycans present in BSSL further permitted the more detailed studies through collision-induced dissociation (CID) and sequential exoglycosidase cleavages.
10024660	5	26	theme	monosialylated/complex/dibranched	956:988	arg1	entities					1033:1040	complex/dibranched, fucosylated/complex/dibranched, monosialylated/complex/dibranched, and monosialylated/fucosylated/dibranched entities	904:1040	complex/dibranched, fucosylated/complex/dibranched, monosialylated/complex/dibranched, and monosialylated/fucosylated/dibranched entities	904:1040	The N- glycan structures were elucidated to be complex/dibranched, fucosylated/complex/dibranched, monosialylated/complex/dibranched, and monosialylated/fucosylated/dibranched entities.
10024660	5	26	theme	monosialylated/complex/dibranched	956:988	arg1	structures					871:880	The N- glycan structures	857:880	The N- glycan structures	857:880	The N- glycan structures were elucidated to be complex/dibranched, fucosylated/complex/dibranched, monosialylated/complex/dibranched, and monosialylated/fucosylated/dibranched entities.
10024660	1	27	theme	laser	308:312	arg1	spectrometry					356:367	matrix-assisted laser desorption/ionization time-of-flight mass spectrometry	292:367	matrix-assisted laser desorption/ionization time-of-flight mass spectrometry	292:367	The detailed structures of N- glycans derived from bile salt-stimulated lipase (BSSL) found in human milk were determined by combining exoglycosidase digestion with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry.
10024660	4	28	theme	esterified	689:698	arg1	glycans					703:709	esterified N- glycans	689:709	esterified N- glycans present in BSSL	689:725	The molecular mass profile of esterified N- glycans present in BSSL further permitted the more detailed studies through collision-induced dissociation (CID) and sequential exoglycosidase cleavages.
10024660	3	29	theme	monosialylated	632:645	arg1	structures					647:656	monosialylated structures	632:656	monosialylated structures	632:656	Ion-exchange chromatography with pulsed amperometric detection, together with mass-spectral analysis of the esterified N- glycans, indicated the presence of monosialylated structures.
10024660	2	30	theme	fucosylation	461:472	arg1	complexity					436:445	complexity	436:445	complexity	436:445	The N- glycan structures were conclusively determined in terms of complexity and degree of fucosylation.
10024660	2	30	theme	fucosylation	461:472	arg1	degree					451:456	degree	451:456	degree	451:456	The N- glycan structures were conclusively determined in terms of complexity and degree of fucosylation.
10024660	0	31	theme	oligosaccharides	44:59	arg1	characterization					11:26	Structural characterization	0:26	Structural characterization of the N-linked oligosaccharides in bile salt-stimulated lipase	0:90	Structural characterization of the N-linked oligosaccharides in bile salt-stimulated lipase originated from human breast milk.
10024660	1	32	theme	desorption/ionization	314:334	arg1	spectrometry					356:367	matrix-assisted laser desorption/ionization time-of-flight mass spectrometry	292:367	matrix-assisted laser desorption/ionization time-of-flight mass spectrometry	292:367	The detailed structures of N- glycans derived from bile salt-stimulated lipase (BSSL) found in human milk were determined by combining exoglycosidase digestion with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry.
10024660	4	33	from	present	711:717	arg1	BSSL					722:725	BSSL	722:725	BSSL	722:725	The molecular mass profile of esterified N- glycans present in BSSL further permitted the more detailed studies through collision-induced dissociation (CID) and sequential exoglycosidase cleavages.
10024660	3	34	theme	amperometric	515:526	arg1	detection					528:536	pulsed amperometric detection	508:536	pulsed amperometric detection	508:536	Ion-exchange chromatography with pulsed amperometric detection, together with mass-spectral analysis of the esterified N- glycans, indicated the presence of monosialylated structures.
10024660	0	35	theme	N-linked	35:42	arg1	oligosaccharides					44:59	the N-linked oligosaccharides	31:59	the N-linked oligosaccharides	31:59	Structural characterization of the N-linked oligosaccharides in bile salt-stimulated lipase originated from human breast milk.
10024660	1	36	theme	time-of-flight	336:349	arg1	spectrometry					356:367	matrix-assisted laser desorption/ionization time-of-flight mass spectrometry	292:367	matrix-assisted laser desorption/ionization time-of-flight mass spectrometry	292:367	The detailed structures of N- glycans derived from bile salt-stimulated lipase (BSSL) found in human milk were determined by combining exoglycosidase digestion with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry.
10024660	4	37	theme	glycans	703:709	arg1	profile					678:684	The molecular mass profile	659:684	The molecular mass profile of esterified N- glycans present in BSSL	659:725	The molecular mass profile of esterified N- glycans present in BSSL further permitted the more detailed studies through collision-induced dissociation (CID) and sequential exoglycosidase cleavages.
10024660	5	38	theme	monosialylated/fucosylated/dibranched	995:1031	arg1	entities					1033:1040	complex/dibranched, fucosylated/complex/dibranched, monosialylated/complex/dibranched, and monosialylated/fucosylated/dibranched entities	904:1040	complex/dibranched, fucosylated/complex/dibranched, monosialylated/complex/dibranched, and monosialylated/fucosylated/dibranched entities	904:1040	The N- glycan structures were elucidated to be complex/dibranched, fucosylated/complex/dibranched, monosialylated/complex/dibranched, and monosialylated/fucosylated/dibranched entities.
10024660	5	38	theme	monosialylated/fucosylated/dibranched	995:1031	arg1	structures					871:880	The N- glycan structures	857:880	The N- glycan structures	857:880	The N- glycan structures were elucidated to be complex/dibranched, fucosylated/complex/dibranched, monosialylated/complex/dibranched, and monosialylated/fucosylated/dibranched entities.
10024660	2	39	theme	degree	451:456	arg1	terms					427:431	terms	427:431	terms of complexity and degree of fucosylation	427:472	The N- glycan structures were conclusively determined in terms of complexity and degree of fucosylation.
10024660	0	40	theme	bile	64:67	arg1	lipase					85:90	bile salt-stimulated lipase	64:90	bile salt-stimulated lipase	64:90	Structural characterization of the N-linked oligosaccharides in bile salt-stimulated lipase originated from human breast milk.
10024660	1	41	theme	mass	351:354	arg1	spectrometry					356:367	matrix-assisted laser desorption/ionization time-of-flight mass spectrometry	292:367	matrix-assisted laser desorption/ionization time-of-flight mass spectrometry	292:367	The detailed structures of N- glycans derived from bile salt-stimulated lipase (BSSL) found in human milk were determined by combining exoglycosidase digestion with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry.
10024660	5	42	theme	N-	861:862	arg1	entities					1033:1040	complex/dibranched, fucosylated/complex/dibranched, monosialylated/complex/dibranched, and monosialylated/fucosylated/dibranched entities	904:1040	complex/dibranched, fucosylated/complex/dibranched, monosialylated/complex/dibranched, and monosialylated/fucosylated/dibranched entities	904:1040	The N- glycan structures were elucidated to be complex/dibranched, fucosylated/complex/dibranched, monosialylated/complex/dibranched, and monosialylated/fucosylated/dibranched entities.
10024660	5	42	theme	N-	861:862	arg1	structures					871:880	The N- glycan structures	857:880	The N- glycan structures	857:880	The N- glycan structures were elucidated to be complex/dibranched, fucosylated/complex/dibranched, monosialylated/complex/dibranched, and monosialylated/fucosylated/dibranched entities.
10024660	3	43	with	chromatography	488:501	arg1	analysis					567:574	mass-spectral analysis	553:574	mass-spectral analysis of the esterified N- glycans	553:603	Ion-exchange chromatography with pulsed amperometric detection, together with mass-spectral analysis of the esterified N- glycans, indicated the presence of monosialylated structures.
10024660	3	43	with	chromatography	488:501	arg1	detection					528:536	pulsed amperometric detection	508:536	pulsed amperometric detection	508:536	Ion-exchange chromatography with pulsed amperometric detection, together with mass-spectral analysis of the esterified N- glycans, indicated the presence of monosialylated structures.
10024660	4	44	attach	present	711:717	arg2	glycans					703:709	esterified N- glycans	689:709	esterified N- glycans present in BSSL	689:725	The molecular mass profile of esterified N- glycans present in BSSL further permitted the more detailed studies through collision-induced dissociation (CID) and sequential exoglycosidase cleavages.
10024660	4	44	attach	present	711:717	arg1	BSSL					722:725	BSSL	722:725	BSSL	722:725	The molecular mass profile of esterified N- glycans present in BSSL further permitted the more detailed studies through collision-induced dissociation (CID) and sequential exoglycosidase cleavages.
10024660	1	45	theme	detailed	131:138	arg1	structures					140:149	The detailed structures	127:149	The detailed structures of N- glycans derived from bile salt-stimulated lipase (BSSL) found in human milk	127:231	The detailed structures of N- glycans derived from bile salt-stimulated lipase (BSSL) found in human milk were determined by combining exoglycosidase digestion with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry.
10024660	2	46	theme	N-	374:375	arg1	structures					384:393	The N- glycan structures	370:393	The N- glycan structures	370:393	The N- glycan structures were conclusively determined in terms of complexity and degree of fucosylation.
10024660	1	47	theme	human	222:226	arg1	milk					228:231	human milk	222:231	human milk	222:231	The detailed structures of N- glycans derived from bile salt-stimulated lipase (BSSL) found in human milk were determined by combining exoglycosidase digestion with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry.
10024660	3	48	theme	glycans	597:603	arg1	analysis					567:574	mass-spectral analysis	553:574	mass-spectral analysis of the esterified N- glycans	553:603	Ion-exchange chromatography with pulsed amperometric detection, together with mass-spectral analysis of the esterified N- glycans, indicated the presence of monosialylated structures.
10024660	3	49	gly	monosialylated	632:645	arg1	structures					647:656	monosialylated structures	632:656	monosialylated structures	632:656	Ion-exchange chromatography with pulsed amperometric detection, together with mass-spectral analysis of the esterified N- glycans, indicated the presence of monosialylated structures.
10024660	3	50	theme	pulsed	508:513	arg1	detection					528:536	pulsed amperometric detection	508:536	pulsed amperometric detection	508:536	Ion-exchange chromatography with pulsed amperometric detection, together with mass-spectral analysis of the esterified N- glycans, indicated the presence of monosialylated structures.
10024660	1	51	located	found	213:217	arg1	milk					228:231	human milk	222:231	human milk	222:231	The detailed structures of N- glycans derived from bile salt-stimulated lipase (BSSL) found in human milk were determined by combining exoglycosidase digestion with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry.
10024660	1	51	located	found	213:217	arg2	BSSL					207:210	BSSL	207:210	BSSL	207:210	The detailed structures of N- glycans derived from bile salt-stimulated lipase (BSSL) found in human milk were determined by combining exoglycosidase digestion with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry.
10024660	1	51	located	found	213:217	arg2	lipase					199:204	bile salt-stimulated lipase	178:204	bile salt-stimulated lipase (BSSL) found in human milk	178:231	The detailed structures of N- glycans derived from bile salt-stimulated lipase (BSSL) found in human milk were determined by combining exoglycosidase digestion with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry.
10024660	1	52	theme	N-	154:155	arg1	glycans					157:163	N- glycans	154:163	N- glycans derived from bile salt-stimulated lipase (BSSL) found in human milk	154:231	The detailed structures of N- glycans derived from bile salt-stimulated lipase (BSSL) found in human milk were determined by combining exoglycosidase digestion with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry.
10024660	2	53	theme	complexity	436:445	arg1	terms					427:431	terms	427:431	terms of complexity and degree of fucosylation	427:472	The N- glycan structures were conclusively determined in terms of complexity and degree of fucosylation.
10024660	2	54	theme	glycan	377:382	arg1	structures					384:393	The N- glycan structures	370:393	The N- glycan structures	370:393	The N- glycan structures were conclusively determined in terms of complexity and degree of fucosylation.
10024660	0	55	theme	salt-stimulated	69:83	arg1	lipase					85:90	bile salt-stimulated lipase	64:90	bile salt-stimulated lipase	64:90	Structural characterization of the N-linked oligosaccharides in bile salt-stimulated lipase originated from human breast milk.
10024660	3	56	dep	together	539:546	arg1	with					548:551	with	548:551	with	548:551	Ion-exchange chromatography with pulsed amperometric detection, together with mass-spectral analysis of the esterified N- glycans, indicated the presence of monosialylated structures.
10024660	1	57	theme	glycans	157:163	arg1	structures					140:149	The detailed structures	127:149	The detailed structures of N- glycans derived from bile salt-stimulated lipase (BSSL) found in human milk	127:231	The detailed structures of N- glycans derived from bile salt-stimulated lipase (BSSL) found in human milk were determined by combining exoglycosidase digestion with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry.
10024660	4	58	theme	N-	700:701	arg1	glycans					703:709	esterified N- glycans	689:709	esterified N- glycans present in BSSL	689:725	The molecular mass profile of esterified N- glycans present in BSSL further permitted the more detailed studies through collision-induced dissociation (CID) and sequential exoglycosidase cleavages.
8202534	0	0	theme	deposits	71:78	arg1	constituent					48:58	an invariant constituent	35:58	an invariant constituent of amyloid deposits	35:78	Human serum amyloid P component is an invariant constituent of amyloid deposits and has a uniquely homogeneous glycostructure.
8202534	0	0	theme	deposits	71:78	arg1	component					22:30	Human serum amyloid P component	0:30	Human serum amyloid P component	0:30	Human serum amyloid P component is an invariant constituent of amyloid deposits and has a uniquely homogeneous glycostructure.
8202534	1	1	theme	tissue	279:284	arg1	deposits					286:293	the abnormal tissue deposits	266:293	the abnormal tissue deposits	266:293	Human serum amyloid P component (SAP) is a normal plasma protein and the precursor of amyloid P component (AP), a universal constituent of the abnormal tissue deposits in amyloidosis, including Alzheimer disease.
8202534	1	1	theme	tissue	279:284	arg1	disease					331:337	Alzheimer disease	321:337	Alzheimer disease	321:337	Human serum amyloid P component (SAP) is a normal plasma protein and the precursor of amyloid P component (AP), a universal constituent of the abnormal tissue deposits in amyloidosis, including Alzheimer disease.
8202534	1	2	theme	P	147:147	arg1	protein					184:190	a normal plasma protein	168:190	a normal plasma protein	168:190	Human serum amyloid P component (SAP) is a normal plasma protein and the precursor of amyloid P component (AP), a universal constituent of the abnormal tissue deposits in amyloidosis, including Alzheimer disease.
8202534	1	2	theme	P	147:147	arg1	SAP					160:162	SAP	160:162	SAP	160:162	Human serum amyloid P component (SAP) is a normal plasma protein and the precursor of amyloid P component (AP), a universal constituent of the abnormal tissue deposits in amyloidosis, including Alzheimer disease.
8202534	1	2	theme	P	147:147	arg1	component					149:157	Human serum amyloid P component	127:157	Human serum amyloid P component (SAP)	127:163	Human serum amyloid P component (SAP) is a normal plasma protein and the precursor of amyloid P component (AP), a universal constituent of the abnormal tissue deposits in amyloidosis, including Alzheimer disease.
8202534	1	3	theme	amyloid	213:219	arg1	component					223:231	amyloid P component	213:231	amyloid P component	213:231	Human serum amyloid P component (SAP) is a normal plasma protein and the precursor of amyloid P component (AP), a universal constituent of the abnormal tissue deposits in amyloidosis, including Alzheimer disease.
8202534	0	4	theme	amyloid	63:69	arg1	deposits					71:78	amyloid deposits	63:78	amyloid deposits	63:78	Human serum amyloid P component is an invariant constituent of amyloid deposits and has a uniquely homogeneous glycostructure.
8202534	1	5	theme	deposits	286:293	arg1	constituent					251:261	a universal constituent	239:261	a universal constituent of the abnormal tissue deposits in amyloidosis, including Alzheimer disease	239:337	Human serum amyloid P component (SAP) is a normal plasma protein and the precursor of amyloid P component (AP), a universal constituent of the abnormal tissue deposits in amyloidosis, including Alzheimer disease.
8202534	1	5	theme	deposits	286:293	arg1	protein					184:190	a normal plasma protein	168:190	a normal plasma protein	168:190	Human serum amyloid P component (SAP) is a normal plasma protein and the precursor of amyloid P component (AP), a universal constituent of the abnormal tissue deposits in amyloidosis, including Alzheimer disease.
8202534	2	6	theme	characteristic	454:467	arg1	microheterogeneity					427:444	the microheterogeneity	423:444	the microheterogeneity usually characteristic of glycoproteins	423:484	We show here that its single N-linked biantennary oligosaccharide does not display the microheterogeneity usually characteristic of glycoproteins.
8202534	3	7	dep	invariant	541:549	arg1	structures					514:523	the glycan structures	503:523	the glycan structures of AP	503:529	The protein and the glycan structures of AP were also invariant, their resistance to degradation suggesting a role in persistence of amyloid deposits.
8202534	3	7	dep	invariant	541:549	arg1	suggesting					584:593	suggesting	584:593	suggesting a role in persistence of amyloid deposits	584:635	The protein and the glycan structures of AP were also invariant, their resistance to degradation suggesting a role in persistence of amyloid deposits.
8202534	3	7	dep	invariant	541:549	arg1	protein					491:497	The protein	487:497	The protein	487:497	The protein and the glycan structures of AP were also invariant, their resistance to degradation suggesting a role in persistence of amyloid deposits.
8202534	3	7	dep	invariant	541:549	arg1	invariant					541:549	invariant	541:549	invariant	541:549	The protein and the glycan structures of AP were also invariant, their resistance to degradation suggesting a role in persistence of amyloid deposits.
8202534	1	8	theme	P	221:221	arg1	component					223:231	amyloid P component	213:231	amyloid P component	213:231	Human serum amyloid P component (SAP) is a normal plasma protein and the precursor of amyloid P component (AP), a universal constituent of the abnormal tissue deposits in amyloidosis, including Alzheimer disease.
8202534	6	9	theme	hepatic	873:879	arg1	uptake					881:886	Rapid hepatic uptake	867:886	Rapid hepatic uptake	867:886	Rapid hepatic uptake and catabolism of human asialo-SAP in man were also directly demonstrated.
8202534	2	10	link	N-linked	369:376	arg1	oligosaccharide					390:404	its single N-linked biantennary oligosaccharide	358:404	its single N-linked biantennary oligosaccharide	358:404	We show here that its single N-linked biantennary oligosaccharide does not display the microheterogeneity usually characteristic of glycoproteins.
8202534	4	11	theme	galactose	735:743	arg1	residues					745:752	terminal galactose residues	726:752	terminal galactose residues	726:752	Asialo-SAP was rapidly cleared from the circulation in mice by a mechanism dependent on terminal galactose residues and was catabolized in hepatocytes.
8202534	1	12	theme	component	223:231	arg1	precursor					200:208	the precursor	196:208	the precursor of amyloid P component	196:231	Human serum amyloid P component (SAP) is a normal plasma protein and the precursor of amyloid P component (AP), a universal constituent of the abnormal tissue deposits in amyloidosis, including Alzheimer disease.
8202534	1	12	theme	component	223:231	arg1	constituent					251:261	a universal constituent	239:261	a universal constituent of the abnormal tissue deposits in amyloidosis, including Alzheimer disease	239:337	Human serum amyloid P component (SAP) is a normal plasma protein and the precursor of amyloid P component (AP), a universal constituent of the abnormal tissue deposits in amyloidosis, including Alzheimer disease.
8202534	1	12	theme	component	223:231	arg1	AP					234:235	AP	234:235	AP	234:235	Human serum amyloid P component (SAP) is a normal plasma protein and the precursor of amyloid P component (AP), a universal constituent of the abnormal tissue deposits in amyloidosis, including Alzheimer disease.
8202534	1	12	theme	component	223:231	arg1	component					149:157	Human serum amyloid P component	127:157	Human serum amyloid P component (SAP)	127:163	Human serum amyloid P component (SAP) is a normal plasma protein and the precursor of amyloid P component (AP), a universal constituent of the abnormal tissue deposits in amyloidosis, including Alzheimer disease.
8202534	1	12	theme	component	223:231	arg1	protein					184:190	a normal plasma protein	168:190	a normal plasma protein	168:190	Human serum amyloid P component (SAP) is a normal plasma protein and the precursor of amyloid P component (AP), a universal constituent of the abnormal tissue deposits in amyloidosis, including Alzheimer disease.
8202534	6	13	theme	Rapid	867:871	arg1	uptake					881:886	Rapid hepatic uptake	867:886	Rapid hepatic uptake	867:886	Rapid hepatic uptake and catabolism of human asialo-SAP in man were also directly demonstrated.
8202534	1	14	from	constituent	251:261	arg1	amyloidosis					298:308	amyloidosis	298:308	amyloidosis	298:308	Human serum amyloid P component (SAP) is a normal plasma protein and the precursor of amyloid P component (AP), a universal constituent of the abnormal tissue deposits in amyloidosis, including Alzheimer disease.
8202534	4	15	theme	terminal	726:733	arg1	residues					745:752	terminal galactose residues	726:752	terminal galactose residues	726:752	Asialo-SAP was rapidly cleared from the circulation in mice by a mechanism dependent on terminal galactose residues and was catabolized in hepatocytes.
8202534	7	16	theme	glycoprotein	1055:1066	arg1	important					1081:1089	important	1081:1089	important	1081:1089	The protein and glycan homogeneity of SAP and the integrity of AP suggest that the complete glycoprotein structure is important for the normal and the pathophysiological functions of this molecule.
8202534	7	16	theme	glycoprotein	1055:1066	arg1	structure					1068:1076	the complete glycoprotein structure	1042:1076	the complete glycoprotein structure	1042:1076	The protein and glycan homogeneity of SAP and the integrity of AP suggest that the complete glycoprotein structure is important for the normal and the pathophysiological functions of this molecule.
8202534	5	17	theme	pathway	815:821	arg1	blockade					798:805	blockade	798:805	blockade of this pathway	798:821	However blockade of this pathway did not affect the clearance of native SAP.
8202534	7	18	theme	molecule	1151:1158	arg1	functions					1133:1141	the pathophysiological functions	1110:1141	the pathophysiological functions of this molecule	1110:1158	The protein and glycan homogeneity of SAP and the integrity of AP suggest that the complete glycoprotein structure is important for the normal and the pathophysiological functions of this molecule.
8202534	3	19	theme	glycan	507:512	arg1	structures					514:523	the glycan structures	503:523	the glycan structures of AP	503:529	The protein and the glycan structures of AP were also invariant, their resistance to degradation suggesting a role in persistence of amyloid deposits.
8202534	3	19	theme	glycan	507:512	arg1	suggesting					584:593	suggesting	584:593	suggesting a role in persistence of amyloid deposits	584:635	The protein and the glycan structures of AP were also invariant, their resistance to degradation suggesting a role in persistence of amyloid deposits.
8202534	3	19	theme	glycan	507:512	arg1	invariant					541:549	invariant	541:549	invariant	541:549	The protein and the glycan structures of AP were also invariant, their resistance to degradation suggesting a role in persistence of amyloid deposits.
8202534	7	20	gly	glycoprotein	1055:1066	arg1	glycoprotein					1055:1066	the complete glycoprotein structure	1042:1076	the complete glycoprotein structure	1042:1076	The protein and glycan homogeneity of SAP and the integrity of AP suggest that the complete glycoprotein structure is important for the normal and the pathophysiological functions of this molecule.
8202534	0	21	theme	serum	6:10	arg1	constituent					48:58	an invariant constituent	35:58	an invariant constituent of amyloid deposits	35:78	Human serum amyloid P component is an invariant constituent of amyloid deposits and has a uniquely homogeneous glycostructure.
8202534	0	21	theme	serum	6:10	arg1	component					22:30	Human serum amyloid P component	0:30	Human serum amyloid P component	0:30	Human serum amyloid P component is an invariant constituent of amyloid deposits and has a uniquely homogeneous glycostructure.
8202534	1	22	theme	Alzheimer	321:329	arg1	disease					331:337	Alzheimer disease	321:337	Alzheimer disease	321:337	Human serum amyloid P component (SAP) is a normal plasma protein and the precursor of amyloid P component (AP), a universal constituent of the abnormal tissue deposits in amyloidosis, including Alzheimer disease.
8202534	6	23	from	uptake	881:886	arg1	man					926:928	man	926:928	man	926:928	Rapid hepatic uptake and catabolism of human asialo-SAP in man were also directly demonstrated.
8202534	3	24	from	role	597:600	arg1	persistence					605:615	persistence	605:615	persistence of amyloid deposits	605:635	The protein and the glycan structures of AP were also invariant, their resistance to degradation suggesting a role in persistence of amyloid deposits.
8202534	0	25	theme	Human	0:4	arg1	constituent					48:58	an invariant constituent	35:58	an invariant constituent of amyloid deposits	35:78	Human serum amyloid P component is an invariant constituent of amyloid deposits and has a uniquely homogeneous glycostructure.
8202534	0	25	theme	Human	0:4	arg1	component					22:30	Human serum amyloid P component	0:30	Human serum amyloid P component	0:30	Human serum amyloid P component is an invariant constituent of amyloid deposits and has a uniquely homogeneous glycostructure.
8202534	7	26	gly	homogeneity	986:996	arg1	AP					1026:1027	AP	1026:1027	AP	1026:1027	The protein and glycan homogeneity of SAP and the integrity of AP suggest that the complete glycoprotein structure is important for the normal and the pathophysiological functions of this molecule.
8202534	7	26	gly	homogeneity	986:996	arg1	SAP					1001:1003	SAP	1001:1003	SAP	1001:1003	The protein and glycan homogeneity of SAP and the integrity of AP suggest that the complete glycoprotein structure is important for the normal and the pathophysiological functions of this molecule.
8202534	7	27	theme	complete	1046:1053	arg1	important					1081:1089	important	1081:1089	important	1081:1089	The protein and glycan homogeneity of SAP and the integrity of AP suggest that the complete glycoprotein structure is important for the normal and the pathophysiological functions of this molecule.
8202534	7	27	theme	complete	1046:1053	arg1	structure					1068:1076	the complete glycoprotein structure	1042:1076	the complete glycoprotein structure	1042:1076	The protein and glycan homogeneity of SAP and the integrity of AP suggest that the complete glycoprotein structure is important for the normal and the pathophysiological functions of this molecule.
8202534	2	28	gly	glycoproteins	472:484	arg1	glycoproteins					472:484	glycoproteins	472:484	glycoproteins	472:484	We show here that its single N-linked biantennary oligosaccharide does not display the microheterogeneity usually characteristic of glycoproteins.
8202534	0	29	theme	P	20:20	arg1	constituent					48:58	an invariant constituent	35:58	an invariant constituent of amyloid deposits	35:78	Human serum amyloid P component is an invariant constituent of amyloid deposits and has a uniquely homogeneous glycostructure.
8202534	0	29	theme	P	20:20	arg1	component					22:30	Human serum amyloid P component	0:30	Human serum amyloid P component	0:30	Human serum amyloid P component is an invariant constituent of amyloid deposits and has a uniquely homogeneous glycostructure.
8202534	3	30	theme	AP	528:529	arg1	structures					514:523	the glycan structures	503:523	the glycan structures of AP	503:529	The protein and the glycan structures of AP were also invariant, their resistance to degradation suggesting a role in persistence of amyloid deposits.
8202534	3	30	theme	AP	528:529	arg1	suggesting					584:593	suggesting	584:593	suggesting a role in persistence of amyloid deposits	584:635	The protein and the glycan structures of AP were also invariant, their resistance to degradation suggesting a role in persistence of amyloid deposits.
8202534	3	30	theme	AP	528:529	arg1	protein					491:497	The protein	487:497	The protein	487:497	The protein and the glycan structures of AP were also invariant, their resistance to degradation suggesting a role in persistence of amyloid deposits.
8202534	3	30	theme	AP	528:529	arg1	invariant					541:549	invariant	541:549	invariant	541:549	The protein and the glycan structures of AP were also invariant, their resistance to degradation suggesting a role in persistence of amyloid deposits.
8202534	2	31	theme	single	362:367	arg1	oligosaccharide					390:404	its single N-linked biantennary oligosaccharide	358:404	its single N-linked biantennary oligosaccharide	358:404	We show here that its single N-linked biantennary oligosaccharide does not display the microheterogeneity usually characteristic of glycoproteins.
8202534	0	32	theme	amyloid	12:18	arg1	constituent					48:58	an invariant constituent	35:58	an invariant constituent of amyloid deposits	35:78	Human serum amyloid P component is an invariant constituent of amyloid deposits and has a uniquely homogeneous glycostructure.
8202534	0	32	theme	amyloid	12:18	arg1	component					22:30	Human serum amyloid P component	0:30	Human serum amyloid P component	0:30	Human serum amyloid P component is an invariant constituent of amyloid deposits and has a uniquely homogeneous glycostructure.
8202534	0	33	theme	homogeneous	99:109	arg1	glycostructure					111:124	a uniquely homogeneous glycostructure	88:124	a uniquely homogeneous glycostructure	88:124	Human serum amyloid P component is an invariant constituent of amyloid deposits and has a uniquely homogeneous glycostructure.
8202534	4	34	theme	dependent	713:721	arg1	mechanism					703:711	a mechanism	701:711	a mechanism dependent on terminal galactose residues	701:752	Asialo-SAP was rapidly cleared from the circulation in mice by a mechanism dependent on terminal galactose residues and was catabolized in hepatocytes.
8202534	1	35	theme	normal	170:175	arg1	constituent					251:261	a universal constituent	239:261	a universal constituent of the abnormal tissue deposits in amyloidosis, including Alzheimer disease	239:337	Human serum amyloid P component (SAP) is a normal plasma protein and the precursor of amyloid P component (AP), a universal constituent of the abnormal tissue deposits in amyloidosis, including Alzheimer disease.
8202534	1	35	theme	normal	170:175	arg1	AP					234:235	AP	234:235	AP	234:235	Human serum amyloid P component (SAP) is a normal plasma protein and the precursor of amyloid P component (AP), a universal constituent of the abnormal tissue deposits in amyloidosis, including Alzheimer disease.
8202534	1	35	theme	normal	170:175	arg1	component					149:157	Human serum amyloid P component	127:157	Human serum amyloid P component (SAP)	127:163	Human serum amyloid P component (SAP) is a normal plasma protein and the precursor of amyloid P component (AP), a universal constituent of the abnormal tissue deposits in amyloidosis, including Alzheimer disease.
8202534	1	35	theme	normal	170:175	arg1	protein					184:190	a normal plasma protein	168:190	a normal plasma protein	168:190	Human serum amyloid P component (SAP) is a normal plasma protein and the precursor of amyloid P component (AP), a universal constituent of the abnormal tissue deposits in amyloidosis, including Alzheimer disease.
8202534	1	36	from	deposits	286:293	arg1	amyloidosis					298:308	amyloidosis	298:308	amyloidosis	298:308	Human serum amyloid P component (SAP) is a normal plasma protein and the precursor of amyloid P component (AP), a universal constituent of the abnormal tissue deposits in amyloidosis, including Alzheimer disease.
8202534	3	37	theme	amyloid	620:626	arg1	deposits					628:635	amyloid deposits	620:635	amyloid deposits	620:635	The protein and the glycan structures of AP were also invariant, their resistance to degradation suggesting a role in persistence of amyloid deposits.
8202534	1	38	theme	plasma	177:182	arg1	constituent					251:261	a universal constituent	239:261	a universal constituent of the abnormal tissue deposits in amyloidosis, including Alzheimer disease	239:337	Human serum amyloid P component (SAP) is a normal plasma protein and the precursor of amyloid P component (AP), a universal constituent of the abnormal tissue deposits in amyloidosis, including Alzheimer disease.
8202534	1	38	theme	plasma	177:182	arg1	AP					234:235	AP	234:235	AP	234:235	Human serum amyloid P component (SAP) is a normal plasma protein and the precursor of amyloid P component (AP), a universal constituent of the abnormal tissue deposits in amyloidosis, including Alzheimer disease.
8202534	1	38	theme	plasma	177:182	arg1	component					149:157	Human serum amyloid P component	127:157	Human serum amyloid P component (SAP)	127:163	Human serum amyloid P component (SAP) is a normal plasma protein and the precursor of amyloid P component (AP), a universal constituent of the abnormal tissue deposits in amyloidosis, including Alzheimer disease.
8202534	1	38	theme	plasma	177:182	arg1	protein					184:190	a normal plasma protein	168:190	a normal plasma protein	168:190	Human serum amyloid P component (SAP) is a normal plasma protein and the precursor of amyloid P component (AP), a universal constituent of the abnormal tissue deposits in amyloidosis, including Alzheimer disease.
8202534	7	39	theme	pathophysiological	1114:1131	arg1	functions					1133:1141	the pathophysiological functions	1110:1141	the pathophysiological functions of this molecule	1110:1158	The protein and glycan homogeneity of SAP and the integrity of AP suggest that the complete glycoprotein structure is important for the normal and the pathophysiological functions of this molecule.
8202534	1	40	theme	universal	241:249	arg1	constituent					251:261	a universal constituent	239:261	a universal constituent of the abnormal tissue deposits in amyloidosis, including Alzheimer disease	239:337	Human serum amyloid P component (SAP) is a normal plasma protein and the precursor of amyloid P component (AP), a universal constituent of the abnormal tissue deposits in amyloidosis, including Alzheimer disease.
8202534	1	40	theme	universal	241:249	arg1	protein					184:190	a normal plasma protein	168:190	a normal plasma protein	168:190	Human serum amyloid P component (SAP) is a normal plasma protein and the precursor of amyloid P component (AP), a universal constituent of the abnormal tissue deposits in amyloidosis, including Alzheimer disease.
8202534	7	41	theme	AP	1026:1027	arg1	integrity					1013:1021	the integrity	1009:1021	the integrity of AP	1009:1027	The protein and glycan homogeneity of SAP and the integrity of AP suggest that the complete glycoprotein structure is important for the normal and the pathophysiological functions of this molecule.
8202534	7	41	theme	AP	1026:1027	arg1	homogeneity					986:996	The protein and glycan homogeneity	963:996	homogeneity	986:996	The protein and glycan homogeneity of SAP and the integrity of AP suggest that the complete glycoprotein structure is important for the normal and the pathophysiological functions of this molecule.
8202534	1	42	from	amyloidosis	298:308	arg1	constituent					251:261	a universal constituent	239:261	a universal constituent of the abnormal tissue deposits in amyloidosis, including Alzheimer disease	239:337	Human serum amyloid P component (SAP) is a normal plasma protein and the precursor of amyloid P component (AP), a universal constituent of the abnormal tissue deposits in amyloidosis, including Alzheimer disease.
8202534	1	42	from	amyloidosis	298:308	arg1	protein					184:190	a normal plasma protein	168:190	a normal plasma protein	168:190	Human serum amyloid P component (SAP) is a normal plasma protein and the precursor of amyloid P component (AP), a universal constituent of the abnormal tissue deposits in amyloidosis, including Alzheimer disease.
8202534	0	43	theme	invariant	38:46	arg1	constituent					48:58	an invariant constituent	35:58	an invariant constituent of amyloid deposits	35:78	Human serum amyloid P component is an invariant constituent of amyloid deposits and has a uniquely homogeneous glycostructure.
8202534	0	43	theme	invariant	38:46	arg1	component					22:30	Human serum amyloid P component	0:30	Human serum amyloid P component	0:30	Human serum amyloid P component is an invariant constituent of amyloid deposits and has a uniquely homogeneous glycostructure.
8202534	5	44	theme	native	855:860	arg1	SAP					862:864	native SAP	855:864	native SAP	855:864	However blockade of this pathway did not affect the clearance of native SAP.
8202534	2	45	theme	biantennary	378:388	arg1	oligosaccharide					390:404	its single N-linked biantennary oligosaccharide	358:404	its single N-linked biantennary oligosaccharide	358:404	We show here that its single N-linked biantennary oligosaccharide does not display the microheterogeneity usually characteristic of glycoproteins.
8202534	6	46	theme	human	906:910	arg1	asialo-SAP					912:921	human asialo-SAP	906:921	human asialo-SAP	906:921	Rapid hepatic uptake and catabolism of human asialo-SAP in man were also directly demonstrated.
8202534	7	47	theme	SAP	1001:1003	arg1	integrity					1013:1021	the integrity	1009:1021	the integrity of AP	1009:1027	The protein and glycan homogeneity of SAP and the integrity of AP suggest that the complete glycoprotein structure is important for the normal and the pathophysiological functions of this molecule.
8202534	7	47	theme	SAP	1001:1003	arg1	homogeneity					986:996	The protein and glycan homogeneity	963:996	homogeneity	986:996	The protein and glycan homogeneity of SAP and the integrity of AP suggest that the complete glycoprotein structure is important for the normal and the pathophysiological functions of this molecule.
8202534	0	48	contain	has	84:86	arg1	constituent					48:58	an invariant constituent	35:58	an invariant constituent of amyloid deposits	35:78	Human serum amyloid P component is an invariant constituent of amyloid deposits and has a uniquely homogeneous glycostructure.
8202534	0	48	contain	has	84:86	arg2	glycostructure					111:124	a uniquely homogeneous glycostructure	88:124	a uniquely homogeneous glycostructure	88:124	Human serum amyloid P component is an invariant constituent of amyloid deposits and has a uniquely homogeneous glycostructure.
8202534	0	48	contain	has	84:86	arg1	component					22:30	Human serum amyloid P component	0:30	Human serum amyloid P component	0:30	Human serum amyloid P component is an invariant constituent of amyloid deposits and has a uniquely homogeneous glycostructure.
8202534	7	49	theme	glycan	979:984	arg1	homogeneity					986:996	The protein and glycan homogeneity	963:996	homogeneity	986:996	The protein and glycan homogeneity of SAP and the integrity of AP suggest that the complete glycoprotein structure is important for the normal and the pathophysiological functions of this molecule.
8202534	3	50	theme	deposits	628:635	arg1	persistence					605:615	persistence	605:615	persistence of amyloid deposits	605:635	The protein and the glycan structures of AP were also invariant, their resistance to degradation suggesting a role in persistence of amyloid deposits.
8202534	1	51	theme	Human	127:131	arg1	protein					184:190	a normal plasma protein	168:190	a normal plasma protein	168:190	Human serum amyloid P component (SAP) is a normal plasma protein and the precursor of amyloid P component (AP), a universal constituent of the abnormal tissue deposits in amyloidosis, including Alzheimer disease.
8202534	1	51	theme	Human	127:131	arg1	SAP					160:162	SAP	160:162	SAP	160:162	Human serum amyloid P component (SAP) is a normal plasma protein and the precursor of amyloid P component (AP), a universal constituent of the abnormal tissue deposits in amyloidosis, including Alzheimer disease.
8202534	1	51	theme	Human	127:131	arg1	component					149:157	Human serum amyloid P component	127:157	Human serum amyloid P component (SAP)	127:163	Human serum amyloid P component (SAP) is a normal plasma protein and the precursor of amyloid P component (AP), a universal constituent of the abnormal tissue deposits in amyloidosis, including Alzheimer disease.
8202534	2	52	theme	glycoproteins	472:484	arg1	characteristic					454:467	characteristic	454:467	characteristic	454:467	We show here that its single N-linked biantennary oligosaccharide does not display the microheterogeneity usually characteristic of glycoproteins.
8202534	5	53	theme	SAP	862:864	arg1	clearance					842:850	the clearance	838:850	the clearance of native SAP	838:864	However blockade of this pathway did not affect the clearance of native SAP.
8202534	7	54	theme	protein	967:973	arg1	homogeneity					986:996	The protein and glycan homogeneity	963:996	homogeneity	986:996	The protein and glycan homogeneity of SAP and the integrity of AP suggest that the complete glycoprotein structure is important for the normal and the pathophysiological functions of this molecule.
8202534	1	55	theme	serum	133:137	arg1	protein					184:190	a normal plasma protein	168:190	a normal plasma protein	168:190	Human serum amyloid P component (SAP) is a normal plasma protein and the precursor of amyloid P component (AP), a universal constituent of the abnormal tissue deposits in amyloidosis, including Alzheimer disease.
8202534	1	55	theme	serum	133:137	arg1	SAP					160:162	SAP	160:162	SAP	160:162	Human serum amyloid P component (SAP) is a normal plasma protein and the precursor of amyloid P component (AP), a universal constituent of the abnormal tissue deposits in amyloidosis, including Alzheimer disease.
8202534	1	55	theme	serum	133:137	arg1	component					149:157	Human serum amyloid P component	127:157	Human serum amyloid P component (SAP)	127:163	Human serum amyloid P component (SAP) is a normal plasma protein and the precursor of amyloid P component (AP), a universal constituent of the abnormal tissue deposits in amyloidosis, including Alzheimer disease.
8202534	4	56	from	circulation	678:688	arg1	mice					693:696	mice	693:696	mice	693:696	Asialo-SAP was rapidly cleared from the circulation in mice by a mechanism dependent on terminal galactose residues and was catabolized in hepatocytes.
8202534	1	57	theme	abnormal	270:277	arg1	deposits					286:293	the abnormal tissue deposits	266:293	the abnormal tissue deposits	266:293	Human serum amyloid P component (SAP) is a normal plasma protein and the precursor of amyloid P component (AP), a universal constituent of the abnormal tissue deposits in amyloidosis, including Alzheimer disease.
8202534	1	57	theme	abnormal	270:277	arg1	disease					331:337	Alzheimer disease	321:337	Alzheimer disease	321:337	Human serum amyloid P component (SAP) is a normal plasma protein and the precursor of amyloid P component (AP), a universal constituent of the abnormal tissue deposits in amyloidosis, including Alzheimer disease.
8202534	2	58	theme	N-linked	369:376	arg1	oligosaccharide					390:404	its single N-linked biantennary oligosaccharide	358:404	its single N-linked biantennary oligosaccharide	358:404	We show here that its single N-linked biantennary oligosaccharide does not display the microheterogeneity usually characteristic of glycoproteins.
8202534	1	59	theme	amyloid	139:145	arg1	protein					184:190	a normal plasma protein	168:190	a normal plasma protein	168:190	Human serum amyloid P component (SAP) is a normal plasma protein and the precursor of amyloid P component (AP), a universal constituent of the abnormal tissue deposits in amyloidosis, including Alzheimer disease.
8202534	1	59	theme	amyloid	139:145	arg1	SAP					160:162	SAP	160:162	SAP	160:162	Human serum amyloid P component (SAP) is a normal plasma protein and the precursor of amyloid P component (AP), a universal constituent of the abnormal tissue deposits in amyloidosis, including Alzheimer disease.
8202534	1	59	theme	amyloid	139:145	arg1	component					149:157	Human serum amyloid P component	127:157	Human serum amyloid P component (SAP)	127:163	Human serum amyloid P component (SAP) is a normal plasma protein and the precursor of amyloid P component (AP), a universal constituent of the abnormal tissue deposits in amyloidosis, including Alzheimer disease.
8202534	6	60	from	catabolism	892:901	arg1	man					926:928	man	926:928	man	926:928	Rapid hepatic uptake and catabolism of human asialo-SAP in man were also directly demonstrated.
8202534	6	61	theme	asialo-SAP	912:921	arg1	uptake					881:886	Rapid hepatic uptake	867:886	Rapid hepatic uptake	867:886	Rapid hepatic uptake and catabolism of human asialo-SAP in man were also directly demonstrated.
8202534	6	61	theme	asialo-SAP	912:921	arg1	catabolism					892:901	catabolism	892:901	catabolism	892:901	Rapid hepatic uptake and catabolism of human asialo-SAP in man were also directly demonstrated.
108268	3	0	from	19,500	605:610	arg1	weight					583:588	apparent molecular weight	564:588	apparent molecular weight from 23,500 to 19,500	564:610	The structure and proportion of each of these is: formula : (see text) : Removal of the oligosaccharide moiety with glycosidases results in an increased mobility of J chain in sodium dodecyl sulfate polyacrylamide gel electrophoresis corresponding to a shift in apparent molecular weight from 23,500 to 19,500.
108268	3	0	from	19,500	605:610	arg1	shift					555:559	a shift	553:559	a shift in apparent molecular weight from 23,500 to 19,500	553:610	The structure and proportion of each of these is: formula : (see text) : Removal of the oligosaccharide moiety with glycosidases results in an increased mobility of J chain in sodium dodecyl sulfate polyacrylamide gel electrophoresis corresponding to a shift in apparent molecular weight from 23,500 to 19,500.
108268	1	1	theme	Waldenströms	131:142	arg1	Wa					158:159	a Waldenströms macroglobulin Wa	129:159	a Waldenströms macroglobulin Wa	129:159	The complete structure of the oligosaccharide moiety of J chain isolated from a Waldenströms macroglobulin Wa has been established.
108268	3	2	dep	19,500	605:610	arg1	to					602:603	to	602:603	to	602:603	The structure and proportion of each of these is: formula : (see text) : Removal of the oligosaccharide moiety with glycosidases results in an increased mobility of J chain in sodium dodecyl sulfate polyacrylamide gel electrophoresis corresponding to a shift in apparent molecular weight from 23,500 to 19,500.
108268	3	3	with	Removal	375:381	arg1	glycosidases					418:429	glycosidases	418:429	glycosidases	418:429	The structure and proportion of each of these is: formula : (see text) : Removal of the oligosaccharide moiety with glycosidases results in an increased mobility of J chain in sodium dodecyl sulfate polyacrylamide gel electrophoresis corresponding to a shift in apparent molecular weight from 23,500 to 19,500.
108268	1	4	attach	isolated	115:122	arg1	Wa					158:159	a Waldenströms macroglobulin Wa	129:159	a Waldenströms macroglobulin Wa	129:159	The complete structure of the oligosaccharide moiety of J chain isolated from a Waldenströms macroglobulin Wa has been established.
108268	1	4	attach	isolated	115:122	arg2	structure					64:72	The complete structure	51:72	The complete structure of the oligosaccharide moiety of J chain isolated from a Waldenströms macroglobulin Wa	51:159	The complete structure of the oligosaccharide moiety of J chain isolated from a Waldenströms macroglobulin Wa has been established.
108268	1	5	theme	macroglobulin	144:156	arg1	Wa					158:159	a Waldenströms macroglobulin Wa	129:159	a Waldenströms macroglobulin Wa	129:159	The complete structure of the oligosaccharide moiety of J chain isolated from a Waldenströms macroglobulin Wa has been established.
108268	3	6	theme	J	467:467	arg1	chain					469:473	J chain	467:473	J chain in sodium dodecyl sulfate polyacrylamide gel electrophoresis corresponding to a shift in apparent molecular weight from 23,500 to 19,500	467:610	The structure and proportion of each of these is: formula : (see text) : Removal of the oligosaccharide moiety with glycosidases results in an increased mobility of J chain in sodium dodecyl sulfate polyacrylamide gel electrophoresis corresponding to a shift in apparent molecular weight from 23,500 to 19,500.
108268	3	7	theme	sodium	478:483	arg1	electrophoresis					520:534	sodium dodecyl sulfate polyacrylamide gel electrophoresis	478:534	sodium dodecyl sulfate polyacrylamide gel electrophoresis corresponding to a shift in apparent molecular weight from 23,500 to 19,500	478:610	The structure and proportion of each of these is: formula : (see text) : Removal of the oligosaccharide moiety with glycosidases results in an increased mobility of J chain in sodium dodecyl sulfate polyacrylamide gel electrophoresis corresponding to a shift in apparent molecular weight from 23,500 to 19,500.
108268	2	8	located	present	206:212	arg2	oligosaccharide					187:201	The oligosaccharide	183:201	The oligosaccharide	183:201	The oligosaccharide is present in three forms differing in the amount of sialic acid and designated J-A, J-B, and J-C.
108268	2	8	located	present	206:212	arg1	forms					223:227	three forms	217:227	three forms differing in the amount of sialic acid and designated J-A, J-B, and J-C	217:299	The oligosaccharide is present in three forms differing in the amount of sialic acid and designated J-A, J-B, and J-C.
108268	2	8	located	present	206:212	arg2	present					206:212	present	206:212	present	206:212	The oligosaccharide is present in three forms differing in the amount of sialic acid and designated J-A, J-B, and J-C.
108268	3	9	theme	chain	469:473	arg1	mobility					455:462	an increased mobility	442:462	an increased mobility of J chain in sodium dodecyl sulfate polyacrylamide gel electrophoresis corresponding to a shift in apparent molecular weight from 23,500 to 19,500	442:610	The structure and proportion of each of these is: formula : (see text) : Removal of the oligosaccharide moiety with glycosidases results in an increased mobility of J chain in sodium dodecyl sulfate polyacrylamide gel electrophoresis corresponding to a shift in apparent molecular weight from 23,500 to 19,500.
108268	2	10	theme	acid	263:266	arg1	acid					263:266	sialic acid	256:266	sialic acid	256:266	The oligosaccharide is present in three forms differing in the amount of sialic acid and designated J-A, J-B, and J-C.
108268	2	10	theme	acid	263:266	arg1	J-A					283:285	designated J-A	272:285	designated J-A	272:285	The oligosaccharide is present in three forms differing in the amount of sialic acid and designated J-A, J-B, and J-C.
108268	2	10	theme	acid	263:266	arg1	J-B					288:290	J-B	288:290	J-B	288:290	The oligosaccharide is present in three forms differing in the amount of sialic acid and designated J-A, J-B, and J-C.
108268	2	10	theme	acid	263:266	arg1	amount					246:251	the amount	242:251	the amount of sialic acid and designated J-A	242:285	The oligosaccharide is present in three forms differing in the amount of sialic acid and designated J-A, J-B, and J-C.
108268	4	11	theme	glycopeptides	658:670	arg1	utilization					633:643	utilization	633:643	utilization	633:643	The preparation and utilization of iodinated glycopeptides for sequence analysis is presented.
108268	4	11	theme	glycopeptides	658:670	arg1	preparation					617:627	preparation	617:627	preparation	617:627	The preparation and utilization of iodinated glycopeptides for sequence analysis is presented.
108268	1	12	theme	complete	55:62	arg1	structure					64:72	The complete structure	51:72	The complete structure of the oligosaccharide moiety of J chain isolated from a Waldenströms macroglobulin Wa	51:159	The complete structure of the oligosaccharide moiety of J chain isolated from a Waldenströms macroglobulin Wa has been established.
108268	2	13	from	present	206:212	arg1	forms					223:227	three forms	217:227	three forms differing in the amount of sialic acid and designated J-A, J-B, and J-C	217:299	The oligosaccharide is present in three forms differing in the amount of sialic acid and designated J-A, J-B, and J-C.
108268	3	14	from	shift	555:559	arg1	weight					583:588	apparent molecular weight	564:588	apparent molecular weight from 23,500 to 19,500	564:610	The structure and proportion of each of these is: formula : (see text) : Removal of the oligosaccharide moiety with glycosidases results in an increased mobility of J chain in sodium dodecyl sulfate polyacrylamide gel electrophoresis corresponding to a shift in apparent molecular weight from 23,500 to 19,500.
108268	3	14	from	shift	555:559	arg1	19,500					605:610	19,500	605:610	19,500	605:610	The structure and proportion of each of these is: formula : (see text) : Removal of the oligosaccharide moiety with glycosidases results in an increased mobility of J chain in sodium dodecyl sulfate polyacrylamide gel electrophoresis corresponding to a shift in apparent molecular weight from 23,500 to 19,500.
108268	2	15	from	forms	223:227	arg1	present					206:212	present	206:212	present	206:212	The oligosaccharide is present in three forms differing in the amount of sialic acid and designated J-A, J-B, and J-C.
108268	2	15	from	forms	223:227	arg1	oligosaccharide					187:201	The oligosaccharide	183:201	The oligosaccharide	183:201	The oligosaccharide is present in three forms differing in the amount of sialic acid and designated J-A, J-B, and J-C.
108268	3	16	dep	formula	352:358	arg1	see					363:365	see	363:365	see text	363:370	The structure and proportion of each of these is: formula : (see text) : Removal of the oligosaccharide moiety with glycosidases results in an increased mobility of J chain in sodium dodecyl sulfate polyacrylamide gel electrophoresis corresponding to a shift in apparent molecular weight from 23,500 to 19,500.
108268	3	17	theme	dodecyl	485:491	arg1	electrophoresis					520:534	sodium dodecyl sulfate polyacrylamide gel electrophoresis	478:534	sodium dodecyl sulfate polyacrylamide gel electrophoresis corresponding to a shift in apparent molecular weight from 23,500 to 19,500	478:610	The structure and proportion of each of these is: formula : (see text) : Removal of the oligosaccharide moiety with glycosidases results in an increased mobility of J chain in sodium dodecyl sulfate polyacrylamide gel electrophoresis corresponding to a shift in apparent molecular weight from 23,500 to 19,500.
108268	4	18	dep	preparation	617:627	arg1	The					613:615	The	613:615	The	613:615	The preparation and utilization of iodinated glycopeptides for sequence analysis is presented.
108268	3	19	dep	these	342:346	arg1	is					348:349	is	348:349	is	348:349	The structure and proportion of each of these is: formula : (see text) : Removal of the oligosaccharide moiety with glycosidases results in an increased mobility of J chain in sodium dodecyl sulfate polyacrylamide gel electrophoresis corresponding to a shift in apparent molecular weight from 23,500 to 19,500.
108268	3	20	theme	sulfate	493:499	arg1	electrophoresis					520:534	sodium dodecyl sulfate polyacrylamide gel electrophoresis	478:534	sodium dodecyl sulfate polyacrylamide gel electrophoresis corresponding to a shift in apparent molecular weight from 23,500 to 19,500	478:610	The structure and proportion of each of these is: formula : (see text) : Removal of the oligosaccharide moiety with glycosidases results in an increased mobility of J chain in sodium dodecyl sulfate polyacrylamide gel electrophoresis corresponding to a shift in apparent molecular weight from 23,500 to 19,500.
108268	0	21	theme	oligosaccharide	17:31	arg1	Structure					0:8	Structure	0:8	Structure of the oligosaccharide of human J chain	0:48	Structure of the oligosaccharide of human J chain.
108268	4	22	theme	sequence	676:683	arg1	analysis					685:692	sequence analysis	676:692	sequence analysis	676:692	The preparation and utilization of iodinated glycopeptides for sequence analysis is presented.
108268	2	23	theme	J-A	283:285	arg1	acid					263:266	sialic acid	256:266	sialic acid	256:266	The oligosaccharide is present in three forms differing in the amount of sialic acid and designated J-A, J-B, and J-C.
108268	2	23	theme	J-A	283:285	arg1	J-A					283:285	designated J-A	272:285	designated J-A	272:285	The oligosaccharide is present in three forms differing in the amount of sialic acid and designated J-A, J-B, and J-C.
108268	2	23	theme	J-A	283:285	arg1	J-B					288:290	J-B	288:290	J-B	288:290	The oligosaccharide is present in three forms differing in the amount of sialic acid and designated J-A, J-B, and J-C.
108268	2	23	theme	J-A	283:285	arg1	amount					246:251	the amount	242:251	the amount of sialic acid and designated J-A	242:285	The oligosaccharide is present in three forms differing in the amount of sialic acid and designated J-A, J-B, and J-C.
108268	3	24	theme	each	334:337	arg1	structure					306:314	The structure	302:314	The structure	302:314	The structure and proportion of each of these is: formula : (see text) : Removal of the oligosaccharide moiety with glycosidases results in an increased mobility of J chain in sodium dodecyl sulfate polyacrylamide gel electrophoresis corresponding to a shift in apparent molecular weight from 23,500 to 19,500.
108268	3	24	theme	each	334:337	arg1	proportion					320:329	proportion	320:329	proportion	320:329	The structure and proportion of each of these is: formula : (see text) : Removal of the oligosaccharide moiety with glycosidases results in an increased mobility of J chain in sodium dodecyl sulfate polyacrylamide gel electrophoresis corresponding to a shift in apparent molecular weight from 23,500 to 19,500.
108268	2	25	theme	sialic	256:261	arg1	acid					263:266	sialic acid	256:266	sialic acid	256:266	The oligosaccharide is present in three forms differing in the amount of sialic acid and designated J-A, J-B, and J-C.
108268	1	26	theme	moiety	97:102	arg1	structure					64:72	The complete structure	51:72	The complete structure of the oligosaccharide moiety of J chain isolated from a Waldenströms macroglobulin Wa	51:159	The complete structure of the oligosaccharide moiety of J chain isolated from a Waldenströms macroglobulin Wa has been established.
108268	3	27	from	electrophoresis	520:534	arg1	mobility					455:462	an increased mobility	442:462	an increased mobility of J chain in sodium dodecyl sulfate polyacrylamide gel electrophoresis corresponding to a shift in apparent molecular weight from 23,500 to 19,500	442:610	The structure and proportion of each of these is: formula : (see text) : Removal of the oligosaccharide moiety with glycosidases results in an increased mobility of J chain in sodium dodecyl sulfate polyacrylamide gel electrophoresis corresponding to a shift in apparent molecular weight from 23,500 to 19,500.
108268	0	28	theme	human	36:40	arg1	chain					44:48	human J chain	36:48	human J chain	36:48	Structure of the oligosaccharide of human J chain.
108268	4	29	gly	glycopeptides	658:670	arg2	glycopeptides					658:670	iodinated glycopeptides	648:670	iodinated glycopeptides	648:670	The preparation and utilization of iodinated glycopeptides for sequence analysis is presented.
108268	3	30	theme	apparent	564:571	arg1	weight					583:588	apparent molecular weight	564:588	apparent molecular weight from 23,500 to 19,500	564:610	The structure and proportion of each of these is: formula : (see text) : Removal of the oligosaccharide moiety with glycosidases results in an increased mobility of J chain in sodium dodecyl sulfate polyacrylamide gel electrophoresis corresponding to a shift in apparent molecular weight from 23,500 to 19,500.
108268	0	31	theme	chain	44:48	arg1	oligosaccharide					17:31	the oligosaccharide	13:31	the oligosaccharide of human J chain	13:48	Structure of the oligosaccharide of human J chain.
108268	3	32	theme	molecular	573:581	arg1	weight					583:588	apparent molecular weight	564:588	apparent molecular weight from 23,500 to 19,500	564:610	The structure and proportion of each of these is: formula : (see text) : Removal of the oligosaccharide moiety with glycosidases results in an increased mobility of J chain in sodium dodecyl sulfate polyacrylamide gel electrophoresis corresponding to a shift in apparent molecular weight from 23,500 to 19,500.
108268	3	33	theme	polyacrylamide	501:514	arg1	electrophoresis					520:534	sodium dodecyl sulfate polyacrylamide gel electrophoresis	478:534	sodium dodecyl sulfate polyacrylamide gel electrophoresis corresponding to a shift in apparent molecular weight from 23,500 to 19,500	478:610	The structure and proportion of each of these is: formula : (see text) : Removal of the oligosaccharide moiety with glycosidases results in an increased mobility of J chain in sodium dodecyl sulfate polyacrylamide gel electrophoresis corresponding to a shift in apparent molecular weight from 23,500 to 19,500.
108268	4	34	theme	iodinated	648:656	arg1	glycopeptides					658:670	iodinated glycopeptides	648:670	iodinated glycopeptides	648:670	The preparation and utilization of iodinated glycopeptides for sequence analysis is presented.
108268	0	35	theme	J	42:42	arg1	chain					44:48	human J chain	36:48	human J chain	36:48	Structure of the oligosaccharide of human J chain.
108268	3	36	dep	structure	306:314	arg1	formula					352:358	formula :	352:360	The structure and proportion of each of these is: formula : (see text) : Removal of the oligosaccharide moiety with glycosidases results in an increased mobility of J chain in sodium dodecyl sulfate polyacrylamide gel electrophoresis corresponding to a shift in apparent molecular weight from 23,500 to 19,500.	302:611	The structure and proportion of each of these is: formula : (see text) : Removal of the oligosaccharide moiety with glycosidases results in an increased mobility of J chain in sodium dodecyl sulfate polyacrylamide gel electrophoresis corresponding to a shift in apparent molecular weight from 23,500 to 19,500.
108268	3	36	dep	structure	306:314	arg1	results					431:437	results	431:437	results in an increased mobility of J chain in sodium dodecyl sulfate polyacrylamide gel electrophoresis corresponding to a shift in apparent molecular weight from 23,500 to 19,500	431:610	The structure and proportion of each of these is: formula : (see text) : Removal of the oligosaccharide moiety with glycosidases results in an increased mobility of J chain in sodium dodecyl sulfate polyacrylamide gel electrophoresis corresponding to a shift in apparent molecular weight from 23,500 to 19,500.
108268	3	37	theme	gel	516:518	arg1	electrophoresis					520:534	sodium dodecyl sulfate polyacrylamide gel electrophoresis	478:534	sodium dodecyl sulfate polyacrylamide gel electrophoresis corresponding to a shift in apparent molecular weight from 23,500 to 19,500	478:610	The structure and proportion of each of these is: formula : (see text) : Removal of the oligosaccharide moiety with glycosidases results in an increased mobility of J chain in sodium dodecyl sulfate polyacrylamide gel electrophoresis corresponding to a shift in apparent molecular weight from 23,500 to 19,500.
108268	1	38	theme	J	107:107	arg1	chain					109:113	J chain	107:113	J chain	107:113	The complete structure of the oligosaccharide moiety of J chain isolated from a Waldenströms macroglobulin Wa has been established.
108268	2	39	theme	designated	272:281	arg1	J-A					283:285	designated J-A	272:285	designated J-A	272:285	The oligosaccharide is present in three forms differing in the amount of sialic acid and designated J-A, J-B, and J-C.
108268	1	40	theme	chain	109:113	arg1	moiety					97:102	the oligosaccharide moiety	77:102	the oligosaccharide moiety of J chain	77:113	The complete structure of the oligosaccharide moiety of J chain isolated from a Waldenströms macroglobulin Wa has been established.
108268	1	41	theme	oligosaccharide	81:95	arg1	moiety					97:102	the oligosaccharide moiety	77:102	the oligosaccharide moiety of J chain	77:113	The complete structure of the oligosaccharide moiety of J chain isolated from a Waldenströms macroglobulin Wa has been established.
108268	3	42	theme	moiety	406:411	arg1	Removal					375:381	Removal	375:381	Removal of the oligosaccharide moiety with glycosidases	375:429	The structure and proportion of each of these is: formula : (see text) : Removal of the oligosaccharide moiety with glycosidases results in an increased mobility of J chain in sodium dodecyl sulfate polyacrylamide gel electrophoresis corresponding to a shift in apparent molecular weight from 23,500 to 19,500.
108268	3	43	theme	oligosaccharide	390:404	arg1	moiety					406:411	the oligosaccharide moiety	386:411	the oligosaccharide moiety	386:411	The structure and proportion of each of these is: formula : (see text) : Removal of the oligosaccharide moiety with glycosidases results in an increased mobility of J chain in sodium dodecyl sulfate polyacrylamide gel electrophoresis corresponding to a shift in apparent molecular weight from 23,500 to 19,500.
108268	3	44	from	chain	469:473	arg1	electrophoresis					520:534	sodium dodecyl sulfate polyacrylamide gel electrophoresis	478:534	sodium dodecyl sulfate polyacrylamide gel electrophoresis corresponding to a shift in apparent molecular weight from 23,500 to 19,500	478:610	The structure and proportion of each of these is: formula : (see text) : Removal of the oligosaccharide moiety with glycosidases results in an increased mobility of J chain in sodium dodecyl sulfate polyacrylamide gel electrophoresis corresponding to a shift in apparent molecular weight from 23,500 to 19,500.
108268	2	45	attach	present	206:212	arg2	present					206:212	present	206:212	present	206:212	The oligosaccharide is present in three forms differing in the amount of sialic acid and designated J-A, J-B, and J-C.
108268	2	45	attach	present	206:212	arg2	oligosaccharide					187:201	The oligosaccharide	183:201	The oligosaccharide	183:201	The oligosaccharide is present in three forms differing in the amount of sialic acid and designated J-A, J-B, and J-C.
108268	2	45	attach	present	206:212	arg1	forms					223:227	three forms	217:227	three forms differing in the amount of sialic acid and designated J-A, J-B, and J-C	217:299	The oligosaccharide is present in three forms differing in the amount of sialic acid and designated J-A, J-B, and J-C.
108268	3	46	theme	increased	445:453	arg1	mobility					455:462	an increased mobility	442:462	an increased mobility of J chain in sodium dodecyl sulfate polyacrylamide gel electrophoresis corresponding to a shift in apparent molecular weight from 23,500 to 19,500	442:610	The structure and proportion of each of these is: formula : (see text) : Removal of the oligosaccharide moiety with glycosidases results in an increased mobility of J chain in sodium dodecyl sulfate polyacrylamide gel electrophoresis corresponding to a shift in apparent molecular weight from 23,500 to 19,500.
108268	3	47	from	mobility	455:462	arg1	electrophoresis					520:534	sodium dodecyl sulfate polyacrylamide gel electrophoresis	478:534	sodium dodecyl sulfate polyacrylamide gel electrophoresis corresponding to a shift in apparent molecular weight from 23,500 to 19,500	478:610	The structure and proportion of each of these is: formula : (see text) : Removal of the oligosaccharide moiety with glycosidases results in an increased mobility of J chain in sodium dodecyl sulfate polyacrylamide gel electrophoresis corresponding to a shift in apparent molecular weight from 23,500 to 19,500.
9334252	3	0	theme	cultured	627:634	arg1	cells					648:652	cultured human HL-60 cells	627:652	cultured human HL-60 cells	627:652	To answer the first question, RNase 2, which is identical to the eosinophil-derived neurotoxin, was isolated from intracellular stores of cultured human HL-60 cells.
9334252	1	1	from	urine	168:172	arg1	RNase					149:153	RNase 2	149:155	RNase 2 from human urine	149:172	C2-alpha-Mannosyltryptophan was discovered in RNase 2 from human urine, representing a novel way of attaching carbohydrate to a protein.
9334252	5	2	theme	immunological	822:834	arg1	analysis					849:856	immunological and chemical analysis	822:856	immunological and chemical analysis of RNase 2 purified from the supernatant of transiently transformed cells from different organisms	822:955	The second question was investigated by immunological and chemical analysis of RNase 2 purified from the supernatant of transiently transformed cells from different organisms.
9334252	8	3	theme	plant	1409:1413	arg1	protoplasts					1415:1425	plant protoplasts	1409:1425	plant protoplasts	1409:1425	Recombinant RNase 2 isolated from insect cells, plant protoplasts, and Escherichia coli was not C-mannosylated.
9334252	7	4	gly	C-mannosylated	1311:1324	arg1	proteins					1326:1333	C-mannosylated proteins	1311:1333	C-mannosylated proteins other than RNase 2	1311:1352	The observation that pig kidney cells contain the machinery for C-mannosylation of Trp-7 of human RNase 2 but that the homologous RNase from porcine kidney is not a substrate, since it does not contain a tryptophan at position 7, strongly suggests that C-mannosylated proteins other than RNase 2 exist.
9334252	7	5	theme	Trp-7	1141:1145	arg1	substrate					1223:1231	a substrate	1221:1231	a substrate	1221:1231	The observation that pig kidney cells contain the machinery for C-mannosylation of Trp-7 of human RNase 2 but that the homologous RNase from porcine kidney is not a substrate, since it does not contain a tryptophan at position 7, strongly suggests that C-mannosylated proteins other than RNase 2 exist.
9334252	7	5	theme	Trp-7	1141:1145	arg1	C-mannosylation					1122:1136	C-mannosylation	1122:1136	C-mannosylation of Trp-7 of human RNase 2 but that the homologous RNase from porcine kidney	1122:1212	The observation that pig kidney cells contain the machinery for C-mannosylation of Trp-7 of human RNase 2 but that the homologous RNase from porcine kidney is not a substrate, since it does not contain a tryptophan at position 7, strongly suggests that C-mannosylated proteins other than RNase 2 exist.
9334252	3	6	theme	intracellular	603:615	arg1	stores					617:622	intracellular stores	603:622	intracellular stores of cultured human HL-60 cells	603:652	To answer the first question, RNase 2, which is identical to the eosinophil-derived neurotoxin, was isolated from intracellular stores of cultured human HL-60 cells.
9334252	9	7	theme	C-mannosylation	1561:1575	arg1	aspects					1550:1556	the biochemical aspects	1534:1556	the biochemical aspects of C-mannosylation	1534:1575	These results not only form the basis for further studies on the biochemical aspects of C-mannosylation but also have implications for the choice of cells for production of recombinant glycoproteins.
9334252	6	8	from	man	1014:1016	arg1	cells					1003:1007	cells	1003:1007	cells from man, green monkey, pig, mouse, and hamster	1003:1055	This revealed that C-mannosylation occurs in cells from man, green monkey, pig, mouse, and hamster.
9334252	9	9	theme	biochemical	1538:1548	arg1	aspects					1550:1556	the biochemical aspects	1534:1556	the biochemical aspects of C-mannosylation	1534:1575	These results not only form the basis for further studies on the biochemical aspects of C-mannosylation but also have implications for the choice of cells for production of recombinant glycoproteins.
9334252	3	10	link	eosinophil-derived	554:571	arg1	neurotoxin					573:582	the eosinophil-derived neurotoxin	550:582	the eosinophil-derived neurotoxin	550:582	To answer the first question, RNase 2, which is identical to the eosinophil-derived neurotoxin, was isolated from intracellular stores of cultured human HL-60 cells.
9334252	9	11	theme	glycoproteins	1658:1670	arg1	production					1632:1641	production	1632:1641	production of recombinant glycoproteins	1632:1670	These results not only form the basis for further studies on the biochemical aspects of C-mannosylation but also have implications for the choice of cells for production of recombinant glycoproteins.
9334252	8	12	theme	insect	1395:1400	arg1	cells					1402:1406	insect cells	1395:1406	insect cells	1395:1406	Recombinant RNase 2 isolated from insect cells, plant protoplasts, and Escherichia coli was not C-mannosylated.
9334252	8	13	gly	C-mannosylated	1457:1470	arg1	RNase					1373:1377	Recombinant RNase 2	1361:1379	Recombinant RNase 2 isolated from insect cells, plant protoplasts, and Escherichia coli	1361:1447	Recombinant RNase 2 isolated from insect cells, plant protoplasts, and Escherichia coli was not C-mannosylated.
9334252	7	14	gly	C-mannosylation	1122:1136	arg1	Trp-7					1141:1145	Trp-7	1141:1145	Trp-7 of human RNase 2	1141:1162	The observation that pig kidney cells contain the machinery for C-mannosylation of Trp-7 of human RNase 2 but that the homologous RNase from porcine kidney is not a substrate, since it does not contain a tryptophan at position 7, strongly suggests that C-mannosylated proteins other than RNase 2 exist.
9334252	6	15	from	pig	1033:1035	arg1	cells					1003:1007	cells	1003:1007	cells from man, green monkey, pig, mouse, and hamster	1003:1055	This revealed that C-mannosylation occurs in cells from man, green monkey, pig, mouse, and hamster.
9334252	3	16	theme	cells	648:652	arg1	stores					617:622	intracellular stores	603:622	intracellular stores of cultured human HL-60 cells	603:652	To answer the first question, RNase 2, which is identical to the eosinophil-derived neurotoxin, was isolated from intracellular stores of cultured human HL-60 cells.
9334252	7	17	theme	other	1335:1339	arg1	proteins					1326:1333	C-mannosylated proteins	1311:1333	C-mannosylated proteins other than RNase 2	1311:1352	The observation that pig kidney cells contain the machinery for C-mannosylation of Trp-7 of human RNase 2 but that the homologous RNase from porcine kidney is not a substrate, since it does not contain a tryptophan at position 7, strongly suggests that C-mannosylated proteins other than RNase 2 exist.
9334252	4	18	from	Trp-7	688:692	arg1	C-mannosylated					670:683	C-mannosylated	670:683	C-mannosylated	670:683	The enzyme was C-mannosylated at Trp-7, showing that the modification occurs intracellularly, before secretion of the protein.
9334252	4	18	from	Trp-7	688:692	arg1	enzyme					659:664	The enzyme	655:664	The enzyme	655:664	The enzyme was C-mannosylated at Trp-7, showing that the modification occurs intracellularly, before secretion of the protein.
9334252	7	19	theme	RNase	1156:1160	arg1	Trp-7					1141:1145	Trp-7	1141:1145	Trp-7 of human RNase 2	1141:1162	The observation that pig kidney cells contain the machinery for C-mannosylation of Trp-7 of human RNase 2 but that the homologous RNase from porcine kidney is not a substrate, since it does not contain a tryptophan at position 7, strongly suggests that C-mannosylated proteins other than RNase 2 exist.
9334252	8	20	attach	isolated	1381:1388	arg1	cells					1402:1406	insect cells	1395:1406	insect cells	1395:1406	Recombinant RNase 2 isolated from insect cells, plant protoplasts, and Escherichia coli was not C-mannosylated.
9334252	8	20	attach	isolated	1381:1388	arg1	coli					1444:1447	Escherichia coli	1432:1447	Escherichia coli	1432:1447	Recombinant RNase 2 isolated from insect cells, plant protoplasts, and Escherichia coli was not C-mannosylated.
9334252	8	20	attach	isolated	1381:1388	arg2	RNase					1373:1377	Recombinant RNase 2	1361:1379	Recombinant RNase 2 isolated from insect cells, plant protoplasts, and Escherichia coli	1361:1447	Recombinant RNase 2 isolated from insect cells, plant protoplasts, and Escherichia coli was not C-mannosylated.
9334252	8	20	attach	isolated	1381:1388	arg1	protoplasts					1415:1425	plant protoplasts	1409:1425	plant protoplasts	1409:1425	Recombinant RNase 2 isolated from insect cells, plant protoplasts, and Escherichia coli was not C-mannosylated.
9334252	7	21	theme	homologous	1177:1186	arg1	RNase					1188:1192	the homologous RNase	1173:1192	the homologous RNase from porcine kidney	1173:1212	The observation that pig kidney cells contain the machinery for C-mannosylation of Trp-7 of human RNase 2 but that the homologous RNase from porcine kidney is not a substrate, since it does not contain a tryptophan at position 7, strongly suggests that C-mannosylated proteins other than RNase 2 exist.
9334252	0	22	theme	cells	96:100	arg1	variety					76:82	a variety	74:82	a variety of cultured cells	74:100	C-Mannosylation of human RNase 2 is an intracellular process performed by a variety of cultured cells.
9334252	0	22	theme	cells	96:100	arg1	cells					96:100	cultured cells	87:100	cultured cells	87:100	C-Mannosylation of human RNase 2 is an intracellular process performed by a variety of cultured cells.
9334252	5	23	theme	chemical	840:847	arg1	analysis					849:856	immunological and chemical analysis	822:856	immunological and chemical analysis of RNase 2 purified from the supernatant of transiently transformed cells from different organisms	822:955	The second question was investigated by immunological and chemical analysis of RNase 2 purified from the supernatant of transiently transformed cells from different organisms.
9334252	2	24	theme	intracellular	370:382	arg1	route					397:401	the normal intracellular biosynthetic route	359:401	the normal intracellular biosynthetic route	359:401	Here, we have addressed two questions related to the biosynthesis of this modification: (i) is C-mannosylation part of the normal intracellular biosynthetic route, and (ii) how general is it, i.e. which organisms perform this kind of glycosylation?
9334252	5	25	from	organisms	947:955	arg1	cells					926:930	transiently transformed cells	902:930	transiently transformed cells from different organisms	902:955	The second question was investigated by immunological and chemical analysis of RNase 2 purified from the supernatant of transiently transformed cells from different organisms.
9334252	5	25	from	organisms	947:955	arg1	supernatant					887:897	the supernatant	883:897	the supernatant of transiently transformed cells from different organisms	883:955	The second question was investigated by immunological and chemical analysis of RNase 2 purified from the supernatant of transiently transformed cells from different organisms.
9334252	1	26	theme	human	162:166	arg1	urine					168:172	human urine	162:172	human urine	162:172	C2-alpha-Mannosyltryptophan was discovered in RNase 2 from human urine, representing a novel way of attaching carbohydrate to a protein.
9334252	0	27	theme	cultured	87:94	arg1	cells					96:100	cultured cells	87:100	cultured cells	87:100	C-Mannosylation of human RNase 2 is an intracellular process performed by a variety of cultured cells.
9334252	3	28	theme	human	636:640	arg1	cells					648:652	cultured human HL-60 cells	627:652	cultured human HL-60 cells	627:652	To answer the first question, RNase 2, which is identical to the eosinophil-derived neurotoxin, was isolated from intracellular stores of cultured human HL-60 cells.
9334252	5	29	theme	transformed	914:924	arg1	cells					926:930	transiently transformed cells	902:930	transiently transformed cells from different organisms	902:955	The second question was investigated by immunological and chemical analysis of RNase 2 purified from the supernatant of transiently transformed cells from different organisms.
9334252	5	30	theme	second	786:791	arg1	question					793:800	The second question	782:800	The second question	782:800	The second question was investigated by immunological and chemical analysis of RNase 2 purified from the supernatant of transiently transformed cells from different organisms.
9334252	3	31	theme	HL-60	642:646	arg1	cells					648:652	cultured human HL-60 cells	627:652	cultured human HL-60 cells	627:652	To answer the first question, RNase 2, which is identical to the eosinophil-derived neurotoxin, was isolated from intracellular stores of cultured human HL-60 cells.
9334252	6	32	theme	green	1019:1023	arg1	monkey					1025:1030	green monkey	1019:1030	green monkey	1019:1030	This revealed that C-mannosylation occurs in cells from man, green monkey, pig, mouse, and hamster.
9334252	2	33	theme	C-mannosylation	335:349	arg1	part					351:354	C-mannosylation part	335:354	C-mannosylation part of the normal intracellular biosynthetic route	335:401	Here, we have addressed two questions related to the biosynthesis of this modification: (i) is C-mannosylation part of the normal intracellular biosynthetic route, and (ii) how general is it, i.e. which organisms perform this kind of glycosylation?
9334252	3	34	attach	isolated	589:596	arg1	stores					617:622	intracellular stores	603:622	intracellular stores of cultured human HL-60 cells	603:652	To answer the first question, RNase 2, which is identical to the eosinophil-derived neurotoxin, was isolated from intracellular stores of cultured human HL-60 cells.
9334252	3	34	attach	isolated	589:596	arg2	RNase					519:523	RNase 2	519:525	RNase 2	519:525	To answer the first question, RNase 2, which is identical to the eosinophil-derived neurotoxin, was isolated from intracellular stores of cultured human HL-60 cells.
9334252	4	35	theme	protein	773:779	arg1	secretion					756:764	secretion	756:764	secretion of the protein	756:779	The enzyme was C-mannosylated at Trp-7, showing that the modification occurs intracellularly, before secretion of the protein.
9334252	7	36	contain	contain	1096:1102	arg1	cells					1090:1094	pig kidney cells	1079:1094	pig kidney cells	1079:1094	The observation that pig kidney cells contain the machinery for C-mannosylation of Trp-7 of human RNase 2 but that the homologous RNase from porcine kidney is not a substrate, since it does not contain a tryptophan at position 7, strongly suggests that C-mannosylated proteins other than RNase 2 exist.
9334252	7	36	contain	contain	1096:1102	arg2	machinery					1108:1116	the machinery for C-mannosylation of Trp-7 of human RNase 2 but that the homologous RNase from porcine kidney is not a substrate, since it does not contain a tryptophan at position 7	1104:1285	the machinery for C-mannosylation of Trp-7 of human RNase 2 but that the homologous RNase from porcine kidney is not a substrate, since it does not contain a tryptophan at position 7	1104:1285	The observation that pig kidney cells contain the machinery for C-mannosylation of Trp-7 of human RNase 2 but that the homologous RNase from porcine kidney is not a substrate, since it does not contain a tryptophan at position 7, strongly suggests that C-mannosylated proteins other than RNase 2 exist.
9334252	3	37	theme	first	503:507	arg1	question					509:516	the first question	499:516	the first question	499:516	To answer the first question, RNase 2, which is identical to the eosinophil-derived neurotoxin, was isolated from intracellular stores of cultured human HL-60 cells.
9334252	7	38	theme	porcine	1199:1205	arg1	kidney					1207:1212	porcine kidney	1199:1212	porcine kidney	1199:1212	The observation that pig kidney cells contain the machinery for C-mannosylation of Trp-7 of human RNase 2 but that the homologous RNase from porcine kidney is not a substrate, since it does not contain a tryptophan at position 7, strongly suggests that C-mannosylated proteins other than RNase 2 exist.
9334252	9	39	gly	glycoproteins	1658:1670	arg1	glycoproteins					1658:1670	recombinant glycoproteins	1646:1670	recombinant glycoproteins	1646:1670	These results not only form the basis for further studies on the biochemical aspects of C-mannosylation but also have implications for the choice of cells for production of recombinant glycoproteins.
9334252	0	40	theme	RNase	25:29	arg1	C-Mannosylation					0:14	C-Mannosylation	0:14	C-Mannosylation of human RNase 2	0:31	C-Mannosylation of human RNase 2 is an intracellular process performed by a variety of cultured cells.
9334252	0	40	theme	RNase	25:29	arg1	process					53:59	an intracellular process	36:59	an intracellular process performed by a variety of cultured cells	36:100	C-Mannosylation of human RNase 2 is an intracellular process performed by a variety of cultured cells.
9334252	9	41	theme	recombinant	1646:1656	arg1	glycoproteins					1658:1670	recombinant glycoproteins	1646:1670	recombinant glycoproteins	1646:1670	These results not only form the basis for further studies on the biochemical aspects of C-mannosylation but also have implications for the choice of cells for production of recombinant glycoproteins.
9334252	2	42	theme	related	278:284	arg1	questions					268:276	two questions	264:276	two questions related to the biosynthesis of this modification	264:325	Here, we have addressed two questions related to the biosynthesis of this modification: (i) is C-mannosylation part of the normal intracellular biosynthetic route, and (ii) how general is it, i.e. which organisms perform this kind of glycosylation?
9334252	2	43	theme	biosynthetic	384:395	arg1	route					397:401	the normal intracellular biosynthetic route	359:401	the normal intracellular biosynthetic route	359:401	Here, we have addressed two questions related to the biosynthesis of this modification: (i) is C-mannosylation part of the normal intracellular biosynthetic route, and (ii) how general is it, i.e. which organisms perform this kind of glycosylation?
9334252	2	44	theme	route	397:401	arg1	part					351:354	C-mannosylation part	335:354	C-mannosylation part of the normal intracellular biosynthetic route	335:401	Here, we have addressed two questions related to the biosynthesis of this modification: (i) is C-mannosylation part of the normal intracellular biosynthetic route, and (ii) how general is it, i.e. which organisms perform this kind of glycosylation?
9334252	2	45	theme	glycosylation	474:486	arg1	kind					466:469	this kind	461:469	this kind of glycosylation	461:486	Here, we have addressed two questions related to the biosynthesis of this modification: (i) is C-mannosylation part of the normal intracellular biosynthetic route, and (ii) how general is it, i.e. which organisms perform this kind of glycosylation?
9334252	3	46	theme	eosinophil-derived	554:571	arg1	neurotoxin					573:582	the eosinophil-derived neurotoxin	550:582	the eosinophil-derived neurotoxin	550:582	To answer the first question, RNase 2, which is identical to the eosinophil-derived neurotoxin, was isolated from intracellular stores of cultured human HL-60 cells.
9334252	1	47	theme	novel	190:194	arg1	way					196:198	a novel way	188:198	a novel way of attaching carbohydrate to a protein	188:237	C2-alpha-Mannosyltryptophan was discovered in RNase 2 from human urine, representing a novel way of attaching carbohydrate to a protein.
9334252	6	48	gly	C-mannosylation	977:991	arg2	cells					1003:1007	cells	1003:1007	cells from man, green monkey, pig, mouse, and hamster	1003:1055	This revealed that C-mannosylation occurs in cells from man, green monkey, pig, mouse, and hamster.
9334252	5	49	from	supernatant	887:897	arg1	organisms					947:955	different organisms	937:955	different organisms	937:955	The second question was investigated by immunological and chemical analysis of RNase 2 purified from the supernatant of transiently transformed cells from different organisms.
9334252	7	50	from	position	1276:1283	arg1	tryptophan					1262:1271	a tryptophan	1260:1271	a tryptophan at position 7	1260:1285	The observation that pig kidney cells contain the machinery for C-mannosylation of Trp-7 of human RNase 2 but that the homologous RNase from porcine kidney is not a substrate, since it does not contain a tryptophan at position 7, strongly suggests that C-mannosylated proteins other than RNase 2 exist.
9334252	2	51	theme	normal	363:368	arg1	route					397:401	the normal intracellular biosynthetic route	359:401	the normal intracellular biosynthetic route	359:401	Here, we have addressed two questions related to the biosynthesis of this modification: (i) is C-mannosylation part of the normal intracellular biosynthetic route, and (ii) how general is it, i.e. which organisms perform this kind of glycosylation?
9334252	0	52	theme	human	19:23	arg1	RNase					25:29	human RNase 2	19:31	human RNase 2	19:31	C-Mannosylation of human RNase 2 is an intracellular process performed by a variety of cultured cells.
9334252	7	53	theme	pig	1079:1081	arg1	cells					1090:1094	pig kidney cells	1079:1094	pig kidney cells	1079:1094	The observation that pig kidney cells contain the machinery for C-mannosylation of Trp-7 of human RNase 2 but that the homologous RNase from porcine kidney is not a substrate, since it does not contain a tryptophan at position 7, strongly suggests that C-mannosylated proteins other than RNase 2 exist.
9334252	4	54	gly	C-mannosylated	670:683	arg2	Trp-7					688:692	Trp-7	688:692	Trp-7	688:692	The enzyme was C-mannosylated at Trp-7, showing that the modification occurs intracellularly, before secretion of the protein.
9334252	4	54	gly	C-mannosylated	670:683	arg1	C-mannosylated					670:683	C-mannosylated	670:683	C-mannosylated	670:683	The enzyme was C-mannosylated at Trp-7, showing that the modification occurs intracellularly, before secretion of the protein.
9334252	4	54	gly	C-mannosylated	670:683	arg1	enzyme					659:664	The enzyme	655:664	The enzyme	655:664	The enzyme was C-mannosylated at Trp-7, showing that the modification occurs intracellularly, before secretion of the protein.
9334252	0	55	theme	intracellular	39:51	arg1	process					53:59	an intracellular process	36:59	an intracellular process performed by a variety of cultured cells	36:100	C-Mannosylation of human RNase 2 is an intracellular process performed by a variety of cultured cells.
9334252	0	55	theme	intracellular	39:51	arg1	C-Mannosylation					0:14	C-Mannosylation	0:14	C-Mannosylation of human RNase 2	0:31	C-Mannosylation of human RNase 2 is an intracellular process performed by a variety of cultured cells.
9334252	2	56	dep	it	428:429	arg1	ii					409:410	ii	409:410	ii	409:410	Here, we have addressed two questions related to the biosynthesis of this modification: (i) is C-mannosylation part of the normal intracellular biosynthetic route, and (ii) how general is it, i.e. which organisms perform this kind of glycosylation?
9334252	6	57	from	mouse	1038:1042	arg1	cells					1003:1007	cells	1003:1007	cells from man, green monkey, pig, mouse, and hamster	1003:1055	This revealed that C-mannosylation occurs in cells from man, green monkey, pig, mouse, and hamster.
9334252	2	58	theme	modification	314:325	arg1	biosynthesis					293:304	the biosynthesis	289:304	the biosynthesis of this modification	289:325	Here, we have addressed two questions related to the biosynthesis of this modification: (i) is C-mannosylation part of the normal intracellular biosynthetic route, and (ii) how general is it, i.e. which organisms perform this kind of glycosylation?
9334252	9	59	theme	cells	1622:1626	arg1	choice					1612:1617	the choice	1608:1617	the choice of cells	1608:1626	These results not only form the basis for further studies on the biochemical aspects of C-mannosylation but also have implications for the choice of cells for production of recombinant glycoproteins.
9334252	9	60	from	studies	1523:1529	arg1	aspects					1550:1556	the biochemical aspects	1534:1556	the biochemical aspects of C-mannosylation	1534:1575	These results not only form the basis for further studies on the biochemical aspects of C-mannosylation but also have implications for the choice of cells for production of recombinant glycoproteins.
9334252	8	61	theme	Recombinant	1361:1371	arg1	RNase					1373:1377	Recombinant RNase 2	1361:1379	Recombinant RNase 2 isolated from insect cells, plant protoplasts, and Escherichia coli	1361:1447	Recombinant RNase 2 isolated from insect cells, plant protoplasts, and Escherichia coli was not C-mannosylated.
9334252	6	62	from	hamster	1049:1055	arg1	cells					1003:1007	cells	1003:1007	cells from man, green monkey, pig, mouse, and hamster	1003:1055	This revealed that C-mannosylation occurs in cells from man, green monkey, pig, mouse, and hamster.
9334252	9	63	theme	further	1515:1521	arg1	studies					1523:1529	further studies	1515:1529	further studies on the biochemical aspects of C-mannosylation	1515:1575	These results not only form the basis for further studies on the biochemical aspects of C-mannosylation but also have implications for the choice of cells for production of recombinant glycoproteins.
9334252	5	64	theme	cells	926:930	arg1	supernatant					887:897	the supernatant	883:897	the supernatant of transiently transformed cells from different organisms	883:955	The second question was investigated by immunological and chemical analysis of RNase 2 purified from the supernatant of transiently transformed cells from different organisms.
9334252	9	65	contain	have	1586:1589	arg1	results					1479:1485	These results	1473:1485	These results	1473:1485	These results not only form the basis for further studies on the biochemical aspects of C-mannosylation but also have implications for the choice of cells for production of recombinant glycoproteins.
9334252	9	65	contain	have	1586:1589	arg2	implications					1591:1602	implications	1591:1602	implications for the choice of cells for production of recombinant glycoproteins	1591:1670	These results not only form the basis for further studies on the biochemical aspects of C-mannosylation but also have implications for the choice of cells for production of recombinant glycoproteins.
9334252	1	66	theme	attaching	203:211	arg1	carbohydrate					213:224	attaching carbohydrate	203:224	attaching carbohydrate	203:224	C2-alpha-Mannosyltryptophan was discovered in RNase 2 from human urine, representing a novel way of attaching carbohydrate to a protein.
9334252	7	67	theme	C-mannosylated	1311:1324	arg1	proteins					1326:1333	C-mannosylated proteins	1311:1333	C-mannosylated proteins other than RNase 2	1311:1352	The observation that pig kidney cells contain the machinery for C-mannosylation of Trp-7 of human RNase 2 but that the homologous RNase from porcine kidney is not a substrate, since it does not contain a tryptophan at position 7, strongly suggests that C-mannosylated proteins other than RNase 2 exist.
9334252	5	68	theme	RNase	861:865	arg1	analysis					849:856	immunological and chemical analysis	822:856	immunological and chemical analysis of RNase 2 purified from the supernatant of transiently transformed cells from different organisms	822:955	The second question was investigated by immunological and chemical analysis of RNase 2 purified from the supernatant of transiently transformed cells from different organisms.
9334252	1	69	theme	carbohydrate	213:224	arg1	way					196:198	a novel way	188:198	a novel way of attaching carbohydrate to a protein	188:237	C2-alpha-Mannosyltryptophan was discovered in RNase 2 from human urine, representing a novel way of attaching carbohydrate to a protein.
9334252	7	70	from	kidney	1207:1212	arg1	RNase					1188:1192	the homologous RNase	1173:1192	the homologous RNase from porcine kidney	1173:1212	The observation that pig kidney cells contain the machinery for C-mannosylation of Trp-7 of human RNase 2 but that the homologous RNase from porcine kidney is not a substrate, since it does not contain a tryptophan at position 7, strongly suggests that C-mannosylated proteins other than RNase 2 exist.
9334252	5	71	theme	different	937:945	arg1	organisms					947:955	different organisms	937:955	different organisms	937:955	The second question was investigated by immunological and chemical analysis of RNase 2 purified from the supernatant of transiently transformed cells from different organisms.
9334252	6	72	from	monkey	1025:1030	arg1	cells					1003:1007	cells	1003:1007	cells from man, green monkey, pig, mouse, and hamster	1003:1055	This revealed that C-mannosylation occurs in cells from man, green monkey, pig, mouse, and hamster.
9334252	7	73	contain	contain	1252:1258	arg1	it					1240:1241	it	1240:1241	it	1240:1241	The observation that pig kidney cells contain the machinery for C-mannosylation of Trp-7 of human RNase 2 but that the homologous RNase from porcine kidney is not a substrate, since it does not contain a tryptophan at position 7, strongly suggests that C-mannosylated proteins other than RNase 2 exist.
9334252	7	73	contain	contain	1252:1258	arg2	tryptophan					1262:1271	a tryptophan	1260:1271	a tryptophan at position 7	1260:1285	The observation that pig kidney cells contain the machinery for C-mannosylation of Trp-7 of human RNase 2 but that the homologous RNase from porcine kidney is not a substrate, since it does not contain a tryptophan at position 7, strongly suggests that C-mannosylated proteins other than RNase 2 exist.
9334252	7	74	theme	human	1150:1154	arg1	RNase					1156:1160	human RNase 2	1150:1162	human RNase 2	1150:1162	The observation that pig kidney cells contain the machinery for C-mannosylation of Trp-7 of human RNase 2 but that the homologous RNase from porcine kidney is not a substrate, since it does not contain a tryptophan at position 7, strongly suggests that C-mannosylated proteins other than RNase 2 exist.
9334252	2	75	dep	part	351:354	arg1	i					329:329	i	329:329	i	329:329	Here, we have addressed two questions related to the biosynthesis of this modification: (i) is C-mannosylation part of the normal intracellular biosynthetic route, and (ii) how general is it, i.e. which organisms perform this kind of glycosylation?
9334252	7	76	theme	kidney	1083:1088	arg1	cells					1090:1094	pig kidney cells	1079:1094	pig kidney cells	1079:1094	The observation that pig kidney cells contain the machinery for C-mannosylation of Trp-7 of human RNase 2 but that the homologous RNase from porcine kidney is not a substrate, since it does not contain a tryptophan at position 7, strongly suggests that C-mannosylated proteins other than RNase 2 exist.
7547911	3	0	theme	Overhauser	606:615	arg1	enhancements					617:628	rotating-frame nuclear Overhauser enhancements	583:628	rotating-frame nuclear Overhauser enhancements	583:628	Using vicinal proton-proton coupling constants and rotating-frame nuclear Overhauser enhancements, ewe demonstrate that the C-linked substituent is alpha-mannopyranose.
7547911	1	1	theme	residue	235:241	arg1	ring					216:219	the indole ring	205:219	the indole ring of tryptophan residue 7 of human RNase U(s)	205:263	Recently, the novel C-glycosidic linkage of a hexopyranosyl residue to the indole ring of tryptophan residue 7 of human RNase U(s) was reported [Hofsteenge, J., Müller, D. R., de Beer, T., Löffler A., Richter, W. J., & Vliegenthart, J. F. G. (1994) Biochemistry 33, 13524-13530].
7547911	3	2	theme	proton-proton	546:558	arg1	constants					569:577	vicinal proton-proton coupling constants	538:577	vicinal proton-proton coupling constants	538:577	Using vicinal proton-proton coupling constants and rotating-frame nuclear Overhauser enhancements, ewe demonstrate that the C-linked substituent is alpha-mannopyranose.
7547911	2	3	theme	biological	510:519	arg1	relevance					521:529	its biological relevance	506:529	its biological relevance	506:529	Identification of this monosaccharide is a prerequisite for studies of its biosynthesis and its biological relevance.
7547911	1	4	theme	novel	148:152	arg1	linkage					167:173	the novel C-glycosidic linkage	144:173	the novel C-glycosidic linkage of a hexopyranosyl residue to the indole ring of tryptophan residue 7 of human RNase U(s)	144:263	Recently, the novel C-glycosidic linkage of a hexopyranosyl residue to the indole ring of tryptophan residue 7 of human RNase U(s) was reported [Hofsteenge, J., Müller, D. R., de Beer, T., Löffler A., Richter, W. J., & Vliegenthart, J. F. G. (1994) Biochemistry 33, 13524-13530].
7547911	3	5	theme	coupling	560:567	arg1	constants					569:577	vicinal proton-proton coupling constants	538:577	vicinal proton-proton coupling constants	538:577	Using vicinal proton-proton coupling constants and rotating-frame nuclear Overhauser enhancements, ewe demonstrate that the C-linked substituent is alpha-mannopyranose.
7547911	4	6	theme	mannopyranose	774:786	arg1	moiety					788:793	the mannopyranose moiety	770:793	the mannopyranose moiety in a glycopeptide derived from RNase U(s)	770:835	Furthermore, the nuclear magnetic resonance (NMR) data indicate that the mannopyranose moiety in a glycopeptide derived from RNase U(s) adopts several conformations on the NMR time scale.
7547911	0	7	theme	tryptophan-7	79:90	arg1	chain					70:74	the side chain	61:74	the side chain of tryptophan-7 in human RNase	61:105	The hexopyranosyl residue that is C-glycosidically linked to the side chain of tryptophan-7 in human RNase Us is alpha-mannopyranose.
7547911	1	8	dep	reported	269:276	arg1	1994					377:380	1994	377:380	1994	377:380	Recently, the novel C-glycosidic linkage of a hexopyranosyl residue to the indole ring of tryptophan residue 7 of human RNase U(s) was reported [Hofsteenge, J., Müller, D. R., de Beer, T., Löffler A., Richter, W. J., & Vliegenthart, J. F. G. (1994) Biochemistry 33, 13524-13530].
7547911	1	8	dep	reported	269:276	arg1	Richter					335:341	Richter	335:341	Richter	335:341	Recently, the novel C-glycosidic linkage of a hexopyranosyl residue to the indole ring of tryptophan residue 7 of human RNase U(s) was reported [Hofsteenge, J., Müller, D. R., de Beer, T., Löffler A., Richter, W. J., & Vliegenthart, J. F. G. (1994) Biochemistry 33, 13524-13530].
7547911	1	8	dep	reported	269:276	arg1	D.					303:304	D.	303:304	D.	303:304	Recently, the novel C-glycosidic linkage of a hexopyranosyl residue to the indole ring of tryptophan residue 7 of human RNase U(s) was reported [Hofsteenge, J., Müller, D. R., de Beer, T., Löffler A., Richter, W. J., & Vliegenthart, J. F. G. (1994) Biochemistry 33, 13524-13530].
7547911	1	8	dep	reported	269:276	arg1	J.					347:348	J.	347:348	J.	347:348	Recently, the novel C-glycosidic linkage of a hexopyranosyl residue to the indole ring of tryptophan residue 7 of human RNase U(s) was reported [Hofsteenge, J., Müller, D. R., de Beer, T., Löffler A., Richter, W. J., & Vliegenthart, J. F. G. (1994) Biochemistry 33, 13524-13530].
7547911	1	8	dep	reported	269:276	arg1	R.					306:307	R.	306:307	R.	306:307	Recently, the novel C-glycosidic linkage of a hexopyranosyl residue to the indole ring of tryptophan residue 7 of human RNase U(s) was reported [Hofsteenge, J., Müller, D. R., de Beer, T., Löffler A., Richter, W. J., & Vliegenthart, J. F. G. (1994) Biochemistry 33, 13524-13530].
7547911	1	8	dep	reported	269:276	arg1	G					373:373	& Vliegenthart, J. F. G	351:373	& Vliegenthart, J. F. G	351:373	Recently, the novel C-glycosidic linkage of a hexopyranosyl residue to the indole ring of tryptophan residue 7 of human RNase U(s) was reported [Hofsteenge, J., Müller, D. R., de Beer, T., Löffler A., Richter, W. J., & Vliegenthart, J. F. G. (1994) Biochemistry 33, 13524-13530].
7547911	1	8	dep	reported	269:276	arg1	A.					331:332	A.	331:332	A.	331:332	Recently, the novel C-glycosidic linkage of a hexopyranosyl residue to the indole ring of tryptophan residue 7 of human RNase U(s) was reported [Hofsteenge, J., Müller, D. R., de Beer, T., Löffler A., Richter, W. J., & Vliegenthart, J. F. G. (1994) Biochemistry 33, 13524-13530].
7547911	1	8	dep	reported	269:276	arg1	Müller					295:300	Müller	295:300	Müller	295:300	Recently, the novel C-glycosidic linkage of a hexopyranosyl residue to the indole ring of tryptophan residue 7 of human RNase U(s) was reported [Hofsteenge, J., Müller, D. R., de Beer, T., Löffler A., Richter, W. J., & Vliegenthart, J. F. G. (1994) Biochemistry 33, 13524-13530].
7547911	2	9	theme	monosaccharide	437:450	arg1	Identification					414:427	Identification	414:427	Identification of this monosaccharide	414:450	Identification of this monosaccharide is a prerequisite for studies of its biosynthesis and its biological relevance.
7547911	2	9	theme	monosaccharide	437:450	arg1	prerequisite					457:468	a prerequisite	455:468	a prerequisite for studies of its biosynthesis and its biological relevance	455:529	Identification of this monosaccharide is a prerequisite for studies of its biosynthesis and its biological relevance.
7547911	4	10	attach	derived	813:819	arg2	glycopeptide					800:811	a glycopeptide	798:811	a glycopeptide derived from RNase U(s)	798:835	Furthermore, the nuclear magnetic resonance (NMR) data indicate that the mannopyranose moiety in a glycopeptide derived from RNase U(s) adopts several conformations on the NMR time scale.
7547911	4	10	attach	derived	813:819	arg1	s					834:834	RNase U(s)	826:835	RNase U(s)	826:835	Furthermore, the nuclear magnetic resonance (NMR) data indicate that the mannopyranose moiety in a glycopeptide derived from RNase U(s) adopts several conformations on the NMR time scale.
7547911	1	11	theme	human	248:252	arg1	s					262:262	s	262:262	s	262:262	Recently, the novel C-glycosidic linkage of a hexopyranosyl residue to the indole ring of tryptophan residue 7 of human RNase U(s) was reported [Hofsteenge, J., Müller, D. R., de Beer, T., Löffler A., Richter, W. J., & Vliegenthart, J. F. G. (1994) Biochemistry 33, 13524-13530].
7547911	1	11	theme	human	248:252	arg1	U					260:260	human RNase U	248:260	human RNase U(s)	248:263	Recently, the novel C-glycosidic linkage of a hexopyranosyl residue to the indole ring of tryptophan residue 7 of human RNase U(s) was reported [Hofsteenge, J., Müller, D. R., de Beer, T., Löffler A., Richter, W. J., & Vliegenthart, J. F. G. (1994) Biochemistry 33, 13524-13530].
7547911	2	12	theme	biosynthesis	489:500	arg1	studies					474:480	studies	474:480	studies of its biosynthesis and its biological relevance	474:529	Identification of this monosaccharide is a prerequisite for studies of its biosynthesis and its biological relevance.
7547911	1	13	theme	C-glycosidic	154:165	arg1	linkage					167:173	the novel C-glycosidic linkage	144:173	the novel C-glycosidic linkage of a hexopyranosyl residue to the indole ring of tryptophan residue 7 of human RNase U(s)	144:263	Recently, the novel C-glycosidic linkage of a hexopyranosyl residue to the indole ring of tryptophan residue 7 of human RNase U(s) was reported [Hofsteenge, J., Müller, D. R., de Beer, T., Löffler A., Richter, W. J., & Vliegenthart, J. F. G. (1994) Biochemistry 33, 13524-13530].
7547911	0	14	theme	human	95:99	arg1	RNase					101:105	human RNase	95:105	human RNase	95:105	The hexopyranosyl residue that is C-glycosidically linked to the side chain of tryptophan-7 in human RNase Us is alpha-mannopyranose.
7547911	3	15	theme	rotating-frame	583:596	arg1	enhancements					617:628	rotating-frame nuclear Overhauser enhancements	583:628	rotating-frame nuclear Overhauser enhancements	583:628	Using vicinal proton-proton coupling constants and rotating-frame nuclear Overhauser enhancements, ewe demonstrate that the C-linked substituent is alpha-mannopyranose.
7547911	0	16	theme	hexopyranosyl	4:16	arg1	residue					18:24	The hexopyranosyl residue	0:24	The hexopyranosyl residue that is C-glycosidically linked to the side chain of tryptophan-7 in human RNase Us	0:108	The hexopyranosyl residue that is C-glycosidically linked to the side chain of tryptophan-7 in human RNase Us is alpha-mannopyranose.
7547911	0	16	theme	hexopyranosyl	4:16	arg1	alpha-mannopyranose					113:131	alpha-mannopyranose	113:131	alpha-mannopyranose	113:131	The hexopyranosyl residue that is C-glycosidically linked to the side chain of tryptophan-7 in human RNase Us is alpha-mannopyranose.
7547911	3	17	theme	nuclear	598:604	arg1	enhancements					617:628	rotating-frame nuclear Overhauser enhancements	583:628	rotating-frame nuclear Overhauser enhancements	583:628	Using vicinal proton-proton coupling constants and rotating-frame nuclear Overhauser enhancements, ewe demonstrate that the C-linked substituent is alpha-mannopyranose.
7547911	4	18	theme	U	832:832	arg1	s					834:834	RNase U(s)	826:835	RNase U(s)	826:835	Furthermore, the nuclear magnetic resonance (NMR) data indicate that the mannopyranose moiety in a glycopeptide derived from RNase U(s) adopts several conformations on the NMR time scale.
7547911	1	19	theme	RNase	254:258	arg1	s					262:262	s	262:262	s	262:262	Recently, the novel C-glycosidic linkage of a hexopyranosyl residue to the indole ring of tryptophan residue 7 of human RNase U(s) was reported [Hofsteenge, J., Müller, D. R., de Beer, T., Löffler A., Richter, W. J., & Vliegenthart, J. F. G. (1994) Biochemistry 33, 13524-13530].
7547911	1	19	theme	RNase	254:258	arg1	U					260:260	human RNase U	248:260	human RNase U(s)	248:263	Recently, the novel C-glycosidic linkage of a hexopyranosyl residue to the indole ring of tryptophan residue 7 of human RNase U(s) was reported [Hofsteenge, J., Müller, D. R., de Beer, T., Löffler A., Richter, W. J., & Vliegenthart, J. F. G. (1994) Biochemistry 33, 13524-13530].
7547911	0	20	attach	linked	51:56	arg1	chain					70:74	the side chain	61:74	the side chain of tryptophan-7 in human RNase	61:105	The hexopyranosyl residue that is C-glycosidically linked to the side chain of tryptophan-7 in human RNase Us is alpha-mannopyranose.
7547911	0	20	attach	linked	51:56	arg2	alpha-mannopyranose					113:131	alpha-mannopyranose	113:131	alpha-mannopyranose	113:131	The hexopyranosyl residue that is C-glycosidically linked to the side chain of tryptophan-7 in human RNase Us is alpha-mannopyranose.
7547911	0	20	attach	linked	51:56	arg2	residue					18:24	The hexopyranosyl residue	0:24	The hexopyranosyl residue that is C-glycosidically linked to the side chain of tryptophan-7 in human RNase Us	0:108	The hexopyranosyl residue that is C-glycosidically linked to the side chain of tryptophan-7 in human RNase Us is alpha-mannopyranose.
7547911	1	21	theme	U	260:260	arg1	U					260:260	human RNase U	248:260	human RNase U(s)	248:263	Recently, the novel C-glycosidic linkage of a hexopyranosyl residue to the indole ring of tryptophan residue 7 of human RNase U(s) was reported [Hofsteenge, J., Müller, D. R., de Beer, T., Löffler A., Richter, W. J., & Vliegenthart, J. F. G. (1994) Biochemistry 33, 13524-13530].
7547911	1	21	theme	U	260:260	arg1	residue					235:241	tryptophan residue 7	224:243	tryptophan residue 7 of human RNase U(s)	224:263	Recently, the novel C-glycosidic linkage of a hexopyranosyl residue to the indole ring of tryptophan residue 7 of human RNase U(s) was reported [Hofsteenge, J., Müller, D. R., de Beer, T., Löffler A., Richter, W. J., & Vliegenthart, J. F. G. (1994) Biochemistry 33, 13524-13530].
7547911	2	22	theme	relevance	521:529	arg1	studies					474:480	studies	474:480	studies of its biosynthesis and its biological relevance	474:529	Identification of this monosaccharide is a prerequisite for studies of its biosynthesis and its biological relevance.
7547911	1	23	theme	hexopyranosyl	180:192	arg1	residue					194:200	a hexopyranosyl residue	178:200	a hexopyranosyl residue	178:200	Recently, the novel C-glycosidic linkage of a hexopyranosyl residue to the indole ring of tryptophan residue 7 of human RNase U(s) was reported [Hofsteenge, J., Müller, D. R., de Beer, T., Löffler A., Richter, W. J., & Vliegenthart, J. F. G. (1994) Biochemistry 33, 13524-13530].
7547911	4	24	gly	glycopeptide	800:811	arg2	glycopeptide					800:811	a glycopeptide	798:811	a glycopeptide derived from RNase U(s)	798:835	Furthermore, the nuclear magnetic resonance (NMR) data indicate that the mannopyranose moiety in a glycopeptide derived from RNase U(s) adopts several conformations on the NMR time scale.
7547911	1	25	theme	residue	194:200	arg1	linkage					167:173	the novel C-glycosidic linkage	144:173	the novel C-glycosidic linkage of a hexopyranosyl residue to the indole ring of tryptophan residue 7 of human RNase U(s)	144:263	Recently, the novel C-glycosidic linkage of a hexopyranosyl residue to the indole ring of tryptophan residue 7 of human RNase U(s) was reported [Hofsteenge, J., Müller, D. R., de Beer, T., Löffler A., Richter, W. J., & Vliegenthart, J. F. G. (1994) Biochemistry 33, 13524-13530].
7547911	4	26	theme	time	877:880	arg1	scale					882:886	the NMR time scale	869:886	the NMR time scale	869:886	Furthermore, the nuclear magnetic resonance (NMR) data indicate that the mannopyranose moiety in a glycopeptide derived from RNase U(s) adopts several conformations on the NMR time scale.
7547911	3	27	link	C-linked	656:663	arg1	alpha-mannopyranose					680:698	alpha-mannopyranose	680:698	alpha-mannopyranose	680:698	Using vicinal proton-proton coupling constants and rotating-frame nuclear Overhauser enhancements, ewe demonstrate that the C-linked substituent is alpha-mannopyranose.
7547911	3	27	link	C-linked	656:663	arg1	substituent					665:675	the C-linked substituent	652:675	the C-linked substituent	652:675	Using vicinal proton-proton coupling constants and rotating-frame nuclear Overhauser enhancements, ewe demonstrate that the C-linked substituent is alpha-mannopyranose.
7547911	0	28	from	chain	70:74	arg1	RNase					101:105	human RNase	95:105	human RNase	95:105	The hexopyranosyl residue that is C-glycosidically linked to the side chain of tryptophan-7 in human RNase Us is alpha-mannopyranose.
7547911	4	29	theme	nuclear	718:724	arg1	NMR					746:748	NMR	746:748	NMR	746:748	Furthermore, the nuclear magnetic resonance (NMR) data indicate that the mannopyranose moiety in a glycopeptide derived from RNase U(s) adopts several conformations on the NMR time scale.
7547911	4	29	theme	nuclear	718:724	arg1	resonance					735:743	nuclear magnetic resonance	718:743	the nuclear magnetic resonance (NMR) data	714:754	Furthermore, the nuclear magnetic resonance (NMR) data indicate that the mannopyranose moiety in a glycopeptide derived from RNase U(s) adopts several conformations on the NMR time scale.
7547911	4	30	theme	NMR	873:875	arg1	scale					882:886	the NMR time scale	869:886	the NMR time scale	869:886	Furthermore, the nuclear magnetic resonance (NMR) data indicate that the mannopyranose moiety in a glycopeptide derived from RNase U(s) adopts several conformations on the NMR time scale.
7547911	1	31	dep	R.	306:307	arg1	Biochemistry					383:394	Biochemistry	383:394	Biochemistry	383:394	Recently, the novel C-glycosidic linkage of a hexopyranosyl residue to the indole ring of tryptophan residue 7 of human RNase U(s) was reported [Hofsteenge, J., Müller, D. R., de Beer, T., Löffler A., Richter, W. J., & Vliegenthart, J. F. G. (1994) Biochemistry 33, 13524-13530].
7547911	4	32	theme	RNase	826:830	arg1	s					834:834	RNase U(s)	826:835	RNase U(s)	826:835	Furthermore, the nuclear magnetic resonance (NMR) data indicate that the mannopyranose moiety in a glycopeptide derived from RNase U(s) adopts several conformations on the NMR time scale.
7547911	4	33	theme	resonance	735:743	arg1	data					751:754	the nuclear magnetic resonance (NMR) data	714:754	the nuclear magnetic resonance (NMR) data	714:754	Furthermore, the nuclear magnetic resonance (NMR) data indicate that the mannopyranose moiety in a glycopeptide derived from RNase U(s) adopts several conformations on the NMR time scale.
7547911	1	34	theme	F.	370:371	arg1	G					373:373	& Vliegenthart, J. F. G	351:373	& Vliegenthart, J. F. G	351:373	Recently, the novel C-glycosidic linkage of a hexopyranosyl residue to the indole ring of tryptophan residue 7 of human RNase U(s) was reported [Hofsteenge, J., Müller, D. R., de Beer, T., Löffler A., Richter, W. J., & Vliegenthart, J. F. G. (1994) Biochemistry 33, 13524-13530].
7547911	1	34	theme	F.	370:371	arg1	R.					306:307	R.	306:307	R.	306:307	Recently, the novel C-glycosidic linkage of a hexopyranosyl residue to the indole ring of tryptophan residue 7 of human RNase U(s) was reported [Hofsteenge, J., Müller, D. R., de Beer, T., Löffler A., Richter, W. J., & Vliegenthart, J. F. G. (1994) Biochemistry 33, 13524-13530].
7547911	4	35	theme	magnetic	726:733	arg1	NMR					746:748	NMR	746:748	NMR	746:748	Furthermore, the nuclear magnetic resonance (NMR) data indicate that the mannopyranose moiety in a glycopeptide derived from RNase U(s) adopts several conformations on the NMR time scale.
7547911	4	35	theme	magnetic	726:733	arg1	resonance					735:743	nuclear magnetic resonance	718:743	the nuclear magnetic resonance (NMR) data	714:754	Furthermore, the nuclear magnetic resonance (NMR) data indicate that the mannopyranose moiety in a glycopeptide derived from RNase U(s) adopts several conformations on the NMR time scale.
7547911	3	36	theme	C-linked	656:663	arg1	alpha-mannopyranose					680:698	alpha-mannopyranose	680:698	alpha-mannopyranose	680:698	Using vicinal proton-proton coupling constants and rotating-frame nuclear Overhauser enhancements, ewe demonstrate that the C-linked substituent is alpha-mannopyranose.
7547911	3	36	theme	C-linked	656:663	arg1	substituent					665:675	the C-linked substituent	652:675	the C-linked substituent	652:675	Using vicinal proton-proton coupling constants and rotating-frame nuclear Overhauser enhancements, ewe demonstrate that the C-linked substituent is alpha-mannopyranose.
7547911	3	37	theme	vicinal	538:544	arg1	constants					569:577	vicinal proton-proton coupling constants	538:577	vicinal proton-proton coupling constants	538:577	Using vicinal proton-proton coupling constants and rotating-frame nuclear Overhauser enhancements, ewe demonstrate that the C-linked substituent is alpha-mannopyranose.
7547911	1	38	theme	indole	209:214	arg1	ring					216:219	the indole ring	205:219	the indole ring of tryptophan residue 7 of human RNase U(s)	205:263	Recently, the novel C-glycosidic linkage of a hexopyranosyl residue to the indole ring of tryptophan residue 7 of human RNase U(s) was reported [Hofsteenge, J., Müller, D. R., de Beer, T., Löffler A., Richter, W. J., & Vliegenthart, J. F. G. (1994) Biochemistry 33, 13524-13530].
7547911	0	39	dep	residue	18:24	arg1	Us					107:108	Us	107:108	Us	107:108	The hexopyranosyl residue that is C-glycosidically linked to the side chain of tryptophan-7 in human RNase Us is alpha-mannopyranose.
7547911	0	40	theme	side	65:68	arg1	chain					70:74	the side chain	61:74	the side chain of tryptophan-7 in human RNase	61:105	The hexopyranosyl residue that is C-glycosidically linked to the side chain of tryptophan-7 in human RNase Us is alpha-mannopyranose.
7547911	4	41	from	moiety	788:793	arg1	glycopeptide					800:811	a glycopeptide	798:811	a glycopeptide derived from RNase U(s)	798:835	Furthermore, the nuclear magnetic resonance (NMR) data indicate that the mannopyranose moiety in a glycopeptide derived from RNase U(s) adopts several conformations on the NMR time scale.
7547911	4	42	from	conformations	852:864	arg1	scale					882:886	the NMR time scale	869:886	the NMR time scale	869:886	Furthermore, the nuclear magnetic resonance (NMR) data indicate that the mannopyranose moiety in a glycopeptide derived from RNase U(s) adopts several conformations on the NMR time scale.
7547911	4	43	theme	several	844:850	arg1	conformations					852:864	several conformations	844:864	several conformations on the NMR time scale	844:886	Furthermore, the nuclear magnetic resonance (NMR) data indicate that the mannopyranose moiety in a glycopeptide derived from RNase U(s) adopts several conformations on the NMR time scale.
7547911	1	44	theme	tryptophan	224:233	arg1	U					260:260	human RNase U	248:260	human RNase U(s)	248:263	Recently, the novel C-glycosidic linkage of a hexopyranosyl residue to the indole ring of tryptophan residue 7 of human RNase U(s) was reported [Hofsteenge, J., Müller, D. R., de Beer, T., Löffler A., Richter, W. J., & Vliegenthart, J. F. G. (1994) Biochemistry 33, 13524-13530].
7547911	1	44	theme	tryptophan	224:233	arg1	residue					235:241	tryptophan residue 7	224:243	tryptophan residue 7 of human RNase U(s)	224:263	Recently, the novel C-glycosidic linkage of a hexopyranosyl residue to the indole ring of tryptophan residue 7 of human RNase U(s) was reported [Hofsteenge, J., Müller, D. R., de Beer, T., Löffler A., Richter, W. J., & Vliegenthart, J. F. G. (1994) Biochemistry 33, 13524-13530].
21609021	1	0	theme	susceptible	280:290	arg1	individuals					292:302	susceptible individuals	280:302	susceptible individuals	280:302	Many autoimmune conditions are believed to result from chronic inflammation as a consequence of the interaction of genetic and environmental factors in susceptible individuals.
21609021	3	1	theme	specific	593:600	arg1	glycosylation					602:614	the antibody subclass specific glycosylation	571:614	the antibody subclass specific glycosylation in patients with myositis, their asymptomatic siblings, and healthy unrelated age- and sex-matched controls	571:722	To determine whether a similar pattern is characteristic for the autoimmune disorder myositis, we analyzed the antibody subclass specific glycosylation in patients with myositis, their asymptomatic siblings, and healthy unrelated age- and sex-matched controls.
21609021	3	2	with	controls	715:722	arg1	myositis					633:640	myositis	633:640	myositis	633:640	To determine whether a similar pattern is characteristic for the autoimmune disorder myositis, we analyzed the antibody subclass specific glycosylation in patients with myositis, their asymptomatic siblings, and healthy unrelated age- and sex-matched controls.
21609021	3	3	theme	antibody	575:582	arg1	glycosylation					602:614	the antibody subclass specific glycosylation	571:614	the antibody subclass specific glycosylation in patients with myositis, their asymptomatic siblings, and healthy unrelated age- and sex-matched controls	571:722	To determine whether a similar pattern is characteristic for the autoimmune disorder myositis, we analyzed the antibody subclass specific glycosylation in patients with myositis, their asymptomatic siblings, and healthy unrelated age- and sex-matched controls.
21609021	5	4	theme	subclasses	932:941	arg1	profiles					912:919	The glycosylation profiles	894:919	The glycosylation profiles of the IgG subclasses	894:941	The glycosylation profiles of the IgG subclasses were determined relative to the total abundance of all glycoforms.
21609021	4	5	theme	antibody	729:736	arg1	glycosylation					756:768	The antibody subclass specific glycosylation	725:768	The antibody subclass specific glycosylation	725:768	The antibody subclass specific glycosylation was determined from the LC-MS analyses of the IgG glycopeptides generated by trypsin digestion of the antibody heavy chain.
21609021	7	6	theme	myositis	1197:1204	arg1	patients					1206:1213	the myositis patients	1193:1213	the myositis patients	1193:1213	Pairwise statistical analyses reveals that galactosylation is statistically different between the myositis patients and control groups.
21609021	6	7	theme	glycoforms	1039:1048	arg1	glycoforms					1039:1048	glycoforms	1039:1048	glycoforms lacking terminal galactose in myositis patients	1039:1096	We found elevated amounts of glycoforms lacking terminal galactose in myositis patients.
21609021	6	7	theme	glycoforms	1039:1048	arg1	amounts					1028:1034	elevated amounts	1019:1034	elevated amounts of glycoforms lacking terminal galactose in myositis patients	1019:1096	We found elevated amounts of glycoforms lacking terminal galactose in myositis patients.
21609021	3	8	theme	asymptomatic	649:660	arg1	siblings					662:669	their asymptomatic siblings	643:669	their asymptomatic siblings	643:669	To determine whether a similar pattern is characteristic for the autoimmune disorder myositis, we analyzed the antibody subclass specific glycosylation in patients with myositis, their asymptomatic siblings, and healthy unrelated age- and sex-matched controls.
21609021	7	9	theme	Pairwise	1099:1106	arg1	analyses					1120:1127	Pairwise statistical analyses	1099:1127	Pairwise statistical analyses	1099:1127	Pairwise statistical analyses reveals that galactosylation is statistically different between the myositis patients and control groups.
21609021	8	10	theme	proteins	1578:1585	arg1	level					1562:1566	the level	1558:1566	the level of plasma proteins	1558:1585	Furthermore, the trend analysis for glycosylation indicates a pattern of decreasing galactosylation in the order controls ≥ siblings ≥ myositis patients, suggesting the existence of a genetic, immune-related predisposition in the group of asymptomatic siblings that can be detected before the onset of clinical symptoms at the level of plasma proteins.
21609021	4	11	theme	LC-MS	794:798	arg1	analyses					800:807	the LC-MS analyses	790:807	the LC-MS analyses of the IgG glycopeptides generated by trypsin digestion of the antibody heavy chain	790:891	The antibody subclass specific glycosylation was determined from the LC-MS analyses of the IgG glycopeptides generated by trypsin digestion of the antibody heavy chain.
21609021	3	12	theme	healthy	676:682	arg1	age-					694:697	healthy unrelated age- and sex-matched controls	676:722	age-	694:697	To determine whether a similar pattern is characteristic for the autoimmune disorder myositis, we analyzed the antibody subclass specific glycosylation in patients with myositis, their asymptomatic siblings, and healthy unrelated age- and sex-matched controls.
21609021	5	13	theme	glycoforms	998:1007	arg1	abundance					981:989	the total abundance	971:989	the total abundance of all glycoforms	971:1007	The glycosylation profiles of the IgG subclasses were determined relative to the total abundance of all glycoforms.
21609021	8	14	theme	genetic	1419:1425	arg1	predisposition					1443:1456	a genetic, immune-related predisposition	1417:1456	predisposition	1443:1456	Furthermore, the trend analysis for glycosylation indicates a pattern of decreasing galactosylation in the order controls ≥ siblings ≥ myositis patients, suggesting the existence of a genetic, immune-related predisposition in the group of asymptomatic siblings that can be detected before the onset of clinical symptoms at the level of plasma proteins.
21609021	3	15	theme	similar	487:493	arg1	pattern					495:501	a similar pattern	485:501	a similar pattern	485:501	To determine whether a similar pattern is characteristic for the autoimmune disorder myositis, we analyzed the antibody subclass specific glycosylation in patients with myositis, their asymptomatic siblings, and healthy unrelated age- and sex-matched controls.
21609021	3	15	theme	similar	487:493	arg1	characteristic					506:519	characteristic	506:519	characteristic	506:519	To determine whether a similar pattern is characteristic for the autoimmune disorder myositis, we analyzed the antibody subclass specific glycosylation in patients with myositis, their asymptomatic siblings, and healthy unrelated age- and sex-matched controls.
21609021	4	16	theme	specific	747:754	arg1	glycosylation					756:768	The antibody subclass specific glycosylation	725:768	The antibody subclass specific glycosylation	725:768	The antibody subclass specific glycosylation was determined from the LC-MS analyses of the IgG glycopeptides generated by trypsin digestion of the antibody heavy chain.
21609021	0	17	from	determination	19:31	arg1	siblings					84:91	siblings	84:91	siblings discordant for myositis syndromes	84:125	Mass spectrometric determination of IgG subclass-specific glycosylation profiles in siblings discordant for myositis syndromes.
21609021	0	18	theme	discordant	93:102	arg1	siblings					84:91	siblings	84:91	siblings discordant for myositis syndromes	84:125	Mass spectrometric determination of IgG subclass-specific glycosylation profiles in siblings discordant for myositis syndromes.
21609021	1	19	theme	chronic	183:189	arg1	inflammation					191:202	chronic inflammation	183:202	chronic inflammation	183:202	Many autoimmune conditions are believed to result from chronic inflammation as a consequence of the interaction of genetic and environmental factors in susceptible individuals.
21609021	0	20	theme	myositis	108:115	arg1	syndromes					117:125	myositis syndromes	108:125	myositis syndromes	108:125	Mass spectrometric determination of IgG subclass-specific glycosylation profiles in siblings discordant for myositis syndromes.
21609021	6	21	theme	terminal	1058:1065	arg1	galactose					1067:1075	terminal galactose	1058:1075	terminal galactose in myositis patients	1058:1096	We found elevated amounts of glycoforms lacking terminal galactose in myositis patients.
21609021	8	22	from	onset	1528:1532	arg1	level					1562:1566	the level	1558:1566	the level of plasma proteins	1558:1585	Furthermore, the trend analysis for glycosylation indicates a pattern of decreasing galactosylation in the order controls ≥ siblings ≥ myositis patients, suggesting the existence of a genetic, immune-related predisposition in the group of asymptomatic siblings that can be detected before the onset of clinical symptoms at the level of plasma proteins.
21609021	6	23	from	galactose	1067:1075	arg1	patients					1089:1096	myositis patients	1080:1096	myositis patients	1080:1096	We found elevated amounts of glycoforms lacking terminal galactose in myositis patients.
21609021	8	24	theme	asymptomatic	1474:1485	arg1	siblings					1487:1494	asymptomatic siblings	1474:1494	asymptomatic siblings that can be detected before the onset of clinical symptoms at the level of plasma proteins	1474:1585	Furthermore, the trend analysis for glycosylation indicates a pattern of decreasing galactosylation in the order controls ≥ siblings ≥ myositis patients, suggesting the existence of a genetic, immune-related predisposition in the group of asymptomatic siblings that can be detected before the onset of clinical symptoms at the level of plasma proteins.
21609021	3	25	with	siblings	662:669	arg1	myositis					633:640	myositis	633:640	myositis	633:640	To determine whether a similar pattern is characteristic for the autoimmune disorder myositis, we analyzed the antibody subclass specific glycosylation in patients with myositis, their asymptomatic siblings, and healthy unrelated age- and sex-matched controls.
21609021	2	26	theme	N-glycan	419:426	arg1	galactosylation					380:394	terminal galactosylation	371:394	terminal galactosylation of the constant region N-glycan of the total plasma immunoglobulin	371:461	One common feature in some autoimmune diseases is the decrease in terminal galactosylation of the constant region N-glycan of the total plasma immunoglobulin.
21609021	0	27	theme	Mass	0:3	arg1	determination					19:31	Mass spectrometric determination	0:31	Mass spectrometric determination of IgG subclass-specific glycosylation profiles in siblings discordant for myositis syndromes.	0:126	Mass spectrometric determination of IgG subclass-specific glycosylation profiles in siblings discordant for myositis syndromes.
21609021	8	28	dep	controls	1348:1355	arg1	siblings					1359:1366	≥ siblings	1357:1366	≥ siblings	1357:1366	Furthermore, the trend analysis for glycosylation indicates a pattern of decreasing galactosylation in the order controls ≥ siblings ≥ myositis patients, suggesting the existence of a genetic, immune-related predisposition in the group of asymptomatic siblings that can be detected before the onset of clinical symptoms at the level of plasma proteins.
21609021	4	29	theme	IgG	816:818	arg1	glycopeptides					820:832	the IgG glycopeptides	812:832	the IgG glycopeptides generated by trypsin digestion of the antibody heavy chain	812:891	The antibody subclass specific glycosylation was determined from the LC-MS analyses of the IgG glycopeptides generated by trypsin digestion of the antibody heavy chain.
21609021	1	30	theme	Many	128:131	arg1	conditions					144:153	Many autoimmune conditions	128:153	Many autoimmune conditions	128:153	Many autoimmune conditions are believed to result from chronic inflammation as a consequence of the interaction of genetic and environmental factors in susceptible individuals.
21609021	8	31	theme	immune-related	1428:1441	arg1	predisposition					1443:1456	a genetic, immune-related predisposition	1417:1456	predisposition	1443:1456	Furthermore, the trend analysis for glycosylation indicates a pattern of decreasing galactosylation in the order controls ≥ siblings ≥ myositis patients, suggesting the existence of a genetic, immune-related predisposition in the group of asymptomatic siblings that can be detected before the onset of clinical symptoms at the level of plasma proteins.
21609021	3	32	theme	sex-matched	703:713	arg1	controls					715:722	healthy unrelated age- and sex-matched controls	676:722	controls	715:722	To determine whether a similar pattern is characteristic for the autoimmune disorder myositis, we analyzed the antibody subclass specific glycosylation in patients with myositis, their asymptomatic siblings, and healthy unrelated age- and sex-matched controls.
21609021	4	33	theme	chain	887:891	arg1	digestion					855:863	trypsin digestion	847:863	trypsin digestion of the antibody heavy chain	847:891	The antibody subclass specific glycosylation was determined from the LC-MS analyses of the IgG glycopeptides generated by trypsin digestion of the antibody heavy chain.
21609021	2	34	theme	plasma	441:446	arg1	immunoglobulin					448:461	the total plasma immunoglobulin	431:461	the total plasma immunoglobulin	431:461	One common feature in some autoimmune diseases is the decrease in terminal galactosylation of the constant region N-glycan of the total plasma immunoglobulin.
21609021	0	35	theme	IgG	36:38	arg1	profiles					72:79	IgG subclass-specific glycosylation profiles	36:79	IgG subclass-specific glycosylation profiles	36:79	Mass spectrometric determination of IgG subclass-specific glycosylation profiles in siblings discordant for myositis syndromes.
21609021	2	36	theme	terminal	371:378	arg1	galactosylation					380:394	terminal galactosylation	371:394	terminal galactosylation of the constant region N-glycan of the total plasma immunoglobulin	371:461	One common feature in some autoimmune diseases is the decrease in terminal galactosylation of the constant region N-glycan of the total plasma immunoglobulin.
21609021	0	37	theme	glycosylation	58:70	arg1	profiles					72:79	IgG subclass-specific glycosylation profiles	36:79	IgG subclass-specific glycosylation profiles	36:79	Mass spectrometric determination of IgG subclass-specific glycosylation profiles in siblings discordant for myositis syndromes.
21609021	8	38	theme	clinical	1537:1544	arg1	symptoms					1546:1553	clinical symptoms	1537:1553	clinical symptoms at the level of plasma proteins	1537:1585	Furthermore, the trend analysis for glycosylation indicates a pattern of decreasing galactosylation in the order controls ≥ siblings ≥ myositis patients, suggesting the existence of a genetic, immune-related predisposition in the group of asymptomatic siblings that can be detected before the onset of clinical symptoms at the level of plasma proteins.
21609021	1	39	theme	genetic	243:249	arg1	factors					269:275	genetic and environmental factors	243:275	genetic and environmental factors	243:275	Many autoimmune conditions are believed to result from chronic inflammation as a consequence of the interaction of genetic and environmental factors in susceptible individuals.
21609021	4	40	theme	antibody	872:879	arg1	chain					887:891	the antibody heavy chain	868:891	the antibody heavy chain	868:891	The antibody subclass specific glycosylation was determined from the LC-MS analyses of the IgG glycopeptides generated by trypsin digestion of the antibody heavy chain.
21609021	2	41	theme	constant	403:410	arg1	N-glycan					419:426	the constant region N-glycan	399:426	the constant region N-glycan of the total plasma immunoglobulin	399:461	One common feature in some autoimmune diseases is the decrease in terminal galactosylation of the constant region N-glycan of the total plasma immunoglobulin.
21609021	1	42	theme	environmental	255:267	arg1	factors					269:275	genetic and environmental factors	243:275	genetic and environmental factors	243:275	Many autoimmune conditions are believed to result from chronic inflammation as a consequence of the interaction of genetic and environmental factors in susceptible individuals.
21609021	8	43	theme	trend	1252:1256	arg1	analysis					1258:1265	the trend analysis	1248:1265	the trend analysis for glycosylation	1248:1283	Furthermore, the trend analysis for glycosylation indicates a pattern of decreasing galactosylation in the order controls ≥ siblings ≥ myositis patients, suggesting the existence of a genetic, immune-related predisposition in the group of asymptomatic siblings that can be detected before the onset of clinical symptoms at the level of plasma proteins.
21609021	2	44	from	decrease	359:366	arg1	galactosylation					380:394	terminal galactosylation	371:394	terminal galactosylation of the constant region N-glycan of the total plasma immunoglobulin	371:461	One common feature in some autoimmune diseases is the decrease in terminal galactosylation of the constant region N-glycan of the total plasma immunoglobulin.
21609021	7	45	theme	control	1219:1225	arg1	groups					1227:1232	control groups	1219:1232	control groups	1219:1232	Pairwise statistical analyses reveals that galactosylation is statistically different between the myositis patients and control groups.
21609021	3	46	theme	subclass	584:591	arg1	glycosylation					602:614	the antibody subclass specific glycosylation	571:614	the antibody subclass specific glycosylation in patients with myositis, their asymptomatic siblings, and healthy unrelated age- and sex-matched controls	571:722	To determine whether a similar pattern is characteristic for the autoimmune disorder myositis, we analyzed the antibody subclass specific glycosylation in patients with myositis, their asymptomatic siblings, and healthy unrelated age- and sex-matched controls.
21609021	3	47	theme	autoimmune	529:538	arg1	myositis					549:556	the autoimmune disorder myositis	525:556	the autoimmune disorder myositis	525:556	To determine whether a similar pattern is characteristic for the autoimmune disorder myositis, we analyzed the antibody subclass specific glycosylation in patients with myositis, their asymptomatic siblings, and healthy unrelated age- and sex-matched controls.
21609021	2	48	theme	common	309:314	arg1	feature					316:322	One common feature	305:322	One common feature in some autoimmune diseases	305:350	One common feature in some autoimmune diseases is the decrease in terminal galactosylation of the constant region N-glycan of the total plasma immunoglobulin.
21609021	2	48	theme	common	309:314	arg1	decrease					359:366	the decrease	355:366	the decrease in terminal galactosylation of the constant region N-glycan of the total plasma immunoglobulin	355:461	One common feature in some autoimmune diseases is the decrease in terminal galactosylation of the constant region N-glycan of the total plasma immunoglobulin.
21609021	8	49	theme	myositis	1370:1377	arg1	patients					1379:1386	myositis patients	1370:1386	myositis patients	1370:1386	Furthermore, the trend analysis for glycosylation indicates a pattern of decreasing galactosylation in the order controls ≥ siblings ≥ myositis patients, suggesting the existence of a genetic, immune-related predisposition in the group of asymptomatic siblings that can be detected before the onset of clinical symptoms at the level of plasma proteins.
21609021	5	50	theme	IgG	928:930	arg1	subclasses					932:941	the IgG subclasses	924:941	the IgG subclasses	924:941	The glycosylation profiles of the IgG subclasses were determined relative to the total abundance of all glycoforms.
21609021	5	51	gly	glycosylation	898:910	arg1	subclasses					932:941	the IgG subclasses	924:941	the IgG subclasses	924:941	The glycosylation profiles of the IgG subclasses were determined relative to the total abundance of all glycoforms.
21609021	8	52	theme	≥	1357:1357	arg1	siblings					1359:1366	≥ siblings	1357:1366	≥ siblings	1357:1366	Furthermore, the trend analysis for glycosylation indicates a pattern of decreasing galactosylation in the order controls ≥ siblings ≥ myositis patients, suggesting the existence of a genetic, immune-related predisposition in the group of asymptomatic siblings that can be detected before the onset of clinical symptoms at the level of plasma proteins.
21609021	1	53	from	individuals	292:302	arg1	consequence					209:219	a consequence	207:219	a consequence of the interaction of genetic and environmental factors in susceptible individuals	207:302	Many autoimmune conditions are believed to result from chronic inflammation as a consequence of the interaction of genetic and environmental factors in susceptible individuals.
21609021	2	54	theme	autoimmune	332:341	arg1	diseases					343:350	some autoimmune diseases	327:350	some autoimmune diseases	327:350	One common feature in some autoimmune diseases is the decrease in terminal galactosylation of the constant region N-glycan of the total plasma immunoglobulin.
21609021	3	55	with	age-	694:697	arg1	myositis					633:640	myositis	633:640	myositis	633:640	To determine whether a similar pattern is characteristic for the autoimmune disorder myositis, we analyzed the antibody subclass specific glycosylation in patients with myositis, their asymptomatic siblings, and healthy unrelated age- and sex-matched controls.
21609021	5	56	theme	glycosylation	898:910	arg1	profiles					912:919	The glycosylation profiles	894:919	The glycosylation profiles of the IgG subclasses	894:941	The glycosylation profiles of the IgG subclasses were determined relative to the total abundance of all glycoforms.
21609021	5	57	theme	total	975:979	arg1	abundance					981:989	the total abundance	971:989	the total abundance of all glycoforms	971:1007	The glycosylation profiles of the IgG subclasses were determined relative to the total abundance of all glycoforms.
21609021	1	58	theme	interaction	228:238	arg1	consequence					209:219	a consequence	207:219	a consequence of the interaction of genetic and environmental factors in susceptible individuals	207:302	Many autoimmune conditions are believed to result from chronic inflammation as a consequence of the interaction of genetic and environmental factors in susceptible individuals.
21609021	6	59	theme	elevated	1019:1026	arg1	glycoforms					1039:1048	glycoforms	1039:1048	glycoforms lacking terminal galactose in myositis patients	1039:1096	We found elevated amounts of glycoforms lacking terminal galactose in myositis patients.
21609021	6	59	theme	elevated	1019:1026	arg1	amounts					1028:1034	elevated amounts	1019:1034	elevated amounts of glycoforms lacking terminal galactose in myositis patients	1019:1096	We found elevated amounts of glycoforms lacking terminal galactose in myositis patients.
21609021	8	60	theme	plasma	1571:1576	arg1	proteins					1578:1585	plasma proteins	1571:1585	plasma proteins	1571:1585	Furthermore, the trend analysis for glycosylation indicates a pattern of decreasing galactosylation in the order controls ≥ siblings ≥ myositis patients, suggesting the existence of a genetic, immune-related predisposition in the group of asymptomatic siblings that can be detected before the onset of clinical symptoms at the level of plasma proteins.
21609021	7	61	theme	statistical	1108:1118	arg1	analyses					1120:1127	Pairwise statistical analyses	1099:1127	Pairwise statistical analyses	1099:1127	Pairwise statistical analyses reveals that galactosylation is statistically different between the myositis patients and control groups.
21609021	1	62	theme	autoimmune	133:142	arg1	conditions					144:153	Many autoimmune conditions	128:153	Many autoimmune conditions	128:153	Many autoimmune conditions are believed to result from chronic inflammation as a consequence of the interaction of genetic and environmental factors in susceptible individuals.
21609021	8	63	theme	order	1342:1346	arg1	controls					1348:1355	the order controls ≥ siblings ≥ myositis patients	1338:1386	controls	1348:1355	Furthermore, the trend analysis for glycosylation indicates a pattern of decreasing galactosylation in the order controls ≥ siblings ≥ myositis patients, suggesting the existence of a genetic, immune-related predisposition in the group of asymptomatic siblings that can be detected before the onset of clinical symptoms at the level of plasma proteins.
21609021	3	64	from	glycosylation	602:614	arg1	patients					619:626	patients	619:626	patients with myositis	619:640	To determine whether a similar pattern is characteristic for the autoimmune disorder myositis, we analyzed the antibody subclass specific glycosylation in patients with myositis, their asymptomatic siblings, and healthy unrelated age- and sex-matched controls.
21609021	3	64	from	glycosylation	602:614	arg1	age-					694:697	healthy unrelated age- and sex-matched controls	676:722	age-	694:697	To determine whether a similar pattern is characteristic for the autoimmune disorder myositis, we analyzed the antibody subclass specific glycosylation in patients with myositis, their asymptomatic siblings, and healthy unrelated age- and sex-matched controls.
21609021	3	64	from	glycosylation	602:614	arg1	siblings					662:669	their asymptomatic siblings	643:669	their asymptomatic siblings	643:669	To determine whether a similar pattern is characteristic for the autoimmune disorder myositis, we analyzed the antibody subclass specific glycosylation in patients with myositis, their asymptomatic siblings, and healthy unrelated age- and sex-matched controls.
21609021	3	65	gly	glycosylation	602:614	arg1	patients					619:626	patients	619:626	patients with myositis	619:640	To determine whether a similar pattern is characteristic for the autoimmune disorder myositis, we analyzed the antibody subclass specific glycosylation in patients with myositis, their asymptomatic siblings, and healthy unrelated age- and sex-matched controls.
21609021	3	65	gly	glycosylation	602:614	arg1	age-					694:697	healthy unrelated age- and sex-matched controls	676:722	age-	694:697	To determine whether a similar pattern is characteristic for the autoimmune disorder myositis, we analyzed the antibody subclass specific glycosylation in patients with myositis, their asymptomatic siblings, and healthy unrelated age- and sex-matched controls.
21609021	3	65	gly	glycosylation	602:614	arg1	siblings					662:669	their asymptomatic siblings	643:669	their asymptomatic siblings	643:669	To determine whether a similar pattern is characteristic for the autoimmune disorder myositis, we analyzed the antibody subclass specific glycosylation in patients with myositis, their asymptomatic siblings, and healthy unrelated age- and sex-matched controls.
21609021	4	66	gly	glycopeptides	820:832	arg2	glycopeptides					820:832	the IgG glycopeptides	812:832	the IgG glycopeptides generated by trypsin digestion of the antibody heavy chain	812:891	The antibody subclass specific glycosylation was determined from the LC-MS analyses of the IgG glycopeptides generated by trypsin digestion of the antibody heavy chain.
21609021	1	67	from	consequence	209:219	arg1	individuals					292:302	susceptible individuals	280:302	susceptible individuals	280:302	Many autoimmune conditions are believed to result from chronic inflammation as a consequence of the interaction of genetic and environmental factors in susceptible individuals.
21609021	2	68	from	feature	316:322	arg1	diseases					343:350	some autoimmune diseases	327:350	some autoimmune diseases	327:350	One common feature in some autoimmune diseases is the decrease in terminal galactosylation of the constant region N-glycan of the total plasma immunoglobulin.
21609021	4	69	theme	subclass	738:745	arg1	glycosylation					756:768	The antibody subclass specific glycosylation	725:768	The antibody subclass specific glycosylation	725:768	The antibody subclass specific glycosylation was determined from the LC-MS analyses of the IgG glycopeptides generated by trypsin digestion of the antibody heavy chain.
21609021	8	70	from	level	1562:1566	arg1	onset					1528:1532	the onset	1524:1532	the onset of clinical symptoms at the level of plasma proteins	1524:1585	Furthermore, the trend analysis for glycosylation indicates a pattern of decreasing galactosylation in the order controls ≥ siblings ≥ myositis patients, suggesting the existence of a genetic, immune-related predisposition in the group of asymptomatic siblings that can be detected before the onset of clinical symptoms at the level of plasma proteins.
21609021	8	70	from	level	1562:1566	arg1	symptoms					1546:1553	clinical symptoms	1537:1553	clinical symptoms at the level of plasma proteins	1537:1585	Furthermore, the trend analysis for glycosylation indicates a pattern of decreasing galactosylation in the order controls ≥ siblings ≥ myositis patients, suggesting the existence of a genetic, immune-related predisposition in the group of asymptomatic siblings that can be detected before the onset of clinical symptoms at the level of plasma proteins.
21609021	6	71	theme	myositis	1080:1087	arg1	patients					1089:1096	myositis patients	1080:1096	myositis patients	1080:1096	We found elevated amounts of glycoforms lacking terminal galactose in myositis patients.
21609021	8	72	theme	predisposition	1443:1456	arg1	existence					1404:1412	the existence	1400:1412	the existence of a genetic, immune-related predisposition in the group of asymptomatic siblings that can be detected before the onset of clinical symptoms at the level of plasma proteins	1400:1585	Furthermore, the trend analysis for glycosylation indicates a pattern of decreasing galactosylation in the order controls ≥ siblings ≥ myositis patients, suggesting the existence of a genetic, immune-related predisposition in the group of asymptomatic siblings that can be detected before the onset of clinical symptoms at the level of plasma proteins.
21609021	4	73	theme	glycopeptides	820:832	arg1	analyses					800:807	the LC-MS analyses	790:807	the LC-MS analyses of the IgG glycopeptides generated by trypsin digestion of the antibody heavy chain	790:891	The antibody subclass specific glycosylation was determined from the LC-MS analyses of the IgG glycopeptides generated by trypsin digestion of the antibody heavy chain.
21609021	8	74	from	existence	1404:1412	arg1	group					1465:1469	the group	1461:1469	the group of asymptomatic siblings that can be detected before the onset of clinical symptoms at the level of plasma proteins	1461:1585	Furthermore, the trend analysis for glycosylation indicates a pattern of decreasing galactosylation in the order controls ≥ siblings ≥ myositis patients, suggesting the existence of a genetic, immune-related predisposition in the group of asymptomatic siblings that can be detected before the onset of clinical symptoms at the level of plasma proteins.
21609021	8	74	from	existence	1404:1412	arg1	siblings					1487:1494	asymptomatic siblings	1474:1494	asymptomatic siblings that can be detected before the onset of clinical symptoms at the level of plasma proteins	1474:1585	Furthermore, the trend analysis for glycosylation indicates a pattern of decreasing galactosylation in the order controls ≥ siblings ≥ myositis patients, suggesting the existence of a genetic, immune-related predisposition in the group of asymptomatic siblings that can be detected before the onset of clinical symptoms at the level of plasma proteins.
21609021	0	75	theme	spectrometric	5:17	arg1	determination					19:31	Mass spectrometric determination	0:31	Mass spectrometric determination of IgG subclass-specific glycosylation profiles in siblings discordant for myositis syndromes.	0:126	Mass spectrometric determination of IgG subclass-specific glycosylation profiles in siblings discordant for myositis syndromes.
21609021	8	76	from	predisposition	1443:1456	arg1	group					1465:1469	the group	1461:1469	the group of asymptomatic siblings that can be detected before the onset of clinical symptoms at the level of plasma proteins	1461:1585	Furthermore, the trend analysis for glycosylation indicates a pattern of decreasing galactosylation in the order controls ≥ siblings ≥ myositis patients, suggesting the existence of a genetic, immune-related predisposition in the group of asymptomatic siblings that can be detected before the onset of clinical symptoms at the level of plasma proteins.
21609021	8	76	from	predisposition	1443:1456	arg1	siblings					1487:1494	asymptomatic siblings	1474:1494	asymptomatic siblings that can be detected before the onset of clinical symptoms at the level of plasma proteins	1474:1585	Furthermore, the trend analysis for glycosylation indicates a pattern of decreasing galactosylation in the order controls ≥ siblings ≥ myositis patients, suggesting the existence of a genetic, immune-related predisposition in the group of asymptomatic siblings that can be detected before the onset of clinical symptoms at the level of plasma proteins.
21609021	8	77	theme	siblings	1487:1494	arg1	group					1465:1469	the group	1461:1469	the group of asymptomatic siblings that can be detected before the onset of clinical symptoms at the level of plasma proteins	1461:1585	Furthermore, the trend analysis for glycosylation indicates a pattern of decreasing galactosylation in the order controls ≥ siblings ≥ myositis patients, suggesting the existence of a genetic, immune-related predisposition in the group of asymptomatic siblings that can be detected before the onset of clinical symptoms at the level of plasma proteins.
21609021	8	77	theme	siblings	1487:1494	arg1	siblings					1487:1494	asymptomatic siblings	1474:1494	asymptomatic siblings that can be detected before the onset of clinical symptoms at the level of plasma proteins	1474:1585	Furthermore, the trend analysis for glycosylation indicates a pattern of decreasing galactosylation in the order controls ≥ siblings ≥ myositis patients, suggesting the existence of a genetic, immune-related predisposition in the group of asymptomatic siblings that can be detected before the onset of clinical symptoms at the level of plasma proteins.
21609021	2	78	theme	region	412:417	arg1	N-glycan					419:426	the constant region N-glycan	399:426	the constant region N-glycan of the total plasma immunoglobulin	399:461	One common feature in some autoimmune diseases is the decrease in terminal galactosylation of the constant region N-glycan of the total plasma immunoglobulin.
21609021	3	79	with	patients	619:626	arg1	myositis					633:640	myositis	633:640	myositis	633:640	To determine whether a similar pattern is characteristic for the autoimmune disorder myositis, we analyzed the antibody subclass specific glycosylation in patients with myositis, their asymptomatic siblings, and healthy unrelated age- and sex-matched controls.
21609021	4	80	theme	trypsin	847:853	arg1	digestion					855:863	trypsin digestion	847:863	trypsin digestion of the antibody heavy chain	847:891	The antibody subclass specific glycosylation was determined from the LC-MS analyses of the IgG glycopeptides generated by trypsin digestion of the antibody heavy chain.
21609021	2	81	theme	immunoglobulin	448:461	arg1	N-glycan					419:426	the constant region N-glycan	399:426	the constant region N-glycan of the total plasma immunoglobulin	399:461	One common feature in some autoimmune diseases is the decrease in terminal galactosylation of the constant region N-glycan of the total plasma immunoglobulin.
21609021	0	82	theme	subclass-specific	40:56	arg1	profiles					72:79	IgG subclass-specific glycosylation profiles	36:79	IgG subclass-specific glycosylation profiles	36:79	Mass spectrometric determination of IgG subclass-specific glycosylation profiles in siblings discordant for myositis syndromes.
21609021	3	83	theme	unrelated	684:692	arg1	age-					694:697	healthy unrelated age- and sex-matched controls	676:722	age-	694:697	To determine whether a similar pattern is characteristic for the autoimmune disorder myositis, we analyzed the antibody subclass specific glycosylation in patients with myositis, their asymptomatic siblings, and healthy unrelated age- and sex-matched controls.
21609021	4	84	theme	heavy	881:885	arg1	chain					887:891	the antibody heavy chain	868:891	the antibody heavy chain	868:891	The antibody subclass specific glycosylation was determined from the LC-MS analyses of the IgG glycopeptides generated by trypsin digestion of the antibody heavy chain.
21609021	2	85	theme	total	435:439	arg1	immunoglobulin					448:461	the total plasma immunoglobulin	431:461	the total plasma immunoglobulin	431:461	One common feature in some autoimmune diseases is the decrease in terminal galactosylation of the constant region N-glycan of the total plasma immunoglobulin.
21609021	0	86	theme	profiles	72:79	arg1	determination					19:31	Mass spectrometric determination	0:31	Mass spectrometric determination of IgG subclass-specific glycosylation profiles in siblings discordant for myositis syndromes.	0:126	Mass spectrometric determination of IgG subclass-specific glycosylation profiles in siblings discordant for myositis syndromes.
21609021	3	87	theme	disorder	540:547	arg1	myositis					549:556	the autoimmune disorder myositis	525:556	the autoimmune disorder myositis	525:556	To determine whether a similar pattern is characteristic for the autoimmune disorder myositis, we analyzed the antibody subclass specific glycosylation in patients with myositis, their asymptomatic siblings, and healthy unrelated age- and sex-matched controls.
21609021	1	88	from	interaction	228:238	arg1	individuals					292:302	susceptible individuals	280:302	susceptible individuals	280:302	Many autoimmune conditions are believed to result from chronic inflammation as a consequence of the interaction of genetic and environmental factors in susceptible individuals.
21609021	8	89	from	group	1465:1469	arg1	existence					1404:1412	the existence	1400:1412	the existence of a genetic, immune-related predisposition in the group of asymptomatic siblings that can be detected before the onset of clinical symptoms at the level of plasma proteins	1400:1585	Furthermore, the trend analysis for glycosylation indicates a pattern of decreasing galactosylation in the order controls ≥ siblings ≥ myositis patients, suggesting the existence of a genetic, immune-related predisposition in the group of asymptomatic siblings that can be detected before the onset of clinical symptoms at the level of plasma proteins.
21609021	8	90	theme	symptoms	1546:1553	arg1	onset					1528:1532	the onset	1524:1532	the onset of clinical symptoms at the level of plasma proteins	1524:1585	Furthermore, the trend analysis for glycosylation indicates a pattern of decreasing galactosylation in the order controls ≥ siblings ≥ myositis patients, suggesting the existence of a genetic, immune-related predisposition in the group of asymptomatic siblings that can be detected before the onset of clinical symptoms at the level of plasma proteins.
21609021	1	91	theme	factors	269:275	arg1	interaction					228:238	the interaction	224:238	the interaction of genetic and environmental factors in susceptible individuals	224:302	Many autoimmune conditions are believed to result from chronic inflammation as a consequence of the interaction of genetic and environmental factors in susceptible individuals.
479158	12	0	from	yields	1141:1146	arg1	present					1123:1129	present	1123:1129	present	1123:1129	Another glycopeptide unit was also found to be present, in lower yields in both variants 1 (1E) and 2 (2E).
479158	12	0	from	yields	1141:1146	arg1	variants					1156:1163	both variants 1 (1E) and 2 (2E)	1151:1181	both variants 1 (1E) and 2 (2E)	1151:1181	Another glycopeptide unit was also found to be present, in lower yields in both variants 1 (1E) and 2 (2E).
479158	9	1	theme	beta-eliminated	792:806	arg1	oligosaccharides					816:831	the beta-eliminated reduced oligosaccharides	788:831	the beta-eliminated reduced oligosaccharides	788:831	This latter structure has been established by combination of methylation data, glycosidase digestions, periodate oxidations, and Smith degradations of the beta-eliminated reduced oligosaccharides.
479158	11	2	from	residue	1031:1037	arg1	sequence					1066:1073	the Glu-plasminogen sequence	1046:1073	the Glu-plasminogen sequence	1046:1073	The threonine was found to be residue 345 in the Glu-plasminogen sequence.
479158	5	3	theme	glycopeptides	293:305	arg1	characterization					273:288	characterization	273:288	characterization	273:288	254, 8768-8771, 8772-8776) describe the isolation and characterization of glycopeptides from human plasminogen affinity chromatography variants 1 and 2.
479158	5	3	theme	glycopeptides	293:305	arg1	isolation					259:267	isolation	259:267	isolation	259:267	254, 8768-8771, 8772-8776) describe the isolation and characterization of glycopeptides from human plasminogen affinity chromatography variants 1 and 2.
479158	6	4	theme	preceding	505:513	arg1	manuscript					515:524	the immediately preceding manuscript	489:524	the immediately preceding manuscript	489:524	Plasminogen variant 1 contains an asparagine288-based branched carbohydrate structure, which has been established in the immediately preceding manuscript.
479158	5	5	dep	isolation	259:267	arg1	the					255:257	the	255:257	the	255:257	254, 8768-8771, 8772-8776) describe the isolation and characterization of glycopeptides from human plasminogen affinity chromatography variants 1 and 2.
479158	9	6	theme	reduced	808:814	arg1	oligosaccharides					816:831	the beta-eliminated reduced oligosaccharides	788:831	the beta-eliminated reduced oligosaccharides	788:831	This latter structure has been established by combination of methylation data, glycosidase digestions, periodate oxidations, and Smith degradations of the beta-eliminated reduced oligosaccharides.
479158	14	7	dep	formula	1268:1274	arg1	see					1278:1280	see	1278:1280	see text	1278:1285	: formula: (see text), alpha 2,6 Sia.
479158	10	8	theme	yields	962:967	arg1	beta					974:977	Sia alpha 2 yields 3Gal beta 1	950:979	Sia alpha 2 yields 3Gal beta 1	950:979	One glycopeptide unit, isolated from both plasminogen variants 1 (1D) and 2 (2D) possessed the following structure: Sia alpha 2 yields 3Gal beta 1 yields 3GalNAc-Thr.
479158	9	9	theme	oligosaccharides	816:831	arg1	degradations					772:783	Smith degradations	766:783	Smith degradations	766:783	This latter structure has been established by combination of methylation data, glycosidase digestions, periodate oxidations, and Smith degradations of the beta-eliminated reduced oligosaccharides.
479158	9	9	theme	oligosaccharides	816:831	arg1	data					710:713	methylation data	698:713	methylation data	698:713	This latter structure has been established by combination of methylation data, glycosidase digestions, periodate oxidations, and Smith degradations of the beta-eliminated reduced oligosaccharides.
479158	9	9	theme	oligosaccharides	816:831	arg1	digestions					728:737	glycosidase digestions	716:737	glycosidase digestions	716:737	This latter structure has been established by combination of methylation data, glycosidase digestions, periodate oxidations, and Smith degradations of the beta-eliminated reduced oligosaccharides.
479158	9	9	theme	oligosaccharides	816:831	arg1	oxidations					750:759	periodate oxidations	740:759	periodate oxidations	740:759	This latter structure has been established by combination of methylation data, glycosidase digestions, periodate oxidations, and Smith degradations of the beta-eliminated reduced oligosaccharides.
479158	5	10	theme	human	312:316	arg1	variants					354:361	human plasminogen affinity chromatography variants 1 and 2	312:369	human plasminogen affinity chromatography variants 1 and 2	312:369	254, 8768-8771, 8772-8776) describe the isolation and characterization of glycopeptides from human plasminogen affinity chromatography variants 1 and 2.
479158	16	11	theme	acid	1361:1364	arg1	NH2-Ala					1425:1431	NH2-Ala	1425:1431	NH2-Ala	1425:1431	The amino acid sequence around the glycosylated threonine was found to be NH2-Ala.
479158	16	11	theme	acid	1361:1364	arg1	sequence					1366:1373	The amino acid sequence	1351:1373	The amino acid sequence around the glycosylated threonine	1351:1407	The amino acid sequence around the glycosylated threonine was found to be NH2-Ala.
479158	10	12	dep	variants	888:895	arg1	2					908:908	2	908:908	2	908:908	One glycopeptide unit, isolated from both plasminogen variants 1 (1D) and 2 (2D) possessed the following structure: Sia alpha 2 yields 3Gal beta 1 yields 3GalNAc-Thr.
479158	10	12	dep	variants	888:895	arg1	1					897:897	1	897:897	1	897:897	One glycopeptide unit, isolated from both plasminogen variants 1 (1D) and 2 (2D) possessed the following structure: Sia alpha 2 yields 3Gal beta 1 yields 3GalNAc-Thr.
479158	10	12	dep	variants	888:895	arg1	2D					911:912	2D	911:912	2D	911:912	One glycopeptide unit, isolated from both plasminogen variants 1 (1D) and 2 (2D) possessed the following structure: Sia alpha 2 yields 3Gal beta 1 yields 3GalNAc-Thr.
479158	10	12	dep	variants	888:895	arg1	1D					900:901	1D	900:901	1D	900:901	One glycopeptide unit, isolated from both plasminogen variants 1 (1D) and 2 (2D) possessed the following structure: Sia alpha 2 yields 3Gal beta 1 yields 3GalNAc-Thr.
479158	5	13	theme	plasminogen	318:328	arg1	variants					354:361	human plasminogen affinity chromatography variants 1 and 2	312:369	human plasminogen affinity chromatography variants 1 and 2	312:369	254, 8768-8771, 8772-8776) describe the isolation and characterization of glycopeptides from human plasminogen affinity chromatography variants 1 and 2.
479158	10	14	contain	possessed	915:923	arg1	unit					851:854	One glycopeptide unit	834:854	One glycopeptide unit	834:854	One glycopeptide unit, isolated from both plasminogen variants 1 (1D) and 2 (2D) possessed the following structure: Sia alpha 2 yields 3Gal beta 1 yields 3GalNAc-Thr.
479158	10	14	contain	possessed	915:923	arg2	structure					939:947	the following structure	925:947	the following structure	925:947	One glycopeptide unit, isolated from both plasminogen variants 1 (1D) and 2 (2D) possessed the following structure: Sia alpha 2 yields 3Gal beta 1 yields 3GalNAc-Thr.
479158	12	15	from	present	1123:1129	arg1	yields					1141:1146	lower yields	1135:1146	lower yields in both variants 1 (1E) and 2 (2E)	1135:1181	Another glycopeptide unit was also found to be present, in lower yields in both variants 1 (1E) and 2 (2E).
479158	6	16	theme	Plasminogen	372:382	arg1	variant					384:390	Plasminogen variant 1	372:392	Plasminogen variant 1	372:392	Plasminogen variant 1 contains an asparagine288-based branched carbohydrate structure, which has been established in the immediately preceding manuscript.
479158	16	17	theme	amino	1355:1359	arg1	NH2-Ala					1425:1431	NH2-Ala	1425:1431	NH2-Ala	1425:1431	The amino acid sequence around the glycosylated threonine was found to be NH2-Ala.
479158	16	17	theme	amino	1355:1359	arg1	sequence					1366:1373	The amino acid sequence	1351:1373	The amino acid sequence around the glycosylated threonine	1351:1407	The amino acid sequence around the glycosylated threonine was found to be NH2-Ala.
479158	9	18	theme	methylation	698:708	arg1	data					710:713	methylation data	698:713	methylation data	698:713	This latter structure has been established by combination of methylation data, glycosidase digestions, periodate oxidations, and Smith degradations of the beta-eliminated reduced oligosaccharides.
479158	8	19	contain	contain	595:601	arg2	glycoconjugate					621:634	a threonine-based glycoconjugate	603:634	a threonine-based glycoconjugate	603:634	Plasminogen variants 1 and 2 contain a threonine-based glycoconjugate.
479158	8	19	contain	contain	595:601	arg1	variants					578:585	Plasminogen variants 1 and 2	566:593	variants	578:585	Plasminogen variants 1 and 2 contain a threonine-based glycoconjugate.
479158	8	19	contain	contain	595:601	arg1	2					593:593	2	593:593	2	593:593	Plasminogen variants 1 and 2 contain a threonine-based glycoconjugate.
479158	13	20	theme	Sia	1216:1218	arg1	alpha					1220:1224	Sia alpha 2	1216:1226	Sia alpha 2	1216:1226	The structure of this unit was: Sia alpha 2 yields 3Gal beta1 yields 3GalNAc-Thr.
479158	13	21	theme	unit	1206:1209	arg1	structure					1188:1196	The structure	1184:1196	The structure of this unit	1184:1209	The structure of this unit was: Sia alpha 2 yields 3Gal beta1 yields 3GalNAc-Thr.
479158	9	22	theme	data	710:713	arg1	combination					683:693	combination	683:693	combination of methylation data, glycosidase digestions, periodate oxidations, and Smith degradations of the beta-eliminated reduced oligosaccharides	683:831	This latter structure has been established by combination of methylation data, glycosidase digestions, periodate oxidations, and Smith degradations of the beta-eliminated reduced oligosaccharides.
479158	6	23	contain	contains	394:401	arg2	structure					448:456	an asparagine288-based branched carbohydrate structure	403:456	an asparagine288-based branched carbohydrate structure	403:456	Plasminogen variant 1 contains an asparagine288-based branched carbohydrate structure, which has been established in the immediately preceding manuscript.
479158	6	23	contain	contains	394:401	arg1	variant					384:390	Plasminogen variant 1	372:392	Plasminogen variant 1	372:392	Plasminogen variant 1 contains an asparagine288-based branched carbohydrate structure, which has been established in the immediately preceding manuscript.
479158	13	24	theme	3GalNAc-Thr	1253:1263	arg1	yields					1246:1251	3Gal beta1 yields 3GalNAc-Thr	1235:1263	3Gal beta1 yields 3GalNAc-Thr	1235:1263	The structure of this unit was: Sia alpha 2 yields 3Gal beta1 yields 3GalNAc-Thr.
479158	15	25	theme	Thr	1310:1312	arg1	345					1314:1316	Thr 345	1310:1316	Thr 345	1310:1316	Again Thr 345 was the glycosylated amino acid.
479158	15	25	theme	Thr	1310:1312	arg1	acid					1345:1348	the glycosylated amino acid	1322:1348	the glycosylated amino acid	1322:1348	Again Thr 345 was the glycosylated amino acid.
479158	5	26	gly	glycopeptides	293:305	arg2	glycopeptides					293:305	glycopeptides	293:305	glycopeptides	293:305	254, 8768-8771, 8772-8776) describe the isolation and characterization of glycopeptides from human plasminogen affinity chromatography variants 1 and 2.
479158	2	27	link	linked	87:92	arg1	unit					110:113	the O-glycosidically linked oligosaccharide unit	66:113	the O-glycosidically linked oligosaccharide unit	66:113	Structure of the O-glycosidically linked oligosaccharide unit.
479158	14	28	theme	alpha	1289:1293	arg1	formula					1268:1274	formula:	1268:1275	formula: (see text)	1268:1286	: formula: (see text), alpha 2,6 Sia.
479158	14	28	theme	alpha	1289:1293	arg1	Sia					1299:1301	alpha 2,6 Sia	1289:1301	alpha 2,6 Sia	1289:1301	: formula: (see text), alpha 2,6 Sia.
479158	5	29	dep	8768-8771	224:232	arg1	8772-8776					235:243	8772-8776	235:243	8772-8776	235:243	254, 8768-8771, 8772-8776) describe the isolation and characterization of glycopeptides from human plasminogen affinity chromatography variants 1 and 2.
479158	15	30	gly	glycosylated	1326:1337	arg1	345					1314:1316	Thr 345	1310:1316	Thr 345	1310:1316	Again Thr 345 was the glycosylated amino acid.
479158	15	30	gly	glycosylated	1326:1337	arg1	acid					1345:1348	the glycosylated amino acid	1322:1348	the glycosylated amino acid	1322:1348	Again Thr 345 was the glycosylated amino acid.
479158	9	31	theme	glycosidase	716:726	arg1	digestions					728:737	glycosidase digestions	716:737	glycosidase digestions	716:737	This latter structure has been established by combination of methylation data, glycosidase digestions, periodate oxidations, and Smith degradations of the beta-eliminated reduced oligosaccharides.
479158	3	32	dep	manuscripts	134:144	arg1	J					194:194	J	194:194	J	194:194	The preceding two manuscripts in this issue (Hayes, M. L., and Castellino, F. J. (1979) J. Biol.
479158	3	32	dep	manuscripts	134:144	arg1	1979					198:201	1979	198:201	1979	198:201	The preceding two manuscripts in this issue (Hayes, M. L., and Castellino, F. J. (1979) J. Biol.
479158	3	32	dep	manuscripts	134:144	arg1	M.					168:169	M.	168:169	M.	168:169	The preceding two manuscripts in this issue (Hayes, M. L., and Castellino, F. J. (1979) J. Biol.
479158	3	32	dep	manuscripts	134:144	arg1	F.					191:192	F.	191:192	F.	191:192	The preceding two manuscripts in this issue (Hayes, M. L., and Castellino, F. J. (1979) J. Biol.
479158	3	32	dep	manuscripts	134:144	arg1	L.					171:172	L.	171:172	L.	171:172	The preceding two manuscripts in this issue (Hayes, M. L., and Castellino, F. J. (1979) J. Biol.
479158	0	33	theme	human	20:24	arg1	variants					38:45	the human plasminogen variants	16:45	the human plasminogen variants	16:45	Carbohydrate of the human plasminogen variants.
479158	16	34	theme	glycosylated	1386:1397	arg1	threonine					1399:1407	the glycosylated threonine	1382:1407	the glycosylated threonine	1382:1407	The amino acid sequence around the glycosylated threonine was found to be NH2-Ala.
479158	12	35	gly	glycopeptide	1084:1095	arg2	glycopeptide					1084:1095	Another glycopeptide unit	1076:1100	Another glycopeptide unit	1076:1100	Another glycopeptide unit was also found to be present, in lower yields in both variants 1 (1E) and 2 (2E).
479158	9	36	theme	digestions	728:737	arg1	combination					683:693	combination	683:693	combination of methylation data, glycosidase digestions, periodate oxidations, and Smith degradations of the beta-eliminated reduced oligosaccharides	683:831	This latter structure has been established by combination of methylation data, glycosidase digestions, periodate oxidations, and Smith degradations of the beta-eliminated reduced oligosaccharides.
479158	10	37	theme	Sia	950:952	arg1	beta					974:977	Sia alpha 2 yields 3Gal beta 1	950:979	Sia alpha 2 yields 3Gal beta 1	950:979	One glycopeptide unit, isolated from both plasminogen variants 1 (1D) and 2 (2D) possessed the following structure: Sia alpha 2 yields 3Gal beta 1 yields 3GalNAc-Thr.
479158	14	38	theme	2,6	1295:1297	arg1	formula					1268:1274	formula:	1268:1275	formula: (see text)	1268:1286	: formula: (see text), alpha 2,6 Sia.
479158	14	38	theme	2,6	1295:1297	arg1	Sia					1299:1301	alpha 2,6 Sia	1289:1301	alpha 2,6 Sia	1289:1301	: formula: (see text), alpha 2,6 Sia.
479158	12	39	dep	variants	1156:1163	arg1	1					1165:1165	1	1165:1165	1	1165:1165	Another glycopeptide unit was also found to be present, in lower yields in both variants 1 (1E) and 2 (2E).
479158	12	39	dep	variants	1156:1163	arg1	2E					1179:1180	2E	1179:1180	2E	1179:1180	Another glycopeptide unit was also found to be present, in lower yields in both variants 1 (1E) and 2 (2E).
479158	12	39	dep	variants	1156:1163	arg1	1E					1168:1169	1E	1168:1169	1E	1168:1169	Another glycopeptide unit was also found to be present, in lower yields in both variants 1 (1E) and 2 (2E).
479158	12	39	dep	variants	1156:1163	arg1	2					1176:1176	2	1176:1176	2	1176:1176	Another glycopeptide unit was also found to be present, in lower yields in both variants 1 (1E) and 2 (2E).
479158	5	40	dep	variants	354:361	arg1	2					369:369	2	369:369	2	369:369	254, 8768-8771, 8772-8776) describe the isolation and characterization of glycopeptides from human plasminogen affinity chromatography variants 1 and 2.
479158	5	40	dep	variants	354:361	arg1	1					363:363	1	363:363	1	363:363	254, 8768-8771, 8772-8776) describe the isolation and characterization of glycopeptides from human plasminogen affinity chromatography variants 1 and 2.
479158	15	41	theme	glycosylated	1326:1337	arg1	345					1314:1316	Thr 345	1310:1316	Thr 345	1310:1316	Again Thr 345 was the glycosylated amino acid.
479158	15	41	theme	glycosylated	1326:1337	arg1	acid					1345:1348	the glycosylated amino acid	1322:1348	the glycosylated amino acid	1322:1348	Again Thr 345 was the glycosylated amino acid.
479158	11	42	theme	Glu-plasminogen	1050:1064	arg1	sequence					1066:1073	the Glu-plasminogen sequence	1046:1073	the Glu-plasminogen sequence	1046:1073	The threonine was found to be residue 345 in the Glu-plasminogen sequence.
479158	0	43	theme	variants	38:45	arg1	Carbohydrate					0:11	Carbohydrate	0:11	Carbohydrate of the human plasminogen variants.	0:46	Carbohydrate of the human plasminogen variants.
479158	13	44	theme	beta1	1240:1244	arg1	yields					1246:1251	3Gal beta1 yields 3GalNAc-Thr	1235:1263	3Gal beta1 yields 3GalNAc-Thr	1235:1263	The structure of this unit was: Sia alpha 2 yields 3Gal beta1 yields 3GalNAc-Thr.
479158	9	45	theme	periodate	740:748	arg1	oxidations					750:759	periodate oxidations	740:759	periodate oxidations	740:759	This latter structure has been established by combination of methylation data, glycosidase digestions, periodate oxidations, and Smith degradations of the beta-eliminated reduced oligosaccharides.
479158	10	46	theme	glycopeptide	838:849	arg1	unit					851:854	One glycopeptide unit	834:854	One glycopeptide unit	834:854	One glycopeptide unit, isolated from both plasminogen variants 1 (1D) and 2 (2D) possessed the following structure: Sia alpha 2 yields 3Gal beta 1 yields 3GalNAc-Thr.
479158	0	47	theme	plasminogen	26:36	arg1	variants					38:45	the human plasminogen variants	16:45	the human plasminogen variants	16:45	Carbohydrate of the human plasminogen variants.
479158	2	48	theme	unit	110:113	arg1	Structure					53:61	Structure	53:61	Structure of the O-glycosidically linked oligosaccharide unit	53:113	Structure of the O-glycosidically linked oligosaccharide unit.
479158	9	49	theme	oxidations	750:759	arg1	combination					683:693	combination	683:693	combination of methylation data, glycosidase digestions, periodate oxidations, and Smith degradations of the beta-eliminated reduced oligosaccharides	683:831	This latter structure has been established by combination of methylation data, glycosidase digestions, periodate oxidations, and Smith degradations of the beta-eliminated reduced oligosaccharides.
479158	13	50	theme	3Gal	1235:1238	arg1	yields					1246:1251	3Gal beta1 yields 3GalNAc-Thr	1235:1263	3Gal beta1 yields 3GalNAc-Thr	1235:1263	The structure of this unit was: Sia alpha 2 yields 3Gal beta1 yields 3GalNAc-Thr.
479158	12	51	theme	glycopeptide	1084:1095	arg1	unit					1097:1100	Another glycopeptide unit	1076:1100	Another glycopeptide unit	1076:1100	Another glycopeptide unit was also found to be present, in lower yields in both variants 1 (1E) and 2 (2E).
479158	2	52	theme	oligosaccharide	94:108	arg1	unit					110:113	the O-glycosidically linked oligosaccharide unit	66:113	the O-glycosidically linked oligosaccharide unit	66:113	Structure of the O-glycosidically linked oligosaccharide unit.
479158	5	53	from	variants	354:361	arg1	characterization					273:288	characterization	273:288	characterization	273:288	254, 8768-8771, 8772-8776) describe the isolation and characterization of glycopeptides from human plasminogen affinity chromatography variants 1 and 2.
479158	5	53	from	variants	354:361	arg1	isolation					259:267	isolation	259:267	isolation	259:267	254, 8768-8771, 8772-8776) describe the isolation and characterization of glycopeptides from human plasminogen affinity chromatography variants 1 and 2.
479158	10	54	gly	glycopeptide	838:849	arg2	glycopeptide					838:849	One glycopeptide unit	834:854	One glycopeptide unit	834:854	One glycopeptide unit, isolated from both plasminogen variants 1 (1D) and 2 (2D) possessed the following structure: Sia alpha 2 yields 3Gal beta 1 yields 3GalNAc-Thr.
479158	10	55	attach	isolated	857:864	arg2	unit					851:854	One glycopeptide unit	834:854	One glycopeptide unit	834:854	One glycopeptide unit, isolated from both plasminogen variants 1 (1D) and 2 (2D) possessed the following structure: Sia alpha 2 yields 3Gal beta 1 yields 3GalNAc-Thr.
479158	10	55	attach	isolated	857:864	arg1	variants					888:895	both plasminogen variants 1 (1D) and 2 (2D)	871:913	both plasminogen variants 1 (1D) and 2 (2D)	871:913	One glycopeptide unit, isolated from both plasminogen variants 1 (1D) and 2 (2D) possessed the following structure: Sia alpha 2 yields 3Gal beta 1 yields 3GalNAc-Thr.
479158	10	56	theme	plasminogen	876:886	arg1	variants					888:895	both plasminogen variants 1 (1D) and 2 (2D)	871:913	both plasminogen variants 1 (1D) and 2 (2D)	871:913	One glycopeptide unit, isolated from both plasminogen variants 1 (1D) and 2 (2D) possessed the following structure: Sia alpha 2 yields 3Gal beta 1 yields 3GalNAc-Thr.
479158	2	57	theme	linked	87:92	arg1	unit					110:113	the O-glycosidically linked oligosaccharide unit	66:113	the O-glycosidically linked oligosaccharide unit	66:113	Structure of the O-glycosidically linked oligosaccharide unit.
479158	6	58	theme	carbohydrate	435:446	arg1	structure					448:456	an asparagine288-based branched carbohydrate structure	403:456	an asparagine288-based branched carbohydrate structure	403:456	Plasminogen variant 1 contains an asparagine288-based branched carbohydrate structure, which has been established in the immediately preceding manuscript.
479158	10	59	theme	following	929:937	arg1	structure					939:947	the following structure	925:947	the following structure	925:947	One glycopeptide unit, isolated from both plasminogen variants 1 (1D) and 2 (2D) possessed the following structure: Sia alpha 2 yields 3Gal beta 1 yields 3GalNAc-Thr.
479158	16	60	gly	glycosylated	1386:1397	arg1	threonine					1399:1407	the glycosylated threonine	1382:1407	the glycosylated threonine	1382:1407	The amino acid sequence around the glycosylated threonine was found to be NH2-Ala.
479158	6	61	theme	branched	426:433	arg1	structure					448:456	an asparagine288-based branched carbohydrate structure	403:456	an asparagine288-based branched carbohydrate structure	403:456	Plasminogen variant 1 contains an asparagine288-based branched carbohydrate structure, which has been established in the immediately preceding manuscript.
479158	10	62	theme	3Gal	969:972	arg1	beta					974:977	Sia alpha 2 yields 3Gal beta 1	950:979	Sia alpha 2 yields 3Gal beta 1	950:979	One glycopeptide unit, isolated from both plasminogen variants 1 (1D) and 2 (2D) possessed the following structure: Sia alpha 2 yields 3Gal beta 1 yields 3GalNAc-Thr.
479158	9	63	theme	Smith	766:770	arg1	degradations					772:783	Smith degradations	766:783	Smith degradations	766:783	This latter structure has been established by combination of methylation data, glycosidase digestions, periodate oxidations, and Smith degradations of the beta-eliminated reduced oligosaccharides.
479158	9	64	theme	latter	642:647	arg1	structure					649:657	This latter structure	637:657	This latter structure	637:657	This latter structure has been established by combination of methylation data, glycosidase digestions, periodate oxidations, and Smith degradations of the beta-eliminated reduced oligosaccharides.
479158	12	65	attach	present	1123:1129	arg1	yields					1141:1146	lower yields	1135:1146	lower yields in both variants 1 (1E) and 2 (2E)	1135:1181	Another glycopeptide unit was also found to be present, in lower yields in both variants 1 (1E) and 2 (2E).
479158	12	65	attach	present	1123:1129	arg2	unit					1097:1100	Another glycopeptide unit	1076:1100	Another glycopeptide unit	1076:1100	Another glycopeptide unit was also found to be present, in lower yields in both variants 1 (1E) and 2 (2E).
479158	5	66	theme	affinity	330:337	arg1	variants					354:361	human plasminogen affinity chromatography variants 1 and 2	312:369	human plasminogen affinity chromatography variants 1 and 2	312:369	254, 8768-8771, 8772-8776) describe the isolation and characterization of glycopeptides from human plasminogen affinity chromatography variants 1 and 2.
479158	6	67	theme	asparagine288-based	406:424	arg1	structure					448:456	an asparagine288-based branched carbohydrate structure	403:456	an asparagine288-based branched carbohydrate structure	403:456	Plasminogen variant 1 contains an asparagine288-based branched carbohydrate structure, which has been established in the immediately preceding manuscript.
479158	9	68	theme	degradations	772:783	arg1	combination					683:693	combination	683:693	combination of methylation data, glycosidase digestions, periodate oxidations, and Smith degradations of the beta-eliminated reduced oligosaccharides	683:831	This latter structure has been established by combination of methylation data, glycosidase digestions, periodate oxidations, and Smith degradations of the beta-eliminated reduced oligosaccharides.
479158	7	69	from	absent	545:550	arg1	variant					555:561	variant 2	555:563	variant 2	555:563	This structure is absent in variant 2.
479158	5	70	theme	chromatography	339:352	arg1	variants					354:361	human plasminogen affinity chromatography variants 1 and 2	312:369	human plasminogen affinity chromatography variants 1 and 2	312:369	254, 8768-8771, 8772-8776) describe the isolation and characterization of glycopeptides from human plasminogen affinity chromatography variants 1 and 2.
479158	12	71	theme	lower	1135:1139	arg1	yields					1141:1146	lower yields	1135:1146	lower yields in both variants 1 (1E) and 2 (2E)	1135:1181	Another glycopeptide unit was also found to be present, in lower yields in both variants 1 (1E) and 2 (2E).
479158	8	72	theme	threonine-based	605:619	arg1	glycoconjugate					621:634	a threonine-based glycoconjugate	603:634	a threonine-based glycoconjugate	603:634	Plasminogen variants 1 and 2 contain a threonine-based glycoconjugate.
479158	8	73	theme	Plasminogen	566:576	arg1	variants					578:585	Plasminogen variants 1 and 2	566:593	variants	578:585	Plasminogen variants 1 and 2 contain a threonine-based glycoconjugate.
479158	7	74	from	variant	555:561	arg1	absent					545:550	absent	545:550	absent	545:550	This structure is absent in variant 2.
479158	10	75	theme	alpha	954:958	arg1	beta					974:977	Sia alpha 2 yields 3Gal beta 1	950:979	Sia alpha 2 yields 3Gal beta 1	950:979	One glycopeptide unit, isolated from both plasminogen variants 1 (1D) and 2 (2D) possessed the following structure: Sia alpha 2 yields 3Gal beta 1 yields 3GalNAc-Thr.
479158	15	76	theme	amino	1339:1343	arg1	345					1314:1316	Thr 345	1310:1316	Thr 345	1310:1316	Again Thr 345 was the glycosylated amino acid.
479158	15	76	theme	amino	1339:1343	arg1	acid					1345:1348	the glycosylated amino acid	1322:1348	the glycosylated amino acid	1322:1348	Again Thr 345 was the glycosylated amino acid.
479158	3	77	dep	L.	171:172	arg1	Biol					207:210	Biol	207:210	Biol	207:210	The preceding two manuscripts in this issue (Hayes, M. L., and Castellino, F. J. (1979) J. Biol.
479158	12	78	located	present	1123:1129	arg1	yields					1141:1146	lower yields	1135:1146	lower yields in both variants 1 (1E) and 2 (2E)	1135:1181	Another glycopeptide unit was also found to be present, in lower yields in both variants 1 (1E) and 2 (2E).
479158	12	78	located	present	1123:1129	arg2	unit					1097:1100	Another glycopeptide unit	1076:1100	Another glycopeptide unit	1076:1100	Another glycopeptide unit was also found to be present, in lower yields in both variants 1 (1E) and 2 (2E).
1823160	1	0	theme	tissue	284:289	arg1	mt-PA					314:318	mt-PA	314:318	mt-PA	314:318	We have employed fast atom bombardment mass spectrometry (FAB-MS) to screen the N-linked oligosaccharides of Bowes melanoma tissue plasminogen activator (mt-PA), and recombinant t-PAs produced by Chinese hamster ovary cells (rt-PA) and by a gene-enriched melanoma cell line (rmt-PA).
1823160	1	0	theme	tissue	284:289	arg1	activator					303:311	Bowes melanoma tissue plasminogen activator (mt-PA)	269:319	Bowes melanoma tissue plasminogen activator (mt-PA)	269:319	We have employed fast atom bombardment mass spectrometry (FAB-MS) to screen the N-linked oligosaccharides of Bowes melanoma tissue plasminogen activator (mt-PA), and recombinant t-PAs produced by Chinese hamster ovary cells (rt-PA) and by a gene-enriched melanoma cell line (rmt-PA).
1823160	7	1	theme	structures	1076:1085	arg1	majority					1056:1063	The majority	1052:1063	The majority of complex structures in rmt-PA	1052:1095	The majority of complex structures in rmt-PA contain N-acetyllactosamine moieties at both the Asn-184 and Asn-448 sites with the novel oligosaccharide occurring as a minor component at the Asn-184 site.
1823160	6	2	from	glycoproteins	1037:1049	arg1	moiety					1008:1013	The sialylated GalNAc moiety	986:1013	The sialylated GalNAc moiety	986:1013	The sialylated GalNAc moiety is unique in N-linked glycoproteins.
1823160	6	2	from	glycoproteins	1037:1049	arg1	unique					1018:1023	unique	1018:1023	unique	1018:1023	The sialylated GalNAc moiety is unique in N-linked glycoproteins.
1823160	1	3	theme	activator	303:311	arg1	oligosaccharides					249:264	the N-linked oligosaccharides	236:264	the N-linked oligosaccharides of Bowes melanoma tissue plasminogen activator (mt-PA), and recombinant t-PAs produced by Chinese hamster ovary cells (rt-PA) and by a gene-enriched melanoma cell line (rmt-PA)	236:441	We have employed fast atom bombardment mass spectrometry (FAB-MS) to screen the N-linked oligosaccharides of Bowes melanoma tissue plasminogen activator (mt-PA), and recombinant t-PAs produced by Chinese hamster ovary cells (rt-PA) and by a gene-enriched melanoma cell line (rmt-PA).
1823160	3	4	attach	attached	675:682	arg2	oligosaccharide					659:673	the major oligosaccharide	649:673	the major oligosaccharide attached to Asn-184 and Asn-448	649:705	In the latter glycoprotein we have identified a novel structure as the major oligosaccharide attached to Asn-184 and Asn-448.
1823160	3	4	attach	attached	675:682	arg1	Asn-184					687:693	Asn-184	687:693	Asn-184	687:693	In the latter glycoprotein we have identified a novel structure as the major oligosaccharide attached to Asn-184 and Asn-448.
1823160	3	4	attach	attached	675:682	arg1	Asn-448					699:705	Asn-448	699:705	Asn-448	699:705	In the latter glycoprotein we have identified a novel structure as the major oligosaccharide attached to Asn-184 and Asn-448.
1823160	4	5	theme	1----4	824:829	arg1	antennae					838:845	two GalNAc(1----4)GlcNAc antennae	813:845	two GalNAc(1----4)GlcNAc antennae	813:845	This is a biantennary oligosaccharide consisting of a fucosylated trimannosyl core to which are attached two GalNAc(1----4)GlcNAc antennae, one of which carries a sialic acid linked at the 6-position of the GalNAc.
1823160	4	6	theme	GlcNAc	831:836	arg1	antennae					838:845	two GalNAc(1----4)GlcNAc antennae	813:845	two GalNAc(1----4)GlcNAc antennae	813:845	This is a biantennary oligosaccharide consisting of a fucosylated trimannosyl core to which are attached two GalNAc(1----4)GlcNAc antennae, one of which carries a sialic acid linked at the 6-position of the GalNAc.
1823160	1	7	link	N-linked	240:247	arg1	oligosaccharides					249:264	the N-linked oligosaccharides	236:264	the N-linked oligosaccharides of Bowes melanoma tissue plasminogen activator (mt-PA), and recombinant t-PAs produced by Chinese hamster ovary cells (rt-PA) and by a gene-enriched melanoma cell line (rmt-PA)	236:441	We have employed fast atom bombardment mass spectrometry (FAB-MS) to screen the N-linked oligosaccharides of Bowes melanoma tissue plasminogen activator (mt-PA), and recombinant t-PAs produced by Chinese hamster ovary cells (rt-PA) and by a gene-enriched melanoma cell line (rmt-PA).
1823160	0	8	from	present	104:110	arg1	Bowes					115:119	Bowes	115:119	Bowes	115:119	A novel sialylated N-acetylgalactosamine-containing oligosaccharide is the major complex-type structure present in Bowes melanoma tissue plasminogen activator.
1823160	8	9	gly	glycoproteins	1414:1426	arg1	glycoproteins					1414:1426	natural and recombinant glycoproteins	1390:1426	natural and recombinant glycoproteins	1390:1426	This study demonstrates the power of mass spectrometric strategies based on high-field two-sector FAB-MS for structure elucidations of natural and recombinant glycoproteins.
1823160	1	10	theme	melanoma	415:422	arg1	rmt-PA					435:440	rmt-PA	435:440	rmt-PA	435:440	We have employed fast atom bombardment mass spectrometry (FAB-MS) to screen the N-linked oligosaccharides of Bowes melanoma tissue plasminogen activator (mt-PA), and recombinant t-PAs produced by Chinese hamster ovary cells (rt-PA) and by a gene-enriched melanoma cell line (rmt-PA).
1823160	1	10	theme	melanoma	415:422	arg1	line					429:432	a gene-enriched melanoma cell line	399:432	a gene-enriched melanoma cell line (rmt-PA)	399:441	We have employed fast atom bombardment mass spectrometry (FAB-MS) to screen the N-linked oligosaccharides of Bowes melanoma tissue plasminogen activator (mt-PA), and recombinant t-PAs produced by Chinese hamster ovary cells (rt-PA) and by a gene-enriched melanoma cell line (rmt-PA).
1823160	4	11	theme	sialic	871:876	arg1	acid					878:881	a sialic acid	869:881	a sialic acid linked at the 6-position of the GalNAc	869:920	This is a biantennary oligosaccharide consisting of a fucosylated trimannosyl core to which are attached two GalNAc(1----4)GlcNAc antennae, one of which carries a sialic acid linked at the 6-position of the GalNAc.
1823160	7	12	contain	contain	1097:1103	arg1	majority					1056:1063	The majority	1052:1063	The majority of complex structures in rmt-PA	1052:1095	The majority of complex structures in rmt-PA contain N-acetyllactosamine moieties at both the Asn-184 and Asn-448 sites with the novel oligosaccharide occurring as a minor component at the Asn-184 site.
1823160	7	12	contain	contain	1097:1103	arg2	majority					1056:1063	The majority	1052:1063	The majority of complex structures in rmt-PA	1052:1095	The majority of complex structures in rmt-PA contain N-acetyllactosamine moieties at both the Asn-184 and Asn-448 sites with the novel oligosaccharide occurring as a minor component at the Asn-184 site.
1823160	7	12	contain	contain	1097:1103	arg1	sites					1166:1170	both the Asn-184 and Asn-448 sites	1137:1170	sites	1166:1170	The majority of complex structures in rmt-PA contain N-acetyllactosamine moieties at both the Asn-184 and Asn-448 sites with the novel oligosaccharide occurring as a minor component at the Asn-184 site.
1823160	7	12	contain	contain	1097:1103	arg2	moieties					1125:1132	N-acetyllactosamine moieties	1105:1132	N-acetyllactosamine moieties	1105:1132	The majority of complex structures in rmt-PA contain N-acetyllactosamine moieties at both the Asn-184 and Asn-448 sites with the novel oligosaccharide occurring as a minor component at the Asn-184 site.
1823160	8	13	theme	recombinant	1402:1412	arg1	glycoproteins					1414:1426	natural and recombinant glycoproteins	1390:1426	natural and recombinant glycoproteins	1390:1426	This study demonstrates the power of mass spectrometric strategies based on high-field two-sector FAB-MS for structure elucidations of natural and recombinant glycoproteins.
1823160	0	14	from	Bowes	115:119	arg1	present					104:110	present	104:110	present	104:110	A novel sialylated N-acetylgalactosamine-containing oligosaccharide is the major complex-type structure present in Bowes melanoma tissue plasminogen activator.
1823160	0	15	theme	complex-type	81:92	arg1	structure					94:102	the major complex-type structure	71:102	the major complex-type structure present in Bowes melanoma tissue plasminogen activator	71:157	A novel sialylated N-acetylgalactosamine-containing oligosaccharide is the major complex-type structure present in Bowes melanoma tissue plasminogen activator.
1823160	0	15	theme	complex-type	81:92	arg1	oligosaccharide					52:66	A novel sialylated N-acetylgalactosamine-containing oligosaccharide	0:66	A novel sialylated N-acetylgalactosamine-containing oligosaccharide	0:66	A novel sialylated N-acetylgalactosamine-containing oligosaccharide is the major complex-type structure present in Bowes melanoma tissue plasminogen activator.
1823160	3	16	theme	latter	589:594	arg1	glycoprotein					596:607	the latter glycoprotein	585:607	the latter glycoprotein	585:607	In the latter glycoprotein we have identified a novel structure as the major oligosaccharide attached to Asn-184 and Asn-448.
1823160	1	17	theme	fast	177:180	arg1	FAB-MS					218:223	FAB-MS	218:223	FAB-MS	218:223	We have employed fast atom bombardment mass spectrometry (FAB-MS) to screen the N-linked oligosaccharides of Bowes melanoma tissue plasminogen activator (mt-PA), and recombinant t-PAs produced by Chinese hamster ovary cells (rt-PA) and by a gene-enriched melanoma cell line (rmt-PA).
1823160	1	17	theme	fast	177:180	arg1	spectrometry					204:215	fast atom bombardment mass spectrometry	177:215	fast atom bombardment mass spectrometry (FAB-MS)	177:224	We have employed fast atom bombardment mass spectrometry (FAB-MS) to screen the N-linked oligosaccharides of Bowes melanoma tissue plasminogen activator (mt-PA), and recombinant t-PAs produced by Chinese hamster ovary cells (rt-PA) and by a gene-enriched melanoma cell line (rmt-PA).
1823160	8	18	theme	spectrometric	1297:1309	arg1	strategies					1311:1320	mass spectrometric strategies	1292:1320	mass spectrometric strategies based on high-field two-sector FAB-MS for structure elucidations of natural and recombinant glycoproteins	1292:1426	This study demonstrates the power of mass spectrometric strategies based on high-field two-sector FAB-MS for structure elucidations of natural and recombinant glycoproteins.
1823160	0	19	theme	present	104:110	arg1	structure					94:102	the major complex-type structure	71:102	the major complex-type structure present in Bowes melanoma tissue plasminogen activator	71:157	A novel sialylated N-acetylgalactosamine-containing oligosaccharide is the major complex-type structure present in Bowes melanoma tissue plasminogen activator.
1823160	0	19	theme	present	104:110	arg1	oligosaccharide					52:66	A novel sialylated N-acetylgalactosamine-containing oligosaccharide	0:66	A novel sialylated N-acetylgalactosamine-containing oligosaccharide	0:66	A novel sialylated N-acetylgalactosamine-containing oligosaccharide is the major complex-type structure present in Bowes melanoma tissue plasminogen activator.
1823160	1	20	theme	hamster	364:370	arg1	rt-PA					385:389	rt-PA	385:389	rt-PA	385:389	We have employed fast atom bombardment mass spectrometry (FAB-MS) to screen the N-linked oligosaccharides of Bowes melanoma tissue plasminogen activator (mt-PA), and recombinant t-PAs produced by Chinese hamster ovary cells (rt-PA) and by a gene-enriched melanoma cell line (rmt-PA).
1823160	1	20	theme	hamster	364:370	arg1	cells					378:382	Chinese hamster ovary cells	356:382	Chinese hamster ovary cells (rt-PA)	356:390	We have employed fast atom bombardment mass spectrometry (FAB-MS) to screen the N-linked oligosaccharides of Bowes melanoma tissue plasminogen activator (mt-PA), and recombinant t-PAs produced by Chinese hamster ovary cells (rt-PA) and by a gene-enriched melanoma cell line (rmt-PA).
1823160	1	21	theme	bombardment	187:197	arg1	FAB-MS					218:223	FAB-MS	218:223	FAB-MS	218:223	We have employed fast atom bombardment mass spectrometry (FAB-MS) to screen the N-linked oligosaccharides of Bowes melanoma tissue plasminogen activator (mt-PA), and recombinant t-PAs produced by Chinese hamster ovary cells (rt-PA) and by a gene-enriched melanoma cell line (rmt-PA).
1823160	1	21	theme	bombardment	187:197	arg1	spectrometry					204:215	fast atom bombardment mass spectrometry	177:215	fast atom bombardment mass spectrometry (FAB-MS)	177:224	We have employed fast atom bombardment mass spectrometry (FAB-MS) to screen the N-linked oligosaccharides of Bowes melanoma tissue plasminogen activator (mt-PA), and recombinant t-PAs produced by Chinese hamster ovary cells (rt-PA) and by a gene-enriched melanoma cell line (rmt-PA).
1823160	5	22	theme	Minor	923:927	arg1	constituents					929:940	Minor constituents	923:940	Minor constituents	923:940	Minor constituents are sialylated on both or neither antennae.
1823160	4	23	theme	GalNAc	915:920	arg1	6-position					897:906	the 6-position	893:906	the 6-position of the GalNAc	893:920	This is a biantennary oligosaccharide consisting of a fucosylated trimannosyl core to which are attached two GalNAc(1----4)GlcNAc antennae, one of which carries a sialic acid linked at the 6-position of the GalNAc.
1823160	4	24	theme	fucosylated	762:772	arg1	core					786:789	a fucosylated trimannosyl core	760:789	a fucosylated trimannosyl core to which are attached two GalNAc(1----4)GlcNAc antennae, one of which carries a sialic acid linked at the 6-position of the GalNAc	760:920	This is a biantennary oligosaccharide consisting of a fucosylated trimannosyl core to which are attached two GalNAc(1----4)GlcNAc antennae, one of which carries a sialic acid linked at the 6-position of the GalNAc.
1823160	0	25	theme	tissue	130:135	arg1	activator					149:157	melanoma tissue plasminogen activator	121:157	Bowes melanoma tissue plasminogen activator	115:157	A novel sialylated N-acetylgalactosamine-containing oligosaccharide is the major complex-type structure present in Bowes melanoma tissue plasminogen activator.
1823160	0	26	dep	Bowes	115:119	arg1	activator					149:157	melanoma tissue plasminogen activator	121:157	Bowes melanoma tissue plasminogen activator	115:157	A novel sialylated N-acetylgalactosamine-containing oligosaccharide is the major complex-type structure present in Bowes melanoma tissue plasminogen activator.
1823160	6	27	theme	N-linked	1028:1035	arg1	glycoproteins					1037:1049	N-linked glycoproteins	1028:1049	N-linked glycoproteins	1028:1049	The sialylated GalNAc moiety is unique in N-linked glycoproteins.
1823160	8	28	theme	structure	1364:1372	arg1	elucidations					1374:1385	structure elucidations	1364:1385	structure elucidations of natural and recombinant glycoproteins	1364:1426	This study demonstrates the power of mass spectrometric strategies based on high-field two-sector FAB-MS for structure elucidations of natural and recombinant glycoproteins.
1823160	0	29	theme	sialylated	8:17	arg1	structure					94:102	the major complex-type structure	71:102	the major complex-type structure present in Bowes melanoma tissue plasminogen activator	71:157	A novel sialylated N-acetylgalactosamine-containing oligosaccharide is the major complex-type structure present in Bowes melanoma tissue plasminogen activator.
1823160	0	29	theme	sialylated	8:17	arg1	oligosaccharide					52:66	A novel sialylated N-acetylgalactosamine-containing oligosaccharide	0:66	A novel sialylated N-acetylgalactosamine-containing oligosaccharide	0:66	A novel sialylated N-acetylgalactosamine-containing oligosaccharide is the major complex-type structure present in Bowes melanoma tissue plasminogen activator.
1823160	6	30	gly	sialylated	990:999	arg1	moiety					1008:1013	The sialylated GalNAc moiety	986:1013	The sialylated GalNAc moiety	986:1013	The sialylated GalNAc moiety is unique in N-linked glycoproteins.
1823160	6	30	gly	sialylated	990:999	arg1	unique					1018:1023	unique	1018:1023	unique	1018:1023	The sialylated GalNAc moiety is unique in N-linked glycoproteins.
1823160	3	31	theme	novel	630:634	arg1	structure					636:644	a novel structure	628:644	a novel structure as the major oligosaccharide attached to Asn-184 and Asn-448	628:705	In the latter glycoprotein we have identified a novel structure as the major oligosaccharide attached to Asn-184 and Asn-448.
1823160	6	32	theme	sialylated	990:999	arg1	moiety					1008:1013	The sialylated GalNAc moiety	986:1013	The sialylated GalNAc moiety	986:1013	The sialylated GalNAc moiety is unique in N-linked glycoproteins.
1823160	6	32	theme	sialylated	990:999	arg1	unique					1018:1023	unique	1018:1023	unique	1018:1023	The sialylated GalNAc moiety is unique in N-linked glycoproteins.
1823160	7	33	from	structures	1076:1085	arg1	rmt-PA					1090:1095	rmt-PA	1090:1095	rmt-PA	1090:1095	The majority of complex structures in rmt-PA contain N-acetyllactosamine moieties at both the Asn-184 and Asn-448 sites with the novel oligosaccharide occurring as a minor component at the Asn-184 site.
1823160	4	34	theme	GalNAc	817:822	arg1	antennae					838:845	two GalNAc(1----4)GlcNAc antennae	813:845	two GalNAc(1----4)GlcNAc antennae	813:845	This is a biantennary oligosaccharide consisting of a fucosylated trimannosyl core to which are attached two GalNAc(1----4)GlcNAc antennae, one of which carries a sialic acid linked at the 6-position of the GalNAc.
1823160	7	35	theme	N-acetyllactosamine	1105:1123	arg1	moieties					1125:1132	N-acetyllactosamine moieties	1105:1132	N-acetyllactosamine moieties	1105:1132	The majority of complex structures in rmt-PA contain N-acetyllactosamine moieties at both the Asn-184 and Asn-448 sites with the novel oligosaccharide occurring as a minor component at the Asn-184 site.
1823160	1	36	theme	t-PAs	338:342	arg1	oligosaccharides					249:264	the N-linked oligosaccharides	236:264	the N-linked oligosaccharides of Bowes melanoma tissue plasminogen activator (mt-PA), and recombinant t-PAs produced by Chinese hamster ovary cells (rt-PA) and by a gene-enriched melanoma cell line (rmt-PA)	236:441	We have employed fast atom bombardment mass spectrometry (FAB-MS) to screen the N-linked oligosaccharides of Bowes melanoma tissue plasminogen activator (mt-PA), and recombinant t-PAs produced by Chinese hamster ovary cells (rt-PA) and by a gene-enriched melanoma cell line (rmt-PA).
1823160	0	37	attach	present	104:110	arg1	Bowes					115:119	Bowes	115:119	Bowes	115:119	A novel sialylated N-acetylgalactosamine-containing oligosaccharide is the major complex-type structure present in Bowes melanoma tissue plasminogen activator.
1823160	0	37	attach	present	104:110	arg2	structure					94:102	the major complex-type structure	71:102	the major complex-type structure present in Bowes melanoma tissue plasminogen activator	71:157	A novel sialylated N-acetylgalactosamine-containing oligosaccharide is the major complex-type structure present in Bowes melanoma tissue plasminogen activator.
1823160	0	37	attach	present	104:110	arg2	oligosaccharide					52:66	A novel sialylated N-acetylgalactosamine-containing oligosaccharide	0:66	A novel sialylated N-acetylgalactosamine-containing oligosaccharide	0:66	A novel sialylated N-acetylgalactosamine-containing oligosaccharide is the major complex-type structure present in Bowes melanoma tissue plasminogen activator.
1823160	7	38	from	rmt-PA	1090:1095	arg1	majority					1056:1063	The majority	1052:1063	The majority of complex structures in rmt-PA	1052:1095	The majority of complex structures in rmt-PA contain N-acetyllactosamine moieties at both the Asn-184 and Asn-448 sites with the novel oligosaccharide occurring as a minor component at the Asn-184 site.
1823160	3	39	theme	major	653:657	arg1	oligosaccharide					659:673	the major oligosaccharide	649:673	the major oligosaccharide attached to Asn-184 and Asn-448	649:705	In the latter glycoprotein we have identified a novel structure as the major oligosaccharide attached to Asn-184 and Asn-448.
1823160	8	40	theme	glycoproteins	1414:1426	arg1	elucidations					1374:1385	structure elucidations	1364:1385	structure elucidations of natural and recombinant glycoproteins	1364:1426	This study demonstrates the power of mass spectrometric strategies based on high-field two-sector FAB-MS for structure elucidations of natural and recombinant glycoproteins.
1823160	1	41	theme	N-linked	240:247	arg1	oligosaccharides					249:264	the N-linked oligosaccharides	236:264	the N-linked oligosaccharides of Bowes melanoma tissue plasminogen activator (mt-PA), and recombinant t-PAs produced by Chinese hamster ovary cells (rt-PA) and by a gene-enriched melanoma cell line (rmt-PA)	236:441	We have employed fast atom bombardment mass spectrometry (FAB-MS) to screen the N-linked oligosaccharides of Bowes melanoma tissue plasminogen activator (mt-PA), and recombinant t-PAs produced by Chinese hamster ovary cells (rt-PA) and by a gene-enriched melanoma cell line (rmt-PA).
1823160	7	42	theme	Asn-184	1241:1247	arg1	site					1249:1252	the Asn-184 site	1237:1252	the Asn-184 site	1237:1252	The majority of complex structures in rmt-PA contain N-acetyllactosamine moieties at both the Asn-184 and Asn-448 sites with the novel oligosaccharide occurring as a minor component at the Asn-184 site.
1823160	1	43	theme	melanoma	275:282	arg1	mt-PA					314:318	mt-PA	314:318	mt-PA	314:318	We have employed fast atom bombardment mass spectrometry (FAB-MS) to screen the N-linked oligosaccharides of Bowes melanoma tissue plasminogen activator (mt-PA), and recombinant t-PAs produced by Chinese hamster ovary cells (rt-PA) and by a gene-enriched melanoma cell line (rmt-PA).
1823160	1	43	theme	melanoma	275:282	arg1	activator					303:311	Bowes melanoma tissue plasminogen activator (mt-PA)	269:319	Bowes melanoma tissue plasminogen activator (mt-PA)	269:319	We have employed fast atom bombardment mass spectrometry (FAB-MS) to screen the N-linked oligosaccharides of Bowes melanoma tissue plasminogen activator (mt-PA), and recombinant t-PAs produced by Chinese hamster ovary cells (rt-PA) and by a gene-enriched melanoma cell line (rmt-PA).
1823160	4	44	theme	antennae	838:845	arg1	one					848:850	one	848:850	one	848:850	This is a biantennary oligosaccharide consisting of a fucosylated trimannosyl core to which are attached two GalNAc(1----4)GlcNAc antennae, one of which carries a sialic acid linked at the 6-position of the GalNAc.
1823160	4	44	theme	antennae	838:845	arg1	antennae					838:845	two GalNAc(1----4)GlcNAc antennae	813:845	two GalNAc(1----4)GlcNAc antennae	813:845	This is a biantennary oligosaccharide consisting of a fucosylated trimannosyl core to which are attached two GalNAc(1----4)GlcNAc antennae, one of which carries a sialic acid linked at the 6-position of the GalNAc.
1823160	7	45	theme	minor	1218:1222	arg1	component					1224:1232	a minor component	1216:1232	a minor component at the Asn-184 site	1216:1252	The majority of complex structures in rmt-PA contain N-acetyllactosamine moieties at both the Asn-184 and Asn-448 sites with the novel oligosaccharide occurring as a minor component at the Asn-184 site.
1823160	6	46	link	N-linked	1028:1035	arg1	glycoproteins					1037:1049	N-linked glycoproteins	1028:1049	N-linked glycoproteins	1028:1049	The sialylated GalNAc moiety is unique in N-linked glycoproteins.
1823160	7	47	theme	complex	1068:1074	arg1	structures					1076:1085	complex structures	1068:1085	complex structures in rmt-PA	1068:1095	The majority of complex structures in rmt-PA contain N-acetyllactosamine moieties at both the Asn-184 and Asn-448 sites with the novel oligosaccharide occurring as a minor component at the Asn-184 site.
1823160	6	48	from	unique	1018:1023	arg1	glycoproteins					1037:1049	N-linked glycoproteins	1028:1049	N-linked glycoproteins	1028:1049	The sialylated GalNAc moiety is unique in N-linked glycoproteins.
1823160	1	49	theme	plasminogen	291:301	arg1	mt-PA					314:318	mt-PA	314:318	mt-PA	314:318	We have employed fast atom bombardment mass spectrometry (FAB-MS) to screen the N-linked oligosaccharides of Bowes melanoma tissue plasminogen activator (mt-PA), and recombinant t-PAs produced by Chinese hamster ovary cells (rt-PA) and by a gene-enriched melanoma cell line (rmt-PA).
1823160	1	49	theme	plasminogen	291:301	arg1	activator					303:311	Bowes melanoma tissue plasminogen activator (mt-PA)	269:319	Bowes melanoma tissue plasminogen activator (mt-PA)	269:319	We have employed fast atom bombardment mass spectrometry (FAB-MS) to screen the N-linked oligosaccharides of Bowes melanoma tissue plasminogen activator (mt-PA), and recombinant t-PAs produced by Chinese hamster ovary cells (rt-PA) and by a gene-enriched melanoma cell line (rmt-PA).
1823160	1	50	theme	mass	199:202	arg1	FAB-MS					218:223	FAB-MS	218:223	FAB-MS	218:223	We have employed fast atom bombardment mass spectrometry (FAB-MS) to screen the N-linked oligosaccharides of Bowes melanoma tissue plasminogen activator (mt-PA), and recombinant t-PAs produced by Chinese hamster ovary cells (rt-PA) and by a gene-enriched melanoma cell line (rmt-PA).
1823160	1	50	theme	mass	199:202	arg1	spectrometry					204:215	fast atom bombardment mass spectrometry	177:215	fast atom bombardment mass spectrometry (FAB-MS)	177:224	We have employed fast atom bombardment mass spectrometry (FAB-MS) to screen the N-linked oligosaccharides of Bowes melanoma tissue plasminogen activator (mt-PA), and recombinant t-PAs produced by Chinese hamster ovary cells (rt-PA) and by a gene-enriched melanoma cell line (rmt-PA).
1823160	3	51	gly	glycoprotein	596:607	arg1	glycoprotein					596:607	the latter glycoprotein	585:607	the latter glycoprotein	585:607	In the latter glycoprotein we have identified a novel structure as the major oligosaccharide attached to Asn-184 and Asn-448.
1823160	4	52	gly	fucosylated	762:772	arg1	core					786:789	a fucosylated trimannosyl core	760:789	a fucosylated trimannosyl core to which are attached two GalNAc(1----4)GlcNAc antennae, one of which carries a sialic acid linked at the 6-position of the GalNAc	760:920	This is a biantennary oligosaccharide consisting of a fucosylated trimannosyl core to which are attached two GalNAc(1----4)GlcNAc antennae, one of which carries a sialic acid linked at the 6-position of the GalNAc.
1823160	7	53	from	site	1249:1252	arg1	component					1224:1232	a minor component	1216:1232	a minor component at the Asn-184 site	1216:1252	The majority of complex structures in rmt-PA contain N-acetyllactosamine moieties at both the Asn-184 and Asn-448 sites with the novel oligosaccharide occurring as a minor component at the Asn-184 site.
1823160	5	54	dep	or	965:966	arg1	neither					968:974	neither	968:974	neither	968:974	Minor constituents are sialylated on both or neither antennae.
1823160	7	55	with	sites	1166:1170	arg1	oligosaccharide					1187:1201	the novel oligosaccharide	1177:1201	the novel oligosaccharide occurring as a minor component at the Asn-184 site	1177:1252	The majority of complex structures in rmt-PA contain N-acetyllactosamine moieties at both the Asn-184 and Asn-448 sites with the novel oligosaccharide occurring as a minor component at the Asn-184 site.
1823160	1	56	theme	gene-enriched	401:413	arg1	rmt-PA					435:440	rmt-PA	435:440	rmt-PA	435:440	We have employed fast atom bombardment mass spectrometry (FAB-MS) to screen the N-linked oligosaccharides of Bowes melanoma tissue plasminogen activator (mt-PA), and recombinant t-PAs produced by Chinese hamster ovary cells (rt-PA) and by a gene-enriched melanoma cell line (rmt-PA).
1823160	1	56	theme	gene-enriched	401:413	arg1	line					429:432	a gene-enriched melanoma cell line	399:432	a gene-enriched melanoma cell line (rmt-PA)	399:441	We have employed fast atom bombardment mass spectrometry (FAB-MS) to screen the N-linked oligosaccharides of Bowes melanoma tissue plasminogen activator (mt-PA), and recombinant t-PAs produced by Chinese hamster ovary cells (rt-PA) and by a gene-enriched melanoma cell line (rmt-PA).
1823160	1	57	theme	cell	424:427	arg1	rmt-PA					435:440	rmt-PA	435:440	rmt-PA	435:440	We have employed fast atom bombardment mass spectrometry (FAB-MS) to screen the N-linked oligosaccharides of Bowes melanoma tissue plasminogen activator (mt-PA), and recombinant t-PAs produced by Chinese hamster ovary cells (rt-PA) and by a gene-enriched melanoma cell line (rmt-PA).
1823160	1	57	theme	cell	424:427	arg1	line					429:432	a gene-enriched melanoma cell line	399:432	a gene-enriched melanoma cell line (rmt-PA)	399:441	We have employed fast atom bombardment mass spectrometry (FAB-MS) to screen the N-linked oligosaccharides of Bowes melanoma tissue plasminogen activator (mt-PA), and recombinant t-PAs produced by Chinese hamster ovary cells (rt-PA) and by a gene-enriched melanoma cell line (rmt-PA).
1823160	7	58	theme	novel	1181:1185	arg1	oligosaccharide					1187:1201	the novel oligosaccharide	1177:1201	the novel oligosaccharide occurring as a minor component at the Asn-184 site	1177:1252	The majority of complex structures in rmt-PA contain N-acetyllactosamine moieties at both the Asn-184 and Asn-448 sites with the novel oligosaccharide occurring as a minor component at the Asn-184 site.
1823160	1	59	theme	Chinese	356:362	arg1	rt-PA					385:389	rt-PA	385:389	rt-PA	385:389	We have employed fast atom bombardment mass spectrometry (FAB-MS) to screen the N-linked oligosaccharides of Bowes melanoma tissue plasminogen activator (mt-PA), and recombinant t-PAs produced by Chinese hamster ovary cells (rt-PA) and by a gene-enriched melanoma cell line (rmt-PA).
1823160	1	59	theme	Chinese	356:362	arg1	cells					378:382	Chinese hamster ovary cells	356:382	Chinese hamster ovary cells (rt-PA)	356:390	We have employed fast atom bombardment mass spectrometry (FAB-MS) to screen the N-linked oligosaccharides of Bowes melanoma tissue plasminogen activator (mt-PA), and recombinant t-PAs produced by Chinese hamster ovary cells (rt-PA) and by a gene-enriched melanoma cell line (rmt-PA).
1823160	1	60	theme	atom	182:185	arg1	FAB-MS					218:223	FAB-MS	218:223	FAB-MS	218:223	We have employed fast atom bombardment mass spectrometry (FAB-MS) to screen the N-linked oligosaccharides of Bowes melanoma tissue plasminogen activator (mt-PA), and recombinant t-PAs produced by Chinese hamster ovary cells (rt-PA) and by a gene-enriched melanoma cell line (rmt-PA).
1823160	1	60	theme	atom	182:185	arg1	spectrometry					204:215	fast atom bombardment mass spectrometry	177:215	fast atom bombardment mass spectrometry (FAB-MS)	177:224	We have employed fast atom bombardment mass spectrometry (FAB-MS) to screen the N-linked oligosaccharides of Bowes melanoma tissue plasminogen activator (mt-PA), and recombinant t-PAs produced by Chinese hamster ovary cells (rt-PA) and by a gene-enriched melanoma cell line (rmt-PA).
1823160	2	61	theme	published	477:485	arg1	structures					487:496	the published structures	473:496	the published structures for rt-PA	473:506	These studies have confirmed the published structures for rt-PA, but are not in agreement with some of the structures reported for mt-PA.
1823160	8	62	theme	mass	1292:1295	arg1	strategies					1311:1320	mass spectrometric strategies	1292:1320	mass spectrometric strategies based on high-field two-sector FAB-MS for structure elucidations of natural and recombinant glycoproteins	1292:1426	This study demonstrates the power of mass spectrometric strategies based on high-field two-sector FAB-MS for structure elucidations of natural and recombinant glycoproteins.
1823160	0	63	theme	melanoma	121:128	arg1	activator					149:157	melanoma tissue plasminogen activator	121:157	Bowes melanoma tissue plasminogen activator	115:157	A novel sialylated N-acetylgalactosamine-containing oligosaccharide is the major complex-type structure present in Bowes melanoma tissue plasminogen activator.
1823160	1	64	theme	ovary	372:376	arg1	rt-PA					385:389	rt-PA	385:389	rt-PA	385:389	We have employed fast atom bombardment mass spectrometry (FAB-MS) to screen the N-linked oligosaccharides of Bowes melanoma tissue plasminogen activator (mt-PA), and recombinant t-PAs produced by Chinese hamster ovary cells (rt-PA) and by a gene-enriched melanoma cell line (rmt-PA).
1823160	1	64	theme	ovary	372:376	arg1	cells					378:382	Chinese hamster ovary cells	356:382	Chinese hamster ovary cells (rt-PA)	356:390	We have employed fast atom bombardment mass spectrometry (FAB-MS) to screen the N-linked oligosaccharides of Bowes melanoma tissue plasminogen activator (mt-PA), and recombinant t-PAs produced by Chinese hamster ovary cells (rt-PA) and by a gene-enriched melanoma cell line (rmt-PA).
1823160	8	65	theme	strategies	1311:1320	arg1	power					1283:1287	the power	1279:1287	the power of mass spectrometric strategies based on high-field two-sector FAB-MS for structure elucidations of natural and recombinant glycoproteins	1279:1426	This study demonstrates the power of mass spectrometric strategies based on high-field two-sector FAB-MS for structure elucidations of natural and recombinant glycoproteins.
1823160	0	66	theme	plasminogen	137:147	arg1	activator					149:157	melanoma tissue plasminogen activator	121:157	Bowes melanoma tissue plasminogen activator	115:157	A novel sialylated N-acetylgalactosamine-containing oligosaccharide is the major complex-type structure present in Bowes melanoma tissue plasminogen activator.
1823160	4	67	attach	linked	883:888	arg3	6-position					897:906	the 6-position	893:906	the 6-position of the GalNAc	893:920	This is a biantennary oligosaccharide consisting of a fucosylated trimannosyl core to which are attached two GalNAc(1----4)GlcNAc antennae, one of which carries a sialic acid linked at the 6-position of the GalNAc.
1823160	4	67	attach	linked	883:888	arg2	acid					878:881	a sialic acid	869:881	a sialic acid linked at the 6-position of the GalNAc	869:920	This is a biantennary oligosaccharide consisting of a fucosylated trimannosyl core to which are attached two GalNAc(1----4)GlcNAc antennae, one of which carries a sialic acid linked at the 6-position of the GalNAc.
1823160	7	68	theme	Asn-448	1158:1164	arg1	sites					1166:1170	both the Asn-184 and Asn-448 sites	1137:1170	sites	1166:1170	The majority of complex structures in rmt-PA contain N-acetyllactosamine moieties at both the Asn-184 and Asn-448 sites with the novel oligosaccharide occurring as a minor component at the Asn-184 site.
1823160	0	69	theme	novel	2:6	arg1	structure					94:102	the major complex-type structure	71:102	the major complex-type structure present in Bowes melanoma tissue plasminogen activator	71:157	A novel sialylated N-acetylgalactosamine-containing oligosaccharide is the major complex-type structure present in Bowes melanoma tissue plasminogen activator.
1823160	0	69	theme	novel	2:6	arg1	oligosaccharide					52:66	A novel sialylated N-acetylgalactosamine-containing oligosaccharide	0:66	A novel sialylated N-acetylgalactosamine-containing oligosaccharide	0:66	A novel sialylated N-acetylgalactosamine-containing oligosaccharide is the major complex-type structure present in Bowes melanoma tissue plasminogen activator.
1823160	4	70	contain	carries	861:867	arg1	one					848:850	one	848:850	one	848:850	This is a biantennary oligosaccharide consisting of a fucosylated trimannosyl core to which are attached two GalNAc(1----4)GlcNAc antennae, one of which carries a sialic acid linked at the 6-position of the GalNAc.
1823160	4	70	contain	carries	861:867	arg2	acid					878:881	a sialic acid	869:881	a sialic acid linked at the 6-position of the GalNAc	869:920	This is a biantennary oligosaccharide consisting of a fucosylated trimannosyl core to which are attached two GalNAc(1----4)GlcNAc antennae, one of which carries a sialic acid linked at the 6-position of the GalNAc.
1823160	4	70	contain	carries	861:867	arg1	antennae					838:845	two GalNAc(1----4)GlcNAc antennae	813:845	two GalNAc(1----4)GlcNAc antennae	813:845	This is a biantennary oligosaccharide consisting of a fucosylated trimannosyl core to which are attached two GalNAc(1----4)GlcNAc antennae, one of which carries a sialic acid linked at the 6-position of the GalNAc.
1823160	8	71	theme	two-sector	1342:1351	arg1	FAB-MS					1353:1358	high-field two-sector FAB-MS	1331:1358	high-field two-sector FAB-MS for structure elucidations of natural and recombinant glycoproteins	1331:1426	This study demonstrates the power of mass spectrometric strategies based on high-field two-sector FAB-MS for structure elucidations of natural and recombinant glycoproteins.
1823160	0	72	theme	N-acetylgalactosamine-containing	19:50	arg1	structure					94:102	the major complex-type structure	71:102	the major complex-type structure present in Bowes melanoma tissue plasminogen activator	71:157	A novel sialylated N-acetylgalactosamine-containing oligosaccharide is the major complex-type structure present in Bowes melanoma tissue plasminogen activator.
1823160	0	72	theme	N-acetylgalactosamine-containing	19:50	arg1	oligosaccharide					52:66	A novel sialylated N-acetylgalactosamine-containing oligosaccharide	0:66	A novel sialylated N-acetylgalactosamine-containing oligosaccharide	0:66	A novel sialylated N-acetylgalactosamine-containing oligosaccharide is the major complex-type structure present in Bowes melanoma tissue plasminogen activator.
1823160	7	73	from	majority	1056:1063	arg1	rmt-PA					1090:1095	rmt-PA	1090:1095	rmt-PA	1090:1095	The majority of complex structures in rmt-PA contain N-acetyllactosamine moieties at both the Asn-184 and Asn-448 sites with the novel oligosaccharide occurring as a minor component at the Asn-184 site.
1823160	8	74	theme	high-field	1331:1340	arg1	FAB-MS					1353:1358	high-field two-sector FAB-MS	1331:1358	high-field two-sector FAB-MS for structure elucidations of natural and recombinant glycoproteins	1331:1426	This study demonstrates the power of mass spectrometric strategies based on high-field two-sector FAB-MS for structure elucidations of natural and recombinant glycoproteins.
1823160	4	75	theme	biantennary	718:728	arg1	oligosaccharide					730:744	a biantennary oligosaccharide	716:744	a biantennary oligosaccharide consisting of a fucosylated trimannosyl core to which are attached two GalNAc(1----4)GlcNAc antennae, one of which carries a sialic acid linked at the 6-position of the GalNAc	716:920	This is a biantennary oligosaccharide consisting of a fucosylated trimannosyl core to which are attached two GalNAc(1----4)GlcNAc antennae, one of which carries a sialic acid linked at the 6-position of the GalNAc.
1823160	4	75	theme	biantennary	718:728	arg1	This					708:711	This	708:711	This	708:711	This is a biantennary oligosaccharide consisting of a fucosylated trimannosyl core to which are attached two GalNAc(1----4)GlcNAc antennae, one of which carries a sialic acid linked at the 6-position of the GalNAc.
1823160	6	76	theme	GalNAc	1001:1006	arg1	moiety					1008:1013	The sialylated GalNAc moiety	986:1013	The sialylated GalNAc moiety	986:1013	The sialylated GalNAc moiety is unique in N-linked glycoproteins.
1823160	6	76	theme	GalNAc	1001:1006	arg1	unique					1018:1023	unique	1018:1023	unique	1018:1023	The sialylated GalNAc moiety is unique in N-linked glycoproteins.
1823160	5	77	gly	sialylated	946:955	arg1	constituents					929:940	Minor constituents	923:940	Minor constituents	923:940	Minor constituents are sialylated on both or neither antennae.
1823160	0	78	theme	major	75:79	arg1	structure					94:102	the major complex-type structure	71:102	the major complex-type structure present in Bowes melanoma tissue plasminogen activator	71:157	A novel sialylated N-acetylgalactosamine-containing oligosaccharide is the major complex-type structure present in Bowes melanoma tissue plasminogen activator.
1823160	0	78	theme	major	75:79	arg1	oligosaccharide					52:66	A novel sialylated N-acetylgalactosamine-containing oligosaccharide	0:66	A novel sialylated N-acetylgalactosamine-containing oligosaccharide	0:66	A novel sialylated N-acetylgalactosamine-containing oligosaccharide is the major complex-type structure present in Bowes melanoma tissue plasminogen activator.
1823160	1	79	theme	recombinant	326:336	arg1	t-PAs					338:342	recombinant t-PAs	326:342	recombinant t-PAs produced by Chinese hamster ovary cells (rt-PA) and by a gene-enriched melanoma cell line (rmt-PA)	326:441	We have employed fast atom bombardment mass spectrometry (FAB-MS) to screen the N-linked oligosaccharides of Bowes melanoma tissue plasminogen activator (mt-PA), and recombinant t-PAs produced by Chinese hamster ovary cells (rt-PA) and by a gene-enriched melanoma cell line (rmt-PA).
1823160	0	80	gly	sialylated	8:17	arg1	structure					94:102	the major complex-type structure	71:102	the major complex-type structure present in Bowes melanoma tissue plasminogen activator	71:157	A novel sialylated N-acetylgalactosamine-containing oligosaccharide is the major complex-type structure present in Bowes melanoma tissue plasminogen activator.
1823160	0	80	gly	sialylated	8:17	arg1	oligosaccharide					52:66	A novel sialylated N-acetylgalactosamine-containing oligosaccharide	0:66	A novel sialylated N-acetylgalactosamine-containing oligosaccharide	0:66	A novel sialylated N-acetylgalactosamine-containing oligosaccharide is the major complex-type structure present in Bowes melanoma tissue plasminogen activator.
1823160	6	81	gly	glycoproteins	1037:1049	arg1	glycoproteins					1037:1049	N-linked glycoproteins	1028:1049	N-linked glycoproteins	1028:1049	The sialylated GalNAc moiety is unique in N-linked glycoproteins.
1823160	8	82	theme	natural	1390:1396	arg1	glycoproteins					1414:1426	natural and recombinant glycoproteins	1390:1426	natural and recombinant glycoproteins	1390:1426	This study demonstrates the power of mass spectrometric strategies based on high-field two-sector FAB-MS for structure elucidations of natural and recombinant glycoproteins.
1823160	2	83	with	agreement	524:532	arg1	some					539:542	some	539:542	some	539:542	These studies have confirmed the published structures for rt-PA, but are not in agreement with some of the structures reported for mt-PA.
1823160	2	83	with	agreement	524:532	arg1	structures					551:560	the structures	547:560	the structures reported for mt-PA	547:579	These studies have confirmed the published structures for rt-PA, but are not in agreement with some of the structures reported for mt-PA.
1823160	4	84	theme	trimannosyl	774:784	arg1	core					786:789	a fucosylated trimannosyl core	760:789	a fucosylated trimannosyl core to which are attached two GalNAc(1----4)GlcNAc antennae, one of which carries a sialic acid linked at the 6-position of the GalNAc	760:920	This is a biantennary oligosaccharide consisting of a fucosylated trimannosyl core to which are attached two GalNAc(1----4)GlcNAc antennae, one of which carries a sialic acid linked at the 6-position of the GalNAc.
1823160	7	85	theme	Asn-184	1146:1152	arg1	sites					1166:1170	both the Asn-184 and Asn-448 sites	1137:1170	sites	1166:1170	The majority of complex structures in rmt-PA contain N-acetyllactosamine moieties at both the Asn-184 and Asn-448 sites with the novel oligosaccharide occurring as a minor component at the Asn-184 site.
1823160	1	86	theme	Bowes	269:273	arg1	mt-PA					314:318	mt-PA	314:318	mt-PA	314:318	We have employed fast atom bombardment mass spectrometry (FAB-MS) to screen the N-linked oligosaccharides of Bowes melanoma tissue plasminogen activator (mt-PA), and recombinant t-PAs produced by Chinese hamster ovary cells (rt-PA) and by a gene-enriched melanoma cell line (rmt-PA).
1823160	1	86	theme	Bowes	269:273	arg1	activator					303:311	Bowes melanoma tissue plasminogen activator (mt-PA)	269:319	Bowes melanoma tissue plasminogen activator (mt-PA)	269:319	We have employed fast atom bombardment mass spectrometry (FAB-MS) to screen the N-linked oligosaccharides of Bowes melanoma tissue plasminogen activator (mt-PA), and recombinant t-PAs produced by Chinese hamster ovary cells (rt-PA) and by a gene-enriched melanoma cell line (rmt-PA).
23395175	4	0	theme	Modulating	543:552	arg1	levels					570:575	Modulating O-GlcNAcylation levels	543:575	Modulating O-GlcNAcylation levels	543:575	Modulating O-GlcNAcylation levels alter circadian period length in both mice and Drosophila; conversely, protein O-GlcNAcylation is circadianly regulated.
23395175	7	1	theme	fine-tune	1189:1197	arg1	clock					1209:1213	fine-tune circadian clock	1189:1213	fine-tune circadian clock	1189:1213	Together, these results indicate that O-GlcNAcylation serves as a metabolic sensor for clock regulation and works coordinately with phosphorylation to fine-tune circadian clock.
23395175	7	2	theme	circadian	1199:1207	arg1	clock					1209:1213	fine-tune circadian clock	1189:1213	fine-tune circadian clock	1189:1213	Together, these results indicate that O-GlcNAcylation serves as a metabolic sensor for clock regulation and works coordinately with phosphorylation to fine-tune circadian clock.
23395175	2	3	theme	GSK3β-dependent	348:362	arg1	pathways					364:371	complex GSK3β-dependent pathways	340:371	complex GSK3β-dependent pathways	340:371	We employed a circadian proteomic approach to demonstrate that circadian timing of phosphorylation is a critical factor in regulating complex GSK3β-dependent pathways and identified O-GlcNAc transferase (OGT) as a substrate of GSK3β.
23395175	4	4	theme	protein	648:654	arg1	O-GlcNAcylation					656:670	protein O-GlcNAcylation	648:670	protein O-GlcNAcylation	648:670	Modulating O-GlcNAcylation levels alter circadian period length in both mice and Drosophila; conversely, protein O-GlcNAcylation is circadianly regulated.
23395175	5	5	theme	transcriptional	801:815	arg1	activities					817:826	their transcriptional activities	795:826	their transcriptional activities	795:826	Central clock proteins, Clock and Period, are reversibly modified by O-GlcNAcylation to regulate their transcriptional activities.
23395175	6	6	theme	region	964:969	arg1	phosphorylation					940:954	phosphorylation	940:954	phosphorylation of this region	940:969	In addition, O-GlcNAcylation of a region in PER2 known to regulate human sleep phase (S662-S674) competes with phosphorylation of this region, and this interplay is at least partly mediated by glucose levels.
23395175	2	7	theme	complex	340:346	arg1	pathways					364:371	complex GSK3β-dependent pathways	340:371	complex GSK3β-dependent pathways	340:371	We employed a circadian proteomic approach to demonstrate that circadian timing of phosphorylation is a critical factor in regulating complex GSK3β-dependent pathways and identified O-GlcNAc transferase (OGT) as a substrate of GSK3β.
23395175	5	8	theme	Central	698:704	arg1	Clock					722:726	Clock	722:726	Clock	722:726	Central clock proteins, Clock and Period, are reversibly modified by O-GlcNAcylation to regulate their transcriptional activities.
23395175	5	8	theme	Central	698:704	arg1	proteins					712:719	Central clock proteins	698:719	Central clock proteins	698:719	Central clock proteins, Clock and Period, are reversibly modified by O-GlcNAcylation to regulate their transcriptional activities.
23395175	5	8	theme	Central	698:704	arg1	Period					732:737	Period	732:737	Period	732:737	Central clock proteins, Clock and Period, are reversibly modified by O-GlcNAcylation to regulate their transcriptional activities.
23395175	1	9	theme	Posttranslational	93:109	arg1	modifications					111:123	Posttranslational modifications	93:123	Posttranslational modifications	93:123	Posttranslational modifications play central roles in myriad biological pathways including circadian regulation.
23395175	0	10	theme	sensor	8:13	arg1	O-GlcNAcylation					15:29	Glucose sensor O-GlcNAcylation	0:29	Glucose sensor O-GlcNAcylation	0:29	Glucose sensor O-GlcNAcylation coordinates with phosphorylation to regulate circadian clock.
23395175	5	11	theme	clock	706:710	arg1	Clock					722:726	Clock	722:726	Clock	722:726	Central clock proteins, Clock and Period, are reversibly modified by O-GlcNAcylation to regulate their transcriptional activities.
23395175	5	11	theme	clock	706:710	arg1	proteins					712:719	Central clock proteins	698:719	Central clock proteins	698:719	Central clock proteins, Clock and Period, are reversibly modified by O-GlcNAcylation to regulate their transcriptional activities.
23395175	5	11	theme	clock	706:710	arg1	Period					732:737	Period	732:737	Period	732:737	Central clock proteins, Clock and Period, are reversibly modified by O-GlcNAcylation to regulate their transcriptional activities.
23395175	6	12	theme	region	863:868	arg1	O-GlcNAcylation					842:856	O-GlcNAcylation	842:856	O-GlcNAcylation of a region in PER2 known to regulate human sleep phase (S662-S674)	842:924	In addition, O-GlcNAcylation of a region in PER2 known to regulate human sleep phase (S662-S674) competes with phosphorylation of this region, and this interplay is at least partly mediated by glucose levels.
23395175	2	13	theme	O-GlcNAc	388:395	arg1	OGT					410:412	OGT	410:412	OGT	410:412	We employed a circadian proteomic approach to demonstrate that circadian timing of phosphorylation is a critical factor in regulating complex GSK3β-dependent pathways and identified O-GlcNAc transferase (OGT) as a substrate of GSK3β.
23395175	2	13	theme	O-GlcNAc	388:395	arg1	transferase					397:407	O-GlcNAc transferase	388:407	O-GlcNAc transferase (OGT)	388:413	We employed a circadian proteomic approach to demonstrate that circadian timing of phosphorylation is a critical factor in regulating complex GSK3β-dependent pathways and identified O-GlcNAc transferase (OGT) as a substrate of GSK3β.
23395175	2	13	theme	O-GlcNAc	388:395	arg1	substrate					420:428	a substrate	418:428	a substrate of GSK3β	418:437	We employed a circadian proteomic approach to demonstrate that circadian timing of phosphorylation is a critical factor in regulating complex GSK3β-dependent pathways and identified O-GlcNAc transferase (OGT) as a substrate of GSK3β.
23395175	0	14	theme	Glucose	0:6	arg1	O-GlcNAcylation					15:29	Glucose sensor O-GlcNAcylation	0:29	Glucose sensor O-GlcNAcylation	0:29	Glucose sensor O-GlcNAcylation coordinates with phosphorylation to regulate circadian clock.
23395175	2	15	theme	GSK3β	433:437	arg1	transferase					397:407	O-GlcNAc transferase	388:407	O-GlcNAc transferase (OGT)	388:413	We employed a circadian proteomic approach to demonstrate that circadian timing of phosphorylation is a critical factor in regulating complex GSK3β-dependent pathways and identified O-GlcNAc transferase (OGT) as a substrate of GSK3β.
23395175	2	15	theme	GSK3β	433:437	arg1	substrate					420:428	a substrate	418:428	a substrate of GSK3β	418:437	We employed a circadian proteomic approach to demonstrate that circadian timing of phosphorylation is a critical factor in regulating complex GSK3β-dependent pathways and identified O-GlcNAc transferase (OGT) as a substrate of GSK3β.
23395175	6	16	theme	glucose	1022:1028	arg1	levels					1030:1035	glucose levels	1022:1035	glucose levels	1022:1035	In addition, O-GlcNAcylation of a region in PER2 known to regulate human sleep phase (S662-S674) competes with phosphorylation of this region, and this interplay is at least partly mediated by glucose levels.
23395175	7	17	theme	clock	1125:1129	arg1	regulation					1131:1140	clock regulation	1125:1140	clock regulation	1125:1140	Together, these results indicate that O-GlcNAcylation serves as a metabolic sensor for clock regulation and works coordinately with phosphorylation to fine-tune circadian clock.
23395175	1	18	theme	central	130:136	arg1	roles					138:142	central roles	130:142	central roles	130:142	Posttranslational modifications play central roles in myriad biological pathways including circadian regulation.
23395175	2	19	theme	proteomic	230:238	arg1	approach					240:247	a circadian proteomic approach	218:247	a circadian proteomic approach to demonstrate that circadian timing of phosphorylation is a critical factor in regulating complex GSK3β-dependent pathways and identified O-GlcNAc transferase (OGT) as a substrate of GSK3β	218:437	We employed a circadian proteomic approach to demonstrate that circadian timing of phosphorylation is a critical factor in regulating complex GSK3β-dependent pathways and identified O-GlcNAc transferase (OGT) as a substrate of GSK3β.
23395175	2	20	theme	circadian	220:228	arg1	approach					240:247	a circadian proteomic approach	218:247	a circadian proteomic approach to demonstrate that circadian timing of phosphorylation is a critical factor in regulating complex GSK3β-dependent pathways and identified O-GlcNAc transferase (OGT) as a substrate of GSK3β	218:437	We employed a circadian proteomic approach to demonstrate that circadian timing of phosphorylation is a critical factor in regulating complex GSK3β-dependent pathways and identified O-GlcNAc transferase (OGT) as a substrate of GSK3β.
23395175	2	21	theme	phosphorylation	289:303	arg1	timing					279:284	circadian timing	269:284	circadian timing of phosphorylation	269:303	We employed a circadian proteomic approach to demonstrate that circadian timing of phosphorylation is a critical factor in regulating complex GSK3β-dependent pathways and identified O-GlcNAc transferase (OGT) as a substrate of GSK3β.
23395175	2	21	theme	phosphorylation	289:303	arg1	factor					319:324	a critical factor	308:324	a critical factor	308:324	We employed a circadian proteomic approach to demonstrate that circadian timing of phosphorylation is a critical factor in regulating complex GSK3β-dependent pathways and identified O-GlcNAc transferase (OGT) as a substrate of GSK3β.
23395175	4	22	theme	period	593:598	arg1	length					600:605	circadian period length	583:605	circadian period length	583:605	Modulating O-GlcNAcylation levels alter circadian period length in both mice and Drosophila; conversely, protein O-GlcNAcylation is circadianly regulated.
23395175	3	23	theme	OGT	455:457	arg1	activity					459:466	OGT activity	455:466	OGT activity	455:466	Interestingly, OGT activity is regulated by GSK3β; hence, OGT and GSK3β exhibit reciprocal regulation.
23395175	4	24	theme	circadian	583:591	arg1	length					600:605	circadian period length	583:605	circadian period length	583:605	Modulating O-GlcNAcylation levels alter circadian period length in both mice and Drosophila; conversely, protein O-GlcNAcylation is circadianly regulated.
23395175	5	25	mod	modified	755:762	arg1	Period					732:737	Period	732:737	Period	732:737	Central clock proteins, Clock and Period, are reversibly modified by O-GlcNAcylation to regulate their transcriptional activities.
23395175	5	25	mod	modified	755:762	arg1	Clock					722:726	Clock	722:726	Clock	722:726	Central clock proteins, Clock and Period, are reversibly modified by O-GlcNAcylation to regulate their transcriptional activities.
23395175	5	25	mod	modified	755:762	arg1	proteins					712:719	Central clock proteins	698:719	Central clock proteins	698:719	Central clock proteins, Clock and Period, are reversibly modified by O-GlcNAcylation to regulate their transcriptional activities.
23395175	5	25	mod	modified	755:762	arg3	O-GlcNAcylation					767:781	O-GlcNAcylation	767:781	O-GlcNAcylation	767:781	Central clock proteins, Clock and Period, are reversibly modified by O-GlcNAcylation to regulate their transcriptional activities.
23395175	7	26	theme	metabolic	1104:1112	arg1	sensor					1114:1119	a metabolic sensor	1102:1119	a metabolic sensor for clock regulation	1102:1140	Together, these results indicate that O-GlcNAcylation serves as a metabolic sensor for clock regulation and works coordinately with phosphorylation to fine-tune circadian clock.
23395175	7	26	theme	metabolic	1104:1112	arg1	O-GlcNAcylation					1076:1090	O-GlcNAcylation	1076:1090	O-GlcNAcylation	1076:1090	Together, these results indicate that O-GlcNAcylation serves as a metabolic sensor for clock regulation and works coordinately with phosphorylation to fine-tune circadian clock.
23395175	2	27	theme	circadian	269:277	arg1	timing					279:284	circadian timing	269:284	circadian timing of phosphorylation	269:303	We employed a circadian proteomic approach to demonstrate that circadian timing of phosphorylation is a critical factor in regulating complex GSK3β-dependent pathways and identified O-GlcNAc transferase (OGT) as a substrate of GSK3β.
23395175	2	27	theme	circadian	269:277	arg1	factor					319:324	a critical factor	308:324	a critical factor	308:324	We employed a circadian proteomic approach to demonstrate that circadian timing of phosphorylation is a critical factor in regulating complex GSK3β-dependent pathways and identified O-GlcNAc transferase (OGT) as a substrate of GSK3β.
23395175	1	28	theme	biological	154:163	arg1	pathways					165:172	biological pathways	154:172	biological pathways including circadian regulation	154:203	Posttranslational modifications play central roles in myriad biological pathways including circadian regulation.
23395175	1	28	theme	biological	154:163	arg1	regulation					194:203	circadian regulation	184:203	circadian regulation	184:203	Posttranslational modifications play central roles in myriad biological pathways including circadian regulation.
23395175	6	29	from	O-GlcNAcylation	842:856	arg1	PER2					873:876	PER2	873:876	PER2 known to regulate human sleep phase (S662-S674)	873:924	In addition, O-GlcNAcylation of a region in PER2 known to regulate human sleep phase (S662-S674) competes with phosphorylation of this region, and this interplay is at least partly mediated by glucose levels.
23395175	6	30	theme	sleep	902:906	arg1	phase					908:912	human sleep phase	896:912	human sleep phase (S662-S674)	896:924	In addition, O-GlcNAcylation of a region in PER2 known to regulate human sleep phase (S662-S674) competes with phosphorylation of this region, and this interplay is at least partly mediated by glucose levels.
23395175	6	30	theme	sleep	902:906	arg1	S662-S674					915:923	S662-S674	915:923	S662-S674	915:923	In addition, O-GlcNAcylation of a region in PER2 known to regulate human sleep phase (S662-S674) competes with phosphorylation of this region, and this interplay is at least partly mediated by glucose levels.
23395175	2	31	theme	critical	310:317	arg1	timing					279:284	circadian timing	269:284	circadian timing of phosphorylation	269:303	We employed a circadian proteomic approach to demonstrate that circadian timing of phosphorylation is a critical factor in regulating complex GSK3β-dependent pathways and identified O-GlcNAc transferase (OGT) as a substrate of GSK3β.
23395175	2	31	theme	critical	310:317	arg1	factor					319:324	a critical factor	308:324	a critical factor	308:324	We employed a circadian proteomic approach to demonstrate that circadian timing of phosphorylation is a critical factor in regulating complex GSK3β-dependent pathways and identified O-GlcNAc transferase (OGT) as a substrate of GSK3β.
23395175	3	32	theme	reciprocal	520:529	arg1	regulation					531:540	reciprocal regulation	520:540	reciprocal regulation	520:540	Interestingly, OGT activity is regulated by GSK3β; hence, OGT and GSK3β exhibit reciprocal regulation.
23395175	6	33	theme	human	896:900	arg1	phase					908:912	human sleep phase	896:912	human sleep phase (S662-S674)	896:924	In addition, O-GlcNAcylation of a region in PER2 known to regulate human sleep phase (S662-S674) competes with phosphorylation of this region, and this interplay is at least partly mediated by glucose levels.
23395175	6	33	theme	human	896:900	arg1	S662-S674					915:923	S662-S674	915:923	S662-S674	915:923	In addition, O-GlcNAcylation of a region in PER2 known to regulate human sleep phase (S662-S674) competes with phosphorylation of this region, and this interplay is at least partly mediated by glucose levels.
23395175	1	34	theme	circadian	184:192	arg1	regulation					194:203	circadian regulation	184:203	circadian regulation	184:203	Posttranslational modifications play central roles in myriad biological pathways including circadian regulation.
23395175	0	35	theme	circadian	76:84	arg1	clock					86:90	circadian clock	76:90	circadian clock	76:90	Glucose sensor O-GlcNAcylation coordinates with phosphorylation to regulate circadian clock.
23395175	4	36	theme	O-GlcNAcylation	554:568	arg1	levels					570:575	Modulating O-GlcNAcylation levels	543:575	Modulating O-GlcNAcylation levels	543:575	Modulating O-GlcNAcylation levels alter circadian period length in both mice and Drosophila; conversely, protein O-GlcNAcylation is circadianly regulated.
27713473	0	0	theme	nuclear	82:88	arg1	regulation					97:106	its nuclear import regulation	78:106	its nuclear import regulation	78:106	Identification of the nuclear localisation signal of O-GlcNAc transferase and its nuclear import regulation.
27713473	3	1	theme	β-galactosidase	598:612	arg1	import					573:578	the nuclear import	561:578	the nuclear import of non-diffusible β-galactosidase	561:612	Here, we characterised three amino acids (DFP; residues 451-453) as the nuclear localisation signal of OGT and demonstrated that this motif mediated the nuclear import of non-diffusible β-galactosidase.
27713473	1	2	theme	single	165:170	arg1	GlcNAc					172:177	a single GlcNAc	163:177	a single GlcNAc	163:177	Nucleocytoplasmic O-GlcNAc transferase (OGT) attaches a single GlcNAc to hydroxyl groups of serine and threonine residues.
27713473	3	3	theme	localisation	492:503	arg1	acids					447:451	three amino acids	435:451	three amino acids (DFP; residues 451-453)	435:475	Here, we characterised three amino acids (DFP; residues 451-453) as the nuclear localisation signal of OGT and demonstrated that this motif mediated the nuclear import of non-diffusible β-galactosidase.
27713473	3	3	theme	localisation	492:503	arg1	signal					505:510	the nuclear localisation signal	480:510	the nuclear localisation signal of OGT	480:517	Here, we characterised three amino acids (DFP; residues 451-453) as the nuclear localisation signal of OGT and demonstrated that this motif mediated the nuclear import of non-diffusible β-galactosidase.
27713473	3	4	dep	residues	459:466	arg1	451-453					468:474	451-453	468:474	451-453	468:474	Here, we characterised three amino acids (DFP; residues 451-453) as the nuclear localisation signal of OGT and demonstrated that this motif mediated the nuclear import of non-diffusible β-galactosidase.
27713473	0	5	theme	import	90:95	arg1	regulation					97:106	its nuclear import regulation	78:106	its nuclear import regulation	78:106	Identification of the nuclear localisation signal of O-GlcNAc transferase and its nuclear import regulation.
27713473	1	6	attach	attaches	154:161	arg1	serine					201:206	serine	201:206	serine	201:206	Nucleocytoplasmic O-GlcNAc transferase (OGT) attaches a single GlcNAc to hydroxyl groups of serine and threonine residues.
27713473	1	6	attach	attaches	154:161	arg1	groups					191:196	hydroxyl groups	182:196	hydroxyl groups of serine and threonine residues	182:229	Nucleocytoplasmic O-GlcNAc transferase (OGT) attaches a single GlcNAc to hydroxyl groups of serine and threonine residues.
27713473	1	6	attach	attaches	154:161	arg2	OGT					149:151	OGT	149:151	OGT	149:151	Nucleocytoplasmic O-GlcNAc transferase (OGT) attaches a single GlcNAc to hydroxyl groups of serine and threonine residues.
27713473	1	6	attach	attaches	154:161	arg2	transferase					136:146	Nucleocytoplasmic O-GlcNAc transferase	109:146	Nucleocytoplasmic O-GlcNAc transferase (OGT)	109:152	Nucleocytoplasmic O-GlcNAc transferase (OGT) attaches a single GlcNAc to hydroxyl groups of serine and threonine residues.
27713473	1	6	attach	attaches	154:161	arg1	threonine					212:220	threonine	212:220	threonine	212:220	Nucleocytoplasmic O-GlcNAc transferase (OGT) attaches a single GlcNAc to hydroxyl groups of serine and threonine residues.
27713473	2	7	theme	molecular	336:344	arg1	unclear					403:409	unclear	403:409	unclear	403:409	Although the cellular localisation of OGT is important to regulate a variety of cellular processes, the molecular mechanisms regulating the nuclear localisation of OGT is unclear.
27713473	2	7	theme	molecular	336:344	arg1	mechanisms					346:355	the molecular mechanisms	332:355	the molecular mechanisms regulating the nuclear localisation of OGT	332:398	Although the cellular localisation of OGT is important to regulate a variety of cellular processes, the molecular mechanisms regulating the nuclear localisation of OGT is unclear.
27713473	5	8	theme	nuclear	863:869	arg1	localisation					871:882	the nuclear localisation	859:882	the nuclear localisation of OGT	859:889	We also revealed that O-GlcNAcylation of Ser389, which resides in the tetratricopeptide repeats, plays an important role in the nuclear localisation of OGT.
27713473	3	9	theme	OGT	515:517	arg1	acids					447:451	three amino acids	435:451	three amino acids (DFP; residues 451-453)	435:475	Here, we characterised three amino acids (DFP; residues 451-453) as the nuclear localisation signal of OGT and demonstrated that this motif mediated the nuclear import of non-diffusible β-galactosidase.
27713473	3	9	theme	OGT	515:517	arg1	signal					505:510	the nuclear localisation signal	480:510	the nuclear localisation signal of OGT	480:517	Here, we characterised three amino acids (DFP; residues 451-453) as the nuclear localisation signal of OGT and demonstrated that this motif mediated the nuclear import of non-diffusible β-galactosidase.
27713473	2	10	theme	OGT	396:398	arg1	localisation					380:391	the nuclear localisation	368:391	the nuclear localisation of OGT	368:398	Although the cellular localisation of OGT is important to regulate a variety of cellular processes, the molecular mechanisms regulating the nuclear localisation of OGT is unclear.
27713473	5	11	theme	Ser389	776:781	arg1	O-GlcNAcylation					757:771	O-GlcNAcylation	757:771	O-GlcNAcylation	757:771	We also revealed that O-GlcNAcylation of Ser389, which resides in the tetratricopeptide repeats, plays an important role in the nuclear localisation of OGT.
27713473	2	12	theme	cellular	312:319	arg1	processes					321:329	cellular processes	312:329	cellular processes	312:329	Although the cellular localisation of OGT is important to regulate a variety of cellular processes, the molecular mechanisms regulating the nuclear localisation of OGT is unclear.
27713473	1	13	theme	hydroxyl	182:189	arg1	serine					201:206	serine	201:206	serine	201:206	Nucleocytoplasmic O-GlcNAc transferase (OGT) attaches a single GlcNAc to hydroxyl groups of serine and threonine residues.
27713473	1	13	theme	hydroxyl	182:189	arg1	groups					191:196	hydroxyl groups	182:196	hydroxyl groups of serine and threonine residues	182:229	Nucleocytoplasmic O-GlcNAc transferase (OGT) attaches a single GlcNAc to hydroxyl groups of serine and threonine residues.
27713473	1	13	theme	hydroxyl	182:189	arg1	threonine					212:220	threonine	212:220	threonine	212:220	Nucleocytoplasmic O-GlcNAc transferase (OGT) attaches a single GlcNAc to hydroxyl groups of serine and threonine residues.
27713473	4	14	theme	OGT	707:709	arg1	motif					698:702	the DFP motif	690:702	the DFP motif of OGT	690:709	OGT bound the importin α5 protein, and this association was abolished when the DFP motif of OGT was mutated or deleted.
27713473	5	15	theme	important	841:849	arg1	role					851:854	an important role	838:854	an important role	838:854	We also revealed that O-GlcNAcylation of Ser389, which resides in the tetratricopeptide repeats, plays an important role in the nuclear localisation of OGT.
27713473	0	16	theme	nuclear	22:28	arg1	signal					43:48	the nuclear localisation signal	18:48	the nuclear localisation signal of O-GlcNAc transferase	18:72	Identification of the nuclear localisation signal of O-GlcNAc transferase and its nuclear import regulation.
27713473	3	17	dep	DFP	454:456	arg1	residues					459:466	residues 451-453	459:474	residues 451-453	459:474	Here, we characterised three amino acids (DFP; residues 451-453) as the nuclear localisation signal of OGT and demonstrated that this motif mediated the nuclear import of non-diffusible β-galactosidase.
27713473	6	18	contain	possesses	932:940	arg1	OGT					921:923	OGT	921:923	OGT	921:923	Our findings may explain how OGT, which possesses a NLS, exists in the nucleus and cytosol simultaneously.
27713473	6	18	contain	possesses	932:940	arg2	NLS					944:946	a NLS	942:946	a NLS	942:946	Our findings may explain how OGT, which possesses a NLS, exists in the nucleus and cytosol simultaneously.
27713473	1	19	theme	Nucleocytoplasmic	109:125	arg1	OGT					149:151	OGT	149:151	OGT	149:151	Nucleocytoplasmic O-GlcNAc transferase (OGT) attaches a single GlcNAc to hydroxyl groups of serine and threonine residues.
27713473	1	19	theme	Nucleocytoplasmic	109:125	arg1	transferase					136:146	Nucleocytoplasmic O-GlcNAc transferase	109:146	Nucleocytoplasmic O-GlcNAc transferase (OGT)	109:152	Nucleocytoplasmic O-GlcNAc transferase (OGT) attaches a single GlcNAc to hydroxyl groups of serine and threonine residues.
27713473	1	20	theme	serine	201:206	arg1	serine					201:206	serine	201:206	serine	201:206	Nucleocytoplasmic O-GlcNAc transferase (OGT) attaches a single GlcNAc to hydroxyl groups of serine and threonine residues.
27713473	1	20	theme	serine	201:206	arg1	groups					191:196	hydroxyl groups	182:196	hydroxyl groups of serine and threonine residues	182:229	Nucleocytoplasmic O-GlcNAc transferase (OGT) attaches a single GlcNAc to hydroxyl groups of serine and threonine residues.
27713473	1	20	theme	serine	201:206	arg1	threonine					212:220	threonine	212:220	threonine	212:220	Nucleocytoplasmic O-GlcNAc transferase (OGT) attaches a single GlcNAc to hydroxyl groups of serine and threonine residues.
27713473	0	21	theme	signal	43:48	arg1	regulation					97:106	its nuclear import regulation	78:106	its nuclear import regulation	78:106	Identification of the nuclear localisation signal of O-GlcNAc transferase and its nuclear import regulation.
27713473	0	21	theme	signal	43:48	arg1	Identification					0:13	Identification	0:13	Identification of the nuclear localisation signal of O-GlcNAc transferase	0:72	Identification of the nuclear localisation signal of O-GlcNAc transferase and its nuclear import regulation.
27713473	5	22	theme	tetratricopeptide	805:821	arg1	repeats					823:829	the tetratricopeptide repeats	801:829	the tetratricopeptide repeats	801:829	We also revealed that O-GlcNAcylation of Ser389, which resides in the tetratricopeptide repeats, plays an important role in the nuclear localisation of OGT.
27713473	4	23	theme	α5	638:639	arg1	protein					641:647	the importin α5 protein	625:647	the importin α5 protein	625:647	OGT bound the importin α5 protein, and this association was abolished when the DFP motif of OGT was mutated or deleted.
27713473	0	24	theme	localisation	30:41	arg1	signal					43:48	the nuclear localisation signal	18:48	the nuclear localisation signal of O-GlcNAc transferase	18:72	Identification of the nuclear localisation signal of O-GlcNAc transferase and its nuclear import regulation.
27713473	1	25	theme	threonine	212:220	arg1	serine					201:206	serine	201:206	serine	201:206	Nucleocytoplasmic O-GlcNAc transferase (OGT) attaches a single GlcNAc to hydroxyl groups of serine and threonine residues.
27713473	1	25	theme	threonine	212:220	arg1	groups					191:196	hydroxyl groups	182:196	hydroxyl groups of serine and threonine residues	182:229	Nucleocytoplasmic O-GlcNAc transferase (OGT) attaches a single GlcNAc to hydroxyl groups of serine and threonine residues.
27713473	1	25	theme	threonine	212:220	arg1	threonine					212:220	threonine	212:220	threonine	212:220	Nucleocytoplasmic O-GlcNAc transferase (OGT) attaches a single GlcNAc to hydroxyl groups of serine and threonine residues.
27713473	0	26	theme	O-GlcNAc	53:60	arg1	transferase					62:72	O-GlcNAc transferase	53:72	O-GlcNAc transferase	53:72	Identification of the nuclear localisation signal of O-GlcNAc transferase and its nuclear import regulation.
27713473	1	27	theme	O-GlcNAc	127:134	arg1	OGT					149:151	OGT	149:151	OGT	149:151	Nucleocytoplasmic O-GlcNAc transferase (OGT) attaches a single GlcNAc to hydroxyl groups of serine and threonine residues.
27713473	1	27	theme	O-GlcNAc	127:134	arg1	transferase					136:146	Nucleocytoplasmic O-GlcNAc transferase	109:146	Nucleocytoplasmic O-GlcNAc transferase (OGT)	109:152	Nucleocytoplasmic O-GlcNAc transferase (OGT) attaches a single GlcNAc to hydroxyl groups of serine and threonine residues.
27713473	3	28	theme	nuclear	565:571	arg1	import					573:578	the nuclear import	561:578	the nuclear import of non-diffusible β-galactosidase	561:612	Here, we characterised three amino acids (DFP; residues 451-453) as the nuclear localisation signal of OGT and demonstrated that this motif mediated the nuclear import of non-diffusible β-galactosidase.
27713473	3	29	theme	nuclear	484:490	arg1	acids					447:451	three amino acids	435:451	three amino acids (DFP; residues 451-453)	435:475	Here, we characterised three amino acids (DFP; residues 451-453) as the nuclear localisation signal of OGT and demonstrated that this motif mediated the nuclear import of non-diffusible β-galactosidase.
27713473	3	29	theme	nuclear	484:490	arg1	signal					505:510	the nuclear localisation signal	480:510	the nuclear localisation signal of OGT	480:517	Here, we characterised three amino acids (DFP; residues 451-453) as the nuclear localisation signal of OGT and demonstrated that this motif mediated the nuclear import of non-diffusible β-galactosidase.
27713473	1	30	dep	serine	201:206	arg1	residues					222:229	residues	222:229	residues	222:229	Nucleocytoplasmic O-GlcNAc transferase (OGT) attaches a single GlcNAc to hydroxyl groups of serine and threonine residues.
27713473	4	31	theme	DFP	694:696	arg1	motif					698:702	the DFP motif	690:702	the DFP motif of OGT	690:709	OGT bound the importin α5 protein, and this association was abolished when the DFP motif of OGT was mutated or deleted.
27713473	2	32	theme	OGT	270:272	arg1	localisation					254:265	the cellular localisation	241:265	the cellular localisation of OGT	241:272	Although the cellular localisation of OGT is important to regulate a variety of cellular processes, the molecular mechanisms regulating the nuclear localisation of OGT is unclear.
27713473	2	32	theme	OGT	270:272	arg1	important					277:285	important	277:285	important	277:285	Although the cellular localisation of OGT is important to regulate a variety of cellular processes, the molecular mechanisms regulating the nuclear localisation of OGT is unclear.
27713473	5	33	theme	OGT	887:889	arg1	localisation					871:882	the nuclear localisation	859:882	the nuclear localisation of OGT	859:889	We also revealed that O-GlcNAcylation of Ser389, which resides in the tetratricopeptide repeats, plays an important role in the nuclear localisation of OGT.
27713473	2	34	theme	processes	321:329	arg1	variety					301:307	a variety	299:307	a variety of cellular processes	299:329	Although the cellular localisation of OGT is important to regulate a variety of cellular processes, the molecular mechanisms regulating the nuclear localisation of OGT is unclear.
27713473	2	34	theme	processes	321:329	arg1	processes					321:329	cellular processes	312:329	cellular processes	312:329	Although the cellular localisation of OGT is important to regulate a variety of cellular processes, the molecular mechanisms regulating the nuclear localisation of OGT is unclear.
27713473	4	35	theme	importin	629:636	arg1	protein					641:647	the importin α5 protein	625:647	the importin α5 protein	625:647	OGT bound the importin α5 protein, and this association was abolished when the DFP motif of OGT was mutated or deleted.
27713473	3	36	theme	non-diffusible	583:596	arg1	β-galactosidase					598:612	non-diffusible β-galactosidase	583:612	non-diffusible β-galactosidase	583:612	Here, we characterised three amino acids (DFP; residues 451-453) as the nuclear localisation signal of OGT and demonstrated that this motif mediated the nuclear import of non-diffusible β-galactosidase.
27713473	2	37	theme	nuclear	372:378	arg1	localisation					380:391	the nuclear localisation	368:391	the nuclear localisation of OGT	368:398	Although the cellular localisation of OGT is important to regulate a variety of cellular processes, the molecular mechanisms regulating the nuclear localisation of OGT is unclear.
27713473	3	38	theme	amino	441:445	arg1	DFP					454:456	DFP	454:456	DFP	454:456	Here, we characterised three amino acids (DFP; residues 451-453) as the nuclear localisation signal of OGT and demonstrated that this motif mediated the nuclear import of non-diffusible β-galactosidase.
27713473	3	38	theme	amino	441:445	arg1	acids					447:451	three amino acids	435:451	three amino acids (DFP; residues 451-453)	435:475	Here, we characterised three amino acids (DFP; residues 451-453) as the nuclear localisation signal of OGT and demonstrated that this motif mediated the nuclear import of non-diffusible β-galactosidase.
27713473	3	38	theme	amino	441:445	arg1	signal					505:510	the nuclear localisation signal	480:510	the nuclear localisation signal of OGT	480:517	Here, we characterised three amino acids (DFP; residues 451-453) as the nuclear localisation signal of OGT and demonstrated that this motif mediated the nuclear import of non-diffusible β-galactosidase.
27713473	0	39	theme	transferase	62:72	arg1	signal					43:48	the nuclear localisation signal	18:48	the nuclear localisation signal of O-GlcNAc transferase	18:72	Identification of the nuclear localisation signal of O-GlcNAc transferase and its nuclear import regulation.
27713473	2	40	theme	cellular	245:252	arg1	localisation					254:265	the cellular localisation	241:265	the cellular localisation of OGT	241:272	Although the cellular localisation of OGT is important to regulate a variety of cellular processes, the molecular mechanisms regulating the nuclear localisation of OGT is unclear.
27713473	2	40	theme	cellular	245:252	arg1	important					277:285	important	277:285	important	277:285	Although the cellular localisation of OGT is important to regulate a variety of cellular processes, the molecular mechanisms regulating the nuclear localisation of OGT is unclear.
29249144	0	0	theme	Biotinylation	73:85	arg1	Quantitation					43:54	Quantitation	43:54	Quantitation	43:54	BioSITe: A Method for Direct Detection and Quantitation of Site-Specific Biotinylation.
29249144	0	0	theme	Biotinylation	73:85	arg1	Detection					29:37	Detection	29:37	Detection	29:37	BioSITe: A Method for Direct Detection and Quantitation of Site-Specific Biotinylation.
29249144	2	1	theme	proteins	375:382	arg1	capture					351:357	the capture	347:357	the capture of biotinylated proteins	347:382	While the high affinity of streptavidin for biotin greatly facilitates the capture of biotinylated proteins, it still presents a challenge, as currently employed, for the recovery of biotinylated peptides.
29249144	1	2	theme	drug	260:263	arg1	discovery					265:273	drug discovery	260:273	drug discovery	260:273	Biotin-based labeling strategies are widely employed to study protein-protein interactions, subcellular proteomes and post-translational modifications, as well as, used in drug discovery.
29249144	0	3	theme	Site-Specific	59:71	arg1	Biotinylation					73:85	Site-Specific Biotinylation	59:85	Site-Specific Biotinylation	59:85	BioSITe: A Method for Direct Detection and Quantitation of Site-Specific Biotinylation.
29249144	5	4	theme	differential	945:956	arg1	analysis					970:977	differential interactome analysis	945:977	differential interactome analysis	945:977	We demonstrate the use of isotopically labeled biotin for quantitative BioSITe experiments that simplify differential interactome analysis and obviate the need for metabolic labeling strategies such as SILAC.
29249144	2	5	theme	biotinylated	362:373	arg1	proteins					375:382	biotinylated proteins	362:382	biotinylated proteins	362:382	While the high affinity of streptavidin for biotin greatly facilitates the capture of biotinylated proteins, it still presents a challenge, as currently employed, for the recovery of biotinylated peptides.
29249144	4	6	theme	chemistry	778:786	arg1	strategies					788:797	biotin-based click chemistry strategies	759:797	proximity-dependent labeling methods, APEX and BioID, as well as biotin-based click chemistry strategies for identifying O-GlcNAc-modified sites	694:837	We demonstrate the utility of BioSITe when applied to proximity-dependent labeling methods, APEX and BioID, as well as biotin-based click chemistry strategies for identifying O-GlcNAc-modified sites.
29249144	5	7	theme	labeling	1014:1021	arg1	strategies					1023:1032	metabolic labeling strategies	1004:1032	metabolic labeling strategies such as SILAC	1004:1046	We demonstrate the use of isotopically labeled biotin for quantitative BioSITe experiments that simplify differential interactome analysis and obviate the need for metabolic labeling strategies such as SILAC.
29249144	5	7	theme	labeling	1014:1021	arg1	SILAC					1042:1046	SILAC	1042:1046	SILAC	1042:1046	We demonstrate the use of isotopically labeled biotin for quantitative BioSITe experiments that simplify differential interactome analysis and obviate the need for metabolic labeling strategies such as SILAC.
29249144	4	8	theme	click	772:776	arg1	strategies					788:797	biotin-based click chemistry strategies	759:797	proximity-dependent labeling methods, APEX and BioID, as well as biotin-based click chemistry strategies for identifying O-GlcNAc-modified sites	694:837	We demonstrate the utility of BioSITe when applied to proximity-dependent labeling methods, APEX and BioID, as well as biotin-based click chemistry strategies for identifying O-GlcNAc-modified sites.
29249144	6	9	theme	protein	1192:1198	arg1	complexes					1200:1208	protein complexes	1192:1208	protein complexes	1192:1208	Our data also highlight the potential value of site-specific biotinylation in providing spatial and topological information about proteins and protein complexes.
29249144	7	10	theme	conventional	1264:1275	arg1	methods					1277:1283	the conventional methods	1260:1283	the conventional methods	1260:1283	Overall, we anticipate that BioSITe will replace the conventional methods in studies where detection of biotinylation sites is important.
29249144	6	11	theme	biotinylation	1110:1122	arg1	value					1087:1091	the potential value	1073:1091	the potential value of site-specific biotinylation in providing spatial and topological information about proteins and protein complexes	1073:1208	Our data also highlight the potential value of site-specific biotinylation in providing spatial and topological information about proteins and protein complexes.
29249144	2	12	theme	high	286:289	arg1	affinity					291:298	the high affinity	282:298	the high affinity of streptavidin for biotin	282:325	While the high affinity of streptavidin for biotin greatly facilitates the capture of biotinylated proteins, it still presents a challenge, as currently employed, for the recovery of biotinylated peptides.
29249144	6	13	theme	spatial	1137:1143	arg1	information					1161:1171	spatial and topological information	1137:1171	spatial and topological information about proteins and protein complexes	1137:1208	Our data also highlight the potential value of site-specific biotinylation in providing spatial and topological information about proteins and protein complexes.
29249144	1	14	theme	subcellular	180:190	arg1	proteomes					192:200	subcellular proteomes	180:200	subcellular proteomes	180:200	Biotin-based labeling strategies are widely employed to study protein-protein interactions, subcellular proteomes and post-translational modifications, as well as, used in drug discovery.
29249144	5	15	theme	interactome	958:968	arg1	analysis					970:977	differential interactome analysis	945:977	differential interactome analysis	945:977	We demonstrate the use of isotopically labeled biotin for quantitative BioSITe experiments that simplify differential interactome analysis and obviate the need for metabolic labeling strategies such as SILAC.
29249144	4	16	theme	BioSITe	670:676	arg1	utility					659:665	the utility	655:665	the utility of BioSITe	655:676	We demonstrate the utility of BioSITe when applied to proximity-dependent labeling methods, APEX and BioID, as well as biotin-based click chemistry strategies for identifying O-GlcNAc-modified sites.
29249144	6	17	theme	topological	1149:1159	arg1	information					1161:1171	spatial and topological information	1137:1171	spatial and topological information about proteins and protein complexes	1137:1208	Our data also highlight the potential value of site-specific biotinylation in providing spatial and topological information about proteins and protein complexes.
29249144	5	18	theme	BioSITe	911:917	arg1	experiments					919:929	quantitative BioSITe experiments	898:929	quantitative BioSITe experiments that simplify differential interactome analysis and obviate the need for metabolic labeling strategies such as SILAC	898:1046	We demonstrate the use of isotopically labeled biotin for quantitative BioSITe experiments that simplify differential interactome analysis and obviate the need for metabolic labeling strategies such as SILAC.
29249144	1	19	theme	Biotin-based	88:99	arg1	strategies					110:119	Biotin-based labeling strategies	88:119	Biotin-based labeling strategies	88:119	Biotin-based labeling strategies are widely employed to study protein-protein interactions, subcellular proteomes and post-translational modifications, as well as, used in drug discovery.
29249144	1	20	theme	post-translational	206:223	arg1	modifications					225:237	post-translational modifications	206:237	post-translational modifications	206:237	Biotin-based labeling strategies are widely employed to study protein-protein interactions, subcellular proteomes and post-translational modifications, as well as, used in drug discovery.
29249144	1	21	theme	labeling	101:108	arg1	strategies					110:119	Biotin-based labeling strategies	88:119	Biotin-based labeling strategies	88:119	Biotin-based labeling strategies are widely employed to study protein-protein interactions, subcellular proteomes and post-translational modifications, as well as, used in drug discovery.
29249144	3	22	theme	Identification	540:553	arg1	BioSITe					567:573	BioSITe	567:573	BioSITe	567:573	Here we describe a strategy designated Biotinylation Site Identification Technology (BioSITe) for the capture of biotinylated peptides for LC-MS/MS analyses.
29249144	3	22	theme	Identification	540:553	arg1	Technology					555:564	Biotinylation Site Identification Technology	521:564	Biotinylation Site Identification Technology (BioSITe) for the capture of biotinylated peptides for LC-MS/MS analyses	521:637	Here we describe a strategy designated Biotinylation Site Identification Technology (BioSITe) for the capture of biotinylated peptides for LC-MS/MS analyses.
29249144	2	23	theme	streptavidin	303:314	arg1	affinity					291:298	the high affinity	282:298	the high affinity of streptavidin for biotin	282:325	While the high affinity of streptavidin for biotin greatly facilitates the capture of biotinylated proteins, it still presents a challenge, as currently employed, for the recovery of biotinylated peptides.
29249144	4	24	theme	labeling	714:721	arg1	methods					723:729	proximity-dependent labeling methods	694:729	proximity-dependent labeling methods	694:729	We demonstrate the utility of BioSITe when applied to proximity-dependent labeling methods, APEX and BioID, as well as biotin-based click chemistry strategies for identifying O-GlcNAc-modified sites.
29249144	4	24	theme	labeling	714:721	arg1	BioID					741:745	BioID	741:745	BioID	741:745	We demonstrate the utility of BioSITe when applied to proximity-dependent labeling methods, APEX and BioID, as well as biotin-based click chemistry strategies for identifying O-GlcNAc-modified sites.
29249144	4	24	theme	labeling	714:721	arg1	APEX					732:735	APEX	732:735	APEX	732:735	We demonstrate the utility of BioSITe when applied to proximity-dependent labeling methods, APEX and BioID, as well as biotin-based click chemistry strategies for identifying O-GlcNAc-modified sites.
29249144	0	25	theme	Direct	22:27	arg1	Detection					29:37	Detection	29:37	Detection	29:37	BioSITe: A Method for Direct Detection and Quantitation of Site-Specific Biotinylation.
29249144	6	26	theme	site-specific	1096:1108	arg1	biotinylation					1110:1122	site-specific biotinylation	1096:1122	site-specific biotinylation	1096:1122	Our data also highlight the potential value of site-specific biotinylation in providing spatial and topological information about proteins and protein complexes.
29249144	3	27	theme	peptides	608:615	arg1	capture					584:590	the capture	580:590	the capture of biotinylated peptides	580:615	Here we describe a strategy designated Biotinylation Site Identification Technology (BioSITe) for the capture of biotinylated peptides for LC-MS/MS analyses.
29249144	5	28	theme	labeled	879:885	arg1	biotin					887:892	isotopically labeled biotin	866:892	isotopically labeled biotin	866:892	We demonstrate the use of isotopically labeled biotin for quantitative BioSITe experiments that simplify differential interactome analysis and obviate the need for metabolic labeling strategies such as SILAC.
29249144	2	29	theme	peptides	472:479	arg1	recovery					447:454	the recovery	443:454	the recovery of biotinylated peptides	443:479	While the high affinity of streptavidin for biotin greatly facilitates the capture of biotinylated proteins, it still presents a challenge, as currently employed, for the recovery of biotinylated peptides.
29249144	5	30	theme	biotin	887:892	arg1	use					859:861	the use	855:861	the use of isotopically labeled biotin	855:892	We demonstrate the use of isotopically labeled biotin for quantitative BioSITe experiments that simplify differential interactome analysis and obviate the need for metabolic labeling strategies such as SILAC.
29249144	2	31	theme	biotinylated	459:470	arg1	peptides					472:479	biotinylated peptides	459:479	biotinylated peptides	459:479	While the high affinity of streptavidin for biotin greatly facilitates the capture of biotinylated proteins, it still presents a challenge, as currently employed, for the recovery of biotinylated peptides.
29249144	5	32	theme	metabolic	1004:1012	arg1	strategies					1023:1032	metabolic labeling strategies	1004:1032	metabolic labeling strategies such as SILAC	1004:1046	We demonstrate the use of isotopically labeled biotin for quantitative BioSITe experiments that simplify differential interactome analysis and obviate the need for metabolic labeling strategies such as SILAC.
29249144	5	32	theme	metabolic	1004:1012	arg1	SILAC					1042:1046	SILAC	1042:1046	SILAC	1042:1046	We demonstrate the use of isotopically labeled biotin for quantitative BioSITe experiments that simplify differential interactome analysis and obviate the need for metabolic labeling strategies such as SILAC.
29249144	3	33	theme	biotinylated	595:606	arg1	peptides					608:615	biotinylated peptides	595:615	biotinylated peptides	595:615	Here we describe a strategy designated Biotinylation Site Identification Technology (BioSITe) for the capture of biotinylated peptides for LC-MS/MS analyses.
29249144	1	34	used	used	252:255	arg2	strategies					110:119	Biotin-based labeling strategies	88:119	Biotin-based labeling strategies	88:119	Biotin-based labeling strategies are widely employed to study protein-protein interactions, subcellular proteomes and post-translational modifications, as well as, used in drug discovery.
29249144	4	35	theme	O-GlcNAc-modified	815:831	arg1	sites					833:837	O-GlcNAc-modified sites	815:837	O-GlcNAc-modified sites	815:837	We demonstrate the utility of BioSITe when applied to proximity-dependent labeling methods, APEX and BioID, as well as biotin-based click chemistry strategies for identifying O-GlcNAc-modified sites.
29249144	4	36	theme	proximity-dependent	694:712	arg1	methods					723:729	proximity-dependent labeling methods	694:729	proximity-dependent labeling methods	694:729	We demonstrate the utility of BioSITe when applied to proximity-dependent labeling methods, APEX and BioID, as well as biotin-based click chemistry strategies for identifying O-GlcNAc-modified sites.
29249144	4	36	theme	proximity-dependent	694:712	arg1	BioID					741:745	BioID	741:745	BioID	741:745	We demonstrate the utility of BioSITe when applied to proximity-dependent labeling methods, APEX and BioID, as well as biotin-based click chemistry strategies for identifying O-GlcNAc-modified sites.
29249144	4	36	theme	proximity-dependent	694:712	arg1	APEX					732:735	APEX	732:735	APEX	732:735	We demonstrate the utility of BioSITe when applied to proximity-dependent labeling methods, APEX and BioID, as well as biotin-based click chemistry strategies for identifying O-GlcNAc-modified sites.
29249144	4	37	theme	biotin-based	759:770	arg1	strategies					788:797	biotin-based click chemistry strategies	759:797	proximity-dependent labeling methods, APEX and BioID, as well as biotin-based click chemistry strategies for identifying O-GlcNAc-modified sites	694:837	We demonstrate the utility of BioSITe when applied to proximity-dependent labeling methods, APEX and BioID, as well as biotin-based click chemistry strategies for identifying O-GlcNAc-modified sites.
29249144	1	38	theme	protein-protein	150:164	arg1	interactions					166:177	protein-protein interactions	150:177	protein-protein interactions	150:177	Biotin-based labeling strategies are widely employed to study protein-protein interactions, subcellular proteomes and post-translational modifications, as well as, used in drug discovery.
29249144	6	39	theme	potential	1077:1085	arg1	value					1087:1091	the potential value	1073:1091	the potential value of site-specific biotinylation in providing spatial and topological information about proteins and protein complexes	1073:1208	Our data also highlight the potential value of site-specific biotinylation in providing spatial and topological information about proteins and protein complexes.
29249144	3	40	theme	LC-MS/MS	621:628	arg1	analyses					630:637	LC-MS/MS analyses	621:637	LC-MS/MS analyses	621:637	Here we describe a strategy designated Biotinylation Site Identification Technology (BioSITe) for the capture of biotinylated peptides for LC-MS/MS analyses.
29249144	3	41	theme	Biotinylation	521:533	arg1	BioSITe					567:573	BioSITe	567:573	BioSITe	567:573	Here we describe a strategy designated Biotinylation Site Identification Technology (BioSITe) for the capture of biotinylated peptides for LC-MS/MS analyses.
29249144	3	41	theme	Biotinylation	521:533	arg1	Technology					555:564	Biotinylation Site Identification Technology	521:564	Biotinylation Site Identification Technology (BioSITe) for the capture of biotinylated peptides for LC-MS/MS analyses	521:637	Here we describe a strategy designated Biotinylation Site Identification Technology (BioSITe) for the capture of biotinylated peptides for LC-MS/MS analyses.
29249144	5	42	theme	quantitative	898:909	arg1	experiments					919:929	quantitative BioSITe experiments	898:929	quantitative BioSITe experiments that simplify differential interactome analysis and obviate the need for metabolic labeling strategies such as SILAC	898:1046	We demonstrate the use of isotopically labeled biotin for quantitative BioSITe experiments that simplify differential interactome analysis and obviate the need for metabolic labeling strategies such as SILAC.
29249144	7	43	theme	biotinylation	1315:1327	arg1	sites					1329:1333	biotinylation sites	1315:1333	biotinylation sites	1315:1333	Overall, we anticipate that BioSITe will replace the conventional methods in studies where detection of biotinylation sites is important.
29249144	0	44	dep	BioSITe	0:6	arg1	Method					11:16	A Method	9:16	BioSITe: A Method for Direct Detection and Quantitation of Site-Specific Biotinylation.	0:86	BioSITe: A Method for Direct Detection and Quantitation of Site-Specific Biotinylation.
29249144	3	45	theme	Site	535:538	arg1	BioSITe					567:573	BioSITe	567:573	BioSITe	567:573	Here we describe a strategy designated Biotinylation Site Identification Technology (BioSITe) for the capture of biotinylated peptides for LC-MS/MS analyses.
29249144	3	45	theme	Site	535:538	arg1	Technology					555:564	Biotinylation Site Identification Technology	521:564	Biotinylation Site Identification Technology (BioSITe) for the capture of biotinylated peptides for LC-MS/MS analyses	521:637	Here we describe a strategy designated Biotinylation Site Identification Technology (BioSITe) for the capture of biotinylated peptides for LC-MS/MS analyses.
29249144	7	46	theme	sites	1329:1333	arg1	detection					1302:1310	detection	1302:1310	detection of biotinylation sites	1302:1333	Overall, we anticipate that BioSITe will replace the conventional methods in studies where detection of biotinylation sites is important.
28604694	7	0	theme	O-GlcNAcase	962:972	arg1	trap					996:999	a substrate trap	984:999	a substrate trap	984:999	Using a catalytically inactive bacterial O-GlcNAcase mutant as a substrate trap, we have enriched the O-GlcNAc proteome of the developing Drosophila embryo, identifying, among others, known regulators of Hox genes as candidate conveyors of OGT function during embryonic development.
28604694	7	0	theme	O-GlcNAcase	962:972	arg1	mutant					974:979	a catalytically inactive bacterial O-GlcNAcase mutant	927:979	a catalytically inactive bacterial O-GlcNAcase mutant	927:979	Using a catalytically inactive bacterial O-GlcNAcase mutant as a substrate trap, we have enriched the O-GlcNAc proteome of the developing Drosophila embryo, identifying, among others, known regulators of Hox genes as candidate conveyors of OGT function during embryonic development.
28604694	7	1	theme	O-GlcNAc	1023:1030	arg1	proteome					1032:1039	the O-GlcNAc proteome	1019:1039	the O-GlcNAc proteome of the developing Drosophila embryo	1019:1075	Using a catalytically inactive bacterial O-GlcNAcase mutant as a substrate trap, we have enriched the O-GlcNAc proteome of the developing Drosophila embryo, identifying, among others, known regulators of Hox genes as candidate conveyors of OGT function during embryonic development.
28604694	6	2	from	Identification	764:777	arg1	samples					822:828	biological samples	811:828	biological samples	811:828	Identification of O-GlcNAcylated proteins from biological samples is hampered by the low stoichiometry of this modification and by limited enrichment tools.
28604694	4	3	dep	gene	443:446	arg1	sxc					464:466	supersex combs (sxc)	448:467	The Drosophila melanogaster gene supersex combs (sxc)	415:467	The Drosophila melanogaster gene supersex combs (sxc), which encodes OGT, is a polycomb gene, whose null mutants display homeotic transformations and die at the pharate adult stage.
28604694	4	4	theme	adult	584:588	arg1	stage					590:594	the pharate adult stage	572:594	the pharate adult stage	572:594	The Drosophila melanogaster gene supersex combs (sxc), which encodes OGT, is a polycomb gene, whose null mutants display homeotic transformations and die at the pharate adult stage.
28604694	5	5	theme	embryonic	719:727	arg1	development					729:739	embryonic development	719:739	embryonic development	719:739	However, the identities of the O-GlcNAcylated proteins involved and the underlying mechanisms linking these phenotypes to embryonic development are poorly understood.
28604694	4	6	theme	null	515:518	arg1	mutants					520:526	null mutants	515:526	null mutants	515:526	The Drosophila melanogaster gene supersex combs (sxc), which encodes OGT, is a polycomb gene, whose null mutants display homeotic transformations and die at the pharate adult stage.
28604694	7	7	theme	OGT	1161:1163	arg1	conveyors					1148:1156	candidate conveyors	1138:1156	candidate conveyors of OGT	1138:1163	Using a catalytically inactive bacterial O-GlcNAcase mutant as a substrate trap, we have enriched the O-GlcNAc proteome of the developing Drosophila embryo, identifying, among others, known regulators of Hox genes as candidate conveyors of OGT function during embryonic development.
28604694	4	8	theme	melanogaster	430:441	arg1	gene					443:446	The Drosophila melanogaster gene	415:446	The Drosophila melanogaster gene supersex combs (sxc)	415:467	The Drosophila melanogaster gene supersex combs (sxc), which encodes OGT, is a polycomb gene, whose null mutants display homeotic transformations and die at the pharate adult stage.
28604694	4	8	theme	melanogaster	430:441	arg1	gene					503:506	a polycomb gene	492:506	a polycomb gene	492:506	The Drosophila melanogaster gene supersex combs (sxc), which encodes OGT, is a polycomb gene, whose null mutants display homeotic transformations and die at the pharate adult stage.
28604694	4	8	theme	melanogaster	430:441	arg1	OGT					484:486	OGT	484:486	OGT	484:486	The Drosophila melanogaster gene supersex combs (sxc), which encodes OGT, is a polycomb gene, whose null mutants display homeotic transformations and die at the pharate adult stage.
28604694	4	9	theme	pharate	576:582	arg1	stage					590:594	the pharate adult stage	572:594	the pharate adult stage	572:594	The Drosophila melanogaster gene supersex combs (sxc), which encodes OGT, is a polycomb gene, whose null mutants display homeotic transformations and die at the pharate adult stage.
28604694	7	10	theme	candidate	1138:1146	arg1	conveyors					1148:1156	candidate conveyors	1138:1156	candidate conveyors of OGT	1138:1163	Using a catalytically inactive bacterial O-GlcNAcase mutant as a substrate trap, we have enriched the O-GlcNAc proteome of the developing Drosophila embryo, identifying, among others, known regulators of Hox genes as candidate conveyors of OGT function during embryonic development.
28604694	4	11	theme	Drosophila	419:428	arg1	gene					443:446	The Drosophila melanogaster gene	415:446	The Drosophila melanogaster gene supersex combs (sxc)	415:467	The Drosophila melanogaster gene supersex combs (sxc), which encodes OGT, is a polycomb gene, whose null mutants display homeotic transformations and die at the pharate adult stage.
28604694	4	11	theme	Drosophila	419:428	arg1	gene					503:506	a polycomb gene	492:506	a polycomb gene	492:506	The Drosophila melanogaster gene supersex combs (sxc), which encodes OGT, is a polycomb gene, whose null mutants display homeotic transformations and die at the pharate adult stage.
28604694	4	11	theme	Drosophila	419:428	arg1	OGT					484:486	OGT	484:486	OGT	484:486	The Drosophila melanogaster gene supersex combs (sxc), which encodes OGT, is a polycomb gene, whose null mutants display homeotic transformations and die at the pharate adult stage.
28604694	1	12	theme	Protein	67:73	arg1	modification					126:137	a reversible post-translational modification	94:137	a reversible post-translational modification of serines and threonines on nucleocytoplasmic proteins	94:193	Protein O-GlcNAcylation is a reversible post-translational modification of serines and threonines on nucleocytoplasmic proteins.
28604694	1	12	theme	Protein	67:73	arg1	O-GlcNAcylation					75:89	Protein O-GlcNAcylation	67:89	Protein O-GlcNAcylation	67:89	Protein O-GlcNAcylation is a reversible post-translational modification of serines and threonines on nucleocytoplasmic proteins.
28604694	5	13	theme	underlying	669:678	arg1	mechanisms					680:689	the underlying mechanisms	665:689	the underlying mechanisms linking these phenotypes to embryonic development	665:739	However, the identities of the O-GlcNAcylated proteins involved and the underlying mechanisms linking these phenotypes to embryonic development are poorly understood.
28604694	4	14	theme	supersex	448:455	arg1	sxc					464:466	supersex combs (sxc)	448:467	The Drosophila melanogaster gene supersex combs (sxc)	415:467	The Drosophila melanogaster gene supersex combs (sxc), which encodes OGT, is a polycomb gene, whose null mutants display homeotic transformations and die at the pharate adult stage.
28604694	7	15	theme	embryo	1070:1075	arg1	proteome					1032:1039	the O-GlcNAc proteome	1019:1039	the O-GlcNAc proteome of the developing Drosophila embryo	1019:1075	Using a catalytically inactive bacterial O-GlcNAcase mutant as a substrate trap, we have enriched the O-GlcNAc proteome of the developing Drosophila embryo, identifying, among others, known regulators of Hox genes as candidate conveyors of OGT function during embryonic development.
28604694	7	16	theme	genes	1129:1133	arg1	regulators					1111:1120	known regulators	1105:1120	known regulators of Hox genes as candidate conveyors of OGT function during embryonic development	1105:1201	Using a catalytically inactive bacterial O-GlcNAcase mutant as a substrate trap, we have enriched the O-GlcNAc proteome of the developing Drosophila embryo, identifying, among others, known regulators of Hox genes as candidate conveyors of OGT function during embryonic development.
28604694	4	17	theme	polycomb	494:501	arg1	gene					443:446	The Drosophila melanogaster gene	415:446	The Drosophila melanogaster gene supersex combs (sxc)	415:467	The Drosophila melanogaster gene supersex combs (sxc), which encodes OGT, is a polycomb gene, whose null mutants display homeotic transformations and die at the pharate adult stage.
28604694	4	17	theme	polycomb	494:501	arg1	gene					503:506	a polycomb gene	492:506	a polycomb gene	492:506	The Drosophila melanogaster gene supersex combs (sxc), which encodes OGT, is a polycomb gene, whose null mutants display homeotic transformations and die at the pharate adult stage.
28604694	7	18	theme	embryonic	1181:1189	arg1	development					1191:1201	embryonic development	1181:1201	embryonic development	1181:1201	Using a catalytically inactive bacterial O-GlcNAcase mutant as a substrate trap, we have enriched the O-GlcNAc proteome of the developing Drosophila embryo, identifying, among others, known regulators of Hox genes as candidate conveyors of OGT function during embryonic development.
28604694	7	19	theme	substrate	986:994	arg1	trap					996:999	a substrate trap	984:999	a substrate trap	984:999	Using a catalytically inactive bacterial O-GlcNAcase mutant as a substrate trap, we have enriched the O-GlcNAc proteome of the developing Drosophila embryo, identifying, among others, known regulators of Hox genes as candidate conveyors of OGT function during embryonic development.
28604694	7	19	theme	substrate	986:994	arg1	mutant					974:979	a catalytically inactive bacterial O-GlcNAcase mutant	927:979	a catalytically inactive bacterial O-GlcNAcase mutant	927:979	Using a catalytically inactive bacterial O-GlcNAcase mutant as a substrate trap, we have enriched the O-GlcNAc proteome of the developing Drosophila embryo, identifying, among others, known regulators of Hox genes as candidate conveyors of OGT function during embryonic development.
28604694	2	20	dep	hydrolase	264:272	arg1	OGA					290:292	OGA	290:292	OGA	290:292	It is cycled by the enzymes O-GlcNAc transferase (OGT) and O-GlcNAc hydrolase (O-GlcNAcase or OGA).
28604694	2	20	dep	hydrolase	264:272	arg1	O-GlcNAcase					275:285	O-GlcNAcase	275:285	O-GlcNAcase	275:285	It is cycled by the enzymes O-GlcNAc transferase (OGT) and O-GlcNAc hydrolase (O-GlcNAcase or OGA).
28604694	0	21	theme	mutant	2:7	arg1	O-GlcNAcase					9:19	A mutant O-GlcNAcase	0:19	A mutant O-GlcNAcase	0:19	A mutant O-GlcNAcase enriches Drosophila developmental regulators.
28604694	5	22	theme	O-GlcNAcylated	628:641	arg1	proteins					643:650	the O-GlcNAcylated proteins	624:650	the O-GlcNAcylated proteins involved	624:659	However, the identities of the O-GlcNAcylated proteins involved and the underlying mechanisms linking these phenotypes to embryonic development are poorly understood.
28604694	1	23	theme	reversible	96:105	arg1	modification					126:137	a reversible post-translational modification	94:137	a reversible post-translational modification of serines and threonines on nucleocytoplasmic proteins	94:193	Protein O-GlcNAcylation is a reversible post-translational modification of serines and threonines on nucleocytoplasmic proteins.
28604694	1	23	theme	reversible	96:105	arg1	O-GlcNAcylation					75:89	Protein O-GlcNAcylation	67:89	Protein O-GlcNAcylation	67:89	Protein O-GlcNAcylation is a reversible post-translational modification of serines and threonines on nucleocytoplasmic proteins.
28604694	5	24	theme	proteins	643:650	arg1	identities					610:619	the identities	606:619	the identities of the O-GlcNAcylated proteins involved and the underlying mechanisms linking these phenotypes to embryonic development	606:739	However, the identities of the O-GlcNAcylated proteins involved and the underlying mechanisms linking these phenotypes to embryonic development are poorly understood.
28604694	1	25	theme	post-translational	107:124	arg1	modification					126:137	a reversible post-translational modification	94:137	a reversible post-translational modification of serines and threonines on nucleocytoplasmic proteins	94:193	Protein O-GlcNAcylation is a reversible post-translational modification of serines and threonines on nucleocytoplasmic proteins.
28604694	1	25	theme	post-translational	107:124	arg1	O-GlcNAcylation					75:89	Protein O-GlcNAcylation	67:89	Protein O-GlcNAcylation	67:89	Protein O-GlcNAcylation is a reversible post-translational modification of serines and threonines on nucleocytoplasmic proteins.
28604694	3	26	theme	early	394:398	arg1	embryogenesis					400:412	early embryogenesis	394:412	early embryogenesis	394:412	Genetic approaches in model organisms have revealed that protein O-GlcNAcylation is essential for early embryogenesis.
28604694	7	27	theme	known	1105:1109	arg1	regulators					1111:1120	known regulators	1105:1120	known regulators of Hox genes as candidate conveyors of OGT function during embryonic development	1105:1201	Using a catalytically inactive bacterial O-GlcNAcase mutant as a substrate trap, we have enriched the O-GlcNAc proteome of the developing Drosophila embryo, identifying, among others, known regulators of Hox genes as candidate conveyors of OGT function during embryonic development.
28604694	6	28	theme	biological	811:820	arg1	samples					822:828	biological samples	811:828	biological samples	811:828	Identification of O-GlcNAcylated proteins from biological samples is hampered by the low stoichiometry of this modification and by limited enrichment tools.
28604694	6	29	from	samples	822:828	arg1	Identification					764:777	Identification	764:777	Identification of O-GlcNAcylated proteins from biological samples	764:828	Identification of O-GlcNAcylated proteins from biological samples is hampered by the low stoichiometry of this modification and by limited enrichment tools.
28604694	6	29	from	samples	822:828	arg1	proteins					797:804	O-GlcNAcylated proteins	782:804	O-GlcNAcylated proteins from biological samples	782:828	Identification of O-GlcNAcylated proteins from biological samples is hampered by the low stoichiometry of this modification and by limited enrichment tools.
28604694	3	30	theme	Genetic	296:302	arg1	approaches					304:313	Genetic approaches	296:313	Genetic approaches in model organisms	296:332	Genetic approaches in model organisms have revealed that protein O-GlcNAcylation is essential for early embryogenesis.
28604694	7	31	theme	Hox	1125:1127	arg1	genes					1129:1133	Hox genes	1125:1133	Hox genes	1125:1133	Using a catalytically inactive bacterial O-GlcNAcase mutant as a substrate trap, we have enriched the O-GlcNAc proteome of the developing Drosophila embryo, identifying, among others, known regulators of Hox genes as candidate conveyors of OGT function during embryonic development.
28604694	0	32	theme	developmental	41:53	arg1	regulators					55:64	Drosophila developmental regulators	30:64	Drosophila developmental regulators	30:64	A mutant O-GlcNAcase enriches Drosophila developmental regulators.
28604694	6	33	theme	enrichment	903:912	arg1	tools					914:918	limited enrichment tools	895:918	limited enrichment tools	895:918	Identification of O-GlcNAcylated proteins from biological samples is hampered by the low stoichiometry of this modification and by limited enrichment tools.
28604694	2	34	theme	O-GlcNAc	255:262	arg1	enzymes					216:222	the enzymes	212:222	the enzymes O-GlcNAc transferase (OGT) and O-GlcNAc hydrolase (O-GlcNAcase or OGA)	212:293	It is cycled by the enzymes O-GlcNAc transferase (OGT) and O-GlcNAc hydrolase (O-GlcNAcase or OGA).
28604694	2	34	theme	O-GlcNAc	255:262	arg1	hydrolase					264:272	O-GlcNAc hydrolase	255:272	O-GlcNAc hydrolase (O-GlcNAcase or OGA)	255:293	It is cycled by the enzymes O-GlcNAc transferase (OGT) and O-GlcNAc hydrolase (O-GlcNAcase or OGA).
28604694	0	35	theme	Drosophila	30:39	arg1	regulators					55:64	Drosophila developmental regulators	30:64	Drosophila developmental regulators	30:64	A mutant O-GlcNAcase enriches Drosophila developmental regulators.
28604694	6	36	theme	limited	895:901	arg1	tools					914:918	limited enrichment tools	895:918	limited enrichment tools	895:918	Identification of O-GlcNAcylated proteins from biological samples is hampered by the low stoichiometry of this modification and by limited enrichment tools.
28604694	7	37	theme	Drosophila	1059:1068	arg1	embryo					1070:1075	the developing Drosophila embryo	1044:1075	the developing Drosophila embryo	1044:1075	Using a catalytically inactive bacterial O-GlcNAcase mutant as a substrate trap, we have enriched the O-GlcNAc proteome of the developing Drosophila embryo, identifying, among others, known regulators of Hox genes as candidate conveyors of OGT function during embryonic development.
28604694	3	38	theme	model	318:322	arg1	organisms					324:332	model organisms	318:332	model organisms	318:332	Genetic approaches in model organisms have revealed that protein O-GlcNAcylation is essential for early embryogenesis.
28604694	6	39	theme	proteins	797:804	arg1	Identification					764:777	Identification	764:777	Identification of O-GlcNAcylated proteins from biological samples	764:828	Identification of O-GlcNAcylated proteins from biological samples is hampered by the low stoichiometry of this modification and by limited enrichment tools.
28604694	1	40	theme	serines	142:148	arg1	modification					126:137	a reversible post-translational modification	94:137	a reversible post-translational modification of serines and threonines on nucleocytoplasmic proteins	94:193	Protein O-GlcNAcylation is a reversible post-translational modification of serines and threonines on nucleocytoplasmic proteins.
28604694	1	40	theme	serines	142:148	arg1	O-GlcNAcylation					75:89	Protein O-GlcNAcylation	67:89	Protein O-GlcNAcylation	67:89	Protein O-GlcNAcylation is a reversible post-translational modification of serines and threonines on nucleocytoplasmic proteins.
28604694	6	41	theme	modification	875:886	arg1	stoichiometry					853:865	the low stoichiometry	845:865	the low stoichiometry of this modification	845:886	Identification of O-GlcNAcylated proteins from biological samples is hampered by the low stoichiometry of this modification and by limited enrichment tools.
28604694	6	42	theme	O-GlcNAcylated	782:795	arg1	proteins					797:804	O-GlcNAcylated proteins	782:804	O-GlcNAcylated proteins from biological samples	782:828	Identification of O-GlcNAcylated proteins from biological samples is hampered by the low stoichiometry of this modification and by limited enrichment tools.
28604694	1	43	from	modification	126:137	arg1	proteins					186:193	nucleocytoplasmic proteins	168:193	nucleocytoplasmic proteins	168:193	Protein O-GlcNAcylation is a reversible post-translational modification of serines and threonines on nucleocytoplasmic proteins.
28604694	4	44	theme	homeotic	536:543	arg1	transformations					545:559	homeotic transformations	536:559	homeotic transformations	536:559	The Drosophila melanogaster gene supersex combs (sxc), which encodes OGT, is a polycomb gene, whose null mutants display homeotic transformations and die at the pharate adult stage.
28604694	5	45	theme	mechanisms	680:689	arg1	identities					610:619	the identities	606:619	the identities of the O-GlcNAcylated proteins involved and the underlying mechanisms linking these phenotypes to embryonic development	606:739	However, the identities of the O-GlcNAcylated proteins involved and the underlying mechanisms linking these phenotypes to embryonic development are poorly understood.
28604694	4	46	theme	combs	457:461	arg1	sxc					464:466	supersex combs (sxc)	448:467	The Drosophila melanogaster gene supersex combs (sxc)	415:467	The Drosophila melanogaster gene supersex combs (sxc), which encodes OGT, is a polycomb gene, whose null mutants display homeotic transformations and die at the pharate adult stage.
28604694	6	47	theme	low	849:851	arg1	stoichiometry					853:865	the low stoichiometry	845:865	the low stoichiometry of this modification	845:886	Identification of O-GlcNAcylated proteins from biological samples is hampered by the low stoichiometry of this modification and by limited enrichment tools.
28604694	1	48	theme	threonines	154:163	arg1	modification					126:137	a reversible post-translational modification	94:137	a reversible post-translational modification of serines and threonines on nucleocytoplasmic proteins	94:193	Protein O-GlcNAcylation is a reversible post-translational modification of serines and threonines on nucleocytoplasmic proteins.
28604694	1	48	theme	threonines	154:163	arg1	O-GlcNAcylation					75:89	Protein O-GlcNAcylation	67:89	Protein O-GlcNAcylation	67:89	Protein O-GlcNAcylation is a reversible post-translational modification of serines and threonines on nucleocytoplasmic proteins.
28604694	3	49	from	approaches	304:313	arg1	organisms					324:332	model organisms	318:332	model organisms	318:332	Genetic approaches in model organisms have revealed that protein O-GlcNAcylation is essential for early embryogenesis.
28604694	7	50	theme	developing	1048:1057	arg1	embryo					1070:1075	the developing Drosophila embryo	1044:1075	the developing Drosophila embryo	1044:1075	Using a catalytically inactive bacterial O-GlcNAcase mutant as a substrate trap, we have enriched the O-GlcNAc proteome of the developing Drosophila embryo, identifying, among others, known regulators of Hox genes as candidate conveyors of OGT function during embryonic development.
28604694	2	51	theme	O-GlcNAc	224:231	arg1	OGT					246:248	OGT	246:248	OGT	246:248	It is cycled by the enzymes O-GlcNAc transferase (OGT) and O-GlcNAc hydrolase (O-GlcNAcase or OGA).
28604694	2	51	theme	O-GlcNAc	224:231	arg1	transferase					233:243	O-GlcNAc transferase	224:243	O-GlcNAc transferase (OGT)	224:249	It is cycled by the enzymes O-GlcNAc transferase (OGT) and O-GlcNAc hydrolase (O-GlcNAcase or OGA).
28604694	2	51	theme	O-GlcNAc	224:231	arg1	enzymes					216:222	the enzymes	212:222	the enzymes O-GlcNAc transferase (OGT) and O-GlcNAc hydrolase (O-GlcNAcase or OGA)	212:293	It is cycled by the enzymes O-GlcNAc transferase (OGT) and O-GlcNAc hydrolase (O-GlcNAcase or OGA).
28604694	7	52	theme	inactive	943:950	arg1	trap					996:999	a substrate trap	984:999	a substrate trap	984:999	Using a catalytically inactive bacterial O-GlcNAcase mutant as a substrate trap, we have enriched the O-GlcNAc proteome of the developing Drosophila embryo, identifying, among others, known regulators of Hox genes as candidate conveyors of OGT function during embryonic development.
28604694	7	52	theme	inactive	943:950	arg1	mutant					974:979	a catalytically inactive bacterial O-GlcNAcase mutant	927:979	a catalytically inactive bacterial O-GlcNAcase mutant	927:979	Using a catalytically inactive bacterial O-GlcNAcase mutant as a substrate trap, we have enriched the O-GlcNAc proteome of the developing Drosophila embryo, identifying, among others, known regulators of Hox genes as candidate conveyors of OGT function during embryonic development.
28604694	2	53	dep	enzymes	216:222	arg1	OGT					246:248	OGT	246:248	OGT	246:248	It is cycled by the enzymes O-GlcNAc transferase (OGT) and O-GlcNAc hydrolase (O-GlcNAcase or OGA).
28604694	2	53	dep	enzymes	216:222	arg1	transferase					233:243	O-GlcNAc transferase	224:243	O-GlcNAc transferase (OGT)	224:249	It is cycled by the enzymes O-GlcNAc transferase (OGT) and O-GlcNAc hydrolase (O-GlcNAcase or OGA).
28604694	2	53	dep	enzymes	216:222	arg1	enzymes					216:222	the enzymes	212:222	the enzymes O-GlcNAc transferase (OGT) and O-GlcNAc hydrolase (O-GlcNAcase or OGA)	212:293	It is cycled by the enzymes O-GlcNAc transferase (OGT) and O-GlcNAc hydrolase (O-GlcNAcase or OGA).
28604694	2	53	dep	enzymes	216:222	arg1	hydrolase					264:272	O-GlcNAc hydrolase	255:272	O-GlcNAc hydrolase (O-GlcNAcase or OGA)	255:293	It is cycled by the enzymes O-GlcNAc transferase (OGT) and O-GlcNAc hydrolase (O-GlcNAcase or OGA).
28604694	1	54	theme	nucleocytoplasmic	168:184	arg1	proteins					186:193	nucleocytoplasmic proteins	168:193	nucleocytoplasmic proteins	168:193	Protein O-GlcNAcylation is a reversible post-translational modification of serines and threonines on nucleocytoplasmic proteins.
28604694	7	55	theme	bacterial	952:960	arg1	trap					996:999	a substrate trap	984:999	a substrate trap	984:999	Using a catalytically inactive bacterial O-GlcNAcase mutant as a substrate trap, we have enriched the O-GlcNAc proteome of the developing Drosophila embryo, identifying, among others, known regulators of Hox genes as candidate conveyors of OGT function during embryonic development.
28604694	7	55	theme	bacterial	952:960	arg1	mutant					974:979	a catalytically inactive bacterial O-GlcNAcase mutant	927:979	a catalytically inactive bacterial O-GlcNAcase mutant	927:979	Using a catalytically inactive bacterial O-GlcNAcase mutant as a substrate trap, we have enriched the O-GlcNAc proteome of the developing Drosophila embryo, identifying, among others, known regulators of Hox genes as candidate conveyors of OGT function during embryonic development.
28604694	3	56	theme	protein	353:359	arg1	O-GlcNAcylation					361:375	protein O-GlcNAcylation	353:375	protein O-GlcNAcylation	353:375	Genetic approaches in model organisms have revealed that protein O-GlcNAcylation is essential for early embryogenesis.
34907035	6	0	theme	cancer	1089:1094	arg1	cells					1096:1100	breast cancer cells	1082:1100	breast cancer cells	1082:1100	Decreased expression of CCL3L1 in lymphocytes not only decreased CCR5 expression in breast cancer cells, but also inhibited the membrane localization and activation of CCR5, thus blocking the migration and invasion of breast cancer cells in vitro.
34907035	6	1	theme	breast	948:953	arg1	cells					962:966	breast cancer cells	948:966	breast cancer cells	948:966	Decreased expression of CCL3L1 in lymphocytes not only decreased CCR5 expression in breast cancer cells, but also inhibited the membrane localization and activation of CCR5, thus blocking the migration and invasion of breast cancer cells in vitro.
34907035	6	2	dep	localization	1001:1012	arg1	the					988:990	the	988:990	the	988:990	Decreased expression of CCL3L1 in lymphocytes not only decreased CCR5 expression in breast cancer cells, but also inhibited the membrane localization and activation of CCR5, thus blocking the migration and invasion of breast cancer cells in vitro.
34907035	5	3	from	Ser448	695:700	arg1	O-GlcNAcylation					676:690	Blimp-1 O-GlcNAcylation	668:690	Blimp-1 O-GlcNAcylation at Ser448 and Ser472 in lymphocytes	668:726	It was found that Blimp-1 O-GlcNAcylation at Ser448 and Ser472 in lymphocytes promoted its nuclear localization, and blocked the bindings to three regions upstream of the ccl3l1 promoter to inhibit its expression.
34907035	4	4	from	lymphocytes	577:587	arg1	O-GlcNAcylation					503:517	O-GlcNAcylation	503:517	O-GlcNAcylation of B lymphocyte-induced maturation protein-1 (Blimp-1) in lymphocytes	503:587	Herein, we showed that O-GlcNAcylation of B lymphocyte-induced maturation protein-1 (Blimp-1) in lymphocytes inhibited the migration and invasion of breast cancer cells.
34907035	0	5	from	O-GlcNAcylation	0:14	arg1	Lymphocytes					30:40	Lymphocytes	30:40	Lymphocytes	30:40	O-GlcNAcylation of Blimp-1 in Lymphocytes Inhibits Its Transcriptional Function and Is Associated with Migration and Invasion of Breast Cancer Cells.
34907035	7	6	theme	new	1180:1182	arg1	target					1184:1189	a new target	1178:1189	a new target for the treatment of metastatic breast cancer	1178:1235	Therefore, O-GlcNAcylation of Blimp-1 in lymphocytes may serve as a new target for the treatment of metastatic breast cancer.
34907035	7	6	theme	new	1180:1182	arg1	O-GlcNAcylation					1123:1137	O-GlcNAcylation	1123:1137	O-GlcNAcylation of Blimp-1 in lymphocytes	1123:1163	Therefore, O-GlcNAcylation of Blimp-1 in lymphocytes may serve as a new target for the treatment of metastatic breast cancer.
34907035	5	7	from	O-GlcNAcylation	676:690	arg1	lymphocytes					716:726	lymphocytes	716:726	lymphocytes	716:726	It was found that Blimp-1 O-GlcNAcylation at Ser448 and Ser472 in lymphocytes promoted its nuclear localization, and blocked the bindings to three regions upstream of the ccl3l1 promoter to inhibit its expression.
34907035	8	8	dep	IMPLICATIONS	1238:1249	arg1	reveals					1262:1268	reveals	1262:1268	reveals a new mechanism by which the lymphatic system promotes breast cancer cell metastasis	1262:1353	IMPLICATIONS This study reveals a new mechanism by which the lymphatic system promotes breast cancer cell metastasis.
34907035	8	9	theme	lymphatic	1299:1307	arg1	system					1309:1314	the lymphatic system	1295:1314	the lymphatic system	1295:1314	IMPLICATIONS This study reveals a new mechanism by which the lymphatic system promotes breast cancer cell metastasis.
34907035	4	10	theme	breast	629:634	arg1	cells					643:647	breast cancer cells	629:647	breast cancer cells	629:647	Herein, we showed that O-GlcNAcylation of B lymphocyte-induced maturation protein-1 (Blimp-1) in lymphocytes inhibited the migration and invasion of breast cancer cells.
34907035	7	11	from	O-GlcNAcylation	1123:1137	arg1	lymphocytes					1153:1163	lymphocytes	1153:1163	lymphocytes	1153:1163	Therefore, O-GlcNAcylation of Blimp-1 in lymphocytes may serve as a new target for the treatment of metastatic breast cancer.
34907035	7	12	theme	metastatic	1212:1221	arg1	cancer					1230:1235	metastatic breast cancer	1212:1235	metastatic breast cancer	1212:1235	Therefore, O-GlcNAcylation of Blimp-1 in lymphocytes may serve as a new target for the treatment of metastatic breast cancer.
34907035	7	13	theme	Blimp-1	1142:1148	arg1	target					1184:1189	a new target	1178:1189	a new target for the treatment of metastatic breast cancer	1178:1235	Therefore, O-GlcNAcylation of Blimp-1 in lymphocytes may serve as a new target for the treatment of metastatic breast cancer.
34907035	7	13	theme	Blimp-1	1142:1148	arg1	O-GlcNAcylation					1123:1137	O-GlcNAcylation	1123:1137	O-GlcNAcylation of Blimp-1 in lymphocytes	1123:1163	Therefore, O-GlcNAcylation of Blimp-1 in lymphocytes may serve as a new target for the treatment of metastatic breast cancer.
34907035	8	14	theme	breast	1325:1330	arg1	metastasis					1344:1353	breast cancer cell metastasis	1325:1353	breast cancer cell metastasis	1325:1353	IMPLICATIONS This study reveals a new mechanism by which the lymphatic system promotes breast cancer cell metastasis.
34907035	4	15	theme	cells	643:647	arg1	invasion					617:624	invasion	617:624	invasion	617:624	Herein, we showed that O-GlcNAcylation of B lymphocyte-induced maturation protein-1 (Blimp-1) in lymphocytes inhibited the migration and invasion of breast cancer cells.
34907035	4	15	theme	cells	643:647	arg1	migration					603:611	migration	603:611	migration	603:611	Herein, we showed that O-GlcNAcylation of B lymphocyte-induced maturation protein-1 (Blimp-1) in lymphocytes inhibited the migration and invasion of breast cancer cells.
34907035	6	16	from	expression	874:883	arg1	lymphocytes					898:908	lymphocytes	898:908	lymphocytes	898:908	Decreased expression of CCL3L1 in lymphocytes not only decreased CCR5 expression in breast cancer cells, but also inhibited the membrane localization and activation of CCR5, thus blocking the migration and invasion of breast cancer cells in vitro.
34907035	6	17	theme	Decreased	864:872	arg1	expression					874:883	Decreased expression	864:883	Decreased expression of CCL3L1 in lymphocytes	864:908	Decreased expression of CCL3L1 in lymphocytes not only decreased CCR5 expression in breast cancer cells, but also inhibited the membrane localization and activation of CCR5, thus blocking the migration and invasion of breast cancer cells in vitro.
34907035	1	18	theme	important	180:188	arg1	feature					190:196	an important feature	177:196	an important feature of cancer	177:206	Lymphocyte infiltration is an important feature of cancer.
34907035	1	18	theme	important	180:188	arg1	infiltration					161:172	Lymphocyte infiltration	150:172	Lymphocyte infiltration	150:172	Lymphocyte infiltration is an important feature of cancer.
34907035	4	19	from	protein-1	554:562	arg1	lymphocytes					577:587	lymphocytes	577:587	lymphocytes	577:587	Herein, we showed that O-GlcNAcylation of B lymphocyte-induced maturation protein-1 (Blimp-1) in lymphocytes inhibited the migration and invasion of breast cancer cells.
34907035	6	20	dep	migration	1056:1064	arg1	the					1052:1054	the	1052:1054	the	1052:1054	Decreased expression of CCL3L1 in lymphocytes not only decreased CCR5 expression in breast cancer cells, but also inhibited the membrane localization and activation of CCR5, thus blocking the migration and invasion of breast cancer cells in vitro.
34907035	8	21	theme	cell	1339:1342	arg1	metastasis					1344:1353	breast cancer cell metastasis	1325:1353	breast cancer cell metastasis	1325:1353	IMPLICATIONS This study reveals a new mechanism by which the lymphatic system promotes breast cancer cell metastasis.
34907035	3	22	theme	heterogeneity	400:412	arg1	obstacle					436:443	a major obstacle	428:443	a major obstacle to the treatment of breast cancer	428:477	High heterogeneity metastasis is a major obstacle to the treatment of breast cancer.
34907035	3	22	theme	heterogeneity	400:412	arg1	metastasis					414:423	High heterogeneity metastasis	395:423	High heterogeneity metastasis	395:423	High heterogeneity metastasis is a major obstacle to the treatment of breast cancer.
34907035	4	23	theme	lymphocyte-induced	524:541	arg1	Blimp-1					565:571	Blimp-1	565:571	Blimp-1	565:571	Herein, we showed that O-GlcNAcylation of B lymphocyte-induced maturation protein-1 (Blimp-1) in lymphocytes inhibited the migration and invasion of breast cancer cells.
34907035	4	23	theme	lymphocyte-induced	524:541	arg1	protein-1					554:562	B lymphocyte-induced maturation protein-1	522:562	B lymphocyte-induced maturation protein-1 (Blimp-1) in lymphocytes	522:587	Herein, we showed that O-GlcNAcylation of B lymphocyte-induced maturation protein-1 (Blimp-1) in lymphocytes inhibited the migration and invasion of breast cancer cells.
34907035	4	24	from	O-GlcNAcylation	503:517	arg1	lymphocytes					577:587	lymphocytes	577:587	lymphocytes	577:587	Herein, we showed that O-GlcNAcylation of B lymphocyte-induced maturation protein-1 (Blimp-1) in lymphocytes inhibited the migration and invasion of breast cancer cells.
34907035	8	25	theme	cancer	1332:1337	arg1	metastasis					1344:1353	breast cancer cell metastasis	1325:1353	breast cancer cell metastasis	1325:1353	IMPLICATIONS This study reveals a new mechanism by which the lymphatic system promotes breast cancer cell metastasis.
34907035	5	26	theme	ccl3l1	821:826	arg1	promoter					828:835	the ccl3l1 promoter	817:835	the ccl3l1 promoter	817:835	It was found that Blimp-1 O-GlcNAcylation at Ser448 and Ser472 in lymphocytes promoted its nuclear localization, and blocked the bindings to three regions upstream of the ccl3l1 promoter to inhibit its expression.
34907035	4	27	theme	B	522:522	arg1	Blimp-1					565:571	Blimp-1	565:571	Blimp-1	565:571	Herein, we showed that O-GlcNAcylation of B lymphocyte-induced maturation protein-1 (Blimp-1) in lymphocytes inhibited the migration and invasion of breast cancer cells.
34907035	4	27	theme	B	522:522	arg1	protein-1					554:562	B lymphocyte-induced maturation protein-1	522:562	B lymphocyte-induced maturation protein-1 (Blimp-1) in lymphocytes	522:587	Herein, we showed that O-GlcNAcylation of B lymphocyte-induced maturation protein-1 (Blimp-1) in lymphocytes inhibited the migration and invasion of breast cancer cells.
34907035	0	28	theme	Breast	129:134	arg1	Cells					143:147	Breast Cancer Cells	129:147	Breast Cancer Cells	129:147	O-GlcNAcylation of Blimp-1 in Lymphocytes Inhibits Its Transcriptional Function and Is Associated with Migration and Invasion of Breast Cancer Cells.
34907035	2	29	dep	growth	333:338	arg1	the					329:331	the	329:331	the	329:331	There is a complex network of chemokines that influence the degree and phenotype of lymphocyte infiltration, as well as the growth, survival, migration, and angiogenesis of tumor cells.
34907035	1	30	theme	cancer	201:206	arg1	feature					190:196	an important feature	177:196	an important feature of cancer	177:206	Lymphocyte infiltration is an important feature of cancer.
34907035	1	30	theme	cancer	201:206	arg1	infiltration					161:172	Lymphocyte infiltration	150:172	Lymphocyte infiltration	150:172	Lymphocyte infiltration is an important feature of cancer.
34907035	0	31	theme	Blimp-1	19:25	arg1	O-GlcNAcylation					0:14	O-GlcNAcylation	0:14	O-GlcNAcylation of Blimp-1 in Lymphocytes	0:40	O-GlcNAcylation of Blimp-1 in Lymphocytes Inhibits Its Transcriptional Function and Is Associated with Migration and Invasion of Breast Cancer Cells.
34907035	4	32	theme	protein-1	554:562	arg1	O-GlcNAcylation					503:517	O-GlcNAcylation	503:517	O-GlcNAcylation of B lymphocyte-induced maturation protein-1 (Blimp-1) in lymphocytes	503:587	Herein, we showed that O-GlcNAcylation of B lymphocyte-induced maturation protein-1 (Blimp-1) in lymphocytes inhibited the migration and invasion of breast cancer cells.
34907035	2	33	theme	lymphocyte	293:302	arg1	infiltration					304:315	lymphocyte infiltration	293:315	lymphocyte infiltration	293:315	There is a complex network of chemokines that influence the degree and phenotype of lymphocyte infiltration, as well as the growth, survival, migration, and angiogenesis of tumor cells.
34907035	6	34	theme	CCR5	1032:1035	arg1	activation					1018:1027	activation	1018:1027	activation	1018:1027	Decreased expression of CCL3L1 in lymphocytes not only decreased CCR5 expression in breast cancer cells, but also inhibited the membrane localization and activation of CCR5, thus blocking the migration and invasion of breast cancer cells in vitro.
34907035	6	34	theme	CCR5	1032:1035	arg1	localization					1001:1012	membrane localization	992:1012	membrane localization	992:1012	Decreased expression of CCL3L1 in lymphocytes not only decreased CCR5 expression in breast cancer cells, but also inhibited the membrane localization and activation of CCR5, thus blocking the migration and invasion of breast cancer cells in vitro.
34907035	4	35	theme	maturation	543:552	arg1	Blimp-1					565:571	Blimp-1	565:571	Blimp-1	565:571	Herein, we showed that O-GlcNAcylation of B lymphocyte-induced maturation protein-1 (Blimp-1) in lymphocytes inhibited the migration and invasion of breast cancer cells.
34907035	4	35	theme	maturation	543:552	arg1	protein-1					554:562	B lymphocyte-induced maturation protein-1	522:562	B lymphocyte-induced maturation protein-1 (Blimp-1) in lymphocytes	522:587	Herein, we showed that O-GlcNAcylation of B lymphocyte-induced maturation protein-1 (Blimp-1) in lymphocytes inhibited the migration and invasion of breast cancer cells.
34907035	0	36	theme	Cells	143:147	arg1	Migration					103:111	Migration	103:111	Migration	103:111	O-GlcNAcylation of Blimp-1 in Lymphocytes Inhibits Its Transcriptional Function and Is Associated with Migration and Invasion of Breast Cancer Cells.
34907035	0	36	theme	Cells	143:147	arg1	Invasion					117:124	Invasion	117:124	Invasion	117:124	O-GlcNAcylation of Blimp-1 in Lymphocytes Inhibits Its Transcriptional Function and Is Associated with Migration and Invasion of Breast Cancer Cells.
34907035	2	37	theme	cells	388:392	arg1	angiogenesis					366:377	angiogenesis	366:377	angiogenesis	366:377	There is a complex network of chemokines that influence the degree and phenotype of lymphocyte infiltration, as well as the growth, survival, migration, and angiogenesis of tumor cells.
34907035	2	37	theme	cells	388:392	arg1	survival					341:348	survival	341:348	survival	341:348	There is a complex network of chemokines that influence the degree and phenotype of lymphocyte infiltration, as well as the growth, survival, migration, and angiogenesis of tumor cells.
34907035	2	37	theme	cells	388:392	arg1	degree					269:274	degree	269:274	degree	269:274	There is a complex network of chemokines that influence the degree and phenotype of lymphocyte infiltration, as well as the growth, survival, migration, and angiogenesis of tumor cells.
34907035	2	37	theme	cells	388:392	arg1	migration					351:359	migration	351:359	migration	351:359	There is a complex network of chemokines that influence the degree and phenotype of lymphocyte infiltration, as well as the growth, survival, migration, and angiogenesis of tumor cells.
34907035	2	37	theme	cells	388:392	arg1	phenotype					280:288	phenotype	280:288	phenotype	280:288	There is a complex network of chemokines that influence the degree and phenotype of lymphocyte infiltration, as well as the growth, survival, migration, and angiogenesis of tumor cells.
34907035	2	37	theme	cells	388:392	arg1	growth					333:338	growth	333:338	growth	333:338	There is a complex network of chemokines that influence the degree and phenotype of lymphocyte infiltration, as well as the growth, survival, migration, and angiogenesis of tumor cells.
34907035	8	38	theme	new	1272:1274	arg1	mechanism					1276:1284	a new mechanism	1270:1284	a new mechanism by which the lymphatic system promotes breast cancer cell metastasis	1270:1353	IMPLICATIONS This study reveals a new mechanism by which the lymphatic system promotes breast cancer cell metastasis.
34907035	3	39	theme	major	430:434	arg1	obstacle					436:443	a major obstacle	428:443	a major obstacle to the treatment of breast cancer	428:477	High heterogeneity metastasis is a major obstacle to the treatment of breast cancer.
34907035	3	39	theme	major	430:434	arg1	metastasis					414:423	High heterogeneity metastasis	395:423	High heterogeneity metastasis	395:423	High heterogeneity metastasis is a major obstacle to the treatment of breast cancer.
34907035	3	40	theme	High	395:398	arg1	obstacle					436:443	a major obstacle	428:443	a major obstacle to the treatment of breast cancer	428:477	High heterogeneity metastasis is a major obstacle to the treatment of breast cancer.
34907035	3	40	theme	High	395:398	arg1	metastasis					414:423	High heterogeneity metastasis	395:423	High heterogeneity metastasis	395:423	High heterogeneity metastasis is a major obstacle to the treatment of breast cancer.
34907035	0	41	theme	Cancer	136:141	arg1	Cells					143:147	Breast Cancer Cells	129:147	Breast Cancer Cells	129:147	O-GlcNAcylation of Blimp-1 in Lymphocytes Inhibits Its Transcriptional Function and Is Associated with Migration and Invasion of Breast Cancer Cells.
34907035	5	42	from	Ser472	706:711	arg1	O-GlcNAcylation					676:690	Blimp-1 O-GlcNAcylation	668:690	Blimp-1 O-GlcNAcylation at Ser448 and Ser472 in lymphocytes	668:726	It was found that Blimp-1 O-GlcNAcylation at Ser448 and Ser472 in lymphocytes promoted its nuclear localization, and blocked the bindings to three regions upstream of the ccl3l1 promoter to inhibit its expression.
34907035	2	43	theme	tumor	382:386	arg1	cells					388:392	tumor cells	382:392	tumor cells	382:392	There is a complex network of chemokines that influence the degree and phenotype of lymphocyte infiltration, as well as the growth, survival, migration, and angiogenesis of tumor cells.
34907035	0	44	theme	Transcriptional	55:69	arg1	Function					71:78	Its Transcriptional Function	51:78	Its Transcriptional Function	51:78	O-GlcNAcylation of Blimp-1 in Lymphocytes Inhibits Its Transcriptional Function and Is Associated with Migration and Invasion of Breast Cancer Cells.
34907035	6	45	theme	CCR5	929:932	arg1	expression					934:943	CCR5 expression	929:943	CCR5 expression in breast cancer cells	929:966	Decreased expression of CCL3L1 in lymphocytes not only decreased CCR5 expression in breast cancer cells, but also inhibited the membrane localization and activation of CCR5, thus blocking the migration and invasion of breast cancer cells in vitro.
34907035	6	46	theme	cancer	955:960	arg1	cells					962:966	breast cancer cells	948:966	breast cancer cells	948:966	Decreased expression of CCL3L1 in lymphocytes not only decreased CCR5 expression in breast cancer cells, but also inhibited the membrane localization and activation of CCR5, thus blocking the migration and invasion of breast cancer cells in vitro.
34907035	2	47	theme	complex	220:226	arg1	network					228:234	a complex network	218:234	a complex network of chemokines that influence the degree and phenotype of lymphocyte infiltration, as well as the growth, survival, migration, and angiogenesis of tumor cells	218:392	There is a complex network of chemokines that influence the degree and phenotype of lymphocyte infiltration, as well as the growth, survival, migration, and angiogenesis of tumor cells.
34907035	3	48	theme	breast	465:470	arg1	cancer					472:477	breast cancer	465:477	breast cancer	465:477	High heterogeneity metastasis is a major obstacle to the treatment of breast cancer.
34907035	6	49	theme	CCL3L1	888:893	arg1	expression					874:883	Decreased expression	864:883	Decreased expression of CCL3L1 in lymphocytes	864:908	Decreased expression of CCL3L1 in lymphocytes not only decreased CCR5 expression in breast cancer cells, but also inhibited the membrane localization and activation of CCR5, thus blocking the migration and invasion of breast cancer cells in vitro.
34907035	4	50	dep	migration	603:611	arg1	the					599:601	the	599:601	the	599:601	Herein, we showed that O-GlcNAcylation of B lymphocyte-induced maturation protein-1 (Blimp-1) in lymphocytes inhibited the migration and invasion of breast cancer cells.
34907035	3	51	theme	cancer	472:477	arg1	treatment					452:460	the treatment	448:460	the treatment of breast cancer	448:477	High heterogeneity metastasis is a major obstacle to the treatment of breast cancer.
34907035	7	52	theme	breast	1223:1228	arg1	cancer					1230:1235	metastatic breast cancer	1212:1235	metastatic breast cancer	1212:1235	Therefore, O-GlcNAcylation of Blimp-1 in lymphocytes may serve as a new target for the treatment of metastatic breast cancer.
34907035	6	53	from	expression	934:943	arg1	cells					962:966	breast cancer cells	948:966	breast cancer cells	948:966	Decreased expression of CCL3L1 in lymphocytes not only decreased CCR5 expression in breast cancer cells, but also inhibited the membrane localization and activation of CCR5, thus blocking the migration and invasion of breast cancer cells in vitro.
34907035	6	54	theme	cells	1096:1100	arg1	invasion					1070:1077	invasion	1070:1077	invasion	1070:1077	Decreased expression of CCL3L1 in lymphocytes not only decreased CCR5 expression in breast cancer cells, but also inhibited the membrane localization and activation of CCR5, thus blocking the migration and invasion of breast cancer cells in vitro.
34907035	6	54	theme	cells	1096:1100	arg1	migration					1056:1064	migration	1056:1064	migration	1056:1064	Decreased expression of CCL3L1 in lymphocytes not only decreased CCR5 expression in breast cancer cells, but also inhibited the membrane localization and activation of CCR5, thus blocking the migration and invasion of breast cancer cells in vitro.
34907035	2	55	theme	infiltration	304:315	arg1	angiogenesis					366:377	angiogenesis	366:377	angiogenesis	366:377	There is a complex network of chemokines that influence the degree and phenotype of lymphocyte infiltration, as well as the growth, survival, migration, and angiogenesis of tumor cells.
34907035	2	55	theme	infiltration	304:315	arg1	survival					341:348	survival	341:348	survival	341:348	There is a complex network of chemokines that influence the degree and phenotype of lymphocyte infiltration, as well as the growth, survival, migration, and angiogenesis of tumor cells.
34907035	2	55	theme	infiltration	304:315	arg1	degree					269:274	degree	269:274	degree	269:274	There is a complex network of chemokines that influence the degree and phenotype of lymphocyte infiltration, as well as the growth, survival, migration, and angiogenesis of tumor cells.
34907035	2	55	theme	infiltration	304:315	arg1	migration					351:359	migration	351:359	migration	351:359	There is a complex network of chemokines that influence the degree and phenotype of lymphocyte infiltration, as well as the growth, survival, migration, and angiogenesis of tumor cells.
34907035	2	55	theme	infiltration	304:315	arg1	phenotype					280:288	phenotype	280:288	phenotype	280:288	There is a complex network of chemokines that influence the degree and phenotype of lymphocyte infiltration, as well as the growth, survival, migration, and angiogenesis of tumor cells.
34907035	2	55	theme	infiltration	304:315	arg1	growth					333:338	growth	333:338	growth	333:338	There is a complex network of chemokines that influence the degree and phenotype of lymphocyte infiltration, as well as the growth, survival, migration, and angiogenesis of tumor cells.
34907035	5	56	theme	Blimp-1	668:674	arg1	O-GlcNAcylation					676:690	Blimp-1 O-GlcNAcylation	668:690	Blimp-1 O-GlcNAcylation at Ser448 and Ser472 in lymphocytes	668:726	It was found that Blimp-1 O-GlcNAcylation at Ser448 and Ser472 in lymphocytes promoted its nuclear localization, and blocked the bindings to three regions upstream of the ccl3l1 promoter to inhibit its expression.
34907035	1	57	theme	Lymphocyte	150:159	arg1	feature					190:196	an important feature	177:196	an important feature of cancer	177:206	Lymphocyte infiltration is an important feature of cancer.
34907035	1	57	theme	Lymphocyte	150:159	arg1	infiltration					161:172	Lymphocyte infiltration	150:172	Lymphocyte infiltration	150:172	Lymphocyte infiltration is an important feature of cancer.
34907035	7	58	theme	cancer	1230:1235	arg1	treatment					1199:1207	the treatment	1195:1207	the treatment of metastatic breast cancer	1195:1235	Therefore, O-GlcNAcylation of Blimp-1 in lymphocytes may serve as a new target for the treatment of metastatic breast cancer.
34907035	6	59	theme	breast	1082:1087	arg1	cells					1096:1100	breast cancer cells	1082:1100	breast cancer cells	1082:1100	Decreased expression of CCL3L1 in lymphocytes not only decreased CCR5 expression in breast cancer cells, but also inhibited the membrane localization and activation of CCR5, thus blocking the migration and invasion of breast cancer cells in vitro.
34907035	4	60	theme	cancer	636:641	arg1	cells					643:647	breast cancer cells	629:647	breast cancer cells	629:647	Herein, we showed that O-GlcNAcylation of B lymphocyte-induced maturation protein-1 (Blimp-1) in lymphocytes inhibited the migration and invasion of breast cancer cells.
34907035	6	61	theme	membrane	992:999	arg1	localization					1001:1012	membrane localization	992:1012	membrane localization	992:1012	Decreased expression of CCL3L1 in lymphocytes not only decreased CCR5 expression in breast cancer cells, but also inhibited the membrane localization and activation of CCR5, thus blocking the migration and invasion of breast cancer cells in vitro.
34907035	5	62	theme	nuclear	741:747	arg1	localization					749:760	its nuclear localization	737:760	its nuclear localization	737:760	It was found that Blimp-1 O-GlcNAcylation at Ser448 and Ser472 in lymphocytes promoted its nuclear localization, and blocked the bindings to three regions upstream of the ccl3l1 promoter to inhibit its expression.
34907035	2	63	theme	chemokines	239:248	arg1	network					228:234	a complex network	218:234	a complex network of chemokines that influence the degree and phenotype of lymphocyte infiltration, as well as the growth, survival, migration, and angiogenesis of tumor cells	218:392	There is a complex network of chemokines that influence the degree and phenotype of lymphocyte infiltration, as well as the growth, survival, migration, and angiogenesis of tumor cells.
34907035	2	64	dep	degree	269:274	arg1	the					265:267	the	265:267	the	265:267	There is a complex network of chemokines that influence the degree and phenotype of lymphocyte infiltration, as well as the growth, survival, migration, and angiogenesis of tumor cells.
28580691	3	0	theme	activity-based	268:281	arg1	analysis					294:301	an activity-based microarray analysis	265:301	an activity-based microarray analysis of 256 tyrosine kinase peptide substrates	265:343	With an activity-based microarray analysis of 256 tyrosine kinase peptide substrates, we found that phosphorylation of six peptides by Jak2 inhibits their subsequent O-GlcNAcylation.
28580691	6	1	attach	presence	648:655	arg1	Tyr364					675:680	Tyr364	675:680	Tyr364 of ZO3_357_371	675:695	Kinetic results show that the presence of a phosphate at Tyr364 of ZO3_357_371 slows the O-GlcNAcylation of nearby Ser369, while the presence of a GlcNAc at Ser369 has no significant effect on the phosphorylation of this peptide at Tyr364.
28580691	6	1	attach	presence	648:655	arg2	phosphate					662:670	a phosphate	660:670	a phosphate	660:670	Kinetic results show that the presence of a phosphate at Tyr364 of ZO3_357_371 slows the O-GlcNAcylation of nearby Ser369, while the presence of a GlcNAc at Ser369 has no significant effect on the phosphorylation of this peptide at Tyr364.
28580691	6	2	from	Ser369	775:780	arg1	presence					751:758	the presence	747:758	the presence of a GlcNAc at Ser369	747:780	Kinetic results show that the presence of a phosphate at Tyr364 of ZO3_357_371 slows the O-GlcNAcylation of nearby Ser369, while the presence of a GlcNAc at Ser369 has no significant effect on the phosphorylation of this peptide at Tyr364.
28580691	7	3	theme	cellular	917:924	arg1	control					936:942	cellular signaling control	917:942	cellular signaling control by cross-talk	917:956	These findings provide a glimpse into the new paradigm for cellular signaling control by cross-talk.
28580691	3	4	theme	microarray	283:292	arg1	analysis					294:301	an activity-based microarray analysis	265:301	an activity-based microarray analysis of 256 tyrosine kinase peptide substrates	265:343	With an activity-based microarray analysis of 256 tyrosine kinase peptide substrates, we found that phosphorylation of six peptides by Jak2 inhibits their subsequent O-GlcNAcylation.
28580691	7	5	theme	new	900:902	arg1	paradigm					904:911	the new paradigm	896:911	the new paradigm for cellular signaling control by cross-talk	896:956	These findings provide a glimpse into the new paradigm for cellular signaling control by cross-talk.
28580691	6	6	theme	peptide	839:845	arg1	phosphorylation					815:829	the phosphorylation	811:829	the phosphorylation of this peptide at Tyr364	811:855	Kinetic results show that the presence of a phosphate at Tyr364 of ZO3_357_371 slows the O-GlcNAcylation of nearby Ser369, while the presence of a GlcNAc at Ser369 has no significant effect on the phosphorylation of this peptide at Tyr364.
28580691	6	7	theme	phosphate	662:670	arg1	presence					648:655	the presence	644:655	the presence of a phosphate at Tyr364 of ZO3_357_371	644:695	Kinetic results show that the presence of a phosphate at Tyr364 of ZO3_357_371 slows the O-GlcNAcylation of nearby Ser369, while the presence of a GlcNAc at Ser369 has no significant effect on the phosphorylation of this peptide at Tyr364.
28580691	3	8	theme	subsequent	415:424	arg1	O-GlcNAcylation					426:440	their subsequent O-GlcNAcylation	409:440	their subsequent O-GlcNAcylation	409:440	With an activity-based microarray analysis of 256 tyrosine kinase peptide substrates, we found that phosphorylation of six peptides by Jak2 inhibits their subsequent O-GlcNAcylation.
28580691	4	9	theme	detectable	475:484	arg1	effect					486:491	no detectable effect	472:491	no detectable effect	472:491	However, O-GlcNAcylation has no detectable effect on their subsequent phosphorylation.
28580691	6	10	attach	presence	751:758	arg1	Ser369					775:780	Ser369	775:780	Ser369	775:780	Kinetic results show that the presence of a phosphate at Tyr364 of ZO3_357_371 slows the O-GlcNAcylation of nearby Ser369, while the presence of a GlcNAc at Ser369 has no significant effect on the phosphorylation of this peptide at Tyr364.
28580691	6	10	attach	presence	751:758	arg2	GlcNAc					765:770	a GlcNAc	763:770	a GlcNAc	763:770	Kinetic results show that the presence of a phosphate at Tyr364 of ZO3_357_371 slows the O-GlcNAcylation of nearby Ser369, while the presence of a GlcNAc at Ser369 has no significant effect on the phosphorylation of this peptide at Tyr364.
28580691	6	11	theme	Kinetic	618:624	arg1	results					626:632	Kinetic results	618:632	Kinetic results	618:632	Kinetic results show that the presence of a phosphate at Tyr364 of ZO3_357_371 slows the O-GlcNAcylation of nearby Ser369, while the presence of a GlcNAc at Ser369 has no significant effect on the phosphorylation of this peptide at Tyr364.
28580691	2	12	theme	few	170:172	arg1	reports					174:180	A few reports	168:180	A few reports	168:180	A few reports noted that O-GlcNAcylation exhibits cross-talk with tyrosine phosphorylation.
28580691	3	13	theme	tyrosine	310:317	arg1	substrates					334:343	256 tyrosine kinase peptide substrates	306:343	256 tyrosine kinase peptide substrates	306:343	With an activity-based microarray analysis of 256 tyrosine kinase peptide substrates, we found that phosphorylation of six peptides by Jak2 inhibits their subsequent O-GlcNAcylation.
28580691	0	14	theme	microarray	8:17	arg1	analysis					19:26	Peptide microarray analysis	0:26	Peptide microarray analysis of the cross-talk between O-GlcNAcylation and tyrosine phosphorylation	0:97	Peptide microarray analysis of the cross-talk between O-GlcNAcylation and tyrosine phosphorylation.
28580691	3	15	theme	peptides	383:390	arg1	phosphorylation					360:374	phosphorylation	360:374	phosphorylation of six peptides by Jak2	360:398	With an activity-based microarray analysis of 256 tyrosine kinase peptide substrates, we found that phosphorylation of six peptides by Jak2 inhibits their subsequent O-GlcNAcylation.
28580691	6	16	from	Tyr364	850:855	arg1	phosphorylation					815:829	the phosphorylation	811:829	the phosphorylation of this peptide at Tyr364	811:855	Kinetic results show that the presence of a phosphate at Tyr364 of ZO3_357_371 slows the O-GlcNAcylation of nearby Ser369, while the presence of a GlcNAc at Ser369 has no significant effect on the phosphorylation of this peptide at Tyr364.
28580691	0	17	theme	Peptide	0:6	arg1	analysis					19:26	Peptide microarray analysis	0:26	Peptide microarray analysis of the cross-talk between O-GlcNAcylation and tyrosine phosphorylation	0:97	Peptide microarray analysis of the cross-talk between O-GlcNAcylation and tyrosine phosphorylation.
28580691	5	18	attach	derived	564:570	arg2	peptide					541:547	A specific peptide	530:547	A specific peptide (ZO3_357_371)	530:561	A specific peptide (ZO3_357_371), derived from the ZO-3 protein, was studied in detail.
28580691	5	18	attach	derived	564:570	arg1	protein					586:592	the ZO-3 protein	577:592	the ZO-3 protein	577:592	A specific peptide (ZO3_357_371), derived from the ZO-3 protein, was studied in detail.
28580691	5	18	attach	derived	564:570	arg2	ZO3_357_371					550:560	ZO3_357_371	550:560	ZO3_357_371	550:560	A specific peptide (ZO3_357_371), derived from the ZO-3 protein, was studied in detail.
28580691	1	19	theme	proteins	119:126	arg1	O-GlcNAcylation					100:114	O-GlcNAcylation	100:114	O-GlcNAcylation of proteins	100:126	O-GlcNAcylation of proteins regulates important cellular processes.
28580691	6	20	theme	Ser369	733:738	arg1	O-GlcNAcylation					707:721	the O-GlcNAcylation	703:721	the O-GlcNAcylation of nearby Ser369	703:738	Kinetic results show that the presence of a phosphate at Tyr364 of ZO3_357_371 slows the O-GlcNAcylation of nearby Ser369, while the presence of a GlcNAc at Ser369 has no significant effect on the phosphorylation of this peptide at Tyr364.
28580691	6	21	theme	nearby	726:731	arg1	Ser369					733:738	nearby Ser369	726:738	nearby Ser369	726:738	Kinetic results show that the presence of a phosphate at Tyr364 of ZO3_357_371 slows the O-GlcNAcylation of nearby Ser369, while the presence of a GlcNAc at Ser369 has no significant effect on the phosphorylation of this peptide at Tyr364.
28580691	0	22	theme	cross-talk	35:44	arg1	analysis					19:26	Peptide microarray analysis	0:26	Peptide microarray analysis of the cross-talk between O-GlcNAcylation and tyrosine phosphorylation	0:97	Peptide microarray analysis of the cross-talk between O-GlcNAcylation and tyrosine phosphorylation.
28580691	3	23	theme	kinase	319:324	arg1	substrates					334:343	256 tyrosine kinase peptide substrates	306:343	256 tyrosine kinase peptide substrates	306:343	With an activity-based microarray analysis of 256 tyrosine kinase peptide substrates, we found that phosphorylation of six peptides by Jak2 inhibits their subsequent O-GlcNAcylation.
28580691	6	24	theme	ZO3_357_371	685:695	arg1	Tyr364					675:680	Tyr364	675:680	Tyr364 of ZO3_357_371	675:695	Kinetic results show that the presence of a phosphate at Tyr364 of ZO3_357_371 slows the O-GlcNAcylation of nearby Ser369, while the presence of a GlcNAc at Ser369 has no significant effect on the phosphorylation of this peptide at Tyr364.
28580691	3	25	theme	peptide	326:332	arg1	substrates					334:343	256 tyrosine kinase peptide substrates	306:343	256 tyrosine kinase peptide substrates	306:343	With an activity-based microarray analysis of 256 tyrosine kinase peptide substrates, we found that phosphorylation of six peptides by Jak2 inhibits their subsequent O-GlcNAcylation.
28580691	6	26	theme	significant	789:799	arg1	effect					801:806	no significant effect	786:806	no significant effect	786:806	Kinetic results show that the presence of a phosphate at Tyr364 of ZO3_357_371 slows the O-GlcNAcylation of nearby Ser369, while the presence of a GlcNAc at Ser369 has no significant effect on the phosphorylation of this peptide at Tyr364.
28580691	1	27	theme	important	138:146	arg1	processes					157:165	important cellular processes	138:165	important cellular processes	138:165	O-GlcNAcylation of proteins regulates important cellular processes.
28580691	4	28	contain	has	468:470	arg2	effect					486:491	no detectable effect	472:491	no detectable effect	472:491	However, O-GlcNAcylation has no detectable effect on their subsequent phosphorylation.
28580691	4	28	contain	has	468:470	arg1	O-GlcNAcylation					452:466	O-GlcNAcylation	452:466	O-GlcNAcylation	452:466	However, O-GlcNAcylation has no detectable effect on their subsequent phosphorylation.
28580691	3	29	theme	substrates	334:343	arg1	analysis					294:301	an activity-based microarray analysis	265:301	an activity-based microarray analysis of 256 tyrosine kinase peptide substrates	265:343	With an activity-based microarray analysis of 256 tyrosine kinase peptide substrates, we found that phosphorylation of six peptides by Jak2 inhibits their subsequent O-GlcNAcylation.
28580691	1	30	theme	cellular	148:155	arg1	processes					157:165	important cellular processes	138:165	important cellular processes	138:165	O-GlcNAcylation of proteins regulates important cellular processes.
28580691	2	31	with	cross-talk	218:227	arg1	phosphorylation					243:257	tyrosine phosphorylation	234:257	tyrosine phosphorylation	234:257	A few reports noted that O-GlcNAcylation exhibits cross-talk with tyrosine phosphorylation.
28580691	4	32	theme	subsequent	502:511	arg1	phosphorylation					513:527	their subsequent phosphorylation	496:527	their subsequent phosphorylation	496:527	However, O-GlcNAcylation has no detectable effect on their subsequent phosphorylation.
28580691	2	33	theme	tyrosine	234:241	arg1	phosphorylation					243:257	tyrosine phosphorylation	234:257	tyrosine phosphorylation	234:257	A few reports noted that O-GlcNAcylation exhibits cross-talk with tyrosine phosphorylation.
28580691	5	34	theme	ZO-3	581:584	arg1	protein					586:592	the ZO-3 protein	577:592	the ZO-3 protein	577:592	A specific peptide (ZO3_357_371), derived from the ZO-3 protein, was studied in detail.
28580691	7	35	theme	signaling	926:934	arg1	control					936:942	cellular signaling control	917:942	cellular signaling control by cross-talk	917:956	These findings provide a glimpse into the new paradigm for cellular signaling control by cross-talk.
28580691	0	36	theme	tyrosine	74:81	arg1	phosphorylation					83:97	tyrosine phosphorylation	74:97	tyrosine phosphorylation	74:97	Peptide microarray analysis of the cross-talk between O-GlcNAcylation and tyrosine phosphorylation.
28580691	5	37	theme	specific	532:539	arg1	ZO3_357_371					550:560	ZO3_357_371	550:560	ZO3_357_371	550:560	A specific peptide (ZO3_357_371), derived from the ZO-3 protein, was studied in detail.
28580691	5	37	theme	specific	532:539	arg1	peptide					541:547	A specific peptide	530:547	A specific peptide (ZO3_357_371)	530:561	A specific peptide (ZO3_357_371), derived from the ZO-3 protein, was studied in detail.
28580691	6	38	from	Tyr364	675:680	arg1	presence					648:655	the presence	644:655	the presence of a phosphate at Tyr364 of ZO3_357_371	644:695	Kinetic results show that the presence of a phosphate at Tyr364 of ZO3_357_371 slows the O-GlcNAcylation of nearby Ser369, while the presence of a GlcNAc at Ser369 has no significant effect on the phosphorylation of this peptide at Tyr364.
28580691	6	39	theme	GlcNAc	765:770	arg1	presence					751:758	the presence	747:758	the presence of a GlcNAc at Ser369	747:780	Kinetic results show that the presence of a phosphate at Tyr364 of ZO3_357_371 slows the O-GlcNAcylation of nearby Ser369, while the presence of a GlcNAc at Ser369 has no significant effect on the phosphorylation of this peptide at Tyr364.
28580691	6	40	contain	has	782:784	arg2	effect					801:806	no significant effect	786:806	no significant effect	786:806	Kinetic results show that the presence of a phosphate at Tyr364 of ZO3_357_371 slows the O-GlcNAcylation of nearby Ser369, while the presence of a GlcNAc at Ser369 has no significant effect on the phosphorylation of this peptide at Tyr364.
28580691	6	40	contain	has	782:784	arg1	presence					751:758	the presence	747:758	the presence of a GlcNAc at Ser369	747:780	Kinetic results show that the presence of a phosphate at Tyr364 of ZO3_357_371 slows the O-GlcNAcylation of nearby Ser369, while the presence of a GlcNAc at Ser369 has no significant effect on the phosphorylation of this peptide at Tyr364.
20959806	5	0	theme	cellular	890:897	arg1	metabolism					907:916	cellular glucose metabolism	890:916	cellular glucose metabolism	890:916	Thus, dynamic reciprocal O-phosphorylation and O-GlcNAc modification of Snail1 constitute a molecular link between cellular glucose metabolism and the control of EMT.
20959806	2	1	theme	programme	385:393	arg1	E-cadherin					307:316	E-cadherin	307:316	E-cadherin	307:316	O-phosphorylation of serine by glycogen synthase kinase-3β on Snail1, a transcriptional repressor of E-cadherin and a key regulator of the epithelial-mesenchymal transition (EMT) programme, results in its proteasomal degradation.
20959806	2	1	theme	programme	385:393	arg1	regulator					328:336	a key regulator	322:336	a key regulator of the epithelial-mesenchymal transition (EMT) programme	322:393	O-phosphorylation of serine by glycogen synthase kinase-3β on Snail1, a transcriptional repressor of E-cadherin and a key regulator of the epithelial-mesenchymal transition (EMT) programme, results in its proteasomal degradation.
20959806	4	2	theme	Hyperglycaemic	640:653	arg1	condition					655:663	Hyperglycaemic condition	640:663	Hyperglycaemic condition	640:663	Hyperglycaemic condition enhances O-GlcNAc modification and initiates EMT by transcriptional suppression of E-cadherin through Snail1.
20959806	2	3	theme	key	324:326	arg1	regulator					328:336	a key regulator	322:336	a key regulator of the epithelial-mesenchymal transition (EMT) programme	322:393	O-phosphorylation of serine by glycogen synthase kinase-3β on Snail1, a transcriptional repressor of E-cadherin and a key regulator of the epithelial-mesenchymal transition (EMT) programme, results in its proteasomal degradation.
20959806	3	4	theme	mRNA	623:626	arg1	expression					628:637	E-cadherin mRNA expression	612:637	E-cadherin mRNA expression	612:637	We show that by suppressing O-phosphorylation-mediated degradation, O-GlcNAc at serine112 stabilizes Snail1 and thus increases its repressor function, which in turn attenuates E-cadherin mRNA expression.
20959806	4	5	theme	O-GlcNAc	674:681	arg1	modification					683:694	O-GlcNAc modification	674:694	O-GlcNAc modification	674:694	Hyperglycaemic condition enhances O-GlcNAc modification and initiates EMT by transcriptional suppression of E-cadherin through Snail1.
20959806	5	6	theme	Snail1	847:852	arg1	O-phosphorylation					800:816	dynamic reciprocal O-phosphorylation	781:816	dynamic reciprocal O-phosphorylation	781:816	Thus, dynamic reciprocal O-phosphorylation and O-GlcNAc modification of Snail1 constitute a molecular link between cellular glucose metabolism and the control of EMT.
20959806	5	6	theme	Snail1	847:852	arg1	modification					831:842	O-GlcNAc modification	822:842	O-GlcNAc modification of Snail1	822:852	Thus, dynamic reciprocal O-phosphorylation and O-GlcNAc modification of Snail1 constitute a molecular link between cellular glucose metabolism and the control of EMT.
20959806	2	7	from	synthase	246:253	arg1	Snail1					268:273	Snail1	268:273	Snail1	268:273	O-phosphorylation of serine by glycogen synthase kinase-3β on Snail1, a transcriptional repressor of E-cadherin and a key regulator of the epithelial-mesenchymal transition (EMT) programme, results in its proteasomal degradation.
20959806	2	7	from	synthase	246:253	arg1	repressor					294:302	a transcriptional repressor	276:302	a transcriptional repressor of E-cadherin and a key regulator of the epithelial-mesenchymal transition (EMT) programme	276:393	O-phosphorylation of serine by glycogen synthase kinase-3β on Snail1, a transcriptional repressor of E-cadherin and a key regulator of the epithelial-mesenchymal transition (EMT) programme, results in its proteasomal degradation.
20959806	1	8	theme	Protein	75:81	arg1	O-phosphorylation					83:99	Protein O-phosphorylation	75:99	Protein O-phosphorylation	75:99	Protein O-phosphorylation often occurs reciprocally with O-GlcNAc modification and represents a regulatory principle for proteins.
20959806	2	9	theme	E-cadherin	307:316	arg1	Snail1					268:273	Snail1	268:273	Snail1	268:273	O-phosphorylation of serine by glycogen synthase kinase-3β on Snail1, a transcriptional repressor of E-cadherin and a key regulator of the epithelial-mesenchymal transition (EMT) programme, results in its proteasomal degradation.
20959806	2	9	theme	E-cadherin	307:316	arg1	repressor					294:302	a transcriptional repressor	276:302	a transcriptional repressor of E-cadherin and a key regulator of the epithelial-mesenchymal transition (EMT) programme	276:393	O-phosphorylation of serine by glycogen synthase kinase-3β on Snail1, a transcriptional repressor of E-cadherin and a key regulator of the epithelial-mesenchymal transition (EMT) programme, results in its proteasomal degradation.
20959806	4	10	theme	E-cadherin	748:757	arg1	suppression					733:743	transcriptional suppression	717:743	transcriptional suppression of E-cadherin through Snail1	717:772	Hyperglycaemic condition enhances O-GlcNAc modification and initiates EMT by transcriptional suppression of E-cadherin through Snail1.
20959806	2	11	theme	epithelial-mesenchymal	345:366	arg1	EMT					380:382	EMT	380:382	EMT	380:382	O-phosphorylation of serine by glycogen synthase kinase-3β on Snail1, a transcriptional repressor of E-cadherin and a key regulator of the epithelial-mesenchymal transition (EMT) programme, results in its proteasomal degradation.
20959806	2	11	theme	epithelial-mesenchymal	345:366	arg1	transition					368:377	the epithelial-mesenchymal transition	341:377	the epithelial-mesenchymal transition (EMT) programme	341:393	O-phosphorylation of serine by glycogen synthase kinase-3β on Snail1, a transcriptional repressor of E-cadherin and a key regulator of the epithelial-mesenchymal transition (EMT) programme, results in its proteasomal degradation.
20959806	2	12	theme	proteasomal	411:421	arg1	degradation					423:433	its proteasomal degradation	407:433	its proteasomal degradation	407:433	O-phosphorylation of serine by glycogen synthase kinase-3β on Snail1, a transcriptional repressor of E-cadherin and a key regulator of the epithelial-mesenchymal transition (EMT) programme, results in its proteasomal degradation.
20959806	3	13	theme	O-phosphorylation-mediated	464:489	arg1	degradation					491:501	O-phosphorylation-mediated degradation	464:501	O-phosphorylation-mediated degradation	464:501	We show that by suppressing O-phosphorylation-mediated degradation, O-GlcNAc at serine112 stabilizes Snail1 and thus increases its repressor function, which in turn attenuates E-cadherin mRNA expression.
20959806	5	14	theme	EMT	937:939	arg1	metabolism					907:916	cellular glucose metabolism	890:916	cellular glucose metabolism	890:916	Thus, dynamic reciprocal O-phosphorylation and O-GlcNAc modification of Snail1 constitute a molecular link between cellular glucose metabolism and the control of EMT.
20959806	5	14	theme	EMT	937:939	arg1	control					926:932	the control	922:932	the control of EMT	922:939	Thus, dynamic reciprocal O-phosphorylation and O-GlcNAc modification of Snail1 constitute a molecular link between cellular glucose metabolism and the control of EMT.
20959806	5	15	mod	modification	831:842	arg1	Snail1					847:852	Snail1	847:852	Snail1	847:852	Thus, dynamic reciprocal O-phosphorylation and O-GlcNAc modification of Snail1 constitute a molecular link between cellular glucose metabolism and the control of EMT.
20959806	5	15	mod	modification	831:842	arg3	O-GlcNAc					822:829	O-GlcNAc modification	822:842	O-GlcNAc modification of Snail1	822:852	Thus, dynamic reciprocal O-phosphorylation and O-GlcNAc modification of Snail1 constitute a molecular link between cellular glucose metabolism and the control of EMT.
20959806	3	16	theme	E-cadherin	612:621	arg1	expression					628:637	E-cadherin mRNA expression	612:637	E-cadherin mRNA expression	612:637	We show that by suppressing O-phosphorylation-mediated degradation, O-GlcNAc at serine112 stabilizes Snail1 and thus increases its repressor function, which in turn attenuates E-cadherin mRNA expression.
20959806	4	17	theme	transcriptional	717:731	arg1	suppression					733:743	transcriptional suppression	717:743	transcriptional suppression of E-cadherin through Snail1	717:772	Hyperglycaemic condition enhances O-GlcNAc modification and initiates EMT by transcriptional suppression of E-cadherin through Snail1.
20959806	2	18	theme	regulator	328:336	arg1	Snail1					268:273	Snail1	268:273	Snail1	268:273	O-phosphorylation of serine by glycogen synthase kinase-3β on Snail1, a transcriptional repressor of E-cadherin and a key regulator of the epithelial-mesenchymal transition (EMT) programme, results in its proteasomal degradation.
20959806	2	18	theme	regulator	328:336	arg1	repressor					294:302	a transcriptional repressor	276:302	a transcriptional repressor of E-cadherin and a key regulator of the epithelial-mesenchymal transition (EMT) programme	276:393	O-phosphorylation of serine by glycogen synthase kinase-3β on Snail1, a transcriptional repressor of E-cadherin and a key regulator of the epithelial-mesenchymal transition (EMT) programme, results in its proteasomal degradation.
20959806	5	19	theme	glucose	899:905	arg1	metabolism					907:916	cellular glucose metabolism	890:916	cellular glucose metabolism	890:916	Thus, dynamic reciprocal O-phosphorylation and O-GlcNAc modification of Snail1 constitute a molecular link between cellular glucose metabolism and the control of EMT.
20959806	5	20	theme	O-GlcNAc	822:829	arg1	modification					831:842	O-GlcNAc modification	822:842	O-GlcNAc modification of Snail1	822:852	Thus, dynamic reciprocal O-phosphorylation and O-GlcNAc modification of Snail1 constitute a molecular link between cellular glucose metabolism and the control of EMT.
20959806	0	21	theme	O-GlcNAc	24:31	arg1	modification					33:44	O-GlcNAc modification	24:44	O-GlcNAc modification	24:44	Snail1 is stabilized by O-GlcNAc modification in hyperglycaemic condition.
20959806	0	22	theme	hyperglycaemic	49:62	arg1	condition					64:72	hyperglycaemic condition	49:72	hyperglycaemic condition	49:72	Snail1 is stabilized by O-GlcNAc modification in hyperglycaemic condition.
20959806	1	23	theme	O-GlcNAc	132:139	arg1	modification					141:152	O-GlcNAc modification	132:152	O-GlcNAc modification	132:152	Protein O-phosphorylation often occurs reciprocally with O-GlcNAc modification and represents a regulatory principle for proteins.
20959806	3	24	from	serine112	516:524	arg1	O-GlcNAc					504:511	O-GlcNAc	504:511	O-GlcNAc at serine112	504:524	We show that by suppressing O-phosphorylation-mediated degradation, O-GlcNAc at serine112 stabilizes Snail1 and thus increases its repressor function, which in turn attenuates E-cadherin mRNA expression.
20959806	5	25	theme	dynamic	781:787	arg1	O-phosphorylation					800:816	dynamic reciprocal O-phosphorylation	781:816	dynamic reciprocal O-phosphorylation	781:816	Thus, dynamic reciprocal O-phosphorylation and O-GlcNAc modification of Snail1 constitute a molecular link between cellular glucose metabolism and the control of EMT.
20959806	2	26	theme	glycogen	237:244	arg1	synthase					246:253	glycogen synthase kinase-3β	237:263	glycogen synthase kinase-3β on Snail1, a transcriptional repressor of E-cadherin and a key regulator of the epithelial-mesenchymal transition (EMT) programme,	237:394	O-phosphorylation of serine by glycogen synthase kinase-3β on Snail1, a transcriptional repressor of E-cadherin and a key regulator of the epithelial-mesenchymal transition (EMT) programme, results in its proteasomal degradation.
20959806	5	27	theme	reciprocal	789:798	arg1	O-phosphorylation					800:816	dynamic reciprocal O-phosphorylation	781:816	dynamic reciprocal O-phosphorylation	781:816	Thus, dynamic reciprocal O-phosphorylation and O-GlcNAc modification of Snail1 constitute a molecular link between cellular glucose metabolism and the control of EMT.
20959806	3	28	theme	repressor	567:575	arg1	function					577:584	its repressor function	563:584	its repressor function	563:584	We show that by suppressing O-phosphorylation-mediated degradation, O-GlcNAc at serine112 stabilizes Snail1 and thus increases its repressor function, which in turn attenuates E-cadherin mRNA expression.
20959806	2	29	theme	transition	368:377	arg1	programme					385:393	the epithelial-mesenchymal transition (EMT) programme	341:393	the epithelial-mesenchymal transition (EMT) programme	341:393	O-phosphorylation of serine by glycogen synthase kinase-3β on Snail1, a transcriptional repressor of E-cadherin and a key regulator of the epithelial-mesenchymal transition (EMT) programme, results in its proteasomal degradation.
20959806	5	30	theme	molecular	867:875	arg1	link					877:880	a molecular link	865:880	a molecular link between cellular glucose metabolism and the control of EMT	865:939	Thus, dynamic reciprocal O-phosphorylation and O-GlcNAc modification of Snail1 constitute a molecular link between cellular glucose metabolism and the control of EMT.
20959806	2	31	theme	serine	227:232	arg1	O-phosphorylation					206:222	O-phosphorylation	206:222	O-phosphorylation of serine by glycogen synthase kinase-3β on Snail1, a transcriptional repressor of E-cadherin and a key regulator of the epithelial-mesenchymal transition (EMT) programme,	206:394	O-phosphorylation of serine by glycogen synthase kinase-3β on Snail1, a transcriptional repressor of E-cadherin and a key regulator of the epithelial-mesenchymal transition (EMT) programme, results in its proteasomal degradation.
20959806	2	32	theme	transcriptional	278:292	arg1	Snail1					268:273	Snail1	268:273	Snail1	268:273	O-phosphorylation of serine by glycogen synthase kinase-3β on Snail1, a transcriptional repressor of E-cadherin and a key regulator of the epithelial-mesenchymal transition (EMT) programme, results in its proteasomal degradation.
20959806	2	32	theme	transcriptional	278:292	arg1	repressor					294:302	a transcriptional repressor	276:302	a transcriptional repressor of E-cadherin and a key regulator of the epithelial-mesenchymal transition (EMT) programme	276:393	O-phosphorylation of serine by glycogen synthase kinase-3β on Snail1, a transcriptional repressor of E-cadherin and a key regulator of the epithelial-mesenchymal transition (EMT) programme, results in its proteasomal degradation.
20959806	1	33	theme	regulatory	171:180	arg1	principle					182:190	a regulatory principle	169:190	a regulatory principle for proteins	169:203	Protein O-phosphorylation often occurs reciprocally with O-GlcNAc modification and represents a regulatory principle for proteins.
33690219	5	0	theme	low-glucose	817:827	arg1	conditions					829:838	low-glucose conditions	817:838	low-glucose conditions	817:838	In this study, PCK1 knockout markedly enhanced the global O-GlcNAcylation levels under low-glucose conditions.
33690219	6	1	theme	uridine	1012:1018	arg1	biosynthesis					1065:1076	uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc) biosynthesis	1012:1076	uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc) biosynthesis	1012:1076	Mechanistically, metabolic reprogramming in PCK1-loss hepatoma cells led to oxaloacetate accumulation and increased de novo uridine triphosphate synthesis contributing to uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc) biosynthesis.
33690219	7	2	theme	PCK1	1102:1105	arg1	Meanwhile					1079:1087	Meanwhile	1079:1087	Meanwhile	1079:1087	Meanwhile, deletion of PCK1 also resulted in AMPK-GFAT1 axis inactivation, promoting UDP-GlcNAc synthesis for elevated O-GlcNAcylation.
33690219	7	2	theme	PCK1	1102:1105	arg1	deletion					1090:1097	deletion	1090:1097	deletion of PCK1	1090:1105	Meanwhile, deletion of PCK1 also resulted in AMPK-GFAT1 axis inactivation, promoting UDP-GlcNAc synthesis for elevated O-GlcNAcylation.
33690219	8	3	theme	PCK1	1244:1247	arg1	expression					1230:1239	lower expression	1224:1239	lower expression of PCK1	1224:1247	Notably, lower expression of PCK1 promoted CHK2 threonine 378 O-GlcNAcylation, counteracting its stability and dimer formation, increasing CHK2-dependent Rb phosphorylation and HCC cell proliferation.
33690219	1	4	theme	protein	283:289	arg1	O-GlcNAcylation					291:305	protein O-GlcNAcylation	283:305	protein O-GlcNAcylation (a nutrient sensor)	283:325	Although cancer cells are frequently faced with a nutrient- and oxygen-poor microenvironment, elevated hexosamine-biosynthesis pathway (HBP) activity and protein O-GlcNAcylation (a nutrient sensor) contribute to rapid growth of tumor and are emerging hallmarks of cancer.
33690219	1	4	theme	protein	283:289	arg1	sensor					319:324	a nutrient sensor	308:324	a nutrient sensor	308:324	Although cancer cells are frequently faced with a nutrient- and oxygen-poor microenvironment, elevated hexosamine-biosynthesis pathway (HBP) activity and protein O-GlcNAcylation (a nutrient sensor) contribute to rapid growth of tumor and are emerging hallmarks of cancer.
33690219	10	5	theme	HCC	1684:1686	arg1	oncogenesis					1688:1698	HCC oncogenesis	1684:1698	HCC oncogenesis	1684:1698	We reveal a link between PCK1 depletion and hyper-O-GlcNAcylation that underlies HCC oncogenesis and suggest therapeutic targets for HCC that act by inhibiting O-GlcNAcylation.
33690219	6	6	theme	hepatoma	895:902	arg1	cells					904:908	PCK1-loss hepatoma cells	885:908	PCK1-loss hepatoma cells	885:908	Mechanistically, metabolic reprogramming in PCK1-loss hepatoma cells led to oxaloacetate accumulation and increased de novo uridine triphosphate synthesis contributing to uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc) biosynthesis.
33690219	1	7	theme	nutrient-	179:187	arg1	microenvironment					205:220	a nutrient- and oxygen-poor microenvironment	177:220	a nutrient- and oxygen-poor microenvironment	177:220	Although cancer cells are frequently faced with a nutrient- and oxygen-poor microenvironment, elevated hexosamine-biosynthesis pathway (HBP) activity and protein O-GlcNAcylation (a nutrient sensor) contribute to rapid growth of tumor and are emerging hallmarks of cancer.
33690219	4	8	from	role	635:638	arg1	activity					664:671	enhanced HBP activity	651:671	enhanced HBP activity	651:671	However, little is known about the potential role of PCK1 in enhanced HBP activity and HCC carcinogenesis under glucose-limited conditions.
33690219	4	8	from	role	635:638	arg1	carcinogenesis					681:694	HCC carcinogenesis	677:694	HCC carcinogenesis	677:694	However, little is known about the potential role of PCK1 in enhanced HBP activity and HCC carcinogenesis under glucose-limited conditions.
33690219	1	9	theme	emerging	371:378	arg1	hallmarks					380:388	emerging hallmarks	371:388	emerging hallmarks of cancer	371:398	Although cancer cells are frequently faced with a nutrient- and oxygen-poor microenvironment, elevated hexosamine-biosynthesis pathway (HBP) activity and protein O-GlcNAcylation (a nutrient sensor) contribute to rapid growth of tumor and are emerging hallmarks of cancer.
33690219	6	10	theme	PCK1-loss	885:893	arg1	cells					904:908	PCK1-loss hepatoma cells	885:908	PCK1-loss hepatoma cells	885:908	Mechanistically, metabolic reprogramming in PCK1-loss hepatoma cells led to oxaloacetate accumulation and increased de novo uridine triphosphate synthesis contributing to uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc) biosynthesis.
33690219	0	11	theme	glucose	108:114	arg1	deprivation					116:126	glucose deprivation	108:126	glucose deprivation	108:126	Gluconeogenic enzyme PCK1 deficiency promotes CHK2 O-GlcNAcylation and hepatocellular carcinoma growth upon glucose deprivation.
33690219	4	12	theme	HBP	660:662	arg1	activity					664:671	enhanced HBP activity	651:671	enhanced HBP activity	651:671	However, little is known about the potential role of PCK1 in enhanced HBP activity and HCC carcinogenesis under glucose-limited conditions.
33690219	9	13	theme	tumor	1547:1551	arg1	progression					1553:1563	tumor progression	1547:1563	tumor progression	1547:1563	Moreover, aminooxyacetic acid hemihydrochloride and 6-diazo-5-oxo-L-norleucine blocked HBP-mediated O-GlcNAcylation and suppressed tumor progression in liver-specific Pck1-knockout mice.
33690219	6	14	theme	increased	947:955	arg1	synthesis					986:994	increased de novo uridine triphosphate synthesis	947:994	increased de novo uridine triphosphate synthesis	947:994	Mechanistically, metabolic reprogramming in PCK1-loss hepatoma cells led to oxaloacetate accumulation and increased de novo uridine triphosphate synthesis contributing to uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc) biosynthesis.
33690219	4	15	theme	potential	625:633	arg1	role					635:638	the potential role	621:638	the potential role of PCK1 in enhanced HBP activity and HCC carcinogenesis	621:694	However, little is known about the potential role of PCK1 in enhanced HBP activity and HCC carcinogenesis under glucose-limited conditions.
33690219	5	16	theme	global	781:786	arg1	levels					804:809	the global O-GlcNAcylation levels	777:809	the global O-GlcNAcylation levels	777:809	In this study, PCK1 knockout markedly enhanced the global O-GlcNAcylation levels under low-glucose conditions.
33690219	6	17	theme	triphosphate	973:984	arg1	synthesis					986:994	increased de novo uridine triphosphate synthesis	947:994	increased de novo uridine triphosphate synthesis	947:994	Mechanistically, metabolic reprogramming in PCK1-loss hepatoma cells led to oxaloacetate accumulation and increased de novo uridine triphosphate synthesis contributing to uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc) biosynthesis.
33690219	1	18	theme	hexosamine-biosynthesis	232:254	arg1	HBP					265:267	HBP	265:267	HBP	265:267	Although cancer cells are frequently faced with a nutrient- and oxygen-poor microenvironment, elevated hexosamine-biosynthesis pathway (HBP) activity and protein O-GlcNAcylation (a nutrient sensor) contribute to rapid growth of tumor and are emerging hallmarks of cancer.
33690219	1	18	theme	hexosamine-biosynthesis	232:254	arg1	pathway					256:262	hexosamine-biosynthesis pathway	232:262	elevated hexosamine-biosynthesis pathway (HBP) activity	223:277	Although cancer cells are frequently faced with a nutrient- and oxygen-poor microenvironment, elevated hexosamine-biosynthesis pathway (HBP) activity and protein O-GlcNAcylation (a nutrient sensor) contribute to rapid growth of tumor and are emerging hallmarks of cancer.
33690219	3	19	theme	gluconeogenic	474:486	arg1	carboxykinase					515:527	The gluconeogenic enzyme phosphoenolpyruvate carboxykinase 1	470:529	The gluconeogenic enzyme phosphoenolpyruvate carboxykinase 1 (PCK1)	470:536	The gluconeogenic enzyme phosphoenolpyruvate carboxykinase 1 (PCK1) is downregulated in hepatocellular carcinoma (HCC).
33690219	3	19	theme	gluconeogenic	474:486	arg1	PCK1					532:535	PCK1	532:535	PCK1	532:535	The gluconeogenic enzyme phosphoenolpyruvate carboxykinase 1 (PCK1) is downregulated in hepatocellular carcinoma (HCC).
33690219	5	20	theme	O-GlcNAcylation	788:802	arg1	levels					804:809	the global O-GlcNAcylation levels	777:809	the global O-GlcNAcylation levels	777:809	In this study, PCK1 knockout markedly enhanced the global O-GlcNAcylation levels under low-glucose conditions.
33690219	1	21	theme	cancer	393:398	arg1	hallmarks					380:388	emerging hallmarks	371:388	emerging hallmarks of cancer	371:398	Although cancer cells are frequently faced with a nutrient- and oxygen-poor microenvironment, elevated hexosamine-biosynthesis pathway (HBP) activity and protein O-GlcNAcylation (a nutrient sensor) contribute to rapid growth of tumor and are emerging hallmarks of cancer.
33690219	8	22	theme	Rb	1369:1370	arg1	phosphorylation					1372:1386	CHK2-dependent Rb phosphorylation	1354:1386	CHK2-dependent Rb phosphorylation	1354:1386	Notably, lower expression of PCK1 promoted CHK2 threonine 378 O-GlcNAcylation, counteracting its stability and dimer formation, increasing CHK2-dependent Rb phosphorylation and HCC cell proliferation.
33690219	6	23	theme	metabolic	858:866	arg1	reprogramming					868:880	metabolic reprogramming	858:880	metabolic reprogramming in PCK1-loss hepatoma cells	858:908	Mechanistically, metabolic reprogramming in PCK1-loss hepatoma cells led to oxaloacetate accumulation and increased de novo uridine triphosphate synthesis contributing to uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc) biosynthesis.
33690219	8	24	theme	dimer	1326:1330	arg1	formation					1332:1340	dimer formation	1326:1340	dimer formation	1326:1340	Notably, lower expression of PCK1 promoted CHK2 threonine 378 O-GlcNAcylation, counteracting its stability and dimer formation, increasing CHK2-dependent Rb phosphorylation and HCC cell proliferation.
33690219	1	25	theme	oxygen-poor	193:203	arg1	microenvironment					205:220	a nutrient- and oxygen-poor microenvironment	177:220	a nutrient- and oxygen-poor microenvironment	177:220	Although cancer cells are frequently faced with a nutrient- and oxygen-poor microenvironment, elevated hexosamine-biosynthesis pathway (HBP) activity and protein O-GlcNAcylation (a nutrient sensor) contribute to rapid growth of tumor and are emerging hallmarks of cancer.
33690219	0	26	theme	enzyme	14:19	arg1	deficiency					26:35	Gluconeogenic enzyme PCK1 deficiency	0:35	Gluconeogenic enzyme PCK1 deficiency	0:35	Gluconeogenic enzyme PCK1 deficiency promotes CHK2 O-GlcNAcylation and hepatocellular carcinoma growth upon glucose deprivation.
33690219	8	27	theme	378	1273:1275	arg1	O-GlcNAcylation					1277:1291	CHK2 threonine 378 O-GlcNAcylation	1258:1291	CHK2 threonine 378 O-GlcNAcylation	1258:1291	Notably, lower expression of PCK1 promoted CHK2 threonine 378 O-GlcNAcylation, counteracting its stability and dimer formation, increasing CHK2-dependent Rb phosphorylation and HCC cell proliferation.
33690219	9	28	theme	HBP-mediated	1503:1514	arg1	O-GlcNAcylation					1516:1530	HBP-mediated O-GlcNAcylation	1503:1530	HBP-mediated O-GlcNAcylation	1503:1530	Moreover, aminooxyacetic acid hemihydrochloride and 6-diazo-5-oxo-L-norleucine blocked HBP-mediated O-GlcNAcylation and suppressed tumor progression in liver-specific Pck1-knockout mice.
33690219	4	29	theme	HCC	677:679	arg1	carcinogenesis					681:694	HCC carcinogenesis	677:694	HCC carcinogenesis	677:694	However, little is known about the potential role of PCK1 in enhanced HBP activity and HCC carcinogenesis under glucose-limited conditions.
33690219	0	30	theme	Gluconeogenic	0:12	arg1	deficiency					26:35	Gluconeogenic enzyme PCK1 deficiency	0:35	Gluconeogenic enzyme PCK1 deficiency	0:35	Gluconeogenic enzyme PCK1 deficiency promotes CHK2 O-GlcNAcylation and hepatocellular carcinoma growth upon glucose deprivation.
33690219	1	31	theme	nutrient	310:317	arg1	O-GlcNAcylation					291:305	protein O-GlcNAcylation	283:305	protein O-GlcNAcylation (a nutrient sensor)	283:325	Although cancer cells are frequently faced with a nutrient- and oxygen-poor microenvironment, elevated hexosamine-biosynthesis pathway (HBP) activity and protein O-GlcNAcylation (a nutrient sensor) contribute to rapid growth of tumor and are emerging hallmarks of cancer.
33690219	1	31	theme	nutrient	310:317	arg1	sensor					319:324	a nutrient sensor	308:324	a nutrient sensor	308:324	Although cancer cells are frequently faced with a nutrient- and oxygen-poor microenvironment, elevated hexosamine-biosynthesis pathway (HBP) activity and protein O-GlcNAcylation (a nutrient sensor) contribute to rapid growth of tumor and are emerging hallmarks of cancer.
33690219	8	32	theme	cell	1396:1399	arg1	proliferation					1401:1413	HCC cell proliferation	1392:1413	HCC cell proliferation	1392:1413	Notably, lower expression of PCK1 promoted CHK2 threonine 378 O-GlcNAcylation, counteracting its stability and dimer formation, increasing CHK2-dependent Rb phosphorylation and HCC cell proliferation.
33690219	2	33	theme	Inhibiting	401:410	arg1	O-GlcNAcylation					412:426	Inhibiting O-GlcNAcylation	401:426	Inhibiting O-GlcNAcylation	401:426	Inhibiting O-GlcNAcylation could be a promising anticancer strategy.
33690219	2	33	theme	Inhibiting	401:410	arg1	strategy					460:467	a promising anticancer strategy	437:467	a promising anticancer strategy	437:467	Inhibiting O-GlcNAcylation could be a promising anticancer strategy.
33690219	10	34	theme	PCK1	1628:1631	arg1	depletion					1633:1641	PCK1 depletion	1628:1641	PCK1 depletion	1628:1641	We reveal a link between PCK1 depletion and hyper-O-GlcNAcylation that underlies HCC oncogenesis and suggest therapeutic targets for HCC that act by inhibiting O-GlcNAcylation.
33690219	1	35	theme	elevated	223:230	arg1	activity					270:277	elevated hexosamine-biosynthesis pathway (HBP) activity	223:277	elevated hexosamine-biosynthesis pathway (HBP) activity	223:277	Although cancer cells are frequently faced with a nutrient- and oxygen-poor microenvironment, elevated hexosamine-biosynthesis pathway (HBP) activity and protein O-GlcNAcylation (a nutrient sensor) contribute to rapid growth of tumor and are emerging hallmarks of cancer.
33690219	0	36	theme	PCK1	21:24	arg1	deficiency					26:35	Gluconeogenic enzyme PCK1 deficiency	0:35	Gluconeogenic enzyme PCK1 deficiency	0:35	Gluconeogenic enzyme PCK1 deficiency promotes CHK2 O-GlcNAcylation and hepatocellular carcinoma growth upon glucose deprivation.
33690219	6	37	theme	de	957:958	arg1	synthesis					986:994	increased de novo uridine triphosphate synthesis	947:994	increased de novo uridine triphosphate synthesis	947:994	Mechanistically, metabolic reprogramming in PCK1-loss hepatoma cells led to oxaloacetate accumulation and increased de novo uridine triphosphate synthesis contributing to uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc) biosynthesis.
33690219	3	38	theme	hepatocellular	558:571	arg1	HCC					584:586	HCC	584:586	HCC	584:586	The gluconeogenic enzyme phosphoenolpyruvate carboxykinase 1 (PCK1) is downregulated in hepatocellular carcinoma (HCC).
33690219	3	38	theme	hepatocellular	558:571	arg1	carcinoma					573:581	hepatocellular carcinoma	558:581	hepatocellular carcinoma (HCC)	558:587	The gluconeogenic enzyme phosphoenolpyruvate carboxykinase 1 (PCK1) is downregulated in hepatocellular carcinoma (HCC).
33690219	2	39	theme	anticancer	449:458	arg1	O-GlcNAcylation					412:426	Inhibiting O-GlcNAcylation	401:426	Inhibiting O-GlcNAcylation	401:426	Inhibiting O-GlcNAcylation could be a promising anticancer strategy.
33690219	2	39	theme	anticancer	449:458	arg1	strategy					460:467	a promising anticancer strategy	437:467	a promising anticancer strategy	437:467	Inhibiting O-GlcNAcylation could be a promising anticancer strategy.
33690219	0	40	theme	CHK2	46:49	arg1	O-GlcNAcylation					51:65	CHK2 O-GlcNAcylation	46:65	CHK2 O-GlcNAcylation	46:65	Gluconeogenic enzyme PCK1 deficiency promotes CHK2 O-GlcNAcylation and hepatocellular carcinoma growth upon glucose deprivation.
33690219	9	41	theme	liver-specific	1568:1581	arg1	mice					1597:1600	liver-specific Pck1-knockout mice	1568:1600	liver-specific Pck1-knockout mice	1568:1600	Moreover, aminooxyacetic acid hemihydrochloride and 6-diazo-5-oxo-L-norleucine blocked HBP-mediated O-GlcNAcylation and suppressed tumor progression in liver-specific Pck1-knockout mice.
33690219	5	42	theme	knockout	750:757	arg1	PCK1					745:748	PCK1 knockout	745:757	PCK1 knockout	745:757	In this study, PCK1 knockout markedly enhanced the global O-GlcNAcylation levels under low-glucose conditions.
33690219	1	43	theme	pathway	256:262	arg1	activity					270:277	elevated hexosamine-biosynthesis pathway (HBP) activity	223:277	elevated hexosamine-biosynthesis pathway (HBP) activity	223:277	Although cancer cells are frequently faced with a nutrient- and oxygen-poor microenvironment, elevated hexosamine-biosynthesis pathway (HBP) activity and protein O-GlcNAcylation (a nutrient sensor) contribute to rapid growth of tumor and are emerging hallmarks of cancer.
33690219	4	44	theme	glucose-limited	702:716	arg1	conditions					718:727	glucose-limited conditions	702:727	glucose-limited conditions	702:727	However, little is known about the potential role of PCK1 in enhanced HBP activity and HCC carcinogenesis under glucose-limited conditions.
33690219	2	45	theme	promising	439:447	arg1	O-GlcNAcylation					412:426	Inhibiting O-GlcNAcylation	401:426	Inhibiting O-GlcNAcylation	401:426	Inhibiting O-GlcNAcylation could be a promising anticancer strategy.
33690219	2	45	theme	promising	439:447	arg1	strategy					460:467	a promising anticancer strategy	437:467	a promising anticancer strategy	437:467	Inhibiting O-GlcNAcylation could be a promising anticancer strategy.
33690219	8	46	theme	HCC	1392:1394	arg1	proliferation					1401:1413	HCC cell proliferation	1392:1413	HCC cell proliferation	1392:1413	Notably, lower expression of PCK1 promoted CHK2 threonine 378 O-GlcNAcylation, counteracting its stability and dimer formation, increasing CHK2-dependent Rb phosphorylation and HCC cell proliferation.
33690219	9	47	theme	Pck1-knockout	1583:1595	arg1	mice					1597:1600	liver-specific Pck1-knockout mice	1568:1600	liver-specific Pck1-knockout mice	1568:1600	Moreover, aminooxyacetic acid hemihydrochloride and 6-diazo-5-oxo-L-norleucine blocked HBP-mediated O-GlcNAcylation and suppressed tumor progression in liver-specific Pck1-knockout mice.
33690219	7	48	theme	elevated	1189:1196	arg1	O-GlcNAcylation					1198:1212	elevated O-GlcNAcylation	1189:1212	elevated O-GlcNAcylation	1189:1212	Meanwhile, deletion of PCK1 also resulted in AMPK-GFAT1 axis inactivation, promoting UDP-GlcNAc synthesis for elevated O-GlcNAcylation.
33690219	7	49	theme	axis	1135:1138	arg1	inactivation					1140:1151	AMPK-GFAT1 axis inactivation	1124:1151	AMPK-GFAT1 axis inactivation	1124:1151	Meanwhile, deletion of PCK1 also resulted in AMPK-GFAT1 axis inactivation, promoting UDP-GlcNAc synthesis for elevated O-GlcNAcylation.
33690219	1	50	theme	rapid	341:345	arg1	growth					347:352	rapid growth	341:352	rapid growth of tumor	341:361	Although cancer cells are frequently faced with a nutrient- and oxygen-poor microenvironment, elevated hexosamine-biosynthesis pathway (HBP) activity and protein O-GlcNAcylation (a nutrient sensor) contribute to rapid growth of tumor and are emerging hallmarks of cancer.
33690219	7	51	theme	UDP-GlcNAc	1164:1173	arg1	synthesis					1175:1183	UDP-GlcNAc synthesis	1164:1183	UDP-GlcNAc synthesis for elevated O-GlcNAcylation	1164:1212	Meanwhile, deletion of PCK1 also resulted in AMPK-GFAT1 axis inactivation, promoting UDP-GlcNAc synthesis for elevated O-GlcNAcylation.
33690219	8	52	theme	threonine	1263:1271	arg1	O-GlcNAcylation					1277:1291	CHK2 threonine 378 O-GlcNAcylation	1258:1291	CHK2 threonine 378 O-GlcNAcylation	1258:1291	Notably, lower expression of PCK1 promoted CHK2 threonine 378 O-GlcNAcylation, counteracting its stability and dimer formation, increasing CHK2-dependent Rb phosphorylation and HCC cell proliferation.
33690219	6	53	theme	uridine	965:971	arg1	synthesis					986:994	increased de novo uridine triphosphate synthesis	947:994	increased de novo uridine triphosphate synthesis	947:994	Mechanistically, metabolic reprogramming in PCK1-loss hepatoma cells led to oxaloacetate accumulation and increased de novo uridine triphosphate synthesis contributing to uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc) biosynthesis.
33690219	1	54	theme	cancer	138:143	arg1	cells					145:149	cancer cells	138:149	cancer cells	138:149	Although cancer cells are frequently faced with a nutrient- and oxygen-poor microenvironment, elevated hexosamine-biosynthesis pathway (HBP) activity and protein O-GlcNAcylation (a nutrient sensor) contribute to rapid growth of tumor and are emerging hallmarks of cancer.
33690219	8	55	theme	lower	1224:1228	arg1	expression					1230:1239	lower expression	1224:1239	lower expression of PCK1	1224:1247	Notably, lower expression of PCK1 promoted CHK2 threonine 378 O-GlcNAcylation, counteracting its stability and dimer formation, increasing CHK2-dependent Rb phosphorylation and HCC cell proliferation.
33690219	6	56	theme	UDP-GlcNAc	1053:1062	arg1	biosynthesis					1065:1076	uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc) biosynthesis	1012:1076	uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc) biosynthesis	1012:1076	Mechanistically, metabolic reprogramming in PCK1-loss hepatoma cells led to oxaloacetate accumulation and increased de novo uridine triphosphate synthesis contributing to uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc) biosynthesis.
33690219	6	57	theme	diphosphate-N-acetylglucosamine	1020:1050	arg1	biosynthesis					1065:1076	uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc) biosynthesis	1012:1076	uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc) biosynthesis	1012:1076	Mechanistically, metabolic reprogramming in PCK1-loss hepatoma cells led to oxaloacetate accumulation and increased de novo uridine triphosphate synthesis contributing to uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc) biosynthesis.
33690219	6	58	theme	oxaloacetate	917:928	arg1	accumulation					930:941	oxaloacetate accumulation	917:941	oxaloacetate accumulation	917:941	Mechanistically, metabolic reprogramming in PCK1-loss hepatoma cells led to oxaloacetate accumulation and increased de novo uridine triphosphate synthesis contributing to uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc) biosynthesis.
33690219	10	59	theme	therapeutic	1712:1722	arg1	targets					1724:1730	therapeutic targets	1712:1730	therapeutic targets for HCC that act by inhibiting O-GlcNAcylation	1712:1777	We reveal a link between PCK1 depletion and hyper-O-GlcNAcylation that underlies HCC oncogenesis and suggest therapeutic targets for HCC that act by inhibiting O-GlcNAcylation.
33690219	8	60	theme	CHK2	1258:1261	arg1	O-GlcNAcylation					1277:1291	CHK2 threonine 378 O-GlcNAcylation	1258:1291	CHK2 threonine 378 O-GlcNAcylation	1258:1291	Notably, lower expression of PCK1 promoted CHK2 threonine 378 O-GlcNAcylation, counteracting its stability and dimer formation, increasing CHK2-dependent Rb phosphorylation and HCC cell proliferation.
33690219	7	61	theme	AMPK-GFAT1	1124:1133	arg1	inactivation					1140:1151	AMPK-GFAT1 axis inactivation	1124:1151	AMPK-GFAT1 axis inactivation	1124:1151	Meanwhile, deletion of PCK1 also resulted in AMPK-GFAT1 axis inactivation, promoting UDP-GlcNAc synthesis for elevated O-GlcNAcylation.
33690219	4	62	theme	PCK1	643:646	arg1	role					635:638	the potential role	621:638	the potential role of PCK1 in enhanced HBP activity and HCC carcinogenesis	621:694	However, little is known about the potential role of PCK1 in enhanced HBP activity and HCC carcinogenesis under glucose-limited conditions.
33690219	9	63	theme	aminooxyacetic	1426:1439	arg1	hemihydrochloride					1446:1462	aminooxyacetic acid hemihydrochloride	1426:1462	aminooxyacetic acid hemihydrochloride	1426:1462	Moreover, aminooxyacetic acid hemihydrochloride and 6-diazo-5-oxo-L-norleucine blocked HBP-mediated O-GlcNAcylation and suppressed tumor progression in liver-specific Pck1-knockout mice.
33690219	8	64	theme	CHK2-dependent	1354:1367	arg1	phosphorylation					1372:1386	CHK2-dependent Rb phosphorylation	1354:1386	CHK2-dependent Rb phosphorylation	1354:1386	Notably, lower expression of PCK1 promoted CHK2 threonine 378 O-GlcNAcylation, counteracting its stability and dimer formation, increasing CHK2-dependent Rb phosphorylation and HCC cell proliferation.
33690219	0	65	theme	carcinoma	86:94	arg1	growth					96:101	hepatocellular carcinoma growth	71:101	hepatocellular carcinoma growth	71:101	Gluconeogenic enzyme PCK1 deficiency promotes CHK2 O-GlcNAcylation and hepatocellular carcinoma growth upon glucose deprivation.
33690219	9	66	theme	acid	1441:1444	arg1	hemihydrochloride					1446:1462	aminooxyacetic acid hemihydrochloride	1426:1462	aminooxyacetic acid hemihydrochloride	1426:1462	Moreover, aminooxyacetic acid hemihydrochloride and 6-diazo-5-oxo-L-norleucine blocked HBP-mediated O-GlcNAcylation and suppressed tumor progression in liver-specific Pck1-knockout mice.
33690219	3	67	theme	phosphoenolpyruvate	495:513	arg1	carboxykinase					515:527	The gluconeogenic enzyme phosphoenolpyruvate carboxykinase 1	470:529	The gluconeogenic enzyme phosphoenolpyruvate carboxykinase 1 (PCK1)	470:536	The gluconeogenic enzyme phosphoenolpyruvate carboxykinase 1 (PCK1) is downregulated in hepatocellular carcinoma (HCC).
33690219	3	67	theme	phosphoenolpyruvate	495:513	arg1	PCK1					532:535	PCK1	532:535	PCK1	532:535	The gluconeogenic enzyme phosphoenolpyruvate carboxykinase 1 (PCK1) is downregulated in hepatocellular carcinoma (HCC).
33690219	3	68	theme	enzyme	488:493	arg1	carboxykinase					515:527	The gluconeogenic enzyme phosphoenolpyruvate carboxykinase 1	470:529	The gluconeogenic enzyme phosphoenolpyruvate carboxykinase 1 (PCK1)	470:536	The gluconeogenic enzyme phosphoenolpyruvate carboxykinase 1 (PCK1) is downregulated in hepatocellular carcinoma (HCC).
33690219	3	68	theme	enzyme	488:493	arg1	PCK1					532:535	PCK1	532:535	PCK1	532:535	The gluconeogenic enzyme phosphoenolpyruvate carboxykinase 1 (PCK1) is downregulated in hepatocellular carcinoma (HCC).
33690219	4	69	theme	enhanced	651:658	arg1	activity					664:671	enhanced HBP activity	651:671	enhanced HBP activity	651:671	However, little is known about the potential role of PCK1 in enhanced HBP activity and HCC carcinogenesis under glucose-limited conditions.
33690219	0	70	theme	hepatocellular	71:84	arg1	carcinoma					86:94	hepatocellular carcinoma	71:94	hepatocellular carcinoma growth	71:101	Gluconeogenic enzyme PCK1 deficiency promotes CHK2 O-GlcNAcylation and hepatocellular carcinoma growth upon glucose deprivation.
33690219	1	71	theme	tumor	357:361	arg1	growth					347:352	rapid growth	341:352	rapid growth of tumor	341:361	Although cancer cells are frequently faced with a nutrient- and oxygen-poor microenvironment, elevated hexosamine-biosynthesis pathway (HBP) activity and protein O-GlcNAcylation (a nutrient sensor) contribute to rapid growth of tumor and are emerging hallmarks of cancer.
33690219	6	72	from	reprogramming	868:880	arg1	cells					904:908	PCK1-loss hepatoma cells	885:908	PCK1-loss hepatoma cells	885:908	Mechanistically, metabolic reprogramming in PCK1-loss hepatoma cells led to oxaloacetate accumulation and increased de novo uridine triphosphate synthesis contributing to uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc) biosynthesis.
33690219	6	73	dep	de	957:958	arg1	novo					960:963	novo	960:963	novo	960:963	Mechanistically, metabolic reprogramming in PCK1-loss hepatoma cells led to oxaloacetate accumulation and increased de novo uridine triphosphate synthesis contributing to uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc) biosynthesis.
26620801	3	0	theme	extensive	334:342	arg1	phosphorylation					344:358	extensive phosphorylation	334:358	extensive phosphorylation of cryAB at Ser59 followed by Ser45 (Ser19 is largely unphosphorylated)	334:430	In glioma cells, notwithstanding extensive phosphorylation of cryAB at Ser59 followed by Ser45 (Ser19 is largely unphosphorylated), we discovered that the majority of secreted exosomal cryAB is nonphosphorylated.
26620801	4	1	theme	Transient	514:522	arg1	expression					532:541	Transient ectopic expression	514:541	Transient ectopic expression of a yellow fluorescent protein (YFP) tagged triple phosphomimic (3-SD) cryAB construct in cryAB absent glioma cells	514:658	Transient ectopic expression of a yellow fluorescent protein (YFP) tagged triple phosphomimic (3-SD) cryAB construct in cryAB absent glioma cells led to the formation of large cytosolic inclusions.
26620801	3	2	dep	Ser45	390:394	arg1	unphosphorylated					414:429	unphosphorylated	414:429	unphosphorylated	414:429	In glioma cells, notwithstanding extensive phosphorylation of cryAB at Ser59 followed by Ser45 (Ser19 is largely unphosphorylated), we discovered that the majority of secreted exosomal cryAB is nonphosphorylated.
26620801	4	3	theme	inclusions	700:709	arg1	formation					671:679	the formation	667:679	the formation of large cytosolic inclusions	667:709	Transient ectopic expression of a yellow fluorescent protein (YFP) tagged triple phosphomimic (3-SD) cryAB construct in cryAB absent glioma cells led to the formation of large cytosolic inclusions.
26620801	8	4	dep	packaging	1368:1376	arg1	the					1364:1366	the	1364:1366	the	1364:1366	Thus, our study points to O-GlcNAcylation and lack of phosphorylation as being the selective processes involved in the packaging and secretion of cryAB via exosomes.
26620801	4	5	theme	phosphomimic	595:606	arg1	construct					621:629	triple phosphomimic (3-SD) cryAB construct	588:629	triple phosphomimic (3-SD) cryAB construct in cryAB absent glioma cells	588:658	Transient ectopic expression of a yellow fluorescent protein (YFP) tagged triple phosphomimic (3-SD) cryAB construct in cryAB absent glioma cells led to the formation of large cytosolic inclusions.
26620801	6	6	theme	3-SD	858:861	arg1	YFP-cryAB					863:871	3-SD YFP-cryAB	858:871	3-SD YFP-cryAB	858:871	Moreover, decreased colocalization of 3-SD YFP-cryAB with multivesicular endosome (MVE) and exosome marker, CD63 or Rab27, a small GTPase regulating exocytosis of MVEs, suggests that phosphorylation deters packaging of cryAB in vesicles bound for secretion as exosomes.
26620801	4	7	theme	cytosolic	690:698	arg1	inclusions					700:709	large cytosolic inclusions	684:709	large cytosolic inclusions	684:709	Transient ectopic expression of a yellow fluorescent protein (YFP) tagged triple phosphomimic (3-SD) cryAB construct in cryAB absent glioma cells led to the formation of large cytosolic inclusions.
26620801	4	8	theme	triple	588:593	arg1	construct					621:629	triple phosphomimic (3-SD) cryAB construct	588:629	triple phosphomimic (3-SD) cryAB construct in cryAB absent glioma cells	588:658	Transient ectopic expression of a yellow fluorescent protein (YFP) tagged triple phosphomimic (3-SD) cryAB construct in cryAB absent glioma cells led to the formation of large cytosolic inclusions.
26620801	7	9	theme	exosomal	1229:1236	arg1	secretion					1238:1246	reduced exosomal secretion	1221:1246	reduced exosomal secretion	1221:1246	Additionally, we found that preventing O-GlcNAcylation on cryAB also curtailed its colocalization with CD63 and Rab27 resulting in reduced exosomal secretion.
26620801	4	10	theme	3-SD	609:612	arg1	construct					621:629	triple phosphomimic (3-SD) cryAB construct	588:629	triple phosphomimic (3-SD) cryAB construct in cryAB absent glioma cells	588:658	Transient ectopic expression of a yellow fluorescent protein (YFP) tagged triple phosphomimic (3-SD) cryAB construct in cryAB absent glioma cells led to the formation of large cytosolic inclusions.
26620801	4	11	theme	cryAB	634:638	arg1	cells					654:658	cryAB absent glioma cells	634:658	cryAB absent glioma cells	634:658	Transient ectopic expression of a yellow fluorescent protein (YFP) tagged triple phosphomimic (3-SD) cryAB construct in cryAB absent glioma cells led to the formation of large cytosolic inclusions.
26620801	7	12	with	colocalization	1173:1186	arg1	Rab27					1202:1206	Rab27	1202:1206	Rab27	1202:1206	Additionally, we found that preventing O-GlcNAcylation on cryAB also curtailed its colocalization with CD63 and Rab27 resulting in reduced exosomal secretion.
26620801	7	12	with	colocalization	1173:1186	arg1	CD63					1193:1196	CD63	1193:1196	CD63	1193:1196	Additionally, we found that preventing O-GlcNAcylation on cryAB also curtailed its colocalization with CD63 and Rab27 resulting in reduced exosomal secretion.
26620801	1	13	theme	characterized	154:166	arg1	chaperone					178:186	a well characterized molecular chaperone	147:186	a well characterized molecular chaperone with anti-apoptotic activity	147:215	Exosomes mediate secretion of crystallin alphaB (cryAB), a well characterized molecular chaperone with anti-apoptotic activity.
26620801	1	13	theme	characterized	154:166	arg1	alphaB					131:136	crystallin alphaB	120:136	crystallin alphaB (cryAB)	120:144	Exosomes mediate secretion of crystallin alphaB (cryAB), a well characterized molecular chaperone with anti-apoptotic activity.
26620801	7	14	theme	reduced	1221:1227	arg1	secretion					1238:1246	reduced exosomal secretion	1221:1246	reduced exosomal secretion	1221:1246	Additionally, we found that preventing O-GlcNAcylation on cryAB also curtailed its colocalization with CD63 and Rab27 resulting in reduced exosomal secretion.
26620801	0	15	from	secretion	54:62	arg1	cells					83:87	glioma cells	76:87	glioma cells	76:87	Phosphorylation negatively regulates exosome mediated secretion of cryAB in glioma cells.
26620801	1	16	theme	molecular	168:176	arg1	chaperone					178:186	a well characterized molecular chaperone	147:186	a well characterized molecular chaperone with anti-apoptotic activity	147:215	Exosomes mediate secretion of crystallin alphaB (cryAB), a well characterized molecular chaperone with anti-apoptotic activity.
26620801	1	16	theme	molecular	168:176	arg1	alphaB					131:136	crystallin alphaB	120:136	crystallin alphaB (cryAB)	120:144	Exosomes mediate secretion of crystallin alphaB (cryAB), a well characterized molecular chaperone with anti-apoptotic activity.
26620801	6	17	with	colocalization	840:853	arg1	MVE					903:905	MVE	903:905	MVE	903:905	Moreover, decreased colocalization of 3-SD YFP-cryAB with multivesicular endosome (MVE) and exosome marker, CD63 or Rab27, a small GTPase regulating exocytosis of MVEs, suggests that phosphorylation deters packaging of cryAB in vesicles bound for secretion as exosomes.
26620801	6	17	with	colocalization	840:853	arg1	endosome					893:900	multivesicular endosome	878:900	multivesicular endosome (MVE)	878:906	Moreover, decreased colocalization of 3-SD YFP-cryAB with multivesicular endosome (MVE) and exosome marker, CD63 or Rab27, a small GTPase regulating exocytosis of MVEs, suggests that phosphorylation deters packaging of cryAB in vesicles bound for secretion as exosomes.
26620801	6	17	with	colocalization	840:853	arg1	marker					920:925	exosome marker	912:925	exosome marker	912:925	Moreover, decreased colocalization of 3-SD YFP-cryAB with multivesicular endosome (MVE) and exosome marker, CD63 or Rab27, a small GTPase regulating exocytosis of MVEs, suggests that phosphorylation deters packaging of cryAB in vesicles bound for secretion as exosomes.
26620801	6	17	with	colocalization	840:853	arg1	GTPase					951:956	a small GTPase	943:956	a small GTPase regulating exocytosis of MVEs	943:986	Moreover, decreased colocalization of 3-SD YFP-cryAB with multivesicular endosome (MVE) and exosome marker, CD63 or Rab27, a small GTPase regulating exocytosis of MVEs, suggests that phosphorylation deters packaging of cryAB in vesicles bound for secretion as exosomes.
26620801	6	18	theme	exosome	912:918	arg1	marker					920:925	exosome marker	912:925	exosome marker	912:925	Moreover, decreased colocalization of 3-SD YFP-cryAB with multivesicular endosome (MVE) and exosome marker, CD63 or Rab27, a small GTPase regulating exocytosis of MVEs, suggests that phosphorylation deters packaging of cryAB in vesicles bound for secretion as exosomes.
26620801	6	18	theme	exosome	912:918	arg1	GTPase					951:956	a small GTPase	943:956	a small GTPase regulating exocytosis of MVEs	943:986	Moreover, decreased colocalization of 3-SD YFP-cryAB with multivesicular endosome (MVE) and exosome marker, CD63 or Rab27, a small GTPase regulating exocytosis of MVEs, suggests that phosphorylation deters packaging of cryAB in vesicles bound for secretion as exosomes.
26620801	6	19	theme	small	945:949	arg1	GTPase					951:956	a small GTPase	943:956	a small GTPase regulating exocytosis of MVEs	943:986	Moreover, decreased colocalization of 3-SD YFP-cryAB with multivesicular endosome (MVE) and exosome marker, CD63 or Rab27, a small GTPase regulating exocytosis of MVEs, suggests that phosphorylation deters packaging of cryAB in vesicles bound for secretion as exosomes.
26620801	6	19	theme	small	945:949	arg1	marker					920:925	exosome marker	912:925	exosome marker	912:925	Moreover, decreased colocalization of 3-SD YFP-cryAB with multivesicular endosome (MVE) and exosome marker, CD63 or Rab27, a small GTPase regulating exocytosis of MVEs, suggests that phosphorylation deters packaging of cryAB in vesicles bound for secretion as exosomes.
26620801	8	20	theme	cryAB	1395:1399	arg1	secretion					1382:1390	secretion	1382:1390	secretion	1382:1390	Thus, our study points to O-GlcNAcylation and lack of phosphorylation as being the selective processes involved in the packaging and secretion of cryAB via exosomes.
26620801	8	20	theme	cryAB	1395:1399	arg1	packaging					1368:1376	packaging	1368:1376	packaging	1368:1376	Thus, our study points to O-GlcNAcylation and lack of phosphorylation as being the selective processes involved in the packaging and secretion of cryAB via exosomes.
26620801	0	21	theme	exosome	37:43	arg1	secretion					54:62	exosome mediated secretion	37:62	exosome mediated secretion of cryAB in glioma cells	37:87	Phosphorylation negatively regulates exosome mediated secretion of cryAB in glioma cells.
26620801	6	22	theme	decreased	830:838	arg1	colocalization					840:853	decreased colocalization	830:853	decreased colocalization of 3-SD YFP-cryAB with multivesicular endosome (MVE) and exosome marker, CD63 or Rab27, a small GTPase regulating exocytosis of MVEs,	830:987	Moreover, decreased colocalization of 3-SD YFP-cryAB with multivesicular endosome (MVE) and exosome marker, CD63 or Rab27, a small GTPase regulating exocytosis of MVEs, suggests that phosphorylation deters packaging of cryAB in vesicles bound for secretion as exosomes.
26620801	3	23	theme	secreted	468:475	arg1	cryAB					486:490	secreted exosomal cryAB	468:490	secreted exosomal cryAB	468:490	In glioma cells, notwithstanding extensive phosphorylation of cryAB at Ser59 followed by Ser45 (Ser19 is largely unphosphorylated), we discovered that the majority of secreted exosomal cryAB is nonphosphorylated.
26620801	6	24	theme	MVEs	983:986	arg1	exocytosis					969:978	exocytosis	969:978	exocytosis of MVEs	969:986	Moreover, decreased colocalization of 3-SD YFP-cryAB with multivesicular endosome (MVE) and exosome marker, CD63 or Rab27, a small GTPase regulating exocytosis of MVEs, suggests that phosphorylation deters packaging of cryAB in vesicles bound for secretion as exosomes.
26620801	3	25	theme	exosomal	477:484	arg1	cryAB					486:490	secreted exosomal cryAB	468:490	secreted exosomal cryAB	468:490	In glioma cells, notwithstanding extensive phosphorylation of cryAB at Ser59 followed by Ser45 (Ser19 is largely unphosphorylated), we discovered that the majority of secreted exosomal cryAB is nonphosphorylated.
26620801	3	26	from	Ser59	372:376	arg1	phosphorylation					344:358	extensive phosphorylation	334:358	extensive phosphorylation of cryAB at Ser59 followed by Ser45 (Ser19 is largely unphosphorylated)	334:430	In glioma cells, notwithstanding extensive phosphorylation of cryAB at Ser59 followed by Ser45 (Ser19 is largely unphosphorylated), we discovered that the majority of secreted exosomal cryAB is nonphosphorylated.
26620801	8	27	theme	phosphorylation	1303:1317	arg1	lack					1295:1298	lack	1295:1298	lack of phosphorylation as being the selective processes involved in the packaging and secretion of cryAB via exosomes	1295:1412	Thus, our study points to O-GlcNAcylation and lack of phosphorylation as being the selective processes involved in the packaging and secretion of cryAB via exosomes.
26620801	8	27	theme	phosphorylation	1303:1317	arg1	O-GlcNAcylation					1275:1289	O-GlcNAcylation	1275:1289	O-GlcNAcylation	1275:1289	Thus, our study points to O-GlcNAcylation and lack of phosphorylation as being the selective processes involved in the packaging and secretion of cryAB via exosomes.
26620801	0	28	theme	mediated	45:52	arg1	secretion					54:62	exosome mediated secretion	37:62	exosome mediated secretion of cryAB in glioma cells	37:87	Phosphorylation negatively regulates exosome mediated secretion of cryAB in glioma cells.
26620801	4	29	theme	yellow	548:553	arg1	YFP					576:578	YFP	576:578	YFP	576:578	Transient ectopic expression of a yellow fluorescent protein (YFP) tagged triple phosphomimic (3-SD) cryAB construct in cryAB absent glioma cells led to the formation of large cytosolic inclusions.
26620801	4	29	theme	yellow	548:553	arg1	protein					567:573	a yellow fluorescent protein	546:573	a yellow fluorescent protein (YFP) tagged triple phosphomimic (3-SD) cryAB construct in cryAB absent glioma cells	546:658	Transient ectopic expression of a yellow fluorescent protein (YFP) tagged triple phosphomimic (3-SD) cryAB construct in cryAB absent glioma cells led to the formation of large cytosolic inclusions.
26620801	4	30	theme	glioma	647:652	arg1	cells					654:658	cryAB absent glioma cells	634:658	cryAB absent glioma cells	634:658	Transient ectopic expression of a yellow fluorescent protein (YFP) tagged triple phosphomimic (3-SD) cryAB construct in cryAB absent glioma cells led to the formation of large cytosolic inclusions.
26620801	0	31	theme	cryAB	67:71	arg1	secretion					54:62	exosome mediated secretion	37:62	exosome mediated secretion of cryAB in glioma cells	37:87	Phosphorylation negatively regulates exosome mediated secretion of cryAB in glioma cells.
26620801	1	32	with	chaperone	178:186	arg1	activity					208:215	anti-apoptotic activity	193:215	anti-apoptotic activity	193:215	Exosomes mediate secretion of crystallin alphaB (cryAB), a well characterized molecular chaperone with anti-apoptotic activity.
26620801	4	33	from	construct	621:629	arg1	cells					654:658	cryAB absent glioma cells	634:658	cryAB absent glioma cells	634:658	Transient ectopic expression of a yellow fluorescent protein (YFP) tagged triple phosphomimic (3-SD) cryAB construct in cryAB absent glioma cells led to the formation of large cytosolic inclusions.
26620801	1	34	theme	crystallin	120:129	arg1	chaperone					178:186	a well characterized molecular chaperone	147:186	a well characterized molecular chaperone with anti-apoptotic activity	147:215	Exosomes mediate secretion of crystallin alphaB (cryAB), a well characterized molecular chaperone with anti-apoptotic activity.
26620801	1	34	theme	crystallin	120:129	arg1	cryAB					139:143	cryAB	139:143	cryAB	139:143	Exosomes mediate secretion of crystallin alphaB (cryAB), a well characterized molecular chaperone with anti-apoptotic activity.
26620801	1	34	theme	crystallin	120:129	arg1	alphaB					131:136	crystallin alphaB	120:136	crystallin alphaB (cryAB)	120:144	Exosomes mediate secretion of crystallin alphaB (cryAB), a well characterized molecular chaperone with anti-apoptotic activity.
26620801	4	35	theme	protein	567:573	arg1	expression					532:541	Transient ectopic expression	514:541	Transient ectopic expression of a yellow fluorescent protein (YFP) tagged triple phosphomimic (3-SD) cryAB construct in cryAB absent glioma cells	514:658	Transient ectopic expression of a yellow fluorescent protein (YFP) tagged triple phosphomimic (3-SD) cryAB construct in cryAB absent glioma cells led to the formation of large cytosolic inclusions.
26620801	1	36	theme	alphaB	131:136	arg1	secretion					107:115	secretion	107:115	secretion of crystallin alphaB (cryAB), a well characterized molecular chaperone with anti-apoptotic activity	107:215	Exosomes mediate secretion of crystallin alphaB (cryAB), a well characterized molecular chaperone with anti-apoptotic activity.
26620801	4	37	theme	fluorescent	555:565	arg1	YFP					576:578	YFP	576:578	YFP	576:578	Transient ectopic expression of a yellow fluorescent protein (YFP) tagged triple phosphomimic (3-SD) cryAB construct in cryAB absent glioma cells led to the formation of large cytosolic inclusions.
26620801	4	37	theme	fluorescent	555:565	arg1	protein					567:573	a yellow fluorescent protein	546:573	a yellow fluorescent protein (YFP) tagged triple phosphomimic (3-SD) cryAB construct in cryAB absent glioma cells	546:658	Transient ectopic expression of a yellow fluorescent protein (YFP) tagged triple phosphomimic (3-SD) cryAB construct in cryAB absent glioma cells led to the formation of large cytosolic inclusions.
26620801	3	38	theme	glioma	304:309	arg1	cells					311:315	glioma cells	304:315	glioma cells	304:315	In glioma cells, notwithstanding extensive phosphorylation of cryAB at Ser59 followed by Ser45 (Ser19 is largely unphosphorylated), we discovered that the majority of secreted exosomal cryAB is nonphosphorylated.
26620801	6	39	theme	multivesicular	878:891	arg1	MVE					903:905	MVE	903:905	MVE	903:905	Moreover, decreased colocalization of 3-SD YFP-cryAB with multivesicular endosome (MVE) and exosome marker, CD63 or Rab27, a small GTPase regulating exocytosis of MVEs, suggests that phosphorylation deters packaging of cryAB in vesicles bound for secretion as exosomes.
26620801	6	39	theme	multivesicular	878:891	arg1	endosome					893:900	multivesicular endosome	878:900	multivesicular endosome (MVE)	878:906	Moreover, decreased colocalization of 3-SD YFP-cryAB with multivesicular endosome (MVE) and exosome marker, CD63 or Rab27, a small GTPase regulating exocytosis of MVEs, suggests that phosphorylation deters packaging of cryAB in vesicles bound for secretion as exosomes.
26620801	5	40	theme	cryAB	790:794	arg1	secretion					796:804	cryAB secretion	790:804	cryAB secretion	790:804	Our findings demonstrate that mimicking phosphorylation significantly reduces cryAB secretion via exosomes.
26620801	3	41	theme	cryAB	486:490	arg1	majority					456:463	the majority	452:463	the majority of secreted exosomal cryAB	452:490	In glioma cells, notwithstanding extensive phosphorylation of cryAB at Ser59 followed by Ser45 (Ser19 is largely unphosphorylated), we discovered that the majority of secreted exosomal cryAB is nonphosphorylated.
26620801	4	42	theme	cryAB	615:619	arg1	construct					621:629	triple phosphomimic (3-SD) cryAB construct	588:629	triple phosphomimic (3-SD) cryAB construct in cryAB absent glioma cells	588:658	Transient ectopic expression of a yellow fluorescent protein (YFP) tagged triple phosphomimic (3-SD) cryAB construct in cryAB absent glioma cells led to the formation of large cytosolic inclusions.
26620801	8	43	theme	selective	1332:1340	arg1	processes					1342:1350	the selective processes	1328:1350	the selective processes involved in the packaging and secretion of cryAB via exosomes	1328:1412	Thus, our study points to O-GlcNAcylation and lack of phosphorylation as being the selective processes involved in the packaging and secretion of cryAB via exosomes.
26620801	0	44	theme	glioma	76:81	arg1	cells					83:87	glioma cells	76:87	glioma cells	76:87	Phosphorylation negatively regulates exosome mediated secretion of cryAB in glioma cells.
26620801	6	45	theme	YFP-cryAB	863:871	arg1	colocalization					840:853	decreased colocalization	830:853	decreased colocalization of 3-SD YFP-cryAB with multivesicular endosome (MVE) and exosome marker, CD63 or Rab27, a small GTPase regulating exocytosis of MVEs,	830:987	Moreover, decreased colocalization of 3-SD YFP-cryAB with multivesicular endosome (MVE) and exosome marker, CD63 or Rab27, a small GTPase regulating exocytosis of MVEs, suggests that phosphorylation deters packaging of cryAB in vesicles bound for secretion as exosomes.
26620801	1	46	theme	anti-apoptotic	193:206	arg1	activity					208:215	anti-apoptotic activity	193:215	anti-apoptotic activity	193:215	Exosomes mediate secretion of crystallin alphaB (cryAB), a well characterized molecular chaperone with anti-apoptotic activity.
26620801	4	47	theme	large	684:688	arg1	inclusions					700:709	large cytosolic inclusions	684:709	large cytosolic inclusions	684:709	Transient ectopic expression of a yellow fluorescent protein (YFP) tagged triple phosphomimic (3-SD) cryAB construct in cryAB absent glioma cells led to the formation of large cytosolic inclusions.
26620801	6	48	theme	cryAB	1039:1043	arg1	packaging					1026:1034	packaging	1026:1034	packaging of cryAB	1026:1043	Moreover, decreased colocalization of 3-SD YFP-cryAB with multivesicular endosome (MVE) and exosome marker, CD63 or Rab27, a small GTPase regulating exocytosis of MVEs, suggests that phosphorylation deters packaging of cryAB in vesicles bound for secretion as exosomes.
26620801	3	49	theme	cryAB	363:367	arg1	phosphorylation					344:358	extensive phosphorylation	334:358	extensive phosphorylation of cryAB at Ser59 followed by Ser45 (Ser19 is largely unphosphorylated)	334:430	In glioma cells, notwithstanding extensive phosphorylation of cryAB at Ser59 followed by Ser45 (Ser19 is largely unphosphorylated), we discovered that the majority of secreted exosomal cryAB is nonphosphorylated.
26620801	4	50	theme	ectopic	524:530	arg1	expression					532:541	Transient ectopic expression	514:541	Transient ectopic expression of a yellow fluorescent protein (YFP) tagged triple phosphomimic (3-SD) cryAB construct in cryAB absent glioma cells	514:658	Transient ectopic expression of a yellow fluorescent protein (YFP) tagged triple phosphomimic (3-SD) cryAB construct in cryAB absent glioma cells led to the formation of large cytosolic inclusions.
26620801	4	51	theme	absent	640:645	arg1	cells					654:658	cryAB absent glioma cells	634:658	cryAB absent glioma cells	634:658	Transient ectopic expression of a yellow fluorescent protein (YFP) tagged triple phosphomimic (3-SD) cryAB construct in cryAB absent glioma cells led to the formation of large cytosolic inclusions.
31521821	10	0	theme	HK2	1238:1240	arg1	cells					1242:1246	HK2 cells	1238:1246	HK2 cells	1238:1246	Collectively, our study indicated that O-GlcNAcylation suppressed the ubiquitination of RAF1, stabilized RAF1 and then modulated the EMT in HK2 cells.
31521821	9	1	dep	in	1015:1016	arg1	vivo					1018:1021	vivo	1018:1021	vivo	1018:1021	The upregulation of RAF1 and O-GlcNAcylation products (O-GlcNAc) in vivo were also observed in unilateral ureteral obstruction (UUO) animal models.
31521821	4	2	theme	current	492:498	arg1	study					500:504	The current study	488:504	The current study	488:504	The current study aimed to determine whether O-GlcNAcylation participates in the regulation of EMT during RIF.
31521821	5	3	theme	HK2	650:652	arg1	cells					654:658	HK2 cells	650:658	HK2 cells	650:658	We proved that O-GlcNAcylation prompted the EMT of HK2 cells.
31521821	8	4	theme	RAF1	890:893	arg1	O-GlcNAcylation					871:885	O-GlcNAcylation	871:885	O-GlcNAcylation of RAF1	871:893	In terms of mechanism, we verified that O-GlcNAcylation of RAF1 inhibited its ubiquitination and thus stabilized RAF1.
31521821	3	5	theme	key	361:363	arg1	modifications					384:396	the key post-translational modifications	357:396	the key post-translational modifications	357:396	O-GlcNAcylation, one of the key post-translational modifications, was rarely mentioned about its role in EMT, especially in EMT during the process of RIF.
31521821	5	6	theme	cells	654:658	arg1	EMT					643:645	the EMT	639:645	the EMT of HK2 cells	639:658	We proved that O-GlcNAcylation prompted the EMT of HK2 cells.
31521821	2	7	theme	post-translational	273:290	arg1	modifications					292:304	post-translational modifications	273:304	post-translational modifications	273:304	Recently the relationship between post-translational modifications and EMT has been reported.
31521821	9	8	theme	unilateral	1045:1054	arg1	obstruction					1065:1075	unilateral ureteral obstruction	1045:1075	unilateral ureteral obstruction (UUO) animal models	1045:1095	The upregulation of RAF1 and O-GlcNAcylation products (O-GlcNAc) in vivo were also observed in unilateral ureteral obstruction (UUO) animal models.
31521821	9	8	theme	unilateral	1045:1054	arg1	UUO					1078:1080	UUO	1078:1080	UUO	1078:1080	The upregulation of RAF1 and O-GlcNAcylation products (O-GlcNAc) in vivo were also observed in unilateral ureteral obstruction (UUO) animal models.
31521821	4	9	theme	EMT	583:585	arg1	regulation					569:578	the regulation	565:578	the regulation of EMT during RIF	565:596	The current study aimed to determine whether O-GlcNAcylation participates in the regulation of EMT during RIF.
31521821	9	10	theme	animal	1083:1088	arg1	models					1090:1095	unilateral ureteral obstruction (UUO) animal models	1045:1095	unilateral ureteral obstruction (UUO) animal models	1045:1095	The upregulation of RAF1 and O-GlcNAcylation products (O-GlcNAc) in vivo were also observed in unilateral ureteral obstruction (UUO) animal models.
31521821	11	11	theme	several	1275:1281	arg1	targets					1287:1293	us several new targets	1272:1293	us several new targets for the treatment of RIF	1272:1318	These results may give us several new targets for the treatment of RIF.
31521821	8	12	theme	mechanism	843:851	arg1	terms					834:838	terms	834:838	terms of mechanism	834:851	In terms of mechanism, we verified that O-GlcNAcylation of RAF1 inhibited its ubiquitination and thus stabilized RAF1.
31521821	10	13	theme	RAF1	1186:1189	arg1	ubiquitination					1168:1181	the ubiquitination	1164:1181	the ubiquitination of RAF1	1164:1189	Collectively, our study indicated that O-GlcNAcylation suppressed the ubiquitination of RAF1, stabilized RAF1 and then modulated the EMT in HK2 cells.
31521821	11	14	theme	new	1283:1285	arg1	targets					1287:1293	us several new targets	1272:1293	us several new targets for the treatment of RIF	1272:1318	These results may give us several new targets for the treatment of RIF.
31521821	9	15	theme	obstruction	1065:1075	arg1	models					1090:1095	unilateral ureteral obstruction (UUO) animal models	1045:1095	unilateral ureteral obstruction (UUO) animal models	1045:1095	The upregulation of RAF1 and O-GlcNAcylation products (O-GlcNAc) in vivo were also observed in unilateral ureteral obstruction (UUO) animal models.
31521821	1	16	theme	important	160:168	arg1	mechanisms					170:179	the most important mechanisms	151:179	the most important mechanisms for the progression of renal interstitial fibrosis (RIF)	151:236	Epithelial-mesenchymal transition (EMT) is considered to be one of the most important mechanisms for the progression of renal interstitial fibrosis (RIF).
31521821	1	17	theme	Epithelial-mesenchymal	84:105	arg1	transition					107:116	Epithelial-mesenchymal transition	84:116	Epithelial-mesenchymal transition (EMT)	84:122	Epithelial-mesenchymal transition (EMT) is considered to be one of the most important mechanisms for the progression of renal interstitial fibrosis (RIF).
31521821	1	17	theme	Epithelial-mesenchymal	84:105	arg1	EMT					119:121	EMT	119:121	EMT	119:121	Epithelial-mesenchymal transition (EMT) is considered to be one of the most important mechanisms for the progression of renal interstitial fibrosis (RIF).
31521821	1	18	theme	mechanisms	170:179	arg1	mechanisms					170:179	the most important mechanisms	151:179	the most important mechanisms for the progression of renal interstitial fibrosis (RIF)	151:236	Epithelial-mesenchymal transition (EMT) is considered to be one of the most important mechanisms for the progression of renal interstitial fibrosis (RIF).
31521821	1	18	theme	mechanisms	170:179	arg1	one					144:146	one	144:146	one	144:146	Epithelial-mesenchymal transition (EMT) is considered to be one of the most important mechanisms for the progression of renal interstitial fibrosis (RIF).
31521821	11	19	theme	us	1272:1273	arg1	targets					1287:1293	us several new targets	1272:1293	us several new targets for the treatment of RIF	1272:1318	These results may give us several new targets for the treatment of RIF.
31521821	10	20	from	EMT	1231:1233	arg1	cells					1242:1246	HK2 cells	1238:1246	HK2 cells	1238:1246	Collectively, our study indicated that O-GlcNAcylation suppressed the ubiquitination of RAF1, stabilized RAF1 and then modulated the EMT in HK2 cells.
31521821	7	21	theme	HK2	820:822	arg1	cells					824:828	HK2 cells	820:828	HK2 cells	820:828	Moreover, O-GlcNAcylation of RAF1 stabilized RAF1 protein and prompted EMT of HK2 cells.
31521821	3	22	theme	post-translational	365:382	arg1	modifications					384:396	the key post-translational modifications	357:396	the key post-translational modifications	357:396	O-GlcNAcylation, one of the key post-translational modifications, was rarely mentioned about its role in EMT, especially in EMT during the process of RIF.
31521821	6	23	theme	O-GlcNAcylated	717:730	arg1	proteins					732:739	the O-GlcNAcylated proteins	713:739	the O-GlcNAcylated proteins	713:739	Mass spectral analysis identified RAF1 to be one of the O-GlcNAcylated proteins.
31521821	6	24	theme	spectral	666:673	arg1	analysis					675:682	Mass spectral analysis	661:682	Mass spectral analysis	661:682	Mass spectral analysis identified RAF1 to be one of the O-GlcNAcylated proteins.
31521821	3	25	theme	modifications	384:396	arg1	O-GlcNAcylation					333:347	O-GlcNAcylation	333:347	O-GlcNAcylation	333:347	O-GlcNAcylation, one of the key post-translational modifications, was rarely mentioned about its role in EMT, especially in EMT during the process of RIF.
31521821	3	25	theme	modifications	384:396	arg1	modifications					384:396	the key post-translational modifications	357:396	the key post-translational modifications	357:396	O-GlcNAcylation, one of the key post-translational modifications, was rarely mentioned about its role in EMT, especially in EMT during the process of RIF.
31521821	3	25	theme	modifications	384:396	arg1	one					350:352	one	350:352	one	350:352	O-GlcNAcylation, one of the key post-translational modifications, was rarely mentioned about its role in EMT, especially in EMT during the process of RIF.
31521821	7	26	theme	RAF1	787:790	arg1	protein					792:798	RAF1 protein	787:798	RAF1 protein	787:798	Moreover, O-GlcNAcylation of RAF1 stabilized RAF1 protein and prompted EMT of HK2 cells.
31521821	6	27	theme	Mass	661:664	arg1	analysis					675:682	Mass spectral analysis	661:682	Mass spectral analysis	661:682	Mass spectral analysis identified RAF1 to be one of the O-GlcNAcylated proteins.
31521821	9	28	theme	ureteral	1056:1063	arg1	obstruction					1065:1075	unilateral ureteral obstruction	1045:1075	unilateral ureteral obstruction (UUO) animal models	1045:1095	The upregulation of RAF1 and O-GlcNAcylation products (O-GlcNAc) in vivo were also observed in unilateral ureteral obstruction (UUO) animal models.
31521821	9	28	theme	ureteral	1056:1063	arg1	UUO					1078:1080	UUO	1078:1080	UUO	1078:1080	The upregulation of RAF1 and O-GlcNAcylation products (O-GlcNAc) in vivo were also observed in unilateral ureteral obstruction (UUO) animal models.
31521821	9	29	theme	O-GlcNAcylation	979:993	arg1	O-GlcNAc					1005:1012	O-GlcNAc	1005:1012	O-GlcNAc	1005:1012	The upregulation of RAF1 and O-GlcNAcylation products (O-GlcNAc) in vivo were also observed in unilateral ureteral obstruction (UUO) animal models.
31521821	9	29	theme	O-GlcNAcylation	979:993	arg1	products					995:1002	RAF1 and O-GlcNAcylation products	970:1002	RAF1 and O-GlcNAcylation products (O-GlcNAc) in vivo	970:1021	The upregulation of RAF1 and O-GlcNAcylation products (O-GlcNAc) in vivo were also observed in unilateral ureteral obstruction (UUO) animal models.
31521821	7	30	theme	RAF1	771:774	arg1	O-GlcNAcylation					752:766	O-GlcNAcylation	752:766	O-GlcNAcylation of RAF1	752:774	Moreover, O-GlcNAcylation of RAF1 stabilized RAF1 protein and prompted EMT of HK2 cells.
31521821	1	31	theme	renal	204:208	arg1	RIF					233:235	RIF	233:235	RIF	233:235	Epithelial-mesenchymal transition (EMT) is considered to be one of the most important mechanisms for the progression of renal interstitial fibrosis (RIF).
31521821	1	31	theme	renal	204:208	arg1	fibrosis					223:230	renal interstitial fibrosis	204:230	renal interstitial fibrosis (RIF)	204:236	Epithelial-mesenchymal transition (EMT) is considered to be one of the most important mechanisms for the progression of renal interstitial fibrosis (RIF).
31521821	9	32	theme	products	995:1002	arg1	upregulation					954:965	The upregulation	950:965	The upregulation of RAF1 and O-GlcNAcylation products (O-GlcNAc) in vivo	950:1021	The upregulation of RAF1 and O-GlcNAcylation products (O-GlcNAc) in vivo were also observed in unilateral ureteral obstruction (UUO) animal models.
31521821	11	33	theme	RIF	1316:1318	arg1	treatment					1303:1311	the treatment	1299:1311	the treatment of RIF	1299:1318	These results may give us several new targets for the treatment of RIF.
31521821	3	34	theme	RIF	483:485	arg1	process					472:478	the process	468:478	the process of RIF	468:485	O-GlcNAcylation, one of the key post-translational modifications, was rarely mentioned about its role in EMT, especially in EMT during the process of RIF.
31521821	6	35	theme	proteins	732:739	arg1	one					706:708	one	706:708	one	706:708	Mass spectral analysis identified RAF1 to be one of the O-GlcNAcylated proteins.
31521821	6	35	theme	proteins	732:739	arg1	proteins					732:739	the O-GlcNAcylated proteins	713:739	the O-GlcNAcylated proteins	713:739	Mass spectral analysis identified RAF1 to be one of the O-GlcNAcylated proteins.
31521821	1	36	theme	interstitial	210:221	arg1	RIF					233:235	RIF	233:235	RIF	233:235	Epithelial-mesenchymal transition (EMT) is considered to be one of the most important mechanisms for the progression of renal interstitial fibrosis (RIF).
31521821	1	36	theme	interstitial	210:221	arg1	fibrosis					223:230	renal interstitial fibrosis	204:230	renal interstitial fibrosis (RIF)	204:236	Epithelial-mesenchymal transition (EMT) is considered to be one of the most important mechanisms for the progression of renal interstitial fibrosis (RIF).
31521821	3	37	from	role	430:433	arg1	EMT					438:440	EMT	438:440	EMT	438:440	O-GlcNAcylation, one of the key post-translational modifications, was rarely mentioned about its role in EMT, especially in EMT during the process of RIF.
31521821	3	37	from	role	430:433	arg1	EMT					457:459	EMT	457:459	EMT	457:459	O-GlcNAcylation, one of the key post-translational modifications, was rarely mentioned about its role in EMT, especially in EMT during the process of RIF.
31521821	7	38	theme	cells	824:828	arg1	EMT					813:815	EMT	813:815	EMT of HK2 cells	813:828	Moreover, O-GlcNAcylation of RAF1 stabilized RAF1 protein and prompted EMT of HK2 cells.
31521821	9	39	theme	in	1015:1016	arg1	O-GlcNAc					1005:1012	O-GlcNAc	1005:1012	O-GlcNAc	1005:1012	The upregulation of RAF1 and O-GlcNAcylation products (O-GlcNAc) in vivo were also observed in unilateral ureteral obstruction (UUO) animal models.
31521821	9	39	theme	in	1015:1016	arg1	products					995:1002	RAF1 and O-GlcNAcylation products	970:1002	RAF1 and O-GlcNAcylation products (O-GlcNAc) in vivo	970:1021	The upregulation of RAF1 and O-GlcNAcylation products (O-GlcNAc) in vivo were also observed in unilateral ureteral obstruction (UUO) animal models.
31521821	1	40	theme	fibrosis	223:230	arg1	progression					189:199	the progression	185:199	the progression of renal interstitial fibrosis (RIF)	185:236	Epithelial-mesenchymal transition (EMT) is considered to be one of the most important mechanisms for the progression of renal interstitial fibrosis (RIF).
31521821	0	41	theme	renal	68:72	arg1	fibrosis					74:81	the renal fibrosis	64:81	the renal fibrosis	64:81	O-GlcNAcylation of RAF1 increases its stabilization and induces the renal fibrosis.
31521821	9	42	located	observed	1033:1040	arg2	upregulation					954:965	The upregulation	950:965	The upregulation of RAF1 and O-GlcNAcylation products (O-GlcNAc) in vivo	950:1021	The upregulation of RAF1 and O-GlcNAcylation products (O-GlcNAc) in vivo were also observed in unilateral ureteral obstruction (UUO) animal models.
31521821	9	42	located	observed	1033:1040	arg1	models					1090:1095	unilateral ureteral obstruction (UUO) animal models	1045:1095	unilateral ureteral obstruction (UUO) animal models	1045:1095	The upregulation of RAF1 and O-GlcNAcylation products (O-GlcNAc) in vivo were also observed in unilateral ureteral obstruction (UUO) animal models.
31521821	0	43	theme	RAF1	19:22	arg1	O-GlcNAcylation					0:14	O-GlcNAcylation	0:14	O-GlcNAcylation of RAF1	0:22	O-GlcNAcylation of RAF1 increases its stabilization and induces the renal fibrosis.
31521821	9	44	theme	RAF1	970:973	arg1	O-GlcNAc					1005:1012	O-GlcNAc	1005:1012	O-GlcNAc	1005:1012	The upregulation of RAF1 and O-GlcNAcylation products (O-GlcNAc) in vivo were also observed in unilateral ureteral obstruction (UUO) animal models.
31521821	9	44	theme	RAF1	970:973	arg1	products					995:1002	RAF1 and O-GlcNAcylation products	970:1002	RAF1 and O-GlcNAcylation products (O-GlcNAc) in vivo	970:1021	The upregulation of RAF1 and O-GlcNAcylation products (O-GlcNAc) in vivo were also observed in unilateral ureteral obstruction (UUO) animal models.
33465208	4	0	theme	enrichment	882:891	arg1	purification					845:856	selective purification	835:856	selective purification of RBPs and HILIC-based enrichment	835:891	In the present study, we developed a tandem enrichment strategy combining metabolic labeling-based RNA tagging for selective purification of RBPs and HILIC-based enrichment for simultaneous O-GlcNAcylation and phosphorylation profiling.
33465208	6	1	theme	RNA-binding	1339:1349	arg1	proteome					1351:1358	the RNA-binding proteome	1335:1358	the RNA-binding proteome	1335:1358	Further HILIC enrichment on the tryptic-digested RBPs and MS analysis led to the first large-scale identification of O-GlcNAcylation and phosphorylation in the RNA-binding proteome, with 461 O-GlcNAc peptides corresponding to 300 RBPs and 671 phosphopeptides corresponding to 389 RBPs.
33465208	4	2	theme	simultaneous	897:908	arg1	O-GlcNAcylation					910:924	simultaneous O-GlcNAcylation	897:924	simultaneous O-GlcNAcylation	897:924	In the present study, we developed a tandem enrichment strategy combining metabolic labeling-based RNA tagging for selective purification of RBPs and HILIC-based enrichment for simultaneous O-GlcNAcylation and phosphorylation profiling.
33465208	8	3	theme	RBPs	1708:1711	arg1	identification					1675:1688	the identification	1671:1688	the identification of O-GlcNAcylated RBPs	1671:1711	This strategy has the advantage of high compatibility with MS and provides peptide-level evidence for the identification of O-GlcNAcylated RBPs.
33465208	3	4	from	profiling	634:642	arg1	RBPs					686:689	RBPs	686:689	RBPs	686:689	However, due to the extremely low abundance of O-GlcNAcylation and the lack of RBP-targeted enrichment strategies, large-scale simultaneous profiling of O-GlcNAcylation and phosphorylation on RBPs is still a challenging task.
33465208	3	5	theme	low	524:526	arg1	abundance					528:536	the extremely low abundance	510:536	the extremely low abundance of O-GlcNAcylation	510:555	However, due to the extremely low abundance of O-GlcNAcylation and the lack of RBP-targeted enrichment strategies, large-scale simultaneous profiling of O-GlcNAcylation and phosphorylation on RBPs is still a challenging task.
33465208	9	6	from	regulation	1888:1897	arg1	elucidation					1831:1841	further elucidation	1823:1841	further elucidation of the crucial roles of OPCT in the function regulation of RBPs	1823:1905	We expect it will support simultaneous mapping of O-GlcNAcylation and phosphorylation on RBPs and facilitate further elucidation of the crucial roles of OPCT in the function regulation of RBPs.
33465208	7	7	theme	%	1483:1483	arg1	RBPs					1485:1488	∼25% RBPs	1480:1488	∼25% RBPs modified by two PTMs	1480:1509	Interestingly, ∼25% RBPs modified by two PTMs were found to be related to multiple metabolism pathways.
33465208	9	8	theme	simultaneous	1740:1751	arg1	mapping					1753:1759	simultaneous mapping	1740:1759	simultaneous mapping of O-GlcNAcylation and phosphorylation on RBPs	1740:1806	We expect it will support simultaneous mapping of O-GlcNAcylation and phosphorylation on RBPs and facilitate further elucidation of the crucial roles of OPCT in the function regulation of RBPs.
33465208	9	9	from	mapping	1753:1759	arg1	RBPs					1803:1806	RBPs	1803:1806	RBPs	1803:1806	We expect it will support simultaneous mapping of O-GlcNAcylation and phosphorylation on RBPs and facilitate further elucidation of the crucial roles of OPCT in the function regulation of RBPs.
33465208	6	10	theme	HILIC	1187:1191	arg1	enrichment					1193:1202	Further HILIC enrichment	1179:1202	Further HILIC enrichment on the tryptic-digested RBPs	1179:1231	Further HILIC enrichment on the tryptic-digested RBPs and MS analysis led to the first large-scale identification of O-GlcNAcylation and phosphorylation in the RNA-binding proteome, with 461 O-GlcNAc peptides corresponding to 300 RBPs and 671 phosphopeptides corresponding to 389 RBPs.
33465208	3	11	theme	RBP-targeted	573:584	arg1	strategies					597:606	RBP-targeted enrichment strategies	573:606	RBP-targeted enrichment strategies	573:606	However, due to the extremely low abundance of O-GlcNAcylation and the lack of RBP-targeted enrichment strategies, large-scale simultaneous profiling of O-GlcNAcylation and phosphorylation on RBPs is still a challenging task.
33465208	0	12	from	profiling	54:62	arg1	proteome					118:125	RNA-binding proteome	106:125	RNA-binding proteome	106:125	A new tandem enrichment strategy for the simultaneous profiling of O-GlcNAcylation and phosphorylation in RNA-binding proteome.
33465208	6	13	theme	first	1260:1264	arg1	identification					1278:1291	the first large-scale identification	1256:1291	the first large-scale identification of O-GlcNAcylation and phosphorylation in the RNA-binding proteome	1256:1358	Further HILIC enrichment on the tryptic-digested RBPs and MS analysis led to the first large-scale identification of O-GlcNAcylation and phosphorylation in the RNA-binding proteome, with 461 O-GlcNAc peptides corresponding to 300 RBPs and 671 phosphopeptides corresponding to 389 RBPs.
33465208	1	14	theme	RNA-protein	128:138	arg1	interactions					140:151	RNA-protein interactions	128:151	RNA-protein interactions	128:151	RNA-protein interactions play important roles in almost every step of the lifetime of RNAs, such as RNA splicing, transporting, localization, translation and degradation.
33465208	3	15	theme	large-scale	609:619	arg1	profiling					634:642	large-scale simultaneous profiling	609:642	large-scale simultaneous profiling of O-GlcNAcylation and phosphorylation on RBPs	609:689	However, due to the extremely low abundance of O-GlcNAcylation and the lack of RBP-targeted enrichment strategies, large-scale simultaneous profiling of O-GlcNAcylation and phosphorylation on RBPs is still a challenging task.
33465208	3	15	theme	large-scale	609:619	arg1	task					714:717	still a challenging task	694:717	still a challenging task	694:717	However, due to the extremely low abundance of O-GlcNAcylation and the lack of RBP-targeted enrichment strategies, large-scale simultaneous profiling of O-GlcNAcylation and phosphorylation on RBPs is still a challenging task.
33465208	9	16	theme	further	1823:1829	arg1	elucidation					1831:1841	further elucidation	1823:1841	further elucidation of the crucial roles of OPCT in the function regulation of RBPs	1823:1905	We expect it will support simultaneous mapping of O-GlcNAcylation and phosphorylation on RBPs and facilitate further elucidation of the crucial roles of OPCT in the function regulation of RBPs.
33465208	6	17	theme	389	1455:1457	arg1	RBPs					1459:1462	389 RBPs	1455:1462	389 RBPs	1455:1462	Further HILIC enrichment on the tryptic-digested RBPs and MS analysis led to the first large-scale identification of O-GlcNAcylation and phosphorylation in the RNA-binding proteome, with 461 O-GlcNAc peptides corresponding to 300 RBPs and 671 phosphopeptides corresponding to 389 RBPs.
33465208	3	18	theme	strategies	597:606	arg1	lack					565:568	the lack	561:568	the lack of RBP-targeted enrichment strategies	561:606	However, due to the extremely low abundance of O-GlcNAcylation and the lack of RBP-targeted enrichment strategies, large-scale simultaneous profiling of O-GlcNAcylation and phosphorylation on RBPs is still a challenging task.
33465208	3	18	theme	strategies	597:606	arg1	abundance					528:536	the extremely low abundance	510:536	the extremely low abundance of O-GlcNAcylation	510:555	However, due to the extremely low abundance of O-GlcNAcylation and the lack of RBP-targeted enrichment strategies, large-scale simultaneous profiling of O-GlcNAcylation and phosphorylation on RBPs is still a challenging task.
33465208	0	19	theme	O-GlcNAcylation	67:81	arg1	profiling					54:62	the simultaneous profiling	37:62	the simultaneous profiling of O-GlcNAcylation and phosphorylation in RNA-binding proteome	37:125	A new tandem enrichment strategy for the simultaneous profiling of O-GlcNAcylation and phosphorylation in RNA-binding proteome.
33465208	9	20	theme	crucial	1850:1856	arg1	roles					1858:1862	the crucial roles	1846:1862	the crucial roles of OPCT in the function regulation of RBPs	1846:1905	We expect it will support simultaneous mapping of O-GlcNAcylation and phosphorylation on RBPs and facilitate further elucidation of the crucial roles of OPCT in the function regulation of RBPs.
33465208	0	21	theme	phosphorylation	87:101	arg1	profiling					54:62	the simultaneous profiling	37:62	the simultaneous profiling of O-GlcNAcylation and phosphorylation in RNA-binding proteome	37:125	A new tandem enrichment strategy for the simultaneous profiling of O-GlcNAcylation and phosphorylation in RNA-binding proteome.
33465208	5	22	theme	quantitative	1133:1144	arg1	spectrometry					1151:1162	quantitative mass spectrometry	1133:1162	quantitative mass spectrometry (MS) analysis	1133:1176	Benefiting from the sequence-independent RNA tagging by ethynyluridine (EU) labeling, 1115 RBPs binding to different types of RNAs were successfully enriched and identified by quantitative mass spectrometry (MS) analysis.
33465208	5	22	theme	quantitative	1133:1144	arg1	MS					1165:1166	MS	1165:1166	MS	1165:1166	Benefiting from the sequence-independent RNA tagging by ethynyluridine (EU) labeling, 1115 RBPs binding to different types of RNAs were successfully enriched and identified by quantitative mass spectrometry (MS) analysis.
33465208	4	23	theme	enrichment	764:773	arg1	strategy					775:782	a tandem enrichment strategy	755:782	a tandem enrichment strategy combining metabolic labeling-based RNA tagging for selective purification of RBPs and HILIC-based enrichment for simultaneous O-GlcNAcylation and phosphorylation profiling	755:954	In the present study, we developed a tandem enrichment strategy combining metabolic labeling-based RNA tagging for selective purification of RBPs and HILIC-based enrichment for simultaneous O-GlcNAcylation and phosphorylation profiling.
33465208	0	24	theme	RNA-binding	106:116	arg1	proteome					118:125	RNA-binding proteome	106:125	RNA-binding proteome	106:125	A new tandem enrichment strategy for the simultaneous profiling of O-GlcNAcylation and phosphorylation in RNA-binding proteome.
33465208	5	25	theme	spectrometry	1151:1162	arg1	analysis					1169:1176	quantitative mass spectrometry (MS) analysis	1133:1176	quantitative mass spectrometry (MS) analysis	1133:1176	Benefiting from the sequence-independent RNA tagging by ethynyluridine (EU) labeling, 1115 RBPs binding to different types of RNAs were successfully enriched and identified by quantitative mass spectrometry (MS) analysis.
33465208	2	26	theme	cross-talk	389:398	arg1	"					399:399	their "cross-talk"	382:399	their "cross-talk" (OPCT)	382:406	Post-translational modifications, such as O-GlcNAcylation and phosphorylation, and their "cross-talk" (OPCT) are essential to the activity and function regulation of RNA-binding proteins (RBPs).
33465208	2	26	theme	cross-talk	389:398	arg1	OPCT					402:405	OPCT	402:405	OPCT	402:405	Post-translational modifications, such as O-GlcNAcylation and phosphorylation, and their "cross-talk" (OPCT) are essential to the activity and function regulation of RNA-binding proteins (RBPs).
33465208	2	27	dep	activity	429:436	arg1	regulation					451:460	regulation	451:460	regulation	451:460	Post-translational modifications, such as O-GlcNAcylation and phosphorylation, and their "cross-talk" (OPCT) are essential to the activity and function regulation of RNA-binding proteins (RBPs).
33465208	2	27	dep	activity	429:436	arg1	the					425:427	the	425:427	the	425:427	Post-translational modifications, such as O-GlcNAcylation and phosphorylation, and their "cross-talk" (OPCT) are essential to the activity and function regulation of RNA-binding proteins (RBPs).
33465208	5	28	theme	RNA	998:1000	arg1	tagging					1002:1008	the sequence-independent RNA tagging	973:1008	the sequence-independent RNA tagging by ethynyluridine (EU) labeling	973:1040	Benefiting from the sequence-independent RNA tagging by ethynyluridine (EU) labeling, 1115 RBPs binding to different types of RNAs were successfully enriched and identified by quantitative mass spectrometry (MS) analysis.
33465208	9	29	theme	function	1879:1886	arg1	regulation					1888:1897	the function regulation	1875:1897	the function regulation of RBPs	1875:1905	We expect it will support simultaneous mapping of O-GlcNAcylation and phosphorylation on RBPs and facilitate further elucidation of the crucial roles of OPCT in the function regulation of RBPs.
33465208	0	30	theme	tandem	6:11	arg1	strategy					24:31	A new tandem enrichment strategy	0:31	A new tandem enrichment strategy for the simultaneous profiling of O-GlcNAcylation and phosphorylation in RNA-binding proteome.	0:126	A new tandem enrichment strategy for the simultaneous profiling of O-GlcNAcylation and phosphorylation in RNA-binding proteome.
33465208	6	31	theme	tryptic-digested	1211:1226	arg1	RBPs					1228:1231	the tryptic-digested RBPs	1207:1231	the tryptic-digested RBPs	1207:1231	Further HILIC enrichment on the tryptic-digested RBPs and MS analysis led to the first large-scale identification of O-GlcNAcylation and phosphorylation in the RNA-binding proteome, with 461 O-GlcNAc peptides corresponding to 300 RBPs and 671 phosphopeptides corresponding to 389 RBPs.
33465208	2	32	theme	RNA-binding	465:475	arg1	RBPs					487:490	RBPs	487:490	RBPs	487:490	Post-translational modifications, such as O-GlcNAcylation and phosphorylation, and their "cross-talk" (OPCT) are essential to the activity and function regulation of RNA-binding proteins (RBPs).
33465208	2	32	theme	RNA-binding	465:475	arg1	proteins					477:484	RNA-binding proteins	465:484	RNA-binding proteins (RBPs)	465:491	Post-translational modifications, such as O-GlcNAcylation and phosphorylation, and their "cross-talk" (OPCT) are essential to the activity and function regulation of RNA-binding proteins (RBPs).
33465208	8	33	theme	high	1604:1607	arg1	compatibility					1609:1621	high compatibility	1604:1621	high compatibility with MS	1604:1629	This strategy has the advantage of high compatibility with MS and provides peptide-level evidence for the identification of O-GlcNAcylated RBPs.
33465208	3	34	theme	O-GlcNAcylation	647:661	arg1	profiling					634:642	large-scale simultaneous profiling	609:642	large-scale simultaneous profiling of O-GlcNAcylation and phosphorylation on RBPs	609:689	However, due to the extremely low abundance of O-GlcNAcylation and the lack of RBP-targeted enrichment strategies, large-scale simultaneous profiling of O-GlcNAcylation and phosphorylation on RBPs is still a challenging task.
33465208	3	34	theme	O-GlcNAcylation	647:661	arg1	task					714:717	still a challenging task	694:717	still a challenging task	694:717	However, due to the extremely low abundance of O-GlcNAcylation and the lack of RBP-targeted enrichment strategies, large-scale simultaneous profiling of O-GlcNAcylation and phosphorylation on RBPs is still a challenging task.
33465208	6	35	from	enrichment	1193:1202	arg1	RBPs					1228:1231	the tryptic-digested RBPs	1207:1231	the tryptic-digested RBPs	1207:1231	Further HILIC enrichment on the tryptic-digested RBPs and MS analysis led to the first large-scale identification of O-GlcNAcylation and phosphorylation in the RNA-binding proteome, with 461 O-GlcNAc peptides corresponding to 300 RBPs and 671 phosphopeptides corresponding to 389 RBPs.
33465208	4	36	theme	selective	835:843	arg1	purification					845:856	selective purification	835:856	selective purification of RBPs and HILIC-based enrichment	835:891	In the present study, we developed a tandem enrichment strategy combining metabolic labeling-based RNA tagging for selective purification of RBPs and HILIC-based enrichment for simultaneous O-GlcNAcylation and phosphorylation profiling.
33465208	7	37	theme	multiple	1539:1546	arg1	pathways					1559:1566	multiple metabolism pathways	1539:1566	multiple metabolism pathways	1539:1566	Interestingly, ∼25% RBPs modified by two PTMs were found to be related to multiple metabolism pathways.
33465208	8	38	theme	peptide-level	1644:1656	arg1	evidence					1658:1665	peptide-level evidence	1644:1665	peptide-level evidence for the identification of O-GlcNAcylated RBPs	1644:1711	This strategy has the advantage of high compatibility with MS and provides peptide-level evidence for the identification of O-GlcNAcylated RBPs.
33465208	3	39	theme	phosphorylation	667:681	arg1	profiling					634:642	large-scale simultaneous profiling	609:642	large-scale simultaneous profiling of O-GlcNAcylation and phosphorylation on RBPs	609:689	However, due to the extremely low abundance of O-GlcNAcylation and the lack of RBP-targeted enrichment strategies, large-scale simultaneous profiling of O-GlcNAcylation and phosphorylation on RBPs is still a challenging task.
33465208	3	39	theme	phosphorylation	667:681	arg1	task					714:717	still a challenging task	694:717	still a challenging task	694:717	However, due to the extremely low abundance of O-GlcNAcylation and the lack of RBP-targeted enrichment strategies, large-scale simultaneous profiling of O-GlcNAcylation and phosphorylation on RBPs is still a challenging task.
33465208	4	40	theme	labeling-based	804:817	arg1	tagging					823:829	metabolic labeling-based RNA tagging	794:829	metabolic labeling-based RNA tagging for selective purification of RBPs and HILIC-based enrichment for simultaneous O-GlcNAcylation and phosphorylation profiling	794:954	In the present study, we developed a tandem enrichment strategy combining metabolic labeling-based RNA tagging for selective purification of RBPs and HILIC-based enrichment for simultaneous O-GlcNAcylation and phosphorylation profiling.
33465208	6	41	from	proteome	1351:1358	arg1	identification					1278:1291	the first large-scale identification	1256:1291	the first large-scale identification of O-GlcNAcylation and phosphorylation in the RNA-binding proteome	1256:1358	Further HILIC enrichment on the tryptic-digested RBPs and MS analysis led to the first large-scale identification of O-GlcNAcylation and phosphorylation in the RNA-binding proteome, with 461 O-GlcNAc peptides corresponding to 300 RBPs and 671 phosphopeptides corresponding to 389 RBPs.
33465208	3	42	theme	challenging	702:712	arg1	profiling					634:642	large-scale simultaneous profiling	609:642	large-scale simultaneous profiling of O-GlcNAcylation and phosphorylation on RBPs	609:689	However, due to the extremely low abundance of O-GlcNAcylation and the lack of RBP-targeted enrichment strategies, large-scale simultaneous profiling of O-GlcNAcylation and phosphorylation on RBPs is still a challenging task.
33465208	3	42	theme	challenging	702:712	arg1	task					714:717	still a challenging task	694:717	still a challenging task	694:717	However, due to the extremely low abundance of O-GlcNAcylation and the lack of RBP-targeted enrichment strategies, large-scale simultaneous profiling of O-GlcNAcylation and phosphorylation on RBPs is still a challenging task.
33465208	6	43	from	O-GlcNAcylation	1296:1310	arg1	proteome					1351:1358	the RNA-binding proteome	1335:1358	the RNA-binding proteome	1335:1358	Further HILIC enrichment on the tryptic-digested RBPs and MS analysis led to the first large-scale identification of O-GlcNAcylation and phosphorylation in the RNA-binding proteome, with 461 O-GlcNAc peptides corresponding to 300 RBPs and 671 phosphopeptides corresponding to 389 RBPs.
33465208	4	44	theme	HILIC-based	870:880	arg1	enrichment					882:891	HILIC-based enrichment	870:891	HILIC-based enrichment	870:891	In the present study, we developed a tandem enrichment strategy combining metabolic labeling-based RNA tagging for selective purification of RBPs and HILIC-based enrichment for simultaneous O-GlcNAcylation and phosphorylation profiling.
33465208	6	45	from	phosphorylation	1316:1330	arg1	proteome					1351:1358	the RNA-binding proteome	1335:1358	the RNA-binding proteome	1335:1358	Further HILIC enrichment on the tryptic-digested RBPs and MS analysis led to the first large-scale identification of O-GlcNAcylation and phosphorylation in the RNA-binding proteome, with 461 O-GlcNAc peptides corresponding to 300 RBPs and 671 phosphopeptides corresponding to 389 RBPs.
33465208	8	46	contain	has	1583:1585	arg1	strategy					1574:1581	This strategy	1569:1581	This strategy	1569:1581	This strategy has the advantage of high compatibility with MS and provides peptide-level evidence for the identification of O-GlcNAcylated RBPs.
33465208	8	46	contain	has	1583:1585	arg2	advantage					1591:1599	the advantage	1587:1599	the advantage of high compatibility with MS	1587:1629	This strategy has the advantage of high compatibility with MS and provides peptide-level evidence for the identification of O-GlcNAcylated RBPs.
33465208	8	47	theme	O-GlcNAcylated	1693:1706	arg1	RBPs					1708:1711	O-GlcNAcylated RBPs	1693:1711	O-GlcNAcylated RBPs	1693:1711	This strategy has the advantage of high compatibility with MS and provides peptide-level evidence for the identification of O-GlcNAcylated RBPs.
33465208	6	48	theme	phosphorylation	1316:1330	arg1	identification					1278:1291	the first large-scale identification	1256:1291	the first large-scale identification of O-GlcNAcylation and phosphorylation in the RNA-binding proteome	1256:1358	Further HILIC enrichment on the tryptic-digested RBPs and MS analysis led to the first large-scale identification of O-GlcNAcylation and phosphorylation in the RNA-binding proteome, with 461 O-GlcNAc peptides corresponding to 300 RBPs and 671 phosphopeptides corresponding to 389 RBPs.
33465208	1	49	theme	every	184:188	arg1	step					190:193	almost every step	177:193	almost every step of the lifetime of RNAs, such as RNA splicing, transporting, localization, translation and degradation	177:296	RNA-protein interactions play important roles in almost every step of the lifetime of RNAs, such as RNA splicing, transporting, localization, translation and degradation.
33465208	6	50	theme	O-GlcNAcylation	1296:1310	arg1	identification					1278:1291	the first large-scale identification	1256:1291	the first large-scale identification of O-GlcNAcylation and phosphorylation in the RNA-binding proteome	1256:1358	Further HILIC enrichment on the tryptic-digested RBPs and MS analysis led to the first large-scale identification of O-GlcNAcylation and phosphorylation in the RNA-binding proteome, with 461 O-GlcNAc peptides corresponding to 300 RBPs and 671 phosphopeptides corresponding to 389 RBPs.
33465208	3	51	theme	O-GlcNAcylation	541:555	arg1	lack					565:568	the lack	561:568	the lack of RBP-targeted enrichment strategies	561:606	However, due to the extremely low abundance of O-GlcNAcylation and the lack of RBP-targeted enrichment strategies, large-scale simultaneous profiling of O-GlcNAcylation and phosphorylation on RBPs is still a challenging task.
33465208	3	51	theme	O-GlcNAcylation	541:555	arg1	abundance					528:536	the extremely low abundance	510:536	the extremely low abundance of O-GlcNAcylation	510:555	However, due to the extremely low abundance of O-GlcNAcylation and the lack of RBP-targeted enrichment strategies, large-scale simultaneous profiling of O-GlcNAcylation and phosphorylation on RBPs is still a challenging task.
33465208	4	52	theme	RBPs	861:864	arg1	purification					845:856	selective purification	835:856	selective purification of RBPs and HILIC-based enrichment	835:891	In the present study, we developed a tandem enrichment strategy combining metabolic labeling-based RNA tagging for selective purification of RBPs and HILIC-based enrichment for simultaneous O-GlcNAcylation and phosphorylation profiling.
33465208	7	53	theme	∼25	1480:1482	arg1	RBPs					1485:1488	∼25% RBPs	1480:1488	∼25% RBPs modified by two PTMs	1480:1509	Interestingly, ∼25% RBPs modified by two PTMs were found to be related to multiple metabolism pathways.
33465208	2	54	theme	Post-translational	299:316	arg1	O-GlcNAcylation					341:355	O-GlcNAcylation	341:355	O-GlcNAcylation	341:355	Post-translational modifications, such as O-GlcNAcylation and phosphorylation, and their "cross-talk" (OPCT) are essential to the activity and function regulation of RNA-binding proteins (RBPs).
33465208	2	54	theme	Post-translational	299:316	arg1	modifications					318:330	Post-translational modifications	299:330	Post-translational modifications	299:330	Post-translational modifications, such as O-GlcNAcylation and phosphorylation, and their "cross-talk" (OPCT) are essential to the activity and function regulation of RNA-binding proteins (RBPs).
33465208	2	54	theme	Post-translational	299:316	arg1	phosphorylation					361:375	phosphorylation	361:375	phosphorylation	361:375	Post-translational modifications, such as O-GlcNAcylation and phosphorylation, and their "cross-talk" (OPCT) are essential to the activity and function regulation of RNA-binding proteins (RBPs).
33465208	1	55	theme	lifetime	202:209	arg1	step					190:193	almost every step	177:193	almost every step of the lifetime of RNAs, such as RNA splicing, transporting, localization, translation and degradation	177:296	RNA-protein interactions play important roles in almost every step of the lifetime of RNAs, such as RNA splicing, transporting, localization, translation and degradation.
33465208	9	56	theme	O-GlcNAcylation	1764:1778	arg1	mapping					1753:1759	simultaneous mapping	1740:1759	simultaneous mapping of O-GlcNAcylation and phosphorylation on RBPs	1740:1806	We expect it will support simultaneous mapping of O-GlcNAcylation and phosphorylation on RBPs and facilitate further elucidation of the crucial roles of OPCT in the function regulation of RBPs.
33465208	6	57	theme	Further	1179:1185	arg1	enrichment					1193:1202	Further HILIC enrichment	1179:1202	Further HILIC enrichment on the tryptic-digested RBPs	1179:1231	Further HILIC enrichment on the tryptic-digested RBPs and MS analysis led to the first large-scale identification of O-GlcNAcylation and phosphorylation in the RNA-binding proteome, with 461 O-GlcNAc peptides corresponding to 300 RBPs and 671 phosphopeptides corresponding to 389 RBPs.
33465208	8	58	with	compatibility	1609:1621	arg1	MS					1628:1629	MS	1628:1629	MS	1628:1629	This strategy has the advantage of high compatibility with MS and provides peptide-level evidence for the identification of O-GlcNAcylated RBPs.
33465208	1	59	theme	RNAs	214:217	arg1	lifetime					202:209	the lifetime	198:209	the lifetime of RNAs, such as RNA splicing, transporting, localization, translation and degradation	198:296	RNA-protein interactions play important roles in almost every step of the lifetime of RNAs, such as RNA splicing, transporting, localization, translation and degradation.
33465208	9	60	theme	phosphorylation	1784:1798	arg1	mapping					1753:1759	simultaneous mapping	1740:1759	simultaneous mapping of O-GlcNAcylation and phosphorylation on RBPs	1740:1806	We expect it will support simultaneous mapping of O-GlcNAcylation and phosphorylation on RBPs and facilitate further elucidation of the crucial roles of OPCT in the function regulation of RBPs.
33465208	6	61	theme	large-scale	1266:1276	arg1	identification					1278:1291	the first large-scale identification	1256:1291	the first large-scale identification of O-GlcNAcylation and phosphorylation in the RNA-binding proteome	1256:1358	Further HILIC enrichment on the tryptic-digested RBPs and MS analysis led to the first large-scale identification of O-GlcNAcylation and phosphorylation in the RNA-binding proteome, with 461 O-GlcNAc peptides corresponding to 300 RBPs and 671 phosphopeptides corresponding to 389 RBPs.
33465208	6	62	theme	O-GlcNAc	1370:1377	arg1	peptides					1379:1386	461 O-GlcNAc peptides	1366:1386	461 O-GlcNAc peptides corresponding to 300 RBPs and 671 phosphopeptides corresponding to 389 RBPs	1366:1462	Further HILIC enrichment on the tryptic-digested RBPs and MS analysis led to the first large-scale identification of O-GlcNAcylation and phosphorylation in the RNA-binding proteome, with 461 O-GlcNAc peptides corresponding to 300 RBPs and 671 phosphopeptides corresponding to 389 RBPs.
33465208	5	63	theme	RNAs	1083:1086	arg1	types					1074:1078	different types	1064:1078	different types of RNAs	1064:1086	Benefiting from the sequence-independent RNA tagging by ethynyluridine (EU) labeling, 1115 RBPs binding to different types of RNAs were successfully enriched and identified by quantitative mass spectrometry (MS) analysis.
33465208	4	64	theme	phosphorylation	930:944	arg1	profiling					946:954	phosphorylation profiling	930:954	phosphorylation profiling	930:954	In the present study, we developed a tandem enrichment strategy combining metabolic labeling-based RNA tagging for selective purification of RBPs and HILIC-based enrichment for simultaneous O-GlcNAcylation and phosphorylation profiling.
33465208	6	65	from	identification	1278:1291	arg1	proteome					1351:1358	the RNA-binding proteome	1335:1358	the RNA-binding proteome	1335:1358	Further HILIC enrichment on the tryptic-digested RBPs and MS analysis led to the first large-scale identification of O-GlcNAcylation and phosphorylation in the RNA-binding proteome, with 461 O-GlcNAc peptides corresponding to 300 RBPs and 671 phosphopeptides corresponding to 389 RBPs.
33465208	3	66	theme	enrichment	586:595	arg1	strategies					597:606	RBP-targeted enrichment strategies	573:606	RBP-targeted enrichment strategies	573:606	However, due to the extremely low abundance of O-GlcNAcylation and the lack of RBP-targeted enrichment strategies, large-scale simultaneous profiling of O-GlcNAcylation and phosphorylation on RBPs is still a challenging task.
33465208	1	67	theme	important	158:166	arg1	roles					168:172	important roles	158:172	important roles	158:172	RNA-protein interactions play important roles in almost every step of the lifetime of RNAs, such as RNA splicing, transporting, localization, translation and degradation.
33465208	6	68	theme	MS	1237:1238	arg1	analysis					1240:1247	MS analysis	1237:1247	MS analysis	1237:1247	Further HILIC enrichment on the tryptic-digested RBPs and MS analysis led to the first large-scale identification of O-GlcNAcylation and phosphorylation in the RNA-binding proteome, with 461 O-GlcNAc peptides corresponding to 300 RBPs and 671 phosphopeptides corresponding to 389 RBPs.
33465208	6	69	from	analysis	1240:1247	arg1	RBPs					1228:1231	the tryptic-digested RBPs	1207:1231	the tryptic-digested RBPs	1207:1231	Further HILIC enrichment on the tryptic-digested RBPs and MS analysis led to the first large-scale identification of O-GlcNAcylation and phosphorylation in the RNA-binding proteome, with 461 O-GlcNAc peptides corresponding to 300 RBPs and 671 phosphopeptides corresponding to 389 RBPs.
33465208	2	70	theme	proteins	477:484	arg1	activity					429:436	activity	429:436	activity	429:436	Post-translational modifications, such as O-GlcNAcylation and phosphorylation, and their "cross-talk" (OPCT) are essential to the activity and function regulation of RNA-binding proteins (RBPs).
33465208	2	70	theme	proteins	477:484	arg1	function					442:449	function	442:449	function	442:449	Post-translational modifications, such as O-GlcNAcylation and phosphorylation, and their "cross-talk" (OPCT) are essential to the activity and function regulation of RNA-binding proteins (RBPs).
33465208	5	71	theme	ethynyluridine	1013:1026	arg1	labeling					1033:1040	ethynyluridine (EU) labeling	1013:1040	ethynyluridine (EU) labeling	1013:1040	Benefiting from the sequence-independent RNA tagging by ethynyluridine (EU) labeling, 1115 RBPs binding to different types of RNAs were successfully enriched and identified by quantitative mass spectrometry (MS) analysis.
33465208	9	72	theme	roles	1858:1862	arg1	elucidation					1831:1841	further elucidation	1823:1841	further elucidation of the crucial roles of OPCT in the function regulation of RBPs	1823:1905	We expect it will support simultaneous mapping of O-GlcNAcylation and phosphorylation on RBPs and facilitate further elucidation of the crucial roles of OPCT in the function regulation of RBPs.
33465208	5	73	theme	mass	1146:1149	arg1	spectrometry					1151:1162	quantitative mass spectrometry	1133:1162	quantitative mass spectrometry (MS) analysis	1133:1176	Benefiting from the sequence-independent RNA tagging by ethynyluridine (EU) labeling, 1115 RBPs binding to different types of RNAs were successfully enriched and identified by quantitative mass spectrometry (MS) analysis.
33465208	5	73	theme	mass	1146:1149	arg1	MS					1165:1166	MS	1165:1166	MS	1165:1166	Benefiting from the sequence-independent RNA tagging by ethynyluridine (EU) labeling, 1115 RBPs binding to different types of RNAs were successfully enriched and identified by quantitative mass spectrometry (MS) analysis.
33465208	9	74	theme	OPCT	1867:1870	arg1	roles					1858:1862	the crucial roles	1846:1862	the crucial roles of OPCT in the function regulation of RBPs	1846:1905	We expect it will support simultaneous mapping of O-GlcNAcylation and phosphorylation on RBPs and facilitate further elucidation of the crucial roles of OPCT in the function regulation of RBPs.
33465208	4	75	theme	tandem	757:762	arg1	strategy					775:782	a tandem enrichment strategy	755:782	a tandem enrichment strategy combining metabolic labeling-based RNA tagging for selective purification of RBPs and HILIC-based enrichment for simultaneous O-GlcNAcylation and phosphorylation profiling	755:954	In the present study, we developed a tandem enrichment strategy combining metabolic labeling-based RNA tagging for selective purification of RBPs and HILIC-based enrichment for simultaneous O-GlcNAcylation and phosphorylation profiling.
33465208	0	76	theme	new	2:4	arg1	strategy					24:31	A new tandem enrichment strategy	0:31	A new tandem enrichment strategy for the simultaneous profiling of O-GlcNAcylation and phosphorylation in RNA-binding proteome.	0:126	A new tandem enrichment strategy for the simultaneous profiling of O-GlcNAcylation and phosphorylation in RNA-binding proteome.
33465208	1	77	theme	RNA	228:230	arg1	splicing					232:239	RNA splicing	228:239	RNA splicing	228:239	RNA-protein interactions play important roles in almost every step of the lifetime of RNAs, such as RNA splicing, transporting, localization, translation and degradation.
33465208	5	78	theme	sequence-independent	977:996	arg1	tagging					1002:1008	the sequence-independent RNA tagging	973:1008	the sequence-independent RNA tagging by ethynyluridine (EU) labeling	973:1040	Benefiting from the sequence-independent RNA tagging by ethynyluridine (EU) labeling, 1115 RBPs binding to different types of RNAs were successfully enriched and identified by quantitative mass spectrometry (MS) analysis.
33465208	9	79	from	elucidation	1831:1841	arg1	regulation					1888:1897	the function regulation	1875:1897	the function regulation of RBPs	1875:1905	We expect it will support simultaneous mapping of O-GlcNAcylation and phosphorylation on RBPs and facilitate further elucidation of the crucial roles of OPCT in the function regulation of RBPs.
33465208	4	80	theme	present	727:733	arg1	study					735:739	the present study	723:739	the present study	723:739	In the present study, we developed a tandem enrichment strategy combining metabolic labeling-based RNA tagging for selective purification of RBPs and HILIC-based enrichment for simultaneous O-GlcNAcylation and phosphorylation profiling.
33465208	0	81	theme	enrichment	13:22	arg1	strategy					24:31	A new tandem enrichment strategy	0:31	A new tandem enrichment strategy for the simultaneous profiling of O-GlcNAcylation and phosphorylation in RNA-binding proteome.	0:126	A new tandem enrichment strategy for the simultaneous profiling of O-GlcNAcylation and phosphorylation in RNA-binding proteome.
33465208	8	82	theme	compatibility	1609:1621	arg1	advantage					1591:1599	the advantage	1587:1599	the advantage of high compatibility with MS	1587:1629	This strategy has the advantage of high compatibility with MS and provides peptide-level evidence for the identification of O-GlcNAcylated RBPs.
33465208	9	83	theme	RBPs	1902:1905	arg1	regulation					1888:1897	the function regulation	1875:1897	the function regulation of RBPs	1875:1905	We expect it will support simultaneous mapping of O-GlcNAcylation and phosphorylation on RBPs and facilitate further elucidation of the crucial roles of OPCT in the function regulation of RBPs.
33465208	3	84	theme	simultaneous	621:632	arg1	profiling					634:642	large-scale simultaneous profiling	609:642	large-scale simultaneous profiling of O-GlcNAcylation and phosphorylation on RBPs	609:689	However, due to the extremely low abundance of O-GlcNAcylation and the lack of RBP-targeted enrichment strategies, large-scale simultaneous profiling of O-GlcNAcylation and phosphorylation on RBPs is still a challenging task.
33465208	3	84	theme	simultaneous	621:632	arg1	task					714:717	still a challenging task	694:717	still a challenging task	694:717	However, due to the extremely low abundance of O-GlcNAcylation and the lack of RBP-targeted enrichment strategies, large-scale simultaneous profiling of O-GlcNAcylation and phosphorylation on RBPs is still a challenging task.
33465208	4	85	theme	RNA	819:821	arg1	tagging					823:829	metabolic labeling-based RNA tagging	794:829	metabolic labeling-based RNA tagging for selective purification of RBPs and HILIC-based enrichment for simultaneous O-GlcNAcylation and phosphorylation profiling	794:954	In the present study, we developed a tandem enrichment strategy combining metabolic labeling-based RNA tagging for selective purification of RBPs and HILIC-based enrichment for simultaneous O-GlcNAcylation and phosphorylation profiling.
33465208	0	86	theme	simultaneous	41:52	arg1	profiling					54:62	the simultaneous profiling	37:62	the simultaneous profiling of O-GlcNAcylation and phosphorylation in RNA-binding proteome	37:125	A new tandem enrichment strategy for the simultaneous profiling of O-GlcNAcylation and phosphorylation in RNA-binding proteome.
33465208	9	87	from	roles	1858:1862	arg1	regulation					1888:1897	the function regulation	1875:1897	the function regulation of RBPs	1875:1905	We expect it will support simultaneous mapping of O-GlcNAcylation and phosphorylation on RBPs and facilitate further elucidation of the crucial roles of OPCT in the function regulation of RBPs.
33465208	5	88	theme	different	1064:1072	arg1	types					1074:1078	different types	1064:1078	different types of RNAs	1064:1086	Benefiting from the sequence-independent RNA tagging by ethynyluridine (EU) labeling, 1115 RBPs binding to different types of RNAs were successfully enriched and identified by quantitative mass spectrometry (MS) analysis.
33465208	7	89	theme	metabolism	1548:1557	arg1	pathways					1559:1566	multiple metabolism pathways	1539:1566	multiple metabolism pathways	1539:1566	Interestingly, ∼25% RBPs modified by two PTMs were found to be related to multiple metabolism pathways.
33465208	5	90	theme	1115	1043:1046	arg1	RBPs					1048:1051	1115 RBPs	1043:1051	1115 RBPs binding to different types of RNAs	1043:1086	Benefiting from the sequence-independent RNA tagging by ethynyluridine (EU) labeling, 1115 RBPs binding to different types of RNAs were successfully enriched and identified by quantitative mass spectrometry (MS) analysis.
33465208	4	91	theme	metabolic	794:802	arg1	tagging					823:829	metabolic labeling-based RNA tagging	794:829	metabolic labeling-based RNA tagging for selective purification of RBPs and HILIC-based enrichment for simultaneous O-GlcNAcylation and phosphorylation profiling	794:954	In the present study, we developed a tandem enrichment strategy combining metabolic labeling-based RNA tagging for selective purification of RBPs and HILIC-based enrichment for simultaneous O-GlcNAcylation and phosphorylation profiling.
30987996	5	0	theme	DR5-neutralizing	860:875	arg1	antibody					877:884	a DR5-neutralizing antibody	858:884	a DR5-neutralizing antibody	858:884	Using O-GlcNAc transferase knockdown cells, DR4-preferred versus DR5-preferred cancer cells, and a DR5-neutralizing antibody, we evaluated the essential role of DR4-specific O-GlcNAc modification in TRAIL cytotoxicity.
30987996	7	1	theme	cell	1174:1177	arg1	lines					1179:1183	various cancer cell lines	1159:1183	various cancer cell lines originated from stomach, colon, lung, and glioblastoma	1159:1238	Apart from genetic changes in DR4-Ser424, we further classified various cancer cell lines originated from stomach, colon, lung, and glioblastoma according to their sensitivity to and receptor preference upon TRAIL death signaling and generated TRAIL-tolerant persister-derived DLD-1PER cells.
30987996	1	2	theme	TRAIL	286:290	arg1	therapy					292:298	TRAIL therapy	286:298	TRAIL therapy	286:298	TNF-related apoptosis-inducing ligand (TRAIL) resistance, including nongenetically acquired tolerance in cancer persister cells, is a major obstacle to translating TRAIL therapy into patients with cancer.
30987996	12	3	theme	receptors	2124:2132	arg1	one					2097:2099	one	2097:2099	one	2097:2099	SIGNIFICANCE: This study reports that a novel posttranslational modification by O-GlcNAcylation of one of the two human TRAIL receptors with a death domain, TRAIL-R1 (DR4), plays a crucial role in enabling both apoptotic and necroptotic cell death induction by TRAIL.
30987996	12	3	theme	receptors	2124:2132	arg1	receptors					2124:2132	the two human TRAIL receptors	2104:2132	the two human TRAIL receptors with a death domain	2104:2152	SIGNIFICANCE: This study reports that a novel posttranslational modification by O-GlcNAcylation of one of the two human TRAIL receptors with a death domain, TRAIL-R1 (DR4), plays a crucial role in enabling both apoptotic and necroptotic cell death induction by TRAIL.
30987996	12	3	theme	receptors	2124:2132	arg1	TRAIL-R1					2155:2162	TRAIL-R1	2155:2162	TRAIL-R1 (DR4)	2155:2168	SIGNIFICANCE: This study reports that a novel posttranslational modification by O-GlcNAcylation of one of the two human TRAIL receptors with a death domain, TRAIL-R1 (DR4), plays a crucial role in enabling both apoptotic and necroptotic cell death induction by TRAIL.
30987996	7	4	link	persister-derived	1354:1370	arg1	cells					1381:1385	generated TRAIL-tolerant persister-derived DLD-1PER cells	1329:1385	generated TRAIL-tolerant persister-derived DLD-1PER cells	1329:1385	Apart from genetic changes in DR4-Ser424, we further classified various cancer cell lines originated from stomach, colon, lung, and glioblastoma according to their sensitivity to and receptor preference upon TRAIL death signaling and generated TRAIL-tolerant persister-derived DLD-1PER cells.
30987996	7	5	from	changes	1114:1120	arg1	DR4-Ser424					1125:1134	DR4-Ser424	1125:1134	DR4-Ser424	1125:1134	Apart from genetic changes in DR4-Ser424, we further classified various cancer cell lines originated from stomach, colon, lung, and glioblastoma according to their sensitivity to and receptor preference upon TRAIL death signaling and generated TRAIL-tolerant persister-derived DLD-1PER cells.
30987996	7	6	theme	various	1159:1165	arg1	lines					1179:1183	various cancer cell lines	1159:1183	various cancer cell lines originated from stomach, colon, lung, and glioblastoma	1159:1238	Apart from genetic changes in DR4-Ser424, we further classified various cancer cell lines originated from stomach, colon, lung, and glioblastoma according to their sensitivity to and receptor preference upon TRAIL death signaling and generated TRAIL-tolerant persister-derived DLD-1PER cells.
30987996	1	7	theme	ligand	153:158	arg1	obstacle					262:269	a major obstacle	254:269	a major obstacle to translating TRAIL therapy into patients with cancer	254:324	TNF-related apoptosis-inducing ligand (TRAIL) resistance, including nongenetically acquired tolerance in cancer persister cells, is a major obstacle to translating TRAIL therapy into patients with cancer.
30987996	1	7	theme	ligand	153:158	arg1	resistance					168:177	TNF-related apoptosis-inducing ligand (TRAIL) resistance	122:177	TNF-related apoptosis-inducing ligand (TRAIL) resistance	122:177	TNF-related apoptosis-inducing ligand (TRAIL) resistance, including nongenetically acquired tolerance in cancer persister cells, is a major obstacle to translating TRAIL therapy into patients with cancer.
30987996	4	8	theme	Genome	687:692	arg1	Atlas					694:698	The Cancer Genome Atlas	676:698	The Cancer Genome Atlas	676:698	We found that DR4-Ser424 mutations, identified from our cell-based functional screen using a cancer patient-derived cDNA expression library and from The Cancer Genome Atlas, caused TRAIL resistance in various human cancer cell lines.
30987996	12	9	theme	death	2240:2244	arg1	induction					2246:2254	both apoptotic and necroptotic cell death induction	2204:2254	both apoptotic and necroptotic cell death induction by TRAIL	2204:2263	SIGNIFICANCE: This study reports that a novel posttranslational modification by O-GlcNAcylation of one of the two human TRAIL receptors with a death domain, TRAIL-R1 (DR4), plays a crucial role in enabling both apoptotic and necroptotic cell death induction by TRAIL.
30987996	1	10	theme	cancer	227:232	arg1	cells					244:248	cancer persister cells	227:248	cancer persister cells	227:248	TNF-related apoptosis-inducing ligand (TRAIL) resistance, including nongenetically acquired tolerance in cancer persister cells, is a major obstacle to translating TRAIL therapy into patients with cancer.
30987996	12	11	theme	human	2112:2116	arg1	receptors					2124:2132	the two human TRAIL receptors	2104:2132	the two human TRAIL receptors with a death domain	2104:2152	SIGNIFICANCE: This study reports that a novel posttranslational modification by O-GlcNAcylation of one of the two human TRAIL receptors with a death domain, TRAIL-R1 (DR4), plays a crucial role in enabling both apoptotic and necroptotic cell death induction by TRAIL.
30987996	12	11	theme	human	2112:2116	arg1	TRAIL-R1					2155:2162	TRAIL-R1	2155:2162	TRAIL-R1 (DR4)	2155:2168	SIGNIFICANCE: This study reports that a novel posttranslational modification by O-GlcNAcylation of one of the two human TRAIL receptors with a death domain, TRAIL-R1 (DR4), plays a crucial role in enabling both apoptotic and necroptotic cell death induction by TRAIL.
30987996	12	12	theme	apoptotic	2209:2217	arg1	induction					2246:2254	both apoptotic and necroptotic cell death induction	2204:2254	both apoptotic and necroptotic cell death induction by TRAIL	2204:2263	SIGNIFICANCE: This study reports that a novel posttranslational modification by O-GlcNAcylation of one of the two human TRAIL receptors with a death domain, TRAIL-R1 (DR4), plays a crucial role in enabling both apoptotic and necroptotic cell death induction by TRAIL.
30987996	11	13	theme	TRAIL	1944:1948	arg1	therapy					1950:1956	TRAIL therapy	1944:1956	TRAIL therapy	1944:1956	Our findings demonstrate that DR4 O-GlcNAcylation is crucial for TRAIL death signaling, providing new opportunities for TRAIL therapy overcoming TRAIL resistance in cancers.
30987996	7	14	theme	genetic	1106:1112	arg1	changes					1114:1120	genetic changes	1106:1120	genetic changes in DR4-Ser424	1106:1134	Apart from genetic changes in DR4-Ser424, we further classified various cancer cell lines originated from stomach, colon, lung, and glioblastoma according to their sensitivity to and receptor preference upon TRAIL death signaling and generated TRAIL-tolerant persister-derived DLD-1PER cells.
30987996	9	15	theme	promoting	1532:1540	arg1	O-GlcNAcylation					1546:1560	promoting DR4 O-GlcNAcylation	1532:1560	promoting DR4 O-GlcNAcylation intentionally using 2-deoxy-d-glucose or a high concentration of glucose	1532:1633	Interestingly, promoting DR4 O-GlcNAcylation intentionally using 2-deoxy-d-glucose or a high concentration of glucose sensitized those resistant cancer cells to TRAIL.
30987996	12	16	theme	one	2097:2099	arg1	modification					2062:2073	a novel posttranslational modification	2036:2073	a novel posttranslational modification by O-GlcNAcylation of one of the two human TRAIL receptors with a death domain, TRAIL-R1 (DR4),	2036:2169	SIGNIFICANCE: This study reports that a novel posttranslational modification by O-GlcNAcylation of one of the two human TRAIL receptors with a death domain, TRAIL-R1 (DR4), plays a crucial role in enabling both apoptotic and necroptotic cell death induction by TRAIL.
30987996	8	17	theme	DLD-1PER	1501:1508	arg1	cells					1510:1514	DLD-1PER cells	1501:1514	DLD-1PER cells	1501:1514	Among these, we discovered that DR4 was not modified by O-GlcNAc in most of the TRAIL-resistant cancer cells and DLD-1PER cells.
30987996	4	18	theme	human	736:740	arg1	lines					754:758	various human cancer cell lines	728:758	various human cancer cell lines	728:758	We found that DR4-Ser424 mutations, identified from our cell-based functional screen using a cancer patient-derived cDNA expression library and from The Cancer Genome Atlas, caused TRAIL resistance in various human cancer cell lines.
30987996	10	19	theme	O-GlcNAcylation-defective	1689:1713	arg1	DR4					1715:1717	The O-GlcNAcylation-defective DR4	1685:1717	The O-GlcNAcylation-defective DR4	1685:1717	The O-GlcNAcylation-defective DR4 failed to form DISC/necrosome and could not translocate to aggregated platforms for receptor clustering.
30987996	5	20	theme	TRAIL	960:964	arg1	cytotoxicity					966:977	TRAIL cytotoxicity	960:977	TRAIL cytotoxicity	960:977	Using O-GlcNAc transferase knockdown cells, DR4-preferred versus DR5-preferred cancer cells, and a DR5-neutralizing antibody, we evaluated the essential role of DR4-specific O-GlcNAc modification in TRAIL cytotoxicity.
30987996	4	21	theme	cell	749:752	arg1	lines					754:758	various human cancer cell lines	728:758	various human cancer cell lines	728:758	We found that DR4-Ser424 mutations, identified from our cell-based functional screen using a cancer patient-derived cDNA expression library and from The Cancer Genome Atlas, caused TRAIL resistance in various human cancer cell lines.
30987996	9	22	theme	cancer	1662:1667	arg1	cells					1669:1673	those resistant cancer cells	1646:1673	those resistant cancer cells	1646:1673	Interestingly, promoting DR4 O-GlcNAcylation intentionally using 2-deoxy-d-glucose or a high concentration of glucose sensitized those resistant cancer cells to TRAIL.
30987996	12	23	with	receptors	2124:2132	arg1	domain					2147:2152	a death domain	2139:2152	a death domain	2139:2152	SIGNIFICANCE: This study reports that a novel posttranslational modification by O-GlcNAcylation of one of the two human TRAIL receptors with a death domain, TRAIL-R1 (DR4), plays a crucial role in enabling both apoptotic and necroptotic cell death induction by TRAIL.
30987996	4	24	theme	TRAIL	708:712	arg1	resistance					714:723	TRAIL resistance	708:723	TRAIL resistance in various human cancer cell lines	708:758	We found that DR4-Ser424 mutations, identified from our cell-based functional screen using a cancer patient-derived cDNA expression library and from The Cancer Genome Atlas, caused TRAIL resistance in various human cancer cell lines.
30987996	5	25	theme	knockdown	788:796	arg1	cells					798:802	O-GlcNAc transferase knockdown cells	767:802	O-GlcNAc transferase knockdown cells	767:802	Using O-GlcNAc transferase knockdown cells, DR4-preferred versus DR5-preferred cancer cells, and a DR5-neutralizing antibody, we evaluated the essential role of DR4-specific O-GlcNAc modification in TRAIL cytotoxicity.
30987996	5	26	theme	DR4-specific	922:933	arg1	modification					944:955	DR4-specific O-GlcNAc modification	922:955	DR4-specific O-GlcNAc modification	922:955	Using O-GlcNAc transferase knockdown cells, DR4-preferred versus DR5-preferred cancer cells, and a DR5-neutralizing antibody, we evaluated the essential role of DR4-specific O-GlcNAc modification in TRAIL cytotoxicity.
30987996	11	27	theme	TRAIL	1889:1893	arg1	signaling					1901:1909	TRAIL death signaling	1889:1909	TRAIL death signaling	1889:1909	Our findings demonstrate that DR4 O-GlcNAcylation is crucial for TRAIL death signaling, providing new opportunities for TRAIL therapy overcoming TRAIL resistance in cancers.
30987996	0	28	theme	Cells	106:110	arg1	Sensitization					36:48	Sensitization	36:48	Sensitization of TRAIL-Tolerant Persisters and TRAIL-Resistant Cancer Cells to Death	36:119	DR4-Ser424 O-GlcNAcylation Promotes Sensitization of TRAIL-Tolerant Persisters and TRAIL-Resistant Cancer Cells to Death.
30987996	5	29	theme	modification	944:955	arg1	role					914:917	the essential role	900:917	the essential role of DR4-specific O-GlcNAc modification in TRAIL cytotoxicity	900:977	Using O-GlcNAc transferase knockdown cells, DR4-preferred versus DR5-preferred cancer cells, and a DR5-neutralizing antibody, we evaluated the essential role of DR4-specific O-GlcNAc modification in TRAIL cytotoxicity.
30987996	6	30	theme	TRAIL	1030:1034	arg1	treatment					1036:1044	TRAIL treatment	1030:1044	TRAIL treatment	1030:1044	In contrast to DR4, DR5 was not O-GlcNAcylated by TRAIL treatment, discriminating DR4 from DR5-mediated signaling.
30987996	12	31	theme	posttranslational	2044:2060	arg1	modification					2062:2073	a novel posttranslational modification	2036:2073	a novel posttranslational modification by O-GlcNAcylation of one of the two human TRAIL receptors with a death domain, TRAIL-R1 (DR4),	2036:2169	SIGNIFICANCE: This study reports that a novel posttranslational modification by O-GlcNAcylation of one of the two human TRAIL receptors with a death domain, TRAIL-R1 (DR4), plays a crucial role in enabling both apoptotic and necroptotic cell death induction by TRAIL.
30987996	12	32	theme	crucial	2179:2185	arg1	role					2187:2190	a crucial role	2177:2190	a crucial role	2177:2190	SIGNIFICANCE: This study reports that a novel posttranslational modification by O-GlcNAcylation of one of the two human TRAIL receptors with a death domain, TRAIL-R1 (DR4), plays a crucial role in enabling both apoptotic and necroptotic cell death induction by TRAIL.
30987996	3	33	theme	death	454:458	arg1	domain					460:465	its death domain	450:465	its death domain	450:465	Here, we show that DR4/TRAIL-R1 is O-GlcNAcylated at Ser424 in its death domain to mediate both apoptosis and necrosis upon TRAIL ligation.
30987996	5	34	theme	O-GlcNAc	767:774	arg1	transferase					776:786	O-GlcNAc transferase	767:786	O-GlcNAc transferase knockdown cells	767:802	Using O-GlcNAc transferase knockdown cells, DR4-preferred versus DR5-preferred cancer cells, and a DR5-neutralizing antibody, we evaluated the essential role of DR4-specific O-GlcNAc modification in TRAIL cytotoxicity.
30987996	0	35	theme	TRAIL-Tolerant	53:66	arg1	Persisters					68:77	TRAIL-Tolerant Persisters	53:77	TRAIL-Tolerant Persisters	53:77	DR4-Ser424 O-GlcNAcylation Promotes Sensitization of TRAIL-Tolerant Persisters and TRAIL-Resistant Cancer Cells to Death.
30987996	0	36	theme	Cancer	99:104	arg1	Cells					106:110	TRAIL-Resistant Cancer Cells	83:110	TRAIL-Resistant Cancer Cells	83:110	DR4-Ser424 O-GlcNAcylation Promotes Sensitization of TRAIL-Tolerant Persisters and TRAIL-Resistant Cancer Cells to Death.
30987996	0	37	theme	DR4-Ser424	0:9	arg1	O-GlcNAcylation					11:25	DR4-Ser424 O-GlcNAcylation	0:25	DR4-Ser424 O-GlcNAcylation	0:25	DR4-Ser424 O-GlcNAcylation Promotes Sensitization of TRAIL-Tolerant Persisters and TRAIL-Resistant Cancer Cells to Death.
30987996	9	38	theme	resistant	1652:1660	arg1	cells					1669:1673	those resistant cancer cells	1646:1673	those resistant cancer cells	1646:1673	Interestingly, promoting DR4 O-GlcNAcylation intentionally using 2-deoxy-d-glucose or a high concentration of glucose sensitized those resistant cancer cells to TRAIL.
30987996	10	39	theme	aggregated	1778:1787	arg1	platforms					1789:1797	aggregated platforms	1778:1797	aggregated platforms for receptor clustering	1778:1821	The O-GlcNAcylation-defective DR4 failed to form DISC/necrosome and could not translocate to aggregated platforms for receptor clustering.
30987996	1	40	theme	apoptosis-inducing	134:151	arg1	TRAIL					161:165	TRAIL	161:165	TRAIL	161:165	TNF-related apoptosis-inducing ligand (TRAIL) resistance, including nongenetically acquired tolerance in cancer persister cells, is a major obstacle to translating TRAIL therapy into patients with cancer.
30987996	1	40	theme	apoptosis-inducing	134:151	arg1	ligand					153:158	TNF-related apoptosis-inducing ligand	122:158	TNF-related apoptosis-inducing ligand (TRAIL) resistance	122:177	TNF-related apoptosis-inducing ligand (TRAIL) resistance, including nongenetically acquired tolerance in cancer persister cells, is a major obstacle to translating TRAIL therapy into patients with cancer.
30987996	7	41	theme	DLD-1PER	1372:1379	arg1	cells					1381:1385	generated TRAIL-tolerant persister-derived DLD-1PER cells	1329:1385	generated TRAIL-tolerant persister-derived DLD-1PER cells	1329:1385	Apart from genetic changes in DR4-Ser424, we further classified various cancer cell lines originated from stomach, colon, lung, and glioblastoma according to their sensitivity to and receptor preference upon TRAIL death signaling and generated TRAIL-tolerant persister-derived DLD-1PER cells.
30987996	12	42	theme	necroptotic	2223:2233	arg1	induction					2246:2254	both apoptotic and necroptotic cell death induction	2204:2254	both apoptotic and necroptotic cell death induction by TRAIL	2204:2263	SIGNIFICANCE: This study reports that a novel posttranslational modification by O-GlcNAcylation of one of the two human TRAIL receptors with a death domain, TRAIL-R1 (DR4), plays a crucial role in enabling both apoptotic and necroptotic cell death induction by TRAIL.
30987996	4	43	link	patient-derived	627:641	arg1	library					659:665	a cancer patient-derived cDNA expression library	618:665	a cancer patient-derived cDNA expression library	618:665	We found that DR4-Ser424 mutations, identified from our cell-based functional screen using a cancer patient-derived cDNA expression library and from The Cancer Genome Atlas, caused TRAIL resistance in various human cancer cell lines.
30987996	7	44	theme	TRAIL-tolerant	1339:1352	arg1	cells					1381:1385	generated TRAIL-tolerant persister-derived DLD-1PER cells	1329:1385	generated TRAIL-tolerant persister-derived DLD-1PER cells	1329:1385	Apart from genetic changes in DR4-Ser424, we further classified various cancer cell lines originated from stomach, colon, lung, and glioblastoma according to their sensitivity to and receptor preference upon TRAIL death signaling and generated TRAIL-tolerant persister-derived DLD-1PER cells.
30987996	6	45	from	contrast	983:990	arg1	O-GlcNAcylated					1012:1025	O-GlcNAcylated	1012:1025	O-GlcNAcylated	1012:1025	In contrast to DR4, DR5 was not O-GlcNAcylated by TRAIL treatment, discriminating DR4 from DR5-mediated signaling.
30987996	0	46	theme	TRAIL-Resistant	83:97	arg1	Cells					106:110	TRAIL-Resistant Cancer Cells	83:110	TRAIL-Resistant Cancer Cells	83:110	DR4-Ser424 O-GlcNAcylation Promotes Sensitization of TRAIL-Tolerant Persisters and TRAIL-Resistant Cancer Cells to Death.
30987996	5	47	theme	cancer	840:845	arg1	cells					847:851	DR4-preferred versus DR5-preferred cancer cells	805:851	DR4-preferred versus DR5-preferred cancer cells	805:851	Using O-GlcNAc transferase knockdown cells, DR4-preferred versus DR5-preferred cancer cells, and a DR5-neutralizing antibody, we evaluated the essential role of DR4-specific O-GlcNAc modification in TRAIL cytotoxicity.
30987996	7	48	theme	death	1309:1313	arg1	signaling					1315:1323	TRAIL death signaling	1303:1323	TRAIL death signaling	1303:1323	Apart from genetic changes in DR4-Ser424, we further classified various cancer cell lines originated from stomach, colon, lung, and glioblastoma according to their sensitivity to and receptor preference upon TRAIL death signaling and generated TRAIL-tolerant persister-derived DLD-1PER cells.
30987996	4	49	theme	cancer	620:625	arg1	library					659:665	a cancer patient-derived cDNA expression library	618:665	a cancer patient-derived cDNA expression library	618:665	We found that DR4-Ser424 mutations, identified from our cell-based functional screen using a cancer patient-derived cDNA expression library and from The Cancer Genome Atlas, caused TRAIL resistance in various human cancer cell lines.
30987996	6	50	theme	DR5-mediated	1071:1082	arg1	signaling					1084:1092	DR5-mediated signaling	1071:1092	DR5-mediated signaling	1071:1092	In contrast to DR4, DR5 was not O-GlcNAcylated by TRAIL treatment, discriminating DR4 from DR5-mediated signaling.
30987996	8	51	theme	cancer	1484:1489	arg1	cells					1491:1495	the TRAIL-resistant cancer cells	1464:1495	the TRAIL-resistant cancer cells	1464:1495	Among these, we discovered that DR4 was not modified by O-GlcNAc in most of the TRAIL-resistant cancer cells and DLD-1PER cells.
30987996	12	52	theme	death	2141:2145	arg1	domain					2147:2152	a death domain	2139:2152	a death domain	2139:2152	SIGNIFICANCE: This study reports that a novel posttranslational modification by O-GlcNAcylation of one of the two human TRAIL receptors with a death domain, TRAIL-R1 (DR4), plays a crucial role in enabling both apoptotic and necroptotic cell death induction by TRAIL.
30987996	4	53	theme	cDNA	643:646	arg1	library					659:665	a cancer patient-derived cDNA expression library	618:665	a cancer patient-derived cDNA expression library	618:665	We found that DR4-Ser424 mutations, identified from our cell-based functional screen using a cancer patient-derived cDNA expression library and from The Cancer Genome Atlas, caused TRAIL resistance in various human cancer cell lines.
30987996	7	54	theme	cancer	1167:1172	arg1	lines					1179:1183	various cancer cell lines	1159:1183	various cancer cell lines originated from stomach, colon, lung, and glioblastoma	1159:1238	Apart from genetic changes in DR4-Ser424, we further classified various cancer cell lines originated from stomach, colon, lung, and glioblastoma according to their sensitivity to and receptor preference upon TRAIL death signaling and generated TRAIL-tolerant persister-derived DLD-1PER cells.
30987996	4	55	from	resistance	714:723	arg1	lines					754:758	various human cancer cell lines	728:758	various human cancer cell lines	728:758	We found that DR4-Ser424 mutations, identified from our cell-based functional screen using a cancer patient-derived cDNA expression library and from The Cancer Genome Atlas, caused TRAIL resistance in various human cancer cell lines.
30987996	7	56	theme	receptor	1278:1285	arg1	preference					1287:1296	receptor preference	1278:1296	receptor preference upon TRAIL death signaling	1278:1323	Apart from genetic changes in DR4-Ser424, we further classified various cancer cell lines originated from stomach, colon, lung, and glioblastoma according to their sensitivity to and receptor preference upon TRAIL death signaling and generated TRAIL-tolerant persister-derived DLD-1PER cells.
30987996	4	57	theme	functional	594:603	arg1	screen					605:610	our cell-based functional screen	579:610	our cell-based functional screen using a cancer patient-derived cDNA expression library	579:665	We found that DR4-Ser424 mutations, identified from our cell-based functional screen using a cancer patient-derived cDNA expression library and from The Cancer Genome Atlas, caused TRAIL resistance in various human cancer cell lines.
30987996	12	58	theme	TRAIL	2118:2122	arg1	receptors					2124:2132	the two human TRAIL receptors	2104:2132	the two human TRAIL receptors with a death domain	2104:2152	SIGNIFICANCE: This study reports that a novel posttranslational modification by O-GlcNAcylation of one of the two human TRAIL receptors with a death domain, TRAIL-R1 (DR4), plays a crucial role in enabling both apoptotic and necroptotic cell death induction by TRAIL.
30987996	12	58	theme	TRAIL	2118:2122	arg1	TRAIL-R1					2155:2162	TRAIL-R1	2155:2162	TRAIL-R1 (DR4)	2155:2168	SIGNIFICANCE: This study reports that a novel posttranslational modification by O-GlcNAcylation of one of the two human TRAIL receptors with a death domain, TRAIL-R1 (DR4), plays a crucial role in enabling both apoptotic and necroptotic cell death induction by TRAIL.
30987996	1	59	theme	acquired	205:212	arg1	tolerance					214:222	nongenetically acquired tolerance	190:222	nongenetically acquired tolerance in cancer persister cells	190:248	TNF-related apoptosis-inducing ligand (TRAIL) resistance, including nongenetically acquired tolerance in cancer persister cells, is a major obstacle to translating TRAIL therapy into patients with cancer.
30987996	0	60	theme	Persisters	68:77	arg1	Sensitization					36:48	Sensitization	36:48	Sensitization of TRAIL-Tolerant Persisters and TRAIL-Resistant Cancer Cells to Death	36:119	DR4-Ser424 O-GlcNAcylation Promotes Sensitization of TRAIL-Tolerant Persisters and TRAIL-Resistant Cancer Cells to Death.
30987996	4	61	theme	Cancer	680:685	arg1	Atlas					694:698	The Cancer Genome Atlas	676:698	The Cancer Genome Atlas	676:698	We found that DR4-Ser424 mutations, identified from our cell-based functional screen using a cancer patient-derived cDNA expression library and from The Cancer Genome Atlas, caused TRAIL resistance in various human cancer cell lines.
30987996	2	62	theme	underlying	340:349	arg1	mechanisms					351:360	the underlying mechanisms	336:360	the underlying mechanisms	336:360	However, the underlying mechanisms remain to be elucidated.
30987996	5	63	theme	essential	904:912	arg1	role					914:917	the essential role	900:917	the essential role of DR4-specific O-GlcNAc modification in TRAIL cytotoxicity	900:977	Using O-GlcNAc transferase knockdown cells, DR4-preferred versus DR5-preferred cancer cells, and a DR5-neutralizing antibody, we evaluated the essential role of DR4-specific O-GlcNAc modification in TRAIL cytotoxicity.
30987996	1	64	with	patients	305:312	arg1	cancer					319:324	cancer	319:324	cancer	319:324	TNF-related apoptosis-inducing ligand (TRAIL) resistance, including nongenetically acquired tolerance in cancer persister cells, is a major obstacle to translating TRAIL therapy into patients with cancer.
30987996	12	65	theme	cell	2235:2238	arg1	induction					2246:2254	both apoptotic and necroptotic cell death induction	2204:2254	both apoptotic and necroptotic cell death induction by TRAIL	2204:2263	SIGNIFICANCE: This study reports that a novel posttranslational modification by O-GlcNAcylation of one of the two human TRAIL receptors with a death domain, TRAIL-R1 (DR4), plays a crucial role in enabling both apoptotic and necroptotic cell death induction by TRAIL.
30987996	11	66	theme	new	1922:1924	arg1	opportunities					1926:1938	new opportunities	1922:1938	new opportunities for TRAIL therapy	1922:1956	Our findings demonstrate that DR4 O-GlcNAcylation is crucial for TRAIL death signaling, providing new opportunities for TRAIL therapy overcoming TRAIL resistance in cancers.
30987996	1	67	theme	persister	234:242	arg1	cells					244:248	cancer persister cells	227:248	cancer persister cells	227:248	TNF-related apoptosis-inducing ligand (TRAIL) resistance, including nongenetically acquired tolerance in cancer persister cells, is a major obstacle to translating TRAIL therapy into patients with cancer.
30987996	9	68	theme	high	1605:1608	arg1	concentration					1610:1622	a high concentration	1603:1622	a high concentration of glucose	1603:1633	Interestingly, promoting DR4 O-GlcNAcylation intentionally using 2-deoxy-d-glucose or a high concentration of glucose sensitized those resistant cancer cells to TRAIL.
30987996	3	69	theme	TRAIL	511:515	arg1	ligation					517:524	TRAIL ligation	511:524	TRAIL ligation	511:524	Here, we show that DR4/TRAIL-R1 is O-GlcNAcylated at Ser424 in its death domain to mediate both apoptosis and necrosis upon TRAIL ligation.
30987996	8	70	mod	modified	1432:1439	arg3	O-GlcNAc					1444:1451	O-GlcNAc	1444:1451	O-GlcNAc	1444:1451	Among these, we discovered that DR4 was not modified by O-GlcNAc in most of the TRAIL-resistant cancer cells and DLD-1PER cells.
30987996	8	70	mod	modified	1432:1439	arg1	DR4					1420:1422	DR4	1420:1422	DR4	1420:1422	Among these, we discovered that DR4 was not modified by O-GlcNAc in most of the TRAIL-resistant cancer cells and DLD-1PER cells.
30987996	9	71	theme	DR4	1542:1544	arg1	O-GlcNAcylation					1546:1560	promoting DR4 O-GlcNAcylation	1532:1560	promoting DR4 O-GlcNAcylation intentionally using 2-deoxy-d-glucose or a high concentration of glucose	1532:1633	Interestingly, promoting DR4 O-GlcNAcylation intentionally using 2-deoxy-d-glucose or a high concentration of glucose sensitized those resistant cancer cells to TRAIL.
30987996	4	72	theme	various	728:734	arg1	lines					754:758	various human cancer cell lines	728:758	various human cancer cell lines	728:758	We found that DR4-Ser424 mutations, identified from our cell-based functional screen using a cancer patient-derived cDNA expression library and from The Cancer Genome Atlas, caused TRAIL resistance in various human cancer cell lines.
30987996	4	73	theme	cancer	742:747	arg1	lines					754:758	various human cancer cell lines	728:758	various human cancer cell lines	728:758	We found that DR4-Ser424 mutations, identified from our cell-based functional screen using a cancer patient-derived cDNA expression library and from The Cancer Genome Atlas, caused TRAIL resistance in various human cancer cell lines.
30987996	5	74	theme	transferase	776:786	arg1	cells					798:802	O-GlcNAc transferase knockdown cells	767:802	O-GlcNAc transferase knockdown cells	767:802	Using O-GlcNAc transferase knockdown cells, DR4-preferred versus DR5-preferred cancer cells, and a DR5-neutralizing antibody, we evaluated the essential role of DR4-specific O-GlcNAc modification in TRAIL cytotoxicity.
30987996	5	75	from	role	914:917	arg1	cytotoxicity					966:977	TRAIL cytotoxicity	960:977	TRAIL cytotoxicity	960:977	Using O-GlcNAc transferase knockdown cells, DR4-preferred versus DR5-preferred cancer cells, and a DR5-neutralizing antibody, we evaluated the essential role of DR4-specific O-GlcNAc modification in TRAIL cytotoxicity.
30987996	11	76	theme	DR4	1854:1856	arg1	O-GlcNAcylation					1858:1872	DR4 O-GlcNAcylation	1854:1872	DR4 O-GlcNAcylation	1854:1872	Our findings demonstrate that DR4 O-GlcNAcylation is crucial for TRAIL death signaling, providing new opportunities for TRAIL therapy overcoming TRAIL resistance in cancers.
30987996	12	77	theme	novel	2038:2042	arg1	modification					2062:2073	a novel posttranslational modification	2036:2073	a novel posttranslational modification by O-GlcNAcylation of one of the two human TRAIL receptors with a death domain, TRAIL-R1 (DR4),	2036:2169	SIGNIFICANCE: This study reports that a novel posttranslational modification by O-GlcNAcylation of one of the two human TRAIL receptors with a death domain, TRAIL-R1 (DR4), plays a crucial role in enabling both apoptotic and necroptotic cell death induction by TRAIL.
30987996	1	78	from	tolerance	214:222	arg1	cells					244:248	cancer persister cells	227:248	cancer persister cells	227:248	TNF-related apoptosis-inducing ligand (TRAIL) resistance, including nongenetically acquired tolerance in cancer persister cells, is a major obstacle to translating TRAIL therapy into patients with cancer.
30987996	5	79	theme	O-GlcNAc	935:942	arg1	modification					944:955	DR4-specific O-GlcNAc modification	922:955	DR4-specific O-GlcNAc modification	922:955	Using O-GlcNAc transferase knockdown cells, DR4-preferred versus DR5-preferred cancer cells, and a DR5-neutralizing antibody, we evaluated the essential role of DR4-specific O-GlcNAc modification in TRAIL cytotoxicity.
30987996	11	80	theme	death	1895:1899	arg1	signaling					1901:1909	TRAIL death signaling	1889:1909	TRAIL death signaling	1889:1909	Our findings demonstrate that DR4 O-GlcNAcylation is crucial for TRAIL death signaling, providing new opportunities for TRAIL therapy overcoming TRAIL resistance in cancers.
30987996	3	81	from	Ser424	440:445	arg1	O-GlcNAcylated					422:435	O-GlcNAcylated	422:435	O-GlcNAcylated	422:435	Here, we show that DR4/TRAIL-R1 is O-GlcNAcylated at Ser424 in its death domain to mediate both apoptosis and necrosis upon TRAIL ligation.
30987996	9	82	theme	glucose	1627:1633	arg1	concentration					1610:1622	a high concentration	1603:1622	a high concentration of glucose	1603:1633	Interestingly, promoting DR4 O-GlcNAcylation intentionally using 2-deoxy-d-glucose or a high concentration of glucose sensitized those resistant cancer cells to TRAIL.
30987996	9	82	theme	glucose	1627:1633	arg1	2-deoxy-d-glucose					1582:1598	2-deoxy-d-glucose	1582:1598	2-deoxy-d-glucose	1582:1598	Interestingly, promoting DR4 O-GlcNAcylation intentionally using 2-deoxy-d-glucose or a high concentration of glucose sensitized those resistant cancer cells to TRAIL.
30987996	6	83	from	O-GlcNAcylated	1012:1025	arg1	contrast					983:990	contrast	983:990	contrast to DR4	983:997	In contrast to DR4, DR5 was not O-GlcNAcylated by TRAIL treatment, discriminating DR4 from DR5-mediated signaling.
30987996	11	84	from	resistance	1975:1984	arg1	cancers					1989:1995	cancers	1989:1995	cancers	1989:1995	Our findings demonstrate that DR4 O-GlcNAcylation is crucial for TRAIL death signaling, providing new opportunities for TRAIL therapy overcoming TRAIL resistance in cancers.
30987996	1	85	theme	TNF-related	122:132	arg1	TRAIL					161:165	TRAIL	161:165	TRAIL	161:165	TNF-related apoptosis-inducing ligand (TRAIL) resistance, including nongenetically acquired tolerance in cancer persister cells, is a major obstacle to translating TRAIL therapy into patients with cancer.
30987996	1	85	theme	TNF-related	122:132	arg1	ligand					153:158	TNF-related apoptosis-inducing ligand	122:158	TNF-related apoptosis-inducing ligand (TRAIL) resistance	122:177	TNF-related apoptosis-inducing ligand (TRAIL) resistance, including nongenetically acquired tolerance in cancer persister cells, is a major obstacle to translating TRAIL therapy into patients with cancer.
30987996	7	86	theme	persister-derived	1354:1370	arg1	cells					1381:1385	generated TRAIL-tolerant persister-derived DLD-1PER cells	1329:1385	generated TRAIL-tolerant persister-derived DLD-1PER cells	1329:1385	Apart from genetic changes in DR4-Ser424, we further classified various cancer cell lines originated from stomach, colon, lung, and glioblastoma according to their sensitivity to and receptor preference upon TRAIL death signaling and generated TRAIL-tolerant persister-derived DLD-1PER cells.
30987996	4	87	theme	cell-based	583:592	arg1	screen					605:610	our cell-based functional screen	579:610	our cell-based functional screen using a cancer patient-derived cDNA expression library	579:665	We found that DR4-Ser424 mutations, identified from our cell-based functional screen using a cancer patient-derived cDNA expression library and from The Cancer Genome Atlas, caused TRAIL resistance in various human cancer cell lines.
30987996	5	88	theme	DR4-preferred	805:817	arg1	cells					847:851	DR4-preferred versus DR5-preferred cancer cells	805:851	DR4-preferred versus DR5-preferred cancer cells	805:851	Using O-GlcNAc transferase knockdown cells, DR4-preferred versus DR5-preferred cancer cells, and a DR5-neutralizing antibody, we evaluated the essential role of DR4-specific O-GlcNAc modification in TRAIL cytotoxicity.
30987996	7	89	theme	generated	1329:1337	arg1	cells					1381:1385	generated TRAIL-tolerant persister-derived DLD-1PER cells	1329:1385	generated TRAIL-tolerant persister-derived DLD-1PER cells	1329:1385	Apart from genetic changes in DR4-Ser424, we further classified various cancer cell lines originated from stomach, colon, lung, and glioblastoma according to their sensitivity to and receptor preference upon TRAIL death signaling and generated TRAIL-tolerant persister-derived DLD-1PER cells.
30987996	4	90	theme	DR4-Ser424	541:550	arg1	mutations					552:560	DR4-Ser424 mutations	541:560	DR4-Ser424 mutations	541:560	We found that DR4-Ser424 mutations, identified from our cell-based functional screen using a cancer patient-derived cDNA expression library and from The Cancer Genome Atlas, caused TRAIL resistance in various human cancer cell lines.
30987996	5	91	theme	DR5-preferred	826:838	arg1	cells					847:851	DR4-preferred versus DR5-preferred cancer cells	805:851	DR4-preferred versus DR5-preferred cancer cells	805:851	Using O-GlcNAc transferase knockdown cells, DR4-preferred versus DR5-preferred cancer cells, and a DR5-neutralizing antibody, we evaluated the essential role of DR4-specific O-GlcNAc modification in TRAIL cytotoxicity.
30987996	10	92	theme	receptor	1803:1810	arg1	clustering					1812:1821	receptor clustering	1803:1821	receptor clustering	1803:1821	The O-GlcNAcylation-defective DR4 failed to form DISC/necrosome and could not translocate to aggregated platforms for receptor clustering.
30987996	7	93	theme	TRAIL	1303:1307	arg1	signaling					1315:1323	TRAIL death signaling	1303:1323	TRAIL death signaling	1303:1323	Apart from genetic changes in DR4-Ser424, we further classified various cancer cell lines originated from stomach, colon, lung, and glioblastoma according to their sensitivity to and receptor preference upon TRAIL death signaling and generated TRAIL-tolerant persister-derived DLD-1PER cells.
30987996	4	94	theme	patient-derived	627:641	arg1	library					659:665	a cancer patient-derived cDNA expression library	618:665	a cancer patient-derived cDNA expression library	618:665	We found that DR4-Ser424 mutations, identified from our cell-based functional screen using a cancer patient-derived cDNA expression library and from The Cancer Genome Atlas, caused TRAIL resistance in various human cancer cell lines.
30987996	11	95	theme	TRAIL	1969:1973	arg1	resistance					1975:1984	TRAIL resistance	1969:1984	TRAIL resistance in cancers	1969:1995	Our findings demonstrate that DR4 O-GlcNAcylation is crucial for TRAIL death signaling, providing new opportunities for TRAIL therapy overcoming TRAIL resistance in cancers.
30987996	1	96	theme	major	256:260	arg1	obstacle					262:269	a major obstacle	254:269	a major obstacle to translating TRAIL therapy into patients with cancer	254:324	TNF-related apoptosis-inducing ligand (TRAIL) resistance, including nongenetically acquired tolerance in cancer persister cells, is a major obstacle to translating TRAIL therapy into patients with cancer.
30987996	1	96	theme	major	256:260	arg1	resistance					168:177	TNF-related apoptosis-inducing ligand (TRAIL) resistance	122:177	TNF-related apoptosis-inducing ligand (TRAIL) resistance	122:177	TNF-related apoptosis-inducing ligand (TRAIL) resistance, including nongenetically acquired tolerance in cancer persister cells, is a major obstacle to translating TRAIL therapy into patients with cancer.
30987996	5	97	mod	modification	944:955	arg1	TRAIL					960:964	TRAIL cytotoxicity	960:977	TRAIL cytotoxicity	960:977	Using O-GlcNAc transferase knockdown cells, DR4-preferred versus DR5-preferred cancer cells, and a DR5-neutralizing antibody, we evaluated the essential role of DR4-specific O-GlcNAc modification in TRAIL cytotoxicity.
30987996	4	98	theme	expression	648:657	arg1	library					659:665	a cancer patient-derived cDNA expression library	618:665	a cancer patient-derived cDNA expression library	618:665	We found that DR4-Ser424 mutations, identified from our cell-based functional screen using a cancer patient-derived cDNA expression library and from The Cancer Genome Atlas, caused TRAIL resistance in various human cancer cell lines.
30987996	8	99	theme	TRAIL-resistant	1468:1482	arg1	cells					1491:1495	the TRAIL-resistant cancer cells	1464:1495	the TRAIL-resistant cancer cells	1464:1495	Among these, we discovered that DR4 was not modified by O-GlcNAc in most of the TRAIL-resistant cancer cells and DLD-1PER cells.
23301498	7	0	theme	protein	1438:1444	arg1	modification					1446:1457	O-GlcNAc protein modification	1429:1457	O-GlcNAc protein modification	1429:1457	About 200 proteins including several key players involved in the hexosamine signaling pathway showed significantly increased O-GlcNAcylation levels in response to the drug, which further strengthens the link of O-GlcNAc protein modification to cellular nutrient sensing and response.
23301498	6	1	from	effects	1106:1112	arg1	level					1165:1169	the level	1161:1169	the level of O-GlcNAc modification of cellular proteins	1161:1215	To demonstrate the practical utility of the developed approach, we studied the global effects of the O-GlcNAcase inhibitor GlcNAcstatin G on the level of O-GlcNAc modification of cellular proteins.
23301498	5	2	from	identification	954:967	arg1	proteins					1010:1017	80 proteins	1007:1017	80 proteins	1007:1017	Subsequent elution of covalently resin bound O-GlcNAc peptides using selective β-elimination enabled the identification of 185 O-GlcNAc modification sites on 80 proteins.
23301498	2	3	theme	systematic	375:384	arg1	identification					386:399	the systematic identification	371:399	the systematic identification of O-GlcNAc proteins	371:420	Despite its emerging biological significance, the systematic identification of O-GlcNAc proteins is still challenging.
23301498	1	4	theme	processes	265:273	arg1	variety					245:251	a wide variety	238:251	a wide variety of cellular processes	238:273	The post-translational modification of proteins with N-acetylglucosamine (O-GlcNAc) is involved in the regulation of a wide variety of cellular processes and associated with a number of chronic diseases.
23301498	1	4	theme	processes	265:273	arg1	processes					265:273	cellular processes	256:273	cellular processes	256:273	The post-translational modification of proteins with N-acetylglucosamine (O-GlcNAc) is involved in the regulation of a wide variety of cellular processes and associated with a number of chronic diseases.
23301498	7	5	theme	increased	1333:1341	arg1	levels					1359:1364	significantly increased O-GlcNAcylation levels	1319:1364	significantly increased O-GlcNAcylation levels in response to the drug, which further strengthens the link of O-GlcNAc protein modification to cellular nutrient sensing and response	1319:1499	About 200 proteins including several key players involved in the hexosamine signaling pathway showed significantly increased O-GlcNAcylation levels in response to the drug, which further strengthens the link of O-GlcNAc protein modification to cellular nutrient sensing and response.
23301498	5	6	theme	sites	998:1002	arg1	identification					954:967	the identification	950:967	the identification of 185 O-GlcNAc modification sites on 80 proteins	950:1017	Subsequent elution of covalently resin bound O-GlcNAc peptides using selective β-elimination enabled the identification of 185 O-GlcNAc modification sites on 80 proteins.
23301498	6	7	theme	O-GlcNAc	1174:1181	arg1	modification					1183:1194	O-GlcNAc modification	1174:1194	O-GlcNAc modification of cellular proteins	1174:1215	To demonstrate the practical utility of the developed approach, we studied the global effects of the O-GlcNAcase inhibitor GlcNAcstatin G on the level of O-GlcNAc modification of cellular proteins.
23301498	6	8	theme	modification	1183:1194	arg1	level					1165:1169	the level	1161:1169	the level of O-GlcNAc modification of cellular proteins	1161:1215	To demonstrate the practical utility of the developed approach, we studied the global effects of the O-GlcNAcase inhibitor GlcNAcstatin G on the level of O-GlcNAc modification of cellular proteins.
23301498	4	9	from	line	843:846	arg1	proteins					815:822	around 1500 O-GlcNAc proteins	794:822	around 1500 O-GlcNAc proteins from a single cell line	794:846	On-resin proteolysis using trypsin followed by LC-MS/MS afforded the identification of around 1500 O-GlcNAc proteins from a single cell line.
23301498	4	9	from	line	843:846	arg1	identification					776:789	the identification	772:789	the identification of around 1500 O-GlcNAc proteins from a single cell line	772:846	On-resin proteolysis using trypsin followed by LC-MS/MS afforded the identification of around 1500 O-GlcNAc proteins from a single cell line.
23301498	3	10	theme	cells	582:586	arg1	labeling					570:577	metabolic labeling	560:577	metabolic labeling of cells by azide-modified GlcNAc and copper-mediated Click chemistry for purification of modified proteins on an alkyne-resin	560:704	In the present study, we demonstrate a significantly improved O-GlcNAc protein enrichment procedure, which exploits metabolic labeling of cells by azide-modified GlcNAc and copper-mediated Click chemistry for purification of modified proteins on an alkyne-resin.
23301498	0	11	theme	mass	102:105	arg1	spectrometry					107:118	mass spectrometry	102:118	mass spectrometry	102:118	Proteome wide purification and identification of O-GlcNAc-modified proteins using click chemistry and mass spectrometry.
23301498	5	12	dep	bound	888:892	arg1	resin					882:886	resin	882:886	resin	882:886	Subsequent elution of covalently resin bound O-GlcNAc peptides using selective β-elimination enabled the identification of 185 O-GlcNAc modification sites on 80 proteins.
23301498	7	13	theme	several	1247:1253	arg1	players					1259:1265	several key players	1247:1265	several key players involved in the hexosamine signaling pathway	1247:1310	About 200 proteins including several key players involved in the hexosamine signaling pathway showed significantly increased O-GlcNAcylation levels in response to the drug, which further strengthens the link of O-GlcNAc protein modification to cellular nutrient sensing and response.
23301498	4	14	theme	single	831:836	arg1	line					843:846	a single cell line	829:846	a single cell line	829:846	On-resin proteolysis using trypsin followed by LC-MS/MS afforded the identification of around 1500 O-GlcNAc proteins from a single cell line.
23301498	4	15	from	identification	776:789	arg1	line					843:846	a single cell line	829:846	a single cell line	829:846	On-resin proteolysis using trypsin followed by LC-MS/MS afforded the identification of around 1500 O-GlcNAc proteins from a single cell line.
23301498	2	16	theme	emerging	337:344	arg1	significance					357:368	its emerging biological significance	333:368	its emerging biological significance	333:368	Despite its emerging biological significance, the systematic identification of O-GlcNAc proteins is still challenging.
23301498	7	17	theme	hexosamine	1283:1292	arg1	pathway					1304:1310	the hexosamine signaling pathway	1279:1310	the hexosamine signaling pathway	1279:1310	About 200 proteins including several key players involved in the hexosamine signaling pathway showed significantly increased O-GlcNAcylation levels in response to the drug, which further strengthens the link of O-GlcNAc protein modification to cellular nutrient sensing and response.
23301498	3	18	theme	enrichment	523:532	arg1	procedure					534:542	a significantly improved O-GlcNAc protein enrichment procedure	481:542	a significantly improved O-GlcNAc protein enrichment procedure	481:542	In the present study, we demonstrate a significantly improved O-GlcNAc protein enrichment procedure, which exploits metabolic labeling of cells by azide-modified GlcNAc and copper-mediated Click chemistry for purification of modified proteins on an alkyne-resin.
23301498	5	19	theme	selective	918:926	arg1	β-elimination					928:940	selective β-elimination	918:940	selective β-elimination	918:940	Subsequent elution of covalently resin bound O-GlcNAc peptides using selective β-elimination enabled the identification of 185 O-GlcNAc modification sites on 80 proteins.
23301498	3	20	theme	present	451:457	arg1	study					459:463	the present study	447:463	the present study	447:463	In the present study, we demonstrate a significantly improved O-GlcNAc protein enrichment procedure, which exploits metabolic labeling of cells by azide-modified GlcNAc and copper-mediated Click chemistry for purification of modified proteins on an alkyne-resin.
23301498	6	21	theme	GlcNAcstatin	1143:1154	arg1	G					1156:1156	the O-GlcNAcase inhibitor GlcNAcstatin G	1117:1156	the O-GlcNAcase inhibitor GlcNAcstatin G	1117:1156	To demonstrate the practical utility of the developed approach, we studied the global effects of the O-GlcNAcase inhibitor GlcNAcstatin G on the level of O-GlcNAc modification of cellular proteins.
23301498	7	22	theme	signaling	1294:1302	arg1	pathway					1304:1310	the hexosamine signaling pathway	1279:1310	the hexosamine signaling pathway	1279:1310	About 200 proteins including several key players involved in the hexosamine signaling pathway showed significantly increased O-GlcNAcylation levels in response to the drug, which further strengthens the link of O-GlcNAc protein modification to cellular nutrient sensing and response.
23301498	6	23	mod	modification	1183:1194	arg3	O-GlcNAc					1174:1181	O-GlcNAc modification	1174:1194	O-GlcNAc modification of cellular proteins	1174:1215	To demonstrate the practical utility of the developed approach, we studied the global effects of the O-GlcNAcase inhibitor GlcNAcstatin G on the level of O-GlcNAc modification of cellular proteins.
23301498	6	23	mod	modification	1183:1194	arg1	proteins					1208:1215	cellular proteins	1199:1215	cellular proteins	1199:1215	To demonstrate the practical utility of the developed approach, we studied the global effects of the O-GlcNAcase inhibitor GlcNAcstatin G on the level of O-GlcNAc modification of cellular proteins.
23301498	5	24	theme	bound	888:892	arg1	peptides					903:910	covalently resin bound O-GlcNAc peptides	871:910	covalently resin bound O-GlcNAc peptides using selective β-elimination	871:940	Subsequent elution of covalently resin bound O-GlcNAc peptides using selective β-elimination enabled the identification of 185 O-GlcNAc modification sites on 80 proteins.
23301498	0	25	theme	wide	9:12	arg1	purification					14:25	Proteome wide purification	0:25	Proteome wide purification	0:25	Proteome wide purification and identification of O-GlcNAc-modified proteins using click chemistry and mass spectrometry.
23301498	7	26	theme	O-GlcNAcylation	1343:1357	arg1	levels					1359:1364	significantly increased O-GlcNAcylation levels	1319:1364	significantly increased O-GlcNAcylation levels in response to the drug, which further strengthens the link of O-GlcNAc protein modification to cellular nutrient sensing and response	1319:1499	About 200 proteins including several key players involved in the hexosamine signaling pathway showed significantly increased O-GlcNAcylation levels in response to the drug, which further strengthens the link of O-GlcNAc protein modification to cellular nutrient sensing and response.
23301498	4	27	theme	proteins	815:822	arg1	identification					776:789	the identification	772:789	the identification of around 1500 O-GlcNAc proteins from a single cell line	772:846	On-resin proteolysis using trypsin followed by LC-MS/MS afforded the identification of around 1500 O-GlcNAc proteins from a single cell line.
23301498	2	28	theme	proteins	413:420	arg1	identification					386:399	the systematic identification	371:399	the systematic identification of O-GlcNAc proteins	371:420	Despite its emerging biological significance, the systematic identification of O-GlcNAc proteins is still challenging.
23301498	0	29	theme	Proteome	0:7	arg1	purification					14:25	Proteome wide purification	0:25	Proteome wide purification	0:25	Proteome wide purification and identification of O-GlcNAc-modified proteins using click chemistry and mass spectrometry.
23301498	6	30	theme	approach	1074:1081	arg1	utility					1049:1055	the practical utility	1035:1055	the practical utility of the developed approach	1035:1081	To demonstrate the practical utility of the developed approach, we studied the global effects of the O-GlcNAcase inhibitor GlcNAcstatin G on the level of O-GlcNAc modification of cellular proteins.
23301498	1	31	with	modification	144:155	arg1	N-acetylglucosamine					174:192	N-acetylglucosamine	174:192	N-acetylglucosamine (O-GlcNAc)	174:203	The post-translational modification of proteins with N-acetylglucosamine (O-GlcNAc) is involved in the regulation of a wide variety of cellular processes and associated with a number of chronic diseases.
23301498	1	31	with	modification	144:155	arg1	O-GlcNAc					195:202	O-GlcNAc	195:202	O-GlcNAc	195:202	The post-translational modification of proteins with N-acetylglucosamine (O-GlcNAc) is involved in the regulation of a wide variety of cellular processes and associated with a number of chronic diseases.
23301498	3	32	theme	copper-mediated	617:631	arg1	chemistry					639:647	copper-mediated Click chemistry	617:647	copper-mediated Click chemistry	617:647	In the present study, we demonstrate a significantly improved O-GlcNAc protein enrichment procedure, which exploits metabolic labeling of cells by azide-modified GlcNAc and copper-mediated Click chemistry for purification of modified proteins on an alkyne-resin.
23301498	2	33	theme	O-GlcNAc	404:411	arg1	proteins					413:420	O-GlcNAc proteins	404:420	O-GlcNAc proteins	404:420	Despite its emerging biological significance, the systematic identification of O-GlcNAc proteins is still challenging.
23301498	5	34	theme	O-GlcNAc	894:901	arg1	peptides					903:910	covalently resin bound O-GlcNAc peptides	871:910	covalently resin bound O-GlcNAc peptides using selective β-elimination	871:940	Subsequent elution of covalently resin bound O-GlcNAc peptides using selective β-elimination enabled the identification of 185 O-GlcNAc modification sites on 80 proteins.
23301498	6	35	theme	developed	1064:1072	arg1	approach					1074:1081	the developed approach	1060:1081	the developed approach	1060:1081	To demonstrate the practical utility of the developed approach, we studied the global effects of the O-GlcNAcase inhibitor GlcNAcstatin G on the level of O-GlcNAc modification of cellular proteins.
23301498	5	36	from	proteins	1010:1017	arg1	identification					954:967	the identification	950:967	the identification of 185 O-GlcNAc modification sites on 80 proteins	950:1017	Subsequent elution of covalently resin bound O-GlcNAc peptides using selective β-elimination enabled the identification of 185 O-GlcNAc modification sites on 80 proteins.
23301498	3	37	theme	azide-modified	591:604	arg1	GlcNAc					606:611	azide-modified GlcNAc	591:611	azide-modified GlcNAc	591:611	In the present study, we demonstrate a significantly improved O-GlcNAc protein enrichment procedure, which exploits metabolic labeling of cells by azide-modified GlcNAc and copper-mediated Click chemistry for purification of modified proteins on an alkyne-resin.
23301498	5	38	from	sites	998:1002	arg1	proteins					1010:1017	80 proteins	1007:1017	80 proteins	1007:1017	Subsequent elution of covalently resin bound O-GlcNAc peptides using selective β-elimination enabled the identification of 185 O-GlcNAc modification sites on 80 proteins.
23301498	6	39	theme	G	1156:1156	arg1	effects					1106:1112	the global effects	1095:1112	the global effects of the O-GlcNAcase inhibitor GlcNAcstatin G on the level of O-GlcNAc modification of cellular proteins	1095:1215	To demonstrate the practical utility of the developed approach, we studied the global effects of the O-GlcNAcase inhibitor GlcNAcstatin G on the level of O-GlcNAc modification of cellular proteins.
23301498	4	40	theme	O-GlcNAc	806:813	arg1	proteins					815:822	around 1500 O-GlcNAc proteins	794:822	around 1500 O-GlcNAc proteins from a single cell line	794:846	On-resin proteolysis using trypsin followed by LC-MS/MS afforded the identification of around 1500 O-GlcNAc proteins from a single cell line.
23301498	7	41	from	levels	1359:1364	arg1	response					1369:1376	response	1369:1376	response to the drug, which further strengthens the link of O-GlcNAc protein modification to cellular nutrient sensing and response	1369:1499	About 200 proteins including several key players involved in the hexosamine signaling pathway showed significantly increased O-GlcNAcylation levels in response to the drug, which further strengthens the link of O-GlcNAc protein modification to cellular nutrient sensing and response.
23301498	7	42	theme	O-GlcNAc	1429:1436	arg1	modification					1446:1457	O-GlcNAc protein modification	1429:1457	O-GlcNAc protein modification	1429:1457	About 200 proteins including several key players involved in the hexosamine signaling pathway showed significantly increased O-GlcNAcylation levels in response to the drug, which further strengthens the link of O-GlcNAc protein modification to cellular nutrient sensing and response.
23301498	3	43	theme	improved	497:504	arg1	procedure					534:542	a significantly improved O-GlcNAc protein enrichment procedure	481:542	a significantly improved O-GlcNAc protein enrichment procedure	481:542	In the present study, we demonstrate a significantly improved O-GlcNAc protein enrichment procedure, which exploits metabolic labeling of cells by azide-modified GlcNAc and copper-mediated Click chemistry for purification of modified proteins on an alkyne-resin.
23301498	5	44	theme	Subsequent	849:858	arg1	elution					860:866	Subsequent elution	849:866	Subsequent elution of covalently resin bound O-GlcNAc peptides using selective β-elimination	849:940	Subsequent elution of covalently resin bound O-GlcNAc peptides using selective β-elimination enabled the identification of 185 O-GlcNAc modification sites on 80 proteins.
23301498	1	45	theme	chronic	307:313	arg1	diseases					315:322	chronic diseases	307:322	chronic diseases	307:322	The post-translational modification of proteins with N-acetylglucosamine (O-GlcNAc) is involved in the regulation of a wide variety of cellular processes and associated with a number of chronic diseases.
23301498	6	46	theme	inhibitor	1133:1141	arg1	G					1156:1156	the O-GlcNAcase inhibitor GlcNAcstatin G	1117:1156	the O-GlcNAcase inhibitor GlcNAcstatin G	1117:1156	To demonstrate the practical utility of the developed approach, we studied the global effects of the O-GlcNAcase inhibitor GlcNAcstatin G on the level of O-GlcNAc modification of cellular proteins.
23301498	3	47	from	purification	653:664	arg1	alkyne-resin					693:704	an alkyne-resin	690:704	an alkyne-resin	690:704	In the present study, we demonstrate a significantly improved O-GlcNAc protein enrichment procedure, which exploits metabolic labeling of cells by azide-modified GlcNAc and copper-mediated Click chemistry for purification of modified proteins on an alkyne-resin.
23301498	4	48	theme	On-resin	707:714	arg1	proteolysis					716:726	On-resin proteolysis	707:726	On-resin proteolysis using trypsin followed by LC-MS/MS	707:761	On-resin proteolysis using trypsin followed by LC-MS/MS afforded the identification of around 1500 O-GlcNAc proteins from a single cell line.
23301498	7	49	theme	modification	1446:1457	arg1	link					1421:1424	the link	1417:1424	the link of O-GlcNAc protein modification to cellular nutrient sensing and response	1417:1499	About 200 proteins including several key players involved in the hexosamine signaling pathway showed significantly increased O-GlcNAcylation levels in response to the drug, which further strengthens the link of O-GlcNAc protein modification to cellular nutrient sensing and response.
23301498	1	50	theme	diseases	315:322	arg1	number					297:302	a number	295:302	a number of chronic diseases	295:322	The post-translational modification of proteins with N-acetylglucosamine (O-GlcNAc) is involved in the regulation of a wide variety of cellular processes and associated with a number of chronic diseases.
23301498	7	51	theme	key	1255:1257	arg1	players					1259:1265	several key players	1247:1265	several key players involved in the hexosamine signaling pathway	1247:1310	About 200 proteins including several key players involved in the hexosamine signaling pathway showed significantly increased O-GlcNAcylation levels in response to the drug, which further strengthens the link of O-GlcNAc protein modification to cellular nutrient sensing and response.
23301498	6	52	theme	global	1099:1104	arg1	effects					1106:1112	the global effects	1095:1112	the global effects of the O-GlcNAcase inhibitor GlcNAcstatin G on the level of O-GlcNAc modification of cellular proteins	1095:1215	To demonstrate the practical utility of the developed approach, we studied the global effects of the O-GlcNAcase inhibitor GlcNAcstatin G on the level of O-GlcNAc modification of cellular proteins.
23301498	6	53	theme	O-GlcNAcase	1121:1131	arg1	G					1156:1156	the O-GlcNAcase inhibitor GlcNAcstatin G	1117:1156	the O-GlcNAcase inhibitor GlcNAcstatin G	1117:1156	To demonstrate the practical utility of the developed approach, we studied the global effects of the O-GlcNAcase inhibitor GlcNAcstatin G on the level of O-GlcNAc modification of cellular proteins.
23301498	0	54	theme	proteins	67:74	arg1	purification					14:25	Proteome wide purification	0:25	Proteome wide purification	0:25	Proteome wide purification and identification of O-GlcNAc-modified proteins using click chemistry and mass spectrometry.
23301498	0	54	theme	proteins	67:74	arg1	identification					31:44	identification	31:44	identification	31:44	Proteome wide purification and identification of O-GlcNAc-modified proteins using click chemistry and mass spectrometry.
23301498	6	55	theme	practical	1039:1047	arg1	utility					1049:1055	the practical utility	1035:1055	the practical utility of the developed approach	1035:1081	To demonstrate the practical utility of the developed approach, we studied the global effects of the O-GlcNAcase inhibitor GlcNAcstatin G on the level of O-GlcNAc modification of cellular proteins.
23301498	5	56	theme	peptides	903:910	arg1	elution					860:866	Subsequent elution	849:866	Subsequent elution of covalently resin bound O-GlcNAc peptides using selective β-elimination	849:940	Subsequent elution of covalently resin bound O-GlcNAc peptides using selective β-elimination enabled the identification of 185 O-GlcNAc modification sites on 80 proteins.
23301498	3	57	theme	Click	633:637	arg1	chemistry					639:647	copper-mediated Click chemistry	617:647	copper-mediated Click chemistry	617:647	In the present study, we demonstrate a significantly improved O-GlcNAc protein enrichment procedure, which exploits metabolic labeling of cells by azide-modified GlcNAc and copper-mediated Click chemistry for purification of modified proteins on an alkyne-resin.
23301498	6	58	theme	cellular	1199:1206	arg1	proteins					1208:1215	cellular proteins	1199:1215	cellular proteins	1199:1215	To demonstrate the practical utility of the developed approach, we studied the global effects of the O-GlcNAcase inhibitor GlcNAcstatin G on the level of O-GlcNAc modification of cellular proteins.
23301498	1	59	theme	post-translational	125:142	arg1	modification					144:155	The post-translational modification	121:155	The post-translational modification of proteins with N-acetylglucosamine (O-GlcNAc)	121:203	The post-translational modification of proteins with N-acetylglucosamine (O-GlcNAc) is involved in the regulation of a wide variety of cellular processes and associated with a number of chronic diseases.
23301498	0	60	theme	O-GlcNAc-modified	49:65	arg1	proteins					67:74	O-GlcNAc-modified proteins	49:74	O-GlcNAc-modified proteins using click chemistry and mass spectrometry	49:118	Proteome wide purification and identification of O-GlcNAc-modified proteins using click chemistry and mass spectrometry.
23301498	3	61	theme	O-GlcNAc	506:513	arg1	procedure					534:542	a significantly improved O-GlcNAc protein enrichment procedure	481:542	a significantly improved O-GlcNAc protein enrichment procedure	481:542	In the present study, we demonstrate a significantly improved O-GlcNAc protein enrichment procedure, which exploits metabolic labeling of cells by azide-modified GlcNAc and copper-mediated Click chemistry for purification of modified proteins on an alkyne-resin.
23301498	7	62	theme	nutrient	1471:1478	arg1	sensing					1480:1486	cellular nutrient sensing	1462:1486	cellular nutrient sensing	1462:1486	About 200 proteins including several key players involved in the hexosamine signaling pathway showed significantly increased O-GlcNAcylation levels in response to the drug, which further strengthens the link of O-GlcNAc protein modification to cellular nutrient sensing and response.
23301498	3	63	theme	proteins	678:685	arg1	purification					653:664	purification	653:664	purification of modified proteins on an alkyne-resin	653:704	In the present study, we demonstrate a significantly improved O-GlcNAc protein enrichment procedure, which exploits metabolic labeling of cells by azide-modified GlcNAc and copper-mediated Click chemistry for purification of modified proteins on an alkyne-resin.
23301498	2	64	theme	biological	346:355	arg1	significance					357:368	its emerging biological significance	333:368	its emerging biological significance	333:368	Despite its emerging biological significance, the systematic identification of O-GlcNAc proteins is still challenging.
23301498	6	65	theme	proteins	1208:1215	arg1	modification					1183:1194	O-GlcNAc modification	1174:1194	O-GlcNAc modification of cellular proteins	1174:1215	To demonstrate the practical utility of the developed approach, we studied the global effects of the O-GlcNAcase inhibitor GlcNAcstatin G on the level of O-GlcNAc modification of cellular proteins.
23301498	1	66	theme	wide	240:243	arg1	variety					245:251	a wide variety	238:251	a wide variety of cellular processes	238:273	The post-translational modification of proteins with N-acetylglucosamine (O-GlcNAc) is involved in the regulation of a wide variety of cellular processes and associated with a number of chronic diseases.
23301498	1	66	theme	wide	240:243	arg1	processes					265:273	cellular processes	256:273	cellular processes	256:273	The post-translational modification of proteins with N-acetylglucosamine (O-GlcNAc) is involved in the regulation of a wide variety of cellular processes and associated with a number of chronic diseases.
23301498	4	67	theme	cell	838:841	arg1	line					843:846	a single cell line	829:846	a single cell line	829:846	On-resin proteolysis using trypsin followed by LC-MS/MS afforded the identification of around 1500 O-GlcNAc proteins from a single cell line.
23301498	1	68	theme	proteins	160:167	arg1	modification					144:155	The post-translational modification	121:155	The post-translational modification of proteins with N-acetylglucosamine (O-GlcNAc)	121:203	The post-translational modification of proteins with N-acetylglucosamine (O-GlcNAc) is involved in the regulation of a wide variety of cellular processes and associated with a number of chronic diseases.
23301498	1	69	theme	variety	245:251	arg1	regulation					224:233	the regulation	220:233	the regulation of a wide variety of cellular processes	220:273	The post-translational modification of proteins with N-acetylglucosamine (O-GlcNAc) is involved in the regulation of a wide variety of cellular processes and associated with a number of chronic diseases.
23301498	0	70	theme	click	82:86	arg1	chemistry					88:96	click chemistry	82:96	click chemistry	82:96	Proteome wide purification and identification of O-GlcNAc-modified proteins using click chemistry and mass spectrometry.
23301498	5	71	theme	modification	985:996	arg1	sites					998:1002	185 O-GlcNAc modification sites	972:1002	185 O-GlcNAc modification sites on 80 proteins	972:1017	Subsequent elution of covalently resin bound O-GlcNAc peptides using selective β-elimination enabled the identification of 185 O-GlcNAc modification sites on 80 proteins.
23301498	7	72	theme	cellular	1462:1469	arg1	sensing					1480:1486	cellular nutrient sensing	1462:1486	cellular nutrient sensing	1462:1486	About 200 proteins including several key players involved in the hexosamine signaling pathway showed significantly increased O-GlcNAcylation levels in response to the drug, which further strengthens the link of O-GlcNAc protein modification to cellular nutrient sensing and response.
23301498	5	73	theme	O-GlcNAc	976:983	arg1	sites					998:1002	185 O-GlcNAc modification sites	972:1002	185 O-GlcNAc modification sites on 80 proteins	972:1017	Subsequent elution of covalently resin bound O-GlcNAc peptides using selective β-elimination enabled the identification of 185 O-GlcNAc modification sites on 80 proteins.
23301498	3	74	theme	protein	515:521	arg1	procedure					534:542	a significantly improved O-GlcNAc protein enrichment procedure	481:542	a significantly improved O-GlcNAc protein enrichment procedure	481:542	In the present study, we demonstrate a significantly improved O-GlcNAc protein enrichment procedure, which exploits metabolic labeling of cells by azide-modified GlcNAc and copper-mediated Click chemistry for purification of modified proteins on an alkyne-resin.
23301498	3	75	theme	modified	669:676	arg1	proteins					678:685	modified proteins	669:685	modified proteins	669:685	In the present study, we demonstrate a significantly improved O-GlcNAc protein enrichment procedure, which exploits metabolic labeling of cells by azide-modified GlcNAc and copper-mediated Click chemistry for purification of modified proteins on an alkyne-resin.
23301498	3	76	theme	metabolic	560:568	arg1	labeling					570:577	metabolic labeling	560:577	metabolic labeling of cells by azide-modified GlcNAc and copper-mediated Click chemistry for purification of modified proteins on an alkyne-resin	560:704	In the present study, we demonstrate a significantly improved O-GlcNAc protein enrichment procedure, which exploits metabolic labeling of cells by azide-modified GlcNAc and copper-mediated Click chemistry for purification of modified proteins on an alkyne-resin.
23301498	1	77	theme	cellular	256:263	arg1	processes					265:273	cellular processes	256:273	cellular processes	256:273	The post-translational modification of proteins with N-acetylglucosamine (O-GlcNAc) is involved in the regulation of a wide variety of cellular processes and associated with a number of chronic diseases.
23395176	3	0	theme	peripheral	382:391	arg1	oscillation					399:409	peripheral clock oscillation	382:409	peripheral clock oscillation	382:409	Here we show that the hexosamine/O-GlcNAc pathway modulates peripheral clock oscillation.
23395176	6	1	theme	mice	746:749	arg1	analysis					713:720	In vivo analysis	705:720	In vivo analysis of genetically modified mice with perturbed hepatic OGT expression	705:787	In vivo analysis of genetically modified mice with perturbed hepatic OGT expression shows aberrant circadian rhythms of glucose homeostasis.
23395176	3	2	theme	clock	393:397	arg1	oscillation					399:409	peripheral clock oscillation	382:409	peripheral clock oscillation	382:409	Here we show that the hexosamine/O-GlcNAc pathway modulates peripheral clock oscillation.
23395176	4	3	theme	target genes	474:485	arg1	expression					448:457	expression	448:457	expression of BMAL1/CLOCK target genes	448:485	O-GlcNAc transferase (OGT) promotes expression of BMAL1/CLOCK target genes and affects circadian oscillation of clock genes in vitro and in vivo.
23395176	6	4	theme	modified	737:744	arg1	mice					746:749	genetically modified mice	725:749	genetically modified mice	725:749	In vivo analysis of genetically modified mice with perturbed hepatic OGT expression shows aberrant circadian rhythms of glucose homeostasis.
23395176	4	5	theme	BMAL1/CLOCK	462:472	arg1	target genes					474:485	BMAL1/CLOCK target genes	462:485	BMAL1/CLOCK target genes	462:485	O-GlcNAc transferase (OGT) promotes expression of BMAL1/CLOCK target genes and affects circadian oscillation of clock genes in vitro and in vivo.
23395176	7	6	theme	circadian	969:977	arg1	clock					979:983	the circadian clock	965:983	the circadian clock	965:983	These results establish the counteraction between O-GlcNAcylation and ubiquitination as a key mechanism that regulates the circadian clock and suggest a crucial role for O-GlcNAc signaling in transducing nutritional signals to the core circadian timing machinery.
23395176	2	7	theme	Nutrient	180:187	arg1	flux					189:192	Nutrient flux	180:192	Nutrient flux into the hexosamine biosynthesis pathway	180:233	Nutrient flux into the hexosamine biosynthesis pathway triggers covalent protein modification by O-linked β-D-N-acetylglucosamine (O-GlcNAc).
23395176	7	8	theme	O-GlcNAc	1016:1023	arg1	signaling					1025:1033	O-GlcNAc signaling	1016:1033	O-GlcNAc signaling	1016:1033	These results establish the counteraction between O-GlcNAcylation and ubiquitination as a key mechanism that regulates the circadian clock and suggest a crucial role for O-GlcNAc signaling in transducing nutritional signals to the core circadian timing machinery.
23395176	6	9	with	analysis	713:720	arg1	expression					778:787	perturbed hepatic OGT expression	756:787	perturbed hepatic OGT expression	756:787	In vivo analysis of genetically modified mice with perturbed hepatic OGT expression shows aberrant circadian rhythms of glucose homeostasis.
23395176	6	10	theme	homeostasis	833:843	arg1	rhythms					814:820	aberrant circadian rhythms	795:820	aberrant circadian rhythms of glucose homeostasis	795:843	In vivo analysis of genetically modified mice with perturbed hepatic OGT expression shows aberrant circadian rhythms of glucose homeostasis.
23395176	7	11	theme	timing	1092:1097	arg1	machinery					1099:1107	the core circadian timing machinery	1073:1107	the core circadian timing machinery	1073:1107	These results establish the counteraction between O-GlcNAcylation and ubiquitination as a key mechanism that regulates the circadian clock and suggest a crucial role for O-GlcNAc signaling in transducing nutritional signals to the core circadian timing machinery.
23395176	1	12	theme	Circadian	90:98	arg1	clocks					100:105	Circadian clocks	90:105	Circadian clocks	90:105	Circadian clocks are coupled to metabolic oscillations through nutrient-sensing pathways.
23395176	6	13	theme	glucose	825:831	arg1	homeostasis					833:843	glucose homeostasis	825:843	glucose homeostasis	825:843	In vivo analysis of genetically modified mice with perturbed hepatic OGT expression shows aberrant circadian rhythms of glucose homeostasis.
23395176	7	14	theme	crucial	999:1005	arg1	role					1007:1010	a crucial role	997:1010	a crucial role for O-GlcNAc signaling in transducing nutritional signals to the core circadian timing machinery	997:1107	These results establish the counteraction between O-GlcNAcylation and ubiquitination as a key mechanism that regulates the circadian clock and suggest a crucial role for O-GlcNAc signaling in transducing nutritional signals to the core circadian timing machinery.
23395176	0	15	theme	O-GlcNAc	0:7	arg1	signaling					9:17	O-GlcNAc signaling	0:17	O-GlcNAc signaling	0:17	O-GlcNAc signaling entrains the circadian clock by inhibiting BMAL1/CLOCK ubiquitination.
23395176	7	16	theme	core	1077:1080	arg1	machinery					1099:1107	the core circadian timing machinery	1073:1107	the core circadian timing machinery	1073:1107	These results establish the counteraction between O-GlcNAcylation and ubiquitination as a key mechanism that regulates the circadian clock and suggest a crucial role for O-GlcNAc signaling in transducing nutritional signals to the core circadian timing machinery.
23395176	7	17	theme	nutritional	1050:1060	arg1	signals					1062:1068	nutritional signals	1050:1068	nutritional signals	1050:1068	These results establish the counteraction between O-GlcNAcylation and ubiquitination as a key mechanism that regulates the circadian clock and suggest a crucial role for O-GlcNAc signaling in transducing nutritional signals to the core circadian timing machinery.
23395176	6	18	theme	In vivo	705:711	arg1	analysis					713:720	In vivo analysis	705:720	In vivo analysis of genetically modified mice with perturbed hepatic OGT expression	705:787	In vivo analysis of genetically modified mice with perturbed hepatic OGT expression shows aberrant circadian rhythms of glucose homeostasis.
23395176	7	19	theme	circadian	1082:1090	arg1	machinery					1099:1107	the core circadian timing machinery	1073:1107	the core circadian timing machinery	1073:1107	These results establish the counteraction between O-GlcNAcylation and ubiquitination as a key mechanism that regulates the circadian clock and suggest a crucial role for O-GlcNAc signaling in transducing nutritional signals to the core circadian timing machinery.
23395176	6	20	theme	circadian	804:812	arg1	rhythms					814:820	aberrant circadian rhythms	795:820	aberrant circadian rhythms of glucose homeostasis	795:843	In vivo analysis of genetically modified mice with perturbed hepatic OGT expression shows aberrant circadian rhythms of glucose homeostasis.
23395176	2	21	theme	biosynthesis	214:225	arg1	pathway					227:233	the hexosamine biosynthesis pathway	199:233	the hexosamine biosynthesis pathway	199:233	Nutrient flux into the hexosamine biosynthesis pathway triggers covalent protein modification by O-linked β-D-N-acetylglucosamine (O-GlcNAc).
23395176	6	22	theme	aberrant	795:802	arg1	rhythms					814:820	aberrant circadian rhythms	795:820	aberrant circadian rhythms of glucose homeostasis	795:843	In vivo analysis of genetically modified mice with perturbed hepatic OGT expression shows aberrant circadian rhythms of glucose homeostasis.
23395176	2	23	theme	hexosamine	203:212	arg1	pathway					227:233	the hexosamine biosynthesis pathway	199:233	the hexosamine biosynthesis pathway	199:233	Nutrient flux into the hexosamine biosynthesis pathway triggers covalent protein modification by O-linked β-D-N-acetylglucosamine (O-GlcNAc).
23395176	0	24	theme	circadian	32:40	arg1	clock					42:46	the circadian clock	28:46	the circadian clock	28:46	O-GlcNAc signaling entrains the circadian clock by inhibiting BMAL1/CLOCK ubiquitination.
23395176	2	25	theme	O-linked	277:284	arg1	O-GlcNAc					311:318	O-GlcNAc	311:318	O-GlcNAc	311:318	Nutrient flux into the hexosamine biosynthesis pathway triggers covalent protein modification by O-linked β-D-N-acetylglucosamine (O-GlcNAc).
23395176	2	25	theme	O-linked	277:284	arg1	β-D-N-acetylglucosamine					286:308	O-linked β-D-N-acetylglucosamine	277:308	O-linked β-D-N-acetylglucosamine (O-GlcNAc)	277:319	Nutrient flux into the hexosamine biosynthesis pathway triggers covalent protein modification by O-linked β-D-N-acetylglucosamine (O-GlcNAc).
23395176	7	26	theme	key	936:938	arg1	counteraction					874:886	the counteraction	870:886	the counteraction between O-GlcNAcylation and ubiquitination	870:929	These results establish the counteraction between O-GlcNAcylation and ubiquitination as a key mechanism that regulates the circadian clock and suggest a crucial role for O-GlcNAc signaling in transducing nutritional signals to the core circadian timing machinery.
23395176	7	26	theme	key	936:938	arg1	mechanism					940:948	a key mechanism	934:948	a key mechanism that regulates the circadian clock	934:983	These results establish the counteraction between O-GlcNAcylation and ubiquitination as a key mechanism that regulates the circadian clock and suggest a crucial role for O-GlcNAc signaling in transducing nutritional signals to the core circadian timing machinery.
23395176	4	27	theme	O-GlcNAc	412:419	arg1	transferase					421:431	O-GlcNAc transferase	412:431	O-GlcNAc transferase (OGT)	412:437	O-GlcNAc transferase (OGT) promotes expression of BMAL1/CLOCK target genes and affects circadian oscillation of clock genes in vitro and in vivo.
23395176	4	27	theme	O-GlcNAc	412:419	arg1	OGT					434:436	OGT	434:436	OGT	434:436	O-GlcNAc transferase (OGT) promotes expression of BMAL1/CLOCK target genes and affects circadian oscillation of clock genes in vitro and in vivo.
23395176	1	28	theme	metabolic	122:130	arg1	oscillations					132:143	metabolic oscillations	122:143	metabolic oscillations	122:143	Circadian clocks are coupled to metabolic oscillations through nutrient-sensing pathways.
23395176	2	29	theme	protein	253:259	arg1	modification					261:272	covalent protein modification	244:272	covalent protein modification	244:272	Nutrient flux into the hexosamine biosynthesis pathway triggers covalent protein modification by O-linked β-D-N-acetylglucosamine (O-GlcNAc).
23395176	4	30	theme	circadian	499:507	arg1	oscillation					509:519	circadian oscillation	499:519	circadian oscillation of clock genes in vitro and in vivo	499:555	O-GlcNAc transferase (OGT) promotes expression of BMAL1/CLOCK target genes and affects circadian oscillation of clock genes in vitro and in vivo.
23395176	2	31	theme	covalent	244:251	arg1	modification					261:272	covalent protein modification	244:272	covalent protein modification	244:272	Nutrient flux into the hexosamine biosynthesis pathway triggers covalent protein modification by O-linked β-D-N-acetylglucosamine (O-GlcNAc).
23395176	6	32	theme	OGT	774:776	arg1	expression					778:787	perturbed hepatic OGT expression	756:787	perturbed hepatic OGT expression	756:787	In vivo analysis of genetically modified mice with perturbed hepatic OGT expression shows aberrant circadian rhythms of glucose homeostasis.
23395176	4	33	dep	clock genes	524:534	arg1	clock genes					524:534	clock genes in vitro and in vivo	524:555	clock genes in vitro and in vivo	524:555	O-GlcNAc transferase (OGT) promotes expression of BMAL1/CLOCK target genes and affects circadian oscillation of clock genes in vitro and in vivo.
23395176	4	33	dep	clock genes	524:534	arg1	in vivo					549:555	in vivo	549:555	in vivo	549:555	O-GlcNAc transferase (OGT) promotes expression of BMAL1/CLOCK target genes and affects circadian oscillation of clock genes in vitro and in vivo.
23395176	4	33	dep	clock genes	524:534	arg1	in vitro					536:543	in vitro	536:543	in vitro	536:543	O-GlcNAc transferase (OGT) promotes expression of BMAL1/CLOCK target genes and affects circadian oscillation of clock genes in vitro and in vivo.
23395176	3	34	theme	hexosamine/O-GlcNAc	344:362	arg1	pathway					364:370	the hexosamine/O-GlcNAc pathway	340:370	the hexosamine/O-GlcNAc pathway	340:370	Here we show that the hexosamine/O-GlcNAc pathway modulates peripheral clock oscillation.
23395176	4	35	theme	clock genes	524:534	arg1	oscillation					509:519	circadian oscillation	499:519	circadian oscillation of clock genes in vitro and in vivo	499:555	O-GlcNAc transferase (OGT) promotes expression of BMAL1/CLOCK target genes and affects circadian oscillation of clock genes in vitro and in vivo.
23395176	1	36	theme	nutrient-sensing	153:168	arg1	pathways					170:177	nutrient-sensing pathways	153:177	nutrient-sensing pathways	153:177	Circadian clocks are coupled to metabolic oscillations through nutrient-sensing pathways.
23395176	6	37	theme	hepatic	766:772	arg1	expression					778:787	perturbed hepatic OGT expression	756:787	perturbed hepatic OGT expression	756:787	In vivo analysis of genetically modified mice with perturbed hepatic OGT expression shows aberrant circadian rhythms of glucose homeostasis.
23395176	6	38	theme	perturbed	756:764	arg1	expression					778:787	perturbed hepatic OGT expression	756:787	perturbed hepatic OGT expression	756:787	In vivo analysis of genetically modified mice with perturbed hepatic OGT expression shows aberrant circadian rhythms of glucose homeostasis.
23395176	0	39	theme	BMAL1/CLOCK	62:72	arg1	ubiquitination					74:87	BMAL1/CLOCK ubiquitination	62:87	BMAL1/CLOCK ubiquitination	62:87	O-GlcNAc signaling entrains the circadian clock by inhibiting BMAL1/CLOCK ubiquitination.
23395176	5	40	theme	protein	621:627	arg1	modification					629:640	this protein modification	616:640	this protein modification	616:640	Both BMAL1 and CLOCK are rhythmically O-GlcNAcylated, and this protein modification stabilizes BMAL1 and CLOCK by inhibiting their ubiquitination.
23395176	2	41	link	O-linked	277:284	arg1	O-GlcNAc					311:318	O-GlcNAc	311:318	O-GlcNAc	311:318	Nutrient flux into the hexosamine biosynthesis pathway triggers covalent protein modification by O-linked β-D-N-acetylglucosamine (O-GlcNAc).
23395176	2	41	link	O-linked	277:284	arg1	β-D-N-acetylglucosamine					286:308	O-linked β-D-N-acetylglucosamine	277:308	O-linked β-D-N-acetylglucosamine (O-GlcNAc)	277:319	Nutrient flux into the hexosamine biosynthesis pathway triggers covalent protein modification by O-linked β-D-N-acetylglucosamine (O-GlcNAc).
22661428	5	0	theme	O-GlcNAc	788:795	arg1	strategy					812:819	a straightforward O-GlcNAc identification strategy	770:819	a straightforward O-GlcNAc identification strategy based on our recently developed Oscore software that automatically analyzes tandem mass spectra for the presence and intensity of O-GlcNAc diagnostic fragment ions	770:983	To this end, we conceived a straightforward O-GlcNAc identification strategy based on our recently developed Oscore software that automatically analyzes tandem mass spectra for the presence and intensity of O-GlcNAc diagnostic fragment ions.
22661428	1	1	from	modification	185:196	arg1	proteins					225:232	nuclear and cytoplasmic proteins	201:232	nuclear and cytoplasmic proteins with emerging roles in numerous cellular processes, such as signal transduction, transcription, and translation	201:344	The attachment of N-acetylglucosamine to serine or threonine residues (O-GlcNAc) is a post-translational modification on nuclear and cytoplasmic proteins with emerging roles in numerous cellular processes, such as signal transduction, transcription, and translation.
22661428	4	2	theme	data	733:736	arg1	sets					738:741	large-scale proteome data sets	712:741	large-scale proteome data sets	712:741	In the present study, we assessed if, and to which extent, O-GlcNAc-modified proteins can be discovered from existing large-scale proteome data sets.
22661428	1	3	theme	cellular	266:273	arg1	transduction					301:312	signal transduction	294:312	signal transduction	294:312	The attachment of N-acetylglucosamine to serine or threonine residues (O-GlcNAc) is a post-translational modification on nuclear and cytoplasmic proteins with emerging roles in numerous cellular processes, such as signal transduction, transcription, and translation.
22661428	1	3	theme	cellular	266:273	arg1	processes					275:283	numerous cellular processes	257:283	numerous cellular processes	257:283	The attachment of N-acetylglucosamine to serine or threonine residues (O-GlcNAc) is a post-translational modification on nuclear and cytoplasmic proteins with emerging roles in numerous cellular processes, such as signal transduction, transcription, and translation.
22661428	1	3	theme	cellular	266:273	arg1	transcription					315:327	transcription	315:327	transcription	315:327	The attachment of N-acetylglucosamine to serine or threonine residues (O-GlcNAc) is a post-translational modification on nuclear and cytoplasmic proteins with emerging roles in numerous cellular processes, such as signal transduction, transcription, and translation.
22661428	1	3	theme	cellular	266:273	arg1	translation					334:344	translation	334:344	translation	334:344	The attachment of N-acetylglucosamine to serine or threonine residues (O-GlcNAc) is a post-translational modification on nuclear and cytoplasmic proteins with emerging roles in numerous cellular processes, such as signal transduction, transcription, and translation.
22661428	5	4	theme	identification	797:810	arg1	strategy					812:819	a straightforward O-GlcNAc identification strategy	770:819	a straightforward O-GlcNAc identification strategy based on our recently developed Oscore software that automatically analyzes tandem mass spectra for the presence and intensity of O-GlcNAc diagnostic fragment ions	770:983	To this end, we conceived a straightforward O-GlcNAc identification strategy based on our recently developed Oscore software that automatically analyzes tandem mass spectra for the presence and intensity of O-GlcNAc diagnostic fragment ions.
22661428	4	5	theme	proteome	724:731	arg1	sets					738:741	large-scale proteome data sets	712:741	large-scale proteome data sets	712:741	In the present study, we assessed if, and to which extent, O-GlcNAc-modified proteins can be discovered from existing large-scale proteome data sets.
22661428	8	6	from	comparison	1416:1425	arg1	data					1486:1489	the very same data	1472:1489	the very same data	1472:1489	However, a comparison of O-GlcNAc and phospho-identifications from the very same data indicates that the O-GlcNAc modification is considerably less abundant than phosphorylation.
22661428	6	7	theme	peptides	1039:1046	arg1	hundreds					1018:1025	hundreds	1018:1025	hundreds	1018:1025	Using the Oscore, we discovered hundreds of O-GlcNAc peptides not initially identified in these studies, and most of which have not been described before.
22661428	0	8	from	Discovery	0:8	arg1	data					74:77	published large-scale proteome data	43:77	published large-scale proteome data	43:77	Discovery of O-GlcNAc-modified proteins in published large-scale proteome data.
22661428	3	9	theme	enrichment	582:591	arg1	form					562:565	some form	557:565	some form of biochemical enrichment	557:591	O-GlcNAc proteins are commonly identified by tandem mass spectrometry following some form of biochemical enrichment.
22661428	6	10	theme	O-GlcNAc	1030:1037	arg1	peptides					1039:1046	O-GlcNAc peptides	1030:1046	O-GlcNAc peptides not initially identified in these studies	1030:1088	Using the Oscore, we discovered hundreds of O-GlcNAc peptides not initially identified in these studies, and most of which have not been described before.
22661428	9	11	dep	peptides	1641:1648	arg1	i.e.					1636:1639	i.e.	1636:1639	i.e.	1636:1639	The discovery of numerous doubly modified peptides (i.e. peptides with one or multiple O-GlcNAc or phosphate moieties), suggests that O-GlcNAc and phosphorylation are not necessarily mutually exclusive, but can occur simultaneously at adjacent sites.
22661428	9	12	theme	peptides	1626:1633	arg1	discovery					1588:1596	The discovery	1584:1596	The discovery	1584:1596	The discovery of numerous doubly modified peptides (i.e. peptides with one or multiple O-GlcNAc or phosphate moieties), suggests that O-GlcNAc and phosphorylation are not necessarily mutually exclusive, but can occur simultaneously at adjacent sites.
22661428	9	13	theme	adjacent	1819:1826	arg1	sites					1828:1832	adjacent sites	1819:1832	adjacent sites	1819:1832	The discovery of numerous doubly modified peptides (i.e. peptides with one or multiple O-GlcNAc or phosphate moieties), suggests that O-GlcNAc and phosphorylation are not necessarily mutually exclusive, but can occur simultaneously at adjacent sites.
22661428	5	14	theme	O-GlcNAc	951:958	arg1	ions					980:983	O-GlcNAc diagnostic fragment ions	951:983	O-GlcNAc diagnostic fragment ions	951:983	To this end, we conceived a straightforward O-GlcNAc identification strategy based on our recently developed Oscore software that automatically analyzes tandem mass spectra for the presence and intensity of O-GlcNAc diagnostic fragment ions.
22661428	7	15	dep	extended	1171:1178	arg1	re-searching					1148:1159	re-searching	1148:1159	re-searching	1148:1159	Merely re-searching this data extended the number of known O-GlcNAc proteins by almost 100 suggesting that this modification exists even more widely than previously anticipated and the modification is often sufficiently abundant to be detected without enrichment.
22661428	1	16	theme	post-translational	166:183	arg1	attachment					84:93	The attachment	80:93	The attachment of N-acetylglucosamine to serine or threonine residues (O-GlcNAc)	80:159	The attachment of N-acetylglucosamine to serine or threonine residues (O-GlcNAc) is a post-translational modification on nuclear and cytoplasmic proteins with emerging roles in numerous cellular processes, such as signal transduction, transcription, and translation.
22661428	1	16	theme	post-translational	166:183	arg1	modification					185:196	a post-translational modification	164:196	a post-translational modification on nuclear and cytoplasmic proteins with emerging roles in numerous cellular processes, such as signal transduction, transcription, and translation	164:344	The attachment of N-acetylglucosamine to serine or threonine residues (O-GlcNAc) is a post-translational modification on nuclear and cytoplasmic proteins with emerging roles in numerous cellular processes, such as signal transduction, transcription, and translation.
22661428	3	17	theme	biochemical	570:580	arg1	enrichment					582:591	biochemical enrichment	570:591	biochemical enrichment	570:591	O-GlcNAc proteins are commonly identified by tandem mass spectrometry following some form of biochemical enrichment.
22661428	2	18	theme	site-specific	398:410	arg1	interplay					445:453	a site-specific, dynamic and possibly functional interplay	396:453	a site-specific, dynamic and possibly functional interplay with phosphorylation	396:474	It is further presumed that O-GlcNAc can exhibit a site-specific, dynamic and possibly functional interplay with phosphorylation.
22661428	7	19	theme	proteins	1209:1216	arg1	number					1184:1189	the number	1180:1189	the number of known O-GlcNAc proteins	1180:1216	Merely re-searching this data extended the number of known O-GlcNAc proteins by almost 100 suggesting that this modification exists even more widely than previously anticipated and the modification is often sufficiently abundant to be detected without enrichment.
22661428	9	20	theme	numerous	1601:1608	arg1	peptides					1626:1633	numerous doubly modified peptides	1601:1633	numerous doubly modified peptides (i.e. peptides with one or multiple O-GlcNAc or phosphate moieties)	1601:1701	The discovery of numerous doubly modified peptides (i.e. peptides with one or multiple O-GlcNAc or phosphate moieties), suggests that O-GlcNAc and phosphorylation are not necessarily mutually exclusive, but can occur simultaneously at adjacent sites.
22661428	9	21	theme	multiple	1662:1669	arg1	O-GlcNAc					1671:1678	multiple O-GlcNAc or phosphate moieties	1662:1700	O-GlcNAc	1671:1678	The discovery of numerous doubly modified peptides (i.e. peptides with one or multiple O-GlcNAc or phosphate moieties), suggests that O-GlcNAc and phosphorylation are not necessarily mutually exclusive, but can occur simultaneously at adjacent sites.
22661428	5	22	theme	developed	843:851	arg1	software					860:867	our recently developed Oscore software	830:867	our recently developed Oscore software that automatically analyzes tandem mass spectra for the presence and intensity of O-GlcNAc diagnostic fragment ions	830:983	To this end, we conceived a straightforward O-GlcNAc identification strategy based on our recently developed Oscore software that automatically analyzes tandem mass spectra for the presence and intensity of O-GlcNAc diagnostic fragment ions.
22661428	1	23	theme	N-acetylglucosamine	98:116	arg1	attachment					84:93	The attachment	80:93	The attachment of N-acetylglucosamine to serine or threonine residues (O-GlcNAc)	80:159	The attachment of N-acetylglucosamine to serine or threonine residues (O-GlcNAc) is a post-translational modification on nuclear and cytoplasmic proteins with emerging roles in numerous cellular processes, such as signal transduction, transcription, and translation.
22661428	1	23	theme	N-acetylglucosamine	98:116	arg1	modification					185:196	a post-translational modification	164:196	a post-translational modification on nuclear and cytoplasmic proteins with emerging roles in numerous cellular processes, such as signal transduction, transcription, and translation	164:344	The attachment of N-acetylglucosamine to serine or threonine residues (O-GlcNAc) is a post-translational modification on nuclear and cytoplasmic proteins with emerging roles in numerous cellular processes, such as signal transduction, transcription, and translation.
22661428	1	24	theme	nuclear	201:207	arg1	proteins					225:232	nuclear and cytoplasmic proteins	201:232	nuclear and cytoplasmic proteins with emerging roles in numerous cellular processes, such as signal transduction, transcription, and translation	201:344	The attachment of N-acetylglucosamine to serine or threonine residues (O-GlcNAc) is a post-translational modification on nuclear and cytoplasmic proteins with emerging roles in numerous cellular processes, such as signal transduction, transcription, and translation.
22661428	0	25	theme	proteins	31:38	arg1	Discovery					0:8	Discovery	0:8	Discovery of O-GlcNAc-modified proteins in published large-scale proteome data.	0:78	Discovery of O-GlcNAc-modified proteins in published large-scale proteome data.
22661428	1	26	theme	signal	294:299	arg1	transduction					301:312	signal transduction	294:312	signal transduction	294:312	The attachment of N-acetylglucosamine to serine or threonine residues (O-GlcNAc) is a post-translational modification on nuclear and cytoplasmic proteins with emerging roles in numerous cellular processes, such as signal transduction, transcription, and translation.
22661428	1	27	with	proteins	225:232	arg1	roles					248:252	emerging roles	239:252	emerging roles in numerous cellular processes, such as signal transduction, transcription, and translation	239:344	The attachment of N-acetylglucosamine to serine or threonine residues (O-GlcNAc) is a post-translational modification on nuclear and cytoplasmic proteins with emerging roles in numerous cellular processes, such as signal transduction, transcription, and translation.
22661428	5	28	dep	presence	925:932	arg1	the					921:923	the	921:923	the	921:923	To this end, we conceived a straightforward O-GlcNAc identification strategy based on our recently developed Oscore software that automatically analyzes tandem mass spectra for the presence and intensity of O-GlcNAc diagnostic fragment ions.
22661428	8	29	from	data	1486:1489	arg1	comparison					1416:1425	a comparison	1414:1425	a comparison of O-GlcNAc and phospho-identifications from the very same data	1414:1489	However, a comparison of O-GlcNAc and phospho-identifications from the very same data indicates that the O-GlcNAc modification is considerably less abundant than phosphorylation.
22661428	8	29	from	data	1486:1489	arg1	phospho-identifications					1443:1465	phospho-identifications	1443:1465	phospho-identifications from the very same data	1443:1489	However, a comparison of O-GlcNAc and phospho-identifications from the very same data indicates that the O-GlcNAc modification is considerably less abundant than phosphorylation.
22661428	8	29	from	data	1486:1489	arg1	O-GlcNAc					1430:1437	O-GlcNAc	1430:1437	O-GlcNAc	1430:1437	However, a comparison of O-GlcNAc and phospho-identifications from the very same data indicates that the O-GlcNAc modification is considerably less abundant than phosphorylation.
22661428	2	30	theme	functional	434:443	arg1	interplay					445:453	a site-specific, dynamic and possibly functional interplay	396:453	a site-specific, dynamic and possibly functional interplay with phosphorylation	396:474	It is further presumed that O-GlcNAc can exhibit a site-specific, dynamic and possibly functional interplay with phosphorylation.
22661428	0	31	theme	O-GlcNAc-modified	13:29	arg1	proteins					31:38	O-GlcNAc-modified proteins	13:38	O-GlcNAc-modified proteins	13:38	Discovery of O-GlcNAc-modified proteins in published large-scale proteome data.
22661428	1	32	attach	attachment	84:93	arg2	N-acetylglucosamine					98:116	N-acetylglucosamine	98:116	N-acetylglucosamine	98:116	The attachment of N-acetylglucosamine to serine or threonine residues (O-GlcNAc) is a post-translational modification on nuclear and cytoplasmic proteins with emerging roles in numerous cellular processes, such as signal transduction, transcription, and translation.
22661428	1	32	attach	attachment	84:93	arg1	threonine					131:139	threonine	131:139	threonine	131:139	The attachment of N-acetylglucosamine to serine or threonine residues (O-GlcNAc) is a post-translational modification on nuclear and cytoplasmic proteins with emerging roles in numerous cellular processes, such as signal transduction, transcription, and translation.
22661428	1	32	attach	attachment	84:93	arg1	O-GlcNAc					151:158	O-GlcNAc	151:158	O-GlcNAc	151:158	The attachment of N-acetylglucosamine to serine or threonine residues (O-GlcNAc) is a post-translational modification on nuclear and cytoplasmic proteins with emerging roles in numerous cellular processes, such as signal transduction, transcription, and translation.
22661428	1	32	attach	attachment	84:93	arg1	serine					121:126	serine	121:126	serine	121:126	The attachment of N-acetylglucosamine to serine or threonine residues (O-GlcNAc) is a post-translational modification on nuclear and cytoplasmic proteins with emerging roles in numerous cellular processes, such as signal transduction, transcription, and translation.
22661428	9	33	dep	peptides	1626:1633	arg1	peptides					1641:1648	peptides	1641:1648	peptides with one or multiple O-GlcNAc or phosphate moieties	1641:1700	The discovery of numerous doubly modified peptides (i.e. peptides with one or multiple O-GlcNAc or phosphate moieties), suggests that O-GlcNAc and phosphorylation are not necessarily mutually exclusive, but can occur simultaneously at adjacent sites.
22661428	1	34	theme	cytoplasmic	213:223	arg1	proteins					225:232	nuclear and cytoplasmic proteins	201:232	nuclear and cytoplasmic proteins with emerging roles in numerous cellular processes, such as signal transduction, transcription, and translation	201:344	The attachment of N-acetylglucosamine to serine or threonine residues (O-GlcNAc) is a post-translational modification on nuclear and cytoplasmic proteins with emerging roles in numerous cellular processes, such as signal transduction, transcription, and translation.
22661428	0	35	theme	published	43:51	arg1	data					74:77	published large-scale proteome data	43:77	published large-scale proteome data	43:77	Discovery of O-GlcNAc-modified proteins in published large-scale proteome data.
22661428	4	36	theme	present	601:607	arg1	study					609:613	the present study	597:613	the present study	597:613	In the present study, we assessed if, and to which extent, O-GlcNAc-modified proteins can be discovered from existing large-scale proteome data sets.
22661428	8	37	theme	phospho-identifications	1443:1465	arg1	comparison					1416:1425	a comparison	1414:1425	a comparison of O-GlcNAc and phospho-identifications from the very same data	1414:1489	However, a comparison of O-GlcNAc and phospho-identifications from the very same data indicates that the O-GlcNAc modification is considerably less abundant than phosphorylation.
22661428	3	38	theme	O-GlcNAc	477:484	arg1	proteins					486:493	O-GlcNAc proteins	477:493	O-GlcNAc proteins	477:493	O-GlcNAc proteins are commonly identified by tandem mass spectrometry following some form of biochemical enrichment.
22661428	5	39	theme	mass	904:907	arg1	spectra					909:915	tandem mass spectra	897:915	tandem mass spectra	897:915	To this end, we conceived a straightforward O-GlcNAc identification strategy based on our recently developed Oscore software that automatically analyzes tandem mass spectra for the presence and intensity of O-GlcNAc diagnostic fragment ions.
22661428	5	40	theme	Oscore	853:858	arg1	software					860:867	our recently developed Oscore software	830:867	our recently developed Oscore software that automatically analyzes tandem mass spectra for the presence and intensity of O-GlcNAc diagnostic fragment ions	830:983	To this end, we conceived a straightforward O-GlcNAc identification strategy based on our recently developed Oscore software that automatically analyzes tandem mass spectra for the presence and intensity of O-GlcNAc diagnostic fragment ions.
22661428	5	41	theme	tandem	897:902	arg1	spectra					909:915	tandem mass spectra	897:915	tandem mass spectra	897:915	To this end, we conceived a straightforward O-GlcNAc identification strategy based on our recently developed Oscore software that automatically analyzes tandem mass spectra for the presence and intensity of O-GlcNAc diagnostic fragment ions.
22661428	2	42	theme	dynamic	413:419	arg1	interplay					445:453	a site-specific, dynamic and possibly functional interplay	396:453	a site-specific, dynamic and possibly functional interplay with phosphorylation	396:474	It is further presumed that O-GlcNAc can exhibit a site-specific, dynamic and possibly functional interplay with phosphorylation.
22661428	0	43	theme	proteome	65:72	arg1	data					74:77	published large-scale proteome data	43:77	published large-scale proteome data	43:77	Discovery of O-GlcNAc-modified proteins in published large-scale proteome data.
22661428	8	44	theme	O-GlcNAc	1510:1517	arg1	modification					1519:1530	the O-GlcNAc modification	1506:1530	the O-GlcNAc modification	1506:1530	However, a comparison of O-GlcNAc and phospho-identifications from the very same data indicates that the O-GlcNAc modification is considerably less abundant than phosphorylation.
22661428	8	44	theme	O-GlcNAc	1510:1517	arg1	abundant					1553:1560	abundant	1553:1560	abundant	1553:1560	However, a comparison of O-GlcNAc and phospho-identifications from the very same data indicates that the O-GlcNAc modification is considerably less abundant than phosphorylation.
22661428	2	45	with	interplay	445:453	arg1	phosphorylation					460:474	phosphorylation	460:474	phosphorylation	460:474	It is further presumed that O-GlcNAc can exhibit a site-specific, dynamic and possibly functional interplay with phosphorylation.
22661428	3	46	theme	tandem	522:527	arg1	spectrometry					534:545	tandem mass spectrometry	522:545	tandem mass spectrometry following some form of biochemical enrichment	522:591	O-GlcNAc proteins are commonly identified by tandem mass spectrometry following some form of biochemical enrichment.
22661428	0	47	theme	large-scale	53:63	arg1	data					74:77	published large-scale proteome data	43:77	published large-scale proteome data	43:77	Discovery of O-GlcNAc-modified proteins in published large-scale proteome data.
22661428	9	48	theme	phosphate	1683:1691	arg1	moieties					1693:1700	multiple O-GlcNAc or phosphate moieties	1662:1700	moieties	1693:1700	The discovery of numerous doubly modified peptides (i.e. peptides with one or multiple O-GlcNAc or phosphate moieties), suggests that O-GlcNAc and phosphorylation are not necessarily mutually exclusive, but can occur simultaneously at adjacent sites.
22661428	3	49	theme	mass	529:532	arg1	spectrometry					534:545	tandem mass spectrometry	522:545	tandem mass spectrometry following some form of biochemical enrichment	522:591	O-GlcNAc proteins are commonly identified by tandem mass spectrometry following some form of biochemical enrichment.
22661428	7	50	theme	known	1194:1198	arg1	proteins					1209:1216	known O-GlcNAc proteins	1194:1216	known O-GlcNAc proteins	1194:1216	Merely re-searching this data extended the number of known O-GlcNAc proteins by almost 100 suggesting that this modification exists even more widely than previously anticipated and the modification is often sufficiently abundant to be detected without enrichment.
22661428	5	51	theme	diagnostic	960:969	arg1	ions					980:983	O-GlcNAc diagnostic fragment ions	951:983	O-GlcNAc diagnostic fragment ions	951:983	To this end, we conceived a straightforward O-GlcNAc identification strategy based on our recently developed Oscore software that automatically analyzes tandem mass spectra for the presence and intensity of O-GlcNAc diagnostic fragment ions.
22661428	8	52	theme	same	1481:1484	arg1	data					1486:1489	the very same data	1472:1489	the very same data	1472:1489	However, a comparison of O-GlcNAc and phospho-identifications from the very same data indicates that the O-GlcNAc modification is considerably less abundant than phosphorylation.
22661428	5	53	theme	fragment	971:978	arg1	ions					980:983	O-GlcNAc diagnostic fragment ions	951:983	O-GlcNAc diagnostic fragment ions	951:983	To this end, we conceived a straightforward O-GlcNAc identification strategy based on our recently developed Oscore software that automatically analyzes tandem mass spectra for the presence and intensity of O-GlcNAc diagnostic fragment ions.
22661428	8	54	theme	O-GlcNAc	1430:1437	arg1	comparison					1416:1425	a comparison	1414:1425	a comparison of O-GlcNAc and phospho-identifications from the very same data	1414:1489	However, a comparison of O-GlcNAc and phospho-identifications from the very same data indicates that the O-GlcNAc modification is considerably less abundant than phosphorylation.
22661428	1	55	theme	emerging	239:246	arg1	roles					248:252	emerging roles	239:252	emerging roles in numerous cellular processes, such as signal transduction, transcription, and translation	239:344	The attachment of N-acetylglucosamine to serine or threonine residues (O-GlcNAc) is a post-translational modification on nuclear and cytoplasmic proteins with emerging roles in numerous cellular processes, such as signal transduction, transcription, and translation.
22661428	1	56	from	roles	248:252	arg1	transduction					301:312	signal transduction	294:312	signal transduction	294:312	The attachment of N-acetylglucosamine to serine or threonine residues (O-GlcNAc) is a post-translational modification on nuclear and cytoplasmic proteins with emerging roles in numerous cellular processes, such as signal transduction, transcription, and translation.
22661428	1	56	from	roles	248:252	arg1	processes					275:283	numerous cellular processes	257:283	numerous cellular processes	257:283	The attachment of N-acetylglucosamine to serine or threonine residues (O-GlcNAc) is a post-translational modification on nuclear and cytoplasmic proteins with emerging roles in numerous cellular processes, such as signal transduction, transcription, and translation.
22661428	1	56	from	roles	248:252	arg1	transcription					315:327	transcription	315:327	transcription	315:327	The attachment of N-acetylglucosamine to serine or threonine residues (O-GlcNAc) is a post-translational modification on nuclear and cytoplasmic proteins with emerging roles in numerous cellular processes, such as signal transduction, transcription, and translation.
22661428	1	56	from	roles	248:252	arg1	translation					334:344	translation	334:344	translation	334:344	The attachment of N-acetylglucosamine to serine or threonine residues (O-GlcNAc) is a post-translational modification on nuclear and cytoplasmic proteins with emerging roles in numerous cellular processes, such as signal transduction, transcription, and translation.
22661428	9	57	theme	modified	1617:1624	arg1	peptides					1626:1633	numerous doubly modified peptides	1601:1633	numerous doubly modified peptides (i.e. peptides with one or multiple O-GlcNAc or phosphate moieties)	1601:1701	The discovery of numerous doubly modified peptides (i.e. peptides with one or multiple O-GlcNAc or phosphate moieties), suggests that O-GlcNAc and phosphorylation are not necessarily mutually exclusive, but can occur simultaneously at adjacent sites.
22661428	5	58	theme	ions	980:983	arg1	intensity					938:946	intensity	938:946	intensity	938:946	To this end, we conceived a straightforward O-GlcNAc identification strategy based on our recently developed Oscore software that automatically analyzes tandem mass spectra for the presence and intensity of O-GlcNAc diagnostic fragment ions.
22661428	5	58	theme	ions	980:983	arg1	presence					925:932	presence	925:932	presence	925:932	To this end, we conceived a straightforward O-GlcNAc identification strategy based on our recently developed Oscore software that automatically analyzes tandem mass spectra for the presence and intensity of O-GlcNAc diagnostic fragment ions.
22661428	4	59	theme	O-GlcNAc-modified	653:669	arg1	extent					645:650	extent	645:650	extent	645:650	In the present study, we assessed if, and to which extent, O-GlcNAc-modified proteins can be discovered from existing large-scale proteome data sets.
22661428	4	59	theme	O-GlcNAc-modified	653:669	arg1	proteins					671:678	O-GlcNAc-modified proteins	653:678	O-GlcNAc-modified proteins	653:678	In the present study, we assessed if, and to which extent, O-GlcNAc-modified proteins can be discovered from existing large-scale proteome data sets.
22661428	9	60	with	peptides	1641:1648	arg1	one					1655:1657	one	1655:1657	one	1655:1657	The discovery of numerous doubly modified peptides (i.e. peptides with one or multiple O-GlcNAc or phosphate moieties), suggests that O-GlcNAc and phosphorylation are not necessarily mutually exclusive, but can occur simultaneously at adjacent sites.
22661428	9	60	with	peptides	1641:1648	arg1	O-GlcNAc					1671:1678	multiple O-GlcNAc or phosphate moieties	1662:1700	O-GlcNAc	1671:1678	The discovery of numerous doubly modified peptides (i.e. peptides with one or multiple O-GlcNAc or phosphate moieties), suggests that O-GlcNAc and phosphorylation are not necessarily mutually exclusive, but can occur simultaneously at adjacent sites.
22661428	4	61	theme	large-scale	712:722	arg1	sets					738:741	large-scale proteome data sets	712:741	large-scale proteome data sets	712:741	In the present study, we assessed if, and to which extent, O-GlcNAc-modified proteins can be discovered from existing large-scale proteome data sets.
22661428	5	62	theme	straightforward	772:786	arg1	strategy					812:819	a straightforward O-GlcNAc identification strategy	770:819	a straightforward O-GlcNAc identification strategy based on our recently developed Oscore software that automatically analyzes tandem mass spectra for the presence and intensity of O-GlcNAc diagnostic fragment ions	770:983	To this end, we conceived a straightforward O-GlcNAc identification strategy based on our recently developed Oscore software that automatically analyzes tandem mass spectra for the presence and intensity of O-GlcNAc diagnostic fragment ions.
22661428	7	63	theme	O-GlcNAc	1200:1207	arg1	proteins					1209:1216	known O-GlcNAc proteins	1194:1216	known O-GlcNAc proteins	1194:1216	Merely re-searching this data extended the number of known O-GlcNAc proteins by almost 100 suggesting that this modification exists even more widely than previously anticipated and the modification is often sufficiently abundant to be detected without enrichment.
22661428	1	64	dep	serine	121:126	arg1	residues					141:148	residues	141:148	residues	141:148	The attachment of N-acetylglucosamine to serine or threonine residues (O-GlcNAc) is a post-translational modification on nuclear and cytoplasmic proteins with emerging roles in numerous cellular processes, such as signal transduction, transcription, and translation.
22661428	1	65	theme	numerous	257:264	arg1	transduction					301:312	signal transduction	294:312	signal transduction	294:312	The attachment of N-acetylglucosamine to serine or threonine residues (O-GlcNAc) is a post-translational modification on nuclear and cytoplasmic proteins with emerging roles in numerous cellular processes, such as signal transduction, transcription, and translation.
22661428	1	65	theme	numerous	257:264	arg1	processes					275:283	numerous cellular processes	257:283	numerous cellular processes	257:283	The attachment of N-acetylglucosamine to serine or threonine residues (O-GlcNAc) is a post-translational modification on nuclear and cytoplasmic proteins with emerging roles in numerous cellular processes, such as signal transduction, transcription, and translation.
22661428	1	65	theme	numerous	257:264	arg1	transcription					315:327	transcription	315:327	transcription	315:327	The attachment of N-acetylglucosamine to serine or threonine residues (O-GlcNAc) is a post-translational modification on nuclear and cytoplasmic proteins with emerging roles in numerous cellular processes, such as signal transduction, transcription, and translation.
22661428	1	65	theme	numerous	257:264	arg1	translation					334:344	translation	334:344	translation	334:344	The attachment of N-acetylglucosamine to serine or threonine residues (O-GlcNAc) is a post-translational modification on nuclear and cytoplasmic proteins with emerging roles in numerous cellular processes, such as signal transduction, transcription, and translation.
16964247	4	0	dep	O-GlcNAc	664:671	arg1	modifications					689:701	modifications	689:701	modifications	689:701	Our results indicate that the dynamic interplay between O-GlcNAc and O-phosphate modifications coordinately regulate p53 stability and activity.
16964247	2	1	theme	decreased	362:370	arg1	phosphorylation					372:386	decreased phosphorylation	362:386	decreased phosphorylation of p53 at Thr 155, which is a site that is targeted by the COP9 signalosome, resulting in decreased p53 ubiquitination	362:505	Here, we show that Ser 149 of p53 is O-GlcNAcylated and that this modification is associated with decreased phosphorylation of p53 at Thr 155, which is a site that is targeted by the COP9 signalosome, resulting in decreased p53 ubiquitination.
16964247	2	2	theme	COP9	447:450	arg1	signalosome					452:462	the COP9 signalosome	443:462	the COP9 signalosome	443:462	Here, we show that Ser 149 of p53 is O-GlcNAcylated and that this modification is associated with decreased phosphorylation of p53 at Thr 155, which is a site that is targeted by the COP9 signalosome, resulting in decreased p53 ubiquitination.
16964247	1	3	theme	Post-translational	92:109	arg1	addition					111:118	Post-translational addition	92:118	Post-translational addition of O-linked N-acetylglucosamine (O-GlcNAc) to p53	92:168	Post-translational addition of O-linked N-acetylglucosamine (O-GlcNAc) to p53 is known to occur, but the site of O-GlcNAcylation and its effects on p53 are not understood.
16964247	4	4	theme	dynamic	638:644	arg1	interplay					646:654	the dynamic interplay	634:654	the dynamic interplay between O-GlcNAc and O-phosphate modifications	634:701	Our results indicate that the dynamic interplay between O-GlcNAc and O-phosphate modifications coordinately regulate p53 stability and activity.
16964247	4	5	theme	p53	725:727	arg1	stability					729:737	p53 stability	725:737	p53 stability	725:737	Our results indicate that the dynamic interplay between O-GlcNAc and O-phosphate modifications coordinately regulate p53 stability and activity.
16964247	0	6	link	O-linked	25:32	arg1	N-acetylglucosamine					34:52	O-linked N-acetylglucosamine	25:52	O-linked N-acetylglucosamine	25:52	Modification of p53 with O-linked N-acetylglucosamine regulates p53 activity and stability.
16964247	3	7	from	Ser	540:542	arg1	O-GlcNAcylation					521:535	O-GlcNAcylation	521:535	O-GlcNAcylation at Ser 149	521:546	Accordingly, O-GlcNAcylation at Ser 149 stabilizes p53 by blocking ubiquitin-dependent proteolysis.
16964247	2	8	theme	Thr	398:400	arg1	site					418:421	a site	416:421	a site that is targeted by the COP9 signalosome, resulting in decreased p53 ubiquitination	416:505	Here, we show that Ser 149 of p53 is O-GlcNAcylated and that this modification is associated with decreased phosphorylation of p53 at Thr 155, which is a site that is targeted by the COP9 signalosome, resulting in decreased p53 ubiquitination.
16964247	2	8	theme	Thr	398:400	arg1	155					402:404	Thr 155	398:404	Thr 155	398:404	Here, we show that Ser 149 of p53 is O-GlcNAcylated and that this modification is associated with decreased phosphorylation of p53 at Thr 155, which is a site that is targeted by the COP9 signalosome, resulting in decreased p53 ubiquitination.
16964247	2	9	theme	p53	488:490	arg1	ubiquitination					492:505	decreased p53 ubiquitination	478:505	decreased p53 ubiquitination	478:505	Here, we show that Ser 149 of p53 is O-GlcNAcylated and that this modification is associated with decreased phosphorylation of p53 at Thr 155, which is a site that is targeted by the COP9 signalosome, resulting in decreased p53 ubiquitination.
16964247	1	10	theme	O-linked	123:130	arg1	O-GlcNAc					153:160	O-GlcNAc	153:160	O-GlcNAc	153:160	Post-translational addition of O-linked N-acetylglucosamine (O-GlcNAc) to p53 is known to occur, but the site of O-GlcNAcylation and its effects on p53 are not understood.
16964247	1	10	theme	O-linked	123:130	arg1	N-acetylglucosamine					132:150	O-linked N-acetylglucosamine	123:150	O-linked N-acetylglucosamine (O-GlcNAc)	123:161	Post-translational addition of O-linked N-acetylglucosamine (O-GlcNAc) to p53 is known to occur, but the site of O-GlcNAcylation and its effects on p53 are not understood.
16964247	2	11	theme	p53	391:393	arg1	phosphorylation					372:386	decreased phosphorylation	362:386	decreased phosphorylation of p53 at Thr 155, which is a site that is targeted by the COP9 signalosome, resulting in decreased p53 ubiquitination	362:505	Here, we show that Ser 149 of p53 is O-GlcNAcylated and that this modification is associated with decreased phosphorylation of p53 at Thr 155, which is a site that is targeted by the COP9 signalosome, resulting in decreased p53 ubiquitination.
16964247	2	12	theme	decreased	478:486	arg1	ubiquitination					492:505	decreased p53 ubiquitination	478:505	decreased p53 ubiquitination	478:505	Here, we show that Ser 149 of p53 is O-GlcNAcylated and that this modification is associated with decreased phosphorylation of p53 at Thr 155, which is a site that is targeted by the COP9 signalosome, resulting in decreased p53 ubiquitination.
16964247	0	13	theme	O-linked	25:32	arg1	N-acetylglucosamine					34:52	O-linked N-acetylglucosamine	25:52	O-linked N-acetylglucosamine	25:52	Modification of p53 with O-linked N-acetylglucosamine regulates p53 activity and stability.
16964247	1	14	theme	O-GlcNAcylation	205:219	arg1	effects					229:235	its effects	225:235	its effects on p53	225:242	Post-translational addition of O-linked N-acetylglucosamine (O-GlcNAc) to p53 is known to occur, but the site of O-GlcNAcylation and its effects on p53 are not understood.
16964247	1	14	theme	O-GlcNAcylation	205:219	arg1	site					197:200	the site	193:200	the site of O-GlcNAcylation	193:219	Post-translational addition of O-linked N-acetylglucosamine (O-GlcNAc) to p53 is known to occur, but the site of O-GlcNAcylation and its effects on p53 are not understood.
16964247	1	14	theme	O-GlcNAcylation	205:219	arg1	O-GlcNAcylation					205:219	O-GlcNAcylation	205:219	O-GlcNAcylation	205:219	Post-translational addition of O-linked N-acetylglucosamine (O-GlcNAc) to p53 is known to occur, but the site of O-GlcNAcylation and its effects on p53 are not understood.
16964247	0	15	theme	p53	64:66	arg1	activity					68:75	p53 activity	64:75	p53 activity	64:75	Modification of p53 with O-linked N-acetylglucosamine regulates p53 activity and stability.
16964247	1	16	from	effects	229:235	arg1	p53					240:242	p53	240:242	p53	240:242	Post-translational addition of O-linked N-acetylglucosamine (O-GlcNAc) to p53 is known to occur, but the site of O-GlcNAcylation and its effects on p53 are not understood.
16964247	1	17	theme	N-acetylglucosamine	132:150	arg1	addition					111:118	Post-translational addition	92:118	Post-translational addition of O-linked N-acetylglucosamine (O-GlcNAc) to p53	92:168	Post-translational addition of O-linked N-acetylglucosamine (O-GlcNAc) to p53 is known to occur, but the site of O-GlcNAcylation and its effects on p53 are not understood.
16964247	0	18	with	Modification	0:11	arg1	N-acetylglucosamine					34:52	O-linked N-acetylglucosamine	25:52	O-linked N-acetylglucosamine	25:52	Modification of p53 with O-linked N-acetylglucosamine regulates p53 activity and stability.
16964247	2	19	theme	p53	294:296	arg1	Ser					283:285	Ser 149	283:289	Ser 149 of p53	283:296	Here, we show that Ser 149 of p53 is O-GlcNAcylated and that this modification is associated with decreased phosphorylation of p53 at Thr 155, which is a site that is targeted by the COP9 signalosome, resulting in decreased p53 ubiquitination.
16964247	1	20	from	site	197:200	arg1	p53					240:242	p53	240:242	p53	240:242	Post-translational addition of O-linked N-acetylglucosamine (O-GlcNAc) to p53 is known to occur, but the site of O-GlcNAcylation and its effects on p53 are not understood.
16964247	3	21	theme	ubiquitin-dependent	575:593	arg1	proteolysis					595:605	ubiquitin-dependent proteolysis	575:605	ubiquitin-dependent proteolysis	575:605	Accordingly, O-GlcNAcylation at Ser 149 stabilizes p53 by blocking ubiquitin-dependent proteolysis.
16964247	1	22	link	O-linked	123:130	arg1	O-GlcNAc					153:160	O-GlcNAc	153:160	O-GlcNAc	153:160	Post-translational addition of O-linked N-acetylglucosamine (O-GlcNAc) to p53 is known to occur, but the site of O-GlcNAcylation and its effects on p53 are not understood.
16964247	1	22	link	O-linked	123:130	arg1	N-acetylglucosamine					132:150	O-linked N-acetylglucosamine	123:150	O-linked N-acetylglucosamine (O-GlcNAc)	123:161	Post-translational addition of O-linked N-acetylglucosamine (O-GlcNAc) to p53 is known to occur, but the site of O-GlcNAcylation and its effects on p53 are not understood.
16964247	2	23	from	155	402:404	arg1	phosphorylation					372:386	decreased phosphorylation	362:386	decreased phosphorylation of p53 at Thr 155, which is a site that is targeted by the COP9 signalosome, resulting in decreased p53 ubiquitination	362:505	Here, we show that Ser 149 of p53 is O-GlcNAcylated and that this modification is associated with decreased phosphorylation of p53 at Thr 155, which is a site that is targeted by the COP9 signalosome, resulting in decreased p53 ubiquitination.
16964247	0	24	theme	p53	16:18	arg1	Modification					0:11	Modification	0:11	Modification of p53 with O-linked N-acetylglucosamine	0:52	Modification of p53 with O-linked N-acetylglucosamine regulates p53 activity and stability.
34417460	6	0	theme	glucose	944:950	arg1	levels					952:957	glucose levels	944:957	glucose levels	944:957	Glucagon, adrenaline and glucocorticoids augment protein levels of p53, and administration of these hormones to p53 deficient human hepatocytes and to liver-specific p53 deficient mice fails to increase glucose levels.
34417460	9	1	theme	in	1345:1346	arg1	homeostasis					1361:1371	in vivo glucose homeostasis	1345:1371	in vivo glucose homeostasis	1345:1371	Overall these results indicate that the O-GlcNAcylation of p53 plays an unsuspected key role regulating in vivo glucose homeostasis.
34417460	0	2	from	p53	15:17	arg1	liver					26:30	the liver	22:30	the liver	22:30	O-GlcNAcylated p53 in the liver modulates hepatic glucose production.
34417460	6	3	theme	hormones	841:848	arg1	administration					817:830	administration	817:830	administration of these hormones to p53 deficient human hepatocytes and to liver-specific p53 deficient mice	817:924	Glucagon, adrenaline and glucocorticoids augment protein levels of p53, and administration of these hormones to p53 deficient human hepatocytes and to liver-specific p53 deficient mice fails to increase glucose levels.
34417460	4	4	theme	transcriptional	569:583	arg1	activation					585:594	its transcriptional activation	565:594	its transcriptional activation	565:594	More specifically, p53 binds to PCK1 promoter and regulates its transcriptional activation, thereby controlling hepatic glucose production.
34417460	9	5	theme	unsuspected	1313:1323	arg1	role					1329:1332	an unsuspected key role	1310:1332	an unsuspected key role regulating in vivo glucose homeostasis	1310:1371	Overall these results indicate that the O-GlcNAcylation of p53 plays an unsuspected key role regulating in vivo glucose homeostasis.
34417460	8	6	theme	type	1165:1168	arg1	patients					1181:1188	type 2 diabetic patients	1165:1188	type 2 diabetic patients	1165:1188	Finally, protein levels of p53, as well as genes responsible of O-GlcNAcylation are elevated in the liver of type 2 diabetic patients and positively correlate with glucose and HOMA-IR.
34417460	9	7	theme	key	1325:1327	arg1	role					1329:1332	an unsuspected key role	1310:1332	an unsuspected key role regulating in vivo glucose homeostasis	1310:1371	Overall these results indicate that the O-GlcNAcylation of p53 plays an unsuspected key role regulating in vivo glucose homeostasis.
34417460	8	8	theme	protein	1065:1071	arg1	levels					1073:1078	protein levels	1065:1078	protein levels of p53, as well as genes responsible of O-GlcNAcylation	1065:1134	Finally, protein levels of p53, as well as genes responsible of O-GlcNAcylation are elevated in the liver of type 2 diabetic patients and positively correlate with glucose and HOMA-IR.
34417460	8	9	theme	patients	1181:1188	arg1	liver					1156:1160	the liver	1152:1160	the liver of type 2 diabetic patients	1152:1188	Finally, protein levels of p53, as well as genes responsible of O-GlcNAcylation are elevated in the liver of type 2 diabetic patients and positively correlate with glucose and HOMA-IR.
34417460	8	10	theme	p53	1083:1085	arg1	levels					1073:1078	protein levels	1065:1078	protein levels of p53, as well as genes responsible of O-GlcNAcylation	1065:1134	Finally, protein levels of p53, as well as genes responsible of O-GlcNAcylation are elevated in the liver of type 2 diabetic patients and positively correlate with glucose and HOMA-IR.
34417460	7	11	theme	p53	988:990	arg1	levels					992:997	p53 levels	988:997	p53 levels	988:997	Moreover, insulin decreases p53 levels, and over-expression of p53 impairs insulin sensitivity.
34417460	8	12	theme	diabetic	1172:1179	arg1	patients					1181:1188	type 2 diabetic patients	1165:1188	type 2 diabetic patients	1165:1188	Finally, protein levels of p53, as well as genes responsible of O-GlcNAcylation are elevated in the liver of type 2 diabetic patients and positively correlate with glucose and HOMA-IR.
34417460	6	13	theme	deficient	911:919	arg1	mice					921:924	liver-specific p53 deficient mice	892:924	liver-specific p53 deficient mice	892:924	Glucagon, adrenaline and glucocorticoids augment protein levels of p53, and administration of these hormones to p53 deficient human hepatocytes and to liver-specific p53 deficient mice fails to increase glucose levels.
34417460	1	14	theme	cellular	176:183	arg1	response					185:192	the cellular response	172:192	the cellular response to stress	172:202	p53 regulates several signaling pathways to maintain the metabolic homeostasis of cells and modulates the cellular response to stress.
34417460	3	15	theme	hepatic	376:382	arg1	p53					384:386	hepatic p53	376:386	hepatic p53	376:386	We show here that upon starvation hepatic p53 is stabilized by O-GlcNAcylation and plays an essential role in the physiological regulation of glucose homeostasis.
34417460	6	16	theme	p53	907:909	arg1	mice					921:924	liver-specific p53 deficient mice	892:924	liver-specific p53 deficient mice	892:924	Glucagon, adrenaline and glucocorticoids augment protein levels of p53, and administration of these hormones to p53 deficient human hepatocytes and to liver-specific p53 deficient mice fails to increase glucose levels.
34417460	1	17	theme	several	84:90	arg1	pathways					102:109	several signaling pathways	84:109	several signaling pathways to maintain the metabolic homeostasis of cells	84:156	p53 regulates several signaling pathways to maintain the metabolic homeostasis of cells and modulates the cellular response to stress.
34417460	0	18	theme	O-GlcNAcylated	0:13	arg1	p53					15:17	O-GlcNAcylated p53	0:17	O-GlcNAcylated p53 in the liver	0:30	O-GlcNAcylated p53 in the liver modulates hepatic glucose production.
34417460	6	19	theme	p53	808:810	arg1	levels					798:803	protein levels	790:803	protein levels of p53	790:810	Glucagon, adrenaline and glucocorticoids augment protein levels of p53, and administration of these hormones to p53 deficient human hepatocytes and to liver-specific p53 deficient mice fails to increase glucose levels.
34417460	1	20	theme	signaling	92:100	arg1	pathways					102:109	several signaling pathways	84:109	several signaling pathways to maintain the metabolic homeostasis of cells	84:156	p53 regulates several signaling pathways to maintain the metabolic homeostasis of cells and modulates the cellular response to stress.
34417460	2	21	attach	linked	311:316	arg1	maintenance					329:339	glucose maintenance	321:339	glucose maintenance	321:339	Deficiency or excess of nutrients causes cellular metabolic stress, and we hypothesized that p53 could be linked to glucose maintenance.
34417460	2	21	attach	linked	311:316	arg2	p53					298:300	p53	298:300	p53	298:300	Deficiency or excess of nutrients causes cellular metabolic stress, and we hypothesized that p53 could be linked to glucose maintenance.
34417460	5	22	theme	calorie	720:726	arg1	restriction					728:738	calorie restriction	720:738	calorie restriction	720:738	Mice lacking p53 in the liver show a reduced gluconeogenic response during calorie restriction.
34417460	6	23	theme	liver-specific	892:905	arg1	mice					921:924	liver-specific p53 deficient mice	892:924	liver-specific p53 deficient mice	892:924	Glucagon, adrenaline and glucocorticoids augment protein levels of p53, and administration of these hormones to p53 deficient human hepatocytes and to liver-specific p53 deficient mice fails to increase glucose levels.
34417460	3	24	theme	physiological	456:468	arg1	regulation					470:479	the physiological regulation	452:479	the physiological regulation of glucose homeostasis	452:502	We show here that upon starvation hepatic p53 is stabilized by O-GlcNAcylation and plays an essential role in the physiological regulation of glucose homeostasis.
34417460	8	25	theme	responsible	1105:1115	arg1	genes					1099:1103	genes	1099:1103	genes responsible of O-GlcNAcylation	1099:1134	Finally, protein levels of p53, as well as genes responsible of O-GlcNAcylation are elevated in the liver of type 2 diabetic patients and positively correlate with glucose and HOMA-IR.
34417460	8	26	theme	genes	1099:1103	arg1	levels					1073:1078	protein levels	1065:1078	protein levels of p53, as well as genes responsible of O-GlcNAcylation	1065:1134	Finally, protein levels of p53, as well as genes responsible of O-GlcNAcylation are elevated in the liver of type 2 diabetic patients and positively correlate with glucose and HOMA-IR.
34417460	2	27	theme	nutrients	229:237	arg1	excess					219:224	excess	219:224	excess	219:224	Deficiency or excess of nutrients causes cellular metabolic stress, and we hypothesized that p53 could be linked to glucose maintenance.
34417460	2	27	theme	nutrients	229:237	arg1	Deficiency					205:214	Deficiency	205:214	Deficiency	205:214	Deficiency or excess of nutrients causes cellular metabolic stress, and we hypothesized that p53 could be linked to glucose maintenance.
34417460	0	28	theme	glucose	50:56	arg1	production					58:67	hepatic glucose production	42:67	hepatic glucose production	42:67	O-GlcNAcylated p53 in the liver modulates hepatic glucose production.
34417460	9	29	dep	in	1345:1346	arg1	vivo					1348:1351	vivo	1348:1351	vivo	1348:1351	Overall these results indicate that the O-GlcNAcylation of p53 plays an unsuspected key role regulating in vivo glucose homeostasis.
34417460	8	30	theme	O-GlcNAcylation	1120:1134	arg1	responsible					1105:1115	responsible	1105:1115	responsible	1105:1115	Finally, protein levels of p53, as well as genes responsible of O-GlcNAcylation are elevated in the liver of type 2 diabetic patients and positively correlate with glucose and HOMA-IR.
34417460	9	31	theme	glucose	1353:1359	arg1	homeostasis					1361:1371	in vivo glucose homeostasis	1345:1371	in vivo glucose homeostasis	1345:1371	Overall these results indicate that the O-GlcNAcylation of p53 plays an unsuspected key role regulating in vivo glucose homeostasis.
34417460	6	32	theme	protein	790:796	arg1	levels					798:803	protein levels	790:803	protein levels of p53	790:810	Glucagon, adrenaline and glucocorticoids augment protein levels of p53, and administration of these hormones to p53 deficient human hepatocytes and to liver-specific p53 deficient mice fails to increase glucose levels.
34417460	3	33	theme	glucose	484:490	arg1	homeostasis					492:502	glucose homeostasis	484:502	glucose homeostasis	484:502	We show here that upon starvation hepatic p53 is stabilized by O-GlcNAcylation and plays an essential role in the physiological regulation of glucose homeostasis.
34417460	0	34	theme	hepatic	42:48	arg1	production					58:67	hepatic glucose production	42:67	hepatic glucose production	42:67	O-GlcNAcylated p53 in the liver modulates hepatic glucose production.
34417460	4	35	theme	PCK1	537:540	arg1	promoter					542:549	PCK1 promoter	537:549	PCK1 promoter	537:549	More specifically, p53 binds to PCK1 promoter and regulates its transcriptional activation, thereby controlling hepatic glucose production.
34417460	5	36	theme	reduced	682:688	arg1	response					704:711	a reduced gluconeogenic response	680:711	a reduced gluconeogenic response	680:711	Mice lacking p53 in the liver show a reduced gluconeogenic response during calorie restriction.
34417460	6	37	theme	human	867:871	arg1	hepatocytes					873:883	p53 deficient human hepatocytes	853:883	p53 deficient human hepatocytes	853:883	Glucagon, adrenaline and glucocorticoids augment protein levels of p53, and administration of these hormones to p53 deficient human hepatocytes and to liver-specific p53 deficient mice fails to increase glucose levels.
34417460	3	38	theme	homeostasis	492:502	arg1	regulation					470:479	the physiological regulation	452:479	the physiological regulation of glucose homeostasis	452:502	We show here that upon starvation hepatic p53 is stabilized by O-GlcNAcylation and plays an essential role in the physiological regulation of glucose homeostasis.
34417460	5	39	theme	gluconeogenic	690:702	arg1	response					704:711	a reduced gluconeogenic response	680:711	a reduced gluconeogenic response	680:711	Mice lacking p53 in the liver show a reduced gluconeogenic response during calorie restriction.
34417460	6	40	theme	deficient	857:865	arg1	hepatocytes					873:883	p53 deficient human hepatocytes	853:883	p53 deficient human hepatocytes	853:883	Glucagon, adrenaline and glucocorticoids augment protein levels of p53, and administration of these hormones to p53 deficient human hepatocytes and to liver-specific p53 deficient mice fails to increase glucose levels.
34417460	7	41	theme	insulin	1035:1041	arg1	sensitivity					1043:1053	insulin sensitivity	1035:1053	insulin sensitivity	1035:1053	Moreover, insulin decreases p53 levels, and over-expression of p53 impairs insulin sensitivity.
34417460	1	42	theme	metabolic	127:135	arg1	homeostasis					137:147	the metabolic homeostasis	123:147	the metabolic homeostasis of cells	123:156	p53 regulates several signaling pathways to maintain the metabolic homeostasis of cells and modulates the cellular response to stress.
34417460	4	43	theme	hepatic	617:623	arg1	production					633:642	hepatic glucose production	617:642	hepatic glucose production	617:642	More specifically, p53 binds to PCK1 promoter and regulates its transcriptional activation, thereby controlling hepatic glucose production.
34417460	2	44	theme	glucose	321:327	arg1	maintenance					329:339	glucose maintenance	321:339	glucose maintenance	321:339	Deficiency or excess of nutrients causes cellular metabolic stress, and we hypothesized that p53 could be linked to glucose maintenance.
34417460	2	45	theme	metabolic	255:263	arg1	stress					265:270	cellular metabolic stress	246:270	cellular metabolic stress	246:270	Deficiency or excess of nutrients causes cellular metabolic stress, and we hypothesized that p53 could be linked to glucose maintenance.
34417460	7	46	theme	p53	1023:1025	arg1	over-expression					1004:1018	over-expression	1004:1018	over-expression of p53	1004:1025	Moreover, insulin decreases p53 levels, and over-expression of p53 impairs insulin sensitivity.
34417460	1	47	dep	pathways	102:109	arg1	maintain					114:121	maintain	114:121	to maintain the metabolic homeostasis of cells	111:156	p53 regulates several signaling pathways to maintain the metabolic homeostasis of cells and modulates the cellular response to stress.
34417460	3	48	theme	essential	434:442	arg1	role					444:447	an essential role	431:447	an essential role	431:447	We show here that upon starvation hepatic p53 is stabilized by O-GlcNAcylation and plays an essential role in the physiological regulation of glucose homeostasis.
34417460	9	49	theme	p53	1300:1302	arg1	O-GlcNAcylation					1281:1295	the O-GlcNAcylation	1277:1295	the O-GlcNAcylation of p53	1277:1302	Overall these results indicate that the O-GlcNAcylation of p53 plays an unsuspected key role regulating in vivo glucose homeostasis.
34417460	2	50	theme	cellular	246:253	arg1	stress					265:270	cellular metabolic stress	246:270	cellular metabolic stress	246:270	Deficiency or excess of nutrients causes cellular metabolic stress, and we hypothesized that p53 could be linked to glucose maintenance.
34417460	1	51	theme	cells	152:156	arg1	homeostasis					137:147	the metabolic homeostasis	123:147	the metabolic homeostasis of cells	123:156	p53 regulates several signaling pathways to maintain the metabolic homeostasis of cells and modulates the cellular response to stress.
34417460	4	52	theme	glucose	625:631	arg1	production					633:642	hepatic glucose production	617:642	hepatic glucose production	617:642	More specifically, p53 binds to PCK1 promoter and regulates its transcriptional activation, thereby controlling hepatic glucose production.
25937070	7	0	theme	O-GlcNAcylation	1139:1153	arg1	level					1130:1134	The level	1126:1134	The level of O-GlcNAcylation of eIF2α	1126:1162	The level of O-GlcNAcylation of eIF2α was changed by dithiothreitol treatment dependent on its phosphorylation at Ser 51.
25937070	11	1	theme	cellular	1730:1737	arg1	homeostasis					1739:1749	cellular homeostasis	1730:1749	cellular homeostasis	1730:1749	In conclusion, proper regulation of O-GlcNAcylation and phosphorylation of eIF2α is important to maintain cellular homeostasis upon ER stress.
25937070	2	2	theme	O-GlcNAcylation	370:384	arg1	level					361:365	the total cellular level	342:365	the total cellular level of O-GlcNAcylation	342:384	For example, glucosamine-induced flux through the hexosamine biosynthetic pathway can promote ER stress and ER stress inducers can change the total cellular level of O-GlcNAcylation.
25937070	4	3	from	Thr	644:646	arg1	O-GlcNAcylated					617:630	O-GlcNAcylated	617:630	O-GlcNAcylated	617:630	In this study, eukaryotic translation initiation factor 2α (eIF2α), a major branch of the UPR, was O-GlcNAcylated at Ser 219, Thr 239, and Thr 241.
25937070	8	4	theme	increased	1377:1385	arg1	apoptosis					1387:1395	increased apoptosis	1377:1395	increased apoptosis upon ER stress	1377:1410	Point mutation of the O-GlcNAcylation sites of eIF2α increased its phosphorylation at Ser 51 and CHOP expression and resulted in increased apoptosis upon ER stress.
25937070	1	5	gly	O-GlcNAcylation	82:96	arg1	response					194:201	the endoplasmic reticulum (ER) stress response	156:201	the endoplasmic reticulum (ER) stress response	156:201	O-GlcNAcylation is highly involved in cellular stress responses including the endoplasmic reticulum (ER) stress response.
25937070	1	5	gly	O-GlcNAcylation	82:96	arg1	responses					136:144	cellular stress responses	120:144	cellular stress responses including the endoplasmic reticulum (ER) stress response	120:201	O-GlcNAcylation is highly involved in cellular stress responses including the endoplasmic reticulum (ER) stress response.
25937070	5	6	theme	specific	821:828	arg1	factor					872:877	activating transcription factor 4	847:879	activating transcription factor 4	847:879	Upon ER stress, eIF2α is phosphorylated at Ser 51 by phosphorylated PKR-like ER kinase and this inhibits global translation initiation, except for that of specific mRNAs, including activating transcription factor 4, that induce stress-responsive genes such as C/EBP homologous protein (CHOP).
25937070	5	6	theme	specific	821:828	arg1	mRNAs					830:834	specific mRNAs	821:834	specific mRNAs	821:834	Upon ER stress, eIF2α is phosphorylated at Ser 51 by phosphorylated PKR-like ER kinase and this inhibits global translation initiation, except for that of specific mRNAs, including activating transcription factor 4, that induce stress-responsive genes such as C/EBP homologous protein (CHOP).
25937070	8	7	theme	Point	1248:1252	arg1	mutation					1254:1261	Point mutation	1248:1261	Point mutation of the O-GlcNAcylation sites of eIF2α	1248:1299	Point mutation of the O-GlcNAcylation sites of eIF2α increased its phosphorylation at Ser 51 and CHOP expression and resulted in increased apoptosis upon ER stress.
25937070	11	8	theme	ER	1756:1757	arg1	stress					1759:1764	ER stress	1756:1764	ER stress	1756:1764	In conclusion, proper regulation of O-GlcNAcylation and phosphorylation of eIF2α is important to maintain cellular homeostasis upon ER stress.
25937070	2	9	theme	ER	312:313	arg1	inducers					322:329	ER stress inducers	312:329	ER stress inducers	312:329	For example, glucosamine-induced flux through the hexosamine biosynthetic pathway can promote ER stress and ER stress inducers can change the total cellular level of O-GlcNAcylation.
25937070	2	10	theme	stress	315:320	arg1	inducers					322:329	ER stress inducers	312:329	ER stress inducers	312:329	For example, glucosamine-induced flux through the hexosamine biosynthetic pathway can promote ER stress and ER stress inducers can change the total cellular level of O-GlcNAcylation.
25937070	8	11	from	Ser	1334:1336	arg1	phosphorylation					1315:1329	its phosphorylation	1311:1329	its phosphorylation at Ser 51	1311:1339	Point mutation of the O-GlcNAcylation sites of eIF2α increased its phosphorylation at Ser 51 and CHOP expression and resulted in increased apoptosis upon ER stress.
25937070	8	11	from	Ser	1334:1336	arg1	expression					1350:1359	CHOP expression	1345:1359	CHOP expression	1345:1359	Point mutation of the O-GlcNAcylation sites of eIF2α increased its phosphorylation at Ser 51 and CHOP expression and resulted in increased apoptosis upon ER stress.
25937070	11	12	theme	eIF2α	1699:1703	arg1	regulation					1646:1655	proper regulation	1639:1655	proper regulation of O-GlcNAcylation	1639:1674	In conclusion, proper regulation of O-GlcNAcylation and phosphorylation of eIF2α is important to maintain cellular homeostasis upon ER stress.
25937070	11	12	theme	eIF2α	1699:1703	arg1	phosphorylation					1680:1694	phosphorylation	1680:1694	phosphorylation of eIF2α	1680:1703	In conclusion, proper regulation of O-GlcNAcylation and phosphorylation of eIF2α is important to maintain cellular homeostasis upon ER stress.
25937070	8	13	theme	O-GlcNAcylation	1270:1284	arg1	eIF2α					1295:1299	eIF2α	1295:1299	eIF2α	1295:1299	Point mutation of the O-GlcNAcylation sites of eIF2α increased its phosphorylation at Ser 51 and CHOP expression and resulted in increased apoptosis upon ER stress.
25937070	8	13	theme	O-GlcNAcylation	1270:1284	arg1	sites					1286:1290	the O-GlcNAcylation sites	1266:1290	the O-GlcNAcylation sites of eIF2α	1266:1299	Point mutation of the O-GlcNAcylation sites of eIF2α increased its phosphorylation at Ser 51 and CHOP expression and resulted in increased apoptosis upon ER stress.
25937070	4	14	from	Ser	635:637	arg1	O-GlcNAcylated					617:630	O-GlcNAcylated	617:630	O-GlcNAcylated	617:630	In this study, eukaryotic translation initiation factor 2α (eIF2α), a major branch of the UPR, was O-GlcNAcylated at Ser 219, Thr 239, and Thr 241.
25937070	6	15	theme	transferase	1048:1058	arg1	overexpression					1066:1079	O-GlcNAc transferase (OGT) overexpression	1039:1079	O-GlcNAc transferase (OGT) overexpression	1039:1079	Hyper-O-GlcNAcylation induced by O-GlcNAcase inhibitor (thiamet-G) treatment or O-GlcNAc transferase (OGT) overexpression hindered phosphorylation of eIF2α at Ser 51.
25937070	5	16	theme	ER	671:672	arg1	stress					674:679	ER stress	671:679	ER stress	671:679	Upon ER stress, eIF2α is phosphorylated at Ser 51 by phosphorylated PKR-like ER kinase and this inhibits global translation initiation, except for that of specific mRNAs, including activating transcription factor 4, that induce stress-responsive genes such as C/EBP homologous protein (CHOP).
25937070	11	17	theme	proper	1639:1644	arg1	regulation					1646:1655	proper regulation	1639:1655	proper regulation of O-GlcNAcylation	1639:1674	In conclusion, proper regulation of O-GlcNAcylation and phosphorylation of eIF2α is important to maintain cellular homeostasis upon ER stress.
25937070	6	18	theme	thiamet-G	1015:1023	arg1	treatment					1026:1034	O-GlcNAcase inhibitor (thiamet-G) treatment	992:1034	O-GlcNAcase inhibitor (thiamet-G) treatment	992:1034	Hyper-O-GlcNAcylation induced by O-GlcNAcase inhibitor (thiamet-G) treatment or O-GlcNAc transferase (OGT) overexpression hindered phosphorylation of eIF2α at Ser 51.
25937070	5	19	theme	stress-responsive	894:910	arg1	protein					943:949	C/EBP homologous protein	926:949	C/EBP homologous protein (CHOP)	926:956	Upon ER stress, eIF2α is phosphorylated at Ser 51 by phosphorylated PKR-like ER kinase and this inhibits global translation initiation, except for that of specific mRNAs, including activating transcription factor 4, that induce stress-responsive genes such as C/EBP homologous protein (CHOP).
25937070	5	19	theme	stress-responsive	894:910	arg1	genes					912:916	stress-responsive genes	894:916	stress-responsive genes such as C/EBP homologous protein (CHOP)	894:956	Upon ER stress, eIF2α is phosphorylated at Ser 51 by phosphorylated PKR-like ER kinase and this inhibits global translation initiation, except for that of specific mRNAs, including activating transcription factor 4, that induce stress-responsive genes such as C/EBP homologous protein (CHOP).
25937070	10	20	theme	mouse	1611:1615	arg1	liver					1617:1621	thiamet-G-injected mouse liver	1592:1621	thiamet-G-injected mouse liver	1592:1621	This O-GlcNAcylation of eIF2α was reproduced in thiamet-G-injected mouse liver.
25937070	5	21	theme	translation	778:788	arg1	initiation					790:799	global translation initiation	771:799	global translation initiation	771:799	Upon ER stress, eIF2α is phosphorylated at Ser 51 by phosphorylated PKR-like ER kinase and this inhibits global translation initiation, except for that of specific mRNAs, including activating transcription factor 4, that induce stress-responsive genes such as C/EBP homologous protein (CHOP).
25937070	10	22	theme	eIF2α	1568:1572	arg1	O-GlcNAcylation					1549:1563	This O-GlcNAcylation	1544:1563	This O-GlcNAcylation of eIF2α	1544:1572	This O-GlcNAcylation of eIF2α was reproduced in thiamet-G-injected mouse liver.
25937070	0	23	theme	phospho-eIF2α-mediated	39:60	arg1	response					72:79	the phospho-eIF2α-mediated ER stress response	35:79	the phospho-eIF2α-mediated ER stress response	35:79	O-GlcNAcylation of eIF2α regulates the phospho-eIF2α-mediated ER stress response.
25937070	10	24	gly	O-GlcNAcylation	1549:1563	arg1	liver					1617:1621	thiamet-G-injected mouse liver	1592:1621	thiamet-G-injected mouse liver	1592:1621	This O-GlcNAcylation of eIF2α was reproduced in thiamet-G-injected mouse liver.
25937070	2	25	theme	ER	298:299	arg1	stress					301:306	ER stress	298:306	ER stress	298:306	For example, glucosamine-induced flux through the hexosamine biosynthetic pathway can promote ER stress and ER stress inducers can change the total cellular level of O-GlcNAcylation.
25937070	4	26	from	O-GlcNAcylated	617:630	arg1	study					526:530	this study	521:530	this study	521:530	In this study, eukaryotic translation initiation factor 2α (eIF2α), a major branch of the UPR, was O-GlcNAcylated at Ser 219, Thr 239, and Thr 241.
25937070	1	27	theme	stress	187:192	arg1	response					194:201	the endoplasmic reticulum (ER) stress response	156:201	the endoplasmic reticulum (ER) stress response	156:201	O-GlcNAcylation is highly involved in cellular stress responses including the endoplasmic reticulum (ER) stress response.
25937070	5	28	theme	phosphorylated	719:732	arg1	kinase					746:751	phosphorylated PKR-like ER kinase	719:751	phosphorylated PKR-like ER kinase	719:751	Upon ER stress, eIF2α is phosphorylated at Ser 51 by phosphorylated PKR-like ER kinase and this inhibits global translation initiation, except for that of specific mRNAs, including activating transcription factor 4, that induce stress-responsive genes such as C/EBP homologous protein (CHOP).
25937070	5	29	theme	transcription	858:870	arg1	factor					872:877	activating transcription factor 4	847:879	activating transcription factor 4	847:879	Upon ER stress, eIF2α is phosphorylated at Ser 51 by phosphorylated PKR-like ER kinase and this inhibits global translation initiation, except for that of specific mRNAs, including activating transcription factor 4, that induce stress-responsive genes such as C/EBP homologous protein (CHOP).
25937070	6	30	from	Ser	1118:1120	arg1	phosphorylation					1090:1104	phosphorylation	1090:1104	phosphorylation of eIF2α at Ser 51	1090:1123	Hyper-O-GlcNAcylation induced by O-GlcNAcase inhibitor (thiamet-G) treatment or O-GlcNAc transferase (OGT) overexpression hindered phosphorylation of eIF2α at Ser 51.
25937070	6	31	theme	inhibitor	1004:1012	arg1	treatment					1026:1034	O-GlcNAcase inhibitor (thiamet-G) treatment	992:1034	O-GlcNAcase inhibitor (thiamet-G) treatment	992:1034	Hyper-O-GlcNAcylation induced by O-GlcNAcase inhibitor (thiamet-G) treatment or O-GlcNAc transferase (OGT) overexpression hindered phosphorylation of eIF2α at Ser 51.
25937070	5	32	theme	PKR-like	734:741	arg1	kinase					746:751	phosphorylated PKR-like ER kinase	719:751	phosphorylated PKR-like ER kinase	719:751	Upon ER stress, eIF2α is phosphorylated at Ser 51 by phosphorylated PKR-like ER kinase and this inhibits global translation initiation, except for that of specific mRNAs, including activating transcription factor 4, that induce stress-responsive genes such as C/EBP homologous protein (CHOP).
25937070	4	33	theme	translation	544:554	arg1	eIF2α					578:582	eIF2α	578:582	eIF2α	578:582	In this study, eukaryotic translation initiation factor 2α (eIF2α), a major branch of the UPR, was O-GlcNAcylated at Ser 219, Thr 239, and Thr 241.
25937070	4	33	theme	translation	544:554	arg1	branch					594:599	a major branch	586:599	a major branch of the UPR	586:610	In this study, eukaryotic translation initiation factor 2α (eIF2α), a major branch of the UPR, was O-GlcNAcylated at Ser 219, Thr 239, and Thr 241.
25937070	4	33	theme	translation	544:554	arg1	factor					567:572	eukaryotic translation initiation factor 2α	533:575	eukaryotic translation initiation factor 2α (eIF2α)	533:583	In this study, eukaryotic translation initiation factor 2α (eIF2α), a major branch of the UPR, was O-GlcNAcylated at Ser 219, Thr 239, and Thr 241.
25937070	9	34	theme	CHOP-mediated	1518:1530	arg1	death					1537:1541	CHOP-mediated cell death	1518:1541	CHOP-mediated cell death	1518:1541	These results suggest that O-GlcNAcylation of eIF2α affects its phosphorylation at Ser 51 and influences CHOP-mediated cell death.
25937070	6	35	theme	O-GlcNAcase	992:1002	arg1	treatment					1026:1034	O-GlcNAcase inhibitor (thiamet-G) treatment	992:1034	O-GlcNAcase inhibitor (thiamet-G) treatment	992:1034	Hyper-O-GlcNAcylation induced by O-GlcNAcase inhibitor (thiamet-G) treatment or O-GlcNAc transferase (OGT) overexpression hindered phosphorylation of eIF2α at Ser 51.
25937070	5	36	theme	ER	743:744	arg1	kinase					746:751	phosphorylated PKR-like ER kinase	719:751	phosphorylated PKR-like ER kinase	719:751	Upon ER stress, eIF2α is phosphorylated at Ser 51 by phosphorylated PKR-like ER kinase and this inhibits global translation initiation, except for that of specific mRNAs, including activating transcription factor 4, that induce stress-responsive genes such as C/EBP homologous protein (CHOP).
25937070	4	37	theme	eukaryotic	533:542	arg1	eIF2α					578:582	eIF2α	578:582	eIF2α	578:582	In this study, eukaryotic translation initiation factor 2α (eIF2α), a major branch of the UPR, was O-GlcNAcylated at Ser 219, Thr 239, and Thr 241.
25937070	4	37	theme	eukaryotic	533:542	arg1	branch					594:599	a major branch	586:599	a major branch of the UPR	586:610	In this study, eukaryotic translation initiation factor 2α (eIF2α), a major branch of the UPR, was O-GlcNAcylated at Ser 219, Thr 239, and Thr 241.
25937070	4	37	theme	eukaryotic	533:542	arg1	factor					567:572	eukaryotic translation initiation factor 2α	533:575	eukaryotic translation initiation factor 2α (eIF2α)	533:583	In this study, eukaryotic translation initiation factor 2α (eIF2α), a major branch of the UPR, was O-GlcNAcylated at Ser 219, Thr 239, and Thr 241.
25937070	11	38	from	conclusion	1627:1636	arg1	important					1708:1716	important	1708:1716	important	1708:1716	In conclusion, proper regulation of O-GlcNAcylation and phosphorylation of eIF2α is important to maintain cellular homeostasis upon ER stress.
25937070	9	39	theme	cell	1532:1535	arg1	death					1537:1541	CHOP-mediated cell death	1518:1541	CHOP-mediated cell death	1518:1541	These results suggest that O-GlcNAcylation of eIF2α affects its phosphorylation at Ser 51 and influences CHOP-mediated cell death.
25937070	3	40	theme	response	461:468	arg1	s					434:434	s	434:434	s	434:434	However, it is largely unknown which component(s) of the unfolded protein response (UPR) is directly regulated by O-GlcNAcylation.
25937070	0	41	theme	eIF2α	19:23	arg1	O-GlcNAcylation					0:14	O-GlcNAcylation	0:14	O-GlcNAcylation of eIF2α	0:23	O-GlcNAcylation of eIF2α regulates the phospho-eIF2α-mediated ER stress response.
25937070	8	42	theme	eIF2α	1295:1299	arg1	eIF2α					1295:1299	eIF2α	1295:1299	eIF2α	1295:1299	Point mutation of the O-GlcNAcylation sites of eIF2α increased its phosphorylation at Ser 51 and CHOP expression and resulted in increased apoptosis upon ER stress.
25937070	8	42	theme	eIF2α	1295:1299	arg1	sites					1286:1290	the O-GlcNAcylation sites	1266:1290	the O-GlcNAcylation sites of eIF2α	1266:1299	Point mutation of the O-GlcNAcylation sites of eIF2α increased its phosphorylation at Ser 51 and CHOP expression and resulted in increased apoptosis upon ER stress.
25937070	11	43	theme	O-GlcNAcylation	1660:1674	arg1	regulation					1646:1655	proper regulation	1639:1655	proper regulation of O-GlcNAcylation	1639:1674	In conclusion, proper regulation of O-GlcNAcylation and phosphorylation of eIF2α is important to maintain cellular homeostasis upon ER stress.
25937070	11	43	theme	O-GlcNAcylation	1660:1674	arg1	phosphorylation					1680:1694	phosphorylation	1680:1694	phosphorylation of eIF2α	1680:1703	In conclusion, proper regulation of O-GlcNAcylation and phosphorylation of eIF2α is important to maintain cellular homeostasis upon ER stress.
25937070	1	44	theme	cellular	120:127	arg1	response					194:201	the endoplasmic reticulum (ER) stress response	156:201	the endoplasmic reticulum (ER) stress response	156:201	O-GlcNAcylation is highly involved in cellular stress responses including the endoplasmic reticulum (ER) stress response.
25937070	1	44	theme	cellular	120:127	arg1	responses					136:144	cellular stress responses	120:144	cellular stress responses including the endoplasmic reticulum (ER) stress response	120:201	O-GlcNAcylation is highly involved in cellular stress responses including the endoplasmic reticulum (ER) stress response.
25937070	6	45	theme	O-GlcNAc	1039:1046	arg1	OGT					1061:1063	OGT	1061:1063	OGT	1061:1063	Hyper-O-GlcNAcylation induced by O-GlcNAcase inhibitor (thiamet-G) treatment or O-GlcNAc transferase (OGT) overexpression hindered phosphorylation of eIF2α at Ser 51.
25937070	6	45	theme	O-GlcNAc	1039:1046	arg1	transferase					1048:1058	O-GlcNAc transferase	1039:1058	O-GlcNAc transferase (OGT) overexpression	1039:1079	Hyper-O-GlcNAcylation induced by O-GlcNAcase inhibitor (thiamet-G) treatment or O-GlcNAc transferase (OGT) overexpression hindered phosphorylation of eIF2α at Ser 51.
25937070	3	46	theme	component	424:432	arg1	s					434:434	s	434:434	s	434:434	However, it is largely unknown which component(s) of the unfolded protein response (UPR) is directly regulated by O-GlcNAcylation.
25937070	4	47	theme	initiation	556:565	arg1	eIF2α					578:582	eIF2α	578:582	eIF2α	578:582	In this study, eukaryotic translation initiation factor 2α (eIF2α), a major branch of the UPR, was O-GlcNAcylated at Ser 219, Thr 239, and Thr 241.
25937070	4	47	theme	initiation	556:565	arg1	branch					594:599	a major branch	586:599	a major branch of the UPR	586:610	In this study, eukaryotic translation initiation factor 2α (eIF2α), a major branch of the UPR, was O-GlcNAcylated at Ser 219, Thr 239, and Thr 241.
25937070	4	47	theme	initiation	556:565	arg1	factor					567:572	eukaryotic translation initiation factor 2α	533:575	eukaryotic translation initiation factor 2α (eIF2α)	533:583	In this study, eukaryotic translation initiation factor 2α (eIF2α), a major branch of the UPR, was O-GlcNAcylated at Ser 219, Thr 239, and Thr 241.
25937070	7	48	theme	dithiothreitol	1179:1192	arg1	treatment					1194:1202	dithiothreitol treatment	1179:1202	dithiothreitol treatment dependent on its phosphorylation at Ser 51	1179:1245	The level of O-GlcNAcylation of eIF2α was changed by dithiothreitol treatment dependent on its phosphorylation at Ser 51.
25937070	2	49	theme	hexosamine	254:263	arg1	pathway					278:284	the hexosamine biosynthetic pathway	250:284	the hexosamine biosynthetic pathway	250:284	For example, glucosamine-induced flux through the hexosamine biosynthetic pathway can promote ER stress and ER stress inducers can change the total cellular level of O-GlcNAcylation.
25937070	10	50	theme	thiamet-G-injected	1592:1609	arg1	liver					1617:1621	thiamet-G-injected mouse liver	1592:1621	thiamet-G-injected mouse liver	1592:1621	This O-GlcNAcylation of eIF2α was reproduced in thiamet-G-injected mouse liver.
25937070	3	51	theme	unfolded	444:451	arg1	UPR					471:473	UPR	471:473	UPR	471:473	However, it is largely unknown which component(s) of the unfolded protein response (UPR) is directly regulated by O-GlcNAcylation.
25937070	3	51	theme	unfolded	444:451	arg1	response					461:468	the unfolded protein response	440:468	the unfolded protein response (UPR)	440:474	However, it is largely unknown which component(s) of the unfolded protein response (UPR) is directly regulated by O-GlcNAcylation.
25937070	4	52	from	study	526:530	arg1	O-GlcNAcylated					617:630	O-GlcNAcylated	617:630	O-GlcNAcylated	617:630	In this study, eukaryotic translation initiation factor 2α (eIF2α), a major branch of the UPR, was O-GlcNAcylated at Ser 219, Thr 239, and Thr 241.
25937070	8	53	theme	ER	1402:1403	arg1	stress					1405:1410	ER stress	1402:1410	ER stress	1402:1410	Point mutation of the O-GlcNAcylation sites of eIF2α increased its phosphorylation at Ser 51 and CHOP expression and resulted in increased apoptosis upon ER stress.
25937070	5	54	theme	global	771:776	arg1	initiation					790:799	global translation initiation	771:799	global translation initiation	771:799	Upon ER stress, eIF2α is phosphorylated at Ser 51 by phosphorylated PKR-like ER kinase and this inhibits global translation initiation, except for that of specific mRNAs, including activating transcription factor 4, that induce stress-responsive genes such as C/EBP homologous protein (CHOP).
25937070	3	55	theme	protein	453:459	arg1	UPR					471:473	UPR	471:473	UPR	471:473	However, it is largely unknown which component(s) of the unfolded protein response (UPR) is directly regulated by O-GlcNAcylation.
25937070	3	55	theme	protein	453:459	arg1	response					461:468	the unfolded protein response	440:468	the unfolded protein response (UPR)	440:474	However, it is largely unknown which component(s) of the unfolded protein response (UPR) is directly regulated by O-GlcNAcylation.
25937070	0	56	theme	stress	65:70	arg1	response					72:79	the phospho-eIF2α-mediated ER stress response	35:79	the phospho-eIF2α-mediated ER stress response	35:79	O-GlcNAcylation of eIF2α regulates the phospho-eIF2α-mediated ER stress response.
25937070	11	57	from	important	1708:1716	arg1	conclusion					1627:1636	conclusion	1627:1636	conclusion	1627:1636	In conclusion, proper regulation of O-GlcNAcylation and phosphorylation of eIF2α is important to maintain cellular homeostasis upon ER stress.
25937070	8	58	theme	CHOP	1345:1348	arg1	expression					1350:1359	CHOP expression	1345:1359	CHOP expression	1345:1359	Point mutation of the O-GlcNAcylation sites of eIF2α increased its phosphorylation at Ser 51 and CHOP expression and resulted in increased apoptosis upon ER stress.
25937070	7	59	from	Ser	1240:1242	arg1	phosphorylation					1221:1235	its phosphorylation	1217:1235	its phosphorylation at Ser 51	1217:1245	The level of O-GlcNAcylation of eIF2α was changed by dithiothreitol treatment dependent on its phosphorylation at Ser 51.
25937070	1	60	theme	stress	129:134	arg1	response					194:201	the endoplasmic reticulum (ER) stress response	156:201	the endoplasmic reticulum (ER) stress response	156:201	O-GlcNAcylation is highly involved in cellular stress responses including the endoplasmic reticulum (ER) stress response.
25937070	1	60	theme	stress	129:134	arg1	responses					136:144	cellular stress responses	120:144	cellular stress responses including the endoplasmic reticulum (ER) stress response	120:201	O-GlcNAcylation is highly involved in cellular stress responses including the endoplasmic reticulum (ER) stress response.
25937070	0	61	theme	ER	62:63	arg1	response					72:79	the phospho-eIF2α-mediated ER stress response	35:79	the phospho-eIF2α-mediated ER stress response	35:79	O-GlcNAcylation of eIF2α regulates the phospho-eIF2α-mediated ER stress response.
25937070	2	62	theme	glucosamine-induced	217:235	arg1	flux					237:240	glucosamine-induced flux	217:240	glucosamine-induced flux through the hexosamine biosynthetic pathway	217:284	For example, glucosamine-induced flux through the hexosamine biosynthetic pathway can promote ER stress and ER stress inducers can change the total cellular level of O-GlcNAcylation.
25937070	2	63	theme	cellular	352:359	arg1	level					361:365	the total cellular level	342:365	the total cellular level of O-GlcNAcylation	342:384	For example, glucosamine-induced flux through the hexosamine biosynthetic pathway can promote ER stress and ER stress inducers can change the total cellular level of O-GlcNAcylation.
25937070	5	64	theme	homologous	932:941	arg1	CHOP					952:955	CHOP	952:955	CHOP	952:955	Upon ER stress, eIF2α is phosphorylated at Ser 51 by phosphorylated PKR-like ER kinase and this inhibits global translation initiation, except for that of specific mRNAs, including activating transcription factor 4, that induce stress-responsive genes such as C/EBP homologous protein (CHOP).
25937070	5	64	theme	homologous	932:941	arg1	protein					943:949	C/EBP homologous protein	926:949	C/EBP homologous protein (CHOP)	926:956	Upon ER stress, eIF2α is phosphorylated at Ser 51 by phosphorylated PKR-like ER kinase and this inhibits global translation initiation, except for that of specific mRNAs, including activating transcription factor 4, that induce stress-responsive genes such as C/EBP homologous protein (CHOP).
25937070	2	65	theme	total	346:350	arg1	level					361:365	the total cellular level	342:365	the total cellular level of O-GlcNAcylation	342:384	For example, glucosamine-induced flux through the hexosamine biosynthetic pathway can promote ER stress and ER stress inducers can change the total cellular level of O-GlcNAcylation.
25937070	4	66	from	Thr	657:659	arg1	O-GlcNAcylated					617:630	O-GlcNAcylated	617:630	O-GlcNAcylated	617:630	In this study, eukaryotic translation initiation factor 2α (eIF2α), a major branch of the UPR, was O-GlcNAcylated at Ser 219, Thr 239, and Thr 241.
25937070	6	67	theme	eIF2α	1109:1113	arg1	phosphorylation					1090:1104	phosphorylation	1090:1104	phosphorylation of eIF2α at Ser 51	1090:1123	Hyper-O-GlcNAcylation induced by O-GlcNAcase inhibitor (thiamet-G) treatment or O-GlcNAc transferase (OGT) overexpression hindered phosphorylation of eIF2α at Ser 51.
25937070	8	68	theme	sites	1286:1290	arg1	mutation					1254:1261	Point mutation	1248:1261	Point mutation of the O-GlcNAcylation sites of eIF2α	1248:1299	Point mutation of the O-GlcNAcylation sites of eIF2α increased its phosphorylation at Ser 51 and CHOP expression and resulted in increased apoptosis upon ER stress.
25937070	5	69	theme	activating	847:856	arg1	factor					872:877	activating transcription factor 4	847:879	activating transcription factor 4	847:879	Upon ER stress, eIF2α is phosphorylated at Ser 51 by phosphorylated PKR-like ER kinase and this inhibits global translation initiation, except for that of specific mRNAs, including activating transcription factor 4, that induce stress-responsive genes such as C/EBP homologous protein (CHOP).
25937070	7	70	theme	dependent	1204:1212	arg1	treatment					1194:1202	dithiothreitol treatment	1179:1202	dithiothreitol treatment dependent on its phosphorylation at Ser 51	1179:1245	The level of O-GlcNAcylation of eIF2α was changed by dithiothreitol treatment dependent on its phosphorylation at Ser 51.
25937070	7	71	theme	eIF2α	1158:1162	arg1	O-GlcNAcylation					1139:1153	O-GlcNAcylation	1139:1153	O-GlcNAcylation of eIF2α	1139:1162	The level of O-GlcNAcylation of eIF2α was changed by dithiothreitol treatment dependent on its phosphorylation at Ser 51.
25937070	4	72	theme	UPR	608:610	arg1	factor					567:572	eukaryotic translation initiation factor 2α	533:575	eukaryotic translation initiation factor 2α (eIF2α)	533:583	In this study, eukaryotic translation initiation factor 2α (eIF2α), a major branch of the UPR, was O-GlcNAcylated at Ser 219, Thr 239, and Thr 241.
25937070	4	72	theme	UPR	608:610	arg1	branch					594:599	a major branch	586:599	a major branch of the UPR	586:610	In this study, eukaryotic translation initiation factor 2α (eIF2α), a major branch of the UPR, was O-GlcNAcylated at Ser 219, Thr 239, and Thr 241.
25937070	5	73	theme	C/EBP	926:930	arg1	CHOP					952:955	CHOP	952:955	CHOP	952:955	Upon ER stress, eIF2α is phosphorylated at Ser 51 by phosphorylated PKR-like ER kinase and this inhibits global translation initiation, except for that of specific mRNAs, including activating transcription factor 4, that induce stress-responsive genes such as C/EBP homologous protein (CHOP).
25937070	5	73	theme	C/EBP	926:930	arg1	protein					943:949	C/EBP homologous protein	926:949	C/EBP homologous protein (CHOP)	926:956	Upon ER stress, eIF2α is phosphorylated at Ser 51 by phosphorylated PKR-like ER kinase and this inhibits global translation initiation, except for that of specific mRNAs, including activating transcription factor 4, that induce stress-responsive genes such as C/EBP homologous protein (CHOP).
25937070	9	74	theme	eIF2α	1459:1463	arg1	O-GlcNAcylation					1440:1454	O-GlcNAcylation	1440:1454	O-GlcNAcylation of eIF2α	1440:1463	These results suggest that O-GlcNAcylation of eIF2α affects its phosphorylation at Ser 51 and influences CHOP-mediated cell death.
25937070	1	75	theme	endoplasmic	160:170	arg1	reticulum					172:180	endoplasmic reticulum	160:180	the endoplasmic reticulum (ER) stress response	156:201	O-GlcNAcylation is highly involved in cellular stress responses including the endoplasmic reticulum (ER) stress response.
25937070	1	75	theme	endoplasmic	160:170	arg1	ER					183:184	ER	183:184	ER	183:184	O-GlcNAcylation is highly involved in cellular stress responses including the endoplasmic reticulum (ER) stress response.
25937070	9	76	from	Ser	1496:1498	arg1	phosphorylation					1477:1491	its phosphorylation	1473:1491	its phosphorylation at Ser 51	1473:1501	These results suggest that O-GlcNAcylation of eIF2α affects its phosphorylation at Ser 51 and influences CHOP-mediated cell death.
25937070	2	77	theme	biosynthetic	265:276	arg1	pathway					278:284	the hexosamine biosynthetic pathway	250:284	the hexosamine biosynthetic pathway	250:284	For example, glucosamine-induced flux through the hexosamine biosynthetic pathway can promote ER stress and ER stress inducers can change the total cellular level of O-GlcNAcylation.
25937070	1	78	theme	reticulum	172:180	arg1	response					194:201	the endoplasmic reticulum (ER) stress response	156:201	the endoplasmic reticulum (ER) stress response	156:201	O-GlcNAcylation is highly involved in cellular stress responses including the endoplasmic reticulum (ER) stress response.
25937070	4	79	theme	major	588:592	arg1	factor					567:572	eukaryotic translation initiation factor 2α	533:575	eukaryotic translation initiation factor 2α (eIF2α)	533:583	In this study, eukaryotic translation initiation factor 2α (eIF2α), a major branch of the UPR, was O-GlcNAcylated at Ser 219, Thr 239, and Thr 241.
25937070	4	79	theme	major	588:592	arg1	branch					594:599	a major branch	586:599	a major branch of the UPR	586:610	In this study, eukaryotic translation initiation factor 2α (eIF2α), a major branch of the UPR, was O-GlcNAcylated at Ser 219, Thr 239, and Thr 241.
30012597	0	0	theme	AP-1	92:95	arg1	factor					111:116	AP-1 transcription factor	92:116	the AP-1 transcription factor JUN	88:120	Schwann cell O-GlcNAcylation promotes peripheral nerve remyelination via attenuation of the AP-1 transcription factor JUN.
30012597	11	1	theme	transcriptional	1619:1633	arg1	activity					1635:1642	AP-1 transcriptional activity	1614:1642	AP-1 transcriptional activity	1614:1642	Mechanistically, OGT O-GlcNAcylates JUN at multiple sites, which then leads to an attenuation of AP-1 transcriptional activity.
30012597	10	2	theme	injury	1433:1438	arg1	response					1440:1447	This aberrant nerve injury response	1413:1447	This aberrant nerve injury response	1413:1447	This aberrant nerve injury response is normalized in OGT-SCKO mice with reduced Jun gene dosage in SCs.
30012597	9	3	theme	JUN	1292:1294	arg1	activity					1296:1303	This aberrant JUN activity	1278:1303	This aberrant JUN activity	1278:1303	This aberrant JUN activity results in abnormalities in repair SC function and redifferentiation and prevents the timely remyelination.
30012597	8	4	theme	SCs	1124:1126	arg1	profiling					1102:1110	Gene expression profiling	1086:1110	Gene expression profiling of OGT-SCKO SCs	1086:1126	Gene expression profiling of OGT-SCKO SCs revealed that the JUN-dependent SC injury program was elevated in the absence of injury and failed to shut down at the appropriate time after injury.
30012597	10	5	theme	nerve	1427:1431	arg1	response					1440:1447	This aberrant nerve injury response	1413:1447	This aberrant nerve injury response	1413:1447	This aberrant nerve injury response is normalized in OGT-SCKO mice with reduced Jun gene dosage in SCs.
30012597	12	6	theme	activity	1758:1765	arg1	regulation					1740:1749	the regulation	1736:1749	the regulation of JUN activity by O-GlcNAcylation, a pathway that could be important in the neuropathy associated with diabetes and aging	1736:1872	Together, these results highlight the metabolic oversight of the nerve injury response via the regulation of JUN activity by O-GlcNAcylation, a pathway that could be important in the neuropathy associated with diabetes and aging.
30012597	9	7	theme	timely	1391:1396	arg1	remyelination					1398:1410	the timely remyelination	1387:1410	the timely remyelination	1387:1410	This aberrant JUN activity results in abnormalities in repair SC function and redifferentiation and prevents the timely remyelination.
30012597	0	8	theme	factor	111:116	arg1	JUN					118:120	the AP-1 transcription factor JUN	88:120	the AP-1 transcription factor JUN	88:120	Schwann cell O-GlcNAcylation promotes peripheral nerve remyelination via attenuation of the AP-1 transcription factor JUN.
30012597	4	9	with	mice	667:670	arg1	deletion					691:698	a SC-specific deletion	677:698	a SC-specific deletion of O-GlcNAc transferase (OGT)	677:728	Previously, we produced mice with a SC-specific deletion of O-GlcNAc transferase (OGT).
30012597	10	10	theme	aberrant	1418:1425	arg1	response					1440:1447	This aberrant nerve injury response	1413:1447	This aberrant nerve injury response	1413:1447	This aberrant nerve injury response is normalized in OGT-SCKO mice with reduced Jun gene dosage in SCs.
30012597	0	11	theme	transcription	97:109	arg1	factor					111:116	AP-1 transcription factor	92:116	the AP-1 transcription factor JUN	88:120	Schwann cell O-GlcNAcylation promotes peripheral nerve remyelination via attenuation of the AP-1 transcription factor JUN.
30012597	12	12	theme	JUN	1754:1756	arg1	activity					1758:1765	JUN activity	1754:1765	JUN activity	1754:1765	Together, these results highlight the metabolic oversight of the nerve injury response via the regulation of JUN activity by O-GlcNAcylation, a pathway that could be important in the neuropathy associated with diabetes and aging.
30012597	3	13	dep	factor	451:456	arg1	JUN					458:460	JUN	458:460	The AP-1 transcription factor JUN	428:460	The AP-1 transcription factor JUN is promptly induced in SCs upon nerve injury and potently mediates this injury-induced SC plasticity; however, the regulation of these JUN-dependent SC injury responses is unclear.
30012597	9	14	theme	repair	1333:1338	arg1	function					1343:1350	repair SC function	1333:1350	repair SC function	1333:1350	This aberrant JUN activity results in abnormalities in repair SC function and redifferentiation and prevents the timely remyelination.
30012597	10	15	from	dosage	1502:1507	arg1	SCs					1512:1514	SCs	1512:1514	SCs	1512:1514	This aberrant nerve injury response is normalized in OGT-SCKO mice with reduced Jun gene dosage in SCs.
30012597	6	16	from	OGT	868:870	arg1	SCs					875:877	SCs	875:877	SCs	875:877	Mice lacking OGT in SCs develop a progressive demyelinating peripheral neuropathy.
30012597	8	17	theme	SC	1160:1161	arg1	program					1170:1176	the JUN-dependent SC injury program	1142:1176	the JUN-dependent SC injury program	1142:1176	Gene expression profiling of OGT-SCKO SCs revealed that the JUN-dependent SC injury program was elevated in the absence of injury and failed to shut down at the appropriate time after injury.
30012597	11	18	theme	activity	1635:1642	arg1	attenuation					1599:1609	an attenuation	1596:1609	an attenuation of AP-1 transcriptional activity	1596:1642	Mechanistically, OGT O-GlcNAcylates JUN at multiple sites, which then leads to an attenuation of AP-1 transcriptional activity.
30012597	1	19	theme	peripheral	160:169	arg1	system					179:184	the peripheral nervous system	156:184	the peripheral nervous system	156:184	Schwann cells (SCs), the glia of the peripheral nervous system, play an essential role in nerve regeneration.
30012597	0	20	theme	JUN	118:120	arg1	attenuation					73:83	attenuation	73:83	attenuation of the AP-1 transcription factor JUN	73:120	Schwann cell O-GlcNAcylation promotes peripheral nerve remyelination via attenuation of the AP-1 transcription factor JUN.
30012597	9	21	theme	aberrant	1283:1290	arg1	activity					1296:1303	This aberrant JUN activity	1278:1303	This aberrant JUN activity	1278:1303	This aberrant JUN activity results in abnormalities in repair SC function and redifferentiation and prevents the timely remyelination.
30012597	9	22	from	abnormalities	1316:1328	arg1	redifferentiation					1356:1372	redifferentiation	1356:1372	redifferentiation	1356:1372	This aberrant JUN activity results in abnormalities in repair SC function and redifferentiation and prevents the timely remyelination.
30012597	9	22	from	abnormalities	1316:1328	arg1	function					1343:1350	repair SC function	1333:1350	repair SC function	1333:1350	This aberrant JUN activity results in abnormalities in repair SC function and redifferentiation and prevents the timely remyelination.
30012597	12	23	theme	injury	1716:1721	arg1	response					1723:1730	the nerve injury response	1706:1730	the nerve injury response	1706:1730	Together, these results highlight the metabolic oversight of the nerve injury response via the regulation of JUN activity by O-GlcNAcylation, a pathway that could be important in the neuropathy associated with diabetes and aging.
30012597	3	24	theme	nerve	494:498	arg1	injury					500:505	nerve injury	494:505	nerve injury	494:505	The AP-1 transcription factor JUN is promptly induced in SCs upon nerve injury and potently mediates this injury-induced SC plasticity; however, the regulation of these JUN-dependent SC injury responses is unclear.
30012597	5	25	theme	cellular	829:836	arg1	state					848:852	the cellular metabolic state	825:852	the cellular metabolic state	825:852	This enzyme catalyzes O-GlcNAcylation, a posttranslational modification that is influenced by the cellular metabolic state.
30012597	2	26	theme	regenerating	408:419	arg1	axons					421:425	regenerating axons	408:425	regenerating axons	408:425	Upon nerve injury, SCs are reprogrammed into unique "repair SCs," and these cells remove degenerating axons/myelin debris, promote axonal regrowth, and ultimately remyelinate regenerating axons.
30012597	7	27	from	process	977:983	arg1	mice					1004:1007	OGT-SCKO mutant mice	988:1007	OGT-SCKO mutant mice	988:1007	Here, we investigated the nerve repair process in OGT-SCKO mutant mice and found that the remyelination of regenerating axons is severely impaired.
30012597	7	28	theme	axons	1058:1062	arg1	remyelination					1028:1040	the remyelination	1024:1040	the remyelination of regenerating axons	1024:1062	Here, we investigated the nerve repair process in OGT-SCKO mutant mice and found that the remyelination of regenerating axons is severely impaired.
30012597	12	29	theme	nerve	1710:1714	arg1	response					1723:1730	the nerve injury response	1706:1730	the nerve injury response	1706:1730	Together, these results highlight the metabolic oversight of the nerve injury response via the regulation of JUN activity by O-GlcNAcylation, a pathway that could be important in the neuropathy associated with diabetes and aging.
30012597	10	30	theme	Jun	1493:1495	arg1	dosage					1502:1507	reduced Jun gene dosage	1485:1507	reduced Jun gene dosage in SCs	1485:1514	This aberrant nerve injury response is normalized in OGT-SCKO mice with reduced Jun gene dosage in SCs.
30012597	2	31	theme	axons/myelin	335:346	arg1	debris					348:353	degenerating axons/myelin debris	322:353	degenerating axons/myelin debris	322:353	Upon nerve injury, SCs are reprogrammed into unique "repair SCs," and these cells remove degenerating axons/myelin debris, promote axonal regrowth, and ultimately remyelinate regenerating axons.
30012597	0	32	theme	Schwann	0:6	arg1	O-GlcNAcylation					13:27	Schwann cell O-GlcNAcylation	0:27	Schwann cell O-GlcNAcylation	0:27	Schwann cell O-GlcNAcylation promotes peripheral nerve remyelination via attenuation of the AP-1 transcription factor JUN.
30012597	9	33	theme	SC	1340:1341	arg1	function					1343:1350	repair SC function	1333:1350	repair SC function	1333:1350	This aberrant JUN activity results in abnormalities in repair SC function and redifferentiation and prevents the timely remyelination.
30012597	2	34	theme	unique	278:283	arg1	SCs					293:295	unique "repair SCs	278:295	unique "repair SCs	278:295	Upon nerve injury, SCs are reprogrammed into unique "repair SCs," and these cells remove degenerating axons/myelin debris, promote axonal regrowth, and ultimately remyelinate regenerating axons.
30012597	2	35	theme	degenerating	322:333	arg1	debris					348:353	degenerating axons/myelin debris	322:353	degenerating axons/myelin debris	322:353	Upon nerve injury, SCs are reprogrammed into unique "repair SCs," and these cells remove degenerating axons/myelin debris, promote axonal regrowth, and ultimately remyelinate regenerating axons.
30012597	5	36	theme	posttranslational	772:788	arg1	O-GlcNAcylation					753:767	O-GlcNAcylation	753:767	O-GlcNAcylation	753:767	This enzyme catalyzes O-GlcNAcylation, a posttranslational modification that is influenced by the cellular metabolic state.
30012597	5	36	theme	posttranslational	772:788	arg1	modification					790:801	a posttranslational modification	770:801	a posttranslational modification that is influenced by the cellular metabolic state	770:852	This enzyme catalyzes O-GlcNAcylation, a posttranslational modification that is influenced by the cellular metabolic state.
30012597	10	37	theme	reduced	1485:1491	arg1	dosage					1502:1507	reduced Jun gene dosage	1485:1507	reduced Jun gene dosage in SCs	1485:1514	This aberrant nerve injury response is normalized in OGT-SCKO mice with reduced Jun gene dosage in SCs.
30012597	4	38	theme	transferase	712:722	arg1	deletion					691:698	a SC-specific deletion	677:698	a SC-specific deletion of O-GlcNAc transferase (OGT)	677:728	Previously, we produced mice with a SC-specific deletion of O-GlcNAc transferase (OGT).
30012597	1	39	theme	system	179:184	arg1	cells					131:135	Schwann cells	123:135	Schwann cells (SCs)	123:141	Schwann cells (SCs), the glia of the peripheral nervous system, play an essential role in nerve regeneration.
30012597	1	39	theme	system	179:184	arg1	glia					148:151	the glia	144:151	the glia of the peripheral nervous system	144:184	Schwann cells (SCs), the glia of the peripheral nervous system, play an essential role in nerve regeneration.
30012597	3	40	theme	injury-induced	534:547	arg1	plasticity					552:561	this injury-induced SC plasticity	529:561	this injury-induced SC plasticity	529:561	The AP-1 transcription factor JUN is promptly induced in SCs upon nerve injury and potently mediates this injury-induced SC plasticity; however, the regulation of these JUN-dependent SC injury responses is unclear.
30012597	7	41	theme	regenerating	1045:1056	arg1	axons					1058:1062	regenerating axons	1045:1062	regenerating axons	1045:1062	Here, we investigated the nerve repair process in OGT-SCKO mutant mice and found that the remyelination of regenerating axons is severely impaired.
30012597	3	42	theme	SC	611:612	arg1	responses					621:629	these JUN-dependent SC injury responses	591:629	these JUN-dependent SC injury responses	591:629	The AP-1 transcription factor JUN is promptly induced in SCs upon nerve injury and potently mediates this injury-induced SC plasticity; however, the regulation of these JUN-dependent SC injury responses is unclear.
30012597	4	43	theme	O-GlcNAc	703:710	arg1	OGT					725:727	OGT	725:727	OGT	725:727	Previously, we produced mice with a SC-specific deletion of O-GlcNAc transferase (OGT).
30012597	4	43	theme	O-GlcNAc	703:710	arg1	transferase					712:722	O-GlcNAc transferase	703:722	O-GlcNAc transferase (OGT)	703:728	Previously, we produced mice with a SC-specific deletion of O-GlcNAc transferase (OGT).
30012597	3	44	theme	AP-1	432:435	arg1	factor					451:456	The AP-1 transcription factor	428:456	The AP-1 transcription factor JUN	428:460	The AP-1 transcription factor JUN is promptly induced in SCs upon nerve injury and potently mediates this injury-induced SC plasticity; however, the regulation of these JUN-dependent SC injury responses is unclear.
30012597	0	45	theme	nerve	49:53	arg1	remyelination					55:67	peripheral nerve remyelination	38:67	peripheral nerve remyelination	38:67	Schwann cell O-GlcNAcylation promotes peripheral nerve remyelination via attenuation of the AP-1 transcription factor JUN.
30012597	12	46	from	neuropathy	1828:1837	arg1	O-GlcNAcylation					1770:1784	O-GlcNAcylation	1770:1784	O-GlcNAcylation	1770:1784	Together, these results highlight the metabolic oversight of the nerve injury response via the regulation of JUN activity by O-GlcNAcylation, a pathway that could be important in the neuropathy associated with diabetes and aging.
30012597	12	46	from	neuropathy	1828:1837	arg1	pathway					1789:1795	a pathway	1787:1795	a pathway that could be important in the neuropathy associated with diabetes and aging	1787:1872	Together, these results highlight the metabolic oversight of the nerve injury response via the regulation of JUN activity by O-GlcNAcylation, a pathway that could be important in the neuropathy associated with diabetes and aging.
30012597	12	46	from	neuropathy	1828:1837	arg1	important					1811:1819	important	1811:1819	important	1811:1819	Together, these results highlight the metabolic oversight of the nerve injury response via the regulation of JUN activity by O-GlcNAcylation, a pathway that could be important in the neuropathy associated with diabetes and aging.
30012597	12	47	from	important	1811:1819	arg1	neuropathy					1828:1837	the neuropathy	1824:1837	the neuropathy associated with diabetes and aging	1824:1872	Together, these results highlight the metabolic oversight of the nerve injury response via the regulation of JUN activity by O-GlcNAcylation, a pathway that could be important in the neuropathy associated with diabetes and aging.
30012597	3	48	theme	injury	614:619	arg1	responses					621:629	these JUN-dependent SC injury responses	591:629	these JUN-dependent SC injury responses	591:629	The AP-1 transcription factor JUN is promptly induced in SCs upon nerve injury and potently mediates this injury-induced SC plasticity; however, the regulation of these JUN-dependent SC injury responses is unclear.
30012597	1	49	theme	nervous	171:177	arg1	system					179:184	the peripheral nervous system	156:184	the peripheral nervous system	156:184	Schwann cells (SCs), the glia of the peripheral nervous system, play an essential role in nerve regeneration.
30012597	2	50	theme	axonal	364:369	arg1	regrowth					371:378	axonal regrowth	364:378	axonal regrowth	364:378	Upon nerve injury, SCs are reprogrammed into unique "repair SCs," and these cells remove degenerating axons/myelin debris, promote axonal regrowth, and ultimately remyelinate regenerating axons.
30012597	0	51	theme	peripheral	38:47	arg1	remyelination					55:67	peripheral nerve remyelination	38:67	peripheral nerve remyelination	38:67	Schwann cell O-GlcNAcylation promotes peripheral nerve remyelination via attenuation of the AP-1 transcription factor JUN.
30012597	5	52	theme	metabolic	838:846	arg1	state					848:852	the cellular metabolic state	825:852	the cellular metabolic state	825:852	This enzyme catalyzes O-GlcNAcylation, a posttranslational modification that is influenced by the cellular metabolic state.
30012597	7	53	theme	OGT-SCKO	988:995	arg1	mice					1004:1007	OGT-SCKO mutant mice	988:1007	OGT-SCKO mutant mice	988:1007	Here, we investigated the nerve repair process in OGT-SCKO mutant mice and found that the remyelination of regenerating axons is severely impaired.
30012597	8	54	theme	JUN-dependent	1146:1158	arg1	program					1170:1176	the JUN-dependent SC injury program	1142:1176	the JUN-dependent SC injury program	1142:1176	Gene expression profiling of OGT-SCKO SCs revealed that the JUN-dependent SC injury program was elevated in the absence of injury and failed to shut down at the appropriate time after injury.
30012597	6	55	theme	peripheral	915:924	arg1	neuropathy					926:935	a progressive demyelinating peripheral neuropathy	887:935	a progressive demyelinating peripheral neuropathy	887:935	Mice lacking OGT in SCs develop a progressive demyelinating peripheral neuropathy.
30012597	8	56	theme	Gene	1086:1089	arg1	profiling					1102:1110	Gene expression profiling	1086:1110	Gene expression profiling of OGT-SCKO SCs	1086:1126	Gene expression profiling of OGT-SCKO SCs revealed that the JUN-dependent SC injury program was elevated in the absence of injury and failed to shut down at the appropriate time after injury.
30012597	3	57	theme	JUN-dependent	597:609	arg1	responses					621:629	these JUN-dependent SC injury responses	591:629	these JUN-dependent SC injury responses	591:629	The AP-1 transcription factor JUN is promptly induced in SCs upon nerve injury and potently mediates this injury-induced SC plasticity; however, the regulation of these JUN-dependent SC injury responses is unclear.
30012597	3	58	theme	SC	549:550	arg1	plasticity					552:561	this injury-induced SC plasticity	529:561	this injury-induced SC plasticity	529:561	The AP-1 transcription factor JUN is promptly induced in SCs upon nerve injury and potently mediates this injury-induced SC plasticity; however, the regulation of these JUN-dependent SC injury responses is unclear.
30012597	7	59	theme	mutant	997:1002	arg1	mice					1004:1007	OGT-SCKO mutant mice	988:1007	OGT-SCKO mutant mice	988:1007	Here, we investigated the nerve repair process in OGT-SCKO mutant mice and found that the remyelination of regenerating axons is severely impaired.
30012597	1	60	theme	Schwann	123:129	arg1	SCs					138:140	SCs	138:140	SCs	138:140	Schwann cells (SCs), the glia of the peripheral nervous system, play an essential role in nerve regeneration.
30012597	1	60	theme	Schwann	123:129	arg1	cells					131:135	Schwann cells	123:135	Schwann cells (SCs)	123:141	Schwann cells (SCs), the glia of the peripheral nervous system, play an essential role in nerve regeneration.
30012597	1	60	theme	Schwann	123:129	arg1	glia					148:151	the glia	144:151	the glia of the peripheral nervous system	144:184	Schwann cells (SCs), the glia of the peripheral nervous system, play an essential role in nerve regeneration.
30012597	10	61	theme	OGT-SCKO	1466:1473	arg1	mice					1475:1478	OGT-SCKO mice	1466:1478	OGT-SCKO mice with reduced Jun gene dosage in SCs	1466:1514	This aberrant nerve injury response is normalized in OGT-SCKO mice with reduced Jun gene dosage in SCs.
30012597	6	62	theme	demyelinating	901:913	arg1	neuropathy					926:935	a progressive demyelinating peripheral neuropathy	887:935	a progressive demyelinating peripheral neuropathy	887:935	Mice lacking OGT in SCs develop a progressive demyelinating peripheral neuropathy.
30012597	11	63	theme	multiple	1560:1567	arg1	sites					1569:1573	multiple sites	1560:1573	multiple sites	1560:1573	Mechanistically, OGT O-GlcNAcylates JUN at multiple sites, which then leads to an attenuation of AP-1 transcriptional activity.
30012597	8	64	theme	appropriate	1247:1257	arg1	time					1259:1262	the appropriate time	1243:1262	the appropriate time after injury	1243:1275	Gene expression profiling of OGT-SCKO SCs revealed that the JUN-dependent SC injury program was elevated in the absence of injury and failed to shut down at the appropriate time after injury.
30012597	10	65	with	mice	1475:1478	arg1	dosage					1502:1507	reduced Jun gene dosage	1485:1507	reduced Jun gene dosage in SCs	1485:1514	This aberrant nerve injury response is normalized in OGT-SCKO mice with reduced Jun gene dosage in SCs.
30012597	6	66	theme	progressive	889:899	arg1	neuropathy					926:935	a progressive demyelinating peripheral neuropathy	887:935	a progressive demyelinating peripheral neuropathy	887:935	Mice lacking OGT in SCs develop a progressive demyelinating peripheral neuropathy.
30012597	10	67	theme	gene	1497:1500	arg1	dosage					1502:1507	reduced Jun gene dosage	1485:1507	reduced Jun gene dosage in SCs	1485:1514	This aberrant nerve injury response is normalized in OGT-SCKO mice with reduced Jun gene dosage in SCs.
30012597	2	68	theme	nerve	238:242	arg1	injury					244:249	nerve injury	238:249	nerve injury	238:249	Upon nerve injury, SCs are reprogrammed into unique "repair SCs," and these cells remove degenerating axons/myelin debris, promote axonal regrowth, and ultimately remyelinate regenerating axons.
30012597	3	69	theme	transcription	437:449	arg1	factor					451:456	The AP-1 transcription factor	428:456	The AP-1 transcription factor JUN	428:460	The AP-1 transcription factor JUN is promptly induced in SCs upon nerve injury and potently mediates this injury-induced SC plasticity; however, the regulation of these JUN-dependent SC injury responses is unclear.
30012597	1	70	theme	essential	195:203	arg1	role					205:208	an essential role	192:208	an essential role	192:208	Schwann cells (SCs), the glia of the peripheral nervous system, play an essential role in nerve regeneration.
30012597	8	71	theme	expression	1091:1100	arg1	profiling					1102:1110	Gene expression profiling	1086:1110	Gene expression profiling of OGT-SCKO SCs	1086:1126	Gene expression profiling of OGT-SCKO SCs revealed that the JUN-dependent SC injury program was elevated in the absence of injury and failed to shut down at the appropriate time after injury.
30012597	3	72	theme	responses	621:629	arg1	unclear					634:640	unclear	634:640	unclear	634:640	The AP-1 transcription factor JUN is promptly induced in SCs upon nerve injury and potently mediates this injury-induced SC plasticity; however, the regulation of these JUN-dependent SC injury responses is unclear.
30012597	3	72	theme	responses	621:629	arg1	regulation					577:586	the regulation	573:586	the regulation of these JUN-dependent SC injury responses	573:629	The AP-1 transcription factor JUN is promptly induced in SCs upon nerve injury and potently mediates this injury-induced SC plasticity; however, the regulation of these JUN-dependent SC injury responses is unclear.
30012597	8	73	theme	injury	1163:1168	arg1	program					1170:1176	the JUN-dependent SC injury program	1142:1176	the JUN-dependent SC injury program	1142:1176	Gene expression profiling of OGT-SCKO SCs revealed that the JUN-dependent SC injury program was elevated in the absence of injury and failed to shut down at the appropriate time after injury.
30012597	7	74	theme	nerve	964:968	arg1	process					977:983	the nerve repair process	960:983	the nerve repair process in OGT-SCKO mutant mice	960:1007	Here, we investigated the nerve repair process in OGT-SCKO mutant mice and found that the remyelination of regenerating axons is severely impaired.
30012597	2	75	theme	repair	286:291	arg1	SCs					293:295	unique "repair SCs	278:295	unique "repair SCs	278:295	Upon nerve injury, SCs are reprogrammed into unique "repair SCs," and these cells remove degenerating axons/myelin debris, promote axonal regrowth, and ultimately remyelinate regenerating axons.
30012597	4	76	theme	SC-specific	679:689	arg1	deletion					691:698	a SC-specific deletion	677:698	a SC-specific deletion of O-GlcNAc transferase (OGT)	677:728	Previously, we produced mice with a SC-specific deletion of O-GlcNAc transferase (OGT).
30012597	8	77	theme	OGT-SCKO	1115:1122	arg1	SCs					1124:1126	OGT-SCKO SCs	1115:1126	OGT-SCKO SCs	1115:1126	Gene expression profiling of OGT-SCKO SCs revealed that the JUN-dependent SC injury program was elevated in the absence of injury and failed to shut down at the appropriate time after injury.
30012597	7	78	theme	repair	970:975	arg1	process					977:983	the nerve repair process	960:983	the nerve repair process in OGT-SCKO mutant mice	960:1007	Here, we investigated the nerve repair process in OGT-SCKO mutant mice and found that the remyelination of regenerating axons is severely impaired.
30012597	8	79	theme	injury	1209:1214	arg1	absence					1198:1204	the absence	1194:1204	the absence of injury	1194:1214	Gene expression profiling of OGT-SCKO SCs revealed that the JUN-dependent SC injury program was elevated in the absence of injury and failed to shut down at the appropriate time after injury.
30012597	11	80	theme	AP-1	1614:1617	arg1	activity					1635:1642	AP-1 transcriptional activity	1614:1642	AP-1 transcriptional activity	1614:1642	Mechanistically, OGT O-GlcNAcylates JUN at multiple sites, which then leads to an attenuation of AP-1 transcriptional activity.
30012597	0	81	theme	cell	8:11	arg1	O-GlcNAcylation					13:27	Schwann cell O-GlcNAcylation	0:27	Schwann cell O-GlcNAcylation	0:27	Schwann cell O-GlcNAcylation promotes peripheral nerve remyelination via attenuation of the AP-1 transcription factor JUN.
30012597	11	82	from	sites	1569:1573	arg1	JUN					1553:1555	JUN	1553:1555	JUN	1553:1555	Mechanistically, OGT O-GlcNAcylates JUN at multiple sites, which then leads to an attenuation of AP-1 transcriptional activity.
30012597	1	83	theme	nerve	213:217	arg1	regeneration					219:230	nerve regeneration	213:230	nerve regeneration	213:230	Schwann cells (SCs), the glia of the peripheral nervous system, play an essential role in nerve regeneration.
30677218	0	0	theme	eukaryotic	102:111	arg1	4E					131:132	eukaryotic initiation factor 4E	102:132	eukaryotic initiation factor 4E	102:132	O-GlcNAc transferase activates stem-like cell potential in hepatocarcinoma through O-GlcNAcylation of eukaryotic initiation factor 4E.
30677218	3	1	theme	high	388:391	arg1	glucose					393:399	high glucose	388:399	high glucose	388:399	Dysregulation of O-GlcNAcylation in response to high glucose or OGT expression has been implicated in metabolic diseases and cancer.
30677218	5	2	theme	cell	725:728	arg1	potential					730:738	stem-like cell potential	715:738	stem-like cell potential	715:738	Here, we employed the lentiviral shRNA-based system to knockdown OGT to analyse the contribution of OGT in hepatoma cell proliferation and stem-like cell potential.
30677218	5	3	theme	shRNA-based	609:619	arg1	system					621:626	the lentiviral shRNA-based system	594:626	the lentiviral shRNA-based system to knockdown OGT	594:643	Here, we employed the lentiviral shRNA-based system to knockdown OGT to analyse the contribution of OGT in hepatoma cell proliferation and stem-like cell potential.
30677218	7	4	theme	hepatocellular	970:983	arg1	carcinoma					985:993	hepatocellular carcinoma	970:993	hepatocellular carcinoma	970:993	We found that the level of total O-GlcNAcylation or OGT protein was increased in hepatocellular carcinoma.
30677218	11	5	theme	cell	1502:1505	arg1	potential					1507:1515	stem-like cell potential	1492:1515	stem-like cell potential of hepatoma cell	1492:1532	High glucose promoted stem-like cell potential of hepatoma cell through OGT-eIF4E axis.
30677218	8	6	theme	stem-related	1110:1121	arg1	region					1149:1154	stem-related gene Sox2 5'-untranslated region	1110:1154	stem-related gene Sox2 5'-untranslated region	1110:1154	OGT activated stem-like cell potential in hepatoma through eukaryotic initiation factor 4E (eIF4E) which bound to stem-related gene Sox2 5'-untranslated region.
30677218	8	7	theme	gene	1123:1126	arg1	region					1149:1154	stem-related gene Sox2 5'-untranslated region	1110:1154	stem-related gene Sox2 5'-untranslated region	1110:1154	OGT activated stem-like cell potential in hepatoma through eukaryotic initiation factor 4E (eIF4E) which bound to stem-related gene Sox2 5'-untranslated region.
30677218	0	8	theme	factor	124:129	arg1	4E					131:132	eukaryotic initiation factor 4E	102:132	eukaryotic initiation factor 4E	102:132	O-GlcNAc transferase activates stem-like cell potential in hepatocarcinoma through O-GlcNAcylation of eukaryotic initiation factor 4E.
30677218	8	9	theme	5'-untranslated	1133:1147	arg1	region					1149:1154	stem-related gene Sox2 5'-untranslated region	1110:1154	stem-related gene Sox2 5'-untranslated region	1110:1154	OGT activated stem-like cell potential in hepatoma through eukaryotic initiation factor 4E (eIF4E) which bound to stem-related gene Sox2 5'-untranslated region.
30677218	5	10	theme	OGT	676:678	arg1	contribution					660:671	the contribution	656:671	the contribution of OGT in hepatoma cell proliferation and stem-like cell potential	656:738	Here, we employed the lentiviral shRNA-based system to knockdown OGT to analyse the contribution of OGT in hepatoma cell proliferation and stem-like cell potential.
30677218	13	11	theme	HCC	1729:1731	arg1	development					1733:1743	HCC development	1729:1743	HCC development	1729:1743	These results provide a mechanism of HCC development and a cue between the pathogenesis of HCC and high glucose condition.
30677218	6	12	theme	gene	808:811	arg1	expression					813:822	stem-related gene expression	795:822	stem-related gene expression	795:822	The sphere-forming assay and western blot analysis of stem-related gene expression were used to evaluate stem-like cell potential of hepatoma cell.
30677218	3	13	from	Dysregulation	340:352	arg1	response					376:383	response	376:383	response to high glucose or OGT expression	376:417	Dysregulation of O-GlcNAcylation in response to high glucose or OGT expression has been implicated in metabolic diseases and cancer.
30677218	0	14	theme	initiation	113:122	arg1	4E					131:132	eukaryotic initiation factor 4E	102:132	eukaryotic initiation factor 4E	102:132	O-GlcNAc transferase activates stem-like cell potential in hepatocarcinoma through O-GlcNAcylation of eukaryotic initiation factor 4E.
30677218	8	15	theme	Sox2	1128:1131	arg1	region					1149:1154	stem-related gene Sox2 5'-untranslated region	1110:1154	stem-related gene Sox2 5'-untranslated region	1110:1154	OGT activated stem-like cell potential in hepatoma through eukaryotic initiation factor 4E (eIF4E) which bound to stem-related gene Sox2 5'-untranslated region.
30677218	13	16	theme	development	1733:1743	arg1	mechanism					1716:1724	a mechanism	1714:1724	a mechanism of HCC development	1714:1743	These results provide a mechanism of HCC development and a cue between the pathogenesis of HCC and high glucose condition.
30677218	13	16	theme	development	1733:1743	arg1	cue					1751:1753	a cue	1749:1753	a cue between the pathogenesis of HCC and high glucose condition	1749:1812	These results provide a mechanism of HCC development and a cue between the pathogenesis of HCC and high glucose condition.
30677218	6	17	theme	stem-related	795:806	arg1	expression					813:822	stem-related gene expression	795:822	stem-related gene expression	795:822	The sphere-forming assay and western blot analysis of stem-related gene expression were used to evaluate stem-like cell potential of hepatoma cell.
30677218	6	18	used	used	829:832	arg2	analysis					783:790	The sphere-forming assay and western blot analysis	741:790	analysis	783:790	The sphere-forming assay and western blot analysis of stem-related gene expression were used to evaluate stem-like cell potential of hepatoma cell.
30677218	6	18	used	used	829:832	arg2	assay					760:764	The sphere-forming assay and western blot analysis	741:790	assay	760:764	The sphere-forming assay and western blot analysis of stem-related gene expression were used to evaluate stem-like cell potential of hepatoma cell.
30677218	8	19	theme	eukaryotic	1055:1064	arg1	eIF4E					1088:1092	eIF4E	1088:1092	eIF4E	1088:1092	OGT activated stem-like cell potential in hepatoma through eukaryotic initiation factor 4E (eIF4E) which bound to stem-related gene Sox2 5'-untranslated region.
30677218	8	19	theme	eukaryotic	1055:1064	arg1	4E					1084:1085	eukaryotic initiation factor 4E	1055:1085	eukaryotic initiation factor 4E (eIF4E) which bound to stem-related gene Sox2 5'-untranslated region	1055:1154	OGT activated stem-like cell potential in hepatoma through eukaryotic initiation factor 4E (eIF4E) which bound to stem-related gene Sox2 5'-untranslated region.
30677218	7	20	theme	OGT	941:943	arg1	protein					945:951	OGT protein	941:951	OGT protein	941:951	We found that the level of total O-GlcNAcylation or OGT protein was increased in hepatocellular carcinoma.
30677218	5	21	theme	cell	692:695	arg1	proliferation					697:709	hepatoma cell proliferation	683:709	hepatoma cell proliferation	683:709	Here, we employed the lentiviral shRNA-based system to knockdown OGT to analyse the contribution of OGT in hepatoma cell proliferation and stem-like cell potential.
30677218	5	22	theme	hepatoma	683:690	arg1	proliferation					697:709	hepatoma cell proliferation	683:709	hepatoma cell proliferation	683:709	Here, we employed the lentiviral shRNA-based system to knockdown OGT to analyse the contribution of OGT in hepatoma cell proliferation and stem-like cell potential.
30677218	7	23	theme	protein	945:951	arg1	level					907:911	the level	903:911	the level of total O-GlcNAcylation or OGT protein	903:951	We found that the level of total O-GlcNAcylation or OGT protein was increased in hepatocellular carcinoma.
30677218	0	24	theme	4E	131:132	arg1	O-GlcNAcylation					83:97	O-GlcNAcylation	83:97	O-GlcNAcylation of eukaryotic initiation factor 4E	83:132	O-GlcNAc transferase activates stem-like cell potential in hepatocarcinoma through O-GlcNAcylation of eukaryotic initiation factor 4E.
30677218	13	25	theme	condition	1804:1812	arg1	pathogenesis					1767:1778	the pathogenesis	1763:1778	the pathogenesis of HCC and high glucose condition	1763:1812	These results provide a mechanism of HCC development and a cue between the pathogenesis of HCC and high glucose condition.
30677218	6	26	theme	cell	883:886	arg1	potential					861:869	stem-like cell potential	846:869	stem-like cell potential of hepatoma cell	846:886	The sphere-forming assay and western blot analysis of stem-related gene expression were used to evaluate stem-like cell potential of hepatoma cell.
30677218	12	27	theme	eIF4E	1685:1689	arg1	O-GlcNAcylation					1666:1680	O-GlcNAcylation	1666:1680	O-GlcNAcylation of eIF4E	1666:1689	Collectively, our findings indicate that OGT promotes the stem-like cell potential of hepatoma cell through O-GlcNAcylation of eIF4E.
30677218	7	28	theme	O-GlcNAcylation	922:936	arg1	level					907:911	the level	903:911	the level of total O-GlcNAcylation or OGT protein	903:951	We found that the level of total O-GlcNAcylation or OGT protein was increased in hepatocellular carcinoma.
30677218	11	29	theme	hepatoma	1520:1527	arg1	cell					1529:1532	hepatoma cell	1520:1532	hepatoma cell	1520:1532	High glucose promoted stem-like cell potential of hepatoma cell through OGT-eIF4E axis.
30677218	10	30	from	Expression	1275:1284	arg1	hepatoma					1298:1305	hepatoma	1298:1305	hepatoma	1298:1305	Expression of eIF4E in hepatoma was determined by immunostaining in 232 HCC patients, and Kaplan-Meier survival analysis was used to determine the correlation of eIF4E expression with prognosis.
30677218	6	31	theme	hepatoma	874:881	arg1	cell					883:886	hepatoma cell	874:886	hepatoma cell	874:886	The sphere-forming assay and western blot analysis of stem-related gene expression were used to evaluate stem-like cell potential of hepatoma cell.
30677218	12	32	theme	cell	1626:1629	arg1	potential					1631:1639	the stem-like cell potential	1612:1639	the stem-like cell potential of hepatoma cell	1612:1656	Collectively, our findings indicate that OGT promotes the stem-like cell potential of hepatoma cell through O-GlcNAcylation of eIF4E.
30677218	6	33	theme	blot	778:781	arg1	analysis					783:790	The sphere-forming assay and western blot analysis	741:790	analysis	783:790	The sphere-forming assay and western blot analysis of stem-related gene expression were used to evaluate stem-like cell potential of hepatoma cell.
30677218	1	34	theme	reversible	196:205	arg1	O-GlcNAcylation					135:149	O-GlcNAcylation	135:149	O-GlcNAcylation catalysed by O-GlcNAc transferase (OGT)	135:189	O-GlcNAcylation catalysed by O-GlcNAc transferase (OGT) is a reversible post-translational modification.
30677218	1	34	theme	reversible	196:205	arg1	modification					226:237	a reversible post-translational modification	194:237	a reversible post-translational modification	194:237	O-GlcNAcylation catalysed by O-GlcNAc transferase (OGT) is a reversible post-translational modification.
30677218	0	35	theme	O-GlcNAc	0:7	arg1	transferase					9:19	O-GlcNAc transferase	0:19	O-GlcNAc transferase	0:19	O-GlcNAc transferase activates stem-like cell potential in hepatocarcinoma through O-GlcNAcylation of eukaryotic initiation factor 4E.
30677218	5	36	theme	stem-like	715:723	arg1	potential					730:738	stem-like cell potential	715:738	stem-like cell potential	715:738	Here, we employed the lentiviral shRNA-based system to knockdown OGT to analyse the contribution of OGT in hepatoma cell proliferation and stem-like cell potential.
30677218	10	37	used	used	1400:1403	arg2	analysis					1387:1394	Kaplan-Meier survival analysis	1365:1394	Kaplan-Meier survival analysis	1365:1394	Expression of eIF4E in hepatoma was determined by immunostaining in 232 HCC patients, and Kaplan-Meier survival analysis was used to determine the correlation of eIF4E expression with prognosis.
30677218	13	38	theme	glucose	1796:1802	arg1	condition					1804:1812	high glucose condition	1791:1812	high glucose condition	1791:1812	These results provide a mechanism of HCC development and a cue between the pathogenesis of HCC and high glucose condition.
30677218	6	39	theme	western	770:776	arg1	analysis					783:790	The sphere-forming assay and western blot analysis	741:790	analysis	783:790	The sphere-forming assay and western blot analysis of stem-related gene expression were used to evaluate stem-like cell potential of hepatoma cell.
30677218	1	40	theme	post-translational	207:224	arg1	O-GlcNAcylation					135:149	O-GlcNAcylation	135:149	O-GlcNAcylation catalysed by O-GlcNAc transferase (OGT)	135:189	O-GlcNAcylation catalysed by O-GlcNAc transferase (OGT) is a reversible post-translational modification.
30677218	1	40	theme	post-translational	207:224	arg1	modification					226:237	a reversible post-translational modification	194:237	a reversible post-translational modification	194:237	O-GlcNAcylation catalysed by O-GlcNAc transferase (OGT) is a reversible post-translational modification.
30677218	0	41	theme	stem-like	31:39	arg1	potential					46:54	stem-like cell potential	31:54	stem-like cell potential	31:54	O-GlcNAc transferase activates stem-like cell potential in hepatocarcinoma through O-GlcNAcylation of eukaryotic initiation factor 4E.
30677218	7	42	theme	total	916:920	arg1	O-GlcNAcylation					922:936	total O-GlcNAcylation	916:936	total O-GlcNAcylation	916:936	We found that the level of total O-GlcNAcylation or OGT protein was increased in hepatocellular carcinoma.
30677218	3	43	theme	metabolic	442:450	arg1	diseases					452:459	metabolic diseases	442:459	metabolic diseases	442:459	Dysregulation of O-GlcNAcylation in response to high glucose or OGT expression has been implicated in metabolic diseases and cancer.
30677218	10	44	theme	expression	1443:1452	arg1	correlation					1422:1432	the correlation	1418:1432	the correlation of eIF4E expression with prognosis	1418:1467	Expression of eIF4E in hepatoma was determined by immunostaining in 232 HCC patients, and Kaplan-Meier survival analysis was used to determine the correlation of eIF4E expression with prognosis.
30677218	13	45	theme	HCC	1783:1785	arg1	pathogenesis					1767:1778	the pathogenesis	1763:1778	the pathogenesis of HCC and high glucose condition	1763:1812	These results provide a mechanism of HCC development and a cue between the pathogenesis of HCC and high glucose condition.
30677218	10	46	from	immunostaining	1325:1338	arg1	patients					1351:1358	232 HCC patients	1343:1358	232 HCC patients	1343:1358	Expression of eIF4E in hepatoma was determined by immunostaining in 232 HCC patients, and Kaplan-Meier survival analysis was used to determine the correlation of eIF4E expression with prognosis.
30677218	2	47	theme	epigenetic	287:296	arg1	regulation					298:307	epigenetic regulation	287:307	epigenetic regulation	287:307	O-GlcNAcylation participates in transcription, epigenetic regulation, and intracellular signalling.
30677218	6	48	theme	sphere-forming	745:758	arg1	assay					760:764	The sphere-forming assay and western blot analysis	741:790	assay	760:764	The sphere-forming assay and western blot analysis of stem-related gene expression were used to evaluate stem-like cell potential of hepatoma cell.
30677218	0	49	theme	cell	41:44	arg1	potential					46:54	stem-like cell potential	31:54	stem-like cell potential	31:54	O-GlcNAc transferase activates stem-like cell potential in hepatocarcinoma through O-GlcNAcylation of eukaryotic initiation factor 4E.
30677218	11	50	theme	stem-like	1492:1500	arg1	potential					1507:1515	stem-like cell potential	1492:1515	stem-like cell potential of hepatoma cell	1492:1532	High glucose promoted stem-like cell potential of hepatoma cell through OGT-eIF4E axis.
30677218	12	51	theme	cell	1653:1656	arg1	potential					1631:1639	the stem-like cell potential	1612:1639	the stem-like cell potential of hepatoma cell	1612:1656	Collectively, our findings indicate that OGT promotes the stem-like cell potential of hepatoma cell through O-GlcNAcylation of eIF4E.
30677218	4	52	theme	hepatoma	531:538	arg1	development					540:550	hepatoma development	531:550	hepatoma development	531:550	However, the underlying mechanisms by which OGT regulates hepatoma development remain largely unknown.
30677218	6	53	theme	cell	856:859	arg1	potential					861:869	stem-like cell potential	846:869	stem-like cell potential of hepatoma cell	846:886	The sphere-forming assay and western blot analysis of stem-related gene expression were used to evaluate stem-like cell potential of hepatoma cell.
30677218	11	54	theme	cell	1529:1532	arg1	potential					1507:1515	stem-like cell potential	1492:1515	stem-like cell potential of hepatoma cell	1492:1532	High glucose promoted stem-like cell potential of hepatoma cell through OGT-eIF4E axis.
30677218	10	55	with	correlation	1422:1432	arg1	prognosis					1459:1467	prognosis	1459:1467	prognosis	1459:1467	Expression of eIF4E in hepatoma was determined by immunostaining in 232 HCC patients, and Kaplan-Meier survival analysis was used to determine the correlation of eIF4E expression with prognosis.
30677218	6	56	theme	stem-like	846:854	arg1	potential					861:869	stem-like cell potential	846:869	stem-like cell potential of hepatoma cell	846:886	The sphere-forming assay and western blot analysis of stem-related gene expression were used to evaluate stem-like cell potential of hepatoma cell.
30677218	12	57	theme	hepatoma	1644:1651	arg1	cell					1653:1656	hepatoma cell	1644:1656	hepatoma cell	1644:1656	Collectively, our findings indicate that OGT promotes the stem-like cell potential of hepatoma cell through O-GlcNAcylation of eIF4E.
30677218	11	58	theme	High	1470:1473	arg1	glucose					1475:1481	High glucose	1470:1481	High glucose	1470:1481	High glucose promoted stem-like cell potential of hepatoma cell through OGT-eIF4E axis.
30677218	4	59	theme	underlying	486:495	arg1	mechanisms					497:506	the underlying mechanisms	482:506	the underlying mechanisms by which OGT regulates hepatoma development	482:550	However, the underlying mechanisms by which OGT regulates hepatoma development remain largely unknown.
30677218	9	60	from	threonine	1203:1211	arg1	O-GlcNAcylation					1157:1171	O-GlcNAcylation	1157:1171	O-GlcNAcylation of eIF4E at threonine 168 and threonine 177	1157:1215	O-GlcNAcylation of eIF4E at threonine 168 and threonine 177 protected it from degradation through proteasome pathway.
30677218	5	61	theme	knockdown	631:639	arg1	OGT					641:643	knockdown OGT	631:643	knockdown OGT	631:643	Here, we employed the lentiviral shRNA-based system to knockdown OGT to analyse the contribution of OGT in hepatoma cell proliferation and stem-like cell potential.
30677218	5	62	from	contribution	660:671	arg1	potential					730:738	stem-like cell potential	715:738	stem-like cell potential	715:738	Here, we employed the lentiviral shRNA-based system to knockdown OGT to analyse the contribution of OGT in hepatoma cell proliferation and stem-like cell potential.
30677218	5	62	from	contribution	660:671	arg1	proliferation					697:709	hepatoma cell proliferation	683:709	hepatoma cell proliferation	683:709	Here, we employed the lentiviral shRNA-based system to knockdown OGT to analyse the contribution of OGT in hepatoma cell proliferation and stem-like cell potential.
30677218	8	63	theme	stem-like	1010:1018	arg1	potential					1025:1033	stem-like cell potential	1010:1033	stem-like cell potential	1010:1033	OGT activated stem-like cell potential in hepatoma through eukaryotic initiation factor 4E (eIF4E) which bound to stem-related gene Sox2 5'-untranslated region.
30677218	3	64	theme	O-GlcNAcylation	357:371	arg1	Dysregulation					340:352	Dysregulation	340:352	Dysregulation of O-GlcNAcylation in response to high glucose or OGT expression	340:417	Dysregulation of O-GlcNAcylation in response to high glucose or OGT expression has been implicated in metabolic diseases and cancer.
30677218	8	65	theme	initiation	1066:1075	arg1	eIF4E					1088:1092	eIF4E	1088:1092	eIF4E	1088:1092	OGT activated stem-like cell potential in hepatoma through eukaryotic initiation factor 4E (eIF4E) which bound to stem-related gene Sox2 5'-untranslated region.
30677218	8	65	theme	initiation	1066:1075	arg1	4E					1084:1085	eukaryotic initiation factor 4E	1055:1085	eukaryotic initiation factor 4E (eIF4E) which bound to stem-related gene Sox2 5'-untranslated region	1055:1154	OGT activated stem-like cell potential in hepatoma through eukaryotic initiation factor 4E (eIF4E) which bound to stem-related gene Sox2 5'-untranslated region.
30677218	2	66	theme	intracellular	314:326	arg1	signalling					328:337	intracellular signalling	314:337	intracellular signalling	314:337	O-GlcNAcylation participates in transcription, epigenetic regulation, and intracellular signalling.
30677218	8	67	theme	factor	1077:1082	arg1	eIF4E					1088:1092	eIF4E	1088:1092	eIF4E	1088:1092	OGT activated stem-like cell potential in hepatoma through eukaryotic initiation factor 4E (eIF4E) which bound to stem-related gene Sox2 5'-untranslated region.
30677218	8	67	theme	factor	1077:1082	arg1	4E					1084:1085	eukaryotic initiation factor 4E	1055:1085	eukaryotic initiation factor 4E (eIF4E) which bound to stem-related gene Sox2 5'-untranslated region	1055:1154	OGT activated stem-like cell potential in hepatoma through eukaryotic initiation factor 4E (eIF4E) which bound to stem-related gene Sox2 5'-untranslated region.
30677218	6	68	theme	expression	813:822	arg1	analysis					783:790	The sphere-forming assay and western blot analysis	741:790	analysis	783:790	The sphere-forming assay and western blot analysis of stem-related gene expression were used to evaluate stem-like cell potential of hepatoma cell.
30677218	6	68	theme	expression	813:822	arg1	assay					760:764	The sphere-forming assay and western blot analysis	741:790	assay	760:764	The sphere-forming assay and western blot analysis of stem-related gene expression were used to evaluate stem-like cell potential of hepatoma cell.
30677218	10	69	theme	eIF4E	1437:1441	arg1	expression					1443:1452	eIF4E expression	1437:1452	eIF4E expression	1437:1452	Expression of eIF4E in hepatoma was determined by immunostaining in 232 HCC patients, and Kaplan-Meier survival analysis was used to determine the correlation of eIF4E expression with prognosis.
30677218	12	70	theme	stem-like	1616:1624	arg1	potential					1631:1639	the stem-like cell potential	1612:1639	the stem-like cell potential of hepatoma cell	1612:1656	Collectively, our findings indicate that OGT promotes the stem-like cell potential of hepatoma cell through O-GlcNAcylation of eIF4E.
30677218	8	71	theme	cell	1020:1023	arg1	potential					1025:1033	stem-like cell potential	1010:1033	stem-like cell potential	1010:1033	OGT activated stem-like cell potential in hepatoma through eukaryotic initiation factor 4E (eIF4E) which bound to stem-related gene Sox2 5'-untranslated region.
30677218	9	72	theme	proteasome	1255:1264	arg1	pathway					1266:1272	proteasome pathway	1255:1272	proteasome pathway	1255:1272	O-GlcNAcylation of eIF4E at threonine 168 and threonine 177 protected it from degradation through proteasome pathway.
30677218	1	73	theme	O-GlcNAc	164:171	arg1	OGT					186:188	OGT	186:188	OGT	186:188	O-GlcNAcylation catalysed by O-GlcNAc transferase (OGT) is a reversible post-translational modification.
30677218	1	73	theme	O-GlcNAc	164:171	arg1	transferase					173:183	O-GlcNAc transferase	164:183	O-GlcNAc transferase (OGT)	164:189	O-GlcNAcylation catalysed by O-GlcNAc transferase (OGT) is a reversible post-translational modification.
30677218	10	74	theme	232	1343:1345	arg1	patients					1351:1358	232 HCC patients	1343:1358	232 HCC patients	1343:1358	Expression of eIF4E in hepatoma was determined by immunostaining in 232 HCC patients, and Kaplan-Meier survival analysis was used to determine the correlation of eIF4E expression with prognosis.
30677218	9	75	from	threonine	1185:1193	arg1	O-GlcNAcylation					1157:1171	O-GlcNAcylation	1157:1171	O-GlcNAcylation of eIF4E at threonine 168 and threonine 177	1157:1215	O-GlcNAcylation of eIF4E at threonine 168 and threonine 177 protected it from degradation through proteasome pathway.
30677218	10	76	theme	Kaplan-Meier	1365:1376	arg1	analysis					1387:1394	Kaplan-Meier survival analysis	1365:1394	Kaplan-Meier survival analysis	1365:1394	Expression of eIF4E in hepatoma was determined by immunostaining in 232 HCC patients, and Kaplan-Meier survival analysis was used to determine the correlation of eIF4E expression with prognosis.
30677218	10	77	theme	survival	1378:1385	arg1	analysis					1387:1394	Kaplan-Meier survival analysis	1365:1394	Kaplan-Meier survival analysis	1365:1394	Expression of eIF4E in hepatoma was determined by immunostaining in 232 HCC patients, and Kaplan-Meier survival analysis was used to determine the correlation of eIF4E expression with prognosis.
30677218	13	78	theme	high	1791:1794	arg1	condition					1804:1812	high glucose condition	1791:1812	high glucose condition	1791:1812	These results provide a mechanism of HCC development and a cue between the pathogenesis of HCC and high glucose condition.
30677218	10	79	theme	HCC	1347:1349	arg1	patients					1351:1358	232 HCC patients	1343:1358	232 HCC patients	1343:1358	Expression of eIF4E in hepatoma was determined by immunostaining in 232 HCC patients, and Kaplan-Meier survival analysis was used to determine the correlation of eIF4E expression with prognosis.
30677218	10	80	theme	eIF4E	1289:1293	arg1	Expression					1275:1284	Expression	1275:1284	Expression of eIF4E in hepatoma	1275:1305	Expression of eIF4E in hepatoma was determined by immunostaining in 232 HCC patients, and Kaplan-Meier survival analysis was used to determine the correlation of eIF4E expression with prognosis.
30677218	3	81	theme	OGT	404:406	arg1	expression					408:417	OGT expression	404:417	OGT expression	404:417	Dysregulation of O-GlcNAcylation in response to high glucose or OGT expression has been implicated in metabolic diseases and cancer.
30677218	5	82	theme	lentiviral	598:607	arg1	system					621:626	the lentiviral shRNA-based system	594:626	the lentiviral shRNA-based system to knockdown OGT	594:643	Here, we employed the lentiviral shRNA-based system to knockdown OGT to analyse the contribution of OGT in hepatoma cell proliferation and stem-like cell potential.
30677218	9	83	theme	eIF4E	1176:1180	arg1	O-GlcNAcylation					1157:1171	O-GlcNAcylation	1157:1171	O-GlcNAcylation of eIF4E at threonine 168 and threonine 177	1157:1215	O-GlcNAcylation of eIF4E at threonine 168 and threonine 177 protected it from degradation through proteasome pathway.
23580612	7	0	theme	O-GlcNAc	778:785	arg1	important					810:818	important	810:818	important	810:818	The O-GlcNAc modification sites are important for both Gadd45a repression and anchorage-independent survival.
23580612	7	0	theme	O-GlcNAc	778:785	arg1	sites					800:804	The O-GlcNAc modification sites	774:804	The O-GlcNAc modification sites	774:804	The O-GlcNAc modification sites are important for both Gadd45a repression and anchorage-independent survival.
23580612	6	1	theme	quantitative	664:675	arg1	reductions					677:686	quantitative reductions	664:686	quantitative reductions in Oct1 nuclear periphery-associated puncta, and a reduced association with lamin B1	664:771	Increased binding correlates with quantitative reductions in Oct1 nuclear periphery-associated puncta, and a reduced association with lamin B1.
23580612	7	2	theme	modification	787:798	arg1	important					810:818	important	810:818	important	810:818	The O-GlcNAc modification sites are important for both Gadd45a repression and anchorage-independent survival.
23580612	7	2	theme	modification	787:798	arg1	sites					800:804	The O-GlcNAc modification sites	774:804	The O-GlcNAc modification sites	774:804	The O-GlcNAc modification sites are important for both Gadd45a repression and anchorage-independent survival.
23580612	6	3	with	puncta	725:730	arg1	B1					770:771	lamin B1	764:771	lamin B1	764:771	Increased binding correlates with quantitative reductions in Oct1 nuclear periphery-associated puncta, and a reduced association with lamin B1.
23580612	3	4	link	O-linked	341:348	arg1	moieties					383:390	O-linked β-N-acetylglucosamine (O-GlcNAc) moieties	341:390	O-linked β-N-acetylglucosamine (O-GlcNAc) moieties	341:390	Here we show that Oct1 is modified by O-linked β-N-acetylglucosamine (O-GlcNAc) moieties.
23580612	3	5	theme	O-GlcNAc	373:380	arg1	moieties					383:390	O-linked β-N-acetylglucosamine (O-GlcNAc) moieties	341:390	O-linked β-N-acetylglucosamine (O-GlcNAc) moieties	341:390	Here we show that Oct1 is modified by O-linked β-N-acetylglucosamine (O-GlcNAc) moieties.
23580612	1	6	theme	Oct1	73:76	arg1	factor					92:97	The Oct1 transcription factor	69:97	The Oct1 transcription factor	69:97	The Oct1 transcription factor is a potent regulator of stress responses, metabolism, and tumorigenicity.
23580612	1	6	theme	Oct1	73:76	arg1	regulator					111:119	a potent regulator	102:119	a potent regulator of stress responses	102:139	The Oct1 transcription factor is a potent regulator of stress responses, metabolism, and tumorigenicity.
23580612	5	7	theme	overgrowth	503:512	arg1	conditions					514:523	anchorage-independent overgrowth conditions	481:523	anchorage-independent overgrowth conditions	481:523	Under anchorage-independent overgrowth conditions, Oct1 associates 3-fold more strongly with the Gadd45a promoter and mediates transcriptional repression.
23580612	3	8	theme	O-linked	341:348	arg1	moieties					383:390	O-linked β-N-acetylglucosamine (O-GlcNAc) moieties	341:390	O-linked β-N-acetylglucosamine (O-GlcNAc) moieties	341:390	Here we show that Oct1 is modified by O-linked β-N-acetylglucosamine (O-GlcNAc) moieties.
23580612	1	9	theme	transcription	78:90	arg1	factor					92:97	The Oct1 transcription factor	69:97	The Oct1 transcription factor	69:97	The Oct1 transcription factor is a potent regulator of stress responses, metabolism, and tumorigenicity.
23580612	1	9	theme	transcription	78:90	arg1	regulator					111:119	a potent regulator	102:119	a potent regulator of stress responses	102:139	The Oct1 transcription factor is a potent regulator of stress responses, metabolism, and tumorigenicity.
23580612	6	10	theme	lamin	764:768	arg1	B1					770:771	lamin B1	764:771	lamin B1	764:771	Increased binding correlates with quantitative reductions in Oct1 nuclear periphery-associated puncta, and a reduced association with lamin B1.
23580612	3	11	theme	β-N-acetylglucosamine	350:370	arg1	moieties					383:390	O-linked β-N-acetylglucosamine (O-GlcNAc) moieties	341:390	O-linked β-N-acetylglucosamine (O-GlcNAc) moieties	341:390	Here we show that Oct1 is modified by O-linked β-N-acetylglucosamine (O-GlcNAc) moieties.
23580612	2	12	theme	modifications	277:289	arg1	importance					257:266	importance	257:266	importance	257:266	Although Oct1 is regulated by phosphorylation and ubiquitination, the presence and importance of other modifications is unknown.
23580612	2	12	theme	modifications	277:289	arg1	presence					244:251	presence	244:251	presence	244:251	Although Oct1 is regulated by phosphorylation and ubiquitination, the presence and importance of other modifications is unknown.
23580612	9	13	theme	Gadd45a	1042:1048	arg1	activation					1050:1059	Gadd45a activation	1042:1059	Gadd45a activation under these conditions	1042:1082	The O-GlcNAc sites are also important for Gadd45a activation under these conditions.
23580612	5	14	theme	transcriptional	602:616	arg1	repression					618:627	transcriptional repression	602:627	transcriptional repression	602:627	Under anchorage-independent overgrowth conditions, Oct1 associates 3-fold more strongly with the Gadd45a promoter and mediates transcriptional repression.
23580612	6	15	theme	reduced	739:745	arg1	association					747:757	a reduced association	737:757	a reduced association with lamin B1	737:771	Increased binding correlates with quantitative reductions in Oct1 nuclear periphery-associated puncta, and a reduced association with lamin B1.
23580612	0	16	theme	transcription	26:38	arg1	activity					40:47	Oct1/Pou2f1 transcription activity	14:47	Oct1/Pou2f1 transcription activity	14:47	Regulation of Oct1/Pou2f1 transcription activity by O-GlcNAcylation.
23580612	1	17	theme	potent	104:109	arg1	factor					92:97	The Oct1 transcription factor	69:97	The Oct1 transcription factor	69:97	The Oct1 transcription factor is a potent regulator of stress responses, metabolism, and tumorigenicity.
23580612	1	17	theme	potent	104:109	arg1	regulator					111:119	a potent regulator	102:119	a potent regulator of stress responses	102:139	The Oct1 transcription factor is a potent regulator of stress responses, metabolism, and tumorigenicity.
23580612	8	18	theme	Gadd45a	980:986	arg1	activation					988:997	Gadd45a activation	980:997	Gadd45a activation	980:997	In contrast to chronic overgrowth conditions, following acute nutrient starvation Oct1 mediates Gadd45a activation.
23580612	0	19	theme	Oct1/Pou2f1	14:24	arg1	activity					40:47	Oct1/Pou2f1 transcription activity	14:47	Oct1/Pou2f1 transcription activity	14:47	Regulation of Oct1/Pou2f1 transcription activity by O-GlcNAcylation.
23580612	7	20	theme	anchorage-independent	852:872	arg1	survival					874:881	anchorage-independent survival	852:881	anchorage-independent survival	852:881	The O-GlcNAc modification sites are important for both Gadd45a repression and anchorage-independent survival.
23580612	6	21	with	association	747:757	arg1	B1					770:771	lamin B1	764:771	lamin B1	764:771	Increased binding correlates with quantitative reductions in Oct1 nuclear periphery-associated puncta, and a reduced association with lamin B1.
23580612	8	22	theme	nutrient	946:953	arg1	starvation					955:964	acute nutrient starvation	940:964	acute nutrient starvation	940:964	In contrast to chronic overgrowth conditions, following acute nutrient starvation Oct1 mediates Gadd45a activation.
23580612	10	23	theme	first	1102:1106	arg1	time					1108:1111	the first time	1098:1111	the first time	1098:1111	We also, for the first time, identify specific Oct1 ubiquitination sites.
23580612	8	24	theme	acute	940:944	arg1	starvation					955:964	acute nutrient starvation	940:964	acute nutrient starvation	940:964	In contrast to chronic overgrowth conditions, following acute nutrient starvation Oct1 mediates Gadd45a activation.
23580612	11	25	theme	stress	1215:1220	arg1	signals					1222:1228	metabolic and stress signals	1201:1228	signals	1222:1228	The findings suggest that Oct1 integrates metabolic and stress signals via O-GlcNAc modification to regulate target gene activity.
23580612	5	26	theme	anchorage-independent	481:501	arg1	conditions					514:523	anchorage-independent overgrowth conditions	481:523	anchorage-independent overgrowth conditions	481:523	Under anchorage-independent overgrowth conditions, Oct1 associates 3-fold more strongly with the Gadd45a promoter and mediates transcriptional repression.
23580612	2	27	dep	presence	244:251	arg1	the					240:242	the	240:242	the	240:242	Although Oct1 is regulated by phosphorylation and ubiquitination, the presence and importance of other modifications is unknown.
23580612	0	28	theme	activity	40:47	arg1	Regulation					0:9	Regulation	0:9	Regulation of Oct1/Pou2f1 transcription activity by O-GlcNAcylation.	0:67	Regulation of Oct1/Pou2f1 transcription activity by O-GlcNAcylation.
23580612	4	29	theme	human	463:467	arg1	Oct1					469:472	human Oct1	463:472	human Oct1	463:472	We map two sites of O-GlcNAcylation at positions T255 and S728 within human Oct1.
23580612	6	30	theme	Increased	630:638	arg1	binding					640:646	Increased binding	630:646	Increased binding	630:646	Increased binding correlates with quantitative reductions in Oct1 nuclear periphery-associated puncta, and a reduced association with lamin B1.
23580612	11	31	theme	metabolic	1201:1209	arg1	signals					1222:1228	metabolic and stress signals	1201:1228	signals	1222:1228	The findings suggest that Oct1 integrates metabolic and stress signals via O-GlcNAc modification to regulate target gene activity.
23580612	8	32	theme	overgrowth	907:916	arg1	conditions					918:927	chronic overgrowth conditions	899:927	chronic overgrowth conditions	899:927	In contrast to chronic overgrowth conditions, following acute nutrient starvation Oct1 mediates Gadd45a activation.
23580612	3	33	mod	modified	329:336	arg1	Oct1					321:324	Oct1	321:324	Oct1	321:324	Here we show that Oct1 is modified by O-linked β-N-acetylglucosamine (O-GlcNAc) moieties.
23580612	3	33	mod	modified	329:336	arg3	moieties					383:390	O-linked β-N-acetylglucosamine (O-GlcNAc) moieties	341:390	O-linked β-N-acetylglucosamine (O-GlcNAc) moieties	341:390	Here we show that Oct1 is modified by O-linked β-N-acetylglucosamine (O-GlcNAc) moieties.
23580612	10	34	theme	ubiquitination	1137:1150	arg1	sites					1152:1156	specific Oct1 ubiquitination sites	1123:1156	specific Oct1 ubiquitination sites	1123:1156	We also, for the first time, identify specific Oct1 ubiquitination sites.
23580612	10	35	theme	Oct1	1132:1135	arg1	sites					1152:1156	specific Oct1 ubiquitination sites	1123:1156	specific Oct1 ubiquitination sites	1123:1156	We also, for the first time, identify specific Oct1 ubiquitination sites.
23580612	5	36	theme	Gadd45a	572:578	arg1	promoter					580:587	the Gadd45a promoter	568:587	the Gadd45a promoter	568:587	Under anchorage-independent overgrowth conditions, Oct1 associates 3-fold more strongly with the Gadd45a promoter and mediates transcriptional repression.
23580612	1	37	theme	stress	124:129	arg1	responses					131:139	stress responses	124:139	stress responses	124:139	The Oct1 transcription factor is a potent regulator of stress responses, metabolism, and tumorigenicity.
23580612	7	38	theme	Gadd45a	829:835	arg1	repression					837:846	Gadd45a repression	829:846	Gadd45a repression	829:846	The O-GlcNAc modification sites are important for both Gadd45a repression and anchorage-independent survival.
23580612	4	39	theme	O-GlcNAcylation	413:427	arg1	O-GlcNAcylation					413:427	O-GlcNAcylation	413:427	O-GlcNAcylation	413:427	We map two sites of O-GlcNAcylation at positions T255 and S728 within human Oct1.
23580612	4	39	theme	O-GlcNAcylation	413:427	arg1	sites					404:408	two sites	400:408	two sites of O-GlcNAcylation	400:427	We map two sites of O-GlcNAcylation at positions T255 and S728 within human Oct1.
23580612	2	40	theme	other	271:275	arg1	modifications					277:289	other modifications	271:289	other modifications	271:289	Although Oct1 is regulated by phosphorylation and ubiquitination, the presence and importance of other modifications is unknown.
23580612	8	41	dep	conditions	918:927	arg1	contrast					887:894	contrast	887:894	contrast	887:894	In contrast to chronic overgrowth conditions, following acute nutrient starvation Oct1 mediates Gadd45a activation.
23580612	1	42	theme	responses	131:139	arg1	tumorigenicity					158:171	tumorigenicity	158:171	tumorigenicity	158:171	The Oct1 transcription factor is a potent regulator of stress responses, metabolism, and tumorigenicity.
23580612	1	42	theme	responses	131:139	arg1	factor					92:97	The Oct1 transcription factor	69:97	The Oct1 transcription factor	69:97	The Oct1 transcription factor is a potent regulator of stress responses, metabolism, and tumorigenicity.
23580612	1	42	theme	responses	131:139	arg1	metabolism					142:151	metabolism	142:151	metabolism	142:151	The Oct1 transcription factor is a potent regulator of stress responses, metabolism, and tumorigenicity.
23580612	1	42	theme	responses	131:139	arg1	regulator					111:119	a potent regulator	102:119	a potent regulator of stress responses	102:139	The Oct1 transcription factor is a potent regulator of stress responses, metabolism, and tumorigenicity.
23580612	6	43	theme	periphery-associated	704:723	arg1	puncta					725:730	Oct1 nuclear periphery-associated puncta	691:730	Oct1 nuclear periphery-associated puncta	691:730	Increased binding correlates with quantitative reductions in Oct1 nuclear periphery-associated puncta, and a reduced association with lamin B1.
23580612	11	44	theme	target	1268:1273	arg1	activity					1280:1287	target gene activity	1268:1287	target gene activity	1268:1287	The findings suggest that Oct1 integrates metabolic and stress signals via O-GlcNAc modification to regulate target gene activity.
23580612	10	45	theme	specific	1123:1130	arg1	sites					1152:1156	specific Oct1 ubiquitination sites	1123:1156	specific Oct1 ubiquitination sites	1123:1156	We also, for the first time, identify specific Oct1 ubiquitination sites.
23580612	11	46	theme	gene	1275:1278	arg1	activity					1280:1287	target gene activity	1268:1287	target gene activity	1268:1287	The findings suggest that Oct1 integrates metabolic and stress signals via O-GlcNAc modification to regulate target gene activity.
23580612	11	47	theme	O-GlcNAc	1234:1241	arg1	modification					1243:1254	O-GlcNAc modification	1234:1254	O-GlcNAc modification	1234:1254	The findings suggest that Oct1 integrates metabolic and stress signals via O-GlcNAc modification to regulate target gene activity.
23580612	6	48	theme	nuclear	696:702	arg1	puncta					725:730	Oct1 nuclear periphery-associated puncta	691:730	Oct1 nuclear periphery-associated puncta	691:730	Increased binding correlates with quantitative reductions in Oct1 nuclear periphery-associated puncta, and a reduced association with lamin B1.
23580612	4	49	dep	positions	432:440	arg1	positions					432:440	positions T255 and S728	432:454	positions T255 and S728 within human Oct1	432:472	We map two sites of O-GlcNAcylation at positions T255 and S728 within human Oct1.
23580612	4	49	dep	positions	432:440	arg1	S728					451:454	S728	451:454	S728	451:454	We map two sites of O-GlcNAcylation at positions T255 and S728 within human Oct1.
23580612	4	49	dep	positions	432:440	arg1	T255					442:445	T255	442:445	T255	442:445	We map two sites of O-GlcNAcylation at positions T255 and S728 within human Oct1.
23580612	9	50	theme	O-GlcNAc	1004:1011	arg1	sites					1013:1017	The O-GlcNAc sites	1000:1017	The O-GlcNAc sites	1000:1017	The O-GlcNAc sites are also important for Gadd45a activation under these conditions.
23580612	9	50	theme	O-GlcNAc	1004:1011	arg1	important					1028:1036	important	1028:1036	important	1028:1036	The O-GlcNAc sites are also important for Gadd45a activation under these conditions.
23580612	8	51	theme	chronic	899:905	arg1	conditions					918:927	chronic overgrowth conditions	899:927	chronic overgrowth conditions	899:927	In contrast to chronic overgrowth conditions, following acute nutrient starvation Oct1 mediates Gadd45a activation.
23580612	6	52	theme	Oct1	691:694	arg1	puncta					725:730	Oct1 nuclear periphery-associated puncta	691:730	Oct1 nuclear periphery-associated puncta	691:730	Increased binding correlates with quantitative reductions in Oct1 nuclear periphery-associated puncta, and a reduced association with lamin B1.
23580612	6	53	from	reductions	677:686	arg1	association					747:757	a reduced association	737:757	a reduced association with lamin B1	737:771	Increased binding correlates with quantitative reductions in Oct1 nuclear periphery-associated puncta, and a reduced association with lamin B1.
23580612	6	53	from	reductions	677:686	arg1	puncta					725:730	Oct1 nuclear periphery-associated puncta	691:730	Oct1 nuclear periphery-associated puncta	691:730	Increased binding correlates with quantitative reductions in Oct1 nuclear periphery-associated puncta, and a reduced association with lamin B1.
31410220	7	0	theme	poor	1062:1065	arg1	survival					1067:1074	poor survival	1062:1074	poor survival	1062:1074	Results: High CD36 expression is a predictor of poor survival and promotes metastasis of GC cells and the use of neutralizing antibodies to block CD36 inhibits GC metastasis in mice.
31410220	5	1	used	used	646:649	arg2	assay					620:624	Transwell assay	610:624	Transwell assay	610:624	Transwell assay and xenografts were used to assess cell metastasis abilities in vitro and in vivo after indicated treatment.
31410220	5	1	used	used	646:649	arg2	xenografts					630:639	xenografts	630:639	xenografts	630:639	Transwell assay and xenografts were used to assess cell metastasis abilities in vitro and in vivo after indicated treatment.
31410220	6	2	theme	O-GlcNAcylation	828:842	arg1	level					844:848	O-GlcNAcylation level	828:848	O-GlcNAcylation level	828:848	Luciferase reporter assay was carried out to evaluate the changes in signaling pathways when O-GlcNAcylation level was increased in GC cells and in vitro O-GlcNAcylation assay was utilized for wild and mutant types of CD36 protein to explore the potential O-GlcNAcylation sites.
31410220	4	3	theme	CD36	547:550	arg1	expression					552:561	CD36 expression	547:561	CD36 expression in gastric cancer (GC) tissues and cell lines	547:607	Methods: RT-qPCR, FACS analysis, immunoblotting and immunohistochemistry, as well as retrieving TCGA database, were carried out to quantitate CD36 expression in gastric cancer (GC) tissues and cell lines.
31410220	3	4	theme	molecular	315:323	arg1	basis					325:329	the molecular basis	311:329	the molecular basis of the fatty acid (FA)-induced upregulation of CD36	311:381	However, the molecular basis of the fatty acid (FA)-induced upregulation of CD36 has remained unclear.
31410220	6	5	theme	GC	867:868	arg1	cells					870:874	GC cells	867:874	GC cells	867:874	Luciferase reporter assay was carried out to evaluate the changes in signaling pathways when O-GlcNAcylation level was increased in GC cells and in vitro O-GlcNAcylation assay was utilized for wild and mutant types of CD36 protein to explore the potential O-GlcNAcylation sites.
31410220	7	6	theme	survival	1067:1074	arg1	Results					1014:1020	Results	1014:1020	Results: High CD36 expression is a predictor of poor survival and promotes metastasis of GC cells and the use of neutralizing antibodies to block CD36 inhibits GC metastasis in mice.	1014:1195	Results: High CD36 expression is a predictor of poor survival and promotes metastasis of GC cells and the use of neutralizing antibodies to block CD36 inhibits GC metastasis in mice.
31410220	7	6	theme	survival	1067:1074	arg1	expression					1033:1042	High CD36 expression	1023:1042	High CD36 expression	1023:1042	Results: High CD36 expression is a predictor of poor survival and promotes metastasis of GC cells and the use of neutralizing antibodies to block CD36 inhibits GC metastasis in mice.
31410220	7	6	theme	survival	1067:1074	arg1	predictor					1049:1057	a predictor	1047:1057	a predictor of poor survival	1047:1074	Results: High CD36 expression is a predictor of poor survival and promotes metastasis of GC cells and the use of neutralizing antibodies to block CD36 inhibits GC metastasis in mice.
31410220	8	7	theme	GC	1246:1247	arg1	cells					1249:1253	GC cells	1246:1253	GC cells	1246:1253	FA or a HFD promotes the metastatic potential of GC cells by upregulating CD36 via increasing the O-GlcNAcylation level.
31410220	7	8	theme	GC	1103:1104	arg1	cells					1106:1110	GC cells	1103:1110	GC cells	1103:1110	Results: High CD36 expression is a predictor of poor survival and promotes metastasis of GC cells and the use of neutralizing antibodies to block CD36 inhibits GC metastasis in mice.
31410220	3	9	dep	-induced	353:360	arg1	acid					344:347	fatty acid	338:347	fatty acid	338:347	However, the molecular basis of the fatty acid (FA)-induced upregulation of CD36 has remained unclear.
31410220	7	10	from	metastasis	1177:1186	arg1	mice					1191:1194	mice	1191:1194	mice	1191:1194	Results: High CD36 expression is a predictor of poor survival and promotes metastasis of GC cells and the use of neutralizing antibodies to block CD36 inhibits GC metastasis in mice.
31410220	2	11	theme	CD36-dependent	279:292	arg1	manner					294:299	a CD36-dependent manner	277:299	a CD36-dependent manner	277:299	Recently, a high-fat diet was shown to specifically promote the metastatic potential of specific cancer cells in a CD36-dependent manner.
31410220	6	12	theme	mutant	937:942	arg1	types					944:948	wild and mutant types	928:948	wild and mutant types of CD36 protein	928:964	Luciferase reporter assay was carried out to evaluate the changes in signaling pathways when O-GlcNAcylation level was increased in GC cells and in vitro O-GlcNAcylation assay was utilized for wild and mutant types of CD36 protein to explore the potential O-GlcNAcylation sites.
31410220	4	13	from	expression	552:561	arg1	tissues					586:592	gastric cancer (GC) tissues	566:592	gastric cancer (GC) tissues	566:592	Methods: RT-qPCR, FACS analysis, immunoblotting and immunohistochemistry, as well as retrieving TCGA database, were carried out to quantitate CD36 expression in gastric cancer (GC) tissues and cell lines.
31410220	4	13	from	expression	552:561	arg1	lines					603:607	cell lines	598:607	cell lines	598:607	Methods: RT-qPCR, FACS analysis, immunoblotting and immunohistochemistry, as well as retrieving TCGA database, were carried out to quantitate CD36 expression in gastric cancer (GC) tissues and cell lines.
31410220	0	14	theme	Fatty	0:4	arg1	expression					24:33	Fatty acid-induced CD36 expression	0:33	Fatty acid-induced CD36 expression via O-GlcNAcylation	0:53	Fatty acid-induced CD36 expression via O-GlcNAcylation drives gastric cancer metastasis.
31410220	9	15	theme	uptake	1442:1447	arg1	activity					1449:1456	its FA uptake activity	1435:1456	its FA uptake activity	1435:1456	Increased O-GlcNAcylation levels promote the transcription of CD36 by activating the NF-κB pathway and also increase its FA uptake activity by directly modifying CD36 at S468 and T470.
31410220	9	16	theme	O-GlcNAcylation	1328:1342	arg1	levels					1344:1349	Increased O-GlcNAcylation levels	1318:1349	Increased O-GlcNAcylation levels	1318:1349	Increased O-GlcNAcylation levels promote the transcription of CD36 by activating the NF-κB pathway and also increase its FA uptake activity by directly modifying CD36 at S468 and T470.
31410220	7	17	theme	cells	1106:1110	arg1	metastasis					1089:1098	metastasis	1089:1098	metastasis of GC cells	1089:1110	Results: High CD36 expression is a predictor of poor survival and promotes metastasis of GC cells and the use of neutralizing antibodies to block CD36 inhibits GC metastasis in mice.
31410220	10	18	theme	GC	1687:1688	arg1	metastasis					1690:1699	GC metastasis	1687:1699	GC metastasis	1687:1699	Conclusion: FA-induced hyper-O-GlcNAcylation promotes the transcription and function of CD36 by activating the NF-κB pathway and directly modifying CD36 at S468 and T470, which drives GC metastasis.
31410220	8	19	theme	cells	1249:1253	arg1	potential					1233:1241	the metastatic potential	1218:1241	the metastatic potential of GC cells	1218:1253	FA or a HFD promotes the metastatic potential of GC cells by upregulating CD36 via increasing the O-GlcNAcylation level.
31410220	3	20	theme	fatty	338:342	arg1	acid					344:347	fatty acid	338:347	fatty acid	338:347	However, the molecular basis of the fatty acid (FA)-induced upregulation of CD36 has remained unclear.
31410220	1	21	with	patients	133:140	arg1	cancer					156:161	advanced cancer	147:161	advanced cancer	147:161	Metastasis is the primary cause of death in patients with advanced cancer.
31410220	6	22	theme	reporter	746:753	arg1	assay					755:759	Luciferase reporter assay	735:759	Luciferase reporter assay	735:759	Luciferase reporter assay was carried out to evaluate the changes in signaling pathways when O-GlcNAcylation level was increased in GC cells and in vitro O-GlcNAcylation assay was utilized for wild and mutant types of CD36 protein to explore the potential O-GlcNAcylation sites.
31410220	2	23	theme	cells	268:272	arg1	potential					239:247	the metastatic potential	224:247	the metastatic potential of specific cancer cells	224:272	Recently, a high-fat diet was shown to specifically promote the metastatic potential of specific cancer cells in a CD36-dependent manner.
31410220	0	24	theme	acid-induced	6:17	arg1	expression					24:33	Fatty acid-induced CD36 expression	0:33	Fatty acid-induced CD36 expression via O-GlcNAcylation	0:53	Fatty acid-induced CD36 expression via O-GlcNAcylation drives gastric cancer metastasis.
31410220	5	25	theme	indicated	714:722	arg1	treatment					724:732	indicated treatment	714:732	indicated treatment	714:732	Transwell assay and xenografts were used to assess cell metastasis abilities in vitro and in vivo after indicated treatment.
31410220	7	26	theme	CD36	1028:1031	arg1	Results					1014:1020	Results	1014:1020	Results: High CD36 expression is a predictor of poor survival and promotes metastasis of GC cells and the use of neutralizing antibodies to block CD36 inhibits GC metastasis in mice.	1014:1195	Results: High CD36 expression is a predictor of poor survival and promotes metastasis of GC cells and the use of neutralizing antibodies to block CD36 inhibits GC metastasis in mice.
31410220	7	26	theme	CD36	1028:1031	arg1	expression					1033:1042	High CD36 expression	1023:1042	High CD36 expression	1023:1042	Results: High CD36 expression is a predictor of poor survival and promotes metastasis of GC cells and the use of neutralizing antibodies to block CD36 inhibits GC metastasis in mice.
31410220	7	26	theme	CD36	1028:1031	arg1	predictor					1049:1057	a predictor	1047:1057	a predictor of poor survival	1047:1074	Results: High CD36 expression is a predictor of poor survival and promotes metastasis of GC cells and the use of neutralizing antibodies to block CD36 inhibits GC metastasis in mice.
31410220	6	27	theme	Luciferase	735:744	arg1	assay					755:759	Luciferase reporter assay	735:759	Luciferase reporter assay	735:759	Luciferase reporter assay was carried out to evaluate the changes in signaling pathways when O-GlcNAcylation level was increased in GC cells and in vitro O-GlcNAcylation assay was utilized for wild and mutant types of CD36 protein to explore the potential O-GlcNAcylation sites.
31410220	3	28	theme	upregulation	362:373	arg1	basis					325:329	the molecular basis	311:329	the molecular basis of the fatty acid (FA)-induced upregulation of CD36	311:381	However, the molecular basis of the fatty acid (FA)-induced upregulation of CD36 has remained unclear.
31410220	6	29	theme	wild	928:931	arg1	types					944:948	wild and mutant types	928:948	wild and mutant types of CD36 protein	928:964	Luciferase reporter assay was carried out to evaluate the changes in signaling pathways when O-GlcNAcylation level was increased in GC cells and in vitro O-GlcNAcylation assay was utilized for wild and mutant types of CD36 protein to explore the potential O-GlcNAcylation sites.
31410220	10	30	dep	transcription	1561:1573	arg1	the					1557:1559	the	1557:1559	the	1557:1559	Conclusion: FA-induced hyper-O-GlcNAcylation promotes the transcription and function of CD36 by activating the NF-κB pathway and directly modifying CD36 at S468 and T470, which drives GC metastasis.
31410220	6	31	dep	in	880:881	arg1	vitro					883:887	vitro	883:887	vitro	883:887	Luciferase reporter assay was carried out to evaluate the changes in signaling pathways when O-GlcNAcylation level was increased in GC cells and in vitro O-GlcNAcylation assay was utilized for wild and mutant types of CD36 protein to explore the potential O-GlcNAcylation sites.
31410220	6	32	from	changes	793:799	arg1	pathways					814:821	signaling pathways	804:821	signaling pathways	804:821	Luciferase reporter assay was carried out to evaluate the changes in signaling pathways when O-GlcNAcylation level was increased in GC cells and in vitro O-GlcNAcylation assay was utilized for wild and mutant types of CD36 protein to explore the potential O-GlcNAcylation sites.
31410220	9	33	theme	FA	1439:1440	arg1	activity					1449:1456	its FA uptake activity	1435:1456	its FA uptake activity	1435:1456	Increased O-GlcNAcylation levels promote the transcription of CD36 by activating the NF-κB pathway and also increase its FA uptake activity by directly modifying CD36 at S468 and T470.
31410220	1	34	theme	primary	107:113	arg1	Metastasis					89:98	Metastasis	89:98	Metastasis	89:98	Metastasis is the primary cause of death in patients with advanced cancer.
31410220	1	34	theme	primary	107:113	arg1	cause					115:119	the primary cause	103:119	the primary cause of death in patients with advanced cancer	103:161	Metastasis is the primary cause of death in patients with advanced cancer.
31410220	9	35	theme	NF-κB	1403:1407	arg1	pathway					1409:1415	the NF-κB pathway	1399:1415	the NF-κB pathway	1399:1415	Increased O-GlcNAcylation levels promote the transcription of CD36 by activating the NF-κB pathway and also increase its FA uptake activity by directly modifying CD36 at S468 and T470.
31410220	0	36	theme	CD36	19:22	arg1	expression					24:33	Fatty acid-induced CD36 expression	0:33	Fatty acid-induced CD36 expression via O-GlcNAcylation	0:53	Fatty acid-induced CD36 expression via O-GlcNAcylation drives gastric cancer metastasis.
31410220	7	37	theme	High	1023:1026	arg1	Results					1014:1020	Results	1014:1020	Results: High CD36 expression is a predictor of poor survival and promotes metastasis of GC cells and the use of neutralizing antibodies to block CD36 inhibits GC metastasis in mice.	1014:1195	Results: High CD36 expression is a predictor of poor survival and promotes metastasis of GC cells and the use of neutralizing antibodies to block CD36 inhibits GC metastasis in mice.
31410220	7	37	theme	High	1023:1026	arg1	expression					1033:1042	High CD36 expression	1023:1042	High CD36 expression	1023:1042	Results: High CD36 expression is a predictor of poor survival and promotes metastasis of GC cells and the use of neutralizing antibodies to block CD36 inhibits GC metastasis in mice.
31410220	7	37	theme	High	1023:1026	arg1	predictor					1049:1057	a predictor	1047:1057	a predictor of poor survival	1047:1074	Results: High CD36 expression is a predictor of poor survival and promotes metastasis of GC cells and the use of neutralizing antibodies to block CD36 inhibits GC metastasis in mice.
31410220	2	38	theme	high-fat	176:183	arg1	diet					185:188	a high-fat diet	174:188	a high-fat diet	174:188	Recently, a high-fat diet was shown to specifically promote the metastatic potential of specific cancer cells in a CD36-dependent manner.
31410220	8	39	theme	O-GlcNAcylation	1295:1309	arg1	level					1311:1315	the O-GlcNAcylation level	1291:1315	the O-GlcNAcylation level	1291:1315	FA or a HFD promotes the metastatic potential of GC cells by upregulating CD36 via increasing the O-GlcNAcylation level.
31410220	6	40	theme	O-GlcNAcylation	991:1005	arg1	sites					1007:1011	the potential O-GlcNAcylation sites	977:1011	the potential O-GlcNAcylation sites	977:1011	Luciferase reporter assay was carried out to evaluate the changes in signaling pathways when O-GlcNAcylation level was increased in GC cells and in vitro O-GlcNAcylation assay was utilized for wild and mutant types of CD36 protein to explore the potential O-GlcNAcylation sites.
31410220	7	41	theme	neutralizing	1127:1138	arg1	antibodies					1140:1149	neutralizing antibodies	1127:1149	neutralizing antibodies	1127:1149	Results: High CD36 expression is a predictor of poor survival and promotes metastasis of GC cells and the use of neutralizing antibodies to block CD36 inhibits GC metastasis in mice.
31410220	5	42	theme	cell	661:664	arg1	abilities					677:685	cell metastasis abilities	661:685	cell metastasis abilities	661:685	Transwell assay and xenografts were used to assess cell metastasis abilities in vitro and in vivo after indicated treatment.
31410220	6	43	theme	potential	981:989	arg1	sites					1007:1011	the potential O-GlcNAcylation sites	977:1011	the potential O-GlcNAcylation sites	977:1011	Luciferase reporter assay was carried out to evaluate the changes in signaling pathways when O-GlcNAcylation level was increased in GC cells and in vitro O-GlcNAcylation assay was utilized for wild and mutant types of CD36 protein to explore the potential O-GlcNAcylation sites.
31410220	2	44	theme	metastatic	228:237	arg1	potential					239:247	the metastatic potential	224:247	the metastatic potential of specific cancer cells	224:272	Recently, a high-fat diet was shown to specifically promote the metastatic potential of specific cancer cells in a CD36-dependent manner.
31410220	10	45	theme	CD36	1591:1594	arg1	function					1579:1586	function	1579:1586	function	1579:1586	Conclusion: FA-induced hyper-O-GlcNAcylation promotes the transcription and function of CD36 by activating the NF-κB pathway and directly modifying CD36 at S468 and T470, which drives GC metastasis.
31410220	10	45	theme	CD36	1591:1594	arg1	transcription					1561:1573	transcription	1561:1573	transcription	1561:1573	Conclusion: FA-induced hyper-O-GlcNAcylation promotes the transcription and function of CD36 by activating the NF-κB pathway and directly modifying CD36 at S468 and T470, which drives GC metastasis.
31410220	4	46	theme	cell	598:601	arg1	lines					603:607	cell lines	598:607	cell lines	598:607	Methods: RT-qPCR, FACS analysis, immunoblotting and immunohistochemistry, as well as retrieving TCGA database, were carried out to quantitate CD36 expression in gastric cancer (GC) tissues and cell lines.
31410220	9	47	theme	CD36	1380:1383	arg1	transcription					1363:1375	the transcription	1359:1375	the transcription of CD36	1359:1383	Increased O-GlcNAcylation levels promote the transcription of CD36 by activating the NF-κB pathway and also increase its FA uptake activity by directly modifying CD36 at S468 and T470.
31410220	4	48	theme	TCGA	501:504	arg1	database					506:513	retrieving TCGA database	490:513	retrieving TCGA database	490:513	Methods: RT-qPCR, FACS analysis, immunoblotting and immunohistochemistry, as well as retrieving TCGA database, were carried out to quantitate CD36 expression in gastric cancer (GC) tissues and cell lines.
31410220	5	49	theme	metastasis	666:675	arg1	abilities					677:685	cell metastasis abilities	661:685	cell metastasis abilities	661:685	Transwell assay and xenografts were used to assess cell metastasis abilities in vitro and in vivo after indicated treatment.
31410220	6	50	theme	signaling	804:812	arg1	pathways					814:821	signaling pathways	804:821	signaling pathways	804:821	Luciferase reporter assay was carried out to evaluate the changes in signaling pathways when O-GlcNAcylation level was increased in GC cells and in vitro O-GlcNAcylation assay was utilized for wild and mutant types of CD36 protein to explore the potential O-GlcNAcylation sites.
31410220	6	51	theme	protein	958:964	arg1	types					944:948	wild and mutant types	928:948	wild and mutant types of CD36 protein	928:964	Luciferase reporter assay was carried out to evaluate the changes in signaling pathways when O-GlcNAcylation level was increased in GC cells and in vitro O-GlcNAcylation assay was utilized for wild and mutant types of CD36 protein to explore the potential O-GlcNAcylation sites.
31410220	10	52	theme	NF-κB	1614:1618	arg1	pathway					1620:1626	the NF-κB pathway	1610:1626	the NF-κB pathway	1610:1626	Conclusion: FA-induced hyper-O-GlcNAcylation promotes the transcription and function of CD36 by activating the NF-κB pathway and directly modifying CD36 at S468 and T470, which drives GC metastasis.
31410220	0	53	theme	gastric	62:68	arg1	metastasis					77:86	gastric cancer metastasis	62:86	gastric cancer metastasis	62:86	Fatty acid-induced CD36 expression via O-GlcNAcylation drives gastric cancer metastasis.
31410220	4	54	theme	retrieving	490:499	arg1	database					506:513	retrieving TCGA database	490:513	retrieving TCGA database	490:513	Methods: RT-qPCR, FACS analysis, immunoblotting and immunohistochemistry, as well as retrieving TCGA database, were carried out to quantitate CD36 expression in gastric cancer (GC) tissues and cell lines.
31410220	4	55	theme	FACS	423:426	arg1	analysis					428:435	FACS analysis	423:435	FACS analysis	423:435	Methods: RT-qPCR, FACS analysis, immunoblotting and immunohistochemistry, as well as retrieving TCGA database, were carried out to quantitate CD36 expression in gastric cancer (GC) tissues and cell lines.
31410220	3	56	theme	CD36	378:381	arg1	upregulation					362:373	the fatty acid (FA)-induced upregulation	334:373	the fatty acid (FA)-induced upregulation of CD36	334:381	However, the molecular basis of the fatty acid (FA)-induced upregulation of CD36 has remained unclear.
31410220	6	57	used	utilized	915:922	arg2	assay					905:909	in vitro O-GlcNAcylation assay	880:909	in vitro O-GlcNAcylation assay	880:909	Luciferase reporter assay was carried out to evaluate the changes in signaling pathways when O-GlcNAcylation level was increased in GC cells and in vitro O-GlcNAcylation assay was utilized for wild and mutant types of CD36 protein to explore the potential O-GlcNAcylation sites.
31410220	5	58	theme	Transwell	610:618	arg1	assay					620:624	Transwell assay	610:624	Transwell assay	610:624	Transwell assay and xenografts were used to assess cell metastasis abilities in vitro and in vivo after indicated treatment.
31410220	7	59	theme	antibodies	1140:1149	arg1	use					1120:1122	the use	1116:1122	the use of neutralizing antibodies to block CD36	1116:1163	Results: High CD36 expression is a predictor of poor survival and promotes metastasis of GC cells and the use of neutralizing antibodies to block CD36 inhibits GC metastasis in mice.
31410220	1	60	theme	death	124:128	arg1	Metastasis					89:98	Metastasis	89:98	Metastasis	89:98	Metastasis is the primary cause of death in patients with advanced cancer.
31410220	1	60	theme	death	124:128	arg1	cause					115:119	the primary cause	103:119	the primary cause of death in patients with advanced cancer	103:161	Metastasis is the primary cause of death in patients with advanced cancer.
31410220	6	61	theme	in	880:881	arg1	assay					905:909	in vitro O-GlcNAcylation assay	880:909	in vitro O-GlcNAcylation assay	880:909	Luciferase reporter assay was carried out to evaluate the changes in signaling pathways when O-GlcNAcylation level was increased in GC cells and in vitro O-GlcNAcylation assay was utilized for wild and mutant types of CD36 protein to explore the potential O-GlcNAcylation sites.
31410220	2	62	theme	cancer	261:266	arg1	cells					268:272	specific cancer cells	252:272	specific cancer cells	252:272	Recently, a high-fat diet was shown to specifically promote the metastatic potential of specific cancer cells in a CD36-dependent manner.
31410220	8	63	theme	metastatic	1222:1231	arg1	potential					1233:1241	the metastatic potential	1218:1241	the metastatic potential of GC cells	1218:1253	FA or a HFD promotes the metastatic potential of GC cells by upregulating CD36 via increasing the O-GlcNAcylation level.
31410220	1	64	from	cause	115:119	arg1	patients					133:140	patients	133:140	patients with advanced cancer	133:161	Metastasis is the primary cause of death in patients with advanced cancer.
31410220	4	65	theme	cancer	574:579	arg1	tissues					586:592	gastric cancer (GC) tissues	566:592	gastric cancer (GC) tissues	566:592	Methods: RT-qPCR, FACS analysis, immunoblotting and immunohistochemistry, as well as retrieving TCGA database, were carried out to quantitate CD36 expression in gastric cancer (GC) tissues and cell lines.
31410220	9	66	theme	Increased	1318:1326	arg1	levels					1344:1349	Increased O-GlcNAcylation levels	1318:1349	Increased O-GlcNAcylation levels	1318:1349	Increased O-GlcNAcylation levels promote the transcription of CD36 by activating the NF-κB pathway and also increase its FA uptake activity by directly modifying CD36 at S468 and T470.
31410220	2	67	theme	specific	252:259	arg1	cells					268:272	specific cancer cells	252:272	specific cancer cells	252:272	Recently, a high-fat diet was shown to specifically promote the metastatic potential of specific cancer cells in a CD36-dependent manner.
31410220	1	68	theme	advanced	147:154	arg1	cancer					156:161	advanced cancer	147:161	advanced cancer	147:161	Metastasis is the primary cause of death in patients with advanced cancer.
31410220	4	69	theme	gastric	566:572	arg1	tissues					586:592	gastric cancer (GC) tissues	566:592	gastric cancer (GC) tissues	566:592	Methods: RT-qPCR, FACS analysis, immunoblotting and immunohistochemistry, as well as retrieving TCGA database, were carried out to quantitate CD36 expression in gastric cancer (GC) tissues and cell lines.
31410220	4	70	theme	GC	582:583	arg1	tissues					586:592	gastric cancer (GC) tissues	566:592	gastric cancer (GC) tissues	566:592	Methods: RT-qPCR, FACS analysis, immunoblotting and immunohistochemistry, as well as retrieving TCGA database, were carried out to quantitate CD36 expression in gastric cancer (GC) tissues and cell lines.
31410220	0	71	theme	cancer	70:75	arg1	metastasis					77:86	gastric cancer metastasis	62:86	gastric cancer metastasis	62:86	Fatty acid-induced CD36 expression via O-GlcNAcylation drives gastric cancer metastasis.
31410220	6	72	theme	CD36	953:956	arg1	protein					958:964	CD36 protein	953:964	CD36 protein	953:964	Luciferase reporter assay was carried out to evaluate the changes in signaling pathways when O-GlcNAcylation level was increased in GC cells and in vitro O-GlcNAcylation assay was utilized for wild and mutant types of CD36 protein to explore the potential O-GlcNAcylation sites.
31410220	10	73	theme	FA-induced	1515:1524	arg1	hyper-O-GlcNAcylation					1526:1546	FA-induced hyper-O-GlcNAcylation	1515:1546	FA-induced hyper-O-GlcNAcylation	1515:1546	Conclusion: FA-induced hyper-O-GlcNAcylation promotes the transcription and function of CD36 by activating the NF-κB pathway and directly modifying CD36 at S468 and T470, which drives GC metastasis.
31410220	3	74	theme	-induced	353:360	arg1	upregulation					362:373	the fatty acid (FA)-induced upregulation	334:373	the fatty acid (FA)-induced upregulation of CD36	334:381	However, the molecular basis of the fatty acid (FA)-induced upregulation of CD36 has remained unclear.
31410220	7	75	theme	GC	1174:1175	arg1	metastasis					1177:1186	GC metastasis	1174:1186	GC metastasis in mice	1174:1194	Results: High CD36 expression is a predictor of poor survival and promotes metastasis of GC cells and the use of neutralizing antibodies to block CD36 inhibits GC metastasis in mice.
31410220	6	76	theme	O-GlcNAcylation	889:903	arg1	assay					905:909	in vitro O-GlcNAcylation assay	880:909	in vitro O-GlcNAcylation assay	880:909	Luciferase reporter assay was carried out to evaluate the changes in signaling pathways when O-GlcNAcylation level was increased in GC cells and in vitro O-GlcNAcylation assay was utilized for wild and mutant types of CD36 protein to explore the potential O-GlcNAcylation sites.
22923583	5	0	theme	cell	699:702	arg1	proliferation					704:716	cancer cell proliferation	692:716	cancer cell proliferation	692:716	Blocking glycosylation of PFK1 at serine 529 reduced cancer cell proliferation in vitro and impaired tumor formation in vivo.
22923583	1	1	theme	changing	164:171	arg1	microenvironment					173:188	a continually changing microenvironment	150:188	a continually changing microenvironment	150:188	Cancer cells must satisfy the metabolic demands of rapid cell growth within a continually changing microenvironment.
22923583	2	2	link	O-linked	270:277	arg1	β-N-acetylglucosamine					279:299	O-linked β-N-acetylglucosamine	270:299	O-linked β-N-acetylglucosamine (O-GlcNAcylation)	270:317	We demonstrated that the dynamic posttranslational modification of proteins by O-linked β-N-acetylglucosamine (O-GlcNAcylation) is a key metabolic regulator of glucose metabolism.
22923583	2	2	link	O-linked	270:277	arg1	O-GlcNAcylation					302:316	O-GlcNAcylation	302:316	O-GlcNAcylation	302:316	We demonstrated that the dynamic posttranslational modification of proteins by O-linked β-N-acetylglucosamine (O-GlcNAcylation) is a key metabolic regulator of glucose metabolism.
22923583	3	3	theme	serine	402:407	arg1	529					409:411	serine 529	402:411	serine 529 of phosphofructokinase 1 (PFK1)	402:443	O-GlcNAcylation was induced at serine 529 of phosphofructokinase 1 (PFK1) in response to hypoxia.
22923583	4	4	theme	phosphate	555:563	arg1	pathway					565:571	the pentose phosphate pathway	543:571	the pentose phosphate pathway	543:571	Glycosylation inhibited PFK1 activity and redirected glucose flux through the pentose phosphate pathway, thereby conferring a selective growth advantage on cancer cells.
22923583	2	5	theme	key	324:326	arg1	regulator					338:346	a key metabolic regulator	322:346	a key metabolic regulator of glucose metabolism	322:368	We demonstrated that the dynamic posttranslational modification of proteins by O-linked β-N-acetylglucosamine (O-GlcNAcylation) is a key metabolic regulator of glucose metabolism.
22923583	2	5	theme	key	324:326	arg1	modification					242:253	the dynamic posttranslational modification	212:253	the dynamic posttranslational modification of proteins by O-linked β-N-acetylglucosamine (O-GlcNAcylation)	212:317	We demonstrated that the dynamic posttranslational modification of proteins by O-linked β-N-acetylglucosamine (O-GlcNAcylation) is a key metabolic regulator of glucose metabolism.
22923583	4	6	theme	glucose	522:528	arg1	flux					530:533	redirected glucose flux	511:533	redirected glucose flux	511:533	Glycosylation inhibited PFK1 activity and redirected glucose flux through the pentose phosphate pathway, thereby conferring a selective growth advantage on cancer cells.
22923583	5	7	theme	PFK1	665:668	arg1	glycosylation					648:660	glycosylation	648:660	glycosylation of PFK1	648:668	Blocking glycosylation of PFK1 at serine 529 reduced cancer cell proliferation in vitro and impaired tumor formation in vivo.
22923583	1	8	theme	Cancer	74:79	arg1	cells					81:85	Cancer cells	74:85	Cancer cells	74:85	Cancer cells must satisfy the metabolic demands of rapid cell growth within a continually changing microenvironment.
22923583	2	9	theme	metabolism	359:368	arg1	regulator					338:346	a key metabolic regulator	322:346	a key metabolic regulator of glucose metabolism	322:368	We demonstrated that the dynamic posttranslational modification of proteins by O-linked β-N-acetylglucosamine (O-GlcNAcylation) is a key metabolic regulator of glucose metabolism.
22923583	2	9	theme	metabolism	359:368	arg1	modification					242:253	the dynamic posttranslational modification	212:253	the dynamic posttranslational modification of proteins by O-linked β-N-acetylglucosamine (O-GlcNAcylation)	212:317	We demonstrated that the dynamic posttranslational modification of proteins by O-linked β-N-acetylglucosamine (O-GlcNAcylation) is a key metabolic regulator of glucose metabolism.
22923583	4	10	theme	redirected	511:520	arg1	flux					530:533	redirected glucose flux	511:533	redirected glucose flux	511:533	Glycosylation inhibited PFK1 activity and redirected glucose flux through the pentose phosphate pathway, thereby conferring a selective growth advantage on cancer cells.
22923583	6	11	from	cancer	869:874	arg1	regulation					833:842	the regulation	829:842	the regulation of metabolic pathways in cancer	829:874	These studies reveal a previously uncharacterized mechanism for the regulation of metabolic pathways in cancer and a possible target for therapeutic intervention.
22923583	6	12	theme	pathways	857:864	arg1	regulation					833:842	the regulation	829:842	the regulation of metabolic pathways in cancer	829:874	These studies reveal a previously uncharacterized mechanism for the regulation of metabolic pathways in cancer and a possible target for therapeutic intervention.
22923583	4	13	from	advantage	612:620	arg1	cells					632:636	cancer cells	625:636	cancer cells	625:636	Glycosylation inhibited PFK1 activity and redirected glucose flux through the pentose phosphate pathway, thereby conferring a selective growth advantage on cancer cells.
22923583	6	14	theme	metabolic	847:855	arg1	pathways					857:864	metabolic pathways	847:864	metabolic pathways in cancer	847:874	These studies reveal a previously uncharacterized mechanism for the regulation of metabolic pathways in cancer and a possible target for therapeutic intervention.
22923583	2	15	theme	glucose	351:357	arg1	metabolism					359:368	glucose metabolism	351:368	glucose metabolism	351:368	We demonstrated that the dynamic posttranslational modification of proteins by O-linked β-N-acetylglucosamine (O-GlcNAcylation) is a key metabolic regulator of glucose metabolism.
22923583	0	16	theme	Phosphofructokinase	0:18	arg1	glycosylation					22:34	Phosphofructokinase 1 glycosylation	0:34	Phosphofructokinase 1 glycosylation	0:34	Phosphofructokinase 1 glycosylation regulates cell growth and metabolism.
22923583	4	17	theme	growth	605:610	arg1	advantage					612:620	a selective growth advantage	593:620	a selective growth advantage on cancer cells	593:636	Glycosylation inhibited PFK1 activity and redirected glucose flux through the pentose phosphate pathway, thereby conferring a selective growth advantage on cancer cells.
22923583	5	18	theme	cancer	692:697	arg1	proliferation					704:716	cancer cell proliferation	692:716	cancer cell proliferation	692:716	Blocking glycosylation of PFK1 at serine 529 reduced cancer cell proliferation in vitro and impaired tumor formation in vivo.
22923583	6	19	theme	therapeutic	902:912	arg1	intervention					914:925	therapeutic intervention	902:925	therapeutic intervention	902:925	These studies reveal a previously uncharacterized mechanism for the regulation of metabolic pathways in cancer and a possible target for therapeutic intervention.
22923583	4	20	theme	selective	595:603	arg1	advantage					612:620	a selective growth advantage	593:620	a selective growth advantage on cancer cells	593:636	Glycosylation inhibited PFK1 activity and redirected glucose flux through the pentose phosphate pathway, thereby conferring a selective growth advantage on cancer cells.
22923583	1	21	theme	metabolic	104:112	arg1	demands					114:120	the metabolic demands	100:120	the metabolic demands of rapid cell growth	100:141	Cancer cells must satisfy the metabolic demands of rapid cell growth within a continually changing microenvironment.
22923583	3	22	theme	phosphofructokinase	416:434	arg1	529					409:411	serine 529	402:411	serine 529 of phosphofructokinase 1 (PFK1)	402:443	O-GlcNAcylation was induced at serine 529 of phosphofructokinase 1 (PFK1) in response to hypoxia.
22923583	4	23	theme	PFK1	493:496	arg1	activity					498:505	PFK1 activity	493:505	PFK1 activity	493:505	Glycosylation inhibited PFK1 activity and redirected glucose flux through the pentose phosphate pathway, thereby conferring a selective growth advantage on cancer cells.
22923583	2	24	theme	metabolic	328:336	arg1	regulator					338:346	a key metabolic regulator	322:346	a key metabolic regulator of glucose metabolism	322:368	We demonstrated that the dynamic posttranslational modification of proteins by O-linked β-N-acetylglucosamine (O-GlcNAcylation) is a key metabolic regulator of glucose metabolism.
22923583	2	24	theme	metabolic	328:336	arg1	modification					242:253	the dynamic posttranslational modification	212:253	the dynamic posttranslational modification of proteins by O-linked β-N-acetylglucosamine (O-GlcNAcylation)	212:317	We demonstrated that the dynamic posttranslational modification of proteins by O-linked β-N-acetylglucosamine (O-GlcNAcylation) is a key metabolic regulator of glucose metabolism.
22923583	6	25	from	regulation	833:842	arg1	cancer					869:874	cancer	869:874	cancer	869:874	These studies reveal a previously uncharacterized mechanism for the regulation of metabolic pathways in cancer and a possible target for therapeutic intervention.
22923583	6	26	from	pathways	857:864	arg1	cancer					869:874	cancer	869:874	cancer	869:874	These studies reveal a previously uncharacterized mechanism for the regulation of metabolic pathways in cancer and a possible target for therapeutic intervention.
22923583	4	27	theme	cancer	625:630	arg1	cells					632:636	cancer cells	625:636	cancer cells	625:636	Glycosylation inhibited PFK1 activity and redirected glucose flux through the pentose phosphate pathway, thereby conferring a selective growth advantage on cancer cells.
22923583	2	28	theme	proteins	258:265	arg1	regulator					338:346	a key metabolic regulator	322:346	a key metabolic regulator of glucose metabolism	322:368	We demonstrated that the dynamic posttranslational modification of proteins by O-linked β-N-acetylglucosamine (O-GlcNAcylation) is a key metabolic regulator of glucose metabolism.
22923583	2	28	theme	proteins	258:265	arg1	modification					242:253	the dynamic posttranslational modification	212:253	the dynamic posttranslational modification of proteins by O-linked β-N-acetylglucosamine (O-GlcNAcylation)	212:317	We demonstrated that the dynamic posttranslational modification of proteins by O-linked β-N-acetylglucosamine (O-GlcNAcylation) is a key metabolic regulator of glucose metabolism.
22923583	3	29	gly	O-GlcNAcylation	371:385	arg1	response					448:455	response	448:455	response to hypoxia	448:466	O-GlcNAcylation was induced at serine 529 of phosphofructokinase 1 (PFK1) in response to hypoxia.
22923583	3	29	gly	O-GlcNAcylation	371:385	arg1	529					409:411	serine 529	402:411	serine 529 of phosphofructokinase 1 (PFK1)	402:443	O-GlcNAcylation was induced at serine 529 of phosphofructokinase 1 (PFK1) in response to hypoxia.
22923583	2	30	theme	posttranslational	224:240	arg1	regulator					338:346	a key metabolic regulator	322:346	a key metabolic regulator of glucose metabolism	322:368	We demonstrated that the dynamic posttranslational modification of proteins by O-linked β-N-acetylglucosamine (O-GlcNAcylation) is a key metabolic regulator of glucose metabolism.
22923583	2	30	theme	posttranslational	224:240	arg1	modification					242:253	the dynamic posttranslational modification	212:253	the dynamic posttranslational modification of proteins by O-linked β-N-acetylglucosamine (O-GlcNAcylation)	212:317	We demonstrated that the dynamic posttranslational modification of proteins by O-linked β-N-acetylglucosamine (O-GlcNAcylation) is a key metabolic regulator of glucose metabolism.
22923583	0	31	dep	cell	46:49	arg1	growth					51:56	growth	51:56	growth	51:56	Phosphofructokinase 1 glycosylation regulates cell growth and metabolism.
22923583	0	31	dep	cell	46:49	arg1	metabolism					62:71	metabolism	62:71	metabolism	62:71	Phosphofructokinase 1 glycosylation regulates cell growth and metabolism.
22923583	1	32	theme	rapid	125:129	arg1	growth					136:141	rapid cell growth	125:141	rapid cell growth	125:141	Cancer cells must satisfy the metabolic demands of rapid cell growth within a continually changing microenvironment.
22923583	5	33	theme	tumor	740:744	arg1	formation					746:754	tumor formation	740:754	tumor formation	740:754	Blocking glycosylation of PFK1 at serine 529 reduced cancer cell proliferation in vitro and impaired tumor formation in vivo.
22923583	2	34	theme	dynamic	216:222	arg1	regulator					338:346	a key metabolic regulator	322:346	a key metabolic regulator of glucose metabolism	322:368	We demonstrated that the dynamic posttranslational modification of proteins by O-linked β-N-acetylglucosamine (O-GlcNAcylation) is a key metabolic regulator of glucose metabolism.
22923583	2	34	theme	dynamic	216:222	arg1	modification					242:253	the dynamic posttranslational modification	212:253	the dynamic posttranslational modification of proteins by O-linked β-N-acetylglucosamine (O-GlcNAcylation)	212:317	We demonstrated that the dynamic posttranslational modification of proteins by O-linked β-N-acetylglucosamine (O-GlcNAcylation) is a key metabolic regulator of glucose metabolism.
22923583	6	35	theme	uncharacterized	799:813	arg1	mechanism					815:823	a previously uncharacterized mechanism	786:823	a previously uncharacterized mechanism for the regulation of metabolic pathways in cancer	786:874	These studies reveal a previously uncharacterized mechanism for the regulation of metabolic pathways in cancer and a possible target for therapeutic intervention.
22923583	1	36	theme	cell	131:134	arg1	growth					136:141	rapid cell growth	125:141	rapid cell growth	125:141	Cancer cells must satisfy the metabolic demands of rapid cell growth within a continually changing microenvironment.
22923583	1	37	theme	growth	136:141	arg1	demands					114:120	the metabolic demands	100:120	the metabolic demands of rapid cell growth	100:141	Cancer cells must satisfy the metabolic demands of rapid cell growth within a continually changing microenvironment.
22923583	5	38	gly	glycosylation	648:660	arg1	serine					673:678	serine 529	673:682	serine 529	673:682	Blocking glycosylation of PFK1 at serine 529 reduced cancer cell proliferation in vitro and impaired tumor formation in vivo.
22923583	5	38	gly	glycosylation	648:660	arg1	PFK1					665:668	PFK1	665:668	PFK1	665:668	Blocking glycosylation of PFK1 at serine 529 reduced cancer cell proliferation in vitro and impaired tumor formation in vivo.
22923583	6	39	theme	possible	882:889	arg1	target					891:896	a possible target	880:896	a possible target for therapeutic intervention	880:925	These studies reveal a previously uncharacterized mechanism for the regulation of metabolic pathways in cancer and a possible target for therapeutic intervention.
22923583	4	40	theme	pentose	547:553	arg1	pathway					565:571	the pentose phosphate pathway	543:571	the pentose phosphate pathway	543:571	Glycosylation inhibited PFK1 activity and redirected glucose flux through the pentose phosphate pathway, thereby conferring a selective growth advantage on cancer cells.
22923583	2	41	theme	O-linked	270:277	arg1	β-N-acetylglucosamine					279:299	O-linked β-N-acetylglucosamine	270:299	O-linked β-N-acetylglucosamine (O-GlcNAcylation)	270:317	We demonstrated that the dynamic posttranslational modification of proteins by O-linked β-N-acetylglucosamine (O-GlcNAcylation) is a key metabolic regulator of glucose metabolism.
22923583	2	41	theme	O-linked	270:277	arg1	O-GlcNAcylation					302:316	O-GlcNAcylation	302:316	O-GlcNAcylation	302:316	We demonstrated that the dynamic posttranslational modification of proteins by O-linked β-N-acetylglucosamine (O-GlcNAcylation) is a key metabolic regulator of glucose metabolism.
26402673	2	0	theme	several	395:401	arg1	components					413:422	several important components	395:422	several important components of insulin signal pathway	395:448	Accumulating evidence has demonstrated that O-GlcNAc modification regulates functions of several important components of insulin signal pathway.
26402673	0	1	from	Role	4:7	arg1	Resistance					53:62	Hepatic Insulin Resistance	37:62	Hepatic Insulin Resistance	37:62	The Role of PTP1B O-GlcNAcylation in Hepatic Insulin Resistance.
26402673	4	2	theme	HepG2	834:838	arg1	cells					840:844	HepG2 cells	834:844	HepG2 cells	834:844	Palmitate acid (PA) impaired the insulin signaling, indicated by decreased phosphorylation of both serine/threonine-protein kinase B (Akt) and glycogen synthase kinase 3 beta (GSK3β) following insulin administration, and upregulated PTP1B O-GlcNAcylation in HepG2 cells.
26402673	1	3	theme	insulin	229:235	arg1	signaling					237:245	insulin signaling	229:245	insulin signaling	229:245	Protein tyrosine phosphatase 1B (PTP1B), which can directly dephosphorylate both the insulin receptor and insulin receptor substrate 1 (IRS-1), thereby terminating insulin signaling, reportedly plays an important role in insulin resistance.
26402673	4	4	theme	decreased	641:649	arg1	phosphorylation					651:665	decreased phosphorylation	641:665	decreased phosphorylation of both serine/threonine-protein kinase B (Akt) and glycogen synthase kinase 3 beta (GSK3β)	641:757	Palmitate acid (PA) impaired the insulin signaling, indicated by decreased phosphorylation of both serine/threonine-protein kinase B (Akt) and glycogen synthase kinase 3 beta (GSK3β) following insulin administration, and upregulated PTP1B O-GlcNAcylation in HepG2 cells.
26402673	4	5	theme	kinase	737:742	arg1	phosphorylation					651:665	decreased phosphorylation	641:665	decreased phosphorylation of both serine/threonine-protein kinase B (Akt) and glycogen synthase kinase 3 beta (GSK3β)	641:757	Palmitate acid (PA) impaired the insulin signaling, indicated by decreased phosphorylation of both serine/threonine-protein kinase B (Akt) and glycogen synthase kinase 3 beta (GSK3β) following insulin administration, and upregulated PTP1B O-GlcNAcylation in HepG2 cells.
26402673	5	6	theme	site-directed	914:926	arg1	mutation					933:940	site-directed gene mutation	914:940	site-directed gene mutation	914:940	Compared with the wild-type, intervention PTP1B O-GlcNAcylation by site-directed gene mutation inhibited PTP1B phosphatase activity, resulted in a higher level of phosphorylated Akt and GSK3β, recovered insulin sensitivity, and improved lipid deposition in HepG2 cells.
26402673	5	7	theme	phosphatase	958:968	arg1	activity					970:977	PTP1B phosphatase activity	952:977	PTP1B phosphatase activity	952:977	Compared with the wild-type, intervention PTP1B O-GlcNAcylation by site-directed gene mutation inhibited PTP1B phosphatase activity, resulted in a higher level of phosphorylated Akt and GSK3β, recovered insulin sensitivity, and improved lipid deposition in HepG2 cells.
26402673	4	8	theme	synthase	728:735	arg1	kinase					737:742	glycogen synthase kinase	719:742	glycogen synthase kinase	719:742	Palmitate acid (PA) impaired the insulin signaling, indicated by decreased phosphorylation of both serine/threonine-protein kinase B (Akt) and glycogen synthase kinase 3 beta (GSK3β) following insulin administration, and upregulated PTP1B O-GlcNAcylation in HepG2 cells.
26402673	4	9	from	O-GlcNAcylation	815:829	arg1	cells					840:844	HepG2 cells	834:844	HepG2 cells	834:844	Palmitate acid (PA) impaired the insulin signaling, indicated by decreased phosphorylation of both serine/threonine-protein kinase B (Akt) and glycogen synthase kinase 3 beta (GSK3β) following insulin administration, and upregulated PTP1B O-GlcNAcylation in HepG2 cells.
26402673	4	10	theme	PTP1B	809:813	arg1	O-GlcNAcylation					815:829	PTP1B O-GlcNAcylation	809:829	PTP1B O-GlcNAcylation in HepG2 cells	809:844	Palmitate acid (PA) impaired the insulin signaling, indicated by decreased phosphorylation of both serine/threonine-protein kinase B (Akt) and glycogen synthase kinase 3 beta (GSK3β) following insulin administration, and upregulated PTP1B O-GlcNAcylation in HepG2 cells.
26402673	1	11	theme	Protein	65:71	arg1	phosphatase					82:92	Protein tyrosine phosphatase	65:92	Protein tyrosine phosphatase 1B (PTP1B)	65:103	Protein tyrosine phosphatase 1B (PTP1B), which can directly dephosphorylate both the insulin receptor and insulin receptor substrate 1 (IRS-1), thereby terminating insulin signaling, reportedly plays an important role in insulin resistance.
26402673	1	12	theme	insulin	150:156	arg1	receptor					158:165	the insulin receptor	146:165	the insulin receptor	146:165	Protein tyrosine phosphatase 1B (PTP1B), which can directly dephosphorylate both the insulin receptor and insulin receptor substrate 1 (IRS-1), thereby terminating insulin signaling, reportedly plays an important role in insulin resistance.
26402673	6	13	theme	phosphatase	1247:1257	arg1	activity					1259:1266	its own phosphatase activity	1239:1266	its own phosphatase activity	1239:1266	Taken together, our research showed that O-GlcNAcylation of PTP1B can influence insulin signal transduction by modulating its own phosphatase activity, which participates in the process of hepatic insulin resistance.
26402673	1	14	theme	tyrosine	73:80	arg1	phosphatase					82:92	Protein tyrosine phosphatase	65:92	Protein tyrosine phosphatase 1B (PTP1B)	65:103	Protein tyrosine phosphatase 1B (PTP1B), which can directly dephosphorylate both the insulin receptor and insulin receptor substrate 1 (IRS-1), thereby terminating insulin signaling, reportedly plays an important role in insulin resistance.
26402673	3	15	mod	modified	494:501	arg1	PTP1B					485:489	PTP1B	485:489	PTP1B	485:489	In this study, we identified that PTP1B is modified by O-GlcNAcylation at three O-GlcNAc sites (Ser104, Ser201, and Ser386).
26402673	3	15	mod	modified	494:501	arg3	O-GlcNAcylation					506:520	O-GlcNAcylation	506:520	O-GlcNAcylation	506:520	In this study, we identified that PTP1B is modified by O-GlcNAcylation at three O-GlcNAc sites (Ser104, Ser201, and Ser386).
26402673	5	16	from	deposition	1090:1099	arg1	cells					1110:1114	HepG2 cells	1104:1114	HepG2 cells	1104:1114	Compared with the wild-type, intervention PTP1B O-GlcNAcylation by site-directed gene mutation inhibited PTP1B phosphatase activity, resulted in a higher level of phosphorylated Akt and GSK3β, recovered insulin sensitivity, and improved lipid deposition in HepG2 cells.
26402673	6	17	theme	own	1243:1245	arg1	activity					1259:1266	its own phosphatase activity	1239:1266	its own phosphatase activity	1239:1266	Taken together, our research showed that O-GlcNAcylation of PTP1B can influence insulin signal transduction by modulating its own phosphatase activity, which participates in the process of hepatic insulin resistance.
26402673	1	18	theme	phosphatase	82:92	arg1	1B					94:95	Protein tyrosine phosphatase 1B	65:95	Protein tyrosine phosphatase 1B (PTP1B)	65:103	Protein tyrosine phosphatase 1B (PTP1B), which can directly dephosphorylate both the insulin receptor and insulin receptor substrate 1 (IRS-1), thereby terminating insulin signaling, reportedly plays an important role in insulin resistance.
26402673	1	18	theme	phosphatase	82:92	arg1	PTP1B					98:102	PTP1B	98:102	PTP1B	98:102	Protein tyrosine phosphatase 1B (PTP1B), which can directly dephosphorylate both the insulin receptor and insulin receptor substrate 1 (IRS-1), thereby terminating insulin signaling, reportedly plays an important role in insulin resistance.
26402673	5	19	theme	lipid	1084:1088	arg1	deposition					1090:1099	lipid deposition	1084:1099	lipid deposition in HepG2 cells	1084:1114	Compared with the wild-type, intervention PTP1B O-GlcNAcylation by site-directed gene mutation inhibited PTP1B phosphatase activity, resulted in a higher level of phosphorylated Akt and GSK3β, recovered insulin sensitivity, and improved lipid deposition in HepG2 cells.
26402673	4	20	dep	B	707:707	arg1	GSK3β					752:756	GSK3β	752:756	GSK3β	752:756	Palmitate acid (PA) impaired the insulin signaling, indicated by decreased phosphorylation of both serine/threonine-protein kinase B (Akt) and glycogen synthase kinase 3 beta (GSK3β) following insulin administration, and upregulated PTP1B O-GlcNAcylation in HepG2 cells.
26402673	4	20	dep	B	707:707	arg1	beta					746:749	3 beta	744:749	3 beta (GSK3β)	744:757	Palmitate acid (PA) impaired the insulin signaling, indicated by decreased phosphorylation of both serine/threonine-protein kinase B (Akt) and glycogen synthase kinase 3 beta (GSK3β) following insulin administration, and upregulated PTP1B O-GlcNAcylation in HepG2 cells.
26402673	1	21	theme	insulin	171:177	arg1	substrate					188:196	insulin receptor substrate 1	171:198	insulin receptor substrate 1 (IRS-1)	171:206	Protein tyrosine phosphatase 1B (PTP1B), which can directly dephosphorylate both the insulin receptor and insulin receptor substrate 1 (IRS-1), thereby terminating insulin signaling, reportedly plays an important role in insulin resistance.
26402673	1	21	theme	insulin	171:177	arg1	IRS-1					201:205	IRS-1	201:205	IRS-1	201:205	Protein tyrosine phosphatase 1B (PTP1B), which can directly dephosphorylate both the insulin receptor and insulin receptor substrate 1 (IRS-1), thereby terminating insulin signaling, reportedly plays an important role in insulin resistance.
26402673	2	22	theme	pathway	442:448	arg1	components					413:422	several important components	395:422	several important components of insulin signal pathway	395:448	Accumulating evidence has demonstrated that O-GlcNAc modification regulates functions of several important components of insulin signal pathway.
26402673	6	23	theme	signal	1205:1210	arg1	transduction					1212:1223	insulin signal transduction	1197:1223	insulin signal transduction	1197:1223	Taken together, our research showed that O-GlcNAcylation of PTP1B can influence insulin signal transduction by modulating its own phosphatase activity, which participates in the process of hepatic insulin resistance.
26402673	4	24	theme	glycogen	719:726	arg1	kinase					737:742	glycogen synthase kinase	719:742	glycogen synthase kinase	719:742	Palmitate acid (PA) impaired the insulin signaling, indicated by decreased phosphorylation of both serine/threonine-protein kinase B (Akt) and glycogen synthase kinase 3 beta (GSK3β) following insulin administration, and upregulated PTP1B O-GlcNAcylation in HepG2 cells.
26402673	2	25	theme	insulin	427:433	arg1	pathway					442:448	insulin signal pathway	427:448	insulin signal pathway	427:448	Accumulating evidence has demonstrated that O-GlcNAc modification regulates functions of several important components of insulin signal pathway.
26402673	2	26	theme	signal	435:440	arg1	pathway					442:448	insulin signal pathway	427:448	insulin signal pathway	427:448	Accumulating evidence has demonstrated that O-GlcNAc modification regulates functions of several important components of insulin signal pathway.
26402673	5	27	theme	gene	928:931	arg1	mutation					933:940	site-directed gene mutation	914:940	site-directed gene mutation	914:940	Compared with the wild-type, intervention PTP1B O-GlcNAcylation by site-directed gene mutation inhibited PTP1B phosphatase activity, resulted in a higher level of phosphorylated Akt and GSK3β, recovered insulin sensitivity, and improved lipid deposition in HepG2 cells.
26402673	5	28	theme	insulin	1050:1056	arg1	sensitivity					1058:1068	insulin sensitivity	1050:1068	insulin sensitivity	1050:1068	Compared with the wild-type, intervention PTP1B O-GlcNAcylation by site-directed gene mutation inhibited PTP1B phosphatase activity, resulted in a higher level of phosphorylated Akt and GSK3β, recovered insulin sensitivity, and improved lipid deposition in HepG2 cells.
26402673	1	29	theme	important	268:276	arg1	role					278:281	an important role	265:281	an important role	265:281	Protein tyrosine phosphatase 1B (PTP1B), which can directly dephosphorylate both the insulin receptor and insulin receptor substrate 1 (IRS-1), thereby terminating insulin signaling, reportedly plays an important role in insulin resistance.
26402673	6	30	theme	resistance	1322:1331	arg1	process					1295:1301	the process	1291:1301	the process of hepatic insulin resistance	1291:1331	Taken together, our research showed that O-GlcNAcylation of PTP1B can influence insulin signal transduction by modulating its own phosphatase activity, which participates in the process of hepatic insulin resistance.
26402673	4	31	theme	insulin	609:615	arg1	signaling					617:625	the insulin signaling	605:625	the insulin signaling	605:625	Palmitate acid (PA) impaired the insulin signaling, indicated by decreased phosphorylation of both serine/threonine-protein kinase B (Akt) and glycogen synthase kinase 3 beta (GSK3β) following insulin administration, and upregulated PTP1B O-GlcNAcylation in HepG2 cells.
26402673	2	32	theme	components	413:422	arg1	functions					382:390	functions	382:390	functions of several important components of insulin signal pathway	382:448	Accumulating evidence has demonstrated that O-GlcNAc modification regulates functions of several important components of insulin signal pathway.
26402673	0	33	theme	O-GlcNAcylation	18:32	arg1	Role					4:7	The Role	0:7	The Role of PTP1B O-GlcNAcylation in Hepatic Insulin Resistance	0:62	The Role of PTP1B O-GlcNAcylation in Hepatic Insulin Resistance.
26402673	6	34	theme	insulin	1314:1320	arg1	resistance					1322:1331	hepatic insulin resistance	1306:1331	hepatic insulin resistance	1306:1331	Taken together, our research showed that O-GlcNAcylation of PTP1B can influence insulin signal transduction by modulating its own phosphatase activity, which participates in the process of hepatic insulin resistance.
26402673	0	35	theme	PTP1B	12:16	arg1	O-GlcNAcylation					18:32	PTP1B O-GlcNAcylation	12:32	PTP1B O-GlcNAcylation	12:32	The Role of PTP1B O-GlcNAcylation in Hepatic Insulin Resistance.
26402673	2	36	theme	important	403:411	arg1	components					413:422	several important components	395:422	several important components of insulin signal pathway	395:448	Accumulating evidence has demonstrated that O-GlcNAc modification regulates functions of several important components of insulin signal pathway.
26402673	0	37	theme	Insulin	45:51	arg1	Resistance					53:62	Hepatic Insulin Resistance	37:62	Hepatic Insulin Resistance	37:62	The Role of PTP1B O-GlcNAcylation in Hepatic Insulin Resistance.
26402673	6	38	theme	hepatic	1306:1312	arg1	resistance					1322:1331	hepatic insulin resistance	1306:1331	hepatic insulin resistance	1306:1331	Taken together, our research showed that O-GlcNAcylation of PTP1B can influence insulin signal transduction by modulating its own phosphatase activity, which participates in the process of hepatic insulin resistance.
26402673	5	39	theme	GSK3β	1033:1037	arg1	level					1001:1005	a higher level	992:1005	a higher level of phosphorylated Akt and GSK3β	992:1037	Compared with the wild-type, intervention PTP1B O-GlcNAcylation by site-directed gene mutation inhibited PTP1B phosphatase activity, resulted in a higher level of phosphorylated Akt and GSK3β, recovered insulin sensitivity, and improved lipid deposition in HepG2 cells.
26402673	5	40	theme	phosphorylated	1010:1023	arg1	Akt					1025:1027	phosphorylated Akt	1010:1027	phosphorylated Akt	1010:1027	Compared with the wild-type, intervention PTP1B O-GlcNAcylation by site-directed gene mutation inhibited PTP1B phosphatase activity, resulted in a higher level of phosphorylated Akt and GSK3β, recovered insulin sensitivity, and improved lipid deposition in HepG2 cells.
26402673	4	41	theme	kinase	700:705	arg1	Akt					710:712	Akt	710:712	Akt	710:712	Palmitate acid (PA) impaired the insulin signaling, indicated by decreased phosphorylation of both serine/threonine-protein kinase B (Akt) and glycogen synthase kinase 3 beta (GSK3β) following insulin administration, and upregulated PTP1B O-GlcNAcylation in HepG2 cells.
26402673	4	41	theme	kinase	700:705	arg1	B					707:707	serine/threonine-protein kinase B	675:707	serine/threonine-protein kinase B (Akt)	675:713	Palmitate acid (PA) impaired the insulin signaling, indicated by decreased phosphorylation of both serine/threonine-protein kinase B (Akt) and glycogen synthase kinase 3 beta (GSK3β) following insulin administration, and upregulated PTP1B O-GlcNAcylation in HepG2 cells.
26402673	0	42	theme	Hepatic	37:43	arg1	Resistance					53:62	Hepatic Insulin Resistance	37:62	Hepatic Insulin Resistance	37:62	The Role of PTP1B O-GlcNAcylation in Hepatic Insulin Resistance.
26402673	1	43	theme	insulin	286:292	arg1	resistance					294:303	insulin resistance	286:303	insulin resistance	286:303	Protein tyrosine phosphatase 1B (PTP1B), which can directly dephosphorylate both the insulin receptor and insulin receptor substrate 1 (IRS-1), thereby terminating insulin signaling, reportedly plays an important role in insulin resistance.
26402673	5	44	theme	Akt	1025:1027	arg1	level					1001:1005	a higher level	992:1005	a higher level of phosphorylated Akt and GSK3β	992:1037	Compared with the wild-type, intervention PTP1B O-GlcNAcylation by site-directed gene mutation inhibited PTP1B phosphatase activity, resulted in a higher level of phosphorylated Akt and GSK3β, recovered insulin sensitivity, and improved lipid deposition in HepG2 cells.
26402673	4	45	theme	serine/threonine-protein	675:698	arg1	Akt					710:712	Akt	710:712	Akt	710:712	Palmitate acid (PA) impaired the insulin signaling, indicated by decreased phosphorylation of both serine/threonine-protein kinase B (Akt) and glycogen synthase kinase 3 beta (GSK3β) following insulin administration, and upregulated PTP1B O-GlcNAcylation in HepG2 cells.
26402673	4	45	theme	serine/threonine-protein	675:698	arg1	B					707:707	serine/threonine-protein kinase B	675:707	serine/threonine-protein kinase B (Akt)	675:713	Palmitate acid (PA) impaired the insulin signaling, indicated by decreased phosphorylation of both serine/threonine-protein kinase B (Akt) and glycogen synthase kinase 3 beta (GSK3β) following insulin administration, and upregulated PTP1B O-GlcNAcylation in HepG2 cells.
26402673	6	46	theme	PTP1B	1177:1181	arg1	O-GlcNAcylation					1158:1172	O-GlcNAcylation	1158:1172	O-GlcNAcylation of PTP1B	1158:1181	Taken together, our research showed that O-GlcNAcylation of PTP1B can influence insulin signal transduction by modulating its own phosphatase activity, which participates in the process of hepatic insulin resistance.
26402673	5	47	theme	PTP1B	889:893	arg1	O-GlcNAcylation					895:909	intervention PTP1B O-GlcNAcylation	876:909	intervention PTP1B O-GlcNAcylation by site-directed gene mutation	876:940	Compared with the wild-type, intervention PTP1B O-GlcNAcylation by site-directed gene mutation inhibited PTP1B phosphatase activity, resulted in a higher level of phosphorylated Akt and GSK3β, recovered insulin sensitivity, and improved lipid deposition in HepG2 cells.
26402673	6	48	theme	insulin	1197:1203	arg1	transduction					1212:1223	insulin signal transduction	1197:1223	insulin signal transduction	1197:1223	Taken together, our research showed that O-GlcNAcylation of PTP1B can influence insulin signal transduction by modulating its own phosphatase activity, which participates in the process of hepatic insulin resistance.
26402673	4	49	theme	insulin	769:775	arg1	administration					777:790	insulin administration	769:790	insulin administration	769:790	Palmitate acid (PA) impaired the insulin signaling, indicated by decreased phosphorylation of both serine/threonine-protein kinase B (Akt) and glycogen synthase kinase 3 beta (GSK3β) following insulin administration, and upregulated PTP1B O-GlcNAcylation in HepG2 cells.
26402673	2	50	theme	Accumulating	306:317	arg1	evidence					319:326	Accumulating evidence	306:326	Accumulating evidence	306:326	Accumulating evidence has demonstrated that O-GlcNAc modification regulates functions of several important components of insulin signal pathway.
26402673	3	51	theme	O-GlcNAc	531:538	arg1	sites					540:544	three O-GlcNAc sites	525:544	three O-GlcNAc sites (Ser104, Ser201, and Ser386)	525:573	In this study, we identified that PTP1B is modified by O-GlcNAcylation at three O-GlcNAc sites (Ser104, Ser201, and Ser386).
26402673	3	51	theme	O-GlcNAc	531:538	arg1	Ser201					555:560	Ser201	555:560	Ser201	555:560	In this study, we identified that PTP1B is modified by O-GlcNAcylation at three O-GlcNAc sites (Ser104, Ser201, and Ser386).
26402673	3	51	theme	O-GlcNAc	531:538	arg1	Ser386					567:572	Ser386	567:572	Ser386	567:572	In this study, we identified that PTP1B is modified by O-GlcNAcylation at three O-GlcNAc sites (Ser104, Ser201, and Ser386).
26402673	3	51	theme	O-GlcNAc	531:538	arg1	Ser104					547:552	Ser104	547:552	Ser104	547:552	In this study, we identified that PTP1B is modified by O-GlcNAcylation at three O-GlcNAc sites (Ser104, Ser201, and Ser386).
26402673	5	52	theme	intervention	876:887	arg1	O-GlcNAcylation					895:909	intervention PTP1B O-GlcNAcylation	876:909	intervention PTP1B O-GlcNAcylation by site-directed gene mutation	876:940	Compared with the wild-type, intervention PTP1B O-GlcNAcylation by site-directed gene mutation inhibited PTP1B phosphatase activity, resulted in a higher level of phosphorylated Akt and GSK3β, recovered insulin sensitivity, and improved lipid deposition in HepG2 cells.
26402673	5	53	theme	PTP1B	952:956	arg1	activity					970:977	PTP1B phosphatase activity	952:977	PTP1B phosphatase activity	952:977	Compared with the wild-type, intervention PTP1B O-GlcNAcylation by site-directed gene mutation inhibited PTP1B phosphatase activity, resulted in a higher level of phosphorylated Akt and GSK3β, recovered insulin sensitivity, and improved lipid deposition in HepG2 cells.
26402673	4	54	theme	B	707:707	arg1	phosphorylation					651:665	decreased phosphorylation	641:665	decreased phosphorylation of both serine/threonine-protein kinase B (Akt) and glycogen synthase kinase 3 beta (GSK3β)	641:757	Palmitate acid (PA) impaired the insulin signaling, indicated by decreased phosphorylation of both serine/threonine-protein kinase B (Akt) and glycogen synthase kinase 3 beta (GSK3β) following insulin administration, and upregulated PTP1B O-GlcNAcylation in HepG2 cells.
26402673	3	55	dep	sites	540:544	arg1	sites					540:544	three O-GlcNAc sites	525:544	three O-GlcNAc sites (Ser104, Ser201, and Ser386)	525:573	In this study, we identified that PTP1B is modified by O-GlcNAcylation at three O-GlcNAc sites (Ser104, Ser201, and Ser386).
26402673	3	55	dep	sites	540:544	arg1	Ser201					555:560	Ser201	555:560	Ser201	555:560	In this study, we identified that PTP1B is modified by O-GlcNAcylation at three O-GlcNAc sites (Ser104, Ser201, and Ser386).
26402673	3	55	dep	sites	540:544	arg1	Ser386					567:572	Ser386	567:572	Ser386	567:572	In this study, we identified that PTP1B is modified by O-GlcNAcylation at three O-GlcNAc sites (Ser104, Ser201, and Ser386).
26402673	3	55	dep	sites	540:544	arg1	Ser104					547:552	Ser104	547:552	Ser104	547:552	In this study, we identified that PTP1B is modified by O-GlcNAcylation at three O-GlcNAc sites (Ser104, Ser201, and Ser386).
26402673	1	56	theme	receptor	179:186	arg1	substrate					188:196	insulin receptor substrate 1	171:198	insulin receptor substrate 1 (IRS-1)	171:206	Protein tyrosine phosphatase 1B (PTP1B), which can directly dephosphorylate both the insulin receptor and insulin receptor substrate 1 (IRS-1), thereby terminating insulin signaling, reportedly plays an important role in insulin resistance.
26402673	1	56	theme	receptor	179:186	arg1	IRS-1					201:205	IRS-1	201:205	IRS-1	201:205	Protein tyrosine phosphatase 1B (PTP1B), which can directly dephosphorylate both the insulin receptor and insulin receptor substrate 1 (IRS-1), thereby terminating insulin signaling, reportedly plays an important role in insulin resistance.
26402673	5	57	theme	HepG2	1104:1108	arg1	cells					1110:1114	HepG2 cells	1104:1114	HepG2 cells	1104:1114	Compared with the wild-type, intervention PTP1B O-GlcNAcylation by site-directed gene mutation inhibited PTP1B phosphatase activity, resulted in a higher level of phosphorylated Akt and GSK3β, recovered insulin sensitivity, and improved lipid deposition in HepG2 cells.
26402673	5	58	theme	higher	994:999	arg1	level					1001:1005	a higher level	992:1005	a higher level of phosphorylated Akt and GSK3β	992:1037	Compared with the wild-type, intervention PTP1B O-GlcNAcylation by site-directed gene mutation inhibited PTP1B phosphatase activity, resulted in a higher level of phosphorylated Akt and GSK3β, recovered insulin sensitivity, and improved lipid deposition in HepG2 cells.
26402673	4	59	theme	Palmitate	576:584	arg1	acid					586:589	Palmitate acid	576:589	Palmitate acid (PA)	576:594	Palmitate acid (PA) impaired the insulin signaling, indicated by decreased phosphorylation of both serine/threonine-protein kinase B (Akt) and glycogen synthase kinase 3 beta (GSK3β) following insulin administration, and upregulated PTP1B O-GlcNAcylation in HepG2 cells.
26402673	4	59	theme	Palmitate	576:584	arg1	PA					592:593	PA	592:593	PA	592:593	Palmitate acid (PA) impaired the insulin signaling, indicated by decreased phosphorylation of both serine/threonine-protein kinase B (Akt) and glycogen synthase kinase 3 beta (GSK3β) following insulin administration, and upregulated PTP1B O-GlcNAcylation in HepG2 cells.
26402673	2	60	theme	O-GlcNAc	350:357	arg1	modification					359:370	O-GlcNAc modification	350:370	O-GlcNAc modification	350:370	Accumulating evidence has demonstrated that O-GlcNAc modification regulates functions of several important components of insulin signal pathway.
31866147	0	0	theme	Complex	84:90	arg1	Formation					59:67	Formation	59:67	Formation of the B-TFIID Complex	59:90	TATA-Box Binding Protein O-GlcNAcylation at T114 Regulates Formation of the B-TFIID Complex and Is Critical for Metabolic Gene Regulation.
31866147	4	1	from	T114	581:584	arg1	O-GlcNAcylation					562:576	O-GlcNAcylation	562:576	O-GlcNAcylation at T114 of TBP	562:591	We show that O-GlcNAcylation at T114 of TBP blocks its interaction with BTAF1, hence the formation of the B-TFIID complex, and its dynamic cycling on and off of DNA.
31866147	4	2	theme	B-TFIID	655:661	arg1	complex					663:669	the B-TFIID complex	651:669	the B-TFIID complex	651:669	We show that O-GlcNAcylation at T114 of TBP blocks its interaction with BTAF1, hence the formation of the B-TFIID complex, and its dynamic cycling on and off of DNA.
31866147	0	3	theme	B-TFIID	76:82	arg1	Complex					84:90	the B-TFIID Complex	72:90	the B-TFIID Complex	72:90	TATA-Box Binding Protein O-GlcNAcylation at T114 Regulates Formation of the B-TFIID Complex and Is Critical for Metabolic Gene Regulation.
31866147	1	4	theme	gene	154:157	arg1	expression					159:168	gene expression	154:168	gene expression	154:168	In eukaryotes, gene expression is performed by three RNA polymerases that are targeted to promoters by molecular complexes.
31866147	1	5	theme	molecular	242:250	arg1	complexes					252:260	molecular complexes	242:260	molecular complexes	242:260	In eukaryotes, gene expression is performed by three RNA polymerases that are targeted to promoters by molecular complexes.
31866147	6	6	theme	transcriptome	1054:1066	arg1	modification					1034:1045	a profound modification	1023:1045	a profound modification of the transcriptome	1023:1066	Lack of O-GlcNAcylation at T114 is associated with a striking reprogramming of cellular metabolism induced by a profound modification of the transcriptome, leading to gross alterations in lipid storage.
31866147	4	7	from	formation	638:646	arg1	and					699:701	and	699:701	and	699:701	We show that O-GlcNAcylation at T114 of TBP blocks its interaction with BTAF1, hence the formation of the B-TFIID complex, and its dynamic cycling on and off of DNA.
31866147	2	8	theme	binding	300:306	arg1	TBP					317:319	TBP	317:319	TBP	317:319	A unique common factor, the TATA-box binding protein (TBP), is thought to serve as a platform to assemble pre-initiation complexes competent for transcription.
31866147	2	8	theme	binding	300:306	arg1	protein					308:314	TATA-box binding protein	291:314	the TATA-box binding protein (TBP)	287:320	A unique common factor, the TATA-box binding protein (TBP), is thought to serve as a platform to assemble pre-initiation complexes competent for transcription.
31866147	2	8	theme	binding	300:306	arg1	factor					279:284	A unique common factor	263:284	A unique common factor	263:284	A unique common factor, the TATA-box binding protein (TBP), is thought to serve as a platform to assemble pre-initiation complexes competent for transcription.
31866147	5	9	theme	TBPT114A	758:765	arg1	cells					786:790	TBPT114A CRISPR/Cas9-edited cells	758:790	TBPT114A CRISPR/Cas9-edited cells	758:790	Transcriptomic and metabolomic analyses of TBPT114A CRISPR/Cas9-edited cells showed that loss of O-GlcNAcylation at T114 increases TBP binding to BTAF1 and directly impacts expression of 408 genes.
31866147	3	10	theme	dynamic	517:523	arg1	O-GlcNAcylation					525:539	dynamic O-GlcNAcylation	517:539	dynamic O-GlcNAcylation of TBP	517:546	Here, we describe a novel molecular mechanism of nutrient regulation of gene transcription by dynamic O-GlcNAcylation of TBP.
31866147	2	11	theme	common	272:277	arg1	protein					308:314	TATA-box binding protein	291:314	the TATA-box binding protein (TBP)	287:320	A unique common factor, the TATA-box binding protein (TBP), is thought to serve as a platform to assemble pre-initiation complexes competent for transcription.
31866147	2	11	theme	common	272:277	arg1	factor					279:284	A unique common factor	263:284	A unique common factor	263:284	A unique common factor, the TATA-box binding protein (TBP), is thought to serve as a platform to assemble pre-initiation complexes competent for transcription.
31866147	2	11	theme	common	272:277	arg1	platform					348:355	a platform	346:355	a platform	346:355	A unique common factor, the TATA-box binding protein (TBP), is thought to serve as a platform to assemble pre-initiation complexes competent for transcription.
31866147	2	12	theme	pre-initiation	369:382	arg1	complexes					384:392	pre-initiation complexes	369:392	pre-initiation complexes competent for transcription	369:420	A unique common factor, the TATA-box binding protein (TBP), is thought to serve as a platform to assemble pre-initiation complexes competent for transcription.
31866147	3	13	theme	gene	495:498	arg1	transcription					500:512	gene transcription	495:512	gene transcription	495:512	Here, we describe a novel molecular mechanism of nutrient regulation of gene transcription by dynamic O-GlcNAcylation of TBP.
31866147	5	14	theme	O-GlcNAcylation	812:826	arg1	loss					804:807	loss	804:807	loss of O-GlcNAcylation at T114	804:834	Transcriptomic and metabolomic analyses of TBPT114A CRISPR/Cas9-edited cells showed that loss of O-GlcNAcylation at T114 increases TBP binding to BTAF1 and directly impacts expression of 408 genes.
31866147	0	15	from	T114	44:47	arg1	O-GlcNAcylation					25:39	TATA-Box Binding Protein O-GlcNAcylation	0:39	TATA-Box Binding Protein O-GlcNAcylation at T114	0:47	TATA-Box Binding Protein O-GlcNAcylation at T114 Regulates Formation of the B-TFIID Complex and Is Critical for Metabolic Gene Regulation.
31866147	6	16	from	T114	940:943	arg1	Lack					913:916	Lack	913:916	Lack of O-GlcNAcylation at T114	913:943	Lack of O-GlcNAcylation at T114 is associated with a striking reprogramming of cellular metabolism induced by a profound modification of the transcriptome, leading to gross alterations in lipid storage.
31866147	3	17	theme	transcription	500:512	arg1	regulation					481:490	nutrient regulation	472:490	nutrient regulation of gene transcription by dynamic O-GlcNAcylation of TBP	472:546	Here, we describe a novel molecular mechanism of nutrient regulation of gene transcription by dynamic O-GlcNAcylation of TBP.
31866147	0	18	theme	Binding	9:15	arg1	O-GlcNAcylation					25:39	TATA-Box Binding Protein O-GlcNAcylation	0:39	TATA-Box Binding Protein O-GlcNAcylation at T114	0:47	TATA-Box Binding Protein O-GlcNAcylation at T114 Regulates Formation of the B-TFIID Complex and Is Critical for Metabolic Gene Regulation.
31866147	4	19	with	formation	638:646	arg1	BTAF1					621:625	BTAF1	621:625	BTAF1	621:625	We show that O-GlcNAcylation at T114 of TBP blocks its interaction with BTAF1, hence the formation of the B-TFIID complex, and its dynamic cycling on and off of DNA.
31866147	3	20	theme	TBP	544:546	arg1	O-GlcNAcylation					525:539	dynamic O-GlcNAcylation	517:539	dynamic O-GlcNAcylation of TBP	517:546	Here, we describe a novel molecular mechanism of nutrient regulation of gene transcription by dynamic O-GlcNAcylation of TBP.
31866147	6	21	theme	profound	1025:1032	arg1	modification					1034:1045	a profound modification	1023:1045	a profound modification of the transcriptome	1023:1066	Lack of O-GlcNAcylation at T114 is associated with a striking reprogramming of cellular metabolism induced by a profound modification of the transcriptome, leading to gross alterations in lipid storage.
31866147	0	22	theme	TATA-Box	0:7	arg1	O-GlcNAcylation					25:39	TATA-Box Binding Protein O-GlcNAcylation	0:39	TATA-Box Binding Protein O-GlcNAcylation at T114	0:47	TATA-Box Binding Protein O-GlcNAcylation at T114 Regulates Formation of the B-TFIID Complex and Is Critical for Metabolic Gene Regulation.
31866147	4	23	from	cycling	688:694	arg1	and					699:701	and	699:701	and	699:701	We show that O-GlcNAcylation at T114 of TBP blocks its interaction with BTAF1, hence the formation of the B-TFIID complex, and its dynamic cycling on and off of DNA.
31866147	2	24	theme	TATA-box	291:298	arg1	TBP					317:319	TBP	317:319	TBP	317:319	A unique common factor, the TATA-box binding protein (TBP), is thought to serve as a platform to assemble pre-initiation complexes competent for transcription.
31866147	2	24	theme	TATA-box	291:298	arg1	protein					308:314	TATA-box binding protein	291:314	the TATA-box binding protein (TBP)	287:320	A unique common factor, the TATA-box binding protein (TBP), is thought to serve as a platform to assemble pre-initiation complexes competent for transcription.
31866147	2	24	theme	TATA-box	291:298	arg1	factor					279:284	A unique common factor	263:284	A unique common factor	263:284	A unique common factor, the TATA-box binding protein (TBP), is thought to serve as a platform to assemble pre-initiation complexes competent for transcription.
31866147	5	25	theme	CRISPR/Cas9-edited	767:784	arg1	cells					786:790	TBPT114A CRISPR/Cas9-edited cells	758:790	TBPT114A CRISPR/Cas9-edited cells	758:790	Transcriptomic and metabolomic analyses of TBPT114A CRISPR/Cas9-edited cells showed that loss of O-GlcNAcylation at T114 increases TBP binding to BTAF1 and directly impacts expression of 408 genes.
31866147	4	26	theme	dynamic	680:686	arg1	cycling					688:694	its dynamic cycling	676:694	its dynamic cycling on and off of DNA	676:712	We show that O-GlcNAcylation at T114 of TBP blocks its interaction with BTAF1, hence the formation of the B-TFIID complex, and its dynamic cycling on and off of DNA.
31866147	0	27	theme	Gene	122:125	arg1	Regulation					127:136	Metabolic Gene Regulation	112:136	Metabolic Gene Regulation	112:136	TATA-Box Binding Protein O-GlcNAcylation at T114 Regulates Formation of the B-TFIID Complex and Is Critical for Metabolic Gene Regulation.
31866147	5	28	theme	genes	906:910	arg1	expression					888:897	expression	888:897	expression of 408 genes	888:910	Transcriptomic and metabolomic analyses of TBPT114A CRISPR/Cas9-edited cells showed that loss of O-GlcNAcylation at T114 increases TBP binding to BTAF1 and directly impacts expression of 408 genes.
31866147	4	29	from	interaction	604:614	arg1	and					699:701	and	699:701	and	699:701	We show that O-GlcNAcylation at T114 of TBP blocks its interaction with BTAF1, hence the formation of the B-TFIID complex, and its dynamic cycling on and off of DNA.
31866147	2	30	theme	competent	394:402	arg1	complexes					384:392	pre-initiation complexes	369:392	pre-initiation complexes competent for transcription	369:420	A unique common factor, the TATA-box binding protein (TBP), is thought to serve as a platform to assemble pre-initiation complexes competent for transcription.
31866147	0	31	theme	Metabolic	112:120	arg1	Regulation					127:136	Metabolic Gene Regulation	112:136	Metabolic Gene Regulation	112:136	TATA-Box Binding Protein O-GlcNAcylation at T114 Regulates Formation of the B-TFIID Complex and Is Critical for Metabolic Gene Regulation.
31866147	3	32	theme	nutrient	472:479	arg1	regulation					481:490	nutrient regulation	472:490	nutrient regulation of gene transcription by dynamic O-GlcNAcylation of TBP	472:546	Here, we describe a novel molecular mechanism of nutrient regulation of gene transcription by dynamic O-GlcNAcylation of TBP.
31866147	1	33	theme	RNA	192:194	arg1	polymerases					196:206	three RNA polymerases	186:206	three RNA polymerases that are targeted to promoters by molecular complexes	186:260	In eukaryotes, gene expression is performed by three RNA polymerases that are targeted to promoters by molecular complexes.
31866147	5	34	theme	Transcriptomic	715:728	arg1	analyses					746:753	Transcriptomic and metabolomic analyses	715:753	Transcriptomic and metabolomic analyses of TBPT114A CRISPR/Cas9-edited cells	715:790	Transcriptomic and metabolomic analyses of TBPT114A CRISPR/Cas9-edited cells showed that loss of O-GlcNAcylation at T114 increases TBP binding to BTAF1 and directly impacts expression of 408 genes.
31866147	6	35	theme	metabolism	1001:1010	arg1	reprogramming					975:987	a striking reprogramming	964:987	a striking reprogramming of cellular metabolism induced by a profound modification of the transcriptome	964:1066	Lack of O-GlcNAcylation at T114 is associated with a striking reprogramming of cellular metabolism induced by a profound modification of the transcriptome, leading to gross alterations in lipid storage.
31866147	6	36	theme	striking	966:973	arg1	reprogramming					975:987	a striking reprogramming	964:987	a striking reprogramming of cellular metabolism induced by a profound modification of the transcriptome	964:1066	Lack of O-GlcNAcylation at T114 is associated with a striking reprogramming of cellular metabolism induced by a profound modification of the transcriptome, leading to gross alterations in lipid storage.
31866147	6	37	theme	cellular	992:999	arg1	metabolism					1001:1010	cellular metabolism	992:1010	cellular metabolism induced by a profound modification of the transcriptome	992:1066	Lack of O-GlcNAcylation at T114 is associated with a striking reprogramming of cellular metabolism induced by a profound modification of the transcriptome, leading to gross alterations in lipid storage.
31866147	5	38	theme	metabolomic	734:744	arg1	analyses					746:753	Transcriptomic and metabolomic analyses	715:753	Transcriptomic and metabolomic analyses of TBPT114A CRISPR/Cas9-edited cells	715:790	Transcriptomic and metabolomic analyses of TBPT114A CRISPR/Cas9-edited cells showed that loss of O-GlcNAcylation at T114 increases TBP binding to BTAF1 and directly impacts expression of 408 genes.
31866147	5	39	theme	TBP	846:848	arg1	binding					850:856	TBP binding	846:856	TBP binding to BTAF1	846:865	Transcriptomic and metabolomic analyses of TBPT114A CRISPR/Cas9-edited cells showed that loss of O-GlcNAcylation at T114 increases TBP binding to BTAF1 and directly impacts expression of 408 genes.
31866147	6	40	theme	O-GlcNAcylation	921:935	arg1	Lack					913:916	Lack	913:916	Lack of O-GlcNAcylation at T114	913:943	Lack of O-GlcNAcylation at T114 is associated with a striking reprogramming of cellular metabolism induced by a profound modification of the transcriptome, leading to gross alterations in lipid storage.
31866147	3	41	theme	molecular	449:457	arg1	mechanism					459:467	a novel molecular mechanism	441:467	a novel molecular mechanism of nutrient regulation of gene transcription by dynamic O-GlcNAcylation of TBP	441:546	Here, we describe a novel molecular mechanism of nutrient regulation of gene transcription by dynamic O-GlcNAcylation of TBP.
31866147	4	42	with	cycling	688:694	arg1	BTAF1					621:625	BTAF1	621:625	BTAF1	621:625	We show that O-GlcNAcylation at T114 of TBP blocks its interaction with BTAF1, hence the formation of the B-TFIID complex, and its dynamic cycling on and off of DNA.
31866147	2	43	theme	unique	265:270	arg1	protein					308:314	TATA-box binding protein	291:314	the TATA-box binding protein (TBP)	287:320	A unique common factor, the TATA-box binding protein (TBP), is thought to serve as a platform to assemble pre-initiation complexes competent for transcription.
31866147	2	43	theme	unique	265:270	arg1	factor					279:284	A unique common factor	263:284	A unique common factor	263:284	A unique common factor, the TATA-box binding protein (TBP), is thought to serve as a platform to assemble pre-initiation complexes competent for transcription.
31866147	2	43	theme	unique	265:270	arg1	platform					348:355	a platform	346:355	a platform	346:355	A unique common factor, the TATA-box binding protein (TBP), is thought to serve as a platform to assemble pre-initiation complexes competent for transcription.
31866147	4	44	theme	complex	663:669	arg1	interaction					604:614	its interaction	600:614	its interaction with BTAF1	600:625	We show that O-GlcNAcylation at T114 of TBP blocks its interaction with BTAF1, hence the formation of the B-TFIID complex, and its dynamic cycling on and off of DNA.
31866147	4	44	theme	complex	663:669	arg1	formation					638:646	hence the formation	628:646	hence the formation of the B-TFIID complex	628:669	We show that O-GlcNAcylation at T114 of TBP blocks its interaction with BTAF1, hence the formation of the B-TFIID complex, and its dynamic cycling on and off of DNA.
31866147	4	44	theme	complex	663:669	arg1	cycling					688:694	its dynamic cycling	676:694	its dynamic cycling on and off of DNA	676:712	We show that O-GlcNAcylation at T114 of TBP blocks its interaction with BTAF1, hence the formation of the B-TFIID complex, and its dynamic cycling on and off of DNA.
31866147	4	45	with	interaction	604:614	arg1	BTAF1					621:625	BTAF1	621:625	BTAF1	621:625	We show that O-GlcNAcylation at T114 of TBP blocks its interaction with BTAF1, hence the formation of the B-TFIID complex, and its dynamic cycling on and off of DNA.
31866147	6	46	from	alterations	1086:1096	arg1	storage					1107:1113	lipid storage	1101:1113	lipid storage	1101:1113	Lack of O-GlcNAcylation at T114 is associated with a striking reprogramming of cellular metabolism induced by a profound modification of the transcriptome, leading to gross alterations in lipid storage.
31866147	6	47	theme	gross	1080:1084	arg1	alterations					1086:1096	gross alterations	1080:1096	gross alterations in lipid storage	1080:1113	Lack of O-GlcNAcylation at T114 is associated with a striking reprogramming of cellular metabolism induced by a profound modification of the transcriptome, leading to gross alterations in lipid storage.
31866147	5	48	theme	cells	786:790	arg1	analyses					746:753	Transcriptomic and metabolomic analyses	715:753	Transcriptomic and metabolomic analyses of TBPT114A CRISPR/Cas9-edited cells	715:790	Transcriptomic and metabolomic analyses of TBPT114A CRISPR/Cas9-edited cells showed that loss of O-GlcNAcylation at T114 increases TBP binding to BTAF1 and directly impacts expression of 408 genes.
31866147	5	49	from	T114	831:834	arg1	loss					804:807	loss	804:807	loss of O-GlcNAcylation at T114	804:834	Transcriptomic and metabolomic analyses of TBPT114A CRISPR/Cas9-edited cells showed that loss of O-GlcNAcylation at T114 increases TBP binding to BTAF1 and directly impacts expression of 408 genes.
31866147	3	50	theme	novel	443:447	arg1	mechanism					459:467	a novel molecular mechanism	441:467	a novel molecular mechanism of nutrient regulation of gene transcription by dynamic O-GlcNAcylation of TBP	441:546	Here, we describe a novel molecular mechanism of nutrient regulation of gene transcription by dynamic O-GlcNAcylation of TBP.
31866147	3	51	theme	regulation	481:490	arg1	mechanism					459:467	a novel molecular mechanism	441:467	a novel molecular mechanism of nutrient regulation of gene transcription by dynamic O-GlcNAcylation of TBP	441:546	Here, we describe a novel molecular mechanism of nutrient regulation of gene transcription by dynamic O-GlcNAcylation of TBP.
31866147	4	52	theme	TBP	589:591	arg1	T114					581:584	T114	581:584	T114 of TBP	581:591	We show that O-GlcNAcylation at T114 of TBP blocks its interaction with BTAF1, hence the formation of the B-TFIID complex, and its dynamic cycling on and off of DNA.
31866147	6	53	theme	lipid	1101:1105	arg1	storage					1107:1113	lipid storage	1101:1113	lipid storage	1101:1113	Lack of O-GlcNAcylation at T114 is associated with a striking reprogramming of cellular metabolism induced by a profound modification of the transcriptome, leading to gross alterations in lipid storage.
31866147	0	54	theme	Protein	17:23	arg1	O-GlcNAcylation					25:39	TATA-Box Binding Protein O-GlcNAcylation	0:39	TATA-Box Binding Protein O-GlcNAcylation at T114	0:47	TATA-Box Binding Protein O-GlcNAcylation at T114 Regulates Formation of the B-TFIID Complex and Is Critical for Metabolic Gene Regulation.
31866147	4	55	dep	DNA	710:712	arg1	off					703:705	off	703:705	off	703:705	We show that O-GlcNAcylation at T114 of TBP blocks its interaction with BTAF1, hence the formation of the B-TFIID complex, and its dynamic cycling on and off of DNA.
30953348	0	0	theme	O-GlcNAc	69:76	arg1	transferase					78:88	O-GlcNAc transferase	69:88	O-GlcNAc transferase	69:88	Hepatocyte nuclear factor 1 alpha (HNF1A) regulates transcription of O-GlcNAc transferase in a negative feedback mechanism.
30953348	6	1	from	Thr563/564	893:902	arg1	loss					852:855	loss	852:855	loss of O-GlcNAcylation at Ser303/304 or Thr563/564	852:902	We further found that loss of O-GlcNAcylation at Ser303/304 or Thr563/564 significantly elevates ogt transcription.
30953348	7	2	theme	negative	973:980	arg1	mechanism					991:999	a negative feedback mechanism	971:999	a negative feedback mechanism for ogt transcription, which partially explains the homeostasis of cellular O-GlcNAcylation	971:1091	These findings highlight a negative feedback mechanism for ogt transcription, which partially explains the homeostasis of cellular O-GlcNAcylation.
30953348	7	3	theme	O-GlcNAcylation	1077:1091	arg1	homeostasis					1053:1063	the homeostasis	1049:1063	the homeostasis of cellular O-GlcNAcylation	1049:1091	These findings highlight a negative feedback mechanism for ogt transcription, which partially explains the homeostasis of cellular O-GlcNAcylation.
30953348	2	4	theme	homologue	330:338	arg1	A					340:340	the hepatocyte nuclear factor 1 homologue A	298:340	the hepatocyte nuclear factor 1 homologue A (HNF1A) in HEK293T cells	298:365	In the present study, we report the regulation of ogt transcription by the hepatocyte nuclear factor 1 homologue A (HNF1A) in HEK293T cells.
30953348	2	4	theme	homologue	330:338	arg1	HNF1A					343:347	HNF1A	343:347	HNF1A	343:347	In the present study, we report the regulation of ogt transcription by the hepatocyte nuclear factor 1 homologue A (HNF1A) in HEK293T cells.
30953348	4	5	theme	ogt	517:519	arg1	transcription					521:533	ogt transcription	517:533	ogt transcription	517:533	We found that HNF1A regulates ogt transcription in a time-dependent manner and that O-GlcNAcylation of HNF1A represses ogt transcription.
30953348	5	6	theme	O-GlcNAc	708:715	arg1	Ser560					806:811	Ser560	806:811	Ser560	806:811	Electron-transfer dissociation based tandem mass spectrometry analysis revealed 14 O-GlcNAc sites on HNF1A, six of which are predominantly modified, including Ser303/304 , Ser471 , Ser560 and Thr563/564 .
30953348	5	6	theme	O-GlcNAc	708:715	arg1	Thr563/564					817:826	Thr563/564	817:826	Thr563/564	817:826	Electron-transfer dissociation based tandem mass spectrometry analysis revealed 14 O-GlcNAc sites on HNF1A, six of which are predominantly modified, including Ser303/304 , Ser471 , Ser560 and Thr563/564 .
30953348	5	6	theme	O-GlcNAc	708:715	arg1	sites					717:721	14 O-GlcNAc sites	705:721	14 O-GlcNAc sites	705:721	Electron-transfer dissociation based tandem mass spectrometry analysis revealed 14 O-GlcNAc sites on HNF1A, six of which are predominantly modified, including Ser303/304 , Ser471 , Ser560 and Thr563/564 .
30953348	5	6	theme	O-GlcNAc	708:715	arg1	Ser471					797:802	Ser471	797:802	Ser471	797:802	Electron-transfer dissociation based tandem mass spectrometry analysis revealed 14 O-GlcNAc sites on HNF1A, six of which are predominantly modified, including Ser303/304 , Ser471 , Ser560 and Thr563/564 .
30953348	0	7	theme	transferase	78:88	arg1	transcription					52:64	transcription	52:64	transcription of O-GlcNAc transferase	52:88	Hepatocyte nuclear factor 1 alpha (HNF1A) regulates transcription of O-GlcNAc transferase in a negative feedback mechanism.
30953348	6	8	theme	O-GlcNAcylation	860:874	arg1	loss					852:855	loss	852:855	loss of O-GlcNAcylation at Ser303/304 or Thr563/564	852:902	We further found that loss of O-GlcNAcylation at Ser303/304 or Thr563/564 significantly elevates ogt transcription.
30953348	1	9	gly	O-GlcNAcylation	169:183	arg1	events					219:224	diverse cellular events	202:224	diverse cellular events	202:224	O-GlcNAc transferase (OGT)-catalyzed protein O-GlcNAcylation is implicated in diverse cellular events.
30953348	2	10	theme	hepatocyte	302:311	arg1	factor					321:326	hepatocyte nuclear factor 1	302:328	the hepatocyte nuclear factor 1 homologue A (HNF1A) in HEK293T cells	298:365	In the present study, we report the regulation of ogt transcription by the hepatocyte nuclear factor 1 homologue A (HNF1A) in HEK293T cells.
30953348	0	11	theme	negative	95:102	arg1	mechanism					113:121	a negative feedback mechanism	93:121	a negative feedback mechanism	93:121	Hepatocyte nuclear factor 1 alpha (HNF1A) regulates transcription of O-GlcNAc transferase in a negative feedback mechanism.
30953348	3	12	theme	factor	473:478	arg1	HNF1A					480:484	the transcription factor HNF1A	455:484	the transcription factor HNF1A	455:484	We first identified a core ogt promoter (-150 to +200 bp) and confirmed its binding to the transcription factor HNF1A.
30953348	1	13	theme	-catalyzed	150:159	arg1	O-GlcNAcylation					169:183	O-GlcNAc transferase (OGT)-catalyzed protein O-GlcNAcylation	124:183	O-GlcNAc transferase (OGT)-catalyzed protein O-GlcNAcylation	124:183	O-GlcNAc transferase (OGT)-catalyzed protein O-GlcNAcylation is implicated in diverse cellular events.
30953348	2	14	from	A	340:340	arg1	cells					361:365	HEK293T cells	353:365	HEK293T cells	353:365	In the present study, we report the regulation of ogt transcription by the hepatocyte nuclear factor 1 homologue A (HNF1A) in HEK293T cells.
30953348	2	15	theme	HEK293T	353:359	arg1	cells					361:365	HEK293T cells	353:365	HEK293T cells	353:365	In the present study, we report the regulation of ogt transcription by the hepatocyte nuclear factor 1 homologue A (HNF1A) in HEK293T cells.
30953348	0	16	theme	nuclear	11:17	arg1	HNF1A					35:39	HNF1A	35:39	HNF1A	35:39	Hepatocyte nuclear factor 1 alpha (HNF1A) regulates transcription of O-GlcNAc transferase in a negative feedback mechanism.
30953348	0	16	theme	nuclear	11:17	arg1	alpha					28:32	Hepatocyte nuclear factor 1 alpha	0:32	Hepatocyte nuclear factor 1 alpha (HNF1A)	0:40	Hepatocyte nuclear factor 1 alpha (HNF1A) regulates transcription of O-GlcNAc transferase in a negative feedback mechanism.
30953348	4	17	theme	ogt	606:608	arg1	transcription					610:622	ogt transcription	606:622	ogt transcription	606:622	We found that HNF1A regulates ogt transcription in a time-dependent manner and that O-GlcNAcylation of HNF1A represses ogt transcription.
30953348	0	18	theme	Hepatocyte	0:9	arg1	HNF1A					35:39	HNF1A	35:39	HNF1A	35:39	Hepatocyte nuclear factor 1 alpha (HNF1A) regulates transcription of O-GlcNAc transferase in a negative feedback mechanism.
30953348	0	18	theme	Hepatocyte	0:9	arg1	alpha					28:32	Hepatocyte nuclear factor 1 alpha	0:32	Hepatocyte nuclear factor 1 alpha (HNF1A)	0:40	Hepatocyte nuclear factor 1 alpha (HNF1A) regulates transcription of O-GlcNAc transferase in a negative feedback mechanism.
30953348	7	19	theme	cellular	1068:1075	arg1	O-GlcNAcylation					1077:1091	cellular O-GlcNAcylation	1068:1091	cellular O-GlcNAcylation	1068:1091	These findings highlight a negative feedback mechanism for ogt transcription, which partially explains the homeostasis of cellular O-GlcNAcylation.
30953348	3	20	theme	core	390:393	arg1	promoter					399:406	a core ogt promoter	388:406	a core ogt promoter (-150 to +200 bp)	388:424	We first identified a core ogt promoter (-150 to +200 bp) and confirmed its binding to the transcription factor HNF1A.
30953348	3	20	theme	core	390:393	arg1	+200 bp					417:423	+200 bp	417:423	+200 bp	417:423	We first identified a core ogt promoter (-150 to +200 bp) and confirmed its binding to the transcription factor HNF1A.
30953348	5	21	theme	spectrometry	674:685	arg1	analysis					687:694	Electron-transfer dissociation based tandem mass spectrometry analysis	625:694	Electron-transfer dissociation based tandem mass spectrometry analysis	625:694	Electron-transfer dissociation based tandem mass spectrometry analysis revealed 14 O-GlcNAc sites on HNF1A, six of which are predominantly modified, including Ser303/304 , Ser471 , Ser560 and Thr563/564 .
30953348	2	22	theme	transcription	281:293	arg1	regulation					263:272	the regulation	259:272	the regulation of ogt transcription by the hepatocyte nuclear factor 1 homologue A (HNF1A) in HEK293T cells	259:365	In the present study, we report the regulation of ogt transcription by the hepatocyte nuclear factor 1 homologue A (HNF1A) in HEK293T cells.
30953348	0	23	theme	factor	19:24	arg1	HNF1A					35:39	HNF1A	35:39	HNF1A	35:39	Hepatocyte nuclear factor 1 alpha (HNF1A) regulates transcription of O-GlcNAc transferase in a negative feedback mechanism.
30953348	0	23	theme	factor	19:24	arg1	alpha					28:32	Hepatocyte nuclear factor 1 alpha	0:32	Hepatocyte nuclear factor 1 alpha (HNF1A)	0:40	Hepatocyte nuclear factor 1 alpha (HNF1A) regulates transcription of O-GlcNAc transferase in a negative feedback mechanism.
30953348	0	24	theme	feedback	104:111	arg1	mechanism					113:121	a negative feedback mechanism	93:121	a negative feedback mechanism	93:121	Hepatocyte nuclear factor 1 alpha (HNF1A) regulates transcription of O-GlcNAc transferase in a negative feedback mechanism.
30953348	2	25	theme	ogt	277:279	arg1	transcription					281:293	ogt transcription	277:293	ogt transcription	277:293	In the present study, we report the regulation of ogt transcription by the hepatocyte nuclear factor 1 homologue A (HNF1A) in HEK293T cells.
30953348	1	26	theme	diverse	202:208	arg1	events					219:224	diverse cellular events	202:224	diverse cellular events	202:224	O-GlcNAc transferase (OGT)-catalyzed protein O-GlcNAcylation is implicated in diverse cellular events.
30953348	3	27	theme	ogt	395:397	arg1	promoter					399:406	a core ogt promoter	388:406	a core ogt promoter (-150 to +200 bp)	388:424	We first identified a core ogt promoter (-150 to +200 bp) and confirmed its binding to the transcription factor HNF1A.
30953348	3	27	theme	ogt	395:397	arg1	+200 bp					417:423	+200 bp	417:423	+200 bp	417:423	We first identified a core ogt promoter (-150 to +200 bp) and confirmed its binding to the transcription factor HNF1A.
30953348	1	28	theme	cellular	210:217	arg1	events					219:224	diverse cellular events	202:224	diverse cellular events	202:224	O-GlcNAc transferase (OGT)-catalyzed protein O-GlcNAcylation is implicated in diverse cellular events.
30953348	6	29	theme	ogt	927:929	arg1	transcription					931:943	ogt transcription	927:943	ogt transcription	927:943	We further found that loss of O-GlcNAcylation at Ser303/304 or Thr563/564 significantly elevates ogt transcription.
30953348	5	30	theme	dissociation	643:654	arg1	analysis					687:694	Electron-transfer dissociation based tandem mass spectrometry analysis	625:694	Electron-transfer dissociation based tandem mass spectrometry analysis	625:694	Electron-transfer dissociation based tandem mass spectrometry analysis revealed 14 O-GlcNAc sites on HNF1A, six of which are predominantly modified, including Ser303/304 , Ser471 , Ser560 and Thr563/564 .
30953348	5	31	from	sites	717:721	arg1	HNF1A					726:730	HNF1A	726:730	HNF1A	726:730	Electron-transfer dissociation based tandem mass spectrometry analysis revealed 14 O-GlcNAc sites on HNF1A, six of which are predominantly modified, including Ser303/304 , Ser471 , Ser560 and Thr563/564 .
30953348	5	32	theme	based	656:660	arg1	analysis					687:694	Electron-transfer dissociation based tandem mass spectrometry analysis	625:694	Electron-transfer dissociation based tandem mass spectrometry analysis	625:694	Electron-transfer dissociation based tandem mass spectrometry analysis revealed 14 O-GlcNAc sites on HNF1A, six of which are predominantly modified, including Ser303/304 , Ser471 , Ser560 and Thr563/564 .
30953348	2	33	theme	factor	321:326	arg1	A					340:340	the hepatocyte nuclear factor 1 homologue A	298:340	the hepatocyte nuclear factor 1 homologue A (HNF1A) in HEK293T cells	298:365	In the present study, we report the regulation of ogt transcription by the hepatocyte nuclear factor 1 homologue A (HNF1A) in HEK293T cells.
30953348	2	33	theme	factor	321:326	arg1	HNF1A					343:347	HNF1A	343:347	HNF1A	343:347	In the present study, we report the regulation of ogt transcription by the hepatocyte nuclear factor 1 homologue A (HNF1A) in HEK293T cells.
30953348	3	34	dep	+200 bp	417:423	arg1	to					414:415	to	414:415	to	414:415	We first identified a core ogt promoter (-150 to +200 bp) and confirmed its binding to the transcription factor HNF1A.
30953348	5	35	theme	tandem	662:667	arg1	analysis					687:694	Electron-transfer dissociation based tandem mass spectrometry analysis	625:694	Electron-transfer dissociation based tandem mass spectrometry analysis	625:694	Electron-transfer dissociation based tandem mass spectrometry analysis revealed 14 O-GlcNAc sites on HNF1A, six of which are predominantly modified, including Ser303/304 , Ser471 , Ser560 and Thr563/564 .
30953348	7	36	theme	ogt	1005:1007	arg1	transcription					1009:1021	ogt transcription	1005:1021	ogt transcription	1005:1021	These findings highlight a negative feedback mechanism for ogt transcription, which partially explains the homeostasis of cellular O-GlcNAcylation.
30953348	2	37	theme	nuclear	313:319	arg1	factor					321:326	hepatocyte nuclear factor 1	302:328	the hepatocyte nuclear factor 1 homologue A (HNF1A) in HEK293T cells	298:365	In the present study, we report the regulation of ogt transcription by the hepatocyte nuclear factor 1 homologue A (HNF1A) in HEK293T cells.
30953348	5	38	theme	mass	669:672	arg1	analysis					687:694	Electron-transfer dissociation based tandem mass spectrometry analysis	625:694	Electron-transfer dissociation based tandem mass spectrometry analysis	625:694	Electron-transfer dissociation based tandem mass spectrometry analysis revealed 14 O-GlcNAc sites on HNF1A, six of which are predominantly modified, including Ser303/304 , Ser471 , Ser560 and Thr563/564 .
30953348	7	39	theme	feedback	982:989	arg1	mechanism					991:999	a negative feedback mechanism	971:999	a negative feedback mechanism for ogt transcription, which partially explains the homeostasis of cellular O-GlcNAcylation	971:1091	These findings highlight a negative feedback mechanism for ogt transcription, which partially explains the homeostasis of cellular O-GlcNAcylation.
30953348	1	40	theme	O-GlcNAc	124:131	arg1	OGT					146:148	OGT	146:148	OGT	146:148	O-GlcNAc transferase (OGT)-catalyzed protein O-GlcNAcylation is implicated in diverse cellular events.
30953348	1	40	theme	O-GlcNAc	124:131	arg1	transferase					133:143	O-GlcNAc transferase	124:143	O-GlcNAc transferase (OGT)-catalyzed protein O-GlcNAcylation	124:183	O-GlcNAc transferase (OGT)-catalyzed protein O-GlcNAcylation is implicated in diverse cellular events.
30953348	4	41	theme	time-dependent	540:553	arg1	manner					555:560	a time-dependent manner	538:560	a time-dependent manner	538:560	We found that HNF1A regulates ogt transcription in a time-dependent manner and that O-GlcNAcylation of HNF1A represses ogt transcription.
30953348	6	42	from	Ser303/304	879:888	arg1	loss					852:855	loss	852:855	loss of O-GlcNAcylation at Ser303/304 or Thr563/564	852:902	We further found that loss of O-GlcNAcylation at Ser303/304 or Thr563/564 significantly elevates ogt transcription.
30953348	4	43	theme	HNF1A	590:594	arg1	O-GlcNAcylation					571:585	O-GlcNAcylation	571:585	O-GlcNAcylation of HNF1A	571:594	We found that HNF1A regulates ogt transcription in a time-dependent manner and that O-GlcNAcylation of HNF1A represses ogt transcription.
30953348	1	44	theme	transferase	133:143	arg1	O-GlcNAcylation					169:183	O-GlcNAc transferase (OGT)-catalyzed protein O-GlcNAcylation	124:183	O-GlcNAc transferase (OGT)-catalyzed protein O-GlcNAcylation	124:183	O-GlcNAc transferase (OGT)-catalyzed protein O-GlcNAcylation is implicated in diverse cellular events.
30953348	1	45	theme	protein	161:167	arg1	O-GlcNAcylation					169:183	O-GlcNAc transferase (OGT)-catalyzed protein O-GlcNAcylation	124:183	O-GlcNAc transferase (OGT)-catalyzed protein O-GlcNAcylation	124:183	O-GlcNAc transferase (OGT)-catalyzed protein O-GlcNAcylation is implicated in diverse cellular events.
30953348	5	46	theme	Electron-transfer	625:641	arg1	analysis					687:694	Electron-transfer dissociation based tandem mass spectrometry analysis	625:694	Electron-transfer dissociation based tandem mass spectrometry analysis	625:694	Electron-transfer dissociation based tandem mass spectrometry analysis revealed 14 O-GlcNAc sites on HNF1A, six of which are predominantly modified, including Ser303/304 , Ser471 , Ser560 and Thr563/564 .
30953348	2	47	theme	present	234:240	arg1	study					242:246	the present study	230:246	the present study	230:246	In the present study, we report the regulation of ogt transcription by the hepatocyte nuclear factor 1 homologue A (HNF1A) in HEK293T cells.
30953348	3	48	theme	transcription	459:471	arg1	HNF1A					480:484	the transcription factor HNF1A	455:484	the transcription factor HNF1A	455:484	We first identified a core ogt promoter (-150 to +200 bp) and confirmed its binding to the transcription factor HNF1A.
30953348	5	49	theme	sites	717:721	arg1	Ser560					806:811	Ser560	806:811	Ser560	806:811	Electron-transfer dissociation based tandem mass spectrometry analysis revealed 14 O-GlcNAc sites on HNF1A, six of which are predominantly modified, including Ser303/304 , Ser471 , Ser560 and Thr563/564 .
30953348	5	49	theme	sites	717:721	arg1	six					733:735	six	733:735	six	733:735	Electron-transfer dissociation based tandem mass spectrometry analysis revealed 14 O-GlcNAc sites on HNF1A, six of which are predominantly modified, including Ser303/304 , Ser471 , Ser560 and Thr563/564 .
30953348	5	49	theme	sites	717:721	arg1	Thr563/564					817:826	Thr563/564	817:826	Thr563/564	817:826	Electron-transfer dissociation based tandem mass spectrometry analysis revealed 14 O-GlcNAc sites on HNF1A, six of which are predominantly modified, including Ser303/304 , Ser471 , Ser560 and Thr563/564 .
30953348	5	49	theme	sites	717:721	arg1	sites					717:721	14 O-GlcNAc sites	705:721	14 O-GlcNAc sites	705:721	Electron-transfer dissociation based tandem mass spectrometry analysis revealed 14 O-GlcNAc sites on HNF1A, six of which are predominantly modified, including Ser303/304 , Ser471 , Ser560 and Thr563/564 .
30953348	5	49	theme	sites	717:721	arg1	Ser471					797:802	Ser471	797:802	Ser471	797:802	Electron-transfer dissociation based tandem mass spectrometry analysis revealed 14 O-GlcNAc sites on HNF1A, six of which are predominantly modified, including Ser303/304 , Ser471 , Ser560 and Thr563/564 .
31061102	5	0	theme	O-GlcNAcylated	858:871	arg1	peptides					892:899	O-GlcNAcylated and phosphorylated peptides	858:899	O-GlcNAcylated and phosphorylated peptides	858:899	Over a vernalization time-course, O-GlcNAcylated and phosphorylated peptides were enriched from winter wheat plumules by Lectin weak affinity chromatography and iTRAQ-TiO2, respectively.
31061102	6	1	theme	gene	1044:1047	arg1	analysis					1074:1081	gene ontology term enrichment analysis	1044:1081	gene ontology term enrichment analysis	1044:1081	Subsequent mass spectrometry and gene ontology term enrichment analysis identified 168 O-GlcNAcylated proteins that are mainly involved in responses to abiotic stimulus and hormones, metabolic processing, and gene expression; and 124 differentially expressed phosphorylated proteins that participate in translation, transcription, and metabolic processing.
31061102	8	2	theme	TaVRN1	1817:1822	arg1	motif					1808:1812	the RIP3 motif	1799:1812	the RIP3 motif of TaVRN1	1799:1822	Among these, TaGRP2 was decorated with dynamic O-GlcNAcylation (S87) and phosphorylation (S152) modifications, and the mutation of S87 and S152 affected the binding of TaGRP2 to the RIP3 motif of TaVRN1 in vitro.
31061102	9	3	theme	phosphorylation	1897:1911	arg1	network					1866:1872	a dynamic network	1856:1872	a dynamic network of O-GlcNAcylation and phosphorylation at key pathway nodes	1856:1932	Our data suggest that a dynamic network of O-GlcNAcylation and phosphorylation at key pathway nodes regulate the vernalization response and mediate flowering in wheat.
31061102	4	4	theme	genes	769:773	arg1	expression					751:760	the expression	747:760	the expression of VRN genes	747:773	Altering O-GlcNAc signaling by chemical inhibitors affected the vernalization response, modifying the expression of VRN genes and subsequently affecting flowering transition.
31061102	0	5	theme	Winter	113:118	arg1	Wheat					120:124	Winter Wheat	113:124	Winter Wheat	113:124	The Protein Modifications of O-GlcNAcylation and Phosphorylation Mediate Vernalization Response for Flowering in Winter Wheat.
31061102	9	6	from	flowering	1982:1990	arg1	wheat					1995:1999	wheat	1995:1999	wheat	1995:1999	Our data suggest that a dynamic network of O-GlcNAcylation and phosphorylation at key pathway nodes regulate the vernalization response and mediate flowering in wheat.
31061102	4	7	theme	O-GlcNAc	658:665	arg1	signaling					667:675	O-GlcNAc signaling	658:675	O-GlcNAc signaling	658:675	Altering O-GlcNAc signaling by chemical inhibitors affected the vernalization response, modifying the expression of VRN genes and subsequently affecting flowering transition.
31061102	3	8	theme	O-GlcNAcylation	404:418	arg1	role					396:399	the role	392:399	the role of O-GlcNAcylation	392:418	Here we investigated the role of O-GlcNAcylation during vernalization, a process whereby prolonged cold exposure promotes flowering in winter wheat (Triticum aestivum), and analyzed the dynamic profile of O-GlcNAcylated and phosphorylated proteins in response to vernalization.
31061102	6	9	theme	mass	1022:1025	arg1	spectrometry					1027:1038	Subsequent mass spectrometry	1011:1038	Subsequent mass spectrometry	1011:1038	Subsequent mass spectrometry and gene ontology term enrichment analysis identified 168 O-GlcNAcylated proteins that are mainly involved in responses to abiotic stimulus and hormones, metabolic processing, and gene expression; and 124 differentially expressed phosphorylated proteins that participate in translation, transcription, and metabolic processing.
31061102	3	10	theme	phosphorylated	595:608	arg1	proteins					610:617	O-GlcNAcylated and phosphorylated proteins	576:617	O-GlcNAcylated and phosphorylated proteins	576:617	Here we investigated the role of O-GlcNAcylation during vernalization, a process whereby prolonged cold exposure promotes flowering in winter wheat (Triticum aestivum), and analyzed the dynamic profile of O-GlcNAcylated and phosphorylated proteins in response to vernalization.
31061102	8	11	theme	TaGRP2	1789:1794	arg1	binding					1778:1784	the binding	1774:1784	the binding of TaGRP2 to the RIP3 motif of TaVRN1	1774:1822	Among these, TaGRP2 was decorated with dynamic O-GlcNAcylation (S87) and phosphorylation (S152) modifications, and the mutation of S87 and S152 affected the binding of TaGRP2 to the RIP3 motif of TaVRN1 in vitro.
31061102	6	12	theme	Subsequent	1011:1020	arg1	spectrometry					1027:1038	Subsequent mass spectrometry	1011:1038	Subsequent mass spectrometry	1011:1038	Subsequent mass spectrometry and gene ontology term enrichment analysis identified 168 O-GlcNAcylated proteins that are mainly involved in responses to abiotic stimulus and hormones, metabolic processing, and gene expression; and 124 differentially expressed phosphorylated proteins that participate in translation, transcription, and metabolic processing.
31061102	5	13	theme	Lectin	945:950	arg1	chromatography					966:979	Lectin weak affinity chromatography	945:979	Lectin weak affinity chromatography	945:979	Over a vernalization time-course, O-GlcNAcylated and phosphorylated peptides were enriched from winter wheat plumules by Lectin weak affinity chromatography and iTRAQ-TiO2, respectively.
31061102	2	14	theme	protein	316:322	arg1	modifications					324:336	these two protein modifications	306:336	these two protein modifications	306:336	However, the regulation of and the cross talk between these two protein modifications are poorly understood in plants.
31061102	9	15	theme	vernalization	1947:1959	arg1	response					1961:1968	the vernalization response	1943:1968	the vernalization response	1943:1968	Our data suggest that a dynamic network of O-GlcNAcylation and phosphorylation at key pathway nodes regulate the vernalization response and mediate flowering in wheat.
31061102	3	16	dep	vernalization	634:646	arg1	response					622:629	response	622:629	response	622:629	Here we investigated the role of O-GlcNAcylation during vernalization, a process whereby prolonged cold exposure promotes flowering in winter wheat (Triticum aestivum), and analyzed the dynamic profile of O-GlcNAcylated and phosphorylated proteins in response to vernalization.
31061102	8	17	dep	O-GlcNAcylation	1668:1682	arg1	modifications					1717:1729	modifications	1717:1729	modifications	1717:1729	Among these, TaGRP2 was decorated with dynamic O-GlcNAcylation (S87) and phosphorylation (S152) modifications, and the mutation of S87 and S152 affected the binding of TaGRP2 to the RIP3 motif of TaVRN1 in vitro.
31061102	5	18	theme	phosphorylated	877:890	arg1	peptides					892:899	O-GlcNAcylated and phosphorylated peptides	858:899	O-GlcNAcylated and phosphorylated peptides	858:899	Over a vernalization time-course, O-GlcNAcylated and phosphorylated peptides were enriched from winter wheat plumules by Lectin weak affinity chromatography and iTRAQ-TiO2, respectively.
31061102	3	19	theme	O-GlcNAcylated	576:589	arg1	proteins					610:617	O-GlcNAcylated and phosphorylated proteins	576:617	O-GlcNAcylated and phosphorylated proteins	576:617	Here we investigated the role of O-GlcNAcylation during vernalization, a process whereby prolonged cold exposure promotes flowering in winter wheat (Triticum aestivum), and analyzed the dynamic profile of O-GlcNAcylated and phosphorylated proteins in response to vernalization.
31061102	8	20	theme	S87	1752:1754	arg1	mutation					1740:1747	the mutation	1736:1747	the mutation of S87 and S152	1736:1763	Among these, TaGRP2 was decorated with dynamic O-GlcNAcylation (S87) and phosphorylation (S152) modifications, and the mutation of S87 and S152 affected the binding of TaGRP2 to the RIP3 motif of TaVRN1 in vitro.
31061102	0	21	theme	Protein	4:10	arg1	Modifications					12:24	The Protein Modifications	0:24	The Protein Modifications of O-GlcNAcylation and Phosphorylation	0:63	The Protein Modifications of O-GlcNAcylation and Phosphorylation Mediate Vernalization Response for Flowering in Winter Wheat.
31061102	6	22	theme	gene	1220:1223	arg1	expression					1225:1234	gene expression	1220:1234	gene expression	1220:1234	Subsequent mass spectrometry and gene ontology term enrichment analysis identified 168 O-GlcNAcylated proteins that are mainly involved in responses to abiotic stimulus and hormones, metabolic processing, and gene expression; and 124 differentially expressed phosphorylated proteins that participate in translation, transcription, and metabolic processing.
31061102	7	23	contain	carried	1435:1441	arg2	phosphorylation					1448:1462	phosphorylation	1448:1462	phosphorylation	1448:1462	Of note, 31 vernalization-associated proteins were identified that carried both phosphorylation and O-GlcNAcylation modifications, of which the majority (97%) exhibited the coexisting module and the remainder exhibited the potential competitive module.
31061102	7	23	contain	carried	1435:1441	arg1	that					1430:1433	that	1430:1433	that	1430:1433	Of note, 31 vernalization-associated proteins were identified that carried both phosphorylation and O-GlcNAcylation modifications, of which the majority (97%) exhibited the coexisting module and the remainder exhibited the potential competitive module.
31061102	7	23	contain	carried	1435:1441	arg2	modifications					1484:1496	O-GlcNAcylation modifications	1468:1496	O-GlcNAcylation modifications	1468:1496	Of note, 31 vernalization-associated proteins were identified that carried both phosphorylation and O-GlcNAcylation modifications, of which the majority (97%) exhibited the coexisting module and the remainder exhibited the potential competitive module.
31061102	1	24	theme	protein	234:240	arg1	function					242:249	protein function	234:249	protein function	234:249	O-GlcNAcylation and phosphorylation are two posttranslational modifications that antagonistically regulate protein function.
31061102	5	25	theme	winter	920:925	arg1	plumules					933:940	winter wheat plumules	920:940	winter wheat plumules	920:940	Over a vernalization time-course, O-GlcNAcylated and phosphorylated peptides were enriched from winter wheat plumules by Lectin weak affinity chromatography and iTRAQ-TiO2, respectively.
31061102	6	26	theme	term	1058:1061	arg1	analysis					1074:1081	gene ontology term enrichment analysis	1044:1081	gene ontology term enrichment analysis	1044:1081	Subsequent mass spectrometry and gene ontology term enrichment analysis identified 168 O-GlcNAcylated proteins that are mainly involved in responses to abiotic stimulus and hormones, metabolic processing, and gene expression; and 124 differentially expressed phosphorylated proteins that participate in translation, transcription, and metabolic processing.
31061102	7	27	theme	O-GlcNAcylation	1468:1482	arg1	modifications					1484:1496	O-GlcNAcylation modifications	1468:1496	O-GlcNAcylation modifications	1468:1496	Of note, 31 vernalization-associated proteins were identified that carried both phosphorylation and O-GlcNAcylation modifications, of which the majority (97%) exhibited the coexisting module and the remainder exhibited the potential competitive module.
31061102	5	28	theme	wheat	927:931	arg1	plumules					933:940	winter wheat plumules	920:940	winter wheat plumules	920:940	Over a vernalization time-course, O-GlcNAcylated and phosphorylated peptides were enriched from winter wheat plumules by Lectin weak affinity chromatography and iTRAQ-TiO2, respectively.
31061102	9	29	theme	pathway	1920:1926	arg1	nodes					1928:1932	key pathway nodes	1916:1932	key pathway nodes	1916:1932	Our data suggest that a dynamic network of O-GlcNAcylation and phosphorylation at key pathway nodes regulate the vernalization response and mediate flowering in wheat.
31061102	7	30	theme	coexisting	1541:1550	arg1	module					1552:1557	the coexisting module	1537:1557	the coexisting module	1537:1557	Of note, 31 vernalization-associated proteins were identified that carried both phosphorylation and O-GlcNAcylation modifications, of which the majority (97%) exhibited the coexisting module and the remainder exhibited the potential competitive module.
31061102	3	31	theme	proteins	610:617	arg1	profile					565:571	the dynamic profile	553:571	the dynamic profile of O-GlcNAcylated and phosphorylated proteins	553:617	Here we investigated the role of O-GlcNAcylation during vernalization, a process whereby prolonged cold exposure promotes flowering in winter wheat (Triticum aestivum), and analyzed the dynamic profile of O-GlcNAcylated and phosphorylated proteins in response to vernalization.
31061102	6	32	theme	metabolic	1194:1202	arg1	processing					1204:1213	metabolic processing	1194:1213	metabolic processing	1194:1213	Subsequent mass spectrometry and gene ontology term enrichment analysis identified 168 O-GlcNAcylated proteins that are mainly involved in responses to abiotic stimulus and hormones, metabolic processing, and gene expression; and 124 differentially expressed phosphorylated proteins that participate in translation, transcription, and metabolic processing.
31061102	6	33	theme	O-GlcNAcylated	1098:1111	arg1	proteins					1113:1120	168 O-GlcNAcylated proteins	1094:1120	168 O-GlcNAcylated proteins that are mainly involved in responses to abiotic stimulus and hormones, metabolic processing, and gene expression	1094:1234	Subsequent mass spectrometry and gene ontology term enrichment analysis identified 168 O-GlcNAcylated proteins that are mainly involved in responses to abiotic stimulus and hormones, metabolic processing, and gene expression; and 124 differentially expressed phosphorylated proteins that participate in translation, transcription, and metabolic processing.
31061102	7	34	theme	potential	1591:1599	arg1	module					1613:1618	the potential competitive module	1587:1618	the potential competitive module	1587:1618	Of note, 31 vernalization-associated proteins were identified that carried both phosphorylation and O-GlcNAcylation modifications, of which the majority (97%) exhibited the coexisting module and the remainder exhibited the potential competitive module.
31061102	9	35	from	nodes	1928:1932	arg1	network					1866:1872	a dynamic network	1856:1872	a dynamic network of O-GlcNAcylation and phosphorylation at key pathway nodes	1856:1932	Our data suggest that a dynamic network of O-GlcNAcylation and phosphorylation at key pathway nodes regulate the vernalization response and mediate flowering in wheat.
31061102	4	36	theme	VRN	765:767	arg1	genes					769:773	VRN genes	765:773	VRN genes	765:773	Altering O-GlcNAc signaling by chemical inhibitors affected the vernalization response, modifying the expression of VRN genes and subsequently affecting flowering transition.
31061102	3	37	theme	prolonged	460:468	arg1	exposure					475:482	prolonged cold exposure	460:482	prolonged cold exposure	460:482	Here we investigated the role of O-GlcNAcylation during vernalization, a process whereby prolonged cold exposure promotes flowering in winter wheat (Triticum aestivum), and analyzed the dynamic profile of O-GlcNAcylated and phosphorylated proteins in response to vernalization.
31061102	5	38	theme	weak	952:955	arg1	chromatography					966:979	Lectin weak affinity chromatography	945:979	Lectin weak affinity chromatography	945:979	Over a vernalization time-course, O-GlcNAcylated and phosphorylated peptides were enriched from winter wheat plumules by Lectin weak affinity chromatography and iTRAQ-TiO2, respectively.
31061102	6	39	theme	metabolic	1346:1354	arg1	processing					1356:1365	metabolic processing	1346:1365	metabolic processing	1346:1365	Subsequent mass spectrometry and gene ontology term enrichment analysis identified 168 O-GlcNAcylated proteins that are mainly involved in responses to abiotic stimulus and hormones, metabolic processing, and gene expression; and 124 differentially expressed phosphorylated proteins that participate in translation, transcription, and metabolic processing.
31061102	3	40	theme	winter	506:511	arg1	wheat					513:517	winter wheat	506:517	winter wheat (Triticum aestivum)	506:537	Here we investigated the role of O-GlcNAcylation during vernalization, a process whereby prolonged cold exposure promotes flowering in winter wheat (Triticum aestivum), and analyzed the dynamic profile of O-GlcNAcylated and phosphorylated proteins in response to vernalization.
31061102	3	40	theme	winter	506:511	arg1	Triticum					520:527	Triticum	520:527	Triticum	520:527	Here we investigated the role of O-GlcNAcylation during vernalization, a process whereby prolonged cold exposure promotes flowering in winter wheat (Triticum aestivum), and analyzed the dynamic profile of O-GlcNAcylated and phosphorylated proteins in response to vernalization.
31061102	0	41	theme	O-GlcNAcylation	29:43	arg1	Modifications					12:24	The Protein Modifications	0:24	The Protein Modifications of O-GlcNAcylation and Phosphorylation	0:63	The Protein Modifications of O-GlcNAcylation and Phosphorylation Mediate Vernalization Response for Flowering in Winter Wheat.
31061102	0	42	mod	Modifications	12:24	arg3	Protein					4:10	The Protein Modifications	0:24	The Protein Modifications of O-GlcNAcylation and Phosphorylation	0:63	The Protein Modifications of O-GlcNAcylation and Phosphorylation Mediate Vernalization Response for Flowering in Winter Wheat.
31061102	0	42	mod	Modifications	12:24	arg1	Phosphorylation					49:63	Phosphorylation	49:63	Phosphorylation	49:63	The Protein Modifications of O-GlcNAcylation and Phosphorylation Mediate Vernalization Response for Flowering in Winter Wheat.
31061102	0	42	mod	Modifications	12:24	arg1	O-GlcNAcylation					29:43	O-GlcNAcylation	29:43	O-GlcNAcylation	29:43	The Protein Modifications of O-GlcNAcylation and Phosphorylation Mediate Vernalization Response for Flowering in Winter Wheat.
31061102	3	43	theme	cold	470:473	arg1	exposure					475:482	prolonged cold exposure	460:482	prolonged cold exposure	460:482	Here we investigated the role of O-GlcNAcylation during vernalization, a process whereby prolonged cold exposure promotes flowering in winter wheat (Triticum aestivum), and analyzed the dynamic profile of O-GlcNAcylated and phosphorylated proteins in response to vernalization.
31061102	0	44	from	Response	87:94	arg1	Wheat					120:124	Winter Wheat	113:124	Winter Wheat	113:124	The Protein Modifications of O-GlcNAcylation and Phosphorylation Mediate Vernalization Response for Flowering in Winter Wheat.
31061102	4	45	theme	vernalization	713:725	arg1	response					727:734	the vernalization response	709:734	the vernalization response	709:734	Altering O-GlcNAc signaling by chemical inhibitors affected the vernalization response, modifying the expression of VRN genes and subsequently affecting flowering transition.
31061102	9	46	theme	key	1916:1918	arg1	nodes					1928:1932	key pathway nodes	1916:1932	key pathway nodes	1916:1932	Our data suggest that a dynamic network of O-GlcNAcylation and phosphorylation at key pathway nodes regulate the vernalization response and mediate flowering in wheat.
31061102	7	47	theme	vernalization-associated	1380:1403	arg1	proteins					1405:1412	31 vernalization-associated proteins	1377:1412	31 vernalization-associated proteins	1377:1412	Of note, 31 vernalization-associated proteins were identified that carried both phosphorylation and O-GlcNAcylation modifications, of which the majority (97%) exhibited the coexisting module and the remainder exhibited the potential competitive module.
31061102	0	48	theme	Phosphorylation	49:63	arg1	Modifications					12:24	The Protein Modifications	0:24	The Protein Modifications of O-GlcNAcylation and Phosphorylation	0:63	The Protein Modifications of O-GlcNAcylation and Phosphorylation Mediate Vernalization Response for Flowering in Winter Wheat.
31061102	6	49	theme	enrichment	1063:1072	arg1	analysis					1074:1081	gene ontology term enrichment analysis	1044:1081	gene ontology term enrichment analysis	1044:1081	Subsequent mass spectrometry and gene ontology term enrichment analysis identified 168 O-GlcNAcylated proteins that are mainly involved in responses to abiotic stimulus and hormones, metabolic processing, and gene expression; and 124 differentially expressed phosphorylated proteins that participate in translation, transcription, and metabolic processing.
31061102	9	50	theme	dynamic	1858:1864	arg1	network					1866:1872	a dynamic network	1856:1872	a dynamic network of O-GlcNAcylation and phosphorylation at key pathway nodes	1856:1932	Our data suggest that a dynamic network of O-GlcNAcylation and phosphorylation at key pathway nodes regulate the vernalization response and mediate flowering in wheat.
31061102	4	51	dep	affected	700:707	arg1	affecting					792:800	affecting	792:800	subsequently affecting flowering transition	779:821	Altering O-GlcNAc signaling by chemical inhibitors affected the vernalization response, modifying the expression of VRN genes and subsequently affecting flowering transition.
31061102	4	51	dep	affected	700:707	arg1	modifying					737:745	modifying	737:745	modifying the expression of VRN genes	737:773	Altering O-GlcNAc signaling by chemical inhibitors affected the vernalization response, modifying the expression of VRN genes and subsequently affecting flowering transition.
31061102	6	52	theme	phosphorylated	1270:1283	arg1	proteins					1285:1292	124 differentially expressed phosphorylated proteins	1241:1292	124 differentially expressed phosphorylated proteins that participate in translation, transcription, and metabolic processing	1241:1365	Subsequent mass spectrometry and gene ontology term enrichment analysis identified 168 O-GlcNAcylated proteins that are mainly involved in responses to abiotic stimulus and hormones, metabolic processing, and gene expression; and 124 differentially expressed phosphorylated proteins that participate in translation, transcription, and metabolic processing.
31061102	8	53	theme	RIP3	1803:1806	arg1	motif					1808:1812	the RIP3 motif	1799:1812	the RIP3 motif of TaVRN1	1799:1822	Among these, TaGRP2 was decorated with dynamic O-GlcNAcylation (S87) and phosphorylation (S152) modifications, and the mutation of S87 and S152 affected the binding of TaGRP2 to the RIP3 motif of TaVRN1 in vitro.
31061102	3	54	dep	Triticum	520:527	arg1	aestivum					529:536	Triticum aestivum	520:536	Triticum aestivum	520:536	Here we investigated the role of O-GlcNAcylation during vernalization, a process whereby prolonged cold exposure promotes flowering in winter wheat (Triticum aestivum), and analyzed the dynamic profile of O-GlcNAcylated and phosphorylated proteins in response to vernalization.
31061102	6	55	theme	expressed	1260:1268	arg1	proteins					1285:1292	124 differentially expressed phosphorylated proteins	1241:1292	124 differentially expressed phosphorylated proteins that participate in translation, transcription, and metabolic processing	1241:1365	Subsequent mass spectrometry and gene ontology term enrichment analysis identified 168 O-GlcNAcylated proteins that are mainly involved in responses to abiotic stimulus and hormones, metabolic processing, and gene expression; and 124 differentially expressed phosphorylated proteins that participate in translation, transcription, and metabolic processing.
31061102	7	56	dep	identified	1419:1428	arg1	exhibited					1577:1585	exhibited	1577:1585	exhibited the potential competitive module	1577:1618	Of note, 31 vernalization-associated proteins were identified that carried both phosphorylation and O-GlcNAcylation modifications, of which the majority (97%) exhibited the coexisting module and the remainder exhibited the potential competitive module.
31061102	7	56	dep	identified	1419:1428	arg1	exhibited					1527:1535	exhibited	1527:1535	exhibited the coexisting module	1527:1557	Of note, 31 vernalization-associated proteins were identified that carried both phosphorylation and O-GlcNAcylation modifications, of which the majority (97%) exhibited the coexisting module and the remainder exhibited the potential competitive module.
31061102	8	57	theme	S152	1760:1763	arg1	mutation					1740:1747	the mutation	1736:1747	the mutation of S87 and S152	1736:1763	Among these, TaGRP2 was decorated with dynamic O-GlcNAcylation (S87) and phosphorylation (S152) modifications, and the mutation of S87 and S152 affected the binding of TaGRP2 to the RIP3 motif of TaVRN1 in vitro.
31061102	7	58	theme	competitive	1601:1611	arg1	module					1613:1618	the potential competitive module	1587:1618	the potential competitive module	1587:1618	Of note, 31 vernalization-associated proteins were identified that carried both phosphorylation and O-GlcNAcylation modifications, of which the majority (97%) exhibited the coexisting module and the remainder exhibited the potential competitive module.
31061102	8	59	theme	dynamic	1660:1666	arg1	S87					1685:1687	S87	1685:1687	S87	1685:1687	Among these, TaGRP2 was decorated with dynamic O-GlcNAcylation (S87) and phosphorylation (S152) modifications, and the mutation of S87 and S152 affected the binding of TaGRP2 to the RIP3 motif of TaVRN1 in vitro.
31061102	8	59	theme	dynamic	1660:1666	arg1	O-GlcNAcylation					1668:1682	dynamic O-GlcNAcylation	1660:1682	dynamic O-GlcNAcylation (S87)	1660:1688	Among these, TaGRP2 was decorated with dynamic O-GlcNAcylation (S87) and phosphorylation (S152) modifications, and the mutation of S87 and S152 affected the binding of TaGRP2 to the RIP3 motif of TaVRN1 in vitro.
31061102	4	60	theme	flowering	802:810	arg1	transition					812:821	flowering transition	802:821	flowering transition	802:821	Altering O-GlcNAc signaling by chemical inhibitors affected the vernalization response, modifying the expression of VRN genes and subsequently affecting flowering transition.
31061102	6	61	theme	abiotic	1163:1169	arg1	stimulus					1171:1178	abiotic stimulus	1163:1178	abiotic stimulus	1163:1178	Subsequent mass spectrometry and gene ontology term enrichment analysis identified 168 O-GlcNAcylated proteins that are mainly involved in responses to abiotic stimulus and hormones, metabolic processing, and gene expression; and 124 differentially expressed phosphorylated proteins that participate in translation, transcription, and metabolic processing.
31061102	9	62	theme	O-GlcNAcylation	1877:1891	arg1	network					1866:1872	a dynamic network	1856:1872	a dynamic network of O-GlcNAcylation and phosphorylation at key pathway nodes	1856:1932	Our data suggest that a dynamic network of O-GlcNAcylation and phosphorylation at key pathway nodes regulate the vernalization response and mediate flowering in wheat.
31061102	5	63	theme	affinity	957:964	arg1	chromatography					966:979	Lectin weak affinity chromatography	945:979	Lectin weak affinity chromatography	945:979	Over a vernalization time-course, O-GlcNAcylated and phosphorylated peptides were enriched from winter wheat plumules by Lectin weak affinity chromatography and iTRAQ-TiO2, respectively.
31061102	3	64	theme	dynamic	557:563	arg1	profile					565:571	the dynamic profile	553:571	the dynamic profile of O-GlcNAcylated and phosphorylated proteins	553:617	Here we investigated the role of O-GlcNAcylation during vernalization, a process whereby prolonged cold exposure promotes flowering in winter wheat (Triticum aestivum), and analyzed the dynamic profile of O-GlcNAcylated and phosphorylated proteins in response to vernalization.
31061102	0	65	theme	Vernalization	73:85	arg1	Response					87:94	Vernalization Response	73:94	Vernalization Response for Flowering in Winter Wheat	73:124	The Protein Modifications of O-GlcNAcylation and Phosphorylation Mediate Vernalization Response for Flowering in Winter Wheat.
31061102	6	66	theme	ontology	1049:1056	arg1	analysis					1074:1081	gene ontology term enrichment analysis	1044:1081	gene ontology term enrichment analysis	1044:1081	Subsequent mass spectrometry and gene ontology term enrichment analysis identified 168 O-GlcNAcylated proteins that are mainly involved in responses to abiotic stimulus and hormones, metabolic processing, and gene expression; and 124 differentially expressed phosphorylated proteins that participate in translation, transcription, and metabolic processing.
31061102	2	67	theme	cross	287:291	arg1	talk					293:296	the cross talk	283:296	the cross talk between these two protein modifications	283:336	However, the regulation of and the cross talk between these two protein modifications are poorly understood in plants.
31061102	3	68	from	flowering	493:501	arg1	wheat					513:517	winter wheat	506:517	winter wheat (Triticum aestivum)	506:537	Here we investigated the role of O-GlcNAcylation during vernalization, a process whereby prolonged cold exposure promotes flowering in winter wheat (Triticum aestivum), and analyzed the dynamic profile of O-GlcNAcylated and phosphorylated proteins in response to vernalization.
31061102	3	68	from	flowering	493:501	arg1	Triticum					520:527	Triticum	520:527	Triticum	520:527	Here we investigated the role of O-GlcNAcylation during vernalization, a process whereby prolonged cold exposure promotes flowering in winter wheat (Triticum aestivum), and analyzed the dynamic profile of O-GlcNAcylated and phosphorylated proteins in response to vernalization.
31061102	1	69	theme	posttranslational	171:187	arg1	phosphorylation					147:161	phosphorylation	147:161	phosphorylation	147:161	O-GlcNAcylation and phosphorylation are two posttranslational modifications that antagonistically regulate protein function.
31061102	1	69	theme	posttranslational	171:187	arg1	O-GlcNAcylation					127:141	O-GlcNAcylation	127:141	O-GlcNAcylation	127:141	O-GlcNAcylation and phosphorylation are two posttranslational modifications that antagonistically regulate protein function.
31061102	1	69	theme	posttranslational	171:187	arg1	modifications					189:201	two posttranslational modifications	167:201	two posttranslational modifications that antagonistically regulate protein function	167:249	O-GlcNAcylation and phosphorylation are two posttranslational modifications that antagonistically regulate protein function.
31061102	4	70	theme	chemical	680:687	arg1	inhibitors					689:698	chemical inhibitors	680:698	chemical inhibitors	680:698	Altering O-GlcNAc signaling by chemical inhibitors affected the vernalization response, modifying the expression of VRN genes and subsequently affecting flowering transition.
32601203	3	0	theme	signaling	351:359	arg1	role					284:287	an unexpected role	270:287	an unexpected role of nutrient-sensing O-linked β-N-acetylglucosamine (O-GlcNAc) signaling in suppressing macrophage proinflammatory activation and preventing diet-induced metabolic dysfunction	270:462	Here, we report an unexpected role of nutrient-sensing O-linked β-N-acetylglucosamine (O-GlcNAc) signaling in suppressing macrophage proinflammatory activation and preventing diet-induced metabolic dysfunction.
32601203	6	1	theme	whole-body	883:892	arg1	resistance					902:911	tissue-specific and whole-body insulin resistance	863:911	tissue-specific and whole-body insulin resistance in high-fat-diet-induced obese mice	863:947	Suppressing O-GlcNAc signaling by O-GlcNAc transferase (OGT) knockout enhances macrophage proinflammatory polarization, promotes adipose tissue inflammation and lipolysis, increases lipid accumulation in peripheral tissues, and exacerbates tissue-specific and whole-body insulin resistance in high-fat-diet-induced obese mice.
32601203	7	2	theme	S6	1033:1034	arg1	kinase					1036:1041	ribosomal protein S6 kinase	1015:1041	ribosomal protein S6 kinase beta-1 (S6K1) O-GlcNAcylation	1015:1071	OGT inhibits macrophage proinflammatory activation by catalyzing ribosomal protein S6 kinase beta-1 (S6K1) O-GlcNAcylation and suppressing S6K1 phosphorylation and mTORC1 signaling.
32601203	3	3	link	O-linked	309:316	arg1	O-GlcNAc					341:348	O-GlcNAc	341:348	O-GlcNAc	341:348	Here, we report an unexpected role of nutrient-sensing O-linked β-N-acetylglucosamine (O-GlcNAc) signaling in suppressing macrophage proinflammatory activation and preventing diet-induced metabolic dysfunction.
32601203	3	3	link	O-linked	309:316	arg1	β-N-acetylglucosamine					318:338	nutrient-sensing O-linked β-N-acetylglucosamine	292:338	nutrient-sensing O-linked β-N-acetylglucosamine (O-GlcNAc) signaling	292:359	Here, we report an unexpected role of nutrient-sensing O-linked β-N-acetylglucosamine (O-GlcNAc) signaling in suppressing macrophage proinflammatory activation and preventing diet-induced metabolic dysfunction.
32601203	6	4	theme	O-GlcNAc	657:664	arg1	OGT					679:681	OGT	679:681	OGT	679:681	Suppressing O-GlcNAc signaling by O-GlcNAc transferase (OGT) knockout enhances macrophage proinflammatory polarization, promotes adipose tissue inflammation and lipolysis, increases lipid accumulation in peripheral tissues, and exacerbates tissue-specific and whole-body insulin resistance in high-fat-diet-induced obese mice.
32601203	6	4	theme	O-GlcNAc	657:664	arg1	transferase					666:676	O-GlcNAc transferase	657:676	O-GlcNAc transferase (OGT) knockout	657:691	Suppressing O-GlcNAc signaling by O-GlcNAc transferase (OGT) knockout enhances macrophage proinflammatory polarization, promotes adipose tissue inflammation and lipolysis, increases lipid accumulation in peripheral tissues, and exacerbates tissue-specific and whole-body insulin resistance in high-fat-diet-induced obese mice.
32601203	4	5	from	increase	493:500	arg1	signaling					514:522	O-GlcNAc signaling	505:522	O-GlcNAc signaling in macrophages	505:537	Overnutrition stimulates an increase in O-GlcNAc signaling in macrophages.
32601203	6	6	theme	tissue	760:765	arg1	inflammation					767:778	adipose tissue inflammation	752:778	adipose tissue inflammation	752:778	Suppressing O-GlcNAc signaling by O-GlcNAc transferase (OGT) knockout enhances macrophage proinflammatory polarization, promotes adipose tissue inflammation and lipolysis, increases lipid accumulation in peripheral tissues, and exacerbates tissue-specific and whole-body insulin resistance in high-fat-diet-induced obese mice.
32601203	8	7	theme	O-GlcNAc	1172:1179	arg1	mechanism					1208:1216	a homeostatic mechanism	1194:1216	a homeostatic mechanism maintaining whole-body metabolism under overnutrition	1194:1270	These findings thus identify macrophage O-GlcNAc signaling as a homeostatic mechanism maintaining whole-body metabolism under overnutrition.
32601203	8	7	theme	O-GlcNAc	1172:1179	arg1	signaling					1181:1189	macrophage O-GlcNAc signaling	1161:1189	macrophage O-GlcNAc signaling	1161:1189	These findings thus identify macrophage O-GlcNAc signaling as a homeostatic mechanism maintaining whole-body metabolism under overnutrition.
32601203	1	8	theme	Enhanced	80:87	arg1	inflammation					89:100	Enhanced inflammation	80:100	Enhanced inflammation	80:100	Enhanced inflammation is believed to contribute to overnutrition-induced metabolic disturbance.
32601203	5	9	theme	proinflammatory	595:609	arg1	activation					611:620	macrophage proinflammatory activation	584:620	macrophage proinflammatory activation	584:620	O-GlcNAc signaling is down-regulated during macrophage proinflammatory activation.
32601203	3	10	theme	proinflammatory	387:401	arg1	activation					403:412	macrophage proinflammatory activation	376:412	macrophage proinflammatory activation	376:412	Here, we report an unexpected role of nutrient-sensing O-linked β-N-acetylglucosamine (O-GlcNAc) signaling in suppressing macrophage proinflammatory activation and preventing diet-induced metabolic dysfunction.
32601203	6	11	theme	tissue-specific	863:877	arg1	resistance					902:911	tissue-specific and whole-body insulin resistance	863:911	tissue-specific and whole-body insulin resistance in high-fat-diet-induced obese mice	863:947	Suppressing O-GlcNAc signaling by O-GlcNAc transferase (OGT) knockout enhances macrophage proinflammatory polarization, promotes adipose tissue inflammation and lipolysis, increases lipid accumulation in peripheral tissues, and exacerbates tissue-specific and whole-body insulin resistance in high-fat-diet-induced obese mice.
32601203	6	12	theme	O-GlcNAc	635:642	arg1	signaling					644:652	Suppressing O-GlcNAc signaling	623:652	Suppressing O-GlcNAc signaling by O-GlcNAc transferase (OGT) knockout	623:691	Suppressing O-GlcNAc signaling by O-GlcNAc transferase (OGT) knockout enhances macrophage proinflammatory polarization, promotes adipose tissue inflammation and lipolysis, increases lipid accumulation in peripheral tissues, and exacerbates tissue-specific and whole-body insulin resistance in high-fat-diet-induced obese mice.
32601203	3	13	theme	unexpected	273:282	arg1	role					284:287	an unexpected role	270:287	an unexpected role of nutrient-sensing O-linked β-N-acetylglucosamine (O-GlcNAc) signaling in suppressing macrophage proinflammatory activation and preventing diet-induced metabolic dysfunction	270:462	Here, we report an unexpected role of nutrient-sensing O-linked β-N-acetylglucosamine (O-GlcNAc) signaling in suppressing macrophage proinflammatory activation and preventing diet-induced metabolic dysfunction.
32601203	6	14	theme	adipose	752:758	arg1	inflammation					767:778	adipose tissue inflammation	752:778	adipose tissue inflammation	752:778	Suppressing O-GlcNAc signaling by O-GlcNAc transferase (OGT) knockout enhances macrophage proinflammatory polarization, promotes adipose tissue inflammation and lipolysis, increases lipid accumulation in peripheral tissues, and exacerbates tissue-specific and whole-body insulin resistance in high-fat-diet-induced obese mice.
32601203	2	15	theme	Nutrient	176:183	arg1	flux					185:188	Nutrient flux	176:188	Nutrient flux	176:188	Nutrient flux has also been shown to be essential for immune cell activation.
32601203	8	16	theme	whole-body	1230:1239	arg1	metabolism					1241:1250	whole-body metabolism	1230:1250	whole-body metabolism	1230:1250	These findings thus identify macrophage O-GlcNAc signaling as a homeostatic mechanism maintaining whole-body metabolism under overnutrition.
32601203	2	17	theme	cell	237:240	arg1	activation					242:251	immune cell activation	230:251	immune cell activation	230:251	Nutrient flux has also been shown to be essential for immune cell activation.
32601203	7	18	theme	kinase	1036:1041	arg1	S6K1					1051:1054	S6K1	1051:1054	S6K1	1051:1054	OGT inhibits macrophage proinflammatory activation by catalyzing ribosomal protein S6 kinase beta-1 (S6K1) O-GlcNAcylation and suppressing S6K1 phosphorylation and mTORC1 signaling.
32601203	7	18	theme	kinase	1036:1041	arg1	beta-1					1043:1048	ribosomal protein S6 kinase beta-1	1015:1048	ribosomal protein S6 kinase beta-1 (S6K1) O-GlcNAcylation	1015:1071	OGT inhibits macrophage proinflammatory activation by catalyzing ribosomal protein S6 kinase beta-1 (S6K1) O-GlcNAcylation and suppressing S6K1 phosphorylation and mTORC1 signaling.
32601203	6	19	theme	Suppressing	623:633	arg1	signaling					644:652	Suppressing O-GlcNAc signaling	623:652	Suppressing O-GlcNAc signaling by O-GlcNAc transferase (OGT) knockout	623:691	Suppressing O-GlcNAc signaling by O-GlcNAc transferase (OGT) knockout enhances macrophage proinflammatory polarization, promotes adipose tissue inflammation and lipolysis, increases lipid accumulation in peripheral tissues, and exacerbates tissue-specific and whole-body insulin resistance in high-fat-diet-induced obese mice.
32601203	3	20	theme	diet-induced	429:440	arg1	dysfunction					452:462	diet-induced metabolic dysfunction	429:462	diet-induced metabolic dysfunction	429:462	Here, we report an unexpected role of nutrient-sensing O-linked β-N-acetylglucosamine (O-GlcNAc) signaling in suppressing macrophage proinflammatory activation and preventing diet-induced metabolic dysfunction.
32601203	7	21	theme	ribosomal	1015:1023	arg1	kinase					1036:1041	ribosomal protein S6 kinase	1015:1041	ribosomal protein S6 kinase beta-1 (S6K1) O-GlcNAcylation	1015:1071	OGT inhibits macrophage proinflammatory activation by catalyzing ribosomal protein S6 kinase beta-1 (S6K1) O-GlcNAcylation and suppressing S6K1 phosphorylation and mTORC1 signaling.
32601203	3	22	theme	nutrient-sensing	292:307	arg1	O-GlcNAc					341:348	O-GlcNAc	341:348	O-GlcNAc	341:348	Here, we report an unexpected role of nutrient-sensing O-linked β-N-acetylglucosamine (O-GlcNAc) signaling in suppressing macrophage proinflammatory activation and preventing diet-induced metabolic dysfunction.
32601203	3	22	theme	nutrient-sensing	292:307	arg1	β-N-acetylglucosamine					318:338	nutrient-sensing O-linked β-N-acetylglucosamine	292:338	nutrient-sensing O-linked β-N-acetylglucosamine (O-GlcNAc) signaling	292:359	Here, we report an unexpected role of nutrient-sensing O-linked β-N-acetylglucosamine (O-GlcNAc) signaling in suppressing macrophage proinflammatory activation and preventing diet-induced metabolic dysfunction.
32601203	7	23	theme	beta-1	1043:1048	arg1	O-GlcNAcylation					1057:1071	ribosomal protein S6 kinase beta-1 (S6K1) O-GlcNAcylation	1015:1071	ribosomal protein S6 kinase beta-1 (S6K1) O-GlcNAcylation	1015:1071	OGT inhibits macrophage proinflammatory activation by catalyzing ribosomal protein S6 kinase beta-1 (S6K1) O-GlcNAcylation and suppressing S6K1 phosphorylation and mTORC1 signaling.
32601203	3	24	theme	metabolic	442:450	arg1	dysfunction					452:462	diet-induced metabolic dysfunction	429:462	diet-induced metabolic dysfunction	429:462	Here, we report an unexpected role of nutrient-sensing O-linked β-N-acetylglucosamine (O-GlcNAc) signaling in suppressing macrophage proinflammatory activation and preventing diet-induced metabolic dysfunction.
32601203	3	25	theme	O-linked	309:316	arg1	O-GlcNAc					341:348	O-GlcNAc	341:348	O-GlcNAc	341:348	Here, we report an unexpected role of nutrient-sensing O-linked β-N-acetylglucosamine (O-GlcNAc) signaling in suppressing macrophage proinflammatory activation and preventing diet-induced metabolic dysfunction.
32601203	3	25	theme	O-linked	309:316	arg1	β-N-acetylglucosamine					318:338	nutrient-sensing O-linked β-N-acetylglucosamine	292:338	nutrient-sensing O-linked β-N-acetylglucosamine (O-GlcNAc) signaling	292:359	Here, we report an unexpected role of nutrient-sensing O-linked β-N-acetylglucosamine (O-GlcNAc) signaling in suppressing macrophage proinflammatory activation and preventing diet-induced metabolic dysfunction.
32601203	6	26	from	resistance	902:911	arg1	mice					944:947	high-fat-diet-induced obese mice	916:947	high-fat-diet-induced obese mice	916:947	Suppressing O-GlcNAc signaling by O-GlcNAc transferase (OGT) knockout enhances macrophage proinflammatory polarization, promotes adipose tissue inflammation and lipolysis, increases lipid accumulation in peripheral tissues, and exacerbates tissue-specific and whole-body insulin resistance in high-fat-diet-induced obese mice.
32601203	6	27	theme	peripheral	827:836	arg1	tissues					838:844	peripheral tissues	827:844	peripheral tissues	827:844	Suppressing O-GlcNAc signaling by O-GlcNAc transferase (OGT) knockout enhances macrophage proinflammatory polarization, promotes adipose tissue inflammation and lipolysis, increases lipid accumulation in peripheral tissues, and exacerbates tissue-specific and whole-body insulin resistance in high-fat-diet-induced obese mice.
32601203	6	28	theme	proinflammatory	713:727	arg1	polarization					729:740	macrophage proinflammatory polarization	702:740	macrophage proinflammatory polarization	702:740	Suppressing O-GlcNAc signaling by O-GlcNAc transferase (OGT) knockout enhances macrophage proinflammatory polarization, promotes adipose tissue inflammation and lipolysis, increases lipid accumulation in peripheral tissues, and exacerbates tissue-specific and whole-body insulin resistance in high-fat-diet-induced obese mice.
32601203	8	29	theme	homeostatic	1196:1206	arg1	mechanism					1208:1216	a homeostatic mechanism	1194:1216	a homeostatic mechanism maintaining whole-body metabolism under overnutrition	1194:1270	These findings thus identify macrophage O-GlcNAc signaling as a homeostatic mechanism maintaining whole-body metabolism under overnutrition.
32601203	8	29	theme	homeostatic	1196:1206	arg1	signaling					1181:1189	macrophage O-GlcNAc signaling	1161:1189	macrophage O-GlcNAc signaling	1161:1189	These findings thus identify macrophage O-GlcNAc signaling as a homeostatic mechanism maintaining whole-body metabolism under overnutrition.
32601203	5	30	theme	macrophage	584:593	arg1	activation					611:620	macrophage proinflammatory activation	584:620	macrophage proinflammatory activation	584:620	O-GlcNAc signaling is down-regulated during macrophage proinflammatory activation.
32601203	6	31	theme	macrophage	702:711	arg1	polarization					729:740	macrophage proinflammatory polarization	702:740	macrophage proinflammatory polarization	702:740	Suppressing O-GlcNAc signaling by O-GlcNAc transferase (OGT) knockout enhances macrophage proinflammatory polarization, promotes adipose tissue inflammation and lipolysis, increases lipid accumulation in peripheral tissues, and exacerbates tissue-specific and whole-body insulin resistance in high-fat-diet-induced obese mice.
32601203	7	32	theme	macrophage	963:972	arg1	activation					990:999	macrophage proinflammatory activation	963:999	macrophage proinflammatory activation	963:999	OGT inhibits macrophage proinflammatory activation by catalyzing ribosomal protein S6 kinase beta-1 (S6K1) O-GlcNAcylation and suppressing S6K1 phosphorylation and mTORC1 signaling.
32601203	0	33	theme	macrophage	29:38	arg1	inflammation					40:51	S6K1-mediated macrophage inflammation	15:51	S6K1-mediated macrophage inflammation	15:51	OGT suppresses S6K1-mediated macrophage inflammation and metabolic disturbance.
32601203	7	34	theme	proinflammatory	974:988	arg1	activation					990:999	macrophage proinflammatory activation	963:999	macrophage proinflammatory activation	963:999	OGT inhibits macrophage proinflammatory activation by catalyzing ribosomal protein S6 kinase beta-1 (S6K1) O-GlcNAcylation and suppressing S6K1 phosphorylation and mTORC1 signaling.
32601203	6	35	from	accumulation	811:822	arg1	tissues					838:844	peripheral tissues	827:844	peripheral tissues	827:844	Suppressing O-GlcNAc signaling by O-GlcNAc transferase (OGT) knockout enhances macrophage proinflammatory polarization, promotes adipose tissue inflammation and lipolysis, increases lipid accumulation in peripheral tissues, and exacerbates tissue-specific and whole-body insulin resistance in high-fat-diet-induced obese mice.
32601203	1	36	theme	overnutrition-induced	131:151	arg1	disturbance					163:173	overnutrition-induced metabolic disturbance	131:173	overnutrition-induced metabolic disturbance	131:173	Enhanced inflammation is believed to contribute to overnutrition-induced metabolic disturbance.
32601203	0	37	theme	metabolic	57:65	arg1	disturbance					67:77	metabolic disturbance	57:77	metabolic disturbance	57:77	OGT suppresses S6K1-mediated macrophage inflammation and metabolic disturbance.
32601203	4	38	from	signaling	514:522	arg1	macrophages					527:537	macrophages	527:537	macrophages	527:537	Overnutrition stimulates an increase in O-GlcNAc signaling in macrophages.
32601203	4	39	theme	O-GlcNAc	505:512	arg1	signaling					514:522	O-GlcNAc signaling	505:522	O-GlcNAc signaling in macrophages	505:537	Overnutrition stimulates an increase in O-GlcNAc signaling in macrophages.
32601203	6	40	theme	obese	938:942	arg1	mice					944:947	high-fat-diet-induced obese mice	916:947	high-fat-diet-induced obese mice	916:947	Suppressing O-GlcNAc signaling by O-GlcNAc transferase (OGT) knockout enhances macrophage proinflammatory polarization, promotes adipose tissue inflammation and lipolysis, increases lipid accumulation in peripheral tissues, and exacerbates tissue-specific and whole-body insulin resistance in high-fat-diet-induced obese mice.
32601203	1	41	theme	metabolic	153:161	arg1	disturbance					163:173	overnutrition-induced metabolic disturbance	131:173	overnutrition-induced metabolic disturbance	131:173	Enhanced inflammation is believed to contribute to overnutrition-induced metabolic disturbance.
32601203	3	42	theme	β-N-acetylglucosamine	318:338	arg1	signaling					351:359	nutrient-sensing O-linked β-N-acetylglucosamine (O-GlcNAc) signaling	292:359	nutrient-sensing O-linked β-N-acetylglucosamine (O-GlcNAc) signaling	292:359	Here, we report an unexpected role of nutrient-sensing O-linked β-N-acetylglucosamine (O-GlcNAc) signaling in suppressing macrophage proinflammatory activation and preventing diet-induced metabolic dysfunction.
32601203	2	43	theme	immune	230:235	arg1	activation					242:251	immune cell activation	230:251	immune cell activation	230:251	Nutrient flux has also been shown to be essential for immune cell activation.
32601203	6	44	theme	high-fat-diet-induced	916:936	arg1	mice					944:947	high-fat-diet-induced obese mice	916:947	high-fat-diet-induced obese mice	916:947	Suppressing O-GlcNAc signaling by O-GlcNAc transferase (OGT) knockout enhances macrophage proinflammatory polarization, promotes adipose tissue inflammation and lipolysis, increases lipid accumulation in peripheral tissues, and exacerbates tissue-specific and whole-body insulin resistance in high-fat-diet-induced obese mice.
32601203	6	45	theme	lipid	805:809	arg1	accumulation					811:822	lipid accumulation	805:822	lipid accumulation in peripheral tissues	805:844	Suppressing O-GlcNAc signaling by O-GlcNAc transferase (OGT) knockout enhances macrophage proinflammatory polarization, promotes adipose tissue inflammation and lipolysis, increases lipid accumulation in peripheral tissues, and exacerbates tissue-specific and whole-body insulin resistance in high-fat-diet-induced obese mice.
32601203	7	46	theme	protein	1025:1031	arg1	kinase					1036:1041	ribosomal protein S6 kinase	1015:1041	ribosomal protein S6 kinase beta-1 (S6K1) O-GlcNAcylation	1015:1071	OGT inhibits macrophage proinflammatory activation by catalyzing ribosomal protein S6 kinase beta-1 (S6K1) O-GlcNAcylation and suppressing S6K1 phosphorylation and mTORC1 signaling.
32601203	6	47	theme	knockout	684:691	arg1	OGT					679:681	OGT	679:681	OGT	679:681	Suppressing O-GlcNAc signaling by O-GlcNAc transferase (OGT) knockout enhances macrophage proinflammatory polarization, promotes adipose tissue inflammation and lipolysis, increases lipid accumulation in peripheral tissues, and exacerbates tissue-specific and whole-body insulin resistance in high-fat-diet-induced obese mice.
32601203	6	47	theme	knockout	684:691	arg1	transferase					666:676	O-GlcNAc transferase	657:676	O-GlcNAc transferase (OGT) knockout	657:691	Suppressing O-GlcNAc signaling by O-GlcNAc transferase (OGT) knockout enhances macrophage proinflammatory polarization, promotes adipose tissue inflammation and lipolysis, increases lipid accumulation in peripheral tissues, and exacerbates tissue-specific and whole-body insulin resistance in high-fat-diet-induced obese mice.
32601203	5	48	theme	O-GlcNAc	540:547	arg1	signaling					549:557	O-GlcNAc signaling	540:557	O-GlcNAc signaling	540:557	O-GlcNAc signaling is down-regulated during macrophage proinflammatory activation.
32601203	8	49	theme	macrophage	1161:1170	arg1	mechanism					1208:1216	a homeostatic mechanism	1194:1216	a homeostatic mechanism maintaining whole-body metabolism under overnutrition	1194:1270	These findings thus identify macrophage O-GlcNAc signaling as a homeostatic mechanism maintaining whole-body metabolism under overnutrition.
32601203	8	49	theme	macrophage	1161:1170	arg1	signaling					1181:1189	macrophage O-GlcNAc signaling	1161:1189	macrophage O-GlcNAc signaling	1161:1189	These findings thus identify macrophage O-GlcNAc signaling as a homeostatic mechanism maintaining whole-body metabolism under overnutrition.
32601203	7	50	theme	mTORC1	1114:1119	arg1	signaling					1121:1129	mTORC1 signaling	1114:1129	mTORC1 signaling	1114:1129	OGT inhibits macrophage proinflammatory activation by catalyzing ribosomal protein S6 kinase beta-1 (S6K1) O-GlcNAcylation and suppressing S6K1 phosphorylation and mTORC1 signaling.
32601203	3	51	theme	macrophage	376:385	arg1	activation					403:412	macrophage proinflammatory activation	376:412	macrophage proinflammatory activation	376:412	Here, we report an unexpected role of nutrient-sensing O-linked β-N-acetylglucosamine (O-GlcNAc) signaling in suppressing macrophage proinflammatory activation and preventing diet-induced metabolic dysfunction.
32601203	0	52	theme	S6K1-mediated	15:27	arg1	inflammation					40:51	S6K1-mediated macrophage inflammation	15:51	S6K1-mediated macrophage inflammation	15:51	OGT suppresses S6K1-mediated macrophage inflammation and metabolic disturbance.
32601203	6	53	theme	insulin	894:900	arg1	resistance					902:911	tissue-specific and whole-body insulin resistance	863:911	tissue-specific and whole-body insulin resistance in high-fat-diet-induced obese mice	863:947	Suppressing O-GlcNAc signaling by O-GlcNAc transferase (OGT) knockout enhances macrophage proinflammatory polarization, promotes adipose tissue inflammation and lipolysis, increases lipid accumulation in peripheral tissues, and exacerbates tissue-specific and whole-body insulin resistance in high-fat-diet-induced obese mice.
32601203	7	54	theme	S6K1	1089:1092	arg1	phosphorylation					1094:1108	S6K1 phosphorylation	1089:1108	S6K1 phosphorylation	1089:1108	OGT inhibits macrophage proinflammatory activation by catalyzing ribosomal protein S6 kinase beta-1 (S6K1) O-GlcNAcylation and suppressing S6K1 phosphorylation and mTORC1 signaling.
24214978	1	0	theme	cytoplasmic	162:172	arg1	proteins					174:181	nuclear and cytoplasmic proteins	150:181	nuclear and cytoplasmic proteins	150:181	O-GlcNAcylation is a post-translational modification that regulates a broad range of nuclear and cytoplasmic proteins and is emerging as a key regulator of various biological processes.
24214978	1	1	theme	proteins	174:181	arg1	range					141:145	a broad range	133:145	a broad range of nuclear and cytoplasmic proteins	133:181	O-GlcNAcylation is a post-translational modification that regulates a broad range of nuclear and cytoplasmic proteins and is emerging as a key regulator of various biological processes.
24214978	2	2	attach	linked	362:367	arg1	incidence					376:384	the incidence	372:384	the incidence of metastasis in breast cancer patients	372:424	Previous studies have shown that increased levels of global O-GlcNAcylation and O-GlcNAc transferase (OGT) are linked to the incidence of metastasis in breast cancer patients, but the molecular basis behind this is not fully known.
24214978	2	2	attach	linked	362:367	arg2	levels					294:299	increased levels	284:299	increased levels of global O-GlcNAcylation and O-GlcNAc transferase (OGT)	284:356	Previous studies have shown that increased levels of global O-GlcNAcylation and O-GlcNAc transferase (OGT) are linked to the incidence of metastasis in breast cancer patients, but the molecular basis behind this is not fully known.
24214978	6	3	theme	cancer	1191:1196	arg1	metastasis					1198:1207	cancer metastasis	1191:1207	cancer metastasis	1191:1207	Our study provides insights into the mechanism of post-translational modification in fine-tuning the regulation of cofilin activity and suggests its important implications in cancer metastasis.
24214978	5	4	theme	actin-severing	945:958	arg1	activity					960:967	the actin-severing activity	941:967	the actin-severing activity	941:967	Loss of O-GlcNAcylation of cofilin leads to destabilization of invadopodia and impairs cell invasion, although the actin-severing activity or lamellipodial localization is not affected.
24214978	3	5	theme	protein	540:546	arg1	mediates					612:619	mediates	612:619	mediates OGT modulation of cell mobility	612:651	In this study, we have determined that the actin-binding protein cofilin is O-GlcNAcylated by OGT and mainly, if not completely, mediates OGT modulation of cell mobility.
24214978	3	5	theme	protein	540:546	arg1	O-GlcNAcylated					559:572	O-GlcNAcylated	559:572	O-GlcNAcylated	559:572	In this study, we have determined that the actin-binding protein cofilin is O-GlcNAcylated by OGT and mainly, if not completely, mediates OGT modulation of cell mobility.
24214978	3	5	theme	protein	540:546	arg1	cofilin					548:554	the actin-binding protein cofilin	522:554	the actin-binding protein cofilin	522:554	In this study, we have determined that the actin-binding protein cofilin is O-GlcNAcylated by OGT and mainly, if not completely, mediates OGT modulation of cell mobility.
24214978	2	6	theme	O-GlcNAc	331:338	arg1	OGT					353:355	OGT	353:355	OGT	353:355	Previous studies have shown that increased levels of global O-GlcNAcylation and O-GlcNAc transferase (OGT) are linked to the incidence of metastasis in breast cancer patients, but the molecular basis behind this is not fully known.
24214978	2	6	theme	O-GlcNAc	331:338	arg1	transferase					340:350	O-GlcNAc transferase	331:350	O-GlcNAc transferase (OGT)	331:356	Previous studies have shown that increased levels of global O-GlcNAcylation and O-GlcNAc transferase (OGT) are linked to the incidence of metastasis in breast cancer patients, but the molecular basis behind this is not fully known.
24214978	5	7	theme	cell	917:920	arg1	invasion					922:929	cell invasion	917:929	cell invasion	917:929	Loss of O-GlcNAcylation of cofilin leads to destabilization of invadopodia and impairs cell invasion, although the actin-severing activity or lamellipodial localization is not affected.
24214978	5	8	theme	invadopodia	893:903	arg1	destabilization					874:888	destabilization	874:888	destabilization of invadopodia	874:903	Loss of O-GlcNAcylation of cofilin leads to destabilization of invadopodia and impairs cell invasion, although the actin-severing activity or lamellipodial localization is not affected.
24214978	2	9	theme	increased	284:292	arg1	levels					294:299	increased levels	284:299	increased levels of global O-GlcNAcylation and O-GlcNAc transferase (OGT)	284:356	Previous studies have shown that increased levels of global O-GlcNAcylation and O-GlcNAc transferase (OGT) are linked to the incidence of metastasis in breast cancer patients, but the molecular basis behind this is not fully known.
24214978	3	10	dep	O-GlcNAcylated	559:572	arg1	mediates					612:619	mediates	612:619	mediates OGT modulation of cell mobility	612:651	In this study, we have determined that the actin-binding protein cofilin is O-GlcNAcylated by OGT and mainly, if not completely, mediates OGT modulation of cell mobility.
24214978	3	10	dep	O-GlcNAcylated	559:572	arg1	O-GlcNAcylated					559:572	O-GlcNAcylated	559:572	O-GlcNAcylated	559:572	In this study, we have determined that the actin-binding protein cofilin is O-GlcNAcylated by OGT and mainly, if not completely, mediates OGT modulation of cell mobility.
24214978	3	10	dep	O-GlcNAcylated	559:572	arg1	cofilin					548:554	the actin-binding protein cofilin	522:554	the actin-binding protein cofilin	522:554	In this study, we have determined that the actin-binding protein cofilin is O-GlcNAcylated by OGT and mainly, if not completely, mediates OGT modulation of cell mobility.
24214978	4	11	theme	cell	815:818	arg1	invasion					820:827	three-dimensional cell invasion	797:827	three-dimensional cell invasion	797:827	O-GlcNAcylation at Ser-108 of cofilin is required for its proper localization in invadopodia at the leading edge of breast cancer cells during three-dimensional cell invasion.
24214978	4	12	from	localization	719:730	arg1	invadopodia					735:745	invadopodia	735:745	invadopodia at the leading edge of breast cancer cells during three-dimensional cell invasion	735:827	O-GlcNAcylation at Ser-108 of cofilin is required for its proper localization in invadopodia at the leading edge of breast cancer cells during three-dimensional cell invasion.
24214978	4	12	from	localization	719:730	arg1	edge					762:765	the leading edge	750:765	the leading edge of breast cancer cells during three-dimensional cell invasion	750:827	O-GlcNAcylation at Ser-108 of cofilin is required for its proper localization in invadopodia at the leading edge of breast cancer cells during three-dimensional cell invasion.
24214978	5	13	theme	lamellipodial	972:984	arg1	localization					986:997	lamellipodial localization	972:997	lamellipodial localization	972:997	Loss of O-GlcNAcylation of cofilin leads to destabilization of invadopodia and impairs cell invasion, although the actin-severing activity or lamellipodial localization is not affected.
24214978	2	14	theme	metastasis	389:398	arg1	incidence					376:384	the incidence	372:384	the incidence of metastasis in breast cancer patients	372:424	Previous studies have shown that increased levels of global O-GlcNAcylation and O-GlcNAc transferase (OGT) are linked to the incidence of metastasis in breast cancer patients, but the molecular basis behind this is not fully known.
24214978	1	15	theme	post-translational	86:103	arg1	modification					105:116	a post-translational modification	84:116	a post-translational modification that regulates a broad range of nuclear and cytoplasmic proteins and is emerging as a key regulator of various biological processes	84:248	O-GlcNAcylation is a post-translational modification that regulates a broad range of nuclear and cytoplasmic proteins and is emerging as a key regulator of various biological processes.
24214978	1	15	theme	post-translational	86:103	arg1	O-GlcNAcylation					65:79	O-GlcNAcylation	65:79	O-GlcNAcylation	65:79	O-GlcNAcylation is a post-translational modification that regulates a broad range of nuclear and cytoplasmic proteins and is emerging as a key regulator of various biological processes.
24214978	6	16	theme	post-translational	1066:1083	arg1	modification					1085:1096	post-translational modification	1066:1096	post-translational modification in fine-tuning the regulation of cofilin activity	1066:1146	Our study provides insights into the mechanism of post-translational modification in fine-tuning the regulation of cofilin activity and suggests its important implications in cancer metastasis.
24214978	2	17	theme	molecular	435:443	arg1	basis					445:449	the molecular basis	431:449	the molecular basis behind this	431:461	Previous studies have shown that increased levels of global O-GlcNAcylation and O-GlcNAc transferase (OGT) are linked to the incidence of metastasis in breast cancer patients, but the molecular basis behind this is not fully known.
24214978	5	18	theme	cofilin	857:863	arg1	Loss					830:833	Loss	830:833	Loss of O-GlcNAcylation of cofilin	830:863	Loss of O-GlcNAcylation of cofilin leads to destabilization of invadopodia and impairs cell invasion, although the actin-severing activity or lamellipodial localization is not affected.
24214978	6	19	theme	modification	1085:1096	arg1	mechanism					1053:1061	the mechanism	1049:1061	the mechanism of post-translational modification in fine-tuning the regulation of cofilin activity	1049:1146	Our study provides insights into the mechanism of post-translational modification in fine-tuning the regulation of cofilin activity and suggests its important implications in cancer metastasis.
24214978	2	20	theme	O-GlcNAcylation	311:325	arg1	levels					294:299	increased levels	284:299	increased levels of global O-GlcNAcylation and O-GlcNAc transferase (OGT)	284:356	Previous studies have shown that increased levels of global O-GlcNAcylation and O-GlcNAc transferase (OGT) are linked to the incidence of metastasis in breast cancer patients, but the molecular basis behind this is not fully known.
24214978	0	21	theme	cofilin	19:25	arg1	O-GlcNAcylation					0:14	O-GlcNAcylation	0:14	O-GlcNAcylation of cofilin	0:25	O-GlcNAcylation of cofilin promotes breast cancer cell invasion.
24214978	2	22	theme	global	304:309	arg1	O-GlcNAcylation					311:325	global O-GlcNAcylation	304:325	global O-GlcNAcylation	304:325	Previous studies have shown that increased levels of global O-GlcNAcylation and O-GlcNAc transferase (OGT) are linked to the incidence of metastasis in breast cancer patients, but the molecular basis behind this is not fully known.
24214978	1	23	theme	key	204:206	arg1	regulator					208:216	a key regulator	202:216	a key regulator of various biological processes	202:248	O-GlcNAcylation is a post-translational modification that regulates a broad range of nuclear and cytoplasmic proteins and is emerging as a key regulator of various biological processes.
24214978	0	24	theme	cancer	43:48	arg1	invasion					55:62	breast cancer cell invasion	36:62	breast cancer cell invasion	36:62	O-GlcNAcylation of cofilin promotes breast cancer cell invasion.
24214978	3	25	theme	OGT	621:623	arg1	modulation					625:634	OGT modulation	621:634	OGT modulation of cell mobility	621:651	In this study, we have determined that the actin-binding protein cofilin is O-GlcNAcylated by OGT and mainly, if not completely, mediates OGT modulation of cell mobility.
24214978	4	26	theme	cells	784:788	arg1	edge					762:765	the leading edge	750:765	the leading edge of breast cancer cells during three-dimensional cell invasion	750:827	O-GlcNAcylation at Ser-108 of cofilin is required for its proper localization in invadopodia at the leading edge of breast cancer cells during three-dimensional cell invasion.
24214978	6	27	from	implications	1175:1186	arg1	metastasis					1198:1207	cancer metastasis	1191:1207	cancer metastasis	1191:1207	Our study provides insights into the mechanism of post-translational modification in fine-tuning the regulation of cofilin activity and suggests its important implications in cancer metastasis.
24214978	2	28	theme	cancer	410:415	arg1	patients					417:424	breast cancer patients	403:424	breast cancer patients	403:424	Previous studies have shown that increased levels of global O-GlcNAcylation and O-GlcNAc transferase (OGT) are linked to the incidence of metastasis in breast cancer patients, but the molecular basis behind this is not fully known.
24214978	0	29	theme	breast	36:41	arg1	invasion					55:62	breast cancer cell invasion	36:62	breast cancer cell invasion	36:62	O-GlcNAcylation of cofilin promotes breast cancer cell invasion.
24214978	4	30	theme	cancer	777:782	arg1	cells					784:788	breast cancer cells	770:788	breast cancer cells	770:788	O-GlcNAcylation at Ser-108 of cofilin is required for its proper localization in invadopodia at the leading edge of breast cancer cells during three-dimensional cell invasion.
24214978	2	31	theme	breast	403:408	arg1	patients					417:424	breast cancer patients	403:424	breast cancer patients	403:424	Previous studies have shown that increased levels of global O-GlcNAcylation and O-GlcNAc transferase (OGT) are linked to the incidence of metastasis in breast cancer patients, but the molecular basis behind this is not fully known.
24214978	4	32	theme	three-dimensional	797:813	arg1	invasion					820:827	three-dimensional cell invasion	797:827	three-dimensional cell invasion	797:827	O-GlcNAcylation at Ser-108 of cofilin is required for its proper localization in invadopodia at the leading edge of breast cancer cells during three-dimensional cell invasion.
24214978	2	33	from	incidence	376:384	arg1	patients					417:424	breast cancer patients	403:424	breast cancer patients	403:424	Previous studies have shown that increased levels of global O-GlcNAcylation and O-GlcNAc transferase (OGT) are linked to the incidence of metastasis in breast cancer patients, but the molecular basis behind this is not fully known.
24214978	4	34	theme	cofilin	684:690	arg1	Ser-108					673:679	Ser-108	673:679	Ser-108 of cofilin	673:690	O-GlcNAcylation at Ser-108 of cofilin is required for its proper localization in invadopodia at the leading edge of breast cancer cells during three-dimensional cell invasion.
24214978	0	35	theme	cell	50:53	arg1	invasion					55:62	breast cancer cell invasion	36:62	breast cancer cell invasion	36:62	O-GlcNAcylation of cofilin promotes breast cancer cell invasion.
24214978	3	36	theme	cell	639:642	arg1	mobility					644:651	cell mobility	639:651	cell mobility	639:651	In this study, we have determined that the actin-binding protein cofilin is O-GlcNAcylated by OGT and mainly, if not completely, mediates OGT modulation of cell mobility.
24214978	6	37	theme	important	1165:1173	arg1	implications					1175:1186	its important implications	1161:1186	its important implications in cancer metastasis	1161:1207	Our study provides insights into the mechanism of post-translational modification in fine-tuning the regulation of cofilin activity and suggests its important implications in cancer metastasis.
24214978	1	38	theme	broad	135:139	arg1	range					141:145	a broad range	133:145	a broad range of nuclear and cytoplasmic proteins	133:181	O-GlcNAcylation is a post-translational modification that regulates a broad range of nuclear and cytoplasmic proteins and is emerging as a key regulator of various biological processes.
24214978	3	39	theme	mobility	644:651	arg1	modulation					625:634	OGT modulation	621:634	OGT modulation of cell mobility	621:651	In this study, we have determined that the actin-binding protein cofilin is O-GlcNAcylated by OGT and mainly, if not completely, mediates OGT modulation of cell mobility.
24214978	6	40	theme	activity	1139:1146	arg1	regulation					1117:1126	the regulation	1113:1126	the regulation of cofilin activity	1113:1146	Our study provides insights into the mechanism of post-translational modification in fine-tuning the regulation of cofilin activity and suggests its important implications in cancer metastasis.
24214978	3	41	theme	actin-binding	526:538	arg1	mediates					612:619	mediates	612:619	mediates OGT modulation of cell mobility	612:651	In this study, we have determined that the actin-binding protein cofilin is O-GlcNAcylated by OGT and mainly, if not completely, mediates OGT modulation of cell mobility.
24214978	3	41	theme	actin-binding	526:538	arg1	O-GlcNAcylated					559:572	O-GlcNAcylated	559:572	O-GlcNAcylated	559:572	In this study, we have determined that the actin-binding protein cofilin is O-GlcNAcylated by OGT and mainly, if not completely, mediates OGT modulation of cell mobility.
24214978	3	41	theme	actin-binding	526:538	arg1	cofilin					548:554	the actin-binding protein cofilin	522:554	the actin-binding protein cofilin	522:554	In this study, we have determined that the actin-binding protein cofilin is O-GlcNAcylated by OGT and mainly, if not completely, mediates OGT modulation of cell mobility.
24214978	1	42	theme	various	221:227	arg1	processes					240:248	various biological processes	221:248	various biological processes	221:248	O-GlcNAcylation is a post-translational modification that regulates a broad range of nuclear and cytoplasmic proteins and is emerging as a key regulator of various biological processes.
24214978	6	43	theme	cofilin	1131:1137	arg1	activity					1139:1146	cofilin activity	1131:1146	cofilin activity	1131:1146	Our study provides insights into the mechanism of post-translational modification in fine-tuning the regulation of cofilin activity and suggests its important implications in cancer metastasis.
24214978	4	44	theme	leading	754:760	arg1	edge					762:765	the leading edge	750:765	the leading edge of breast cancer cells during three-dimensional cell invasion	750:827	O-GlcNAcylation at Ser-108 of cofilin is required for its proper localization in invadopodia at the leading edge of breast cancer cells during three-dimensional cell invasion.
24214978	4	45	theme	proper	712:717	arg1	localization					719:730	its proper localization	708:730	its proper localization in invadopodia at the leading edge of breast cancer cells during three-dimensional cell invasion	708:827	O-GlcNAcylation at Ser-108 of cofilin is required for its proper localization in invadopodia at the leading edge of breast cancer cells during three-dimensional cell invasion.
24214978	2	46	theme	transferase	340:350	arg1	levels					294:299	increased levels	284:299	increased levels of global O-GlcNAcylation and O-GlcNAc transferase (OGT)	284:356	Previous studies have shown that increased levels of global O-GlcNAcylation and O-GlcNAc transferase (OGT) are linked to the incidence of metastasis in breast cancer patients, but the molecular basis behind this is not fully known.
24214978	1	47	theme	biological	229:238	arg1	processes					240:248	various biological processes	221:248	various biological processes	221:248	O-GlcNAcylation is a post-translational modification that regulates a broad range of nuclear and cytoplasmic proteins and is emerging as a key regulator of various biological processes.
24214978	3	48	dep	not	596:598	arg1	if					593:594	if	593:594	if	593:594	In this study, we have determined that the actin-binding protein cofilin is O-GlcNAcylated by OGT and mainly, if not completely, mediates OGT modulation of cell mobility.
24214978	4	49	theme	breast	770:775	arg1	cells					784:788	breast cancer cells	770:788	breast cancer cells	770:788	O-GlcNAcylation at Ser-108 of cofilin is required for its proper localization in invadopodia at the leading edge of breast cancer cells during three-dimensional cell invasion.
24214978	1	50	theme	nuclear	150:156	arg1	proteins					174:181	nuclear and cytoplasmic proteins	150:181	nuclear and cytoplasmic proteins	150:181	O-GlcNAcylation is a post-translational modification that regulates a broad range of nuclear and cytoplasmic proteins and is emerging as a key regulator of various biological processes.
24214978	5	51	theme	O-GlcNAcylation	838:852	arg1	Loss					830:833	Loss	830:833	Loss of O-GlcNAcylation of cofilin	830:863	Loss of O-GlcNAcylation of cofilin leads to destabilization of invadopodia and impairs cell invasion, although the actin-severing activity or lamellipodial localization is not affected.
24214978	1	52	theme	processes	240:248	arg1	regulator					208:216	a key regulator	202:216	a key regulator of various biological processes	202:248	O-GlcNAcylation is a post-translational modification that regulates a broad range of nuclear and cytoplasmic proteins and is emerging as a key regulator of various biological processes.
24214978	2	53	theme	Previous	251:258	arg1	studies					260:266	Previous studies	251:266	Previous studies	251:266	Previous studies have shown that increased levels of global O-GlcNAcylation and O-GlcNAc transferase (OGT) are linked to the incidence of metastasis in breast cancer patients, but the molecular basis behind this is not fully known.
24214978	4	54	from	edge	762:765	arg1	invadopodia					735:745	invadopodia	735:745	invadopodia at the leading edge of breast cancer cells during three-dimensional cell invasion	735:827	O-GlcNAcylation at Ser-108 of cofilin is required for its proper localization in invadopodia at the leading edge of breast cancer cells during three-dimensional cell invasion.
24214978	4	54	from	edge	762:765	arg1	localization					719:730	its proper localization	708:730	its proper localization in invadopodia at the leading edge of breast cancer cells during three-dimensional cell invasion	708:827	O-GlcNAcylation at Ser-108 of cofilin is required for its proper localization in invadopodia at the leading edge of breast cancer cells during three-dimensional cell invasion.
24214978	4	55	from	Ser-108	673:679	arg1	O-GlcNAcylation					654:668	O-GlcNAcylation	654:668	O-GlcNAcylation at Ser-108 of cofilin	654:690	O-GlcNAcylation at Ser-108 of cofilin is required for its proper localization in invadopodia at the leading edge of breast cancer cells during three-dimensional cell invasion.
30715269	4	0	theme	YY1-dependent	510:522	arg1	manner					524:529	a YY1-dependent manner	508:529	a YY1-dependent manner	508:529	O-GlcNAcylation facilitated transformative phenotypes of CRC cell in a YY1-dependent manner.
30715269	1	1	theme	pivotal	166:172	arg1	roles					174:178	pivotal roles	166:178	pivotal roles	166:178	Emerging studies have revealed that O-GlcNAcylation plays pivotal roles in the tumorigenesis of colorectal cancers.
30715269	7	2	theme	YY1	910:912	arg1	capacities					896:905	the pro-tumorigenic capacities	876:905	the pro-tumorigenic capacities of YY1	876:912	Furthermore, we identified the main putative O-GlcNAc site of YY1 at Thr236, and mutating of this site decreased the pro-tumorigenic capacities of YY1.
30715269	3	3	theme	YY1	369:371	arg1	O-GlcNAcylation					350:364	O-GlcNAcylation	350:364	O-GlcNAcylation of YY1	350:371	Here, we demonstrated that YY1 was O-GlcNAcylated by OGT and O-GlcNAcylation of YY1 could increase the protein expression by enhancing its stability.
30715269	8	4	dep	potential	1074:1082	arg1	therapeutic					1094:1104	therapeutic	1094:1104	therapeutic	1094:1104	We concluded that O-GlcNAcylation of YY1 stimulates tumorigenesis in CRC cells by targeting SLC22A15 and AANAT, suggesting that YY1 O-GlcNAcylation might be a potential effective therapeutic target for treating CRC.
30715269	8	5	theme	potential	1074:1082	arg1	target					1106:1111	a potential effective therapeutic target	1072:1111	a potential effective therapeutic target for treating CRC	1072:1128	We concluded that O-GlcNAcylation of YY1 stimulates tumorigenesis in CRC cells by targeting SLC22A15 and AANAT, suggesting that YY1 O-GlcNAcylation might be a potential effective therapeutic target for treating CRC.
30715269	8	5	theme	potential	1074:1082	arg1	O-GlcNAcylation					1047:1061	YY1 O-GlcNAcylation	1043:1061	YY1 O-GlcNAcylation	1043:1061	We concluded that O-GlcNAcylation of YY1 stimulates tumorigenesis in CRC cells by targeting SLC22A15 and AANAT, suggesting that YY1 O-GlcNAcylation might be a potential effective therapeutic target for treating CRC.
30715269	7	6	theme	pro-tumorigenic	880:894	arg1	capacities					896:905	the pro-tumorigenic capacities	876:905	the pro-tumorigenic capacities of YY1	876:912	Furthermore, we identified the main putative O-GlcNAc site of YY1 at Thr236, and mutating of this site decreased the pro-tumorigenic capacities of YY1.
30715269	7	7	from	Thr236	832:837	arg1	YY1					825:827	YY1	825:827	YY1	825:827	Furthermore, we identified the main putative O-GlcNAc site of YY1 at Thr236, and mutating of this site decreased the pro-tumorigenic capacities of YY1.
30715269	7	7	from	Thr236	832:837	arg1	site					817:820	the main putative O-GlcNAc site	790:820	the main putative O-GlcNAc site of YY1 at Thr236	790:837	Furthermore, we identified the main putative O-GlcNAc site of YY1 at Thr236, and mutating of this site decreased the pro-tumorigenic capacities of YY1.
30715269	8	8	theme	YY1	1043:1045	arg1	target					1106:1111	a potential effective therapeutic target	1072:1111	a potential effective therapeutic target for treating CRC	1072:1128	We concluded that O-GlcNAcylation of YY1 stimulates tumorigenesis in CRC cells by targeting SLC22A15 and AANAT, suggesting that YY1 O-GlcNAcylation might be a potential effective therapeutic target for treating CRC.
30715269	8	8	theme	YY1	1043:1045	arg1	O-GlcNAcylation					1047:1061	YY1 O-GlcNAcylation	1043:1061	YY1 O-GlcNAcylation	1043:1061	We concluded that O-GlcNAcylation of YY1 stimulates tumorigenesis in CRC cells by targeting SLC22A15 and AANAT, suggesting that YY1 O-GlcNAcylation might be a potential effective therapeutic target for treating CRC.
30715269	6	9	theme	stimulated	737:746	arg1	tumorigenesis					748:760	the YY1 stimulated tumorigenesis	729:760	the YY1 stimulated tumorigenesis	729:760	Besides, we also identified the oncoproteins, SLC22A15 and AANAT, which were regulated by YY1 directly, are responsible for the YY1 stimulated tumorigenesis.
30715269	3	10	theme	protein	392:398	arg1	expression					400:409	the protein expression	388:409	the protein expression	388:409	Here, we demonstrated that YY1 was O-GlcNAcylated by OGT and O-GlcNAcylation of YY1 could increase the protein expression by enhancing its stability.
30715269	0	11	from	tumorigenesis	34:46	arg1	cells					69:73	colorectal cancer cells	51:73	colorectal cancer cells	51:73	O-GlcNAcylation of YY1 stimulates tumorigenesis in colorectal cancer cells by targeting SLC22A15 and AANAT.
30715269	6	12	theme	YY1	733:735	arg1	tumorigenesis					748:760	the YY1 stimulated tumorigenesis	729:760	the YY1 stimulated tumorigenesis	729:760	Besides, we also identified the oncoproteins, SLC22A15 and AANAT, which were regulated by YY1 directly, are responsible for the YY1 stimulated tumorigenesis.
30715269	8	13	from	tumorigenesis	967:979	arg1	cells					988:992	CRC cells	984:992	CRC cells	984:992	We concluded that O-GlcNAcylation of YY1 stimulates tumorigenesis in CRC cells by targeting SLC22A15 and AANAT, suggesting that YY1 O-GlcNAcylation might be a potential effective therapeutic target for treating CRC.
30715269	1	14	theme	colorectal	204:213	arg1	cancers					215:221	colorectal cancers	204:221	colorectal cancers	204:221	Emerging studies have revealed that O-GlcNAcylation plays pivotal roles in the tumorigenesis of colorectal cancers.
30715269	0	15	theme	YY1	19:21	arg1	O-GlcNAcylation					0:14	O-GlcNAcylation	0:14	O-GlcNAcylation of YY1	0:21	O-GlcNAcylation of YY1 stimulates tumorigenesis in colorectal cancer cells by targeting SLC22A15 and AANAT.
30715269	1	16	theme	Emerging	108:115	arg1	studies					117:123	Emerging studies	108:123	Emerging studies	108:123	Emerging studies have revealed that O-GlcNAcylation plays pivotal roles in the tumorigenesis of colorectal cancers.
30715269	8	17	theme	YY1	952:954	arg1	O-GlcNAcylation					933:947	O-GlcNAcylation	933:947	O-GlcNAcylation of YY1	933:954	We concluded that O-GlcNAcylation of YY1 stimulates tumorigenesis in CRC cells by targeting SLC22A15 and AANAT, suggesting that YY1 O-GlcNAcylation might be a potential effective therapeutic target for treating CRC.
30715269	1	18	theme	cancers	215:221	arg1	tumorigenesis					187:199	the tumorigenesis	183:199	the tumorigenesis of colorectal cancers	183:221	Emerging studies have revealed that O-GlcNAcylation plays pivotal roles in the tumorigenesis of colorectal cancers.
30715269	7	19	theme	YY1	825:827	arg1	YY1					825:827	YY1	825:827	YY1	825:827	Furthermore, we identified the main putative O-GlcNAc site of YY1 at Thr236, and mutating of this site decreased the pro-tumorigenic capacities of YY1.
30715269	7	19	theme	YY1	825:827	arg1	site					817:820	the main putative O-GlcNAc site	790:820	the main putative O-GlcNAc site of YY1 at Thr236	790:837	Furthermore, we identified the main putative O-GlcNAc site of YY1 at Thr236, and mutating of this site decreased the pro-tumorigenic capacities of YY1.
30715269	4	20	theme	cell	500:503	arg1	phenotypes					482:491	transformative phenotypes	467:491	transformative phenotypes of CRC cell	467:503	O-GlcNAcylation facilitated transformative phenotypes of CRC cell in a YY1-dependent manner.
30715269	2	21	theme	underlying	237:246	arg1	mechanism					248:256	the underlying mechanism	233:256	the underlying mechanism	233:256	However, the underlying mechanism still remains largely unknown.
30715269	0	22	theme	cancer	62:67	arg1	cells					69:73	colorectal cancer cells	51:73	colorectal cancer cells	51:73	O-GlcNAcylation of YY1 stimulates tumorigenesis in colorectal cancer cells by targeting SLC22A15 and AANAT.
30715269	4	23	theme	CRC	496:498	arg1	cell					500:503	CRC cell	496:503	CRC cell	496:503	O-GlcNAcylation facilitated transformative phenotypes of CRC cell in a YY1-dependent manner.
30715269	0	24	theme	colorectal	51:60	arg1	cells					69:73	colorectal cancer cells	51:73	colorectal cancer cells	51:73	O-GlcNAcylation of YY1 stimulates tumorigenesis in colorectal cancer cells by targeting SLC22A15 and AANAT.
30715269	8	25	theme	CRC	984:986	arg1	cells					988:992	CRC cells	984:992	CRC cells	984:992	We concluded that O-GlcNAcylation of YY1 stimulates tumorigenesis in CRC cells by targeting SLC22A15 and AANAT, suggesting that YY1 O-GlcNAcylation might be a potential effective therapeutic target for treating CRC.
30715269	7	26	theme	putative	799:806	arg1	YY1					825:827	YY1	825:827	YY1	825:827	Furthermore, we identified the main putative O-GlcNAc site of YY1 at Thr236, and mutating of this site decreased the pro-tumorigenic capacities of YY1.
30715269	7	26	theme	putative	799:806	arg1	site					817:820	the main putative O-GlcNAc site	790:820	the main putative O-GlcNAc site of YY1 at Thr236	790:837	Furthermore, we identified the main putative O-GlcNAc site of YY1 at Thr236, and mutating of this site decreased the pro-tumorigenic capacities of YY1.
30715269	4	27	theme	transformative	467:480	arg1	phenotypes					482:491	transformative phenotypes	467:491	transformative phenotypes of CRC cell	467:503	O-GlcNAcylation facilitated transformative phenotypes of CRC cell in a YY1-dependent manner.
30715269	7	28	theme	O-GlcNAc	808:815	arg1	YY1					825:827	YY1	825:827	YY1	825:827	Furthermore, we identified the main putative O-GlcNAc site of YY1 at Thr236, and mutating of this site decreased the pro-tumorigenic capacities of YY1.
30715269	7	28	theme	O-GlcNAc	808:815	arg1	site					817:820	the main putative O-GlcNAc site	790:820	the main putative O-GlcNAc site of YY1 at Thr236	790:837	Furthermore, we identified the main putative O-GlcNAc site of YY1 at Thr236, and mutating of this site decreased the pro-tumorigenic capacities of YY1.
30715269	5	29	theme	YY1-dependent	565:577	arg1	activity					595:602	YY1-dependent transcriptional activity	565:602	YY1-dependent transcriptional activity	565:602	Also, O-GlcNAcylation stimulates YY1-dependent transcriptional activity.
30715269	5	30	theme	transcriptional	579:593	arg1	activity					595:602	YY1-dependent transcriptional activity	565:602	YY1-dependent transcriptional activity	565:602	Also, O-GlcNAcylation stimulates YY1-dependent transcriptional activity.
30715269	7	31	theme	main	794:797	arg1	YY1					825:827	YY1	825:827	YY1	825:827	Furthermore, we identified the main putative O-GlcNAc site of YY1 at Thr236, and mutating of this site decreased the pro-tumorigenic capacities of YY1.
30715269	7	31	theme	main	794:797	arg1	site					817:820	the main putative O-GlcNAc site	790:820	the main putative O-GlcNAc site of YY1 at Thr236	790:837	Furthermore, we identified the main putative O-GlcNAc site of YY1 at Thr236, and mutating of this site decreased the pro-tumorigenic capacities of YY1.
34939084	3	0	theme	many	340:343	arg1	pathways					355:362	many metabolic pathways	340:362	many metabolic pathways	340:362	It promotes the invasion, metastasis, proliferation and survival of tumor cells, and alters many metabolic pathways.
34939084	11	1	theme	post-translational	1275:1292	arg1	network					1305:1311	the intricate post-translational regulation network	1261:1311	the intricate post-translational regulation network of PYGL	1261:1319	Our results provided another molecular insight into the intricate post-translational regulation network of PYGL.
34939084	3	2	theme	metabolic	345:353	arg1	pathways					355:362	many metabolic pathways	340:362	many metabolic pathways	340:362	It promotes the invasion, metastasis, proliferation and survival of tumor cells, and alters many metabolic pathways.
34939084	4	3	theme	important	449:457	arg1	it					440:441	it	440:441	it	440:441	Glycogen metabolism increases in a wide variety of tumors, suggesting that it is an important aspect of cancer pathophysiology.
34939084	4	3	theme	important	449:457	arg1	aspect					459:464	an important aspect	446:464	an important aspect of cancer pathophysiology	446:490	Glycogen metabolism increases in a wide variety of tumors, suggesting that it is an important aspect of cancer pathophysiology.
34939084	5	4	theme	glycogen	611:618	arg1	pathway					631:637	the glycogen metabolism pathway	607:637	the glycogen metabolism pathway	607:637	Herein we focused on the O-GlcNAcylation of liver glycogen phosphorylase (PYGL)-an important catabolism enzyme in the glycogen metabolism pathway.
34939084	11	5	theme	PYGL	1316:1319	arg1	network					1305:1311	the intricate post-translational regulation network	1261:1311	the intricate post-translational regulation network of PYGL	1261:1319	Our results provided another molecular insight into the intricate post-translational regulation network of PYGL.
34939084	9	6	theme	Ser430	1055:1060	arg1	O-GlcNAcylation					1062:1076	Ser430 O-GlcNAcylation	1055:1076	Ser430 O-GlcNAcylation	1055:1076	Lastly, we found that Ser430 O-GlcNAcylation was fundamental for PYGL activity.
34939084	5	7	theme	metabolism	620:629	arg1	pathway					631:637	the glycogen metabolism pathway	607:637	the glycogen metabolism pathway	607:637	Herein we focused on the O-GlcNAcylation of liver glycogen phosphorylase (PYGL)-an important catabolism enzyme in the glycogen metabolism pathway.
34939084	8	8	theme	O-GlcNAcylation	916:930	arg1	site					932:935	the major O-GlcNAcylation site	906:935	the major O-GlcNAcylation site	906:935	Then, we identified the major O-GlcNAcylation site to be Ser430, and demonstrated that pSer15 and Ser430 O-GlcNAcylation were mutually reinforced.
34939084	8	9	theme	Ser430	984:989	arg1	O-GlcNAcylation					991:1005	Ser430 O-GlcNAcylation	984:1005	Ser430 O-GlcNAcylation	984:1005	Then, we identified the major O-GlcNAcylation site to be Ser430, and demonstrated that pSer15 and Ser430 O-GlcNAcylation were mutually reinforced.
34939084	5	10	dep	-an	572:574	arg1	phosphorylase					552:564	liver glycogen phosphorylase	537:564	liver glycogen phosphorylase	537:564	Herein we focused on the O-GlcNAcylation of liver glycogen phosphorylase (PYGL)-an important catabolism enzyme in the glycogen metabolism pathway.
34939084	4	11	theme	wide	400:403	arg1	variety					405:411	a wide variety	398:411	a wide variety of tumors	398:421	Glycogen metabolism increases in a wide variety of tumors, suggesting that it is an important aspect of cancer pathophysiology.
34939084	4	11	theme	wide	400:403	arg1	tumors					416:421	tumors	416:421	tumors	416:421	Glycogen metabolism increases in a wide variety of tumors, suggesting that it is an important aspect of cancer pathophysiology.
34939084	1	12	theme	post-translational	91:108	arg1	O-GlcNAcylation					70:84	O-GlcNAcylation	70:84	O-GlcNAcylation	70:84	O-GlcNAcylation is a post-translational modification that links metabolism with signal transduction.
34939084	1	12	theme	post-translational	91:108	arg1	modification					110:121	a post-translational modification	89:121	a post-translational modification that links metabolism with signal transduction	89:168	O-GlcNAcylation is a post-translational modification that links metabolism with signal transduction.
34939084	7	13	theme	Na2S2O4	856:862	arg1	conditions					874:883	glucagon and Na2S2O4 (hypoxia) conditions	843:883	glucagon and Na2S2O4 (hypoxia) conditions	843:883	And both PYGL O-GlcNAcylation and phosphorylation of Ser15 (pSer15) were decreased under glucose and insulin, whereas increased under glucagon and Na2S2O4 (hypoxia) conditions.
34939084	2	14	theme	High	171:174	arg1	O-GlcNAcylation					176:190	High O-GlcNAcylation	171:190	High O-GlcNAcylation	171:190	High O-GlcNAcylation appears to be a general characteristic of cancer cells.
34939084	2	14	theme	High	171:174	arg1	characteristic					216:229	a general characteristic	206:229	a general characteristic of cancer cells	206:245	High O-GlcNAcylation appears to be a general characteristic of cancer cells.
34939084	5	15	theme	enzyme	597:602	arg1	O-GlcNAcylation					518:532	the O-GlcNAcylation	514:532	the O-GlcNAcylation of liver glycogen phosphorylase (PYGL)-an important catabolism enzyme in the glycogen metabolism pathway	514:637	Herein we focused on the O-GlcNAcylation of liver glycogen phosphorylase (PYGL)-an important catabolism enzyme in the glycogen metabolism pathway.
34939084	9	16	theme	PYGL	1098:1101	arg1	activity					1103:1110	PYGL activity	1098:1110	PYGL activity	1098:1110	Lastly, we found that Ser430 O-GlcNAcylation was fundamental for PYGL activity.
34939084	7	17	theme	glucagon	843:850	arg1	conditions					874:883	glucagon and Na2S2O4 (hypoxia) conditions	843:883	glucagon and Na2S2O4 (hypoxia) conditions	843:883	And both PYGL O-GlcNAcylation and phosphorylation of Ser15 (pSer15) were decreased under glucose and insulin, whereas increased under glucagon and Na2S2O4 (hypoxia) conditions.
34939084	7	18	theme	PYGL	718:721	arg1	O-GlcNAcylation					723:737	PYGL O-GlcNAcylation	718:737	PYGL O-GlcNAcylation	718:737	And both PYGL O-GlcNAcylation and phosphorylation of Ser15 (pSer15) were decreased under glucose and insulin, whereas increased under glucagon and Na2S2O4 (hypoxia) conditions.
34939084	10	19	theme	PYGL	1138:1141	arg1	O-GlcNAcylation					1119:1133	O-GlcNAcylation	1119:1133	O-GlcNAcylation of PYGL	1119:1141	Thus, O-GlcNAcylation of PYGL positively regulated pSer15 and therefore its enzymatic activity.
34939084	3	20	dep	invasion	264:271	arg1	the					260:262	the	260:262	the	260:262	It promotes the invasion, metastasis, proliferation and survival of tumor cells, and alters many metabolic pathways.
34939084	3	21	theme	tumor	316:320	arg1	cells					322:326	tumor cells	316:326	tumor cells	316:326	It promotes the invasion, metastasis, proliferation and survival of tumor cells, and alters many metabolic pathways.
34939084	8	22	theme	major	910:914	arg1	site					932:935	the major O-GlcNAcylation site	906:935	the major O-GlcNAcylation site	906:935	Then, we identified the major O-GlcNAcylation site to be Ser430, and demonstrated that pSer15 and Ser430 O-GlcNAcylation were mutually reinforced.
34939084	11	23	theme	intricate	1265:1273	arg1	network					1305:1311	the intricate post-translational regulation network	1261:1311	the intricate post-translational regulation network of PYGL	1261:1319	Our results provided another molecular insight into the intricate post-translational regulation network of PYGL.
34939084	11	24	theme	molecular	1238:1246	arg1	insight					1248:1254	another molecular insight	1230:1254	another molecular insight into the intricate post-translational regulation network of PYGL	1230:1319	Our results provided another molecular insight into the intricate post-translational regulation network of PYGL.
34939084	2	25	theme	general	208:214	arg1	O-GlcNAcylation					176:190	High O-GlcNAcylation	171:190	High O-GlcNAcylation	171:190	High O-GlcNAcylation appears to be a general characteristic of cancer cells.
34939084	2	25	theme	general	208:214	arg1	characteristic					216:229	a general characteristic	206:229	a general characteristic of cancer cells	206:245	High O-GlcNAcylation appears to be a general characteristic of cancer cells.
34939084	5	26	theme	catabolism	586:595	arg1	enzyme					597:602	liver glycogen phosphorylase (PYGL)-an important catabolism enzyme	537:602	liver glycogen phosphorylase (PYGL)-an important catabolism enzyme	537:602	Herein we focused on the O-GlcNAcylation of liver glycogen phosphorylase (PYGL)-an important catabolism enzyme in the glycogen metabolism pathway.
34939084	4	27	theme	pathophysiology	476:490	arg1	it					440:441	it	440:441	it	440:441	Glycogen metabolism increases in a wide variety of tumors, suggesting that it is an important aspect of cancer pathophysiology.
34939084	4	27	theme	pathophysiology	476:490	arg1	aspect					459:464	an important aspect	446:464	an important aspect of cancer pathophysiology	446:490	Glycogen metabolism increases in a wide variety of tumors, suggesting that it is an important aspect of cancer pathophysiology.
34939084	10	28	theme	enzymatic	1189:1197	arg1	activity					1199:1206	its enzymatic activity	1185:1206	its enzymatic activity	1185:1206	Thus, O-GlcNAcylation of PYGL positively regulated pSer15 and therefore its enzymatic activity.
34939084	11	29	theme	regulation	1294:1303	arg1	network					1305:1311	the intricate post-translational regulation network	1261:1311	the intricate post-translational regulation network of PYGL	1261:1319	Our results provided another molecular insight into the intricate post-translational regulation network of PYGL.
34939084	4	30	theme	cancer	469:474	arg1	pathophysiology					476:490	cancer pathophysiology	469:490	cancer pathophysiology	469:490	Glycogen metabolism increases in a wide variety of tumors, suggesting that it is an important aspect of cancer pathophysiology.
34939084	4	31	theme	Glycogen	365:372	arg1	metabolism					374:383	Glycogen metabolism	365:383	Glycogen metabolism	365:383	Glycogen metabolism increases in a wide variety of tumors, suggesting that it is an important aspect of cancer pathophysiology.
34939084	5	32	theme	-an	572:574	arg1	enzyme					597:602	liver glycogen phosphorylase (PYGL)-an important catabolism enzyme	537:602	liver glycogen phosphorylase (PYGL)-an important catabolism enzyme	537:602	Herein we focused on the O-GlcNAcylation of liver glycogen phosphorylase (PYGL)-an important catabolism enzyme in the glycogen metabolism pathway.
34939084	1	33	theme	signal	150:155	arg1	transduction					157:168	signal transduction	150:168	signal transduction	150:168	O-GlcNAcylation is a post-translational modification that links metabolism with signal transduction.
34939084	3	34	theme	cells	322:326	arg1	metastasis					274:283	metastasis	274:283	metastasis	274:283	It promotes the invasion, metastasis, proliferation and survival of tumor cells, and alters many metabolic pathways.
34939084	3	34	theme	cells	322:326	arg1	invasion					264:271	invasion	264:271	invasion	264:271	It promotes the invasion, metastasis, proliferation and survival of tumor cells, and alters many metabolic pathways.
34939084	3	34	theme	cells	322:326	arg1	survival					304:311	survival	304:311	survival	304:311	It promotes the invasion, metastasis, proliferation and survival of tumor cells, and alters many metabolic pathways.
34939084	3	34	theme	cells	322:326	arg1	proliferation					286:298	proliferation	286:298	proliferation	286:298	It promotes the invasion, metastasis, proliferation and survival of tumor cells, and alters many metabolic pathways.
34939084	2	35	theme	cells	241:245	arg1	O-GlcNAcylation					176:190	High O-GlcNAcylation	171:190	High O-GlcNAcylation	171:190	High O-GlcNAcylation appears to be a general characteristic of cancer cells.
34939084	2	35	theme	cells	241:245	arg1	characteristic					216:229	a general characteristic	206:229	a general characteristic of cancer cells	206:245	High O-GlcNAcylation appears to be a general characteristic of cancer cells.
34939084	5	36	from	O-GlcNAcylation	518:532	arg1	pathway					631:637	the glycogen metabolism pathway	607:637	the glycogen metabolism pathway	607:637	Herein we focused on the O-GlcNAcylation of liver glycogen phosphorylase (PYGL)-an important catabolism enzyme in the glycogen metabolism pathway.
34939084	4	37	theme	tumors	416:421	arg1	variety					405:411	a wide variety	398:411	a wide variety of tumors	398:421	Glycogen metabolism increases in a wide variety of tumors, suggesting that it is an important aspect of cancer pathophysiology.
34939084	4	37	theme	tumors	416:421	arg1	tumors					416:421	tumors	416:421	tumors	416:421	Glycogen metabolism increases in a wide variety of tumors, suggesting that it is an important aspect of cancer pathophysiology.
34939084	5	38	theme	important	576:584	arg1	enzyme					597:602	liver glycogen phosphorylase (PYGL)-an important catabolism enzyme	537:602	liver glycogen phosphorylase (PYGL)-an important catabolism enzyme	537:602	Herein we focused on the O-GlcNAcylation of liver glycogen phosphorylase (PYGL)-an important catabolism enzyme in the glycogen metabolism pathway.
34939084	2	39	theme	cancer	234:239	arg1	cells					241:245	cancer cells	234:245	cancer cells	234:245	High O-GlcNAcylation appears to be a general characteristic of cancer cells.
34939084	5	40	theme	liver	537:541	arg1	phosphorylase					552:564	liver glycogen phosphorylase	537:564	liver glycogen phosphorylase	537:564	Herein we focused on the O-GlcNAcylation of liver glycogen phosphorylase (PYGL)-an important catabolism enzyme in the glycogen metabolism pathway.
34939084	5	41	theme	glycogen	543:550	arg1	phosphorylase					552:564	liver glycogen phosphorylase	537:564	liver glycogen phosphorylase	537:564	Herein we focused on the O-GlcNAcylation of liver glycogen phosphorylase (PYGL)-an important catabolism enzyme in the glycogen metabolism pathway.
34939084	6	42	theme	HEK	663:665	arg1	293T					667:670	HEK 293T	663:670	HEK 293T	663:670	PYGL expressed in both HEK 293T and HCT116 was modified by O-GlcNAc.
34939084	7	43	theme	Ser15	762:766	arg1	phosphorylation					743:757	phosphorylation	743:757	phosphorylation of Ser15 (pSer15)	743:775	And both PYGL O-GlcNAcylation and phosphorylation of Ser15 (pSer15) were decreased under glucose and insulin, whereas increased under glucagon and Na2S2O4 (hypoxia) conditions.
34939084	7	43	theme	Ser15	762:766	arg1	O-GlcNAcylation					723:737	PYGL O-GlcNAcylation	718:737	PYGL O-GlcNAcylation	718:737	And both PYGL O-GlcNAcylation and phosphorylation of Ser15 (pSer15) were decreased under glucose and insulin, whereas increased under glucagon and Na2S2O4 (hypoxia) conditions.
34939084	0	44	theme	PYGL	26:29	arg1	activity					31:38	PYGL activity	26:38	PYGL activity	26:38	O-GlcNAcylation increases PYGL activity by promoting phosphorylation.
34939084	6	45	mod	modified	687:694	arg1	PYGL					640:643	PYGL	640:643	PYGL expressed in both HEK 293T and HCT116	640:681	PYGL expressed in both HEK 293T and HCT116 was modified by O-GlcNAc.
34939084	6	45	mod	modified	687:694	arg3	O-GlcNAc					699:706	O-GlcNAc	699:706	O-GlcNAc	699:706	PYGL expressed in both HEK 293T and HCT116 was modified by O-GlcNAc.
25484640	1	0	link	O-linked	80:87	arg1	modification					122:133	O-linked β-N-acetylglucosamine (O-GlcNAc) modification	80:133	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of proteins	80:145	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of proteins has been shown to be involved in many different cellular processes, such as cell cycle control, nutrient sensing, signal transduction, stress response and transcriptional regulation.
25484640	2	1	theme	complex	351:357	arg1	systems					370:376	complex regulatory systems	351:376	complex regulatory systems	351:376	Cells have developed complex regulatory systems in order to regulate gene expression appropriately in response to environmental and intracellular cues.
25484640	3	2	theme	manners	740:746	arg1	manners					740:746	manners	740:746	manners	740:746	Control of eukaryotic gene transcription often involves post-translational modification of a multitude of proteins including transcription factors, basal transcription machinery, and chromatin remodeling complexes to modulate their functions in a variety of manners.
25484640	3	2	theme	manners	740:746	arg1	variety					729:735	a variety	727:735	a variety of manners	727:746	Control of eukaryotic gene transcription often involves post-translational modification of a multitude of proteins including transcription factors, basal transcription machinery, and chromatin remodeling complexes to modulate their functions in a variety of manners.
25484640	3	3	theme	multitude	575:583	arg1	modification					557:568	post-translational modification	538:568	post-translational modification of a multitude of proteins including transcription factors, basal transcription machinery, and chromatin remodeling complexes to modulate their functions in a variety of manners	538:746	Control of eukaryotic gene transcription often involves post-translational modification of a multitude of proteins including transcription factors, basal transcription machinery, and chromatin remodeling complexes to modulate their functions in a variety of manners.
25484640	4	4	theme	functional	789:798	arg1	roles					800:804	the emerging functional roles	776:804	the emerging functional roles for and techniques to detect and modulate the O-GlcNAc modification	776:872	In this review we describe the emerging functional roles for and techniques to detect and modulate the O-GlcNAc modification and illustrate that the O-GlcNAc modification is intricately involved in at least seven different general mechanisms for the control of gene transcription.
25484640	1	5	theme	nutrient	243:250	arg1	sensing					252:258	nutrient sensing	243:258	nutrient sensing	243:258	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of proteins has been shown to be involved in many different cellular processes, such as cell cycle control, nutrient sensing, signal transduction, stress response and transcriptional regulation.
25484640	3	6	theme	transcription	607:619	arg1	factors					621:627	transcription factors	607:627	transcription factors	607:627	Control of eukaryotic gene transcription often involves post-translational modification of a multitude of proteins including transcription factors, basal transcription machinery, and chromatin remodeling complexes to modulate their functions in a variety of manners.
25484640	3	7	theme	eukaryotic	493:502	arg1	transcription					509:521	eukaryotic gene transcription	493:521	eukaryotic gene transcription	493:521	Control of eukaryotic gene transcription often involves post-translational modification of a multitude of proteins including transcription factors, basal transcription machinery, and chromatin remodeling complexes to modulate their functions in a variety of manners.
25484640	4	8	theme	transcription	1015:1027	arg1	control					999:1005	the control	995:1005	the control of gene transcription	995:1027	In this review we describe the emerging functional roles for and techniques to detect and modulate the O-GlcNAc modification and illustrate that the O-GlcNAc modification is intricately involved in at least seven different general mechanisms for the control of gene transcription.
25484640	4	9	theme	emerging	780:787	arg1	roles					800:804	the emerging functional roles	776:804	the emerging functional roles for and techniques to detect and modulate the O-GlcNAc modification	776:872	In this review we describe the emerging functional roles for and techniques to detect and modulate the O-GlcNAc modification and illustrate that the O-GlcNAc modification is intricately involved in at least seven different general mechanisms for the control of gene transcription.
25484640	4	10	theme	gene	1010:1013	arg1	transcription					1015:1027	gene transcription	1010:1027	gene transcription	1010:1027	In this review we describe the emerging functional roles for and techniques to detect and modulate the O-GlcNAc modification and illustrate that the O-GlcNAc modification is intricately involved in at least seven different general mechanisms for the control of gene transcription.
25484640	1	11	theme	O-linked	80:87	arg1	modification					122:133	O-linked β-N-acetylglucosamine (O-GlcNAc) modification	80:133	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of proteins	80:145	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of proteins has been shown to be involved in many different cellular processes, such as cell cycle control, nutrient sensing, signal transduction, stress response and transcriptional regulation.
25484640	4	12	dep	techniques	814:823	arg1	modulate					839:846	modulate	839:846	modulate the O-GlcNAc modification	839:872	In this review we describe the emerging functional roles for and techniques to detect and modulate the O-GlcNAc modification and illustrate that the O-GlcNAc modification is intricately involved in at least seven different general mechanisms for the control of gene transcription.
25484640	4	12	dep	techniques	814:823	arg1	detect					828:833	detect	828:833	detect	828:833	In this review we describe the emerging functional roles for and techniques to detect and modulate the O-GlcNAc modification and illustrate that the O-GlcNAc modification is intricately involved in at least seven different general mechanisms for the control of gene transcription.
25484640	1	13	mod	modification	122:133	arg3	O-GlcNAc					112:119	O-linked β-N-acetylglucosamine (O-GlcNAc) modification	80:133	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of proteins	80:145	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of proteins has been shown to be involved in many different cellular processes, such as cell cycle control, nutrient sensing, signal transduction, stress response and transcriptional regulation.
25484640	1	13	mod	modification	122:133	arg1	proteins					138:145	proteins	138:145	proteins	138:145	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of proteins has been shown to be involved in many different cellular processes, such as cell cycle control, nutrient sensing, signal transduction, stress response and transcriptional regulation.
25484640	1	13	mod	modification	122:133	arg3	β-N-acetylglucosamine					89:109	O-linked β-N-acetylglucosamine (O-GlcNAc) modification	80:133	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of proteins	80:145	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of proteins has been shown to be involved in many different cellular processes, such as cell cycle control, nutrient sensing, signal transduction, stress response and transcriptional regulation.
25484640	2	14	theme	environmental	444:456	arg1	cues					476:479	environmental and intracellular cues	444:479	environmental and intracellular cues	444:479	Cells have developed complex regulatory systems in order to regulate gene expression appropriately in response to environmental and intracellular cues.
25484640	4	15	theme	O-GlcNAc	898:905	arg1	modification					907:918	the O-GlcNAc modification	894:918	the O-GlcNAc modification	894:918	In this review we describe the emerging functional roles for and techniques to detect and modulate the O-GlcNAc modification and illustrate that the O-GlcNAc modification is intricately involved in at least seven different general mechanisms for the control of gene transcription.
25484640	1	16	theme	β-N-acetylglucosamine	89:109	arg1	modification					122:133	O-linked β-N-acetylglucosamine (O-GlcNAc) modification	80:133	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of proteins	80:145	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of proteins has been shown to be involved in many different cellular processes, such as cell cycle control, nutrient sensing, signal transduction, stress response and transcriptional regulation.
25484640	1	17	theme	many	180:183	arg1	response					289:296	stress response	282:296	stress response	282:296	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of proteins has been shown to be involved in many different cellular processes, such as cell cycle control, nutrient sensing, signal transduction, stress response and transcriptional regulation.
25484640	1	17	theme	many	180:183	arg1	transduction					268:279	signal transduction	261:279	signal transduction	261:279	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of proteins has been shown to be involved in many different cellular processes, such as cell cycle control, nutrient sensing, signal transduction, stress response and transcriptional regulation.
25484640	1	17	theme	many	180:183	arg1	regulation					318:327	transcriptional regulation	302:327	transcriptional regulation	302:327	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of proteins has been shown to be involved in many different cellular processes, such as cell cycle control, nutrient sensing, signal transduction, stress response and transcriptional regulation.
25484640	1	17	theme	many	180:183	arg1	processes					204:212	many different cellular processes	180:212	many different cellular processes	180:212	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of proteins has been shown to be involved in many different cellular processes, such as cell cycle control, nutrient sensing, signal transduction, stress response and transcriptional regulation.
25484640	1	17	theme	many	180:183	arg1	control					234:240	cell cycle control	223:240	cell cycle control	223:240	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of proteins has been shown to be involved in many different cellular processes, such as cell cycle control, nutrient sensing, signal transduction, stress response and transcriptional regulation.
25484640	1	17	theme	many	180:183	arg1	sensing					252:258	nutrient sensing	243:258	nutrient sensing	243:258	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of proteins has been shown to be involved in many different cellular processes, such as cell cycle control, nutrient sensing, signal transduction, stress response and transcriptional regulation.
25484640	1	18	theme	signal	261:266	arg1	transduction					268:279	signal transduction	261:279	signal transduction	261:279	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of proteins has been shown to be involved in many different cellular processes, such as cell cycle control, nutrient sensing, signal transduction, stress response and transcriptional regulation.
25484640	3	19	theme	proteins	588:595	arg1	multitude					575:583	a multitude	573:583	a multitude of proteins including transcription factors, basal transcription machinery, and chromatin remodeling complexes	573:694	Control of eukaryotic gene transcription often involves post-translational modification of a multitude of proteins including transcription factors, basal transcription machinery, and chromatin remodeling complexes to modulate their functions in a variety of manners.
25484640	1	20	theme	different	185:193	arg1	response					289:296	stress response	282:296	stress response	282:296	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of proteins has been shown to be involved in many different cellular processes, such as cell cycle control, nutrient sensing, signal transduction, stress response and transcriptional regulation.
25484640	1	20	theme	different	185:193	arg1	transduction					268:279	signal transduction	261:279	signal transduction	261:279	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of proteins has been shown to be involved in many different cellular processes, such as cell cycle control, nutrient sensing, signal transduction, stress response and transcriptional regulation.
25484640	1	20	theme	different	185:193	arg1	regulation					318:327	transcriptional regulation	302:327	transcriptional regulation	302:327	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of proteins has been shown to be involved in many different cellular processes, such as cell cycle control, nutrient sensing, signal transduction, stress response and transcriptional regulation.
25484640	1	20	theme	different	185:193	arg1	processes					204:212	many different cellular processes	180:212	many different cellular processes	180:212	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of proteins has been shown to be involved in many different cellular processes, such as cell cycle control, nutrient sensing, signal transduction, stress response and transcriptional regulation.
25484640	1	20	theme	different	185:193	arg1	control					234:240	cell cycle control	223:240	cell cycle control	223:240	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of proteins has been shown to be involved in many different cellular processes, such as cell cycle control, nutrient sensing, signal transduction, stress response and transcriptional regulation.
25484640	1	20	theme	different	185:193	arg1	sensing					252:258	nutrient sensing	243:258	nutrient sensing	243:258	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of proteins has been shown to be involved in many different cellular processes, such as cell cycle control, nutrient sensing, signal transduction, stress response and transcriptional regulation.
25484640	4	21	theme	general	972:978	arg1	mechanisms					980:989	at least seven different general mechanisms	947:989	at least seven different general mechanisms for the control of gene transcription	947:1027	In this review we describe the emerging functional roles for and techniques to detect and modulate the O-GlcNAc modification and illustrate that the O-GlcNAc modification is intricately involved in at least seven different general mechanisms for the control of gene transcription.
25484640	1	22	theme	O-GlcNAc	112:119	arg1	modification					122:133	O-linked β-N-acetylglucosamine (O-GlcNAc) modification	80:133	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of proteins	80:145	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of proteins has been shown to be involved in many different cellular processes, such as cell cycle control, nutrient sensing, signal transduction, stress response and transcriptional regulation.
25484640	1	23	theme	cellular	195:202	arg1	response					289:296	stress response	282:296	stress response	282:296	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of proteins has been shown to be involved in many different cellular processes, such as cell cycle control, nutrient sensing, signal transduction, stress response and transcriptional regulation.
25484640	1	23	theme	cellular	195:202	arg1	transduction					268:279	signal transduction	261:279	signal transduction	261:279	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of proteins has been shown to be involved in many different cellular processes, such as cell cycle control, nutrient sensing, signal transduction, stress response and transcriptional regulation.
25484640	1	23	theme	cellular	195:202	arg1	regulation					318:327	transcriptional regulation	302:327	transcriptional regulation	302:327	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of proteins has been shown to be involved in many different cellular processes, such as cell cycle control, nutrient sensing, signal transduction, stress response and transcriptional regulation.
25484640	1	23	theme	cellular	195:202	arg1	processes					204:212	many different cellular processes	180:212	many different cellular processes	180:212	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of proteins has been shown to be involved in many different cellular processes, such as cell cycle control, nutrient sensing, signal transduction, stress response and transcriptional regulation.
25484640	1	23	theme	cellular	195:202	arg1	control					234:240	cell cycle control	223:240	cell cycle control	223:240	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of proteins has been shown to be involved in many different cellular processes, such as cell cycle control, nutrient sensing, signal transduction, stress response and transcriptional regulation.
25484640	1	23	theme	cellular	195:202	arg1	sensing					252:258	nutrient sensing	243:258	nutrient sensing	243:258	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of proteins has been shown to be involved in many different cellular processes, such as cell cycle control, nutrient sensing, signal transduction, stress response and transcriptional regulation.
25484640	0	24	theme	Modification	25:36	arg1	Role					4:7	The Role	0:7	The Role of the O-GlcNAc Modification in Regulating Eukaryotic Gene Expression	0:77	The Role of the O-GlcNAc Modification in Regulating Eukaryotic Gene Expression.
25484640	3	25	theme	transcription	636:648	arg1	machinery					650:658	basal transcription machinery	630:658	basal transcription machinery	630:658	Control of eukaryotic gene transcription often involves post-translational modification of a multitude of proteins including transcription factors, basal transcription machinery, and chromatin remodeling complexes to modulate their functions in a variety of manners.
25484640	0	26	theme	O-GlcNAc	16:23	arg1	Modification					25:36	the O-GlcNAc Modification	12:36	the O-GlcNAc Modification	12:36	The Role of the O-GlcNAc Modification in Regulating Eukaryotic Gene Expression.
25484640	1	27	theme	stress	282:287	arg1	response					289:296	stress response	282:296	stress response	282:296	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of proteins has been shown to be involved in many different cellular processes, such as cell cycle control, nutrient sensing, signal transduction, stress response and transcriptional regulation.
25484640	4	28	theme	O-GlcNAc	852:859	arg1	modification					861:872	the O-GlcNAc modification	848:872	the O-GlcNAc modification	848:872	In this review we describe the emerging functional roles for and techniques to detect and modulate the O-GlcNAc modification and illustrate that the O-GlcNAc modification is intricately involved in at least seven different general mechanisms for the control of gene transcription.
25484640	2	29	theme	gene	399:402	arg1	expression					404:413	gene expression	399:413	gene expression	399:413	Cells have developed complex regulatory systems in order to regulate gene expression appropriately in response to environmental and intracellular cues.
25484640	3	30	theme	gene	504:507	arg1	transcription					509:521	eukaryotic gene transcription	493:521	eukaryotic gene transcription	493:521	Control of eukaryotic gene transcription often involves post-translational modification of a multitude of proteins including transcription factors, basal transcription machinery, and chromatin remodeling complexes to modulate their functions in a variety of manners.
25484640	2	31	theme	intracellular	462:474	arg1	cues					476:479	environmental and intracellular cues	444:479	environmental and intracellular cues	444:479	Cells have developed complex regulatory systems in order to regulate gene expression appropriately in response to environmental and intracellular cues.
25484640	3	32	theme	basal	630:634	arg1	machinery					650:658	basal transcription machinery	630:658	basal transcription machinery	630:658	Control of eukaryotic gene transcription often involves post-translational modification of a multitude of proteins including transcription factors, basal transcription machinery, and chromatin remodeling complexes to modulate their functions in a variety of manners.
25484640	3	33	theme	transcription	509:521	arg1	Control					482:488	Control	482:488	Control of eukaryotic gene transcription	482:521	Control of eukaryotic gene transcription often involves post-translational modification of a multitude of proteins including transcription factors, basal transcription machinery, and chromatin remodeling complexes to modulate their functions in a variety of manners.
25484640	1	34	theme	transcriptional	302:316	arg1	regulation					318:327	transcriptional regulation	302:327	transcriptional regulation	302:327	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of proteins has been shown to be involved in many different cellular processes, such as cell cycle control, nutrient sensing, signal transduction, stress response and transcriptional regulation.
25484640	4	35	theme	different	962:970	arg1	mechanisms					980:989	at least seven different general mechanisms	947:989	at least seven different general mechanisms for the control of gene transcription	947:1027	In this review we describe the emerging functional roles for and techniques to detect and modulate the O-GlcNAc modification and illustrate that the O-GlcNAc modification is intricately involved in at least seven different general mechanisms for the control of gene transcription.
25484640	3	36	theme	chromatin	665:673	arg1	complexes					686:694	chromatin remodeling complexes	665:694	chromatin remodeling complexes	665:694	Control of eukaryotic gene transcription often involves post-translational modification of a multitude of proteins including transcription factors, basal transcription machinery, and chromatin remodeling complexes to modulate their functions in a variety of manners.
25484640	3	37	theme	remodeling	675:684	arg1	complexes					686:694	chromatin remodeling complexes	665:694	chromatin remodeling complexes	665:694	Control of eukaryotic gene transcription often involves post-translational modification of a multitude of proteins including transcription factors, basal transcription machinery, and chromatin remodeling complexes to modulate their functions in a variety of manners.
25484640	1	38	theme	proteins	138:145	arg1	modification					122:133	O-linked β-N-acetylglucosamine (O-GlcNAc) modification	80:133	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of proteins	80:145	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of proteins has been shown to be involved in many different cellular processes, such as cell cycle control, nutrient sensing, signal transduction, stress response and transcriptional regulation.
25484640	0	39	theme	Gene	63:66	arg1	Expression					68:77	Eukaryotic Gene Expression	52:77	Eukaryotic Gene Expression	52:77	The Role of the O-GlcNAc Modification in Regulating Eukaryotic Gene Expression.
25484640	3	40	theme	post-translational	538:555	arg1	modification					557:568	post-translational modification	538:568	post-translational modification of a multitude of proteins including transcription factors, basal transcription machinery, and chromatin remodeling complexes to modulate their functions in a variety of manners	538:746	Control of eukaryotic gene transcription often involves post-translational modification of a multitude of proteins including transcription factors, basal transcription machinery, and chromatin remodeling complexes to modulate their functions in a variety of manners.
25484640	1	41	theme	cell	223:226	arg1	control					234:240	cell cycle control	223:240	cell cycle control	223:240	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of proteins has been shown to be involved in many different cellular processes, such as cell cycle control, nutrient sensing, signal transduction, stress response and transcriptional regulation.
25484640	0	42	theme	Eukaryotic	52:61	arg1	Expression					68:77	Eukaryotic Gene Expression	52:77	Eukaryotic Gene Expression	52:77	The Role of the O-GlcNAc Modification in Regulating Eukaryotic Gene Expression.
25484640	2	43	theme	regulatory	359:368	arg1	systems					370:376	complex regulatory systems	351:376	complex regulatory systems	351:376	Cells have developed complex regulatory systems in order to regulate gene expression appropriately in response to environmental and intracellular cues.
25484640	1	44	theme	cycle	228:232	arg1	control					234:240	cell cycle control	223:240	cell cycle control	223:240	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of proteins has been shown to be involved in many different cellular processes, such as cell cycle control, nutrient sensing, signal transduction, stress response and transcriptional regulation.
17507370	7	0	theme	proteins	1272:1279	arg1	subset					1258:1263	a subset	1256:1263	a subset of the proteins	1256:1279	O-GlcNAcylation changes on a subset of the proteins were confirmed by follow-up experiments.
17507370	6	1	theme	Quantitative	1032:1043	arg1	measurements					1045:1056	Quantitative measurements	1032:1056	Quantitative measurements	1032:1056	Quantitative measurements indicated that at least 10 proteins had an apparent increase of O-GlcNAcylation upon GSK-3 inhibition by lithium, whereas surprisingly 19 other proteins showed decreases.
17507370	5	2	with	labeling	897:904	arg1	acids					917:921	amino acids	911:921	amino acids in cell culture	911:937	By combining immunoaffinity chromatography and SILAC (stable isotope labeling with amino acids in cell culture)-based quantitative mass spectrometry, we identified 45 potentially O-GlcNAcylated proteins.
17507370	5	3	theme	cell	926:929	arg1	culture					931:937	cell culture	926:937	cell culture	926:937	By combining immunoaffinity chromatography and SILAC (stable isotope labeling with amino acids in cell culture)-based quantitative mass spectrometry, we identified 45 potentially O-GlcNAcylated proteins.
17507370	9	4	theme	MS	1580:1581	arg1	data					1583:1586	the MS data	1576:1586	the MS data	1576:1586	Based on the MS data, we further investigated potential roles of O-GlcNAc on host cell factor-1, a transcription co-activator, and showed that dynamic regulation of O-GlcNAcylation on host cell factor-1 influenced its subcellular distribution.
17507370	8	5	theme	new	1337:1339	arg1	method					1369:1374	a new O-GlcNAc peptide enrichment method	1335:1374	a new O-GlcNAc peptide enrichment method	1335:1374	By combining a new O-GlcNAc peptide enrichment method and beta-elimination followed by Michael addition with DTT, we also mapped the O-GlcNAc site (Ser-55) of vimentin, which showed an apparent increase of O-GlcNAcylation upon GSK-3 inhibition.
17507370	4	6	theme	pivotal	776:782	arg1	kinase					784:789	a pivotal kinase	774:789	a pivotal kinase involved in many signaling pathways	774:825	Here we report the O-GlcNAc perturbations in response to inhibition of glycogen synthase kinase-3 (GSK-3), a pivotal kinase involved in many signaling pathways.
17507370	4	6	theme	pivotal	776:782	arg1	kinase-3					756:763	glycogen synthase kinase-3	738:763	glycogen synthase kinase-3 (GSK-3)	738:771	Here we report the O-GlcNAc perturbations in response to inhibition of glycogen synthase kinase-3 (GSK-3), a pivotal kinase involved in many signaling pathways.
17507370	2	7	theme	dynamic	374:380	arg1	interplay					382:390	a dynamic interplay	372:390	a dynamic interplay with O-phosphate	372:407	O-GlcNAcylation is remarkably similar to O-phosphorylation and appears to have a dynamic interplay with O-phosphate in cellular regulation.
17507370	8	8	theme	peptide	1350:1356	arg1	method					1369:1374	a new O-GlcNAc peptide enrichment method	1335:1374	a new O-GlcNAc peptide enrichment method	1335:1374	By combining a new O-GlcNAc peptide enrichment method and beta-elimination followed by Michael addition with DTT, we also mapped the O-GlcNAc site (Ser-55) of vimentin, which showed an apparent increase of O-GlcNAcylation upon GSK-3 inhibition.
17507370	6	9	theme	apparent	1101:1108	arg1	increase					1110:1117	an apparent increase	1098:1117	an apparent increase of O-GlcNAcylation	1098:1136	Quantitative measurements indicated that at least 10 proteins had an apparent increase of O-GlcNAcylation upon GSK-3 inhibition by lithium, whereas surprisingly 19 other proteins showed decreases.
17507370	4	10	theme	kinase-3	756:763	arg1	inhibition					724:733	inhibition	724:733	inhibition of glycogen synthase kinase-3 (GSK-3), a pivotal kinase involved in many signaling pathways	724:825	Here we report the O-GlcNAc perturbations in response to inhibition of glycogen synthase kinase-3 (GSK-3), a pivotal kinase involved in many signaling pathways.
17507370	10	11	theme	signaling	1933:1941	arg1	networks					1943:1950	signaling networks	1933:1950	signaling networks	1933:1950	Taken together, these data indicated the complex interplay between phosphorylation and O-GlcNAcylation that occurs within signaling networks.
17507370	5	12	theme	quantitative	946:957	arg1	spectrometry					964:975	SILAC (stable isotope labeling with amino acids in cell culture)-based quantitative mass spectrometry	875:975	SILAC (stable isotope labeling with amino acids in cell culture)-based quantitative mass spectrometry	875:975	By combining immunoaffinity chromatography and SILAC (stable isotope labeling with amino acids in cell culture)-based quantitative mass spectrometry, we identified 45 potentially O-GlcNAcylated proteins.
17507370	9	13	theme	potential	1613:1621	arg1	roles					1623:1627	potential roles	1613:1627	potential roles of O-GlcNAc on host cell factor-1, a transcription co-activator,	1613:1692	Based on the MS data, we further investigated potential roles of O-GlcNAc on host cell factor-1, a transcription co-activator, and showed that dynamic regulation of O-GlcNAcylation on host cell factor-1 influenced its subcellular distribution.
17507370	10	14	theme	complex	1852:1858	arg1	interplay					1860:1868	the complex interplay	1848:1868	the complex interplay between phosphorylation and O-GlcNAcylation that occurs within signaling networks	1848:1950	Taken together, these data indicated the complex interplay between phosphorylation and O-GlcNAcylation that occurs within signaling networks.
17507370	8	15	theme	O-GlcNAc	1455:1462	arg1	Ser-55					1470:1475	Ser-55	1470:1475	Ser-55	1470:1475	By combining a new O-GlcNAc peptide enrichment method and beta-elimination followed by Michael addition with DTT, we also mapped the O-GlcNAc site (Ser-55) of vimentin, which showed an apparent increase of O-GlcNAcylation upon GSK-3 inhibition.
17507370	8	15	theme	O-GlcNAc	1455:1462	arg1	vimentin					1481:1488	vimentin	1481:1488	vimentin	1481:1488	By combining a new O-GlcNAc peptide enrichment method and beta-elimination followed by Michael addition with DTT, we also mapped the O-GlcNAc site (Ser-55) of vimentin, which showed an apparent increase of O-GlcNAcylation upon GSK-3 inhibition.
17507370	8	15	theme	O-GlcNAc	1455:1462	arg1	site					1464:1467	the O-GlcNAc site	1451:1467	the O-GlcNAc site (Ser-55)	1451:1476	By combining a new O-GlcNAc peptide enrichment method and beta-elimination followed by Michael addition with DTT, we also mapped the O-GlcNAc site (Ser-55) of vimentin, which showed an apparent increase of O-GlcNAcylation upon GSK-3 inhibition.
17507370	1	16	theme	nuclear	174:180	arg1	proteins					198:205	nuclear and cytoplasmic proteins	174:205	nuclear and cytoplasmic proteins	174:205	O-GlcNAcylation on serine and threonine side chains of nuclear and cytoplasmic proteins is dynamically regulated in response to various environmental and biological stimuli.
17507370	0	17	theme	kinase-3-dependent	83:100	arg1	phosphorylation					102:116	kinase-3-dependent phosphorylation	83:116	kinase-3-dependent phosphorylation	83:116	Dynamic interplay between O-linked N-acetylglucosaminylation and glycogen synthase kinase-3-dependent phosphorylation.
17507370	5	18	theme	O-GlcNAcylated	1007:1020	arg1	proteins					1022:1029	45 potentially O-GlcNAcylated proteins	992:1029	45 potentially O-GlcNAcylated proteins	992:1029	By combining immunoaffinity chromatography and SILAC (stable isotope labeling with amino acids in cell culture)-based quantitative mass spectrometry, we identified 45 potentially O-GlcNAcylated proteins.
17507370	4	19	theme	many	803:806	arg1	pathways					818:825	many signaling pathways	803:825	many signaling pathways	803:825	Here we report the O-GlcNAc perturbations in response to inhibition of glycogen synthase kinase-3 (GSK-3), a pivotal kinase involved in many signaling pathways.
17507370	5	20	theme	isotope	889:895	arg1	labeling					897:904	stable isotope labeling	882:904	stable isotope labeling with amino acids in cell culture	882:937	By combining immunoaffinity chromatography and SILAC (stable isotope labeling with amino acids in cell culture)-based quantitative mass spectrometry, we identified 45 potentially O-GlcNAcylated proteins.
17507370	8	21	theme	vimentin	1481:1488	arg1	Ser-55					1470:1475	Ser-55	1470:1475	Ser-55	1470:1475	By combining a new O-GlcNAc peptide enrichment method and beta-elimination followed by Michael addition with DTT, we also mapped the O-GlcNAc site (Ser-55) of vimentin, which showed an apparent increase of O-GlcNAcylation upon GSK-3 inhibition.
17507370	8	21	theme	vimentin	1481:1488	arg1	vimentin					1481:1488	vimentin	1481:1488	vimentin	1481:1488	By combining a new O-GlcNAc peptide enrichment method and beta-elimination followed by Michael addition with DTT, we also mapped the O-GlcNAc site (Ser-55) of vimentin, which showed an apparent increase of O-GlcNAcylation upon GSK-3 inhibition.
17507370	8	21	theme	vimentin	1481:1488	arg1	site					1464:1467	the O-GlcNAc site	1451:1467	the O-GlcNAc site (Ser-55)	1451:1476	By combining a new O-GlcNAc peptide enrichment method and beta-elimination followed by Michael addition with DTT, we also mapped the O-GlcNAc site (Ser-55) of vimentin, which showed an apparent increase of O-GlcNAcylation upon GSK-3 inhibition.
17507370	5	22	theme	immunoaffinity	841:854	arg1	chromatography					856:869	immunoaffinity chromatography	841:869	immunoaffinity chromatography	841:869	By combining immunoaffinity chromatography and SILAC (stable isotope labeling with amino acids in cell culture)-based quantitative mass spectrometry, we identified 45 potentially O-GlcNAcylated proteins.
17507370	9	23	theme	transcription	1666:1678	arg1	co-activator					1680:1691	a transcription co-activator	1664:1691	a transcription co-activator	1664:1691	Based on the MS data, we further investigated potential roles of O-GlcNAc on host cell factor-1, a transcription co-activator, and showed that dynamic regulation of O-GlcNAcylation on host cell factor-1 influenced its subcellular distribution.
17507370	9	23	theme	transcription	1666:1678	arg1	factor-1					1654:1661	host cell factor-1	1644:1661	host cell factor-1	1644:1661	Based on the MS data, we further investigated potential roles of O-GlcNAc on host cell factor-1, a transcription co-activator, and showed that dynamic regulation of O-GlcNAcylation on host cell factor-1 influenced its subcellular distribution.
17507370	0	24	theme	Dynamic	0:6	arg1	interplay					8:16	Dynamic interplay	0:16	Dynamic interplay between O-linked N-acetylglucosaminylation and glycogen synthase kinase-3-dependent phosphorylation.	0:117	Dynamic interplay between O-linked N-acetylglucosaminylation and glycogen synthase kinase-3-dependent phosphorylation.
17507370	3	25	theme	glycoproteomics	446:460	arg1	analysis					462:469	A systematic glycoproteomics analysis	433:469	A systematic glycoproteomics analysis of the affects of inhibiting specific kinases on O-GlcNAcylation	433:534	A systematic glycoproteomics analysis of the affects of inhibiting specific kinases on O-GlcNAcylation should help reveal both the global and specific dynamic relationships between these two abundant post-translational modifications.
17507370	7	26	from	changes	1245:1251	arg1	subset					1258:1263	a subset	1256:1263	a subset of the proteins	1256:1279	O-GlcNAcylation changes on a subset of the proteins were confirmed by follow-up experiments.
17507370	6	27	contain	had	1094:1096	arg2	increase					1110:1117	an apparent increase	1098:1117	an apparent increase of O-GlcNAcylation	1098:1136	Quantitative measurements indicated that at least 10 proteins had an apparent increase of O-GlcNAcylation upon GSK-3 inhibition by lithium, whereas surprisingly 19 other proteins showed decreases.
17507370	6	27	contain	had	1094:1096	arg1	proteins					1085:1092	at least 10 proteins	1073:1092	at least 10 proteins	1073:1092	Quantitative measurements indicated that at least 10 proteins had an apparent increase of O-GlcNAcylation upon GSK-3 inhibition by lithium, whereas surprisingly 19 other proteins showed decreases.
17507370	9	28	theme	dynamic	1710:1716	arg1	regulation					1718:1727	dynamic regulation	1710:1727	dynamic regulation of O-GlcNAcylation on host cell factor-1	1710:1768	Based on the MS data, we further investigated potential roles of O-GlcNAc on host cell factor-1, a transcription co-activator, and showed that dynamic regulation of O-GlcNAcylation on host cell factor-1 influenced its subcellular distribution.
17507370	9	29	from	regulation	1718:1727	arg1	factor-1					1761:1768	host cell factor-1	1751:1768	host cell factor-1	1751:1768	Based on the MS data, we further investigated potential roles of O-GlcNAc on host cell factor-1, a transcription co-activator, and showed that dynamic regulation of O-GlcNAcylation on host cell factor-1 influenced its subcellular distribution.
17507370	8	30	theme	O-GlcNAcylation	1528:1542	arg1	increase					1516:1523	an apparent increase	1504:1523	an apparent increase of O-GlcNAcylation	1504:1542	By combining a new O-GlcNAc peptide enrichment method and beta-elimination followed by Michael addition with DTT, we also mapped the O-GlcNAc site (Ser-55) of vimentin, which showed an apparent increase of O-GlcNAcylation upon GSK-3 inhibition.
17507370	7	31	theme	follow-up	1299:1307	arg1	experiments					1309:1319	follow-up experiments	1299:1319	follow-up experiments	1299:1319	O-GlcNAcylation changes on a subset of the proteins were confirmed by follow-up experiments.
17507370	2	32	contain	have	367:370	arg2	interplay					382:390	a dynamic interplay	372:390	a dynamic interplay with O-phosphate	372:407	O-GlcNAcylation is remarkably similar to O-phosphorylation and appears to have a dynamic interplay with O-phosphate in cellular regulation.
17507370	2	32	contain	have	367:370	arg1	O-GlcNAcylation					293:307	O-GlcNAcylation	293:307	O-GlcNAcylation	293:307	O-GlcNAcylation is remarkably similar to O-phosphorylation and appears to have a dynamic interplay with O-phosphate in cellular regulation.
17507370	8	33	theme	GSK-3	1549:1553	arg1	inhibition					1555:1564	GSK-3 inhibition	1549:1564	GSK-3 inhibition	1549:1564	By combining a new O-GlcNAc peptide enrichment method and beta-elimination followed by Michael addition with DTT, we also mapped the O-GlcNAc site (Ser-55) of vimentin, which showed an apparent increase of O-GlcNAcylation upon GSK-3 inhibition.
17507370	3	34	theme	specific	575:582	arg1	relationships					592:604	both the global and specific dynamic relationships	555:604	relationships	592:604	A systematic glycoproteomics analysis of the affects of inhibiting specific kinases on O-GlcNAcylation should help reveal both the global and specific dynamic relationships between these two abundant post-translational modifications.
17507370	0	35	theme	glycogen	65:72	arg1	synthase					74:81	glycogen synthase	65:81	glycogen synthase	65:81	Dynamic interplay between O-linked N-acetylglucosaminylation and glycogen synthase kinase-3-dependent phosphorylation.
17507370	0	36	dep	N-acetylglucosaminylation	35:59	arg1	phosphorylation					102:116	kinase-3-dependent phosphorylation	83:116	kinase-3-dependent phosphorylation	83:116	Dynamic interplay between O-linked N-acetylglucosaminylation and glycogen synthase kinase-3-dependent phosphorylation.
17507370	3	37	theme	global	564:569	arg1	relationships					592:604	both the global and specific dynamic relationships	555:604	relationships	592:604	A systematic glycoproteomics analysis of the affects of inhibiting specific kinases on O-GlcNAcylation should help reveal both the global and specific dynamic relationships between these two abundant post-translational modifications.
17507370	1	38	theme	biological	273:282	arg1	stimuli					284:290	various environmental and biological stimuli	247:290	various environmental and biological stimuli	247:290	O-GlcNAcylation on serine and threonine side chains of nuclear and cytoplasmic proteins is dynamically regulated in response to various environmental and biological stimuli.
17507370	3	39	theme	post-translational	633:650	arg1	modifications					652:664	these two abundant post-translational modifications	614:664	these two abundant post-translational modifications	614:664	A systematic glycoproteomics analysis of the affects of inhibiting specific kinases on O-GlcNAcylation should help reveal both the global and specific dynamic relationships between these two abundant post-translational modifications.
17507370	9	40	theme	cell	1756:1759	arg1	factor-1					1761:1768	host cell factor-1	1751:1768	host cell factor-1	1751:1768	Based on the MS data, we further investigated potential roles of O-GlcNAc on host cell factor-1, a transcription co-activator, and showed that dynamic regulation of O-GlcNAcylation on host cell factor-1 influenced its subcellular distribution.
17507370	9	41	theme	cell	1649:1652	arg1	co-activator					1680:1691	a transcription co-activator	1664:1691	a transcription co-activator	1664:1691	Based on the MS data, we further investigated potential roles of O-GlcNAc on host cell factor-1, a transcription co-activator, and showed that dynamic regulation of O-GlcNAcylation on host cell factor-1 influenced its subcellular distribution.
17507370	9	41	theme	cell	1649:1652	arg1	factor-1					1654:1661	host cell factor-1	1644:1661	host cell factor-1	1644:1661	Based on the MS data, we further investigated potential roles of O-GlcNAc on host cell factor-1, a transcription co-activator, and showed that dynamic regulation of O-GlcNAcylation on host cell factor-1 influenced its subcellular distribution.
17507370	5	42	dep	-based	939:944	arg1	labeling					897:904	stable isotope labeling	882:904	stable isotope labeling with amino acids in cell culture	882:937	By combining immunoaffinity chromatography and SILAC (stable isotope labeling with amino acids in cell culture)-based quantitative mass spectrometry, we identified 45 potentially O-GlcNAcylated proteins.
17507370	5	43	theme	stable	882:887	arg1	labeling					897:904	stable isotope labeling	882:904	stable isotope labeling with amino acids in cell culture	882:937	By combining immunoaffinity chromatography and SILAC (stable isotope labeling with amino acids in cell culture)-based quantitative mass spectrometry, we identified 45 potentially O-GlcNAcylated proteins.
17507370	1	44	from	O-GlcNAcylation	119:133	arg1	serine					138:143	serine	138:143	serine	138:143	O-GlcNAcylation on serine and threonine side chains of nuclear and cytoplasmic proteins is dynamically regulated in response to various environmental and biological stimuli.
17507370	1	44	from	O-GlcNAcylation	119:133	arg1	threonine					149:157	threonine	149:157	threonine	149:157	O-GlcNAcylation on serine and threonine side chains of nuclear and cytoplasmic proteins is dynamically regulated in response to various environmental and biological stimuli.
17507370	9	45	theme	subcellular	1785:1795	arg1	distribution					1797:1808	its subcellular distribution	1781:1808	its subcellular distribution	1781:1808	Based on the MS data, we further investigated potential roles of O-GlcNAc on host cell factor-1, a transcription co-activator, and showed that dynamic regulation of O-GlcNAcylation on host cell factor-1 influenced its subcellular distribution.
17507370	0	46	link	O-linked	26:33	arg1	N-acetylglucosaminylation					35:59	O-linked N-acetylglucosaminylation	26:59	O-linked N-acetylglucosaminylation	26:59	Dynamic interplay between O-linked N-acetylglucosaminylation and glycogen synthase kinase-3-dependent phosphorylation.
17507370	4	47	theme	O-GlcNAc	686:693	arg1	perturbations					695:707	the O-GlcNAc perturbations	682:707	the O-GlcNAc perturbations in response to inhibition of glycogen synthase kinase-3 (GSK-3), a pivotal kinase involved in many signaling pathways	682:825	Here we report the O-GlcNAc perturbations in response to inhibition of glycogen synthase kinase-3 (GSK-3), a pivotal kinase involved in many signaling pathways.
17507370	2	48	theme	cellular	412:419	arg1	regulation					421:430	cellular regulation	412:430	cellular regulation	412:430	O-GlcNAcylation is remarkably similar to O-phosphorylation and appears to have a dynamic interplay with O-phosphate in cellular regulation.
17507370	3	49	theme	abundant	624:631	arg1	modifications					652:664	these two abundant post-translational modifications	614:664	these two abundant post-translational modifications	614:664	A systematic glycoproteomics analysis of the affects of inhibiting specific kinases on O-GlcNAcylation should help reveal both the global and specific dynamic relationships between these two abundant post-translational modifications.
17507370	7	50	theme	O-GlcNAcylation	1229:1243	arg1	changes					1245:1251	O-GlcNAcylation changes	1229:1251	O-GlcNAcylation changes on a subset of the proteins	1229:1279	O-GlcNAcylation changes on a subset of the proteins were confirmed by follow-up experiments.
17507370	9	51	from	roles	1623:1627	arg1	co-activator					1680:1691	a transcription co-activator	1664:1691	a transcription co-activator	1664:1691	Based on the MS data, we further investigated potential roles of O-GlcNAc on host cell factor-1, a transcription co-activator, and showed that dynamic regulation of O-GlcNAcylation on host cell factor-1 influenced its subcellular distribution.
17507370	9	51	from	roles	1623:1627	arg1	factor-1					1654:1661	host cell factor-1	1644:1661	host cell factor-1	1644:1661	Based on the MS data, we further investigated potential roles of O-GlcNAc on host cell factor-1, a transcription co-activator, and showed that dynamic regulation of O-GlcNAcylation on host cell factor-1 influenced its subcellular distribution.
17507370	8	52	theme	Michael	1409:1415	arg1	addition					1417:1424	Michael addition	1409:1424	Michael addition with DTT	1409:1433	By combining a new O-GlcNAc peptide enrichment method and beta-elimination followed by Michael addition with DTT, we also mapped the O-GlcNAc site (Ser-55) of vimentin, which showed an apparent increase of O-GlcNAcylation upon GSK-3 inhibition.
17507370	5	53	theme	-based	939:944	arg1	spectrometry					964:975	SILAC (stable isotope labeling with amino acids in cell culture)-based quantitative mass spectrometry	875:975	SILAC (stable isotope labeling with amino acids in cell culture)-based quantitative mass spectrometry	875:975	By combining immunoaffinity chromatography and SILAC (stable isotope labeling with amino acids in cell culture)-based quantitative mass spectrometry, we identified 45 potentially O-GlcNAcylated proteins.
17507370	8	54	theme	O-GlcNAc	1341:1348	arg1	method					1369:1374	a new O-GlcNAc peptide enrichment method	1335:1374	a new O-GlcNAc peptide enrichment method	1335:1374	By combining a new O-GlcNAc peptide enrichment method and beta-elimination followed by Michael addition with DTT, we also mapped the O-GlcNAc site (Ser-55) of vimentin, which showed an apparent increase of O-GlcNAcylation upon GSK-3 inhibition.
17507370	4	55	theme	synthase	747:754	arg1	kinase					784:789	a pivotal kinase	774:789	a pivotal kinase involved in many signaling pathways	774:825	Here we report the O-GlcNAc perturbations in response to inhibition of glycogen synthase kinase-3 (GSK-3), a pivotal kinase involved in many signaling pathways.
17507370	4	55	theme	synthase	747:754	arg1	GSK-3					766:770	GSK-3	766:770	GSK-3	766:770	Here we report the O-GlcNAc perturbations in response to inhibition of glycogen synthase kinase-3 (GSK-3), a pivotal kinase involved in many signaling pathways.
17507370	4	55	theme	synthase	747:754	arg1	kinase-3					756:763	glycogen synthase kinase-3	738:763	glycogen synthase kinase-3 (GSK-3)	738:771	Here we report the O-GlcNAc perturbations in response to inhibition of glycogen synthase kinase-3 (GSK-3), a pivotal kinase involved in many signaling pathways.
17507370	5	56	theme	mass	959:962	arg1	spectrometry					964:975	SILAC (stable isotope labeling with amino acids in cell culture)-based quantitative mass spectrometry	875:975	SILAC (stable isotope labeling with amino acids in cell culture)-based quantitative mass spectrometry	875:975	By combining immunoaffinity chromatography and SILAC (stable isotope labeling with amino acids in cell culture)-based quantitative mass spectrometry, we identified 45 potentially O-GlcNAcylated proteins.
17507370	8	57	theme	enrichment	1358:1367	arg1	method					1369:1374	a new O-GlcNAc peptide enrichment method	1335:1374	a new O-GlcNAc peptide enrichment method	1335:1374	By combining a new O-GlcNAc peptide enrichment method and beta-elimination followed by Michael addition with DTT, we also mapped the O-GlcNAc site (Ser-55) of vimentin, which showed an apparent increase of O-GlcNAcylation upon GSK-3 inhibition.
17507370	1	58	theme	side	159:162	arg1	chains					164:169	side chains	159:169	side chains	159:169	O-GlcNAcylation on serine and threonine side chains of nuclear and cytoplasmic proteins is dynamically regulated in response to various environmental and biological stimuli.
17507370	4	59	theme	signaling	808:816	arg1	pathways					818:825	many signaling pathways	803:825	many signaling pathways	803:825	Here we report the O-GlcNAc perturbations in response to inhibition of glycogen synthase kinase-3 (GSK-3), a pivotal kinase involved in many signaling pathways.
17507370	9	60	theme	O-GlcNAc	1632:1639	arg1	roles					1623:1627	potential roles	1613:1627	potential roles of O-GlcNAc on host cell factor-1, a transcription co-activator,	1613:1692	Based on the MS data, we further investigated potential roles of O-GlcNAc on host cell factor-1, a transcription co-activator, and showed that dynamic regulation of O-GlcNAcylation on host cell factor-1 influenced its subcellular distribution.
17507370	9	61	theme	host	1644:1647	arg1	co-activator					1680:1691	a transcription co-activator	1664:1691	a transcription co-activator	1664:1691	Based on the MS data, we further investigated potential roles of O-GlcNAc on host cell factor-1, a transcription co-activator, and showed that dynamic regulation of O-GlcNAcylation on host cell factor-1 influenced its subcellular distribution.
17507370	9	61	theme	host	1644:1647	arg1	factor-1					1654:1661	host cell factor-1	1644:1661	host cell factor-1	1644:1661	Based on the MS data, we further investigated potential roles of O-GlcNAc on host cell factor-1, a transcription co-activator, and showed that dynamic regulation of O-GlcNAcylation on host cell factor-1 influenced its subcellular distribution.
17507370	6	62	theme	O-GlcNAcylation	1122:1136	arg1	increase					1110:1117	an apparent increase	1098:1117	an apparent increase of O-GlcNAcylation	1098:1136	Quantitative measurements indicated that at least 10 proteins had an apparent increase of O-GlcNAcylation upon GSK-3 inhibition by lithium, whereas surprisingly 19 other proteins showed decreases.
17507370	1	63	gly	O-GlcNAcylation	119:133	arg1	response					235:242	response	235:242	response to various environmental and biological stimuli	235:290	O-GlcNAcylation on serine and threonine side chains of nuclear and cytoplasmic proteins is dynamically regulated in response to various environmental and biological stimuli.
17507370	5	64	from	acids	917:921	arg1	culture					931:937	cell culture	926:937	cell culture	926:937	By combining immunoaffinity chromatography and SILAC (stable isotope labeling with amino acids in cell culture)-based quantitative mass spectrometry, we identified 45 potentially O-GlcNAcylated proteins.
17507370	1	65	theme	proteins	198:205	arg1	serine					138:143	serine	138:143	serine	138:143	O-GlcNAcylation on serine and threonine side chains of nuclear and cytoplasmic proteins is dynamically regulated in response to various environmental and biological stimuli.
17507370	1	65	theme	proteins	198:205	arg1	threonine					149:157	threonine	149:157	threonine	149:157	O-GlcNAcylation on serine and threonine side chains of nuclear and cytoplasmic proteins is dynamically regulated in response to various environmental and biological stimuli.
17507370	6	66	theme	GSK-3	1143:1147	arg1	inhibition					1149:1158	GSK-3 inhibition	1143:1158	GSK-3 inhibition by lithium	1143:1169	Quantitative measurements indicated that at least 10 proteins had an apparent increase of O-GlcNAcylation upon GSK-3 inhibition by lithium, whereas surprisingly 19 other proteins showed decreases.
17507370	1	67	dep	serine	138:143	arg1	chains					164:169	side chains	159:169	side chains	159:169	O-GlcNAcylation on serine and threonine side chains of nuclear and cytoplasmic proteins is dynamically regulated in response to various environmental and biological stimuli.
17507370	2	68	with	interplay	382:390	arg1	O-phosphate					397:407	O-phosphate	397:407	O-phosphate	397:407	O-GlcNAcylation is remarkably similar to O-phosphorylation and appears to have a dynamic interplay with O-phosphate in cellular regulation.
17507370	3	69	theme	systematic	435:444	arg1	analysis					462:469	A systematic glycoproteomics analysis	433:469	A systematic glycoproteomics analysis of the affects of inhibiting specific kinases on O-GlcNAcylation	433:534	A systematic glycoproteomics analysis of the affects of inhibiting specific kinases on O-GlcNAcylation should help reveal both the global and specific dynamic relationships between these two abundant post-translational modifications.
17507370	3	70	dep	the	474:476	arg1	affects					478:484	affects	478:484	affects	478:484	A systematic glycoproteomics analysis of the affects of inhibiting specific kinases on O-GlcNAcylation should help reveal both the global and specific dynamic relationships between these two abundant post-translational modifications.
17507370	4	71	from	perturbations	695:707	arg1	response					712:719	response	712:719	response to inhibition of glycogen synthase kinase-3 (GSK-3), a pivotal kinase involved in many signaling pathways	712:825	Here we report the O-GlcNAc perturbations in response to inhibition of glycogen synthase kinase-3 (GSK-3), a pivotal kinase involved in many signaling pathways.
17507370	1	72	theme	various	247:253	arg1	stimuli					284:290	various environmental and biological stimuli	247:290	various environmental and biological stimuli	247:290	O-GlcNAcylation on serine and threonine side chains of nuclear and cytoplasmic proteins is dynamically regulated in response to various environmental and biological stimuli.
17507370	3	73	dep	relationships	592:604	arg1	both					555:558	both	555:558	both	555:558	A systematic glycoproteomics analysis of the affects of inhibiting specific kinases on O-GlcNAcylation should help reveal both the global and specific dynamic relationships between these two abundant post-translational modifications.
17507370	3	74	theme	the	474:476	arg1	analysis					462:469	A systematic glycoproteomics analysis	433:469	A systematic glycoproteomics analysis of the affects of inhibiting specific kinases on O-GlcNAcylation	433:534	A systematic glycoproteomics analysis of the affects of inhibiting specific kinases on O-GlcNAcylation should help reveal both the global and specific dynamic relationships between these two abundant post-translational modifications.
17507370	0	75	theme	O-linked	26:33	arg1	N-acetylglucosaminylation					35:59	O-linked N-acetylglucosaminylation	26:59	O-linked N-acetylglucosaminylation	26:59	Dynamic interplay between O-linked N-acetylglucosaminylation and glycogen synthase kinase-3-dependent phosphorylation.
17507370	6	76	theme	other	1196:1200	arg1	proteins					1202:1209	surprisingly 19 other proteins	1180:1209	surprisingly 19 other proteins	1180:1209	Quantitative measurements indicated that at least 10 proteins had an apparent increase of O-GlcNAcylation upon GSK-3 inhibition by lithium, whereas surprisingly 19 other proteins showed decreases.
17507370	8	77	theme	apparent	1507:1514	arg1	increase					1516:1523	an apparent increase	1504:1523	an apparent increase of O-GlcNAcylation	1504:1542	By combining a new O-GlcNAc peptide enrichment method and beta-elimination followed by Michael addition with DTT, we also mapped the O-GlcNAc site (Ser-55) of vimentin, which showed an apparent increase of O-GlcNAcylation upon GSK-3 inhibition.
17507370	1	78	theme	environmental	255:267	arg1	stimuli					284:290	various environmental and biological stimuli	247:290	various environmental and biological stimuli	247:290	O-GlcNAcylation on serine and threonine side chains of nuclear and cytoplasmic proteins is dynamically regulated in response to various environmental and biological stimuli.
17507370	3	79	theme	specific	500:507	arg1	kinases					509:515	specific kinases	500:515	specific kinases on O-GlcNAcylation	500:534	A systematic glycoproteomics analysis of the affects of inhibiting specific kinases on O-GlcNAcylation should help reveal both the global and specific dynamic relationships between these two abundant post-translational modifications.
17507370	5	80	theme	amino	911:915	arg1	acids					917:921	amino acids	911:921	amino acids in cell culture	911:937	By combining immunoaffinity chromatography and SILAC (stable isotope labeling with amino acids in cell culture)-based quantitative mass spectrometry, we identified 45 potentially O-GlcNAcylated proteins.
17507370	9	81	theme	O-GlcNAcylation	1732:1746	arg1	regulation					1718:1727	dynamic regulation	1710:1727	dynamic regulation of O-GlcNAcylation on host cell factor-1	1710:1768	Based on the MS data, we further investigated potential roles of O-GlcNAc on host cell factor-1, a transcription co-activator, and showed that dynamic regulation of O-GlcNAcylation on host cell factor-1 influenced its subcellular distribution.
17507370	1	82	theme	cytoplasmic	186:196	arg1	proteins					198:205	nuclear and cytoplasmic proteins	174:205	nuclear and cytoplasmic proteins	174:205	O-GlcNAcylation on serine and threonine side chains of nuclear and cytoplasmic proteins is dynamically regulated in response to various environmental and biological stimuli.
17507370	3	83	theme	dynamic	584:590	arg1	relationships					592:604	both the global and specific dynamic relationships	555:604	relationships	592:604	A systematic glycoproteomics analysis of the affects of inhibiting specific kinases on O-GlcNAcylation should help reveal both the global and specific dynamic relationships between these two abundant post-translational modifications.
17507370	9	84	theme	host	1751:1754	arg1	factor-1					1761:1768	host cell factor-1	1751:1768	host cell factor-1	1751:1768	Based on the MS data, we further investigated potential roles of O-GlcNAc on host cell factor-1, a transcription co-activator, and showed that dynamic regulation of O-GlcNAcylation on host cell factor-1 influenced its subcellular distribution.
17507370	3	85	from	kinases	509:515	arg1	O-GlcNAcylation					520:534	O-GlcNAcylation	520:534	O-GlcNAcylation	520:534	A systematic glycoproteomics analysis of the affects of inhibiting specific kinases on O-GlcNAcylation should help reveal both the global and specific dynamic relationships between these two abundant post-translational modifications.
17507370	4	86	theme	glycogen	738:745	arg1	kinase					784:789	a pivotal kinase	774:789	a pivotal kinase involved in many signaling pathways	774:825	Here we report the O-GlcNAc perturbations in response to inhibition of glycogen synthase kinase-3 (GSK-3), a pivotal kinase involved in many signaling pathways.
17507370	4	86	theme	glycogen	738:745	arg1	GSK-3					766:770	GSK-3	766:770	GSK-3	766:770	Here we report the O-GlcNAc perturbations in response to inhibition of glycogen synthase kinase-3 (GSK-3), a pivotal kinase involved in many signaling pathways.
17507370	4	86	theme	glycogen	738:745	arg1	kinase-3					756:763	glycogen synthase kinase-3	738:763	glycogen synthase kinase-3 (GSK-3)	738:771	Here we report the O-GlcNAc perturbations in response to inhibition of glycogen synthase kinase-3 (GSK-3), a pivotal kinase involved in many signaling pathways.
17507370	8	87	with	addition	1417:1424	arg1	DTT					1431:1433	DTT	1431:1433	DTT	1431:1433	By combining a new O-GlcNAc peptide enrichment method and beta-elimination followed by Michael addition with DTT, we also mapped the O-GlcNAc site (Ser-55) of vimentin, which showed an apparent increase of O-GlcNAcylation upon GSK-3 inhibition.
34546745	7	0	theme	molecular	1214:1222	arg1	consequences					1224:1235	the molecular consequences	1210:1235	the molecular consequences of O-GlcNAc	1210:1247	Our results expand our understanding of the molecular consequences of O-GlcNAc and how it affects protein-DNA interfaces.
34546745	5	1	theme	cruciform	883:891	arg1	DNA					931:933	linear, nucleosomal, supercoiled, cruciform, and interstrand cross-linked damaged DNA	849:933	linear, nucleosomal, supercoiled, cruciform, and interstrand cross-linked damaged DNA	849:933	We found that O-GlcNAc alters HMGB1 binding to linear, nucleosomal, supercoiled, cruciform, and interstrand cross-linked damaged DNA, generally resulting in enhanced oligomerization on these DNA structures.
34546745	2	2	theme	potential	351:359	arg1	link					361:364	a potential link	349:364	a potential link between this modification and DNA damage responses	349:415	Proteomic studies have identified the multifunctional nuclear protein HMGB1 as O-GlcNAcylated, providing a potential link between this modification and DNA damage responses.
34546745	8	3	from	rates	1388:1392	arg1	states					1425:1430	certain cancer states	1410:1430	certain cancer states	1410:1430	Importantly, our work may also support a link between upregulated O-GlcNAc levels and increased rates of mutations in certain cancer states.
34546745	6	4	theme	cell-free	1015:1023	arg1	extracts					1025:1032	cell-free extracts	1015:1032	cell-free extracts	1015:1032	Using cell-free extracts, we also found that O-GlcNAc reduces the ability of HMGB1 to facilitate DNA repair, resulting in error-prone processing of damaged DNA.
34546745	5	5	theme	enhanced	959:966	arg1	oligomerization					968:982	enhanced oligomerization	959:982	enhanced oligomerization on these DNA structures	959:1006	We found that O-GlcNAc alters HMGB1 binding to linear, nucleosomal, supercoiled, cruciform, and interstrand cross-linked damaged DNA, generally resulting in enhanced oligomerization on these DNA structures.
34546745	5	6	theme	interstrand	898:908	arg1	DNA					931:933	linear, nucleosomal, supercoiled, cruciform, and interstrand cross-linked damaged DNA	849:933	linear, nucleosomal, supercoiled, cruciform, and interstrand cross-linked damaged DNA	849:933	We found that O-GlcNAc alters HMGB1 binding to linear, nucleosomal, supercoiled, cruciform, and interstrand cross-linked damaged DNA, generally resulting in enhanced oligomerization on these DNA structures.
34546745	5	7	from	oligomerization	968:982	arg1	structures					997:1006	these DNA structures	987:1006	these DNA structures	987:1006	We found that O-GlcNAc alters HMGB1 binding to linear, nucleosomal, supercoiled, cruciform, and interstrand cross-linked damaged DNA, generally resulting in enhanced oligomerization on these DNA structures.
34546745	5	8	theme	DNA	993:995	arg1	structures					997:1006	these DNA structures	987:1006	these DNA structures	987:1006	We found that O-GlcNAc alters HMGB1 binding to linear, nucleosomal, supercoiled, cruciform, and interstrand cross-linked damaged DNA, generally resulting in enhanced oligomerization on these DNA structures.
34546745	8	9	from	levels	1367:1372	arg1	states					1425:1430	certain cancer states	1410:1430	certain cancer states	1410:1430	Importantly, our work may also support a link between upregulated O-GlcNAc levels and increased rates of mutations in certain cancer states.
34546745	8	10	theme	upregulated	1346:1356	arg1	levels					1367:1372	upregulated O-GlcNAc levels	1346:1372	upregulated O-GlcNAc levels	1346:1372	Importantly, our work may also support a link between upregulated O-GlcNAc levels and increased rates of mutations in certain cancer states.
34546745	4	11	theme	sugar	754:758	arg1	modification					760:771	the sugar modification	750:771	the sugar modification	750:771	Using synthetic protein chemistry, we generated site-specifically O-GlcNAc-modified HMGB1 at S100 and characterized biochemically the effect of the sugar modification on its DNA binding activity.
34546745	0	12	theme	DNA	64:66	arg1	Binding					68:74	Its DNA Binding	60:74	Its DNA Binding	60:74	O-GlcNAcylation of High Mobility Group Box 1 (HMGB1) Alters Its DNA Binding and DNA Damage Processing Activities.
34546745	6	13	theme	damaged	1157:1163	arg1	DNA					1165:1167	damaged DNA	1157:1167	damaged DNA	1157:1167	Using cell-free extracts, we also found that O-GlcNAc reduces the ability of HMGB1 to facilitate DNA repair, resulting in error-prone processing of damaged DNA.
34546745	7	14	dep	expand	1182:1187	arg1	affects					1260:1266	affects	1260:1266	affects protein-DNA interfaces	1260:1289	Our results expand our understanding of the molecular consequences of O-GlcNAc and how it affects protein-DNA interfaces.
34546745	5	15	theme	nucleosomal	857:867	arg1	DNA					931:933	linear, nucleosomal, supercoiled, cruciform, and interstrand cross-linked damaged DNA	849:933	linear, nucleosomal, supercoiled, cruciform, and interstrand cross-linked damaged DNA	849:933	We found that O-GlcNAc alters HMGB1 binding to linear, nucleosomal, supercoiled, cruciform, and interstrand cross-linked damaged DNA, generally resulting in enhanced oligomerization on these DNA structures.
34546745	0	16	theme	DNA	80:82	arg1	Activities					102:111	DNA Damage Processing Activities	80:111	DNA Damage Processing Activities	80:111	O-GlcNAcylation of High Mobility Group Box 1 (HMGB1) Alters Its DNA Binding and DNA Damage Processing Activities.
34546745	6	17	theme	error-prone	1131:1141	arg1	processing					1143:1152	error-prone processing	1131:1152	error-prone processing of damaged DNA	1131:1167	Using cell-free extracts, we also found that O-GlcNAc reduces the ability of HMGB1 to facilitate DNA repair, resulting in error-prone processing of damaged DNA.
34546745	4	18	theme	synthetic	612:620	arg1	chemistry					630:638	synthetic protein chemistry	612:638	synthetic protein chemistry	612:638	Using synthetic protein chemistry, we generated site-specifically O-GlcNAc-modified HMGB1 at S100 and characterized biochemically the effect of the sugar modification on its DNA binding activity.
34546745	3	19	theme	major	508:512	arg1	site					527:530	the major modification site	504:530	the major modification site	504:530	Here, we verify the protein's endogenous modification at S100 and S107 and found that the major modification site is S100, a residue that can potentially influence HMGB1-DNA interactions.
34546745	3	19	theme	major	508:512	arg1	S100					535:538	S100	535:538	S100	535:538	Here, we verify the protein's endogenous modification at S100 and S107 and found that the major modification site is S100, a residue that can potentially influence HMGB1-DNA interactions.
34546745	4	20	theme	O-GlcNAc-modified	672:688	arg1	HMGB1					690:694	site-specifically O-GlcNAc-modified HMGB1	654:694	site-specifically O-GlcNAc-modified HMGB1	654:694	Using synthetic protein chemistry, we generated site-specifically O-GlcNAc-modified HMGB1 at S100 and characterized biochemically the effect of the sugar modification on its DNA binding activity.
34546745	1	21	theme	essential	144:152	arg1	O-GlcNAcylation					122:136	Protein O-GlcNAcylation	114:136	Protein O-GlcNAcylation	114:136	Protein O-GlcNAcylation is an essential and dynamic regulator of myriad cellular processes, including DNA replication and repair.
34546745	1	21	theme	essential	144:152	arg1	regulator					166:174	an essential and dynamic regulator	141:174	an essential and dynamic regulator of myriad cellular processes, including DNA replication and repair	141:241	Protein O-GlcNAcylation is an essential and dynamic regulator of myriad cellular processes, including DNA replication and repair.
34546745	8	22	theme	O-GlcNAc	1358:1365	arg1	levels					1367:1372	upregulated O-GlcNAc levels	1346:1372	upregulated O-GlcNAc levels	1346:1372	Importantly, our work may also support a link between upregulated O-GlcNAc levels and increased rates of mutations in certain cancer states.
34546745	3	23	theme	modification	514:525	arg1	site					527:530	the major modification site	504:530	the major modification site	504:530	Here, we verify the protein's endogenous modification at S100 and S107 and found that the major modification site is S100, a residue that can potentially influence HMGB1-DNA interactions.
34546745	3	23	theme	modification	514:525	arg1	S100					535:538	S100	535:538	S100	535:538	Here, we verify the protein's endogenous modification at S100 and S107 and found that the major modification site is S100, a residue that can potentially influence HMGB1-DNA interactions.
34546745	7	24	theme	consequences	1224:1235	arg1	understanding					1193:1205	our understanding	1189:1205	our understanding of the molecular consequences of O-GlcNAc	1189:1247	Our results expand our understanding of the molecular consequences of O-GlcNAc and how it affects protein-DNA interfaces.
34546745	6	25	theme	HMGB1	1086:1090	arg1	ability					1075:1081	the ability	1071:1081	the ability of HMGB1 to facilitate DNA repair	1071:1115	Using cell-free extracts, we also found that O-GlcNAc reduces the ability of HMGB1 to facilitate DNA repair, resulting in error-prone processing of damaged DNA.
34546745	6	26	theme	DNA	1165:1167	arg1	processing					1143:1152	error-prone processing	1131:1152	error-prone processing of damaged DNA	1131:1167	Using cell-free extracts, we also found that O-GlcNAc reduces the ability of HMGB1 to facilitate DNA repair, resulting in error-prone processing of damaged DNA.
34546745	8	27	from	mutations	1397:1405	arg1	states					1425:1430	certain cancer states	1410:1430	certain cancer states	1410:1430	Importantly, our work may also support a link between upregulated O-GlcNAc levels and increased rates of mutations in certain cancer states.
34546745	1	28	theme	dynamic	158:164	arg1	O-GlcNAcylation					122:136	Protein O-GlcNAcylation	114:136	Protein O-GlcNAcylation	114:136	Protein O-GlcNAcylation is an essential and dynamic regulator of myriad cellular processes, including DNA replication and repair.
34546745	1	28	theme	dynamic	158:164	arg1	regulator					166:174	an essential and dynamic regulator	141:174	an essential and dynamic regulator of myriad cellular processes, including DNA replication and repair	141:241	Protein O-GlcNAcylation is an essential and dynamic regulator of myriad cellular processes, including DNA replication and repair.
34546745	2	29	theme	protein	306:312	arg1	HMGB1					314:318	the multifunctional nuclear protein HMGB1	278:318	the multifunctional nuclear protein HMGB1	278:318	Proteomic studies have identified the multifunctional nuclear protein HMGB1 as O-GlcNAcylated, providing a potential link between this modification and DNA damage responses.
34546745	0	30	theme	Mobility	24:31	arg1	Box					39:41	High Mobility Group Box 1	19:43	High Mobility Group Box 1 (HMGB1)	19:51	O-GlcNAcylation of High Mobility Group Box 1 (HMGB1) Alters Its DNA Binding and DNA Damage Processing Activities.
34546745	0	30	theme	Mobility	24:31	arg1	HMGB1					46:50	HMGB1	46:50	HMGB1	46:50	O-GlcNAcylation of High Mobility Group Box 1 (HMGB1) Alters Its DNA Binding and DNA Damage Processing Activities.
34546745	0	31	theme	Processing	91:100	arg1	Activities					102:111	DNA Damage Processing Activities	80:111	DNA Damage Processing Activities	80:111	O-GlcNAcylation of High Mobility Group Box 1 (HMGB1) Alters Its DNA Binding and DNA Damage Processing Activities.
34546745	2	32	theme	nuclear	298:304	arg1	protein					306:312	the multifunctional nuclear protein	278:312	the multifunctional nuclear protein HMGB1	278:318	Proteomic studies have identified the multifunctional nuclear protein HMGB1 as O-GlcNAcylated, providing a potential link between this modification and DNA damage responses.
34546745	3	33	theme	endogenous	448:457	arg1	modification					459:470	the protein's endogenous modification	434:470	the protein's endogenous modification	434:470	Here, we verify the protein's endogenous modification at S100 and S107 and found that the major modification site is S100, a residue that can potentially influence HMGB1-DNA interactions.
34546745	0	34	theme	High	19:22	arg1	Box					39:41	High Mobility Group Box 1	19:43	High Mobility Group Box 1 (HMGB1)	19:51	O-GlcNAcylation of High Mobility Group Box 1 (HMGB1) Alters Its DNA Binding and DNA Damage Processing Activities.
34546745	0	34	theme	High	19:22	arg1	HMGB1					46:50	HMGB1	46:50	HMGB1	46:50	O-GlcNAcylation of High Mobility Group Box 1 (HMGB1) Alters Its DNA Binding and DNA Damage Processing Activities.
34546745	0	35	theme	Damage	84:89	arg1	Activities					102:111	DNA Damage Processing Activities	80:111	DNA Damage Processing Activities	80:111	O-GlcNAcylation of High Mobility Group Box 1 (HMGB1) Alters Its DNA Binding and DNA Damage Processing Activities.
34546745	2	36	theme	multifunctional	282:296	arg1	protein					306:312	the multifunctional nuclear protein	278:312	the multifunctional nuclear protein HMGB1	278:318	Proteomic studies have identified the multifunctional nuclear protein HMGB1 as O-GlcNAcylated, providing a potential link between this modification and DNA damage responses.
34546745	1	37	theme	myriad	179:184	arg1	repair					236:241	repair	236:241	repair	236:241	Protein O-GlcNAcylation is an essential and dynamic regulator of myriad cellular processes, including DNA replication and repair.
34546745	1	37	theme	myriad	179:184	arg1	replication					220:230	DNA replication	216:230	DNA replication	216:230	Protein O-GlcNAcylation is an essential and dynamic regulator of myriad cellular processes, including DNA replication and repair.
34546745	1	37	theme	myriad	179:184	arg1	processes					195:203	myriad cellular processes	179:203	myriad cellular processes	179:203	Protein O-GlcNAcylation is an essential and dynamic regulator of myriad cellular processes, including DNA replication and repair.
34546745	0	38	theme	Box	39:41	arg1	O-GlcNAcylation					0:14	O-GlcNAcylation	0:14	O-GlcNAcylation of High Mobility Group Box 1 (HMGB1)	0:51	O-GlcNAcylation of High Mobility Group Box 1 (HMGB1) Alters Its DNA Binding and DNA Damage Processing Activities.
34546745	5	39	theme	linear	849:854	arg1	DNA					931:933	linear, nucleosomal, supercoiled, cruciform, and interstrand cross-linked damaged DNA	849:933	linear, nucleosomal, supercoiled, cruciform, and interstrand cross-linked damaged DNA	849:933	We found that O-GlcNAc alters HMGB1 binding to linear, nucleosomal, supercoiled, cruciform, and interstrand cross-linked damaged DNA, generally resulting in enhanced oligomerization on these DNA structures.
34546745	8	40	from	states	1425:1430	arg1	levels					1367:1372	upregulated O-GlcNAc levels	1346:1372	upregulated O-GlcNAc levels	1346:1372	Importantly, our work may also support a link between upregulated O-GlcNAc levels and increased rates of mutations in certain cancer states.
34546745	8	40	from	states	1425:1430	arg1	rates					1388:1392	increased rates	1378:1392	increased rates of mutations in certain cancer states	1378:1430	Importantly, our work may also support a link between upregulated O-GlcNAc levels and increased rates of mutations in certain cancer states.
34546745	1	41	theme	cellular	186:193	arg1	repair					236:241	repair	236:241	repair	236:241	Protein O-GlcNAcylation is an essential and dynamic regulator of myriad cellular processes, including DNA replication and repair.
34546745	1	41	theme	cellular	186:193	arg1	replication					220:230	DNA replication	216:230	DNA replication	216:230	Protein O-GlcNAcylation is an essential and dynamic regulator of myriad cellular processes, including DNA replication and repair.
34546745	1	41	theme	cellular	186:193	arg1	processes					195:203	myriad cellular processes	179:203	myriad cellular processes	179:203	Protein O-GlcNAcylation is an essential and dynamic regulator of myriad cellular processes, including DNA replication and repair.
34546745	2	42	theme	DNA	396:398	arg1	damage					400:405	DNA damage	396:405	DNA damage	396:405	Proteomic studies have identified the multifunctional nuclear protein HMGB1 as O-GlcNAcylated, providing a potential link between this modification and DNA damage responses.
34546745	0	43	theme	Group	33:37	arg1	Box					39:41	High Mobility Group Box 1	19:43	High Mobility Group Box 1 (HMGB1)	19:51	O-GlcNAcylation of High Mobility Group Box 1 (HMGB1) Alters Its DNA Binding and DNA Damage Processing Activities.
34546745	0	43	theme	Group	33:37	arg1	HMGB1					46:50	HMGB1	46:50	HMGB1	46:50	O-GlcNAcylation of High Mobility Group Box 1 (HMGB1) Alters Its DNA Binding and DNA Damage Processing Activities.
34546745	8	44	theme	mutations	1397:1405	arg1	levels					1367:1372	upregulated O-GlcNAc levels	1346:1372	upregulated O-GlcNAc levels	1346:1372	Importantly, our work may also support a link between upregulated O-GlcNAc levels and increased rates of mutations in certain cancer states.
34546745	8	44	theme	mutations	1397:1405	arg1	rates					1388:1392	increased rates	1378:1392	increased rates of mutations in certain cancer states	1378:1430	Importantly, our work may also support a link between upregulated O-GlcNAc levels and increased rates of mutations in certain cancer states.
34546745	1	45	theme	processes	195:203	arg1	O-GlcNAcylation					122:136	Protein O-GlcNAcylation	114:136	Protein O-GlcNAcylation	114:136	Protein O-GlcNAcylation is an essential and dynamic regulator of myriad cellular processes, including DNA replication and repair.
34546745	1	45	theme	processes	195:203	arg1	regulator					166:174	an essential and dynamic regulator	141:174	an essential and dynamic regulator of myriad cellular processes, including DNA replication and repair	141:241	Protein O-GlcNAcylation is an essential and dynamic regulator of myriad cellular processes, including DNA replication and repair.
34546745	5	46	theme	supercoiled	870:880	arg1	DNA					931:933	linear, nucleosomal, supercoiled, cruciform, and interstrand cross-linked damaged DNA	849:933	linear, nucleosomal, supercoiled, cruciform, and interstrand cross-linked damaged DNA	849:933	We found that O-GlcNAc alters HMGB1 binding to linear, nucleosomal, supercoiled, cruciform, and interstrand cross-linked damaged DNA, generally resulting in enhanced oligomerization on these DNA structures.
34546745	8	47	theme	increased	1378:1386	arg1	rates					1388:1392	increased rates	1378:1392	increased rates of mutations in certain cancer states	1378:1430	Importantly, our work may also support a link between upregulated O-GlcNAc levels and increased rates of mutations in certain cancer states.
34546745	8	48	theme	cancer	1418:1423	arg1	states					1425:1430	certain cancer states	1410:1430	certain cancer states	1410:1430	Importantly, our work may also support a link between upregulated O-GlcNAc levels and increased rates of mutations in certain cancer states.
34546745	5	49	theme	cross-linked	910:921	arg1	DNA					931:933	linear, nucleosomal, supercoiled, cruciform, and interstrand cross-linked damaged DNA	849:933	linear, nucleosomal, supercoiled, cruciform, and interstrand cross-linked damaged DNA	849:933	We found that O-GlcNAc alters HMGB1 binding to linear, nucleosomal, supercoiled, cruciform, and interstrand cross-linked damaged DNA, generally resulting in enhanced oligomerization on these DNA structures.
34546745	8	50	theme	certain	1410:1416	arg1	states					1425:1430	certain cancer states	1410:1430	certain cancer states	1410:1430	Importantly, our work may also support a link between upregulated O-GlcNAc levels and increased rates of mutations in certain cancer states.
34546745	5	51	theme	damaged	923:929	arg1	DNA					931:933	linear, nucleosomal, supercoiled, cruciform, and interstrand cross-linked damaged DNA	849:933	linear, nucleosomal, supercoiled, cruciform, and interstrand cross-linked damaged DNA	849:933	We found that O-GlcNAc alters HMGB1 binding to linear, nucleosomal, supercoiled, cruciform, and interstrand cross-linked damaged DNA, generally resulting in enhanced oligomerization on these DNA structures.
34546745	4	52	from	effect	740:745	arg1	activity					792:799	its DNA binding activity	776:799	its DNA binding activity	776:799	Using synthetic protein chemistry, we generated site-specifically O-GlcNAc-modified HMGB1 at S100 and characterized biochemically the effect of the sugar modification on its DNA binding activity.
34546745	5	53	link	cross-linked	910:921	arg1	DNA					931:933	linear, nucleosomal, supercoiled, cruciform, and interstrand cross-linked damaged DNA	849:933	linear, nucleosomal, supercoiled, cruciform, and interstrand cross-linked damaged DNA	849:933	We found that O-GlcNAc alters HMGB1 binding to linear, nucleosomal, supercoiled, cruciform, and interstrand cross-linked damaged DNA, generally resulting in enhanced oligomerization on these DNA structures.
34546745	2	54	theme	Proteomic	244:252	arg1	studies					254:260	Proteomic studies	244:260	Proteomic studies	244:260	Proteomic studies have identified the multifunctional nuclear protein HMGB1 as O-GlcNAcylated, providing a potential link between this modification and DNA damage responses.
34546745	2	55	dep	modification	379:390	arg1	responses					407:415	responses	407:415	responses	407:415	Proteomic studies have identified the multifunctional nuclear protein HMGB1 as O-GlcNAcylated, providing a potential link between this modification and DNA damage responses.
34546745	2	55	dep	modification	379:390	arg1	this					374:377	this	374:377	this	374:377	Proteomic studies have identified the multifunctional nuclear protein HMGB1 as O-GlcNAcylated, providing a potential link between this modification and DNA damage responses.
34546745	7	56	theme	protein-DNA	1268:1278	arg1	interfaces					1280:1289	protein-DNA interfaces	1268:1289	protein-DNA interfaces	1268:1289	Our results expand our understanding of the molecular consequences of O-GlcNAc and how it affects protein-DNA interfaces.
34546745	4	57	theme	modification	760:771	arg1	effect					740:745	the effect	736:745	the effect of the sugar modification on its DNA binding activity	736:799	Using synthetic protein chemistry, we generated site-specifically O-GlcNAc-modified HMGB1 at S100 and characterized biochemically the effect of the sugar modification on its DNA binding activity.
34546745	4	58	theme	DNA	780:782	arg1	activity					792:799	its DNA binding activity	776:799	its DNA binding activity	776:799	Using synthetic protein chemistry, we generated site-specifically O-GlcNAc-modified HMGB1 at S100 and characterized biochemically the effect of the sugar modification on its DNA binding activity.
34546745	4	59	theme	binding	784:790	arg1	activity					792:799	its DNA binding activity	776:799	its DNA binding activity	776:799	Using synthetic protein chemistry, we generated site-specifically O-GlcNAc-modified HMGB1 at S100 and characterized biochemically the effect of the sugar modification on its DNA binding activity.
34546745	3	60	theme	HMGB1-DNA	582:590	arg1	interactions					592:603	HMGB1-DNA interactions	582:603	HMGB1-DNA interactions	582:603	Here, we verify the protein's endogenous modification at S100 and S107 and found that the major modification site is S100, a residue that can potentially influence HMGB1-DNA interactions.
34546745	4	61	theme	protein	622:628	arg1	chemistry					630:638	synthetic protein chemistry	612:638	synthetic protein chemistry	612:638	Using synthetic protein chemistry, we generated site-specifically O-GlcNAc-modified HMGB1 at S100 and characterized biochemically the effect of the sugar modification on its DNA binding activity.
34546745	1	62	theme	Protein	114:120	arg1	O-GlcNAcylation					122:136	Protein O-GlcNAcylation	114:136	Protein O-GlcNAcylation	114:136	Protein O-GlcNAcylation is an essential and dynamic regulator of myriad cellular processes, including DNA replication and repair.
34546745	1	62	theme	Protein	114:120	arg1	regulator					166:174	an essential and dynamic regulator	141:174	an essential and dynamic regulator of myriad cellular processes, including DNA replication and repair	141:241	Protein O-GlcNAcylation is an essential and dynamic regulator of myriad cellular processes, including DNA replication and repair.
34546745	1	63	theme	DNA	216:218	arg1	replication					220:230	DNA replication	216:230	DNA replication	216:230	Protein O-GlcNAcylation is an essential and dynamic regulator of myriad cellular processes, including DNA replication and repair.
34546745	7	64	theme	O-GlcNAc	1240:1247	arg1	consequences					1224:1235	the molecular consequences	1210:1235	the molecular consequences of O-GlcNAc	1210:1247	Our results expand our understanding of the molecular consequences of O-GlcNAc and how it affects protein-DNA interfaces.
34546745	5	65	theme	HMGB1	832:836	arg1	binding					838:844	HMGB1 binding	832:844	HMGB1 binding to linear, nucleosomal, supercoiled, cruciform, and interstrand cross-linked damaged DNA	832:933	We found that O-GlcNAc alters HMGB1 binding to linear, nucleosomal, supercoiled, cruciform, and interstrand cross-linked damaged DNA, generally resulting in enhanced oligomerization on these DNA structures.
34546745	6	66	theme	DNA	1106:1108	arg1	repair					1110:1115	DNA repair	1106:1115	DNA repair	1106:1115	Using cell-free extracts, we also found that O-GlcNAc reduces the ability of HMGB1 to facilitate DNA repair, resulting in error-prone processing of damaged DNA.
34220449	0	0	theme	Local	79:83	arg1	Changes					100:106	Local Conformational Changes	79:106	Local Conformational Changes of the C-Terminus	79:124	Phosphorylation and O-GlcNAcylation of the PHF-1 Epitope of Tau Protein Induce Local Conformational Changes of the C-Terminus and Modulate Tau Self-Assembly Into Fibrillar Aggregates.
34220449	2	1	dep	Tau	505:507	arg1	dys					510:512	dys	510:512	dys	510:512	In recent years, other posttranslational modifications (PTMs) have been highlighted in the regulation of Tau (dys)functions.
34220449	4	2	theme	Tau	707:709	arg1	domain					722:727	Tau C-terminal domain	707:727	Tau C-terminal domain	707:727	We here focus on the role of the PHF-1 phospho-epitope of Tau C-terminal domain that is hyperphosphorylated in AD (at pS396/pS404) and encompasses S400 as the major O-GlcNAc site of Tau while two additional O-GlcNAc sites were found in the extreme C-terminus at S412 and S413.
34220449	5	3	theme	small	1184:1188	arg1	peptides					1190:1197	small peptides	1184:1197	small peptides	1184:1197	Using high resolution NMR spectroscopy, we showed that the O-GlcNAc glycosylation reduces phosphorylation of PHF-1 epitope by GSK3β alone or after priming by CDK2/cyclin A. Furthermore, investigations of the impact of PTMs on local conformation performed in small peptides highlight the role of S404 phosphorylation in inducing helical propensity in the region downstream pS404 that is exacerbated by other phosphorylations of PHF-1 epitope at S396 and S400, or O-GlcNAcylation of S400.
34220449	4	4	theme	O-GlcNAc	856:863	arg1	sites					865:869	two additional O-GlcNAc sites	841:869	two additional O-GlcNAc sites	841:869	We here focus on the role of the PHF-1 phospho-epitope of Tau C-terminal domain that is hyperphosphorylated in AD (at pS396/pS404) and encompasses S400 as the major O-GlcNAc site of Tau while two additional O-GlcNAc sites were found in the extreme C-terminus at S412 and S413.
34220449	5	5	theme	PTMs	1144:1147	arg1	impact					1134:1139	the impact	1130:1139	the impact of PTMs on local conformation	1130:1169	Using high resolution NMR spectroscopy, we showed that the O-GlcNAc glycosylation reduces phosphorylation of PHF-1 epitope by GSK3β alone or after priming by CDK2/cyclin A. Furthermore, investigations of the impact of PTMs on local conformation performed in small peptides highlight the role of S404 phosphorylation in inducing helical propensity in the region downstream pS404 that is exacerbated by other phosphorylations of PHF-1 epitope at S396 and S400, or O-GlcNAcylation of S400.
34220449	5	6	theme	helical	1254:1260	arg1	propensity					1262:1271	helical propensity	1254:1271	helical propensity	1254:1271	Using high resolution NMR spectroscopy, we showed that the O-GlcNAc glycosylation reduces phosphorylation of PHF-1 epitope by GSK3β alone or after priming by CDK2/cyclin A. Furthermore, investigations of the impact of PTMs on local conformation performed in small peptides highlight the role of S404 phosphorylation in inducing helical propensity in the region downstream pS404 that is exacerbated by other phosphorylations of PHF-1 epitope at S396 and S400, or O-GlcNAcylation of S400.
34220449	1	7	theme	disease	379:385	arg1	brains					392:397	Alzheimer's disease (AD) brains	367:397	Alzheimer's disease (AD) brains	367:397	Phosphorylation of the neuronal microtubule-associated Tau protein plays a critical role in the aggregation process leading to the formation of insoluble intraneuronal fibrils within Alzheimer's disease (AD) brains.
34220449	5	8	from	impact	1134:1139	arg1	conformation					1158:1169	local conformation	1152:1169	local conformation	1152:1169	Using high resolution NMR spectroscopy, we showed that the O-GlcNAc glycosylation reduces phosphorylation of PHF-1 epitope by GSK3β alone or after priming by CDK2/cyclin A. Furthermore, investigations of the impact of PTMs on local conformation performed in small peptides highlight the role of S404 phosphorylation in inducing helical propensity in the region downstream pS404 that is exacerbated by other phosphorylations of PHF-1 epitope at S396 and S400, or O-GlcNAcylation of S400.
34220449	5	9	theme	NMR	948:950	arg1	spectroscopy					952:963	high resolution NMR spectroscopy	932:963	high resolution NMR spectroscopy	932:963	Using high resolution NMR spectroscopy, we showed that the O-GlcNAc glycosylation reduces phosphorylation of PHF-1 epitope by GSK3β alone or after priming by CDK2/cyclin A. Furthermore, investigations of the impact of PTMs on local conformation performed in small peptides highlight the role of S404 phosphorylation in inducing helical propensity in the region downstream pS404 that is exacerbated by other phosphorylations of PHF-1 epitope at S396 and S400, or O-GlcNAcylation of S400.
34220449	5	10	theme	resolution	937:946	arg1	spectroscopy					952:963	high resolution NMR spectroscopy	932:963	high resolution NMR spectroscopy	932:963	Using high resolution NMR spectroscopy, we showed that the O-GlcNAc glycosylation reduces phosphorylation of PHF-1 epitope by GSK3β alone or after priming by CDK2/cyclin A. Furthermore, investigations of the impact of PTMs on local conformation performed in small peptides highlight the role of S404 phosphorylation in inducing helical propensity in the region downstream pS404 that is exacerbated by other phosphorylations of PHF-1 epitope at S396 and S400, or O-GlcNAcylation of S400.
34220449	1	11	theme	aggregation	280:290	arg1	process					292:298	the aggregation process	276:298	the aggregation process leading to the formation of insoluble intraneuronal fibrils within Alzheimer's disease (AD) brains	276:397	Phosphorylation of the neuronal microtubule-associated Tau protein plays a critical role in the aggregation process leading to the formation of insoluble intraneuronal fibrils within Alzheimer's disease (AD) brains.
34220449	2	12	theme	functions	514:522	arg1	regulation					491:500	the regulation	487:500	the regulation of Tau (dys)functions	487:522	In recent years, other posttranslational modifications (PTMs) have been highlighted in the regulation of Tau (dys)functions.
34220449	5	13	theme	S404	1221:1224	arg1	phosphorylation					1226:1240	S404 phosphorylation	1221:1240	S404 phosphorylation	1221:1240	Using high resolution NMR spectroscopy, we showed that the O-GlcNAc glycosylation reduces phosphorylation of PHF-1 epitope by GSK3β alone or after priming by CDK2/cyclin A. Furthermore, investigations of the impact of PTMs on local conformation performed in small peptides highlight the role of S404 phosphorylation in inducing helical propensity in the region downstream pS404 that is exacerbated by other phosphorylations of PHF-1 epitope at S396 and S400, or O-GlcNAcylation of S400.
34220449	5	14	theme	phosphorylation	1226:1240	arg1	O-GlcNAcylation					1388:1402	O-GlcNAcylation	1388:1402	O-GlcNAcylation of S400	1388:1410	Using high resolution NMR spectroscopy, we showed that the O-GlcNAc glycosylation reduces phosphorylation of PHF-1 epitope by GSK3β alone or after priming by CDK2/cyclin A. Furthermore, investigations of the impact of PTMs on local conformation performed in small peptides highlight the role of S404 phosphorylation in inducing helical propensity in the region downstream pS404 that is exacerbated by other phosphorylations of PHF-1 epitope at S396 and S400, or O-GlcNAcylation of S400.
34220449	5	14	theme	phosphorylation	1226:1240	arg1	role					1213:1216	the role	1209:1216	the role of S404 phosphorylation in inducing helical propensity in the region downstream pS404 that is exacerbated by other phosphorylations of PHF-1 epitope at S396 and S400	1209:1382	Using high resolution NMR spectroscopy, we showed that the O-GlcNAc glycosylation reduces phosphorylation of PHF-1 epitope by GSK3β alone or after priming by CDK2/cyclin A. Furthermore, investigations of the impact of PTMs on local conformation performed in small peptides highlight the role of S404 phosphorylation in inducing helical propensity in the region downstream pS404 that is exacerbated by other phosphorylations of PHF-1 epitope at S396 and S400, or O-GlcNAcylation of S400.
34220449	4	15	from	pS396/pS404	767:777	arg1	AD					760:761	AD	760:761	AD (at pS396/pS404)	760:778	We here focus on the role of the PHF-1 phospho-epitope of Tau C-terminal domain that is hyperphosphorylated in AD (at pS396/pS404) and encompasses S400 as the major O-GlcNAc site of Tau while two additional O-GlcNAc sites were found in the extreme C-terminus at S412 and S413.
34220449	2	16	theme	posttranslational	423:439	arg1	PTMs					456:459	PTMs	456:459	PTMs	456:459	In recent years, other posttranslational modifications (PTMs) have been highlighted in the regulation of Tau (dys)functions.
34220449	2	16	theme	posttranslational	423:439	arg1	modifications					441:453	other posttranslational modifications	417:453	other posttranslational modifications (PTMs)	417:460	In recent years, other posttranslational modifications (PTMs) have been highlighted in the regulation of Tau (dys)functions.
34220449	5	17	theme	other	1327:1331	arg1	phosphorylations					1333:1348	other phosphorylations	1327:1348	other phosphorylations of PHF-1 epitope at S396 and S400	1327:1382	Using high resolution NMR spectroscopy, we showed that the O-GlcNAc glycosylation reduces phosphorylation of PHF-1 epitope by GSK3β alone or after priming by CDK2/cyclin A. Furthermore, investigations of the impact of PTMs on local conformation performed in small peptides highlight the role of S404 phosphorylation in inducing helical propensity in the region downstream pS404 that is exacerbated by other phosphorylations of PHF-1 epitope at S396 and S400, or O-GlcNAcylation of S400.
34220449	5	18	from	investigations	1112:1125	arg1	conformation					1158:1169	local conformation	1152:1169	local conformation	1152:1169	Using high resolution NMR spectroscopy, we showed that the O-GlcNAc glycosylation reduces phosphorylation of PHF-1 epitope by GSK3β alone or after priming by CDK2/cyclin A. Furthermore, investigations of the impact of PTMs on local conformation performed in small peptides highlight the role of S404 phosphorylation in inducing helical propensity in the region downstream pS404 that is exacerbated by other phosphorylations of PHF-1 epitope at S396 and S400, or O-GlcNAcylation of S400.
34220449	4	19	theme	Tau	831:833	arg1	Tau					831:833	Tau	831:833	Tau	831:833	We here focus on the role of the PHF-1 phospho-epitope of Tau C-terminal domain that is hyperphosphorylated in AD (at pS396/pS404) and encompasses S400 as the major O-GlcNAc site of Tau while two additional O-GlcNAc sites were found in the extreme C-terminus at S412 and S413.
34220449	4	19	theme	Tau	831:833	arg1	site					823:826	the major O-GlcNAc site	804:826	the major O-GlcNAc site of Tau	804:833	We here focus on the role of the PHF-1 phospho-epitope of Tau C-terminal domain that is hyperphosphorylated in AD (at pS396/pS404) and encompasses S400 as the major O-GlcNAc site of Tau while two additional O-GlcNAc sites were found in the extreme C-terminus at S412 and S413.
34220449	4	19	theme	Tau	831:833	arg1	S400					796:799	S400	796:799	S400	796:799	We here focus on the role of the PHF-1 phospho-epitope of Tau C-terminal domain that is hyperphosphorylated in AD (at pS396/pS404) and encompasses S400 as the major O-GlcNAc site of Tau while two additional O-GlcNAc sites were found in the extreme C-terminus at S412 and S413.
34220449	2	20	theme	recent	403:408	arg1	years					410:414	recent years	403:414	recent years	403:414	In recent years, other posttranslational modifications (PTMs) have been highlighted in the regulation of Tau (dys)functions.
34220449	4	21	theme	extreme	889:895	arg1	C-terminus					897:906	the extreme C-terminus	885:906	the extreme C-terminus	885:906	We here focus on the role of the PHF-1 phospho-epitope of Tau C-terminal domain that is hyperphosphorylated in AD (at pS396/pS404) and encompasses S400 as the major O-GlcNAc site of Tau while two additional O-GlcNAc sites were found in the extreme C-terminus at S412 and S413.
34220449	4	22	theme	additional	845:854	arg1	sites					865:869	two additional O-GlcNAc sites	841:869	two additional O-GlcNAc sites	841:869	We here focus on the role of the PHF-1 phospho-epitope of Tau C-terminal domain that is hyperphosphorylated in AD (at pS396/pS404) and encompasses S400 as the major O-GlcNAc site of Tau while two additional O-GlcNAc sites were found in the extreme C-terminus at S412 and S413.
34220449	6	23	theme	phosphorylation	1434:1448	arg1	role					1426:1429	the role	1422:1429	the role of phosphorylation and O-GlcNAcylation of PHF-1 epitope	1422:1485	Finally, the role of phosphorylation and O-GlcNAcylation of PHF-1 epitope was probed in in-vitro fibrillization assays in which O-GlcNAcylation slows down the rate of fibrillar assembly while GSK3β phosphorylation stimulates aggregation counteracting the effect of glycosylation.
34220449	5	24	theme	local	1152:1156	arg1	conformation					1158:1169	local conformation	1152:1169	local conformation	1152:1169	Using high resolution NMR spectroscopy, we showed that the O-GlcNAc glycosylation reduces phosphorylation of PHF-1 epitope by GSK3β alone or after priming by CDK2/cyclin A. Furthermore, investigations of the impact of PTMs on local conformation performed in small peptides highlight the role of S404 phosphorylation in inducing helical propensity in the region downstream pS404 that is exacerbated by other phosphorylations of PHF-1 epitope at S396 and S400, or O-GlcNAcylation of S400.
34220449	5	25	from	conformation	1158:1169	arg1	investigations					1112:1125	investigations	1112:1125	investigations of the impact of PTMs on local conformation performed in small peptides	1112:1197	Using high resolution NMR spectroscopy, we showed that the O-GlcNAc glycosylation reduces phosphorylation of PHF-1 epitope by GSK3β alone or after priming by CDK2/cyclin A. Furthermore, investigations of the impact of PTMs on local conformation performed in small peptides highlight the role of S404 phosphorylation in inducing helical propensity in the region downstream pS404 that is exacerbated by other phosphorylations of PHF-1 epitope at S396 and S400, or O-GlcNAcylation of S400.
34220449	5	26	theme	S400	1407:1410	arg1	O-GlcNAcylation					1388:1402	O-GlcNAcylation	1388:1402	O-GlcNAcylation of S400	1388:1410	Using high resolution NMR spectroscopy, we showed that the O-GlcNAc glycosylation reduces phosphorylation of PHF-1 epitope by GSK3β alone or after priming by CDK2/cyclin A. Furthermore, investigations of the impact of PTMs on local conformation performed in small peptides highlight the role of S404 phosphorylation in inducing helical propensity in the region downstream pS404 that is exacerbated by other phosphorylations of PHF-1 epitope at S396 and S400, or O-GlcNAcylation of S400.
34220449	5	26	theme	S400	1407:1410	arg1	role					1213:1216	the role	1209:1216	the role of S404 phosphorylation in inducing helical propensity in the region downstream pS404 that is exacerbated by other phosphorylations of PHF-1 epitope at S396 and S400	1209:1382	Using high resolution NMR spectroscopy, we showed that the O-GlcNAc glycosylation reduces phosphorylation of PHF-1 epitope by GSK3β alone or after priming by CDK2/cyclin A. Furthermore, investigations of the impact of PTMs on local conformation performed in small peptides highlight the role of S404 phosphorylation in inducing helical propensity in the region downstream pS404 that is exacerbated by other phosphorylations of PHF-1 epitope at S396 and S400, or O-GlcNAcylation of S400.
34220449	6	27	theme	fibrillization	1510:1523	arg1	assays					1525:1530	in-vitro fibrillization assays	1501:1530	in-vitro fibrillization assays in which O-GlcNAcylation slows down the rate of fibrillar assembly while GSK3β phosphorylation stimulates aggregation counteracting the effect of glycosylation	1501:1690	Finally, the role of phosphorylation and O-GlcNAcylation of PHF-1 epitope was probed in in-vitro fibrillization assays in which O-GlcNAcylation slows down the rate of fibrillar assembly while GSK3β phosphorylation stimulates aggregation counteracting the effect of glycosylation.
34220449	5	28	from	S396	1370:1373	arg1	phosphorylations					1333:1348	other phosphorylations	1327:1348	other phosphorylations of PHF-1 epitope at S396 and S400	1327:1382	Using high resolution NMR spectroscopy, we showed that the O-GlcNAc glycosylation reduces phosphorylation of PHF-1 epitope by GSK3β alone or after priming by CDK2/cyclin A. Furthermore, investigations of the impact of PTMs on local conformation performed in small peptides highlight the role of S404 phosphorylation in inducing helical propensity in the region downstream pS404 that is exacerbated by other phosphorylations of PHF-1 epitope at S396 and S400, or O-GlcNAcylation of S400.
34220449	5	28	from	S396	1370:1373	arg1	epitope					1359:1365	PHF-1 epitope	1353:1365	PHF-1 epitope at S396 and S400	1353:1382	Using high resolution NMR spectroscopy, we showed that the O-GlcNAc glycosylation reduces phosphorylation of PHF-1 epitope by GSK3β alone or after priming by CDK2/cyclin A. Furthermore, investigations of the impact of PTMs on local conformation performed in small peptides highlight the role of S404 phosphorylation in inducing helical propensity in the region downstream pS404 that is exacerbated by other phosphorylations of PHF-1 epitope at S396 and S400, or O-GlcNAcylation of S400.
34220449	6	29	theme	GSK3β	1605:1609	arg1	phosphorylation					1611:1625	GSK3β phosphorylation	1605:1625	GSK3β phosphorylation	1605:1625	Finally, the role of phosphorylation and O-GlcNAcylation of PHF-1 epitope was probed in in-vitro fibrillization assays in which O-GlcNAcylation slows down the rate of fibrillar assembly while GSK3β phosphorylation stimulates aggregation counteracting the effect of glycosylation.
34220449	5	30	theme	high	932:935	arg1	spectroscopy					952:963	high resolution NMR spectroscopy	932:963	high resolution NMR spectroscopy	932:963	Using high resolution NMR spectroscopy, we showed that the O-GlcNAc glycosylation reduces phosphorylation of PHF-1 epitope by GSK3β alone or after priming by CDK2/cyclin A. Furthermore, investigations of the impact of PTMs on local conformation performed in small peptides highlight the role of S404 phosphorylation in inducing helical propensity in the region downstream pS404 that is exacerbated by other phosphorylations of PHF-1 epitope at S396 and S400, or O-GlcNAcylation of S400.
34220449	6	31	theme	in-vitro	1501:1508	arg1	assays					1525:1530	in-vitro fibrillization assays	1501:1530	in-vitro fibrillization assays in which O-GlcNAcylation slows down the rate of fibrillar assembly while GSK3β phosphorylation stimulates aggregation counteracting the effect of glycosylation	1501:1690	Finally, the role of phosphorylation and O-GlcNAcylation of PHF-1 epitope was probed in in-vitro fibrillization assays in which O-GlcNAcylation slows down the rate of fibrillar assembly while GSK3β phosphorylation stimulates aggregation counteracting the effect of glycosylation.
34220449	1	32	theme	neuronal	207:214	arg1	protein					243:249	the neuronal microtubule-associated Tau protein	203:249	the neuronal microtubule-associated Tau protein	203:249	Phosphorylation of the neuronal microtubule-associated Tau protein plays a critical role in the aggregation process leading to the formation of insoluble intraneuronal fibrils within Alzheimer's disease (AD) brains.
34220449	0	33	theme	C-Terminus	115:124	arg1	Changes					100:106	Local Conformational Changes	79:106	Local Conformational Changes of the C-Terminus	79:124	Phosphorylation and O-GlcNAcylation of the PHF-1 Epitope of Tau Protein Induce Local Conformational Changes of the C-Terminus and Modulate Tau Self-Assembly Into Fibrillar Aggregates.
34220449	3	34	theme	O-β-linked	547:556	arg1	O-GlcNAcylation					585:599	O-GlcNAcylation	585:599	O-GlcNAcylation	585:599	Among these PTMs, the O-β-linked N-acetylglucosaminylation (O-GlcNAcylation) modulates Tau phosphorylation and aggregation.
34220449	3	34	theme	O-β-linked	547:556	arg1	N-acetylglucosaminylation					558:582	the O-β-linked N-acetylglucosaminylation	543:582	the O-β-linked N-acetylglucosaminylation (O-GlcNAcylation)	543:600	Among these PTMs, the O-β-linked N-acetylglucosaminylation (O-GlcNAcylation) modulates Tau phosphorylation and aggregation.
34220449	1	35	theme	microtubule-associated	216:237	arg1	protein					243:249	the neuronal microtubule-associated Tau protein	203:249	the neuronal microtubule-associated Tau protein	203:249	Phosphorylation of the neuronal microtubule-associated Tau protein plays a critical role in the aggregation process leading to the formation of insoluble intraneuronal fibrils within Alzheimer's disease (AD) brains.
34220449	0	36	theme	PHF-1	43:47	arg1	Epitope					49:55	the PHF-1 Epitope	39:55	the PHF-1 Epitope	39:55	Phosphorylation and O-GlcNAcylation of the PHF-1 Epitope of Tau Protein Induce Local Conformational Changes of the C-Terminus and Modulate Tau Self-Assembly Into Fibrillar Aggregates.
34220449	5	37	dep	CDK2/cyclin	1084:1094	arg1	A.					1096:1097	CDK2/cyclin A. Furthermore, investigations of the impact of PTMs on local conformation performed in small peptides highlight the role of S404 phosphorylation in inducing helical propensity in the region downstream pS404 that is exacerbated by other phosphorylations of PHF-1 epitope at S396 and S400, or O-GlcNAcylation of S400	1084:1410	CDK2/cyclin A. Furthermore, investigations of the impact of PTMs on local conformation performed in small peptides highlight the role of S404 phosphorylation in inducing helical propensity in the region downstream pS404 that is exacerbated by other phosphorylations of PHF-1 epitope at S396 and S400, or O-GlcNAcylation of S400	1084:1410	Using high resolution NMR spectroscopy, we showed that the O-GlcNAc glycosylation reduces phosphorylation of PHF-1 epitope by GSK3β alone or after priming by CDK2/cyclin A. Furthermore, investigations of the impact of PTMs on local conformation performed in small peptides highlight the role of S404 phosphorylation in inducing helical propensity in the region downstream pS404 that is exacerbated by other phosphorylations of PHF-1 epitope at S396 and S400, or O-GlcNAcylation of S400.
34220449	5	37	dep	CDK2/cyclin	1084:1094	arg1	highlight					1199:1207	highlight	1199:1207	highlight the role of S404 phosphorylation in inducing helical propensity in the region downstream pS404 that is exacerbated by other phosphorylations of PHF-1 epitope at S396 and S400, or O-GlcNAcylation of S400	1199:1410	Using high resolution NMR spectroscopy, we showed that the O-GlcNAc glycosylation reduces phosphorylation of PHF-1 epitope by GSK3β alone or after priming by CDK2/cyclin A. Furthermore, investigations of the impact of PTMs on local conformation performed in small peptides highlight the role of S404 phosphorylation in inducing helical propensity in the region downstream pS404 that is exacerbated by other phosphorylations of PHF-1 epitope at S396 and S400, or O-GlcNAcylation of S400.
34220449	0	38	theme	Tau	139:141	arg1	Self-Assembly					143:155	Tau Self-Assembly	139:155	Tau Self-Assembly Into Fibrillar Aggregates	139:181	Phosphorylation and O-GlcNAcylation of the PHF-1 Epitope of Tau Protein Induce Local Conformational Changes of the C-Terminus and Modulate Tau Self-Assembly Into Fibrillar Aggregates.
34220449	1	39	theme	Tau	239:241	arg1	protein					243:249	the neuronal microtubule-associated Tau protein	203:249	the neuronal microtubule-associated Tau protein	203:249	Phosphorylation of the neuronal microtubule-associated Tau protein plays a critical role in the aggregation process leading to the formation of insoluble intraneuronal fibrils within Alzheimer's disease (AD) brains.
34220449	4	40	theme	O-GlcNAc	814:821	arg1	Tau					831:833	Tau	831:833	Tau	831:833	We here focus on the role of the PHF-1 phospho-epitope of Tau C-terminal domain that is hyperphosphorylated in AD (at pS396/pS404) and encompasses S400 as the major O-GlcNAc site of Tau while two additional O-GlcNAc sites were found in the extreme C-terminus at S412 and S413.
34220449	4	40	theme	O-GlcNAc	814:821	arg1	site					823:826	the major O-GlcNAc site	804:826	the major O-GlcNAc site of Tau	804:833	We here focus on the role of the PHF-1 phospho-epitope of Tau C-terminal domain that is hyperphosphorylated in AD (at pS396/pS404) and encompasses S400 as the major O-GlcNAc site of Tau while two additional O-GlcNAc sites were found in the extreme C-terminus at S412 and S413.
34220449	4	40	theme	O-GlcNAc	814:821	arg1	S400					796:799	S400	796:799	S400	796:799	We here focus on the role of the PHF-1 phospho-epitope of Tau C-terminal domain that is hyperphosphorylated in AD (at pS396/pS404) and encompasses S400 as the major O-GlcNAc site of Tau while two additional O-GlcNAc sites were found in the extreme C-terminus at S412 and S413.
34220449	5	41	theme	downstream	1287:1296	arg1	exacerbated					1312:1322	exacerbated	1312:1322	exacerbated	1312:1322	Using high resolution NMR spectroscopy, we showed that the O-GlcNAc glycosylation reduces phosphorylation of PHF-1 epitope by GSK3β alone or after priming by CDK2/cyclin A. Furthermore, investigations of the impact of PTMs on local conformation performed in small peptides highlight the role of S404 phosphorylation in inducing helical propensity in the region downstream pS404 that is exacerbated by other phosphorylations of PHF-1 epitope at S396 and S400, or O-GlcNAcylation of S400.
34220449	5	41	theme	downstream	1287:1296	arg1	region					1280:1285	the region downstream pS404	1276:1302	the region downstream pS404 that is exacerbated by other phosphorylations of PHF-1 epitope at S396 and S400	1276:1382	Using high resolution NMR spectroscopy, we showed that the O-GlcNAc glycosylation reduces phosphorylation of PHF-1 epitope by GSK3β alone or after priming by CDK2/cyclin A. Furthermore, investigations of the impact of PTMs on local conformation performed in small peptides highlight the role of S404 phosphorylation in inducing helical propensity in the region downstream pS404 that is exacerbated by other phosphorylations of PHF-1 epitope at S396 and S400, or O-GlcNAcylation of S400.
34220449	2	42	theme	other	417:421	arg1	PTMs					456:459	PTMs	456:459	PTMs	456:459	In recent years, other posttranslational modifications (PTMs) have been highlighted in the regulation of Tau (dys)functions.
34220449	2	42	theme	other	417:421	arg1	modifications					441:453	other posttranslational modifications	417:453	other posttranslational modifications (PTMs)	417:460	In recent years, other posttranslational modifications (PTMs) have been highlighted in the regulation of Tau (dys)functions.
34220449	5	43	theme	impact	1134:1139	arg1	investigations					1112:1125	investigations	1112:1125	investigations of the impact of PTMs on local conformation performed in small peptides	1112:1197	Using high resolution NMR spectroscopy, we showed that the O-GlcNAc glycosylation reduces phosphorylation of PHF-1 epitope by GSK3β alone or after priming by CDK2/cyclin A. Furthermore, investigations of the impact of PTMs on local conformation performed in small peptides highlight the role of S404 phosphorylation in inducing helical propensity in the region downstream pS404 that is exacerbated by other phosphorylations of PHF-1 epitope at S396 and S400, or O-GlcNAcylation of S400.
34220449	3	44	link	O-β-linked	547:556	arg1	O-GlcNAcylation					585:599	O-GlcNAcylation	585:599	O-GlcNAcylation	585:599	Among these PTMs, the O-β-linked N-acetylglucosaminylation (O-GlcNAcylation) modulates Tau phosphorylation and aggregation.
34220449	3	44	link	O-β-linked	547:556	arg1	N-acetylglucosaminylation					558:582	the O-β-linked N-acetylglucosaminylation	543:582	the O-β-linked N-acetylglucosaminylation (O-GlcNAcylation)	543:600	Among these PTMs, the O-β-linked N-acetylglucosaminylation (O-GlcNAcylation) modulates Tau phosphorylation and aggregation.
34220449	3	45	theme	Tau	612:614	arg1	phosphorylation					616:630	Tau phosphorylation	612:630	Tau phosphorylation	612:630	Among these PTMs, the O-β-linked N-acetylglucosaminylation (O-GlcNAcylation) modulates Tau phosphorylation and aggregation.
34220449	1	46	theme	protein	243:249	arg1	Phosphorylation					184:198	Phosphorylation	184:198	Phosphorylation of the neuronal microtubule-associated Tau protein	184:249	Phosphorylation of the neuronal microtubule-associated Tau protein plays a critical role in the aggregation process leading to the formation of insoluble intraneuronal fibrils within Alzheimer's disease (AD) brains.
34220449	1	47	theme	insoluble	328:336	arg1	fibrils					352:358	insoluble intraneuronal fibrils	328:358	insoluble intraneuronal fibrils within Alzheimer's disease (AD) brains	328:397	Phosphorylation of the neuronal microtubule-associated Tau protein plays a critical role in the aggregation process leading to the formation of insoluble intraneuronal fibrils within Alzheimer's disease (AD) brains.
34220449	0	48	theme	Tau	60:62	arg1	Protein					64:70	Tau Protein	60:70	Tau Protein	60:70	Phosphorylation and O-GlcNAcylation of the PHF-1 Epitope of Tau Protein Induce Local Conformational Changes of the C-Terminus and Modulate Tau Self-Assembly Into Fibrillar Aggregates.
34220449	6	49	theme	glycosylation	1678:1690	arg1	effect					1668:1673	the effect	1664:1673	the effect of glycosylation	1664:1690	Finally, the role of phosphorylation and O-GlcNAcylation of PHF-1 epitope was probed in in-vitro fibrillization assays in which O-GlcNAcylation slows down the rate of fibrillar assembly while GSK3β phosphorylation stimulates aggregation counteracting the effect of glycosylation.
34220449	6	50	theme	assembly	1590:1597	arg1	rate					1572:1575	the rate	1568:1575	the rate of fibrillar assembly	1568:1597	Finally, the role of phosphorylation and O-GlcNAcylation of PHF-1 epitope was probed in in-vitro fibrillization assays in which O-GlcNAcylation slows down the rate of fibrillar assembly while GSK3β phosphorylation stimulates aggregation counteracting the effect of glycosylation.
34220449	4	51	theme	domain	722:727	arg1	phospho-epitope					688:702	the PHF-1 phospho-epitope	678:702	the PHF-1 phospho-epitope of Tau C-terminal domain that is hyperphosphorylated in AD (at pS396/pS404) and encompasses S400 as the major O-GlcNAc site of Tau while two additional O-GlcNAc sites were found in the extreme C-terminus at S412 and S413	678:923	We here focus on the role of the PHF-1 phospho-epitope of Tau C-terminal domain that is hyperphosphorylated in AD (at pS396/pS404) and encompasses S400 as the major O-GlcNAc site of Tau while two additional O-GlcNAc sites were found in the extreme C-terminus at S412 and S413.
34220449	0	52	theme	Epitope	49:55	arg1	O-GlcNAcylation					20:34	O-GlcNAcylation	20:34	O-GlcNAcylation	20:34	Phosphorylation and O-GlcNAcylation of the PHF-1 Epitope of Tau Protein Induce Local Conformational Changes of the C-Terminus and Modulate Tau Self-Assembly Into Fibrillar Aggregates.
34220449	0	52	theme	Epitope	49:55	arg1	Phosphorylation					0:14	Phosphorylation	0:14	Phosphorylation	0:14	Phosphorylation and O-GlcNAcylation of the PHF-1 Epitope of Tau Protein Induce Local Conformational Changes of the C-Terminus and Modulate Tau Self-Assembly Into Fibrillar Aggregates.
34220449	1	53	theme	intraneuronal	338:350	arg1	fibrils					352:358	insoluble intraneuronal fibrils	328:358	insoluble intraneuronal fibrils within Alzheimer's disease (AD) brains	328:397	Phosphorylation of the neuronal microtubule-associated Tau protein plays a critical role in the aggregation process leading to the formation of insoluble intraneuronal fibrils within Alzheimer's disease (AD) brains.
34220449	5	54	theme	PHF-1	1035:1039	arg1	epitope					1041:1047	PHF-1 epitope	1035:1047	PHF-1 epitope	1035:1047	Using high resolution NMR spectroscopy, we showed that the O-GlcNAc glycosylation reduces phosphorylation of PHF-1 epitope by GSK3β alone or after priming by CDK2/cyclin A. Furthermore, investigations of the impact of PTMs on local conformation performed in small peptides highlight the role of S404 phosphorylation in inducing helical propensity in the region downstream pS404 that is exacerbated by other phosphorylations of PHF-1 epitope at S396 and S400, or O-GlcNAcylation of S400.
34220449	6	55	theme	fibrillar	1580:1588	arg1	assembly					1590:1597	fibrillar assembly	1580:1597	fibrillar assembly	1580:1597	Finally, the role of phosphorylation and O-GlcNAcylation of PHF-1 epitope was probed in in-vitro fibrillization assays in which O-GlcNAcylation slows down the rate of fibrillar assembly while GSK3β phosphorylation stimulates aggregation counteracting the effect of glycosylation.
34220449	4	56	theme	C-terminal	711:720	arg1	domain					722:727	Tau C-terminal domain	707:727	Tau C-terminal domain	707:727	We here focus on the role of the PHF-1 phospho-epitope of Tau C-terminal domain that is hyperphosphorylated in AD (at pS396/pS404) and encompasses S400 as the major O-GlcNAc site of Tau while two additional O-GlcNAc sites were found in the extreme C-terminus at S412 and S413.
34220449	1	57	theme	fibrils	352:358	arg1	formation					315:323	the formation	311:323	the formation of insoluble intraneuronal fibrils within Alzheimer's disease (AD) brains	311:397	Phosphorylation of the neuronal microtubule-associated Tau protein plays a critical role in the aggregation process leading to the formation of insoluble intraneuronal fibrils within Alzheimer's disease (AD) brains.
34220449	5	58	theme	epitope	1041:1047	arg1	phosphorylation					1016:1030	phosphorylation	1016:1030	phosphorylation of PHF-1 epitope	1016:1047	Using high resolution NMR spectroscopy, we showed that the O-GlcNAc glycosylation reduces phosphorylation of PHF-1 epitope by GSK3β alone or after priming by CDK2/cyclin A. Furthermore, investigations of the impact of PTMs on local conformation performed in small peptides highlight the role of S404 phosphorylation in inducing helical propensity in the region downstream pS404 that is exacerbated by other phosphorylations of PHF-1 epitope at S396 and S400, or O-GlcNAcylation of S400.
34220449	5	59	from	phosphorylations	1333:1348	arg1	S400					1379:1382	S400	1379:1382	S400	1379:1382	Using high resolution NMR spectroscopy, we showed that the O-GlcNAc glycosylation reduces phosphorylation of PHF-1 epitope by GSK3β alone or after priming by CDK2/cyclin A. Furthermore, investigations of the impact of PTMs on local conformation performed in small peptides highlight the role of S404 phosphorylation in inducing helical propensity in the region downstream pS404 that is exacerbated by other phosphorylations of PHF-1 epitope at S396 and S400, or O-GlcNAcylation of S400.
34220449	5	59	from	phosphorylations	1333:1348	arg1	S396					1370:1373	S396	1370:1373	S396	1370:1373	Using high resolution NMR spectroscopy, we showed that the O-GlcNAc glycosylation reduces phosphorylation of PHF-1 epitope by GSK3β alone or after priming by CDK2/cyclin A. Furthermore, investigations of the impact of PTMs on local conformation performed in small peptides highlight the role of S404 phosphorylation in inducing helical propensity in the region downstream pS404 that is exacerbated by other phosphorylations of PHF-1 epitope at S396 and S400, or O-GlcNAcylation of S400.
34220449	4	60	theme	major	808:812	arg1	Tau					831:833	Tau	831:833	Tau	831:833	We here focus on the role of the PHF-1 phospho-epitope of Tau C-terminal domain that is hyperphosphorylated in AD (at pS396/pS404) and encompasses S400 as the major O-GlcNAc site of Tau while two additional O-GlcNAc sites were found in the extreme C-terminus at S412 and S413.
34220449	4	60	theme	major	808:812	arg1	site					823:826	the major O-GlcNAc site	804:826	the major O-GlcNAc site of Tau	804:833	We here focus on the role of the PHF-1 phospho-epitope of Tau C-terminal domain that is hyperphosphorylated in AD (at pS396/pS404) and encompasses S400 as the major O-GlcNAc site of Tau while two additional O-GlcNAc sites were found in the extreme C-terminus at S412 and S413.
34220449	4	60	theme	major	808:812	arg1	S400					796:799	S400	796:799	S400	796:799	We here focus on the role of the PHF-1 phospho-epitope of Tau C-terminal domain that is hyperphosphorylated in AD (at pS396/pS404) and encompasses S400 as the major O-GlcNAc site of Tau while two additional O-GlcNAc sites were found in the extreme C-terminus at S412 and S413.
34220449	6	61	theme	epitope	1479:1485	arg1	role					1426:1429	the role	1422:1429	the role of phosphorylation and O-GlcNAcylation of PHF-1 epitope	1422:1485	Finally, the role of phosphorylation and O-GlcNAcylation of PHF-1 epitope was probed in in-vitro fibrillization assays in which O-GlcNAcylation slows down the rate of fibrillar assembly while GSK3β phosphorylation stimulates aggregation counteracting the effect of glycosylation.
34220449	0	62	theme	Fibrillar	162:170	arg1	Aggregates					172:181	Fibrillar Aggregates	162:181	Fibrillar Aggregates	162:181	Phosphorylation and O-GlcNAcylation of the PHF-1 Epitope of Tau Protein Induce Local Conformational Changes of the C-Terminus and Modulate Tau Self-Assembly Into Fibrillar Aggregates.
34220449	5	63	theme	PHF-1	1353:1357	arg1	epitope					1359:1365	PHF-1 epitope	1353:1365	PHF-1 epitope at S396 and S400	1353:1382	Using high resolution NMR spectroscopy, we showed that the O-GlcNAc glycosylation reduces phosphorylation of PHF-1 epitope by GSK3β alone or after priming by CDK2/cyclin A. Furthermore, investigations of the impact of PTMs on local conformation performed in small peptides highlight the role of S404 phosphorylation in inducing helical propensity in the region downstream pS404 that is exacerbated by other phosphorylations of PHF-1 epitope at S396 and S400, or O-GlcNAcylation of S400.
34220449	6	64	theme	PHF-1	1473:1477	arg1	epitope					1479:1485	PHF-1 epitope	1473:1485	PHF-1 epitope	1473:1485	Finally, the role of phosphorylation and O-GlcNAcylation of PHF-1 epitope was probed in in-vitro fibrillization assays in which O-GlcNAcylation slows down the rate of fibrillar assembly while GSK3β phosphorylation stimulates aggregation counteracting the effect of glycosylation.
34220449	0	65	theme	Protein	64:70	arg1	O-GlcNAcylation					20:34	O-GlcNAcylation	20:34	O-GlcNAcylation	20:34	Phosphorylation and O-GlcNAcylation of the PHF-1 Epitope of Tau Protein Induce Local Conformational Changes of the C-Terminus and Modulate Tau Self-Assembly Into Fibrillar Aggregates.
34220449	0	65	theme	Protein	64:70	arg1	Phosphorylation					0:14	Phosphorylation	0:14	Phosphorylation	0:14	Phosphorylation and O-GlcNAcylation of the PHF-1 Epitope of Tau Protein Induce Local Conformational Changes of the C-Terminus and Modulate Tau Self-Assembly Into Fibrillar Aggregates.
34220449	5	66	from	S400	1379:1382	arg1	phosphorylations					1333:1348	other phosphorylations	1327:1348	other phosphorylations of PHF-1 epitope at S396 and S400	1327:1382	Using high resolution NMR spectroscopy, we showed that the O-GlcNAc glycosylation reduces phosphorylation of PHF-1 epitope by GSK3β alone or after priming by CDK2/cyclin A. Furthermore, investigations of the impact of PTMs on local conformation performed in small peptides highlight the role of S404 phosphorylation in inducing helical propensity in the region downstream pS404 that is exacerbated by other phosphorylations of PHF-1 epitope at S396 and S400, or O-GlcNAcylation of S400.
34220449	5	66	from	S400	1379:1382	arg1	epitope					1359:1365	PHF-1 epitope	1353:1365	PHF-1 epitope at S396 and S400	1353:1382	Using high resolution NMR spectroscopy, we showed that the O-GlcNAc glycosylation reduces phosphorylation of PHF-1 epitope by GSK3β alone or after priming by CDK2/cyclin A. Furthermore, investigations of the impact of PTMs on local conformation performed in small peptides highlight the role of S404 phosphorylation in inducing helical propensity in the region downstream pS404 that is exacerbated by other phosphorylations of PHF-1 epitope at S396 and S400, or O-GlcNAcylation of S400.
34220449	5	67	theme	epitope	1359:1365	arg1	phosphorylations					1333:1348	other phosphorylations	1327:1348	other phosphorylations of PHF-1 epitope at S396 and S400	1327:1382	Using high resolution NMR spectroscopy, we showed that the O-GlcNAc glycosylation reduces phosphorylation of PHF-1 epitope by GSK3β alone or after priming by CDK2/cyclin A. Furthermore, investigations of the impact of PTMs on local conformation performed in small peptides highlight the role of S404 phosphorylation in inducing helical propensity in the region downstream pS404 that is exacerbated by other phosphorylations of PHF-1 epitope at S396 and S400, or O-GlcNAcylation of S400.
34220449	4	68	theme	phospho-epitope	688:702	arg1	role					670:673	the role	666:673	the role of the PHF-1 phospho-epitope of Tau C-terminal domain that is hyperphosphorylated in AD (at pS396/pS404) and encompasses S400 as the major O-GlcNAc site of Tau while two additional O-GlcNAc sites were found in the extreme C-terminus at S412 and S413	666:923	We here focus on the role of the PHF-1 phospho-epitope of Tau C-terminal domain that is hyperphosphorylated in AD (at pS396/pS404) and encompasses S400 as the major O-GlcNAc site of Tau while two additional O-GlcNAc sites were found in the extreme C-terminus at S412 and S413.
34220449	4	69	located	found	876:880	arg1	S412					911:914	S412	911:914	S412	911:914	We here focus on the role of the PHF-1 phospho-epitope of Tau C-terminal domain that is hyperphosphorylated in AD (at pS396/pS404) and encompasses S400 as the major O-GlcNAc site of Tau while two additional O-GlcNAc sites were found in the extreme C-terminus at S412 and S413.
34220449	4	69	located	found	876:880	arg2	sites					865:869	two additional O-GlcNAc sites	841:869	two additional O-GlcNAc sites	841:869	We here focus on the role of the PHF-1 phospho-epitope of Tau C-terminal domain that is hyperphosphorylated in AD (at pS396/pS404) and encompasses S400 as the major O-GlcNAc site of Tau while two additional O-GlcNAc sites were found in the extreme C-terminus at S412 and S413.
34220449	4	69	located	found	876:880	arg1	C-terminus					897:906	the extreme C-terminus	885:906	the extreme C-terminus	885:906	We here focus on the role of the PHF-1 phospho-epitope of Tau C-terminal domain that is hyperphosphorylated in AD (at pS396/pS404) and encompasses S400 as the major O-GlcNAc site of Tau while two additional O-GlcNAc sites were found in the extreme C-terminus at S412 and S413.
34220449	4	69	located	found	876:880	arg1	S413					920:923	S413	920:923	S413	920:923	We here focus on the role of the PHF-1 phospho-epitope of Tau C-terminal domain that is hyperphosphorylated in AD (at pS396/pS404) and encompasses S400 as the major O-GlcNAc site of Tau while two additional O-GlcNAc sites were found in the extreme C-terminus at S412 and S413.
34220449	1	70	theme	critical	259:266	arg1	role					268:271	a critical role	257:271	a critical role	257:271	Phosphorylation of the neuronal microtubule-associated Tau protein plays a critical role in the aggregation process leading to the formation of insoluble intraneuronal fibrils within Alzheimer's disease (AD) brains.
34220449	2	71	theme	Tau	505:507	arg1	functions					514:522	Tau (dys)functions	505:522	Tau (dys)functions	505:522	In recent years, other posttranslational modifications (PTMs) have been highlighted in the regulation of Tau (dys)functions.
34220449	5	72	theme	O-GlcNAc	985:992	arg1	glycosylation					994:1006	the O-GlcNAc glycosylation	981:1006	the O-GlcNAc glycosylation	981:1006	Using high resolution NMR spectroscopy, we showed that the O-GlcNAc glycosylation reduces phosphorylation of PHF-1 epitope by GSK3β alone or after priming by CDK2/cyclin A. Furthermore, investigations of the impact of PTMs on local conformation performed in small peptides highlight the role of S404 phosphorylation in inducing helical propensity in the region downstream pS404 that is exacerbated by other phosphorylations of PHF-1 epitope at S396 and S400, or O-GlcNAcylation of S400.
34220449	4	73	theme	PHF-1	682:686	arg1	phospho-epitope					688:702	the PHF-1 phospho-epitope	678:702	the PHF-1 phospho-epitope of Tau C-terminal domain that is hyperphosphorylated in AD (at pS396/pS404) and encompasses S400 as the major O-GlcNAc site of Tau while two additional O-GlcNAc sites were found in the extreme C-terminus at S412 and S413	678:923	We here focus on the role of the PHF-1 phospho-epitope of Tau C-terminal domain that is hyperphosphorylated in AD (at pS396/pS404) and encompasses S400 as the major O-GlcNAc site of Tau while two additional O-GlcNAc sites were found in the extreme C-terminus at S412 and S413.
34220449	6	74	theme	O-GlcNAcylation	1454:1468	arg1	role					1426:1429	the role	1422:1429	the role of phosphorylation and O-GlcNAcylation of PHF-1 epitope	1422:1485	Finally, the role of phosphorylation and O-GlcNAcylation of PHF-1 epitope was probed in in-vitro fibrillization assays in which O-GlcNAcylation slows down the rate of fibrillar assembly while GSK3β phosphorylation stimulates aggregation counteracting the effect of glycosylation.
34220449	0	75	theme	Conformational	85:98	arg1	Changes					100:106	Local Conformational Changes	79:106	Local Conformational Changes of the C-Terminus	79:124	Phosphorylation and O-GlcNAcylation of the PHF-1 Epitope of Tau Protein Induce Local Conformational Changes of the C-Terminus and Modulate Tau Self-Assembly Into Fibrillar Aggregates.
32863226	5	0	theme	eNOS	780:783	arg1	function					785:792	eNOS function	780:792	eNOS function	780:792	In diabetes, dysregulated glucose metabolism has been shown to regulate eNOS function through inhibition of Ser-1177 phosphorylation.
32863226	9	1	theme	O-GlcNAc	1333:1340	arg1	modification					1342:1353	the O-GlcNAc modification	1329:1353	the O-GlcNAc modification of Ser-615	1329:1364	Here we demonstrate a previously unidentified regulatory mechanism of eNOS whereby the O-GlcNAc modification of Ser-615 results in reduced eNOS activity and endothelial dysfunction under conditions of glucose dysregulation.
32863226	9	2	theme	dysregulation	1455:1467	arg1	conditions					1433:1442	conditions	1433:1442	conditions of glucose dysregulation	1433:1467	Here we demonstrate a previously unidentified regulatory mechanism of eNOS whereby the O-GlcNAc modification of Ser-615 results in reduced eNOS activity and endothelial dysfunction under conditions of glucose dysregulation.
32863226	3	3	theme	nitric	485:490	arg1	eNOS					508:511	eNOS	508:511	eNOS	508:511	Nitric Oxide (NO) deficiency is considered a hallmark of IPAH and altered function of endothelial nitric oxide synthase (eNOS), decreases NO production.
32863226	3	3	theme	nitric	485:490	arg1	synthase					498:505	endothelial nitric oxide synthase	473:505	endothelial nitric oxide synthase (eNOS)	473:512	Nitric Oxide (NO) deficiency is considered a hallmark of IPAH and altered function of endothelial nitric oxide synthase (eNOS), decreases NO production.
32863226	2	4	from	resistance	298:307	arg1	lung					316:319	the lung	312:319	the lung	312:319	The increased resistance in the lung and the higher pressures generated result in right heart failure.
32863226	8	5	theme	Functional	1083:1092	arg1	characterization					1094:1109	Functional characterization	1083:1109	Functional characterization of Ser-615	1083:1120	Functional characterization of Ser-615 demonstrated the importance of this residue on the regulation of eNOS activity through control of Ser-1177 phosphorylation.
32863226	3	6	theme	oxide	492:496	arg1	eNOS					508:511	eNOS	508:511	eNOS	508:511	Nitric Oxide (NO) deficiency is considered a hallmark of IPAH and altered function of endothelial nitric oxide synthase (eNOS), decreases NO production.
32863226	3	6	theme	oxide	492:496	arg1	synthase					498:505	endothelial nitric oxide synthase	473:505	endothelial nitric oxide synthase (eNOS)	473:512	Nitric Oxide (NO) deficiency is considered a hallmark of IPAH and altered function of endothelial nitric oxide synthase (eNOS), decreases NO production.
32863226	1	7	theme	vessels	263:269	arg1	narrowing					246:254	a narrowing	244:254	a narrowing of the vessels in the lung	244:281	Idiopathic pulmonary arterial hypertension (IPAH) is a progressive and devastating disease characterized by vascular smooth muscle and endothelial cell proliferation leading to a narrowing of the vessels in the lung.
32863226	8	8	theme	eNOS	1187:1190	arg1	activity					1192:1199	eNOS activity	1187:1199	eNOS activity	1187:1199	Functional characterization of Ser-615 demonstrated the importance of this residue on the regulation of eNOS activity through control of Ser-1177 phosphorylation.
32863226	3	9	theme	Nitric	387:392	arg1	NO					401:402	NO	401:402	NO	401:402	Nitric Oxide (NO) deficiency is considered a hallmark of IPAH and altered function of endothelial nitric oxide synthase (eNOS), decreases NO production.
32863226	3	9	theme	Nitric	387:392	arg1	Oxide					394:398	Nitric Oxide	387:398	Nitric Oxide (NO) deficiency	387:414	Nitric Oxide (NO) deficiency is considered a hallmark of IPAH and altered function of endothelial nitric oxide synthase (eNOS), decreases NO production.
32863226	3	10	theme	synthase	498:505	arg1	function					461:468	altered function	453:468	altered function	453:468	Nitric Oxide (NO) deficiency is considered a hallmark of IPAH and altered function of endothelial nitric oxide synthase (eNOS), decreases NO production.
32863226	2	11	theme	increased	288:296	arg1	resistance					298:307	The increased resistance	284:307	The increased resistance in the lung	284:319	The increased resistance in the lung and the higher pressures generated result in right heart failure.
32863226	4	12	theme	glucose	570:576	arg1	dysregulation					578:590	glucose dysregulation	570:590	glucose dysregulation	570:590	We recently demonstrated that glucose dysregulation results in augmented protein serine/threonine hydroxyl-linked N-Acetyl-glucosamine (O-GlcNAc) modification in IPAH.
32863226	9	13	theme	Ser-615	1358:1364	arg1	modification					1342:1353	the O-GlcNAc modification	1329:1353	the O-GlcNAc modification of Ser-615	1329:1364	Here we demonstrate a previously unidentified regulatory mechanism of eNOS whereby the O-GlcNAc modification of Ser-615 results in reduced eNOS activity and endothelial dysfunction under conditions of glucose dysregulation.
32863226	2	14	from	pressures	336:344	arg1	lung					316:319	the lung	312:319	the lung	312:319	The increased resistance in the lung and the higher pressures generated result in right heart failure.
32863226	1	15	theme	Idiopathic	67:76	arg1	disease					150:156	a progressive and devastating disease	120:156	a progressive and devastating disease characterized by vascular smooth muscle and endothelial cell proliferation leading to a narrowing of the vessels in the lung	120:281	Idiopathic pulmonary arterial hypertension (IPAH) is a progressive and devastating disease characterized by vascular smooth muscle and endothelial cell proliferation leading to a narrowing of the vessels in the lung.
32863226	1	15	theme	Idiopathic	67:76	arg1	IPAH					111:114	IPAH	111:114	IPAH	111:114	Idiopathic pulmonary arterial hypertension (IPAH) is a progressive and devastating disease characterized by vascular smooth muscle and endothelial cell proliferation leading to a narrowing of the vessels in the lung.
32863226	1	15	theme	Idiopathic	67:76	arg1	hypertension					97:108	Idiopathic pulmonary arterial hypertension	67:108	Idiopathic pulmonary arterial hypertension (IPAH)	67:115	Idiopathic pulmonary arterial hypertension (IPAH) is a progressive and devastating disease characterized by vascular smooth muscle and endothelial cell proliferation leading to a narrowing of the vessels in the lung.
32863226	4	16	from	modification	686:697	arg1	IPAH					702:705	IPAH	702:705	IPAH	702:705	We recently demonstrated that glucose dysregulation results in augmented protein serine/threonine hydroxyl-linked N-Acetyl-glucosamine (O-GlcNAc) modification in IPAH.
32863226	4	17	theme	protein	613:619	arg1	modification					686:697	augmented protein serine/threonine hydroxyl-linked N-Acetyl-glucosamine (O-GlcNAc) modification	603:697	augmented protein serine/threonine hydroxyl-linked N-Acetyl-glucosamine (O-GlcNAc) modification in IPAH	603:705	We recently demonstrated that glucose dysregulation results in augmented protein serine/threonine hydroxyl-linked N-Acetyl-glucosamine (O-GlcNAc) modification in IPAH.
32863226	1	18	theme	pulmonary	78:86	arg1	disease					150:156	a progressive and devastating disease	120:156	a progressive and devastating disease characterized by vascular smooth muscle and endothelial cell proliferation leading to a narrowing of the vessels in the lung	120:281	Idiopathic pulmonary arterial hypertension (IPAH) is a progressive and devastating disease characterized by vascular smooth muscle and endothelial cell proliferation leading to a narrowing of the vessels in the lung.
32863226	1	18	theme	pulmonary	78:86	arg1	IPAH					111:114	IPAH	111:114	IPAH	111:114	Idiopathic pulmonary arterial hypertension (IPAH) is a progressive and devastating disease characterized by vascular smooth muscle and endothelial cell proliferation leading to a narrowing of the vessels in the lung.
32863226	1	18	theme	pulmonary	78:86	arg1	hypertension					97:108	Idiopathic pulmonary arterial hypertension	67:108	Idiopathic pulmonary arterial hypertension (IPAH)	67:115	Idiopathic pulmonary arterial hypertension (IPAH) is a progressive and devastating disease characterized by vascular smooth muscle and endothelial cell proliferation leading to a narrowing of the vessels in the lung.
32863226	1	19	theme	vascular	175:182	arg1	muscle					191:196	vascular smooth muscle	175:196	vascular smooth muscle	175:196	Idiopathic pulmonary arterial hypertension (IPAH) is a progressive and devastating disease characterized by vascular smooth muscle and endothelial cell proliferation leading to a narrowing of the vessels in the lung.
32863226	5	20	theme	Ser-1177	816:823	arg1	phosphorylation					825:839	Ser-1177 phosphorylation	816:839	Ser-1177 phosphorylation	816:839	In diabetes, dysregulated glucose metabolism has been shown to regulate eNOS function through inhibition of Ser-1177 phosphorylation.
32863226	9	21	theme	glucose	1447:1453	arg1	dysregulation					1455:1467	glucose dysregulation	1447:1467	glucose dysregulation	1447:1467	Here we demonstrate a previously unidentified regulatory mechanism of eNOS whereby the O-GlcNAc modification of Ser-615 results in reduced eNOS activity and endothelial dysfunction under conditions of glucose dysregulation.
32863226	1	22	theme	arterial	88:95	arg1	disease					150:156	a progressive and devastating disease	120:156	a progressive and devastating disease characterized by vascular smooth muscle and endothelial cell proliferation leading to a narrowing of the vessels in the lung	120:281	Idiopathic pulmonary arterial hypertension (IPAH) is a progressive and devastating disease characterized by vascular smooth muscle and endothelial cell proliferation leading to a narrowing of the vessels in the lung.
32863226	1	22	theme	arterial	88:95	arg1	IPAH					111:114	IPAH	111:114	IPAH	111:114	Idiopathic pulmonary arterial hypertension (IPAH) is a progressive and devastating disease characterized by vascular smooth muscle and endothelial cell proliferation leading to a narrowing of the vessels in the lung.
32863226	1	22	theme	arterial	88:95	arg1	hypertension					97:108	Idiopathic pulmonary arterial hypertension	67:108	Idiopathic pulmonary arterial hypertension (IPAH)	67:115	Idiopathic pulmonary arterial hypertension (IPAH) is a progressive and devastating disease characterized by vascular smooth muscle and endothelial cell proliferation leading to a narrowing of the vessels in the lung.
32863226	1	23	theme	smooth	184:189	arg1	muscle					191:196	vascular smooth muscle	175:196	vascular smooth muscle	175:196	Idiopathic pulmonary arterial hypertension (IPAH) is a progressive and devastating disease characterized by vascular smooth muscle and endothelial cell proliferation leading to a narrowing of the vessels in the lung.
32863226	0	24	theme	O-GlcNAc	9:16	arg1	modification					18:29	Specific O-GlcNAc modification	0:29	Specific O-GlcNAc modification at Ser-615	0:40	Specific O-GlcNAc modification at Ser-615 modulates eNOS function.
32863226	0	25	from	Ser-615	34:40	arg1	modification					18:29	Specific O-GlcNAc modification	0:29	Specific O-GlcNAc modification at Ser-615	0:40	Specific O-GlcNAc modification at Ser-615 modulates eNOS function.
32863226	1	26	from	lung	278:281	arg1	narrowing					246:254	a narrowing	244:254	a narrowing of the vessels in the lung	244:281	Idiopathic pulmonary arterial hypertension (IPAH) is a progressive and devastating disease characterized by vascular smooth muscle and endothelial cell proliferation leading to a narrowing of the vessels in the lung.
32863226	7	27	theme	eNOS	1064:1067	arg1	dimerization					1069:1080	reduced eNOS dimerization	1056:1080	reduced eNOS dimerization	1056:1080	Here we show that increased protein O-GlcNAc occurs on eNOS in PAH and Ser-615 appears to be a novel site of O-GlcNAc modification resulting in reduced eNOS dimerization.
32863226	0	28	theme	Specific	0:7	arg1	modification					18:29	Specific O-GlcNAc modification	0:29	Specific O-GlcNAc modification at Ser-615	0:40	Specific O-GlcNAc modification at Ser-615 modulates eNOS function.
32863226	9	29	theme	eNOS	1385:1388	arg1	activity					1390:1397	reduced eNOS activity	1377:1397	reduced eNOS activity	1377:1397	Here we demonstrate a previously unidentified regulatory mechanism of eNOS whereby the O-GlcNAc modification of Ser-615 results in reduced eNOS activity and endothelial dysfunction under conditions of glucose dysregulation.
32863226	2	30	theme	heart	372:376	arg1	failure					378:384	right heart failure	366:384	right heart failure	366:384	The increased resistance in the lung and the higher pressures generated result in right heart failure.
32863226	8	31	theme	phosphorylation	1229:1243	arg1	control					1209:1215	control	1209:1215	control of Ser-1177 phosphorylation	1209:1243	Functional characterization of Ser-615 demonstrated the importance of this residue on the regulation of eNOS activity through control of Ser-1177 phosphorylation.
32863226	8	32	theme	activity	1192:1199	arg1	regulation					1173:1182	the regulation	1169:1182	the regulation of eNOS activity through control of Ser-1177 phosphorylation	1169:1243	Functional characterization of Ser-615 demonstrated the importance of this residue on the regulation of eNOS activity through control of Ser-1177 phosphorylation.
32863226	3	33	theme	NO	525:526	arg1	production					528:537	NO production	525:537	NO production	525:537	Nitric Oxide (NO) deficiency is considered a hallmark of IPAH and altered function of endothelial nitric oxide synthase (eNOS), decreases NO production.
32863226	1	34	theme	endothelial	202:212	arg1	proliferation					219:231	endothelial cell proliferation	202:231	endothelial cell proliferation	202:231	Idiopathic pulmonary arterial hypertension (IPAH) is a progressive and devastating disease characterized by vascular smooth muscle and endothelial cell proliferation leading to a narrowing of the vessels in the lung.
32863226	8	35	theme	Ser-1177	1220:1227	arg1	phosphorylation					1229:1243	Ser-1177 phosphorylation	1220:1243	Ser-1177 phosphorylation	1220:1243	Functional characterization of Ser-615 demonstrated the importance of this residue on the regulation of eNOS activity through control of Ser-1177 phosphorylation.
32863226	6	36	dep	O-GlcNAc	868:875	arg1	function					886:893	function	886:893	function	886:893	However, the link between O-GlcNAc and eNOS function remains unknown.
32863226	1	37	theme	cell	214:217	arg1	proliferation					219:231	endothelial cell proliferation	202:231	endothelial cell proliferation	202:231	Idiopathic pulmonary arterial hypertension (IPAH) is a progressive and devastating disease characterized by vascular smooth muscle and endothelial cell proliferation leading to a narrowing of the vessels in the lung.
32863226	3	38	theme	endothelial	473:483	arg1	eNOS					508:511	eNOS	508:511	eNOS	508:511	Nitric Oxide (NO) deficiency is considered a hallmark of IPAH and altered function of endothelial nitric oxide synthase (eNOS), decreases NO production.
32863226	3	38	theme	endothelial	473:483	arg1	synthase					498:505	endothelial nitric oxide synthase	473:505	endothelial nitric oxide synthase (eNOS)	473:512	Nitric Oxide (NO) deficiency is considered a hallmark of IPAH and altered function of endothelial nitric oxide synthase (eNOS), decreases NO production.
32863226	5	39	theme	dysregulated	721:732	arg1	metabolism					742:751	dysregulated glucose metabolism	721:751	dysregulated glucose metabolism	721:751	In diabetes, dysregulated glucose metabolism has been shown to regulate eNOS function through inhibition of Ser-1177 phosphorylation.
32863226	5	40	theme	glucose	734:740	arg1	metabolism					742:751	dysregulated glucose metabolism	721:751	dysregulated glucose metabolism	721:751	In diabetes, dysregulated glucose metabolism has been shown to regulate eNOS function through inhibition of Ser-1177 phosphorylation.
32863226	4	41	theme	N-Acetyl-glucosamine	654:673	arg1	modification					686:697	augmented protein serine/threonine hydroxyl-linked N-Acetyl-glucosamine (O-GlcNAc) modification	603:697	augmented protein serine/threonine hydroxyl-linked N-Acetyl-glucosamine (O-GlcNAc) modification in IPAH	603:705	We recently demonstrated that glucose dysregulation results in augmented protein serine/threonine hydroxyl-linked N-Acetyl-glucosamine (O-GlcNAc) modification in IPAH.
32863226	4	42	theme	O-GlcNAc	676:683	arg1	modification					686:697	augmented protein serine/threonine hydroxyl-linked N-Acetyl-glucosamine (O-GlcNAc) modification	603:697	augmented protein serine/threonine hydroxyl-linked N-Acetyl-glucosamine (O-GlcNAc) modification in IPAH	603:705	We recently demonstrated that glucose dysregulation results in augmented protein serine/threonine hydroxyl-linked N-Acetyl-glucosamine (O-GlcNAc) modification in IPAH.
32863226	1	43	from	vessels	263:269	arg1	lung					278:281	the lung	274:281	the lung	274:281	Idiopathic pulmonary arterial hypertension (IPAH) is a progressive and devastating disease characterized by vascular smooth muscle and endothelial cell proliferation leading to a narrowing of the vessels in the lung.
32863226	9	44	theme	unidentified	1279:1290	arg1	mechanism					1303:1311	a previously unidentified regulatory mechanism	1266:1311	a previously unidentified regulatory mechanism of eNOS whereby the O-GlcNAc modification of Ser-615 results in reduced eNOS activity and endothelial dysfunction under conditions of glucose dysregulation	1266:1467	Here we demonstrate a previously unidentified regulatory mechanism of eNOS whereby the O-GlcNAc modification of Ser-615 results in reduced eNOS activity and endothelial dysfunction under conditions of glucose dysregulation.
32863226	4	45	theme	hydroxyl-linked	638:652	arg1	modification					686:697	augmented protein serine/threonine hydroxyl-linked N-Acetyl-glucosamine (O-GlcNAc) modification	603:697	augmented protein serine/threonine hydroxyl-linked N-Acetyl-glucosamine (O-GlcNAc) modification in IPAH	603:705	We recently demonstrated that glucose dysregulation results in augmented protein serine/threonine hydroxyl-linked N-Acetyl-glucosamine (O-GlcNAc) modification in IPAH.
32863226	3	46	theme	Oxide	394:398	arg1	deficiency					405:414	Nitric Oxide (NO) deficiency	387:414	Nitric Oxide (NO) deficiency	387:414	Nitric Oxide (NO) deficiency is considered a hallmark of IPAH and altered function of endothelial nitric oxide synthase (eNOS), decreases NO production.
32863226	1	47	from	narrowing	246:254	arg1	lung					278:281	the lung	274:281	the lung	274:281	Idiopathic pulmonary arterial hypertension (IPAH) is a progressive and devastating disease characterized by vascular smooth muscle and endothelial cell proliferation leading to a narrowing of the vessels in the lung.
32863226	9	48	theme	regulatory	1292:1301	arg1	mechanism					1303:1311	a previously unidentified regulatory mechanism	1266:1311	a previously unidentified regulatory mechanism of eNOS whereby the O-GlcNAc modification of Ser-615 results in reduced eNOS activity and endothelial dysfunction under conditions of glucose dysregulation	1266:1467	Here we demonstrate a previously unidentified regulatory mechanism of eNOS whereby the O-GlcNAc modification of Ser-615 results in reduced eNOS activity and endothelial dysfunction under conditions of glucose dysregulation.
32863226	7	49	theme	O-GlcNAc	1021:1028	arg1	modification					1030:1041	O-GlcNAc modification	1021:1041	O-GlcNAc modification resulting in reduced eNOS dimerization	1021:1080	Here we show that increased protein O-GlcNAc occurs on eNOS in PAH and Ser-615 appears to be a novel site of O-GlcNAc modification resulting in reduced eNOS dimerization.
32863226	0	50	theme	eNOS	52:55	arg1	function					57:64	eNOS function	52:64	eNOS function	52:64	Specific O-GlcNAc modification at Ser-615 modulates eNOS function.
32863226	7	51	theme	reduced	1056:1062	arg1	dimerization					1069:1080	reduced eNOS dimerization	1056:1080	reduced eNOS dimerization	1056:1080	Here we show that increased protein O-GlcNAc occurs on eNOS in PAH and Ser-615 appears to be a novel site of O-GlcNAc modification resulting in reduced eNOS dimerization.
32863226	7	52	theme	novel	1007:1011	arg1	site					1013:1016	a novel site	1005:1016	a novel site of O-GlcNAc modification resulting in reduced eNOS dimerization	1005:1080	Here we show that increased protein O-GlcNAc occurs on eNOS in PAH and Ser-615 appears to be a novel site of O-GlcNAc modification resulting in reduced eNOS dimerization.
32863226	7	52	theme	novel	1007:1011	arg1	modification					1030:1041	O-GlcNAc modification	1021:1041	O-GlcNAc modification resulting in reduced eNOS dimerization	1021:1080	Here we show that increased protein O-GlcNAc occurs on eNOS in PAH and Ser-615 appears to be a novel site of O-GlcNAc modification resulting in reduced eNOS dimerization.
32863226	7	52	theme	novel	1007:1011	arg1	Ser-615					983:989	Ser-615	983:989	Ser-615	983:989	Here we show that increased protein O-GlcNAc occurs on eNOS in PAH and Ser-615 appears to be a novel site of O-GlcNAc modification resulting in reduced eNOS dimerization.
32863226	2	53	theme	higher	329:334	arg1	pressures					336:344	the higher pressures	325:344	the higher pressures generated	325:354	The increased resistance in the lung and the higher pressures generated result in right heart failure.
32863226	7	54	theme	increased	930:938	arg1	O-GlcNAc					948:955	increased protein O-GlcNAc	930:955	increased protein O-GlcNAc	930:955	Here we show that increased protein O-GlcNAc occurs on eNOS in PAH and Ser-615 appears to be a novel site of O-GlcNAc modification resulting in reduced eNOS dimerization.
32863226	7	55	theme	modification	1030:1041	arg1	site					1013:1016	a novel site	1005:1016	a novel site of O-GlcNAc modification resulting in reduced eNOS dimerization	1005:1080	Here we show that increased protein O-GlcNAc occurs on eNOS in PAH and Ser-615 appears to be a novel site of O-GlcNAc modification resulting in reduced eNOS dimerization.
32863226	7	55	theme	modification	1030:1041	arg1	modification					1030:1041	O-GlcNAc modification	1021:1041	O-GlcNAc modification resulting in reduced eNOS dimerization	1021:1080	Here we show that increased protein O-GlcNAc occurs on eNOS in PAH and Ser-615 appears to be a novel site of O-GlcNAc modification resulting in reduced eNOS dimerization.
32863226	7	55	theme	modification	1030:1041	arg1	Ser-615					983:989	Ser-615	983:989	Ser-615	983:989	Here we show that increased protein O-GlcNAc occurs on eNOS in PAH and Ser-615 appears to be a novel site of O-GlcNAc modification resulting in reduced eNOS dimerization.
32863226	1	56	theme	devastating	138:148	arg1	disease					150:156	a progressive and devastating disease	120:156	a progressive and devastating disease characterized by vascular smooth muscle and endothelial cell proliferation leading to a narrowing of the vessels in the lung	120:281	Idiopathic pulmonary arterial hypertension (IPAH) is a progressive and devastating disease characterized by vascular smooth muscle and endothelial cell proliferation leading to a narrowing of the vessels in the lung.
32863226	1	56	theme	devastating	138:148	arg1	hypertension					97:108	Idiopathic pulmonary arterial hypertension	67:108	Idiopathic pulmonary arterial hypertension (IPAH)	67:115	Idiopathic pulmonary arterial hypertension (IPAH) is a progressive and devastating disease characterized by vascular smooth muscle and endothelial cell proliferation leading to a narrowing of the vessels in the lung.
32863226	9	57	theme	endothelial	1403:1413	arg1	dysfunction					1415:1425	endothelial dysfunction	1403:1425	endothelial dysfunction	1403:1425	Here we demonstrate a previously unidentified regulatory mechanism of eNOS whereby the O-GlcNAc modification of Ser-615 results in reduced eNOS activity and endothelial dysfunction under conditions of glucose dysregulation.
32863226	1	58	theme	progressive	122:132	arg1	disease					150:156	a progressive and devastating disease	120:156	a progressive and devastating disease characterized by vascular smooth muscle and endothelial cell proliferation leading to a narrowing of the vessels in the lung	120:281	Idiopathic pulmonary arterial hypertension (IPAH) is a progressive and devastating disease characterized by vascular smooth muscle and endothelial cell proliferation leading to a narrowing of the vessels in the lung.
32863226	1	58	theme	progressive	122:132	arg1	hypertension					97:108	Idiopathic pulmonary arterial hypertension	67:108	Idiopathic pulmonary arterial hypertension (IPAH)	67:115	Idiopathic pulmonary arterial hypertension (IPAH) is a progressive and devastating disease characterized by vascular smooth muscle and endothelial cell proliferation leading to a narrowing of the vessels in the lung.
32863226	7	59	theme	protein	940:946	arg1	O-GlcNAc					948:955	increased protein O-GlcNAc	930:955	increased protein O-GlcNAc	930:955	Here we show that increased protein O-GlcNAc occurs on eNOS in PAH and Ser-615 appears to be a novel site of O-GlcNAc modification resulting in reduced eNOS dimerization.
32863226	8	60	from	importance	1139:1148	arg1	regulation					1173:1182	the regulation	1169:1182	the regulation of eNOS activity through control of Ser-1177 phosphorylation	1169:1243	Functional characterization of Ser-615 demonstrated the importance of this residue on the regulation of eNOS activity through control of Ser-1177 phosphorylation.
32863226	9	61	theme	eNOS	1316:1319	arg1	mechanism					1303:1311	a previously unidentified regulatory mechanism	1266:1311	a previously unidentified regulatory mechanism of eNOS whereby the O-GlcNAc modification of Ser-615 results in reduced eNOS activity and endothelial dysfunction under conditions of glucose dysregulation	1266:1467	Here we demonstrate a previously unidentified regulatory mechanism of eNOS whereby the O-GlcNAc modification of Ser-615 results in reduced eNOS activity and endothelial dysfunction under conditions of glucose dysregulation.
32863226	4	62	link	hydroxyl-linked	638:652	arg1	modification					686:697	augmented protein serine/threonine hydroxyl-linked N-Acetyl-glucosamine (O-GlcNAc) modification	603:697	augmented protein serine/threonine hydroxyl-linked N-Acetyl-glucosamine (O-GlcNAc) modification in IPAH	603:705	We recently demonstrated that glucose dysregulation results in augmented protein serine/threonine hydroxyl-linked N-Acetyl-glucosamine (O-GlcNAc) modification in IPAH.
32863226	3	63	theme	altered	453:459	arg1	function					461:468	altered function	453:468	altered function	453:468	Nitric Oxide (NO) deficiency is considered a hallmark of IPAH and altered function of endothelial nitric oxide synthase (eNOS), decreases NO production.
32863226	9	64	theme	reduced	1377:1383	arg1	activity					1390:1397	reduced eNOS activity	1377:1397	reduced eNOS activity	1377:1397	Here we demonstrate a previously unidentified regulatory mechanism of eNOS whereby the O-GlcNAc modification of Ser-615 results in reduced eNOS activity and endothelial dysfunction under conditions of glucose dysregulation.
32863226	3	65	theme	IPAH	444:447	arg1	hallmark					432:439	a hallmark	430:439	a hallmark of IPAH	430:447	Nitric Oxide (NO) deficiency is considered a hallmark of IPAH and altered function of endothelial nitric oxide synthase (eNOS), decreases NO production.
32863226	2	66	theme	right	366:370	arg1	failure					378:384	right heart failure	366:384	right heart failure	366:384	The increased resistance in the lung and the higher pressures generated result in right heart failure.
32863226	4	67	theme	augmented	603:611	arg1	modification					686:697	augmented protein serine/threonine hydroxyl-linked N-Acetyl-glucosamine (O-GlcNAc) modification	603:697	augmented protein serine/threonine hydroxyl-linked N-Acetyl-glucosamine (O-GlcNAc) modification in IPAH	603:705	We recently demonstrated that glucose dysregulation results in augmented protein serine/threonine hydroxyl-linked N-Acetyl-glucosamine (O-GlcNAc) modification in IPAH.
32863226	8	68	theme	residue	1158:1164	arg1	importance					1139:1148	the importance	1135:1148	the importance of this residue on the regulation of eNOS activity through control of Ser-1177 phosphorylation	1135:1243	Functional characterization of Ser-615 demonstrated the importance of this residue on the regulation of eNOS activity through control of Ser-1177 phosphorylation.
32863226	4	69	theme	serine/threonine	621:636	arg1	modification					686:697	augmented protein serine/threonine hydroxyl-linked N-Acetyl-glucosamine (O-GlcNAc) modification	603:697	augmented protein serine/threonine hydroxyl-linked N-Acetyl-glucosamine (O-GlcNAc) modification in IPAH	603:705	We recently demonstrated that glucose dysregulation results in augmented protein serine/threonine hydroxyl-linked N-Acetyl-glucosamine (O-GlcNAc) modification in IPAH.
32863226	5	70	theme	phosphorylation	825:839	arg1	inhibition					802:811	inhibition	802:811	inhibition of Ser-1177 phosphorylation	802:839	In diabetes, dysregulated glucose metabolism has been shown to regulate eNOS function through inhibition of Ser-1177 phosphorylation.
32863226	8	71	theme	Ser-615	1114:1120	arg1	characterization					1094:1109	Functional characterization	1083:1109	Functional characterization of Ser-615	1083:1120	Functional characterization of Ser-615 demonstrated the importance of this residue on the regulation of eNOS activity through control of Ser-1177 phosphorylation.
22629392	4	0	theme	endogenous	747:756	arg1	subpopulations					794:807	endogenous glycosylated and phosphorylated Akt subpopulations	747:807	endogenous glycosylated and phosphorylated Akt subpopulations	747:807	Such an easy method enabled us to visualize endogenous glycosylated and phosphorylated Akt subpopulations in parallel and observed the inhibitory effect of Akt O-GlcNAcylations on its phosphorylation.
22629392	4	1	theme	inhibitory	838:847	arg1	effect					849:854	the inhibitory effect	834:854	the inhibitory effect of Akt O-GlcNAcylations on its phosphorylation	834:901	Such an easy method enabled us to visualize endogenous glycosylated and phosphorylated Akt subpopulations in parallel and observed the inhibitory effect of Akt O-GlcNAcylations on its phosphorylation.
22629392	4	2	from	effect	849:854	arg1	phosphorylation					887:901	its phosphorylation	883:901	its phosphorylation	883:901	Such an easy method enabled us to visualize endogenous glycosylated and phosphorylated Akt subpopulations in parallel and observed the inhibitory effect of Akt O-GlcNAcylations on its phosphorylation.
22629392	2	3	theme	Akt	382:384	arg1	activity					386:393	Akt activity	382:393	Akt activity	382:393	In addition to the well documented phosphorylations that control Akt activity, Akt also undergoes O-GlcNAcylation, but the interplay between these two modifications and the biological significance remain unclear, largely due to the technique challenges.
22629392	1	4	link	O-linked	89:96	arg1	types					206:210	as two important types	189:210	as two important types of post-translational modifications	189:246	O-linked N-acetylglucosamine glycosylations (O-GlcNAc) and O-linked phosphorylations (O-phosphate), as two important types of post-translational modifications, often occur on the same protein and bear a reciprocal relationship.
22629392	1	4	link	O-linked	89:96	arg1	O-GlcNAc					134:141	O-GlcNAc	134:141	O-GlcNAc	134:141	O-linked N-acetylglucosamine glycosylations (O-GlcNAc) and O-linked phosphorylations (O-phosphate), as two important types of post-translational modifications, often occur on the same protein and bear a reciprocal relationship.
22629392	1	4	link	O-linked	89:96	arg1	glycosylations					118:131	O-linked N-acetylglucosamine glycosylations	89:131	O-linked N-acetylglucosamine glycosylations (O-GlcNAc)	89:142	O-linked N-acetylglucosamine glycosylations (O-GlcNAc) and O-linked phosphorylations (O-phosphate), as two important types of post-translational modifications, often occur on the same protein and bear a reciprocal relationship.
22629392	3	5	theme	subsequent	663:672	arg1	immunodetection					686:700	subsequent O-phosphate immunodetection	663:700	subsequent O-phosphate immunodetection	663:700	Here, we applied a two-step analytic approach composed of the O-GlcNAc immunoenrichment and subsequent O-phosphate immunodetection.
22629392	5	6	from	Thr	1007:1009	arg1	O-GlcNAcylations					987:1002	O-GlcNAcylations	987:1002	O-GlcNAcylations at Thr 305 and Thr 312	987:1025	Further studies utilizing mass spectrometry and mutagenesis approaches showed that O-GlcNAcylations at Thr 305 and Thr 312 inhibited Akt phosphorylation at Thr 308 via disrupting the interaction between Akt and PDK1.
22629392	2	7	theme	technique	549:557	arg1	challenges					559:568	the technique challenges	545:568	the technique challenges	545:568	In addition to the well documented phosphorylations that control Akt activity, Akt also undergoes O-GlcNAcylation, but the interplay between these two modifications and the biological significance remain unclear, largely due to the technique challenges.
22629392	6	8	theme	cell	1241:1244	arg1	proliferation					1246:1258	suppressed cell proliferation	1230:1258	suppressed cell proliferation	1230:1258	The impaired Akt activation in turn resulted in the compromised biological functions of Akt, as evidenced by suppressed cell proliferation and migration capabilities.
22629392	6	9	theme	biological	1185:1194	arg1	functions					1196:1204	the compromised biological functions	1169:1204	the compromised biological functions of Akt	1169:1211	The impaired Akt activation in turn resulted in the compromised biological functions of Akt, as evidenced by suppressed cell proliferation and migration capabilities.
22629392	4	10	theme	phosphorylated	775:788	arg1	subpopulations					794:807	endogenous glycosylated and phosphorylated Akt subpopulations	747:807	endogenous glycosylated and phosphorylated Akt subpopulations	747:807	Such an easy method enabled us to visualize endogenous glycosylated and phosphorylated Akt subpopulations in parallel and observed the inhibitory effect of Akt O-GlcNAcylations on its phosphorylation.
22629392	7	11	theme	new	1432:1434	arg1	modification					1447:1458	a new regulatory modification	1430:1458	a new regulatory modification for Akt signaling	1430:1476	Together, this study revealed an extensive crosstalk between O-GlcNAcylations and phosphorylations of Akt and demonstrated O-GlcNAcylation as a new regulatory modification for Akt signaling.
22629392	7	11	theme	new	1432:1434	arg1	O-GlcNAcylation					1411:1425	O-GlcNAcylation	1411:1425	O-GlcNAcylation	1411:1425	Together, this study revealed an extensive crosstalk between O-GlcNAcylations and phosphorylations of Akt and demonstrated O-GlcNAcylation as a new regulatory modification for Akt signaling.
22629392	1	12	theme	O-linked	89:96	arg1	types					206:210	as two important types	189:210	as two important types of post-translational modifications	189:246	O-linked N-acetylglucosamine glycosylations (O-GlcNAc) and O-linked phosphorylations (O-phosphate), as two important types of post-translational modifications, often occur on the same protein and bear a reciprocal relationship.
22629392	1	12	theme	O-linked	89:96	arg1	O-GlcNAc					134:141	O-GlcNAc	134:141	O-GlcNAc	134:141	O-linked N-acetylglucosamine glycosylations (O-GlcNAc) and O-linked phosphorylations (O-phosphate), as two important types of post-translational modifications, often occur on the same protein and bear a reciprocal relationship.
22629392	1	12	theme	O-linked	89:96	arg1	glycosylations					118:131	O-linked N-acetylglucosamine glycosylations	89:131	O-linked N-acetylglucosamine glycosylations (O-GlcNAc)	89:142	O-linked N-acetylglucosamine glycosylations (O-GlcNAc) and O-linked phosphorylations (O-phosphate), as two important types of post-translational modifications, often occur on the same protein and bear a reciprocal relationship.
22629392	7	13	theme	regulatory	1436:1445	arg1	modification					1447:1458	a new regulatory modification	1430:1458	a new regulatory modification for Akt signaling	1430:1476	Together, this study revealed an extensive crosstalk between O-GlcNAcylations and phosphorylations of Akt and demonstrated O-GlcNAcylation as a new regulatory modification for Akt signaling.
22629392	7	13	theme	regulatory	1436:1445	arg1	O-GlcNAcylation					1411:1425	O-GlcNAcylation	1411:1425	O-GlcNAcylation	1411:1425	Together, this study revealed an extensive crosstalk between O-GlcNAcylations and phosphorylations of Akt and demonstrated O-GlcNAcylation as a new regulatory modification for Akt signaling.
22629392	4	14	theme	easy	711:714	arg1	method					716:721	Such an easy method	703:721	Such an easy method	703:721	Such an easy method enabled us to visualize endogenous glycosylated and phosphorylated Akt subpopulations in parallel and observed the inhibitory effect of Akt O-GlcNAcylations on its phosphorylation.
22629392	5	15	from	Thr	1019:1021	arg1	O-GlcNAcylations					987:1002	O-GlcNAcylations	987:1002	O-GlcNAcylations at Thr 305 and Thr 312	987:1025	Further studies utilizing mass spectrometry and mutagenesis approaches showed that O-GlcNAcylations at Thr 305 and Thr 312 inhibited Akt phosphorylation at Thr 308 via disrupting the interaction between Akt and PDK1.
22629392	1	16	theme	N-acetylglucosamine	98:116	arg1	types					206:210	as two important types	189:210	as two important types of post-translational modifications	189:246	O-linked N-acetylglucosamine glycosylations (O-GlcNAc) and O-linked phosphorylations (O-phosphate), as two important types of post-translational modifications, often occur on the same protein and bear a reciprocal relationship.
22629392	1	16	theme	N-acetylglucosamine	98:116	arg1	O-GlcNAc					134:141	O-GlcNAc	134:141	O-GlcNAc	134:141	O-linked N-acetylglucosamine glycosylations (O-GlcNAc) and O-linked phosphorylations (O-phosphate), as two important types of post-translational modifications, often occur on the same protein and bear a reciprocal relationship.
22629392	1	16	theme	N-acetylglucosamine	98:116	arg1	glycosylations					118:131	O-linked N-acetylglucosamine glycosylations	89:131	O-linked N-acetylglucosamine glycosylations (O-GlcNAc)	89:142	O-linked N-acetylglucosamine glycosylations (O-GlcNAc) and O-linked phosphorylations (O-phosphate), as two important types of post-translational modifications, often occur on the same protein and bear a reciprocal relationship.
22629392	1	17	theme	important	196:204	arg1	types					206:210	as two important types	189:210	as two important types of post-translational modifications	189:246	O-linked N-acetylglucosamine glycosylations (O-GlcNAc) and O-linked phosphorylations (O-phosphate), as two important types of post-translational modifications, often occur on the same protein and bear a reciprocal relationship.
22629392	1	17	theme	important	196:204	arg1	glycosylations					118:131	O-linked N-acetylglucosamine glycosylations	89:131	O-linked N-acetylglucosamine glycosylations (O-GlcNAc)	89:142	O-linked N-acetylglucosamine glycosylations (O-GlcNAc) and O-linked phosphorylations (O-phosphate), as two important types of post-translational modifications, often occur on the same protein and bear a reciprocal relationship.
22629392	2	18	dep	phosphorylations	352:367	arg1	addition					320:327	addition	320:327	addition	320:327	In addition to the well documented phosphorylations that control Akt activity, Akt also undergoes O-GlcNAcylation, but the interplay between these two modifications and the biological significance remain unclear, largely due to the technique challenges.
22629392	7	19	theme	Akt	1390:1392	arg1	phosphorylations					1370:1385	phosphorylations	1370:1385	phosphorylations	1370:1385	Together, this study revealed an extensive crosstalk between O-GlcNAcylations and phosphorylations of Akt and demonstrated O-GlcNAcylation as a new regulatory modification for Akt signaling.
22629392	7	19	theme	Akt	1390:1392	arg1	O-GlcNAcylations					1349:1364	O-GlcNAcylations	1349:1364	O-GlcNAcylations	1349:1364	Together, this study revealed an extensive crosstalk between O-GlcNAcylations and phosphorylations of Akt and demonstrated O-GlcNAcylation as a new regulatory modification for Akt signaling.
22629392	6	20	dep	proliferation	1246:1258	arg1	capabilities					1274:1285	capabilities	1274:1285	capabilities	1274:1285	The impaired Akt activation in turn resulted in the compromised biological functions of Akt, as evidenced by suppressed cell proliferation and migration capabilities.
22629392	0	21	theme	Extensive	0:8	arg1	crosstalk					10:18	Extensive crosstalk	0:18	Extensive crosstalk between O-GlcNAcylation and phosphorylation	0:62	Extensive crosstalk between O-GlcNAcylation and phosphorylation regulates Akt signaling.
22629392	1	22	theme	reciprocal	292:301	arg1	relationship					303:314	a reciprocal relationship	290:314	a reciprocal relationship	290:314	O-linked N-acetylglucosamine glycosylations (O-GlcNAc) and O-linked phosphorylations (O-phosphate), as two important types of post-translational modifications, often occur on the same protein and bear a reciprocal relationship.
22629392	3	23	theme	analytic	599:606	arg1	approach					608:615	a two-step analytic approach	588:615	a two-step analytic approach composed of the O-GlcNAc immunoenrichment and subsequent O-phosphate immunodetection	588:700	Here, we applied a two-step analytic approach composed of the O-GlcNAc immunoenrichment and subsequent O-phosphate immunodetection.
22629392	4	24	gly	glycosylated	758:769	arg1	subpopulations					794:807	endogenous glycosylated and phosphorylated Akt subpopulations	747:807	endogenous glycosylated and phosphorylated Akt subpopulations	747:807	Such an easy method enabled us to visualize endogenous glycosylated and phosphorylated Akt subpopulations in parallel and observed the inhibitory effect of Akt O-GlcNAcylations on its phosphorylation.
22629392	6	25	from	activation	1138:1147	arg1	turn					1152:1155	turn	1152:1155	turn	1152:1155	The impaired Akt activation in turn resulted in the compromised biological functions of Akt, as evidenced by suppressed cell proliferation and migration capabilities.
22629392	6	26	theme	suppressed	1230:1239	arg1	proliferation					1246:1258	suppressed cell proliferation	1230:1258	suppressed cell proliferation	1230:1258	The impaired Akt activation in turn resulted in the compromised biological functions of Akt, as evidenced by suppressed cell proliferation and migration capabilities.
22629392	1	27	theme	post-translational	215:232	arg1	modifications					234:246	post-translational modifications	215:246	post-translational modifications	215:246	O-linked N-acetylglucosamine glycosylations (O-GlcNAc) and O-linked phosphorylations (O-phosphate), as two important types of post-translational modifications, often occur on the same protein and bear a reciprocal relationship.
22629392	5	28	theme	Akt	1037:1039	arg1	phosphorylation					1041:1055	Akt phosphorylation	1037:1055	Akt phosphorylation	1037:1055	Further studies utilizing mass spectrometry and mutagenesis approaches showed that O-GlcNAcylations at Thr 305 and Thr 312 inhibited Akt phosphorylation at Thr 308 via disrupting the interaction between Akt and PDK1.
22629392	6	29	theme	compromised	1173:1183	arg1	functions					1196:1204	the compromised biological functions	1169:1204	the compromised biological functions of Akt	1169:1211	The impaired Akt activation in turn resulted in the compromised biological functions of Akt, as evidenced by suppressed cell proliferation and migration capabilities.
22629392	1	30	theme	modifications	234:246	arg1	types					206:210	as two important types	189:210	as two important types of post-translational modifications	189:246	O-linked N-acetylglucosamine glycosylations (O-GlcNAc) and O-linked phosphorylations (O-phosphate), as two important types of post-translational modifications, often occur on the same protein and bear a reciprocal relationship.
22629392	1	30	theme	modifications	234:246	arg1	glycosylations					118:131	O-linked N-acetylglucosamine glycosylations	89:131	O-linked N-acetylglucosamine glycosylations (O-GlcNAc)	89:142	O-linked N-acetylglucosamine glycosylations (O-GlcNAc) and O-linked phosphorylations (O-phosphate), as two important types of post-translational modifications, often occur on the same protein and bear a reciprocal relationship.
22629392	4	31	theme	glycosylated	758:769	arg1	subpopulations					794:807	endogenous glycosylated and phosphorylated Akt subpopulations	747:807	endogenous glycosylated and phosphorylated Akt subpopulations	747:807	Such an easy method enabled us to visualize endogenous glycosylated and phosphorylated Akt subpopulations in parallel and observed the inhibitory effect of Akt O-GlcNAcylations on its phosphorylation.
22629392	6	32	theme	Akt	1134:1136	arg1	activation					1138:1147	The impaired Akt activation	1121:1147	The impaired Akt activation in turn	1121:1155	The impaired Akt activation in turn resulted in the compromised biological functions of Akt, as evidenced by suppressed cell proliferation and migration capabilities.
22629392	5	33	theme	mass	930:933	arg1	spectrometry					935:946	mass spectrometry	930:946	mass spectrometry	930:946	Further studies utilizing mass spectrometry and mutagenesis approaches showed that O-GlcNAcylations at Thr 305 and Thr 312 inhibited Akt phosphorylation at Thr 308 via disrupting the interaction between Akt and PDK1.
22629392	3	34	theme	O-phosphate	674:684	arg1	immunodetection					686:700	subsequent O-phosphate immunodetection	663:700	subsequent O-phosphate immunodetection	663:700	Here, we applied a two-step analytic approach composed of the O-GlcNAc immunoenrichment and subsequent O-phosphate immunodetection.
22629392	6	35	theme	impaired	1125:1132	arg1	activation					1138:1147	The impaired Akt activation	1121:1147	The impaired Akt activation in turn	1121:1155	The impaired Akt activation in turn resulted in the compromised biological functions of Akt, as evidenced by suppressed cell proliferation and migration capabilities.
22629392	0	36	theme	Akt	74:76	arg1	signaling					78:86	Akt signaling	74:86	Akt signaling	74:86	Extensive crosstalk between O-GlcNAcylation and phosphorylation regulates Akt signaling.
22629392	5	37	theme	Further	904:910	arg1	studies					912:918	Further studies	904:918	Further studies utilizing mass spectrometry and mutagenesis approaches	904:973	Further studies utilizing mass spectrometry and mutagenesis approaches showed that O-GlcNAcylations at Thr 305 and Thr 312 inhibited Akt phosphorylation at Thr 308 via disrupting the interaction between Akt and PDK1.
22629392	2	38	dep	unclear	521:527	arg1	due					538:540	due	538:540	due	538:540	In addition to the well documented phosphorylations that control Akt activity, Akt also undergoes O-GlcNAcylation, but the interplay between these two modifications and the biological significance remain unclear, largely due to the technique challenges.
22629392	7	39	theme	Akt	1464:1466	arg1	signaling					1468:1476	Akt signaling	1464:1476	Akt signaling	1464:1476	Together, this study revealed an extensive crosstalk between O-GlcNAcylations and phosphorylations of Akt and demonstrated O-GlcNAcylation as a new regulatory modification for Akt signaling.
22629392	1	40	theme	O-linked	148:155	arg1	phosphorylations					157:172	O-linked phosphorylations	148:172	O-linked phosphorylations (O-phosphate)	148:186	O-linked N-acetylglucosamine glycosylations (O-GlcNAc) and O-linked phosphorylations (O-phosphate), as two important types of post-translational modifications, often occur on the same protein and bear a reciprocal relationship.
22629392	1	40	theme	O-linked	148:155	arg1	O-phosphate					175:185	O-phosphate	175:185	O-phosphate	175:185	O-linked N-acetylglucosamine glycosylations (O-GlcNAc) and O-linked phosphorylations (O-phosphate), as two important types of post-translational modifications, often occur on the same protein and bear a reciprocal relationship.
22629392	3	41	theme	two-step	590:597	arg1	approach					608:615	a two-step analytic approach	588:615	a two-step analytic approach composed of the O-GlcNAc immunoenrichment and subsequent O-phosphate immunodetection	588:700	Here, we applied a two-step analytic approach composed of the O-GlcNAc immunoenrichment and subsequent O-phosphate immunodetection.
22629392	4	42	theme	Akt	859:861	arg1	O-GlcNAcylations					863:878	Akt O-GlcNAcylations	859:878	Akt O-GlcNAcylations	859:878	Such an easy method enabled us to visualize endogenous glycosylated and phosphorylated Akt subpopulations in parallel and observed the inhibitory effect of Akt O-GlcNAcylations on its phosphorylation.
22629392	4	43	theme	Akt	790:792	arg1	subpopulations					794:807	endogenous glycosylated and phosphorylated Akt subpopulations	747:807	endogenous glycosylated and phosphorylated Akt subpopulations	747:807	Such an easy method enabled us to visualize endogenous glycosylated and phosphorylated Akt subpopulations in parallel and observed the inhibitory effect of Akt O-GlcNAcylations on its phosphorylation.
22629392	6	44	theme	Akt	1209:1211	arg1	functions					1196:1204	the compromised biological functions	1169:1204	the compromised biological functions of Akt	1169:1211	The impaired Akt activation in turn resulted in the compromised biological functions of Akt, as evidenced by suppressed cell proliferation and migration capabilities.
22629392	1	45	link	O-linked	148:155	arg1	phosphorylations					157:172	O-linked phosphorylations	148:172	O-linked phosphorylations (O-phosphate)	148:186	O-linked N-acetylglucosamine glycosylations (O-GlcNAc) and O-linked phosphorylations (O-phosphate), as two important types of post-translational modifications, often occur on the same protein and bear a reciprocal relationship.
22629392	1	45	link	O-linked	148:155	arg1	O-phosphate					175:185	O-phosphate	175:185	O-phosphate	175:185	O-linked N-acetylglucosamine glycosylations (O-GlcNAc) and O-linked phosphorylations (O-phosphate), as two important types of post-translational modifications, often occur on the same protein and bear a reciprocal relationship.
22629392	1	46	contain	bear	285:288	arg1	types					206:210	as two important types	189:210	as two important types of post-translational modifications	189:246	O-linked N-acetylglucosamine glycosylations (O-GlcNAc) and O-linked phosphorylations (O-phosphate), as two important types of post-translational modifications, often occur on the same protein and bear a reciprocal relationship.
22629392	1	46	contain	bear	285:288	arg1	O-GlcNAc					134:141	O-GlcNAc	134:141	O-GlcNAc	134:141	O-linked N-acetylglucosamine glycosylations (O-GlcNAc) and O-linked phosphorylations (O-phosphate), as two important types of post-translational modifications, often occur on the same protein and bear a reciprocal relationship.
22629392	1	46	contain	bear	285:288	arg2	relationship					303:314	a reciprocal relationship	290:314	a reciprocal relationship	290:314	O-linked N-acetylglucosamine glycosylations (O-GlcNAc) and O-linked phosphorylations (O-phosphate), as two important types of post-translational modifications, often occur on the same protein and bear a reciprocal relationship.
22629392	1	46	contain	bear	285:288	arg1	glycosylations					118:131	O-linked N-acetylglucosamine glycosylations	89:131	O-linked N-acetylglucosamine glycosylations (O-GlcNAc)	89:142	O-linked N-acetylglucosamine glycosylations (O-GlcNAc) and O-linked phosphorylations (O-phosphate), as two important types of post-translational modifications, often occur on the same protein and bear a reciprocal relationship.
22629392	2	47	theme	documented	341:350	arg1	phosphorylations					352:367	the well documented phosphorylations	332:367	the well documented phosphorylations that control Akt activity	332:393	In addition to the well documented phosphorylations that control Akt activity, Akt also undergoes O-GlcNAcylation, but the interplay between these two modifications and the biological significance remain unclear, largely due to the technique challenges.
22629392	7	48	theme	extensive	1321:1329	arg1	crosstalk					1331:1339	an extensive crosstalk	1318:1339	an extensive crosstalk between O-GlcNAcylations and phosphorylations of Akt	1318:1392	Together, this study revealed an extensive crosstalk between O-GlcNAcylations and phosphorylations of Akt and demonstrated O-GlcNAcylation as a new regulatory modification for Akt signaling.
22629392	3	49	theme	O-GlcNAc	633:640	arg1	immunoenrichment					642:657	the O-GlcNAc immunoenrichment	629:657	the O-GlcNAc immunoenrichment	629:657	Here, we applied a two-step analytic approach composed of the O-GlcNAc immunoenrichment and subsequent O-phosphate immunodetection.
22629392	5	50	theme	mutagenesis	952:962	arg1	approaches					964:973	mutagenesis approaches	952:973	mutagenesis approaches	952:973	Further studies utilizing mass spectrometry and mutagenesis approaches showed that O-GlcNAcylations at Thr 305 and Thr 312 inhibited Akt phosphorylation at Thr 308 via disrupting the interaction between Akt and PDK1.
22629392	2	51	theme	biological	490:499	arg1	significance					501:512	the biological significance	486:512	the biological significance	486:512	In addition to the well documented phosphorylations that control Akt activity, Akt also undergoes O-GlcNAcylation, but the interplay between these two modifications and the biological significance remain unclear, largely due to the technique challenges.
22629392	4	52	theme	O-GlcNAcylations	863:878	arg1	effect					849:854	the inhibitory effect	834:854	the inhibitory effect of Akt O-GlcNAcylations on its phosphorylation	834:901	Such an easy method enabled us to visualize endogenous glycosylated and phosphorylated Akt subpopulations in parallel and observed the inhibitory effect of Akt O-GlcNAcylations on its phosphorylation.
22629392	1	53	theme	same	268:271	arg1	protein					273:279	the same protein	264:279	the same protein	264:279	O-linked N-acetylglucosamine glycosylations (O-GlcNAc) and O-linked phosphorylations (O-phosphate), as two important types of post-translational modifications, often occur on the same protein and bear a reciprocal relationship.
33626323	0	0	theme	trophoblast	94:104	arg1	syncytialization					106:121	trophoblast syncytialization	94:121	trophoblast syncytialization	94:121	Quantitative chemoproteomics reveals O-GlcNAcylation of cystathionine γ-lyase (CSE) represses trophoblast syncytialization.
33626323	2	1	theme	human	401:405	arg1	trophoblasts					417:428	human placental trophoblasts	401:428	human placental trophoblasts	401:428	Herein, by applying the quantitative O-GlcNAc proteomics, we established a database of O-GlcNAcylated proteins in human placental trophoblasts.
33626323	6	2	from	dynamics	1092:1099	arg1	placenta					1110:1117	human placenta	1104:1117	human placenta	1104:1117	The findings establish a resource of O-GlcNAc dynamics in human placenta, and provide a deeper insight into the biological significance of O-GlcNAcylation in placental development as well as potential therapeutic targets for the relevant pregnant complications.
33626323	5	3	theme	trophoblast	1017:1027	arg1	differentiation					1029:1043	restricted trophoblast differentiation	1006:1043	restricted trophoblast differentiation	1006:1043	Consistently, in preeclamptic placentas, remarkably enhanced CSE O-GlcNAcylation and H2S production were associated with restricted trophoblast differentiation.
33626323	1	4	theme	placental	196:204	arg1	development					206:216	placental development	196:216	placental development	196:216	Emerging evidence indicates the involvement of O-GlcNAc modification in placental development and pregnant health through mechanisms that are not well understood.
33626323	4	5	theme	androgen	853:860	arg1	dimerization					871:882	androgen receptor dimerization	853:882	androgen receptor dimerization	853:882	Site-specific analysis by mass spectrometry revealed Ser138 as the core O-GlcNAc site in CSE, and its O-GlcNAcylation promoted the enzymatic activity to produce H2S, which in turn repressed trophoblast differentiation via inhibiting androgen receptor dimerization.
33626323	6	6	from	targets	1259:1265	arg1	development					1214:1224	placental development	1204:1224	placental development	1204:1224	The findings establish a resource of O-GlcNAc dynamics in human placenta, and provide a deeper insight into the biological significance of O-GlcNAcylation in placental development as well as potential therapeutic targets for the relevant pregnant complications.
33626323	2	7	theme	O-GlcNAc	324:331	arg1	proteomics					333:342	the quantitative O-GlcNAc proteomics	307:342	the quantitative O-GlcNAc proteomics	307:342	Herein, by applying the quantitative O-GlcNAc proteomics, we established a database of O-GlcNAcylated proteins in human placental trophoblasts.
33626323	6	8	theme	relevant	1275:1282	arg1	complications					1293:1305	the relevant pregnant complications	1271:1305	the relevant pregnant complications	1271:1305	The findings establish a resource of O-GlcNAc dynamics in human placenta, and provide a deeper insight into the biological significance of O-GlcNAcylation in placental development as well as potential therapeutic targets for the relevant pregnant complications.
33626323	3	9	theme	significant	600:610	arg1	change					612:617	the most significant change	591:617	the most significant change	591:617	Hundreds of proteins that were dynamically O-GlcNAcylated during trophoblast differentiation were identified, among which cystathionine γ-lyase (CSE) exhibited the most significant change.
33626323	4	10	theme	enzymatic	751:759	arg1	activity					761:768	the enzymatic activity	747:768	the enzymatic activity to produce H2S, which in turn repressed trophoblast differentiation via inhibiting androgen receptor dimerization	747:882	Site-specific analysis by mass spectrometry revealed Ser138 as the core O-GlcNAc site in CSE, and its O-GlcNAcylation promoted the enzymatic activity to produce H2S, which in turn repressed trophoblast differentiation via inhibiting androgen receptor dimerization.
33626323	5	11	theme	H2S	970:972	arg1	production					974:983	H2S production	970:983	H2S production	970:983	Consistently, in preeclamptic placentas, remarkably enhanced CSE O-GlcNAcylation and H2S production were associated with restricted trophoblast differentiation.
33626323	1	12	from	involvement	156:166	arg1	development					206:216	placental development	196:216	placental development	196:216	Emerging evidence indicates the involvement of O-GlcNAc modification in placental development and pregnant health through mechanisms that are not well understood.
33626323	1	12	from	involvement	156:166	arg1	health					231:236	pregnant health	222:236	pregnant health	222:236	Emerging evidence indicates the involvement of O-GlcNAc modification in placental development and pregnant health through mechanisms that are not well understood.
33626323	0	13	theme	Quantitative	0:11	arg1	chemoproteomics					13:27	Quantitative chemoproteomics	0:27	Quantitative chemoproteomics	0:27	Quantitative chemoproteomics reveals O-GlcNAcylation of cystathionine γ-lyase (CSE) represses trophoblast syncytialization.
33626323	5	14	theme	preeclamptic	902:913	arg1	placentas					915:923	preeclamptic placentas	902:923	preeclamptic placentas	902:923	Consistently, in preeclamptic placentas, remarkably enhanced CSE O-GlcNAcylation and H2S production were associated with restricted trophoblast differentiation.
33626323	6	15	theme	dynamics	1092:1099	arg1	resource					1071:1078	a resource	1069:1078	a resource of O-GlcNAc dynamics in human placenta	1069:1117	The findings establish a resource of O-GlcNAc dynamics in human placenta, and provide a deeper insight into the biological significance of O-GlcNAcylation in placental development as well as potential therapeutic targets for the relevant pregnant complications.
33626323	4	16	theme	trophoblast	810:820	arg1	differentiation					822:836	trophoblast differentiation	810:836	trophoblast differentiation	810:836	Site-specific analysis by mass spectrometry revealed Ser138 as the core O-GlcNAc site in CSE, and its O-GlcNAcylation promoted the enzymatic activity to produce H2S, which in turn repressed trophoblast differentiation via inhibiting androgen receptor dimerization.
33626323	1	17	theme	pregnant	222:229	arg1	health					231:236	pregnant health	222:236	pregnant health	222:236	Emerging evidence indicates the involvement of O-GlcNAc modification in placental development and pregnant health through mechanisms that are not well understood.
33626323	3	18	theme	proteins	443:450	arg1	Hundreds					431:438	Hundreds	431:438	Hundreds of proteins that were dynamically O-GlcNAcylated during trophoblast differentiation	431:522	Hundreds of proteins that were dynamically O-GlcNAcylated during trophoblast differentiation were identified, among which cystathionine γ-lyase (CSE) exhibited the most significant change.
33626323	5	19	gly	O-GlcNAcylation	950:964	arg1	placentas					915:923	preeclamptic placentas	902:923	preeclamptic placentas	902:923	Consistently, in preeclamptic placentas, remarkably enhanced CSE O-GlcNAcylation and H2S production were associated with restricted trophoblast differentiation.
33626323	3	20	theme	trophoblast	496:506	arg1	differentiation					508:522	trophoblast differentiation	496:522	trophoblast differentiation	496:522	Hundreds of proteins that were dynamically O-GlcNAcylated during trophoblast differentiation were identified, among which cystathionine γ-lyase (CSE) exhibited the most significant change.
33626323	6	21	theme	human	1104:1108	arg1	placenta					1110:1117	human placenta	1104:1117	human placenta	1104:1117	The findings establish a resource of O-GlcNAc dynamics in human placenta, and provide a deeper insight into the biological significance of O-GlcNAcylation in placental development as well as potential therapeutic targets for the relevant pregnant complications.
33626323	1	22	theme	Emerging	124:131	arg1	evidence					133:140	Emerging evidence	124:140	Emerging evidence	124:140	Emerging evidence indicates the involvement of O-GlcNAc modification in placental development and pregnant health through mechanisms that are not well understood.
33626323	5	23	theme	enhanced	937:944	arg1	O-GlcNAcylation					950:964	remarkably enhanced CSE O-GlcNAcylation	926:964	remarkably enhanced CSE O-GlcNAcylation	926:964	Consistently, in preeclamptic placentas, remarkably enhanced CSE O-GlcNAcylation and H2S production were associated with restricted trophoblast differentiation.
33626323	2	24	theme	quantitative	311:322	arg1	proteomics					333:342	the quantitative O-GlcNAc proteomics	307:342	the quantitative O-GlcNAc proteomics	307:342	Herein, by applying the quantitative O-GlcNAc proteomics, we established a database of O-GlcNAcylated proteins in human placental trophoblasts.
33626323	6	25	theme	pregnant	1284:1291	arg1	complications					1293:1305	the relevant pregnant complications	1271:1305	the relevant pregnant complications	1271:1305	The findings establish a resource of O-GlcNAc dynamics in human placenta, and provide a deeper insight into the biological significance of O-GlcNAcylation in placental development as well as potential therapeutic targets for the relevant pregnant complications.
33626323	5	26	theme	CSE	946:948	arg1	O-GlcNAcylation					950:964	remarkably enhanced CSE O-GlcNAcylation	926:964	remarkably enhanced CSE O-GlcNAcylation	926:964	Consistently, in preeclamptic placentas, remarkably enhanced CSE O-GlcNAcylation and H2S production were associated with restricted trophoblast differentiation.
33626323	0	27	theme	cystathionine	56:68	arg1	CSE					79:81	CSE	79:81	CSE	79:81	Quantitative chemoproteomics reveals O-GlcNAcylation of cystathionine γ-lyase (CSE) represses trophoblast syncytialization.
33626323	0	27	theme	cystathionine	56:68	arg1	γ-lyase					70:76	cystathionine γ-lyase	56:76	cystathionine γ-lyase (CSE)	56:82	Quantitative chemoproteomics reveals O-GlcNAcylation of cystathionine γ-lyase (CSE) represses trophoblast syncytialization.
33626323	4	28	theme	mass	646:649	arg1	spectrometry					651:662	mass spectrometry	646:662	mass spectrometry	646:662	Site-specific analysis by mass spectrometry revealed Ser138 as the core O-GlcNAc site in CSE, and its O-GlcNAcylation promoted the enzymatic activity to produce H2S, which in turn repressed trophoblast differentiation via inhibiting androgen receptor dimerization.
33626323	6	29	from	placenta	1110:1117	arg1	resource					1071:1078	a resource	1069:1078	a resource of O-GlcNAc dynamics in human placenta	1069:1117	The findings establish a resource of O-GlcNAc dynamics in human placenta, and provide a deeper insight into the biological significance of O-GlcNAcylation in placental development as well as potential therapeutic targets for the relevant pregnant complications.
33626323	6	30	theme	placental	1204:1212	arg1	development					1214:1224	placental development	1204:1224	placental development	1204:1224	The findings establish a resource of O-GlcNAc dynamics in human placenta, and provide a deeper insight into the biological significance of O-GlcNAcylation in placental development as well as potential therapeutic targets for the relevant pregnant complications.
33626323	6	31	theme	O-GlcNAc	1083:1090	arg1	dynamics					1092:1099	O-GlcNAc dynamics	1083:1099	O-GlcNAc dynamics in human placenta	1083:1117	The findings establish a resource of O-GlcNAc dynamics in human placenta, and provide a deeper insight into the biological significance of O-GlcNAcylation in placental development as well as potential therapeutic targets for the relevant pregnant complications.
33626323	6	32	theme	biological	1158:1167	arg1	significance					1169:1180	the biological significance	1154:1180	the biological significance of O-GlcNAcylation in placental development as well as potential therapeutic targets for the relevant pregnant complications	1154:1305	The findings establish a resource of O-GlcNAc dynamics in human placenta, and provide a deeper insight into the biological significance of O-GlcNAcylation in placental development as well as potential therapeutic targets for the relevant pregnant complications.
33626323	6	33	from	resource	1071:1078	arg1	placenta					1110:1117	human placenta	1104:1117	human placenta	1104:1117	The findings establish a resource of O-GlcNAc dynamics in human placenta, and provide a deeper insight into the biological significance of O-GlcNAcylation in placental development as well as potential therapeutic targets for the relevant pregnant complications.
33626323	6	34	theme	potential	1237:1245	arg1	targets					1259:1265	potential therapeutic targets	1237:1265	the biological significance of O-GlcNAcylation in placental development as well as potential therapeutic targets for the relevant pregnant complications	1154:1305	The findings establish a resource of O-GlcNAc dynamics in human placenta, and provide a deeper insight into the biological significance of O-GlcNAcylation in placental development as well as potential therapeutic targets for the relevant pregnant complications.
33626323	2	35	theme	proteins	389:396	arg1	database					362:369	a database	360:369	a database of O-GlcNAcylated proteins	360:396	Herein, by applying the quantitative O-GlcNAc proteomics, we established a database of O-GlcNAcylated proteins in human placental trophoblasts.
33626323	4	36	theme	Site-specific	620:632	arg1	analysis					634:641	Site-specific analysis	620:641	Site-specific analysis by mass spectrometry	620:662	Site-specific analysis by mass spectrometry revealed Ser138 as the core O-GlcNAc site in CSE, and its O-GlcNAcylation promoted the enzymatic activity to produce H2S, which in turn repressed trophoblast differentiation via inhibiting androgen receptor dimerization.
33626323	6	37	dep	potential	1237:1245	arg1	therapeutic					1247:1257	therapeutic	1247:1257	therapeutic	1247:1257	The findings establish a resource of O-GlcNAc dynamics in human placenta, and provide a deeper insight into the biological significance of O-GlcNAcylation in placental development as well as potential therapeutic targets for the relevant pregnant complications.
33626323	2	38	theme	O-GlcNAcylated	374:387	arg1	proteins					389:396	O-GlcNAcylated proteins	374:396	O-GlcNAcylated proteins	374:396	Herein, by applying the quantitative O-GlcNAc proteomics, we established a database of O-GlcNAcylated proteins in human placental trophoblasts.
33626323	6	39	from	significance	1169:1180	arg1	development					1214:1224	placental development	1204:1224	placental development	1204:1224	The findings establish a resource of O-GlcNAc dynamics in human placenta, and provide a deeper insight into the biological significance of O-GlcNAcylation in placental development as well as potential therapeutic targets for the relevant pregnant complications.
33626323	3	40	theme	cystathionine	553:565	arg1	CSE					576:578	CSE	576:578	CSE	576:578	Hundreds of proteins that were dynamically O-GlcNAcylated during trophoblast differentiation were identified, among which cystathionine γ-lyase (CSE) exhibited the most significant change.
33626323	3	40	theme	cystathionine	553:565	arg1	γ-lyase					567:573	cystathionine γ-lyase	553:573	cystathionine γ-lyase (CSE)	553:579	Hundreds of proteins that were dynamically O-GlcNAcylated during trophoblast differentiation were identified, among which cystathionine γ-lyase (CSE) exhibited the most significant change.
33626323	4	41	theme	O-GlcNAc	692:699	arg1	site					701:704	the core O-GlcNAc site	683:704	the core O-GlcNAc site	683:704	Site-specific analysis by mass spectrometry revealed Ser138 as the core O-GlcNAc site in CSE, and its O-GlcNAcylation promoted the enzymatic activity to produce H2S, which in turn repressed trophoblast differentiation via inhibiting androgen receptor dimerization.
33626323	4	41	theme	O-GlcNAc	692:699	arg1	Ser138					673:678	Ser138	673:678	Ser138	673:678	Site-specific analysis by mass spectrometry revealed Ser138 as the core O-GlcNAc site in CSE, and its O-GlcNAcylation promoted the enzymatic activity to produce H2S, which in turn repressed trophoblast differentiation via inhibiting androgen receptor dimerization.
33626323	4	42	theme	receptor	862:869	arg1	dimerization					871:882	androgen receptor dimerization	853:882	androgen receptor dimerization	853:882	Site-specific analysis by mass spectrometry revealed Ser138 as the core O-GlcNAc site in CSE, and its O-GlcNAcylation promoted the enzymatic activity to produce H2S, which in turn repressed trophoblast differentiation via inhibiting androgen receptor dimerization.
33626323	1	43	theme	modification	180:191	arg1	involvement					156:166	the involvement	152:166	the involvement of O-GlcNAc modification in placental development and pregnant health	152:236	Emerging evidence indicates the involvement of O-GlcNAc modification in placental development and pregnant health through mechanisms that are not well understood.
33626323	4	44	theme	core	687:690	arg1	site					701:704	the core O-GlcNAc site	683:704	the core O-GlcNAc site	683:704	Site-specific analysis by mass spectrometry revealed Ser138 as the core O-GlcNAc site in CSE, and its O-GlcNAcylation promoted the enzymatic activity to produce H2S, which in turn repressed trophoblast differentiation via inhibiting androgen receptor dimerization.
33626323	4	44	theme	core	687:690	arg1	Ser138					673:678	Ser138	673:678	Ser138	673:678	Site-specific analysis by mass spectrometry revealed Ser138 as the core O-GlcNAc site in CSE, and its O-GlcNAcylation promoted the enzymatic activity to produce H2S, which in turn repressed trophoblast differentiation via inhibiting androgen receptor dimerization.
33626323	5	45	theme	restricted	1006:1015	arg1	differentiation					1029:1043	restricted trophoblast differentiation	1006:1043	restricted trophoblast differentiation	1006:1043	Consistently, in preeclamptic placentas, remarkably enhanced CSE O-GlcNAcylation and H2S production were associated with restricted trophoblast differentiation.
33626323	6	46	theme	O-GlcNAcylation	1185:1199	arg1	significance					1169:1180	the biological significance	1154:1180	the biological significance of O-GlcNAcylation in placental development as well as potential therapeutic targets for the relevant pregnant complications	1154:1305	The findings establish a resource of O-GlcNAc dynamics in human placenta, and provide a deeper insight into the biological significance of O-GlcNAcylation in placental development as well as potential therapeutic targets for the relevant pregnant complications.
33626323	6	46	theme	O-GlcNAcylation	1185:1199	arg1	targets					1259:1265	potential therapeutic targets	1237:1265	the biological significance of O-GlcNAcylation in placental development as well as potential therapeutic targets for the relevant pregnant complications	1154:1305	The findings establish a resource of O-GlcNAc dynamics in human placenta, and provide a deeper insight into the biological significance of O-GlcNAcylation in placental development as well as potential therapeutic targets for the relevant pregnant complications.
33626323	1	47	theme	O-GlcNAc	171:178	arg1	modification					180:191	O-GlcNAc modification	171:191	O-GlcNAc modification	171:191	Emerging evidence indicates the involvement of O-GlcNAc modification in placental development and pregnant health through mechanisms that are not well understood.
33626323	2	48	theme	placental	407:415	arg1	trophoblasts					417:428	human placental trophoblasts	401:428	human placental trophoblasts	401:428	Herein, by applying the quantitative O-GlcNAc proteomics, we established a database of O-GlcNAcylated proteins in human placental trophoblasts.
33626323	6	49	theme	deeper	1134:1139	arg1	insight					1141:1147	a deeper insight	1132:1147	a deeper insight into the biological significance of O-GlcNAcylation in placental development as well as potential therapeutic targets for the relevant pregnant complications	1132:1305	The findings establish a resource of O-GlcNAc dynamics in human placenta, and provide a deeper insight into the biological significance of O-GlcNAcylation in placental development as well as potential therapeutic targets for the relevant pregnant complications.
28714959	0	0	theme	prostate	86:93	arg1	cancer					95:100	prostate cancer	86:100	prostate cancer	86:100	O-GlcNAcylation modulates Bmi-1 protein stability and potential oncogenic function in prostate cancer.
28714959	5	1	theme	Bmi-1	667:671	arg1	O-GlcNAcylation					673:687	Bmi-1 O-GlcNAcylation	667:687	Bmi-1 O-GlcNAcylation	667:687	Furthermore, we identified that Ser255 is the site for Bmi-1 O-GlcNAcylation, and O-GlcNAcylation promoted Bmi-1 protein stability and its oncogenic activity.
28714959	7	2	theme	TP53	1026:1029	arg1	pathway					1055:1061	the TP53, PTEN and CDKN1A/CDKN2A pathway	1022:1061	the TP53, PTEN and CDKN1A/CDKN2A pathway	1022:1061	Taken together, these results indicate that OGT-mediated O-GlcNAcylation at Ser255 stabilizes Bmi-1 and hence inhibits the TP53, PTEN and CDKN1A/CDKN2A pathway.
28714959	8	3	from	role	1161:1164	arg1	cancer					1197:1202	prostate cancer	1188:1202	prostate cancer	1188:1202	The study not only uncovers a novel functional PTMs of Bmi-1 but also reveals a unique oncogenic role of O-GlcNAcylation in prostate cancer.
28714959	3	4	theme	underlying	389:398	arg1	regulation					405:414	the underlying PTMs regulation	385:414	the underlying PTMs regulation of Bmi-1	385:423	Nobly, the underlying PTMs regulation of Bmi-1 is poorly known.
28714959	8	5	theme	novel	1094:1098	arg1	PTMs					1111:1114	a novel functional PTMs	1092:1114	a novel functional PTMs of Bmi-1	1092:1123	The study not only uncovers a novel functional PTMs of Bmi-1 but also reveals a unique oncogenic role of O-GlcNAcylation in prostate cancer.
28714959	7	6	from	Ser255	979:984	arg1	O-GlcNAcylation					960:974	OGT-mediated O-GlcNAcylation	947:974	OGT-mediated O-GlcNAcylation at Ser255	947:984	Taken together, these results indicate that OGT-mediated O-GlcNAcylation at Ser255 stabilizes Bmi-1 and hence inhibits the TP53, PTEN and CDKN1A/CDKN2A pathway.
28714959	3	7	theme	PTMs	400:403	arg1	regulation					405:414	the underlying PTMs regulation	385:414	the underlying PTMs regulation of Bmi-1	385:423	Nobly, the underlying PTMs regulation of Bmi-1 is poorly known.
28714959	1	8	theme	stem	194:197	arg1	cells					199:203	stem cells	194:203	stem cells self-renewal and tumorigenesis initiating of prostate cancer	194:264	The Polycomb group transcriptional repressor Bmi-1 often overexpressed and participated in stem cells self-renewal and tumorigenesis initiating of prostate cancer.
28714959	8	9	theme	functional	1100:1109	arg1	PTMs					1111:1114	a novel functional PTMs	1092:1114	a novel functional PTMs of Bmi-1	1092:1123	The study not only uncovers a novel functional PTMs of Bmi-1 but also reveals a unique oncogenic role of O-GlcNAcylation in prostate cancer.
28714959	6	10	dep	associated	838:847	arg1	oncogenes					828:836	potential oncogenes	818:836	potential oncogenes associated pathway subject to repression via the OGT-Bmi-1 axis	818:900	Finally, microarray analysis has characterized potential oncogenes associated pathway subject to repression via the OGT-Bmi-1 axis.
28714959	6	10	dep	associated	838:847	arg1	pathway					849:855	pathway	849:855	pathway	849:855	Finally, microarray analysis has characterized potential oncogenes associated pathway subject to repression via the OGT-Bmi-1 axis.
28714959	3	11	theme	Bmi-1	419:423	arg1	regulation					405:414	the underlying PTMs regulation	385:414	the underlying PTMs regulation of Bmi-1	385:423	Nobly, the underlying PTMs regulation of Bmi-1 is poorly known.
28714959	8	12	theme	prostate	1188:1195	arg1	cancer					1197:1202	prostate cancer	1188:1202	prostate cancer	1188:1202	The study not only uncovers a novel functional PTMs of Bmi-1 but also reveals a unique oncogenic role of O-GlcNAcylation in prostate cancer.
28714959	8	13	theme	Bmi-1	1119:1123	arg1	PTMs					1111:1114	a novel functional PTMs	1092:1114	a novel functional PTMs of Bmi-1	1092:1123	The study not only uncovers a novel functional PTMs of Bmi-1 but also reveals a unique oncogenic role of O-GlcNAcylation in prostate cancer.
28714959	1	14	theme	self-renewal	205:216	arg1	cells					199:203	stem cells	194:203	stem cells self-renewal and tumorigenesis initiating of prostate cancer	194:264	The Polycomb group transcriptional repressor Bmi-1 often overexpressed and participated in stem cells self-renewal and tumorigenesis initiating of prostate cancer.
28714959	6	15	theme	potential	818:826	arg1	oncogenes					828:836	potential oncogenes	818:836	potential oncogenes associated pathway subject to repression via the OGT-Bmi-1 axis	818:900	Finally, microarray analysis has characterized potential oncogenes associated pathway subject to repression via the OGT-Bmi-1 axis.
28714959	6	15	theme	potential	818:826	arg1	pathway					849:855	pathway	849:855	pathway	849:855	Finally, microarray analysis has characterized potential oncogenes associated pathway subject to repression via the OGT-Bmi-1 axis.
28714959	0	16	theme	protein	32:38	arg1	stability					40:48	Bmi-1 protein stability	26:48	Bmi-1 protein stability	26:48	O-GlcNAcylation modulates Bmi-1 protein stability and potential oncogenic function in prostate cancer.
28714959	5	17	theme	protein	725:731	arg1	stability					733:741	Bmi-1 protein stability	719:741	Bmi-1 protein stability	719:741	Furthermore, we identified that Ser255 is the site for Bmi-1 O-GlcNAcylation, and O-GlcNAcylation promoted Bmi-1 protein stability and its oncogenic activity.
28714959	2	18	theme	post-translational	337:354	arg1	PTMs					371:374	PTMs	371:374	PTMs	371:374	In this progression, Bmi-1 protein was regulated by transcription and post-translational modifications (PTMs).
28714959	2	18	theme	post-translational	337:354	arg1	modifications					356:368	post-translational modifications	337:368	post-translational modifications (PTMs)	337:375	In this progression, Bmi-1 protein was regulated by transcription and post-translational modifications (PTMs).
28714959	1	19	theme	tumorigenesis	222:234	arg1	cells					199:203	stem cells	194:203	stem cells self-renewal and tumorigenesis initiating of prostate cancer	194:264	The Polycomb group transcriptional repressor Bmi-1 often overexpressed and participated in stem cells self-renewal and tumorigenesis initiating of prostate cancer.
28714959	0	20	theme	Bmi-1	26:30	arg1	stability					40:48	Bmi-1 protein stability	26:48	Bmi-1 protein stability	26:48	O-GlcNAcylation modulates Bmi-1 protein stability and potential oncogenic function in prostate cancer.
28714959	1	21	theme	group	116:120	arg1	repressor					138:146	The Polycomb group transcriptional repressor	103:146	The Polycomb group transcriptional repressor Bmi-1	103:152	The Polycomb group transcriptional repressor Bmi-1 often overexpressed and participated in stem cells self-renewal and tumorigenesis initiating of prostate cancer.
28714959	1	22	theme	initiating	236:245	arg1	tumorigenesis					222:234	tumorigenesis initiating	222:245	tumorigenesis initiating of prostate cancer	222:264	The Polycomb group transcriptional repressor Bmi-1 often overexpressed and participated in stem cells self-renewal and tumorigenesis initiating of prostate cancer.
28714959	4	23	theme	cell	495:498	arg1	line					500:503	C4-2 cell line	490:503	C4-2 cell line	490:503	Here we use co-immunoprecipitation show that in C4-2 cell line, Bmi-1 directly interacted with OGT which is the only known enzyme catalyzed the O-GlcNAcylation in human.
28714959	1	24	theme	prostate	250:257	arg1	cancer					259:264	prostate cancer	250:264	prostate cancer	250:264	The Polycomb group transcriptional repressor Bmi-1 often overexpressed and participated in stem cells self-renewal and tumorigenesis initiating of prostate cancer.
28714959	0	25	theme	oncogenic	64:72	arg1	function					74:81	potential oncogenic function	54:81	potential oncogenic function	54:81	O-GlcNAcylation modulates Bmi-1 protein stability and potential oncogenic function in prostate cancer.
28714959	5	26	theme	oncogenic	751:759	arg1	activity					761:768	its oncogenic activity	747:768	its oncogenic activity	747:768	Furthermore, we identified that Ser255 is the site for Bmi-1 O-GlcNAcylation, and O-GlcNAcylation promoted Bmi-1 protein stability and its oncogenic activity.
28714959	8	27	theme	oncogenic	1151:1159	arg1	role					1161:1164	a unique oncogenic role	1142:1164	a unique oncogenic role of O-GlcNAcylation in prostate cancer	1142:1202	The study not only uncovers a novel functional PTMs of Bmi-1 but also reveals a unique oncogenic role of O-GlcNAcylation in prostate cancer.
28714959	4	28	theme	C4-2	490:493	arg1	line					500:503	C4-2 cell line	490:503	C4-2 cell line	490:503	Here we use co-immunoprecipitation show that in C4-2 cell line, Bmi-1 directly interacted with OGT which is the only known enzyme catalyzed the O-GlcNAcylation in human.
28714959	1	29	theme	transcriptional	122:136	arg1	repressor					138:146	The Polycomb group transcriptional repressor	103:146	The Polycomb group transcriptional repressor Bmi-1	103:152	The Polycomb group transcriptional repressor Bmi-1 often overexpressed and participated in stem cells self-renewal and tumorigenesis initiating of prostate cancer.
28714959	0	30	theme	potential	54:62	arg1	function					74:81	potential oncogenic function	54:81	potential oncogenic function	54:81	O-GlcNAcylation modulates Bmi-1 protein stability and potential oncogenic function in prostate cancer.
28714959	4	31	theme	known	559:563	arg1	OGT					537:539	OGT	537:539	OGT which is the only known enzyme catalyzed the O-GlcNAcylation in human	537:609	Here we use co-immunoprecipitation show that in C4-2 cell line, Bmi-1 directly interacted with OGT which is the only known enzyme catalyzed the O-GlcNAcylation in human.
28714959	4	31	theme	known	559:563	arg1	enzyme					565:570	the only known enzyme	550:570	the only known enzyme catalyzed the O-GlcNAcylation in human	550:609	Here we use co-immunoprecipitation show that in C4-2 cell line, Bmi-1 directly interacted with OGT which is the only known enzyme catalyzed the O-GlcNAcylation in human.
28714959	8	32	theme	unique	1144:1149	arg1	role					1161:1164	a unique oncogenic role	1142:1164	a unique oncogenic role of O-GlcNAcylation in prostate cancer	1142:1202	The study not only uncovers a novel functional PTMs of Bmi-1 but also reveals a unique oncogenic role of O-GlcNAcylation in prostate cancer.
28714959	6	33	theme	microarray	780:789	arg1	analysis					791:798	microarray analysis	780:798	microarray analysis	780:798	Finally, microarray analysis has characterized potential oncogenes associated pathway subject to repression via the OGT-Bmi-1 axis.
28714959	1	34	theme	repressor	138:146	arg1	Bmi-1					148:152	The Polycomb group transcriptional repressor Bmi-1	103:152	The Polycomb group transcriptional repressor Bmi-1	103:152	The Polycomb group transcriptional repressor Bmi-1 often overexpressed and participated in stem cells self-renewal and tumorigenesis initiating of prostate cancer.
28714959	6	35	theme	OGT-Bmi-1	887:895	arg1	axis					897:900	the OGT-Bmi-1 axis	883:900	the OGT-Bmi-1 axis	883:900	Finally, microarray analysis has characterized potential oncogenes associated pathway subject to repression via the OGT-Bmi-1 axis.
28714959	1	36	theme	Polycomb	107:114	arg1	repressor					138:146	The Polycomb group transcriptional repressor	103:146	The Polycomb group transcriptional repressor Bmi-1	103:152	The Polycomb group transcriptional repressor Bmi-1 often overexpressed and participated in stem cells self-renewal and tumorigenesis initiating of prostate cancer.
28714959	1	37	theme	cancer	259:264	arg1	tumorigenesis					222:234	tumorigenesis initiating	222:245	tumorigenesis initiating of prostate cancer	222:264	The Polycomb group transcriptional repressor Bmi-1 often overexpressed and participated in stem cells self-renewal and tumorigenesis initiating of prostate cancer.
28714959	5	38	theme	Bmi-1	719:723	arg1	stability					733:741	Bmi-1 protein stability	719:741	Bmi-1 protein stability	719:741	Furthermore, we identified that Ser255 is the site for Bmi-1 O-GlcNAcylation, and O-GlcNAcylation promoted Bmi-1 protein stability and its oncogenic activity.
28714959	2	39	theme	Bmi-1	288:292	arg1	protein					294:300	Bmi-1 protein	288:300	Bmi-1 protein	288:300	In this progression, Bmi-1 protein was regulated by transcription and post-translational modifications (PTMs).
28714959	7	40	theme	CDKN1A/CDKN2A	1041:1053	arg1	pathway					1055:1061	the TP53, PTEN and CDKN1A/CDKN2A pathway	1022:1061	the TP53, PTEN and CDKN1A/CDKN2A pathway	1022:1061	Taken together, these results indicate that OGT-mediated O-GlcNAcylation at Ser255 stabilizes Bmi-1 and hence inhibits the TP53, PTEN and CDKN1A/CDKN2A pathway.
28714959	7	41	theme	OGT-mediated	947:958	arg1	O-GlcNAcylation					960:974	OGT-mediated O-GlcNAcylation	947:974	OGT-mediated O-GlcNAcylation at Ser255	947:984	Taken together, these results indicate that OGT-mediated O-GlcNAcylation at Ser255 stabilizes Bmi-1 and hence inhibits the TP53, PTEN and CDKN1A/CDKN2A pathway.
28714959	4	42	dep	use	450:452	arg1	show					477:480	show	477:480	use co-immunoprecipitation show that in C4-2 cell line, Bmi-1 directly interacted with OGT which is the only known enzyme catalyzed the O-GlcNAcylation in human	450:609	Here we use co-immunoprecipitation show that in C4-2 cell line, Bmi-1 directly interacted with OGT which is the only known enzyme catalyzed the O-GlcNAcylation in human.
28714959	8	43	theme	O-GlcNAcylation	1169:1183	arg1	role					1161:1164	a unique oncogenic role	1142:1164	a unique oncogenic role of O-GlcNAcylation in prostate cancer	1142:1202	The study not only uncovers a novel functional PTMs of Bmi-1 but also reveals a unique oncogenic role of O-GlcNAcylation in prostate cancer.
28714959	7	44	theme	PTEN	1032:1035	arg1	pathway					1055:1061	the TP53, PTEN and CDKN1A/CDKN2A pathway	1022:1061	the TP53, PTEN and CDKN1A/CDKN2A pathway	1022:1061	Taken together, these results indicate that OGT-mediated O-GlcNAcylation at Ser255 stabilizes Bmi-1 and hence inhibits the TP53, PTEN and CDKN1A/CDKN2A pathway.
28714959	4	45	from	O-GlcNAcylation	586:600	arg1	human					605:609	human	605:609	human	605:609	Here we use co-immunoprecipitation show that in C4-2 cell line, Bmi-1 directly interacted with OGT which is the only known enzyme catalyzed the O-GlcNAcylation in human.
19238206	3	0	link	O-linked	430:437	arg1	transferase					464:474	O-linked beta-N-acetylglucosamine transferase	430:474	O-linked beta-N-acetylglucosamine transferase (O-GlcNAc transferase, OGT)	430:502	Here we report for the first time that PHB interacts with O-linked beta-N-acetylglucosamine transferase (O-GlcNAc transferase, OGT) and is O-GlcNAc modified; and also undergoes tyrosine phosphorylation in response to insulin.
19238206	3	0	link	O-linked	430:437	arg1	transferase					486:496	O-GlcNAc transferase	477:496	O-GlcNAc transferase	477:496	Here we report for the first time that PHB interacts with O-linked beta-N-acetylglucosamine transferase (O-GlcNAc transferase, OGT) and is O-GlcNAc modified; and also undergoes tyrosine phosphorylation in response to insulin.
19238206	7	1	theme	similar	1089:1095	arg1	motifs					1106:1111	similar tyrosine motifs	1089:1111	similar tyrosine motifs	1089:1111	This is attributed to the presence of similar tyrosine motifs in PHB and OGT.
19238206	9	2	theme	known	1421:1425	arg1	s					1454:1454	s	1454:1454	s	1454:1454	Sequence analysis of O-GlcNAc modified proteins having known O-GlcNAc modification site(s) or known tyrosine phosphorylation site(s) revealed a strong potential association between these two posttranslational modifications in various proteins.
19238206	9	2	theme	known	1421:1425	arg1	site					1449:1452	known O-GlcNAc modification site	1421:1452	known O-GlcNAc modification site(s)	1421:1455	Sequence analysis of O-GlcNAc modified proteins having known O-GlcNAc modification site(s) or known tyrosine phosphorylation site(s) revealed a strong potential association between these two posttranslational modifications in various proteins.
19238206	1	3	theme	plasma	270:275	arg1	membrane					277:284	the plasma membrane	266:284	the plasma membrane	266:284	Prohibitin (PHB or PHB1) is an evolutionarily conserved, multifunctional protein which is present in various cellular compartments including the plasma membrane.
19238206	10	4	theme	growth	1766:1771	arg1	factors					1773:1779	growth factors	1766:1779	growth factors	1766:1779	We speculate that O-GlcNAc modification and tyrosine phosphorylation of PHB play an important role in tyrosine kinase signaling pathways including insulin, growth factors and immune receptors signaling.
19238206	8	5	theme	Ser121	1145:1150	arg1	Substitution					1129:1140	Substitution	1129:1140	Substitution of Ser121 and Thr258 with alanine and isoleucine	1129:1189	Substitution of Ser121 and Thr258 with alanine and isoleucine respectively resulted in attenuation of O-GlcNAc modification and increased tyrosine phosphorylation of PHB suggesting an association between these two dynamic modifications.
19238206	8	6	theme	Thr258	1156:1161	arg1	Substitution					1129:1140	Substitution	1129:1140	Substitution of Ser121 and Thr258 with alanine and isoleucine	1129:1189	Substitution of Ser121 and Thr258 with alanine and isoleucine respectively resulted in attenuation of O-GlcNAc modification and increased tyrosine phosphorylation of PHB suggesting an association between these two dynamic modifications.
19238206	8	7	theme	O-GlcNAc	1231:1238	arg1	modification					1240:1251	O-GlcNAc modification	1231:1251	O-GlcNAc modification	1231:1251	Substitution of Ser121 and Thr258 with alanine and isoleucine respectively resulted in attenuation of O-GlcNAc modification and increased tyrosine phosphorylation of PHB suggesting an association between these two dynamic modifications.
19238206	3	8	theme	tyrosine	549:556	arg1	phosphorylation					558:572	tyrosine phosphorylation	549:572	tyrosine phosphorylation	549:572	Here we report for the first time that PHB interacts with O-linked beta-N-acetylglucosamine transferase (O-GlcNAc transferase, OGT) and is O-GlcNAc modified; and also undergoes tyrosine phosphorylation in response to insulin.
19238206	9	9	theme	known	1460:1464	arg1	s					1496:1496	s	1496:1496	s	1496:1496	Sequence analysis of O-GlcNAc modified proteins having known O-GlcNAc modification site(s) or known tyrosine phosphorylation site(s) revealed a strong potential association between these two posttranslational modifications in various proteins.
19238206	9	9	theme	known	1460:1464	arg1	site					1491:1494	known tyrosine phosphorylation site	1460:1494	known tyrosine phosphorylation site(s)	1460:1497	Sequence analysis of O-GlcNAc modified proteins having known O-GlcNAc modification site(s) or known tyrosine phosphorylation site(s) revealed a strong potential association between these two posttranslational modifications in various proteins.
19238206	4	10	theme	close	664:668	arg1	proximity					670:678	the close proximity	660:678	the close proximity of potential O-GlcNAc sites serine 121 (Ser121) and threonine 258 (Thr258) respectively	660:766	Tyrosine 114 (Tyr114) and tyrosine 259 (Tyr259) in PHB are in the close proximity of potential O-GlcNAc sites serine 121 (Ser121) and threonine 258 (Thr258) respectively.
19238206	1	11	attach	present	215:221	arg2	present					215:221	present	215:221	present	215:221	Prohibitin (PHB or PHB1) is an evolutionarily conserved, multifunctional protein which is present in various cellular compartments including the plasma membrane.
19238206	1	11	attach	present	215:221	arg2	protein					198:204	an evolutionarily conserved, multifunctional protein	153:204	an evolutionarily conserved, multifunctional protein which is present in various cellular compartments including the plasma membrane	153:284	Prohibitin (PHB or PHB1) is an evolutionarily conserved, multifunctional protein which is present in various cellular compartments including the plasma membrane.
19238206	1	11	attach	present	215:221	arg1	membrane					277:284	the plasma membrane	266:284	the plasma membrane	266:284	Prohibitin (PHB or PHB1) is an evolutionarily conserved, multifunctional protein which is present in various cellular compartments including the plasma membrane.
19238206	1	11	attach	present	215:221	arg2	Prohibitin					125:134	Prohibitin	125:134	Prohibitin (PHB or PHB1)	125:148	Prohibitin (PHB or PHB1) is an evolutionarily conserved, multifunctional protein which is present in various cellular compartments including the plasma membrane.
19238206	1	11	attach	present	215:221	arg1	compartments					243:254	various cellular compartments	226:254	various cellular compartments including the plasma membrane	226:284	Prohibitin (PHB or PHB1) is an evolutionarily conserved, multifunctional protein which is present in various cellular compartments including the plasma membrane.
19238206	9	12	theme	phosphorylation	1475:1489	arg1	s					1496:1496	s	1496:1496	s	1496:1496	Sequence analysis of O-GlcNAc modified proteins having known O-GlcNAc modification site(s) or known tyrosine phosphorylation site(s) revealed a strong potential association between these two posttranslational modifications in various proteins.
19238206	9	12	theme	phosphorylation	1475:1489	arg1	site					1491:1494	known tyrosine phosphorylation site	1460:1494	known tyrosine phosphorylation site(s)	1460:1497	Sequence analysis of O-GlcNAc modified proteins having known O-GlcNAc modification site(s) or known tyrosine phosphorylation site(s) revealed a strong potential association between these two posttranslational modifications in various proteins.
19238206	8	13	theme	tyrosine	1267:1274	arg1	phosphorylation					1276:1290	increased tyrosine phosphorylation	1257:1290	increased tyrosine phosphorylation of PHB	1257:1297	Substitution of Ser121 and Thr258 with alanine and isoleucine respectively resulted in attenuation of O-GlcNAc modification and increased tyrosine phosphorylation of PHB suggesting an association between these two dynamic modifications.
19238206	11	14	theme	signaling	1995:2003	arg1	pathways					2005:2012	cell signaling pathways	1990:2012	cell signaling pathways	1990:2012	In addition, we propose that O-GlcNAc modification and tyrosine phosphorylation is a novel previously unidentified binary switch which may provide new mechanistic insights into cell signaling pathways and is open for direct experimental examination.
19238206	4	15	theme	potential	683:691	arg1	serine					708:713	serine 121	708:717	serine 121 (Ser121)	708:726	Tyrosine 114 (Tyr114) and tyrosine 259 (Tyr259) in PHB are in the close proximity of potential O-GlcNAc sites serine 121 (Ser121) and threonine 258 (Thr258) respectively.
19238206	4	15	theme	potential	683:691	arg1	threonine					732:740	threonine 258	732:744	threonine 258 (Thr258)	732:753	Tyrosine 114 (Tyr114) and tyrosine 259 (Tyr259) in PHB are in the close proximity of potential O-GlcNAc sites serine 121 (Ser121) and threonine 258 (Thr258) respectively.
19238206	4	15	theme	potential	683:691	arg1	sites					702:706	potential O-GlcNAc sites	683:706	potential O-GlcNAc sites serine 121 (Ser121) and threonine 258 (Thr258) respectively	683:766	Tyrosine 114 (Tyr114) and tyrosine 259 (Tyr259) in PHB are in the close proximity of potential O-GlcNAc sites serine 121 (Ser121) and threonine 258 (Thr258) respectively.
19238206	11	16	theme	direct	2030:2035	arg1	examination					2050:2060	direct experimental examination	2030:2060	direct experimental examination	2030:2060	In addition, we propose that O-GlcNAc modification and tyrosine phosphorylation is a novel previously unidentified binary switch which may provide new mechanistic insights into cell signaling pathways and is open for direct experimental examination.
19238206	5	17	theme	tyrosine	886:893	arg1	phosphorylation					895:909	reduced tyrosine phosphorylation	878:909	reduced tyrosine phosphorylation as well as reduced O-GlcNAc modification of PHB	878:957	Substitution of Tyr114 and Tyr259 residues in PHB with phenylalanine by site-directed mutagenesis results in reduced tyrosine phosphorylation as well as reduced O-GlcNAc modification of PHB.
19238206	5	18	theme	reduced	878:884	arg1	phosphorylation					895:909	reduced tyrosine phosphorylation	878:909	reduced tyrosine phosphorylation as well as reduced O-GlcNAc modification of PHB	878:957	Substitution of Tyr114 and Tyr259 residues in PHB with phenylalanine by site-directed mutagenesis results in reduced tyrosine phosphorylation as well as reduced O-GlcNAc modification of PHB.
19238206	0	19	theme	prohibitin	74:83	arg1	modification					29:40	O-GlcNAc modification	20:40	O-GlcNAc modification	20:40	Interaction between O-GlcNAc modification and tyrosine phosphorylation of prohibitin: implication for a novel binary switch.
19238206	0	19	theme	prohibitin	74:83	arg1	phosphorylation					55:69	tyrosine phosphorylation	46:69	tyrosine phosphorylation	46:69	Interaction between O-GlcNAc modification and tyrosine phosphorylation of prohibitin: implication for a novel binary switch.
19238206	11	20	theme	tyrosine	1868:1875	arg1	open					2021:2024	open	2021:2024	open	2021:2024	In addition, we propose that O-GlcNAc modification and tyrosine phosphorylation is a novel previously unidentified binary switch which may provide new mechanistic insights into cell signaling pathways and is open for direct experimental examination.
19238206	11	20	theme	tyrosine	1868:1875	arg1	switch					1935:1940	a novel previously unidentified binary switch	1896:1940	a novel previously unidentified binary switch which may provide new mechanistic insights into cell signaling pathways and is open for direct experimental examination	1896:2060	In addition, we propose that O-GlcNAc modification and tyrosine phosphorylation is a novel previously unidentified binary switch which may provide new mechanistic insights into cell signaling pathways and is open for direct experimental examination.
19238206	11	20	theme	tyrosine	1868:1875	arg1	modification					1851:1862	O-GlcNAc modification	1842:1862	O-GlcNAc modification	1842:1862	In addition, we propose that O-GlcNAc modification and tyrosine phosphorylation is a novel previously unidentified binary switch which may provide new mechanistic insights into cell signaling pathways and is open for direct experimental examination.
19238206	11	20	theme	tyrosine	1868:1875	arg1	phosphorylation					1877:1891	tyrosine phosphorylation	1868:1891	tyrosine phosphorylation	1868:1891	In addition, we propose that O-GlcNAc modification and tyrosine phosphorylation is a novel previously unidentified binary switch which may provide new mechanistic insights into cell signaling pathways and is open for direct experimental examination.
19238206	4	21	from	Tyrosine	598:605	arg1	PHB					649:651	PHB	649:651	PHB	649:651	Tyrosine 114 (Tyr114) and tyrosine 259 (Tyr259) in PHB are in the close proximity of potential O-GlcNAc sites serine 121 (Ser121) and threonine 258 (Thr258) respectively.
19238206	9	22	theme	potential	1517:1525	arg1	association					1527:1537	a strong potential association	1508:1537	a strong potential association between these two posttranslational modifications in various proteins	1508:1607	Sequence analysis of O-GlcNAc modified proteins having known O-GlcNAc modification site(s) or known tyrosine phosphorylation site(s) revealed a strong potential association between these two posttranslational modifications in various proteins.
19238206	3	23	dep	transferase	486:496	arg1	OGT					499:501	OGT	499:501	OGT	499:501	Here we report for the first time that PHB interacts with O-linked beta-N-acetylglucosamine transferase (O-GlcNAc transferase, OGT) and is O-GlcNAc modified; and also undergoes tyrosine phosphorylation in response to insulin.
19238206	8	24	theme	dynamic	1343:1349	arg1	modifications					1351:1363	these two dynamic modifications	1333:1363	these two dynamic modifications	1333:1363	Substitution of Ser121 and Thr258 with alanine and isoleucine respectively resulted in attenuation of O-GlcNAc modification and increased tyrosine phosphorylation of PHB suggesting an association between these two dynamic modifications.
19238206	10	25	theme	PHB	1682:1684	arg1	modification					1637:1648	O-GlcNAc modification	1628:1648	O-GlcNAc modification	1628:1648	We speculate that O-GlcNAc modification and tyrosine phosphorylation of PHB play an important role in tyrosine kinase signaling pathways including insulin, growth factors and immune receptors signaling.
19238206	10	25	theme	PHB	1682:1684	arg1	phosphorylation					1663:1677	tyrosine phosphorylation	1654:1677	tyrosine phosphorylation	1654:1677	We speculate that O-GlcNAc modification and tyrosine phosphorylation of PHB play an important role in tyrosine kinase signaling pathways including insulin, growth factors and immune receptors signaling.
19238206	0	26	theme	binary	110:115	arg1	switch					117:122	a novel binary switch	102:122	a novel binary switch	102:122	Interaction between O-GlcNAc modification and tyrosine phosphorylation of prohibitin: implication for a novel binary switch.
19238206	6	27	theme	OGT	1046:1048	arg1	phosphorylation					1014:1028	enhanced tyrosine phosphorylation	996:1028	enhanced tyrosine phosphorylation	996:1028	Surprisingly, this also resulted in enhanced tyrosine phosphorylation and activity of OGT.
19238206	6	27	theme	OGT	1046:1048	arg1	activity					1034:1041	activity	1034:1041	activity	1034:1041	Surprisingly, this also resulted in enhanced tyrosine phosphorylation and activity of OGT.
19238206	9	28	theme	strong	1510:1515	arg1	association					1527:1537	a strong potential association	1508:1537	a strong potential association between these two posttranslational modifications in various proteins	1508:1607	Sequence analysis of O-GlcNAc modified proteins having known O-GlcNAc modification site(s) or known tyrosine phosphorylation site(s) revealed a strong potential association between these two posttranslational modifications in various proteins.
19238206	4	29	theme	sites	702:706	arg1	proximity					670:678	the close proximity	660:678	the close proximity of potential O-GlcNAc sites serine 121 (Ser121) and threonine 258 (Thr258) respectively	660:766	Tyrosine 114 (Tyr114) and tyrosine 259 (Tyr259) in PHB are in the close proximity of potential O-GlcNAc sites serine 121 (Ser121) and threonine 258 (Thr258) respectively.
19238206	0	30	theme	O-GlcNAc	20:27	arg1	modification					29:40	O-GlcNAc modification	20:40	O-GlcNAc modification	20:40	Interaction between O-GlcNAc modification and tyrosine phosphorylation of prohibitin: implication for a novel binary switch.
19238206	9	31	theme	various	1592:1598	arg1	proteins					1600:1607	various proteins	1592:1607	various proteins	1592:1607	Sequence analysis of O-GlcNAc modified proteins having known O-GlcNAc modification site(s) or known tyrosine phosphorylation site(s) revealed a strong potential association between these two posttranslational modifications in various proteins.
19238206	3	32	theme	first	395:399	arg1	time					401:404	the first time that PHB interacts with O-linked beta-N-acetylglucosamine transferase (O-GlcNAc transferase, OGT) and is O-GlcNAc modified; and also undergoes tyrosine phosphorylation in response to insulin	391:595	the first time that PHB interacts with O-linked beta-N-acetylglucosamine transferase (O-GlcNAc transferase, OGT) and is O-GlcNAc modified; and also undergoes tyrosine phosphorylation in response to insulin	391:595	Here we report for the first time that PHB interacts with O-linked beta-N-acetylglucosamine transferase (O-GlcNAc transferase, OGT) and is O-GlcNAc modified; and also undergoes tyrosine phosphorylation in response to insulin.
19238206	11	33	theme	new	1960:1962	arg1	insights					1976:1983	new mechanistic insights	1960:1983	new mechanistic insights into cell signaling pathways	1960:2012	In addition, we propose that O-GlcNAc modification and tyrosine phosphorylation is a novel previously unidentified binary switch which may provide new mechanistic insights into cell signaling pathways and is open for direct experimental examination.
19238206	1	34	dep	conserved	171:179	arg1	multifunctional					182:196	multifunctional	182:196	multifunctional	182:196	Prohibitin (PHB or PHB1) is an evolutionarily conserved, multifunctional protein which is present in various cellular compartments including the plasma membrane.
19238206	3	35	theme	O-linked	430:437	arg1	transferase					464:474	O-linked beta-N-acetylglucosamine transferase	430:474	O-linked beta-N-acetylglucosamine transferase (O-GlcNAc transferase, OGT)	430:502	Here we report for the first time that PHB interacts with O-linked beta-N-acetylglucosamine transferase (O-GlcNAc transferase, OGT) and is O-GlcNAc modified; and also undergoes tyrosine phosphorylation in response to insulin.
19238206	3	35	theme	O-linked	430:437	arg1	transferase					486:496	O-GlcNAc transferase	477:496	O-GlcNAc transferase	477:496	Here we report for the first time that PHB interacts with O-linked beta-N-acetylglucosamine transferase (O-GlcNAc transferase, OGT) and is O-GlcNAc modified; and also undergoes tyrosine phosphorylation in response to insulin.
19238206	1	36	located	present	215:221	arg2	present					215:221	present	215:221	present	215:221	Prohibitin (PHB or PHB1) is an evolutionarily conserved, multifunctional protein which is present in various cellular compartments including the plasma membrane.
19238206	1	36	located	present	215:221	arg2	protein					198:204	an evolutionarily conserved, multifunctional protein	153:204	an evolutionarily conserved, multifunctional protein which is present in various cellular compartments including the plasma membrane	153:284	Prohibitin (PHB or PHB1) is an evolutionarily conserved, multifunctional protein which is present in various cellular compartments including the plasma membrane.
19238206	1	36	located	present	215:221	arg1	membrane					277:284	the plasma membrane	266:284	the plasma membrane	266:284	Prohibitin (PHB or PHB1) is an evolutionarily conserved, multifunctional protein which is present in various cellular compartments including the plasma membrane.
19238206	1	36	located	present	215:221	arg2	Prohibitin					125:134	Prohibitin	125:134	Prohibitin (PHB or PHB1)	125:148	Prohibitin (PHB or PHB1) is an evolutionarily conserved, multifunctional protein which is present in various cellular compartments including the plasma membrane.
19238206	1	36	located	present	215:221	arg1	compartments					243:254	various cellular compartments	226:254	various cellular compartments including the plasma membrane	226:284	Prohibitin (PHB or PHB1) is an evolutionarily conserved, multifunctional protein which is present in various cellular compartments including the plasma membrane.
19238206	6	37	theme	enhanced	996:1003	arg1	phosphorylation					1014:1028	enhanced tyrosine phosphorylation	996:1028	enhanced tyrosine phosphorylation	996:1028	Surprisingly, this also resulted in enhanced tyrosine phosphorylation and activity of OGT.
19238206	7	38	from	presence	1077:1084	arg1	OGT					1124:1126	OGT	1124:1126	OGT	1124:1126	This is attributed to the presence of similar tyrosine motifs in PHB and OGT.
19238206	7	38	from	presence	1077:1084	arg1	PHB					1116:1118	PHB	1116:1118	PHB	1116:1118	This is attributed to the presence of similar tyrosine motifs in PHB and OGT.
19238206	5	39	with	PHB	815:817	arg1	phenylalanine					824:836	phenylalanine	824:836	phenylalanine	824:836	Substitution of Tyr114 and Tyr259 residues in PHB with phenylalanine by site-directed mutagenesis results in reduced tyrosine phosphorylation as well as reduced O-GlcNAc modification of PHB.
19238206	10	40	theme	signaling	1728:1736	arg1	receptors					1792:1800	immune receptors	1785:1800	immune receptors	1785:1800	We speculate that O-GlcNAc modification and tyrosine phosphorylation of PHB play an important role in tyrosine kinase signaling pathways including insulin, growth factors and immune receptors signaling.
19238206	10	40	theme	signaling	1728:1736	arg1	insulin					1757:1763	insulin	1757:1763	insulin	1757:1763	We speculate that O-GlcNAc modification and tyrosine phosphorylation of PHB play an important role in tyrosine kinase signaling pathways including insulin, growth factors and immune receptors signaling.
19238206	10	40	theme	signaling	1728:1736	arg1	factors					1773:1779	growth factors	1766:1779	growth factors	1766:1779	We speculate that O-GlcNAc modification and tyrosine phosphorylation of PHB play an important role in tyrosine kinase signaling pathways including insulin, growth factors and immune receptors signaling.
19238206	10	40	theme	signaling	1728:1736	arg1	pathways					1738:1745	tyrosine kinase signaling pathways	1712:1745	tyrosine kinase signaling pathways including insulin, growth factors and immune receptors signaling	1712:1810	We speculate that O-GlcNAc modification and tyrosine phosphorylation of PHB play an important role in tyrosine kinase signaling pathways including insulin, growth factors and immune receptors signaling.
19238206	7	41	theme	motifs	1106:1111	arg1	presence					1077:1084	the presence	1073:1084	the presence of similar tyrosine motifs in PHB and OGT	1073:1126	This is attributed to the presence of similar tyrosine motifs in PHB and OGT.
19238206	9	42	theme	Sequence	1366:1373	arg1	analysis					1375:1382	Sequence analysis	1366:1382	Sequence analysis of O-GlcNAc modified proteins having known O-GlcNAc modification site(s) or known tyrosine phosphorylation site(s)	1366:1497	Sequence analysis of O-GlcNAc modified proteins having known O-GlcNAc modification site(s) or known tyrosine phosphorylation site(s) revealed a strong potential association between these two posttranslational modifications in various proteins.
19238206	10	43	theme	tyrosine	1712:1719	arg1	receptors					1792:1800	immune receptors	1785:1800	immune receptors	1785:1800	We speculate that O-GlcNAc modification and tyrosine phosphorylation of PHB play an important role in tyrosine kinase signaling pathways including insulin, growth factors and immune receptors signaling.
19238206	10	43	theme	tyrosine	1712:1719	arg1	insulin					1757:1763	insulin	1757:1763	insulin	1757:1763	We speculate that O-GlcNAc modification and tyrosine phosphorylation of PHB play an important role in tyrosine kinase signaling pathways including insulin, growth factors and immune receptors signaling.
19238206	10	43	theme	tyrosine	1712:1719	arg1	factors					1773:1779	growth factors	1766:1779	growth factors	1766:1779	We speculate that O-GlcNAc modification and tyrosine phosphorylation of PHB play an important role in tyrosine kinase signaling pathways including insulin, growth factors and immune receptors signaling.
19238206	10	43	theme	tyrosine	1712:1719	arg1	pathways					1738:1745	tyrosine kinase signaling pathways	1712:1745	tyrosine kinase signaling pathways including insulin, growth factors and immune receptors signaling	1712:1810	We speculate that O-GlcNAc modification and tyrosine phosphorylation of PHB play an important role in tyrosine kinase signaling pathways including insulin, growth factors and immune receptors signaling.
19238206	11	44	theme	mechanistic	1964:1974	arg1	insights					1976:1983	new mechanistic insights	1960:1983	new mechanistic insights into cell signaling pathways	1960:2012	In addition, we propose that O-GlcNAc modification and tyrosine phosphorylation is a novel previously unidentified binary switch which may provide new mechanistic insights into cell signaling pathways and is open for direct experimental examination.
19238206	11	45	theme	unidentified	1915:1926	arg1	open					2021:2024	open	2021:2024	open	2021:2024	In addition, we propose that O-GlcNAc modification and tyrosine phosphorylation is a novel previously unidentified binary switch which may provide new mechanistic insights into cell signaling pathways and is open for direct experimental examination.
19238206	11	45	theme	unidentified	1915:1926	arg1	switch					1935:1940	a novel previously unidentified binary switch	1896:1940	a novel previously unidentified binary switch which may provide new mechanistic insights into cell signaling pathways and is open for direct experimental examination	1896:2060	In addition, we propose that O-GlcNAc modification and tyrosine phosphorylation is a novel previously unidentified binary switch which may provide new mechanistic insights into cell signaling pathways and is open for direct experimental examination.
19238206	11	45	theme	unidentified	1915:1926	arg1	modification					1851:1862	O-GlcNAc modification	1842:1862	O-GlcNAc modification	1842:1862	In addition, we propose that O-GlcNAc modification and tyrosine phosphorylation is a novel previously unidentified binary switch which may provide new mechanistic insights into cell signaling pathways and is open for direct experimental examination.
19238206	11	45	theme	unidentified	1915:1926	arg1	phosphorylation					1877:1891	tyrosine phosphorylation	1868:1891	tyrosine phosphorylation	1868:1891	In addition, we propose that O-GlcNAc modification and tyrosine phosphorylation is a novel previously unidentified binary switch which may provide new mechanistic insights into cell signaling pathways and is open for direct experimental examination.
19238206	9	46	theme	modified	1396:1403	arg1	proteins					1405:1412	O-GlcNAc modified proteins	1387:1412	O-GlcNAc modified proteins having known O-GlcNAc modification site(s) or known tyrosine phosphorylation site(s)	1387:1497	Sequence analysis of O-GlcNAc modified proteins having known O-GlcNAc modification site(s) or known tyrosine phosphorylation site(s) revealed a strong potential association between these two posttranslational modifications in various proteins.
19238206	0	47	dep	Interaction	0:10	arg1	implication					86:96	implication	86:96	Interaction between O-GlcNAc modification and tyrosine phosphorylation of prohibitin: implication for a novel binary switch.	0:123	Interaction between O-GlcNAc modification and tyrosine phosphorylation of prohibitin: implication for a novel binary switch.
19238206	0	48	mod	modification	29:40	arg1	prohibitin					74:83	prohibitin	74:83	prohibitin	74:83	Interaction between O-GlcNAc modification and tyrosine phosphorylation of prohibitin: implication for a novel binary switch.
19238206	0	48	mod	modification	29:40	arg3	O-GlcNAc					20:27	O-GlcNAc modification	20:40	O-GlcNAc modification	20:40	Interaction between O-GlcNAc modification and tyrosine phosphorylation of prohibitin: implication for a novel binary switch.
19238206	11	49	theme	novel	1898:1902	arg1	open					2021:2024	open	2021:2024	open	2021:2024	In addition, we propose that O-GlcNAc modification and tyrosine phosphorylation is a novel previously unidentified binary switch which may provide new mechanistic insights into cell signaling pathways and is open for direct experimental examination.
19238206	11	49	theme	novel	1898:1902	arg1	switch					1935:1940	a novel previously unidentified binary switch	1896:1940	a novel previously unidentified binary switch which may provide new mechanistic insights into cell signaling pathways and is open for direct experimental examination	1896:2060	In addition, we propose that O-GlcNAc modification and tyrosine phosphorylation is a novel previously unidentified binary switch which may provide new mechanistic insights into cell signaling pathways and is open for direct experimental examination.
19238206	11	49	theme	novel	1898:1902	arg1	modification					1851:1862	O-GlcNAc modification	1842:1862	O-GlcNAc modification	1842:1862	In addition, we propose that O-GlcNAc modification and tyrosine phosphorylation is a novel previously unidentified binary switch which may provide new mechanistic insights into cell signaling pathways and is open for direct experimental examination.
19238206	11	49	theme	novel	1898:1902	arg1	phosphorylation					1877:1891	tyrosine phosphorylation	1868:1891	tyrosine phosphorylation	1868:1891	In addition, we propose that O-GlcNAc modification and tyrosine phosphorylation is a novel previously unidentified binary switch which may provide new mechanistic insights into cell signaling pathways and is open for direct experimental examination.
19238206	7	50	attach	presence	1077:1084	arg1	OGT					1124:1126	OGT	1124:1126	OGT	1124:1126	This is attributed to the presence of similar tyrosine motifs in PHB and OGT.
19238206	7	50	attach	presence	1077:1084	arg1	PHB					1116:1118	PHB	1116:1118	PHB	1116:1118	This is attributed to the presence of similar tyrosine motifs in PHB and OGT.
19238206	7	50	attach	presence	1077:1084	arg2	motifs					1106:1111	similar tyrosine motifs	1089:1111	similar tyrosine motifs	1089:1111	This is attributed to the presence of similar tyrosine motifs in PHB and OGT.
19238206	10	51	theme	immune	1785:1790	arg1	receptors					1792:1800	immune receptors	1785:1800	immune receptors	1785:1800	We speculate that O-GlcNAc modification and tyrosine phosphorylation of PHB play an important role in tyrosine kinase signaling pathways including insulin, growth factors and immune receptors signaling.
19238206	9	52	theme	O-GlcNAc	1427:1434	arg1	s					1454:1454	s	1454:1454	s	1454:1454	Sequence analysis of O-GlcNAc modified proteins having known O-GlcNAc modification site(s) or known tyrosine phosphorylation site(s) revealed a strong potential association between these two posttranslational modifications in various proteins.
19238206	9	52	theme	O-GlcNAc	1427:1434	arg1	site					1449:1452	known O-GlcNAc modification site	1421:1452	known O-GlcNAc modification site(s)	1421:1455	Sequence analysis of O-GlcNAc modified proteins having known O-GlcNAc modification site(s) or known tyrosine phosphorylation site(s) revealed a strong potential association between these two posttranslational modifications in various proteins.
19238206	5	53	mod	modification	939:950	arg1	PHB					955:957	PHB	955:957	PHB	955:957	Substitution of Tyr114 and Tyr259 residues in PHB with phenylalanine by site-directed mutagenesis results in reduced tyrosine phosphorylation as well as reduced O-GlcNAc modification of PHB.
19238206	5	53	mod	modification	939:950	arg3	O-GlcNAc					930:937	reduced O-GlcNAc modification	922:950	reduced tyrosine phosphorylation as well as reduced O-GlcNAc modification of PHB	878:957	Substitution of Tyr114 and Tyr259 residues in PHB with phenylalanine by site-directed mutagenesis results in reduced tyrosine phosphorylation as well as reduced O-GlcNAc modification of PHB.
19238206	11	54	theme	experimental	2037:2048	arg1	examination					2050:2060	direct experimental examination	2030:2060	direct experimental examination	2030:2060	In addition, we propose that O-GlcNAc modification and tyrosine phosphorylation is a novel previously unidentified binary switch which may provide new mechanistic insights into cell signaling pathways and is open for direct experimental examination.
19238206	1	55	theme	conserved	171:179	arg1	protein					198:204	an evolutionarily conserved, multifunctional protein	153:204	an evolutionarily conserved, multifunctional protein which is present in various cellular compartments including the plasma membrane	153:284	Prohibitin (PHB or PHB1) is an evolutionarily conserved, multifunctional protein which is present in various cellular compartments including the plasma membrane.
19238206	1	55	theme	conserved	171:179	arg1	present					215:221	present	215:221	present	215:221	Prohibitin (PHB or PHB1) is an evolutionarily conserved, multifunctional protein which is present in various cellular compartments including the plasma membrane.
19238206	1	55	theme	conserved	171:179	arg1	Prohibitin					125:134	Prohibitin	125:134	Prohibitin (PHB or PHB1)	125:148	Prohibitin (PHB or PHB1) is an evolutionarily conserved, multifunctional protein which is present in various cellular compartments including the plasma membrane.
19238206	5	56	theme	residues	803:810	arg1	Substitution					769:780	Substitution	769:780	Substitution of Tyr114 and Tyr259 residues in PHB with phenylalanine by site-directed mutagenesis	769:865	Substitution of Tyr114 and Tyr259 residues in PHB with phenylalanine by site-directed mutagenesis results in reduced tyrosine phosphorylation as well as reduced O-GlcNAc modification of PHB.
19238206	2	57	theme	various	319:325	arg1	functions					327:335	various functions	319:335	various functions of PHB	319:342	However, mechanisms involved in various functions of PHB are not fully explored yet.
19238206	3	58	dep	insulin	589:595	arg1	response					577:584	response	577:584	response	577:584	Here we report for the first time that PHB interacts with O-linked beta-N-acetylglucosamine transferase (O-GlcNAc transferase, OGT) and is O-GlcNAc modified; and also undergoes tyrosine phosphorylation in response to insulin.
19238206	9	59	contain	having	1414:1419	arg2	s					1454:1454	s	1454:1454	s	1454:1454	Sequence analysis of O-GlcNAc modified proteins having known O-GlcNAc modification site(s) or known tyrosine phosphorylation site(s) revealed a strong potential association between these two posttranslational modifications in various proteins.
19238206	9	59	contain	having	1414:1419	arg2	site					1491:1494	known tyrosine phosphorylation site	1460:1494	known tyrosine phosphorylation site(s)	1460:1497	Sequence analysis of O-GlcNAc modified proteins having known O-GlcNAc modification site(s) or known tyrosine phosphorylation site(s) revealed a strong potential association between these two posttranslational modifications in various proteins.
19238206	9	59	contain	having	1414:1419	arg2	s					1496:1496	s	1496:1496	s	1496:1496	Sequence analysis of O-GlcNAc modified proteins having known O-GlcNAc modification site(s) or known tyrosine phosphorylation site(s) revealed a strong potential association between these two posttranslational modifications in various proteins.
19238206	9	59	contain	having	1414:1419	arg1	proteins					1405:1412	O-GlcNAc modified proteins	1387:1412	O-GlcNAc modified proteins having known O-GlcNAc modification site(s) or known tyrosine phosphorylation site(s)	1387:1497	Sequence analysis of O-GlcNAc modified proteins having known O-GlcNAc modification site(s) or known tyrosine phosphorylation site(s) revealed a strong potential association between these two posttranslational modifications in various proteins.
19238206	9	59	contain	having	1414:1419	arg2	site					1449:1452	known O-GlcNAc modification site	1421:1452	known O-GlcNAc modification site(s)	1421:1455	Sequence analysis of O-GlcNAc modified proteins having known O-GlcNAc modification site(s) or known tyrosine phosphorylation site(s) revealed a strong potential association between these two posttranslational modifications in various proteins.
19238206	4	60	from	tyrosine	624:631	arg1	PHB					649:651	PHB	649:651	PHB	649:651	Tyrosine 114 (Tyr114) and tyrosine 259 (Tyr259) in PHB are in the close proximity of potential O-GlcNAc sites serine 121 (Ser121) and threonine 258 (Thr258) respectively.
19238206	2	61	theme	PHB	340:342	arg1	functions					327:335	various functions	319:335	various functions of PHB	319:342	However, mechanisms involved in various functions of PHB are not fully explored yet.
19238206	1	62	from	compartments	243:254	arg1	protein					198:204	an evolutionarily conserved, multifunctional protein	153:204	an evolutionarily conserved, multifunctional protein which is present in various cellular compartments including the plasma membrane	153:284	Prohibitin (PHB or PHB1) is an evolutionarily conserved, multifunctional protein which is present in various cellular compartments including the plasma membrane.
19238206	1	62	from	compartments	243:254	arg1	present					215:221	present	215:221	present	215:221	Prohibitin (PHB or PHB1) is an evolutionarily conserved, multifunctional protein which is present in various cellular compartments including the plasma membrane.
19238206	1	62	from	compartments	243:254	arg1	Prohibitin					125:134	Prohibitin	125:134	Prohibitin (PHB or PHB1)	125:148	Prohibitin (PHB or PHB1) is an evolutionarily conserved, multifunctional protein which is present in various cellular compartments including the plasma membrane.
19238206	9	63	theme	tyrosine	1466:1473	arg1	s					1496:1496	s	1496:1496	s	1496:1496	Sequence analysis of O-GlcNAc modified proteins having known O-GlcNAc modification site(s) or known tyrosine phosphorylation site(s) revealed a strong potential association between these two posttranslational modifications in various proteins.
19238206	9	63	theme	tyrosine	1466:1473	arg1	site					1491:1494	known tyrosine phosphorylation site	1460:1494	known tyrosine phosphorylation site(s)	1460:1497	Sequence analysis of O-GlcNAc modified proteins having known O-GlcNAc modification site(s) or known tyrosine phosphorylation site(s) revealed a strong potential association between these two posttranslational modifications in various proteins.
19238206	8	64	theme	modification	1240:1251	arg1	phosphorylation					1276:1290	increased tyrosine phosphorylation	1257:1290	increased tyrosine phosphorylation of PHB	1257:1297	Substitution of Ser121 and Thr258 with alanine and isoleucine respectively resulted in attenuation of O-GlcNAc modification and increased tyrosine phosphorylation of PHB suggesting an association between these two dynamic modifications.
19238206	8	64	theme	modification	1240:1251	arg1	attenuation					1216:1226	attenuation	1216:1226	attenuation of O-GlcNAc modification	1216:1251	Substitution of Ser121 and Thr258 with alanine and isoleucine respectively resulted in attenuation of O-GlcNAc modification and increased tyrosine phosphorylation of PHB suggesting an association between these two dynamic modifications.
19238206	10	65	theme	O-GlcNAc	1628:1635	arg1	modification					1637:1648	O-GlcNAc modification	1628:1648	O-GlcNAc modification	1628:1648	We speculate that O-GlcNAc modification and tyrosine phosphorylation of PHB play an important role in tyrosine kinase signaling pathways including insulin, growth factors and immune receptors signaling.
19238206	11	66	theme	cell	1990:1993	arg1	pathways					2005:2012	cell signaling pathways	1990:2012	cell signaling pathways	1990:2012	In addition, we propose that O-GlcNAc modification and tyrosine phosphorylation is a novel previously unidentified binary switch which may provide new mechanistic insights into cell signaling pathways and is open for direct experimental examination.
19238206	8	67	theme	increased	1257:1265	arg1	phosphorylation					1276:1290	increased tyrosine phosphorylation	1257:1290	increased tyrosine phosphorylation of PHB	1257:1297	Substitution of Ser121 and Thr258 with alanine and isoleucine respectively resulted in attenuation of O-GlcNAc modification and increased tyrosine phosphorylation of PHB suggesting an association between these two dynamic modifications.
19238206	11	68	theme	O-GlcNAc	1842:1849	arg1	open					2021:2024	open	2021:2024	open	2021:2024	In addition, we propose that O-GlcNAc modification and tyrosine phosphorylation is a novel previously unidentified binary switch which may provide new mechanistic insights into cell signaling pathways and is open for direct experimental examination.
19238206	11	68	theme	O-GlcNAc	1842:1849	arg1	switch					1935:1940	a novel previously unidentified binary switch	1896:1940	a novel previously unidentified binary switch which may provide new mechanistic insights into cell signaling pathways and is open for direct experimental examination	1896:2060	In addition, we propose that O-GlcNAc modification and tyrosine phosphorylation is a novel previously unidentified binary switch which may provide new mechanistic insights into cell signaling pathways and is open for direct experimental examination.
19238206	11	68	theme	O-GlcNAc	1842:1849	arg1	modification					1851:1862	O-GlcNAc modification	1842:1862	O-GlcNAc modification	1842:1862	In addition, we propose that O-GlcNAc modification and tyrosine phosphorylation is a novel previously unidentified binary switch which may provide new mechanistic insights into cell signaling pathways and is open for direct experimental examination.
19238206	11	68	theme	O-GlcNAc	1842:1849	arg1	phosphorylation					1877:1891	tyrosine phosphorylation	1868:1891	tyrosine phosphorylation	1868:1891	In addition, we propose that O-GlcNAc modification and tyrosine phosphorylation is a novel previously unidentified binary switch which may provide new mechanistic insights into cell signaling pathways and is open for direct experimental examination.
19238206	1	69	from	present	215:221	arg1	membrane					277:284	the plasma membrane	266:284	the plasma membrane	266:284	Prohibitin (PHB or PHB1) is an evolutionarily conserved, multifunctional protein which is present in various cellular compartments including the plasma membrane.
19238206	1	69	from	present	215:221	arg1	compartments					243:254	various cellular compartments	226:254	various cellular compartments including the plasma membrane	226:284	Prohibitin (PHB or PHB1) is an evolutionarily conserved, multifunctional protein which is present in various cellular compartments including the plasma membrane.
19238206	4	70	dep	sites	702:706	arg1	serine					708:713	serine 121	708:717	serine 121 (Ser121)	708:726	Tyrosine 114 (Tyr114) and tyrosine 259 (Tyr259) in PHB are in the close proximity of potential O-GlcNAc sites serine 121 (Ser121) and threonine 258 (Thr258) respectively.
19238206	4	70	dep	sites	702:706	arg1	Ser121					720:725	Ser121	720:725	Ser121	720:725	Tyrosine 114 (Tyr114) and tyrosine 259 (Tyr259) in PHB are in the close proximity of potential O-GlcNAc sites serine 121 (Ser121) and threonine 258 (Thr258) respectively.
19238206	4	70	dep	sites	702:706	arg1	threonine					732:740	threonine 258	732:744	threonine 258 (Thr258)	732:753	Tyrosine 114 (Tyr114) and tyrosine 259 (Tyr259) in PHB are in the close proximity of potential O-GlcNAc sites serine 121 (Ser121) and threonine 258 (Thr258) respectively.
19238206	4	70	dep	sites	702:706	arg1	Thr258					747:752	Thr258	747:752	Thr258	747:752	Tyrosine 114 (Tyr114) and tyrosine 259 (Tyr259) in PHB are in the close proximity of potential O-GlcNAc sites serine 121 (Ser121) and threonine 258 (Thr258) respectively.
19238206	4	70	dep	sites	702:706	arg1	sites					702:706	potential O-GlcNAc sites	683:706	potential O-GlcNAc sites serine 121 (Ser121) and threonine 258 (Thr258) respectively	683:766	Tyrosine 114 (Tyr114) and tyrosine 259 (Tyr259) in PHB are in the close proximity of potential O-GlcNAc sites serine 121 (Ser121) and threonine 258 (Thr258) respectively.
19238206	3	71	theme	O-GlcNAc	477:484	arg1	transferase					464:474	O-linked beta-N-acetylglucosamine transferase	430:474	O-linked beta-N-acetylglucosamine transferase (O-GlcNAc transferase, OGT)	430:502	Here we report for the first time that PHB interacts with O-linked beta-N-acetylglucosamine transferase (O-GlcNAc transferase, OGT) and is O-GlcNAc modified; and also undergoes tyrosine phosphorylation in response to insulin.
19238206	3	71	theme	O-GlcNAc	477:484	arg1	transferase					486:496	O-GlcNAc transferase	477:496	O-GlcNAc transferase	477:496	Here we report for the first time that PHB interacts with O-linked beta-N-acetylglucosamine transferase (O-GlcNAc transferase, OGT) and is O-GlcNAc modified; and also undergoes tyrosine phosphorylation in response to insulin.
19238206	9	72	from	modifications	1575:1587	arg1	proteins					1600:1607	various proteins	1592:1607	various proteins	1592:1607	Sequence analysis of O-GlcNAc modified proteins having known O-GlcNAc modification site(s) or known tyrosine phosphorylation site(s) revealed a strong potential association between these two posttranslational modifications in various proteins.
19238206	8	73	theme	PHB	1295:1297	arg1	phosphorylation					1276:1290	increased tyrosine phosphorylation	1257:1290	increased tyrosine phosphorylation of PHB	1257:1297	Substitution of Ser121 and Thr258 with alanine and isoleucine respectively resulted in attenuation of O-GlcNAc modification and increased tyrosine phosphorylation of PHB suggesting an association between these two dynamic modifications.
19238206	8	73	theme	PHB	1295:1297	arg1	attenuation					1216:1226	attenuation	1216:1226	attenuation of O-GlcNAc modification	1216:1251	Substitution of Ser121 and Thr258 with alanine and isoleucine respectively resulted in attenuation of O-GlcNAc modification and increased tyrosine phosphorylation of PHB suggesting an association between these two dynamic modifications.
19238206	5	74	theme	site-directed	841:853	arg1	mutagenesis					855:865	site-directed mutagenesis	841:865	site-directed mutagenesis	841:865	Substitution of Tyr114 and Tyr259 residues in PHB with phenylalanine by site-directed mutagenesis results in reduced tyrosine phosphorylation as well as reduced O-GlcNAc modification of PHB.
19238206	0	75	theme	novel	104:108	arg1	switch					117:122	a novel binary switch	102:122	a novel binary switch	102:122	Interaction between O-GlcNAc modification and tyrosine phosphorylation of prohibitin: implication for a novel binary switch.
19238206	5	76	theme	reduced	922:928	arg1	modification					939:950	reduced O-GlcNAc modification	922:950	reduced tyrosine phosphorylation as well as reduced O-GlcNAc modification of PHB	878:957	Substitution of Tyr114 and Tyr259 residues in PHB with phenylalanine by site-directed mutagenesis results in reduced tyrosine phosphorylation as well as reduced O-GlcNAc modification of PHB.
19238206	5	77	theme	O-GlcNAc	930:937	arg1	modification					939:950	reduced O-GlcNAc modification	922:950	reduced tyrosine phosphorylation as well as reduced O-GlcNAc modification of PHB	878:957	Substitution of Tyr114 and Tyr259 residues in PHB with phenylalanine by site-directed mutagenesis results in reduced tyrosine phosphorylation as well as reduced O-GlcNAc modification of PHB.
19238206	10	78	mod	modification	1637:1648	arg1	PHB					1682:1684	PHB	1682:1684	PHB	1682:1684	We speculate that O-GlcNAc modification and tyrosine phosphorylation of PHB play an important role in tyrosine kinase signaling pathways including insulin, growth factors and immune receptors signaling.
19238206	10	78	mod	modification	1637:1648	arg3	O-GlcNAc					1628:1635	O-GlcNAc modification	1628:1648	O-GlcNAc modification	1628:1648	We speculate that O-GlcNAc modification and tyrosine phosphorylation of PHB play an important role in tyrosine kinase signaling pathways including insulin, growth factors and immune receptors signaling.
19238206	5	79	from	Substitution	769:780	arg1	PHB					815:817	PHB	815:817	PHB with phenylalanine	815:836	Substitution of Tyr114 and Tyr259 residues in PHB with phenylalanine by site-directed mutagenesis results in reduced tyrosine phosphorylation as well as reduced O-GlcNAc modification of PHB.
19238206	9	80	theme	modification	1436:1447	arg1	s					1454:1454	s	1454:1454	s	1454:1454	Sequence analysis of O-GlcNAc modified proteins having known O-GlcNAc modification site(s) or known tyrosine phosphorylation site(s) revealed a strong potential association between these two posttranslational modifications in various proteins.
19238206	9	80	theme	modification	1436:1447	arg1	site					1449:1452	known O-GlcNAc modification site	1421:1452	known O-GlcNAc modification site(s)	1421:1455	Sequence analysis of O-GlcNAc modified proteins having known O-GlcNAc modification site(s) or known tyrosine phosphorylation site(s) revealed a strong potential association between these two posttranslational modifications in various proteins.
19238206	8	81	with	Substitution	1129:1140	arg1	alanine					1168:1174	alanine	1168:1174	alanine	1168:1174	Substitution of Ser121 and Thr258 with alanine and isoleucine respectively resulted in attenuation of O-GlcNAc modification and increased tyrosine phosphorylation of PHB suggesting an association between these two dynamic modifications.
19238206	8	81	with	Substitution	1129:1140	arg1	isoleucine					1180:1189	isoleucine	1180:1189	isoleucine	1180:1189	Substitution of Ser121 and Thr258 with alanine and isoleucine respectively resulted in attenuation of O-GlcNAc modification and increased tyrosine phosphorylation of PHB suggesting an association between these two dynamic modifications.
19238206	1	82	dep	Prohibitin	125:134	arg1	PHB1					144:147	PHB1	144:147	PHB1	144:147	Prohibitin (PHB or PHB1) is an evolutionarily conserved, multifunctional protein which is present in various cellular compartments including the plasma membrane.
19238206	1	82	dep	Prohibitin	125:134	arg1	PHB					137:139	PHB	137:139	PHB	137:139	Prohibitin (PHB or PHB1) is an evolutionarily conserved, multifunctional protein which is present in various cellular compartments including the plasma membrane.
19238206	9	83	theme	posttranslational	1557:1573	arg1	modifications					1575:1587	these two posttranslational modifications	1547:1587	these two posttranslational modifications in various proteins	1547:1607	Sequence analysis of O-GlcNAc modified proteins having known O-GlcNAc modification site(s) or known tyrosine phosphorylation site(s) revealed a strong potential association between these two posttranslational modifications in various proteins.
19238206	4	84	theme	O-GlcNAc	693:700	arg1	serine					708:713	serine 121	708:717	serine 121 (Ser121)	708:726	Tyrosine 114 (Tyr114) and tyrosine 259 (Tyr259) in PHB are in the close proximity of potential O-GlcNAc sites serine 121 (Ser121) and threonine 258 (Thr258) respectively.
19238206	4	84	theme	O-GlcNAc	693:700	arg1	threonine					732:740	threonine 258	732:744	threonine 258 (Thr258)	732:753	Tyrosine 114 (Tyr114) and tyrosine 259 (Tyr259) in PHB are in the close proximity of potential O-GlcNAc sites serine 121 (Ser121) and threonine 258 (Thr258) respectively.
19238206	4	84	theme	O-GlcNAc	693:700	arg1	sites					702:706	potential O-GlcNAc sites	683:706	potential O-GlcNAc sites serine 121 (Ser121) and threonine 258 (Thr258) respectively	683:766	Tyrosine 114 (Tyr114) and tyrosine 259 (Tyr259) in PHB are in the close proximity of potential O-GlcNAc sites serine 121 (Ser121) and threonine 258 (Thr258) respectively.
19238206	10	85	theme	tyrosine	1654:1661	arg1	phosphorylation					1663:1677	tyrosine phosphorylation	1654:1677	tyrosine phosphorylation	1654:1677	We speculate that O-GlcNAc modification and tyrosine phosphorylation of PHB play an important role in tyrosine kinase signaling pathways including insulin, growth factors and immune receptors signaling.
19238206	10	86	theme	important	1694:1702	arg1	role					1704:1707	an important role	1691:1707	an important role	1691:1707	We speculate that O-GlcNAc modification and tyrosine phosphorylation of PHB play an important role in tyrosine kinase signaling pathways including insulin, growth factors and immune receptors signaling.
19238206	0	87	theme	tyrosine	46:53	arg1	phosphorylation					55:69	tyrosine phosphorylation	46:69	tyrosine phosphorylation	46:69	Interaction between O-GlcNAc modification and tyrosine phosphorylation of prohibitin: implication for a novel binary switch.
19238206	6	88	theme	tyrosine	1005:1012	arg1	phosphorylation					1014:1028	enhanced tyrosine phosphorylation	996:1028	enhanced tyrosine phosphorylation	996:1028	Surprisingly, this also resulted in enhanced tyrosine phosphorylation and activity of OGT.
19238206	1	89	theme	various	226:232	arg1	membrane					277:284	the plasma membrane	266:284	the plasma membrane	266:284	Prohibitin (PHB or PHB1) is an evolutionarily conserved, multifunctional protein which is present in various cellular compartments including the plasma membrane.
19238206	1	89	theme	various	226:232	arg1	compartments					243:254	various cellular compartments	226:254	various cellular compartments including the plasma membrane	226:284	Prohibitin (PHB or PHB1) is an evolutionarily conserved, multifunctional protein which is present in various cellular compartments including the plasma membrane.
19238206	3	90	theme	beta-N-acetylglucosamine	439:462	arg1	transferase					464:474	O-linked beta-N-acetylglucosamine transferase	430:474	O-linked beta-N-acetylglucosamine transferase (O-GlcNAc transferase, OGT)	430:502	Here we report for the first time that PHB interacts with O-linked beta-N-acetylglucosamine transferase (O-GlcNAc transferase, OGT) and is O-GlcNAc modified; and also undergoes tyrosine phosphorylation in response to insulin.
19238206	3	90	theme	beta-N-acetylglucosamine	439:462	arg1	transferase					486:496	O-GlcNAc transferase	477:496	O-GlcNAc transferase	477:496	Here we report for the first time that PHB interacts with O-linked beta-N-acetylglucosamine transferase (O-GlcNAc transferase, OGT) and is O-GlcNAc modified; and also undergoes tyrosine phosphorylation in response to insulin.
19238206	7	91	theme	tyrosine	1097:1104	arg1	motifs					1106:1111	similar tyrosine motifs	1089:1111	similar tyrosine motifs	1089:1111	This is attributed to the presence of similar tyrosine motifs in PHB and OGT.
19238206	10	92	theme	kinase	1721:1726	arg1	receptors					1792:1800	immune receptors	1785:1800	immune receptors	1785:1800	We speculate that O-GlcNAc modification and tyrosine phosphorylation of PHB play an important role in tyrosine kinase signaling pathways including insulin, growth factors and immune receptors signaling.
19238206	10	92	theme	kinase	1721:1726	arg1	insulin					1757:1763	insulin	1757:1763	insulin	1757:1763	We speculate that O-GlcNAc modification and tyrosine phosphorylation of PHB play an important role in tyrosine kinase signaling pathways including insulin, growth factors and immune receptors signaling.
19238206	10	92	theme	kinase	1721:1726	arg1	factors					1773:1779	growth factors	1766:1779	growth factors	1766:1779	We speculate that O-GlcNAc modification and tyrosine phosphorylation of PHB play an important role in tyrosine kinase signaling pathways including insulin, growth factors and immune receptors signaling.
19238206	10	92	theme	kinase	1721:1726	arg1	pathways					1738:1745	tyrosine kinase signaling pathways	1712:1745	tyrosine kinase signaling pathways including insulin, growth factors and immune receptors signaling	1712:1810	We speculate that O-GlcNAc modification and tyrosine phosphorylation of PHB play an important role in tyrosine kinase signaling pathways including insulin, growth factors and immune receptors signaling.
19238206	5	93	theme	PHB	955:957	arg1	phosphorylation					895:909	reduced tyrosine phosphorylation	878:909	reduced tyrosine phosphorylation as well as reduced O-GlcNAc modification of PHB	878:957	Substitution of Tyr114 and Tyr259 residues in PHB with phenylalanine by site-directed mutagenesis results in reduced tyrosine phosphorylation as well as reduced O-GlcNAc modification of PHB.
19238206	5	93	theme	PHB	955:957	arg1	modification					939:950	reduced O-GlcNAc modification	922:950	reduced tyrosine phosphorylation as well as reduced O-GlcNAc modification of PHB	878:957	Substitution of Tyr114 and Tyr259 residues in PHB with phenylalanine by site-directed mutagenesis results in reduced tyrosine phosphorylation as well as reduced O-GlcNAc modification of PHB.
19238206	10	94	dep	insulin	1757:1763	arg1	signaling					1802:1810	signaling	1802:1810	signaling	1802:1810	We speculate that O-GlcNAc modification and tyrosine phosphorylation of PHB play an important role in tyrosine kinase signaling pathways including insulin, growth factors and immune receptors signaling.
19238206	1	95	theme	cellular	234:241	arg1	membrane					277:284	the plasma membrane	266:284	the plasma membrane	266:284	Prohibitin (PHB or PHB1) is an evolutionarily conserved, multifunctional protein which is present in various cellular compartments including the plasma membrane.
19238206	1	95	theme	cellular	234:241	arg1	compartments					243:254	various cellular compartments	226:254	various cellular compartments including the plasma membrane	226:284	Prohibitin (PHB or PHB1) is an evolutionarily conserved, multifunctional protein which is present in various cellular compartments including the plasma membrane.
19238206	11	96	theme	binary	1928:1933	arg1	open					2021:2024	open	2021:2024	open	2021:2024	In addition, we propose that O-GlcNAc modification and tyrosine phosphorylation is a novel previously unidentified binary switch which may provide new mechanistic insights into cell signaling pathways and is open for direct experimental examination.
19238206	11	96	theme	binary	1928:1933	arg1	switch					1935:1940	a novel previously unidentified binary switch	1896:1940	a novel previously unidentified binary switch which may provide new mechanistic insights into cell signaling pathways and is open for direct experimental examination	1896:2060	In addition, we propose that O-GlcNAc modification and tyrosine phosphorylation is a novel previously unidentified binary switch which may provide new mechanistic insights into cell signaling pathways and is open for direct experimental examination.
19238206	11	96	theme	binary	1928:1933	arg1	modification					1851:1862	O-GlcNAc modification	1842:1862	O-GlcNAc modification	1842:1862	In addition, we propose that O-GlcNAc modification and tyrosine phosphorylation is a novel previously unidentified binary switch which may provide new mechanistic insights into cell signaling pathways and is open for direct experimental examination.
19238206	11	96	theme	binary	1928:1933	arg1	phosphorylation					1877:1891	tyrosine phosphorylation	1868:1891	tyrosine phosphorylation	1868:1891	In addition, we propose that O-GlcNAc modification and tyrosine phosphorylation is a novel previously unidentified binary switch which may provide new mechanistic insights into cell signaling pathways and is open for direct experimental examination.
19238206	9	97	theme	proteins	1405:1412	arg1	analysis					1375:1382	Sequence analysis	1366:1382	Sequence analysis of O-GlcNAc modified proteins having known O-GlcNAc modification site(s) or known tyrosine phosphorylation site(s)	1366:1497	Sequence analysis of O-GlcNAc modified proteins having known O-GlcNAc modification site(s) or known tyrosine phosphorylation site(s) revealed a strong potential association between these two posttranslational modifications in various proteins.
1512232	7	0	theme	manual	1277:1282	arg1	degradation					1290:1300	manual Edman degradation	1277:1300	manual Edman degradation	1277:1300	Using an array of techniques, including manual Edman degradation, aminopeptidase, and elastase digestion, together with FAB-MS, the major sites of O-GlcNAc attachment were shown to be serine residues within short tandem repeat regions.
1512232	6	1	theme	Fast	857:860	arg1	spectrometry					884:895	Fast atom bombardment mass spectrometry	857:895	Fast atom bombardment mass spectrometry (FAB-MS) of proteolytic digests of SRF	857:934	Fast atom bombardment mass spectrometry (FAB-MS) of proteolytic digests of SRF provides evidence for the presence of a single substoichiometric O-GlcNAc residue on each of four peptides isolated after sequential cyanogen bromide, tryptic, and proline specific enzyme digestion: these peptides are 306VSASVSP312, 274GTTSTIQTAP283, 313SAVSSADGTVLK324, and 374DSSTDLTQTSSSGTVTLP391.
1512232	6	1	theme	Fast	857:860	arg1	FAB-MS					898:903	FAB-MS	898:903	FAB-MS	898:903	Fast atom bombardment mass spectrometry (FAB-MS) of proteolytic digests of SRF provides evidence for the presence of a single substoichiometric O-GlcNAc residue on each of four peptides isolated after sequential cyanogen bromide, tryptic, and proline specific enzyme digestion: these peptides are 306VSASVSP312, 274GTTSTIQTAP283, 313SAVSSADGTVLK324, and 374DSSTDLTQTSSSGTVTLP391.
1512232	9	2	theme	glycosylation	1645:1657	arg1	located					1685:1691	located	1685:1691	located	1685:1691	The other glycosylation sites observed in SRF are located in the region of the protein between the DNA binding domain and the transcriptional activation domain.
1512232	9	2	theme	glycosylation	1645:1657	arg1	sites					1659:1663	The other glycosylation sites	1635:1663	The other glycosylation sites observed in SRF	1635:1679	The other glycosylation sites observed in SRF are located in the region of the protein between the DNA binding domain and the transcriptional activation domain.
1512232	1	3	dep	W.	339:340	arg1	G					342:342	G	342:342	Kelly, W. G. (1989a) Annu	332:356	A unique form of nucleoplasmic and cytoplasmic protein glycosylation, O-linked GlcNAc, has previously been detected, using Gal transferase labeling techniques, on a myriad of proteins (for review see Hart, G. W., Haltiwanger, R. S., Holt, G. D., and Kelly, W. G. (1989a) Annu.
1512232	12	4	from	situated	2102:2109	arg1	region					2133:2138	a relatively short region	2114:2138	a relatively short region of the primary sequence close to or within the transcriptional activation domain which is distant from the major sites of phosphorylation catalyzed by casein kinase II	2114:2306	All the glycosylation sites identified in SRF are situated in a relatively short region of the primary sequence close to or within the transcriptional activation domain which is distant from the major sites of phosphorylation catalyzed by casein kinase II.
1512232	4	5	from	sites	613:617	arg1	factors					662:668	transcription factors	648:668	transcription factors	648:668	However, virtually nothing is known about the degree of glycosylation at individual sites, or, indeed, the actual sites of attachment of O-GlcNAc on transcription factors.
1512232	3	6	theme	transcription	420:432	arg1	factors					434:440	many RNA polymerase II transcription factors	397:440	many RNA polymerase II transcription factors	397:440	58, 841-874), including many RNA polymerase II transcription factors (Jackson, S. P., and Tjian, R. (1988) Cell 55, 125-133).
1512232	1	7	theme	proteins	257:264	arg1	myriad					247:252	a myriad	245:252	a myriad of proteins (for review see Hart, G. W., Haltiwanger, R. S., Holt, G. D., and Kelly, W. G. (1989a) Annu	245:356	A unique form of nucleoplasmic and cytoplasmic protein glycosylation, O-linked GlcNAc, has previously been detected, using Gal transferase labeling techniques, on a myriad of proteins (for review see Hart, G. W., Haltiwanger, R. S., Holt, G. D., and Kelly, W. G. (1989a) Annu.
1512232	8	8	located	found	1512:1516	arg1	repeat					1536:1541	the SSS tandem repeat	1521:1541	the SSS tandem repeat of peptide (374-391) which is situated within the transcriptional activation domain of SRF	1521:1632	The highest level of glycosylation was found on the SSS tandem repeat of peptide (374-391) which is situated within the transcriptional activation domain of SRF.
1512232	8	8	located	found	1512:1516	arg2	level					1485:1489	The highest level	1473:1489	The highest level of glycosylation	1473:1506	The highest level of glycosylation was found on the SSS tandem repeat of peptide (374-391) which is situated within the transcriptional activation domain of SRF.
1512232	6	9	theme	SRF	932:934	arg1	digests					921:927	proteolytic digests	909:927	proteolytic digests of SRF	909:934	Fast atom bombardment mass spectrometry (FAB-MS) of proteolytic digests of SRF provides evidence for the presence of a single substoichiometric O-GlcNAc residue on each of four peptides isolated after sequential cyanogen bromide, tryptic, and proline specific enzyme digestion: these peptides are 306VSASVSP312, 274GTTSTIQTAP283, 313SAVSSADGTVLK324, and 374DSSTDLTQTSSSGTVTLP391.
1512232	12	10	theme	glycosylation	2060:2072	arg1	sites					2074:2078	All the glycosylation sites	2052:2078	All the glycosylation sites identified in SRF	2052:2096	All the glycosylation sites identified in SRF are situated in a relatively short region of the primary sequence close to or within the transcriptional activation domain which is distant from the major sites of phosphorylation catalyzed by casein kinase II.
1512232	12	10	theme	glycosylation	2060:2072	arg1	situated					2102:2109	situated	2102:2109	situated	2102:2109	All the glycosylation sites identified in SRF are situated in a relatively short region of the primary sequence close to or within the transcriptional activation domain which is distant from the major sites of phosphorylation catalyzed by casein kinase II.
1512232	3	11	theme	polymerase	406:415	arg1	factors					434:440	many RNA polymerase II transcription factors	397:440	many RNA polymerase II transcription factors	397:440	58, 841-874), including many RNA polymerase II transcription factors (Jackson, S. P., and Tjian, R. (1988) Cell 55, 125-133).
1512232	8	12	theme	glycosylation	1494:1506	arg1	level					1485:1489	The highest level	1473:1489	The highest level of glycosylation	1473:1506	The highest level of glycosylation was found on the SSS tandem repeat of peptide (374-391) which is situated within the transcriptional activation domain of SRF.
1512232	3	13	dep	P.	455:456	arg1	Cell					480:483	Cell	480:483	Cell	480:483	58, 841-874), including many RNA polymerase II transcription factors (Jackson, S. P., and Tjian, R. (1988) Cell 55, 125-133).
1512232	6	14	theme	digests	921:927	arg1	spectrometry					884:895	Fast atom bombardment mass spectrometry	857:895	Fast atom bombardment mass spectrometry (FAB-MS) of proteolytic digests of SRF	857:934	Fast atom bombardment mass spectrometry (FAB-MS) of proteolytic digests of SRF provides evidence for the presence of a single substoichiometric O-GlcNAc residue on each of four peptides isolated after sequential cyanogen bromide, tryptic, and proline specific enzyme digestion: these peptides are 306VSASVSP312, 274GTTSTIQTAP283, 313SAVSSADGTVLK324, and 374DSSTDLTQTSSSGTVTLP391.
1512232	6	14	theme	digests	921:927	arg1	FAB-MS					898:903	FAB-MS	898:903	FAB-MS	898:903	Fast atom bombardment mass spectrometry (FAB-MS) of proteolytic digests of SRF provides evidence for the presence of a single substoichiometric O-GlcNAc residue on each of four peptides isolated after sequential cyanogen bromide, tryptic, and proline specific enzyme digestion: these peptides are 306VSASVSP312, 274GTTSTIQTAP283, 313SAVSSADGTVLK324, and 374DSSTDLTQTSSSGTVTLP391.
1512232	12	15	theme	transcriptional	2187:2201	arg1	domain					2214:2219	the transcriptional activation domain	2183:2219	the transcriptional activation domain which is distant from the major sites of phosphorylation catalyzed by casein kinase II	2183:2306	All the glycosylation sites identified in SRF are situated in a relatively short region of the primary sequence close to or within the transcriptional activation domain which is distant from the major sites of phosphorylation catalyzed by casein kinase II.
1512232	12	15	theme	transcriptional	2187:2201	arg1	distant					2230:2236	distant	2230:2236	distant	2230:2236	All the glycosylation sites identified in SRF are situated in a relatively short region of the primary sequence close to or within the transcriptional activation domain which is distant from the major sites of phosphorylation catalyzed by casein kinase II.
1512232	6	16	attach	presence	962:969	arg1	each					1021:1024	each	1021:1024	each	1021:1024	Fast atom bombardment mass spectrometry (FAB-MS) of proteolytic digests of SRF provides evidence for the presence of a single substoichiometric O-GlcNAc residue on each of four peptides isolated after sequential cyanogen bromide, tryptic, and proline specific enzyme digestion: these peptides are 306VSASVSP312, 274GTTSTIQTAP283, 313SAVSSADGTVLK324, and 374DSSTDLTQTSSSGTVTLP391.
1512232	6	16	attach	presence	962:969	arg2	residue					1010:1016	a single substoichiometric O-GlcNAc residue	974:1016	a single substoichiometric O-GlcNAc residue	974:1016	Fast atom bombardment mass spectrometry (FAB-MS) of proteolytic digests of SRF provides evidence for the presence of a single substoichiometric O-GlcNAc residue on each of four peptides isolated after sequential cyanogen bromide, tryptic, and proline specific enzyme digestion: these peptides are 306VSASVSP312, 274GTTSTIQTAP283, 313SAVSSADGTVLK324, and 374DSSTDLTQTSSSGTVTLP391.
1512232	6	16	attach	presence	962:969	arg1	peptides					1034:1041	four peptides	1029:1041	four peptides isolated after sequential cyanogen bromide, tryptic, and proline specific enzyme digestion	1029:1132	Fast atom bombardment mass spectrometry (FAB-MS) of proteolytic digests of SRF provides evidence for the presence of a single substoichiometric O-GlcNAc residue on each of four peptides isolated after sequential cyanogen bromide, tryptic, and proline specific enzyme digestion: these peptides are 306VSASVSP312, 274GTTSTIQTAP283, 313SAVSSADGTVLK324, and 374DSSTDLTQTSSSGTVTLP391.
1512232	6	17	theme	residue	1010:1016	arg1	presence					962:969	the presence	958:969	the presence of a single substoichiometric O-GlcNAc residue on each of four peptides isolated after sequential cyanogen bromide, tryptic, and proline specific enzyme digestion	958:1132	Fast atom bombardment mass spectrometry (FAB-MS) of proteolytic digests of SRF provides evidence for the presence of a single substoichiometric O-GlcNAc residue on each of four peptides isolated after sequential cyanogen bromide, tryptic, and proline specific enzyme digestion: these peptides are 306VSASVSP312, 274GTTSTIQTAP283, 313SAVSSADGTVLK324, and 374DSSTDLTQTSSSGTVTLP391.
1512232	7	18	theme	serine	1421:1426	arg1	attachment					1393:1402	O-GlcNAc attachment	1384:1402	O-GlcNAc attachment	1384:1402	Using an array of techniques, including manual Edman degradation, aminopeptidase, and elastase digestion, together with FAB-MS, the major sites of O-GlcNAc attachment were shown to be serine residues within short tandem repeat regions.
1512232	7	18	theme	serine	1421:1426	arg1	residues					1428:1435	serine residues	1421:1435	serine residues within short tandem repeat regions	1421:1470	Using an array of techniques, including manual Edman degradation, aminopeptidase, and elastase digestion, together with FAB-MS, the major sites of O-GlcNAc attachment were shown to be serine residues within short tandem repeat regions.
1512232	7	18	theme	serine	1421:1426	arg1	sites					1375:1379	the major sites	1365:1379	the major sites of O-GlcNAc attachment	1365:1402	Using an array of techniques, including manual Edman degradation, aminopeptidase, and elastase digestion, together with FAB-MS, the major sites of O-GlcNAc attachment were shown to be serine residues within short tandem repeat regions.
1512232	12	19	theme	sequence	2155:2162	arg1	region					2133:2138	a relatively short region	2114:2138	a relatively short region of the primary sequence close to or within the transcriptional activation domain which is distant from the major sites of phosphorylation catalyzed by casein kinase II	2114:2306	All the glycosylation sites identified in SRF are situated in a relatively short region of the primary sequence close to or within the transcriptional activation domain which is distant from the major sites of phosphorylation catalyzed by casein kinase II.
1512232	11	20	theme	tandem	2036:2041	arg1	repeats					2043:2049	tandem repeats	2036:2049	tandem repeats	2036:2049	The lowest level of glycosylation was recovered in peptide (306-312) which lacks tandem repeats.
1512232	6	21	theme	O-GlcNAc	1001:1008	arg1	residue					1010:1016	a single substoichiometric O-GlcNAc residue	974:1016	a single substoichiometric O-GlcNAc residue	974:1016	Fast atom bombardment mass spectrometry (FAB-MS) of proteolytic digests of SRF provides evidence for the presence of a single substoichiometric O-GlcNAc residue on each of four peptides isolated after sequential cyanogen bromide, tryptic, and proline specific enzyme digestion: these peptides are 306VSASVSP312, 274GTTSTIQTAP283, 313SAVSSADGTVLK324, and 374DSSTDLTQTSSSGTVTLP391.
1512232	12	22	from	region	2133:2138	arg1	sites					2074:2078	All the glycosylation sites	2052:2078	All the glycosylation sites identified in SRF	2052:2096	All the glycosylation sites identified in SRF are situated in a relatively short region of the primary sequence close to or within the transcriptional activation domain which is distant from the major sites of phosphorylation catalyzed by casein kinase II.
1512232	12	22	from	region	2133:2138	arg1	situated					2102:2109	situated	2102:2109	situated	2102:2109	All the glycosylation sites identified in SRF are situated in a relatively short region of the primary sequence close to or within the transcriptional activation domain which is distant from the major sites of phosphorylation catalyzed by casein kinase II.
1512232	5	23	theme	cell	846:849	arg1	line					851:854	an insect cell line	836:854	an insect cell line	836:854	In this paper we provide rigorous evidence for the occurrence and locations of O-GlcNAc on the c-fos transcription factor, serum response factor (SRF), expressed in an insect cell line.
1512232	8	24	theme	tandem	1529:1534	arg1	repeat					1536:1541	the SSS tandem repeat	1521:1541	the SSS tandem repeat of peptide (374-391) which is situated within the transcriptional activation domain of SRF	1521:1632	The highest level of glycosylation was found on the SSS tandem repeat of peptide (374-391) which is situated within the transcriptional activation domain of SRF.
1512232	1	25	theme	transferase	209:219	arg1	techniques					230:239	Gal transferase labeling techniques	205:239	Gal transferase labeling techniques	205:239	A unique form of nucleoplasmic and cytoplasmic protein glycosylation, O-linked GlcNAc, has previously been detected, using Gal transferase labeling techniques, on a myriad of proteins (for review see Hart, G. W., Haltiwanger, R. S., Holt, G. D., and Kelly, W. G. (1989a) Annu.
1512232	6	26	theme	single	976:981	arg1	residue					1010:1016	a single substoichiometric O-GlcNAc residue	974:1016	a single substoichiometric O-GlcNAc residue	974:1016	Fast atom bombardment mass spectrometry (FAB-MS) of proteolytic digests of SRF provides evidence for the presence of a single substoichiometric O-GlcNAc residue on each of four peptides isolated after sequential cyanogen bromide, tryptic, and proline specific enzyme digestion: these peptides are 306VSASVSP312, 274GTTSTIQTAP283, 313SAVSSADGTVLK324, and 374DSSTDLTQTSSSGTVTLP391.
1512232	9	27	theme	protein	1714:1720	arg1	region					1700:1705	the region	1696:1705	the region of the protein between the DNA binding domain and the transcriptional activation domain	1696:1793	The other glycosylation sites observed in SRF are located in the region of the protein between the DNA binding domain and the transcriptional activation domain.
1512232	1	28	theme	cytoplasmic	117:127	arg1	glycosylation					137:149	nucleoplasmic and cytoplasmic protein glycosylation	99:149	nucleoplasmic and cytoplasmic protein glycosylation	99:149	A unique form of nucleoplasmic and cytoplasmic protein glycosylation, O-linked GlcNAc, has previously been detected, using Gal transferase labeling techniques, on a myriad of proteins (for review see Hart, G. W., Haltiwanger, R. S., Holt, G. D., and Kelly, W. G. (1989a) Annu.
1512232	7	29	theme	O-GlcNAc	1384:1391	arg1	attachment					1393:1402	O-GlcNAc attachment	1384:1402	O-GlcNAc attachment	1384:1402	Using an array of techniques, including manual Edman degradation, aminopeptidase, and elastase digestion, together with FAB-MS, the major sites of O-GlcNAc attachment were shown to be serine residues within short tandem repeat regions.
1512232	10	30	theme	TTST	1886:1889	arg1	repeat					1898:1903	the TTST tandem repeat	1882:1903	the TTST tandem repeat	1882:1903	Glycosylation of peptides (274-283) and (313-324) was found to occur on the serine in the TTST tandem repeat and on serine 316 in the SS repeat, respectively.
1512232	6	31	theme	sequential	1058:1067	arg1	bromide					1078:1084	sequential cyanogen bromide	1058:1084	sequential cyanogen bromide	1058:1084	Fast atom bombardment mass spectrometry (FAB-MS) of proteolytic digests of SRF provides evidence for the presence of a single substoichiometric O-GlcNAc residue on each of four peptides isolated after sequential cyanogen bromide, tryptic, and proline specific enzyme digestion: these peptides are 306VSASVSP312, 274GTTSTIQTAP283, 313SAVSSADGTVLK324, and 374DSSTDLTQTSSSGTVTLP391.
1512232	9	32	located	observed	1665:1672	arg2	sites					1659:1663	The other glycosylation sites	1635:1663	The other glycosylation sites observed in SRF	1635:1679	The other glycosylation sites observed in SRF are located in the region of the protein between the DNA binding domain and the transcriptional activation domain.
1512232	9	32	located	observed	1665:1672	arg2	located					1685:1691	located	1685:1691	located	1685:1691	The other glycosylation sites observed in SRF are located in the region of the protein between the DNA binding domain and the transcriptional activation domain.
1512232	9	32	located	observed	1665:1672	arg1	SRF					1677:1679	SRF	1677:1679	SRF	1677:1679	The other glycosylation sites observed in SRF are located in the region of the protein between the DNA binding domain and the transcriptional activation domain.
1512232	1	33	theme	glycosylation	137:149	arg1	form					91:94	A unique form	82:94	A unique form of nucleoplasmic and cytoplasmic protein glycosylation	82:149	A unique form of nucleoplasmic and cytoplasmic protein glycosylation, O-linked GlcNAc, has previously been detected, using Gal transferase labeling techniques, on a myriad of proteins (for review see Hart, G. W., Haltiwanger, R. S., Holt, G. D., and Kelly, W. G. (1989a) Annu.
1512232	1	33	theme	glycosylation	137:149	arg1	GlcNAc					161:166	O-linked GlcNAc	152:166	O-linked GlcNAc	152:166	A unique form of nucleoplasmic and cytoplasmic protein glycosylation, O-linked GlcNAc, has previously been detected, using Gal transferase labeling techniques, on a myriad of proteins (for review see Hart, G. W., Haltiwanger, R. S., Holt, G. D., and Kelly, W. G. (1989a) Annu.
1512232	9	34	theme	binding	1738:1744	arg1	domain					1746:1751	the DNA binding domain	1730:1751	the DNA binding domain	1730:1751	The other glycosylation sites observed in SRF are located in the region of the protein between the DNA binding domain and the transcriptional activation domain.
1512232	0	35	theme	transcription	60:72	arg1	factor					74:79	the serum response transcription factor	41:79	the serum response transcription factor	41:79	Localization of O-GlcNAc modification on the serum response transcription factor.
1512232	1	36	theme	O-linked	152:159	arg1	form					91:94	A unique form	82:94	A unique form of nucleoplasmic and cytoplasmic protein glycosylation	82:149	A unique form of nucleoplasmic and cytoplasmic protein glycosylation, O-linked GlcNAc, has previously been detected, using Gal transferase labeling techniques, on a myriad of proteins (for review see Hart, G. W., Haltiwanger, R. S., Holt, G. D., and Kelly, W. G. (1989a) Annu.
1512232	1	36	theme	O-linked	152:159	arg1	GlcNAc					161:166	O-linked GlcNAc	152:166	O-linked GlcNAc	152:166	A unique form of nucleoplasmic and cytoplasmic protein glycosylation, O-linked GlcNAc, has previously been detected, using Gal transferase labeling techniques, on a myriad of proteins (for review see Hart, G. W., Haltiwanger, R. S., Holt, G. D., and Kelly, W. G. (1989a) Annu.
1512232	4	37	attach	attachment	622:631	arg2	O-GlcNAc					636:643	O-GlcNAc	636:643	O-GlcNAc	636:643	However, virtually nothing is known about the degree of glycosylation at individual sites, or, indeed, the actual sites of attachment of O-GlcNAc on transcription factors.
1512232	4	37	attach	attachment	622:631	arg3	factors					662:668	transcription factors	648:668	transcription factors	648:668	However, virtually nothing is known about the degree of glycosylation at individual sites, or, indeed, the actual sites of attachment of O-GlcNAc on transcription factors.
1512232	5	38	dep	occurrence	722:731	arg1	the					718:720	the	718:720	the	718:720	In this paper we provide rigorous evidence for the occurrence and locations of O-GlcNAc on the c-fos transcription factor, serum response factor (SRF), expressed in an insect cell line.
1512232	10	39	theme	peptides	1813:1820	arg1	Glycosylation					1796:1808	Glycosylation	1796:1808	Glycosylation of peptides (274-283) and (313-324)	1796:1844	Glycosylation of peptides (274-283) and (313-324) was found to occur on the serine in the TTST tandem repeat and on serine 316 in the SS repeat, respectively.
1512232	4	40	from	factors	662:668	arg1	attachment					622:631	attachment	622:631	attachment of O-GlcNAc on transcription factors	622:668	However, virtually nothing is known about the degree of glycosylation at individual sites, or, indeed, the actual sites of attachment of O-GlcNAc on transcription factors.
1512232	4	40	from	factors	662:668	arg1	sites					613:617	the actual sites	602:617	the actual sites of attachment of O-GlcNAc on transcription factors	602:668	However, virtually nothing is known about the degree of glycosylation at individual sites, or, indeed, the actual sites of attachment of O-GlcNAc on transcription factors.
1512232	0	41	from	Localization	0:11	arg1	factor					74:79	the serum response transcription factor	41:79	the serum response transcription factor	41:79	Localization of O-GlcNAc modification on the serum response transcription factor.
1512232	9	42	theme	transcriptional	1761:1775	arg1	domain					1788:1793	the transcriptional activation domain	1757:1793	the transcriptional activation domain	1757:1793	The other glycosylation sites observed in SRF are located in the region of the protein between the DNA binding domain and the transcriptional activation domain.
1512232	4	43	theme	individual	572:581	arg1	sites					583:587	individual sites	572:587	individual sites	572:587	However, virtually nothing is known about the degree of glycosylation at individual sites, or, indeed, the actual sites of attachment of O-GlcNAc on transcription factors.
1512232	6	44	from	presence	962:969	arg1	each					1021:1024	each	1021:1024	each	1021:1024	Fast atom bombardment mass spectrometry (FAB-MS) of proteolytic digests of SRF provides evidence for the presence of a single substoichiometric O-GlcNAc residue on each of four peptides isolated after sequential cyanogen bromide, tryptic, and proline specific enzyme digestion: these peptides are 306VSASVSP312, 274GTTSTIQTAP283, 313SAVSSADGTVLK324, and 374DSSTDLTQTSSSGTVTLP391.
1512232	6	44	from	presence	962:969	arg1	peptides					1034:1041	four peptides	1029:1041	four peptides isolated after sequential cyanogen bromide, tryptic, and proline specific enzyme digestion	1029:1132	Fast atom bombardment mass spectrometry (FAB-MS) of proteolytic digests of SRF provides evidence for the presence of a single substoichiometric O-GlcNAc residue on each of four peptides isolated after sequential cyanogen bromide, tryptic, and proline specific enzyme digestion: these peptides are 306VSASVSP312, 274GTTSTIQTAP283, 313SAVSSADGTVLK324, and 374DSSTDLTQTSSSGTVTLP391.
1512232	10	45	theme	SS	1930:1931	arg1	repeat					1933:1938	the SS repeat	1926:1938	the SS repeat	1926:1938	Glycosylation of peptides (274-283) and (313-324) was found to occur on the serine in the TTST tandem repeat and on serine 316 in the SS repeat, respectively.
1512232	6	46	theme	specific	1108:1115	arg1	digestion					1124:1132	proline specific enzyme digestion	1100:1132	proline specific enzyme digestion	1100:1132	Fast atom bombardment mass spectrometry (FAB-MS) of proteolytic digests of SRF provides evidence for the presence of a single substoichiometric O-GlcNAc residue on each of four peptides isolated after sequential cyanogen bromide, tryptic, and proline specific enzyme digestion: these peptides are 306VSASVSP312, 274GTTSTIQTAP283, 313SAVSSADGTVLK324, and 374DSSTDLTQTSSSGTVTLP391.
1512232	8	47	theme	transcriptional	1593:1607	arg1	SRF					1630:1632	SRF	1630:1632	SRF	1630:1632	The highest level of glycosylation was found on the SSS tandem repeat of peptide (374-391) which is situated within the transcriptional activation domain of SRF.
1512232	8	47	theme	transcriptional	1593:1607	arg1	domain					1620:1625	the transcriptional activation domain	1589:1625	the transcriptional activation domain of SRF	1589:1632	The highest level of glycosylation was found on the SSS tandem repeat of peptide (374-391) which is situated within the transcriptional activation domain of SRF.
1512232	5	48	theme	c-fos	766:770	arg1	factor					809:814	serum response factor	794:814	serum response factor (SRF)	794:820	In this paper we provide rigorous evidence for the occurrence and locations of O-GlcNAc on the c-fos transcription factor, serum response factor (SRF), expressed in an insect cell line.
1512232	5	48	theme	c-fos	766:770	arg1	factor					786:791	the c-fos transcription factor	762:791	the c-fos transcription factor	762:791	In this paper we provide rigorous evidence for the occurrence and locations of O-GlcNAc on the c-fos transcription factor, serum response factor (SRF), expressed in an insect cell line.
1512232	7	49	theme	repeat	1457:1462	arg1	regions					1464:1470	short tandem repeat regions	1444:1470	short tandem repeat regions	1444:1470	Using an array of techniques, including manual Edman degradation, aminopeptidase, and elastase digestion, together with FAB-MS, the major sites of O-GlcNAc attachment were shown to be serine residues within short tandem repeat regions.
1512232	7	50	theme	short	1444:1448	arg1	repeat					1457:1462	short tandem repeat	1444:1462	short tandem repeat regions	1444:1470	Using an array of techniques, including manual Edman degradation, aminopeptidase, and elastase digestion, together with FAB-MS, the major sites of O-GlcNAc attachment were shown to be serine residues within short tandem repeat regions.
1512232	4	51	theme	glycosylation	555:567	arg1	degree					545:550	the degree	541:550	the degree of glycosylation at individual sites, or, indeed, the actual sites of attachment of O-GlcNAc on transcription factors	541:668	However, virtually nothing is known about the degree of glycosylation at individual sites, or, indeed, the actual sites of attachment of O-GlcNAc on transcription factors.
1512232	12	52	from	sites	2253:2257	arg1	domain					2214:2219	the transcriptional activation domain	2183:2219	the transcriptional activation domain which is distant from the major sites of phosphorylation catalyzed by casein kinase II	2183:2306	All the glycosylation sites identified in SRF are situated in a relatively short region of the primary sequence close to or within the transcriptional activation domain which is distant from the major sites of phosphorylation catalyzed by casein kinase II.
1512232	12	52	from	sites	2253:2257	arg1	distant					2230:2236	distant	2230:2236	distant	2230:2236	All the glycosylation sites identified in SRF are situated in a relatively short region of the primary sequence close to or within the transcriptional activation domain which is distant from the major sites of phosphorylation catalyzed by casein kinase II.
1512232	0	53	theme	O-GlcNAc	16:23	arg1	modification					25:36	O-GlcNAc modification	16:36	O-GlcNAc modification	16:36	Localization of O-GlcNAc modification on the serum response transcription factor.
1512232	7	54	theme	elastase	1323:1330	arg1	digestion					1332:1340	elastase digestion	1323:1340	elastase digestion	1323:1340	Using an array of techniques, including manual Edman degradation, aminopeptidase, and elastase digestion, together with FAB-MS, the major sites of O-GlcNAc attachment were shown to be serine residues within short tandem repeat regions.
1512232	1	55	theme	nucleoplasmic	99:111	arg1	glycosylation					137:149	nucleoplasmic and cytoplasmic protein glycosylation	99:149	nucleoplasmic and cytoplasmic protein glycosylation	99:149	A unique form of nucleoplasmic and cytoplasmic protein glycosylation, O-linked GlcNAc, has previously been detected, using Gal transferase labeling techniques, on a myriad of proteins (for review see Hart, G. W., Haltiwanger, R. S., Holt, G. D., and Kelly, W. G. (1989a) Annu.
1512232	4	56	theme	actual	606:611	arg1	attachment					622:631	attachment	622:631	attachment of O-GlcNAc on transcription factors	622:668	However, virtually nothing is known about the degree of glycosylation at individual sites, or, indeed, the actual sites of attachment of O-GlcNAc on transcription factors.
1512232	4	56	theme	actual	606:611	arg1	sites					613:617	the actual sites	602:617	the actual sites of attachment of O-GlcNAc on transcription factors	602:668	However, virtually nothing is known about the degree of glycosylation at individual sites, or, indeed, the actual sites of attachment of O-GlcNAc on transcription factors.
1512232	0	57	theme	serum	45:49	arg1	factor					74:79	the serum response transcription factor	41:79	the serum response transcription factor	41:79	Localization of O-GlcNAc modification on the serum response transcription factor.
1512232	10	58	gly	Glycosylation	1796:1808	arg1	313-324					1837:1843	313-324	1837:1843	313-324	1837:1843	Glycosylation of peptides (274-283) and (313-324) was found to occur on the serine in the TTST tandem repeat and on serine 316 in the SS repeat, respectively.
1512232	10	58	gly	Glycosylation	1796:1808	arg1	274-283					1823:1829	274-283	1823:1829	274-283	1823:1829	Glycosylation of peptides (274-283) and (313-324) was found to occur on the serine in the TTST tandem repeat and on serine 316 in the SS repeat, respectively.
1512232	10	58	gly	Glycosylation	1796:1808	arg1	peptides					1813:1820	peptides	1813:1820	peptides (274-283)	1813:1830	Glycosylation of peptides (274-283) and (313-324) was found to occur on the serine in the TTST tandem repeat and on serine 316 in the SS repeat, respectively.
1512232	10	59	from	serine	1872:1877	arg1	repeat					1898:1903	the TTST tandem repeat	1882:1903	the TTST tandem repeat	1882:1903	Glycosylation of peptides (274-283) and (313-324) was found to occur on the serine in the TTST tandem repeat and on serine 316 in the SS repeat, respectively.
1512232	1	60	theme	labeling	221:228	arg1	techniques					230:239	Gal transferase labeling techniques	205:239	Gal transferase labeling techniques	205:239	A unique form of nucleoplasmic and cytoplasmic protein glycosylation, O-linked GlcNAc, has previously been detected, using Gal transferase labeling techniques, on a myriad of proteins (for review see Hart, G. W., Haltiwanger, R. S., Holt, G. D., and Kelly, W. G. (1989a) Annu.
1512232	7	61	theme	Edman	1284:1288	arg1	degradation					1290:1300	manual Edman degradation	1277:1300	manual Edman degradation	1277:1300	Using an array of techniques, including manual Edman degradation, aminopeptidase, and elastase digestion, together with FAB-MS, the major sites of O-GlcNAc attachment were shown to be serine residues within short tandem repeat regions.
1512232	12	62	gly	glycosylation	2060:2072	arg2	situated					2102:2109	situated	2102:2109	situated	2102:2109	All the glycosylation sites identified in SRF are situated in a relatively short region of the primary sequence close to or within the transcriptional activation domain which is distant from the major sites of phosphorylation catalyzed by casein kinase II.
1512232	12	62	gly	glycosylation	2060:2072	arg2	sites					2074:2078	All the glycosylation sites	2052:2078	All the glycosylation sites identified in SRF	2052:2096	All the glycosylation sites identified in SRF are situated in a relatively short region of the primary sequence close to or within the transcriptional activation domain which is distant from the major sites of phosphorylation catalyzed by casein kinase II.
1512232	6	63	theme	mass	879:882	arg1	spectrometry					884:895	Fast atom bombardment mass spectrometry	857:895	Fast atom bombardment mass spectrometry (FAB-MS) of proteolytic digests of SRF	857:934	Fast atom bombardment mass spectrometry (FAB-MS) of proteolytic digests of SRF provides evidence for the presence of a single substoichiometric O-GlcNAc residue on each of four peptides isolated after sequential cyanogen bromide, tryptic, and proline specific enzyme digestion: these peptides are 306VSASVSP312, 274GTTSTIQTAP283, 313SAVSSADGTVLK324, and 374DSSTDLTQTSSSGTVTLP391.
1512232	6	63	theme	mass	879:882	arg1	FAB-MS					898:903	FAB-MS	898:903	FAB-MS	898:903	Fast atom bombardment mass spectrometry (FAB-MS) of proteolytic digests of SRF provides evidence for the presence of a single substoichiometric O-GlcNAc residue on each of four peptides isolated after sequential cyanogen bromide, tryptic, and proline specific enzyme digestion: these peptides are 306VSASVSP312, 274GTTSTIQTAP283, 313SAVSSADGTVLK324, and 374DSSTDLTQTSSSGTVTLP391.
1512232	5	64	theme	serum	794:798	arg1	factor					809:814	serum response factor	794:814	serum response factor (SRF)	794:820	In this paper we provide rigorous evidence for the occurrence and locations of O-GlcNAc on the c-fos transcription factor, serum response factor (SRF), expressed in an insect cell line.
1512232	5	64	theme	serum	794:798	arg1	factor					786:791	the c-fos transcription factor	762:791	the c-fos transcription factor	762:791	In this paper we provide rigorous evidence for the occurrence and locations of O-GlcNAc on the c-fos transcription factor, serum response factor (SRF), expressed in an insect cell line.
1512232	5	64	theme	serum	794:798	arg1	SRF					817:819	SRF	817:819	SRF	817:819	In this paper we provide rigorous evidence for the occurrence and locations of O-GlcNAc on the c-fos transcription factor, serum response factor (SRF), expressed in an insect cell line.
1512232	6	65	theme	atom	862:865	arg1	spectrometry					884:895	Fast atom bombardment mass spectrometry	857:895	Fast atom bombardment mass spectrometry (FAB-MS) of proteolytic digests of SRF	857:934	Fast atom bombardment mass spectrometry (FAB-MS) of proteolytic digests of SRF provides evidence for the presence of a single substoichiometric O-GlcNAc residue on each of four peptides isolated after sequential cyanogen bromide, tryptic, and proline specific enzyme digestion: these peptides are 306VSASVSP312, 274GTTSTIQTAP283, 313SAVSSADGTVLK324, and 374DSSTDLTQTSSSGTVTLP391.
1512232	6	65	theme	atom	862:865	arg1	FAB-MS					898:903	FAB-MS	898:903	FAB-MS	898:903	Fast atom bombardment mass spectrometry (FAB-MS) of proteolytic digests of SRF provides evidence for the presence of a single substoichiometric O-GlcNAc residue on each of four peptides isolated after sequential cyanogen bromide, tryptic, and proline specific enzyme digestion: these peptides are 306VSASVSP312, 274GTTSTIQTAP283, 313SAVSSADGTVLK324, and 374DSSTDLTQTSSSGTVTLP391.
1512232	9	66	theme	other	1639:1643	arg1	located					1685:1691	located	1685:1691	located	1685:1691	The other glycosylation sites observed in SRF are located in the region of the protein between the DNA binding domain and the transcriptional activation domain.
1512232	9	66	theme	other	1639:1643	arg1	sites					1659:1663	The other glycosylation sites	1635:1663	The other glycosylation sites observed in SRF	1635:1679	The other glycosylation sites observed in SRF are located in the region of the protein between the DNA binding domain and the transcriptional activation domain.
1512232	8	67	theme	SRF	1630:1632	arg1	SRF					1630:1632	SRF	1630:1632	SRF	1630:1632	The highest level of glycosylation was found on the SSS tandem repeat of peptide (374-391) which is situated within the transcriptional activation domain of SRF.
1512232	8	67	theme	SRF	1630:1632	arg1	domain					1620:1625	the transcriptional activation domain	1589:1625	the transcriptional activation domain of SRF	1589:1632	The highest level of glycosylation was found on the SSS tandem repeat of peptide (374-391) which is situated within the transcriptional activation domain of SRF.
1512232	7	68	theme	techniques	1255:1264	arg1	array					1246:1250	an array	1243:1250	an array of techniques, including manual Edman degradation, aminopeptidase, and elastase digestion	1243:1340	Using an array of techniques, including manual Edman degradation, aminopeptidase, and elastase digestion, together with FAB-MS, the major sites of O-GlcNAc attachment were shown to be serine residues within short tandem repeat regions.
1512232	4	69	theme	transcription	648:660	arg1	factors					662:668	transcription factors	648:668	transcription factors	648:668	However, virtually nothing is known about the degree of glycosylation at individual sites, or, indeed, the actual sites of attachment of O-GlcNAc on transcription factors.
1512232	10	70	theme	313-324	1837:1843	arg1	Glycosylation					1796:1808	Glycosylation	1796:1808	Glycosylation of peptides (274-283) and (313-324)	1796:1844	Glycosylation of peptides (274-283) and (313-324) was found to occur on the serine in the TTST tandem repeat and on serine 316 in the SS repeat, respectively.
1512232	11	71	theme	glycosylation	1975:1987	arg1	level					1966:1970	The lowest level	1955:1970	The lowest level of glycosylation	1955:1987	The lowest level of glycosylation was recovered in peptide (306-312) which lacks tandem repeats.
1512232	9	72	gly	glycosylation	1645:1657	arg2	sites					1659:1663	The other glycosylation sites	1635:1663	The other glycosylation sites observed in SRF	1635:1679	The other glycosylation sites observed in SRF are located in the region of the protein between the DNA binding domain and the transcriptional activation domain.
1512232	9	72	gly	glycosylation	1645:1657	arg2	located					1685:1691	located	1685:1691	located	1685:1691	The other glycosylation sites observed in SRF are located in the region of the protein between the DNA binding domain and the transcriptional activation domain.
1512232	3	73	theme	RNA	402:404	arg1	polymerase					406:415	RNA polymerase II	402:418	many RNA polymerase II transcription factors	397:440	58, 841-874), including many RNA polymerase II transcription factors (Jackson, S. P., and Tjian, R. (1988) Cell 55, 125-133).
1512232	8	74	theme	highest	1477:1483	arg1	level					1485:1489	The highest level	1473:1489	The highest level of glycosylation	1473:1506	The highest level of glycosylation was found on the SSS tandem repeat of peptide (374-391) which is situated within the transcriptional activation domain of SRF.
1512232	4	75	theme	attachment	622:631	arg1	attachment					622:631	attachment	622:631	attachment of O-GlcNAc on transcription factors	622:668	However, virtually nothing is known about the degree of glycosylation at individual sites, or, indeed, the actual sites of attachment of O-GlcNAc on transcription factors.
1512232	4	75	theme	attachment	622:631	arg1	sites					613:617	the actual sites	602:617	the actual sites of attachment of O-GlcNAc on transcription factors	602:668	However, virtually nothing is known about the degree of glycosylation at individual sites, or, indeed, the actual sites of attachment of O-GlcNAc on transcription factors.
1512232	12	76	theme	activation	2203:2212	arg1	domain					2214:2219	the transcriptional activation domain	2183:2219	the transcriptional activation domain which is distant from the major sites of phosphorylation catalyzed by casein kinase II	2183:2306	All the glycosylation sites identified in SRF are situated in a relatively short region of the primary sequence close to or within the transcriptional activation domain which is distant from the major sites of phosphorylation catalyzed by casein kinase II.
1512232	12	76	theme	activation	2203:2212	arg1	distant					2230:2236	distant	2230:2236	distant	2230:2236	All the glycosylation sites identified in SRF are situated in a relatively short region of the primary sequence close to or within the transcriptional activation domain which is distant from the major sites of phosphorylation catalyzed by casein kinase II.
1512232	9	77	located	located	1685:1691	arg2	located					1685:1691	located	1685:1691	located	1685:1691	The other glycosylation sites observed in SRF are located in the region of the protein between the DNA binding domain and the transcriptional activation domain.
1512232	9	77	located	located	1685:1691	arg2	sites					1659:1663	The other glycosylation sites	1635:1663	The other glycosylation sites observed in SRF	1635:1679	The other glycosylation sites observed in SRF are located in the region of the protein between the DNA binding domain and the transcriptional activation domain.
1512232	9	77	located	located	1685:1691	arg1	region					1700:1705	the region	1696:1705	the region of the protein between the DNA binding domain and the transcriptional activation domain	1696:1793	The other glycosylation sites observed in SRF are located in the region of the protein between the DNA binding domain and the transcriptional activation domain.
1512232	4	78	theme	O-GlcNAc	636:643	arg1	attachment					622:631	attachment	622:631	attachment of O-GlcNAc on transcription factors	622:668	However, virtually nothing is known about the degree of glycosylation at individual sites, or, indeed, the actual sites of attachment of O-GlcNAc on transcription factors.
1512232	6	79	theme	proteolytic	909:919	arg1	digests					921:927	proteolytic digests	909:927	proteolytic digests of SRF	909:934	Fast atom bombardment mass spectrometry (FAB-MS) of proteolytic digests of SRF provides evidence for the presence of a single substoichiometric O-GlcNAc residue on each of four peptides isolated after sequential cyanogen bromide, tryptic, and proline specific enzyme digestion: these peptides are 306VSASVSP312, 274GTTSTIQTAP283, 313SAVSSADGTVLK324, and 374DSSTDLTQTSSSGTVTLP391.
1512232	6	80	theme	proline	1100:1106	arg1	digestion					1124:1132	proline specific enzyme digestion	1100:1132	proline specific enzyme digestion	1100:1132	Fast atom bombardment mass spectrometry (FAB-MS) of proteolytic digests of SRF provides evidence for the presence of a single substoichiometric O-GlcNAc residue on each of four peptides isolated after sequential cyanogen bromide, tryptic, and proline specific enzyme digestion: these peptides are 306VSASVSP312, 274GTTSTIQTAP283, 313SAVSSADGTVLK324, and 374DSSTDLTQTSSSGTVTLP391.
1512232	5	81	theme	insect	839:844	arg1	line					851:854	an insect cell line	836:854	an insect cell line	836:854	In this paper we provide rigorous evidence for the occurrence and locations of O-GlcNAc on the c-fos transcription factor, serum response factor (SRF), expressed in an insect cell line.
1512232	1	82	theme	Gal	205:207	arg1	techniques					230:239	Gal transferase labeling techniques	205:239	Gal transferase labeling techniques	205:239	A unique form of nucleoplasmic and cytoplasmic protein glycosylation, O-linked GlcNAc, has previously been detected, using Gal transferase labeling techniques, on a myriad of proteins (for review see Hart, G. W., Haltiwanger, R. S., Holt, G. D., and Kelly, W. G. (1989a) Annu.
1512232	7	83	theme	attachment	1393:1402	arg1	attachment					1393:1402	O-GlcNAc attachment	1384:1402	O-GlcNAc attachment	1384:1402	Using an array of techniques, including manual Edman degradation, aminopeptidase, and elastase digestion, together with FAB-MS, the major sites of O-GlcNAc attachment were shown to be serine residues within short tandem repeat regions.
1512232	7	83	theme	attachment	1393:1402	arg1	residues					1428:1435	serine residues	1421:1435	serine residues within short tandem repeat regions	1421:1470	Using an array of techniques, including manual Edman degradation, aminopeptidase, and elastase digestion, together with FAB-MS, the major sites of O-GlcNAc attachment were shown to be serine residues within short tandem repeat regions.
1512232	7	83	theme	attachment	1393:1402	arg1	sites					1375:1379	the major sites	1365:1379	the major sites of O-GlcNAc attachment	1365:1402	Using an array of techniques, including manual Edman degradation, aminopeptidase, and elastase digestion, together with FAB-MS, the major sites of O-GlcNAc attachment were shown to be serine residues within short tandem repeat regions.
1512232	6	84	theme	substoichiometric	983:999	arg1	residue					1010:1016	a single substoichiometric O-GlcNAc residue	974:1016	a single substoichiometric O-GlcNAc residue	974:1016	Fast atom bombardment mass spectrometry (FAB-MS) of proteolytic digests of SRF provides evidence for the presence of a single substoichiometric O-GlcNAc residue on each of four peptides isolated after sequential cyanogen bromide, tryptic, and proline specific enzyme digestion: these peptides are 306VSASVSP312, 274GTTSTIQTAP283, 313SAVSSADGTVLK324, and 374DSSTDLTQTSSSGTVTLP391.
1512232	8	85	theme	SSS	1525:1527	arg1	repeat					1536:1541	the SSS tandem repeat	1521:1541	the SSS tandem repeat of peptide (374-391) which is situated within the transcriptional activation domain of SRF	1521:1632	The highest level of glycosylation was found on the SSS tandem repeat of peptide (374-391) which is situated within the transcriptional activation domain of SRF.
1512232	5	86	theme	rigorous	696:703	arg1	evidence					705:712	rigorous evidence	696:712	rigorous evidence for the occurrence and locations of O-GlcNAc on the c-fos transcription factor, serum response factor (SRF), expressed in an insect cell line	696:854	In this paper we provide rigorous evidence for the occurrence and locations of O-GlcNAc on the c-fos transcription factor, serum response factor (SRF), expressed in an insect cell line.
1512232	10	87	theme	tandem	1891:1896	arg1	repeat					1898:1903	the TTST tandem repeat	1882:1903	the TTST tandem repeat	1882:1903	Glycosylation of peptides (274-283) and (313-324) was found to occur on the serine in the TTST tandem repeat and on serine 316 in the SS repeat, respectively.
1512232	6	88	theme	cyanogen	1069:1076	arg1	bromide					1078:1084	sequential cyanogen bromide	1058:1084	sequential cyanogen bromide	1058:1084	Fast atom bombardment mass spectrometry (FAB-MS) of proteolytic digests of SRF provides evidence for the presence of a single substoichiometric O-GlcNAc residue on each of four peptides isolated after sequential cyanogen bromide, tryptic, and proline specific enzyme digestion: these peptides are 306VSASVSP312, 274GTTSTIQTAP283, 313SAVSSADGTVLK324, and 374DSSTDLTQTSSSGTVTLP391.
1512232	7	89	dep	together	1343:1350	arg1	with					1352:1355	with	1352:1355	with	1352:1355	Using an array of techniques, including manual Edman degradation, aminopeptidase, and elastase digestion, together with FAB-MS, the major sites of O-GlcNAc attachment were shown to be serine residues within short tandem repeat regions.
1512232	12	90	theme	casein	2291:2296	arg1	kinase					2298:2303	casein kinase II	2291:2306	casein kinase II	2291:2306	All the glycosylation sites identified in SRF are situated in a relatively short region of the primary sequence close to or within the transcriptional activation domain which is distant from the major sites of phosphorylation catalyzed by casein kinase II.
1512232	1	91	theme	protein	129:135	arg1	glycosylation					137:149	nucleoplasmic and cytoplasmic protein glycosylation	99:149	nucleoplasmic and cytoplasmic protein glycosylation	99:149	A unique form of nucleoplasmic and cytoplasmic protein glycosylation, O-linked GlcNAc, has previously been detected, using Gal transferase labeling techniques, on a myriad of proteins (for review see Hart, G. W., Haltiwanger, R. S., Holt, G. D., and Kelly, W. G. (1989a) Annu.
1512232	7	92	theme	major	1369:1373	arg1	attachment					1393:1402	O-GlcNAc attachment	1384:1402	O-GlcNAc attachment	1384:1402	Using an array of techniques, including manual Edman degradation, aminopeptidase, and elastase digestion, together with FAB-MS, the major sites of O-GlcNAc attachment were shown to be serine residues within short tandem repeat regions.
1512232	7	92	theme	major	1369:1373	arg1	residues					1428:1435	serine residues	1421:1435	serine residues within short tandem repeat regions	1421:1470	Using an array of techniques, including manual Edman degradation, aminopeptidase, and elastase digestion, together with FAB-MS, the major sites of O-GlcNAc attachment were shown to be serine residues within short tandem repeat regions.
1512232	7	92	theme	major	1369:1373	arg1	sites					1375:1379	the major sites	1365:1379	the major sites of O-GlcNAc attachment	1365:1402	Using an array of techniques, including manual Edman degradation, aminopeptidase, and elastase digestion, together with FAB-MS, the major sites of O-GlcNAc attachment were shown to be serine residues within short tandem repeat regions.
1512232	9	93	from	located	1685:1691	arg1	region					1700:1705	the region	1696:1705	the region of the protein between the DNA binding domain and the transcriptional activation domain	1696:1793	The other glycosylation sites observed in SRF are located in the region of the protein between the DNA binding domain and the transcriptional activation domain.
1512232	9	94	theme	DNA	1734:1736	arg1	domain					1746:1751	the DNA binding domain	1730:1751	the DNA binding domain	1730:1751	The other glycosylation sites observed in SRF are located in the region of the protein between the DNA binding domain and the transcriptional activation domain.
1512232	8	95	theme	peptide	1546:1552	arg1	repeat					1536:1541	the SSS tandem repeat	1521:1541	the SSS tandem repeat of peptide (374-391) which is situated within the transcriptional activation domain of SRF	1521:1632	The highest level of glycosylation was found on the SSS tandem repeat of peptide (374-391) which is situated within the transcriptional activation domain of SRF.
1512232	1	96	dep	review	271:276	arg1	see					278:280	see	278:280	see Hart, G. W., Haltiwanger, R. S., Holt, G. D., and Kelly, W. G. (1989a) Annu	278:356	A unique form of nucleoplasmic and cytoplasmic protein glycosylation, O-linked GlcNAc, has previously been detected, using Gal transferase labeling techniques, on a myriad of proteins (for review see Hart, G. W., Haltiwanger, R. S., Holt, G. D., and Kelly, W. G. (1989a) Annu.
1512232	4	97	from	sites	583:587	arg1	attachment					622:631	attachment	622:631	attachment of O-GlcNAc on transcription factors	622:668	However, virtually nothing is known about the degree of glycosylation at individual sites, or, indeed, the actual sites of attachment of O-GlcNAc on transcription factors.
1512232	4	97	from	sites	583:587	arg1	sites					613:617	the actual sites	602:617	the actual sites of attachment of O-GlcNAc on transcription factors	602:668	However, virtually nothing is known about the degree of glycosylation at individual sites, or, indeed, the actual sites of attachment of O-GlcNAc on transcription factors.
1512232	5	98	theme	O-GlcNAc	750:757	arg1	locations					737:745	locations	737:745	locations	737:745	In this paper we provide rigorous evidence for the occurrence and locations of O-GlcNAc on the c-fos transcription factor, serum response factor (SRF), expressed in an insect cell line.
1512232	5	98	theme	O-GlcNAc	750:757	arg1	occurrence					722:731	occurrence	722:731	occurrence	722:731	In this paper we provide rigorous evidence for the occurrence and locations of O-GlcNAc on the c-fos transcription factor, serum response factor (SRF), expressed in an insect cell line.
1512232	11	99	theme	lowest	1959:1964	arg1	level					1966:1970	The lowest level	1955:1970	The lowest level of glycosylation	1955:1987	The lowest level of glycosylation was recovered in peptide (306-312) which lacks tandem repeats.
1512232	9	100	theme	activation	1777:1786	arg1	domain					1788:1793	the transcriptional activation domain	1757:1793	the transcriptional activation domain	1757:1793	The other glycosylation sites observed in SRF are located in the region of the protein between the DNA binding domain and the transcriptional activation domain.
1512232	6	101	theme	enzyme	1117:1122	arg1	digestion					1124:1132	proline specific enzyme digestion	1100:1132	proline specific enzyme digestion	1100:1132	Fast atom bombardment mass spectrometry (FAB-MS) of proteolytic digests of SRF provides evidence for the presence of a single substoichiometric O-GlcNAc residue on each of four peptides isolated after sequential cyanogen bromide, tryptic, and proline specific enzyme digestion: these peptides are 306VSASVSP312, 274GTTSTIQTAP283, 313SAVSSADGTVLK324, and 374DSSTDLTQTSSSGTVTLP391.
1512232	9	102	from	region	1700:1705	arg1	located					1685:1691	located	1685:1691	located	1685:1691	The other glycosylation sites observed in SRF are located in the region of the protein between the DNA binding domain and the transcriptional activation domain.
1512232	9	102	from	region	1700:1705	arg1	sites					1659:1663	The other glycosylation sites	1635:1663	The other glycosylation sites observed in SRF	1635:1679	The other glycosylation sites observed in SRF are located in the region of the protein between the DNA binding domain and the transcriptional activation domain.
1512232	12	103	theme	phosphorylation	2262:2276	arg1	phosphorylation					2262:2276	phosphorylation	2262:2276	phosphorylation catalyzed by casein kinase II	2262:2306	All the glycosylation sites identified in SRF are situated in a relatively short region of the primary sequence close to or within the transcriptional activation domain which is distant from the major sites of phosphorylation catalyzed by casein kinase II.
1512232	12	103	theme	phosphorylation	2262:2276	arg1	sites					2253:2257	the major sites	2243:2257	the major sites of phosphorylation catalyzed by casein kinase II	2243:2306	All the glycosylation sites identified in SRF are situated in a relatively short region of the primary sequence close to or within the transcriptional activation domain which is distant from the major sites of phosphorylation catalyzed by casein kinase II.
1512232	4	104	from	attachment	622:631	arg1	factors					662:668	transcription factors	648:668	transcription factors	648:668	However, virtually nothing is known about the degree of glycosylation at individual sites, or, indeed, the actual sites of attachment of O-GlcNAc on transcription factors.
1512232	1	105	theme	unique	84:89	arg1	form					91:94	A unique form	82:94	A unique form of nucleoplasmic and cytoplasmic protein glycosylation	82:149	A unique form of nucleoplasmic and cytoplasmic protein glycosylation, O-linked GlcNAc, has previously been detected, using Gal transferase labeling techniques, on a myriad of proteins (for review see Hart, G. W., Haltiwanger, R. S., Holt, G. D., and Kelly, W. G. (1989a) Annu.
1512232	1	105	theme	unique	84:89	arg1	GlcNAc					161:166	O-linked GlcNAc	152:166	O-linked GlcNAc	152:166	A unique form of nucleoplasmic and cytoplasmic protein glycosylation, O-linked GlcNAc, has previously been detected, using Gal transferase labeling techniques, on a myriad of proteins (for review see Hart, G. W., Haltiwanger, R. S., Holt, G. D., and Kelly, W. G. (1989a) Annu.
1512232	0	106	theme	modification	25:36	arg1	Localization					0:11	Localization	0:11	Localization of O-GlcNAc modification on the serum response transcription factor.	0:80	Localization of O-GlcNAc modification on the serum response transcription factor.
1512232	8	107	theme	activation	1609:1618	arg1	SRF					1630:1632	SRF	1630:1632	SRF	1630:1632	The highest level of glycosylation was found on the SSS tandem repeat of peptide (374-391) which is situated within the transcriptional activation domain of SRF.
1512232	8	107	theme	activation	1609:1618	arg1	domain					1620:1625	the transcriptional activation domain	1589:1625	the transcriptional activation domain of SRF	1589:1632	The highest level of glycosylation was found on the SSS tandem repeat of peptide (374-391) which is situated within the transcriptional activation domain of SRF.
1512232	3	108	dep	including	387:395	arg1	S.					452:453	S.	452:453	S.	452:453	58, 841-874), including many RNA polymerase II transcription factors (Jackson, S. P., and Tjian, R. (1988) Cell 55, 125-133).
1512232	3	108	dep	including	387:395	arg1	R					470:470	R	470:470	R	470:470	58, 841-874), including many RNA polymerase II transcription factors (Jackson, S. P., and Tjian, R. (1988) Cell 55, 125-133).
1512232	3	108	dep	including	387:395	arg1	P.					455:456	P.	455:456	P.	455:456	58, 841-874), including many RNA polymerase II transcription factors (Jackson, S. P., and Tjian, R. (1988) Cell 55, 125-133).
1512232	3	108	dep	including	387:395	arg1	Tjian					463:467	Tjian	463:467	Tjian	463:467	58, 841-874), including many RNA polymerase II transcription factors (Jackson, S. P., and Tjian, R. (1988) Cell 55, 125-133).
1512232	3	108	dep	including	387:395	arg1	1988					474:477	1988	474:477	1988	474:477	58, 841-874), including many RNA polymerase II transcription factors (Jackson, S. P., and Tjian, R. (1988) Cell 55, 125-133).
1512232	7	109	theme	tandem	1450:1455	arg1	repeat					1457:1462	short tandem repeat	1444:1462	short tandem repeat regions	1444:1470	Using an array of techniques, including manual Edman degradation, aminopeptidase, and elastase digestion, together with FAB-MS, the major sites of O-GlcNAc attachment were shown to be serine residues within short tandem repeat regions.
1512232	12	110	theme	primary	2147:2153	arg1	sequence					2155:2162	the primary sequence	2143:2162	the primary sequence close to or within the transcriptional activation domain which is distant from the major sites of phosphorylation catalyzed by casein kinase II	2143:2306	All the glycosylation sites identified in SRF are situated in a relatively short region of the primary sequence close to or within the transcriptional activation domain which is distant from the major sites of phosphorylation catalyzed by casein kinase II.
1512232	5	111	theme	response	800:807	arg1	factor					809:814	serum response factor	794:814	serum response factor (SRF)	794:820	In this paper we provide rigorous evidence for the occurrence and locations of O-GlcNAc on the c-fos transcription factor, serum response factor (SRF), expressed in an insect cell line.
1512232	5	111	theme	response	800:807	arg1	factor					786:791	the c-fos transcription factor	762:791	the c-fos transcription factor	762:791	In this paper we provide rigorous evidence for the occurrence and locations of O-GlcNAc on the c-fos transcription factor, serum response factor (SRF), expressed in an insect cell line.
1512232	5	111	theme	response	800:807	arg1	SRF					817:819	SRF	817:819	SRF	817:819	In this paper we provide rigorous evidence for the occurrence and locations of O-GlcNAc on the c-fos transcription factor, serum response factor (SRF), expressed in an insect cell line.
1512232	1	112	link	O-linked	152:159	arg1	form					91:94	A unique form	82:94	A unique form of nucleoplasmic and cytoplasmic protein glycosylation	82:149	A unique form of nucleoplasmic and cytoplasmic protein glycosylation, O-linked GlcNAc, has previously been detected, using Gal transferase labeling techniques, on a myriad of proteins (for review see Hart, G. W., Haltiwanger, R. S., Holt, G. D., and Kelly, W. G. (1989a) Annu.
1512232	1	112	link	O-linked	152:159	arg1	GlcNAc					161:166	O-linked GlcNAc	152:166	O-linked GlcNAc	152:166	A unique form of nucleoplasmic and cytoplasmic protein glycosylation, O-linked GlcNAc, has previously been detected, using Gal transferase labeling techniques, on a myriad of proteins (for review see Hart, G. W., Haltiwanger, R. S., Holt, G. D., and Kelly, W. G. (1989a) Annu.
1512232	0	113	theme	response	51:58	arg1	factor					74:79	the serum response transcription factor	41:79	the serum response transcription factor	41:79	Localization of O-GlcNAc modification on the serum response transcription factor.
1512232	12	114	theme	short	2127:2131	arg1	region					2133:2138	a relatively short region	2114:2138	a relatively short region of the primary sequence close to or within the transcriptional activation domain which is distant from the major sites of phosphorylation catalyzed by casein kinase II	2114:2306	All the glycosylation sites identified in SRF are situated in a relatively short region of the primary sequence close to or within the transcriptional activation domain which is distant from the major sites of phosphorylation catalyzed by casein kinase II.
1512232	5	115	from	locations	737:745	arg1	factor					809:814	serum response factor	794:814	serum response factor (SRF)	794:820	In this paper we provide rigorous evidence for the occurrence and locations of O-GlcNAc on the c-fos transcription factor, serum response factor (SRF), expressed in an insect cell line.
1512232	5	115	from	locations	737:745	arg1	factor					786:791	the c-fos transcription factor	762:791	the c-fos transcription factor	762:791	In this paper we provide rigorous evidence for the occurrence and locations of O-GlcNAc on the c-fos transcription factor, serum response factor (SRF), expressed in an insect cell line.
1512232	5	116	theme	transcription	772:784	arg1	factor					809:814	serum response factor	794:814	serum response factor (SRF)	794:820	In this paper we provide rigorous evidence for the occurrence and locations of O-GlcNAc on the c-fos transcription factor, serum response factor (SRF), expressed in an insect cell line.
1512232	5	116	theme	transcription	772:784	arg1	factor					786:791	the c-fos transcription factor	762:791	the c-fos transcription factor	762:791	In this paper we provide rigorous evidence for the occurrence and locations of O-GlcNAc on the c-fos transcription factor, serum response factor (SRF), expressed in an insect cell line.
1512232	5	117	from	occurrence	722:731	arg1	factor					809:814	serum response factor	794:814	serum response factor (SRF)	794:820	In this paper we provide rigorous evidence for the occurrence and locations of O-GlcNAc on the c-fos transcription factor, serum response factor (SRF), expressed in an insect cell line.
1512232	5	117	from	occurrence	722:731	arg1	factor					786:791	the c-fos transcription factor	762:791	the c-fos transcription factor	762:791	In this paper we provide rigorous evidence for the occurrence and locations of O-GlcNAc on the c-fos transcription factor, serum response factor (SRF), expressed in an insect cell line.
1512232	6	118	theme	bombardment	867:877	arg1	spectrometry					884:895	Fast atom bombardment mass spectrometry	857:895	Fast atom bombardment mass spectrometry (FAB-MS) of proteolytic digests of SRF	857:934	Fast atom bombardment mass spectrometry (FAB-MS) of proteolytic digests of SRF provides evidence for the presence of a single substoichiometric O-GlcNAc residue on each of four peptides isolated after sequential cyanogen bromide, tryptic, and proline specific enzyme digestion: these peptides are 306VSASVSP312, 274GTTSTIQTAP283, 313SAVSSADGTVLK324, and 374DSSTDLTQTSSSGTVTLP391.
1512232	6	118	theme	bombardment	867:877	arg1	FAB-MS					898:903	FAB-MS	898:903	FAB-MS	898:903	Fast atom bombardment mass spectrometry (FAB-MS) of proteolytic digests of SRF provides evidence for the presence of a single substoichiometric O-GlcNAc residue on each of four peptides isolated after sequential cyanogen bromide, tryptic, and proline specific enzyme digestion: these peptides are 306VSASVSP312, 274GTTSTIQTAP283, 313SAVSSADGTVLK324, and 374DSSTDLTQTSSSGTVTLP391.
1512232	12	119	theme	major	2247:2251	arg1	phosphorylation					2262:2276	phosphorylation	2262:2276	phosphorylation catalyzed by casein kinase II	2262:2306	All the glycosylation sites identified in SRF are situated in a relatively short region of the primary sequence close to or within the transcriptional activation domain which is distant from the major sites of phosphorylation catalyzed by casein kinase II.
1512232	12	119	theme	major	2247:2251	arg1	sites					2253:2257	the major sites	2243:2257	the major sites of phosphorylation catalyzed by casein kinase II	2243:2306	All the glycosylation sites identified in SRF are situated in a relatively short region of the primary sequence close to or within the transcriptional activation domain which is distant from the major sites of phosphorylation catalyzed by casein kinase II.
1512232	3	120	theme	many	397:400	arg1	factors					434:440	many RNA polymerase II transcription factors	397:440	many RNA polymerase II transcription factors	397:440	58, 841-874), including many RNA polymerase II transcription factors (Jackson, S. P., and Tjian, R. (1988) Cell 55, 125-133).
12684542	1	0	theme	N-acetylglucosamine	169:187	arg1	moiety					189:194	a single N-acetylglucosamine moiety	160:194	a single N-acetylglucosamine moiety O-linked to serine and threonine residues of nuclear and cytoplasmic proteins	160:272	The addition of a single N-acetylglucosamine moiety O-linked to serine and threonine residues of nuclear and cytoplasmic proteins is a widespread post-translational modification.
12684542	8	1	theme	modification	874:885	arg1	sites					856:860	previously undetected sites	834:860	previously undetected sites of O-GlcNAc modification of the transcription factor serum response factor	834:935	In this work utilization of this new approach has revealed previously undetected sites of O-GlcNAc modification of the transcription factor serum response factor.
12684542	8	1	theme	modification	874:885	arg1	modification					874:885	O-GlcNAc modification	865:885	O-GlcNAc modification of the transcription factor serum response factor	865:935	In this work utilization of this new approach has revealed previously undetected sites of O-GlcNAc modification of the transcription factor serum response factor.
12684542	0	2	theme	factor	86:91	arg1	modification					55:66	O-N-acetylglucosamine modification	33:66	O-N-acetylglucosamine modification of serum response factor using quadrupole time-of-flight mass spectrometry	33:141	Identification of novel sites of O-N-acetylglucosamine modification of serum response factor using quadrupole time-of-flight mass spectrometry.
12684542	1	3	theme	moiety	189:194	arg1	addition					148:155	The addition	144:155	The addition of a single N-acetylglucosamine moiety O-linked to serine and threonine residues of nuclear and cytoplasmic proteins	144:272	The addition of a single N-acetylglucosamine moiety O-linked to serine and threonine residues of nuclear and cytoplasmic proteins is a widespread post-translational modification.
12684542	1	3	theme	moiety	189:194	arg1	modification					309:320	a widespread post-translational modification	277:320	a widespread post-translational modification	277:320	The addition of a single N-acetylglucosamine moiety O-linked to serine and threonine residues of nuclear and cytoplasmic proteins is a widespread post-translational modification.
12684542	8	4	theme	transcription	894:906	arg1	factor					930:935	the transcription factor serum response factor	890:935	the transcription factor serum response factor	890:935	In this work utilization of this new approach has revealed previously undetected sites of O-GlcNAc modification of the transcription factor serum response factor.
12684542	1	5	theme	widespread	279:288	arg1	addition					148:155	The addition	144:155	The addition of a single N-acetylglucosamine moiety O-linked to serine and threonine residues of nuclear and cytoplasmic proteins	144:272	The addition of a single N-acetylglucosamine moiety O-linked to serine and threonine residues of nuclear and cytoplasmic proteins is a widespread post-translational modification.
12684542	1	5	theme	widespread	279:288	arg1	modification					309:320	a widespread post-translational modification	277:320	a widespread post-translational modification	277:320	The addition of a single N-acetylglucosamine moiety O-linked to serine and threonine residues of nuclear and cytoplasmic proteins is a widespread post-translational modification.
12684542	0	6	theme	time-of-flight	110:123	arg1	spectrometry					130:141	quadrupole time-of-flight mass spectrometry	99:141	quadrupole time-of-flight mass spectrometry	99:141	Identification of novel sites of O-N-acetylglucosamine modification of serum response factor using quadrupole time-of-flight mass spectrometry.
12684542	1	7	theme	post-translational	290:307	arg1	addition					148:155	The addition	144:155	The addition of a single N-acetylglucosamine moiety O-linked to serine and threonine residues of nuclear and cytoplasmic proteins	144:272	The addition of a single N-acetylglucosamine moiety O-linked to serine and threonine residues of nuclear and cytoplasmic proteins is a widespread post-translational modification.
12684542	1	7	theme	post-translational	290:307	arg1	modification					309:320	a widespread post-translational modification	277:320	a widespread post-translational modification	277:320	The addition of a single N-acetylglucosamine moiety O-linked to serine and threonine residues of nuclear and cytoplasmic proteins is a widespread post-translational modification.
12684542	0	8	theme	quadrupole	99:108	arg1	spectrometry					130:141	quadrupole time-of-flight mass spectrometry	99:141	quadrupole time-of-flight mass spectrometry	99:141	Identification of novel sites of O-N-acetylglucosamine modification of serum response factor using quadrupole time-of-flight mass spectrometry.
12684542	2	9	theme	conventional	327:338	arg1	method					340:345	The conventional method	323:345	The conventional method for detecting and locating sites of modification	323:394	The conventional method for detecting and locating sites of modification is through a multistep radioactivity-based approach.
12684542	8	10	theme	serum	915:919	arg1	factor					930:935	the transcription factor serum response factor	890:935	the transcription factor serum response factor	890:935	In this work utilization of this new approach has revealed previously undetected sites of O-GlcNAc modification of the transcription factor serum response factor.
12684542	3	11	theme	tandem	558:563	arg1	spectrometry					570:581	quadrupole time-of-flight tandem mass spectrometry	532:581	quadrupole time-of-flight tandem mass spectrometry (Chalkley, R. J., and Burlingame, A. L. (2001) Identification of GlcNAcylation sites of peptides and alpha-crystallin using Q-TOF mass spectrometry	532:729	We have recently shown that sites of O-GlcNAc modification can be determined using quadrupole time-of-flight tandem mass spectrometry (Chalkley, R. J., and Burlingame, A. L. (2001) Identification of GlcNAcylation sites of peptides and alpha-crystallin using Q-TOF mass spectrometry.
12684542	3	12	dep	J.	597:598	arg1	Identification					630:643	Identification	630:643	Chalkley, R. J., and Burlingame, A. L. (2001) Identification of GlcNAcylation sites of peptides and alpha-crystallin using Q-TOF mass spectrometry	584:729	We have recently shown that sites of O-GlcNAc modification can be determined using quadrupole time-of-flight tandem mass spectrometry (Chalkley, R. J., and Burlingame, A. L. (2001) Identification of GlcNAcylation sites of peptides and alpha-crystallin using Q-TOF mass spectrometry.
12684542	3	12	dep	J.	597:598	arg1	L					620:620	L	620:620	L	620:620	We have recently shown that sites of O-GlcNAc modification can be determined using quadrupole time-of-flight tandem mass spectrometry (Chalkley, R. J., and Burlingame, A. L. (2001) Identification of GlcNAcylation sites of peptides and alpha-crystallin using Q-TOF mass spectrometry.
12684542	8	13	theme	factor	908:913	arg1	factor					930:935	the transcription factor serum response factor	890:935	the transcription factor serum response factor	890:935	In this work utilization of this new approach has revealed previously undetected sites of O-GlcNAc modification of the transcription factor serum response factor.
12684542	1	14	theme	O-linked	196:203	arg1	moiety					189:194	a single N-acetylglucosamine moiety	160:194	a single N-acetylglucosamine moiety O-linked to serine and threonine residues of nuclear and cytoplasmic proteins	160:272	The addition of a single N-acetylglucosamine moiety O-linked to serine and threonine residues of nuclear and cytoplasmic proteins is a widespread post-translational modification.
12684542	0	15	theme	mass	125:128	arg1	spectrometry					130:141	quadrupole time-of-flight mass spectrometry	99:141	quadrupole time-of-flight mass spectrometry	99:141	Identification of novel sites of O-N-acetylglucosamine modification of serum response factor using quadrupole time-of-flight mass spectrometry.
12684542	3	16	dep	spectrometry	570:581	arg1	A.					617:618	A.	617:618	A.	617:618	We have recently shown that sites of O-GlcNAc modification can be determined using quadrupole time-of-flight tandem mass spectrometry (Chalkley, R. J., and Burlingame, A. L. (2001) Identification of GlcNAcylation sites of peptides and alpha-crystallin using Q-TOF mass spectrometry.
12684542	3	16	dep	spectrometry	570:581	arg1	J.					597:598	J.	597:598	J.	597:598	We have recently shown that sites of O-GlcNAc modification can be determined using quadrupole time-of-flight tandem mass spectrometry (Chalkley, R. J., and Burlingame, A. L. (2001) Identification of GlcNAcylation sites of peptides and alpha-crystallin using Q-TOF mass spectrometry.
12684542	3	16	dep	spectrometry	570:581	arg1	2001					624:627	2001	624:627	2001	624:627	We have recently shown that sites of O-GlcNAc modification can be determined using quadrupole time-of-flight tandem mass spectrometry (Chalkley, R. J., and Burlingame, A. L. (2001) Identification of GlcNAcylation sites of peptides and alpha-crystallin using Q-TOF mass spectrometry.
12684542	3	16	dep	spectrometry	570:581	arg1	R.					594:595	R.	594:595	R.	594:595	We have recently shown that sites of O-GlcNAc modification can be determined using quadrupole time-of-flight tandem mass spectrometry (Chalkley, R. J., and Burlingame, A. L. (2001) Identification of GlcNAcylation sites of peptides and alpha-crystallin using Q-TOF mass spectrometry.
12684542	6	17	theme	Mass	744:747	arg1	Spectrom					749:756	Mass Spectrom	744:756	Mass Spectrom.	744:757	Mass Spectrom.
12684542	8	18	theme	factor	930:935	arg1	modification					874:885	O-GlcNAc modification	865:885	O-GlcNAc modification of the transcription factor serum response factor	865:935	In this work utilization of this new approach has revealed previously undetected sites of O-GlcNAc modification of the transcription factor serum response factor.
12684542	1	19	link	O-linked	196:203	arg1	moiety					189:194	a single N-acetylglucosamine moiety	160:194	a single N-acetylglucosamine moiety O-linked to serine and threonine residues of nuclear and cytoplasmic proteins	160:272	The addition of a single N-acetylglucosamine moiety O-linked to serine and threonine residues of nuclear and cytoplasmic proteins is a widespread post-translational modification.
12684542	2	20	theme	locating	365:372	arg1	modification					383:394	modification	383:394	modification	383:394	The conventional method for detecting and locating sites of modification is through a multistep radioactivity-based approach.
12684542	2	20	theme	locating	365:372	arg1	sites					374:378	detecting and locating sites	351:378	detecting and locating sites of modification	351:394	The conventional method for detecting and locating sites of modification is through a multistep radioactivity-based approach.
12684542	8	21	theme	response	921:928	arg1	factor					930:935	the transcription factor serum response factor	890:935	the transcription factor serum response factor	890:935	In this work utilization of this new approach has revealed previously undetected sites of O-GlcNAc modification of the transcription factor serum response factor.
12684542	0	22	mod	modification	55:66	arg1	factor					86:91	serum response factor	71:91	serum response factor using quadrupole time-of-flight mass spectrometry	71:141	Identification of novel sites of O-N-acetylglucosamine modification of serum response factor using quadrupole time-of-flight mass spectrometry.
12684542	0	22	mod	modification	55:66	arg3	O-N-acetylglucosamine					33:53	O-N-acetylglucosamine modification	33:66	O-N-acetylglucosamine modification of serum response factor using quadrupole time-of-flight mass spectrometry	33:141	Identification of novel sites of O-N-acetylglucosamine modification of serum response factor using quadrupole time-of-flight mass spectrometry.
12684542	3	23	theme	O-GlcNAc	486:493	arg1	modification					495:506	O-GlcNAc modification	486:506	O-GlcNAc modification	486:506	We have recently shown that sites of O-GlcNAc modification can be determined using quadrupole time-of-flight tandem mass spectrometry (Chalkley, R. J., and Burlingame, A. L. (2001) Identification of GlcNAcylation sites of peptides and alpha-crystallin using Q-TOF mass spectrometry.
12684542	0	24	theme	sites	24:28	arg1	Identification					0:13	Identification	0:13	Identification of novel sites of O-N-acetylglucosamine modification of serum response factor using quadrupole time-of-flight mass spectrometry.	0:142	Identification of novel sites of O-N-acetylglucosamine modification of serum response factor using quadrupole time-of-flight mass spectrometry.
12684542	2	25	theme	detecting	351:359	arg1	modification					383:394	modification	383:394	modification	383:394	The conventional method for detecting and locating sites of modification is through a multistep radioactivity-based approach.
12684542	2	25	theme	detecting	351:359	arg1	sites					374:378	detecting and locating sites	351:378	detecting and locating sites of modification	351:394	The conventional method for detecting and locating sites of modification is through a multistep radioactivity-based approach.
12684542	0	26	theme	novel	18:22	arg1	sites					24:28	novel sites	18:28	novel sites of O-N-acetylglucosamine modification of serum response factor using quadrupole time-of-flight mass spectrometry	18:141	Identification of novel sites of O-N-acetylglucosamine modification of serum response factor using quadrupole time-of-flight mass spectrometry.
12684542	0	26	theme	novel	18:22	arg1	modification					55:66	O-N-acetylglucosamine modification	33:66	O-N-acetylglucosamine modification of serum response factor using quadrupole time-of-flight mass spectrometry	33:141	Identification of novel sites of O-N-acetylglucosamine modification of serum response factor using quadrupole time-of-flight mass spectrometry.
12684542	3	27	theme	alpha-crystallin	684:699	arg1	alpha-crystallin					684:699	alpha-crystallin	684:699	alpha-crystallin using Q-TOF mass spectrometry	684:729	We have recently shown that sites of O-GlcNAc modification can be determined using quadrupole time-of-flight tandem mass spectrometry (Chalkley, R. J., and Burlingame, A. L. (2001) Identification of GlcNAcylation sites of peptides and alpha-crystallin using Q-TOF mass spectrometry.
12684542	3	27	theme	alpha-crystallin	684:699	arg1	peptides					671:678	peptides	671:678	peptides	671:678	We have recently shown that sites of O-GlcNAc modification can be determined using quadrupole time-of-flight tandem mass spectrometry (Chalkley, R. J., and Burlingame, A. L. (2001) Identification of GlcNAcylation sites of peptides and alpha-crystallin using Q-TOF mass spectrometry.
12684542	3	27	theme	alpha-crystallin	684:699	arg1	sites					662:666	GlcNAcylation sites	648:666	GlcNAcylation sites of peptides and alpha-crystallin using Q-TOF mass spectrometry	648:729	We have recently shown that sites of O-GlcNAc modification can be determined using quadrupole time-of-flight tandem mass spectrometry (Chalkley, R. J., and Burlingame, A. L. (2001) Identification of GlcNAcylation sites of peptides and alpha-crystallin using Q-TOF mass spectrometry.
12684542	3	28	theme	quadrupole	532:541	arg1	spectrometry					570:581	quadrupole time-of-flight tandem mass spectrometry	532:581	quadrupole time-of-flight tandem mass spectrometry (Chalkley, R. J., and Burlingame, A. L. (2001) Identification of GlcNAcylation sites of peptides and alpha-crystallin using Q-TOF mass spectrometry	532:729	We have recently shown that sites of O-GlcNAc modification can be determined using quadrupole time-of-flight tandem mass spectrometry (Chalkley, R. J., and Burlingame, A. L. (2001) Identification of GlcNAcylation sites of peptides and alpha-crystallin using Q-TOF mass spectrometry.
12684542	0	29	theme	O-N-acetylglucosamine	33:53	arg1	modification					55:66	O-N-acetylglucosamine modification	33:66	O-N-acetylglucosamine modification of serum response factor using quadrupole time-of-flight mass spectrometry	33:141	Identification of novel sites of O-N-acetylglucosamine modification of serum response factor using quadrupole time-of-flight mass spectrometry.
12684542	1	30	dep	serine	208:213	arg1	residues					229:236	residues	229:236	residues	229:236	The addition of a single N-acetylglucosamine moiety O-linked to serine and threonine residues of nuclear and cytoplasmic proteins is a widespread post-translational modification.
12684542	8	31	mod	modification	874:885	arg1	factor					930:935	the transcription factor serum response factor	890:935	the transcription factor serum response factor	890:935	In this work utilization of this new approach has revealed previously undetected sites of O-GlcNAc modification of the transcription factor serum response factor.
12684542	8	31	mod	modification	874:885	arg3	O-GlcNAc					865:872	O-GlcNAc modification	865:885	O-GlcNAc modification of the transcription factor serum response factor	865:935	In this work utilization of this new approach has revealed previously undetected sites of O-GlcNAc modification of the transcription factor serum response factor.
12684542	3	32	theme	modification	495:506	arg1	modification					495:506	O-GlcNAc modification	486:506	O-GlcNAc modification	486:506	We have recently shown that sites of O-GlcNAc modification can be determined using quadrupole time-of-flight tandem mass spectrometry (Chalkley, R. J., and Burlingame, A. L. (2001) Identification of GlcNAcylation sites of peptides and alpha-crystallin using Q-TOF mass spectrometry.
12684542	3	32	theme	modification	495:506	arg1	sites					477:481	sites	477:481	sites of O-GlcNAc modification	477:506	We have recently shown that sites of O-GlcNAc modification can be determined using quadrupole time-of-flight tandem mass spectrometry (Chalkley, R. J., and Burlingame, A. L. (2001) Identification of GlcNAcylation sites of peptides and alpha-crystallin using Q-TOF mass spectrometry.
12684542	8	33	theme	approach	812:819	arg1	utilization					788:798	utilization	788:798	utilization of this new approach	788:819	In this work utilization of this new approach has revealed previously undetected sites of O-GlcNAc modification of the transcription factor serum response factor.
12684542	3	34	theme	peptides	671:678	arg1	alpha-crystallin					684:699	alpha-crystallin	684:699	alpha-crystallin using Q-TOF mass spectrometry	684:729	We have recently shown that sites of O-GlcNAc modification can be determined using quadrupole time-of-flight tandem mass spectrometry (Chalkley, R. J., and Burlingame, A. L. (2001) Identification of GlcNAcylation sites of peptides and alpha-crystallin using Q-TOF mass spectrometry.
12684542	3	34	theme	peptides	671:678	arg1	peptides					671:678	peptides	671:678	peptides	671:678	We have recently shown that sites of O-GlcNAc modification can be determined using quadrupole time-of-flight tandem mass spectrometry (Chalkley, R. J., and Burlingame, A. L. (2001) Identification of GlcNAcylation sites of peptides and alpha-crystallin using Q-TOF mass spectrometry.
12684542	3	34	theme	peptides	671:678	arg1	sites					662:666	GlcNAcylation sites	648:666	GlcNAcylation sites of peptides and alpha-crystallin using Q-TOF mass spectrometry	648:729	We have recently shown that sites of O-GlcNAc modification can be determined using quadrupole time-of-flight tandem mass spectrometry (Chalkley, R. J., and Burlingame, A. L. (2001) Identification of GlcNAcylation sites of peptides and alpha-crystallin using Q-TOF mass spectrometry.
12684542	8	35	theme	new	808:810	arg1	approach					812:819	this new approach	803:819	this new approach	803:819	In this work utilization of this new approach has revealed previously undetected sites of O-GlcNAc modification of the transcription factor serum response factor.
12684542	1	36	theme	nuclear	241:247	arg1	proteins					265:272	nuclear and cytoplasmic proteins	241:272	nuclear and cytoplasmic proteins	241:272	The addition of a single N-acetylglucosamine moiety O-linked to serine and threonine residues of nuclear and cytoplasmic proteins is a widespread post-translational modification.
12684542	3	37	theme	mass	565:568	arg1	spectrometry					570:581	quadrupole time-of-flight tandem mass spectrometry	532:581	quadrupole time-of-flight tandem mass spectrometry (Chalkley, R. J., and Burlingame, A. L. (2001) Identification of GlcNAcylation sites of peptides and alpha-crystallin using Q-TOF mass spectrometry	532:729	We have recently shown that sites of O-GlcNAc modification can be determined using quadrupole time-of-flight tandem mass spectrometry (Chalkley, R. J., and Burlingame, A. L. (2001) Identification of GlcNAcylation sites of peptides and alpha-crystallin using Q-TOF mass spectrometry.
12684542	0	38	theme	modification	55:66	arg1	sites					24:28	novel sites	18:28	novel sites of O-N-acetylglucosamine modification of serum response factor using quadrupole time-of-flight mass spectrometry	18:141	Identification of novel sites of O-N-acetylglucosamine modification of serum response factor using quadrupole time-of-flight mass spectrometry.
12684542	0	38	theme	modification	55:66	arg1	modification					55:66	O-N-acetylglucosamine modification	33:66	O-N-acetylglucosamine modification of serum response factor using quadrupole time-of-flight mass spectrometry	33:141	Identification of novel sites of O-N-acetylglucosamine modification of serum response factor using quadrupole time-of-flight mass spectrometry.
12684542	2	39	theme	modification	383:394	arg1	modification					383:394	modification	383:394	modification	383:394	The conventional method for detecting and locating sites of modification is through a multistep radioactivity-based approach.
12684542	2	39	theme	modification	383:394	arg1	sites					374:378	detecting and locating sites	351:378	detecting and locating sites of modification	351:394	The conventional method for detecting and locating sites of modification is through a multistep radioactivity-based approach.
12684542	3	40	theme	sites	662:666	arg1	Identification					630:643	Identification	630:643	Chalkley, R. J., and Burlingame, A. L. (2001) Identification of GlcNAcylation sites of peptides and alpha-crystallin using Q-TOF mass spectrometry	584:729	We have recently shown that sites of O-GlcNAc modification can be determined using quadrupole time-of-flight tandem mass spectrometry (Chalkley, R. J., and Burlingame, A. L. (2001) Identification of GlcNAcylation sites of peptides and alpha-crystallin using Q-TOF mass spectrometry.
12684542	3	41	theme	time-of-flight	543:556	arg1	spectrometry					570:581	quadrupole time-of-flight tandem mass spectrometry	532:581	quadrupole time-of-flight tandem mass spectrometry (Chalkley, R. J., and Burlingame, A. L. (2001) Identification of GlcNAcylation sites of peptides and alpha-crystallin using Q-TOF mass spectrometry	532:729	We have recently shown that sites of O-GlcNAc modification can be determined using quadrupole time-of-flight tandem mass spectrometry (Chalkley, R. J., and Burlingame, A. L. (2001) Identification of GlcNAcylation sites of peptides and alpha-crystallin using Q-TOF mass spectrometry.
12684542	8	42	theme	undetected	845:854	arg1	sites					856:860	previously undetected sites	834:860	previously undetected sites of O-GlcNAc modification of the transcription factor serum response factor	834:935	In this work utilization of this new approach has revealed previously undetected sites of O-GlcNAc modification of the transcription factor serum response factor.
12684542	8	42	theme	undetected	845:854	arg1	modification					874:885	O-GlcNAc modification	865:885	O-GlcNAc modification of the transcription factor serum response factor	865:935	In this work utilization of this new approach has revealed previously undetected sites of O-GlcNAc modification of the transcription factor serum response factor.
12684542	3	43	theme	Q-TOF	707:711	arg1	spectrometry					718:729	Q-TOF mass spectrometry	707:729	Q-TOF mass spectrometry	707:729	We have recently shown that sites of O-GlcNAc modification can be determined using quadrupole time-of-flight tandem mass spectrometry (Chalkley, R. J., and Burlingame, A. L. (2001) Identification of GlcNAcylation sites of peptides and alpha-crystallin using Q-TOF mass spectrometry.
12684542	2	44	theme	multistep	409:417	arg1	approach					439:446	a multistep radioactivity-based approach	407:446	a multistep radioactivity-based approach	407:446	The conventional method for detecting and locating sites of modification is through a multistep radioactivity-based approach.
12684542	8	45	theme	O-GlcNAc	865:872	arg1	modification					874:885	O-GlcNAc modification	865:885	O-GlcNAc modification of the transcription factor serum response factor	865:935	In this work utilization of this new approach has revealed previously undetected sites of O-GlcNAc modification of the transcription factor serum response factor.
12684542	1	46	theme	cytoplasmic	253:263	arg1	proteins					265:272	nuclear and cytoplasmic proteins	241:272	nuclear and cytoplasmic proteins	241:272	The addition of a single N-acetylglucosamine moiety O-linked to serine and threonine residues of nuclear and cytoplasmic proteins is a widespread post-translational modification.
12684542	0	47	theme	response	77:84	arg1	factor					86:91	serum response factor	71:91	serum response factor using quadrupole time-of-flight mass spectrometry	71:141	Identification of novel sites of O-N-acetylglucosamine modification of serum response factor using quadrupole time-of-flight mass spectrometry.
12684542	3	48	theme	mass	713:716	arg1	spectrometry					718:729	Q-TOF mass spectrometry	707:729	Q-TOF mass spectrometry	707:729	We have recently shown that sites of O-GlcNAc modification can be determined using quadrupole time-of-flight tandem mass spectrometry (Chalkley, R. J., and Burlingame, A. L. (2001) Identification of GlcNAcylation sites of peptides and alpha-crystallin using Q-TOF mass spectrometry.
12684542	2	49	theme	radioactivity-based	419:437	arg1	approach					439:446	a multistep radioactivity-based approach	407:446	a multistep radioactivity-based approach	407:446	The conventional method for detecting and locating sites of modification is through a multistep radioactivity-based approach.
12684542	1	50	theme	proteins	265:272	arg1	serine					208:213	serine	208:213	serine	208:213	The addition of a single N-acetylglucosamine moiety O-linked to serine and threonine residues of nuclear and cytoplasmic proteins is a widespread post-translational modification.
12684542	1	50	theme	proteins	265:272	arg1	threonine					219:227	threonine	219:227	threonine	219:227	The addition of a single N-acetylglucosamine moiety O-linked to serine and threonine residues of nuclear and cytoplasmic proteins is a widespread post-translational modification.
12684542	0	51	theme	serum	71:75	arg1	factor					86:91	serum response factor	71:91	serum response factor using quadrupole time-of-flight mass spectrometry	71:141	Identification of novel sites of O-N-acetylglucosamine modification of serum response factor using quadrupole time-of-flight mass spectrometry.
12684542	3	52	theme	GlcNAcylation	648:660	arg1	alpha-crystallin					684:699	alpha-crystallin	684:699	alpha-crystallin using Q-TOF mass spectrometry	684:729	We have recently shown that sites of O-GlcNAc modification can be determined using quadrupole time-of-flight tandem mass spectrometry (Chalkley, R. J., and Burlingame, A. L. (2001) Identification of GlcNAcylation sites of peptides and alpha-crystallin using Q-TOF mass spectrometry.
12684542	3	52	theme	GlcNAcylation	648:660	arg1	peptides					671:678	peptides	671:678	peptides	671:678	We have recently shown that sites of O-GlcNAc modification can be determined using quadrupole time-of-flight tandem mass spectrometry (Chalkley, R. J., and Burlingame, A. L. (2001) Identification of GlcNAcylation sites of peptides and alpha-crystallin using Q-TOF mass spectrometry.
12684542	3	52	theme	GlcNAcylation	648:660	arg1	sites					662:666	GlcNAcylation sites	648:666	GlcNAcylation sites of peptides and alpha-crystallin using Q-TOF mass spectrometry	648:729	We have recently shown that sites of O-GlcNAc modification can be determined using quadrupole time-of-flight tandem mass spectrometry (Chalkley, R. J., and Burlingame, A. L. (2001) Identification of GlcNAcylation sites of peptides and alpha-crystallin using Q-TOF mass spectrometry.
12684542	1	53	theme	single	162:167	arg1	moiety					189:194	a single N-acetylglucosamine moiety	160:194	a single N-acetylglucosamine moiety O-linked to serine and threonine residues of nuclear and cytoplasmic proteins	160:272	The addition of a single N-acetylglucosamine moiety O-linked to serine and threonine residues of nuclear and cytoplasmic proteins is a widespread post-translational modification.
26280537	5	0	theme	MIF	826:828	arg1	regulation					812:821	the negative regulation	799:821	the negative regulation of MIF on EGFR	799:836	Activation of EGFR through mutation or its ligand binding enhances the secretion of MMP13, which degrades extracellular MIF, and results in abrogation of the negative regulation of MIF on EGFR.
26280537	4	1	theme	tumour	627:632	arg1	formation					634:642	brain tumour formation	621:642	brain tumour formation	621:642	The naturally secreted and O-GlcNAcylated MIF binds to EGFR, thereby inhibiting the binding of EGF to EGFR and EGF-induced EGFR activation, phosphorylation of ERK and c-Jun, cell invasion, proliferation and brain tumour formation.
26280537	3	2	theme	migration	318:326	arg1	MIF					347:349	MIF	347:349	MIF	347:349	We found that human macrophage migration inhibitory factor (MIF) is O-GlcNAcylated at Ser 112/Thr 113 at its carboxy terminus.
26280537	3	2	theme	migration	318:326	arg1	factor					339:344	human macrophage migration inhibitory factor	301:344	human macrophage migration inhibitory factor (MIF)	301:350	We found that human macrophage migration inhibitory factor (MIF) is O-GlcNAcylated at Ser 112/Thr 113 at its carboxy terminus.
26280537	2	3	theme	human	255:259	arg1	EGFR					261:264	human EGFR	255:264	human EGFR	255:264	However, no extracellular antagonist of human EGFR has been identified.
26280537	4	4	theme	EGFR	537:540	arg1	activation					542:551	EGF-induced EGFR activation	525:551	EGF-induced EGFR activation	525:551	The naturally secreted and O-GlcNAcylated MIF binds to EGFR, thereby inhibiting the binding of EGF to EGFR and EGF-induced EGFR activation, phosphorylation of ERK and c-Jun, cell invasion, proliferation and brain tumour formation.
26280537	3	5	theme	inhibitory	328:337	arg1	MIF					347:349	MIF	347:349	MIF	347:349	We found that human macrophage migration inhibitory factor (MIF) is O-GlcNAcylated at Ser 112/Thr 113 at its carboxy terminus.
26280537	3	5	theme	inhibitory	328:337	arg1	factor					339:344	human macrophage migration inhibitory factor	301:344	human macrophage migration inhibitory factor (MIF)	301:350	We found that human macrophage migration inhibitory factor (MIF) is O-GlcNAcylated at Ser 112/Thr 113 at its carboxy terminus.
26280537	4	6	theme	secreted	428:435	arg1	MIF					456:458	The naturally secreted and O-GlcNAcylated MIF	414:458	The naturally secreted and O-GlcNAcylated MIF	414:458	The naturally secreted and O-GlcNAcylated MIF binds to EGFR, thereby inhibiting the binding of EGF to EGFR and EGF-induced EGFR activation, phosphorylation of ERK and c-Jun, cell invasion, proliferation and brain tumour formation.
26280537	6	7	theme	tumour	908:913	arg1	microenvironment					915:930	the tumour microenvironment	904:930	the tumour microenvironment	904:930	The finding that EGFR activation downregulates its antagonist in the tumour microenvironment represents an important feedforward mechanism for human tumour cells to enhance EGFR signalling and promote tumorigenesis.
26280537	5	8	from	regulation	812:821	arg1	EGFR					833:836	EGFR	833:836	EGFR	833:836	Activation of EGFR through mutation or its ligand binding enhances the secretion of MMP13, which degrades extracellular MIF, and results in abrogation of the negative regulation of MIF on EGFR.
26280537	4	9	theme	EGF-induced	525:535	arg1	activation					542:551	EGF-induced EGFR activation	525:551	EGF-induced EGFR activation	525:551	The naturally secreted and O-GlcNAcylated MIF binds to EGFR, thereby inhibiting the binding of EGF to EGFR and EGF-induced EGFR activation, phosphorylation of ERK and c-Jun, cell invasion, proliferation and brain tumour formation.
26280537	3	10	theme	human	301:305	arg1	MIF					347:349	MIF	347:349	MIF	347:349	We found that human macrophage migration inhibitory factor (MIF) is O-GlcNAcylated at Ser 112/Thr 113 at its carboxy terminus.
26280537	3	10	theme	human	301:305	arg1	factor					339:344	human macrophage migration inhibitory factor	301:344	human macrophage migration inhibitory factor (MIF)	301:350	We found that human macrophage migration inhibitory factor (MIF) is O-GlcNAcylated at Ser 112/Thr 113 at its carboxy terminus.
26280537	4	11	theme	ERK	573:575	arg1	activation					542:551	EGF-induced EGFR activation	525:551	EGF-induced EGFR activation	525:551	The naturally secreted and O-GlcNAcylated MIF binds to EGFR, thereby inhibiting the binding of EGF to EGFR and EGF-induced EGFR activation, phosphorylation of ERK and c-Jun, cell invasion, proliferation and brain tumour formation.
26280537	4	11	theme	ERK	573:575	arg1	formation					634:642	brain tumour formation	621:642	brain tumour formation	621:642	The naturally secreted and O-GlcNAcylated MIF binds to EGFR, thereby inhibiting the binding of EGF to EGFR and EGF-induced EGFR activation, phosphorylation of ERK and c-Jun, cell invasion, proliferation and brain tumour formation.
26280537	4	11	theme	ERK	573:575	arg1	phosphorylation					554:568	phosphorylation	554:568	phosphorylation of ERK and c-Jun	554:585	The naturally secreted and O-GlcNAcylated MIF binds to EGFR, thereby inhibiting the binding of EGF to EGFR and EGF-induced EGFR activation, phosphorylation of ERK and c-Jun, cell invasion, proliferation and brain tumour formation.
26280537	4	11	theme	ERK	573:575	arg1	invasion					593:600	cell invasion	588:600	cell invasion	588:600	The naturally secreted and O-GlcNAcylated MIF binds to EGFR, thereby inhibiting the binding of EGF to EGFR and EGF-induced EGFR activation, phosphorylation of ERK and c-Jun, cell invasion, proliferation and brain tumour formation.
26280537	4	11	theme	ERK	573:575	arg1	EGFR					516:519	EGFR	516:519	EGFR	516:519	The naturally secreted and O-GlcNAcylated MIF binds to EGFR, thereby inhibiting the binding of EGF to EGFR and EGF-induced EGFR activation, phosphorylation of ERK and c-Jun, cell invasion, proliferation and brain tumour formation.
26280537	4	11	theme	ERK	573:575	arg1	proliferation					603:615	proliferation	603:615	proliferation	603:615	The naturally secreted and O-GlcNAcylated MIF binds to EGFR, thereby inhibiting the binding of EGF to EGFR and EGF-induced EGFR activation, phosphorylation of ERK and c-Jun, cell invasion, proliferation and brain tumour formation.
26280537	3	12	theme	macrophage	307:316	arg1	MIF					347:349	MIF	347:349	MIF	347:349	We found that human macrophage migration inhibitory factor (MIF) is O-GlcNAcylated at Ser 112/Thr 113 at its carboxy terminus.
26280537	3	12	theme	macrophage	307:316	arg1	factor					339:344	human macrophage migration inhibitory factor	301:344	human macrophage migration inhibitory factor (MIF)	301:350	We found that human macrophage migration inhibitory factor (MIF) is O-GlcNAcylated at Ser 112/Thr 113 at its carboxy terminus.
26280537	4	13	theme	O-GlcNAcylated	441:454	arg1	MIF					456:458	The naturally secreted and O-GlcNAcylated MIF	414:458	The naturally secreted and O-GlcNAcylated MIF	414:458	The naturally secreted and O-GlcNAcylated MIF binds to EGFR, thereby inhibiting the binding of EGF to EGFR and EGF-induced EGFR activation, phosphorylation of ERK and c-Jun, cell invasion, proliferation and brain tumour formation.
26280537	2	14	theme	extracellular	227:239	arg1	antagonist					241:250	no extracellular antagonist	224:250	no extracellular antagonist of human EGFR	224:264	However, no extracellular antagonist of human EGFR has been identified.
26280537	4	15	theme	cell	588:591	arg1	invasion					593:600	cell invasion	588:600	cell invasion	588:600	The naturally secreted and O-GlcNAcylated MIF binds to EGFR, thereby inhibiting the binding of EGF to EGFR and EGF-induced EGFR activation, phosphorylation of ERK and c-Jun, cell invasion, proliferation and brain tumour formation.
26280537	6	16	theme	EGFR	1012:1015	arg1	signalling					1017:1026	EGFR signalling	1012:1026	EGFR signalling	1012:1026	The finding that EGFR activation downregulates its antagonist in the tumour microenvironment represents an important feedforward mechanism for human tumour cells to enhance EGFR signalling and promote tumorigenesis.
26280537	0	17	theme	Secreted	0:7	arg1	MIF					28:30	Secreted and O-GlcNAcylated MIF	0:30	Secreted and O-GlcNAcylated MIF	0:30	Secreted and O-GlcNAcylated MIF binds to the human EGF receptor and inhibits its activation.
26280537	5	18	from	EGFR	833:836	arg1	abrogation					785:794	abrogation	785:794	abrogation of the negative regulation of MIF on EGFR	785:836	Activation of EGFR through mutation or its ligand binding enhances the secretion of MMP13, which degrades extracellular MIF, and results in abrogation of the negative regulation of MIF on EGFR.
26280537	5	19	theme	negative	803:810	arg1	regulation					812:821	the negative regulation	799:821	the negative regulation of MIF on EGFR	799:836	Activation of EGFR through mutation or its ligand binding enhances the secretion of MMP13, which degrades extracellular MIF, and results in abrogation of the negative regulation of MIF on EGFR.
26280537	5	20	theme	extracellular	751:763	arg1	MIF					765:767	extracellular MIF	751:767	extracellular MIF	751:767	Activation of EGFR through mutation or its ligand binding enhances the secretion of MMP13, which degrades extracellular MIF, and results in abrogation of the negative regulation of MIF on EGFR.
26280537	6	21	from	antagonist	890:899	arg1	microenvironment					915:930	the tumour microenvironment	904:930	the tumour microenvironment	904:930	The finding that EGFR activation downregulates its antagonist in the tumour microenvironment represents an important feedforward mechanism for human tumour cells to enhance EGFR signalling and promote tumorigenesis.
26280537	5	22	theme	MMP13	729:733	arg1	secretion					716:724	the secretion	712:724	the secretion	712:724	Activation of EGFR through mutation or its ligand binding enhances the secretion of MMP13, which degrades extracellular MIF, and results in abrogation of the negative regulation of MIF on EGFR.
26280537	1	23	theme	many	164:167	arg1	types					169:173	many types	164:173	many types of tumour	164:183	Activation of epidermal growth factor receptor (EGFR), which occurs in many types of tumour, promotes tumour progression.
26280537	0	24	theme	O-GlcNAcylated	13:26	arg1	MIF					28:30	Secreted and O-GlcNAcylated MIF	0:30	Secreted and O-GlcNAcylated MIF	0:30	Secreted and O-GlcNAcylated MIF binds to the human EGF receptor and inhibits its activation.
26280537	2	25	theme	EGFR	261:264	arg1	antagonist					241:250	no extracellular antagonist	224:250	no extracellular antagonist of human EGFR	224:264	However, no extracellular antagonist of human EGFR has been identified.
26280537	4	26	theme	brain	621:625	arg1	formation					634:642	brain tumour formation	621:642	brain tumour formation	621:642	The naturally secreted and O-GlcNAcylated MIF binds to EGFR, thereby inhibiting the binding of EGF to EGFR and EGF-induced EGFR activation, phosphorylation of ERK and c-Jun, cell invasion, proliferation and brain tumour formation.
26280537	4	27	theme	EGF	509:511	arg1	binding					498:504	the binding	494:504	the binding of EGF to EGFR and EGF-induced EGFR activation, phosphorylation of ERK and c-Jun, cell invasion, proliferation and brain tumour formation	494:642	The naturally secreted and O-GlcNAcylated MIF binds to EGFR, thereby inhibiting the binding of EGF to EGFR and EGF-induced EGFR activation, phosphorylation of ERK and c-Jun, cell invasion, proliferation and brain tumour formation.
26280537	6	28	theme	tumour	988:993	arg1	cells					995:999	human tumour cells	982:999	human tumour cells	982:999	The finding that EGFR activation downregulates its antagonist in the tumour microenvironment represents an important feedforward mechanism for human tumour cells to enhance EGFR signalling and promote tumorigenesis.
26280537	3	29	theme	carboxy	396:402	arg1	terminus					404:411	its carboxy terminus	392:411	its carboxy terminus	392:411	We found that human macrophage migration inhibitory factor (MIF) is O-GlcNAcylated at Ser 112/Thr 113 at its carboxy terminus.
26280537	3	30	theme	Ser	373:375	arg1	112/Thr					377:383	Ser 112/Thr 113	373:387	Ser 112/Thr 113 at its carboxy terminus	373:411	We found that human macrophage migration inhibitory factor (MIF) is O-GlcNAcylated at Ser 112/Thr 113 at its carboxy terminus.
26280537	5	31	theme	EGFR	659:662	arg1	Activation					645:654	Activation	645:654	Activation of EGFR through mutation or its ligand binding	645:701	Activation of EGFR through mutation or its ligand binding enhances the secretion of MMP13, which degrades extracellular MIF, and results in abrogation of the negative regulation of MIF on EGFR.
26280537	6	32	theme	feedforward	956:966	arg1	mechanism					968:976	an important feedforward mechanism	943:976	an important feedforward mechanism for human tumour cells	943:999	The finding that EGFR activation downregulates its antagonist in the tumour microenvironment represents an important feedforward mechanism for human tumour cells to enhance EGFR signalling and promote tumorigenesis.
26280537	1	33	theme	tumour	178:183	arg1	types					169:173	many types	164:173	many types of tumour	164:183	Activation of epidermal growth factor receptor (EGFR), which occurs in many types of tumour, promotes tumour progression.
26280537	0	34	theme	human	45:49	arg1	receptor					55:62	the human EGF receptor	41:62	the human EGF receptor	41:62	Secreted and O-GlcNAcylated MIF binds to the human EGF receptor and inhibits its activation.
26280537	5	35	theme	regulation	812:821	arg1	abrogation					785:794	abrogation	785:794	abrogation of the negative regulation of MIF on EGFR	785:836	Activation of EGFR through mutation or its ligand binding enhances the secretion of MMP13, which degrades extracellular MIF, and results in abrogation of the negative regulation of MIF on EGFR.
26280537	6	36	theme	human	982:986	arg1	cells					995:999	human tumour cells	982:999	human tumour cells	982:999	The finding that EGFR activation downregulates its antagonist in the tumour microenvironment represents an important feedforward mechanism for human tumour cells to enhance EGFR signalling and promote tumorigenesis.
26280537	3	37	from	terminus	404:411	arg1	112/Thr					377:383	Ser 112/Thr 113	373:387	Ser 112/Thr 113 at its carboxy terminus	373:411	We found that human macrophage migration inhibitory factor (MIF) is O-GlcNAcylated at Ser 112/Thr 113 at its carboxy terminus.
26280537	6	38	theme	EGFR	856:859	arg1	activation					861:870	EGFR activation	856:870	EGFR activation	856:870	The finding that EGFR activation downregulates its antagonist in the tumour microenvironment represents an important feedforward mechanism for human tumour cells to enhance EGFR signalling and promote tumorigenesis.
26280537	1	39	theme	epidermal	107:115	arg1	EGFR					141:144	EGFR	141:144	EGFR	141:144	Activation of epidermal growth factor receptor (EGFR), which occurs in many types of tumour, promotes tumour progression.
26280537	1	39	theme	epidermal	107:115	arg1	receptor					131:138	epidermal growth factor receptor	107:138	epidermal growth factor receptor (EGFR)	107:145	Activation of epidermal growth factor receptor (EGFR), which occurs in many types of tumour, promotes tumour progression.
26280537	1	40	theme	growth	117:122	arg1	EGFR					141:144	EGFR	141:144	EGFR	141:144	Activation of epidermal growth factor receptor (EGFR), which occurs in many types of tumour, promotes tumour progression.
26280537	1	40	theme	growth	117:122	arg1	receptor					131:138	epidermal growth factor receptor	107:138	epidermal growth factor receptor (EGFR)	107:145	Activation of epidermal growth factor receptor (EGFR), which occurs in many types of tumour, promotes tumour progression.
26280537	3	41	from	112/Thr	377:383	arg1	O-GlcNAcylated					355:368	O-GlcNAcylated	355:368	O-GlcNAcylated	355:368	We found that human macrophage migration inhibitory factor (MIF) is O-GlcNAcylated at Ser 112/Thr 113 at its carboxy terminus.
26280537	1	42	theme	factor	124:129	arg1	EGFR					141:144	EGFR	141:144	EGFR	141:144	Activation of epidermal growth factor receptor (EGFR), which occurs in many types of tumour, promotes tumour progression.
26280537	1	42	theme	factor	124:129	arg1	receptor					131:138	epidermal growth factor receptor	107:138	epidermal growth factor receptor (EGFR)	107:145	Activation of epidermal growth factor receptor (EGFR), which occurs in many types of tumour, promotes tumour progression.
26280537	5	43	theme	ligand	688:693	arg1	binding					695:701	its ligand binding	684:701	its ligand binding	684:701	Activation of EGFR through mutation or its ligand binding enhances the secretion of MMP13, which degrades extracellular MIF, and results in abrogation of the negative regulation of MIF on EGFR.
26280537	4	44	theme	c-Jun	581:585	arg1	activation					542:551	EGF-induced EGFR activation	525:551	EGF-induced EGFR activation	525:551	The naturally secreted and O-GlcNAcylated MIF binds to EGFR, thereby inhibiting the binding of EGF to EGFR and EGF-induced EGFR activation, phosphorylation of ERK and c-Jun, cell invasion, proliferation and brain tumour formation.
26280537	4	44	theme	c-Jun	581:585	arg1	formation					634:642	brain tumour formation	621:642	brain tumour formation	621:642	The naturally secreted and O-GlcNAcylated MIF binds to EGFR, thereby inhibiting the binding of EGF to EGFR and EGF-induced EGFR activation, phosphorylation of ERK and c-Jun, cell invasion, proliferation and brain tumour formation.
26280537	4	44	theme	c-Jun	581:585	arg1	phosphorylation					554:568	phosphorylation	554:568	phosphorylation of ERK and c-Jun	554:585	The naturally secreted and O-GlcNAcylated MIF binds to EGFR, thereby inhibiting the binding of EGF to EGFR and EGF-induced EGFR activation, phosphorylation of ERK and c-Jun, cell invasion, proliferation and brain tumour formation.
26280537	4	44	theme	c-Jun	581:585	arg1	invasion					593:600	cell invasion	588:600	cell invasion	588:600	The naturally secreted and O-GlcNAcylated MIF binds to EGFR, thereby inhibiting the binding of EGF to EGFR and EGF-induced EGFR activation, phosphorylation of ERK and c-Jun, cell invasion, proliferation and brain tumour formation.
26280537	4	44	theme	c-Jun	581:585	arg1	EGFR					516:519	EGFR	516:519	EGFR	516:519	The naturally secreted and O-GlcNAcylated MIF binds to EGFR, thereby inhibiting the binding of EGF to EGFR and EGF-induced EGFR activation, phosphorylation of ERK and c-Jun, cell invasion, proliferation and brain tumour formation.
26280537	4	44	theme	c-Jun	581:585	arg1	proliferation					603:615	proliferation	603:615	proliferation	603:615	The naturally secreted and O-GlcNAcylated MIF binds to EGFR, thereby inhibiting the binding of EGF to EGFR and EGF-induced EGFR activation, phosphorylation of ERK and c-Jun, cell invasion, proliferation and brain tumour formation.
26280537	1	45	theme	receptor	131:138	arg1	Activation					93:102	Activation	93:102	Activation of epidermal growth factor receptor (EGFR), which occurs in many types of tumour,	93:184	Activation of epidermal growth factor receptor (EGFR), which occurs in many types of tumour, promotes tumour progression.
26280537	1	46	theme	tumour	195:200	arg1	progression					202:212	tumour progression	195:212	tumour progression	195:212	Activation of epidermal growth factor receptor (EGFR), which occurs in many types of tumour, promotes tumour progression.
26280537	0	47	theme	EGF	51:53	arg1	receptor					55:62	the human EGF receptor	41:62	the human EGF receptor	41:62	Secreted and O-GlcNAcylated MIF binds to the human EGF receptor and inhibits its activation.
26280537	5	48	from	abrogation	785:794	arg1	EGFR					833:836	EGFR	833:836	EGFR	833:836	Activation of EGFR through mutation or its ligand binding enhances the secretion of MMP13, which degrades extracellular MIF, and results in abrogation of the negative regulation of MIF on EGFR.
26280537	6	49	theme	important	946:954	arg1	mechanism					968:976	an important feedforward mechanism	943:976	an important feedforward mechanism for human tumour cells	943:999	The finding that EGFR activation downregulates its antagonist in the tumour microenvironment represents an important feedforward mechanism for human tumour cells to enhance EGFR signalling and promote tumorigenesis.
25128556	11	0	theme	GRP78	1687:1691	arg1	up-regulation					1649:1661	the up-regulation	1645:1661	the up-regulation of the ER stress marker GRP78	1645:1691	The O-HexNAc sites were regulated by glucosamine treatment and correlated with the up-regulation of the ER stress marker GRP78.
25128556	12	1	theme	higher	1808:1813	arg1	occupancy					1815:1823	a higher occupancy	1806:1823	a higher occupancy in the cytosolic fraction	1806:1849	The occupancy of O-HexNAc on GLU2B and calnexin sites differed between the cytosolic and nuclear fractions with a higher occupancy in the cytosolic fraction.
25128556	7	2	dep	induced	1095:1101	arg1	observed					1171:1178	observed	1171:1178	observed global and local changes in acetylation, methylation, and phosphorylation	1171:1252	We mainly observed glucosamine induced O-GlcNAcylation/O-GalNAcylation (O-HexNAcylation); however, we also observed global and local changes in acetylation, methylation, and phosphorylation.
25128556	3	3	from	focus	552:556	arg1	subproteome					572:582	a specific subproteome	561:582	a specific subproteome	561:582	We questioned whether the differences in the effects observed in previous studies were associated with the focus on a specific subproteome or with the use of specific cell lines or tissues.
25128556	3	4	theme	specific	563:570	arg1	subproteome					572:582	a specific subproteome	561:582	a specific subproteome	561:582	We questioned whether the differences in the effects observed in previous studies were associated with the focus on a specific subproteome or with the use of specific cell lines or tissues.
25128556	1	5	theme	glucosamine	191:201	arg1	supplements					203:213	glucosamine supplements	191:213	glucosamine supplements	191:213	We investigated the molecular effects of glucosamine supplements, a popular and safe alternative to nonsteroidal anti-inflammatory drugs, for decreasing pain, inflammation, and maintaining healthy joints.
25128556	1	5	theme	glucosamine	191:201	arg1	alternative					235:245	a popular and safe alternative	216:245	a popular and safe alternative to nonsteroidal anti-inflammatory drugs	216:285	We investigated the molecular effects of glucosamine supplements, a popular and safe alternative to nonsteroidal anti-inflammatory drugs, for decreasing pain, inflammation, and maintaining healthy joints.
25128556	12	6	theme	nuclear	1783:1789	arg1	fractions					1791:1799	the cytosolic and nuclear fractions	1765:1799	the cytosolic and nuclear fractions with a higher occupancy in the cytosolic fraction	1765:1849	The occupancy of O-HexNAc on GLU2B and calnexin sites differed between the cytosolic and nuclear fractions with a higher occupancy in the cytosolic fraction.
25128556	12	7	from	occupancy	1698:1706	arg1	calnexin					1733:1740	calnexin	1733:1740	calnexin	1733:1740	The occupancy of O-HexNAc on GLU2B and calnexin sites differed between the cytosolic and nuclear fractions with a higher occupancy in the cytosolic fraction.
25128556	12	7	from	occupancy	1698:1706	arg1	GLU2B					1723:1727	GLU2B	1723:1727	GLU2B	1723:1727	The occupancy of O-HexNAc on GLU2B and calnexin sites differed between the cytosolic and nuclear fractions with a higher occupancy in the cytosolic fraction.
25128556	4	8	theme	transcription	691:703	arg1	profiling					734:742	transcription array-based glucosamine drug profiling	691:742	transcription array-based glucosamine drug profiling	691:742	To address this question, global mass spectrometry- and transcription array-based glucosamine drug profiling was performed on malignant cell lines from different stages of lymphocyte development.
25128556	11	9	theme	glucosamine	1603:1613	arg1	treatment					1615:1623	glucosamine treatment	1603:1623	glucosamine treatment	1603:1623	The O-HexNAc sites were regulated by glucosamine treatment and correlated with the up-regulation of the ER stress marker GRP78.
25128556	0	10	theme	reticulum	132:140	arg1	stress					142:147	endoplasmic reticulum stress	120:147	endoplasmic reticulum stress	120:147	Global mass spectrometry and transcriptomics array based drug profiling provides novel insight into glucosamine induced endoplasmic reticulum stress.
25128556	1	11	theme	popular	218:224	arg1	supplements					203:213	glucosamine supplements	191:213	glucosamine supplements	191:213	We investigated the molecular effects of glucosamine supplements, a popular and safe alternative to nonsteroidal anti-inflammatory drugs, for decreasing pain, inflammation, and maintaining healthy joints.
25128556	1	11	theme	popular	218:224	arg1	alternative					235:245	a popular and safe alternative	216:245	a popular and safe alternative to nonsteroidal anti-inflammatory drugs	216:285	We investigated the molecular effects of glucosamine supplements, a popular and safe alternative to nonsteroidal anti-inflammatory drugs, for decreasing pain, inflammation, and maintaining healthy joints.
25128556	6	12	theme	previous	1014:1021	arg1	studies					1023:1029	previous studies	1014:1029	previous studies in a variety of cellular models	1014:1061	Our data were largely consistent with previous studies in a variety of cellular models.
25128556	4	13	theme	global	661:666	arg1	spectrometry-					673:685	global mass spectrometry-	661:685	global mass spectrometry-	661:685	To address this question, global mass spectrometry- and transcription array-based glucosamine drug profiling was performed on malignant cell lines from different stages of lymphocyte development.
25128556	1	14	theme	safe	230:233	arg1	supplements					203:213	glucosamine supplements	191:213	glucosamine supplements	191:213	We investigated the molecular effects of glucosamine supplements, a popular and safe alternative to nonsteroidal anti-inflammatory drugs, for decreasing pain, inflammation, and maintaining healthy joints.
25128556	1	14	theme	safe	230:233	arg1	alternative					235:245	a popular and safe alternative	216:245	a popular and safe alternative to nonsteroidal anti-inflammatory drugs	216:285	We investigated the molecular effects of glucosamine supplements, a popular and safe alternative to nonsteroidal anti-inflammatory drugs, for decreasing pain, inflammation, and maintaining healthy joints.
25128556	8	15	theme	additional	1290:1299	arg1	examples					1301:1308	two additional examples	1286:1308	two additional examples of "yin-yang" between phosphorylation and O-HexNAcylation	1286:1366	For example, our data provides two additional examples of "yin-yang" between phosphorylation and O-HexNAcylation.
25128556	10	16	theme	quality	1549:1555	arg1	control					1557:1563	quality control	1549:1563	quality control	1549:1563	GLU2B and calnexin are known to be located in the endoplasmic reticulum (ER) and involved in protein folding and quality control.
25128556	3	17	theme	cell	612:615	arg1	lines					617:621	specific cell lines	603:621	specific cell lines	603:621	We questioned whether the differences in the effects observed in previous studies were associated with the focus on a specific subproteome or with the use of specific cell lines or tissues.
25128556	4	18	theme	malignant	761:769	arg1	lines					776:780	malignant cell lines	761:780	malignant cell lines from different stages of lymphocyte development	761:828	To address this question, global mass spectrometry- and transcription array-based glucosamine drug profiling was performed on malignant cell lines from different stages of lymphocyte development.
25128556	13	19	theme	cytosolic	1963:1971	arg1	fraction					1973:1980	the cytosolic fraction	1959:1980	the cytosolic fraction	1959:1980	Based on our data we propose the hypothesis that O-HexNAc either inactivates calnexin and/or targets it to the cytosolic fraction.
25128556	4	20	theme	glucosamine	717:727	arg1	profiling					734:742	transcription array-based glucosamine drug profiling	691:742	transcription array-based glucosamine drug profiling	691:742	To address this question, global mass spectrometry- and transcription array-based glucosamine drug profiling was performed on malignant cell lines from different stages of lymphocyte development.
25128556	11	21	theme	O-HexNAc	1570:1577	arg1	sites					1579:1583	The O-HexNAc sites	1566:1583	The O-HexNAc sites	1566:1583	The O-HexNAc sites were regulated by glucosamine treatment and correlated with the up-regulation of the ER stress marker GRP78.
25128556	0	22	theme	novel	81:85	arg1	insight					87:93	novel insight	81:93	novel insight into glucosamine induced endoplasmic reticulum stress	81:147	Global mass spectrometry and transcriptomics array based drug profiling provides novel insight into glucosamine induced endoplasmic reticulum stress.
25128556	5	23	theme	proteome	957:964	arg1	coverage					966:973	the best possible proteome coverage	939:973	the best possible proteome coverage	939:973	We combined global label-free MS-based protein quantitation with an open search for modifications to obtain the best possible proteome coverage.
25128556	6	24	theme	cellular	1047:1054	arg1	models					1056:1061	cellular models	1047:1061	cellular models	1047:1061	Our data were largely consistent with previous studies in a variety of cellular models.
25128556	12	25	theme	O-HexNAc	1711:1718	arg1	occupancy					1698:1706	The occupancy	1694:1706	The occupancy of O-HexNAc on GLU2B and calnexin sites	1694:1746	The occupancy of O-HexNAc on GLU2B and calnexin sites differed between the cytosolic and nuclear fractions with a higher occupancy in the cytosolic fraction.
25128556	4	26	theme	development	818:828	arg1	stages					797:802	different stages	787:802	different stages of lymphocyte development	787:828	To address this question, global mass spectrometry- and transcription array-based glucosamine drug profiling was performed on malignant cell lines from different stages of lymphocyte development.
25128556	2	27	theme	glucosamine	422:432	arg1	treatment					434:442	glucosamine treatment	422:442	glucosamine treatment	422:442	Numerous studies have reported an array of molecular effects after glucosamine treatment.
25128556	9	28	theme	novel	1392:1396	arg1	sites					1407:1411	novel O-HexNAc sites	1392:1411	novel O-HexNAc sites	1392:1411	Furthermore, we mapped novel O-HexNAc sites on GLU2B and calnexin.
25128556	7	29	dep	observed	1074:1081	arg1	induced					1095:1101	induced	1095:1101	induced O-GlcNAcylation/O-GalNAcylation (O-HexNAcylation)	1095:1151	We mainly observed glucosamine induced O-GlcNAcylation/O-GalNAcylation (O-HexNAcylation); however, we also observed global and local changes in acetylation, methylation, and phosphorylation.
25128556	2	30	theme	effects	408:414	arg1	array					389:393	an array	386:393	an array of molecular effects after glucosamine treatment	386:442	Numerous studies have reported an array of molecular effects after glucosamine treatment.
25128556	0	31	theme	Global	0:5	arg1	profiling					62:70	Global mass spectrometry and transcriptomics array based drug profiling	0:70	Global mass spectrometry and transcriptomics array based drug profiling	0:70	Global mass spectrometry and transcriptomics array based drug profiling provides novel insight into glucosamine induced endoplasmic reticulum stress.
25128556	6	32	from	studies	1023:1029	arg1	variety					1036:1042	a variety	1034:1042	a variety of cellular models	1034:1061	Our data were largely consistent with previous studies in a variety of cellular models.
25128556	6	32	from	studies	1023:1029	arg1	models					1056:1061	cellular models	1047:1061	cellular models	1047:1061	Our data were largely consistent with previous studies in a variety of cellular models.
25128556	4	33	theme	different	787:795	arg1	stages					797:802	different stages	787:802	different stages of lymphocyte development	787:828	To address this question, global mass spectrometry- and transcription array-based glucosamine drug profiling was performed on malignant cell lines from different stages of lymphocyte development.
25128556	0	34	theme	spectrometry	12:23	arg1	profiling					62:70	Global mass spectrometry and transcriptomics array based drug profiling	0:70	Global mass spectrometry and transcriptomics array based drug profiling	0:70	Global mass spectrometry and transcriptomics array based drug profiling provides novel insight into glucosamine induced endoplasmic reticulum stress.
25128556	14	35	theme	glucosamine	2039:2049	arg1	treatment					2051:2059	glucosamine treatment	2039:2059	glucosamine treatment	2039:2059	Further, we hypothesize that O-HexNAcylation induced by glucosamine treatment enhances protein trafficking.
25128556	0	36	theme	transcriptomics	29:43	arg1	profiling					62:70	Global mass spectrometry and transcriptomics array based drug profiling	0:70	Global mass spectrometry and transcriptomics array based drug profiling	0:70	Global mass spectrometry and transcriptomics array based drug profiling provides novel insight into glucosamine induced endoplasmic reticulum stress.
25128556	5	37	theme	global	843:848	arg1	quantitation					878:889	global label-free MS-based protein quantitation	843:889	global label-free MS-based protein quantitation	843:889	We combined global label-free MS-based protein quantitation with an open search for modifications to obtain the best possible proteome coverage.
25128556	1	38	theme	healthy	339:345	arg1	joints					347:352	maintaining healthy joints	327:352	maintaining healthy joints	327:352	We investigated the molecular effects of glucosamine supplements, a popular and safe alternative to nonsteroidal anti-inflammatory drugs, for decreasing pain, inflammation, and maintaining healthy joints.
25128556	7	39	from	changes	1197:1203	arg1	methylation					1221:1231	methylation	1221:1231	methylation	1221:1231	We mainly observed glucosamine induced O-GlcNAcylation/O-GalNAcylation (O-HexNAcylation); however, we also observed global and local changes in acetylation, methylation, and phosphorylation.
25128556	7	39	from	changes	1197:1203	arg1	phosphorylation					1238:1252	phosphorylation	1238:1252	phosphorylation	1238:1252	We mainly observed glucosamine induced O-GlcNAcylation/O-GalNAcylation (O-HexNAcylation); however, we also observed global and local changes in acetylation, methylation, and phosphorylation.
25128556	7	39	from	changes	1197:1203	arg1	acetylation					1208:1218	acetylation	1208:1218	acetylation	1208:1218	We mainly observed glucosamine induced O-GlcNAcylation/O-GalNAcylation (O-HexNAcylation); however, we also observed global and local changes in acetylation, methylation, and phosphorylation.
25128556	2	40	theme	Numerous	355:362	arg1	studies					364:370	Numerous studies	355:370	Numerous studies	355:370	Numerous studies have reported an array of molecular effects after glucosamine treatment.
25128556	11	41	theme	marker	1680:1685	arg1	GRP78					1687:1691	the ER stress marker GRP78	1666:1691	the ER stress marker GRP78	1666:1691	The O-HexNAc sites were regulated by glucosamine treatment and correlated with the up-regulation of the ER stress marker GRP78.
25128556	1	42	theme	nonsteroidal	250:261	arg1	drugs					281:285	nonsteroidal anti-inflammatory drugs	250:285	nonsteroidal anti-inflammatory drugs	250:285	We investigated the molecular effects of glucosamine supplements, a popular and safe alternative to nonsteroidal anti-inflammatory drugs, for decreasing pain, inflammation, and maintaining healthy joints.
25128556	7	43	theme	local	1191:1195	arg1	changes					1197:1203	global and local changes	1180:1203	global and local changes in acetylation, methylation, and phosphorylation	1180:1252	We mainly observed glucosamine induced O-GlcNAcylation/O-GalNAcylation (O-HexNAcylation); however, we also observed global and local changes in acetylation, methylation, and phosphorylation.
25128556	11	44	theme	ER	1670:1671	arg1	GRP78					1687:1691	the ER stress marker GRP78	1666:1691	the ER stress marker GRP78	1666:1691	The O-HexNAc sites were regulated by glucosamine treatment and correlated with the up-regulation of the ER stress marker GRP78.
25128556	7	45	theme	global	1180:1185	arg1	changes					1197:1203	global and local changes	1180:1203	global and local changes in acetylation, methylation, and phosphorylation	1180:1252	We mainly observed glucosamine induced O-GlcNAcylation/O-GalNAcylation (O-HexNAcylation); however, we also observed global and local changes in acetylation, methylation, and phosphorylation.
25128556	5	46	theme	possible	948:955	arg1	coverage					966:973	the best possible proteome coverage	939:973	the best possible proteome coverage	939:973	We combined global label-free MS-based protein quantitation with an open search for modifications to obtain the best possible proteome coverage.
25128556	8	47	theme	yin-yang	1314:1321	arg1	"					1322:1322	"yin-yang"	1313:1322	"yin-yang" between phosphorylation and O-HexNAcylation	1313:1366	For example, our data provides two additional examples of "yin-yang" between phosphorylation and O-HexNAcylation.
25128556	0	48	theme	based	51:55	arg1	profiling					62:70	Global mass spectrometry and transcriptomics array based drug profiling	0:70	Global mass spectrometry and transcriptomics array based drug profiling	0:70	Global mass spectrometry and transcriptomics array based drug profiling provides novel insight into glucosamine induced endoplasmic reticulum stress.
25128556	4	49	theme	mass	668:671	arg1	spectrometry-					673:685	global mass spectrometry-	661:685	global mass spectrometry-	661:685	To address this question, global mass spectrometry- and transcription array-based glucosamine drug profiling was performed on malignant cell lines from different stages of lymphocyte development.
25128556	1	50	theme	supplements	203:213	arg1	effects					180:186	the molecular effects	166:186	the molecular effects of glucosamine supplements, a popular and safe alternative to nonsteroidal anti-inflammatory drugs, for decreasing pain, inflammation, and maintaining healthy joints	166:352	We investigated the molecular effects of glucosamine supplements, a popular and safe alternative to nonsteroidal anti-inflammatory drugs, for decreasing pain, inflammation, and maintaining healthy joints.
25128556	10	51	from	reticulum	1498:1506	arg1	located					1471:1477	located	1471:1477	located	1471:1477	GLU2B and calnexin are known to be located in the endoplasmic reticulum (ER) and involved in protein folding and quality control.
25128556	6	52	with	consistent	998:1007	arg1	studies					1023:1029	previous studies	1014:1029	previous studies in a variety of cellular models	1014:1061	Our data were largely consistent with previous studies in a variety of cellular models.
25128556	8	53	theme	"	1322:1322	arg1	examples					1301:1308	two additional examples	1286:1308	two additional examples of "yin-yang" between phosphorylation and O-HexNAcylation	1286:1366	For example, our data provides two additional examples of "yin-yang" between phosphorylation and O-HexNAcylation.
25128556	3	54	theme	lines	617:621	arg1	use					596:598	the use	592:598	the use of specific cell lines or tissues	592:632	We questioned whether the differences in the effects observed in previous studies were associated with the focus on a specific subproteome or with the use of specific cell lines or tissues.
25128556	5	55	theme	open	899:902	arg1	search					904:909	an open search	896:909	an open search for modifications to obtain the best possible proteome coverage	896:973	We combined global label-free MS-based protein quantitation with an open search for modifications to obtain the best possible proteome coverage.
25128556	3	56	theme	specific	603:610	arg1	lines					617:621	specific cell lines	603:621	specific cell lines	603:621	We questioned whether the differences in the effects observed in previous studies were associated with the focus on a specific subproteome or with the use of specific cell lines or tissues.
25128556	3	57	theme	previous	510:517	arg1	studies					519:525	previous studies	510:525	previous studies	510:525	We questioned whether the differences in the effects observed in previous studies were associated with the focus on a specific subproteome or with the use of specific cell lines or tissues.
25128556	3	58	theme	tissues	626:632	arg1	use					596:598	the use	592:598	the use of specific cell lines or tissues	592:632	We questioned whether the differences in the effects observed in previous studies were associated with the focus on a specific subproteome or with the use of specific cell lines or tissues.
25128556	12	59	theme	cytosolic	1769:1777	arg1	fractions					1791:1799	the cytosolic and nuclear fractions	1765:1799	the cytosolic and nuclear fractions with a higher occupancy in the cytosolic fraction	1765:1849	The occupancy of O-HexNAc on GLU2B and calnexin sites differed between the cytosolic and nuclear fractions with a higher occupancy in the cytosolic fraction.
25128556	4	60	theme	array-based	705:715	arg1	profiling					734:742	transcription array-based glucosamine drug profiling	691:742	transcription array-based glucosamine drug profiling	691:742	To address this question, global mass spectrometry- and transcription array-based glucosamine drug profiling was performed on malignant cell lines from different stages of lymphocyte development.
25128556	1	61	theme	molecular	170:178	arg1	effects					180:186	the molecular effects	166:186	the molecular effects of glucosamine supplements, a popular and safe alternative to nonsteroidal anti-inflammatory drugs, for decreasing pain, inflammation, and maintaining healthy joints	166:352	We investigated the molecular effects of glucosamine supplements, a popular and safe alternative to nonsteroidal anti-inflammatory drugs, for decreasing pain, inflammation, and maintaining healthy joints.
25128556	6	62	theme	models	1056:1061	arg1	variety					1036:1042	a variety	1034:1042	a variety of cellular models	1034:1061	Our data were largely consistent with previous studies in a variety of cellular models.
25128556	6	62	theme	models	1056:1061	arg1	models					1056:1061	cellular models	1047:1061	cellular models	1047:1061	Our data were largely consistent with previous studies in a variety of cellular models.
25128556	4	63	theme	drug	729:732	arg1	profiling					734:742	transcription array-based glucosamine drug profiling	691:742	transcription array-based glucosamine drug profiling	691:742	To address this question, global mass spectrometry- and transcription array-based glucosamine drug profiling was performed on malignant cell lines from different stages of lymphocyte development.
25128556	3	64	located	observed	498:505	arg2	effects					490:496	the effects	486:496	the effects observed in previous studies	486:525	We questioned whether the differences in the effects observed in previous studies were associated with the focus on a specific subproteome or with the use of specific cell lines or tissues.
25128556	3	64	located	observed	498:505	arg1	studies					519:525	previous studies	510:525	previous studies	510:525	We questioned whether the differences in the effects observed in previous studies were associated with the focus on a specific subproteome or with the use of specific cell lines or tissues.
25128556	12	65	dep	GLU2B	1723:1727	arg1	sites					1742:1746	sites	1742:1746	sites	1742:1746	The occupancy of O-HexNAc on GLU2B and calnexin sites differed between the cytosolic and nuclear fractions with a higher occupancy in the cytosolic fraction.
25128556	10	66	theme	endoplasmic	1486:1496	arg1	ER					1509:1510	ER	1509:1510	ER	1509:1510	GLU2B and calnexin are known to be located in the endoplasmic reticulum (ER) and involved in protein folding and quality control.
25128556	10	66	theme	endoplasmic	1486:1496	arg1	reticulum					1498:1506	the endoplasmic reticulum	1482:1506	the endoplasmic reticulum (ER)	1482:1511	GLU2B and calnexin are known to be located in the endoplasmic reticulum (ER) and involved in protein folding and quality control.
25128556	0	67	theme	endoplasmic	120:130	arg1	reticulum					132:140	endoplasmic reticulum	120:140	endoplasmic reticulum stress	120:147	Global mass spectrometry and transcriptomics array based drug profiling provides novel insight into glucosamine induced endoplasmic reticulum stress.
25128556	4	68	from	stages	797:802	arg1	lines					776:780	malignant cell lines	761:780	malignant cell lines from different stages of lymphocyte development	761:828	To address this question, global mass spectrometry- and transcription array-based glucosamine drug profiling was performed on malignant cell lines from different stages of lymphocyte development.
25128556	4	69	theme	lymphocyte	807:816	arg1	development					818:828	lymphocyte development	807:828	lymphocyte development	807:828	To address this question, global mass spectrometry- and transcription array-based glucosamine drug profiling was performed on malignant cell lines from different stages of lymphocyte development.
25128556	5	70	theme	label-free	850:859	arg1	quantitation					878:889	global label-free MS-based protein quantitation	843:889	global label-free MS-based protein quantitation	843:889	We combined global label-free MS-based protein quantitation with an open search for modifications to obtain the best possible proteome coverage.
25128556	9	71	theme	O-HexNAc	1398:1405	arg1	sites					1407:1411	novel O-HexNAc sites	1392:1411	novel O-HexNAc sites	1392:1411	Furthermore, we mapped novel O-HexNAc sites on GLU2B and calnexin.
25128556	14	72	theme	protein	2070:2076	arg1	trafficking					2078:2088	protein trafficking	2070:2088	protein trafficking	2070:2088	Further, we hypothesize that O-HexNAcylation induced by glucosamine treatment enhances protein trafficking.
25128556	12	73	from	occupancy	1815:1823	arg1	fraction					1842:1849	the cytosolic fraction	1828:1849	the cytosolic fraction	1828:1849	The occupancy of O-HexNAc on GLU2B and calnexin sites differed between the cytosolic and nuclear fractions with a higher occupancy in the cytosolic fraction.
25128556	4	74	theme	cell	771:774	arg1	lines					776:780	malignant cell lines	761:780	malignant cell lines from different stages of lymphocyte development	761:828	To address this question, global mass spectrometry- and transcription array-based glucosamine drug profiling was performed on malignant cell lines from different stages of lymphocyte development.
25128556	2	75	theme	molecular	398:406	arg1	effects					408:414	molecular effects	398:414	molecular effects after glucosamine treatment	398:442	Numerous studies have reported an array of molecular effects after glucosamine treatment.
25128556	5	76	theme	protein	870:876	arg1	quantitation					878:889	global label-free MS-based protein quantitation	843:889	global label-free MS-based protein quantitation	843:889	We combined global label-free MS-based protein quantitation with an open search for modifications to obtain the best possible proteome coverage.
25128556	5	77	theme	MS-based	861:868	arg1	quantitation					878:889	global label-free MS-based protein quantitation	843:889	global label-free MS-based protein quantitation	843:889	We combined global label-free MS-based protein quantitation with an open search for modifications to obtain the best possible proteome coverage.
25128556	0	78	theme	array	45:49	arg1	profiling					62:70	Global mass spectrometry and transcriptomics array based drug profiling	0:70	Global mass spectrometry and transcriptomics array based drug profiling	0:70	Global mass spectrometry and transcriptomics array based drug profiling provides novel insight into glucosamine induced endoplasmic reticulum stress.
25128556	10	79	theme	protein	1529:1535	arg1	folding					1537:1543	protein folding	1529:1543	protein folding	1529:1543	GLU2B and calnexin are known to be located in the endoplasmic reticulum (ER) and involved in protein folding and quality control.
25128556	0	80	theme	drug	57:60	arg1	profiling					62:70	Global mass spectrometry and transcriptomics array based drug profiling	0:70	Global mass spectrometry and transcriptomics array based drug profiling	0:70	Global mass spectrometry and transcriptomics array based drug profiling provides novel insight into glucosamine induced endoplasmic reticulum stress.
25128556	1	81	theme	maintaining	327:337	arg1	joints					347:352	maintaining healthy joints	327:352	maintaining healthy joints	327:352	We investigated the molecular effects of glucosamine supplements, a popular and safe alternative to nonsteroidal anti-inflammatory drugs, for decreasing pain, inflammation, and maintaining healthy joints.
25128556	12	82	with	fractions	1791:1799	arg1	occupancy					1815:1823	a higher occupancy	1806:1823	a higher occupancy in the cytosolic fraction	1806:1849	The occupancy of O-HexNAc on GLU2B and calnexin sites differed between the cytosolic and nuclear fractions with a higher occupancy in the cytosolic fraction.
25128556	12	83	gly	occupancy	1698:1706	arg2	O-HexNAc					1711:1718	O-HexNAc	1711:1718	O-HexNAc	1711:1718	The occupancy of O-HexNAc on GLU2B and calnexin sites differed between the cytosolic and nuclear fractions with a higher occupancy in the cytosolic fraction.
25128556	11	84	theme	stress	1673:1678	arg1	GRP78					1687:1691	the ER stress marker GRP78	1666:1691	the ER stress marker GRP78	1666:1691	The O-HexNAc sites were regulated by glucosamine treatment and correlated with the up-regulation of the ER stress marker GRP78.
25128556	12	85	theme	cytosolic	1832:1840	arg1	fraction					1842:1849	the cytosolic fraction	1828:1849	the cytosolic fraction	1828:1849	The occupancy of O-HexNAc on GLU2B and calnexin sites differed between the cytosolic and nuclear fractions with a higher occupancy in the cytosolic fraction.
25128556	10	86	from	located	1471:1477	arg1	ER					1509:1510	ER	1509:1510	ER	1509:1510	GLU2B and calnexin are known to be located in the endoplasmic reticulum (ER) and involved in protein folding and quality control.
25128556	10	86	from	located	1471:1477	arg1	reticulum					1498:1506	the endoplasmic reticulum	1482:1506	the endoplasmic reticulum (ER)	1482:1511	GLU2B and calnexin are known to be located in the endoplasmic reticulum (ER) and involved in protein folding and quality control.
25128556	3	87	from	differences	471:481	arg1	effects					490:496	the effects	486:496	the effects observed in previous studies	486:525	We questioned whether the differences in the effects observed in previous studies were associated with the focus on a specific subproteome or with the use of specific cell lines or tissues.
25128556	0	88	theme	mass	7:10	arg1	spectrometry					12:23	mass spectrometry	7:23	mass spectrometry	7:23	Global mass spectrometry and transcriptomics array based drug profiling provides novel insight into glucosamine induced endoplasmic reticulum stress.
25128556	1	89	theme	anti-inflammatory	263:279	arg1	drugs					281:285	nonsteroidal anti-inflammatory drugs	250:285	nonsteroidal anti-inflammatory drugs	250:285	We investigated the molecular effects of glucosamine supplements, a popular and safe alternative to nonsteroidal anti-inflammatory drugs, for decreasing pain, inflammation, and maintaining healthy joints.
29229835	1	0	theme	lactate	153:159	arg1	production					161:170	lactate production	153:170	lactate production	153:170	The Warburg effect, characterized by increased glucose uptake and lactate production, is a well-known universal across cancer cells and other proliferating cells.
29229835	8	1	theme	Warburg	1441:1447	arg1	effect					1449:1454	the Warburg effect	1437:1454	the Warburg effect	1437:1454	Thus, we demonstrate that O-GlcNAcylation is a regulatory mechanism for PKM2 in cancer cells and serves as a bridge between PKM2 and metabolic reprogramming typical of the Warburg effect.
29229835	7	2	theme	blocking	1214:1221	arg1	O-GlcNAcylation					1228:1242	blocking PKM2 O-GlcNAcylation	1214:1242	blocking PKM2 O-GlcNAcylation	1214:1242	In vivo experiments showed that blocking PKM2 O-GlcNAcylation attenuated tumor growth.
29229835	2	3	with	regulator	358:366	arg1	activity					419:426	an adjustable activity	405:426	an adjustable activity subjected to numerous allosteric effectors and posttranslational modifications	405:505	PKM2, a splice isoform of the pyruvate kinase (PK) specifically expressed in these cells, serves as a major regulator of this metabolic reprogramming with an adjustable activity subjected to numerous allosteric effectors and posttranslational modifications.
29229835	7	4	theme	tumor	1255:1259	arg1	growth					1261:1266	tumor growth	1255:1266	tumor growth	1255:1266	In vivo experiments showed that blocking PKM2 O-GlcNAcylation attenuated tumor growth.
29229835	3	5	theme	spliced	690:696	arg1	exon					698:701	the alternatively spliced exon 10	672:704	the alternatively spliced exon 10 in cancer cells	672:720	Here, we have identified a posttranslational modification on PKM2, O-GlcNAcylation, which specifically targets Thr405 and Ser406, residues of the region encoded by the alternatively spliced exon 10 in cancer cells.
29229835	8	6	theme	metabolic	1402:1410	arg1	reprogramming					1412:1424	metabolic reprogramming	1402:1424	metabolic reprogramming	1402:1424	Thus, we demonstrate that O-GlcNAcylation is a regulatory mechanism for PKM2 in cancer cells and serves as a bridge between PKM2 and metabolic reprogramming typical of the Warburg effect.
29229835	8	7	theme	cancer	1349:1354	arg1	cells					1356:1360	cancer cells	1349:1360	cancer cells	1349:1360	Thus, we demonstrate that O-GlcNAcylation is a regulatory mechanism for PKM2 in cancer cells and serves as a bridge between PKM2 and metabolic reprogramming typical of the Warburg effect.
29229835	5	8	theme	PKM2	953:956	arg1	translocation					936:948	nuclear translocation	928:948	nuclear translocation of PKM2	928:956	The modification destabilized the active tetrameric PKM2, reduced PK activity, and led to nuclear translocation of PKM2.
29229835	3	9	theme	posttranslational	535:551	arg1	modification					553:564	a posttranslational modification	533:564	a posttranslational modification on PKM2, O-GlcNAcylation, which specifically targets Thr405 and Ser406, residues of the region encoded by the alternatively spliced exon 10 in cancer cells	533:720	Here, we have identified a posttranslational modification on PKM2, O-GlcNAcylation, which specifically targets Thr405 and Ser406, residues of the region encoded by the alternatively spliced exon 10 in cancer cells.
29229835	7	10	theme	In	1182:1183	arg1	experiments					1190:1200	In vivo experiments	1182:1200	In vivo experiments	1182:1200	In vivo experiments showed that blocking PKM2 O-GlcNAcylation attenuated tumor growth.
29229835	4	11	theme	tissues	829:835	arg1	types					784:788	various types	776:788	various types of human tumor cells and patient tumor tissues	776:835	We show that PKM2 O-GlcNAcylation is up-regulated in various types of human tumor cells and patient tumor tissues.
29229835	6	12	theme	glucose	1031:1037	arg1	consumption					1039:1049	an increased glucose consumption	1018:1049	an increased glucose consumption	1018:1049	We also observed that the modification was associated with an increased glucose consumption and lactate production and enhanced level of lipid and DNA synthesis, indicating that O-GlcNAcylation promotes the Warburg effect.
29229835	6	13	theme	Warburg	1166:1172	arg1	effect					1174:1179	the Warburg effect	1162:1179	the Warburg effect	1162:1179	We also observed that the modification was associated with an increased glucose consumption and lactate production and enhanced level of lipid and DNA synthesis, indicating that O-GlcNAcylation promotes the Warburg effect.
29229835	4	14	theme	tumor	823:827	arg1	tissues					829:835	patient tumor tissues	815:835	patient tumor tissues	815:835	We show that PKM2 O-GlcNAcylation is up-regulated in various types of human tumor cells and patient tumor tissues.
29229835	2	15	theme	splice	258:263	arg1	PKM2					250:253	PKM2	250:253	PKM2	250:253	PKM2, a splice isoform of the pyruvate kinase (PK) specifically expressed in these cells, serves as a major regulator of this metabolic reprogramming with an adjustable activity subjected to numerous allosteric effectors and posttranslational modifications.
29229835	2	15	theme	splice	258:263	arg1	isoform					265:271	a splice isoform	256:271	a splice isoform of the pyruvate kinase (PK) specifically expressed in these cells	256:337	PKM2, a splice isoform of the pyruvate kinase (PK) specifically expressed in these cells, serves as a major regulator of this metabolic reprogramming with an adjustable activity subjected to numerous allosteric effectors and posttranslational modifications.
29229835	2	16	theme	major	352:356	arg1	PKM2					250:253	PKM2	250:253	PKM2	250:253	PKM2, a splice isoform of the pyruvate kinase (PK) specifically expressed in these cells, serves as a major regulator of this metabolic reprogramming with an adjustable activity subjected to numerous allosteric effectors and posttranslational modifications.
29229835	2	16	theme	major	352:356	arg1	regulator					358:366	a major regulator	350:366	a major regulator of this metabolic reprogramming with an adjustable activity subjected to numerous allosteric effectors and posttranslational modifications	350:505	PKM2, a splice isoform of the pyruvate kinase (PK) specifically expressed in these cells, serves as a major regulator of this metabolic reprogramming with an adjustable activity subjected to numerous allosteric effectors and posttranslational modifications.
29229835	3	17	theme	cancer	709:714	arg1	cells					716:720	cancer cells	709:720	cancer cells	709:720	Here, we have identified a posttranslational modification on PKM2, O-GlcNAcylation, which specifically targets Thr405 and Ser406, residues of the region encoded by the alternatively spliced exon 10 in cancer cells.
29229835	4	18	gly	O-GlcNAcylation	741:755	arg1	types					784:788	various types	776:788	various types of human tumor cells and patient tumor tissues	776:835	We show that PKM2 O-GlcNAcylation is up-regulated in various types of human tumor cells and patient tumor tissues.
29229835	6	19	theme	lactate	1055:1061	arg1	production					1063:1072	lactate production	1055:1072	lactate production	1055:1072	We also observed that the modification was associated with an increased glucose consumption and lactate production and enhanced level of lipid and DNA synthesis, indicating that O-GlcNAcylation promotes the Warburg effect.
29229835	2	20	theme	adjustable	408:417	arg1	activity					419:426	an adjustable activity	405:426	an adjustable activity subjected to numerous allosteric effectors and posttranslational modifications	405:505	PKM2, a splice isoform of the pyruvate kinase (PK) specifically expressed in these cells, serves as a major regulator of this metabolic reprogramming with an adjustable activity subjected to numerous allosteric effectors and posttranslational modifications.
29229835	8	21	from	mechanism	1327:1335	arg1	cells					1356:1360	cancer cells	1349:1360	cancer cells	1349:1360	Thus, we demonstrate that O-GlcNAcylation is a regulatory mechanism for PKM2 in cancer cells and serves as a bridge between PKM2 and metabolic reprogramming typical of the Warburg effect.
29229835	1	22	theme	Warburg	91:97	arg1	effect					99:104	The Warburg effect	87:104	The Warburg effect	87:104	The Warburg effect, characterized by increased glucose uptake and lactate production, is a well-known universal across cancer cells and other proliferating cells.
29229835	1	22	theme	Warburg	91:97	arg1	universal					189:197	universal	189:197	universal	189:197	The Warburg effect, characterized by increased glucose uptake and lactate production, is a well-known universal across cancer cells and other proliferating cells.
29229835	5	23	theme	active	872:877	arg1	PKM2					890:893	the active tetrameric PKM2	868:893	the active tetrameric PKM2	868:893	The modification destabilized the active tetrameric PKM2, reduced PK activity, and led to nuclear translocation of PKM2.
29229835	0	24	theme	active	33:38	arg1	PKM2					51:54	the active tetrameric PKM2	29:54	the active tetrameric PKM2 to promote the Warburg effect	29:84	O-GlcNAcylation destabilizes the active tetrameric PKM2 to promote the Warburg effect.
29229835	2	25	theme	kinase	289:294	arg1	PKM2					250:253	PKM2	250:253	PKM2	250:253	PKM2, a splice isoform of the pyruvate kinase (PK) specifically expressed in these cells, serves as a major regulator of this metabolic reprogramming with an adjustable activity subjected to numerous allosteric effectors and posttranslational modifications.
29229835	2	25	theme	kinase	289:294	arg1	isoform					265:271	a splice isoform	256:271	a splice isoform of the pyruvate kinase (PK) specifically expressed in these cells	256:337	PKM2, a splice isoform of the pyruvate kinase (PK) specifically expressed in these cells, serves as a major regulator of this metabolic reprogramming with an adjustable activity subjected to numerous allosteric effectors and posttranslational modifications.
29229835	2	26	theme	reprogramming	386:398	arg1	PKM2					250:253	PKM2	250:253	PKM2	250:253	PKM2, a splice isoform of the pyruvate kinase (PK) specifically expressed in these cells, serves as a major regulator of this metabolic reprogramming with an adjustable activity subjected to numerous allosteric effectors and posttranslational modifications.
29229835	2	26	theme	reprogramming	386:398	arg1	regulator					358:366	a major regulator	350:366	a major regulator of this metabolic reprogramming with an adjustable activity subjected to numerous allosteric effectors and posttranslational modifications	350:505	PKM2, a splice isoform of the pyruvate kinase (PK) specifically expressed in these cells, serves as a major regulator of this metabolic reprogramming with an adjustable activity subjected to numerous allosteric effectors and posttranslational modifications.
29229835	8	27	theme	effect	1449:1454	arg1	typical					1426:1432	typical	1426:1432	typical	1426:1432	Thus, we demonstrate that O-GlcNAcylation is a regulatory mechanism for PKM2 in cancer cells and serves as a bridge between PKM2 and metabolic reprogramming typical of the Warburg effect.
29229835	2	28	theme	pyruvate	280:287	arg1	kinase					289:294	the pyruvate kinase	276:294	the pyruvate kinase (PK) specifically expressed in these cells	276:337	PKM2, a splice isoform of the pyruvate kinase (PK) specifically expressed in these cells, serves as a major regulator of this metabolic reprogramming with an adjustable activity subjected to numerous allosteric effectors and posttranslational modifications.
29229835	2	28	theme	pyruvate	280:287	arg1	PK					297:298	PK	297:298	PK	297:298	PKM2, a splice isoform of the pyruvate kinase (PK) specifically expressed in these cells, serves as a major regulator of this metabolic reprogramming with an adjustable activity subjected to numerous allosteric effectors and posttranslational modifications.
29229835	2	29	theme	metabolic	376:384	arg1	reprogramming					386:398	this metabolic reprogramming	371:398	this metabolic reprogramming	371:398	PKM2, a splice isoform of the pyruvate kinase (PK) specifically expressed in these cells, serves as a major regulator of this metabolic reprogramming with an adjustable activity subjected to numerous allosteric effectors and posttranslational modifications.
29229835	2	30	theme	allosteric	450:459	arg1	effectors					461:469	numerous allosteric effectors	441:469	numerous allosteric effectors	441:469	PKM2, a splice isoform of the pyruvate kinase (PK) specifically expressed in these cells, serves as a major regulator of this metabolic reprogramming with an adjustable activity subjected to numerous allosteric effectors and posttranslational modifications.
29229835	6	31	theme	lipid	1096:1100	arg1	level					1087:1091	level	1087:1091	level of lipid and DNA synthesis	1087:1118	We also observed that the modification was associated with an increased glucose consumption and lactate production and enhanced level of lipid and DNA synthesis, indicating that O-GlcNAcylation promotes the Warburg effect.
29229835	6	32	theme	increased	1021:1029	arg1	consumption					1039:1049	an increased glucose consumption	1018:1049	an increased glucose consumption	1018:1049	We also observed that the modification was associated with an increased glucose consumption and lactate production and enhanced level of lipid and DNA synthesis, indicating that O-GlcNAcylation promotes the Warburg effect.
29229835	4	33	theme	cells	805:809	arg1	types					784:788	various types	776:788	various types of human tumor cells and patient tumor tissues	776:835	We show that PKM2 O-GlcNAcylation is up-regulated in various types of human tumor cells and patient tumor tissues.
29229835	1	34	theme	cancer	206:211	arg1	cells					213:217	cancer cells	206:217	cancer cells	206:217	The Warburg effect, characterized by increased glucose uptake and lactate production, is a well-known universal across cancer cells and other proliferating cells.
29229835	2	35	theme	numerous	441:448	arg1	effectors					461:469	numerous allosteric effectors	441:469	numerous allosteric effectors	441:469	PKM2, a splice isoform of the pyruvate kinase (PK) specifically expressed in these cells, serves as a major regulator of this metabolic reprogramming with an adjustable activity subjected to numerous allosteric effectors and posttranslational modifications.
29229835	0	36	theme	tetrameric	40:49	arg1	PKM2					51:54	the active tetrameric PKM2	29:54	the active tetrameric PKM2 to promote the Warburg effect	29:84	O-GlcNAcylation destabilizes the active tetrameric PKM2 to promote the Warburg effect.
29229835	4	37	theme	tumor	799:803	arg1	cells					805:809	human tumor cells	793:809	human tumor cells	793:809	We show that PKM2 O-GlcNAcylation is up-regulated in various types of human tumor cells and patient tumor tissues.
29229835	3	38	from	exon	698:701	arg1	cells					716:720	cancer cells	709:720	cancer cells	709:720	Here, we have identified a posttranslational modification on PKM2, O-GlcNAcylation, which specifically targets Thr405 and Ser406, residues of the region encoded by the alternatively spliced exon 10 in cancer cells.
29229835	7	39	dep	In	1182:1183	arg1	vivo					1185:1188	vivo	1185:1188	vivo	1185:1188	In vivo experiments showed that blocking PKM2 O-GlcNAcylation attenuated tumor growth.
29229835	4	40	theme	patient	815:821	arg1	tissues					829:835	patient tumor tissues	815:835	patient tumor tissues	815:835	We show that PKM2 O-GlcNAcylation is up-regulated in various types of human tumor cells and patient tumor tissues.
29229835	6	41	theme	DNA	1106:1108	arg1	synthesis					1110:1118	DNA synthesis	1106:1118	DNA synthesis	1106:1118	We also observed that the modification was associated with an increased glucose consumption and lactate production and enhanced level of lipid and DNA synthesis, indicating that O-GlcNAcylation promotes the Warburg effect.
29229835	5	42	theme	PK	904:905	arg1	activity					907:914	PK activity	904:914	PK activity	904:914	The modification destabilized the active tetrameric PKM2, reduced PK activity, and led to nuclear translocation of PKM2.
29229835	5	43	theme	nuclear	928:934	arg1	translocation					936:948	nuclear translocation	928:948	nuclear translocation of PKM2	928:956	The modification destabilized the active tetrameric PKM2, reduced PK activity, and led to nuclear translocation of PKM2.
29229835	7	44	theme	PKM2	1223:1226	arg1	O-GlcNAcylation					1228:1242	blocking PKM2 O-GlcNAcylation	1214:1242	blocking PKM2 O-GlcNAcylation	1214:1242	In vivo experiments showed that blocking PKM2 O-GlcNAcylation attenuated tumor growth.
29229835	6	45	theme	synthesis	1110:1118	arg1	level					1087:1091	level	1087:1091	level of lipid and DNA synthesis	1087:1118	We also observed that the modification was associated with an increased glucose consumption and lactate production and enhanced level of lipid and DNA synthesis, indicating that O-GlcNAcylation promotes the Warburg effect.
29229835	3	46	from	modification	553:564	arg1	O-GlcNAcylation					575:589	O-GlcNAcylation	575:589	O-GlcNAcylation	575:589	Here, we have identified a posttranslational modification on PKM2, O-GlcNAcylation, which specifically targets Thr405 and Ser406, residues of the region encoded by the alternatively spliced exon 10 in cancer cells.
29229835	3	46	from	modification	553:564	arg1	PKM2					569:572	PKM2	569:572	PKM2	569:572	Here, we have identified a posttranslational modification on PKM2, O-GlcNAcylation, which specifically targets Thr405 and Ser406, residues of the region encoded by the alternatively spliced exon 10 in cancer cells.
29229835	8	47	theme	typical	1426:1432	arg1	PKM2					1393:1396	PKM2	1393:1396	PKM2	1393:1396	Thus, we demonstrate that O-GlcNAcylation is a regulatory mechanism for PKM2 in cancer cells and serves as a bridge between PKM2 and metabolic reprogramming typical of the Warburg effect.
29229835	1	48	theme	increased	124:132	arg1	uptake					142:147	increased glucose uptake	124:147	increased glucose uptake	124:147	The Warburg effect, characterized by increased glucose uptake and lactate production, is a well-known universal across cancer cells and other proliferating cells.
29229835	4	49	theme	PKM2	736:739	arg1	O-GlcNAcylation					741:755	PKM2 O-GlcNAcylation	736:755	PKM2 O-GlcNAcylation	736:755	We show that PKM2 O-GlcNAcylation is up-regulated in various types of human tumor cells and patient tumor tissues.
29229835	3	50	theme	region	654:659	arg1	Thr405					619:624	Thr405	619:624	Thr405	619:624	Here, we have identified a posttranslational modification on PKM2, O-GlcNAcylation, which specifically targets Thr405 and Ser406, residues of the region encoded by the alternatively spliced exon 10 in cancer cells.
29229835	3	50	theme	region	654:659	arg1	residues					638:645	residues	638:645	residues of the region encoded by the alternatively spliced exon 10 in cancer cells	638:720	Here, we have identified a posttranslational modification on PKM2, O-GlcNAcylation, which specifically targets Thr405 and Ser406, residues of the region encoded by the alternatively spliced exon 10 in cancer cells.
29229835	3	50	theme	region	654:659	arg1	region					654:659	the region	650:659	the region encoded by the alternatively spliced exon 10 in cancer cells	650:720	Here, we have identified a posttranslational modification on PKM2, O-GlcNAcylation, which specifically targets Thr405 and Ser406, residues of the region encoded by the alternatively spliced exon 10 in cancer cells.
29229835	4	51	theme	various	776:782	arg1	types					784:788	various types	776:788	various types of human tumor cells and patient tumor tissues	776:835	We show that PKM2 O-GlcNAcylation is up-regulated in various types of human tumor cells and patient tumor tissues.
29229835	1	52	theme	glucose	134:140	arg1	uptake					142:147	increased glucose uptake	124:147	increased glucose uptake	124:147	The Warburg effect, characterized by increased glucose uptake and lactate production, is a well-known universal across cancer cells and other proliferating cells.
29229835	1	53	theme	other	223:227	arg1	cells					243:247	other proliferating cells	223:247	other proliferating cells	223:247	The Warburg effect, characterized by increased glucose uptake and lactate production, is a well-known universal across cancer cells and other proliferating cells.
29229835	0	54	theme	Warburg	71:77	arg1	effect					79:84	the Warburg effect	67:84	the Warburg effect	67:84	O-GlcNAcylation destabilizes the active tetrameric PKM2 to promote the Warburg effect.
29229835	4	55	theme	human	793:797	arg1	cells					805:809	human tumor cells	793:809	human tumor cells	793:809	We show that PKM2 O-GlcNAcylation is up-regulated in various types of human tumor cells and patient tumor tissues.
29229835	5	56	theme	tetrameric	879:888	arg1	PKM2					890:893	the active tetrameric PKM2	868:893	the active tetrameric PKM2	868:893	The modification destabilized the active tetrameric PKM2, reduced PK activity, and led to nuclear translocation of PKM2.
29229835	1	57	theme	proliferating	229:241	arg1	cells					243:247	other proliferating cells	223:247	other proliferating cells	223:247	The Warburg effect, characterized by increased glucose uptake and lactate production, is a well-known universal across cancer cells and other proliferating cells.
29229835	2	58	theme	posttranslational	475:491	arg1	modifications					493:505	posttranslational modifications	475:505	posttranslational modifications	475:505	PKM2, a splice isoform of the pyruvate kinase (PK) specifically expressed in these cells, serves as a major regulator of this metabolic reprogramming with an adjustable activity subjected to numerous allosteric effectors and posttranslational modifications.
29229835	8	59	theme	regulatory	1316:1325	arg1	mechanism					1327:1335	a regulatory mechanism	1314:1335	a regulatory mechanism for PKM2 in cancer cells	1314:1360	Thus, we demonstrate that O-GlcNAcylation is a regulatory mechanism for PKM2 in cancer cells and serves as a bridge between PKM2 and metabolic reprogramming typical of the Warburg effect.
29229835	8	59	theme	regulatory	1316:1325	arg1	O-GlcNAcylation					1295:1309	O-GlcNAcylation	1295:1309	O-GlcNAcylation	1295:1309	Thus, we demonstrate that O-GlcNAcylation is a regulatory mechanism for PKM2 in cancer cells and serves as a bridge between PKM2 and metabolic reprogramming typical of the Warburg effect.
18988733	4	0	theme	p65	721:723	arg1	Thr-352					701:707	Thr-352	701:707	Thr-352 of NFkappaB p65	701:723	Also, we demonstrate that both Thr-322 and Thr-352 of NFkappaB p65 can be modified with O-GlcNAc, but modification on Thr-352, not Thr-322, is important for transcriptional activation.
18988733	4	0	theme	p65	721:723	arg1	Thr-322					689:695	Thr-322	689:695	Thr-322	689:695	Also, we demonstrate that both Thr-322 and Thr-352 of NFkappaB p65 can be modified with O-GlcNAc, but modification on Thr-352, not Thr-322, is important for transcriptional activation.
18988733	4	1	theme	NFkappaB	712:719	arg1	p65					721:723	NFkappaB p65	712:723	NFkappaB p65	712:723	Also, we demonstrate that both Thr-322 and Thr-352 of NFkappaB p65 can be modified with O-GlcNAc, but modification on Thr-352, not Thr-322, is important for transcriptional activation.
18988733	2	2	theme	subunit	320:326	arg1	modification					287:298	posttranslational modification	269:298	posttranslational modification of the NFkappaB p65 subunit by O-linked N-acetylglucosamine (O-GlcNAc)	269:369	Additionally, posttranslational modification of the NFkappaB p65 subunit by O-linked N-acetylglucosamine (O-GlcNAc) has been reported, but the modification site of O-GlcNAc on NFkappaB p65 and its exact function have not been elucidated.
18988733	5	3	theme	hyperglycemic	966:978	arg1	conditions					980:989	hyperglycemic conditions	966:989	hyperglycemic conditions	966:989	Our findings suggest that site-specific O-GlcNAcylation may be a reason why NFkappaB activity increases continuously under hyperglycemic conditions.
18988733	2	4	theme	p65	316:318	arg1	subunit					320:326	the NFkappaB p65 subunit	303:326	the NFkappaB p65 subunit	303:326	Additionally, posttranslational modification of the NFkappaB p65 subunit by O-linked N-acetylglucosamine (O-GlcNAc) has been reported, but the modification site of O-GlcNAc on NFkappaB p65 and its exact function have not been elucidated.
18988733	5	5	theme	site-specific	869:881	arg1	O-GlcNAcylation					883:897	site-specific O-GlcNAcylation	869:897	site-specific O-GlcNAcylation	869:897	Our findings suggest that site-specific O-GlcNAcylation may be a reason why NFkappaB activity increases continuously under hyperglycemic conditions.
18988733	5	5	theme	site-specific	869:881	arg1	reason					908:913	a reason	906:913	a reason why NFkappaB activity increases continuously under hyperglycemic conditions	906:989	Our findings suggest that site-specific O-GlcNAcylation may be a reason why NFkappaB activity increases continuously under hyperglycemic conditions.
18988733	2	6	theme	NFkappaB	307:314	arg1	subunit					320:326	the NFkappaB p65 subunit	303:326	the NFkappaB p65 subunit	303:326	Additionally, posttranslational modification of the NFkappaB p65 subunit by O-linked N-acetylglucosamine (O-GlcNAc) has been reported, but the modification site of O-GlcNAc on NFkappaB p65 and its exact function have not been elucidated.
18988733	1	7	theme	important	189:197	arg1	roles					199:203	important roles	189:203	important roles	189:203	The transcription factor NFkappaB is activated by phosphorylation and acetylation and plays important roles in inflammatory and immune responses in the cell.
18988733	4	8	from	modification	760:771	arg1	Thr-352					776:782	Thr-352	776:782	Thr-352	776:782	Also, we demonstrate that both Thr-322 and Thr-352 of NFkappaB p65 can be modified with O-GlcNAc, but modification on Thr-352, not Thr-322, is important for transcriptional activation.
18988733	4	8	from	modification	760:771	arg1	Thr-322					789:795	Thr-322	789:795	Thr-322	789:795	Also, we demonstrate that both Thr-322 and Thr-352 of NFkappaB p65 can be modified with O-GlcNAc, but modification on Thr-352, not Thr-322, is important for transcriptional activation.
18988733	3	9	theme	NFkappaB	539:546	arg1	p65					548:550	NFkappaB p65	539:550	NFkappaB p65	539:550	In this work, we show that O-GlcNAcylation of NFkappaB p65 decreases binding to IkappaB alpha and increases transcriptional activity under hyperglycemic conditions.
18988733	3	10	theme	IkappaB	573:579	arg1	alpha					581:585	IkappaB alpha	573:585	IkappaB alpha	573:585	In this work, we show that O-GlcNAcylation of NFkappaB p65 decreases binding to IkappaB alpha and increases transcriptional activity under hyperglycemic conditions.
18988733	0	11	theme	NFkappaB	0:7	arg1	activation					9:18	NFkappaB activation	0:18	NFkappaB activation	0:18	NFkappaB activation is associated with its O-GlcNAcylation state under hyperglycemic conditions.
18988733	1	12	theme	transcription	101:113	arg1	NFkappaB					122:129	The transcription factor NFkappaB	97:129	The transcription factor NFkappaB	97:129	The transcription factor NFkappaB is activated by phosphorylation and acetylation and plays important roles in inflammatory and immune responses in the cell.
18988733	2	13	theme	modification	398:409	arg1	O-GlcNAc					419:426	O-GlcNAc	419:426	O-GlcNAc	419:426	Additionally, posttranslational modification of the NFkappaB p65 subunit by O-linked N-acetylglucosamine (O-GlcNAc) has been reported, but the modification site of O-GlcNAc on NFkappaB p65 and its exact function have not been elucidated.
18988733	2	13	theme	modification	398:409	arg1	site					411:414	the modification site	394:414	the modification site of O-GlcNAc on NFkappaB p65 and its exact function	394:465	Additionally, posttranslational modification of the NFkappaB p65 subunit by O-linked N-acetylglucosamine (O-GlcNAc) has been reported, but the modification site of O-GlcNAc on NFkappaB p65 and its exact function have not been elucidated.
18988733	2	14	theme	exact	452:456	arg1	function					458:465	its exact function	448:465	its exact function	448:465	Additionally, posttranslational modification of the NFkappaB p65 subunit by O-linked N-acetylglucosamine (O-GlcNAc) has been reported, but the modification site of O-GlcNAc on NFkappaB p65 and its exact function have not been elucidated.
18988733	2	15	theme	O-linked	331:338	arg1	O-GlcNAc					361:368	O-GlcNAc	361:368	O-GlcNAc	361:368	Additionally, posttranslational modification of the NFkappaB p65 subunit by O-linked N-acetylglucosamine (O-GlcNAc) has been reported, but the modification site of O-GlcNAc on NFkappaB p65 and its exact function have not been elucidated.
18988733	2	15	theme	O-linked	331:338	arg1	N-acetylglucosamine					340:358	O-linked N-acetylglucosamine	331:358	O-linked N-acetylglucosamine (O-GlcNAc)	331:369	Additionally, posttranslational modification of the NFkappaB p65 subunit by O-linked N-acetylglucosamine (O-GlcNAc) has been reported, but the modification site of O-GlcNAc on NFkappaB p65 and its exact function have not been elucidated.
18988733	4	16	theme	transcriptional	815:829	arg1	activation					831:840	transcriptional activation	815:840	transcriptional activation	815:840	Also, we demonstrate that both Thr-322 and Thr-352 of NFkappaB p65 can be modified with O-GlcNAc, but modification on Thr-352, not Thr-322, is important for transcriptional activation.
18988733	5	17	theme	NFkappaB	919:926	arg1	activity					928:935	NFkappaB activity	919:935	NFkappaB activity	919:935	Our findings suggest that site-specific O-GlcNAcylation may be a reason why NFkappaB activity increases continuously under hyperglycemic conditions.
18988733	1	18	theme	immune	225:230	arg1	responses					232:240	inflammatory and immune responses	208:240	inflammatory and immune responses in the cell	208:252	The transcription factor NFkappaB is activated by phosphorylation and acetylation and plays important roles in inflammatory and immune responses in the cell.
18988733	3	19	theme	transcriptional	601:615	arg1	activity					617:624	transcriptional activity	601:624	transcriptional activity under hyperglycemic conditions	601:655	In this work, we show that O-GlcNAcylation of NFkappaB p65 decreases binding to IkappaB alpha and increases transcriptional activity under hyperglycemic conditions.
18988733	1	20	theme	inflammatory	208:219	arg1	responses					232:240	inflammatory and immune responses	208:240	inflammatory and immune responses in the cell	208:252	The transcription factor NFkappaB is activated by phosphorylation and acetylation and plays important roles in inflammatory and immune responses in the cell.
18988733	2	21	theme	NFkappaB	431:438	arg1	p65					440:442	NFkappaB p65	431:442	NFkappaB p65	431:442	Additionally, posttranslational modification of the NFkappaB p65 subunit by O-linked N-acetylglucosamine (O-GlcNAc) has been reported, but the modification site of O-GlcNAc on NFkappaB p65 and its exact function have not been elucidated.
18988733	2	22	theme	O-GlcNAc	419:426	arg1	O-GlcNAc					419:426	O-GlcNAc	419:426	O-GlcNAc	419:426	Additionally, posttranslational modification of the NFkappaB p65 subunit by O-linked N-acetylglucosamine (O-GlcNAc) has been reported, but the modification site of O-GlcNAc on NFkappaB p65 and its exact function have not been elucidated.
18988733	2	22	theme	O-GlcNAc	419:426	arg1	site					411:414	the modification site	394:414	the modification site of O-GlcNAc on NFkappaB p65 and its exact function	394:465	Additionally, posttranslational modification of the NFkappaB p65 subunit by O-linked N-acetylglucosamine (O-GlcNAc) has been reported, but the modification site of O-GlcNAc on NFkappaB p65 and its exact function have not been elucidated.
18988733	2	23	link	O-linked	331:338	arg1	O-GlcNAc					361:368	O-GlcNAc	361:368	O-GlcNAc	361:368	Additionally, posttranslational modification of the NFkappaB p65 subunit by O-linked N-acetylglucosamine (O-GlcNAc) has been reported, but the modification site of O-GlcNAc on NFkappaB p65 and its exact function have not been elucidated.
18988733	2	23	link	O-linked	331:338	arg1	N-acetylglucosamine					340:358	O-linked N-acetylglucosamine	331:358	O-linked N-acetylglucosamine (O-GlcNAc)	331:369	Additionally, posttranslational modification of the NFkappaB p65 subunit by O-linked N-acetylglucosamine (O-GlcNAc) has been reported, but the modification site of O-GlcNAc on NFkappaB p65 and its exact function have not been elucidated.
18988733	2	24	from	site	411:414	arg1	function					458:465	its exact function	448:465	its exact function	448:465	Additionally, posttranslational modification of the NFkappaB p65 subunit by O-linked N-acetylglucosamine (O-GlcNAc) has been reported, but the modification site of O-GlcNAc on NFkappaB p65 and its exact function have not been elucidated.
18988733	2	24	from	site	411:414	arg1	p65					440:442	NFkappaB p65	431:442	NFkappaB p65	431:442	Additionally, posttranslational modification of the NFkappaB p65 subunit by O-linked N-acetylglucosamine (O-GlcNAc) has been reported, but the modification site of O-GlcNAc on NFkappaB p65 and its exact function have not been elucidated.
18988733	0	25	theme	O-GlcNAcylation	43:57	arg1	state					59:63	its O-GlcNAcylation state	39:63	its O-GlcNAcylation state	39:63	NFkappaB activation is associated with its O-GlcNAcylation state under hyperglycemic conditions.
18988733	1	26	theme	factor	115:120	arg1	NFkappaB					122:129	The transcription factor NFkappaB	97:129	The transcription factor NFkappaB	97:129	The transcription factor NFkappaB is activated by phosphorylation and acetylation and plays important roles in inflammatory and immune responses in the cell.
18988733	1	27	from	responses	232:240	arg1	cell					249:252	the cell	245:252	the cell	245:252	The transcription factor NFkappaB is activated by phosphorylation and acetylation and plays important roles in inflammatory and immune responses in the cell.
18988733	0	28	theme	hyperglycemic	71:83	arg1	conditions					85:94	hyperglycemic conditions	71:94	hyperglycemic conditions	71:94	NFkappaB activation is associated with its O-GlcNAcylation state under hyperglycemic conditions.
18988733	2	29	theme	posttranslational	269:285	arg1	modification					287:298	posttranslational modification	269:298	posttranslational modification of the NFkappaB p65 subunit by O-linked N-acetylglucosamine (O-GlcNAc)	269:369	Additionally, posttranslational modification of the NFkappaB p65 subunit by O-linked N-acetylglucosamine (O-GlcNAc) has been reported, but the modification site of O-GlcNAc on NFkappaB p65 and its exact function have not been elucidated.
18988733	3	30	theme	p65	548:550	arg1	O-GlcNAcylation					520:534	O-GlcNAcylation	520:534	O-GlcNAcylation of NFkappaB p65	520:550	In this work, we show that O-GlcNAcylation of NFkappaB p65 decreases binding to IkappaB alpha and increases transcriptional activity under hyperglycemic conditions.
18988733	3	31	theme	hyperglycemic	632:644	arg1	conditions					646:655	hyperglycemic conditions	632:655	hyperglycemic conditions	632:655	In this work, we show that O-GlcNAcylation of NFkappaB p65 decreases binding to IkappaB alpha and increases transcriptional activity under hyperglycemic conditions.
18988733	4	32	mod	modified	732:739	arg3	O-GlcNAc					746:753	O-GlcNAc	746:753	O-GlcNAc	746:753	Also, we demonstrate that both Thr-322 and Thr-352 of NFkappaB p65 can be modified with O-GlcNAc, but modification on Thr-352, not Thr-322, is important for transcriptional activation.
18988733	4	32	mod	modified	732:739	arg1	Thr-352					701:707	Thr-352	701:707	Thr-352 of NFkappaB p65	701:723	Also, we demonstrate that both Thr-322 and Thr-352 of NFkappaB p65 can be modified with O-GlcNAc, but modification on Thr-352, not Thr-322, is important for transcriptional activation.
18988733	4	32	mod	modified	732:739	arg1	Thr-322					689:695	Thr-322	689:695	Thr-322	689:695	Also, we demonstrate that both Thr-322 and Thr-352 of NFkappaB p65 can be modified with O-GlcNAc, but modification on Thr-352, not Thr-322, is important for transcriptional activation.
26960196	0	0	theme	Dynamic	91:97	arg1	Microarray					107:116	a Dynamic Peptide Microarray	89:116	a Dynamic Peptide Microarray	89:116	Activity Based High-Throughput Screening for Novel O-GlcNAc Transferase Substrates Using a Dynamic Peptide Microarray.
26960196	5	1	theme	microarray	788:797	arg1	approach					799:806	the peptide microarray approach	776:806	the peptide microarray approach	776:806	Here we demonstrated the utility of the peptide microarray approach to discover novel OGT substrates and study its specificity.
26960196	1	2	theme	post-translational	171:188	arg1	O-GlcNAcylation					119:133	O-GlcNAcylation	119:133	O-GlcNAcylation	119:133	O-GlcNAcylation is a reversible and dynamic protein post-translational modification in mammalian cells.
26960196	1	2	theme	post-translational	171:188	arg1	modification					190:201	a reversible and dynamic protein post-translational modification	138:201	a reversible and dynamic protein post-translational modification in mammalian cells	138:220	O-GlcNAcylation is a reversible and dynamic protein post-translational modification in mammalian cells.
26960196	9	3	theme	OGT	1381:1383	arg1	specificity					1385:1395	OGT specificity	1381:1395	OGT specificity	1381:1395	This approach will prove useful for both discovery of novel OGT substrates and studying OGT specificity.
26960196	5	4	theme	approach	799:806	arg1	utility					765:771	the utility	761:771	the utility of the peptide microarray approach to discover novel OGT substrates and study its specificity	761:865	Here we demonstrated the utility of the peptide microarray approach to discover novel OGT substrates and study its specificity.
26960196	7	5	from	site	1122:1125	arg1	RBL-2					1130:1134	RBL-2	1130:1134	RBL-2	1130:1134	Using peptide Ala scanning, we found Ser 420 is one possible O-GlcNAc site in RBL-2.
26960196	7	6	theme	possible	1104:1111	arg1	site					1122:1125	one possible O-GlcNAc site	1100:1125	one possible O-GlcNAc site in RBL-2	1100:1134	Using peptide Ala scanning, we found Ser 420 is one possible O-GlcNAc site in RBL-2.
26960196	1	7	from	modification	190:201	arg1	cells					216:220	mammalian cells	206:220	mammalian cells	206:220	O-GlcNAcylation is a reversible and dynamic protein post-translational modification in mammalian cells.
26960196	4	8	theme	OGT	631:633	arg1	substrates					635:644	OGT substrates	631:644	OGT substrates	631:644	Recently, numerous approaches have been developed to identify OGT substrates and study their function, but there is still a strong demand for highly efficient techniques.
26960196	0	9	theme	Peptide	99:105	arg1	Microarray					107:116	a Dynamic Peptide Microarray	89:116	a Dynamic Peptide Microarray	89:116	Activity Based High-Throughput Screening for Novel O-GlcNAc Transferase Substrates Using a Dynamic Peptide Microarray.
26960196	6	10	theme	key	913:915	arg1	RBL-2					895:899	the protein RBL-2	883:899	the protein RBL-2	883:899	Interestingly, the protein RBL-2, which is a key regulator of entry into cell division and may function as a tumor suppressor, was identified as a substrate for three isoforms of OGT.
26960196	6	10	theme	key	913:915	arg1	regulator					917:925	a key regulator	911:925	a key regulator of entry into cell division	911:953	Interestingly, the protein RBL-2, which is a key regulator of entry into cell division and may function as a tumor suppressor, was identified as a substrate for three isoforms of OGT.
26960196	4	11	theme	efficient	718:726	arg1	techniques					728:737	highly efficient techniques	711:737	highly efficient techniques	711:737	Recently, numerous approaches have been developed to identify OGT substrates and study their function, but there is still a strong demand for highly efficient techniques.
26960196	8	12	theme	development	1251:1261	arg1	possibility					1220:1230	the possibility	1216:1230	the possibility of mechanism-based development for selective OGT inhibitors	1216:1290	Moreover, substitution of Ser 420, on its own, inhibited OGT activity, raising the possibility of mechanism-based development for selective OGT inhibitors.
26960196	3	13	theme	cellular	359:366	arg1	events					368:373	many vital cellular events	348:373	many vital cellular events including transcription, cell cycle regulation, stress response and protein degradation	348:461	O-GlcNAcylation plays important role in many vital cellular events including transcription, cell cycle regulation, stress response and protein degradation, and altered O-GlcNAcylation has long been implicated in cancer, diabetes and neurodegenerative diseases.
26960196	3	13	theme	cellular	359:366	arg1	regulation					411:420	cell cycle regulation	400:420	cell cycle regulation	400:420	O-GlcNAcylation plays important role in many vital cellular events including transcription, cell cycle regulation, stress response and protein degradation, and altered O-GlcNAcylation has long been implicated in cancer, diabetes and neurodegenerative diseases.
26960196	3	13	theme	cellular	359:366	arg1	response					430:437	stress response	423:437	stress response	423:437	O-GlcNAcylation plays important role in many vital cellular events including transcription, cell cycle regulation, stress response and protein degradation, and altered O-GlcNAcylation has long been implicated in cancer, diabetes and neurodegenerative diseases.
26960196	3	13	theme	cellular	359:366	arg1	degradation					451:461	protein degradation	443:461	protein degradation	443:461	O-GlcNAcylation plays important role in many vital cellular events including transcription, cell cycle regulation, stress response and protein degradation, and altered O-GlcNAcylation has long been implicated in cancer, diabetes and neurodegenerative diseases.
26960196	3	13	theme	cellular	359:366	arg1	transcription					385:397	transcription	385:397	transcription	385:397	O-GlcNAcylation plays important role in many vital cellular events including transcription, cell cycle regulation, stress response and protein degradation, and altered O-GlcNAcylation has long been implicated in cancer, diabetes and neurodegenerative diseases.
26960196	8	14	theme	mechanism-based	1235:1249	arg1	development					1251:1261	mechanism-based development	1235:1261	mechanism-based development	1235:1261	Moreover, substitution of Ser 420, on its own, inhibited OGT activity, raising the possibility of mechanism-based development for selective OGT inhibitors.
26960196	4	15	theme	strong	693:698	arg1	demand					700:705	a strong demand	691:705	a strong demand for highly efficient techniques	691:737	Recently, numerous approaches have been developed to identify OGT substrates and study their function, but there is still a strong demand for highly efficient techniques.
26960196	0	16	theme	O-GlcNAc	51:58	arg1	Substrates					72:81	Novel O-GlcNAc Transferase Substrates	45:81	Novel O-GlcNAc Transferase Substrates Using a Dynamic Peptide Microarray	45:116	Activity Based High-Throughput Screening for Novel O-GlcNAc Transferase Substrates Using a Dynamic Peptide Microarray.
26960196	1	17	theme	mammalian	206:214	arg1	cells					216:220	mammalian cells	206:220	mammalian cells	206:220	O-GlcNAcylation is a reversible and dynamic protein post-translational modification in mammalian cells.
26960196	3	18	theme	cycle	405:409	arg1	regulation					411:420	cell cycle regulation	400:420	cell cycle regulation	400:420	O-GlcNAcylation plays important role in many vital cellular events including transcription, cell cycle regulation, stress response and protein degradation, and altered O-GlcNAcylation has long been implicated in cancer, diabetes and neurodegenerative diseases.
26960196	3	19	theme	protein	443:449	arg1	degradation					451:461	protein degradation	443:461	protein degradation	443:461	O-GlcNAcylation plays important role in many vital cellular events including transcription, cell cycle regulation, stress response and protein degradation, and altered O-GlcNAcylation has long been implicated in cancer, diabetes and neurodegenerative diseases.
26960196	6	20	theme	tumor	977:981	arg1	suppressor					983:992	a tumor suppressor	975:992	a tumor suppressor	975:992	Interestingly, the protein RBL-2, which is a key regulator of entry into cell division and may function as a tumor suppressor, was identified as a substrate for three isoforms of OGT.
26960196	6	20	theme	tumor	977:981	arg1	RBL-2					895:899	the protein RBL-2	883:899	the protein RBL-2	883:899	Interestingly, the protein RBL-2, which is a key regulator of entry into cell division and may function as a tumor suppressor, was identified as a substrate for three isoforms of OGT.
26960196	8	21	theme	OGT	1194:1196	arg1	activity					1198:1205	OGT activity	1194:1205	OGT activity	1194:1205	Moreover, substitution of Ser 420, on its own, inhibited OGT activity, raising the possibility of mechanism-based development for selective OGT inhibitors.
26960196	4	22	theme	numerous	579:586	arg1	approaches					588:597	numerous approaches	579:597	numerous approaches	579:597	Recently, numerous approaches have been developed to identify OGT substrates and study their function, but there is still a strong demand for highly efficient techniques.
26960196	7	23	theme	peptide	1058:1064	arg1	scanning					1070:1077	peptide Ala scanning	1058:1077	peptide Ala scanning	1058:1077	Using peptide Ala scanning, we found Ser 420 is one possible O-GlcNAc site in RBL-2.
26960196	5	24	theme	novel	820:824	arg1	substrates					830:839	novel OGT substrates	820:839	novel OGT substrates	820:839	Here we demonstrated the utility of the peptide microarray approach to discover novel OGT substrates and study its specificity.
26960196	6	25	theme	OGT	1047:1049	arg1	isoforms					1035:1042	three isoforms	1029:1042	three isoforms of OGT	1029:1049	Interestingly, the protein RBL-2, which is a key regulator of entry into cell division and may function as a tumor suppressor, was identified as a substrate for three isoforms of OGT.
26960196	3	26	theme	cell	400:403	arg1	regulation					411:420	cell cycle regulation	400:420	cell cycle regulation	400:420	O-GlcNAcylation plays important role in many vital cellular events including transcription, cell cycle regulation, stress response and protein degradation, and altered O-GlcNAcylation has long been implicated in cancer, diabetes and neurodegenerative diseases.
26960196	7	27	theme	Ala	1066:1068	arg1	scanning					1070:1077	peptide Ala scanning	1058:1077	peptide Ala scanning	1058:1077	Using peptide Ala scanning, we found Ser 420 is one possible O-GlcNAc site in RBL-2.
26960196	6	28	theme	entry	930:934	arg1	RBL-2					895:899	the protein RBL-2	883:899	the protein RBL-2	883:899	Interestingly, the protein RBL-2, which is a key regulator of entry into cell division and may function as a tumor suppressor, was identified as a substrate for three isoforms of OGT.
26960196	6	28	theme	entry	930:934	arg1	regulator					917:925	a key regulator	911:925	a key regulator of entry into cell division	911:953	Interestingly, the protein RBL-2, which is a key regulator of entry into cell division and may function as a tumor suppressor, was identified as a substrate for three isoforms of OGT.
26960196	8	29	theme	OGT	1277:1279	arg1	inhibitors					1281:1290	selective OGT inhibitors	1267:1290	selective OGT inhibitors	1267:1290	Moreover, substitution of Ser 420, on its own, inhibited OGT activity, raising the possibility of mechanism-based development for selective OGT inhibitors.
26960196	0	30	theme	Novel	45:49	arg1	Substrates					72:81	Novel O-GlcNAc Transferase Substrates	45:81	Novel O-GlcNAc Transferase Substrates Using a Dynamic Peptide Microarray	45:116	Activity Based High-Throughput Screening for Novel O-GlcNAc Transferase Substrates Using a Dynamic Peptide Microarray.
26960196	8	31	theme	Ser	1163:1165	arg1	substitution					1147:1158	substitution	1147:1158	substitution of Ser 420	1147:1169	Moreover, substitution of Ser 420, on its own, inhibited OGT activity, raising the possibility of mechanism-based development for selective OGT inhibitors.
26960196	3	32	theme	altered	468:474	arg1	O-GlcNAcylation					476:490	altered O-GlcNAcylation	468:490	altered O-GlcNAcylation	468:490	O-GlcNAcylation plays important role in many vital cellular events including transcription, cell cycle regulation, stress response and protein degradation, and altered O-GlcNAcylation has long been implicated in cancer, diabetes and neurodegenerative diseases.
26960196	6	33	theme	protein	887:893	arg1	substrate					1015:1023	a substrate	1013:1023	a substrate for three isoforms of OGT	1013:1049	Interestingly, the protein RBL-2, which is a key regulator of entry into cell division and may function as a tumor suppressor, was identified as a substrate for three isoforms of OGT.
26960196	6	33	theme	protein	887:893	arg1	suppressor					983:992	a tumor suppressor	975:992	a tumor suppressor	975:992	Interestingly, the protein RBL-2, which is a key regulator of entry into cell division and may function as a tumor suppressor, was identified as a substrate for three isoforms of OGT.
26960196	6	33	theme	protein	887:893	arg1	RBL-2					895:899	the protein RBL-2	883:899	the protein RBL-2	883:899	Interestingly, the protein RBL-2, which is a key regulator of entry into cell division and may function as a tumor suppressor, was identified as a substrate for three isoforms of OGT.
26960196	6	33	theme	protein	887:893	arg1	regulator					917:925	a key regulator	911:925	a key regulator of entry into cell division	911:953	Interestingly, the protein RBL-2, which is a key regulator of entry into cell division and may function as a tumor suppressor, was identified as a substrate for three isoforms of OGT.
26960196	2	34	theme	O-GlcNAc	258:265	arg1	OGT					280:282	OGT	280:282	OGT	280:282	The O-GlcNAc cycle is catalyzed by O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA).
26960196	2	34	theme	O-GlcNAc	258:265	arg1	transferase					267:277	O-GlcNAc transferase	258:277	O-GlcNAc transferase (OGT)	258:283	The O-GlcNAc cycle is catalyzed by O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA).
26960196	0	35	theme	Transferase	60:70	arg1	Substrates					72:81	Novel O-GlcNAc Transferase Substrates	45:81	Novel O-GlcNAc Transferase Substrates Using a Dynamic Peptide Microarray	45:116	Activity Based High-Throughput Screening for Novel O-GlcNAc Transferase Substrates Using a Dynamic Peptide Microarray.
26960196	5	36	theme	OGT	826:828	arg1	substrates					830:839	novel OGT substrates	820:839	novel OGT substrates	820:839	Here we demonstrated the utility of the peptide microarray approach to discover novel OGT substrates and study its specificity.
26960196	5	37	theme	peptide	780:786	arg1	approach					799:806	the peptide microarray approach	776:806	the peptide microarray approach	776:806	Here we demonstrated the utility of the peptide microarray approach to discover novel OGT substrates and study its specificity.
26960196	3	38	gly	O-GlcNAcylation	476:490	arg1	diabetes					528:535	diabetes	528:535	diabetes	528:535	O-GlcNAcylation plays important role in many vital cellular events including transcription, cell cycle regulation, stress response and protein degradation, and altered O-GlcNAcylation has long been implicated in cancer, diabetes and neurodegenerative diseases.
26960196	3	38	gly	O-GlcNAcylation	476:490	arg1	diseases					559:566	neurodegenerative diseases	541:566	neurodegenerative diseases	541:566	O-GlcNAcylation plays important role in many vital cellular events including transcription, cell cycle regulation, stress response and protein degradation, and altered O-GlcNAcylation has long been implicated in cancer, diabetes and neurodegenerative diseases.
26960196	3	38	gly	O-GlcNAcylation	476:490	arg1	cancer					520:525	cancer	520:525	cancer	520:525	O-GlcNAcylation plays important role in many vital cellular events including transcription, cell cycle regulation, stress response and protein degradation, and altered O-GlcNAcylation has long been implicated in cancer, diabetes and neurodegenerative diseases.
26960196	8	39	theme	selective	1267:1275	arg1	inhibitors					1281:1290	selective OGT inhibitors	1267:1290	selective OGT inhibitors	1267:1290	Moreover, substitution of Ser 420, on its own, inhibited OGT activity, raising the possibility of mechanism-based development for selective OGT inhibitors.
26960196	3	40	theme	stress	423:428	arg1	response					430:437	stress response	423:437	stress response	423:437	O-GlcNAcylation plays important role in many vital cellular events including transcription, cell cycle regulation, stress response and protein degradation, and altered O-GlcNAcylation has long been implicated in cancer, diabetes and neurodegenerative diseases.
26960196	3	41	theme	important	330:338	arg1	role					340:343	important role	330:343	important role	330:343	O-GlcNAcylation plays important role in many vital cellular events including transcription, cell cycle regulation, stress response and protein degradation, and altered O-GlcNAcylation has long been implicated in cancer, diabetes and neurodegenerative diseases.
26960196	6	42	theme	cell	941:944	arg1	division					946:953	cell division	941:953	cell division	941:953	Interestingly, the protein RBL-2, which is a key regulator of entry into cell division and may function as a tumor suppressor, was identified as a substrate for three isoforms of OGT.
26960196	7	43	theme	O-GlcNAc	1113:1120	arg1	site					1122:1125	one possible O-GlcNAc site	1100:1125	one possible O-GlcNAc site in RBL-2	1100:1134	Using peptide Ala scanning, we found Ser 420 is one possible O-GlcNAc site in RBL-2.
26960196	1	44	theme	reversible	140:149	arg1	O-GlcNAcylation					119:133	O-GlcNAcylation	119:133	O-GlcNAcylation	119:133	O-GlcNAcylation is a reversible and dynamic protein post-translational modification in mammalian cells.
26960196	1	44	theme	reversible	140:149	arg1	modification					190:201	a reversible and dynamic protein post-translational modification	138:201	a reversible and dynamic protein post-translational modification in mammalian cells	138:220	O-GlcNAcylation is a reversible and dynamic protein post-translational modification in mammalian cells.
26960196	2	45	theme	O-GlcNAc	227:234	arg1	cycle					236:240	The O-GlcNAc cycle	223:240	The O-GlcNAc cycle	223:240	The O-GlcNAc cycle is catalyzed by O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA).
26960196	1	46	theme	protein	163:169	arg1	O-GlcNAcylation					119:133	O-GlcNAcylation	119:133	O-GlcNAcylation	119:133	O-GlcNAcylation is a reversible and dynamic protein post-translational modification in mammalian cells.
26960196	1	46	theme	protein	163:169	arg1	modification					190:201	a reversible and dynamic protein post-translational modification	138:201	a reversible and dynamic protein post-translational modification in mammalian cells	138:220	O-GlcNAcylation is a reversible and dynamic protein post-translational modification in mammalian cells.
26960196	9	47	theme	novel	1347:1351	arg1	substrates					1357:1366	novel OGT substrates	1347:1366	novel OGT substrates	1347:1366	This approach will prove useful for both discovery of novel OGT substrates and studying OGT specificity.
26960196	3	48	theme	many	348:351	arg1	events					368:373	many vital cellular events	348:373	many vital cellular events including transcription, cell cycle regulation, stress response and protein degradation	348:461	O-GlcNAcylation plays important role in many vital cellular events including transcription, cell cycle regulation, stress response and protein degradation, and altered O-GlcNAcylation has long been implicated in cancer, diabetes and neurodegenerative diseases.
26960196	3	48	theme	many	348:351	arg1	regulation					411:420	cell cycle regulation	400:420	cell cycle regulation	400:420	O-GlcNAcylation plays important role in many vital cellular events including transcription, cell cycle regulation, stress response and protein degradation, and altered O-GlcNAcylation has long been implicated in cancer, diabetes and neurodegenerative diseases.
26960196	3	48	theme	many	348:351	arg1	response					430:437	stress response	423:437	stress response	423:437	O-GlcNAcylation plays important role in many vital cellular events including transcription, cell cycle regulation, stress response and protein degradation, and altered O-GlcNAcylation has long been implicated in cancer, diabetes and neurodegenerative diseases.
26960196	3	48	theme	many	348:351	arg1	degradation					451:461	protein degradation	443:461	protein degradation	443:461	O-GlcNAcylation plays important role in many vital cellular events including transcription, cell cycle regulation, stress response and protein degradation, and altered O-GlcNAcylation has long been implicated in cancer, diabetes and neurodegenerative diseases.
26960196	3	48	theme	many	348:351	arg1	transcription					385:397	transcription	385:397	transcription	385:397	O-GlcNAcylation plays important role in many vital cellular events including transcription, cell cycle regulation, stress response and protein degradation, and altered O-GlcNAcylation has long been implicated in cancer, diabetes and neurodegenerative diseases.
26960196	1	49	theme	dynamic	155:161	arg1	O-GlcNAcylation					119:133	O-GlcNAcylation	119:133	O-GlcNAcylation	119:133	O-GlcNAcylation is a reversible and dynamic protein post-translational modification in mammalian cells.
26960196	1	49	theme	dynamic	155:161	arg1	modification					190:201	a reversible and dynamic protein post-translational modification	138:201	a reversible and dynamic protein post-translational modification in mammalian cells	138:220	O-GlcNAcylation is a reversible and dynamic protein post-translational modification in mammalian cells.
26960196	9	50	theme	OGT	1353:1355	arg1	substrates					1357:1366	novel OGT substrates	1347:1366	novel OGT substrates	1347:1366	This approach will prove useful for both discovery of novel OGT substrates and studying OGT specificity.
26960196	3	51	theme	vital	353:357	arg1	events					368:373	many vital cellular events	348:373	many vital cellular events including transcription, cell cycle regulation, stress response and protein degradation	348:461	O-GlcNAcylation plays important role in many vital cellular events including transcription, cell cycle regulation, stress response and protein degradation, and altered O-GlcNAcylation has long been implicated in cancer, diabetes and neurodegenerative diseases.
26960196	3	51	theme	vital	353:357	arg1	regulation					411:420	cell cycle regulation	400:420	cell cycle regulation	400:420	O-GlcNAcylation plays important role in many vital cellular events including transcription, cell cycle regulation, stress response and protein degradation, and altered O-GlcNAcylation has long been implicated in cancer, diabetes and neurodegenerative diseases.
26960196	3	51	theme	vital	353:357	arg1	response					430:437	stress response	423:437	stress response	423:437	O-GlcNAcylation plays important role in many vital cellular events including transcription, cell cycle regulation, stress response and protein degradation, and altered O-GlcNAcylation has long been implicated in cancer, diabetes and neurodegenerative diseases.
26960196	3	51	theme	vital	353:357	arg1	degradation					451:461	protein degradation	443:461	protein degradation	443:461	O-GlcNAcylation plays important role in many vital cellular events including transcription, cell cycle regulation, stress response and protein degradation, and altered O-GlcNAcylation has long been implicated in cancer, diabetes and neurodegenerative diseases.
26960196	3	51	theme	vital	353:357	arg1	transcription					385:397	transcription	385:397	transcription	385:397	O-GlcNAcylation plays important role in many vital cellular events including transcription, cell cycle regulation, stress response and protein degradation, and altered O-GlcNAcylation has long been implicated in cancer, diabetes and neurodegenerative diseases.
26960196	0	52	theme	High-Throughput	15:29	arg1	Screening					31:39	High-Throughput Screening	15:39	High-Throughput Screening for Novel O-GlcNAc Transferase Substrates Using a Dynamic Peptide Microarray	15:116	Activity Based High-Throughput Screening for Novel O-GlcNAc Transferase Substrates Using a Dynamic Peptide Microarray.
26960196	3	53	theme	neurodegenerative	541:557	arg1	diseases					559:566	neurodegenerative diseases	541:566	neurodegenerative diseases	541:566	O-GlcNAcylation plays important role in many vital cellular events including transcription, cell cycle regulation, stress response and protein degradation, and altered O-GlcNAcylation has long been implicated in cancer, diabetes and neurodegenerative diseases.
26960196	9	54	theme	substrates	1357:1366	arg1	discovery					1334:1342	both discovery	1329:1342	both discovery of novel OGT substrates	1329:1366	This approach will prove useful for both discovery of novel OGT substrates and studying OGT specificity.
33855783	4	0	theme	O-GlcNAcylation	786:800	arg1	sites					802:806	the O-GlcNAcylation sites	782:806	the O-GlcNAcylation sites	782:806	We further show that TDP-43 mutations in the O-GlcNAcylation sites improve locomotion defects of larvae and adult flies and extend adult life spans, following TDP-43 overexpression in Drosophila motor neurons.
33855783	0	1	theme	splicing	80:87	arg1	activity					89:96	TDP-43's mRNA splicing activity	66:96	TDP-43's mRNA splicing activity	66:96	O-GlcNAcylation of TDP-43 suppresses proteinopathies and promotes TDP-43's mRNA splicing activity.
33855783	5	2	theme	proper	1014:1019	arg1	splicing					1021:1028	proper splicing	1014:1028	proper splicing of many mRNAs, including STMN2, which is required for normal axonal outgrowth and regeneration	1014:1123	We finally demonstrate that O-GlcNAcylation of TDP-43 promotes proper splicing of many mRNAs, including STMN2, which is required for normal axonal outgrowth and regeneration.
33855783	5	3	theme	axonal	1091:1096	arg1	outgrowth					1098:1106	normal axonal outgrowth	1084:1106	normal axonal outgrowth	1084:1106	We finally demonstrate that O-GlcNAcylation of TDP-43 promotes proper splicing of many mRNAs, including STMN2, which is required for normal axonal outgrowth and regeneration.
33855783	5	4	theme	TDP-43	998:1003	arg1	O-GlcNAcylation					979:993	O-GlcNAcylation	979:993	O-GlcNAcylation of TDP-43	979:1003	We finally demonstrate that O-GlcNAcylation of TDP-43 promotes proper splicing of many mRNAs, including STMN2, which is required for normal axonal outgrowth and regeneration.
33855783	4	5	from	mutations	769:777	arg1	sites					802:806	the O-GlcNAcylation sites	782:806	the O-GlcNAcylation sites	782:806	We further show that TDP-43 mutations in the O-GlcNAcylation sites improve locomotion defects of larvae and adult flies and extend adult life spans, following TDP-43 overexpression in Drosophila motor neurons.
33855783	4	6	theme	flies	855:859	arg1	defects					827:833	locomotion defects	816:833	locomotion defects of larvae and adult flies	816:859	We further show that TDP-43 mutations in the O-GlcNAcylation sites improve locomotion defects of larvae and adult flies and extend adult life spans, following TDP-43 overexpression in Drosophila motor neurons.
33855783	3	7	theme	TDP-43	615:620	arg1	aggregation					622:632	TDP-43 aggregation	615:632	TDP-43 aggregation	615:632	Biochemical and cell-based assays indicate that OGT's catalytic activity suppresses TDP-43 aggregation and hyperphosphorylation, whereas abolishment of TDP-43 O-GlcNAcylation impairs its RNA splicing activity.
33855783	4	8	theme	locomotion	816:825	arg1	defects					827:833	locomotion defects	816:833	locomotion defects of larvae and adult flies	816:859	We further show that TDP-43 mutations in the O-GlcNAcylation sites improve locomotion defects of larvae and adult flies and extend adult life spans, following TDP-43 overexpression in Drosophila motor neurons.
33855783	3	9	theme	catalytic	585:593	arg1	activity					595:602	OGT's catalytic activity	579:602	OGT's catalytic activity	579:602	Biochemical and cell-based assays indicate that OGT's catalytic activity suppresses TDP-43 aggregation and hyperphosphorylation, whereas abolishment of TDP-43 O-GlcNAcylation impairs its RNA splicing activity.
33855783	4	10	theme	TDP-43	762:767	arg1	mutations					769:777	TDP-43 mutations	762:777	TDP-43 mutations in the O-GlcNAcylation sites	762:806	We further show that TDP-43 mutations in the O-GlcNAcylation sites improve locomotion defects of larvae and adult flies and extend adult life spans, following TDP-43 overexpression in Drosophila motor neurons.
33855783	1	11	theme	amyotrophic	198:208	arg1	sclerosis					218:226	amyotrophic lateral sclerosis	198:226	amyotrophic lateral sclerosis (ALS)	198:232	Pathological TDP-43 aggregation is characteristic of several neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD-TDP); however, how TDP-43 aggregation and function are regulated remain poorly understood.
33855783	1	11	theme	amyotrophic	198:208	arg1	ALS					229:231	ALS	229:231	ALS	229:231	Pathological TDP-43 aggregation is characteristic of several neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD-TDP); however, how TDP-43 aggregation and function are regulated remain poorly understood.
33855783	4	12	theme	motor	936:940	arg1	neurons					942:948	Drosophila motor neurons	925:948	Drosophila motor neurons	925:948	We further show that TDP-43 mutations in the O-GlcNAcylation sites improve locomotion defects of larvae and adult flies and extend adult life spans, following TDP-43 overexpression in Drosophila motor neurons.
33855783	1	13	theme	lateral	210:216	arg1	sclerosis					218:226	amyotrophic lateral sclerosis	198:226	amyotrophic lateral sclerosis (ALS)	198:232	Pathological TDP-43 aggregation is characteristic of several neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD-TDP); however, how TDP-43 aggregation and function are regulated remain poorly understood.
33855783	1	13	theme	lateral	210:216	arg1	ALS					229:231	ALS	229:231	ALS	229:231	Pathological TDP-43 aggregation is characteristic of several neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD-TDP); however, how TDP-43 aggregation and function are regulated remain poorly understood.
33855783	4	14	theme	larvae	838:843	arg1	defects					827:833	locomotion defects	816:833	locomotion defects of larvae and adult flies	816:859	We further show that TDP-43 mutations in the O-GlcNAcylation sites improve locomotion defects of larvae and adult flies and extend adult life spans, following TDP-43 overexpression in Drosophila motor neurons.
33855783	2	15	theme	transferase	397:407	arg1	O-GlcNAcylation					422:436	O-GlcNAc transferase OGT-mediated O-GlcNAcylation	388:436	O-GlcNAc transferase OGT-mediated O-GlcNAcylation of TDP-43	388:446	Here, we show that O-GlcNAc transferase OGT-mediated O-GlcNAcylation of TDP-43 suppresses ALS-associated proteinopathies and promotes TDP-43's splicing function.
33855783	1	16	theme	Pathological	99:110	arg1	aggregation					119:129	Pathological TDP-43 aggregation	99:129	Pathological TDP-43 aggregation	99:129	Pathological TDP-43 aggregation is characteristic of several neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD-TDP); however, how TDP-43 aggregation and function are regulated remain poorly understood.
33855783	2	17	theme	O-GlcNAc	388:395	arg1	transferase					397:407	O-GlcNAc transferase	388:407	O-GlcNAc transferase OGT-mediated O-GlcNAcylation of TDP-43	388:446	Here, we show that O-GlcNAc transferase OGT-mediated O-GlcNAcylation of TDP-43 suppresses ALS-associated proteinopathies and promotes TDP-43's splicing function.
33855783	1	18	theme	TDP-43	297:302	arg1	aggregation					304:314	TDP-43 aggregation	297:314	TDP-43 aggregation	297:314	Pathological TDP-43 aggregation is characteristic of several neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD-TDP); however, how TDP-43 aggregation and function are regulated remain poorly understood.
33855783	5	19	theme	mRNAs	1038:1042	arg1	splicing					1021:1028	proper splicing	1014:1028	proper splicing of many mRNAs, including STMN2, which is required for normal axonal outgrowth and regeneration	1014:1123	We finally demonstrate that O-GlcNAcylation of TDP-43 promotes proper splicing of many mRNAs, including STMN2, which is required for normal axonal outgrowth and regeneration.
33855783	1	20	theme	TDP-43	112:117	arg1	aggregation					119:129	Pathological TDP-43 aggregation	99:129	Pathological TDP-43 aggregation	99:129	Pathological TDP-43 aggregation is characteristic of several neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD-TDP); however, how TDP-43 aggregation and function are regulated remain poorly understood.
33855783	2	21	theme	ALS-associated	459:472	arg1	proteinopathies					474:488	ALS-associated proteinopathies	459:488	ALS-associated proteinopathies	459:488	Here, we show that O-GlcNAc transferase OGT-mediated O-GlcNAcylation of TDP-43 suppresses ALS-associated proteinopathies and promotes TDP-43's splicing function.
33855783	0	22	theme	TDP-43	19:24	arg1	O-GlcNAcylation					0:14	O-GlcNAcylation	0:14	O-GlcNAcylation of TDP-43	0:24	O-GlcNAcylation of TDP-43 suppresses proteinopathies and promotes TDP-43's mRNA splicing activity.
33855783	4	23	theme	adult	872:876	arg1	life					878:881	adult life spans	872:887	adult life spans	872:887	We further show that TDP-43 mutations in the O-GlcNAcylation sites improve locomotion defects of larvae and adult flies and extend adult life spans, following TDP-43 overexpression in Drosophila motor neurons.
33855783	6	24	theme	TDP-43-linked	1207:1219	arg1	pathogenesis					1221:1232	TDP-43-linked pathogenesis	1207:1232	TDP-43-linked pathogenesis	1207:1232	Our findings suggest that O-GlcNAcylation might be a target for the treatment of TDP-43-linked pathogenesis.
33855783	4	25	dep	life	878:881	arg1	spans					883:887	spans	883:887	spans	883:887	We further show that TDP-43 mutations in the O-GlcNAcylation sites improve locomotion defects of larvae and adult flies and extend adult life spans, following TDP-43 overexpression in Drosophila motor neurons.
33855783	2	26	theme	TDP-43	441:446	arg1	O-GlcNAcylation					422:436	O-GlcNAc transferase OGT-mediated O-GlcNAcylation	388:436	O-GlcNAc transferase OGT-mediated O-GlcNAcylation of TDP-43	388:446	Here, we show that O-GlcNAc transferase OGT-mediated O-GlcNAcylation of TDP-43 suppresses ALS-associated proteinopathies and promotes TDP-43's splicing function.
33855783	3	27	theme	splicing	722:729	arg1	activity					731:738	its RNA splicing activity	714:738	its RNA splicing activity	714:738	Biochemical and cell-based assays indicate that OGT's catalytic activity suppresses TDP-43 aggregation and hyperphosphorylation, whereas abolishment of TDP-43 O-GlcNAcylation impairs its RNA splicing activity.
33855783	3	28	theme	TDP-43	683:688	arg1	O-GlcNAcylation					690:704	TDP-43 O-GlcNAcylation	683:704	TDP-43 O-GlcNAcylation	683:704	Biochemical and cell-based assays indicate that OGT's catalytic activity suppresses TDP-43 aggregation and hyperphosphorylation, whereas abolishment of TDP-43 O-GlcNAcylation impairs its RNA splicing activity.
33855783	1	29	theme	frontotemporal	238:251	arg1	FTLD-TDP					273:280	FTLD-TDP	273:280	FTLD-TDP	273:280	Pathological TDP-43 aggregation is characteristic of several neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD-TDP); however, how TDP-43 aggregation and function are regulated remain poorly understood.
33855783	1	29	theme	frontotemporal	238:251	arg1	degeneration					259:270	frontotemporal lobar degeneration	238:270	frontotemporal lobar degeneration (FTLD-TDP)	238:281	Pathological TDP-43 aggregation is characteristic of several neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD-TDP); however, how TDP-43 aggregation and function are regulated remain poorly understood.
33855783	2	30	theme	splicing	512:519	arg1	function					521:528	TDP-43's splicing function	503:528	TDP-43's splicing function	503:528	Here, we show that O-GlcNAc transferase OGT-mediated O-GlcNAcylation of TDP-43 suppresses ALS-associated proteinopathies and promotes TDP-43's splicing function.
33855783	4	31	theme	Drosophila	925:934	arg1	neurons					942:948	Drosophila motor neurons	925:948	Drosophila motor neurons	925:948	We further show that TDP-43 mutations in the O-GlcNAcylation sites improve locomotion defects of larvae and adult flies and extend adult life spans, following TDP-43 overexpression in Drosophila motor neurons.
33855783	3	32	theme	cell-based	547:556	arg1	assays					558:563	Biochemical and cell-based assays	531:563	assays	558:563	Biochemical and cell-based assays indicate that OGT's catalytic activity suppresses TDP-43 aggregation and hyperphosphorylation, whereas abolishment of TDP-43 O-GlcNAcylation impairs its RNA splicing activity.
33855783	4	33	from	overexpression	907:920	arg1	neurons					942:948	Drosophila motor neurons	925:948	Drosophila motor neurons	925:948	We further show that TDP-43 mutations in the O-GlcNAcylation sites improve locomotion defects of larvae and adult flies and extend adult life spans, following TDP-43 overexpression in Drosophila motor neurons.
33855783	5	34	theme	normal	1084:1089	arg1	outgrowth					1098:1106	normal axonal outgrowth	1084:1106	normal axonal outgrowth	1084:1106	We finally demonstrate that O-GlcNAcylation of TDP-43 promotes proper splicing of many mRNAs, including STMN2, which is required for normal axonal outgrowth and regeneration.
33855783	4	35	theme	TDP-43	900:905	arg1	overexpression					907:920	TDP-43 overexpression	900:920	TDP-43 overexpression in Drosophila motor neurons	900:948	We further show that TDP-43 mutations in the O-GlcNAcylation sites improve locomotion defects of larvae and adult flies and extend adult life spans, following TDP-43 overexpression in Drosophila motor neurons.
33855783	3	36	theme	Biochemical	531:541	arg1	assays					558:563	Biochemical and cell-based assays	531:563	assays	558:563	Biochemical and cell-based assays indicate that OGT's catalytic activity suppresses TDP-43 aggregation and hyperphosphorylation, whereas abolishment of TDP-43 O-GlcNAcylation impairs its RNA splicing activity.
33855783	4	37	theme	adult	849:853	arg1	flies					855:859	adult flies	849:859	adult flies	849:859	We further show that TDP-43 mutations in the O-GlcNAcylation sites improve locomotion defects of larvae and adult flies and extend adult life spans, following TDP-43 overexpression in Drosophila motor neurons.
33855783	1	38	theme	lobar	253:257	arg1	FTLD-TDP					273:280	FTLD-TDP	273:280	FTLD-TDP	273:280	Pathological TDP-43 aggregation is characteristic of several neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD-TDP); however, how TDP-43 aggregation and function are regulated remain poorly understood.
33855783	1	38	theme	lobar	253:257	arg1	degeneration					259:270	frontotemporal lobar degeneration	238:270	frontotemporal lobar degeneration (FTLD-TDP)	238:281	Pathological TDP-43 aggregation is characteristic of several neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD-TDP); however, how TDP-43 aggregation and function are regulated remain poorly understood.
33855783	6	39	link	TDP-43-linked	1207:1219	arg1	pathogenesis					1221:1232	TDP-43-linked pathogenesis	1207:1232	TDP-43-linked pathogenesis	1207:1232	Our findings suggest that O-GlcNAcylation might be a target for the treatment of TDP-43-linked pathogenesis.
33855783	3	40	theme	RNA	718:720	arg1	activity					731:738	its RNA splicing activity	714:738	its RNA splicing activity	714:738	Biochemical and cell-based assays indicate that OGT's catalytic activity suppresses TDP-43 aggregation and hyperphosphorylation, whereas abolishment of TDP-43 O-GlcNAcylation impairs its RNA splicing activity.
33855783	1	41	theme	several	152:158	arg1	sclerosis					218:226	amyotrophic lateral sclerosis	198:226	amyotrophic lateral sclerosis (ALS)	198:232	Pathological TDP-43 aggregation is characteristic of several neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD-TDP); however, how TDP-43 aggregation and function are regulated remain poorly understood.
33855783	1	41	theme	several	152:158	arg1	diseases					178:185	several neurodegenerative diseases	152:185	several neurodegenerative diseases	152:185	Pathological TDP-43 aggregation is characteristic of several neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD-TDP); however, how TDP-43 aggregation and function are regulated remain poorly understood.
33855783	1	41	theme	several	152:158	arg1	degeneration					259:270	frontotemporal lobar degeneration	238:270	frontotemporal lobar degeneration (FTLD-TDP)	238:281	Pathological TDP-43 aggregation is characteristic of several neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD-TDP); however, how TDP-43 aggregation and function are regulated remain poorly understood.
33855783	5	42	theme	many	1033:1036	arg1	STMN2					1055:1059	STMN2	1055:1059	STMN2	1055:1059	We finally demonstrate that O-GlcNAcylation of TDP-43 promotes proper splicing of many mRNAs, including STMN2, which is required for normal axonal outgrowth and regeneration.
33855783	5	42	theme	many	1033:1036	arg1	mRNAs					1038:1042	many mRNAs	1033:1042	many mRNAs	1033:1042	We finally demonstrate that O-GlcNAcylation of TDP-43 promotes proper splicing of many mRNAs, including STMN2, which is required for normal axonal outgrowth and regeneration.
33855783	0	43	theme	mRNA	75:78	arg1	activity					89:96	TDP-43's mRNA splicing activity	66:96	TDP-43's mRNA splicing activity	66:96	O-GlcNAcylation of TDP-43 suppresses proteinopathies and promotes TDP-43's mRNA splicing activity.
33855783	3	44	theme	O-GlcNAcylation	690:704	arg1	abolishment					668:678	abolishment	668:678	abolishment of TDP-43 O-GlcNAcylation	668:704	Biochemical and cell-based assays indicate that OGT's catalytic activity suppresses TDP-43 aggregation and hyperphosphorylation, whereas abolishment of TDP-43 O-GlcNAcylation impairs its RNA splicing activity.
33855783	1	45	theme	neurodegenerative	160:176	arg1	sclerosis					218:226	amyotrophic lateral sclerosis	198:226	amyotrophic lateral sclerosis (ALS)	198:232	Pathological TDP-43 aggregation is characteristic of several neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD-TDP); however, how TDP-43 aggregation and function are regulated remain poorly understood.
33855783	1	45	theme	neurodegenerative	160:176	arg1	diseases					178:185	several neurodegenerative diseases	152:185	several neurodegenerative diseases	152:185	Pathological TDP-43 aggregation is characteristic of several neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD-TDP); however, how TDP-43 aggregation and function are regulated remain poorly understood.
33855783	1	45	theme	neurodegenerative	160:176	arg1	degeneration					259:270	frontotemporal lobar degeneration	238:270	frontotemporal lobar degeneration (FTLD-TDP)	238:281	Pathological TDP-43 aggregation is characteristic of several neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD-TDP); however, how TDP-43 aggregation and function are regulated remain poorly understood.
33855783	2	46	theme	OGT-mediated	409:420	arg1	O-GlcNAcylation					422:436	O-GlcNAc transferase OGT-mediated O-GlcNAcylation	388:436	O-GlcNAc transferase OGT-mediated O-GlcNAcylation of TDP-43	388:446	Here, we show that O-GlcNAc transferase OGT-mediated O-GlcNAcylation of TDP-43 suppresses ALS-associated proteinopathies and promotes TDP-43's splicing function.
33855783	6	47	theme	pathogenesis	1221:1232	arg1	treatment					1194:1202	the treatment	1190:1202	the treatment of TDP-43-linked pathogenesis	1190:1232	Our findings suggest that O-GlcNAcylation might be a target for the treatment of TDP-43-linked pathogenesis.
33855783	1	48	theme	diseases	178:185	arg1	characteristic					134:147	characteristic	134:147	characteristic of several neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD-TDP)	134:281	Pathological TDP-43 aggregation is characteristic of several neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD-TDP); however, how TDP-43 aggregation and function are regulated remain poorly understood.
34019948	6	0	theme	deacetylation	1305:1317	arg1	complex					1326:1332	nucleosome remodeling and histone deacetylation (NuRD) complex	1271:1332	nucleosome remodeling and histone deacetylation (NuRD) complex	1271:1332	MTA1 is modified with O-GlcNAc residues at serine (S) residues S237/S241/S246 in adriamycin-adaptive breast cancer cells, and this modification improves the genome-wide interactions of MTA1 with gene promotor regions by enhancing its association with nucleosome remodeling and histone deacetylation (NuRD) complex.
34019948	8	1	from	regulation	1721:1730	arg1	cancers					1761:1767	breast cancers	1754:1767	breast cancers	1754:1767	CONCLUSIONS Our findings reveal a previously unrecognized role for O-GlcNAc-modified MTA1 in transcriptional regulation and suggest that the O-GlcNAc modification is a key to the molecular regulation of chemoresistance in breast cancers.
34019948	4	2	theme	O-GlcNAc	568:575	arg1	modification					577:588	its O-GlcNAc modification	564:588	its O-GlcNAc modification	564:588	METHODS In the current study, the role of MTA1 and its O-GlcNAc modification in breast cancer cell genotoxic adaptation was investigated through quantitative proteomics, chromatin immunoprecipitation followed by sequencing (ChIP-seq), transcriptome analysis, and loss- and gain-of-function experiments.
34019948	0	3	theme	genotoxic	88:96	arg1	adaptation					98:107	breast cancer cell genotoxic adaptation	69:107	breast cancer cell genotoxic adaptation	69:107	O-GlcNAc modification regulates MTA1 transcriptional activity during breast cancer cell genotoxic adaptation.
34019948	8	4	theme	O-GlcNAc	1673:1680	arg1	modification					1682:1693	the O-GlcNAc modification	1669:1693	the O-GlcNAc modification	1669:1693	CONCLUSIONS Our findings reveal a previously unrecognized role for O-GlcNAc-modified MTA1 in transcriptional regulation and suggest that the O-GlcNAc modification is a key to the molecular regulation of chemoresistance in breast cancers.
34019948	8	4	theme	O-GlcNAc	1673:1680	arg1	key					1700:1702	key	1700:1702	key	1700:1702	CONCLUSIONS Our findings reveal a previously unrecognized role for O-GlcNAc-modified MTA1 in transcriptional regulation and suggest that the O-GlcNAc modification is a key to the molecular regulation of chemoresistance in breast cancers.
34019948	7	5	theme	cancer	1498:1503	arg1	cells					1505:1509	breast cancer cells	1491:1509	breast cancer cells	1491:1509	Further, O-GlcNAc modification modulates MTA1 chromatin binding, influencing the specific transcriptional regulation of genes involved in the adaptation of breast cancer cells to genotoxic stress.
34019948	4	6	dep	loss-	776:780	arg1	experiments					803:813	experiments	803:813	experiments	803:813	METHODS In the current study, the role of MTA1 and its O-GlcNAc modification in breast cancer cell genotoxic adaptation was investigated through quantitative proteomics, chromatin immunoprecipitation followed by sequencing (ChIP-seq), transcriptome analysis, and loss- and gain-of-function experiments.
34019948	1	7	theme	gene	268:271	arg1	expression					273:282	gene expression	268:282	gene expression	268:282	BACKGROUND Chromatin modifier metastasis-associated protein 1 (MTA1), closely associated with tumor angiogenesis in breast cancer, plays an important role in gene expression and cancer cell behavior.
34019948	5	8	theme	genotoxic	998:1006	arg1	adaptation					1008:1017	breast cancer cell genotoxic adaptation	979:1017	breast cancer cell genotoxic adaptation	979:1017	RESULTS We demonstrate that the O-GlcNAc modification promotes MTA1 to interaction with chromatin and thus changes the expression of target genes, contributing to breast cancer cell genotoxic adaptation.
34019948	5	9	theme	cell	993:996	arg1	adaptation					1008:1017	breast cancer cell genotoxic adaptation	979:1017	breast cancer cell genotoxic adaptation	979:1017	RESULTS We demonstrate that the O-GlcNAc modification promotes MTA1 to interaction with chromatin and thus changes the expression of target genes, contributing to breast cancer cell genotoxic adaptation.
34019948	8	10	theme	molecular	1711:1719	arg1	regulation					1721:1730	the molecular regulation	1707:1730	the molecular regulation of chemoresistance in breast cancers	1707:1767	CONCLUSIONS Our findings reveal a previously unrecognized role for O-GlcNAc-modified MTA1 in transcriptional regulation and suggest that the O-GlcNAc modification is a key to the molecular regulation of chemoresistance in breast cancers.
34019948	6	11	theme	MTA1	1205:1208	arg1	interactions					1189:1200	the genome-wide interactions	1173:1200	the genome-wide interactions of MTA1 with gene promotor regions	1173:1235	MTA1 is modified with O-GlcNAc residues at serine (S) residues S237/S241/S246 in adriamycin-adaptive breast cancer cells, and this modification improves the genome-wide interactions of MTA1 with gene promotor regions by enhancing its association with nucleosome remodeling and histone deacetylation (NuRD) complex.
34019948	7	12	theme	genotoxic	1514:1522	arg1	stress					1524:1529	genotoxic stress	1514:1529	genotoxic stress	1514:1529	Further, O-GlcNAc modification modulates MTA1 chromatin binding, influencing the specific transcriptional regulation of genes involved in the adaptation of breast cancer cells to genotoxic stress.
34019948	8	13	theme	chemoresistance	1735:1749	arg1	regulation					1721:1730	the molecular regulation	1707:1730	the molecular regulation of chemoresistance in breast cancers	1707:1767	CONCLUSIONS Our findings reveal a previously unrecognized role for O-GlcNAc-modified MTA1 in transcriptional regulation and suggest that the O-GlcNAc modification is a key to the molecular regulation of chemoresistance in breast cancers.
34019948	7	14	theme	cells	1505:1509	arg1	adaptation					1477:1486	the adaptation	1473:1486	the adaptation of breast cancer cells to genotoxic stress	1473:1529	Further, O-GlcNAc modification modulates MTA1 chromatin binding, influencing the specific transcriptional regulation of genes involved in the adaptation of breast cancer cells to genotoxic stress.
34019948	4	15	theme	modification	577:588	arg1	role					547:550	the role	543:550	the role of MTA1 and its O-GlcNAc modification in breast cancer cell genotoxic adaptation	543:631	METHODS In the current study, the role of MTA1 and its O-GlcNAc modification in breast cancer cell genotoxic adaptation was investigated through quantitative proteomics, chromatin immunoprecipitation followed by sequencing (ChIP-seq), transcriptome analysis, and loss- and gain-of-function experiments.
34019948	5	16	theme	target	949:954	arg1	genes					956:960	target genes	949:960	target genes	949:960	RESULTS We demonstrate that the O-GlcNAc modification promotes MTA1 to interaction with chromatin and thus changes the expression of target genes, contributing to breast cancer cell genotoxic adaptation.
34019948	6	17	theme	cancer	1128:1133	arg1	cells					1135:1139	adriamycin-adaptive breast cancer cells	1101:1139	adriamycin-adaptive breast cancer cells	1101:1139	MTA1 is modified with O-GlcNAc residues at serine (S) residues S237/S241/S246 in adriamycin-adaptive breast cancer cells, and this modification improves the genome-wide interactions of MTA1 with gene promotor regions by enhancing its association with nucleosome remodeling and histone deacetylation (NuRD) complex.
34019948	6	18	theme	promotor	1220:1227	arg1	regions					1229:1235	gene promotor regions	1215:1235	gene promotor regions	1215:1235	MTA1 is modified with O-GlcNAc residues at serine (S) residues S237/S241/S246 in adriamycin-adaptive breast cancer cells, and this modification improves the genome-wide interactions of MTA1 with gene promotor regions by enhancing its association with nucleosome remodeling and histone deacetylation (NuRD) complex.
34019948	4	19	theme	chromatin	683:691	arg1	proteomics					671:680	quantitative proteomics	658:680	quantitative proteomics	658:680	METHODS In the current study, the role of MTA1 and its O-GlcNAc modification in breast cancer cell genotoxic adaptation was investigated through quantitative proteomics, chromatin immunoprecipitation followed by sequencing (ChIP-seq), transcriptome analysis, and loss- and gain-of-function experiments.
34019948	4	19	theme	chromatin	683:691	arg1	immunoprecipitation					693:711	chromatin immunoprecipitation	683:711	chromatin immunoprecipitation followed by sequencing (ChIP-seq), transcriptome analysis, and loss- and gain-of-function experiments	683:813	METHODS In the current study, the role of MTA1 and its O-GlcNAc modification in breast cancer cell genotoxic adaptation was investigated through quantitative proteomics, chromatin immunoprecipitation followed by sequencing (ChIP-seq), transcriptome analysis, and loss- and gain-of-function experiments.
34019948	2	20	theme	mass	397:400	arg1	spectroscopy					402:413	mass spectroscopy	397:413	mass spectroscopy	397:413	Recently, an association between O-GlcNAc transferase (OGT) and MTA1 was identified by mass spectroscopy.
34019948	6	21	with	association	1254:1264	arg1	complex					1326:1332	nucleosome remodeling and histone deacetylation (NuRD) complex	1271:1332	nucleosome remodeling and histone deacetylation (NuRD) complex	1271:1332	MTA1 is modified with O-GlcNAc residues at serine (S) residues S237/S241/S246 in adriamycin-adaptive breast cancer cells, and this modification improves the genome-wide interactions of MTA1 with gene promotor regions by enhancing its association with nucleosome remodeling and histone deacetylation (NuRD) complex.
34019948	5	22	with	interaction	887:897	arg1	chromatin					904:912	chromatin	904:912	chromatin	904:912	RESULTS We demonstrate that the O-GlcNAc modification promotes MTA1 to interaction with chromatin and thus changes the expression of target genes, contributing to breast cancer cell genotoxic adaptation.
34019948	6	23	theme	O-GlcNAc	1042:1049	arg1	residues					1051:1058	O-GlcNAc residues	1042:1058	O-GlcNAc residues at serine (S) residues S237/S241/S246 in adriamycin-adaptive breast cancer cells	1042:1139	MTA1 is modified with O-GlcNAc residues at serine (S) residues S237/S241/S246 in adriamycin-adaptive breast cancer cells, and this modification improves the genome-wide interactions of MTA1 with gene promotor regions by enhancing its association with nucleosome remodeling and histone deacetylation (NuRD) complex.
34019948	7	24	theme	MTA1	1376:1379	arg1	binding					1391:1397	MTA1 chromatin binding	1376:1397	MTA1 chromatin binding	1376:1397	Further, O-GlcNAc modification modulates MTA1 chromatin binding, influencing the specific transcriptional regulation of genes involved in the adaptation of breast cancer cells to genotoxic stress.
34019948	6	25	theme	gene	1215:1218	arg1	regions					1229:1235	gene promotor regions	1215:1235	gene promotor regions	1215:1235	MTA1 is modified with O-GlcNAc residues at serine (S) residues S237/S241/S246 in adriamycin-adaptive breast cancer cells, and this modification improves the genome-wide interactions of MTA1 with gene promotor regions by enhancing its association with nucleosome remodeling and histone deacetylation (NuRD) complex.
34019948	4	26	theme	quantitative	658:669	arg1	proteomics					671:680	quantitative proteomics	658:680	quantitative proteomics	658:680	METHODS In the current study, the role of MTA1 and its O-GlcNAc modification in breast cancer cell genotoxic adaptation was investigated through quantitative proteomics, chromatin immunoprecipitation followed by sequencing (ChIP-seq), transcriptome analysis, and loss- and gain-of-function experiments.
34019948	4	26	theme	quantitative	658:669	arg1	immunoprecipitation					693:711	chromatin immunoprecipitation	683:711	chromatin immunoprecipitation followed by sequencing (ChIP-seq), transcriptome analysis, and loss- and gain-of-function experiments	683:813	METHODS In the current study, the role of MTA1 and its O-GlcNAc modification in breast cancer cell genotoxic adaptation was investigated through quantitative proteomics, chromatin immunoprecipitation followed by sequencing (ChIP-seq), transcriptome analysis, and loss- and gain-of-function experiments.
34019948	8	27	dep	CONCLUSIONS	1532:1542	arg1	reveal					1557:1562	reveal	1557:1562	reveal a previously unrecognized role for O-GlcNAc-modified MTA1 in transcriptional regulation	1557:1650	CONCLUSIONS Our findings reveal a previously unrecognized role for O-GlcNAc-modified MTA1 in transcriptional regulation and suggest that the O-GlcNAc modification is a key to the molecular regulation of chemoresistance in breast cancers.
34019948	8	27	dep	CONCLUSIONS	1532:1542	arg1	suggest					1656:1662	suggest	1656:1662	suggest that the O-GlcNAc modification is a key to the molecular regulation of chemoresistance in breast cancers	1656:1767	CONCLUSIONS Our findings reveal a previously unrecognized role for O-GlcNAc-modified MTA1 in transcriptional regulation and suggest that the O-GlcNAc modification is a key to the molecular regulation of chemoresistance in breast cancers.
34019948	8	28	theme	transcriptional	1625:1639	arg1	regulation					1641:1650	transcriptional regulation	1625:1650	transcriptional regulation	1625:1650	CONCLUSIONS Our findings reveal a previously unrecognized role for O-GlcNAc-modified MTA1 in transcriptional regulation and suggest that the O-GlcNAc modification is a key to the molecular regulation of chemoresistance in breast cancers.
34019948	4	29	mod	modification	577:588	arg1	cancer					600:605	breast cancer	593:605	breast cancer cell genotoxic adaptation	593:631	METHODS In the current study, the role of MTA1 and its O-GlcNAc modification in breast cancer cell genotoxic adaptation was investigated through quantitative proteomics, chromatin immunoprecipitation followed by sequencing (ChIP-seq), transcriptome analysis, and loss- and gain-of-function experiments.
34019948	4	29	mod	modification	577:588	arg1	cell					607:610	breast cancer cell genotoxic adaptation	593:631	breast cancer cell genotoxic adaptation	593:631	METHODS In the current study, the role of MTA1 and its O-GlcNAc modification in breast cancer cell genotoxic adaptation was investigated through quantitative proteomics, chromatin immunoprecipitation followed by sequencing (ChIP-seq), transcriptome analysis, and loss- and gain-of-function experiments.
34019948	6	30	theme	adriamycin-adaptive	1101:1119	arg1	cells					1135:1139	adriamycin-adaptive breast cancer cells	1101:1139	adriamycin-adaptive breast cancer cells	1101:1139	MTA1 is modified with O-GlcNAc residues at serine (S) residues S237/S241/S246 in adriamycin-adaptive breast cancer cells, and this modification improves the genome-wide interactions of MTA1 with gene promotor regions by enhancing its association with nucleosome remodeling and histone deacetylation (NuRD) complex.
34019948	1	31	theme	tumor	204:208	arg1	angiogenesis					210:221	tumor angiogenesis	204:221	tumor angiogenesis in breast cancer	204:238	BACKGROUND Chromatin modifier metastasis-associated protein 1 (MTA1), closely associated with tumor angiogenesis in breast cancer, plays an important role in gene expression and cancer cell behavior.
34019948	0	32	theme	O-GlcNAc	0:7	arg1	modification					9:20	O-GlcNAc modification	0:20	O-GlcNAc modification	0:20	O-GlcNAc modification regulates MTA1 transcriptional activity during breast cancer cell genotoxic adaptation.
34019948	1	33	theme	cancer	288:293	arg1	behavior					300:307	cancer cell behavior	288:307	cancer cell behavior	288:307	BACKGROUND Chromatin modifier metastasis-associated protein 1 (MTA1), closely associated with tumor angiogenesis in breast cancer, plays an important role in gene expression and cancer cell behavior.
34019948	5	34	dep	RESULTS	816:822	arg1	demonstrate					827:837	demonstrate	827:837	demonstrate that the O-GlcNAc modification promotes MTA1 to interaction with chromatin and thus changes the expression of target genes, contributing to breast cancer cell genotoxic adaptation	827:1017	RESULTS We demonstrate that the O-GlcNAc modification promotes MTA1 to interaction with chromatin and thus changes the expression of target genes, contributing to breast cancer cell genotoxic adaptation.
34019948	8	35	theme	unrecognized	1577:1588	arg1	role					1590:1593	a previously unrecognized role	1564:1593	a previously unrecognized role for O-GlcNAc-modified MTA1 in transcriptional regulation	1564:1650	CONCLUSIONS Our findings reveal a previously unrecognized role for O-GlcNAc-modified MTA1 in transcriptional regulation and suggest that the O-GlcNAc modification is a key to the molecular regulation of chemoresistance in breast cancers.
34019948	1	36	theme	BACKGROUND	110:119	arg1	protein					162:168	BACKGROUND Chromatin modifier metastasis-associated protein 1	110:170	BACKGROUND Chromatin modifier metastasis-associated protein 1 (MTA1)	110:177	BACKGROUND Chromatin modifier metastasis-associated protein 1 (MTA1), closely associated with tumor angiogenesis in breast cancer, plays an important role in gene expression and cancer cell behavior.
34019948	1	36	theme	BACKGROUND	110:119	arg1	MTA1					173:176	MTA1	173:176	MTA1	173:176	BACKGROUND Chromatin modifier metastasis-associated protein 1 (MTA1), closely associated with tumor angiogenesis in breast cancer, plays an important role in gene expression and cancer cell behavior.
34019948	3	37	theme	potential	429:437	arg1	relationship					439:450	the potential relationship	425:450	the potential relationship between MTA1 and O-GlcNAc modification	425:489	However, the potential relationship between MTA1 and O-GlcNAc modification has not yet explored.
34019948	0	38	theme	MTA1	32:35	arg1	activity					53:60	MTA1 transcriptional activity	32:60	MTA1 transcriptional activity	32:60	O-GlcNAc modification regulates MTA1 transcriptional activity during breast cancer cell genotoxic adaptation.
34019948	1	39	theme	cell	295:298	arg1	behavior					300:307	cancer cell behavior	288:307	cancer cell behavior	288:307	BACKGROUND Chromatin modifier metastasis-associated protein 1 (MTA1), closely associated with tumor angiogenesis in breast cancer, plays an important role in gene expression and cancer cell behavior.
34019948	6	40	from	residues	1074:1081	arg1	cells					1135:1139	adriamycin-adaptive breast cancer cells	1101:1139	adriamycin-adaptive breast cancer cells	1101:1139	MTA1 is modified with O-GlcNAc residues at serine (S) residues S237/S241/S246 in adriamycin-adaptive breast cancer cells, and this modification improves the genome-wide interactions of MTA1 with gene promotor regions by enhancing its association with nucleosome remodeling and histone deacetylation (NuRD) complex.
34019948	6	40	from	residues	1074:1081	arg1	residues					1051:1058	O-GlcNAc residues	1042:1058	O-GlcNAc residues at serine (S) residues S237/S241/S246 in adriamycin-adaptive breast cancer cells	1042:1139	MTA1 is modified with O-GlcNAc residues at serine (S) residues S237/S241/S246 in adriamycin-adaptive breast cancer cells, and this modification improves the genome-wide interactions of MTA1 with gene promotor regions by enhancing its association with nucleosome remodeling and histone deacetylation (NuRD) complex.
34019948	1	41	theme	Chromatin	121:129	arg1	protein					162:168	BACKGROUND Chromatin modifier metastasis-associated protein 1	110:170	BACKGROUND Chromatin modifier metastasis-associated protein 1 (MTA1)	110:177	BACKGROUND Chromatin modifier metastasis-associated protein 1 (MTA1), closely associated with tumor angiogenesis in breast cancer, plays an important role in gene expression and cancer cell behavior.
34019948	1	41	theme	Chromatin	121:129	arg1	MTA1					173:176	MTA1	173:176	MTA1	173:176	BACKGROUND Chromatin modifier metastasis-associated protein 1 (MTA1), closely associated with tumor angiogenesis in breast cancer, plays an important role in gene expression and cancer cell behavior.
34019948	3	42	theme	O-GlcNAc	469:476	arg1	modification					478:489	O-GlcNAc modification	469:489	O-GlcNAc modification	469:489	However, the potential relationship between MTA1 and O-GlcNAc modification has not yet explored.
34019948	4	43	theme	transcriptome	748:760	arg1	analysis					762:769	transcriptome analysis	748:769	transcriptome analysis	748:769	METHODS In the current study, the role of MTA1 and its O-GlcNAc modification in breast cancer cell genotoxic adaptation was investigated through quantitative proteomics, chromatin immunoprecipitation followed by sequencing (ChIP-seq), transcriptome analysis, and loss- and gain-of-function experiments.
34019948	5	44	theme	breast	979:984	arg1	adaptation					1008:1017	breast cancer cell genotoxic adaptation	979:1017	breast cancer cell genotoxic adaptation	979:1017	RESULTS We demonstrate that the O-GlcNAc modification promotes MTA1 to interaction with chromatin and thus changes the expression of target genes, contributing to breast cancer cell genotoxic adaptation.
34019948	1	45	theme	modifier	131:138	arg1	protein					162:168	BACKGROUND Chromatin modifier metastasis-associated protein 1	110:170	BACKGROUND Chromatin modifier metastasis-associated protein 1 (MTA1)	110:177	BACKGROUND Chromatin modifier metastasis-associated protein 1 (MTA1), closely associated with tumor angiogenesis in breast cancer, plays an important role in gene expression and cancer cell behavior.
34019948	1	45	theme	modifier	131:138	arg1	MTA1					173:176	MTA1	173:176	MTA1	173:176	BACKGROUND Chromatin modifier metastasis-associated protein 1 (MTA1), closely associated with tumor angiogenesis in breast cancer, plays an important role in gene expression and cancer cell behavior.
34019948	1	46	theme	breast	226:231	arg1	cancer					233:238	breast cancer	226:238	breast cancer	226:238	BACKGROUND Chromatin modifier metastasis-associated protein 1 (MTA1), closely associated with tumor angiogenesis in breast cancer, plays an important role in gene expression and cancer cell behavior.
34019948	4	47	theme	MTA1	555:558	arg1	role					547:550	the role	543:550	the role of MTA1 and its O-GlcNAc modification in breast cancer cell genotoxic adaptation	543:631	METHODS In the current study, the role of MTA1 and its O-GlcNAc modification in breast cancer cell genotoxic adaptation was investigated through quantitative proteomics, chromatin immunoprecipitation followed by sequencing (ChIP-seq), transcriptome analysis, and loss- and gain-of-function experiments.
34019948	6	48	theme	histone	1297:1303	arg1	NuRD					1320:1323	NuRD	1320:1323	NuRD	1320:1323	MTA1 is modified with O-GlcNAc residues at serine (S) residues S237/S241/S246 in adriamycin-adaptive breast cancer cells, and this modification improves the genome-wide interactions of MTA1 with gene promotor regions by enhancing its association with nucleosome remodeling and histone deacetylation (NuRD) complex.
34019948	6	48	theme	histone	1297:1303	arg1	deacetylation					1305:1317	histone deacetylation	1297:1317	histone deacetylation (NuRD)	1297:1324	MTA1 is modified with O-GlcNAc residues at serine (S) residues S237/S241/S246 in adriamycin-adaptive breast cancer cells, and this modification improves the genome-wide interactions of MTA1 with gene promotor regions by enhancing its association with nucleosome remodeling and histone deacetylation (NuRD) complex.
34019948	7	49	theme	O-GlcNAc	1344:1351	arg1	modification					1353:1364	O-GlcNAc modification	1344:1364	O-GlcNAc modification	1344:1364	Further, O-GlcNAc modification modulates MTA1 chromatin binding, influencing the specific transcriptional regulation of genes involved in the adaptation of breast cancer cells to genotoxic stress.
34019948	0	50	theme	transcriptional	37:51	arg1	activity					53:60	MTA1 transcriptional activity	32:60	MTA1 transcriptional activity	32:60	O-GlcNAc modification regulates MTA1 transcriptional activity during breast cancer cell genotoxic adaptation.
34019948	6	51	mod	modified	1028:1035	arg3	residues					1051:1058	O-GlcNAc residues	1042:1058	O-GlcNAc residues at serine (S) residues S237/S241/S246 in adriamycin-adaptive breast cancer cells	1042:1139	MTA1 is modified with O-GlcNAc residues at serine (S) residues S237/S241/S246 in adriamycin-adaptive breast cancer cells, and this modification improves the genome-wide interactions of MTA1 with gene promotor regions by enhancing its association with nucleosome remodeling and histone deacetylation (NuRD) complex.
34019948	6	51	mod	modified	1028:1035	arg1	MTA1					1020:1023	MTA1	1020:1023	MTA1	1020:1023	MTA1 is modified with O-GlcNAc residues at serine (S) residues S237/S241/S246 in adriamycin-adaptive breast cancer cells, and this modification improves the genome-wide interactions of MTA1 with gene promotor regions by enhancing its association with nucleosome remodeling and histone deacetylation (NuRD) complex.
34019948	7	52	theme	chromatin	1381:1389	arg1	binding					1391:1397	MTA1 chromatin binding	1376:1397	MTA1 chromatin binding	1376:1397	Further, O-GlcNAc modification modulates MTA1 chromatin binding, influencing the specific transcriptional regulation of genes involved in the adaptation of breast cancer cells to genotoxic stress.
34019948	4	53	theme	genotoxic	612:620	arg1	adaptation					622:631	breast cancer cell genotoxic adaptation	593:631	breast cancer cell genotoxic adaptation	593:631	METHODS In the current study, the role of MTA1 and its O-GlcNAc modification in breast cancer cell genotoxic adaptation was investigated through quantitative proteomics, chromatin immunoprecipitation followed by sequencing (ChIP-seq), transcriptome analysis, and loss- and gain-of-function experiments.
34019948	7	54	theme	genes	1455:1459	arg1	regulation					1441:1450	the specific transcriptional regulation	1412:1450	the specific transcriptional regulation of genes involved in the adaptation of breast cancer cells to genotoxic stress	1412:1529	Further, O-GlcNAc modification modulates MTA1 chromatin binding, influencing the specific transcriptional regulation of genes involved in the adaptation of breast cancer cells to genotoxic stress.
34019948	5	55	theme	O-GlcNAc	848:855	arg1	modification					857:868	the O-GlcNAc modification	844:868	the O-GlcNAc modification	844:868	RESULTS We demonstrate that the O-GlcNAc modification promotes MTA1 to interaction with chromatin and thus changes the expression of target genes, contributing to breast cancer cell genotoxic adaptation.
34019948	0	56	theme	breast	69:74	arg1	adaptation					98:107	breast cancer cell genotoxic adaptation	69:107	breast cancer cell genotoxic adaptation	69:107	O-GlcNAc modification regulates MTA1 transcriptional activity during breast cancer cell genotoxic adaptation.
34019948	4	57	theme	current	528:534	arg1	study					536:540	the current study	524:540	the current study	524:540	METHODS In the current study, the role of MTA1 and its O-GlcNAc modification in breast cancer cell genotoxic adaptation was investigated through quantitative proteomics, chromatin immunoprecipitation followed by sequencing (ChIP-seq), transcriptome analysis, and loss- and gain-of-function experiments.
34019948	6	58	theme	remodeling	1282:1291	arg1	complex					1326:1332	nucleosome remodeling and histone deacetylation (NuRD) complex	1271:1332	nucleosome remodeling and histone deacetylation (NuRD) complex	1271:1332	MTA1 is modified with O-GlcNAc residues at serine (S) residues S237/S241/S246 in adriamycin-adaptive breast cancer cells, and this modification improves the genome-wide interactions of MTA1 with gene promotor regions by enhancing its association with nucleosome remodeling and histone deacetylation (NuRD) complex.
34019948	1	59	theme	metastasis-associated	140:160	arg1	protein					162:168	BACKGROUND Chromatin modifier metastasis-associated protein 1	110:170	BACKGROUND Chromatin modifier metastasis-associated protein 1 (MTA1)	110:177	BACKGROUND Chromatin modifier metastasis-associated protein 1 (MTA1), closely associated with tumor angiogenesis in breast cancer, plays an important role in gene expression and cancer cell behavior.
34019948	1	59	theme	metastasis-associated	140:160	arg1	MTA1					173:176	MTA1	173:176	MTA1	173:176	BACKGROUND Chromatin modifier metastasis-associated protein 1 (MTA1), closely associated with tumor angiogenesis in breast cancer, plays an important role in gene expression and cancer cell behavior.
34019948	8	60	theme	breast	1754:1759	arg1	cancers					1761:1767	breast cancers	1754:1767	breast cancers	1754:1767	CONCLUSIONS Our findings reveal a previously unrecognized role for O-GlcNAc-modified MTA1 in transcriptional regulation and suggest that the O-GlcNAc modification is a key to the molecular regulation of chemoresistance in breast cancers.
34019948	6	61	with	interactions	1189:1200	arg1	regions					1229:1235	gene promotor regions	1215:1235	gene promotor regions	1215:1235	MTA1 is modified with O-GlcNAc residues at serine (S) residues S237/S241/S246 in adriamycin-adaptive breast cancer cells, and this modification improves the genome-wide interactions of MTA1 with gene promotor regions by enhancing its association with nucleosome remodeling and histone deacetylation (NuRD) complex.
34019948	6	62	theme	nucleosome	1271:1280	arg1	remodeling					1282:1291	nucleosome remodeling	1271:1291	nucleosome remodeling	1271:1291	MTA1 is modified with O-GlcNAc residues at serine (S) residues S237/S241/S246 in adriamycin-adaptive breast cancer cells, and this modification improves the genome-wide interactions of MTA1 with gene promotor regions by enhancing its association with nucleosome remodeling and histone deacetylation (NuRD) complex.
34019948	5	63	theme	genes	956:960	arg1	expression					935:944	the expression	931:944	the expression of target genes	931:960	RESULTS We demonstrate that the O-GlcNAc modification promotes MTA1 to interaction with chromatin and thus changes the expression of target genes, contributing to breast cancer cell genotoxic adaptation.
34019948	8	64	from	role	1590:1593	arg1	regulation					1641:1650	transcriptional regulation	1625:1650	transcriptional regulation	1625:1650	CONCLUSIONS Our findings reveal a previously unrecognized role for O-GlcNAc-modified MTA1 in transcriptional regulation and suggest that the O-GlcNAc modification is a key to the molecular regulation of chemoresistance in breast cancers.
34019948	7	65	theme	specific	1416:1423	arg1	regulation					1441:1450	the specific transcriptional regulation	1412:1450	the specific transcriptional regulation of genes involved in the adaptation of breast cancer cells to genotoxic stress	1412:1529	Further, O-GlcNAc modification modulates MTA1 chromatin binding, influencing the specific transcriptional regulation of genes involved in the adaptation of breast cancer cells to genotoxic stress.
34019948	7	66	theme	transcriptional	1425:1439	arg1	regulation					1441:1450	the specific transcriptional regulation	1412:1450	the specific transcriptional regulation of genes involved in the adaptation of breast cancer cells to genotoxic stress	1412:1529	Further, O-GlcNAc modification modulates MTA1 chromatin binding, influencing the specific transcriptional regulation of genes involved in the adaptation of breast cancer cells to genotoxic stress.
34019948	6	67	theme	serine	1063:1068	arg1	residues					1074:1081	serine (S) residues	1063:1081	serine (S) residues S237/S241/S246 in adriamycin-adaptive breast cancer cells	1063:1139	MTA1 is modified with O-GlcNAc residues at serine (S) residues S237/S241/S246 in adriamycin-adaptive breast cancer cells, and this modification improves the genome-wide interactions of MTA1 with gene promotor regions by enhancing its association with nucleosome remodeling and histone deacetylation (NuRD) complex.
34019948	2	68	theme	O-GlcNAc	343:350	arg1	transferase					352:362	O-GlcNAc transferase	343:362	O-GlcNAc transferase (OGT)	343:368	Recently, an association between O-GlcNAc transferase (OGT) and MTA1 was identified by mass spectroscopy.
34019948	2	68	theme	O-GlcNAc	343:350	arg1	OGT					365:367	OGT	365:367	OGT	365:367	Recently, an association between O-GlcNAc transferase (OGT) and MTA1 was identified by mass spectroscopy.
34019948	5	69	theme	cancer	986:991	arg1	adaptation					1008:1017	breast cancer cell genotoxic adaptation	979:1017	breast cancer cell genotoxic adaptation	979:1017	RESULTS We demonstrate that the O-GlcNAc modification promotes MTA1 to interaction with chromatin and thus changes the expression of target genes, contributing to breast cancer cell genotoxic adaptation.
34019948	4	70	theme	cancer	600:605	arg1	adaptation					622:631	breast cancer cell genotoxic adaptation	593:631	breast cancer cell genotoxic adaptation	593:631	METHODS In the current study, the role of MTA1 and its O-GlcNAc modification in breast cancer cell genotoxic adaptation was investigated through quantitative proteomics, chromatin immunoprecipitation followed by sequencing (ChIP-seq), transcriptome analysis, and loss- and gain-of-function experiments.
34019948	6	71	dep	residues	1074:1081	arg1	S237/S241/S246					1083:1096	S237/S241/S246	1083:1096	S237/S241/S246	1083:1096	MTA1 is modified with O-GlcNAc residues at serine (S) residues S237/S241/S246 in adriamycin-adaptive breast cancer cells, and this modification improves the genome-wide interactions of MTA1 with gene promotor regions by enhancing its association with nucleosome remodeling and histone deacetylation (NuRD) complex.
34019948	7	72	theme	breast	1491:1496	arg1	cells					1505:1509	breast cancer cells	1491:1509	breast cancer cells	1491:1509	Further, O-GlcNAc modification modulates MTA1 chromatin binding, influencing the specific transcriptional regulation of genes involved in the adaptation of breast cancer cells to genotoxic stress.
34019948	6	73	theme	genome-wide	1177:1187	arg1	interactions					1189:1200	the genome-wide interactions	1173:1200	the genome-wide interactions of MTA1 with gene promotor regions	1173:1235	MTA1 is modified with O-GlcNAc residues at serine (S) residues S237/S241/S246 in adriamycin-adaptive breast cancer cells, and this modification improves the genome-wide interactions of MTA1 with gene promotor regions by enhancing its association with nucleosome remodeling and histone deacetylation (NuRD) complex.
34019948	4	74	theme	breast	593:598	arg1	cancer					600:605	breast cancer	593:605	breast cancer cell genotoxic adaptation	593:631	METHODS In the current study, the role of MTA1 and its O-GlcNAc modification in breast cancer cell genotoxic adaptation was investigated through quantitative proteomics, chromatin immunoprecipitation followed by sequencing (ChIP-seq), transcriptome analysis, and loss- and gain-of-function experiments.
34019948	0	75	theme	cell	83:86	arg1	adaptation					98:107	breast cancer cell genotoxic adaptation	69:107	breast cancer cell genotoxic adaptation	69:107	O-GlcNAc modification regulates MTA1 transcriptional activity during breast cancer cell genotoxic adaptation.
34019948	6	76	theme	S	1071:1071	arg1	residues					1074:1081	serine (S) residues	1063:1081	serine (S) residues S237/S241/S246 in adriamycin-adaptive breast cancer cells	1063:1139	MTA1 is modified with O-GlcNAc residues at serine (S) residues S237/S241/S246 in adriamycin-adaptive breast cancer cells, and this modification improves the genome-wide interactions of MTA1 with gene promotor regions by enhancing its association with nucleosome remodeling and histone deacetylation (NuRD) complex.
34019948	1	77	from	angiogenesis	210:221	arg1	cancer					233:238	breast cancer	226:238	breast cancer	226:238	BACKGROUND Chromatin modifier metastasis-associated protein 1 (MTA1), closely associated with tumor angiogenesis in breast cancer, plays an important role in gene expression and cancer cell behavior.
34019948	6	78	theme	breast	1121:1126	arg1	cells					1135:1139	adriamycin-adaptive breast cancer cells	1101:1139	adriamycin-adaptive breast cancer cells	1101:1139	MTA1 is modified with O-GlcNAc residues at serine (S) residues S237/S241/S246 in adriamycin-adaptive breast cancer cells, and this modification improves the genome-wide interactions of MTA1 with gene promotor regions by enhancing its association with nucleosome remodeling and histone deacetylation (NuRD) complex.
34019948	1	79	theme	important	250:258	arg1	role					260:263	an important role	247:263	an important role	247:263	BACKGROUND Chromatin modifier metastasis-associated protein 1 (MTA1), closely associated with tumor angiogenesis in breast cancer, plays an important role in gene expression and cancer cell behavior.
34019948	0	80	theme	cancer	76:81	arg1	adaptation					98:107	breast cancer cell genotoxic adaptation	69:107	breast cancer cell genotoxic adaptation	69:107	O-GlcNAc modification regulates MTA1 transcriptional activity during breast cancer cell genotoxic adaptation.
34019948	4	81	from	role	547:550	arg1	adaptation					622:631	breast cancer cell genotoxic adaptation	593:631	breast cancer cell genotoxic adaptation	593:631	METHODS In the current study, the role of MTA1 and its O-GlcNAc modification in breast cancer cell genotoxic adaptation was investigated through quantitative proteomics, chromatin immunoprecipitation followed by sequencing (ChIP-seq), transcriptome analysis, and loss- and gain-of-function experiments.
34019948	8	82	theme	O-GlcNAc-modified	1599:1615	arg1	MTA1					1617:1620	O-GlcNAc-modified MTA1	1599:1620	O-GlcNAc-modified MTA1	1599:1620	CONCLUSIONS Our findings reveal a previously unrecognized role for O-GlcNAc-modified MTA1 in transcriptional regulation and suggest that the O-GlcNAc modification is a key to the molecular regulation of chemoresistance in breast cancers.
34019948	4	83	theme	cell	607:610	arg1	adaptation					622:631	breast cancer cell genotoxic adaptation	593:631	breast cancer cell genotoxic adaptation	593:631	METHODS In the current study, the role of MTA1 and its O-GlcNAc modification in breast cancer cell genotoxic adaptation was investigated through quantitative proteomics, chromatin immunoprecipitation followed by sequencing (ChIP-seq), transcriptome analysis, and loss- and gain-of-function experiments.
27060025	6	0	theme	HDAC1	616:620	arg1	phosphorylation					597:611	the activated phosphorylation	583:611	the activated phosphorylation	583:611	HDAC1 O-GlcNAcylation increases the activated phosphorylation of HDAC1, which enhances its enzyme activity.
27060025	9	1	dep	occurrence	1061:1070	arg1	the					1057:1059	the	1057:1059	the	1057:1059	E-cadherin level is highly up-regulated in HDAC1 O-GlcNAc mutant-treated liver cancer cells, which inhibit the occurrence and development of HCC.
27060025	0	2	from	O-GlcNAcylation	0:14	arg1	carcinoma					60:68	hepatocellular carcinoma	45:68	hepatocellular carcinoma	45:68	O-GlcNAcylation of histone deacetylases 1 in hepatocellular carcinoma promotes cancer progression.
27060025	7	3	from	chromosome	781:790	arg1	histones					767:774	histones	767:774	histones from chromosome	767:790	HDAC1 O-GlcNAc mutants promote the p21 transcription regulation through affecting the acetylation levels of histones from chromosome, and then influence the proliferation of HCC cells.
27060025	7	3	from	chromosome	781:790	arg1	levels					757:762	the acetylation levels	741:762	the acetylation levels of histones from chromosome	741:790	HDAC1 O-GlcNAc mutants promote the p21 transcription regulation through affecting the acetylation levels of histones from chromosome, and then influence the proliferation of HCC cells.
27060025	5	4	contain	has	477:479	arg1	HDAC1					471:475	HDAC1	471:475	HDAC1	471:475	We found that HDAC1 has two major sites of O-GlcNAcylation in its histone deacetylase domain.
27060025	5	4	contain	has	477:479	arg2	O-GlcNAcylation					500:514	O-GlcNAcylation	500:514	O-GlcNAcylation	500:514	We found that HDAC1 has two major sites of O-GlcNAcylation in its histone deacetylase domain.
27060025	5	4	contain	has	477:479	arg2	sites					491:495	two major sites	481:495	two major sites of O-GlcNAcylation	481:514	We found that HDAC1 has two major sites of O-GlcNAcylation in its histone deacetylase domain.
27060025	4	5	gly	O-GlcNAcylation	407:421	arg1	HCC					452:454	HCC	452:454	HCC	452:454	The O-GlcNAcylation of HDAC1 is overexpressed in HCC.
27060025	7	6	theme	transcription	698:710	arg1	regulation					712:721	the p21 transcription regulation	690:721	the p21 transcription regulation	690:721	HDAC1 O-GlcNAc mutants promote the p21 transcription regulation through affecting the acetylation levels of histones from chromosome, and then influence the proliferation of HCC cells.
27060025	3	7	theme	present	331:337	arg1	study					339:343	the present study	327:343	the present study	327:343	In the present study, we investigated the physical link between OGT and HDAC1.
27060025	5	8	theme	deacetylase	531:541	arg1	domain					543:548	its histone deacetylase domain	519:548	its histone deacetylase domain	519:548	We found that HDAC1 has two major sites of O-GlcNAcylation in its histone deacetylase domain.
27060025	8	9	theme	O-GlcNAcylation	874:888	arg1	HDAC1					898:902	HDAC1	898:902	HDAC1	898:902	We also found that mutants of O-GlcNAcylation site of HDAC1 affect invasion and migration of HepG2 cells.
27060025	8	9	theme	O-GlcNAcylation	874:888	arg1	site					890:893	O-GlcNAcylation site	874:893	O-GlcNAcylation site of HDAC1	874:902	We also found that mutants of O-GlcNAcylation site of HDAC1 affect invasion and migration of HepG2 cells.
27060025	6	10	theme	activated	587:595	arg1	phosphorylation					597:611	the activated phosphorylation	583:611	the activated phosphorylation	583:611	HDAC1 O-GlcNAcylation increases the activated phosphorylation of HDAC1, which enhances its enzyme activity.
27060025	9	11	theme	liver	1023:1027	arg1	cells					1036:1040	HDAC1 O-GlcNAc mutant-treated liver cancer cells	993:1040	HDAC1 O-GlcNAc mutant-treated liver cancer cells	993:1040	E-cadherin level is highly up-regulated in HDAC1 O-GlcNAc mutant-treated liver cancer cells, which inhibit the occurrence and development of HCC.
27060025	1	12	theme	Hepatocellular	99:112	arg1	carcinoma					114:122	Hepatocellular carcinoma	99:122	Hepatocellular carcinoma (HCC)	99:128	Hepatocellular carcinoma (HCC) is a malignant tumor originating in the liver.
27060025	1	12	theme	Hepatocellular	99:112	arg1	tumor					145:149	a malignant tumor	133:149	a malignant tumor originating in the liver	133:174	Hepatocellular carcinoma (HCC) is a malignant tumor originating in the liver.
27060025	1	12	theme	Hepatocellular	99:112	arg1	HCC					125:127	HCC	125:127	HCC	125:127	Hepatocellular carcinoma (HCC) is a malignant tumor originating in the liver.
27060025	9	13	theme	HCC	1091:1093	arg1	development					1076:1086	development	1076:1086	development	1076:1086	E-cadherin level is highly up-regulated in HDAC1 O-GlcNAc mutant-treated liver cancer cells, which inhibit the occurrence and development of HCC.
27060025	9	13	theme	HCC	1091:1093	arg1	occurrence					1061:1070	occurrence	1061:1070	occurrence	1061:1070	E-cadherin level is highly up-regulated in HDAC1 O-GlcNAc mutant-treated liver cancer cells, which inhibit the occurrence and development of HCC.
27060025	3	14	theme	physical	366:373	arg1	link					375:378	the physical link	362:378	the physical link between OGT and HDAC1	362:400	In the present study, we investigated the physical link between OGT and HDAC1.
27060025	7	15	theme	HDAC1	659:663	arg1	mutants					674:680	HDAC1 O-GlcNAc mutants	659:680	HDAC1 O-GlcNAc mutants	659:680	HDAC1 O-GlcNAc mutants promote the p21 transcription regulation through affecting the acetylation levels of histones from chromosome, and then influence the proliferation of HCC cells.
27060025	7	16	theme	HCC	833:835	arg1	cells					837:841	HCC cells	833:841	HCC cells	833:841	HDAC1 O-GlcNAc mutants promote the p21 transcription regulation through affecting the acetylation levels of histones from chromosome, and then influence the proliferation of HCC cells.
27060025	7	17	theme	p21	694:696	arg1	regulation					712:721	the p21 transcription regulation	690:721	the p21 transcription regulation	690:721	HDAC1 O-GlcNAc mutants promote the p21 transcription regulation through affecting the acetylation levels of histones from chromosome, and then influence the proliferation of HCC cells.
27060025	0	18	theme	deacetylases	27:38	arg1	O-GlcNAcylation					0:14	O-GlcNAcylation	0:14	O-GlcNAcylation of histone deacetylases 1 in hepatocellular carcinoma	0:68	O-GlcNAcylation of histone deacetylases 1 in hepatocellular carcinoma promotes cancer progression.
27060025	11	19	theme	HDAC1	1237:1241	arg1	O-GlcNAcylation					1218:1232	inhibiting O-GlcNAcylation	1207:1232	inhibiting O-GlcNAcylation of HDAC1	1207:1241	Therefore, inhibiting O-GlcNAcylation of HDAC1 may repress the progression of HCC.
27060025	7	20	theme	cells	837:841	arg1	proliferation					816:828	the proliferation	812:828	the proliferation of HCC cells	812:841	HDAC1 O-GlcNAc mutants promote the p21 transcription regulation through affecting the acetylation levels of histones from chromosome, and then influence the proliferation of HCC cells.
27060025	0	21	theme	histone	19:25	arg1	deacetylases					27:38	histone deacetylases 1	19:40	histone deacetylases 1	19:40	O-GlcNAcylation of histone deacetylases 1 in hepatocellular carcinoma promotes cancer progression.
27060025	4	22	theme	HDAC1	426:430	arg1	O-GlcNAcylation					407:421	The O-GlcNAcylation	403:421	The O-GlcNAcylation of HDAC1	403:430	The O-GlcNAcylation of HDAC1 is overexpressed in HCC.
27060025	8	23	theme	HDAC1	898:902	arg1	HDAC1					898:902	HDAC1	898:902	HDAC1	898:902	We also found that mutants of O-GlcNAcylation site of HDAC1 affect invasion and migration of HepG2 cells.
27060025	8	23	theme	HDAC1	898:902	arg1	site					890:893	O-GlcNAcylation site	874:893	O-GlcNAcylation site of HDAC1	874:902	We also found that mutants of O-GlcNAcylation site of HDAC1 affect invasion and migration of HepG2 cells.
27060025	6	24	theme	HDAC1	551:555	arg1	O-GlcNAcylation					557:571	HDAC1 O-GlcNAcylation	551:571	HDAC1 O-GlcNAcylation	551:571	HDAC1 O-GlcNAcylation increases the activated phosphorylation of HDAC1, which enhances its enzyme activity.
27060025	2	25	theme	Previous	177:184	arg1	studies					186:192	Previous studies	177:192	Previous studies	177:192	Previous studies have indicated that O-GlcNAc transferase (OGT) and histone deacetylase-1 (HDAC1) play important roles in the pathogenesis of HCC.
27060025	8	26	theme	HepG2	937:941	arg1	cells					943:947	HepG2 cells	937:947	HepG2 cells	937:947	We also found that mutants of O-GlcNAcylation site of HDAC1 affect invasion and migration of HepG2 cells.
27060025	9	27	theme	HDAC1	993:997	arg1	cells					1036:1040	HDAC1 O-GlcNAc mutant-treated liver cancer cells	993:1040	HDAC1 O-GlcNAc mutant-treated liver cancer cells	993:1040	E-cadherin level is highly up-regulated in HDAC1 O-GlcNAc mutant-treated liver cancer cells, which inhibit the occurrence and development of HCC.
27060025	10	28	theme	HDAC1in	1164:1170	arg1	modification					1148:1159	the O-GlcNAc modification	1135:1159	the O-GlcNAc modification of HDAC1in	1135:1170	Our findings suggest that OGT promotes the O-GlcNAc modification of HDAC1in the development of HCC.
27060025	9	29	theme	mutant-treated	1008:1021	arg1	cells					1036:1040	HDAC1 O-GlcNAc mutant-treated liver cancer cells	993:1040	HDAC1 O-GlcNAc mutant-treated liver cancer cells	993:1040	E-cadherin level is highly up-regulated in HDAC1 O-GlcNAc mutant-treated liver cancer cells, which inhibit the occurrence and development of HCC.
27060025	5	30	theme	O-GlcNAcylation	500:514	arg1	sites					491:495	two major sites	481:495	two major sites of O-GlcNAcylation	481:514	We found that HDAC1 has two major sites of O-GlcNAcylation in its histone deacetylase domain.
27060025	5	30	theme	O-GlcNAcylation	500:514	arg1	O-GlcNAcylation					500:514	O-GlcNAcylation	500:514	O-GlcNAcylation	500:514	We found that HDAC1 has two major sites of O-GlcNAcylation in its histone deacetylase domain.
27060025	9	31	theme	E-cadherin	950:959	arg1	level					961:965	E-cadherin level	950:965	E-cadherin level	950:965	E-cadherin level is highly up-regulated in HDAC1 O-GlcNAc mutant-treated liver cancer cells, which inhibit the occurrence and development of HCC.
27060025	9	32	theme	O-GlcNAc	999:1006	arg1	cells					1036:1040	HDAC1 O-GlcNAc mutant-treated liver cancer cells	993:1040	HDAC1 O-GlcNAc mutant-treated liver cancer cells	993:1040	E-cadherin level is highly up-regulated in HDAC1 O-GlcNAc mutant-treated liver cancer cells, which inhibit the occurrence and development of HCC.
27060025	0	33	theme	hepatocellular	45:58	arg1	carcinoma					60:68	hepatocellular carcinoma	45:68	hepatocellular carcinoma	45:68	O-GlcNAcylation of histone deacetylases 1 in hepatocellular carcinoma promotes cancer progression.
27060025	7	34	theme	histones	767:774	arg1	levels					757:762	the acetylation levels	741:762	the acetylation levels of histones from chromosome	741:790	HDAC1 O-GlcNAc mutants promote the p21 transcription regulation through affecting the acetylation levels of histones from chromosome, and then influence the proliferation of HCC cells.
27060025	2	35	theme	O-GlcNAc	214:221	arg1	OGT					236:238	OGT	236:238	OGT	236:238	Previous studies have indicated that O-GlcNAc transferase (OGT) and histone deacetylase-1 (HDAC1) play important roles in the pathogenesis of HCC.
27060025	2	35	theme	O-GlcNAc	214:221	arg1	transferase					223:233	O-GlcNAc transferase	214:233	O-GlcNAc transferase (OGT)	214:239	Previous studies have indicated that O-GlcNAc transferase (OGT) and histone deacetylase-1 (HDAC1) play important roles in the pathogenesis of HCC.
27060025	11	36	theme	HCC	1274:1276	arg1	progression					1259:1269	the progression	1255:1269	the progression of HCC	1255:1276	Therefore, inhibiting O-GlcNAcylation of HDAC1 may repress the progression of HCC.
27060025	6	37	theme	enzyme	642:647	arg1	activity					649:656	its enzyme activity	638:656	its enzyme activity	638:656	HDAC1 O-GlcNAcylation increases the activated phosphorylation of HDAC1, which enhances its enzyme activity.
27060025	10	38	theme	O-GlcNAc	1139:1146	arg1	modification					1148:1159	the O-GlcNAc modification	1135:1159	the O-GlcNAc modification of HDAC1in	1135:1170	Our findings suggest that OGT promotes the O-GlcNAc modification of HDAC1in the development of HCC.
27060025	7	39	from	levels	757:762	arg1	chromosome					781:790	chromosome	781:790	chromosome	781:790	HDAC1 O-GlcNAc mutants promote the p21 transcription regulation through affecting the acetylation levels of histones from chromosome, and then influence the proliferation of HCC cells.
27060025	7	40	theme	O-GlcNAc	665:672	arg1	mutants					674:680	HDAC1 O-GlcNAc mutants	659:680	HDAC1 O-GlcNAc mutants	659:680	HDAC1 O-GlcNAc mutants promote the p21 transcription regulation through affecting the acetylation levels of histones from chromosome, and then influence the proliferation of HCC cells.
27060025	5	41	theme	histone	523:529	arg1	domain					543:548	its histone deacetylase domain	519:548	its histone deacetylase domain	519:548	We found that HDAC1 has two major sites of O-GlcNAcylation in its histone deacetylase domain.
27060025	2	42	theme	HCC	319:321	arg1	pathogenesis					303:314	the pathogenesis	299:314	the pathogenesis of HCC	299:321	Previous studies have indicated that O-GlcNAc transferase (OGT) and histone deacetylase-1 (HDAC1) play important roles in the pathogenesis of HCC.
27060025	9	43	theme	cancer	1029:1034	arg1	cells					1036:1040	HDAC1 O-GlcNAc mutant-treated liver cancer cells	993:1040	HDAC1 O-GlcNAc mutant-treated liver cancer cells	993:1040	E-cadherin level is highly up-regulated in HDAC1 O-GlcNAc mutant-treated liver cancer cells, which inhibit the occurrence and development of HCC.
27060025	10	44	theme	HCC	1191:1193	arg1	development					1176:1186	the development	1172:1186	the development of HCC	1172:1193	Our findings suggest that OGT promotes the O-GlcNAc modification of HDAC1in the development of HCC.
27060025	2	45	theme	important	280:288	arg1	roles					290:294	important roles	280:294	important roles	280:294	Previous studies have indicated that O-GlcNAc transferase (OGT) and histone deacetylase-1 (HDAC1) play important roles in the pathogenesis of HCC.
27060025	8	46	theme	cells	943:947	arg1	migration					924:932	migration	924:932	migration	924:932	We also found that mutants of O-GlcNAcylation site of HDAC1 affect invasion and migration of HepG2 cells.
27060025	8	46	theme	cells	943:947	arg1	invasion					911:918	invasion	911:918	invasion	911:918	We also found that mutants of O-GlcNAcylation site of HDAC1 affect invasion and migration of HepG2 cells.
27060025	1	47	theme	malignant	135:143	arg1	carcinoma					114:122	Hepatocellular carcinoma	99:122	Hepatocellular carcinoma (HCC)	99:128	Hepatocellular carcinoma (HCC) is a malignant tumor originating in the liver.
27060025	1	47	theme	malignant	135:143	arg1	tumor					145:149	a malignant tumor	133:149	a malignant tumor originating in the liver	133:174	Hepatocellular carcinoma (HCC) is a malignant tumor originating in the liver.
27060025	11	48	theme	inhibiting	1207:1216	arg1	O-GlcNAcylation					1218:1232	inhibiting O-GlcNAcylation	1207:1232	inhibiting O-GlcNAcylation of HDAC1	1207:1241	Therefore, inhibiting O-GlcNAcylation of HDAC1 may repress the progression of HCC.
27060025	0	49	theme	cancer	79:84	arg1	progression					86:96	cancer progression	79:96	cancer progression	79:96	O-GlcNAcylation of histone deacetylases 1 in hepatocellular carcinoma promotes cancer progression.
27060025	2	50	theme	histone	245:251	arg1	HDAC1					268:272	HDAC1	268:272	HDAC1	268:272	Previous studies have indicated that O-GlcNAc transferase (OGT) and histone deacetylase-1 (HDAC1) play important roles in the pathogenesis of HCC.
27060025	2	50	theme	histone	245:251	arg1	deacetylase-1					253:265	histone deacetylase-1	245:265	histone deacetylase-1 (HDAC1)	245:273	Previous studies have indicated that O-GlcNAc transferase (OGT) and histone deacetylase-1 (HDAC1) play important roles in the pathogenesis of HCC.
27060025	5	51	theme	major	485:489	arg1	sites					491:495	two major sites	481:495	two major sites of O-GlcNAcylation	481:514	We found that HDAC1 has two major sites of O-GlcNAcylation in its histone deacetylase domain.
27060025	5	51	theme	major	485:489	arg1	O-GlcNAcylation					500:514	O-GlcNAcylation	500:514	O-GlcNAcylation	500:514	We found that HDAC1 has two major sites of O-GlcNAcylation in its histone deacetylase domain.
27060025	8	52	theme	site	890:893	arg1	mutants					863:869	mutants	863:869	mutants of O-GlcNAcylation site of HDAC1	863:902	We also found that mutants of O-GlcNAcylation site of HDAC1 affect invasion and migration of HepG2 cells.
27060025	7	53	theme	acetylation	745:755	arg1	levels					757:762	the acetylation levels	741:762	the acetylation levels of histones from chromosome	741:790	HDAC1 O-GlcNAc mutants promote the p21 transcription regulation through affecting the acetylation levels of histones from chromosome, and then influence the proliferation of HCC cells.
27751836	0	0	theme	hepatocellular	96:109	arg1	carcinoma					111:119	hepatocellular carcinoma	96:119	hepatocellular carcinoma	96:119	Hyper-O-GlcNAcylation of YB-1 affects Ser102 phosphorylation and promotes cell proliferation in hepatocellular carcinoma.
27751836	7	1	theme	specific	1287:1294	arg1	sites					1305:1309	four specific O-GlcNAc sites	1282:1309	four specific O-GlcNAc sites	1282:1309	Moreover, we detected four specific O-GlcNAc sites and confirmed T126A to be the most effective mutant in HCC cell proliferation via close O-GlcNAcylation-phosphorylation interaction.
27751836	9	2	theme	indispensable	1791:1803	arg1	roles					1805:1809	indispensable roles	1791:1809	indispensable roles	1791:1809	From all above, it is not difficult to find that glycosylated-YB-1 mainly enhanced cell proliferation through congenerous actions with YB-1 phosphorylation and thus played indispensable roles in fine-tuning cell proliferation and procession of HCC.
27751836	7	3	theme	O-GlcNAc	1296:1303	arg1	sites					1305:1309	four specific O-GlcNAc sites	1282:1309	four specific O-GlcNAc sites	1282:1309	Moreover, we detected four specific O-GlcNAc sites and confirmed T126A to be the most effective mutant in HCC cell proliferation via close O-GlcNAcylation-phosphorylation interaction.
27751836	1	4	theme	cell	360:363	arg1	growth					365:370	cell growth	360:370	cell growth	360:370	As an essential post-translational modification, O-GlcNAcylation has been thought to be able to modulate various nuclear and cytoplasmic proteins and is emerging as a key regulator of multiple biological processes, such as transcription, cell growth, signal transduction, and cell motility.
27751836	4	5	theme	development	927:937	arg1	process					912:918	the process	908:918	the process of HCC development	908:937	Therefore, our study aimed to determine whether YB-1 was O-GlcNAc modified and whether such modification could interact with its phosphorylation during the process of HCC development.
27751836	6	6	theme	HCC	1209:1211	arg1	proliferation					1218:1230	HCC cell proliferation	1209:1230	HCC cell proliferation	1209:1230	What is more, not only YB-1 was identified to be O-GlcNAcylated but hyper-O-GlcNAcylation was demonstrated to facilitate HCC cell proliferation in a YB-1 dependent manner.
27751836	8	7	theme	YB-1	1563:1566	arg1	retardation					1511:1521	T126A-induced HCC cell retardation	1488:1521	T126A-induced HCC cell retardation	1488:1521	Even more interestingly, we discovered that T126A-induced HCC cell retardation and subdued transcriptional activity of YB-1 could be partially reversed by T126A/S102E mutant.
27751836	8	7	theme	YB-1	1563:1566	arg1	activity					1551:1558	subdued transcriptional activity	1527:1558	subdued transcriptional activity of YB-1	1527:1566	Even more interestingly, we discovered that T126A-induced HCC cell retardation and subdued transcriptional activity of YB-1 could be partially reversed by T126A/S102E mutant.
27751836	5	8	theme	HCC	1075:1077	arg1	tissues					1079:1085	HCC tissues	1075:1085	HCC tissues	1075:1085	Western blot and immunohistochemistry were firstly conducted to reveal obvious up-regulation of YB-1, OGT and O-GlcNAc modification in HCC tissues.
27751836	2	9	theme	cellular	635:642	arg1	processes					644:652	other cellular processes	629:652	other cellular processes	629:652	Recently, authoritative glycomics analyses have reported extensive crosstalk between O-GlcNAcylation and phosphorylation, which always dynamically interplay with each other and regulate signaling, transcription, and other cellular processes.
27751836	5	10	theme	OGT	1042:1044	arg1	up-regulation					1019:1031	obvious up-regulation	1011:1031	obvious up-regulation of YB-1, OGT and O-GlcNAc modification in HCC tissues	1011:1085	Western blot and immunohistochemistry were firstly conducted to reveal obvious up-regulation of YB-1, OGT and O-GlcNAc modification in HCC tissues.
27751836	2	11	theme	other	629:633	arg1	processes					644:652	other cellular processes	629:652	other cellular processes	629:652	Recently, authoritative glycomics analyses have reported extensive crosstalk between O-GlcNAcylation and phosphorylation, which always dynamically interplay with each other and regulate signaling, transcription, and other cellular processes.
27751836	9	12	from	above	1628:1632	arg1	difficult					1645:1653	difficult	1645:1653	difficult	1645:1653	From all above, it is not difficult to find that glycosylated-YB-1 mainly enhanced cell proliferation through congenerous actions with YB-1 phosphorylation and thus played indispensable roles in fine-tuning cell proliferation and procession of HCC.
27751836	1	13	theme	key	289:291	arg1	regulator					293:301	a key regulator	287:301	a key regulator of multiple biological processes, such as transcription, cell growth, signal transduction, and cell motility	287:410	As an essential post-translational modification, O-GlcNAcylation has been thought to be able to modulate various nuclear and cytoplasmic proteins and is emerging as a key regulator of multiple biological processes, such as transcription, cell growth, signal transduction, and cell motility.
27751836	1	14	theme	signal	373:378	arg1	transduction					380:391	signal transduction	373:391	signal transduction	373:391	As an essential post-translational modification, O-GlcNAcylation has been thought to be able to modulate various nuclear and cytoplasmic proteins and is emerging as a key regulator of multiple biological processes, such as transcription, cell growth, signal transduction, and cell motility.
27751836	9	15	with	actions	1741:1747	arg1	phosphorylation					1759:1773	YB-1 phosphorylation	1754:1773	YB-1 phosphorylation	1754:1773	From all above, it is not difficult to find that glycosylated-YB-1 mainly enhanced cell proliferation through congenerous actions with YB-1 phosphorylation and thus played indispensable roles in fine-tuning cell proliferation and procession of HCC.
27751836	2	16	theme	authoritative	423:435	arg1	analyses					447:454	authoritative glycomics analyses	423:454	authoritative glycomics analyses	423:454	Recently, authoritative glycomics analyses have reported extensive crosstalk between O-GlcNAcylation and phosphorylation, which always dynamically interplay with each other and regulate signaling, transcription, and other cellular processes.
27751836	5	17	theme	O-GlcNAc	1050:1057	arg1	modification					1059:1070	O-GlcNAc modification	1050:1070	O-GlcNAc modification	1050:1070	Western blot and immunohistochemistry were firstly conducted to reveal obvious up-regulation of YB-1, OGT and O-GlcNAc modification in HCC tissues.
27751836	7	18	theme	O-GlcNAcylation-phosphorylation	1399:1429	arg1	interaction					1431:1441	close O-GlcNAcylation-phosphorylation interaction	1393:1441	close O-GlcNAcylation-phosphorylation interaction	1393:1441	Moreover, we detected four specific O-GlcNAc sites and confirmed T126A to be the most effective mutant in HCC cell proliferation via close O-GlcNAcylation-phosphorylation interaction.
27751836	2	19	with	interplay	560:568	arg1	other					580:584	other	580:584	other	580:584	Recently, authoritative glycomics analyses have reported extensive crosstalk between O-GlcNAcylation and phosphorylation, which always dynamically interplay with each other and regulate signaling, transcription, and other cellular processes.
27751836	5	20	theme	modification	1059:1070	arg1	up-regulation					1019:1031	obvious up-regulation	1011:1031	obvious up-regulation of YB-1, OGT and O-GlcNAc modification in HCC tissues	1011:1085	Western blot and immunohistochemistry were firstly conducted to reveal obvious up-regulation of YB-1, OGT and O-GlcNAc modification in HCC tissues.
27751836	2	21	theme	extensive	470:478	arg1	crosstalk					480:488	extensive crosstalk	470:488	extensive crosstalk	470:488	Recently, authoritative glycomics analyses have reported extensive crosstalk between O-GlcNAcylation and phosphorylation, which always dynamically interplay with each other and regulate signaling, transcription, and other cellular processes.
27751836	6	22	dep	more	1096:1099	arg1	only					1106:1109	only	1106:1109	only	1106:1109	What is more, not only YB-1 was identified to be O-GlcNAcylated but hyper-O-GlcNAcylation was demonstrated to facilitate HCC cell proliferation in a YB-1 dependent manner.
27751836	4	23	theme	HCC	923:925	arg1	development					927:937	HCC development	923:937	HCC development	923:937	Therefore, our study aimed to determine whether YB-1 was O-GlcNAc modified and whether such modification could interact with its phosphorylation during the process of HCC development.
27751836	5	24	theme	Western	940:946	arg1	blot					948:951	Western blot	940:951	Western blot	940:951	Western blot and immunohistochemistry were firstly conducted to reveal obvious up-regulation of YB-1, OGT and O-GlcNAc modification in HCC tissues.
27751836	6	25	theme	cell	1213:1216	arg1	proliferation					1218:1230	HCC cell proliferation	1209:1230	HCC cell proliferation	1209:1230	What is more, not only YB-1 was identified to be O-GlcNAcylated but hyper-O-GlcNAcylation was demonstrated to facilitate HCC cell proliferation in a YB-1 dependent manner.
27751836	7	26	theme	close	1393:1397	arg1	interaction					1431:1441	close O-GlcNAcylation-phosphorylation interaction	1393:1441	close O-GlcNAcylation-phosphorylation interaction	1393:1441	Moreover, we detected four specific O-GlcNAc sites and confirmed T126A to be the most effective mutant in HCC cell proliferation via close O-GlcNAcylation-phosphorylation interaction.
27751836	7	27	from	mutant	1356:1361	arg1	proliferation					1375:1387	HCC cell proliferation	1366:1387	HCC cell proliferation	1366:1387	Moreover, we detected four specific O-GlcNAc sites and confirmed T126A to be the most effective mutant in HCC cell proliferation via close O-GlcNAcylation-phosphorylation interaction.
27751836	5	28	theme	YB-1	1036:1039	arg1	up-regulation					1019:1031	obvious up-regulation	1011:1031	obvious up-regulation of YB-1, OGT and O-GlcNAc modification in HCC tissues	1011:1085	Western blot and immunohistochemistry were firstly conducted to reveal obvious up-regulation of YB-1, OGT and O-GlcNAc modification in HCC tissues.
27751836	8	29	theme	HCC	1502:1504	arg1	retardation					1511:1521	T126A-induced HCC cell retardation	1488:1521	T126A-induced HCC cell retardation	1488:1521	Even more interestingly, we discovered that T126A-induced HCC cell retardation and subdued transcriptional activity of YB-1 could be partially reversed by T126A/S102E mutant.
27751836	2	30	theme	glycomics	437:445	arg1	analyses					447:454	authoritative glycomics analyses	423:454	authoritative glycomics analyses	423:454	Recently, authoritative glycomics analyses have reported extensive crosstalk between O-GlcNAcylation and phosphorylation, which always dynamically interplay with each other and regulate signaling, transcription, and other cellular processes.
27751836	0	31	theme	YB-1	25:28	arg1	Hyper-O-GlcNAcylation					0:20	Hyper-O-GlcNAcylation	0:20	Hyper-O-GlcNAcylation of YB-1	0:28	Hyper-O-GlcNAcylation of YB-1 affects Ser102 phosphorylation and promotes cell proliferation in hepatocellular carcinoma.
27751836	1	32	theme	multiple	306:313	arg1	motility					403:410	cell motility	398:410	cell motility	398:410	As an essential post-translational modification, O-GlcNAcylation has been thought to be able to modulate various nuclear and cytoplasmic proteins and is emerging as a key regulator of multiple biological processes, such as transcription, cell growth, signal transduction, and cell motility.
27751836	1	32	theme	multiple	306:313	arg1	transcription					345:357	transcription	345:357	transcription	345:357	As an essential post-translational modification, O-GlcNAcylation has been thought to be able to modulate various nuclear and cytoplasmic proteins and is emerging as a key regulator of multiple biological processes, such as transcription, cell growth, signal transduction, and cell motility.
27751836	1	32	theme	multiple	306:313	arg1	growth					365:370	cell growth	360:370	cell growth	360:370	As an essential post-translational modification, O-GlcNAcylation has been thought to be able to modulate various nuclear and cytoplasmic proteins and is emerging as a key regulator of multiple biological processes, such as transcription, cell growth, signal transduction, and cell motility.
27751836	1	32	theme	multiple	306:313	arg1	transduction					380:391	signal transduction	373:391	signal transduction	373:391	As an essential post-translational modification, O-GlcNAcylation has been thought to be able to modulate various nuclear and cytoplasmic proteins and is emerging as a key regulator of multiple biological processes, such as transcription, cell growth, signal transduction, and cell motility.
27751836	1	32	theme	multiple	306:313	arg1	processes					326:334	multiple biological processes	306:334	multiple biological processes	306:334	As an essential post-translational modification, O-GlcNAcylation has been thought to be able to modulate various nuclear and cytoplasmic proteins and is emerging as a key regulator of multiple biological processes, such as transcription, cell growth, signal transduction, and cell motility.
27751836	3	33	theme	close	690:694	arg1	correlation					696:706	close correlation	690:706	close correlation between YB-1 phosphorylation and tumorigenesis	690:753	Also, plentiful studies have shown close correlation between YB-1 phosphorylation and tumorigenesis.
27751836	1	34	theme	various	227:233	arg1	proteins					259:266	various nuclear and cytoplasmic proteins	227:266	various nuclear and cytoplasmic proteins	227:266	As an essential post-translational modification, O-GlcNAcylation has been thought to be able to modulate various nuclear and cytoplasmic proteins and is emerging as a key regulator of multiple biological processes, such as transcription, cell growth, signal transduction, and cell motility.
27751836	1	35	theme	biological	315:324	arg1	motility					403:410	cell motility	398:410	cell motility	398:410	As an essential post-translational modification, O-GlcNAcylation has been thought to be able to modulate various nuclear and cytoplasmic proteins and is emerging as a key regulator of multiple biological processes, such as transcription, cell growth, signal transduction, and cell motility.
27751836	1	35	theme	biological	315:324	arg1	transcription					345:357	transcription	345:357	transcription	345:357	As an essential post-translational modification, O-GlcNAcylation has been thought to be able to modulate various nuclear and cytoplasmic proteins and is emerging as a key regulator of multiple biological processes, such as transcription, cell growth, signal transduction, and cell motility.
27751836	1	35	theme	biological	315:324	arg1	growth					365:370	cell growth	360:370	cell growth	360:370	As an essential post-translational modification, O-GlcNAcylation has been thought to be able to modulate various nuclear and cytoplasmic proteins and is emerging as a key regulator of multiple biological processes, such as transcription, cell growth, signal transduction, and cell motility.
27751836	1	35	theme	biological	315:324	arg1	transduction					380:391	signal transduction	373:391	signal transduction	373:391	As an essential post-translational modification, O-GlcNAcylation has been thought to be able to modulate various nuclear and cytoplasmic proteins and is emerging as a key regulator of multiple biological processes, such as transcription, cell growth, signal transduction, and cell motility.
27751836	1	35	theme	biological	315:324	arg1	processes					326:334	multiple biological processes	306:334	multiple biological processes	306:334	As an essential post-translational modification, O-GlcNAcylation has been thought to be able to modulate various nuclear and cytoplasmic proteins and is emerging as a key regulator of multiple biological processes, such as transcription, cell growth, signal transduction, and cell motility.
27751836	9	36	theme	cell	1826:1829	arg1	proliferation					1831:1843	cell proliferation	1826:1843	cell proliferation	1826:1843	From all above, it is not difficult to find that glycosylated-YB-1 mainly enhanced cell proliferation through congenerous actions with YB-1 phosphorylation and thus played indispensable roles in fine-tuning cell proliferation and procession of HCC.
27751836	1	37	theme	cell	398:401	arg1	motility					403:410	cell motility	398:410	cell motility	398:410	As an essential post-translational modification, O-GlcNAcylation has been thought to be able to modulate various nuclear and cytoplasmic proteins and is emerging as a key regulator of multiple biological processes, such as transcription, cell growth, signal transduction, and cell motility.
27751836	1	38	dep	able	210:213	arg1	modulate					218:225	modulate	218:225	to modulate various nuclear and cytoplasmic proteins	215:266	As an essential post-translational modification, O-GlcNAcylation has been thought to be able to modulate various nuclear and cytoplasmic proteins and is emerging as a key regulator of multiple biological processes, such as transcription, cell growth, signal transduction, and cell motility.
27751836	1	38	dep	able	210:213	arg1	emerging					275:282	emerging	275:282	is emerging as a key regulator of multiple biological processes, such as transcription, cell growth, signal transduction, and cell motility	272:410	As an essential post-translational modification, O-GlcNAcylation has been thought to be able to modulate various nuclear and cytoplasmic proteins and is emerging as a key regulator of multiple biological processes, such as transcription, cell growth, signal transduction, and cell motility.
27751836	1	39	theme	nuclear	235:241	arg1	proteins					259:266	various nuclear and cytoplasmic proteins	227:266	various nuclear and cytoplasmic proteins	227:266	As an essential post-translational modification, O-GlcNAcylation has been thought to be able to modulate various nuclear and cytoplasmic proteins and is emerging as a key regulator of multiple biological processes, such as transcription, cell growth, signal transduction, and cell motility.
27751836	0	40	theme	Ser102	38:43	arg1	phosphorylation					45:59	Ser102 phosphorylation	38:59	Ser102 phosphorylation	38:59	Hyper-O-GlcNAcylation of YB-1 affects Ser102 phosphorylation and promotes cell proliferation in hepatocellular carcinoma.
27751836	1	41	theme	processes	326:334	arg1	regulator					293:301	a key regulator	287:301	a key regulator of multiple biological processes, such as transcription, cell growth, signal transduction, and cell motility	287:410	As an essential post-translational modification, O-GlcNAcylation has been thought to be able to modulate various nuclear and cytoplasmic proteins and is emerging as a key regulator of multiple biological processes, such as transcription, cell growth, signal transduction, and cell motility.
27751836	0	42	from	proliferation	79:91	arg1	carcinoma					111:119	hepatocellular carcinoma	96:119	hepatocellular carcinoma	96:119	Hyper-O-GlcNAcylation of YB-1 affects Ser102 phosphorylation and promotes cell proliferation in hepatocellular carcinoma.
27751836	8	43	theme	T126A-induced	1488:1500	arg1	retardation					1511:1521	T126A-induced HCC cell retardation	1488:1521	T126A-induced HCC cell retardation	1488:1521	Even more interestingly, we discovered that T126A-induced HCC cell retardation and subdued transcriptional activity of YB-1 could be partially reversed by T126A/S102E mutant.
27751836	7	44	theme	HCC	1366:1368	arg1	proliferation					1375:1387	HCC cell proliferation	1366:1387	HCC cell proliferation	1366:1387	Moreover, we detected four specific O-GlcNAc sites and confirmed T126A to be the most effective mutant in HCC cell proliferation via close O-GlcNAcylation-phosphorylation interaction.
27751836	9	45	theme	HCC	1863:1865	arg1	procession					1849:1858	procession	1849:1858	procession	1849:1858	From all above, it is not difficult to find that glycosylated-YB-1 mainly enhanced cell proliferation through congenerous actions with YB-1 phosphorylation and thus played indispensable roles in fine-tuning cell proliferation and procession of HCC.
27751836	9	45	theme	HCC	1863:1865	arg1	proliferation					1831:1843	cell proliferation	1826:1843	cell proliferation	1826:1843	From all above, it is not difficult to find that glycosylated-YB-1 mainly enhanced cell proliferation through congenerous actions with YB-1 phosphorylation and thus played indispensable roles in fine-tuning cell proliferation and procession of HCC.
27751836	1	46	theme	essential	128:136	arg1	modification					157:168	an essential post-translational modification	125:168	an essential post-translational modification	125:168	As an essential post-translational modification, O-GlcNAcylation has been thought to be able to modulate various nuclear and cytoplasmic proteins and is emerging as a key regulator of multiple biological processes, such as transcription, cell growth, signal transduction, and cell motility.
27751836	1	46	theme	essential	128:136	arg1	O-GlcNAcylation					171:185	O-GlcNAcylation	171:185	O-GlcNAcylation	171:185	As an essential post-translational modification, O-GlcNAcylation has been thought to be able to modulate various nuclear and cytoplasmic proteins and is emerging as a key regulator of multiple biological processes, such as transcription, cell growth, signal transduction, and cell motility.
27751836	8	47	theme	cell	1506:1509	arg1	retardation					1511:1521	T126A-induced HCC cell retardation	1488:1521	T126A-induced HCC cell retardation	1488:1521	Even more interestingly, we discovered that T126A-induced HCC cell retardation and subdued transcriptional activity of YB-1 could be partially reversed by T126A/S102E mutant.
27751836	7	48	theme	effective	1346:1354	arg1	mutant					1356:1361	the most effective mutant	1337:1361	the most effective mutant in HCC cell proliferation	1337:1387	Moreover, we detected four specific O-GlcNAc sites and confirmed T126A to be the most effective mutant in HCC cell proliferation via close O-GlcNAcylation-phosphorylation interaction.
27751836	1	49	theme	post-translational	138:155	arg1	modification					157:168	an essential post-translational modification	125:168	an essential post-translational modification	125:168	As an essential post-translational modification, O-GlcNAcylation has been thought to be able to modulate various nuclear and cytoplasmic proteins and is emerging as a key regulator of multiple biological processes, such as transcription, cell growth, signal transduction, and cell motility.
27751836	1	49	theme	post-translational	138:155	arg1	O-GlcNAcylation					171:185	O-GlcNAcylation	171:185	O-GlcNAcylation	171:185	As an essential post-translational modification, O-GlcNAcylation has been thought to be able to modulate various nuclear and cytoplasmic proteins and is emerging as a key regulator of multiple biological processes, such as transcription, cell growth, signal transduction, and cell motility.
27751836	8	50	theme	subdued	1527:1533	arg1	activity					1551:1558	subdued transcriptional activity	1527:1558	subdued transcriptional activity of YB-1	1527:1566	Even more interestingly, we discovered that T126A-induced HCC cell retardation and subdued transcriptional activity of YB-1 could be partially reversed by T126A/S102E mutant.
27751836	3	51	theme	plentiful	661:669	arg1	studies					671:677	plentiful studies	661:677	plentiful studies	661:677	Also, plentiful studies have shown close correlation between YB-1 phosphorylation and tumorigenesis.
27751836	1	52	theme	cytoplasmic	247:257	arg1	proteins					259:266	various nuclear and cytoplasmic proteins	227:266	various nuclear and cytoplasmic proteins	227:266	As an essential post-translational modification, O-GlcNAcylation has been thought to be able to modulate various nuclear and cytoplasmic proteins and is emerging as a key regulator of multiple biological processes, such as transcription, cell growth, signal transduction, and cell motility.
27751836	6	53	theme	dependent	1242:1250	arg1	manner					1252:1257	a YB-1 dependent manner	1235:1257	a YB-1 dependent manner	1235:1257	What is more, not only YB-1 was identified to be O-GlcNAcylated but hyper-O-GlcNAcylation was demonstrated to facilitate HCC cell proliferation in a YB-1 dependent manner.
27751836	8	54	theme	T126A/S102E	1599:1609	arg1	mutant					1611:1616	T126A/S102E mutant	1599:1616	T126A/S102E mutant	1599:1616	Even more interestingly, we discovered that T126A-induced HCC cell retardation and subdued transcriptional activity of YB-1 could be partially reversed by T126A/S102E mutant.
27751836	4	55	theme	such	843:846	arg1	modification					848:859	such modification	843:859	such modification	843:859	Therefore, our study aimed to determine whether YB-1 was O-GlcNAc modified and whether such modification could interact with its phosphorylation during the process of HCC development.
27751836	5	56	theme	obvious	1011:1017	arg1	up-regulation					1019:1031	obvious up-regulation	1011:1031	obvious up-regulation of YB-1, OGT and O-GlcNAc modification in HCC tissues	1011:1085	Western blot and immunohistochemistry were firstly conducted to reveal obvious up-regulation of YB-1, OGT and O-GlcNAc modification in HCC tissues.
27751836	5	57	from	up-regulation	1019:1031	arg1	tissues					1079:1085	HCC tissues	1075:1085	HCC tissues	1075:1085	Western blot and immunohistochemistry were firstly conducted to reveal obvious up-regulation of YB-1, OGT and O-GlcNAc modification in HCC tissues.
27751836	3	58	theme	YB-1	716:719	arg1	phosphorylation					721:735	YB-1 phosphorylation	716:735	YB-1 phosphorylation	716:735	Also, plentiful studies have shown close correlation between YB-1 phosphorylation and tumorigenesis.
27751836	9	59	theme	YB-1	1754:1757	arg1	phosphorylation					1759:1773	YB-1 phosphorylation	1754:1773	YB-1 phosphorylation	1754:1773	From all above, it is not difficult to find that glycosylated-YB-1 mainly enhanced cell proliferation through congenerous actions with YB-1 phosphorylation and thus played indispensable roles in fine-tuning cell proliferation and procession of HCC.
27751836	7	60	theme	cell	1370:1373	arg1	proliferation					1375:1387	HCC cell proliferation	1366:1387	HCC cell proliferation	1366:1387	Moreover, we detected four specific O-GlcNAc sites and confirmed T126A to be the most effective mutant in HCC cell proliferation via close O-GlcNAcylation-phosphorylation interaction.
27751836	9	61	theme	cell	1702:1705	arg1	proliferation					1707:1719	cell proliferation	1702:1719	cell proliferation	1702:1719	From all above, it is not difficult to find that glycosylated-YB-1 mainly enhanced cell proliferation through congenerous actions with YB-1 phosphorylation and thus played indispensable roles in fine-tuning cell proliferation and procession of HCC.
27751836	0	62	theme	cell	74:77	arg1	proliferation					79:91	cell proliferation	74:91	cell proliferation in hepatocellular carcinoma	74:119	Hyper-O-GlcNAcylation of YB-1 affects Ser102 phosphorylation and promotes cell proliferation in hepatocellular carcinoma.
27751836	8	63	theme	transcriptional	1535:1549	arg1	activity					1551:1558	subdued transcriptional activity	1527:1558	subdued transcriptional activity of YB-1	1527:1566	Even more interestingly, we discovered that T126A-induced HCC cell retardation and subdued transcriptional activity of YB-1 could be partially reversed by T126A/S102E mutant.
27751836	9	64	theme	congenerous	1729:1739	arg1	actions					1741:1747	congenerous actions	1729:1747	congenerous actions with YB-1 phosphorylation	1729:1773	From all above, it is not difficult to find that glycosylated-YB-1 mainly enhanced cell proliferation through congenerous actions with YB-1 phosphorylation and thus played indispensable roles in fine-tuning cell proliferation and procession of HCC.
20665223	2	0	from	outgrowth	422:430	arg1	line					458:461	the MN9D neuronal cell line	435:461	the MN9D neuronal cell line	435:461	Here, we found that the O-GlcNAc modification pattern was altered during all-trans retinoic acid (tRA)-induced neurite outgrowth in the MN9D neuronal cell line.
20665223	3	1	theme	mass	516:519	arg1	analysis					535:542	mass spectrometric analysis	516:542	mass spectrometric analysis	516:542	We identified several O-GlcNAcylated proteins using mass spectrometric analysis, including α- and β-tubulin.
20665223	3	2	theme	spectrometric	521:533	arg1	analysis					535:542	mass spectrometric analysis	516:542	mass spectrometric analysis	516:542	We identified several O-GlcNAcylated proteins using mass spectrometric analysis, including α- and β-tubulin.
20665223	4	3	theme	α-	593:594	arg1	analysis					581:588	Further analysis	573:588	Further analysis of α- and β-tubulin	573:608	Further analysis of α- and β-tubulin revealed that O-GlcNAcylated peptides mapped between residues 173 and 185 of α-tubulin and between residues 216 and 238 of β-tubulin, respectively.
20665223	1	4	link	O-linked	74:81	arg1	O-GlcNAc					106:113	O-GlcNAc	106:113	O-GlcNAc	106:113	The attachment of O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins is an abundant and reversible modification that involves many cellular processes including transcription, translation, cell proliferation, apoptosis, and signal transduction.
20665223	1	4	link	O-linked	74:81	arg1	β-N-acetylglucosamine					83:103	O-linked β-N-acetylglucosamine	74:103	O-linked β-N-acetylglucosamine (O-GlcNAc)	74:114	The attachment of O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins is an abundant and reversible modification that involves many cellular processes including transcription, translation, cell proliferation, apoptosis, and signal transduction.
20665223	2	5	theme	O-GlcNAc	327:334	arg1	pattern					349:355	the O-GlcNAc modification pattern	323:355	the O-GlcNAc modification pattern	323:355	Here, we found that the O-GlcNAc modification pattern was altered during all-trans retinoic acid (tRA)-induced neurite outgrowth in the MN9D neuronal cell line.
20665223	7	6	theme	microtubule	1135:1145	arg1	formation					1147:1155	microtubule formation	1135:1155	microtubule formation	1135:1155	Thus, our data indicate that the O-GlcNAcylation of tubulin negatively regulates microtubule formation.
20665223	1	7	theme	O-linked	74:81	arg1	O-GlcNAc					106:113	O-GlcNAc	106:113	O-GlcNAc	106:113	The attachment of O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins is an abundant and reversible modification that involves many cellular processes including transcription, translation, cell proliferation, apoptosis, and signal transduction.
20665223	1	7	theme	O-linked	74:81	arg1	β-N-acetylglucosamine					83:103	O-linked β-N-acetylglucosamine	74:103	O-linked β-N-acetylglucosamine (O-GlcNAc)	74:114	The attachment of O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins is an abundant and reversible modification that involves many cellular processes including transcription, translation, cell proliferation, apoptosis, and signal transduction.
20665223	1	8	theme	signal	282:287	arg1	transduction					289:300	signal transduction	282:300	signal transduction	282:300	The attachment of O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins is an abundant and reversible modification that involves many cellular processes including transcription, translation, cell proliferation, apoptosis, and signal transduction.
20665223	6	9	theme	O-GlcNAcase	929:939	arg1	inhibitors					941:950	O-GlcNAcase inhibitors	929:950	O-GlcNAcase inhibitors	929:950	Consequently, when O-GlcNAcase inhibitors were co-incubated with tRA, the extent of neurite outgrowth was decreased by 20% compared to control.
20665223	1	10	theme	β-N-acetylglucosamine	83:103	arg1	attachment					60:69	The attachment	56:69	The attachment of O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins	56:126	The attachment of O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins is an abundant and reversible modification that involves many cellular processes including transcription, translation, cell proliferation, apoptosis, and signal transduction.
20665223	1	10	theme	β-N-acetylglucosamine	83:103	arg1	modification					158:169	an abundant and reversible modification	131:169	an abundant and reversible modification that involves many cellular processes including transcription, translation, cell proliferation, apoptosis, and signal transduction	131:300	The attachment of O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins is an abundant and reversible modification that involves many cellular processes including transcription, translation, cell proliferation, apoptosis, and signal transduction.
20665223	1	11	theme	many	185:188	arg1	processes					199:207	many cellular processes	185:207	many cellular processes including transcription, translation, cell proliferation, apoptosis, and signal transduction	185:300	The attachment of O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins is an abundant and reversible modification that involves many cellular processes including transcription, translation, cell proliferation, apoptosis, and signal transduction.
20665223	1	11	theme	many	185:188	arg1	proliferation					252:264	cell proliferation	247:264	cell proliferation	247:264	The attachment of O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins is an abundant and reversible modification that involves many cellular processes including transcription, translation, cell proliferation, apoptosis, and signal transduction.
20665223	1	11	theme	many	185:188	arg1	transduction					289:300	signal transduction	282:300	signal transduction	282:300	The attachment of O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins is an abundant and reversible modification that involves many cellular processes including transcription, translation, cell proliferation, apoptosis, and signal transduction.
20665223	1	11	theme	many	185:188	arg1	transcription					219:231	transcription	219:231	transcription	219:231	The attachment of O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins is an abundant and reversible modification that involves many cellular processes including transcription, translation, cell proliferation, apoptosis, and signal transduction.
20665223	1	11	theme	many	185:188	arg1	apoptosis					267:275	apoptosis	267:275	apoptosis	267:275	The attachment of O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins is an abundant and reversible modification that involves many cellular processes including transcription, translation, cell proliferation, apoptosis, and signal transduction.
20665223	1	11	theme	many	185:188	arg1	translation					234:244	translation	234:244	translation	234:244	The attachment of O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins is an abundant and reversible modification that involves many cellular processes including transcription, translation, cell proliferation, apoptosis, and signal transduction.
20665223	2	12	theme	cell	453:456	arg1	line					458:461	the MN9D neuronal cell line	435:461	the MN9D neuronal cell line	435:461	Here, we found that the O-GlcNAc modification pattern was altered during all-trans retinoic acid (tRA)-induced neurite outgrowth in the MN9D neuronal cell line.
20665223	1	13	theme	cellular	190:197	arg1	processes					199:207	many cellular processes	185:207	many cellular processes including transcription, translation, cell proliferation, apoptosis, and signal transduction	185:300	The attachment of O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins is an abundant and reversible modification that involves many cellular processes including transcription, translation, cell proliferation, apoptosis, and signal transduction.
20665223	1	13	theme	cellular	190:197	arg1	proliferation					252:264	cell proliferation	247:264	cell proliferation	247:264	The attachment of O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins is an abundant and reversible modification that involves many cellular processes including transcription, translation, cell proliferation, apoptosis, and signal transduction.
20665223	1	13	theme	cellular	190:197	arg1	transduction					289:300	signal transduction	282:300	signal transduction	282:300	The attachment of O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins is an abundant and reversible modification that involves many cellular processes including transcription, translation, cell proliferation, apoptosis, and signal transduction.
20665223	1	13	theme	cellular	190:197	arg1	transcription					219:231	transcription	219:231	transcription	219:231	The attachment of O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins is an abundant and reversible modification that involves many cellular processes including transcription, translation, cell proliferation, apoptosis, and signal transduction.
20665223	1	13	theme	cellular	190:197	arg1	apoptosis					267:275	apoptosis	267:275	apoptosis	267:275	The attachment of O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins is an abundant and reversible modification that involves many cellular processes including transcription, translation, cell proliferation, apoptosis, and signal transduction.
20665223	1	13	theme	cellular	190:197	arg1	translation					234:244	translation	234:244	translation	234:244	The attachment of O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins is an abundant and reversible modification that involves many cellular processes including transcription, translation, cell proliferation, apoptosis, and signal transduction.
20665223	2	14	theme	neuronal	444:451	arg1	line					458:461	the MN9D neuronal cell line	435:461	the MN9D neuronal cell line	435:461	Here, we found that the O-GlcNAc modification pattern was altered during all-trans retinoic acid (tRA)-induced neurite outgrowth in the MN9D neuronal cell line.
20665223	4	15	theme	Further	573:579	arg1	analysis					581:588	Further analysis	573:588	Further analysis of α- and β-tubulin	573:608	Further analysis of α- and β-tubulin revealed that O-GlcNAcylated peptides mapped between residues 173 and 185 of α-tubulin and between residues 216 and 238 of β-tubulin, respectively.
20665223	4	16	theme	β-tubulin	733:741	arg1	β-tubulin					733:741	β-tubulin	733:741	β-tubulin	733:741	Further analysis of α- and β-tubulin revealed that O-GlcNAcylated peptides mapped between residues 173 and 185 of α-tubulin and between residues 216 and 238 of β-tubulin, respectively.
20665223	4	16	theme	β-tubulin	733:741	arg1	residues					709:716	residues 216 and 238	709:728	residues	709:716	Further analysis of α- and β-tubulin revealed that O-GlcNAcylated peptides mapped between residues 173 and 185 of α-tubulin and between residues 216 and 238 of β-tubulin, respectively.
20665223	4	17	theme	α-tubulin	687:695	arg1	α-tubulin					687:695	α-tubulin	687:695	α-tubulin	687:695	Further analysis of α- and β-tubulin revealed that O-GlcNAcylated peptides mapped between residues 173 and 185 of α-tubulin and between residues 216 and 238 of β-tubulin, respectively.
20665223	4	17	theme	α-tubulin	687:695	arg1	residues					663:670	residues 173 and 185	663:682	residues	663:670	Further analysis of α- and β-tubulin revealed that O-GlcNAcylated peptides mapped between residues 173 and 185 of α-tubulin and between residues 216 and 238 of β-tubulin, respectively.
20665223	2	18	theme	MN9D	439:442	arg1	line					458:461	the MN9D neuronal cell line	435:461	the MN9D neuronal cell line	435:461	Here, we found that the O-GlcNAc modification pattern was altered during all-trans retinoic acid (tRA)-induced neurite outgrowth in the MN9D neuronal cell line.
20665223	1	19	attach	attachment	60:69	arg1	proteins					119:126	proteins	119:126	proteins	119:126	The attachment of O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins is an abundant and reversible modification that involves many cellular processes including transcription, translation, cell proliferation, apoptosis, and signal transduction.
20665223	1	19	attach	attachment	60:69	arg2	β-N-acetylglucosamine					83:103	O-linked β-N-acetylglucosamine	74:103	O-linked β-N-acetylglucosamine (O-GlcNAc)	74:114	The attachment of O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins is an abundant and reversible modification that involves many cellular processes including transcription, translation, cell proliferation, apoptosis, and signal transduction.
20665223	1	19	attach	attachment	60:69	arg2	O-GlcNAc					106:113	O-GlcNAc	106:113	O-GlcNAc	106:113	The attachment of O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins is an abundant and reversible modification that involves many cellular processes including transcription, translation, cell proliferation, apoptosis, and signal transduction.
20665223	0	20	theme	tubulin	19:25	arg1	O-GlcNAcylation					0:14	O-GlcNAcylation	0:14	O-GlcNAcylation of tubulin	0:25	O-GlcNAcylation of tubulin inhibits its polymerization.
20665223	7	21	theme	tubulin	1106:1112	arg1	O-GlcNAcylation					1087:1101	the O-GlcNAcylation	1083:1101	the O-GlcNAcylation of tubulin	1083:1112	Thus, our data indicate that the O-GlcNAcylation of tubulin negatively regulates microtubule formation.
20665223	5	22	theme	α-tubulin	787:795	arg1	O-GlcNAcylation					797:811	α-tubulin O-GlcNAcylation	787:811	α-tubulin O-GlcNAcylation	787:811	We found that an increase in α-tubulin O-GlcNAcylation reduced heterodimerization and that O-GlcNAcylated tubulin did not polymerize into microtubules.
20665223	6	23	theme	outgrowth	1002:1010	arg1	extent					984:989	the extent	980:989	the extent of neurite outgrowth	980:1010	Consequently, when O-GlcNAcase inhibitors were co-incubated with tRA, the extent of neurite outgrowth was decreased by 20% compared to control.
20665223	2	24	theme	neurite	414:420	arg1	outgrowth					422:430	all-trans retinoic acid (tRA)-induced neurite outgrowth	376:430	all-trans retinoic acid (tRA)-induced neurite outgrowth in the MN9D neuronal cell line	376:461	Here, we found that the O-GlcNAc modification pattern was altered during all-trans retinoic acid (tRA)-induced neurite outgrowth in the MN9D neuronal cell line.
20665223	6	25	theme	neurite	994:1000	arg1	outgrowth					1002:1010	neurite outgrowth	994:1010	neurite outgrowth	994:1010	Consequently, when O-GlcNAcase inhibitors were co-incubated with tRA, the extent of neurite outgrowth was decreased by 20% compared to control.
20665223	5	26	theme	O-GlcNAcylated	849:862	arg1	tubulin					864:870	O-GlcNAcylated tubulin	849:870	O-GlcNAcylated tubulin	849:870	We found that an increase in α-tubulin O-GlcNAcylation reduced heterodimerization and that O-GlcNAcylated tubulin did not polymerize into microtubules.
20665223	2	27	theme	-induced	405:412	arg1	outgrowth					422:430	all-trans retinoic acid (tRA)-induced neurite outgrowth	376:430	all-trans retinoic acid (tRA)-induced neurite outgrowth in the MN9D neuronal cell line	376:461	Here, we found that the O-GlcNAc modification pattern was altered during all-trans retinoic acid (tRA)-induced neurite outgrowth in the MN9D neuronal cell line.
20665223	3	28	theme	several	478:484	arg1	proteins					501:508	several O-GlcNAcylated proteins	478:508	several O-GlcNAcylated proteins	478:508	We identified several O-GlcNAcylated proteins using mass spectrometric analysis, including α- and β-tubulin.
20665223	3	28	theme	several	478:484	arg1	β-tubulin					562:570	β-tubulin	562:570	β-tubulin	562:570	We identified several O-GlcNAcylated proteins using mass spectrometric analysis, including α- and β-tubulin.
20665223	3	28	theme	several	478:484	arg1	α-					555:556	α-	555:556	α-	555:556	We identified several O-GlcNAcylated proteins using mass spectrometric analysis, including α- and β-tubulin.
20665223	5	29	from	increase	775:782	arg1	O-GlcNAcylation					797:811	α-tubulin O-GlcNAcylation	787:811	α-tubulin O-GlcNAcylation	787:811	We found that an increase in α-tubulin O-GlcNAcylation reduced heterodimerization and that O-GlcNAcylated tubulin did not polymerize into microtubules.
20665223	1	30	theme	reversible	147:156	arg1	attachment					60:69	The attachment	56:69	The attachment of O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins	56:126	The attachment of O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins is an abundant and reversible modification that involves many cellular processes including transcription, translation, cell proliferation, apoptosis, and signal transduction.
20665223	1	30	theme	reversible	147:156	arg1	modification					158:169	an abundant and reversible modification	131:169	an abundant and reversible modification that involves many cellular processes including transcription, translation, cell proliferation, apoptosis, and signal transduction	131:300	The attachment of O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins is an abundant and reversible modification that involves many cellular processes including transcription, translation, cell proliferation, apoptosis, and signal transduction.
20665223	2	31	theme	modification	336:347	arg1	pattern					349:355	the O-GlcNAc modification pattern	323:355	the O-GlcNAc modification pattern	323:355	Here, we found that the O-GlcNAc modification pattern was altered during all-trans retinoic acid (tRA)-induced neurite outgrowth in the MN9D neuronal cell line.
20665223	4	32	theme	O-GlcNAcylated	624:637	arg1	peptides					639:646	O-GlcNAcylated peptides	624:646	O-GlcNAcylated peptides	624:646	Further analysis of α- and β-tubulin revealed that O-GlcNAcylated peptides mapped between residues 173 and 185 of α-tubulin and between residues 216 and 238 of β-tubulin, respectively.
20665223	1	33	theme	abundant	134:141	arg1	attachment					60:69	The attachment	56:69	The attachment of O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins	56:126	The attachment of O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins is an abundant and reversible modification that involves many cellular processes including transcription, translation, cell proliferation, apoptosis, and signal transduction.
20665223	1	33	theme	abundant	134:141	arg1	modification					158:169	an abundant and reversible modification	131:169	an abundant and reversible modification that involves many cellular processes including transcription, translation, cell proliferation, apoptosis, and signal transduction	131:300	The attachment of O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins is an abundant and reversible modification that involves many cellular processes including transcription, translation, cell proliferation, apoptosis, and signal transduction.
20665223	1	34	theme	cell	247:250	arg1	proliferation					252:264	cell proliferation	247:264	cell proliferation	247:264	The attachment of O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins is an abundant and reversible modification that involves many cellular processes including transcription, translation, cell proliferation, apoptosis, and signal transduction.
20665223	2	35	theme	retinoic	386:393	arg1	tRA					401:403	tRA	401:403	tRA	401:403	Here, we found that the O-GlcNAc modification pattern was altered during all-trans retinoic acid (tRA)-induced neurite outgrowth in the MN9D neuronal cell line.
20665223	2	35	theme	retinoic	386:393	arg1	acid					395:398	all-trans retinoic acid	376:398	all-trans retinoic acid (tRA)	376:404	Here, we found that the O-GlcNAc modification pattern was altered during all-trans retinoic acid (tRA)-induced neurite outgrowth in the MN9D neuronal cell line.
20665223	3	36	theme	O-GlcNAcylated	486:499	arg1	proteins					501:508	several O-GlcNAcylated proteins	478:508	several O-GlcNAcylated proteins	478:508	We identified several O-GlcNAcylated proteins using mass spectrometric analysis, including α- and β-tubulin.
20665223	3	36	theme	O-GlcNAcylated	486:499	arg1	β-tubulin					562:570	β-tubulin	562:570	β-tubulin	562:570	We identified several O-GlcNAcylated proteins using mass spectrometric analysis, including α- and β-tubulin.
20665223	3	36	theme	O-GlcNAcylated	486:499	arg1	α-					555:556	α-	555:556	α-	555:556	We identified several O-GlcNAcylated proteins using mass spectrometric analysis, including α- and β-tubulin.
20665223	4	37	theme	β-tubulin	600:608	arg1	analysis					581:588	Further analysis	573:588	Further analysis of α- and β-tubulin	573:608	Further analysis of α- and β-tubulin revealed that O-GlcNAcylated peptides mapped between residues 173 and 185 of α-tubulin and between residues 216 and 238 of β-tubulin, respectively.
20665223	2	38	theme	all-trans	376:384	arg1	tRA					401:403	tRA	401:403	tRA	401:403	Here, we found that the O-GlcNAc modification pattern was altered during all-trans retinoic acid (tRA)-induced neurite outgrowth in the MN9D neuronal cell line.
20665223	2	38	theme	all-trans	376:384	arg1	acid					395:398	all-trans retinoic acid	376:398	all-trans retinoic acid (tRA)	376:404	Here, we found that the O-GlcNAc modification pattern was altered during all-trans retinoic acid (tRA)-induced neurite outgrowth in the MN9D neuronal cell line.
28609614	8	0	theme	alternative	1201:1211	arg1	tool					1213:1216	an alternative tool	1198:1216	an alternative tool to monitor kinetics on one of the most labile of protein post-translational modifications	1198:1306	Together, the data highlight that high resolution native MS may provide an alternative tool to monitor kinetics on one of the most labile of protein post-translational modifications, in an efficient, reliable, and quantitative manner.
28609614	4	1	theme	mass	560:563	arg1	spectrometry					565:576	high-resolution native mass spectrometry	537:576	high-resolution native mass spectrometry	537:576	Here, we demonstrate that high-resolution native mass spectrometry can be employed to monitor the small mass shifts induced by modification by O-GlcNAc on two known protein substrates, CK2α and TAB1, without the need for radioactive labeling or chemoenzymatic tagging using large mass tags.
28609614	7	2	theme	MS	1025:1026	arg1	conditions					1028:1037	native MS conditions	1018:1037	native MS conditions	1018:1037	In contrast, we demonstrate that the O-GlcNAc is retained under native MS conditions, enabling precise quantitative analysis of stoichiometry and O-GlcNAcylation kinetics.
28609614	8	3	theme	resolution	1165:1174	arg1	MS					1183:1184	high resolution native MS	1160:1184	high resolution native MS	1160:1184	Together, the data highlight that high resolution native MS may provide an alternative tool to monitor kinetics on one of the most labile of protein post-translational modifications, in an efficient, reliable, and quantitative manner.
28609614	5	4	theme	further	830:836	arg1	localization					838:849	further localization	830:849	further localization of the O-GlcNAc sites	830:871	Limited proteolysis enabled further localization of the O-GlcNAc sites.
28609614	6	5	theme	peptide-centric	877:891	arg1	analysis					896:903	peptide-centric MS analysis	877:903	peptide-centric MS analysis	877:903	In peptide-centric MS analysis, the O-GlcNAc moiety is known to be easily lost.
28609614	4	6	theme	radioactive	732:742	arg1	labeling					744:751	radioactive labeling	732:751	radioactive labeling	732:751	Here, we demonstrate that high-resolution native mass spectrometry can be employed to monitor the small mass shifts induced by modification by O-GlcNAc on two known protein substrates, CK2α and TAB1, without the need for radioactive labeling or chemoenzymatic tagging using large mass tags.
28609614	8	7	theme	modifications	1294:1306	arg1	labile					1257:1262	labile	1257:1262	labile	1257:1262	Together, the data highlight that high resolution native MS may provide an alternative tool to monitor kinetics on one of the most labile of protein post-translational modifications, in an efficient, reliable, and quantitative manner.
28609614	3	8	from	studies	323:329	arg1	O-GlcNAcylation					342:356	protein O-GlcNAcylation	334:356	protein O-GlcNAcylation	334:356	Mechanistic studies on protein O-GlcNAcylation are hampered by the lack of methods that can simultaneously quantify O-GlcNAcylation, determine its stoichiometry, and monitor O-GlcNAcylation kinetics.
28609614	3	9	theme	O-GlcNAcylation	485:499	arg1	kinetics					501:508	O-GlcNAcylation kinetics	485:508	O-GlcNAcylation kinetics	485:508	Mechanistic studies on protein O-GlcNAcylation are hampered by the lack of methods that can simultaneously quantify O-GlcNAcylation, determine its stoichiometry, and monitor O-GlcNAcylation kinetics.
28609614	3	10	theme	methods	386:392	arg1	lack					378:381	the lack	374:381	the lack of methods that can simultaneously quantify O-GlcNAcylation, determine its stoichiometry, and monitor O-GlcNAcylation kinetics	374:508	Mechanistic studies on protein O-GlcNAcylation are hampered by the lack of methods that can simultaneously quantify O-GlcNAcylation, determine its stoichiometry, and monitor O-GlcNAcylation kinetics.
28609614	4	11	theme	native	553:558	arg1	spectrometry					565:576	high-resolution native mass spectrometry	537:576	high-resolution native mass spectrometry	537:576	Here, we demonstrate that high-resolution native mass spectrometry can be employed to monitor the small mass shifts induced by modification by O-GlcNAc on two known protein substrates, CK2α and TAB1, without the need for radioactive labeling or chemoenzymatic tagging using large mass tags.
28609614	8	12	theme	post-translational	1275:1292	arg1	modifications					1294:1306	protein post-translational modifications	1267:1306	protein post-translational modifications	1267:1306	Together, the data highlight that high resolution native MS may provide an alternative tool to monitor kinetics on one of the most labile of protein post-translational modifications, in an efficient, reliable, and quantitative manner.
28609614	5	13	theme	sites	867:871	arg1	localization					838:849	further localization	830:849	further localization of the O-GlcNAc sites	830:871	Limited proteolysis enabled further localization of the O-GlcNAc sites.
28609614	4	14	theme	high-resolution	537:551	arg1	spectrometry					565:576	high-resolution native mass spectrometry	537:576	high-resolution native mass spectrometry	537:576	Here, we demonstrate that high-resolution native mass spectrometry can be employed to monitor the small mass shifts induced by modification by O-GlcNAc on two known protein substrates, CK2α and TAB1, without the need for radioactive labeling or chemoenzymatic tagging using large mass tags.
28609614	4	15	theme	mass	791:794	arg1	tags					796:799	large mass tags	785:799	large mass tags	785:799	Here, we demonstrate that high-resolution native mass spectrometry can be employed to monitor the small mass shifts induced by modification by O-GlcNAc on two known protein substrates, CK2α and TAB1, without the need for radioactive labeling or chemoenzymatic tagging using large mass tags.
28609614	8	16	theme	high	1160:1163	arg1	MS					1183:1184	high resolution native MS	1160:1184	high resolution native MS	1160:1184	Together, the data highlight that high resolution native MS may provide an alternative tool to monitor kinetics on one of the most labile of protein post-translational modifications, in an efficient, reliable, and quantitative manner.
28609614	0	17	theme	Direct	0:5	arg1	Monitoring					7:16	Direct Monitoring	0:16	Direct Monitoring of Protein O-GlcNAcylation by High-Resolution Native Mass Spectrometry	0:87	Direct Monitoring of Protein O-GlcNAcylation by High-Resolution Native Mass Spectrometry.
28609614	4	18	theme	mass	615:618	arg1	shifts					620:625	the small mass shifts	605:625	the small mass shifts induced by modification by O-GlcNAc	605:661	Here, we demonstrate that high-resolution native mass spectrometry can be employed to monitor the small mass shifts induced by modification by O-GlcNAc on two known protein substrates, CK2α and TAB1, without the need for radioactive labeling or chemoenzymatic tagging using large mass tags.
28609614	6	19	theme	MS	893:894	arg1	analysis					896:903	peptide-centric MS analysis	877:903	peptide-centric MS analysis	877:903	In peptide-centric MS analysis, the O-GlcNAc moiety is known to be easily lost.
28609614	4	20	theme	large	785:789	arg1	tags					796:799	large mass tags	785:799	large mass tags	785:799	Here, we demonstrate that high-resolution native mass spectrometry can be employed to monitor the small mass shifts induced by modification by O-GlcNAc on two known protein substrates, CK2α and TAB1, without the need for radioactive labeling or chemoenzymatic tagging using large mass tags.
28609614	0	21	theme	Protein	21:27	arg1	O-GlcNAcylation					29:43	Protein O-GlcNAcylation	21:43	Protein O-GlcNAcylation	21:43	Direct Monitoring of Protein O-GlcNAcylation by High-Resolution Native Mass Spectrometry.
28609614	4	22	theme	small	609:613	arg1	shifts					620:625	the small mass shifts	605:625	the small mass shifts induced by modification by O-GlcNAc	605:661	Here, we demonstrate that high-resolution native mass spectrometry can be employed to monitor the small mass shifts induced by modification by O-GlcNAc on two known protein substrates, CK2α and TAB1, without the need for radioactive labeling or chemoenzymatic tagging using large mass tags.
28609614	3	23	theme	Mechanistic	311:321	arg1	studies					323:329	Mechanistic studies	311:329	Mechanistic studies on protein O-GlcNAcylation	311:356	Mechanistic studies on protein O-GlcNAcylation are hampered by the lack of methods that can simultaneously quantify O-GlcNAcylation, determine its stoichiometry, and monitor O-GlcNAcylation kinetics.
28609614	8	24	theme	efficient	1315:1323	arg1	manner					1353:1358	an efficient, reliable, and quantitative manner	1312:1358	an efficient, reliable, and quantitative manner	1312:1358	Together, the data highlight that high resolution native MS may provide an alternative tool to monitor kinetics on one of the most labile of protein post-translational modifications, in an efficient, reliable, and quantitative manner.
28609614	7	25	theme	stoichiometry	1082:1094	arg1	kinetics					1116:1123	stoichiometry and O-GlcNAcylation kinetics	1082:1123	stoichiometry and O-GlcNAcylation kinetics	1082:1123	In contrast, we demonstrate that the O-GlcNAc is retained under native MS conditions, enabling precise quantitative analysis of stoichiometry and O-GlcNAcylation kinetics.
28609614	8	26	theme	labile	1257:1262	arg1	labile					1257:1262	labile	1257:1262	labile	1257:1262	Together, the data highlight that high resolution native MS may provide an alternative tool to monitor kinetics on one of the most labile of protein post-translational modifications, in an efficient, reliable, and quantitative manner.
28609614	8	26	theme	labile	1257:1262	arg1	one					1241:1243	one	1241:1243	one	1241:1243	Together, the data highlight that high resolution native MS may provide an alternative tool to monitor kinetics on one of the most labile of protein post-translational modifications, in an efficient, reliable, and quantitative manner.
28609614	7	27	theme	kinetics	1116:1123	arg1	analysis					1070:1077	precise quantitative analysis	1049:1077	precise quantitative analysis of stoichiometry and O-GlcNAcylation kinetics	1049:1123	In contrast, we demonstrate that the O-GlcNAc is retained under native MS conditions, enabling precise quantitative analysis of stoichiometry and O-GlcNAcylation kinetics.
28609614	8	28	theme	reliable	1326:1333	arg1	manner					1353:1358	an efficient, reliable, and quantitative manner	1312:1358	an efficient, reliable, and quantitative manner	1312:1358	Together, the data highlight that high resolution native MS may provide an alternative tool to monitor kinetics on one of the most labile of protein post-translational modifications, in an efficient, reliable, and quantitative manner.
28609614	0	29	theme	O-GlcNAcylation	29:43	arg1	Monitoring					7:16	Direct Monitoring	0:16	Direct Monitoring of Protein O-GlcNAcylation by High-Resolution Native Mass Spectrometry	0:87	Direct Monitoring of Protein O-GlcNAcylation by High-Resolution Native Mass Spectrometry.
28609614	7	30	theme	quantitative	1057:1068	arg1	analysis					1070:1077	precise quantitative analysis	1049:1077	precise quantitative analysis of stoichiometry and O-GlcNAcylation kinetics	1049:1123	In contrast, we demonstrate that the O-GlcNAc is retained under native MS conditions, enabling precise quantitative analysis of stoichiometry and O-GlcNAcylation kinetics.
28609614	8	31	theme	quantitative	1340:1351	arg1	manner					1353:1358	an efficient, reliable, and quantitative manner	1312:1358	an efficient, reliable, and quantitative manner	1312:1358	Together, the data highlight that high resolution native MS may provide an alternative tool to monitor kinetics on one of the most labile of protein post-translational modifications, in an efficient, reliable, and quantitative manner.
28609614	0	32	theme	Native	64:69	arg1	Spectrometry					76:87	High-Resolution Native Mass Spectrometry	48:87	High-Resolution Native Mass Spectrometry	48:87	Direct Monitoring of Protein O-GlcNAcylation by High-Resolution Native Mass Spectrometry.
28609614	5	33	theme	O-GlcNAc	858:865	arg1	sites					867:871	the O-GlcNAc sites	854:871	the O-GlcNAc sites	854:871	Limited proteolysis enabled further localization of the O-GlcNAc sites.
28609614	6	34	theme	O-GlcNAc	910:917	arg1	moiety					919:924	the O-GlcNAc moiety	906:924	the O-GlcNAc moiety	906:924	In peptide-centric MS analysis, the O-GlcNAc moiety is known to be easily lost.
28609614	4	35	theme	chemoenzymatic	756:769	arg1	tagging					771:777	chemoenzymatic tagging	756:777	chemoenzymatic tagging	756:777	Here, we demonstrate that high-resolution native mass spectrometry can be employed to monitor the small mass shifts induced by modification by O-GlcNAc on two known protein substrates, CK2α and TAB1, without the need for radioactive labeling or chemoenzymatic tagging using large mass tags.
28609614	0	36	theme	High-Resolution	48:62	arg1	Spectrometry					76:87	High-Resolution Native Mass Spectrometry	48:87	High-Resolution Native Mass Spectrometry	48:87	Direct Monitoring of Protein O-GlcNAcylation by High-Resolution Native Mass Spectrometry.
28609614	7	37	theme	O-GlcNAcylation	1100:1114	arg1	kinetics					1116:1123	stoichiometry and O-GlcNAcylation kinetics	1082:1123	stoichiometry and O-GlcNAcylation kinetics	1082:1123	In contrast, we demonstrate that the O-GlcNAc is retained under native MS conditions, enabling precise quantitative analysis of stoichiometry and O-GlcNAcylation kinetics.
28609614	8	38	from	kinetics	1229:1236	arg1	labile					1257:1262	labile	1257:1262	labile	1257:1262	Together, the data highlight that high resolution native MS may provide an alternative tool to monitor kinetics on one of the most labile of protein post-translational modifications, in an efficient, reliable, and quantitative manner.
28609614	8	38	from	kinetics	1229:1236	arg1	one					1241:1243	one	1241:1243	one	1241:1243	Together, the data highlight that high resolution native MS may provide an alternative tool to monitor kinetics on one of the most labile of protein post-translational modifications, in an efficient, reliable, and quantitative manner.
28609614	1	39	theme	abundant	125:132	arg1	modifications					182:194	the most abundant metazoan nuclear-cytoplasmic post-translational modifications	116:194	the most abundant metazoan nuclear-cytoplasmic post-translational modifications	116:194	O-GlcNAcylation is one of the most abundant metazoan nuclear-cytoplasmic post-translational modifications.
28609614	2	40	theme	cell	296:299	arg1	division					301:308	cell division	296:308	cell division	296:308	Proteins modified by O-GlcNAc play key cellular roles in signaling, transcription, metabolism, and cell division.
28609614	7	41	theme	precise	1049:1055	arg1	analysis					1070:1077	precise quantitative analysis	1049:1077	precise quantitative analysis of stoichiometry and O-GlcNAcylation kinetics	1049:1123	In contrast, we demonstrate that the O-GlcNAc is retained under native MS conditions, enabling precise quantitative analysis of stoichiometry and O-GlcNAcylation kinetics.
28609614	1	42	theme	metazoan	134:141	arg1	modifications					182:194	the most abundant metazoan nuclear-cytoplasmic post-translational modifications	116:194	the most abundant metazoan nuclear-cytoplasmic post-translational modifications	116:194	O-GlcNAcylation is one of the most abundant metazoan nuclear-cytoplasmic post-translational modifications.
28609614	3	43	theme	protein	334:340	arg1	O-GlcNAcylation					342:356	protein O-GlcNAcylation	334:356	protein O-GlcNAcylation	334:356	Mechanistic studies on protein O-GlcNAcylation are hampered by the lack of methods that can simultaneously quantify O-GlcNAcylation, determine its stoichiometry, and monitor O-GlcNAcylation kinetics.
28609614	2	44	theme	cellular	236:243	arg1	roles					245:249	key cellular roles	232:249	key cellular roles	232:249	Proteins modified by O-GlcNAc play key cellular roles in signaling, transcription, metabolism, and cell division.
28609614	1	45	theme	nuclear-cytoplasmic	143:161	arg1	modifications					182:194	the most abundant metazoan nuclear-cytoplasmic post-translational modifications	116:194	the most abundant metazoan nuclear-cytoplasmic post-translational modifications	116:194	O-GlcNAcylation is one of the most abundant metazoan nuclear-cytoplasmic post-translational modifications.
28609614	8	46	theme	protein	1267:1273	arg1	modifications					1294:1306	protein post-translational modifications	1267:1306	protein post-translational modifications	1267:1306	Together, the data highlight that high resolution native MS may provide an alternative tool to monitor kinetics on one of the most labile of protein post-translational modifications, in an efficient, reliable, and quantitative manner.
28609614	5	47	theme	Limited	802:808	arg1	proteolysis					810:820	Limited proteolysis	802:820	Limited proteolysis	802:820	Limited proteolysis enabled further localization of the O-GlcNAc sites.
28609614	2	48	theme	key	232:234	arg1	roles					245:249	key cellular roles	232:249	key cellular roles	232:249	Proteins modified by O-GlcNAc play key cellular roles in signaling, transcription, metabolism, and cell division.
28609614	1	49	theme	post-translational	163:180	arg1	modifications					182:194	the most abundant metazoan nuclear-cytoplasmic post-translational modifications	116:194	the most abundant metazoan nuclear-cytoplasmic post-translational modifications	116:194	O-GlcNAcylation is one of the most abundant metazoan nuclear-cytoplasmic post-translational modifications.
28609614	4	50	theme	protein	676:682	arg1	CK2α					696:699	CK2α	696:699	CK2α	696:699	Here, we demonstrate that high-resolution native mass spectrometry can be employed to monitor the small mass shifts induced by modification by O-GlcNAc on two known protein substrates, CK2α and TAB1, without the need for radioactive labeling or chemoenzymatic tagging using large mass tags.
28609614	4	50	theme	protein	676:682	arg1	substrates					684:693	two known protein substrates	666:693	two known protein substrates	666:693	Here, we demonstrate that high-resolution native mass spectrometry can be employed to monitor the small mass shifts induced by modification by O-GlcNAc on two known protein substrates, CK2α and TAB1, without the need for radioactive labeling or chemoenzymatic tagging using large mass tags.
28609614	4	50	theme	protein	676:682	arg1	TAB1					705:708	TAB1	705:708	TAB1	705:708	Here, we demonstrate that high-resolution native mass spectrometry can be employed to monitor the small mass shifts induced by modification by O-GlcNAc on two known protein substrates, CK2α and TAB1, without the need for radioactive labeling or chemoenzymatic tagging using large mass tags.
28609614	0	51	theme	Mass	71:74	arg1	Spectrometry					76:87	High-Resolution Native Mass Spectrometry	48:87	High-Resolution Native Mass Spectrometry	48:87	Direct Monitoring of Protein O-GlcNAcylation by High-Resolution Native Mass Spectrometry.
28609614	7	52	theme	native	1018:1023	arg1	conditions					1028:1037	native MS conditions	1018:1037	native MS conditions	1018:1037	In contrast, we demonstrate that the O-GlcNAc is retained under native MS conditions, enabling precise quantitative analysis of stoichiometry and O-GlcNAcylation kinetics.
28609614	1	53	theme	modifications	182:194	arg1	one					109:111	one	109:111	one	109:111	O-GlcNAcylation is one of the most abundant metazoan nuclear-cytoplasmic post-translational modifications.
28609614	1	53	theme	modifications	182:194	arg1	modifications					182:194	the most abundant metazoan nuclear-cytoplasmic post-translational modifications	116:194	the most abundant metazoan nuclear-cytoplasmic post-translational modifications	116:194	O-GlcNAcylation is one of the most abundant metazoan nuclear-cytoplasmic post-translational modifications.
28609614	8	54	theme	native	1176:1181	arg1	MS					1183:1184	high resolution native MS	1160:1184	high resolution native MS	1160:1184	Together, the data highlight that high resolution native MS may provide an alternative tool to monitor kinetics on one of the most labile of protein post-translational modifications, in an efficient, reliable, and quantitative manner.
28609614	4	55	theme	known	670:674	arg1	CK2α					696:699	CK2α	696:699	CK2α	696:699	Here, we demonstrate that high-resolution native mass spectrometry can be employed to monitor the small mass shifts induced by modification by O-GlcNAc on two known protein substrates, CK2α and TAB1, without the need for radioactive labeling or chemoenzymatic tagging using large mass tags.
28609614	4	55	theme	known	670:674	arg1	substrates					684:693	two known protein substrates	666:693	two known protein substrates	666:693	Here, we demonstrate that high-resolution native mass spectrometry can be employed to monitor the small mass shifts induced by modification by O-GlcNAc on two known protein substrates, CK2α and TAB1, without the need for radioactive labeling or chemoenzymatic tagging using large mass tags.
28609614	4	55	theme	known	670:674	arg1	TAB1					705:708	TAB1	705:708	TAB1	705:708	Here, we demonstrate that high-resolution native mass spectrometry can be employed to monitor the small mass shifts induced by modification by O-GlcNAc on two known protein substrates, CK2α and TAB1, without the need for radioactive labeling or chemoenzymatic tagging using large mass tags.
32994395	5	0	theme	ligase	813:818	arg1	activity					820:827	the E3 ubiquitin ligase activity	796:827	the E3 ubiquitin ligase activity of XIAP toward specifically OGT	796:859	Interestingly, OGT catalyzes the O-GlcNAc modification of XIAP at serine 406 and this modification is required for the E3 ubiquitin ligase activity of XIAP toward specifically OGT.
32994395	1	1	theme	many	227:230	arg1	types					232:236	many types	227:236	many types of cancer	227:246	O-GlcNAc transferase (OGT) is an enzyme that catalyzes the O-GlcNAc modification of nucleocytoplasmic proteins and is highly expressed in many types of cancer.
32994395	0	2	theme	cell	63:66	arg1	growth					68:73	colon cancer cell growth	50:73	colon cancer cell growth	50:73	Mutual regulation between OGT and XIAP to control colon cancer cell growth and invasion.
32994395	3	3	link	X-linked	406:413	arg1	XIAP					439:442	XIAP	439:442	XIAP	439:442	This study shows that OGT is a substrate of the E3 ubiquitin ligase X-linked inhibitor of apoptosis (XIAP) which plays an important role in cancer pathogenesis.
32994395	3	3	link	X-linked	406:413	arg1	inhibitor					415:423	the E3 ubiquitin ligase X-linked inhibitor	382:423	the E3 ubiquitin ligase X-linked inhibitor of apoptosis (XIAP)	382:443	This study shows that OGT is a substrate of the E3 ubiquitin ligase X-linked inhibitor of apoptosis (XIAP) which plays an important role in cancer pathogenesis.
32994395	7	4	theme	O-GlcNAc	1170:1177	arg1	modification					1179:1190	O-GlcNAc modification	1170:1190	O-GlcNAc modification	1170:1190	Therefore, our findings regarding the reciprocal regulation of OGT and XIAP provide a novel molecular mechanism for controlling cancer growth and invasion regulated by OGT and O-GlcNAc modification.
32994395	2	5	from	expression	287:296	arg1	cells					308:312	cancer cells	301:312	cancer cells	301:312	However, the mechanism regulating its expression in cancer cells is not well understood.
32994395	6	6	theme	cell	920:923	arg1	growth					925:930	colon cancer cell growth	907:930	colon cancer cell growth	907:930	Moreover, O-GlcNAcylation of XIAP suppresses colon cancer cell growth and invasion by promoting the proteasomal degradation of OGT.
32994395	7	7	theme	reciprocal	1032:1041	arg1	regulation					1043:1052	the reciprocal regulation	1028:1052	the reciprocal regulation of OGT and XIAP	1028:1068	Therefore, our findings regarding the reciprocal regulation of OGT and XIAP provide a novel molecular mechanism for controlling cancer growth and invasion regulated by OGT and O-GlcNAc modification.
32994395	3	8	theme	cancer	478:483	arg1	pathogenesis					485:496	cancer pathogenesis	478:496	cancer pathogenesis	478:496	This study shows that OGT is a substrate of the E3 ubiquitin ligase X-linked inhibitor of apoptosis (XIAP) which plays an important role in cancer pathogenesis.
32994395	4	9	theme	cancer	667:672	arg1	cells					674:678	colon cancer cells	661:678	colon cancer cells	661:678	Although LSD2 histone demethylase has already been reported as an E3 ubiquitin ligase in lung cancer cells, we identified XIAP as the main E3 ubiquitin ligase in colon cancer cells.
32994395	6	10	theme	cancer	913:918	arg1	growth					925:930	colon cancer cell growth	907:930	colon cancer cell growth	907:930	Moreover, O-GlcNAcylation of XIAP suppresses colon cancer cell growth and invasion by promoting the proteasomal degradation of OGT.
32994395	7	11	theme	cancer	1122:1127	arg1	growth					1129:1134	cancer growth	1122:1134	cancer growth	1122:1134	Therefore, our findings regarding the reciprocal regulation of OGT and XIAP provide a novel molecular mechanism for controlling cancer growth and invasion regulated by OGT and O-GlcNAc modification.
32994395	1	12	theme	cancer	241:246	arg1	types					232:236	many types	227:236	many types of cancer	227:246	O-GlcNAc transferase (OGT) is an enzyme that catalyzes the O-GlcNAc modification of nucleocytoplasmic proteins and is highly expressed in many types of cancer.
32994395	4	13	theme	lung	588:591	arg1	cells					600:604	lung cancer cells	588:604	lung cancer cells	588:604	Although LSD2 histone demethylase has already been reported as an E3 ubiquitin ligase in lung cancer cells, we identified XIAP as the main E3 ubiquitin ligase in colon cancer cells.
32994395	4	14	theme	ubiquitin	568:576	arg1	demethylase					521:531	LSD2 histone demethylase	508:531	LSD2 histone demethylase	508:531	Although LSD2 histone demethylase has already been reported as an E3 ubiquitin ligase in lung cancer cells, we identified XIAP as the main E3 ubiquitin ligase in colon cancer cells.
32994395	4	14	theme	ubiquitin	568:576	arg1	ligase					578:583	an E3 ubiquitin ligase	562:583	an E3 ubiquitin ligase in lung cancer cells	562:604	Although LSD2 histone demethylase has already been reported as an E3 ubiquitin ligase in lung cancer cells, we identified XIAP as the main E3 ubiquitin ligase in colon cancer cells.
32994395	3	15	theme	E3	386:387	arg1	ligase					399:404	the E3 ubiquitin ligase	382:404	the E3 ubiquitin ligase X-linked inhibitor of apoptosis (XIAP)	382:443	This study shows that OGT is a substrate of the E3 ubiquitin ligase X-linked inhibitor of apoptosis (XIAP) which plays an important role in cancer pathogenesis.
32994395	6	16	theme	colon	907:911	arg1	growth					925:930	colon cancer cell growth	907:930	colon cancer cell growth	907:930	Moreover, O-GlcNAcylation of XIAP suppresses colon cancer cell growth and invasion by promoting the proteasomal degradation of OGT.
32994395	5	17	theme	XIAP	739:742	arg1	modification					723:734	the O-GlcNAc modification	710:734	the O-GlcNAc modification of XIAP	710:742	Interestingly, OGT catalyzes the O-GlcNAc modification of XIAP at serine 406 and this modification is required for the E3 ubiquitin ligase activity of XIAP toward specifically OGT.
32994395	3	18	theme	ubiquitin	389:397	arg1	ligase					399:404	the E3 ubiquitin ligase	382:404	the E3 ubiquitin ligase X-linked inhibitor of apoptosis (XIAP)	382:443	This study shows that OGT is a substrate of the E3 ubiquitin ligase X-linked inhibitor of apoptosis (XIAP) which plays an important role in cancer pathogenesis.
32994395	4	19	theme	colon	661:665	arg1	cells					674:678	colon cancer cells	661:678	colon cancer cells	661:678	Although LSD2 histone demethylase has already been reported as an E3 ubiquitin ligase in lung cancer cells, we identified XIAP as the main E3 ubiquitin ligase in colon cancer cells.
32994395	1	20	theme	O-GlcNAc	148:155	arg1	modification					157:168	the O-GlcNAc modification	144:168	the O-GlcNAc modification of nucleocytoplasmic proteins	144:198	O-GlcNAc transferase (OGT) is an enzyme that catalyzes the O-GlcNAc modification of nucleocytoplasmic proteins and is highly expressed in many types of cancer.
32994395	0	21	theme	Mutual	0:5	arg1	regulation					7:16	Mutual regulation	0:16	Mutual regulation between OGT and XIAP	0:37	Mutual regulation between OGT and XIAP to control colon cancer cell growth and invasion.
32994395	6	22	theme	OGT	989:991	arg1	degradation					974:984	the proteasomal degradation	958:984	the proteasomal degradation of OGT	958:991	Moreover, O-GlcNAcylation of XIAP suppresses colon cancer cell growth and invasion by promoting the proteasomal degradation of OGT.
32994395	7	23	theme	novel	1080:1084	arg1	mechanism					1096:1104	a novel molecular mechanism	1078:1104	a novel molecular mechanism for controlling cancer growth and invasion regulated by OGT and O-GlcNAc modification	1078:1190	Therefore, our findings regarding the reciprocal regulation of OGT and XIAP provide a novel molecular mechanism for controlling cancer growth and invasion regulated by OGT and O-GlcNAc modification.
32994395	6	24	theme	XIAP	891:894	arg1	O-GlcNAcylation					872:886	O-GlcNAcylation	872:886	O-GlcNAcylation of XIAP	872:894	Moreover, O-GlcNAcylation of XIAP suppresses colon cancer cell growth and invasion by promoting the proteasomal degradation of OGT.
32994395	6	25	theme	proteasomal	962:972	arg1	degradation					974:984	the proteasomal degradation	958:984	the proteasomal degradation of OGT	958:991	Moreover, O-GlcNAcylation of XIAP suppresses colon cancer cell growth and invasion by promoting the proteasomal degradation of OGT.
32994395	3	26	theme	inhibitor	415:423	arg1	OGT					360:362	OGT	360:362	OGT	360:362	This study shows that OGT is a substrate of the E3 ubiquitin ligase X-linked inhibitor of apoptosis (XIAP) which plays an important role in cancer pathogenesis.
32994395	3	26	theme	inhibitor	415:423	arg1	substrate					369:377	a substrate	367:377	a substrate of the E3 ubiquitin ligase X-linked inhibitor of apoptosis (XIAP) which plays an important role in cancer pathogenesis	367:496	This study shows that OGT is a substrate of the E3 ubiquitin ligase X-linked inhibitor of apoptosis (XIAP) which plays an important role in cancer pathogenesis.
32994395	7	27	theme	molecular	1086:1094	arg1	mechanism					1096:1104	a novel molecular mechanism	1078:1104	a novel molecular mechanism for controlling cancer growth and invasion regulated by OGT and O-GlcNAc modification	1078:1190	Therefore, our findings regarding the reciprocal regulation of OGT and XIAP provide a novel molecular mechanism for controlling cancer growth and invasion regulated by OGT and O-GlcNAc modification.
32994395	4	28	theme	histone	513:519	arg1	demethylase					521:531	LSD2 histone demethylase	508:531	LSD2 histone demethylase	508:531	Although LSD2 histone demethylase has already been reported as an E3 ubiquitin ligase in lung cancer cells, we identified XIAP as the main E3 ubiquitin ligase in colon cancer cells.
32994395	4	28	theme	histone	513:519	arg1	ligase					578:583	an E3 ubiquitin ligase	562:583	an E3 ubiquitin ligase in lung cancer cells	562:604	Although LSD2 histone demethylase has already been reported as an E3 ubiquitin ligase in lung cancer cells, we identified XIAP as the main E3 ubiquitin ligase in colon cancer cells.
32994395	1	29	theme	O-GlcNAc	89:96	arg1	OGT					111:113	OGT	111:113	OGT	111:113	O-GlcNAc transferase (OGT) is an enzyme that catalyzes the O-GlcNAc modification of nucleocytoplasmic proteins and is highly expressed in many types of cancer.
32994395	1	29	theme	O-GlcNAc	89:96	arg1	transferase					98:108	O-GlcNAc transferase	89:108	O-GlcNAc transferase (OGT)	89:114	O-GlcNAc transferase (OGT) is an enzyme that catalyzes the O-GlcNAc modification of nucleocytoplasmic proteins and is highly expressed in many types of cancer.
32994395	1	29	theme	O-GlcNAc	89:96	arg1	enzyme					122:127	an enzyme	119:127	an enzyme that catalyzes the O-GlcNAc modification of nucleocytoplasmic proteins and is highly expressed in many types of cancer	119:246	O-GlcNAc transferase (OGT) is an enzyme that catalyzes the O-GlcNAc modification of nucleocytoplasmic proteins and is highly expressed in many types of cancer.
32994395	4	30	from	ligase	578:583	arg1	cells					600:604	lung cancer cells	588:604	lung cancer cells	588:604	Although LSD2 histone demethylase has already been reported as an E3 ubiquitin ligase in lung cancer cells, we identified XIAP as the main E3 ubiquitin ligase in colon cancer cells.
32994395	1	31	theme	nucleocytoplasmic	173:189	arg1	proteins					191:198	nucleocytoplasmic proteins	173:198	nucleocytoplasmic proteins	173:198	O-GlcNAc transferase (OGT) is an enzyme that catalyzes the O-GlcNAc modification of nucleocytoplasmic proteins and is highly expressed in many types of cancer.
32994395	4	32	theme	LSD2	508:511	arg1	demethylase					521:531	LSD2 histone demethylase	508:531	LSD2 histone demethylase	508:531	Although LSD2 histone demethylase has already been reported as an E3 ubiquitin ligase in lung cancer cells, we identified XIAP as the main E3 ubiquitin ligase in colon cancer cells.
32994395	4	32	theme	LSD2	508:511	arg1	ligase					578:583	an E3 ubiquitin ligase	562:583	an E3 ubiquitin ligase in lung cancer cells	562:604	Although LSD2 histone demethylase has already been reported as an E3 ubiquitin ligase in lung cancer cells, we identified XIAP as the main E3 ubiquitin ligase in colon cancer cells.
32994395	3	33	theme	ligase	399:404	arg1	XIAP					439:442	XIAP	439:442	XIAP	439:442	This study shows that OGT is a substrate of the E3 ubiquitin ligase X-linked inhibitor of apoptosis (XIAP) which plays an important role in cancer pathogenesis.
32994395	3	33	theme	ligase	399:404	arg1	inhibitor					415:423	the E3 ubiquitin ligase X-linked inhibitor	382:423	the E3 ubiquitin ligase X-linked inhibitor of apoptosis (XIAP)	382:443	This study shows that OGT is a substrate of the E3 ubiquitin ligase X-linked inhibitor of apoptosis (XIAP) which plays an important role in cancer pathogenesis.
32994395	1	34	theme	proteins	191:198	arg1	modification					157:168	the O-GlcNAc modification	144:168	the O-GlcNAc modification of nucleocytoplasmic proteins	144:198	O-GlcNAc transferase (OGT) is an enzyme that catalyzes the O-GlcNAc modification of nucleocytoplasmic proteins and is highly expressed in many types of cancer.
32994395	5	35	theme	XIAP	832:835	arg1	activity					820:827	the E3 ubiquitin ligase activity	796:827	the E3 ubiquitin ligase activity of XIAP toward specifically OGT	796:859	Interestingly, OGT catalyzes the O-GlcNAc modification of XIAP at serine 406 and this modification is required for the E3 ubiquitin ligase activity of XIAP toward specifically OGT.
32994395	3	36	theme	X-linked	406:413	arg1	XIAP					439:442	XIAP	439:442	XIAP	439:442	This study shows that OGT is a substrate of the E3 ubiquitin ligase X-linked inhibitor of apoptosis (XIAP) which plays an important role in cancer pathogenesis.
32994395	3	36	theme	X-linked	406:413	arg1	inhibitor					415:423	the E3 ubiquitin ligase X-linked inhibitor	382:423	the E3 ubiquitin ligase X-linked inhibitor of apoptosis (XIAP)	382:443	This study shows that OGT is a substrate of the E3 ubiquitin ligase X-linked inhibitor of apoptosis (XIAP) which plays an important role in cancer pathogenesis.
32994395	5	37	theme	O-GlcNAc	714:721	arg1	modification					723:734	the O-GlcNAc modification	710:734	the O-GlcNAc modification of XIAP	710:742	Interestingly, OGT catalyzes the O-GlcNAc modification of XIAP at serine 406 and this modification is required for the E3 ubiquitin ligase activity of XIAP toward specifically OGT.
32994395	4	38	theme	E3	638:639	arg1	XIAP					621:624	XIAP	621:624	XIAP	621:624	Although LSD2 histone demethylase has already been reported as an E3 ubiquitin ligase in lung cancer cells, we identified XIAP as the main E3 ubiquitin ligase in colon cancer cells.
32994395	4	38	theme	E3	638:639	arg1	ligase					651:656	the main E3 ubiquitin ligase	629:656	the main E3 ubiquitin ligase in colon cancer cells	629:678	Although LSD2 histone demethylase has already been reported as an E3 ubiquitin ligase in lung cancer cells, we identified XIAP as the main E3 ubiquitin ligase in colon cancer cells.
32994395	7	39	theme	XIAP	1065:1068	arg1	regulation					1043:1052	the reciprocal regulation	1028:1052	the reciprocal regulation of OGT and XIAP	1028:1068	Therefore, our findings regarding the reciprocal regulation of OGT and XIAP provide a novel molecular mechanism for controlling cancer growth and invasion regulated by OGT and O-GlcNAc modification.
32994395	7	40	theme	OGT	1057:1059	arg1	regulation					1043:1052	the reciprocal regulation	1028:1052	the reciprocal regulation of OGT and XIAP	1028:1068	Therefore, our findings regarding the reciprocal regulation of OGT and XIAP provide a novel molecular mechanism for controlling cancer growth and invasion regulated by OGT and O-GlcNAc modification.
32994395	4	41	theme	main	633:636	arg1	XIAP					621:624	XIAP	621:624	XIAP	621:624	Although LSD2 histone demethylase has already been reported as an E3 ubiquitin ligase in lung cancer cells, we identified XIAP as the main E3 ubiquitin ligase in colon cancer cells.
32994395	4	41	theme	main	633:636	arg1	ligase					651:656	the main E3 ubiquitin ligase	629:656	the main E3 ubiquitin ligase in colon cancer cells	629:678	Although LSD2 histone demethylase has already been reported as an E3 ubiquitin ligase in lung cancer cells, we identified XIAP as the main E3 ubiquitin ligase in colon cancer cells.
32994395	4	42	from	ligase	651:656	arg1	cells					674:678	colon cancer cells	661:678	colon cancer cells	661:678	Although LSD2 histone demethylase has already been reported as an E3 ubiquitin ligase in lung cancer cells, we identified XIAP as the main E3 ubiquitin ligase in colon cancer cells.
32994395	2	43	theme	cancer	301:306	arg1	cells					308:312	cancer cells	301:312	cancer cells	301:312	However, the mechanism regulating its expression in cancer cells is not well understood.
32994395	4	44	theme	ubiquitin	641:649	arg1	XIAP					621:624	XIAP	621:624	XIAP	621:624	Although LSD2 histone demethylase has already been reported as an E3 ubiquitin ligase in lung cancer cells, we identified XIAP as the main E3 ubiquitin ligase in colon cancer cells.
32994395	4	44	theme	ubiquitin	641:649	arg1	ligase					651:656	the main E3 ubiquitin ligase	629:656	the main E3 ubiquitin ligase in colon cancer cells	629:678	Although LSD2 histone demethylase has already been reported as an E3 ubiquitin ligase in lung cancer cells, we identified XIAP as the main E3 ubiquitin ligase in colon cancer cells.
32994395	3	45	theme	apoptosis	428:436	arg1	XIAP					439:442	XIAP	439:442	XIAP	439:442	This study shows that OGT is a substrate of the E3 ubiquitin ligase X-linked inhibitor of apoptosis (XIAP) which plays an important role in cancer pathogenesis.
32994395	3	45	theme	apoptosis	428:436	arg1	inhibitor					415:423	the E3 ubiquitin ligase X-linked inhibitor	382:423	the E3 ubiquitin ligase X-linked inhibitor of apoptosis (XIAP)	382:443	This study shows that OGT is a substrate of the E3 ubiquitin ligase X-linked inhibitor of apoptosis (XIAP) which plays an important role in cancer pathogenesis.
32994395	0	46	theme	cancer	56:61	arg1	growth					68:73	colon cancer cell growth	50:73	colon cancer cell growth	50:73	Mutual regulation between OGT and XIAP to control colon cancer cell growth and invasion.
32994395	5	47	theme	ubiquitin	803:811	arg1	ligase					813:818	E3 ubiquitin ligase	800:818	the E3 ubiquitin ligase activity of XIAP toward specifically OGT	796:859	Interestingly, OGT catalyzes the O-GlcNAc modification of XIAP at serine 406 and this modification is required for the E3 ubiquitin ligase activity of XIAP toward specifically OGT.
32994395	5	48	theme	E3	800:801	arg1	ligase					813:818	E3 ubiquitin ligase	800:818	the E3 ubiquitin ligase activity of XIAP toward specifically OGT	796:859	Interestingly, OGT catalyzes the O-GlcNAc modification of XIAP at serine 406 and this modification is required for the E3 ubiquitin ligase activity of XIAP toward specifically OGT.
32994395	4	49	theme	cancer	593:598	arg1	cells					600:604	lung cancer cells	588:604	lung cancer cells	588:604	Although LSD2 histone demethylase has already been reported as an E3 ubiquitin ligase in lung cancer cells, we identified XIAP as the main E3 ubiquitin ligase in colon cancer cells.
32994395	4	50	theme	E3	565:566	arg1	demethylase					521:531	LSD2 histone demethylase	508:531	LSD2 histone demethylase	508:531	Although LSD2 histone demethylase has already been reported as an E3 ubiquitin ligase in lung cancer cells, we identified XIAP as the main E3 ubiquitin ligase in colon cancer cells.
32994395	4	50	theme	E3	565:566	arg1	ligase					578:583	an E3 ubiquitin ligase	562:583	an E3 ubiquitin ligase in lung cancer cells	562:604	Although LSD2 histone demethylase has already been reported as an E3 ubiquitin ligase in lung cancer cells, we identified XIAP as the main E3 ubiquitin ligase in colon cancer cells.
32994395	0	51	theme	colon	50:54	arg1	growth					68:73	colon cancer cell growth	50:73	colon cancer cell growth	50:73	Mutual regulation between OGT and XIAP to control colon cancer cell growth and invasion.
32994395	3	52	theme	important	460:468	arg1	role					470:473	an important role	457:473	an important role	457:473	This study shows that OGT is a substrate of the E3 ubiquitin ligase X-linked inhibitor of apoptosis (XIAP) which plays an important role in cancer pathogenesis.
23027940	2	0	from	expression	462:471	arg1	response					476:483	response	476:483	response to tumor necrosis factor (TNF) or etoposide	476:527	Using nuclear factor-κB (NF-κB) as a glucose-responsive transcription factor, we show that cells use the hexosamine biosynthesis pathway and O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) to potentiate gene expression in response to tumor necrosis factor (TNF) or etoposide.
23027940	1	1	from	undercharacterized	203:220	arg1	cells					235:239	mammalian cells	225:239	mammalian cells	225:239	The molecular mechanisms linking glucose metabolism with active transcription remain undercharacterized in mammalian cells.
23027940	1	2	theme	active	175:180	arg1	transcription					182:194	active transcription	175:194	active transcription	175:194	The molecular mechanisms linking glucose metabolism with active transcription remain undercharacterized in mammalian cells.
23027940	7	3	with	Reconstitution	1036:1049	arg1	mutant					1091:1096	the RelA(T305A) mutant	1075:1096	the RelA(T305A) mutant	1075:1096	Reconstitution of RelA null cells with the RelA(T305A) mutant illustrates the importance of this residue for NF-κB-dependent gene expression and cell survival.
23027940	0	4	theme	NF-κB	81:85	arg1	acetylation					87:97	NF-κB acetylation	81:97	NF-κB acetylation	81:97	Modification of RelA by O-linked N-acetylglucosamine links glucose metabolism to NF-κB acetylation and transcription.
23027940	6	5	theme	full-length	954:964	arg1	mutant					978:983	a full-length RelA(T305A) mutant	952:983	a full-length RelA(T305A) mutant	952:983	Furthermore, p300 fails to acetylate a full-length RelA(T305A) mutant, linking O-GlcNAc and acetylation events on NF-κB.
23027940	7	6	theme	NF-κB-dependent	1145:1159	arg1	expression					1166:1175	NF-κB-dependent gene expression	1145:1175	NF-κB-dependent gene expression	1145:1175	Reconstitution of RelA null cells with the RelA(T305A) mutant illustrates the importance of this residue for NF-κB-dependent gene expression and cell survival.
23027940	2	7	theme	O-linked	383:390	arg1	OGT					438:440	OGT	438:440	OGT	438:440	Using nuclear factor-κB (NF-κB) as a glucose-responsive transcription factor, we show that cells use the hexosamine biosynthesis pathway and O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) to potentiate gene expression in response to tumor necrosis factor (TNF) or etoposide.
23027940	2	7	theme	O-linked	383:390	arg1	transferase					425:435	O-linked β-N-acetylglucosamine (O-GlcNAc) transferase	383:435	O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT)	383:441	Using nuclear factor-κB (NF-κB) as a glucose-responsive transcription factor, we show that cells use the hexosamine biosynthesis pathway and O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) to potentiate gene expression in response to tumor necrosis factor (TNF) or etoposide.
23027940	8	8	attach	attachment	1253:1262	arg1	RelA					1290:1293	RelA	1290:1293	RelA	1290:1293	Our work provides evidence for a unique regulation where attachment of the O-GlcNAc moiety to RelA potentiates p300 acetylation and NF-κB transcription.
23027940	8	8	attach	attachment	1253:1262	arg2	moiety					1280:1285	the O-GlcNAc moiety	1267:1285	the O-GlcNAc moiety	1267:1285	Our work provides evidence for a unique regulation where attachment of the O-GlcNAc moiety to RelA potentiates p300 acetylation and NF-κB transcription.
23027940	4	9	dep	posttranslational	745:761	arg1	mark					763:766	mark	763:766	mark	763:766	Knockdown of OGT abolishes p300-mediated acetylation of RelA on K310, a posttranslational mark required for full NF-κB transcription.
23027940	5	10	from	attachment	872:881	arg1	RelA					909:912	RelA	909:912	RelA	909:912	Mapping studies reveal T305 as an important residue required for attachment of the O-GlcNAc moiety on RelA.
23027940	7	11	theme	residue	1133:1139	arg1	importance					1114:1123	the importance	1110:1123	the importance of this residue for NF-κB-dependent gene expression and cell survival	1110:1193	Reconstitution of RelA null cells with the RelA(T305A) mutant illustrates the importance of this residue for NF-κB-dependent gene expression and cell survival.
23027940	2	12	theme	β-N-acetylglucosamine	392:412	arg1	OGT					438:440	OGT	438:440	OGT	438:440	Using nuclear factor-κB (NF-κB) as a glucose-responsive transcription factor, we show that cells use the hexosamine biosynthesis pathway and O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) to potentiate gene expression in response to tumor necrosis factor (TNF) or etoposide.
23027940	2	12	theme	β-N-acetylglucosamine	392:412	arg1	transferase					425:435	O-linked β-N-acetylglucosamine (O-GlcNAc) transferase	383:435	O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT)	383:441	Using nuclear factor-κB (NF-κB) as a glucose-responsive transcription factor, we show that cells use the hexosamine biosynthesis pathway and O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) to potentiate gene expression in response to tumor necrosis factor (TNF) or etoposide.
23027940	2	13	theme	hexosamine	347:356	arg1	pathway					371:377	the hexosamine biosynthesis pathway	343:377	the hexosamine biosynthesis pathway	343:377	Using nuclear factor-κB (NF-κB) as a glucose-responsive transcription factor, we show that cells use the hexosamine biosynthesis pathway and O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) to potentiate gene expression in response to tumor necrosis factor (TNF) or etoposide.
23027940	2	14	link	O-linked	383:390	arg1	OGT					438:440	OGT	438:440	OGT	438:440	Using nuclear factor-κB (NF-κB) as a glucose-responsive transcription factor, we show that cells use the hexosamine biosynthesis pathway and O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) to potentiate gene expression in response to tumor necrosis factor (TNF) or etoposide.
23027940	2	14	link	O-linked	383:390	arg1	transferase					425:435	O-linked β-N-acetylglucosamine (O-GlcNAc) transferase	383:435	O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT)	383:441	Using nuclear factor-κB (NF-κB) as a glucose-responsive transcription factor, we show that cells use the hexosamine biosynthesis pathway and O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) to potentiate gene expression in response to tumor necrosis factor (TNF) or etoposide.
23027940	5	15	theme	O-GlcNAc	890:897	arg1	moiety					899:904	the O-GlcNAc moiety	886:904	the O-GlcNAc moiety	886:904	Mapping studies reveal T305 as an important residue required for attachment of the O-GlcNAc moiety on RelA.
23027940	5	16	attach	attachment	872:881	arg3	RelA					909:912	RelA	909:912	RelA	909:912	Mapping studies reveal T305 as an important residue required for attachment of the O-GlcNAc moiety on RelA.
23027940	5	16	attach	attachment	872:881	arg2	moiety					899:904	the O-GlcNAc moiety	886:904	the O-GlcNAc moiety	886:904	Mapping studies reveal T305 as an important residue required for attachment of the O-GlcNAc moiety on RelA.
23027940	8	17	theme	moiety	1280:1285	arg1	attachment					1253:1262	attachment	1253:1262	attachment of the O-GlcNAc moiety to RelA	1253:1293	Our work provides evidence for a unique regulation where attachment of the O-GlcNAc moiety to RelA potentiates p300 acetylation and NF-κB transcription.
23027940	7	18	theme	gene	1161:1164	arg1	expression					1166:1175	NF-κB-dependent gene expression	1145:1175	NF-κB-dependent gene expression	1145:1175	Reconstitution of RelA null cells with the RelA(T305A) mutant illustrates the importance of this residue for NF-κB-dependent gene expression and cell survival.
23027940	4	19	from	acetylation	714:724	arg1	K310					737:740	K310	737:740	K310	737:740	Knockdown of OGT abolishes p300-mediated acetylation of RelA on K310, a posttranslational mark required for full NF-κB transcription.
23027940	4	20	theme	p300-mediated	700:712	arg1	acetylation					714:724	p300-mediated acetylation	700:724	p300-mediated acetylation of RelA on K310	700:740	Knockdown of OGT abolishes p300-mediated acetylation of RelA on K310, a posttranslational mark required for full NF-κB transcription.
23027940	4	20	theme	p300-mediated	700:712	arg1	posttranslational					745:761	posttranslational	745:761	posttranslational	745:761	Knockdown of OGT abolishes p300-mediated acetylation of RelA on K310, a posttranslational mark required for full NF-κB transcription.
23027940	4	21	theme	NF-κB	786:790	arg1	transcription					792:804	full NF-κB transcription	781:804	full NF-κB transcription	781:804	Knockdown of OGT abolishes p300-mediated acetylation of RelA on K310, a posttranslational mark required for full NF-κB transcription.
23027940	4	22	theme	RelA	729:732	arg1	acetylation					714:724	p300-mediated acetylation	700:724	p300-mediated acetylation of RelA on K310	700:740	Knockdown of OGT abolishes p300-mediated acetylation of RelA on K310, a posttranslational mark required for full NF-κB transcription.
23027940	4	22	theme	RelA	729:732	arg1	posttranslational					745:761	posttranslational	745:761	posttranslational	745:761	Knockdown of OGT abolishes p300-mediated acetylation of RelA on K310, a posttranslational mark required for full NF-κB transcription.
23027940	6	23	theme	acetylation	1007:1017	arg1	events					1019:1024	O-GlcNAc and acetylation events	994:1024	O-GlcNAc and acetylation events	994:1024	Furthermore, p300 fails to acetylate a full-length RelA(T305A) mutant, linking O-GlcNAc and acetylation events on NF-κB.
23027940	0	24	attach	links	53:57	arg2	Modification					0:11	Modification	0:11	Modification of RelA by O-linked N-acetylglucosamine	0:51	Modification of RelA by O-linked N-acetylglucosamine links glucose metabolism to NF-κB acetylation and transcription.
23027940	0	24	attach	links	53:57	arg1	acetylation					87:97	NF-κB acetylation	81:97	NF-κB acetylation	81:97	Modification of RelA by O-linked N-acetylglucosamine links glucose metabolism to NF-κB acetylation and transcription.
23027940	0	24	attach	links	53:57	arg1	transcription					103:115	transcription	103:115	transcription	103:115	Modification of RelA by O-linked N-acetylglucosamine links glucose metabolism to NF-κB acetylation and transcription.
23027940	4	25	theme	full	781:784	arg1	transcription					792:804	full NF-κB transcription	781:804	full NF-κB transcription	781:804	Knockdown of OGT abolishes p300-mediated acetylation of RelA on K310, a posttranslational mark required for full NF-κB transcription.
23027940	1	26	theme	mammalian	225:233	arg1	cells					235:239	mammalian cells	225:239	mammalian cells	225:239	The molecular mechanisms linking glucose metabolism with active transcription remain undercharacterized in mammalian cells.
23027940	8	27	theme	NF-κB	1328:1332	arg1	transcription					1334:1346	NF-κB transcription	1328:1346	NF-κB transcription	1328:1346	Our work provides evidence for a unique regulation where attachment of the O-GlcNAc moiety to RelA potentiates p300 acetylation and NF-κB transcription.
23027940	0	28	link	O-linked	24:31	arg1	N-acetylglucosamine					33:51	O-linked N-acetylglucosamine	24:51	O-linked N-acetylglucosamine	24:51	Modification of RelA by O-linked N-acetylglucosamine links glucose metabolism to NF-κB acetylation and transcription.
23027940	5	29	theme	important	841:849	arg1	residue					851:857	an important residue	838:857	an important residue required for attachment of the O-GlcNAc moiety on RelA	838:912	Mapping studies reveal T305 as an important residue required for attachment of the O-GlcNAc moiety on RelA.
23027940	5	29	theme	important	841:849	arg1	T305					830:833	T305	830:833	T305	830:833	Mapping studies reveal T305 as an important residue required for attachment of the O-GlcNAc moiety on RelA.
23027940	2	30	theme	gene	457:460	arg1	expression					462:471	gene expression	457:471	gene expression in response to tumor necrosis factor (TNF) or etoposide	457:527	Using nuclear factor-κB (NF-κB) as a glucose-responsive transcription factor, we show that cells use the hexosamine biosynthesis pathway and O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) to potentiate gene expression in response to tumor necrosis factor (TNF) or etoposide.
23027940	0	31	theme	RelA	16:19	arg1	Modification					0:11	Modification	0:11	Modification of RelA by O-linked N-acetylglucosamine	0:51	Modification of RelA by O-linked N-acetylglucosamine links glucose metabolism to NF-κB acetylation and transcription.
23027940	6	32	theme	O-GlcNAc	994:1001	arg1	events					1019:1024	O-GlcNAc and acetylation events	994:1024	O-GlcNAc and acetylation events	994:1024	Furthermore, p300 fails to acetylate a full-length RelA(T305A) mutant, linking O-GlcNAc and acetylation events on NF-κB.
23027940	3	33	theme	Chromatin	530:538	arg1	assays					560:565	Chromatin immunoprecipitation assays	530:565	Chromatin immunoprecipitation assays	530:565	Chromatin immunoprecipitation assays demonstrate that, upon induction, OGT localizes to NF-κB-regulated promoters to enhance RelA acetylation.
23027940	6	34	theme	RelA	966:969	arg1	mutant					978:983	a full-length RelA(T305A) mutant	952:983	a full-length RelA(T305A) mutant	952:983	Furthermore, p300 fails to acetylate a full-length RelA(T305A) mutant, linking O-GlcNAc and acetylation events on NF-κB.
23027940	3	35	theme	immunoprecipitation	540:558	arg1	assays					560:565	Chromatin immunoprecipitation assays	530:565	Chromatin immunoprecipitation assays	530:565	Chromatin immunoprecipitation assays demonstrate that, upon induction, OGT localizes to NF-κB-regulated promoters to enhance RelA acetylation.
23027940	8	36	theme	p300	1307:1310	arg1	acetylation					1312:1322	p300 acetylation	1307:1322	p300 acetylation	1307:1322	Our work provides evidence for a unique regulation where attachment of the O-GlcNAc moiety to RelA potentiates p300 acetylation and NF-κB transcription.
23027940	8	37	theme	O-GlcNAc	1271:1278	arg1	moiety					1280:1285	the O-GlcNAc moiety	1267:1285	the O-GlcNAc moiety	1267:1285	Our work provides evidence for a unique regulation where attachment of the O-GlcNAc moiety to RelA potentiates p300 acetylation and NF-κB transcription.
23027940	5	38	theme	moiety	899:904	arg1	attachment					872:881	attachment	872:881	attachment of the O-GlcNAc moiety on RelA	872:912	Mapping studies reveal T305 as an important residue required for attachment of the O-GlcNAc moiety on RelA.
23027940	0	39	theme	O-linked	24:31	arg1	N-acetylglucosamine					33:51	O-linked N-acetylglucosamine	24:51	O-linked N-acetylglucosamine	24:51	Modification of RelA by O-linked N-acetylglucosamine links glucose metabolism to NF-κB acetylation and transcription.
23027940	7	40	theme	cell	1181:1184	arg1	survival					1186:1193	cell survival	1181:1193	cell survival	1181:1193	Reconstitution of RelA null cells with the RelA(T305A) mutant illustrates the importance of this residue for NF-κB-dependent gene expression and cell survival.
23027940	7	41	theme	RelA	1054:1057	arg1	cells					1064:1068	RelA null cells	1054:1068	RelA null cells	1054:1068	Reconstitution of RelA null cells with the RelA(T305A) mutant illustrates the importance of this residue for NF-κB-dependent gene expression and cell survival.
23027940	4	42	theme	OGT	686:688	arg1	Knockdown					673:681	Knockdown	673:681	Knockdown of OGT	673:688	Knockdown of OGT abolishes p300-mediated acetylation of RelA on K310, a posttranslational mark required for full NF-κB transcription.
23027940	0	43	theme	glucose	59:65	arg1	metabolism					67:76	glucose metabolism	59:76	glucose metabolism	59:76	Modification of RelA by O-linked N-acetylglucosamine links glucose metabolism to NF-κB acetylation and transcription.
23027940	8	44	theme	unique	1229:1234	arg1	regulation					1236:1245	a unique regulation	1227:1245	a unique regulation where attachment of the O-GlcNAc moiety to RelA potentiates p300 acetylation and NF-κB transcription	1227:1346	Our work provides evidence for a unique regulation where attachment of the O-GlcNAc moiety to RelA potentiates p300 acetylation and NF-κB transcription.
23027940	7	45	theme	null	1059:1062	arg1	cells					1064:1068	RelA null cells	1054:1068	RelA null cells	1054:1068	Reconstitution of RelA null cells with the RelA(T305A) mutant illustrates the importance of this residue for NF-κB-dependent gene expression and cell survival.
23027940	1	46	theme	molecular	122:130	arg1	mechanisms					132:141	The molecular mechanisms	118:141	The molecular mechanisms linking glucose metabolism with active transcription	118:194	The molecular mechanisms linking glucose metabolism with active transcription remain undercharacterized in mammalian cells.
23027940	2	47	theme	tumor	488:492	arg1	TNF					511:513	TNF	511:513	TNF	511:513	Using nuclear factor-κB (NF-κB) as a glucose-responsive transcription factor, we show that cells use the hexosamine biosynthesis pathway and O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) to potentiate gene expression in response to tumor necrosis factor (TNF) or etoposide.
23027940	2	47	theme	tumor	488:492	arg1	factor					503:508	tumor necrosis factor	488:508	tumor necrosis factor (TNF)	488:514	Using nuclear factor-κB (NF-κB) as a glucose-responsive transcription factor, we show that cells use the hexosamine biosynthesis pathway and O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) to potentiate gene expression in response to tumor necrosis factor (TNF) or etoposide.
23027940	7	48	theme	RelA	1079:1082	arg1	mutant					1091:1096	the RelA(T305A) mutant	1075:1096	the RelA(T305A) mutant	1075:1096	Reconstitution of RelA null cells with the RelA(T305A) mutant illustrates the importance of this residue for NF-κB-dependent gene expression and cell survival.
23027940	2	49	theme	nuclear	248:254	arg1	NF-κB					267:271	NF-κB	267:271	NF-κB	267:271	Using nuclear factor-κB (NF-κB) as a glucose-responsive transcription factor, we show that cells use the hexosamine biosynthesis pathway and O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) to potentiate gene expression in response to tumor necrosis factor (TNF) or etoposide.
23027940	2	49	theme	nuclear	248:254	arg1	factor-κB					256:264	nuclear factor-κB	248:264	nuclear factor-κB (NF-κB)	248:272	Using nuclear factor-κB (NF-κB) as a glucose-responsive transcription factor, we show that cells use the hexosamine biosynthesis pathway and O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) to potentiate gene expression in response to tumor necrosis factor (TNF) or etoposide.
23027940	2	49	theme	nuclear	248:254	arg1	factor					312:317	a glucose-responsive transcription factor	277:317	a glucose-responsive transcription factor	277:317	Using nuclear factor-κB (NF-κB) as a glucose-responsive transcription factor, we show that cells use the hexosamine biosynthesis pathway and O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) to potentiate gene expression in response to tumor necrosis factor (TNF) or etoposide.
23027940	3	50	theme	NF-κB-regulated	618:632	arg1	promoters					634:642	NF-κB-regulated promoters	618:642	NF-κB-regulated promoters	618:642	Chromatin immunoprecipitation assays demonstrate that, upon induction, OGT localizes to NF-κB-regulated promoters to enhance RelA acetylation.
23027940	1	51	from	cells	235:239	arg1	undercharacterized					203:220	undercharacterized	203:220	undercharacterized	203:220	The molecular mechanisms linking glucose metabolism with active transcription remain undercharacterized in mammalian cells.
23027940	6	52	theme	T305A	971:975	arg1	mutant					978:983	a full-length RelA(T305A) mutant	952:983	a full-length RelA(T305A) mutant	952:983	Furthermore, p300 fails to acetylate a full-length RelA(T305A) mutant, linking O-GlcNAc and acetylation events on NF-κB.
23027940	7	53	theme	cells	1064:1068	arg1	Reconstitution					1036:1049	Reconstitution	1036:1049	Reconstitution of RelA null cells with the RelA(T305A) mutant	1036:1096	Reconstitution of RelA null cells with the RelA(T305A) mutant illustrates the importance of this residue for NF-κB-dependent gene expression and cell survival.
23027940	2	54	theme	transcription	298:310	arg1	factor					312:317	a glucose-responsive transcription factor	277:317	a glucose-responsive transcription factor	277:317	Using nuclear factor-κB (NF-κB) as a glucose-responsive transcription factor, we show that cells use the hexosamine biosynthesis pathway and O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) to potentiate gene expression in response to tumor necrosis factor (TNF) or etoposide.
23027940	2	54	theme	transcription	298:310	arg1	factor-κB					256:264	nuclear factor-κB	248:264	nuclear factor-κB (NF-κB)	248:272	Using nuclear factor-κB (NF-κB) as a glucose-responsive transcription factor, we show that cells use the hexosamine biosynthesis pathway and O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) to potentiate gene expression in response to tumor necrosis factor (TNF) or etoposide.
23027940	2	55	theme	biosynthesis	358:369	arg1	pathway					371:377	the hexosamine biosynthesis pathway	343:377	the hexosamine biosynthesis pathway	343:377	Using nuclear factor-κB (NF-κB) as a glucose-responsive transcription factor, we show that cells use the hexosamine biosynthesis pathway and O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) to potentiate gene expression in response to tumor necrosis factor (TNF) or etoposide.
23027940	2	56	theme	glucose-responsive	279:296	arg1	factor					312:317	a glucose-responsive transcription factor	277:317	a glucose-responsive transcription factor	277:317	Using nuclear factor-κB (NF-κB) as a glucose-responsive transcription factor, we show that cells use the hexosamine biosynthesis pathway and O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) to potentiate gene expression in response to tumor necrosis factor (TNF) or etoposide.
23027940	2	56	theme	glucose-responsive	279:296	arg1	factor-κB					256:264	nuclear factor-κB	248:264	nuclear factor-κB (NF-κB)	248:272	Using nuclear factor-κB (NF-κB) as a glucose-responsive transcription factor, we show that cells use the hexosamine biosynthesis pathway and O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) to potentiate gene expression in response to tumor necrosis factor (TNF) or etoposide.
23027940	1	57	theme	glucose	151:157	arg1	metabolism					159:168	glucose metabolism	151:168	glucose metabolism	151:168	The molecular mechanisms linking glucose metabolism with active transcription remain undercharacterized in mammalian cells.
23027940	5	58	theme	Mapping	807:813	arg1	studies					815:821	Mapping studies	807:821	Mapping studies	807:821	Mapping studies reveal T305 as an important residue required for attachment of the O-GlcNAc moiety on RelA.
23027940	7	59	theme	T305A	1084:1088	arg1	mutant					1091:1096	the RelA(T305A) mutant	1075:1096	the RelA(T305A) mutant	1075:1096	Reconstitution of RelA null cells with the RelA(T305A) mutant illustrates the importance of this residue for NF-κB-dependent gene expression and cell survival.
23027940	2	60	theme	O-GlcNAc	415:422	arg1	OGT					438:440	OGT	438:440	OGT	438:440	Using nuclear factor-κB (NF-κB) as a glucose-responsive transcription factor, we show that cells use the hexosamine biosynthesis pathway and O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) to potentiate gene expression in response to tumor necrosis factor (TNF) or etoposide.
23027940	2	60	theme	O-GlcNAc	415:422	arg1	transferase					425:435	O-linked β-N-acetylglucosamine (O-GlcNAc) transferase	383:435	O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT)	383:441	Using nuclear factor-κB (NF-κB) as a glucose-responsive transcription factor, we show that cells use the hexosamine biosynthesis pathway and O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) to potentiate gene expression in response to tumor necrosis factor (TNF) or etoposide.
23027940	2	61	theme	necrosis	494:501	arg1	TNF					511:513	TNF	511:513	TNF	511:513	Using nuclear factor-κB (NF-κB) as a glucose-responsive transcription factor, we show that cells use the hexosamine biosynthesis pathway and O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) to potentiate gene expression in response to tumor necrosis factor (TNF) or etoposide.
23027940	2	61	theme	necrosis	494:501	arg1	factor					503:508	tumor necrosis factor	488:508	tumor necrosis factor (TNF)	488:514	Using nuclear factor-κB (NF-κB) as a glucose-responsive transcription factor, we show that cells use the hexosamine biosynthesis pathway and O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) to potentiate gene expression in response to tumor necrosis factor (TNF) or etoposide.
23027940	3	62	theme	RelA	655:658	arg1	acetylation					660:670	RelA acetylation	655:670	RelA acetylation	655:670	Chromatin immunoprecipitation assays demonstrate that, upon induction, OGT localizes to NF-κB-regulated promoters to enhance RelA acetylation.
19671924	2	0	theme	feedback	366:373	arg1	regulation					392:401	feedback and feed forward regulation	366:401	regulation	392:401	Ser/Thr kinases impact the metabolic and mitogenic effects elicited by insulin and IGF-1 through feedback and feed forward regulation at the level of IRS-1.
19671924	10	1	from	GlcNAc	1686:1691	arg1	cells					1708:1712	HEPG2 liver cells	1696:1712	HEPG2 liver cells	1696:1712	The accumulation of IRS-1 Ser(1011) GlcNAc in HEPG2 liver cells and MC3T3-E1 preosteoblasts upon inhibition of O-GlcNAcase indicates that O-GlcNAcylation of endogenously expressed IRS-1 is a dynamic process that occurs at normal glucose concentrations (5 mm).
19671924	10	1	from	GlcNAc	1686:1691	arg1	preosteoblasts					1727:1740	MC3T3-E1 preosteoblasts	1718:1740	MC3T3-E1 preosteoblasts	1718:1740	The accumulation of IRS-1 Ser(1011) GlcNAc in HEPG2 liver cells and MC3T3-E1 preosteoblasts upon inhibition of O-GlcNAcase indicates that O-GlcNAcylation of endogenously expressed IRS-1 is a dynamic process that occurs at normal glucose concentrations (5 mm).
19671924	5	2	from	residues	943:950	arg1	rich					851:854	rich	851:854	rich	851:854	Tandem mass spectrometric analysis of IRS-1, exogenously expressed in HEK293 cells, revealed that the C terminus, which is rich in docking sites for SH2 domain-containing proteins, was O-GlcNAc-modified at multiple residues.
19671924	5	2	from	residues	943:950	arg1	terminus					832:839	the C terminus	826:839	the C terminus	826:839	Tandem mass spectrometric analysis of IRS-1, exogenously expressed in HEK293 cells, revealed that the C terminus, which is rich in docking sites for SH2 domain-containing proteins, was O-GlcNAc-modified at multiple residues.
19671924	5	2	from	residues	943:950	arg1	O-GlcNAc-modified					913:929	O-GlcNAc-modified	913:929	O-GlcNAc-modified	913:929	Tandem mass spectrometric analysis of IRS-1, exogenously expressed in HEK293 cells, revealed that the C terminus, which is rich in docking sites for SH2 domain-containing proteins, was O-GlcNAc-modified at multiple residues.
19671924	4	3	theme	modification	613:624	arg1	effects					593:599	the functional effects	578:599	the functional effects of O-GlcNAc modification on IRS-1-mediated signaling	578:652	To facilitate the understanding of the functional effects of O-GlcNAc modification on IRS-1-mediated signaling, we identified the sites of O-GlcNAc modification of rat and human IRS-1.
19671924	2	4	theme	metabolic	296:304	arg1	effects					320:326	the metabolic and mitogenic effects	292:326	the metabolic and mitogenic effects elicited by insulin and IGF-1 through feedback and feed forward regulation at the level of IRS-1	292:423	Ser/Thr kinases impact the metabolic and mitogenic effects elicited by insulin and IGF-1 through feedback and feed forward regulation at the level of IRS-1.
19671924	11	5	theme	known	1953:1957	arg1	sites					2003:2007	any known or newly identified Ser/Thr phosphorylation sites	1949:2007	any known or newly identified Ser/Thr phosphorylation sites	1949:2007	O-GlcNAc modification did not occur at any known or newly identified Ser/Thr phosphorylation sites and in most cases occurred simultaneously with phosphorylation of nearby residues.
19671924	0	6	link	O-linked	0:7	arg1	modification					29:40	O-linked N-acetylglucosamine modification	0:40	O-linked N-acetylglucosamine modification of insulin receptor substrate-1	0:72	O-linked N-acetylglucosamine modification of insulin receptor substrate-1 occurs in close proximity to multiple SH2 domain binding motifs.
19671924	4	7	theme	O-GlcNAc	682:689	arg1	modification					691:702	O-GlcNAc modification	682:702	O-GlcNAc modification of rat and human IRS-1	682:725	To facilitate the understanding of the functional effects of O-GlcNAc modification on IRS-1-mediated signaling, we identified the sites of O-GlcNAc modification of rat and human IRS-1.
19671924	7	8	theme	Human	1035:1039	arg1	IRS-1					1041:1045	Human IRS-1	1035:1045	Human IRS-1	1035:1045	Human IRS-1 was O-GlcNAc-modified at Ser(984) or Ser(985), at Ser(1011), and possibly at multiple sites within residues 1025-1045.
19671924	0	9	theme	O-linked	0:7	arg1	modification					29:40	O-linked N-acetylglucosamine modification	0:40	O-linked N-acetylglucosamine modification of insulin receptor substrate-1	0:72	O-linked N-acetylglucosamine modification of insulin receptor substrate-1 occurs in close proximity to multiple SH2 domain binding motifs.
19671924	10	10	from	cells	1708:1712	arg1	accumulation					1654:1665	The accumulation	1650:1665	The accumulation of IRS-1 Ser(1011) GlcNAc in HEPG2 liver cells and MC3T3-E1 preosteoblasts upon inhibition of O-GlcNAcase	1650:1771	The accumulation of IRS-1 Ser(1011) GlcNAc in HEPG2 liver cells and MC3T3-E1 preosteoblasts upon inhibition of O-GlcNAcase indicates that O-GlcNAcylation of endogenously expressed IRS-1 is a dynamic process that occurs at normal glucose concentrations (5 mm).
19671924	9	11	theme	IRS-1	1512:1516	arg1	GlcNAc					1528:1533	human IRS-1 Ser(1011) GlcNAc	1506:1533	human IRS-1 Ser(1011) GlcNAc	1506:1533	Immunoblot analysis using an antibody generated against human IRS-1 Ser(1011) GlcNAc further confirmed the site of attachment and the identity of the +203.2-Da mass shift as beta-N-acetylglucosamine.
19671924	12	12	theme	additional	2156:2165	arg1	layer					2167:2171	an additional layer	2153:2171	an additional layer of posttranslational regulation that may impact the specificity of effects elicited by insulin and IGF-1	2153:2276	These findings suggest that O-GlcNAc modification represents an additional layer of posttranslational regulation that may impact the specificity of effects elicited by insulin and IGF-1.
19671924	8	13	from	IRS-1	1252:1256	arg1	modification					1175:1186	O-GlcNAc modification	1166:1186	O-GlcNAc modification at a conserved residue in rat (Ser(1009)) and human (Ser(1011)) IRS-1	1166:1256	O-GlcNAc modification at a conserved residue in rat (Ser(1009)) and human (Ser(1011)) IRS-1 is adjacent to a putative binding motif for the N-terminal SH2 domains of p85alpha and p85beta regulatory subunits of phosphatidylinositol 3-kinase and the tyrosine phosphatase SHP2 (PTPN11).
19671924	8	13	from	IRS-1	1252:1256	arg1	rat					1214:1216	rat	1214:1216	rat	1214:1216	O-GlcNAc modification at a conserved residue in rat (Ser(1009)) and human (Ser(1011)) IRS-1 is adjacent to a putative binding motif for the N-terminal SH2 domains of p85alpha and p85beta regulatory subunits of phosphatidylinositol 3-kinase and the tyrosine phosphatase SHP2 (PTPN11).
19671924	1	14	theme	phosphorylated	188:201	arg1	protein					211:217	a highly phosphorylated adaptor protein	179:217	a highly phosphorylated adaptor protein critical to insulin and IGF-1 receptor signaling	179:266	Insulin receptor substrate-1 (IRS-1) is a highly phosphorylated adaptor protein critical to insulin and IGF-1 receptor signaling.
19671924	1	14	theme	phosphorylated	188:201	arg1	substrate-1					156:166	Insulin receptor substrate-1	139:166	Insulin receptor substrate-1 (IRS-1)	139:174	Insulin receptor substrate-1 (IRS-1) is a highly phosphorylated adaptor protein critical to insulin and IGF-1 receptor signaling.
19671924	12	15	theme	O-GlcNAc	2120:2127	arg1	modification					2129:2140	O-GlcNAc modification	2120:2140	O-GlcNAc modification	2120:2140	These findings suggest that O-GlcNAc modification represents an additional layer of posttranslational regulation that may impact the specificity of effects elicited by insulin and IGF-1.
19671924	5	16	theme	Tandem	728:733	arg1	analysis					754:761	Tandem mass spectrometric analysis	728:761	Tandem mass spectrometric analysis	728:761	Tandem mass spectrometric analysis of IRS-1, exogenously expressed in HEK293 cells, revealed that the C terminus, which is rich in docking sites for SH2 domain-containing proteins, was O-GlcNAc-modified at multiple residues.
19671924	2	17	theme	mitogenic	310:318	arg1	effects					320:326	the metabolic and mitogenic effects	292:326	the metabolic and mitogenic effects elicited by insulin and IGF-1 through feedback and feed forward regulation at the level of IRS-1	292:423	Ser/Thr kinases impact the metabolic and mitogenic effects elicited by insulin and IGF-1 through feedback and feed forward regulation at the level of IRS-1.
19671924	12	18	theme	posttranslational	2176:2192	arg1	regulation					2194:2203	posttranslational regulation	2176:2203	posttranslational regulation	2176:2203	These findings suggest that O-GlcNAc modification represents an additional layer of posttranslational regulation that may impact the specificity of effects elicited by insulin and IGF-1.
19671924	10	19	theme	IRS-1	1830:1834	arg1	O-GlcNAcylation					1788:1802	O-GlcNAcylation	1788:1802	O-GlcNAcylation of endogenously expressed IRS-1	1788:1834	The accumulation of IRS-1 Ser(1011) GlcNAc in HEPG2 liver cells and MC3T3-E1 preosteoblasts upon inhibition of O-GlcNAcase indicates that O-GlcNAcylation of endogenously expressed IRS-1 is a dynamic process that occurs at normal glucose concentrations (5 mm).
19671924	10	19	theme	IRS-1	1830:1834	arg1	process					1849:1855	a dynamic process	1839:1855	a dynamic process that occurs at normal glucose concentrations (5 mm)	1839:1907	The accumulation of IRS-1 Ser(1011) GlcNAc in HEPG2 liver cells and MC3T3-E1 preosteoblasts upon inhibition of O-GlcNAcase indicates that O-GlcNAcylation of endogenously expressed IRS-1 is a dynamic process that occurs at normal glucose concentrations (5 mm).
19671924	5	20	theme	spectrometric	740:752	arg1	analysis					754:761	Tandem mass spectrometric analysis	728:761	Tandem mass spectrometric analysis	728:761	Tandem mass spectrometric analysis of IRS-1, exogenously expressed in HEK293 cells, revealed that the C terminus, which is rich in docking sites for SH2 domain-containing proteins, was O-GlcNAc-modified at multiple residues.
19671924	5	21	from	rich	851:854	arg1	sites					867:871	docking sites	859:871	docking sites for SH2 domain-containing proteins	859:906	Tandem mass spectrometric analysis of IRS-1, exogenously expressed in HEK293 cells, revealed that the C terminus, which is rich in docking sites for SH2 domain-containing proteins, was O-GlcNAc-modified at multiple residues.
19671924	7	22	from	Ser	1097:1099	arg1	O-GlcNAc-modified					1051:1067	O-GlcNAc-modified	1051:1067	O-GlcNAc-modified	1051:1067	Human IRS-1 was O-GlcNAc-modified at Ser(984) or Ser(985), at Ser(1011), and possibly at multiple sites within residues 1025-1045.
19671924	8	23	theme	O-GlcNAc	1166:1173	arg1	modification					1175:1186	O-GlcNAc modification	1166:1186	O-GlcNAc modification at a conserved residue in rat (Ser(1009)) and human (Ser(1011)) IRS-1	1166:1256	O-GlcNAc modification at a conserved residue in rat (Ser(1009)) and human (Ser(1011)) IRS-1 is adjacent to a putative binding motif for the N-terminal SH2 domains of p85alpha and p85beta regulatory subunits of phosphatidylinositol 3-kinase and the tyrosine phosphatase SHP2 (PTPN11).
19671924	8	24	theme	putative	1275:1282	arg1	motif					1292:1296	a putative binding motif	1273:1296	a putative binding motif for the N-terminal SH2 domains of p85alpha and p85beta regulatory subunits of phosphatidylinositol 3-kinase and the tyrosine phosphatase SHP2 (PTPN11)	1273:1447	O-GlcNAc modification at a conserved residue in rat (Ser(1009)) and human (Ser(1011)) IRS-1 is adjacent to a putative binding motif for the N-terminal SH2 domains of p85alpha and p85beta regulatory subunits of phosphatidylinositol 3-kinase and the tyrosine phosphatase SHP2 (PTPN11).
19671924	2	25	theme	Ser/Thr	269:275	arg1	kinases					277:283	Ser/Thr kinases	269:283	Ser/Thr kinases	269:283	Ser/Thr kinases impact the metabolic and mitogenic effects elicited by insulin and IGF-1 through feedback and feed forward regulation at the level of IRS-1.
19671924	1	26	theme	receptor	147:154	arg1	protein					211:217	a highly phosphorylated adaptor protein	179:217	a highly phosphorylated adaptor protein critical to insulin and IGF-1 receptor signaling	179:266	Insulin receptor substrate-1 (IRS-1) is a highly phosphorylated adaptor protein critical to insulin and IGF-1 receptor signaling.
19671924	1	26	theme	receptor	147:154	arg1	IRS-1					169:173	IRS-1	169:173	IRS-1	169:173	Insulin receptor substrate-1 (IRS-1) is a highly phosphorylated adaptor protein critical to insulin and IGF-1 receptor signaling.
19671924	1	26	theme	receptor	147:154	arg1	substrate-1					156:166	Insulin receptor substrate-1	139:166	Insulin receptor substrate-1 (IRS-1)	139:174	Insulin receptor substrate-1 (IRS-1) is a highly phosphorylated adaptor protein critical to insulin and IGF-1 receptor signaling.
19671924	5	27	theme	multiple	934:941	arg1	residues					943:950	multiple residues	934:950	multiple residues	934:950	Tandem mass spectrometric analysis of IRS-1, exogenously expressed in HEK293 cells, revealed that the C terminus, which is rich in docking sites for SH2 domain-containing proteins, was O-GlcNAc-modified at multiple residues.
19671924	8	28	theme	conserved	1193:1201	arg1	Ser					1219:1221	Ser(1009)	1219:1227	Ser(1009)	1219:1227	O-GlcNAc modification at a conserved residue in rat (Ser(1009)) and human (Ser(1011)) IRS-1 is adjacent to a putative binding motif for the N-terminal SH2 domains of p85alpha and p85beta regulatory subunits of phosphatidylinositol 3-kinase and the tyrosine phosphatase SHP2 (PTPN11).
19671924	8	28	theme	conserved	1193:1201	arg1	residue					1203:1209	a conserved residue	1191:1209	a conserved residue in rat (Ser(1009))	1191:1228	O-GlcNAc modification at a conserved residue in rat (Ser(1009)) and human (Ser(1011)) IRS-1 is adjacent to a putative binding motif for the N-terminal SH2 domains of p85alpha and p85beta regulatory subunits of phosphatidylinositol 3-kinase and the tyrosine phosphatase SHP2 (PTPN11).
19671924	4	29	from	signaling	644:652	arg1	understanding					561:573	the understanding	557:573	the understanding of the functional effects of O-GlcNAc modification on IRS-1-mediated signaling	557:652	To facilitate the understanding of the functional effects of O-GlcNAc modification on IRS-1-mediated signaling, we identified the sites of O-GlcNAc modification of rat and human IRS-1.
19671924	4	30	theme	functional	582:591	arg1	effects					593:599	the functional effects	578:599	the functional effects of O-GlcNAc modification on IRS-1-mediated signaling	578:652	To facilitate the understanding of the functional effects of O-GlcNAc modification on IRS-1-mediated signaling, we identified the sites of O-GlcNAc modification of rat and human IRS-1.
19671924	4	31	theme	IRS-1	721:725	arg1	modification					691:702	O-GlcNAc modification	682:702	O-GlcNAc modification of rat and human IRS-1	682:725	To facilitate the understanding of the functional effects of O-GlcNAc modification on IRS-1-mediated signaling, we identified the sites of O-GlcNAc modification of rat and human IRS-1.
19671924	10	32	theme	normal	1872:1877	arg1	concentrations					1887:1900	normal glucose concentrations	1872:1900	normal glucose concentrations (5 mm)	1872:1907	The accumulation of IRS-1 Ser(1011) GlcNAc in HEPG2 liver cells and MC3T3-E1 preosteoblasts upon inhibition of O-GlcNAcase indicates that O-GlcNAcylation of endogenously expressed IRS-1 is a dynamic process that occurs at normal glucose concentrations (5 mm).
19671924	10	32	theme	normal	1872:1877	arg1	mm					1905:1906	5 mm	1903:1906	5 mm	1903:1906	The accumulation of IRS-1 Ser(1011) GlcNAc in HEPG2 liver cells and MC3T3-E1 preosteoblasts upon inhibition of O-GlcNAcase indicates that O-GlcNAcylation of endogenously expressed IRS-1 is a dynamic process that occurs at normal glucose concentrations (5 mm).
19671924	5	33	theme	HEK293	798:803	arg1	cells					805:809	HEK293 cells	798:809	HEK293 cells	798:809	Tandem mass spectrometric analysis of IRS-1, exogenously expressed in HEK293 cells, revealed that the C terminus, which is rich in docking sites for SH2 domain-containing proteins, was O-GlcNAc-modified at multiple residues.
19671924	11	34	theme	nearby	2075:2080	arg1	residues					2082:2089	nearby residues	2075:2089	nearby residues	2075:2089	O-GlcNAc modification did not occur at any known or newly identified Ser/Thr phosphorylation sites and in most cases occurred simultaneously with phosphorylation of nearby residues.
19671924	8	35	theme	SH2	1317:1319	arg1	p85alpha					1332:1339	p85alpha	1332:1339	p85alpha	1332:1339	O-GlcNAc modification at a conserved residue in rat (Ser(1009)) and human (Ser(1011)) IRS-1 is adjacent to a putative binding motif for the N-terminal SH2 domains of p85alpha and p85beta regulatory subunits of phosphatidylinositol 3-kinase and the tyrosine phosphatase SHP2 (PTPN11).
19671924	8	35	theme	SH2	1317:1319	arg1	domains					1321:1327	the N-terminal SH2 domains	1302:1327	the N-terminal SH2 domains of p85alpha and p85beta regulatory subunits of phosphatidylinositol 3-kinase and the tyrosine phosphatase SHP2 (PTPN11)	1302:1447	O-GlcNAc modification at a conserved residue in rat (Ser(1009)) and human (Ser(1011)) IRS-1 is adjacent to a putative binding motif for the N-terminal SH2 domains of p85alpha and p85beta regulatory subunits of phosphatidylinositol 3-kinase and the tyrosine phosphatase SHP2 (PTPN11).
19671924	8	35	theme	SH2	1317:1319	arg1	subunits					1364:1371	p85beta regulatory subunits	1345:1371	p85beta regulatory subunits	1345:1371	O-GlcNAc modification at a conserved residue in rat (Ser(1009)) and human (Ser(1011)) IRS-1 is adjacent to a putative binding motif for the N-terminal SH2 domains of p85alpha and p85beta regulatory subunits of phosphatidylinositol 3-kinase and the tyrosine phosphatase SHP2 (PTPN11).
19671924	0	36	theme	multiple	103:110	arg1	motifs					131:136	multiple SH2 domain binding motifs	103:136	multiple SH2 domain binding motifs	103:136	O-linked N-acetylglucosamine modification of insulin receptor substrate-1 occurs in close proximity to multiple SH2 domain binding motifs.
19671924	3	37	theme	IRS-1	446:450	arg1	IRS-1					446:450	IRS-1	446:450	IRS-1	446:450	Ser/Thr residues of IRS-1 are also O-GlcNAc-modified, which may influence the phosphorylation status of the protein.
19671924	3	37	theme	IRS-1	446:450	arg1	residues					434:441	Ser/Thr residues	426:441	Ser/Thr residues of IRS-1	426:450	Ser/Thr residues of IRS-1 are also O-GlcNAc-modified, which may influence the phosphorylation status of the protein.
19671924	0	38	theme	domain	116:121	arg1	motifs					131:136	multiple SH2 domain binding motifs	103:136	multiple SH2 domain binding motifs	103:136	O-linked N-acetylglucosamine modification of insulin receptor substrate-1 occurs in close proximity to multiple SH2 domain binding motifs.
19671924	9	39	theme	mass	1610:1613	arg1	shift					1615:1619	the +203.2-Da mass shift	1596:1619	the +203.2-Da mass shift	1596:1619	Immunoblot analysis using an antibody generated against human IRS-1 Ser(1011) GlcNAc further confirmed the site of attachment and the identity of the +203.2-Da mass shift as beta-N-acetylglucosamine.
19671924	6	40	from	Ser	998:1000	arg1	O-GlcNAc-modified					967:983	O-GlcNAc-modified	967:983	O-GlcNAc-modified	967:983	Rat IRS-1 was O-GlcNAc-modified at Ser(914), Ser(1009), Ser(1036), and Ser(1041).
19671924	11	41	theme	phosphorylation	1987:2001	arg1	sites					2003:2007	any known or newly identified Ser/Thr phosphorylation sites	1949:2007	any known or newly identified Ser/Thr phosphorylation sites	1949:2007	O-GlcNAc modification did not occur at any known or newly identified Ser/Thr phosphorylation sites and in most cases occurred simultaneously with phosphorylation of nearby residues.
19671924	5	42	theme	C	830:830	arg1	rich					851:854	rich	851:854	rich	851:854	Tandem mass spectrometric analysis of IRS-1, exogenously expressed in HEK293 cells, revealed that the C terminus, which is rich in docking sites for SH2 domain-containing proteins, was O-GlcNAc-modified at multiple residues.
19671924	5	42	theme	C	830:830	arg1	terminus					832:839	the C terminus	826:839	the C terminus	826:839	Tandem mass spectrometric analysis of IRS-1, exogenously expressed in HEK293 cells, revealed that the C terminus, which is rich in docking sites for SH2 domain-containing proteins, was O-GlcNAc-modified at multiple residues.
19671924	5	42	theme	C	830:830	arg1	O-GlcNAc-modified					913:929	O-GlcNAc-modified	913:929	O-GlcNAc-modified	913:929	Tandem mass spectrometric analysis of IRS-1, exogenously expressed in HEK293 cells, revealed that the C terminus, which is rich in docking sites for SH2 domain-containing proteins, was O-GlcNAc-modified at multiple residues.
19671924	8	43	theme	regulatory	1353:1362	arg1	subunits					1364:1371	p85beta regulatory subunits	1345:1371	p85beta regulatory subunits	1345:1371	O-GlcNAc modification at a conserved residue in rat (Ser(1009)) and human (Ser(1011)) IRS-1 is adjacent to a putative binding motif for the N-terminal SH2 domains of p85alpha and p85beta regulatory subunits of phosphatidylinositol 3-kinase and the tyrosine phosphatase SHP2 (PTPN11).
19671924	4	44	from	understanding	561:573	arg1	signaling					644:652	IRS-1-mediated signaling	629:652	IRS-1-mediated signaling	629:652	To facilitate the understanding of the functional effects of O-GlcNAc modification on IRS-1-mediated signaling, we identified the sites of O-GlcNAc modification of rat and human IRS-1.
19671924	2	45	theme	IRS-1	419:423	arg1	level					410:414	the level	406:414	the level of IRS-1	406:423	Ser/Thr kinases impact the metabolic and mitogenic effects elicited by insulin and IGF-1 through feedback and feed forward regulation at the level of IRS-1.
19671924	0	46	theme	insulin	45:51	arg1	substrate-1					62:72	insulin receptor substrate-1	45:72	insulin receptor substrate-1	45:72	O-linked N-acetylglucosamine modification of insulin receptor substrate-1 occurs in close proximity to multiple SH2 domain binding motifs.
19671924	11	47	theme	most	2016:2019	arg1	cases					2021:2025	most cases	2016:2025	most cases	2016:2025	O-GlcNAc modification did not occur at any known or newly identified Ser/Thr phosphorylation sites and in most cases occurred simultaneously with phosphorylation of nearby residues.
19671924	8	48	theme	3-kinase	1397:1404	arg1	p85alpha					1332:1339	p85alpha	1332:1339	p85alpha	1332:1339	O-GlcNAc modification at a conserved residue in rat (Ser(1009)) and human (Ser(1011)) IRS-1 is adjacent to a putative binding motif for the N-terminal SH2 domains of p85alpha and p85beta regulatory subunits of phosphatidylinositol 3-kinase and the tyrosine phosphatase SHP2 (PTPN11).
19671924	8	48	theme	3-kinase	1397:1404	arg1	subunits					1364:1371	p85beta regulatory subunits	1345:1371	p85beta regulatory subunits	1345:1371	O-GlcNAc modification at a conserved residue in rat (Ser(1009)) and human (Ser(1011)) IRS-1 is adjacent to a putative binding motif for the N-terminal SH2 domains of p85alpha and p85beta regulatory subunits of phosphatidylinositol 3-kinase and the tyrosine phosphatase SHP2 (PTPN11).
19671924	10	49	theme	IRS-1	1670:1674	arg1	GlcNAc					1686:1691	IRS-1 Ser(1011) GlcNAc	1670:1691	IRS-1 Ser(1011) GlcNAc in HEPG2 liver cells and MC3T3-E1 preosteoblasts	1670:1740	The accumulation of IRS-1 Ser(1011) GlcNAc in HEPG2 liver cells and MC3T3-E1 preosteoblasts upon inhibition of O-GlcNAcase indicates that O-GlcNAcylation of endogenously expressed IRS-1 is a dynamic process that occurs at normal glucose concentrations (5 mm).
19671924	0	50	theme	substrate-1	62:72	arg1	modification					29:40	O-linked N-acetylglucosamine modification	0:40	O-linked N-acetylglucosamine modification of insulin receptor substrate-1	0:72	O-linked N-acetylglucosamine modification of insulin receptor substrate-1 occurs in close proximity to multiple SH2 domain binding motifs.
19671924	7	51	from	Ser	1072:1074	arg1	O-GlcNAc-modified					1051:1067	O-GlcNAc-modified	1051:1067	O-GlcNAc-modified	1051:1067	Human IRS-1 was O-GlcNAc-modified at Ser(984) or Ser(985), at Ser(1011), and possibly at multiple sites within residues 1025-1045.
19671924	2	52	from	level	410:414	arg1	regulation					392:401	feedback and feed forward regulation	366:401	regulation	392:401	Ser/Thr kinases impact the metabolic and mitogenic effects elicited by insulin and IGF-1 through feedback and feed forward regulation at the level of IRS-1.
19671924	8	53	theme	phosphatase	1423:1433	arg1	PTPN11					1441:1446	PTPN11	1441:1446	PTPN11	1441:1446	O-GlcNAc modification at a conserved residue in rat (Ser(1009)) and human (Ser(1011)) IRS-1 is adjacent to a putative binding motif for the N-terminal SH2 domains of p85alpha and p85beta regulatory subunits of phosphatidylinositol 3-kinase and the tyrosine phosphatase SHP2 (PTPN11).
19671924	8	53	theme	phosphatase	1423:1433	arg1	SHP2					1435:1438	the tyrosine phosphatase SHP2	1410:1438	the tyrosine phosphatase SHP2 (PTPN11)	1410:1447	O-GlcNAc modification at a conserved residue in rat (Ser(1009)) and human (Ser(1011)) IRS-1 is adjacent to a putative binding motif for the N-terminal SH2 domains of p85alpha and p85beta regulatory subunits of phosphatidylinositol 3-kinase and the tyrosine phosphatase SHP2 (PTPN11).
19671924	2	54	theme	forward	384:390	arg1	regulation					392:401	feedback and feed forward regulation	366:401	regulation	392:401	Ser/Thr kinases impact the metabolic and mitogenic effects elicited by insulin and IGF-1 through feedback and feed forward regulation at the level of IRS-1.
19671924	7	55	theme	multiple	1124:1131	arg1	sites					1133:1137	multiple sites	1124:1137	multiple sites within residues 1025-1045	1124:1163	Human IRS-1 was O-GlcNAc-modified at Ser(984) or Ser(985), at Ser(1011), and possibly at multiple sites within residues 1025-1045.
19671924	4	56	theme	effects	593:599	arg1	understanding					561:573	the understanding	557:573	the understanding of the functional effects of O-GlcNAc modification on IRS-1-mediated signaling	557:652	To facilitate the understanding of the functional effects of O-GlcNAc modification on IRS-1-mediated signaling, we identified the sites of O-GlcNAc modification of rat and human IRS-1.
19671924	10	57	theme	liver	1702:1706	arg1	cells					1708:1712	HEPG2 liver cells	1696:1712	HEPG2 liver cells	1696:1712	The accumulation of IRS-1 Ser(1011) GlcNAc in HEPG2 liver cells and MC3T3-E1 preosteoblasts upon inhibition of O-GlcNAcase indicates that O-GlcNAcylation of endogenously expressed IRS-1 is a dynamic process that occurs at normal glucose concentrations (5 mm).
19671924	11	58	theme	Ser/Thr	1979:1985	arg1	sites					2003:2007	any known or newly identified Ser/Thr phosphorylation sites	1949:2007	any known or newly identified Ser/Thr phosphorylation sites	1949:2007	O-GlcNAc modification did not occur at any known or newly identified Ser/Thr phosphorylation sites and in most cases occurred simultaneously with phosphorylation of nearby residues.
19671924	4	59	theme	O-GlcNAc	604:611	arg1	modification					613:624	O-GlcNAc modification	604:624	O-GlcNAc modification	604:624	To facilitate the understanding of the functional effects of O-GlcNAc modification on IRS-1-mediated signaling, we identified the sites of O-GlcNAc modification of rat and human IRS-1.
19671924	6	60	from	Ser	1024:1026	arg1	O-GlcNAc-modified					967:983	O-GlcNAc-modified	967:983	O-GlcNAc-modified	967:983	Rat IRS-1 was O-GlcNAc-modified at Ser(914), Ser(1009), Ser(1036), and Ser(1041).
19671924	5	61	theme	docking	859:865	arg1	sites					867:871	docking sites	859:871	docking sites for SH2 domain-containing proteins	859:906	Tandem mass spectrometric analysis of IRS-1, exogenously expressed in HEK293 cells, revealed that the C terminus, which is rich in docking sites for SH2 domain-containing proteins, was O-GlcNAc-modified at multiple residues.
19671924	9	62	theme	human	1506:1510	arg1	GlcNAc					1528:1533	human IRS-1 Ser(1011) GlcNAc	1506:1533	human IRS-1 Ser(1011) GlcNAc	1506:1533	Immunoblot analysis using an antibody generated against human IRS-1 Ser(1011) GlcNAc further confirmed the site of attachment and the identity of the +203.2-Da mass shift as beta-N-acetylglucosamine.
19671924	7	63	from	sites	1133:1137	arg1	O-GlcNAc-modified					1051:1067	O-GlcNAc-modified	1051:1067	O-GlcNAc-modified	1051:1067	Human IRS-1 was O-GlcNAc-modified at Ser(984) or Ser(985), at Ser(1011), and possibly at multiple sites within residues 1025-1045.
19671924	6	64	from	Ser	1009:1011	arg1	O-GlcNAc-modified					967:983	O-GlcNAc-modified	967:983	O-GlcNAc-modified	967:983	Rat IRS-1 was O-GlcNAc-modified at Ser(914), Ser(1009), Ser(1036), and Ser(1041).
19671924	9	65	theme	Ser	1518:1520	arg1	GlcNAc					1528:1533	human IRS-1 Ser(1011) GlcNAc	1506:1533	human IRS-1 Ser(1011) GlcNAc	1506:1533	Immunoblot analysis using an antibody generated against human IRS-1 Ser(1011) GlcNAc further confirmed the site of attachment and the identity of the +203.2-Da mass shift as beta-N-acetylglucosamine.
19671924	4	66	theme	modification	691:702	arg1	sites					673:677	the sites	669:677	the sites of O-GlcNAc modification of rat and human IRS-1	669:725	To facilitate the understanding of the functional effects of O-GlcNAc modification on IRS-1-mediated signaling, we identified the sites of O-GlcNAc modification of rat and human IRS-1.
19671924	4	66	theme	modification	691:702	arg1	modification					691:702	O-GlcNAc modification	682:702	O-GlcNAc modification of rat and human IRS-1	682:725	To facilitate the understanding of the functional effects of O-GlcNAc modification on IRS-1-mediated signaling, we identified the sites of O-GlcNAc modification of rat and human IRS-1.
19671924	1	67	theme	adaptor	203:209	arg1	protein					211:217	a highly phosphorylated adaptor protein	179:217	a highly phosphorylated adaptor protein critical to insulin and IGF-1 receptor signaling	179:266	Insulin receptor substrate-1 (IRS-1) is a highly phosphorylated adaptor protein critical to insulin and IGF-1 receptor signaling.
19671924	1	67	theme	adaptor	203:209	arg1	substrate-1					156:166	Insulin receptor substrate-1	139:166	Insulin receptor substrate-1 (IRS-1)	139:174	Insulin receptor substrate-1 (IRS-1) is a highly phosphorylated adaptor protein critical to insulin and IGF-1 receptor signaling.
19671924	9	68	theme	1011	1522:1525	arg1	GlcNAc					1528:1533	human IRS-1 Ser(1011) GlcNAc	1506:1533	human IRS-1 Ser(1011) GlcNAc	1506:1533	Immunoblot analysis using an antibody generated against human IRS-1 Ser(1011) GlcNAc further confirmed the site of attachment and the identity of the +203.2-Da mass shift as beta-N-acetylglucosamine.
19671924	12	69	theme	regulation	2194:2203	arg1	layer					2167:2171	an additional layer	2153:2171	an additional layer of posttranslational regulation that may impact the specificity of effects elicited by insulin and IGF-1	2153:2276	These findings suggest that O-GlcNAc modification represents an additional layer of posttranslational regulation that may impact the specificity of effects elicited by insulin and IGF-1.
19671924	4	70	mod	modification	691:702	arg1	rat					707:709	rat	707:709	rat	707:709	To facilitate the understanding of the functional effects of O-GlcNAc modification on IRS-1-mediated signaling, we identified the sites of O-GlcNAc modification of rat and human IRS-1.
19671924	4	70	mod	modification	691:702	arg1	IRS-1					721:725	human IRS-1	715:725	human IRS-1	715:725	To facilitate the understanding of the functional effects of O-GlcNAc modification on IRS-1-mediated signaling, we identified the sites of O-GlcNAc modification of rat and human IRS-1.
19671924	4	70	mod	modification	691:702	arg3	O-GlcNAc					682:689	O-GlcNAc modification	682:702	O-GlcNAc modification of rat and human IRS-1	682:725	To facilitate the understanding of the functional effects of O-GlcNAc modification on IRS-1-mediated signaling, we identified the sites of O-GlcNAc modification of rat and human IRS-1.
19671924	10	71	theme	O-GlcNAcase	1761:1771	arg1	inhibition					1747:1756	inhibition	1747:1756	inhibition of O-GlcNAcase	1747:1771	The accumulation of IRS-1 Ser(1011) GlcNAc in HEPG2 liver cells and MC3T3-E1 preosteoblasts upon inhibition of O-GlcNAcase indicates that O-GlcNAcylation of endogenously expressed IRS-1 is a dynamic process that occurs at normal glucose concentrations (5 mm).
19671924	5	72	theme	mass	735:738	arg1	analysis					754:761	Tandem mass spectrometric analysis	728:761	Tandem mass spectrometric analysis	728:761	Tandem mass spectrometric analysis of IRS-1, exogenously expressed in HEK293 cells, revealed that the C terminus, which is rich in docking sites for SH2 domain-containing proteins, was O-GlcNAc-modified at multiple residues.
19671924	5	73	theme	SH2	877:879	arg1	proteins					899:906	SH2 domain-containing proteins	877:906	SH2 domain-containing proteins	877:906	Tandem mass spectrometric analysis of IRS-1, exogenously expressed in HEK293 cells, revealed that the C terminus, which is rich in docking sites for SH2 domain-containing proteins, was O-GlcNAc-modified at multiple residues.
19671924	1	74	theme	critical	219:226	arg1	protein					211:217	a highly phosphorylated adaptor protein	179:217	a highly phosphorylated adaptor protein critical to insulin and IGF-1 receptor signaling	179:266	Insulin receptor substrate-1 (IRS-1) is a highly phosphorylated adaptor protein critical to insulin and IGF-1 receptor signaling.
19671924	1	74	theme	critical	219:226	arg1	substrate-1					156:166	Insulin receptor substrate-1	139:166	Insulin receptor substrate-1 (IRS-1)	139:174	Insulin receptor substrate-1 (IRS-1) is a highly phosphorylated adaptor protein critical to insulin and IGF-1 receptor signaling.
19671924	10	75	from	preosteoblasts	1727:1740	arg1	accumulation					1654:1665	The accumulation	1650:1665	The accumulation of IRS-1 Ser(1011) GlcNAc in HEPG2 liver cells and MC3T3-E1 preosteoblasts upon inhibition of O-GlcNAcase	1650:1771	The accumulation of IRS-1 Ser(1011) GlcNAc in HEPG2 liver cells and MC3T3-E1 preosteoblasts upon inhibition of O-GlcNAcase indicates that O-GlcNAcylation of endogenously expressed IRS-1 is a dynamic process that occurs at normal glucose concentrations (5 mm).
19671924	1	76	dep	insulin	231:237	arg1	signaling					258:266	receptor signaling	249:266	receptor signaling	249:266	Insulin receptor substrate-1 (IRS-1) is a highly phosphorylated adaptor protein critical to insulin and IGF-1 receptor signaling.
19671924	10	77	theme	expressed	1820:1828	arg1	IRS-1					1830:1834	endogenously expressed IRS-1	1807:1834	endogenously expressed IRS-1	1807:1834	The accumulation of IRS-1 Ser(1011) GlcNAc in HEPG2 liver cells and MC3T3-E1 preosteoblasts upon inhibition of O-GlcNAcase indicates that O-GlcNAcylation of endogenously expressed IRS-1 is a dynamic process that occurs at normal glucose concentrations (5 mm).
19671924	8	78	dep	IRS-1	1252:1256	arg1	Ser					1241:1243	Ser	1241:1243	Ser(1011)	1241:1249	O-GlcNAc modification at a conserved residue in rat (Ser(1009)) and human (Ser(1011)) IRS-1 is adjacent to a putative binding motif for the N-terminal SH2 domains of p85alpha and p85beta regulatory subunits of phosphatidylinositol 3-kinase and the tyrosine phosphatase SHP2 (PTPN11).
19671924	8	78	dep	IRS-1	1252:1256	arg1	1011					1245:1248	1011	1245:1248	1011	1245:1248	O-GlcNAc modification at a conserved residue in rat (Ser(1009)) and human (Ser(1011)) IRS-1 is adjacent to a putative binding motif for the N-terminal SH2 domains of p85alpha and p85beta regulatory subunits of phosphatidylinositol 3-kinase and the tyrosine phosphatase SHP2 (PTPN11).
19671924	6	79	theme	Rat	953:955	arg1	IRS-1					957:961	Rat IRS-1	953:961	Rat IRS-1	953:961	Rat IRS-1 was O-GlcNAc-modified at Ser(914), Ser(1009), Ser(1036), and Ser(1041).
19671924	11	80	theme	O-GlcNAc	1910:1917	arg1	modification					1919:1930	O-GlcNAc modification	1910:1930	O-GlcNAc modification	1910:1930	O-GlcNAc modification did not occur at any known or newly identified Ser/Thr phosphorylation sites and in most cases occurred simultaneously with phosphorylation of nearby residues.
19671924	8	81	theme	binding	1284:1290	arg1	motif					1292:1296	a putative binding motif	1273:1296	a putative binding motif for the N-terminal SH2 domains of p85alpha and p85beta regulatory subunits of phosphatidylinositol 3-kinase and the tyrosine phosphatase SHP2 (PTPN11)	1273:1447	O-GlcNAc modification at a conserved residue in rat (Ser(1009)) and human (Ser(1011)) IRS-1 is adjacent to a putative binding motif for the N-terminal SH2 domains of p85alpha and p85beta regulatory subunits of phosphatidylinositol 3-kinase and the tyrosine phosphatase SHP2 (PTPN11).
19671924	1	82	theme	Insulin	139:145	arg1	protein					211:217	a highly phosphorylated adaptor protein	179:217	a highly phosphorylated adaptor protein critical to insulin and IGF-1 receptor signaling	179:266	Insulin receptor substrate-1 (IRS-1) is a highly phosphorylated adaptor protein critical to insulin and IGF-1 receptor signaling.
19671924	1	82	theme	Insulin	139:145	arg1	IRS-1					169:173	IRS-1	169:173	IRS-1	169:173	Insulin receptor substrate-1 (IRS-1) is a highly phosphorylated adaptor protein critical to insulin and IGF-1 receptor signaling.
19671924	1	82	theme	Insulin	139:145	arg1	substrate-1					156:166	Insulin receptor substrate-1	139:166	Insulin receptor substrate-1 (IRS-1)	139:174	Insulin receptor substrate-1 (IRS-1) is a highly phosphorylated adaptor protein critical to insulin and IGF-1 receptor signaling.
19671924	10	83	theme	dynamic	1841:1847	arg1	process					1849:1855	a dynamic process	1839:1855	a dynamic process that occurs at normal glucose concentrations (5 mm)	1839:1907	The accumulation of IRS-1 Ser(1011) GlcNAc in HEPG2 liver cells and MC3T3-E1 preosteoblasts upon inhibition of O-GlcNAcase indicates that O-GlcNAcylation of endogenously expressed IRS-1 is a dynamic process that occurs at normal glucose concentrations (5 mm).
19671924	10	83	theme	dynamic	1841:1847	arg1	O-GlcNAcylation					1788:1802	O-GlcNAcylation	1788:1802	O-GlcNAcylation of endogenously expressed IRS-1	1788:1834	The accumulation of IRS-1 Ser(1011) GlcNAc in HEPG2 liver cells and MC3T3-E1 preosteoblasts upon inhibition of O-GlcNAcase indicates that O-GlcNAcylation of endogenously expressed IRS-1 is a dynamic process that occurs at normal glucose concentrations (5 mm).
19671924	0	84	theme	close	84:88	arg1	proximity					90:98	close proximity	84:98	close proximity to multiple SH2 domain binding motifs	84:136	O-linked N-acetylglucosamine modification of insulin receptor substrate-1 occurs in close proximity to multiple SH2 domain binding motifs.
19671924	5	85	theme	domain-containing	881:897	arg1	proteins					899:906	SH2 domain-containing proteins	877:906	SH2 domain-containing proteins	877:906	Tandem mass spectrometric analysis of IRS-1, exogenously expressed in HEK293 cells, revealed that the C terminus, which is rich in docking sites for SH2 domain-containing proteins, was O-GlcNAc-modified at multiple residues.
19671924	9	86	theme	attachment	1565:1574	arg1	shift					1615:1619	the +203.2-Da mass shift	1596:1619	the +203.2-Da mass shift	1596:1619	Immunoblot analysis using an antibody generated against human IRS-1 Ser(1011) GlcNAc further confirmed the site of attachment and the identity of the +203.2-Da mass shift as beta-N-acetylglucosamine.
19671924	9	86	theme	attachment	1565:1574	arg1	attachment					1565:1574	attachment	1565:1574	attachment	1565:1574	Immunoblot analysis using an antibody generated against human IRS-1 Ser(1011) GlcNAc further confirmed the site of attachment and the identity of the +203.2-Da mass shift as beta-N-acetylglucosamine.
19671924	9	86	theme	attachment	1565:1574	arg1	identity					1584:1591	the identity	1580:1591	the identity of the +203.2-Da mass shift	1580:1619	Immunoblot analysis using an antibody generated against human IRS-1 Ser(1011) GlcNAc further confirmed the site of attachment and the identity of the +203.2-Da mass shift as beta-N-acetylglucosamine.
19671924	9	86	theme	attachment	1565:1574	arg1	site					1557:1560	the site	1553:1560	the site of attachment	1553:1574	Immunoblot analysis using an antibody generated against human IRS-1 Ser(1011) GlcNAc further confirmed the site of attachment and the identity of the +203.2-Da mass shift as beta-N-acetylglucosamine.
19671924	8	87	theme	N-terminal	1306:1315	arg1	p85alpha					1332:1339	p85alpha	1332:1339	p85alpha	1332:1339	O-GlcNAc modification at a conserved residue in rat (Ser(1009)) and human (Ser(1011)) IRS-1 is adjacent to a putative binding motif for the N-terminal SH2 domains of p85alpha and p85beta regulatory subunits of phosphatidylinositol 3-kinase and the tyrosine phosphatase SHP2 (PTPN11).
19671924	8	87	theme	N-terminal	1306:1315	arg1	domains					1321:1327	the N-terminal SH2 domains	1302:1327	the N-terminal SH2 domains of p85alpha and p85beta regulatory subunits of phosphatidylinositol 3-kinase and the tyrosine phosphatase SHP2 (PTPN11)	1302:1447	O-GlcNAc modification at a conserved residue in rat (Ser(1009)) and human (Ser(1011)) IRS-1 is adjacent to a putative binding motif for the N-terminal SH2 domains of p85alpha and p85beta regulatory subunits of phosphatidylinositol 3-kinase and the tyrosine phosphatase SHP2 (PTPN11).
19671924	8	87	theme	N-terminal	1306:1315	arg1	subunits					1364:1371	p85beta regulatory subunits	1345:1371	p85beta regulatory subunits	1345:1371	O-GlcNAc modification at a conserved residue in rat (Ser(1009)) and human (Ser(1011)) IRS-1 is adjacent to a putative binding motif for the N-terminal SH2 domains of p85alpha and p85beta regulatory subunits of phosphatidylinositol 3-kinase and the tyrosine phosphatase SHP2 (PTPN11).
19671924	4	88	theme	rat	707:709	arg1	modification					691:702	O-GlcNAc modification	682:702	O-GlcNAc modification of rat and human IRS-1	682:725	To facilitate the understanding of the functional effects of O-GlcNAc modification on IRS-1-mediated signaling, we identified the sites of O-GlcNAc modification of rat and human IRS-1.
19671924	5	89	from	sites	867:871	arg1	rich					851:854	rich	851:854	rich	851:854	Tandem mass spectrometric analysis of IRS-1, exogenously expressed in HEK293 cells, revealed that the C terminus, which is rich in docking sites for SH2 domain-containing proteins, was O-GlcNAc-modified at multiple residues.
19671924	5	89	from	sites	867:871	arg1	terminus					832:839	the C terminus	826:839	the C terminus	826:839	Tandem mass spectrometric analysis of IRS-1, exogenously expressed in HEK293 cells, revealed that the C terminus, which is rich in docking sites for SH2 domain-containing proteins, was O-GlcNAc-modified at multiple residues.
19671924	5	89	from	sites	867:871	arg1	O-GlcNAc-modified					913:929	O-GlcNAc-modified	913:929	O-GlcNAc-modified	913:929	Tandem mass spectrometric analysis of IRS-1, exogenously expressed in HEK293 cells, revealed that the C terminus, which is rich in docking sites for SH2 domain-containing proteins, was O-GlcNAc-modified at multiple residues.
19671924	4	90	theme	human	715:719	arg1	IRS-1					721:725	human IRS-1	715:725	human IRS-1	715:725	To facilitate the understanding of the functional effects of O-GlcNAc modification on IRS-1-mediated signaling, we identified the sites of O-GlcNAc modification of rat and human IRS-1.
19671924	0	91	theme	SH2	112:114	arg1	motifs					131:136	multiple SH2 domain binding motifs	103:136	multiple SH2 domain binding motifs	103:136	O-linked N-acetylglucosamine modification of insulin receptor substrate-1 occurs in close proximity to multiple SH2 domain binding motifs.
19671924	11	92	theme	residues	2082:2089	arg1	phosphorylation					2056:2070	phosphorylation	2056:2070	phosphorylation of nearby residues	2056:2089	O-GlcNAc modification did not occur at any known or newly identified Ser/Thr phosphorylation sites and in most cases occurred simultaneously with phosphorylation of nearby residues.
19671924	8	93	theme	p85alpha	1332:1339	arg1	p85alpha					1332:1339	p85alpha	1332:1339	p85alpha	1332:1339	O-GlcNAc modification at a conserved residue in rat (Ser(1009)) and human (Ser(1011)) IRS-1 is adjacent to a putative binding motif for the N-terminal SH2 domains of p85alpha and p85beta regulatory subunits of phosphatidylinositol 3-kinase and the tyrosine phosphatase SHP2 (PTPN11).
19671924	8	93	theme	p85alpha	1332:1339	arg1	domains					1321:1327	the N-terminal SH2 domains	1302:1327	the N-terminal SH2 domains of p85alpha and p85beta regulatory subunits of phosphatidylinositol 3-kinase and the tyrosine phosphatase SHP2 (PTPN11)	1302:1447	O-GlcNAc modification at a conserved residue in rat (Ser(1009)) and human (Ser(1011)) IRS-1 is adjacent to a putative binding motif for the N-terminal SH2 domains of p85alpha and p85beta regulatory subunits of phosphatidylinositol 3-kinase and the tyrosine phosphatase SHP2 (PTPN11).
19671924	8	93	theme	p85alpha	1332:1339	arg1	subunits					1364:1371	p85beta regulatory subunits	1345:1371	p85beta regulatory subunits	1345:1371	O-GlcNAc modification at a conserved residue in rat (Ser(1009)) and human (Ser(1011)) IRS-1 is adjacent to a putative binding motif for the N-terminal SH2 domains of p85alpha and p85beta regulatory subunits of phosphatidylinositol 3-kinase and the tyrosine phosphatase SHP2 (PTPN11).
19671924	0	94	theme	binding	123:129	arg1	motifs					131:136	multiple SH2 domain binding motifs	103:136	multiple SH2 domain binding motifs	103:136	O-linked N-acetylglucosamine modification of insulin receptor substrate-1 occurs in close proximity to multiple SH2 domain binding motifs.
19671924	9	95	theme	+203.2-Da	1600:1608	arg1	shift					1615:1619	the +203.2-Da mass shift	1596:1619	the +203.2-Da mass shift	1596:1619	Immunoblot analysis using an antibody generated against human IRS-1 Ser(1011) GlcNAc further confirmed the site of attachment and the identity of the +203.2-Da mass shift as beta-N-acetylglucosamine.
19671924	8	96	theme	p85beta	1345:1351	arg1	subunits					1364:1371	p85beta regulatory subunits	1345:1371	p85beta regulatory subunits	1345:1371	O-GlcNAc modification at a conserved residue in rat (Ser(1009)) and human (Ser(1011)) IRS-1 is adjacent to a putative binding motif for the N-terminal SH2 domains of p85alpha and p85beta regulatory subunits of phosphatidylinositol 3-kinase and the tyrosine phosphatase SHP2 (PTPN11).
19671924	12	97	theme	effects	2240:2246	arg1	specificity					2225:2235	the specificity	2221:2235	the specificity of effects elicited by insulin and IGF-1	2221:2276	These findings suggest that O-GlcNAc modification represents an additional layer of posttranslational regulation that may impact the specificity of effects elicited by insulin and IGF-1.
19671924	5	98	theme	IRS-1	766:770	arg1	analysis					754:761	Tandem mass spectrometric analysis	728:761	Tandem mass spectrometric analysis	728:761	Tandem mass spectrometric analysis of IRS-1, exogenously expressed in HEK293 cells, revealed that the C terminus, which is rich in docking sites for SH2 domain-containing proteins, was O-GlcNAc-modified at multiple residues.
19671924	0	99	theme	N-acetylglucosamine	9:27	arg1	modification					29:40	O-linked N-acetylglucosamine modification	0:40	O-linked N-acetylglucosamine modification of insulin receptor substrate-1	0:72	O-linked N-acetylglucosamine modification of insulin receptor substrate-1 occurs in close proximity to multiple SH2 domain binding motifs.
19671924	8	100	from	residue	1203:1209	arg1	modification					1175:1186	O-GlcNAc modification	1166:1186	O-GlcNAc modification at a conserved residue in rat (Ser(1009)) and human (Ser(1011)) IRS-1	1166:1256	O-GlcNAc modification at a conserved residue in rat (Ser(1009)) and human (Ser(1011)) IRS-1 is adjacent to a putative binding motif for the N-terminal SH2 domains of p85alpha and p85beta regulatory subunits of phosphatidylinositol 3-kinase and the tyrosine phosphatase SHP2 (PTPN11).
19671924	8	100	from	residue	1203:1209	arg1	rat					1214:1216	rat	1214:1216	rat	1214:1216	O-GlcNAc modification at a conserved residue in rat (Ser(1009)) and human (Ser(1011)) IRS-1 is adjacent to a putative binding motif for the N-terminal SH2 domains of p85alpha and p85beta regulatory subunits of phosphatidylinositol 3-kinase and the tyrosine phosphatase SHP2 (PTPN11).
19671924	9	101	theme	shift	1615:1619	arg1	shift					1615:1619	the +203.2-Da mass shift	1596:1619	the +203.2-Da mass shift	1596:1619	Immunoblot analysis using an antibody generated against human IRS-1 Ser(1011) GlcNAc further confirmed the site of attachment and the identity of the +203.2-Da mass shift as beta-N-acetylglucosamine.
19671924	9	101	theme	shift	1615:1619	arg1	attachment					1565:1574	attachment	1565:1574	attachment	1565:1574	Immunoblot analysis using an antibody generated against human IRS-1 Ser(1011) GlcNAc further confirmed the site of attachment and the identity of the +203.2-Da mass shift as beta-N-acetylglucosamine.
19671924	9	101	theme	shift	1615:1619	arg1	identity					1584:1591	the identity	1580:1591	the identity of the +203.2-Da mass shift	1580:1619	Immunoblot analysis using an antibody generated against human IRS-1 Ser(1011) GlcNAc further confirmed the site of attachment and the identity of the +203.2-Da mass shift as beta-N-acetylglucosamine.
19671924	9	101	theme	shift	1615:1619	arg1	site					1557:1560	the site	1553:1560	the site of attachment	1553:1574	Immunoblot analysis using an antibody generated against human IRS-1 Ser(1011) GlcNAc further confirmed the site of attachment and the identity of the +203.2-Da mass shift as beta-N-acetylglucosamine.
19671924	8	102	theme	subunits	1364:1371	arg1	p85alpha					1332:1339	p85alpha	1332:1339	p85alpha	1332:1339	O-GlcNAc modification at a conserved residue in rat (Ser(1009)) and human (Ser(1011)) IRS-1 is adjacent to a putative binding motif for the N-terminal SH2 domains of p85alpha and p85beta regulatory subunits of phosphatidylinositol 3-kinase and the tyrosine phosphatase SHP2 (PTPN11).
19671924	8	102	theme	subunits	1364:1371	arg1	domains					1321:1327	the N-terminal SH2 domains	1302:1327	the N-terminal SH2 domains of p85alpha and p85beta regulatory subunits of phosphatidylinositol 3-kinase and the tyrosine phosphatase SHP2 (PTPN11)	1302:1447	O-GlcNAc modification at a conserved residue in rat (Ser(1009)) and human (Ser(1011)) IRS-1 is adjacent to a putative binding motif for the N-terminal SH2 domains of p85alpha and p85beta regulatory subunits of phosphatidylinositol 3-kinase and the tyrosine phosphatase SHP2 (PTPN11).
19671924	8	102	theme	subunits	1364:1371	arg1	subunits					1364:1371	p85beta regulatory subunits	1345:1371	p85beta regulatory subunits	1345:1371	O-GlcNAc modification at a conserved residue in rat (Ser(1009)) and human (Ser(1011)) IRS-1 is adjacent to a putative binding motif for the N-terminal SH2 domains of p85alpha and p85beta regulatory subunits of phosphatidylinositol 3-kinase and the tyrosine phosphatase SHP2 (PTPN11).
19671924	11	103	theme	identified	1968:1977	arg1	sites					2003:2007	any known or newly identified Ser/Thr phosphorylation sites	1949:2007	any known or newly identified Ser/Thr phosphorylation sites	1949:2007	O-GlcNAc modification did not occur at any known or newly identified Ser/Thr phosphorylation sites and in most cases occurred simultaneously with phosphorylation of nearby residues.
19671924	8	104	theme	phosphatidylinositol	1376:1395	arg1	3-kinase					1397:1404	phosphatidylinositol 3-kinase	1376:1404	phosphatidylinositol 3-kinase	1376:1404	O-GlcNAc modification at a conserved residue in rat (Ser(1009)) and human (Ser(1011)) IRS-1 is adjacent to a putative binding motif for the N-terminal SH2 domains of p85alpha and p85beta regulatory subunits of phosphatidylinositol 3-kinase and the tyrosine phosphatase SHP2 (PTPN11).
19671924	4	105	theme	IRS-1-mediated	629:642	arg1	signaling					644:652	IRS-1-mediated signaling	629:652	IRS-1-mediated signaling	629:652	To facilitate the understanding of the functional effects of O-GlcNAc modification on IRS-1-mediated signaling, we identified the sites of O-GlcNAc modification of rat and human IRS-1.
19671924	10	106	theme	1011	1680:1683	arg1	GlcNAc					1686:1691	IRS-1 Ser(1011) GlcNAc	1670:1691	IRS-1 Ser(1011) GlcNAc in HEPG2 liver cells and MC3T3-E1 preosteoblasts	1670:1740	The accumulation of IRS-1 Ser(1011) GlcNAc in HEPG2 liver cells and MC3T3-E1 preosteoblasts upon inhibition of O-GlcNAcase indicates that O-GlcNAcylation of endogenously expressed IRS-1 is a dynamic process that occurs at normal glucose concentrations (5 mm).
19671924	0	107	theme	receptor	53:60	arg1	substrate-1					62:72	insulin receptor substrate-1	45:72	insulin receptor substrate-1	45:72	O-linked N-acetylglucosamine modification of insulin receptor substrate-1 occurs in close proximity to multiple SH2 domain binding motifs.
19671924	10	108	from	accumulation	1654:1665	arg1	cells					1708:1712	HEPG2 liver cells	1696:1712	HEPG2 liver cells	1696:1712	The accumulation of IRS-1 Ser(1011) GlcNAc in HEPG2 liver cells and MC3T3-E1 preosteoblasts upon inhibition of O-GlcNAcase indicates that O-GlcNAcylation of endogenously expressed IRS-1 is a dynamic process that occurs at normal glucose concentrations (5 mm).
19671924	10	108	from	accumulation	1654:1665	arg1	preosteoblasts					1727:1740	MC3T3-E1 preosteoblasts	1718:1740	MC3T3-E1 preosteoblasts	1718:1740	The accumulation of IRS-1 Ser(1011) GlcNAc in HEPG2 liver cells and MC3T3-E1 preosteoblasts upon inhibition of O-GlcNAcase indicates that O-GlcNAcylation of endogenously expressed IRS-1 is a dynamic process that occurs at normal glucose concentrations (5 mm).
19671924	3	109	theme	Ser/Thr	426:432	arg1	IRS-1					446:450	IRS-1	446:450	IRS-1	446:450	Ser/Thr residues of IRS-1 are also O-GlcNAc-modified, which may influence the phosphorylation status of the protein.
19671924	3	109	theme	Ser/Thr	426:432	arg1	residues					434:441	Ser/Thr residues	426:441	Ser/Thr residues of IRS-1	426:450	Ser/Thr residues of IRS-1 are also O-GlcNAc-modified, which may influence the phosphorylation status of the protein.
19671924	0	110	mod	modification	29:40	arg3	N-acetylglucosamine					9:27	O-linked N-acetylglucosamine modification	0:40	O-linked N-acetylglucosamine modification of insulin receptor substrate-1	0:72	O-linked N-acetylglucosamine modification of insulin receptor substrate-1 occurs in close proximity to multiple SH2 domain binding motifs.
19671924	0	110	mod	modification	29:40	arg1	substrate-1					62:72	insulin receptor substrate-1	45:72	insulin receptor substrate-1	45:72	O-linked N-acetylglucosamine modification of insulin receptor substrate-1 occurs in close proximity to multiple SH2 domain binding motifs.
19671924	6	111	from	Ser	988:990	arg1	O-GlcNAc-modified					967:983	O-GlcNAc-modified	967:983	O-GlcNAc-modified	967:983	Rat IRS-1 was O-GlcNAc-modified at Ser(914), Ser(1009), Ser(1036), and Ser(1041).
19671924	10	112	theme	Ser	1676:1678	arg1	GlcNAc					1686:1691	IRS-1 Ser(1011) GlcNAc	1670:1691	IRS-1 Ser(1011) GlcNAc in HEPG2 liver cells and MC3T3-E1 preosteoblasts	1670:1740	The accumulation of IRS-1 Ser(1011) GlcNAc in HEPG2 liver cells and MC3T3-E1 preosteoblasts upon inhibition of O-GlcNAcase indicates that O-GlcNAcylation of endogenously expressed IRS-1 is a dynamic process that occurs at normal glucose concentrations (5 mm).
19671924	8	113	theme	human	1234:1238	arg1	IRS-1					1252:1256	human (Ser(1011)) IRS-1	1234:1256	human (Ser(1011)) IRS-1	1234:1256	O-GlcNAc modification at a conserved residue in rat (Ser(1009)) and human (Ser(1011)) IRS-1 is adjacent to a putative binding motif for the N-terminal SH2 domains of p85alpha and p85beta regulatory subunits of phosphatidylinositol 3-kinase and the tyrosine phosphatase SHP2 (PTPN11).
19671924	4	114	from	effects	593:599	arg1	signaling					644:652	IRS-1-mediated signaling	629:652	IRS-1-mediated signaling	629:652	To facilitate the understanding of the functional effects of O-GlcNAc modification on IRS-1-mediated signaling, we identified the sites of O-GlcNAc modification of rat and human IRS-1.
19671924	8	115	theme	tyrosine	1414:1421	arg1	PTPN11					1441:1446	PTPN11	1441:1446	PTPN11	1441:1446	O-GlcNAc modification at a conserved residue in rat (Ser(1009)) and human (Ser(1011)) IRS-1 is adjacent to a putative binding motif for the N-terminal SH2 domains of p85alpha and p85beta regulatory subunits of phosphatidylinositol 3-kinase and the tyrosine phosphatase SHP2 (PTPN11).
19671924	8	115	theme	tyrosine	1414:1421	arg1	SHP2					1435:1438	the tyrosine phosphatase SHP2	1410:1438	the tyrosine phosphatase SHP2 (PTPN11)	1410:1447	O-GlcNAc modification at a conserved residue in rat (Ser(1009)) and human (Ser(1011)) IRS-1 is adjacent to a putative binding motif for the N-terminal SH2 domains of p85alpha and p85beta regulatory subunits of phosphatidylinositol 3-kinase and the tyrosine phosphatase SHP2 (PTPN11).
19671924	10	116	theme	HEPG2	1696:1700	arg1	cells					1708:1712	HEPG2 liver cells	1696:1712	HEPG2 liver cells	1696:1712	The accumulation of IRS-1 Ser(1011) GlcNAc in HEPG2 liver cells and MC3T3-E1 preosteoblasts upon inhibition of O-GlcNAcase indicates that O-GlcNAcylation of endogenously expressed IRS-1 is a dynamic process that occurs at normal glucose concentrations (5 mm).
19671924	3	117	theme	phosphorylation	504:518	arg1	status					520:525	the phosphorylation status	500:525	the phosphorylation status of the protein	500:540	Ser/Thr residues of IRS-1 are also O-GlcNAc-modified, which may influence the phosphorylation status of the protein.
19671924	8	118	theme	SHP2	1435:1438	arg1	p85alpha					1332:1339	p85alpha	1332:1339	p85alpha	1332:1339	O-GlcNAc modification at a conserved residue in rat (Ser(1009)) and human (Ser(1011)) IRS-1 is adjacent to a putative binding motif for the N-terminal SH2 domains of p85alpha and p85beta regulatory subunits of phosphatidylinositol 3-kinase and the tyrosine phosphatase SHP2 (PTPN11).
19671924	8	118	theme	SHP2	1435:1438	arg1	subunits					1364:1371	p85beta regulatory subunits	1345:1371	p85beta regulatory subunits	1345:1371	O-GlcNAc modification at a conserved residue in rat (Ser(1009)) and human (Ser(1011)) IRS-1 is adjacent to a putative binding motif for the N-terminal SH2 domains of p85alpha and p85beta regulatory subunits of phosphatidylinositol 3-kinase and the tyrosine phosphatase SHP2 (PTPN11).
19671924	10	119	theme	GlcNAc	1686:1691	arg1	accumulation					1654:1665	The accumulation	1650:1665	The accumulation of IRS-1 Ser(1011) GlcNAc in HEPG2 liver cells and MC3T3-E1 preosteoblasts upon inhibition of O-GlcNAcase	1650:1771	The accumulation of IRS-1 Ser(1011) GlcNAc in HEPG2 liver cells and MC3T3-E1 preosteoblasts upon inhibition of O-GlcNAcase indicates that O-GlcNAcylation of endogenously expressed IRS-1 is a dynamic process that occurs at normal glucose concentrations (5 mm).
19671924	2	120	theme	feed	379:382	arg1	regulation					392:401	feedback and feed forward regulation	366:401	regulation	392:401	Ser/Thr kinases impact the metabolic and mitogenic effects elicited by insulin and IGF-1 through feedback and feed forward regulation at the level of IRS-1.
19671924	9	121	theme	Immunoblot	1450:1459	arg1	analysis					1461:1468	Immunoblot analysis	1450:1468	Immunoblot analysis using an antibody generated against human IRS-1 Ser(1011) GlcNAc	1450:1533	Immunoblot analysis using an antibody generated against human IRS-1 Ser(1011) GlcNAc further confirmed the site of attachment and the identity of the +203.2-Da mass shift as beta-N-acetylglucosamine.
19671924	10	122	theme	glucose	1879:1885	arg1	concentrations					1887:1900	normal glucose concentrations	1872:1900	normal glucose concentrations (5 mm)	1872:1907	The accumulation of IRS-1 Ser(1011) GlcNAc in HEPG2 liver cells and MC3T3-E1 preosteoblasts upon inhibition of O-GlcNAcase indicates that O-GlcNAcylation of endogenously expressed IRS-1 is a dynamic process that occurs at normal glucose concentrations (5 mm).
19671924	10	122	theme	glucose	1879:1885	arg1	mm					1905:1906	5 mm	1903:1906	5 mm	1903:1906	The accumulation of IRS-1 Ser(1011) GlcNAc in HEPG2 liver cells and MC3T3-E1 preosteoblasts upon inhibition of O-GlcNAcase indicates that O-GlcNAcylation of endogenously expressed IRS-1 is a dynamic process that occurs at normal glucose concentrations (5 mm).
19671924	10	123	theme	MC3T3-E1	1718:1725	arg1	preosteoblasts					1727:1740	MC3T3-E1 preosteoblasts	1718:1740	MC3T3-E1 preosteoblasts	1718:1740	The accumulation of IRS-1 Ser(1011) GlcNAc in HEPG2 liver cells and MC3T3-E1 preosteoblasts upon inhibition of O-GlcNAcase indicates that O-GlcNAcylation of endogenously expressed IRS-1 is a dynamic process that occurs at normal glucose concentrations (5 mm).
19671924	3	124	theme	protein	534:540	arg1	status					520:525	the phosphorylation status	500:525	the phosphorylation status of the protein	500:540	Ser/Thr residues of IRS-1 are also O-GlcNAc-modified, which may influence the phosphorylation status of the protein.
19671924	1	125	theme	receptor	249:256	arg1	signaling					258:266	receptor signaling	249:266	receptor signaling	249:266	Insulin receptor substrate-1 (IRS-1) is a highly phosphorylated adaptor protein critical to insulin and IGF-1 receptor signaling.
32798372	2	0	theme	defective	298:306	arg1	responses					308:316	defective responses	298:316	defective responses to insulin	298:327	T2DM results from defective responses to insulin and obesity is a major factor behind insulin resistance in T2DM.
32798372	9	1	theme	possible	1555:1562	arg1	involvement					1564:1574	their possible involvement	1549:1574	their possible involvement in Advanced Glycation End products (AGEs)	1549:1616	DISCUSSION In this work OGlcNAc-modified proteins were specifically detected using O-Glc- NAc-specific antibodies, suggesting that elevated levels of O-GlcNAc-modified proteins are found, independently of their possible involvement in Advanced Glycation End products (AGEs).
32798372	3	2	theme	adaptor	440:446	arg1	proteins					427:434	Insulin receptor substrate (IRS) proteins	394:434	Insulin receptor substrate (IRS) proteins	394:434	Insulin receptor substrate (IRS) proteins are adaptor proteins in the insulin receptor signalling pathway.
32798372	3	2	theme	adaptor	440:446	arg1	proteins					448:455	adaptor proteins	440:455	adaptor proteins	440:455	Insulin receptor substrate (IRS) proteins are adaptor proteins in the insulin receptor signalling pathway.
32798372	6	3	theme	bioinformatics	1047:1060	arg1	tools					1062:1066	bioinformatics tools	1047:1066	bioinformatics tools	1047:1066	METHODS Phosphorylation and O-GlcNAc modifications (Ser1101 in IRS-1 and Ser1149 in IRS-2) proteins were determined experimentally by sandwich ELISA with specific antibodies and with bioinformatics tools.
32798372	3	4	theme	receptor	472:479	arg1	pathway					492:498	the insulin receptor signalling pathway	460:498	the insulin receptor signalling pathway	460:498	Insulin receptor substrate (IRS) proteins are adaptor proteins in the insulin receptor signalling pathway.
32798372	6	5	dep	METHODS	864:870	arg1	proteins					955:962	Phosphorylation and O-GlcNAc modifications (Ser1101 in IRS-1 and Ser1149 in IRS-2) proteins	872:962	METHODS Phosphorylation and O-GlcNAc modifications (Ser1101 in IRS-1 and Ser1149 in IRS-2) proteins	864:962	METHODS Phosphorylation and O-GlcNAc modifications (Ser1101 in IRS-1 and Ser1149 in IRS-2) proteins were determined experimentally by sandwich ELISA with specific antibodies and with bioinformatics tools.
32798372	7	6	from	IRS-2	1105:1109	arg1	Ser1101					1092:1098	Ser1101	1092:1098	Ser1101	1092:1098	RESULTS When IRS-1 (on Ser1101) and IRS-2 (Ser1149) become glycosylated following an increase in UDP-GlcNAc pools, it may contribute to insulin resistance.
32798372	1	7	from	epidemic	252:259	arg1	countries					269:277	some countries	264:277	some countries	264:277	BACKGROUND The prevalence of the chronic metabolic disorder Type 2 diabetes mellitus (T2DM) is increasing steadily, and has even turned into an epidemic in some countries.
32798372	3	8	from	proteins	448:455	arg1	pathway					492:498	the insulin receptor signalling pathway	460:498	the insulin receptor signalling pathway	460:498	Insulin receptor substrate (IRS) proteins are adaptor proteins in the insulin receptor signalling pathway.
32798372	3	9	theme	signalling	481:490	arg1	pathway					492:498	the insulin receptor signalling pathway	460:498	the insulin receptor signalling pathway	460:498	Insulin receptor substrate (IRS) proteins are adaptor proteins in the insulin receptor signalling pathway.
32798372	8	10	dep	inhibited	1333:1341	arg1	Whereas					1225:1231	Whereas	1225:1231	Whereas	1225:1231	Whereas when the same (IRS-1 on Ser1101 and IRS-2 on Ser1149) are phosphorylated, the insulin signalling is inhibited.
32798372	0	11	theme	Human	84:88	arg1	Type					99:102	Human Diabetes Type II	84:105	Human Diabetes Type II	84:105	Phosphorylated and O-GlcNAc Modified IRS-1 (Ser1101) and -2 (Ser1149) Contribute to Human Diabetes Type II.
32798372	6	12	theme	sandwich	998:1005	arg1	ELISA					1007:1011	sandwich ELISA	998:1011	sandwich ELISA with specific antibodies and with bioinformatics tools	998:1066	METHODS Phosphorylation and O-GlcNAc modifications (Ser1101 in IRS-1 and Ser1149 in IRS-2) proteins were determined experimentally by sandwich ELISA with specific antibodies and with bioinformatics tools.
32798372	9	13	theme	proteins	1512:1519	arg1	levels					1484:1489	elevated levels	1475:1489	elevated levels of O-GlcNAc-modified proteins	1475:1519	DISCUSSION In this work OGlcNAc-modified proteins were specifically detected using O-Glc- NAc-specific antibodies, suggesting that elevated levels of O-GlcNAc-modified proteins are found, independently of their possible involvement in Advanced Glycation End products (AGEs).
32798372	4	14	theme	proteins	616:623	arg1	dysregulation					595:607	dysregulation	595:607	dysregulation of IRS proteins signalling	595:634	The insulin signalling is controlled through tyrosine phosphorylation of IRS-1 and IRS-2, and dysregulation of IRS proteins signalling may lead to glucose intolerance and eventually insulin resistance.
32798372	5	15	theme	IRS-1	809:813	arg1	phosphorylation					790:804	phosphorylation	790:804	phosphorylation of IRS-1 and -2	790:820	OBJECTIVE In this work, we suggest that both glycosylation (O-GlcNAc modification) and phosphorylation of IRS-1 and -2 are involved in the pathogenesis of T2DM.
32798372	5	15	theme	IRS-1	809:813	arg1	glycosylation					748:760	glycosylation	748:760	glycosylation (O-GlcNAc modification)	748:784	OBJECTIVE In this work, we suggest that both glycosylation (O-GlcNAc modification) and phosphorylation of IRS-1 and -2 are involved in the pathogenesis of T2DM.
32798372	5	15	theme	IRS-1	809:813	arg1	modification					772:783	O-GlcNAc modification	763:783	O-GlcNAc modification	763:783	OBJECTIVE In this work, we suggest that both glycosylation (O-GlcNAc modification) and phosphorylation of IRS-1 and -2 are involved in the pathogenesis of T2DM.
32798372	3	16	theme	insulin	464:470	arg1	pathway					492:498	the insulin receptor signalling pathway	460:498	the insulin receptor signalling pathway	460:498	Insulin receptor substrate (IRS) proteins are adaptor proteins in the insulin receptor signalling pathway.
32798372	1	17	theme	chronic	141:147	arg1	disorder					159:166	the chronic metabolic disorder Type 2 diabetes mellitus (T2DM)	137:198	the chronic metabolic disorder Type 2 diabetes mellitus (T2DM)	137:198	BACKGROUND The prevalence of the chronic metabolic disorder Type 2 diabetes mellitus (T2DM) is increasing steadily, and has even turned into an epidemic in some countries.
32798372	9	18	theme	elevated	1475:1482	arg1	levels					1484:1489	elevated levels	1475:1489	elevated levels of O-GlcNAc-modified proteins	1475:1519	DISCUSSION In this work OGlcNAc-modified proteins were specifically detected using O-Glc- NAc-specific antibodies, suggesting that elevated levels of O-GlcNAc-modified proteins are found, independently of their possible involvement in Advanced Glycation End products (AGEs).
32798372	1	19	theme	metabolic	149:157	arg1	disorder					159:166	the chronic metabolic disorder Type 2 diabetes mellitus (T2DM)	137:198	the chronic metabolic disorder Type 2 diabetes mellitus (T2DM)	137:198	BACKGROUND The prevalence of the chronic metabolic disorder Type 2 diabetes mellitus (T2DM) is increasing steadily, and has even turned into an epidemic in some countries.
32798372	0	20	theme	Phosphorylated	0:13	arg1	Ser1101					44:50	Ser1101	44:50	Ser1101	44:50	Phosphorylated and O-GlcNAc Modified IRS-1 (Ser1101) and -2 (Ser1149) Contribute to Human Diabetes Type II.
32798372	0	20	theme	Phosphorylated	0:13	arg1	IRS-1					37:41	Phosphorylated and O-GlcNAc Modified IRS-1	0:41	Phosphorylated and O-GlcNAc Modified IRS-1 (Ser1101)	0:51	Phosphorylated and O-GlcNAc Modified IRS-1 (Ser1101) and -2 (Ser1149) Contribute to Human Diabetes Type II.
32798372	8	21	from	IRS-1	1248:1252	arg1	Ser1149					1278:1284	Ser1149	1278:1284	Ser1149	1278:1284	Whereas when the same (IRS-1 on Ser1101 and IRS-2 on Ser1149) are phosphorylated, the insulin signalling is inhibited.
32798372	8	21	from	IRS-1	1248:1252	arg1	Ser1101					1257:1263	Ser1101	1257:1263	Ser1101	1257:1263	Whereas when the same (IRS-1 on Ser1101 and IRS-2 on Ser1149) are phosphorylated, the insulin signalling is inhibited.
32798372	4	22	theme	insulin	683:689	arg1	resistance					691:700	insulin resistance	683:700	insulin resistance	683:700	The insulin signalling is controlled through tyrosine phosphorylation of IRS-1 and IRS-2, and dysregulation of IRS proteins signalling may lead to glucose intolerance and eventually insulin resistance.
32798372	9	23	from	involvement	1564:1574	arg1	AGEs					1612:1615	AGEs	1612:1615	AGEs	1612:1615	DISCUSSION In this work OGlcNAc-modified proteins were specifically detected using O-Glc- NAc-specific antibodies, suggesting that elevated levels of O-GlcNAc-modified proteins are found, independently of their possible involvement in Advanced Glycation End products (AGEs).
32798372	9	23	from	involvement	1564:1574	arg1	products					1602:1609	Advanced Glycation End products	1579:1609	Advanced Glycation End products (AGEs)	1579:1616	DISCUSSION In this work OGlcNAc-modified proteins were specifically detected using O-Glc- NAc-specific antibodies, suggesting that elevated levels of O-GlcNAc-modified proteins are found, independently of their possible involvement in Advanced Glycation End products (AGEs).
32798372	1	24	theme	disorder	159:166	arg1	prevalence					123:132	The prevalence	119:132	The prevalence of the chronic metabolic disorder Type 2 diabetes mellitus (T2DM)	119:198	BACKGROUND The prevalence of the chronic metabolic disorder Type 2 diabetes mellitus (T2DM) is increasing steadily, and has even turned into an epidemic in some countries.
32798372	0	25	theme	Modified	28:35	arg1	Ser1101					44:50	Ser1101	44:50	Ser1101	44:50	Phosphorylated and O-GlcNAc Modified IRS-1 (Ser1101) and -2 (Ser1149) Contribute to Human Diabetes Type II.
32798372	0	25	theme	Modified	28:35	arg1	IRS-1					37:41	Phosphorylated and O-GlcNAc Modified IRS-1	0:41	Phosphorylated and O-GlcNAc Modified IRS-1 (Ser1101)	0:51	Phosphorylated and O-GlcNAc Modified IRS-1 (Ser1101) and -2 (Ser1149) Contribute to Human Diabetes Type II.
32798372	6	26	from	Ser1101	916:922	arg1	IRS-2					948:952	IRS-2	948:952	IRS-2	948:952	METHODS Phosphorylation and O-GlcNAc modifications (Ser1101 in IRS-1 and Ser1149 in IRS-2) proteins were determined experimentally by sandwich ELISA with specific antibodies and with bioinformatics tools.
32798372	6	26	from	Ser1101	916:922	arg1	Ser1149					937:943	Ser1149	937:943	Ser1149	937:943	METHODS Phosphorylation and O-GlcNAc modifications (Ser1101 in IRS-1 and Ser1149 in IRS-2) proteins were determined experimentally by sandwich ELISA with specific antibodies and with bioinformatics tools.
32798372	6	26	from	Ser1101	916:922	arg1	IRS-1					927:931	IRS-1	927:931	IRS-1	927:931	METHODS Phosphorylation and O-GlcNAc modifications (Ser1101 in IRS-1 and Ser1149 in IRS-2) proteins were determined experimentally by sandwich ELISA with specific antibodies and with bioinformatics tools.
32798372	1	27	dep	BACKGROUND	108:117	arg1	turned					237:242	turned	237:242	has even turned into an epidemic in some countries	228:277	BACKGROUND The prevalence of the chronic metabolic disorder Type 2 diabetes mellitus (T2DM) is increasing steadily, and has even turned into an epidemic in some countries.
32798372	1	27	dep	BACKGROUND	108:117	arg1	increasing					203:212	increasing	203:212	is increasing steadily	200:221	BACKGROUND The prevalence of the chronic metabolic disorder Type 2 diabetes mellitus (T2DM) is increasing steadily, and has even turned into an epidemic in some countries.
32798372	9	28	theme	OGlcNAc-modified	1368:1383	arg1	proteins					1385:1392	OGlcNAc-modified proteins	1368:1392	this work OGlcNAc-modified proteins	1358:1392	DISCUSSION In this work OGlcNAc-modified proteins were specifically detected using O-Glc- NAc-specific antibodies, suggesting that elevated levels of O-GlcNAc-modified proteins are found, independently of their possible involvement in Advanced Glycation End products (AGEs).
32798372	1	29	theme	Type	168:171	arg1	T2DM					194:197	T2DM	194:197	T2DM	194:197	BACKGROUND The prevalence of the chronic metabolic disorder Type 2 diabetes mellitus (T2DM) is increasing steadily, and has even turned into an epidemic in some countries.
32798372	1	29	theme	Type	168:171	arg1	mellitus					184:191	Type 2 diabetes mellitus	168:191	the chronic metabolic disorder Type 2 diabetes mellitus (T2DM)	137:198	BACKGROUND The prevalence of the chronic metabolic disorder Type 2 diabetes mellitus (T2DM) is increasing steadily, and has even turned into an epidemic in some countries.
32798372	2	30	theme	insulin	366:372	arg1	resistance					374:383	insulin resistance	366:383	insulin resistance in T2DM	366:391	T2DM results from defective responses to insulin and obesity is a major factor behind insulin resistance in T2DM.
32798372	4	31	theme	insulin	505:511	arg1	signalling					513:522	The insulin signalling	501:522	The insulin signalling	501:522	The insulin signalling is controlled through tyrosine phosphorylation of IRS-1 and IRS-2, and dysregulation of IRS proteins signalling may lead to glucose intolerance and eventually insulin resistance.
32798372	0	32	theme	Diabetes	90:97	arg1	Type					99:102	Human Diabetes Type II	84:105	Human Diabetes Type II	84:105	Phosphorylated and O-GlcNAc Modified IRS-1 (Ser1101) and -2 (Ser1149) Contribute to Human Diabetes Type II.
32798372	5	33	theme	O-GlcNAc	763:770	arg1	glycosylation					748:760	glycosylation	748:760	glycosylation (O-GlcNAc modification)	748:784	OBJECTIVE In this work, we suggest that both glycosylation (O-GlcNAc modification) and phosphorylation of IRS-1 and -2 are involved in the pathogenesis of T2DM.
32798372	5	33	theme	O-GlcNAc	763:770	arg1	modification					772:783	O-GlcNAc modification	763:783	O-GlcNAc modification	763:783	OBJECTIVE In this work, we suggest that both glycosylation (O-GlcNAc modification) and phosphorylation of IRS-1 and -2 are involved in the pathogenesis of T2DM.
32798372	3	34	theme	substrate	411:419	arg1	proteins					427:434	Insulin receptor substrate (IRS) proteins	394:434	Insulin receptor substrate (IRS) proteins	394:434	Insulin receptor substrate (IRS) proteins are adaptor proteins in the insulin receptor signalling pathway.
32798372	3	34	theme	substrate	411:419	arg1	proteins					448:455	adaptor proteins	440:455	adaptor proteins	440:455	Insulin receptor substrate (IRS) proteins are adaptor proteins in the insulin receptor signalling pathway.
32798372	5	35	theme	T2DM	858:861	arg1	pathogenesis					842:853	the pathogenesis	838:853	the pathogenesis of T2DM	838:861	OBJECTIVE In this work, we suggest that both glycosylation (O-GlcNAc modification) and phosphorylation of IRS-1 and -2 are involved in the pathogenesis of T2DM.
32798372	1	36	theme	diabetes	175:182	arg1	T2DM					194:197	T2DM	194:197	T2DM	194:197	BACKGROUND The prevalence of the chronic metabolic disorder Type 2 diabetes mellitus (T2DM) is increasing steadily, and has even turned into an epidemic in some countries.
32798372	1	36	theme	diabetes	175:182	arg1	mellitus					184:191	Type 2 diabetes mellitus	168:191	the chronic metabolic disorder Type 2 diabetes mellitus (T2DM)	137:198	BACKGROUND The prevalence of the chronic metabolic disorder Type 2 diabetes mellitus (T2DM) is increasing steadily, and has even turned into an epidemic in some countries.
32798372	8	37	theme	insulin	1311:1317	arg1	signalling					1319:1328	the insulin signalling	1307:1328	the insulin signalling	1307:1328	Whereas when the same (IRS-1 on Ser1101 and IRS-2 on Ser1149) are phosphorylated, the insulin signalling is inhibited.
32798372	4	38	theme	IRS	612:614	arg1	proteins					616:623	IRS proteins	612:623	IRS proteins signalling	612:634	The insulin signalling is controlled through tyrosine phosphorylation of IRS-1 and IRS-2, and dysregulation of IRS proteins signalling may lead to glucose intolerance and eventually insulin resistance.
32798372	2	39	theme	major	346:350	arg1	obesity					333:339	obesity	333:339	obesity	333:339	T2DM results from defective responses to insulin and obesity is a major factor behind insulin resistance in T2DM.
32798372	2	39	theme	major	346:350	arg1	factor					352:357	a major factor	344:357	a major factor behind insulin resistance in T2DM	344:391	T2DM results from defective responses to insulin and obesity is a major factor behind insulin resistance in T2DM.
32798372	6	40	theme	specific	1018:1025	arg1	antibodies					1027:1036	specific antibodies	1018:1036	specific antibodies	1018:1036	METHODS Phosphorylation and O-GlcNAc modifications (Ser1101 in IRS-1 and Ser1149 in IRS-2) proteins were determined experimentally by sandwich ELISA with specific antibodies and with bioinformatics tools.
32798372	6	41	theme	modifications	901:913	arg1	proteins					955:962	Phosphorylation and O-GlcNAc modifications (Ser1101 in IRS-1 and Ser1149 in IRS-2) proteins	872:962	METHODS Phosphorylation and O-GlcNAc modifications (Ser1101 in IRS-1 and Ser1149 in IRS-2) proteins	864:962	METHODS Phosphorylation and O-GlcNAc modifications (Ser1101 in IRS-1 and Ser1149 in IRS-2) proteins were determined experimentally by sandwich ELISA with specific antibodies and with bioinformatics tools.
32798372	5	42	theme	-2	819:820	arg1	phosphorylation					790:804	phosphorylation	790:804	phosphorylation of IRS-1 and -2	790:820	OBJECTIVE In this work, we suggest that both glycosylation (O-GlcNAc modification) and phosphorylation of IRS-1 and -2 are involved in the pathogenesis of T2DM.
32798372	5	42	theme	-2	819:820	arg1	glycosylation					748:760	glycosylation	748:760	glycosylation (O-GlcNAc modification)	748:784	OBJECTIVE In this work, we suggest that both glycosylation (O-GlcNAc modification) and phosphorylation of IRS-1 and -2 are involved in the pathogenesis of T2DM.
32798372	5	42	theme	-2	819:820	arg1	modification					772:783	O-GlcNAc modification	763:783	O-GlcNAc modification	763:783	OBJECTIVE In this work, we suggest that both glycosylation (O-GlcNAc modification) and phosphorylation of IRS-1 and -2 are involved in the pathogenesis of T2DM.
32798372	1	43	dep	disorder	159:166	arg1	T2DM					194:197	T2DM	194:197	T2DM	194:197	BACKGROUND The prevalence of the chronic metabolic disorder Type 2 diabetes mellitus (T2DM) is increasing steadily, and has even turned into an epidemic in some countries.
32798372	1	43	dep	disorder	159:166	arg1	mellitus					184:191	Type 2 diabetes mellitus	168:191	the chronic metabolic disorder Type 2 diabetes mellitus (T2DM)	137:198	BACKGROUND The prevalence of the chronic metabolic disorder Type 2 diabetes mellitus (T2DM) is increasing steadily, and has even turned into an epidemic in some countries.
32798372	3	44	theme	Insulin	394:400	arg1	IRS					422:424	IRS	422:424	IRS	422:424	Insulin receptor substrate (IRS) proteins are adaptor proteins in the insulin receptor signalling pathway.
32798372	3	44	theme	Insulin	394:400	arg1	substrate					411:419	Insulin receptor substrate	394:419	Insulin receptor substrate (IRS) proteins	394:434	Insulin receptor substrate (IRS) proteins are adaptor proteins in the insulin receptor signalling pathway.
32798372	1	45	from	countries	269:277	arg1	epidemic					252:259	epidemic	252:259	epidemic	252:259	BACKGROUND The prevalence of the chronic metabolic disorder Type 2 diabetes mellitus (T2DM) is increasing steadily, and has even turned into an epidemic in some countries.
32798372	6	46	theme	O-GlcNAc	892:899	arg1	modifications					901:913	O-GlcNAc modifications	892:913	O-GlcNAc modifications	892:913	METHODS Phosphorylation and O-GlcNAc modifications (Ser1101 in IRS-1 and Ser1149 in IRS-2) proteins were determined experimentally by sandwich ELISA with specific antibodies and with bioinformatics tools.
32798372	6	47	dep	Phosphorylation	872:886	arg1	Ser1101					916:922	Ser1101	916:922	Ser1101 in IRS-1 and Ser1149 in IRS-2	916:952	METHODS Phosphorylation and O-GlcNAc modifications (Ser1101 in IRS-1 and Ser1149 in IRS-2) proteins were determined experimentally by sandwich ELISA with specific antibodies and with bioinformatics tools.
32798372	10	48	theme	type	1761:1764	arg1	diabetes					1769:1776	type II diabetes	1761:1776	type II diabetes	1761:1776	CONCLUSION This study suggests a mechanism, which is controlled by posttranslational modifications, and may contribute to the pathogenesis of type II diabetes.
32798372	9	49	theme	O-Glc-	1427:1432	arg1	antibodies					1447:1456	O-Glc- NAc-specific antibodies	1427:1456	O-Glc- NAc-specific antibodies	1427:1456	DISCUSSION In this work OGlcNAc-modified proteins were specifically detected using O-Glc- NAc-specific antibodies, suggesting that elevated levels of O-GlcNAc-modified proteins are found, independently of their possible involvement in Advanced Glycation End products (AGEs).
32798372	7	50	from	IRS-1	1082:1086	arg1	Ser1101					1092:1098	Ser1101	1092:1098	Ser1101	1092:1098	RESULTS When IRS-1 (on Ser1101) and IRS-2 (Ser1149) become glycosylated following an increase in UDP-GlcNAc pools, it may contribute to insulin resistance.
32798372	9	51	from	DISCUSSION	1344:1353	arg1	work					1363:1366	this work OGlcNAc-modified proteins	1358:1392	this work OGlcNAc-modified proteins	1358:1392	DISCUSSION In this work OGlcNAc-modified proteins were specifically detected using O-Glc- NAc-specific antibodies, suggesting that elevated levels of O-GlcNAc-modified proteins are found, independently of their possible involvement in Advanced Glycation End products (AGEs).
32798372	7	52	from	increase	1154:1161	arg1	pools					1177:1181	UDP-GlcNAc pools	1166:1181	UDP-GlcNAc pools	1166:1181	RESULTS When IRS-1 (on Ser1101) and IRS-2 (Ser1149) become glycosylated following an increase in UDP-GlcNAc pools, it may contribute to insulin resistance.
32798372	9	53	dep	work	1363:1366	arg1	proteins					1385:1392	OGlcNAc-modified proteins	1368:1392	this work OGlcNAc-modified proteins	1358:1392	DISCUSSION In this work OGlcNAc-modified proteins were specifically detected using O-Glc- NAc-specific antibodies, suggesting that elevated levels of O-GlcNAc-modified proteins are found, independently of their possible involvement in Advanced Glycation End products (AGEs).
32798372	4	54	theme	glucose	648:654	arg1	intolerance					656:666	glucose intolerance	648:666	glucose intolerance	648:666	The insulin signalling is controlled through tyrosine phosphorylation of IRS-1 and IRS-2, and dysregulation of IRS proteins signalling may lead to glucose intolerance and eventually insulin resistance.
32798372	10	55	dep	CONCLUSION	1619:1628	arg1	suggests					1641:1648	suggests	1641:1648	suggests a mechanism, which is controlled by posttranslational modifications, and may contribute to the pathogenesis of type II diabetes	1641:1776	CONCLUSION This study suggests a mechanism, which is controlled by posttranslational modifications, and may contribute to the pathogenesis of type II diabetes.
32798372	6	56	theme	Phosphorylation	872:886	arg1	proteins					955:962	Phosphorylation and O-GlcNAc modifications (Ser1101 in IRS-1 and Ser1149 in IRS-2) proteins	872:962	METHODS Phosphorylation and O-GlcNAc modifications (Ser1101 in IRS-1 and Ser1149 in IRS-2) proteins	864:962	METHODS Phosphorylation and O-GlcNAc modifications (Ser1101 in IRS-1 and Ser1149 in IRS-2) proteins were determined experimentally by sandwich ELISA with specific antibodies and with bioinformatics tools.
32798372	9	57	theme	Advanced	1579:1586	arg1	AGEs					1612:1615	AGEs	1612:1615	AGEs	1612:1615	DISCUSSION In this work OGlcNAc-modified proteins were specifically detected using O-Glc- NAc-specific antibodies, suggesting that elevated levels of O-GlcNAc-modified proteins are found, independently of their possible involvement in Advanced Glycation End products (AGEs).
32798372	9	57	theme	Advanced	1579:1586	arg1	products					1602:1609	Advanced Glycation End products	1579:1609	Advanced Glycation End products (AGEs)	1579:1616	DISCUSSION In this work OGlcNAc-modified proteins were specifically detected using O-Glc- NAc-specific antibodies, suggesting that elevated levels of O-GlcNAc-modified proteins are found, independently of their possible involvement in Advanced Glycation End products (AGEs).
32798372	8	58	dep	same	1242:1245	arg1	IRS-1					1248:1252	IRS-1	1248:1252	IRS-1 on Ser1101	1248:1263	Whereas when the same (IRS-1 on Ser1101 and IRS-2 on Ser1149) are phosphorylated, the insulin signalling is inhibited.
32798372	8	58	dep	same	1242:1245	arg1	IRS-2					1269:1273	IRS-2	1269:1273	IRS-2 on Ser1149	1269:1284	Whereas when the same (IRS-1 on Ser1101 and IRS-2 on Ser1149) are phosphorylated, the insulin signalling is inhibited.
32798372	5	59	gly	glycosylation	748:760	arg1	pathogenesis					842:853	the pathogenesis	838:853	the pathogenesis of T2DM	838:861	OBJECTIVE In this work, we suggest that both glycosylation (O-GlcNAc modification) and phosphorylation of IRS-1 and -2 are involved in the pathogenesis of T2DM.
32798372	5	59	gly	glycosylation	748:760	arg1	-2					819:820	-2	819:820	-2	819:820	OBJECTIVE In this work, we suggest that both glycosylation (O-GlcNAc modification) and phosphorylation of IRS-1 and -2 are involved in the pathogenesis of T2DM.
32798372	5	59	gly	glycosylation	748:760	arg1	IRS-1					809:813	IRS-1	809:813	IRS-1	809:813	OBJECTIVE In this work, we suggest that both glycosylation (O-GlcNAc modification) and phosphorylation of IRS-1 and -2 are involved in the pathogenesis of T2DM.
32798372	10	60	theme	posttranslational	1686:1702	arg1	modifications					1704:1716	posttranslational modifications	1686:1716	posttranslational modifications	1686:1716	CONCLUSION This study suggests a mechanism, which is controlled by posttranslational modifications, and may contribute to the pathogenesis of type II diabetes.
32798372	6	61	with	ELISA	1007:1011	arg1	tools					1062:1066	bioinformatics tools	1047:1066	bioinformatics tools	1047:1066	METHODS Phosphorylation and O-GlcNAc modifications (Ser1101 in IRS-1 and Ser1149 in IRS-2) proteins were determined experimentally by sandwich ELISA with specific antibodies and with bioinformatics tools.
32798372	6	61	with	ELISA	1007:1011	arg1	antibodies					1027:1036	specific antibodies	1018:1036	specific antibodies	1018:1036	METHODS Phosphorylation and O-GlcNAc modifications (Ser1101 in IRS-1 and Ser1149 in IRS-2) proteins were determined experimentally by sandwich ELISA with specific antibodies and with bioinformatics tools.
32798372	9	62	theme	Glycation	1588:1596	arg1	AGEs					1612:1615	AGEs	1612:1615	AGEs	1612:1615	DISCUSSION In this work OGlcNAc-modified proteins were specifically detected using O-Glc- NAc-specific antibodies, suggesting that elevated levels of O-GlcNAc-modified proteins are found, independently of their possible involvement in Advanced Glycation End products (AGEs).
32798372	9	62	theme	Glycation	1588:1596	arg1	products					1602:1609	Advanced Glycation End products	1579:1609	Advanced Glycation End products (AGEs)	1579:1616	DISCUSSION In this work OGlcNAc-modified proteins were specifically detected using O-Glc- NAc-specific antibodies, suggesting that elevated levels of O-GlcNAc-modified proteins are found, independently of their possible involvement in Advanced Glycation End products (AGEs).
32798372	7	63	theme	insulin	1205:1211	arg1	resistance					1213:1222	insulin resistance	1205:1222	insulin resistance	1205:1222	RESULTS When IRS-1 (on Ser1101) and IRS-2 (Ser1149) become glycosylated following an increase in UDP-GlcNAc pools, it may contribute to insulin resistance.
32798372	8	64	from	IRS-2	1269:1273	arg1	Ser1149					1278:1284	Ser1149	1278:1284	Ser1149	1278:1284	Whereas when the same (IRS-1 on Ser1101 and IRS-2 on Ser1149) are phosphorylated, the insulin signalling is inhibited.
32798372	8	64	from	IRS-2	1269:1273	arg1	Ser1101					1257:1263	Ser1101	1257:1263	Ser1101	1257:1263	Whereas when the same (IRS-1 on Ser1101 and IRS-2 on Ser1149) are phosphorylated, the insulin signalling is inhibited.
32798372	4	65	theme	tyrosine	546:553	arg1	phosphorylation					555:569	tyrosine phosphorylation	546:569	tyrosine phosphorylation of IRS-1 and IRS-2	546:588	The insulin signalling is controlled through tyrosine phosphorylation of IRS-1 and IRS-2, and dysregulation of IRS proteins signalling may lead to glucose intolerance and eventually insulin resistance.
32798372	7	66	theme	UDP-GlcNAc	1166:1175	arg1	pools					1177:1181	UDP-GlcNAc pools	1166:1181	UDP-GlcNAc pools	1166:1181	RESULTS When IRS-1 (on Ser1101) and IRS-2 (Ser1149) become glycosylated following an increase in UDP-GlcNAc pools, it may contribute to insulin resistance.
32798372	9	67	theme	End	1598:1600	arg1	AGEs					1612:1615	AGEs	1612:1615	AGEs	1612:1615	DISCUSSION In this work OGlcNAc-modified proteins were specifically detected using O-Glc- NAc-specific antibodies, suggesting that elevated levels of O-GlcNAc-modified proteins are found, independently of their possible involvement in Advanced Glycation End products (AGEs).
32798372	9	67	theme	End	1598:1600	arg1	products					1602:1609	Advanced Glycation End products	1579:1609	Advanced Glycation End products (AGEs)	1579:1616	DISCUSSION In this work OGlcNAc-modified proteins were specifically detected using O-Glc- NAc-specific antibodies, suggesting that elevated levels of O-GlcNAc-modified proteins are found, independently of their possible involvement in Advanced Glycation End products (AGEs).
32798372	3	68	theme	receptor	402:409	arg1	IRS					422:424	IRS	422:424	IRS	422:424	Insulin receptor substrate (IRS) proteins are adaptor proteins in the insulin receptor signalling pathway.
32798372	3	68	theme	receptor	402:409	arg1	substrate					411:419	Insulin receptor substrate	394:419	Insulin receptor substrate (IRS) proteins	394:434	Insulin receptor substrate (IRS) proteins are adaptor proteins in the insulin receptor signalling pathway.
32798372	9	69	theme	NAc-specific	1434:1445	arg1	antibodies					1447:1456	O-Glc- NAc-specific antibodies	1427:1456	O-Glc- NAc-specific antibodies	1427:1456	DISCUSSION In this work OGlcNAc-modified proteins were specifically detected using O-Glc- NAc-specific antibodies, suggesting that elevated levels of O-GlcNAc-modified proteins are found, independently of their possible involvement in Advanced Glycation End products (AGEs).
32798372	4	70	theme	IRS-1	574:578	arg1	phosphorylation					555:569	tyrosine phosphorylation	546:569	tyrosine phosphorylation of IRS-1 and IRS-2	546:588	The insulin signalling is controlled through tyrosine phosphorylation of IRS-1 and IRS-2, and dysregulation of IRS proteins signalling may lead to glucose intolerance and eventually insulin resistance.
32798372	2	71	from	resistance	374:383	arg1	T2DM					388:391	T2DM	388:391	T2DM	388:391	T2DM results from defective responses to insulin and obesity is a major factor behind insulin resistance in T2DM.
32798372	4	72	theme	IRS-2	584:588	arg1	phosphorylation					555:569	tyrosine phosphorylation	546:569	tyrosine phosphorylation of IRS-1 and IRS-2	546:588	The insulin signalling is controlled through tyrosine phosphorylation of IRS-1 and IRS-2, and dysregulation of IRS proteins signalling may lead to glucose intolerance and eventually insulin resistance.
32798372	10	73	theme	diabetes	1769:1776	arg1	pathogenesis					1745:1756	the pathogenesis	1741:1756	the pathogenesis of type II diabetes	1741:1776	CONCLUSION This study suggests a mechanism, which is controlled by posttranslational modifications, and may contribute to the pathogenesis of type II diabetes.
32798372	9	74	theme	O-GlcNAc-modified	1494:1510	arg1	proteins					1512:1519	O-GlcNAc-modified proteins	1494:1519	O-GlcNAc-modified proteins	1494:1519	DISCUSSION In this work OGlcNAc-modified proteins were specifically detected using O-Glc- NAc-specific antibodies, suggesting that elevated levels of O-GlcNAc-modified proteins are found, independently of their possible involvement in Advanced Glycation End products (AGEs).
33226073	0	0	theme	cells	82:86	arg1	proliferation					37:49	proliferation	37:49	proliferation	37:49	O-GlcNAcylation of MEK2 promotes the proliferation and migration of breast cancer cells.
33226073	0	0	theme	cells	82:86	arg1	migration					55:63	migration	55:63	migration	55:63	O-GlcNAcylation of MEK2 promotes the proliferation and migration of breast cancer cells.
33226073	6	1	theme	spectrometry	730:741	arg1	analysis					743:750	Mass spectrometry analysis	725:750	Mass spectrometry analysis	725:750	Mass spectrometry analysis further verified that O-GlcNAcylation of MEK2 occurred at Thr13, which was in the docking domain for specifically identifying its target proteins.
33226073	1	2	theme	evolutionary	155:166	arg1	modules					188:194	evolutionary conserved signaling modules	155:194	evolutionary conserved signaling modules that are involved in a variety of cellular processes in response to environmental stimuli	155:284	Mitogen-activated protein kinase kinases are an important part of evolutionary conserved signaling modules that are involved in a variety of cellular processes in response to environmental stimuli.
33226073	5	3	mod	modified	703:710	arg1	MEK2					670:673	MEK2	670:673	MEK2	670:673	We found that MEK2 associated with OGT and was modified by O-GlcNAc.
33226073	5	3	mod	modified	703:710	arg3	O-GlcNAc					715:722	O-GlcNAc	715:722	O-GlcNAc	715:722	We found that MEK2 associated with OGT and was modified by O-GlcNAc.
33226073	0	4	theme	cancer	75:80	arg1	cells					82:86	breast cancer cells	68:86	breast cancer cells	68:86	O-GlcNAcylation of MEK2 promotes the proliferation and migration of breast cancer cells.
33226073	1	5	theme	conserved	168:176	arg1	modules					188:194	evolutionary conserved signaling modules	155:194	evolutionary conserved signaling modules that are involved in a variety of cellular processes in response to environmental stimuli	155:284	Mitogen-activated protein kinase kinases are an important part of evolutionary conserved signaling modules that are involved in a variety of cellular processes in response to environmental stimuli.
33226073	7	6	theme	MEK2	983:986	arg1	phosphorylation					964:978	phosphorylation	964:978	phosphorylation of MEK2	964:986	While total O-GlcNAcylation stimulated the protein stability and phosphorylation of MEK2, Thr13 O-GlcNAcylation of MEK2 specifically enhanced its Thr394 phosphorylation as well as downstream ERK1/2 activation.
33226073	7	6	theme	MEK2	983:986	arg1	stability					950:958	the protein stability	938:958	the protein stability	938:958	While total O-GlcNAcylation stimulated the protein stability and phosphorylation of MEK2, Thr13 O-GlcNAcylation of MEK2 specifically enhanced its Thr394 phosphorylation as well as downstream ERK1/2 activation.
33226073	2	7	theme	mitogen-activated	299:315	arg1	pathway					387:393	the most crucial upstream signaling pathway	351:393	the most crucial upstream signaling pathway of ERK1/2 cascade	351:411	Among them, mitogen-activated protein kinase kinase 2 (MEK2) is the most crucial upstream signaling pathway of ERK1/2 cascade as a therapeutic target for overcoming Ras-driven cancers.
33226073	2	7	theme	mitogen-activated	299:315	arg1	MEK2					342:345	MEK2	342:345	MEK2	342:345	Among them, mitogen-activated protein kinase kinase 2 (MEK2) is the most crucial upstream signaling pathway of ERK1/2 cascade as a therapeutic target for overcoming Ras-driven cancers.
33226073	2	7	theme	mitogen-activated	299:315	arg1	kinase					332:337	mitogen-activated protein kinase kinase 2	299:339	mitogen-activated protein kinase kinase 2 (MEK2)	299:346	Among them, mitogen-activated protein kinase kinase 2 (MEK2) is the most crucial upstream signaling pathway of ERK1/2 cascade as a therapeutic target for overcoming Ras-driven cancers.
33226073	1	8	theme	environmental	264:276	arg1	stimuli					278:284	environmental stimuli	264:284	environmental stimuli	264:284	Mitogen-activated protein kinase kinases are an important part of evolutionary conserved signaling modules that are involved in a variety of cellular processes in response to environmental stimuli.
33226073	3	9	theme	MEK2	499:502	arg1	regulation					504:513	MEK2 regulation	499:513	MEK2 regulation during tumor progression	499:538	However, the mechanisms of MEK2 regulation during tumor progression remain not fully elucidated.
33226073	6	10	theme	Mass	725:728	arg1	analysis					743:750	Mass spectrometry analysis	725:750	Mass spectrometry analysis	725:750	Mass spectrometry analysis further verified that O-GlcNAcylation of MEK2 occurred at Thr13, which was in the docking domain for specifically identifying its target proteins.
33226073	8	11	theme	cancer	1234:1239	arg1	cells					1241:1245	breast cancer cells	1227:1245	breast cancer cells	1227:1245	Genetic ablation of MEK2 O-GlcNAcylation at Thr13 abrogated its ability to promote the proliferation and migration of breast cancer cells.
33226073	8	12	theme	Genetic	1109:1115	arg1	ablation					1117:1124	Genetic ablation	1109:1124	Genetic ablation of MEK2 O-GlcNAcylation at Thr13	1109:1157	Genetic ablation of MEK2 O-GlcNAcylation at Thr13 abrogated its ability to promote the proliferation and migration of breast cancer cells.
33226073	7	13	theme	Thr13	989:993	arg1	O-GlcNAcylation					995:1009	Thr13 O-GlcNAcylation	989:1009	Thr13 O-GlcNAcylation of MEK2	989:1017	While total O-GlcNAcylation stimulated the protein stability and phosphorylation of MEK2, Thr13 O-GlcNAcylation of MEK2 specifically enhanced its Thr394 phosphorylation as well as downstream ERK1/2 activation.
33226073	1	14	theme	signaling	178:186	arg1	modules					188:194	evolutionary conserved signaling modules	155:194	evolutionary conserved signaling modules that are involved in a variety of cellular processes in response to environmental stimuli	155:284	Mitogen-activated protein kinase kinases are an important part of evolutionary conserved signaling modules that are involved in a variety of cellular processes in response to environmental stimuli.
33226073	8	15	theme	breast	1227:1232	arg1	cells					1241:1245	breast cancer cells	1227:1245	breast cancer cells	1227:1245	Genetic ablation of MEK2 O-GlcNAcylation at Thr13 abrogated its ability to promote the proliferation and migration of breast cancer cells.
33226073	9	16	theme	potential	1374:1382	arg1	target					1396:1401	a potential therapeutic target	1372:1401	a potential therapeutic target for tumor treatment	1372:1421	Together, our data demonstrate that O-GlcNAcylation of MEK2 might be a key regulatory mechanism during tumorigenesis and is a potential therapeutic target for tumor treatment.
33226073	1	17	theme	modules	188:194	arg1	kinases					122:128	Mitogen-activated protein kinase kinases	89:128	Mitogen-activated protein kinase kinases	89:128	Mitogen-activated protein kinase kinases are an important part of evolutionary conserved signaling modules that are involved in a variety of cellular processes in response to environmental stimuli.
33226073	1	17	theme	modules	188:194	arg1	part					147:150	an important part	134:150	an important part of evolutionary conserved signaling modules that are involved in a variety of cellular processes in response to environmental stimuli	134:284	Mitogen-activated protein kinase kinases are an important part of evolutionary conserved signaling modules that are involved in a variety of cellular processes in response to environmental stimuli.
33226073	2	18	theme	kinase	325:330	arg1	pathway					387:393	the most crucial upstream signaling pathway	351:393	the most crucial upstream signaling pathway of ERK1/2 cascade	351:411	Among them, mitogen-activated protein kinase kinase 2 (MEK2) is the most crucial upstream signaling pathway of ERK1/2 cascade as a therapeutic target for overcoming Ras-driven cancers.
33226073	2	18	theme	kinase	325:330	arg1	MEK2					342:345	MEK2	342:345	MEK2	342:345	Among them, mitogen-activated protein kinase kinase 2 (MEK2) is the most crucial upstream signaling pathway of ERK1/2 cascade as a therapeutic target for overcoming Ras-driven cancers.
33226073	2	18	theme	kinase	325:330	arg1	kinase					332:337	mitogen-activated protein kinase kinase 2	299:339	mitogen-activated protein kinase kinase 2 (MEK2)	299:346	Among them, mitogen-activated protein kinase kinase 2 (MEK2) is the most crucial upstream signaling pathway of ERK1/2 cascade as a therapeutic target for overcoming Ras-driven cancers.
33226073	2	19	theme	signaling	377:385	arg1	pathway					387:393	the most crucial upstream signaling pathway	351:393	the most crucial upstream signaling pathway of ERK1/2 cascade	351:411	Among them, mitogen-activated protein kinase kinase 2 (MEK2) is the most crucial upstream signaling pathway of ERK1/2 cascade as a therapeutic target for overcoming Ras-driven cancers.
33226073	2	19	theme	signaling	377:385	arg1	kinase					332:337	mitogen-activated protein kinase kinase 2	299:339	mitogen-activated protein kinase kinase 2 (MEK2)	299:346	Among them, mitogen-activated protein kinase kinase 2 (MEK2) is the most crucial upstream signaling pathway of ERK1/2 cascade as a therapeutic target for overcoming Ras-driven cancers.
33226073	8	20	theme	cells	1241:1245	arg1	proliferation					1196:1208	proliferation	1196:1208	proliferation	1196:1208	Genetic ablation of MEK2 O-GlcNAcylation at Thr13 abrogated its ability to promote the proliferation and migration of breast cancer cells.
33226073	8	20	theme	cells	1241:1245	arg1	migration					1214:1222	migration	1214:1222	migration	1214:1222	Genetic ablation of MEK2 O-GlcNAcylation at Thr13 abrogated its ability to promote the proliferation and migration of breast cancer cells.
33226073	9	21	theme	regulatory	1323:1332	arg1	mechanism					1334:1342	a key regulatory mechanism	1317:1342	a key regulatory mechanism	1317:1342	Together, our data demonstrate that O-GlcNAcylation of MEK2 might be a key regulatory mechanism during tumorigenesis and is a potential therapeutic target for tumor treatment.
33226073	9	21	theme	regulatory	1323:1332	arg1	O-GlcNAcylation					1284:1298	O-GlcNAcylation	1284:1298	O-GlcNAcylation of MEK2	1284:1306	Together, our data demonstrate that O-GlcNAcylation of MEK2 might be a key regulatory mechanism during tumorigenesis and is a potential therapeutic target for tumor treatment.
33226073	1	22	theme	Mitogen-activated	89:105	arg1	kinases					122:128	Mitogen-activated protein kinase kinases	89:128	Mitogen-activated protein kinase kinases	89:128	Mitogen-activated protein kinase kinases are an important part of evolutionary conserved signaling modules that are involved in a variety of cellular processes in response to environmental stimuli.
33226073	1	22	theme	Mitogen-activated	89:105	arg1	part					147:150	an important part	134:150	an important part of evolutionary conserved signaling modules that are involved in a variety of cellular processes in response to environmental stimuli	134:284	Mitogen-activated protein kinase kinases are an important part of evolutionary conserved signaling modules that are involved in a variety of cellular processes in response to environmental stimuli.
33226073	2	23	theme	upstream	368:375	arg1	pathway					387:393	the most crucial upstream signaling pathway	351:393	the most crucial upstream signaling pathway of ERK1/2 cascade	351:411	Among them, mitogen-activated protein kinase kinase 2 (MEK2) is the most crucial upstream signaling pathway of ERK1/2 cascade as a therapeutic target for overcoming Ras-driven cancers.
33226073	2	23	theme	upstream	368:375	arg1	kinase					332:337	mitogen-activated protein kinase kinase 2	299:339	mitogen-activated protein kinase kinase 2 (MEK2)	299:346	Among them, mitogen-activated protein kinase kinase 2 (MEK2) is the most crucial upstream signaling pathway of ERK1/2 cascade as a therapeutic target for overcoming Ras-driven cancers.
33226073	8	24	theme	O-GlcNAcylation	1134:1148	arg1	ablation					1117:1124	Genetic ablation	1109:1124	Genetic ablation of MEK2 O-GlcNAcylation at Thr13	1109:1157	Genetic ablation of MEK2 O-GlcNAcylation at Thr13 abrogated its ability to promote the proliferation and migration of breast cancer cells.
33226073	2	25	theme	protein	317:323	arg1	pathway					387:393	the most crucial upstream signaling pathway	351:393	the most crucial upstream signaling pathway of ERK1/2 cascade	351:411	Among them, mitogen-activated protein kinase kinase 2 (MEK2) is the most crucial upstream signaling pathway of ERK1/2 cascade as a therapeutic target for overcoming Ras-driven cancers.
33226073	2	25	theme	protein	317:323	arg1	MEK2					342:345	MEK2	342:345	MEK2	342:345	Among them, mitogen-activated protein kinase kinase 2 (MEK2) is the most crucial upstream signaling pathway of ERK1/2 cascade as a therapeutic target for overcoming Ras-driven cancers.
33226073	2	25	theme	protein	317:323	arg1	kinase					332:337	mitogen-activated protein kinase kinase 2	299:339	mitogen-activated protein kinase kinase 2 (MEK2)	299:346	Among them, mitogen-activated protein kinase kinase 2 (MEK2) is the most crucial upstream signaling pathway of ERK1/2 cascade as a therapeutic target for overcoming Ras-driven cancers.
33226073	0	26	theme	MEK2	19:22	arg1	O-GlcNAcylation					0:14	O-GlcNAcylation	0:14	O-GlcNAcylation of MEK2	0:22	O-GlcNAcylation of MEK2 promotes the proliferation and migration of breast cancer cells.
33226073	9	27	theme	tumor	1407:1411	arg1	treatment					1413:1421	tumor treatment	1407:1421	tumor treatment	1407:1421	Together, our data demonstrate that O-GlcNAcylation of MEK2 might be a key regulatory mechanism during tumorigenesis and is a potential therapeutic target for tumor treatment.
33226073	7	28	theme	Thr394	1045:1050	arg1	phosphorylation					1052:1066	its Thr394 phosphorylation	1041:1066	its Thr394 phosphorylation as well as downstream ERK1/2 activation	1041:1106	While total O-GlcNAcylation stimulated the protein stability and phosphorylation of MEK2, Thr13 O-GlcNAcylation of MEK2 specifically enhanced its Thr394 phosphorylation as well as downstream ERK1/2 activation.
33226073	1	29	theme	kinase	115:120	arg1	kinases					122:128	Mitogen-activated protein kinase kinases	89:128	Mitogen-activated protein kinase kinases	89:128	Mitogen-activated protein kinase kinases are an important part of evolutionary conserved signaling modules that are involved in a variety of cellular processes in response to environmental stimuli.
33226073	1	29	theme	kinase	115:120	arg1	part					147:150	an important part	134:150	an important part of evolutionary conserved signaling modules that are involved in a variety of cellular processes in response to environmental stimuli	134:284	Mitogen-activated protein kinase kinases are an important part of evolutionary conserved signaling modules that are involved in a variety of cellular processes in response to environmental stimuli.
33226073	1	30	from	response	252:259	arg1	processes					239:247	cellular processes	230:247	cellular processes in response to environmental stimuli	230:284	Mitogen-activated protein kinase kinases are an important part of evolutionary conserved signaling modules that are involved in a variety of cellular processes in response to environmental stimuli.
33226073	1	30	from	response	252:259	arg1	variety					219:225	a variety	217:225	a variety of cellular processes in response to environmental stimuli	217:284	Mitogen-activated protein kinase kinases are an important part of evolutionary conserved signaling modules that are involved in a variety of cellular processes in response to environmental stimuli.
33226073	6	31	theme	target	882:887	arg1	proteins					889:896	its target proteins	878:896	its target proteins	878:896	Mass spectrometry analysis further verified that O-GlcNAcylation of MEK2 occurred at Thr13, which was in the docking domain for specifically identifying its target proteins.
33226073	8	32	theme	MEK2	1129:1132	arg1	O-GlcNAcylation					1134:1148	MEK2 O-GlcNAcylation	1129:1148	MEK2 O-GlcNAcylation	1129:1148	Genetic ablation of MEK2 O-GlcNAcylation at Thr13 abrogated its ability to promote the proliferation and migration of breast cancer cells.
33226073	2	33	theme	cascade	405:411	arg1	pathway					387:393	the most crucial upstream signaling pathway	351:393	the most crucial upstream signaling pathway of ERK1/2 cascade	351:411	Among them, mitogen-activated protein kinase kinase 2 (MEK2) is the most crucial upstream signaling pathway of ERK1/2 cascade as a therapeutic target for overcoming Ras-driven cancers.
33226073	2	33	theme	cascade	405:411	arg1	kinase					332:337	mitogen-activated protein kinase kinase 2	299:339	mitogen-activated protein kinase kinase 2 (MEK2)	299:346	Among them, mitogen-activated protein kinase kinase 2 (MEK2) is the most crucial upstream signaling pathway of ERK1/2 cascade as a therapeutic target for overcoming Ras-driven cancers.
33226073	9	34	dep	potential	1374:1382	arg1	therapeutic					1384:1394	therapeutic	1384:1394	therapeutic	1384:1394	Together, our data demonstrate that O-GlcNAcylation of MEK2 might be a key regulatory mechanism during tumorigenesis and is a potential therapeutic target for tumor treatment.
33226073	9	35	theme	MEK2	1303:1306	arg1	O-GlcNAcylation					1284:1298	O-GlcNAcylation	1284:1298	O-GlcNAcylation of MEK2	1284:1306	Together, our data demonstrate that O-GlcNAcylation of MEK2 might be a key regulatory mechanism during tumorigenesis and is a potential therapeutic target for tumor treatment.
33226073	9	35	theme	MEK2	1303:1306	arg1	mechanism					1334:1342	a key regulatory mechanism	1317:1342	a key regulatory mechanism	1317:1342	Together, our data demonstrate that O-GlcNAcylation of MEK2 might be a key regulatory mechanism during tumorigenesis and is a potential therapeutic target for tumor treatment.
33226073	6	36	theme	MEK2	793:796	arg1	O-GlcNAcylation					774:788	O-GlcNAcylation	774:788	O-GlcNAcylation of MEK2	774:796	Mass spectrometry analysis further verified that O-GlcNAcylation of MEK2 occurred at Thr13, which was in the docking domain for specifically identifying its target proteins.
33226073	2	37	theme	ERK1/2	398:403	arg1	cascade					405:411	ERK1/2 cascade	398:411	ERK1/2 cascade	398:411	Among them, mitogen-activated protein kinase kinase 2 (MEK2) is the most crucial upstream signaling pathway of ERK1/2 cascade as a therapeutic target for overcoming Ras-driven cancers.
33226073	1	38	from	processes	239:247	arg1	response					252:259	response	252:259	response to environmental stimuli	252:284	Mitogen-activated protein kinase kinases are an important part of evolutionary conserved signaling modules that are involved in a variety of cellular processes in response to environmental stimuli.
33226073	0	39	dep	proliferation	37:49	arg1	the					33:35	the	33:35	the	33:35	O-GlcNAcylation of MEK2 promotes the proliferation and migration of breast cancer cells.
33226073	1	40	from	variety	219:225	arg1	response					252:259	response	252:259	response to environmental stimuli	252:284	Mitogen-activated protein kinase kinases are an important part of evolutionary conserved signaling modules that are involved in a variety of cellular processes in response to environmental stimuli.
33226073	2	41	theme	Ras-driven	452:461	arg1	cancers					463:469	Ras-driven cancers	452:469	Ras-driven cancers	452:469	Among them, mitogen-activated protein kinase kinase 2 (MEK2) is the most crucial upstream signaling pathway of ERK1/2 cascade as a therapeutic target for overcoming Ras-driven cancers.
33226073	3	42	theme	regulation	504:513	arg1	mechanisms					485:494	the mechanisms	481:494	the mechanisms of MEK2 regulation during tumor progression	481:538	However, the mechanisms of MEK2 regulation during tumor progression remain not fully elucidated.
33226073	7	43	theme	protein	942:948	arg1	stability					950:958	the protein stability	938:958	the protein stability	938:958	While total O-GlcNAcylation stimulated the protein stability and phosphorylation of MEK2, Thr13 O-GlcNAcylation of MEK2 specifically enhanced its Thr394 phosphorylation as well as downstream ERK1/2 activation.
33226073	1	44	theme	protein	107:113	arg1	kinases					122:128	Mitogen-activated protein kinase kinases	89:128	Mitogen-activated protein kinase kinases	89:128	Mitogen-activated protein kinase kinases are an important part of evolutionary conserved signaling modules that are involved in a variety of cellular processes in response to environmental stimuli.
33226073	1	44	theme	protein	107:113	arg1	part					147:150	an important part	134:150	an important part of evolutionary conserved signaling modules that are involved in a variety of cellular processes in response to environmental stimuli	134:284	Mitogen-activated protein kinase kinases are an important part of evolutionary conserved signaling modules that are involved in a variety of cellular processes in response to environmental stimuli.
33226073	8	45	from	Thr13	1153:1157	arg1	ablation					1117:1124	Genetic ablation	1109:1124	Genetic ablation of MEK2 O-GlcNAcylation at Thr13	1109:1157	Genetic ablation of MEK2 O-GlcNAcylation at Thr13 abrogated its ability to promote the proliferation and migration of breast cancer cells.
33226073	7	46	theme	downstream	1079:1088	arg1	activation					1097:1106	downstream ERK1/2 activation	1079:1106	its Thr394 phosphorylation as well as downstream ERK1/2 activation	1041:1106	While total O-GlcNAcylation stimulated the protein stability and phosphorylation of MEK2, Thr13 O-GlcNAcylation of MEK2 specifically enhanced its Thr394 phosphorylation as well as downstream ERK1/2 activation.
33226073	9	47	theme	key	1319:1321	arg1	mechanism					1334:1342	a key regulatory mechanism	1317:1342	a key regulatory mechanism	1317:1342	Together, our data demonstrate that O-GlcNAcylation of MEK2 might be a key regulatory mechanism during tumorigenesis and is a potential therapeutic target for tumor treatment.
33226073	9	47	theme	key	1319:1321	arg1	O-GlcNAcylation					1284:1298	O-GlcNAcylation	1284:1298	O-GlcNAcylation of MEK2	1284:1306	Together, our data demonstrate that O-GlcNAcylation of MEK2 might be a key regulatory mechanism during tumorigenesis and is a potential therapeutic target for tumor treatment.
33226073	1	48	theme	important	137:145	arg1	kinases					122:128	Mitogen-activated protein kinase kinases	89:128	Mitogen-activated protein kinase kinases	89:128	Mitogen-activated protein kinase kinases are an important part of evolutionary conserved signaling modules that are involved in a variety of cellular processes in response to environmental stimuli.
33226073	1	48	theme	important	137:145	arg1	part					147:150	an important part	134:150	an important part of evolutionary conserved signaling modules that are involved in a variety of cellular processes in response to environmental stimuli	134:284	Mitogen-activated protein kinase kinases are an important part of evolutionary conserved signaling modules that are involved in a variety of cellular processes in response to environmental stimuli.
33226073	1	49	theme	cellular	230:237	arg1	processes					239:247	cellular processes	230:247	cellular processes in response to environmental stimuli	230:284	Mitogen-activated protein kinase kinases are an important part of evolutionary conserved signaling modules that are involved in a variety of cellular processes in response to environmental stimuli.
33226073	0	50	theme	breast	68:73	arg1	cells					82:86	breast cancer cells	68:86	breast cancer cells	68:86	O-GlcNAcylation of MEK2 promotes the proliferation and migration of breast cancer cells.
33226073	6	51	theme	docking	834:840	arg1	domain					842:847	the docking domain	830:847	the docking domain for specifically identifying its target proteins	830:896	Mass spectrometry analysis further verified that O-GlcNAcylation of MEK2 occurred at Thr13, which was in the docking domain for specifically identifying its target proteins.
33226073	7	52	theme	ERK1/2	1090:1095	arg1	activation					1097:1106	downstream ERK1/2 activation	1079:1106	its Thr394 phosphorylation as well as downstream ERK1/2 activation	1041:1106	While total O-GlcNAcylation stimulated the protein stability and phosphorylation of MEK2, Thr13 O-GlcNAcylation of MEK2 specifically enhanced its Thr394 phosphorylation as well as downstream ERK1/2 activation.
33226073	2	53	theme	crucial	360:366	arg1	pathway					387:393	the most crucial upstream signaling pathway	351:393	the most crucial upstream signaling pathway of ERK1/2 cascade	351:411	Among them, mitogen-activated protein kinase kinase 2 (MEK2) is the most crucial upstream signaling pathway of ERK1/2 cascade as a therapeutic target for overcoming Ras-driven cancers.
33226073	2	53	theme	crucial	360:366	arg1	kinase					332:337	mitogen-activated protein kinase kinase 2	299:339	mitogen-activated protein kinase kinase 2 (MEK2)	299:346	Among them, mitogen-activated protein kinase kinase 2 (MEK2) is the most crucial upstream signaling pathway of ERK1/2 cascade as a therapeutic target for overcoming Ras-driven cancers.
33226073	1	54	theme	processes	239:247	arg1	processes					239:247	cellular processes	230:247	cellular processes in response to environmental stimuli	230:284	Mitogen-activated protein kinase kinases are an important part of evolutionary conserved signaling modules that are involved in a variety of cellular processes in response to environmental stimuli.
33226073	1	54	theme	processes	239:247	arg1	variety					219:225	a variety	217:225	a variety of cellular processes in response to environmental stimuli	217:284	Mitogen-activated protein kinase kinases are an important part of evolutionary conserved signaling modules that are involved in a variety of cellular processes in response to environmental stimuli.
33226073	2	55	theme	therapeutic	418:428	arg1	target					430:435	a therapeutic target	416:435	a therapeutic target for overcoming Ras-driven cancers	416:469	Among them, mitogen-activated protein kinase kinase 2 (MEK2) is the most crucial upstream signaling pathway of ERK1/2 cascade as a therapeutic target for overcoming Ras-driven cancers.
33226073	7	56	theme	MEK2	1014:1017	arg1	O-GlcNAcylation					995:1009	Thr13 O-GlcNAcylation	989:1009	Thr13 O-GlcNAcylation of MEK2	989:1017	While total O-GlcNAcylation stimulated the protein stability and phosphorylation of MEK2, Thr13 O-GlcNAcylation of MEK2 specifically enhanced its Thr394 phosphorylation as well as downstream ERK1/2 activation.
33226073	3	57	theme	tumor	522:526	arg1	progression					528:538	tumor progression	522:538	tumor progression	522:538	However, the mechanisms of MEK2 regulation during tumor progression remain not fully elucidated.
33226073	7	58	theme	total	905:909	arg1	O-GlcNAcylation					911:925	total O-GlcNAcylation	905:925	total O-GlcNAcylation	905:925	While total O-GlcNAcylation stimulated the protein stability and phosphorylation of MEK2, Thr13 O-GlcNAcylation of MEK2 specifically enhanced its Thr394 phosphorylation as well as downstream ERK1/2 activation.
14597631	11	0	theme	CBP	1578:1580	arg1	coactivator					1549:1559	the coactivator	1545:1559	the coactivator of transcription CBP, an essential interaction for Stat5-mediated gene transcription	1545:1644	Only the glycosylated form of Stat5 was able to bind the coactivator of transcription CBP, an essential interaction for Stat5-mediated gene transcription.
14597631	2	1	theme	transcription	354:366	arg1	induction					336:344	interferon induction	325:344	interferon induction of gene transcription	325:366	Members of this gene family mediate interferon induction of gene transcription and the response to a large number of growth factors and hormones.
14597631	2	1	theme	transcription	354:366	arg1	response					376:383	the response	372:383	the response to a large number of growth factors and hormones	372:432	Members of this gene family mediate interferon induction of gene transcription and the response to a large number of growth factors and hormones.
14597631	0	2	theme	glycosylated	88:99	arg1	form					101:104	the glycosylated form	84:104	the glycosylated form of Stat5	84:113	The coactivator of transcription CREB-binding protein interacts preferentially with the glycosylated form of Stat5.
14597631	5	3	from	tyrosine	814:821	arg1	phosphorylation					795:809	the crucial phosphorylation	783:809	the crucial phosphorylation at tyrosine 694	783:825	In addition to the crucial phosphorylation at tyrosine 694, we have identified an O-linked N-acetylglucosamine (O-GlcNAc) as another secondary modification essential for the transcriptional induction by Stat5.
14597631	2	4	theme	gene	349:352	arg1	transcription					354:366	gene transcription	349:366	gene transcription	349:366	Members of this gene family mediate interferon induction of gene transcription and the response to a large number of growth factors and hormones.
14597631	0	5	theme	Stat5	109:113	arg1	form					101:104	the glycosylated form	84:104	the glycosylated form of Stat5	84:113	The coactivator of transcription CREB-binding protein interacts preferentially with the glycosylated form of Stat5.
14597631	11	6	theme	Stat5-mediated	1612:1625	arg1	transcription					1632:1644	Stat5-mediated gene transcription	1612:1644	Stat5-mediated gene transcription	1612:1644	Only the glycosylated form of Stat5 was able to bind the coactivator of transcription CBP, an essential interaction for Stat5-mediated gene transcription.
14597631	10	7	theme	promoter	1482:1489	arg1	transactivation					1449:1463	transactivation	1449:1463	transactivation of a target gene promoter	1449:1489	Replacement of threonine 92 by an alanine residue (Stat5a-T92A) strongly reduced the prolactin induction of Stat5a glycosylation and abolished transactivation of a target gene promoter.
14597631	9	8	theme	Mass	1211:1214	arg1	analysis					1230:1237	Mass spectrometric analysis	1211:1237	Mass spectrometric analysis	1211:1237	Mass spectrometric analysis revealed a glycosylated peptide in the N-terminal region of Stat5.
14597631	4	9	theme	key	690:692	arg1	phosphorylation					660:674	Prolactin-induced phosphorylation	642:674	Prolactin-induced phosphorylation of Stat5	642:683	Prolactin-induced phosphorylation of Stat5 is a key event in the development and differentiation of mammary epithelial cells.
14597631	4	9	theme	key	690:692	arg1	event					694:698	a key event	688:698	a key event in the development and differentiation of mammary epithelial cells	688:765	Prolactin-induced phosphorylation of Stat5 is a key event in the development and differentiation of mammary epithelial cells.
14597631	1	10	theme	common	262:267	arg1	mode					269:272	a common mode	260:272	a common mode of activation	260:286	The signal transducer and activator of transcription (Stat) gene family comprises seven members with similarities in their domain structure and a common mode of activation.
14597631	11	11	theme	gene	1627:1630	arg1	transcription					1632:1644	Stat5-mediated gene transcription	1612:1644	Stat5-mediated gene transcription	1612:1644	Only the glycosylated form of Stat5 was able to bind the coactivator of transcription CBP, an essential interaction for Stat5-mediated gene transcription.
14597631	1	12	from	similarities	217:228	arg1	structure					246:254	their domain structure	233:254	their domain structure	233:254	The signal transducer and activator of transcription (Stat) gene family comprises seven members with similarities in their domain structure and a common mode of activation.
14597631	9	13	theme	spectrometric	1216:1228	arg1	analysis					1230:1237	Mass spectrometric analysis	1211:1237	Mass spectrometric analysis	1211:1237	Mass spectrometric analysis revealed a glycosylated peptide in the N-terminal region of Stat5.
14597631	8	14	gly	Glycosylation	1116:1128	arg1	Stat5					1133:1137	Stat5	1133:1137	Stat5	1133:1137	Glycosylation of Stat5, however, does not seem to be a prerequisite for nuclear translocation.
14597631	4	15	theme	epithelial	750:759	arg1	cells					761:765	mammary epithelial cells	742:765	mammary epithelial cells	742:765	Prolactin-induced phosphorylation of Stat5 is a key event in the development and differentiation of mammary epithelial cells.
14597631	4	16	theme	mammary	742:748	arg1	cells					761:765	mammary epithelial cells	742:765	mammary epithelial cells	742:765	Prolactin-induced phosphorylation of Stat5 is a key event in the development and differentiation of mammary epithelial cells.
14597631	3	17	theme	transmembrane	467:479	arg1	receptors					481:489	transmembrane receptors	467:489	transmembrane receptors	467:489	Extracellular ligand binding to transmembrane receptors causes the intracellular activation of associated tyrosine kinases, phosphorylation of Stat molecules, dimerization, and translocation to the nucleus.
14597631	0	18	gly	glycosylated	88:99	arg1	Stat5					109:113	Stat5	109:113	Stat5	109:113	The coactivator of transcription CREB-binding protein interacts preferentially with the glycosylated form of Stat5.
14597631	0	18	gly	glycosylated	88:99	arg1	form					101:104	the glycosylated form	84:104	the glycosylated form of Stat5	84:113	The coactivator of transcription CREB-binding protein interacts preferentially with the glycosylated form of Stat5.
14597631	4	19	from	event	694:698	arg1	differentiation					723:737	differentiation	723:737	differentiation	723:737	Prolactin-induced phosphorylation of Stat5 is a key event in the development and differentiation of mammary epithelial cells.
14597631	4	19	from	event	694:698	arg1	development					707:717	development	707:717	development	707:717	Prolactin-induced phosphorylation of Stat5 is a key event in the development and differentiation of mammary epithelial cells.
14597631	2	20	theme	large	390:394	arg1	number					396:401	a large number	388:401	a large number of growth factors and hormones	388:432	Members of this gene family mediate interferon induction of gene transcription and the response to a large number of growth factors and hormones.
14597631	8	21	theme	nuclear	1188:1194	arg1	translocation					1196:1208	nuclear translocation	1188:1208	nuclear translocation	1188:1208	Glycosylation of Stat5, however, does not seem to be a prerequisite for nuclear translocation.
14597631	5	22	theme	transcriptional	942:956	arg1	induction					958:966	the transcriptional induction	938:966	the transcriptional induction by Stat5	938:975	In addition to the crucial phosphorylation at tyrosine 694, we have identified an O-linked N-acetylglucosamine (O-GlcNAc) as another secondary modification essential for the transcriptional induction by Stat5.
14597631	9	23	gly	glycosylated	1250:1261	arg1	peptide					1263:1269	a glycosylated peptide	1248:1269	a glycosylated peptide in the N-terminal region of Stat5	1248:1303	Mass spectrometric analysis revealed a glycosylated peptide in the N-terminal region of Stat5.
14597631	10	24	theme	target	1470:1475	arg1	promoter					1482:1489	a target gene promoter	1468:1489	a target gene promoter	1468:1489	Replacement of threonine 92 by an alanine residue (Stat5a-T92A) strongly reduced the prolactin induction of Stat5a glycosylation and abolished transactivation of a target gene promoter.
14597631	10	25	theme	threonine	1321:1329	arg1	Replacement					1306:1316	Replacement	1306:1316	Replacement of threonine 92 by an alanine residue (Stat5a-T92A)	1306:1368	Replacement of threonine 92 by an alanine residue (Stat5a-T92A) strongly reduced the prolactin induction of Stat5a glycosylation and abolished transactivation of a target gene promoter.
14597631	1	26	theme	gene	176:179	arg1	family					181:186	The signal transducer and activator of transcription (Stat) gene family	116:186	The signal transducer and activator of transcription (Stat) gene family	116:186	The signal transducer and activator of transcription (Stat) gene family comprises seven members with similarities in their domain structure and a common mode of activation.
14597631	3	27	theme	tyrosine	541:548	arg1	kinases					550:556	associated tyrosine kinases	530:556	associated tyrosine kinases	530:556	Extracellular ligand binding to transmembrane receptors causes the intracellular activation of associated tyrosine kinases, phosphorylation of Stat molecules, dimerization, and translocation to the nucleus.
14597631	11	28	gly	glycosylated	1501:1512	arg1	able					1532:1535	able	1532:1535	able	1532:1535	Only the glycosylated form of Stat5 was able to bind the coactivator of transcription CBP, an essential interaction for Stat5-mediated gene transcription.
14597631	11	28	gly	glycosylated	1501:1512	arg1	Stat5					1522:1526	Stat5	1522:1526	Stat5	1522:1526	Only the glycosylated form of Stat5 was able to bind the coactivator of transcription CBP, an essential interaction for Stat5-mediated gene transcription.
14597631	11	28	gly	glycosylated	1501:1512	arg1	form					1514:1517	Only the glycosylated form	1492:1517	Only the glycosylated form of Stat5	1492:1526	Only the glycosylated form of Stat5 was able to bind the coactivator of transcription CBP, an essential interaction for Stat5-mediated gene transcription.
14597631	2	29	theme	family	310:315	arg1	Members					289:295	Members	289:295	Members of this gene family	289:315	Members of this gene family mediate interferon induction of gene transcription and the response to a large number of growth factors and hormones.
14597631	5	30	theme	secondary	901:909	arg1	modification					911:922	another secondary modification	893:922	another secondary modification essential for the transcriptional induction by Stat5	893:975	In addition to the crucial phosphorylation at tyrosine 694, we have identified an O-linked N-acetylglucosamine (O-GlcNAc) as another secondary modification essential for the transcriptional induction by Stat5.
14597631	4	31	dep	development	707:717	arg1	the					703:705	the	703:705	the	703:705	Prolactin-induced phosphorylation of Stat5 is a key event in the development and differentiation of mammary epithelial cells.
14597631	9	32	theme	glycosylated	1250:1261	arg1	peptide					1263:1269	a glycosylated peptide	1248:1269	a glycosylated peptide in the N-terminal region of Stat5	1248:1303	Mass spectrometric analysis revealed a glycosylated peptide in the N-terminal region of Stat5.
14597631	2	33	theme	gene	305:308	arg1	family					310:315	this gene family	300:315	this gene family	300:315	Members of this gene family mediate interferon induction of gene transcription and the response to a large number of growth factors and hormones.
14597631	0	34	theme	transcription	19:31	arg1	protein					46:52	transcription CREB-binding protein	19:52	transcription CREB-binding protein	19:52	The coactivator of transcription CREB-binding protein interacts preferentially with the glycosylated form of Stat5.
14597631	1	35	theme	activation	277:286	arg1	members					204:210	seven members	198:210	seven members with similarities in their domain structure	198:254	The signal transducer and activator of transcription (Stat) gene family comprises seven members with similarities in their domain structure and a common mode of activation.
14597631	1	35	theme	activation	277:286	arg1	mode					269:272	a common mode	260:272	a common mode of activation	260:286	The signal transducer and activator of transcription (Stat) gene family comprises seven members with similarities in their domain structure and a common mode of activation.
14597631	10	36	theme	Stat5a	1414:1419	arg1	glycosylation					1421:1433	Stat5a glycosylation	1414:1433	Stat5a glycosylation	1414:1433	Replacement of threonine 92 by an alanine residue (Stat5a-T92A) strongly reduced the prolactin induction of Stat5a glycosylation and abolished transactivation of a target gene promoter.
14597631	3	37	theme	Stat	578:581	arg1	molecules					583:591	Stat molecules	578:591	Stat molecules	578:591	Extracellular ligand binding to transmembrane receptors causes the intracellular activation of associated tyrosine kinases, phosphorylation of Stat molecules, dimerization, and translocation to the nucleus.
14597631	2	38	theme	factors	413:419	arg1	number					396:401	a large number	388:401	a large number of growth factors and hormones	388:432	Members of this gene family mediate interferon induction of gene transcription and the response to a large number of growth factors and hormones.
14597631	5	39	theme	O-linked	850:857	arg1	O-GlcNAc					880:887	O-GlcNAc	880:887	O-GlcNAc	880:887	In addition to the crucial phosphorylation at tyrosine 694, we have identified an O-linked N-acetylglucosamine (O-GlcNAc) as another secondary modification essential for the transcriptional induction by Stat5.
14597631	5	39	theme	O-linked	850:857	arg1	N-acetylglucosamine					859:877	an O-linked N-acetylglucosamine	847:877	an O-linked N-acetylglucosamine (O-GlcNAc)	847:888	In addition to the crucial phosphorylation at tyrosine 694, we have identified an O-linked N-acetylglucosamine (O-GlcNAc) as another secondary modification essential for the transcriptional induction by Stat5.
14597631	3	40	theme	kinases	550:556	arg1	translocation					612:624	translocation	612:624	translocation	612:624	Extracellular ligand binding to transmembrane receptors causes the intracellular activation of associated tyrosine kinases, phosphorylation of Stat molecules, dimerization, and translocation to the nucleus.
14597631	3	40	theme	kinases	550:556	arg1	phosphorylation					559:573	phosphorylation	559:573	phosphorylation of Stat molecules	559:591	Extracellular ligand binding to transmembrane receptors causes the intracellular activation of associated tyrosine kinases, phosphorylation of Stat molecules, dimerization, and translocation to the nucleus.
14597631	3	40	theme	kinases	550:556	arg1	activation					516:525	the intracellular activation	498:525	the intracellular activation of associated tyrosine kinases	498:556	Extracellular ligand binding to transmembrane receptors causes the intracellular activation of associated tyrosine kinases, phosphorylation of Stat molecules, dimerization, and translocation to the nucleus.
14597631	3	40	theme	kinases	550:556	arg1	dimerization					594:605	dimerization	594:605	dimerization	594:605	Extracellular ligand binding to transmembrane receptors causes the intracellular activation of associated tyrosine kinases, phosphorylation of Stat molecules, dimerization, and translocation to the nucleus.
14597631	3	41	theme	molecules	583:591	arg1	translocation					612:624	translocation	612:624	translocation	612:624	Extracellular ligand binding to transmembrane receptors causes the intracellular activation of associated tyrosine kinases, phosphorylation of Stat molecules, dimerization, and translocation to the nucleus.
14597631	3	41	theme	molecules	583:591	arg1	phosphorylation					559:573	phosphorylation	559:573	phosphorylation of Stat molecules	559:591	Extracellular ligand binding to transmembrane receptors causes the intracellular activation of associated tyrosine kinases, phosphorylation of Stat molecules, dimerization, and translocation to the nucleus.
14597631	3	41	theme	molecules	583:591	arg1	activation					516:525	the intracellular activation	498:525	the intracellular activation of associated tyrosine kinases	498:556	Extracellular ligand binding to transmembrane receptors causes the intracellular activation of associated tyrosine kinases, phosphorylation of Stat molecules, dimerization, and translocation to the nucleus.
14597631	3	41	theme	molecules	583:591	arg1	dimerization					594:605	dimerization	594:605	dimerization	594:605	Extracellular ligand binding to transmembrane receptors causes the intracellular activation of associated tyrosine kinases, phosphorylation of Stat molecules, dimerization, and translocation to the nucleus.
14597631	10	42	theme	alanine	1340:1346	arg1	Stat5a-T92A					1357:1367	Stat5a-T92A	1357:1367	Stat5a-T92A	1357:1367	Replacement of threonine 92 by an alanine residue (Stat5a-T92A) strongly reduced the prolactin induction of Stat5a glycosylation and abolished transactivation of a target gene promoter.
14597631	10	42	theme	alanine	1340:1346	arg1	residue					1348:1354	an alanine residue	1337:1354	an alanine residue (Stat5a-T92A)	1337:1368	Replacement of threonine 92 by an alanine residue (Stat5a-T92A) strongly reduced the prolactin induction of Stat5a glycosylation and abolished transactivation of a target gene promoter.
14597631	2	43	theme	growth	406:411	arg1	factors					413:419	growth factors	406:419	growth factors	406:419	Members of this gene family mediate interferon induction of gene transcription and the response to a large number of growth factors and hormones.
14597631	0	44	theme	protein	46:52	arg1	coactivator					4:14	The coactivator	0:14	The coactivator of transcription CREB-binding protein	0:52	The coactivator of transcription CREB-binding protein interacts preferentially with the glycosylated form of Stat5.
14597631	3	45	theme	intracellular	502:514	arg1	activation					516:525	the intracellular activation	498:525	the intracellular activation of associated tyrosine kinases	498:556	Extracellular ligand binding to transmembrane receptors causes the intracellular activation of associated tyrosine kinases, phosphorylation of Stat molecules, dimerization, and translocation to the nucleus.
14597631	11	46	theme	glycosylated	1501:1512	arg1	able					1532:1535	able	1532:1535	able	1532:1535	Only the glycosylated form of Stat5 was able to bind the coactivator of transcription CBP, an essential interaction for Stat5-mediated gene transcription.
14597631	11	46	theme	glycosylated	1501:1512	arg1	form					1514:1517	Only the glycosylated form	1492:1517	Only the glycosylated form of Stat5	1492:1526	Only the glycosylated form of Stat5 was able to bind the coactivator of transcription CBP, an essential interaction for Stat5-mediated gene transcription.
14597631	3	47	theme	ligand	449:454	arg1	binding					456:462	Extracellular ligand binding	435:462	Extracellular ligand binding to transmembrane receptors	435:489	Extracellular ligand binding to transmembrane receptors causes the intracellular activation of associated tyrosine kinases, phosphorylation of Stat molecules, dimerization, and translocation to the nucleus.
14597631	0	48	theme	CREB-binding	33:44	arg1	protein					46:52	transcription CREB-binding protein	19:52	transcription CREB-binding protein	19:52	The coactivator of transcription CREB-binding protein interacts preferentially with the glycosylated form of Stat5.
14597631	1	49	with	members	204:210	arg1	similarities					217:228	similarities	217:228	similarities in their domain structure	217:254	The signal transducer and activator of transcription (Stat) gene family comprises seven members with similarities in their domain structure and a common mode of activation.
14597631	9	50	theme	N-terminal	1278:1287	arg1	region					1289:1294	the N-terminal region	1274:1294	the N-terminal region of Stat5	1274:1303	Mass spectrometric analysis revealed a glycosylated peptide in the N-terminal region of Stat5.
14597631	2	51	theme	hormones	425:432	arg1	number					396:401	a large number	388:401	a large number of growth factors and hormones	388:432	Members of this gene family mediate interferon induction of gene transcription and the response to a large number of growth factors and hormones.
14597631	4	52	theme	Stat5	679:683	arg1	phosphorylation					660:674	Prolactin-induced phosphorylation	642:674	Prolactin-induced phosphorylation of Stat5	642:683	Prolactin-induced phosphorylation of Stat5 is a key event in the development and differentiation of mammary epithelial cells.
14597631	4	52	theme	Stat5	679:683	arg1	event					694:698	a key event	688:698	a key event in the development and differentiation of mammary epithelial cells	688:765	Prolactin-induced phosphorylation of Stat5 is a key event in the development and differentiation of mammary epithelial cells.
14597631	10	53	theme	gene	1477:1480	arg1	promoter					1482:1489	a target gene promoter	1468:1489	a target gene promoter	1468:1489	Replacement of threonine 92 by an alanine residue (Stat5a-T92A) strongly reduced the prolactin induction of Stat5a glycosylation and abolished transactivation of a target gene promoter.
14597631	5	54	theme	essential	924:932	arg1	modification					911:922	another secondary modification	893:922	another secondary modification essential for the transcriptional induction by Stat5	893:975	In addition to the crucial phosphorylation at tyrosine 694, we have identified an O-linked N-acetylglucosamine (O-GlcNAc) as another secondary modification essential for the transcriptional induction by Stat5.
14597631	6	55	theme	nuclear	1014:1020	arg1	Stat5					1022:1026	nuclear Stat5	1014:1026	nuclear Stat5	1014:1026	This modification was only found on nuclear Stat5 after cytokine activation.
14597631	1	56	with	mode	269:272	arg1	similarities					217:228	similarities	217:228	similarities in their domain structure	217:254	The signal transducer and activator of transcription (Stat) gene family comprises seven members with similarities in their domain structure and a common mode of activation.
14597631	1	57	theme	signal	120:125	arg1	transducer					127:136	signal transducer	120:136	signal transducer	120:136	The signal transducer and activator of transcription (Stat) gene family comprises seven members with similarities in their domain structure and a common mode of activation.
14597631	8	58	theme	Stat5	1133:1137	arg1	Glycosylation					1116:1128	Glycosylation	1116:1128	Glycosylation of Stat5	1116:1137	Glycosylation of Stat5, however, does not seem to be a prerequisite for nuclear translocation.
14597631	8	58	theme	Stat5	1133:1137	arg1	prerequisite					1171:1182	a prerequisite	1169:1182	a prerequisite for nuclear translocation	1169:1208	Glycosylation of Stat5, however, does not seem to be a prerequisite for nuclear translocation.
14597631	7	59	theme	Similar	1055:1061	arg1	observations					1063:1074	Similar observations	1055:1074	Similar observations	1055:1074	Similar observations were made with Stat1, Stat3, and Stat6.
14597631	1	60	theme	transducer	127:136	arg1	family					181:186	The signal transducer and activator of transcription (Stat) gene family	116:186	The signal transducer and activator of transcription (Stat) gene family	116:186	The signal transducer and activator of transcription (Stat) gene family comprises seven members with similarities in their domain structure and a common mode of activation.
14597631	10	61	theme	glycosylation	1421:1433	arg1	induction					1401:1409	the prolactin induction	1387:1409	the prolactin induction of Stat5a glycosylation	1387:1433	Replacement of threonine 92 by an alanine residue (Stat5a-T92A) strongly reduced the prolactin induction of Stat5a glycosylation and abolished transactivation of a target gene promoter.
14597631	9	62	theme	Stat5	1299:1303	arg1	region					1289:1294	the N-terminal region	1274:1294	the N-terminal region of Stat5	1274:1303	Mass spectrometric analysis revealed a glycosylated peptide in the N-terminal region of Stat5.
14597631	11	63	theme	transcription	1564:1576	arg1	interaction					1596:1606	an essential interaction	1583:1606	an essential interaction for Stat5-mediated gene transcription	1583:1644	Only the glycosylated form of Stat5 was able to bind the coactivator of transcription CBP, an essential interaction for Stat5-mediated gene transcription.
14597631	11	63	theme	transcription	1564:1576	arg1	CBP					1578:1580	transcription CBP	1564:1580	transcription CBP	1564:1580	Only the glycosylated form of Stat5 was able to bind the coactivator of transcription CBP, an essential interaction for Stat5-mediated gene transcription.
14597631	2	64	theme	interferon	325:334	arg1	induction					336:344	interferon induction	325:344	interferon induction of gene transcription	325:366	Members of this gene family mediate interferon induction of gene transcription and the response to a large number of growth factors and hormones.
14597631	6	65	theme	cytokine	1034:1041	arg1	activation					1043:1052	cytokine activation	1034:1052	cytokine activation	1034:1052	This modification was only found on nuclear Stat5 after cytokine activation.
14597631	5	66	link	O-linked	850:857	arg1	O-GlcNAc					880:887	O-GlcNAc	880:887	O-GlcNAc	880:887	In addition to the crucial phosphorylation at tyrosine 694, we have identified an O-linked N-acetylglucosamine (O-GlcNAc) as another secondary modification essential for the transcriptional induction by Stat5.
14597631	5	66	link	O-linked	850:857	arg1	N-acetylglucosamine					859:877	an O-linked N-acetylglucosamine	847:877	an O-linked N-acetylglucosamine (O-GlcNAc)	847:888	In addition to the crucial phosphorylation at tyrosine 694, we have identified an O-linked N-acetylglucosamine (O-GlcNAc) as another secondary modification essential for the transcriptional induction by Stat5.
14597631	1	67	theme	activator	142:150	arg1	family					181:186	The signal transducer and activator of transcription (Stat) gene family	116:186	The signal transducer and activator of transcription (Stat) gene family	116:186	The signal transducer and activator of transcription (Stat) gene family comprises seven members with similarities in their domain structure and a common mode of activation.
14597631	11	68	theme	Stat5	1522:1526	arg1	able					1532:1535	able	1532:1535	able	1532:1535	Only the glycosylated form of Stat5 was able to bind the coactivator of transcription CBP, an essential interaction for Stat5-mediated gene transcription.
14597631	11	68	theme	Stat5	1522:1526	arg1	form					1514:1517	Only the glycosylated form	1492:1517	Only the glycosylated form of Stat5	1492:1526	Only the glycosylated form of Stat5 was able to bind the coactivator of transcription CBP, an essential interaction for Stat5-mediated gene transcription.
14597631	4	69	theme	cells	761:765	arg1	differentiation					723:737	differentiation	723:737	differentiation	723:737	Prolactin-induced phosphorylation of Stat5 is a key event in the development and differentiation of mammary epithelial cells.
14597631	4	69	theme	cells	761:765	arg1	development					707:717	development	707:717	development	707:717	Prolactin-induced phosphorylation of Stat5 is a key event in the development and differentiation of mammary epithelial cells.
14597631	11	70	theme	essential	1586:1594	arg1	interaction					1596:1606	an essential interaction	1583:1606	an essential interaction for Stat5-mediated gene transcription	1583:1644	Only the glycosylated form of Stat5 was able to bind the coactivator of transcription CBP, an essential interaction for Stat5-mediated gene transcription.
14597631	11	70	theme	essential	1586:1594	arg1	CBP					1578:1580	transcription CBP	1564:1580	transcription CBP	1564:1580	Only the glycosylated form of Stat5 was able to bind the coactivator of transcription CBP, an essential interaction for Stat5-mediated gene transcription.
14597631	6	71	located	found	1005:1009	arg2	modification					983:994	This modification	978:994	This modification	978:994	This modification was only found on nuclear Stat5 after cytokine activation.
14597631	6	71	located	found	1005:1009	arg1	Stat5					1022:1026	nuclear Stat5	1014:1026	nuclear Stat5	1014:1026	This modification was only found on nuclear Stat5 after cytokine activation.
14597631	4	72	theme	Prolactin-induced	642:658	arg1	phosphorylation					660:674	Prolactin-induced phosphorylation	642:674	Prolactin-induced phosphorylation of Stat5	642:683	Prolactin-induced phosphorylation of Stat5 is a key event in the development and differentiation of mammary epithelial cells.
14597631	4	72	theme	Prolactin-induced	642:658	arg1	event					694:698	a key event	688:698	a key event in the development and differentiation of mammary epithelial cells	688:765	Prolactin-induced phosphorylation of Stat5 is a key event in the development and differentiation of mammary epithelial cells.
14597631	3	73	theme	associated	530:539	arg1	kinases					550:556	associated tyrosine kinases	530:556	associated tyrosine kinases	530:556	Extracellular ligand binding to transmembrane receptors causes the intracellular activation of associated tyrosine kinases, phosphorylation of Stat molecules, dimerization, and translocation to the nucleus.
14597631	3	74	theme	Extracellular	435:447	arg1	binding					456:462	Extracellular ligand binding	435:462	Extracellular ligand binding to transmembrane receptors	435:489	Extracellular ligand binding to transmembrane receptors causes the intracellular activation of associated tyrosine kinases, phosphorylation of Stat molecules, dimerization, and translocation to the nucleus.
14597631	1	75	theme	domain	239:244	arg1	structure					246:254	their domain structure	233:254	their domain structure	233:254	The signal transducer and activator of transcription (Stat) gene family comprises seven members with similarities in their domain structure and a common mode of activation.
14597631	5	76	theme	crucial	787:793	arg1	phosphorylation					795:809	the crucial phosphorylation	783:809	the crucial phosphorylation at tyrosine 694	783:825	In addition to the crucial phosphorylation at tyrosine 694, we have identified an O-linked N-acetylglucosamine (O-GlcNAc) as another secondary modification essential for the transcriptional induction by Stat5.
14597631	10	77	theme	prolactin	1391:1399	arg1	induction					1401:1409	the prolactin induction	1387:1409	the prolactin induction of Stat5a glycosylation	1387:1433	Replacement of threonine 92 by an alanine residue (Stat5a-T92A) strongly reduced the prolactin induction of Stat5a glycosylation and abolished transactivation of a target gene promoter.
14597631	1	78	theme	transcription	155:167	arg1	activator					142:150	activator	142:150	activator of transcription (Stat)	142:174	The signal transducer and activator of transcription (Stat) gene family comprises seven members with similarities in their domain structure and a common mode of activation.
14597631	1	78	theme	transcription	155:167	arg1	transducer					127:136	signal transducer	120:136	signal transducer	120:136	The signal transducer and activator of transcription (Stat) gene family comprises seven members with similarities in their domain structure and a common mode of activation.
14597631	9	79	from	peptide	1263:1269	arg1	region					1289:1294	the N-terminal region	1274:1294	the N-terminal region of Stat5	1274:1303	Mass spectrometric analysis revealed a glycosylated peptide in the N-terminal region of Stat5.
29100056	10	0	theme	HBP	1039:1041	arg1	mechanism					994:1002	a molecular mechanism	982:1002	a molecular mechanism	982:1002	Together, our data establish a molecular mechanism and functional significance of the HBP in directly linking extracellular glucose signal to the Hippo-YAP pathway and tumorigenesis.
29100056	10	0	theme	HBP	1039:1041	arg1	significance					1019:1030	functional significance	1008:1030	functional significance	1008:1030	Together, our data establish a molecular mechanism and functional significance of the HBP in directly linking extracellular glucose signal to the Hippo-YAP pathway and tumorigenesis.
29100056	5	1	theme	O-GlcNAc	541:548	arg1	transferase					550:560	O-GlcNAc transferase	541:560	O-GlcNAc transferase (OGT) at serine 109	541:580	Mechanistically, the core component of Hippo pathway (YAP) is O-GlcNAcylated by O-GlcNAc transferase (OGT) at serine 109.
29100056	5	1	theme	O-GlcNAc	541:548	arg1	OGT					563:565	OGT	563:565	OGT	563:565	Mechanistically, the core component of Hippo pathway (YAP) is O-GlcNAcylated by O-GlcNAc transferase (OGT) at serine 109.
29100056	9	2	theme	glucose-induced	878:892	arg1	O-GlcNAcylation					898:912	glucose-induced YAP O-GlcNAcylation	878:912	glucose-induced YAP O-GlcNAcylation	878:912	Finally, we confirmed that glucose-induced YAP O-GlcNAcylation and activation promoted tumorigenesis.
29100056	10	3	theme	glucose	1077:1083	arg1	signal					1085:1090	extracellular glucose signal	1063:1090	extracellular glucose signal	1063:1090	Together, our data establish a molecular mechanism and functional significance of the HBP in directly linking extracellular glucose signal to the Hippo-YAP pathway and tumorigenesis.
29100056	6	4	theme	transcriptional	704:718	arg1	activity					720:727	its transcriptional activity	700:727	its transcriptional activity	700:727	YAP O-GlcNAcylation disrupts its interaction with upstream kinase LATS1, prevents its phosphorylation, and activates its transcriptional activity.
29100056	9	5	theme	YAP	894:896	arg1	O-GlcNAcylation					898:912	glucose-induced YAP O-GlcNAcylation	878:912	glucose-induced YAP O-GlcNAcylation	878:912	Finally, we confirmed that glucose-induced YAP O-GlcNAcylation and activation promoted tumorigenesis.
29100056	10	6	theme	extracellular	1063:1075	arg1	signal					1085:1090	extracellular glucose signal	1063:1090	extracellular glucose signal	1063:1090	Together, our data establish a molecular mechanism and functional significance of the HBP in directly linking extracellular glucose signal to the Hippo-YAP pathway and tumorigenesis.
29100056	1	7	from	homeostasis	133:143	arg1	crucial					92:98	crucial	92:98	crucial	92:98	The Hippo pathway is crucial in organ size control and tissue homeostasis, with deregulation leading to cancer.
29100056	1	7	from	homeostasis	133:143	arg1	pathway					81:87	The Hippo pathway	71:87	The Hippo pathway	71:87	The Hippo pathway is crucial in organ size control and tissue homeostasis, with deregulation leading to cancer.
29100056	2	8	theme	pathway	255:261	arg1	activation					263:272	the Hippo pathway activation	245:272	the Hippo pathway activation	245:272	An extracellular nutrition signal, such as glucose, regulates the Hippo pathway activation.
29100056	8	9	theme	YAP-regulated	804:816	arg1	OGT					795:797	OGT	795:797	OGT	795:797	We also identified OGT as a YAP-regulated gene that forms a feedback loop.
29100056	8	9	theme	YAP-regulated	804:816	arg1	gene					818:821	a YAP-regulated gene	802:821	a YAP-regulated gene that forms a feedback loop	802:848	We also identified OGT as a YAP-regulated gene that forms a feedback loop.
29100056	4	10	theme	metabolic	440:448	arg1	nutrients					450:458	metabolic nutrients	440:458	metabolic nutrients	440:458	Here, we found that the Hippo pathway is directly regulated by the hexosamine biosynthesis pathway (HBP) in response to metabolic nutrients.
29100056	1	11	from	control	114:120	arg1	crucial					92:98	crucial	92:98	crucial	92:98	The Hippo pathway is crucial in organ size control and tissue homeostasis, with deregulation leading to cancer.
29100056	1	11	from	control	114:120	arg1	pathway					81:87	The Hippo pathway	71:87	The Hippo pathway	71:87	The Hippo pathway is crucial in organ size control and tissue homeostasis, with deregulation leading to cancer.
29100056	1	12	theme	Hippo	75:79	arg1	crucial					92:98	crucial	92:98	crucial	92:98	The Hippo pathway is crucial in organ size control and tissue homeostasis, with deregulation leading to cancer.
29100056	1	12	theme	Hippo	75:79	arg1	pathway					81:87	The Hippo pathway	71:87	The Hippo pathway	71:87	The Hippo pathway is crucial in organ size control and tissue homeostasis, with deregulation leading to cancer.
29100056	1	13	with	crucial	92:98	arg1	deregulation					151:162	deregulation	151:162	deregulation leading to cancer	151:180	The Hippo pathway is crucial in organ size control and tissue homeostasis, with deregulation leading to cancer.
29100056	10	14	theme	Hippo-YAP	1099:1107	arg1	pathway					1109:1115	the Hippo-YAP pathway	1095:1115	the Hippo-YAP pathway	1095:1115	Together, our data establish a molecular mechanism and functional significance of the HBP in directly linking extracellular glucose signal to the Hippo-YAP pathway and tumorigenesis.
29100056	6	15	theme	kinase	642:647	arg1	LATS1					649:653	upstream kinase LATS1	633:653	upstream kinase LATS1	633:653	YAP O-GlcNAcylation disrupts its interaction with upstream kinase LATS1, prevents its phosphorylation, and activates its transcriptional activity.
29100056	5	16	from	serine	571:576	arg1	transferase					550:560	O-GlcNAc transferase	541:560	O-GlcNAc transferase (OGT) at serine 109	541:580	Mechanistically, the core component of Hippo pathway (YAP) is O-GlcNAcylated by O-GlcNAc transferase (OGT) at serine 109.
29100056	5	16	from	serine	571:576	arg1	OGT					563:565	OGT	563:565	OGT	563:565	Mechanistically, the core component of Hippo pathway (YAP) is O-GlcNAcylated by O-GlcNAc transferase (OGT) at serine 109.
29100056	4	17	theme	Hippo	344:348	arg1	pathway					350:356	the Hippo pathway	340:356	the Hippo pathway	340:356	Here, we found that the Hippo pathway is directly regulated by the hexosamine biosynthesis pathway (HBP) in response to metabolic nutrients.
29100056	6	18	theme	upstream	633:640	arg1	LATS1					649:653	upstream kinase LATS1	633:653	upstream kinase LATS1	633:653	YAP O-GlcNAcylation disrupts its interaction with upstream kinase LATS1, prevents its phosphorylation, and activates its transcriptional activity.
29100056	0	19	theme	Hippo-YAP	18:26	arg1	Pathway					28:34	the Hippo-YAP Pathway	14:34	the Hippo-YAP Pathway	14:34	Regulation of the Hippo-YAP Pathway by Glucose Sensor O-GlcNAcylation.
29100056	10	20	theme	molecular	984:992	arg1	mechanism					994:1002	a molecular mechanism	982:1002	a molecular mechanism	982:1002	Together, our data establish a molecular mechanism and functional significance of the HBP in directly linking extracellular glucose signal to the Hippo-YAP pathway and tumorigenesis.
29100056	8	21	theme	feedback	836:843	arg1	loop					845:848	a feedback loop	834:848	a feedback loop	834:848	We also identified OGT as a YAP-regulated gene that forms a feedback loop.
29100056	0	22	theme	Pathway	28:34	arg1	Regulation					0:9	Regulation	0:9	Regulation of the Hippo-YAP Pathway by Glucose Sensor O-GlcNAcylation.	0:69	Regulation of the Hippo-YAP Pathway by Glucose Sensor O-GlcNAcylation.
29100056	5	23	theme	Hippo	500:504	arg1	pathway					506:512	Hippo pathway	500:512	Hippo pathway (YAP)	500:518	Mechanistically, the core component of Hippo pathway (YAP) is O-GlcNAcylated by O-GlcNAc transferase (OGT) at serine 109.
29100056	5	23	theme	Hippo	500:504	arg1	YAP					515:517	YAP	515:517	YAP	515:517	Mechanistically, the core component of Hippo pathway (YAP) is O-GlcNAcylated by O-GlcNAc transferase (OGT) at serine 109.
29100056	2	24	dep	such	218:221	arg1	as					223:224	as	223:224	as	223:224	An extracellular nutrition signal, such as glucose, regulates the Hippo pathway activation.
29100056	0	25	theme	Sensor	47:52	arg1	O-GlcNAcylation					54:68	Glucose Sensor O-GlcNAcylation	39:68	Glucose Sensor O-GlcNAcylation	39:68	Regulation of the Hippo-YAP Pathway by Glucose Sensor O-GlcNAcylation.
29100056	6	26	with	interaction	616:626	arg1	LATS1					649:653	upstream kinase LATS1	633:653	upstream kinase LATS1	633:653	YAP O-GlcNAcylation disrupts its interaction with upstream kinase LATS1, prevents its phosphorylation, and activates its transcriptional activity.
29100056	5	27	theme	pathway	506:512	arg1	component					487:495	the core component	478:495	the core component of Hippo pathway (YAP)	478:518	Mechanistically, the core component of Hippo pathway (YAP) is O-GlcNAcylated by O-GlcNAc transferase (OGT) at serine 109.
29100056	5	27	theme	pathway	506:512	arg1	O-GlcNAcylated					523:536	O-GlcNAcylated	523:536	O-GlcNAcylated	523:536	Mechanistically, the core component of Hippo pathway (YAP) is O-GlcNAcylated by O-GlcNAc transferase (OGT) at serine 109.
29100056	1	28	theme	organ	103:107	arg1	control					114:120	organ size control	103:120	organ size control	103:120	The Hippo pathway is crucial in organ size control and tissue homeostasis, with deregulation leading to cancer.
29100056	0	29	theme	Glucose	39:45	arg1	O-GlcNAcylation					54:68	Glucose Sensor O-GlcNAcylation	39:68	Glucose Sensor O-GlcNAcylation	39:68	Regulation of the Hippo-YAP Pathway by Glucose Sensor O-GlcNAcylation.
29100056	2	30	theme	nutrition	200:208	arg1	signal					210:215	An extracellular nutrition signal	183:215	An extracellular nutrition signal	183:215	An extracellular nutrition signal, such as glucose, regulates the Hippo pathway activation.
29100056	10	31	theme	functional	1008:1017	arg1	significance					1019:1030	functional significance	1008:1030	functional significance	1008:1030	Together, our data establish a molecular mechanism and functional significance of the HBP in directly linking extracellular glucose signal to the Hippo-YAP pathway and tumorigenesis.
29100056	1	32	theme	size	109:112	arg1	control					114:120	organ size control	103:120	organ size control	103:120	The Hippo pathway is crucial in organ size control and tissue homeostasis, with deregulation leading to cancer.
29100056	1	33	from	crucial	92:98	arg1	control					114:120	organ size control	103:120	organ size control	103:120	The Hippo pathway is crucial in organ size control and tissue homeostasis, with deregulation leading to cancer.
29100056	1	33	from	crucial	92:98	arg1	homeostasis					133:143	tissue homeostasis	126:143	tissue homeostasis	126:143	The Hippo pathway is crucial in organ size control and tissue homeostasis, with deregulation leading to cancer.
29100056	2	34	theme	extracellular	186:198	arg1	signal					210:215	An extracellular nutrition signal	183:215	An extracellular nutrition signal	183:215	An extracellular nutrition signal, such as glucose, regulates the Hippo pathway activation.
29100056	2	35	theme	Hippo	249:253	arg1	activation					263:272	the Hippo pathway activation	245:272	the Hippo pathway activation	245:272	An extracellular nutrition signal, such as glucose, regulates the Hippo pathway activation.
29100056	4	36	theme	biosynthesis	398:409	arg1	HBP					420:422	HBP	420:422	HBP	420:422	Here, we found that the Hippo pathway is directly regulated by the hexosamine biosynthesis pathway (HBP) in response to metabolic nutrients.
29100056	4	36	theme	biosynthesis	398:409	arg1	pathway					411:417	the hexosamine biosynthesis pathway	383:417	the hexosamine biosynthesis pathway (HBP)	383:423	Here, we found that the Hippo pathway is directly regulated by the hexosamine biosynthesis pathway (HBP) in response to metabolic nutrients.
29100056	6	37	theme	YAP	583:585	arg1	O-GlcNAcylation					587:601	YAP O-GlcNAcylation	583:601	YAP O-GlcNAcylation	583:601	YAP O-GlcNAcylation disrupts its interaction with upstream kinase LATS1, prevents its phosphorylation, and activates its transcriptional activity.
29100056	4	38	theme	hexosamine	387:396	arg1	HBP					420:422	HBP	420:422	HBP	420:422	Here, we found that the Hippo pathway is directly regulated by the hexosamine biosynthesis pathway (HBP) in response to metabolic nutrients.
29100056	4	38	theme	hexosamine	387:396	arg1	pathway					411:417	the hexosamine biosynthesis pathway	383:417	the hexosamine biosynthesis pathway (HBP)	383:423	Here, we found that the Hippo pathway is directly regulated by the hexosamine biosynthesis pathway (HBP) in response to metabolic nutrients.
29100056	5	39	theme	core	482:485	arg1	component					487:495	the core component	478:495	the core component of Hippo pathway (YAP)	478:518	Mechanistically, the core component of Hippo pathway (YAP) is O-GlcNAcylated by O-GlcNAc transferase (OGT) at serine 109.
29100056	5	39	theme	core	482:485	arg1	O-GlcNAcylated					523:536	O-GlcNAcylated	523:536	O-GlcNAcylated	523:536	Mechanistically, the core component of Hippo pathway (YAP) is O-GlcNAcylated by O-GlcNAc transferase (OGT) at serine 109.
29100056	1	40	theme	tissue	126:131	arg1	homeostasis					133:143	tissue homeostasis	126:143	tissue homeostasis	126:143	The Hippo pathway is crucial in organ size control and tissue homeostasis, with deregulation leading to cancer.
24077098	5	0	theme	O-GlcNAc	707:714	arg1	modification					716:727	O-GlcNAc modification	707:727	O-GlcNAc modification of CaMKII at Ser 279	707:748	O-GlcNAc modification of CaMKII at Ser 279 activates CaMKII autonomously, creating molecular memory even after Ca(2+) concentration declines.
24077098	5	1	from	Ser 279	742:748	arg1	modification					716:727	O-GlcNAc modification	707:727	O-GlcNAc modification of CaMKII at Ser 279	707:748	O-GlcNAc modification of CaMKII at Ser 279 activates CaMKII autonomously, creating molecular memory even after Ca(2+) concentration declines.
24077098	7	2	theme	events	1094:1099	arg1	activation					1030:1039	CaMKII-dependent activation	1013:1039	CaMKII-dependent activation of spontaneous sarcoplasmic reticulum Ca(2+) release events that can contribute to cardiac mechanical dysfunction and arrhythmias	1013:1169	In cardiomyocytes, increased glucose concentration significantly enhances CaMKII-dependent activation of spontaneous sarcoplasmic reticulum Ca(2+) release events that can contribute to cardiac mechanical dysfunction and arrhythmias.
24077098	4	3	theme	covalent	631:638	arg1	modification					640:651	covalent modification	631:651	covalent modification of CaMKII by O-linked N-acetylglucosamine (O-GlcNAc)	631:704	Acute hyperglycaemia causes covalent modification of CaMKII by O-linked N-acetylglucosamine (O-GlcNAc).
24077098	11	4	theme	signalling	1550:1559	arg1	event					1561:1565	a novel signalling event	1542:1565	a novel signalling event in pathways that may contribute critically to cardiac and neuronal pathophysiology in diabetes and other diseases	1542:1679	Thus, O-GlcNAc modification of CaMKII is a novel signalling event in pathways that may contribute critically to cardiac and neuronal pathophysiology in diabetes and other diseases.
24077098	11	4	theme	signalling	1550:1559	arg1	modification					1516:1527	O-GlcNAc modification	1507:1527	O-GlcNAc modification of CaMKII	1507:1537	Thus, O-GlcNAc modification of CaMKII is a novel signalling event in pathways that may contribute critically to cardiac and neuronal pathophysiology in diabetes and other diseases.
24077098	1	5	theme	chronic	220:226	arg1	activation					228:237	its chronic activation	216:237	its chronic activation	216:237	Ca(2+)/calmodulin-dependent protein kinase II (CaMKII) is an enzyme with important regulatory functions in the heart and brain, and its chronic activation can be pathological.
24077098	11	6	from	event	1561:1565	arg1	pathways					1570:1577	pathways	1570:1577	pathways that may contribute critically to cardiac and neuronal pathophysiology in diabetes and other diseases	1570:1679	Thus, O-GlcNAc modification of CaMKII is a novel signalling event in pathways that may contribute critically to cardiac and neuronal pathophysiology in diabetes and other diseases.
24077098	9	7	theme	intact	1289:1294	arg1	hearts					1305:1310	intact perfused hearts	1289:1310	intact perfused hearts	1289:1310	In intact perfused hearts, arrhythmias were aggravated by increased glucose concentration through O-GlcNAc- and CaMKII-dependent pathways.
24077098	1	8	with	enzyme	145:150	arg1	functions					178:186	important regulatory functions	157:186	important regulatory functions in the heart and brain	157:209	Ca(2+)/calmodulin-dependent protein kinase II (CaMKII) is an enzyme with important regulatory functions in the heart and brain, and its chronic activation can be pathological.
24077098	6	9	dep	heart	894:898	arg1	the					890:892	the	890:892	the	890:892	O-GlcNAc-modified CaMKII is increased in the heart and brain of diabetic humans and rats.
24077098	4	10	link	O-linked	666:673	arg1	O-GlcNAc					696:703	O-GlcNAc	696:703	O-GlcNAc	696:703	Acute hyperglycaemia causes covalent modification of CaMKII by O-linked N-acetylglucosamine (O-GlcNAc).
24077098	4	10	link	O-linked	666:673	arg1	N-acetylglucosamine					675:693	O-linked N-acetylglucosamine	666:693	O-linked N-acetylglucosamine (O-GlcNAc)	666:704	Acute hyperglycaemia causes covalent modification of CaMKII by O-linked N-acetylglucosamine (O-GlcNAc).
24077098	10	11	theme	O-GlcNAc	1464:1471	arg1	blockade					1452:1459	acute blockade	1446:1459	acute blockade of O-GlcNAc	1446:1471	In diabetic animals, acute blockade of O-GlcNAc inhibited arrhythmogenesis.
24077098	6	12	theme	O-GlcNAc-modified	849:865	arg1	CaMKII					867:872	O-GlcNAc-modified CaMKII	849:872	O-GlcNAc-modified CaMKII	849:872	O-GlcNAc-modified CaMKII is increased in the heart and brain of diabetic humans and rats.
24077098	6	13	theme	rats	933:936	arg1	heart					894:898	heart	894:898	heart	894:898	O-GlcNAc-modified CaMKII is increased in the heart and brain of diabetic humans and rats.
24077098	6	13	theme	rats	933:936	arg1	brain					904:908	brain	904:908	brain	904:908	O-GlcNAc-modified CaMKII is increased in the heart and brain of diabetic humans and rats.
24077098	1	14	theme	2+	87:88	arg1	kinase					120:125	Ca(2+)/calmodulin-dependent protein kinase II	84:128	Ca(2+)/calmodulin-dependent protein kinase II (CaMKII)	84:137	Ca(2+)/calmodulin-dependent protein kinase II (CaMKII) is an enzyme with important regulatory functions in the heart and brain, and its chronic activation can be pathological.
24077098	1	14	theme	2+	87:88	arg1	CaMKII					131:136	CaMKII	131:136	CaMKII	131:136	Ca(2+)/calmodulin-dependent protein kinase II (CaMKII) is an enzyme with important regulatory functions in the heart and brain, and its chronic activation can be pathological.
24077098	1	14	theme	2+	87:88	arg1	enzyme					145:150	an enzyme	142:150	an enzyme with important regulatory functions in the heart and brain	142:209	Ca(2+)/calmodulin-dependent protein kinase II (CaMKII) is an enzyme with important regulatory functions in the heart and brain, and its chronic activation can be pathological.
24077098	7	15	theme	release	1086:1092	arg1	events					1094:1099	spontaneous sarcoplasmic reticulum Ca(2+) release events	1044:1099	spontaneous sarcoplasmic reticulum Ca(2+) release events that can contribute to cardiac mechanical dysfunction and arrhythmias	1044:1169	In cardiomyocytes, increased glucose concentration significantly enhances CaMKII-dependent activation of spontaneous sarcoplasmic reticulum Ca(2+) release events that can contribute to cardiac mechanical dysfunction and arrhythmias.
24077098	2	16	theme	CaMKII	260:265	arg1	activation					267:276	CaMKII activation	260:276	CaMKII activation	260:276	CaMKII activation is seen in heart failure, and can directly induce pathological changes in ion channels, Ca(2+) handling and gene transcription.
24077098	11	17	from	pathophysiology	1634:1648	arg1	diabetes					1653:1660	diabetes	1653:1660	diabetes	1653:1660	Thus, O-GlcNAc modification of CaMKII is a novel signalling event in pathways that may contribute critically to cardiac and neuronal pathophysiology in diabetes and other diseases.
24077098	11	17	from	pathophysiology	1634:1648	arg1	diseases					1672:1679	other diseases	1666:1679	other diseases	1666:1679	Thus, O-GlcNAc modification of CaMKII is a novel signalling event in pathways that may contribute critically to cardiac and neuronal pathophysiology in diabetes and other diseases.
24077098	5	18	theme	molecular	790:798	arg1	memory					800:805	molecular memory	790:805	molecular memory	790:805	O-GlcNAc modification of CaMKII at Ser 279 activates CaMKII autonomously, creating molecular memory even after Ca(2+) concentration declines.
24077098	5	19	theme	Ca	818:819	arg1	concentration					825:837	Ca(2+) concentration	818:837	Ca(2+) concentration	818:837	O-GlcNAc modification of CaMKII at Ser 279 activates CaMKII autonomously, creating molecular memory even after Ca(2+) concentration declines.
24077098	1	20	theme	Ca	84:85	arg1	kinase					120:125	Ca(2+)/calmodulin-dependent protein kinase II	84:128	Ca(2+)/calmodulin-dependent protein kinase II (CaMKII)	84:137	Ca(2+)/calmodulin-dependent protein kinase II (CaMKII) is an enzyme with important regulatory functions in the heart and brain, and its chronic activation can be pathological.
24077098	1	20	theme	Ca	84:85	arg1	CaMKII					131:136	CaMKII	131:136	CaMKII	131:136	Ca(2+)/calmodulin-dependent protein kinase II (CaMKII) is an enzyme with important regulatory functions in the heart and brain, and its chronic activation can be pathological.
24077098	1	20	theme	Ca	84:85	arg1	enzyme					145:150	an enzyme	142:150	an enzyme with important regulatory functions in the heart and brain	142:209	Ca(2+)/calmodulin-dependent protein kinase II (CaMKII) is an enzyme with important regulatory functions in the heart and brain, and its chronic activation can be pathological.
24077098	1	21	theme	regulatory	167:176	arg1	functions					178:186	important regulatory functions	157:186	important regulatory functions in the heart and brain	157:209	Ca(2+)/calmodulin-dependent protein kinase II (CaMKII) is an enzyme with important regulatory functions in the heart and brain, and its chronic activation can be pathological.
24077098	8	22	theme	O-GlcNAc	1234:1241	arg1	signalling					1243:1252	O-GlcNAc signalling	1234:1252	O-GlcNAc signalling	1234:1252	These effects were prevented by pharmacological inhibition of O-GlcNAc signalling or genetic ablation of CaMKIIδ.
24077098	9	23	theme	perfused	1296:1303	arg1	hearts					1305:1310	intact perfused hearts	1289:1310	intact perfused hearts	1289:1310	In intact perfused hearts, arrhythmias were aggravated by increased glucose concentration through O-GlcNAc- and CaMKII-dependent pathways.
24077098	0	24	link	O-linked	60:67	arg1	glycosylation					69:81	O-linked glycosylation	60:81	O-linked glycosylation	60:81	Diabetic hyperglycaemia activates CaMKII and arrhythmias by O-linked glycosylation.
24077098	0	25	theme	Diabetic	0:7	arg1	hyperglycaemia					9:22	Diabetic hyperglycaemia	0:22	Diabetic hyperglycaemia	0:22	Diabetic hyperglycaemia activates CaMKII and arrhythmias by O-linked glycosylation.
24077098	1	26	theme	important	157:165	arg1	functions					178:186	important regulatory functions	157:186	important regulatory functions in the heart and brain	157:209	Ca(2+)/calmodulin-dependent protein kinase II (CaMKII) is an enzyme with important regulatory functions in the heart and brain, and its chronic activation can be pathological.
24077098	7	27	theme	reticulum	1069:1077	arg1	2+					1082:1083	2+	1082:1083	2+	1082:1083	In cardiomyocytes, increased glucose concentration significantly enhances CaMKII-dependent activation of spontaneous sarcoplasmic reticulum Ca(2+) release events that can contribute to cardiac mechanical dysfunction and arrhythmias.
24077098	7	27	theme	reticulum	1069:1077	arg1	Ca					1079:1080	sarcoplasmic reticulum Ca	1056:1080	spontaneous sarcoplasmic reticulum Ca(2+) release events that can contribute to cardiac mechanical dysfunction and arrhythmias	1044:1169	In cardiomyocytes, increased glucose concentration significantly enhances CaMKII-dependent activation of spontaneous sarcoplasmic reticulum Ca(2+) release events that can contribute to cardiac mechanical dysfunction and arrhythmias.
24077098	2	28	theme	heart	289:293	arg1	failure					295:301	heart failure	289:301	heart failure	289:301	CaMKII activation is seen in heart failure, and can directly induce pathological changes in ion channels, Ca(2+) handling and gene transcription.
24077098	2	29	theme	ion	352:354	arg1	channels					356:363	ion channels	352:363	ion channels	352:363	CaMKII activation is seen in heart failure, and can directly induce pathological changes in ion channels, Ca(2+) handling and gene transcription.
24077098	2	30	theme	gene	386:389	arg1	transcription					391:403	gene transcription	386:403	gene transcription	386:403	CaMKII activation is seen in heart failure, and can directly induce pathological changes in ion channels, Ca(2+) handling and gene transcription.
24077098	2	30	theme	gene	386:389	arg1	changes					341:347	pathological changes	328:347	pathological changes in ion channels	328:363	CaMKII activation is seen in heart failure, and can directly induce pathological changes in ion channels, Ca(2+) handling and gene transcription.
24077098	6	31	theme	humans	922:927	arg1	heart					894:898	heart	894:898	heart	894:898	O-GlcNAc-modified CaMKII is increased in the heart and brain of diabetic humans and rats.
24077098	6	31	theme	humans	922:927	arg1	brain					904:908	brain	904:908	brain	904:908	O-GlcNAc-modified CaMKII is increased in the heart and brain of diabetic humans and rats.
24077098	7	32	theme	Ca	1079:1080	arg1	events					1094:1099	spontaneous sarcoplasmic reticulum Ca(2+) release events	1044:1099	spontaneous sarcoplasmic reticulum Ca(2+) release events that can contribute to cardiac mechanical dysfunction and arrhythmias	1044:1169	In cardiomyocytes, increased glucose concentration significantly enhances CaMKII-dependent activation of spontaneous sarcoplasmic reticulum Ca(2+) release events that can contribute to cardiac mechanical dysfunction and arrhythmias.
24077098	2	33	from	changes	341:347	arg1	channels					356:363	ion channels	352:363	ion channels	352:363	CaMKII activation is seen in heart failure, and can directly induce pathological changes in ion channels, Ca(2+) handling and gene transcription.
24077098	4	34	theme	O-linked	666:673	arg1	O-GlcNAc					696:703	O-GlcNAc	696:703	O-GlcNAc	696:703	Acute hyperglycaemia causes covalent modification of CaMKII by O-linked N-acetylglucosamine (O-GlcNAc).
24077098	4	34	theme	O-linked	666:673	arg1	N-acetylglucosamine					675:693	O-linked N-acetylglucosamine	666:693	O-linked N-acetylglucosamine (O-GlcNAc)	666:704	Acute hyperglycaemia causes covalent modification of CaMKII by O-linked N-acetylglucosamine (O-GlcNAc).
24077098	8	35	theme	genetic	1257:1263	arg1	ablation					1265:1272	genetic ablation	1257:1272	genetic ablation of CaMKIIδ	1257:1283	These effects were prevented by pharmacological inhibition of O-GlcNAc signalling or genetic ablation of CaMKIIδ.
24077098	8	36	theme	signalling	1243:1252	arg1	ablation					1265:1272	genetic ablation	1257:1272	genetic ablation of CaMKIIδ	1257:1283	These effects were prevented by pharmacological inhibition of O-GlcNAc signalling or genetic ablation of CaMKIIδ.
24077098	8	36	theme	signalling	1243:1252	arg1	inhibition					1220:1229	pharmacological inhibition	1204:1229	pharmacological inhibition of O-GlcNAc signalling	1204:1252	These effects were prevented by pharmacological inhibition of O-GlcNAc signalling or genetic ablation of CaMKIIδ.
24077098	7	37	theme	mechanical	1132:1141	arg1	dysfunction					1143:1153	cardiac mechanical dysfunction	1124:1153	cardiac mechanical dysfunction	1124:1153	In cardiomyocytes, increased glucose concentration significantly enhances CaMKII-dependent activation of spontaneous sarcoplasmic reticulum Ca(2+) release events that can contribute to cardiac mechanical dysfunction and arrhythmias.
24077098	5	38	theme	CaMKII	760:765	arg1	autonomously					767:778	CaMKII autonomously	760:778	CaMKII autonomously	760:778	O-GlcNAc modification of CaMKII at Ser 279 activates CaMKII autonomously, creating molecular memory even after Ca(2+) concentration declines.
24077098	7	39	theme	spontaneous	1044:1054	arg1	events					1094:1099	spontaneous sarcoplasmic reticulum Ca(2+) release events	1044:1099	spontaneous sarcoplasmic reticulum Ca(2+) release events that can contribute to cardiac mechanical dysfunction and arrhythmias	1044:1169	In cardiomyocytes, increased glucose concentration significantly enhances CaMKII-dependent activation of spontaneous sarcoplasmic reticulum Ca(2+) release events that can contribute to cardiac mechanical dysfunction and arrhythmias.
24077098	10	40	theme	diabetic	1428:1435	arg1	animals					1437:1443	diabetic animals	1428:1443	diabetic animals	1428:1443	In diabetic animals, acute blockade of O-GlcNAc inhibited arrhythmogenesis.
24077098	1	41	theme	/calmodulin-dependent	90:110	arg1	kinase					120:125	Ca(2+)/calmodulin-dependent protein kinase II	84:128	Ca(2+)/calmodulin-dependent protein kinase II (CaMKII)	84:137	Ca(2+)/calmodulin-dependent protein kinase II (CaMKII) is an enzyme with important regulatory functions in the heart and brain, and its chronic activation can be pathological.
24077098	1	41	theme	/calmodulin-dependent	90:110	arg1	CaMKII					131:136	CaMKII	131:136	CaMKII	131:136	Ca(2+)/calmodulin-dependent protein kinase II (CaMKII) is an enzyme with important regulatory functions in the heart and brain, and its chronic activation can be pathological.
24077098	1	41	theme	/calmodulin-dependent	90:110	arg1	enzyme					145:150	an enzyme	142:150	an enzyme with important regulatory functions in the heart and brain	142:209	Ca(2+)/calmodulin-dependent protein kinase II (CaMKII) is an enzyme with important regulatory functions in the heart and brain, and its chronic activation can be pathological.
24077098	11	42	theme	other	1666:1670	arg1	diseases					1672:1679	other diseases	1666:1679	other diseases	1666:1679	Thus, O-GlcNAc modification of CaMKII is a novel signalling event in pathways that may contribute critically to cardiac and neuronal pathophysiology in diabetes and other diseases.
24077098	9	43	theme	increased	1344:1352	arg1	concentration					1362:1374	increased glucose concentration	1344:1374	increased glucose concentration	1344:1374	In intact perfused hearts, arrhythmias were aggravated by increased glucose concentration through O-GlcNAc- and CaMKII-dependent pathways.
24077098	7	44	theme	sarcoplasmic	1056:1067	arg1	reticulum					1069:1077	sarcoplasmic reticulum	1056:1077	spontaneous sarcoplasmic reticulum Ca(2+) release events that can contribute to cardiac mechanical dysfunction and arrhythmias	1044:1169	In cardiomyocytes, increased glucose concentration significantly enhances CaMKII-dependent activation of spontaneous sarcoplasmic reticulum Ca(2+) release events that can contribute to cardiac mechanical dysfunction and arrhythmias.
24077098	11	45	theme	neuronal	1625:1632	arg1	pathophysiology					1634:1648	cardiac and neuronal pathophysiology	1613:1648	pathophysiology	1634:1648	Thus, O-GlcNAc modification of CaMKII is a novel signalling event in pathways that may contribute critically to cardiac and neuronal pathophysiology in diabetes and other diseases.
24077098	1	46	theme	protein	112:118	arg1	kinase					120:125	Ca(2+)/calmodulin-dependent protein kinase II	84:128	Ca(2+)/calmodulin-dependent protein kinase II (CaMKII)	84:137	Ca(2+)/calmodulin-dependent protein kinase II (CaMKII) is an enzyme with important regulatory functions in the heart and brain, and its chronic activation can be pathological.
24077098	1	46	theme	protein	112:118	arg1	CaMKII					131:136	CaMKII	131:136	CaMKII	131:136	Ca(2+)/calmodulin-dependent protein kinase II (CaMKII) is an enzyme with important regulatory functions in the heart and brain, and its chronic activation can be pathological.
24077098	1	46	theme	protein	112:118	arg1	enzyme					145:150	an enzyme	142:150	an enzyme with important regulatory functions in the heart and brain	142:209	Ca(2+)/calmodulin-dependent protein kinase II (CaMKII) is an enzyme with important regulatory functions in the heart and brain, and its chronic activation can be pathological.
24077098	2	47	theme	2+	369:370	arg1	handling					373:380	Ca(2+) handling	366:380	Ca(2+) handling	366:380	CaMKII activation is seen in heart failure, and can directly induce pathological changes in ion channels, Ca(2+) handling and gene transcription.
24077098	2	47	theme	2+	369:370	arg1	changes					341:347	pathological changes	328:347	pathological changes in ion channels	328:363	CaMKII activation is seen in heart failure, and can directly induce pathological changes in ion channels, Ca(2+) handling and gene transcription.
24077098	9	48	theme	glucose	1354:1360	arg1	concentration					1362:1374	increased glucose concentration	1344:1374	increased glucose concentration	1344:1374	In intact perfused hearts, arrhythmias were aggravated by increased glucose concentration through O-GlcNAc- and CaMKII-dependent pathways.
24077098	8	49	theme	CaMKIIδ	1277:1283	arg1	ablation					1265:1272	genetic ablation	1257:1272	genetic ablation of CaMKIIδ	1257:1283	These effects were prevented by pharmacological inhibition of O-GlcNAc signalling or genetic ablation of CaMKIIδ.
24077098	8	49	theme	CaMKIIδ	1277:1283	arg1	inhibition					1220:1229	pharmacological inhibition	1204:1229	pharmacological inhibition of O-GlcNAc signalling	1204:1252	These effects were prevented by pharmacological inhibition of O-GlcNAc signalling or genetic ablation of CaMKIIδ.
24077098	5	50	theme	CaMKII	732:737	arg1	modification					716:727	O-GlcNAc modification	707:727	O-GlcNAc modification of CaMKII at Ser 279	707:748	O-GlcNAc modification of CaMKII at Ser 279 activates CaMKII autonomously, creating molecular memory even after Ca(2+) concentration declines.
24077098	7	51	theme	cardiac	1124:1130	arg1	dysfunction					1143:1153	cardiac mechanical dysfunction	1124:1153	cardiac mechanical dysfunction	1124:1153	In cardiomyocytes, increased glucose concentration significantly enhances CaMKII-dependent activation of spontaneous sarcoplasmic reticulum Ca(2+) release events that can contribute to cardiac mechanical dysfunction and arrhythmias.
24077098	3	52	theme	risk	549:552	arg1	mechanism					457:465	a novel mechanism	449:465	a novel mechanism	449:465	Here, in human, rat and mouse, we identify a novel mechanism linking CaMKII and hyperglycaemic signalling in diabetes mellitus, which is a key risk factor for heart and neurodegenerative diseases.
24077098	3	52	theme	risk	549:552	arg1	factor					554:559	a key risk factor	543:559	a key risk factor for heart and neurodegenerative diseases	543:600	Here, in human, rat and mouse, we identify a novel mechanism linking CaMKII and hyperglycaemic signalling in diabetes mellitus, which is a key risk factor for heart and neurodegenerative diseases.
24077098	7	53	theme	increased	958:966	arg1	concentration					976:988	increased glucose concentration	958:988	increased glucose concentration	958:988	In cardiomyocytes, increased glucose concentration significantly enhances CaMKII-dependent activation of spontaneous sarcoplasmic reticulum Ca(2+) release events that can contribute to cardiac mechanical dysfunction and arrhythmias.
24077098	2	54	theme	Ca	366:367	arg1	handling					373:380	Ca(2+) handling	366:380	Ca(2+) handling	366:380	CaMKII activation is seen in heart failure, and can directly induce pathological changes in ion channels, Ca(2+) handling and gene transcription.
24077098	2	54	theme	Ca	366:367	arg1	changes					341:347	pathological changes	328:347	pathological changes in ion channels	328:363	CaMKII activation is seen in heart failure, and can directly induce pathological changes in ion channels, Ca(2+) handling and gene transcription.
24077098	0	55	theme	O-linked	60:67	arg1	glycosylation					69:81	O-linked glycosylation	60:81	O-linked glycosylation	60:81	Diabetic hyperglycaemia activates CaMKII and arrhythmias by O-linked glycosylation.
24077098	6	56	theme	diabetic	913:920	arg1	humans					922:927	diabetic humans	913:927	diabetic humans	913:927	O-GlcNAc-modified CaMKII is increased in the heart and brain of diabetic humans and rats.
24077098	7	57	theme	glucose	968:974	arg1	concentration					976:988	increased glucose concentration	958:988	increased glucose concentration	958:988	In cardiomyocytes, increased glucose concentration significantly enhances CaMKII-dependent activation of spontaneous sarcoplasmic reticulum Ca(2+) release events that can contribute to cardiac mechanical dysfunction and arrhythmias.
24077098	8	58	theme	pharmacological	1204:1218	arg1	inhibition					1220:1229	pharmacological inhibition	1204:1229	pharmacological inhibition of O-GlcNAc signalling	1204:1252	These effects were prevented by pharmacological inhibition of O-GlcNAc signalling or genetic ablation of CaMKIIδ.
24077098	9	59	theme	O-GlcNAc-	1384:1392	arg1	pathways					1415:1422	O-GlcNAc- and CaMKII-dependent pathways	1384:1422	O-GlcNAc- and CaMKII-dependent pathways	1384:1422	In intact perfused hearts, arrhythmias were aggravated by increased glucose concentration through O-GlcNAc- and CaMKII-dependent pathways.
24077098	7	60	theme	CaMKII-dependent	1013:1028	arg1	activation					1030:1039	CaMKII-dependent activation	1013:1039	CaMKII-dependent activation of spontaneous sarcoplasmic reticulum Ca(2+) release events that can contribute to cardiac mechanical dysfunction and arrhythmias	1013:1169	In cardiomyocytes, increased glucose concentration significantly enhances CaMKII-dependent activation of spontaneous sarcoplasmic reticulum Ca(2+) release events that can contribute to cardiac mechanical dysfunction and arrhythmias.
24077098	3	61	theme	diabetes	515:522	arg1	mellitus					524:531	diabetes mellitus	515:531	diabetes mellitus	515:531	Here, in human, rat and mouse, we identify a novel mechanism linking CaMKII and hyperglycaemic signalling in diabetes mellitus, which is a key risk factor for heart and neurodegenerative diseases.
24077098	11	62	theme	cardiac	1613:1619	arg1	pathophysiology					1634:1648	cardiac and neuronal pathophysiology	1613:1648	pathophysiology	1634:1648	Thus, O-GlcNAc modification of CaMKII is a novel signalling event in pathways that may contribute critically to cardiac and neuronal pathophysiology in diabetes and other diseases.
24077098	3	63	from	CaMKII	475:480	arg1	mellitus					524:531	diabetes mellitus	515:531	diabetes mellitus	515:531	Here, in human, rat and mouse, we identify a novel mechanism linking CaMKII and hyperglycaemic signalling in diabetes mellitus, which is a key risk factor for heart and neurodegenerative diseases.
24077098	3	64	theme	hyperglycaemic	486:499	arg1	signalling					501:510	hyperglycaemic signalling	486:510	hyperglycaemic signalling	486:510	Here, in human, rat and mouse, we identify a novel mechanism linking CaMKII and hyperglycaemic signalling in diabetes mellitus, which is a key risk factor for heart and neurodegenerative diseases.
24077098	10	65	theme	acute	1446:1450	arg1	blockade					1452:1459	acute blockade	1446:1459	acute blockade of O-GlcNAc	1446:1471	In diabetic animals, acute blockade of O-GlcNAc inhibited arrhythmogenesis.
24077098	4	66	theme	Acute	603:607	arg1	hyperglycaemia					609:622	Acute hyperglycaemia	603:622	Acute hyperglycaemia	603:622	Acute hyperglycaemia causes covalent modification of CaMKII by O-linked N-acetylglucosamine (O-GlcNAc).
24077098	11	67	theme	CaMKII	1532:1537	arg1	event					1561:1565	a novel signalling event	1542:1565	a novel signalling event in pathways that may contribute critically to cardiac and neuronal pathophysiology in diabetes and other diseases	1542:1679	Thus, O-GlcNAc modification of CaMKII is a novel signalling event in pathways that may contribute critically to cardiac and neuronal pathophysiology in diabetes and other diseases.
24077098	11	67	theme	CaMKII	1532:1537	arg1	modification					1516:1527	O-GlcNAc modification	1507:1527	O-GlcNAc modification of CaMKII	1507:1537	Thus, O-GlcNAc modification of CaMKII is a novel signalling event in pathways that may contribute critically to cardiac and neuronal pathophysiology in diabetes and other diseases.
24077098	9	68	theme	CaMKII-dependent	1398:1413	arg1	pathways					1415:1422	O-GlcNAc- and CaMKII-dependent pathways	1384:1422	O-GlcNAc- and CaMKII-dependent pathways	1384:1422	In intact perfused hearts, arrhythmias were aggravated by increased glucose concentration through O-GlcNAc- and CaMKII-dependent pathways.
24077098	3	69	theme	novel	451:455	arg1	mechanism					457:465	a novel mechanism	449:465	a novel mechanism	449:465	Here, in human, rat and mouse, we identify a novel mechanism linking CaMKII and hyperglycaemic signalling in diabetes mellitus, which is a key risk factor for heart and neurodegenerative diseases.
24077098	3	69	theme	novel	451:455	arg1	factor					554:559	a key risk factor	543:559	a key risk factor for heart and neurodegenerative diseases	543:600	Here, in human, rat and mouse, we identify a novel mechanism linking CaMKII and hyperglycaemic signalling in diabetes mellitus, which is a key risk factor for heart and neurodegenerative diseases.
24077098	3	70	theme	key	545:547	arg1	mechanism					457:465	a novel mechanism	449:465	a novel mechanism	449:465	Here, in human, rat and mouse, we identify a novel mechanism linking CaMKII and hyperglycaemic signalling in diabetes mellitus, which is a key risk factor for heart and neurodegenerative diseases.
24077098	3	70	theme	key	545:547	arg1	factor					554:559	a key risk factor	543:559	a key risk factor for heart and neurodegenerative diseases	543:600	Here, in human, rat and mouse, we identify a novel mechanism linking CaMKII and hyperglycaemic signalling in diabetes mellitus, which is a key risk factor for heart and neurodegenerative diseases.
24077098	4	71	theme	CaMKII	656:661	arg1	modification					640:651	covalent modification	631:651	covalent modification of CaMKII by O-linked N-acetylglucosamine (O-GlcNAc)	631:704	Acute hyperglycaemia causes covalent modification of CaMKII by O-linked N-acetylglucosamine (O-GlcNAc).
24077098	11	72	theme	O-GlcNAc	1507:1514	arg1	event					1561:1565	a novel signalling event	1542:1565	a novel signalling event in pathways that may contribute critically to cardiac and neuronal pathophysiology in diabetes and other diseases	1542:1679	Thus, O-GlcNAc modification of CaMKII is a novel signalling event in pathways that may contribute critically to cardiac and neuronal pathophysiology in diabetes and other diseases.
24077098	11	72	theme	O-GlcNAc	1507:1514	arg1	modification					1516:1527	O-GlcNAc modification	1507:1527	O-GlcNAc modification of CaMKII	1507:1537	Thus, O-GlcNAc modification of CaMKII is a novel signalling event in pathways that may contribute critically to cardiac and neuronal pathophysiology in diabetes and other diseases.
24077098	3	73	theme	neurodegenerative	575:591	arg1	diseases					593:600	neurodegenerative diseases	575:600	neurodegenerative diseases	575:600	Here, in human, rat and mouse, we identify a novel mechanism linking CaMKII and hyperglycaemic signalling in diabetes mellitus, which is a key risk factor for heart and neurodegenerative diseases.
24077098	5	74	dep	creating	781:788	arg1	declines					839:846	declines	839:846	creating molecular memory even after Ca(2+) concentration declines	781:846	O-GlcNAc modification of CaMKII at Ser 279 activates CaMKII autonomously, creating molecular memory even after Ca(2+) concentration declines.
24077098	1	75	from	functions	178:186	arg1	brain					205:209	brain	205:209	brain	205:209	Ca(2+)/calmodulin-dependent protein kinase II (CaMKII) is an enzyme with important regulatory functions in the heart and brain, and its chronic activation can be pathological.
24077098	1	75	from	functions	178:186	arg1	heart					195:199	heart	195:199	heart	195:199	Ca(2+)/calmodulin-dependent protein kinase II (CaMKII) is an enzyme with important regulatory functions in the heart and brain, and its chronic activation can be pathological.
24077098	11	76	mod	modification	1516:1527	arg3	O-GlcNAc					1507:1514	O-GlcNAc modification	1507:1527	O-GlcNAc modification of CaMKII	1507:1537	Thus, O-GlcNAc modification of CaMKII is a novel signalling event in pathways that may contribute critically to cardiac and neuronal pathophysiology in diabetes and other diseases.
24077098	11	76	mod	modification	1516:1527	arg1	CaMKII					1532:1537	CaMKII	1532:1537	CaMKII	1532:1537	Thus, O-GlcNAc modification of CaMKII is a novel signalling event in pathways that may contribute critically to cardiac and neuronal pathophysiology in diabetes and other diseases.
24077098	3	77	from	signalling	501:510	arg1	mellitus					524:531	diabetes mellitus	515:531	diabetes mellitus	515:531	Here, in human, rat and mouse, we identify a novel mechanism linking CaMKII and hyperglycaemic signalling in diabetes mellitus, which is a key risk factor for heart and neurodegenerative diseases.
24077098	2	78	theme	pathological	328:339	arg1	handling					373:380	Ca(2+) handling	366:380	Ca(2+) handling	366:380	CaMKII activation is seen in heart failure, and can directly induce pathological changes in ion channels, Ca(2+) handling and gene transcription.
24077098	2	78	theme	pathological	328:339	arg1	transcription					391:403	gene transcription	386:403	gene transcription	386:403	CaMKII activation is seen in heart failure, and can directly induce pathological changes in ion channels, Ca(2+) handling and gene transcription.
24077098	2	78	theme	pathological	328:339	arg1	changes					341:347	pathological changes	328:347	pathological changes in ion channels	328:363	CaMKII activation is seen in heart failure, and can directly induce pathological changes in ion channels, Ca(2+) handling and gene transcription.
24077098	11	79	theme	novel	1544:1548	arg1	event					1561:1565	a novel signalling event	1542:1565	a novel signalling event in pathways that may contribute critically to cardiac and neuronal pathophysiology in diabetes and other diseases	1542:1679	Thus, O-GlcNAc modification of CaMKII is a novel signalling event in pathways that may contribute critically to cardiac and neuronal pathophysiology in diabetes and other diseases.
24077098	11	79	theme	novel	1544:1548	arg1	modification					1516:1527	O-GlcNAc modification	1507:1527	O-GlcNAc modification of CaMKII	1507:1537	Thus, O-GlcNAc modification of CaMKII is a novel signalling event in pathways that may contribute critically to cardiac and neuronal pathophysiology in diabetes and other diseases.
33926209	0	0	attach	Links	34:38	arg1	Proarrhythmia					66:78	Proarrhythmia	66:78	Proarrhythmia	66:78	CaMKII Serine 280 O-GlcNAcylation Links Diabetic Hyperglycemia to Proarrhythmia.
33926209	0	0	attach	Links	34:38	arg2	O-GlcNAcylation					18:32	CaMKII Serine 280 O-GlcNAcylation	0:32	CaMKII Serine 280 O-GlcNAcylation	0:32	CaMKII Serine 280 O-GlcNAcylation Links Diabetic Hyperglycemia to Proarrhythmia.
33926209	0	1	theme	Diabetic	40:47	arg1	Hyperglycemia					49:61	Diabetic Hyperglycemia	40:61	Diabetic Hyperglycemia	40:61	CaMKII Serine 280 O-GlcNAcylation Links Diabetic Hyperglycemia to Proarrhythmia.
33926209	0	2	theme	Serine	7:12	arg1	O-GlcNAcylation					18:32	CaMKII Serine 280 O-GlcNAcylation	0:32	CaMKII Serine 280 O-GlcNAcylation	0:32	CaMKII Serine 280 O-GlcNAcylation Links Diabetic Hyperglycemia to Proarrhythmia.
33926209	0	3	theme	CaMKII	0:5	arg1	O-GlcNAcylation					18:32	CaMKII Serine 280 O-GlcNAcylation	0:32	CaMKII Serine 280 O-GlcNAcylation	0:32	CaMKII Serine 280 O-GlcNAcylation Links Diabetic Hyperglycemia to Proarrhythmia.
33926209	1	4	dep	[Figure	81:87	arg1	see					90:92	see	90:92	see text	90:97	[Figure: see text].
33926209	0	5	theme	280	14:16	arg1	O-GlcNAcylation					18:32	CaMKII Serine 280 O-GlcNAcylation	0:32	CaMKII Serine 280 O-GlcNAcylation	0:32	CaMKII Serine 280 O-GlcNAcylation Links Diabetic Hyperglycemia to Proarrhythmia.
25187572	9	0	theme	OGA	1970:1972	arg1	inhibitor					1974:1982	the OGA inhibitor	1966:1982	the OGA inhibitor	1966:1982	Furthermore, BMP2/7-induced ALP activity was enhanced by 35.6% in bone marrow-derived mesenchymal stem cells differentiated in the presence of the OGA inhibitor, demonstrating that direct or BMP2/7-induced inhibition of OGA is associated with increased ALP activity.
25187572	3	1	theme	tandem	578:583	arg1	spectrometry					590:601	electron transfer dissociation tandem mass spectrometry	547:601	electron transfer dissociation tandem mass spectrometry	547:601	Characterization of Runx2 by electron transfer dissociation tandem mass spectrometry revealed sites of O-linked N-acetylglucosamine (O-GlcNAc) modification, a nutrient-responsive post-translational modification that modulates the action of numerous transcriptional effectors.
25187572	8	2	theme	Runx2	1779:1783	arg1	abundance					1751:1759	the abundance	1747:1759	the abundance of O-GlcNAcylated Runx2	1747:1783	Osteogenic differentiation of bone marrow-derived mesenchymal stem cells in the presence of BMP2/7 for 8 days culminated in decreased OGA activity (39.0%) and an increase in the abundance of O-GlcNAcylated Runx2, as compared with unstimulated cells.
25187572	7	3	theme	formation	1524:1532	arg1	target					1556:1561	a transcriptional target	1538:1561	a transcriptional target of Runx2	1538:1570	In bone marrow-derived mesenchymal stem cells differentiated for 6 days in osteogenic media, inhibition of OGA resulted in elevated expression (24.3%) and activity (65.8%) of alkaline phosphatase (ALP) an early marker of bone formation and a transcriptional target of Runx2.
25187572	7	3	theme	formation	1524:1532	arg1	marker					1509:1514	an early marker	1500:1514	an early marker of bone formation	1500:1532	In bone marrow-derived mesenchymal stem cells differentiated for 6 days in osteogenic media, inhibition of OGA resulted in elevated expression (24.3%) and activity (65.8%) of alkaline phosphatase (ALP) an early marker of bone formation and a transcriptional target of Runx2.
25187572	10	4	theme	early	2180:2184	arg1	marker					2190:2195	the early ALP marker	2176:2195	the early ALP marker	2176:2195	Altogether, these findings link O-GlcNAc cycling to the Runx2-dependent regulation of the early ALP marker under osteoblast differentiation conditions.
25187572	3	5	theme	O-linked	621:628	arg1	O-GlcNAc					651:658	O-GlcNAc	651:658	O-GlcNAc	651:658	Characterization of Runx2 by electron transfer dissociation tandem mass spectrometry revealed sites of O-linked N-acetylglucosamine (O-GlcNAc) modification, a nutrient-responsive post-translational modification that modulates the action of numerous transcriptional effectors.
25187572	3	5	theme	O-linked	621:628	arg1	N-acetylglucosamine					630:648	O-linked N-acetylglucosamine	621:648	O-linked N-acetylglucosamine (O-GlcNAc) modification	621:672	Characterization of Runx2 by electron transfer dissociation tandem mass spectrometry revealed sites of O-linked N-acetylglucosamine (O-GlcNAc) modification, a nutrient-responsive post-translational modification that modulates the action of numerous transcriptional effectors.
25187572	10	6	theme	marker	2190:2195	arg1	regulation					2162:2171	the Runx2-dependent regulation	2142:2171	the Runx2-dependent regulation of the early ALP marker	2142:2195	Altogether, these findings link O-GlcNAc cycling to the Runx2-dependent regulation of the early ALP marker under osteoblast differentiation conditions.
25187572	0	7	theme	O-GlcNAc	0:7	arg1	modification					9:20	O-GlcNAc modification	0:20	O-GlcNAc modification of the runt-related transcription factor 2 (Runx2)	0:71	O-GlcNAc modification of the runt-related transcription factor 2 (Runx2) links osteogenesis and nutrient metabolism in bone marrow mesenchymal stem cells.
25187572	7	8	dep	phosphatase	1482:1492	arg1	target					1556:1561	a transcriptional target	1538:1561	a transcriptional target of Runx2	1538:1570	In bone marrow-derived mesenchymal stem cells differentiated for 6 days in osteogenic media, inhibition of OGA resulted in elevated expression (24.3%) and activity (65.8%) of alkaline phosphatase (ALP) an early marker of bone formation and a transcriptional target of Runx2.
25187572	7	8	dep	phosphatase	1482:1492	arg1	marker					1509:1514	an early marker	1500:1514	an early marker of bone formation	1500:1532	In bone marrow-derived mesenchymal stem cells differentiated for 6 days in osteogenic media, inhibition of OGA resulted in elevated expression (24.3%) and activity (65.8%) of alkaline phosphatase (ALP) an early marker of bone formation and a transcriptional target of Runx2.
25187572	7	9	theme	transcriptional	1540:1554	arg1	target					1556:1561	a transcriptional target	1538:1561	a transcriptional target of Runx2	1538:1570	In bone marrow-derived mesenchymal stem cells differentiated for 6 days in osteogenic media, inhibition of OGA resulted in elevated expression (24.3%) and activity (65.8%) of alkaline phosphatase (ALP) an early marker of bone formation and a transcriptional target of Runx2.
25187572	7	10	theme	early	1503:1507	arg1	marker					1509:1514	an early marker	1500:1514	an early marker of bone formation	1500:1532	In bone marrow-derived mesenchymal stem cells differentiated for 6 days in osteogenic media, inhibition of OGA resulted in elevated expression (24.3%) and activity (65.8%) of alkaline phosphatase (ALP) an early marker of bone formation and a transcriptional target of Runx2.
25187572	10	11	theme	osteoblast	2203:2212	arg1	conditions					2230:2239	osteoblast differentiation conditions	2203:2239	osteoblast differentiation conditions	2203:2239	Altogether, these findings link O-GlcNAc cycling to the Runx2-dependent regulation of the early ALP marker under osteoblast differentiation conditions.
25187572	4	12	theme	O-GlcNAc	794:801	arg1	modification					803:814	O-GlcNAc modification	794:814	O-GlcNAc modification	794:814	O-GlcNAc modification occurs in close proximity to phosphorylated residues and novel sites of arginine methylation within regions known to regulate Runx2 transactivation.
25187572	7	13	theme	Runx2	1566:1570	arg1	target					1556:1561	a transcriptional target	1538:1561	a transcriptional target of Runx2	1538:1570	In bone marrow-derived mesenchymal stem cells differentiated for 6 days in osteogenic media, inhibition of OGA resulted in elevated expression (24.3%) and activity (65.8%) of alkaline phosphatase (ALP) an early marker of bone formation and a transcriptional target of Runx2.
25187572	7	13	theme	Runx2	1566:1570	arg1	marker					1509:1514	an early marker	1500:1514	an early marker of bone formation	1500:1532	In bone marrow-derived mesenchymal stem cells differentiated for 6 days in osteogenic media, inhibition of OGA resulted in elevated expression (24.3%) and activity (65.8%) of alkaline phosphatase (ALP) an early marker of bone formation and a transcriptional target of Runx2.
25187572	5	14	theme	transferase	1027:1037	arg1	enzyme					1039:1044	the O-GlcNAcylated, O-GlcNAc transferase enzyme	998:1044	the O-GlcNAcylated, O-GlcNAc transferase enzyme	998:1044	An interaction between Runx2 and the O-GlcNAcylated, O-GlcNAc transferase enzyme was also detected.
25187572	6	15	theme	MC3T3-E1	1272:1279	arg1	pre-osteoblasts					1281:1295	MC3T3-E1 pre-osteoblasts	1272:1295	MC3T3-E1 pre-osteoblasts	1272:1295	Pharmacological inhibition of O-GlcNAcase (OGA), the enzyme responsible for the removal of O-GlcNAc from Ser/Thr residues, enhanced basal (39.9%) and BMP2/7-induced (43.3%) Runx2 transcriptional activity in MC3T3-E1 pre-osteoblasts.
25187572	8	16	from	activity	1711:1718	arg1	abundance					1751:1759	the abundance	1747:1759	the abundance of O-GlcNAcylated Runx2	1747:1783	Osteogenic differentiation of bone marrow-derived mesenchymal stem cells in the presence of BMP2/7 for 8 days culminated in decreased OGA activity (39.0%) and an increase in the abundance of O-GlcNAcylated Runx2, as compared with unstimulated cells.
25187572	1	17	theme	osteoblast	194:203	arg1	differentiation					205:219	osteoblast differentiation	194:219	osteoblast differentiation	194:219	Runx2 is the master switch controlling osteoblast differentiation and formation of the mineralized skeleton.
25187572	10	18	theme	ALP	2186:2188	arg1	marker					2190:2195	the early ALP marker	2176:2195	the early ALP marker	2176:2195	Altogether, these findings link O-GlcNAc cycling to the Runx2-dependent regulation of the early ALP marker under osteoblast differentiation conditions.
25187572	9	19	theme	OGA	2043:2045	arg1	inhibition					2029:2038	direct or BMP2/7-induced inhibition	2004:2038	direct or BMP2/7-induced inhibition of OGA	2004:2045	Furthermore, BMP2/7-induced ALP activity was enhanced by 35.6% in bone marrow-derived mesenchymal stem cells differentiated in the presence of the OGA inhibitor, demonstrating that direct or BMP2/7-induced inhibition of OGA is associated with increased ALP activity.
25187572	0	20	theme	marrow	124:129	arg1	cells					148:152	bone marrow mesenchymal stem cells	119:152	bone marrow mesenchymal stem cells	119:152	O-GlcNAc modification of the runt-related transcription factor 2 (Runx2) links osteogenesis and nutrient metabolism in bone marrow mesenchymal stem cells.
25187572	3	21	theme	nutrient-responsive	677:695	arg1	modification					716:727	a nutrient-responsive post-translational modification	675:727	a nutrient-responsive post-translational modification that modulates the action of numerous transcriptional effectors	675:791	Characterization of Runx2 by electron transfer dissociation tandem mass spectrometry revealed sites of O-linked N-acetylglucosamine (O-GlcNAc) modification, a nutrient-responsive post-translational modification that modulates the action of numerous transcriptional effectors.
25187572	3	21	theme	nutrient-responsive	677:695	arg1	modification					661:672	O-linked N-acetylglucosamine (O-GlcNAc) modification	621:672	O-linked N-acetylglucosamine (O-GlcNAc) modification	621:672	Characterization of Runx2 by electron transfer dissociation tandem mass spectrometry revealed sites of O-linked N-acetylglucosamine (O-GlcNAc) modification, a nutrient-responsive post-translational modification that modulates the action of numerous transcriptional effectors.
25187572	7	22	theme	alkaline	1473:1480	arg1	phosphatase					1482:1492	alkaline phosphatase	1473:1492	alkaline phosphatase (ALP) an early marker of bone formation and a transcriptional target of Runx2	1473:1570	In bone marrow-derived mesenchymal stem cells differentiated for 6 days in osteogenic media, inhibition of OGA resulted in elevated expression (24.3%) and activity (65.8%) of alkaline phosphatase (ALP) an early marker of bone formation and a transcriptional target of Runx2.
25187572	7	22	theme	alkaline	1473:1480	arg1	ALP					1495:1497	ALP	1495:1497	ALP	1495:1497	In bone marrow-derived mesenchymal stem cells differentiated for 6 days in osteogenic media, inhibition of OGA resulted in elevated expression (24.3%) and activity (65.8%) of alkaline phosphatase (ALP) an early marker of bone formation and a transcriptional target of Runx2.
25187572	0	23	theme	stem	143:146	arg1	cells					148:152	bone marrow mesenchymal stem cells	119:152	bone marrow mesenchymal stem cells	119:152	O-GlcNAc modification of the runt-related transcription factor 2 (Runx2) links osteogenesis and nutrient metabolism in bone marrow mesenchymal stem cells.
25187572	6	24	theme	O-GlcNAcase	1095:1105	arg1	inhibition					1081:1090	Pharmacological inhibition	1065:1090	Pharmacological inhibition of O-GlcNAcase (OGA), the enzyme responsible for the removal of O-GlcNAc from Ser/Thr residues,	1065:1186	Pharmacological inhibition of O-GlcNAcase (OGA), the enzyme responsible for the removal of O-GlcNAc from Ser/Thr residues, enhanced basal (39.9%) and BMP2/7-induced (43.3%) Runx2 transcriptional activity in MC3T3-E1 pre-osteoblasts.
25187572	9	25	theme	increased	2066:2074	arg1	activity					2080:2087	increased ALP activity	2066:2087	increased ALP activity	2066:2087	Furthermore, BMP2/7-induced ALP activity was enhanced by 35.6% in bone marrow-derived mesenchymal stem cells differentiated in the presence of the OGA inhibitor, demonstrating that direct or BMP2/7-induced inhibition of OGA is associated with increased ALP activity.
25187572	6	26	theme	Ser/Thr	1170:1176	arg1	residues					1178:1185	Ser/Thr residues	1170:1185	Ser/Thr residues	1170:1185	Pharmacological inhibition of O-GlcNAcase (OGA), the enzyme responsible for the removal of O-GlcNAc from Ser/Thr residues, enhanced basal (39.9%) and BMP2/7-induced (43.3%) Runx2 transcriptional activity in MC3T3-E1 pre-osteoblasts.
25187572	0	27	from	osteogenesis	79:90	arg1	cells					148:152	bone marrow mesenchymal stem cells	119:152	bone marrow mesenchymal stem cells	119:152	O-GlcNAc modification of the runt-related transcription factor 2 (Runx2) links osteogenesis and nutrient metabolism in bone marrow mesenchymal stem cells.
25187572	7	28	theme	osteogenic	1373:1382	arg1	media					1384:1388	osteogenic media	1373:1388	osteogenic media	1373:1388	In bone marrow-derived mesenchymal stem cells differentiated for 6 days in osteogenic media, inhibition of OGA resulted in elevated expression (24.3%) and activity (65.8%) of alkaline phosphatase (ALP) an early marker of bone formation and a transcriptional target of Runx2.
25187572	6	29	theme	O-GlcNAc	1156:1163	arg1	removal					1145:1151	the removal	1141:1151	the removal of O-GlcNAc from Ser/Thr residues	1141:1185	Pharmacological inhibition of O-GlcNAcase (OGA), the enzyme responsible for the removal of O-GlcNAc from Ser/Thr residues, enhanced basal (39.9%) and BMP2/7-induced (43.3%) Runx2 transcriptional activity in MC3T3-E1 pre-osteoblasts.
25187572	9	30	theme	ALP	1851:1853	arg1	activity					1855:1862	BMP2/7-induced ALP activity	1836:1862	BMP2/7-induced ALP activity	1836:1862	Furthermore, BMP2/7-induced ALP activity was enhanced by 35.6% in bone marrow-derived mesenchymal stem cells differentiated in the presence of the OGA inhibitor, demonstrating that direct or BMP2/7-induced inhibition of OGA is associated with increased ALP activity.
25187572	4	31	theme	close	826:830	arg1	proximity					832:840	close proximity	826:840	close proximity to phosphorylated residues and novel sites of arginine methylation within regions known to regulate Runx2 transactivation	826:962	O-GlcNAc modification occurs in close proximity to phosphorylated residues and novel sites of arginine methylation within regions known to regulate Runx2 transactivation.
25187572	8	32	theme	marrow-derived	1608:1621	arg1	cells					1640:1644	bone marrow-derived mesenchymal stem cells	1603:1644	bone marrow-derived mesenchymal stem cells	1603:1644	Osteogenic differentiation of bone marrow-derived mesenchymal stem cells in the presence of BMP2/7 for 8 days culminated in decreased OGA activity (39.0%) and an increase in the abundance of O-GlcNAcylated Runx2, as compared with unstimulated cells.
25187572	6	33	from	residues	1178:1185	arg1	removal					1145:1151	the removal	1141:1151	the removal of O-GlcNAc from Ser/Thr residues	1141:1185	Pharmacological inhibition of O-GlcNAcase (OGA), the enzyme responsible for the removal of O-GlcNAc from Ser/Thr residues, enhanced basal (39.9%) and BMP2/7-induced (43.3%) Runx2 transcriptional activity in MC3T3-E1 pre-osteoblasts.
25187572	4	34	theme	methylation	897:907	arg1	sites					879:883	novel sites	873:883	novel sites of arginine methylation	873:907	O-GlcNAc modification occurs in close proximity to phosphorylated residues and novel sites of arginine methylation within regions known to regulate Runx2 transactivation.
25187572	4	34	theme	methylation	897:907	arg1	methylation					897:907	arginine methylation	888:907	arginine methylation	888:907	O-GlcNAc modification occurs in close proximity to phosphorylated residues and novel sites of arginine methylation within regions known to regulate Runx2 transactivation.
25187572	4	34	theme	methylation	897:907	arg1	residues					860:867	phosphorylated residues	845:867	phosphorylated residues	845:867	O-GlcNAc modification occurs in close proximity to phosphorylated residues and novel sites of arginine methylation within regions known to regulate Runx2 transactivation.
25187572	2	35	theme	Runx2	303:307	arg1	modification					287:298	The post-translational modification	264:298	The post-translational modification of Runx2 by phosphorylation, ubiquitinylation, and acetylation	264:361	The post-translational modification of Runx2 by phosphorylation, ubiquitinylation, and acetylation modulates its activity, stability, and interactions with transcriptional co-regulators and chromatin remodeling proteins downstream of osteogenic signals.
25187572	8	36	theme	stem	1635:1638	arg1	cells					1640:1644	bone marrow-derived mesenchymal stem cells	1603:1644	bone marrow-derived mesenchymal stem cells	1603:1644	Osteogenic differentiation of bone marrow-derived mesenchymal stem cells in the presence of BMP2/7 for 8 days culminated in decreased OGA activity (39.0%) and an increase in the abundance of O-GlcNAcylated Runx2, as compared with unstimulated cells.
25187572	8	37	from	increase	1735:1742	arg1	abundance					1751:1759	the abundance	1747:1759	the abundance of O-GlcNAcylated Runx2	1747:1783	Osteogenic differentiation of bone marrow-derived mesenchymal stem cells in the presence of BMP2/7 for 8 days culminated in decreased OGA activity (39.0%) and an increase in the abundance of O-GlcNAcylated Runx2, as compared with unstimulated cells.
25187572	2	38	theme	transcriptional	420:434	arg1	co-regulators					436:448	transcriptional co-regulators	420:448	transcriptional co-regulators	420:448	The post-translational modification of Runx2 by phosphorylation, ubiquitinylation, and acetylation modulates its activity, stability, and interactions with transcriptional co-regulators and chromatin remodeling proteins downstream of osteogenic signals.
25187572	0	39	theme	nutrient	96:103	arg1	metabolism					105:114	nutrient metabolism	96:114	nutrient metabolism	96:114	O-GlcNAc modification of the runt-related transcription factor 2 (Runx2) links osteogenesis and nutrient metabolism in bone marrow mesenchymal stem cells.
25187572	2	40	theme	osteogenic	498:507	arg1	signals					509:515	osteogenic signals	498:515	osteogenic signals	498:515	The post-translational modification of Runx2 by phosphorylation, ubiquitinylation, and acetylation modulates its activity, stability, and interactions with transcriptional co-regulators and chromatin remodeling proteins downstream of osteogenic signals.
25187572	4	41	theme	novel	873:877	arg1	sites					879:883	novel sites	873:883	novel sites of arginine methylation	873:907	O-GlcNAc modification occurs in close proximity to phosphorylated residues and novel sites of arginine methylation within regions known to regulate Runx2 transactivation.
25187572	4	41	theme	novel	873:877	arg1	methylation					897:907	arginine methylation	888:907	arginine methylation	888:907	O-GlcNAc modification occurs in close proximity to phosphorylated residues and novel sites of arginine methylation within regions known to regulate Runx2 transactivation.
25187572	7	42	theme	mesenchymal	1321:1331	arg1	cells					1338:1342	bone marrow-derived mesenchymal stem cells	1301:1342	bone marrow-derived mesenchymal stem cells differentiated for 6 days in osteogenic media	1301:1388	In bone marrow-derived mesenchymal stem cells differentiated for 6 days in osteogenic media, inhibition of OGA resulted in elevated expression (24.3%) and activity (65.8%) of alkaline phosphatase (ALP) an early marker of bone formation and a transcriptional target of Runx2.
25187572	8	43	theme	Osteogenic	1573:1582	arg1	differentiation					1584:1598	Osteogenic differentiation	1573:1598	Osteogenic differentiation of bone marrow-derived mesenchymal stem cells in the presence of BMP2/7 for 8 days	1573:1681	Osteogenic differentiation of bone marrow-derived mesenchymal stem cells in the presence of BMP2/7 for 8 days culminated in decreased OGA activity (39.0%) and an increase in the abundance of O-GlcNAcylated Runx2, as compared with unstimulated cells.
25187572	2	44	theme	downstream	484:493	arg1	co-regulators					436:448	transcriptional co-regulators	420:448	transcriptional co-regulators	420:448	The post-translational modification of Runx2 by phosphorylation, ubiquitinylation, and acetylation modulates its activity, stability, and interactions with transcriptional co-regulators and chromatin remodeling proteins downstream of osteogenic signals.
25187572	3	45	theme	post-translational	697:714	arg1	modification					716:727	a nutrient-responsive post-translational modification	675:727	a nutrient-responsive post-translational modification that modulates the action of numerous transcriptional effectors	675:791	Characterization of Runx2 by electron transfer dissociation tandem mass spectrometry revealed sites of O-linked N-acetylglucosamine (O-GlcNAc) modification, a nutrient-responsive post-translational modification that modulates the action of numerous transcriptional effectors.
25187572	3	45	theme	post-translational	697:714	arg1	modification					661:672	O-linked N-acetylglucosamine (O-GlcNAc) modification	621:672	O-linked N-acetylglucosamine (O-GlcNAc) modification	621:672	Characterization of Runx2 by electron transfer dissociation tandem mass spectrometry revealed sites of O-linked N-acetylglucosamine (O-GlcNAc) modification, a nutrient-responsive post-translational modification that modulates the action of numerous transcriptional effectors.
25187572	9	46	theme	bone	1889:1892	arg1	cells					1926:1930	bone marrow-derived mesenchymal stem cells	1889:1930	bone marrow-derived mesenchymal stem cells differentiated in the presence of the OGA inhibitor	1889:1982	Furthermore, BMP2/7-induced ALP activity was enhanced by 35.6% in bone marrow-derived mesenchymal stem cells differentiated in the presence of the OGA inhibitor, demonstrating that direct or BMP2/7-induced inhibition of OGA is associated with increased ALP activity.
25187572	2	47	theme	remodeling	464:473	arg1	proteins					475:482	chromatin remodeling proteins	454:482	chromatin remodeling proteins	454:482	The post-translational modification of Runx2 by phosphorylation, ubiquitinylation, and acetylation modulates its activity, stability, and interactions with transcriptional co-regulators and chromatin remodeling proteins downstream of osteogenic signals.
25187572	6	48	theme	basal	1197:1201	arg1	activity					1260:1267	basal (39.9%) and BMP2/7-induced (43.3%) Runx2 transcriptional activity	1197:1267	basal (39.9%) and BMP2/7-induced (43.3%) Runx2 transcriptional activity in MC3T3-E1 pre-osteoblasts	1197:1295	Pharmacological inhibition of O-GlcNAcase (OGA), the enzyme responsible for the removal of O-GlcNAc from Ser/Thr residues, enhanced basal (39.9%) and BMP2/7-induced (43.3%) Runx2 transcriptional activity in MC3T3-E1 pre-osteoblasts.
25187572	9	49	theme	mesenchymal	1909:1919	arg1	cells					1926:1930	bone marrow-derived mesenchymal stem cells	1889:1930	bone marrow-derived mesenchymal stem cells differentiated in the presence of the OGA inhibitor	1889:1982	Furthermore, BMP2/7-induced ALP activity was enhanced by 35.6% in bone marrow-derived mesenchymal stem cells differentiated in the presence of the OGA inhibitor, demonstrating that direct or BMP2/7-induced inhibition of OGA is associated with increased ALP activity.
25187572	8	50	theme	BMP2/7	1665:1670	arg1	presence					1653:1660	the presence	1649:1660	the presence of BMP2/7 for 8 days	1649:1681	Osteogenic differentiation of bone marrow-derived mesenchymal stem cells in the presence of BMP2/7 for 8 days culminated in decreased OGA activity (39.0%) and an increase in the abundance of O-GlcNAcylated Runx2, as compared with unstimulated cells.
25187572	3	51	theme	numerous	758:765	arg1	effectors					783:791	numerous transcriptional effectors	758:791	numerous transcriptional effectors	758:791	Characterization of Runx2 by electron transfer dissociation tandem mass spectrometry revealed sites of O-linked N-acetylglucosamine (O-GlcNAc) modification, a nutrient-responsive post-translational modification that modulates the action of numerous transcriptional effectors.
25187572	0	52	theme	runt-related	29:40	arg1	factor					56:61	the runt-related transcription factor 2	25:63	the runt-related transcription factor 2 (Runx2)	25:71	O-GlcNAc modification of the runt-related transcription factor 2 (Runx2) links osteogenesis and nutrient metabolism in bone marrow mesenchymal stem cells.
25187572	0	52	theme	runt-related	29:40	arg1	Runx2					66:70	Runx2	66:70	Runx2	66:70	O-GlcNAc modification of the runt-related transcription factor 2 (Runx2) links osteogenesis and nutrient metabolism in bone marrow mesenchymal stem cells.
25187572	5	53	dep	O-GlcNAcylated	1002:1015	arg1	O-GlcNAc					1018:1025	O-GlcNAc	1018:1025	O-GlcNAc	1018:1025	An interaction between Runx2 and the O-GlcNAcylated, O-GlcNAc transferase enzyme was also detected.
25187572	3	54	theme	electron	547:554	arg1	spectrometry					590:601	electron transfer dissociation tandem mass spectrometry	547:601	electron transfer dissociation tandem mass spectrometry	547:601	Characterization of Runx2 by electron transfer dissociation tandem mass spectrometry revealed sites of O-linked N-acetylglucosamine (O-GlcNAc) modification, a nutrient-responsive post-translational modification that modulates the action of numerous transcriptional effectors.
25187572	0	55	theme	factor	56:61	arg1	modification					9:20	O-GlcNAc modification	0:20	O-GlcNAc modification of the runt-related transcription factor 2 (Runx2)	0:71	O-GlcNAc modification of the runt-related transcription factor 2 (Runx2) links osteogenesis and nutrient metabolism in bone marrow mesenchymal stem cells.
25187572	8	56	link	marrow-derived	1608:1621	arg1	cells					1640:1644	bone marrow-derived mesenchymal stem cells	1603:1644	bone marrow-derived mesenchymal stem cells	1603:1644	Osteogenic differentiation of bone marrow-derived mesenchymal stem cells in the presence of BMP2/7 for 8 days culminated in decreased OGA activity (39.0%) and an increase in the abundance of O-GlcNAcylated Runx2, as compared with unstimulated cells.
25187572	3	57	theme	Runx2	538:542	arg1	Characterization					518:533	Characterization	518:533	Characterization of Runx2 by electron transfer dissociation tandem mass spectrometry	518:601	Characterization of Runx2 by electron transfer dissociation tandem mass spectrometry revealed sites of O-linked N-acetylglucosamine (O-GlcNAc) modification, a nutrient-responsive post-translational modification that modulates the action of numerous transcriptional effectors.
25187572	8	58	theme	decreased	1697:1705	arg1	activity					1711:1718	decreased OGA activity	1697:1718	decreased OGA activity (39.0%)	1697:1726	Osteogenic differentiation of bone marrow-derived mesenchymal stem cells in the presence of BMP2/7 for 8 days culminated in decreased OGA activity (39.0%) and an increase in the abundance of O-GlcNAcylated Runx2, as compared with unstimulated cells.
25187572	8	58	theme	decreased	1697:1705	arg1	%					1725:1725	39.0%	1721:1725	39.0%	1721:1725	Osteogenic differentiation of bone marrow-derived mesenchymal stem cells in the presence of BMP2/7 for 8 days culminated in decreased OGA activity (39.0%) and an increase in the abundance of O-GlcNAcylated Runx2, as compared with unstimulated cells.
25187572	3	59	theme	effectors	783:791	arg1	action					748:753	the action	744:753	the action of numerous transcriptional effectors	744:791	Characterization of Runx2 by electron transfer dissociation tandem mass spectrometry revealed sites of O-linked N-acetylglucosamine (O-GlcNAc) modification, a nutrient-responsive post-translational modification that modulates the action of numerous transcriptional effectors.
25187572	4	60	theme	Runx2	942:946	arg1	transactivation					948:962	Runx2 transactivation	942:962	Runx2 transactivation	942:962	O-GlcNAc modification occurs in close proximity to phosphorylated residues and novel sites of arginine methylation within regions known to regulate Runx2 transactivation.
25187572	3	61	theme	mass	585:588	arg1	spectrometry					590:601	electron transfer dissociation tandem mass spectrometry	547:601	electron transfer dissociation tandem mass spectrometry	547:601	Characterization of Runx2 by electron transfer dissociation tandem mass spectrometry revealed sites of O-linked N-acetylglucosamine (O-GlcNAc) modification, a nutrient-responsive post-translational modification that modulates the action of numerous transcriptional effectors.
25187572	2	62	with	interactions	402:413	arg1	proteins					475:482	chromatin remodeling proteins	454:482	chromatin remodeling proteins	454:482	The post-translational modification of Runx2 by phosphorylation, ubiquitinylation, and acetylation modulates its activity, stability, and interactions with transcriptional co-regulators and chromatin remodeling proteins downstream of osteogenic signals.
25187572	2	62	with	interactions	402:413	arg1	co-regulators					436:448	transcriptional co-regulators	420:448	transcriptional co-regulators	420:448	The post-translational modification of Runx2 by phosphorylation, ubiquitinylation, and acetylation modulates its activity, stability, and interactions with transcriptional co-regulators and chromatin remodeling proteins downstream of osteogenic signals.
25187572	7	63	theme	elevated	1421:1428	arg1	expression					1430:1439	elevated expression	1421:1439	elevated expression (24.3%)	1421:1447	In bone marrow-derived mesenchymal stem cells differentiated for 6 days in osteogenic media, inhibition of OGA resulted in elevated expression (24.3%) and activity (65.8%) of alkaline phosphatase (ALP) an early marker of bone formation and a transcriptional target of Runx2.
25187572	7	63	theme	elevated	1421:1428	arg1	%					1446:1446	24.3%	1442:1446	24.3%	1442:1446	In bone marrow-derived mesenchymal stem cells differentiated for 6 days in osteogenic media, inhibition of OGA resulted in elevated expression (24.3%) and activity (65.8%) of alkaline phosphatase (ALP) an early marker of bone formation and a transcriptional target of Runx2.
25187572	10	64	theme	differentiation	2214:2228	arg1	conditions					2230:2239	osteoblast differentiation conditions	2203:2239	osteoblast differentiation conditions	2203:2239	Altogether, these findings link O-GlcNAc cycling to the Runx2-dependent regulation of the early ALP marker under osteoblast differentiation conditions.
25187572	3	65	theme	dissociation	565:576	arg1	spectrometry					590:601	electron transfer dissociation tandem mass spectrometry	547:601	electron transfer dissociation tandem mass spectrometry	547:601	Characterization of Runx2 by electron transfer dissociation tandem mass spectrometry revealed sites of O-linked N-acetylglucosamine (O-GlcNAc) modification, a nutrient-responsive post-translational modification that modulates the action of numerous transcriptional effectors.
25187572	1	66	theme	skeleton	254:261	arg1	formation					225:233	formation	225:233	formation of the mineralized skeleton	225:261	Runx2 is the master switch controlling osteoblast differentiation and formation of the mineralized skeleton.
25187572	1	66	theme	skeleton	254:261	arg1	differentiation					205:219	osteoblast differentiation	194:219	osteoblast differentiation	194:219	Runx2 is the master switch controlling osteoblast differentiation and formation of the mineralized skeleton.
25187572	6	67	theme	Pharmacological	1065:1079	arg1	inhibition					1081:1090	Pharmacological inhibition	1065:1090	Pharmacological inhibition of O-GlcNAcase (OGA), the enzyme responsible for the removal of O-GlcNAc from Ser/Thr residues,	1065:1186	Pharmacological inhibition of O-GlcNAcase (OGA), the enzyme responsible for the removal of O-GlcNAc from Ser/Thr residues, enhanced basal (39.9%) and BMP2/7-induced (43.3%) Runx2 transcriptional activity in MC3T3-E1 pre-osteoblasts.
25187572	6	68	theme	BMP2/7-induced	1215:1228	arg1	activity					1260:1267	basal (39.9%) and BMP2/7-induced (43.3%) Runx2 transcriptional activity	1197:1267	basal (39.9%) and BMP2/7-induced (43.3%) Runx2 transcriptional activity in MC3T3-E1 pre-osteoblasts	1197:1295	Pharmacological inhibition of O-GlcNAcase (OGA), the enzyme responsible for the removal of O-GlcNAc from Ser/Thr residues, enhanced basal (39.9%) and BMP2/7-induced (43.3%) Runx2 transcriptional activity in MC3T3-E1 pre-osteoblasts.
25187572	9	69	theme	inhibitor	1974:1982	arg1	presence					1954:1961	the presence	1950:1961	the presence of the OGA inhibitor	1950:1982	Furthermore, BMP2/7-induced ALP activity was enhanced by 35.6% in bone marrow-derived mesenchymal stem cells differentiated in the presence of the OGA inhibitor, demonstrating that direct or BMP2/7-induced inhibition of OGA is associated with increased ALP activity.
25187572	8	70	theme	O-GlcNAcylated	1764:1777	arg1	Runx2					1779:1783	O-GlcNAcylated Runx2	1764:1783	O-GlcNAcylated Runx2	1764:1783	Osteogenic differentiation of bone marrow-derived mesenchymal stem cells in the presence of BMP2/7 for 8 days culminated in decreased OGA activity (39.0%) and an increase in the abundance of O-GlcNAcylated Runx2, as compared with unstimulated cells.
25187572	5	71	theme	O-GlcNAcylated	1002:1015	arg1	enzyme					1039:1044	the O-GlcNAcylated, O-GlcNAc transferase enzyme	998:1044	the O-GlcNAcylated, O-GlcNAc transferase enzyme	998:1044	An interaction between Runx2 and the O-GlcNAcylated, O-GlcNAc transferase enzyme was also detected.
25187572	9	72	from	%	1884:1884	arg1	cells					1926:1930	bone marrow-derived mesenchymal stem cells	1889:1930	bone marrow-derived mesenchymal stem cells differentiated in the presence of the OGA inhibitor	1889:1982	Furthermore, BMP2/7-induced ALP activity was enhanced by 35.6% in bone marrow-derived mesenchymal stem cells differentiated in the presence of the OGA inhibitor, demonstrating that direct or BMP2/7-induced inhibition of OGA is associated with increased ALP activity.
25187572	7	73	theme	bone	1519:1522	arg1	formation					1524:1532	bone formation	1519:1532	bone formation	1519:1532	In bone marrow-derived mesenchymal stem cells differentiated for 6 days in osteogenic media, inhibition of OGA resulted in elevated expression (24.3%) and activity (65.8%) of alkaline phosphatase (ALP) an early marker of bone formation and a transcriptional target of Runx2.
25187572	9	74	theme	direct	2004:2009	arg1	inhibition					2029:2038	direct or BMP2/7-induced inhibition	2004:2038	direct or BMP2/7-induced inhibition of OGA	2004:2045	Furthermore, BMP2/7-induced ALP activity was enhanced by 35.6% in bone marrow-derived mesenchymal stem cells differentiated in the presence of the OGA inhibitor, demonstrating that direct or BMP2/7-induced inhibition of OGA is associated with increased ALP activity.
25187572	10	75	attach	link	2117:2120	arg1	regulation					2162:2171	the Runx2-dependent regulation	2142:2171	the Runx2-dependent regulation of the early ALP marker	2142:2195	Altogether, these findings link O-GlcNAc cycling to the Runx2-dependent regulation of the early ALP marker under osteoblast differentiation conditions.
25187572	10	75	attach	link	2117:2120	arg2	findings					2108:2115	these findings	2102:2115	these findings	2102:2115	Altogether, these findings link O-GlcNAc cycling to the Runx2-dependent regulation of the early ALP marker under osteoblast differentiation conditions.
25187572	1	76	theme	master	168:173	arg1	switch					175:180	the master switch	164:180	the master switch controlling osteoblast differentiation and formation of the mineralized skeleton	164:261	Runx2 is the master switch controlling osteoblast differentiation and formation of the mineralized skeleton.
25187572	1	76	theme	master	168:173	arg1	Runx2					155:159	Runx2	155:159	Runx2	155:159	Runx2 is the master switch controlling osteoblast differentiation and formation of the mineralized skeleton.
25187572	6	77	theme	responsible	1125:1135	arg1	O-GlcNAcase					1095:1105	O-GlcNAcase	1095:1105	O-GlcNAcase (OGA)	1095:1111	Pharmacological inhibition of O-GlcNAcase (OGA), the enzyme responsible for the removal of O-GlcNAc from Ser/Thr residues, enhanced basal (39.9%) and BMP2/7-induced (43.3%) Runx2 transcriptional activity in MC3T3-E1 pre-osteoblasts.
25187572	6	77	theme	responsible	1125:1135	arg1	enzyme					1118:1123	the enzyme	1114:1123	the enzyme responsible for the removal of O-GlcNAc from Ser/Thr residues	1114:1185	Pharmacological inhibition of O-GlcNAcase (OGA), the enzyme responsible for the removal of O-GlcNAc from Ser/Thr residues, enhanced basal (39.9%) and BMP2/7-induced (43.3%) Runx2 transcriptional activity in MC3T3-E1 pre-osteoblasts.
25187572	9	78	theme	BMP2/7-induced	2014:2027	arg1	inhibition					2029:2038	direct or BMP2/7-induced inhibition	2004:2038	direct or BMP2/7-induced inhibition of OGA	2004:2045	Furthermore, BMP2/7-induced ALP activity was enhanced by 35.6% in bone marrow-derived mesenchymal stem cells differentiated in the presence of the OGA inhibitor, demonstrating that direct or BMP2/7-induced inhibition of OGA is associated with increased ALP activity.
25187572	0	79	theme	bone	119:122	arg1	marrow					124:129	bone marrow	119:129	bone marrow mesenchymal stem cells	119:152	O-GlcNAc modification of the runt-related transcription factor 2 (Runx2) links osteogenesis and nutrient metabolism in bone marrow mesenchymal stem cells.
25187572	3	80	theme	N-acetylglucosamine	630:648	arg1	modification					716:727	a nutrient-responsive post-translational modification	675:727	a nutrient-responsive post-translational modification that modulates the action of numerous transcriptional effectors	675:791	Characterization of Runx2 by electron transfer dissociation tandem mass spectrometry revealed sites of O-linked N-acetylglucosamine (O-GlcNAc) modification, a nutrient-responsive post-translational modification that modulates the action of numerous transcriptional effectors.
25187572	3	80	theme	N-acetylglucosamine	630:648	arg1	modification					661:672	O-linked N-acetylglucosamine (O-GlcNAc) modification	621:672	O-linked N-acetylglucosamine (O-GlcNAc) modification	621:672	Characterization of Runx2 by electron transfer dissociation tandem mass spectrometry revealed sites of O-linked N-acetylglucosamine (O-GlcNAc) modification, a nutrient-responsive post-translational modification that modulates the action of numerous transcriptional effectors.
25187572	8	81	theme	unstimulated	1803:1814	arg1	cells					1816:1820	unstimulated cells	1803:1820	unstimulated cells	1803:1820	Osteogenic differentiation of bone marrow-derived mesenchymal stem cells in the presence of BMP2/7 for 8 days culminated in decreased OGA activity (39.0%) and an increase in the abundance of O-GlcNAcylated Runx2, as compared with unstimulated cells.
25187572	6	82	theme	transcriptional	1244:1258	arg1	activity					1260:1267	basal (39.9%) and BMP2/7-induced (43.3%) Runx2 transcriptional activity	1197:1267	basal (39.9%) and BMP2/7-induced (43.3%) Runx2 transcriptional activity in MC3T3-E1 pre-osteoblasts	1197:1295	Pharmacological inhibition of O-GlcNAcase (OGA), the enzyme responsible for the removal of O-GlcNAc from Ser/Thr residues, enhanced basal (39.9%) and BMP2/7-induced (43.3%) Runx2 transcriptional activity in MC3T3-E1 pre-osteoblasts.
25187572	0	83	theme	mesenchymal	131:141	arg1	cells					148:152	bone marrow mesenchymal stem cells	119:152	bone marrow mesenchymal stem cells	119:152	O-GlcNAc modification of the runt-related transcription factor 2 (Runx2) links osteogenesis and nutrient metabolism in bone marrow mesenchymal stem cells.
25187572	3	84	theme	modification	661:672	arg1	modification					661:672	O-linked N-acetylglucosamine (O-GlcNAc) modification	621:672	O-linked N-acetylglucosamine (O-GlcNAc) modification	621:672	Characterization of Runx2 by electron transfer dissociation tandem mass spectrometry revealed sites of O-linked N-acetylglucosamine (O-GlcNAc) modification, a nutrient-responsive post-translational modification that modulates the action of numerous transcriptional effectors.
25187572	3	84	theme	modification	661:672	arg1	sites					612:616	sites	612:616	sites of O-linked N-acetylglucosamine (O-GlcNAc) modification, a nutrient-responsive post-translational modification that modulates the action of numerous transcriptional effectors	612:791	Characterization of Runx2 by electron transfer dissociation tandem mass spectrometry revealed sites of O-linked N-acetylglucosamine (O-GlcNAc) modification, a nutrient-responsive post-translational modification that modulates the action of numerous transcriptional effectors.
25187572	0	85	from	metabolism	105:114	arg1	cells					148:152	bone marrow mesenchymal stem cells	119:152	bone marrow mesenchymal stem cells	119:152	O-GlcNAc modification of the runt-related transcription factor 2 (Runx2) links osteogenesis and nutrient metabolism in bone marrow mesenchymal stem cells.
25187572	7	86	theme	phosphatase	1482:1492	arg1	expression					1430:1439	elevated expression	1421:1439	elevated expression (24.3%)	1421:1447	In bone marrow-derived mesenchymal stem cells differentiated for 6 days in osteogenic media, inhibition of OGA resulted in elevated expression (24.3%) and activity (65.8%) of alkaline phosphatase (ALP) an early marker of bone formation and a transcriptional target of Runx2.
25187572	7	86	theme	phosphatase	1482:1492	arg1	%					1446:1446	24.3%	1442:1446	24.3%	1442:1446	In bone marrow-derived mesenchymal stem cells differentiated for 6 days in osteogenic media, inhibition of OGA resulted in elevated expression (24.3%) and activity (65.8%) of alkaline phosphatase (ALP) an early marker of bone formation and a transcriptional target of Runx2.
25187572	7	86	theme	phosphatase	1482:1492	arg1	activity					1453:1460	activity	1453:1460	activity (65.8%)	1453:1468	In bone marrow-derived mesenchymal stem cells differentiated for 6 days in osteogenic media, inhibition of OGA resulted in elevated expression (24.3%) and activity (65.8%) of alkaline phosphatase (ALP) an early marker of bone formation and a transcriptional target of Runx2.
25187572	7	86	theme	phosphatase	1482:1492	arg1	%					1467:1467	65.8%	1463:1467	65.8%	1463:1467	In bone marrow-derived mesenchymal stem cells differentiated for 6 days in osteogenic media, inhibition of OGA resulted in elevated expression (24.3%) and activity (65.8%) of alkaline phosphatase (ALP) an early marker of bone formation and a transcriptional target of Runx2.
25187572	2	87	theme	post-translational	268:285	arg1	modification					287:298	The post-translational modification	264:298	The post-translational modification of Runx2 by phosphorylation, ubiquitinylation, and acetylation	264:361	The post-translational modification of Runx2 by phosphorylation, ubiquitinylation, and acetylation modulates its activity, stability, and interactions with transcriptional co-regulators and chromatin remodeling proteins downstream of osteogenic signals.
25187572	9	88	link	marrow-derived	1894:1907	arg1	cells					1926:1930	bone marrow-derived mesenchymal stem cells	1889:1930	bone marrow-derived mesenchymal stem cells differentiated in the presence of the OGA inhibitor	1889:1982	Furthermore, BMP2/7-induced ALP activity was enhanced by 35.6% in bone marrow-derived mesenchymal stem cells differentiated in the presence of the OGA inhibitor, demonstrating that direct or BMP2/7-induced inhibition of OGA is associated with increased ALP activity.
25187572	9	89	theme	ALP	2076:2078	arg1	activity					2080:2087	increased ALP activity	2066:2087	increased ALP activity	2066:2087	Furthermore, BMP2/7-induced ALP activity was enhanced by 35.6% in bone marrow-derived mesenchymal stem cells differentiated in the presence of the OGA inhibitor, demonstrating that direct or BMP2/7-induced inhibition of OGA is associated with increased ALP activity.
25187572	4	90	theme	phosphorylated	845:858	arg1	methylation					897:907	arginine methylation	888:907	arginine methylation	888:907	O-GlcNAc modification occurs in close proximity to phosphorylated residues and novel sites of arginine methylation within regions known to regulate Runx2 transactivation.
25187572	4	90	theme	phosphorylated	845:858	arg1	residues					860:867	phosphorylated residues	845:867	phosphorylated residues	845:867	O-GlcNAc modification occurs in close proximity to phosphorylated residues and novel sites of arginine methylation within regions known to regulate Runx2 transactivation.
25187572	6	91	theme	Runx2	1238:1242	arg1	activity					1260:1267	basal (39.9%) and BMP2/7-induced (43.3%) Runx2 transcriptional activity	1197:1267	basal (39.9%) and BMP2/7-induced (43.3%) Runx2 transcriptional activity in MC3T3-E1 pre-osteoblasts	1197:1295	Pharmacological inhibition of O-GlcNAcase (OGA), the enzyme responsible for the removal of O-GlcNAc from Ser/Thr residues, enhanced basal (39.9%) and BMP2/7-induced (43.3%) Runx2 transcriptional activity in MC3T3-E1 pre-osteoblasts.
25187572	7	92	link	marrow-derived	1306:1319	arg1	cells					1338:1342	bone marrow-derived mesenchymal stem cells	1301:1342	bone marrow-derived mesenchymal stem cells differentiated for 6 days in osteogenic media	1301:1388	In bone marrow-derived mesenchymal stem cells differentiated for 6 days in osteogenic media, inhibition of OGA resulted in elevated expression (24.3%) and activity (65.8%) of alkaline phosphatase (ALP) an early marker of bone formation and a transcriptional target of Runx2.
25187572	9	93	theme	BMP2/7-induced	1836:1849	arg1	activity					1855:1862	BMP2/7-induced ALP activity	1836:1862	BMP2/7-induced ALP activity	1836:1862	Furthermore, BMP2/7-induced ALP activity was enhanced by 35.6% in bone marrow-derived mesenchymal stem cells differentiated in the presence of the OGA inhibitor, demonstrating that direct or BMP2/7-induced inhibition of OGA is associated with increased ALP activity.
25187572	8	94	theme	mesenchymal	1623:1633	arg1	cells					1640:1644	bone marrow-derived mesenchymal stem cells	1603:1644	bone marrow-derived mesenchymal stem cells	1603:1644	Osteogenic differentiation of bone marrow-derived mesenchymal stem cells in the presence of BMP2/7 for 8 days culminated in decreased OGA activity (39.0%) and an increase in the abundance of O-GlcNAcylated Runx2, as compared with unstimulated cells.
25187572	8	95	from	differentiation	1584:1598	arg1	presence					1653:1660	the presence	1649:1660	the presence of BMP2/7 for 8 days	1649:1681	Osteogenic differentiation of bone marrow-derived mesenchymal stem cells in the presence of BMP2/7 for 8 days culminated in decreased OGA activity (39.0%) and an increase in the abundance of O-GlcNAcylated Runx2, as compared with unstimulated cells.
25187572	8	96	theme	cells	1640:1644	arg1	differentiation					1584:1598	Osteogenic differentiation	1573:1598	Osteogenic differentiation of bone marrow-derived mesenchymal stem cells in the presence of BMP2/7 for 8 days	1573:1681	Osteogenic differentiation of bone marrow-derived mesenchymal stem cells in the presence of BMP2/7 for 8 days culminated in decreased OGA activity (39.0%) and an increase in the abundance of O-GlcNAcylated Runx2, as compared with unstimulated cells.
25187572	4	97	theme	arginine	888:895	arg1	methylation					897:907	arginine methylation	888:907	arginine methylation	888:907	O-GlcNAc modification occurs in close proximity to phosphorylated residues and novel sites of arginine methylation within regions known to regulate Runx2 transactivation.
25187572	10	98	theme	O-GlcNAc	2122:2129	arg1	cycling					2131:2137	O-GlcNAc cycling	2122:2137	O-GlcNAc cycling	2122:2137	Altogether, these findings link O-GlcNAc cycling to the Runx2-dependent regulation of the early ALP marker under osteoblast differentiation conditions.
25187572	7	99	theme	stem	1333:1336	arg1	cells					1338:1342	bone marrow-derived mesenchymal stem cells	1301:1342	bone marrow-derived mesenchymal stem cells differentiated for 6 days in osteogenic media	1301:1388	In bone marrow-derived mesenchymal stem cells differentiated for 6 days in osteogenic media, inhibition of OGA resulted in elevated expression (24.3%) and activity (65.8%) of alkaline phosphatase (ALP) an early marker of bone formation and a transcriptional target of Runx2.
25187572	3	100	link	O-linked	621:628	arg1	O-GlcNAc					651:658	O-GlcNAc	651:658	O-GlcNAc	651:658	Characterization of Runx2 by electron transfer dissociation tandem mass spectrometry revealed sites of O-linked N-acetylglucosamine (O-GlcNAc) modification, a nutrient-responsive post-translational modification that modulates the action of numerous transcriptional effectors.
25187572	3	100	link	O-linked	621:628	arg1	N-acetylglucosamine					630:648	O-linked N-acetylglucosamine	621:648	O-linked N-acetylglucosamine (O-GlcNAc) modification	621:672	Characterization of Runx2 by electron transfer dissociation tandem mass spectrometry revealed sites of O-linked N-acetylglucosamine (O-GlcNAc) modification, a nutrient-responsive post-translational modification that modulates the action of numerous transcriptional effectors.
25187572	6	101	dep	basal	1197:1201	arg1	%					1208:1208	39.9%	1204:1208	39.9%	1204:1208	Pharmacological inhibition of O-GlcNAcase (OGA), the enzyme responsible for the removal of O-GlcNAc from Ser/Thr residues, enhanced basal (39.9%) and BMP2/7-induced (43.3%) Runx2 transcriptional activity in MC3T3-E1 pre-osteoblasts.
25187572	7	102	theme	marrow-derived	1306:1319	arg1	cells					1338:1342	bone marrow-derived mesenchymal stem cells	1301:1342	bone marrow-derived mesenchymal stem cells differentiated for 6 days in osteogenic media	1301:1388	In bone marrow-derived mesenchymal stem cells differentiated for 6 days in osteogenic media, inhibition of OGA resulted in elevated expression (24.3%) and activity (65.8%) of alkaline phosphatase (ALP) an early marker of bone formation and a transcriptional target of Runx2.
25187572	9	103	theme	marrow-derived	1894:1907	arg1	cells					1926:1930	bone marrow-derived mesenchymal stem cells	1889:1930	bone marrow-derived mesenchymal stem cells differentiated in the presence of the OGA inhibitor	1889:1982	Furthermore, BMP2/7-induced ALP activity was enhanced by 35.6% in bone marrow-derived mesenchymal stem cells differentiated in the presence of the OGA inhibitor, demonstrating that direct or BMP2/7-induced inhibition of OGA is associated with increased ALP activity.
25187572	2	104	theme	chromatin	454:462	arg1	proteins					475:482	chromatin remodeling proteins	454:482	chromatin remodeling proteins	454:482	The post-translational modification of Runx2 by phosphorylation, ubiquitinylation, and acetylation modulates its activity, stability, and interactions with transcriptional co-regulators and chromatin remodeling proteins downstream of osteogenic signals.
25187572	0	105	theme	transcription	42:54	arg1	factor					56:61	the runt-related transcription factor 2	25:63	the runt-related transcription factor 2 (Runx2)	25:71	O-GlcNAc modification of the runt-related transcription factor 2 (Runx2) links osteogenesis and nutrient metabolism in bone marrow mesenchymal stem cells.
25187572	0	105	theme	transcription	42:54	arg1	Runx2					66:70	Runx2	66:70	Runx2	66:70	O-GlcNAc modification of the runt-related transcription factor 2 (Runx2) links osteogenesis and nutrient metabolism in bone marrow mesenchymal stem cells.
25187572	9	106	theme	stem	1921:1924	arg1	cells					1926:1930	bone marrow-derived mesenchymal stem cells	1889:1930	bone marrow-derived mesenchymal stem cells differentiated in the presence of the OGA inhibitor	1889:1982	Furthermore, BMP2/7-induced ALP activity was enhanced by 35.6% in bone marrow-derived mesenchymal stem cells differentiated in the presence of the OGA inhibitor, demonstrating that direct or BMP2/7-induced inhibition of OGA is associated with increased ALP activity.
25187572	6	107	dep	BMP2/7-induced	1215:1228	arg1	%					1235:1235	43.3%	1231:1235	43.3%	1231:1235	Pharmacological inhibition of O-GlcNAcase (OGA), the enzyme responsible for the removal of O-GlcNAc from Ser/Thr residues, enhanced basal (39.9%) and BMP2/7-induced (43.3%) Runx2 transcriptional activity in MC3T3-E1 pre-osteoblasts.
25187572	2	108	theme	signals	509:515	arg1	downstream					484:493	downstream	484:493	downstream	484:493	The post-translational modification of Runx2 by phosphorylation, ubiquitinylation, and acetylation modulates its activity, stability, and interactions with transcriptional co-regulators and chromatin remodeling proteins downstream of osteogenic signals.
25187572	6	109	from	activity	1260:1267	arg1	pre-osteoblasts					1281:1295	MC3T3-E1 pre-osteoblasts	1272:1295	MC3T3-E1 pre-osteoblasts	1272:1295	Pharmacological inhibition of O-GlcNAcase (OGA), the enzyme responsible for the removal of O-GlcNAc from Ser/Thr residues, enhanced basal (39.9%) and BMP2/7-induced (43.3%) Runx2 transcriptional activity in MC3T3-E1 pre-osteoblasts.
25187572	3	110	theme	transfer	556:563	arg1	spectrometry					590:601	electron transfer dissociation tandem mass spectrometry	547:601	electron transfer dissociation tandem mass spectrometry	547:601	Characterization of Runx2 by electron transfer dissociation tandem mass spectrometry revealed sites of O-linked N-acetylglucosamine (O-GlcNAc) modification, a nutrient-responsive post-translational modification that modulates the action of numerous transcriptional effectors.
25187572	2	111	with	activity	377:384	arg1	proteins					475:482	chromatin remodeling proteins	454:482	chromatin remodeling proteins	454:482	The post-translational modification of Runx2 by phosphorylation, ubiquitinylation, and acetylation modulates its activity, stability, and interactions with transcriptional co-regulators and chromatin remodeling proteins downstream of osteogenic signals.
25187572	2	111	with	activity	377:384	arg1	co-regulators					436:448	transcriptional co-regulators	420:448	transcriptional co-regulators	420:448	The post-translational modification of Runx2 by phosphorylation, ubiquitinylation, and acetylation modulates its activity, stability, and interactions with transcriptional co-regulators and chromatin remodeling proteins downstream of osteogenic signals.
25187572	7	112	theme	OGA	1405:1407	arg1	inhibition					1391:1400	inhibition	1391:1400	inhibition of OGA	1391:1407	In bone marrow-derived mesenchymal stem cells differentiated for 6 days in osteogenic media, inhibition of OGA resulted in elevated expression (24.3%) and activity (65.8%) of alkaline phosphatase (ALP) an early marker of bone formation and a transcriptional target of Runx2.
25187572	8	113	theme	OGA	1707:1709	arg1	activity					1711:1718	decreased OGA activity	1697:1718	decreased OGA activity (39.0%)	1697:1726	Osteogenic differentiation of bone marrow-derived mesenchymal stem cells in the presence of BMP2/7 for 8 days culminated in decreased OGA activity (39.0%) and an increase in the abundance of O-GlcNAcylated Runx2, as compared with unstimulated cells.
25187572	8	113	theme	OGA	1707:1709	arg1	%					1725:1725	39.0%	1721:1725	39.0%	1721:1725	Osteogenic differentiation of bone marrow-derived mesenchymal stem cells in the presence of BMP2/7 for 8 days culminated in decreased OGA activity (39.0%) and an increase in the abundance of O-GlcNAcylated Runx2, as compared with unstimulated cells.
25187572	3	114	theme	transcriptional	767:781	arg1	effectors					783:791	numerous transcriptional effectors	758:791	numerous transcriptional effectors	758:791	Characterization of Runx2 by electron transfer dissociation tandem mass spectrometry revealed sites of O-linked N-acetylglucosamine (O-GlcNAc) modification, a nutrient-responsive post-translational modification that modulates the action of numerous transcriptional effectors.
25187572	2	115	with	stability	387:395	arg1	proteins					475:482	chromatin remodeling proteins	454:482	chromatin remodeling proteins	454:482	The post-translational modification of Runx2 by phosphorylation, ubiquitinylation, and acetylation modulates its activity, stability, and interactions with transcriptional co-regulators and chromatin remodeling proteins downstream of osteogenic signals.
25187572	2	115	with	stability	387:395	arg1	co-regulators					436:448	transcriptional co-regulators	420:448	transcriptional co-regulators	420:448	The post-translational modification of Runx2 by phosphorylation, ubiquitinylation, and acetylation modulates its activity, stability, and interactions with transcriptional co-regulators and chromatin remodeling proteins downstream of osteogenic signals.
25187572	10	116	theme	Runx2-dependent	2146:2160	arg1	regulation					2162:2171	the Runx2-dependent regulation	2142:2171	the Runx2-dependent regulation of the early ALP marker	2142:2195	Altogether, these findings link O-GlcNAc cycling to the Runx2-dependent regulation of the early ALP marker under osteoblast differentiation conditions.
25187572	1	117	theme	mineralized	242:252	arg1	skeleton					254:261	the mineralized skeleton	238:261	the mineralized skeleton	238:261	Runx2 is the master switch controlling osteoblast differentiation and formation of the mineralized skeleton.
28663241	3	0	theme	many	362:365	arg1	effects					383:389	many transcriptional effects	362:389	many transcriptional effects of O-GlcNAc transferase (OGT) inhibition	362:430	Unexpectedly, many transcriptional effects of O-GlcNAc transferase (OGT) inhibition were due to the activation of NRF2, the master regulator of redox stress tolerance.
28663241	3	0	theme	many	362:365	arg1	activation					448:457	the activation	444:457	the activation of NRF2, the master regulator of redox stress tolerance	444:513	Unexpectedly, many transcriptional effects of O-GlcNAc transferase (OGT) inhibition were due to the activation of NRF2, the master regulator of redox stress tolerance.
28663241	7	1	theme	future	1242:1247	arg1	approaches					1249:1258	future approaches	1242:1258	future approaches	1242:1258	Our results reveal a novel regulatory connection between nutrient-sensitive glycosylation and NRF2 signaling and provide a blueprint for future approaches to discover functionally important O-GlcNAcylation events on other KLHL family proteins in various experimental and disease contexts.
28663241	7	2	theme	novel	1126:1130	arg1	connection					1143:1152	a novel regulatory connection	1124:1152	a novel regulatory connection between nutrient-sensitive glycosylation and NRF2 signaling	1124:1212	Our results reveal a novel regulatory connection between nutrient-sensitive glycosylation and NRF2 signaling and provide a blueprint for future approaches to discover functionally important O-GlcNAcylation events on other KLHL family proteins in various experimental and disease contexts.
28663241	1	3	theme	biochemical	166:176	arg1	effects					193:199	its biochemical and phenotypic effects	162:199	its biochemical and phenotypic effects	162:199	O-GlcNAcylation is an essential, nutrient-sensitive post-translational modification, but its biochemical and phenotypic effects remain incompletely understood.
28663241	6	4	theme	glucose	989:995	arg1	fluctuations					997:1008	glucose fluctuations	989:1008	glucose fluctuations	989:1008	Interestingly, O-GlcNAc levels and NRF2 activation co-vary in response to glucose fluctuations, indicating that KEAP1 O-GlcNAcylation links nutrient sensing to downstream stress resistance.
28663241	3	5	theme	transcriptional	367:381	arg1	effects					383:389	many transcriptional effects	362:389	many transcriptional effects of O-GlcNAc transferase (OGT) inhibition	362:430	Unexpectedly, many transcriptional effects of O-GlcNAc transferase (OGT) inhibition were due to the activation of NRF2, the master regulator of redox stress tolerance.
28663241	3	5	theme	transcriptional	367:381	arg1	activation					448:457	the activation	444:457	the activation of NRF2, the master regulator of redox stress tolerance	444:513	Unexpectedly, many transcriptional effects of O-GlcNAc transferase (OGT) inhibition were due to the activation of NRF2, the master regulator of redox stress tolerance.
28663241	7	6	theme	regulatory	1132:1141	arg1	connection					1143:1152	a novel regulatory connection	1124:1152	a novel regulatory connection between nutrient-sensitive glycosylation and NRF2 signaling	1124:1212	Our results reveal a novel regulatory connection between nutrient-sensitive glycosylation and NRF2 signaling and provide a blueprint for future approaches to discover functionally important O-GlcNAcylation events on other KLHL family proteins in various experimental and disease contexts.
28663241	7	7	theme	important	1285:1293	arg1	events					1311:1316	functionally important O-GlcNAcylation events	1272:1316	functionally important O-GlcNAcylation events	1272:1316	Our results reveal a novel regulatory connection between nutrient-sensitive glycosylation and NRF2 signaling and provide a blueprint for future approaches to discover functionally important O-GlcNAcylation events on other KLHL family proteins in various experimental and disease contexts.
28663241	4	8	theme	NRF2	597:600	arg1	activation					602:611	NRF2 activation	597:611	NRF2 activation in multiple tumor expression datasets	597:649	Moreover, we found that a signature of low OGT activity strongly correlates with NRF2 activation in multiple tumor expression datasets.
28663241	5	9	theme	primary	728:734	arg1	regulator					745:753	the primary negative regulator	724:753	the primary negative regulator of NRF2	724:761	Guided by this information, we identified KEAP1 (also known as KLHL19), the primary negative regulator of NRF2, as a direct substrate of OGT We show that O-GlcNAcylation of KEAP1 at serine 104 is required for the efficient ubiquitination and degradation of NRF2.
28663241	5	9	theme	primary	728:734	arg1	KEAP1					694:698	KEAP1	694:698	KEAP1 (also known as KLHL19)	694:721	Guided by this information, we identified KEAP1 (also known as KLHL19), the primary negative regulator of NRF2, as a direct substrate of OGT We show that O-GlcNAcylation of KEAP1 at serine 104 is required for the efficient ubiquitination and degradation of NRF2.
28663241	7	10	theme	various	1351:1357	arg1	contexts					1384:1391	various experimental and disease contexts	1351:1391	various experimental and disease contexts	1351:1391	Our results reveal a novel regulatory connection between nutrient-sensitive glycosylation and NRF2 signaling and provide a blueprint for future approaches to discover functionally important O-GlcNAcylation events on other KLHL family proteins in various experimental and disease contexts.
28663241	7	11	theme	experimental	1359:1370	arg1	contexts					1384:1391	various experimental and disease contexts	1351:1391	various experimental and disease contexts	1351:1391	Our results reveal a novel regulatory connection between nutrient-sensitive glycosylation and NRF2 signaling and provide a blueprint for future approaches to discover functionally important O-GlcNAcylation events on other KLHL family proteins in various experimental and disease contexts.
28663241	4	12	theme	multiple	616:623	arg1	datasets					642:649	multiple tumor expression datasets	616:649	multiple tumor expression datasets	616:649	Moreover, we found that a signature of low OGT activity strongly correlates with NRF2 activation in multiple tumor expression datasets.
28663241	5	13	theme	negative	736:743	arg1	regulator					745:753	the primary negative regulator	724:753	the primary negative regulator of NRF2	724:761	Guided by this information, we identified KEAP1 (also known as KLHL19), the primary negative regulator of NRF2, as a direct substrate of OGT We show that O-GlcNAcylation of KEAP1 at serine 104 is required for the efficient ubiquitination and degradation of NRF2.
28663241	5	13	theme	negative	736:743	arg1	KEAP1					694:698	KEAP1	694:698	KEAP1 (also known as KLHL19)	694:721	Guided by this information, we identified KEAP1 (also known as KLHL19), the primary negative regulator of NRF2, as a direct substrate of OGT We show that O-GlcNAcylation of KEAP1 at serine 104 is required for the efficient ubiquitination and degradation of NRF2.
28663241	5	14	dep	show	796:799	arg1	Guided					652:657	Guided	652:657	Guided by this information	652:677	Guided by this information, we identified KEAP1 (also known as KLHL19), the primary negative regulator of NRF2, as a direct substrate of OGT We show that O-GlcNAcylation of KEAP1 at serine 104 is required for the efficient ubiquitination and degradation of NRF2.
28663241	3	15	theme	O-GlcNAc	394:401	arg1	transferase					403:413	O-GlcNAc transferase	394:413	O-GlcNAc transferase (OGT) inhibition	394:430	Unexpectedly, many transcriptional effects of O-GlcNAc transferase (OGT) inhibition were due to the activation of NRF2, the master regulator of redox stress tolerance.
28663241	3	15	theme	O-GlcNAc	394:401	arg1	OGT					416:418	OGT	416:418	OGT	416:418	Unexpectedly, many transcriptional effects of O-GlcNAc transferase (OGT) inhibition were due to the activation of NRF2, the master regulator of redox stress tolerance.
28663241	6	16	dep	fluctuations	997:1008	arg1	response					977:984	response	977:984	response	977:984	Interestingly, O-GlcNAc levels and NRF2 activation co-vary in response to glucose fluctuations, indicating that KEAP1 O-GlcNAcylation links nutrient sensing to downstream stress resistance.
28663241	5	17	theme	KEAP1	825:829	arg1	O-GlcNAcylation					806:820	O-GlcNAcylation	806:820	O-GlcNAcylation of KEAP1 at serine 104	806:843	Guided by this information, we identified KEAP1 (also known as KLHL19), the primary negative regulator of NRF2, as a direct substrate of OGT We show that O-GlcNAcylation of KEAP1 at serine 104 is required for the efficient ubiquitination and degradation of NRF2.
28663241	0	18	attach	links	23:27	arg2	Glycosylation					0:12	Glycosylation	0:12	Glycosylation of KEAP1	0:21	Glycosylation of KEAP1 links nutrient sensing to redox stress signaling.
28663241	0	18	attach	links	23:27	arg1	signaling					62:70	redox stress signaling	49:70	redox stress signaling	49:70	Glycosylation of KEAP1 links nutrient sensing to redox stress signaling.
28663241	5	19	theme	NRF2	909:912	arg1	ubiquitination					875:888	efficient ubiquitination	865:888	efficient ubiquitination	865:888	Guided by this information, we identified KEAP1 (also known as KLHL19), the primary negative regulator of NRF2, as a direct substrate of OGT We show that O-GlcNAcylation of KEAP1 at serine 104 is required for the efficient ubiquitination and degradation of NRF2.
28663241	5	19	theme	NRF2	909:912	arg1	degradation					894:904	degradation	894:904	degradation	894:904	Guided by this information, we identified KEAP1 (also known as KLHL19), the primary negative regulator of NRF2, as a direct substrate of OGT We show that O-GlcNAcylation of KEAP1 at serine 104 is required for the efficient ubiquitination and degradation of NRF2.
28663241	1	20	theme	phenotypic	182:191	arg1	effects					193:199	its biochemical and phenotypic effects	162:199	its biochemical and phenotypic effects	162:199	O-GlcNAcylation is an essential, nutrient-sensitive post-translational modification, but its biochemical and phenotypic effects remain incompletely understood.
28663241	3	21	theme	transferase	403:413	arg1	inhibition					421:430	O-GlcNAc transferase (OGT) inhibition	394:430	O-GlcNAc transferase (OGT) inhibition	394:430	Unexpectedly, many transcriptional effects of O-GlcNAc transferase (OGT) inhibition were due to the activation of NRF2, the master regulator of redox stress tolerance.
28663241	7	22	theme	nutrient-sensitive	1162:1179	arg1	glycosylation					1181:1193	nutrient-sensitive glycosylation	1162:1193	nutrient-sensitive glycosylation	1162:1193	Our results reveal a novel regulatory connection between nutrient-sensitive glycosylation and NRF2 signaling and provide a blueprint for future approaches to discover functionally important O-GlcNAcylation events on other KLHL family proteins in various experimental and disease contexts.
28663241	3	23	theme	master	472:477	arg1	NRF2					462:465	NRF2	462:465	NRF2	462:465	Unexpectedly, many transcriptional effects of O-GlcNAc transferase (OGT) inhibition were due to the activation of NRF2, the master regulator of redox stress tolerance.
28663241	3	23	theme	master	472:477	arg1	regulator					479:487	the master regulator	468:487	the master regulator of redox stress tolerance	468:513	Unexpectedly, many transcriptional effects of O-GlcNAc transferase (OGT) inhibition were due to the activation of NRF2, the master regulator of redox stress tolerance.
28663241	6	24	theme	stress	1086:1091	arg1	resistance					1093:1102	downstream stress resistance	1075:1102	downstream stress resistance	1075:1102	Interestingly, O-GlcNAc levels and NRF2 activation co-vary in response to glucose fluctuations, indicating that KEAP1 O-GlcNAcylation links nutrient sensing to downstream stress resistance.
28663241	5	25	dep	ubiquitination	875:888	arg1	the					861:863	the	861:863	the	861:863	Guided by this information, we identified KEAP1 (also known as KLHL19), the primary negative regulator of NRF2, as a direct substrate of OGT We show that O-GlcNAcylation of KEAP1 at serine 104 is required for the efficient ubiquitination and degradation of NRF2.
28663241	3	26	theme	NRF2	462:465	arg1	effects					383:389	many transcriptional effects	362:389	many transcriptional effects of O-GlcNAc transferase (OGT) inhibition	362:430	Unexpectedly, many transcriptional effects of O-GlcNAc transferase (OGT) inhibition were due to the activation of NRF2, the master regulator of redox stress tolerance.
28663241	3	26	theme	NRF2	462:465	arg1	activation					448:457	the activation	444:457	the activation of NRF2, the master regulator of redox stress tolerance	444:513	Unexpectedly, many transcriptional effects of O-GlcNAc transferase (OGT) inhibition were due to the activation of NRF2, the master regulator of redox stress tolerance.
28663241	5	27	dep	KEAP1	694:698	arg1	known					706:710	known	706:710	known as KLHL19	706:720	Guided by this information, we identified KEAP1 (also known as KLHL19), the primary negative regulator of NRF2, as a direct substrate of OGT We show that O-GlcNAcylation of KEAP1 at serine 104 is required for the efficient ubiquitination and degradation of NRF2.
28663241	4	28	from	activation	602:611	arg1	datasets					642:649	multiple tumor expression datasets	616:649	multiple tumor expression datasets	616:649	Moreover, we found that a signature of low OGT activity strongly correlates with NRF2 activation in multiple tumor expression datasets.
28663241	4	29	theme	activity	563:570	arg1	signature					542:550	a signature	540:550	a signature of low OGT activity	540:570	Moreover, we found that a signature of low OGT activity strongly correlates with NRF2 activation in multiple tumor expression datasets.
28663241	1	30	theme	essential	95:103	arg1	modification					144:155	an essential, nutrient-sensitive post-translational modification	92:155	an essential, nutrient-sensitive post-translational modification	92:155	O-GlcNAcylation is an essential, nutrient-sensitive post-translational modification, but its biochemical and phenotypic effects remain incompletely understood.
28663241	1	30	theme	essential	95:103	arg1	O-GlcNAcylation					73:87	O-GlcNAcylation	73:87	O-GlcNAcylation	73:87	O-GlcNAcylation is an essential, nutrient-sensitive post-translational modification, but its biochemical and phenotypic effects remain incompletely understood.
28663241	6	31	theme	downstream	1075:1084	arg1	resistance					1093:1102	downstream stress resistance	1075:1102	downstream stress resistance	1075:1102	Interestingly, O-GlcNAc levels and NRF2 activation co-vary in response to glucose fluctuations, indicating that KEAP1 O-GlcNAcylation links nutrient sensing to downstream stress resistance.
28663241	3	32	theme	redox	492:496	arg1	tolerance					505:513	redox stress tolerance	492:513	redox stress tolerance	492:513	Unexpectedly, many transcriptional effects of O-GlcNAc transferase (OGT) inhibition were due to the activation of NRF2, the master regulator of redox stress tolerance.
28663241	3	33	theme	inhibition	421:430	arg1	effects					383:389	many transcriptional effects	362:389	many transcriptional effects of O-GlcNAc transferase (OGT) inhibition	362:430	Unexpectedly, many transcriptional effects of O-GlcNAc transferase (OGT) inhibition were due to the activation of NRF2, the master regulator of redox stress tolerance.
28663241	3	33	theme	inhibition	421:430	arg1	activation					448:457	the activation	444:457	the activation of NRF2, the master regulator of redox stress tolerance	444:513	Unexpectedly, many transcriptional effects of O-GlcNAc transferase (OGT) inhibition were due to the activation of NRF2, the master regulator of redox stress tolerance.
28663241	6	34	theme	NRF2	950:953	arg1	activation					955:964	NRF2 activation	950:964	NRF2 activation	950:964	Interestingly, O-GlcNAc levels and NRF2 activation co-vary in response to glucose fluctuations, indicating that KEAP1 O-GlcNAcylation links nutrient sensing to downstream stress resistance.
28663241	3	35	theme	stress	498:503	arg1	tolerance					505:513	redox stress tolerance	492:513	redox stress tolerance	492:513	Unexpectedly, many transcriptional effects of O-GlcNAc transferase (OGT) inhibition were due to the activation of NRF2, the master regulator of redox stress tolerance.
28663241	5	36	theme	direct	769:774	arg1	substrate					776:784	a direct substrate	767:784	a direct substrate of OGT	767:791	Guided by this information, we identified KEAP1 (also known as KLHL19), the primary negative regulator of NRF2, as a direct substrate of OGT We show that O-GlcNAcylation of KEAP1 at serine 104 is required for the efficient ubiquitination and degradation of NRF2.
28663241	5	36	theme	direct	769:774	arg1	KEAP1					694:698	KEAP1	694:698	KEAP1 (also known as KLHL19)	694:721	Guided by this information, we identified KEAP1 (also known as KLHL19), the primary negative regulator of NRF2, as a direct substrate of OGT We show that O-GlcNAcylation of KEAP1 at serine 104 is required for the efficient ubiquitination and degradation of NRF2.
28663241	7	37	theme	family	1332:1337	arg1	proteins					1339:1346	other KLHL family proteins	1321:1346	other KLHL family proteins in various experimental and disease contexts	1321:1391	Our results reveal a novel regulatory connection between nutrient-sensitive glycosylation and NRF2 signaling and provide a blueprint for future approaches to discover functionally important O-GlcNAcylation events on other KLHL family proteins in various experimental and disease contexts.
28663241	7	38	theme	O-GlcNAcylation	1295:1309	arg1	events					1311:1316	functionally important O-GlcNAcylation events	1272:1316	functionally important O-GlcNAcylation events	1272:1316	Our results reveal a novel regulatory connection between nutrient-sensitive glycosylation and NRF2 signaling and provide a blueprint for future approaches to discover functionally important O-GlcNAcylation events on other KLHL family proteins in various experimental and disease contexts.
28663241	0	39	gly	Glycosylation	0:12	arg1	KEAP1					17:21	KEAP1	17:21	KEAP1	17:21	Glycosylation of KEAP1 links nutrient sensing to redox stress signaling.
28663241	7	40	theme	disease	1376:1382	arg1	contexts					1384:1391	various experimental and disease contexts	1351:1391	various experimental and disease contexts	1351:1391	Our results reveal a novel regulatory connection between nutrient-sensitive glycosylation and NRF2 signaling and provide a blueprint for future approaches to discover functionally important O-GlcNAcylation events on other KLHL family proteins in various experimental and disease contexts.
28663241	0	41	theme	nutrient	29:36	arg1	sensing					38:44	nutrient sensing	29:44	nutrient sensing	29:44	Glycosylation of KEAP1 links nutrient sensing to redox stress signaling.
28663241	7	42	from	proteins	1339:1346	arg1	contexts					1384:1391	various experimental and disease contexts	1351:1391	various experimental and disease contexts	1351:1391	Our results reveal a novel regulatory connection between nutrient-sensitive glycosylation and NRF2 signaling and provide a blueprint for future approaches to discover functionally important O-GlcNAcylation events on other KLHL family proteins in various experimental and disease contexts.
28663241	6	43	theme	KEAP1	1027:1031	arg1	O-GlcNAcylation					1033:1047	KEAP1 O-GlcNAcylation	1027:1047	KEAP1 O-GlcNAcylation	1027:1047	Interestingly, O-GlcNAc levels and NRF2 activation co-vary in response to glucose fluctuations, indicating that KEAP1 O-GlcNAcylation links nutrient sensing to downstream stress resistance.
28663241	0	44	theme	redox	49:53	arg1	signaling					62:70	redox stress signaling	49:70	redox stress signaling	49:70	Glycosylation of KEAP1 links nutrient sensing to redox stress signaling.
28663241	5	45	dep	known	706:710	arg1	also					701:704	also	701:704	also	701:704	Guided by this information, we identified KEAP1 (also known as KLHL19), the primary negative regulator of NRF2, as a direct substrate of OGT We show that O-GlcNAcylation of KEAP1 at serine 104 is required for the efficient ubiquitination and degradation of NRF2.
28663241	5	46	from	serine	834:839	arg1	O-GlcNAcylation					806:820	O-GlcNAcylation	806:820	O-GlcNAcylation of KEAP1 at serine 104	806:843	Guided by this information, we identified KEAP1 (also known as KLHL19), the primary negative regulator of NRF2, as a direct substrate of OGT We show that O-GlcNAcylation of KEAP1 at serine 104 is required for the efficient ubiquitination and degradation of NRF2.
28663241	7	47	theme	KLHL	1327:1330	arg1	proteins					1339:1346	other KLHL family proteins	1321:1346	other KLHL family proteins in various experimental and disease contexts	1321:1391	Our results reveal a novel regulatory connection between nutrient-sensitive glycosylation and NRF2 signaling and provide a blueprint for future approaches to discover functionally important O-GlcNAcylation events on other KLHL family proteins in various experimental and disease contexts.
28663241	5	48	theme	OGT	789:791	arg1	substrate					776:784	a direct substrate	767:784	a direct substrate of OGT	767:791	Guided by this information, we identified KEAP1 (also known as KLHL19), the primary negative regulator of NRF2, as a direct substrate of OGT We show that O-GlcNAcylation of KEAP1 at serine 104 is required for the efficient ubiquitination and degradation of NRF2.
28663241	5	48	theme	OGT	789:791	arg1	KEAP1					694:698	KEAP1	694:698	KEAP1 (also known as KLHL19)	694:721	Guided by this information, we identified KEAP1 (also known as KLHL19), the primary negative regulator of NRF2, as a direct substrate of OGT We show that O-GlcNAcylation of KEAP1 at serine 104 is required for the efficient ubiquitination and degradation of NRF2.
28663241	4	49	theme	OGT	559:561	arg1	activity					563:570	low OGT activity	555:570	low OGT activity	555:570	Moreover, we found that a signature of low OGT activity strongly correlates with NRF2 activation in multiple tumor expression datasets.
28663241	7	50	theme	NRF2	1199:1202	arg1	signaling					1204:1212	NRF2 signaling	1199:1212	NRF2 signaling	1199:1212	Our results reveal a novel regulatory connection between nutrient-sensitive glycosylation and NRF2 signaling and provide a blueprint for future approaches to discover functionally important O-GlcNAcylation events on other KLHL family proteins in various experimental and disease contexts.
28663241	1	51	theme	post-translational	125:142	arg1	modification					144:155	an essential, nutrient-sensitive post-translational modification	92:155	an essential, nutrient-sensitive post-translational modification	92:155	O-GlcNAcylation is an essential, nutrient-sensitive post-translational modification, but its biochemical and phenotypic effects remain incompletely understood.
28663241	1	51	theme	post-translational	125:142	arg1	O-GlcNAcylation					73:87	O-GlcNAcylation	73:87	O-GlcNAcylation	73:87	O-GlcNAcylation is an essential, nutrient-sensitive post-translational modification, but its biochemical and phenotypic effects remain incompletely understood.
28663241	4	52	theme	low	555:557	arg1	activity					563:570	low OGT activity	555:570	low OGT activity	555:570	Moreover, we found that a signature of low OGT activity strongly correlates with NRF2 activation in multiple tumor expression datasets.
28663241	2	53	theme	transcriptional	286:300	arg1	response					302:309	the global transcriptional response	275:309	the global transcriptional response to perturbations in O-GlcNAcylation	275:345	To address this question, we investigated the global transcriptional response to perturbations in O-GlcNAcylation.
28663241	3	54	theme	tolerance	505:513	arg1	NRF2					462:465	NRF2	462:465	NRF2	462:465	Unexpectedly, many transcriptional effects of O-GlcNAc transferase (OGT) inhibition were due to the activation of NRF2, the master regulator of redox stress tolerance.
28663241	3	54	theme	tolerance	505:513	arg1	regulator					479:487	the master regulator	468:487	the master regulator of redox stress tolerance	468:513	Unexpectedly, many transcriptional effects of O-GlcNAc transferase (OGT) inhibition were due to the activation of NRF2, the master regulator of redox stress tolerance.
28663241	4	55	theme	expression	631:640	arg1	datasets					642:649	multiple tumor expression datasets	616:649	multiple tumor expression datasets	616:649	Moreover, we found that a signature of low OGT activity strongly correlates with NRF2 activation in multiple tumor expression datasets.
28663241	2	56	theme	global	279:284	arg1	response					302:309	the global transcriptional response	275:309	the global transcriptional response to perturbations in O-GlcNAcylation	275:345	To address this question, we investigated the global transcriptional response to perturbations in O-GlcNAcylation.
28663241	7	57	theme	other	1321:1325	arg1	proteins					1339:1346	other KLHL family proteins	1321:1346	other KLHL family proteins in various experimental and disease contexts	1321:1391	Our results reveal a novel regulatory connection between nutrient-sensitive glycosylation and NRF2 signaling and provide a blueprint for future approaches to discover functionally important O-GlcNAcylation events on other KLHL family proteins in various experimental and disease contexts.
28663241	4	58	theme	tumor	625:629	arg1	datasets					642:649	multiple tumor expression datasets	616:649	multiple tumor expression datasets	616:649	Moreover, we found that a signature of low OGT activity strongly correlates with NRF2 activation in multiple tumor expression datasets.
28663241	5	59	theme	NRF2	758:761	arg1	regulator					745:753	the primary negative regulator	724:753	the primary negative regulator of NRF2	724:761	Guided by this information, we identified KEAP1 (also known as KLHL19), the primary negative regulator of NRF2, as a direct substrate of OGT We show that O-GlcNAcylation of KEAP1 at serine 104 is required for the efficient ubiquitination and degradation of NRF2.
28663241	5	59	theme	NRF2	758:761	arg1	KEAP1					694:698	KEAP1	694:698	KEAP1 (also known as KLHL19)	694:721	Guided by this information, we identified KEAP1 (also known as KLHL19), the primary negative regulator of NRF2, as a direct substrate of OGT We show that O-GlcNAcylation of KEAP1 at serine 104 is required for the efficient ubiquitination and degradation of NRF2.
28663241	6	60	theme	nutrient	1055:1062	arg1	sensing					1064:1070	nutrient sensing	1055:1070	nutrient sensing	1055:1070	Interestingly, O-GlcNAc levels and NRF2 activation co-vary in response to glucose fluctuations, indicating that KEAP1 O-GlcNAcylation links nutrient sensing to downstream stress resistance.
28663241	1	61	dep	essential	95:103	arg1	nutrient-sensitive					106:123	nutrient-sensitive	106:123	nutrient-sensitive	106:123	O-GlcNAcylation is an essential, nutrient-sensitive post-translational modification, but its biochemical and phenotypic effects remain incompletely understood.
28663241	2	62	from	perturbations	314:326	arg1	O-GlcNAcylation					331:345	O-GlcNAcylation	331:345	O-GlcNAcylation	331:345	To address this question, we investigated the global transcriptional response to perturbations in O-GlcNAcylation.
28663241	0	63	theme	stress	55:60	arg1	signaling					62:70	redox stress signaling	49:70	redox stress signaling	49:70	Glycosylation of KEAP1 links nutrient sensing to redox stress signaling.
28663241	6	64	attach	links	1049:1053	arg1	resistance					1093:1102	downstream stress resistance	1075:1102	downstream stress resistance	1075:1102	Interestingly, O-GlcNAc levels and NRF2 activation co-vary in response to glucose fluctuations, indicating that KEAP1 O-GlcNAcylation links nutrient sensing to downstream stress resistance.
28663241	6	64	attach	links	1049:1053	arg2	O-GlcNAcylation					1033:1047	KEAP1 O-GlcNAcylation	1027:1047	KEAP1 O-GlcNAcylation	1027:1047	Interestingly, O-GlcNAc levels and NRF2 activation co-vary in response to glucose fluctuations, indicating that KEAP1 O-GlcNAcylation links nutrient sensing to downstream stress resistance.
28663241	0	65	theme	KEAP1	17:21	arg1	Glycosylation					0:12	Glycosylation	0:12	Glycosylation of KEAP1	0:21	Glycosylation of KEAP1 links nutrient sensing to redox stress signaling.
28663241	5	66	theme	efficient	865:873	arg1	ubiquitination					875:888	efficient ubiquitination	865:888	efficient ubiquitination	865:888	Guided by this information, we identified KEAP1 (also known as KLHL19), the primary negative regulator of NRF2, as a direct substrate of OGT We show that O-GlcNAcylation of KEAP1 at serine 104 is required for the efficient ubiquitination and degradation of NRF2.
28663241	6	67	theme	O-GlcNAc	930:937	arg1	levels					939:944	O-GlcNAc levels	930:944	O-GlcNAc levels	930:944	Interestingly, O-GlcNAc levels and NRF2 activation co-vary in response to glucose fluctuations, indicating that KEAP1 O-GlcNAcylation links nutrient sensing to downstream stress resistance.
22307082	4	0	theme	site-specific	626:638	arg1	antibody					640:647	a novel O-GlcNAc site-specific antibody	609:647	a novel O-GlcNAc site-specific antibody	609:647	With the help of a novel O-GlcNAc site-specific antibody, we demonstrate that O-GlcNAcylation of TAB1 is induced by IL-1 and osmotic stress, known inducers of the TAK1 signalling cascade.
22307082	1	1	theme	key	132:134	arg1	kinase					161:166	a key serine/threonine protein kinase	130:166	a key serine/threonine protein kinase that mediates signals transduced by pro-inflammatory cytokines such as transforming growth factor-β, tumour necrosis factor (TNF), interleukin-1 (IL-1) and wnt family ligands	130:341	Transforming growth factor (TGF)-β-activated kinase 1 (TAK1) is a key serine/threonine protein kinase that mediates signals transduced by pro-inflammatory cytokines such as transforming growth factor-β, tumour necrosis factor (TNF), interleukin-1 (IL-1) and wnt family ligands.
22307082	1	1	theme	key	132:134	arg1	kinase					111:116	Transforming growth factor (TGF)-β-activated kinase 1	66:118	Transforming growth factor (TGF)-β-activated kinase 1 (TAK1)	66:125	Transforming growth factor (TGF)-β-activated kinase 1 (TAK1) is a key serine/threonine protein kinase that mediates signals transduced by pro-inflammatory cytokines such as transforming growth factor-β, tumour necrosis factor (TNF), interleukin-1 (IL-1) and wnt family ligands.
22307082	1	2	theme	growth	252:257	arg1	TNF					293:295	TNF	293:295	TNF	293:295	Transforming growth factor (TGF)-β-activated kinase 1 (TAK1) is a key serine/threonine protein kinase that mediates signals transduced by pro-inflammatory cytokines such as transforming growth factor-β, tumour necrosis factor (TNF), interleukin-1 (IL-1) and wnt family ligands.
22307082	1	2	theme	growth	252:257	arg1	factor					285:290	transforming growth factor-β, tumour necrosis factor	239:290	factor	285:290	Transforming growth factor (TGF)-β-activated kinase 1 (TAK1) is a key serine/threonine protein kinase that mediates signals transduced by pro-inflammatory cytokines such as transforming growth factor-β, tumour necrosis factor (TNF), interleukin-1 (IL-1) and wnt family ligands.
22307082	2	3	with	complex	361:367	arg1	partners					382:389	binding partners TAB1-3	374:396	binding partners TAB1-3	374:396	TAK1 is found in complex with binding partners TAB1-3, phosphorylation and ubiquitination of which has been found to regulate TAK1 activity.
22307082	1	4	theme	serine/threonine	136:151	arg1	kinase					161:166	a key serine/threonine protein kinase	130:166	a key serine/threonine protein kinase that mediates signals transduced by pro-inflammatory cytokines such as transforming growth factor-β, tumour necrosis factor (TNF), interleukin-1 (IL-1) and wnt family ligands	130:341	Transforming growth factor (TGF)-β-activated kinase 1 (TAK1) is a key serine/threonine protein kinase that mediates signals transduced by pro-inflammatory cytokines such as transforming growth factor-β, tumour necrosis factor (TNF), interleukin-1 (IL-1) and wnt family ligands.
22307082	1	4	theme	serine/threonine	136:151	arg1	kinase					111:116	Transforming growth factor (TGF)-β-activated kinase 1	66:118	Transforming growth factor (TGF)-β-activated kinase 1 (TAK1)	66:125	Transforming growth factor (TGF)-β-activated kinase 1 (TAK1) is a key serine/threonine protein kinase that mediates signals transduced by pro-inflammatory cytokines such as transforming growth factor-β, tumour necrosis factor (TNF), interleukin-1 (IL-1) and wnt family ligands.
22307082	1	5	theme	factor-β	259:266	arg1	TNF					293:295	TNF	293:295	TNF	293:295	Transforming growth factor (TGF)-β-activated kinase 1 (TAK1) is a key serine/threonine protein kinase that mediates signals transduced by pro-inflammatory cytokines such as transforming growth factor-β, tumour necrosis factor (TNF), interleukin-1 (IL-1) and wnt family ligands.
22307082	1	5	theme	factor-β	259:266	arg1	factor					285:290	transforming growth factor-β, tumour necrosis factor	239:290	factor	285:290	Transforming growth factor (TGF)-β-activated kinase 1 (TAK1) is a key serine/threonine protein kinase that mediates signals transduced by pro-inflammatory cytokines such as transforming growth factor-β, tumour necrosis factor (TNF), interleukin-1 (IL-1) and wnt family ligands.
22307082	1	6	theme	wnt	324:326	arg1	ligands					335:341	wnt family ligands	324:341	wnt family ligands	324:341	Transforming growth factor (TGF)-β-activated kinase 1 (TAK1) is a key serine/threonine protein kinase that mediates signals transduced by pro-inflammatory cytokines such as transforming growth factor-β, tumour necrosis factor (TNF), interleukin-1 (IL-1) and wnt family ligands.
22307082	1	7	theme	Transforming	66:77	arg1	TAK1					121:124	TAK1	121:124	TAK1	121:124	Transforming growth factor (TGF)-β-activated kinase 1 (TAK1) is a key serine/threonine protein kinase that mediates signals transduced by pro-inflammatory cytokines such as transforming growth factor-β, tumour necrosis factor (TNF), interleukin-1 (IL-1) and wnt family ligands.
22307082	1	7	theme	Transforming	66:77	arg1	kinase					161:166	a key serine/threonine protein kinase	130:166	a key serine/threonine protein kinase that mediates signals transduced by pro-inflammatory cytokines such as transforming growth factor-β, tumour necrosis factor (TNF), interleukin-1 (IL-1) and wnt family ligands	130:341	Transforming growth factor (TGF)-β-activated kinase 1 (TAK1) is a key serine/threonine protein kinase that mediates signals transduced by pro-inflammatory cytokines such as transforming growth factor-β, tumour necrosis factor (TNF), interleukin-1 (IL-1) and wnt family ligands.
22307082	1	7	theme	Transforming	66:77	arg1	kinase					111:116	Transforming growth factor (TGF)-β-activated kinase 1	66:118	Transforming growth factor (TGF)-β-activated kinase 1 (TAK1)	66:125	Transforming growth factor (TGF)-β-activated kinase 1 (TAK1) is a key serine/threonine protein kinase that mediates signals transduced by pro-inflammatory cytokines such as transforming growth factor-β, tumour necrosis factor (TNF), interleukin-1 (IL-1) and wnt family ligands.
22307082	6	8	theme	examples	1132:1139	arg1	one					1115:1117	one	1115:1117	one	1115:1117	This is one of the first examples of a single O-GlcNAc site on a signalling protein modulating a key innate immunity signalling pathway.
22307082	6	8	theme	examples	1132:1139	arg1	examples					1132:1139	the first examples	1122:1139	the first examples of a single O-GlcNAc site on a signalling protein modulating a key innate immunity signalling pathway	1122:1241	This is one of the first examples of a single O-GlcNAc site on a signalling protein modulating a key innate immunity signalling pathway.
22307082	5	9	theme	Tab1	857:860	arg1	fibroblasts					883:893	Tab1(-/-) mouse embryonic fibroblasts	857:893	Tab1(-/-) mouse embryonic fibroblasts	857:893	By reintroducing wild-type or an O-GlcNAc-deficient mutant TAB1 (S395A) into Tab1(-/-) mouse embryonic fibroblasts, we determined that O-GlcNAcylation of TAB1 is required for full TAK1 activation upon stimulation with IL-1/osmotic stress, for downstream activation of nuclear factor κB and finally production of IL-6 and TNFα.
22307082	1	10	theme	family	328:333	arg1	ligands					335:341	wnt family ligands	324:341	wnt family ligands	324:341	Transforming growth factor (TGF)-β-activated kinase 1 (TAK1) is a key serine/threonine protein kinase that mediates signals transduced by pro-inflammatory cytokines such as transforming growth factor-β, tumour necrosis factor (TNF), interleukin-1 (IL-1) and wnt family ligands.
22307082	5	11	theme	embryonic	873:881	arg1	fibroblasts					883:893	Tab1(-/-) mouse embryonic fibroblasts	857:893	Tab1(-/-) mouse embryonic fibroblasts	857:893	By reintroducing wild-type or an O-GlcNAc-deficient mutant TAB1 (S395A) into Tab1(-/-) mouse embryonic fibroblasts, we determined that O-GlcNAcylation of TAB1 is required for full TAK1 activation upon stimulation with IL-1/osmotic stress, for downstream activation of nuclear factor κB and finally production of IL-6 and TNFα.
22307082	6	12	theme	site	1162:1165	arg1	examples					1132:1139	the first examples	1122:1139	the first examples of a single O-GlcNAc site on a signalling protein modulating a key innate immunity signalling pathway	1122:1241	This is one of the first examples of a single O-GlcNAc site on a signalling protein modulating a key innate immunity signalling pathway.
22307082	1	13	theme	growth	79:84	arg1	TAK1					121:124	TAK1	121:124	TAK1	121:124	Transforming growth factor (TGF)-β-activated kinase 1 (TAK1) is a key serine/threonine protein kinase that mediates signals transduced by pro-inflammatory cytokines such as transforming growth factor-β, tumour necrosis factor (TNF), interleukin-1 (IL-1) and wnt family ligands.
22307082	1	13	theme	growth	79:84	arg1	kinase					161:166	a key serine/threonine protein kinase	130:166	a key serine/threonine protein kinase that mediates signals transduced by pro-inflammatory cytokines such as transforming growth factor-β, tumour necrosis factor (TNF), interleukin-1 (IL-1) and wnt family ligands	130:341	Transforming growth factor (TGF)-β-activated kinase 1 (TAK1) is a key serine/threonine protein kinase that mediates signals transduced by pro-inflammatory cytokines such as transforming growth factor-β, tumour necrosis factor (TNF), interleukin-1 (IL-1) and wnt family ligands.
22307082	1	13	theme	growth	79:84	arg1	kinase					111:116	Transforming growth factor (TGF)-β-activated kinase 1	66:118	Transforming growth factor (TGF)-β-activated kinase 1 (TAK1)	66:125	Transforming growth factor (TGF)-β-activated kinase 1 (TAK1) is a key serine/threonine protein kinase that mediates signals transduced by pro-inflammatory cytokines such as transforming growth factor-β, tumour necrosis factor (TNF), interleukin-1 (IL-1) and wnt family ligands.
22307082	4	14	theme	signalling	760:769	arg1	cascade					771:777	the TAK1 signalling cascade	751:777	the TAK1 signalling cascade	751:777	With the help of a novel O-GlcNAc site-specific antibody, we demonstrate that O-GlcNAcylation of TAB1 is induced by IL-1 and osmotic stress, known inducers of the TAK1 signalling cascade.
22307082	1	15	theme	factor	86:91	arg1	TAK1					121:124	TAK1	121:124	TAK1	121:124	Transforming growth factor (TGF)-β-activated kinase 1 (TAK1) is a key serine/threonine protein kinase that mediates signals transduced by pro-inflammatory cytokines such as transforming growth factor-β, tumour necrosis factor (TNF), interleukin-1 (IL-1) and wnt family ligands.
22307082	1	15	theme	factor	86:91	arg1	kinase					161:166	a key serine/threonine protein kinase	130:166	a key serine/threonine protein kinase that mediates signals transduced by pro-inflammatory cytokines such as transforming growth factor-β, tumour necrosis factor (TNF), interleukin-1 (IL-1) and wnt family ligands	130:341	Transforming growth factor (TGF)-β-activated kinase 1 (TAK1) is a key serine/threonine protein kinase that mediates signals transduced by pro-inflammatory cytokines such as transforming growth factor-β, tumour necrosis factor (TNF), interleukin-1 (IL-1) and wnt family ligands.
22307082	1	15	theme	factor	86:91	arg1	kinase					111:116	Transforming growth factor (TGF)-β-activated kinase 1	66:118	Transforming growth factor (TGF)-β-activated kinase 1 (TAK1)	66:125	Transforming growth factor (TGF)-β-activated kinase 1 (TAK1) is a key serine/threonine protein kinase that mediates signals transduced by pro-inflammatory cytokines such as transforming growth factor-β, tumour necrosis factor (TNF), interleukin-1 (IL-1) and wnt family ligands.
22307082	6	16	theme	signalling	1172:1181	arg1	protein					1183:1189	a signalling protein	1170:1189	a signalling protein modulating a key innate immunity signalling pathway	1170:1241	This is one of the first examples of a single O-GlcNAc site on a signalling protein modulating a key innate immunity signalling pathway.
22307082	1	17	theme	protein	153:159	arg1	kinase					161:166	a key serine/threonine protein kinase	130:166	a key serine/threonine protein kinase that mediates signals transduced by pro-inflammatory cytokines such as transforming growth factor-β, tumour necrosis factor (TNF), interleukin-1 (IL-1) and wnt family ligands	130:341	Transforming growth factor (TGF)-β-activated kinase 1 (TAK1) is a key serine/threonine protein kinase that mediates signals transduced by pro-inflammatory cytokines such as transforming growth factor-β, tumour necrosis factor (TNF), interleukin-1 (IL-1) and wnt family ligands.
22307082	1	17	theme	protein	153:159	arg1	kinase					111:116	Transforming growth factor (TGF)-β-activated kinase 1	66:118	Transforming growth factor (TGF)-β-activated kinase 1 (TAK1)	66:125	Transforming growth factor (TGF)-β-activated kinase 1 (TAK1) is a key serine/threonine protein kinase that mediates signals transduced by pro-inflammatory cytokines such as transforming growth factor-β, tumour necrosis factor (TNF), interleukin-1 (IL-1) and wnt family ligands.
22307082	4	18	theme	TAK1	755:758	arg1	cascade					771:777	the TAK1 signalling cascade	751:777	the TAK1 signalling cascade	751:777	With the help of a novel O-GlcNAc site-specific antibody, we demonstrate that O-GlcNAcylation of TAB1 is induced by IL-1 and osmotic stress, known inducers of the TAK1 signalling cascade.
22307082	5	19	dep	wild-type	797:805	arg1	S395A					845:849	S395A	845:849	S395A	845:849	By reintroducing wild-type or an O-GlcNAc-deficient mutant TAB1 (S395A) into Tab1(-/-) mouse embryonic fibroblasts, we determined that O-GlcNAcylation of TAB1 is required for full TAK1 activation upon stimulation with IL-1/osmotic stress, for downstream activation of nuclear factor κB and finally production of IL-6 and TNFα.
22307082	5	19	dep	wild-type	797:805	arg1	TAB1					839:842	TAB1	839:842	TAB1 (S395A)	839:850	By reintroducing wild-type or an O-GlcNAc-deficient mutant TAB1 (S395A) into Tab1(-/-) mouse embryonic fibroblasts, we determined that O-GlcNAcylation of TAB1 is required for full TAK1 activation upon stimulation with IL-1/osmotic stress, for downstream activation of nuclear factor κB and finally production of IL-6 and TNFα.
22307082	5	20	theme	downstream	1023:1032	arg1	activation					1034:1043	downstream activation	1023:1043	downstream activation of nuclear factor κB	1023:1064	By reintroducing wild-type or an O-GlcNAc-deficient mutant TAB1 (S395A) into Tab1(-/-) mouse embryonic fibroblasts, we determined that O-GlcNAcylation of TAB1 is required for full TAK1 activation upon stimulation with IL-1/osmotic stress, for downstream activation of nuclear factor κB and finally production of IL-6 and TNFα.
22307082	1	21	theme	TGF	94:96	arg1	TAK1					121:124	TAK1	121:124	TAK1	121:124	Transforming growth factor (TGF)-β-activated kinase 1 (TAK1) is a key serine/threonine protein kinase that mediates signals transduced by pro-inflammatory cytokines such as transforming growth factor-β, tumour necrosis factor (TNF), interleukin-1 (IL-1) and wnt family ligands.
22307082	1	21	theme	TGF	94:96	arg1	kinase					161:166	a key serine/threonine protein kinase	130:166	a key serine/threonine protein kinase that mediates signals transduced by pro-inflammatory cytokines such as transforming growth factor-β, tumour necrosis factor (TNF), interleukin-1 (IL-1) and wnt family ligands	130:341	Transforming growth factor (TGF)-β-activated kinase 1 (TAK1) is a key serine/threonine protein kinase that mediates signals transduced by pro-inflammatory cytokines such as transforming growth factor-β, tumour necrosis factor (TNF), interleukin-1 (IL-1) and wnt family ligands.
22307082	1	21	theme	TGF	94:96	arg1	kinase					111:116	Transforming growth factor (TGF)-β-activated kinase 1	66:118	Transforming growth factor (TGF)-β-activated kinase 1 (TAK1)	66:125	Transforming growth factor (TGF)-β-activated kinase 1 (TAK1) is a key serine/threonine protein kinase that mediates signals transduced by pro-inflammatory cytokines such as transforming growth factor-β, tumour necrosis factor (TNF), interleukin-1 (IL-1) and wnt family ligands.
22307082	5	22	theme	nuclear	1048:1054	arg1	κB					1063:1064	nuclear factor κB	1048:1064	nuclear factor κB	1048:1064	By reintroducing wild-type or an O-GlcNAc-deficient mutant TAB1 (S395A) into Tab1(-/-) mouse embryonic fibroblasts, we determined that O-GlcNAcylation of TAB1 is required for full TAK1 activation upon stimulation with IL-1/osmotic stress, for downstream activation of nuclear factor κB and finally production of IL-6 and TNFα.
22307082	1	23	theme	necrosis	276:283	arg1	TNF					293:295	TNF	293:295	TNF	293:295	Transforming growth factor (TGF)-β-activated kinase 1 (TAK1) is a key serine/threonine protein kinase that mediates signals transduced by pro-inflammatory cytokines such as transforming growth factor-β, tumour necrosis factor (TNF), interleukin-1 (IL-1) and wnt family ligands.
22307082	1	23	theme	necrosis	276:283	arg1	factor					285:290	transforming growth factor-β, tumour necrosis factor	239:290	factor	285:290	Transforming growth factor (TGF)-β-activated kinase 1 (TAK1) is a key serine/threonine protein kinase that mediates signals transduced by pro-inflammatory cytokines such as transforming growth factor-β, tumour necrosis factor (TNF), interleukin-1 (IL-1) and wnt family ligands.
22307082	4	24	theme	cascade	771:777	arg1	inducers					739:746	known inducers	733:746	known inducers of the TAK1 signalling cascade	733:777	With the help of a novel O-GlcNAc site-specific antibody, we demonstrate that O-GlcNAcylation of TAB1 is induced by IL-1 and osmotic stress, known inducers of the TAK1 signalling cascade.
22307082	4	24	theme	cascade	771:777	arg1	IL-1					708:711	IL-1	708:711	IL-1	708:711	With the help of a novel O-GlcNAc site-specific antibody, we demonstrate that O-GlcNAcylation of TAB1 is induced by IL-1 and osmotic stress, known inducers of the TAK1 signalling cascade.
22307082	6	25	theme	O-GlcNAc	1153:1160	arg1	site					1162:1165	a single O-GlcNAc site	1144:1165	a single O-GlcNAc site on a signalling protein modulating a key innate immunity signalling pathway	1144:1241	This is one of the first examples of a single O-GlcNAc site on a signalling protein modulating a key innate immunity signalling pathway.
22307082	5	26	theme	IL-6	1092:1095	arg1	production					1078:1087	finally production	1070:1087	finally production of IL-6 and TNFα	1070:1104	By reintroducing wild-type or an O-GlcNAc-deficient mutant TAB1 (S395A) into Tab1(-/-) mouse embryonic fibroblasts, we determined that O-GlcNAcylation of TAB1 is required for full TAK1 activation upon stimulation with IL-1/osmotic stress, for downstream activation of nuclear factor κB and finally production of IL-6 and TNFα.
22307082	5	26	theme	IL-6	1092:1095	arg1	activation					1034:1043	downstream activation	1023:1043	downstream activation of nuclear factor κB	1023:1064	By reintroducing wild-type or an O-GlcNAc-deficient mutant TAB1 (S395A) into Tab1(-/-) mouse embryonic fibroblasts, we determined that O-GlcNAcylation of TAB1 is required for full TAK1 activation upon stimulation with IL-1/osmotic stress, for downstream activation of nuclear factor κB and finally production of IL-6 and TNFα.
22307082	1	27	theme	-β-activated	98:109	arg1	TAK1					121:124	TAK1	121:124	TAK1	121:124	Transforming growth factor (TGF)-β-activated kinase 1 (TAK1) is a key serine/threonine protein kinase that mediates signals transduced by pro-inflammatory cytokines such as transforming growth factor-β, tumour necrosis factor (TNF), interleukin-1 (IL-1) and wnt family ligands.
22307082	1	27	theme	-β-activated	98:109	arg1	kinase					161:166	a key serine/threonine protein kinase	130:166	a key serine/threonine protein kinase that mediates signals transduced by pro-inflammatory cytokines such as transforming growth factor-β, tumour necrosis factor (TNF), interleukin-1 (IL-1) and wnt family ligands	130:341	Transforming growth factor (TGF)-β-activated kinase 1 (TAK1) is a key serine/threonine protein kinase that mediates signals transduced by pro-inflammatory cytokines such as transforming growth factor-β, tumour necrosis factor (TNF), interleukin-1 (IL-1) and wnt family ligands.
22307082	1	27	theme	-β-activated	98:109	arg1	kinase					111:116	Transforming growth factor (TGF)-β-activated kinase 1	66:118	Transforming growth factor (TGF)-β-activated kinase 1 (TAK1)	66:125	Transforming growth factor (TGF)-β-activated kinase 1 (TAK1) is a key serine/threonine protein kinase that mediates signals transduced by pro-inflammatory cytokines such as transforming growth factor-β, tumour necrosis factor (TNF), interleukin-1 (IL-1) and wnt family ligands.
22307082	3	28	from	N-acetylglucosamine	535:553	arg1	Ser395					584:589	Ser395	584:589	Ser395	584:589	In this study, we show that TAB1 is modified with N-acetylglucosamine (O-GlcNAc) on a single site, Ser395.
22307082	3	28	from	N-acetylglucosamine	535:553	arg1	site					578:581	a single site	569:581	a single site	569:581	In this study, we show that TAB1 is modified with N-acetylglucosamine (O-GlcNAc) on a single site, Ser395.
22307082	5	29	theme	mouse	867:871	arg1	fibroblasts					883:893	Tab1(-/-) mouse embryonic fibroblasts	857:893	Tab1(-/-) mouse embryonic fibroblasts	857:893	By reintroducing wild-type or an O-GlcNAc-deficient mutant TAB1 (S395A) into Tab1(-/-) mouse embryonic fibroblasts, we determined that O-GlcNAcylation of TAB1 is required for full TAK1 activation upon stimulation with IL-1/osmotic stress, for downstream activation of nuclear factor κB and finally production of IL-6 and TNFα.
22307082	0	30	theme	TAB1	19:22	arg1	O-GlcNAcylation					0:14	O-GlcNAcylation	0:14	O-GlcNAcylation of TAB1	0:22	O-GlcNAcylation of TAB1 modulates TAK1-mediated cytokine release.
22307082	6	31	theme	signalling	1224:1233	arg1	pathway					1235:1241	a key innate immunity signalling pathway	1202:1241	a key innate immunity signalling pathway	1202:1241	This is one of the first examples of a single O-GlcNAc site on a signalling protein modulating a key innate immunity signalling pathway.
22307082	5	32	theme	-/-	862:864	arg1	fibroblasts					883:893	Tab1(-/-) mouse embryonic fibroblasts	857:893	Tab1(-/-) mouse embryonic fibroblasts	857:893	By reintroducing wild-type or an O-GlcNAc-deficient mutant TAB1 (S395A) into Tab1(-/-) mouse embryonic fibroblasts, we determined that O-GlcNAcylation of TAB1 is required for full TAK1 activation upon stimulation with IL-1/osmotic stress, for downstream activation of nuclear factor κB and finally production of IL-6 and TNFα.
22307082	4	33	theme	O-GlcNAc	617:624	arg1	antibody					640:647	a novel O-GlcNAc site-specific antibody	609:647	a novel O-GlcNAc site-specific antibody	609:647	With the help of a novel O-GlcNAc site-specific antibody, we demonstrate that O-GlcNAcylation of TAB1 is induced by IL-1 and osmotic stress, known inducers of the TAK1 signalling cascade.
22307082	2	34	theme	partners	382:389	arg1	ubiquitination					419:432	ubiquitination	419:432	ubiquitination	419:432	TAK1 is found in complex with binding partners TAB1-3, phosphorylation and ubiquitination of which has been found to regulate TAK1 activity.
22307082	2	34	theme	partners	382:389	arg1	phosphorylation					399:413	phosphorylation	399:413	phosphorylation	399:413	TAK1 is found in complex with binding partners TAB1-3, phosphorylation and ubiquitination of which has been found to regulate TAK1 activity.
22307082	0	35	theme	cytokine	48:55	arg1	release					57:63	TAK1-mediated cytokine release	34:63	TAK1-mediated cytokine release	34:63	O-GlcNAcylation of TAB1 modulates TAK1-mediated cytokine release.
22307082	5	36	theme	TNFα	1101:1104	arg1	production					1078:1087	finally production	1070:1087	finally production of IL-6 and TNFα	1070:1104	By reintroducing wild-type or an O-GlcNAc-deficient mutant TAB1 (S395A) into Tab1(-/-) mouse embryonic fibroblasts, we determined that O-GlcNAcylation of TAB1 is required for full TAK1 activation upon stimulation with IL-1/osmotic stress, for downstream activation of nuclear factor κB and finally production of IL-6 and TNFα.
22307082	5	36	theme	TNFα	1101:1104	arg1	activation					1034:1043	downstream activation	1023:1043	downstream activation of nuclear factor κB	1023:1064	By reintroducing wild-type or an O-GlcNAc-deficient mutant TAB1 (S395A) into Tab1(-/-) mouse embryonic fibroblasts, we determined that O-GlcNAcylation of TAB1 is required for full TAK1 activation upon stimulation with IL-1/osmotic stress, for downstream activation of nuclear factor κB and finally production of IL-6 and TNFα.
22307082	6	37	theme	immunity	1215:1222	arg1	pathway					1235:1241	a key innate immunity signalling pathway	1202:1241	a key innate immunity signalling pathway	1202:1241	This is one of the first examples of a single O-GlcNAc site on a signalling protein modulating a key innate immunity signalling pathway.
22307082	5	38	theme	factor	1056:1061	arg1	κB					1063:1064	nuclear factor κB	1048:1064	nuclear factor κB	1048:1064	By reintroducing wild-type or an O-GlcNAc-deficient mutant TAB1 (S395A) into Tab1(-/-) mouse embryonic fibroblasts, we determined that O-GlcNAcylation of TAB1 is required for full TAK1 activation upon stimulation with IL-1/osmotic stress, for downstream activation of nuclear factor κB and finally production of IL-6 and TNFα.
22307082	5	39	with	stimulation	981:991	arg1	stress					1011:1016	IL-1/osmotic stress	998:1016	IL-1/osmotic stress	998:1016	By reintroducing wild-type or an O-GlcNAc-deficient mutant TAB1 (S395A) into Tab1(-/-) mouse embryonic fibroblasts, we determined that O-GlcNAcylation of TAB1 is required for full TAK1 activation upon stimulation with IL-1/osmotic stress, for downstream activation of nuclear factor κB and finally production of IL-6 and TNFα.
22307082	2	40	theme	binding	374:380	arg1	partners					382:389	binding partners TAB1-3	374:396	binding partners TAB1-3	374:396	TAK1 is found in complex with binding partners TAB1-3, phosphorylation and ubiquitination of which has been found to regulate TAK1 activity.
22307082	0	41	theme	TAK1-mediated	34:46	arg1	release					57:63	TAK1-mediated cytokine release	34:63	TAK1-mediated cytokine release	34:63	O-GlcNAcylation of TAB1 modulates TAK1-mediated cytokine release.
22307082	5	42	theme	κB	1063:1064	arg1	production					1078:1087	finally production	1070:1087	finally production of IL-6 and TNFα	1070:1104	By reintroducing wild-type or an O-GlcNAc-deficient mutant TAB1 (S395A) into Tab1(-/-) mouse embryonic fibroblasts, we determined that O-GlcNAcylation of TAB1 is required for full TAK1 activation upon stimulation with IL-1/osmotic stress, for downstream activation of nuclear factor κB and finally production of IL-6 and TNFα.
22307082	5	42	theme	κB	1063:1064	arg1	activation					1034:1043	downstream activation	1023:1043	downstream activation of nuclear factor κB	1023:1064	By reintroducing wild-type or an O-GlcNAc-deficient mutant TAB1 (S395A) into Tab1(-/-) mouse embryonic fibroblasts, we determined that O-GlcNAcylation of TAB1 is required for full TAK1 activation upon stimulation with IL-1/osmotic stress, for downstream activation of nuclear factor κB and finally production of IL-6 and TNFα.
22307082	6	43	theme	innate	1208:1213	arg1	immunity					1215:1222	innate immunity	1208:1222	a key innate immunity signalling pathway	1202:1241	This is one of the first examples of a single O-GlcNAc site on a signalling protein modulating a key innate immunity signalling pathway.
22307082	4	44	theme	known	733:737	arg1	inducers					739:746	known inducers	733:746	known inducers of the TAK1 signalling cascade	733:777	With the help of a novel O-GlcNAc site-specific antibody, we demonstrate that O-GlcNAcylation of TAB1 is induced by IL-1 and osmotic stress, known inducers of the TAK1 signalling cascade.
22307082	4	44	theme	known	733:737	arg1	IL-1					708:711	IL-1	708:711	IL-1	708:711	With the help of a novel O-GlcNAc site-specific antibody, we demonstrate that O-GlcNAcylation of TAB1 is induced by IL-1 and osmotic stress, known inducers of the TAK1 signalling cascade.
22307082	1	45	theme	pro-inflammatory	204:219	arg1	ligands					335:341	wnt family ligands	324:341	wnt family ligands	324:341	Transforming growth factor (TGF)-β-activated kinase 1 (TAK1) is a key serine/threonine protein kinase that mediates signals transduced by pro-inflammatory cytokines such as transforming growth factor-β, tumour necrosis factor (TNF), interleukin-1 (IL-1) and wnt family ligands.
22307082	1	45	theme	pro-inflammatory	204:219	arg1	cytokines					221:229	pro-inflammatory cytokines	204:229	pro-inflammatory cytokines such as transforming growth factor-β, tumour necrosis factor (TNF), interleukin-1 (IL-1) and wnt family ligands	204:341	Transforming growth factor (TGF)-β-activated kinase 1 (TAK1) is a key serine/threonine protein kinase that mediates signals transduced by pro-inflammatory cytokines such as transforming growth factor-β, tumour necrosis factor (TNF), interleukin-1 (IL-1) and wnt family ligands.
22307082	1	45	theme	pro-inflammatory	204:219	arg1	interleukin-1					299:311	interleukin-1	299:311	interleukin-1 (IL-1)	299:318	Transforming growth factor (TGF)-β-activated kinase 1 (TAK1) is a key serine/threonine protein kinase that mediates signals transduced by pro-inflammatory cytokines such as transforming growth factor-β, tumour necrosis factor (TNF), interleukin-1 (IL-1) and wnt family ligands.
22307082	1	45	theme	pro-inflammatory	204:219	arg1	factor					285:290	transforming growth factor-β, tumour necrosis factor	239:290	factor	285:290	Transforming growth factor (TGF)-β-activated kinase 1 (TAK1) is a key serine/threonine protein kinase that mediates signals transduced by pro-inflammatory cytokines such as transforming growth factor-β, tumour necrosis factor (TNF), interleukin-1 (IL-1) and wnt family ligands.
22307082	6	46	from	protein	1183:1189	arg1	examples					1132:1139	the first examples	1122:1139	the first examples of a single O-GlcNAc site on a signalling protein modulating a key innate immunity signalling pathway	1122:1241	This is one of the first examples of a single O-GlcNAc site on a signalling protein modulating a key innate immunity signalling pathway.
22307082	6	47	theme	key	1204:1206	arg1	pathway					1235:1241	a key innate immunity signalling pathway	1202:1241	a key innate immunity signalling pathway	1202:1241	This is one of the first examples of a single O-GlcNAc site on a signalling protein modulating a key innate immunity signalling pathway.
22307082	5	48	theme	IL-1/osmotic	998:1009	arg1	stress					1011:1016	IL-1/osmotic stress	998:1016	IL-1/osmotic stress	998:1016	By reintroducing wild-type or an O-GlcNAc-deficient mutant TAB1 (S395A) into Tab1(-/-) mouse embryonic fibroblasts, we determined that O-GlcNAcylation of TAB1 is required for full TAK1 activation upon stimulation with IL-1/osmotic stress, for downstream activation of nuclear factor κB and finally production of IL-6 and TNFα.
22307082	3	49	mod	modified	521:528	arg1	TAB1					513:516	TAB1	513:516	TAB1	513:516	In this study, we show that TAB1 is modified with N-acetylglucosamine (O-GlcNAc) on a single site, Ser395.
22307082	3	49	mod	modified	521:528	arg3	N-acetylglucosamine					535:553	N-acetylglucosamine	535:553	N-acetylglucosamine (O-GlcNAc) on a single site, Ser395	535:589	In this study, we show that TAB1 is modified with N-acetylglucosamine (O-GlcNAc) on a single site, Ser395.
22307082	3	49	mod	modified	521:528	arg3	O-GlcNAc					556:563	O-GlcNAc	556:563	O-GlcNAc	556:563	In this study, we show that TAB1 is modified with N-acetylglucosamine (O-GlcNAc) on a single site, Ser395.
22307082	1	50	dep	factor	285:290	arg1	tumour					269:274	transforming growth factor-β, tumour necrosis factor	239:290	tumour	269:274	Transforming growth factor (TGF)-β-activated kinase 1 (TAK1) is a key serine/threonine protein kinase that mediates signals transduced by pro-inflammatory cytokines such as transforming growth factor-β, tumour necrosis factor (TNF), interleukin-1 (IL-1) and wnt family ligands.
22307082	6	51	theme	first	1126:1130	arg1	examples					1132:1139	the first examples	1122:1139	the first examples of a single O-GlcNAc site on a signalling protein modulating a key innate immunity signalling pathway	1122:1241	This is one of the first examples of a single O-GlcNAc site on a signalling protein modulating a key innate immunity signalling pathway.
22307082	6	52	theme	single	1146:1151	arg1	site					1162:1165	a single O-GlcNAc site	1144:1165	a single O-GlcNAc site on a signalling protein modulating a key innate immunity signalling pathway	1144:1241	This is one of the first examples of a single O-GlcNAc site on a signalling protein modulating a key innate immunity signalling pathway.
22307082	5	53	theme	full	955:958	arg1	activation					965:974	full TAK1 activation	955:974	full TAK1 activation upon stimulation with IL-1/osmotic stress	955:1016	By reintroducing wild-type or an O-GlcNAc-deficient mutant TAB1 (S395A) into Tab1(-/-) mouse embryonic fibroblasts, we determined that O-GlcNAcylation of TAB1 is required for full TAK1 activation upon stimulation with IL-1/osmotic stress, for downstream activation of nuclear factor κB and finally production of IL-6 and TNFα.
22307082	4	54	theme	osmotic	717:723	arg1	stress					725:730	osmotic stress	717:730	osmotic stress	717:730	With the help of a novel O-GlcNAc site-specific antibody, we demonstrate that O-GlcNAcylation of TAB1 is induced by IL-1 and osmotic stress, known inducers of the TAK1 signalling cascade.
22307082	5	55	theme	TAB1	934:937	arg1	O-GlcNAcylation					915:929	O-GlcNAcylation	915:929	O-GlcNAcylation of TAB1	915:937	By reintroducing wild-type or an O-GlcNAc-deficient mutant TAB1 (S395A) into Tab1(-/-) mouse embryonic fibroblasts, we determined that O-GlcNAcylation of TAB1 is required for full TAK1 activation upon stimulation with IL-1/osmotic stress, for downstream activation of nuclear factor κB and finally production of IL-6 and TNFα.
22307082	4	56	theme	TAB1	689:692	arg1	O-GlcNAcylation					670:684	O-GlcNAcylation	670:684	O-GlcNAcylation of TAB1	670:692	With the help of a novel O-GlcNAc site-specific antibody, we demonstrate that O-GlcNAcylation of TAB1 is induced by IL-1 and osmotic stress, known inducers of the TAK1 signalling cascade.
22307082	5	57	theme	TAK1	960:963	arg1	activation					965:974	full TAK1 activation	955:974	full TAK1 activation upon stimulation with IL-1/osmotic stress	955:1016	By reintroducing wild-type or an O-GlcNAc-deficient mutant TAB1 (S395A) into Tab1(-/-) mouse embryonic fibroblasts, we determined that O-GlcNAcylation of TAB1 is required for full TAK1 activation upon stimulation with IL-1/osmotic stress, for downstream activation of nuclear factor κB and finally production of IL-6 and TNFα.
22307082	3	58	theme	single	571:576	arg1	Ser395					584:589	Ser395	584:589	Ser395	584:589	In this study, we show that TAB1 is modified with N-acetylglucosamine (O-GlcNAc) on a single site, Ser395.
22307082	3	58	theme	single	571:576	arg1	site					578:581	a single site	569:581	a single site	569:581	In this study, we show that TAB1 is modified with N-acetylglucosamine (O-GlcNAc) on a single site, Ser395.
22307082	6	59	from	examples	1132:1139	arg1	protein					1183:1189	a signalling protein	1170:1189	a signalling protein modulating a key innate immunity signalling pathway	1170:1241	This is one of the first examples of a single O-GlcNAc site on a signalling protein modulating a key innate immunity signalling pathway.
22307082	6	60	from	site	1162:1165	arg1	protein					1183:1189	a signalling protein	1170:1189	a signalling protein modulating a key innate immunity signalling pathway	1170:1241	This is one of the first examples of a single O-GlcNAc site on a signalling protein modulating a key innate immunity signalling pathway.
22307082	2	61	theme	TAK1	470:473	arg1	activity					475:482	TAK1 activity	470:482	TAK1 activity	470:482	TAK1 is found in complex with binding partners TAB1-3, phosphorylation and ubiquitination of which has been found to regulate TAK1 activity.
22307082	2	62	located	found	352:356	arg2	TAK1					344:347	TAK1	344:347	TAK1	344:347	TAK1 is found in complex with binding partners TAB1-3, phosphorylation and ubiquitination of which has been found to regulate TAK1 activity.
22307082	2	62	located	found	352:356	arg1	complex					361:367	complex	361:367	complex with binding partners TAB1-3, phosphorylation and ubiquitination of which has been found to regulate TAK1 activity	361:482	TAK1 is found in complex with binding partners TAB1-3, phosphorylation and ubiquitination of which has been found to regulate TAK1 activity.
22307082	4	63	dep	the	597:599	arg1	help					601:604	help	601:604	help	601:604	With the help of a novel O-GlcNAc site-specific antibody, we demonstrate that O-GlcNAcylation of TAB1 is induced by IL-1 and osmotic stress, known inducers of the TAK1 signalling cascade.
22307082	4	64	theme	novel	611:615	arg1	antibody					640:647	a novel O-GlcNAc site-specific antibody	609:647	a novel O-GlcNAc site-specific antibody	609:647	With the help of a novel O-GlcNAc site-specific antibody, we demonstrate that O-GlcNAcylation of TAB1 is induced by IL-1 and osmotic stress, known inducers of the TAK1 signalling cascade.
22307082	5	65	theme	O-GlcNAc-deficient	813:830	arg1	mutant					832:837	an O-GlcNAc-deficient mutant	810:837	an O-GlcNAc-deficient mutant	810:837	By reintroducing wild-type or an O-GlcNAc-deficient mutant TAB1 (S395A) into Tab1(-/-) mouse embryonic fibroblasts, we determined that O-GlcNAcylation of TAB1 is required for full TAK1 activation upon stimulation with IL-1/osmotic stress, for downstream activation of nuclear factor κB and finally production of IL-6 and TNFα.
22307082	1	66	theme	transforming	239:250	arg1	TNF					293:295	TNF	293:295	TNF	293:295	Transforming growth factor (TGF)-β-activated kinase 1 (TAK1) is a key serine/threonine protein kinase that mediates signals transduced by pro-inflammatory cytokines such as transforming growth factor-β, tumour necrosis factor (TNF), interleukin-1 (IL-1) and wnt family ligands.
22307082	1	66	theme	transforming	239:250	arg1	factor					285:290	transforming growth factor-β, tumour necrosis factor	239:290	factor	285:290	Transforming growth factor (TGF)-β-activated kinase 1 (TAK1) is a key serine/threonine protein kinase that mediates signals transduced by pro-inflammatory cytokines such as transforming growth factor-β, tumour necrosis factor (TNF), interleukin-1 (IL-1) and wnt family ligands.
20829364	0	0	theme	rat	94:96	arg1	cells					115:119	rat insulinoma INS-1 cells	94:119	rat insulinoma INS-1 cells	94:119	Glucosamine treatment-mediated O-GlcNAc modification of paxillin depends on adhesion state of rat insulinoma INS-1 cells.
20829364	5	1	mod	modified	955:962	arg1	Ser-84/85					912:920	Ser-84/85	912:920	Ser-84/85 in human paxillin	912:938	Ser-84/85 in human paxillin appeared to be modified by O-GlcNAc, which was inversely correlated to Ser-85 phosphorylation (Ser-83 in rat paxillin).
20829364	5	1	mod	modified	955:962	arg3	O-GlcNAc					967:974	O-GlcNAc	967:974	O-GlcNAc	967:974	Ser-84/85 in human paxillin appeared to be modified by O-GlcNAc, which was inversely correlated to Ser-85 phosphorylation (Ser-83 in rat paxillin).
20829364	5	2	from	Ser-84/85	912:920	arg1	paxillin					931:938	human paxillin	925:938	human paxillin	925:938	Ser-84/85 in human paxillin appeared to be modified by O-GlcNAc, which was inversely correlated to Ser-85 phosphorylation (Ser-83 in rat paxillin).
20829364	1	3	theme	focal	182:186	arg1	adhesions					188:196	focal adhesions	182:196	focal adhesions	182:196	Protein-protein interactions and/or signaling activities at focal adhesions, where integrin-mediated adhesion to extracellular matrix occurs, are critical for the regulation of adhesion-dependent cellular functions.
20829364	4	4	theme	INS-1	818:822	arg1	cells					824:828	INS-1 cells	818:828	INS-1 cells treated with GlcN	818:846	We found that paxillin, a key adaptor molecule in focal adhesions, could be modified by O-GlcNAc in INS-1 cells treated with GlcN and in pancreatic islets from mice treated with streptozotocin.
20829364	4	5	mod	modified	794:801	arg3	O-GlcNAc					806:813	O-GlcNAc	806:813	O-GlcNAc	806:813	We found that paxillin, a key adaptor molecule in focal adhesions, could be modified by O-GlcNAc in INS-1 cells treated with GlcN and in pancreatic islets from mice treated with streptozotocin.
20829364	4	5	mod	modified	794:801	arg1	molecule					756:763	a key adaptor molecule	742:763	a key adaptor molecule in focal adhesions	742:782	We found that paxillin, a key adaptor molecule in focal adhesions, could be modified by O-GlcNAc in INS-1 cells treated with GlcN and in pancreatic islets from mice treated with streptozotocin.
20829364	4	5	mod	modified	794:801	arg1	paxillin					732:739	paxillin	732:739	paxillin	732:739	We found that paxillin, a key adaptor molecule in focal adhesions, could be modified by O-GlcNAc in INS-1 cells treated with GlcN and in pancreatic islets from mice treated with streptozotocin.
20829364	4	6	theme	adaptor	748:754	arg1	molecule					756:763	a key adaptor molecule	742:763	a key adaptor molecule in focal adhesions	742:782	We found that paxillin, a key adaptor molecule in focal adhesions, could be modified by O-GlcNAc in INS-1 cells treated with GlcN and in pancreatic islets from mice treated with streptozotocin.
20829364	4	6	theme	adaptor	748:754	arg1	paxillin					732:739	paxillin	732:739	paxillin	732:739	We found that paxillin, a key adaptor molecule in focal adhesions, could be modified by O-GlcNAc in INS-1 cells treated with GlcN and in pancreatic islets from mice treated with streptozotocin.
20829364	9	7	theme	modification	1600:1611	arg1	virtue					1577:1582	virtue	1577:1582	virtue of the O-GlcNAc modification of paxillin, which can be antagonized by a persistent cell adhesion process	1577:1687	Together these observations suggest that murine pancreatic β cells may have restricted actin organization upon GlcN treatment by virtue of the O-GlcNAc modification of paxillin, which can be antagonized by a persistent cell adhesion process.
20829364	9	8	theme	restricted	1524:1533	arg1	organization					1541:1552	restricted actin organization	1524:1552	restricted actin organization	1524:1552	Together these observations suggest that murine pancreatic β cells may have restricted actin organization upon GlcN treatment by virtue of the O-GlcNAc modification of paxillin, which can be antagonized by a persistent cell adhesion process.
20829364	0	9	theme	INS-1	109:113	arg1	cells					115:119	rat insulinoma INS-1 cells	94:119	rat insulinoma INS-1 cells	94:119	Glucosamine treatment-mediated O-GlcNAc modification of paxillin depends on adhesion state of rat insulinoma INS-1 cells.
20829364	1	10	from	adhesions	188:196	arg1	interactions					138:149	Protein-protein interactions	122:149	Protein-protein interactions	122:149	Protein-protein interactions and/or signaling activities at focal adhesions, where integrin-mediated adhesion to extracellular matrix occurs, are critical for the regulation of adhesion-dependent cellular functions.
20829364	9	11	theme	persistent	1656:1665	arg1	process					1681:1687	a persistent cell adhesion process	1654:1687	a persistent cell adhesion process	1654:1687	Together these observations suggest that murine pancreatic β cells may have restricted actin organization upon GlcN treatment by virtue of the O-GlcNAc modification of paxillin, which can be antagonized by a persistent cell adhesion process.
20829364	9	12	theme	actin	1535:1539	arg1	organization					1541:1552	restricted actin organization	1524:1552	restricted actin organization	1524:1552	Together these observations suggest that murine pancreatic β cells may have restricted actin organization upon GlcN treatment by virtue of the O-GlcNAc modification of paxillin, which can be antagonized by a persistent cell adhesion process.
20829364	0	13	theme	insulinoma	98:107	arg1	cells					115:119	rat insulinoma INS-1 cells	94:119	rat insulinoma INS-1 cells	94:119	Glucosamine treatment-mediated O-GlcNAc modification of paxillin depends on adhesion state of rat insulinoma INS-1 cells.
20829364	5	14	theme	Ser-85	1011:1016	arg1	phosphorylation					1018:1032	Ser-85 phosphorylation	1011:1032	Ser-85 phosphorylation (Ser-83 in rat paxillin)	1011:1057	Ser-84/85 in human paxillin appeared to be modified by O-GlcNAc, which was inversely correlated to Ser-85 phosphorylation (Ser-83 in rat paxillin).
20829364	3	15	from	effects	580:586	arg1	morphology					641:650	morphology	641:650	morphology	641:650	We investigated the effects of O-GlcNAc modification on actin reorganization and morphology of rat insulinoma INS-1 cells after glucosamine (GlcN) treatment.
20829364	3	15	from	effects	580:586	arg1	reorganization					622:635	actin reorganization	616:635	actin reorganization	616:635	We investigated the effects of O-GlcNAc modification on actin reorganization and morphology of rat insulinoma INS-1 cells after glucosamine (GlcN) treatment.
20829364	3	16	theme	actin	616:620	arg1	reorganization					622:635	actin reorganization	616:635	actin reorganization	616:635	We investigated the effects of O-GlcNAc modification on actin reorganization and morphology of rat insulinoma INS-1 cells after glucosamine (GlcN) treatment.
20829364	1	17	theme	adhesion-dependent	299:316	arg1	functions					327:335	adhesion-dependent cellular functions	299:335	adhesion-dependent cellular functions	299:335	Protein-protein interactions and/or signaling activities at focal adhesions, where integrin-mediated adhesion to extracellular matrix occurs, are critical for the regulation of adhesion-dependent cellular functions.
20829364	7	18	theme	active	1271:1276	arg1	protrusions					1278:1288	active protrusions	1271:1288	active protrusions for multiple-elongated morphologies	1271:1324	Adherent INS-1 cells treated with GlcN showed restricted protrusions, whereas untreated cells showed active protrusions for multiple-elongated morphologies.
20829364	2	19	theme	molecules	400:408	arg1	phosphorylation					351:365	the phosphorylation and activities	347:380	phosphorylation	351:365	Although the phosphorylation and activities of focal adhesion molecules have been intensively studied, the effects of the O-GlcNAc modification of their Ser/Thr residues on cellular functions have been largely unexplored.
20829364	2	19	theme	molecules	400:408	arg1	activities					371:380	the phosphorylation and activities	347:380	activities	371:380	Although the phosphorylation and activities of focal adhesion molecules have been intensively studied, the effects of the O-GlcNAc modification of their Ser/Thr residues on cellular functions have been largely unexplored.
20829364	7	20	theme	Adherent	1170:1177	arg1	cells					1185:1189	Adherent INS-1 cells	1170:1189	Adherent INS-1 cells treated with GlcN	1170:1207	Adherent INS-1 cells treated with GlcN showed restricted protrusions, whereas untreated cells showed active protrusions for multiple-elongated morphologies.
20829364	2	21	theme	modification	469:480	arg1	effects					445:451	the effects	441:451	the effects of the O-GlcNAc modification of their Ser/Thr residues on cellular functions	441:528	Although the phosphorylation and activities of focal adhesion molecules have been intensively studied, the effects of the O-GlcNAc modification of their Ser/Thr residues on cellular functions have been largely unexplored.
20829364	3	22	theme	O-GlcNAc	591:598	arg1	modification					600:611	O-GlcNAc modification	591:611	O-GlcNAc modification	591:611	We investigated the effects of O-GlcNAc modification on actin reorganization and morphology of rat insulinoma INS-1 cells after glucosamine (GlcN) treatment.
20829364	6	23	theme	O-GlcNAc	1135:1142	arg1	modification					1144:1155	the GlcN treatment-enhanced O-GlcNAc modification	1107:1155	the GlcN treatment-enhanced O-GlcNAc modification of paxillin	1107:1167	Integrin-mediated adhesion signaling inhibited the GlcN treatment-enhanced O-GlcNAc modification of paxillin.
20829364	0	24	theme	cells	115:119	arg1	state					85:89	adhesion state	76:89	adhesion state of rat insulinoma INS-1 cells	76:119	Glucosamine treatment-mediated O-GlcNAc modification of paxillin depends on adhesion state of rat insulinoma INS-1 cells.
20829364	8	25	theme	further	1412:1418	arg1	restriction					1420:1430	no further restriction	1409:1430	no further restriction of protrusions	1409:1445	Upon GlcN treatment, expression of a triple mutation (S83A/S84A/S85A) resulted in no further restriction of protrusions.
20829364	7	26	theme	INS-1	1179:1183	arg1	cells					1185:1189	Adherent INS-1 cells	1170:1189	Adherent INS-1 cells treated with GlcN	1170:1207	Adherent INS-1 cells treated with GlcN showed restricted protrusions, whereas untreated cells showed active protrusions for multiple-elongated morphologies.
20829364	2	27	theme	residues	499:506	arg1	modification					469:480	the O-GlcNAc modification	456:480	the O-GlcNAc modification of their Ser/Thr residues	456:506	Although the phosphorylation and activities of focal adhesion molecules have been intensively studied, the effects of the O-GlcNAc modification of their Ser/Thr residues on cellular functions have been largely unexplored.
20829364	5	28	from	Ser-83	1035:1040	arg1	paxillin					1049:1056	rat paxillin	1045:1056	rat paxillin	1045:1056	Ser-84/85 in human paxillin appeared to be modified by O-GlcNAc, which was inversely correlated to Ser-85 phosphorylation (Ser-83 in rat paxillin).
20829364	9	29	theme	GlcN	1559:1562	arg1	treatment					1564:1572	GlcN treatment	1559:1572	GlcN treatment	1559:1572	Together these observations suggest that murine pancreatic β cells may have restricted actin organization upon GlcN treatment by virtue of the O-GlcNAc modification of paxillin, which can be antagonized by a persistent cell adhesion process.
20829364	0	30	theme	treatment-mediated	12:29	arg1	modification					40:51	Glucosamine treatment-mediated O-GlcNAc modification	0:51	Glucosamine treatment-mediated O-GlcNAc modification of paxillin	0:63	Glucosamine treatment-mediated O-GlcNAc modification of paxillin depends on adhesion state of rat insulinoma INS-1 cells.
20829364	4	31	from	mice	878:881	arg1	islets					866:871	pancreatic islets	855:871	pancreatic islets from mice treated with streptozotocin	855:909	We found that paxillin, a key adaptor molecule in focal adhesions, could be modified by O-GlcNAc in INS-1 cells treated with GlcN and in pancreatic islets from mice treated with streptozotocin.
20829364	9	32	theme	cell	1667:1670	arg1	process					1681:1687	a persistent cell adhesion process	1654:1687	a persistent cell adhesion process	1654:1687	Together these observations suggest that murine pancreatic β cells may have restricted actin organization upon GlcN treatment by virtue of the O-GlcNAc modification of paxillin, which can be antagonized by a persistent cell adhesion process.
20829364	9	33	theme	adhesion	1672:1679	arg1	process					1681:1687	a persistent cell adhesion process	1654:1687	a persistent cell adhesion process	1654:1687	Together these observations suggest that murine pancreatic β cells may have restricted actin organization upon GlcN treatment by virtue of the O-GlcNAc modification of paxillin, which can be antagonized by a persistent cell adhesion process.
20829364	1	34	theme	integrin-mediated	205:221	arg1	adhesion					223:230	integrin-mediated adhesion	205:230	integrin-mediated adhesion to extracellular matrix	205:254	Protein-protein interactions and/or signaling activities at focal adhesions, where integrin-mediated adhesion to extracellular matrix occurs, are critical for the regulation of adhesion-dependent cellular functions.
20829364	0	35	theme	Glucosamine	0:10	arg1	modification					40:51	Glucosamine treatment-mediated O-GlcNAc modification	0:51	Glucosamine treatment-mediated O-GlcNAc modification of paxillin	0:63	Glucosamine treatment-mediated O-GlcNAc modification of paxillin depends on adhesion state of rat insulinoma INS-1 cells.
20829364	1	36	theme	cellular	318:325	arg1	functions					327:335	adhesion-dependent cellular functions	299:335	adhesion-dependent cellular functions	299:335	Protein-protein interactions and/or signaling activities at focal adhesions, where integrin-mediated adhesion to extracellular matrix occurs, are critical for the regulation of adhesion-dependent cellular functions.
20829364	5	37	theme	human	925:929	arg1	paxillin					931:938	human paxillin	925:938	human paxillin	925:938	Ser-84/85 in human paxillin appeared to be modified by O-GlcNAc, which was inversely correlated to Ser-85 phosphorylation (Ser-83 in rat paxillin).
20829364	2	38	theme	Ser/Thr	491:497	arg1	residues					499:506	their Ser/Thr residues	485:506	their Ser/Thr residues	485:506	Although the phosphorylation and activities of focal adhesion molecules have been intensively studied, the effects of the O-GlcNAc modification of their Ser/Thr residues on cellular functions have been largely unexplored.
20829364	1	39	theme	functions	327:335	arg1	regulation					285:294	the regulation	281:294	the regulation of adhesion-dependent cellular functions	281:335	Protein-protein interactions and/or signaling activities at focal adhesions, where integrin-mediated adhesion to extracellular matrix occurs, are critical for the regulation of adhesion-dependent cellular functions.
20829364	9	40	contain	have	1519:1522	arg1	cells					1509:1513	murine pancreatic β cells	1489:1513	murine pancreatic β cells	1489:1513	Together these observations suggest that murine pancreatic β cells may have restricted actin organization upon GlcN treatment by virtue of the O-GlcNAc modification of paxillin, which can be antagonized by a persistent cell adhesion process.
20829364	9	40	contain	have	1519:1522	arg2	organization					1541:1552	restricted actin organization	1524:1552	restricted actin organization	1524:1552	Together these observations suggest that murine pancreatic β cells may have restricted actin organization upon GlcN treatment by virtue of the O-GlcNAc modification of paxillin, which can be antagonized by a persistent cell adhesion process.
20829364	4	41	theme	pancreatic	855:864	arg1	islets					866:871	pancreatic islets	855:871	pancreatic islets from mice treated with streptozotocin	855:909	We found that paxillin, a key adaptor molecule in focal adhesions, could be modified by O-GlcNAc in INS-1 cells treated with GlcN and in pancreatic islets from mice treated with streptozotocin.
20829364	6	42	theme	GlcN	1111:1114	arg1	modification					1144:1155	the GlcN treatment-enhanced O-GlcNAc modification	1107:1155	the GlcN treatment-enhanced O-GlcNAc modification of paxillin	1107:1167	Integrin-mediated adhesion signaling inhibited the GlcN treatment-enhanced O-GlcNAc modification of paxillin.
20829364	0	43	theme	O-GlcNAc	31:38	arg1	modification					40:51	Glucosamine treatment-mediated O-GlcNAc modification	0:51	Glucosamine treatment-mediated O-GlcNAc modification of paxillin	0:63	Glucosamine treatment-mediated O-GlcNAc modification of paxillin depends on adhesion state of rat insulinoma INS-1 cells.
20829364	9	44	theme	paxillin	1616:1623	arg1	modification					1600:1611	the O-GlcNAc modification	1587:1611	the O-GlcNAc modification of paxillin, which can be antagonized by a persistent cell adhesion process	1587:1687	Together these observations suggest that murine pancreatic β cells may have restricted actin organization upon GlcN treatment by virtue of the O-GlcNAc modification of paxillin, which can be antagonized by a persistent cell adhesion process.
20829364	6	45	theme	paxillin	1160:1167	arg1	modification					1144:1155	the GlcN treatment-enhanced O-GlcNAc modification	1107:1155	the GlcN treatment-enhanced O-GlcNAc modification of paxillin	1107:1167	Integrin-mediated adhesion signaling inhibited the GlcN treatment-enhanced O-GlcNAc modification of paxillin.
20829364	1	46	theme	extracellular	235:247	arg1	matrix					249:254	extracellular matrix	235:254	extracellular matrix	235:254	Protein-protein interactions and/or signaling activities at focal adhesions, where integrin-mediated adhesion to extracellular matrix occurs, are critical for the regulation of adhesion-dependent cellular functions.
20829364	0	47	theme	paxillin	56:63	arg1	modification					40:51	Glucosamine treatment-mediated O-GlcNAc modification	0:51	Glucosamine treatment-mediated O-GlcNAc modification of paxillin	0:63	Glucosamine treatment-mediated O-GlcNAc modification of paxillin depends on adhesion state of rat insulinoma INS-1 cells.
20829364	3	48	theme	INS-1	670:674	arg1	cells					676:680	rat insulinoma INS-1 cells	655:680	rat insulinoma INS-1 cells	655:680	We investigated the effects of O-GlcNAc modification on actin reorganization and morphology of rat insulinoma INS-1 cells after glucosamine (GlcN) treatment.
20829364	6	49	theme	treatment-enhanced	1116:1133	arg1	modification					1144:1155	the GlcN treatment-enhanced O-GlcNAc modification	1107:1155	the GlcN treatment-enhanced O-GlcNAc modification of paxillin	1107:1167	Integrin-mediated adhesion signaling inhibited the GlcN treatment-enhanced O-GlcNAc modification of paxillin.
20829364	2	50	theme	O-GlcNAc	460:467	arg1	modification					469:480	the O-GlcNAc modification	456:480	the O-GlcNAc modification of their Ser/Thr residues	456:506	Although the phosphorylation and activities of focal adhesion molecules have been intensively studied, the effects of the O-GlcNAc modification of their Ser/Thr residues on cellular functions have been largely unexplored.
20829364	8	51	theme	protrusions	1435:1445	arg1	restriction					1420:1430	no further restriction	1409:1430	no further restriction of protrusions	1409:1445	Upon GlcN treatment, expression of a triple mutation (S83A/S84A/S85A) resulted in no further restriction of protrusions.
20829364	3	52	theme	cells	676:680	arg1	morphology					641:650	morphology	641:650	morphology	641:650	We investigated the effects of O-GlcNAc modification on actin reorganization and morphology of rat insulinoma INS-1 cells after glucosamine (GlcN) treatment.
20829364	3	52	theme	cells	676:680	arg1	reorganization					622:635	actin reorganization	616:635	actin reorganization	616:635	We investigated the effects of O-GlcNAc modification on actin reorganization and morphology of rat insulinoma INS-1 cells after glucosamine (GlcN) treatment.
20829364	8	53	theme	mutation	1371:1378	arg1	expression					1348:1357	expression	1348:1357	expression of a triple mutation (S83A/S84A/S85A)	1348:1395	Upon GlcN treatment, expression of a triple mutation (S83A/S84A/S85A) resulted in no further restriction of protrusions.
20829364	8	54	theme	GlcN	1332:1335	arg1	treatment					1337:1345	GlcN treatment	1332:1345	GlcN treatment	1332:1345	Upon GlcN treatment, expression of a triple mutation (S83A/S84A/S85A) resulted in no further restriction of protrusions.
20829364	0	55	mod	modification	40:51	arg3	Glucosamine					0:10	Glucosamine treatment-mediated O-GlcNAc modification	0:51	Glucosamine treatment-mediated O-GlcNAc modification of paxillin	0:63	Glucosamine treatment-mediated O-GlcNAc modification of paxillin depends on adhesion state of rat insulinoma INS-1 cells.
20829364	0	55	mod	modification	40:51	arg1	paxillin					56:63	paxillin	56:63	paxillin	56:63	Glucosamine treatment-mediated O-GlcNAc modification of paxillin depends on adhesion state of rat insulinoma INS-1 cells.
20829364	0	55	mod	modification	40:51	arg3	O-GlcNAc					31:38	Glucosamine treatment-mediated O-GlcNAc modification	0:51	Glucosamine treatment-mediated O-GlcNAc modification of paxillin	0:63	Glucosamine treatment-mediated O-GlcNAc modification of paxillin depends on adhesion state of rat insulinoma INS-1 cells.
20829364	3	56	theme	rat	655:657	arg1	cells					676:680	rat insulinoma INS-1 cells	655:680	rat insulinoma INS-1 cells	655:680	We investigated the effects of O-GlcNAc modification on actin reorganization and morphology of rat insulinoma INS-1 cells after glucosamine (GlcN) treatment.
20829364	1	57	theme	Protein-protein	122:136	arg1	interactions					138:149	Protein-protein interactions	122:149	Protein-protein interactions	122:149	Protein-protein interactions and/or signaling activities at focal adhesions, where integrin-mediated adhesion to extracellular matrix occurs, are critical for the regulation of adhesion-dependent cellular functions.
20829364	2	58	theme	cellular	511:518	arg1	functions					520:528	cellular functions	511:528	cellular functions	511:528	Although the phosphorylation and activities of focal adhesion molecules have been intensively studied, the effects of the O-GlcNAc modification of their Ser/Thr residues on cellular functions have been largely unexplored.
20829364	9	59	theme	β	1507:1507	arg1	cells					1509:1513	murine pancreatic β cells	1489:1513	murine pancreatic β cells	1489:1513	Together these observations suggest that murine pancreatic β cells may have restricted actin organization upon GlcN treatment by virtue of the O-GlcNAc modification of paxillin, which can be antagonized by a persistent cell adhesion process.
20829364	3	60	theme	insulinoma	659:668	arg1	cells					676:680	rat insulinoma INS-1 cells	655:680	rat insulinoma INS-1 cells	655:680	We investigated the effects of O-GlcNAc modification on actin reorganization and morphology of rat insulinoma INS-1 cells after glucosamine (GlcN) treatment.
20829364	5	61	dep	phosphorylation	1018:1032	arg1	Ser-83					1035:1040	Ser-83	1035:1040	Ser-83 in rat paxillin	1035:1056	Ser-84/85 in human paxillin appeared to be modified by O-GlcNAc, which was inversely correlated to Ser-85 phosphorylation (Ser-83 in rat paxillin).
20829364	2	62	theme	adhesion	391:398	arg1	molecules					400:408	focal adhesion molecules	385:408	focal adhesion molecules	385:408	Although the phosphorylation and activities of focal adhesion molecules have been intensively studied, the effects of the O-GlcNAc modification of their Ser/Thr residues on cellular functions have been largely unexplored.
20829364	9	63	theme	murine	1489:1494	arg1	cells					1509:1513	murine pancreatic β cells	1489:1513	murine pancreatic β cells	1489:1513	Together these observations suggest that murine pancreatic β cells may have restricted actin organization upon GlcN treatment by virtue of the O-GlcNAc modification of paxillin, which can be antagonized by a persistent cell adhesion process.
20829364	4	64	theme	focal	768:772	arg1	adhesions					774:782	focal adhesions	768:782	focal adhesions	768:782	We found that paxillin, a key adaptor molecule in focal adhesions, could be modified by O-GlcNAc in INS-1 cells treated with GlcN and in pancreatic islets from mice treated with streptozotocin.
20829364	7	65	theme	restricted	1216:1225	arg1	protrusions					1227:1237	restricted protrusions	1216:1237	restricted protrusions	1216:1237	Adherent INS-1 cells treated with GlcN showed restricted protrusions, whereas untreated cells showed active protrusions for multiple-elongated morphologies.
20829364	2	66	from	effects	445:451	arg1	functions					520:528	cellular functions	511:528	cellular functions	511:528	Although the phosphorylation and activities of focal adhesion molecules have been intensively studied, the effects of the O-GlcNAc modification of their Ser/Thr residues on cellular functions have been largely unexplored.
20829364	2	67	theme	focal	385:389	arg1	molecules					400:408	focal adhesion molecules	385:408	focal adhesion molecules	385:408	Although the phosphorylation and activities of focal adhesion molecules have been intensively studied, the effects of the O-GlcNAc modification of their Ser/Thr residues on cellular functions have been largely unexplored.
20829364	9	68	theme	pancreatic	1496:1505	arg1	cells					1509:1513	murine pancreatic β cells	1489:1513	murine pancreatic β cells	1489:1513	Together these observations suggest that murine pancreatic β cells may have restricted actin organization upon GlcN treatment by virtue of the O-GlcNAc modification of paxillin, which can be antagonized by a persistent cell adhesion process.
20829364	6	69	theme	adhesion	1078:1085	arg1	signaling					1087:1095	Integrin-mediated adhesion signaling	1060:1095	Integrin-mediated adhesion signaling	1060:1095	Integrin-mediated adhesion signaling inhibited the GlcN treatment-enhanced O-GlcNAc modification of paxillin.
20829364	3	70	theme	modification	600:611	arg1	effects					580:586	the effects	576:586	the effects of O-GlcNAc modification on actin reorganization and morphology of rat insulinoma INS-1 cells	576:680	We investigated the effects of O-GlcNAc modification on actin reorganization and morphology of rat insulinoma INS-1 cells after glucosamine (GlcN) treatment.
20829364	3	71	theme	GlcN	701:704	arg1	treatment					707:715	glucosamine (GlcN) treatment	688:715	glucosamine (GlcN) treatment	688:715	We investigated the effects of O-GlcNAc modification on actin reorganization and morphology of rat insulinoma INS-1 cells after glucosamine (GlcN) treatment.
20829364	1	72	theme	signaling	158:166	arg1	activities					168:177	signaling activities	158:177	signaling activities	158:177	Protein-protein interactions and/or signaling activities at focal adhesions, where integrin-mediated adhesion to extracellular matrix occurs, are critical for the regulation of adhesion-dependent cellular functions.
20829364	6	73	mod	modification	1144:1155	arg1	paxillin					1160:1167	paxillin	1160:1167	paxillin	1160:1167	Integrin-mediated adhesion signaling inhibited the GlcN treatment-enhanced O-GlcNAc modification of paxillin.
20829364	6	73	mod	modification	1144:1155	arg3	O-GlcNAc					1135:1142	the GlcN treatment-enhanced O-GlcNAc modification	1107:1155	the GlcN treatment-enhanced O-GlcNAc modification of paxillin	1107:1167	Integrin-mediated adhesion signaling inhibited the GlcN treatment-enhanced O-GlcNAc modification of paxillin.
20829364	6	74	theme	Integrin-mediated	1060:1076	arg1	signaling					1087:1095	Integrin-mediated adhesion signaling	1060:1095	Integrin-mediated adhesion signaling	1060:1095	Integrin-mediated adhesion signaling inhibited the GlcN treatment-enhanced O-GlcNAc modification of paxillin.
20829364	9	75	theme	O-GlcNAc	1591:1598	arg1	modification					1600:1611	the O-GlcNAc modification	1587:1611	the O-GlcNAc modification of paxillin, which can be antagonized by a persistent cell adhesion process	1587:1687	Together these observations suggest that murine pancreatic β cells may have restricted actin organization upon GlcN treatment by virtue of the O-GlcNAc modification of paxillin, which can be antagonized by a persistent cell adhesion process.
20829364	5	76	theme	rat	1045:1047	arg1	paxillin					1049:1056	rat paxillin	1045:1056	rat paxillin	1045:1056	Ser-84/85 in human paxillin appeared to be modified by O-GlcNAc, which was inversely correlated to Ser-85 phosphorylation (Ser-83 in rat paxillin).
20829364	8	77	theme	triple	1364:1369	arg1	S83A/S84A/S85A					1381:1394	S83A/S84A/S85A	1381:1394	S83A/S84A/S85A	1381:1394	Upon GlcN treatment, expression of a triple mutation (S83A/S84A/S85A) resulted in no further restriction of protrusions.
20829364	8	77	theme	triple	1364:1369	arg1	mutation					1371:1378	a triple mutation	1362:1378	a triple mutation (S83A/S84A/S85A)	1362:1395	Upon GlcN treatment, expression of a triple mutation (S83A/S84A/S85A) resulted in no further restriction of protrusions.
20829364	4	78	theme	key	744:746	arg1	molecule					756:763	a key adaptor molecule	742:763	a key adaptor molecule in focal adhesions	742:782	We found that paxillin, a key adaptor molecule in focal adhesions, could be modified by O-GlcNAc in INS-1 cells treated with GlcN and in pancreatic islets from mice treated with streptozotocin.
20829364	4	78	theme	key	744:746	arg1	paxillin					732:739	paxillin	732:739	paxillin	732:739	We found that paxillin, a key adaptor molecule in focal adhesions, could be modified by O-GlcNAc in INS-1 cells treated with GlcN and in pancreatic islets from mice treated with streptozotocin.
20829364	0	79	theme	adhesion	76:83	arg1	state					85:89	adhesion state	76:89	adhesion state of rat insulinoma INS-1 cells	76:119	Glucosamine treatment-mediated O-GlcNAc modification of paxillin depends on adhesion state of rat insulinoma INS-1 cells.
20829364	3	80	theme	glucosamine	688:698	arg1	treatment					707:715	glucosamine (GlcN) treatment	688:715	glucosamine (GlcN) treatment	688:715	We investigated the effects of O-GlcNAc modification on actin reorganization and morphology of rat insulinoma INS-1 cells after glucosamine (GlcN) treatment.
20829364	7	81	theme	untreated	1248:1256	arg1	cells					1258:1262	untreated cells	1248:1262	untreated cells	1248:1262	Adherent INS-1 cells treated with GlcN showed restricted protrusions, whereas untreated cells showed active protrusions for multiple-elongated morphologies.
20829364	4	82	from	molecule	756:763	arg1	adhesions					774:782	focal adhesions	768:782	focal adhesions	768:782	We found that paxillin, a key adaptor molecule in focal adhesions, could be modified by O-GlcNAc in INS-1 cells treated with GlcN and in pancreatic islets from mice treated with streptozotocin.
20829364	7	83	theme	multiple-elongated	1294:1311	arg1	morphologies					1313:1324	multiple-elongated morphologies	1294:1324	multiple-elongated morphologies	1294:1324	Adherent INS-1 cells treated with GlcN showed restricted protrusions, whereas untreated cells showed active protrusions for multiple-elongated morphologies.
24014020	0	0	theme	autointegration	81:95	arg1	BAF					105:107	BAF	105:107	BAF	105:107	O-Linked β-N-acetylglucosamine (O-GlcNAc) regulates emerin binding to barrier to autointegration factor (BAF) in a chromatin- and lamin B-enriched "niche".
24014020	0	0	theme	autointegration	81:95	arg1	factor					97:102	autointegration factor	81:102	autointegration factor (BAF)	81:108	O-Linked β-N-acetylglucosamine (O-GlcNAc) regulates emerin binding to barrier to autointegration factor (BAF) in a chromatin- and lamin B-enriched "niche".
24014020	1	1	dep	factor	257:262	arg1	to					238:239	to	238:239	to	238:239	Emerin, a membrane component of nuclear "lamina" networks with lamins and barrier to autointegration factor (BAF), is highly O-GlcNAc-modified ("O-GlcNAcylated") in mammalian cells.
24014020	11	2	theme	component	1501:1509	arg1	control					1452:1458	direct control	1445:1458	direct control of a conserved LEM domain nuclear lamina component	1445:1509	These results reveal direct control of a conserved LEM domain nuclear lamina component by β-N-acetylglucosaminyltransferase, a nutrient sensor that regulates cell stress responses, mitosis, and epigenetics.
24014020	1	3	theme	networks	205:212	arg1	Emerin					156:161	Emerin	156:161	Emerin	156:161	Emerin, a membrane component of nuclear "lamina" networks with lamins and barrier to autointegration factor (BAF), is highly O-GlcNAc-modified ("O-GlcNAcylated") in mammalian cells.
24014020	1	3	theme	networks	205:212	arg1	component					175:183	a membrane component	164:183	a membrane component of nuclear "lamina" networks with lamins and barrier to autointegration factor (BAF)	164:268	Emerin, a membrane component of nuclear "lamina" networks with lamins and barrier to autointegration factor (BAF), is highly O-GlcNAc-modified ("O-GlcNAcylated") in mammalian cells.
24014020	4	4	theme	S52A/S53A/S54A	596:609	arg1	mutant					611:616	the triple S52A/S53A/S54A mutant	585:616	the triple S52A/S53A/S54A mutant	585:616	O-GlcNAcylation was reduced ~66% by the triple S52A/S53A/S54A mutant, and S173A reduced O-GlcNAcylation of the S52A/S53A/S54A mutant by ~30%, in vivo.
24014020	1	5	from	cells	331:335	arg1	O-GlcNAc-modified					281:297	O-GlcNAc-modified	281:297	O-GlcNAc-modified	281:297	Emerin, a membrane component of nuclear "lamina" networks with lamins and barrier to autointegration factor (BAF), is highly O-GlcNAc-modified ("O-GlcNAcylated") in mammalian cells.
24014020	10	6	theme	second	1324:1329	arg1	region					1331:1336	the second region	1320:1336	the second region	1320:1336	O-GlcNAc modification at Ser-173, in the second region, is proposed to promote emerin association with BAF in the chromatin/lamin B "niche."
24014020	6	7	theme	lamin-B-containing	920:937	arg1	fractions					939:947	histone- and lamin-B-containing fractions	907:947	histone- and lamin-B-containing fractions	907:947	Emerin and BAF associated only in histone- and lamin-B-containing fractions.
24014020	11	8	theme	cell	1582:1585	arg1	responses					1594:1602	cell stress responses	1582:1602	cell stress responses	1582:1602	These results reveal direct control of a conserved LEM domain nuclear lamina component by β-N-acetylglucosaminyltransferase, a nutrient sensor that regulates cell stress responses, mitosis, and epigenetics.
24014020	11	9	theme	nuclear	1486:1492	arg1	component					1501:1509	a conserved LEM domain nuclear lamina component	1463:1509	a conserved LEM domain nuclear lamina component	1463:1509	These results reveal direct control of a conserved LEM domain nuclear lamina component by β-N-acetylglucosaminyltransferase, a nutrient sensor that regulates cell stress responses, mitosis, and epigenetics.
24014020	4	10	theme	mutant	675:680	arg1	O-GlcNAcylation					637:651	O-GlcNAcylation	637:651	O-GlcNAcylation of the S52A/S53A/S54A mutant	637:680	O-GlcNAcylation was reduced ~66% by the triple S52A/S53A/S54A mutant, and S173A reduced O-GlcNAcylation of the S52A/S53A/S54A mutant by ~30%, in vivo.
24014020	1	11	theme	O-GlcNAcylated	301:314	arg1	"					315:315	"O-GlcNAcylated"	300:315	"O-GlcNAcylated"	300:315	Emerin, a membrane component of nuclear "lamina" networks with lamins and barrier to autointegration factor (BAF), is highly O-GlcNAc-modified ("O-GlcNAcylated") in mammalian cells.
24014020	5	12	theme	emerin	732:737	arg1	BAF					758:760	BAF	758:760	BAF	758:760	We separated two populations of emerin, A-type lamins and BAF; one population solubilized easily, and the other required sonication and included histones and B-type lamins.
24014020	5	12	theme	emerin	732:737	arg1	lamins					747:752	A-type lamins	740:752	A-type lamins	740:752	We separated two populations of emerin, A-type lamins and BAF; one population solubilized easily, and the other required sonication and included histones and B-type lamins.
24014020	5	12	theme	emerin	732:737	arg1	populations					717:727	two populations	713:727	two populations of emerin	713:737	We separated two populations of emerin, A-type lamins and BAF; one population solubilized easily, and the other required sonication and included histones and B-type lamins.
24014020	5	13	theme	B-type	858:863	arg1	lamins					865:870	B-type lamins	858:870	B-type lamins	858:870	We separated two populations of emerin, A-type lamins and BAF; one population solubilized easily, and the other required sonication and included histones and B-type lamins.
24014020	8	14	theme	essential	1153:1161	arg1	β-N-acetylglucosaminyltransferase					1115:1147	β-N-acetylglucosaminyltransferase	1115:1147	β-N-acetylglucosaminyltransferase	1115:1147	We conclude that β-N-acetylglucosaminyltransferase, an essential enzyme, controls two regions in emerin.
24014020	8	14	theme	essential	1153:1161	arg1	enzyme					1163:1168	an essential enzyme	1150:1168	an essential enzyme	1150:1168	We conclude that β-N-acetylglucosaminyltransferase, an essential enzyme, controls two regions in emerin.
24014020	7	15	theme	GFP-emerin	1006:1015	arg1	association					1017:1027	GFP-emerin association	1006:1027	GFP-emerin association with BAF	1006:1036	The S173D mutation specifically and selectively reduced GFP-emerin association with BAF by 58% and also increased GFP-emerin hyper-phosphorylation.
24014020	3	16	theme	Emerin	462:467	arg1	O-GlcNAcylation					469:483	Emerin O-GlcNAcylation	462:483	Emerin O-GlcNAcylation	462:483	Emerin O-GlcNAcylation was reduced ~50% by S53A or S54A mutation in vitro and in vivo.
24014020	2	17	theme	O-GlcNAcylation	389:403	arg1	sites					380:384	eight sites	374:384	eight sites	374:384	Mass spectrometry analysis revealed eight sites of O-GlcNAcylation, including Ser-53, Ser-54, Ser-87, Ser-171, and Ser-173.
24014020	2	17	theme	O-GlcNAcylation	389:403	arg1	Ser-173					453:459	Ser-173	453:459	Ser-173	453:459	Mass spectrometry analysis revealed eight sites of O-GlcNAcylation, including Ser-53, Ser-54, Ser-87, Ser-171, and Ser-173.
24014020	2	17	theme	O-GlcNAcylation	389:403	arg1	Ser-54					424:429	Ser-54	424:429	Ser-54	424:429	Mass spectrometry analysis revealed eight sites of O-GlcNAcylation, including Ser-53, Ser-54, Ser-87, Ser-171, and Ser-173.
24014020	2	17	theme	O-GlcNAcylation	389:403	arg1	O-GlcNAcylation					389:403	O-GlcNAcylation	389:403	O-GlcNAcylation	389:403	Mass spectrometry analysis revealed eight sites of O-GlcNAcylation, including Ser-53, Ser-54, Ser-87, Ser-171, and Ser-173.
24014020	2	17	theme	O-GlcNAcylation	389:403	arg1	Ser-87					432:437	Ser-87	432:437	Ser-87	432:437	Mass spectrometry analysis revealed eight sites of O-GlcNAcylation, including Ser-53, Ser-54, Ser-87, Ser-171, and Ser-173.
24014020	2	17	theme	O-GlcNAcylation	389:403	arg1	Ser-53					416:421	Ser-53	416:421	Ser-53	416:421	Mass spectrometry analysis revealed eight sites of O-GlcNAcylation, including Ser-53, Ser-54, Ser-87, Ser-171, and Ser-173.
24014020	2	17	theme	O-GlcNAcylation	389:403	arg1	Ser-171					440:446	Ser-171	440:446	Ser-171	440:446	Mass spectrometry analysis revealed eight sites of O-GlcNAcylation, including Ser-53, Ser-54, Ser-87, Ser-171, and Ser-173.
24014020	10	18	theme	emerin	1362:1367	arg1	association					1369:1379	emerin association	1362:1379	emerin association with BAF	1362:1388	O-GlcNAc modification at Ser-173, in the second region, is proposed to promote emerin association with BAF in the chromatin/lamin B "niche."
24014020	1	19	theme	barrier	230:236	arg1	BAF					265:267	BAF	265:267	BAF	265:267	Emerin, a membrane component of nuclear "lamina" networks with lamins and barrier to autointegration factor (BAF), is highly O-GlcNAc-modified ("O-GlcNAcylated") in mammalian cells.
24014020	1	19	theme	barrier	230:236	arg1	factor					257:262	barrier to autointegration factor	230:262	barrier to autointegration factor (BAF)	230:268	Emerin, a membrane component of nuclear "lamina" networks with lamins and barrier to autointegration factor (BAF), is highly O-GlcNAc-modified ("O-GlcNAcylated") in mammalian cells.
24014020	11	20	theme	stress	1587:1592	arg1	responses					1594:1602	cell stress responses	1582:1602	cell stress responses	1582:1602	These results reveal direct control of a conserved LEM domain nuclear lamina component by β-N-acetylglucosaminyltransferase, a nutrient sensor that regulates cell stress responses, mitosis, and epigenetics.
24014020	0	21	theme	O-Linked	0:7	arg1	O-GlcNAc					32:39	O-GlcNAc	32:39	O-GlcNAc	32:39	O-Linked β-N-acetylglucosamine (O-GlcNAc) regulates emerin binding to barrier to autointegration factor (BAF) in a chromatin- and lamin B-enriched "niche".
24014020	0	21	theme	O-Linked	0:7	arg1	β-N-acetylglucosamine					9:29	O-Linked β-N-acetylglucosamine	0:29	O-Linked β-N-acetylglucosamine (O-GlcNAc)	0:40	O-Linked β-N-acetylglucosamine (O-GlcNAc) regulates emerin binding to barrier to autointegration factor (BAF) in a chromatin- and lamin B-enriched "niche".
24014020	1	22	dep	O-GlcNAc-modified	281:297	arg1	"					315:315	"O-GlcNAcylated"	300:315	"O-GlcNAcylated"	300:315	Emerin, a membrane component of nuclear "lamina" networks with lamins and barrier to autointegration factor (BAF), is highly O-GlcNAc-modified ("O-GlcNAcylated") in mammalian cells.
24014020	11	23	theme	direct	1445:1450	arg1	control					1452:1458	direct control	1445:1458	direct control of a conserved LEM domain nuclear lamina component	1445:1509	These results reveal direct control of a conserved LEM domain nuclear lamina component by β-N-acetylglucosaminyltransferase, a nutrient sensor that regulates cell stress responses, mitosis, and epigenetics.
24014020	10	24	theme	chromatin/lamin	1397:1411	arg1	niche					1416:1420	the chromatin/lamin B "niche	1393:1420	the chromatin/lamin B "niche	1393:1420	O-GlcNAc modification at Ser-173, in the second region, is proposed to promote emerin association with BAF in the chromatin/lamin B "niche."
24014020	4	25	theme	S52A/S53A/S54A	660:673	arg1	mutant					675:680	the S52A/S53A/S54A mutant	656:680	the S52A/S53A/S54A mutant	656:680	O-GlcNAcylation was reduced ~66% by the triple S52A/S53A/S54A mutant, and S173A reduced O-GlcNAcylation of the S52A/S53A/S54A mutant by ~30%, in vivo.
24014020	7	26	theme	GFP-emerin	1064:1073	arg1	hyper-phosphorylation					1075:1095	GFP-emerin hyper-phosphorylation	1064:1095	GFP-emerin hyper-phosphorylation	1064:1095	The S173D mutation specifically and selectively reduced GFP-emerin association with BAF by 58% and also increased GFP-emerin hyper-phosphorylation.
24014020	1	27	theme	autointegration	241:255	arg1	BAF					265:267	BAF	265:267	BAF	265:267	Emerin, a membrane component of nuclear "lamina" networks with lamins and barrier to autointegration factor (BAF), is highly O-GlcNAc-modified ("O-GlcNAcylated") in mammalian cells.
24014020	1	27	theme	autointegration	241:255	arg1	factor					257:262	barrier to autointegration factor	230:262	barrier to autointegration factor (BAF)	230:268	Emerin, a membrane component of nuclear "lamina" networks with lamins and barrier to autointegration factor (BAF), is highly O-GlcNAc-modified ("O-GlcNAcylated") in mammalian cells.
24014020	11	28	theme	conserved	1465:1473	arg1	component					1501:1509	a conserved LEM domain nuclear lamina component	1463:1509	a conserved LEM domain nuclear lamina component	1463:1509	These results reveal direct control of a conserved LEM domain nuclear lamina component by β-N-acetylglucosaminyltransferase, a nutrient sensor that regulates cell stress responses, mitosis, and epigenetics.
24014020	10	29	dep	proposed	1342:1349	arg1	"					1422:1422	"	1422:1422	"	1422:1422	O-GlcNAc modification at Ser-173, in the second region, is proposed to promote emerin association with BAF in the chromatin/lamin B "niche."
24014020	1	30	theme	membrane	166:173	arg1	Emerin					156:161	Emerin	156:161	Emerin	156:161	Emerin, a membrane component of nuclear "lamina" networks with lamins and barrier to autointegration factor (BAF), is highly O-GlcNAc-modified ("O-GlcNAcylated") in mammalian cells.
24014020	1	30	theme	membrane	166:173	arg1	component					175:183	a membrane component	164:183	a membrane component of nuclear "lamina" networks with lamins and barrier to autointegration factor (BAF)	164:268	Emerin, a membrane component of nuclear "lamina" networks with lamins and barrier to autointegration factor (BAF), is highly O-GlcNAc-modified ("O-GlcNAcylated") in mammalian cells.
24014020	1	31	from	O-GlcNAc-modified	281:297	arg1	cells					331:335	mammalian cells	321:335	mammalian cells	321:335	Emerin, a membrane component of nuclear "lamina" networks with lamins and barrier to autointegration factor (BAF), is highly O-GlcNAc-modified ("O-GlcNAcylated") in mammalian cells.
24014020	1	32	theme	mammalian	321:329	arg1	cells					331:335	mammalian cells	321:335	mammalian cells	321:335	Emerin, a membrane component of nuclear "lamina" networks with lamins and barrier to autointegration factor (BAF), is highly O-GlcNAc-modified ("O-GlcNAcylated") in mammalian cells.
24014020	3	33	theme	S54A	513:516	arg1	mutation					518:525	S54A mutation	513:525	S54A mutation	513:525	Emerin O-GlcNAcylation was reduced ~50% by S53A or S54A mutation in vitro and in vivo.
24014020	10	34	with	association	1369:1379	arg1	BAF					1386:1388	BAF	1386:1388	BAF	1386:1388	O-GlcNAc modification at Ser-173, in the second region, is proposed to promote emerin association with BAF in the chromatin/lamin B "niche."
24014020	2	35	theme	spectrometry	343:354	arg1	analysis					356:363	Mass spectrometry analysis	338:363	Mass spectrometry analysis	338:363	Mass spectrometry analysis revealed eight sites of O-GlcNAcylation, including Ser-53, Ser-54, Ser-87, Ser-171, and Ser-173.
24014020	9	36	theme	LEM	1271:1273	arg1	domain					1275:1280	the LEM domain	1267:1280	the LEM domain	1267:1280	The first region, defined by residues Ser-53 and Ser-54, flanks the LEM domain.
24014020	0	37	theme	chromatin-	115:124	arg1	"					153:153	a chromatin- and lamin B-enriched "niche"	113:153	a chromatin- and lamin B-enriched "niche"	113:153	O-Linked β-N-acetylglucosamine (O-GlcNAc) regulates emerin binding to barrier to autointegration factor (BAF) in a chromatin- and lamin B-enriched "niche".
24014020	8	38	from	regions	1184:1190	arg1	emerin					1195:1200	emerin	1195:1200	emerin	1195:1200	We conclude that β-N-acetylglucosaminyltransferase, an essential enzyme, controls two regions in emerin.
24014020	2	39	theme	Mass	338:341	arg1	analysis					356:363	Mass spectrometry analysis	338:363	Mass spectrometry analysis	338:363	Mass spectrometry analysis revealed eight sites of O-GlcNAcylation, including Ser-53, Ser-54, Ser-87, Ser-171, and Ser-173.
24014020	0	40	theme	B-enriched	136:145	arg1	"					153:153	a chromatin- and lamin B-enriched "niche"	113:153	a chromatin- and lamin B-enriched "niche"	113:153	O-Linked β-N-acetylglucosamine (O-GlcNAc) regulates emerin binding to barrier to autointegration factor (BAF) in a chromatin- and lamin B-enriched "niche".
24014020	7	41	with	association	1017:1027	arg1	BAF					1034:1036	BAF	1034:1036	BAF	1034:1036	The S173D mutation specifically and selectively reduced GFP-emerin association with BAF by 58% and also increased GFP-emerin hyper-phosphorylation.
24014020	7	42	theme	S173D	954:958	arg1	mutation					960:967	The S173D mutation	950:967	The S173D mutation	950:967	The S173D mutation specifically and selectively reduced GFP-emerin association with BAF by 58% and also increased GFP-emerin hyper-phosphorylation.
24014020	0	43	theme	emerin	52:57	arg1	binding					59:65	emerin binding	52:65	emerin binding to barrier to autointegration factor (BAF)	52:108	O-Linked β-N-acetylglucosamine (O-GlcNAc) regulates emerin binding to barrier to autointegration factor (BAF) in a chromatin- and lamin B-enriched "niche".
24014020	11	44	theme	nutrient	1551:1558	arg1	sensor					1560:1565	a nutrient sensor	1549:1565	a nutrient sensor that regulates cell stress responses	1549:1602	These results reveal direct control of a conserved LEM domain nuclear lamina component by β-N-acetylglucosaminyltransferase, a nutrient sensor that regulates cell stress responses, mitosis, and epigenetics.
24014020	1	45	with	networks	205:212	arg1	BAF					265:267	BAF	265:267	BAF	265:267	Emerin, a membrane component of nuclear "lamina" networks with lamins and barrier to autointegration factor (BAF), is highly O-GlcNAc-modified ("O-GlcNAcylated") in mammalian cells.
24014020	1	45	with	networks	205:212	arg1	factor					257:262	barrier to autointegration factor	230:262	barrier to autointegration factor (BAF)	230:268	Emerin, a membrane component of nuclear "lamina" networks with lamins and barrier to autointegration factor (BAF), is highly O-GlcNAc-modified ("O-GlcNAcylated") in mammalian cells.
24014020	1	45	with	networks	205:212	arg1	lamins					219:224	lamins	219:224	lamins	219:224	Emerin, a membrane component of nuclear "lamina" networks with lamins and barrier to autointegration factor (BAF), is highly O-GlcNAc-modified ("O-GlcNAcylated") in mammalian cells.
24014020	10	46	from	modification	1292:1303	arg1	region					1331:1336	the second region	1320:1336	the second region	1320:1336	O-GlcNAc modification at Ser-173, in the second region, is proposed to promote emerin association with BAF in the chromatin/lamin B "niche."
24014020	9	47	dep	residues	1232:1239	arg1	residues					1232:1239	residues Ser-53 and Ser-54	1232:1257	residues Ser-53 and Ser-54	1232:1257	The first region, defined by residues Ser-53 and Ser-54, flanks the LEM domain.
24014020	9	47	dep	residues	1232:1239	arg1	Ser-54					1252:1257	Ser-54	1252:1257	Ser-54	1252:1257	The first region, defined by residues Ser-53 and Ser-54, flanks the LEM domain.
24014020	9	47	dep	residues	1232:1239	arg1	Ser-53					1241:1246	Ser-53	1241:1246	Ser-53	1241:1246	The first region, defined by residues Ser-53 and Ser-54, flanks the LEM domain.
24014020	0	48	theme	niche	148:152	arg1	"					153:153	a chromatin- and lamin B-enriched "niche"	113:153	a chromatin- and lamin B-enriched "niche"	113:153	O-Linked β-N-acetylglucosamine (O-GlcNAc) regulates emerin binding to barrier to autointegration factor (BAF) in a chromatin- and lamin B-enriched "niche".
24014020	11	49	theme	LEM	1475:1477	arg1	component					1501:1509	a conserved LEM domain nuclear lamina component	1463:1509	a conserved LEM domain nuclear lamina component	1463:1509	These results reveal direct control of a conserved LEM domain nuclear lamina component by β-N-acetylglucosaminyltransferase, a nutrient sensor that regulates cell stress responses, mitosis, and epigenetics.
24014020	1	50	theme	nuclear	188:194	arg1	networks					205:212	nuclear "lamina" networks	188:212	nuclear "lamina" networks with lamins and barrier to autointegration factor (BAF)	188:268	Emerin, a membrane component of nuclear "lamina" networks with lamins and barrier to autointegration factor (BAF), is highly O-GlcNAc-modified ("O-GlcNAcylated") in mammalian cells.
24014020	10	51	theme	B	1413:1413	arg1	niche					1416:1420	the chromatin/lamin B "niche	1393:1420	the chromatin/lamin B "niche	1393:1420	O-GlcNAc modification at Ser-173, in the second region, is proposed to promote emerin association with BAF in the chromatin/lamin B "niche."
24014020	11	52	theme	domain	1479:1484	arg1	component					1501:1509	a conserved LEM domain nuclear lamina component	1463:1509	a conserved LEM domain nuclear lamina component	1463:1509	These results reveal direct control of a conserved LEM domain nuclear lamina component by β-N-acetylglucosaminyltransferase, a nutrient sensor that regulates cell stress responses, mitosis, and epigenetics.
24014020	10	53	theme	O-GlcNAc	1283:1290	arg1	modification					1292:1303	O-GlcNAc modification	1283:1303	O-GlcNAc modification	1283:1303	O-GlcNAc modification at Ser-173, in the second region, is proposed to promote emerin association with BAF in the chromatin/lamin B "niche."
24014020	10	54	from	Ser-173	1308:1314	arg1	modification					1292:1303	O-GlcNAc modification	1283:1303	O-GlcNAc modification	1283:1303	O-GlcNAc modification at Ser-173, in the second region, is proposed to promote emerin association with BAF in the chromatin/lamin B "niche."
24014020	5	55	theme	A-type	740:745	arg1	lamins					747:752	A-type lamins	740:752	A-type lamins	740:752	We separated two populations of emerin, A-type lamins and BAF; one population solubilized easily, and the other required sonication and included histones and B-type lamins.
24014020	5	55	theme	A-type	740:745	arg1	populations					717:727	two populations	713:727	two populations of emerin	713:737	We separated two populations of emerin, A-type lamins and BAF; one population solubilized easily, and the other required sonication and included histones and B-type lamins.
24014020	4	56	theme	triple	589:594	arg1	mutant					611:616	the triple S52A/S53A/S54A mutant	585:616	the triple S52A/S53A/S54A mutant	585:616	O-GlcNAcylation was reduced ~66% by the triple S52A/S53A/S54A mutant, and S173A reduced O-GlcNAcylation of the S52A/S53A/S54A mutant by ~30%, in vivo.
24014020	1	57	theme	lamina	197:202	arg1	networks					205:212	nuclear "lamina" networks	188:212	nuclear "lamina" networks with lamins and barrier to autointegration factor (BAF)	188:268	Emerin, a membrane component of nuclear "lamina" networks with lamins and barrier to autointegration factor (BAF), is highly O-GlcNAc-modified ("O-GlcNAcylated") in mammalian cells.
24014020	9	58	theme	first	1207:1211	arg1	region					1213:1218	The first region	1203:1218	The first region	1203:1218	The first region, defined by residues Ser-53 and Ser-54, flanks the LEM domain.
24014020	11	59	theme	lamina	1494:1499	arg1	component					1501:1509	a conserved LEM domain nuclear lamina component	1463:1509	a conserved LEM domain nuclear lamina component	1463:1509	These results reveal direct control of a conserved LEM domain nuclear lamina component by β-N-acetylglucosaminyltransferase, a nutrient sensor that regulates cell stress responses, mitosis, and epigenetics.
24014020	6	60	theme	histone-	907:914	arg1	fractions					939:947	histone- and lamin-B-containing fractions	907:947	histone- and lamin-B-containing fractions	907:947	Emerin and BAF associated only in histone- and lamin-B-containing fractions.
24014020	1	61	theme	"	203:203	arg1	networks					205:212	nuclear "lamina" networks	188:212	nuclear "lamina" networks with lamins and barrier to autointegration factor (BAF)	188:268	Emerin, a membrane component of nuclear "lamina" networks with lamins and barrier to autointegration factor (BAF), is highly O-GlcNAc-modified ("O-GlcNAcylated") in mammalian cells.
33330510	2	0	theme	decrease	509:516	arg1	reaction					475:482	the homeostatic reaction	459:482	the homeostatic reaction of the regulatory volume decrease (RVD) after cell swelling	459:542	Our previous work showed that increases in the O-GlcNAcylation of cellular proteins impair the homeostatic reaction of the regulatory volume decrease (RVD) after cell swelling by an unknown mechanism.
33330510	5	1	theme	ICln	1119:1122	arg1	binding					1108:1114	the binding	1104:1114	the binding of ICln to the intracellular domain of α-integrin, a process that is essential for the activation of IClswell	1104:1224	In parallel, increases or decreases in O-GlcNAcylation, respectively, weakened or stabilized the binding of ICln to the intracellular domain of α-integrin, a process that is essential for the activation of IClswell.
33330510	7	2	theme	cells	1453:1457	arg1	exposure					1441:1448	exposure	1441:1448	exposure of cells to a hypotonic solution	1441:1481	In addition, exposure of cells to a hypotonic solution reduced the O-GlcNAcylation of cellular proteins.
33330510	7	3	theme	hypotonic	1464:1472	arg1	solution					1474:1481	a hypotonic solution	1462:1481	a hypotonic solution	1462:1481	In addition, exposure of cells to a hypotonic solution reduced the O-GlcNAcylation of cellular proteins.
33330510	9	4	theme	volume	1838:1843	arg1	regulation					1815:1824	the regulation	1811:1824	the regulation of cellular volume	1811:1843	We propose that disturbances in the regulation of cellular volume may contribute to disease in settings of chronically elevated O-GlcNAcylation, including diabetic nephropathy.
33330510	1	5	theme	diabetes	252:259	arg1	mellitus					261:268	diabetes mellitus	252:268	diabetes mellitus	252:268	O-GlcNAcylation is a post-translational modification of proteins that controls a variety of cellular processes, is chronically elevated in diabetes mellitus, and may contribute to the progression of diabetic complications, including diabetic nephropathy.
33330510	2	6	theme	volume	502:507	arg1	RVD					519:521	RVD	519:521	RVD	519:521	Our previous work showed that increases in the O-GlcNAcylation of cellular proteins impair the homeostatic reaction of the regulatory volume decrease (RVD) after cell swelling by an unknown mechanism.
33330510	2	6	theme	volume	502:507	arg1	decrease					509:516	the regulatory volume decrease	487:516	the regulatory volume decrease (RVD) after cell swelling	487:542	Our previous work showed that increases in the O-GlcNAcylation of cellular proteins impair the homeostatic reaction of the regulatory volume decrease (RVD) after cell swelling by an unknown mechanism.
33330510	1	7	theme	diabetic	346:353	arg1	nephropathy					355:365	diabetic nephropathy	346:365	diabetic nephropathy	346:365	O-GlcNAcylation is a post-translational modification of proteins that controls a variety of cellular processes, is chronically elevated in diabetes mellitus, and may contribute to the progression of diabetic complications, including diabetic nephropathy.
33330510	1	8	theme	proteins	169:176	arg1	modification					153:164	a post-translational modification	132:164	a post-translational modification of proteins that controls a variety of cellular processes, is chronically elevated in diabetes mellitus, and may contribute to the progression of diabetic complications, including diabetic nephropathy	132:365	O-GlcNAcylation is a post-translational modification of proteins that controls a variety of cellular processes, is chronically elevated in diabetes mellitus, and may contribute to the progression of diabetic complications, including diabetic nephropathy.
33330510	1	8	theme	proteins	169:176	arg1	O-GlcNAcylation					113:127	O-GlcNAcylation	113:127	O-GlcNAcylation	113:127	O-GlcNAcylation is a post-translational modification of proteins that controls a variety of cellular processes, is chronically elevated in diabetes mellitus, and may contribute to the progression of diabetic complications, including diabetic nephropathy.
33330510	0	9	theme	ICln	93:96	arg1	Binding					70:76	the Binding	66:76	the Binding of the Protein ICln to α-Integrin	66:110	O-GlcNAcylation Suppresses the Ion Current IClswell by Preventing the Binding of the Protein ICln to α-Integrin.
33330510	4	10	theme	IClswell	880:887	arg1	current					889:895	the ICln-induced IClswell current	863:895	the endogenous as well as the ICln-induced IClswell current	837:895	Here, we show that experimentally increased O-GlcNAcylation of cellular proteins inhibited the endogenous as well as the ICln-induced IClswell current and prevented RVD in a human renal cell line, while decreases in O-GlcNAcylation augmented the current magnitude.
33330510	4	11	from	decreases	949:957	arg1	O-GlcNAcylation					962:976	O-GlcNAcylation	962:976	O-GlcNAcylation	962:976	Here, we show that experimentally increased O-GlcNAcylation of cellular proteins inhibited the endogenous as well as the ICln-induced IClswell current and prevented RVD in a human renal cell line, while decreases in O-GlcNAcylation augmented the current magnitude.
33330510	8	12	theme	ICln	1716:1719	arg1	O-GlcNAcylation					1697:1711	the O-GlcNAcylation	1693:1711	the O-GlcNAcylation of ICln at Ser67	1693:1728	Together, these findings show that O-GlcNAcylation affects RVD by influencing IClswell and further indicate that hypotonicity may activate IClswell by reducing the O-GlcNAcylation of ICln at Ser67, therefore permitting its binding to α-integrin.
33330510	0	13	theme	Protein	85:91	arg1	ICln					93:96	the Protein ICln	81:96	the Protein ICln	81:96	O-GlcNAcylation Suppresses the Ion Current IClswell by Preventing the Binding of the Protein ICln to α-Integrin.
33330510	4	14	theme	ICln-induced	867:878	arg1	current					889:895	the ICln-induced IClswell current	863:895	the endogenous as well as the ICln-induced IClswell current	837:895	Here, we show that experimentally increased O-GlcNAcylation of cellular proteins inhibited the endogenous as well as the ICln-induced IClswell current and prevented RVD in a human renal cell line, while decreases in O-GlcNAcylation augmented the current magnitude.
33330510	6	15	theme	YinOYang	1252:1259	arg1	site					1261:1264	the putative YinOYang site	1239:1264	the putative YinOYang site	1239:1264	Mutation of the putative YinOYang site at Ser67 rendered the ICln-induced IClswell current unresponsive to O-GlcNAc variations, and the ICln interaction with α-integrin insensitive to O-GlcNAcylation.
33330510	9	16	from	disturbances	1795:1806	arg1	regulation					1815:1824	the regulation	1811:1824	the regulation of cellular volume	1811:1843	We propose that disturbances in the regulation of cellular volume may contribute to disease in settings of chronically elevated O-GlcNAcylation, including diabetic nephropathy.
33330510	3	17	theme	IClswell	717:724	arg1	activation					703:712	the activation	699:712	the activation of IClswell	699:724	The activation of the swelling-induced chloride current IClswell is a key step in RVD, and ICln, a ubiquitous protein involved in the activation of IClswell, is O-GlcNAcylated.
33330510	6	18	theme	putative	1243:1250	arg1	site					1261:1264	the putative YinOYang site	1239:1264	the putative YinOYang site	1239:1264	Mutation of the putative YinOYang site at Ser67 rendered the ICln-induced IClswell current unresponsive to O-GlcNAc variations, and the ICln interaction with α-integrin insensitive to O-GlcNAcylation.
33330510	4	19	theme	current	992:998	arg1	magnitude					1000:1008	the current magnitude	988:1008	the current magnitude	988:1008	Here, we show that experimentally increased O-GlcNAcylation of cellular proteins inhibited the endogenous as well as the ICln-induced IClswell current and prevented RVD in a human renal cell line, while decreases in O-GlcNAcylation augmented the current magnitude.
33330510	9	20	theme	cellular	1829:1836	arg1	volume					1838:1843	cellular volume	1829:1843	cellular volume	1829:1843	We propose that disturbances in the regulation of cellular volume may contribute to disease in settings of chronically elevated O-GlcNAcylation, including diabetic nephropathy.
33330510	4	21	theme	renal	926:930	arg1	line					937:940	a human renal cell line	918:940	a human renal cell line	918:940	Here, we show that experimentally increased O-GlcNAcylation of cellular proteins inhibited the endogenous as well as the ICln-induced IClswell current and prevented RVD in a human renal cell line, while decreases in O-GlcNAcylation augmented the current magnitude.
33330510	2	22	theme	homeostatic	463:473	arg1	reaction					475:482	the homeostatic reaction	459:482	the homeostatic reaction of the regulatory volume decrease (RVD) after cell swelling	459:542	Our previous work showed that increases in the O-GlcNAcylation of cellular proteins impair the homeostatic reaction of the regulatory volume decrease (RVD) after cell swelling by an unknown mechanism.
33330510	5	23	from	decreases	1037:1045	arg1	O-GlcNAcylation					1050:1064	O-GlcNAcylation	1050:1064	O-GlcNAcylation	1050:1064	In parallel, increases or decreases in O-GlcNAcylation, respectively, weakened or stabilized the binding of ICln to the intracellular domain of α-integrin, a process that is essential for the activation of IClswell.
33330510	6	24	from	Ser67	1269:1273	arg1	Mutation					1227:1234	Mutation	1227:1234	Mutation of the putative YinOYang site at Ser67	1227:1273	Mutation of the putative YinOYang site at Ser67 rendered the ICln-induced IClswell current unresponsive to O-GlcNAc variations, and the ICln interaction with α-integrin insensitive to O-GlcNAcylation.
33330510	3	25	theme	ubiquitous	668:677	arg1	ICln					660:663	ICln	660:663	ICln	660:663	The activation of the swelling-induced chloride current IClswell is a key step in RVD, and ICln, a ubiquitous protein involved in the activation of IClswell, is O-GlcNAcylated.
33330510	3	25	theme	ubiquitous	668:677	arg1	protein					679:685	a ubiquitous protein	666:685	a ubiquitous protein involved in the activation of IClswell	666:724	The activation of the swelling-induced chloride current IClswell is a key step in RVD, and ICln, a ubiquitous protein involved in the activation of IClswell, is O-GlcNAcylated.
33330510	0	26	theme	Ion	31:33	arg1	IClswell					43:50	the Ion Current IClswell	27:50	the Ion Current IClswell	27:50	O-GlcNAcylation Suppresses the Ion Current IClswell by Preventing the Binding of the Protein ICln to α-Integrin.
33330510	6	27	theme	O-GlcNAc	1334:1341	arg1	variations					1343:1352	O-GlcNAc variations	1334:1352	O-GlcNAc variations	1334:1352	Mutation of the putative YinOYang site at Ser67 rendered the ICln-induced IClswell current unresponsive to O-GlcNAc variations, and the ICln interaction with α-integrin insensitive to O-GlcNAcylation.
33330510	4	28	theme	proteins	818:825	arg1	O-GlcNAcylation					790:804	experimentally increased O-GlcNAcylation	765:804	experimentally increased O-GlcNAcylation of cellular proteins	765:825	Here, we show that experimentally increased O-GlcNAcylation of cellular proteins inhibited the endogenous as well as the ICln-induced IClswell current and prevented RVD in a human renal cell line, while decreases in O-GlcNAcylation augmented the current magnitude.
33330510	6	29	theme	ICln	1363:1366	arg1	interaction					1368:1378	the ICln interaction	1359:1378	the ICln interaction with α-integrin insensitive to O-GlcNAcylation	1359:1425	Mutation of the putative YinOYang site at Ser67 rendered the ICln-induced IClswell current unresponsive to O-GlcNAc variations, and the ICln interaction with α-integrin insensitive to O-GlcNAcylation.
33330510	4	30	theme	cellular	809:816	arg1	proteins					818:825	cellular proteins	809:825	cellular proteins	809:825	Here, we show that experimentally increased O-GlcNAcylation of cellular proteins inhibited the endogenous as well as the ICln-induced IClswell current and prevented RVD in a human renal cell line, while decreases in O-GlcNAcylation augmented the current magnitude.
33330510	2	31	theme	cellular	434:441	arg1	proteins					443:450	cellular proteins	434:450	cellular proteins	434:450	Our previous work showed that increases in the O-GlcNAcylation of cellular proteins impair the homeostatic reaction of the regulatory volume decrease (RVD) after cell swelling by an unknown mechanism.
33330510	2	32	theme	proteins	443:450	arg1	O-GlcNAcylation					415:429	the O-GlcNAcylation	411:429	the O-GlcNAcylation of cellular proteins	411:450	Our previous work showed that increases in the O-GlcNAcylation of cellular proteins impair the homeostatic reaction of the regulatory volume decrease (RVD) after cell swelling by an unknown mechanism.
33330510	2	33	theme	unknown	550:556	arg1	mechanism					558:566	an unknown mechanism	547:566	an unknown mechanism	547:566	Our previous work showed that increases in the O-GlcNAcylation of cellular proteins impair the homeostatic reaction of the regulatory volume decrease (RVD) after cell swelling by an unknown mechanism.
33330510	1	34	theme	cellular	205:212	arg1	processes					214:222	cellular processes	205:222	cellular processes	205:222	O-GlcNAcylation is a post-translational modification of proteins that controls a variety of cellular processes, is chronically elevated in diabetes mellitus, and may contribute to the progression of diabetic complications, including diabetic nephropathy.
33330510	2	35	theme	regulatory	491:500	arg1	RVD					519:521	RVD	519:521	RVD	519:521	Our previous work showed that increases in the O-GlcNAcylation of cellular proteins impair the homeostatic reaction of the regulatory volume decrease (RVD) after cell swelling by an unknown mechanism.
33330510	2	35	theme	regulatory	491:500	arg1	decrease					509:516	the regulatory volume decrease	487:516	the regulatory volume decrease (RVD) after cell swelling	487:542	Our previous work showed that increases in the O-GlcNAcylation of cellular proteins impair the homeostatic reaction of the regulatory volume decrease (RVD) after cell swelling by an unknown mechanism.
33330510	4	36	theme	cell	932:935	arg1	line					937:940	a human renal cell line	918:940	a human renal cell line	918:940	Here, we show that experimentally increased O-GlcNAcylation of cellular proteins inhibited the endogenous as well as the ICln-induced IClswell current and prevented RVD in a human renal cell line, while decreases in O-GlcNAcylation augmented the current magnitude.
33330510	3	37	theme	chloride	608:615	arg1	current					617:623	the swelling-induced chloride current	587:623	the swelling-induced chloride current IClswell	587:632	The activation of the swelling-induced chloride current IClswell is a key step in RVD, and ICln, a ubiquitous protein involved in the activation of IClswell, is O-GlcNAcylated.
33330510	1	38	theme	processes	214:222	arg1	variety					194:200	a variety	192:200	a variety of cellular processes	192:222	O-GlcNAcylation is a post-translational modification of proteins that controls a variety of cellular processes, is chronically elevated in diabetes mellitus, and may contribute to the progression of diabetic complications, including diabetic nephropathy.
33330510	1	38	theme	processes	214:222	arg1	processes					214:222	cellular processes	205:222	cellular processes	205:222	O-GlcNAcylation is a post-translational modification of proteins that controls a variety of cellular processes, is chronically elevated in diabetes mellitus, and may contribute to the progression of diabetic complications, including diabetic nephropathy.
33330510	0	39	theme	Current	35:41	arg1	IClswell					43:50	the Ion Current IClswell	27:50	the Ion Current IClswell	27:50	O-GlcNAcylation Suppresses the Ion Current IClswell by Preventing the Binding of the Protein ICln to α-Integrin.
33330510	5	40	theme	intracellular	1131:1143	arg1	α-integrin					1155:1164	α-integrin	1155:1164	α-integrin	1155:1164	In parallel, increases or decreases in O-GlcNAcylation, respectively, weakened or stabilized the binding of ICln to the intracellular domain of α-integrin, a process that is essential for the activation of IClswell.
33330510	5	40	theme	intracellular	1131:1143	arg1	domain					1145:1150	the intracellular domain	1127:1150	the intracellular domain of α-integrin, a process that is essential for the activation of IClswell	1127:1224	In parallel, increases or decreases in O-GlcNAcylation, respectively, weakened or stabilized the binding of ICln to the intracellular domain of α-integrin, a process that is essential for the activation of IClswell.
33330510	4	41	theme	human	920:924	arg1	line					937:940	a human renal cell line	918:940	a human renal cell line	918:940	Here, we show that experimentally increased O-GlcNAcylation of cellular proteins inhibited the endogenous as well as the ICln-induced IClswell current and prevented RVD in a human renal cell line, while decreases in O-GlcNAcylation augmented the current magnitude.
33330510	6	42	theme	unresponsive	1318:1329	arg1	current					1310:1316	the ICln-induced IClswell current	1284:1316	the ICln-induced IClswell current unresponsive to O-GlcNAc variations, and the ICln interaction with α-integrin insensitive to O-GlcNAcylation	1284:1425	Mutation of the putative YinOYang site at Ser67 rendered the ICln-induced IClswell current unresponsive to O-GlcNAc variations, and the ICln interaction with α-integrin insensitive to O-GlcNAcylation.
33330510	3	43	theme	current	617:623	arg1	IClswell					625:632	the swelling-induced chloride current IClswell	587:632	the swelling-induced chloride current IClswell	587:632	The activation of the swelling-induced chloride current IClswell is a key step in RVD, and ICln, a ubiquitous protein involved in the activation of IClswell, is O-GlcNAcylated.
33330510	6	44	with	interaction	1368:1378	arg1	α-integrin					1385:1394	α-integrin	1385:1394	α-integrin insensitive to O-GlcNAcylation	1385:1425	Mutation of the putative YinOYang site at Ser67 rendered the ICln-induced IClswell current unresponsive to O-GlcNAc variations, and the ICln interaction with α-integrin insensitive to O-GlcNAcylation.
33330510	5	45	theme	α-integrin	1155:1164	arg1	α-integrin					1155:1164	α-integrin	1155:1164	α-integrin	1155:1164	In parallel, increases or decreases in O-GlcNAcylation, respectively, weakened or stabilized the binding of ICln to the intracellular domain of α-integrin, a process that is essential for the activation of IClswell.
33330510	5	45	theme	α-integrin	1155:1164	arg1	domain					1145:1150	the intracellular domain	1127:1150	the intracellular domain of α-integrin, a process that is essential for the activation of IClswell	1127:1224	In parallel, increases or decreases in O-GlcNAcylation, respectively, weakened or stabilized the binding of ICln to the intracellular domain of α-integrin, a process that is essential for the activation of IClswell.
33330510	3	46	from	step	643:646	arg1	RVD					651:653	RVD	651:653	RVD	651:653	The activation of the swelling-induced chloride current IClswell is a key step in RVD, and ICln, a ubiquitous protein involved in the activation of IClswell, is O-GlcNAcylated.
33330510	6	47	theme	IClswell	1301:1308	arg1	current					1310:1316	the ICln-induced IClswell current	1284:1316	the ICln-induced IClswell current unresponsive to O-GlcNAc variations, and the ICln interaction with α-integrin insensitive to O-GlcNAcylation	1284:1425	Mutation of the putative YinOYang site at Ser67 rendered the ICln-induced IClswell current unresponsive to O-GlcNAc variations, and the ICln interaction with α-integrin insensitive to O-GlcNAcylation.
33330510	8	48	from	Ser67	1724:1728	arg1	O-GlcNAcylation					1697:1711	the O-GlcNAcylation	1693:1711	the O-GlcNAcylation of ICln at Ser67	1693:1728	Together, these findings show that O-GlcNAcylation affects RVD by influencing IClswell and further indicate that hypotonicity may activate IClswell by reducing the O-GlcNAcylation of ICln at Ser67, therefore permitting its binding to α-integrin.
33330510	6	49	theme	insensitive	1396:1406	arg1	α-integrin					1385:1394	α-integrin	1385:1394	α-integrin insensitive to O-GlcNAcylation	1385:1425	Mutation of the putative YinOYang site at Ser67 rendered the ICln-induced IClswell current unresponsive to O-GlcNAc variations, and the ICln interaction with α-integrin insensitive to O-GlcNAcylation.
33330510	1	50	theme	diabetic	312:319	arg1	nephropathy					355:365	diabetic nephropathy	346:365	diabetic nephropathy	346:365	O-GlcNAcylation is a post-translational modification of proteins that controls a variety of cellular processes, is chronically elevated in diabetes mellitus, and may contribute to the progression of diabetic complications, including diabetic nephropathy.
33330510	1	50	theme	diabetic	312:319	arg1	complications					321:333	diabetic complications	312:333	diabetic complications	312:333	O-GlcNAcylation is a post-translational modification of proteins that controls a variety of cellular processes, is chronically elevated in diabetes mellitus, and may contribute to the progression of diabetic complications, including diabetic nephropathy.
33330510	6	51	theme	ICln-induced	1288:1299	arg1	current					1310:1316	the ICln-induced IClswell current	1284:1316	the ICln-induced IClswell current unresponsive to O-GlcNAc variations, and the ICln interaction with α-integrin insensitive to O-GlcNAcylation	1284:1425	Mutation of the putative YinOYang site at Ser67 rendered the ICln-induced IClswell current unresponsive to O-GlcNAc variations, and the ICln interaction with α-integrin insensitive to O-GlcNAcylation.
33330510	7	52	theme	cellular	1514:1521	arg1	proteins					1523:1530	cellular proteins	1514:1530	cellular proteins	1514:1530	In addition, exposure of cells to a hypotonic solution reduced the O-GlcNAcylation of cellular proteins.
33330510	3	53	theme	swelling-induced	591:606	arg1	current					617:623	the swelling-induced chloride current	587:623	the swelling-induced chloride current IClswell	587:632	The activation of the swelling-induced chloride current IClswell is a key step in RVD, and ICln, a ubiquitous protein involved in the activation of IClswell, is O-GlcNAcylated.
33330510	6	54	theme	site	1261:1264	arg1	Mutation					1227:1234	Mutation	1227:1234	Mutation of the putative YinOYang site at Ser67	1227:1273	Mutation of the putative YinOYang site at Ser67 rendered the ICln-induced IClswell current unresponsive to O-GlcNAc variations, and the ICln interaction with α-integrin insensitive to O-GlcNAcylation.
33330510	1	55	theme	complications	321:333	arg1	progression					297:307	the progression	293:307	the progression of diabetic complications, including diabetic nephropathy	293:365	O-GlcNAcylation is a post-translational modification of proteins that controls a variety of cellular processes, is chronically elevated in diabetes mellitus, and may contribute to the progression of diabetic complications, including diabetic nephropathy.
33330510	7	56	theme	proteins	1523:1530	arg1	O-GlcNAcylation					1495:1509	the O-GlcNAcylation	1491:1509	the O-GlcNAcylation of cellular proteins	1491:1530	In addition, exposure of cells to a hypotonic solution reduced the O-GlcNAcylation of cellular proteins.
33330510	2	57	from	increases	398:406	arg1	O-GlcNAcylation					415:429	the O-GlcNAcylation	411:429	the O-GlcNAcylation of cellular proteins	411:450	Our previous work showed that increases in the O-GlcNAcylation of cellular proteins impair the homeostatic reaction of the regulatory volume decrease (RVD) after cell swelling by an unknown mechanism.
33330510	3	58	theme	key	639:641	arg1	step					643:646	a key step	637:646	a key step in RVD	637:653	The activation of the swelling-induced chloride current IClswell is a key step in RVD, and ICln, a ubiquitous protein involved in the activation of IClswell, is O-GlcNAcylated.
33330510	3	58	theme	key	639:641	arg1	activation					573:582	The activation	569:582	The activation of the swelling-induced chloride current IClswell	569:632	The activation of the swelling-induced chloride current IClswell is a key step in RVD, and ICln, a ubiquitous protein involved in the activation of IClswell, is O-GlcNAcylated.
33330510	5	59	from	increases	1024:1032	arg1	O-GlcNAcylation					1050:1064	O-GlcNAcylation	1050:1064	O-GlcNAcylation	1050:1064	In parallel, increases or decreases in O-GlcNAcylation, respectively, weakened or stabilized the binding of ICln to the intracellular domain of α-integrin, a process that is essential for the activation of IClswell.
33330510	9	60	theme	diabetic	1934:1941	arg1	nephropathy					1943:1953	diabetic nephropathy	1934:1953	diabetic nephropathy	1934:1953	We propose that disturbances in the regulation of cellular volume may contribute to disease in settings of chronically elevated O-GlcNAcylation, including diabetic nephropathy.
33330510	3	61	theme	IClswell	625:632	arg1	step					643:646	a key step	637:646	a key step in RVD	637:653	The activation of the swelling-induced chloride current IClswell is a key step in RVD, and ICln, a ubiquitous protein involved in the activation of IClswell, is O-GlcNAcylated.
33330510	3	61	theme	IClswell	625:632	arg1	activation					573:582	The activation	569:582	The activation of the swelling-induced chloride current IClswell	569:632	The activation of the swelling-induced chloride current IClswell is a key step in RVD, and ICln, a ubiquitous protein involved in the activation of IClswell, is O-GlcNAcylated.
33330510	6	62	with	variations	1343:1352	arg1	α-integrin					1385:1394	α-integrin	1385:1394	α-integrin insensitive to O-GlcNAcylation	1385:1425	Mutation of the putative YinOYang site at Ser67 rendered the ICln-induced IClswell current unresponsive to O-GlcNAc variations, and the ICln interaction with α-integrin insensitive to O-GlcNAcylation.
33330510	1	63	theme	post-translational	134:151	arg1	modification					153:164	a post-translational modification	132:164	a post-translational modification of proteins that controls a variety of cellular processes, is chronically elevated in diabetes mellitus, and may contribute to the progression of diabetic complications, including diabetic nephropathy	132:365	O-GlcNAcylation is a post-translational modification of proteins that controls a variety of cellular processes, is chronically elevated in diabetes mellitus, and may contribute to the progression of diabetic complications, including diabetic nephropathy.
33330510	1	63	theme	post-translational	134:151	arg1	O-GlcNAcylation					113:127	O-GlcNAcylation	113:127	O-GlcNAcylation	113:127	O-GlcNAcylation is a post-translational modification of proteins that controls a variety of cellular processes, is chronically elevated in diabetes mellitus, and may contribute to the progression of diabetic complications, including diabetic nephropathy.
33330510	9	64	theme	elevated	1898:1905	arg1	O-GlcNAcylation					1907:1921	chronically elevated O-GlcNAcylation	1886:1921	chronically elevated O-GlcNAcylation	1886:1921	We propose that disturbances in the regulation of cellular volume may contribute to disease in settings of chronically elevated O-GlcNAcylation, including diabetic nephropathy.
33330510	5	65	theme	IClswell	1217:1224	arg1	activation					1203:1212	the activation	1199:1212	the activation of IClswell	1199:1224	In parallel, increases or decreases in O-GlcNAcylation, respectively, weakened or stabilized the binding of ICln to the intracellular domain of α-integrin, a process that is essential for the activation of IClswell.
33330510	4	66	theme	increased	780:788	arg1	O-GlcNAcylation					790:804	experimentally increased O-GlcNAcylation	765:804	experimentally increased O-GlcNAcylation of cellular proteins	765:825	Here, we show that experimentally increased O-GlcNAcylation of cellular proteins inhibited the endogenous as well as the ICln-induced IClswell current and prevented RVD in a human renal cell line, while decreases in O-GlcNAcylation augmented the current magnitude.
33330510	2	67	theme	previous	372:379	arg1	work					381:384	Our previous work	368:384	Our previous work	368:384	Our previous work showed that increases in the O-GlcNAcylation of cellular proteins impair the homeostatic reaction of the regulatory volume decrease (RVD) after cell swelling by an unknown mechanism.
33330510	9	68	theme	O-GlcNAcylation	1907:1921	arg1	settings					1874:1881	settings	1874:1881	settings	1874:1881	We propose that disturbances in the regulation of cellular volume may contribute to disease in settings of chronically elevated O-GlcNAcylation, including diabetic nephropathy.
33330510	9	68	theme	O-GlcNAcylation	1907:1921	arg1	nephropathy					1943:1953	diabetic nephropathy	1934:1953	diabetic nephropathy	1934:1953	We propose that disturbances in the regulation of cellular volume may contribute to disease in settings of chronically elevated O-GlcNAcylation, including diabetic nephropathy.
33330510	2	69	theme	cell	530:533	arg1	swelling					535:542	cell swelling	530:542	cell swelling	530:542	Our previous work showed that increases in the O-GlcNAcylation of cellular proteins impair the homeostatic reaction of the regulatory volume decrease (RVD) after cell swelling by an unknown mechanism.
31195810	11	0	theme	II-mediated	2198:2208	arg1	phosphorylation					2210:2224	Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation	2157:2224	Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation at Ser-632	2157:2235	Preventing O-GlcNAcylation at Ser-642 not only entirely precluded production of the N-terminal fragment of HDAC4 but also promoted Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation at Ser-632, pointing to a mutual posttranslational modification cross talk of (cardio-detrimental) phosphorylation at Ser-632 and (cardio-protective) O-GlcNAcylation at Ser-642.
31195810	7	1	theme	N-terminal	1255:1264	arg1	fragment					1278:1285	the cardio-protective N-terminal proteolytic fragment	1233:1285	the cardio-protective N-terminal proteolytic fragment of HDAC4	1233:1294	RESULTS We show that the cardio-protective N-terminal proteolytic fragment of HDAC4 is enhanced in vivo in patients with diabetes mellitus and mouse models, as well as in vitro under high-glucose and high-O-GlcNAc conditions.
31195810	11	2	from	talk	2296:2299	arg1	O-GlcNAcylation					2376:2390	(cardio-protective) O-GlcNAcylation	2356:2390	(cardio-protective) O-GlcNAcylation	2356:2390	Preventing O-GlcNAcylation at Ser-642 not only entirely precluded production of the N-terminal fragment of HDAC4 but also promoted Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation at Ser-632, pointing to a mutual posttranslational modification cross talk of (cardio-detrimental) phosphorylation at Ser-632 and (cardio-protective) O-GlcNAcylation at Ser-642.
31195810	11	2	from	talk	2296:2299	arg1	Ser-632					2344:2350	Ser-632	2344:2350	Ser-632	2344:2350	Preventing O-GlcNAcylation at Ser-642 not only entirely precluded production of the N-terminal fragment of HDAC4 but also promoted Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation at Ser-632, pointing to a mutual posttranslational modification cross talk of (cardio-detrimental) phosphorylation at Ser-632 and (cardio-protective) O-GlcNAcylation at Ser-642.
31195810	11	2	from	talk	2296:2299	arg1	Ser-642					2395:2401	Ser-642	2395:2401	Ser-642	2395:2401	Preventing O-GlcNAcylation at Ser-642 not only entirely precluded production of the N-terminal fragment of HDAC4 but also promoted Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation at Ser-632, pointing to a mutual posttranslational modification cross talk of (cardio-detrimental) phosphorylation at Ser-632 and (cardio-protective) O-GlcNAcylation at Ser-642.
31195810	3	3	theme	deacetylase	537:547	arg1	subdomain					559:567	a histone deacetylase 4 (HDAC4) subdomain	527:567	a histone deacetylase 4 (HDAC4) subdomain	527:567	Here, we identified a histone deacetylase 4 (HDAC4) subdomain as a molecular checkpoint of adaptive and maladaptive signaling in the diabetic heart.
31195810	3	3	theme	deacetylase	537:547	arg1	checkpoint					584:593	a molecular checkpoint	572:593	a molecular checkpoint of adaptive and maladaptive signaling in the diabetic heart	572:653	Here, we identified a histone deacetylase 4 (HDAC4) subdomain as a molecular checkpoint of adaptive and maladaptive signaling in the diabetic heart.
31195810	11	4	theme	protein	2183:2189	arg1	kinase					2191:2196	Ca2+/calmodulin-dependent protein kinase	2157:2196	Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation at Ser-632	2157:2235	Preventing O-GlcNAcylation at Ser-642 not only entirely precluded production of the N-terminal fragment of HDAC4 but also promoted Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation at Ser-632, pointing to a mutual posttranslational modification cross talk of (cardio-detrimental) phosphorylation at Ser-632 and (cardio-protective) O-GlcNAcylation at Ser-642.
31195810	6	5	theme	cellular	1195:1202	arg1	assays					1204:1209	biochemical and cellular assays	1179:1209	biochemical and cellular assays	1179:1209	Effects of glucose and the posttranslational modification by β-linked N-acetylglucosamine (O-GlcNAc) on HDAC4 were investigated in vivo and in vitro by biochemical and cellular assays.
31195810	1	6	theme	BACKGROUND	83:92	arg1	Worldwide					94:102	BACKGROUND Worldwide	83:102	BACKGROUND Worldwide	83:102	BACKGROUND Worldwide, diabetes mellitus and heart failure represent frequent comorbidities with high socioeconomic impact and steadily growing incidence, calling for a better understanding of how diabetic metabolism promotes cardiac dysfunction.
31195810	10	7	theme	kinase	1979:1984	arg1	phosphorylation					1998:2012	Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation	1945:2012	Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation at Ser-632	1945:2023	Mechanistically, the posttranslational modification of HDAC4 at serine (Ser)-642 by O-GlcNAcylation is an essential step for production of the N-terminal fragment of HDAC4, which was attenuated by Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation at Ser-632.
31195810	12	8	from	cardio-protective	2484:2500	arg1	mellitus					2514:2521	diabetes mellitus	2505:2521	diabetes mellitus	2505:2521	CONCLUSIONS In this study, we found that O-GlcNAcylation of HDAC4 at Ser-642 is cardio-protective in diabetes mellitus and counteracts pathological Ca2+/calmodulin-dependent protein kinase II signaling.
31195810	6	9	from	N-acetylglucosamine	1097:1115	arg1	HDAC4					1131:1135	HDAC4	1131:1135	HDAC4	1131:1135	Effects of glucose and the posttranslational modification by β-linked N-acetylglucosamine (O-GlcNAc) on HDAC4 were investigated in vivo and in vitro by biochemical and cellular assays.
31195810	1	10	theme	diabetic	279:286	arg1	metabolism					288:297	diabetic metabolism	279:297	diabetic metabolism	279:297	BACKGROUND Worldwide, diabetes mellitus and heart failure represent frequent comorbidities with high socioeconomic impact and steadily growing incidence, calling for a better understanding of how diabetic metabolism promotes cardiac dysfunction.
31195810	9	11	theme	N-terminal	1669:1678	arg1	fragment					1680:1687	the N-terminal fragment	1665:1687	the N-terminal fragment of HDAC4	1665:1696	Reexpression of the N-terminal fragment of HDAC4 prevents HDAC4-dependent diabetic cardiomyopathy.
31195810	6	12	theme	biochemical	1179:1189	arg1	assays					1204:1209	biochemical and cellular assays	1179:1209	biochemical and cellular assays	1179:1209	Effects of glucose and the posttranslational modification by β-linked N-acetylglucosamine (O-GlcNAc) on HDAC4 were investigated in vivo and in vitro by biochemical and cellular assays.
31195810	10	13	theme	Ca2+/calmodulin-dependent	1945:1969	arg1	kinase					1979:1984	Ca2+/calmodulin-dependent protein kinase	1945:1984	Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation at Ser-632	1945:2023	Mechanistically, the posttranslational modification of HDAC4 at serine (Ser)-642 by O-GlcNAcylation is an essential step for production of the N-terminal fragment of HDAC4, which was attenuated by Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation at Ser-632.
31195810	12	14	from	Ser-642	2473:2479	arg1	O-GlcNAcylation					2445:2459	O-GlcNAcylation	2445:2459	O-GlcNAcylation of HDAC4 at Ser-642	2445:2479	CONCLUSIONS In this study, we found that O-GlcNAcylation of HDAC4 at Ser-642 is cardio-protective in diabetes mellitus and counteracts pathological Ca2+/calmodulin-dependent protein kinase II signaling.
31195810	10	15	theme	posttranslational	1769:1785	arg1	modification					1787:1798	the posttranslational modification	1765:1798	the posttranslational modification of HDAC4 at serine (Ser)-642 by O-GlcNAcylation	1765:1846	Mechanistically, the posttranslational modification of HDAC4 at serine (Ser)-642 by O-GlcNAcylation is an essential step for production of the N-terminal fragment of HDAC4, which was attenuated by Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation at Ser-632.
31195810	10	15	theme	posttranslational	1769:1785	arg1	step					1864:1867	an essential step	1851:1867	an essential step for production of the N-terminal fragment of HDAC4, which was attenuated by Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation at Ser-632	1851:2023	Mechanistically, the posttranslational modification of HDAC4 at serine (Ser)-642 by O-GlcNAcylation is an essential step for production of the N-terminal fragment of HDAC4, which was attenuated by Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation at Ser-632.
31195810	1	16	theme	socioeconomic	184:196	arg1	impact					198:203	high socioeconomic impact	179:203	high socioeconomic impact	179:203	BACKGROUND Worldwide, diabetes mellitus and heart failure represent frequent comorbidities with high socioeconomic impact and steadily growing incidence, calling for a better understanding of how diabetic metabolism promotes cardiac dysfunction.
31195810	12	17	theme	Ca2+/calmodulin-dependent	2552:2576	arg1	kinase					2586:2591	pathological Ca2+/calmodulin-dependent protein kinase II	2539:2594	pathological Ca2+/calmodulin-dependent protein kinase II signaling	2539:2604	CONCLUSIONS In this study, we found that O-GlcNAcylation of HDAC4 at Ser-642 is cardio-protective in diabetes mellitus and counteracts pathological Ca2+/calmodulin-dependent protein kinase II signaling.
31195810	7	18	theme	high-O-GlcNAc	1412:1424	arg1	conditions					1426:1435	high-glucose and high-O-GlcNAc conditions	1395:1435	high-glucose and high-O-GlcNAc conditions	1395:1435	RESULTS We show that the cardio-protective N-terminal proteolytic fragment of HDAC4 is enhanced in vivo in patients with diabetes mellitus and mouse models, as well as in vitro under high-glucose and high-O-GlcNAc conditions.
31195810	13	19	theme	important	2683:2691	arg1	features					2711:2718	important cardio-protective features	2683:2718	important cardio-protective features besides its known detrimental effects	2683:2756	We introduce a molecular model explaining how diabetic metabolism possesses important cardio-protective features besides its known detrimental effects.
31195810	7	20	theme	high-glucose	1395:1406	arg1	conditions					1426:1435	high-glucose and high-O-GlcNAc conditions	1395:1435	high-glucose and high-O-GlcNAc conditions	1395:1435	RESULTS We show that the cardio-protective N-terminal proteolytic fragment of HDAC4 is enhanced in vivo in patients with diabetes mellitus and mouse models, as well as in vitro under high-glucose and high-O-GlcNAc conditions.
31195810	3	21	theme	molecular	574:582	arg1	subdomain					559:567	a histone deacetylase 4 (HDAC4) subdomain	527:567	a histone deacetylase 4 (HDAC4) subdomain	527:567	Here, we identified a histone deacetylase 4 (HDAC4) subdomain as a molecular checkpoint of adaptive and maladaptive signaling in the diabetic heart.
31195810	3	21	theme	molecular	574:582	arg1	checkpoint					584:593	a molecular checkpoint	572:593	a molecular checkpoint of adaptive and maladaptive signaling in the diabetic heart	572:653	Here, we identified a histone deacetylase 4 (HDAC4) subdomain as a molecular checkpoint of adaptive and maladaptive signaling in the diabetic heart.
31195810	1	22	theme	growing	218:224	arg1	incidence					226:234	steadily growing incidence	209:234	steadily growing incidence	209:234	BACKGROUND Worldwide, diabetes mellitus and heart failure represent frequent comorbidities with high socioeconomic impact and steadily growing incidence, calling for a better understanding of how diabetic metabolism promotes cardiac dysfunction.
31195810	14	23	theme	cross	2835:2839	arg1	talk					2841:2844	the here-described posttranslational modification cross talk	2785:2844	the here-described posttranslational modification cross talk	2785:2844	A deeper understanding of the here-described posttranslational modification cross talk may lay the groundwork for the development of specific therapeutic concepts to treat heart failure in the context of diabetes mellitus.
31195810	9	24	theme	diabetic	1723:1730	arg1	cardiomyopathy					1732:1745	HDAC4-dependent diabetic cardiomyopathy	1707:1745	HDAC4-dependent diabetic cardiomyopathy	1707:1745	Reexpression of the N-terminal fragment of HDAC4 prevents HDAC4-dependent diabetic cardiomyopathy.
31195810	8	25	theme	heart	1466:1470	arg1	failure					1472:1478	heart failure	1466:1478	heart failure	1466:1478	HDAC4-knockout mice develop heart failure in models of type 1 and type 2 diabetes mellitus, whereas wild-type mice do not develop clear signs of heart failure, indicating that HDAC4 protects the diabetic heart.
31195810	4	26	theme	conditional	666:676	arg1	allele					684:689	A conditional HDAC4 allele	664:689	A conditional HDAC4 allele	664:689	METHODS A conditional HDAC4 allele was used to delete HDAC4 specifically in cardiomyocytes (HDAC4-knockout).
31195810	3	27	theme	signaling	623:631	arg1	subdomain					559:567	a histone deacetylase 4 (HDAC4) subdomain	527:567	a histone deacetylase 4 (HDAC4) subdomain	527:567	Here, we identified a histone deacetylase 4 (HDAC4) subdomain as a molecular checkpoint of adaptive and maladaptive signaling in the diabetic heart.
31195810	3	27	theme	signaling	623:631	arg1	checkpoint					584:593	a molecular checkpoint	572:593	a molecular checkpoint of adaptive and maladaptive signaling in the diabetic heart	572:653	Here, we identified a histone deacetylase 4 (HDAC4) subdomain as a molecular checkpoint of adaptive and maladaptive signaling in the diabetic heart.
31195810	14	28	theme	posttranslational	2804:2820	arg1	modification					2822:2833	the here-described posttranslational modification	2785:2833	the here-described posttranslational modification cross talk	2785:2844	A deeper understanding of the here-described posttranslational modification cross talk may lay the groundwork for the development of specific therapeutic concepts to treat heart failure in the context of diabetes mellitus.
31195810	10	29	theme	essential	1854:1862	arg1	modification					1787:1798	the posttranslational modification	1765:1798	the posttranslational modification of HDAC4 at serine (Ser)-642 by O-GlcNAcylation	1765:1846	Mechanistically, the posttranslational modification of HDAC4 at serine (Ser)-642 by O-GlcNAcylation is an essential step for production of the N-terminal fragment of HDAC4, which was attenuated by Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation at Ser-632.
31195810	10	29	theme	essential	1854:1862	arg1	step					1864:1867	an essential step	1851:1867	an essential step for production of the N-terminal fragment of HDAC4, which was attenuated by Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation at Ser-632	1851:2023	Mechanistically, the posttranslational modification of HDAC4 at serine (Ser)-642 by O-GlcNAcylation is an essential step for production of the N-terminal fragment of HDAC4, which was attenuated by Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation at Ser-632.
31195810	14	30	theme	diabetes	2963:2970	arg1	mellitus					2972:2979	diabetes mellitus	2963:2979	diabetes mellitus	2963:2979	A deeper understanding of the here-described posttranslational modification cross talk may lay the groundwork for the development of specific therapeutic concepts to treat heart failure in the context of diabetes mellitus.
31195810	14	31	theme	heart	2931:2935	arg1	failure					2937:2943	heart failure	2931:2943	heart failure	2931:2943	A deeper understanding of the here-described posttranslational modification cross talk may lay the groundwork for the development of specific therapeutic concepts to treat heart failure in the context of diabetes mellitus.
31195810	7	32	theme	cardio-protective	1237:1253	arg1	fragment					1278:1285	the cardio-protective N-terminal proteolytic fragment	1233:1285	the cardio-protective N-terminal proteolytic fragment of HDAC4	1233:1294	RESULTS We show that the cardio-protective N-terminal proteolytic fragment of HDAC4 is enhanced in vivo in patients with diabetes mellitus and mouse models, as well as in vitro under high-glucose and high-O-GlcNAc conditions.
31195810	5	33	theme	diabetes	850:857	arg1	mellitus					859:866	type 1 diabetes mellitus	843:866	type 1 diabetes mellitus model	843:872	Mice were subjected to diabetes mellitus either by streptozotocin injections (type 1 diabetes mellitus model) or by crossing into mice carrying a leptin receptor mutation (db/db; type 2 diabetes mellitus model) and monitored for remodeling and cardiac function.
31195810	1	34	theme	frequent	151:158	arg1	comorbidities					160:172	frequent comorbidities	151:172	frequent comorbidities with high socioeconomic impact and steadily growing incidence	151:234	BACKGROUND Worldwide, diabetes mellitus and heart failure represent frequent comorbidities with high socioeconomic impact and steadily growing incidence, calling for a better understanding of how diabetic metabolism promotes cardiac dysfunction.
31195810	10	35	from	serine	1812:1817	arg1	modification					1787:1798	the posttranslational modification	1765:1798	the posttranslational modification of HDAC4 at serine (Ser)-642 by O-GlcNAcylation	1765:1846	Mechanistically, the posttranslational modification of HDAC4 at serine (Ser)-642 by O-GlcNAcylation is an essential step for production of the N-terminal fragment of HDAC4, which was attenuated by Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation at Ser-632.
31195810	10	35	from	serine	1812:1817	arg1	step					1864:1867	an essential step	1851:1867	an essential step for production of the N-terminal fragment of HDAC4, which was attenuated by Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation at Ser-632	1851:2023	Mechanistically, the posttranslational modification of HDAC4 at serine (Ser)-642 by O-GlcNAcylation is an essential step for production of the N-terminal fragment of HDAC4, which was attenuated by Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation at Ser-632.
31195810	8	36	theme	type	1504:1507	arg1	mellitus					1520:1527	type 1 and type 2 diabetes mellitus	1493:1527	mellitus	1520:1527	HDAC4-knockout mice develop heart failure in models of type 1 and type 2 diabetes mellitus, whereas wild-type mice do not develop clear signs of heart failure, indicating that HDAC4 protects the diabetic heart.
31195810	5	37	contain	carrying	900:907	arg2	mutation					927:934	a leptin receptor mutation	909:934	a leptin receptor mutation (db/db; type 2 diabetes mellitus model)	909:974	Mice were subjected to diabetes mellitus either by streptozotocin injections (type 1 diabetes mellitus model) or by crossing into mice carrying a leptin receptor mutation (db/db; type 2 diabetes mellitus model) and monitored for remodeling and cardiac function.
31195810	5	37	contain	carrying	900:907	arg1	mice					895:898	mice	895:898	mice carrying a leptin receptor mutation (db/db; type 2 diabetes mellitus model)	895:974	Mice were subjected to diabetes mellitus either by streptozotocin injections (type 1 diabetes mellitus model) or by crossing into mice carrying a leptin receptor mutation (db/db; type 2 diabetes mellitus model) and monitored for remodeling and cardiac function.
31195810	5	38	theme	receptor	918:925	arg1	mutation					927:934	a leptin receptor mutation	909:934	a leptin receptor mutation (db/db; type 2 diabetes mellitus model)	909:974	Mice were subjected to diabetes mellitus either by streptozotocin injections (type 1 diabetes mellitus model) or by crossing into mice carrying a leptin receptor mutation (db/db; type 2 diabetes mellitus model) and monitored for remodeling and cardiac function.
31195810	8	39	theme	diabetes	1511:1518	arg1	mellitus					1520:1527	type 1 and type 2 diabetes mellitus	1493:1527	mellitus	1520:1527	HDAC4-knockout mice develop heart failure in models of type 1 and type 2 diabetes mellitus, whereas wild-type mice do not develop clear signs of heart failure, indicating that HDAC4 protects the diabetic heart.
31195810	5	40	dep	db/db	937:941	arg1	model					969:973	type 2 diabetes mellitus model	944:973	db/db; type 2 diabetes mellitus model	937:973	Mice were subjected to diabetes mellitus either by streptozotocin injections (type 1 diabetes mellitus model) or by crossing into mice carrying a leptin receptor mutation (db/db; type 2 diabetes mellitus model) and monitored for remodeling and cardiac function.
31195810	1	41	theme	diabetes	105:112	arg1	mellitus					114:121	diabetes mellitus	105:121	diabetes mellitus	105:121	BACKGROUND Worldwide, diabetes mellitus and heart failure represent frequent comorbidities with high socioeconomic impact and steadily growing incidence, calling for a better understanding of how diabetic metabolism promotes cardiac dysfunction.
31195810	5	42	dep	mutation	927:934	arg1	db/db					937:941	db/db	937:941	db/db; type 2 diabetes mellitus model	937:973	Mice were subjected to diabetes mellitus either by streptozotocin injections (type 1 diabetes mellitus model) or by crossing into mice carrying a leptin receptor mutation (db/db; type 2 diabetes mellitus model) and monitored for remodeling and cardiac function.
31195810	6	43	theme	β-linked	1088:1095	arg1	O-GlcNAc					1118:1125	O-GlcNAc	1118:1125	O-GlcNAc	1118:1125	Effects of glucose and the posttranslational modification by β-linked N-acetylglucosamine (O-GlcNAc) on HDAC4 were investigated in vivo and in vitro by biochemical and cellular assays.
31195810	6	43	theme	β-linked	1088:1095	arg1	N-acetylglucosamine					1097:1115	β-linked N-acetylglucosamine	1088:1115	β-linked N-acetylglucosamine (O-GlcNAc) on HDAC4	1088:1135	Effects of glucose and the posttranslational modification by β-linked N-acetylglucosamine (O-GlcNAc) on HDAC4 were investigated in vivo and in vitro by biochemical and cellular assays.
31195810	2	44	theme	detrimental	476:486	arg1	signaling					496:504	protective versus detrimental cardiac signaling	458:504	protective versus detrimental cardiac signaling	458:504	Paradoxically, some glucose-lowering drugs have been shown to worsen heart failure, raising the question of how glucose mediates protective versus detrimental cardiac signaling.
31195810	8	45	theme	wild-type	1538:1546	arg1	mice					1548:1551	wild-type mice	1538:1551	wild-type mice	1538:1551	HDAC4-knockout mice develop heart failure in models of type 1 and type 2 diabetes mellitus, whereas wild-type mice do not develop clear signs of heart failure, indicating that HDAC4 protects the diabetic heart.
31195810	11	46	theme	posttranslational	2259:2275	arg1	modification					2277:2288	a mutual posttranslational modification	2250:2288	a mutual posttranslational modification cross talk of (cardio-detrimental) phosphorylation at Ser-632 and (cardio-protective) O-GlcNAcylation at Ser-642	2250:2401	Preventing O-GlcNAcylation at Ser-642 not only entirely precluded production of the N-terminal fragment of HDAC4 but also promoted Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation at Ser-632, pointing to a mutual posttranslational modification cross talk of (cardio-detrimental) phosphorylation at Ser-632 and (cardio-protective) O-GlcNAcylation at Ser-642.
31195810	5	47	theme	type	843:846	arg1	mellitus					859:866	type 1 diabetes mellitus	843:866	type 1 diabetes mellitus model	843:872	Mice were subjected to diabetes mellitus either by streptozotocin injections (type 1 diabetes mellitus model) or by crossing into mice carrying a leptin receptor mutation (db/db; type 2 diabetes mellitus model) and monitored for remodeling and cardiac function.
31195810	2	48	theme	protective	458:467	arg1	signaling					496:504	protective versus detrimental cardiac signaling	458:504	protective versus detrimental cardiac signaling	458:504	Paradoxically, some glucose-lowering drugs have been shown to worsen heart failure, raising the question of how glucose mediates protective versus detrimental cardiac signaling.
31195810	12	49	theme	protein	2578:2584	arg1	kinase					2586:2591	pathological Ca2+/calmodulin-dependent protein kinase II	2539:2594	pathological Ca2+/calmodulin-dependent protein kinase II signaling	2539:2604	CONCLUSIONS In this study, we found that O-GlcNAcylation of HDAC4 at Ser-642 is cardio-protective in diabetes mellitus and counteracts pathological Ca2+/calmodulin-dependent protein kinase II signaling.
31195810	0	50	theme	Histone	19:25	arg1	Deacetylase					27:37	Histone Deacetylase 4	19:39	Histone Deacetylase 4	19:39	O-GlcNAcylation of Histone Deacetylase 4 Protects the Diabetic Heart From Failure.
31195810	1	51	theme	cardiac	308:314	arg1	dysfunction					316:326	cardiac dysfunction	308:326	cardiac dysfunction	308:326	BACKGROUND Worldwide, diabetes mellitus and heart failure represent frequent comorbidities with high socioeconomic impact and steadily growing incidence, calling for a better understanding of how diabetic metabolism promotes cardiac dysfunction.
31195810	5	52	theme	mellitus	960:967	arg1	model					969:973	type 2 diabetes mellitus model	944:973	db/db; type 2 diabetes mellitus model	937:973	Mice were subjected to diabetes mellitus either by streptozotocin injections (type 1 diabetes mellitus model) or by crossing into mice carrying a leptin receptor mutation (db/db; type 2 diabetes mellitus model) and monitored for remodeling and cardiac function.
31195810	11	53	from	Ser-632	2344:2350	arg1	phosphorylation					2325:2339	(cardio-detrimental) phosphorylation	2304:2339	(cardio-detrimental) phosphorylation at Ser-632 and (cardio-protective) O-GlcNAcylation at Ser-642	2304:2401	Preventing O-GlcNAcylation at Ser-642 not only entirely precluded production of the N-terminal fragment of HDAC4 but also promoted Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation at Ser-632, pointing to a mutual posttranslational modification cross talk of (cardio-detrimental) phosphorylation at Ser-632 and (cardio-protective) O-GlcNAcylation at Ser-642.
31195810	11	53	from	Ser-632	2344:2350	arg1	talk					2296:2299	a mutual posttranslational modification cross talk	2250:2299	a mutual posttranslational modification cross talk of (cardio-detrimental) phosphorylation at Ser-632 and (cardio-protective) O-GlcNAcylation at Ser-642	2250:2401	Preventing O-GlcNAcylation at Ser-642 not only entirely precluded production of the N-terminal fragment of HDAC4 but also promoted Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation at Ser-632, pointing to a mutual posttranslational modification cross talk of (cardio-detrimental) phosphorylation at Ser-632 and (cardio-protective) O-GlcNAcylation at Ser-642.
31195810	13	54	theme	detrimental	2738:2748	arg1	effects					2750:2756	its known detrimental effects	2728:2756	its known detrimental effects	2728:2756	We introduce a molecular model explaining how diabetic metabolism possesses important cardio-protective features besides its known detrimental effects.
31195810	13	55	contain	possesses	2673:2681	arg2	features					2711:2718	important cardio-protective features	2683:2718	important cardio-protective features besides its known detrimental effects	2683:2756	We introduce a molecular model explaining how diabetic metabolism possesses important cardio-protective features besides its known detrimental effects.
31195810	13	55	contain	possesses	2673:2681	arg1	metabolism					2662:2671	diabetic metabolism	2653:2671	diabetic metabolism	2653:2671	We introduce a molecular model explaining how diabetic metabolism possesses important cardio-protective features besides its known detrimental effects.
31195810	6	56	theme	glucose	1038:1044	arg1	Effects					1027:1033	Effects	1027:1033	Effects of glucose	1027:1044	Effects of glucose and the posttranslational modification by β-linked N-acetylglucosamine (O-GlcNAc) on HDAC4 were investigated in vivo and in vitro by biochemical and cellular assays.
31195810	6	56	theme	glucose	1038:1044	arg1	modification					1072:1083	the posttranslational modification	1050:1083	the posttranslational modification by β-linked N-acetylglucosamine (O-GlcNAc) on HDAC4	1050:1135	Effects of glucose and the posttranslational modification by β-linked N-acetylglucosamine (O-GlcNAc) on HDAC4 were investigated in vivo and in vitro by biochemical and cellular assays.
31195810	11	57	theme	modification	2277:2288	arg1	talk					2296:2299	a mutual posttranslational modification cross talk	2250:2299	a mutual posttranslational modification cross talk of (cardio-detrimental) phosphorylation at Ser-632 and (cardio-protective) O-GlcNAcylation at Ser-642	2250:2401	Preventing O-GlcNAcylation at Ser-642 not only entirely precluded production of the N-terminal fragment of HDAC4 but also promoted Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation at Ser-632, pointing to a mutual posttranslational modification cross talk of (cardio-detrimental) phosphorylation at Ser-632 and (cardio-protective) O-GlcNAcylation at Ser-642.
31195810	14	58	theme	specific	2892:2899	arg1	concepts					2913:2920	specific therapeutic concepts	2892:2920	specific therapeutic concepts	2892:2920	A deeper understanding of the here-described posttranslational modification cross talk may lay the groundwork for the development of specific therapeutic concepts to treat heart failure in the context of diabetes mellitus.
31195810	8	59	theme	heart	1583:1587	arg1	failure					1589:1595	heart failure	1583:1595	heart failure	1583:1595	HDAC4-knockout mice develop heart failure in models of type 1 and type 2 diabetes mellitus, whereas wild-type mice do not develop clear signs of heart failure, indicating that HDAC4 protects the diabetic heart.
31195810	7	60	dep	RESULTS	1212:1218	arg1	show					1223:1226	show	1223:1226	show that the cardio-protective N-terminal proteolytic fragment of HDAC4 is enhanced in vivo in patients with diabetes mellitus and mouse models, as well as in vitro under high-glucose and high-O-GlcNAc conditions	1223:1435	RESULTS We show that the cardio-protective N-terminal proteolytic fragment of HDAC4 is enhanced in vivo in patients with diabetes mellitus and mouse models, as well as in vitro under high-glucose and high-O-GlcNAc conditions.
31195810	8	61	theme	HDAC4-knockout	1438:1451	arg1	mice					1453:1456	HDAC4-knockout mice	1438:1456	HDAC4-knockout mice	1438:1456	HDAC4-knockout mice develop heart failure in models of type 1 and type 2 diabetes mellitus, whereas wild-type mice do not develop clear signs of heart failure, indicating that HDAC4 protects the diabetic heart.
31195810	10	62	theme	N-terminal	1891:1900	arg1	fragment					1902:1909	the N-terminal fragment	1887:1909	the N-terminal fragment of HDAC4	1887:1918	Mechanistically, the posttranslational modification of HDAC4 at serine (Ser)-642 by O-GlcNAcylation is an essential step for production of the N-terminal fragment of HDAC4, which was attenuated by Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation at Ser-632.
31195810	2	63	theme	heart	398:402	arg1	failure					404:410	heart failure	398:410	heart failure	398:410	Paradoxically, some glucose-lowering drugs have been shown to worsen heart failure, raising the question of how glucose mediates protective versus detrimental cardiac signaling.
31195810	5	64	theme	streptozotocin	816:829	arg1	injections					831:840	streptozotocin injections	816:840	streptozotocin injections (type 1 diabetes mellitus model)	816:873	Mice were subjected to diabetes mellitus either by streptozotocin injections (type 1 diabetes mellitus model) or by crossing into mice carrying a leptin receptor mutation (db/db; type 2 diabetes mellitus model) and monitored for remodeling and cardiac function.
31195810	5	64	theme	streptozotocin	816:829	arg1	model					868:872	type 1 diabetes mellitus model	843:872	type 1 diabetes mellitus model	843:872	Mice were subjected to diabetes mellitus either by streptozotocin injections (type 1 diabetes mellitus model) or by crossing into mice carrying a leptin receptor mutation (db/db; type 2 diabetes mellitus model) and monitored for remodeling and cardiac function.
31195810	5	65	theme	cardiac	1009:1015	arg1	function					1017:1024	cardiac function	1009:1024	cardiac function	1009:1024	Mice were subjected to diabetes mellitus either by streptozotocin injections (type 1 diabetes mellitus model) or by crossing into mice carrying a leptin receptor mutation (db/db; type 2 diabetes mellitus model) and monitored for remodeling and cardiac function.
31195810	12	66	theme	diabetes	2505:2512	arg1	mellitus					2514:2521	diabetes mellitus	2505:2521	diabetes mellitus	2505:2521	CONCLUSIONS In this study, we found that O-GlcNAcylation of HDAC4 at Ser-642 is cardio-protective in diabetes mellitus and counteracts pathological Ca2+/calmodulin-dependent protein kinase II signaling.
31195810	13	67	theme	cardio-protective	2693:2709	arg1	features					2711:2718	important cardio-protective features	2683:2718	important cardio-protective features besides its known detrimental effects	2683:2756	We introduce a molecular model explaining how diabetic metabolism possesses important cardio-protective features besides its known detrimental effects.
31195810	3	68	theme	histone	529:535	arg1	deacetylase					537:547	histone deacetylase 4	529:549	a histone deacetylase 4 (HDAC4) subdomain	527:567	Here, we identified a histone deacetylase 4 (HDAC4) subdomain as a molecular checkpoint of adaptive and maladaptive signaling in the diabetic heart.
31195810	3	68	theme	histone	529:535	arg1	HDAC4					552:556	HDAC4	552:556	HDAC4	552:556	Here, we identified a histone deacetylase 4 (HDAC4) subdomain as a molecular checkpoint of adaptive and maladaptive signaling in the diabetic heart.
31195810	7	69	theme	proteolytic	1266:1276	arg1	fragment					1278:1285	the cardio-protective N-terminal proteolytic fragment	1233:1285	the cardio-protective N-terminal proteolytic fragment of HDAC4	1233:1294	RESULTS We show that the cardio-protective N-terminal proteolytic fragment of HDAC4 is enhanced in vivo in patients with diabetes mellitus and mouse models, as well as in vitro under high-glucose and high-O-GlcNAc conditions.
31195810	12	70	theme	HDAC4	2464:2468	arg1	O-GlcNAcylation					2445:2459	O-GlcNAcylation	2445:2459	O-GlcNAcylation of HDAC4 at Ser-642	2445:2479	CONCLUSIONS In this study, we found that O-GlcNAcylation of HDAC4 at Ser-642 is cardio-protective in diabetes mellitus and counteracts pathological Ca2+/calmodulin-dependent protein kinase II signaling.
31195810	6	71	link	β-linked	1088:1095	arg1	O-GlcNAc					1118:1125	O-GlcNAc	1118:1125	O-GlcNAc	1118:1125	Effects of glucose and the posttranslational modification by β-linked N-acetylglucosamine (O-GlcNAc) on HDAC4 were investigated in vivo and in vitro by biochemical and cellular assays.
31195810	6	71	link	β-linked	1088:1095	arg1	N-acetylglucosamine					1097:1115	β-linked N-acetylglucosamine	1088:1115	β-linked N-acetylglucosamine (O-GlcNAc) on HDAC4	1088:1135	Effects of glucose and the posttranslational modification by β-linked N-acetylglucosamine (O-GlcNAc) on HDAC4 were investigated in vivo and in vitro by biochemical and cellular assays.
31195810	10	72	theme	HDAC4	1803:1807	arg1	modification					1787:1798	the posttranslational modification	1765:1798	the posttranslational modification of HDAC4 at serine (Ser)-642 by O-GlcNAcylation	1765:1846	Mechanistically, the posttranslational modification of HDAC4 at serine (Ser)-642 by O-GlcNAcylation is an essential step for production of the N-terminal fragment of HDAC4, which was attenuated by Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation at Ser-632.
31195810	10	72	theme	HDAC4	1803:1807	arg1	step					1864:1867	an essential step	1851:1867	an essential step for production of the N-terminal fragment of HDAC4, which was attenuated by Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation at Ser-632	1851:2023	Mechanistically, the posttranslational modification of HDAC4 at serine (Ser)-642 by O-GlcNAcylation is an essential step for production of the N-terminal fragment of HDAC4, which was attenuated by Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation at Ser-632.
31195810	11	73	theme	kinase	2191:2196	arg1	phosphorylation					2210:2224	Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation	2157:2224	Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation at Ser-632	2157:2235	Preventing O-GlcNAcylation at Ser-642 not only entirely precluded production of the N-terminal fragment of HDAC4 but also promoted Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation at Ser-632, pointing to a mutual posttranslational modification cross talk of (cardio-detrimental) phosphorylation at Ser-632 and (cardio-protective) O-GlcNAcylation at Ser-642.
31195810	8	74	theme	diabetic	1633:1640	arg1	heart					1642:1646	the diabetic heart	1629:1646	the diabetic heart	1629:1646	HDAC4-knockout mice develop heart failure in models of type 1 and type 2 diabetes mellitus, whereas wild-type mice do not develop clear signs of heart failure, indicating that HDAC4 protects the diabetic heart.
31195810	10	75	theme	protein	1971:1977	arg1	kinase					1979:1984	Ca2+/calmodulin-dependent protein kinase	1945:1984	Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation at Ser-632	1945:2023	Mechanistically, the posttranslational modification of HDAC4 at serine (Ser)-642 by O-GlcNAcylation is an essential step for production of the N-terminal fragment of HDAC4, which was attenuated by Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation at Ser-632.
31195810	13	76	theme	diabetic	2653:2660	arg1	metabolism					2662:2671	diabetic metabolism	2653:2671	diabetic metabolism	2653:2671	We introduce a molecular model explaining how diabetic metabolism possesses important cardio-protective features besides its known detrimental effects.
31195810	1	77	theme	high	179:182	arg1	impact					198:203	high socioeconomic impact	179:203	high socioeconomic impact	179:203	BACKGROUND Worldwide, diabetes mellitus and heart failure represent frequent comorbidities with high socioeconomic impact and steadily growing incidence, calling for a better understanding of how diabetic metabolism promotes cardiac dysfunction.
31195810	11	78	theme	cross	2290:2294	arg1	talk					2296:2299	a mutual posttranslational modification cross talk	2250:2299	a mutual posttranslational modification cross talk of (cardio-detrimental) phosphorylation at Ser-632 and (cardio-protective) O-GlcNAcylation at Ser-642	2250:2401	Preventing O-GlcNAcylation at Ser-642 not only entirely precluded production of the N-terminal fragment of HDAC4 but also promoted Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation at Ser-632, pointing to a mutual posttranslational modification cross talk of (cardio-detrimental) phosphorylation at Ser-632 and (cardio-protective) O-GlcNAcylation at Ser-642.
31195810	9	79	theme	fragment	1680:1687	arg1	Reexpression					1649:1660	Reexpression	1649:1660	Reexpression of the N-terminal fragment of HDAC4	1649:1696	Reexpression of the N-terminal fragment of HDAC4 prevents HDAC4-dependent diabetic cardiomyopathy.
31195810	11	80	theme	cardio-protective	2357:2373	arg1	O-GlcNAcylation					2376:2390	(cardio-protective) O-GlcNAcylation	2356:2390	(cardio-protective) O-GlcNAcylation	2356:2390	Preventing O-GlcNAcylation at Ser-642 not only entirely precluded production of the N-terminal fragment of HDAC4 but also promoted Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation at Ser-632, pointing to a mutual posttranslational modification cross talk of (cardio-detrimental) phosphorylation at Ser-632 and (cardio-protective) O-GlcNAcylation at Ser-642.
31195810	4	81	theme	HDAC4	678:682	arg1	allele					684:689	A conditional HDAC4 allele	664:689	A conditional HDAC4 allele	664:689	METHODS A conditional HDAC4 allele was used to delete HDAC4 specifically in cardiomyocytes (HDAC4-knockout).
31195810	11	82	theme	cardio-detrimental	2305:2322	arg1	phosphorylation					2325:2339	(cardio-detrimental) phosphorylation	2304:2339	(cardio-detrimental) phosphorylation at Ser-632 and (cardio-protective) O-GlcNAcylation at Ser-642	2304:2401	Preventing O-GlcNAcylation at Ser-642 not only entirely precluded production of the N-terminal fragment of HDAC4 but also promoted Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation at Ser-632, pointing to a mutual posttranslational modification cross talk of (cardio-detrimental) phosphorylation at Ser-632 and (cardio-protective) O-GlcNAcylation at Ser-642.
31195810	9	83	theme	HDAC4	1692:1696	arg1	fragment					1680:1687	the N-terminal fragment	1665:1687	the N-terminal fragment of HDAC4	1665:1696	Reexpression of the N-terminal fragment of HDAC4 prevents HDAC4-dependent diabetic cardiomyopathy.
31195810	11	84	from	Ser-632	2229:2235	arg1	phosphorylation					2210:2224	Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation	2157:2224	Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation at Ser-632	2157:2235	Preventing O-GlcNAcylation at Ser-642 not only entirely precluded production of the N-terminal fragment of HDAC4 but also promoted Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation at Ser-632, pointing to a mutual posttranslational modification cross talk of (cardio-detrimental) phosphorylation at Ser-632 and (cardio-protective) O-GlcNAcylation at Ser-642.
31195810	13	85	theme	molecular	2622:2630	arg1	model					2632:2636	a molecular model	2620:2636	a molecular model explaining how diabetic metabolism possesses important cardio-protective features besides its known detrimental effects	2620:2756	We introduce a molecular model explaining how diabetic metabolism possesses important cardio-protective features besides its known detrimental effects.
31195810	5	86	theme	mellitus	859:866	arg1	injections					831:840	streptozotocin injections	816:840	streptozotocin injections (type 1 diabetes mellitus model)	816:873	Mice were subjected to diabetes mellitus either by streptozotocin injections (type 1 diabetes mellitus model) or by crossing into mice carrying a leptin receptor mutation (db/db; type 2 diabetes mellitus model) and monitored for remodeling and cardiac function.
31195810	5	86	theme	mellitus	859:866	arg1	model					868:872	type 1 diabetes mellitus model	843:872	type 1 diabetes mellitus model	843:872	Mice were subjected to diabetes mellitus either by streptozotocin injections (type 1 diabetes mellitus model) or by crossing into mice carrying a leptin receptor mutation (db/db; type 2 diabetes mellitus model) and monitored for remodeling and cardiac function.
31195810	14	87	theme	talk	2841:2844	arg1	understanding					2768:2780	A deeper understanding	2759:2780	A deeper understanding of the here-described posttranslational modification cross talk	2759:2844	A deeper understanding of the here-described posttranslational modification cross talk may lay the groundwork for the development of specific therapeutic concepts to treat heart failure in the context of diabetes mellitus.
31195810	9	88	theme	HDAC4-dependent	1707:1721	arg1	cardiomyopathy					1732:1745	HDAC4-dependent diabetic cardiomyopathy	1707:1745	HDAC4-dependent diabetic cardiomyopathy	1707:1745	Reexpression of the N-terminal fragment of HDAC4 prevents HDAC4-dependent diabetic cardiomyopathy.
31195810	10	89	theme	II-mediated	1986:1996	arg1	phosphorylation					1998:2012	Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation	1945:2012	Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation at Ser-632	1945:2023	Mechanistically, the posttranslational modification of HDAC4 at serine (Ser)-642 by O-GlcNAcylation is an essential step for production of the N-terminal fragment of HDAC4, which was attenuated by Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation at Ser-632.
31195810	7	90	with	patients	1319:1326	arg1	mellitus					1342:1349	diabetes mellitus	1333:1349	diabetes mellitus	1333:1349	RESULTS We show that the cardio-protective N-terminal proteolytic fragment of HDAC4 is enhanced in vivo in patients with diabetes mellitus and mouse models, as well as in vitro under high-glucose and high-O-GlcNAc conditions.
31195810	7	90	with	patients	1319:1326	arg1	models					1361:1366	mouse models	1355:1366	mouse models	1355:1366	RESULTS We show that the cardio-protective N-terminal proteolytic fragment of HDAC4 is enhanced in vivo in patients with diabetes mellitus and mouse models, as well as in vitro under high-glucose and high-O-GlcNAc conditions.
31195810	3	91	theme	maladaptive	611:621	arg1	signaling					623:631	adaptive and maladaptive signaling	598:631	adaptive and maladaptive signaling	598:631	Here, we identified a histone deacetylase 4 (HDAC4) subdomain as a molecular checkpoint of adaptive and maladaptive signaling in the diabetic heart.
31195810	14	92	theme	modification	2822:2833	arg1	talk					2841:2844	the here-described posttranslational modification cross talk	2785:2844	the here-described posttranslational modification cross talk	2785:2844	A deeper understanding of the here-described posttranslational modification cross talk may lay the groundwork for the development of specific therapeutic concepts to treat heart failure in the context of diabetes mellitus.
31195810	11	93	theme	fragment	2121:2128	arg1	production					2092:2101	production	2092:2101	production of the N-terminal fragment of HDAC4	2092:2137	Preventing O-GlcNAcylation at Ser-642 not only entirely precluded production of the N-terminal fragment of HDAC4 but also promoted Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation at Ser-632, pointing to a mutual posttranslational modification cross talk of (cardio-detrimental) phosphorylation at Ser-632 and (cardio-protective) O-GlcNAcylation at Ser-642.
31195810	12	94	theme	pathological	2539:2550	arg1	kinase					2586:2591	pathological Ca2+/calmodulin-dependent protein kinase II	2539:2594	pathological Ca2+/calmodulin-dependent protein kinase II signaling	2539:2604	CONCLUSIONS In this study, we found that O-GlcNAcylation of HDAC4 at Ser-642 is cardio-protective in diabetes mellitus and counteracts pathological Ca2+/calmodulin-dependent protein kinase II signaling.
31195810	3	95	theme	adaptive	598:605	arg1	signaling					623:631	adaptive and maladaptive signaling	598:631	adaptive and maladaptive signaling	598:631	Here, we identified a histone deacetylase 4 (HDAC4) subdomain as a molecular checkpoint of adaptive and maladaptive signaling in the diabetic heart.
31195810	4	96	used	used	695:698	arg2	allele					684:689	A conditional HDAC4 allele	664:689	A conditional HDAC4 allele	664:689	METHODS A conditional HDAC4 allele was used to delete HDAC4 specifically in cardiomyocytes (HDAC4-knockout).
31195810	14	97	theme	here-described	2789:2802	arg1	modification					2822:2833	the here-described posttranslational modification	2785:2833	the here-described posttranslational modification cross talk	2785:2844	A deeper understanding of the here-described posttranslational modification cross talk may lay the groundwork for the development of specific therapeutic concepts to treat heart failure in the context of diabetes mellitus.
31195810	11	98	theme	Ca2+/calmodulin-dependent	2157:2181	arg1	kinase					2191:2196	Ca2+/calmodulin-dependent protein kinase	2157:2196	Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation at Ser-632	2157:2235	Preventing O-GlcNAcylation at Ser-642 not only entirely precluded production of the N-terminal fragment of HDAC4 but also promoted Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation at Ser-632, pointing to a mutual posttranslational modification cross talk of (cardio-detrimental) phosphorylation at Ser-632 and (cardio-protective) O-GlcNAcylation at Ser-642.
31195810	8	99	theme	type	1493:1496	arg1	models					1483:1488	models	1483:1488	models of type 1 and type 2 diabetes mellitus	1483:1527	HDAC4-knockout mice develop heart failure in models of type 1 and type 2 diabetes mellitus, whereas wild-type mice do not develop clear signs of heart failure, indicating that HDAC4 protects the diabetic heart.
31195810	3	100	theme	diabetic	640:647	arg1	heart					649:653	the diabetic heart	636:653	the diabetic heart	636:653	Here, we identified a histone deacetylase 4 (HDAC4) subdomain as a molecular checkpoint of adaptive and maladaptive signaling in the diabetic heart.
31195810	1	101	theme	heart	127:131	arg1	failure					133:139	heart failure	127:139	heart failure	127:139	BACKGROUND Worldwide, diabetes mellitus and heart failure represent frequent comorbidities with high socioeconomic impact and steadily growing incidence, calling for a better understanding of how diabetic metabolism promotes cardiac dysfunction.
31195810	14	102	theme	mellitus	2972:2979	arg1	context					2952:2958	the context	2948:2958	the context of diabetes mellitus	2948:2979	A deeper understanding of the here-described posttranslational modification cross talk may lay the groundwork for the development of specific therapeutic concepts to treat heart failure in the context of diabetes mellitus.
31195810	3	103	from	checkpoint	584:593	arg1	heart					649:653	the diabetic heart	636:653	the diabetic heart	636:653	Here, we identified a histone deacetylase 4 (HDAC4) subdomain as a molecular checkpoint of adaptive and maladaptive signaling in the diabetic heart.
31195810	11	104	from	O-GlcNAcylation	2376:2390	arg1	phosphorylation					2325:2339	(cardio-detrimental) phosphorylation	2304:2339	(cardio-detrimental) phosphorylation at Ser-632 and (cardio-protective) O-GlcNAcylation at Ser-642	2304:2401	Preventing O-GlcNAcylation at Ser-642 not only entirely precluded production of the N-terminal fragment of HDAC4 but also promoted Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation at Ser-632, pointing to a mutual posttranslational modification cross talk of (cardio-detrimental) phosphorylation at Ser-632 and (cardio-protective) O-GlcNAcylation at Ser-642.
31195810	11	104	from	O-GlcNAcylation	2376:2390	arg1	talk					2296:2299	a mutual posttranslational modification cross talk	2250:2299	a mutual posttranslational modification cross talk of (cardio-detrimental) phosphorylation at Ser-632 and (cardio-protective) O-GlcNAcylation at Ser-642	2250:2401	Preventing O-GlcNAcylation at Ser-642 not only entirely precluded production of the N-terminal fragment of HDAC4 but also promoted Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation at Ser-632, pointing to a mutual posttranslational modification cross talk of (cardio-detrimental) phosphorylation at Ser-632 and (cardio-protective) O-GlcNAcylation at Ser-642.
31195810	14	105	theme	deeper	2761:2766	arg1	understanding					2768:2780	A deeper understanding	2759:2780	A deeper understanding of the here-described posttranslational modification cross talk	2759:2844	A deeper understanding of the here-described posttranslational modification cross talk may lay the groundwork for the development of specific therapeutic concepts to treat heart failure in the context of diabetes mellitus.
31195810	11	106	theme	phosphorylation	2325:2339	arg1	talk					2296:2299	a mutual posttranslational modification cross talk	2250:2299	a mutual posttranslational modification cross talk of (cardio-detrimental) phosphorylation at Ser-632 and (cardio-protective) O-GlcNAcylation at Ser-642	2250:2401	Preventing O-GlcNAcylation at Ser-642 not only entirely precluded production of the N-terminal fragment of HDAC4 but also promoted Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation at Ser-632, pointing to a mutual posttranslational modification cross talk of (cardio-detrimental) phosphorylation at Ser-632 and (cardio-protective) O-GlcNAcylation at Ser-642.
31195810	5	107	theme	diabetes	788:795	arg1	mellitus					797:804	diabetes mellitus	788:804	diabetes mellitus	788:804	Mice were subjected to diabetes mellitus either by streptozotocin injections (type 1 diabetes mellitus model) or by crossing into mice carrying a leptin receptor mutation (db/db; type 2 diabetes mellitus model) and monitored for remodeling and cardiac function.
31195810	1	108	with	comorbidities	160:172	arg1	impact					198:203	high socioeconomic impact	179:203	high socioeconomic impact	179:203	BACKGROUND Worldwide, diabetes mellitus and heart failure represent frequent comorbidities with high socioeconomic impact and steadily growing incidence, calling for a better understanding of how diabetic metabolism promotes cardiac dysfunction.
31195810	1	108	with	comorbidities	160:172	arg1	incidence					226:234	steadily growing incidence	209:234	steadily growing incidence	209:234	BACKGROUND Worldwide, diabetes mellitus and heart failure represent frequent comorbidities with high socioeconomic impact and steadily growing incidence, calling for a better understanding of how diabetic metabolism promotes cardiac dysfunction.
31195810	5	109	theme	leptin	911:916	arg1	mutation					927:934	a leptin receptor mutation	909:934	a leptin receptor mutation (db/db; type 2 diabetes mellitus model)	909:974	Mice were subjected to diabetes mellitus either by streptozotocin injections (type 1 diabetes mellitus model) or by crossing into mice carrying a leptin receptor mutation (db/db; type 2 diabetes mellitus model) and monitored for remodeling and cardiac function.
31195810	14	110	theme	concepts	2913:2920	arg1	development					2877:2887	the development	2873:2887	the development of specific therapeutic concepts to treat heart failure in the context of diabetes mellitus	2873:2979	A deeper understanding of the here-described posttranslational modification cross talk may lay the groundwork for the development of specific therapeutic concepts to treat heart failure in the context of diabetes mellitus.
31195810	11	111	theme	HDAC4	2133:2137	arg1	fragment					2121:2128	the N-terminal fragment	2106:2128	the N-terminal fragment of HDAC4	2106:2137	Preventing O-GlcNAcylation at Ser-642 not only entirely precluded production of the N-terminal fragment of HDAC4 but also promoted Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation at Ser-632, pointing to a mutual posttranslational modification cross talk of (cardio-detrimental) phosphorylation at Ser-632 and (cardio-protective) O-GlcNAcylation at Ser-642.
31195810	8	112	theme	mellitus	1520:1527	arg1	models					1483:1488	models	1483:1488	models of type 1 and type 2 diabetes mellitus	1483:1527	HDAC4-knockout mice develop heart failure in models of type 1 and type 2 diabetes mellitus, whereas wild-type mice do not develop clear signs of heart failure, indicating that HDAC4 protects the diabetic heart.
31195810	10	113	from	Ser-632	2017:2023	arg1	phosphorylation					1998:2012	Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation	1945:2012	Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation at Ser-632	1945:2023	Mechanistically, the posttranslational modification of HDAC4 at serine (Ser)-642 by O-GlcNAcylation is an essential step for production of the N-terminal fragment of HDAC4, which was attenuated by Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation at Ser-632.
31195810	5	114	theme	type	944:947	arg1	mellitus					960:967	type 2 diabetes mellitus	944:967	db/db; type 2 diabetes mellitus model	937:973	Mice were subjected to diabetes mellitus either by streptozotocin injections (type 1 diabetes mellitus model) or by crossing into mice carrying a leptin receptor mutation (db/db; type 2 diabetes mellitus model) and monitored for remodeling and cardiac function.
31195810	7	115	theme	diabetes	1333:1340	arg1	mellitus					1342:1349	diabetes mellitus	1333:1349	diabetes mellitus	1333:1349	RESULTS We show that the cardio-protective N-terminal proteolytic fragment of HDAC4 is enhanced in vivo in patients with diabetes mellitus and mouse models, as well as in vitro under high-glucose and high-O-GlcNAc conditions.
31195810	11	116	theme	N-terminal	2110:2119	arg1	fragment					2121:2128	the N-terminal fragment	2106:2128	the N-terminal fragment of HDAC4	2106:2137	Preventing O-GlcNAcylation at Ser-642 not only entirely precluded production of the N-terminal fragment of HDAC4 but also promoted Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation at Ser-632, pointing to a mutual posttranslational modification cross talk of (cardio-detrimental) phosphorylation at Ser-632 and (cardio-protective) O-GlcNAcylation at Ser-642.
31195810	12	117	theme	kinase	2586:2591	arg1	signaling					2596:2604	pathological Ca2+/calmodulin-dependent protein kinase II signaling	2539:2604	pathological Ca2+/calmodulin-dependent protein kinase II signaling	2539:2604	CONCLUSIONS In this study, we found that O-GlcNAcylation of HDAC4 at Ser-642 is cardio-protective in diabetes mellitus and counteracts pathological Ca2+/calmodulin-dependent protein kinase II signaling.
31195810	0	118	theme	Deacetylase	27:37	arg1	O-GlcNAcylation					0:14	O-GlcNAcylation	0:14	O-GlcNAcylation of Histone Deacetylase 4	0:39	O-GlcNAcylation of Histone Deacetylase 4 Protects the Diabetic Heart From Failure.
31195810	5	119	theme	diabetes	951:958	arg1	mellitus					960:967	type 2 diabetes mellitus	944:967	db/db; type 2 diabetes mellitus model	937:973	Mice were subjected to diabetes mellitus either by streptozotocin injections (type 1 diabetes mellitus model) or by crossing into mice carrying a leptin receptor mutation (db/db; type 2 diabetes mellitus model) and monitored for remodeling and cardiac function.
31195810	11	120	from	Ser-642	2395:2401	arg1	phosphorylation					2325:2339	(cardio-detrimental) phosphorylation	2304:2339	(cardio-detrimental) phosphorylation at Ser-632 and (cardio-protective) O-GlcNAcylation at Ser-642	2304:2401	Preventing O-GlcNAcylation at Ser-642 not only entirely precluded production of the N-terminal fragment of HDAC4 but also promoted Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation at Ser-632, pointing to a mutual posttranslational modification cross talk of (cardio-detrimental) phosphorylation at Ser-632 and (cardio-protective) O-GlcNAcylation at Ser-642.
31195810	11	120	from	Ser-642	2395:2401	arg1	talk					2296:2299	a mutual posttranslational modification cross talk	2250:2299	a mutual posttranslational modification cross talk of (cardio-detrimental) phosphorylation at Ser-632 and (cardio-protective) O-GlcNAcylation at Ser-642	2250:2401	Preventing O-GlcNAcylation at Ser-642 not only entirely precluded production of the N-terminal fragment of HDAC4 but also promoted Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation at Ser-632, pointing to a mutual posttranslational modification cross talk of (cardio-detrimental) phosphorylation at Ser-632 and (cardio-protective) O-GlcNAcylation at Ser-642.
31195810	6	121	theme	posttranslational	1054:1070	arg1	modification					1072:1083	the posttranslational modification	1050:1083	the posttranslational modification by β-linked N-acetylglucosamine (O-GlcNAc) on HDAC4	1050:1135	Effects of glucose and the posttranslational modification by β-linked N-acetylglucosamine (O-GlcNAc) on HDAC4 were investigated in vivo and in vitro by biochemical and cellular assays.
31195810	8	122	theme	clear	1568:1572	arg1	signs					1574:1578	clear signs	1568:1578	clear signs of heart failure	1568:1595	HDAC4-knockout mice develop heart failure in models of type 1 and type 2 diabetes mellitus, whereas wild-type mice do not develop clear signs of heart failure, indicating that HDAC4 protects the diabetic heart.
31195810	13	123	theme	known	2732:2736	arg1	effects					2750:2756	its known detrimental effects	2728:2756	its known detrimental effects	2728:2756	We introduce a molecular model explaining how diabetic metabolism possesses important cardio-protective features besides its known detrimental effects.
31195810	0	124	theme	Diabetic	54:61	arg1	Heart					63:67	the Diabetic Heart	50:67	the Diabetic Heart	50:67	O-GlcNAcylation of Histone Deacetylase 4 Protects the Diabetic Heart From Failure.
31195810	12	125	dep	CONCLUSIONS	2404:2414	arg1	found					2434:2438	found	2434:2438	found that O-GlcNAcylation of HDAC4 at Ser-642 is cardio-protective in diabetes mellitus and counteracts pathological Ca2+/calmodulin-dependent protein kinase II signaling	2434:2604	CONCLUSIONS In this study, we found that O-GlcNAcylation of HDAC4 at Ser-642 is cardio-protective in diabetes mellitus and counteracts pathological Ca2+/calmodulin-dependent protein kinase II signaling.
31195810	4	126	dep	METHODS	656:662	arg1	used					695:698	used	695:698	was used to delete HDAC4 specifically in cardiomyocytes (HDAC4-knockout)	691:762	METHODS A conditional HDAC4 allele was used to delete HDAC4 specifically in cardiomyocytes (HDAC4-knockout).
31195810	14	127	theme	therapeutic	2901:2911	arg1	concepts					2913:2920	specific therapeutic concepts	2892:2920	specific therapeutic concepts	2892:2920	A deeper understanding of the here-described posttranslational modification cross talk may lay the groundwork for the development of specific therapeutic concepts to treat heart failure in the context of diabetes mellitus.
31195810	2	128	theme	cardiac	488:494	arg1	signaling					496:504	protective versus detrimental cardiac signaling	458:504	protective versus detrimental cardiac signaling	458:504	Paradoxically, some glucose-lowering drugs have been shown to worsen heart failure, raising the question of how glucose mediates protective versus detrimental cardiac signaling.
31195810	8	129	theme	failure	1589:1595	arg1	signs					1574:1578	clear signs	1568:1578	clear signs of heart failure	1568:1595	HDAC4-knockout mice develop heart failure in models of type 1 and type 2 diabetes mellitus, whereas wild-type mice do not develop clear signs of heart failure, indicating that HDAC4 protects the diabetic heart.
31195810	10	130	theme	HDAC4	1914:1918	arg1	fragment					1902:1909	the N-terminal fragment	1887:1909	the N-terminal fragment of HDAC4	1887:1918	Mechanistically, the posttranslational modification of HDAC4 at serine (Ser)-642 by O-GlcNAcylation is an essential step for production of the N-terminal fragment of HDAC4, which was attenuated by Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation at Ser-632.
31195810	7	131	theme	HDAC4	1290:1294	arg1	fragment					1278:1285	the cardio-protective N-terminal proteolytic fragment	1233:1285	the cardio-protective N-terminal proteolytic fragment of HDAC4	1233:1294	RESULTS We show that the cardio-protective N-terminal proteolytic fragment of HDAC4 is enhanced in vivo in patients with diabetes mellitus and mouse models, as well as in vitro under high-glucose and high-O-GlcNAc conditions.
31195810	10	132	theme	fragment	1902:1909	arg1	production					1873:1882	production	1873:1882	production	1873:1882	Mechanistically, the posttranslational modification of HDAC4 at serine (Ser)-642 by O-GlcNAcylation is an essential step for production of the N-terminal fragment of HDAC4, which was attenuated by Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation at Ser-632.
31195810	2	133	theme	glucose-lowering	349:364	arg1	drugs					366:370	some glucose-lowering drugs	344:370	some glucose-lowering drugs	344:370	Paradoxically, some glucose-lowering drugs have been shown to worsen heart failure, raising the question of how glucose mediates protective versus detrimental cardiac signaling.
31195810	7	134	theme	mouse	1355:1359	arg1	models					1361:1366	mouse models	1355:1366	mouse models	1355:1366	RESULTS We show that the cardio-protective N-terminal proteolytic fragment of HDAC4 is enhanced in vivo in patients with diabetes mellitus and mouse models, as well as in vitro under high-glucose and high-O-GlcNAc conditions.
31195810	11	135	theme	mutual	2252:2257	arg1	modification					2277:2288	a mutual posttranslational modification	2250:2288	a mutual posttranslational modification cross talk of (cardio-detrimental) phosphorylation at Ser-632 and (cardio-protective) O-GlcNAcylation at Ser-642	2250:2401	Preventing O-GlcNAcylation at Ser-642 not only entirely precluded production of the N-terminal fragment of HDAC4 but also promoted Ca2+/calmodulin-dependent protein kinase II-mediated phosphorylation at Ser-632, pointing to a mutual posttranslational modification cross talk of (cardio-detrimental) phosphorylation at Ser-632 and (cardio-protective) O-GlcNAcylation at Ser-642.
31195810	1	136	theme	better	251:256	arg1	understanding					258:270	a better understanding	249:270	a better understanding of how diabetic metabolism promotes cardiac dysfunction	249:326	BACKGROUND Worldwide, diabetes mellitus and heart failure represent frequent comorbidities with high socioeconomic impact and steadily growing incidence, calling for a better understanding of how diabetic metabolism promotes cardiac dysfunction.
22121020	8	0	theme	ubiquitin	993:1001	arg1	ligase					1003:1008	a histone H2B ubiquitin ligase	979:1008	a histone H2B ubiquitin ligase	979:1008	H2B S112 GlcNAcylation promotes K120 monoubiquitination, in which the GlcNAc moiety can serve as an anchor for a histone H2B ubiquitin ligase.
22121020	4	1	link	O-linked	441:448	arg1	GlcNAc					471:476	GlcNAc	471:476	GlcNAc	471:476	In metazoans, reversible protein modification by O-linked N-acetylglucosamine (GlcNAc) is catalysed by two enzymes, O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA).
22121020	4	1	link	O-linked	441:448	arg1	N-acetylglucosamine					450:468	O-linked N-acetylglucosamine	441:468	O-linked N-acetylglucosamine (GlcNAc)	441:477	In metazoans, reversible protein modification by O-linked N-acetylglucosamine (GlcNAc) is catalysed by two enzymes, O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA).
22121020	10	2	theme	H2B	1265:1267	arg1	monoubiquitination					1274:1291	H2B K120 monoubiquitination	1265:1291	H2B K120 monoubiquitination	1265:1291	In a genome-wide analysis, H2B S112 GlcNAcylation sites were observed widely distributed over chromosomes including transcribed gene loci, with some sites co-localizing with H2B K120 monoubiquitination.
22121020	9	3	theme	S112	1015:1018	arg1	GlcNAc					1020:1025	H2B S112 GlcNAc	1011:1025	H2B S112 GlcNAc	1011:1025	H2B S112 GlcNAc was localized to euchromatic areas on fly polytene chromosomes.
22121020	11	4	theme	S112	1326:1329	arg1	modification					1358:1369	a histone modification	1348:1369	a histone modification that facilitates H2BK120 monoubiquitination, presumably for transcriptional activation	1348:1456	These findings suggest that H2B S112 GlcNAcylation is a histone modification that facilitates H2BK120 monoubiquitination, presumably for transcriptional activation.
22121020	11	4	theme	S112	1326:1329	arg1	GlcNAcylation					1331:1343	H2B S112 GlcNAcylation	1322:1343	H2B S112 GlcNAcylation	1322:1343	These findings suggest that H2B S112 GlcNAcylation is a histone modification that facilitates H2BK120 monoubiquitination, presumably for transcriptional activation.
22121020	1	5	theme	Chromatin	65:73	arg1	reorganization					75:88	Chromatin reorganization	65:88	Chromatin reorganization	65:88	Chromatin reorganization is governed by multiple post-translational modifications of chromosomal proteins and DNA.
22121020	6	6	theme	histone	666:672	arg1	H2B					674:676	histone H2B	666:676	histone H2B	666:676	Here we report that histone H2B is GlcNAcylated at residue S112 by OGT in vitro and in living cells.
22121020	7	7	theme	Histone	747:753	arg1	GlcNAcylation					755:767	Histone GlcNAcylation	747:767	Histone GlcNAcylation	747:767	Histone GlcNAcylation fluctuated in response to extracellular glucose through the hexosamine biosynthesis pathway (HBP).
22121020	2	8	theme	histone	186:192	arg1	events					232:237	reversible, dynamic events	212:237	reversible, dynamic events that can regulate DNA-driven cellular processes	212:285	These histone modifications are reversible, dynamic events that can regulate DNA-driven cellular processes.
22121020	2	8	theme	histone	186:192	arg1	modifications					194:206	These histone modifications	180:206	These histone modifications	180:206	These histone modifications are reversible, dynamic events that can regulate DNA-driven cellular processes.
22121020	2	9	dep	reversible	212:221	arg1	dynamic					224:230	dynamic	224:230	dynamic	224:230	These histone modifications are reversible, dynamic events that can regulate DNA-driven cellular processes.
22121020	10	10	theme	K120	1269:1272	arg1	monoubiquitination					1274:1291	H2B K120 monoubiquitination	1265:1291	H2B K120 monoubiquitination	1265:1291	In a genome-wide analysis, H2B S112 GlcNAcylation sites were observed widely distributed over chromosomes including transcribed gene loci, with some sites co-localizing with H2B K120 monoubiquitination.
22121020	11	11	theme	H2BK120	1388:1394	arg1	monoubiquitination					1396:1413	H2BK120 monoubiquitination	1388:1413	H2BK120 monoubiquitination	1388:1413	These findings suggest that H2B S112 GlcNAcylation is a histone modification that facilitates H2BK120 monoubiquitination, presumably for transcriptional activation.
22121020	10	12	theme	gene	1219:1222	arg1	loci					1224:1227	transcribed gene loci	1207:1227	transcribed gene loci	1207:1227	In a genome-wide analysis, H2B S112 GlcNAcylation sites were observed widely distributed over chromosomes including transcribed gene loci, with some sites co-localizing with H2B K120 monoubiquitination.
22121020	11	13	theme	transcriptional	1431:1445	arg1	activation					1447:1456	transcriptional activation	1431:1456	transcriptional activation	1431:1456	These findings suggest that H2B S112 GlcNAcylation is a histone modification that facilitates H2BK120 monoubiquitination, presumably for transcriptional activation.
22121020	10	14	theme	GlcNAcylation	1127:1139	arg1	sites					1141:1145	H2B S112 GlcNAcylation sites	1118:1145	H2B S112 GlcNAcylation sites	1118:1145	In a genome-wide analysis, H2B S112 GlcNAcylation sites were observed widely distributed over chromosomes including transcribed gene loci, with some sites co-localizing with H2B K120 monoubiquitination.
22121020	6	15	theme	living	733:738	arg1	cells					740:744	living cells	733:744	living cells	733:744	Here we report that histone H2B is GlcNAcylated at residue S112 by OGT in vitro and in living cells.
22121020	5	16	from	significance	571:582	arg1	reorganization					614:627	chromatin reorganization	604:627	chromatin reorganization	604:627	However, the significance of GlcNAcylation in chromatin reorganization remains elusive.
22121020	10	17	theme	S112	1122:1125	arg1	sites					1141:1145	H2B S112 GlcNAcylation sites	1118:1145	H2B S112 GlcNAcylation sites	1118:1145	In a genome-wide analysis, H2B S112 GlcNAcylation sites were observed widely distributed over chromosomes including transcribed gene loci, with some sites co-localizing with H2B K120 monoubiquitination.
22121020	11	18	theme	histone	1350:1356	arg1	modification					1358:1369	a histone modification	1348:1369	a histone modification that facilitates H2BK120 monoubiquitination, presumably for transcriptional activation	1348:1456	These findings suggest that H2B S112 GlcNAcylation is a histone modification that facilitates H2BK120 monoubiquitination, presumably for transcriptional activation.
22121020	11	18	theme	histone	1350:1356	arg1	GlcNAcylation					1331:1343	H2B S112 GlcNAcylation	1322:1343	H2B S112 GlcNAcylation	1322:1343	These findings suggest that H2B S112 GlcNAcylation is a histone modification that facilitates H2BK120 monoubiquitination, presumably for transcriptional activation.
22121020	10	19	with	co-localizing	1246:1258	arg1	monoubiquitination					1274:1291	H2B K120 monoubiquitination	1265:1291	H2B K120 monoubiquitination	1265:1291	In a genome-wide analysis, H2B S112 GlcNAcylation sites were observed widely distributed over chromosomes including transcribed gene loci, with some sites co-localizing with H2B K120 monoubiquitination.
22121020	9	20	theme	H2B	1011:1013	arg1	GlcNAc					1020:1025	H2B S112 GlcNAc	1011:1025	H2B S112 GlcNAc	1011:1025	H2B S112 GlcNAc was localized to euchromatic areas on fly polytene chromosomes.
22121020	10	21	theme	genome-wide	1096:1106	arg1	analysis					1108:1115	a genome-wide analysis	1094:1115	a genome-wide analysis	1094:1115	In a genome-wide analysis, H2B S112 GlcNAcylation sites were observed widely distributed over chromosomes including transcribed gene loci, with some sites co-localizing with H2B K120 monoubiquitination.
22121020	1	22	theme	multiple	105:112	arg1	modifications					133:145	multiple post-translational modifications	105:145	multiple post-translational modifications of chromosomal proteins and DNA	105:177	Chromatin reorganization is governed by multiple post-translational modifications of chromosomal proteins and DNA.
22121020	0	23	theme	H2B	25:27	arg1	GlcNAcylation					0:12	GlcNAcylation	0:12	GlcNAcylation of histone H2B	0:27	GlcNAcylation of histone H2B facilitates its monoubiquitination.
22121020	4	24	theme	O-linked	441:448	arg1	GlcNAc					471:476	GlcNAc	471:476	GlcNAc	471:476	In metazoans, reversible protein modification by O-linked N-acetylglucosamine (GlcNAc) is catalysed by two enzymes, O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA).
22121020	4	24	theme	O-linked	441:448	arg1	N-acetylglucosamine					450:468	O-linked N-acetylglucosamine	441:468	O-linked N-acetylglucosamine (GlcNAc)	441:477	In metazoans, reversible protein modification by O-linked N-acetylglucosamine (GlcNAc) is catalysed by two enzymes, O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA).
22121020	1	25	theme	post-translational	114:131	arg1	modifications					133:145	multiple post-translational modifications	105:145	multiple post-translational modifications of chromosomal proteins and DNA	105:177	Chromatin reorganization is governed by multiple post-translational modifications of chromosomal proteins and DNA.
22121020	0	26	theme	histone	17:23	arg1	H2B					25:27	histone H2B	17:27	histone H2B	17:27	GlcNAcylation of histone H2B facilitates its monoubiquitination.
22121020	4	27	theme	O-GlcNAc	508:515	arg1	OGT					530:532	OGT	530:532	OGT	530:532	In metazoans, reversible protein modification by O-linked N-acetylglucosamine (GlcNAc) is catalysed by two enzymes, O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA).
22121020	4	27	theme	O-GlcNAc	508:515	arg1	enzymes					499:505	two enzymes	495:505	two enzymes	495:505	In metazoans, reversible protein modification by O-linked N-acetylglucosamine (GlcNAc) is catalysed by two enzymes, O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA).
22121020	4	27	theme	O-GlcNAc	508:515	arg1	transferase					517:527	O-GlcNAc transferase	508:527	O-GlcNAc transferase (OGT)	508:533	In metazoans, reversible protein modification by O-linked N-acetylglucosamine (GlcNAc) is catalysed by two enzymes, O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA).
22121020	3	28	theme	molecular	301:309	arg1	mechanisms					311:320	the molecular mechanisms	297:320	the molecular mechanisms that coordinate histone modification patterns	297:366	However, the molecular mechanisms that coordinate histone modification patterns remain largely unknown.
22121020	2	29	theme	reversible	212:221	arg1	events					232:237	reversible, dynamic events	212:237	reversible, dynamic events that can regulate DNA-driven cellular processes	212:285	These histone modifications are reversible, dynamic events that can regulate DNA-driven cellular processes.
22121020	2	29	theme	reversible	212:221	arg1	modifications					194:206	These histone modifications	180:206	These histone modifications	180:206	These histone modifications are reversible, dynamic events that can regulate DNA-driven cellular processes.
22121020	9	30	theme	polytene	1069:1076	arg1	chromosomes					1078:1088	fly polytene chromosomes	1065:1088	fly polytene chromosomes	1065:1088	H2B S112 GlcNAc was localized to euchromatic areas on fly polytene chromosomes.
22121020	7	31	theme	hexosamine	829:838	arg1	HBP					862:864	HBP	862:864	HBP	862:864	Histone GlcNAcylation fluctuated in response to extracellular glucose through the hexosamine biosynthesis pathway (HBP).
22121020	7	31	theme	hexosamine	829:838	arg1	pathway					853:859	the hexosamine biosynthesis pathway	825:859	the hexosamine biosynthesis pathway (HBP)	825:865	Histone GlcNAcylation fluctuated in response to extracellular glucose through the hexosamine biosynthesis pathway (HBP).
22121020	2	32	theme	cellular	268:275	arg1	processes					277:285	DNA-driven cellular processes	257:285	DNA-driven cellular processes	257:285	These histone modifications are reversible, dynamic events that can regulate DNA-driven cellular processes.
22121020	7	33	theme	biosynthesis	840:851	arg1	HBP					862:864	HBP	862:864	HBP	862:864	Histone GlcNAcylation fluctuated in response to extracellular glucose through the hexosamine biosynthesis pathway (HBP).
22121020	7	33	theme	biosynthesis	840:851	arg1	pathway					853:859	the hexosamine biosynthesis pathway	825:859	the hexosamine biosynthesis pathway (HBP)	825:865	Histone GlcNAcylation fluctuated in response to extracellular glucose through the hexosamine biosynthesis pathway (HBP).
22121020	7	34	dep	glucose	809:815	arg1	response					783:790	response	783:790	response	783:790	Histone GlcNAcylation fluctuated in response to extracellular glucose through the hexosamine biosynthesis pathway (HBP).
22121020	2	35	theme	DNA-driven	257:266	arg1	processes					277:285	DNA-driven cellular processes	257:285	DNA-driven cellular processes	257:285	These histone modifications are reversible, dynamic events that can regulate DNA-driven cellular processes.
22121020	5	36	theme	GlcNAcylation	587:599	arg1	significance					571:582	the significance	567:582	the significance of GlcNAcylation in chromatin reorganization	567:627	However, the significance of GlcNAcylation in chromatin reorganization remains elusive.
22121020	9	37	theme	euchromatic	1044:1054	arg1	areas					1056:1060	euchromatic areas	1044:1060	euchromatic areas	1044:1060	H2B S112 GlcNAc was localized to euchromatic areas on fly polytene chromosomes.
22121020	11	38	theme	H2B	1322:1324	arg1	modification					1358:1369	a histone modification	1348:1369	a histone modification that facilitates H2BK120 monoubiquitination, presumably for transcriptional activation	1348:1456	These findings suggest that H2B S112 GlcNAcylation is a histone modification that facilitates H2BK120 monoubiquitination, presumably for transcriptional activation.
22121020	11	38	theme	H2B	1322:1324	arg1	GlcNAcylation					1331:1343	H2B S112 GlcNAcylation	1322:1343	H2B S112 GlcNAcylation	1322:1343	These findings suggest that H2B S112 GlcNAcylation is a histone modification that facilitates H2BK120 monoubiquitination, presumably for transcriptional activation.
22121020	4	39	theme	protein	417:423	arg1	modification					425:436	reversible protein modification	406:436	reversible protein modification by O-linked N-acetylglucosamine (GlcNAc)	406:477	In metazoans, reversible protein modification by O-linked N-acetylglucosamine (GlcNAc) is catalysed by two enzymes, O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA).
22121020	1	40	theme	chromosomal	150:160	arg1	proteins					162:169	chromosomal proteins	150:169	chromosomal proteins	150:169	Chromatin reorganization is governed by multiple post-translational modifications of chromosomal proteins and DNA.
22121020	8	41	theme	H2B	868:870	arg1	GlcNAcylation					877:889	H2B S112 GlcNAcylation	868:889	H2B S112 GlcNAcylation	868:889	H2B S112 GlcNAcylation promotes K120 monoubiquitination, in which the GlcNAc moiety can serve as an anchor for a histone H2B ubiquitin ligase.
22121020	5	42	theme	chromatin	604:612	arg1	reorganization					614:627	chromatin reorganization	604:627	chromatin reorganization	604:627	However, the significance of GlcNAcylation in chromatin reorganization remains elusive.
22121020	3	43	theme	histone	338:344	arg1	patterns					359:366	histone modification patterns	338:366	histone modification patterns	338:366	However, the molecular mechanisms that coordinate histone modification patterns remain largely unknown.
22121020	9	44	located	localized	1031:1039	arg2	GlcNAc					1020:1025	H2B S112 GlcNAc	1011:1025	H2B S112 GlcNAc	1011:1025	H2B S112 GlcNAc was localized to euchromatic areas on fly polytene chromosomes.
22121020	9	44	located	localized	1031:1039	arg1	chromosomes					1078:1088	fly polytene chromosomes	1065:1088	fly polytene chromosomes	1065:1088	H2B S112 GlcNAc was localized to euchromatic areas on fly polytene chromosomes.
22121020	4	45	theme	reversible	406:415	arg1	modification					425:436	reversible protein modification	406:436	reversible protein modification by O-linked N-acetylglucosamine (GlcNAc)	406:477	In metazoans, reversible protein modification by O-linked N-acetylglucosamine (GlcNAc) is catalysed by two enzymes, O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA).
22121020	1	46	theme	proteins	162:169	arg1	modifications					133:145	multiple post-translational modifications	105:145	multiple post-translational modifications of chromosomal proteins and DNA	105:177	Chromatin reorganization is governed by multiple post-translational modifications of chromosomal proteins and DNA.
22121020	7	47	theme	extracellular	795:807	arg1	glucose					809:815	extracellular glucose	795:815	extracellular glucose	795:815	Histone GlcNAcylation fluctuated in response to extracellular glucose through the hexosamine biosynthesis pathway (HBP).
22121020	3	48	theme	modification	346:357	arg1	patterns					359:366	histone modification patterns	338:366	histone modification patterns	338:366	However, the molecular mechanisms that coordinate histone modification patterns remain largely unknown.
22121020	8	49	theme	H2B	989:991	arg1	ligase					1003:1008	a histone H2B ubiquitin ligase	979:1008	a histone H2B ubiquitin ligase	979:1008	H2B S112 GlcNAcylation promotes K120 monoubiquitination, in which the GlcNAc moiety can serve as an anchor for a histone H2B ubiquitin ligase.
22121020	9	50	theme	fly	1065:1067	arg1	chromosomes					1078:1088	fly polytene chromosomes	1065:1088	fly polytene chromosomes	1065:1088	H2B S112 GlcNAc was localized to euchromatic areas on fly polytene chromosomes.
22121020	8	51	theme	GlcNAc	938:943	arg1	anchor					968:973	an anchor	965:973	an anchor for a histone H2B ubiquitin ligase	965:1008	H2B S112 GlcNAcylation promotes K120 monoubiquitination, in which the GlcNAc moiety can serve as an anchor for a histone H2B ubiquitin ligase.
22121020	8	51	theme	GlcNAc	938:943	arg1	moiety					945:950	the GlcNAc moiety	934:950	the GlcNAc moiety	934:950	H2B S112 GlcNAcylation promotes K120 monoubiquitination, in which the GlcNAc moiety can serve as an anchor for a histone H2B ubiquitin ligase.
22121020	8	52	theme	histone	981:987	arg1	ligase					1003:1008	a histone H2B ubiquitin ligase	979:1008	a histone H2B ubiquitin ligase	979:1008	H2B S112 GlcNAcylation promotes K120 monoubiquitination, in which the GlcNAc moiety can serve as an anchor for a histone H2B ubiquitin ligase.
22121020	1	53	theme	DNA	175:177	arg1	modifications					133:145	multiple post-translational modifications	105:145	multiple post-translational modifications of chromosomal proteins and DNA	105:177	Chromatin reorganization is governed by multiple post-translational modifications of chromosomal proteins and DNA.
22121020	8	54	theme	S112	872:875	arg1	GlcNAcylation					877:889	H2B S112 GlcNAcylation	868:889	H2B S112 GlcNAcylation	868:889	H2B S112 GlcNAcylation promotes K120 monoubiquitination, in which the GlcNAc moiety can serve as an anchor for a histone H2B ubiquitin ligase.
22121020	10	55	theme	co-localizing	1246:1258	arg1	sites					1240:1244	some sites	1235:1244	some sites co-localizing with H2B K120 monoubiquitination	1235:1291	In a genome-wide analysis, H2B S112 GlcNAcylation sites were observed widely distributed over chromosomes including transcribed gene loci, with some sites co-localizing with H2B K120 monoubiquitination.
22121020	10	56	theme	H2B	1118:1120	arg1	sites					1141:1145	H2B S112 GlcNAcylation sites	1118:1145	H2B S112 GlcNAcylation sites	1118:1145	In a genome-wide analysis, H2B S112 GlcNAcylation sites were observed widely distributed over chromosomes including transcribed gene loci, with some sites co-localizing with H2B K120 monoubiquitination.
22121020	10	57	located	observed	1152:1159	arg2	sites					1141:1145	H2B S112 GlcNAcylation sites	1118:1145	H2B S112 GlcNAcylation sites	1118:1145	In a genome-wide analysis, H2B S112 GlcNAcylation sites were observed widely distributed over chromosomes including transcribed gene loci, with some sites co-localizing with H2B K120 monoubiquitination.
22121020	10	57	located	observed	1152:1159	arg1	analysis					1108:1115	a genome-wide analysis	1094:1115	a genome-wide analysis	1094:1115	In a genome-wide analysis, H2B S112 GlcNAcylation sites were observed widely distributed over chromosomes including transcribed gene loci, with some sites co-localizing with H2B K120 monoubiquitination.
22121020	8	58	theme	K120	900:903	arg1	monoubiquitination					905:922	K120 monoubiquitination	900:922	K120 monoubiquitination	900:922	H2B S112 GlcNAcylation promotes K120 monoubiquitination, in which the GlcNAc moiety can serve as an anchor for a histone H2B ubiquitin ligase.
22121020	10	59	theme	transcribed	1207:1217	arg1	loci					1224:1227	transcribed gene loci	1207:1227	transcribed gene loci	1207:1227	In a genome-wide analysis, H2B S112 GlcNAcylation sites were observed widely distributed over chromosomes including transcribed gene loci, with some sites co-localizing with H2B K120 monoubiquitination.
31932432	9	0	theme	protein	1156:1162	arg1	stability					1164:1172	the protein stability	1152:1172	the protein stability	1152:1172	Together, our data demonstrate a conserved role of OGT in positively regulating the protein stability of HIPKs (fly Hipk and human HIPK2), which likely permits the nutritional responsiveness of HIPKs.
31932432	3	1	theme	-induced	487:494	arg1	abnormalities					503:515	Drosophila homeodomain-interacting protein kinase (Hipk)-induced growth abnormalities	431:515	Drosophila homeodomain-interacting protein kinase (Hipk)-induced growth abnormalities in response to a high sugar diet	431:548	Here, we identify the requirements of hexosamine biosynthetic pathway (HBP) and O-GlcNAc transferase (OGT) for Drosophila homeodomain-interacting protein kinase (Hipk)-induced growth abnormalities in response to a high sugar diet.
31932432	7	2	theme	Mass	889:892	arg1	analyses					907:914	Mass spectrometry analyses	889:914	Mass spectrometry analyses	889:914	Mass spectrometry analyses reveal that HIPK2 is at least O-GlcNAc modified at S852, T1009, and S1147 residues.
31932432	4	3	theme	normal	556:561	arg1	diet					563:566	a normal diet	554:566	a normal diet	554:566	On a normal diet, OGT is both necessary and sufficient for inducing Hipk-mediated tumor-like growth.
31932432	8	4	dep	HIPK2	1035:1039	arg1	O-GlcNAcylation					1041:1055	O-GlcNAcylation	1041:1055	O-GlcNAcylation	1041:1055	Mutations of these residues reduce HIPK2 O-GlcNAcylation and stability.
31932432	9	5	theme	HIPKs	1266:1270	arg1	responsiveness					1248:1261	the nutritional responsiveness	1232:1261	the nutritional responsiveness of HIPKs	1232:1270	Together, our data demonstrate a conserved role of OGT in positively regulating the protein stability of HIPKs (fly Hipk and human HIPK2), which likely permits the nutritional responsiveness of HIPKs.
31932432	6	6	theme	mammalian	793:801	arg1	cells					803:807	mammalian cells	793:807	mammalian cells	793:807	In mammalian cells, human HIPK2 proteins accumulate posttranscriptionally upon OGT overexpression.
31932432	3	7	theme	growth	496:501	arg1	abnormalities					503:515	Drosophila homeodomain-interacting protein kinase (Hipk)-induced growth abnormalities	431:515	Drosophila homeodomain-interacting protein kinase (Hipk)-induced growth abnormalities in response to a high sugar diet	431:548	Here, we identify the requirements of hexosamine biosynthetic pathway (HBP) and O-GlcNAc transferase (OGT) for Drosophila homeodomain-interacting protein kinase (Hipk)-induced growth abnormalities in response to a high sugar diet.
31932432	3	8	theme	biosynthetic	369:380	arg1	pathway					382:388	hexosamine biosynthetic pathway	358:388	hexosamine biosynthetic pathway (HBP)	358:394	Here, we identify the requirements of hexosamine biosynthetic pathway (HBP) and O-GlcNAc transferase (OGT) for Drosophila homeodomain-interacting protein kinase (Hipk)-induced growth abnormalities in response to a high sugar diet.
31932432	3	8	theme	biosynthetic	369:380	arg1	HBP					391:393	HBP	391:393	HBP	391:393	Here, we identify the requirements of hexosamine biosynthetic pathway (HBP) and O-GlcNAc transferase (OGT) for Drosophila homeodomain-interacting protein kinase (Hipk)-induced growth abnormalities in response to a high sugar diet.
31932432	9	9	theme	HIPKs	1177:1181	arg1	stability					1164:1172	the protein stability	1152:1172	the protein stability	1152:1172	Together, our data demonstrate a conserved role of OGT in positively regulating the protein stability of HIPKs (fly Hipk and human HIPK2), which likely permits the nutritional responsiveness of HIPKs.
31932432	2	10	theme	dietary	280:286	arg1	sugars					288:293	dietary sugars	280:293	dietary sugars	280:293	Of emerging interest is the link observed between effects of dietary sugars on cancer proliferation.
31932432	9	11	dep	HIPKs	1177:1181	arg1	HIPKs					1177:1181	HIPKs	1177:1181	HIPKs (fly Hipk and human HIPK2)	1177:1208	Together, our data demonstrate a conserved role of OGT in positively regulating the protein stability of HIPKs (fly Hipk and human HIPK2), which likely permits the nutritional responsiveness of HIPKs.
31932432	9	11	dep	HIPKs	1177:1181	arg1	Hipk					1188:1191	fly Hipk	1184:1191	fly Hipk	1184:1191	Together, our data demonstrate a conserved role of OGT in positively regulating the protein stability of HIPKs (fly Hipk and human HIPK2), which likely permits the nutritional responsiveness of HIPKs.
31932432	9	11	dep	HIPKs	1177:1181	arg1	HIPK2					1203:1207	human HIPK2	1197:1207	human HIPK2	1197:1207	Together, our data demonstrate a conserved role of OGT in positively regulating the protein stability of HIPKs (fly Hipk and human HIPK2), which likely permits the nutritional responsiveness of HIPKs.
31932432	8	12	theme	residues	1019:1026	arg1	Mutations					1000:1008	Mutations	1000:1008	Mutations of these residues	1000:1026	Mutations of these residues reduce HIPK2 O-GlcNAcylation and stability.
31932432	3	13	from	abnormalities	503:515	arg1	response					520:527	response	520:527	response to a high sugar diet	520:548	Here, we identify the requirements of hexosamine biosynthetic pathway (HBP) and O-GlcNAc transferase (OGT) for Drosophila homeodomain-interacting protein kinase (Hipk)-induced growth abnormalities in response to a high sugar diet.
31932432	3	14	theme	high	534:537	arg1	diet					545:548	a high sugar diet	532:548	a high sugar diet	532:548	Here, we identify the requirements of hexosamine biosynthetic pathway (HBP) and O-GlcNAc transferase (OGT) for Drosophila homeodomain-interacting protein kinase (Hipk)-induced growth abnormalities in response to a high sugar diet.
31932432	3	15	theme	protein	466:472	arg1	kinase					474:479	Drosophila homeodomain-interacting protein kinase	431:479	Drosophila homeodomain-interacting protein kinase	431:479	Here, we identify the requirements of hexosamine biosynthetic pathway (HBP) and O-GlcNAc transferase (OGT) for Drosophila homeodomain-interacting protein kinase (Hipk)-induced growth abnormalities in response to a high sugar diet.
31932432	4	16	theme	tumor-like	633:642	arg1	growth					644:649	Hipk-mediated tumor-like growth	619:649	Hipk-mediated tumor-like growth	619:649	On a normal diet, OGT is both necessary and sufficient for inducing Hipk-mediated tumor-like growth.
31932432	9	17	theme	fly	1184:1186	arg1	HIPKs					1177:1181	HIPKs	1177:1181	HIPKs (fly Hipk and human HIPK2)	1177:1208	Together, our data demonstrate a conserved role of OGT in positively regulating the protein stability of HIPKs (fly Hipk and human HIPK2), which likely permits the nutritional responsiveness of HIPKs.
31932432	9	17	theme	fly	1184:1186	arg1	Hipk					1188:1191	fly Hipk	1184:1191	fly Hipk	1184:1191	Together, our data demonstrate a conserved role of OGT in positively regulating the protein stability of HIPKs (fly Hipk and human HIPK2), which likely permits the nutritional responsiveness of HIPKs.
31932432	1	18	theme	wide	173:176	arg1	array					178:182	a wide array	171:182	a wide array of molecular sensors inside cells	171:216	Environmental cues such as nutrients alter cellular behaviors by acting on a wide array of molecular sensors inside cells.
31932432	0	19	theme	nutrient	4:11	arg1	OGT					20:22	The nutrient sensor OGT	0:22	The nutrient sensor OGT	0:22	The nutrient sensor OGT regulates Hipk stability and tumorigenic-like activities in Drosophila.
31932432	6	20	theme	OGT	869:871	arg1	overexpression					873:886	OGT overexpression	869:886	OGT overexpression	869:886	In mammalian cells, human HIPK2 proteins accumulate posttranscriptionally upon OGT overexpression.
31932432	3	21	dep	-induced	487:494	arg1	kinase					474:479	Drosophila homeodomain-interacting protein kinase	431:479	Drosophila homeodomain-interacting protein kinase	431:479	Here, we identify the requirements of hexosamine biosynthetic pathway (HBP) and O-GlcNAc transferase (OGT) for Drosophila homeodomain-interacting protein kinase (Hipk)-induced growth abnormalities in response to a high sugar diet.
31932432	3	22	theme	transferase	409:419	arg1	requirements					342:353	the requirements	338:353	the requirements of hexosamine biosynthetic pathway (HBP) and O-GlcNAc transferase (OGT) for Drosophila homeodomain-interacting protein kinase (Hipk)-induced growth abnormalities in response to a high sugar diet	338:548	Here, we identify the requirements of hexosamine biosynthetic pathway (HBP) and O-GlcNAc transferase (OGT) for Drosophila homeodomain-interacting protein kinase (Hipk)-induced growth abnormalities in response to a high sugar diet.
31932432	2	23	theme	cancer	298:303	arg1	proliferation					305:317	cancer proliferation	298:317	cancer proliferation	298:317	Of emerging interest is the link observed between effects of dietary sugars on cancer proliferation.
31932432	3	24	theme	hexosamine	358:367	arg1	pathway					382:388	hexosamine biosynthetic pathway	358:388	hexosamine biosynthetic pathway (HBP)	358:394	Here, we identify the requirements of hexosamine biosynthetic pathway (HBP) and O-GlcNAc transferase (OGT) for Drosophila homeodomain-interacting protein kinase (Hipk)-induced growth abnormalities in response to a high sugar diet.
31932432	3	24	theme	hexosamine	358:367	arg1	HBP					391:393	HBP	391:393	HBP	391:393	Here, we identify the requirements of hexosamine biosynthetic pathway (HBP) and O-GlcNAc transferase (OGT) for Drosophila homeodomain-interacting protein kinase (Hipk)-induced growth abnormalities in response to a high sugar diet.
31932432	9	25	theme	human	1197:1201	arg1	HIPKs					1177:1181	HIPKs	1177:1181	HIPKs (fly Hipk and human HIPK2)	1177:1208	Together, our data demonstrate a conserved role of OGT in positively regulating the protein stability of HIPKs (fly Hipk and human HIPK2), which likely permits the nutritional responsiveness of HIPKs.
31932432	9	25	theme	human	1197:1201	arg1	HIPK2					1203:1207	human HIPK2	1197:1207	human HIPK2	1197:1207	Together, our data demonstrate a conserved role of OGT in positively regulating the protein stability of HIPKs (fly Hipk and human HIPK2), which likely permits the nutritional responsiveness of HIPKs.
31932432	3	26	theme	sugar	539:543	arg1	diet					545:548	a high sugar diet	532:548	a high sugar diet	532:548	Here, we identify the requirements of hexosamine biosynthetic pathway (HBP) and O-GlcNAc transferase (OGT) for Drosophila homeodomain-interacting protein kinase (Hipk)-induced growth abnormalities in response to a high sugar diet.
31932432	1	27	theme	molecular	187:195	arg1	sensors					197:203	molecular sensors	187:203	molecular sensors inside cells	187:216	Environmental cues such as nutrients alter cellular behaviors by acting on a wide array of molecular sensors inside cells.
31932432	1	28	theme	Environmental	96:108	arg1	cues					110:113	Environmental cues	96:113	Environmental cues such as nutrients	96:131	Environmental cues such as nutrients alter cellular behaviors by acting on a wide array of molecular sensors inside cells.
31932432	1	28	theme	Environmental	96:108	arg1	nutrients					123:131	nutrients	123:131	nutrients	123:131	Environmental cues such as nutrients alter cellular behaviors by acting on a wide array of molecular sensors inside cells.
31932432	2	29	theme	sugars	288:293	arg1	effects					269:275	effects	269:275	effects of dietary sugars on cancer proliferation	269:317	Of emerging interest is the link observed between effects of dietary sugars on cancer proliferation.
31932432	1	30	theme	sensors	197:203	arg1	array					178:182	a wide array	171:182	a wide array of molecular sensors inside cells	171:216	Environmental cues such as nutrients alter cellular behaviors by acting on a wide array of molecular sensors inside cells.
31932432	0	31	theme	Hipk	34:37	arg1	stability					39:47	Hipk stability	34:47	Hipk stability	34:47	The nutrient sensor OGT regulates Hipk stability and tumorigenic-like activities in Drosophila.
31932432	5	32	theme	Hipk	687:690	arg1	stability					700:708	Hipk protein stability	687:708	Hipk protein stability	687:708	We further show that OGT maintains Hipk protein stability by blocking its proteasomal degradation and that Hipk is O-GlcNAcylated by OGT.
31932432	2	33	theme	interest	231:238	arg1	link					247:250	the link	243:250	the link observed between effects of dietary sugars on cancer proliferation	243:317	Of emerging interest is the link observed between effects of dietary sugars on cancer proliferation.
31932432	9	34	theme	conserved	1105:1113	arg1	role					1115:1118	a conserved role	1103:1118	a conserved role of OGT in positively regulating the protein stability of HIPKs (fly Hipk and human HIPK2), which likely permits the nutritional responsiveness of HIPKs	1103:1270	Together, our data demonstrate a conserved role of OGT in positively regulating the protein stability of HIPKs (fly Hipk and human HIPK2), which likely permits the nutritional responsiveness of HIPKs.
31932432	7	35	from	residues	990:997	arg1	modified					955:962	modified	955:962	modified	955:962	Mass spectrometry analyses reveal that HIPK2 is at least O-GlcNAc modified at S852, T1009, and S1147 residues.
31932432	3	36	theme	O-GlcNAc	400:407	arg1	OGT					422:424	OGT	422:424	OGT	422:424	Here, we identify the requirements of hexosamine biosynthetic pathway (HBP) and O-GlcNAc transferase (OGT) for Drosophila homeodomain-interacting protein kinase (Hipk)-induced growth abnormalities in response to a high sugar diet.
31932432	3	36	theme	O-GlcNAc	400:407	arg1	transferase					409:419	O-GlcNAc transferase	400:419	O-GlcNAc transferase (OGT)	400:425	Here, we identify the requirements of hexosamine biosynthetic pathway (HBP) and O-GlcNAc transferase (OGT) for Drosophila homeodomain-interacting protein kinase (Hipk)-induced growth abnormalities in response to a high sugar diet.
31932432	5	37	theme	protein	692:698	arg1	stability					700:708	Hipk protein stability	687:708	Hipk protein stability	687:708	We further show that OGT maintains Hipk protein stability by blocking its proteasomal degradation and that Hipk is O-GlcNAcylated by OGT.
31932432	2	38	theme	emerging	222:229	arg1	interest					231:238	emerging interest	222:238	emerging interest	222:238	Of emerging interest is the link observed between effects of dietary sugars on cancer proliferation.
31932432	3	39	theme	Drosophila	431:440	arg1	kinase					474:479	Drosophila homeodomain-interacting protein kinase	431:479	Drosophila homeodomain-interacting protein kinase	431:479	Here, we identify the requirements of hexosamine biosynthetic pathway (HBP) and O-GlcNAc transferase (OGT) for Drosophila homeodomain-interacting protein kinase (Hipk)-induced growth abnormalities in response to a high sugar diet.
31932432	6	40	theme	HIPK2	816:820	arg1	proteins					822:829	human HIPK2 proteins	810:829	human HIPK2 proteins	810:829	In mammalian cells, human HIPK2 proteins accumulate posttranscriptionally upon OGT overexpression.
31932432	9	41	theme	OGT	1123:1125	arg1	role					1115:1118	a conserved role	1103:1118	a conserved role of OGT in positively regulating the protein stability of HIPKs (fly Hipk and human HIPK2), which likely permits the nutritional responsiveness of HIPKs	1103:1270	Together, our data demonstrate a conserved role of OGT in positively regulating the protein stability of HIPKs (fly Hipk and human HIPK2), which likely permits the nutritional responsiveness of HIPKs.
31932432	2	42	from	effects	269:275	arg1	proliferation					305:317	cancer proliferation	298:317	cancer proliferation	298:317	Of emerging interest is the link observed between effects of dietary sugars on cancer proliferation.
31932432	6	43	theme	human	810:814	arg1	proteins					822:829	human HIPK2 proteins	810:829	human HIPK2 proteins	810:829	In mammalian cells, human HIPK2 proteins accumulate posttranscriptionally upon OGT overexpression.
31932432	1	44	theme	cellular	139:146	arg1	behaviors					148:156	cellular behaviors	139:156	cellular behaviors	139:156	Environmental cues such as nutrients alter cellular behaviors by acting on a wide array of molecular sensors inside cells.
31932432	7	45	theme	spectrometry	894:905	arg1	analyses					907:914	Mass spectrometry analyses	889:914	Mass spectrometry analyses	889:914	Mass spectrometry analyses reveal that HIPK2 is at least O-GlcNAc modified at S852, T1009, and S1147 residues.
31932432	5	46	theme	proteasomal	726:736	arg1	degradation					738:748	its proteasomal degradation	722:748	its proteasomal degradation	722:748	We further show that OGT maintains Hipk protein stability by blocking its proteasomal degradation and that Hipk is O-GlcNAcylated by OGT.
31932432	9	47	theme	nutritional	1236:1246	arg1	responsiveness					1248:1261	the nutritional responsiveness	1232:1261	the nutritional responsiveness of HIPKs	1232:1270	Together, our data demonstrate a conserved role of OGT in positively regulating the protein stability of HIPKs (fly Hipk and human HIPK2), which likely permits the nutritional responsiveness of HIPKs.
31932432	3	48	theme	homeodomain-interacting	442:464	arg1	kinase					474:479	Drosophila homeodomain-interacting protein kinase	431:479	Drosophila homeodomain-interacting protein kinase	431:479	Here, we identify the requirements of hexosamine biosynthetic pathway (HBP) and O-GlcNAc transferase (OGT) for Drosophila homeodomain-interacting protein kinase (Hipk)-induced growth abnormalities in response to a high sugar diet.
31932432	4	49	theme	Hipk-mediated	619:631	arg1	growth					644:649	Hipk-mediated tumor-like growth	619:649	Hipk-mediated tumor-like growth	619:649	On a normal diet, OGT is both necessary and sufficient for inducing Hipk-mediated tumor-like growth.
31932432	0	50	theme	tumorigenic-like	53:68	arg1	activities					70:79	tumorigenic-like activities	53:79	tumorigenic-like activities	53:79	The nutrient sensor OGT regulates Hipk stability and tumorigenic-like activities in Drosophila.
31932432	0	51	theme	sensor	13:18	arg1	OGT					20:22	The nutrient sensor OGT	0:22	The nutrient sensor OGT	0:22	The nutrient sensor OGT regulates Hipk stability and tumorigenic-like activities in Drosophila.
31932432	3	52	theme	pathway	382:388	arg1	requirements					342:353	the requirements	338:353	the requirements of hexosamine biosynthetic pathway (HBP) and O-GlcNAc transferase (OGT) for Drosophila homeodomain-interacting protein kinase (Hipk)-induced growth abnormalities in response to a high sugar diet	338:548	Here, we identify the requirements of hexosamine biosynthetic pathway (HBP) and O-GlcNAc transferase (OGT) for Drosophila homeodomain-interacting protein kinase (Hipk)-induced growth abnormalities in response to a high sugar diet.
28450420	0	0	theme	Dynamics	93:100	arg1	Identification					12:25	Identification	12:25	Identification	12:25	Validation, Identification, and Biological Consequences of the Site-specific O-GlcNAcylation Dynamics of Carbohydrate-responsive Element-binding Protein (ChREBP).
28450420	0	0	theme	Dynamics	93:100	arg1	Validation					0:9	Validation	0:9	Validation	0:9	Validation, Identification, and Biological Consequences of the Site-specific O-GlcNAcylation Dynamics of Carbohydrate-responsive Element-binding Protein (ChREBP).
28450420	0	0	theme	Dynamics	93:100	arg1	Consequences					43:54	Biological Consequences	32:54	Biological Consequences of the Site-specific O-GlcNAcylation Dynamics of Carbohydrate-responsive Element-binding Protein (ChREBP)	32:160	Validation, Identification, and Biological Consequences of the Site-specific O-GlcNAcylation Dynamics of Carbohydrate-responsive Element-binding Protein (ChREBP).
28450420	1	1	theme	O-GlcNAcylation	372:386	arg1	sites					388:392	no exact O-GlcNAcylation sites	363:392	no exact O-GlcNAcylation sites	363:392	O-GlcNAcylation of carbohydrate-responsive element-binding protein (ChREBP) is believed as an important modulator of ChREBP activities, however little direct evidence of O-GlcNAcylation on ChREBP and no exact O-GlcNAcylation sites have been reported so far.
28450420	1	2	theme	carbohydrate-responsive	182:204	arg1	ChREBP					231:236	ChREBP	231:236	ChREBP	231:236	O-GlcNAcylation of carbohydrate-responsive element-binding protein (ChREBP) is believed as an important modulator of ChREBP activities, however little direct evidence of O-GlcNAcylation on ChREBP and no exact O-GlcNAcylation sites have been reported so far.
28450420	1	2	theme	carbohydrate-responsive	182:204	arg1	protein					222:228	carbohydrate-responsive element-binding protein	182:228	carbohydrate-responsive element-binding protein (ChREBP)	182:237	O-GlcNAcylation of carbohydrate-responsive element-binding protein (ChREBP) is believed as an important modulator of ChREBP activities, however little direct evidence of O-GlcNAcylation on ChREBP and no exact O-GlcNAcylation sites have been reported so far.
28450420	1	3	theme	activities	287:296	arg1	modulator					267:275	an important modulator	254:275	an important modulator of ChREBP activities	254:296	O-GlcNAcylation of carbohydrate-responsive element-binding protein (ChREBP) is believed as an important modulator of ChREBP activities, however little direct evidence of O-GlcNAcylation on ChREBP and no exact O-GlcNAcylation sites have been reported so far.
28450420	1	3	theme	activities	287:296	arg1	O-GlcNAcylation					163:177	O-GlcNAcylation	163:177	O-GlcNAcylation of carbohydrate-responsive element-binding protein (ChREBP)	163:237	O-GlcNAcylation of carbohydrate-responsive element-binding protein (ChREBP) is believed as an important modulator of ChREBP activities, however little direct evidence of O-GlcNAcylation on ChREBP and no exact O-GlcNAcylation sites have been reported so far.
28450420	1	3	theme	activities	287:296	arg1	evidence					321:328	little direct evidence	307:328	little direct evidence of O-GlcNAcylation on ChREBP	307:357	O-GlcNAcylation of carbohydrate-responsive element-binding protein (ChREBP) is believed as an important modulator of ChREBP activities, however little direct evidence of O-GlcNAcylation on ChREBP and no exact O-GlcNAcylation sites have been reported so far.
28450420	0	4	theme	O-GlcNAcylation	77:91	arg1	Dynamics					93:100	the Site-specific O-GlcNAcylation Dynamics	59:100	the Site-specific O-GlcNAcylation Dynamics of Carbohydrate-responsive Element-binding Protein (ChREBP)	59:160	Validation, Identification, and Biological Consequences of the Site-specific O-GlcNAcylation Dynamics of Carbohydrate-responsive Element-binding Protein (ChREBP).
28450420	2	5	theme	chemoenzymatic	535:548	arg1	labeling					564:571	chemoenzymatic and metabolic labeling	535:571	chemoenzymatic and metabolic labeling	535:571	Here, we validate O-GlcNAcylation on ChREBP in cell-free coupled transcription/translation system and in cells by chemoenzymatic and metabolic labeling, respectively.
28450420	1	6	theme	element-binding	206:220	arg1	ChREBP					231:236	ChREBP	231:236	ChREBP	231:236	O-GlcNAcylation of carbohydrate-responsive element-binding protein (ChREBP) is believed as an important modulator of ChREBP activities, however little direct evidence of O-GlcNAcylation on ChREBP and no exact O-GlcNAcylation sites have been reported so far.
28450420	1	6	theme	element-binding	206:220	arg1	protein					222:228	carbohydrate-responsive element-binding protein	182:228	carbohydrate-responsive element-binding protein (ChREBP)	182:237	O-GlcNAcylation of carbohydrate-responsive element-binding protein (ChREBP) is believed as an important modulator of ChREBP activities, however little direct evidence of O-GlcNAcylation on ChREBP and no exact O-GlcNAcylation sites have been reported so far.
28450420	0	7	theme	Carbohydrate-responsive	105:127	arg1	ChREBP					154:159	ChREBP	154:159	ChREBP	154:159	Validation, Identification, and Biological Consequences of the Site-specific O-GlcNAcylation Dynamics of Carbohydrate-responsive Element-binding Protein (ChREBP).
28450420	0	7	theme	Carbohydrate-responsive	105:127	arg1	Protein					145:151	Carbohydrate-responsive Element-binding Protein	105:151	Carbohydrate-responsive Element-binding Protein (ChREBP)	105:160	Validation, Identification, and Biological Consequences of the Site-specific O-GlcNAcylation Dynamics of Carbohydrate-responsive Element-binding Protein (ChREBP).
28450420	6	8	theme	dynamics	1393:1400	arg1	consequences					1343:1354	the biological consequences	1328:1354	the biological consequences of the site-specific O-GlcNAcylation dynamics of ChREBP	1328:1410	This work is a detailed study of ChREBP O-GlcNAcylation and highlights the biological consequences of the site-specific O-GlcNAcylation dynamics of ChREBP.
28450420	4	9	theme	transcriptional	945:959	arg1	activity					961:968	the transcriptional activity	941:968	the transcriptional activity of ChREBP	941:978	Under high glucose conditions, Ser514 phosphorylation enhances ChREBP O-GlcNAcylation, maintaining the transcriptional activity of ChREBP; Ser839 O-GlcNAcylation is essential for Mlx-heterodimerization and DNA-binding activity enhancement, consequently inducing transcriptional activity.
28450420	1	10	theme	little	307:312	arg1	evidence					321:328	little direct evidence	307:328	little direct evidence of O-GlcNAcylation on ChREBP	307:357	O-GlcNAcylation of carbohydrate-responsive element-binding protein (ChREBP) is believed as an important modulator of ChREBP activities, however little direct evidence of O-GlcNAcylation on ChREBP and no exact O-GlcNAcylation sites have been reported so far.
28450420	1	10	theme	little	307:312	arg1	O-GlcNAcylation					163:177	O-GlcNAcylation	163:177	O-GlcNAcylation of carbohydrate-responsive element-binding protein (ChREBP)	163:237	O-GlcNAcylation of carbohydrate-responsive element-binding protein (ChREBP) is believed as an important modulator of ChREBP activities, however little direct evidence of O-GlcNAcylation on ChREBP and no exact O-GlcNAcylation sites have been reported so far.
28450420	1	10	theme	little	307:312	arg1	modulator					267:275	an important modulator	254:275	an important modulator of ChREBP activities	254:296	O-GlcNAcylation of carbohydrate-responsive element-binding protein (ChREBP) is believed as an important modulator of ChREBP activities, however little direct evidence of O-GlcNAcylation on ChREBP and no exact O-GlcNAcylation sites have been reported so far.
28450420	0	11	theme	Protein	145:151	arg1	Dynamics					93:100	the Site-specific O-GlcNAcylation Dynamics	59:100	the Site-specific O-GlcNAcylation Dynamics of Carbohydrate-responsive Element-binding Protein (ChREBP)	59:160	Validation, Identification, and Biological Consequences of the Site-specific O-GlcNAcylation Dynamics of Carbohydrate-responsive Element-binding Protein (ChREBP).
28450420	4	12	theme	ChREBP	905:910	arg1	O-GlcNAcylation					912:926	ChREBP O-GlcNAcylation	905:926	ChREBP O-GlcNAcylation	905:926	Under high glucose conditions, Ser514 phosphorylation enhances ChREBP O-GlcNAcylation, maintaining the transcriptional activity of ChREBP; Ser839 O-GlcNAcylation is essential for Mlx-heterodimerization and DNA-binding activity enhancement, consequently inducing transcriptional activity.
28450420	6	13	theme	O-GlcNAcylation	1297:1311	arg1	study					1281:1285	a detailed study	1270:1285	a detailed study of ChREBP O-GlcNAcylation	1270:1311	This work is a detailed study of ChREBP O-GlcNAcylation and highlights the biological consequences of the site-specific O-GlcNAcylation dynamics of ChREBP.
28450420	6	13	theme	O-GlcNAcylation	1297:1311	arg1	work					1262:1265	This work	1257:1265	This work	1257:1265	This work is a detailed study of ChREBP O-GlcNAcylation and highlights the biological consequences of the site-specific O-GlcNAcylation dynamics of ChREBP.
28450420	1	14	theme	protein	222:228	arg1	modulator					267:275	an important modulator	254:275	an important modulator of ChREBP activities	254:296	O-GlcNAcylation of carbohydrate-responsive element-binding protein (ChREBP) is believed as an important modulator of ChREBP activities, however little direct evidence of O-GlcNAcylation on ChREBP and no exact O-GlcNAcylation sites have been reported so far.
28450420	1	14	theme	protein	222:228	arg1	O-GlcNAcylation					163:177	O-GlcNAcylation	163:177	O-GlcNAcylation of carbohydrate-responsive element-binding protein (ChREBP)	163:237	O-GlcNAcylation of carbohydrate-responsive element-binding protein (ChREBP) is believed as an important modulator of ChREBP activities, however little direct evidence of O-GlcNAcylation on ChREBP and no exact O-GlcNAcylation sites have been reported so far.
28450420	1	14	theme	protein	222:228	arg1	evidence					321:328	little direct evidence	307:328	little direct evidence of O-GlcNAcylation on ChREBP	307:357	O-GlcNAcylation of carbohydrate-responsive element-binding protein (ChREBP) is believed as an important modulator of ChREBP activities, however little direct evidence of O-GlcNAcylation on ChREBP and no exact O-GlcNAcylation sites have been reported so far.
28450420	0	15	theme	Element-binding	129:143	arg1	ChREBP					154:159	ChREBP	154:159	ChREBP	154:159	Validation, Identification, and Biological Consequences of the Site-specific O-GlcNAcylation Dynamics of Carbohydrate-responsive Element-binding Protein (ChREBP).
28450420	0	15	theme	Element-binding	129:143	arg1	Protein					145:151	Carbohydrate-responsive Element-binding Protein	105:151	Carbohydrate-responsive Element-binding Protein (ChREBP)	105:160	Validation, Identification, and Biological Consequences of the Site-specific O-GlcNAcylation Dynamics of Carbohydrate-responsive Element-binding Protein (ChREBP).
28450420	6	16	theme	ChREBP	1290:1295	arg1	O-GlcNAcylation					1297:1311	ChREBP O-GlcNAcylation	1290:1311	ChREBP O-GlcNAcylation	1290:1311	This work is a detailed study of ChREBP O-GlcNAcylation and highlights the biological consequences of the site-specific O-GlcNAcylation dynamics of ChREBP.
28450420	4	17	theme	activity	1060:1067	arg1	enhancement					1069:1079	DNA-binding activity enhancement	1048:1079	DNA-binding activity enhancement	1048:1079	Under high glucose conditions, Ser514 phosphorylation enhances ChREBP O-GlcNAcylation, maintaining the transcriptional activity of ChREBP; Ser839 O-GlcNAcylation is essential for Mlx-heterodimerization and DNA-binding activity enhancement, consequently inducing transcriptional activity.
28450420	2	18	theme	transcription/translation	486:510	arg1	system					512:517	cell-free coupled transcription/translation system	468:517	cell-free coupled transcription/translation system	468:517	Here, we validate O-GlcNAcylation on ChREBP in cell-free coupled transcription/translation system and in cells by chemoenzymatic and metabolic labeling, respectively.
28450420	6	19	theme	ChREBP	1405:1410	arg1	dynamics					1393:1400	the site-specific O-GlcNAcylation dynamics	1359:1400	the site-specific O-GlcNAcylation dynamics of ChREBP	1359:1410	This work is a detailed study of ChREBP O-GlcNAcylation and highlights the biological consequences of the site-specific O-GlcNAcylation dynamics of ChREBP.
28450420	2	20	theme	metabolic	554:562	arg1	labeling					564:571	chemoenzymatic and metabolic labeling	535:571	chemoenzymatic and metabolic labeling	535:571	Here, we validate O-GlcNAcylation on ChREBP in cell-free coupled transcription/translation system and in cells by chemoenzymatic and metabolic labeling, respectively.
28450420	2	21	theme	coupled	478:484	arg1	system					512:517	cell-free coupled transcription/translation system	468:517	cell-free coupled transcription/translation system	468:517	Here, we validate O-GlcNAcylation on ChREBP in cell-free coupled transcription/translation system and in cells by chemoenzymatic and metabolic labeling, respectively.
28450420	1	22	theme	direct	314:319	arg1	evidence					321:328	little direct evidence	307:328	little direct evidence of O-GlcNAcylation on ChREBP	307:357	O-GlcNAcylation of carbohydrate-responsive element-binding protein (ChREBP) is believed as an important modulator of ChREBP activities, however little direct evidence of O-GlcNAcylation on ChREBP and no exact O-GlcNAcylation sites have been reported so far.
28450420	1	22	theme	direct	314:319	arg1	O-GlcNAcylation					163:177	O-GlcNAcylation	163:177	O-GlcNAcylation of carbohydrate-responsive element-binding protein (ChREBP)	163:237	O-GlcNAcylation of carbohydrate-responsive element-binding protein (ChREBP) is believed as an important modulator of ChREBP activities, however little direct evidence of O-GlcNAcylation on ChREBP and no exact O-GlcNAcylation sites have been reported so far.
28450420	1	22	theme	direct	314:319	arg1	modulator					267:275	an important modulator	254:275	an important modulator of ChREBP activities	254:296	O-GlcNAcylation of carbohydrate-responsive element-binding protein (ChREBP) is believed as an important modulator of ChREBP activities, however little direct evidence of O-GlcNAcylation on ChREBP and no exact O-GlcNAcylation sites have been reported so far.
28450420	1	23	from	evidence	321:328	arg1	ChREBP					352:357	ChREBP	352:357	ChREBP	352:357	O-GlcNAcylation of carbohydrate-responsive element-binding protein (ChREBP) is believed as an important modulator of ChREBP activities, however little direct evidence of O-GlcNAcylation on ChREBP and no exact O-GlcNAcylation sites have been reported so far.
28450420	2	24	theme	cell-free	468:476	arg1	system					512:517	cell-free coupled transcription/translation system	468:517	cell-free coupled transcription/translation system	468:517	Here, we validate O-GlcNAcylation on ChREBP in cell-free coupled transcription/translation system and in cells by chemoenzymatic and metabolic labeling, respectively.
28450420	3	25	theme	molecular	800:808	arg1	method					834:839	molecular and chemical biological method	800:839	molecular and chemical biological method	800:839	Moreover, for the first time, we identify O-GlcNAcylation on Ser614 in the C-terminus of ChREBP by mass spectrometry and validate two important sites, Thr517 and Ser839 for O-GlcNAcylation and their function via molecular and chemical biological method.
28450420	3	26	theme	first	606:610	arg1	time					612:615	the first time	602:615	the first time	602:615	Moreover, for the first time, we identify O-GlcNAcylation on Ser614 in the C-terminus of ChREBP by mass spectrometry and validate two important sites, Thr517 and Ser839 for O-GlcNAcylation and their function via molecular and chemical biological method.
28450420	3	27	from	O-GlcNAcylation	630:644	arg1	Ser614					649:654	Ser614	649:654	Ser614	649:654	Moreover, for the first time, we identify O-GlcNAcylation on Ser614 in the C-terminus of ChREBP by mass spectrometry and validate two important sites, Thr517 and Ser839 for O-GlcNAcylation and their function via molecular and chemical biological method.
28450420	3	27	from	O-GlcNAcylation	630:644	arg1	C-terminus					663:672	the C-terminus	659:672	the C-terminus of ChREBP	659:682	Moreover, for the first time, we identify O-GlcNAcylation on Ser614 in the C-terminus of ChREBP by mass spectrometry and validate two important sites, Thr517 and Ser839 for O-GlcNAcylation and their function via molecular and chemical biological method.
28450420	3	28	theme	mass	687:690	arg1	spectrometry					692:703	mass spectrometry	687:703	mass spectrometry	687:703	Moreover, for the first time, we identify O-GlcNAcylation on Ser614 in the C-terminus of ChREBP by mass spectrometry and validate two important sites, Thr517 and Ser839 for O-GlcNAcylation and their function via molecular and chemical biological method.
28450420	6	29	theme	biological	1332:1341	arg1	consequences					1343:1354	the biological consequences	1328:1354	the biological consequences of the site-specific O-GlcNAcylation dynamics of ChREBP	1328:1410	This work is a detailed study of ChREBP O-GlcNAcylation and highlights the biological consequences of the site-specific O-GlcNAcylation dynamics of ChREBP.
28450420	0	30	theme	Biological	32:41	arg1	Consequences					43:54	Biological Consequences	32:54	Biological Consequences of the Site-specific O-GlcNAcylation Dynamics of Carbohydrate-responsive Element-binding Protein (ChREBP)	32:160	Validation, Identification, and Biological Consequences of the Site-specific O-GlcNAcylation Dynamics of Carbohydrate-responsive Element-binding Protein (ChREBP).
28450420	1	31	theme	O-GlcNAcylation	333:347	arg1	evidence					321:328	little direct evidence	307:328	little direct evidence of O-GlcNAcylation on ChREBP	307:357	O-GlcNAcylation of carbohydrate-responsive element-binding protein (ChREBP) is believed as an important modulator of ChREBP activities, however little direct evidence of O-GlcNAcylation on ChREBP and no exact O-GlcNAcylation sites have been reported so far.
28450420	1	31	theme	O-GlcNAcylation	333:347	arg1	O-GlcNAcylation					163:177	O-GlcNAcylation	163:177	O-GlcNAcylation of carbohydrate-responsive element-binding protein (ChREBP)	163:237	O-GlcNAcylation of carbohydrate-responsive element-binding protein (ChREBP) is believed as an important modulator of ChREBP activities, however little direct evidence of O-GlcNAcylation on ChREBP and no exact O-GlcNAcylation sites have been reported so far.
28450420	1	31	theme	O-GlcNAcylation	333:347	arg1	modulator					267:275	an important modulator	254:275	an important modulator of ChREBP activities	254:296	O-GlcNAcylation of carbohydrate-responsive element-binding protein (ChREBP) is believed as an important modulator of ChREBP activities, however little direct evidence of O-GlcNAcylation on ChREBP and no exact O-GlcNAcylation sites have been reported so far.
28450420	5	32	theme	Ser839	1130:1135	arg1	O-GlcNAcylation					1137:1151	Ser839 O-GlcNAcylation	1130:1151	Ser839 O-GlcNAcylation	1130:1151	Ser839 O-GlcNAcylation is also crucial for ChREBP nuclear export partially by strengthening interactions with CRM1 and 14-3-3.
28450420	4	33	theme	transcriptional	1104:1118	arg1	activity					1120:1127	transcriptional activity	1104:1127	transcriptional activity	1104:1127	Under high glucose conditions, Ser514 phosphorylation enhances ChREBP O-GlcNAcylation, maintaining the transcriptional activity of ChREBP; Ser839 O-GlcNAcylation is essential for Mlx-heterodimerization and DNA-binding activity enhancement, consequently inducing transcriptional activity.
28450420	3	34	theme	biological	823:832	arg1	method					834:839	molecular and chemical biological method	800:839	molecular and chemical biological method	800:839	Moreover, for the first time, we identify O-GlcNAcylation on Ser614 in the C-terminus of ChREBP by mass spectrometry and validate two important sites, Thr517 and Ser839 for O-GlcNAcylation and their function via molecular and chemical biological method.
28450420	3	35	theme	ChREBP	677:682	arg1	C-terminus					663:672	the C-terminus	659:672	the C-terminus of ChREBP	659:682	Moreover, for the first time, we identify O-GlcNAcylation on Ser614 in the C-terminus of ChREBP by mass spectrometry and validate two important sites, Thr517 and Ser839 for O-GlcNAcylation and their function via molecular and chemical biological method.
28450420	6	36	theme	O-GlcNAcylation	1377:1391	arg1	dynamics					1393:1400	the site-specific O-GlcNAcylation dynamics	1359:1400	the site-specific O-GlcNAcylation dynamics of ChREBP	1359:1410	This work is a detailed study of ChREBP O-GlcNAcylation and highlights the biological consequences of the site-specific O-GlcNAcylation dynamics of ChREBP.
28450420	4	37	theme	DNA-binding	1048:1058	arg1	enhancement					1069:1079	DNA-binding activity enhancement	1048:1079	DNA-binding activity enhancement	1048:1079	Under high glucose conditions, Ser514 phosphorylation enhances ChREBP O-GlcNAcylation, maintaining the transcriptional activity of ChREBP; Ser839 O-GlcNAcylation is essential for Mlx-heterodimerization and DNA-binding activity enhancement, consequently inducing transcriptional activity.
28450420	4	38	theme	ChREBP	973:978	arg1	activity					961:968	the transcriptional activity	941:968	the transcriptional activity of ChREBP	941:978	Under high glucose conditions, Ser514 phosphorylation enhances ChREBP O-GlcNAcylation, maintaining the transcriptional activity of ChREBP; Ser839 O-GlcNAcylation is essential for Mlx-heterodimerization and DNA-binding activity enhancement, consequently inducing transcriptional activity.
28450420	5	39	theme	ChREBP	1173:1178	arg1	export					1188:1193	ChREBP nuclear export	1173:1193	ChREBP nuclear export	1173:1193	Ser839 O-GlcNAcylation is also crucial for ChREBP nuclear export partially by strengthening interactions with CRM1 and 14-3-3.
28450420	6	40	theme	site-specific	1363:1375	arg1	dynamics					1393:1400	the site-specific O-GlcNAcylation dynamics	1359:1400	the site-specific O-GlcNAcylation dynamics of ChREBP	1359:1410	This work is a detailed study of ChREBP O-GlcNAcylation and highlights the biological consequences of the site-specific O-GlcNAcylation dynamics of ChREBP.
28450420	4	41	theme	Ser514	873:878	arg1	phosphorylation					880:894	Ser514 phosphorylation	873:894	Ser514 phosphorylation	873:894	Under high glucose conditions, Ser514 phosphorylation enhances ChREBP O-GlcNAcylation, maintaining the transcriptional activity of ChREBP; Ser839 O-GlcNAcylation is essential for Mlx-heterodimerization and DNA-binding activity enhancement, consequently inducing transcriptional activity.
28450420	3	42	theme	chemical	814:821	arg1	method					834:839	molecular and chemical biological method	800:839	molecular and chemical biological method	800:839	Moreover, for the first time, we identify O-GlcNAcylation on Ser614 in the C-terminus of ChREBP by mass spectrometry and validate two important sites, Thr517 and Ser839 for O-GlcNAcylation and their function via molecular and chemical biological method.
28450420	4	43	theme	Ser839	981:986	arg1	O-GlcNAcylation					988:1002	Ser839 O-GlcNAcylation	981:1002	Ser839 O-GlcNAcylation	981:1002	Under high glucose conditions, Ser514 phosphorylation enhances ChREBP O-GlcNAcylation, maintaining the transcriptional activity of ChREBP; Ser839 O-GlcNAcylation is essential for Mlx-heterodimerization and DNA-binding activity enhancement, consequently inducing transcriptional activity.
28450420	3	44	theme	important	722:730	arg1	Thr517					739:744	Thr517	739:744	Thr517	739:744	Moreover, for the first time, we identify O-GlcNAcylation on Ser614 in the C-terminus of ChREBP by mass spectrometry and validate two important sites, Thr517 and Ser839 for O-GlcNAcylation and their function via molecular and chemical biological method.
28450420	3	44	theme	important	722:730	arg1	sites					732:736	two important sites	718:736	two important sites	718:736	Moreover, for the first time, we identify O-GlcNAcylation on Ser614 in the C-terminus of ChREBP by mass spectrometry and validate two important sites, Thr517 and Ser839 for O-GlcNAcylation and their function via molecular and chemical biological method.
28450420	3	44	theme	important	722:730	arg1	Ser839					750:755	Ser839	750:755	Ser839	750:755	Moreover, for the first time, we identify O-GlcNAcylation on Ser614 in the C-terminus of ChREBP by mass spectrometry and validate two important sites, Thr517 and Ser839 for O-GlcNAcylation and their function via molecular and chemical biological method.
28450420	6	45	theme	detailed	1272:1279	arg1	study					1281:1285	a detailed study	1270:1285	a detailed study of ChREBP O-GlcNAcylation	1270:1311	This work is a detailed study of ChREBP O-GlcNAcylation and highlights the biological consequences of the site-specific O-GlcNAcylation dynamics of ChREBP.
28450420	6	45	theme	detailed	1272:1279	arg1	work					1262:1265	This work	1257:1265	This work	1257:1265	This work is a detailed study of ChREBP O-GlcNAcylation and highlights the biological consequences of the site-specific O-GlcNAcylation dynamics of ChREBP.
28450420	1	46	theme	important	257:265	arg1	modulator					267:275	an important modulator	254:275	an important modulator of ChREBP activities	254:296	O-GlcNAcylation of carbohydrate-responsive element-binding protein (ChREBP) is believed as an important modulator of ChREBP activities, however little direct evidence of O-GlcNAcylation on ChREBP and no exact O-GlcNAcylation sites have been reported so far.
28450420	1	46	theme	important	257:265	arg1	O-GlcNAcylation					163:177	O-GlcNAcylation	163:177	O-GlcNAcylation of carbohydrate-responsive element-binding protein (ChREBP)	163:237	O-GlcNAcylation of carbohydrate-responsive element-binding protein (ChREBP) is believed as an important modulator of ChREBP activities, however little direct evidence of O-GlcNAcylation on ChREBP and no exact O-GlcNAcylation sites have been reported so far.
28450420	1	46	theme	important	257:265	arg1	evidence					321:328	little direct evidence	307:328	little direct evidence of O-GlcNAcylation on ChREBP	307:357	O-GlcNAcylation of carbohydrate-responsive element-binding protein (ChREBP) is believed as an important modulator of ChREBP activities, however little direct evidence of O-GlcNAcylation on ChREBP and no exact O-GlcNAcylation sites have been reported so far.
28450420	5	47	theme	nuclear	1180:1186	arg1	export					1188:1193	ChREBP nuclear export	1173:1193	ChREBP nuclear export	1173:1193	Ser839 O-GlcNAcylation is also crucial for ChREBP nuclear export partially by strengthening interactions with CRM1 and 14-3-3.
28450420	2	48	from	O-GlcNAcylation	439:453	arg1	ChREBP					458:463	ChREBP	458:463	ChREBP	458:463	Here, we validate O-GlcNAcylation on ChREBP in cell-free coupled transcription/translation system and in cells by chemoenzymatic and metabolic labeling, respectively.
28450420	2	48	from	O-GlcNAcylation	439:453	arg1	system					512:517	cell-free coupled transcription/translation system	468:517	cell-free coupled transcription/translation system	468:517	Here, we validate O-GlcNAcylation on ChREBP in cell-free coupled transcription/translation system and in cells by chemoenzymatic and metabolic labeling, respectively.
28450420	2	48	from	O-GlcNAcylation	439:453	arg1	cells					526:530	cells	526:530	cells	526:530	Here, we validate O-GlcNAcylation on ChREBP in cell-free coupled transcription/translation system and in cells by chemoenzymatic and metabolic labeling, respectively.
28450420	5	49	with	interactions	1222:1233	arg1	14-3-3					1249:1254	14-3-3	1249:1254	14-3-3	1249:1254	Ser839 O-GlcNAcylation is also crucial for ChREBP nuclear export partially by strengthening interactions with CRM1 and 14-3-3.
28450420	5	49	with	interactions	1222:1233	arg1	CRM1					1240:1243	CRM1	1240:1243	CRM1	1240:1243	Ser839 O-GlcNAcylation is also crucial for ChREBP nuclear export partially by strengthening interactions with CRM1 and 14-3-3.
28450420	0	50	theme	Site-specific	63:75	arg1	Dynamics					93:100	the Site-specific O-GlcNAcylation Dynamics	59:100	the Site-specific O-GlcNAcylation Dynamics of Carbohydrate-responsive Element-binding Protein (ChREBP)	59:160	Validation, Identification, and Biological Consequences of the Site-specific O-GlcNAcylation Dynamics of Carbohydrate-responsive Element-binding Protein (ChREBP).
28450420	4	51	theme	glucose	853:859	arg1	conditions					861:870	high glucose conditions	848:870	high glucose conditions	848:870	Under high glucose conditions, Ser514 phosphorylation enhances ChREBP O-GlcNAcylation, maintaining the transcriptional activity of ChREBP; Ser839 O-GlcNAcylation is essential for Mlx-heterodimerization and DNA-binding activity enhancement, consequently inducing transcriptional activity.
28450420	1	52	theme	exact	366:370	arg1	sites					388:392	no exact O-GlcNAcylation sites	363:392	no exact O-GlcNAcylation sites	363:392	O-GlcNAcylation of carbohydrate-responsive element-binding protein (ChREBP) is believed as an important modulator of ChREBP activities, however little direct evidence of O-GlcNAcylation on ChREBP and no exact O-GlcNAcylation sites have been reported so far.
28450420	4	53	theme	high	848:851	arg1	conditions					861:870	high glucose conditions	848:870	high glucose conditions	848:870	Under high glucose conditions, Ser514 phosphorylation enhances ChREBP O-GlcNAcylation, maintaining the transcriptional activity of ChREBP; Ser839 O-GlcNAcylation is essential for Mlx-heterodimerization and DNA-binding activity enhancement, consequently inducing transcriptional activity.
28450420	1	54	theme	ChREBP	280:285	arg1	activities					287:296	ChREBP activities	280:296	ChREBP activities	280:296	O-GlcNAcylation of carbohydrate-responsive element-binding protein (ChREBP) is believed as an important modulator of ChREBP activities, however little direct evidence of O-GlcNAcylation on ChREBP and no exact O-GlcNAcylation sites have been reported so far.
32513743	10	0	gly	O-GlcNAcylation	1254:1268	arg1	growth					1298:1303	tumor growth	1292:1303	tumor growth	1292:1303	Thus, this study suggests that LATS2 O-GlcNAcylation is deeply involved in tumor growth by playing a critical role in dysregulation of the Hippo pathway in cancer cells.
32513743	4	1	from	cells	520:524	arg1	cause					478:482	a cause	476:482	a cause of hyperactivation of YAP in cancer cells	476:524	Aberrantly increased O-GlcNAcylation has recently emerged as a cause of hyperactivation of YAP in cancer cells.
32513743	5	2	theme	LATS-mediated	599:611	arg1	feedback					622:629	LATS-mediated negative feedback	599:629	LATS-mediated negative feedback	599:629	However, the mechanism, which induces hyperactivation of TAZ and blocks LATS-mediated negative feedback, remains to be elucidated in cancer cells.
32513743	9	3	theme	feedback	1202:1209	arg1	loop					1211:1214	the LATS-mediated negative feedback loop	1175:1214	the LATS-mediated negative feedback loop	1175:1214	LATS2 is a core component in the LATS-mediated negative feedback loop.
32513743	7	4	theme	O-GlcNAcylated	877:890	arg1	components					892:901	the newly identified O-GlcNAcylated components	856:901	the newly identified O-GlcNAcylated components in the MST-LATS kinase cascade	856:932	LATS2 is one of the newly identified O-GlcNAcylated components in the MST-LATS kinase cascade.
32513743	3	5	theme	various	366:372	arg1	cells					381:385	various cancer cells	366:385	various cancer cells which lead to tumor growth	366:412	YAP and TAZ are hyperactivated in various cancer cells which lead to tumor growth.
32513743	0	6	from	O-GlcNAcylation	0:14	arg1	LATS2					19:23	LATS2	19:23	LATS2	19:23	O-GlcNAcylation on LATS2 disrupts the Hippo pathway by inhibiting its activity.
32513743	5	7	theme	negative	613:620	arg1	feedback					622:629	LATS-mediated negative feedback	599:629	LATS-mediated negative feedback	599:629	However, the mechanism, which induces hyperactivation of TAZ and blocks LATS-mediated negative feedback, remains to be elucidated in cancer cells.
32513743	7	8	theme	components	892:901	arg1	one					849:851	one	849:851	one	849:851	LATS2 is one of the newly identified O-GlcNAcylated components in the MST-LATS kinase cascade.
32513743	7	8	theme	components	892:901	arg1	components					892:901	the newly identified O-GlcNAcylated components	856:901	the newly identified O-GlcNAcylated components in the MST-LATS kinase cascade	856:932	LATS2 is one of the newly identified O-GlcNAcylated components in the MST-LATS kinase cascade.
32513743	3	9	theme	cancer	374:379	arg1	cells					381:385	various cancer cells	366:385	various cancer cells which lead to tumor growth	366:412	YAP and TAZ are hyperactivated in various cancer cells which lead to tumor growth.
32513743	4	10	theme	hyperactivation	487:501	arg1	cause					478:482	a cause	476:482	a cause of hyperactivation of YAP in cancer cells	476:524	Aberrantly increased O-GlcNAcylation has recently emerged as a cause of hyperactivation of YAP in cancer cells.
32513743	9	11	theme	LATS-mediated	1179:1191	arg1	loop					1211:1214	the LATS-mediated negative feedback loop	1175:1214	the LATS-mediated negative feedback loop	1175:1214	LATS2 is a core component in the LATS-mediated negative feedback loop.
32513743	7	12	from	components	892:901	arg1	cascade					926:932	the MST-LATS kinase cascade	906:932	the MST-LATS kinase cascade	906:932	LATS2 is one of the newly identified O-GlcNAcylated components in the MST-LATS kinase cascade.
32513743	10	13	theme	tumor	1292:1296	arg1	growth					1298:1303	tumor growth	1292:1303	tumor growth	1292:1303	Thus, this study suggests that LATS2 O-GlcNAcylation is deeply involved in tumor growth by playing a critical role in dysregulation of the Hippo pathway in cancer cells.
32513743	6	14	theme	negative	809:816	arg1	regulator					818:826	a direct negative regulator	800:826	a direct negative regulator of YAP/TAZ	800:837	This study found that in breast cancer cells, abnormally increased O-GlcNAcylation hyperactivates YAP/TAZ and inhibits LATS2, a direct negative regulator of YAP/TAZ.
32513743	6	14	theme	negative	809:816	arg1	LATS2					793:797	LATS2	793:797	LATS2	793:797	This study found that in breast cancer cells, abnormally increased O-GlcNAcylation hyperactivates YAP/TAZ and inhibits LATS2, a direct negative regulator of YAP/TAZ.
32513743	6	15	theme	cancer	706:711	arg1	cells					713:717	breast cancer cells	699:717	breast cancer cells	699:717	This study found that in breast cancer cells, abnormally increased O-GlcNAcylation hyperactivates YAP/TAZ and inhibits LATS2, a direct negative regulator of YAP/TAZ.
32513743	4	16	theme	YAP	506:508	arg1	hyperactivation					487:501	hyperactivation	487:501	hyperactivation of YAP in cancer cells	487:524	Aberrantly increased O-GlcNAcylation has recently emerged as a cause of hyperactivation of YAP in cancer cells.
32513743	6	17	theme	direct	802:807	arg1	regulator					818:826	a direct negative regulator	800:826	a direct negative regulator of YAP/TAZ	800:837	This study found that in breast cancer cells, abnormally increased O-GlcNAcylation hyperactivates YAP/TAZ and inhibits LATS2, a direct negative regulator of YAP/TAZ.
32513743	6	17	theme	direct	802:807	arg1	LATS2					793:797	LATS2	793:797	LATS2	793:797	This study found that in breast cancer cells, abnormally increased O-GlcNAcylation hyperactivates YAP/TAZ and inhibits LATS2, a direct negative regulator of YAP/TAZ.
32513743	6	18	theme	breast	699:704	arg1	cells					713:717	breast cancer cells	699:717	breast cancer cells	699:717	This study found that in breast cancer cells, abnormally increased O-GlcNAcylation hyperactivates YAP/TAZ and inhibits LATS2, a direct negative regulator of YAP/TAZ.
32513743	9	19	from	component	1162:1170	arg1	loop					1211:1214	the LATS-mediated negative feedback loop	1175:1214	the LATS-mediated negative feedback loop	1175:1214	LATS2 is a core component in the LATS-mediated negative feedback loop.
32513743	4	20	from	hyperactivation	487:501	arg1	cells					520:524	cancer cells	513:524	cancer cells	513:524	Aberrantly increased O-GlcNAcylation has recently emerged as a cause of hyperactivation of YAP in cancer cells.
32513743	5	21	theme	TAZ	584:586	arg1	hyperactivation					565:579	hyperactivation	565:579	hyperactivation of TAZ	565:586	However, the mechanism, which induces hyperactivation of TAZ and blocks LATS-mediated negative feedback, remains to be elucidated in cancer cells.
32513743	10	22	from	dysregulation	1335:1347	arg1	cells					1380:1384	cancer cells	1373:1384	cancer cells	1373:1384	Thus, this study suggests that LATS2 O-GlcNAcylation is deeply involved in tumor growth by playing a critical role in dysregulation of the Hippo pathway in cancer cells.
32513743	1	23	theme	Hippo	84:88	arg1	pathway					90:96	The Hippo pathway	80:96	The Hippo pathway	80:96	The Hippo pathway controls organ size and tissue homeostasis by regulating cell proliferation and apoptosis.
32513743	8	24	theme	adaptor	1029:1035	arg1	protein					1037:1043	the MOB1 adaptor protein	1020:1043	the MOB1 adaptor protein	1020:1043	Here, we found that O-GlcNAcylation at LATS2 Thr436 interrupted its interaction with the MOB1 adaptor protein, which connects MST to LATS2, leading to activation of YAP/TAZ by suppressing LATS2 kinase activity.
32513743	2	25	theme	pathway	323:329	arg1	homeostasis					298:308	homeostasis	298:308	homeostasis of the Hippo pathway	298:329	The LATS-mediated negative feedback loop prevents excessive activation of the effectors YAP/TAZ, maintaining homeostasis of the Hippo pathway.
32513743	5	26	theme	cancer	660:665	arg1	cells					667:671	cancer cells	660:671	cancer cells	660:671	However, the mechanism, which induces hyperactivation of TAZ and blocks LATS-mediated negative feedback, remains to be elucidated in cancer cells.
32513743	4	27	from	cause	478:482	arg1	cells					520:524	cancer cells	513:524	cancer cells	513:524	Aberrantly increased O-GlcNAcylation has recently emerged as a cause of hyperactivation of YAP in cancer cells.
32513743	8	28	theme	MOB1	1024:1027	arg1	protein					1037:1043	the MOB1 adaptor protein	1020:1043	the MOB1 adaptor protein	1020:1043	Here, we found that O-GlcNAcylation at LATS2 Thr436 interrupted its interaction with the MOB1 adaptor protein, which connects MST to LATS2, leading to activation of YAP/TAZ by suppressing LATS2 kinase activity.
32513743	2	29	theme	Hippo	317:321	arg1	pathway					323:329	the Hippo pathway	313:329	the Hippo pathway	313:329	The LATS-mediated negative feedback loop prevents excessive activation of the effectors YAP/TAZ, maintaining homeostasis of the Hippo pathway.
32513743	6	30	theme	YAP/TAZ	831:837	arg1	regulator					818:826	a direct negative regulator	800:826	a direct negative regulator of YAP/TAZ	800:837	This study found that in breast cancer cells, abnormally increased O-GlcNAcylation hyperactivates YAP/TAZ and inhibits LATS2, a direct negative regulator of YAP/TAZ.
32513743	6	30	theme	YAP/TAZ	831:837	arg1	LATS2					793:797	LATS2	793:797	LATS2	793:797	This study found that in breast cancer cells, abnormally increased O-GlcNAcylation hyperactivates YAP/TAZ and inhibits LATS2, a direct negative regulator of YAP/TAZ.
32513743	8	31	from	LATS2	974:978	arg1	O-GlcNAcylation					955:969	O-GlcNAcylation	955:969	O-GlcNAcylation at LATS2 Thr436	955:985	Here, we found that O-GlcNAcylation at LATS2 Thr436 interrupted its interaction with the MOB1 adaptor protein, which connects MST to LATS2, leading to activation of YAP/TAZ by suppressing LATS2 kinase activity.
32513743	1	32	dep	cell	155:158	arg1	apoptosis					178:186	apoptosis	178:186	apoptosis	178:186	The Hippo pathway controls organ size and tissue homeostasis by regulating cell proliferation and apoptosis.
32513743	1	32	dep	cell	155:158	arg1	proliferation					160:172	proliferation	160:172	proliferation	160:172	The Hippo pathway controls organ size and tissue homeostasis by regulating cell proliferation and apoptosis.
32513743	0	33	theme	Hippo	38:42	arg1	pathway					44:50	the Hippo pathway	34:50	the Hippo pathway	34:50	O-GlcNAcylation on LATS2 disrupts the Hippo pathway by inhibiting its activity.
32513743	7	34	theme	identified	866:875	arg1	components					892:901	the newly identified O-GlcNAcylated components	856:901	the newly identified O-GlcNAcylated components in the MST-LATS kinase cascade	856:932	LATS2 is one of the newly identified O-GlcNAcylated components in the MST-LATS kinase cascade.
32513743	10	35	theme	LATS2	1248:1252	arg1	O-GlcNAcylation					1254:1268	LATS2 O-GlcNAcylation	1248:1268	LATS2 O-GlcNAcylation	1248:1268	Thus, this study suggests that LATS2 O-GlcNAcylation is deeply involved in tumor growth by playing a critical role in dysregulation of the Hippo pathway in cancer cells.
32513743	2	36	theme	excessive	239:247	arg1	activation					249:258	excessive activation	239:258	excessive activation of the effectors YAP/TAZ	239:283	The LATS-mediated negative feedback loop prevents excessive activation of the effectors YAP/TAZ, maintaining homeostasis of the Hippo pathway.
32513743	9	37	theme	negative	1193:1200	arg1	loop					1211:1214	the LATS-mediated negative feedback loop	1175:1214	the LATS-mediated negative feedback loop	1175:1214	LATS2 is a core component in the LATS-mediated negative feedback loop.
32513743	3	38	theme	tumor	401:405	arg1	growth					407:412	tumor growth	401:412	tumor growth	401:412	YAP and TAZ are hyperactivated in various cancer cells which lead to tumor growth.
32513743	1	39	theme	organ	107:111	arg1	size					113:116	organ size	107:116	organ size	107:116	The Hippo pathway controls organ size and tissue homeostasis by regulating cell proliferation and apoptosis.
32513743	8	40	theme	YAP/TAZ	1100:1106	arg1	activation					1086:1095	activation	1086:1095	activation of YAP/TAZ by suppressing LATS2 kinase activity	1086:1143	Here, we found that O-GlcNAcylation at LATS2 Thr436 interrupted its interaction with the MOB1 adaptor protein, which connects MST to LATS2, leading to activation of YAP/TAZ by suppressing LATS2 kinase activity.
32513743	2	41	theme	feedback	216:223	arg1	loop					225:228	The LATS-mediated negative feedback loop	189:228	The LATS-mediated negative feedback loop	189:228	The LATS-mediated negative feedback loop prevents excessive activation of the effectors YAP/TAZ, maintaining homeostasis of the Hippo pathway.
32513743	4	42	theme	increased	426:434	arg1	O-GlcNAcylation					436:450	Aberrantly increased O-GlcNAcylation	415:450	Aberrantly increased O-GlcNAcylation	415:450	Aberrantly increased O-GlcNAcylation has recently emerged as a cause of hyperactivation of YAP in cancer cells.
32513743	8	43	theme	LATS2	1123:1127	arg1	activity					1136:1143	LATS2 kinase activity	1123:1143	LATS2 kinase activity	1123:1143	Here, we found that O-GlcNAcylation at LATS2 Thr436 interrupted its interaction with the MOB1 adaptor protein, which connects MST to LATS2, leading to activation of YAP/TAZ by suppressing LATS2 kinase activity.
32513743	2	44	theme	negative	207:214	arg1	loop					225:228	The LATS-mediated negative feedback loop	189:228	The LATS-mediated negative feedback loop	189:228	The LATS-mediated negative feedback loop prevents excessive activation of the effectors YAP/TAZ, maintaining homeostasis of the Hippo pathway.
32513743	2	45	theme	YAP/TAZ	277:283	arg1	activation					249:258	excessive activation	239:258	excessive activation of the effectors YAP/TAZ	239:283	The LATS-mediated negative feedback loop prevents excessive activation of the effectors YAP/TAZ, maintaining homeostasis of the Hippo pathway.
32513743	10	46	theme	critical	1318:1325	arg1	role					1327:1330	a critical role	1316:1330	a critical role	1316:1330	Thus, this study suggests that LATS2 O-GlcNAcylation is deeply involved in tumor growth by playing a critical role in dysregulation of the Hippo pathway in cancer cells.
32513743	2	47	theme	LATS-mediated	193:205	arg1	loop					225:228	The LATS-mediated negative feedback loop	189:228	The LATS-mediated negative feedback loop	189:228	The LATS-mediated negative feedback loop prevents excessive activation of the effectors YAP/TAZ, maintaining homeostasis of the Hippo pathway.
32513743	2	48	theme	effectors	267:275	arg1	YAP/TAZ					277:283	the effectors YAP/TAZ	263:283	the effectors YAP/TAZ	263:283	The LATS-mediated negative feedback loop prevents excessive activation of the effectors YAP/TAZ, maintaining homeostasis of the Hippo pathway.
32513743	10	49	theme	pathway	1362:1368	arg1	dysregulation					1335:1347	dysregulation	1335:1347	dysregulation of the Hippo pathway in cancer cells	1335:1384	Thus, this study suggests that LATS2 O-GlcNAcylation is deeply involved in tumor growth by playing a critical role in dysregulation of the Hippo pathway in cancer cells.
32513743	1	50	theme	tissue	122:127	arg1	homeostasis					129:139	tissue homeostasis	122:139	tissue homeostasis	122:139	The Hippo pathway controls organ size and tissue homeostasis by regulating cell proliferation and apoptosis.
32513743	7	51	theme	MST-LATS	910:917	arg1	cascade					926:932	the MST-LATS kinase cascade	906:932	the MST-LATS kinase cascade	906:932	LATS2 is one of the newly identified O-GlcNAcylated components in the MST-LATS kinase cascade.
32513743	8	52	with	interaction	1003:1013	arg1	protein					1037:1043	the MOB1 adaptor protein	1020:1043	the MOB1 adaptor protein	1020:1043	Here, we found that O-GlcNAcylation at LATS2 Thr436 interrupted its interaction with the MOB1 adaptor protein, which connects MST to LATS2, leading to activation of YAP/TAZ by suppressing LATS2 kinase activity.
32513743	10	53	theme	Hippo	1356:1360	arg1	pathway					1362:1368	the Hippo pathway	1352:1368	the Hippo pathway	1352:1368	Thus, this study suggests that LATS2 O-GlcNAcylation is deeply involved in tumor growth by playing a critical role in dysregulation of the Hippo pathway in cancer cells.
32513743	6	54	theme	increased	731:739	arg1	O-GlcNAcylation					741:755	abnormally increased O-GlcNAcylation	720:755	abnormally increased O-GlcNAcylation	720:755	This study found that in breast cancer cells, abnormally increased O-GlcNAcylation hyperactivates YAP/TAZ and inhibits LATS2, a direct negative regulator of YAP/TAZ.
32513743	10	55	theme	cancer	1373:1378	arg1	cells					1380:1384	cancer cells	1373:1384	cancer cells	1373:1384	Thus, this study suggests that LATS2 O-GlcNAcylation is deeply involved in tumor growth by playing a critical role in dysregulation of the Hippo pathway in cancer cells.
32513743	7	56	theme	kinase	919:924	arg1	cascade					926:932	the MST-LATS kinase cascade	906:932	the MST-LATS kinase cascade	906:932	LATS2 is one of the newly identified O-GlcNAcylated components in the MST-LATS kinase cascade.
32513743	8	57	theme	kinase	1129:1134	arg1	activity					1136:1143	LATS2 kinase activity	1123:1143	LATS2 kinase activity	1123:1143	Here, we found that O-GlcNAcylation at LATS2 Thr436 interrupted its interaction with the MOB1 adaptor protein, which connects MST to LATS2, leading to activation of YAP/TAZ by suppressing LATS2 kinase activity.
32513743	4	58	theme	cancer	513:518	arg1	cells					520:524	cancer cells	513:524	cancer cells	513:524	Aberrantly increased O-GlcNAcylation has recently emerged as a cause of hyperactivation of YAP in cancer cells.
32513743	9	59	theme	core	1157:1160	arg1	LATS2					1146:1150	LATS2	1146:1150	LATS2	1146:1150	LATS2 is a core component in the LATS-mediated negative feedback loop.
32513743	9	59	theme	core	1157:1160	arg1	component					1162:1170	a core component	1155:1170	a core component in the LATS-mediated negative feedback loop	1155:1214	LATS2 is a core component in the LATS-mediated negative feedback loop.
29208956	4	0	from	lysine	648:653	arg1	polyubiquitination					626:643	CRL4CDT2-dependent Polη polyubiquitination	602:643	CRL4CDT2-dependent Polη polyubiquitination at lysine 462	602:657	Abrogation of this modification results in a reduced level of CRL4CDT2-dependent Polη polyubiquitination at lysine 462, a delayed p97-dependent removal of Polη from replication forks, and significantly enhanced UV-induced mutagenesis even though Polη focus formation and its efficacy to bypass across cyclobutane pyrimidine dimers after UV irradiation are not affected.
29208956	4	0	from	lysine	648:653	arg1	mutagenesis					762:772	significantly enhanced UV-induced mutagenesis	728:772	significantly enhanced UV-induced mutagenesis	728:772	Abrogation of this modification results in a reduced level of CRL4CDT2-dependent Polη polyubiquitination at lysine 462, a delayed p97-dependent removal of Polη from replication forks, and significantly enhanced UV-induced mutagenesis even though Polη focus formation and its efficacy to bypass across cyclobutane pyrimidine dimers after UV irradiation are not affected.
29208956	4	0	from	lysine	648:653	arg1	removal					684:690	a delayed p97-dependent removal	660:690	a delayed p97-dependent removal of Polη from replication forks	660:721	Abrogation of this modification results in a reduced level of CRL4CDT2-dependent Polη polyubiquitination at lysine 462, a delayed p97-dependent removal of Polη from replication forks, and significantly enhanced UV-induced mutagenesis even though Polη focus formation and its efficacy to bypass across cyclobutane pyrimidine dimers after UV irradiation are not affected.
29208956	4	0	from	lysine	648:653	arg1	level					593:597	a reduced level	583:597	a reduced level of CRL4CDT2-dependent Polη polyubiquitination at lysine 462, a delayed p97-dependent removal of Polη from replication forks, and significantly enhanced UV-induced mutagenesis	583:772	Abrogation of this modification results in a reduced level of CRL4CDT2-dependent Polη polyubiquitination at lysine 462, a delayed p97-dependent removal of Polη from replication forks, and significantly enhanced UV-induced mutagenesis even though Polη focus formation and its efficacy to bypass across cyclobutane pyrimidine dimers after UV irradiation are not affected.
29208956	3	1	theme	DNA	528:530	arg1	damage					532:537	DNA damage	528:537	DNA damage	528:537	Here, we reported that human Polη undergoes O-GlcNAcylation at threonine 457 by O-GlcNAc transferase upon DNA damage.
29208956	4	2	theme	CRL4CDT2-dependent	602:619	arg1	polyubiquitination					626:643	CRL4CDT2-dependent Polη polyubiquitination	602:643	CRL4CDT2-dependent Polη polyubiquitination at lysine 462	602:657	Abrogation of this modification results in a reduced level of CRL4CDT2-dependent Polη polyubiquitination at lysine 462, a delayed p97-dependent removal of Polη from replication forks, and significantly enhanced UV-induced mutagenesis even though Polη focus formation and its efficacy to bypass across cyclobutane pyrimidine dimers after UV irradiation are not affected.
29208956	5	3	theme	increased	1025:1033	arg1	sensitivity					1044:1054	increased cellular sensitivity	1025:1054	increased cellular sensitivity to cisplatin	1025:1067	Furthermore, the O-GlcNAc-deficient T457A mutation impairs TLS to bypass across cisplatin-induced lesions, causing increased cellular sensitivity to cisplatin.
29208956	5	4	theme	cellular	1035:1042	arg1	sensitivity					1044:1054	increased cellular sensitivity	1025:1054	increased cellular sensitivity to cisplatin	1025:1067	Furthermore, the O-GlcNAc-deficient T457A mutation impairs TLS to bypass across cisplatin-induced lesions, causing increased cellular sensitivity to cisplatin.
29208956	4	5	from	forks	717:721	arg1	polyubiquitination					626:643	CRL4CDT2-dependent Polη polyubiquitination	602:643	CRL4CDT2-dependent Polη polyubiquitination at lysine 462	602:657	Abrogation of this modification results in a reduced level of CRL4CDT2-dependent Polη polyubiquitination at lysine 462, a delayed p97-dependent removal of Polη from replication forks, and significantly enhanced UV-induced mutagenesis even though Polη focus formation and its efficacy to bypass across cyclobutane pyrimidine dimers after UV irradiation are not affected.
29208956	4	5	from	forks	717:721	arg1	mutagenesis					762:772	significantly enhanced UV-induced mutagenesis	728:772	significantly enhanced UV-induced mutagenesis	728:772	Abrogation of this modification results in a reduced level of CRL4CDT2-dependent Polη polyubiquitination at lysine 462, a delayed p97-dependent removal of Polη from replication forks, and significantly enhanced UV-induced mutagenesis even though Polη focus formation and its efficacy to bypass across cyclobutane pyrimidine dimers after UV irradiation are not affected.
29208956	4	5	from	forks	717:721	arg1	removal					684:690	a delayed p97-dependent removal	660:690	a delayed p97-dependent removal of Polη from replication forks	660:721	Abrogation of this modification results in a reduced level of CRL4CDT2-dependent Polη polyubiquitination at lysine 462, a delayed p97-dependent removal of Polη from replication forks, and significantly enhanced UV-induced mutagenesis even though Polη focus formation and its efficacy to bypass across cyclobutane pyrimidine dimers after UV irradiation are not affected.
29208956	4	5	from	forks	717:721	arg1	level					593:597	a reduced level	583:597	a reduced level of CRL4CDT2-dependent Polη polyubiquitination at lysine 462, a delayed p97-dependent removal of Polη from replication forks, and significantly enhanced UV-induced mutagenesis	583:772	Abrogation of this modification results in a reduced level of CRL4CDT2-dependent Polη polyubiquitination at lysine 462, a delayed p97-dependent removal of Polη from replication forks, and significantly enhanced UV-induced mutagenesis even though Polη focus formation and its efficacy to bypass across cyclobutane pyrimidine dimers after UV irradiation are not affected.
29208956	1	6	theme	chemoresistant	257:270	arg1	formation					282:290	chemoresistant phenotype formation	257:290	chemoresistant phenotype formation	257:290	DNA polymerase η (Polη) facilitates translesion DNA synthesis (TLS) across ultraviolet (UV) irradiation- and cisplatin-induced DNA lesions implicated in skin carcinogenesis and chemoresistant phenotype formation, respectively.
29208956	4	7	theme	Polη	786:789	arg1	formation					797:805	Polη focus formation	786:805	Polη focus formation	786:805	Abrogation of this modification results in a reduced level of CRL4CDT2-dependent Polη polyubiquitination at lysine 462, a delayed p97-dependent removal of Polη from replication forks, and significantly enhanced UV-induced mutagenesis even though Polη focus formation and its efficacy to bypass across cyclobutane pyrimidine dimers after UV irradiation are not affected.
29208956	6	8	from	role	1103:1106	arg1	regulation					1139:1148	TLS regulation	1135:1148	TLS regulation	1135:1148	Our findings demonstrate a novel role of Polη O-GlcNAcylation in TLS regulation and genome stability maintenance and establish a new rationale to improve chemotherapeutic treatment.
29208956	6	8	from	role	1103:1106	arg1	stability					1161:1169	genome stability	1154:1169	genome stability	1154:1169	Our findings demonstrate a novel role of Polη O-GlcNAcylation in TLS regulation and genome stability maintenance and establish a new rationale to improve chemotherapeutic treatment.
29208956	1	9	theme	phenotype	272:280	arg1	formation					282:290	chemoresistant phenotype formation	257:290	chemoresistant phenotype formation	257:290	DNA polymerase η (Polη) facilitates translesion DNA synthesis (TLS) across ultraviolet (UV) irradiation- and cisplatin-induced DNA lesions implicated in skin carcinogenesis and chemoresistant phenotype formation, respectively.
29208956	1	10	theme	DNA	80:82	arg1	polymerase					84:93	DNA polymerase η	80:95	DNA polymerase η (Polη)	80:102	DNA polymerase η (Polη) facilitates translesion DNA synthesis (TLS) across ultraviolet (UV) irradiation- and cisplatin-induced DNA lesions implicated in skin carcinogenesis and chemoresistant phenotype formation, respectively.
29208956	1	10	theme	DNA	80:82	arg1	Polη					98:101	Polη	98:101	Polη	98:101	DNA polymerase η (Polη) facilitates translesion DNA synthesis (TLS) across ultraviolet (UV) irradiation- and cisplatin-induced DNA lesions implicated in skin carcinogenesis and chemoresistant phenotype formation, respectively.
29208956	4	11	theme	Polη	695:698	arg1	polyubiquitination					626:643	CRL4CDT2-dependent Polη polyubiquitination	602:643	CRL4CDT2-dependent Polη polyubiquitination at lysine 462	602:657	Abrogation of this modification results in a reduced level of CRL4CDT2-dependent Polη polyubiquitination at lysine 462, a delayed p97-dependent removal of Polη from replication forks, and significantly enhanced UV-induced mutagenesis even though Polη focus formation and its efficacy to bypass across cyclobutane pyrimidine dimers after UV irradiation are not affected.
29208956	4	11	theme	Polη	695:698	arg1	mutagenesis					762:772	significantly enhanced UV-induced mutagenesis	728:772	significantly enhanced UV-induced mutagenesis	728:772	Abrogation of this modification results in a reduced level of CRL4CDT2-dependent Polη polyubiquitination at lysine 462, a delayed p97-dependent removal of Polη from replication forks, and significantly enhanced UV-induced mutagenesis even though Polη focus formation and its efficacy to bypass across cyclobutane pyrimidine dimers after UV irradiation are not affected.
29208956	4	11	theme	Polη	695:698	arg1	removal					684:690	a delayed p97-dependent removal	660:690	a delayed p97-dependent removal of Polη from replication forks	660:721	Abrogation of this modification results in a reduced level of CRL4CDT2-dependent Polη polyubiquitination at lysine 462, a delayed p97-dependent removal of Polη from replication forks, and significantly enhanced UV-induced mutagenesis even though Polη focus formation and its efficacy to bypass across cyclobutane pyrimidine dimers after UV irradiation are not affected.
29208956	4	12	theme	Polη	621:624	arg1	polyubiquitination					626:643	CRL4CDT2-dependent Polη polyubiquitination	602:643	CRL4CDT2-dependent Polη polyubiquitination at lysine 462	602:657	Abrogation of this modification results in a reduced level of CRL4CDT2-dependent Polη polyubiquitination at lysine 462, a delayed p97-dependent removal of Polη from replication forks, and significantly enhanced UV-induced mutagenesis even though Polη focus formation and its efficacy to bypass across cyclobutane pyrimidine dimers after UV irradiation are not affected.
29208956	6	13	theme	genome	1154:1159	arg1	stability					1161:1169	genome stability	1154:1169	genome stability	1154:1169	Our findings demonstrate a novel role of Polη O-GlcNAcylation in TLS regulation and genome stability maintenance and establish a new rationale to improve chemotherapeutic treatment.
29208956	4	14	from	level	593:597	arg1	lysine					648:653	lysine 462	648:657	lysine 462	648:657	Abrogation of this modification results in a reduced level of CRL4CDT2-dependent Polη polyubiquitination at lysine 462, a delayed p97-dependent removal of Polη from replication forks, and significantly enhanced UV-induced mutagenesis even though Polη focus formation and its efficacy to bypass across cyclobutane pyrimidine dimers after UV irradiation are not affected.
29208956	4	14	from	level	593:597	arg1	forks					717:721	replication forks	705:721	replication forks	705:721	Abrogation of this modification results in a reduced level of CRL4CDT2-dependent Polη polyubiquitination at lysine 462, a delayed p97-dependent removal of Polη from replication forks, and significantly enhanced UV-induced mutagenesis even though Polη focus formation and its efficacy to bypass across cyclobutane pyrimidine dimers after UV irradiation are not affected.
29208956	4	15	theme	reduced	585:591	arg1	level					593:597	a reduced level	583:597	a reduced level of CRL4CDT2-dependent Polη polyubiquitination at lysine 462, a delayed p97-dependent removal of Polη from replication forks, and significantly enhanced UV-induced mutagenesis	583:772	Abrogation of this modification results in a reduced level of CRL4CDT2-dependent Polη polyubiquitination at lysine 462, a delayed p97-dependent removal of Polη from replication forks, and significantly enhanced UV-induced mutagenesis even though Polη focus formation and its efficacy to bypass across cyclobutane pyrimidine dimers after UV irradiation are not affected.
29208956	2	16	theme	post-translational	324:341	arg1	modifications					343:355	post-translational modifications	324:355	post-translational modifications of Polη	324:363	However, whether post-translational modifications of Polη are involved in these processes remains largely unknown.
29208956	4	17	theme	replication	705:715	arg1	forks					717:721	replication forks	705:721	replication forks	705:721	Abrogation of this modification results in a reduced level of CRL4CDT2-dependent Polη polyubiquitination at lysine 462, a delayed p97-dependent removal of Polη from replication forks, and significantly enhanced UV-induced mutagenesis even though Polη focus formation and its efficacy to bypass across cyclobutane pyrimidine dimers after UV irradiation are not affected.
29208956	0	18	theme	Polη	0:3	arg1	O-GlcNAcylation					5:19	Polη O-GlcNAcylation	0:19	Polη O-GlcNAcylation	0:19	Polη O-GlcNAcylation governs genome integrity during translesion DNA synthesis.
29208956	4	19	theme	mutagenesis	762:772	arg1	level					593:597	a reduced level	583:597	a reduced level of CRL4CDT2-dependent Polη polyubiquitination at lysine 462, a delayed p97-dependent removal of Polη from replication forks, and significantly enhanced UV-induced mutagenesis	583:772	Abrogation of this modification results in a reduced level of CRL4CDT2-dependent Polη polyubiquitination at lysine 462, a delayed p97-dependent removal of Polη from replication forks, and significantly enhanced UV-induced mutagenesis even though Polη focus formation and its efficacy to bypass across cyclobutane pyrimidine dimers after UV irradiation are not affected.
29208956	5	20	dep	TLS	969:971	arg1	bypass					976:981	bypass	976:981	bypass	976:981	Furthermore, the O-GlcNAc-deficient T457A mutation impairs TLS to bypass across cisplatin-induced lesions, causing increased cellular sensitivity to cisplatin.
29208956	5	20	dep	TLS	969:971	arg1	to					973:974	to	973:974	to	973:974	Furthermore, the O-GlcNAc-deficient T457A mutation impairs TLS to bypass across cisplatin-induced lesions, causing increased cellular sensitivity to cisplatin.
29208956	3	21	theme	human	445:449	arg1	Polη					451:454	human Polη	445:454	human Polη	445:454	Here, we reported that human Polη undergoes O-GlcNAcylation at threonine 457 by O-GlcNAc transferase upon DNA damage.
29208956	0	22	theme	genome	29:34	arg1	integrity					36:44	genome integrity	29:44	genome integrity	29:44	Polη O-GlcNAcylation governs genome integrity during translesion DNA synthesis.
29208956	5	23	theme	cisplatin-induced	990:1006	arg1	lesions					1008:1014	cisplatin-induced lesions	990:1014	cisplatin-induced lesions	990:1014	Furthermore, the O-GlcNAc-deficient T457A mutation impairs TLS to bypass across cisplatin-induced lesions, causing increased cellular sensitivity to cisplatin.
29208956	6	24	theme	O-GlcNAcylation	1116:1130	arg1	role					1103:1106	a novel role	1095:1106	a novel role of Polη O-GlcNAcylation in TLS regulation and genome stability maintenance	1095:1181	Our findings demonstrate a novel role of Polη O-GlcNAcylation in TLS regulation and genome stability maintenance and establish a new rationale to improve chemotherapeutic treatment.
29208956	1	25	theme	irradiation-	172:183	arg1	lesions					211:217	ultraviolet (UV) irradiation- and cisplatin-induced DNA lesions	155:217	ultraviolet (UV) irradiation- and cisplatin-induced DNA lesions implicated in skin carcinogenesis and chemoresistant phenotype formation, respectively	155:304	DNA polymerase η (Polη) facilitates translesion DNA synthesis (TLS) across ultraviolet (UV) irradiation- and cisplatin-induced DNA lesions implicated in skin carcinogenesis and chemoresistant phenotype formation, respectively.
29208956	6	26	theme	new	1199:1201	arg1	rationale					1203:1211	a new rationale	1197:1211	a new rationale to improve chemotherapeutic treatment	1197:1249	Our findings demonstrate a novel role of Polη O-GlcNAcylation in TLS regulation and genome stability maintenance and establish a new rationale to improve chemotherapeutic treatment.
29208956	4	27	theme	focus	791:795	arg1	formation					797:805	Polη focus formation	786:805	Polη focus formation	786:805	Abrogation of this modification results in a reduced level of CRL4CDT2-dependent Polη polyubiquitination at lysine 462, a delayed p97-dependent removal of Polη from replication forks, and significantly enhanced UV-induced mutagenesis even though Polη focus formation and its efficacy to bypass across cyclobutane pyrimidine dimers after UV irradiation are not affected.
29208956	6	28	dep	regulation	1139:1148	arg1	maintenance					1171:1181	maintenance	1171:1181	maintenance	1171:1181	Our findings demonstrate a novel role of Polη O-GlcNAcylation in TLS regulation and genome stability maintenance and establish a new rationale to improve chemotherapeutic treatment.
29208956	2	29	theme	Polη	360:363	arg1	modifications					343:355	post-translational modifications	324:355	post-translational modifications of Polη	324:363	However, whether post-translational modifications of Polη are involved in these processes remains largely unknown.
29208956	4	30	theme	removal	684:690	arg1	level					593:597	a reduced level	583:597	a reduced level of CRL4CDT2-dependent Polη polyubiquitination at lysine 462, a delayed p97-dependent removal of Polη from replication forks, and significantly enhanced UV-induced mutagenesis	583:772	Abrogation of this modification results in a reduced level of CRL4CDT2-dependent Polη polyubiquitination at lysine 462, a delayed p97-dependent removal of Polη from replication forks, and significantly enhanced UV-induced mutagenesis even though Polη focus formation and its efficacy to bypass across cyclobutane pyrimidine dimers after UV irradiation are not affected.
29208956	4	31	theme	p97-dependent	670:682	arg1	removal					684:690	a delayed p97-dependent removal	660:690	a delayed p97-dependent removal of Polη from replication forks	660:721	Abrogation of this modification results in a reduced level of CRL4CDT2-dependent Polη polyubiquitination at lysine 462, a delayed p97-dependent removal of Polη from replication forks, and significantly enhanced UV-induced mutagenesis even though Polη focus formation and its efficacy to bypass across cyclobutane pyrimidine dimers after UV irradiation are not affected.
29208956	5	32	theme	O-GlcNAc-deficient	927:944	arg1	mutation					952:959	the O-GlcNAc-deficient T457A mutation	923:959	the O-GlcNAc-deficient T457A mutation	923:959	Furthermore, the O-GlcNAc-deficient T457A mutation impairs TLS to bypass across cisplatin-induced lesions, causing increased cellular sensitivity to cisplatin.
29208956	1	33	theme	cisplatin-induced	189:205	arg1	lesions					211:217	ultraviolet (UV) irradiation- and cisplatin-induced DNA lesions	155:217	ultraviolet (UV) irradiation- and cisplatin-induced DNA lesions implicated in skin carcinogenesis and chemoresistant phenotype formation, respectively	155:304	DNA polymerase η (Polη) facilitates translesion DNA synthesis (TLS) across ultraviolet (UV) irradiation- and cisplatin-induced DNA lesions implicated in skin carcinogenesis and chemoresistant phenotype formation, respectively.
29208956	4	34	theme	enhanced	742:749	arg1	mutagenesis					762:772	significantly enhanced UV-induced mutagenesis	728:772	significantly enhanced UV-induced mutagenesis	728:772	Abrogation of this modification results in a reduced level of CRL4CDT2-dependent Polη polyubiquitination at lysine 462, a delayed p97-dependent removal of Polη from replication forks, and significantly enhanced UV-induced mutagenesis even though Polη focus formation and its efficacy to bypass across cyclobutane pyrimidine dimers after UV irradiation are not affected.
29208956	1	35	theme	DNA	207:209	arg1	lesions					211:217	ultraviolet (UV) irradiation- and cisplatin-induced DNA lesions	155:217	ultraviolet (UV) irradiation- and cisplatin-induced DNA lesions implicated in skin carcinogenesis and chemoresistant phenotype formation, respectively	155:304	DNA polymerase η (Polη) facilitates translesion DNA synthesis (TLS) across ultraviolet (UV) irradiation- and cisplatin-induced DNA lesions implicated in skin carcinogenesis and chemoresistant phenotype formation, respectively.
29208956	0	36	theme	DNA	65:67	arg1	synthesis					69:77	translesion DNA synthesis	53:77	translesion DNA synthesis	53:77	Polη O-GlcNAcylation governs genome integrity during translesion DNA synthesis.
29208956	6	37	theme	Polη	1111:1114	arg1	O-GlcNAcylation					1116:1130	Polη O-GlcNAcylation	1111:1130	Polη O-GlcNAcylation	1111:1130	Our findings demonstrate a novel role of Polη O-GlcNAcylation in TLS regulation and genome stability maintenance and establish a new rationale to improve chemotherapeutic treatment.
29208956	4	38	theme	UV-induced	751:760	arg1	mutagenesis					762:772	significantly enhanced UV-induced mutagenesis	728:772	significantly enhanced UV-induced mutagenesis	728:772	Abrogation of this modification results in a reduced level of CRL4CDT2-dependent Polη polyubiquitination at lysine 462, a delayed p97-dependent removal of Polη from replication forks, and significantly enhanced UV-induced mutagenesis even though Polη focus formation and its efficacy to bypass across cyclobutane pyrimidine dimers after UV irradiation are not affected.
29208956	0	39	theme	translesion	53:63	arg1	synthesis					69:77	translesion DNA synthesis	53:77	translesion DNA synthesis	53:77	Polη O-GlcNAcylation governs genome integrity during translesion DNA synthesis.
29208956	4	40	theme	UV	877:878	arg1	irradiation					880:890	UV irradiation	877:890	UV irradiation	877:890	Abrogation of this modification results in a reduced level of CRL4CDT2-dependent Polη polyubiquitination at lysine 462, a delayed p97-dependent removal of Polη from replication forks, and significantly enhanced UV-induced mutagenesis even though Polη focus formation and its efficacy to bypass across cyclobutane pyrimidine dimers after UV irradiation are not affected.
29208956	3	41	from	threonine	485:493	arg1	O-GlcNAcylation					466:480	O-GlcNAcylation	466:480	O-GlcNAcylation at threonine 457 by O-GlcNAc transferase	466:521	Here, we reported that human Polη undergoes O-GlcNAcylation at threonine 457 by O-GlcNAc transferase upon DNA damage.
29208956	1	42	theme	translesion	116:126	arg1	TLS					143:145	TLS	143:145	TLS	143:145	DNA polymerase η (Polη) facilitates translesion DNA synthesis (TLS) across ultraviolet (UV) irradiation- and cisplatin-induced DNA lesions implicated in skin carcinogenesis and chemoresistant phenotype formation, respectively.
29208956	1	42	theme	translesion	116:126	arg1	synthesis					132:140	translesion DNA synthesis	116:140	translesion DNA synthesis (TLS)	116:146	DNA polymerase η (Polη) facilitates translesion DNA synthesis (TLS) across ultraviolet (UV) irradiation- and cisplatin-induced DNA lesions implicated in skin carcinogenesis and chemoresistant phenotype formation, respectively.
29208956	4	43	theme	modification	559:570	arg1	Abrogation					540:549	Abrogation	540:549	Abrogation of this modification	540:570	Abrogation of this modification results in a reduced level of CRL4CDT2-dependent Polη polyubiquitination at lysine 462, a delayed p97-dependent removal of Polη from replication forks, and significantly enhanced UV-induced mutagenesis even though Polη focus formation and its efficacy to bypass across cyclobutane pyrimidine dimers after UV irradiation are not affected.
29208956	1	44	theme	DNA	128:130	arg1	TLS					143:145	TLS	143:145	TLS	143:145	DNA polymerase η (Polη) facilitates translesion DNA synthesis (TLS) across ultraviolet (UV) irradiation- and cisplatin-induced DNA lesions implicated in skin carcinogenesis and chemoresistant phenotype formation, respectively.
29208956	1	44	theme	DNA	128:130	arg1	synthesis					132:140	translesion DNA synthesis	116:140	translesion DNA synthesis (TLS)	116:146	DNA polymerase η (Polη) facilitates translesion DNA synthesis (TLS) across ultraviolet (UV) irradiation- and cisplatin-induced DNA lesions implicated in skin carcinogenesis and chemoresistant phenotype formation, respectively.
29208956	6	45	theme	TLS	1135:1137	arg1	regulation					1139:1148	TLS regulation	1135:1148	TLS regulation	1135:1148	Our findings demonstrate a novel role of Polη O-GlcNAcylation in TLS regulation and genome stability maintenance and establish a new rationale to improve chemotherapeutic treatment.
29208956	3	46	theme	O-GlcNAc	502:509	arg1	transferase					511:521	O-GlcNAc transferase	502:521	O-GlcNAc transferase	502:521	Here, we reported that human Polη undergoes O-GlcNAcylation at threonine 457 by O-GlcNAc transferase upon DNA damage.
29208956	4	47	attach	removal	684:690	arg2	Polη					695:698	Polη	695:698	Polη	695:698	Abrogation of this modification results in a reduced level of CRL4CDT2-dependent Polη polyubiquitination at lysine 462, a delayed p97-dependent removal of Polη from replication forks, and significantly enhanced UV-induced mutagenesis even though Polη focus formation and its efficacy to bypass across cyclobutane pyrimidine dimers after UV irradiation are not affected.
29208956	4	47	attach	removal	684:690	arg3	lysine					648:653	lysine 462	648:657	lysine 462	648:657	Abrogation of this modification results in a reduced level of CRL4CDT2-dependent Polη polyubiquitination at lysine 462, a delayed p97-dependent removal of Polη from replication forks, and significantly enhanced UV-induced mutagenesis even though Polη focus formation and its efficacy to bypass across cyclobutane pyrimidine dimers after UV irradiation are not affected.
29208956	4	48	theme	pyrimidine	853:862	arg1	dimers					864:869	cyclobutane pyrimidine dimers	841:869	cyclobutane pyrimidine dimers	841:869	Abrogation of this modification results in a reduced level of CRL4CDT2-dependent Polη polyubiquitination at lysine 462, a delayed p97-dependent removal of Polη from replication forks, and significantly enhanced UV-induced mutagenesis even though Polη focus formation and its efficacy to bypass across cyclobutane pyrimidine dimers after UV irradiation are not affected.
29208956	4	49	theme	delayed	662:668	arg1	removal					684:690	a delayed p97-dependent removal	660:690	a delayed p97-dependent removal of Polη from replication forks	660:721	Abrogation of this modification results in a reduced level of CRL4CDT2-dependent Polη polyubiquitination at lysine 462, a delayed p97-dependent removal of Polη from replication forks, and significantly enhanced UV-induced mutagenesis even though Polη focus formation and its efficacy to bypass across cyclobutane pyrimidine dimers after UV irradiation are not affected.
29208956	5	50	theme	T457A	946:950	arg1	mutation					952:959	the O-GlcNAc-deficient T457A mutation	923:959	the O-GlcNAc-deficient T457A mutation	923:959	Furthermore, the O-GlcNAc-deficient T457A mutation impairs TLS to bypass across cisplatin-induced lesions, causing increased cellular sensitivity to cisplatin.
29208956	6	51	theme	novel	1097:1101	arg1	role					1103:1106	a novel role	1095:1106	a novel role of Polη O-GlcNAcylation in TLS regulation and genome stability maintenance	1095:1181	Our findings demonstrate a novel role of Polη O-GlcNAcylation in TLS regulation and genome stability maintenance and establish a new rationale to improve chemotherapeutic treatment.
29208956	4	52	theme	polyubiquitination	626:643	arg1	level					593:597	a reduced level	583:597	a reduced level of CRL4CDT2-dependent Polη polyubiquitination at lysine 462, a delayed p97-dependent removal of Polη from replication forks, and significantly enhanced UV-induced mutagenesis	583:772	Abrogation of this modification results in a reduced level of CRL4CDT2-dependent Polη polyubiquitination at lysine 462, a delayed p97-dependent removal of Polη from replication forks, and significantly enhanced UV-induced mutagenesis even though Polη focus formation and its efficacy to bypass across cyclobutane pyrimidine dimers after UV irradiation are not affected.
29208956	6	53	theme	chemotherapeutic	1224:1239	arg1	treatment					1241:1249	chemotherapeutic treatment	1224:1249	chemotherapeutic treatment	1224:1249	Our findings demonstrate a novel role of Polη O-GlcNAcylation in TLS regulation and genome stability maintenance and establish a new rationale to improve chemotherapeutic treatment.
29208956	4	54	theme	cyclobutane	841:851	arg1	dimers					864:869	cyclobutane pyrimidine dimers	841:869	cyclobutane pyrimidine dimers	841:869	Abrogation of this modification results in a reduced level of CRL4CDT2-dependent Polη polyubiquitination at lysine 462, a delayed p97-dependent removal of Polη from replication forks, and significantly enhanced UV-induced mutagenesis even though Polη focus formation and its efficacy to bypass across cyclobutane pyrimidine dimers after UV irradiation are not affected.
29208956	1	55	theme	skin	233:236	arg1	carcinogenesis					238:251	skin carcinogenesis	233:251	skin carcinogenesis	233:251	DNA polymerase η (Polη) facilitates translesion DNA synthesis (TLS) across ultraviolet (UV) irradiation- and cisplatin-induced DNA lesions implicated in skin carcinogenesis and chemoresistant phenotype formation, respectively.
27527864	9	0	theme	metabolic	1161:1169	arg1	condition					1178:1186	metabolic stress condition	1161:1186	metabolic stress condition	1161:1186	Taken together, these results imply that O-GlcNAcylation of ATG4B regulates autophagy activation by increasing its proteolytic activity under metabolic stress condition.
27527864	7	1	theme	activation	805:814	arg1	conditions					816:825	autophagy activation conditions	795:825	autophagy activation conditions	795:825	We also found that the O-GlcNAcylated ATG4B was increased in autophagy activation conditions, and down-regulation of OGT reduces O-GlcNAcylation of ATG4B under low glucose condition.
27527864	4	2	theme	novel	424:428	arg1	target					430:435	novel target	424:435	novel target for O-GlcNAcylation	424:455	Here, we identified that ATG4B is novel target for O-GlcNAcylation under metabolic stress condition.
27527864	9	3	theme	stress	1171:1176	arg1	condition					1178:1186	metabolic stress condition	1161:1186	metabolic stress condition	1161:1186	Taken together, these results imply that O-GlcNAcylation of ATG4B regulates autophagy activation by increasing its proteolytic activity under metabolic stress condition.
27527864	5	4	with	Treatment	491:499	arg1	PugNAc					506:511	PugNAc	506:511	PugNAc	506:511	Treatment with PugNAc, an O-GlcNAcase inhibitor increased activation of autophagy in SH-SY5Y cells.
27527864	5	4	with	Treatment	491:499	arg1	inhibitor					529:537	an O-GlcNAcase inhibitor	514:537	an O-GlcNAcase inhibitor	514:537	Treatment with PugNAc, an O-GlcNAcase inhibitor increased activation of autophagy in SH-SY5Y cells.
27527864	7	5	theme	autophagy	795:803	arg1	conditions					816:825	autophagy activation conditions	795:825	autophagy activation conditions	795:825	We also found that the O-GlcNAcylated ATG4B was increased in autophagy activation conditions, and down-regulation of OGT reduces O-GlcNAcylation of ATG4B under low glucose condition.
27527864	8	6	theme	ATG4B	958:962	arg1	activity					946:953	the proteolytic activity	930:953	the proteolytic activity of ATG4B for LC3 cleavage	930:979	Furthermore, the proteolytic activity of ATG4B for LC3 cleavage was enhanced in PugNAc-treated cells.
27527864	0	7	theme	hydroxylase	74:84	arg1	activity					86:93	its hydroxylase activity	70:93	its hydroxylase activity	70:93	O-GlcNAcylation of ATG4B positively regulates autophagy by increasing its hydroxylase activity.
27527864	8	8	theme	LC3	968:970	arg1	cleavage					972:979	LC3 cleavage	968:979	LC3 cleavage	968:979	Furthermore, the proteolytic activity of ATG4B for LC3 cleavage was enhanced in PugNAc-treated cells.
27527864	7	9	theme	low	894:896	arg1	condition					906:914	low glucose condition	894:914	low glucose condition	894:914	We also found that the O-GlcNAcylated ATG4B was increased in autophagy activation conditions, and down-regulation of OGT reduces O-GlcNAcylation of ATG4B under low glucose condition.
27527864	7	10	theme	glucose	898:904	arg1	condition					906:914	low glucose condition	894:914	low glucose condition	894:914	We also found that the O-GlcNAcylated ATG4B was increased in autophagy activation conditions, and down-regulation of OGT reduces O-GlcNAcylation of ATG4B under low glucose condition.
27527864	0	11	theme	ATG4B	19:23	arg1	O-GlcNAcylation					0:14	O-GlcNAcylation	0:14	O-GlcNAcylation of ATG4B	0:23	O-GlcNAcylation of ATG4B positively regulates autophagy by increasing its hydroxylase activity.
27527864	7	12	theme	ATG4B	882:886	arg1	O-GlcNAcylation					863:877	O-GlcNAcylation	863:877	O-GlcNAcylation of ATG4B	863:886	We also found that the O-GlcNAcylated ATG4B was increased in autophagy activation conditions, and down-regulation of OGT reduces O-GlcNAcylation of ATG4B under low glucose condition.
27527864	1	13	theme	catabolic	111:119	arg1	process					133:139	a catabolic degradation process	109:139	a catabolic degradation process	109:139	Autophagy is a catabolic degradation process and maintains cellular homeostasis.
27527864	1	13	theme	catabolic	111:119	arg1	Autophagy					96:104	Autophagy	96:104	Autophagy	96:104	Autophagy is a catabolic degradation process and maintains cellular homeostasis.
27527864	8	14	theme	PugNAc-treated	997:1010	arg1	cells					1012:1016	PugNAc-treated cells	997:1016	PugNAc-treated cells	997:1016	Furthermore, the proteolytic activity of ATG4B for LC3 cleavage was enhanced in PugNAc-treated cells.
27527864	2	15	dep	conditions	234:243	arg1	response					207:214	response	207:214	response	207:214	And autophagy is activated in response to various stress conditions.
27527864	5	16	theme	O-GlcNAcase	517:527	arg1	PugNAc					506:511	PugNAc	506:511	PugNAc	506:511	Treatment with PugNAc, an O-GlcNAcase inhibitor increased activation of autophagy in SH-SY5Y cells.
27527864	5	16	theme	O-GlcNAcase	517:527	arg1	inhibitor					529:537	an O-GlcNAcase inhibitor	514:537	an O-GlcNAcase inhibitor	514:537	Treatment with PugNAc, an O-GlcNAcase inhibitor increased activation of autophagy in SH-SY5Y cells.
27527864	6	17	theme	immunoprecipitation	641:659	arg1	assay					661:665	immunoprecipitation assay	641:665	immunoprecipitation assay	641:665	Both bimolecular fluorescence complementation and immunoprecipitation assay indicated that OGT directly interacts with ATG4B in SH-SY5Y cells.
27527864	9	18	theme	autophagy	1095:1103	arg1	activation					1105:1114	autophagy activation	1095:1114	autophagy activation	1095:1114	Taken together, these results imply that O-GlcNAcylation of ATG4B regulates autophagy activation by increasing its proteolytic activity under metabolic stress condition.
27527864	7	19	theme	O-GlcNAcylated	757:770	arg1	ATG4B					772:776	the O-GlcNAcylated ATG4B	753:776	the O-GlcNAcylated ATG4B	753:776	We also found that the O-GlcNAcylated ATG4B was increased in autophagy activation conditions, and down-regulation of OGT reduces O-GlcNAcylation of ATG4B under low glucose condition.
27527864	1	20	theme	degradation	121:131	arg1	process					133:139	a catabolic degradation process	109:139	a catabolic degradation process	109:139	Autophagy is a catabolic degradation process and maintains cellular homeostasis.
27527864	1	20	theme	degradation	121:131	arg1	Autophagy					96:104	Autophagy	96:104	Autophagy	96:104	Autophagy is a catabolic degradation process and maintains cellular homeostasis.
27527864	7	21	theme	OGT	851:853	arg1	down-regulation					832:846	down-regulation	832:846	down-regulation of OGT	832:853	We also found that the O-GlcNAcylated ATG4B was increased in autophagy activation conditions, and down-regulation of OGT reduces O-GlcNAcylation of ATG4B under low glucose condition.
27527864	2	22	theme	stress	227:232	arg1	conditions					234:243	various stress conditions	219:243	various stress conditions	219:243	And autophagy is activated in response to various stress conditions.
27527864	2	23	theme	various	219:225	arg1	conditions					234:243	various stress conditions	219:243	various stress conditions	219:243	And autophagy is activated in response to various stress conditions.
27527864	5	24	from	activation	549:558	arg1	cells					584:588	SH-SY5Y cells	576:588	SH-SY5Y cells	576:588	Treatment with PugNAc, an O-GlcNAcase inhibitor increased activation of autophagy in SH-SY5Y cells.
27527864	4	25	theme	stress	473:478	arg1	condition					480:488	metabolic stress condition	463:488	metabolic stress condition	463:488	Here, we identified that ATG4B is novel target for O-GlcNAcylation under metabolic stress condition.
27527864	5	26	theme	autophagy	563:571	arg1	activation					549:558	activation	549:558	activation of autophagy in SH-SY5Y cells	549:588	Treatment with PugNAc, an O-GlcNAcase inhibitor increased activation of autophagy in SH-SY5Y cells.
27527864	9	27	theme	proteolytic	1134:1144	arg1	activity					1146:1153	its proteolytic activity	1130:1153	its proteolytic activity	1130:1153	Taken together, these results imply that O-GlcNAcylation of ATG4B regulates autophagy activation by increasing its proteolytic activity under metabolic stress condition.
27527864	6	28	theme	fluorescence	608:619	arg1	complementation					621:635	bimolecular fluorescence complementation	596:635	bimolecular fluorescence complementation	596:635	Both bimolecular fluorescence complementation and immunoprecipitation assay indicated that OGT directly interacts with ATG4B in SH-SY5Y cells.
27527864	4	29	theme	metabolic	463:471	arg1	condition					480:488	metabolic stress condition	463:488	metabolic stress condition	463:488	Here, we identified that ATG4B is novel target for O-GlcNAcylation under metabolic stress condition.
27527864	1	30	theme	cellular	155:162	arg1	homeostasis					164:174	cellular homeostasis	155:174	cellular homeostasis	155:174	Autophagy is a catabolic degradation process and maintains cellular homeostasis.
27527864	6	31	theme	SH-SY5Y	719:725	arg1	cells					727:731	SH-SY5Y cells	719:731	SH-SY5Y cells	719:731	Both bimolecular fluorescence complementation and immunoprecipitation assay indicated that OGT directly interacts with ATG4B in SH-SY5Y cells.
27527864	6	32	theme	bimolecular	596:606	arg1	complementation					621:635	bimolecular fluorescence complementation	596:635	bimolecular fluorescence complementation	596:635	Both bimolecular fluorescence complementation and immunoprecipitation assay indicated that OGT directly interacts with ATG4B in SH-SY5Y cells.
27527864	9	33	theme	ATG4B	1079:1083	arg1	O-GlcNAcylation					1060:1074	O-GlcNAcylation	1060:1074	O-GlcNAcylation of ATG4B	1060:1083	Taken together, these results imply that O-GlcNAcylation of ATG4B regulates autophagy activation by increasing its proteolytic activity under metabolic stress condition.
27527864	5	34	theme	SH-SY5Y	576:582	arg1	cells					584:588	SH-SY5Y cells	576:588	SH-SY5Y cells	576:588	Treatment with PugNAc, an O-GlcNAcase inhibitor increased activation of autophagy in SH-SY5Y cells.
27527864	8	35	theme	proteolytic	934:944	arg1	activity					946:953	the proteolytic activity	930:953	the proteolytic activity of ATG4B for LC3 cleavage	930:979	Furthermore, the proteolytic activity of ATG4B for LC3 cleavage was enhanced in PugNAc-treated cells.
34551297	8	0	theme	malignancy	1193:1202	arg1	progression					1204:1214	malignancy progression	1193:1214	malignancy progression	1193:1214	Overall, our work uncovers O-GlcNAcylation and UBE3C as critical determinants of DOT1L protein abundance, revealing a mechanism by which glucose metabolism affects malignancy progression through histone methylation.
34551297	5	1	theme	ubiquitin	659:667	arg1	ligase					669:674	a DOT1L E3 ubiquitin ligase	648:674	a DOT1L E3 ubiquitin ligase promoting DOT1L degradation whose interaction with DOT1L is susceptible to O-GlcNAcylation	648:765	We identify UBE3C as a DOT1L E3 ubiquitin ligase promoting DOT1L degradation whose interaction with DOT1L is susceptible to O-GlcNAcylation.
34551297	5	1	theme	ubiquitin	659:667	arg1	UBE3C					639:643	UBE3C	639:643	UBE3C	639:643	We identify UBE3C as a DOT1L E3 ubiquitin ligase promoting DOT1L degradation whose interaction with DOT1L is susceptible to O-GlcNAcylation.
34551297	1	2	theme	environment	172:182	arg1	interface					141:149	the interface	137:149	the interface of the extracellular environment and intracellular gene expression	137:216	Histone lysine methylation functions at the interface of the extracellular environment and intracellular gene expression.
34551297	8	3	theme	abundance	1124:1132	arg1	UBE3C					1076:1080	UBE3C	1076:1080	UBE3C	1076:1080	Overall, our work uncovers O-GlcNAcylation and UBE3C as critical determinants of DOT1L protein abundance, revealing a mechanism by which glucose metabolism affects malignancy progression through histone methylation.
34551297	8	3	theme	abundance	1124:1132	arg1	determinants					1094:1105	critical determinants	1085:1105	critical determinants of DOT1L protein abundance	1085:1132	Overall, our work uncovers O-GlcNAcylation and UBE3C as critical determinants of DOT1L protein abundance, revealing a mechanism by which glucose metabolism affects malignancy progression through histone methylation.
34551297	8	3	theme	abundance	1124:1132	arg1	O-GlcNAcylation					1056:1070	O-GlcNAcylation	1056:1070	O-GlcNAcylation	1056:1070	Overall, our work uncovers O-GlcNAcylation and UBE3C as critical determinants of DOT1L protein abundance, revealing a mechanism by which glucose metabolism affects malignancy progression through histone methylation.
34551297	7	4	theme	DOT1L	1012:1016	arg1	inhibitor					1018:1026	DOT1L inhibitor	1012:1026	DOT1L inhibitor	1012:1026	Inhibiting HBP or O-GlcNAc transferase (OGT) increases cellular sensitivity to DOT1L inhibitor.
34551297	2	5	theme	extracellular	366:378	arg1	stimuli					380:386	extracellular stimuli	366:386	extracellular stimuli	366:386	DOT1L is a versatile histone H3K79 methyltransferase with a prominent role in MLL-fusion leukemia, yet little is known about how DOT1L responds to extracellular stimuli.
34551297	6	6	theme	genes	853:857	arg1	expression					817:826	expression	817:826	expression	817:826	Consequently, HBP enhances H3K79 methylation and expression of critical DOT1L target genes such as HOXA9/MEIS1, promoting cell proliferation in MLL-fusion leukemia.
34551297	6	6	theme	genes	853:857	arg1	methylation					801:811	H3K79 methylation	795:811	H3K79 methylation	795:811	Consequently, HBP enhances H3K79 methylation and expression of critical DOT1L target genes such as HOXA9/MEIS1, promoting cell proliferation in MLL-fusion leukemia.
34551297	3	7	theme	DOT1L	410:414	arg1	stability					424:432	DOT1L protein stability	410:432	DOT1L protein stability	410:432	Here, we report that DOT1L protein stability is regulated by the extracellular glucose level through the hexosamine biosynthetic pathway (HBP).
34551297	8	8	theme	protein	1116:1122	arg1	abundance					1124:1132	DOT1L protein abundance	1110:1132	DOT1L protein abundance	1110:1132	Overall, our work uncovers O-GlcNAcylation and UBE3C as critical determinants of DOT1L protein abundance, revealing a mechanism by which glucose metabolism affects malignancy progression through histone methylation.
34551297	5	9	theme	DOT1L	686:690	arg1	degradation					692:702	DOT1L degradation	686:702	DOT1L degradation whose interaction with DOT1L is susceptible to O-GlcNAcylation	686:765	We identify UBE3C as a DOT1L E3 ubiquitin ligase promoting DOT1L degradation whose interaction with DOT1L is susceptible to O-GlcNAcylation.
34551297	6	10	theme	target	846:851	arg1	genes					853:857	critical DOT1L target genes	831:857	critical DOT1L target genes such as HOXA9/MEIS1	831:877	Consequently, HBP enhances H3K79 methylation and expression of critical DOT1L target genes such as HOXA9/MEIS1, promoting cell proliferation in MLL-fusion leukemia.
34551297	6	10	theme	target	846:851	arg1	HOXA9/MEIS1					867:877	HOXA9/MEIS1	867:877	HOXA9/MEIS1	867:877	Consequently, HBP enhances H3K79 methylation and expression of critical DOT1L target genes such as HOXA9/MEIS1, promoting cell proliferation in MLL-fusion leukemia.
34551297	4	11	theme	C	615:615	arg1	terminus					617:624	its C terminus	611:624	its C terminus	611:624	Mechanistically, DOT1L is O-GlcNAcylated at evolutionarily conserved S1511 in its C terminus.
34551297	8	12	theme	DOT1L	1110:1114	arg1	abundance					1124:1132	DOT1L protein abundance	1110:1132	DOT1L protein abundance	1110:1132	Overall, our work uncovers O-GlcNAcylation and UBE3C as critical determinants of DOT1L protein abundance, revealing a mechanism by which glucose metabolism affects malignancy progression through histone methylation.
34551297	6	13	theme	DOT1L	840:844	arg1	genes					853:857	critical DOT1L target genes	831:857	critical DOT1L target genes such as HOXA9/MEIS1	831:877	Consequently, HBP enhances H3K79 methylation and expression of critical DOT1L target genes such as HOXA9/MEIS1, promoting cell proliferation in MLL-fusion leukemia.
34551297	6	13	theme	DOT1L	840:844	arg1	HOXA9/MEIS1					867:877	HOXA9/MEIS1	867:877	HOXA9/MEIS1	867:877	Consequently, HBP enhances H3K79 methylation and expression of critical DOT1L target genes such as HOXA9/MEIS1, promoting cell proliferation in MLL-fusion leukemia.
34551297	1	14	theme	intracellular	188:200	arg1	expression					207:216	intracellular gene expression	188:216	intracellular gene expression	188:216	Histone lysine methylation functions at the interface of the extracellular environment and intracellular gene expression.
34551297	8	15	theme	critical	1085:1092	arg1	UBE3C					1076:1080	UBE3C	1076:1080	UBE3C	1076:1080	Overall, our work uncovers O-GlcNAcylation and UBE3C as critical determinants of DOT1L protein abundance, revealing a mechanism by which glucose metabolism affects malignancy progression through histone methylation.
34551297	8	15	theme	critical	1085:1092	arg1	determinants					1094:1105	critical determinants	1085:1105	critical determinants of DOT1L protein abundance	1085:1132	Overall, our work uncovers O-GlcNAcylation and UBE3C as critical determinants of DOT1L protein abundance, revealing a mechanism by which glucose metabolism affects malignancy progression through histone methylation.
34551297	8	15	theme	critical	1085:1092	arg1	O-GlcNAcylation					1056:1070	O-GlcNAcylation	1056:1070	O-GlcNAcylation	1056:1070	Overall, our work uncovers O-GlcNAcylation and UBE3C as critical determinants of DOT1L protein abundance, revealing a mechanism by which glucose metabolism affects malignancy progression through histone methylation.
34551297	6	16	theme	critical	831:838	arg1	genes					853:857	critical DOT1L target genes	831:857	critical DOT1L target genes such as HOXA9/MEIS1	831:877	Consequently, HBP enhances H3K79 methylation and expression of critical DOT1L target genes such as HOXA9/MEIS1, promoting cell proliferation in MLL-fusion leukemia.
34551297	6	16	theme	critical	831:838	arg1	HOXA9/MEIS1					867:877	HOXA9/MEIS1	867:877	HOXA9/MEIS1	867:877	Consequently, HBP enhances H3K79 methylation and expression of critical DOT1L target genes such as HOXA9/MEIS1, promoting cell proliferation in MLL-fusion leukemia.
34551297	2	17	theme	MLL-fusion	297:306	arg1	leukemia					308:315	MLL-fusion leukemia	297:315	MLL-fusion leukemia	297:315	DOT1L is a versatile histone H3K79 methyltransferase with a prominent role in MLL-fusion leukemia, yet little is known about how DOT1L responds to extracellular stimuli.
34551297	1	18	theme	gene	202:205	arg1	expression					207:216	intracellular gene expression	188:216	intracellular gene expression	188:216	Histone lysine methylation functions at the interface of the extracellular environment and intracellular gene expression.
34551297	4	19	from	S1511	602:606	arg1	O-GlcNAcylated					559:572	O-GlcNAcylated	559:572	O-GlcNAcylated	559:572	Mechanistically, DOT1L is O-GlcNAcylated at evolutionarily conserved S1511 in its C terminus.
34551297	4	19	from	S1511	602:606	arg1	terminus					617:624	its C terminus	611:624	its C terminus	611:624	Mechanistically, DOT1L is O-GlcNAcylated at evolutionarily conserved S1511 in its C terminus.
34551297	4	20	theme	conserved	592:600	arg1	S1511					602:606	evolutionarily conserved S1511	577:606	evolutionarily conserved S1511 in its C terminus	577:624	Mechanistically, DOT1L is O-GlcNAcylated at evolutionarily conserved S1511 in its C terminus.
34551297	5	21	theme	DOT1L	650:654	arg1	ligase					669:674	a DOT1L E3 ubiquitin ligase	648:674	a DOT1L E3 ubiquitin ligase promoting DOT1L degradation whose interaction with DOT1L is susceptible to O-GlcNAcylation	648:765	We identify UBE3C as a DOT1L E3 ubiquitin ligase promoting DOT1L degradation whose interaction with DOT1L is susceptible to O-GlcNAcylation.
34551297	5	21	theme	DOT1L	650:654	arg1	UBE3C					639:643	UBE3C	639:643	UBE3C	639:643	We identify UBE3C as a DOT1L E3 ubiquitin ligase promoting DOT1L degradation whose interaction with DOT1L is susceptible to O-GlcNAcylation.
34551297	7	22	theme	cellular	988:995	arg1	sensitivity					997:1007	cellular sensitivity	988:1007	cellular sensitivity to DOT1L inhibitor	988:1026	Inhibiting HBP or O-GlcNAc transferase (OGT) increases cellular sensitivity to DOT1L inhibitor.
34551297	1	23	theme	Histone	97:103	arg1	methylation					112:122	Histone lysine methylation	97:122	Histone lysine methylation	97:122	Histone lysine methylation functions at the interface of the extracellular environment and intracellular gene expression.
34551297	1	24	theme	expression	207:216	arg1	interface					141:149	the interface	137:149	the interface of the extracellular environment and intracellular gene expression	137:216	Histone lysine methylation functions at the interface of the extracellular environment and intracellular gene expression.
34551297	0	25	theme	DOT1L	0:4	arg1	O-GlcNAcylation					6:20	DOT1L O-GlcNAcylation	0:20	DOT1L O-GlcNAcylation	0:20	DOT1L O-GlcNAcylation promotes its protein stability and MLL-fusion leukemia cell proliferation.
34551297	5	26	theme	E3	656:657	arg1	ligase					669:674	a DOT1L E3 ubiquitin ligase	648:674	a DOT1L E3 ubiquitin ligase promoting DOT1L degradation whose interaction with DOT1L is susceptible to O-GlcNAcylation	648:765	We identify UBE3C as a DOT1L E3 ubiquitin ligase promoting DOT1L degradation whose interaction with DOT1L is susceptible to O-GlcNAcylation.
34551297	5	26	theme	E3	656:657	arg1	UBE3C					639:643	UBE3C	639:643	UBE3C	639:643	We identify UBE3C as a DOT1L E3 ubiquitin ligase promoting DOT1L degradation whose interaction with DOT1L is susceptible to O-GlcNAcylation.
34551297	1	27	theme	lysine	105:110	arg1	methylation					112:122	Histone lysine methylation	97:122	Histone lysine methylation	97:122	Histone lysine methylation functions at the interface of the extracellular environment and intracellular gene expression.
34551297	5	28	with	interaction	710:720	arg1	DOT1L					727:731	DOT1L	727:731	DOT1L	727:731	We identify UBE3C as a DOT1L E3 ubiquitin ligase promoting DOT1L degradation whose interaction with DOT1L is susceptible to O-GlcNAcylation.
34551297	6	29	theme	MLL-fusion	912:921	arg1	leukemia					923:930	MLL-fusion leukemia	912:930	MLL-fusion leukemia	912:930	Consequently, HBP enhances H3K79 methylation and expression of critical DOT1L target genes such as HOXA9/MEIS1, promoting cell proliferation in MLL-fusion leukemia.
34551297	2	30	with	methyltransferase	254:270	arg1	role					289:292	a prominent role	277:292	a prominent role in MLL-fusion leukemia	277:315	DOT1L is a versatile histone H3K79 methyltransferase with a prominent role in MLL-fusion leukemia, yet little is known about how DOT1L responds to extracellular stimuli.
34551297	2	31	from	role	289:292	arg1	leukemia					308:315	MLL-fusion leukemia	297:315	MLL-fusion leukemia	297:315	DOT1L is a versatile histone H3K79 methyltransferase with a prominent role in MLL-fusion leukemia, yet little is known about how DOT1L responds to extracellular stimuli.
34551297	3	32	theme	glucose	468:474	arg1	level					476:480	the extracellular glucose level	450:480	the extracellular glucose level	450:480	Here, we report that DOT1L protein stability is regulated by the extracellular glucose level through the hexosamine biosynthetic pathway (HBP).
34551297	0	33	theme	protein	35:41	arg1	stability					43:51	its protein stability	31:51	its protein stability	31:51	DOT1L O-GlcNAcylation promotes its protein stability and MLL-fusion leukemia cell proliferation.
34551297	7	34	theme	O-GlcNAc	951:958	arg1	OGT					973:975	OGT	973:975	OGT	973:975	Inhibiting HBP or O-GlcNAc transferase (OGT) increases cellular sensitivity to DOT1L inhibitor.
34551297	7	34	theme	O-GlcNAc	951:958	arg1	transferase					960:970	O-GlcNAc transferase	951:970	O-GlcNAc transferase (OGT)	951:976	Inhibiting HBP or O-GlcNAc transferase (OGT) increases cellular sensitivity to DOT1L inhibitor.
34551297	0	35	theme	MLL-fusion	57:66	arg1	proliferation					82:94	MLL-fusion leukemia cell proliferation	57:94	MLL-fusion leukemia cell proliferation	57:94	DOT1L O-GlcNAcylation promotes its protein stability and MLL-fusion leukemia cell proliferation.
34551297	6	36	theme	cell	890:893	arg1	proliferation					895:907	cell proliferation	890:907	cell proliferation	890:907	Consequently, HBP enhances H3K79 methylation and expression of critical DOT1L target genes such as HOXA9/MEIS1, promoting cell proliferation in MLL-fusion leukemia.
34551297	2	37	theme	H3K79	248:252	arg1	methyltransferase					254:270	a versatile histone H3K79 methyltransferase	228:270	a versatile histone H3K79 methyltransferase with a prominent role in MLL-fusion leukemia	228:315	DOT1L is a versatile histone H3K79 methyltransferase with a prominent role in MLL-fusion leukemia, yet little is known about how DOT1L responds to extracellular stimuli.
34551297	2	37	theme	H3K79	248:252	arg1	DOT1L					219:223	DOT1L	219:223	DOT1L	219:223	DOT1L is a versatile histone H3K79 methyltransferase with a prominent role in MLL-fusion leukemia, yet little is known about how DOT1L responds to extracellular stimuli.
34551297	6	38	theme	H3K79	795:799	arg1	methylation					801:811	H3K79 methylation	795:811	H3K79 methylation	795:811	Consequently, HBP enhances H3K79 methylation and expression of critical DOT1L target genes such as HOXA9/MEIS1, promoting cell proliferation in MLL-fusion leukemia.
34551297	3	39	theme	protein	416:422	arg1	stability					424:432	DOT1L protein stability	410:432	DOT1L protein stability	410:432	Here, we report that DOT1L protein stability is regulated by the extracellular glucose level through the hexosamine biosynthetic pathway (HBP).
34551297	2	40	theme	versatile	230:238	arg1	methyltransferase					254:270	a versatile histone H3K79 methyltransferase	228:270	a versatile histone H3K79 methyltransferase with a prominent role in MLL-fusion leukemia	228:315	DOT1L is a versatile histone H3K79 methyltransferase with a prominent role in MLL-fusion leukemia, yet little is known about how DOT1L responds to extracellular stimuli.
34551297	2	40	theme	versatile	230:238	arg1	DOT1L					219:223	DOT1L	219:223	DOT1L	219:223	DOT1L is a versatile histone H3K79 methyltransferase with a prominent role in MLL-fusion leukemia, yet little is known about how DOT1L responds to extracellular stimuli.
34551297	2	41	theme	histone	240:246	arg1	methyltransferase					254:270	a versatile histone H3K79 methyltransferase	228:270	a versatile histone H3K79 methyltransferase with a prominent role in MLL-fusion leukemia	228:315	DOT1L is a versatile histone H3K79 methyltransferase with a prominent role in MLL-fusion leukemia, yet little is known about how DOT1L responds to extracellular stimuli.
34551297	2	41	theme	histone	240:246	arg1	DOT1L					219:223	DOT1L	219:223	DOT1L	219:223	DOT1L is a versatile histone H3K79 methyltransferase with a prominent role in MLL-fusion leukemia, yet little is known about how DOT1L responds to extracellular stimuli.
34551297	3	42	theme	hexosamine	494:503	arg1	pathway					518:524	the hexosamine biosynthetic pathway	490:524	the hexosamine biosynthetic pathway (HBP)	490:530	Here, we report that DOT1L protein stability is regulated by the extracellular glucose level through the hexosamine biosynthetic pathway (HBP).
34551297	3	42	theme	hexosamine	494:503	arg1	HBP					527:529	HBP	527:529	HBP	527:529	Here, we report that DOT1L protein stability is regulated by the extracellular glucose level through the hexosamine biosynthetic pathway (HBP).
34551297	8	43	theme	glucose	1166:1172	arg1	metabolism					1174:1183	glucose metabolism	1166:1183	glucose metabolism	1166:1183	Overall, our work uncovers O-GlcNAcylation and UBE3C as critical determinants of DOT1L protein abundance, revealing a mechanism by which glucose metabolism affects malignancy progression through histone methylation.
34551297	3	44	theme	biosynthetic	505:516	arg1	pathway					518:524	the hexosamine biosynthetic pathway	490:524	the hexosamine biosynthetic pathway (HBP)	490:530	Here, we report that DOT1L protein stability is regulated by the extracellular glucose level through the hexosamine biosynthetic pathway (HBP).
34551297	3	44	theme	biosynthetic	505:516	arg1	HBP					527:529	HBP	527:529	HBP	527:529	Here, we report that DOT1L protein stability is regulated by the extracellular glucose level through the hexosamine biosynthetic pathway (HBP).
34551297	0	45	theme	cell	77:80	arg1	proliferation					82:94	MLL-fusion leukemia cell proliferation	57:94	MLL-fusion leukemia cell proliferation	57:94	DOT1L O-GlcNAcylation promotes its protein stability and MLL-fusion leukemia cell proliferation.
34551297	2	46	theme	prominent	279:287	arg1	role					289:292	a prominent role	277:292	a prominent role in MLL-fusion leukemia	277:315	DOT1L is a versatile histone H3K79 methyltransferase with a prominent role in MLL-fusion leukemia, yet little is known about how DOT1L responds to extracellular stimuli.
34551297	3	47	theme	extracellular	454:466	arg1	level					476:480	the extracellular glucose level	450:480	the extracellular glucose level	450:480	Here, we report that DOT1L protein stability is regulated by the extracellular glucose level through the hexosamine biosynthetic pathway (HBP).
34551297	0	48	theme	leukemia	68:75	arg1	proliferation					82:94	MLL-fusion leukemia cell proliferation	57:94	MLL-fusion leukemia cell proliferation	57:94	DOT1L O-GlcNAcylation promotes its protein stability and MLL-fusion leukemia cell proliferation.
34551297	1	49	theme	extracellular	158:170	arg1	environment					172:182	the extracellular environment	154:182	the extracellular environment	154:182	Histone lysine methylation functions at the interface of the extracellular environment and intracellular gene expression.
34551297	8	50	theme	histone	1224:1230	arg1	methylation					1232:1242	histone methylation	1224:1242	histone methylation	1224:1242	Overall, our work uncovers O-GlcNAcylation and UBE3C as critical determinants of DOT1L protein abundance, revealing a mechanism by which glucose metabolism affects malignancy progression through histone methylation.
22503002	3	0	link	O-linked	445:452	arg1	β-N-acetylglucosamine					454:474	O-linked β-N-acetylglucosamine	445:474	O-linked β-N-acetylglucosamine (O-GlcNAc)	445:485	Here we examined the relationship between O-GlcNAcylation, which is a glucose level-dependent post-translational modification that adds O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins, and Aβ production in a mouse model of AD carrying 5XFAD genes.
22503002	3	0	link	O-linked	445:452	arg1	O-GlcNAc					477:484	O-GlcNAc	477:484	O-GlcNAc	477:484	Here we examined the relationship between O-GlcNAcylation, which is a glucose level-dependent post-translational modification that adds O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins, and Aβ production in a mouse model of AD carrying 5XFAD genes.
22503002	1	1	theme	glucose	165:171	arg1	characteristics					197:211	two main characteristics	188:211	two main characteristics of Alzheimer's disease (AD)	188:239	Deposition of β-amyloid (Aβ) as senile plaques and disrupted glucose metabolism are two main characteristics of Alzheimer's disease (AD).
22503002	1	1	theme	glucose	165:171	arg1	Deposition					104:113	Deposition	104:113	Deposition of β-amyloid (Aβ) as senile plaques	104:149	Deposition of β-amyloid (Aβ) as senile plaques and disrupted glucose metabolism are two main characteristics of Alzheimer's disease (AD).
22503002	1	1	theme	glucose	165:171	arg1	metabolism					173:182	disrupted glucose metabolism	155:182	disrupted glucose metabolism	155:182	Deposition of β-amyloid (Aβ) as senile plaques and disrupted glucose metabolism are two main characteristics of Alzheimer's disease (AD).
22503002	2	2	from	AD	305:306	arg1	related					294:300	related	294:300	related	294:300	It is unknown, however, how these two processes are related in AD.
22503002	3	3	theme	Aβ	504:505	arg1	production					507:516	Aβ production	504:516	Aβ production	504:516	Here we examined the relationship between O-GlcNAcylation, which is a glucose level-dependent post-translational modification that adds O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins, and Aβ production in a mouse model of AD carrying 5XFAD genes.
22503002	3	3	theme	Aβ	504:505	arg1	modification					422:433	a glucose level-dependent post-translational modification	377:433	a glucose level-dependent post-translational modification that adds O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins	377:497	Here we examined the relationship between O-GlcNAcylation, which is a glucose level-dependent post-translational modification that adds O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins, and Aβ production in a mouse model of AD carrying 5XFAD genes.
22503002	3	3	theme	Aβ	504:505	arg1	O-GlcNAcylation					351:365	O-GlcNAcylation	351:365	O-GlcNAcylation	351:365	Here we examined the relationship between O-GlcNAcylation, which is a glucose level-dependent post-translational modification that adds O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins, and Aβ production in a mouse model of AD carrying 5XFAD genes.
22503002	2	4	from	related	294:300	arg1	AD					305:306	AD	305:306	AD	305:306	It is unknown, however, how these two processes are related in AD.
22503002	6	5	theme	impairment	969:978	arg1	accumulation					919:930	the accumulation	915:930	the accumulation of Aβ, neuroinflammation, and memory impairment in the 5XFAD mice	915:996	Moreover, NButGT attenuated the accumulation of Aβ, neuroinflammation, and memory impairment in the 5XFAD mice.
22503002	6	6	theme	memory	962:967	arg1	impairment					969:978	memory impairment	962:978	memory impairment	962:978	Moreover, NButGT attenuated the accumulation of Aβ, neuroinflammation, and memory impairment in the 5XFAD mice.
22503002	4	7	theme	Aβ	695:696	arg1	production					698:707	Aβ production	695:707	Aβ production	695:707	We found that 1,2-dideoxy-2'-propyl-α-d-glucopyranoso-[2,1-D]-Δ2'-thiazoline (NButGT), a specific inhibitor of O-GlcNAcase, reduces Aβ production by lowering γ-secretase activity both in vitro and in vivo.
22503002	5	8	theme	nicastrin	839:847	arg1	residue					828:834	the S708 residue	819:834	the S708 residue	819:834	We also found that O-GlcNAcylation takes place at the S708 residue of nicastrin, which is a component of γ-secretase.
22503002	5	8	theme	nicastrin	839:847	arg1	component					861:869	a component	859:869	a component of γ-secretase	859:884	We also found that O-GlcNAcylation takes place at the S708 residue of nicastrin, which is a component of γ-secretase.
22503002	5	8	theme	nicastrin	839:847	arg1	nicastrin					839:847	nicastrin	839:847	nicastrin	839:847	We also found that O-GlcNAcylation takes place at the S708 residue of nicastrin, which is a component of γ-secretase.
22503002	7	9	theme	Aβ	1056:1057	arg1	generation					1059:1068	Aβ generation	1056:1068	Aβ generation	1056:1068	This is the first study to show the relationship between Aβ generation and O-GlcNAcylation in vivo.
22503002	0	10	link	O-linked	0:7	arg1	inhibitor					35:43	O-linked β-N-acetylglucosaminidase inhibitor	0:43	O-linked β-N-acetylglucosaminidase inhibitor	0:43	O-linked β-N-acetylglucosaminidase inhibitor attenuates β-amyloid plaque and rescues memory impairment.
22503002	1	11	theme	main	192:195	arg1	characteristics					197:211	two main characteristics	188:211	two main characteristics of Alzheimer's disease (AD)	188:239	Deposition of β-amyloid (Aβ) as senile plaques and disrupted glucose metabolism are two main characteristics of Alzheimer's disease (AD).
22503002	1	11	theme	main	192:195	arg1	Deposition					104:113	Deposition	104:113	Deposition of β-amyloid (Aβ) as senile plaques	104:149	Deposition of β-amyloid (Aβ) as senile plaques and disrupted glucose metabolism are two main characteristics of Alzheimer's disease (AD).
22503002	1	11	theme	main	192:195	arg1	metabolism					173:182	disrupted glucose metabolism	155:182	disrupted glucose metabolism	155:182	Deposition of β-amyloid (Aβ) as senile plaques and disrupted glucose metabolism are two main characteristics of Alzheimer's disease (AD).
22503002	4	12	theme	specific	652:659	arg1	inhibitor					661:669	a specific inhibitor	650:669	a specific inhibitor of O-GlcNAcase	650:684	We found that 1,2-dideoxy-2'-propyl-α-d-glucopyranoso-[2,1-D]-Δ2'-thiazoline (NButGT), a specific inhibitor of O-GlcNAcase, reduces Aβ production by lowering γ-secretase activity both in vitro and in vivo.
22503002	4	12	theme	specific	652:659	arg1	-Δ2'-thiazoline					624:638	1,2-dideoxy-2'-propyl-α-d-glucopyranoso-[2,1-D]-Δ2'-thiazoline	577:638	1,2-dideoxy-2'-propyl-α-d-glucopyranoso-[2,1-D]-Δ2'-thiazoline (NButGT)	577:647	We found that 1,2-dideoxy-2'-propyl-α-d-glucopyranoso-[2,1-D]-Δ2'-thiazoline (NButGT), a specific inhibitor of O-GlcNAcase, reduces Aβ production by lowering γ-secretase activity both in vitro and in vivo.
22503002	3	13	theme	mouse	523:527	arg1	model					529:533	a mouse model	521:533	a mouse model of AD carrying 5XFAD genes	521:560	Here we examined the relationship between O-GlcNAcylation, which is a glucose level-dependent post-translational modification that adds O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins, and Aβ production in a mouse model of AD carrying 5XFAD genes.
22503002	8	14	theme	AD	1200:1201	arg1	treatment					1187:1195	the treatment	1183:1195	the treatment of AD	1183:1201	These results suggest that O-GlcNAcylation may be a suitable therapeutic target for the treatment of AD.
22503002	0	15	theme	β-N-acetylglucosaminidase	9:33	arg1	inhibitor					35:43	O-linked β-N-acetylglucosaminidase inhibitor	0:43	O-linked β-N-acetylglucosaminidase inhibitor	0:43	O-linked β-N-acetylglucosaminidase inhibitor attenuates β-amyloid plaque and rescues memory impairment.
22503002	3	16	theme	5XFAD	550:554	arg1	genes					556:560	5XFAD genes	550:560	5XFAD genes	550:560	Here we examined the relationship between O-GlcNAcylation, which is a glucose level-dependent post-translational modification that adds O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins, and Aβ production in a mouse model of AD carrying 5XFAD genes.
22503002	3	17	theme	post-translational	403:420	arg1	production					507:516	Aβ production	504:516	Aβ production	504:516	Here we examined the relationship between O-GlcNAcylation, which is a glucose level-dependent post-translational modification that adds O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins, and Aβ production in a mouse model of AD carrying 5XFAD genes.
22503002	3	17	theme	post-translational	403:420	arg1	modification					422:433	a glucose level-dependent post-translational modification	377:433	a glucose level-dependent post-translational modification that adds O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins	377:497	Here we examined the relationship between O-GlcNAcylation, which is a glucose level-dependent post-translational modification that adds O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins, and Aβ production in a mouse model of AD carrying 5XFAD genes.
22503002	3	17	theme	post-translational	403:420	arg1	O-GlcNAcylation					351:365	O-GlcNAcylation	351:365	O-GlcNAcylation	351:365	Here we examined the relationship between O-GlcNAcylation, which is a glucose level-dependent post-translational modification that adds O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins, and Aβ production in a mouse model of AD carrying 5XFAD genes.
22503002	0	18	theme	O-linked	0:7	arg1	inhibitor					35:43	O-linked β-N-acetylglucosaminidase inhibitor	0:43	O-linked β-N-acetylglucosaminidase inhibitor	0:43	O-linked β-N-acetylglucosaminidase inhibitor attenuates β-amyloid plaque and rescues memory impairment.
22503002	3	19	contain	carrying	541:548	arg2	genes					556:560	5XFAD genes	550:560	5XFAD genes	550:560	Here we examined the relationship between O-GlcNAcylation, which is a glucose level-dependent post-translational modification that adds O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins, and Aβ production in a mouse model of AD carrying 5XFAD genes.
22503002	3	19	contain	carrying	541:548	arg1	AD					538:539	AD	538:539	AD carrying 5XFAD genes	538:560	Here we examined the relationship between O-GlcNAcylation, which is a glucose level-dependent post-translational modification that adds O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins, and Aβ production in a mouse model of AD carrying 5XFAD genes.
22503002	1	20	theme	β-amyloid	118:126	arg1	Deposition					104:113	Deposition	104:113	Deposition of β-amyloid (Aβ) as senile plaques	104:149	Deposition of β-amyloid (Aβ) as senile plaques and disrupted glucose metabolism are two main characteristics of Alzheimer's disease (AD).
22503002	1	20	theme	β-amyloid	118:126	arg1	characteristics					197:211	two main characteristics	188:211	two main characteristics of Alzheimer's disease (AD)	188:239	Deposition of β-amyloid (Aβ) as senile plaques and disrupted glucose metabolism are two main characteristics of Alzheimer's disease (AD).
22503002	1	20	theme	β-amyloid	118:126	arg1	metabolism					173:182	disrupted glucose metabolism	155:182	disrupted glucose metabolism	155:182	Deposition of β-amyloid (Aβ) as senile plaques and disrupted glucose metabolism are two main characteristics of Alzheimer's disease (AD).
22503002	6	21	theme	neuroinflammation	939:955	arg1	accumulation					919:930	the accumulation	915:930	the accumulation of Aβ, neuroinflammation, and memory impairment in the 5XFAD mice	915:996	Moreover, NButGT attenuated the accumulation of Aβ, neuroinflammation, and memory impairment in the 5XFAD mice.
22503002	3	22	theme	AD	538:539	arg1	model					529:533	a mouse model	521:533	a mouse model of AD carrying 5XFAD genes	521:560	Here we examined the relationship between O-GlcNAcylation, which is a glucose level-dependent post-translational modification that adds O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins, and Aβ production in a mouse model of AD carrying 5XFAD genes.
22503002	8	23	theme	therapeutic	1160:1170	arg1	O-GlcNAcylation					1126:1140	O-GlcNAcylation	1126:1140	O-GlcNAcylation	1126:1140	These results suggest that O-GlcNAcylation may be a suitable therapeutic target for the treatment of AD.
22503002	8	23	theme	therapeutic	1160:1170	arg1	target					1172:1177	a suitable therapeutic target	1149:1177	a suitable therapeutic target for the treatment of AD	1149:1201	These results suggest that O-GlcNAcylation may be a suitable therapeutic target for the treatment of AD.
22503002	5	24	theme	γ-secretase	874:884	arg1	residue					828:834	the S708 residue	819:834	the S708 residue	819:834	We also found that O-GlcNAcylation takes place at the S708 residue of nicastrin, which is a component of γ-secretase.
22503002	5	24	theme	γ-secretase	874:884	arg1	component					861:869	a component	859:869	a component of γ-secretase	859:884	We also found that O-GlcNAcylation takes place at the S708 residue of nicastrin, which is a component of γ-secretase.
22503002	5	24	theme	γ-secretase	874:884	arg1	nicastrin					839:847	nicastrin	839:847	nicastrin	839:847	We also found that O-GlcNAcylation takes place at the S708 residue of nicastrin, which is a component of γ-secretase.
22503002	5	25	theme	S708	823:826	arg1	residue					828:834	the S708 residue	819:834	the S708 residue	819:834	We also found that O-GlcNAcylation takes place at the S708 residue of nicastrin, which is a component of γ-secretase.
22503002	5	25	theme	S708	823:826	arg1	component					861:869	a component	859:869	a component of γ-secretase	859:884	We also found that O-GlcNAcylation takes place at the S708 residue of nicastrin, which is a component of γ-secretase.
22503002	5	25	theme	S708	823:826	arg1	nicastrin					839:847	nicastrin	839:847	nicastrin	839:847	We also found that O-GlcNAcylation takes place at the S708 residue of nicastrin, which is a component of γ-secretase.
22503002	3	26	theme	glucose	379:385	arg1	production					507:516	Aβ production	504:516	Aβ production	504:516	Here we examined the relationship between O-GlcNAcylation, which is a glucose level-dependent post-translational modification that adds O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins, and Aβ production in a mouse model of AD carrying 5XFAD genes.
22503002	3	26	theme	glucose	379:385	arg1	modification					422:433	a glucose level-dependent post-translational modification	377:433	a glucose level-dependent post-translational modification that adds O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins	377:497	Here we examined the relationship between O-GlcNAcylation, which is a glucose level-dependent post-translational modification that adds O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins, and Aβ production in a mouse model of AD carrying 5XFAD genes.
22503002	3	26	theme	glucose	379:385	arg1	O-GlcNAcylation					351:365	O-GlcNAcylation	351:365	O-GlcNAcylation	351:365	Here we examined the relationship between O-GlcNAcylation, which is a glucose level-dependent post-translational modification that adds O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins, and Aβ production in a mouse model of AD carrying 5XFAD genes.
22503002	6	27	theme	Aβ	935:936	arg1	accumulation					919:930	the accumulation	915:930	the accumulation of Aβ, neuroinflammation, and memory impairment in the 5XFAD mice	915:996	Moreover, NButGT attenuated the accumulation of Aβ, neuroinflammation, and memory impairment in the 5XFAD mice.
22503002	3	28	theme	O-linked	445:452	arg1	β-N-acetylglucosamine					454:474	O-linked β-N-acetylglucosamine	445:474	O-linked β-N-acetylglucosamine (O-GlcNAc)	445:485	Here we examined the relationship between O-GlcNAcylation, which is a glucose level-dependent post-translational modification that adds O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins, and Aβ production in a mouse model of AD carrying 5XFAD genes.
22503002	3	28	theme	O-linked	445:452	arg1	O-GlcNAc					477:484	O-GlcNAc	477:484	O-GlcNAc	477:484	Here we examined the relationship between O-GlcNAcylation, which is a glucose level-dependent post-translational modification that adds O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins, and Aβ production in a mouse model of AD carrying 5XFAD genes.
22503002	0	29	theme	β-amyloid	56:64	arg1	plaque					66:71	β-amyloid plaque	56:71	β-amyloid plaque	56:71	O-linked β-N-acetylglucosaminidase inhibitor attenuates β-amyloid plaque and rescues memory impairment.
22503002	3	30	theme	level-dependent	387:401	arg1	production					507:516	Aβ production	504:516	Aβ production	504:516	Here we examined the relationship between O-GlcNAcylation, which is a glucose level-dependent post-translational modification that adds O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins, and Aβ production in a mouse model of AD carrying 5XFAD genes.
22503002	3	30	theme	level-dependent	387:401	arg1	modification					422:433	a glucose level-dependent post-translational modification	377:433	a glucose level-dependent post-translational modification that adds O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins	377:497	Here we examined the relationship between O-GlcNAcylation, which is a glucose level-dependent post-translational modification that adds O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins, and Aβ production in a mouse model of AD carrying 5XFAD genes.
22503002	3	30	theme	level-dependent	387:401	arg1	O-GlcNAcylation					351:365	O-GlcNAcylation	351:365	O-GlcNAcylation	351:365	Here we examined the relationship between O-GlcNAcylation, which is a glucose level-dependent post-translational modification that adds O-linked β-N-acetylglucosamine (O-GlcNAc) to proteins, and Aβ production in a mouse model of AD carrying 5XFAD genes.
22503002	8	31	theme	suitable	1151:1158	arg1	O-GlcNAcylation					1126:1140	O-GlcNAcylation	1126:1140	O-GlcNAcylation	1126:1140	These results suggest that O-GlcNAcylation may be a suitable therapeutic target for the treatment of AD.
22503002	8	31	theme	suitable	1151:1158	arg1	target					1172:1177	a suitable therapeutic target	1149:1177	a suitable therapeutic target for the treatment of AD	1149:1201	These results suggest that O-GlcNAcylation may be a suitable therapeutic target for the treatment of AD.
22503002	4	32	theme	1,2-dideoxy-2'-propyl-	577:598	arg1	inhibitor					661:669	a specific inhibitor	650:669	a specific inhibitor of O-GlcNAcase	650:684	We found that 1,2-dideoxy-2'-propyl-α-d-glucopyranoso-[2,1-D]-Δ2'-thiazoline (NButGT), a specific inhibitor of O-GlcNAcase, reduces Aβ production by lowering γ-secretase activity both in vitro and in vivo.
22503002	4	32	theme	1,2-dideoxy-2'-propyl-	577:598	arg1	NButGT					641:646	NButGT	641:646	NButGT	641:646	We found that 1,2-dideoxy-2'-propyl-α-d-glucopyranoso-[2,1-D]-Δ2'-thiazoline (NButGT), a specific inhibitor of O-GlcNAcase, reduces Aβ production by lowering γ-secretase activity both in vitro and in vivo.
22503002	4	32	theme	1,2-dideoxy-2'-propyl-	577:598	arg1	-Δ2'-thiazoline					624:638	1,2-dideoxy-2'-propyl-α-d-glucopyranoso-[2,1-D]-Δ2'-thiazoline	577:638	1,2-dideoxy-2'-propyl-α-d-glucopyranoso-[2,1-D]-Δ2'-thiazoline (NButGT)	577:647	We found that 1,2-dideoxy-2'-propyl-α-d-glucopyranoso-[2,1-D]-Δ2'-thiazoline (NButGT), a specific inhibitor of O-GlcNAcase, reduces Aβ production by lowering γ-secretase activity both in vitro and in vivo.
22503002	7	33	theme	first	1011:1015	arg1	This					999:1002	This	999:1002	This	999:1002	This is the first study to show the relationship between Aβ generation and O-GlcNAcylation in vivo.
22503002	7	33	theme	first	1011:1015	arg1	study					1017:1021	the first study	1007:1021	the first study to show the relationship between Aβ generation and O-GlcNAcylation in vivo	1007:1096	This is the first study to show the relationship between Aβ generation and O-GlcNAcylation in vivo.
22503002	1	34	theme	senile	136:141	arg1	plaques					143:149	senile plaques	136:149	senile plaques	136:149	Deposition of β-amyloid (Aβ) as senile plaques and disrupted glucose metabolism are two main characteristics of Alzheimer's disease (AD).
22503002	4	35	theme	α-d-glucopyranoso-[2,1-D	599:622	arg1	inhibitor					661:669	a specific inhibitor	650:669	a specific inhibitor of O-GlcNAcase	650:684	We found that 1,2-dideoxy-2'-propyl-α-d-glucopyranoso-[2,1-D]-Δ2'-thiazoline (NButGT), a specific inhibitor of O-GlcNAcase, reduces Aβ production by lowering γ-secretase activity both in vitro and in vivo.
22503002	4	35	theme	α-d-glucopyranoso-[2,1-D	599:622	arg1	NButGT					641:646	NButGT	641:646	NButGT	641:646	We found that 1,2-dideoxy-2'-propyl-α-d-glucopyranoso-[2,1-D]-Δ2'-thiazoline (NButGT), a specific inhibitor of O-GlcNAcase, reduces Aβ production by lowering γ-secretase activity both in vitro and in vivo.
22503002	4	35	theme	α-d-glucopyranoso-[2,1-D	599:622	arg1	-Δ2'-thiazoline					624:638	1,2-dideoxy-2'-propyl-α-d-glucopyranoso-[2,1-D]-Δ2'-thiazoline	577:638	1,2-dideoxy-2'-propyl-α-d-glucopyranoso-[2,1-D]-Δ2'-thiazoline (NButGT)	577:647	We found that 1,2-dideoxy-2'-propyl-α-d-glucopyranoso-[2,1-D]-Δ2'-thiazoline (NButGT), a specific inhibitor of O-GlcNAcase, reduces Aβ production by lowering γ-secretase activity both in vitro and in vivo.
22503002	6	36	from	accumulation	919:930	arg1	mice					993:996	the 5XFAD mice	983:996	the 5XFAD mice	983:996	Moreover, NButGT attenuated the accumulation of Aβ, neuroinflammation, and memory impairment in the 5XFAD mice.
22503002	4	37	theme	O-GlcNAcase	674:684	arg1	inhibitor					661:669	a specific inhibitor	650:669	a specific inhibitor of O-GlcNAcase	650:684	We found that 1,2-dideoxy-2'-propyl-α-d-glucopyranoso-[2,1-D]-Δ2'-thiazoline (NButGT), a specific inhibitor of O-GlcNAcase, reduces Aβ production by lowering γ-secretase activity both in vitro and in vivo.
22503002	4	37	theme	O-GlcNAcase	674:684	arg1	-Δ2'-thiazoline					624:638	1,2-dideoxy-2'-propyl-α-d-glucopyranoso-[2,1-D]-Δ2'-thiazoline	577:638	1,2-dideoxy-2'-propyl-α-d-glucopyranoso-[2,1-D]-Δ2'-thiazoline (NButGT)	577:647	We found that 1,2-dideoxy-2'-propyl-α-d-glucopyranoso-[2,1-D]-Δ2'-thiazoline (NButGT), a specific inhibitor of O-GlcNAcase, reduces Aβ production by lowering γ-secretase activity both in vitro and in vivo.
22503002	4	38	theme	γ-secretase	721:731	arg1	activity					733:740	γ-secretase activity	721:740	γ-secretase activity	721:740	We found that 1,2-dideoxy-2'-propyl-α-d-glucopyranoso-[2,1-D]-Δ2'-thiazoline (NButGT), a specific inhibitor of O-GlcNAcase, reduces Aβ production by lowering γ-secretase activity both in vitro and in vivo.
22503002	6	39	theme	5XFAD	987:991	arg1	mice					993:996	the 5XFAD mice	983:996	the 5XFAD mice	983:996	Moreover, NButGT attenuated the accumulation of Aβ, neuroinflammation, and memory impairment in the 5XFAD mice.
22503002	0	40	theme	memory	85:90	arg1	impairment					92:101	memory impairment	85:101	memory impairment	85:101	O-linked β-N-acetylglucosaminidase inhibitor attenuates β-amyloid plaque and rescues memory impairment.
22503002	1	41	theme	disrupted	155:163	arg1	characteristics					197:211	two main characteristics	188:211	two main characteristics of Alzheimer's disease (AD)	188:239	Deposition of β-amyloid (Aβ) as senile plaques and disrupted glucose metabolism are two main characteristics of Alzheimer's disease (AD).
22503002	1	41	theme	disrupted	155:163	arg1	Deposition					104:113	Deposition	104:113	Deposition of β-amyloid (Aβ) as senile plaques	104:149	Deposition of β-amyloid (Aβ) as senile plaques and disrupted glucose metabolism are two main characteristics of Alzheimer's disease (AD).
22503002	1	41	theme	disrupted	155:163	arg1	metabolism					173:182	disrupted glucose metabolism	155:182	disrupted glucose metabolism	155:182	Deposition of β-amyloid (Aβ) as senile plaques and disrupted glucose metabolism are two main characteristics of Alzheimer's disease (AD).
22887999	4	0	theme	smooth	874:879	arg1	cells					888:892	primary human aortic smooth muscle cells	853:892	primary human aortic smooth muscle cells	853:892	Therefore, we analyzed the effect of UDP-GlcNAc availability and protein glycosylation with O-linked N-acetylglucosamine (O-GlcNAcylation) on HA and chondroitin sulfate synthesis in primary human aortic smooth muscle cells.
22887999	2	1	theme	other	348:352	arg1	glycosaminoglycans					354:371	other glycosaminoglycans	348:371	other glycosaminoglycans	348:371	In contrast with other glycosaminoglycans, which are synthesized in the Golgi, HA is synthesized at the plasma membrane by one or more of the three HA synthases (HAS1-3), which use cytoplasmic UDP-glucuronic acid and UDP-N-acetylglucosamine as substrates.
22887999	9	2	theme	critical	1749:1756	arg1	processes					1739:1747	cell dedifferentiation processes	1716:1747	cell dedifferentiation processes critical in vascular pathologies	1716:1780	These findings could explain the elevated matrix HA observed in diabetic vessels that, in turn, could mediate cell dedifferentiation processes critical in vascular pathologies.
22887999	8	3	theme	S221A	1463:1467	arg1	mutation					1469:1476	S221A mutation	1463:1476	S221A mutation	1463:1476	S221A mutation prevented HAS2 O-GlcNAcylation, which maintained the rapid turnover rate even in the presence of GlcN and increased UDP-GlcNAc.
22887999	0	4	theme	synthase	75:82	arg1	UDP-N-acetylglucosamine					8:30	UDP-N-acetylglucosamine	8:30	UDP-N-acetylglucosamine (GlcNAc)	8:39	Role of UDP-N-acetylglucosamine (GlcNAc) and O-GlcNAcylation of hyaluronan synthase 2 in the control of chondroitin sulfate and hyaluronan synthesis.
22887999	0	4	theme	synthase	75:82	arg1	GlcNAc					33:38	GlcNAc	33:38	GlcNAc	33:38	Role of UDP-N-acetylglucosamine (GlcNAc) and O-GlcNAcylation of hyaluronan synthase 2 in the control of chondroitin sulfate and hyaluronan synthesis.
22887999	0	4	theme	synthase	75:82	arg1	O-GlcNAcylation					45:59	O-GlcNAcylation	45:59	O-GlcNAcylation of hyaluronan synthase 2	45:84	Role of UDP-N-acetylglucosamine (GlcNAc) and O-GlcNAcylation of hyaluronan synthase 2 in the control of chondroitin sulfate and hyaluronan synthesis.
22887999	4	5	theme	aortic	867:872	arg1	cells					888:892	primary human aortic smooth muscle cells	853:892	primary human aortic smooth muscle cells	853:892	Therefore, we analyzed the effect of UDP-GlcNAc availability and protein glycosylation with O-linked N-acetylglucosamine (O-GlcNAcylation) on HA and chondroitin sulfate synthesis in primary human aortic smooth muscle cells.
22887999	6	6	theme	UDP-GlcNAc	1202:1211	arg1	increase					1190:1197	a concomitant increase	1176:1197	a concomitant increase of UDP-GlcNAc	1176:1211	However, increasing O-GlcNAcylation by stimulation with O-(2-acetamido-2-deoxy-d-glucopyranosylidene)amino-N-phenylcarbamate without a concomitant increase of UDP-GlcNAc increased only HA synthesis.
22887999	8	7	theme	turnover	1537:1544	arg1	rate					1546:1549	the rapid turnover rate	1527:1549	the rapid turnover rate	1527:1549	S221A mutation prevented HAS2 O-GlcNAcylation, which maintained the rapid turnover rate even in the presence of GlcN and increased UDP-GlcNAc.
22887999	1	8	theme	many	248:251	arg1	proliferation					279:291	proliferation	279:291	proliferation	279:291	Hyaluronan (HA) is a glycosaminoglycan present in most tissue microenvironments that can modulate many cell behaviors, including proliferation, migration, and adhesive proprieties.
22887999	1	8	theme	many	248:251	arg1	proprieties					318:328	adhesive proprieties	309:328	adhesive proprieties	309:328	Hyaluronan (HA) is a glycosaminoglycan present in most tissue microenvironments that can modulate many cell behaviors, including proliferation, migration, and adhesive proprieties.
22887999	1	8	theme	many	248:251	arg1	migration					294:302	migration	294:302	migration	294:302	Hyaluronan (HA) is a glycosaminoglycan present in most tissue microenvironments that can modulate many cell behaviors, including proliferation, migration, and adhesive proprieties.
22887999	1	8	theme	many	248:251	arg1	behaviors					258:266	many cell behaviors	248:266	many cell behaviors	248:266	Hyaluronan (HA) is a glycosaminoglycan present in most tissue microenvironments that can modulate many cell behaviors, including proliferation, migration, and adhesive proprieties.
22887999	7	9	theme	main	1266:1269	arg1	synthase					1271:1278	the main synthase	1262:1278	the main synthase in aortic smooth muscle cells	1262:1308	We found that HAS2, the main synthase in aortic smooth muscle cells, can be O-GlcNAcylated on serine 221, which strongly increased its activity and its stability (t(&frac12;) >5 h versus ∼17 min without O-GlcNAcylation).
22887999	7	9	theme	main	1266:1269	arg1	HAS2					1256:1259	HAS2	1256:1259	HAS2	1256:1259	We found that HAS2, the main synthase in aortic smooth muscle cells, can be O-GlcNAcylated on serine 221, which strongly increased its activity and its stability (t(&frac12;) >5 h versus ∼17 min without O-GlcNAcylation).
22887999	0	10	from	Role	0:3	arg1	control					93:99	the control	89:99	the control of chondroitin sulfate and hyaluronan synthesis	89:147	Role of UDP-N-acetylglucosamine (GlcNAc) and O-GlcNAcylation of hyaluronan synthase 2 in the control of chondroitin sulfate and hyaluronan synthesis.
22887999	9	11	theme	diabetic	1670:1677	arg1	vessels					1679:1685	diabetic vessels	1670:1685	diabetic vessels that, in turn, could mediate cell dedifferentiation processes critical in vascular pathologies	1670:1780	These findings could explain the elevated matrix HA observed in diabetic vessels that, in turn, could mediate cell dedifferentiation processes critical in vascular pathologies.
22887999	1	12	theme	cell	253:256	arg1	proliferation					279:291	proliferation	279:291	proliferation	279:291	Hyaluronan (HA) is a glycosaminoglycan present in most tissue microenvironments that can modulate many cell behaviors, including proliferation, migration, and adhesive proprieties.
22887999	1	12	theme	cell	253:256	arg1	proprieties					318:328	adhesive proprieties	309:328	adhesive proprieties	309:328	Hyaluronan (HA) is a glycosaminoglycan present in most tissue microenvironments that can modulate many cell behaviors, including proliferation, migration, and adhesive proprieties.
22887999	1	12	theme	cell	253:256	arg1	migration					294:302	migration	294:302	migration	294:302	Hyaluronan (HA) is a glycosaminoglycan present in most tissue microenvironments that can modulate many cell behaviors, including proliferation, migration, and adhesive proprieties.
22887999	1	12	theme	cell	253:256	arg1	behaviors					258:266	many cell behaviors	248:266	many cell behaviors	248:266	Hyaluronan (HA) is a glycosaminoglycan present in most tissue microenvironments that can modulate many cell behaviors, including proliferation, migration, and adhesive proprieties.
22887999	2	13	theme	synthases	482:490	arg1	HAS1-3					493:498	HAS1-3	493:498	HAS1-3	493:498	In contrast with other glycosaminoglycans, which are synthesized in the Golgi, HA is synthesized at the plasma membrane by one or more of the three HA synthases (HAS1-3), which use cytoplasmic UDP-glucuronic acid and UDP-N-acetylglucosamine as substrates.
22887999	2	13	theme	synthases	482:490	arg1	synthases					482:490	the three HA synthases	469:490	the three HA synthases (HAS1-3)	469:499	In contrast with other glycosaminoglycans, which are synthesized in the Golgi, HA is synthesized at the plasma membrane by one or more of the three HA synthases (HAS1-3), which use cytoplasmic UDP-glucuronic acid and UDP-N-acetylglucosamine as substrates.
22887999	2	13	theme	synthases	482:490	arg1	one					454:456	one	454:456	one	454:456	In contrast with other glycosaminoglycans, which are synthesized in the Golgi, HA is synthesized at the plasma membrane by one or more of the three HA synthases (HAS1-3), which use cytoplasmic UDP-glucuronic acid and UDP-N-acetylglucosamine as substrates.
22887999	4	14	theme	muscle	881:886	arg1	cells					888:892	primary human aortic smooth muscle cells	853:892	primary human aortic smooth muscle cells	853:892	Therefore, we analyzed the effect of UDP-GlcNAc availability and protein glycosylation with O-linked N-acetylglucosamine (O-GlcNAcylation) on HA and chondroitin sulfate synthesis in primary human aortic smooth muscle cells.
22887999	4	15	theme	glycosylation	744:756	arg1	effect					698:703	the effect	694:703	the effect of UDP-GlcNAc availability and protein glycosylation with O-linked N-acetylglucosamine (O-GlcNAcylation) on HA and chondroitin sulfate synthesis in primary human aortic smooth muscle cells	694:892	Therefore, we analyzed the effect of UDP-GlcNAc availability and protein glycosylation with O-linked N-acetylglucosamine (O-GlcNAcylation) on HA and chondroitin sulfate synthesis in primary human aortic smooth muscle cells.
22887999	2	16	theme	HA	479:480	arg1	HAS1-3					493:498	HAS1-3	493:498	HAS1-3	493:498	In contrast with other glycosaminoglycans, which are synthesized in the Golgi, HA is synthesized at the plasma membrane by one or more of the three HA synthases (HAS1-3), which use cytoplasmic UDP-glucuronic acid and UDP-N-acetylglucosamine as substrates.
22887999	2	16	theme	HA	479:480	arg1	synthases					482:490	the three HA synthases	469:490	the three HA synthases (HAS1-3)	469:499	In contrast with other glycosaminoglycans, which are synthesized in the Golgi, HA is synthesized at the plasma membrane by one or more of the three HA synthases (HAS1-3), which use cytoplasmic UDP-glucuronic acid and UDP-N-acetylglucosamine as substrates.
22887999	5	17	theme	protein	962:968	arg1	O-GlcNAcylation					970:984	protein O-GlcNAcylation	962:984	protein O-GlcNAcylation	962:984	Glucosamine treatment, which increases UDP-GlcNAc availability and protein O-GlcNAcylation, increased synthesis of both HA and chondroitin sulfate.
22887999	8	18	theme	HAS2	1488:1491	arg1	O-GlcNAcylation					1493:1507	HAS2 O-GlcNAcylation	1488:1507	HAS2 O-GlcNAcylation	1488:1507	S221A mutation prevented HAS2 O-GlcNAcylation, which maintained the rapid turnover rate even in the presence of GlcN and increased UDP-GlcNAc.
22887999	9	19	located	observed	1658:1665	arg2	HA					1655:1656	the elevated matrix HA	1635:1656	the elevated matrix HA observed in diabetic vessels that, in turn, could mediate cell dedifferentiation processes critical in vascular pathologies	1635:1780	These findings could explain the elevated matrix HA observed in diabetic vessels that, in turn, could mediate cell dedifferentiation processes critical in vascular pathologies.
22887999	9	19	located	observed	1658:1665	arg1	vessels					1679:1685	diabetic vessels	1670:1685	diabetic vessels that, in turn, could mediate cell dedifferentiation processes critical in vascular pathologies	1670:1780	These findings could explain the elevated matrix HA observed in diabetic vessels that, in turn, could mediate cell dedifferentiation processes critical in vascular pathologies.
22887999	6	20	theme	HA	1228:1229	arg1	synthesis					1231:1239	only HA synthesis	1223:1239	only HA synthesis	1223:1239	However, increasing O-GlcNAcylation by stimulation with O-(2-acetamido-2-deoxy-d-glucopyranosylidene)amino-N-phenylcarbamate without a concomitant increase of UDP-GlcNAc increased only HA synthesis.
22887999	4	21	theme	O-linked	763:770	arg1	O-GlcNAcylation					793:807	O-GlcNAcylation	793:807	O-GlcNAcylation	793:807	Therefore, we analyzed the effect of UDP-GlcNAc availability and protein glycosylation with O-linked N-acetylglucosamine (O-GlcNAcylation) on HA and chondroitin sulfate synthesis in primary human aortic smooth muscle cells.
22887999	4	21	theme	O-linked	763:770	arg1	N-acetylglucosamine					772:790	O-linked N-acetylglucosamine	763:790	O-linked N-acetylglucosamine (O-GlcNAcylation)	763:808	Therefore, we analyzed the effect of UDP-GlcNAc availability and protein glycosylation with O-linked N-acetylglucosamine (O-GlcNAcylation) on HA and chondroitin sulfate synthesis in primary human aortic smooth muscle cells.
22887999	6	22	theme	2-acetamido-2-deoxy-d-glucopyranosylidene	1102:1142	arg1	amino-N-phenylcarbamate					1144:1166	O-(2-acetamido-2-deoxy-d-glucopyranosylidene)amino-N-phenylcarbamate	1099:1166	O-(2-acetamido-2-deoxy-d-glucopyranosylidene)amino-N-phenylcarbamate	1099:1166	However, increasing O-GlcNAcylation by stimulation with O-(2-acetamido-2-deoxy-d-glucopyranosylidene)amino-N-phenylcarbamate without a concomitant increase of UDP-GlcNAc increased only HA synthesis.
22887999	4	23	from	synthesis	840:848	arg1	cells					888:892	primary human aortic smooth muscle cells	853:892	primary human aortic smooth muscle cells	853:892	Therefore, we analyzed the effect of UDP-GlcNAc availability and protein glycosylation with O-linked N-acetylglucosamine (O-GlcNAcylation) on HA and chondroitin sulfate synthesis in primary human aortic smooth muscle cells.
22887999	4	24	theme	human	861:865	arg1	cells					888:892	primary human aortic smooth muscle cells	853:892	primary human aortic smooth muscle cells	853:892	Therefore, we analyzed the effect of UDP-GlcNAc availability and protein glycosylation with O-linked N-acetylglucosamine (O-GlcNAcylation) on HA and chondroitin sulfate synthesis in primary human aortic smooth muscle cells.
22887999	4	25	gly	glycosylation	744:756	arg1	sulfate					832:838	chondroitin sulfate synthesis	820:848	chondroitin sulfate synthesis	820:848	Therefore, we analyzed the effect of UDP-GlcNAc availability and protein glycosylation with O-linked N-acetylglucosamine (O-GlcNAcylation) on HA and chondroitin sulfate synthesis in primary human aortic smooth muscle cells.
22887999	4	26	theme	availability	719:730	arg1	effect					698:703	the effect	694:703	the effect of UDP-GlcNAc availability and protein glycosylation with O-linked N-acetylglucosamine (O-GlcNAcylation) on HA and chondroitin sulfate synthesis in primary human aortic smooth muscle cells	694:892	Therefore, we analyzed the effect of UDP-GlcNAc availability and protein glycosylation with O-linked N-acetylglucosamine (O-GlcNAcylation) on HA and chondroitin sulfate synthesis in primary human aortic smooth muscle cells.
22887999	2	27	theme	UDP-glucuronic	524:537	arg1	substrates					575:584	substrates	575:584	substrates	575:584	In contrast with other glycosaminoglycans, which are synthesized in the Golgi, HA is synthesized at the plasma membrane by one or more of the three HA synthases (HAS1-3), which use cytoplasmic UDP-glucuronic acid and UDP-N-acetylglucosamine as substrates.
22887999	2	27	theme	UDP-glucuronic	524:537	arg1	UDP-N-acetylglucosamine					548:570	UDP-N-acetylglucosamine	548:570	UDP-N-acetylglucosamine	548:570	In contrast with other glycosaminoglycans, which are synthesized in the Golgi, HA is synthesized at the plasma membrane by one or more of the three HA synthases (HAS1-3), which use cytoplasmic UDP-glucuronic acid and UDP-N-acetylglucosamine as substrates.
22887999	2	27	theme	UDP-glucuronic	524:537	arg1	acid					539:542	cytoplasmic UDP-glucuronic acid	512:542	cytoplasmic UDP-glucuronic acid	512:542	In contrast with other glycosaminoglycans, which are synthesized in the Golgi, HA is synthesized at the plasma membrane by one or more of the three HA synthases (HAS1-3), which use cytoplasmic UDP-glucuronic acid and UDP-N-acetylglucosamine as substrates.
22887999	9	28	theme	dedifferentiation	1721:1737	arg1	processes					1739:1747	cell dedifferentiation processes	1716:1747	cell dedifferentiation processes critical in vascular pathologies	1716:1780	These findings could explain the elevated matrix HA observed in diabetic vessels that, in turn, could mediate cell dedifferentiation processes critical in vascular pathologies.
22887999	4	29	from	HA	813:814	arg1	cells					888:892	primary human aortic smooth muscle cells	853:892	primary human aortic smooth muscle cells	853:892	Therefore, we analyzed the effect of UDP-GlcNAc availability and protein glycosylation with O-linked N-acetylglucosamine (O-GlcNAcylation) on HA and chondroitin sulfate synthesis in primary human aortic smooth muscle cells.
22887999	4	30	theme	primary	853:859	arg1	cells					888:892	primary human aortic smooth muscle cells	853:892	primary human aortic smooth muscle cells	853:892	Therefore, we analyzed the effect of UDP-GlcNAc availability and protein glycosylation with O-linked N-acetylglucosamine (O-GlcNAcylation) on HA and chondroitin sulfate synthesis in primary human aortic smooth muscle cells.
22887999	3	31	theme	HA	657:658	arg1	synthesis					660:668	HA synthesis	657:668	HA synthesis	657:668	Previous studies revealed the importance of UDP-sugars for regulating HA synthesis.
22887999	6	32	theme	O-	1099:1100	arg1	amino-N-phenylcarbamate					1144:1166	O-(2-acetamido-2-deoxy-d-glucopyranosylidene)amino-N-phenylcarbamate	1099:1166	O-(2-acetamido-2-deoxy-d-glucopyranosylidene)amino-N-phenylcarbamate	1099:1166	However, increasing O-GlcNAcylation by stimulation with O-(2-acetamido-2-deoxy-d-glucopyranosylidene)amino-N-phenylcarbamate without a concomitant increase of UDP-GlcNAc increased only HA synthesis.
22887999	4	33	theme	UDP-GlcNAc	708:717	arg1	availability					719:730	UDP-GlcNAc availability	708:730	UDP-GlcNAc availability	708:730	Therefore, we analyzed the effect of UDP-GlcNAc availability and protein glycosylation with O-linked N-acetylglucosamine (O-GlcNAcylation) on HA and chondroitin sulfate synthesis in primary human aortic smooth muscle cells.
22887999	0	34	theme	sulfate	116:122	arg1	control					93:99	the control	89:99	the control of chondroitin sulfate and hyaluronan synthesis	89:147	Role of UDP-N-acetylglucosamine (GlcNAc) and O-GlcNAcylation of hyaluronan synthase 2 in the control of chondroitin sulfate and hyaluronan synthesis.
22887999	9	35	theme	elevated	1639:1646	arg1	HA					1655:1656	the elevated matrix HA	1635:1656	the elevated matrix HA observed in diabetic vessels that, in turn, could mediate cell dedifferentiation processes critical in vascular pathologies	1635:1780	These findings could explain the elevated matrix HA observed in diabetic vessels that, in turn, could mediate cell dedifferentiation processes critical in vascular pathologies.
22887999	4	36	theme	protein	736:742	arg1	glycosylation					744:756	protein glycosylation	736:756	protein glycosylation	736:756	Therefore, we analyzed the effect of UDP-GlcNAc availability and protein glycosylation with O-linked N-acetylglucosamine (O-GlcNAcylation) on HA and chondroitin sulfate synthesis in primary human aortic smooth muscle cells.
22887999	7	37	dep	stability	1394:1402	arg1	h					1420:1420	t(&frac12;) >5 h	1405:1420	t(&frac12;) >5 h	1405:1420	We found that HAS2, the main synthase in aortic smooth muscle cells, can be O-GlcNAcylated on serine 221, which strongly increased its activity and its stability (t(&frac12;) >5 h versus ∼17 min without O-GlcNAcylation).
22887999	7	37	dep	stability	1394:1402	arg1	min					1433:1435	∼17 min	1429:1435	∼17 min without O-GlcNAcylation	1429:1459	We found that HAS2, the main synthase in aortic smooth muscle cells, can be O-GlcNAcylated on serine 221, which strongly increased its activity and its stability (t(&frac12;) >5 h versus ∼17 min without O-GlcNAcylation).
22887999	7	37	dep	stability	1394:1402	arg1	&frac12					1407:1413	&frac12;	1407:1414	&frac12;	1407:1414	We found that HAS2, the main synthase in aortic smooth muscle cells, can be O-GlcNAcylated on serine 221, which strongly increased its activity and its stability (t(&frac12;) >5 h versus ∼17 min without O-GlcNAcylation).
22887999	0	38	theme	UDP-N-acetylglucosamine	8:30	arg1	Role					0:3	Role	0:3	Role of UDP-N-acetylglucosamine (GlcNAc) and O-GlcNAcylation of hyaluronan synthase 2 in the control of chondroitin sulfate and hyaluronan synthesis.	0:148	Role of UDP-N-acetylglucosamine (GlcNAc) and O-GlcNAcylation of hyaluronan synthase 2 in the control of chondroitin sulfate and hyaluronan synthesis.
22887999	0	39	theme	chondroitin	104:114	arg1	sulfate					116:122	chondroitin sulfate	104:122	chondroitin sulfate	104:122	Role of UDP-N-acetylglucosamine (GlcNAc) and O-GlcNAcylation of hyaluronan synthase 2 in the control of chondroitin sulfate and hyaluronan synthesis.
22887999	6	40	theme	only	1223:1226	arg1	synthesis					1231:1239	only HA synthesis	1223:1239	only HA synthesis	1223:1239	However, increasing O-GlcNAcylation by stimulation with O-(2-acetamido-2-deoxy-d-glucopyranosylidene)amino-N-phenylcarbamate without a concomitant increase of UDP-GlcNAc increased only HA synthesis.
22887999	1	41	theme	present	189:195	arg1	Hyaluronan					150:159	Hyaluronan	150:159	Hyaluronan (HA)	150:164	Hyaluronan (HA) is a glycosaminoglycan present in most tissue microenvironments that can modulate many cell behaviors, including proliferation, migration, and adhesive proprieties.
22887999	1	41	theme	present	189:195	arg1	glycosaminoglycan					171:187	a glycosaminoglycan	169:187	a glycosaminoglycan present in most tissue microenvironments that can modulate many cell behaviors, including proliferation, migration, and adhesive proprieties	169:328	Hyaluronan (HA) is a glycosaminoglycan present in most tissue microenvironments that can modulate many cell behaviors, including proliferation, migration, and adhesive proprieties.
22887999	7	42	theme	aortic	1283:1288	arg1	cells					1304:1308	aortic smooth muscle cells	1283:1308	aortic smooth muscle cells	1283:1308	We found that HAS2, the main synthase in aortic smooth muscle cells, can be O-GlcNAcylated on serine 221, which strongly increased its activity and its stability (t(&frac12;) >5 h versus ∼17 min without O-GlcNAcylation).
22887999	4	43	with	glycosylation	744:756	arg1	O-GlcNAcylation					793:807	O-GlcNAcylation	793:807	O-GlcNAcylation	793:807	Therefore, we analyzed the effect of UDP-GlcNAc availability and protein glycosylation with O-linked N-acetylglucosamine (O-GlcNAcylation) on HA and chondroitin sulfate synthesis in primary human aortic smooth muscle cells.
22887999	4	43	with	glycosylation	744:756	arg1	N-acetylglucosamine					772:790	O-linked N-acetylglucosamine	763:790	O-linked N-acetylglucosamine (O-GlcNAcylation)	763:808	Therefore, we analyzed the effect of UDP-GlcNAc availability and protein glycosylation with O-linked N-acetylglucosamine (O-GlcNAcylation) on HA and chondroitin sulfate synthesis in primary human aortic smooth muscle cells.
22887999	0	44	theme	hyaluronan	128:137	arg1	synthesis					139:147	hyaluronan synthesis	128:147	hyaluronan synthesis	128:147	Role of UDP-N-acetylglucosamine (GlcNAc) and O-GlcNAcylation of hyaluronan synthase 2 in the control of chondroitin sulfate and hyaluronan synthesis.
22887999	3	45	theme	UDP-sugars	631:640	arg1	importance					617:626	the importance	613:626	the importance of UDP-sugars for regulating HA synthesis	613:668	Previous studies revealed the importance of UDP-sugars for regulating HA synthesis.
22887999	5	46	theme	sulfate	1034:1040	arg1	synthesis					997:1005	synthesis	997:1005	synthesis of both HA and chondroitin sulfate	997:1040	Glucosamine treatment, which increases UDP-GlcNAc availability and protein O-GlcNAcylation, increased synthesis of both HA and chondroitin sulfate.
22887999	2	47	with	contrast	334:341	arg1	glycosaminoglycans					354:371	other glycosaminoglycans	348:371	other glycosaminoglycans	348:371	In contrast with other glycosaminoglycans, which are synthesized in the Golgi, HA is synthesized at the plasma membrane by one or more of the three HA synthases (HAS1-3), which use cytoplasmic UDP-glucuronic acid and UDP-N-acetylglucosamine as substrates.
22887999	7	48	theme	>5	1417:1418	arg1	h					1420:1420	t(&frac12;) >5 h	1405:1420	t(&frac12;) >5 h	1405:1420	We found that HAS2, the main synthase in aortic smooth muscle cells, can be O-GlcNAcylated on serine 221, which strongly increased its activity and its stability (t(&frac12;) >5 h versus ∼17 min without O-GlcNAcylation).
22887999	7	48	theme	>5	1417:1418	arg1	&frac12					1407:1413	&frac12;	1407:1414	&frac12;	1407:1414	We found that HAS2, the main synthase in aortic smooth muscle cells, can be O-GlcNAcylated on serine 221, which strongly increased its activity and its stability (t(&frac12;) >5 h versus ∼17 min without O-GlcNAcylation).
22887999	1	49	theme	most	200:203	arg1	microenvironments					212:228	most tissue microenvironments	200:228	most tissue microenvironments	200:228	Hyaluronan (HA) is a glycosaminoglycan present in most tissue microenvironments that can modulate many cell behaviors, including proliferation, migration, and adhesive proprieties.
22887999	0	50	theme	O-GlcNAcylation	45:59	arg1	Role					0:3	Role	0:3	Role of UDP-N-acetylglucosamine (GlcNAc) and O-GlcNAcylation of hyaluronan synthase 2 in the control of chondroitin sulfate and hyaluronan synthesis.	0:148	Role of UDP-N-acetylglucosamine (GlcNAc) and O-GlcNAcylation of hyaluronan synthase 2 in the control of chondroitin sulfate and hyaluronan synthesis.
22887999	8	51	dep	prevented	1478:1486	arg1	increased					1584:1592	increased	1584:1592	increased UDP-GlcNAc	1584:1603	S221A mutation prevented HAS2 O-GlcNAcylation, which maintained the rapid turnover rate even in the presence of GlcN and increased UDP-GlcNAc.
22887999	8	51	dep	prevented	1478:1486	arg1	maintained					1516:1525	maintained	1516:1525	maintained the rapid turnover rate even in the presence of GlcN	1516:1578	S221A mutation prevented HAS2 O-GlcNAcylation, which maintained the rapid turnover rate even in the presence of GlcN and increased UDP-GlcNAc.
22887999	7	52	theme	smooth	1290:1295	arg1	cells					1304:1308	aortic smooth muscle cells	1283:1308	aortic smooth muscle cells	1283:1308	We found that HAS2, the main synthase in aortic smooth muscle cells, can be O-GlcNAcylated on serine 221, which strongly increased its activity and its stability (t(&frac12;) >5 h versus ∼17 min without O-GlcNAcylation).
22887999	7	53	from	synthase	1271:1278	arg1	cells					1304:1308	aortic smooth muscle cells	1283:1308	aortic smooth muscle cells	1283:1308	We found that HAS2, the main synthase in aortic smooth muscle cells, can be O-GlcNAcylated on serine 221, which strongly increased its activity and its stability (t(&frac12;) >5 h versus ∼17 min without O-GlcNAcylation).
22887999	4	54	theme	sulfate	832:838	arg1	synthesis					840:848	chondroitin sulfate synthesis	820:848	chondroitin sulfate synthesis	820:848	Therefore, we analyzed the effect of UDP-GlcNAc availability and protein glycosylation with O-linked N-acetylglucosamine (O-GlcNAcylation) on HA and chondroitin sulfate synthesis in primary human aortic smooth muscle cells.
22887999	9	55	theme	vascular	1761:1768	arg1	pathologies					1770:1780	vascular pathologies	1761:1780	vascular pathologies	1761:1780	These findings could explain the elevated matrix HA observed in diabetic vessels that, in turn, could mediate cell dedifferentiation processes critical in vascular pathologies.
22887999	2	56	theme	plasma	435:440	arg1	membrane					442:449	the plasma membrane	431:449	the plasma membrane	431:449	In contrast with other glycosaminoglycans, which are synthesized in the Golgi, HA is synthesized at the plasma membrane by one or more of the three HA synthases (HAS1-3), which use cytoplasmic UDP-glucuronic acid and UDP-N-acetylglucosamine as substrates.
22887999	4	57	with	availability	719:730	arg1	O-GlcNAcylation					793:807	O-GlcNAcylation	793:807	O-GlcNAcylation	793:807	Therefore, we analyzed the effect of UDP-GlcNAc availability and protein glycosylation with O-linked N-acetylglucosamine (O-GlcNAcylation) on HA and chondroitin sulfate synthesis in primary human aortic smooth muscle cells.
22887999	4	57	with	availability	719:730	arg1	N-acetylglucosamine					772:790	O-linked N-acetylglucosamine	763:790	O-linked N-acetylglucosamine (O-GlcNAcylation)	763:808	Therefore, we analyzed the effect of UDP-GlcNAc availability and protein glycosylation with O-linked N-acetylglucosamine (O-GlcNAcylation) on HA and chondroitin sulfate synthesis in primary human aortic smooth muscle cells.
22887999	0	58	theme	synthesis	139:147	arg1	control					93:99	the control	89:99	the control of chondroitin sulfate and hyaluronan synthesis	89:147	Role of UDP-N-acetylglucosamine (GlcNAc) and O-GlcNAcylation of hyaluronan synthase 2 in the control of chondroitin sulfate and hyaluronan synthesis.
22887999	1	59	attach	present	189:195	arg2	Hyaluronan					150:159	Hyaluronan	150:159	Hyaluronan (HA)	150:164	Hyaluronan (HA) is a glycosaminoglycan present in most tissue microenvironments that can modulate many cell behaviors, including proliferation, migration, and adhesive proprieties.
22887999	1	59	attach	present	189:195	arg2	glycosaminoglycan					171:187	a glycosaminoglycan	169:187	a glycosaminoglycan present in most tissue microenvironments that can modulate many cell behaviors, including proliferation, migration, and adhesive proprieties	169:328	Hyaluronan (HA) is a glycosaminoglycan present in most tissue microenvironments that can modulate many cell behaviors, including proliferation, migration, and adhesive proprieties.
22887999	1	59	attach	present	189:195	arg1	microenvironments					212:228	most tissue microenvironments	200:228	most tissue microenvironments	200:228	Hyaluronan (HA) is a glycosaminoglycan present in most tissue microenvironments that can modulate many cell behaviors, including proliferation, migration, and adhesive proprieties.
22887999	4	60	theme	chondroitin	820:830	arg1	synthesis					840:848	chondroitin sulfate synthesis	820:848	chondroitin sulfate synthesis	820:848	Therefore, we analyzed the effect of UDP-GlcNAc availability and protein glycosylation with O-linked N-acetylglucosamine (O-GlcNAcylation) on HA and chondroitin sulfate synthesis in primary human aortic smooth muscle cells.
22887999	4	61	link	O-linked	763:770	arg1	O-GlcNAcylation					793:807	O-GlcNAcylation	793:807	O-GlcNAcylation	793:807	Therefore, we analyzed the effect of UDP-GlcNAc availability and protein glycosylation with O-linked N-acetylglucosamine (O-GlcNAcylation) on HA and chondroitin sulfate synthesis in primary human aortic smooth muscle cells.
22887999	4	61	link	O-linked	763:770	arg1	N-acetylglucosamine					772:790	O-linked N-acetylglucosamine	763:790	O-linked N-acetylglucosamine (O-GlcNAcylation)	763:808	Therefore, we analyzed the effect of UDP-GlcNAc availability and protein glycosylation with O-linked N-acetylglucosamine (O-GlcNAcylation) on HA and chondroitin sulfate synthesis in primary human aortic smooth muscle cells.
22887999	1	62	theme	adhesive	309:316	arg1	proprieties					318:328	adhesive proprieties	309:328	adhesive proprieties	309:328	Hyaluronan (HA) is a glycosaminoglycan present in most tissue microenvironments that can modulate many cell behaviors, including proliferation, migration, and adhesive proprieties.
22887999	2	63	theme	cytoplasmic	512:522	arg1	substrates					575:584	substrates	575:584	substrates	575:584	In contrast with other glycosaminoglycans, which are synthesized in the Golgi, HA is synthesized at the plasma membrane by one or more of the three HA synthases (HAS1-3), which use cytoplasmic UDP-glucuronic acid and UDP-N-acetylglucosamine as substrates.
22887999	2	63	theme	cytoplasmic	512:522	arg1	UDP-N-acetylglucosamine					548:570	UDP-N-acetylglucosamine	548:570	UDP-N-acetylglucosamine	548:570	In contrast with other glycosaminoglycans, which are synthesized in the Golgi, HA is synthesized at the plasma membrane by one or more of the three HA synthases (HAS1-3), which use cytoplasmic UDP-glucuronic acid and UDP-N-acetylglucosamine as substrates.
22887999	2	63	theme	cytoplasmic	512:522	arg1	acid					539:542	cytoplasmic UDP-glucuronic acid	512:542	cytoplasmic UDP-glucuronic acid	512:542	In contrast with other glycosaminoglycans, which are synthesized in the Golgi, HA is synthesized at the plasma membrane by one or more of the three HA synthases (HAS1-3), which use cytoplasmic UDP-glucuronic acid and UDP-N-acetylglucosamine as substrates.
22887999	7	64	theme	t	1405:1405	arg1	h					1420:1420	t(&frac12;) >5 h	1405:1420	t(&frac12;) >5 h	1405:1420	We found that HAS2, the main synthase in aortic smooth muscle cells, can be O-GlcNAcylated on serine 221, which strongly increased its activity and its stability (t(&frac12;) >5 h versus ∼17 min without O-GlcNAcylation).
22887999	7	64	theme	t	1405:1405	arg1	&frac12					1407:1413	&frac12;	1407:1414	&frac12;	1407:1414	We found that HAS2, the main synthase in aortic smooth muscle cells, can be O-GlcNAcylated on serine 221, which strongly increased its activity and its stability (t(&frac12;) >5 h versus ∼17 min without O-GlcNAcylation).
22887999	5	65	theme	HA	1015:1016	arg1	synthesis					997:1005	synthesis	997:1005	synthesis of both HA and chondroitin sulfate	997:1040	Glucosamine treatment, which increases UDP-GlcNAc availability and protein O-GlcNAcylation, increased synthesis of both HA and chondroitin sulfate.
22887999	1	66	from	present	189:195	arg1	microenvironments					212:228	most tissue microenvironments	200:228	most tissue microenvironments	200:228	Hyaluronan (HA) is a glycosaminoglycan present in most tissue microenvironments that can modulate many cell behaviors, including proliferation, migration, and adhesive proprieties.
22887999	5	67	theme	UDP-GlcNAc	934:943	arg1	availability					945:956	UDP-GlcNAc availability	934:956	UDP-GlcNAc availability	934:956	Glucosamine treatment, which increases UDP-GlcNAc availability and protein O-GlcNAcylation, increased synthesis of both HA and chondroitin sulfate.
22887999	4	68	from	effect	698:703	arg1	synthesis					840:848	chondroitin sulfate synthesis	820:848	chondroitin sulfate synthesis	820:848	Therefore, we analyzed the effect of UDP-GlcNAc availability and protein glycosylation with O-linked N-acetylglucosamine (O-GlcNAcylation) on HA and chondroitin sulfate synthesis in primary human aortic smooth muscle cells.
22887999	4	68	from	effect	698:703	arg1	HA					813:814	HA	813:814	HA	813:814	Therefore, we analyzed the effect of UDP-GlcNAc availability and protein glycosylation with O-linked N-acetylglucosamine (O-GlcNAcylation) on HA and chondroitin sulfate synthesis in primary human aortic smooth muscle cells.
22887999	1	69	theme	tissue	205:210	arg1	microenvironments					212:228	most tissue microenvironments	200:228	most tissue microenvironments	200:228	Hyaluronan (HA) is a glycosaminoglycan present in most tissue microenvironments that can modulate many cell behaviors, including proliferation, migration, and adhesive proprieties.
22887999	1	70	from	microenvironments	212:228	arg1	present					189:195	present	189:195	present	189:195	Hyaluronan (HA) is a glycosaminoglycan present in most tissue microenvironments that can modulate many cell behaviors, including proliferation, migration, and adhesive proprieties.
22887999	8	71	dep	GlcN	1575:1578	arg1	the					1559:1561	the	1559:1561	the	1559:1561	S221A mutation prevented HAS2 O-GlcNAcylation, which maintained the rapid turnover rate even in the presence of GlcN and increased UDP-GlcNAc.
22887999	8	71	dep	GlcN	1575:1578	arg1	presence					1563:1570	presence	1563:1570	presence	1563:1570	S221A mutation prevented HAS2 O-GlcNAcylation, which maintained the rapid turnover rate even in the presence of GlcN and increased UDP-GlcNAc.
22887999	9	72	from	pathologies	1770:1780	arg1	critical					1749:1756	critical	1749:1756	critical	1749:1756	These findings could explain the elevated matrix HA observed in diabetic vessels that, in turn, could mediate cell dedifferentiation processes critical in vascular pathologies.
22887999	0	73	theme	hyaluronan	64:73	arg1	synthase					75:82	hyaluronan synthase 2	64:84	hyaluronan synthase 2	64:84	Role of UDP-N-acetylglucosamine (GlcNAc) and O-GlcNAcylation of hyaluronan synthase 2 in the control of chondroitin sulfate and hyaluronan synthesis.
22887999	6	74	with	stimulation	1082:1092	arg1	amino-N-phenylcarbamate					1144:1166	O-(2-acetamido-2-deoxy-d-glucopyranosylidene)amino-N-phenylcarbamate	1099:1166	O-(2-acetamido-2-deoxy-d-glucopyranosylidene)amino-N-phenylcarbamate	1099:1166	However, increasing O-GlcNAcylation by stimulation with O-(2-acetamido-2-deoxy-d-glucopyranosylidene)amino-N-phenylcarbamate without a concomitant increase of UDP-GlcNAc increased only HA synthesis.
22887999	5	75	theme	chondroitin	1022:1032	arg1	sulfate					1034:1040	chondroitin sulfate	1022:1040	chondroitin sulfate	1022:1040	Glucosamine treatment, which increases UDP-GlcNAc availability and protein O-GlcNAcylation, increased synthesis of both HA and chondroitin sulfate.
22887999	9	76	theme	matrix	1648:1653	arg1	HA					1655:1656	the elevated matrix HA	1635:1656	the elevated matrix HA observed in diabetic vessels that, in turn, could mediate cell dedifferentiation processes critical in vascular pathologies	1635:1780	These findings could explain the elevated matrix HA observed in diabetic vessels that, in turn, could mediate cell dedifferentiation processes critical in vascular pathologies.
22887999	6	77	theme	concomitant	1178:1188	arg1	increase					1190:1197	a concomitant increase	1176:1197	a concomitant increase of UDP-GlcNAc	1176:1211	However, increasing O-GlcNAcylation by stimulation with O-(2-acetamido-2-deoxy-d-glucopyranosylidene)amino-N-phenylcarbamate without a concomitant increase of UDP-GlcNAc increased only HA synthesis.
22887999	9	78	from	critical	1749:1756	arg1	pathologies					1770:1780	vascular pathologies	1761:1780	vascular pathologies	1761:1780	These findings could explain the elevated matrix HA observed in diabetic vessels that, in turn, could mediate cell dedifferentiation processes critical in vascular pathologies.
22887999	7	79	theme	muscle	1297:1302	arg1	cells					1304:1308	aortic smooth muscle cells	1283:1308	aortic smooth muscle cells	1283:1308	We found that HAS2, the main synthase in aortic smooth muscle cells, can be O-GlcNAcylated on serine 221, which strongly increased its activity and its stability (t(&frac12;) >5 h versus ∼17 min without O-GlcNAcylation).
22887999	8	80	theme	rapid	1531:1535	arg1	rate					1546:1549	the rapid turnover rate	1527:1549	the rapid turnover rate	1527:1549	S221A mutation prevented HAS2 O-GlcNAcylation, which maintained the rapid turnover rate even in the presence of GlcN and increased UDP-GlcNAc.
22887999	3	81	theme	Previous	587:594	arg1	studies					596:602	Previous studies	587:602	Previous studies	587:602	Previous studies revealed the importance of UDP-sugars for regulating HA synthesis.
22887999	5	82	theme	Glucosamine	895:905	arg1	treatment					907:915	Glucosamine treatment	895:915	Glucosamine treatment	895:915	Glucosamine treatment, which increases UDP-GlcNAc availability and protein O-GlcNAcylation, increased synthesis of both HA and chondroitin sulfate.
22887999	9	83	theme	cell	1716:1719	arg1	processes					1739:1747	cell dedifferentiation processes	1716:1747	cell dedifferentiation processes critical in vascular pathologies	1716:1780	These findings could explain the elevated matrix HA observed in diabetic vessels that, in turn, could mediate cell dedifferentiation processes critical in vascular pathologies.
29133780	4	0	theme	genotoxic	646:654	arg1	stimuli					689:695	genotoxic, oxidative, and metabolic stress stimuli	646:695	genotoxic, oxidative, and metabolic stress stimuli in cellular and mouse models	646:724	The O-GlcNAcylation of SIRT1 is elevated during genotoxic, oxidative, and metabolic stress stimuli in cellular and mouse models, thereby increasing SIRT1 deacetylase activity and protecting cells from stress-induced apoptosis.
29133780	1	1	theme	genome	240:245	arg1	stability					247:255	genome stability	240:255	genome stability	240:255	SIRT1 is the most evolutionarily conserved mammalian sirtuin, and it plays a vital role in the regulation of metabolism, stress responses, genome stability, and ageing.
29133780	4	2	theme	mouse	713:717	arg1	models					719:724	cellular and mouse models	700:724	models	719:724	The O-GlcNAcylation of SIRT1 is elevated during genotoxic, oxidative, and metabolic stress stimuli in cellular and mouse models, thereby increasing SIRT1 deacetylase activity and protecting cells from stress-induced apoptosis.
29133780	1	3	theme	stability	247:255	arg1	regulation					196:205	the regulation	192:205	the regulation of metabolism, stress responses, genome stability, and ageing	192:267	SIRT1 is the most evolutionarily conserved mammalian sirtuin, and it plays a vital role in the regulation of metabolism, stress responses, genome stability, and ageing.
29133780	5	4	theme	novel	932:936	arg1	target					960:965	a novel potential therapeutic target	930:965	a novel potential therapeutic target for preventing age-related diseases and extending healthspan	930:1026	Our findings demonstrate a new mechanism for the activation of SIRT1 under stress conditions and suggest a novel potential therapeutic target for preventing age-related diseases and extending healthspan.
29133780	3	5	theme	carboxy-terminal	496:511	arg1	region					513:518	its carboxy-terminal region	492:518	its carboxy-terminal region	492:518	Here, we show that SIRT1 is dynamically modified with O-GlcNAc at Ser 549 in its carboxy-terminal region, which directly increases its deacetylase activity both in vitro and in vivo.
29133780	1	6	theme	mammalian	144:152	arg1	SIRT1					101:105	SIRT1	101:105	SIRT1	101:105	SIRT1 is the most evolutionarily conserved mammalian sirtuin, and it plays a vital role in the regulation of metabolism, stress responses, genome stability, and ageing.
29133780	1	6	theme	mammalian	144:152	arg1	sirtuin					154:160	the most evolutionarily conserved mammalian sirtuin	110:160	the most evolutionarily conserved mammalian sirtuin	110:160	SIRT1 is the most evolutionarily conserved mammalian sirtuin, and it plays a vital role in the regulation of metabolism, stress responses, genome stability, and ageing.
29133780	4	7	from	apoptosis	814:822	arg1	cells					788:792	cells	788:792	cells from stress-induced apoptosis	788:822	The O-GlcNAcylation of SIRT1 is elevated during genotoxic, oxidative, and metabolic stress stimuli in cellular and mouse models, thereby increasing SIRT1 deacetylase activity and protecting cells from stress-induced apoptosis.
29133780	4	8	theme	stress-induced	799:812	arg1	apoptosis					814:822	stress-induced apoptosis	799:822	stress-induced apoptosis	799:822	The O-GlcNAcylation of SIRT1 is elevated during genotoxic, oxidative, and metabolic stress stimuli in cellular and mouse models, thereby increasing SIRT1 deacetylase activity and protecting cells from stress-induced apoptosis.
29133780	5	9	theme	potential	938:946	arg1	target					960:965	a novel potential therapeutic target	930:965	a novel potential therapeutic target for preventing age-related diseases and extending healthspan	930:1026	Our findings demonstrate a new mechanism for the activation of SIRT1 under stress conditions and suggest a novel potential therapeutic target for preventing age-related diseases and extending healthspan.
29133780	5	10	theme	SIRT1	888:892	arg1	activation					874:883	the activation	870:883	the activation of SIRT1 under stress conditions	870:916	Our findings demonstrate a new mechanism for the activation of SIRT1 under stress conditions and suggest a novel potential therapeutic target for preventing age-related diseases and extending healthspan.
29133780	2	11	theme	molecular	369:377	arg1	clear					408:412	clear	408:412	clear	408:412	As a stress sensor, SIRT1 deacetylase activity is significantly increased during stresses, but the molecular mechanisms are not yet fully clear.
29133780	2	11	theme	molecular	369:377	arg1	mechanisms					379:388	the molecular mechanisms	365:388	the molecular mechanisms	365:388	As a stress sensor, SIRT1 deacetylase activity is significantly increased during stresses, but the molecular mechanisms are not yet fully clear.
29133780	5	12	theme	stress	900:905	arg1	conditions					907:916	stress conditions	900:916	stress conditions	900:916	Our findings demonstrate a new mechanism for the activation of SIRT1 under stress conditions and suggest a novel potential therapeutic target for preventing age-related diseases and extending healthspan.
29133780	1	13	theme	vital	178:182	arg1	role					184:187	a vital role	176:187	a vital role	176:187	SIRT1 is the most evolutionarily conserved mammalian sirtuin, and it plays a vital role in the regulation of metabolism, stress responses, genome stability, and ageing.
29133780	4	14	from	stimuli	689:695	arg1	models					719:724	cellular and mouse models	700:724	models	719:724	The O-GlcNAcylation of SIRT1 is elevated during genotoxic, oxidative, and metabolic stress stimuli in cellular and mouse models, thereby increasing SIRT1 deacetylase activity and protecting cells from stress-induced apoptosis.
29133780	4	15	theme	stress	682:687	arg1	stimuli					689:695	genotoxic, oxidative, and metabolic stress stimuli	646:695	genotoxic, oxidative, and metabolic stress stimuli in cellular and mouse models	646:724	The O-GlcNAcylation of SIRT1 is elevated during genotoxic, oxidative, and metabolic stress stimuli in cellular and mouse models, thereby increasing SIRT1 deacetylase activity and protecting cells from stress-induced apoptosis.
29133780	4	16	theme	SIRT1	621:625	arg1	O-GlcNAcylation					602:616	The O-GlcNAcylation	598:616	The O-GlcNAcylation of SIRT1	598:625	The O-GlcNAcylation of SIRT1 is elevated during genotoxic, oxidative, and metabolic stress stimuli in cellular and mouse models, thereby increasing SIRT1 deacetylase activity and protecting cells from stress-induced apoptosis.
29133780	1	17	theme	ageing	262:267	arg1	regulation					196:205	the regulation	192:205	the regulation of metabolism, stress responses, genome stability, and ageing	192:267	SIRT1 is the most evolutionarily conserved mammalian sirtuin, and it plays a vital role in the regulation of metabolism, stress responses, genome stability, and ageing.
29133780	2	18	theme	stress	275:280	arg1	activity					308:315	SIRT1 deacetylase activity	290:315	SIRT1 deacetylase activity	290:315	As a stress sensor, SIRT1 deacetylase activity is significantly increased during stresses, but the molecular mechanisms are not yet fully clear.
29133780	2	18	theme	stress	275:280	arg1	sensor					282:287	a stress sensor	273:287	a stress sensor	273:287	As a stress sensor, SIRT1 deacetylase activity is significantly increased during stresses, but the molecular mechanisms are not yet fully clear.
29133780	0	19	theme	SIRT1	19:23	arg1	O-GlcNAcylation					0:14	O-GlcNAcylation	0:14	O-GlcNAcylation of SIRT1	0:23	O-GlcNAcylation of SIRT1 enhances its deacetylase activity and promotes cytoprotection under stress.
29133780	0	20	theme	deacetylase	38:48	arg1	activity					50:57	its deacetylase activity	34:57	its deacetylase activity	34:57	O-GlcNAcylation of SIRT1 enhances its deacetylase activity and promotes cytoprotection under stress.
29133780	3	21	theme	deacetylase	550:560	arg1	activity					562:569	its deacetylase activity	546:569	its deacetylase activity	546:569	Here, we show that SIRT1 is dynamically modified with O-GlcNAc at Ser 549 in its carboxy-terminal region, which directly increases its deacetylase activity both in vitro and in vivo.
29133780	3	22	mod	modified	455:462	arg1	SIRT1					434:438	SIRT1	434:438	SIRT1	434:438	Here, we show that SIRT1 is dynamically modified with O-GlcNAc at Ser 549 in its carboxy-terminal region, which directly increases its deacetylase activity both in vitro and in vivo.
29133780	3	22	mod	modified	455:462	arg3	O-GlcNAc					469:476	O-GlcNAc	469:476	O-GlcNAc	469:476	Here, we show that SIRT1 is dynamically modified with O-GlcNAc at Ser 549 in its carboxy-terminal region, which directly increases its deacetylase activity both in vitro and in vivo.
29133780	5	23	dep	potential	938:946	arg1	therapeutic					948:958	therapeutic	948:958	therapeutic	948:958	Our findings demonstrate a new mechanism for the activation of SIRT1 under stress conditions and suggest a novel potential therapeutic target for preventing age-related diseases and extending healthspan.
29133780	4	24	theme	oxidative	657:665	arg1	stimuli					689:695	genotoxic, oxidative, and metabolic stress stimuli	646:695	genotoxic, oxidative, and metabolic stress stimuli in cellular and mouse models	646:724	The O-GlcNAcylation of SIRT1 is elevated during genotoxic, oxidative, and metabolic stress stimuli in cellular and mouse models, thereby increasing SIRT1 deacetylase activity and protecting cells from stress-induced apoptosis.
29133780	5	25	theme	age-related	982:992	arg1	diseases					994:1001	age-related diseases	982:1001	age-related diseases	982:1001	Our findings demonstrate a new mechanism for the activation of SIRT1 under stress conditions and suggest a novel potential therapeutic target for preventing age-related diseases and extending healthspan.
29133780	1	26	theme	conserved	134:142	arg1	SIRT1					101:105	SIRT1	101:105	SIRT1	101:105	SIRT1 is the most evolutionarily conserved mammalian sirtuin, and it plays a vital role in the regulation of metabolism, stress responses, genome stability, and ageing.
29133780	1	26	theme	conserved	134:142	arg1	sirtuin					154:160	the most evolutionarily conserved mammalian sirtuin	110:160	the most evolutionarily conserved mammalian sirtuin	110:160	SIRT1 is the most evolutionarily conserved mammalian sirtuin, and it plays a vital role in the regulation of metabolism, stress responses, genome stability, and ageing.
29133780	4	27	theme	cellular	700:707	arg1	models					719:724	cellular and mouse models	700:724	models	719:724	The O-GlcNAcylation of SIRT1 is elevated during genotoxic, oxidative, and metabolic stress stimuli in cellular and mouse models, thereby increasing SIRT1 deacetylase activity and protecting cells from stress-induced apoptosis.
29133780	1	28	theme	metabolism	210:219	arg1	regulation					196:205	the regulation	192:205	the regulation of metabolism, stress responses, genome stability, and ageing	192:267	SIRT1 is the most evolutionarily conserved mammalian sirtuin, and it plays a vital role in the regulation of metabolism, stress responses, genome stability, and ageing.
29133780	4	29	theme	metabolic	672:680	arg1	stimuli					689:695	genotoxic, oxidative, and metabolic stress stimuli	646:695	genotoxic, oxidative, and metabolic stress stimuli in cellular and mouse models	646:724	The O-GlcNAcylation of SIRT1 is elevated during genotoxic, oxidative, and metabolic stress stimuli in cellular and mouse models, thereby increasing SIRT1 deacetylase activity and protecting cells from stress-induced apoptosis.
29133780	2	30	theme	SIRT1	290:294	arg1	deacetylase					296:306	SIRT1 deacetylase	290:306	SIRT1 deacetylase activity	290:315	As a stress sensor, SIRT1 deacetylase activity is significantly increased during stresses, but the molecular mechanisms are not yet fully clear.
29133780	2	31	theme	deacetylase	296:306	arg1	activity					308:315	SIRT1 deacetylase activity	290:315	SIRT1 deacetylase activity	290:315	As a stress sensor, SIRT1 deacetylase activity is significantly increased during stresses, but the molecular mechanisms are not yet fully clear.
29133780	2	31	theme	deacetylase	296:306	arg1	sensor					282:287	a stress sensor	273:287	a stress sensor	273:287	As a stress sensor, SIRT1 deacetylase activity is significantly increased during stresses, but the molecular mechanisms are not yet fully clear.
29133780	4	32	theme	deacetylase	752:762	arg1	activity					764:771	SIRT1 deacetylase activity	746:771	SIRT1 deacetylase activity	746:771	The O-GlcNAcylation of SIRT1 is elevated during genotoxic, oxidative, and metabolic stress stimuli in cellular and mouse models, thereby increasing SIRT1 deacetylase activity and protecting cells from stress-induced apoptosis.
29133780	5	33	theme	new	852:854	arg1	mechanism					856:864	a new mechanism	850:864	a new mechanism for the activation of SIRT1 under stress conditions	850:916	Our findings demonstrate a new mechanism for the activation of SIRT1 under stress conditions and suggest a novel potential therapeutic target for preventing age-related diseases and extending healthspan.
29133780	1	34	theme	stress	222:227	arg1	responses					229:237	stress responses	222:237	stress responses	222:237	SIRT1 is the most evolutionarily conserved mammalian sirtuin, and it plays a vital role in the regulation of metabolism, stress responses, genome stability, and ageing.
29133780	4	35	theme	SIRT1	746:750	arg1	activity					764:771	SIRT1 deacetylase activity	746:771	SIRT1 deacetylase activity	746:771	The O-GlcNAcylation of SIRT1 is elevated during genotoxic, oxidative, and metabolic stress stimuli in cellular and mouse models, thereby increasing SIRT1 deacetylase activity and protecting cells from stress-induced apoptosis.
29133780	1	36	theme	responses	229:237	arg1	regulation					196:205	the regulation	192:205	the regulation of metabolism, stress responses, genome stability, and ageing	192:267	SIRT1 is the most evolutionarily conserved mammalian sirtuin, and it plays a vital role in the regulation of metabolism, stress responses, genome stability, and ageing.
31944090	1	0	theme	neurodegenerative	325:341	arg1	disease					343:349	the fatal neurodegenerative disease	315:349	the fatal neurodegenerative disease giant axonal neuropathy (GAN)	315:379	Mutations in human gigaxonin cause the fatal neurodegenerative disease giant axonal neuropathy (GAN), in which IF proteins accumulate and aggregate in axons throughout the nervous system, impairing neuronal function and viability.
31944090	0	1	theme	ligase	168:173	arg1	protein					183:189	an E3 ligase adaptor protein	162:189	an E3 ligase adaptor protein that promotes the ubiquitination and degradation of intermediate filament (IF) proteins	162:277	Gigaxonin glycosylation regulates intermediate filament turnover and may impact giant axonal neuropathy etiology or treatment Gigaxonin (also known as KLHL16) is an E3 ligase adaptor protein that promotes the ubiquitination and degradation of intermediate filament (IF) proteins.
31944090	0	1	theme	ligase	168:173	arg1	etiology					104:111	etiology	104:111	etiology	104:111	Gigaxonin glycosylation regulates intermediate filament turnover and may impact giant axonal neuropathy etiology or treatment Gigaxonin (also known as KLHL16) is an E3 ligase adaptor protein that promotes the ubiquitination and degradation of intermediate filament (IF) proteins.
31944090	0	1	theme	ligase	168:173	arg1	Gigaxonin					126:134	treatment Gigaxonin	116:134	treatment Gigaxonin	116:134	Gigaxonin glycosylation regulates intermediate filament turnover and may impact giant axonal neuropathy etiology or treatment Gigaxonin (also known as KLHL16) is an E3 ligase adaptor protein that promotes the ubiquitination and degradation of intermediate filament (IF) proteins.
31944090	1	2	from	aggregate	418:426	arg1	axons					431:435	axons	431:435	axons throughout the nervous system	431:465	Mutations in human gigaxonin cause the fatal neurodegenerative disease giant axonal neuropathy (GAN), in which IF proteins accumulate and aggregate in axons throughout the nervous system, impairing neuronal function and viability.
31944090	4	3	theme	sites	953:957	arg1	2					979:979	2	979:979	2	979:979	MS analyses of human gigaxonin revealed 9 candidate sites of O-GlcNAcylation, 2 of which — serine 272 and threonine 277 — are required for its ability to mediate IF turnover in gigaxonin-deficient human cell models that we created.
31944090	4	3	theme	sites	953:957	arg1	O-GlcNAcylation					962:976	O-GlcNAcylation	962:976	O-GlcNAcylation	962:976	MS analyses of human gigaxonin revealed 9 candidate sites of O-GlcNAcylation, 2 of which — serine 272 and threonine 277 — are required for its ability to mediate IF turnover in gigaxonin-deficient human cell models that we created.
31944090	4	3	theme	sites	953:957	arg1	sites					953:957	9 candidate sites	941:957	9 candidate sites	941:957	MS analyses of human gigaxonin revealed 9 candidate sites of O-GlcNAcylation, 2 of which — serine 272 and threonine 277 — are required for its ability to mediate IF turnover in gigaxonin-deficient human cell models that we created.
31944090	3	4	theme	factor–dependent	876:891	arg1	manner					893:898	a nutrient- and growth factor–dependent manner	853:898	a nutrient- and growth factor–dependent manner	853:898	Here, we report that gigaxonin is modified by <italic>O</italic>-linked β-<italic>N</italic>-acetylglucosamine (O-GlcNAc), a prevalent form of intracellular glycosylation, in a nutrient- and growth factor–dependent manner.
31944090	0	5	theme	axonal	86:91	arg1	neuropathy					93:102	giant axonal neuropathy	80:102	giant axonal neuropathy	80:102	Gigaxonin glycosylation regulates intermediate filament turnover and may impact giant axonal neuropathy etiology or treatment Gigaxonin (also known as KLHL16) is an E3 ligase adaptor protein that promotes the ubiquitination and degradation of intermediate filament (IF) proteins.
31944090	0	6	theme	E3	165:166	arg1	protein					183:189	an E3 ligase adaptor protein	162:189	an E3 ligase adaptor protein that promotes the ubiquitination and degradation of intermediate filament (IF) proteins	162:277	Gigaxonin glycosylation regulates intermediate filament turnover and may impact giant axonal neuropathy etiology or treatment Gigaxonin (also known as KLHL16) is an E3 ligase adaptor protein that promotes the ubiquitination and degradation of intermediate filament (IF) proteins.
31944090	0	6	theme	E3	165:166	arg1	etiology					104:111	etiology	104:111	etiology	104:111	Gigaxonin glycosylation regulates intermediate filament turnover and may impact giant axonal neuropathy etiology or treatment Gigaxonin (also known as KLHL16) is an E3 ligase adaptor protein that promotes the ubiquitination and degradation of intermediate filament (IF) proteins.
31944090	0	6	theme	E3	165:166	arg1	Gigaxonin					126:134	treatment Gigaxonin	116:134	treatment Gigaxonin	116:134	Gigaxonin glycosylation regulates intermediate filament turnover and may impact giant axonal neuropathy etiology or treatment Gigaxonin (also known as KLHL16) is an E3 ligase adaptor protein that promotes the ubiquitination and degradation of intermediate filament (IF) proteins.
31944090	4	7	theme	cell	1104:1107	arg1	models					1109:1114	gigaxonin-deficient human cell models	1078:1114	gigaxonin-deficient human cell models that we created	1078:1130	MS analyses of human gigaxonin revealed 9 candidate sites of O-GlcNAcylation, 2 of which — serine 272 and threonine 277 — are required for its ability to mediate IF turnover in gigaxonin-deficient human cell models that we created.
31944090	4	8	theme	gigaxonin	922:930	arg1	analyses					904:911	MS analyses	901:911	MS analyses of human gigaxonin	901:930	MS analyses of human gigaxonin revealed 9 candidate sites of O-GlcNAcylation, 2 of which — serine 272 and threonine 277 — are required for its ability to mediate IF turnover in gigaxonin-deficient human cell models that we created.
31944090	0	9	theme	proteins	270:277	arg1	degradation					228:238	degradation	228:238	degradation	228:238	Gigaxonin glycosylation regulates intermediate filament turnover and may impact giant axonal neuropathy etiology or treatment Gigaxonin (also known as KLHL16) is an E3 ligase adaptor protein that promotes the ubiquitination and degradation of intermediate filament (IF) proteins.
31944090	0	9	theme	proteins	270:277	arg1	ubiquitination					209:222	ubiquitination	209:222	ubiquitination	209:222	Gigaxonin glycosylation regulates intermediate filament turnover and may impact giant axonal neuropathy etiology or treatment Gigaxonin (also known as KLHL16) is an E3 ligase adaptor protein that promotes the ubiquitination and degradation of intermediate filament (IF) proteins.
31944090	0	10	theme	filament	256:263	arg1	proteins					270:277	intermediate filament (IF) proteins	243:277	intermediate filament (IF) proteins	243:277	Gigaxonin glycosylation regulates intermediate filament turnover and may impact giant axonal neuropathy etiology or treatment Gigaxonin (also known as KLHL16) is an E3 ligase adaptor protein that promotes the ubiquitination and degradation of intermediate filament (IF) proteins.
31944090	4	11	theme	human	1098:1102	arg1	models					1109:1114	gigaxonin-deficient human cell models	1078:1114	gigaxonin-deficient human cell models that we created	1078:1130	MS analyses of human gigaxonin revealed 9 candidate sites of O-GlcNAcylation, 2 of which — serine 272 and threonine 277 — are required for its ability to mediate IF turnover in gigaxonin-deficient human cell models that we created.
31944090	4	12	theme	—	990:990	arg1	—					1021:1021	— serine 272 and threonine 277 —	990:1021	— serine 272 and threonine 277 —	990:1021	MS analyses of human gigaxonin revealed 9 candidate sites of O-GlcNAcylation, 2 of which — serine 272 and threonine 277 — are required for its ability to mediate IF turnover in gigaxonin-deficient human cell models that we created.
31944090	1	13	theme	axonal	357:362	arg1	neuropathy					364:373	giant axonal neuropathy	351:373	the fatal neurodegenerative disease giant axonal neuropathy (GAN)	315:379	Mutations in human gigaxonin cause the fatal neurodegenerative disease giant axonal neuropathy (GAN), in which IF proteins accumulate and aggregate in axons throughout the nervous system, impairing neuronal function and viability.
31944090	1	13	theme	axonal	357:362	arg1	GAN					376:378	GAN	376:378	GAN	376:378	Mutations in human gigaxonin cause the fatal neurodegenerative disease giant axonal neuropathy (GAN), in which IF proteins accumulate and aggregate in axons throughout the nervous system, impairing neuronal function and viability.
31944090	0	14	theme	adaptor	175:181	arg1	protein					183:189	an E3 ligase adaptor protein	162:189	an E3 ligase adaptor protein that promotes the ubiquitination and degradation of intermediate filament (IF) proteins	162:277	Gigaxonin glycosylation regulates intermediate filament turnover and may impact giant axonal neuropathy etiology or treatment Gigaxonin (also known as KLHL16) is an E3 ligase adaptor protein that promotes the ubiquitination and degradation of intermediate filament (IF) proteins.
31944090	0	14	theme	adaptor	175:181	arg1	etiology					104:111	etiology	104:111	etiology	104:111	Gigaxonin glycosylation regulates intermediate filament turnover and may impact giant axonal neuropathy etiology or treatment Gigaxonin (also known as KLHL16) is an E3 ligase adaptor protein that promotes the ubiquitination and degradation of intermediate filament (IF) proteins.
31944090	0	14	theme	adaptor	175:181	arg1	Gigaxonin					126:134	treatment Gigaxonin	116:134	treatment Gigaxonin	116:134	Gigaxonin glycosylation regulates intermediate filament turnover and may impact giant axonal neuropathy etiology or treatment Gigaxonin (also known as KLHL16) is an E3 ligase adaptor protein that promotes the ubiquitination and degradation of intermediate filament (IF) proteins.
31944090	0	15	theme	intermediate	243:254	arg1	filament					256:263	intermediate filament	243:263	intermediate filament (IF) proteins	243:277	Gigaxonin glycosylation regulates intermediate filament turnover and may impact giant axonal neuropathy etiology or treatment Gigaxonin (also known as KLHL16) is an E3 ligase adaptor protein that promotes the ubiquitination and degradation of intermediate filament (IF) proteins.
31944090	3	16	link	<italic>O</italic>-linked	724:748	arg1	β-<italic>N</italic>-acetylglucosamine					750:787	<italic>O</italic>-linked β-<italic>N</italic>-acetylglucosamine	724:787	<italic>O</italic>-linked β-<italic>N</italic>-acetylglucosamine (O-GlcNAc)	724:798	Here, we report that gigaxonin is modified by <italic>O</italic>-linked β-<italic>N</italic>-acetylglucosamine (O-GlcNAc), a prevalent form of intracellular glycosylation, in a nutrient- and growth factor–dependent manner.
31944090	3	16	link	<italic>O</italic>-linked	724:748	arg1	form					813:816	a prevalent form	801:816	a prevalent form of intracellular glycosylation	801:847	Here, we report that gigaxonin is modified by <italic>O</italic>-linked β-<italic>N</italic>-acetylglucosamine (O-GlcNAc), a prevalent form of intracellular glycosylation, in a nutrient- and growth factor–dependent manner.
31944090	3	16	link	<italic>O</italic>-linked	724:748	arg1	O-GlcNAc					790:797	O-GlcNAc	790:797	O-GlcNAc	790:797	Here, we report that gigaxonin is modified by <italic>O</italic>-linked β-<italic>N</italic>-acetylglucosamine (O-GlcNAc), a prevalent form of intracellular glycosylation, in a nutrient- and growth factor–dependent manner.
31944090	3	17	theme	intracellular	821:833	arg1	glycosylation					835:847	intracellular glycosylation	821:847	intracellular glycosylation	821:847	Here, we report that gigaxonin is modified by <italic>O</italic>-linked β-<italic>N</italic>-acetylglucosamine (O-GlcNAc), a prevalent form of intracellular glycosylation, in a nutrient- and growth factor–dependent manner.
31944090	6	18	theme	GAN	1373:1375	arg1	phenotypes					1377:1386	GAN phenotypes	1373:1386	GAN phenotypes	1373:1386	Our work may have significant implications for understanding the nongenetic modifiers of GAN phenotypes and for the optimization of gene therapy for this disease.
31944090	1	19	from	Mutations	280:288	arg1	gigaxonin					299:307	human gigaxonin	293:307	human gigaxonin	293:307	Mutations in human gigaxonin cause the fatal neurodegenerative disease giant axonal neuropathy (GAN), in which IF proteins accumulate and aggregate in axons throughout the nervous system, impairing neuronal function and viability.
31944090	3	20	theme	nutrient-	855:863	arg1	manner					893:898	a nutrient- and growth factor–dependent manner	853:898	a nutrient- and growth factor–dependent manner	853:898	Here, we report that gigaxonin is modified by <italic>O</italic>-linked β-<italic>N</italic>-acetylglucosamine (O-GlcNAc), a prevalent form of intracellular glycosylation, in a nutrient- and growth factor–dependent manner.
31944090	0	21	dep	ubiquitination	209:222	arg1	the					205:207	the	205:207	the	205:207	Gigaxonin glycosylation regulates intermediate filament turnover and may impact giant axonal neuropathy etiology or treatment Gigaxonin (also known as KLHL16) is an E3 ligase adaptor protein that promotes the ubiquitination and degradation of intermediate filament (IF) proteins.
31944090	0	22	theme	treatment	116:124	arg1	protein					183:189	an E3 ligase adaptor protein	162:189	an E3 ligase adaptor protein that promotes the ubiquitination and degradation of intermediate filament (IF) proteins	162:277	Gigaxonin glycosylation regulates intermediate filament turnover and may impact giant axonal neuropathy etiology or treatment Gigaxonin (also known as KLHL16) is an E3 ligase adaptor protein that promotes the ubiquitination and degradation of intermediate filament (IF) proteins.
31944090	0	22	theme	treatment	116:124	arg1	etiology					104:111	etiology	104:111	etiology	104:111	Gigaxonin glycosylation regulates intermediate filament turnover and may impact giant axonal neuropathy etiology or treatment Gigaxonin (also known as KLHL16) is an E3 ligase adaptor protein that promotes the ubiquitination and degradation of intermediate filament (IF) proteins.
31944090	0	22	theme	treatment	116:124	arg1	Gigaxonin					126:134	treatment Gigaxonin	116:134	treatment Gigaxonin	116:134	Gigaxonin glycosylation regulates intermediate filament turnover and may impact giant axonal neuropathy etiology or treatment Gigaxonin (also known as KLHL16) is an E3 ligase adaptor protein that promotes the ubiquitination and degradation of intermediate filament (IF) proteins.
31944090	3	23	theme	<italic>O</italic>-linked	724:748	arg1	β-<italic>N</italic>-acetylglucosamine					750:787	<italic>O</italic>-linked β-<italic>N</italic>-acetylglucosamine	724:787	<italic>O</italic>-linked β-<italic>N</italic>-acetylglucosamine (O-GlcNAc)	724:798	Here, we report that gigaxonin is modified by <italic>O</italic>-linked β-<italic>N</italic>-acetylglucosamine (O-GlcNAc), a prevalent form of intracellular glycosylation, in a nutrient- and growth factor–dependent manner.
31944090	3	23	theme	<italic>O</italic>-linked	724:748	arg1	form					813:816	a prevalent form	801:816	a prevalent form of intracellular glycosylation	801:847	Here, we report that gigaxonin is modified by <italic>O</italic>-linked β-<italic>N</italic>-acetylglucosamine (O-GlcNAc), a prevalent form of intracellular glycosylation, in a nutrient- and growth factor–dependent manner.
31944090	3	23	theme	<italic>O</italic>-linked	724:748	arg1	O-GlcNAc					790:797	O-GlcNAc	790:797	O-GlcNAc	790:797	Here, we report that gigaxonin is modified by <italic>O</italic>-linked β-<italic>N</italic>-acetylglucosamine (O-GlcNAc), a prevalent form of intracellular glycosylation, in a nutrient- and growth factor–dependent manner.
31944090	2	24	theme	function	637:644	arg1	regulation					570:579	upstream regulation	561:579	upstream regulation	561:579	Despite this pathophysiological significance, the upstream regulation and downstream effects of normal and aberrant gigaxonin function remain incompletely understood.
31944090	2	24	theme	function	637:644	arg1	effects					596:602	downstream effects	585:602	downstream effects	585:602	Despite this pathophysiological significance, the upstream regulation and downstream effects of normal and aberrant gigaxonin function remain incompletely understood.
31944090	0	25	dep	etiology	104:111	arg1	known					142:146	known	142:146	known as KLHL16	142:156	Gigaxonin glycosylation regulates intermediate filament turnover and may impact giant axonal neuropathy etiology or treatment Gigaxonin (also known as KLHL16) is an E3 ligase adaptor protein that promotes the ubiquitination and degradation of intermediate filament (IF) proteins.
31944090	6	26	theme	therapy	1421:1427	arg1	optimization					1400:1411	the optimization	1396:1411	the optimization of gene therapy for this disease	1396:1444	Our work may have significant implications for understanding the nongenetic modifiers of GAN phenotypes and for the optimization of gene therapy for this disease.
31944090	2	27	theme	gigaxonin	627:635	arg1	function					637:644	normal and aberrant gigaxonin function	607:644	normal and aberrant gigaxonin function	607:644	Despite this pathophysiological significance, the upstream regulation and downstream effects of normal and aberrant gigaxonin function remain incompletely understood.
31944090	1	28	theme	nervous	452:458	arg1	system					460:465	the nervous system	448:465	the nervous system	448:465	Mutations in human gigaxonin cause the fatal neurodegenerative disease giant axonal neuropathy (GAN), in which IF proteins accumulate and aggregate in axons throughout the nervous system, impairing neuronal function and viability.
31944090	4	29	theme	serine	992:997	arg1	—					1021:1021	— serine 272 and threonine 277 —	990:1021	— serine 272 and threonine 277 —	990:1021	MS analyses of human gigaxonin revealed 9 candidate sites of O-GlcNAcylation, 2 of which — serine 272 and threonine 277 — are required for its ability to mediate IF turnover in gigaxonin-deficient human cell models that we created.
31944090	6	30	theme	phenotypes	1377:1386	arg1	modifiers					1360:1368	the nongenetic modifiers	1345:1368	the nongenetic modifiers of GAN phenotypes	1345:1386	Our work may have significant implications for understanding the nongenetic modifiers of GAN phenotypes and for the optimization of gene therapy for this disease.
31944090	0	31	theme	Gigaxonin	0:8	arg1	glycosylation					10:22	Gigaxonin glycosylation	0:22	Gigaxonin glycosylation	0:22	Gigaxonin glycosylation regulates intermediate filament turnover and may impact giant axonal neuropathy etiology or treatment Gigaxonin (also known as KLHL16) is an E3 ligase adaptor protein that promotes the ubiquitination and degradation of intermediate filament (IF) proteins.
31944090	1	32	dep	disease	343:349	arg1	neuropathy					364:373	giant axonal neuropathy	351:373	the fatal neurodegenerative disease giant axonal neuropathy (GAN)	315:379	Mutations in human gigaxonin cause the fatal neurodegenerative disease giant axonal neuropathy (GAN), in which IF proteins accumulate and aggregate in axons throughout the nervous system, impairing neuronal function and viability.
31944090	1	32	dep	disease	343:349	arg1	GAN					376:378	GAN	376:378	GAN	376:378	Mutations in human gigaxonin cause the fatal neurodegenerative disease giant axonal neuropathy (GAN), in which IF proteins accumulate and aggregate in axons throughout the nervous system, impairing neuronal function and viability.
31944090	2	33	theme	aberrant	618:625	arg1	function					637:644	normal and aberrant gigaxonin function	607:644	normal and aberrant gigaxonin function	607:644	Despite this pathophysiological significance, the upstream regulation and downstream effects of normal and aberrant gigaxonin function remain incompletely understood.
31944090	4	34	theme	MS	901:902	arg1	analyses					904:911	MS analyses	901:911	MS analyses of human gigaxonin	901:930	MS analyses of human gigaxonin revealed 9 candidate sites of O-GlcNAcylation, 2 of which — serine 272 and threonine 277 — are required for its ability to mediate IF turnover in gigaxonin-deficient human cell models that we created.
31944090	6	35	contain	have	1297:1300	arg1	work					1288:1291	Our work	1284:1291	Our work	1284:1291	Our work may have significant implications for understanding the nongenetic modifiers of GAN phenotypes and for the optimization of gene therapy for this disease.
31944090	6	35	contain	have	1297:1300	arg2	implications					1314:1325	significant implications	1302:1325	significant implications for understanding the nongenetic modifiers of GAN phenotypes and for the optimization of gene therapy for this disease	1302:1444	Our work may have significant implications for understanding the nongenetic modifiers of GAN phenotypes and for the optimization of gene therapy for this disease.
31944090	2	36	theme	normal	607:612	arg1	function					637:644	normal and aberrant gigaxonin function	607:644	normal and aberrant gigaxonin function	607:644	Despite this pathophysiological significance, the upstream regulation and downstream effects of normal and aberrant gigaxonin function remain incompletely understood.
31944090	0	37	theme	intermediate	34:45	arg1	turnover					56:63	intermediate filament turnover	34:63	intermediate filament turnover	34:63	Gigaxonin glycosylation regulates intermediate filament turnover and may impact giant axonal neuropathy etiology or treatment Gigaxonin (also known as KLHL16) is an E3 ligase adaptor protein that promotes the ubiquitination and degradation of intermediate filament (IF) proteins.
31944090	3	38	theme	prevalent	803:811	arg1	β-<italic>N</italic>-acetylglucosamine					750:787	<italic>O</italic>-linked β-<italic>N</italic>-acetylglucosamine	724:787	<italic>O</italic>-linked β-<italic>N</italic>-acetylglucosamine (O-GlcNAc)	724:798	Here, we report that gigaxonin is modified by <italic>O</italic>-linked β-<italic>N</italic>-acetylglucosamine (O-GlcNAc), a prevalent form of intracellular glycosylation, in a nutrient- and growth factor–dependent manner.
31944090	3	38	theme	prevalent	803:811	arg1	form					813:816	a prevalent form	801:816	a prevalent form of intracellular glycosylation	801:847	Here, we report that gigaxonin is modified by <italic>O</italic>-linked β-<italic>N</italic>-acetylglucosamine (O-GlcNAc), a prevalent form of intracellular glycosylation, in a nutrient- and growth factor–dependent manner.
31944090	6	39	theme	nongenetic	1349:1358	arg1	modifiers					1360:1368	the nongenetic modifiers	1345:1368	the nongenetic modifiers of GAN phenotypes	1345:1386	Our work may have significant implications for understanding the nongenetic modifiers of GAN phenotypes and for the optimization of gene therapy for this disease.
31944090	4	40	theme	human	916:920	arg1	gigaxonin					922:930	human gigaxonin	916:930	human gigaxonin	916:930	MS analyses of human gigaxonin revealed 9 candidate sites of O-GlcNAcylation, 2 of which — serine 272 and threonine 277 — are required for its ability to mediate IF turnover in gigaxonin-deficient human cell models that we created.
31944090	0	41	theme	filament	47:54	arg1	turnover					56:63	intermediate filament turnover	34:63	intermediate filament turnover	34:63	Gigaxonin glycosylation regulates intermediate filament turnover and may impact giant axonal neuropathy etiology or treatment Gigaxonin (also known as KLHL16) is an E3 ligase adaptor protein that promotes the ubiquitination and degradation of intermediate filament (IF) proteins.
31944090	1	42	theme	human	293:297	arg1	gigaxonin					299:307	human gigaxonin	293:307	human gigaxonin	293:307	Mutations in human gigaxonin cause the fatal neurodegenerative disease giant axonal neuropathy (GAN), in which IF proteins accumulate and aggregate in axons throughout the nervous system, impairing neuronal function and viability.
31944090	2	43	theme	pathophysiological	524:541	arg1	significance					543:554	this pathophysiological significance	519:554	this pathophysiological significance	519:554	Despite this pathophysiological significance, the upstream regulation and downstream effects of normal and aberrant gigaxonin function remain incompletely understood.
31944090	6	44	theme	gene	1416:1419	arg1	therapy					1421:1427	gene therapy	1416:1427	gene therapy for this disease	1416:1444	Our work may have significant implications for understanding the nongenetic modifiers of GAN phenotypes and for the optimization of gene therapy for this disease.
31944090	3	45	theme	glycosylation	835:847	arg1	β-<italic>N</italic>-acetylglucosamine					750:787	<italic>O</italic>-linked β-<italic>N</italic>-acetylglucosamine	724:787	<italic>O</italic>-linked β-<italic>N</italic>-acetylglucosamine (O-GlcNAc)	724:798	Here, we report that gigaxonin is modified by <italic>O</italic>-linked β-<italic>N</italic>-acetylglucosamine (O-GlcNAc), a prevalent form of intracellular glycosylation, in a nutrient- and growth factor–dependent manner.
31944090	3	45	theme	glycosylation	835:847	arg1	form					813:816	a prevalent form	801:816	a prevalent form of intracellular glycosylation	801:847	Here, we report that gigaxonin is modified by <italic>O</italic>-linked β-<italic>N</italic>-acetylglucosamine (O-GlcNAc), a prevalent form of intracellular glycosylation, in a nutrient- and growth factor–dependent manner.
31944090	2	46	theme	downstream	585:594	arg1	effects					596:602	downstream effects	585:602	downstream effects	585:602	Despite this pathophysiological significance, the upstream regulation and downstream effects of normal and aberrant gigaxonin function remain incompletely understood.
31944090	5	47	theme	regulatory	1228:1237	arg1	link					1239:1242	a regulatory link	1226:1242	a regulatory link between metabolism and IF proteostasis	1226:1281	Taken together, the results suggest that nutrient-responsive gigaxonin O-GlcNAcylation forms a regulatory link between metabolism and IF proteostasis.
31944090	1	48	theme	neuronal	478:485	arg1	function					487:494	neuronal function	478:494	neuronal function	478:494	Mutations in human gigaxonin cause the fatal neurodegenerative disease giant axonal neuropathy (GAN), in which IF proteins accumulate and aggregate in axons throughout the nervous system, impairing neuronal function and viability.
31944090	1	49	theme	giant	351:355	arg1	neuropathy					364:373	giant axonal neuropathy	351:373	the fatal neurodegenerative disease giant axonal neuropathy (GAN)	315:379	Mutations in human gigaxonin cause the fatal neurodegenerative disease giant axonal neuropathy (GAN), in which IF proteins accumulate and aggregate in axons throughout the nervous system, impairing neuronal function and viability.
31944090	1	49	theme	giant	351:355	arg1	GAN					376:378	GAN	376:378	GAN	376:378	Mutations in human gigaxonin cause the fatal neurodegenerative disease giant axonal neuropathy (GAN), in which IF proteins accumulate and aggregate in axons throughout the nervous system, impairing neuronal function and viability.
31944090	4	50	theme	candidate	943:951	arg1	O-GlcNAcylation					962:976	O-GlcNAcylation	962:976	O-GlcNAcylation	962:976	MS analyses of human gigaxonin revealed 9 candidate sites of O-GlcNAcylation, 2 of which — serine 272 and threonine 277 — are required for its ability to mediate IF turnover in gigaxonin-deficient human cell models that we created.
31944090	4	50	theme	candidate	943:951	arg1	sites					953:957	9 candidate sites	941:957	9 candidate sites	941:957	MS analyses of human gigaxonin revealed 9 candidate sites of O-GlcNAcylation, 2 of which — serine 272 and threonine 277 — are required for its ability to mediate IF turnover in gigaxonin-deficient human cell models that we created.
31944090	5	51	theme	nutrient-responsive	1174:1192	arg1	O-GlcNAcylation					1204:1218	nutrient-responsive gigaxonin O-GlcNAcylation	1174:1218	nutrient-responsive gigaxonin O-GlcNAcylation	1174:1218	Taken together, the results suggest that nutrient-responsive gigaxonin O-GlcNAcylation forms a regulatory link between metabolism and IF proteostasis.
31944090	4	52	theme	O-GlcNAcylation	962:976	arg1	O-GlcNAcylation					962:976	O-GlcNAcylation	962:976	O-GlcNAcylation	962:976	MS analyses of human gigaxonin revealed 9 candidate sites of O-GlcNAcylation, 2 of which — serine 272 and threonine 277 — are required for its ability to mediate IF turnover in gigaxonin-deficient human cell models that we created.
31944090	4	52	theme	O-GlcNAcylation	962:976	arg1	sites					953:957	9 candidate sites	941:957	9 candidate sites	941:957	MS analyses of human gigaxonin revealed 9 candidate sites of O-GlcNAcylation, 2 of which — serine 272 and threonine 277 — are required for its ability to mediate IF turnover in gigaxonin-deficient human cell models that we created.
31944090	6	53	theme	significant	1302:1312	arg1	implications					1314:1325	significant implications	1302:1325	significant implications for understanding the nongenetic modifiers of GAN phenotypes and for the optimization of gene therapy for this disease	1302:1444	Our work may have significant implications for understanding the nongenetic modifiers of GAN phenotypes and for the optimization of gene therapy for this disease.
31944090	2	54	theme	upstream	561:568	arg1	regulation					570:579	upstream regulation	561:579	upstream regulation	561:579	Despite this pathophysiological significance, the upstream regulation and downstream effects of normal and aberrant gigaxonin function remain incompletely understood.
31944090	2	55	dep	regulation	570:579	arg1	the					557:559	the	557:559	the	557:559	Despite this pathophysiological significance, the upstream regulation and downstream effects of normal and aberrant gigaxonin function remain incompletely understood.
31944090	0	56	theme	giant	80:84	arg1	neuropathy					93:102	giant axonal neuropathy	80:102	giant axonal neuropathy	80:102	Gigaxonin glycosylation regulates intermediate filament turnover and may impact giant axonal neuropathy etiology or treatment Gigaxonin (also known as KLHL16) is an E3 ligase adaptor protein that promotes the ubiquitination and degradation of intermediate filament (IF) proteins.
31944090	3	57	mod	modified	712:719	arg3	O-GlcNAc					790:797	O-GlcNAc	790:797	O-GlcNAc	790:797	Here, we report that gigaxonin is modified by <italic>O</italic>-linked β-<italic>N</italic>-acetylglucosamine (O-GlcNAc), a prevalent form of intracellular glycosylation, in a nutrient- and growth factor–dependent manner.
31944090	3	57	mod	modified	712:719	arg1	gigaxonin					699:707	gigaxonin	699:707	gigaxonin	699:707	Here, we report that gigaxonin is modified by <italic>O</italic>-linked β-<italic>N</italic>-acetylglucosamine (O-GlcNAc), a prevalent form of intracellular glycosylation, in a nutrient- and growth factor–dependent manner.
31944090	3	57	mod	modified	712:719	arg3	form					813:816	a prevalent form	801:816	a prevalent form of intracellular glycosylation	801:847	Here, we report that gigaxonin is modified by <italic>O</italic>-linked β-<italic>N</italic>-acetylglucosamine (O-GlcNAc), a prevalent form of intracellular glycosylation, in a nutrient- and growth factor–dependent manner.
31944090	3	57	mod	modified	712:719	arg3	β-<italic>N</italic>-acetylglucosamine					750:787	<italic>O</italic>-linked β-<italic>N</italic>-acetylglucosamine	724:787	<italic>O</italic>-linked β-<italic>N</italic>-acetylglucosamine (O-GlcNAc)	724:798	Here, we report that gigaxonin is modified by <italic>O</italic>-linked β-<italic>N</italic>-acetylglucosamine (O-GlcNAc), a prevalent form of intracellular glycosylation, in a nutrient- and growth factor–dependent manner.
31944090	4	58	theme	threonine	1007:1015	arg1	—					1021:1021	— serine 272 and threonine 277 —	990:1021	— serine 272 and threonine 277 —	990:1021	MS analyses of human gigaxonin revealed 9 candidate sites of O-GlcNAcylation, 2 of which — serine 272 and threonine 277 — are required for its ability to mediate IF turnover in gigaxonin-deficient human cell models that we created.
31944090	1	59	theme	fatal	319:323	arg1	disease					343:349	the fatal neurodegenerative disease	315:349	the fatal neurodegenerative disease giant axonal neuropathy (GAN)	315:379	Mutations in human gigaxonin cause the fatal neurodegenerative disease giant axonal neuropathy (GAN), in which IF proteins accumulate and aggregate in axons throughout the nervous system, impairing neuronal function and viability.
31944090	0	60	dep	known	142:146	arg1	also					137:140	also	137:140	also	137:140	Gigaxonin glycosylation regulates intermediate filament turnover and may impact giant axonal neuropathy etiology or treatment Gigaxonin (also known as KLHL16) is an E3 ligase adaptor protein that promotes the ubiquitination and degradation of intermediate filament (IF) proteins.
31944090	4	61	theme	gigaxonin-deficient	1078:1096	arg1	models					1109:1114	gigaxonin-deficient human cell models	1078:1114	gigaxonin-deficient human cell models that we created	1078:1130	MS analyses of human gigaxonin revealed 9 candidate sites of O-GlcNAcylation, 2 of which — serine 272 and threonine 277 — are required for its ability to mediate IF turnover in gigaxonin-deficient human cell models that we created.
31944090	5	62	theme	gigaxonin	1194:1202	arg1	O-GlcNAcylation					1204:1218	nutrient-responsive gigaxonin O-GlcNAcylation	1174:1218	nutrient-responsive gigaxonin O-GlcNAcylation	1174:1218	Taken together, the results suggest that nutrient-responsive gigaxonin O-GlcNAcylation forms a regulatory link between metabolism and IF proteostasis.
19506079	2	0	theme	cell	360:363	arg1	cycle					365:369	cell cycle	360:369	cell cycle	360:369	GlcNAcylated proteins are crucial in regulating virtually all cellular processes, including signaling, cell cycle, and transcription.
19506079	7	1	theme	GlcNAcylation	902:914	arg1	sites					916:920	the GlcNAcylation sites	898:920	the GlcNAcylation sites located in the active site of CaMKIV	898:957	Using site-directed mutagenesis, we determine that the GlcNAcylation sites located in the active site of CaMKIV can modulate its phosphorylation at Thr-200 and its activity toward cAMP-response element-binding transcription factor.
19506079	1	2	theme	post-translational	224:241	arg1	modification					243:254	an abundant, dynamic, and inducible post-translational modification	188:254	an abundant, dynamic, and inducible post-translational modification	188:254	Similar to phosphorylation, GlcNAcylation (the addition of O-GlcNAc to Ser(Thr) residues on polypeptides) is an abundant, dynamic, and inducible post-translational modification.
19506079	1	2	theme	post-translational	224:241	arg1	GlcNAcylation					107:119	GlcNAcylation	107:119	GlcNAcylation (the addition of O-GlcNAc to Ser(Thr) residues on polypeptides)	107:183	Similar to phosphorylation, GlcNAcylation (the addition of O-GlcNAc to Ser(Thr) residues on polypeptides) is an abundant, dynamic, and inducible post-translational modification.
19506079	9	3	theme	O-GlcNAc	1352:1359	arg1	cross-talk					1380:1389	O-GlcNAc transferase/kinase cross-talk	1352:1389	O-GlcNAc transferase/kinase cross-talk	1352:1389	This is the first example of an O-GlcNAc/phosphate cycle involving O-GlcNAc transferase/kinase cross-talk.
19506079	6	4	theme	GlcNAcylation	822:834	arg1	sites					813:817	at least five sites	799:817	at least five sites of GlcNAcylation on CaMKIV	799:844	Furthermore, we identify at least five sites of GlcNAcylation on CaMKIV.
19506079	6	4	theme	GlcNAcylation	822:834	arg1	GlcNAcylation					822:834	GlcNAcylation	822:834	GlcNAcylation	822:834	Furthermore, we identify at least five sites of GlcNAcylation on CaMKIV.
19506079	1	5	dep	GlcNAcylation	107:119	arg1	addition					126:133	the addition	122:133	the addition of O-GlcNAc to Ser(Thr) residues on polypeptides	122:182	Similar to phosphorylation, GlcNAcylation (the addition of O-GlcNAc to Ser(Thr) residues on polypeptides) is an abundant, dynamic, and inducible post-translational modification.
19506079	4	6	theme	CaMKIV	569:574	arg1	GlcNAcylation					576:588	hemagglutinin-tagged CaMKIV GlcNAcylation	548:588	hemagglutinin-tagged CaMKIV GlcNAcylation	548:588	In addition, we show that upon activation of HEK293 cells, hemagglutinin-tagged CaMKIV GlcNAcylation rapidly decreases, in a manner directly opposing its phosphorylation at Thr-200.
19506079	9	7	theme	transferase/kinase	1361:1378	arg1	cross-talk					1380:1389	O-GlcNAc transferase/kinase cross-talk	1352:1389	O-GlcNAc transferase/kinase cross-talk	1352:1389	This is the first example of an O-GlcNAc/phosphate cycle involving O-GlcNAc transferase/kinase cross-talk.
19506079	5	8	from	increase	700:707	arg1	interaction					719:729	CaMKIV interaction	712:729	CaMKIV interaction with O-GlcNAcase during CaMKIV activation	712:771	Correspondingly, there is an increase in CaMKIV interaction with O-GlcNAcase during CaMKIV activation.
19506079	8	9	theme	nutritional	1228:1238	arg1	signals					1240:1246	nutritional signals	1228:1246	nutritional signals	1228:1246	Our results strongly indicate that the O-GlcNAc modification participates in the regulation of CaMKIV activation and function, possibly coordinating nutritional signals with the immune and nervous systems.
19506079	6	10	from	sites	813:817	arg1	CaMKIV					839:844	CaMKIV	839:844	CaMKIV	839:844	Furthermore, we identify at least five sites of GlcNAcylation on CaMKIV.
19506079	5	11	theme	CaMKIV	755:760	arg1	activation					762:771	CaMKIV activation	755:771	CaMKIV activation	755:771	Correspondingly, there is an increase in CaMKIV interaction with O-GlcNAcase during CaMKIV activation.
19506079	7	12	theme	site-directed	853:865	arg1	mutagenesis					867:877	site-directed mutagenesis	853:877	site-directed mutagenesis	853:877	Using site-directed mutagenesis, we determine that the GlcNAcylation sites located in the active site of CaMKIV can modulate its phosphorylation at Thr-200 and its activity toward cAMP-response element-binding transcription factor.
19506079	7	13	from	Thr-200	995:1001	arg1	activity					1011:1018	its activity	1007:1018	its activity toward cAMP-response element-binding transcription factor	1007:1076	Using site-directed mutagenesis, we determine that the GlcNAcylation sites located in the active site of CaMKIV can modulate its phosphorylation at Thr-200 and its activity toward cAMP-response element-binding transcription factor.
19506079	7	13	from	Thr-200	995:1001	arg1	phosphorylation					976:990	its phosphorylation	972:990	its phosphorylation at Thr-200	972:1001	Using site-directed mutagenesis, we determine that the GlcNAcylation sites located in the active site of CaMKIV can modulate its phosphorylation at Thr-200 and its activity toward cAMP-response element-binding transcription factor.
19506079	7	14	theme	CaMKIV	952:957	arg1	CaMKIV					952:957	CaMKIV	952:957	CaMKIV	952:957	Using site-directed mutagenesis, we determine that the GlcNAcylation sites located in the active site of CaMKIV can modulate its phosphorylation at Thr-200 and its activity toward cAMP-response element-binding transcription factor.
19506079	7	14	theme	CaMKIV	952:957	arg1	site					944:947	the active site	933:947	the active site of CaMKIV	933:957	Using site-directed mutagenesis, we determine that the GlcNAcylation sites located in the active site of CaMKIV can modulate its phosphorylation at Thr-200 and its activity toward cAMP-response element-binding transcription factor.
19506079	2	15	theme	cellular	319:326	arg1	processes					328:336	virtually all cellular processes	305:336	virtually all cellular processes	305:336	GlcNAcylated proteins are crucial in regulating virtually all cellular processes, including signaling, cell cycle, and transcription.
19506079	2	15	theme	cellular	319:326	arg1	signaling					349:357	signaling	349:357	signaling	349:357	GlcNAcylated proteins are crucial in regulating virtually all cellular processes, including signaling, cell cycle, and transcription.
19506079	2	15	theme	cellular	319:326	arg1	cycle					365:369	cell cycle	360:369	cell cycle	360:369	GlcNAcylated proteins are crucial in regulating virtually all cellular processes, including signaling, cell cycle, and transcription.
19506079	2	15	theme	cellular	319:326	arg1	transcription					376:388	transcription	376:388	transcription	376:388	GlcNAcylated proteins are crucial in regulating virtually all cellular processes, including signaling, cell cycle, and transcription.
19506079	4	16	theme	cells	541:545	arg1	activation					520:529	activation	520:529	activation of HEK293 cells	520:545	In addition, we show that upon activation of HEK293 cells, hemagglutinin-tagged CaMKIV GlcNAcylation rapidly decreases, in a manner directly opposing its phosphorylation at Thr-200.
19506079	7	17	theme	active	937:942	arg1	CaMKIV					952:957	CaMKIV	952:957	CaMKIV	952:957	Using site-directed mutagenesis, we determine that the GlcNAcylation sites located in the active site of CaMKIV can modulate its phosphorylation at Thr-200 and its activity toward cAMP-response element-binding transcription factor.
19506079	7	17	theme	active	937:942	arg1	site					944:947	the active site	933:947	the active site of CaMKIV	933:957	Using site-directed mutagenesis, we determine that the GlcNAcylation sites located in the active site of CaMKIV can modulate its phosphorylation at Thr-200 and its activity toward cAMP-response element-binding transcription factor.
19506079	2	18	theme	all	315:317	arg1	processes					328:336	virtually all cellular processes	305:336	virtually all cellular processes	305:336	GlcNAcylated proteins are crucial in regulating virtually all cellular processes, including signaling, cell cycle, and transcription.
19506079	2	18	theme	all	315:317	arg1	signaling					349:357	signaling	349:357	signaling	349:357	GlcNAcylated proteins are crucial in regulating virtually all cellular processes, including signaling, cell cycle, and transcription.
19506079	2	18	theme	all	315:317	arg1	cycle					365:369	cell cycle	360:369	cell cycle	360:369	GlcNAcylated proteins are crucial in regulating virtually all cellular processes, including signaling, cell cycle, and transcription.
19506079	2	18	theme	all	315:317	arg1	transcription					376:388	transcription	376:388	transcription	376:388	GlcNAcylated proteins are crucial in regulating virtually all cellular processes, including signaling, cell cycle, and transcription.
19506079	0	19	theme	kinase	43:48	arg1	Regulation					0:9	Regulation	0:9	Regulation of calcium/calmodulin-dependent kinase IV by O-GlcNAc modification.	0:77	Regulation of calcium/calmodulin-dependent kinase IV by O-GlcNAc modification.
19506079	4	20	theme	HEK293	534:539	arg1	cells					541:545	HEK293 cells	534:545	HEK293 cells	534:545	In addition, we show that upon activation of HEK293 cells, hemagglutinin-tagged CaMKIV GlcNAcylation rapidly decreases, in a manner directly opposing its phosphorylation at Thr-200.
19506079	8	21	theme	O-GlcNAc	1118:1125	arg1	modification					1127:1138	the O-GlcNAc modification	1114:1138	the O-GlcNAc modification	1114:1138	Our results strongly indicate that the O-GlcNAc modification participates in the regulation of CaMKIV activation and function, possibly coordinating nutritional signals with the immune and nervous systems.
19506079	0	22	theme	calcium/calmodulin-dependent	14:41	arg1	kinase					43:48	calcium/calmodulin-dependent kinase IV	14:51	calcium/calmodulin-dependent kinase IV	14:51	Regulation of calcium/calmodulin-dependent kinase IV by O-GlcNAc modification.
19506079	4	23	theme	hemagglutinin-tagged	548:567	arg1	GlcNAcylation					576:588	hemagglutinin-tagged CaMKIV GlcNAcylation	548:588	hemagglutinin-tagged CaMKIV GlcNAcylation	548:588	In addition, we show that upon activation of HEK293 cells, hemagglutinin-tagged CaMKIV GlcNAcylation rapidly decreases, in a manner directly opposing its phosphorylation at Thr-200.
19506079	5	24	with	interaction	719:729	arg1	O-GlcNAcase					736:746	O-GlcNAcase	736:746	O-GlcNAcase	736:746	Correspondingly, there is an increase in CaMKIV interaction with O-GlcNAcase during CaMKIV activation.
19506079	8	25	theme	nervous	1268:1274	arg1	systems					1276:1282	the immune and nervous systems	1253:1282	the immune and nervous systems	1253:1282	Our results strongly indicate that the O-GlcNAc modification participates in the regulation of CaMKIV activation and function, possibly coordinating nutritional signals with the immune and nervous systems.
19506079	5	26	theme	CaMKIV	712:717	arg1	interaction					719:729	CaMKIV interaction	712:729	CaMKIV interaction with O-GlcNAcase during CaMKIV activation	712:771	Correspondingly, there is an increase in CaMKIV interaction with O-GlcNAcase during CaMKIV activation.
19506079	1	27	theme	abundant	191:198	arg1	modification					243:254	an abundant, dynamic, and inducible post-translational modification	188:254	an abundant, dynamic, and inducible post-translational modification	188:254	Similar to phosphorylation, GlcNAcylation (the addition of O-GlcNAc to Ser(Thr) residues on polypeptides) is an abundant, dynamic, and inducible post-translational modification.
19506079	1	27	theme	abundant	191:198	arg1	GlcNAcylation					107:119	GlcNAcylation	107:119	GlcNAcylation (the addition of O-GlcNAc to Ser(Thr) residues on polypeptides)	107:183	Similar to phosphorylation, GlcNAcylation (the addition of O-GlcNAc to Ser(Thr) residues on polypeptides) is an abundant, dynamic, and inducible post-translational modification.
19506079	3	28	theme	calcium/calmodulin-dependent	409:436	arg1	kinase					438:443	calcium/calmodulin-dependent kinase IV	409:446	calcium/calmodulin-dependent kinase IV (CaMKIV)	409:455	Here we show that calcium/calmodulin-dependent kinase IV (CaMKIV) is highly GlcNAcylated in vivo.
19506079	3	28	theme	calcium/calmodulin-dependent	409:436	arg1	CaMKIV					449:454	CaMKIV	449:454	CaMKIV	449:454	Here we show that calcium/calmodulin-dependent kinase IV (CaMKIV) is highly GlcNAcylated in vivo.
19506079	8	29	theme	immune	1257:1262	arg1	systems					1276:1282	the immune and nervous systems	1253:1282	the immune and nervous systems	1253:1282	Our results strongly indicate that the O-GlcNAc modification participates in the regulation of CaMKIV activation and function, possibly coordinating nutritional signals with the immune and nervous systems.
19506079	7	30	theme	cAMP-response	1027:1039	arg1	factor					1071:1076	cAMP-response element-binding transcription factor	1027:1076	cAMP-response element-binding transcription factor	1027:1076	Using site-directed mutagenesis, we determine that the GlcNAcylation sites located in the active site of CaMKIV can modulate its phosphorylation at Thr-200 and its activity toward cAMP-response element-binding transcription factor.
19506079	9	31	theme	first	1297:1301	arg1	This					1285:1288	This	1285:1288	This	1285:1288	This is the first example of an O-GlcNAc/phosphate cycle involving O-GlcNAc transferase/kinase cross-talk.
19506079	9	31	theme	first	1297:1301	arg1	example					1303:1309	the first example	1293:1309	the first example of an O-GlcNAc/phosphate cycle involving O-GlcNAc transferase/kinase cross-talk	1293:1389	This is the first example of an O-GlcNAc/phosphate cycle involving O-GlcNAc transferase/kinase cross-talk.
19506079	7	32	theme	element-binding	1041:1055	arg1	factor					1071:1076	cAMP-response element-binding transcription factor	1027:1076	cAMP-response element-binding transcription factor	1027:1076	Using site-directed mutagenesis, we determine that the GlcNAcylation sites located in the active site of CaMKIV can modulate its phosphorylation at Thr-200 and its activity toward cAMP-response element-binding transcription factor.
19506079	0	33	theme	O-GlcNAc	56:63	arg1	modification					65:76	O-GlcNAc modification	56:76	O-GlcNAc modification	56:76	Regulation of calcium/calmodulin-dependent kinase IV by O-GlcNAc modification.
19506079	7	34	from	site	944:947	arg1	located					922:928	located	922:928	located	922:928	Using site-directed mutagenesis, we determine that the GlcNAcylation sites located in the active site of CaMKIV can modulate its phosphorylation at Thr-200 and its activity toward cAMP-response element-binding transcription factor.
19506079	7	35	theme	transcription	1057:1069	arg1	factor					1071:1076	cAMP-response element-binding transcription factor	1027:1076	cAMP-response element-binding transcription factor	1027:1076	Using site-directed mutagenesis, we determine that the GlcNAcylation sites located in the active site of CaMKIV can modulate its phosphorylation at Thr-200 and its activity toward cAMP-response element-binding transcription factor.
19506079	2	36	theme	GlcNAcylated	257:268	arg1	proteins					270:277	GlcNAcylated proteins	257:277	GlcNAcylated proteins	257:277	GlcNAcylated proteins are crucial in regulating virtually all cellular processes, including signaling, cell cycle, and transcription.
19506079	1	37	theme	O-GlcNAc	138:145	arg1	addition					126:133	the addition	122:133	the addition of O-GlcNAc to Ser(Thr) residues on polypeptides	122:182	Similar to phosphorylation, GlcNAcylation (the addition of O-GlcNAc to Ser(Thr) residues on polypeptides) is an abundant, dynamic, and inducible post-translational modification.
19506079	7	38	from	located	922:928	arg1	CaMKIV					952:957	CaMKIV	952:957	CaMKIV	952:957	Using site-directed mutagenesis, we determine that the GlcNAcylation sites located in the active site of CaMKIV can modulate its phosphorylation at Thr-200 and its activity toward cAMP-response element-binding transcription factor.
19506079	7	38	from	located	922:928	arg1	site					944:947	the active site	933:947	the active site of CaMKIV	933:957	Using site-directed mutagenesis, we determine that the GlcNAcylation sites located in the active site of CaMKIV can modulate its phosphorylation at Thr-200 and its activity toward cAMP-response element-binding transcription factor.
19506079	1	39	theme	dynamic	201:207	arg1	modification					243:254	an abundant, dynamic, and inducible post-translational modification	188:254	an abundant, dynamic, and inducible post-translational modification	188:254	Similar to phosphorylation, GlcNAcylation (the addition of O-GlcNAc to Ser(Thr) residues on polypeptides) is an abundant, dynamic, and inducible post-translational modification.
19506079	1	39	theme	dynamic	201:207	arg1	GlcNAcylation					107:119	GlcNAcylation	107:119	GlcNAcylation (the addition of O-GlcNAc to Ser(Thr) residues on polypeptides)	107:183	Similar to phosphorylation, GlcNAcylation (the addition of O-GlcNAc to Ser(Thr) residues on polypeptides) is an abundant, dynamic, and inducible post-translational modification.
19506079	8	40	theme	activation	1181:1190	arg1	function					1196:1203	function	1196:1203	function	1196:1203	Our results strongly indicate that the O-GlcNAc modification participates in the regulation of CaMKIV activation and function, possibly coordinating nutritional signals with the immune and nervous systems.
19506079	8	40	theme	activation	1181:1190	arg1	regulation					1160:1169	the regulation	1156:1169	the regulation of CaMKIV activation	1156:1190	Our results strongly indicate that the O-GlcNAc modification participates in the regulation of CaMKIV activation and function, possibly coordinating nutritional signals with the immune and nervous systems.
19506079	9	41	theme	O-GlcNAc/phosphate	1317:1334	arg1	cycle					1336:1340	an O-GlcNAc/phosphate cycle	1314:1340	an O-GlcNAc/phosphate cycle involving O-GlcNAc transferase/kinase cross-talk	1314:1389	This is the first example of an O-GlcNAc/phosphate cycle involving O-GlcNAc transferase/kinase cross-talk.
19506079	1	42	theme	Ser	150:152	arg1	residues					159:166	Ser(Thr) residues	150:166	Ser(Thr) residues on polypeptides	150:182	Similar to phosphorylation, GlcNAcylation (the addition of O-GlcNAc to Ser(Thr) residues on polypeptides) is an abundant, dynamic, and inducible post-translational modification.
19506079	7	43	theme	located	922:928	arg1	sites					916:920	the GlcNAcylation sites	898:920	the GlcNAcylation sites located in the active site of CaMKIV	898:957	Using site-directed mutagenesis, we determine that the GlcNAcylation sites located in the active site of CaMKIV can modulate its phosphorylation at Thr-200 and its activity toward cAMP-response element-binding transcription factor.
19506079	8	44	theme	CaMKIV	1174:1179	arg1	activation					1181:1190	CaMKIV activation	1174:1190	CaMKIV activation	1174:1190	Our results strongly indicate that the O-GlcNAc modification participates in the regulation of CaMKIV activation and function, possibly coordinating nutritional signals with the immune and nervous systems.
19506079	9	45	theme	cycle	1336:1340	arg1	This					1285:1288	This	1285:1288	This	1285:1288	This is the first example of an O-GlcNAc/phosphate cycle involving O-GlcNAc transferase/kinase cross-talk.
19506079	9	45	theme	cycle	1336:1340	arg1	example					1303:1309	the first example	1293:1309	the first example of an O-GlcNAc/phosphate cycle involving O-GlcNAc transferase/kinase cross-talk	1293:1389	This is the first example of an O-GlcNAc/phosphate cycle involving O-GlcNAc transferase/kinase cross-talk.
19506079	1	46	from	residues	159:166	arg1	polypeptides					171:182	polypeptides	171:182	polypeptides	171:182	Similar to phosphorylation, GlcNAcylation (the addition of O-GlcNAc to Ser(Thr) residues on polypeptides) is an abundant, dynamic, and inducible post-translational modification.
19506079	1	47	theme	inducible	214:222	arg1	modification					243:254	an abundant, dynamic, and inducible post-translational modification	188:254	an abundant, dynamic, and inducible post-translational modification	188:254	Similar to phosphorylation, GlcNAcylation (the addition of O-GlcNAc to Ser(Thr) residues on polypeptides) is an abundant, dynamic, and inducible post-translational modification.
19506079	1	47	theme	inducible	214:222	arg1	GlcNAcylation					107:119	GlcNAcylation	107:119	GlcNAcylation (the addition of O-GlcNAc to Ser(Thr) residues on polypeptides)	107:183	Similar to phosphorylation, GlcNAcylation (the addition of O-GlcNAc to Ser(Thr) residues on polypeptides) is an abundant, dynamic, and inducible post-translational modification.
32060258	8	0	theme	OGT	1073:1075	arg1	level					1077:1081	the OGT level	1069:1081	the OGT level in pancreatic cancer patients	1069:1111	Consistently, the PFKFB3-Ser172 phosphorylation level inversely correlated with the OGT level in pancreatic cancer patients.
32060258	6	1	theme	Phosphorylated	665:678	arg1	PFKFB3					680:685	Phosphorylated PFKFB3	665:685	Phosphorylated PFKFB3	665:685	Phosphorylated PFKFB3 could interact with the protein G3BP2 and retain in the cytosol; this in turn led to the accumulation of hypoxia-induced-P27 in the nucleus resulting in the cell cycle arrest.
32060258	6	2	theme	cell	844:847	arg1	arrest					855:860	the cell cycle arrest	840:860	the cell cycle arrest	840:860	Phosphorylated PFKFB3 could interact with the protein G3BP2 and retain in the cytosol; this in turn led to the accumulation of hypoxia-induced-P27 in the nucleus resulting in the cell cycle arrest.
32060258	7	3	theme	cell	965:968	arg1	progression					976:986	cell cycle progression	965:986	cell cycle progression	965:986	Such a pathway was compromised by high level of PFKFB3 O-GlcNAcylation in tumor cells contributing to cell cycle progression.
32060258	4	4	from	response	521:528	arg1	O-GlcNAcylated					503:516	O-GlcNAcylated	503:516	O-GlcNAcylated	503:516	Here, we showed that the glycolytic regulator 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFKFB3), which also promotes cell cycle progression in the nucleus, was O-GlcNAcylated in response to hypoxia.
32060258	4	4	from	response	521:528	arg1	6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase					377:428	the glycolytic regulator 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase	352:428	the glycolytic regulator 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFKFB3)	352:437	Here, we showed that the glycolytic regulator 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFKFB3), which also promotes cell cycle progression in the nucleus, was O-GlcNAcylated in response to hypoxia.
32060258	5	5	theme	same	634:637	arg1	site					652:655	the same modification site Ser172	630:662	the same modification site Ser172	630:662	The O-GlcNAcylation of PFKFB3 could compete phosphorylation by hypoxia-activated ERK at the same modification site Ser172.
32060258	7	6	theme	high	897:900	arg1	level					902:906	high level	897:906	high level of PFKFB3 O-GlcNAcylation in tumor cells contributing to cell cycle progression	897:986	Such a pathway was compromised by high level of PFKFB3 O-GlcNAcylation in tumor cells contributing to cell cycle progression.
32060258	3	7	dep	mechanism	296:304	arg1	behind					306:311	behind	306:311	behind	306:311	However, the mechanism behind is still unclear.
32060258	5	8	theme	modification	639:650	arg1	site					652:655	the same modification site Ser172	630:662	the same modification site Ser172	630:662	The O-GlcNAcylation of PFKFB3 could compete phosphorylation by hypoxia-activated ERK at the same modification site Ser172.
32060258	4	9	from	O-GlcNAcylated	503:516	arg1	response					521:528	response	521:528	response to hypoxia	521:539	Here, we showed that the glycolytic regulator 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFKFB3), which also promotes cell cycle progression in the nucleus, was O-GlcNAcylated in response to hypoxia.
32060258	9	10	theme	OGT	1256:1258	arg1	activity					1260:1267	the aberrant OGT activity	1243:1267	the aberrant OGT activity	1243:1267	Our findings uncovered an O-GlcNAcylation mediated mechanism to promote tumor cell proliferation under metabolic stress, linking the aberrant OGT activity to tumorigenesis in pancreatic cancer.
32060258	7	11	from	level	902:906	arg1	cells					943:947	tumor cells	937:947	tumor cells contributing to cell cycle progression	937:986	Such a pathway was compromised by high level of PFKFB3 O-GlcNAcylation in tumor cells contributing to cell cycle progression.
32060258	8	12	theme	pancreatic	1086:1095	arg1	patients					1104:1111	pancreatic cancer patients	1086:1111	pancreatic cancer patients	1086:1111	Consistently, the PFKFB3-Ser172 phosphorylation level inversely correlated with the OGT level in pancreatic cancer patients.
32060258	4	13	theme	glycolytic	356:365	arg1	PFKFB3					431:436	PFKFB3	431:436	PFKFB3	431:436	Here, we showed that the glycolytic regulator 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFKFB3), which also promotes cell cycle progression in the nucleus, was O-GlcNAcylated in response to hypoxia.
32060258	4	13	theme	glycolytic	356:365	arg1	6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase					377:428	the glycolytic regulator 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase	352:428	the glycolytic regulator 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFKFB3)	352:437	Here, we showed that the glycolytic regulator 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFKFB3), which also promotes cell cycle progression in the nucleus, was O-GlcNAcylated in response to hypoxia.
32060258	4	13	theme	glycolytic	356:365	arg1	O-GlcNAcylated					503:516	O-GlcNAcylated	503:516	O-GlcNAcylated	503:516	Here, we showed that the glycolytic regulator 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFKFB3), which also promotes cell cycle progression in the nucleus, was O-GlcNAcylated in response to hypoxia.
32060258	7	14	theme	cycle	970:974	arg1	progression					976:986	cell cycle progression	965:986	cell cycle progression	965:986	Such a pathway was compromised by high level of PFKFB3 O-GlcNAcylation in tumor cells contributing to cell cycle progression.
32060258	5	15	theme	hypoxia-activated	605:621	arg1	ERK					623:625	hypoxia-activated ERK	605:625	hypoxia-activated ERK	605:625	The O-GlcNAcylation of PFKFB3 could compete phosphorylation by hypoxia-activated ERK at the same modification site Ser172.
32060258	1	16	theme	glucose	174:180	arg1	availability					182:193	glucose availability	174:193	glucose availability	174:193	The protein O-GlcNAcylation catalysed by O-GlcNAc transferase (OGT) is tightly regulated by glucose availability.
32060258	1	17	theme	protein	86:92	arg1	O-GlcNAcylation					94:108	The protein O-GlcNAcylation	82:108	The protein O-GlcNAcylation catalysed by O-GlcNAc transferase (OGT)	82:148	The protein O-GlcNAcylation catalysed by O-GlcNAc transferase (OGT) is tightly regulated by glucose availability.
32060258	8	18	from	level	1077:1081	arg1	patients					1104:1111	pancreatic cancer patients	1086:1111	pancreatic cancer patients	1086:1111	Consistently, the PFKFB3-Ser172 phosphorylation level inversely correlated with the OGT level in pancreatic cancer patients.
32060258	4	19	theme	regulator	367:375	arg1	PFKFB3					431:436	PFKFB3	431:436	PFKFB3	431:436	Here, we showed that the glycolytic regulator 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFKFB3), which also promotes cell cycle progression in the nucleus, was O-GlcNAcylated in response to hypoxia.
32060258	4	19	theme	regulator	367:375	arg1	6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase					377:428	the glycolytic regulator 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase	352:428	the glycolytic regulator 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFKFB3)	352:437	Here, we showed that the glycolytic regulator 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFKFB3), which also promotes cell cycle progression in the nucleus, was O-GlcNAcylated in response to hypoxia.
32060258	4	19	theme	regulator	367:375	arg1	O-GlcNAcylated					503:516	O-GlcNAcylated	503:516	O-GlcNAcylated	503:516	Here, we showed that the glycolytic regulator 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFKFB3), which also promotes cell cycle progression in the nucleus, was O-GlcNAcylated in response to hypoxia.
32060258	9	20	theme	mediated	1156:1163	arg1	mechanism					1165:1173	an O-GlcNAcylation mediated mechanism	1137:1173	an O-GlcNAcylation mediated mechanism to promote tumor cell proliferation under metabolic stress, linking the aberrant OGT activity to tumorigenesis in pancreatic cancer	1137:1305	Our findings uncovered an O-GlcNAcylation mediated mechanism to promote tumor cell proliferation under metabolic stress, linking the aberrant OGT activity to tumorigenesis in pancreatic cancer.
32060258	0	21	theme	PFKFB3	19:24	arg1	O-GlcNAcylation					0:14	O-GlcNAcylation	0:14	O-GlcNAcylation of PFKFB3	0:24	O-GlcNAcylation of PFKFB3 is required for tumor cell proliferation under hypoxia.
32060258	9	22	theme	pancreatic	1289:1298	arg1	cancer					1300:1305	pancreatic cancer	1289:1305	pancreatic cancer	1289:1305	Our findings uncovered an O-GlcNAcylation mediated mechanism to promote tumor cell proliferation under metabolic stress, linking the aberrant OGT activity to tumorigenesis in pancreatic cancer.
32060258	8	23	theme	cancer	1097:1102	arg1	patients					1104:1111	pancreatic cancer patients	1086:1111	pancreatic cancer patients	1086:1111	Consistently, the PFKFB3-Ser172 phosphorylation level inversely correlated with the OGT level in pancreatic cancer patients.
32060258	4	24	theme	cycle	465:469	arg1	progression					471:481	cell cycle progression	460:481	cell cycle progression	460:481	Here, we showed that the glycolytic regulator 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFKFB3), which also promotes cell cycle progression in the nucleus, was O-GlcNAcylated in response to hypoxia.
32060258	2	25	theme	tumor	232:236	arg1	proliferation					243:255	tumor cell proliferation	232:255	tumor cell proliferation under hypoxic conditions	232:280	It is upregulated and essential for tumor cell proliferation under hypoxic conditions.
32060258	6	26	theme	protein	711:717	arg1	G3BP2					719:723	the protein G3BP2	707:723	the protein G3BP2	707:723	Phosphorylated PFKFB3 could interact with the protein G3BP2 and retain in the cytosol; this in turn led to the accumulation of hypoxia-induced-P27 in the nucleus resulting in the cell cycle arrest.
32060258	8	27	theme	phosphorylation	1021:1035	arg1	level					1037:1041	the PFKFB3-Ser172 phosphorylation level	1003:1041	the PFKFB3-Ser172 phosphorylation level	1003:1041	Consistently, the PFKFB3-Ser172 phosphorylation level inversely correlated with the OGT level in pancreatic cancer patients.
32060258	5	28	theme	PFKFB3	565:570	arg1	O-GlcNAcylation					546:560	The O-GlcNAcylation	542:560	The O-GlcNAcylation of PFKFB3	542:570	The O-GlcNAcylation of PFKFB3 could compete phosphorylation by hypoxia-activated ERK at the same modification site Ser172.
32060258	0	29	theme	cell	48:51	arg1	proliferation					53:65	tumor cell proliferation	42:65	tumor cell proliferation under hypoxia	42:79	O-GlcNAcylation of PFKFB3 is required for tumor cell proliferation under hypoxia.
32060258	9	30	theme	aberrant	1247:1254	arg1	activity					1260:1267	the aberrant OGT activity	1243:1267	the aberrant OGT activity	1243:1267	Our findings uncovered an O-GlcNAcylation mediated mechanism to promote tumor cell proliferation under metabolic stress, linking the aberrant OGT activity to tumorigenesis in pancreatic cancer.
32060258	9	31	theme	tumor	1186:1190	arg1	proliferation					1197:1209	tumor cell proliferation	1186:1209	tumor cell proliferation	1186:1209	Our findings uncovered an O-GlcNAcylation mediated mechanism to promote tumor cell proliferation under metabolic stress, linking the aberrant OGT activity to tumorigenesis in pancreatic cancer.
32060258	9	32	from	tumorigenesis	1272:1284	arg1	cancer					1300:1305	pancreatic cancer	1289:1305	pancreatic cancer	1289:1305	Our findings uncovered an O-GlcNAcylation mediated mechanism to promote tumor cell proliferation under metabolic stress, linking the aberrant OGT activity to tumorigenesis in pancreatic cancer.
32060258	0	33	theme	tumor	42:46	arg1	proliferation					53:65	tumor cell proliferation	42:65	tumor cell proliferation under hypoxia	42:79	O-GlcNAcylation of PFKFB3 is required for tumor cell proliferation under hypoxia.
32060258	9	34	theme	cell	1192:1195	arg1	proliferation					1197:1209	tumor cell proliferation	1186:1209	tumor cell proliferation	1186:1209	Our findings uncovered an O-GlcNAcylation mediated mechanism to promote tumor cell proliferation under metabolic stress, linking the aberrant OGT activity to tumorigenesis in pancreatic cancer.
32060258	1	35	theme	O-GlcNAc	123:130	arg1	transferase					132:142	O-GlcNAc transferase	123:142	O-GlcNAc transferase (OGT)	123:148	The protein O-GlcNAcylation catalysed by O-GlcNAc transferase (OGT) is tightly regulated by glucose availability.
32060258	1	35	theme	O-GlcNAc	123:130	arg1	OGT					145:147	OGT	145:147	OGT	145:147	The protein O-GlcNAcylation catalysed by O-GlcNAc transferase (OGT) is tightly regulated by glucose availability.
32060258	6	36	theme	hypoxia-induced-P27	792:810	arg1	accumulation					776:787	the accumulation	772:787	the accumulation of hypoxia-induced-P27 in the nucleus resulting in the cell cycle arrest	772:860	Phosphorylated PFKFB3 could interact with the protein G3BP2 and retain in the cytosol; this in turn led to the accumulation of hypoxia-induced-P27 in the nucleus resulting in the cell cycle arrest.
32060258	2	37	theme	hypoxic	263:269	arg1	conditions					271:280	hypoxic conditions	263:280	hypoxic conditions	263:280	It is upregulated and essential for tumor cell proliferation under hypoxic conditions.
32060258	7	38	theme	tumor	937:941	arg1	cells					943:947	tumor cells	937:947	tumor cells contributing to cell cycle progression	937:986	Such a pathway was compromised by high level of PFKFB3 O-GlcNAcylation in tumor cells contributing to cell cycle progression.
32060258	4	39	theme	cell	460:463	arg1	progression					471:481	cell cycle progression	460:481	cell cycle progression	460:481	Here, we showed that the glycolytic regulator 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFKFB3), which also promotes cell cycle progression in the nucleus, was O-GlcNAcylated in response to hypoxia.
32060258	6	40	from	accumulation	776:787	arg1	nucleus					819:825	the nucleus	815:825	the nucleus resulting in the cell cycle arrest	815:860	Phosphorylated PFKFB3 could interact with the protein G3BP2 and retain in the cytosol; this in turn led to the accumulation of hypoxia-induced-P27 in the nucleus resulting in the cell cycle arrest.
32060258	7	41	theme	PFKFB3	911:916	arg1	O-GlcNAcylation					918:932	PFKFB3 O-GlcNAcylation	911:932	PFKFB3 O-GlcNAcylation	911:932	Such a pathway was compromised by high level of PFKFB3 O-GlcNAcylation in tumor cells contributing to cell cycle progression.
32060258	6	42	theme	cycle	849:853	arg1	arrest					855:860	the cell cycle arrest	840:860	the cell cycle arrest	840:860	Phosphorylated PFKFB3 could interact with the protein G3BP2 and retain in the cytosol; this in turn led to the accumulation of hypoxia-induced-P27 in the nucleus resulting in the cell cycle arrest.
32060258	9	43	theme	metabolic	1217:1225	arg1	stress					1227:1232	metabolic stress	1217:1232	metabolic stress	1217:1232	Our findings uncovered an O-GlcNAcylation mediated mechanism to promote tumor cell proliferation under metabolic stress, linking the aberrant OGT activity to tumorigenesis in pancreatic cancer.
32060258	7	44	theme	O-GlcNAcylation	918:932	arg1	level					902:906	high level	897:906	high level of PFKFB3 O-GlcNAcylation in tumor cells contributing to cell cycle progression	897:986	Such a pathway was compromised by high level of PFKFB3 O-GlcNAcylation in tumor cells contributing to cell cycle progression.
32060258	2	45	theme	cell	238:241	arg1	proliferation					243:255	tumor cell proliferation	232:255	tumor cell proliferation under hypoxic conditions	232:280	It is upregulated and essential for tumor cell proliferation under hypoxic conditions.
32060258	5	46	from	site	652:655	arg1	phosphorylation					586:600	phosphorylation	586:600	phosphorylation by hypoxia-activated ERK at the same modification site Ser172	586:662	The O-GlcNAcylation of PFKFB3 could compete phosphorylation by hypoxia-activated ERK at the same modification site Ser172.
29556021	1	0	theme	HOXA	307:310	arg1	loci					312:315	posterior HOXA loci	297:315	posterior HOXA loci	297:315	ASXL1 plays key roles in epigenetic regulation of gene expression through methylation of histone H3K27, and disruption of ASXL1 drives myeloid malignancies, at least in part, via derepression of posterior HOXA loci.
29556021	0	1	theme	tumor	59:63	arg1	suppression					65:75	tumor suppression	59:75	tumor suppression	59:75	A novel ASXL1-OGT axis plays roles in H3K4 methylation and tumor suppression in myeloid malignancies.
29556021	1	2	theme	loci	312:315	arg1	derepression					281:292	derepression	281:292	derepression of posterior HOXA loci	281:315	ASXL1 plays key roles in epigenetic regulation of gene expression through methylation of histone H3K27, and disruption of ASXL1 drives myeloid malignancies, at least in part, via derepression of posterior HOXA loci.
29556021	4	3	theme	genes	792:796	arg1	transcription					775:787	transcription	775:787	transcription of genes involved in myeloid differentiation, splicing, and ribosomal functions	775:867	Disruption of this novel axis inhibited myeloid differentiation and H3K4 methylation as well as H2B glycosylation and impaired transcription of genes involved in myeloid differentiation, splicing, and ribosomal functions; this has implications for myelodysplastic syndrome (MDS) pathogenesis, as each of these processes are perturbed in the disease.
29556021	1	4	theme	myeloid	237:243	arg1	malignancies					245:256	myeloid malignancies	237:256	myeloid malignancies	237:256	ASXL1 plays key roles in epigenetic regulation of gene expression through methylation of histone H3K27, and disruption of ASXL1 drives myeloid malignancies, at least in part, via derepression of posterior HOXA loci.
29556021	0	5	theme	myeloid	80:86	arg1	malignancies					88:99	myeloid malignancies	80:99	myeloid malignancies	80:99	A novel ASXL1-OGT axis plays roles in H3K4 methylation and tumor suppression in myeloid malignancies.
29556021	5	6	theme	myeloid	1052:1058	arg1	compartment					1060:1070	the myeloid compartment	1048:1070	the myeloid compartment	1048:1070	This axis is responsible for tumor suppression in the myeloid compartment, as reactivation of OGT induced myeloid differentiation and reduced leukemogenecity both in vivo and in vitro.
29556021	3	7	theme	protein	556:562	arg1	complex					564:570	a protein complex	554:570	a protein complex containing HCFC1 and OGT	554:595	In this study, we demonstrate that ASXL1 is a part of a protein complex containing HCFC1 and OGT; OGT directly stabilizes ASXL1 by O-GlcNAcylation.
29556021	5	8	theme	reduced	1132:1138	arg1	leukemogenecity					1140:1154	reduced leukemogenecity	1132:1154	reduced leukemogenecity	1132:1154	This axis is responsible for tumor suppression in the myeloid compartment, as reactivation of OGT induced myeloid differentiation and reduced leukemogenecity both in vivo and in vitro.
29556021	6	9	theme	gene	1274:1277	arg1	activation					1279:1288	gene activation	1274:1288	gene activation by the ASXL1-OGT axis	1274:1310	Our data also suggest that MLL5, a known HCFC1/OGT-interacting protein, is responsible for gene activation by the ASXL1-OGT axis.
29556021	2	10	from	functions	413:421	arg1	modulation					435:444	modulation	435:444	modulation of the active histone mark	435:471	However, little is known about the identity of proteins that interact with ASXL1 and about the functions of ASXL1 in modulation of the active histone mark, such as H3K4 methylation.
29556021	7	11	theme	novel	1342:1346	arg1	roles					1348:1352	the novel roles	1338:1352	the novel roles of the ASXL1-OGT axis in H3K4 methylation and activation of transcription	1338:1426	These data shed light on the novel roles of the ASXL1-OGT axis in H3K4 methylation and activation of transcription.
29556021	4	12	theme	axis	673:676	arg1	Disruption					648:657	Disruption	648:657	Disruption of this novel axis	648:676	Disruption of this novel axis inhibited myeloid differentiation and H3K4 methylation as well as H2B glycosylation and impaired transcription of genes involved in myeloid differentiation, splicing, and ribosomal functions; this has implications for myelodysplastic syndrome (MDS) pathogenesis, as each of these processes are perturbed in the disease.
29556021	2	13	theme	histone	460:466	arg1	modulation					435:444	modulation	435:444	modulation of the active histone mark	435:471	However, little is known about the identity of proteins that interact with ASXL1 and about the functions of ASXL1 in modulation of the active histone mark, such as H3K4 methylation.
29556021	7	14	theme	ASXL1-OGT	1361:1369	arg1	axis					1371:1374	the ASXL1-OGT axis	1357:1374	the ASXL1-OGT axis	1357:1374	These data shed light on the novel roles of the ASXL1-OGT axis in H3K4 methylation and activation of transcription.
29556021	1	15	theme	gene	152:155	arg1	expression					157:166	gene expression	152:166	gene expression	152:166	ASXL1 plays key roles in epigenetic regulation of gene expression through methylation of histone H3K27, and disruption of ASXL1 drives myeloid malignancies, at least in part, via derepression of posterior HOXA loci.
29556021	2	16	theme	active	453:458	arg1	histone					460:466	the active histone	449:466	the active histone mark	449:471	However, little is known about the identity of proteins that interact with ASXL1 and about the functions of ASXL1 in modulation of the active histone mark, such as H3K4 methylation.
29556021	2	17	from	ASXL1	426:430	arg1	modulation					435:444	modulation	435:444	modulation of the active histone mark	435:471	However, little is known about the identity of proteins that interact with ASXL1 and about the functions of ASXL1 in modulation of the active histone mark, such as H3K4 methylation.
29556021	4	18	theme	myeloid	688:694	arg1	differentiation					696:710	myeloid differentiation	688:710	myeloid differentiation	688:710	Disruption of this novel axis inhibited myeloid differentiation and H3K4 methylation as well as H2B glycosylation and impaired transcription of genes involved in myeloid differentiation, splicing, and ribosomal functions; this has implications for myelodysplastic syndrome (MDS) pathogenesis, as each of these processes are perturbed in the disease.
29556021	1	19	theme	expression	157:166	arg1	regulation					138:147	epigenetic regulation	127:147	epigenetic regulation of gene expression through methylation of histone H3K27	127:203	ASXL1 plays key roles in epigenetic regulation of gene expression through methylation of histone H3K27, and disruption of ASXL1 drives myeloid malignancies, at least in part, via derepression of posterior HOXA loci.
29556021	0	20	theme	novel	2:6	arg1	axis					18:21	A novel ASXL1-OGT axis	0:21	A novel ASXL1-OGT axis	0:21	A novel ASXL1-OGT axis plays roles in H3K4 methylation and tumor suppression in myeloid malignancies.
29556021	5	21	theme	tumor	1027:1031	arg1	suppression					1033:1043	tumor suppression	1027:1043	tumor suppression in the myeloid compartment	1027:1070	This axis is responsible for tumor suppression in the myeloid compartment, as reactivation of OGT induced myeloid differentiation and reduced leukemogenecity both in vivo and in vitro.
29556021	7	22	theme	H3K4	1379:1382	arg1	methylation					1384:1394	H3K4 methylation	1379:1394	H3K4 methylation	1379:1394	These data shed light on the novel roles of the ASXL1-OGT axis in H3K4 methylation and activation of transcription.
29556021	7	23	theme	axis	1371:1374	arg1	roles					1348:1352	the novel roles	1338:1352	the novel roles of the ASXL1-OGT axis in H3K4 methylation and activation of transcription	1338:1426	These data shed light on the novel roles of the ASXL1-OGT axis in H3K4 methylation and activation of transcription.
29556021	3	24	theme	complex	564:570	arg1	ASXL1					535:539	ASXL1	535:539	ASXL1	535:539	In this study, we demonstrate that ASXL1 is a part of a protein complex containing HCFC1 and OGT; OGT directly stabilizes ASXL1 by O-GlcNAcylation.
29556021	3	24	theme	complex	564:570	arg1	part					546:549	a part	544:549	a part of a protein complex containing HCFC1 and OGT	544:595	In this study, we demonstrate that ASXL1 is a part of a protein complex containing HCFC1 and OGT; OGT directly stabilizes ASXL1 by O-GlcNAcylation.
29556021	5	25	theme	OGT	1092:1094	arg1	reactivation					1076:1087	reactivation	1076:1087	reactivation of OGT	1076:1094	This axis is responsible for tumor suppression in the myeloid compartment, as reactivation of OGT induced myeloid differentiation and reduced leukemogenecity both in vivo and in vitro.
29556021	2	26	dep	histone	460:466	arg1	mark					468:471	mark	468:471	mark	468:471	However, little is known about the identity of proteins that interact with ASXL1 and about the functions of ASXL1 in modulation of the active histone mark, such as H3K4 methylation.
29556021	4	27	theme	novel	667:671	arg1	axis					673:676	this novel axis	662:676	this novel axis	662:676	Disruption of this novel axis inhibited myeloid differentiation and H3K4 methylation as well as H2B glycosylation and impaired transcription of genes involved in myeloid differentiation, splicing, and ribosomal functions; this has implications for myelodysplastic syndrome (MDS) pathogenesis, as each of these processes are perturbed in the disease.
29556021	0	28	theme	ASXL1-OGT	8:16	arg1	axis					18:21	A novel ASXL1-OGT axis	0:21	A novel ASXL1-OGT axis	0:21	A novel ASXL1-OGT axis plays roles in H3K4 methylation and tumor suppression in myeloid malignancies.
29556021	2	29	theme	H3K4	482:485	arg1	methylation					487:497	H3K4 methylation	482:497	H3K4 methylation	482:497	However, little is known about the identity of proteins that interact with ASXL1 and about the functions of ASXL1 in modulation of the active histone mark, such as H3K4 methylation.
29556021	0	30	from	suppression	65:75	arg1	malignancies					88:99	myeloid malignancies	80:99	myeloid malignancies	80:99	A novel ASXL1-OGT axis plays roles in H3K4 methylation and tumor suppression in myeloid malignancies.
29556021	1	31	theme	histone	191:197	arg1	H3K27					199:203	histone H3K27	191:203	histone H3K27	191:203	ASXL1 plays key roles in epigenetic regulation of gene expression through methylation of histone H3K27, and disruption of ASXL1 drives myeloid malignancies, at least in part, via derepression of posterior HOXA loci.
29556021	2	32	theme	ASXL1	426:430	arg1	functions					413:421	the functions	409:421	the functions	409:421	However, little is known about the identity of proteins that interact with ASXL1 and about the functions of ASXL1 in modulation of the active histone mark, such as H3K4 methylation.
29556021	2	32	theme	ASXL1	426:430	arg1	methylation					487:497	H3K4 methylation	482:497	H3K4 methylation	482:497	However, little is known about the identity of proteins that interact with ASXL1 and about the functions of ASXL1 in modulation of the active histone mark, such as H3K4 methylation.
29556021	5	33	theme	myeloid	1104:1110	arg1	differentiation					1112:1126	myeloid differentiation	1104:1126	myeloid differentiation	1104:1126	This axis is responsible for tumor suppression in the myeloid compartment, as reactivation of OGT induced myeloid differentiation and reduced leukemogenecity both in vivo and in vitro.
29556021	1	34	theme	H3K27	199:203	arg1	methylation					176:186	methylation	176:186	methylation of histone H3K27	176:203	ASXL1 plays key roles in epigenetic regulation of gene expression through methylation of histone H3K27, and disruption of ASXL1 drives myeloid malignancies, at least in part, via derepression of posterior HOXA loci.
29556021	2	35	theme	proteins	365:372	arg1	identity					353:360	the identity	349:360	the identity of proteins that interact with ASXL1	349:397	However, little is known about the identity of proteins that interact with ASXL1 and about the functions of ASXL1 in modulation of the active histone mark, such as H3K4 methylation.
29556021	6	36	theme	ASXL1-OGT	1297:1305	arg1	axis					1307:1310	the ASXL1-OGT axis	1293:1310	the ASXL1-OGT axis	1293:1310	Our data also suggest that MLL5, a known HCFC1/OGT-interacting protein, is responsible for gene activation by the ASXL1-OGT axis.
29556021	6	37	theme	HCFC1/OGT-interacting	1224:1244	arg1	protein					1246:1252	a known HCFC1/OGT-interacting protein	1216:1252	a known HCFC1/OGT-interacting protein	1216:1252	Our data also suggest that MLL5, a known HCFC1/OGT-interacting protein, is responsible for gene activation by the ASXL1-OGT axis.
29556021	6	37	theme	HCFC1/OGT-interacting	1224:1244	arg1	MLL5					1210:1213	MLL5	1210:1213	MLL5	1210:1213	Our data also suggest that MLL5, a known HCFC1/OGT-interacting protein, is responsible for gene activation by the ASXL1-OGT axis.
29556021	0	38	theme	H3K4	38:41	arg1	methylation					43:53	H3K4 methylation	38:53	H3K4 methylation	38:53	A novel ASXL1-OGT axis plays roles in H3K4 methylation and tumor suppression in myeloid malignancies.
29556021	6	39	theme	known	1218:1222	arg1	protein					1246:1252	a known HCFC1/OGT-interacting protein	1216:1252	a known HCFC1/OGT-interacting protein	1216:1252	Our data also suggest that MLL5, a known HCFC1/OGT-interacting protein, is responsible for gene activation by the ASXL1-OGT axis.
29556021	6	39	theme	known	1218:1222	arg1	MLL5					1210:1213	MLL5	1210:1213	MLL5	1210:1213	Our data also suggest that MLL5, a known HCFC1/OGT-interacting protein, is responsible for gene activation by the ASXL1-OGT axis.
29556021	0	40	from	methylation	43:53	arg1	malignancies					88:99	myeloid malignancies	80:99	myeloid malignancies	80:99	A novel ASXL1-OGT axis plays roles in H3K4 methylation and tumor suppression in myeloid malignancies.
29556021	5	41	from	suppression	1033:1043	arg1	compartment					1060:1070	the myeloid compartment	1048:1070	the myeloid compartment	1048:1070	This axis is responsible for tumor suppression in the myeloid compartment, as reactivation of OGT induced myeloid differentiation and reduced leukemogenecity both in vivo and in vitro.
29556021	4	42	theme	ribosomal	849:857	arg1	functions					859:867	ribosomal functions	849:867	ribosomal functions	849:867	Disruption of this novel axis inhibited myeloid differentiation and H3K4 methylation as well as H2B glycosylation and impaired transcription of genes involved in myeloid differentiation, splicing, and ribosomal functions; this has implications for myelodysplastic syndrome (MDS) pathogenesis, as each of these processes are perturbed in the disease.
29556021	4	43	theme	H2B	744:746	arg1	glycosylation					748:760	H2B glycosylation	744:760	myeloid differentiation and H3K4 methylation as well as H2B glycosylation	688:760	Disruption of this novel axis inhibited myeloid differentiation and H3K4 methylation as well as H2B glycosylation and impaired transcription of genes involved in myeloid differentiation, splicing, and ribosomal functions; this has implications for myelodysplastic syndrome (MDS) pathogenesis, as each of these processes are perturbed in the disease.
29556021	4	44	theme	myeloid	810:816	arg1	differentiation					818:832	myeloid differentiation	810:832	myeloid differentiation	810:832	Disruption of this novel axis inhibited myeloid differentiation and H3K4 methylation as well as H2B glycosylation and impaired transcription of genes involved in myeloid differentiation, splicing, and ribosomal functions; this has implications for myelodysplastic syndrome (MDS) pathogenesis, as each of these processes are perturbed in the disease.
29556021	7	45	from	roles	1348:1352	arg1	activation					1400:1409	activation	1400:1409	activation of transcription	1400:1426	These data shed light on the novel roles of the ASXL1-OGT axis in H3K4 methylation and activation of transcription.
29556021	7	45	from	roles	1348:1352	arg1	methylation					1384:1394	H3K4 methylation	1379:1394	H3K4 methylation	1379:1394	These data shed light on the novel roles of the ASXL1-OGT axis in H3K4 methylation and activation of transcription.
29556021	7	46	theme	transcription	1414:1426	arg1	activation					1400:1409	activation	1400:1409	activation of transcription	1400:1426	These data shed light on the novel roles of the ASXL1-OGT axis in H3K4 methylation and activation of transcription.
29556021	7	46	theme	transcription	1414:1426	arg1	methylation					1384:1394	H3K4 methylation	1379:1394	H3K4 methylation	1379:1394	These data shed light on the novel roles of the ASXL1-OGT axis in H3K4 methylation and activation of transcription.
29556021	4	47	theme	H3K4	716:719	arg1	methylation					721:731	H3K4 methylation	716:731	H3K4 methylation	716:731	Disruption of this novel axis inhibited myeloid differentiation and H3K4 methylation as well as H2B glycosylation and impaired transcription of genes involved in myeloid differentiation, splicing, and ribosomal functions; this has implications for myelodysplastic syndrome (MDS) pathogenesis, as each of these processes are perturbed in the disease.
29556021	4	48	contain	has	875:877	arg1	this					870:873	this	870:873	this	870:873	Disruption of this novel axis inhibited myeloid differentiation and H3K4 methylation as well as H2B glycosylation and impaired transcription of genes involved in myeloid differentiation, splicing, and ribosomal functions; this has implications for myelodysplastic syndrome (MDS) pathogenesis, as each of these processes are perturbed in the disease.
29556021	4	48	contain	has	875:877	arg2	implications					879:890	implications	879:890	implications for myelodysplastic syndrome (MDS) pathogenesis	879:938	Disruption of this novel axis inhibited myeloid differentiation and H3K4 methylation as well as H2B glycosylation and impaired transcription of genes involved in myeloid differentiation, splicing, and ribosomal functions; this has implications for myelodysplastic syndrome (MDS) pathogenesis, as each of these processes are perturbed in the disease.
29556021	1	49	theme	key	114:116	arg1	roles					118:122	key roles	114:122	key roles	114:122	ASXL1 plays key roles in epigenetic regulation of gene expression through methylation of histone H3K27, and disruption of ASXL1 drives myeloid malignancies, at least in part, via derepression of posterior HOXA loci.
29556021	2	50	from	modulation	435:444	arg1	functions					413:421	the functions	409:421	the functions	409:421	However, little is known about the identity of proteins that interact with ASXL1 and about the functions of ASXL1 in modulation of the active histone mark, such as H3K4 methylation.
29556021	2	50	from	modulation	435:444	arg1	methylation					487:497	H3K4 methylation	482:497	H3K4 methylation	482:497	However, little is known about the identity of proteins that interact with ASXL1 and about the functions of ASXL1 in modulation of the active histone mark, such as H3K4 methylation.
29556021	4	51	theme	syndrome	912:919	arg1	pathogenesis					927:938	myelodysplastic syndrome (MDS) pathogenesis	896:938	myelodysplastic syndrome (MDS) pathogenesis	896:938	Disruption of this novel axis inhibited myeloid differentiation and H3K4 methylation as well as H2B glycosylation and impaired transcription of genes involved in myeloid differentiation, splicing, and ribosomal functions; this has implications for myelodysplastic syndrome (MDS) pathogenesis, as each of these processes are perturbed in the disease.
29556021	3	52	contain	containing	572:581	arg2	OGT					593:595	OGT	593:595	OGT	593:595	In this study, we demonstrate that ASXL1 is a part of a protein complex containing HCFC1 and OGT; OGT directly stabilizes ASXL1 by O-GlcNAcylation.
29556021	3	52	contain	containing	572:581	arg2	HCFC1					583:587	HCFC1	583:587	HCFC1	583:587	In this study, we demonstrate that ASXL1 is a part of a protein complex containing HCFC1 and OGT; OGT directly stabilizes ASXL1 by O-GlcNAcylation.
29556021	3	52	contain	containing	572:581	arg1	complex					564:570	a protein complex	554:570	a protein complex containing HCFC1 and OGT	554:595	In this study, we demonstrate that ASXL1 is a part of a protein complex containing HCFC1 and OGT; OGT directly stabilizes ASXL1 by O-GlcNAcylation.
29556021	4	53	theme	myelodysplastic	896:910	arg1	syndrome					912:919	myelodysplastic syndrome	896:919	myelodysplastic syndrome (MDS) pathogenesis	896:938	Disruption of this novel axis inhibited myeloid differentiation and H3K4 methylation as well as H2B glycosylation and impaired transcription of genes involved in myeloid differentiation, splicing, and ribosomal functions; this has implications for myelodysplastic syndrome (MDS) pathogenesis, as each of these processes are perturbed in the disease.
29556021	4	53	theme	myelodysplastic	896:910	arg1	MDS					922:924	MDS	922:924	MDS	922:924	Disruption of this novel axis inhibited myeloid differentiation and H3K4 methylation as well as H2B glycosylation and impaired transcription of genes involved in myeloid differentiation, splicing, and ribosomal functions; this has implications for myelodysplastic syndrome (MDS) pathogenesis, as each of these processes are perturbed in the disease.
29556021	1	54	theme	posterior	297:305	arg1	loci					312:315	posterior HOXA loci	297:315	posterior HOXA loci	297:315	ASXL1 plays key roles in epigenetic regulation of gene expression through methylation of histone H3K27, and disruption of ASXL1 drives myeloid malignancies, at least in part, via derepression of posterior HOXA loci.
29556021	1	55	theme	epigenetic	127:136	arg1	regulation					138:147	epigenetic regulation	127:147	epigenetic regulation of gene expression through methylation of histone H3K27	127:203	ASXL1 plays key roles in epigenetic regulation of gene expression through methylation of histone H3K27, and disruption of ASXL1 drives myeloid malignancies, at least in part, via derepression of posterior HOXA loci.
29556021	1	56	theme	ASXL1	224:228	arg1	disruption					210:219	disruption	210:219	disruption of ASXL1	210:228	ASXL1 plays key roles in epigenetic regulation of gene expression through methylation of histone H3K27, and disruption of ASXL1 drives myeloid malignancies, at least in part, via derepression of posterior HOXA loci.
26678539	1	0	theme	diverse	270:276	arg1	hematopoiesis					334:346	hematopoiesis	334:346	hematopoiesis	334:346	Mixed lineage leukemia 5 (MLL5) protein is a trithorax family histone 3 lysine 4 (H3K4) methyltransferase that regulates diverse biological processes, including cell cycle progression, hematopoiesis and cancer.
26678539	1	0	theme	diverse	270:276	arg1	progression					321:331	cell cycle progression	310:331	cell cycle progression	310:331	Mixed lineage leukemia 5 (MLL5) protein is a trithorax family histone 3 lysine 4 (H3K4) methyltransferase that regulates diverse biological processes, including cell cycle progression, hematopoiesis and cancer.
26678539	1	0	theme	diverse	270:276	arg1	processes					289:297	diverse biological processes	270:297	diverse biological processes	270:297	Mixed lineage leukemia 5 (MLL5) protein is a trithorax family histone 3 lysine 4 (H3K4) methyltransferase that regulates diverse biological processes, including cell cycle progression, hematopoiesis and cancer.
26678539	1	0	theme	diverse	270:276	arg1	cancer					352:357	cancer	352:357	cancer	352:357	Mixed lineage leukemia 5 (MLL5) protein is a trithorax family histone 3 lysine 4 (H3K4) methyltransferase that regulates diverse biological processes, including cell cycle progression, hematopoiesis and cancer.
26678539	10	1	theme	increased	1430:1438	arg1	expression					1440:1449	increased expression	1430:1449	increased expression of OGT and USP7 in human primary cervical adenocarcinomas	1430:1507	In addition, upregulation of MLL5 expression was correlated with increased expression of OGT and USP7 in human primary cervical adenocarcinomas.
26678539	9	2	theme	ternary	1303:1309	arg1	complex					1311:1317	a stable ternary complex	1294:1317	a stable ternary complex that is predominantly located in the nucleus	1294:1362	Co-immunoprecipitation and co-immunostaining assays revealed that MLL5, OGT and USP7 interact with each other to form a stable ternary complex that is predominantly located in the nucleus.
26678539	9	2	theme	ternary	1303:1309	arg1	located					1341:1347	located	1341:1347	located	1341:1347	Co-immunoprecipitation and co-immunostaining assays revealed that MLL5, OGT and USP7 interact with each other to form a stable ternary complex that is predominantly located in the nucleus.
26678539	5	3	theme	novel	849:853	arg1	protein					871:877	a novel MLL5-associated protein	847:877	a novel MLL5-associated protein using mass spectrometry	847:901	We further identified deubiquitinase USP7 as a novel MLL5-associated protein using mass spectrometry.
26678539	5	3	theme	novel	849:853	arg1	USP7					839:842	deubiquitinase USP7	824:842	deubiquitinase USP7	824:842	We further identified deubiquitinase USP7 as a novel MLL5-associated protein using mass spectrometry.
26678539	11	4	theme	functional	1652:1661	arg1	interplay					1663:1671	the functional interplay	1648:1671	the functional interplay among O-GlcNAc transferase, deubiquitinase and histone methyltransferase	1648:1744	Our results collectively reveal a novel molecular mechanism underlying regulation of MLL5 protein stability and provide new insights into the functional interplay among O-GlcNAc transferase, deubiquitinase and histone methyltransferase.
26678539	1	5	theme	biological	278:287	arg1	hematopoiesis					334:346	hematopoiesis	334:346	hematopoiesis	334:346	Mixed lineage leukemia 5 (MLL5) protein is a trithorax family histone 3 lysine 4 (H3K4) methyltransferase that regulates diverse biological processes, including cell cycle progression, hematopoiesis and cancer.
26678539	1	5	theme	biological	278:287	arg1	progression					321:331	cell cycle progression	310:331	cell cycle progression	310:331	Mixed lineage leukemia 5 (MLL5) protein is a trithorax family histone 3 lysine 4 (H3K4) methyltransferase that regulates diverse biological processes, including cell cycle progression, hematopoiesis and cancer.
26678539	1	5	theme	biological	278:287	arg1	processes					289:297	diverse biological processes	270:297	diverse biological processes	270:297	Mixed lineage leukemia 5 (MLL5) protein is a trithorax family histone 3 lysine 4 (H3K4) methyltransferase that regulates diverse biological processes, including cell cycle progression, hematopoiesis and cancer.
26678539	1	5	theme	biological	278:287	arg1	cancer					352:357	cancer	352:357	cancer	352:357	Mixed lineage leukemia 5 (MLL5) protein is a trithorax family histone 3 lysine 4 (H3K4) methyltransferase that regulates diverse biological processes, including cell cycle progression, hematopoiesis and cancer.
26678539	9	6	from	nucleus	1356:1362	arg1	complex					1311:1317	a stable ternary complex	1294:1317	a stable ternary complex that is predominantly located in the nucleus	1294:1362	Co-immunoprecipitation and co-immunostaining assays revealed that MLL5, OGT and USP7 interact with each other to form a stable ternary complex that is predominantly located in the nucleus.
26678539	9	6	from	nucleus	1356:1362	arg1	located					1341:1347	located	1341:1347	located	1341:1347	Co-immunoprecipitation and co-immunostaining assays revealed that MLL5, OGT and USP7 interact with each other to form a stable ternary complex that is predominantly located in the nucleus.
26678539	5	7	theme	MLL5-associated	855:869	arg1	protein					871:877	a novel MLL5-associated protein	847:877	a novel MLL5-associated protein using mass spectrometry	847:901	We further identified deubiquitinase USP7 as a novel MLL5-associated protein using mass spectrometry.
26678539	5	7	theme	MLL5-associated	855:869	arg1	USP7					839:842	deubiquitinase USP7	824:842	deubiquitinase USP7	824:842	We further identified deubiquitinase USP7 as a novel MLL5-associated protein using mass spectrometry.
26678539	1	8	theme	trithorax	194:202	arg1	protein					181:187	Mixed lineage leukemia 5 (MLL5) protein	149:187	Mixed lineage leukemia 5 (MLL5) protein	149:187	Mixed lineage leukemia 5 (MLL5) protein is a trithorax family histone 3 lysine 4 (H3K4) methyltransferase that regulates diverse biological processes, including cell cycle progression, hematopoiesis and cancer.
26678539	1	8	theme	trithorax	194:202	arg1	methyltransferase					237:253	a trithorax family histone 3 lysine 4 (H3K4) methyltransferase	192:253	a trithorax family histone 3 lysine 4 (H3K4) methyltransferase that regulates diverse biological processes, including cell cycle progression, hematopoiesis and cancer	192:357	Mixed lineage leukemia 5 (MLL5) protein is a trithorax family histone 3 lysine 4 (H3K4) methyltransferase that regulates diverse biological processes, including cell cycle progression, hematopoiesis and cancer.
26678539	0	9	theme	O-GlcNac	80:87	arg1	OGT					102:104	OGT	102:104	OGT	102:104	Mixed Lineage Leukemia 5 (MLL5) Protein Stability Is Cooperatively Regulated by O-GlcNac Transferase (OGT) and Ubiquitin Specific Protease 7 (USP7).
26678539	0	9	theme	O-GlcNac	80:87	arg1	Transferase					89:99	O-GlcNac Transferase	80:99	O-GlcNac Transferase (OGT)	80:105	Mixed Lineage Leukemia 5 (MLL5) Protein Stability Is Cooperatively Regulated by O-GlcNac Transferase (OGT) and Ubiquitin Specific Protease 7 (USP7).
26678539	10	10	theme	cervical	1484:1491	arg1	adenocarcinomas					1493:1507	human primary cervical adenocarcinomas	1470:1507	human primary cervical adenocarcinomas	1470:1507	In addition, upregulation of MLL5 expression was correlated with increased expression of OGT and USP7 in human primary cervical adenocarcinomas.
26678539	8	11	theme	increased	1150:1158	arg1	stability					1165:1173	increased MLL5 stability	1150:1173	increased MLL5 stability	1150:1173	Conversely, overexpression of USP7, but not a catalytically inactive USP7 mutant, led to decreased ubiquitylation and increased MLL5 stability.
26678539	3	12	theme	MLL5	472:475	arg1	stability					485:493	MLL5 protein stability	472:493	MLL5 protein stability	472:493	Here, we showed that MLL5 protein stability is cooperatively regulated by O-GlcNAc transferase (OGT) and ubiquitin-specific protease 7 (USP7).
26678539	1	13	theme	family	204:209	arg1	protein					181:187	Mixed lineage leukemia 5 (MLL5) protein	149:187	Mixed lineage leukemia 5 (MLL5) protein	149:187	Mixed lineage leukemia 5 (MLL5) protein is a trithorax family histone 3 lysine 4 (H3K4) methyltransferase that regulates diverse biological processes, including cell cycle progression, hematopoiesis and cancer.
26678539	1	13	theme	family	204:209	arg1	methyltransferase					237:253	a trithorax family histone 3 lysine 4 (H3K4) methyltransferase	192:253	a trithorax family histone 3 lysine 4 (H3K4) methyltransferase that regulates diverse biological processes, including cell cycle progression, hematopoiesis and cancer	192:357	Mixed lineage leukemia 5 (MLL5) protein is a trithorax family histone 3 lysine 4 (H3K4) methyltransferase that regulates diverse biological processes, including cell cycle progression, hematopoiesis and cancer.
26678539	11	14	theme	O-GlcNAc	1679:1686	arg1	transferase					1688:1698	O-GlcNAc transferase	1679:1698	O-GlcNAc transferase	1679:1698	Our results collectively reveal a novel molecular mechanism underlying regulation of MLL5 protein stability and provide new insights into the functional interplay among O-GlcNAc transferase, deubiquitinase and histone methyltransferase.
26678539	11	15	theme	protein	1600:1606	arg1	stability					1608:1616	MLL5 protein stability	1595:1616	MLL5 protein stability	1595:1616	Our results collectively reveal a novel molecular mechanism underlying regulation of MLL5 protein stability and provide new insights into the functional interplay among O-GlcNAc transferase, deubiquitinase and histone methyltransferase.
26678539	3	16	theme	protein	477:483	arg1	stability					485:493	MLL5 protein stability	472:493	MLL5 protein stability	472:493	Here, we showed that MLL5 protein stability is cooperatively regulated by O-GlcNAc transferase (OGT) and ubiquitin-specific protease 7 (USP7).
26678539	1	17	theme	histone	211:217	arg1	protein					181:187	Mixed lineage leukemia 5 (MLL5) protein	149:187	Mixed lineage leukemia 5 (MLL5) protein	149:187	Mixed lineage leukemia 5 (MLL5) protein is a trithorax family histone 3 lysine 4 (H3K4) methyltransferase that regulates diverse biological processes, including cell cycle progression, hematopoiesis and cancer.
26678539	1	17	theme	histone	211:217	arg1	methyltransferase					237:253	a trithorax family histone 3 lysine 4 (H3K4) methyltransferase	192:253	a trithorax family histone 3 lysine 4 (H3K4) methyltransferase that regulates diverse biological processes, including cell cycle progression, hematopoiesis and cancer	192:357	Mixed lineage leukemia 5 (MLL5) protein is a trithorax family histone 3 lysine 4 (H3K4) methyltransferase that regulates diverse biological processes, including cell cycle progression, hematopoiesis and cancer.
26678539	11	18	theme	new	1630:1632	arg1	insights					1634:1641	new insights	1630:1641	new insights into the functional interplay among O-GlcNAc transferase, deubiquitinase and histone methyltransferase	1630:1744	Our results collectively reveal a novel molecular mechanism underlying regulation of MLL5 protein stability and provide new insights into the functional interplay among O-GlcNAc transferase, deubiquitinase and histone methyltransferase.
26678539	4	19	from	Depletion	594:602	arg1	cells					614:618	cells	614:618	cells	614:618	Depletion of OGT in cells led to a decrease in the MLL5 protein level through ubiquitin/proteasome-dependent proteolytic degradation, whereas ectopic expression of OGT protein suppressed MLL5 ubiquitylation.
26678539	1	20	theme	cell	310:313	arg1	progression					321:331	cell cycle progression	310:331	cell cycle progression	310:331	Mixed lineage leukemia 5 (MLL5) protein is a trithorax family histone 3 lysine 4 (H3K4) methyltransferase that regulates diverse biological processes, including cell cycle progression, hematopoiesis and cancer.
26678539	4	21	theme	MLL5	781:784	arg1	ubiquitylation					786:799	MLL5 ubiquitylation	781:799	MLL5 ubiquitylation	781:799	Depletion of OGT in cells led to a decrease in the MLL5 protein level through ubiquitin/proteasome-dependent proteolytic degradation, whereas ectopic expression of OGT protein suppressed MLL5 ubiquitylation.
26678539	10	22	theme	expression	1399:1408	arg1	upregulation					1378:1389	upregulation	1378:1389	upregulation of MLL5 expression	1378:1408	In addition, upregulation of MLL5 expression was correlated with increased expression of OGT and USP7 in human primary cervical adenocarcinomas.
26678539	0	23	theme	Mixed	0:4	arg1	Leukemia					14:21	Mixed Lineage Leukemia 5	0:23	Mixed Lineage Leukemia 5 (MLL5) Protein Stability	0:48	Mixed Lineage Leukemia 5 (MLL5) Protein Stability Is Cooperatively Regulated by O-GlcNac Transferase (OGT) and Ubiquitin Specific Protease 7 (USP7).
26678539	0	23	theme	Mixed	0:4	arg1	MLL5					26:29	MLL5	26:29	MLL5	26:29	Mixed Lineage Leukemia 5 (MLL5) Protein Stability Is Cooperatively Regulated by O-GlcNac Transferase (OGT) and Ubiquitin Specific Protease 7 (USP7).
26678539	10	24	theme	OGT	1454:1456	arg1	expression					1440:1449	increased expression	1430:1449	increased expression of OGT and USP7 in human primary cervical adenocarcinomas	1430:1507	In addition, upregulation of MLL5 expression was correlated with increased expression of OGT and USP7 in human primary cervical adenocarcinomas.
26678539	0	25	theme	Lineage	6:12	arg1	Leukemia					14:21	Mixed Lineage Leukemia 5	0:23	Mixed Lineage Leukemia 5 (MLL5) Protein Stability	0:48	Mixed Lineage Leukemia 5 (MLL5) Protein Stability Is Cooperatively Regulated by O-GlcNac Transferase (OGT) and Ubiquitin Specific Protease 7 (USP7).
26678539	0	25	theme	Lineage	6:12	arg1	MLL5					26:29	MLL5	26:29	MLL5	26:29	Mixed Lineage Leukemia 5 (MLL5) Protein Stability Is Cooperatively Regulated by O-GlcNac Transferase (OGT) and Ubiquitin Specific Protease 7 (USP7).
26678539	1	26	theme	cycle	315:319	arg1	progression					321:331	cell cycle progression	310:331	cell cycle progression	310:331	Mixed lineage leukemia 5 (MLL5) protein is a trithorax family histone 3 lysine 4 (H3K4) methyltransferase that regulates diverse biological processes, including cell cycle progression, hematopoiesis and cancer.
26678539	10	27	theme	MLL5	1394:1397	arg1	expression					1399:1408	MLL5 expression	1394:1408	MLL5 expression	1394:1408	In addition, upregulation of MLL5 expression was correlated with increased expression of OGT and USP7 in human primary cervical adenocarcinomas.
26678539	4	28	theme	MLL5	645:648	arg1	level					658:662	the MLL5 protein level	641:662	the MLL5 protein level through ubiquitin/proteasome-dependent proteolytic degradation	641:725	Depletion of OGT in cells led to a decrease in the MLL5 protein level through ubiquitin/proteasome-dependent proteolytic degradation, whereas ectopic expression of OGT protein suppressed MLL5 ubiquitylation.
26678539	7	29	theme	protein	1023:1029	arg1	degradation					1003:1013	degradation	1003:1013	degradation of MLL5 protein	1003:1029	Loss of USP7 induced degradation of MLL5 protein.
26678539	5	30	theme	deubiquitinase	824:837	arg1	protein					871:877	a novel MLL5-associated protein	847:877	a novel MLL5-associated protein using mass spectrometry	847:901	We further identified deubiquitinase USP7 as a novel MLL5-associated protein using mass spectrometry.
26678539	5	30	theme	deubiquitinase	824:837	arg1	USP7					839:842	deubiquitinase USP7	824:842	deubiquitinase USP7	824:842	We further identified deubiquitinase USP7 as a novel MLL5-associated protein using mass spectrometry.
26678539	2	31	theme	MLL5	384:387	arg1	stability					397:405	MLL5 protein stability	384:405	MLL5 protein stability	384:405	The mechanisms by which MLL5 protein stability is regulated have remained unclear to date.
26678539	6	32	theme	direct	945:950	arg1	binding					952:958	direct binding	945:958	direct binding	945:958	USP7 stabilized the MLL5 protein through direct binding and deubiquitylation.
26678539	9	33	theme	co-immunostaining	1203:1219	arg1	assays					1221:1226	co-immunostaining assays	1203:1226	co-immunostaining assays	1203:1226	Co-immunoprecipitation and co-immunostaining assays revealed that MLL5, OGT and USP7 interact with each other to form a stable ternary complex that is predominantly located in the nucleus.
26678539	11	34	theme	novel	1544:1548	arg1	mechanism					1560:1568	a novel molecular mechanism	1542:1568	a novel molecular mechanism underlying regulation of MLL5 protein stability	1542:1616	Our results collectively reveal a novel molecular mechanism underlying regulation of MLL5 protein stability and provide new insights into the functional interplay among O-GlcNAc transferase, deubiquitinase and histone methyltransferase.
26678539	4	35	theme	ubiquitin/proteasome-dependent	672:701	arg1	degradation					715:725	ubiquitin/proteasome-dependent proteolytic degradation	672:725	ubiquitin/proteasome-dependent proteolytic degradation	672:725	Depletion of OGT in cells led to a decrease in the MLL5 protein level through ubiquitin/proteasome-dependent proteolytic degradation, whereas ectopic expression of OGT protein suppressed MLL5 ubiquitylation.
26678539	1	36	theme	Mixed	149:153	arg1	leukemia					163:170	Mixed lineage leukemia 5	149:172	Mixed lineage leukemia 5 (MLL5) protein	149:187	Mixed lineage leukemia 5 (MLL5) protein is a trithorax family histone 3 lysine 4 (H3K4) methyltransferase that regulates diverse biological processes, including cell cycle progression, hematopoiesis and cancer.
26678539	1	36	theme	Mixed	149:153	arg1	MLL5					175:178	MLL5	175:178	MLL5	175:178	Mixed lineage leukemia 5 (MLL5) protein is a trithorax family histone 3 lysine 4 (H3K4) methyltransferase that regulates diverse biological processes, including cell cycle progression, hematopoiesis and cancer.
26678539	1	37	theme	lysine	221:226	arg1	protein					181:187	Mixed lineage leukemia 5 (MLL5) protein	149:187	Mixed lineage leukemia 5 (MLL5) protein	149:187	Mixed lineage leukemia 5 (MLL5) protein is a trithorax family histone 3 lysine 4 (H3K4) methyltransferase that regulates diverse biological processes, including cell cycle progression, hematopoiesis and cancer.
26678539	1	37	theme	lysine	221:226	arg1	methyltransferase					237:253	a trithorax family histone 3 lysine 4 (H3K4) methyltransferase	192:253	a trithorax family histone 3 lysine 4 (H3K4) methyltransferase that regulates diverse biological processes, including cell cycle progression, hematopoiesis and cancer	192:357	Mixed lineage leukemia 5 (MLL5) protein is a trithorax family histone 3 lysine 4 (H3K4) methyltransferase that regulates diverse biological processes, including cell cycle progression, hematopoiesis and cancer.
26678539	8	38	theme	USP7	1062:1065	arg1	overexpression					1044:1057	overexpression	1044:1057	overexpression of USP7	1044:1065	Conversely, overexpression of USP7, but not a catalytically inactive USP7 mutant, led to decreased ubiquitylation and increased MLL5 stability.
26678539	4	39	theme	protein	762:768	arg1	expression					744:753	ectopic expression	736:753	ectopic expression of OGT protein	736:768	Depletion of OGT in cells led to a decrease in the MLL5 protein level through ubiquitin/proteasome-dependent proteolytic degradation, whereas ectopic expression of OGT protein suppressed MLL5 ubiquitylation.
26678539	1	40	theme	lineage	155:161	arg1	leukemia					163:170	Mixed lineage leukemia 5	149:172	Mixed lineage leukemia 5 (MLL5) protein	149:187	Mixed lineage leukemia 5 (MLL5) protein is a trithorax family histone 3 lysine 4 (H3K4) methyltransferase that regulates diverse biological processes, including cell cycle progression, hematopoiesis and cancer.
26678539	1	40	theme	lineage	155:161	arg1	MLL5					175:178	MLL5	175:178	MLL5	175:178	Mixed lineage leukemia 5 (MLL5) protein is a trithorax family histone 3 lysine 4 (H3K4) methyltransferase that regulates diverse biological processes, including cell cycle progression, hematopoiesis and cancer.
26678539	0	41	theme	Leukemia	14:21	arg1	Stability					40:48	Mixed Lineage Leukemia 5 (MLL5) Protein Stability	0:48	Mixed Lineage Leukemia 5 (MLL5) Protein Stability	0:48	Mixed Lineage Leukemia 5 (MLL5) Protein Stability Is Cooperatively Regulated by O-GlcNac Transferase (OGT) and Ubiquitin Specific Protease 7 (USP7).
26678539	10	42	theme	human	1470:1474	arg1	adenocarcinomas					1493:1507	human primary cervical adenocarcinomas	1470:1507	human primary cervical adenocarcinomas	1470:1507	In addition, upregulation of MLL5 expression was correlated with increased expression of OGT and USP7 in human primary cervical adenocarcinomas.
26678539	4	43	theme	protein	650:656	arg1	level					658:662	the MLL5 protein level	641:662	the MLL5 protein level through ubiquitin/proteasome-dependent proteolytic degradation	641:725	Depletion of OGT in cells led to a decrease in the MLL5 protein level through ubiquitin/proteasome-dependent proteolytic degradation, whereas ectopic expression of OGT protein suppressed MLL5 ubiquitylation.
26678539	1	44	theme	leukemia	163:170	arg1	protein					181:187	Mixed lineage leukemia 5 (MLL5) protein	149:187	Mixed lineage leukemia 5 (MLL5) protein	149:187	Mixed lineage leukemia 5 (MLL5) protein is a trithorax family histone 3 lysine 4 (H3K4) methyltransferase that regulates diverse biological processes, including cell cycle progression, hematopoiesis and cancer.
26678539	1	44	theme	leukemia	163:170	arg1	methyltransferase					237:253	a trithorax family histone 3 lysine 4 (H3K4) methyltransferase	192:253	a trithorax family histone 3 lysine 4 (H3K4) methyltransferase that regulates diverse biological processes, including cell cycle progression, hematopoiesis and cancer	192:357	Mixed lineage leukemia 5 (MLL5) protein is a trithorax family histone 3 lysine 4 (H3K4) methyltransferase that regulates diverse biological processes, including cell cycle progression, hematopoiesis and cancer.
26678539	6	45	theme	MLL5	924:927	arg1	protein					929:935	the MLL5 protein	920:935	the MLL5 protein	920:935	USP7 stabilized the MLL5 protein through direct binding and deubiquitylation.
26678539	0	46	theme	Ubiquitin	111:119	arg1	Protease					130:137	Ubiquitin Specific Protease 7	111:139	Ubiquitin Specific Protease 7 (USP7)	111:146	Mixed Lineage Leukemia 5 (MLL5) Protein Stability Is Cooperatively Regulated by O-GlcNac Transferase (OGT) and Ubiquitin Specific Protease 7 (USP7).
26678539	0	46	theme	Ubiquitin	111:119	arg1	USP7					142:145	USP7	142:145	USP7	142:145	Mixed Lineage Leukemia 5 (MLL5) Protein Stability Is Cooperatively Regulated by O-GlcNac Transferase (OGT) and Ubiquitin Specific Protease 7 (USP7).
26678539	11	47	theme	histone	1720:1726	arg1	methyltransferase					1728:1744	histone methyltransferase	1720:1744	histone methyltransferase	1720:1744	Our results collectively reveal a novel molecular mechanism underlying regulation of MLL5 protein stability and provide new insights into the functional interplay among O-GlcNAc transferase, deubiquitinase and histone methyltransferase.
26678539	4	48	theme	OGT	758:760	arg1	protein					762:768	OGT protein	758:768	OGT protein	758:768	Depletion of OGT in cells led to a decrease in the MLL5 protein level through ubiquitin/proteasome-dependent proteolytic degradation, whereas ectopic expression of OGT protein suppressed MLL5 ubiquitylation.
26678539	1	49	theme	H3K4	231:234	arg1	protein					181:187	Mixed lineage leukemia 5 (MLL5) protein	149:187	Mixed lineage leukemia 5 (MLL5) protein	149:187	Mixed lineage leukemia 5 (MLL5) protein is a trithorax family histone 3 lysine 4 (H3K4) methyltransferase that regulates diverse biological processes, including cell cycle progression, hematopoiesis and cancer.
26678539	1	49	theme	H3K4	231:234	arg1	methyltransferase					237:253	a trithorax family histone 3 lysine 4 (H3K4) methyltransferase	192:253	a trithorax family histone 3 lysine 4 (H3K4) methyltransferase that regulates diverse biological processes, including cell cycle progression, hematopoiesis and cancer	192:357	Mixed lineage leukemia 5 (MLL5) protein is a trithorax family histone 3 lysine 4 (H3K4) methyltransferase that regulates diverse biological processes, including cell cycle progression, hematopoiesis and cancer.
26678539	10	50	theme	USP7	1462:1465	arg1	expression					1440:1449	increased expression	1430:1449	increased expression of OGT and USP7 in human primary cervical adenocarcinomas	1430:1507	In addition, upregulation of MLL5 expression was correlated with increased expression of OGT and USP7 in human primary cervical adenocarcinomas.
26678539	7	51	theme	USP7	990:993	arg1	Loss					982:985	Loss	982:985	Loss of USP7	982:993	Loss of USP7 induced degradation of MLL5 protein.
26678539	8	52	theme	MLL5	1160:1163	arg1	stability					1165:1173	increased MLL5 stability	1150:1173	increased MLL5 stability	1150:1173	Conversely, overexpression of USP7, but not a catalytically inactive USP7 mutant, led to decreased ubiquitylation and increased MLL5 stability.
26678539	0	53	theme	Protein	32:38	arg1	Stability					40:48	Mixed Lineage Leukemia 5 (MLL5) Protein Stability	0:48	Mixed Lineage Leukemia 5 (MLL5) Protein Stability	0:48	Mixed Lineage Leukemia 5 (MLL5) Protein Stability Is Cooperatively Regulated by O-GlcNac Transferase (OGT) and Ubiquitin Specific Protease 7 (USP7).
26678539	8	54	theme	decreased	1121:1129	arg1	ubiquitylation					1131:1144	decreased ubiquitylation	1121:1144	decreased ubiquitylation	1121:1144	Conversely, overexpression of USP7, but not a catalytically inactive USP7 mutant, led to decreased ubiquitylation and increased MLL5 stability.
26678539	7	55	theme	MLL5	1018:1021	arg1	protein					1023:1029	MLL5 protein	1018:1029	MLL5 protein	1018:1029	Loss of USP7 induced degradation of MLL5 protein.
26678539	10	56	theme	primary	1476:1482	arg1	adenocarcinomas					1493:1507	human primary cervical adenocarcinomas	1470:1507	human primary cervical adenocarcinomas	1470:1507	In addition, upregulation of MLL5 expression was correlated with increased expression of OGT and USP7 in human primary cervical adenocarcinomas.
26678539	9	57	theme	stable	1296:1301	arg1	complex					1311:1317	a stable ternary complex	1294:1317	a stable ternary complex that is predominantly located in the nucleus	1294:1362	Co-immunoprecipitation and co-immunostaining assays revealed that MLL5, OGT and USP7 interact with each other to form a stable ternary complex that is predominantly located in the nucleus.
26678539	9	57	theme	stable	1296:1301	arg1	located					1341:1347	located	1341:1347	located	1341:1347	Co-immunoprecipitation and co-immunostaining assays revealed that MLL5, OGT and USP7 interact with each other to form a stable ternary complex that is predominantly located in the nucleus.
26678539	0	58	theme	Specific	121:128	arg1	Protease					130:137	Ubiquitin Specific Protease 7	111:139	Ubiquitin Specific Protease 7 (USP7)	111:146	Mixed Lineage Leukemia 5 (MLL5) Protein Stability Is Cooperatively Regulated by O-GlcNac Transferase (OGT) and Ubiquitin Specific Protease 7 (USP7).
26678539	0	58	theme	Specific	121:128	arg1	USP7					142:145	USP7	142:145	USP7	142:145	Mixed Lineage Leukemia 5 (MLL5) Protein Stability Is Cooperatively Regulated by O-GlcNac Transferase (OGT) and Ubiquitin Specific Protease 7 (USP7).
26678539	3	59	theme	O-GlcNAc	525:532	arg1	transferase					534:544	O-GlcNAc transferase	525:544	O-GlcNAc transferase (OGT)	525:550	Here, we showed that MLL5 protein stability is cooperatively regulated by O-GlcNAc transferase (OGT) and ubiquitin-specific protease 7 (USP7).
26678539	3	59	theme	O-GlcNAc	525:532	arg1	OGT					547:549	OGT	547:549	OGT	547:549	Here, we showed that MLL5 protein stability is cooperatively regulated by O-GlcNAc transferase (OGT) and ubiquitin-specific protease 7 (USP7).
26678539	11	60	theme	MLL5	1595:1598	arg1	stability					1608:1616	MLL5 protein stability	1595:1616	MLL5 protein stability	1595:1616	Our results collectively reveal a novel molecular mechanism underlying regulation of MLL5 protein stability and provide new insights into the functional interplay among O-GlcNAc transferase, deubiquitinase and histone methyltransferase.
26678539	9	61	from	located	1341:1347	arg1	nucleus					1356:1362	the nucleus	1352:1362	the nucleus	1352:1362	Co-immunoprecipitation and co-immunostaining assays revealed that MLL5, OGT and USP7 interact with each other to form a stable ternary complex that is predominantly located in the nucleus.
26678539	11	62	theme	molecular	1550:1558	arg1	mechanism					1560:1568	a novel molecular mechanism	1542:1568	a novel molecular mechanism underlying regulation of MLL5 protein stability	1542:1616	Our results collectively reveal a novel molecular mechanism underlying regulation of MLL5 protein stability and provide new insights into the functional interplay among O-GlcNAc transferase, deubiquitinase and histone methyltransferase.
26678539	8	63	theme	inactive	1092:1099	arg1	mutant					1106:1111	a catalytically inactive USP7 mutant	1076:1111	a catalytically inactive USP7 mutant	1076:1111	Conversely, overexpression of USP7, but not a catalytically inactive USP7 mutant, led to decreased ubiquitylation and increased MLL5 stability.
26678539	5	64	theme	mass	885:888	arg1	spectrometry					890:901	mass spectrometry	885:901	mass spectrometry	885:901	We further identified deubiquitinase USP7 as a novel MLL5-associated protein using mass spectrometry.
26678539	4	65	from	decrease	629:636	arg1	level					658:662	the MLL5 protein level	641:662	the MLL5 protein level through ubiquitin/proteasome-dependent proteolytic degradation	641:725	Depletion of OGT in cells led to a decrease in the MLL5 protein level through ubiquitin/proteasome-dependent proteolytic degradation, whereas ectopic expression of OGT protein suppressed MLL5 ubiquitylation.
26678539	4	66	theme	proteolytic	703:713	arg1	degradation					715:725	ubiquitin/proteasome-dependent proteolytic degradation	672:725	ubiquitin/proteasome-dependent proteolytic degradation	672:725	Depletion of OGT in cells led to a decrease in the MLL5 protein level through ubiquitin/proteasome-dependent proteolytic degradation, whereas ectopic expression of OGT protein suppressed MLL5 ubiquitylation.
26678539	3	67	theme	ubiquitin-specific	556:573	arg1	protease					575:582	ubiquitin-specific protease 7	556:584	ubiquitin-specific protease 7 (USP7)	556:591	Here, we showed that MLL5 protein stability is cooperatively regulated by O-GlcNAc transferase (OGT) and ubiquitin-specific protease 7 (USP7).
26678539	3	67	theme	ubiquitin-specific	556:573	arg1	USP7					587:590	USP7	587:590	USP7	587:590	Here, we showed that MLL5 protein stability is cooperatively regulated by O-GlcNAc transferase (OGT) and ubiquitin-specific protease 7 (USP7).
26678539	4	68	theme	OGT	607:609	arg1	Depletion					594:602	Depletion	594:602	Depletion of OGT in cells	594:618	Depletion of OGT in cells led to a decrease in the MLL5 protein level through ubiquitin/proteasome-dependent proteolytic degradation, whereas ectopic expression of OGT protein suppressed MLL5 ubiquitylation.
26678539	9	69	located	located	1341:1347	arg2	complex					1311:1317	a stable ternary complex	1294:1317	a stable ternary complex that is predominantly located in the nucleus	1294:1362	Co-immunoprecipitation and co-immunostaining assays revealed that MLL5, OGT and USP7 interact with each other to form a stable ternary complex that is predominantly located in the nucleus.
26678539	9	69	located	located	1341:1347	arg2	located					1341:1347	located	1341:1347	located	1341:1347	Co-immunoprecipitation and co-immunostaining assays revealed that MLL5, OGT and USP7 interact with each other to form a stable ternary complex that is predominantly located in the nucleus.
26678539	9	69	located	located	1341:1347	arg1	nucleus					1356:1362	the nucleus	1352:1362	the nucleus	1352:1362	Co-immunoprecipitation and co-immunostaining assays revealed that MLL5, OGT and USP7 interact with each other to form a stable ternary complex that is predominantly located in the nucleus.
26678539	8	70	theme	USP7	1101:1104	arg1	mutant					1106:1111	a catalytically inactive USP7 mutant	1076:1111	a catalytically inactive USP7 mutant	1076:1111	Conversely, overexpression of USP7, but not a catalytically inactive USP7 mutant, led to decreased ubiquitylation and increased MLL5 stability.
26678539	4	71	theme	ectopic	736:742	arg1	expression					744:753	ectopic expression	736:753	ectopic expression of OGT protein	736:768	Depletion of OGT in cells led to a decrease in the MLL5 protein level through ubiquitin/proteasome-dependent proteolytic degradation, whereas ectopic expression of OGT protein suppressed MLL5 ubiquitylation.
26678539	11	72	theme	stability	1608:1616	arg1	regulation					1581:1590	regulation	1581:1590	regulation of MLL5 protein stability	1581:1616	Our results collectively reveal a novel molecular mechanism underlying regulation of MLL5 protein stability and provide new insights into the functional interplay among O-GlcNAc transferase, deubiquitinase and histone methyltransferase.
26678539	2	73	theme	protein	389:395	arg1	stability					397:405	MLL5 protein stability	384:405	MLL5 protein stability	384:405	The mechanisms by which MLL5 protein stability is regulated have remained unclear to date.
26678539	10	74	from	expression	1440:1449	arg1	adenocarcinomas					1493:1507	human primary cervical adenocarcinomas	1470:1507	human primary cervical adenocarcinomas	1470:1507	In addition, upregulation of MLL5 expression was correlated with increased expression of OGT and USP7 in human primary cervical adenocarcinomas.
27009840	4	0	theme	NF-κB	939:943	arg1	activation					945:954	TAB3mediated NF-κB activation	926:954	TAB3mediated NF-κB activation	926:954	O-GlcNAcylation of TAB3 was induced by p38 MAPK and it in turn enhances the TAK1 mediated p38MAPK activation, which forms the positive feedback loop in TAB3mediated NF-κB activation.
27009840	7	1	from	implications	1300:1311	arg1	metastasis					1321:1330	TNBC metastasis	1316:1330	TNBC metastasis	1316:1330	Our study provides insights into the mechanism of TAB3 regulating activity and suggests its important implications in TNBC metastasis.
27009840	4	2	theme	p38	813:815	arg1	MAPK					817:820	p38 MAPK	813:820	p38 MAPK	813:820	O-GlcNAcylation of TAB3 was induced by p38 MAPK and it in turn enhances the TAK1 mediated p38MAPK activation, which forms the positive feedback loop in TAB3mediated NF-κB activation.
27009840	1	3	theme	cytoplasmic	172:182	arg1	proteins					184:191	nuclear and cytoplasmic proteins	160:191	nuclear and cytoplasmic proteins	160:191	O-GlcNAcylation is a post-translational modification that regulates a broad range of nuclear and cytoplasmic proteins and is emerging as a key regulator of various biological processes.
27009840	2	4	theme	O-GlcNActransferase	350:368	arg1	levels					313:318	increased levels	303:318	increased levels of global O-GlcNAcylation and O-GlcNActransferase	303:368	Although previous studies have shown that increased levels of global O-GlcNAcylation and O-GlcNActransferase are linked to the incidence of metastasis in triple negative breast cancer (TNBC) patients, the molecular basis behind this is not fully understood.
27009840	3	5	from	Ser408	614:619	arg1	protein					575:581	TAK1 binding protein 3	562:583	the TAK1 binding protein 3 (TAB3)	558:590	In this study, we have determined that the TAK1 binding protein 3 (TAB3) was O-GlcNAcylated at Ser408 by OGT in the TNBC, which was required for its Thr404 phosphorylation, TAK1 activation and downstream nuclear factor kappa B (NF-κB) activation in TNBC.
27009840	3	5	from	Ser408	614:619	arg1	O-GlcNAcylated					596:609	O-GlcNAcylated	596:609	O-GlcNAcylated	596:609	In this study, we have determined that the TAK1 binding protein 3 (TAB3) was O-GlcNAcylated at Ser408 by OGT in the TNBC, which was required for its Thr404 phosphorylation, TAK1 activation and downstream nuclear factor kappa B (NF-κB) activation in TNBC.
27009840	6	6	theme	poor	1166:1169	arg1	prognoses					1171:1179	poor prognoses	1166:1179	poor prognoses of the patients	1166:1195	The expression of TAB3 O-GlcNAcylation increased in TNBC patients, and it was significantly correlated with poor prognoses of the patients.
27009840	2	7	theme	increased	303:311	arg1	levels					313:318	increased levels	303:318	increased levels of global O-GlcNAcylation and O-GlcNActransferase	303:368	Although previous studies have shown that increased levels of global O-GlcNAcylation and O-GlcNActransferase are linked to the incidence of metastasis in triple negative breast cancer (TNBC) patients, the molecular basis behind this is not fully understood.
27009840	5	8	theme	downstream	1040:1049	arg1	NF-κB					1051:1055	its downstream NF-κB	1036:1055	its downstream NF-κB	1036:1055	In TNBC, TAB3O-GlcNAcylationmediated cell migration and invasion by activating its downstream NF-κB.
27009840	3	9	theme	TAK1	562:565	arg1	protein					575:581	TAK1 binding protein 3	562:583	the TAK1 binding protein 3 (TAB3)	558:590	In this study, we have determined that the TAK1 binding protein 3 (TAB3) was O-GlcNAcylated at Ser408 by OGT in the TNBC, which was required for its Thr404 phosphorylation, TAK1 activation and downstream nuclear factor kappa B (NF-κB) activation in TNBC.
27009840	3	9	theme	TAK1	562:565	arg1	TAB3					586:589	TAB3	586:589	TAB3	586:589	In this study, we have determined that the TAK1 binding protein 3 (TAB3) was O-GlcNAcylated at Ser408 by OGT in the TNBC, which was required for its Thr404 phosphorylation, TAK1 activation and downstream nuclear factor kappa B (NF-κB) activation in TNBC.
27009840	3	9	theme	TAK1	562:565	arg1	O-GlcNAcylated					596:609	O-GlcNAcylated	596:609	O-GlcNAcylated	596:609	In this study, we have determined that the TAK1 binding protein 3 (TAB3) was O-GlcNAcylated at Ser408 by OGT in the TNBC, which was required for its Thr404 phosphorylation, TAK1 activation and downstream nuclear factor kappa B (NF-κB) activation in TNBC.
27009840	4	10	theme	TAB3mediated	926:937	arg1	activation					945:954	TAB3mediated NF-κB activation	926:954	TAB3mediated NF-κB activation	926:954	O-GlcNAcylation of TAB3 was induced by p38 MAPK and it in turn enhances the TAK1 mediated p38MAPK activation, which forms the positive feedback loop in TAB3mediated NF-κB activation.
27009840	3	11	theme	binding	567:573	arg1	protein					575:581	TAK1 binding protein 3	562:583	the TAK1 binding protein 3 (TAB3)	558:590	In this study, we have determined that the TAK1 binding protein 3 (TAB3) was O-GlcNAcylated at Ser408 by OGT in the TNBC, which was required for its Thr404 phosphorylation, TAK1 activation and downstream nuclear factor kappa B (NF-κB) activation in TNBC.
27009840	3	11	theme	binding	567:573	arg1	TAB3					586:589	TAB3	586:589	TAB3	586:589	In this study, we have determined that the TAK1 binding protein 3 (TAB3) was O-GlcNAcylated at Ser408 by OGT in the TNBC, which was required for its Thr404 phosphorylation, TAK1 activation and downstream nuclear factor kappa B (NF-κB) activation in TNBC.
27009840	3	11	theme	binding	567:573	arg1	O-GlcNAcylated					596:609	O-GlcNAcylated	596:609	O-GlcNAcylated	596:609	In this study, we have determined that the TAK1 binding protein 3 (TAB3) was O-GlcNAcylated at Ser408 by OGT in the TNBC, which was required for its Thr404 phosphorylation, TAK1 activation and downstream nuclear factor kappa B (NF-κB) activation in TNBC.
27009840	2	12	attach	linked	374:379	arg1	incidence					388:396	the incidence	384:396	the incidence of metastasis in triple negative breast cancer (TNBC) patients	384:459	Although previous studies have shown that increased levels of global O-GlcNAcylation and O-GlcNActransferase are linked to the incidence of metastasis in triple negative breast cancer (TNBC) patients, the molecular basis behind this is not fully understood.
27009840	2	12	attach	linked	374:379	arg2	levels					313:318	increased levels	303:318	increased levels of global O-GlcNAcylation and O-GlcNActransferase	303:368	Although previous studies have shown that increased levels of global O-GlcNAcylation and O-GlcNActransferase are linked to the incidence of metastasis in triple negative breast cancer (TNBC) patients, the molecular basis behind this is not fully understood.
27009840	3	13	from	activation	697:706	arg1	TNBC					768:771	TNBC	768:771	TNBC	768:771	In this study, we have determined that the TAK1 binding protein 3 (TAB3) was O-GlcNAcylated at Ser408 by OGT in the TNBC, which was required for its Thr404 phosphorylation, TAK1 activation and downstream nuclear factor kappa B (NF-κB) activation in TNBC.
27009840	1	14	theme	proteins	184:191	arg1	range					151:155	a broad range	143:155	a broad range of nuclear and cytoplasmic proteins	143:191	O-GlcNAcylation is a post-translational modification that regulates a broad range of nuclear and cytoplasmic proteins and is emerging as a key regulator of various biological processes.
27009840	0	15	theme	negative	51:58	arg1	cancer					67:72	triple negative breast cancer	44:72	triple negative breast cancer	44:72	TAB3 O-GlcNAcylation promotes metastasis of triple negative breast cancer.
27009840	3	16	theme	Thr404	668:673	arg1	phosphorylation					675:689	Thr404 phosphorylation	668:689	Thr404 phosphorylation	668:689	In this study, we have determined that the TAK1 binding protein 3 (TAB3) was O-GlcNAcylated at Ser408 by OGT in the TNBC, which was required for its Thr404 phosphorylation, TAK1 activation and downstream nuclear factor kappa B (NF-κB) activation in TNBC.
27009840	4	17	theme	TAB3	793:796	arg1	O-GlcNAcylation					774:788	O-GlcNAcylation	774:788	O-GlcNAcylation of TAB3	774:796	O-GlcNAcylation of TAB3 was induced by p38 MAPK and it in turn enhances the TAK1 mediated p38MAPK activation, which forms the positive feedback loop in TAB3mediated NF-κB activation.
27009840	3	18	from	phosphorylation	675:689	arg1	TNBC					768:771	TNBC	768:771	TNBC	768:771	In this study, we have determined that the TAK1 binding protein 3 (TAB3) was O-GlcNAcylated at Ser408 by OGT in the TNBC, which was required for its Thr404 phosphorylation, TAK1 activation and downstream nuclear factor kappa B (NF-κB) activation in TNBC.
27009840	3	19	from	O-GlcNAcylated	596:609	arg1	TNBC					635:638	the TNBC	631:638	the TNBC	631:638	In this study, we have determined that the TAK1 binding protein 3 (TAB3) was O-GlcNAcylated at Ser408 by OGT in the TNBC, which was required for its Thr404 phosphorylation, TAK1 activation and downstream nuclear factor kappa B (NF-κB) activation in TNBC.
27009840	2	20	theme	triple	415:420	arg1	patients					452:459	triple negative breast cancer (TNBC) patients	415:459	triple negative breast cancer (TNBC) patients	415:459	Although previous studies have shown that increased levels of global O-GlcNAcylation and O-GlcNActransferase are linked to the incidence of metastasis in triple negative breast cancer (TNBC) patients, the molecular basis behind this is not fully understood.
27009840	7	21	theme	TAB3	1248:1251	arg1	activity					1264:1271	TAB3 regulating activity	1248:1271	TAB3 regulating activity	1248:1271	Our study provides insights into the mechanism of TAB3 regulating activity and suggests its important implications in TNBC metastasis.
27009840	2	22	theme	O-GlcNAcylation	330:344	arg1	levels					313:318	increased levels	303:318	increased levels of global O-GlcNAcylation and O-GlcNActransferase	303:368	Although previous studies have shown that increased levels of global O-GlcNAcylation and O-GlcNActransferase are linked to the incidence of metastasis in triple negative breast cancer (TNBC) patients, the molecular basis behind this is not fully understood.
27009840	3	23	theme	TAK1	692:695	arg1	activation					697:706	TAK1 activation	692:706	TAK1 activation	692:706	In this study, we have determined that the TAK1 binding protein 3 (TAB3) was O-GlcNAcylated at Ser408 by OGT in the TNBC, which was required for its Thr404 phosphorylation, TAK1 activation and downstream nuclear factor kappa B (NF-κB) activation in TNBC.
27009840	0	24	theme	TAB3	0:3	arg1	O-GlcNAcylation					5:19	TAB3 O-GlcNAcylation	0:19	TAB3 O-GlcNAcylation	0:19	TAB3 O-GlcNAcylation promotes metastasis of triple negative breast cancer.
27009840	3	25	theme	downstream	712:721	arg1	activation					754:763	downstream nuclear factor kappa B (NF-κB) activation	712:763	downstream nuclear factor kappa B (NF-κB) activation	712:763	In this study, we have determined that the TAK1 binding protein 3 (TAB3) was O-GlcNAcylated at Ser408 by OGT in the TNBC, which was required for its Thr404 phosphorylation, TAK1 activation and downstream nuclear factor kappa B (NF-κB) activation in TNBC.
27009840	1	26	theme	post-translational	96:113	arg1	O-GlcNAcylation					75:89	O-GlcNAcylation	75:89	O-GlcNAcylation	75:89	O-GlcNAcylation is a post-translational modification that regulates a broad range of nuclear and cytoplasmic proteins and is emerging as a key regulator of various biological processes.
27009840	1	26	theme	post-translational	96:113	arg1	modification					115:126	a post-translational modification	94:126	a post-translational modification that regulates a broad range of nuclear and cytoplasmic proteins and is emerging as a key regulator of various biological processes	94:258	O-GlcNAcylation is a post-translational modification that regulates a broad range of nuclear and cytoplasmic proteins and is emerging as a key regulator of various biological processes.
27009840	2	27	theme	metastasis	401:410	arg1	incidence					388:396	the incidence	384:396	the incidence of metastasis in triple negative breast cancer (TNBC) patients	384:459	Although previous studies have shown that increased levels of global O-GlcNAcylation and O-GlcNActransferase are linked to the incidence of metastasis in triple negative breast cancer (TNBC) patients, the molecular basis behind this is not fully understood.
27009840	3	28	theme	nuclear	723:729	arg1	NF-κB					747:751	NF-κB	747:751	NF-κB	747:751	In this study, we have determined that the TAK1 binding protein 3 (TAB3) was O-GlcNAcylated at Ser408 by OGT in the TNBC, which was required for its Thr404 phosphorylation, TAK1 activation and downstream nuclear factor kappa B (NF-κB) activation in TNBC.
27009840	3	28	theme	nuclear	723:729	arg1	B					744:744	nuclear factor kappa B	723:744	downstream nuclear factor kappa B (NF-κB) activation	712:763	In this study, we have determined that the TAK1 binding protein 3 (TAB3) was O-GlcNAcylated at Ser408 by OGT in the TNBC, which was required for its Thr404 phosphorylation, TAK1 activation and downstream nuclear factor kappa B (NF-κB) activation in TNBC.
27009840	4	29	theme	mediated	855:862	arg1	activation					872:881	the TAK1 mediated p38MAPK activation	846:881	the TAK1 mediated p38MAPK activation	846:881	O-GlcNAcylation of TAB3 was induced by p38 MAPK and it in turn enhances the TAK1 mediated p38MAPK activation, which forms the positive feedback loop in TAB3mediated NF-κB activation.
27009840	2	30	from	incidence	388:396	arg1	patients					452:459	triple negative breast cancer (TNBC) patients	415:459	triple negative breast cancer (TNBC) patients	415:459	Although previous studies have shown that increased levels of global O-GlcNAcylation and O-GlcNActransferase are linked to the incidence of metastasis in triple negative breast cancer (TNBC) patients, the molecular basis behind this is not fully understood.
27009840	6	31	theme	TNBC	1110:1113	arg1	patients					1115:1122	TNBC patients	1110:1122	TNBC patients	1110:1122	The expression of TAB3 O-GlcNAcylation increased in TNBC patients, and it was significantly correlated with poor prognoses of the patients.
27009840	2	32	theme	TNBC	446:449	arg1	patients					452:459	triple negative breast cancer (TNBC) patients	415:459	triple negative breast cancer (TNBC) patients	415:459	Although previous studies have shown that increased levels of global O-GlcNAcylation and O-GlcNActransferase are linked to the incidence of metastasis in triple negative breast cancer (TNBC) patients, the molecular basis behind this is not fully understood.
27009840	2	33	theme	global	323:328	arg1	O-GlcNAcylation					330:344	global O-GlcNAcylation	323:344	global O-GlcNAcylation	323:344	Although previous studies have shown that increased levels of global O-GlcNAcylation and O-GlcNActransferase are linked to the incidence of metastasis in triple negative breast cancer (TNBC) patients, the molecular basis behind this is not fully understood.
27009840	0	34	theme	triple	44:49	arg1	cancer					67:72	triple negative breast cancer	44:72	triple negative breast cancer	44:72	TAB3 O-GlcNAcylation promotes metastasis of triple negative breast cancer.
27009840	1	35	theme	key	214:216	arg1	regulator					218:226	a key regulator	212:226	a key regulator of various biological processes	212:258	O-GlcNAcylation is a post-translational modification that regulates a broad range of nuclear and cytoplasmic proteins and is emerging as a key regulator of various biological processes.
27009840	2	36	theme	cancer	438:443	arg1	patients					452:459	triple negative breast cancer (TNBC) patients	415:459	triple negative breast cancer (TNBC) patients	415:459	Although previous studies have shown that increased levels of global O-GlcNAcylation and O-GlcNActransferase are linked to the incidence of metastasis in triple negative breast cancer (TNBC) patients, the molecular basis behind this is not fully understood.
27009840	2	37	theme	negative	422:429	arg1	patients					452:459	triple negative breast cancer (TNBC) patients	415:459	triple negative breast cancer (TNBC) patients	415:459	Although previous studies have shown that increased levels of global O-GlcNAcylation and O-GlcNActransferase are linked to the incidence of metastasis in triple negative breast cancer (TNBC) patients, the molecular basis behind this is not fully understood.
27009840	3	38	theme	B	744:744	arg1	activation					754:763	downstream nuclear factor kappa B (NF-κB) activation	712:763	downstream nuclear factor kappa B (NF-κB) activation	712:763	In this study, we have determined that the TAK1 binding protein 3 (TAB3) was O-GlcNAcylated at Ser408 by OGT in the TNBC, which was required for its Thr404 phosphorylation, TAK1 activation and downstream nuclear factor kappa B (NF-κB) activation in TNBC.
27009840	4	39	theme	p38MAPK	864:870	arg1	activation					872:881	the TAK1 mediated p38MAPK activation	846:881	the TAK1 mediated p38MAPK activation	846:881	O-GlcNAcylation of TAB3 was induced by p38 MAPK and it in turn enhances the TAK1 mediated p38MAPK activation, which forms the positive feedback loop in TAB3mediated NF-κB activation.
27009840	7	40	theme	important	1290:1298	arg1	implications					1300:1311	its important implications	1286:1311	its important implications in TNBC metastasis	1286:1330	Our study provides insights into the mechanism of TAB3 regulating activity and suggests its important implications in TNBC metastasis.
27009840	6	41	theme	patients	1188:1195	arg1	prognoses					1171:1179	poor prognoses	1166:1179	poor prognoses of the patients	1166:1195	The expression of TAB3 O-GlcNAcylation increased in TNBC patients, and it was significantly correlated with poor prognoses of the patients.
27009840	2	42	theme	breast	431:436	arg1	patients					452:459	triple negative breast cancer (TNBC) patients	415:459	triple negative breast cancer (TNBC) patients	415:459	Although previous studies have shown that increased levels of global O-GlcNAcylation and O-GlcNActransferase are linked to the incidence of metastasis in triple negative breast cancer (TNBC) patients, the molecular basis behind this is not fully understood.
27009840	0	43	theme	breast	60:65	arg1	cancer					67:72	triple negative breast cancer	44:72	triple negative breast cancer	44:72	TAB3 O-GlcNAcylation promotes metastasis of triple negative breast cancer.
27009840	3	44	from	TNBC	635:638	arg1	protein					575:581	TAK1 binding protein 3	562:583	the TAK1 binding protein 3 (TAB3)	558:590	In this study, we have determined that the TAK1 binding protein 3 (TAB3) was O-GlcNAcylated at Ser408 by OGT in the TNBC, which was required for its Thr404 phosphorylation, TAK1 activation and downstream nuclear factor kappa B (NF-κB) activation in TNBC.
27009840	3	44	from	TNBC	635:638	arg1	O-GlcNAcylated					596:609	O-GlcNAcylated	596:609	O-GlcNAcylated	596:609	In this study, we have determined that the TAK1 binding protein 3 (TAB3) was O-GlcNAcylated at Ser408 by OGT in the TNBC, which was required for its Thr404 phosphorylation, TAK1 activation and downstream nuclear factor kappa B (NF-κB) activation in TNBC.
27009840	6	45	theme	TAB3	1076:1079	arg1	O-GlcNAcylation					1081:1095	TAB3 O-GlcNAcylation	1076:1095	TAB3 O-GlcNAcylation	1076:1095	The expression of TAB3 O-GlcNAcylation increased in TNBC patients, and it was significantly correlated with poor prognoses of the patients.
27009840	2	46	theme	molecular	466:474	arg1	basis					476:480	the molecular basis	462:480	the molecular basis behind this	462:492	Although previous studies have shown that increased levels of global O-GlcNAcylation and O-GlcNActransferase are linked to the incidence of metastasis in triple negative breast cancer (TNBC) patients, the molecular basis behind this is not fully understood.
27009840	3	47	theme	factor	731:736	arg1	NF-κB					747:751	NF-κB	747:751	NF-κB	747:751	In this study, we have determined that the TAK1 binding protein 3 (TAB3) was O-GlcNAcylated at Ser408 by OGT in the TNBC, which was required for its Thr404 phosphorylation, TAK1 activation and downstream nuclear factor kappa B (NF-κB) activation in TNBC.
27009840	3	47	theme	factor	731:736	arg1	B					744:744	nuclear factor kappa B	723:744	downstream nuclear factor kappa B (NF-κB) activation	712:763	In this study, we have determined that the TAK1 binding protein 3 (TAB3) was O-GlcNAcylated at Ser408 by OGT in the TNBC, which was required for its Thr404 phosphorylation, TAK1 activation and downstream nuclear factor kappa B (NF-κB) activation in TNBC.
27009840	5	48	theme	cell	994:997	arg1	migration					999:1007	cell migration	994:1007	cell migration	994:1007	In TNBC, TAB3O-GlcNAcylationmediated cell migration and invasion by activating its downstream NF-κB.
27009840	4	49	theme	positive	900:907	arg1	loop					918:921	the positive feedback loop	896:921	the positive feedback loop in TAB3mediated NF-κB activation	896:954	O-GlcNAcylation of TAB3 was induced by p38 MAPK and it in turn enhances the TAK1 mediated p38MAPK activation, which forms the positive feedback loop in TAB3mediated NF-κB activation.
27009840	6	50	theme	O-GlcNAcylation	1081:1095	arg1	expression					1062:1071	The expression	1058:1071	The expression of TAB3 O-GlcNAcylation	1058:1095	The expression of TAB3 O-GlcNAcylation increased in TNBC patients, and it was significantly correlated with poor prognoses of the patients.
27009840	3	51	theme	kappa	738:742	arg1	NF-κB					747:751	NF-κB	747:751	NF-κB	747:751	In this study, we have determined that the TAK1 binding protein 3 (TAB3) was O-GlcNAcylated at Ser408 by OGT in the TNBC, which was required for its Thr404 phosphorylation, TAK1 activation and downstream nuclear factor kappa B (NF-κB) activation in TNBC.
27009840	3	51	theme	kappa	738:742	arg1	B					744:744	nuclear factor kappa B	723:744	downstream nuclear factor kappa B (NF-κB) activation	712:763	In this study, we have determined that the TAK1 binding protein 3 (TAB3) was O-GlcNAcylated at Ser408 by OGT in the TNBC, which was required for its Thr404 phosphorylation, TAK1 activation and downstream nuclear factor kappa B (NF-κB) activation in TNBC.
27009840	3	52	from	activation	754:763	arg1	TNBC					768:771	TNBC	768:771	TNBC	768:771	In this study, we have determined that the TAK1 binding protein 3 (TAB3) was O-GlcNAcylated at Ser408 by OGT in the TNBC, which was required for its Thr404 phosphorylation, TAK1 activation and downstream nuclear factor kappa B (NF-κB) activation in TNBC.
27009840	1	53	theme	broad	145:149	arg1	range					151:155	a broad range	143:155	a broad range of nuclear and cytoplasmic proteins	143:191	O-GlcNAcylation is a post-translational modification that regulates a broad range of nuclear and cytoplasmic proteins and is emerging as a key regulator of various biological processes.
27009840	2	54	theme	previous	270:277	arg1	studies					279:285	previous studies	270:285	previous studies	270:285	Although previous studies have shown that increased levels of global O-GlcNAcylation and O-GlcNActransferase are linked to the incidence of metastasis in triple negative breast cancer (TNBC) patients, the molecular basis behind this is not fully understood.
27009840	4	55	from	loop	918:921	arg1	activation					945:954	TAB3mediated NF-κB activation	926:954	TAB3mediated NF-κB activation	926:954	O-GlcNAcylation of TAB3 was induced by p38 MAPK and it in turn enhances the TAK1 mediated p38MAPK activation, which forms the positive feedback loop in TAB3mediated NF-κB activation.
27009840	1	56	theme	various	231:237	arg1	processes					250:258	various biological processes	231:258	various biological processes	231:258	O-GlcNAcylation is a post-translational modification that regulates a broad range of nuclear and cytoplasmic proteins and is emerging as a key regulator of various biological processes.
27009840	4	57	theme	feedback	909:916	arg1	loop					918:921	the positive feedback loop	896:921	the positive feedback loop in TAB3mediated NF-κB activation	896:954	O-GlcNAcylation of TAB3 was induced by p38 MAPK and it in turn enhances the TAK1 mediated p38MAPK activation, which forms the positive feedback loop in TAB3mediated NF-κB activation.
27009840	7	58	theme	regulating	1253:1262	arg1	activity					1264:1271	TAB3 regulating activity	1248:1271	TAB3 regulating activity	1248:1271	Our study provides insights into the mechanism of TAB3 regulating activity and suggests its important implications in TNBC metastasis.
27009840	7	59	theme	activity	1264:1271	arg1	mechanism					1235:1243	the mechanism	1231:1243	the mechanism of TAB3 regulating activity	1231:1271	Our study provides insights into the mechanism of TAB3 regulating activity and suggests its important implications in TNBC metastasis.
27009840	1	60	theme	biological	239:248	arg1	processes					250:258	various biological processes	231:258	various biological processes	231:258	O-GlcNAcylation is a post-translational modification that regulates a broad range of nuclear and cytoplasmic proteins and is emerging as a key regulator of various biological processes.
27009840	0	61	theme	cancer	67:72	arg1	metastasis					30:39	metastasis	30:39	metastasis of triple negative breast cancer	30:72	TAB3 O-GlcNAcylation promotes metastasis of triple negative breast cancer.
27009840	7	62	theme	TNBC	1316:1319	arg1	metastasis					1321:1330	TNBC metastasis	1316:1330	TNBC metastasis	1316:1330	Our study provides insights into the mechanism of TAB3 regulating activity and suggests its important implications in TNBC metastasis.
27009840	1	63	theme	nuclear	160:166	arg1	proteins					184:191	nuclear and cytoplasmic proteins	160:191	nuclear and cytoplasmic proteins	160:191	O-GlcNAcylation is a post-translational modification that regulates a broad range of nuclear and cytoplasmic proteins and is emerging as a key regulator of various biological processes.
27009840	1	64	theme	processes	250:258	arg1	regulator					218:226	a key regulator	212:226	a key regulator of various biological processes	212:258	O-GlcNAcylation is a post-translational modification that regulates a broad range of nuclear and cytoplasmic proteins and is emerging as a key regulator of various biological processes.
30444036	4	0	theme	CCA	536:538	arg1	KKU-214					564:570	KKU-214	564:570	KKU-214	564:570	OGPs were isolated from human CCA cell lines, KKU-213 and KKU-214, using a click chemistry-based enzymatic labeling system, identified using LC-MS/MS, and searched against an OGP database.
30444036	4	0	theme	CCA	536:538	arg1	KKU-213					552:558	KKU-213	552:558	KKU-213	552:558	OGPs were isolated from human CCA cell lines, KKU-213 and KKU-214, using a click chemistry-based enzymatic labeling system, identified using LC-MS/MS, and searched against an OGP database.
30444036	4	0	theme	CCA	536:538	arg1	lines					545:549	human CCA cell lines	530:549	human CCA cell lines	530:549	OGPs were isolated from human CCA cell lines, KKU-213 and KKU-214, using a click chemistry-based enzymatic labeling system, identified using LC-MS/MS, and searched against an OGP database.
30444036	12	1	theme	O-GlcNAcylation	1786:1800	arg1	significance					1770:1781	the significance	1766:1781	the significance of O-GlcNAcylation on the nuclear translocation of hnRNP-K and its impact on the progression of CCA	1766:1881	This study demonstrates the significance of O-GlcNAcylation on the nuclear translocation of hnRNP-K and its impact on the progression of CCA.
30444036	11	2	theme	O-GlcNAcylation	1662:1676	arg1	levels					1678:1683	high O-GlcNAcylation levels	1657:1683	high O-GlcNAcylation levels	1657:1683	In human CCA tissues, expression of nuclear hnRNP-K was positively correlated with high O-GlcNAcylation levels, metastatic stage, and shorter survival of CCA patients.
30444036	11	2	theme	O-GlcNAcylation	1662:1676	arg1	stage					1697:1701	metastatic stage	1686:1701	metastatic stage	1686:1701	In human CCA tissues, expression of nuclear hnRNP-K was positively correlated with high O-GlcNAcylation levels, metastatic stage, and shorter survival of CCA patients.
30444036	11	2	theme	O-GlcNAcylation	1662:1676	arg1	survival					1716:1723	shorter survival	1708:1723	shorter survival of CCA patients	1708:1739	In human CCA tissues, expression of nuclear hnRNP-K was positively correlated with high O-GlcNAcylation levels, metastatic stage, and shorter survival of CCA patients.
30444036	4	3	theme	labeling	613:620	arg1	system					622:627	a click chemistry-based enzymatic labeling system	579:627	a click chemistry-based enzymatic labeling system	579:627	OGPs were isolated from human CCA cell lines, KKU-213 and KKU-214, using a click chemistry-based enzymatic labeling system, identified using LC-MS/MS, and searched against an OGP database.
30444036	8	4	theme	CCA	1170:1172	arg1	perpetuation					1154:1165	The perpetuation	1150:1165	The perpetuation of CCA by hnRNP-K	1150:1183	The perpetuation of CCA by hnRNP-K was evaluated using siRNA, which revealed modulation of cyclin D1, XIAP, EMT markers, and MMP2 and MMP7 expression.
30444036	6	5	theme	pre-mRNA-binding	914:929	arg1	protein					931:937	a pre-mRNA-binding protein	912:937	a pre-mRNA-binding protein	912:937	Among these, hnRNP-K, a multifaceted RNA- and DNA-binding protein known as a pre-mRNA-binding protein, was one of the most abundantly expressed, suggesting its involvement in CCA progression.
30444036	6	6	from	involvement	997:1007	arg1	progression					1016:1026	CCA progression	1012:1026	CCA progression	1012:1026	Among these, hnRNP-K, a multifaceted RNA- and DNA-binding protein known as a pre-mRNA-binding protein, was one of the most abundantly expressed, suggesting its involvement in CCA progression.
30444036	12	7	from	significance	1770:1781	arg1	impact					1850:1855	its impact	1846:1855	its impact on the progression of CCA	1846:1881	This study demonstrates the significance of O-GlcNAcylation on the nuclear translocation of hnRNP-K and its impact on the progression of CCA.
30444036	12	7	from	significance	1770:1781	arg1	translocation					1817:1829	the nuclear translocation	1805:1829	the nuclear translocation of hnRNP-K	1805:1840	This study demonstrates the significance of O-GlcNAcylation on the nuclear translocation of hnRNP-K and its impact on the progression of CCA.
30444036	4	8	theme	enzymatic	603:611	arg1	system					622:627	a click chemistry-based enzymatic labeling system	579:627	a click chemistry-based enzymatic labeling system	579:627	OGPs were isolated from human CCA cell lines, KKU-213 and KKU-214, using a click chemistry-based enzymatic labeling system, identified using LC-MS/MS, and searched against an OGP database.
30444036	3	9	theme	specific	394:401	arg1	OGPs					428:431	OGPs	428:431	OGPs	428:431	However, the specific O-GlcNAcylated proteins (OGPs) that participate in promotion of CCA progression are poorly understood.
30444036	3	9	theme	specific	394:401	arg1	proteins					418:425	the specific O-GlcNAcylated proteins	390:425	the specific O-GlcNAcylated proteins (OGPs) that participate in promotion of CCA progression	390:481	However, the specific O-GlcNAcylated proteins (OGPs) that participate in promotion of CCA progression are poorly understood.
30444036	11	10	theme	hnRNP-K	1618:1624	arg1	expression					1596:1605	expression	1596:1605	expression of nuclear hnRNP-K	1596:1624	In human CCA tissues, expression of nuclear hnRNP-K was positively correlated with high O-GlcNAcylation levels, metastatic stage, and shorter survival of CCA patients.
30444036	7	11	theme	pull-down	1132:1140	arg1	assays					1142:1147	sWGA pull-down assays	1127:1147	sWGA pull-down assays	1127:1147	O-GlcNAcylation of hnRNP-K was further verified by anti-OGP/anti-hnRNP-K immunoprecipitations and sWGA pull-down assays.
30444036	10	12	theme	cells	1567:1571	arg1	accumulation					1505:1516	nuclear accumulation	1497:1516	nuclear accumulation of hnRNP-K	1497:1527	These data signify an association between nuclear accumulation of hnRNP-K and the migratory capabilities of CCA cells.
30444036	10	12	theme	cells	1567:1571	arg1	capabilities					1547:1558	the migratory capabilities	1533:1558	the migratory capabilities of CCA cells	1533:1571	These data signify an association between nuclear accumulation of hnRNP-K and the migratory capabilities of CCA cells.
30444036	3	13	theme	O-GlcNAcylated	403:416	arg1	OGPs					428:431	OGPs	428:431	OGPs	428:431	However, the specific O-GlcNAcylated proteins (OGPs) that participate in promotion of CCA progression are poorly understood.
30444036	3	13	theme	O-GlcNAcylated	403:416	arg1	proteins					418:425	the specific O-GlcNAcylated proteins	390:425	the specific O-GlcNAcylated proteins (OGPs) that participate in promotion of CCA progression	390:481	However, the specific O-GlcNAcylated proteins (OGPs) that participate in promotion of CCA progression are poorly understood.
30444036	11	14	theme	high	1657:1660	arg1	levels					1678:1683	high O-GlcNAcylation levels	1657:1683	high O-GlcNAcylation levels	1657:1683	In human CCA tissues, expression of nuclear hnRNP-K was positively correlated with high O-GlcNAcylation levels, metastatic stage, and shorter survival of CCA patients.
30444036	11	14	theme	high	1657:1660	arg1	stage					1697:1701	metastatic stage	1686:1701	metastatic stage	1686:1701	In human CCA tissues, expression of nuclear hnRNP-K was positively correlated with high O-GlcNAcylation levels, metastatic stage, and shorter survival of CCA patients.
30444036	11	14	theme	high	1657:1660	arg1	survival					1716:1723	shorter survival	1708:1723	shorter survival of CCA patients	1708:1739	In human CCA tissues, expression of nuclear hnRNP-K was positively correlated with high O-GlcNAcylation levels, metastatic stage, and shorter survival of CCA patients.
30444036	11	15	theme	CCA	1583:1585	arg1	tissues					1587:1593	human CCA tissues	1577:1593	human CCA tissues	1577:1593	In human CCA tissues, expression of nuclear hnRNP-K was positively correlated with high O-GlcNAcylation levels, metastatic stage, and shorter survival of CCA patients.
30444036	11	16	theme	shorter	1708:1714	arg1	levels					1678:1683	high O-GlcNAcylation levels	1657:1683	high O-GlcNAcylation levels	1657:1683	In human CCA tissues, expression of nuclear hnRNP-K was positively correlated with high O-GlcNAcylation levels, metastatic stage, and shorter survival of CCA patients.
30444036	11	16	theme	shorter	1708:1714	arg1	survival					1716:1723	shorter survival	1708:1723	shorter survival of CCA patients	1708:1739	In human CCA tissues, expression of nuclear hnRNP-K was positively correlated with high O-GlcNAcylation levels, metastatic stage, and shorter survival of CCA patients.
30444036	11	17	theme	metastatic	1686:1695	arg1	levels					1678:1683	high O-GlcNAcylation levels	1657:1683	high O-GlcNAcylation levels	1657:1683	In human CCA tissues, expression of nuclear hnRNP-K was positively correlated with high O-GlcNAcylation levels, metastatic stage, and shorter survival of CCA patients.
30444036	11	17	theme	metastatic	1686:1695	arg1	stage					1697:1701	metastatic stage	1686:1701	metastatic stage	1686:1701	In human CCA tissues, expression of nuclear hnRNP-K was positively correlated with high O-GlcNAcylation levels, metastatic stage, and shorter survival of CCA patients.
30444036	6	18	theme	DNA-binding	883:893	arg1	protein					895:901	a multifaceted RNA- and DNA-binding protein	859:901	a multifaceted RNA- and DNA-binding protein known as a pre-mRNA-binding protein	859:937	Among these, hnRNP-K, a multifaceted RNA- and DNA-binding protein known as a pre-mRNA-binding protein, was one of the most abundantly expressed, suggesting its involvement in CCA progression.
30444036	6	18	theme	DNA-binding	883:893	arg1	hnRNP-K					850:856	hnRNP-K	850:856	hnRNP-K	850:856	Among these, hnRNP-K, a multifaceted RNA- and DNA-binding protein known as a pre-mRNA-binding protein, was one of the most abundantly expressed, suggesting its involvement in CCA progression.
30444036	2	19	theme	increased	314:322	arg1	migration/invasion					324:341	increased migration/invasion	314:341	increased migration/invasion of CCA cell lines	314:359	Associations between O-GlcNAcylation, shorter survival of cholangiocarcinoma (CCA) patients, and increased migration/invasion of CCA cell lines have been reported.
30444036	3	20	theme	progression	471:481	arg1	promotion					454:462	promotion	454:462	promotion of CCA progression	454:481	However, the specific O-GlcNAcylated proteins (OGPs) that participate in promotion of CCA progression are poorly understood.
30444036	5	21	theme	cancer	754:759	arg1	progression					761:771	cancer progression	754:771	cancer progression	754:771	From the proteomic analysis, a total of 21 OGPs related to cancer progression were identified, of which 12 have not been previously reported.
30444036	4	22	theme	human	530:534	arg1	KKU-214					564:570	KKU-214	564:570	KKU-214	564:570	OGPs were isolated from human CCA cell lines, KKU-213 and KKU-214, using a click chemistry-based enzymatic labeling system, identified using LC-MS/MS, and searched against an OGP database.
30444036	4	22	theme	human	530:534	arg1	KKU-213					552:558	KKU-213	552:558	KKU-213	552:558	OGPs were isolated from human CCA cell lines, KKU-213 and KKU-214, using a click chemistry-based enzymatic labeling system, identified using LC-MS/MS, and searched against an OGP database.
30444036	4	22	theme	human	530:534	arg1	lines					545:549	human CCA cell lines	530:549	human CCA cell lines	530:549	OGPs were isolated from human CCA cell lines, KKU-213 and KKU-214, using a click chemistry-based enzymatic labeling system, identified using LC-MS/MS, and searched against an OGP database.
30444036	7	23	theme	sWGA	1127:1130	arg1	assays					1142:1147	sWGA pull-down assays	1127:1147	sWGA pull-down assays	1127:1147	O-GlcNAcylation of hnRNP-K was further verified by anti-OGP/anti-hnRNP-K immunoprecipitations and sWGA pull-down assays.
30444036	12	24	theme	nuclear	1809:1815	arg1	translocation					1817:1829	the nuclear translocation	1805:1829	the nuclear translocation of hnRNP-K	1805:1840	This study demonstrates the significance of O-GlcNAcylation on the nuclear translocation of hnRNP-K and its impact on the progression of CCA.
30444036	4	25	theme	OGP	681:683	arg1	database					685:692	an OGP database	678:692	an OGP database	678:692	OGPs were isolated from human CCA cell lines, KKU-213 and KKU-214, using a click chemistry-based enzymatic labeling system, identified using LC-MS/MS, and searched against an OGP database.
30444036	0	26	theme	nuclear	17:23	arg1	translocation					25:37	O-GlcNAc-induced nuclear translocation	0:37	O-GlcNAc-induced nuclear translocation of hnRNP-K	0:48	O-GlcNAc-induced nuclear translocation of hnRNP-K is associated with progression and metastasis of cholangiocarcinoma.
30444036	6	27	theme	RNA-	874:877	arg1	protein					895:901	a multifaceted RNA- and DNA-binding protein	859:901	a multifaceted RNA- and DNA-binding protein known as a pre-mRNA-binding protein	859:937	Among these, hnRNP-K, a multifaceted RNA- and DNA-binding protein known as a pre-mRNA-binding protein, was one of the most abundantly expressed, suggesting its involvement in CCA progression.
30444036	6	27	theme	RNA-	874:877	arg1	hnRNP-K					850:856	hnRNP-K	850:856	hnRNP-K	850:856	Among these, hnRNP-K, a multifaceted RNA- and DNA-binding protein known as a pre-mRNA-binding protein, was one of the most abundantly expressed, suggesting its involvement in CCA progression.
30444036	7	28	theme	anti-OGP/anti-hnRNP-K	1080:1100	arg1	immunoprecipitations					1102:1121	anti-OGP/anti-hnRNP-K immunoprecipitations	1080:1121	anti-OGP/anti-hnRNP-K immunoprecipitations	1080:1121	O-GlcNAcylation of hnRNP-K was further verified by anti-OGP/anti-hnRNP-K immunoprecipitations and sWGA pull-down assays.
30444036	7	29	theme	hnRNP-K	1048:1054	arg1	O-GlcNAcylation					1029:1043	O-GlcNAcylation	1029:1043	O-GlcNAcylation of hnRNP-K	1029:1054	O-GlcNAcylation of hnRNP-K was further verified by anti-OGP/anti-hnRNP-K immunoprecipitations and sWGA pull-down assays.
30444036	8	30	theme	EMT	1258:1260	arg1	markers					1262:1268	EMT markers	1258:1268	EMT markers	1258:1268	The perpetuation of CCA by hnRNP-K was evaluated using siRNA, which revealed modulation of cyclin D1, XIAP, EMT markers, and MMP2 and MMP7 expression.
30444036	0	31	theme	O-GlcNAc-induced	0:15	arg1	translocation					25:37	O-GlcNAc-induced nuclear translocation	0:37	O-GlcNAc-induced nuclear translocation of hnRNP-K	0:48	O-GlcNAc-induced nuclear translocation of hnRNP-K is associated with progression and metastasis of cholangiocarcinoma.
30444036	8	32	theme	XIAP	1252:1255	arg1	modulation					1227:1236	modulation	1227:1236	modulation of cyclin D1, XIAP, EMT markers, and MMP2 and MMP7 expression	1227:1298	The perpetuation of CCA by hnRNP-K was evaluated using siRNA, which revealed modulation of cyclin D1, XIAP, EMT markers, and MMP2 and MMP7 expression.
30444036	2	33	theme	lines	355:359	arg1	migration/invasion					324:341	increased migration/invasion	314:341	increased migration/invasion of CCA cell lines	314:359	Associations between O-GlcNAcylation, shorter survival of cholangiocarcinoma (CCA) patients, and increased migration/invasion of CCA cell lines have been reported.
30444036	2	33	theme	lines	355:359	arg1	O-GlcNAcylation					238:252	O-GlcNAcylation	238:252	O-GlcNAcylation	238:252	Associations between O-GlcNAcylation, shorter survival of cholangiocarcinoma (CCA) patients, and increased migration/invasion of CCA cell lines have been reported.
30444036	2	33	theme	lines	355:359	arg1	survival					263:270	shorter survival	255:270	shorter survival of cholangiocarcinoma (CCA) patients	255:307	Associations between O-GlcNAcylation, shorter survival of cholangiocarcinoma (CCA) patients, and increased migration/invasion of CCA cell lines have been reported.
30444036	11	34	theme	nuclear	1610:1616	arg1	hnRNP-K					1618:1624	nuclear hnRNP-K	1610:1624	nuclear hnRNP-K	1610:1624	In human CCA tissues, expression of nuclear hnRNP-K was positively correlated with high O-GlcNAcylation levels, metastatic stage, and shorter survival of CCA patients.
30444036	3	35	theme	CCA	467:469	arg1	progression					471:481	CCA progression	467:481	CCA progression	467:481	However, the specific O-GlcNAcylated proteins (OGPs) that participate in promotion of CCA progression are poorly understood.
30444036	6	36	theme	most	955:958	arg1	one					944:946	one	944:946	one	944:946	Among these, hnRNP-K, a multifaceted RNA- and DNA-binding protein known as a pre-mRNA-binding protein, was one of the most abundantly expressed, suggesting its involvement in CCA progression.
30444036	6	36	theme	most	955:958	arg1	most					955:958	most	955:958	most	955:958	Among these, hnRNP-K, a multifaceted RNA- and DNA-binding protein known as a pre-mRNA-binding protein, was one of the most abundantly expressed, suggesting its involvement in CCA progression.
30444036	12	37	theme	hnRNP-K	1834:1840	arg1	impact					1850:1855	its impact	1846:1855	its impact on the progression of CCA	1846:1881	This study demonstrates the significance of O-GlcNAcylation on the nuclear translocation of hnRNP-K and its impact on the progression of CCA.
30444036	12	37	theme	hnRNP-K	1834:1840	arg1	translocation					1817:1829	the nuclear translocation	1805:1829	the nuclear translocation of hnRNP-K	1805:1840	This study demonstrates the significance of O-GlcNAcylation on the nuclear translocation of hnRNP-K and its impact on the progression of CCA.
30444036	2	38	theme	cell	350:353	arg1	lines					355:359	CCA cell lines	346:359	CCA cell lines	346:359	Associations between O-GlcNAcylation, shorter survival of cholangiocarcinoma (CCA) patients, and increased migration/invasion of CCA cell lines have been reported.
30444036	12	39	from	translocation	1817:1829	arg1	progression					1864:1874	the progression	1860:1874	the progression of CCA	1860:1881	This study demonstrates the significance of O-GlcNAcylation on the nuclear translocation of hnRNP-K and its impact on the progression of CCA.
30444036	4	40	theme	chemistry-based	587:601	arg1	system					622:627	a click chemistry-based enzymatic labeling system	579:627	a click chemistry-based enzymatic labeling system	579:627	OGPs were isolated from human CCA cell lines, KKU-213 and KKU-214, using a click chemistry-based enzymatic labeling system, identified using LC-MS/MS, and searched against an OGP database.
30444036	6	41	theme	multifaceted	861:872	arg1	protein					895:901	a multifaceted RNA- and DNA-binding protein	859:901	a multifaceted RNA- and DNA-binding protein known as a pre-mRNA-binding protein	859:937	Among these, hnRNP-K, a multifaceted RNA- and DNA-binding protein known as a pre-mRNA-binding protein, was one of the most abundantly expressed, suggesting its involvement in CCA progression.
30444036	6	41	theme	multifaceted	861:872	arg1	hnRNP-K					850:856	hnRNP-K	850:856	hnRNP-K	850:856	Among these, hnRNP-K, a multifaceted RNA- and DNA-binding protein known as a pre-mRNA-binding protein, was one of the most abundantly expressed, suggesting its involvement in CCA progression.
30444036	2	42	theme	CCA	346:348	arg1	lines					355:359	CCA cell lines	346:359	CCA cell lines	346:359	Associations between O-GlcNAcylation, shorter survival of cholangiocarcinoma (CCA) patients, and increased migration/invasion of CCA cell lines have been reported.
30444036	8	43	theme	markers	1262:1268	arg1	modulation					1227:1236	modulation	1227:1236	modulation of cyclin D1, XIAP, EMT markers, and MMP2 and MMP7 expression	1227:1298	The perpetuation of CCA by hnRNP-K was evaluated using siRNA, which revealed modulation of cyclin D1, XIAP, EMT markers, and MMP2 and MMP7 expression.
30444036	4	44	theme	click	581:585	arg1	system					622:627	a click chemistry-based enzymatic labeling system	579:627	a click chemistry-based enzymatic labeling system	579:627	OGPs were isolated from human CCA cell lines, KKU-213 and KKU-214, using a click chemistry-based enzymatic labeling system, identified using LC-MS/MS, and searched against an OGP database.
30444036	9	45	theme	native	1304:1309	arg1	cells					1315:1319	native CCA cells	1304:1319	native CCA cells	1304:1319	In native CCA cells, hnRNP-K was primarily localized in the nucleus; however, when O-GlcNAcylation was suppressed, hnRNP-K was retained in the cytoplasm.
30444036	8	46	theme	MMP2	1275:1278	arg1	expression					1289:1298	MMP2 and MMP7 expression	1275:1298	expression	1289:1298	The perpetuation of CCA by hnRNP-K was evaluated using siRNA, which revealed modulation of cyclin D1, XIAP, EMT markers, and MMP2 and MMP7 expression.
30444036	0	47	theme	hnRNP-K	42:48	arg1	translocation					25:37	O-GlcNAc-induced nuclear translocation	0:37	O-GlcNAc-induced nuclear translocation of hnRNP-K	0:48	O-GlcNAc-induced nuclear translocation of hnRNP-K is associated with progression and metastasis of cholangiocarcinoma.
30444036	12	48	from	impact	1850:1855	arg1	progression					1864:1874	the progression	1860:1874	the progression of CCA	1860:1881	This study demonstrates the significance of O-GlcNAcylation on the nuclear translocation of hnRNP-K and its impact on the progression of CCA.
30444036	5	49	theme	related	743:749	arg1	OGPs					738:741	21 OGPs	735:741	21 OGPs related to cancer progression	735:771	From the proteomic analysis, a total of 21 OGPs related to cancer progression were identified, of which 12 have not been previously reported.
30444036	2	50	theme	cholangiocarcinoma	275:292	arg1	patients					300:307	cholangiocarcinoma (CCA) patients	275:307	cholangiocarcinoma (CCA) patients	275:307	Associations between O-GlcNAcylation, shorter survival of cholangiocarcinoma (CCA) patients, and increased migration/invasion of CCA cell lines have been reported.
30444036	11	51	theme	human	1577:1581	arg1	tissues					1587:1593	human CCA tissues	1577:1593	human CCA tissues	1577:1593	In human CCA tissues, expression of nuclear hnRNP-K was positively correlated with high O-GlcNAcylation levels, metastatic stage, and shorter survival of CCA patients.
30444036	8	52	theme	D1	1248:1249	arg1	modulation					1227:1236	modulation	1227:1236	modulation of cyclin D1, XIAP, EMT markers, and MMP2 and MMP7 expression	1227:1298	The perpetuation of CCA by hnRNP-K was evaluated using siRNA, which revealed modulation of cyclin D1, XIAP, EMT markers, and MMP2 and MMP7 expression.
30444036	5	53	theme	OGPs	738:741	arg1	total					726:730	a total	724:730	a total of 21 OGPs related to cancer progression	724:771	From the proteomic analysis, a total of 21 OGPs related to cancer progression were identified, of which 12 have not been previously reported.
30444036	9	54	theme	CCA	1311:1313	arg1	cells					1315:1319	native CCA cells	1304:1319	native CCA cells	1304:1319	In native CCA cells, hnRNP-K was primarily localized in the nucleus; however, when O-GlcNAcylation was suppressed, hnRNP-K was retained in the cytoplasm.
30444036	8	55	theme	MMP7	1284:1287	arg1	expression					1289:1298	MMP2 and MMP7 expression	1275:1298	expression	1289:1298	The perpetuation of CCA by hnRNP-K was evaluated using siRNA, which revealed modulation of cyclin D1, XIAP, EMT markers, and MMP2 and MMP7 expression.
30444036	8	56	theme	cyclin	1241:1246	arg1	D1					1248:1249	cyclin D1	1241:1249	cyclin D1	1241:1249	The perpetuation of CCA by hnRNP-K was evaluated using siRNA, which revealed modulation of cyclin D1, XIAP, EMT markers, and MMP2 and MMP7 expression.
30444036	5	57	theme	proteomic	704:712	arg1	analysis					714:721	the proteomic analysis	700:721	the proteomic analysis	700:721	From the proteomic analysis, a total of 21 OGPs related to cancer progression were identified, of which 12 have not been previously reported.
30444036	2	58	theme	shorter	255:261	arg1	survival					263:270	shorter survival	255:270	shorter survival of cholangiocarcinoma (CCA) patients	255:307	Associations between O-GlcNAcylation, shorter survival of cholangiocarcinoma (CCA) patients, and increased migration/invasion of CCA cell lines have been reported.
30444036	12	59	theme	CCA	1879:1881	arg1	progression					1864:1874	the progression	1860:1874	the progression of CCA	1860:1881	This study demonstrates the significance of O-GlcNAcylation on the nuclear translocation of hnRNP-K and its impact on the progression of CCA.
30444036	1	60	theme	key	140:142	arg1	modification					163:174	a key post-translational modification	138:174	a key post-translational modification that modifies the functions of proteins	138:214	O-GlcNAcylation is a key post-translational modification that modifies the functions of proteins.
30444036	1	60	theme	key	140:142	arg1	O-GlcNAcylation					119:133	O-GlcNAcylation	119:133	O-GlcNAcylation	119:133	O-GlcNAcylation is a key post-translational modification that modifies the functions of proteins.
30444036	10	61	theme	nuclear	1497:1503	arg1	accumulation					1505:1516	nuclear accumulation	1497:1516	nuclear accumulation of hnRNP-K	1497:1527	These data signify an association between nuclear accumulation of hnRNP-K and the migratory capabilities of CCA cells.
30444036	10	62	theme	CCA	1563:1565	arg1	cells					1567:1571	CCA cells	1563:1571	CCA cells	1563:1571	These data signify an association between nuclear accumulation of hnRNP-K and the migratory capabilities of CCA cells.
30444036	1	63	theme	post-translational	144:161	arg1	modification					163:174	a key post-translational modification	138:174	a key post-translational modification that modifies the functions of proteins	138:214	O-GlcNAcylation is a key post-translational modification that modifies the functions of proteins.
30444036	1	63	theme	post-translational	144:161	arg1	O-GlcNAcylation					119:133	O-GlcNAcylation	119:133	O-GlcNAcylation	119:133	O-GlcNAcylation is a key post-translational modification that modifies the functions of proteins.
30444036	11	64	theme	patients	1732:1739	arg1	levels					1678:1683	high O-GlcNAcylation levels	1657:1683	high O-GlcNAcylation levels	1657:1683	In human CCA tissues, expression of nuclear hnRNP-K was positively correlated with high O-GlcNAcylation levels, metastatic stage, and shorter survival of CCA patients.
30444036	11	64	theme	patients	1732:1739	arg1	stage					1697:1701	metastatic stage	1686:1701	metastatic stage	1686:1701	In human CCA tissues, expression of nuclear hnRNP-K was positively correlated with high O-GlcNAcylation levels, metastatic stage, and shorter survival of CCA patients.
30444036	11	64	theme	patients	1732:1739	arg1	survival					1716:1723	shorter survival	1708:1723	shorter survival of CCA patients	1708:1739	In human CCA tissues, expression of nuclear hnRNP-K was positively correlated with high O-GlcNAcylation levels, metastatic stage, and shorter survival of CCA patients.
30444036	2	65	theme	patients	300:307	arg1	migration/invasion					324:341	increased migration/invasion	314:341	increased migration/invasion of CCA cell lines	314:359	Associations between O-GlcNAcylation, shorter survival of cholangiocarcinoma (CCA) patients, and increased migration/invasion of CCA cell lines have been reported.
30444036	2	65	theme	patients	300:307	arg1	O-GlcNAcylation					238:252	O-GlcNAcylation	238:252	O-GlcNAcylation	238:252	Associations between O-GlcNAcylation, shorter survival of cholangiocarcinoma (CCA) patients, and increased migration/invasion of CCA cell lines have been reported.
30444036	2	65	theme	patients	300:307	arg1	survival					263:270	shorter survival	255:270	shorter survival of cholangiocarcinoma (CCA) patients	255:307	Associations between O-GlcNAcylation, shorter survival of cholangiocarcinoma (CCA) patients, and increased migration/invasion of CCA cell lines have been reported.
30444036	8	66	theme	expression	1289:1298	arg1	modulation					1227:1236	modulation	1227:1236	modulation of cyclin D1, XIAP, EMT markers, and MMP2 and MMP7 expression	1227:1298	The perpetuation of CCA by hnRNP-K was evaluated using siRNA, which revealed modulation of cyclin D1, XIAP, EMT markers, and MMP2 and MMP7 expression.
30444036	6	67	theme	CCA	1012:1014	arg1	progression					1016:1026	CCA progression	1012:1026	CCA progression	1012:1026	Among these, hnRNP-K, a multifaceted RNA- and DNA-binding protein known as a pre-mRNA-binding protein, was one of the most abundantly expressed, suggesting its involvement in CCA progression.
30444036	10	68	theme	migratory	1537:1545	arg1	capabilities					1547:1558	the migratory capabilities	1533:1558	the migratory capabilities of CCA cells	1533:1571	These data signify an association between nuclear accumulation of hnRNP-K and the migratory capabilities of CCA cells.
30444036	9	69	located	localized	1344:1352	arg1	nucleus					1361:1367	the nucleus	1357:1367	the nucleus	1357:1367	In native CCA cells, hnRNP-K was primarily localized in the nucleus; however, when O-GlcNAcylation was suppressed, hnRNP-K was retained in the cytoplasm.
30444036	9	69	located	localized	1344:1352	arg2	hnRNP-K					1322:1328	hnRNP-K	1322:1328	hnRNP-K	1322:1328	In native CCA cells, hnRNP-K was primarily localized in the nucleus; however, when O-GlcNAcylation was suppressed, hnRNP-K was retained in the cytoplasm.
30444036	9	69	located	localized	1344:1352	arg1	cells					1315:1319	native CCA cells	1304:1319	native CCA cells	1304:1319	In native CCA cells, hnRNP-K was primarily localized in the nucleus; however, when O-GlcNAcylation was suppressed, hnRNP-K was retained in the cytoplasm.
30444036	1	70	theme	proteins	207:214	arg1	functions					194:202	the functions	190:202	the functions of proteins	190:214	O-GlcNAcylation is a key post-translational modification that modifies the functions of proteins.
30444036	10	71	theme	hnRNP-K	1521:1527	arg1	accumulation					1505:1516	nuclear accumulation	1497:1516	nuclear accumulation of hnRNP-K	1497:1527	These data signify an association between nuclear accumulation of hnRNP-K and the migratory capabilities of CCA cells.
30444036	10	71	theme	hnRNP-K	1521:1527	arg1	capabilities					1547:1558	the migratory capabilities	1533:1558	the migratory capabilities of CCA cells	1533:1571	These data signify an association between nuclear accumulation of hnRNP-K and the migratory capabilities of CCA cells.
30444036	4	72	theme	cell	540:543	arg1	KKU-214					564:570	KKU-214	564:570	KKU-214	564:570	OGPs were isolated from human CCA cell lines, KKU-213 and KKU-214, using a click chemistry-based enzymatic labeling system, identified using LC-MS/MS, and searched against an OGP database.
30444036	4	72	theme	cell	540:543	arg1	KKU-213					552:558	KKU-213	552:558	KKU-213	552:558	OGPs were isolated from human CCA cell lines, KKU-213 and KKU-214, using a click chemistry-based enzymatic labeling system, identified using LC-MS/MS, and searched against an OGP database.
30444036	4	72	theme	cell	540:543	arg1	lines					545:549	human CCA cell lines	530:549	human CCA cell lines	530:549	OGPs were isolated from human CCA cell lines, KKU-213 and KKU-214, using a click chemistry-based enzymatic labeling system, identified using LC-MS/MS, and searched against an OGP database.
30444036	11	73	theme	CCA	1728:1730	arg1	patients					1732:1739	CCA patients	1728:1739	CCA patients	1728:1739	In human CCA tissues, expression of nuclear hnRNP-K was positively correlated with high O-GlcNAcylation levels, metastatic stage, and shorter survival of CCA patients.
30444036	4	74	attach	isolated	516:523	arg2	OGPs					506:509	OGPs	506:509	OGPs	506:509	OGPs were isolated from human CCA cell lines, KKU-213 and KKU-214, using a click chemistry-based enzymatic labeling system, identified using LC-MS/MS, and searched against an OGP database.
30444036	4	74	attach	isolated	516:523	arg1	KKU-214					564:570	KKU-214	564:570	KKU-214	564:570	OGPs were isolated from human CCA cell lines, KKU-213 and KKU-214, using a click chemistry-based enzymatic labeling system, identified using LC-MS/MS, and searched against an OGP database.
30444036	4	74	attach	isolated	516:523	arg1	KKU-213					552:558	KKU-213	552:558	KKU-213	552:558	OGPs were isolated from human CCA cell lines, KKU-213 and KKU-214, using a click chemistry-based enzymatic labeling system, identified using LC-MS/MS, and searched against an OGP database.
30444036	4	74	attach	isolated	516:523	arg1	lines					545:549	human CCA cell lines	530:549	human CCA cell lines	530:549	OGPs were isolated from human CCA cell lines, KKU-213 and KKU-214, using a click chemistry-based enzymatic labeling system, identified using LC-MS/MS, and searched against an OGP database.
30444036	0	75	theme	cholangiocarcinoma	99:116	arg1	metastasis					85:94	metastasis	85:94	metastasis	85:94	O-GlcNAc-induced nuclear translocation of hnRNP-K is associated with progression and metastasis of cholangiocarcinoma.
30444036	0	75	theme	cholangiocarcinoma	99:116	arg1	progression					69:79	progression	69:79	progression	69:79	O-GlcNAc-induced nuclear translocation of hnRNP-K is associated with progression and metastasis of cholangiocarcinoma.
33214551	0	0	theme	O-GlcNAc-regulated	96:113	arg1	response					132:139	an O-GlcNAc-regulated genotoxic stress response	93:139	an O-GlcNAc-regulated genotoxic stress response	93:139	Proteomic profiling and genome-wide mapping of O-GlcNAc chromatin-associated proteins reveal an O-GlcNAc-regulated genotoxic stress response.
33214551	3	1	theme	comprehensive	358:370	arg1	data					372:375	comprehensive data	358:375	comprehensive data	358:375	Here, comprehensive data are obtained by a chemical reporter-based method to survey O-GlcNAc function in human breast cancer cells stimulated with the genotoxic agent adriamycin.
33214551	4	2	theme	transcriptional	774:788	arg1	network					804:810	a comprehensive transcriptional reprogramming network	758:810	a comprehensive transcriptional reprogramming network	758:810	We identify 875 genotoxic stress-induced O-GlcNAc chromatin-associated proteins (OCPs), including 88 O-GlcNAc chromatin-associated transcription factors and cofactors (OCTFs), subsequently map their genomic loci, and construct a comprehensive transcriptional reprogramming network.
33214551	4	3	theme	transcription	662:674	arg1	factors					676:682	88 O-GlcNAc chromatin-associated transcription factors	629:682	88 O-GlcNAc chromatin-associated transcription factors	629:682	We identify 875 genotoxic stress-induced O-GlcNAc chromatin-associated proteins (OCPs), including 88 O-GlcNAc chromatin-associated transcription factors and cofactors (OCTFs), subsequently map their genomic loci, and construct a comprehensive transcriptional reprogramming network.
33214551	4	4	theme	genotoxic	547:555	arg1	OCPs					612:615	OCPs	612:615	OCPs	612:615	We identify 875 genotoxic stress-induced O-GlcNAc chromatin-associated proteins (OCPs), including 88 O-GlcNAc chromatin-associated transcription factors and cofactors (OCTFs), subsequently map their genomic loci, and construct a comprehensive transcriptional reprogramming network.
33214551	4	4	theme	genotoxic	547:555	arg1	factors					676:682	88 O-GlcNAc chromatin-associated transcription factors	629:682	88 O-GlcNAc chromatin-associated transcription factors	629:682	We identify 875 genotoxic stress-induced O-GlcNAc chromatin-associated proteins (OCPs), including 88 O-GlcNAc chromatin-associated transcription factors and cofactors (OCTFs), subsequently map their genomic loci, and construct a comprehensive transcriptional reprogramming network.
33214551	4	4	theme	genotoxic	547:555	arg1	proteins					602:609	875 genotoxic stress-induced O-GlcNAc chromatin-associated proteins	543:609	875 genotoxic stress-induced O-GlcNAc chromatin-associated proteins (OCPs)	543:616	We identify 875 genotoxic stress-induced O-GlcNAc chromatin-associated proteins (OCPs), including 88 O-GlcNAc chromatin-associated transcription factors and cofactors (OCTFs), subsequently map their genomic loci, and construct a comprehensive transcriptional reprogramming network.
33214551	4	4	theme	genotoxic	547:555	arg1	cofactors					688:696	cofactors	688:696	cofactors (OCTFs)	688:704	We identify 875 genotoxic stress-induced O-GlcNAc chromatin-associated proteins (OCPs), including 88 O-GlcNAc chromatin-associated transcription factors and cofactors (OCTFs), subsequently map their genomic loci, and construct a comprehensive transcriptional reprogramming network.
33214551	4	5	theme	chromatin-associated	581:600	arg1	OCPs					612:615	OCPs	612:615	OCPs	612:615	We identify 875 genotoxic stress-induced O-GlcNAc chromatin-associated proteins (OCPs), including 88 O-GlcNAc chromatin-associated transcription factors and cofactors (OCTFs), subsequently map their genomic loci, and construct a comprehensive transcriptional reprogramming network.
33214551	4	5	theme	chromatin-associated	581:600	arg1	factors					676:682	88 O-GlcNAc chromatin-associated transcription factors	629:682	88 O-GlcNAc chromatin-associated transcription factors	629:682	We identify 875 genotoxic stress-induced O-GlcNAc chromatin-associated proteins (OCPs), including 88 O-GlcNAc chromatin-associated transcription factors and cofactors (OCTFs), subsequently map their genomic loci, and construct a comprehensive transcriptional reprogramming network.
33214551	4	5	theme	chromatin-associated	581:600	arg1	proteins					602:609	875 genotoxic stress-induced O-GlcNAc chromatin-associated proteins	543:609	875 genotoxic stress-induced O-GlcNAc chromatin-associated proteins (OCPs)	543:616	We identify 875 genotoxic stress-induced O-GlcNAc chromatin-associated proteins (OCPs), including 88 O-GlcNAc chromatin-associated transcription factors and cofactors (OCTFs), subsequently map their genomic loci, and construct a comprehensive transcriptional reprogramming network.
33214551	4	5	theme	chromatin-associated	581:600	arg1	cofactors					688:696	cofactors	688:696	cofactors (OCTFs)	688:704	We identify 875 genotoxic stress-induced O-GlcNAc chromatin-associated proteins (OCPs), including 88 O-GlcNAc chromatin-associated transcription factors and cofactors (OCTFs), subsequently map their genomic loci, and construct a comprehensive transcriptional reprogramming network.
33214551	7	6	theme	key	1217:1219	arg1	factor-1					1184:1191	The OCTF nuclear factor erythroid 2-related factor-1	1140:1191	The OCTF nuclear factor erythroid 2-related factor-1 (NRF1)	1140:1198	The OCTF nuclear factor erythroid 2-related factor-1 (NRF1) is found to be a key response regulator in O-GlcNAc-modulated cellular homeostasis.
33214551	7	6	theme	key	1217:1219	arg1	regulator					1230:1238	a key response regulator	1215:1238	a key response regulator	1215:1238	The OCTF nuclear factor erythroid 2-related factor-1 (NRF1) is found to be a key response regulator in O-GlcNAc-modulated cellular homeostasis.
33214551	4	7	theme	comprehensive	760:772	arg1	network					804:810	a comprehensive transcriptional reprogramming network	758:810	a comprehensive transcriptional reprogramming network	758:810	We identify 875 genotoxic stress-induced O-GlcNAc chromatin-associated proteins (OCPs), including 88 O-GlcNAc chromatin-associated transcription factors and cofactors (OCTFs), subsequently map their genomic loci, and construct a comprehensive transcriptional reprogramming network.
33214551	4	8	theme	chromatin-associated	641:660	arg1	factors					676:682	88 O-GlcNAc chromatin-associated transcription factors	629:682	88 O-GlcNAc chromatin-associated transcription factors	629:682	We identify 875 genotoxic stress-induced O-GlcNAc chromatin-associated proteins (OCPs), including 88 O-GlcNAc chromatin-associated transcription factors and cofactors (OCTFs), subsequently map their genomic loci, and construct a comprehensive transcriptional reprogramming network.
33214551	0	9	theme	stress	125:130	arg1	response					132:139	an O-GlcNAc-regulated genotoxic stress response	93:139	an O-GlcNAc-regulated genotoxic stress response	93:139	Proteomic profiling and genome-wide mapping of O-GlcNAc chromatin-associated proteins reveal an O-GlcNAc-regulated genotoxic stress response.
33214551	4	10	theme	O-GlcNAc	572:579	arg1	OCPs					612:615	OCPs	612:615	OCPs	612:615	We identify 875 genotoxic stress-induced O-GlcNAc chromatin-associated proteins (OCPs), including 88 O-GlcNAc chromatin-associated transcription factors and cofactors (OCTFs), subsequently map their genomic loci, and construct a comprehensive transcriptional reprogramming network.
33214551	4	10	theme	O-GlcNAc	572:579	arg1	factors					676:682	88 O-GlcNAc chromatin-associated transcription factors	629:682	88 O-GlcNAc chromatin-associated transcription factors	629:682	We identify 875 genotoxic stress-induced O-GlcNAc chromatin-associated proteins (OCPs), including 88 O-GlcNAc chromatin-associated transcription factors and cofactors (OCTFs), subsequently map their genomic loci, and construct a comprehensive transcriptional reprogramming network.
33214551	4	10	theme	O-GlcNAc	572:579	arg1	proteins					602:609	875 genotoxic stress-induced O-GlcNAc chromatin-associated proteins	543:609	875 genotoxic stress-induced O-GlcNAc chromatin-associated proteins (OCPs)	543:616	We identify 875 genotoxic stress-induced O-GlcNAc chromatin-associated proteins (OCPs), including 88 O-GlcNAc chromatin-associated transcription factors and cofactors (OCTFs), subsequently map their genomic loci, and construct a comprehensive transcriptional reprogramming network.
33214551	4	10	theme	O-GlcNAc	572:579	arg1	cofactors					688:696	cofactors	688:696	cofactors (OCTFs)	688:704	We identify 875 genotoxic stress-induced O-GlcNAc chromatin-associated proteins (OCPs), including 88 O-GlcNAc chromatin-associated transcription factors and cofactors (OCTFs), subsequently map their genomic loci, and construct a comprehensive transcriptional reprogramming network.
33214551	3	11	theme	O-GlcNAc	436:443	arg1	function					445:452	survey O-GlcNAc function	429:452	survey O-GlcNAc function in human breast cancer cells stimulated with the genotoxic agent adriamycin	429:528	Here, comprehensive data are obtained by a chemical reporter-based method to survey O-GlcNAc function in human breast cancer cells stimulated with the genotoxic agent adriamycin.
33214551	0	12	theme	genotoxic	115:123	arg1	response					132:139	an O-GlcNAc-regulated genotoxic stress response	93:139	an O-GlcNAc-regulated genotoxic stress response	93:139	Proteomic profiling and genome-wide mapping of O-GlcNAc chromatin-associated proteins reveal an O-GlcNAc-regulated genotoxic stress response.
33214551	6	13	theme	dynamic	918:924	arg1	feature					1016:1022	a crucial feature	1006:1022	a crucial feature in the specific transcriptional activation of genes involved in the adaptation of cancer cells to genotoxic stress	1006:1137	The dynamic binding switch of hundreds of OCPs from enhancers to promoters is identified as a crucial feature in the specific transcriptional activation of genes involved in the adaptation of cancer cells to genotoxic stress.
33214551	6	13	theme	dynamic	918:924	arg1	switch					934:939	The dynamic binding switch	914:939	The dynamic binding switch of hundreds of OCPs from enhancers to promoters	914:987	The dynamic binding switch of hundreds of OCPs from enhancers to promoters is identified as a crucial feature in the specific transcriptional activation of genes involved in the adaptation of cancer cells to genotoxic stress.
33214551	8	14	theme	genotoxic	1440:1448	arg1	stress					1450:1455	genotoxic stress	1440:1455	genotoxic stress	1440:1455	These results provide a valuable clue suggesting that OCPs act as stress sensors by regulating the expression of various genes to protect cancer cells from genotoxic stress.
33214551	8	15	theme	genes	1405:1409	arg1	expression					1383:1392	the expression	1379:1392	the expression of various genes to protect cancer cells from genotoxic stress	1379:1455	These results provide a valuable clue suggesting that OCPs act as stress sensors by regulating the expression of various genes to protect cancer cells from genotoxic stress.
33214551	8	16	theme	various	1397:1403	arg1	genes					1405:1409	various genes	1397:1409	various genes	1397:1409	These results provide a valuable clue suggesting that OCPs act as stress sensors by regulating the expression of various genes to protect cancer cells from genotoxic stress.
33214551	1	17	theme	stress	203:208	arg1	program					219:225	the stress response program	199:225	the stress response program	199:225	O-GlcNAc modification plays critical roles in regulating the stress response program and cellular homeostasis.
33214551	5	18	theme	OCPs	893:896	arg1	interactions					877:888	the genome-wide interactions	861:888	the genome-wide interactions of OCPs with chromatin	861:911	Notably, genotoxicity-induced O-GlcNAc enhances the genome-wide interactions of OCPs with chromatin.
33214551	2	19	theme	regulated	313:321	arg1	mechanism					323:331	the O-GlcNAc regulated mechanism	300:331	the O-GlcNAc regulated mechanism	300:331	However, systematic and multi-omics studies on the O-GlcNAc regulated mechanism have been limited.
33214551	1	20	theme	response	210:217	arg1	program					219:225	the stress response program	199:225	the stress response program	199:225	O-GlcNAc modification plays critical roles in regulating the stress response program and cellular homeostasis.
33214551	3	21	theme	survey	429:434	arg1	function					445:452	survey O-GlcNAc function	429:452	survey O-GlcNAc function in human breast cancer cells stimulated with the genotoxic agent adriamycin	429:528	Here, comprehensive data are obtained by a chemical reporter-based method to survey O-GlcNAc function in human breast cancer cells stimulated with the genotoxic agent adriamycin.
33214551	7	22	theme	factor	1157:1162	arg1	NRF1					1194:1197	NRF1	1194:1197	NRF1	1194:1197	The OCTF nuclear factor erythroid 2-related factor-1 (NRF1) is found to be a key response regulator in O-GlcNAc-modulated cellular homeostasis.
33214551	7	22	theme	factor	1157:1162	arg1	factor-1					1184:1191	The OCTF nuclear factor erythroid 2-related factor-1	1140:1191	The OCTF nuclear factor erythroid 2-related factor-1 (NRF1)	1140:1198	The OCTF nuclear factor erythroid 2-related factor-1 (NRF1) is found to be a key response regulator in O-GlcNAc-modulated cellular homeostasis.
33214551	7	22	theme	factor	1157:1162	arg1	regulator					1230:1238	a key response regulator	1215:1238	a key response regulator	1215:1238	The OCTF nuclear factor erythroid 2-related factor-1 (NRF1) is found to be a key response regulator in O-GlcNAc-modulated cellular homeostasis.
33214551	3	23	theme	cancer	470:475	arg1	cells					477:481	human breast cancer cells	457:481	human breast cancer cells stimulated with the genotoxic agent adriamycin	457:528	Here, comprehensive data are obtained by a chemical reporter-based method to survey O-GlcNAc function in human breast cancer cells stimulated with the genotoxic agent adriamycin.
33214551	0	24	theme	Proteomic	0:8	arg1	profiling					10:18	Proteomic profiling	0:18	Proteomic profiling	0:18	Proteomic profiling and genome-wide mapping of O-GlcNAc chromatin-associated proteins reveal an O-GlcNAc-regulated genotoxic stress response.
33214551	7	25	theme	O-GlcNAc-modulated	1243:1260	arg1	homeostasis					1271:1281	O-GlcNAc-modulated cellular homeostasis	1243:1281	O-GlcNAc-modulated cellular homeostasis	1243:1281	The OCTF nuclear factor erythroid 2-related factor-1 (NRF1) is found to be a key response regulator in O-GlcNAc-modulated cellular homeostasis.
33214551	7	26	theme	2-related	1174:1182	arg1	NRF1					1194:1197	NRF1	1194:1197	NRF1	1194:1197	The OCTF nuclear factor erythroid 2-related factor-1 (NRF1) is found to be a key response regulator in O-GlcNAc-modulated cellular homeostasis.
33214551	7	26	theme	2-related	1174:1182	arg1	factor-1					1184:1191	The OCTF nuclear factor erythroid 2-related factor-1	1140:1191	The OCTF nuclear factor erythroid 2-related factor-1 (NRF1)	1140:1198	The OCTF nuclear factor erythroid 2-related factor-1 (NRF1) is found to be a key response regulator in O-GlcNAc-modulated cellular homeostasis.
33214551	7	26	theme	2-related	1174:1182	arg1	regulator					1230:1238	a key response regulator	1215:1238	a key response regulator	1215:1238	The OCTF nuclear factor erythroid 2-related factor-1 (NRF1) is found to be a key response regulator in O-GlcNAc-modulated cellular homeostasis.
33214551	6	27	theme	cells	1113:1117	arg1	adaptation					1092:1101	the adaptation	1088:1101	the adaptation of cancer cells to genotoxic stress	1088:1137	The dynamic binding switch of hundreds of OCPs from enhancers to promoters is identified as a crucial feature in the specific transcriptional activation of genes involved in the adaptation of cancer cells to genotoxic stress.
33214551	8	28	theme	stress	1350:1355	arg1	sensors					1357:1363	stress sensors	1350:1363	stress sensors	1350:1363	These results provide a valuable clue suggesting that OCPs act as stress sensors by regulating the expression of various genes to protect cancer cells from genotoxic stress.
33214551	8	28	theme	stress	1350:1355	arg1	OCPs					1338:1341	OCPs	1338:1341	OCPs	1338:1341	These results provide a valuable clue suggesting that OCPs act as stress sensors by regulating the expression of various genes to protect cancer cells from genotoxic stress.
33214551	0	29	theme	genome-wide	24:34	arg1	mapping					36:42	genome-wide mapping	24:42	genome-wide mapping of O-GlcNAc chromatin-associated proteins	24:84	Proteomic profiling and genome-wide mapping of O-GlcNAc chromatin-associated proteins reveal an O-GlcNAc-regulated genotoxic stress response.
33214551	8	30	theme	valuable	1308:1315	arg1	clue					1317:1320	a valuable clue	1306:1320	a valuable clue suggesting that OCPs act as stress sensors by regulating the expression of various genes to protect cancer cells from genotoxic stress	1306:1455	These results provide a valuable clue suggesting that OCPs act as stress sensors by regulating the expression of various genes to protect cancer cells from genotoxic stress.
33214551	2	31	from	studies	289:295	arg1	mechanism					323:331	the O-GlcNAc regulated mechanism	300:331	the O-GlcNAc regulated mechanism	300:331	However, systematic and multi-omics studies on the O-GlcNAc regulated mechanism have been limited.
33214551	1	32	theme	cellular	231:238	arg1	homeostasis					240:250	cellular homeostasis	231:250	cellular homeostasis	231:250	O-GlcNAc modification plays critical roles in regulating the stress response program and cellular homeostasis.
33214551	4	33	theme	O-GlcNAc	632:639	arg1	factors					676:682	88 O-GlcNAc chromatin-associated transcription factors	629:682	88 O-GlcNAc chromatin-associated transcription factors	629:682	We identify 875 genotoxic stress-induced O-GlcNAc chromatin-associated proteins (OCPs), including 88 O-GlcNAc chromatin-associated transcription factors and cofactors (OCTFs), subsequently map their genomic loci, and construct a comprehensive transcriptional reprogramming network.
33214551	3	34	theme	human	457:461	arg1	cells					477:481	human breast cancer cells	457:481	human breast cancer cells stimulated with the genotoxic agent adriamycin	457:528	Here, comprehensive data are obtained by a chemical reporter-based method to survey O-GlcNAc function in human breast cancer cells stimulated with the genotoxic agent adriamycin.
33214551	6	35	theme	genes	1070:1074	arg1	activation					1056:1065	the specific transcriptional activation	1027:1065	the specific transcriptional activation of genes involved in the adaptation of cancer cells to genotoxic stress	1027:1137	The dynamic binding switch of hundreds of OCPs from enhancers to promoters is identified as a crucial feature in the specific transcriptional activation of genes involved in the adaptation of cancer cells to genotoxic stress.
33214551	7	36	theme	erythroid	1164:1172	arg1	NRF1					1194:1197	NRF1	1194:1197	NRF1	1194:1197	The OCTF nuclear factor erythroid 2-related factor-1 (NRF1) is found to be a key response regulator in O-GlcNAc-modulated cellular homeostasis.
33214551	7	36	theme	erythroid	1164:1172	arg1	factor-1					1184:1191	The OCTF nuclear factor erythroid 2-related factor-1	1140:1191	The OCTF nuclear factor erythroid 2-related factor-1 (NRF1)	1140:1198	The OCTF nuclear factor erythroid 2-related factor-1 (NRF1) is found to be a key response regulator in O-GlcNAc-modulated cellular homeostasis.
33214551	7	36	theme	erythroid	1164:1172	arg1	regulator					1230:1238	a key response regulator	1215:1238	a key response regulator	1215:1238	The OCTF nuclear factor erythroid 2-related factor-1 (NRF1) is found to be a key response regulator in O-GlcNAc-modulated cellular homeostasis.
33214551	2	37	theme	multi-omics	277:287	arg1	studies					289:295	systematic and multi-omics studies	262:295	systematic and multi-omics studies on the O-GlcNAc regulated mechanism	262:331	However, systematic and multi-omics studies on the O-GlcNAc regulated mechanism have been limited.
33214551	7	38	theme	response	1221:1228	arg1	factor-1					1184:1191	The OCTF nuclear factor erythroid 2-related factor-1	1140:1191	The OCTF nuclear factor erythroid 2-related factor-1 (NRF1)	1140:1198	The OCTF nuclear factor erythroid 2-related factor-1 (NRF1) is found to be a key response regulator in O-GlcNAc-modulated cellular homeostasis.
33214551	7	38	theme	response	1221:1228	arg1	regulator					1230:1238	a key response regulator	1215:1238	a key response regulator	1215:1238	The OCTF nuclear factor erythroid 2-related factor-1 (NRF1) is found to be a key response regulator in O-GlcNAc-modulated cellular homeostasis.
33214551	3	39	theme	breast	463:468	arg1	cells					477:481	human breast cancer cells	457:481	human breast cancer cells stimulated with the genotoxic agent adriamycin	457:528	Here, comprehensive data are obtained by a chemical reporter-based method to survey O-GlcNAc function in human breast cancer cells stimulated with the genotoxic agent adriamycin.
33214551	6	40	theme	cancer	1106:1111	arg1	cells					1113:1117	cancer cells	1106:1117	cancer cells	1106:1117	The dynamic binding switch of hundreds of OCPs from enhancers to promoters is identified as a crucial feature in the specific transcriptional activation of genes involved in the adaptation of cancer cells to genotoxic stress.
33214551	5	41	theme	genotoxicity-induced	822:841	arg1	O-GlcNAc					843:850	genotoxicity-induced O-GlcNAc	822:850	genotoxicity-induced O-GlcNAc	822:850	Notably, genotoxicity-induced O-GlcNAc enhances the genome-wide interactions of OCPs with chromatin.
33214551	6	42	theme	genotoxic	1122:1130	arg1	stress					1132:1137	genotoxic stress	1122:1137	genotoxic stress	1122:1137	The dynamic binding switch of hundreds of OCPs from enhancers to promoters is identified as a crucial feature in the specific transcriptional activation of genes involved in the adaptation of cancer cells to genotoxic stress.
33214551	3	43	theme	genotoxic	503:511	arg1	adriamycin					519:528	the genotoxic agent adriamycin	499:528	the genotoxic agent adriamycin	499:528	Here, comprehensive data are obtained by a chemical reporter-based method to survey O-GlcNAc function in human breast cancer cells stimulated with the genotoxic agent adriamycin.
33214551	0	44	theme	chromatin-associated	56:75	arg1	proteins					77:84	O-GlcNAc chromatin-associated proteins	47:84	O-GlcNAc chromatin-associated proteins	47:84	Proteomic profiling and genome-wide mapping of O-GlcNAc chromatin-associated proteins reveal an O-GlcNAc-regulated genotoxic stress response.
33214551	3	45	theme	chemical	395:402	arg1	method					419:424	a chemical reporter-based method	393:424	a chemical reporter-based method to survey O-GlcNAc function in human breast cancer cells stimulated with the genotoxic agent adriamycin	393:528	Here, comprehensive data are obtained by a chemical reporter-based method to survey O-GlcNAc function in human breast cancer cells stimulated with the genotoxic agent adriamycin.
33214551	7	46	theme	nuclear	1149:1155	arg1	NRF1					1194:1197	NRF1	1194:1197	NRF1	1194:1197	The OCTF nuclear factor erythroid 2-related factor-1 (NRF1) is found to be a key response regulator in O-GlcNAc-modulated cellular homeostasis.
33214551	7	46	theme	nuclear	1149:1155	arg1	factor-1					1184:1191	The OCTF nuclear factor erythroid 2-related factor-1	1140:1191	The OCTF nuclear factor erythroid 2-related factor-1 (NRF1)	1140:1198	The OCTF nuclear factor erythroid 2-related factor-1 (NRF1) is found to be a key response regulator in O-GlcNAc-modulated cellular homeostasis.
33214551	7	46	theme	nuclear	1149:1155	arg1	regulator					1230:1238	a key response regulator	1215:1238	a key response regulator	1215:1238	The OCTF nuclear factor erythroid 2-related factor-1 (NRF1) is found to be a key response regulator in O-GlcNAc-modulated cellular homeostasis.
33214551	5	47	theme	genome-wide	865:875	arg1	interactions					877:888	the genome-wide interactions	861:888	the genome-wide interactions of OCPs with chromatin	861:911	Notably, genotoxicity-induced O-GlcNAc enhances the genome-wide interactions of OCPs with chromatin.
33214551	2	48	theme	systematic	262:271	arg1	studies					289:295	systematic and multi-omics studies	262:295	systematic and multi-omics studies on the O-GlcNAc regulated mechanism	262:331	However, systematic and multi-omics studies on the O-GlcNAc regulated mechanism have been limited.
33214551	1	49	theme	O-GlcNAc	142:149	arg1	modification					151:162	O-GlcNAc modification	142:162	O-GlcNAc modification	142:162	O-GlcNAc modification plays critical roles in regulating the stress response program and cellular homeostasis.
33214551	0	50	theme	O-GlcNAc	47:54	arg1	proteins					77:84	O-GlcNAc chromatin-associated proteins	47:84	O-GlcNAc chromatin-associated proteins	47:84	Proteomic profiling and genome-wide mapping of O-GlcNAc chromatin-associated proteins reveal an O-GlcNAc-regulated genotoxic stress response.
33214551	6	51	theme	transcriptional	1040:1054	arg1	activation					1056:1065	the specific transcriptional activation	1027:1065	the specific transcriptional activation of genes involved in the adaptation of cancer cells to genotoxic stress	1027:1137	The dynamic binding switch of hundreds of OCPs from enhancers to promoters is identified as a crucial feature in the specific transcriptional activation of genes involved in the adaptation of cancer cells to genotoxic stress.
33214551	4	52	theme	stress-induced	557:570	arg1	OCPs					612:615	OCPs	612:615	OCPs	612:615	We identify 875 genotoxic stress-induced O-GlcNAc chromatin-associated proteins (OCPs), including 88 O-GlcNAc chromatin-associated transcription factors and cofactors (OCTFs), subsequently map their genomic loci, and construct a comprehensive transcriptional reprogramming network.
33214551	4	52	theme	stress-induced	557:570	arg1	factors					676:682	88 O-GlcNAc chromatin-associated transcription factors	629:682	88 O-GlcNAc chromatin-associated transcription factors	629:682	We identify 875 genotoxic stress-induced O-GlcNAc chromatin-associated proteins (OCPs), including 88 O-GlcNAc chromatin-associated transcription factors and cofactors (OCTFs), subsequently map their genomic loci, and construct a comprehensive transcriptional reprogramming network.
33214551	4	52	theme	stress-induced	557:570	arg1	proteins					602:609	875 genotoxic stress-induced O-GlcNAc chromatin-associated proteins	543:609	875 genotoxic stress-induced O-GlcNAc chromatin-associated proteins (OCPs)	543:616	We identify 875 genotoxic stress-induced O-GlcNAc chromatin-associated proteins (OCPs), including 88 O-GlcNAc chromatin-associated transcription factors and cofactors (OCTFs), subsequently map their genomic loci, and construct a comprehensive transcriptional reprogramming network.
33214551	4	52	theme	stress-induced	557:570	arg1	cofactors					688:696	cofactors	688:696	cofactors (OCTFs)	688:704	We identify 875 genotoxic stress-induced O-GlcNAc chromatin-associated proteins (OCPs), including 88 O-GlcNAc chromatin-associated transcription factors and cofactors (OCTFs), subsequently map their genomic loci, and construct a comprehensive transcriptional reprogramming network.
33214551	6	53	theme	OCPs	956:959	arg1	hundreds					944:951	hundreds	944:951	hundreds of OCPs from enhancers	944:974	The dynamic binding switch of hundreds of OCPs from enhancers to promoters is identified as a crucial feature in the specific transcriptional activation of genes involved in the adaptation of cancer cells to genotoxic stress.
33214551	4	54	theme	reprogramming	790:802	arg1	network					804:810	a comprehensive transcriptional reprogramming network	758:810	a comprehensive transcriptional reprogramming network	758:810	We identify 875 genotoxic stress-induced O-GlcNAc chromatin-associated proteins (OCPs), including 88 O-GlcNAc chromatin-associated transcription factors and cofactors (OCTFs), subsequently map their genomic loci, and construct a comprehensive transcriptional reprogramming network.
33214551	6	55	theme	specific	1031:1038	arg1	activation					1056:1065	the specific transcriptional activation	1027:1065	the specific transcriptional activation of genes involved in the adaptation of cancer cells to genotoxic stress	1027:1137	The dynamic binding switch of hundreds of OCPs from enhancers to promoters is identified as a crucial feature in the specific transcriptional activation of genes involved in the adaptation of cancer cells to genotoxic stress.
33214551	5	56	with	interactions	877:888	arg1	chromatin					903:911	chromatin	903:911	chromatin	903:911	Notably, genotoxicity-induced O-GlcNAc enhances the genome-wide interactions of OCPs with chromatin.
33214551	2	57	theme	O-GlcNAc	304:311	arg1	mechanism					323:331	the O-GlcNAc regulated mechanism	300:331	the O-GlcNAc regulated mechanism	300:331	However, systematic and multi-omics studies on the O-GlcNAc regulated mechanism have been limited.
33214551	6	58	theme	binding	926:932	arg1	feature					1016:1022	a crucial feature	1006:1022	a crucial feature in the specific transcriptional activation of genes involved in the adaptation of cancer cells to genotoxic stress	1006:1137	The dynamic binding switch of hundreds of OCPs from enhancers to promoters is identified as a crucial feature in the specific transcriptional activation of genes involved in the adaptation of cancer cells to genotoxic stress.
33214551	6	58	theme	binding	926:932	arg1	switch					934:939	The dynamic binding switch	914:939	The dynamic binding switch of hundreds of OCPs from enhancers to promoters	914:987	The dynamic binding switch of hundreds of OCPs from enhancers to promoters is identified as a crucial feature in the specific transcriptional activation of genes involved in the adaptation of cancer cells to genotoxic stress.
33214551	7	59	from	regulator	1230:1238	arg1	homeostasis					1271:1281	O-GlcNAc-modulated cellular homeostasis	1243:1281	O-GlcNAc-modulated cellular homeostasis	1243:1281	The OCTF nuclear factor erythroid 2-related factor-1 (NRF1) is found to be a key response regulator in O-GlcNAc-modulated cellular homeostasis.
33214551	7	60	theme	OCTF	1144:1147	arg1	NRF1					1194:1197	NRF1	1194:1197	NRF1	1194:1197	The OCTF nuclear factor erythroid 2-related factor-1 (NRF1) is found to be a key response regulator in O-GlcNAc-modulated cellular homeostasis.
33214551	7	60	theme	OCTF	1144:1147	arg1	factor-1					1184:1191	The OCTF nuclear factor erythroid 2-related factor-1	1140:1191	The OCTF nuclear factor erythroid 2-related factor-1 (NRF1)	1140:1198	The OCTF nuclear factor erythroid 2-related factor-1 (NRF1) is found to be a key response regulator in O-GlcNAc-modulated cellular homeostasis.
33214551	7	60	theme	OCTF	1144:1147	arg1	regulator					1230:1238	a key response regulator	1215:1238	a key response regulator	1215:1238	The OCTF nuclear factor erythroid 2-related factor-1 (NRF1) is found to be a key response regulator in O-GlcNAc-modulated cellular homeostasis.
33214551	6	61	theme	hundreds	944:951	arg1	feature					1016:1022	a crucial feature	1006:1022	a crucial feature in the specific transcriptional activation of genes involved in the adaptation of cancer cells to genotoxic stress	1006:1137	The dynamic binding switch of hundreds of OCPs from enhancers to promoters is identified as a crucial feature in the specific transcriptional activation of genes involved in the adaptation of cancer cells to genotoxic stress.
33214551	6	61	theme	hundreds	944:951	arg1	switch					934:939	The dynamic binding switch	914:939	The dynamic binding switch of hundreds of OCPs from enhancers to promoters	914:987	The dynamic binding switch of hundreds of OCPs from enhancers to promoters is identified as a crucial feature in the specific transcriptional activation of genes involved in the adaptation of cancer cells to genotoxic stress.
33214551	1	62	theme	critical	170:177	arg1	roles					179:183	critical roles	170:183	critical roles	170:183	O-GlcNAc modification plays critical roles in regulating the stress response program and cellular homeostasis.
33214551	7	63	theme	cellular	1262:1269	arg1	homeostasis					1271:1281	O-GlcNAc-modulated cellular homeostasis	1243:1281	O-GlcNAc-modulated cellular homeostasis	1243:1281	The OCTF nuclear factor erythroid 2-related factor-1 (NRF1) is found to be a key response regulator in O-GlcNAc-modulated cellular homeostasis.
33214551	6	64	from	feature	1016:1022	arg1	activation					1056:1065	the specific transcriptional activation	1027:1065	the specific transcriptional activation of genes involved in the adaptation of cancer cells to genotoxic stress	1027:1137	The dynamic binding switch of hundreds of OCPs from enhancers to promoters is identified as a crucial feature in the specific transcriptional activation of genes involved in the adaptation of cancer cells to genotoxic stress.
33214551	3	65	theme	agent	513:517	arg1	adriamycin					519:528	the genotoxic agent adriamycin	499:528	the genotoxic agent adriamycin	499:528	Here, comprehensive data are obtained by a chemical reporter-based method to survey O-GlcNAc function in human breast cancer cells stimulated with the genotoxic agent adriamycin.
33214551	8	66	theme	cancer	1422:1427	arg1	cells					1429:1433	cancer cells	1422:1433	cancer cells	1422:1433	These results provide a valuable clue suggesting that OCPs act as stress sensors by regulating the expression of various genes to protect cancer cells from genotoxic stress.
33214551	4	67	theme	genomic	730:736	arg1	loci					738:741	their genomic loci	724:741	their genomic loci	724:741	We identify 875 genotoxic stress-induced O-GlcNAc chromatin-associated proteins (OCPs), including 88 O-GlcNAc chromatin-associated transcription factors and cofactors (OCTFs), subsequently map their genomic loci, and construct a comprehensive transcriptional reprogramming network.
33214551	6	68	theme	crucial	1008:1014	arg1	feature					1016:1022	a crucial feature	1006:1022	a crucial feature in the specific transcriptional activation of genes involved in the adaptation of cancer cells to genotoxic stress	1006:1137	The dynamic binding switch of hundreds of OCPs from enhancers to promoters is identified as a crucial feature in the specific transcriptional activation of genes involved in the adaptation of cancer cells to genotoxic stress.
33214551	6	68	theme	crucial	1008:1014	arg1	switch					934:939	The dynamic binding switch	914:939	The dynamic binding switch of hundreds of OCPs from enhancers to promoters	914:987	The dynamic binding switch of hundreds of OCPs from enhancers to promoters is identified as a crucial feature in the specific transcriptional activation of genes involved in the adaptation of cancer cells to genotoxic stress.
33214551	0	69	theme	proteins	77:84	arg1	profiling					10:18	Proteomic profiling	0:18	Proteomic profiling	0:18	Proteomic profiling and genome-wide mapping of O-GlcNAc chromatin-associated proteins reveal an O-GlcNAc-regulated genotoxic stress response.
33214551	0	69	theme	proteins	77:84	arg1	mapping					36:42	genome-wide mapping	24:42	genome-wide mapping of O-GlcNAc chromatin-associated proteins	24:84	Proteomic profiling and genome-wide mapping of O-GlcNAc chromatin-associated proteins reveal an O-GlcNAc-regulated genotoxic stress response.
33214551	3	70	from	function	445:452	arg1	cells					477:481	human breast cancer cells	457:481	human breast cancer cells stimulated with the genotoxic agent adriamycin	457:528	Here, comprehensive data are obtained by a chemical reporter-based method to survey O-GlcNAc function in human breast cancer cells stimulated with the genotoxic agent adriamycin.
33214551	6	71	from	hundreds	944:951	arg1	enhancers					966:974	enhancers	966:974	enhancers	966:974	The dynamic binding switch of hundreds of OCPs from enhancers to promoters is identified as a crucial feature in the specific transcriptional activation of genes involved in the adaptation of cancer cells to genotoxic stress.
33214551	6	72	from	enhancers	966:974	arg1	OCPs					956:959	OCPs	956:959	OCPs from enhancers	956:974	The dynamic binding switch of hundreds of OCPs from enhancers to promoters is identified as a crucial feature in the specific transcriptional activation of genes involved in the adaptation of cancer cells to genotoxic stress.
33214551	6	72	from	enhancers	966:974	arg1	hundreds					944:951	hundreds	944:951	hundreds of OCPs from enhancers	944:974	The dynamic binding switch of hundreds of OCPs from enhancers to promoters is identified as a crucial feature in the specific transcriptional activation of genes involved in the adaptation of cancer cells to genotoxic stress.
33214551	3	73	theme	reporter-based	404:417	arg1	method					419:424	a chemical reporter-based method	393:424	a chemical reporter-based method to survey O-GlcNAc function in human breast cancer cells stimulated with the genotoxic agent adriamycin	393:528	Here, comprehensive data are obtained by a chemical reporter-based method to survey O-GlcNAc function in human breast cancer cells stimulated with the genotoxic agent adriamycin.
35008409	0	0	theme	Lung	82:85	arg1	Aggressiveness					94:107	Lung Cancer Aggressiveness	82:107	Lung Cancer Aggressiveness	82:107	Comparative O-GlcNAc Proteomic Analysis Reveals a Role of O-GlcNAcylated SAM68 in Lung Cancer Aggressiveness.
35008409	6	1	theme	N-terminal	963:972	arg1	region					974:979	the N-terminal region	959:979	the N-terminal region	959:979	Eleven O-GlcNAcylation sites were identified, and data from mutant analysis suggested that multiple serine residues in the N-terminal region are important for O-GlcNAcylation and the function of SAM68 in modulating cancer cell migration and invasion.
35008409	7	2	theme	cancer	1180:1185	arg1	stages					1187:1192	late cancer stages	1175:1192	late cancer stages	1175:1192	Analysis of clinical specimens found that high SAM68 expression was associated with late cancer stages, and patients with high-OGT/high-SAM68 expression in their tumors had poorer overall survival compared to those with low-OGT/low-SAM68 expression.
35008409	1	3	theme	protein	173:179	arg1	O-GlcNAcylation					110:124	O-GlcNAcylation	110:124	O-GlcNAcylation	110:124	O-GlcNAcylation is a reversible and dynamic post-translational protein modification catalyzed by O-GlcNAc transferase (OGT).
35008409	1	3	theme	protein	173:179	arg1	modification					181:192	a reversible and dynamic post-translational protein modification	129:192	a reversible and dynamic post-translational protein modification catalyzed by O-GlcNAc transferase (OGT)	129:232	O-GlcNAcylation is a reversible and dynamic post-translational protein modification catalyzed by O-GlcNAc transferase (OGT).
35008409	6	4	theme	cancer	1055:1060	arg1	cell					1062:1065	cancer cell migration and invasion	1055:1088	cell	1062:1065	Eleven O-GlcNAcylation sites were identified, and data from mutant analysis suggested that multiple serine residues in the N-terminal region are important for O-GlcNAcylation and the function of SAM68 in modulating cancer cell migration and invasion.
35008409	3	5	theme	up-regulated	567:578	arg1	candidates					580:589	106 up-regulated candidates	563:589	106 up-regulated candidates	563:589	Here, we report our comparative O-GlcNAc proteome profiling of two differentially invasive lung adenocarcinoma cell lines, which identified 158 down-regulated and 106 up-regulated candidates in highly invasive cells.
35008409	7	6	theme	poorer	1264:1269	arg1	survival					1279:1286	poorer overall survival	1264:1286	poorer overall survival	1264:1286	Analysis of clinical specimens found that high SAM68 expression was associated with late cancer stages, and patients with high-OGT/high-SAM68 expression in their tumors had poorer overall survival compared to those with low-OGT/low-SAM68 expression.
35008409	6	7	dep	cell	1062:1065	arg1	migration					1067:1075	migration	1067:1075	migration	1067:1075	Eleven O-GlcNAcylation sites were identified, and data from mutant analysis suggested that multiple serine residues in the N-terminal region are important for O-GlcNAcylation and the function of SAM68 in modulating cancer cell migration and invasion.
35008409	2	8	theme	O-GlcNAc	315:322	arg1	profile					333:339	the O-GlcNAc proteome profile	311:339	the O-GlcNAc proteome profile for cancer aggressiveness	311:365	Despite the reported association of O-GlcNAcylation with cancer metastasis, the O-GlcNAc proteome profile for cancer aggressiveness remains largely uncharacterized.
35008409	4	9	theme	RNA-binding	662:672	arg1	SAM68					683:687	SAM68	683:687	SAM68 (SRC associated in mitosis of 68 kDa)	683:725	Among these differential proteins, a nuclear RNA-binding protein, SAM68 (SRC associated in mitosis of 68 kDa), was further investigated.
35008409	4	9	theme	RNA-binding	662:672	arg1	protein					674:680	a nuclear RNA-binding protein	652:680	a nuclear RNA-binding protein	652:680	Among these differential proteins, a nuclear RNA-binding protein, SAM68 (SRC associated in mitosis of 68 kDa), was further investigated.
35008409	0	10	theme	Cancer	87:92	arg1	Aggressiveness					94:107	Lung Cancer Aggressiveness	82:107	Lung Cancer Aggressiveness	82:107	Comparative O-GlcNAc Proteomic Analysis Reveals a Role of O-GlcNAcylated SAM68 in Lung Cancer Aggressiveness.
35008409	7	11	theme	late	1175:1178	arg1	stages					1187:1192	late cancer stages	1175:1192	late cancer stages	1175:1192	Analysis of clinical specimens found that high SAM68 expression was associated with late cancer stages, and patients with high-OGT/high-SAM68 expression in their tumors had poorer overall survival compared to those with low-OGT/low-SAM68 expression.
35008409	6	12	theme	O-GlcNAcylation	847:861	arg1	sites					863:867	Eleven O-GlcNAcylation sites	840:867	Eleven O-GlcNAcylation sites	840:867	Eleven O-GlcNAcylation sites were identified, and data from mutant analysis suggested that multiple serine residues in the N-terminal region are important for O-GlcNAcylation and the function of SAM68 in modulating cancer cell migration and invasion.
35008409	4	13	theme	nuclear	654:660	arg1	SAM68					683:687	SAM68	683:687	SAM68 (SRC associated in mitosis of 68 kDa)	683:725	Among these differential proteins, a nuclear RNA-binding protein, SAM68 (SRC associated in mitosis of 68 kDa), was further investigated.
35008409	4	13	theme	nuclear	654:660	arg1	protein					674:680	a nuclear RNA-binding protein	652:680	a nuclear RNA-binding protein	652:680	Among these differential proteins, a nuclear RNA-binding protein, SAM68 (SRC associated in mitosis of 68 kDa), was further investigated.
35008409	6	14	from	residues	947:954	arg1	region					974:979	the N-terminal region	959:979	the N-terminal region	959:979	Eleven O-GlcNAcylation sites were identified, and data from mutant analysis suggested that multiple serine residues in the N-terminal region are important for O-GlcNAcylation and the function of SAM68 in modulating cancer cell migration and invasion.
35008409	0	15	from	Role	50:53	arg1	Aggressiveness					94:107	Lung Cancer Aggressiveness	82:107	Lung Cancer Aggressiveness	82:107	Comparative O-GlcNAc Proteomic Analysis Reveals a Role of O-GlcNAcylated SAM68 in Lung Cancer Aggressiveness.
35008409	7	16	with	patients	1199:1206	arg1	expression					1233:1242	high-OGT/high-SAM68 expression	1213:1242	high-OGT/high-SAM68 expression in their tumors	1213:1258	Analysis of clinical specimens found that high SAM68 expression was associated with late cancer stages, and patients with high-OGT/high-SAM68 expression in their tumors had poorer overall survival compared to those with low-OGT/low-SAM68 expression.
35008409	3	17	theme	lung	491:494	arg1	lines					516:520	two differentially invasive lung adenocarcinoma cell lines	463:520	two differentially invasive lung adenocarcinoma cell lines	463:520	Here, we report our comparative O-GlcNAc proteome profiling of two differentially invasive lung adenocarcinoma cell lines, which identified 158 down-regulated and 106 up-regulated candidates in highly invasive cells.
35008409	6	18	theme	SAM68	1035:1039	arg1	O-GlcNAcylation					999:1013	O-GlcNAcylation	999:1013	O-GlcNAcylation	999:1013	Eleven O-GlcNAcylation sites were identified, and data from mutant analysis suggested that multiple serine residues in the N-terminal region are important for O-GlcNAcylation and the function of SAM68 in modulating cancer cell migration and invasion.
35008409	6	18	theme	SAM68	1035:1039	arg1	function					1023:1030	the function	1019:1030	the function of SAM68 in modulating cancer cell migration and invasion	1019:1088	Eleven O-GlcNAcylation sites were identified, and data from mutant analysis suggested that multiple serine residues in the N-terminal region are important for O-GlcNAcylation and the function of SAM68 in modulating cancer cell migration and invasion.
35008409	6	19	theme	multiple	931:938	arg1	residues					947:954	multiple serine residues	931:954	multiple serine residues in the N-terminal region	931:979	Eleven O-GlcNAcylation sites were identified, and data from mutant analysis suggested that multiple serine residues in the N-terminal region are important for O-GlcNAcylation and the function of SAM68 in modulating cancer cell migration and invasion.
35008409	8	20	theme	cancer	1456:1461	arg1	aggressiveness					1463:1476	lung cancer aggressiveness	1451:1476	lung cancer aggressiveness	1451:1476	Our study revealed an invasiveness-associated O-GlcNAc proteome profile and connected O-GlcNAcylated SAM68 to lung cancer aggressiveness.
35008409	3	21	theme	O-GlcNAc	432:439	arg1	profiling					450:458	our comparative O-GlcNAc proteome profiling	416:458	our comparative O-GlcNAc proteome profiling	416:458	Here, we report our comparative O-GlcNAc proteome profiling of two differentially invasive lung adenocarcinoma cell lines, which identified 158 down-regulated and 106 up-regulated candidates in highly invasive cells.
35008409	7	22	from	expression	1233:1242	arg1	tumors					1253:1258	their tumors	1247:1258	their tumors	1247:1258	Analysis of clinical specimens found that high SAM68 expression was associated with late cancer stages, and patients with high-OGT/high-SAM68 expression in their tumors had poorer overall survival compared to those with low-OGT/low-SAM68 expression.
35008409	3	23	theme	adenocarcinoma	496:509	arg1	lines					516:520	two differentially invasive lung adenocarcinoma cell lines	463:520	two differentially invasive lung adenocarcinoma cell lines	463:520	Here, we report our comparative O-GlcNAc proteome profiling of two differentially invasive lung adenocarcinoma cell lines, which identified 158 down-regulated and 106 up-regulated candidates in highly invasive cells.
35008409	0	24	theme	O-GlcNAc	12:19	arg1	Analysis					31:38	Comparative O-GlcNAc Proteomic Analysis	0:38	Comparative O-GlcNAc Proteomic Analysis	0:38	Comparative O-GlcNAc Proteomic Analysis Reveals a Role of O-GlcNAcylated SAM68 in Lung Cancer Aggressiveness.
35008409	7	25	theme	SAM68	1138:1142	arg1	expression					1144:1153	high SAM68 expression	1133:1153	high SAM68 expression	1133:1153	Analysis of clinical specimens found that high SAM68 expression was associated with late cancer stages, and patients with high-OGT/high-SAM68 expression in their tumors had poorer overall survival compared to those with low-OGT/low-SAM68 expression.
35008409	2	26	theme	cancer	345:350	arg1	aggressiveness					352:365	cancer aggressiveness	345:365	cancer aggressiveness	345:365	Despite the reported association of O-GlcNAcylation with cancer metastasis, the O-GlcNAc proteome profile for cancer aggressiveness remains largely uncharacterized.
35008409	6	27	theme	serine	940:945	arg1	residues					947:954	multiple serine residues	931:954	multiple serine residues in the N-terminal region	931:979	Eleven O-GlcNAcylation sites were identified, and data from mutant analysis suggested that multiple serine residues in the N-terminal region are important for O-GlcNAcylation and the function of SAM68 in modulating cancer cell migration and invasion.
35008409	1	28	theme	O-GlcNAc	207:214	arg1	OGT					229:231	OGT	229:231	OGT	229:231	O-GlcNAcylation is a reversible and dynamic post-translational protein modification catalyzed by O-GlcNAc transferase (OGT).
35008409	1	28	theme	O-GlcNAc	207:214	arg1	transferase					216:226	O-GlcNAc transferase	207:226	O-GlcNAc transferase (OGT)	207:232	O-GlcNAcylation is a reversible and dynamic post-translational protein modification catalyzed by O-GlcNAc transferase (OGT).
35008409	0	29	theme	Comparative	0:10	arg1	Analysis					31:38	Comparative O-GlcNAc Proteomic Analysis	0:38	Comparative O-GlcNAc Proteomic Analysis	0:38	Comparative O-GlcNAc Proteomic Analysis Reveals a Role of O-GlcNAcylated SAM68 in Lung Cancer Aggressiveness.
35008409	3	30	theme	invasive	482:489	arg1	lines					516:520	two differentially invasive lung adenocarcinoma cell lines	463:520	two differentially invasive lung adenocarcinoma cell lines	463:520	Here, we report our comparative O-GlcNAc proteome profiling of two differentially invasive lung adenocarcinoma cell lines, which identified 158 down-regulated and 106 up-regulated candidates in highly invasive cells.
35008409	7	31	theme	high-OGT/high-SAM68	1213:1231	arg1	expression					1233:1242	high-OGT/high-SAM68 expression	1213:1242	high-OGT/high-SAM68 expression in their tumors	1213:1258	Analysis of clinical specimens found that high SAM68 expression was associated with late cancer stages, and patients with high-OGT/high-SAM68 expression in their tumors had poorer overall survival compared to those with low-OGT/low-SAM68 expression.
35008409	8	32	theme	O-GlcNAcylated	1427:1440	arg1	SAM68					1442:1446	connected O-GlcNAcylated SAM68	1417:1446	connected O-GlcNAcylated SAM68 to lung cancer aggressiveness	1417:1476	Our study revealed an invasiveness-associated O-GlcNAc proteome profile and connected O-GlcNAcylated SAM68 to lung cancer aggressiveness.
35008409	0	33	theme	Proteomic	21:29	arg1	Analysis					31:38	Comparative O-GlcNAc Proteomic Analysis	0:38	Comparative O-GlcNAc Proteomic Analysis	0:38	Comparative O-GlcNAc Proteomic Analysis Reveals a Role of O-GlcNAcylated SAM68 in Lung Cancer Aggressiveness.
35008409	2	34	with	association	256:266	arg1	metastasis					299:308	cancer metastasis	292:308	cancer metastasis	292:308	Despite the reported association of O-GlcNAcylation with cancer metastasis, the O-GlcNAc proteome profile for cancer aggressiveness remains largely uncharacterized.
35008409	7	35	theme	high	1133:1136	arg1	expression					1144:1153	high SAM68 expression	1133:1153	high SAM68 expression	1133:1153	Analysis of clinical specimens found that high SAM68 expression was associated with late cancer stages, and patients with high-OGT/high-SAM68 expression in their tumors had poorer overall survival compared to those with low-OGT/low-SAM68 expression.
35008409	2	36	theme	proteome	324:331	arg1	profile					333:339	the O-GlcNAc proteome profile	311:339	the O-GlcNAc proteome profile for cancer aggressiveness	311:365	Despite the reported association of O-GlcNAcylation with cancer metastasis, the O-GlcNAc proteome profile for cancer aggressiveness remains largely uncharacterized.
35008409	8	37	theme	connected	1417:1425	arg1	SAM68					1442:1446	connected O-GlcNAcylated SAM68	1417:1446	connected O-GlcNAcylated SAM68 to lung cancer aggressiveness	1417:1476	Our study revealed an invasiveness-associated O-GlcNAc proteome profile and connected O-GlcNAcylated SAM68 to lung cancer aggressiveness.
35008409	4	38	theme	differential	629:640	arg1	proteins					642:649	these differential proteins	623:649	these differential proteins	623:649	Among these differential proteins, a nuclear RNA-binding protein, SAM68 (SRC associated in mitosis of 68 kDa), was further investigated.
35008409	7	39	theme	specimens	1112:1120	arg1	Analysis					1091:1098	Analysis	1091:1098	Analysis of clinical specimens	1091:1120	Analysis of clinical specimens found that high SAM68 expression was associated with late cancer stages, and patients with high-OGT/high-SAM68 expression in their tumors had poorer overall survival compared to those with low-OGT/low-SAM68 expression.
35008409	4	40	theme	kDa	722:724	arg1	mitosis					708:714	mitosis	708:714	mitosis of 68 kDa	708:724	Among these differential proteins, a nuclear RNA-binding protein, SAM68 (SRC associated in mitosis of 68 kDa), was further investigated.
35008409	3	41	theme	cell	511:514	arg1	lines					516:520	two differentially invasive lung adenocarcinoma cell lines	463:520	two differentially invasive lung adenocarcinoma cell lines	463:520	Here, we report our comparative O-GlcNAc proteome profiling of two differentially invasive lung adenocarcinoma cell lines, which identified 158 down-regulated and 106 up-regulated candidates in highly invasive cells.
35008409	6	42	theme	mutant	900:905	arg1	analysis					907:914	mutant analysis	900:914	mutant analysis	900:914	Eleven O-GlcNAcylation sites were identified, and data from mutant analysis suggested that multiple serine residues in the N-terminal region are important for O-GlcNAcylation and the function of SAM68 in modulating cancer cell migration and invasion.
35008409	2	43	theme	reported	247:254	arg1	association					256:266	the reported association	243:266	the reported association of O-GlcNAcylation with cancer metastasis	243:308	Despite the reported association of O-GlcNAcylation with cancer metastasis, the O-GlcNAc proteome profile for cancer aggressiveness remains largely uncharacterized.
35008409	7	44	contain	had	1260:1262	arg1	patients					1199:1206	patients	1199:1206	patients with high-OGT/high-SAM68 expression in their tumors	1199:1258	Analysis of clinical specimens found that high SAM68 expression was associated with late cancer stages, and patients with high-OGT/high-SAM68 expression in their tumors had poorer overall survival compared to those with low-OGT/low-SAM68 expression.
35008409	7	44	contain	had	1260:1262	arg2	survival					1279:1286	poorer overall survival	1264:1286	poorer overall survival	1264:1286	Analysis of clinical specimens found that high SAM68 expression was associated with late cancer stages, and patients with high-OGT/high-SAM68 expression in their tumors had poorer overall survival compared to those with low-OGT/low-SAM68 expression.
35008409	3	45	theme	lines	516:520	arg1	profiling					450:458	our comparative O-GlcNAc proteome profiling	416:458	our comparative O-GlcNAc proteome profiling	416:458	Here, we report our comparative O-GlcNAc proteome profiling of two differentially invasive lung adenocarcinoma cell lines, which identified 158 down-regulated and 106 up-regulated candidates in highly invasive cells.
35008409	3	46	theme	proteome	441:448	arg1	profiling					450:458	our comparative O-GlcNAc proteome profiling	416:458	our comparative O-GlcNAc proteome profiling	416:458	Here, we report our comparative O-GlcNAc proteome profiling of two differentially invasive lung adenocarcinoma cell lines, which identified 158 down-regulated and 106 up-regulated candidates in highly invasive cells.
35008409	8	47	theme	O-GlcNAc	1387:1394	arg1	profile					1405:1411	an invasiveness-associated O-GlcNAc proteome profile	1360:1411	an invasiveness-associated O-GlcNAc proteome profile	1360:1411	Our study revealed an invasiveness-associated O-GlcNAc proteome profile and connected O-GlcNAcylated SAM68 to lung cancer aggressiveness.
35008409	7	48	theme	clinical	1103:1110	arg1	specimens					1112:1120	clinical specimens	1103:1120	clinical specimens	1103:1120	Analysis of clinical specimens found that high SAM68 expression was associated with late cancer stages, and patients with high-OGT/high-SAM68 expression in their tumors had poorer overall survival compared to those with low-OGT/low-SAM68 expression.
35008409	8	49	theme	invasiveness-associated	1363:1385	arg1	profile					1405:1411	an invasiveness-associated O-GlcNAc proteome profile	1360:1411	an invasiveness-associated O-GlcNAc proteome profile	1360:1411	Our study revealed an invasiveness-associated O-GlcNAc proteome profile and connected O-GlcNAcylated SAM68 to lung cancer aggressiveness.
35008409	4	50	dep	SAM68	683:687	arg1	SRC					690:692	SRC	690:692	SRC associated in mitosis of 68 kDa	690:724	Among these differential proteins, a nuclear RNA-binding protein, SAM68 (SRC associated in mitosis of 68 kDa), was further investigated.
35008409	2	51	theme	cancer	292:297	arg1	metastasis					299:308	cancer metastasis	292:308	cancer metastasis	292:308	Despite the reported association of O-GlcNAcylation with cancer metastasis, the O-GlcNAc proteome profile for cancer aggressiveness remains largely uncharacterized.
35008409	1	52	theme	reversible	131:140	arg1	O-GlcNAcylation					110:124	O-GlcNAcylation	110:124	O-GlcNAcylation	110:124	O-GlcNAcylation is a reversible and dynamic post-translational protein modification catalyzed by O-GlcNAc transferase (OGT).
35008409	1	52	theme	reversible	131:140	arg1	modification					181:192	a reversible and dynamic post-translational protein modification	129:192	a reversible and dynamic post-translational protein modification catalyzed by O-GlcNAc transferase (OGT)	129:232	O-GlcNAcylation is a reversible and dynamic post-translational protein modification catalyzed by O-GlcNAc transferase (OGT).
35008409	3	53	theme	invasive	601:608	arg1	cells					610:614	highly invasive cells	594:614	highly invasive cells	594:614	Here, we report our comparative O-GlcNAc proteome profiling of two differentially invasive lung adenocarcinoma cell lines, which identified 158 down-regulated and 106 up-regulated candidates in highly invasive cells.
35008409	8	54	theme	lung	1451:1454	arg1	aggressiveness					1463:1476	lung cancer aggressiveness	1451:1476	lung cancer aggressiveness	1451:1476	Our study revealed an invasiveness-associated O-GlcNAc proteome profile and connected O-GlcNAcylated SAM68 to lung cancer aggressiveness.
35008409	8	55	theme	proteome	1396:1403	arg1	profile					1405:1411	an invasiveness-associated O-GlcNAc proteome profile	1360:1411	an invasiveness-associated O-GlcNAc proteome profile	1360:1411	Our study revealed an invasiveness-associated O-GlcNAc proteome profile and connected O-GlcNAcylated SAM68 to lung cancer aggressiveness.
35008409	0	56	theme	SAM68	73:77	arg1	Role					50:53	a Role	48:53	a Role of O-GlcNAcylated SAM68 in Lung Cancer Aggressiveness	48:107	Comparative O-GlcNAc Proteomic Analysis Reveals a Role of O-GlcNAcylated SAM68 in Lung Cancer Aggressiveness.
35008409	2	57	theme	O-GlcNAcylation	271:285	arg1	association					256:266	the reported association	243:266	the reported association of O-GlcNAcylation with cancer metastasis	243:308	Despite the reported association of O-GlcNAcylation with cancer metastasis, the O-GlcNAc proteome profile for cancer aggressiveness remains largely uncharacterized.
35008409	1	58	theme	dynamic	146:152	arg1	O-GlcNAcylation					110:124	O-GlcNAcylation	110:124	O-GlcNAcylation	110:124	O-GlcNAcylation is a reversible and dynamic post-translational protein modification catalyzed by O-GlcNAc transferase (OGT).
35008409	1	58	theme	dynamic	146:152	arg1	modification					181:192	a reversible and dynamic post-translational protein modification	129:192	a reversible and dynamic post-translational protein modification catalyzed by O-GlcNAc transferase (OGT)	129:232	O-GlcNAcylation is a reversible and dynamic post-translational protein modification catalyzed by O-GlcNAc transferase (OGT).
35008409	3	59	theme	comparative	420:430	arg1	profiling					450:458	our comparative O-GlcNAc proteome profiling	416:458	our comparative O-GlcNAc proteome profiling	416:458	Here, we report our comparative O-GlcNAc proteome profiling of two differentially invasive lung adenocarcinoma cell lines, which identified 158 down-regulated and 106 up-regulated candidates in highly invasive cells.
35008409	0	60	theme	O-GlcNAcylated	58:71	arg1	SAM68					73:77	O-GlcNAcylated SAM68	58:77	O-GlcNAcylated SAM68	58:77	Comparative O-GlcNAc Proteomic Analysis Reveals a Role of O-GlcNAcylated SAM68 in Lung Cancer Aggressiveness.
35008409	6	61	from	analysis	907:914	arg1	data					890:893	data	890:893	data from mutant analysis	890:914	Eleven O-GlcNAcylation sites were identified, and data from mutant analysis suggested that multiple serine residues in the N-terminal region are important for O-GlcNAcylation and the function of SAM68 in modulating cancer cell migration and invasion.
35008409	1	62	theme	post-translational	154:171	arg1	O-GlcNAcylation					110:124	O-GlcNAcylation	110:124	O-GlcNAcylation	110:124	O-GlcNAcylation is a reversible and dynamic post-translational protein modification catalyzed by O-GlcNAc transferase (OGT).
35008409	1	62	theme	post-translational	154:171	arg1	modification					181:192	a reversible and dynamic post-translational protein modification	129:192	a reversible and dynamic post-translational protein modification catalyzed by O-GlcNAc transferase (OGT)	129:232	O-GlcNAcylation is a reversible and dynamic post-translational protein modification catalyzed by O-GlcNAc transferase (OGT).
35008409	7	63	theme	overall	1271:1277	arg1	survival					1279:1286	poorer overall survival	1264:1286	poorer overall survival	1264:1286	Analysis of clinical specimens found that high SAM68 expression was associated with late cancer stages, and patients with high-OGT/high-SAM68 expression in their tumors had poorer overall survival compared to those with low-OGT/low-SAM68 expression.
20305658	5	0	theme	inhibition	830:839	arg1	ELISAs					841:846	inhibition ELISAs	830:846	inhibition ELISAs	830:846	This observation, combined with the results of inhibition ELISAs, suggests that the antibodies, in addition to their O-GlcNAc dependence, also appear to have different but overlapping local peptide determinants.
20305658	4	1	gly	glycoproteins	724:736	arg1	glycoproteins					724:736	the glycoproteins	720:736	the glycoproteins	720:736	A substantial number of the glycoproteins were enriched by only one of the antibodies.
20305658	5	2	contain	have	936:939	arg2	determinants					981:992	different but overlapping local peptide determinants	941:992	different but overlapping local peptide determinants	941:992	This observation, combined with the results of inhibition ELISAs, suggests that the antibodies, in addition to their O-GlcNAc dependence, also appear to have different but overlapping local peptide determinants.
20305658	5	2	contain	have	936:939	arg1	antibodies					867:876	the antibodies	863:876	the antibodies	863:876	This observation, combined with the results of inhibition ELISAs, suggests that the antibodies, in addition to their O-GlcNAc dependence, also appear to have different but overlapping local peptide determinants.
20305658	2	3	theme	partners	418:425	arg1	spectrum					398:405	a broad spectrum	390:405	a broad spectrum of binding partners	390:425	We have obtained a large panel of O-GlcNAc-specific IgG monoclonal antibodies having a broad spectrum of binding partners by combining three-component immunogen methodology with hybridoma technology.
20305658	2	4	theme	antibodies	372:381	arg1	panel					330:334	a large panel	322:334	a large panel of O-GlcNAc-specific IgG monoclonal antibodies having a broad spectrum of binding partners	322:425	We have obtained a large panel of O-GlcNAc-specific IgG monoclonal antibodies having a broad spectrum of binding partners by combining three-component immunogen methodology with hybridoma technology.
20305658	6	5	from	trauma-hemorrhage	1108:1124	arg1	model					1153:1157	a rat model	1147:1157	a rat model	1147:1157	The monoclonal antibodies made it possible to delineate differentially modified proteins of liver in response to trauma-hemorrhage and resuscitation in a rat model.
20305658	6	6	theme	modified	1066:1073	arg1	proteins					1075:1082	differentially modified proteins	1051:1082	differentially modified proteins of liver	1051:1091	The monoclonal antibodies made it possible to delineate differentially modified proteins of liver in response to trauma-hemorrhage and resuscitation in a rat model.
20305658	6	7	dep	trauma-hemorrhage	1108:1124	arg1	response					1096:1103	response	1096:1103	response	1096:1103	The monoclonal antibodies made it possible to delineate differentially modified proteins of liver in response to trauma-hemorrhage and resuscitation in a rat model.
20305658	3	8	theme	mammalian	611:619	arg1	number					667:672	a large number	659:672	a large number of new glycoproteins	659:693	Immunoprecipitation followed by large-scale shotgun proteomics led to the identification of more than 200 mammalian O-GlcNAc-modified proteins, including a large number of new glycoproteins.
20305658	3	8	theme	mammalian	611:619	arg1	proteins					639:646	more than 200 mammalian O-GlcNAc-modified proteins	597:646	more than 200 mammalian O-GlcNAc-modified proteins	597:646	Immunoprecipitation followed by large-scale shotgun proteomics led to the identification of more than 200 mammalian O-GlcNAc-modified proteins, including a large number of new glycoproteins.
20305658	1	9	theme	site	286:289	arg1	localization					291:302	site localization	286:302	site localization	286:302	Studies of post-translational modification by beta-N-acetyl-D-glucosamine (O-GlcNAc) are hampered by a lack of efficient tools such as O-GlcNAc-specific antibodies that can be used for detection, isolation and site localization.
20305658	2	10	contain	having	383:388	arg2	spectrum					398:405	a broad spectrum	390:405	a broad spectrum of binding partners	390:425	We have obtained a large panel of O-GlcNAc-specific IgG monoclonal antibodies having a broad spectrum of binding partners by combining three-component immunogen methodology with hybridoma technology.
20305658	2	10	contain	having	383:388	arg1	antibodies					372:381	O-GlcNAc-specific IgG monoclonal antibodies	339:381	O-GlcNAc-specific IgG monoclonal antibodies having a broad spectrum of binding partners	339:425	We have obtained a large panel of O-GlcNAc-specific IgG monoclonal antibodies having a broad spectrum of binding partners by combining three-component immunogen methodology with hybridoma technology.
20305658	4	11	theme	substantial	698:708	arg1	number					710:715	A substantial number	696:715	A substantial number of the glycoproteins	696:736	A substantial number of the glycoproteins were enriched by only one of the antibodies.
20305658	6	12	theme	rat	1149:1151	arg1	model					1153:1157	a rat model	1147:1157	a rat model	1147:1157	The monoclonal antibodies made it possible to delineate differentially modified proteins of liver in response to trauma-hemorrhage and resuscitation in a rat model.
20305658	1	13	theme	efficient	187:195	arg1	antibodies					229:238	O-GlcNAc-specific antibodies	211:238	O-GlcNAc-specific antibodies that can be used for detection, isolation and site localization	211:302	Studies of post-translational modification by beta-N-acetyl-D-glucosamine (O-GlcNAc) are hampered by a lack of efficient tools such as O-GlcNAc-specific antibodies that can be used for detection, isolation and site localization.
20305658	1	13	theme	efficient	187:195	arg1	tools					197:201	efficient tools	187:201	efficient tools such as O-GlcNAc-specific antibodies that can be used for detection, isolation and site localization	187:302	Studies of post-translational modification by beta-N-acetyl-D-glucosamine (O-GlcNAc) are hampered by a lack of efficient tools such as O-GlcNAc-specific antibodies that can be used for detection, isolation and site localization.
20305658	5	14	theme	overlapping	955:965	arg1	determinants					981:992	different but overlapping local peptide determinants	941:992	different but overlapping local peptide determinants	941:992	This observation, combined with the results of inhibition ELISAs, suggests that the antibodies, in addition to their O-GlcNAc dependence, also appear to have different but overlapping local peptide determinants.
20305658	1	15	theme	post-translational	87:104	arg1	modification					106:117	post-translational modification	87:117	post-translational modification by beta-N-acetyl-D-glucosamine (O-GlcNAc)	87:159	Studies of post-translational modification by beta-N-acetyl-D-glucosamine (O-GlcNAc) are hampered by a lack of efficient tools such as O-GlcNAc-specific antibodies that can be used for detection, isolation and site localization.
20305658	1	16	theme	tools	197:201	arg1	lack					179:182	a lack	177:182	a lack of efficient tools such as O-GlcNAc-specific antibodies that can be used for detection, isolation and site localization	177:302	Studies of post-translational modification by beta-N-acetyl-D-glucosamine (O-GlcNAc) are hampered by a lack of efficient tools such as O-GlcNAc-specific antibodies that can be used for detection, isolation and site localization.
20305658	0	17	theme	monoclonal	22:31	arg1	antibodies					33:42	Glycopeptide-specific monoclonal antibodies	0:42	Glycopeptide-specific monoclonal antibodies	0:42	Glycopeptide-specific monoclonal antibodies suggest new roles for O-GlcNAc.
20305658	5	18	theme	ELISAs	841:846	arg1	results					819:825	the results	815:825	the results of inhibition ELISAs	815:846	This observation, combined with the results of inhibition ELISAs, suggests that the antibodies, in addition to their O-GlcNAc dependence, also appear to have different but overlapping local peptide determinants.
20305658	4	19	theme	glycoproteins	724:736	arg1	number					710:715	A substantial number	696:715	A substantial number of the glycoproteins	696:736	A substantial number of the glycoproteins were enriched by only one of the antibodies.
20305658	1	20	theme	modification	106:117	arg1	Studies					76:82	Studies	76:82	Studies of post-translational modification by beta-N-acetyl-D-glucosamine (O-GlcNAc)	76:159	Studies of post-translational modification by beta-N-acetyl-D-glucosamine (O-GlcNAc) are hampered by a lack of efficient tools such as O-GlcNAc-specific antibodies that can be used for detection, isolation and site localization.
20305658	3	21	gly	glycoproteins	681:693	arg1	glycoproteins					681:693	new glycoproteins	677:693	new glycoproteins	677:693	Immunoprecipitation followed by large-scale shotgun proteomics led to the identification of more than 200 mammalian O-GlcNAc-modified proteins, including a large number of new glycoproteins.
20305658	0	22	theme	Glycopeptide-specific	0:20	arg1	antibodies					33:42	Glycopeptide-specific monoclonal antibodies	0:42	Glycopeptide-specific monoclonal antibodies	0:42	Glycopeptide-specific monoclonal antibodies suggest new roles for O-GlcNAc.
20305658	2	23	theme	large	324:328	arg1	panel					330:334	a large panel	322:334	a large panel of O-GlcNAc-specific IgG monoclonal antibodies having a broad spectrum of binding partners	322:425	We have obtained a large panel of O-GlcNAc-specific IgG monoclonal antibodies having a broad spectrum of binding partners by combining three-component immunogen methodology with hybridoma technology.
20305658	5	24	theme	local	967:971	arg1	determinants					981:992	different but overlapping local peptide determinants	941:992	different but overlapping local peptide determinants	941:992	This observation, combined with the results of inhibition ELISAs, suggests that the antibodies, in addition to their O-GlcNAc dependence, also appear to have different but overlapping local peptide determinants.
20305658	3	25	theme	O-GlcNAc-modified	621:637	arg1	number					667:672	a large number	659:672	a large number of new glycoproteins	659:693	Immunoprecipitation followed by large-scale shotgun proteomics led to the identification of more than 200 mammalian O-GlcNAc-modified proteins, including a large number of new glycoproteins.
20305658	3	25	theme	O-GlcNAc-modified	621:637	arg1	proteins					639:646	more than 200 mammalian O-GlcNAc-modified proteins	597:646	more than 200 mammalian O-GlcNAc-modified proteins	597:646	Immunoprecipitation followed by large-scale shotgun proteomics led to the identification of more than 200 mammalian O-GlcNAc-modified proteins, including a large number of new glycoproteins.
20305658	2	26	theme	immunogen	456:464	arg1	methodology					466:476	three-component immunogen methodology	440:476	three-component immunogen methodology	440:476	We have obtained a large panel of O-GlcNAc-specific IgG monoclonal antibodies having a broad spectrum of binding partners by combining three-component immunogen methodology with hybridoma technology.
20305658	2	27	theme	hybridoma	483:491	arg1	technology					493:502	hybridoma technology	483:502	hybridoma technology	483:502	We have obtained a large panel of O-GlcNAc-specific IgG monoclonal antibodies having a broad spectrum of binding partners by combining three-component immunogen methodology with hybridoma technology.
20305658	3	28	theme	proteins	639:646	arg1	identification					579:592	the identification	575:592	the identification of more than 200 mammalian O-GlcNAc-modified proteins, including a large number of new glycoproteins	575:693	Immunoprecipitation followed by large-scale shotgun proteomics led to the identification of more than 200 mammalian O-GlcNAc-modified proteins, including a large number of new glycoproteins.
20305658	2	29	theme	three-component	440:454	arg1	methodology					466:476	three-component immunogen methodology	440:476	three-component immunogen methodology	440:476	We have obtained a large panel of O-GlcNAc-specific IgG monoclonal antibodies having a broad spectrum of binding partners by combining three-component immunogen methodology with hybridoma technology.
20305658	4	30	theme	antibodies	771:780	arg1	one					760:762	one	760:762	one	760:762	A substantial number of the glycoproteins were enriched by only one of the antibodies.
20305658	4	30	theme	antibodies	771:780	arg1	antibodies					771:780	the antibodies	767:780	the antibodies	767:780	A substantial number of the glycoproteins were enriched by only one of the antibodies.
20305658	5	31	theme	O-GlcNAc	900:907	arg1	dependence					909:918	their O-GlcNAc dependence	894:918	their O-GlcNAc dependence	894:918	This observation, combined with the results of inhibition ELISAs, suggests that the antibodies, in addition to their O-GlcNAc dependence, also appear to have different but overlapping local peptide determinants.
20305658	0	32	theme	new	52:54	arg1	roles					56:60	new roles	52:60	new roles for O-GlcNAc	52:73	Glycopeptide-specific monoclonal antibodies suggest new roles for O-GlcNAc.
20305658	5	33	theme	peptide	973:979	arg1	determinants					981:992	different but overlapping local peptide determinants	941:992	different but overlapping local peptide determinants	941:992	This observation, combined with the results of inhibition ELISAs, suggests that the antibodies, in addition to their O-GlcNAc dependence, also appear to have different but overlapping local peptide determinants.
20305658	2	34	theme	monoclonal	361:370	arg1	antibodies					372:381	O-GlcNAc-specific IgG monoclonal antibodies	339:381	O-GlcNAc-specific IgG monoclonal antibodies having a broad spectrum of binding partners	339:425	We have obtained a large panel of O-GlcNAc-specific IgG monoclonal antibodies having a broad spectrum of binding partners by combining three-component immunogen methodology with hybridoma technology.
20305658	6	35	theme	monoclonal	999:1008	arg1	antibodies					1010:1019	The monoclonal antibodies	995:1019	The monoclonal antibodies	995:1019	The monoclonal antibodies made it possible to delineate differentially modified proteins of liver in response to trauma-hemorrhage and resuscitation in a rat model.
20305658	3	36	theme	large	661:665	arg1	number					667:672	a large number	659:672	a large number of new glycoproteins	659:693	Immunoprecipitation followed by large-scale shotgun proteomics led to the identification of more than 200 mammalian O-GlcNAc-modified proteins, including a large number of new glycoproteins.
20305658	2	37	theme	IgG	357:359	arg1	antibodies					372:381	O-GlcNAc-specific IgG monoclonal antibodies	339:381	O-GlcNAc-specific IgG monoclonal antibodies having a broad spectrum of binding partners	339:425	We have obtained a large panel of O-GlcNAc-specific IgG monoclonal antibodies having a broad spectrum of binding partners by combining three-component immunogen methodology with hybridoma technology.
20305658	6	38	from	resuscitation	1130:1142	arg1	model					1153:1157	a rat model	1147:1157	a rat model	1147:1157	The monoclonal antibodies made it possible to delineate differentially modified proteins of liver in response to trauma-hemorrhage and resuscitation in a rat model.
20305658	2	39	theme	O-GlcNAc-specific	339:355	arg1	antibodies					372:381	O-GlcNAc-specific IgG monoclonal antibodies	339:381	O-GlcNAc-specific IgG monoclonal antibodies having a broad spectrum of binding partners	339:425	We have obtained a large panel of O-GlcNAc-specific IgG monoclonal antibodies having a broad spectrum of binding partners by combining three-component immunogen methodology with hybridoma technology.
20305658	1	40	used	used	252:255	arg2	antibodies					229:238	O-GlcNAc-specific antibodies	211:238	O-GlcNAc-specific antibodies that can be used for detection, isolation and site localization	211:302	Studies of post-translational modification by beta-N-acetyl-D-glucosamine (O-GlcNAc) are hampered by a lack of efficient tools such as O-GlcNAc-specific antibodies that can be used for detection, isolation and site localization.
20305658	5	41	dep	dependence	909:918	arg1	addition					882:889	addition	882:889	addition	882:889	This observation, combined with the results of inhibition ELISAs, suggests that the antibodies, in addition to their O-GlcNAc dependence, also appear to have different but overlapping local peptide determinants.
20305658	3	42	theme	shotgun	549:555	arg1	proteomics					557:566	large-scale shotgun proteomics	537:566	large-scale shotgun proteomics	537:566	Immunoprecipitation followed by large-scale shotgun proteomics led to the identification of more than 200 mammalian O-GlcNAc-modified proteins, including a large number of new glycoproteins.
20305658	3	43	theme	large-scale	537:547	arg1	proteomics					557:566	large-scale shotgun proteomics	537:566	large-scale shotgun proteomics	537:566	Immunoprecipitation followed by large-scale shotgun proteomics led to the identification of more than 200 mammalian O-GlcNAc-modified proteins, including a large number of new glycoproteins.
20305658	3	44	theme	new	677:679	arg1	glycoproteins					681:693	new glycoproteins	677:693	new glycoproteins	677:693	Immunoprecipitation followed by large-scale shotgun proteomics led to the identification of more than 200 mammalian O-GlcNAc-modified proteins, including a large number of new glycoproteins.
20305658	1	45	theme	O-GlcNAc-specific	211:227	arg1	antibodies					229:238	O-GlcNAc-specific antibodies	211:238	O-GlcNAc-specific antibodies that can be used for detection, isolation and site localization	211:302	Studies of post-translational modification by beta-N-acetyl-D-glucosamine (O-GlcNAc) are hampered by a lack of efficient tools such as O-GlcNAc-specific antibodies that can be used for detection, isolation and site localization.
20305658	2	46	theme	broad	392:396	arg1	spectrum					398:405	a broad spectrum	390:405	a broad spectrum of binding partners	390:425	We have obtained a large panel of O-GlcNAc-specific IgG monoclonal antibodies having a broad spectrum of binding partners by combining three-component immunogen methodology with hybridoma technology.
20305658	2	47	theme	binding	410:416	arg1	partners					418:425	binding partners	410:425	binding partners	410:425	We have obtained a large panel of O-GlcNAc-specific IgG monoclonal antibodies having a broad spectrum of binding partners by combining three-component immunogen methodology with hybridoma technology.
20305658	3	48	theme	glycoproteins	681:693	arg1	number					667:672	a large number	659:672	a large number of new glycoproteins	659:693	Immunoprecipitation followed by large-scale shotgun proteomics led to the identification of more than 200 mammalian O-GlcNAc-modified proteins, including a large number of new glycoproteins.
20305658	5	49	theme	different	941:949	arg1	determinants					981:992	different but overlapping local peptide determinants	941:992	different but overlapping local peptide determinants	941:992	This observation, combined with the results of inhibition ELISAs, suggests that the antibodies, in addition to their O-GlcNAc dependence, also appear to have different but overlapping local peptide determinants.
20305658	6	50	theme	liver	1087:1091	arg1	proteins					1075:1082	differentially modified proteins	1051:1082	differentially modified proteins of liver	1051:1091	The monoclonal antibodies made it possible to delineate differentially modified proteins of liver in response to trauma-hemorrhage and resuscitation in a rat model.
30397120	8	0	theme	nuclear	1445:1451	arg1	processes					1468:1476	cytoplasmic and nuclear OGT-controlled processes	1429:1476	cytoplasmic and nuclear OGT-controlled processes that integrate at the hepatic SREBF1 locus to control basal and insulin-induced expression of the temporally and nutritionally regulated lipogenic SREBP-1c transcript	1429:1643	Conclusion: REV-ERBα regulates cytoplasmic and nuclear OGT-controlled processes that integrate at the hepatic SREBF1 locus to control basal and insulin-induced expression of the temporally and nutritionally regulated lipogenic SREBP-1c transcript.
30397120	6	1	theme	REV-ERBα	1108:1115	arg1	sites					1133:1137	REV-ERBα genomic binding sites	1108:1137	REV-ERBα genomic binding sites	1108:1137	REV-ERBα enhanced TET activity and DNA hydroxymethylated cytosine (5hmC) levels in the vicinity of REV-ERBα genomic binding sites.
30397120	1	2	with	clock	177:181	arg1	glucose					196:202	hepatic glucose and lipid metabolism	188:223	glucose	196:202	The nuclear receptor REV-ERBα integrates the circadian clock with hepatic glucose and lipid metabolism by nucleating transcriptional comodulators at genomic regulatory regions.
30397120	1	2	with	clock	177:181	arg1	metabolism					214:223	hepatic glucose and lipid metabolism	188:223	metabolism	214:223	The nuclear receptor REV-ERBα integrates the circadian clock with hepatic glucose and lipid metabolism by nucleating transcriptional comodulators at genomic regulatory regions.
30397120	3	3	theme	proteins	579:586	arg1	O-GlcNAcylation					527:541	O-GlcNAcylation	527:541	O-GlcNAcylation of multiple cytoplasmic and nuclear proteins	527:586	By shielding cytoplasmic OGT from proteasomal degradation and favoring OGT activity in the nucleus, REV-ERBα cyclically increased O-GlcNAcylation of multiple cytoplasmic and nuclear proteins as a function of its rhythmically regulated expression, while REV-ERBα ligands mostly affected cytoplasmic OGT activity.
30397120	3	3	theme	proteins	579:586	arg1	function					593:600	a function	591:600	a function of its rhythmically regulated expression	591:641	By shielding cytoplasmic OGT from proteasomal degradation and favoring OGT activity in the nucleus, REV-ERBα cyclically increased O-GlcNAcylation of multiple cytoplasmic and nuclear proteins as a function of its rhythmically regulated expression, while REV-ERBα ligands mostly affected cytoplasmic OGT activity.
30397120	8	4	theme	cytoplasmic	1429:1439	arg1	processes					1468:1476	cytoplasmic and nuclear OGT-controlled processes	1429:1476	cytoplasmic and nuclear OGT-controlled processes that integrate at the hepatic SREBF1 locus to control basal and insulin-induced expression of the temporally and nutritionally regulated lipogenic SREBP-1c transcript	1429:1643	Conclusion: REV-ERBα regulates cytoplasmic and nuclear OGT-controlled processes that integrate at the hepatic SREBF1 locus to control basal and insulin-induced expression of the temporally and nutritionally regulated lipogenic SREBP-1c transcript.
30397120	3	5	from	activity	472:479	arg1	nucleus					488:494	the nucleus	484:494	the nucleus	484:494	By shielding cytoplasmic OGT from proteasomal degradation and favoring OGT activity in the nucleus, REV-ERBα cyclically increased O-GlcNAcylation of multiple cytoplasmic and nuclear proteins as a function of its rhythmically regulated expression, while REV-ERBα ligands mostly affected cytoplasmic OGT activity.
30397120	5	6	theme	REV-ERBα	988:995	arg1	expression					997:1006	REV-ERBα expression	988:1006	REV-ERBα expression	988:1006	AKT phosphorylation was inversely correlated to REV-ERBα expression.
30397120	7	7	theme	SREBP-1c	1203:1210	arg1	expression					1217:1226	SREBP-1c gene expression	1203:1226	SREBP-1c gene expression	1203:1226	As an example, we show that the REV-ERBα/OGT complex modulates SREBP-1c gene expression throughout the fasting/feeding periods by first repressing AKT phosphorylation and by epigenomically priming the Srebf1 promoter for a further rapid response to insulin.
30397120	4	8	from	activities	784:793	arg1	nucleus					931:937	the nucleus	927:937	the nucleus	927:937	We illustrate this finding by showing that REV-ERBα controls OGT-dependent activities of the cytoplasmic protein kinase AKT, an essential relay in insulin signaling, and of ten-of-eleven translocation (TET) enzymes in the nucleus.
30397120	7	9	theme	gene	1212:1215	arg1	expression					1217:1226	SREBP-1c gene expression	1203:1226	SREBP-1c gene expression	1203:1226	As an example, we show that the REV-ERBα/OGT complex modulates SREBP-1c gene expression throughout the fasting/feeding periods by first repressing AKT phosphorylation and by epigenomically priming the Srebf1 promoter for a further rapid response to insulin.
30397120	3	10	theme	cytoplasmic	410:420	arg1	OGT					422:424	cytoplasmic OGT	410:424	cytoplasmic OGT from proteasomal degradation	410:453	By shielding cytoplasmic OGT from proteasomal degradation and favoring OGT activity in the nucleus, REV-ERBα cyclically increased O-GlcNAcylation of multiple cytoplasmic and nuclear proteins as a function of its rhythmically regulated expression, while REV-ERBα ligands mostly affected cytoplasmic OGT activity.
30397120	8	11	theme	insulin-induced	1542:1556	arg1	expression					1558:1567	basal and insulin-induced expression	1532:1567	basal and insulin-induced expression of the temporally and nutritionally regulated lipogenic SREBP-1c transcript	1532:1643	Conclusion: REV-ERBα regulates cytoplasmic and nuclear OGT-controlled processes that integrate at the hepatic SREBF1 locus to control basal and insulin-induced expression of the temporally and nutritionally regulated lipogenic SREBP-1c transcript.
30397120	4	12	theme	insulin	856:862	arg1	signaling					864:872	insulin signaling	856:872	insulin signaling	856:872	We illustrate this finding by showing that REV-ERBα controls OGT-dependent activities of the cytoplasmic protein kinase AKT, an essential relay in insulin signaling, and of ten-of-eleven translocation (TET) enzymes in the nucleus.
30397120	8	13	theme	SREBF1	1508:1513	arg1	locus					1515:1519	the hepatic SREBF1 locus	1496:1519	the hepatic SREBF1 locus	1496:1519	Conclusion: REV-ERBα regulates cytoplasmic and nuclear OGT-controlled processes that integrate at the hepatic SREBF1 locus to control basal and insulin-induced expression of the temporally and nutritionally regulated lipogenic SREBP-1c transcript.
30397120	0	14	theme	OGT/REV-ERBα	100:111	arg1	complex					113:119	the OGT/REV-ERBα complex	96:119	the OGT/REV-ERBα complex	96:119	Combinatorial regulation of hepatic cytoplasmic signaling and nuclear transcriptional events by the OGT/REV-ERBα complex.
30397120	3	15	theme	regulated	622:630	arg1	expression					632:641	its rhythmically regulated expression	605:641	its rhythmically regulated expression	605:641	By shielding cytoplasmic OGT from proteasomal degradation and favoring OGT activity in the nucleus, REV-ERBα cyclically increased O-GlcNAcylation of multiple cytoplasmic and nuclear proteins as a function of its rhythmically regulated expression, while REV-ERBα ligands mostly affected cytoplasmic OGT activity.
30397120	2	16	theme	O-GlcNAc	335:342	arg1	protein					388:394	a REV-ERBα-interacting protein	365:394	a REV-ERBα-interacting protein	365:394	An interactomic approach identified O-GlcNAc transferase (OGT) as a REV-ERBα-interacting protein.
30397120	2	16	theme	O-GlcNAc	335:342	arg1	OGT					357:359	OGT	357:359	OGT	357:359	An interactomic approach identified O-GlcNAc transferase (OGT) as a REV-ERBα-interacting protein.
30397120	2	16	theme	O-GlcNAc	335:342	arg1	transferase					344:354	O-GlcNAc transferase	335:354	O-GlcNAc transferase (OGT)	335:360	An interactomic approach identified O-GlcNAc transferase (OGT) as a REV-ERBα-interacting protein.
30397120	4	17	theme	kinase	822:827	arg1	relay					847:851	an essential relay	834:851	an essential relay in insulin signaling	834:872	We illustrate this finding by showing that REV-ERBα controls OGT-dependent activities of the cytoplasmic protein kinase AKT, an essential relay in insulin signaling, and of ten-of-eleven translocation (TET) enzymes in the nucleus.
30397120	4	17	theme	kinase	822:827	arg1	AKT					829:831	the cytoplasmic protein kinase AKT	798:831	the cytoplasmic protein kinase AKT	798:831	We illustrate this finding by showing that REV-ERBα controls OGT-dependent activities of the cytoplasmic protein kinase AKT, an essential relay in insulin signaling, and of ten-of-eleven translocation (TET) enzymes in the nucleus.
30397120	4	18	theme	protein	814:820	arg1	relay					847:851	an essential relay	834:851	an essential relay in insulin signaling	834:872	We illustrate this finding by showing that REV-ERBα controls OGT-dependent activities of the cytoplasmic protein kinase AKT, an essential relay in insulin signaling, and of ten-of-eleven translocation (TET) enzymes in the nucleus.
30397120	4	18	theme	protein	814:820	arg1	AKT					829:831	the cytoplasmic protein kinase AKT	798:831	the cytoplasmic protein kinase AKT	798:831	We illustrate this finding by showing that REV-ERBα controls OGT-dependent activities of the cytoplasmic protein kinase AKT, an essential relay in insulin signaling, and of ten-of-eleven translocation (TET) enzymes in the nucleus.
30397120	7	19	theme	REV-ERBα/OGT	1172:1183	arg1	complex					1185:1191	the REV-ERBα/OGT complex	1168:1191	the REV-ERBα/OGT complex	1168:1191	As an example, we show that the REV-ERBα/OGT complex modulates SREBP-1c gene expression throughout the fasting/feeding periods by first repressing AKT phosphorylation and by epigenomically priming the Srebf1 promoter for a further rapid response to insulin.
30397120	8	20	theme	regulated	1605:1613	arg1	transcript					1634:1643	the temporally and nutritionally regulated lipogenic SREBP-1c transcript	1572:1643	the temporally and nutritionally regulated lipogenic SREBP-1c transcript	1572:1643	Conclusion: REV-ERBα regulates cytoplasmic and nuclear OGT-controlled processes that integrate at the hepatic SREBF1 locus to control basal and insulin-induced expression of the temporally and nutritionally regulated lipogenic SREBP-1c transcript.
30397120	1	21	theme	hepatic	188:194	arg1	glucose					196:202	hepatic glucose and lipid metabolism	188:223	glucose	196:202	The nuclear receptor REV-ERBα integrates the circadian clock with hepatic glucose and lipid metabolism by nucleating transcriptional comodulators at genomic regulatory regions.
30397120	3	22	from	degradation	443:453	arg1	OGT					422:424	cytoplasmic OGT	410:424	cytoplasmic OGT from proteasomal degradation	410:453	By shielding cytoplasmic OGT from proteasomal degradation and favoring OGT activity in the nucleus, REV-ERBα cyclically increased O-GlcNAcylation of multiple cytoplasmic and nuclear proteins as a function of its rhythmically regulated expression, while REV-ERBα ligands mostly affected cytoplasmic OGT activity.
30397120	7	23	theme	fasting/feeding	1243:1257	arg1	periods					1259:1265	the fasting/feeding periods	1239:1265	the fasting/feeding periods	1239:1265	As an example, we show that the REV-ERBα/OGT complex modulates SREBP-1c gene expression throughout the fasting/feeding periods by first repressing AKT phosphorylation and by epigenomically priming the Srebf1 promoter for a further rapid response to insulin.
30397120	4	24	from	relay	847:851	arg1	signaling					864:872	insulin signaling	856:872	insulin signaling	856:872	We illustrate this finding by showing that REV-ERBα controls OGT-dependent activities of the cytoplasmic protein kinase AKT, an essential relay in insulin signaling, and of ten-of-eleven translocation (TET) enzymes in the nucleus.
30397120	6	25	theme	genomic	1117:1123	arg1	sites					1133:1137	REV-ERBα genomic binding sites	1108:1137	REV-ERBα genomic binding sites	1108:1137	REV-ERBα enhanced TET activity and DNA hydroxymethylated cytosine (5hmC) levels in the vicinity of REV-ERBα genomic binding sites.
30397120	7	26	dep	modulates	1193:1201	arg1	repressing					1276:1285	repressing	1276:1285	first repressing AKT phosphorylation	1270:1305	As an example, we show that the REV-ERBα/OGT complex modulates SREBP-1c gene expression throughout the fasting/feeding periods by first repressing AKT phosphorylation and by epigenomically priming the Srebf1 promoter for a further rapid response to insulin.
30397120	7	26	dep	modulates	1193:1201	arg1	priming					1329:1335	priming	1329:1335	priming the Srebf1 promoter for a further rapid response to insulin	1329:1395	As an example, we show that the REV-ERBα/OGT complex modulates SREBP-1c gene expression throughout the fasting/feeding periods by first repressing AKT phosphorylation and by epigenomically priming the Srebf1 promoter for a further rapid response to insulin.
30397120	6	27	theme	cytosine	1066:1073	arg1	levels					1082:1087	DNA hydroxymethylated cytosine (5hmC) levels	1044:1087	DNA hydroxymethylated cytosine (5hmC) levels	1044:1087	REV-ERBα enhanced TET activity and DNA hydroxymethylated cytosine (5hmC) levels in the vicinity of REV-ERBα genomic binding sites.
30397120	7	28	theme	Srebf1	1341:1346	arg1	promoter					1348:1355	the Srebf1 promoter	1337:1355	the Srebf1 promoter	1337:1355	As an example, we show that the REV-ERBα/OGT complex modulates SREBP-1c gene expression throughout the fasting/feeding periods by first repressing AKT phosphorylation and by epigenomically priming the Srebf1 promoter for a further rapid response to insulin.
30397120	8	29	theme	hepatic	1500:1506	arg1	locus					1515:1519	the hepatic SREBF1 locus	1496:1519	the hepatic SREBF1 locus	1496:1519	Conclusion: REV-ERBα regulates cytoplasmic and nuclear OGT-controlled processes that integrate at the hepatic SREBF1 locus to control basal and insulin-induced expression of the temporally and nutritionally regulated lipogenic SREBP-1c transcript.
30397120	4	30	from	nucleus	931:937	arg1	activities					784:793	OGT-dependent activities	770:793	OGT-dependent activities of the cytoplasmic protein kinase AKT, an essential relay in insulin signaling, and of ten-of-eleven translocation (TET) enzymes in the nucleus	770:937	We illustrate this finding by showing that REV-ERBα controls OGT-dependent activities of the cytoplasmic protein kinase AKT, an essential relay in insulin signaling, and of ten-of-eleven translocation (TET) enzymes in the nucleus.
30397120	0	31	theme	Combinatorial	0:12	arg1	regulation					14:23	Combinatorial regulation	0:23	Combinatorial regulation of hepatic cytoplasmic signaling and nuclear transcriptional events by the OGT/REV-ERBα complex.	0:120	Combinatorial regulation of hepatic cytoplasmic signaling and nuclear transcriptional events by the OGT/REV-ERBα complex.
30397120	8	32	theme	transcript	1634:1643	arg1	expression					1558:1567	basal and insulin-induced expression	1532:1567	basal and insulin-induced expression of the temporally and nutritionally regulated lipogenic SREBP-1c transcript	1532:1643	Conclusion: REV-ERBα regulates cytoplasmic and nuclear OGT-controlled processes that integrate at the hepatic SREBF1 locus to control basal and insulin-induced expression of the temporally and nutritionally regulated lipogenic SREBP-1c transcript.
30397120	5	33	theme	AKT	940:942	arg1	phosphorylation					944:958	AKT phosphorylation	940:958	AKT phosphorylation	940:958	AKT phosphorylation was inversely correlated to REV-ERBα expression.
30397120	3	34	theme	REV-ERBα	650:657	arg1	ligands					659:665	REV-ERBα ligands	650:665	REV-ERBα ligands	650:665	By shielding cytoplasmic OGT from proteasomal degradation and favoring OGT activity in the nucleus, REV-ERBα cyclically increased O-GlcNAcylation of multiple cytoplasmic and nuclear proteins as a function of its rhythmically regulated expression, while REV-ERBα ligands mostly affected cytoplasmic OGT activity.
30397120	1	35	theme	lipid	208:212	arg1	metabolism					214:223	hepatic glucose and lipid metabolism	188:223	metabolism	214:223	The nuclear receptor REV-ERBα integrates the circadian clock with hepatic glucose and lipid metabolism by nucleating transcriptional comodulators at genomic regulatory regions.
30397120	0	36	theme	hepatic	28:34	arg1	signaling					48:56	hepatic cytoplasmic signaling	28:56	hepatic cytoplasmic signaling	28:56	Combinatorial regulation of hepatic cytoplasmic signaling and nuclear transcriptional events by the OGT/REV-ERBα complex.
30397120	4	37	theme	translocation	896:908	arg1	enzymes					916:922	ten-of-eleven translocation (TET) enzymes	882:922	ten-of-eleven translocation (TET) enzymes in the nucleus	882:937	We illustrate this finding by showing that REV-ERBα controls OGT-dependent activities of the cytoplasmic protein kinase AKT, an essential relay in insulin signaling, and of ten-of-eleven translocation (TET) enzymes in the nucleus.
30397120	3	38	theme	expression	632:641	arg1	O-GlcNAcylation					527:541	O-GlcNAcylation	527:541	O-GlcNAcylation of multiple cytoplasmic and nuclear proteins	527:586	By shielding cytoplasmic OGT from proteasomal degradation and favoring OGT activity in the nucleus, REV-ERBα cyclically increased O-GlcNAcylation of multiple cytoplasmic and nuclear proteins as a function of its rhythmically regulated expression, while REV-ERBα ligands mostly affected cytoplasmic OGT activity.
30397120	3	38	theme	expression	632:641	arg1	function					593:600	a function	591:600	a function of its rhythmically regulated expression	591:641	By shielding cytoplasmic OGT from proteasomal degradation and favoring OGT activity in the nucleus, REV-ERBα cyclically increased O-GlcNAcylation of multiple cytoplasmic and nuclear proteins as a function of its rhythmically regulated expression, while REV-ERBα ligands mostly affected cytoplasmic OGT activity.
30397120	3	39	theme	proteasomal	431:441	arg1	degradation					443:453	proteasomal degradation	431:453	proteasomal degradation	431:453	By shielding cytoplasmic OGT from proteasomal degradation and favoring OGT activity in the nucleus, REV-ERBα cyclically increased O-GlcNAcylation of multiple cytoplasmic and nuclear proteins as a function of its rhythmically regulated expression, while REV-ERBα ligands mostly affected cytoplasmic OGT activity.
30397120	4	40	theme	essential	837:845	arg1	relay					847:851	an essential relay	834:851	an essential relay in insulin signaling	834:872	We illustrate this finding by showing that REV-ERBα controls OGT-dependent activities of the cytoplasmic protein kinase AKT, an essential relay in insulin signaling, and of ten-of-eleven translocation (TET) enzymes in the nucleus.
30397120	4	40	theme	essential	837:845	arg1	AKT					829:831	the cytoplasmic protein kinase AKT	798:831	the cytoplasmic protein kinase AKT	798:831	We illustrate this finding by showing that REV-ERBα controls OGT-dependent activities of the cytoplasmic protein kinase AKT, an essential relay in insulin signaling, and of ten-of-eleven translocation (TET) enzymes in the nucleus.
30397120	0	41	theme	signaling	48:56	arg1	regulation					14:23	Combinatorial regulation	0:23	Combinatorial regulation of hepatic cytoplasmic signaling and nuclear transcriptional events by the OGT/REV-ERBα complex.	0:120	Combinatorial regulation of hepatic cytoplasmic signaling and nuclear transcriptional events by the OGT/REV-ERBα complex.
30397120	3	42	theme	nuclear	571:577	arg1	proteins					579:586	multiple cytoplasmic and nuclear proteins	546:586	multiple cytoplasmic and nuclear proteins	546:586	By shielding cytoplasmic OGT from proteasomal degradation and favoring OGT activity in the nucleus, REV-ERBα cyclically increased O-GlcNAcylation of multiple cytoplasmic and nuclear proteins as a function of its rhythmically regulated expression, while REV-ERBα ligands mostly affected cytoplasmic OGT activity.
30397120	7	43	theme	AKT	1287:1289	arg1	phosphorylation					1291:1305	AKT phosphorylation	1287:1305	AKT phosphorylation	1287:1305	As an example, we show that the REV-ERBα/OGT complex modulates SREBP-1c gene expression throughout the fasting/feeding periods by first repressing AKT phosphorylation and by epigenomically priming the Srebf1 promoter for a further rapid response to insulin.
30397120	0	44	theme	cytoplasmic	36:46	arg1	signaling					48:56	hepatic cytoplasmic signaling	28:56	hepatic cytoplasmic signaling	28:56	Combinatorial regulation of hepatic cytoplasmic signaling and nuclear transcriptional events by the OGT/REV-ERBα complex.
30397120	6	45	theme	hydroxymethylated	1048:1064	arg1	levels					1082:1087	DNA hydroxymethylated cytosine (5hmC) levels	1044:1087	DNA hydroxymethylated cytosine (5hmC) levels	1044:1087	REV-ERBα enhanced TET activity and DNA hydroxymethylated cytosine (5hmC) levels in the vicinity of REV-ERBα genomic binding sites.
30397120	4	46	theme	cytoplasmic	802:812	arg1	relay					847:851	an essential relay	834:851	an essential relay in insulin signaling	834:872	We illustrate this finding by showing that REV-ERBα controls OGT-dependent activities of the cytoplasmic protein kinase AKT, an essential relay in insulin signaling, and of ten-of-eleven translocation (TET) enzymes in the nucleus.
30397120	4	46	theme	cytoplasmic	802:812	arg1	AKT					829:831	the cytoplasmic protein kinase AKT	798:831	the cytoplasmic protein kinase AKT	798:831	We illustrate this finding by showing that REV-ERBα controls OGT-dependent activities of the cytoplasmic protein kinase AKT, an essential relay in insulin signaling, and of ten-of-eleven translocation (TET) enzymes in the nucleus.
30397120	3	47	theme	cytoplasmic	683:693	arg1	activity					699:706	cytoplasmic OGT activity	683:706	cytoplasmic OGT activity	683:706	By shielding cytoplasmic OGT from proteasomal degradation and favoring OGT activity in the nucleus, REV-ERBα cyclically increased O-GlcNAcylation of multiple cytoplasmic and nuclear proteins as a function of its rhythmically regulated expression, while REV-ERBα ligands mostly affected cytoplasmic OGT activity.
30397120	4	48	from	enzymes	916:922	arg1	nucleus					931:937	the nucleus	927:937	the nucleus	927:937	We illustrate this finding by showing that REV-ERBα controls OGT-dependent activities of the cytoplasmic protein kinase AKT, an essential relay in insulin signaling, and of ten-of-eleven translocation (TET) enzymes in the nucleus.
30397120	1	49	theme	transcriptional	239:253	arg1	comodulators					255:266	transcriptional comodulators	239:266	transcriptional comodulators	239:266	The nuclear receptor REV-ERBα integrates the circadian clock with hepatic glucose and lipid metabolism by nucleating transcriptional comodulators at genomic regulatory regions.
30397120	0	50	theme	nuclear	62:68	arg1	events					86:91	nuclear transcriptional events	62:91	nuclear transcriptional events	62:91	Combinatorial regulation of hepatic cytoplasmic signaling and nuclear transcriptional events by the OGT/REV-ERBα complex.
30397120	6	51	theme	DNA	1044:1046	arg1	levels					1082:1087	DNA hydroxymethylated cytosine (5hmC) levels	1044:1087	DNA hydroxymethylated cytosine (5hmC) levels	1044:1087	REV-ERBα enhanced TET activity and DNA hydroxymethylated cytosine (5hmC) levels in the vicinity of REV-ERBα genomic binding sites.
30397120	6	52	theme	5hmC	1076:1079	arg1	levels					1082:1087	DNA hydroxymethylated cytosine (5hmC) levels	1044:1087	DNA hydroxymethylated cytosine (5hmC) levels	1044:1087	REV-ERBα enhanced TET activity and DNA hydroxymethylated cytosine (5hmC) levels in the vicinity of REV-ERBα genomic binding sites.
30397120	4	53	theme	enzymes	916:922	arg1	activities					784:793	OGT-dependent activities	770:793	OGT-dependent activities of the cytoplasmic protein kinase AKT, an essential relay in insulin signaling, and of ten-of-eleven translocation (TET) enzymes in the nucleus	770:937	We illustrate this finding by showing that REV-ERBα controls OGT-dependent activities of the cytoplasmic protein kinase AKT, an essential relay in insulin signaling, and of ten-of-eleven translocation (TET) enzymes in the nucleus.
30397120	1	54	theme	nuclear	126:132	arg1	REV-ERBα					143:150	The nuclear receptor REV-ERBα	122:150	The nuclear receptor REV-ERBα	122:150	The nuclear receptor REV-ERBα integrates the circadian clock with hepatic glucose and lipid metabolism by nucleating transcriptional comodulators at genomic regulatory regions.
30397120	3	55	theme	OGT	468:470	arg1	activity					472:479	OGT activity	468:479	OGT activity in the nucleus	468:494	By shielding cytoplasmic OGT from proteasomal degradation and favoring OGT activity in the nucleus, REV-ERBα cyclically increased O-GlcNAcylation of multiple cytoplasmic and nuclear proteins as a function of its rhythmically regulated expression, while REV-ERBα ligands mostly affected cytoplasmic OGT activity.
30397120	8	56	theme	SREBP-1c	1625:1632	arg1	transcript					1634:1643	the temporally and nutritionally regulated lipogenic SREBP-1c transcript	1572:1643	the temporally and nutritionally regulated lipogenic SREBP-1c transcript	1572:1643	Conclusion: REV-ERBα regulates cytoplasmic and nuclear OGT-controlled processes that integrate at the hepatic SREBF1 locus to control basal and insulin-induced expression of the temporally and nutritionally regulated lipogenic SREBP-1c transcript.
30397120	8	57	theme	basal	1532:1536	arg1	expression					1558:1567	basal and insulin-induced expression	1532:1567	basal and insulin-induced expression of the temporally and nutritionally regulated lipogenic SREBP-1c transcript	1532:1643	Conclusion: REV-ERBα regulates cytoplasmic and nuclear OGT-controlled processes that integrate at the hepatic SREBF1 locus to control basal and insulin-induced expression of the temporally and nutritionally regulated lipogenic SREBP-1c transcript.
30397120	1	58	theme	receptor	134:141	arg1	REV-ERBα					143:150	The nuclear receptor REV-ERBα	122:150	The nuclear receptor REV-ERBα	122:150	The nuclear receptor REV-ERBα integrates the circadian clock with hepatic glucose and lipid metabolism by nucleating transcriptional comodulators at genomic regulatory regions.
30397120	7	59	theme	rapid	1371:1375	arg1	response					1377:1384	a further rapid response	1361:1384	a further rapid response to insulin	1361:1395	As an example, we show that the REV-ERBα/OGT complex modulates SREBP-1c gene expression throughout the fasting/feeding periods by first repressing AKT phosphorylation and by epigenomically priming the Srebf1 promoter for a further rapid response to insulin.
30397120	8	60	theme	lipogenic	1615:1623	arg1	transcript					1634:1643	the temporally and nutritionally regulated lipogenic SREBP-1c transcript	1572:1643	the temporally and nutritionally regulated lipogenic SREBP-1c transcript	1572:1643	Conclusion: REV-ERBα regulates cytoplasmic and nuclear OGT-controlled processes that integrate at the hepatic SREBF1 locus to control basal and insulin-induced expression of the temporally and nutritionally regulated lipogenic SREBP-1c transcript.
30397120	2	61	theme	interactomic	302:313	arg1	approach					315:322	An interactomic approach	299:322	An interactomic approach	299:322	An interactomic approach identified O-GlcNAc transferase (OGT) as a REV-ERBα-interacting protein.
30397120	4	62	theme	OGT-dependent	770:782	arg1	activities					784:793	OGT-dependent activities	770:793	OGT-dependent activities of the cytoplasmic protein kinase AKT, an essential relay in insulin signaling, and of ten-of-eleven translocation (TET) enzymes in the nucleus	770:937	We illustrate this finding by showing that REV-ERBα controls OGT-dependent activities of the cytoplasmic protein kinase AKT, an essential relay in insulin signaling, and of ten-of-eleven translocation (TET) enzymes in the nucleus.
30397120	2	63	theme	REV-ERBα-interacting	367:386	arg1	protein					388:394	a REV-ERBα-interacting protein	365:394	a REV-ERBα-interacting protein	365:394	An interactomic approach identified O-GlcNAc transferase (OGT) as a REV-ERBα-interacting protein.
30397120	2	63	theme	REV-ERBα-interacting	367:386	arg1	transferase					344:354	O-GlcNAc transferase	335:354	O-GlcNAc transferase (OGT)	335:360	An interactomic approach identified O-GlcNAc transferase (OGT) as a REV-ERBα-interacting protein.
30397120	6	64	theme	binding	1125:1131	arg1	sites					1133:1137	REV-ERBα genomic binding sites	1108:1137	REV-ERBα genomic binding sites	1108:1137	REV-ERBα enhanced TET activity and DNA hydroxymethylated cytosine (5hmC) levels in the vicinity of REV-ERBα genomic binding sites.
30397120	4	65	theme	AKT	829:831	arg1	activities					784:793	OGT-dependent activities	770:793	OGT-dependent activities of the cytoplasmic protein kinase AKT, an essential relay in insulin signaling, and of ten-of-eleven translocation (TET) enzymes in the nucleus	770:937	We illustrate this finding by showing that REV-ERBα controls OGT-dependent activities of the cytoplasmic protein kinase AKT, an essential relay in insulin signaling, and of ten-of-eleven translocation (TET) enzymes in the nucleus.
30397120	3	66	theme	cytoplasmic	555:565	arg1	proteins					579:586	multiple cytoplasmic and nuclear proteins	546:586	multiple cytoplasmic and nuclear proteins	546:586	By shielding cytoplasmic OGT from proteasomal degradation and favoring OGT activity in the nucleus, REV-ERBα cyclically increased O-GlcNAcylation of multiple cytoplasmic and nuclear proteins as a function of its rhythmically regulated expression, while REV-ERBα ligands mostly affected cytoplasmic OGT activity.
30397120	8	67	theme	OGT-controlled	1453:1466	arg1	processes					1468:1476	cytoplasmic and nuclear OGT-controlled processes	1429:1476	cytoplasmic and nuclear OGT-controlled processes that integrate at the hepatic SREBF1 locus to control basal and insulin-induced expression of the temporally and nutritionally regulated lipogenic SREBP-1c transcript	1429:1643	Conclusion: REV-ERBα regulates cytoplasmic and nuclear OGT-controlled processes that integrate at the hepatic SREBF1 locus to control basal and insulin-induced expression of the temporally and nutritionally regulated lipogenic SREBP-1c transcript.
30397120	3	68	theme	multiple	546:553	arg1	proteins					579:586	multiple cytoplasmic and nuclear proteins	546:586	multiple cytoplasmic and nuclear proteins	546:586	By shielding cytoplasmic OGT from proteasomal degradation and favoring OGT activity in the nucleus, REV-ERBα cyclically increased O-GlcNAcylation of multiple cytoplasmic and nuclear proteins as a function of its rhythmically regulated expression, while REV-ERBα ligands mostly affected cytoplasmic OGT activity.
30397120	0	69	theme	events	86:91	arg1	regulation					14:23	Combinatorial regulation	0:23	Combinatorial regulation of hepatic cytoplasmic signaling and nuclear transcriptional events by the OGT/REV-ERBα complex.	0:120	Combinatorial regulation of hepatic cytoplasmic signaling and nuclear transcriptional events by the OGT/REV-ERBα complex.
30397120	6	70	theme	sites	1133:1137	arg1	vicinity					1096:1103	the vicinity	1092:1103	the vicinity of REV-ERBα genomic binding sites	1092:1137	REV-ERBα enhanced TET activity and DNA hydroxymethylated cytosine (5hmC) levels in the vicinity of REV-ERBα genomic binding sites.
30397120	3	71	theme	OGT	695:697	arg1	activity					699:706	cytoplasmic OGT activity	683:706	cytoplasmic OGT activity	683:706	By shielding cytoplasmic OGT from proteasomal degradation and favoring OGT activity in the nucleus, REV-ERBα cyclically increased O-GlcNAcylation of multiple cytoplasmic and nuclear proteins as a function of its rhythmically regulated expression, while REV-ERBα ligands mostly affected cytoplasmic OGT activity.
30397120	7	72	theme	further	1363:1369	arg1	response					1377:1384	a further rapid response	1361:1384	a further rapid response to insulin	1361:1395	As an example, we show that the REV-ERBα/OGT complex modulates SREBP-1c gene expression throughout the fasting/feeding periods by first repressing AKT phosphorylation and by epigenomically priming the Srebf1 promoter for a further rapid response to insulin.
30397120	1	73	theme	genomic	271:277	arg1	regions					290:296	genomic regulatory regions	271:296	genomic regulatory regions	271:296	The nuclear receptor REV-ERBα integrates the circadian clock with hepatic glucose and lipid metabolism by nucleating transcriptional comodulators at genomic regulatory regions.
30397120	0	74	theme	transcriptional	70:84	arg1	events					86:91	nuclear transcriptional events	62:91	nuclear transcriptional events	62:91	Combinatorial regulation of hepatic cytoplasmic signaling and nuclear transcriptional events by the OGT/REV-ERBα complex.
30397120	6	75	theme	TET	1027:1029	arg1	activity					1031:1038	TET activity	1027:1038	TET activity	1027:1038	REV-ERBα enhanced TET activity and DNA hydroxymethylated cytosine (5hmC) levels in the vicinity of REV-ERBα genomic binding sites.
30397120	4	76	theme	ten-of-eleven	882:894	arg1	TET					911:913	TET	911:913	TET	911:913	We illustrate this finding by showing that REV-ERBα controls OGT-dependent activities of the cytoplasmic protein kinase AKT, an essential relay in insulin signaling, and of ten-of-eleven translocation (TET) enzymes in the nucleus.
30397120	4	76	theme	ten-of-eleven	882:894	arg1	translocation					896:908	ten-of-eleven translocation	882:908	ten-of-eleven translocation (TET) enzymes in the nucleus	882:937	We illustrate this finding by showing that REV-ERBα controls OGT-dependent activities of the cytoplasmic protein kinase AKT, an essential relay in insulin signaling, and of ten-of-eleven translocation (TET) enzymes in the nucleus.
30397120	1	77	theme	circadian	167:175	arg1	clock					177:181	the circadian clock	163:181	the circadian clock with hepatic glucose and lipid metabolism	163:223	The nuclear receptor REV-ERBα integrates the circadian clock with hepatic glucose and lipid metabolism by nucleating transcriptional comodulators at genomic regulatory regions.
30397120	1	78	theme	regulatory	279:288	arg1	regions					290:296	genomic regulatory regions	271:296	genomic regulatory regions	271:296	The nuclear receptor REV-ERBα integrates the circadian clock with hepatic glucose and lipid metabolism by nucleating transcriptional comodulators at genomic regulatory regions.
36580660	1	0	theme	simple	176:181	arg1	modification					212:223	a simple but essential monosaccharide modification	174:223	a simple but essential monosaccharide modification	174:223	Among diverse protein post-translational modifications, O-GlcNAcylation, a simple but essential monosaccharide modification, plays crucial roles in cellular processes and is closely related to various diseases.
36580660	1	0	theme	simple	176:181	arg1	O-GlcNAcylation					157:171	O-GlcNAcylation	157:171	O-GlcNAcylation	157:171	Among diverse protein post-translational modifications, O-GlcNAcylation, a simple but essential monosaccharide modification, plays crucial roles in cellular processes and is closely related to various diseases.
36580660	2	1	from	ubiquity	324:331	arg1	cells					336:340	cells	336:340	cells	336:340	Despite its ubiquity in cells, properties of low stoichiometry and reversibility are hard nuts to crack in system-wide research of O-GlcNAc.
36580660	4	2	theme	proteins	614:621	arg1	curves					604:609	Melting curves	596:609	Melting curves of proteins under different treatments	596:648	Melting curves of proteins under different treatments were profiled and compared with high reproducibility and consistency.
36580660	0	3	theme	System-wide	81:91	arg1	Method					93:98	a System-wide Method	79:98	a System-wide Method	79:98	Multi-comparative Thermal Proteome Profiling Uncovers New O-GlcNAc Proteins in a System-wide Method.
36580660	3	4	theme	O-GlcNAc	548:555	arg1	OGT					570:572	OGT	570:572	OGT	570:572	Herein, we developed a novel method employing multi-comparative thermal proteome profiling for O-GlcNAc transferase (OGT) substrate discovery.
36580660	3	4	theme	O-GlcNAc	548:555	arg1	transferase					557:567	O-GlcNAc transferase	548:567	O-GlcNAc transferase (OGT) substrate discovery	548:593	Herein, we developed a novel method employing multi-comparative thermal proteome profiling for O-GlcNAc transferase (OGT) substrate discovery.
36580660	4	5	theme	different	629:637	arg1	treatments					639:648	different treatments	629:648	different treatments	629:648	Melting curves of proteins under different treatments were profiled and compared with high reproducibility and consistency.
36580660	3	6	theme	substrate	575:583	arg1	discovery					585:593	O-GlcNAc transferase (OGT) substrate discovery	548:593	O-GlcNAc transferase (OGT) substrate discovery	548:593	Herein, we developed a novel method employing multi-comparative thermal proteome profiling for O-GlcNAc transferase (OGT) substrate discovery.
36580660	2	7	theme	reversibility	379:391	arg1	properties					343:352	properties	343:352	properties of low stoichiometry and reversibility	343:391	Despite its ubiquity in cells, properties of low stoichiometry and reversibility are hard nuts to crack in system-wide research of O-GlcNAc.
36580660	2	7	theme	reversibility	379:391	arg1	nuts					402:405	hard nuts	397:405	hard nuts to crack in system-wide research of O-GlcNAc	397:450	Despite its ubiquity in cells, properties of low stoichiometry and reversibility are hard nuts to crack in system-wide research of O-GlcNAc.
36580660	1	8	theme	various	294:300	arg1	diseases					302:309	various diseases	294:309	various diseases	294:309	Among diverse protein post-translational modifications, O-GlcNAcylation, a simple but essential monosaccharide modification, plays crucial roles in cellular processes and is closely related to various diseases.
36580660	1	9	theme	post-translational	123:140	arg1	modifications					142:154	diverse protein post-translational modifications	107:154	diverse protein post-translational modifications	107:154	Among diverse protein post-translational modifications, O-GlcNAcylation, a simple but essential monosaccharide modification, plays crucial roles in cellular processes and is closely related to various diseases.
36580660	1	10	theme	essential	187:195	arg1	modification					212:223	a simple but essential monosaccharide modification	174:223	a simple but essential monosaccharide modification	174:223	Among diverse protein post-translational modifications, O-GlcNAcylation, a simple but essential monosaccharide modification, plays crucial roles in cellular processes and is closely related to various diseases.
36580660	1	10	theme	essential	187:195	arg1	O-GlcNAcylation					157:171	O-GlcNAcylation	157:171	O-GlcNAcylation	157:171	Among diverse protein post-translational modifications, O-GlcNAcylation, a simple but essential monosaccharide modification, plays crucial roles in cellular processes and is closely related to various diseases.
36580660	3	11	theme	thermal	517:523	arg1	profiling					534:542	multi-comparative thermal proteome profiling	499:542	multi-comparative thermal proteome profiling for O-GlcNAc transferase (OGT) substrate discovery	499:593	Herein, we developed a novel method employing multi-comparative thermal proteome profiling for O-GlcNAc transferase (OGT) substrate discovery.
36580660	1	12	theme	monosaccharide	197:210	arg1	modification					212:223	a simple but essential monosaccharide modification	174:223	a simple but essential monosaccharide modification	174:223	Among diverse protein post-translational modifications, O-GlcNAcylation, a simple but essential monosaccharide modification, plays crucial roles in cellular processes and is closely related to various diseases.
36580660	1	12	theme	monosaccharide	197:210	arg1	O-GlcNAcylation					157:171	O-GlcNAcylation	157:171	O-GlcNAcylation	157:171	Among diverse protein post-translational modifications, O-GlcNAcylation, a simple but essential monosaccharide modification, plays crucial roles in cellular processes and is closely related to various diseases.
36580660	0	13	theme	Thermal	18:24	arg1	Profiling					35:43	Multi-comparative Thermal Proteome Profiling	0:43	Multi-comparative Thermal Proteome Profiling	0:43	Multi-comparative Thermal Proteome Profiling Uncovers New O-GlcNAc Proteins in a System-wide Method.
36580660	4	14	theme	Melting	596:602	arg1	curves					604:609	Melting curves	596:609	Melting curves of proteins under different treatments	596:648	Melting curves of proteins under different treatments were profiled and compared with high reproducibility and consistency.
36580660	0	15	theme	Multi-comparative	0:16	arg1	Profiling					35:43	Multi-comparative Thermal Proteome Profiling	0:43	Multi-comparative Thermal Proteome Profiling	0:43	Multi-comparative Thermal Proteome Profiling Uncovers New O-GlcNAc Proteins in a System-wide Method.
36580660	5	16	with	proteins	734:741	arg1	stabilities					770:780	significantly shifted stabilities	748:780	significantly shifted stabilities caused by OGT and uridine-5'-diphosphate N-acetylglucosamine	748:841	Consequently, proteins with significantly shifted stabilities caused by OGT and uridine-5'-diphosphate N-acetylglucosamine were screened out from which new O-GlcNAcylated proteins were uncovered.
36580660	5	17	theme	shifted	762:768	arg1	stabilities					770:780	significantly shifted stabilities	748:780	significantly shifted stabilities caused by OGT and uridine-5'-diphosphate N-acetylglucosamine	748:841	Consequently, proteins with significantly shifted stabilities caused by OGT and uridine-5'-diphosphate N-acetylglucosamine were screened out from which new O-GlcNAcylated proteins were uncovered.
36580660	1	18	theme	diverse	107:113	arg1	modifications					142:154	diverse protein post-translational modifications	107:154	diverse protein post-translational modifications	107:154	Among diverse protein post-translational modifications, O-GlcNAcylation, a simple but essential monosaccharide modification, plays crucial roles in cellular processes and is closely related to various diseases.
36580660	2	19	theme	O-GlcNAc	443:450	arg1	research					431:438	system-wide research	419:438	system-wide research of O-GlcNAc	419:450	Despite its ubiquity in cells, properties of low stoichiometry and reversibility are hard nuts to crack in system-wide research of O-GlcNAc.
36580660	0	20	theme	Proteome	26:33	arg1	Profiling					35:43	Multi-comparative Thermal Proteome Profiling	0:43	Multi-comparative Thermal Proteome Profiling	0:43	Multi-comparative Thermal Proteome Profiling Uncovers New O-GlcNAc Proteins in a System-wide Method.
36580660	1	21	theme	protein	115:121	arg1	modifications					142:154	diverse protein post-translational modifications	107:154	diverse protein post-translational modifications	107:154	Among diverse protein post-translational modifications, O-GlcNAcylation, a simple but essential monosaccharide modification, plays crucial roles in cellular processes and is closely related to various diseases.
36580660	1	22	theme	crucial	232:238	arg1	roles					240:244	crucial roles	232:244	crucial roles	232:244	Among diverse protein post-translational modifications, O-GlcNAcylation, a simple but essential monosaccharide modification, plays crucial roles in cellular processes and is closely related to various diseases.
36580660	0	23	theme	New	54:56	arg1	Proteins					67:74	New O-GlcNAc Proteins	54:74	New O-GlcNAc Proteins	54:74	Multi-comparative Thermal Proteome Profiling Uncovers New O-GlcNAc Proteins in a System-wide Method.
36580660	3	24	theme	proteome	525:532	arg1	profiling					534:542	multi-comparative thermal proteome profiling	499:542	multi-comparative thermal proteome profiling for O-GlcNAc transferase (OGT) substrate discovery	499:593	Herein, we developed a novel method employing multi-comparative thermal proteome profiling for O-GlcNAc transferase (OGT) substrate discovery.
36580660	5	25	theme	new	872:874	arg1	proteins					891:898	new O-GlcNAcylated proteins	872:898	new O-GlcNAcylated proteins	872:898	Consequently, proteins with significantly shifted stabilities caused by OGT and uridine-5'-diphosphate N-acetylglucosamine were screened out from which new O-GlcNAcylated proteins were uncovered.
36580660	5	26	dep	screened	848:855	arg1	out					857:859	out	857:859	out	857:859	Consequently, proteins with significantly shifted stabilities caused by OGT and uridine-5'-diphosphate N-acetylglucosamine were screened out from which new O-GlcNAcylated proteins were uncovered.
36580660	2	27	theme	system-wide	419:429	arg1	research					431:438	system-wide research	419:438	system-wide research of O-GlcNAc	419:450	Despite its ubiquity in cells, properties of low stoichiometry and reversibility are hard nuts to crack in system-wide research of O-GlcNAc.
36580660	5	28	theme	O-GlcNAcylated	876:889	arg1	proteins					891:898	new O-GlcNAcylated proteins	872:898	new O-GlcNAcylated proteins	872:898	Consequently, proteins with significantly shifted stabilities caused by OGT and uridine-5'-diphosphate N-acetylglucosamine were screened out from which new O-GlcNAcylated proteins were uncovered.
36580660	2	29	theme	stoichiometry	361:373	arg1	properties					343:352	properties	343:352	properties of low stoichiometry and reversibility	343:391	Despite its ubiquity in cells, properties of low stoichiometry and reversibility are hard nuts to crack in system-wide research of O-GlcNAc.
36580660	2	29	theme	stoichiometry	361:373	arg1	nuts					402:405	hard nuts	397:405	hard nuts to crack in system-wide research of O-GlcNAc	397:450	Despite its ubiquity in cells, properties of low stoichiometry and reversibility are hard nuts to crack in system-wide research of O-GlcNAc.
36580660	0	30	theme	O-GlcNAc	58:65	arg1	Proteins					67:74	New O-GlcNAc Proteins	54:74	New O-GlcNAc Proteins	54:74	Multi-comparative Thermal Proteome Profiling Uncovers New O-GlcNAc Proteins in a System-wide Method.
36580660	2	31	theme	low	357:359	arg1	stoichiometry					361:373	stoichiometry	361:373	stoichiometry	361:373	Despite its ubiquity in cells, properties of low stoichiometry and reversibility are hard nuts to crack in system-wide research of O-GlcNAc.
36580660	5	32	dep	OGT	792:794	arg1	N-acetylglucosamine					823:841	N-acetylglucosamine	823:841	N-acetylglucosamine	823:841	Consequently, proteins with significantly shifted stabilities caused by OGT and uridine-5'-diphosphate N-acetylglucosamine were screened out from which new O-GlcNAcylated proteins were uncovered.
36580660	2	33	from	crack	410:414	arg1	research					431:438	system-wide research	419:438	system-wide research of O-GlcNAc	419:450	Despite its ubiquity in cells, properties of low stoichiometry and reversibility are hard nuts to crack in system-wide research of O-GlcNAc.
36580660	1	34	theme	cellular	249:256	arg1	processes					258:266	cellular processes	249:266	cellular processes	249:266	Among diverse protein post-translational modifications, O-GlcNAcylation, a simple but essential monosaccharide modification, plays crucial roles in cellular processes and is closely related to various diseases.
36580660	3	35	theme	multi-comparative	499:515	arg1	profiling					534:542	multi-comparative thermal proteome profiling	499:542	multi-comparative thermal proteome profiling for O-GlcNAc transferase (OGT) substrate discovery	499:593	Herein, we developed a novel method employing multi-comparative thermal proteome profiling for O-GlcNAc transferase (OGT) substrate discovery.
36580660	4	36	theme	high	682:685	arg1	reproducibility					687:701	high reproducibility	682:701	high reproducibility	682:701	Melting curves of proteins under different treatments were profiled and compared with high reproducibility and consistency.
36580660	3	37	theme	novel	476:480	arg1	method					482:487	a novel method	474:487	a novel method employing multi-comparative thermal proteome profiling for O-GlcNAc transferase (OGT) substrate discovery	474:593	Herein, we developed a novel method employing multi-comparative thermal proteome profiling for O-GlcNAc transferase (OGT) substrate discovery.
36580660	2	38	theme	hard	397:400	arg1	nuts					402:405	hard nuts	397:405	hard nuts to crack in system-wide research of O-GlcNAc	397:450	Despite its ubiquity in cells, properties of low stoichiometry and reversibility are hard nuts to crack in system-wide research of O-GlcNAc.
36580660	2	38	theme	hard	397:400	arg1	properties					343:352	properties	343:352	properties of low stoichiometry and reversibility	343:391	Despite its ubiquity in cells, properties of low stoichiometry and reversibility are hard nuts to crack in system-wide research of O-GlcNAc.
36580660	3	39	theme	transferase	557:567	arg1	discovery					585:593	O-GlcNAc transferase (OGT) substrate discovery	548:593	O-GlcNAc transferase (OGT) substrate discovery	548:593	Herein, we developed a novel method employing multi-comparative thermal proteome profiling for O-GlcNAc transferase (OGT) substrate discovery.
34764359	5	0	theme	corresponding	743:755	arg1	increase					757:764	a corresponding increase	741:764	a corresponding increase in number and total mitochondrial mass	741:803	In a cellular environment with hyper O-GlcNAcylation due to the deletion of O-GlcNAcase (OGA), mitochondria showed a dramatic reduction in size and a corresponding increase in number and total mitochondrial mass.
34764359	11	1	from	impact	1720:1725	arg1	dynamics					1763:1770	mitochondrial dynamics	1749:1770	mitochondrial dynamics	1749:1770	Collectively, these results highlight the impact of O-GlcNAcylation on mitochondrial dynamics and ETC function and mimic the changes that may occur during glucose toxicity from hyperglycemia.
34764359	11	1	from	impact	1720:1725	arg1	function					1780:1787	ETC function	1776:1787	ETC function	1776:1787	Collectively, these results highlight the impact of O-GlcNAcylation on mitochondrial dynamics and ETC function and mimic the changes that may occur during glucose toxicity from hyperglycemia.
34764359	9	2	theme	characterized	1523:1535	arg1	residues					1537:1544	the previously characterized residues	1508:1544	the previously characterized residues in the variable domain (VD)	1508:1572	Individual regions of Drp1 were evaluated for O-GlcNAc modifications, and we found that this post-translational modification (PTM) was not limited to the previously characterized residues in the variable domain (VD).
34764359	9	3	theme	post-translational	1451:1468	arg1	PTM					1484:1486	PTM	1484:1486	PTM	1484:1486	Individual regions of Drp1 were evaluated for O-GlcNAc modifications, and we found that this post-translational modification (PTM) was not limited to the previously characterized residues in the variable domain (VD).
34764359	9	3	theme	post-translational	1451:1468	arg1	modification					1470:1481	this post-translational modification	1446:1481	this post-translational modification (PTM)	1446:1487	Individual regions of Drp1 were evaluated for O-GlcNAc modifications, and we found that this post-translational modification (PTM) was not limited to the previously characterized residues in the variable domain (VD).
34764359	4	4	theme	complexes	567:575	arg1	activity					524:531	the activity	520:531	the activity of electron transport chain (ETC) complexes	520:575	In this manuscript, the role of O-GlcNAcylation on mitochondrial fission, oxidative phosphorylation (Oxphos), and the activity of electron transport chain (ETC) complexes were evaluated.
34764359	4	4	theme	complexes	567:575	arg1	Oxphos					507:512	Oxphos	507:512	Oxphos	507:512	In this manuscript, the role of O-GlcNAcylation on mitochondrial fission, oxidative phosphorylation (Oxphos), and the activity of electron transport chain (ETC) complexes were evaluated.
34764359	4	4	theme	complexes	567:575	arg1	fission					471:477	mitochondrial fission	457:477	mitochondrial fission	457:477	In this manuscript, the role of O-GlcNAcylation on mitochondrial fission, oxidative phosphorylation (Oxphos), and the activity of electron transport chain (ETC) complexes were evaluated.
34764359	4	4	theme	complexes	567:575	arg1	phosphorylation					490:504	oxidative phosphorylation	480:504	oxidative phosphorylation (Oxphos)	480:513	In this manuscript, the role of O-GlcNAcylation on mitochondrial fission, oxidative phosphorylation (Oxphos), and the activity of electron transport chain (ETC) complexes were evaluated.
34764359	5	5	theme	dramatic	710:717	arg1	reduction					719:727	a dramatic reduction	708:727	a dramatic reduction in size	708:735	In a cellular environment with hyper O-GlcNAcylation due to the deletion of O-GlcNAcase (OGA), mitochondria showed a dramatic reduction in size and a corresponding increase in number and total mitochondrial mass.
34764359	6	6	theme	mitochondrial	902:914	arg1	Oxphos					916:921	comparable coupled mitochondrial Oxphos and ATP levels	883:936	Oxphos	916:921	Because of the increased mitochondrial content, OGA knockout cells exhibited comparable coupled mitochondrial Oxphos and ATP levels when compared to WT cells.
34764359	9	7	from	residues	1537:1544	arg1	VD					1570:1571	VD	1570:1571	VD	1570:1571	Individual regions of Drp1 were evaluated for O-GlcNAc modifications, and we found that this post-translational modification (PTM) was not limited to the previously characterized residues in the variable domain (VD).
34764359	9	7	from	residues	1537:1544	arg1	domain					1562:1567	the variable domain	1549:1567	the variable domain (VD)	1549:1572	Individual regions of Drp1 were evaluated for O-GlcNAc modifications, and we found that this post-translational modification (PTM) was not limited to the previously characterized residues in the variable domain (VD).
34764359	2	8	theme	signaling	284:292	arg1	interactions					294:305	signaling interactions	284:305	signaling interactions	284:305	The O-GlcNAc modification can affect protein cellular localization, function, and signaling interactions.
34764359	6	9	theme	coupled	894:900	arg1	Oxphos					916:921	comparable coupled mitochondrial Oxphos and ATP levels	883:936	Oxphos	916:921	Because of the increased mitochondrial content, OGA knockout cells exhibited comparable coupled mitochondrial Oxphos and ATP levels when compared to WT cells.
34764359	5	10	theme	cellular	598:605	arg1	environment					607:617	a cellular environment	596:617	a cellular environment with hyper O-GlcNAcylation due to the deletion of O-GlcNAcase (OGA)	596:685	In a cellular environment with hyper O-GlcNAcylation due to the deletion of O-GlcNAcase (OGA), mitochondria showed a dramatic reduction in size and a corresponding increase in number and total mitochondrial mass.
34764359	11	11	theme	ETC	1776:1778	arg1	function					1780:1787	ETC function	1776:1787	ETC function	1776:1787	Collectively, these results highlight the impact of O-GlcNAcylation on mitochondrial dynamics and ETC function and mimic the changes that may occur during glucose toxicity from hyperglycemia.
34764359	3	12	theme	mitochondrial	350:362	arg1	morphology					364:373	mitochondrial morphology	350:373	mitochondrial morphology	350:373	The specific impact of O-GlcNAcylation on mitochondrial morphology and function has been elusive.
34764359	4	13	theme	oxidative	480:488	arg1	Oxphos					507:512	Oxphos	507:512	Oxphos	507:512	In this manuscript, the role of O-GlcNAcylation on mitochondrial fission, oxidative phosphorylation (Oxphos), and the activity of electron transport chain (ETC) complexes were evaluated.
34764359	4	13	theme	oxidative	480:488	arg1	phosphorylation					490:504	oxidative phosphorylation	480:504	oxidative phosphorylation (Oxphos)	480:513	In this manuscript, the role of O-GlcNAcylation on mitochondrial fission, oxidative phosphorylation (Oxphos), and the activity of electron transport chain (ETC) complexes were evaluated.
34764359	7	14	theme	linked	1090:1095	arg1	activity					1097:1104	linked activity	1090:1104	linked activity for complexes I and III	1090:1128	However, we observed reduced protein levels for complex I and II when comparing normalized mitochondrial content and reduced linked activity for complexes I and III when examining individual ETC complex activities.
34764359	9	15	theme	variable	1553:1560	arg1	VD					1570:1571	VD	1570:1571	VD	1570:1571	Individual regions of Drp1 were evaluated for O-GlcNAc modifications, and we found that this post-translational modification (PTM) was not limited to the previously characterized residues in the variable domain (VD).
34764359	9	15	theme	variable	1553:1560	arg1	domain					1562:1567	the variable domain	1549:1567	the variable domain (VD)	1549:1572	Individual regions of Drp1 were evaluated for O-GlcNAc modifications, and we found that this post-translational modification (PTM) was not limited to the previously characterized residues in the variable domain (VD).
34764359	8	16	theme	dynamin-related	1264:1278	arg1	protein					1280:1286	O-GlcNAcylated dynamin-related protein 1	1249:1288	O-GlcNAcylated dynamin-related protein 1 (Drp1)	1249:1295	In assessing mitochondrial fission, we observed increased amounts of O-GlcNAcylated dynamin-related protein 1 (Drp1) in cells genetically null for OGA and in glioblastoma cells.
34764359	8	16	theme	dynamin-related	1264:1278	arg1	Drp1					1291:1294	Drp1	1291:1294	Drp1	1291:1294	In assessing mitochondrial fission, we observed increased amounts of O-GlcNAcylated dynamin-related protein 1 (Drp1) in cells genetically null for OGA and in glioblastoma cells.
34764359	5	17	theme	hyper	624:628	arg1	O-GlcNAcylation					630:644	hyper O-GlcNAcylation	624:644	hyper O-GlcNAcylation due to the deletion of O-GlcNAcase (OGA)	624:685	In a cellular environment with hyper O-GlcNAcylation due to the deletion of O-GlcNAcase (OGA), mitochondria showed a dramatic reduction in size and a corresponding increase in number and total mitochondrial mass.
34764359	0	18	theme	O-GlcNAc	8:15	arg1	cycling					17:23	Blocked O-GlcNAc cycling	0:23	Blocked O-GlcNAc cycling	0:23	Blocked O-GlcNAc cycling alters mitochondrial morphology, function, and mass.
34764359	6	19	theme	comparable	883:892	arg1	Oxphos					916:921	comparable coupled mitochondrial Oxphos and ATP levels	883:936	Oxphos	916:921	Because of the increased mitochondrial content, OGA knockout cells exhibited comparable coupled mitochondrial Oxphos and ATP levels when compared to WT cells.
34764359	7	20	link	linked	1090:1095	arg1	activity					1097:1104	linked activity	1090:1104	linked activity for complexes I and III	1090:1128	However, we observed reduced protein levels for complex I and II when comparing normalized mitochondrial content and reduced linked activity for complexes I and III when examining individual ETC complex activities.
34764359	0	21	theme	Blocked	0:6	arg1	cycling					17:23	Blocked O-GlcNAc cycling	0:23	Blocked O-GlcNAc cycling	0:23	Blocked O-GlcNAc cycling alters mitochondrial morphology, function, and mass.
34764359	7	22	theme	individual	1145:1154	arg1	activities					1168:1177	individual ETC complex activities	1145:1177	individual ETC complex activities	1145:1177	However, we observed reduced protein levels for complex I and II when comparing normalized mitochondrial content and reduced linked activity for complexes I and III when examining individual ETC complex activities.
34764359	11	23	from	hyperglycemia	1855:1867	arg1	toxicity					1841:1848	glucose toxicity	1833:1848	glucose toxicity from hyperglycemia	1833:1867	Collectively, these results highlight the impact of O-GlcNAcylation on mitochondrial dynamics and ETC function and mimic the changes that may occur during glucose toxicity from hyperglycemia.
34764359	6	24	theme	mitochondrial	831:843	arg1	content					845:851	the increased mitochondrial content	817:851	the increased mitochondrial content	817:851	Because of the increased mitochondrial content, OGA knockout cells exhibited comparable coupled mitochondrial Oxphos and ATP levels when compared to WT cells.
34764359	6	25	theme	increased	821:829	arg1	content					845:851	the increased mitochondrial content	817:851	the increased mitochondrial content	817:851	Because of the increased mitochondrial content, OGA knockout cells exhibited comparable coupled mitochondrial Oxphos and ATP levels when compared to WT cells.
34764359	8	26	theme	O-GlcNAcylated	1249:1262	arg1	protein					1280:1286	O-GlcNAcylated dynamin-related protein 1	1249:1288	O-GlcNAcylated dynamin-related protein 1 (Drp1)	1249:1295	In assessing mitochondrial fission, we observed increased amounts of O-GlcNAcylated dynamin-related protein 1 (Drp1) in cells genetically null for OGA and in glioblastoma cells.
34764359	8	26	theme	O-GlcNAcylated	1249:1262	arg1	Drp1					1291:1294	Drp1	1291:1294	Drp1	1291:1294	In assessing mitochondrial fission, we observed increased amounts of O-GlcNAcylated dynamin-related protein 1 (Drp1) in cells genetically null for OGA and in glioblastoma cells.
34764359	7	27	theme	ETC	1156:1158	arg1	activities					1168:1177	individual ETC complex activities	1145:1177	individual ETC complex activities	1145:1177	However, we observed reduced protein levels for complex I and II when comparing normalized mitochondrial content and reduced linked activity for complexes I and III when examining individual ETC complex activities.
34764359	4	28	theme	chain	555:559	arg1	complexes					567:575	electron transport chain (ETC) complexes	536:575	electron transport chain (ETC) complexes	536:575	In this manuscript, the role of O-GlcNAcylation on mitochondrial fission, oxidative phosphorylation (Oxphos), and the activity of electron transport chain (ETC) complexes were evaluated.
34764359	7	29	theme	mitochondrial	1056:1068	arg1	content					1070:1076	normalized mitochondrial content	1045:1076	normalized mitochondrial content	1045:1076	However, we observed reduced protein levels for complex I and II when comparing normalized mitochondrial content and reduced linked activity for complexes I and III when examining individual ETC complex activities.
34764359	11	30	theme	glucose	1833:1839	arg1	toxicity					1841:1848	glucose toxicity	1833:1848	glucose toxicity from hyperglycemia	1833:1867	Collectively, these results highlight the impact of O-GlcNAcylation on mitochondrial dynamics and ETC function and mimic the changes that may occur during glucose toxicity from hyperglycemia.
34764359	7	31	theme	complex	1160:1166	arg1	activities					1168:1177	individual ETC complex activities	1145:1177	individual ETC complex activities	1145:1177	However, we observed reduced protein levels for complex I and II when comparing normalized mitochondrial content and reduced linked activity for complexes I and III when examining individual ETC complex activities.
34764359	4	32	theme	mitochondrial	457:469	arg1	fission					471:477	mitochondrial fission	457:477	mitochondrial fission	457:477	In this manuscript, the role of O-GlcNAcylation on mitochondrial fission, oxidative phosphorylation (Oxphos), and the activity of electron transport chain (ETC) complexes were evaluated.
34764359	1	33	theme	prevalent	99:107	arg1	form					109:112	a prevalent form	97:112	a prevalent form of glycosylation that regulates proteins within the cytosol, nucleus, and mitochondria	97:199	O-GlcNAcylation is a prevalent form of glycosylation that regulates proteins within the cytosol, nucleus, and mitochondria.
34764359	1	33	theme	prevalent	99:107	arg1	O-GlcNAcylation					78:92	O-GlcNAcylation	78:92	O-GlcNAcylation	78:92	O-GlcNAcylation is a prevalent form of glycosylation that regulates proteins within the cytosol, nucleus, and mitochondria.
34764359	8	34	theme	protein	1280:1286	arg1	amounts					1238:1244	increased amounts	1228:1244	increased amounts of O-GlcNAcylated dynamin-related protein 1 (Drp1)	1228:1295	In assessing mitochondrial fission, we observed increased amounts of O-GlcNAcylated dynamin-related protein 1 (Drp1) in cells genetically null for OGA and in glioblastoma cells.
34764359	8	34	theme	protein	1280:1286	arg1	protein					1280:1286	O-GlcNAcylated dynamin-related protein 1	1249:1288	O-GlcNAcylated dynamin-related protein 1 (Drp1)	1249:1295	In assessing mitochondrial fission, we observed increased amounts of O-GlcNAcylated dynamin-related protein 1 (Drp1) in cells genetically null for OGA and in glioblastoma cells.
34764359	8	34	theme	protein	1280:1286	arg1	Drp1					1291:1294	Drp1	1291:1294	Drp1	1291:1294	In assessing mitochondrial fission, we observed increased amounts of O-GlcNAcylated dynamin-related protein 1 (Drp1) in cells genetically null for OGA and in glioblastoma cells.
34764359	10	35	theme	GTPase	1626:1631	arg1	domain					1633:1638	the GTPase domain	1622:1638	the GTPase domain	1622:1638	Additional modification sites are predicted in the GTPase domain, which may influence enzyme activity.
34764359	6	36	theme	WT	955:956	arg1	cells					958:962	WT cells	955:962	WT cells	955:962	Because of the increased mitochondrial content, OGA knockout cells exhibited comparable coupled mitochondrial Oxphos and ATP levels when compared to WT cells.
34764359	6	37	theme	OGA	854:856	arg1	cells					867:871	OGA knockout cells	854:871	OGA knockout cells	854:871	Because of the increased mitochondrial content, OGA knockout cells exhibited comparable coupled mitochondrial Oxphos and ATP levels when compared to WT cells.
34764359	8	38	theme	mitochondrial	1193:1205	arg1	fission					1207:1213	mitochondrial fission	1193:1213	mitochondrial fission	1193:1213	In assessing mitochondrial fission, we observed increased amounts of O-GlcNAcylated dynamin-related protein 1 (Drp1) in cells genetically null for OGA and in glioblastoma cells.
34764359	10	39	theme	enzyme	1661:1666	arg1	activity					1668:1675	enzyme activity	1661:1675	enzyme activity	1661:1675	Additional modification sites are predicted in the GTPase domain, which may influence enzyme activity.
34764359	0	40	theme	mitochondrial	32:44	arg1	morphology					46:55	mitochondrial morphology	32:55	mitochondrial morphology	32:55	Blocked O-GlcNAc cycling alters mitochondrial morphology, function, and mass.
34764359	9	41	theme	Individual	1358:1367	arg1	regions					1369:1375	Individual regions	1358:1375	Individual regions of Drp1	1358:1383	Individual regions of Drp1 were evaluated for O-GlcNAc modifications, and we found that this post-translational modification (PTM) was not limited to the previously characterized residues in the variable domain (VD).
34764359	7	42	theme	normalized	1045:1054	arg1	content					1070:1076	normalized mitochondrial content	1045:1076	normalized mitochondrial content	1045:1076	However, we observed reduced protein levels for complex I and II when comparing normalized mitochondrial content and reduced linked activity for complexes I and III when examining individual ETC complex activities.
34764359	10	43	theme	modification	1586:1597	arg1	sites					1599:1603	Additional modification sites	1575:1603	Additional modification sites	1575:1603	Additional modification sites are predicted in the GTPase domain, which may influence enzyme activity.
34764359	9	44	theme	Drp1	1380:1383	arg1	regions					1369:1375	Individual regions	1358:1375	Individual regions of Drp1	1358:1383	Individual regions of Drp1 were evaluated for O-GlcNAc modifications, and we found that this post-translational modification (PTM) was not limited to the previously characterized residues in the variable domain (VD).
34764359	8	45	theme	increased	1228:1236	arg1	amounts					1238:1244	increased amounts	1228:1244	increased amounts of O-GlcNAcylated dynamin-related protein 1 (Drp1)	1228:1295	In assessing mitochondrial fission, we observed increased amounts of O-GlcNAcylated dynamin-related protein 1 (Drp1) in cells genetically null for OGA and in glioblastoma cells.
34764359	8	45	theme	increased	1228:1236	arg1	protein					1280:1286	O-GlcNAcylated dynamin-related protein 1	1249:1288	O-GlcNAcylated dynamin-related protein 1 (Drp1)	1249:1295	In assessing mitochondrial fission, we observed increased amounts of O-GlcNAcylated dynamin-related protein 1 (Drp1) in cells genetically null for OGA and in glioblastoma cells.
34764359	8	45	theme	increased	1228:1236	arg1	Drp1					1291:1294	Drp1	1291:1294	Drp1	1291:1294	In assessing mitochondrial fission, we observed increased amounts of O-GlcNAcylated dynamin-related protein 1 (Drp1) in cells genetically null for OGA and in glioblastoma cells.
34764359	5	46	with	environment	607:617	arg1	O-GlcNAcylation					630:644	hyper O-GlcNAcylation	624:644	hyper O-GlcNAcylation due to the deletion of O-GlcNAcase (OGA)	624:685	In a cellular environment with hyper O-GlcNAcylation due to the deletion of O-GlcNAcase (OGA), mitochondria showed a dramatic reduction in size and a corresponding increase in number and total mitochondrial mass.
34764359	5	47	theme	O-GlcNAcase	669:679	arg1	deletion					657:664	the deletion	653:664	the deletion of O-GlcNAcase (OGA)	653:685	In a cellular environment with hyper O-GlcNAcylation due to the deletion of O-GlcNAcase (OGA), mitochondria showed a dramatic reduction in size and a corresponding increase in number and total mitochondrial mass.
34764359	5	48	from	reduction	719:727	arg1	mass					800:803	total mitochondrial mass	780:803	total mitochondrial mass	780:803	In a cellular environment with hyper O-GlcNAcylation due to the deletion of O-GlcNAcase (OGA), mitochondria showed a dramatic reduction in size and a corresponding increase in number and total mitochondrial mass.
34764359	5	48	from	reduction	719:727	arg1	size					732:735	size	732:735	size	732:735	In a cellular environment with hyper O-GlcNAcylation due to the deletion of O-GlcNAcase (OGA), mitochondria showed a dramatic reduction in size and a corresponding increase in number and total mitochondrial mass.
34764359	5	48	from	reduction	719:727	arg1	number					769:774	number	769:774	number	769:774	In a cellular environment with hyper O-GlcNAcylation due to the deletion of O-GlcNAcase (OGA), mitochondria showed a dramatic reduction in size and a corresponding increase in number and total mitochondrial mass.
34764359	6	49	theme	knockout	858:865	arg1	cells					867:871	OGA knockout cells	854:871	OGA knockout cells	854:871	Because of the increased mitochondrial content, OGA knockout cells exhibited comparable coupled mitochondrial Oxphos and ATP levels when compared to WT cells.
34764359	5	50	theme	total	780:784	arg1	mass					800:803	total mitochondrial mass	780:803	total mitochondrial mass	780:803	In a cellular environment with hyper O-GlcNAcylation due to the deletion of O-GlcNAcase (OGA), mitochondria showed a dramatic reduction in size and a corresponding increase in number and total mitochondrial mass.
34764359	4	51	theme	transport	545:553	arg1	ETC					562:564	ETC	562:564	ETC	562:564	In this manuscript, the role of O-GlcNAcylation on mitochondrial fission, oxidative phosphorylation (Oxphos), and the activity of electron transport chain (ETC) complexes were evaluated.
34764359	4	51	theme	transport	545:553	arg1	chain					555:559	electron transport chain	536:559	electron transport chain (ETC) complexes	536:575	In this manuscript, the role of O-GlcNAcylation on mitochondrial fission, oxidative phosphorylation (Oxphos), and the activity of electron transport chain (ETC) complexes were evaluated.
34764359	3	52	theme	specific	312:319	arg1	elusive					397:403	elusive	397:403	elusive	397:403	The specific impact of O-GlcNAcylation on mitochondrial morphology and function has been elusive.
34764359	3	52	theme	specific	312:319	arg1	impact					321:326	The specific impact	308:326	The specific impact of O-GlcNAcylation on mitochondrial morphology and function	308:386	The specific impact of O-GlcNAcylation on mitochondrial morphology and function has been elusive.
34764359	3	53	from	impact	321:326	arg1	morphology					364:373	mitochondrial morphology	350:373	mitochondrial morphology	350:373	The specific impact of O-GlcNAcylation on mitochondrial morphology and function has been elusive.
34764359	3	53	from	impact	321:326	arg1	function					379:386	function	379:386	function	379:386	The specific impact of O-GlcNAcylation on mitochondrial morphology and function has been elusive.
34764359	2	54	theme	O-GlcNAc	206:213	arg1	modification					215:226	The O-GlcNAc modification	202:226	The O-GlcNAc modification	202:226	The O-GlcNAc modification can affect protein cellular localization, function, and signaling interactions.
34764359	7	55	theme	protein	994:1000	arg1	levels					1002:1007	reduced protein levels	986:1007	reduced protein levels for complex I and II	986:1028	However, we observed reduced protein levels for complex I and II when comparing normalized mitochondrial content and reduced linked activity for complexes I and III when examining individual ETC complex activities.
34764359	4	56	theme	electron	536:543	arg1	ETC					562:564	ETC	562:564	ETC	562:564	In this manuscript, the role of O-GlcNAcylation on mitochondrial fission, oxidative phosphorylation (Oxphos), and the activity of electron transport chain (ETC) complexes were evaluated.
34764359	4	56	theme	electron	536:543	arg1	chain					555:559	electron transport chain	536:559	electron transport chain (ETC) complexes	536:575	In this manuscript, the role of O-GlcNAcylation on mitochondrial fission, oxidative phosphorylation (Oxphos), and the activity of electron transport chain (ETC) complexes were evaluated.
34764359	4	57	from	role	430:433	arg1	activity					524:531	the activity	520:531	the activity of electron transport chain (ETC) complexes	520:575	In this manuscript, the role of O-GlcNAcylation on mitochondrial fission, oxidative phosphorylation (Oxphos), and the activity of electron transport chain (ETC) complexes were evaluated.
34764359	4	57	from	role	430:433	arg1	Oxphos					507:512	Oxphos	507:512	Oxphos	507:512	In this manuscript, the role of O-GlcNAcylation on mitochondrial fission, oxidative phosphorylation (Oxphos), and the activity of electron transport chain (ETC) complexes were evaluated.
34764359	4	57	from	role	430:433	arg1	fission					471:477	mitochondrial fission	457:477	mitochondrial fission	457:477	In this manuscript, the role of O-GlcNAcylation on mitochondrial fission, oxidative phosphorylation (Oxphos), and the activity of electron transport chain (ETC) complexes were evaluated.
34764359	4	57	from	role	430:433	arg1	phosphorylation					490:504	oxidative phosphorylation	480:504	oxidative phosphorylation (Oxphos)	480:513	In this manuscript, the role of O-GlcNAcylation on mitochondrial fission, oxidative phosphorylation (Oxphos), and the activity of electron transport chain (ETC) complexes were evaluated.
34764359	5	58	from	increase	757:764	arg1	mass					800:803	total mitochondrial mass	780:803	total mitochondrial mass	780:803	In a cellular environment with hyper O-GlcNAcylation due to the deletion of O-GlcNAcase (OGA), mitochondria showed a dramatic reduction in size and a corresponding increase in number and total mitochondrial mass.
34764359	5	58	from	increase	757:764	arg1	size					732:735	size	732:735	size	732:735	In a cellular environment with hyper O-GlcNAcylation due to the deletion of O-GlcNAcase (OGA), mitochondria showed a dramatic reduction in size and a corresponding increase in number and total mitochondrial mass.
34764359	5	58	from	increase	757:764	arg1	number					769:774	number	769:774	number	769:774	In a cellular environment with hyper O-GlcNAcylation due to the deletion of O-GlcNAcase (OGA), mitochondria showed a dramatic reduction in size and a corresponding increase in number and total mitochondrial mass.
34764359	1	59	theme	glycosylation	117:129	arg1	form					109:112	a prevalent form	97:112	a prevalent form of glycosylation that regulates proteins within the cytosol, nucleus, and mitochondria	97:199	O-GlcNAcylation is a prevalent form of glycosylation that regulates proteins within the cytosol, nucleus, and mitochondria.
34764359	1	59	theme	glycosylation	117:129	arg1	O-GlcNAcylation					78:92	O-GlcNAcylation	78:92	O-GlcNAcylation	78:92	O-GlcNAcylation is a prevalent form of glycosylation that regulates proteins within the cytosol, nucleus, and mitochondria.
34764359	11	60	theme	mitochondrial	1749:1761	arg1	dynamics					1763:1770	mitochondrial dynamics	1749:1770	mitochondrial dynamics	1749:1770	Collectively, these results highlight the impact of O-GlcNAcylation on mitochondrial dynamics and ETC function and mimic the changes that may occur during glucose toxicity from hyperglycemia.
34764359	4	61	theme	O-GlcNAcylation	438:452	arg1	role					430:433	the role	426:433	the role of O-GlcNAcylation on mitochondrial fission, oxidative phosphorylation (Oxphos), and the activity of electron transport chain (ETC) complexes	426:575	In this manuscript, the role of O-GlcNAcylation on mitochondrial fission, oxidative phosphorylation (Oxphos), and the activity of electron transport chain (ETC) complexes were evaluated.
34764359	8	62	theme	glioblastoma	1338:1349	arg1	cells					1351:1355	glioblastoma cells	1338:1355	glioblastoma cells	1338:1355	In assessing mitochondrial fission, we observed increased amounts of O-GlcNAcylated dynamin-related protein 1 (Drp1) in cells genetically null for OGA and in glioblastoma cells.
34764359	8	63	theme	null	1318:1321	arg1	cells					1300:1304	cells	1300:1304	cells genetically null for OGA	1300:1329	In assessing mitochondrial fission, we observed increased amounts of O-GlcNAcylated dynamin-related protein 1 (Drp1) in cells genetically null for OGA and in glioblastoma cells.
34764359	3	64	theme	O-GlcNAcylation	331:345	arg1	elusive					397:403	elusive	397:403	elusive	397:403	The specific impact of O-GlcNAcylation on mitochondrial morphology and function has been elusive.
34764359	3	64	theme	O-GlcNAcylation	331:345	arg1	impact					321:326	The specific impact	308:326	The specific impact of O-GlcNAcylation on mitochondrial morphology and function	308:386	The specific impact of O-GlcNAcylation on mitochondrial morphology and function has been elusive.
34764359	2	65	theme	cellular	247:254	arg1	localization					256:267	protein cellular localization	239:267	protein cellular localization	239:267	The O-GlcNAc modification can affect protein cellular localization, function, and signaling interactions.
34764359	7	66	theme	reduced	986:992	arg1	levels					1002:1007	reduced protein levels	986:1007	reduced protein levels for complex I and II	986:1028	However, we observed reduced protein levels for complex I and II when comparing normalized mitochondrial content and reduced linked activity for complexes I and III when examining individual ETC complex activities.
34764359	11	67	theme	O-GlcNAcylation	1730:1744	arg1	impact					1720:1725	the impact	1716:1725	the impact of O-GlcNAcylation on mitochondrial dynamics and ETC function	1716:1787	Collectively, these results highlight the impact of O-GlcNAcylation on mitochondrial dynamics and ETC function and mimic the changes that may occur during glucose toxicity from hyperglycemia.
34764359	6	68	theme	ATP	927:929	arg1	levels					931:936	comparable coupled mitochondrial Oxphos and ATP levels	883:936	levels	931:936	Because of the increased mitochondrial content, OGA knockout cells exhibited comparable coupled mitochondrial Oxphos and ATP levels when compared to WT cells.
34764359	2	69	theme	protein	239:245	arg1	localization					256:267	protein cellular localization	239:267	protein cellular localization	239:267	The O-GlcNAc modification can affect protein cellular localization, function, and signaling interactions.
34764359	10	70	theme	Additional	1575:1584	arg1	sites					1599:1603	Additional modification sites	1575:1603	Additional modification sites	1575:1603	Additional modification sites are predicted in the GTPase domain, which may influence enzyme activity.
34764359	5	71	theme	mitochondrial	786:798	arg1	mass					800:803	total mitochondrial mass	780:803	total mitochondrial mass	780:803	In a cellular environment with hyper O-GlcNAcylation due to the deletion of O-GlcNAcase (OGA), mitochondria showed a dramatic reduction in size and a corresponding increase in number and total mitochondrial mass.
34764359	9	72	theme	O-GlcNAc	1404:1411	arg1	modifications					1413:1425	O-GlcNAc modifications	1404:1425	O-GlcNAc modifications	1404:1425	Individual regions of Drp1 were evaluated for O-GlcNAc modifications, and we found that this post-translational modification (PTM) was not limited to the previously characterized residues in the variable domain (VD).
22564745	6	0	from	phosphorylation	776:790	arg1	signaling					804:812	cellular signaling	795:812	cellular signaling	795:812	Our results suggest that O-GlcNAcylation may directly regulate a substantial number of kinases and illustrates the increasingly complex relationship between O-GlcNAcylation and phosphorylation in cellular signaling.
22564745	3	1	dep	in	373:374	arg1	vitro					376:380	vitro	376:380	vitro	376:380	Here, we identify additional kinases that are substrates for O-GlcNAcylation using an in vitro OGT assay on a functional kinase array.
22564745	3	2	theme	OGT	382:384	arg1	assay					386:390	an in vitro OGT assay	370:390	an in vitro OGT assay on a functional kinase array	370:419	Here, we identify additional kinases that are substrates for O-GlcNAcylation using an in vitro OGT assay on a functional kinase array.
22564745	1	3	theme	site-specific	59:71	arg1	crosstalk					73:81	site-specific crosstalk	59:81	site-specific crosstalk between O-GlcNAcylation and phosphorylation	59:125	Recent evidence indicates that site-specific crosstalk between O-GlcNAcylation and phosphorylation and the O-GlcNAcylation of kinases play an important role in regulating cell signaling.
22564745	3	4	theme	in	373:374	arg1	assay					386:390	an in vitro OGT assay	370:390	an in vitro OGT assay on a functional kinase array	370:419	Here, we identify additional kinases that are substrates for O-GlcNAcylation using an in vitro OGT assay on a functional kinase array.
22564745	4	5	theme	Forty-two	422:430	arg1	kinases					432:438	Forty-two kinases	422:438	Forty-two kinases	422:438	Forty-two kinases were O-GlcNAcylated in vitro, representing 39% of the kinases on the array.
22564745	6	6	theme	complex	727:733	arg1	relationship					735:746	the increasingly complex relationship	710:746	the increasingly complex relationship between O-GlcNAcylation and phosphorylation in cellular signaling	710:812	Our results suggest that O-GlcNAcylation may directly regulate a substantial number of kinases and illustrates the increasingly complex relationship between O-GlcNAcylation and phosphorylation in cellular signaling.
22564745	1	7	theme	cell	199:202	arg1	signaling					204:212	cell signaling	199:212	cell signaling	199:212	Recent evidence indicates that site-specific crosstalk between O-GlcNAcylation and phosphorylation and the O-GlcNAcylation of kinases play an important role in regulating cell signaling.
22564745	3	8	theme	functional	397:406	arg1	array					415:419	a functional kinase array	395:419	a functional kinase array	395:419	Here, we identify additional kinases that are substrates for O-GlcNAcylation using an in vitro OGT assay on a functional kinase array.
22564745	4	9	theme	kinases	494:500	arg1	kinases					494:500	the kinases	490:500	the kinases	490:500	Forty-two kinases were O-GlcNAcylated in vitro, representing 39% of the kinases on the array.
22564745	4	9	theme	kinases	494:500	arg1	%					485:485	39%	483:485	39% of the kinases	483:500	Forty-two kinases were O-GlcNAcylated in vitro, representing 39% of the kinases on the array.
22564745	5	10	dep	in	546:547	arg1	vivo					549:552	vivo	549:552	vivo	549:552	In addition, we confirmed the in vivo O-GlcNAcylation of three identified kinases.
22564745	3	11	theme	kinase	408:413	arg1	array					415:419	a functional kinase array	395:419	a functional kinase array	395:419	Here, we identify additional kinases that are substrates for O-GlcNAcylation using an in vitro OGT assay on a functional kinase array.
22564745	5	12	theme	identified	579:588	arg1	kinases					590:596	three identified kinases	573:596	three identified kinases	573:596	In addition, we confirmed the in vivo O-GlcNAcylation of three identified kinases.
22564745	5	13	theme	kinases	590:596	arg1	O-GlcNAcylation					554:568	the in vivo O-GlcNAcylation	542:568	the in vivo O-GlcNAcylation of three identified kinases	542:596	In addition, we confirmed the in vivo O-GlcNAcylation of three identified kinases.
22564745	0	14	theme	kinases	19:25	arg1	O-GlcNAcylation					0:14	O-GlcNAcylation	0:14	O-GlcNAcylation of kinases.	0:26	O-GlcNAcylation of kinases.
22564745	3	15	theme	additional	305:314	arg1	kinases					316:322	additional kinases	305:322	additional kinases that are substrates for O-GlcNAcylation using an in vitro OGT assay on a functional kinase array	305:419	Here, we identify additional kinases that are substrates for O-GlcNAcylation using an in vitro OGT assay on a functional kinase array.
22564745	3	15	theme	additional	305:314	arg1	substrates					333:342	substrates	333:342	substrates for O-GlcNAcylation using an in vitro OGT assay on a functional kinase array	333:419	Here, we identify additional kinases that are substrates for O-GlcNAcylation using an in vitro OGT assay on a functional kinase array.
22564745	6	16	theme	kinases	686:692	arg1	number					676:681	a substantial number	662:681	a substantial number of kinases	662:692	Our results suggest that O-GlcNAcylation may directly regulate a substantial number of kinases and illustrates the increasingly complex relationship between O-GlcNAcylation and phosphorylation in cellular signaling.
22564745	4	17	from	vitro	463:467	arg1	O-GlcNAcylated					445:458	O-GlcNAcylated	445:458	O-GlcNAcylated	445:458	Forty-two kinases were O-GlcNAcylated in vitro, representing 39% of the kinases on the array.
22564745	3	18	from	assay	386:390	arg1	array					415:419	a functional kinase array	395:419	a functional kinase array	395:419	Here, we identify additional kinases that are substrates for O-GlcNAcylation using an in vitro OGT assay on a functional kinase array.
22564745	5	19	theme	in	546:547	arg1	O-GlcNAcylation					554:568	the in vivo O-GlcNAcylation	542:568	the in vivo O-GlcNAcylation of three identified kinases	542:596	In addition, we confirmed the in vivo O-GlcNAcylation of three identified kinases.
22564745	2	20	theme	few	235:237	arg1	kinases					239:245	relatively few kinases	224:245	relatively few kinases	224:245	However, relatively few kinases have been analyzed for O-GlcNAcylation.
22564745	6	21	theme	cellular	795:802	arg1	signaling					804:812	cellular signaling	795:812	cellular signaling	795:812	Our results suggest that O-GlcNAcylation may directly regulate a substantial number of kinases and illustrates the increasingly complex relationship between O-GlcNAcylation and phosphorylation in cellular signaling.
22564745	4	22	from	O-GlcNAcylated	445:458	arg1	vitro					463:467	vitro	463:467	vitro	463:467	Forty-two kinases were O-GlcNAcylated in vitro, representing 39% of the kinases on the array.
22564745	1	23	theme	Recent	28:33	arg1	evidence					35:42	Recent evidence	28:42	Recent evidence	28:42	Recent evidence indicates that site-specific crosstalk between O-GlcNAcylation and phosphorylation and the O-GlcNAcylation of kinases play an important role in regulating cell signaling.
22564745	1	24	theme	kinases	154:160	arg1	O-GlcNAcylation					135:149	the O-GlcNAcylation	131:149	the O-GlcNAcylation of kinases	131:160	Recent evidence indicates that site-specific crosstalk between O-GlcNAcylation and phosphorylation and the O-GlcNAcylation of kinases play an important role in regulating cell signaling.
22564745	1	24	theme	kinases	154:160	arg1	crosstalk					73:81	site-specific crosstalk	59:81	site-specific crosstalk between O-GlcNAcylation and phosphorylation	59:125	Recent evidence indicates that site-specific crosstalk between O-GlcNAcylation and phosphorylation and the O-GlcNAcylation of kinases play an important role in regulating cell signaling.
22564745	6	25	theme	substantial	664:674	arg1	number					676:681	a substantial number	662:681	a substantial number of kinases	662:692	Our results suggest that O-GlcNAcylation may directly regulate a substantial number of kinases and illustrates the increasingly complex relationship between O-GlcNAcylation and phosphorylation in cellular signaling.
22564745	6	26	from	O-GlcNAcylation	756:770	arg1	signaling					804:812	cellular signaling	795:812	cellular signaling	795:812	Our results suggest that O-GlcNAcylation may directly regulate a substantial number of kinases and illustrates the increasingly complex relationship between O-GlcNAcylation and phosphorylation in cellular signaling.
22564745	1	27	theme	important	170:178	arg1	role					180:183	an important role	167:183	an important role	167:183	Recent evidence indicates that site-specific crosstalk between O-GlcNAcylation and phosphorylation and the O-GlcNAcylation of kinases play an important role in regulating cell signaling.
17511965	5	0	from	GR	1148:1149	arg1	assays					1190:1195	transient co-transfection assays	1164:1195	transient co-transfection assays in JEG-3 cells	1164:1210	Though, their DNA-binding specificities were not altered as compared to the corresponding wild-type transcription factors, the C-terminal region of the NFI-B isoform was shown to preferentially activate WAP gene transcription in cooperation with GR and STAT5 in transient co-transfection assays in JEG-3 cells.
17511965	1	1	theme	acidic	278:283	arg1	protein					285:291	whey acidic protein	273:291	whey acidic protein (WAP) gene transcription	273:316	The transcription factor nuclear factor I (NFI) has been shown previously both in vivo and in vitro to be involved in the cooperative regulation of whey acidic protein (WAP) gene transcription along with the glucocorticoid receptor and STAT5.
17511965	1	1	theme	acidic	278:283	arg1	WAP					294:296	WAP	294:296	WAP	294:296	The transcription factor nuclear factor I (NFI) has been shown previously both in vivo and in vitro to be involved in the cooperative regulation of whey acidic protein (WAP) gene transcription along with the glucocorticoid receptor and STAT5.
17511965	4	2	theme	transactivation	796:810	arg1	regions					812:818	the transactivation regions	792:818	the transactivation regions of two NFI isoforms	792:838	Here, we analyzed the transactivation regions of two NFI isoforms by making chimeric proteins between the NFI-A and B isoforms.
17511965	3	3	theme	specificities	638:650	arg1	comparison					608:617	A comparison	606:617	A comparison of the DNA-binding specificities of the different NFI isoforms	606:680	A comparison of the DNA-binding specificities of the different NFI isoforms only partially explained their differential ability to activate the WAP gene transcription.
17511965	1	4	theme	transcription	129:141	arg1	factor					158:163	The transcription factor nuclear factor I	125:165	The transcription factor nuclear factor I (NFI)	125:171	The transcription factor nuclear factor I (NFI) has been shown previously both in vivo and in vitro to be involved in the cooperative regulation of whey acidic protein (WAP) gene transcription along with the glucocorticoid receptor and STAT5.
17511965	1	4	theme	transcription	129:141	arg1	NFI					168:170	NFI	168:170	NFI	168:170	The transcription factor nuclear factor I (NFI) has been shown previously both in vivo and in vitro to be involved in the cooperative regulation of whey acidic protein (WAP) gene transcription along with the glucocorticoid receptor and STAT5.
17511965	5	5	theme	JEG-3	1200:1204	arg1	cells					1206:1210	JEG-3 cells	1200:1210	JEG-3 cells	1200:1210	Though, their DNA-binding specificities were not altered as compared to the corresponding wild-type transcription factors, the C-terminal region of the NFI-B isoform was shown to preferentially activate WAP gene transcription in cooperation with GR and STAT5 in transient co-transfection assays in JEG-3 cells.
17511965	2	6	theme	isoforms	405:412	arg1	NFI-B2					415:420	NFI-B2	415:420	NFI-B2	415:420	In addition, one of the specific NFI isoforms, NFI-B2, was demonstrated in transient co-transfection experiments in JEG cells, which lack endogenous NFI, to be preferentially involved in the cooperative regulation of WAP gene expression.
17511965	2	6	theme	isoforms	405:412	arg1	isoforms					405:412	the specific NFI isoforms	388:412	the specific NFI isoforms	388:412	In addition, one of the specific NFI isoforms, NFI-B2, was demonstrated in transient co-transfection experiments in JEG cells, which lack endogenous NFI, to be preferentially involved in the cooperative regulation of WAP gene expression.
17511965	2	6	theme	isoforms	405:412	arg1	one					381:383	one	381:383	one	381:383	In addition, one of the specific NFI isoforms, NFI-B2, was demonstrated in transient co-transfection experiments in JEG cells, which lack endogenous NFI, to be preferentially involved in the cooperative regulation of WAP gene expression.
17511965	1	7	theme	protein	285:291	arg1	transcription					304:316	whey acidic protein (WAP) gene transcription	273:316	whey acidic protein (WAP) gene transcription	273:316	The transcription factor nuclear factor I (NFI) has been shown previously both in vivo and in vitro to be involved in the cooperative regulation of whey acidic protein (WAP) gene transcription along with the glucocorticoid receptor and STAT5.
17511965	1	8	theme	factor	143:148	arg1	factor					158:163	The transcription factor nuclear factor I	125:165	The transcription factor nuclear factor I (NFI)	125:171	The transcription factor nuclear factor I (NFI) has been shown previously both in vivo and in vitro to be involved in the cooperative regulation of whey acidic protein (WAP) gene transcription along with the glucocorticoid receptor and STAT5.
17511965	1	8	theme	factor	143:148	arg1	NFI					168:170	NFI	168:170	NFI	168:170	The transcription factor nuclear factor I (NFI) has been shown previously both in vivo and in vitro to be involved in the cooperative regulation of whey acidic protein (WAP) gene transcription along with the glucocorticoid receptor and STAT5.
17511965	2	9	theme	transient	443:451	arg1	experiments					469:479	transient co-transfection experiments	443:479	transient co-transfection experiments in JEG cells, which lack endogenous NFI, to be preferentially involved in the cooperative regulation of WAP gene expression	443:603	In addition, one of the specific NFI isoforms, NFI-B2, was demonstrated in transient co-transfection experiments in JEG cells, which lack endogenous NFI, to be preferentially involved in the cooperative regulation of WAP gene expression.
17511965	5	10	with	cooperation	1131:1141	arg1	STAT5					1155:1159	STAT5	1155:1159	STAT5	1155:1159	Though, their DNA-binding specificities were not altered as compared to the corresponding wild-type transcription factors, the C-terminal region of the NFI-B isoform was shown to preferentially activate WAP gene transcription in cooperation with GR and STAT5 in transient co-transfection assays in JEG-3 cells.
17511965	5	10	with	cooperation	1131:1141	arg1	GR					1148:1149	GR	1148:1149	GR	1148:1149	Though, their DNA-binding specificities were not altered as compared to the corresponding wild-type transcription factors, the C-terminal region of the NFI-B isoform was shown to preferentially activate WAP gene transcription in cooperation with GR and STAT5 in transient co-transfection assays in JEG-3 cells.
17511965	5	11	theme	NFI-B	1054:1058	arg1	isoform					1060:1066	the NFI-B isoform	1050:1066	the NFI-B isoform	1050:1066	Though, their DNA-binding specificities were not altered as compared to the corresponding wild-type transcription factors, the C-terminal region of the NFI-B isoform was shown to preferentially activate WAP gene transcription in cooperation with GR and STAT5 in transient co-transfection assays in JEG-3 cells.
17511965	6	12	theme	WAP	1462:1464	arg1	transcription					1471:1483	WAP gene transcription	1462:1483	WAP gene transcription	1462:1483	Furthermore, determination of serine and threonine-specific glycosylation (O-linked N-acetylglucosamine) of the C-terminus of the NFI-B isoform suggested that the secondary modification by O-GlcNAc might play a role in the cooperative regulation of WAP gene transcription by NFI-B2 and STAT5.
17511965	3	13	theme	WAP	750:752	arg1	transcription					759:771	the WAP gene transcription	746:771	the WAP gene transcription	746:771	A comparison of the DNA-binding specificities of the different NFI isoforms only partially explained their differential ability to activate the WAP gene transcription.
17511965	6	14	theme	C-terminus	1325:1334	arg1	determination					1226:1238	determination	1226:1238	determination of serine and threonine-specific glycosylation (O-linked N-acetylglucosamine) of the C-terminus of the NFI-B isoform	1226:1355	Furthermore, determination of serine and threonine-specific glycosylation (O-linked N-acetylglucosamine) of the C-terminus of the NFI-B isoform suggested that the secondary modification by O-GlcNAc might play a role in the cooperative regulation of WAP gene transcription by NFI-B2 and STAT5.
17511965	5	15	theme	C-terminal	1029:1038	arg1	region					1040:1045	the C-terminal region	1025:1045	the C-terminal region of the NFI-B isoform	1025:1066	Though, their DNA-binding specificities were not altered as compared to the corresponding wild-type transcription factors, the C-terminal region of the NFI-B isoform was shown to preferentially activate WAP gene transcription in cooperation with GR and STAT5 in transient co-transfection assays in JEG-3 cells.
17511965	2	16	theme	endogenous	506:515	arg1	NFI					517:519	endogenous NFI	506:519	endogenous NFI	506:519	In addition, one of the specific NFI isoforms, NFI-B2, was demonstrated in transient co-transfection experiments in JEG cells, which lack endogenous NFI, to be preferentially involved in the cooperative regulation of WAP gene expression.
17511965	2	17	theme	cooperative	559:569	arg1	regulation					571:580	the cooperative regulation	555:580	the cooperative regulation of WAP gene expression	555:603	In addition, one of the specific NFI isoforms, NFI-B2, was demonstrated in transient co-transfection experiments in JEG cells, which lack endogenous NFI, to be preferentially involved in the cooperative regulation of WAP gene expression.
17511965	3	18	theme	gene	754:757	arg1	transcription					759:771	the WAP gene transcription	746:771	the WAP gene transcription	746:771	A comparison of the DNA-binding specificities of the different NFI isoforms only partially explained their differential ability to activate the WAP gene transcription.
17511965	4	19	theme	B	890:890	arg1	isoforms					892:899	the NFI-A and B isoforms	876:899	isoforms	892:899	Here, we analyzed the transactivation regions of two NFI isoforms by making chimeric proteins between the NFI-A and B isoforms.
17511965	6	20	theme	threonine-specific	1254:1271	arg1	glycosylation					1273:1285	threonine-specific glycosylation	1254:1285	threonine-specific glycosylation (O-linked N-acetylglucosamine)	1254:1316	Furthermore, determination of serine and threonine-specific glycosylation (O-linked N-acetylglucosamine) of the C-terminus of the NFI-B isoform suggested that the secondary modification by O-GlcNAc might play a role in the cooperative regulation of WAP gene transcription by NFI-B2 and STAT5.
17511965	6	20	theme	threonine-specific	1254:1271	arg1	N-acetylglucosamine					1297:1315	O-linked N-acetylglucosamine	1288:1315	O-linked N-acetylglucosamine	1288:1315	Furthermore, determination of serine and threonine-specific glycosylation (O-linked N-acetylglucosamine) of the C-terminus of the NFI-B isoform suggested that the secondary modification by O-GlcNAc might play a role in the cooperative regulation of WAP gene transcription by NFI-B2 and STAT5.
17511965	0	21	gly	glycosylated	60:71	arg1	domain					15:20	The C-terminal domain	0:20	The C-terminal domain of the nuclear factor I-B2 isoform	0:55	The C-terminal domain of the nuclear factor I-B2 isoform is glycosylated and transactivates the WAP gene in the JEG-3 cells.
17511965	0	21	gly	glycosylated	60:71	arg1	isoform					49:55	the nuclear factor I-B2 isoform	25:55	the nuclear factor I-B2 isoform	25:55	The C-terminal domain of the nuclear factor I-B2 isoform is glycosylated and transactivates the WAP gene in the JEG-3 cells.
17511965	1	22	theme	nuclear	150:156	arg1	factor					158:163	The transcription factor nuclear factor I	125:165	The transcription factor nuclear factor I (NFI)	125:171	The transcription factor nuclear factor I (NFI) has been shown previously both in vivo and in vitro to be involved in the cooperative regulation of whey acidic protein (WAP) gene transcription along with the glucocorticoid receptor and STAT5.
17511965	1	22	theme	nuclear	150:156	arg1	NFI					168:170	NFI	168:170	NFI	168:170	The transcription factor nuclear factor I (NFI) has been shown previously both in vivo and in vitro to be involved in the cooperative regulation of whey acidic protein (WAP) gene transcription along with the glucocorticoid receptor and STAT5.
17511965	0	23	theme	WAP	96:98	arg1	gene					100:103	the WAP gene	92:103	the WAP gene in the JEG-3 cells	92:122	The C-terminal domain of the nuclear factor I-B2 isoform is glycosylated and transactivates the WAP gene in the JEG-3 cells.
17511965	1	24	theme	gene	299:302	arg1	transcription					304:316	whey acidic protein (WAP) gene transcription	273:316	whey acidic protein (WAP) gene transcription	273:316	The transcription factor nuclear factor I (NFI) has been shown previously both in vivo and in vitro to be involved in the cooperative regulation of whey acidic protein (WAP) gene transcription along with the glucocorticoid receptor and STAT5.
17511965	2	25	theme	NFI	401:403	arg1	isoforms					405:412	the specific NFI isoforms	388:412	the specific NFI isoforms	388:412	In addition, one of the specific NFI isoforms, NFI-B2, was demonstrated in transient co-transfection experiments in JEG cells, which lack endogenous NFI, to be preferentially involved in the cooperative regulation of WAP gene expression.
17511965	0	26	theme	C-terminal	4:13	arg1	domain					15:20	The C-terminal domain	0:20	The C-terminal domain of the nuclear factor I-B2 isoform	0:55	The C-terminal domain of the nuclear factor I-B2 isoform is glycosylated and transactivates the WAP gene in the JEG-3 cells.
17511965	0	26	theme	C-terminal	4:13	arg1	isoform					49:55	the nuclear factor I-B2 isoform	25:55	the nuclear factor I-B2 isoform	25:55	The C-terminal domain of the nuclear factor I-B2 isoform is glycosylated and transactivates the WAP gene in the JEG-3 cells.
17511965	1	27	theme	transcription	304:316	arg1	regulation					259:268	the cooperative regulation	243:268	the cooperative regulation of whey acidic protein (WAP) gene transcription along with the glucocorticoid receptor and STAT5	243:365	The transcription factor nuclear factor I (NFI) has been shown previously both in vivo and in vitro to be involved in the cooperative regulation of whey acidic protein (WAP) gene transcription along with the glucocorticoid receptor and STAT5.
17511965	2	28	theme	expression	594:603	arg1	regulation					571:580	the cooperative regulation	555:580	the cooperative regulation of WAP gene expression	555:603	In addition, one of the specific NFI isoforms, NFI-B2, was demonstrated in transient co-transfection experiments in JEG cells, which lack endogenous NFI, to be preferentially involved in the cooperative regulation of WAP gene expression.
17511965	4	29	theme	NFI-A	880:884	arg1	isoforms					892:899	the NFI-A and B isoforms	876:899	isoforms	892:899	Here, we analyzed the transactivation regions of two NFI isoforms by making chimeric proteins between the NFI-A and B isoforms.
17511965	5	30	from	assays	1190:1195	arg1	cells					1206:1210	JEG-3 cells	1200:1210	JEG-3 cells	1200:1210	Though, their DNA-binding specificities were not altered as compared to the corresponding wild-type transcription factors, the C-terminal region of the NFI-B isoform was shown to preferentially activate WAP gene transcription in cooperation with GR and STAT5 in transient co-transfection assays in JEG-3 cells.
17511965	3	31	theme	isoforms	673:680	arg1	specificities					638:650	the DNA-binding specificities	622:650	the DNA-binding specificities of the different NFI isoforms	622:680	A comparison of the DNA-binding specificities of the different NFI isoforms only partially explained their differential ability to activate the WAP gene transcription.
17511965	2	32	theme	gene	589:592	arg1	expression					594:603	WAP gene expression	585:603	WAP gene expression	585:603	In addition, one of the specific NFI isoforms, NFI-B2, was demonstrated in transient co-transfection experiments in JEG cells, which lack endogenous NFI, to be preferentially involved in the cooperative regulation of WAP gene expression.
17511965	0	33	theme	factor	37:42	arg1	isoform					49:55	the nuclear factor I-B2 isoform	25:55	the nuclear factor I-B2 isoform	25:55	The C-terminal domain of the nuclear factor I-B2 isoform is glycosylated and transactivates the WAP gene in the JEG-3 cells.
17511965	6	34	theme	NFI-B	1343:1347	arg1	isoform					1349:1355	the NFI-B isoform	1339:1355	the NFI-B isoform	1339:1355	Furthermore, determination of serine and threonine-specific glycosylation (O-linked N-acetylglucosamine) of the C-terminus of the NFI-B isoform suggested that the secondary modification by O-GlcNAc might play a role in the cooperative regulation of WAP gene transcription by NFI-B2 and STAT5.
17511965	2	35	theme	JEG	484:486	arg1	cells					488:492	JEG cells	484:492	JEG cells	484:492	In addition, one of the specific NFI isoforms, NFI-B2, was demonstrated in transient co-transfection experiments in JEG cells, which lack endogenous NFI, to be preferentially involved in the cooperative regulation of WAP gene expression.
17511965	2	36	theme	WAP	585:587	arg1	expression					594:603	WAP gene expression	585:603	WAP gene expression	585:603	In addition, one of the specific NFI isoforms, NFI-B2, was demonstrated in transient co-transfection experiments in JEG cells, which lack endogenous NFI, to be preferentially involved in the cooperative regulation of WAP gene expression.
17511965	3	37	theme	different	659:667	arg1	isoforms					673:680	the different NFI isoforms	655:680	the different NFI isoforms	655:680	A comparison of the DNA-binding specificities of the different NFI isoforms only partially explained their differential ability to activate the WAP gene transcription.
17511965	5	38	from	STAT5	1155:1159	arg1	assays					1190:1195	transient co-transfection assays	1164:1195	transient co-transfection assays in JEG-3 cells	1164:1210	Though, their DNA-binding specificities were not altered as compared to the corresponding wild-type transcription factors, the C-terminal region of the NFI-B isoform was shown to preferentially activate WAP gene transcription in cooperation with GR and STAT5 in transient co-transfection assays in JEG-3 cells.
17511965	5	39	theme	transcription	1002:1014	arg1	factors					1016:1022	the corresponding wild-type transcription factors	974:1022	the corresponding wild-type transcription factors	974:1022	Though, their DNA-binding specificities were not altered as compared to the corresponding wild-type transcription factors, the C-terminal region of the NFI-B isoform was shown to preferentially activate WAP gene transcription in cooperation with GR and STAT5 in transient co-transfection assays in JEG-3 cells.
17511965	6	40	theme	transcription	1471:1483	arg1	regulation					1448:1457	the cooperative regulation	1432:1457	the cooperative regulation of WAP gene transcription by NFI-B2 and STAT5	1432:1503	Furthermore, determination of serine and threonine-specific glycosylation (O-linked N-acetylglucosamine) of the C-terminus of the NFI-B isoform suggested that the secondary modification by O-GlcNAc might play a role in the cooperative regulation of WAP gene transcription by NFI-B2 and STAT5.
17511965	6	41	theme	glycosylation	1273:1285	arg1	determination					1226:1238	determination	1226:1238	determination of serine and threonine-specific glycosylation (O-linked N-acetylglucosamine) of the C-terminus of the NFI-B isoform	1226:1355	Furthermore, determination of serine and threonine-specific glycosylation (O-linked N-acetylglucosamine) of the C-terminus of the NFI-B isoform suggested that the secondary modification by O-GlcNAc might play a role in the cooperative regulation of WAP gene transcription by NFI-B2 and STAT5.
17511965	0	42	theme	nuclear	29:35	arg1	isoform					49:55	the nuclear factor I-B2 isoform	25:55	the nuclear factor I-B2 isoform	25:55	The C-terminal domain of the nuclear factor I-B2 isoform is glycosylated and transactivates the WAP gene in the JEG-3 cells.
17511965	3	43	theme	NFI	669:671	arg1	isoforms					673:680	the different NFI isoforms	655:680	the different NFI isoforms	655:680	A comparison of the DNA-binding specificities of the different NFI isoforms only partially explained their differential ability to activate the WAP gene transcription.
17511965	6	44	theme	O-linked	1288:1295	arg1	glycosylation					1273:1285	threonine-specific glycosylation	1254:1285	threonine-specific glycosylation (O-linked N-acetylglucosamine)	1254:1316	Furthermore, determination of serine and threonine-specific glycosylation (O-linked N-acetylglucosamine) of the C-terminus of the NFI-B isoform suggested that the secondary modification by O-GlcNAc might play a role in the cooperative regulation of WAP gene transcription by NFI-B2 and STAT5.
17511965	6	44	theme	O-linked	1288:1295	arg1	N-acetylglucosamine					1297:1315	O-linked N-acetylglucosamine	1288:1315	O-linked N-acetylglucosamine	1288:1315	Furthermore, determination of serine and threonine-specific glycosylation (O-linked N-acetylglucosamine) of the C-terminus of the NFI-B isoform suggested that the secondary modification by O-GlcNAc might play a role in the cooperative regulation of WAP gene transcription by NFI-B2 and STAT5.
17511965	6	45	theme	secondary	1376:1384	arg1	modification					1386:1397	the secondary modification	1372:1397	the secondary modification by O-GlcNAc	1372:1409	Furthermore, determination of serine and threonine-specific glycosylation (O-linked N-acetylglucosamine) of the C-terminus of the NFI-B isoform suggested that the secondary modification by O-GlcNAc might play a role in the cooperative regulation of WAP gene transcription by NFI-B2 and STAT5.
17511965	6	46	theme	gene	1466:1469	arg1	transcription					1471:1483	WAP gene transcription	1462:1483	WAP gene transcription	1462:1483	Furthermore, determination of serine and threonine-specific glycosylation (O-linked N-acetylglucosamine) of the C-terminus of the NFI-B isoform suggested that the secondary modification by O-GlcNAc might play a role in the cooperative regulation of WAP gene transcription by NFI-B2 and STAT5.
17511965	2	47	theme	specific	392:399	arg1	isoforms					405:412	the specific NFI isoforms	388:412	the specific NFI isoforms	388:412	In addition, one of the specific NFI isoforms, NFI-B2, was demonstrated in transient co-transfection experiments in JEG cells, which lack endogenous NFI, to be preferentially involved in the cooperative regulation of WAP gene expression.
17511965	6	48	theme	isoform	1349:1355	arg1	C-terminus					1325:1334	the C-terminus	1321:1334	the C-terminus of the NFI-B isoform	1321:1355	Furthermore, determination of serine and threonine-specific glycosylation (O-linked N-acetylglucosamine) of the C-terminus of the NFI-B isoform suggested that the secondary modification by O-GlcNAc might play a role in the cooperative regulation of WAP gene transcription by NFI-B2 and STAT5.
17511965	0	49	theme	JEG-3	112:116	arg1	cells					118:122	the JEG-3 cells	108:122	the JEG-3 cells	108:122	The C-terminal domain of the nuclear factor I-B2 isoform is glycosylated and transactivates the WAP gene in the JEG-3 cells.
17511965	6	50	theme	serine	1243:1248	arg1	determination					1226:1238	determination	1226:1238	determination of serine and threonine-specific glycosylation (O-linked N-acetylglucosamine) of the C-terminus of the NFI-B isoform	1226:1355	Furthermore, determination of serine and threonine-specific glycosylation (O-linked N-acetylglucosamine) of the C-terminus of the NFI-B isoform suggested that the secondary modification by O-GlcNAc might play a role in the cooperative regulation of WAP gene transcription by NFI-B2 and STAT5.
17511965	0	51	theme	I-B2	44:47	arg1	isoform					49:55	the nuclear factor I-B2 isoform	25:55	the nuclear factor I-B2 isoform	25:55	The C-terminal domain of the nuclear factor I-B2 isoform is glycosylated and transactivates the WAP gene in the JEG-3 cells.
17511965	1	52	theme	cooperative	247:257	arg1	regulation					259:268	the cooperative regulation	243:268	the cooperative regulation of whey acidic protein (WAP) gene transcription along with the glucocorticoid receptor and STAT5	243:365	The transcription factor nuclear factor I (NFI) has been shown previously both in vivo and in vitro to be involved in the cooperative regulation of whey acidic protein (WAP) gene transcription along with the glucocorticoid receptor and STAT5.
17511965	4	53	theme	NFI	827:829	arg1	isoforms					831:838	two NFI isoforms	823:838	two NFI isoforms	823:838	Here, we analyzed the transactivation regions of two NFI isoforms by making chimeric proteins between the NFI-A and B isoforms.
17511965	1	54	theme	glucocorticoid	333:346	arg1	receptor					348:355	the glucocorticoid receptor	329:355	the glucocorticoid receptor	329:355	The transcription factor nuclear factor I (NFI) has been shown previously both in vivo and in vitro to be involved in the cooperative regulation of whey acidic protein (WAP) gene transcription along with the glucocorticoid receptor and STAT5.
17511965	3	55	theme	DNA-binding	626:636	arg1	specificities					638:650	the DNA-binding specificities	622:650	the DNA-binding specificities of the different NFI isoforms	622:680	A comparison of the DNA-binding specificities of the different NFI isoforms only partially explained their differential ability to activate the WAP gene transcription.
17511965	2	56	theme	co-transfection	453:467	arg1	experiments					469:479	transient co-transfection experiments	443:479	transient co-transfection experiments in JEG cells, which lack endogenous NFI, to be preferentially involved in the cooperative regulation of WAP gene expression	443:603	In addition, one of the specific NFI isoforms, NFI-B2, was demonstrated in transient co-transfection experiments in JEG cells, which lack endogenous NFI, to be preferentially involved in the cooperative regulation of WAP gene expression.
17511965	4	57	theme	chimeric	850:857	arg1	proteins					859:866	chimeric proteins	850:866	chimeric proteins between the NFI-A and B isoforms	850:899	Here, we analyzed the transactivation regions of two NFI isoforms by making chimeric proteins between the NFI-A and B isoforms.
17511965	0	58	from	gene	100:103	arg1	cells					118:122	the JEG-3 cells	108:122	the JEG-3 cells	108:122	The C-terminal domain of the nuclear factor I-B2 isoform is glycosylated and transactivates the WAP gene in the JEG-3 cells.
17511965	6	59	theme	cooperative	1436:1446	arg1	regulation					1448:1457	the cooperative regulation	1432:1457	the cooperative regulation of WAP gene transcription by NFI-B2 and STAT5	1432:1503	Furthermore, determination of serine and threonine-specific glycosylation (O-linked N-acetylglucosamine) of the C-terminus of the NFI-B isoform suggested that the secondary modification by O-GlcNAc might play a role in the cooperative regulation of WAP gene transcription by NFI-B2 and STAT5.
17511965	6	60	link	O-linked	1288:1295	arg1	glycosylation					1273:1285	threonine-specific glycosylation	1254:1285	threonine-specific glycosylation (O-linked N-acetylglucosamine)	1254:1316	Furthermore, determination of serine and threonine-specific glycosylation (O-linked N-acetylglucosamine) of the C-terminus of the NFI-B isoform suggested that the secondary modification by O-GlcNAc might play a role in the cooperative regulation of WAP gene transcription by NFI-B2 and STAT5.
17511965	6	60	link	O-linked	1288:1295	arg1	N-acetylglucosamine					1297:1315	O-linked N-acetylglucosamine	1288:1315	O-linked N-acetylglucosamine	1288:1315	Furthermore, determination of serine and threonine-specific glycosylation (O-linked N-acetylglucosamine) of the C-terminus of the NFI-B isoform suggested that the secondary modification by O-GlcNAc might play a role in the cooperative regulation of WAP gene transcription by NFI-B2 and STAT5.
17511965	5	61	theme	WAP	1105:1107	arg1	transcription					1114:1126	WAP gene transcription	1105:1126	WAP gene transcription	1105:1126	Though, their DNA-binding specificities were not altered as compared to the corresponding wild-type transcription factors, the C-terminal region of the NFI-B isoform was shown to preferentially activate WAP gene transcription in cooperation with GR and STAT5 in transient co-transfection assays in JEG-3 cells.
17511965	2	62	from	experiments	469:479	arg1	cells					488:492	JEG cells	484:492	JEG cells	484:492	In addition, one of the specific NFI isoforms, NFI-B2, was demonstrated in transient co-transfection experiments in JEG cells, which lack endogenous NFI, to be preferentially involved in the cooperative regulation of WAP gene expression.
17511965	4	63	theme	isoforms	831:838	arg1	regions					812:818	the transactivation regions	792:818	the transactivation regions of two NFI isoforms	792:838	Here, we analyzed the transactivation regions of two NFI isoforms by making chimeric proteins between the NFI-A and B isoforms.
17511965	5	64	theme	corresponding	978:990	arg1	factors					1016:1022	the corresponding wild-type transcription factors	974:1022	the corresponding wild-type transcription factors	974:1022	Though, their DNA-binding specificities were not altered as compared to the corresponding wild-type transcription factors, the C-terminal region of the NFI-B isoform was shown to preferentially activate WAP gene transcription in cooperation with GR and STAT5 in transient co-transfection assays in JEG-3 cells.
17511965	5	65	theme	DNA-binding	916:926	arg1	specificities					928:940	their DNA-binding specificities	910:940	their DNA-binding specificities	910:940	Though, their DNA-binding specificities were not altered as compared to the corresponding wild-type transcription factors, the C-terminal region of the NFI-B isoform was shown to preferentially activate WAP gene transcription in cooperation with GR and STAT5 in transient co-transfection assays in JEG-3 cells.
17511965	5	66	theme	transient	1164:1172	arg1	assays					1190:1195	transient co-transfection assays	1164:1195	transient co-transfection assays in JEG-3 cells	1164:1210	Though, their DNA-binding specificities were not altered as compared to the corresponding wild-type transcription factors, the C-terminal region of the NFI-B isoform was shown to preferentially activate WAP gene transcription in cooperation with GR and STAT5 in transient co-transfection assays in JEG-3 cells.
17511965	5	67	theme	wild-type	992:1000	arg1	factors					1016:1022	the corresponding wild-type transcription factors	974:1022	the corresponding wild-type transcription factors	974:1022	Though, their DNA-binding specificities were not altered as compared to the corresponding wild-type transcription factors, the C-terminal region of the NFI-B isoform was shown to preferentially activate WAP gene transcription in cooperation with GR and STAT5 in transient co-transfection assays in JEG-3 cells.
17511965	5	68	theme	isoform	1060:1066	arg1	region					1040:1045	the C-terminal region	1025:1045	the C-terminal region of the NFI-B isoform	1025:1066	Though, their DNA-binding specificities were not altered as compared to the corresponding wild-type transcription factors, the C-terminal region of the NFI-B isoform was shown to preferentially activate WAP gene transcription in cooperation with GR and STAT5 in transient co-transfection assays in JEG-3 cells.
17511965	5	69	theme	gene	1109:1112	arg1	transcription					1114:1126	WAP gene transcription	1105:1126	WAP gene transcription	1105:1126	Though, their DNA-binding specificities were not altered as compared to the corresponding wild-type transcription factors, the C-terminal region of the NFI-B isoform was shown to preferentially activate WAP gene transcription in cooperation with GR and STAT5 in transient co-transfection assays in JEG-3 cells.
17511965	5	70	theme	co-transfection	1174:1188	arg1	assays					1190:1195	transient co-transfection assays	1164:1195	transient co-transfection assays in JEG-3 cells	1164:1210	Though, their DNA-binding specificities were not altered as compared to the corresponding wild-type transcription factors, the C-terminal region of the NFI-B isoform was shown to preferentially activate WAP gene transcription in cooperation with GR and STAT5 in transient co-transfection assays in JEG-3 cells.
17511965	0	71	theme	isoform	49:55	arg1	domain					15:20	The C-terminal domain	0:20	The C-terminal domain of the nuclear factor I-B2 isoform	0:55	The C-terminal domain of the nuclear factor I-B2 isoform is glycosylated and transactivates the WAP gene in the JEG-3 cells.
17511965	0	71	theme	isoform	49:55	arg1	isoform					49:55	the nuclear factor I-B2 isoform	25:55	the nuclear factor I-B2 isoform	25:55	The C-terminal domain of the nuclear factor I-B2 isoform is glycosylated and transactivates the WAP gene in the JEG-3 cells.
17511965	1	72	theme	whey	273:276	arg1	protein					285:291	whey acidic protein	273:291	whey acidic protein (WAP) gene transcription	273:316	The transcription factor nuclear factor I (NFI) has been shown previously both in vivo and in vitro to be involved in the cooperative regulation of whey acidic protein (WAP) gene transcription along with the glucocorticoid receptor and STAT5.
17511965	1	72	theme	whey	273:276	arg1	WAP					294:296	WAP	294:296	WAP	294:296	The transcription factor nuclear factor I (NFI) has been shown previously both in vivo and in vitro to be involved in the cooperative regulation of whey acidic protein (WAP) gene transcription along with the glucocorticoid receptor and STAT5.
17511965	3	73	theme	differential	713:724	arg1	ability					726:732	their differential ability to activate the WAP gene transcription	707:771	their differential ability to activate the WAP gene transcription	707:771	A comparison of the DNA-binding specificities of the different NFI isoforms only partially explained their differential ability to activate the WAP gene transcription.
31896813	8	0	theme	DR5	1287:1289	arg1	oligomerization					1291:1305	TRA-8-induced DR5 oligomerization	1273:1305	TRA-8-induced DR5 oligomerization	1273:1305	Mechanistic studies revealed direct O-GlcNAc modifications of DR5, which regulated TRA-8-induced DR5 oligomerization.
31896813	5	1	theme	TRAIL-resistant	722:736	arg1	cells					756:760	TRAIL-resistant pancreatic cancer cells	722:760	TRAIL-resistant pancreatic cancer cells	722:760	In this study, we evaluated the role of protein O-GlcNAcylation in pancreatic cancer TRAIL resistance, and identified higher levels of O-GlcNAcylation in TRAIL-resistant pancreatic cancer cells.
31896813	6	2	from	apoptosis	1029:1037	arg1	cells					1059:1063	TRAIL-resistance cells	1042:1063	TRAIL-resistance cells	1042:1063	With gain- and loss-of-function of the O-GlcNAc-adding enzyme, O-GlcNActransferase (OGT), we determined that increasing O-GlcNAcylation rendered TRAIL-sensitive cells more resistant to TRA-8-induced apoptosis, while inhibiting O-GlcNAcylation promoted TRA-8-induced apoptosis in TRAIL-resistance cells.
31896813	6	3	theme	TRA-8-induced	1015:1027	arg1	apoptosis					1029:1037	TRA-8-induced apoptosis	1015:1037	TRA-8-induced apoptosis in TRAIL-resistance cells	1015:1063	With gain- and loss-of-function of the O-GlcNAc-adding enzyme, O-GlcNActransferase (OGT), we determined that increasing O-GlcNAcylation rendered TRAIL-sensitive cells more resistant to TRA-8-induced apoptosis, while inhibiting O-GlcNAcylation promoted TRA-8-induced apoptosis in TRAIL-resistance cells.
31896813	6	4	theme	TRAIL-sensitive	908:922	arg1	cells					924:928	TRAIL-sensitive cells	908:928	TRAIL-sensitive cells	908:928	With gain- and loss-of-function of the O-GlcNAc-adding enzyme, O-GlcNActransferase (OGT), we determined that increasing O-GlcNAcylation rendered TRAIL-sensitive cells more resistant to TRA-8-induced apoptosis, while inhibiting O-GlcNAcylation promoted TRA-8-induced apoptosis in TRAIL-resistance cells.
31896813	5	5	theme	pancreatic	635:644	arg1	resistance					659:668	pancreatic cancer TRAIL resistance	635:668	pancreatic cancer TRAIL resistance	635:668	In this study, we evaluated the role of protein O-GlcNAcylation in pancreatic cancer TRAIL resistance, and identified higher levels of O-GlcNAcylation in TRAIL-resistant pancreatic cancer cells.
31896813	5	6	theme	O-GlcNAcylation	703:717	arg1	levels					693:698	higher levels	686:698	higher levels of O-GlcNAcylation in TRAIL-resistant pancreatic cancer cells	686:760	In this study, we evaluated the role of protein O-GlcNAcylation in pancreatic cancer TRAIL resistance, and identified higher levels of O-GlcNAcylation in TRAIL-resistant pancreatic cancer cells.
31896813	5	7	theme	cancer	646:651	arg1	resistance					659:668	pancreatic cancer TRAIL resistance	635:668	pancreatic cancer TRAIL resistance	635:668	In this study, we evaluated the role of protein O-GlcNAcylation in pancreatic cancer TRAIL resistance, and identified higher levels of O-GlcNAcylation in TRAIL-resistant pancreatic cancer cells.
31896813	9	8	theme	downstream	1405:1414	arg1	signaling					1431:1439	the downstream death-inducing signaling	1401:1439	the downstream death-inducing signaling	1401:1439	We further defined that DR5 O-GlcNAcylation was independent of FADD, the adapter protein for the downstream death-inducing signaling.
31896813	5	9	theme	TRAIL	653:657	arg1	resistance					659:668	pancreatic cancer TRAIL resistance	635:668	pancreatic cancer TRAIL resistance	635:668	In this study, we evaluated the role of protein O-GlcNAcylation in pancreatic cancer TRAIL resistance, and identified higher levels of O-GlcNAcylation in TRAIL-resistant pancreatic cancer cells.
31896813	6	10	theme	inhibiting	979:988	arg1	O-GlcNAcylation					990:1004	inhibiting O-GlcNAcylation	979:1004	inhibiting O-GlcNAcylation	979:1004	With gain- and loss-of-function of the O-GlcNAc-adding enzyme, O-GlcNActransferase (OGT), we determined that increasing O-GlcNAcylation rendered TRAIL-sensitive cells more resistant to TRA-8-induced apoptosis, while inhibiting O-GlcNAcylation promoted TRA-8-induced apoptosis in TRAIL-resistance cells.
31896813	5	11	from	role	600:603	arg1	resistance					659:668	pancreatic cancer TRAIL resistance	635:668	pancreatic cancer TRAIL resistance	635:668	In this study, we evaluated the role of protein O-GlcNAcylation in pancreatic cancer TRAIL resistance, and identified higher levels of O-GlcNAcylation in TRAIL-resistant pancreatic cancer cells.
31896813	1	12	theme	TRAIL-activating	77:92	arg1	therapy					94:100	TRAIL-activating therapy	77:100	TRAIL-activating therapy	77:100	TRAIL-activating therapy is promising in treating various cancers, including pancreatic cancer, a highly malignant neoplasm with poor prognosis.
31896813	9	13	theme	death-inducing	1416:1429	arg1	signaling					1431:1439	the downstream death-inducing signaling	1401:1439	the downstream death-inducing signaling	1401:1439	We further defined that DR5 O-GlcNAcylation was independent of FADD, the adapter protein for the downstream death-inducing signaling.
31896813	3	14	theme	Protein	359:365	arg1	modification					416:427	a versatile posttranslational modification	386:427	a versatile posttranslational modification that regulates various biological processes	386:471	Protein O-GlcNAcylation is a versatile posttranslational modification that regulates various biological processes.
31896813	3	14	theme	Protein	359:365	arg1	O-GlcNAcylation					367:381	Protein O-GlcNAcylation	359:381	Protein O-GlcNAcylation	359:381	Protein O-GlcNAcylation is a versatile posttranslational modification that regulates various biological processes.
31896813	3	15	theme	various	444:450	arg1	processes					463:471	various biological processes	444:471	various biological processes	444:471	Protein O-GlcNAcylation is a versatile posttranslational modification that regulates various biological processes.
31896813	2	16	theme	TRAIL-induced	277:289	arg1	apoptosis					291:299	TRAIL-induced apoptosis	277:299	TRAIL-induced apoptosis despite their expression of intact death receptors (DRs)	277:356	However, many pancreatic cancer cells are resistant to TRAIL-induced apoptosis despite their expression of intact death receptors (DRs).
31896813	9	17	theme	adapter	1381:1387	arg1	protein					1389:1395	the adapter protein	1377:1395	the adapter protein for the downstream death-inducing signaling	1377:1439	We further defined that DR5 O-GlcNAcylation was independent of FADD, the adapter protein for the downstream death-inducing signaling.
31896813	9	17	theme	adapter	1381:1387	arg1	FADD					1371:1374	FADD	1371:1374	FADD	1371:1374	We further defined that DR5 O-GlcNAcylation was independent of FADD, the adapter protein for the downstream death-inducing signaling.
31896813	1	18	theme	malignant	182:190	arg1	neoplasm					192:199	a highly malignant neoplasm	173:199	a highly malignant neoplasm with poor prognosis	173:219	TRAIL-activating therapy is promising in treating various cancers, including pancreatic cancer, a highly malignant neoplasm with poor prognosis.
31896813	1	18	theme	malignant	182:190	arg1	cancer					165:170	pancreatic cancer	154:170	pancreatic cancer	154:170	TRAIL-activating therapy is promising in treating various cancers, including pancreatic cancer, a highly malignant neoplasm with poor prognosis.
31896813	3	19	theme	posttranslational	398:414	arg1	modification					416:427	a versatile posttranslational modification	386:427	a versatile posttranslational modification that regulates various biological processes	386:471	Protein O-GlcNAcylation is a versatile posttranslational modification that regulates various biological processes.
31896813	3	19	theme	posttranslational	398:414	arg1	O-GlcNAcylation					367:381	Protein O-GlcNAcylation	359:381	Protein O-GlcNAcylation	359:381	Protein O-GlcNAcylation is a versatile posttranslational modification that regulates various biological processes.
31896813	4	20	theme	cancer	535:540	arg1	cell					542:545	cancer cell growth and survival	535:565	cancer cell growth and survival	535:565	Elevated protein O-GlcNAcylation has been recently linked to cancer cell growth and survival.
31896813	8	21	theme	Mechanistic	1190:1200	arg1	studies					1202:1208	Mechanistic studies	1190:1208	Mechanistic studies	1190:1208	Mechanistic studies revealed direct O-GlcNAc modifications of DR5, which regulated TRA-8-induced DR5 oligomerization.
31896813	5	22	theme	protein	608:614	arg1	O-GlcNAcylation					616:630	protein O-GlcNAcylation	608:630	protein O-GlcNAcylation	608:630	In this study, we evaluated the role of protein O-GlcNAcylation in pancreatic cancer TRAIL resistance, and identified higher levels of O-GlcNAcylation in TRAIL-resistant pancreatic cancer cells.
31896813	2	23	theme	death	336:340	arg1	DRs					353:355	DRs	353:355	DRs	353:355	However, many pancreatic cancer cells are resistant to TRAIL-induced apoptosis despite their expression of intact death receptors (DRs).
31896813	2	23	theme	death	336:340	arg1	receptors					342:350	intact death receptors	329:350	intact death receptors (DRs)	329:356	However, many pancreatic cancer cells are resistant to TRAIL-induced apoptosis despite their expression of intact death receptors (DRs).
31896813	10	24	theme	DR-inducing	1670:1680	arg1	signaling					1682:1690	DR-inducing signaling	1670:1690	DR-inducing signaling	1670:1690	These studies have demonstrated an important role of protein O-GlcNAcylation in regulating TRAIL resistance of pancreatic cancer cells; and uncovered the contribution of O-GlcNAcylation to DR5 oligomerization and thus mediating DR-inducing signaling.
31896813	4	25	dep	cell	542:545	arg1	survival					558:565	survival	558:565	survival	558:565	Elevated protein O-GlcNAcylation has been recently linked to cancer cell growth and survival.
31896813	4	25	dep	cell	542:545	arg1	growth					547:552	growth	547:552	growth	547:552	Elevated protein O-GlcNAcylation has been recently linked to cancer cell growth and survival.
31896813	5	26	theme	higher	686:691	arg1	levels					693:698	higher levels	686:698	higher levels of O-GlcNAcylation in TRAIL-resistant pancreatic cancer cells	686:760	In this study, we evaluated the role of protein O-GlcNAcylation in pancreatic cancer TRAIL resistance, and identified higher levels of O-GlcNAcylation in TRAIL-resistant pancreatic cancer cells.
31896813	5	27	theme	O-GlcNAcylation	616:630	arg1	role					600:603	the role	596:603	the role of protein O-GlcNAcylation in pancreatic cancer TRAIL resistance	596:668	In this study, we evaluated the role of protein O-GlcNAcylation in pancreatic cancer TRAIL resistance, and identified higher levels of O-GlcNAcylation in TRAIL-resistant pancreatic cancer cells.
31896813	2	28	theme	intact	329:334	arg1	DRs					353:355	DRs	353:355	DRs	353:355	However, many pancreatic cancer cells are resistant to TRAIL-induced apoptosis despite their expression of intact death receptors (DRs).
31896813	2	28	theme	intact	329:334	arg1	receptors					342:350	intact death receptors	329:350	intact death receptors (DRs)	329:356	However, many pancreatic cancer cells are resistant to TRAIL-induced apoptosis despite their expression of intact death receptors (DRs).
31896813	10	29	theme	important	1477:1485	arg1	role					1487:1490	an important role	1474:1490	an important role of protein O-GlcNAcylation in regulating TRAIL resistance of pancreatic cancer cells	1474:1575	These studies have demonstrated an important role of protein O-GlcNAcylation in regulating TRAIL resistance of pancreatic cancer cells; and uncovered the contribution of O-GlcNAcylation to DR5 oligomerization and thus mediating DR-inducing signaling.
31896813	10	30	theme	O-GlcNAcylation	1612:1626	arg1	contribution					1596:1607	the contribution	1592:1607	the contribution of O-GlcNAcylation to DR5 oligomerization	1592:1649	These studies have demonstrated an important role of protein O-GlcNAcylation in regulating TRAIL resistance of pancreatic cancer cells; and uncovered the contribution of O-GlcNAcylation to DR5 oligomerization and thus mediating DR-inducing signaling.
31896813	0	31	theme	cancer	25:30	arg1	resistance					38:47	pancreatic cancer TRAIL resistance	14:47	pancreatic cancer TRAIL resistance	14:47	Regulation of pancreatic cancer TRAIL resistance by protein O-GlcNAcylation.
31896813	9	32	theme	FADD	1371:1374	arg1	independent					1356:1366	independent	1356:1366	independent	1356:1366	We further defined that DR5 O-GlcNAcylation was independent of FADD, the adapter protein for the downstream death-inducing signaling.
31896813	6	33	theme	increasing	872:881	arg1	O-GlcNAcylation					883:897	increasing O-GlcNAcylation	872:897	increasing O-GlcNAcylation	872:897	With gain- and loss-of-function of the O-GlcNAc-adding enzyme, O-GlcNActransferase (OGT), we determined that increasing O-GlcNAcylation rendered TRAIL-sensitive cells more resistant to TRA-8-induced apoptosis, while inhibiting O-GlcNAcylation promoted TRA-8-induced apoptosis in TRAIL-resistance cells.
31896813	10	34	theme	DR5	1631:1633	arg1	oligomerization					1635:1649	DR5 oligomerization	1631:1649	DR5 oligomerization	1631:1649	These studies have demonstrated an important role of protein O-GlcNAcylation in regulating TRAIL resistance of pancreatic cancer cells; and uncovered the contribution of O-GlcNAcylation to DR5 oligomerization and thus mediating DR-inducing signaling.
31896813	1	35	theme	poor	206:209	arg1	prognosis					211:219	poor prognosis	206:219	poor prognosis	206:219	TRAIL-activating therapy is promising in treating various cancers, including pancreatic cancer, a highly malignant neoplasm with poor prognosis.
31896813	3	36	theme	versatile	388:396	arg1	modification					416:427	a versatile posttranslational modification	386:427	a versatile posttranslational modification that regulates various biological processes	386:471	Protein O-GlcNAcylation is a versatile posttranslational modification that regulates various biological processes.
31896813	3	36	theme	versatile	388:396	arg1	O-GlcNAcylation					367:381	Protein O-GlcNAcylation	359:381	Protein O-GlcNAcylation	359:381	Protein O-GlcNAcylation is a versatile posttranslational modification that regulates various biological processes.
31896813	10	37	theme	cells	1571:1575	arg1	resistance					1539:1548	TRAIL resistance	1533:1548	TRAIL resistance of pancreatic cancer cells	1533:1575	These studies have demonstrated an important role of protein O-GlcNAcylation in regulating TRAIL resistance of pancreatic cancer cells; and uncovered the contribution of O-GlcNAcylation to DR5 oligomerization and thus mediating DR-inducing signaling.
31896813	9	38	theme	DR5	1332:1334	arg1	O-GlcNAcylation					1336:1350	DR5 O-GlcNAcylation	1332:1350	DR5 O-GlcNAcylation	1332:1350	We further defined that DR5 O-GlcNAcylation was independent of FADD, the adapter protein for the downstream death-inducing signaling.
31896813	4	39	attach	linked	525:530	arg1	cell					542:545	cancer cell growth and survival	535:565	cancer cell growth and survival	535:565	Elevated protein O-GlcNAcylation has been recently linked to cancer cell growth and survival.
31896813	4	39	attach	linked	525:530	arg2	O-GlcNAcylation					491:505	Elevated protein O-GlcNAcylation	474:505	Elevated protein O-GlcNAcylation	474:505	Elevated protein O-GlcNAcylation has been recently linked to cancer cell growth and survival.
31896813	0	40	theme	resistance	38:47	arg1	Regulation					0:9	Regulation	0:9	Regulation of pancreatic cancer TRAIL resistance by protein O-GlcNAcylation.	0:75	Regulation of pancreatic cancer TRAIL resistance by protein O-GlcNAcylation.
31896813	8	41	theme	O-GlcNAc	1226:1233	arg1	modifications					1235:1247	direct O-GlcNAc modifications	1219:1247	direct O-GlcNAc modifications	1219:1247	Mechanistic studies revealed direct O-GlcNAc modifications of DR5, which regulated TRA-8-induced DR5 oligomerization.
31896813	6	42	theme	TRA-8-induced	948:960	arg1	apoptosis					962:970	TRA-8-induced apoptosis	948:970	TRA-8-induced apoptosis	948:970	With gain- and loss-of-function of the O-GlcNAc-adding enzyme, O-GlcNActransferase (OGT), we determined that increasing O-GlcNAcylation rendered TRAIL-sensitive cells more resistant to TRA-8-induced apoptosis, while inhibiting O-GlcNAcylation promoted TRA-8-induced apoptosis in TRAIL-resistance cells.
31896813	2	43	theme	cancer	247:252	arg1	cells					254:258	many pancreatic cancer cells	231:258	many pancreatic cancer cells	231:258	However, many pancreatic cancer cells are resistant to TRAIL-induced apoptosis despite their expression of intact death receptors (DRs).
31896813	0	44	theme	TRAIL	32:36	arg1	resistance					38:47	pancreatic cancer TRAIL resistance	14:47	pancreatic cancer TRAIL resistance	14:47	Regulation of pancreatic cancer TRAIL resistance by protein O-GlcNAcylation.
31896813	10	45	theme	TRAIL	1533:1537	arg1	resistance					1539:1548	TRAIL resistance	1533:1548	TRAIL resistance of pancreatic cancer cells	1533:1575	These studies have demonstrated an important role of protein O-GlcNAcylation in regulating TRAIL resistance of pancreatic cancer cells; and uncovered the contribution of O-GlcNAcylation to DR5 oligomerization and thus mediating DR-inducing signaling.
31896813	3	46	theme	biological	452:461	arg1	processes					463:471	various biological processes	444:471	various biological processes	444:471	Protein O-GlcNAcylation is a versatile posttranslational modification that regulates various biological processes.
31896813	8	47	theme	TRA-8-induced	1273:1285	arg1	oligomerization					1291:1305	TRA-8-induced DR5 oligomerization	1273:1305	TRA-8-induced DR5 oligomerization	1273:1305	Mechanistic studies revealed direct O-GlcNAc modifications of DR5, which regulated TRA-8-induced DR5 oligomerization.
31896813	2	48	theme	pancreatic	236:245	arg1	cells					254:258	many pancreatic cancer cells	231:258	many pancreatic cancer cells	231:258	However, many pancreatic cancer cells are resistant to TRAIL-induced apoptosis despite their expression of intact death receptors (DRs).
31896813	7	49	theme	TRA-8	1150:1154	arg1	therapy					1156:1162	TRA-8 therapy	1150:1162	TRA-8 therapy in a mouse model	1150:1179	Furthermore, we demonstrated that OGT knockdown sensitized TRAIL-resistant cells to TRA-8 therapy in a mouse model in vivo.
31896813	7	50	from	therapy	1156:1162	arg1	model					1175:1179	a mouse model	1167:1179	a mouse model	1167:1179	Furthermore, we demonstrated that OGT knockdown sensitized TRAIL-resistant cells to TRA-8 therapy in a mouse model in vivo.
31896813	0	51	theme	protein	52:58	arg1	O-GlcNAcylation					60:74	protein O-GlcNAcylation	52:74	protein O-GlcNAcylation	52:74	Regulation of pancreatic cancer TRAIL resistance by protein O-GlcNAcylation.
31896813	1	52	with	neoplasm	192:199	arg1	prognosis					211:219	poor prognosis	206:219	poor prognosis	206:219	TRAIL-activating therapy is promising in treating various cancers, including pancreatic cancer, a highly malignant neoplasm with poor prognosis.
31896813	10	53	theme	cancer	1564:1569	arg1	cells					1571:1575	pancreatic cancer cells	1553:1575	pancreatic cancer cells	1553:1575	These studies have demonstrated an important role of protein O-GlcNAcylation in regulating TRAIL resistance of pancreatic cancer cells; and uncovered the contribution of O-GlcNAcylation to DR5 oligomerization and thus mediating DR-inducing signaling.
31896813	2	54	theme	many	231:234	arg1	cells					254:258	many pancreatic cancer cells	231:258	many pancreatic cancer cells	231:258	However, many pancreatic cancer cells are resistant to TRAIL-induced apoptosis despite their expression of intact death receptors (DRs).
31896813	10	55	theme	protein	1495:1501	arg1	O-GlcNAcylation					1503:1517	protein O-GlcNAcylation	1495:1517	protein O-GlcNAcylation	1495:1517	These studies have demonstrated an important role of protein O-GlcNAcylation in regulating TRAIL resistance of pancreatic cancer cells; and uncovered the contribution of O-GlcNAcylation to DR5 oligomerization and thus mediating DR-inducing signaling.
31896813	1	56	theme	various	127:133	arg1	cancer					165:170	pancreatic cancer	154:170	pancreatic cancer	154:170	TRAIL-activating therapy is promising in treating various cancers, including pancreatic cancer, a highly malignant neoplasm with poor prognosis.
31896813	1	56	theme	various	127:133	arg1	cancers					135:141	various cancers	127:141	various cancers	127:141	TRAIL-activating therapy is promising in treating various cancers, including pancreatic cancer, a highly malignant neoplasm with poor prognosis.
31896813	8	57	theme	direct	1219:1224	arg1	modifications					1235:1247	direct O-GlcNAc modifications	1219:1247	direct O-GlcNAc modifications	1219:1247	Mechanistic studies revealed direct O-GlcNAc modifications of DR5, which regulated TRA-8-induced DR5 oligomerization.
31896813	5	58	from	levels	693:698	arg1	cells					756:760	TRAIL-resistant pancreatic cancer cells	722:760	TRAIL-resistant pancreatic cancer cells	722:760	In this study, we evaluated the role of protein O-GlcNAcylation in pancreatic cancer TRAIL resistance, and identified higher levels of O-GlcNAcylation in TRAIL-resistant pancreatic cancer cells.
31896813	5	59	theme	pancreatic	738:747	arg1	cells					756:760	TRAIL-resistant pancreatic cancer cells	722:760	TRAIL-resistant pancreatic cancer cells	722:760	In this study, we evaluated the role of protein O-GlcNAcylation in pancreatic cancer TRAIL resistance, and identified higher levels of O-GlcNAcylation in TRAIL-resistant pancreatic cancer cells.
31896813	8	60	mod	modifications	1235:1247	arg1	DR5					1252:1254	DR5	1252:1254	DR5	1252:1254	Mechanistic studies revealed direct O-GlcNAc modifications of DR5, which regulated TRA-8-induced DR5 oligomerization.
31896813	8	60	mod	modifications	1235:1247	arg3	O-GlcNAc					1226:1233	direct O-GlcNAc modifications	1219:1247	direct O-GlcNAc modifications	1219:1247	Mechanistic studies revealed direct O-GlcNAc modifications of DR5, which regulated TRA-8-induced DR5 oligomerization.
31896813	6	61	theme	TRAIL-resistance	1042:1057	arg1	cells					1059:1063	TRAIL-resistance cells	1042:1063	TRAIL-resistance cells	1042:1063	With gain- and loss-of-function of the O-GlcNAc-adding enzyme, O-GlcNActransferase (OGT), we determined that increasing O-GlcNAcylation rendered TRAIL-sensitive cells more resistant to TRA-8-induced apoptosis, while inhibiting O-GlcNAcylation promoted TRA-8-induced apoptosis in TRAIL-resistance cells.
31896813	5	62	theme	cancer	749:754	arg1	cells					756:760	TRAIL-resistant pancreatic cancer cells	722:760	TRAIL-resistant pancreatic cancer cells	722:760	In this study, we evaluated the role of protein O-GlcNAcylation in pancreatic cancer TRAIL resistance, and identified higher levels of O-GlcNAcylation in TRAIL-resistant pancreatic cancer cells.
31896813	6	63	theme	enzyme	818:823	arg1	loss-of-function					778:793	loss-of-function	778:793	loss-of-function	778:793	With gain- and loss-of-function of the O-GlcNAc-adding enzyme, O-GlcNActransferase (OGT), we determined that increasing O-GlcNAcylation rendered TRAIL-sensitive cells more resistant to TRA-8-induced apoptosis, while inhibiting O-GlcNAcylation promoted TRA-8-induced apoptosis in TRAIL-resistance cells.
31896813	6	63	theme	enzyme	818:823	arg1	gain-					768:772	gain-	768:772	gain-	768:772	With gain- and loss-of-function of the O-GlcNAc-adding enzyme, O-GlcNActransferase (OGT), we determined that increasing O-GlcNAcylation rendered TRAIL-sensitive cells more resistant to TRA-8-induced apoptosis, while inhibiting O-GlcNAcylation promoted TRA-8-induced apoptosis in TRAIL-resistance cells.
31896813	10	64	theme	pancreatic	1553:1562	arg1	cells					1571:1575	pancreatic cancer cells	1553:1575	pancreatic cancer cells	1553:1575	These studies have demonstrated an important role of protein O-GlcNAcylation in regulating TRAIL resistance of pancreatic cancer cells; and uncovered the contribution of O-GlcNAcylation to DR5 oligomerization and thus mediating DR-inducing signaling.
31896813	8	65	theme	DR5	1252:1254	arg1	modifications					1235:1247	direct O-GlcNAc modifications	1219:1247	direct O-GlcNAc modifications	1219:1247	Mechanistic studies revealed direct O-GlcNAc modifications of DR5, which regulated TRA-8-induced DR5 oligomerization.
31896813	4	66	theme	protein	483:489	arg1	O-GlcNAcylation					491:505	Elevated protein O-GlcNAcylation	474:505	Elevated protein O-GlcNAcylation	474:505	Elevated protein O-GlcNAcylation has been recently linked to cancer cell growth and survival.
31896813	10	67	theme	O-GlcNAcylation	1503:1517	arg1	role					1487:1490	an important role	1474:1490	an important role of protein O-GlcNAcylation in regulating TRAIL resistance of pancreatic cancer cells	1474:1575	These studies have demonstrated an important role of protein O-GlcNAcylation in regulating TRAIL resistance of pancreatic cancer cells; and uncovered the contribution of O-GlcNAcylation to DR5 oligomerization and thus mediating DR-inducing signaling.
31896813	6	68	theme	O-GlcNAc-adding	802:816	arg1	O-GlcNActransferase					826:844	O-GlcNActransferase	826:844	O-GlcNActransferase (OGT)	826:850	With gain- and loss-of-function of the O-GlcNAc-adding enzyme, O-GlcNActransferase (OGT), we determined that increasing O-GlcNAcylation rendered TRAIL-sensitive cells more resistant to TRA-8-induced apoptosis, while inhibiting O-GlcNAcylation promoted TRA-8-induced apoptosis in TRAIL-resistance cells.
31896813	6	68	theme	O-GlcNAc-adding	802:816	arg1	enzyme					818:823	the O-GlcNAc-adding enzyme	798:823	the O-GlcNAc-adding enzyme	798:823	With gain- and loss-of-function of the O-GlcNAc-adding enzyme, O-GlcNActransferase (OGT), we determined that increasing O-GlcNAcylation rendered TRAIL-sensitive cells more resistant to TRA-8-induced apoptosis, while inhibiting O-GlcNAcylation promoted TRA-8-induced apoptosis in TRAIL-resistance cells.
31896813	2	69	theme	receptors	342:350	arg1	expression					315:324	their expression	309:324	their expression of intact death receptors (DRs)	309:356	However, many pancreatic cancer cells are resistant to TRAIL-induced apoptosis despite their expression of intact death receptors (DRs).
31896813	4	70	theme	Elevated	474:481	arg1	O-GlcNAcylation					491:505	Elevated protein O-GlcNAcylation	474:505	Elevated protein O-GlcNAcylation	474:505	Elevated protein O-GlcNAcylation has been recently linked to cancer cell growth and survival.
31896813	7	71	theme	mouse	1169:1173	arg1	model					1175:1179	a mouse model	1167:1179	a mouse model	1167:1179	Furthermore, we demonstrated that OGT knockdown sensitized TRAIL-resistant cells to TRA-8 therapy in a mouse model in vivo.
31896813	7	72	theme	TRAIL-resistant	1125:1139	arg1	cells					1141:1145	TRAIL-resistant cells	1125:1145	TRAIL-resistant cells	1125:1145	Furthermore, we demonstrated that OGT knockdown sensitized TRAIL-resistant cells to TRA-8 therapy in a mouse model in vivo.
31896813	1	73	theme	pancreatic	154:163	arg1	neoplasm					192:199	a highly malignant neoplasm	173:199	a highly malignant neoplasm with poor prognosis	173:219	TRAIL-activating therapy is promising in treating various cancers, including pancreatic cancer, a highly malignant neoplasm with poor prognosis.
31896813	1	73	theme	pancreatic	154:163	arg1	cancer					165:170	pancreatic cancer	154:170	pancreatic cancer	154:170	TRAIL-activating therapy is promising in treating various cancers, including pancreatic cancer, a highly malignant neoplasm with poor prognosis.
31896813	0	74	theme	pancreatic	14:23	arg1	resistance					38:47	pancreatic cancer TRAIL resistance	14:47	pancreatic cancer TRAIL resistance	14:47	Regulation of pancreatic cancer TRAIL resistance by protein O-GlcNAcylation.
31896813	7	75	theme	OGT	1100:1102	arg1	knockdown					1104:1112	OGT knockdown	1100:1112	OGT knockdown	1100:1112	Furthermore, we demonstrated that OGT knockdown sensitized TRAIL-resistant cells to TRA-8 therapy in a mouse model in vivo.
35083852	0	0	theme	pro-survival	84:95	arg1	activity					45:52	fatty acid synthase activity	25:52	fatty acid synthase activity	25:52	O-GlcNAcylation promotes fatty acid synthase activity under nutritional stress as a pro-survival mechanism in cancer cells.
35083852	0	0	theme	pro-survival	84:95	arg1	mechanism					97:105	a pro-survival mechanism	82:105	a pro-survival mechanism in cancer cells	82:121	O-GlcNAcylation promotes fatty acid synthase activity under nutritional stress as a pro-survival mechanism in cancer cells.
35083852	6	1	theme	synthesis	926:934	arg1	activity					942:949	enhanced de novo fatty acid synthesis (FAS) activity	898:949	enhanced de novo fatty acid synthesis (FAS) activity	898:949	O-GlcNAcylation led to enhanced de novo fatty acid synthesis (FAS) activity, and fatty acids contributed to the cytoprotective effects of O-GlcNAcylation under starvation.
35083852	3	2	from	role	440:443	arg1	response					478:485	the stress response	467:485	the stress response	467:485	Despite its ubiquity and importance, the current understanding of the role of O-GlcNAcylation in the stress response remains limited.
35083852	2	3	theme	cancer	352:357	arg1	pathology					359:367	cancer pathology	352:367	cancer pathology	352:367	O-GlcNAcylation is known to be deregulated in cancer and has been linked to multiple aspects of cancer pathology.
35083852	4	4	from	study	578:582	arg1	cells					611:615	HeLa cells	606:615	HeLa cells	606:615	In this study, we performed a quantitative chemical proteomics-based open study of the O-GlcNAcome in HeLa cells, and identified 163 differentially-glycosylated proteins under starvation, involving multiple metabolic pathways.
35083852	6	5	theme	acid	921:924	arg1	FAS					937:939	FAS	937:939	FAS	937:939	O-GlcNAcylation led to enhanced de novo fatty acid synthesis (FAS) activity, and fatty acids contributed to the cytoprotective effects of O-GlcNAcylation under starvation.
35083852	6	5	theme	acid	921:924	arg1	synthesis					926:934	de novo fatty acid synthesis	907:934	enhanced de novo fatty acid synthesis (FAS) activity	898:949	O-GlcNAcylation led to enhanced de novo fatty acid synthesis (FAS) activity, and fatty acids contributed to the cytoprotective effects of O-GlcNAcylation under starvation.
35083852	4	6	theme	metabolic	711:719	arg1	pathways					721:728	multiple metabolic pathways	702:728	multiple metabolic pathways	702:728	In this study, we performed a quantitative chemical proteomics-based open study of the O-GlcNAcome in HeLa cells, and identified 163 differentially-glycosylated proteins under starvation, involving multiple metabolic pathways.
35083852	6	7	theme	cytoprotective	987:1000	arg1	effects					1002:1008	the cytoprotective effects	983:1008	the cytoprotective effects of O-GlcNAcylation under starvation	983:1044	O-GlcNAcylation led to enhanced de novo fatty acid synthesis (FAS) activity, and fatty acids contributed to the cytoprotective effects of O-GlcNAcylation under starvation.
35083852	4	8	from	O-GlcNAcome	591:601	arg1	cells					611:615	HeLa cells	606:615	HeLa cells	606:615	In this study, we performed a quantitative chemical proteomics-based open study of the O-GlcNAcome in HeLa cells, and identified 163 differentially-glycosylated proteins under starvation, involving multiple metabolic pathways.
35083852	6	9	theme	fatty	915:919	arg1	FAS					937:939	FAS	937:939	FAS	937:939	O-GlcNAcylation led to enhanced de novo fatty acid synthesis (FAS) activity, and fatty acids contributed to the cytoprotective effects of O-GlcNAcylation under starvation.
35083852	6	9	theme	fatty	915:919	arg1	synthesis					926:934	de novo fatty acid synthesis	907:934	enhanced de novo fatty acid synthesis (FAS) activity	898:949	O-GlcNAcylation led to enhanced de novo fatty acid synthesis (FAS) activity, and fatty acids contributed to the cytoprotective effects of O-GlcNAcylation under starvation.
35083852	7	10	theme	synergistic	1120:1130	arg1	effect					1132:1137	a strong synergistic effect	1111:1137	a strong synergistic effect	1111:1137	Moreover, dual inhibition of O-GlcNAcylation and FASN displayed a strong synergistic effect in vitro in inducing cell death in cancer cells.
35083852	8	11	from	role	1258:1261	arg1	response					1308:1315	the nutritional stress response	1285:1315	the nutritional stress response	1285:1315	Together, the results from this study provide novel insights into the role of O-GlcNAcylation in the nutritional stress response and suggest the potential of combining inhibition of O-GlcNAcylation and FAS in cancer therapy.
35083852	4	12	theme	O-GlcNAcome	591:601	arg1	study					578:582	a quantitative chemical proteomics-based open study	532:582	a quantitative chemical proteomics-based open study of the O-GlcNAcome in HeLa cells	532:615	In this study, we performed a quantitative chemical proteomics-based open study of the O-GlcNAcome in HeLa cells, and identified 163 differentially-glycosylated proteins under starvation, involving multiple metabolic pathways.
35083852	5	13	theme	acid	749:752	arg1	metabolism					754:763	fatty acid metabolism	743:763	fatty acid metabolism	743:763	Among them, fatty acid metabolism was found to be targeted and subsequent analysis confirmed that fatty acid synthase (FASN) is O-GlcNAcylated.
35083852	8	14	theme	stress	1301:1306	arg1	response					1308:1315	the nutritional stress response	1285:1315	the nutritional stress response	1285:1315	Together, the results from this study provide novel insights into the role of O-GlcNAcylation in the nutritional stress response and suggest the potential of combining inhibition of O-GlcNAcylation and FAS in cancer therapy.
35083852	6	15	theme	de	907:908	arg1	FAS					937:939	FAS	937:939	FAS	937:939	O-GlcNAcylation led to enhanced de novo fatty acid synthesis (FAS) activity, and fatty acids contributed to the cytoprotective effects of O-GlcNAcylation under starvation.
35083852	6	15	theme	de	907:908	arg1	synthesis					926:934	de novo fatty acid synthesis	907:934	enhanced de novo fatty acid synthesis (FAS) activity	898:949	O-GlcNAcylation led to enhanced de novo fatty acid synthesis (FAS) activity, and fatty acids contributed to the cytoprotective effects of O-GlcNAcylation under starvation.
35083852	7	16	theme	cancer	1174:1179	arg1	cells					1181:1185	cancer cells	1174:1185	cancer cells	1174:1185	Moreover, dual inhibition of O-GlcNAcylation and FASN displayed a strong synergistic effect in vitro in inducing cell death in cancer cells.
35083852	8	17	from	FAS	1390:1392	arg1	therapy					1404:1410	cancer therapy	1397:1410	cancer therapy	1397:1410	Together, the results from this study provide novel insights into the role of O-GlcNAcylation in the nutritional stress response and suggest the potential of combining inhibition of O-GlcNAcylation and FAS in cancer therapy.
35083852	1	18	theme	protein	170:176	arg1	glycosylation					178:190	protein glycosylation	170:190	protein glycosylation	170:190	Protein O-GlcNAcylation is a specific form of protein glycosylation that targets a wide range of proteins with important functions.
35083852	0	19	theme	cancer	110:115	arg1	cells					117:121	cancer cells	110:121	cancer cells	110:121	O-GlcNAcylation promotes fatty acid synthase activity under nutritional stress as a pro-survival mechanism in cancer cells.
35083852	2	20	attach	linked	322:327	arg2	O-GlcNAcylation					256:270	O-GlcNAcylation	256:270	O-GlcNAcylation	256:270	O-GlcNAcylation is known to be deregulated in cancer and has been linked to multiple aspects of cancer pathology.
35083852	2	20	attach	linked	322:327	arg1	aspects					341:347	multiple aspects	332:347	multiple aspects of cancer pathology	332:367	O-GlcNAcylation is known to be deregulated in cancer and has been linked to multiple aspects of cancer pathology.
35083852	7	21	theme	strong	1113:1118	arg1	effect					1132:1137	a strong synergistic effect	1111:1137	a strong synergistic effect	1111:1137	Moreover, dual inhibition of O-GlcNAcylation and FASN displayed a strong synergistic effect in vitro in inducing cell death in cancer cells.
35083852	8	22	from	therapy	1404:1410	arg1	inhibition					1356:1365	inhibition	1356:1365	inhibition of O-GlcNAcylation and FAS in cancer therapy	1356:1410	Together, the results from this study provide novel insights into the role of O-GlcNAcylation in the nutritional stress response and suggest the potential of combining inhibition of O-GlcNAcylation and FAS in cancer therapy.
35083852	1	23	theme	glycosylation	178:190	arg1	O-GlcNAcylation					132:146	Protein O-GlcNAcylation	124:146	Protein O-GlcNAcylation	124:146	Protein O-GlcNAcylation is a specific form of protein glycosylation that targets a wide range of proteins with important functions.
35083852	1	23	theme	glycosylation	178:190	arg1	form					162:165	a specific form	151:165	a specific form of protein glycosylation that targets a wide range of proteins with important functions	151:253	Protein O-GlcNAcylation is a specific form of protein glycosylation that targets a wide range of proteins with important functions.
35083852	4	24	theme	proteomics-based	556:571	arg1	study					578:582	a quantitative chemical proteomics-based open study	532:582	a quantitative chemical proteomics-based open study of the O-GlcNAcome in HeLa cells	532:615	In this study, we performed a quantitative chemical proteomics-based open study of the O-GlcNAcome in HeLa cells, and identified 163 differentially-glycosylated proteins under starvation, involving multiple metabolic pathways.
35083852	7	25	theme	FASN	1096:1099	arg1	inhibition					1062:1071	dual inhibition	1057:1071	dual inhibition of O-GlcNAcylation and FASN	1057:1099	Moreover, dual inhibition of O-GlcNAcylation and FASN displayed a strong synergistic effect in vitro in inducing cell death in cancer cells.
35083852	3	26	from	response	478:485	arg1	understanding					419:431	the current understanding	407:431	the current understanding of the role of O-GlcNAcylation in the stress response	407:485	Despite its ubiquity and importance, the current understanding of the role of O-GlcNAcylation in the stress response remains limited.
35083852	8	27	from	study	1220:1224	arg1	results					1202:1208	the results	1198:1208	the results from this study	1198:1224	Together, the results from this study provide novel insights into the role of O-GlcNAcylation in the nutritional stress response and suggest the potential of combining inhibition of O-GlcNAcylation and FAS in cancer therapy.
35083852	6	28	theme	fatty	956:960	arg1	acids					962:966	fatty acids	956:966	fatty acids	956:966	O-GlcNAcylation led to enhanced de novo fatty acid synthesis (FAS) activity, and fatty acids contributed to the cytoprotective effects of O-GlcNAcylation under starvation.
35083852	5	29	theme	fatty	829:833	arg1	FASN					850:853	FASN	850:853	FASN	850:853	Among them, fatty acid metabolism was found to be targeted and subsequent analysis confirmed that fatty acid synthase (FASN) is O-GlcNAcylated.
35083852	5	29	theme	fatty	829:833	arg1	synthase					840:847	fatty acid synthase	829:847	fatty acid synthase (FASN)	829:854	Among them, fatty acid metabolism was found to be targeted and subsequent analysis confirmed that fatty acid synthase (FASN) is O-GlcNAcylated.
35083852	4	30	theme	chemical	547:554	arg1	study					578:582	a quantitative chemical proteomics-based open study	532:582	a quantitative chemical proteomics-based open study of the O-GlcNAcome in HeLa cells	532:615	In this study, we performed a quantitative chemical proteomics-based open study of the O-GlcNAcome in HeLa cells, and identified 163 differentially-glycosylated proteins under starvation, involving multiple metabolic pathways.
35083852	4	31	gly	differentially-glycosylated	637:663	arg1	proteins					665:672	163 differentially-glycosylated proteins	633:672	163 differentially-glycosylated proteins under starvation	633:689	In this study, we performed a quantitative chemical proteomics-based open study of the O-GlcNAcome in HeLa cells, and identified 163 differentially-glycosylated proteins under starvation, involving multiple metabolic pathways.
35083852	8	32	theme	O-GlcNAcylation	1370:1384	arg1	inhibition					1356:1365	inhibition	1356:1365	inhibition of O-GlcNAcylation and FAS in cancer therapy	1356:1410	Together, the results from this study provide novel insights into the role of O-GlcNAcylation in the nutritional stress response and suggest the potential of combining inhibition of O-GlcNAcylation and FAS in cancer therapy.
35083852	0	33	theme	acid	31:34	arg1	synthase					36:43	fatty acid synthase	25:43	fatty acid synthase activity	25:52	O-GlcNAcylation promotes fatty acid synthase activity under nutritional stress as a pro-survival mechanism in cancer cells.
35083852	4	34	theme	quantitative	534:545	arg1	study					578:582	a quantitative chemical proteomics-based open study	532:582	a quantitative chemical proteomics-based open study of the O-GlcNAcome in HeLa cells	532:615	In this study, we performed a quantitative chemical proteomics-based open study of the O-GlcNAcome in HeLa cells, and identified 163 differentially-glycosylated proteins under starvation, involving multiple metabolic pathways.
35083852	7	35	theme	O-GlcNAcylation	1076:1090	arg1	inhibition					1062:1071	dual inhibition	1057:1071	dual inhibition of O-GlcNAcylation and FASN	1057:1099	Moreover, dual inhibition of O-GlcNAcylation and FASN displayed a strong synergistic effect in vitro in inducing cell death in cancer cells.
35083852	2	36	gly	O-GlcNAcylation	256:270	arg1	cancer					302:307	cancer	302:307	cancer	302:307	O-GlcNAcylation is known to be deregulated in cancer and has been linked to multiple aspects of cancer pathology.
35083852	4	37	theme	open	573:576	arg1	study					578:582	a quantitative chemical proteomics-based open study	532:582	a quantitative chemical proteomics-based open study of the O-GlcNAcome in HeLa cells	532:615	In this study, we performed a quantitative chemical proteomics-based open study of the O-GlcNAcome in HeLa cells, and identified 163 differentially-glycosylated proteins under starvation, involving multiple metabolic pathways.
35083852	4	38	theme	HeLa	606:609	arg1	cells					611:615	HeLa cells	606:615	HeLa cells	606:615	In this study, we performed a quantitative chemical proteomics-based open study of the O-GlcNAcome in HeLa cells, and identified 163 differentially-glycosylated proteins under starvation, involving multiple metabolic pathways.
35083852	8	39	theme	FAS	1390:1392	arg1	inhibition					1356:1365	inhibition	1356:1365	inhibition of O-GlcNAcylation and FAS in cancer therapy	1356:1410	Together, the results from this study provide novel insights into the role of O-GlcNAcylation in the nutritional stress response and suggest the potential of combining inhibition of O-GlcNAcylation and FAS in cancer therapy.
35083852	1	40	theme	wide	207:210	arg1	range					212:216	a wide range	205:216	a wide range of proteins with important functions	205:253	Protein O-GlcNAcylation is a specific form of protein glycosylation that targets a wide range of proteins with important functions.
35083852	7	41	theme	cell	1160:1163	arg1	death					1165:1169	cell death	1160:1169	cell death	1160:1169	Moreover, dual inhibition of O-GlcNAcylation and FASN displayed a strong synergistic effect in vitro in inducing cell death in cancer cells.
35083852	2	42	theme	multiple	332:339	arg1	aspects					341:347	multiple aspects	332:347	multiple aspects of cancer pathology	332:367	O-GlcNAcylation is known to be deregulated in cancer and has been linked to multiple aspects of cancer pathology.
35083852	8	43	from	O-GlcNAcylation	1370:1384	arg1	therapy					1404:1410	cancer therapy	1397:1410	cancer therapy	1397:1410	Together, the results from this study provide novel insights into the role of O-GlcNAcylation in the nutritional stress response and suggest the potential of combining inhibition of O-GlcNAcylation and FAS in cancer therapy.
35083852	4	44	theme	differentially-glycosylated	637:663	arg1	proteins					665:672	163 differentially-glycosylated proteins	633:672	163 differentially-glycosylated proteins under starvation	633:689	In this study, we performed a quantitative chemical proteomics-based open study of the O-GlcNAcome in HeLa cells, and identified 163 differentially-glycosylated proteins under starvation, involving multiple metabolic pathways.
35083852	0	45	theme	synthase	36:43	arg1	activity					45:52	fatty acid synthase activity	25:52	fatty acid synthase activity	25:52	O-GlcNAcylation promotes fatty acid synthase activity under nutritional stress as a pro-survival mechanism in cancer cells.
35083852	0	45	theme	synthase	36:43	arg1	mechanism					97:105	a pro-survival mechanism	82:105	a pro-survival mechanism in cancer cells	82:121	O-GlcNAcylation promotes fatty acid synthase activity under nutritional stress as a pro-survival mechanism in cancer cells.
35083852	3	46	theme	current	411:417	arg1	understanding					419:431	the current understanding	407:431	the current understanding of the role of O-GlcNAcylation in the stress response	407:485	Despite its ubiquity and importance, the current understanding of the role of O-GlcNAcylation in the stress response remains limited.
35083852	5	47	theme	acid	835:838	arg1	FASN					850:853	FASN	850:853	FASN	850:853	Among them, fatty acid metabolism was found to be targeted and subsequent analysis confirmed that fatty acid synthase (FASN) is O-GlcNAcylated.
35083852	5	47	theme	acid	835:838	arg1	synthase					840:847	fatty acid synthase	829:847	fatty acid synthase (FASN)	829:854	Among them, fatty acid metabolism was found to be targeted and subsequent analysis confirmed that fatty acid synthase (FASN) is O-GlcNAcylated.
35083852	3	48	theme	O-GlcNAcylation	448:462	arg1	role					440:443	the role	436:443	the role of O-GlcNAcylation in the stress response	436:485	Despite its ubiquity and importance, the current understanding of the role of O-GlcNAcylation in the stress response remains limited.
35083852	0	49	theme	nutritional	60:70	arg1	stress					72:77	nutritional stress	60:77	nutritional stress	60:77	O-GlcNAcylation promotes fatty acid synthase activity under nutritional stress as a pro-survival mechanism in cancer cells.
35083852	5	50	theme	fatty	743:747	arg1	metabolism					754:763	fatty acid metabolism	743:763	fatty acid metabolism	743:763	Among them, fatty acid metabolism was found to be targeted and subsequent analysis confirmed that fatty acid synthase (FASN) is O-GlcNAcylated.
35083852	6	51	theme	enhanced	898:905	arg1	activity					942:949	enhanced de novo fatty acid synthesis (FAS) activity	898:949	enhanced de novo fatty acid synthesis (FAS) activity	898:949	O-GlcNAcylation led to enhanced de novo fatty acid synthesis (FAS) activity, and fatty acids contributed to the cytoprotective effects of O-GlcNAcylation under starvation.
35083852	8	52	theme	nutritional	1289:1299	arg1	response					1308:1315	the nutritional stress response	1285:1315	the nutritional stress response	1285:1315	Together, the results from this study provide novel insights into the role of O-GlcNAcylation in the nutritional stress response and suggest the potential of combining inhibition of O-GlcNAcylation and FAS in cancer therapy.
35083852	7	53	theme	dual	1057:1060	arg1	inhibition					1062:1071	dual inhibition	1057:1071	dual inhibition of O-GlcNAcylation and FASN	1057:1099	Moreover, dual inhibition of O-GlcNAcylation and FASN displayed a strong synergistic effect in vitro in inducing cell death in cancer cells.
35083852	1	54	theme	Protein	124:130	arg1	O-GlcNAcylation					132:146	Protein O-GlcNAcylation	124:146	Protein O-GlcNAcylation	124:146	Protein O-GlcNAcylation is a specific form of protein glycosylation that targets a wide range of proteins with important functions.
35083852	1	54	theme	Protein	124:130	arg1	form					162:165	a specific form	151:165	a specific form of protein glycosylation that targets a wide range of proteins with important functions	151:253	Protein O-GlcNAcylation is a specific form of protein glycosylation that targets a wide range of proteins with important functions.
35083852	6	55	theme	O-GlcNAcylation	1013:1027	arg1	effects					1002:1008	the cytoprotective effects	983:1008	the cytoprotective effects of O-GlcNAcylation under starvation	983:1044	O-GlcNAcylation led to enhanced de novo fatty acid synthesis (FAS) activity, and fatty acids contributed to the cytoprotective effects of O-GlcNAcylation under starvation.
35083852	5	56	theme	subsequent	794:803	arg1	analysis					805:812	subsequent analysis	794:812	subsequent analysis	794:812	Among them, fatty acid metabolism was found to be targeted and subsequent analysis confirmed that fatty acid synthase (FASN) is O-GlcNAcylated.
35083852	8	57	theme	cancer	1397:1402	arg1	therapy					1404:1410	cancer therapy	1397:1410	cancer therapy	1397:1410	Together, the results from this study provide novel insights into the role of O-GlcNAcylation in the nutritional stress response and suggest the potential of combining inhibition of O-GlcNAcylation and FAS in cancer therapy.
35083852	3	58	theme	stress	471:476	arg1	response					478:485	the stress response	467:485	the stress response	467:485	Despite its ubiquity and importance, the current understanding of the role of O-GlcNAcylation in the stress response remains limited.
35083852	8	59	from	inhibition	1356:1365	arg1	therapy					1404:1410	cancer therapy	1397:1410	cancer therapy	1397:1410	Together, the results from this study provide novel insights into the role of O-GlcNAcylation in the nutritional stress response and suggest the potential of combining inhibition of O-GlcNAcylation and FAS in cancer therapy.
35083852	1	60	theme	proteins	221:228	arg1	range					212:216	a wide range	205:216	a wide range of proteins with important functions	205:253	Protein O-GlcNAcylation is a specific form of protein glycosylation that targets a wide range of proteins with important functions.
35083852	3	61	from	understanding	419:431	arg1	response					478:485	the stress response	467:485	the stress response	467:485	Despite its ubiquity and importance, the current understanding of the role of O-GlcNAcylation in the stress response remains limited.
35083852	1	62	theme	specific	153:160	arg1	O-GlcNAcylation					132:146	Protein O-GlcNAcylation	124:146	Protein O-GlcNAcylation	124:146	Protein O-GlcNAcylation is a specific form of protein glycosylation that targets a wide range of proteins with important functions.
35083852	1	62	theme	specific	153:160	arg1	form					162:165	a specific form	151:165	a specific form of protein glycosylation that targets a wide range of proteins with important functions	151:253	Protein O-GlcNAcylation is a specific form of protein glycosylation that targets a wide range of proteins with important functions.
35083852	0	63	from	mechanism	97:105	arg1	cells					117:121	cancer cells	110:121	cancer cells	110:121	O-GlcNAcylation promotes fatty acid synthase activity under nutritional stress as a pro-survival mechanism in cancer cells.
35083852	8	64	theme	O-GlcNAcylation	1266:1280	arg1	role					1258:1261	the role	1254:1261	the role of O-GlcNAcylation in the nutritional stress response	1254:1315	Together, the results from this study provide novel insights into the role of O-GlcNAcylation in the nutritional stress response and suggest the potential of combining inhibition of O-GlcNAcylation and FAS in cancer therapy.
35083852	4	65	theme	multiple	702:709	arg1	pathways					721:728	multiple metabolic pathways	702:728	multiple metabolic pathways	702:728	In this study, we performed a quantitative chemical proteomics-based open study of the O-GlcNAcome in HeLa cells, and identified 163 differentially-glycosylated proteins under starvation, involving multiple metabolic pathways.
35083852	3	66	theme	role	440:443	arg1	understanding					419:431	the current understanding	407:431	the current understanding of the role of O-GlcNAcylation in the stress response	407:485	Despite its ubiquity and importance, the current understanding of the role of O-GlcNAcylation in the stress response remains limited.
35083852	1	67	theme	important	235:243	arg1	functions					245:253	important functions	235:253	important functions	235:253	Protein O-GlcNAcylation is a specific form of protein glycosylation that targets a wide range of proteins with important functions.
35083852	4	68	from	cells	611:615	arg1	study					578:582	a quantitative chemical proteomics-based open study	532:582	a quantitative chemical proteomics-based open study of the O-GlcNAcome in HeLa cells	532:615	In this study, we performed a quantitative chemical proteomics-based open study of the O-GlcNAcome in HeLa cells, and identified 163 differentially-glycosylated proteins under starvation, involving multiple metabolic pathways.
35083852	8	69	theme	novel	1234:1238	arg1	insights					1240:1247	novel insights	1234:1247	novel insights into the role of O-GlcNAcylation in the nutritional stress response	1234:1315	Together, the results from this study provide novel insights into the role of O-GlcNAcylation in the nutritional stress response and suggest the potential of combining inhibition of O-GlcNAcylation and FAS in cancer therapy.
35083852	0	70	theme	fatty	25:29	arg1	synthase					36:43	fatty acid synthase	25:43	fatty acid synthase activity	25:52	O-GlcNAcylation promotes fatty acid synthase activity under nutritional stress as a pro-survival mechanism in cancer cells.
35083852	1	71	with	proteins	221:228	arg1	functions					245:253	important functions	235:253	important functions	235:253	Protein O-GlcNAcylation is a specific form of protein glycosylation that targets a wide range of proteins with important functions.
35083852	2	72	theme	pathology	359:367	arg1	aspects					341:347	multiple aspects	332:347	multiple aspects of cancer pathology	332:367	O-GlcNAcylation is known to be deregulated in cancer and has been linked to multiple aspects of cancer pathology.
35083852	6	73	dep	de	907:908	arg1	novo					910:913	novo	910:913	novo	910:913	O-GlcNAcylation led to enhanced de novo fatty acid synthesis (FAS) activity, and fatty acids contributed to the cytoprotective effects of O-GlcNAcylation under starvation.
26374642	1	0	theme	regional	243:250	arg1	nodes					258:262	regional lymph nodes	243:262	regional lymph nodes	243:262	The potential role of protein O-GlcNAcylation in cancer has been studied extensively, and the spread of cancer cells to regional lymph nodes is the first step in the dissemination of breast cancer.
26374642	8	1	theme	several	1379:1385	arg1	proteins					1402:1409	several O-GlcNAcylated proteins	1379:1409	several O-GlcNAcylated proteins involved in glycolysis and its accessory pathway	1379:1458	Moreover, several O-GlcNAcylated proteins involved in glycolysis and its accessory pathway were identified from LNM and non-LNM groups, respectively.
26374642	1	2	from	step	277:280	arg1	dissemination					289:301	the dissemination	285:301	the dissemination of breast cancer	285:318	The potential role of protein O-GlcNAcylation in cancer has been studied extensively, and the spread of cancer cells to regional lymph nodes is the first step in the dissemination of breast cancer.
26374642	3	3	dep	augmentation	568:579	arg1	response					552:559	response	552:559	response	552:559	In this study, we demonstrated that the overall O-GlcNAcylation as well as O-GlcNAc transferase (OGT) tends to decrease in response to the augmentation of lymph node metastasis (LNM) in invasive ductal breast carcinomas (IDCs).
26374642	2	4	from	correlation	334:344	arg1	cancer					405:410	breast cancer	398:410	breast cancer	398:410	However, the correlation between O-GlcNAcylation and lymphatic metastasis in breast cancer remains elusive.
26374642	8	5	theme	LNM	1481:1483	arg1	groups					1497:1502	LNM and non-LNM groups	1481:1502	groups	1497:1502	Moreover, several O-GlcNAcylated proteins involved in glycolysis and its accessory pathway were identified from LNM and non-LNM groups, respectively.
26374642	4	6	theme	accumulating	666:677	arg1	evidence					679:686	accumulating evidence	666:686	accumulating evidence	666:686	Although accumulating evidence indicates that individual O-GlcNAcylation may be important in the pathogenesis of breast cancer, O-GlcNAcylated proteins in IDCs are still largely unexplored.
26374642	8	7	theme	non-LNM	1489:1495	arg1	groups					1497:1502	LNM and non-LNM groups	1481:1502	groups	1497:1502	Moreover, several O-GlcNAcylated proteins involved in glycolysis and its accessory pathway were identified from LNM and non-LNM groups, respectively.
26374642	10	8	mod	modification	1711:1722	arg1	proteins					1733:1740	these proteins	1727:1740	these proteins	1727:1740	Aberrant O-GlcNAc modification of these proteins might be associated with LNM progression.
26374642	10	8	mod	modification	1711:1722	arg3	O-GlcNAc					1702:1709	Aberrant O-GlcNAc modification	1693:1722	Aberrant O-GlcNAc modification of these proteins	1693:1740	Aberrant O-GlcNAc modification of these proteins might be associated with LNM progression.
26374642	3	9	theme	metastasis	595:604	arg1	augmentation					568:579	the augmentation	564:579	the augmentation of lymph node metastasis (LNM) in invasive ductal breast carcinomas (IDCs)	564:654	In this study, we demonstrated that the overall O-GlcNAcylation as well as O-GlcNAc transferase (OGT) tends to decrease in response to the augmentation of lymph node metastasis (LNM) in invasive ductal breast carcinomas (IDCs).
26374642	6	10	located	observed	1079:1086	arg2	proteins					1031:1038	155 O-GlcNAcylated proteins	1012:1038	155 O-GlcNAcylated proteins	1012:1038	In total, 155 O-GlcNAcylated proteins were determined, of which 41 were only observed in LNM tissues, while 40 were unique in non-LNM samples.
26374642	6	10	located	observed	1079:1086	arg2	41					1066:1067	41	1066:1067	41	1066:1067	In total, 155 O-GlcNAcylated proteins were determined, of which 41 were only observed in LNM tissues, while 40 were unique in non-LNM samples.
26374642	6	10	located	observed	1079:1086	arg1	tissues					1095:1101	LNM tissues	1091:1101	LNM tissues	1091:1101	In total, 155 O-GlcNAcylated proteins were determined, of which 41 were only observed in LNM tissues, while 40 were unique in non-LNM samples.
26374642	6	11	theme	O-GlcNAcylated	1016:1029	arg1	proteins					1031:1038	155 O-GlcNAcylated proteins	1012:1038	155 O-GlcNAcylated proteins	1012:1038	In total, 155 O-GlcNAcylated proteins were determined, of which 41 were only observed in LNM tissues, while 40 were unique in non-LNM samples.
26374642	7	12	theme	non-metastatic	1348:1361	arg1	IDCs					1363:1366	both metastatic and non-metastatic IDCs	1328:1366	both metastatic and non-metastatic IDCs	1328:1366	Gene ontology analysis showed that O-GlcNAc is primarily a nucleocytoplasmic post-translational modification, and most enriched functional terms were related to cancer development in both metastatic and non-metastatic IDCs.
26374642	7	13	theme	post-translational	1222:1239	arg1	O-GlcNAc					1180:1187	O-GlcNAc	1180:1187	O-GlcNAc	1180:1187	Gene ontology analysis showed that O-GlcNAc is primarily a nucleocytoplasmic post-translational modification, and most enriched functional terms were related to cancer development in both metastatic and non-metastatic IDCs.
26374642	7	13	theme	post-translational	1222:1239	arg1	modification					1241:1252	a nucleocytoplasmic post-translational modification	1202:1252	a nucleocytoplasmic post-translational modification	1202:1252	Gene ontology analysis showed that O-GlcNAc is primarily a nucleocytoplasmic post-translational modification, and most enriched functional terms were related to cancer development in both metastatic and non-metastatic IDCs.
26374642	1	14	theme	breast	306:311	arg1	cancer					313:318	breast cancer	306:318	breast cancer	306:318	The potential role of protein O-GlcNAcylation in cancer has been studied extensively, and the spread of cancer cells to regional lymph nodes is the first step in the dissemination of breast cancer.
26374642	3	15	theme	lymph	584:588	arg1	node					590:593	lymph node	584:593	lymph node metastasis (LNM)	584:610	In this study, we demonstrated that the overall O-GlcNAcylation as well as O-GlcNAc transferase (OGT) tends to decrease in response to the augmentation of lymph node metastasis (LNM) in invasive ductal breast carcinomas (IDCs).
26374642	1	16	theme	protein	145:151	arg1	O-GlcNAcylation					153:167	protein O-GlcNAcylation	145:167	protein O-GlcNAcylation	145:167	The potential role of protein O-GlcNAcylation in cancer has been studied extensively, and the spread of cancer cells to regional lymph nodes is the first step in the dissemination of breast cancer.
26374642	5	17	theme	IDCs	882:885	arg1	proteins					870:877	O-GlcNAcylated proteins	855:877	O-GlcNAcylated proteins of IDCs	855:885	Herein, O-GlcNAcylated proteins of IDCs were chemo-enzymatically enriched and identified via liquid chromatography combined with tandem mass spectrometry.
26374642	6	18	dep	determined	1045:1054	arg1	observed					1079:1086	observed	1079:1086	observed in LNM tissues	1079:1101	In total, 155 O-GlcNAcylated proteins were determined, of which 41 were only observed in LNM tissues, while 40 were unique in non-LNM samples.
26374642	4	19	from	important	737:745	arg1	pathogenesis					754:765	the pathogenesis	750:765	the pathogenesis of breast cancer	750:782	Although accumulating evidence indicates that individual O-GlcNAcylation may be important in the pathogenesis of breast cancer, O-GlcNAcylated proteins in IDCs are still largely unexplored.
26374642	9	20	theme	individual	1579:1588	arg1	proteins					1590:1597	individual proteins	1579:1597	individual proteins	1579:1597	These results indicate that the O-GlcNAcylation statuses of individual proteins were independent of the overall O-GlcNAcylation levels of metastatic and non-metastatic IDCs.
26374642	0	21	theme	node	106:109	arg1	metastasis					111:120	lymph node metastasis	100:120	lymph node metastasis	100:120	Proteomic analysis of O-GlcNAcylated proteins in invasive ductal breast carcinomas with and without lymph node metastasis.
26374642	5	22	theme	mass	983:986	arg1	spectrometry					988:999	tandem mass spectrometry	976:999	tandem mass spectrometry	976:999	Herein, O-GlcNAcylated proteins of IDCs were chemo-enzymatically enriched and identified via liquid chromatography combined with tandem mass spectrometry.
26374642	0	23	from	proteins	37:44	arg1	carcinomas					72:81	invasive ductal breast carcinomas	49:81	invasive ductal breast carcinomas with and without lymph node metastasis	49:120	Proteomic analysis of O-GlcNAcylated proteins in invasive ductal breast carcinomas with and without lymph node metastasis.
26374642	4	24	theme	individual	703:712	arg1	O-GlcNAcylation					714:728	individual O-GlcNAcylation	703:728	individual O-GlcNAcylation	703:728	Although accumulating evidence indicates that individual O-GlcNAcylation may be important in the pathogenesis of breast cancer, O-GlcNAcylated proteins in IDCs are still largely unexplored.
26374642	10	25	theme	O-GlcNAc	1702:1709	arg1	modification					1711:1722	Aberrant O-GlcNAc modification	1693:1722	Aberrant O-GlcNAc modification of these proteins	1693:1740	Aberrant O-GlcNAc modification of these proteins might be associated with LNM progression.
26374642	0	26	theme	Proteomic	0:8	arg1	analysis					10:17	Proteomic analysis	0:17	Proteomic analysis of O-GlcNAcylated proteins in invasive ductal breast carcinomas with and without lymph node metastasis.	0:121	Proteomic analysis of O-GlcNAcylated proteins in invasive ductal breast carcinomas with and without lymph node metastasis.
26374642	6	27	from	unique	1118:1123	arg1	samples					1136:1142	non-LNM samples	1128:1142	non-LNM samples	1128:1142	In total, 155 O-GlcNAcylated proteins were determined, of which 41 were only observed in LNM tissues, while 40 were unique in non-LNM samples.
26374642	7	28	theme	Gene	1145:1148	arg1	analysis					1159:1166	Gene ontology analysis	1145:1166	Gene ontology analysis	1145:1166	Gene ontology analysis showed that O-GlcNAc is primarily a nucleocytoplasmic post-translational modification, and most enriched functional terms were related to cancer development in both metastatic and non-metastatic IDCs.
26374642	1	29	theme	first	271:275	arg1	spread					217:222	the spread	213:222	the spread of cancer cells to regional lymph nodes	213:262	The potential role of protein O-GlcNAcylation in cancer has been studied extensively, and the spread of cancer cells to regional lymph nodes is the first step in the dissemination of breast cancer.
26374642	1	29	theme	first	271:275	arg1	step					277:280	the first step	267:280	the first step in the dissemination of breast cancer	267:318	The potential role of protein O-GlcNAcylation in cancer has been studied extensively, and the spread of cancer cells to regional lymph nodes is the first step in the dissemination of breast cancer.
26374642	9	30	theme	overall	1623:1629	arg1	levels					1647:1652	the overall O-GlcNAcylation levels	1619:1652	the overall O-GlcNAcylation levels of metastatic and non-metastatic IDCs	1619:1690	These results indicate that the O-GlcNAcylation statuses of individual proteins were independent of the overall O-GlcNAcylation levels of metastatic and non-metastatic IDCs.
26374642	2	31	theme	breast	398:403	arg1	cancer					405:410	breast cancer	398:410	breast cancer	398:410	However, the correlation between O-GlcNAcylation and lymphatic metastasis in breast cancer remains elusive.
26374642	4	32	theme	O-GlcNAcylated	785:798	arg1	proteins					800:807	O-GlcNAcylated proteins	785:807	O-GlcNAcylated proteins in IDCs	785:815	Although accumulating evidence indicates that individual O-GlcNAcylation may be important in the pathogenesis of breast cancer, O-GlcNAcylated proteins in IDCs are still largely unexplored.
26374642	3	33	from	augmentation	568:579	arg1	IDCs					650:653	IDCs	650:653	IDCs	650:653	In this study, we demonstrated that the overall O-GlcNAcylation as well as O-GlcNAc transferase (OGT) tends to decrease in response to the augmentation of lymph node metastasis (LNM) in invasive ductal breast carcinomas (IDCs).
26374642	3	33	from	augmentation	568:579	arg1	carcinomas					638:647	invasive ductal breast carcinomas	615:647	invasive ductal breast carcinomas (IDCs)	615:654	In this study, we demonstrated that the overall O-GlcNAcylation as well as O-GlcNAc transferase (OGT) tends to decrease in response to the augmentation of lymph node metastasis (LNM) in invasive ductal breast carcinomas (IDCs).
26374642	10	34	theme	proteins	1733:1740	arg1	modification					1711:1722	Aberrant O-GlcNAc modification	1693:1722	Aberrant O-GlcNAc modification of these proteins	1693:1740	Aberrant O-GlcNAc modification of these proteins might be associated with LNM progression.
26374642	0	35	theme	proteins	37:44	arg1	analysis					10:17	Proteomic analysis	0:17	Proteomic analysis of O-GlcNAcylated proteins in invasive ductal breast carcinomas with and without lymph node metastasis.	0:121	Proteomic analysis of O-GlcNAcylated proteins in invasive ductal breast carcinomas with and without lymph node metastasis.
26374642	9	36	theme	levels	1647:1652	arg1	independent					1604:1614	independent	1604:1614	independent	1604:1614	These results indicate that the O-GlcNAcylation statuses of individual proteins were independent of the overall O-GlcNAcylation levels of metastatic and non-metastatic IDCs.
26374642	9	36	theme	levels	1647:1652	arg1	statuses					1567:1574	the O-GlcNAcylation statuses	1547:1574	the O-GlcNAcylation statuses of individual proteins	1547:1597	These results indicate that the O-GlcNAcylation statuses of individual proteins were independent of the overall O-GlcNAcylation levels of metastatic and non-metastatic IDCs.
26374642	0	37	theme	breast	65:70	arg1	carcinomas					72:81	invasive ductal breast carcinomas	49:81	invasive ductal breast carcinomas with and without lymph node metastasis	49:120	Proteomic analysis of O-GlcNAcylated proteins in invasive ductal breast carcinomas with and without lymph node metastasis.
26374642	3	38	theme	overall	469:475	arg1	O-GlcNAcylation					477:491	the overall O-GlcNAcylation	465:491	the overall O-GlcNAcylation as well as O-GlcNAc transferase (OGT)	465:529	In this study, we demonstrated that the overall O-GlcNAcylation as well as O-GlcNAc transferase (OGT) tends to decrease in response to the augmentation of lymph node metastasis (LNM) in invasive ductal breast carcinomas (IDCs).
26374642	0	39	theme	invasive	49:56	arg1	carcinomas					72:81	invasive ductal breast carcinomas	49:81	invasive ductal breast carcinomas with and without lymph node metastasis	49:120	Proteomic analysis of O-GlcNAcylated proteins in invasive ductal breast carcinomas with and without lymph node metastasis.
26374642	9	40	theme	metastatic	1657:1666	arg1	IDCs					1687:1690	metastatic and non-metastatic IDCs	1657:1690	metastatic and non-metastatic IDCs	1657:1690	These results indicate that the O-GlcNAcylation statuses of individual proteins were independent of the overall O-GlcNAcylation levels of metastatic and non-metastatic IDCs.
26374642	8	41	theme	accessory	1442:1450	arg1	pathway					1452:1458	its accessory pathway	1438:1458	its accessory pathway	1438:1458	Moreover, several O-GlcNAcylated proteins involved in glycolysis and its accessory pathway were identified from LNM and non-LNM groups, respectively.
26374642	9	42	theme	non-metastatic	1672:1685	arg1	IDCs					1687:1690	metastatic and non-metastatic IDCs	1657:1690	metastatic and non-metastatic IDCs	1657:1690	These results indicate that the O-GlcNAcylation statuses of individual proteins were independent of the overall O-GlcNAcylation levels of metastatic and non-metastatic IDCs.
26374642	7	43	theme	functional	1273:1282	arg1	terms					1284:1288	most enriched functional terms	1259:1288	most enriched functional terms	1259:1288	Gene ontology analysis showed that O-GlcNAc is primarily a nucleocytoplasmic post-translational modification, and most enriched functional terms were related to cancer development in both metastatic and non-metastatic IDCs.
26374642	3	44	theme	ductal	624:629	arg1	IDCs					650:653	IDCs	650:653	IDCs	650:653	In this study, we demonstrated that the overall O-GlcNAcylation as well as O-GlcNAc transferase (OGT) tends to decrease in response to the augmentation of lymph node metastasis (LNM) in invasive ductal breast carcinomas (IDCs).
26374642	3	44	theme	ductal	624:629	arg1	carcinomas					638:647	invasive ductal breast carcinomas	615:647	invasive ductal breast carcinomas (IDCs)	615:654	In this study, we demonstrated that the overall O-GlcNAcylation as well as O-GlcNAc transferase (OGT) tends to decrease in response to the augmentation of lymph node metastasis (LNM) in invasive ductal breast carcinomas (IDCs).
26374642	4	45	theme	cancer	777:782	arg1	pathogenesis					754:765	the pathogenesis	750:765	the pathogenesis of breast cancer	750:782	Although accumulating evidence indicates that individual O-GlcNAcylation may be important in the pathogenesis of breast cancer, O-GlcNAcylated proteins in IDCs are still largely unexplored.
26374642	1	46	theme	cancer	227:232	arg1	cells					234:238	cancer cells	227:238	cancer cells	227:238	The potential role of protein O-GlcNAcylation in cancer has been studied extensively, and the spread of cancer cells to regional lymph nodes is the first step in the dissemination of breast cancer.
26374642	6	47	theme	LNM	1091:1093	arg1	tissues					1095:1101	LNM tissues	1091:1101	LNM tissues	1091:1101	In total, 155 O-GlcNAcylated proteins were determined, of which 41 were only observed in LNM tissues, while 40 were unique in non-LNM samples.
26374642	1	48	theme	lymph	252:256	arg1	nodes					258:262	regional lymph nodes	243:262	regional lymph nodes	243:262	The potential role of protein O-GlcNAcylation in cancer has been studied extensively, and the spread of cancer cells to regional lymph nodes is the first step in the dissemination of breast cancer.
26374642	9	49	theme	O-GlcNAcylation	1551:1565	arg1	independent					1604:1614	independent	1604:1614	independent	1604:1614	These results indicate that the O-GlcNAcylation statuses of individual proteins were independent of the overall O-GlcNAcylation levels of metastatic and non-metastatic IDCs.
26374642	9	49	theme	O-GlcNAcylation	1551:1565	arg1	statuses					1567:1574	the O-GlcNAcylation statuses	1547:1574	the O-GlcNAcylation statuses of individual proteins	1547:1597	These results indicate that the O-GlcNAcylation statuses of individual proteins were independent of the overall O-GlcNAcylation levels of metastatic and non-metastatic IDCs.
26374642	6	50	theme	non-LNM	1128:1134	arg1	samples					1136:1142	non-LNM samples	1128:1142	non-LNM samples	1128:1142	In total, 155 O-GlcNAcylated proteins were determined, of which 41 were only observed in LNM tissues, while 40 were unique in non-LNM samples.
26374642	0	51	from	carcinomas	72:81	arg1	analysis					10:17	Proteomic analysis	0:17	Proteomic analysis of O-GlcNAcylated proteins in invasive ductal breast carcinomas with and without lymph node metastasis.	0:121	Proteomic analysis of O-GlcNAcylated proteins in invasive ductal breast carcinomas with and without lymph node metastasis.
26374642	4	52	from	proteins	800:807	arg1	IDCs					812:815	IDCs	812:815	IDCs	812:815	Although accumulating evidence indicates that individual O-GlcNAcylation may be important in the pathogenesis of breast cancer, O-GlcNAcylated proteins in IDCs are still largely unexplored.
26374642	3	53	theme	node	590:593	arg1	LNM					607:609	LNM	607:609	LNM	607:609	In this study, we demonstrated that the overall O-GlcNAcylation as well as O-GlcNAc transferase (OGT) tends to decrease in response to the augmentation of lymph node metastasis (LNM) in invasive ductal breast carcinomas (IDCs).
26374642	3	53	theme	node	590:593	arg1	metastasis					595:604	lymph node metastasis	584:604	lymph node metastasis (LNM)	584:610	In this study, we demonstrated that the overall O-GlcNAcylation as well as O-GlcNAc transferase (OGT) tends to decrease in response to the augmentation of lymph node metastasis (LNM) in invasive ductal breast carcinomas (IDCs).
26374642	1	54	theme	potential	127:135	arg1	role					137:140	The potential role	123:140	The potential role of protein O-GlcNAcylation in cancer	123:177	The potential role of protein O-GlcNAcylation in cancer has been studied extensively, and the spread of cancer cells to regional lymph nodes is the first step in the dissemination of breast cancer.
26374642	7	55	theme	nucleocytoplasmic	1204:1220	arg1	O-GlcNAc					1180:1187	O-GlcNAc	1180:1187	O-GlcNAc	1180:1187	Gene ontology analysis showed that O-GlcNAc is primarily a nucleocytoplasmic post-translational modification, and most enriched functional terms were related to cancer development in both metastatic and non-metastatic IDCs.
26374642	7	55	theme	nucleocytoplasmic	1204:1220	arg1	modification					1241:1252	a nucleocytoplasmic post-translational modification	1202:1252	a nucleocytoplasmic post-translational modification	1202:1252	Gene ontology analysis showed that O-GlcNAc is primarily a nucleocytoplasmic post-translational modification, and most enriched functional terms were related to cancer development in both metastatic and non-metastatic IDCs.
26374642	5	56	theme	O-GlcNAcylated	855:868	arg1	proteins					870:877	O-GlcNAcylated proteins	855:877	O-GlcNAcylated proteins of IDCs	855:885	Herein, O-GlcNAcylated proteins of IDCs were chemo-enzymatically enriched and identified via liquid chromatography combined with tandem mass spectrometry.
26374642	1	57	theme	cancer	313:318	arg1	dissemination					289:301	the dissemination	285:301	the dissemination of breast cancer	285:318	The potential role of protein O-GlcNAcylation in cancer has been studied extensively, and the spread of cancer cells to regional lymph nodes is the first step in the dissemination of breast cancer.
26374642	4	58	from	pathogenesis	754:765	arg1	important					737:745	important	737:745	important	737:745	Although accumulating evidence indicates that individual O-GlcNAcylation may be important in the pathogenesis of breast cancer, O-GlcNAcylated proteins in IDCs are still largely unexplored.
26374642	1	59	theme	O-GlcNAcylation	153:167	arg1	role					137:140	The potential role	123:140	The potential role of protein O-GlcNAcylation in cancer	123:177	The potential role of protein O-GlcNAcylation in cancer has been studied extensively, and the spread of cancer cells to regional lymph nodes is the first step in the dissemination of breast cancer.
26374642	0	60	from	analysis	10:17	arg1	carcinomas					72:81	invasive ductal breast carcinomas	49:81	invasive ductal breast carcinomas with and without lymph node metastasis	49:120	Proteomic analysis of O-GlcNAcylated proteins in invasive ductal breast carcinomas with and without lymph node metastasis.
26374642	0	61	theme	lymph	100:104	arg1	metastasis					111:120	lymph node metastasis	100:120	lymph node metastasis	100:120	Proteomic analysis of O-GlcNAcylated proteins in invasive ductal breast carcinomas with and without lymph node metastasis.
26374642	5	62	theme	tandem	976:981	arg1	spectrometry					988:999	tandem mass spectrometry	976:999	tandem mass spectrometry	976:999	Herein, O-GlcNAcylated proteins of IDCs were chemo-enzymatically enriched and identified via liquid chromatography combined with tandem mass spectrometry.
26374642	7	63	theme	metastatic	1333:1342	arg1	IDCs					1363:1366	both metastatic and non-metastatic IDCs	1328:1366	both metastatic and non-metastatic IDCs	1328:1366	Gene ontology analysis showed that O-GlcNAc is primarily a nucleocytoplasmic post-translational modification, and most enriched functional terms were related to cancer development in both metastatic and non-metastatic IDCs.
26374642	2	64	theme	lymphatic	374:382	arg1	metastasis					384:393	lymphatic metastasis	374:393	lymphatic metastasis	374:393	However, the correlation between O-GlcNAcylation and lymphatic metastasis in breast cancer remains elusive.
26374642	7	65	theme	ontology	1150:1157	arg1	analysis					1159:1166	Gene ontology analysis	1145:1166	Gene ontology analysis	1145:1166	Gene ontology analysis showed that O-GlcNAc is primarily a nucleocytoplasmic post-translational modification, and most enriched functional terms were related to cancer development in both metastatic and non-metastatic IDCs.
26374642	1	66	from	role	137:140	arg1	cancer					172:177	cancer	172:177	cancer	172:177	The potential role of protein O-GlcNAcylation in cancer has been studied extensively, and the spread of cancer cells to regional lymph nodes is the first step in the dissemination of breast cancer.
26374642	10	67	theme	Aberrant	1693:1700	arg1	modification					1711:1722	Aberrant O-GlcNAc modification	1693:1722	Aberrant O-GlcNAc modification of these proteins	1693:1740	Aberrant O-GlcNAc modification of these proteins might be associated with LNM progression.
26374642	0	68	theme	O-GlcNAcylated	22:35	arg1	proteins					37:44	O-GlcNAcylated proteins	22:44	O-GlcNAcylated proteins in invasive ductal breast carcinomas with and without lymph node metastasis	22:120	Proteomic analysis of O-GlcNAcylated proteins in invasive ductal breast carcinomas with and without lymph node metastasis.
26374642	5	69	theme	liquid	940:945	arg1	chromatography					947:960	liquid chromatography	940:960	liquid chromatography combined with tandem mass spectrometry	940:999	Herein, O-GlcNAcylated proteins of IDCs were chemo-enzymatically enriched and identified via liquid chromatography combined with tandem mass spectrometry.
26374642	7	70	theme	cancer	1306:1311	arg1	development					1313:1323	cancer development	1306:1323	cancer development in both metastatic and non-metastatic IDCs	1306:1366	Gene ontology analysis showed that O-GlcNAc is primarily a nucleocytoplasmic post-translational modification, and most enriched functional terms were related to cancer development in both metastatic and non-metastatic IDCs.
26374642	9	71	theme	proteins	1590:1597	arg1	independent					1604:1614	independent	1604:1614	independent	1604:1614	These results indicate that the O-GlcNAcylation statuses of individual proteins were independent of the overall O-GlcNAcylation levels of metastatic and non-metastatic IDCs.
26374642	9	71	theme	proteins	1590:1597	arg1	statuses					1567:1574	the O-GlcNAcylation statuses	1547:1574	the O-GlcNAcylation statuses of individual proteins	1547:1597	These results indicate that the O-GlcNAcylation statuses of individual proteins were independent of the overall O-GlcNAcylation levels of metastatic and non-metastatic IDCs.
26374642	8	72	theme	O-GlcNAcylated	1387:1400	arg1	proteins					1402:1409	several O-GlcNAcylated proteins	1379:1409	several O-GlcNAcylated proteins involved in glycolysis and its accessory pathway	1379:1458	Moreover, several O-GlcNAcylated proteins involved in glycolysis and its accessory pathway were identified from LNM and non-LNM groups, respectively.
26374642	6	73	from	samples	1136:1142	arg1	unique					1118:1123	unique	1118:1123	unique	1118:1123	In total, 155 O-GlcNAcylated proteins were determined, of which 41 were only observed in LNM tissues, while 40 were unique in non-LNM samples.
26374642	9	74	theme	O-GlcNAcylation	1631:1645	arg1	levels					1647:1652	the overall O-GlcNAcylation levels	1619:1652	the overall O-GlcNAcylation levels of metastatic and non-metastatic IDCs	1619:1690	These results indicate that the O-GlcNAcylation statuses of individual proteins were independent of the overall O-GlcNAcylation levels of metastatic and non-metastatic IDCs.
26374642	0	75	theme	ductal	58:63	arg1	carcinomas					72:81	invasive ductal breast carcinomas	49:81	invasive ductal breast carcinomas with and without lymph node metastasis	49:120	Proteomic analysis of O-GlcNAcylated proteins in invasive ductal breast carcinomas with and without lymph node metastasis.
26374642	3	76	theme	breast	631:636	arg1	IDCs					650:653	IDCs	650:653	IDCs	650:653	In this study, we demonstrated that the overall O-GlcNAcylation as well as O-GlcNAc transferase (OGT) tends to decrease in response to the augmentation of lymph node metastasis (LNM) in invasive ductal breast carcinomas (IDCs).
26374642	3	76	theme	breast	631:636	arg1	carcinomas					638:647	invasive ductal breast carcinomas	615:647	invasive ductal breast carcinomas (IDCs)	615:654	In this study, we demonstrated that the overall O-GlcNAcylation as well as O-GlcNAc transferase (OGT) tends to decrease in response to the augmentation of lymph node metastasis (LNM) in invasive ductal breast carcinomas (IDCs).
26374642	10	77	theme	LNM	1767:1769	arg1	progression					1771:1781	LNM progression	1767:1781	LNM progression	1767:1781	Aberrant O-GlcNAc modification of these proteins might be associated with LNM progression.
26374642	7	78	from	development	1313:1323	arg1	IDCs					1363:1366	both metastatic and non-metastatic IDCs	1328:1366	both metastatic and non-metastatic IDCs	1328:1366	Gene ontology analysis showed that O-GlcNAc is primarily a nucleocytoplasmic post-translational modification, and most enriched functional terms were related to cancer development in both metastatic and non-metastatic IDCs.
26374642	7	79	theme	enriched	1264:1271	arg1	terms					1284:1288	most enriched functional terms	1259:1288	most enriched functional terms	1259:1288	Gene ontology analysis showed that O-GlcNAc is primarily a nucleocytoplasmic post-translational modification, and most enriched functional terms were related to cancer development in both metastatic and non-metastatic IDCs.
26374642	3	80	theme	invasive	615:622	arg1	IDCs					650:653	IDCs	650:653	IDCs	650:653	In this study, we demonstrated that the overall O-GlcNAcylation as well as O-GlcNAc transferase (OGT) tends to decrease in response to the augmentation of lymph node metastasis (LNM) in invasive ductal breast carcinomas (IDCs).
26374642	3	80	theme	invasive	615:622	arg1	carcinomas					638:647	invasive ductal breast carcinomas	615:647	invasive ductal breast carcinomas (IDCs)	615:654	In this study, we demonstrated that the overall O-GlcNAcylation as well as O-GlcNAc transferase (OGT) tends to decrease in response to the augmentation of lymph node metastasis (LNM) in invasive ductal breast carcinomas (IDCs).
26374642	7	81	theme	most	1259:1262	arg1	terms					1284:1288	most enriched functional terms	1259:1288	most enriched functional terms	1259:1288	Gene ontology analysis showed that O-GlcNAc is primarily a nucleocytoplasmic post-translational modification, and most enriched functional terms were related to cancer development in both metastatic and non-metastatic IDCs.
26374642	9	82	theme	IDCs	1687:1690	arg1	levels					1647:1652	the overall O-GlcNAcylation levels	1619:1652	the overall O-GlcNAcylation levels of metastatic and non-metastatic IDCs	1619:1690	These results indicate that the O-GlcNAcylation statuses of individual proteins were independent of the overall O-GlcNAcylation levels of metastatic and non-metastatic IDCs.
26374642	4	83	theme	breast	770:775	arg1	cancer					777:782	breast cancer	770:782	breast cancer	770:782	Although accumulating evidence indicates that individual O-GlcNAcylation may be important in the pathogenesis of breast cancer, O-GlcNAcylated proteins in IDCs are still largely unexplored.
26374642	3	84	theme	O-GlcNAc	504:511	arg1	OGT					526:528	OGT	526:528	OGT	526:528	In this study, we demonstrated that the overall O-GlcNAcylation as well as O-GlcNAc transferase (OGT) tends to decrease in response to the augmentation of lymph node metastasis (LNM) in invasive ductal breast carcinomas (IDCs).
26374642	3	84	theme	O-GlcNAc	504:511	arg1	transferase					513:523	O-GlcNAc transferase	504:523	the overall O-GlcNAcylation as well as O-GlcNAc transferase (OGT)	465:529	In this study, we demonstrated that the overall O-GlcNAcylation as well as O-GlcNAc transferase (OGT) tends to decrease in response to the augmentation of lymph node metastasis (LNM) in invasive ductal breast carcinomas (IDCs).
26374642	1	85	theme	cells	234:238	arg1	spread					217:222	the spread	213:222	the spread of cancer cells to regional lymph nodes	213:262	The potential role of protein O-GlcNAcylation in cancer has been studied extensively, and the spread of cancer cells to regional lymph nodes is the first step in the dissemination of breast cancer.
26374642	1	85	theme	cells	234:238	arg1	step					277:280	the first step	267:280	the first step in the dissemination of breast cancer	267:318	The potential role of protein O-GlcNAcylation in cancer has been studied extensively, and the spread of cancer cells to regional lymph nodes is the first step in the dissemination of breast cancer.
22967762	7	0	theme	electrophoresis	1139:1153	arg1	combination					1108:1118	A combination	1106:1118	A combination of two-dimensional electrophoresis, Western blotting and mass spectrometry	1106:1193	A combination of two-dimensional electrophoresis, Western blotting and mass spectrometry was then used to detect and identify cell cycle-dependent putative O-GlcNAcylated proteins.
22967762	0	1	theme	proteins	99:106	arg1	Characterization					0:15	Characterization	0:15	Characterization of O-GlcNAc cycling	0:35	Characterization of O-GlcNAc cycling and proteomic identification of differentially O-GlcNAcylated proteins during G1/S transition.
22967762	0	1	theme	proteins	99:106	arg1	identification					51:64	proteomic identification	41:64	proteomic identification of differentially O-GlcNAcylated proteins during G1/S transition	41:129	Characterization of O-GlcNAc cycling and proteomic identification of differentially O-GlcNAcylated proteins during G1/S transition.
22967762	8	2	dep	proteins	1314:1321	arg1	O-GlcNAcylated					1338:1351	O-GlcNAcylated	1338:1351	O-GlcNAcylated	1338:1351	58 cytoplasmic and nuclear proteins differentially O-GlcNAcylated through G1/S transition were identified and the O-GlcNAc variations of Cytokeratin 8, hnRNP K, Caprin-1, Minichromosome Maintenance proteins MCM3, MCM6 and MCM7 were validated by immunoprecipitation.
22967762	6	3	theme	OGA	1101:1103	arg1	activity					1089:1096	the activity	1085:1096	the activity of OGA	1085:1103	A global decrease in O-GlcNAcylation was observed at S phase entry, concomitantly to an increase in the activity of OGA.
22967762	8	4	theme	hnRNP	1439:1443	arg1	Cytokeratin					1424:1434	Cytokeratin 8	1424:1436	Cytokeratin 8	1424:1436	58 cytoplasmic and nuclear proteins differentially O-GlcNAcylated through G1/S transition were identified and the O-GlcNAc variations of Cytokeratin 8, hnRNP K, Caprin-1, Minichromosome Maintenance proteins MCM3, MCM6 and MCM7 were validated by immunoprecipitation.
22967762	8	4	theme	hnRNP	1439:1443	arg1	K					1445:1445	hnRNP K	1439:1445	hnRNP K	1439:1445	58 cytoplasmic and nuclear proteins differentially O-GlcNAcylated through G1/S transition were identified and the O-GlcNAc variations of Cytokeratin 8, hnRNP K, Caprin-1, Minichromosome Maintenance proteins MCM3, MCM6 and MCM7 were validated by immunoprecipitation.
22967762	9	5	theme	mRNA	1694:1697	arg1	networks					1684:1691	the cytoskeleton networks	1667:1691	the cytoskeleton networks	1667:1691	CONCLUSIONS The dynamics of O-GlcNAc is regulated during G1/S transition and observed on key proteins involved in the cytoskeleton networks, mRNA processing, translation, protein folding and DNA replication.
22967762	9	5	theme	mRNA	1694:1697	arg1	processing					1699:1708	mRNA processing	1694:1708	mRNA processing	1694:1708	CONCLUSIONS The dynamics of O-GlcNAc is regulated during G1/S transition and observed on key proteins involved in the cytoskeleton networks, mRNA processing, translation, protein folding and DNA replication.
22967762	9	6	theme	protein	1724:1730	arg1	networks					1684:1691	the cytoskeleton networks	1667:1691	the cytoskeleton networks	1667:1691	CONCLUSIONS The dynamics of O-GlcNAc is regulated during G1/S transition and observed on key proteins involved in the cytoskeleton networks, mRNA processing, translation, protein folding and DNA replication.
22967762	9	6	theme	protein	1724:1730	arg1	folding					1732:1738	protein folding	1724:1738	protein folding	1724:1738	CONCLUSIONS The dynamics of O-GlcNAc is regulated during G1/S transition and observed on key proteins involved in the cytoskeleton networks, mRNA processing, translation, protein folding and DNA replication.
22967762	3	7	theme	PTM	577:579	arg1	impact					562:567	the impact	558:567	the impact of this PTM in the early steps of the cell cycle	558:616	Despite increasing evidences showing that O-GlcNAcylation regulates mitotic events, the impact of this PTM in the early steps of the cell cycle remains poorly understood.
22967762	6	8	located	observed	1026:1033	arg2	decrease					994:1001	A global decrease	985:1001	A global decrease in O-GlcNAcylation	985:1020	A global decrease in O-GlcNAcylation was observed at S phase entry, concomitantly to an increase in the activity of OGA.
22967762	6	8	located	observed	1026:1033	arg1	entry					1046:1050	S phase entry	1038:1050	S phase entry	1038:1050	A global decrease in O-GlcNAcylation was observed at S phase entry, concomitantly to an increase in the activity of OGA.
22967762	3	9	theme	cell	607:610	arg1	cycle					612:616	the cell cycle	603:616	the cell cycle	603:616	Despite increasing evidences showing that O-GlcNAcylation regulates mitotic events, the impact of this PTM in the early steps of the cell cycle remains poorly understood.
22967762	0	10	theme	G1/S	115:118	arg1	transition					120:129	G1/S transition	115:129	G1/S transition	115:129	Characterization of O-GlcNAc cycling and proteomic identification of differentially O-GlcNAcylated proteins during G1/S transition.
22967762	7	11	theme	two-dimensional	1123:1137	arg1	electrophoresis					1139:1153	two-dimensional electrophoresis	1123:1153	two-dimensional electrophoresis	1123:1153	A combination of two-dimensional electrophoresis, Western blotting and mass spectrometry was then used to detect and identify cell cycle-dependent putative O-GlcNAcylated proteins.
22967762	5	12	theme	modified	804:811	arg1	proteins					813:820	O-GlcNAc modified proteins	795:820	O-GlcNAc modified proteins	795:820	The levels of O-GlcNAc modified proteins, O-GlcNAc Transferase (OGT) and O-GlcNAcase (OGA) were examined by Western blotting and OGA activity was measured during the progression of cells towards S phase.
22967762	5	12	theme	modified	804:811	arg1	Transferase					832:842	O-GlcNAc Transferase	823:842	O-GlcNAc Transferase (OGT)	823:848	The levels of O-GlcNAc modified proteins, O-GlcNAc Transferase (OGT) and O-GlcNAcase (OGA) were examined by Western blotting and OGA activity was measured during the progression of cells towards S phase.
22967762	5	12	theme	modified	804:811	arg1	O-GlcNAcase					854:864	O-GlcNAcase	854:864	O-GlcNAcase (OGA)	854:870	The levels of O-GlcNAc modified proteins, O-GlcNAc Transferase (OGT) and O-GlcNAcase (OGA) were examined by Western blotting and OGA activity was measured during the progression of cells towards S phase.
22967762	1	13	theme	genome	298:303	arg1	duplication					305:315	genome duplication	298:315	genome duplication	298:315	BACKGROUND DNA replication represents a critical step of the cell cycle which requires highly controlled and ordered regulatory mechanisms to ensure the integrity of genome duplication.
22967762	4	14	theme	flow	765:768	arg1	cytometry					770:778	flow cytometry	765:778	flow cytometry	765:778	METHODS AND RESULTS Quiescent MCF7 cells were stimulated by serum mitogens and cell cycle progression was determined by flow cytometry.
22967762	3	15	theme	mitotic	542:548	arg1	events					550:555	mitotic events	542:555	mitotic events	542:555	Despite increasing evidences showing that O-GlcNAcylation regulates mitotic events, the impact of this PTM in the early steps of the cell cycle remains poorly understood.
22967762	8	16	theme	Cytokeratin	1424:1434	arg1	variations					1410:1419	the O-GlcNAc variations	1397:1419	the O-GlcNAc variations of Cytokeratin 8, hnRNP K, Caprin-1, Minichromosome Maintenance proteins MCM3, MCM6 and MCM7	1397:1512	58 cytoplasmic and nuclear proteins differentially O-GlcNAcylated through G1/S transition were identified and the O-GlcNAc variations of Cytokeratin 8, hnRNP K, Caprin-1, Minichromosome Maintenance proteins MCM3, MCM6 and MCM7 were validated by immunoprecipitation.
22967762	8	17	theme	cytoplasmic	1290:1300	arg1	proteins					1314:1321	58 cytoplasmic and nuclear proteins	1287:1321	58 cytoplasmic and nuclear proteins differentially O-GlcNAcylated through G1/S transition	1287:1375	58 cytoplasmic and nuclear proteins differentially O-GlcNAcylated through G1/S transition were identified and the O-GlcNAc variations of Cytokeratin 8, hnRNP K, Caprin-1, Minichromosome Maintenance proteins MCM3, MCM6 and MCM7 were validated by immunoprecipitation.
22967762	1	18	theme	cell	193:196	arg1	cycle					198:202	the cell cycle	189:202	the cell cycle	189:202	BACKGROUND DNA replication represents a critical step of the cell cycle which requires highly controlled and ordered regulatory mechanisms to ensure the integrity of genome duplication.
22967762	9	19	theme	DNA	1744:1746	arg1	networks					1684:1691	the cytoskeleton networks	1667:1691	the cytoskeleton networks	1667:1691	CONCLUSIONS The dynamics of O-GlcNAc is regulated during G1/S transition and observed on key proteins involved in the cytoskeleton networks, mRNA processing, translation, protein folding and DNA replication.
22967762	9	19	theme	DNA	1744:1746	arg1	replication					1748:1758	DNA replication	1744:1758	DNA replication	1744:1758	CONCLUSIONS The dynamics of O-GlcNAc is regulated during G1/S transition and observed on key proteins involved in the cytoskeleton networks, mRNA processing, translation, protein folding and DNA replication.
22967762	3	20	theme	early	588:592	arg1	steps					594:598	the early steps	584:598	the early steps of the cell cycle	584:616	Despite increasing evidences showing that O-GlcNAcylation regulates mitotic events, the impact of this PTM in the early steps of the cell cycle remains poorly understood.
22967762	1	21	theme	cycle	198:202	arg1	step					181:184	a critical step	170:184	a critical step of the cell cycle which requires highly controlled and ordered regulatory mechanisms to ensure the integrity of genome duplication	170:315	BACKGROUND DNA replication represents a critical step of the cell cycle which requires highly controlled and ordered regulatory mechanisms to ensure the integrity of genome duplication.
22967762	5	22	theme	O-GlcNAc	823:830	arg1	OGT					845:847	OGT	845:847	OGT	845:847	The levels of O-GlcNAc modified proteins, O-GlcNAc Transferase (OGT) and O-GlcNAcase (OGA) were examined by Western blotting and OGA activity was measured during the progression of cells towards S phase.
22967762	5	22	theme	O-GlcNAc	823:830	arg1	proteins					813:820	O-GlcNAc modified proteins	795:820	O-GlcNAc modified proteins	795:820	The levels of O-GlcNAc modified proteins, O-GlcNAc Transferase (OGT) and O-GlcNAcase (OGA) were examined by Western blotting and OGA activity was measured during the progression of cells towards S phase.
22967762	5	22	theme	O-GlcNAc	823:830	arg1	Transferase					832:842	O-GlcNAc Transferase	823:842	O-GlcNAc Transferase (OGT)	823:848	The levels of O-GlcNAc modified proteins, O-GlcNAc Transferase (OGT) and O-GlcNAcase (OGA) were examined by Western blotting and OGA activity was measured during the progression of cells towards S phase.
22967762	7	23	theme	cycle-dependent	1237:1251	arg1	proteins					1277:1284	cell cycle-dependent putative O-GlcNAcylated proteins	1232:1284	cell cycle-dependent putative O-GlcNAcylated proteins	1232:1284	A combination of two-dimensional electrophoresis, Western blotting and mass spectrometry was then used to detect and identify cell cycle-dependent putative O-GlcNAcylated proteins.
22967762	4	24	theme	serum	705:709	arg1	mitogens					711:718	serum mitogens	705:718	serum mitogens	705:718	METHODS AND RESULTS Quiescent MCF7 cells were stimulated by serum mitogens and cell cycle progression was determined by flow cytometry.
22967762	3	25	theme	cycle	612:616	arg1	steps					594:598	the early steps	584:598	the early steps of the cell cycle	584:616	Despite increasing evidences showing that O-GlcNAcylation regulates mitotic events, the impact of this PTM in the early steps of the cell cycle remains poorly understood.
22967762	4	26	theme	cell	724:727	arg1	progression					735:745	cell cycle progression	724:745	cell cycle progression	724:745	METHODS AND RESULTS Quiescent MCF7 cells were stimulated by serum mitogens and cell cycle progression was determined by flow cytometry.
22967762	1	27	theme	duplication	305:315	arg1	integrity					285:293	the integrity	281:293	the integrity of genome duplication	281:315	BACKGROUND DNA replication represents a critical step of the cell cycle which requires highly controlled and ordered regulatory mechanisms to ensure the integrity of genome duplication.
22967762	10	28	theme	DNA	1884:1886	arg1	initiation					1900:1909	DNA replication initiation	1884:1909	DNA replication initiation	1884:1909	GENERAL SIGNIFICANCE Our results led us to propose that O-GlcNAcylation joins the PTMs that take part in the regulation of DNA replication initiation.
22967762	5	29	theme	Western	889:895	arg1	blotting					897:904	Western blotting	889:904	Western blotting	889:904	The levels of O-GlcNAc modified proteins, O-GlcNAc Transferase (OGT) and O-GlcNAcase (OGA) were examined by Western blotting and OGA activity was measured during the progression of cells towards S phase.
22967762	2	30	theme	elements	338:345	arg1	plethora					326:333	a plethora	324:333	a plethora of elements	324:345	Among a plethora of elements, post-translational modifications (PTMs) ensure the spatiotemporal regulation of pivotal proteins orchestrating cell division.
22967762	5	31	theme	OGA	910:912	arg1	activity					914:921	OGA activity	910:921	OGA activity	910:921	The levels of O-GlcNAc modified proteins, O-GlcNAc Transferase (OGT) and O-GlcNAcase (OGA) were examined by Western blotting and OGA activity was measured during the progression of cells towards S phase.
22967762	0	32	theme	cycling	29:35	arg1	Characterization					0:15	Characterization	0:15	Characterization of O-GlcNAc cycling	0:35	Characterization of O-GlcNAc cycling and proteomic identification of differentially O-GlcNAcylated proteins during G1/S transition.
22967762	0	32	theme	cycling	29:35	arg1	identification					51:64	proteomic identification	41:64	proteomic identification of differentially O-GlcNAcylated proteins during G1/S transition	41:129	Characterization of O-GlcNAc cycling and proteomic identification of differentially O-GlcNAcylated proteins during G1/S transition.
22967762	6	33	from	increase	1073:1080	arg1	activity					1089:1096	the activity	1085:1096	the activity of OGA	1085:1103	A global decrease in O-GlcNAcylation was observed at S phase entry, concomitantly to an increase in the activity of OGA.
22967762	8	34	theme	G1/S	1361:1364	arg1	transition					1366:1375	G1/S transition	1361:1375	G1/S transition	1361:1375	58 cytoplasmic and nuclear proteins differentially O-GlcNAcylated through G1/S transition were identified and the O-GlcNAc variations of Cytokeratin 8, hnRNP K, Caprin-1, Minichromosome Maintenance proteins MCM3, MCM6 and MCM7 were validated by immunoprecipitation.
22967762	3	35	from	impact	562:567	arg1	steps					594:598	the early steps	584:598	the early steps of the cell cycle	584:616	Despite increasing evidences showing that O-GlcNAcylation regulates mitotic events, the impact of this PTM in the early steps of the cell cycle remains poorly understood.
22967762	8	36	theme	nuclear	1306:1312	arg1	proteins					1314:1321	58 cytoplasmic and nuclear proteins	1287:1321	58 cytoplasmic and nuclear proteins differentially O-GlcNAcylated through G1/S transition	1287:1375	58 cytoplasmic and nuclear proteins differentially O-GlcNAcylated through G1/S transition were identified and the O-GlcNAc variations of Cytokeratin 8, hnRNP K, Caprin-1, Minichromosome Maintenance proteins MCM3, MCM6 and MCM7 were validated by immunoprecipitation.
22967762	0	37	theme	O-GlcNAc	20:27	arg1	cycling					29:35	O-GlcNAc cycling	20:35	O-GlcNAc cycling	20:35	Characterization of O-GlcNAc cycling and proteomic identification of differentially O-GlcNAcylated proteins during G1/S transition.
22967762	6	38	theme	global	987:992	arg1	decrease					994:1001	A global decrease	985:1001	A global decrease in O-GlcNAcylation	985:1020	A global decrease in O-GlcNAcylation was observed at S phase entry, concomitantly to an increase in the activity of OGA.
22967762	5	39	theme	S	976:976	arg1	phase					978:982	S phase	976:982	S phase	976:982	The levels of O-GlcNAc modified proteins, O-GlcNAc Transferase (OGT) and O-GlcNAcase (OGA) were examined by Western blotting and OGA activity was measured during the progression of cells towards S phase.
22967762	4	40	dep	METHODS	645:651	arg1	stimulated					691:700	stimulated	691:700	were stimulated by serum mitogens and cell cycle progression	686:745	METHODS AND RESULTS Quiescent MCF7 cells were stimulated by serum mitogens and cell cycle progression was determined by flow cytometry.
22967762	1	41	theme	BACKGROUND	132:141	arg1	replication					147:157	BACKGROUND DNA replication	132:157	BACKGROUND DNA replication	132:157	BACKGROUND DNA replication represents a critical step of the cell cycle which requires highly controlled and ordered regulatory mechanisms to ensure the integrity of genome duplication.
22967762	7	42	theme	mass	1177:1180	arg1	spectrometry					1182:1193	mass spectrometry	1177:1193	mass spectrometry	1177:1193	A combination of two-dimensional electrophoresis, Western blotting and mass spectrometry was then used to detect and identify cell cycle-dependent putative O-GlcNAcylated proteins.
22967762	1	43	theme	critical	172:179	arg1	step					181:184	a critical step	170:184	a critical step of the cell cycle which requires highly controlled and ordered regulatory mechanisms to ensure the integrity of genome duplication	170:315	BACKGROUND DNA replication represents a critical step of the cell cycle which requires highly controlled and ordered regulatory mechanisms to ensure the integrity of genome duplication.
22967762	0	44	theme	proteomic	41:49	arg1	identification					51:64	proteomic identification	41:64	proteomic identification of differentially O-GlcNAcylated proteins during G1/S transition	41:129	Characterization of O-GlcNAc cycling and proteomic identification of differentially O-GlcNAcylated proteins during G1/S transition.
22967762	7	45	used	used	1204:1207	arg2	combination					1108:1118	A combination	1106:1118	A combination of two-dimensional electrophoresis, Western blotting and mass spectrometry	1106:1193	A combination of two-dimensional electrophoresis, Western blotting and mass spectrometry was then used to detect and identify cell cycle-dependent putative O-GlcNAcylated proteins.
22967762	2	46	theme	cell	459:462	arg1	division					464:471	cell division	459:471	cell division	459:471	Among a plethora of elements, post-translational modifications (PTMs) ensure the spatiotemporal regulation of pivotal proteins orchestrating cell division.
22967762	2	47	theme	proteins	436:443	arg1	regulation					414:423	the spatiotemporal regulation	395:423	the spatiotemporal regulation of pivotal proteins orchestrating cell division	395:471	Among a plethora of elements, post-translational modifications (PTMs) ensure the spatiotemporal regulation of pivotal proteins orchestrating cell division.
22967762	6	48	from	decrease	994:1001	arg1	O-GlcNAcylation					1006:1020	O-GlcNAcylation	1006:1020	O-GlcNAcylation	1006:1020	A global decrease in O-GlcNAcylation was observed at S phase entry, concomitantly to an increase in the activity of OGA.
22967762	6	49	theme	phase	1040:1044	arg1	entry					1046:1050	S phase entry	1038:1050	S phase entry	1038:1050	A global decrease in O-GlcNAcylation was observed at S phase entry, concomitantly to an increase in the activity of OGA.
22967762	1	50	theme	ordered	241:247	arg1	mechanisms					260:269	ordered regulatory mechanisms	241:269	ordered regulatory mechanisms	241:269	BACKGROUND DNA replication represents a critical step of the cell cycle which requires highly controlled and ordered regulatory mechanisms to ensure the integrity of genome duplication.
22967762	7	51	theme	Western	1156:1162	arg1	blotting					1164:1171	Western blotting	1156:1171	Western blotting	1156:1171	A combination of two-dimensional electrophoresis, Western blotting and mass spectrometry was then used to detect and identify cell cycle-dependent putative O-GlcNAcylated proteins.
22967762	10	52	theme	initiation	1900:1909	arg1	regulation					1870:1879	the regulation	1866:1879	the regulation of DNA replication initiation	1866:1909	GENERAL SIGNIFICANCE Our results led us to propose that O-GlcNAcylation joins the PTMs that take part in the regulation of DNA replication initiation.
22967762	10	53	dep	led	1794:1796	arg1	SIGNIFICANCE					1769:1780	GENERAL SIGNIFICANCE	1761:1780	GENERAL SIGNIFICANCE	1761:1780	GENERAL SIGNIFICANCE Our results led us to propose that O-GlcNAcylation joins the PTMs that take part in the regulation of DNA replication initiation.
22967762	7	54	theme	O-GlcNAcylated	1262:1275	arg1	proteins					1277:1284	cell cycle-dependent putative O-GlcNAcylated proteins	1232:1284	cell cycle-dependent putative O-GlcNAcylated proteins	1232:1284	A combination of two-dimensional electrophoresis, Western blotting and mass spectrometry was then used to detect and identify cell cycle-dependent putative O-GlcNAcylated proteins.
22967762	8	55	theme	Minichromosome	1458:1471	arg1	MCM7					1509:1512	MCM7	1509:1512	MCM7	1509:1512	58 cytoplasmic and nuclear proteins differentially O-GlcNAcylated through G1/S transition were identified and the O-GlcNAc variations of Cytokeratin 8, hnRNP K, Caprin-1, Minichromosome Maintenance proteins MCM3, MCM6 and MCM7 were validated by immunoprecipitation.
22967762	8	55	theme	Minichromosome	1458:1471	arg1	proteins					1485:1492	Minichromosome Maintenance proteins MCM3, MCM6 and MCM7	1458:1512	Minichromosome Maintenance proteins MCM3, MCM6 and MCM7	1458:1512	58 cytoplasmic and nuclear proteins differentially O-GlcNAcylated through G1/S transition were identified and the O-GlcNAc variations of Cytokeratin 8, hnRNP K, Caprin-1, Minichromosome Maintenance proteins MCM3, MCM6 and MCM7 were validated by immunoprecipitation.
22967762	8	55	theme	Minichromosome	1458:1471	arg1	MCM6					1500:1503	MCM6	1500:1503	MCM6	1500:1503	58 cytoplasmic and nuclear proteins differentially O-GlcNAcylated through G1/S transition were identified and the O-GlcNAc variations of Cytokeratin 8, hnRNP K, Caprin-1, Minichromosome Maintenance proteins MCM3, MCM6 and MCM7 were validated by immunoprecipitation.
22967762	8	55	theme	Minichromosome	1458:1471	arg1	Cytokeratin					1424:1434	Cytokeratin 8	1424:1436	Cytokeratin 8	1424:1436	58 cytoplasmic and nuclear proteins differentially O-GlcNAcylated through G1/S transition were identified and the O-GlcNAc variations of Cytokeratin 8, hnRNP K, Caprin-1, Minichromosome Maintenance proteins MCM3, MCM6 and MCM7 were validated by immunoprecipitation.
22967762	8	55	theme	Minichromosome	1458:1471	arg1	MCM3					1494:1497	MCM3	1494:1497	MCM3	1494:1497	58 cytoplasmic and nuclear proteins differentially O-GlcNAcylated through G1/S transition were identified and the O-GlcNAc variations of Cytokeratin 8, hnRNP K, Caprin-1, Minichromosome Maintenance proteins MCM3, MCM6 and MCM7 were validated by immunoprecipitation.
22967762	1	56	theme	DNA	143:145	arg1	replication					147:157	BACKGROUND DNA replication	132:157	BACKGROUND DNA replication	132:157	BACKGROUND DNA replication represents a critical step of the cell cycle which requires highly controlled and ordered regulatory mechanisms to ensure the integrity of genome duplication.
22967762	7	57	theme	blotting	1164:1171	arg1	combination					1108:1118	A combination	1106:1118	A combination of two-dimensional electrophoresis, Western blotting and mass spectrometry	1106:1193	A combination of two-dimensional electrophoresis, Western blotting and mass spectrometry was then used to detect and identify cell cycle-dependent putative O-GlcNAcylated proteins.
22967762	9	58	dep	CONCLUSIONS	1553:1563	arg1	observed					1630:1637	observed	1630:1637	observed on key proteins involved in the cytoskeleton networks, mRNA processing, translation, protein folding and DNA replication	1630:1758	CONCLUSIONS The dynamics of O-GlcNAc is regulated during G1/S transition and observed on key proteins involved in the cytoskeleton networks, mRNA processing, translation, protein folding and DNA replication.
22967762	9	58	dep	CONCLUSIONS	1553:1563	arg1	regulated					1593:1601	regulated	1593:1601	regulated during G1/S transition	1593:1624	CONCLUSIONS The dynamics of O-GlcNAc is regulated during G1/S transition and observed on key proteins involved in the cytoskeleton networks, mRNA processing, translation, protein folding and DNA replication.
22967762	7	59	theme	putative	1253:1260	arg1	proteins					1277:1284	cell cycle-dependent putative O-GlcNAcylated proteins	1232:1284	cell cycle-dependent putative O-GlcNAcylated proteins	1232:1284	A combination of two-dimensional electrophoresis, Western blotting and mass spectrometry was then used to detect and identify cell cycle-dependent putative O-GlcNAcylated proteins.
22967762	9	60	theme	G1/S	1610:1613	arg1	transition					1615:1624	G1/S transition	1610:1624	G1/S transition	1610:1624	CONCLUSIONS The dynamics of O-GlcNAc is regulated during G1/S transition and observed on key proteins involved in the cytoskeleton networks, mRNA processing, translation, protein folding and DNA replication.
22967762	9	61	theme	key	1642:1644	arg1	proteins					1646:1653	key proteins	1642:1653	key proteins involved in the cytoskeleton networks, mRNA processing, translation, protein folding and DNA replication	1642:1758	CONCLUSIONS The dynamics of O-GlcNAc is regulated during G1/S transition and observed on key proteins involved in the cytoskeleton networks, mRNA processing, translation, protein folding and DNA replication.
22967762	7	62	theme	spectrometry	1182:1193	arg1	combination					1108:1118	A combination	1106:1118	A combination of two-dimensional electrophoresis, Western blotting and mass spectrometry	1106:1193	A combination of two-dimensional electrophoresis, Western blotting and mass spectrometry was then used to detect and identify cell cycle-dependent putative O-GlcNAcylated proteins.
22967762	9	63	theme	cytoskeleton	1671:1682	arg1	replication					1748:1758	DNA replication	1744:1758	DNA replication	1744:1758	CONCLUSIONS The dynamics of O-GlcNAc is regulated during G1/S transition and observed on key proteins involved in the cytoskeleton networks, mRNA processing, translation, protein folding and DNA replication.
22967762	9	63	theme	cytoskeleton	1671:1682	arg1	translation					1711:1721	translation	1711:1721	translation	1711:1721	CONCLUSIONS The dynamics of O-GlcNAc is regulated during G1/S transition and observed on key proteins involved in the cytoskeleton networks, mRNA processing, translation, protein folding and DNA replication.
22967762	9	63	theme	cytoskeleton	1671:1682	arg1	networks					1684:1691	the cytoskeleton networks	1667:1691	the cytoskeleton networks	1667:1691	CONCLUSIONS The dynamics of O-GlcNAc is regulated during G1/S transition and observed on key proteins involved in the cytoskeleton networks, mRNA processing, translation, protein folding and DNA replication.
22967762	9	63	theme	cytoskeleton	1671:1682	arg1	processing					1699:1708	mRNA processing	1694:1708	mRNA processing	1694:1708	CONCLUSIONS The dynamics of O-GlcNAc is regulated during G1/S transition and observed on key proteins involved in the cytoskeleton networks, mRNA processing, translation, protein folding and DNA replication.
22967762	9	63	theme	cytoskeleton	1671:1682	arg1	folding					1732:1738	protein folding	1724:1738	protein folding	1724:1738	CONCLUSIONS The dynamics of O-GlcNAc is regulated during G1/S transition and observed on key proteins involved in the cytoskeleton networks, mRNA processing, translation, protein folding and DNA replication.
22967762	10	64	theme	GENERAL	1761:1767	arg1	SIGNIFICANCE					1769:1780	GENERAL SIGNIFICANCE	1761:1780	GENERAL SIGNIFICANCE	1761:1780	GENERAL SIGNIFICANCE Our results led us to propose that O-GlcNAcylation joins the PTMs that take part in the regulation of DNA replication initiation.
22967762	8	65	dep	proteins	1485:1492	arg1	MCM7					1509:1512	MCM7	1509:1512	MCM7	1509:1512	58 cytoplasmic and nuclear proteins differentially O-GlcNAcylated through G1/S transition were identified and the O-GlcNAc variations of Cytokeratin 8, hnRNP K, Caprin-1, Minichromosome Maintenance proteins MCM3, MCM6 and MCM7 were validated by immunoprecipitation.
22967762	8	65	dep	proteins	1485:1492	arg1	proteins					1485:1492	Minichromosome Maintenance proteins MCM3, MCM6 and MCM7	1458:1512	Minichromosome Maintenance proteins MCM3, MCM6 and MCM7	1458:1512	58 cytoplasmic and nuclear proteins differentially O-GlcNAcylated through G1/S transition were identified and the O-GlcNAc variations of Cytokeratin 8, hnRNP K, Caprin-1, Minichromosome Maintenance proteins MCM3, MCM6 and MCM7 were validated by immunoprecipitation.
22967762	8	65	dep	proteins	1485:1492	arg1	MCM6					1500:1503	MCM6	1500:1503	MCM6	1500:1503	58 cytoplasmic and nuclear proteins differentially O-GlcNAcylated through G1/S transition were identified and the O-GlcNAc variations of Cytokeratin 8, hnRNP K, Caprin-1, Minichromosome Maintenance proteins MCM3, MCM6 and MCM7 were validated by immunoprecipitation.
22967762	8	65	dep	proteins	1485:1492	arg1	MCM3					1494:1497	MCM3	1494:1497	MCM3	1494:1497	58 cytoplasmic and nuclear proteins differentially O-GlcNAcylated through G1/S transition were identified and the O-GlcNAc variations of Cytokeratin 8, hnRNP K, Caprin-1, Minichromosome Maintenance proteins MCM3, MCM6 and MCM7 were validated by immunoprecipitation.
22967762	1	66	theme	regulatory	249:258	arg1	mechanisms					260:269	ordered regulatory mechanisms	241:269	ordered regulatory mechanisms	241:269	BACKGROUND DNA replication represents a critical step of the cell cycle which requires highly controlled and ordered regulatory mechanisms to ensure the integrity of genome duplication.
22967762	8	67	theme	Maintenance	1473:1483	arg1	MCM7					1509:1512	MCM7	1509:1512	MCM7	1509:1512	58 cytoplasmic and nuclear proteins differentially O-GlcNAcylated through G1/S transition were identified and the O-GlcNAc variations of Cytokeratin 8, hnRNP K, Caprin-1, Minichromosome Maintenance proteins MCM3, MCM6 and MCM7 were validated by immunoprecipitation.
22967762	8	67	theme	Maintenance	1473:1483	arg1	proteins					1485:1492	Minichromosome Maintenance proteins MCM3, MCM6 and MCM7	1458:1512	Minichromosome Maintenance proteins MCM3, MCM6 and MCM7	1458:1512	58 cytoplasmic and nuclear proteins differentially O-GlcNAcylated through G1/S transition were identified and the O-GlcNAc variations of Cytokeratin 8, hnRNP K, Caprin-1, Minichromosome Maintenance proteins MCM3, MCM6 and MCM7 were validated by immunoprecipitation.
22967762	8	67	theme	Maintenance	1473:1483	arg1	MCM6					1500:1503	MCM6	1500:1503	MCM6	1500:1503	58 cytoplasmic and nuclear proteins differentially O-GlcNAcylated through G1/S transition were identified and the O-GlcNAc variations of Cytokeratin 8, hnRNP K, Caprin-1, Minichromosome Maintenance proteins MCM3, MCM6 and MCM7 were validated by immunoprecipitation.
22967762	8	67	theme	Maintenance	1473:1483	arg1	Cytokeratin					1424:1434	Cytokeratin 8	1424:1436	Cytokeratin 8	1424:1436	58 cytoplasmic and nuclear proteins differentially O-GlcNAcylated through G1/S transition were identified and the O-GlcNAc variations of Cytokeratin 8, hnRNP K, Caprin-1, Minichromosome Maintenance proteins MCM3, MCM6 and MCM7 were validated by immunoprecipitation.
22967762	8	67	theme	Maintenance	1473:1483	arg1	MCM3					1494:1497	MCM3	1494:1497	MCM3	1494:1497	58 cytoplasmic and nuclear proteins differentially O-GlcNAcylated through G1/S transition were identified and the O-GlcNAc variations of Cytokeratin 8, hnRNP K, Caprin-1, Minichromosome Maintenance proteins MCM3, MCM6 and MCM7 were validated by immunoprecipitation.
22967762	2	68	theme	post-translational	348:365	arg1	PTMs					382:385	PTMs	382:385	PTMs	382:385	Among a plethora of elements, post-translational modifications (PTMs) ensure the spatiotemporal regulation of pivotal proteins orchestrating cell division.
22967762	2	68	theme	post-translational	348:365	arg1	modifications					367:379	post-translational modifications	348:379	post-translational modifications (PTMs)	348:386	Among a plethora of elements, post-translational modifications (PTMs) ensure the spatiotemporal regulation of pivotal proteins orchestrating cell division.
22967762	8	69	theme	O-GlcNAc	1401:1408	arg1	variations					1410:1419	the O-GlcNAc variations	1397:1419	the O-GlcNAc variations of Cytokeratin 8, hnRNP K, Caprin-1, Minichromosome Maintenance proteins MCM3, MCM6 and MCM7	1397:1512	58 cytoplasmic and nuclear proteins differentially O-GlcNAcylated through G1/S transition were identified and the O-GlcNAc variations of Cytokeratin 8, hnRNP K, Caprin-1, Minichromosome Maintenance proteins MCM3, MCM6 and MCM7 were validated by immunoprecipitation.
22967762	5	70	theme	cells	962:966	arg1	progression					947:957	the progression	943:957	the progression of cells towards S phase	943:982	The levels of O-GlcNAc modified proteins, O-GlcNAc Transferase (OGT) and O-GlcNAcase (OGA) were examined by Western blotting and OGA activity was measured during the progression of cells towards S phase.
22967762	0	71	theme	O-GlcNAcylated	84:97	arg1	proteins					99:106	differentially O-GlcNAcylated proteins	69:106	differentially O-GlcNAcylated proteins during G1/S transition	69:129	Characterization of O-GlcNAc cycling and proteomic identification of differentially O-GlcNAcylated proteins during G1/S transition.
22967762	10	72	theme	replication	1888:1898	arg1	initiation					1900:1909	DNA replication initiation	1884:1909	DNA replication initiation	1884:1909	GENERAL SIGNIFICANCE Our results led us to propose that O-GlcNAcylation joins the PTMs that take part in the regulation of DNA replication initiation.
22967762	9	73	theme	O-GlcNAc	1581:1588	arg1	dynamics					1569:1576	The dynamics	1565:1576	The dynamics of O-GlcNAc	1565:1588	CONCLUSIONS The dynamics of O-GlcNAc is regulated during G1/S transition and observed on key proteins involved in the cytoskeleton networks, mRNA processing, translation, protein folding and DNA replication.
22967762	2	74	theme	spatiotemporal	399:412	arg1	regulation					414:423	the spatiotemporal regulation	395:423	the spatiotemporal regulation of pivotal proteins orchestrating cell division	395:471	Among a plethora of elements, post-translational modifications (PTMs) ensure the spatiotemporal regulation of pivotal proteins orchestrating cell division.
22967762	2	75	theme	pivotal	428:434	arg1	proteins					436:443	pivotal proteins	428:443	pivotal proteins orchestrating cell division	428:471	Among a plethora of elements, post-translational modifications (PTMs) ensure the spatiotemporal regulation of pivotal proteins orchestrating cell division.
22967762	4	76	theme	MCF7	675:678	arg1	cells					680:684	Quiescent MCF7 cells	665:684	Quiescent MCF7 cells	665:684	METHODS AND RESULTS Quiescent MCF7 cells were stimulated by serum mitogens and cell cycle progression was determined by flow cytometry.
22967762	5	77	theme	proteins	813:820	arg1	levels					785:790	The levels	781:790	The levels of O-GlcNAc modified proteins, O-GlcNAc Transferase (OGT) and O-GlcNAcase (OGA)	781:870	The levels of O-GlcNAc modified proteins, O-GlcNAc Transferase (OGT) and O-GlcNAcase (OGA) were examined by Western blotting and OGA activity was measured during the progression of cells towards S phase.
22967762	6	78	theme	S	1038:1038	arg1	entry					1046:1050	S phase entry	1038:1050	S phase entry	1038:1050	A global decrease in O-GlcNAcylation was observed at S phase entry, concomitantly to an increase in the activity of OGA.
22967762	4	79	theme	cycle	729:733	arg1	progression					735:745	cell cycle progression	724:745	cell cycle progression	724:745	METHODS AND RESULTS Quiescent MCF7 cells were stimulated by serum mitogens and cell cycle progression was determined by flow cytometry.
22967762	4	80	theme	Quiescent	665:673	arg1	cells					680:684	Quiescent MCF7 cells	665:684	Quiescent MCF7 cells	665:684	METHODS AND RESULTS Quiescent MCF7 cells were stimulated by serum mitogens and cell cycle progression was determined by flow cytometry.
26883802	7	0	theme	UDP-GlcNAc	1234:1243	arg1	supply					1245:1250	UDP-GlcNAc supply	1234:1250	UDP-GlcNAc supply	1234:1250	Increasing O-GlcNAcylation reproduced the effects of UDP-GlcNAc surplus on HAS3 trafficking, while its suppression showed the opposite effects, indicating that O-GlcNAc signaling is associated to UDP-GlcNAc supply.
26883802	3	1	theme	present	468:474	arg1	study					476:480	the present study	464:480	the present study	464:480	For the very first time, the present study demonstrated a rapid recycling of HAS3 between PM and endosomes, controlled by the cytosolic levels of the HAS substrates UDP-GlcUA and UDP-GlcNAc.
26883802	1	2	theme	synthesis	250:258	arg1	basis					237:241	the molecular basis	223:241	the molecular basis of its synthesis in cancer	223:268	Hyaluronan content is a powerful prognostic factor in many cancer types, but the molecular basis of its synthesis in cancer still remains unclear.
26883802	9	3	theme	hyaluronan	1660:1669	arg1	synthesis					1671:1679	hyaluronan synthesis	1660:1679	hyaluronan synthesis	1660:1679	In general, changes in glucose metabolism, realized through UDP-sugar contents and O-GlcNAc signaling, are important in HAS3 trafficking, hyaluronan synthesis, and correlates with melanoma progression.
26883802	2	4	from	transport	327:335	arg1	Golgi					375:379	Golgi	375:379	Golgi	375:379	Hyaluronan synthesis requires the transport of hyaluronan synthases (HAS1-3) from Golgi to plasma membrane (PM), where the enzymes are activated.
26883802	9	5	from	general	1525:1531	arg1	important					1629:1637	important	1629:1637	important	1629:1637	In general, changes in glucose metabolism, realized through UDP-sugar contents and O-GlcNAc signaling, are important in HAS3 trafficking, hyaluronan synthesis, and correlates with melanoma progression.
26883802	7	6	theme	UDP-GlcNAc	1091:1100	arg1	surplus					1102:1108	UDP-GlcNAc surplus	1091:1108	UDP-GlcNAc surplus	1091:1108	Increasing O-GlcNAcylation reproduced the effects of UDP-GlcNAc surplus on HAS3 trafficking, while its suppression showed the opposite effects, indicating that O-GlcNAc signaling is associated to UDP-GlcNAc supply.
26883802	3	7	theme	rapid	497:501	arg1	recycling					503:511	a rapid recycling	495:511	a rapid recycling of HAS3 between PM and endosomes, controlled by the cytosolic levels of the HAS substrates UDP-GlcUA and UDP-GlcNAc	495:627	For the very first time, the present study demonstrated a rapid recycling of HAS3 between PM and endosomes, controlled by the cytosolic levels of the HAS substrates UDP-GlcUA and UDP-GlcNAc.
26883802	8	8	from	content	1394:1400	arg1	melanomas					1426:1434	early and deep human melanomas	1405:1434	early and deep human melanomas	1405:1434	Importantly, a similar correlation existed between the expression of GFAT1 (the rate limiting enzyme in UDP-GlcNAc synthesis) and hyaluronan content in early and deep human melanomas, suggesting the association of UDP-sugar metabolism in initiation of melanomagenesis.
26883802	1	9	theme	many	200:203	arg1	types					212:216	many cancer types	200:216	many cancer types	200:216	Hyaluronan content is a powerful prognostic factor in many cancer types, but the molecular basis of its synthesis in cancer still remains unclear.
26883802	9	10	theme	melanoma	1702:1709	arg1	progression					1711:1721	melanoma progression	1702:1721	melanoma progression	1702:1721	In general, changes in glucose metabolism, realized through UDP-sugar contents and O-GlcNAc signaling, are important in HAS3 trafficking, hyaluronan synthesis, and correlates with melanoma progression.
26883802	8	11	theme	UDP-GlcNAc	1357:1366	arg1	synthesis					1368:1376	UDP-GlcNAc synthesis	1357:1376	UDP-GlcNAc synthesis	1357:1376	Importantly, a similar correlation existed between the expression of GFAT1 (the rate limiting enzyme in UDP-GlcNAc synthesis) and hyaluronan content in early and deep human melanomas, suggesting the association of UDP-sugar metabolism in initiation of melanomagenesis.
26883802	1	12	from	cancer	263:268	arg1	basis					237:241	the molecular basis	223:241	the molecular basis of its synthesis in cancer	223:268	Hyaluronan content is a powerful prognostic factor in many cancer types, but the molecular basis of its synthesis in cancer still remains unclear.
26883802	2	13	theme	Hyaluronan	293:302	arg1	synthesis					304:312	Hyaluronan synthesis	293:312	Hyaluronan synthesis	293:312	Hyaluronan synthesis requires the transport of hyaluronan synthases (HAS1-3) from Golgi to plasma membrane (PM), where the enzymes are activated.
26883802	5	14	theme	lysosomal	812:820	arg1	decay					822:826	lysosomal decay	812:826	lysosomal decay	812:826	In contrast, UDP-GlcNAc surplus suppressed endocytosis and lysosomal decay of HAS3, favoring its retention in PM, stimulating hyaluronan synthesis, and HAS3 shedding in extracellular vesicles.
26883802	1	15	from	synthesis	250:258	arg1	cancer					263:268	cancer	263:268	cancer	263:268	Hyaluronan content is a powerful prognostic factor in many cancer types, but the molecular basis of its synthesis in cancer still remains unclear.
26883802	9	16	from	synthesis	1671:1679	arg1	important					1629:1637	important	1629:1637	important	1629:1637	In general, changes in glucose metabolism, realized through UDP-sugar contents and O-GlcNAc signaling, are important in HAS3 trafficking, hyaluronan synthesis, and correlates with melanoma progression.
26883802	5	17	theme	hyaluronan	879:888	arg1	synthesis					890:898	stimulating hyaluronan synthesis	867:898	stimulating hyaluronan synthesis	867:898	In contrast, UDP-GlcNAc surplus suppressed endocytosis and lysosomal decay of HAS3, favoring its retention in PM, stimulating hyaluronan synthesis, and HAS3 shedding in extracellular vesicles.
26883802	9	18	from	changes	1534:1540	arg1	metabolism					1553:1562	glucose metabolism	1545:1562	glucose metabolism	1545:1562	In general, changes in glucose metabolism, realized through UDP-sugar contents and O-GlcNAc signaling, are important in HAS3 trafficking, hyaluronan synthesis, and correlates with melanoma progression.
26883802	1	19	theme	Hyaluronan	146:155	arg1	factor					190:195	a powerful prognostic factor	168:195	a powerful prognostic factor in many cancer types	168:216	Hyaluronan content is a powerful prognostic factor in many cancer types, but the molecular basis of its synthesis in cancer still remains unclear.
26883802	1	19	theme	Hyaluronan	146:155	arg1	content					157:163	Hyaluronan content	146:163	Hyaluronan content	146:163	Hyaluronan content is a powerful prognostic factor in many cancer types, but the molecular basis of its synthesis in cancer still remains unclear.
26883802	8	20	theme	metabolism	1477:1486	arg1	association					1452:1462	the association	1448:1462	the association of UDP-sugar metabolism in initiation of melanomagenesis	1448:1519	Importantly, a similar correlation existed between the expression of GFAT1 (the rate limiting enzyme in UDP-GlcNAc synthesis) and hyaluronan content in early and deep human melanomas, suggesting the association of UDP-sugar metabolism in initiation of melanomagenesis.
26883802	8	21	theme	GFAT1	1322:1326	arg1	expression					1308:1317	the expression	1304:1317	the expression of GFAT1 (the rate limiting enzyme in UDP-GlcNAc synthesis)	1304:1377	Importantly, a similar correlation existed between the expression of GFAT1 (the rate limiting enzyme in UDP-GlcNAc synthesis) and hyaluronan content in early and deep human melanomas, suggesting the association of UDP-sugar metabolism in initiation of melanomagenesis.
26883802	8	21	theme	GFAT1	1322:1326	arg1	content					1394:1400	hyaluronan content	1383:1400	hyaluronan content in early and deep human melanomas	1383:1434	Importantly, a similar correlation existed between the expression of GFAT1 (the rate limiting enzyme in UDP-GlcNAc synthesis) and hyaluronan content in early and deep human melanomas, suggesting the association of UDP-sugar metabolism in initiation of melanomagenesis.
26883802	3	22	theme	cytosolic	565:573	arg1	levels					575:580	the cytosolic levels	561:580	the cytosolic levels of the HAS substrates UDP-GlcUA and UDP-GlcNAc	561:627	For the very first time, the present study demonstrated a rapid recycling of HAS3 between PM and endosomes, controlled by the cytosolic levels of the HAS substrates UDP-GlcUA and UDP-GlcNAc.
26883802	4	23	theme	UDP-GlcUA	657:665	arg1	Depletion					630:638	Depletion	630:638	Depletion of UDP-GlcNAc or UDP-GlcUA	630:665	Depletion of UDP-GlcNAc or UDP-GlcUA shifted the balance towards HAS3 endocytosis, and inhibition of hyaluronan synthesis.
26883802	8	24	from	expression	1308:1317	arg1	melanomas					1426:1434	early and deep human melanomas	1405:1434	early and deep human melanomas	1405:1434	Importantly, a similar correlation existed between the expression of GFAT1 (the rate limiting enzyme in UDP-GlcNAc synthesis) and hyaluronan content in early and deep human melanomas, suggesting the association of UDP-sugar metabolism in initiation of melanomagenesis.
26883802	1	25	theme	powerful	170:177	arg1	factor					190:195	a powerful prognostic factor	168:195	a powerful prognostic factor in many cancer types	168:216	Hyaluronan content is a powerful prognostic factor in many cancer types, but the molecular basis of its synthesis in cancer still remains unclear.
26883802	1	25	theme	powerful	170:177	arg1	content					157:163	Hyaluronan content	146:163	Hyaluronan content	146:163	Hyaluronan content is a powerful prognostic factor in many cancer types, but the molecular basis of its synthesis in cancer still remains unclear.
26883802	6	26	theme	UDP-GlcNAc	967:976	arg1	concentration					950:962	The concentration	946:962	The concentration of UDP-GlcNAc	946:976	The concentration of UDP-GlcNAc also controlled the level of O-GlcNAc modification of HAS3.
26883802	8	27	theme	melanomagenesis	1505:1519	arg1	initiation					1491:1500	initiation	1491:1500	initiation of melanomagenesis	1491:1519	Importantly, a similar correlation existed between the expression of GFAT1 (the rate limiting enzyme in UDP-GlcNAc synthesis) and hyaluronan content in early and deep human melanomas, suggesting the association of UDP-sugar metabolism in initiation of melanomagenesis.
26883802	7	28	theme	O-GlcNAc	1198:1205	arg1	signaling					1207:1215	O-GlcNAc signaling	1198:1215	O-GlcNAc signaling	1198:1215	Increasing O-GlcNAcylation reproduced the effects of UDP-GlcNAc surplus on HAS3 trafficking, while its suppression showed the opposite effects, indicating that O-GlcNAc signaling is associated to UDP-GlcNAc supply.
26883802	5	29	from	retention	850:858	arg1	PM					863:864	PM	863:864	PM	863:864	In contrast, UDP-GlcNAc surplus suppressed endocytosis and lysosomal decay of HAS3, favoring its retention in PM, stimulating hyaluronan synthesis, and HAS3 shedding in extracellular vesicles.
26883802	5	29	from	retention	850:858	arg1	shedding					910:917	HAS3 shedding	905:917	HAS3 shedding	905:917	In contrast, UDP-GlcNAc surplus suppressed endocytosis and lysosomal decay of HAS3, favoring its retention in PM, stimulating hyaluronan synthesis, and HAS3 shedding in extracellular vesicles.
26883802	5	29	from	retention	850:858	arg1	synthesis					890:898	stimulating hyaluronan synthesis	867:898	stimulating hyaluronan synthesis	867:898	In contrast, UDP-GlcNAc surplus suppressed endocytosis and lysosomal decay of HAS3, favoring its retention in PM, stimulating hyaluronan synthesis, and HAS3 shedding in extracellular vesicles.
26883802	5	29	from	retention	850:858	arg1	vesicles					936:943	extracellular vesicles	922:943	extracellular vesicles	922:943	In contrast, UDP-GlcNAc surplus suppressed endocytosis and lysosomal decay of HAS3, favoring its retention in PM, stimulating hyaluronan synthesis, and HAS3 shedding in extracellular vesicles.
26883802	9	30	theme	glucose	1545:1551	arg1	metabolism					1553:1562	glucose metabolism	1545:1562	glucose metabolism	1545:1562	In general, changes in glucose metabolism, realized through UDP-sugar contents and O-GlcNAc signaling, are important in HAS3 trafficking, hyaluronan synthesis, and correlates with melanoma progression.
26883802	4	31	theme	synthesis	742:750	arg1	balance					679:685	the balance	675:685	the balance towards HAS3 endocytosis	675:710	Depletion of UDP-GlcNAc or UDP-GlcUA shifted the balance towards HAS3 endocytosis, and inhibition of hyaluronan synthesis.
26883802	4	31	theme	synthesis	742:750	arg1	inhibition					717:726	inhibition	717:726	inhibition of hyaluronan synthesis	717:750	Depletion of UDP-GlcNAc or UDP-GlcUA shifted the balance towards HAS3 endocytosis, and inhibition of hyaluronan synthesis.
26883802	0	32	theme	UDP-sugar	0:8	arg1	substrates					10:19	UDP-sugar substrates	0:19	UDP-sugar substrates of HAS3	0:27	UDP-sugar substrates of HAS3 regulate its O-GlcNAcylation, intracellular traffic, extracellular shedding and correlate with melanoma progression.
26883802	5	33	theme	HAS3	905:908	arg1	shedding					910:917	HAS3 shedding	905:917	HAS3 shedding	905:917	In contrast, UDP-GlcNAc surplus suppressed endocytosis and lysosomal decay of HAS3, favoring its retention in PM, stimulating hyaluronan synthesis, and HAS3 shedding in extracellular vesicles.
26883802	7	34	from	effects	1080:1086	arg1	trafficking					1118:1128	HAS3 trafficking	1113:1128	HAS3 trafficking	1113:1128	Increasing O-GlcNAcylation reproduced the effects of UDP-GlcNAc surplus on HAS3 trafficking, while its suppression showed the opposite effects, indicating that O-GlcNAc signaling is associated to UDP-GlcNAc supply.
26883802	4	35	theme	UDP-GlcNAc	643:652	arg1	Depletion					630:638	Depletion	630:638	Depletion of UDP-GlcNAc or UDP-GlcUA	630:665	Depletion of UDP-GlcNAc or UDP-GlcUA shifted the balance towards HAS3 endocytosis, and inhibition of hyaluronan synthesis.
26883802	5	36	theme	HAS3	831:834	arg1	decay					822:826	lysosomal decay	812:826	lysosomal decay	812:826	In contrast, UDP-GlcNAc surplus suppressed endocytosis and lysosomal decay of HAS3, favoring its retention in PM, stimulating hyaluronan synthesis, and HAS3 shedding in extracellular vesicles.
26883802	5	36	theme	HAS3	831:834	arg1	endocytosis					796:806	endocytosis	796:806	endocytosis	796:806	In contrast, UDP-GlcNAc surplus suppressed endocytosis and lysosomal decay of HAS3, favoring its retention in PM, stimulating hyaluronan synthesis, and HAS3 shedding in extracellular vesicles.
26883802	9	37	theme	O-GlcNAc	1605:1612	arg1	signaling					1614:1622	O-GlcNAc signaling	1605:1622	O-GlcNAc signaling	1605:1622	In general, changes in glucose metabolism, realized through UDP-sugar contents and O-GlcNAc signaling, are important in HAS3 trafficking, hyaluronan synthesis, and correlates with melanoma progression.
26883802	6	38	theme	O-GlcNAc	1007:1014	arg1	modification					1016:1027	O-GlcNAc modification	1007:1027	O-GlcNAc modification of HAS3	1007:1035	The concentration of UDP-GlcNAc also controlled the level of O-GlcNAc modification of HAS3.
26883802	8	39	theme	early	1405:1409	arg1	melanomas					1426:1434	early and deep human melanomas	1405:1434	early and deep human melanomas	1405:1434	Importantly, a similar correlation existed between the expression of GFAT1 (the rate limiting enzyme in UDP-GlcNAc synthesis) and hyaluronan content in early and deep human melanomas, suggesting the association of UDP-sugar metabolism in initiation of melanomagenesis.
26883802	2	40	theme	synthases	351:359	arg1	transport					327:335	the transport	323:335	the transport of hyaluronan synthases (HAS1-3) from Golgi to plasma membrane (PM), where the enzymes are activated	323:436	Hyaluronan synthesis requires the transport of hyaluronan synthases (HAS1-3) from Golgi to plasma membrane (PM), where the enzymes are activated.
26883802	8	41	theme	deep	1415:1418	arg1	melanomas					1426:1434	early and deep human melanomas	1405:1434	early and deep human melanomas	1405:1434	Importantly, a similar correlation existed between the expression of GFAT1 (the rate limiting enzyme in UDP-GlcNAc synthesis) and hyaluronan content in early and deep human melanomas, suggesting the association of UDP-sugar metabolism in initiation of melanomagenesis.
26883802	8	42	from	enzyme	1347:1352	arg1	synthesis					1368:1376	UDP-GlcNAc synthesis	1357:1376	UDP-GlcNAc synthesis	1357:1376	Importantly, a similar correlation existed between the expression of GFAT1 (the rate limiting enzyme in UDP-GlcNAc synthesis) and hyaluronan content in early and deep human melanomas, suggesting the association of UDP-sugar metabolism in initiation of melanomagenesis.
26883802	3	43	dep	the	585:587	arg1	HAS					589:591	HAS	589:591	HAS substrates UDP-GlcUA and UDP-GlcNAc	589:627	For the very first time, the present study demonstrated a rapid recycling of HAS3 between PM and endosomes, controlled by the cytosolic levels of the HAS substrates UDP-GlcUA and UDP-GlcNAc.
26883802	0	44	with	O-GlcNAcylation	42:56	arg1	progression					133:143	melanoma progression	124:143	melanoma progression	124:143	UDP-sugar substrates of HAS3 regulate its O-GlcNAcylation, intracellular traffic, extracellular shedding and correlate with melanoma progression.
26883802	3	45	dep	substrates	593:602	arg1	substrates					593:602	substrates UDP-GlcUA and UDP-GlcNAc	593:627	substrates UDP-GlcUA and UDP-GlcNAc	593:627	For the very first time, the present study demonstrated a rapid recycling of HAS3 between PM and endosomes, controlled by the cytosolic levels of the HAS substrates UDP-GlcUA and UDP-GlcNAc.
26883802	3	45	dep	substrates	593:602	arg1	UDP-GlcNAc					618:627	UDP-GlcNAc	618:627	UDP-GlcNAc	618:627	For the very first time, the present study demonstrated a rapid recycling of HAS3 between PM and endosomes, controlled by the cytosolic levels of the HAS substrates UDP-GlcUA and UDP-GlcNAc.
26883802	3	45	dep	substrates	593:602	arg1	UDP-GlcUA					604:612	UDP-GlcUA	604:612	UDP-GlcUA	604:612	For the very first time, the present study demonstrated a rapid recycling of HAS3 between PM and endosomes, controlled by the cytosolic levels of the HAS substrates UDP-GlcUA and UDP-GlcNAc.
26883802	9	46	theme	HAS3	1642:1645	arg1	trafficking					1647:1657	HAS3 trafficking	1642:1657	HAS3 trafficking	1642:1657	In general, changes in glucose metabolism, realized through UDP-sugar contents and O-GlcNAc signaling, are important in HAS3 trafficking, hyaluronan synthesis, and correlates with melanoma progression.
26883802	7	47	theme	HAS3	1113:1116	arg1	trafficking					1118:1128	HAS3 trafficking	1113:1128	HAS3 trafficking	1113:1128	Increasing O-GlcNAcylation reproduced the effects of UDP-GlcNAc surplus on HAS3 trafficking, while its suppression showed the opposite effects, indicating that O-GlcNAc signaling is associated to UDP-GlcNAc supply.
26883802	9	48	with	trafficking	1647:1657	arg1	progression					1711:1721	melanoma progression	1702:1721	melanoma progression	1702:1721	In general, changes in glucose metabolism, realized through UDP-sugar contents and O-GlcNAc signaling, are important in HAS3 trafficking, hyaluronan synthesis, and correlates with melanoma progression.
26883802	6	49	mod	modification	1016:1027	arg3	O-GlcNAc					1007:1014	O-GlcNAc modification	1007:1027	O-GlcNAc modification of HAS3	1007:1035	The concentration of UDP-GlcNAc also controlled the level of O-GlcNAc modification of HAS3.
26883802	6	49	mod	modification	1016:1027	arg1	HAS3					1032:1035	HAS3	1032:1035	HAS3	1032:1035	The concentration of UDP-GlcNAc also controlled the level of O-GlcNAc modification of HAS3.
26883802	7	50	theme	surplus	1102:1108	arg1	effects					1080:1086	the effects	1076:1086	the effects of UDP-GlcNAc surplus on HAS3 trafficking	1076:1128	Increasing O-GlcNAcylation reproduced the effects of UDP-GlcNAc surplus on HAS3 trafficking, while its suppression showed the opposite effects, indicating that O-GlcNAc signaling is associated to UDP-GlcNAc supply.
26883802	9	51	with	synthesis	1671:1679	arg1	progression					1711:1721	melanoma progression	1702:1721	melanoma progression	1702:1721	In general, changes in glucose metabolism, realized through UDP-sugar contents and O-GlcNAc signaling, are important in HAS3 trafficking, hyaluronan synthesis, and correlates with melanoma progression.
26883802	9	52	with	correlates	1686:1695	arg1	progression					1711:1721	melanoma progression	1702:1721	melanoma progression	1702:1721	In general, changes in glucose metabolism, realized through UDP-sugar contents and O-GlcNAc signaling, are important in HAS3 trafficking, hyaluronan synthesis, and correlates with melanoma progression.
26883802	1	53	theme	prognostic	179:188	arg1	factor					190:195	a powerful prognostic factor	168:195	a powerful prognostic factor in many cancer types	168:216	Hyaluronan content is a powerful prognostic factor in many cancer types, but the molecular basis of its synthesis in cancer still remains unclear.
26883802	1	53	theme	prognostic	179:188	arg1	content					157:163	Hyaluronan content	146:163	Hyaluronan content	146:163	Hyaluronan content is a powerful prognostic factor in many cancer types, but the molecular basis of its synthesis in cancer still remains unclear.
26883802	0	54	with	correlate	109:117	arg1	progression					133:143	melanoma progression	124:143	melanoma progression	124:143	UDP-sugar substrates of HAS3 regulate its O-GlcNAcylation, intracellular traffic, extracellular shedding and correlate with melanoma progression.
26883802	9	55	from	correlates	1686:1695	arg1	important					1629:1637	important	1629:1637	important	1629:1637	In general, changes in glucose metabolism, realized through UDP-sugar contents and O-GlcNAc signaling, are important in HAS3 trafficking, hyaluronan synthesis, and correlates with melanoma progression.
26883802	0	56	with	shedding	96:103	arg1	progression					133:143	melanoma progression	124:143	melanoma progression	124:143	UDP-sugar substrates of HAS3 regulate its O-GlcNAcylation, intracellular traffic, extracellular shedding and correlate with melanoma progression.
26883802	3	57	theme	HAS3	516:519	arg1	recycling					503:511	a rapid recycling	495:511	a rapid recycling of HAS3 between PM and endosomes, controlled by the cytosolic levels of the HAS substrates UDP-GlcUA and UDP-GlcNAc	495:627	For the very first time, the present study demonstrated a rapid recycling of HAS3 between PM and endosomes, controlled by the cytosolic levels of the HAS substrates UDP-GlcUA and UDP-GlcNAc.
26883802	1	58	theme	cancer	205:210	arg1	types					212:216	many cancer types	200:216	many cancer types	200:216	Hyaluronan content is a powerful prognostic factor in many cancer types, but the molecular basis of its synthesis in cancer still remains unclear.
26883802	8	59	theme	similar	1268:1274	arg1	correlation					1276:1286	a similar correlation	1266:1286	a similar correlation	1266:1286	Importantly, a similar correlation existed between the expression of GFAT1 (the rate limiting enzyme in UDP-GlcNAc synthesis) and hyaluronan content in early and deep human melanomas, suggesting the association of UDP-sugar metabolism in initiation of melanomagenesis.
26883802	1	60	from	basis	237:241	arg1	cancer					263:268	cancer	263:268	cancer	263:268	Hyaluronan content is a powerful prognostic factor in many cancer types, but the molecular basis of its synthesis in cancer still remains unclear.
26883802	5	61	theme	stimulating	867:877	arg1	synthesis					890:898	stimulating hyaluronan synthesis	867:898	stimulating hyaluronan synthesis	867:898	In contrast, UDP-GlcNAc surplus suppressed endocytosis and lysosomal decay of HAS3, favoring its retention in PM, stimulating hyaluronan synthesis, and HAS3 shedding in extracellular vesicles.
26883802	9	62	from	trafficking	1647:1657	arg1	important					1629:1637	important	1629:1637	important	1629:1637	In general, changes in glucose metabolism, realized through UDP-sugar contents and O-GlcNAc signaling, are important in HAS3 trafficking, hyaluronan synthesis, and correlates with melanoma progression.
26883802	8	63	theme	UDP-sugar	1467:1475	arg1	metabolism					1477:1486	UDP-sugar metabolism	1467:1486	UDP-sugar metabolism	1467:1486	Importantly, a similar correlation existed between the expression of GFAT1 (the rate limiting enzyme in UDP-GlcNAc synthesis) and hyaluronan content in early and deep human melanomas, suggesting the association of UDP-sugar metabolism in initiation of melanomagenesis.
26883802	8	64	from	association	1452:1462	arg1	initiation					1491:1500	initiation	1491:1500	initiation of melanomagenesis	1491:1519	Importantly, a similar correlation existed between the expression of GFAT1 (the rate limiting enzyme in UDP-GlcNAc synthesis) and hyaluronan content in early and deep human melanomas, suggesting the association of UDP-sugar metabolism in initiation of melanomagenesis.
26883802	0	65	theme	extracellular	82:94	arg1	shedding					96:103	extracellular shedding	82:103	extracellular shedding	82:103	UDP-sugar substrates of HAS3 regulate its O-GlcNAcylation, intracellular traffic, extracellular shedding and correlate with melanoma progression.
26883802	1	66	from	factor	190:195	arg1	types					212:216	many cancer types	200:216	many cancer types	200:216	Hyaluronan content is a powerful prognostic factor in many cancer types, but the molecular basis of its synthesis in cancer still remains unclear.
26883802	0	67	theme	melanoma	124:131	arg1	progression					133:143	melanoma progression	124:143	melanoma progression	124:143	UDP-sugar substrates of HAS3 regulate its O-GlcNAcylation, intracellular traffic, extracellular shedding and correlate with melanoma progression.
26883802	5	68	theme	extracellular	922:934	arg1	vesicles					936:943	extracellular vesicles	922:943	extracellular vesicles	922:943	In contrast, UDP-GlcNAc surplus suppressed endocytosis and lysosomal decay of HAS3, favoring its retention in PM, stimulating hyaluronan synthesis, and HAS3 shedding in extracellular vesicles.
26883802	4	69	theme	hyaluronan	731:740	arg1	synthesis					742:750	hyaluronan synthesis	731:750	hyaluronan synthesis	731:750	Depletion of UDP-GlcNAc or UDP-GlcUA shifted the balance towards HAS3 endocytosis, and inhibition of hyaluronan synthesis.
26883802	2	70	theme	plasma	384:389	arg1	PM					401:402	PM	401:402	PM	401:402	Hyaluronan synthesis requires the transport of hyaluronan synthases (HAS1-3) from Golgi to plasma membrane (PM), where the enzymes are activated.
26883802	2	70	theme	plasma	384:389	arg1	membrane					391:398	plasma membrane	384:398	plasma membrane (PM)	384:403	Hyaluronan synthesis requires the transport of hyaluronan synthases (HAS1-3) from Golgi to plasma membrane (PM), where the enzymes are activated.
26883802	5	71	theme	UDP-GlcNAc	766:775	arg1	surplus					777:783	UDP-GlcNAc surplus	766:783	UDP-GlcNAc surplus	766:783	In contrast, UDP-GlcNAc surplus suppressed endocytosis and lysosomal decay of HAS3, favoring its retention in PM, stimulating hyaluronan synthesis, and HAS3 shedding in extracellular vesicles.
26883802	9	72	from	important	1629:1637	arg1	general					1525:1531	general	1525:1531	general	1525:1531	In general, changes in glucose metabolism, realized through UDP-sugar contents and O-GlcNAc signaling, are important in HAS3 trafficking, hyaluronan synthesis, and correlates with melanoma progression.
26883802	9	72	from	important	1629:1637	arg1	trafficking					1647:1657	HAS3 trafficking	1642:1657	HAS3 trafficking	1642:1657	In general, changes in glucose metabolism, realized through UDP-sugar contents and O-GlcNAc signaling, are important in HAS3 trafficking, hyaluronan synthesis, and correlates with melanoma progression.
26883802	9	72	from	important	1629:1637	arg1	synthesis					1671:1679	hyaluronan synthesis	1660:1679	hyaluronan synthesis	1660:1679	In general, changes in glucose metabolism, realized through UDP-sugar contents and O-GlcNAc signaling, are important in HAS3 trafficking, hyaluronan synthesis, and correlates with melanoma progression.
26883802	9	72	from	important	1629:1637	arg1	correlates					1686:1695	correlates	1686:1695	correlates with melanoma progression	1686:1721	In general, changes in glucose metabolism, realized through UDP-sugar contents and O-GlcNAc signaling, are important in HAS3 trafficking, hyaluronan synthesis, and correlates with melanoma progression.
26883802	4	73	theme	HAS3	695:698	arg1	endocytosis					700:710	HAS3 endocytosis	695:710	HAS3 endocytosis	695:710	Depletion of UDP-GlcNAc or UDP-GlcUA shifted the balance towards HAS3 endocytosis, and inhibition of hyaluronan synthesis.
26883802	0	74	theme	HAS3	24:27	arg1	substrates					10:19	UDP-sugar substrates	0:19	UDP-sugar substrates of HAS3	0:27	UDP-sugar substrates of HAS3 regulate its O-GlcNAcylation, intracellular traffic, extracellular shedding and correlate with melanoma progression.
26883802	9	75	theme	UDP-sugar	1582:1590	arg1	contents					1592:1599	UDP-sugar contents	1582:1599	UDP-sugar contents	1582:1599	In general, changes in glucose metabolism, realized through UDP-sugar contents and O-GlcNAc signaling, are important in HAS3 trafficking, hyaluronan synthesis, and correlates with melanoma progression.
26883802	6	76	theme	HAS3	1032:1035	arg1	modification					1016:1027	O-GlcNAc modification	1007:1027	O-GlcNAc modification of HAS3	1007:1035	The concentration of UDP-GlcNAc also controlled the level of O-GlcNAc modification of HAS3.
26883802	6	77	theme	modification	1016:1027	arg1	level					998:1002	the level	994:1002	the level of O-GlcNAc modification of HAS3	994:1035	The concentration of UDP-GlcNAc also controlled the level of O-GlcNAc modification of HAS3.
26883802	3	78	theme	the	585:587	arg1	levels					575:580	the cytosolic levels	561:580	the cytosolic levels of the HAS substrates UDP-GlcUA and UDP-GlcNAc	561:627	For the very first time, the present study demonstrated a rapid recycling of HAS3 between PM and endosomes, controlled by the cytosolic levels of the HAS substrates UDP-GlcUA and UDP-GlcNAc.
26883802	8	79	theme	hyaluronan	1383:1392	arg1	content					1394:1400	hyaluronan content	1383:1400	hyaluronan content in early and deep human melanomas	1383:1434	Importantly, a similar correlation existed between the expression of GFAT1 (the rate limiting enzyme in UDP-GlcNAc synthesis) and hyaluronan content in early and deep human melanomas, suggesting the association of UDP-sugar metabolism in initiation of melanomagenesis.
26883802	8	80	dep	GFAT1	1322:1326	arg1	rate					1333:1336	the rate	1329:1336	the rate limiting enzyme in UDP-GlcNAc synthesis	1329:1376	Importantly, a similar correlation existed between the expression of GFAT1 (the rate limiting enzyme in UDP-GlcNAc synthesis) and hyaluronan content in early and deep human melanomas, suggesting the association of UDP-sugar metabolism in initiation of melanomagenesis.
26883802	2	81	from	Golgi	375:379	arg1	HAS1-3					362:367	HAS1-3	362:367	HAS1-3	362:367	Hyaluronan synthesis requires the transport of hyaluronan synthases (HAS1-3) from Golgi to plasma membrane (PM), where the enzymes are activated.
26883802	2	81	from	Golgi	375:379	arg1	transport					327:335	the transport	323:335	the transport of hyaluronan synthases (HAS1-3) from Golgi to plasma membrane (PM), where the enzymes are activated	323:436	Hyaluronan synthesis requires the transport of hyaluronan synthases (HAS1-3) from Golgi to plasma membrane (PM), where the enzymes are activated.
26883802	2	81	from	Golgi	375:379	arg1	synthases					351:359	hyaluronan synthases	340:359	hyaluronan synthases (HAS1-3) from Golgi	340:379	Hyaluronan synthesis requires the transport of hyaluronan synthases (HAS1-3) from Golgi to plasma membrane (PM), where the enzymes are activated.
26883802	7	82	theme	Increasing	1038:1047	arg1	O-GlcNAcylation					1049:1063	Increasing O-GlcNAcylation	1038:1063	Increasing O-GlcNAcylation	1038:1063	Increasing O-GlcNAcylation reproduced the effects of UDP-GlcNAc surplus on HAS3 trafficking, while its suppression showed the opposite effects, indicating that O-GlcNAc signaling is associated to UDP-GlcNAc supply.
26883802	2	83	theme	hyaluronan	340:349	arg1	HAS1-3					362:367	HAS1-3	362:367	HAS1-3	362:367	Hyaluronan synthesis requires the transport of hyaluronan synthases (HAS1-3) from Golgi to plasma membrane (PM), where the enzymes are activated.
26883802	2	83	theme	hyaluronan	340:349	arg1	synthases					351:359	hyaluronan synthases	340:359	hyaluronan synthases (HAS1-3) from Golgi	340:379	Hyaluronan synthesis requires the transport of hyaluronan synthases (HAS1-3) from Golgi to plasma membrane (PM), where the enzymes are activated.
26883802	3	84	theme	first	452:456	arg1	time					458:461	the very first time	443:461	the very first time	443:461	For the very first time, the present study demonstrated a rapid recycling of HAS3 between PM and endosomes, controlled by the cytosolic levels of the HAS substrates UDP-GlcUA and UDP-GlcNAc.
26883802	1	85	theme	molecular	227:235	arg1	basis					237:241	the molecular basis	223:241	the molecular basis of its synthesis in cancer	223:268	Hyaluronan content is a powerful prognostic factor in many cancer types, but the molecular basis of its synthesis in cancer still remains unclear.
26883802	8	86	theme	human	1420:1424	arg1	melanomas					1426:1434	early and deep human melanomas	1405:1434	early and deep human melanomas	1405:1434	Importantly, a similar correlation existed between the expression of GFAT1 (the rate limiting enzyme in UDP-GlcNAc synthesis) and hyaluronan content in early and deep human melanomas, suggesting the association of UDP-sugar metabolism in initiation of melanomagenesis.
26883802	7	87	theme	opposite	1164:1171	arg1	effects					1173:1179	the opposite effects	1160:1179	the opposite effects	1160:1179	Increasing O-GlcNAcylation reproduced the effects of UDP-GlcNAc surplus on HAS3 trafficking, while its suppression showed the opposite effects, indicating that O-GlcNAc signaling is associated to UDP-GlcNAc supply.
16408927	6	0	theme	multiple	977:984	arg1	pathways					995:1002	multiple cellular pathways	977:1002	multiple cellular pathways	977:1002	Functional classification shows that proteins with diverse functions are modified by O-GlcNAc, implying that O-GlcNAc might be involved in the regulation of multiple cellular pathways.
16408927	5	1	theme	HeLa	740:743	arg1	cells					745:749	HeLa cells	740:749	HeLa cells	740:749	Our study led to the identification of 199 putative O-GlcNAc-modified proteins from HeLa cells, among which 23 were confirmed using reciprocal immunoprecipitation.
16408927	1	2	theme	cytosolic	196:204	arg1	proteins					218:225	cytosolic and nuclear proteins	196:225	cytosolic and nuclear proteins	196:225	The O-linked N-acetylglucosamine (O-GlcNAc) modification of serine/threonine residues is an abundant posttranslational modification present in cytosolic and nuclear proteins.
16408927	1	3	theme	N-acetylglucosamine	66:84	arg1	modification					172:183	an abundant posttranslational modification	142:183	an abundant posttranslational modification present in cytosolic and nuclear proteins	142:225	The O-linked N-acetylglucosamine (O-GlcNAc) modification of serine/threonine residues is an abundant posttranslational modification present in cytosolic and nuclear proteins.
16408927	1	3	theme	N-acetylglucosamine	66:84	arg1	modification					97:108	The O-linked N-acetylglucosamine (O-GlcNAc) modification	53:108	The O-linked N-acetylglucosamine (O-GlcNAc) modification of serine/threonine residues	53:137	The O-linked N-acetylglucosamine (O-GlcNAc) modification of serine/threonine residues is an abundant posttranslational modification present in cytosolic and nuclear proteins.
16408927	3	4	theme	O-GlcNAc-modified	413:429	arg1	proteins					431:438	O-GlcNAc-modified proteins	413:438	O-GlcNAc-modified proteins	413:438	Here we report the application of the tagging-via-substrate (TAS) approach for global identification of O-GlcNAc-modified proteins.
16408927	1	5	attach	present	185:191	arg1	proteins					218:225	cytosolic and nuclear proteins	196:225	cytosolic and nuclear proteins	196:225	The O-linked N-acetylglucosamine (O-GlcNAc) modification of serine/threonine residues is an abundant posttranslational modification present in cytosolic and nuclear proteins.
16408927	1	5	attach	present	185:191	arg2	modification					172:183	an abundant posttranslational modification	142:183	an abundant posttranslational modification present in cytosolic and nuclear proteins	142:225	The O-linked N-acetylglucosamine (O-GlcNAc) modification of serine/threonine residues is an abundant posttranslational modification present in cytosolic and nuclear proteins.
16408927	1	5	attach	present	185:191	arg2	modification					97:108	The O-linked N-acetylglucosamine (O-GlcNAc) modification	53:108	The O-linked N-acetylglucosamine (O-GlcNAc) modification of serine/threonine residues	53:137	The O-linked N-acetylglucosamine (O-GlcNAc) modification of serine/threonine residues is an abundant posttranslational modification present in cytosolic and nuclear proteins.
16408927	4	6	theme	O-GlcNAc	468:475	arg1	analogue					483:490	an O-GlcNAc azide analogue	465:490	an O-GlcNAc azide analogue	465:490	The TAS method utilizes an O-GlcNAc azide analogue for metabolic labeling of O-GlcNAc-modified proteins, which can be chemoselectively conjugated for detection and enrichment of the proteins for proteomics studies.
16408927	3	7	theme	global	388:393	arg1	identification					395:408	global identification	388:408	global identification of O-GlcNAc-modified proteins	388:438	Here we report the application of the tagging-via-substrate (TAS) approach for global identification of O-GlcNAc-modified proteins.
16408927	6	8	theme	pathways	995:1002	arg1	regulation					963:972	the regulation	959:972	the regulation of multiple cellular pathways	959:1002	Functional classification shows that proteins with diverse functions are modified by O-GlcNAc, implying that O-GlcNAc might be involved in the regulation of multiple cellular pathways.
16408927	1	9	from	present	185:191	arg1	proteins					218:225	cytosolic and nuclear proteins	196:225	cytosolic and nuclear proteins	196:225	The O-linked N-acetylglucosamine (O-GlcNAc) modification of serine/threonine residues is an abundant posttranslational modification present in cytosolic and nuclear proteins.
16408927	6	10	theme	cellular	986:993	arg1	pathways					995:1002	multiple cellular pathways	977:1002	multiple cellular pathways	977:1002	Functional classification shows that proteins with diverse functions are modified by O-GlcNAc, implying that O-GlcNAc might be involved in the regulation of multiple cellular pathways.
16408927	5	11	theme	putative	699:706	arg1	proteins					726:733	199 putative O-GlcNAc-modified proteins	695:733	199 putative O-GlcNAc-modified proteins from HeLa cells	695:749	Our study led to the identification of 199 putative O-GlcNAc-modified proteins from HeLa cells, among which 23 were confirmed using reciprocal immunoprecipitation.
16408927	3	12	dep	tagging-via-substrate	347:367	arg1	TAS					370:372	TAS	370:372	TAS	370:372	Here we report the application of the tagging-via-substrate (TAS) approach for global identification of O-GlcNAc-modified proteins.
16408927	0	13	theme	Global	0:5	arg1	identification					7:20	Global identification	0:20	Global identification of O-GlcNAc-modified proteins.	0:51	Global identification of O-GlcNAc-modified proteins.
16408927	1	14	theme	nuclear	210:216	arg1	proteins					218:225	cytosolic and nuclear proteins	196:225	cytosolic and nuclear proteins	196:225	The O-linked N-acetylglucosamine (O-GlcNAc) modification of serine/threonine residues is an abundant posttranslational modification present in cytosolic and nuclear proteins.
16408927	3	15	theme	proteins	431:438	arg1	identification					395:408	global identification	388:408	global identification of O-GlcNAc-modified proteins	388:438	Here we report the application of the tagging-via-substrate (TAS) approach for global identification of O-GlcNAc-modified proteins.
16408927	5	16	theme	O-GlcNAc-modified	708:724	arg1	proteins					726:733	199 putative O-GlcNAc-modified proteins	695:733	199 putative O-GlcNAc-modified proteins from HeLa cells	695:749	Our study led to the identification of 199 putative O-GlcNAc-modified proteins from HeLa cells, among which 23 were confirmed using reciprocal immunoprecipitation.
16408927	6	17	with	proteins	857:864	arg1	functions					879:887	diverse functions	871:887	diverse functions	871:887	Functional classification shows that proteins with diverse functions are modified by O-GlcNAc, implying that O-GlcNAc might be involved in the regulation of multiple cellular pathways.
16408927	1	18	link	O-linked	57:64	arg1	O-GlcNAc					87:94	O-GlcNAc	87:94	O-GlcNAc	87:94	The O-linked N-acetylglucosamine (O-GlcNAc) modification of serine/threonine residues is an abundant posttranslational modification present in cytosolic and nuclear proteins.
16408927	1	18	link	O-linked	57:64	arg1	N-acetylglucosamine					66:84	O-linked N-acetylglucosamine	57:84	The O-linked N-acetylglucosamine (O-GlcNAc) modification of serine/threonine residues	53:137	The O-linked N-acetylglucosamine (O-GlcNAc) modification of serine/threonine residues is an abundant posttranslational modification present in cytosolic and nuclear proteins.
16408927	5	19	theme	proteins	726:733	arg1	identification					677:690	the identification	673:690	the identification of 199 putative O-GlcNAc-modified proteins from HeLa cells	673:749	Our study led to the identification of 199 putative O-GlcNAc-modified proteins from HeLa cells, among which 23 were confirmed using reciprocal immunoprecipitation.
16408927	4	20	theme	TAS	445:447	arg1	method					449:454	The TAS method	441:454	The TAS method	441:454	The TAS method utilizes an O-GlcNAc azide analogue for metabolic labeling of O-GlcNAc-modified proteins, which can be chemoselectively conjugated for detection and enrichment of the proteins for proteomics studies.
16408927	0	21	theme	O-GlcNAc-modified	25:41	arg1	proteins					43:50	O-GlcNAc-modified proteins	25:50	O-GlcNAc-modified proteins	25:50	Global identification of O-GlcNAc-modified proteins.
16408927	4	22	theme	proteins	623:630	arg1	enrichment					605:614	enrichment	605:614	enrichment	605:614	The TAS method utilizes an O-GlcNAc azide analogue for metabolic labeling of O-GlcNAc-modified proteins, which can be chemoselectively conjugated for detection and enrichment of the proteins for proteomics studies.
16408927	4	22	theme	proteins	623:630	arg1	detection					591:599	detection	591:599	detection	591:599	The TAS method utilizes an O-GlcNAc azide analogue for metabolic labeling of O-GlcNAc-modified proteins, which can be chemoselectively conjugated for detection and enrichment of the proteins for proteomics studies.
16408927	1	23	theme	serine/threonine	113:128	arg1	residues					130:137	serine/threonine residues	113:137	serine/threonine residues	113:137	The O-linked N-acetylglucosamine (O-GlcNAc) modification of serine/threonine residues is an abundant posttranslational modification present in cytosolic and nuclear proteins.
16408927	1	24	theme	residues	130:137	arg1	modification					172:183	an abundant posttranslational modification	142:183	an abundant posttranslational modification present in cytosolic and nuclear proteins	142:225	The O-linked N-acetylglucosamine (O-GlcNAc) modification of serine/threonine residues is an abundant posttranslational modification present in cytosolic and nuclear proteins.
16408927	1	24	theme	residues	130:137	arg1	modification					97:108	The O-linked N-acetylglucosamine (O-GlcNAc) modification	53:108	The O-linked N-acetylglucosamine (O-GlcNAc) modification of serine/threonine residues	53:137	The O-linked N-acetylglucosamine (O-GlcNAc) modification of serine/threonine residues is an abundant posttranslational modification present in cytosolic and nuclear proteins.
16408927	4	25	theme	proteomics	636:645	arg1	studies					647:653	proteomics studies	636:653	proteomics studies	636:653	The TAS method utilizes an O-GlcNAc azide analogue for metabolic labeling of O-GlcNAc-modified proteins, which can be chemoselectively conjugated for detection and enrichment of the proteins for proteomics studies.
16408927	5	26	theme	reciprocal	788:797	arg1	immunoprecipitation					799:817	reciprocal immunoprecipitation	788:817	reciprocal immunoprecipitation	788:817	Our study led to the identification of 199 putative O-GlcNAc-modified proteins from HeLa cells, among which 23 were confirmed using reciprocal immunoprecipitation.
16408927	0	27	theme	proteins	43:50	arg1	identification					7:20	Global identification	0:20	Global identification of O-GlcNAc-modified proteins.	0:51	Global identification of O-GlcNAc-modified proteins.
16408927	5	28	from	cells	745:749	arg1	proteins					726:733	199 putative O-GlcNAc-modified proteins	695:733	199 putative O-GlcNAc-modified proteins from HeLa cells	695:749	Our study led to the identification of 199 putative O-GlcNAc-modified proteins from HeLa cells, among which 23 were confirmed using reciprocal immunoprecipitation.
16408927	5	28	from	cells	745:749	arg1	identification					677:690	the identification	673:690	the identification of 199 putative O-GlcNAc-modified proteins from HeLa cells	673:749	Our study led to the identification of 199 putative O-GlcNAc-modified proteins from HeLa cells, among which 23 were confirmed using reciprocal immunoprecipitation.
16408927	4	29	theme	proteins	536:543	arg1	labeling					506:513	metabolic labeling	496:513	metabolic labeling of O-GlcNAc-modified proteins	496:543	The TAS method utilizes an O-GlcNAc azide analogue for metabolic labeling of O-GlcNAc-modified proteins, which can be chemoselectively conjugated for detection and enrichment of the proteins for proteomics studies.
16408927	2	30	theme	modification	270:281	arg1	functions					232:240	functions	232:240	functions	232:240	The functions and subproteome of O-GlcNAc modification remain largely undefined.
16408927	2	30	theme	modification	270:281	arg1	subproteome					246:256	subproteome	246:256	subproteome	246:256	The functions and subproteome of O-GlcNAc modification remain largely undefined.
16408927	6	31	theme	diverse	871:877	arg1	functions					879:887	diverse functions	871:887	diverse functions	871:887	Functional classification shows that proteins with diverse functions are modified by O-GlcNAc, implying that O-GlcNAc might be involved in the regulation of multiple cellular pathways.
16408927	3	32	theme	tagging-via-substrate	347:367	arg1	approach					375:382	the tagging-via-substrate (TAS) approach	343:382	the tagging-via-substrate (TAS) approach for global identification of O-GlcNAc-modified proteins	343:438	Here we report the application of the tagging-via-substrate (TAS) approach for global identification of O-GlcNAc-modified proteins.
16408927	4	33	theme	O-GlcNAc-modified	518:534	arg1	proteins					536:543	O-GlcNAc-modified proteins	518:543	O-GlcNAc-modified proteins	518:543	The TAS method utilizes an O-GlcNAc azide analogue for metabolic labeling of O-GlcNAc-modified proteins, which can be chemoselectively conjugated for detection and enrichment of the proteins for proteomics studies.
16408927	2	34	theme	O-GlcNAc	261:268	arg1	modification					270:281	O-GlcNAc modification	261:281	O-GlcNAc modification	261:281	The functions and subproteome of O-GlcNAc modification remain largely undefined.
16408927	1	35	mod	modification	97:108	arg3	N-acetylglucosamine					66:84	O-linked N-acetylglucosamine	57:84	The O-linked N-acetylglucosamine (O-GlcNAc) modification of serine/threonine residues	53:137	The O-linked N-acetylglucosamine (O-GlcNAc) modification of serine/threonine residues is an abundant posttranslational modification present in cytosolic and nuclear proteins.
16408927	1	35	mod	modification	97:108	arg3	O-GlcNAc					87:94	O-GlcNAc	87:94	O-GlcNAc	87:94	The O-linked N-acetylglucosamine (O-GlcNAc) modification of serine/threonine residues is an abundant posttranslational modification present in cytosolic and nuclear proteins.
16408927	1	35	mod	modification	97:108	arg1	residues					130:137	serine/threonine residues	113:137	serine/threonine residues	113:137	The O-linked N-acetylglucosamine (O-GlcNAc) modification of serine/threonine residues is an abundant posttranslational modification present in cytosolic and nuclear proteins.
16408927	4	36	theme	azide	477:481	arg1	analogue					483:490	an O-GlcNAc azide analogue	465:490	an O-GlcNAc azide analogue	465:490	The TAS method utilizes an O-GlcNAc azide analogue for metabolic labeling of O-GlcNAc-modified proteins, which can be chemoselectively conjugated for detection and enrichment of the proteins for proteomics studies.
16408927	1	37	theme	abundant	145:152	arg1	modification					97:108	The O-linked N-acetylglucosamine (O-GlcNAc) modification	53:108	The O-linked N-acetylglucosamine (O-GlcNAc) modification of serine/threonine residues	53:137	The O-linked N-acetylglucosamine (O-GlcNAc) modification of serine/threonine residues is an abundant posttranslational modification present in cytosolic and nuclear proteins.
16408927	1	37	theme	abundant	145:152	arg1	modification					172:183	an abundant posttranslational modification	142:183	an abundant posttranslational modification present in cytosolic and nuclear proteins	142:225	The O-linked N-acetylglucosamine (O-GlcNAc) modification of serine/threonine residues is an abundant posttranslational modification present in cytosolic and nuclear proteins.
16408927	2	38	dep	functions	232:240	arg1	The					228:230	The	228:230	The	228:230	The functions and subproteome of O-GlcNAc modification remain largely undefined.
16408927	4	39	theme	metabolic	496:504	arg1	labeling					506:513	metabolic labeling	496:513	metabolic labeling of O-GlcNAc-modified proteins	496:543	The TAS method utilizes an O-GlcNAc azide analogue for metabolic labeling of O-GlcNAc-modified proteins, which can be chemoselectively conjugated for detection and enrichment of the proteins for proteomics studies.
16408927	1	40	from	proteins	218:225	arg1	present					185:191	present	185:191	present	185:191	The O-linked N-acetylglucosamine (O-GlcNAc) modification of serine/threonine residues is an abundant posttranslational modification present in cytosolic and nuclear proteins.
16408927	1	41	theme	posttranslational	154:170	arg1	modification					97:108	The O-linked N-acetylglucosamine (O-GlcNAc) modification	53:108	The O-linked N-acetylglucosamine (O-GlcNAc) modification of serine/threonine residues	53:137	The O-linked N-acetylglucosamine (O-GlcNAc) modification of serine/threonine residues is an abundant posttranslational modification present in cytosolic and nuclear proteins.
16408927	1	41	theme	posttranslational	154:170	arg1	modification					172:183	an abundant posttranslational modification	142:183	an abundant posttranslational modification present in cytosolic and nuclear proteins	142:225	The O-linked N-acetylglucosamine (O-GlcNAc) modification of serine/threonine residues is an abundant posttranslational modification present in cytosolic and nuclear proteins.
16408927	3	42	theme	approach	375:382	arg1	application					328:338	the application	324:338	the application of the tagging-via-substrate (TAS) approach for global identification of O-GlcNAc-modified proteins	324:438	Here we report the application of the tagging-via-substrate (TAS) approach for global identification of O-GlcNAc-modified proteins.
16408927	6	43	mod	modified	893:900	arg1	proteins					857:864	proteins	857:864	proteins with diverse functions	857:887	Functional classification shows that proteins with diverse functions are modified by O-GlcNAc, implying that O-GlcNAc might be involved in the regulation of multiple cellular pathways.
16408927	6	43	mod	modified	893:900	arg3	O-GlcNAc					905:912	O-GlcNAc	905:912	O-GlcNAc	905:912	Functional classification shows that proteins with diverse functions are modified by O-GlcNAc, implying that O-GlcNAc might be involved in the regulation of multiple cellular pathways.
16408927	5	44	from	identification	677:690	arg1	cells					745:749	HeLa cells	740:749	HeLa cells	740:749	Our study led to the identification of 199 putative O-GlcNAc-modified proteins from HeLa cells, among which 23 were confirmed using reciprocal immunoprecipitation.
16408927	1	45	theme	O-linked	57:64	arg1	O-GlcNAc					87:94	O-GlcNAc	87:94	O-GlcNAc	87:94	The O-linked N-acetylglucosamine (O-GlcNAc) modification of serine/threonine residues is an abundant posttranslational modification present in cytosolic and nuclear proteins.
16408927	1	45	theme	O-linked	57:64	arg1	N-acetylglucosamine					66:84	O-linked N-acetylglucosamine	57:84	The O-linked N-acetylglucosamine (O-GlcNAc) modification of serine/threonine residues	53:137	The O-linked N-acetylglucosamine (O-GlcNAc) modification of serine/threonine residues is an abundant posttranslational modification present in cytosolic and nuclear proteins.
16408927	6	46	theme	Functional	820:829	arg1	classification					831:844	Functional classification	820:844	Functional classification	820:844	Functional classification shows that proteins with diverse functions are modified by O-GlcNAc, implying that O-GlcNAc might be involved in the regulation of multiple cellular pathways.
16408927	1	47	theme	present	185:191	arg1	modification					97:108	The O-linked N-acetylglucosamine (O-GlcNAc) modification	53:108	The O-linked N-acetylglucosamine (O-GlcNAc) modification of serine/threonine residues	53:137	The O-linked N-acetylglucosamine (O-GlcNAc) modification of serine/threonine residues is an abundant posttranslational modification present in cytosolic and nuclear proteins.
16408927	1	47	theme	present	185:191	arg1	modification					172:183	an abundant posttranslational modification	142:183	an abundant posttranslational modification present in cytosolic and nuclear proteins	142:225	The O-linked N-acetylglucosamine (O-GlcNAc) modification of serine/threonine residues is an abundant posttranslational modification present in cytosolic and nuclear proteins.
34229054	0	0	theme	modified	78:85	arg1	proteins					87:94	O-GlcNAc modified proteins	69:94	O-GlcNAc modified proteins	69:94	Synthesis of Na2S2O4 mediated cleavable affinity tag for labeling of O-GlcNAc modified proteins via azide-alkyne cycloaddition.
34229054	3	1	theme	high	545:548	arg1	efficiency					550:559	high efficiency	545:559	high efficiency	545:559	In addition, the azobenzene tag applied in the Ac4GlcNAz-labled proteins demonstrated high efficiency and selectivity in comparison with Biotin-PEG4-Alkyne, which provides a useful platform for enrichment of any desired bioorthogonal proteomics.
34229054	0	2	theme	proteins	87:94	arg1	labeling					57:64	labeling	57:64	labeling of O-GlcNAc modified proteins	57:94	Synthesis of Na2S2O4 mediated cleavable affinity tag for labeling of O-GlcNAc modified proteins via azide-alkyne cycloaddition.
34229054	1	3	theme	sodium	287:292	arg1	dithionite					294:303	sodium dithionite	287:303	sodium dithionite	287:303	A facile and convergent procedure for the synthesis of azobenzene-based probe was reported, which could selectively release interested proteins conducted with sodium dithionite.
34229054	0	4	theme	azide-alkyne	100:111	arg1	cycloaddition					113:125	azide-alkyne cycloaddition	100:125	azide-alkyne cycloaddition	100:125	Synthesis of Na2S2O4 mediated cleavable affinity tag for labeling of O-GlcNAc modified proteins via azide-alkyne cycloaddition.
34229054	2	5	from	features	381:388	arg1	necessary					433:441	necessary	433:441	necessary	433:441	Besides, the cleavage efficiency is closely associated with the structural features, in which an ortho-hydroxyl substituent is necessary for reactivity.
34229054	2	5	from	features	381:388	arg1	substituent					418:428	an ortho-hydroxyl substituent	400:428	an ortho-hydroxyl substituent	400:428	Besides, the cleavage efficiency is closely associated with the structural features, in which an ortho-hydroxyl substituent is necessary for reactivity.
34229054	2	6	theme	ortho-hydroxyl	403:416	arg1	necessary					433:441	necessary	433:441	necessary	433:441	Besides, the cleavage efficiency is closely associated with the structural features, in which an ortho-hydroxyl substituent is necessary for reactivity.
34229054	2	6	theme	ortho-hydroxyl	403:416	arg1	substituent					418:428	an ortho-hydroxyl substituent	400:428	an ortho-hydroxyl substituent	400:428	Besides, the cleavage efficiency is closely associated with the structural features, in which an ortho-hydroxyl substituent is necessary for reactivity.
34229054	1	7	theme	azobenzene-based	183:198	arg1	probe					200:204	azobenzene-based probe	183:204	azobenzene-based probe	183:204	A facile and convergent procedure for the synthesis of azobenzene-based probe was reported, which could selectively release interested proteins conducted with sodium dithionite.
34229054	1	8	theme	probe	200:204	arg1	synthesis					170:178	the synthesis	166:178	the synthesis of azobenzene-based probe	166:204	A facile and convergent procedure for the synthesis of azobenzene-based probe was reported, which could selectively release interested proteins conducted with sodium dithionite.
34229054	2	9	theme	cleavage	319:326	arg1	efficiency					328:337	the cleavage efficiency	315:337	the cleavage efficiency	315:337	Besides, the cleavage efficiency is closely associated with the structural features, in which an ortho-hydroxyl substituent is necessary for reactivity.
34229054	0	10	theme	Na2S2O4	13:19	arg1	Synthesis					0:8	Synthesis	0:8	Synthesis of Na2S2O4	0:19	Synthesis of Na2S2O4 mediated cleavable affinity tag for labeling of O-GlcNAc modified proteins via azide-alkyne cycloaddition.
34229054	2	11	theme	structural	370:379	arg1	features					381:388	the structural features	366:388	the structural features	366:388	Besides, the cleavage efficiency is closely associated with the structural features, in which an ortho-hydroxyl substituent is necessary for reactivity.
34229054	0	12	theme	affinity	40:47	arg1	tag					49:51	cleavable affinity tag	30:51	cleavable affinity tag for labeling of O-GlcNAc modified proteins	30:94	Synthesis of Na2S2O4 mediated cleavable affinity tag for labeling of O-GlcNAc modified proteins via azide-alkyne cycloaddition.
34229054	0	13	theme	cleavable	30:38	arg1	tag					49:51	cleavable affinity tag	30:51	cleavable affinity tag for labeling of O-GlcNAc modified proteins	30:94	Synthesis of Na2S2O4 mediated cleavable affinity tag for labeling of O-GlcNAc modified proteins via azide-alkyne cycloaddition.
34229054	3	14	theme	bioorthogonal	679:691	arg1	proteomics					693:702	any desired bioorthogonal proteomics	667:702	any desired bioorthogonal proteomics	667:702	In addition, the azobenzene tag applied in the Ac4GlcNAz-labled proteins demonstrated high efficiency and selectivity in comparison with Biotin-PEG4-Alkyne, which provides a useful platform for enrichment of any desired bioorthogonal proteomics.
34229054	3	15	theme	azobenzene	476:485	arg1	tag					487:489	the azobenzene tag	472:489	the azobenzene tag applied in the Ac4GlcNAz-labled proteins	472:530	In addition, the azobenzene tag applied in the Ac4GlcNAz-labled proteins demonstrated high efficiency and selectivity in comparison with Biotin-PEG4-Alkyne, which provides a useful platform for enrichment of any desired bioorthogonal proteomics.
34229054	3	16	with	comparison	580:589	arg1	Biotin-PEG4-Alkyne					596:613	Biotin-PEG4-Alkyne	596:613	Biotin-PEG4-Alkyne	596:613	In addition, the azobenzene tag applied in the Ac4GlcNAz-labled proteins demonstrated high efficiency and selectivity in comparison with Biotin-PEG4-Alkyne, which provides a useful platform for enrichment of any desired bioorthogonal proteomics.
34229054	3	17	theme	proteomics	693:702	arg1	enrichment					653:662	enrichment	653:662	enrichment of any desired bioorthogonal proteomics	653:702	In addition, the azobenzene tag applied in the Ac4GlcNAz-labled proteins demonstrated high efficiency and selectivity in comparison with Biotin-PEG4-Alkyne, which provides a useful platform for enrichment of any desired bioorthogonal proteomics.
34229054	3	18	theme	Ac4GlcNAz-labled	506:521	arg1	proteins					523:530	the Ac4GlcNAz-labled proteins	502:530	the Ac4GlcNAz-labled proteins	502:530	In addition, the azobenzene tag applied in the Ac4GlcNAz-labled proteins demonstrated high efficiency and selectivity in comparison with Biotin-PEG4-Alkyne, which provides a useful platform for enrichment of any desired bioorthogonal proteomics.
34229054	3	19	theme	useful	633:638	arg1	platform					640:647	a useful platform	631:647	a useful platform for enrichment of any desired bioorthogonal proteomics	631:702	In addition, the azobenzene tag applied in the Ac4GlcNAz-labled proteins demonstrated high efficiency and selectivity in comparison with Biotin-PEG4-Alkyne, which provides a useful platform for enrichment of any desired bioorthogonal proteomics.
34229054	1	20	theme	facile	130:135	arg1	procedure					152:160	A facile and convergent procedure	128:160	A facile and convergent procedure for the synthesis of azobenzene-based probe	128:204	A facile and convergent procedure for the synthesis of azobenzene-based probe was reported, which could selectively release interested proteins conducted with sodium dithionite.
34229054	3	21	theme	desired	671:677	arg1	proteomics					693:702	any desired bioorthogonal proteomics	667:702	any desired bioorthogonal proteomics	667:702	In addition, the azobenzene tag applied in the Ac4GlcNAz-labled proteins demonstrated high efficiency and selectivity in comparison with Biotin-PEG4-Alkyne, which provides a useful platform for enrichment of any desired bioorthogonal proteomics.
34229054	2	22	from	necessary	433:441	arg1	features					381:388	the structural features	366:388	the structural features	366:388	Besides, the cleavage efficiency is closely associated with the structural features, in which an ortho-hydroxyl substituent is necessary for reactivity.
34229054	1	23	theme	convergent	141:150	arg1	procedure					152:160	A facile and convergent procedure	128:160	A facile and convergent procedure for the synthesis of azobenzene-based probe	128:204	A facile and convergent procedure for the synthesis of azobenzene-based probe was reported, which could selectively release interested proteins conducted with sodium dithionite.
34229054	1	24	theme	interested	252:261	arg1	proteins					263:270	interested proteins	252:270	interested proteins conducted with sodium dithionite	252:303	A facile and convergent procedure for the synthesis of azobenzene-based probe was reported, which could selectively release interested proteins conducted with sodium dithionite.
24126823	2	0	from	sensor	406:411	arg1	cells					437:441	highly proliferating cells	416:441	highly proliferating cells	416:441	This modification is thought to be a nutrient sensor in highly proliferating cells via the hexosamine biosynthesis pathway, a minor branch of glycolysis.
24126823	5	1	theme	2-dimensional	908:920	arg1	immunoblotting					931:944	2-dimensional O-GlcNAc immunoblotting and LC-MS/MS analysis	908:966	immunoblotting	931:944	Using 2-dimensional O-GlcNAc immunoblotting and LC-MS/MS analysis, 16 proteins were successfully identified and 8 proteins showed an increase in O-GlcNAcylation, including cytokeratin 18, heterogeneous nuclear ribonucleoproteins A2/B1 (hnRNP A2/B1), hnRNP H, annexin A2, annexin A7, laminin-binding protein, α-tubulin and protein DJ-1.
24126823	6	2	theme	cancer	1346:1351	arg1	samples					1353:1359	all cancer samples	1342:1359	all cancer samples	1342:1359	Among these identified proteins, annexin A2 was further confirmed to show overexpression of O-GlcNAc in all cancer samples.
24126823	1	3	dep	addition	274:281	arg1	the					270:272	the	270:272	the	270:272	O-GlcNAcylation is a post-translational modification of serine and threonine residues which is dynamically regulated by 2 enzymes; O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) that catalyze the addition and removal of a single N-acetylglucosamine (GlcNAc) molecule, respectively.
24126823	5	4	theme	O-GlcNAc	922:929	arg1	immunoblotting					931:944	2-dimensional O-GlcNAc immunoblotting and LC-MS/MS analysis	908:966	immunoblotting	931:944	Using 2-dimensional O-GlcNAc immunoblotting and LC-MS/MS analysis, 16 proteins were successfully identified and 8 proteins showed an increase in O-GlcNAcylation, including cytokeratin 18, heterogeneous nuclear ribonucleoproteins A2/B1 (hnRNP A2/B1), hnRNP H, annexin A2, annexin A7, laminin-binding protein, α-tubulin and protein DJ-1.
24126823	5	5	theme	annexin	1161:1167	arg1	A2					1169:1170	annexin A2	1161:1170	annexin A2	1161:1170	Using 2-dimensional O-GlcNAc immunoblotting and LC-MS/MS analysis, 16 proteins were successfully identified and 8 proteins showed an increase in O-GlcNAcylation, including cytokeratin 18, heterogeneous nuclear ribonucleoproteins A2/B1 (hnRNP A2/B1), hnRNP H, annexin A2, annexin A7, laminin-binding protein, α-tubulin and protein DJ-1.
24126823	4	6	theme	levels	894:899	arg1	expression					876:885	an increased expression	863:885	an increased expression of OGT levels	863:899	In the present study, we demonstrated that O-GlcNAcylation is increased in primary colorectal cancer tissues, and that this augmentation is associated with an increased expression of OGT levels.
24126823	5	7	theme	annexin	1173:1179	arg1	A7					1181:1182	annexin A7	1173:1182	annexin A7	1173:1182	Using 2-dimensional O-GlcNAc immunoblotting and LC-MS/MS analysis, 16 proteins were successfully identified and 8 proteins showed an increase in O-GlcNAcylation, including cytokeratin 18, heterogeneous nuclear ribonucleoproteins A2/B1 (hnRNP A2/B1), hnRNP H, annexin A2, annexin A7, laminin-binding protein, α-tubulin and protein DJ-1.
24126823	5	8	theme	hnRNP	1138:1142	arg1	A2/B1					1131:1135	heterogeneous nuclear ribonucleoproteins A2/B1	1090:1135	heterogeneous nuclear ribonucleoproteins A2/B1 (hnRNP A2/B1)	1090:1149	Using 2-dimensional O-GlcNAc immunoblotting and LC-MS/MS analysis, 16 proteins were successfully identified and 8 proteins showed an increase in O-GlcNAcylation, including cytokeratin 18, heterogeneous nuclear ribonucleoproteins A2/B1 (hnRNP A2/B1), hnRNP H, annexin A2, annexin A7, laminin-binding protein, α-tubulin and protein DJ-1.
24126823	5	8	theme	hnRNP	1138:1142	arg1	A2/B1					1144:1148	hnRNP A2/B1	1138:1148	hnRNP A2/B1	1138:1148	Using 2-dimensional O-GlcNAc immunoblotting and LC-MS/MS analysis, 16 proteins were successfully identified and 8 proteins showed an increase in O-GlcNAcylation, including cytokeratin 18, heterogeneous nuclear ribonucleoproteins A2/B1 (hnRNP A2/B1), hnRNP H, annexin A2, annexin A7, laminin-binding protein, α-tubulin and protein DJ-1.
24126823	4	9	theme	OGT	890:892	arg1	levels					894:899	OGT levels	890:899	OGT levels	890:899	In the present study, we demonstrated that O-GlcNAcylation is increased in primary colorectal cancer tissues, and that this augmentation is associated with an increased expression of OGT levels.
24126823	7	10	theme	colorectal	1456:1465	arg1	cancer					1467:1472	colorectal cancer	1456:1472	colorectal cancer	1456:1472	The results, therefore, indicate that aberrant O-GlcNAcylation of proteins is associated with colorectal cancer and that identification of O-GlcNAc-modified proteins may provide novel biomarkers of cancer.
24126823	2	11	theme	glycolysis	502:511	arg1	branch					492:497	a minor branch	484:497	a minor branch of glycolysis	484:511	This modification is thought to be a nutrient sensor in highly proliferating cells via the hexosamine biosynthesis pathway, a minor branch of glycolysis.
24126823	2	11	theme	glycolysis	502:511	arg1	sensor					406:411	a nutrient sensor	395:411	a nutrient sensor in highly proliferating cells via the hexosamine biosynthesis pathway	395:481	This modification is thought to be a nutrient sensor in highly proliferating cells via the hexosamine biosynthesis pathway, a minor branch of glycolysis.
24126823	3	12	theme	emerging	523:530	arg1	evidence					532:539	emerging evidence	523:539	emerging evidence	523:539	Although emerging evidence suggests that O-GlcNAc modification is associated with many types of cancer, identification of O-GlcNAc-modified proteins and their role in cancer remain unexplored.
24126823	5	13	from	increase	1035:1042	arg1	O-GlcNAcylation					1047:1061	O-GlcNAcylation	1047:1061	O-GlcNAcylation	1047:1061	Using 2-dimensional O-GlcNAc immunoblotting and LC-MS/MS analysis, 16 proteins were successfully identified and 8 proteins showed an increase in O-GlcNAcylation, including cytokeratin 18, heterogeneous nuclear ribonucleoproteins A2/B1 (hnRNP A2/B1), hnRNP H, annexin A2, annexin A7, laminin-binding protein, α-tubulin and protein DJ-1.
24126823	6	14	theme	annexin	1271:1277	arg1	A2					1279:1280	annexin A2	1271:1280	annexin A2	1271:1280	Among these identified proteins, annexin A2 was further confirmed to show overexpression of O-GlcNAc in all cancer samples.
24126823	4	15	theme	primary	782:788	arg1	tissues					808:814	primary colorectal cancer tissues	782:814	primary colorectal cancer tissues	782:814	In the present study, we demonstrated that O-GlcNAcylation is increased in primary colorectal cancer tissues, and that this augmentation is associated with an increased expression of OGT levels.
24126823	3	16	from	identification	618:631	arg1	cancer					681:686	cancer	681:686	cancer	681:686	Although emerging evidence suggests that O-GlcNAc modification is associated with many types of cancer, identification of O-GlcNAc-modified proteins and their role in cancer remain unexplored.
24126823	4	17	gly	O-GlcNAcylation	750:764	arg1	tissues					808:814	primary colorectal cancer tissues	782:814	primary colorectal cancer tissues	782:814	In the present study, we demonstrated that O-GlcNAcylation is increased in primary colorectal cancer tissues, and that this augmentation is associated with an increased expression of OGT levels.
24126823	0	18	theme	O-GlcNAc-modified	9:25	arg1	proteins					27:34	Aberrant O-GlcNAc-modified proteins	0:34	Aberrant O-GlcNAc-modified proteins	0:34	Aberrant O-GlcNAc-modified proteins expressed in primary colorectal cancer.
24126823	4	19	theme	increased	866:874	arg1	expression					876:885	an increased expression	863:885	an increased expression of OGT levels	863:899	In the present study, we demonstrated that O-GlcNAcylation is increased in primary colorectal cancer tissues, and that this augmentation is associated with an increased expression of OGT levels.
24126823	1	20	theme	post-translational	97:114	arg1	modification					116:127	a post-translational modification	95:127	a post-translational modification of serine and threonine residues which is dynamically regulated by 2 enzymes; O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) that catalyze the addition and removal of a single N-acetylglucosamine (GlcNAc) molecule, respectively	95:357	O-GlcNAcylation is a post-translational modification of serine and threonine residues which is dynamically regulated by 2 enzymes; O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) that catalyze the addition and removal of a single N-acetylglucosamine (GlcNAc) molecule, respectively.
24126823	1	20	theme	post-translational	97:114	arg1	O-GlcNAcylation					76:90	O-GlcNAcylation	76:90	O-GlcNAcylation	76:90	O-GlcNAcylation is a post-translational modification of serine and threonine residues which is dynamically regulated by 2 enzymes; O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) that catalyze the addition and removal of a single N-acetylglucosamine (GlcNAc) molecule, respectively.
24126823	0	21	theme	Aberrant	0:7	arg1	proteins					27:34	Aberrant O-GlcNAc-modified proteins	0:34	Aberrant O-GlcNAc-modified proteins	0:34	Aberrant O-GlcNAc-modified proteins expressed in primary colorectal cancer.
24126823	7	22	theme	novel	1540:1544	arg1	biomarkers					1546:1555	novel biomarkers	1540:1555	novel biomarkers of cancer	1540:1565	The results, therefore, indicate that aberrant O-GlcNAcylation of proteins is associated with colorectal cancer and that identification of O-GlcNAc-modified proteins may provide novel biomarkers of cancer.
24126823	7	23	theme	proteins	1428:1435	arg1	O-GlcNAcylation					1409:1423	aberrant O-GlcNAcylation	1400:1423	aberrant O-GlcNAcylation of proteins	1400:1435	The results, therefore, indicate that aberrant O-GlcNAcylation of proteins is associated with colorectal cancer and that identification of O-GlcNAc-modified proteins may provide novel biomarkers of cancer.
24126823	1	24	theme	O-GlcNAc	207:214	arg1	OGA					251:253	OGA	251:253	OGA	251:253	O-GlcNAcylation is a post-translational modification of serine and threonine residues which is dynamically regulated by 2 enzymes; O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) that catalyze the addition and removal of a single N-acetylglucosamine (GlcNAc) molecule, respectively.
24126823	1	24	theme	O-GlcNAc	207:214	arg1	OGT					229:231	OGT	229:231	OGT	229:231	O-GlcNAcylation is a post-translational modification of serine and threonine residues which is dynamically regulated by 2 enzymes; O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) that catalyze the addition and removal of a single N-acetylglucosamine (GlcNAc) molecule, respectively.
24126823	1	24	theme	O-GlcNAc	207:214	arg1	enzymes					198:204	2 enzymes	196:204	2 enzymes; O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) that catalyze the addition and removal of a single N-acetylglucosamine (GlcNAc) molecule, respectively	196:357	O-GlcNAcylation is a post-translational modification of serine and threonine residues which is dynamically regulated by 2 enzymes; O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) that catalyze the addition and removal of a single N-acetylglucosamine (GlcNAc) molecule, respectively.
24126823	1	24	theme	O-GlcNAc	207:214	arg1	transferase					216:226	O-GlcNAc transferase	207:226	O-GlcNAc transferase (OGT)	207:232	O-GlcNAcylation is a post-translational modification of serine and threonine residues which is dynamically regulated by 2 enzymes; O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) that catalyze the addition and removal of a single N-acetylglucosamine (GlcNAc) molecule, respectively.
24126823	2	25	theme	proliferating	423:435	arg1	cells					437:441	highly proliferating cells	416:441	highly proliferating cells	416:441	This modification is thought to be a nutrient sensor in highly proliferating cells via the hexosamine biosynthesis pathway, a minor branch of glycolysis.
24126823	5	26	theme	laminin-binding	1185:1199	arg1	protein					1201:1207	laminin-binding protein	1185:1207	laminin-binding protein	1185:1207	Using 2-dimensional O-GlcNAc immunoblotting and LC-MS/MS analysis, 16 proteins were successfully identified and 8 proteins showed an increase in O-GlcNAcylation, including cytokeratin 18, heterogeneous nuclear ribonucleoproteins A2/B1 (hnRNP A2/B1), hnRNP H, annexin A2, annexin A7, laminin-binding protein, α-tubulin and protein DJ-1.
24126823	3	27	theme	many	596:599	arg1	types					601:605	many types	596:605	many types of cancer	596:615	Although emerging evidence suggests that O-GlcNAc modification is associated with many types of cancer, identification of O-GlcNAc-modified proteins and their role in cancer remain unexplored.
24126823	3	28	theme	O-GlcNAc	555:562	arg1	modification					564:575	O-GlcNAc modification	555:575	O-GlcNAc modification	555:575	Although emerging evidence suggests that O-GlcNAc modification is associated with many types of cancer, identification of O-GlcNAc-modified proteins and their role in cancer remain unexplored.
24126823	6	29	theme	identified	1250:1259	arg1	proteins					1261:1268	these identified proteins	1244:1268	these identified proteins	1244:1268	Among these identified proteins, annexin A2 was further confirmed to show overexpression of O-GlcNAc in all cancer samples.
24126823	4	30	theme	colorectal	790:799	arg1	tissues					808:814	primary colorectal cancer tissues	782:814	primary colorectal cancer tissues	782:814	In the present study, we demonstrated that O-GlcNAcylation is increased in primary colorectal cancer tissues, and that this augmentation is associated with an increased expression of OGT levels.
24126823	5	31	theme	nuclear	1104:1110	arg1	A2/B1					1131:1135	heterogeneous nuclear ribonucleoproteins A2/B1	1090:1135	heterogeneous nuclear ribonucleoproteins A2/B1 (hnRNP A2/B1)	1090:1149	Using 2-dimensional O-GlcNAc immunoblotting and LC-MS/MS analysis, 16 proteins were successfully identified and 8 proteins showed an increase in O-GlcNAcylation, including cytokeratin 18, heterogeneous nuclear ribonucleoproteins A2/B1 (hnRNP A2/B1), hnRNP H, annexin A2, annexin A7, laminin-binding protein, α-tubulin and protein DJ-1.
24126823	5	31	theme	nuclear	1104:1110	arg1	A2/B1					1144:1148	hnRNP A2/B1	1138:1148	hnRNP A2/B1	1138:1148	Using 2-dimensional O-GlcNAc immunoblotting and LC-MS/MS analysis, 16 proteins were successfully identified and 8 proteins showed an increase in O-GlcNAcylation, including cytokeratin 18, heterogeneous nuclear ribonucleoproteins A2/B1 (hnRNP A2/B1), hnRNP H, annexin A2, annexin A7, laminin-binding protein, α-tubulin and protein DJ-1.
24126823	1	32	theme	serine	132:137	arg1	modification					116:127	a post-translational modification	95:127	a post-translational modification of serine and threonine residues which is dynamically regulated by 2 enzymes; O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) that catalyze the addition and removal of a single N-acetylglucosamine (GlcNAc) molecule, respectively	95:357	O-GlcNAcylation is a post-translational modification of serine and threonine residues which is dynamically regulated by 2 enzymes; O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) that catalyze the addition and removal of a single N-acetylglucosamine (GlcNAc) molecule, respectively.
24126823	1	32	theme	serine	132:137	arg1	O-GlcNAcylation					76:90	O-GlcNAcylation	76:90	O-GlcNAcylation	76:90	O-GlcNAcylation is a post-translational modification of serine and threonine residues which is dynamically regulated by 2 enzymes; O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) that catalyze the addition and removal of a single N-acetylglucosamine (GlcNAc) molecule, respectively.
24126823	0	33	theme	primary	49:55	arg1	cancer					68:73	primary colorectal cancer	49:73	primary colorectal cancer	49:73	Aberrant O-GlcNAc-modified proteins expressed in primary colorectal cancer.
24126823	4	34	theme	present	714:720	arg1	study					722:726	the present study	710:726	the present study	710:726	In the present study, we demonstrated that O-GlcNAcylation is increased in primary colorectal cancer tissues, and that this augmentation is associated with an increased expression of OGT levels.
24126823	5	35	theme	ribonucleoproteins	1112:1129	arg1	A2/B1					1131:1135	heterogeneous nuclear ribonucleoproteins A2/B1	1090:1135	heterogeneous nuclear ribonucleoproteins A2/B1 (hnRNP A2/B1)	1090:1149	Using 2-dimensional O-GlcNAc immunoblotting and LC-MS/MS analysis, 16 proteins were successfully identified and 8 proteins showed an increase in O-GlcNAcylation, including cytokeratin 18, heterogeneous nuclear ribonucleoproteins A2/B1 (hnRNP A2/B1), hnRNP H, annexin A2, annexin A7, laminin-binding protein, α-tubulin and protein DJ-1.
24126823	5	35	theme	ribonucleoproteins	1112:1129	arg1	A2/B1					1144:1148	hnRNP A2/B1	1138:1148	hnRNP A2/B1	1138:1148	Using 2-dimensional O-GlcNAc immunoblotting and LC-MS/MS analysis, 16 proteins were successfully identified and 8 proteins showed an increase in O-GlcNAcylation, including cytokeratin 18, heterogeneous nuclear ribonucleoproteins A2/B1 (hnRNP A2/B1), hnRNP H, annexin A2, annexin A7, laminin-binding protein, α-tubulin and protein DJ-1.
24126823	1	36	theme	molecule	336:343	arg1	removal					287:293	removal	287:293	removal	287:293	O-GlcNAcylation is a post-translational modification of serine and threonine residues which is dynamically regulated by 2 enzymes; O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) that catalyze the addition and removal of a single N-acetylglucosamine (GlcNAc) molecule, respectively.
24126823	1	36	theme	molecule	336:343	arg1	addition					274:281	addition	274:281	addition	274:281	O-GlcNAcylation is a post-translational modification of serine and threonine residues which is dynamically regulated by 2 enzymes; O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) that catalyze the addition and removal of a single N-acetylglucosamine (GlcNAc) molecule, respectively.
24126823	2	37	theme	nutrient	397:404	arg1	branch					492:497	a minor branch	484:497	a minor branch of glycolysis	484:511	This modification is thought to be a nutrient sensor in highly proliferating cells via the hexosamine biosynthesis pathway, a minor branch of glycolysis.
24126823	2	37	theme	nutrient	397:404	arg1	sensor					406:411	a nutrient sensor	395:411	a nutrient sensor in highly proliferating cells via the hexosamine biosynthesis pathway	395:481	This modification is thought to be a nutrient sensor in highly proliferating cells via the hexosamine biosynthesis pathway, a minor branch of glycolysis.
24126823	2	37	theme	nutrient	397:404	arg1	modification					365:376	This modification	360:376	This modification	360:376	This modification is thought to be a nutrient sensor in highly proliferating cells via the hexosamine biosynthesis pathway, a minor branch of glycolysis.
24126823	2	38	theme	biosynthesis	462:473	arg1	pathway					475:481	the hexosamine biosynthesis pathway	447:481	the hexosamine biosynthesis pathway	447:481	This modification is thought to be a nutrient sensor in highly proliferating cells via the hexosamine biosynthesis pathway, a minor branch of glycolysis.
24126823	6	39	from	overexpression	1312:1325	arg1	samples					1353:1359	all cancer samples	1342:1359	all cancer samples	1342:1359	Among these identified proteins, annexin A2 was further confirmed to show overexpression of O-GlcNAc in all cancer samples.
24126823	3	40	theme	O-GlcNAc-modified	636:652	arg1	proteins					654:661	O-GlcNAc-modified proteins	636:661	O-GlcNAc-modified proteins	636:661	Although emerging evidence suggests that O-GlcNAc modification is associated with many types of cancer, identification of O-GlcNAc-modified proteins and their role in cancer remain unexplored.
24126823	2	41	theme	hexosamine	451:460	arg1	pathway					475:481	the hexosamine biosynthesis pathway	447:481	the hexosamine biosynthesis pathway	447:481	This modification is thought to be a nutrient sensor in highly proliferating cells via the hexosamine biosynthesis pathway, a minor branch of glycolysis.
24126823	1	42	theme	single	300:305	arg1	GlcNAc					328:333	GlcNAc	328:333	GlcNAc	328:333	O-GlcNAcylation is a post-translational modification of serine and threonine residues which is dynamically regulated by 2 enzymes; O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) that catalyze the addition and removal of a single N-acetylglucosamine (GlcNAc) molecule, respectively.
24126823	1	42	theme	single	300:305	arg1	N-acetylglucosamine					307:325	a single N-acetylglucosamine	298:325	a single N-acetylglucosamine (GlcNAc) molecule	298:343	O-GlcNAcylation is a post-translational modification of serine and threonine residues which is dynamically regulated by 2 enzymes; O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) that catalyze the addition and removal of a single N-acetylglucosamine (GlcNAc) molecule, respectively.
24126823	6	43	theme	O-GlcNAc	1330:1337	arg1	overexpression					1312:1325	overexpression	1312:1325	overexpression of O-GlcNAc in all cancer samples	1312:1359	Among these identified proteins, annexin A2 was further confirmed to show overexpression of O-GlcNAc in all cancer samples.
24126823	3	44	theme	proteins	654:661	arg1	identification					618:631	identification	618:631	identification of O-GlcNAc-modified proteins	618:661	Although emerging evidence suggests that O-GlcNAc modification is associated with many types of cancer, identification of O-GlcNAc-modified proteins and their role in cancer remain unexplored.
24126823	3	44	theme	proteins	654:661	arg1	role					673:676	their role	667:676	their role in cancer	667:686	Although emerging evidence suggests that O-GlcNAc modification is associated with many types of cancer, identification of O-GlcNAc-modified proteins and their role in cancer remain unexplored.
24126823	0	45	theme	colorectal	57:66	arg1	cancer					68:73	primary colorectal cancer	49:73	primary colorectal cancer	49:73	Aberrant O-GlcNAc-modified proteins expressed in primary colorectal cancer.
24126823	1	46	theme	N-acetylglucosamine	307:325	arg1	molecule					336:343	a single N-acetylglucosamine (GlcNAc) molecule	298:343	a single N-acetylglucosamine (GlcNAc) molecule	298:343	O-GlcNAcylation is a post-translational modification of serine and threonine residues which is dynamically regulated by 2 enzymes; O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) that catalyze the addition and removal of a single N-acetylglucosamine (GlcNAc) molecule, respectively.
24126823	7	47	theme	proteins	1519:1526	arg1	identification					1483:1496	identification	1483:1496	identification of O-GlcNAc-modified proteins	1483:1526	The results, therefore, indicate that aberrant O-GlcNAcylation of proteins is associated with colorectal cancer and that identification of O-GlcNAc-modified proteins may provide novel biomarkers of cancer.
24126823	1	48	dep	enzymes	198:204	arg1	OGA					251:253	OGA	251:253	OGA	251:253	O-GlcNAcylation is a post-translational modification of serine and threonine residues which is dynamically regulated by 2 enzymes; O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) that catalyze the addition and removal of a single N-acetylglucosamine (GlcNAc) molecule, respectively.
24126823	1	48	dep	enzymes	198:204	arg1	OGT					229:231	OGT	229:231	OGT	229:231	O-GlcNAcylation is a post-translational modification of serine and threonine residues which is dynamically regulated by 2 enzymes; O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) that catalyze the addition and removal of a single N-acetylglucosamine (GlcNAc) molecule, respectively.
24126823	1	48	dep	enzymes	198:204	arg1	O-GlcNAcase					238:248	O-GlcNAcase	238:248	O-GlcNAcase	238:248	O-GlcNAcylation is a post-translational modification of serine and threonine residues which is dynamically regulated by 2 enzymes; O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) that catalyze the addition and removal of a single N-acetylglucosamine (GlcNAc) molecule, respectively.
24126823	1	48	dep	enzymes	198:204	arg1	transferase					216:226	O-GlcNAc transferase	207:226	O-GlcNAc transferase (OGT)	207:232	O-GlcNAcylation is a post-translational modification of serine and threonine residues which is dynamically regulated by 2 enzymes; O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) that catalyze the addition and removal of a single N-acetylglucosamine (GlcNAc) molecule, respectively.
24126823	1	48	dep	enzymes	198:204	arg1	enzymes					198:204	2 enzymes	196:204	2 enzymes; O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) that catalyze the addition and removal of a single N-acetylglucosamine (GlcNAc) molecule, respectively	196:357	O-GlcNAcylation is a post-translational modification of serine and threonine residues which is dynamically regulated by 2 enzymes; O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) that catalyze the addition and removal of a single N-acetylglucosamine (GlcNAc) molecule, respectively.
24126823	1	49	theme	threonine	143:151	arg1	residues					153:160	threonine residues	143:160	threonine residues	143:160	O-GlcNAcylation is a post-translational modification of serine and threonine residues which is dynamically regulated by 2 enzymes; O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) that catalyze the addition and removal of a single N-acetylglucosamine (GlcNAc) molecule, respectively.
24126823	7	50	theme	O-GlcNAc-modified	1501:1517	arg1	proteins					1519:1526	O-GlcNAc-modified proteins	1501:1526	O-GlcNAc-modified proteins	1501:1526	The results, therefore, indicate that aberrant O-GlcNAcylation of proteins is associated with colorectal cancer and that identification of O-GlcNAc-modified proteins may provide novel biomarkers of cancer.
24126823	5	51	theme	protein	1224:1230	arg1	DJ-1					1232:1235	protein DJ-1	1224:1235	protein DJ-1	1224:1235	Using 2-dimensional O-GlcNAc immunoblotting and LC-MS/MS analysis, 16 proteins were successfully identified and 8 proteins showed an increase in O-GlcNAcylation, including cytokeratin 18, heterogeneous nuclear ribonucleoproteins A2/B1 (hnRNP A2/B1), hnRNP H, annexin A2, annexin A7, laminin-binding protein, α-tubulin and protein DJ-1.
24126823	1	52	theme	residues	153:160	arg1	modification					116:127	a post-translational modification	95:127	a post-translational modification of serine and threonine residues which is dynamically regulated by 2 enzymes; O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) that catalyze the addition and removal of a single N-acetylglucosamine (GlcNAc) molecule, respectively	95:357	O-GlcNAcylation is a post-translational modification of serine and threonine residues which is dynamically regulated by 2 enzymes; O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) that catalyze the addition and removal of a single N-acetylglucosamine (GlcNAc) molecule, respectively.
24126823	1	52	theme	residues	153:160	arg1	O-GlcNAcylation					76:90	O-GlcNAcylation	76:90	O-GlcNAcylation	76:90	O-GlcNAcylation is a post-translational modification of serine and threonine residues which is dynamically regulated by 2 enzymes; O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) that catalyze the addition and removal of a single N-acetylglucosamine (GlcNAc) molecule, respectively.
24126823	7	53	theme	aberrant	1400:1407	arg1	O-GlcNAcylation					1409:1423	aberrant O-GlcNAcylation	1400:1423	aberrant O-GlcNAcylation of proteins	1400:1435	The results, therefore, indicate that aberrant O-GlcNAcylation of proteins is associated with colorectal cancer and that identification of O-GlcNAc-modified proteins may provide novel biomarkers of cancer.
24126823	4	54	theme	cancer	801:806	arg1	tissues					808:814	primary colorectal cancer tissues	782:814	primary colorectal cancer tissues	782:814	In the present study, we demonstrated that O-GlcNAcylation is increased in primary colorectal cancer tissues, and that this augmentation is associated with an increased expression of OGT levels.
24126823	5	55	theme	LC-MS/MS	950:957	arg1	analysis					959:966	2-dimensional O-GlcNAc immunoblotting and LC-MS/MS analysis	908:966	analysis	959:966	Using 2-dimensional O-GlcNAc immunoblotting and LC-MS/MS analysis, 16 proteins were successfully identified and 8 proteins showed an increase in O-GlcNAcylation, including cytokeratin 18, heterogeneous nuclear ribonucleoproteins A2/B1 (hnRNP A2/B1), hnRNP H, annexin A2, annexin A7, laminin-binding protein, α-tubulin and protein DJ-1.
24126823	3	56	from	role	673:676	arg1	cancer					681:686	cancer	681:686	cancer	681:686	Although emerging evidence suggests that O-GlcNAc modification is associated with many types of cancer, identification of O-GlcNAc-modified proteins and their role in cancer remain unexplored.
24126823	5	57	theme	heterogeneous	1090:1102	arg1	A2/B1					1131:1135	heterogeneous nuclear ribonucleoproteins A2/B1	1090:1135	heterogeneous nuclear ribonucleoproteins A2/B1 (hnRNP A2/B1)	1090:1149	Using 2-dimensional O-GlcNAc immunoblotting and LC-MS/MS analysis, 16 proteins were successfully identified and 8 proteins showed an increase in O-GlcNAcylation, including cytokeratin 18, heterogeneous nuclear ribonucleoproteins A2/B1 (hnRNP A2/B1), hnRNP H, annexin A2, annexin A7, laminin-binding protein, α-tubulin and protein DJ-1.
24126823	5	57	theme	heterogeneous	1090:1102	arg1	A2/B1					1144:1148	hnRNP A2/B1	1138:1148	hnRNP A2/B1	1138:1148	Using 2-dimensional O-GlcNAc immunoblotting and LC-MS/MS analysis, 16 proteins were successfully identified and 8 proteins showed an increase in O-GlcNAcylation, including cytokeratin 18, heterogeneous nuclear ribonucleoproteins A2/B1 (hnRNP A2/B1), hnRNP H, annexin A2, annexin A7, laminin-binding protein, α-tubulin and protein DJ-1.
24126823	3	58	theme	cancer	610:615	arg1	types					601:605	many types	596:605	many types of cancer	596:615	Although emerging evidence suggests that O-GlcNAc modification is associated with many types of cancer, identification of O-GlcNAc-modified proteins and their role in cancer remain unexplored.
24126823	2	59	theme	minor	486:490	arg1	branch					492:497	a minor branch	484:497	a minor branch of glycolysis	484:511	This modification is thought to be a nutrient sensor in highly proliferating cells via the hexosamine biosynthesis pathway, a minor branch of glycolysis.
24126823	2	59	theme	minor	486:490	arg1	sensor					406:411	a nutrient sensor	395:411	a nutrient sensor in highly proliferating cells via the hexosamine biosynthesis pathway	395:481	This modification is thought to be a nutrient sensor in highly proliferating cells via the hexosamine biosynthesis pathway, a minor branch of glycolysis.
24126823	5	60	theme	hnRNP	1152:1156	arg1	H					1158:1158	hnRNP H	1152:1158	hnRNP H	1152:1158	Using 2-dimensional O-GlcNAc immunoblotting and LC-MS/MS analysis, 16 proteins were successfully identified and 8 proteins showed an increase in O-GlcNAcylation, including cytokeratin 18, heterogeneous nuclear ribonucleoproteins A2/B1 (hnRNP A2/B1), hnRNP H, annexin A2, annexin A7, laminin-binding protein, α-tubulin and protein DJ-1.
24126823	7	61	theme	cancer	1560:1565	arg1	biomarkers					1546:1555	novel biomarkers	1540:1555	novel biomarkers of cancer	1540:1565	The results, therefore, indicate that aberrant O-GlcNAcylation of proteins is associated with colorectal cancer and that identification of O-GlcNAc-modified proteins may provide novel biomarkers of cancer.
23576270	0	0	theme	breast	95:100	arg1	cancer					102:107	primary breast cancer	87:107	primary breast cancer	87:107	Proteomic analysis and abrogated expression of O-GlcNAcylated proteins associated with primary breast cancer.
23576270	5	1	theme	2D	784:785	arg1	immnoblotting					796:808	2D O-GlcNAc immnoblotting	784:808	2D O-GlcNAc immnoblotting	784:808	Using 2D O-GlcNAc immnoblotting and LC-MS/MS analysis, we successfully identified 29 proteins, with seven being uniquely O-GlcNAcylated or associated with O-GlcNAcylation in cancer.
23576270	7	2	theme	RNA	1154:1156	arg1	metabolism					1158:1167	RNA metabolism	1154:1167	RNA metabolism	1154:1167	In addition, proteins associated with RNA metabolism, gene expression, and cytoskeleton were highly O-GlcNAcylated or associated with O-GlcNAcylation.
23576270	1	3	theme	cytoplasmic	158:168	arg1	proteins					170:177	nuclear and cytoplasmic proteins	146:177	nuclear and cytoplasmic proteins	146:177	O-GlcNAcylation is a dynamic PTM of nuclear and cytoplasmic proteins, regulated by O-GlcNAc transferase (OGT) and O-GlcNAcase, which catalyze the addition and removal of O-GlcNAc, respectively.
23576270	0	4	theme	primary	87:93	arg1	cancer					102:107	primary breast cancer	87:107	primary breast cancer	87:107	Proteomic analysis and abrogated expression of O-GlcNAcylated proteins associated with primary breast cancer.
23576270	10	5	theme	O-GlcNAc-modified	1525:1541	arg1	proteins					1543:1550	these O-GlcNAc-modified proteins	1519:1550	these O-GlcNAc-modified proteins	1519:1550	Abnormal modification of these O-GlcNAc-modified proteins might be one of the vital malignant characteristics of cancer.
23576270	3	6	theme	total	522:526	arg1	O-GlcNAcylation					528:542	the total O-GlcNAcylation	518:542	the total O-GlcNAcylation in cancer	518:552	Although emerging evidence reveals that some tumor-associated proteins are O-GlcNAc modified, the total O-GlcNAcylation in cancer is still largely unexplored.
23576270	10	7	theme	proteins	1543:1550	arg1	modification					1503:1514	Abnormal modification	1494:1514	Abnormal modification of these O-GlcNAc-modified proteins	1494:1550	Abnormal modification of these O-GlcNAc-modified proteins might be one of the vital malignant characteristics of cancer.
23576270	4	8	theme	OGT	767:769	arg1	level					771:775	OGT level	767:775	OGT level	767:775	Here, we demonstrate that O-GlcNAcylation was increased in primary breast malignant tumors, not in benign tumors and that this augmentation was associated with increased expression of OGT level.
23576270	6	9	theme	Warburg	1015:1021	arg1	effect					1023:1028	the Warburg effect	1011:1028	the Warburg effect	1011:1028	Of these identified proteins, some were related to the Warburg effect, including metabolic enzymes, proteins involved in stress responses and biosynthesis.
23576270	3	10	from	O-GlcNAcylation	528:542	arg1	cancer					547:552	cancer	547:552	cancer	547:552	Although emerging evidence reveals that some tumor-associated proteins are O-GlcNAc modified, the total O-GlcNAcylation in cancer is still largely unexplored.
23576270	9	11	theme	aberrant	1427:1434	arg1	O-GlcNAcylation					1444:1458	aberrant protein O-GlcNAcylation	1427:1458	aberrant protein O-GlcNAcylation	1427:1458	These data indicate that aberrant protein O-GlcNAcylation is associated with breast cancer.
23576270	8	12	theme	decreasing	1303:1312	arg1	O-GlcNAcylation					1314:1328	decreasing O-GlcNAcylation	1303:1328	decreasing O-GlcNAcylation	1303:1328	Moreover, OGT knockdown showed that decreasing O-GlcNAcylation was related to inhibition of the anchorage-independent growth in vitro.
23576270	2	13	theme	many	392:395	arg1	cancer					416:421	cancer	416:421	cancer	416:421	This modification is associated with glucose metabolism, which plays important roles in many diseases including cancer.
23576270	2	13	theme	many	392:395	arg1	diseases					397:404	many diseases	392:404	many diseases including cancer	392:421	This modification is associated with glucose metabolism, which plays important roles in many diseases including cancer.
23576270	7	14	theme	gene	1170:1173	arg1	expression					1175:1184	gene expression	1170:1184	gene expression	1170:1184	In addition, proteins associated with RNA metabolism, gene expression, and cytoskeleton were highly O-GlcNAcylated or associated with O-GlcNAcylation.
23576270	8	15	theme	OGT	1277:1279	arg1	knockdown					1281:1289	OGT knockdown	1277:1289	OGT knockdown	1277:1289	Moreover, OGT knockdown showed that decreasing O-GlcNAcylation was related to inhibition of the anchorage-independent growth in vitro.
23576270	5	16	theme	O-GlcNAc	787:794	arg1	immnoblotting					796:808	2D O-GlcNAc immnoblotting	784:808	2D O-GlcNAc immnoblotting	784:808	Using 2D O-GlcNAc immnoblotting and LC-MS/MS analysis, we successfully identified 29 proteins, with seven being uniquely O-GlcNAcylated or associated with O-GlcNAcylation in cancer.
23576270	10	17	theme	Abnormal	1494:1501	arg1	modification					1503:1514	Abnormal modification	1494:1514	Abnormal modification of these O-GlcNAc-modified proteins	1494:1550	Abnormal modification of these O-GlcNAc-modified proteins might be one of the vital malignant characteristics of cancer.
23576270	0	18	theme	Proteomic	0:8	arg1	analysis					10:17	Proteomic analysis	0:17	Proteomic analysis	0:17	Proteomic analysis and abrogated expression of O-GlcNAcylated proteins associated with primary breast cancer.
23576270	9	19	theme	protein	1436:1442	arg1	O-GlcNAcylation					1444:1458	aberrant protein O-GlcNAcylation	1427:1458	aberrant protein O-GlcNAcylation	1427:1458	These data indicate that aberrant protein O-GlcNAcylation is associated with breast cancer.
23576270	3	20	theme	emerging	433:440	arg1	evidence					442:449	emerging evidence	433:449	emerging evidence	433:449	Although emerging evidence reveals that some tumor-associated proteins are O-GlcNAc modified, the total O-GlcNAcylation in cancer is still largely unexplored.
23576270	0	21	theme	abrogated	23:31	arg1	expression					33:42	abrogated expression	23:42	abrogated expression of O-GlcNAcylated proteins	23:69	Proteomic analysis and abrogated expression of O-GlcNAcylated proteins associated with primary breast cancer.
23576270	7	22	from	addition	1119:1126	arg1	O-GlcNAcylated					1216:1229	O-GlcNAcylated	1216:1229	O-GlcNAcylated	1216:1229	In addition, proteins associated with RNA metabolism, gene expression, and cytoskeleton were highly O-GlcNAcylated or associated with O-GlcNAcylation.
23576270	10	23	theme	characteristics	1588:1602	arg1	characteristics					1588:1602	the vital malignant characteristics	1568:1602	the vital malignant characteristics of cancer	1568:1612	Abnormal modification of these O-GlcNAc-modified proteins might be one of the vital malignant characteristics of cancer.
23576270	10	23	theme	characteristics	1588:1602	arg1	one					1561:1563	one	1561:1563	one	1561:1563	Abnormal modification of these O-GlcNAc-modified proteins might be one of the vital malignant characteristics of cancer.
23576270	4	24	theme	level	771:775	arg1	expression					753:762	increased expression	743:762	increased expression of OGT level	743:775	Here, we demonstrate that O-GlcNAcylation was increased in primary breast malignant tumors, not in benign tumors and that this augmentation was associated with increased expression of OGT level.
23576270	4	25	from	tumors	667:672	arg1	tumors					689:694	benign tumors	682:694	benign tumors	682:694	Here, we demonstrate that O-GlcNAcylation was increased in primary breast malignant tumors, not in benign tumors and that this augmentation was associated with increased expression of OGT level.
23576270	3	26	theme	tumor-associated	469:484	arg1	proteins					486:493	some tumor-associated proteins	464:493	some tumor-associated proteins	464:493	Although emerging evidence reveals that some tumor-associated proteins are O-GlcNAc modified, the total O-GlcNAcylation in cancer is still largely unexplored.
23576270	1	27	theme	O-GlcNAc	280:287	arg1	removal					269:275	removal	269:275	removal	269:275	O-GlcNAcylation is a dynamic PTM of nuclear and cytoplasmic proteins, regulated by O-GlcNAc transferase (OGT) and O-GlcNAcase, which catalyze the addition and removal of O-GlcNAc, respectively.
23576270	1	27	theme	O-GlcNAc	280:287	arg1	addition					256:263	addition	256:263	addition	256:263	O-GlcNAcylation is a dynamic PTM of nuclear and cytoplasmic proteins, regulated by O-GlcNAc transferase (OGT) and O-GlcNAcase, which catalyze the addition and removal of O-GlcNAc, respectively.
23576270	10	28	theme	malignant	1578:1586	arg1	characteristics					1588:1602	the vital malignant characteristics	1568:1602	the vital malignant characteristics of cancer	1568:1612	Abnormal modification of these O-GlcNAc-modified proteins might be one of the vital malignant characteristics of cancer.
23576270	7	29	from	O-GlcNAcylated	1216:1229	arg1	addition					1119:1126	addition	1119:1126	addition	1119:1126	In addition, proteins associated with RNA metabolism, gene expression, and cytoskeleton were highly O-GlcNAcylated or associated with O-GlcNAcylation.
23576270	1	30	theme	proteins	170:177	arg1	PTM					139:141	a dynamic PTM	129:141	a dynamic PTM	129:141	O-GlcNAcylation is a dynamic PTM of nuclear and cytoplasmic proteins, regulated by O-GlcNAc transferase (OGT) and O-GlcNAcase, which catalyze the addition and removal of O-GlcNAc, respectively.
23576270	1	30	theme	proteins	170:177	arg1	O-GlcNAcylation					110:124	O-GlcNAcylation	110:124	O-GlcNAcylation	110:124	O-GlcNAcylation is a dynamic PTM of nuclear and cytoplasmic proteins, regulated by O-GlcNAc transferase (OGT) and O-GlcNAcase, which catalyze the addition and removal of O-GlcNAc, respectively.
23576270	4	31	theme	breast	650:655	arg1	tumors					667:672	primary breast malignant tumors	642:672	primary breast malignant tumors	642:672	Here, we demonstrate that O-GlcNAcylation was increased in primary breast malignant tumors, not in benign tumors and that this augmentation was associated with increased expression of OGT level.
23576270	8	32	theme	in	1392:1393	arg1	inhibition					1345:1354	inhibition	1345:1354	inhibition of the anchorage-independent growth in vitro	1345:1399	Moreover, OGT knockdown showed that decreasing O-GlcNAcylation was related to inhibition of the anchorage-independent growth in vitro.
23576270	10	33	theme	vital	1572:1576	arg1	characteristics					1588:1602	the vital malignant characteristics	1568:1602	the vital malignant characteristics of cancer	1568:1612	Abnormal modification of these O-GlcNAc-modified proteins might be one of the vital malignant characteristics of cancer.
23576270	8	34	theme	growth	1385:1390	arg1	inhibition					1345:1354	inhibition	1345:1354	inhibition of the anchorage-independent growth in vitro	1345:1399	Moreover, OGT knockdown showed that decreasing O-GlcNAcylation was related to inhibition of the anchorage-independent growth in vitro.
23576270	2	35	theme	important	373:381	arg1	roles					383:387	important roles	373:387	important roles	373:387	This modification is associated with glucose metabolism, which plays important roles in many diseases including cancer.
23576270	6	36	theme	metabolic	1041:1049	arg1	proteins					1060:1067	proteins	1060:1067	proteins involved in stress responses and biosynthesis	1060:1113	Of these identified proteins, some were related to the Warburg effect, including metabolic enzymes, proteins involved in stress responses and biosynthesis.
23576270	6	36	theme	metabolic	1041:1049	arg1	enzymes					1051:1057	metabolic enzymes	1041:1057	metabolic enzymes	1041:1057	Of these identified proteins, some were related to the Warburg effect, including metabolic enzymes, proteins involved in stress responses and biosynthesis.
23576270	0	37	theme	proteins	62:69	arg1	analysis					10:17	Proteomic analysis	0:17	Proteomic analysis	0:17	Proteomic analysis and abrogated expression of O-GlcNAcylated proteins associated with primary breast cancer.
23576270	0	37	theme	proteins	62:69	arg1	expression					33:42	abrogated expression	23:42	abrogated expression of O-GlcNAcylated proteins	23:69	Proteomic analysis and abrogated expression of O-GlcNAcylated proteins associated with primary breast cancer.
23576270	6	38	theme	proteins	980:987	arg1	related					1000:1006	related	1000:1006	related	1000:1006	Of these identified proteins, some were related to the Warburg effect, including metabolic enzymes, proteins involved in stress responses and biosynthesis.
23576270	1	39	theme	O-GlcNAc	193:200	arg1	OGT					215:217	OGT	215:217	OGT	215:217	O-GlcNAcylation is a dynamic PTM of nuclear and cytoplasmic proteins, regulated by O-GlcNAc transferase (OGT) and O-GlcNAcase, which catalyze the addition and removal of O-GlcNAc, respectively.
23576270	1	39	theme	O-GlcNAc	193:200	arg1	transferase					202:212	O-GlcNAc transferase	193:212	O-GlcNAc transferase (OGT)	193:218	O-GlcNAcylation is a dynamic PTM of nuclear and cytoplasmic proteins, regulated by O-GlcNAc transferase (OGT) and O-GlcNAcase, which catalyze the addition and removal of O-GlcNAc, respectively.
23576270	2	40	theme	glucose	341:347	arg1	metabolism					349:358	glucose metabolism	341:358	glucose metabolism	341:358	This modification is associated with glucose metabolism, which plays important roles in many diseases including cancer.
23576270	0	41	theme	O-GlcNAcylated	47:60	arg1	proteins					62:69	O-GlcNAcylated proteins	47:69	O-GlcNAcylated proteins	47:69	Proteomic analysis and abrogated expression of O-GlcNAcylated proteins associated with primary breast cancer.
23576270	6	42	theme	identified	969:978	arg1	proteins					980:987	these identified proteins	963:987	these identified proteins	963:987	Of these identified proteins, some were related to the Warburg effect, including metabolic enzymes, proteins involved in stress responses and biosynthesis.
23576270	1	43	dep	addition	256:263	arg1	the					252:254	the	252:254	the	252:254	O-GlcNAcylation is a dynamic PTM of nuclear and cytoplasmic proteins, regulated by O-GlcNAc transferase (OGT) and O-GlcNAcase, which catalyze the addition and removal of O-GlcNAc, respectively.
23576270	1	44	theme	dynamic	131:137	arg1	PTM					139:141	a dynamic PTM	129:141	a dynamic PTM	129:141	O-GlcNAcylation is a dynamic PTM of nuclear and cytoplasmic proteins, regulated by O-GlcNAc transferase (OGT) and O-GlcNAcase, which catalyze the addition and removal of O-GlcNAc, respectively.
23576270	1	44	theme	dynamic	131:137	arg1	O-GlcNAcylation					110:124	O-GlcNAcylation	110:124	O-GlcNAcylation	110:124	O-GlcNAcylation is a dynamic PTM of nuclear and cytoplasmic proteins, regulated by O-GlcNAc transferase (OGT) and O-GlcNAcase, which catalyze the addition and removal of O-GlcNAc, respectively.
23576270	10	45	theme	cancer	1607:1612	arg1	characteristics					1588:1602	the vital malignant characteristics	1568:1602	the vital malignant characteristics of cancer	1568:1612	Abnormal modification of these O-GlcNAc-modified proteins might be one of the vital malignant characteristics of cancer.
23576270	4	46	theme	benign	682:687	arg1	tumors					689:694	benign tumors	682:694	benign tumors	682:694	Here, we demonstrate that O-GlcNAcylation was increased in primary breast malignant tumors, not in benign tumors and that this augmentation was associated with increased expression of OGT level.
23576270	8	47	dep	in	1392:1393	arg1	vitro					1395:1399	vitro	1395:1399	vitro	1395:1399	Moreover, OGT knockdown showed that decreasing O-GlcNAcylation was related to inhibition of the anchorage-independent growth in vitro.
23576270	4	48	theme	increased	743:751	arg1	expression					753:762	increased expression	743:762	increased expression of OGT level	743:775	Here, we demonstrate that O-GlcNAcylation was increased in primary breast malignant tumors, not in benign tumors and that this augmentation was associated with increased expression of OGT level.
23576270	6	49	theme	stress	1081:1086	arg1	responses					1088:1096	stress responses	1081:1096	stress responses	1081:1096	Of these identified proteins, some were related to the Warburg effect, including metabolic enzymes, proteins involved in stress responses and biosynthesis.
23576270	4	50	theme	malignant	657:665	arg1	tumors					667:672	primary breast malignant tumors	642:672	primary breast malignant tumors	642:672	Here, we demonstrate that O-GlcNAcylation was increased in primary breast malignant tumors, not in benign tumors and that this augmentation was associated with increased expression of OGT level.
23576270	1	51	theme	nuclear	146:152	arg1	proteins					170:177	nuclear and cytoplasmic proteins	146:177	nuclear and cytoplasmic proteins	146:177	O-GlcNAcylation is a dynamic PTM of nuclear and cytoplasmic proteins, regulated by O-GlcNAc transferase (OGT) and O-GlcNAcase, which catalyze the addition and removal of O-GlcNAc, respectively.
23576270	4	52	theme	primary	642:648	arg1	tumors					667:672	primary breast malignant tumors	642:672	primary breast malignant tumors	642:672	Here, we demonstrate that O-GlcNAcylation was increased in primary breast malignant tumors, not in benign tumors and that this augmentation was associated with increased expression of OGT level.
23576270	5	53	theme	LC-MS/MS	814:821	arg1	analysis					823:830	LC-MS/MS analysis	814:830	LC-MS/MS analysis	814:830	Using 2D O-GlcNAc immnoblotting and LC-MS/MS analysis, we successfully identified 29 proteins, with seven being uniquely O-GlcNAcylated or associated with O-GlcNAcylation in cancer.
23576270	8	54	theme	anchorage-independent	1363:1383	arg1	growth					1385:1390	the anchorage-independent growth	1359:1390	the anchorage-independent growth	1359:1390	Moreover, OGT knockdown showed that decreasing O-GlcNAcylation was related to inhibition of the anchorage-independent growth in vitro.
23576270	9	55	theme	breast	1479:1484	arg1	cancer					1486:1491	breast cancer	1479:1491	breast cancer	1479:1491	These data indicate that aberrant protein O-GlcNAcylation is associated with breast cancer.
26853435	4	0	theme	Ac4	591:593	arg1	GlcNAz					595:600	Ac4 GlcNAz	591:600	Ac4 GlcNAz	591:600	Here, using peracetylated N-azidoacetylglucosamine (Ac4 GlcNAz) as a bioorthogonal chemical handle, we described a gel-based mass spectrometry method for the identification of proteins with O-GlcNAc modification in A549 cells.
26853435	4	0	theme	Ac4	591:593	arg1	N-azidoacetylglucosamine					565:588	peracetylated N-azidoacetylglucosamine	551:588	peracetylated N-azidoacetylglucosamine (Ac4 GlcNAz)	551:601	Here, using peracetylated N-azidoacetylglucosamine (Ac4 GlcNAz) as a bioorthogonal chemical handle, we described a gel-based mass spectrometry method for the identification of proteins with O-GlcNAc modification in A549 cells.
26853435	4	1	with	proteins	715:722	arg1	modification					738:749	O-GlcNAc modification	729:749	O-GlcNAc modification in A549 cells	729:763	Here, using peracetylated N-azidoacetylglucosamine (Ac4 GlcNAz) as a bioorthogonal chemical handle, we described a gel-based mass spectrometry method for the identification of proteins with O-GlcNAc modification in A549 cells.
26853435	2	2	theme	nutrient	343:350	arg1	sensing					352:358	nutrient sensing	343:358	nutrient sensing	343:358	It is involved in various cellular processes such as nutrient sensing, protein degradation, gene expression, and is associated with many human diseases.
26853435	2	2	theme	nutrient	343:350	arg1	degradation					369:379	protein degradation	361:379	protein degradation	361:379	It is involved in various cellular processes such as nutrient sensing, protein degradation, gene expression, and is associated with many human diseases.
26853435	2	2	theme	nutrient	343:350	arg1	expression					387:396	gene expression	382:396	gene expression	382:396	It is involved in various cellular processes such as nutrient sensing, protein degradation, gene expression, and is associated with many human diseases.
26853435	6	3	with	proteins	1141:1148	arg1	modification					1164:1175	O-GlcNAc modification	1155:1175	O-GlcNAc modification	1155:1175	After conjugation with click chemistry in vitro and enrichment via streptavidin resin, proteins with O-GlcNAc modification were separated by SDS-PAGE and identified with mass spectrometry.
26853435	9	4	theme	protein	1859:1865	arg1	identification					1867:1880	higher protein identification	1852:1880	higher protein identification	1852:1880	These results suggested that CuAAC with Biotin-Diazo-Alkyne represented a more powerful method in proteomics with higher protein identification and better accuracy compared to SPAAC.
26853435	4	5	theme	gel-based	654:662	arg1	method					682:687	a gel-based mass spectrometry method	652:687	a gel-based mass spectrometry method for the identification of proteins with O-GlcNAc modification in A549 cells	652:763	Here, using peracetylated N-azidoacetylglucosamine (Ac4 GlcNAz) as a bioorthogonal chemical handle, we described a gel-based mass spectrometry method for the identification of proteins with O-GlcNAc modification in A549 cells.
26853435	7	6	with	sample	1374:1379	arg1	Biotin-DIBO-Alkyne					1403:1420	Biotin-DIBO-Alkyne	1403:1420	Biotin-DIBO-Alkyne	1403:1420	Proteomics data analysis revealed that 229 putative O-GlcNAc modified proteins were identified with Biotin-Diazo-Alkyne conjugated sample and 188 proteins with Biotin-DIBO-Alkyne conjugated sample, among which 114 proteins were overlapping.
26853435	7	7	theme	data	1254:1257	arg1	analysis					1259:1266	Proteomics data analysis	1243:1266	Proteomics data analysis	1243:1266	Proteomics data analysis revealed that 229 putative O-GlcNAc modified proteins were identified with Biotin-Diazo-Alkyne conjugated sample and 188 proteins with Biotin-DIBO-Alkyne conjugated sample, among which 114 proteins were overlapping.
26853435	0	8	theme	cycloaddition	54:66	arg1	analysis					12:19	Comparative analysis	0:19	Comparative analysis of Cu (I)-catalyzed alkyne-azide cycloaddition (CuAAC) and strain-promoted alkyne-azide cycloaddition (SPAAC) in O-GlcNAc proteomics.	0:153	Comparative analysis of Cu (I)-catalyzed alkyne-azide cycloaddition (CuAAC) and strain-promoted alkyne-azide cycloaddition (SPAAC) in O-GlcNAc proteomics.
26853435	6	9	theme	mass	1224:1227	arg1	spectrometry					1229:1240	mass spectrometry	1224:1240	mass spectrometry	1224:1240	After conjugation with click chemistry in vitro and enrichment via streptavidin resin, proteins with O-GlcNAc modification were separated by SDS-PAGE and identified with mass spectrometry.
26853435	4	10	theme	spectrometry	669:680	arg1	method					682:687	a gel-based mass spectrometry method	652:687	a gel-based mass spectrometry method for the identification of proteins with O-GlcNAc modification in A549 cells	652:763	Here, using peracetylated N-azidoacetylglucosamine (Ac4 GlcNAz) as a bioorthogonal chemical handle, we described a gel-based mass spectrometry method for the identification of proteins with O-GlcNAc modification in A549 cells.
26853435	11	11	theme	SDS-PAGE	2144:2151	arg1	separation					2153:2162	SDS-PAGE separation	2144:2162	SDS-PAGE separation	2144:2162	Together, the method we reported here combining metabolic labeling, click chemistry, affinity-based enrichment, SDS-PAGE separation, and mass spectrometry, would be adaptable for other post-translationally modified proteins in proteomics.
26853435	0	12	theme	cycloaddition	109:121	arg1	analysis					12:19	Comparative analysis	0:19	Comparative analysis of Cu (I)-catalyzed alkyne-azide cycloaddition (CuAAC) and strain-promoted alkyne-azide cycloaddition (SPAAC) in O-GlcNAc proteomics.	0:153	Comparative analysis of Cu (I)-catalyzed alkyne-azide cycloaddition (CuAAC) and strain-promoted alkyne-azide cycloaddition (SPAAC) in O-GlcNAc proteomics.
26853435	9	13	with	proteomics	1836:1845	arg1	identification					1867:1880	higher protein identification	1852:1880	higher protein identification	1852:1880	These results suggested that CuAAC with Biotin-Diazo-Alkyne represented a more powerful method in proteomics with higher protein identification and better accuracy compared to SPAAC.
26853435	10	14	dep	ontology	2017:2024	arg1	GO					2027:2028	GO	2027:2028	GO	2027:2028	The proteomics credibility was also confirmed by the molecular function and cell component gene ontology (GO).
26853435	10	15	theme	gene	2012:2015	arg1	ontology					2017:2024	cell component gene ontology	1997:2024	cell component gene ontology (GO)	1997:2029	The proteomics credibility was also confirmed by the molecular function and cell component gene ontology (GO).
26853435	5	16	theme	bioorthogonal	854:866	arg1	reactions					868:876	azide-alkyne bioorthogonal reactions	841:876	azide-alkyne bioorthogonal reactions in click chemistry	841:895	In addition, we made a labeling efficiency comparison between two modes of azide-alkyne bioorthogonal reactions in click chemistry: copper-catalyzed azide-alkyne cycloaddition (CuAAC) with Biotin-Diazo-Alkyne and stain-promoted azide-alkyne cycloaddition (SPAAC) with Biotin-DIBO-Alkyne.
26853435	8	17	theme	Biotin-DIBO-Alkyne	1588:1605	arg1	conjugates					1607:1616	Biotin-DIBO-Alkyne conjugates	1588:1616	Biotin-DIBO-Alkyne conjugates	1588:1616	Interestingly, 74 proteins identified from Biotin-Diazo-Alkyne conjugates and 46 verified proteins from Biotin-DIBO-Alkyne conjugates could be found in the O-GlcNAc modified proteins database dbOGAP (http://cbsb.lombardi.georgetown.edu/hulab/OGAP.html).
26853435	4	18	theme	proteins	715:722	arg1	identification					697:710	the identification	693:710	the identification of proteins with O-GlcNAc modification in A549 cells	693:763	Here, using peracetylated N-azidoacetylglucosamine (Ac4 GlcNAz) as a bioorthogonal chemical handle, we described a gel-based mass spectrometry method for the identification of proteins with O-GlcNAc modification in A549 cells.
26853435	10	19	theme	cell	1997:2000	arg1	ontology					2017:2024	cell component gene ontology	1997:2024	cell component gene ontology (GO)	1997:2029	The proteomics credibility was also confirmed by the molecular function and cell component gene ontology (GO).
26853435	5	20	from	modes	832:836	arg1	chemistry					887:895	click chemistry	881:895	click chemistry	881:895	In addition, we made a labeling efficiency comparison between two modes of azide-alkyne bioorthogonal reactions in click chemistry: copper-catalyzed azide-alkyne cycloaddition (CuAAC) with Biotin-Diazo-Alkyne and stain-promoted azide-alkyne cycloaddition (SPAAC) with Biotin-DIBO-Alkyne.
26853435	4	21	theme	O-GlcNAc	729:736	arg1	modification					738:749	O-GlcNAc modification	729:749	O-GlcNAc modification in A549 cells	729:763	Here, using peracetylated N-azidoacetylglucosamine (Ac4 GlcNAz) as a bioorthogonal chemical handle, we described a gel-based mass spectrometry method for the identification of proteins with O-GlcNAc modification in A549 cells.
26853435	6	22	theme	click	1077:1081	arg1	chemistry					1083:1091	click chemistry	1077:1091	click chemistry	1077:1091	After conjugation with click chemistry in vitro and enrichment via streptavidin resin, proteins with O-GlcNAc modification were separated by SDS-PAGE and identified with mass spectrometry.
26853435	0	23	theme	alkyne-azide	41:52	arg1	CuAAC					69:73	CuAAC	69:73	CuAAC	69:73	Comparative analysis of Cu (I)-catalyzed alkyne-azide cycloaddition (CuAAC) and strain-promoted alkyne-azide cycloaddition (SPAAC) in O-GlcNAc proteomics.
26853435	0	23	theme	alkyne-azide	41:52	arg1	cycloaddition					54:66	Cu (I)-catalyzed alkyne-azide cycloaddition	24:66	Cu (I)-catalyzed alkyne-azide cycloaddition (CuAAC)	24:74	Comparative analysis of Cu (I)-catalyzed alkyne-azide cycloaddition (CuAAC) and strain-promoted alkyne-azide cycloaddition (SPAAC) in O-GlcNAc proteomics.
26853435	11	24	theme	mass	2169:2172	arg1	spectrometry					2174:2185	mass spectrometry	2169:2185	mass spectrometry	2169:2185	Together, the method we reported here combining metabolic labeling, click chemistry, affinity-based enrichment, SDS-PAGE separation, and mass spectrometry, would be adaptable for other post-translationally modified proteins in proteomics.
26853435	5	25	from	reactions	868:876	arg1	chemistry					887:895	click chemistry	881:895	click chemistry	881:895	In addition, we made a labeling efficiency comparison between two modes of azide-alkyne bioorthogonal reactions in click chemistry: copper-catalyzed azide-alkyne cycloaddition (CuAAC) with Biotin-Diazo-Alkyne and stain-promoted azide-alkyne cycloaddition (SPAAC) with Biotin-DIBO-Alkyne.
26853435	5	26	theme	copper-catalyzed	898:913	arg1	CuAAC					943:947	CuAAC	943:947	CuAAC	943:947	In addition, we made a labeling efficiency comparison between two modes of azide-alkyne bioorthogonal reactions in click chemistry: copper-catalyzed azide-alkyne cycloaddition (CuAAC) with Biotin-Diazo-Alkyne and stain-promoted azide-alkyne cycloaddition (SPAAC) with Biotin-DIBO-Alkyne.
26853435	5	26	theme	copper-catalyzed	898:913	arg1	modes					832:836	two modes	828:836	two modes of azide-alkyne bioorthogonal reactions in click chemistry: copper-catalyzed azide-alkyne cycloaddition (CuAAC) with Biotin-Diazo-Alkyne and stain-promoted azide-alkyne cycloaddition (SPAAC)	828:1027	In addition, we made a labeling efficiency comparison between two modes of azide-alkyne bioorthogonal reactions in click chemistry: copper-catalyzed azide-alkyne cycloaddition (CuAAC) with Biotin-Diazo-Alkyne and stain-promoted azide-alkyne cycloaddition (SPAAC) with Biotin-DIBO-Alkyne.
26853435	5	26	theme	copper-catalyzed	898:913	arg1	cycloaddition					928:940	copper-catalyzed azide-alkyne cycloaddition	898:940	copper-catalyzed azide-alkyne cycloaddition (CuAAC) with Biotin-Diazo-Alkyne	898:973	In addition, we made a labeling efficiency comparison between two modes of azide-alkyne bioorthogonal reactions in click chemistry: copper-catalyzed azide-alkyne cycloaddition (CuAAC) with Biotin-Diazo-Alkyne and stain-promoted azide-alkyne cycloaddition (SPAAC) with Biotin-DIBO-Alkyne.
26853435	8	27	located	found	1627:1631	arg2	proteins					1502:1509	74 proteins	1499:1509	74 proteins identified from Biotin-Diazo-Alkyne conjugates	1499:1556	Interestingly, 74 proteins identified from Biotin-Diazo-Alkyne conjugates and 46 verified proteins from Biotin-DIBO-Alkyne conjugates could be found in the O-GlcNAc modified proteins database dbOGAP (http://cbsb.lombardi.georgetown.edu/hulab/OGAP.html).
26853435	8	27	located	found	1627:1631	arg1	proteins					1658:1665	the O-GlcNAc modified proteins database dbOGAP (http://cbsb.lombardi.georgetown.edu/hulab/OGAP.html)	1636:1735	the O-GlcNAc modified proteins database dbOGAP (http://cbsb.lombardi.georgetown.edu/hulab/OGAP.html)	1636:1735	Interestingly, 74 proteins identified from Biotin-Diazo-Alkyne conjugates and 46 verified proteins from Biotin-DIBO-Alkyne conjugates could be found in the O-GlcNAc modified proteins database dbOGAP (http://cbsb.lombardi.georgetown.edu/hulab/OGAP.html).
26853435	8	27	located	found	1627:1631	arg2	proteins					1574:1581	46 verified proteins	1562:1581	46 verified proteins	1562:1581	Interestingly, 74 proteins identified from Biotin-Diazo-Alkyne conjugates and 46 verified proteins from Biotin-DIBO-Alkyne conjugates could be found in the O-GlcNAc modified proteins database dbOGAP (http://cbsb.lombardi.georgetown.edu/hulab/OGAP.html).
26853435	8	28	theme	modified	1649:1656	arg1	proteins					1658:1665	the O-GlcNAc modified proteins database dbOGAP (http://cbsb.lombardi.georgetown.edu/hulab/OGAP.html)	1636:1735	the O-GlcNAc modified proteins database dbOGAP (http://cbsb.lombardi.georgetown.edu/hulab/OGAP.html)	1636:1735	Interestingly, 74 proteins identified from Biotin-Diazo-Alkyne conjugates and 46 verified proteins from Biotin-DIBO-Alkyne conjugates could be found in the O-GlcNAc modified proteins database dbOGAP (http://cbsb.lombardi.georgetown.edu/hulab/OGAP.html).
26853435	7	29	dep	sample	1374:1379	arg1	sample					1433:1438	conjugated sample	1422:1438	conjugated sample	1422:1438	Proteomics data analysis revealed that 229 putative O-GlcNAc modified proteins were identified with Biotin-Diazo-Alkyne conjugated sample and 188 proteins with Biotin-DIBO-Alkyne conjugated sample, among which 114 proteins were overlapping.
26853435	8	30	theme	database	1667:1674	arg1	dbOGAP					1676:1681	database dbOGAP	1667:1681	the O-GlcNAc modified proteins database dbOGAP (http://cbsb.lombardi.georgetown.edu/hulab/OGAP.html)	1636:1735	Interestingly, 74 proteins identified from Biotin-Diazo-Alkyne conjugates and 46 verified proteins from Biotin-DIBO-Alkyne conjugates could be found in the O-GlcNAc modified proteins database dbOGAP (http://cbsb.lombardi.georgetown.edu/hulab/OGAP.html).
26853435	0	31	theme	strain-promoted	80:94	arg1	SPAAC					124:128	SPAAC	124:128	SPAAC	124:128	Comparative analysis of Cu (I)-catalyzed alkyne-azide cycloaddition (CuAAC) and strain-promoted alkyne-azide cycloaddition (SPAAC) in O-GlcNAc proteomics.
26853435	0	31	theme	strain-promoted	80:94	arg1	cycloaddition					109:121	strain-promoted alkyne-azide cycloaddition	80:121	strain-promoted alkyne-azide cycloaddition (SPAAC)	80:129	Comparative analysis of Cu (I)-catalyzed alkyne-azide cycloaddition (CuAAC) and strain-promoted alkyne-azide cycloaddition (SPAAC) in O-GlcNAc proteomics.
26853435	11	32	dep	method	2046:2051	arg1	we					2053:2054	we	2053:2054	we	2053:2054	Together, the method we reported here combining metabolic labeling, click chemistry, affinity-based enrichment, SDS-PAGE separation, and mass spectrometry, would be adaptable for other post-translationally modified proteins in proteomics.
26853435	1	33	link	O-linked	155:162	arg1	O-GlcNAc					187:194	O-GlcNAc	187:194	O-GlcNAc	187:194	O-linked β-N-acetylglucosamine (O-GlcNAc) is emerging as an essential protein post-translational modification in a range of organisms.
26853435	1	33	link	O-linked	155:162	arg1	β-N-acetylglucosamine					164:184	O-linked β-N-acetylglucosamine	155:184	O-linked β-N-acetylglucosamine (O-GlcNAc)	155:195	O-linked β-N-acetylglucosamine (O-GlcNAc) is emerging as an essential protein post-translational modification in a range of organisms.
26853435	7	34	theme	modified	1304:1311	arg1	proteins					1313:1320	229 putative O-GlcNAc modified proteins	1282:1320	229 putative O-GlcNAc modified proteins	1282:1320	Proteomics data analysis revealed that 229 putative O-GlcNAc modified proteins were identified with Biotin-Diazo-Alkyne conjugated sample and 188 proteins with Biotin-DIBO-Alkyne conjugated sample, among which 114 proteins were overlapping.
26853435	11	35	theme	metabolic	2080:2088	arg1	labeling					2090:2097	metabolic labeling	2080:2097	metabolic labeling	2080:2097	Together, the method we reported here combining metabolic labeling, click chemistry, affinity-based enrichment, SDS-PAGE separation, and mass spectrometry, would be adaptable for other post-translationally modified proteins in proteomics.
26853435	0	36	theme	Comparative	0:10	arg1	analysis					12:19	Comparative analysis	0:19	Comparative analysis of Cu (I)-catalyzed alkyne-azide cycloaddition (CuAAC) and strain-promoted alkyne-azide cycloaddition (SPAAC) in O-GlcNAc proteomics.	0:153	Comparative analysis of Cu (I)-catalyzed alkyne-azide cycloaddition (CuAAC) and strain-promoted alkyne-azide cycloaddition (SPAAC) in O-GlcNAc proteomics.
26853435	2	37	theme	many	422:425	arg1	diseases					433:440	many human diseases	422:440	many human diseases	422:440	It is involved in various cellular processes such as nutrient sensing, protein degradation, gene expression, and is associated with many human diseases.
26853435	11	38	theme	affinity-based	2117:2130	arg1	enrichment					2132:2141	affinity-based enrichment	2117:2141	affinity-based enrichment	2117:2141	Together, the method we reported here combining metabolic labeling, click chemistry, affinity-based enrichment, SDS-PAGE separation, and mass spectrometry, would be adaptable for other post-translationally modified proteins in proteomics.
26853435	5	39	theme	azide-alkyne	994:1005	arg1	modes					832:836	two modes	828:836	two modes of azide-alkyne bioorthogonal reactions in click chemistry: copper-catalyzed azide-alkyne cycloaddition (CuAAC) with Biotin-Diazo-Alkyne and stain-promoted azide-alkyne cycloaddition (SPAAC)	828:1027	In addition, we made a labeling efficiency comparison between two modes of azide-alkyne bioorthogonal reactions in click chemistry: copper-catalyzed azide-alkyne cycloaddition (CuAAC) with Biotin-Diazo-Alkyne and stain-promoted azide-alkyne cycloaddition (SPAAC) with Biotin-DIBO-Alkyne.
26853435	5	39	theme	azide-alkyne	994:1005	arg1	SPAAC					1022:1026	SPAAC	1022:1026	SPAAC	1022:1026	In addition, we made a labeling efficiency comparison between two modes of azide-alkyne bioorthogonal reactions in click chemistry: copper-catalyzed azide-alkyne cycloaddition (CuAAC) with Biotin-Diazo-Alkyne and stain-promoted azide-alkyne cycloaddition (SPAAC) with Biotin-DIBO-Alkyne.
26853435	5	39	theme	azide-alkyne	994:1005	arg1	cycloaddition					1007:1019	stain-promoted azide-alkyne cycloaddition	979:1019	stain-promoted azide-alkyne cycloaddition (SPAAC)	979:1027	In addition, we made a labeling efficiency comparison between two modes of azide-alkyne bioorthogonal reactions in click chemistry: copper-catalyzed azide-alkyne cycloaddition (CuAAC) with Biotin-Diazo-Alkyne and stain-promoted azide-alkyne cycloaddition (SPAAC) with Biotin-DIBO-Alkyne.
26853435	7	40	theme	conjugated	1422:1431	arg1	sample					1433:1438	conjugated sample	1422:1438	conjugated sample	1422:1438	Proteomics data analysis revealed that 229 putative O-GlcNAc modified proteins were identified with Biotin-Diazo-Alkyne conjugated sample and 188 proteins with Biotin-DIBO-Alkyne conjugated sample, among which 114 proteins were overlapping.
26853435	4	41	theme	peracetylated	551:563	arg1	GlcNAz					595:600	Ac4 GlcNAz	591:600	Ac4 GlcNAz	591:600	Here, using peracetylated N-azidoacetylglucosamine (Ac4 GlcNAz) as a bioorthogonal chemical handle, we described a gel-based mass spectrometry method for the identification of proteins with O-GlcNAc modification in A549 cells.
26853435	4	41	theme	peracetylated	551:563	arg1	handle					631:636	a bioorthogonal chemical handle	606:636	a bioorthogonal chemical handle	606:636	Here, using peracetylated N-azidoacetylglucosamine (Ac4 GlcNAz) as a bioorthogonal chemical handle, we described a gel-based mass spectrometry method for the identification of proteins with O-GlcNAc modification in A549 cells.
26853435	4	41	theme	peracetylated	551:563	arg1	N-azidoacetylglucosamine					565:588	peracetylated N-azidoacetylglucosamine	551:588	peracetylated N-azidoacetylglucosamine (Ac4 GlcNAz)	551:601	Here, using peracetylated N-azidoacetylglucosamine (Ac4 GlcNAz) as a bioorthogonal chemical handle, we described a gel-based mass spectrometry method for the identification of proteins with O-GlcNAc modification in A549 cells.
26853435	1	42	theme	O-linked	155:162	arg1	O-GlcNAc					187:194	O-GlcNAc	187:194	O-GlcNAc	187:194	O-linked β-N-acetylglucosamine (O-GlcNAc) is emerging as an essential protein post-translational modification in a range of organisms.
26853435	1	42	theme	O-linked	155:162	arg1	β-N-acetylglucosamine					164:184	O-linked β-N-acetylglucosamine	155:184	O-linked β-N-acetylglucosamine (O-GlcNAc)	155:195	O-linked β-N-acetylglucosamine (O-GlcNAc) is emerging as an essential protein post-translational modification in a range of organisms.
26853435	8	43	theme	Biotin-Diazo-Alkyne	1527:1545	arg1	conjugates					1547:1556	Biotin-Diazo-Alkyne conjugates	1527:1556	Biotin-Diazo-Alkyne conjugates	1527:1556	Interestingly, 74 proteins identified from Biotin-Diazo-Alkyne conjugates and 46 verified proteins from Biotin-DIBO-Alkyne conjugates could be found in the O-GlcNAc modified proteins database dbOGAP (http://cbsb.lombardi.georgetown.edu/hulab/OGAP.html).
26853435	3	44	theme	O-GlcNAcylated	479:492	arg1	proteins					494:501	O-GlcNAcylated proteins	479:501	O-GlcNAcylated proteins	479:501	Despite its importance, identifying O-GlcNAcylated proteins is a major challenge in proteomics.
26853435	5	45	theme	labeling	789:796	arg1	comparison					809:818	a labeling efficiency comparison	787:818	a labeling efficiency comparison between two modes of azide-alkyne bioorthogonal reactions in click chemistry: copper-catalyzed azide-alkyne cycloaddition (CuAAC) with Biotin-Diazo-Alkyne and stain-promoted azide-alkyne cycloaddition (SPAAC) with Biotin-DIBO-Alkyne	787:1051	In addition, we made a labeling efficiency comparison between two modes of azide-alkyne bioorthogonal reactions in click chemistry: copper-catalyzed azide-alkyne cycloaddition (CuAAC) with Biotin-Diazo-Alkyne and stain-promoted azide-alkyne cycloaddition (SPAAC) with Biotin-DIBO-Alkyne.
26853435	8	46	dep	http	1684:1687	arg1	//cbsb.lombardi.georgetown.edu/hulab/OGAP.html					1689:1734	//cbsb.lombardi.georgetown.edu/hulab/OGAP.html	1689:1734	http://cbsb.lombardi.georgetown.edu/hulab/OGAP.html	1684:1734	Interestingly, 74 proteins identified from Biotin-Diazo-Alkyne conjugates and 46 verified proteins from Biotin-DIBO-Alkyne conjugates could be found in the O-GlcNAc modified proteins database dbOGAP (http://cbsb.lombardi.georgetown.edu/hulab/OGAP.html).
26853435	6	47	with	enrichment	1106:1115	arg1	chemistry					1083:1091	click chemistry	1077:1091	click chemistry	1077:1091	After conjugation with click chemistry in vitro and enrichment via streptavidin resin, proteins with O-GlcNAc modification were separated by SDS-PAGE and identified with mass spectrometry.
26853435	6	48	theme	O-GlcNAc	1155:1162	arg1	modification					1164:1175	O-GlcNAc modification	1155:1175	O-GlcNAc modification	1155:1175	After conjugation with click chemistry in vitro and enrichment via streptavidin resin, proteins with O-GlcNAc modification were separated by SDS-PAGE and identified with mass spectrometry.
26853435	8	49	theme	verified	1565:1572	arg1	proteins					1574:1581	46 verified proteins	1562:1581	46 verified proteins	1562:1581	Interestingly, 74 proteins identified from Biotin-Diazo-Alkyne conjugates and 46 verified proteins from Biotin-DIBO-Alkyne conjugates could be found in the O-GlcNAc modified proteins database dbOGAP (http://cbsb.lombardi.georgetown.edu/hulab/OGAP.html).
26853435	3	50	theme	major	508:512	arg1	challenge					514:522	a major challenge	506:522	a major challenge in proteomics	506:536	Despite its importance, identifying O-GlcNAcylated proteins is a major challenge in proteomics.
26853435	8	51	dep	dbOGAP	1676:1681	arg1	http					1684:1687	http	1684:1687	http://cbsb.lombardi.georgetown.edu/hulab/OGAP.html	1684:1734	Interestingly, 74 proteins identified from Biotin-Diazo-Alkyne conjugates and 46 verified proteins from Biotin-DIBO-Alkyne conjugates could be found in the O-GlcNAc modified proteins database dbOGAP (http://cbsb.lombardi.georgetown.edu/hulab/OGAP.html).
26853435	7	52	theme	Biotin-Diazo-Alkyne	1343:1361	arg1	sample					1374:1379	Biotin-Diazo-Alkyne conjugated sample	1343:1379	Biotin-Diazo-Alkyne conjugated sample	1343:1379	Proteomics data analysis revealed that 229 putative O-GlcNAc modified proteins were identified with Biotin-Diazo-Alkyne conjugated sample and 188 proteins with Biotin-DIBO-Alkyne conjugated sample, among which 114 proteins were overlapping.
26853435	4	53	theme	bioorthogonal	608:620	arg1	handle					631:636	a bioorthogonal chemical handle	606:636	a bioorthogonal chemical handle	606:636	Here, using peracetylated N-azidoacetylglucosamine (Ac4 GlcNAz) as a bioorthogonal chemical handle, we described a gel-based mass spectrometry method for the identification of proteins with O-GlcNAc modification in A549 cells.
26853435	4	53	theme	bioorthogonal	608:620	arg1	N-azidoacetylglucosamine					565:588	peracetylated N-azidoacetylglucosamine	551:588	peracetylated N-azidoacetylglucosamine (Ac4 GlcNAz)	551:601	Here, using peracetylated N-azidoacetylglucosamine (Ac4 GlcNAz) as a bioorthogonal chemical handle, we described a gel-based mass spectrometry method for the identification of proteins with O-GlcNAc modification in A549 cells.
26853435	8	54	dep	proteins	1658:1665	arg1	dbOGAP					1676:1681	database dbOGAP	1667:1681	the O-GlcNAc modified proteins database dbOGAP (http://cbsb.lombardi.georgetown.edu/hulab/OGAP.html)	1636:1735	Interestingly, 74 proteins identified from Biotin-Diazo-Alkyne conjugates and 46 verified proteins from Biotin-DIBO-Alkyne conjugates could be found in the O-GlcNAc modified proteins database dbOGAP (http://cbsb.lombardi.georgetown.edu/hulab/OGAP.html).
26853435	11	55	theme	modified	2238:2245	arg1	proteins					2247:2254	other post-translationally modified proteins	2211:2254	other post-translationally modified proteins in proteomics	2211:2268	Together, the method we reported here combining metabolic labeling, click chemistry, affinity-based enrichment, SDS-PAGE separation, and mass spectrometry, would be adaptable for other post-translationally modified proteins in proteomics.
26853435	9	56	theme	higher	1852:1857	arg1	identification					1867:1880	higher protein identification	1852:1880	higher protein identification	1852:1880	These results suggested that CuAAC with Biotin-Diazo-Alkyne represented a more powerful method in proteomics with higher protein identification and better accuracy compared to SPAAC.
26853435	9	57	with	CuAAC	1767:1771	arg1	Biotin-Diazo-Alkyne					1778:1796	Biotin-Diazo-Alkyne	1778:1796	Biotin-Diazo-Alkyne	1778:1796	These results suggested that CuAAC with Biotin-Diazo-Alkyne represented a more powerful method in proteomics with higher protein identification and better accuracy compared to SPAAC.
26853435	3	58	from	challenge	514:522	arg1	proteomics					527:536	proteomics	527:536	proteomics	527:536	Despite its importance, identifying O-GlcNAcylated proteins is a major challenge in proteomics.
26853435	5	59	theme	reactions	868:876	arg1	modes					832:836	two modes	828:836	two modes of azide-alkyne bioorthogonal reactions in click chemistry: copper-catalyzed azide-alkyne cycloaddition (CuAAC) with Biotin-Diazo-Alkyne and stain-promoted azide-alkyne cycloaddition (SPAAC)	828:1027	In addition, we made a labeling efficiency comparison between two modes of azide-alkyne bioorthogonal reactions in click chemistry: copper-catalyzed azide-alkyne cycloaddition (CuAAC) with Biotin-Diazo-Alkyne and stain-promoted azide-alkyne cycloaddition (SPAAC) with Biotin-DIBO-Alkyne.
26853435	5	59	theme	reactions	868:876	arg1	cycloaddition					928:940	copper-catalyzed azide-alkyne cycloaddition	898:940	copper-catalyzed azide-alkyne cycloaddition (CuAAC) with Biotin-Diazo-Alkyne	898:973	In addition, we made a labeling efficiency comparison between two modes of azide-alkyne bioorthogonal reactions in click chemistry: copper-catalyzed azide-alkyne cycloaddition (CuAAC) with Biotin-Diazo-Alkyne and stain-promoted azide-alkyne cycloaddition (SPAAC) with Biotin-DIBO-Alkyne.
26853435	5	59	theme	reactions	868:876	arg1	cycloaddition					1007:1019	stain-promoted azide-alkyne cycloaddition	979:1019	stain-promoted azide-alkyne cycloaddition (SPAAC)	979:1027	In addition, we made a labeling efficiency comparison between two modes of azide-alkyne bioorthogonal reactions in click chemistry: copper-catalyzed azide-alkyne cycloaddition (CuAAC) with Biotin-Diazo-Alkyne and stain-promoted azide-alkyne cycloaddition (SPAAC) with Biotin-DIBO-Alkyne.
26853435	2	60	theme	various	308:314	arg1	sensing					352:358	nutrient sensing	343:358	nutrient sensing	343:358	It is involved in various cellular processes such as nutrient sensing, protein degradation, gene expression, and is associated with many human diseases.
26853435	2	60	theme	various	308:314	arg1	processes					325:333	various cellular processes	308:333	various cellular processes such as nutrient sensing, protein degradation, gene expression,	308:397	It is involved in various cellular processes such as nutrient sensing, protein degradation, gene expression, and is associated with many human diseases.
26853435	5	61	theme	click	881:885	arg1	chemistry					887:895	click chemistry	881:895	click chemistry	881:895	In addition, we made a labeling efficiency comparison between two modes of azide-alkyne bioorthogonal reactions in click chemistry: copper-catalyzed azide-alkyne cycloaddition (CuAAC) with Biotin-Diazo-Alkyne and stain-promoted azide-alkyne cycloaddition (SPAAC) with Biotin-DIBO-Alkyne.
26853435	9	62	theme	better	1886:1891	arg1	accuracy					1893:1900	better accuracy	1886:1900	better accuracy compared to SPAAC	1886:1918	These results suggested that CuAAC with Biotin-Diazo-Alkyne represented a more powerful method in proteomics with higher protein identification and better accuracy compared to SPAAC.
26853435	4	63	theme	mass	664:667	arg1	method					682:687	a gel-based mass spectrometry method	652:687	a gel-based mass spectrometry method for the identification of proteins with O-GlcNAc modification in A549 cells	652:763	Here, using peracetylated N-azidoacetylglucosamine (Ac4 GlcNAz) as a bioorthogonal chemical handle, we described a gel-based mass spectrometry method for the identification of proteins with O-GlcNAc modification in A549 cells.
26853435	7	64	with	proteins	1389:1396	arg1	Biotin-DIBO-Alkyne					1403:1420	Biotin-DIBO-Alkyne	1403:1420	Biotin-DIBO-Alkyne	1403:1420	Proteomics data analysis revealed that 229 putative O-GlcNAc modified proteins were identified with Biotin-Diazo-Alkyne conjugated sample and 188 proteins with Biotin-DIBO-Alkyne conjugated sample, among which 114 proteins were overlapping.
26853435	10	65	theme	molecular	1974:1982	arg1	function					1984:1991	the molecular function	1970:1991	the molecular function	1970:1991	The proteomics credibility was also confirmed by the molecular function and cell component gene ontology (GO).
26853435	5	66	with	comparison	809:818	arg1	Biotin-DIBO-Alkyne					1034:1051	Biotin-DIBO-Alkyne	1034:1051	Biotin-DIBO-Alkyne	1034:1051	In addition, we made a labeling efficiency comparison between two modes of azide-alkyne bioorthogonal reactions in click chemistry: copper-catalyzed azide-alkyne cycloaddition (CuAAC) with Biotin-Diazo-Alkyne and stain-promoted azide-alkyne cycloaddition (SPAAC) with Biotin-DIBO-Alkyne.
26853435	5	67	dep	modes	832:836	arg1	CuAAC					943:947	CuAAC	943:947	CuAAC	943:947	In addition, we made a labeling efficiency comparison between two modes of azide-alkyne bioorthogonal reactions in click chemistry: copper-catalyzed azide-alkyne cycloaddition (CuAAC) with Biotin-Diazo-Alkyne and stain-promoted azide-alkyne cycloaddition (SPAAC) with Biotin-DIBO-Alkyne.
26853435	5	67	dep	modes	832:836	arg1	modes					832:836	two modes	828:836	two modes of azide-alkyne bioorthogonal reactions in click chemistry: copper-catalyzed azide-alkyne cycloaddition (CuAAC) with Biotin-Diazo-Alkyne and stain-promoted azide-alkyne cycloaddition (SPAAC)	828:1027	In addition, we made a labeling efficiency comparison between two modes of azide-alkyne bioorthogonal reactions in click chemistry: copper-catalyzed azide-alkyne cycloaddition (CuAAC) with Biotin-Diazo-Alkyne and stain-promoted azide-alkyne cycloaddition (SPAAC) with Biotin-DIBO-Alkyne.
26853435	5	67	dep	modes	832:836	arg1	cycloaddition					928:940	copper-catalyzed azide-alkyne cycloaddition	898:940	copper-catalyzed azide-alkyne cycloaddition (CuAAC) with Biotin-Diazo-Alkyne	898:973	In addition, we made a labeling efficiency comparison between two modes of azide-alkyne bioorthogonal reactions in click chemistry: copper-catalyzed azide-alkyne cycloaddition (CuAAC) with Biotin-Diazo-Alkyne and stain-promoted azide-alkyne cycloaddition (SPAAC) with Biotin-DIBO-Alkyne.
26853435	5	67	dep	modes	832:836	arg1	SPAAC					1022:1026	SPAAC	1022:1026	SPAAC	1022:1026	In addition, we made a labeling efficiency comparison between two modes of azide-alkyne bioorthogonal reactions in click chemistry: copper-catalyzed azide-alkyne cycloaddition (CuAAC) with Biotin-Diazo-Alkyne and stain-promoted azide-alkyne cycloaddition (SPAAC) with Biotin-DIBO-Alkyne.
26853435	5	67	dep	modes	832:836	arg1	cycloaddition					1007:1019	stain-promoted azide-alkyne cycloaddition	979:1019	stain-promoted azide-alkyne cycloaddition (SPAAC)	979:1027	In addition, we made a labeling efficiency comparison between two modes of azide-alkyne bioorthogonal reactions in click chemistry: copper-catalyzed azide-alkyne cycloaddition (CuAAC) with Biotin-Diazo-Alkyne and stain-promoted azide-alkyne cycloaddition (SPAAC) with Biotin-DIBO-Alkyne.
26853435	1	68	from	modification	252:263	arg1	range					270:274	a range	268:274	a range of organisms	268:287	O-linked β-N-acetylglucosamine (O-GlcNAc) is emerging as an essential protein post-translational modification in a range of organisms.
26853435	5	69	theme	azide-alkyne	841:852	arg1	reactions					868:876	azide-alkyne bioorthogonal reactions	841:876	azide-alkyne bioorthogonal reactions in click chemistry	841:895	In addition, we made a labeling efficiency comparison between two modes of azide-alkyne bioorthogonal reactions in click chemistry: copper-catalyzed azide-alkyne cycloaddition (CuAAC) with Biotin-Diazo-Alkyne and stain-promoted azide-alkyne cycloaddition (SPAAC) with Biotin-DIBO-Alkyne.
26853435	6	70	with	conjugation	1060:1070	arg1	chemistry					1083:1091	click chemistry	1077:1091	click chemistry	1077:1091	After conjugation with click chemistry in vitro and enrichment via streptavidin resin, proteins with O-GlcNAc modification were separated by SDS-PAGE and identified with mass spectrometry.
26853435	5	71	with	cycloaddition	1007:1019	arg1	Biotin-Diazo-Alkyne					955:973	Biotin-Diazo-Alkyne	955:973	Biotin-Diazo-Alkyne	955:973	In addition, we made a labeling efficiency comparison between two modes of azide-alkyne bioorthogonal reactions in click chemistry: copper-catalyzed azide-alkyne cycloaddition (CuAAC) with Biotin-Diazo-Alkyne and stain-promoted azide-alkyne cycloaddition (SPAAC) with Biotin-DIBO-Alkyne.
26853435	0	72	theme	O-GlcNAc	134:141	arg1	proteomics					143:152	O-GlcNAc proteomics	134:152	O-GlcNAc proteomics	134:152	Comparative analysis of Cu (I)-catalyzed alkyne-azide cycloaddition (CuAAC) and strain-promoted alkyne-azide cycloaddition (SPAAC) in O-GlcNAc proteomics.
26853435	10	73	theme	component	2002:2010	arg1	ontology					2017:2024	cell component gene ontology	1997:2024	cell component gene ontology (GO)	1997:2029	The proteomics credibility was also confirmed by the molecular function and cell component gene ontology (GO).
26853435	10	74	theme	proteomics	1925:1934	arg1	credibility					1936:1946	The proteomics credibility	1921:1946	The proteomics credibility	1921:1946	The proteomics credibility was also confirmed by the molecular function and cell component gene ontology (GO).
26853435	11	75	theme	other	2211:2215	arg1	proteins					2247:2254	other post-translationally modified proteins	2211:2254	other post-translationally modified proteins in proteomics	2211:2268	Together, the method we reported here combining metabolic labeling, click chemistry, affinity-based enrichment, SDS-PAGE separation, and mass spectrometry, would be adaptable for other post-translationally modified proteins in proteomics.
26853435	8	76	from	conjugates	1607:1616	arg1	proteins					1502:1509	74 proteins	1499:1509	74 proteins identified from Biotin-Diazo-Alkyne conjugates	1499:1556	Interestingly, 74 proteins identified from Biotin-Diazo-Alkyne conjugates and 46 verified proteins from Biotin-DIBO-Alkyne conjugates could be found in the O-GlcNAc modified proteins database dbOGAP (http://cbsb.lombardi.georgetown.edu/hulab/OGAP.html).
26853435	8	76	from	conjugates	1607:1616	arg1	proteins					1574:1581	46 verified proteins	1562:1581	46 verified proteins	1562:1581	Interestingly, 74 proteins identified from Biotin-Diazo-Alkyne conjugates and 46 verified proteins from Biotin-DIBO-Alkyne conjugates could be found in the O-GlcNAc modified proteins database dbOGAP (http://cbsb.lombardi.georgetown.edu/hulab/OGAP.html).
26853435	5	77	from	chemistry	887:895	arg1	modes					832:836	two modes	828:836	two modes of azide-alkyne bioorthogonal reactions in click chemistry: copper-catalyzed azide-alkyne cycloaddition (CuAAC) with Biotin-Diazo-Alkyne and stain-promoted azide-alkyne cycloaddition (SPAAC)	828:1027	In addition, we made a labeling efficiency comparison between two modes of azide-alkyne bioorthogonal reactions in click chemistry: copper-catalyzed azide-alkyne cycloaddition (CuAAC) with Biotin-Diazo-Alkyne and stain-promoted azide-alkyne cycloaddition (SPAAC) with Biotin-DIBO-Alkyne.
26853435	5	77	from	chemistry	887:895	arg1	cycloaddition					928:940	copper-catalyzed azide-alkyne cycloaddition	898:940	copper-catalyzed azide-alkyne cycloaddition (CuAAC) with Biotin-Diazo-Alkyne	898:973	In addition, we made a labeling efficiency comparison between two modes of azide-alkyne bioorthogonal reactions in click chemistry: copper-catalyzed azide-alkyne cycloaddition (CuAAC) with Biotin-Diazo-Alkyne and stain-promoted azide-alkyne cycloaddition (SPAAC) with Biotin-DIBO-Alkyne.
26853435	5	77	from	chemistry	887:895	arg1	cycloaddition					1007:1019	stain-promoted azide-alkyne cycloaddition	979:1019	stain-promoted azide-alkyne cycloaddition (SPAAC)	979:1027	In addition, we made a labeling efficiency comparison between two modes of azide-alkyne bioorthogonal reactions in click chemistry: copper-catalyzed azide-alkyne cycloaddition (CuAAC) with Biotin-Diazo-Alkyne and stain-promoted azide-alkyne cycloaddition (SPAAC) with Biotin-DIBO-Alkyne.
26853435	8	78	theme	O-GlcNAc	1640:1647	arg1	proteins					1658:1665	the O-GlcNAc modified proteins database dbOGAP (http://cbsb.lombardi.georgetown.edu/hulab/OGAP.html)	1636:1735	the O-GlcNAc modified proteins database dbOGAP (http://cbsb.lombardi.georgetown.edu/hulab/OGAP.html)	1636:1735	Interestingly, 74 proteins identified from Biotin-Diazo-Alkyne conjugates and 46 verified proteins from Biotin-DIBO-Alkyne conjugates could be found in the O-GlcNAc modified proteins database dbOGAP (http://cbsb.lombardi.georgetown.edu/hulab/OGAP.html).
26853435	7	79	theme	putative	1286:1293	arg1	proteins					1313:1320	229 putative O-GlcNAc modified proteins	1282:1320	229 putative O-GlcNAc modified proteins	1282:1320	Proteomics data analysis revealed that 229 putative O-GlcNAc modified proteins were identified with Biotin-Diazo-Alkyne conjugated sample and 188 proteins with Biotin-DIBO-Alkyne conjugated sample, among which 114 proteins were overlapping.
26853435	5	80	theme	azide-alkyne	915:926	arg1	CuAAC					943:947	CuAAC	943:947	CuAAC	943:947	In addition, we made a labeling efficiency comparison between two modes of azide-alkyne bioorthogonal reactions in click chemistry: copper-catalyzed azide-alkyne cycloaddition (CuAAC) with Biotin-Diazo-Alkyne and stain-promoted azide-alkyne cycloaddition (SPAAC) with Biotin-DIBO-Alkyne.
26853435	5	80	theme	azide-alkyne	915:926	arg1	modes					832:836	two modes	828:836	two modes of azide-alkyne bioorthogonal reactions in click chemistry: copper-catalyzed azide-alkyne cycloaddition (CuAAC) with Biotin-Diazo-Alkyne and stain-promoted azide-alkyne cycloaddition (SPAAC)	828:1027	In addition, we made a labeling efficiency comparison between two modes of azide-alkyne bioorthogonal reactions in click chemistry: copper-catalyzed azide-alkyne cycloaddition (CuAAC) with Biotin-Diazo-Alkyne and stain-promoted azide-alkyne cycloaddition (SPAAC) with Biotin-DIBO-Alkyne.
26853435	5	80	theme	azide-alkyne	915:926	arg1	cycloaddition					928:940	copper-catalyzed azide-alkyne cycloaddition	898:940	copper-catalyzed azide-alkyne cycloaddition (CuAAC) with Biotin-Diazo-Alkyne	898:973	In addition, we made a labeling efficiency comparison between two modes of azide-alkyne bioorthogonal reactions in click chemistry: copper-catalyzed azide-alkyne cycloaddition (CuAAC) with Biotin-Diazo-Alkyne and stain-promoted azide-alkyne cycloaddition (SPAAC) with Biotin-DIBO-Alkyne.
26853435	0	81	from	analysis	12:19	arg1	proteomics					143:152	O-GlcNAc proteomics	134:152	O-GlcNAc proteomics	134:152	Comparative analysis of Cu (I)-catalyzed alkyne-azide cycloaddition (CuAAC) and strain-promoted alkyne-azide cycloaddition (SPAAC) in O-GlcNAc proteomics.
26853435	5	82	with	cycloaddition	928:940	arg1	Biotin-Diazo-Alkyne					955:973	Biotin-Diazo-Alkyne	955:973	Biotin-Diazo-Alkyne	955:973	In addition, we made a labeling efficiency comparison between two modes of azide-alkyne bioorthogonal reactions in click chemistry: copper-catalyzed azide-alkyne cycloaddition (CuAAC) with Biotin-Diazo-Alkyne and stain-promoted azide-alkyne cycloaddition (SPAAC) with Biotin-DIBO-Alkyne.
26853435	9	83	from	accuracy	1893:1900	arg1	proteomics					1836:1845	proteomics	1836:1845	proteomics with higher protein identification	1836:1880	These results suggested that CuAAC with Biotin-Diazo-Alkyne represented a more powerful method in proteomics with higher protein identification and better accuracy compared to SPAAC.
26853435	0	84	theme	alkyne-azide	96:107	arg1	SPAAC					124:128	SPAAC	124:128	SPAAC	124:128	Comparative analysis of Cu (I)-catalyzed alkyne-azide cycloaddition (CuAAC) and strain-promoted alkyne-azide cycloaddition (SPAAC) in O-GlcNAc proteomics.
26853435	0	84	theme	alkyne-azide	96:107	arg1	cycloaddition					109:121	strain-promoted alkyne-azide cycloaddition	80:121	strain-promoted alkyne-azide cycloaddition (SPAAC)	80:129	Comparative analysis of Cu (I)-catalyzed alkyne-azide cycloaddition (CuAAC) and strain-promoted alkyne-azide cycloaddition (SPAAC) in O-GlcNAc proteomics.
26853435	9	85	from	method	1826:1831	arg1	proteomics					1836:1845	proteomics	1836:1845	proteomics with higher protein identification	1836:1880	These results suggested that CuAAC with Biotin-Diazo-Alkyne represented a more powerful method in proteomics with higher protein identification and better accuracy compared to SPAAC.
26853435	2	86	theme	gene	382:385	arg1	sensing					352:358	nutrient sensing	343:358	nutrient sensing	343:358	It is involved in various cellular processes such as nutrient sensing, protein degradation, gene expression, and is associated with many human diseases.
26853435	2	86	theme	gene	382:385	arg1	expression					387:396	gene expression	382:396	gene expression	382:396	It is involved in various cellular processes such as nutrient sensing, protein degradation, gene expression, and is associated with many human diseases.
26853435	5	87	theme	efficiency	798:807	arg1	comparison					809:818	a labeling efficiency comparison	787:818	a labeling efficiency comparison between two modes of azide-alkyne bioorthogonal reactions in click chemistry: copper-catalyzed azide-alkyne cycloaddition (CuAAC) with Biotin-Diazo-Alkyne and stain-promoted azide-alkyne cycloaddition (SPAAC) with Biotin-DIBO-Alkyne	787:1051	In addition, we made a labeling efficiency comparison between two modes of azide-alkyne bioorthogonal reactions in click chemistry: copper-catalyzed azide-alkyne cycloaddition (CuAAC) with Biotin-Diazo-Alkyne and stain-promoted azide-alkyne cycloaddition (SPAAC) with Biotin-DIBO-Alkyne.
26853435	6	88	theme	streptavidin	1121:1132	arg1	resin					1134:1138	streptavidin resin	1121:1138	streptavidin resin	1121:1138	After conjugation with click chemistry in vitro and enrichment via streptavidin resin, proteins with O-GlcNAc modification were separated by SDS-PAGE and identified with mass spectrometry.
26853435	2	89	theme	human	427:431	arg1	diseases					433:440	many human diseases	422:440	many human diseases	422:440	It is involved in various cellular processes such as nutrient sensing, protein degradation, gene expression, and is associated with many human diseases.
26853435	1	90	theme	organisms	279:287	arg1	range					270:274	a range	268:274	a range of organisms	268:287	O-linked β-N-acetylglucosamine (O-GlcNAc) is emerging as an essential protein post-translational modification in a range of organisms.
26853435	4	91	from	modification	738:749	arg1	cells					759:763	A549 cells	754:763	A549 cells	754:763	Here, using peracetylated N-azidoacetylglucosamine (Ac4 GlcNAz) as a bioorthogonal chemical handle, we described a gel-based mass spectrometry method for the identification of proteins with O-GlcNAc modification in A549 cells.
26853435	5	92	theme	stain-promoted	979:992	arg1	modes					832:836	two modes	828:836	two modes of azide-alkyne bioorthogonal reactions in click chemistry: copper-catalyzed azide-alkyne cycloaddition (CuAAC) with Biotin-Diazo-Alkyne and stain-promoted azide-alkyne cycloaddition (SPAAC)	828:1027	In addition, we made a labeling efficiency comparison between two modes of azide-alkyne bioorthogonal reactions in click chemistry: copper-catalyzed azide-alkyne cycloaddition (CuAAC) with Biotin-Diazo-Alkyne and stain-promoted azide-alkyne cycloaddition (SPAAC) with Biotin-DIBO-Alkyne.
26853435	5	92	theme	stain-promoted	979:992	arg1	SPAAC					1022:1026	SPAAC	1022:1026	SPAAC	1022:1026	In addition, we made a labeling efficiency comparison between two modes of azide-alkyne bioorthogonal reactions in click chemistry: copper-catalyzed azide-alkyne cycloaddition (CuAAC) with Biotin-Diazo-Alkyne and stain-promoted azide-alkyne cycloaddition (SPAAC) with Biotin-DIBO-Alkyne.
26853435	5	92	theme	stain-promoted	979:992	arg1	cycloaddition					1007:1019	stain-promoted azide-alkyne cycloaddition	979:1019	stain-promoted azide-alkyne cycloaddition (SPAAC)	979:1027	In addition, we made a labeling efficiency comparison between two modes of azide-alkyne bioorthogonal reactions in click chemistry: copper-catalyzed azide-alkyne cycloaddition (CuAAC) with Biotin-Diazo-Alkyne and stain-promoted azide-alkyne cycloaddition (SPAAC) with Biotin-DIBO-Alkyne.
26853435	4	93	theme	A549	754:757	arg1	cells					759:763	A549 cells	754:763	A549 cells	754:763	Here, using peracetylated N-azidoacetylglucosamine (Ac4 GlcNAz) as a bioorthogonal chemical handle, we described a gel-based mass spectrometry method for the identification of proteins with O-GlcNAc modification in A549 cells.
26853435	2	94	theme	protein	361:367	arg1	sensing					352:358	nutrient sensing	343:358	nutrient sensing	343:358	It is involved in various cellular processes such as nutrient sensing, protein degradation, gene expression, and is associated with many human diseases.
26853435	2	94	theme	protein	361:367	arg1	degradation					369:379	protein degradation	361:379	protein degradation	361:379	It is involved in various cellular processes such as nutrient sensing, protein degradation, gene expression, and is associated with many human diseases.
26853435	11	95	from	proteins	2247:2254	arg1	proteomics					2259:2268	proteomics	2259:2268	proteomics	2259:2268	Together, the method we reported here combining metabolic labeling, click chemistry, affinity-based enrichment, SDS-PAGE separation, and mass spectrometry, would be adaptable for other post-translationally modified proteins in proteomics.
26853435	1	96	theme	protein	225:231	arg1	modification					252:263	an essential protein post-translational modification	212:263	an essential protein post-translational modification in a range of organisms	212:287	O-linked β-N-acetylglucosamine (O-GlcNAc) is emerging as an essential protein post-translational modification in a range of organisms.
26853435	0	97	theme	-catalyzed	30:39	arg1	CuAAC					69:73	CuAAC	69:73	CuAAC	69:73	Comparative analysis of Cu (I)-catalyzed alkyne-azide cycloaddition (CuAAC) and strain-promoted alkyne-azide cycloaddition (SPAAC) in O-GlcNAc proteomics.
26853435	0	97	theme	-catalyzed	30:39	arg1	cycloaddition					54:66	Cu (I)-catalyzed alkyne-azide cycloaddition	24:66	Cu (I)-catalyzed alkyne-azide cycloaddition (CuAAC)	24:74	Comparative analysis of Cu (I)-catalyzed alkyne-azide cycloaddition (CuAAC) and strain-promoted alkyne-azide cycloaddition (SPAAC) in O-GlcNAc proteomics.
26853435	7	98	theme	conjugated	1363:1372	arg1	sample					1374:1379	Biotin-Diazo-Alkyne conjugated sample	1343:1379	Biotin-Diazo-Alkyne conjugated sample	1343:1379	Proteomics data analysis revealed that 229 putative O-GlcNAc modified proteins were identified with Biotin-Diazo-Alkyne conjugated sample and 188 proteins with Biotin-DIBO-Alkyne conjugated sample, among which 114 proteins were overlapping.
26853435	2	99	theme	cellular	316:323	arg1	sensing					352:358	nutrient sensing	343:358	nutrient sensing	343:358	It is involved in various cellular processes such as nutrient sensing, protein degradation, gene expression, and is associated with many human diseases.
26853435	2	99	theme	cellular	316:323	arg1	processes					325:333	various cellular processes	308:333	various cellular processes such as nutrient sensing, protein degradation, gene expression,	308:397	It is involved in various cellular processes such as nutrient sensing, protein degradation, gene expression, and is associated with many human diseases.
26853435	1	100	theme	essential	215:223	arg1	modification					252:263	an essential protein post-translational modification	212:263	an essential protein post-translational modification in a range of organisms	212:287	O-linked β-N-acetylglucosamine (O-GlcNAc) is emerging as an essential protein post-translational modification in a range of organisms.
26853435	9	101	theme	powerful	1817:1824	arg1	method					1826:1831	a more powerful method	1810:1831	a more powerful method in proteomics with higher protein identification	1810:1880	These results suggested that CuAAC with Biotin-Diazo-Alkyne represented a more powerful method in proteomics with higher protein identification and better accuracy compared to SPAAC.
26853435	11	102	theme	click	2100:2104	arg1	chemistry					2106:2114	click chemistry	2100:2114	click chemistry	2100:2114	Together, the method we reported here combining metabolic labeling, click chemistry, affinity-based enrichment, SDS-PAGE separation, and mass spectrometry, would be adaptable for other post-translationally modified proteins in proteomics.
26853435	4	103	theme	chemical	622:629	arg1	handle					631:636	a bioorthogonal chemical handle	606:636	a bioorthogonal chemical handle	606:636	Here, using peracetylated N-azidoacetylglucosamine (Ac4 GlcNAz) as a bioorthogonal chemical handle, we described a gel-based mass spectrometry method for the identification of proteins with O-GlcNAc modification in A549 cells.
26853435	4	103	theme	chemical	622:629	arg1	N-azidoacetylglucosamine					565:588	peracetylated N-azidoacetylglucosamine	551:588	peracetylated N-azidoacetylglucosamine (Ac4 GlcNAz)	551:601	Here, using peracetylated N-azidoacetylglucosamine (Ac4 GlcNAz) as a bioorthogonal chemical handle, we described a gel-based mass spectrometry method for the identification of proteins with O-GlcNAc modification in A549 cells.
26853435	7	104	theme	Proteomics	1243:1252	arg1	analysis					1259:1266	Proteomics data analysis	1243:1266	Proteomics data analysis	1243:1266	Proteomics data analysis revealed that 229 putative O-GlcNAc modified proteins were identified with Biotin-Diazo-Alkyne conjugated sample and 188 proteins with Biotin-DIBO-Alkyne conjugated sample, among which 114 proteins were overlapping.
26853435	1	105	theme	post-translational	233:250	arg1	modification					252:263	an essential protein post-translational modification	212:263	an essential protein post-translational modification in a range of organisms	212:287	O-linked β-N-acetylglucosamine (O-GlcNAc) is emerging as an essential protein post-translational modification in a range of organisms.
32870666	2	0	theme	central	376:382	arg1	regulator					384:392	a central regulator	374:392	a central regulator of both cell physiology and human health	374:433	This modification, known as O-GlcNAc, has emerged as a central regulator of both cell physiology and human health.
32870666	1	1	contain	have	197:200	arg2	residues					251:258	specific serine and threonine residues	221:258	specific serine and threonine residues modified by the monosaccharide N-acetylglucosamine (GlcNAc)	221:318	Hundreds of nuclear, cytoplasmic, and mitochondrial proteins within multicellular eukaryotes have hydroxyl groups of specific serine and threonine residues modified by the monosaccharide N-acetylglucosamine (GlcNAc).
32870666	1	1	contain	have	197:200	arg1	Hundreds					104:111	Hundreds	104:111	Hundreds of nuclear, cytoplasmic, and mitochondrial proteins within multicellular eukaryotes	104:195	Hundreds of nuclear, cytoplasmic, and mitochondrial proteins within multicellular eukaryotes have hydroxyl groups of specific serine and threonine residues modified by the monosaccharide N-acetylglucosamine (GlcNAc).
32870666	1	1	contain	have	197:200	arg2	groups					211:216	hydroxyl groups	202:216	hydroxyl groups of specific serine and threonine residues modified by the monosaccharide N-acetylglucosamine (GlcNAc)	202:318	Hundreds of nuclear, cytoplasmic, and mitochondrial proteins within multicellular eukaryotes have hydroxyl groups of specific serine and threonine residues modified by the monosaccharide N-acetylglucosamine (GlcNAc).
32870666	6	2	theme	robust	1288:1293	arg1	labeling					1295:1302	their robust labeling	1282:1302	their robust labeling	1282:1302	Using various combinations of sequential chemoselective ligation strategies, we go on to tag these analytes with a series of labels, allowing us to define conditions that enable their robust labeling.
32870666	2	3	theme	physiology	407:416	arg1	regulator					384:392	a central regulator	374:392	a central regulator of both cell physiology and human health	374:433	This modification, known as O-GlcNAc, has emerged as a central regulator of both cell physiology and human health.
32870666	4	4	theme	nascent	702:708	arg1	chains					722:727	such nascent polypeptide chains	697:727	such nascent polypeptide chains	697:727	We previously showed, using overexpressed model proteins, that O-GlcNAc modification can occur cotranslationally and that this process prevents premature degradation of such nascent polypeptide chains.
32870666	5	5	theme	nascent	923:929	arg1	chains					931:936	nascent chains	923:936	nascent chains that are cotranslationally glycosylated with O-GlcNAc by metabolic saccharide engineering using tetra-O-acetyl-2-N-azidoacetyl-2-deoxy-d-galactopyranose (Ac4GalNAz)	923:1101	Here, we use tandem metabolic engineering strategies to label endogenously occurring nascent polypeptide chains within cells using O-propargyl-puromycin (OPP) and target the specific subset of nascent chains that are cotranslationally glycosylated with O-GlcNAc by metabolic saccharide engineering using tetra-O-acetyl-2-N-azidoacetyl-2-deoxy-d-galactopyranose (Ac4GalNAz).
32870666	4	6	theme	chains	722:727	arg1	degradation					682:692	premature degradation	672:692	premature degradation of such nascent polypeptide chains	672:727	We previously showed, using overexpressed model proteins, that O-GlcNAc modification can occur cotranslationally and that this process prevents premature degradation of such nascent polypeptide chains.
32870666	1	7	theme	specific	221:228	arg1	residues					251:258	specific serine and threonine residues	221:258	specific serine and threonine residues modified by the monosaccharide N-acetylglucosamine (GlcNAc)	221:318	Hundreds of nuclear, cytoplasmic, and mitochondrial proteins within multicellular eukaryotes have hydroxyl groups of specific serine and threonine residues modified by the monosaccharide N-acetylglucosamine (GlcNAc).
32870666	4	8	theme	premature	672:680	arg1	degradation					682:692	premature degradation	672:692	premature degradation of such nascent polypeptide chains	672:727	We previously showed, using overexpressed model proteins, that O-GlcNAc modification can occur cotranslationally and that this process prevents premature degradation of such nascent polypeptide chains.
32870666	5	9	theme	tandem	743:748	arg1	strategies					772:781	tandem metabolic engineering strategies	743:781	tandem metabolic engineering strategies	743:781	Here, we use tandem metabolic engineering strategies to label endogenously occurring nascent polypeptide chains within cells using O-propargyl-puromycin (OPP) and target the specific subset of nascent chains that are cotranslationally glycosylated with O-GlcNAc by metabolic saccharide engineering using tetra-O-acetyl-2-N-azidoacetyl-2-deoxy-d-galactopyranose (Ac4GalNAz).
32870666	10	10	theme	cotranslational	1890:1904	arg1	modifications					1914:1926	other cotranslational protein modifications	1884:1926	other cotranslational protein modifications	1884:1926	Moreover, this work opens the way to studies directed at understanding the roles of O-GlcNAc and other cotranslational protein modifications and should stimulate an improved understanding of the role of O-GlcNAc in cytoplasmic protein quality control and proteostasis.
32870666	10	11	mod	modifications	1914:1926	arg1	O-GlcNAc					1871:1878	O-GlcNAc	1871:1878	O-GlcNAc	1871:1878	Moreover, this work opens the way to studies directed at understanding the roles of O-GlcNAc and other cotranslational protein modifications and should stimulate an improved understanding of the role of O-GlcNAc in cytoplasmic protein quality control and proteostasis.
32870666	10	11	mod	modifications	1914:1926	arg3	protein					1906:1912	other cotranslational protein modifications	1884:1926	other cotranslational protein modifications	1884:1926	Moreover, this work opens the way to studies directed at understanding the roles of O-GlcNAc and other cotranslational protein modifications and should stimulate an improved understanding of the role of O-GlcNAc in cytoplasmic protein quality control and proteostasis.
32870666	5	12	theme	engineering	760:770	arg1	strategies					772:781	tandem metabolic engineering strategies	743:781	tandem metabolic engineering strategies	743:781	Here, we use tandem metabolic engineering strategies to label endogenously occurring nascent polypeptide chains within cells using O-propargyl-puromycin (OPP) and target the specific subset of nascent chains that are cotranslationally glycosylated with O-GlcNAc by metabolic saccharide engineering using tetra-O-acetyl-2-N-azidoacetyl-2-deoxy-d-galactopyranose (Ac4GalNAz).
32870666	1	13	theme	residues	251:258	arg1	groups					211:216	hydroxyl groups	202:216	hydroxyl groups of specific serine and threonine residues modified by the monosaccharide N-acetylglucosamine (GlcNAc)	202:318	Hundreds of nuclear, cytoplasmic, and mitochondrial proteins within multicellular eukaryotes have hydroxyl groups of specific serine and threonine residues modified by the monosaccharide N-acetylglucosamine (GlcNAc).
32870666	1	13	theme	residues	251:258	arg1	residues					251:258	specific serine and threonine residues	221:258	specific serine and threonine residues modified by the monosaccharide N-acetylglucosamine (GlcNAc)	221:318	Hundreds of nuclear, cytoplasmic, and mitochondrial proteins within multicellular eukaryotes have hydroxyl groups of specific serine and threonine residues modified by the monosaccharide N-acetylglucosamine (GlcNAc).
32870666	8	14	theme	cotranslational	1594:1608	arg1	O-GlcNAcylation					1610:1624	their cotranslational O-GlcNAcylation	1588:1624	their cotranslational O-GlcNAcylation	1588:1624	Using alternative targeted methods, we examine three of these identified proteins and further validate their cotranslational O-GlcNAcylation.
32870666	5	15	theme	saccharide	1005:1014	arg1	engineering					1016:1026	metabolic saccharide engineering	995:1026	metabolic saccharide engineering using tetra-O-acetyl-2-N-azidoacetyl-2-deoxy-d-galactopyranose (Ac4GalNAz)	995:1101	Here, we use tandem metabolic engineering strategies to label endogenously occurring nascent polypeptide chains within cells using O-propargyl-puromycin (OPP) and target the specific subset of nascent chains that are cotranslationally glycosylated with O-GlcNAc by metabolic saccharide engineering using tetra-O-acetyl-2-N-azidoacetyl-2-deoxy-d-galactopyranose (Ac4GalNAz).
32870666	6	16	theme	strategies	1169:1178	arg1	combinations					1118:1129	various combinations	1110:1129	various combinations of sequential chemoselective ligation strategies	1110:1178	Using various combinations of sequential chemoselective ligation strategies, we go on to tag these analytes with a series of labels, allowing us to define conditions that enable their robust labeling.
32870666	7	17	theme	proteins	1475:1482	arg1	set					1421:1423	a set	1419:1423	a set of endogenous cotranslationally O-GlcNAc modified proteins	1419:1482	Two-step enrichment of these glycosylated nascent chains, combined with shotgun proteomics, allows us to identify a set of endogenous cotranslationally O-GlcNAc modified proteins.
32870666	7	17	theme	proteins	1475:1482	arg1	proteins					1475:1482	endogenous cotranslationally O-GlcNAc modified proteins	1428:1482	endogenous cotranslationally O-GlcNAc modified proteins	1428:1482	Two-step enrichment of these glycosylated nascent chains, combined with shotgun proteomics, allows us to identify a set of endogenous cotranslationally O-GlcNAc modified proteins.
32870666	5	18	theme	nascent	815:821	arg1	chains					835:840	endogenously occurring nascent polypeptide chains	792:840	endogenously occurring nascent polypeptide chains within cells using O-propargyl-puromycin (OPP)	792:887	Here, we use tandem metabolic engineering strategies to label endogenously occurring nascent polypeptide chains within cells using O-propargyl-puromycin (OPP) and target the specific subset of nascent chains that are cotranslationally glycosylated with O-GlcNAc by metabolic saccharide engineering using tetra-O-acetyl-2-N-azidoacetyl-2-deoxy-d-galactopyranose (Ac4GalNAz).
32870666	10	19	theme	protein	2014:2020	arg1	control					2030:2036	cytoplasmic protein quality control	2002:2036	cytoplasmic protein quality control	2002:2036	Moreover, this work opens the way to studies directed at understanding the roles of O-GlcNAc and other cotranslational protein modifications and should stimulate an improved understanding of the role of O-GlcNAc in cytoplasmic protein quality control and proteostasis.
32870666	1	20	theme	multicellular	172:184	arg1	eukaryotes					186:195	multicellular eukaryotes	172:195	multicellular eukaryotes	172:195	Hundreds of nuclear, cytoplasmic, and mitochondrial proteins within multicellular eukaryotes have hydroxyl groups of specific serine and threonine residues modified by the monosaccharide N-acetylglucosamine (GlcNAc).
32870666	6	21	theme	chemoselective	1145:1158	arg1	strategies					1169:1178	sequential chemoselective ligation strategies	1134:1178	sequential chemoselective ligation strategies	1134:1178	Using various combinations of sequential chemoselective ligation strategies, we go on to tag these analytes with a series of labels, allowing us to define conditions that enable their robust labeling.
32870666	7	22	theme	nascent	1347:1353	arg1	chains					1355:1360	these glycosylated nascent chains	1328:1360	these glycosylated nascent chains	1328:1360	Two-step enrichment of these glycosylated nascent chains, combined with shotgun proteomics, allows us to identify a set of endogenous cotranslationally O-GlcNAc modified proteins.
32870666	10	23	from	role	1982:1985	arg1	proteostasis					2042:2053	proteostasis	2042:2053	proteostasis	2042:2053	Moreover, this work opens the way to studies directed at understanding the roles of O-GlcNAc and other cotranslational protein modifications and should stimulate an improved understanding of the role of O-GlcNAc in cytoplasmic protein quality control and proteostasis.
32870666	10	23	from	role	1982:1985	arg1	control					2030:2036	cytoplasmic protein quality control	2002:2036	cytoplasmic protein quality control	2002:2036	Moreover, this work opens the way to studies directed at understanding the roles of O-GlcNAc and other cotranslational protein modifications and should stimulate an improved understanding of the role of O-GlcNAc in cytoplasmic protein quality control and proteostasis.
32870666	1	24	theme	cytoplasmic	125:135	arg1	proteins					156:163	nuclear, cytoplasmic, and mitochondrial proteins	116:163	nuclear, cytoplasmic, and mitochondrial proteins within multicellular eukaryotes	116:195	Hundreds of nuclear, cytoplasmic, and mitochondrial proteins within multicellular eukaryotes have hydroxyl groups of specific serine and threonine residues modified by the monosaccharide N-acetylglucosamine (GlcNAc).
32870666	9	25	theme	abundance	1716:1724	arg1	analytes					1737:1744	extremely low abundance endogenous analytes	1702:1744	extremely low abundance endogenous analytes present within complex protein mixtures	1702:1784	These findings detail strategies to enable isolation and identification of extremely low abundance endogenous analytes present within complex protein mixtures.
32870666	6	26	theme	various	1110:1116	arg1	combinations					1118:1129	various combinations	1110:1129	various combinations of sequential chemoselective ligation strategies	1110:1178	Using various combinations of sequential chemoselective ligation strategies, we go on to tag these analytes with a series of labels, allowing us to define conditions that enable their robust labeling.
32870666	8	27	theme	alternative	1491:1501	arg1	methods					1512:1518	alternative targeted methods	1491:1518	alternative targeted methods	1491:1518	Using alternative targeted methods, we examine three of these identified proteins and further validate their cotranslational O-GlcNAcylation.
32870666	2	28	theme	human	422:426	arg1	health					428:433	human health	422:433	human health	422:433	This modification, known as O-GlcNAc, has emerged as a central regulator of both cell physiology and human health.
32870666	9	29	theme	analytes	1737:1744	arg1	identification					1684:1697	identification	1684:1697	identification	1684:1697	These findings detail strategies to enable isolation and identification of extremely low abundance endogenous analytes present within complex protein mixtures.
32870666	9	29	theme	analytes	1737:1744	arg1	isolation					1670:1678	isolation	1670:1678	isolation	1670:1678	These findings detail strategies to enable isolation and identification of extremely low abundance endogenous analytes present within complex protein mixtures.
32870666	7	30	theme	modified	1466:1473	arg1	proteins					1475:1482	endogenous cotranslationally O-GlcNAc modified proteins	1428:1482	endogenous cotranslationally O-GlcNAc modified proteins	1428:1482	Two-step enrichment of these glycosylated nascent chains, combined with shotgun proteomics, allows us to identify a set of endogenous cotranslationally O-GlcNAc modified proteins.
32870666	1	31	theme	proteins	156:163	arg1	Hundreds					104:111	Hundreds	104:111	Hundreds of nuclear, cytoplasmic, and mitochondrial proteins within multicellular eukaryotes	104:195	Hundreds of nuclear, cytoplasmic, and mitochondrial proteins within multicellular eukaryotes have hydroxyl groups of specific serine and threonine residues modified by the monosaccharide N-acetylglucosamine (GlcNAc).
32870666	5	32	theme	occurring	805:813	arg1	chains					835:840	endogenously occurring nascent polypeptide chains	792:840	endogenously occurring nascent polypeptide chains within cells using O-propargyl-puromycin (OPP)	792:887	Here, we use tandem metabolic engineering strategies to label endogenously occurring nascent polypeptide chains within cells using O-propargyl-puromycin (OPP) and target the specific subset of nascent chains that are cotranslationally glycosylated with O-GlcNAc by metabolic saccharide engineering using tetra-O-acetyl-2-N-azidoacetyl-2-deoxy-d-galactopyranose (Ac4GalNAz).
32870666	3	33	theme	emerging	442:449	arg1	function					451:458	A key emerging function	436:458	A key emerging function of O-GlcNAc	436:470	A key emerging function of O-GlcNAc appears to be to regulate cellular protein homeostasis.
32870666	0	34	theme	Tandem	0:5	arg1	Labeling					21:28	Tandem Bioorthogonal Labeling	0:28	Tandem Bioorthogonal Labeling	0:28	Tandem Bioorthogonal Labeling Uncovers Endogenous Cotranslationally O-GlcNAc Modified Nascent Proteins.
32870666	1	35	theme	nuclear	116:122	arg1	proteins					156:163	nuclear, cytoplasmic, and mitochondrial proteins	116:163	nuclear, cytoplasmic, and mitochondrial proteins within multicellular eukaryotes	116:195	Hundreds of nuclear, cytoplasmic, and mitochondrial proteins within multicellular eukaryotes have hydroxyl groups of specific serine and threonine residues modified by the monosaccharide N-acetylglucosamine (GlcNAc).
32870666	6	36	with	tag	1193:1195	arg1	series					1219:1224	a series	1217:1224	a series of labels	1217:1234	Using various combinations of sequential chemoselective ligation strategies, we go on to tag these analytes with a series of labels, allowing us to define conditions that enable their robust labeling.
32870666	9	37	theme	protein	1769:1775	arg1	mixtures					1777:1784	complex protein mixtures	1761:1784	complex protein mixtures	1761:1784	These findings detail strategies to enable isolation and identification of extremely low abundance endogenous analytes present within complex protein mixtures.
32870666	0	38	theme	Endogenous	39:48	arg1	Proteins					94:101	Endogenous Cotranslationally O-GlcNAc Modified Nascent Proteins	39:101	Endogenous Cotranslationally O-GlcNAc Modified Nascent Proteins	39:101	Tandem Bioorthogonal Labeling Uncovers Endogenous Cotranslationally O-GlcNAc Modified Nascent Proteins.
32870666	0	39	theme	Nascent	86:92	arg1	Proteins					94:101	Endogenous Cotranslationally O-GlcNAc Modified Nascent Proteins	39:101	Endogenous Cotranslationally O-GlcNAc Modified Nascent Proteins	39:101	Tandem Bioorthogonal Labeling Uncovers Endogenous Cotranslationally O-GlcNAc Modified Nascent Proteins.
32870666	3	40	theme	protein	507:513	arg1	homeostasis					515:525	cellular protein homeostasis	498:525	cellular protein homeostasis	498:525	A key emerging function of O-GlcNAc appears to be to regulate cellular protein homeostasis.
32870666	0	41	theme	O-GlcNAc	68:75	arg1	Proteins					94:101	Endogenous Cotranslationally O-GlcNAc Modified Nascent Proteins	39:101	Endogenous Cotranslationally O-GlcNAc Modified Nascent Proteins	39:101	Tandem Bioorthogonal Labeling Uncovers Endogenous Cotranslationally O-GlcNAc Modified Nascent Proteins.
32870666	4	42	theme	overexpressed	556:568	arg1	proteins					576:583	overexpressed model proteins	556:583	overexpressed model proteins	556:583	We previously showed, using overexpressed model proteins, that O-GlcNAc modification can occur cotranslationally and that this process prevents premature degradation of such nascent polypeptide chains.
32870666	8	43	theme	proteins	1558:1565	arg1	proteins					1558:1565	these identified proteins	1541:1565	these identified proteins	1541:1565	Using alternative targeted methods, we examine three of these identified proteins and further validate their cotranslational O-GlcNAcylation.
32870666	8	43	theme	proteins	1558:1565	arg1	three					1532:1536	three	1532:1536	three	1532:1536	Using alternative targeted methods, we examine three of these identified proteins and further validate their cotranslational O-GlcNAcylation.
32870666	10	44	theme	O-GlcNAc	1871:1878	arg1	modifications					1914:1926	other cotranslational protein modifications	1884:1926	other cotranslational protein modifications	1884:1926	Moreover, this work opens the way to studies directed at understanding the roles of O-GlcNAc and other cotranslational protein modifications and should stimulate an improved understanding of the role of O-GlcNAc in cytoplasmic protein quality control and proteostasis.
32870666	10	44	theme	O-GlcNAc	1871:1878	arg1	roles					1862:1866	the roles	1858:1866	the roles of O-GlcNAc	1858:1878	Moreover, this work opens the way to studies directed at understanding the roles of O-GlcNAc and other cotranslational protein modifications and should stimulate an improved understanding of the role of O-GlcNAc in cytoplasmic protein quality control and proteostasis.
32870666	10	45	from	proteostasis	2042:2053	arg1	understanding					1961:1973	an improved understanding	1949:1973	an improved understanding of the role of O-GlcNAc in cytoplasmic protein quality control and proteostasis	1949:2053	Moreover, this work opens the way to studies directed at understanding the roles of O-GlcNAc and other cotranslational protein modifications and should stimulate an improved understanding of the role of O-GlcNAc in cytoplasmic protein quality control and proteostasis.
32870666	7	46	theme	glycosylated	1334:1345	arg1	chains					1355:1360	these glycosylated nascent chains	1328:1360	these glycosylated nascent chains	1328:1360	Two-step enrichment of these glycosylated nascent chains, combined with shotgun proteomics, allows us to identify a set of endogenous cotranslationally O-GlcNAc modified proteins.
32870666	10	47	theme	protein	1906:1912	arg1	modifications					1914:1926	other cotranslational protein modifications	1884:1926	other cotranslational protein modifications	1884:1926	Moreover, this work opens the way to studies directed at understanding the roles of O-GlcNAc and other cotranslational protein modifications and should stimulate an improved understanding of the role of O-GlcNAc in cytoplasmic protein quality control and proteostasis.
32870666	10	48	theme	improved	1952:1959	arg1	understanding					1961:1973	an improved understanding	1949:1973	an improved understanding of the role of O-GlcNAc in cytoplasmic protein quality control and proteostasis	1949:2053	Moreover, this work opens the way to studies directed at understanding the roles of O-GlcNAc and other cotranslational protein modifications and should stimulate an improved understanding of the role of O-GlcNAc in cytoplasmic protein quality control and proteostasis.
32870666	10	49	theme	other	1884:1888	arg1	modifications					1914:1926	other cotranslational protein modifications	1884:1926	other cotranslational protein modifications	1884:1926	Moreover, this work opens the way to studies directed at understanding the roles of O-GlcNAc and other cotranslational protein modifications and should stimulate an improved understanding of the role of O-GlcNAc in cytoplasmic protein quality control and proteostasis.
32870666	1	50	theme	hydroxyl	202:209	arg1	groups					211:216	hydroxyl groups	202:216	hydroxyl groups of specific serine and threonine residues modified by the monosaccharide N-acetylglucosamine (GlcNAc)	202:318	Hundreds of nuclear, cytoplasmic, and mitochondrial proteins within multicellular eukaryotes have hydroxyl groups of specific serine and threonine residues modified by the monosaccharide N-acetylglucosamine (GlcNAc).
32870666	1	50	theme	hydroxyl	202:209	arg1	residues					251:258	specific serine and threonine residues	221:258	specific serine and threonine residues modified by the monosaccharide N-acetylglucosamine (GlcNAc)	221:318	Hundreds of nuclear, cytoplasmic, and mitochondrial proteins within multicellular eukaryotes have hydroxyl groups of specific serine and threonine residues modified by the monosaccharide N-acetylglucosamine (GlcNAc).
32870666	4	51	theme	such	697:700	arg1	chains					722:727	such nascent polypeptide chains	697:727	such nascent polypeptide chains	697:727	We previously showed, using overexpressed model proteins, that O-GlcNAc modification can occur cotranslationally and that this process prevents premature degradation of such nascent polypeptide chains.
32870666	10	52	theme	role	1982:1985	arg1	understanding					1961:1973	an improved understanding	1949:1973	an improved understanding of the role of O-GlcNAc in cytoplasmic protein quality control and proteostasis	1949:2053	Moreover, this work opens the way to studies directed at understanding the roles of O-GlcNAc and other cotranslational protein modifications and should stimulate an improved understanding of the role of O-GlcNAc in cytoplasmic protein quality control and proteostasis.
32870666	5	53	theme	chains	931:936	arg1	subset					913:918	the specific subset	900:918	the specific subset of nascent chains that are cotranslationally glycosylated with O-GlcNAc by metabolic saccharide engineering using tetra-O-acetyl-2-N-azidoacetyl-2-deoxy-d-galactopyranose (Ac4GalNAz)	900:1101	Here, we use tandem metabolic engineering strategies to label endogenously occurring nascent polypeptide chains within cells using O-propargyl-puromycin (OPP) and target the specific subset of nascent chains that are cotranslationally glycosylated with O-GlcNAc by metabolic saccharide engineering using tetra-O-acetyl-2-N-azidoacetyl-2-deoxy-d-galactopyranose (Ac4GalNAz).
32870666	4	54	theme	polypeptide	710:720	arg1	chains					722:727	such nascent polypeptide chains	697:727	such nascent polypeptide chains	697:727	We previously showed, using overexpressed model proteins, that O-GlcNAc modification can occur cotranslationally and that this process prevents premature degradation of such nascent polypeptide chains.
32870666	1	55	theme	serine	230:235	arg1	residues					251:258	specific serine and threonine residues	221:258	specific serine and threonine residues modified by the monosaccharide N-acetylglucosamine (GlcNAc)	221:318	Hundreds of nuclear, cytoplasmic, and mitochondrial proteins within multicellular eukaryotes have hydroxyl groups of specific serine and threonine residues modified by the monosaccharide N-acetylglucosamine (GlcNAc).
32870666	5	56	theme	metabolic	750:758	arg1	strategies					772:781	tandem metabolic engineering strategies	743:781	tandem metabolic engineering strategies	743:781	Here, we use tandem metabolic engineering strategies to label endogenously occurring nascent polypeptide chains within cells using O-propargyl-puromycin (OPP) and target the specific subset of nascent chains that are cotranslationally glycosylated with O-GlcNAc by metabolic saccharide engineering using tetra-O-acetyl-2-N-azidoacetyl-2-deoxy-d-galactopyranose (Ac4GalNAz).
32870666	10	57	theme	cytoplasmic	2002:2012	arg1	control					2030:2036	cytoplasmic protein quality control	2002:2036	cytoplasmic protein quality control	2002:2036	Moreover, this work opens the way to studies directed at understanding the roles of O-GlcNAc and other cotranslational protein modifications and should stimulate an improved understanding of the role of O-GlcNAc in cytoplasmic protein quality control and proteostasis.
32870666	5	58	theme	specific	904:911	arg1	subset					913:918	the specific subset	900:918	the specific subset of nascent chains that are cotranslationally glycosylated with O-GlcNAc by metabolic saccharide engineering using tetra-O-acetyl-2-N-azidoacetyl-2-deoxy-d-galactopyranose (Ac4GalNAz)	900:1101	Here, we use tandem metabolic engineering strategies to label endogenously occurring nascent polypeptide chains within cells using O-propargyl-puromycin (OPP) and target the specific subset of nascent chains that are cotranslationally glycosylated with O-GlcNAc by metabolic saccharide engineering using tetra-O-acetyl-2-N-azidoacetyl-2-deoxy-d-galactopyranose (Ac4GalNAz).
32870666	10	59	theme	O-GlcNAc	1990:1997	arg1	role					1982:1985	the role	1978:1985	the role of O-GlcNAc in cytoplasmic protein quality control and proteostasis	1978:2053	Moreover, this work opens the way to studies directed at understanding the roles of O-GlcNAc and other cotranslational protein modifications and should stimulate an improved understanding of the role of O-GlcNAc in cytoplasmic protein quality control and proteostasis.
32870666	1	60	theme	mitochondrial	142:154	arg1	proteins					156:163	nuclear, cytoplasmic, and mitochondrial proteins	116:163	nuclear, cytoplasmic, and mitochondrial proteins within multicellular eukaryotes	116:195	Hundreds of nuclear, cytoplasmic, and mitochondrial proteins within multicellular eukaryotes have hydroxyl groups of specific serine and threonine residues modified by the monosaccharide N-acetylglucosamine (GlcNAc).
32870666	5	61	gly	glycosylated	965:976	arg1	chains					931:936	nascent chains	923:936	nascent chains that are cotranslationally glycosylated with O-GlcNAc by metabolic saccharide engineering using tetra-O-acetyl-2-N-azidoacetyl-2-deoxy-d-galactopyranose (Ac4GalNAz)	923:1101	Here, we use tandem metabolic engineering strategies to label endogenously occurring nascent polypeptide chains within cells using O-propargyl-puromycin (OPP) and target the specific subset of nascent chains that are cotranslationally glycosylated with O-GlcNAc by metabolic saccharide engineering using tetra-O-acetyl-2-N-azidoacetyl-2-deoxy-d-galactopyranose (Ac4GalNAz).
32870666	7	62	theme	chains	1355:1360	arg1	enrichment					1314:1323	Two-step enrichment	1305:1323	Two-step enrichment	1305:1323	Two-step enrichment of these glycosylated nascent chains, combined with shotgun proteomics, allows us to identify a set of endogenous cotranslationally O-GlcNAc modified proteins.
32870666	10	63	theme	quality	2022:2028	arg1	control					2030:2036	cytoplasmic protein quality control	2002:2036	cytoplasmic protein quality control	2002:2036	Moreover, this work opens the way to studies directed at understanding the roles of O-GlcNAc and other cotranslational protein modifications and should stimulate an improved understanding of the role of O-GlcNAc in cytoplasmic protein quality control and proteostasis.
32870666	6	64	theme	ligation	1160:1167	arg1	strategies					1169:1178	sequential chemoselective ligation strategies	1134:1178	sequential chemoselective ligation strategies	1134:1178	Using various combinations of sequential chemoselective ligation strategies, we go on to tag these analytes with a series of labels, allowing us to define conditions that enable their robust labeling.
32870666	5	65	theme	polypeptide	823:833	arg1	chains					835:840	endogenously occurring nascent polypeptide chains	792:840	endogenously occurring nascent polypeptide chains within cells using O-propargyl-puromycin (OPP)	792:887	Here, we use tandem metabolic engineering strategies to label endogenously occurring nascent polypeptide chains within cells using O-propargyl-puromycin (OPP) and target the specific subset of nascent chains that are cotranslationally glycosylated with O-GlcNAc by metabolic saccharide engineering using tetra-O-acetyl-2-N-azidoacetyl-2-deoxy-d-galactopyranose (Ac4GalNAz).
32870666	10	66	from	understanding	1961:1973	arg1	proteostasis					2042:2053	proteostasis	2042:2053	proteostasis	2042:2053	Moreover, this work opens the way to studies directed at understanding the roles of O-GlcNAc and other cotranslational protein modifications and should stimulate an improved understanding of the role of O-GlcNAc in cytoplasmic protein quality control and proteostasis.
32870666	10	66	from	understanding	1961:1973	arg1	control					2030:2036	cytoplasmic protein quality control	2002:2036	cytoplasmic protein quality control	2002:2036	Moreover, this work opens the way to studies directed at understanding the roles of O-GlcNAc and other cotranslational protein modifications and should stimulate an improved understanding of the role of O-GlcNAc in cytoplasmic protein quality control and proteostasis.
32870666	6	67	theme	sequential	1134:1143	arg1	strategies					1169:1178	sequential chemoselective ligation strategies	1134:1178	sequential chemoselective ligation strategies	1134:1178	Using various combinations of sequential chemoselective ligation strategies, we go on to tag these analytes with a series of labels, allowing us to define conditions that enable their robust labeling.
32870666	9	68	theme	low	1712:1714	arg1	analytes					1737:1744	extremely low abundance endogenous analytes	1702:1744	extremely low abundance endogenous analytes present within complex protein mixtures	1702:1784	These findings detail strategies to enable isolation and identification of extremely low abundance endogenous analytes present within complex protein mixtures.
32870666	7	69	theme	Two-step	1305:1312	arg1	enrichment					1314:1323	Two-step enrichment	1305:1323	Two-step enrichment	1305:1323	Two-step enrichment of these glycosylated nascent chains, combined with shotgun proteomics, allows us to identify a set of endogenous cotranslationally O-GlcNAc modified proteins.
32870666	9	70	theme	endogenous	1726:1735	arg1	analytes					1737:1744	extremely low abundance endogenous analytes	1702:1744	extremely low abundance endogenous analytes present within complex protein mixtures	1702:1784	These findings detail strategies to enable isolation and identification of extremely low abundance endogenous analytes present within complex protein mixtures.
32870666	5	71	theme	metabolic	995:1003	arg1	engineering					1016:1026	metabolic saccharide engineering	995:1026	metabolic saccharide engineering using tetra-O-acetyl-2-N-azidoacetyl-2-deoxy-d-galactopyranose (Ac4GalNAz)	995:1101	Here, we use tandem metabolic engineering strategies to label endogenously occurring nascent polypeptide chains within cells using O-propargyl-puromycin (OPP) and target the specific subset of nascent chains that are cotranslationally glycosylated with O-GlcNAc by metabolic saccharide engineering using tetra-O-acetyl-2-N-azidoacetyl-2-deoxy-d-galactopyranose (Ac4GalNAz).
32870666	3	72	theme	O-GlcNAc	463:470	arg1	function					451:458	A key emerging function	436:458	A key emerging function of O-GlcNAc	436:470	A key emerging function of O-GlcNAc appears to be to regulate cellular protein homeostasis.
32870666	0	73	theme	Bioorthogonal	7:19	arg1	Labeling					21:28	Tandem Bioorthogonal Labeling	0:28	Tandem Bioorthogonal Labeling	0:28	Tandem Bioorthogonal Labeling Uncovers Endogenous Cotranslationally O-GlcNAc Modified Nascent Proteins.
32870666	9	74	theme	present	1746:1752	arg1	analytes					1737:1744	extremely low abundance endogenous analytes	1702:1744	extremely low abundance endogenous analytes present within complex protein mixtures	1702:1784	These findings detail strategies to enable isolation and identification of extremely low abundance endogenous analytes present within complex protein mixtures.
32870666	7	75	theme	endogenous	1428:1437	arg1	proteins					1475:1482	endogenous cotranslationally O-GlcNAc modified proteins	1428:1482	endogenous cotranslationally O-GlcNAc modified proteins	1428:1482	Two-step enrichment of these glycosylated nascent chains, combined with shotgun proteomics, allows us to identify a set of endogenous cotranslationally O-GlcNAc modified proteins.
32870666	8	76	theme	targeted	1503:1510	arg1	methods					1512:1518	alternative targeted methods	1491:1518	alternative targeted methods	1491:1518	Using alternative targeted methods, we examine three of these identified proteins and further validate their cotranslational O-GlcNAcylation.
32870666	2	77	theme	cell	402:405	arg1	physiology					407:416	cell physiology	402:416	cell physiology	402:416	This modification, known as O-GlcNAc, has emerged as a central regulator of both cell physiology and human health.
32870666	9	78	theme	complex	1761:1767	arg1	mixtures					1777:1784	complex protein mixtures	1761:1784	complex protein mixtures	1761:1784	These findings detail strategies to enable isolation and identification of extremely low abundance endogenous analytes present within complex protein mixtures.
32870666	4	79	theme	O-GlcNAc	591:598	arg1	modification					600:611	O-GlcNAc modification	591:611	O-GlcNAc modification	591:611	We previously showed, using overexpressed model proteins, that O-GlcNAc modification can occur cotranslationally and that this process prevents premature degradation of such nascent polypeptide chains.
32870666	9	80	dep	strategies	1649:1658	arg1	enable					1663:1668	enable	1663:1668	to enable isolation and identification of extremely low abundance endogenous analytes present within complex protein mixtures	1660:1784	These findings detail strategies to enable isolation and identification of extremely low abundance endogenous analytes present within complex protein mixtures.
32870666	7	81	gly	glycosylated	1334:1345	arg1	chains					1355:1360	these glycosylated nascent chains	1328:1360	these glycosylated nascent chains	1328:1360	Two-step enrichment of these glycosylated nascent chains, combined with shotgun proteomics, allows us to identify a set of endogenous cotranslationally O-GlcNAc modified proteins.
32870666	6	82	theme	labels	1229:1234	arg1	series					1219:1224	a series	1217:1224	a series of labels	1217:1234	Using various combinations of sequential chemoselective ligation strategies, we go on to tag these analytes with a series of labels, allowing us to define conditions that enable their robust labeling.
32870666	0	83	theme	Cotranslationally	50:66	arg1	Proteins					94:101	Endogenous Cotranslationally O-GlcNAc Modified Nascent Proteins	39:101	Endogenous Cotranslationally O-GlcNAc Modified Nascent Proteins	39:101	Tandem Bioorthogonal Labeling Uncovers Endogenous Cotranslationally O-GlcNAc Modified Nascent Proteins.
32870666	1	84	theme	threonine	241:249	arg1	residues					251:258	specific serine and threonine residues	221:258	specific serine and threonine residues modified by the monosaccharide N-acetylglucosamine (GlcNAc)	221:318	Hundreds of nuclear, cytoplasmic, and mitochondrial proteins within multicellular eukaryotes have hydroxyl groups of specific serine and threonine residues modified by the monosaccharide N-acetylglucosamine (GlcNAc).
32870666	10	85	from	control	2030:2036	arg1	understanding					1961:1973	an improved understanding	1949:1973	an improved understanding of the role of O-GlcNAc in cytoplasmic protein quality control and proteostasis	1949:2053	Moreover, this work opens the way to studies directed at understanding the roles of O-GlcNAc and other cotranslational protein modifications and should stimulate an improved understanding of the role of O-GlcNAc in cytoplasmic protein quality control and proteostasis.
32870666	3	86	theme	key	438:440	arg1	function					451:458	A key emerging function	436:458	A key emerging function of O-GlcNAc	436:470	A key emerging function of O-GlcNAc appears to be to regulate cellular protein homeostasis.
32870666	2	87	theme	health	428:433	arg1	regulator					384:392	a central regulator	374:392	a central regulator of both cell physiology and human health	374:433	This modification, known as O-GlcNAc, has emerged as a central regulator of both cell physiology and human health.
32870666	0	88	theme	Modified	77:84	arg1	Proteins					94:101	Endogenous Cotranslationally O-GlcNAc Modified Nascent Proteins	39:101	Endogenous Cotranslationally O-GlcNAc Modified Nascent Proteins	39:101	Tandem Bioorthogonal Labeling Uncovers Endogenous Cotranslationally O-GlcNAc Modified Nascent Proteins.
32870666	4	89	theme	model	570:574	arg1	proteins					576:583	overexpressed model proteins	556:583	overexpressed model proteins	556:583	We previously showed, using overexpressed model proteins, that O-GlcNAc modification can occur cotranslationally and that this process prevents premature degradation of such nascent polypeptide chains.
32870666	8	90	theme	identified	1547:1556	arg1	proteins					1558:1565	these identified proteins	1541:1565	these identified proteins	1541:1565	Using alternative targeted methods, we examine three of these identified proteins and further validate their cotranslational O-GlcNAcylation.
32870666	3	91	theme	cellular	498:505	arg1	homeostasis					515:525	cellular protein homeostasis	498:525	cellular protein homeostasis	498:525	A key emerging function of O-GlcNAc appears to be to regulate cellular protein homeostasis.
32870666	7	92	theme	shotgun	1377:1383	arg1	proteomics					1385:1394	shotgun proteomics	1377:1394	shotgun proteomics	1377:1394	Two-step enrichment of these glycosylated nascent chains, combined with shotgun proteomics, allows us to identify a set of endogenous cotranslationally O-GlcNAc modified proteins.
32870666	1	93	theme	monosaccharide	276:289	arg1	GlcNAc					312:317	GlcNAc	312:317	GlcNAc	312:317	Hundreds of nuclear, cytoplasmic, and mitochondrial proteins within multicellular eukaryotes have hydroxyl groups of specific serine and threonine residues modified by the monosaccharide N-acetylglucosamine (GlcNAc).
32870666	1	93	theme	monosaccharide	276:289	arg1	N-acetylglucosamine					291:309	the monosaccharide N-acetylglucosamine	272:309	the monosaccharide N-acetylglucosamine (GlcNAc)	272:318	Hundreds of nuclear, cytoplasmic, and mitochondrial proteins within multicellular eukaryotes have hydroxyl groups of specific serine and threonine residues modified by the monosaccharide N-acetylglucosamine (GlcNAc).
34681736	0	0	theme	Colon	81:85	arg1	Cells					94:98	Colon Cancer Cells	81:98	Colon Cancer Cells	81:98	OSMI-1 Enhances TRAIL-Induced Apoptosis through ER Stress and NF-κB Signaling in Colon Cancer Cells.
34681736	5	1	theme	CHOP-DR5	788:795	arg1	signaling					797:805	CHOP-DR5 signaling	788:805	CHOP-DR5 signaling	788:805	ROS-induced endoplasmic reticulum (ER) stress by OSMI-1 not only upregulated CHOP-DR5 signaling but also activated Jun-N-terminal kinase (JNK), resulting in a decrease in Bcl2 and the release of cytochrome c from mitochondria.
34681736	7	2	theme	degradation	1102:1112	arg1	O-GlcNAcylation					1057:1071	O-GlcNAcylation	1057:1071	O-GlcNAcylation of IκB kinase (IKK) and IκBα degradation	1057:1112	During this process, O-GlcNAcylation of IκB kinase (IKK) and IκBα degradation occurred, followed by translocation of p65 into the nucleus.
34681736	9	3	theme	TRAIL	1378:1382	arg1	treatment					1354:1362	the combined treatment	1341:1362	the combined treatment of OSMI-1 and TRAIL	1341:1382	Therefore, the combined treatment of OSMI-1 and TRAIL synergistically increased TRAIL-induced apoptosis through caspase-8 activation.
34681736	3	4	theme	cancer	494:499	arg1	cells					501:505	HCT116 human colon cancer cells	475:505	HCT116 human colon cancer cells	475:505	We found that OSMI-1 treatment in HCT116 human colon cancer cells has a potent synergistic effect on TRAIL-induced apoptosis signaling.
34681736	9	5	theme	TRAIL-induced	1410:1422	arg1	apoptosis					1424:1432	TRAIL-induced apoptosis	1410:1432	TRAIL-induced apoptosis	1410:1432	Therefore, the combined treatment of OSMI-1 and TRAIL synergistically increased TRAIL-induced apoptosis through caspase-8 activation.
34681736	7	6	theme	IκB	1076:1078	arg1	IKK					1088:1090	IKK	1088:1090	IKK	1088:1090	During this process, O-GlcNAcylation of IκB kinase (IKK) and IκBα degradation occurred, followed by translocation of p65 into the nucleus.
34681736	7	6	theme	IκB	1076:1078	arg1	kinase					1080:1085	IκB kinase	1076:1085	IκB kinase (IKK)	1076:1091	During this process, O-GlcNAcylation of IκB kinase (IKK) and IκBα degradation occurred, followed by translocation of p65 into the nucleus.
34681736	1	7	theme	hyper-O-GlcNAcylation	142:162	arg1	levels					175:180	hyper-O-GlcNAcylation expression levels	142:180	hyper-O-GlcNAcylation expression levels	142:180	Levels of O-GlcNAc transferase (OGT) and hyper-O-GlcNAcylation expression levels are associated with cancer pathogenesis.
34681736	3	8	from	effect	532:537	arg1	signaling					566:574	TRAIL-induced apoptosis signaling	542:574	TRAIL-induced apoptosis signaling	542:574	We found that OSMI-1 treatment in HCT116 human colon cancer cells has a potent synergistic effect on TRAIL-induced apoptosis signaling.
34681736	3	9	contain	has	507:509	arg2	effect					532:537	a potent synergistic effect	511:537	a potent synergistic effect on TRAIL-induced apoptosis signaling	511:574	We found that OSMI-1 treatment in HCT116 human colon cancer cells has a potent synergistic effect on TRAIL-induced apoptosis signaling.
34681736	3	9	contain	has	507:509	arg1	treatment					462:470	OSMI-1 treatment	455:470	OSMI-1 treatment in HCT116 human colon cancer cells	455:505	We found that OSMI-1 treatment in HCT116 human colon cancer cells has a potent synergistic effect on TRAIL-induced apoptosis signaling.
34681736	2	10	theme	OGT	349:351	arg1	inhibitor					353:361	an OGT inhibitor	346:361	an OGT inhibitor (OSMI-1)	346:370	This study aimed to find conditions that maximize the therapeutic effect of cancer and minimize tissue damage by combining an OGT inhibitor (OSMI-1) and tumor necrosis factor-related apoptosis-inducing ligand (TRAIL).
34681736	2	10	theme	OGT	349:351	arg1	OSMI-1					364:369	OSMI-1	364:369	OSMI-1	364:369	This study aimed to find conditions that maximize the therapeutic effect of cancer and minimize tissue damage by combining an OGT inhibitor (OSMI-1) and tumor necrosis factor-related apoptosis-inducing ligand (TRAIL).
34681736	3	11	theme	apoptosis	556:564	arg1	signaling					566:574	TRAIL-induced apoptosis signaling	542:574	TRAIL-induced apoptosis signaling	542:574	We found that OSMI-1 treatment in HCT116 human colon cancer cells has a potent synergistic effect on TRAIL-induced apoptosis signaling.
34681736	0	12	theme	Cancer	87:92	arg1	Cells					94:98	Colon Cancer Cells	81:98	Colon Cancer Cells	81:98	OSMI-1 Enhances TRAIL-Induced Apoptosis through ER Stress and NF-κB Signaling in Colon Cancer Cells.
34681736	7	13	theme	IκBα	1097:1100	arg1	degradation					1102:1112	IκBα degradation	1097:1112	IκBα degradation	1097:1112	During this process, O-GlcNAcylation of IκB kinase (IKK) and IκBα degradation occurred, followed by translocation of p65 into the nucleus.
34681736	9	14	theme	caspase-8	1442:1450	arg1	activation					1452:1461	caspase-8 activation	1442:1461	caspase-8 activation	1442:1461	Therefore, the combined treatment of OSMI-1 and TRAIL synergistically increased TRAIL-induced apoptosis through caspase-8 activation.
34681736	0	15	from	Stress	51:56	arg1	Cells					94:98	Colon Cancer Cells	81:98	Colon Cancer Cells	81:98	OSMI-1 Enhances TRAIL-Induced Apoptosis through ER Stress and NF-κB Signaling in Colon Cancer Cells.
34681736	6	16	from	role	989:992	arg1	resistance					997:1006	resistance	997:1006	resistance	997:1006	TRAIL induced the activation of NF-κB and played a role in resistance as an antiapoptotic factor.
34681736	5	17	from	release	895:901	arg1	Bcl2					882:885	Bcl2	882:885	Bcl2	882:885	ROS-induced endoplasmic reticulum (ER) stress by OSMI-1 not only upregulated CHOP-DR5 signaling but also activated Jun-N-terminal kinase (JNK), resulting in a decrease in Bcl2 and the release of cytochrome c from mitochondria.
34681736	2	18	theme	therapeutic	277:287	arg1	effect					289:294	the therapeutic effect	273:294	the therapeutic effect of cancer	273:304	This study aimed to find conditions that maximize the therapeutic effect of cancer and minimize tissue damage by combining an OGT inhibitor (OSMI-1) and tumor necrosis factor-related apoptosis-inducing ligand (TRAIL).
34681736	1	19	theme	expression	164:173	arg1	levels					175:180	hyper-O-GlcNAcylation expression levels	142:180	hyper-O-GlcNAcylation expression levels	142:180	Levels of O-GlcNAc transferase (OGT) and hyper-O-GlcNAcylation expression levels are associated with cancer pathogenesis.
34681736	10	20	theme	activation	1593:1602	arg1	blockade					1561:1568	the blockade	1557:1568	the blockade of NF-κB signaling and activation of apoptosis through ER stress response	1557:1642	Conclusively, OSMI-1 potentially sensitizes TRAIL-induced cell death in HCT116 cells through the blockade of NF-κB signaling and activation of apoptosis through ER stress response.
34681736	5	21	theme	cytochrome	906:915	arg1	c					917:917	cytochrome c	906:917	cytochrome c	906:917	ROS-induced endoplasmic reticulum (ER) stress by OSMI-1 not only upregulated CHOP-DR5 signaling but also activated Jun-N-terminal kinase (JNK), resulting in a decrease in Bcl2 and the release of cytochrome c from mitochondria.
34681736	5	22	from	mitochondria	924:935	arg1	release					895:901	the release	891:901	the release of cytochrome c from mitochondria	891:935	ROS-induced endoplasmic reticulum (ER) stress by OSMI-1 not only upregulated CHOP-DR5 signaling but also activated Jun-N-terminal kinase (JNK), resulting in a decrease in Bcl2 and the release of cytochrome c from mitochondria.
34681736	5	22	from	mitochondria	924:935	arg1	decrease					870:877	a decrease	868:877	a decrease in Bcl2	868:885	ROS-induced endoplasmic reticulum (ER) stress by OSMI-1 not only upregulated CHOP-DR5 signaling but also activated Jun-N-terminal kinase (JNK), resulting in a decrease in Bcl2 and the release of cytochrome c from mitochondria.
34681736	3	23	theme	synergistic	520:530	arg1	effect					532:537	a potent synergistic effect	511:537	a potent synergistic effect on TRAIL-induced apoptosis signaling	511:574	We found that OSMI-1 treatment in HCT116 human colon cancer cells has a potent synergistic effect on TRAIL-induced apoptosis signaling.
34681736	1	24	theme	levels	175:180	arg1	Levels					101:106	Levels	101:106	Levels of O-GlcNAc transferase (OGT) and hyper-O-GlcNAcylation expression levels	101:180	Levels of O-GlcNAc transferase (OGT) and hyper-O-GlcNAcylation expression levels are associated with cancer pathogenesis.
34681736	7	25	theme	kinase	1080:1085	arg1	O-GlcNAcylation					1057:1071	O-GlcNAcylation	1057:1071	O-GlcNAcylation of IκB kinase (IKK) and IκBα degradation	1057:1112	During this process, O-GlcNAcylation of IκB kinase (IKK) and IκBα degradation occurred, followed by translocation of p65 into the nucleus.
34681736	2	26	theme	tissue	319:324	arg1	damage					326:331	tissue damage	319:331	tissue damage	319:331	This study aimed to find conditions that maximize the therapeutic effect of cancer and minimize tissue damage by combining an OGT inhibitor (OSMI-1) and tumor necrosis factor-related apoptosis-inducing ligand (TRAIL).
34681736	4	27	theme	receptor	697:704	arg1	expression					666:675	the expression	662:675	the expression of the cell surface receptor DR5	662:708	Interestingly, OSMI-1 significantly increased TRAIL-mediated apoptosis by increasing the expression of the cell surface receptor DR5.
34681736	4	28	theme	cell	684:687	arg1	receptor					697:704	cell surface receptor	684:704	the cell surface receptor DR5	680:708	Interestingly, OSMI-1 significantly increased TRAIL-mediated apoptosis by increasing the expression of the cell surface receptor DR5.
34681736	10	29	theme	TRAIL-induced	1508:1520	arg1	death					1527:1531	TRAIL-induced cell death	1508:1531	TRAIL-induced cell death in HCT116 cells	1508:1547	Conclusively, OSMI-1 potentially sensitizes TRAIL-induced cell death in HCT116 cells through the blockade of NF-κB signaling and activation of apoptosis through ER stress response.
34681736	8	30	theme	TRAIL-mediated	1245:1258	arg1	signaling					1266:1274	TRAIL-mediated NF-κB signaling	1245:1274	TRAIL-mediated NF-κB signaling	1245:1274	However, combination treatment with OSMI-1 counteracted the effect of TRAIL-mediated NF-κB signaling, resulting in a more synergistic effect on apoptosis.
34681736	4	31	theme	surface	689:695	arg1	receptor					697:704	cell surface receptor	684:704	the cell surface receptor DR5	680:708	Interestingly, OSMI-1 significantly increased TRAIL-mediated apoptosis by increasing the expression of the cell surface receptor DR5.
34681736	10	32	theme	stress	1628:1633	arg1	response					1635:1642	ER stress response	1625:1642	ER stress response	1625:1642	Conclusively, OSMI-1 potentially sensitizes TRAIL-induced cell death in HCT116 cells through the blockade of NF-κB signaling and activation of apoptosis through ER stress response.
34681736	8	33	from	effect	1309:1314	arg1	apoptosis					1319:1327	apoptosis	1319:1327	apoptosis	1319:1327	However, combination treatment with OSMI-1 counteracted the effect of TRAIL-mediated NF-κB signaling, resulting in a more synergistic effect on apoptosis.
34681736	5	34	theme	reticulum	735:743	arg1	stress					750:755	ROS-induced endoplasmic reticulum (ER) stress	711:755	ROS-induced endoplasmic reticulum (ER) stress by OSMI-1	711:765	ROS-induced endoplasmic reticulum (ER) stress by OSMI-1 not only upregulated CHOP-DR5 signaling but also activated Jun-N-terminal kinase (JNK), resulting in a decrease in Bcl2 and the release of cytochrome c from mitochondria.
34681736	3	35	theme	TRAIL-induced	542:554	arg1	signaling					566:574	TRAIL-induced apoptosis signaling	542:574	TRAIL-induced apoptosis signaling	542:574	We found that OSMI-1 treatment in HCT116 human colon cancer cells has a potent synergistic effect on TRAIL-induced apoptosis signaling.
34681736	3	36	theme	OSMI-1	455:460	arg1	treatment					462:470	OSMI-1 treatment	455:470	OSMI-1 treatment in HCT116 human colon cancer cells	455:505	We found that OSMI-1 treatment in HCT116 human colon cancer cells has a potent synergistic effect on TRAIL-induced apoptosis signaling.
34681736	0	37	theme	TRAIL-Induced	16:28	arg1	Apoptosis					30:38	TRAIL-Induced Apoptosis	16:38	TRAIL-Induced Apoptosis	16:38	OSMI-1 Enhances TRAIL-Induced Apoptosis through ER Stress and NF-κB Signaling in Colon Cancer Cells.
34681736	6	38	theme	NF-κB	970:974	arg1	activation					956:965	the activation	952:965	the activation of NF-κB	952:974	TRAIL induced the activation of NF-κB and played a role in resistance as an antiapoptotic factor.
34681736	3	39	theme	potent	513:518	arg1	effect					532:537	a potent synergistic effect	511:537	a potent synergistic effect on TRAIL-induced apoptosis signaling	511:574	We found that OSMI-1 treatment in HCT116 human colon cancer cells has a potent synergistic effect on TRAIL-induced apoptosis signaling.
34681736	2	40	theme	cancer	299:304	arg1	effect					289:294	the therapeutic effect	273:294	the therapeutic effect of cancer	273:304	This study aimed to find conditions that maximize the therapeutic effect of cancer and minimize tissue damage by combining an OGT inhibitor (OSMI-1) and tumor necrosis factor-related apoptosis-inducing ligand (TRAIL).
34681736	1	41	theme	cancer	202:207	arg1	pathogenesis					209:220	cancer pathogenesis	202:220	cancer pathogenesis	202:220	Levels of O-GlcNAc transferase (OGT) and hyper-O-GlcNAcylation expression levels are associated with cancer pathogenesis.
34681736	0	42	theme	ER	48:49	arg1	Stress					51:56	ER Stress	48:56	ER Stress	48:56	OSMI-1 Enhances TRAIL-Induced Apoptosis through ER Stress and NF-κB Signaling in Colon Cancer Cells.
34681736	3	43	theme	colon	488:492	arg1	cells					501:505	HCT116 human colon cancer cells	475:505	HCT116 human colon cancer cells	475:505	We found that OSMI-1 treatment in HCT116 human colon cancer cells has a potent synergistic effect on TRAIL-induced apoptosis signaling.
34681736	10	44	theme	ER	1625:1626	arg1	response					1635:1642	ER stress response	1625:1642	ER stress response	1625:1642	Conclusively, OSMI-1 potentially sensitizes TRAIL-induced cell death in HCT116 cells through the blockade of NF-κB signaling and activation of apoptosis through ER stress response.
34681736	2	45	theme	apoptosis-inducing	406:423	arg1	TRAIL					433:437	TRAIL	433:437	TRAIL	433:437	This study aimed to find conditions that maximize the therapeutic effect of cancer and minimize tissue damage by combining an OGT inhibitor (OSMI-1) and tumor necrosis factor-related apoptosis-inducing ligand (TRAIL).
34681736	2	45	theme	apoptosis-inducing	406:423	arg1	ligand					425:430	tumor necrosis factor-related apoptosis-inducing ligand	376:430	tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)	376:438	This study aimed to find conditions that maximize the therapeutic effect of cancer and minimize tissue damage by combining an OGT inhibitor (OSMI-1) and tumor necrosis factor-related apoptosis-inducing ligand (TRAIL).
34681736	2	46	theme	necrosis	382:389	arg1	TRAIL					433:437	TRAIL	433:437	TRAIL	433:437	This study aimed to find conditions that maximize the therapeutic effect of cancer and minimize tissue damage by combining an OGT inhibitor (OSMI-1) and tumor necrosis factor-related apoptosis-inducing ligand (TRAIL).
34681736	2	46	theme	necrosis	382:389	arg1	ligand					425:430	tumor necrosis factor-related apoptosis-inducing ligand	376:430	tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)	376:438	This study aimed to find conditions that maximize the therapeutic effect of cancer and minimize tissue damage by combining an OGT inhibitor (OSMI-1) and tumor necrosis factor-related apoptosis-inducing ligand (TRAIL).
34681736	9	47	theme	combined	1345:1352	arg1	treatment					1354:1362	the combined treatment	1341:1362	the combined treatment of OSMI-1 and TRAIL	1341:1382	Therefore, the combined treatment of OSMI-1 and TRAIL synergistically increased TRAIL-induced apoptosis through caspase-8 activation.
34681736	8	48	theme	combination	1184:1194	arg1	treatment					1196:1204	combination treatment	1184:1204	combination treatment with OSMI-1	1184:1216	However, combination treatment with OSMI-1 counteracted the effect of TRAIL-mediated NF-κB signaling, resulting in a more synergistic effect on apoptosis.
34681736	0	49	from	Signaling	68:76	arg1	Cells					94:98	Colon Cancer Cells	81:98	Colon Cancer Cells	81:98	OSMI-1 Enhances TRAIL-Induced Apoptosis through ER Stress and NF-κB Signaling in Colon Cancer Cells.
34681736	10	50	theme	cell	1522:1525	arg1	death					1527:1531	TRAIL-induced cell death	1508:1531	TRAIL-induced cell death in HCT116 cells	1508:1547	Conclusively, OSMI-1 potentially sensitizes TRAIL-induced cell death in HCT116 cells through the blockade of NF-κB signaling and activation of apoptosis through ER stress response.
34681736	2	51	theme	factor-related	391:404	arg1	TRAIL					433:437	TRAIL	433:437	TRAIL	433:437	This study aimed to find conditions that maximize the therapeutic effect of cancer and minimize tissue damage by combining an OGT inhibitor (OSMI-1) and tumor necrosis factor-related apoptosis-inducing ligand (TRAIL).
34681736	2	51	theme	factor-related	391:404	arg1	ligand					425:430	tumor necrosis factor-related apoptosis-inducing ligand	376:430	tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)	376:438	This study aimed to find conditions that maximize the therapeutic effect of cancer and minimize tissue damage by combining an OGT inhibitor (OSMI-1) and tumor necrosis factor-related apoptosis-inducing ligand (TRAIL).
34681736	10	52	theme	signaling	1579:1587	arg1	blockade					1561:1568	the blockade	1557:1568	the blockade of NF-κB signaling and activation of apoptosis through ER stress response	1557:1642	Conclusively, OSMI-1 potentially sensitizes TRAIL-induced cell death in HCT116 cells through the blockade of NF-κB signaling and activation of apoptosis through ER stress response.
34681736	7	53	dep	occurred	1114:1121	arg1	followed					1124:1131	followed	1124:1131	followed by translocation of p65 into the nucleus	1124:1172	During this process, O-GlcNAcylation of IκB kinase (IKK) and IκBα degradation occurred, followed by translocation of p65 into the nucleus.
34681736	3	54	theme	human	482:486	arg1	cells					501:505	HCT116 human colon cancer cells	475:505	HCT116 human colon cancer cells	475:505	We found that OSMI-1 treatment in HCT116 human colon cancer cells has a potent synergistic effect on TRAIL-induced apoptosis signaling.
34681736	5	55	theme	Jun-N-terminal	826:839	arg1	JNK					849:851	JNK	849:851	JNK	849:851	ROS-induced endoplasmic reticulum (ER) stress by OSMI-1 not only upregulated CHOP-DR5 signaling but also activated Jun-N-terminal kinase (JNK), resulting in a decrease in Bcl2 and the release of cytochrome c from mitochondria.
34681736	5	55	theme	Jun-N-terminal	826:839	arg1	kinase					841:846	Jun-N-terminal kinase	826:846	Jun-N-terminal kinase (JNK)	826:852	ROS-induced endoplasmic reticulum (ER) stress by OSMI-1 not only upregulated CHOP-DR5 signaling but also activated Jun-N-terminal kinase (JNK), resulting in a decrease in Bcl2 and the release of cytochrome c from mitochondria.
34681736	10	56	theme	HCT116	1536:1541	arg1	cells					1543:1547	HCT116 cells	1536:1547	HCT116 cells	1536:1547	Conclusively, OSMI-1 potentially sensitizes TRAIL-induced cell death in HCT116 cells through the blockade of NF-κB signaling and activation of apoptosis through ER stress response.
34681736	10	57	theme	NF-κB	1573:1577	arg1	signaling					1579:1587	NF-κB signaling	1573:1587	NF-κB signaling	1573:1587	Conclusively, OSMI-1 potentially sensitizes TRAIL-induced cell death in HCT116 cells through the blockade of NF-κB signaling and activation of apoptosis through ER stress response.
34681736	1	58	theme	O-GlcNAc	111:118	arg1	transferase					120:130	O-GlcNAc transferase	111:130	O-GlcNAc transferase (OGT)	111:136	Levels of O-GlcNAc transferase (OGT) and hyper-O-GlcNAcylation expression levels are associated with cancer pathogenesis.
34681736	1	58	theme	O-GlcNAc	111:118	arg1	OGT					133:135	OGT	133:135	OGT	133:135	Levels of O-GlcNAc transferase (OGT) and hyper-O-GlcNAcylation expression levels are associated with cancer pathogenesis.
34681736	9	59	theme	OSMI-1	1367:1372	arg1	treatment					1354:1362	the combined treatment	1341:1362	the combined treatment of OSMI-1 and TRAIL	1341:1382	Therefore, the combined treatment of OSMI-1 and TRAIL synergistically increased TRAIL-induced apoptosis through caspase-8 activation.
34681736	5	60	theme	ROS-induced	711:721	arg1	stress					750:755	ROS-induced endoplasmic reticulum (ER) stress	711:755	ROS-induced endoplasmic reticulum (ER) stress by OSMI-1	711:765	ROS-induced endoplasmic reticulum (ER) stress by OSMI-1 not only upregulated CHOP-DR5 signaling but also activated Jun-N-terminal kinase (JNK), resulting in a decrease in Bcl2 and the release of cytochrome c from mitochondria.
34681736	10	61	from	death	1527:1531	arg1	cells					1543:1547	HCT116 cells	1536:1547	HCT116 cells	1536:1547	Conclusively, OSMI-1 potentially sensitizes TRAIL-induced cell death in HCT116 cells through the blockade of NF-κB signaling and activation of apoptosis through ER stress response.
34681736	4	62	dep	receptor	697:704	arg1	DR5					706:708	DR5	706:708	the cell surface receptor DR5	680:708	Interestingly, OSMI-1 significantly increased TRAIL-mediated apoptosis by increasing the expression of the cell surface receptor DR5.
34681736	3	63	from	treatment	462:470	arg1	cells					501:505	HCT116 human colon cancer cells	475:505	HCT116 human colon cancer cells	475:505	We found that OSMI-1 treatment in HCT116 human colon cancer cells has a potent synergistic effect on TRAIL-induced apoptosis signaling.
34681736	1	64	theme	transferase	120:130	arg1	Levels					101:106	Levels	101:106	Levels of O-GlcNAc transferase (OGT) and hyper-O-GlcNAcylation expression levels	101:180	Levels of O-GlcNAc transferase (OGT) and hyper-O-GlcNAcylation expression levels are associated with cancer pathogenesis.
34681736	8	65	with	treatment	1196:1204	arg1	OSMI-1					1211:1216	OSMI-1	1211:1216	OSMI-1	1211:1216	However, combination treatment with OSMI-1 counteracted the effect of TRAIL-mediated NF-κB signaling, resulting in a more synergistic effect on apoptosis.
34681736	4	66	theme	TRAIL-mediated	623:636	arg1	apoptosis					638:646	TRAIL-mediated apoptosis	623:646	TRAIL-mediated apoptosis	623:646	Interestingly, OSMI-1 significantly increased TRAIL-mediated apoptosis by increasing the expression of the cell surface receptor DR5.
34681736	5	67	theme	endoplasmic	723:733	arg1	ER					746:747	ER	746:747	ER	746:747	ROS-induced endoplasmic reticulum (ER) stress by OSMI-1 not only upregulated CHOP-DR5 signaling but also activated Jun-N-terminal kinase (JNK), resulting in a decrease in Bcl2 and the release of cytochrome c from mitochondria.
34681736	5	67	theme	endoplasmic	723:733	arg1	reticulum					735:743	endoplasmic reticulum	723:743	ROS-induced endoplasmic reticulum (ER) stress by OSMI-1	711:765	ROS-induced endoplasmic reticulum (ER) stress by OSMI-1 not only upregulated CHOP-DR5 signaling but also activated Jun-N-terminal kinase (JNK), resulting in a decrease in Bcl2 and the release of cytochrome c from mitochondria.
34681736	5	68	theme	c	917:917	arg1	release					895:901	the release	891:901	the release of cytochrome c from mitochondria	891:935	ROS-induced endoplasmic reticulum (ER) stress by OSMI-1 not only upregulated CHOP-DR5 signaling but also activated Jun-N-terminal kinase (JNK), resulting in a decrease in Bcl2 and the release of cytochrome c from mitochondria.
34681736	5	68	theme	c	917:917	arg1	decrease					870:877	a decrease	868:877	a decrease in Bcl2	868:885	ROS-induced endoplasmic reticulum (ER) stress by OSMI-1 not only upregulated CHOP-DR5 signaling but also activated Jun-N-terminal kinase (JNK), resulting in a decrease in Bcl2 and the release of cytochrome c from mitochondria.
34681736	3	69	theme	HCT116	475:480	arg1	cells					501:505	HCT116 human colon cancer cells	475:505	HCT116 human colon cancer cells	475:505	We found that OSMI-1 treatment in HCT116 human colon cancer cells has a potent synergistic effect on TRAIL-induced apoptosis signaling.
34681736	6	70	theme	antiapoptotic	1014:1026	arg1	factor					1028:1033	an antiapoptotic factor	1011:1033	an antiapoptotic factor	1011:1033	TRAIL induced the activation of NF-κB and played a role in resistance as an antiapoptotic factor.
34681736	8	71	theme	signaling	1266:1274	arg1	effect					1235:1240	the effect	1231:1240	the effect of TRAIL-mediated NF-κB signaling	1231:1274	However, combination treatment with OSMI-1 counteracted the effect of TRAIL-mediated NF-κB signaling, resulting in a more synergistic effect on apoptosis.
34681736	8	72	theme	NF-κB	1260:1264	arg1	signaling					1266:1274	TRAIL-mediated NF-κB signaling	1245:1274	TRAIL-mediated NF-κB signaling	1245:1274	However, combination treatment with OSMI-1 counteracted the effect of TRAIL-mediated NF-κB signaling, resulting in a more synergistic effect on apoptosis.
34681736	2	73	theme	tumor	376:380	arg1	TRAIL					433:437	TRAIL	433:437	TRAIL	433:437	This study aimed to find conditions that maximize the therapeutic effect of cancer and minimize tissue damage by combining an OGT inhibitor (OSMI-1) and tumor necrosis factor-related apoptosis-inducing ligand (TRAIL).
34681736	2	73	theme	tumor	376:380	arg1	ligand					425:430	tumor necrosis factor-related apoptosis-inducing ligand	376:430	tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)	376:438	This study aimed to find conditions that maximize the therapeutic effect of cancer and minimize tissue damage by combining an OGT inhibitor (OSMI-1) and tumor necrosis factor-related apoptosis-inducing ligand (TRAIL).
34681736	0	74	theme	NF-κB	62:66	arg1	Signaling					68:76	NF-κB Signaling	62:76	NF-κB Signaling	62:76	OSMI-1 Enhances TRAIL-Induced Apoptosis through ER Stress and NF-κB Signaling in Colon Cancer Cells.
34681736	7	75	theme	p65	1153:1155	arg1	translocation					1136:1148	translocation	1136:1148	translocation of p65 into the nucleus	1136:1172	During this process, O-GlcNAcylation of IκB kinase (IKK) and IκBα degradation occurred, followed by translocation of p65 into the nucleus.
34681736	5	76	from	decrease	870:877	arg1	Bcl2					882:885	Bcl2	882:885	Bcl2	882:885	ROS-induced endoplasmic reticulum (ER) stress by OSMI-1 not only upregulated CHOP-DR5 signaling but also activated Jun-N-terminal kinase (JNK), resulting in a decrease in Bcl2 and the release of cytochrome c from mitochondria.
34681736	8	77	theme	synergistic	1297:1307	arg1	effect					1309:1314	a more synergistic effect	1290:1314	a more synergistic effect on apoptosis	1290:1327	However, combination treatment with OSMI-1 counteracted the effect of TRAIL-mediated NF-κB signaling, resulting in a more synergistic effect on apoptosis.
34681736	10	78	theme	apoptosis	1607:1615	arg1	signaling					1579:1587	NF-κB signaling	1573:1587	NF-κB signaling	1573:1587	Conclusively, OSMI-1 potentially sensitizes TRAIL-induced cell death in HCT116 cells through the blockade of NF-κB signaling and activation of apoptosis through ER stress response.
34681736	10	78	theme	apoptosis	1607:1615	arg1	activation					1593:1602	activation	1593:1602	activation of apoptosis	1593:1615	Conclusively, OSMI-1 potentially sensitizes TRAIL-induced cell death in HCT116 cells through the blockade of NF-κB signaling and activation of apoptosis through ER stress response.
18840611	0	0	theme	other	117:121	arg1	proteins					135:142	other interacting proteins	117:142	other interacting proteins	117:142	O-linked beta-N-acetylglucosaminyltransferase substrate specificity is regulated by myosin phosphatase targeting and other interacting proteins.
18840611	5	1	theme	OGT	604:606	arg1	substrates					590:599	substrates	590:599	substrates of OGT in vitro and in vivo	590:627	MYPT1 and CARM1 are substrates of OGT in vitro and in vivo.
18840611	5	1	theme	OGT	604:606	arg1	CARM1					580:584	CARM1	580:584	CARM1	580:584	MYPT1 and CARM1 are substrates of OGT in vitro and in vivo.
18840611	5	1	theme	OGT	604:606	arg1	MYPT1					570:574	MYPT1	570:574	MYPT1	570:574	MYPT1 and CARM1 are substrates of OGT in vitro and in vivo.
18840611	7	2	theme	MYPT1	730:734	arg1	depletion					717:725	depletion	717:725	depletion of MYPT1 in Neuro-2a neuroblastoma cells	717:766	Furthermore depletion of MYPT1 in Neuro-2a neuroblastoma cells alters GlcNAcylation of several proteins under basal conditions, suggesting that MYPT1 regulates OGT substrate specificity in vivo.
18840611	0	3	theme	interacting	123:133	arg1	proteins					135:142	other interacting proteins	117:142	other interacting proteins	117:142	O-linked beta-N-acetylglucosaminyltransferase substrate specificity is regulated by myosin phosphatase targeting and other interacting proteins.
18840611	7	4	theme	substrate	869:877	arg1	specificity					879:889	OGT substrate specificity	865:889	OGT substrate specificity	865:889	Furthermore depletion of MYPT1 in Neuro-2a neuroblastoma cells alters GlcNAcylation of several proteins under basal conditions, suggesting that MYPT1 regulates OGT substrate specificity in vivo.
18840611	3	5	theme	proteins	390:397	arg1	O-GlcNAcase					419:429	O-GlcNAcase	419:429	O-GlcNAcase	419:429	Two of these proteins, Trak1 (OIP106) and O-GlcNAcase, have been shown previously to interact with and regulate OGT.
18840611	3	5	theme	proteins	390:397	arg1	Trak1					400:404	Trak1	400:404	Trak1 (OIP106)	400:413	Two of these proteins, Trak1 (OIP106) and O-GlcNAcase, have been shown previously to interact with and regulate OGT.
18840611	3	5	theme	proteins	390:397	arg1	Two					377:379	Two	377:379	Two	377:379	Two of these proteins, Trak1 (OIP106) and O-GlcNAcase, have been shown previously to interact with and regulate OGT.
18840611	3	5	theme	proteins	390:397	arg1	proteins					390:397	these proteins	384:397	these proteins	384:397	Two of these proteins, Trak1 (OIP106) and O-GlcNAcase, have been shown previously to interact with and regulate OGT.
18840611	0	6	link	O-linked	0:7	arg1	specificity					56:66	O-linked beta-N-acetylglucosaminyltransferase substrate specificity	0:66	O-linked beta-N-acetylglucosaminyltransferase substrate specificity	0:66	O-linked beta-N-acetylglucosaminyltransferase substrate specificity is regulated by myosin phosphatase targeting and other interacting proteins.
18840611	2	7	theme	OGT-interacting	317:331	arg1	proteins					333:340	27 putative OGT-interacting proteins	305:340	27 putative OGT-interacting proteins	305:340	To further examine the regulation of OGT, we have identified 27 putative OGT-interacting proteins through a yeast two-hybrid screen.
18840611	2	8	theme	putative	308:315	arg1	proteins					333:340	27 putative OGT-interacting proteins	305:340	27 putative OGT-interacting proteins	305:340	To further examine the regulation of OGT, we have identified 27 putative OGT-interacting proteins through a yeast two-hybrid screen.
18840611	1	9	theme	interacting	222:232	arg1	proteins					234:241	transiently interacting proteins	210:241	transiently interacting proteins	210:241	O-GlcNAc-transferase (OGT) substrate specificity is regulated by transiently interacting proteins.
18840611	0	10	theme	beta-N-acetylglucosaminyltransferase	9:44	arg1	specificity					56:66	O-linked beta-N-acetylglucosaminyltransferase substrate specificity	0:66	O-linked beta-N-acetylglucosaminyltransferase substrate specificity	0:66	O-linked beta-N-acetylglucosaminyltransferase substrate specificity is regulated by myosin phosphatase targeting and other interacting proteins.
18840611	7	11	theme	OGT	865:867	arg1	specificity					879:889	OGT substrate specificity	865:889	OGT substrate specificity	865:889	Furthermore depletion of MYPT1 in Neuro-2a neuroblastoma cells alters GlcNAcylation of several proteins under basal conditions, suggesting that MYPT1 regulates OGT substrate specificity in vivo.
18840611	0	12	theme	O-linked	0:7	arg1	specificity					56:66	O-linked beta-N-acetylglucosaminyltransferase substrate specificity	0:66	O-linked beta-N-acetylglucosaminyltransferase substrate specificity	0:66	O-linked beta-N-acetylglucosaminyltransferase substrate specificity is regulated by myosin phosphatase targeting and other interacting proteins.
18840611	7	13	theme	basal	815:819	arg1	conditions					821:830	basal conditions	815:830	basal conditions	815:830	Furthermore depletion of MYPT1 in Neuro-2a neuroblastoma cells alters GlcNAcylation of several proteins under basal conditions, suggesting that MYPT1 regulates OGT substrate specificity in vivo.
18840611	2	14	theme	two-hybrid	358:367	arg1	screen					369:374	a yeast two-hybrid screen	350:374	a yeast two-hybrid screen	350:374	To further examine the regulation of OGT, we have identified 27 putative OGT-interacting proteins through a yeast two-hybrid screen.
18840611	6	15	theme	substrate	673:681	arg1	specificity					683:693	OGT substrate specificity	669:693	OGT substrate specificity	669:693	MYPT1 and CARM1 also function to alter OGT substrate specificity in vitro.
18840611	2	16	theme	yeast	352:356	arg1	screen					369:374	a yeast two-hybrid screen	350:374	a yeast two-hybrid screen	350:374	To further examine the regulation of OGT, we have identified 27 putative OGT-interacting proteins through a yeast two-hybrid screen.
18840611	6	17	theme	OGT	669:671	arg1	specificity					683:693	OGT substrate specificity	669:693	OGT substrate specificity	669:693	MYPT1 and CARM1 also function to alter OGT substrate specificity in vitro.
18840611	0	18	theme	substrate	46:54	arg1	specificity					56:66	O-linked beta-N-acetylglucosaminyltransferase substrate specificity	0:66	O-linked beta-N-acetylglucosaminyltransferase substrate specificity	0:66	O-linked beta-N-acetylglucosaminyltransferase substrate specificity is regulated by myosin phosphatase targeting and other interacting proteins.
18840611	7	19	theme	proteins	800:807	arg1	GlcNAcylation					775:787	GlcNAcylation	775:787	GlcNAcylation of several proteins	775:807	Furthermore depletion of MYPT1 in Neuro-2a neuroblastoma cells alters GlcNAcylation of several proteins under basal conditions, suggesting that MYPT1 regulates OGT substrate specificity in vivo.
18840611	7	20	from	depletion	717:725	arg1	cells					762:766	Neuro-2a neuroblastoma cells	739:766	Neuro-2a neuroblastoma cells	739:766	Furthermore depletion of MYPT1 in Neuro-2a neuroblastoma cells alters GlcNAcylation of several proteins under basal conditions, suggesting that MYPT1 regulates OGT substrate specificity in vivo.
18840611	1	21	theme	O-GlcNAc-transferase	145:164	arg1	specificity					182:192	O-GlcNAc-transferase (OGT) substrate specificity	145:192	O-GlcNAc-transferase (OGT) substrate specificity	145:192	O-GlcNAc-transferase (OGT) substrate specificity is regulated by transiently interacting proteins.
18840611	2	22	theme	OGT	281:283	arg1	regulation					267:276	the regulation	263:276	the regulation of OGT	263:283	To further examine the regulation of OGT, we have identified 27 putative OGT-interacting proteins through a yeast two-hybrid screen.
18840611	0	23	theme	myosin	84:89	arg1	targeting					103:111	myosin phosphatase targeting	84:111	myosin phosphatase targeting	84:111	O-linked beta-N-acetylglucosaminyltransferase substrate specificity is regulated by myosin phosphatase targeting and other interacting proteins.
18840611	7	24	theme	several	792:798	arg1	proteins					800:807	several proteins	792:807	several proteins	792:807	Furthermore depletion of MYPT1 in Neuro-2a neuroblastoma cells alters GlcNAcylation of several proteins under basal conditions, suggesting that MYPT1 regulates OGT substrate specificity in vivo.
18840611	7	25	theme	neuroblastoma	748:760	arg1	cells					762:766	Neuro-2a neuroblastoma cells	739:766	Neuro-2a neuroblastoma cells	739:766	Furthermore depletion of MYPT1 in Neuro-2a neuroblastoma cells alters GlcNAcylation of several proteins under basal conditions, suggesting that MYPT1 regulates OGT substrate specificity in vivo.
18840611	1	26	theme	substrate	172:180	arg1	specificity					182:192	O-GlcNAc-transferase (OGT) substrate specificity	145:192	O-GlcNAc-transferase (OGT) substrate specificity	145:192	O-GlcNAc-transferase (OGT) substrate specificity is regulated by transiently interacting proteins.
18840611	0	27	theme	phosphatase	91:101	arg1	targeting					103:111	myosin phosphatase targeting	84:111	myosin phosphatase targeting	84:111	O-linked beta-N-acetylglucosaminyltransferase substrate specificity is regulated by myosin phosphatase targeting and other interacting proteins.
18840611	7	28	theme	Neuro-2a	739:746	arg1	cells					762:766	Neuro-2a neuroblastoma cells	739:766	Neuro-2a neuroblastoma cells	739:766	Furthermore depletion of MYPT1 in Neuro-2a neuroblastoma cells alters GlcNAcylation of several proteins under basal conditions, suggesting that MYPT1 regulates OGT substrate specificity in vivo.
34019870	8	0	theme	cell	1232:1235	arg1	cultures					1237:1244	2D and 3D cell cultures	1222:1244	2D and 3D cell cultures	1222:1244	Here, we used a combination of small molecule inhibitors, 2D and 3D cell cultures, and biochemistry to confirm our hypothesis.
34019870	5	1	theme	complex	922:928	arg1	chain					896:900	the myosin light chain	879:900	the myosin light chain of the actinomyosin complex	879:928	Specifically, we found that O-GlcNAc modification of the phosphatase MYPT1 maintains its activity, resulting in dephosphorylation and deactivation of the myosin light chain of the actinomyosin complex.
34019870	9	2	theme	O-GlcNAc	1507:1514	arg1	modification					1516:1527	MYPT1 O-GlcNAc modification	1501:1527	MYPT1 O-GlcNAc modification	1501:1527	Specifically, we found that O-GlcNAc levels control the sensitivity of mouse and primary human dermal fibroblasts to lysophosphatidic acid-induced contraction in culture and the phosphorylation of MLC and that MYPT1 O-GlcNAc modification is responsible.
34019870	8	3	theme	3D	1229:1230	arg1	cultures					1237:1244	2D and 3D cell cultures	1222:1244	2D and 3D cell cultures	1222:1244	Here, we used a combination of small molecule inhibitors, 2D and 3D cell cultures, and biochemistry to confirm our hypothesis.
34019870	9	4	theme	primary	1372:1378	arg1	fibroblasts					1393:1403	mouse and primary human dermal fibroblasts	1362:1403	fibroblasts	1393:1403	Specifically, we found that O-GlcNAc levels control the sensitivity of mouse and primary human dermal fibroblasts to lysophosphatidic acid-induced contraction in culture and the phosphorylation of MLC and that MYPT1 O-GlcNAc modification is responsible.
34019870	2	5	theme	dynamic	356:362	arg1	regulator					364:372	a potential dynamic regulator	344:372	it a potential dynamic regulator of cell signaling	341:390	O-GlcNAc is enzymatically added and removed from proteins, making it a potential dynamic regulator of cell signaling.
34019870	3	6	theme	few	487:489	arg1	pathways					510:517	relatively few O-GlcNAc-regulated pathways	476:517	relatively few O-GlcNAc-regulated pathways	476:517	However, compared with other posttranslational modifications like phosphorylation, relatively few O-GlcNAc-regulated pathways have been discovered and biochemically characterized.
34019870	6	7	theme	lysophosphatidic	999:1014	arg1	acid					1016:1019	lysophosphatidic acid	999:1019	lysophosphatidic acid	999:1019	Another signaling lipid that leads to contraction of fibroblasts is lysophosphatidic acid, and this signaling pathway also converges on MYPT1 and actinomyosin.
34019870	9	8	theme	human	1380:1384	arg1	fibroblasts					1393:1403	mouse and primary human dermal fibroblasts	1362:1403	fibroblasts	1393:1403	Specifically, we found that O-GlcNAc levels control the sensitivity of mouse and primary human dermal fibroblasts to lysophosphatidic acid-induced contraction in culture and the phosphorylation of MLC and that MYPT1 O-GlcNAc modification is responsible.
34019870	8	9	theme	cultures	1237:1244	arg1	combination					1180:1190	a combination	1178:1190	a combination of small molecule inhibitors, 2D and 3D cell cultures, and biochemistry	1178:1262	Here, we used a combination of small molecule inhibitors, 2D and 3D cell cultures, and biochemistry to confirm our hypothesis.
34019870	9	10	theme	dermal	1386:1391	arg1	fibroblasts					1393:1403	mouse and primary human dermal fibroblasts	1362:1403	fibroblasts	1393:1403	Specifically, we found that O-GlcNAc levels control the sensitivity of mouse and primary human dermal fibroblasts to lysophosphatidic acid-induced contraction in culture and the phosphorylation of MLC and that MYPT1 O-GlcNAc modification is responsible.
34019870	6	11	theme	signaling	1031:1039	arg1	pathway					1041:1047	this signaling pathway	1026:1047	this signaling pathway	1026:1047	Another signaling lipid that leads to contraction of fibroblasts is lysophosphatidic acid, and this signaling pathway also converges on MYPT1 and actinomyosin.
34019870	8	12	theme	2D	1222:1223	arg1	cultures					1237:1244	2D and 3D cell cultures	1222:1244	2D and 3D cell cultures	1222:1244	Here, we used a combination of small molecule inhibitors, 2D and 3D cell cultures, and biochemistry to confirm our hypothesis.
34019870	8	13	theme	biochemistry	1251:1262	arg1	combination					1180:1190	a combination	1178:1190	a combination of small molecule inhibitors, 2D and 3D cell cultures, and biochemistry	1178:1262	Here, we used a combination of small molecule inhibitors, 2D and 3D cell cultures, and biochemistry to confirm our hypothesis.
34019870	2	14	theme	potential	346:354	arg1	regulator					364:372	a potential dynamic regulator	344:372	it a potential dynamic regulator of cell signaling	341:390	O-GlcNAc is enzymatically added and removed from proteins, making it a potential dynamic regulator of cell signaling.
34019870	4	15	theme	signaling	688:696	arg1	sphingosine-1-phosphate					704:726	the signaling lipid sphingosine-1-phosphate	684:726	the signaling lipid sphingosine-1-phosphate	684:726	We previously discovered one such pathway, where O-GlcNAc controls the contraction of fibroblasts initiated by the signaling lipid sphingosine-1-phosphate.
34019870	5	16	theme	light	890:894	arg1	chain					896:900	the myosin light chain	879:900	the myosin light chain of the actinomyosin complex	879:928	Specifically, we found that O-GlcNAc modification of the phosphatase MYPT1 maintains its activity, resulting in dephosphorylation and deactivation of the myosin light chain of the actinomyosin complex.
34019870	3	17	theme	other	416:420	arg1	modifications					440:452	other posttranslational modifications	416:452	other posttranslational modifications like phosphorylation	416:473	However, compared with other posttranslational modifications like phosphorylation, relatively few O-GlcNAc-regulated pathways have been discovered and biochemically characterized.
34019870	1	18	theme	common	172:177	arg1	modification					193:204	a common glycosylation modification	170:204	a common glycosylation modification of serine and threonine residues	170:237	Thousands of proteins have been found to be modified by O-GlcNAc, a common glycosylation modification of serine and threonine residues throughout the cytosol and nucleus.
34019870	1	18	theme	common	172:177	arg1	O-GlcNAc					160:167	O-GlcNAc	160:167	O-GlcNAc	160:167	Thousands of proteins have been found to be modified by O-GlcNAc, a common glycosylation modification of serine and threonine residues throughout the cytosol and nucleus.
34019870	5	19	theme	chain	896:900	arg1	dephosphorylation					841:857	dephosphorylation	841:857	dephosphorylation	841:857	Specifically, we found that O-GlcNAc modification of the phosphatase MYPT1 maintains its activity, resulting in dephosphorylation and deactivation of the myosin light chain of the actinomyosin complex.
34019870	5	19	theme	chain	896:900	arg1	deactivation					863:874	deactivation	863:874	deactivation	863:874	Specifically, we found that O-GlcNAc modification of the phosphatase MYPT1 maintains its activity, resulting in dephosphorylation and deactivation of the myosin light chain of the actinomyosin complex.
34019870	6	20	theme	fibroblasts	984:994	arg1	contraction					969:979	contraction	969:979	contraction of fibroblasts	969:994	Another signaling lipid that leads to contraction of fibroblasts is lysophosphatidic acid, and this signaling pathway also converges on MYPT1 and actinomyosin.
34019870	9	21	theme	acid-induced	1425:1436	arg1	contraction					1438:1448	lysophosphatidic acid-induced contraction	1408:1448	lysophosphatidic acid-induced contraction in culture	1408:1459	Specifically, we found that O-GlcNAc levels control the sensitivity of mouse and primary human dermal fibroblasts to lysophosphatidic acid-induced contraction in culture and the phosphorylation of MLC and that MYPT1 O-GlcNAc modification is responsible.
34019870	2	22	dep	it	341:342	arg1	regulator					364:372	a potential dynamic regulator	344:372	it a potential dynamic regulator of cell signaling	341:390	O-GlcNAc is enzymatically added and removed from proteins, making it a potential dynamic regulator of cell signaling.
34019870	5	23	theme	O-GlcNAc	757:764	arg1	modification					766:777	O-GlcNAc modification	757:777	O-GlcNAc modification of the phosphatase MYPT1	757:802	Specifically, we found that O-GlcNAc modification of the phosphatase MYPT1 maintains its activity, resulting in dephosphorylation and deactivation of the myosin light chain of the actinomyosin complex.
34019870	1	24	theme	glycosylation	179:191	arg1	modification					193:204	a common glycosylation modification	170:204	a common glycosylation modification of serine and threonine residues	170:237	Thousands of proteins have been found to be modified by O-GlcNAc, a common glycosylation modification of serine and threonine residues throughout the cytosol and nucleus.
34019870	1	24	theme	glycosylation	179:191	arg1	O-GlcNAc					160:167	O-GlcNAc	160:167	O-GlcNAc	160:167	Thousands of proteins have been found to be modified by O-GlcNAc, a common glycosylation modification of serine and threonine residues throughout the cytosol and nucleus.
34019870	0	25	theme	O-GlcNAc	0:7	arg1	modification					9:20	O-GlcNAc modification	0:20	O-GlcNAc modification of MYPT1	0:29	O-GlcNAc modification of MYPT1 modulates lysophosphatidic acid-induced cell contraction in fibroblasts.
34019870	8	26	theme	small	1195:1199	arg1	inhibitors					1210:1219	small molecule inhibitors	1195:1219	small molecule inhibitors	1195:1219	Here, we used a combination of small molecule inhibitors, 2D and 3D cell cultures, and biochemistry to confirm our hypothesis.
34019870	9	27	from	contraction	1438:1448	arg1	culture					1453:1459	culture	1453:1459	culture	1453:1459	Specifically, we found that O-GlcNAc levels control the sensitivity of mouse and primary human dermal fibroblasts to lysophosphatidic acid-induced contraction in culture and the phosphorylation of MLC and that MYPT1 O-GlcNAc modification is responsible.
34019870	2	28	theme	signaling	382:390	arg1	regulator					364:372	a potential dynamic regulator	344:372	it a potential dynamic regulator of cell signaling	341:390	O-GlcNAc is enzymatically added and removed from proteins, making it a potential dynamic regulator of cell signaling.
34019870	0	29	theme	MYPT1	25:29	arg1	modification					9:20	O-GlcNAc modification	0:20	O-GlcNAc modification of MYPT1	0:29	O-GlcNAc modification of MYPT1 modulates lysophosphatidic acid-induced cell contraction in fibroblasts.
34019870	1	30	theme	proteins	117:124	arg1	Thousands					104:112	Thousands	104:112	Thousands of proteins	104:124	Thousands of proteins have been found to be modified by O-GlcNAc, a common glycosylation modification of serine and threonine residues throughout the cytosol and nucleus.
34019870	3	31	theme	O-GlcNAc-regulated	491:508	arg1	pathways					510:517	relatively few O-GlcNAc-regulated pathways	476:517	relatively few O-GlcNAc-regulated pathways	476:517	However, compared with other posttranslational modifications like phosphorylation, relatively few O-GlcNAc-regulated pathways have been discovered and biochemically characterized.
34019870	5	32	theme	actinomyosin	909:920	arg1	complex					922:928	the actinomyosin complex	905:928	the actinomyosin complex	905:928	Specifically, we found that O-GlcNAc modification of the phosphatase MYPT1 maintains its activity, resulting in dephosphorylation and deactivation of the myosin light chain of the actinomyosin complex.
34019870	2	33	attach	removed	311:317	arg2	O-GlcNAc					275:282	O-GlcNAc	275:282	O-GlcNAc	275:282	O-GlcNAc is enzymatically added and removed from proteins, making it a potential dynamic regulator of cell signaling.
34019870	2	33	attach	removed	311:317	arg1	proteins					324:331	proteins	324:331	proteins	324:331	O-GlcNAc is enzymatically added and removed from proteins, making it a potential dynamic regulator of cell signaling.
34019870	5	34	theme	phosphatase	786:796	arg1	MYPT1					798:802	the phosphatase MYPT1	782:802	the phosphatase MYPT1	782:802	Specifically, we found that O-GlcNAc modification of the phosphatase MYPT1 maintains its activity, resulting in dephosphorylation and deactivation of the myosin light chain of the actinomyosin complex.
34019870	10	35	theme	procontractile	1660:1673	arg1	stimuli					1675:1681	procontractile stimuli	1660:1681	procontractile stimuli	1660:1681	These findings further solidify the importance of O-GlcNAc in regulating the biology of fibroblasts in response to procontractile stimuli.
34019870	1	36	theme	serine	209:214	arg1	modification					193:204	a common glycosylation modification	170:204	a common glycosylation modification of serine and threonine residues	170:237	Thousands of proteins have been found to be modified by O-GlcNAc, a common glycosylation modification of serine and threonine residues throughout the cytosol and nucleus.
34019870	1	36	theme	serine	209:214	arg1	O-GlcNAc					160:167	O-GlcNAc	160:167	O-GlcNAc	160:167	Thousands of proteins have been found to be modified by O-GlcNAc, a common glycosylation modification of serine and threonine residues throughout the cytosol and nucleus.
34019870	0	37	theme	lysophosphatidic	41:56	arg1	contraction					76:86	lysophosphatidic acid-induced cell contraction	41:86	lysophosphatidic acid-induced cell contraction in fibroblasts	41:101	O-GlcNAc modification of MYPT1 modulates lysophosphatidic acid-induced cell contraction in fibroblasts.
34019870	5	38	theme	MYPT1	798:802	arg1	modification					766:777	O-GlcNAc modification	757:777	O-GlcNAc modification of the phosphatase MYPT1	757:802	Specifically, we found that O-GlcNAc modification of the phosphatase MYPT1 maintains its activity, resulting in dephosphorylation and deactivation of the myosin light chain of the actinomyosin complex.
34019870	1	39	dep	cytosol	254:260	arg1	the					250:252	the	250:252	the	250:252	Thousands of proteins have been found to be modified by O-GlcNAc, a common glycosylation modification of serine and threonine residues throughout the cytosol and nucleus.
34019870	3	40	theme	posttranslational	422:438	arg1	modifications					440:452	other posttranslational modifications	416:452	other posttranslational modifications like phosphorylation	416:473	However, compared with other posttranslational modifications like phosphorylation, relatively few O-GlcNAc-regulated pathways have been discovered and biochemically characterized.
34019870	10	41	theme	O-GlcNAc	1595:1602	arg1	importance					1581:1590	the importance	1577:1590	the importance of O-GlcNAc in regulating the biology of fibroblasts in response to procontractile stimuli	1577:1681	These findings further solidify the importance of O-GlcNAc in regulating the biology of fibroblasts in response to procontractile stimuli.
34019870	9	42	theme	O-GlcNAc	1319:1326	arg1	levels					1328:1333	O-GlcNAc levels	1319:1333	O-GlcNAc levels	1319:1333	Specifically, we found that O-GlcNAc levels control the sensitivity of mouse and primary human dermal fibroblasts to lysophosphatidic acid-induced contraction in culture and the phosphorylation of MLC and that MYPT1 O-GlcNAc modification is responsible.
34019870	8	43	used	used	1173:1176	arg2	we					1170:1171	we	1170:1171	we	1170:1171	Here, we used a combination of small molecule inhibitors, 2D and 3D cell cultures, and biochemistry to confirm our hypothesis.
34019870	1	44	theme	threonine	220:228	arg1	modification					193:204	a common glycosylation modification	170:204	a common glycosylation modification of serine and threonine residues	170:237	Thousands of proteins have been found to be modified by O-GlcNAc, a common glycosylation modification of serine and threonine residues throughout the cytosol and nucleus.
34019870	1	44	theme	threonine	220:228	arg1	O-GlcNAc					160:167	O-GlcNAc	160:167	O-GlcNAc	160:167	Thousands of proteins have been found to be modified by O-GlcNAc, a common glycosylation modification of serine and threonine residues throughout the cytosol and nucleus.
34019870	0	45	theme	cell	71:74	arg1	contraction					76:86	lysophosphatidic acid-induced cell contraction	41:86	lysophosphatidic acid-induced cell contraction in fibroblasts	41:101	O-GlcNAc modification of MYPT1 modulates lysophosphatidic acid-induced cell contraction in fibroblasts.
34019870	8	46	theme	molecule	1201:1208	arg1	inhibitors					1210:1219	small molecule inhibitors	1195:1219	small molecule inhibitors	1195:1219	Here, we used a combination of small molecule inhibitors, 2D and 3D cell cultures, and biochemistry to confirm our hypothesis.
34019870	0	47	from	contraction	76:86	arg1	fibroblasts					91:101	fibroblasts	91:101	fibroblasts	91:101	O-GlcNAc modification of MYPT1 modulates lysophosphatidic acid-induced cell contraction in fibroblasts.
34019870	1	48	mod	modification	193:204	arg1	serine					209:214	serine	209:214	serine	209:214	Thousands of proteins have been found to be modified by O-GlcNAc, a common glycosylation modification of serine and threonine residues throughout the cytosol and nucleus.
34019870	1	48	mod	modification	193:204	arg3	glycosylation					179:191	a common glycosylation modification	170:204	a common glycosylation modification of serine and threonine residues	170:237	Thousands of proteins have been found to be modified by O-GlcNAc, a common glycosylation modification of serine and threonine residues throughout the cytosol and nucleus.
34019870	1	48	mod	modification	193:204	arg1	threonine					220:228	threonine	220:228	threonine	220:228	Thousands of proteins have been found to be modified by O-GlcNAc, a common glycosylation modification of serine and threonine residues throughout the cytosol and nucleus.
34019870	0	49	theme	acid-induced	58:69	arg1	contraction					76:86	lysophosphatidic acid-induced cell contraction	41:86	lysophosphatidic acid-induced cell contraction in fibroblasts	41:101	O-GlcNAc modification of MYPT1 modulates lysophosphatidic acid-induced cell contraction in fibroblasts.
34019870	4	50	theme	such	602:605	arg1	pathway					607:613	one such pathway	598:613	one such pathway	598:613	We previously discovered one such pathway, where O-GlcNAc controls the contraction of fibroblasts initiated by the signaling lipid sphingosine-1-phosphate.
34019870	5	51	mod	modification	766:777	arg3	O-GlcNAc					757:764	O-GlcNAc modification	757:777	O-GlcNAc modification of the phosphatase MYPT1	757:802	Specifically, we found that O-GlcNAc modification of the phosphatase MYPT1 maintains its activity, resulting in dephosphorylation and deactivation of the myosin light chain of the actinomyosin complex.
34019870	5	51	mod	modification	766:777	arg1	MYPT1					798:802	the phosphatase MYPT1	782:802	the phosphatase MYPT1	782:802	Specifically, we found that O-GlcNAc modification of the phosphatase MYPT1 maintains its activity, resulting in dephosphorylation and deactivation of the myosin light chain of the actinomyosin complex.
34019870	6	52	theme	signaling	939:947	arg1	lipid					949:953	Another signaling lipid	931:953	Another signaling lipid that leads to contraction of fibroblasts	931:994	Another signaling lipid that leads to contraction of fibroblasts is lysophosphatidic acid, and this signaling pathway also converges on MYPT1 and actinomyosin.
34019870	9	53	theme	MLC	1488:1490	arg1	phosphorylation					1469:1483	the phosphorylation	1465:1483	the phosphorylation of MLC	1465:1490	Specifically, we found that O-GlcNAc levels control the sensitivity of mouse and primary human dermal fibroblasts to lysophosphatidic acid-induced contraction in culture and the phosphorylation of MLC and that MYPT1 O-GlcNAc modification is responsible.
34019870	9	53	theme	MLC	1488:1490	arg1	sensitivity					1347:1357	the sensitivity	1343:1357	the sensitivity of mouse and primary human dermal fibroblasts to lysophosphatidic acid-induced contraction in culture	1343:1459	Specifically, we found that O-GlcNAc levels control the sensitivity of mouse and primary human dermal fibroblasts to lysophosphatidic acid-induced contraction in culture and the phosphorylation of MLC and that MYPT1 O-GlcNAc modification is responsible.
34019870	8	54	theme	inhibitors	1210:1219	arg1	combination					1180:1190	a combination	1178:1190	a combination of small molecule inhibitors, 2D and 3D cell cultures, and biochemistry	1178:1262	Here, we used a combination of small molecule inhibitors, 2D and 3D cell cultures, and biochemistry to confirm our hypothesis.
34019870	4	55	theme	fibroblasts	659:669	arg1	contraction					644:654	the contraction	640:654	the contraction of fibroblasts initiated by the signaling lipid sphingosine-1-phosphate	640:726	We previously discovered one such pathway, where O-GlcNAc controls the contraction of fibroblasts initiated by the signaling lipid sphingosine-1-phosphate.
34019870	1	56	mod	modified	148:155	arg3	O-GlcNAc					160:167	O-GlcNAc	160:167	O-GlcNAc	160:167	Thousands of proteins have been found to be modified by O-GlcNAc, a common glycosylation modification of serine and threonine residues throughout the cytosol and nucleus.
34019870	1	56	mod	modified	148:155	arg1	Thousands					104:112	Thousands	104:112	Thousands of proteins	104:124	Thousands of proteins have been found to be modified by O-GlcNAc, a common glycosylation modification of serine and threonine residues throughout the cytosol and nucleus.
34019870	1	56	mod	modified	148:155	arg3	modification					193:204	a common glycosylation modification	170:204	a common glycosylation modification of serine and threonine residues	170:237	Thousands of proteins have been found to be modified by O-GlcNAc, a common glycosylation modification of serine and threonine residues throughout the cytosol and nucleus.
34019870	4	57	theme	lipid	698:702	arg1	sphingosine-1-phosphate					704:726	the signaling lipid sphingosine-1-phosphate	684:726	the signaling lipid sphingosine-1-phosphate	684:726	We previously discovered one such pathway, where O-GlcNAc controls the contraction of fibroblasts initiated by the signaling lipid sphingosine-1-phosphate.
34019870	2	58	theme	cell	377:380	arg1	signaling					382:390	cell signaling	377:390	cell signaling	377:390	O-GlcNAc is enzymatically added and removed from proteins, making it a potential dynamic regulator of cell signaling.
34019870	10	59	theme	fibroblasts	1633:1643	arg1	biology					1622:1628	the biology	1618:1628	the biology of fibroblasts	1618:1643	These findings further solidify the importance of O-GlcNAc in regulating the biology of fibroblasts in response to procontractile stimuli.
34019870	5	60	theme	myosin	883:888	arg1	chain					896:900	the myosin light chain	879:900	the myosin light chain of the actinomyosin complex	879:928	Specifically, we found that O-GlcNAc modification of the phosphatase MYPT1 maintains its activity, resulting in dephosphorylation and deactivation of the myosin light chain of the actinomyosin complex.
34019870	9	61	theme	mouse	1362:1366	arg1	fibroblasts					1393:1403	mouse and primary human dermal fibroblasts	1362:1403	fibroblasts	1393:1403	Specifically, we found that O-GlcNAc levels control the sensitivity of mouse and primary human dermal fibroblasts to lysophosphatidic acid-induced contraction in culture and the phosphorylation of MLC and that MYPT1 O-GlcNAc modification is responsible.
34019870	1	62	dep	serine	209:214	arg1	residues					230:237	residues	230:237	residues	230:237	Thousands of proteins have been found to be modified by O-GlcNAc, a common glycosylation modification of serine and threonine residues throughout the cytosol and nucleus.
34019870	9	63	theme	fibroblasts	1393:1403	arg1	phosphorylation					1469:1483	the phosphorylation	1465:1483	the phosphorylation of MLC	1465:1490	Specifically, we found that O-GlcNAc levels control the sensitivity of mouse and primary human dermal fibroblasts to lysophosphatidic acid-induced contraction in culture and the phosphorylation of MLC and that MYPT1 O-GlcNAc modification is responsible.
34019870	9	63	theme	fibroblasts	1393:1403	arg1	sensitivity					1347:1357	the sensitivity	1343:1357	the sensitivity of mouse and primary human dermal fibroblasts to lysophosphatidic acid-induced contraction in culture	1343:1459	Specifically, we found that O-GlcNAc levels control the sensitivity of mouse and primary human dermal fibroblasts to lysophosphatidic acid-induced contraction in culture and the phosphorylation of MLC and that MYPT1 O-GlcNAc modification is responsible.
34019870	9	64	theme	MYPT1	1501:1505	arg1	modification					1516:1527	MYPT1 O-GlcNAc modification	1501:1527	MYPT1 O-GlcNAc modification	1501:1527	Specifically, we found that O-GlcNAc levels control the sensitivity of mouse and primary human dermal fibroblasts to lysophosphatidic acid-induced contraction in culture and the phosphorylation of MLC and that MYPT1 O-GlcNAc modification is responsible.
23592772	8	0	theme	kinases	1221:1227	arg1	O-GlcNAcylated					1244:1257	O-GlcNAcylated	1244:1257	O-GlcNAcylated	1244:1257	The NF-κB p65 subunit and upstream kinases IKKα/IKKβ were O-GlcNAcylated in PDAC.
23592772	8	0	theme	kinases	1221:1227	arg1	IKKα/IKKβ					1229:1237	The NF-κB p65 subunit and upstream kinases IKKα/IKKβ	1186:1237	The NF-κB p65 subunit and upstream kinases IKKα/IKKβ	1186:1237	The NF-κB p65 subunit and upstream kinases IKKα/IKKβ were O-GlcNAcylated in PDAC.
23592772	6	1	theme	pancreatic	969:978	arg1	growth					996:1001	non-transformed pancreatic epithelial cell growth	953:1001	non-transformed pancreatic epithelial cell growth	953:1001	Reducing hyper-O-GlcNAcylation had no effect on non-transformed pancreatic epithelial cell growth, but inhibited PDAC cell proliferation, anchorage-independent growth, orthotopic tumor growth, and triggered apoptosis.
23592772	10	2	theme	OGA	1528:1530	arg1	inhibition					1514:1523	pharmacological inhibition	1498:1523	pharmacological inhibition of OGA	1498:1530	Conversely, mimicking PDAC hyper-O-GlcNAcylation through pharmacological inhibition of OGA suppressed suspension culture-induced apoptosis and increased IKKα and p65 O-GlcNAcylation, accompanied by activation of NF-κB signaling.
23592772	2	3	theme	increased	373:381	arg1	uptake					405:410	greatly increased glucose and glutamine uptake	365:410	greatly increased glucose and glutamine uptake	365:410	This necessitates greatly increased glucose and glutamine uptake, both of which enter the hexosamine biosynthetic pathway (HBP).
23592772	4	4	from	hyper-O-GlcNAcylation	712:732	arg1	PDAC					777:780	PDAC	777:780	PDAC	777:780	Here, we observed increased HBP flux and hyper-O-GlcNAcylation in human pancreatic ductal adenocarcinoma (PDAC).
23592772	4	4	from	hyper-O-GlcNAcylation	712:732	arg1	adenocarcinoma					761:774	human pancreatic ductal adenocarcinoma	737:774	human pancreatic ductal adenocarcinoma (PDAC)	737:781	Here, we observed increased HBP flux and hyper-O-GlcNAcylation in human pancreatic ductal adenocarcinoma (PDAC).
23592772	1	5	theme	Warburg	276:282	arg1	oxygen					268:273	oxygen	268:273	oxygen (Warburg effect)	268:290	Cancer cell metabolic reprogramming includes a shift in energy production from oxidative phosphorylation to less efficient glycolysis even in the presence of oxygen (Warburg effect) and use of glutamine for increased biosynthetic needs.
23592772	1	5	theme	Warburg	276:282	arg1	effect					284:289	Warburg effect	276:289	Warburg effect	276:289	Cancer cell metabolic reprogramming includes a shift in energy production from oxidative phosphorylation to less efficient glycolysis even in the presence of oxygen (Warburg effect) and use of glutamine for increased biosynthetic needs.
23592772	8	6	from	PDAC	1262:1265	arg1	O-GlcNAcylated					1244:1257	O-GlcNAcylated	1244:1257	O-GlcNAcylated	1244:1257	The NF-κB p65 subunit and upstream kinases IKKα/IKKβ were O-GlcNAcylated in PDAC.
23592772	8	6	from	PDAC	1262:1265	arg1	IKKα/IKKβ					1229:1237	The NF-κB p65 subunit and upstream kinases IKKα/IKKβ	1186:1237	The NF-κB p65 subunit and upstream kinases IKKα/IKKβ	1186:1237	The NF-κB p65 subunit and upstream kinases IKKα/IKKβ were O-GlcNAcylated in PDAC.
23592772	11	7	theme	growth	1834:1839	arg1	induction					1789:1797	the induction	1785:1797	the induction of PDAC cell anchorage-independent growth	1785:1839	Finally, reducing p65 O-GlcNAcylation specifically by mutating two p65 O-GlcNAc sites (T322A and T352A) attenuated the induction of PDAC cell anchorage-independent growth.
23592772	9	8	theme	Reducing	1268:1275	arg1	hyper-O-GlcNAcylation					1277:1297	Reducing hyper-O-GlcNAcylation	1268:1297	Reducing hyper-O-GlcNAcylation	1268:1297	Reducing hyper-O-GlcNAcylation decreased PDAC cell p65 activating phosphorylation (S536), nuclear translocation, NF-κB transcriptional activity, and target gene expression.
23592772	4	9	from	flux	703:706	arg1	PDAC					777:780	PDAC	777:780	PDAC	777:780	Here, we observed increased HBP flux and hyper-O-GlcNAcylation in human pancreatic ductal adenocarcinoma (PDAC).
23592772	4	9	from	flux	703:706	arg1	adenocarcinoma					761:774	human pancreatic ductal adenocarcinoma	737:774	human pancreatic ductal adenocarcinoma (PDAC)	737:781	Here, we observed increased HBP flux and hyper-O-GlcNAcylation in human pancreatic ductal adenocarcinoma (PDAC).
23592772	11	10	dep	sites	1750:1754	arg1	T352A					1767:1771	T352A	1767:1771	T352A	1767:1771	Finally, reducing p65 O-GlcNAcylation specifically by mutating two p65 O-GlcNAc sites (T322A and T352A) attenuated the induction of PDAC cell anchorage-independent growth.
23592772	11	10	dep	sites	1750:1754	arg1	T322A					1757:1761	T322A	1757:1761	T322A	1757:1761	Finally, reducing p65 O-GlcNAcylation specifically by mutating two p65 O-GlcNAc sites (T322A and T352A) attenuated the induction of PDAC cell anchorage-independent growth.
23592772	11	10	dep	sites	1750:1754	arg1	sites					1750:1754	two p65 O-GlcNAc sites	1733:1754	two p65 O-GlcNAc sites (T322A and T352A)	1733:1772	Finally, reducing p65 O-GlcNAcylation specifically by mutating two p65 O-GlcNAc sites (T322A and T352A) attenuated the induction of PDAC cell anchorage-independent growth.
23592772	4	11	theme	increased	689:697	arg1	flux					703:706	increased HBP flux	689:706	increased HBP flux	689:706	Here, we observed increased HBP flux and hyper-O-GlcNAcylation in human pancreatic ductal adenocarcinoma (PDAC).
23592772	11	12	theme	cell	1807:1810	arg1	growth					1834:1839	PDAC cell anchorage-independent growth	1802:1839	PDAC cell anchorage-independent growth	1802:1839	Finally, reducing p65 O-GlcNAcylation specifically by mutating two p65 O-GlcNAc sites (T322A and T352A) attenuated the induction of PDAC cell anchorage-independent growth.
23592772	3	13	theme	enzymatic	544:552	arg1	modification					573:584	enzymatic post-translational modification	544:584	enzymatic post-translational modification of many cytosolic and nuclear proteins by O-linked β-N-acetylglucosamine (O-GlcNAc)	544:668	The HBP end product UDP-N-acetylglucosamine (UDP-GlcNAc) is used in enzymatic post-translational modification of many cytosolic and nuclear proteins by O-linked β-N-acetylglucosamine (O-GlcNAc).
23592772	7	14	theme	NF-κB	1154:1158	arg1	activity					1176:1183	oncogenic NF-κB transcriptional activity	1144:1183	oncogenic NF-κB transcriptional activity	1144:1183	PDAC is supported by oncogenic NF-κB transcriptional activity.
23592772	9	15	theme	cell	1314:1317	arg1	S536					1351:1354	S536	1351:1354	S536	1351:1354	Reducing hyper-O-GlcNAcylation decreased PDAC cell p65 activating phosphorylation (S536), nuclear translocation, NF-κB transcriptional activity, and target gene expression.
23592772	9	15	theme	cell	1314:1317	arg1	phosphorylation					1334:1348	PDAC cell p65 activating phosphorylation	1309:1348	PDAC cell p65 activating phosphorylation (S536)	1309:1355	Reducing hyper-O-GlcNAcylation decreased PDAC cell p65 activating phosphorylation (S536), nuclear translocation, NF-κB transcriptional activity, and target gene expression.
23592772	6	16	theme	cell	1023:1026	arg1	proliferation					1028:1040	PDAC cell proliferation	1018:1040	PDAC cell proliferation	1018:1040	Reducing hyper-O-GlcNAcylation had no effect on non-transformed pancreatic epithelial cell growth, but inhibited PDAC cell proliferation, anchorage-independent growth, orthotopic tumor growth, and triggered apoptosis.
23592772	12	17	theme	NF-κB	1924:1928	arg1	activation					1940:1949	NF-κB oncogenic activation	1924:1949	NF-κB oncogenic activation in PDAC	1924:1957	Our data indicate that hyper-O-GlcNAcylation is anti-apoptotic and contributes to NF-κB oncogenic activation in PDAC.
23592772	9	18	theme	activating	1323:1332	arg1	S536					1351:1354	S536	1351:1354	S536	1351:1354	Reducing hyper-O-GlcNAcylation decreased PDAC cell p65 activating phosphorylation (S536), nuclear translocation, NF-κB transcriptional activity, and target gene expression.
23592772	9	18	theme	activating	1323:1332	arg1	phosphorylation					1334:1348	PDAC cell p65 activating phosphorylation	1309:1348	PDAC cell p65 activating phosphorylation (S536)	1309:1355	Reducing hyper-O-GlcNAcylation decreased PDAC cell p65 activating phosphorylation (S536), nuclear translocation, NF-κB transcriptional activity, and target gene expression.
23592772	3	19	theme	many	589:592	arg1	proteins					616:623	many cytosolic and nuclear proteins	589:623	many cytosolic and nuclear proteins	589:623	The HBP end product UDP-N-acetylglucosamine (UDP-GlcNAc) is used in enzymatic post-translational modification of many cytosolic and nuclear proteins by O-linked β-N-acetylglucosamine (O-GlcNAc).
23592772	1	20	dep	oxygen	268:273	arg1	the					252:254	the	252:254	the	252:254	Cancer cell metabolic reprogramming includes a shift in energy production from oxidative phosphorylation to less efficient glycolysis even in the presence of oxygen (Warburg effect) and use of glutamine for increased biosynthetic needs.
23592772	1	20	dep	oxygen	268:273	arg1	presence					256:263	presence	256:263	presence	256:263	Cancer cell metabolic reprogramming includes a shift in energy production from oxidative phosphorylation to less efficient glycolysis even in the presence of oxygen (Warburg effect) and use of glutamine for increased biosynthetic needs.
23592772	3	21	theme	O-linked	628:635	arg1	O-GlcNAc					660:667	O-GlcNAc	660:667	O-GlcNAc	660:667	The HBP end product UDP-N-acetylglucosamine (UDP-GlcNAc) is used in enzymatic post-translational modification of many cytosolic and nuclear proteins by O-linked β-N-acetylglucosamine (O-GlcNAc).
23592772	3	21	theme	O-linked	628:635	arg1	β-N-acetylglucosamine					637:657	O-linked β-N-acetylglucosamine	628:657	O-linked β-N-acetylglucosamine (O-GlcNAc)	628:668	The HBP end product UDP-N-acetylglucosamine (UDP-GlcNAc) is used in enzymatic post-translational modification of many cytosolic and nuclear proteins by O-linked β-N-acetylglucosamine (O-GlcNAc).
23592772	4	22	theme	ductal	754:759	arg1	PDAC					777:780	PDAC	777:780	PDAC	777:780	Here, we observed increased HBP flux and hyper-O-GlcNAcylation in human pancreatic ductal adenocarcinoma (PDAC).
23592772	4	22	theme	ductal	754:759	arg1	adenocarcinoma					761:774	human pancreatic ductal adenocarcinoma	737:774	human pancreatic ductal adenocarcinoma (PDAC)	737:781	Here, we observed increased HBP flux and hyper-O-GlcNAcylation in human pancreatic ductal adenocarcinoma (PDAC).
23592772	3	23	theme	proteins	616:623	arg1	modification					573:584	enzymatic post-translational modification	544:584	enzymatic post-translational modification of many cytosolic and nuclear proteins by O-linked β-N-acetylglucosamine (O-GlcNAc)	544:668	The HBP end product UDP-N-acetylglucosamine (UDP-GlcNAc) is used in enzymatic post-translational modification of many cytosolic and nuclear proteins by O-linked β-N-acetylglucosamine (O-GlcNAc).
23592772	6	24	theme	cell	991:994	arg1	growth					996:1001	non-transformed pancreatic epithelial cell growth	953:1001	non-transformed pancreatic epithelial cell growth	953:1001	Reducing hyper-O-GlcNAcylation had no effect on non-transformed pancreatic epithelial cell growth, but inhibited PDAC cell proliferation, anchorage-independent growth, orthotopic tumor growth, and triggered apoptosis.
23592772	9	25	theme	nuclear	1358:1364	arg1	translocation					1366:1378	nuclear translocation	1358:1378	nuclear translocation	1358:1378	Reducing hyper-O-GlcNAcylation decreased PDAC cell p65 activating phosphorylation (S536), nuclear translocation, NF-κB transcriptional activity, and target gene expression.
23592772	1	26	theme	energy	166:171	arg1	production					173:182	energy production	166:182	energy production	166:182	Cancer cell metabolic reprogramming includes a shift in energy production from oxidative phosphorylation to less efficient glycolysis even in the presence of oxygen (Warburg effect) and use of glutamine for increased biosynthetic needs.
23592772	6	27	theme	orthotopic	1073:1082	arg1	growth					1090:1095	orthotopic tumor growth	1073:1095	orthotopic tumor growth	1073:1095	Reducing hyper-O-GlcNAcylation had no effect on non-transformed pancreatic epithelial cell growth, but inhibited PDAC cell proliferation, anchorage-independent growth, orthotopic tumor growth, and triggered apoptosis.
23592772	4	28	theme	human	737:741	arg1	PDAC					777:780	PDAC	777:780	PDAC	777:780	Here, we observed increased HBP flux and hyper-O-GlcNAcylation in human pancreatic ductal adenocarcinoma (PDAC).
23592772	4	28	theme	human	737:741	arg1	adenocarcinoma					761:774	human pancreatic ductal adenocarcinoma	737:774	human pancreatic ductal adenocarcinoma (PDAC)	737:781	Here, we observed increased HBP flux and hyper-O-GlcNAcylation in human pancreatic ductal adenocarcinoma (PDAC).
23592772	0	29	theme	cancer	96:101	arg1	cells					103:107	pancreatic cancer cells	85:107	pancreatic cancer cells	85:107	Hyper-O-GlcNAcylation is anti-apoptotic and maintains constitutive NF-κB activity in pancreatic cancer cells.
23592772	9	30	theme	transcriptional	1387:1401	arg1	activity					1403:1410	NF-κB transcriptional activity	1381:1410	NF-κB transcriptional activity	1381:1410	Reducing hyper-O-GlcNAcylation decreased PDAC cell p65 activating phosphorylation (S536), nuclear translocation, NF-κB transcriptional activity, and target gene expression.
23592772	11	31	theme	reducing	1679:1686	arg1	O-GlcNAcylation					1692:1706	reducing p65 O-GlcNAcylation	1679:1706	reducing p65 O-GlcNAcylation specifically by mutating two p65 O-GlcNAc sites (T322A and T352A)	1679:1772	Finally, reducing p65 O-GlcNAcylation specifically by mutating two p65 O-GlcNAc sites (T322A and T352A) attenuated the induction of PDAC cell anchorage-independent growth.
23592772	3	32	dep	product	488:494	arg1	UDP-N-acetylglucosamine					496:518	UDP-N-acetylglucosamine	496:518	The HBP end product UDP-N-acetylglucosamine (UDP-GlcNAc)	476:531	The HBP end product UDP-N-acetylglucosamine (UDP-GlcNAc) is used in enzymatic post-translational modification of many cytosolic and nuclear proteins by O-linked β-N-acetylglucosamine (O-GlcNAc).
23592772	3	32	dep	product	488:494	arg1	UDP-GlcNAc					521:530	UDP-GlcNAc	521:530	UDP-GlcNAc	521:530	The HBP end product UDP-N-acetylglucosamine (UDP-GlcNAc) is used in enzymatic post-translational modification of many cytosolic and nuclear proteins by O-linked β-N-acetylglucosamine (O-GlcNAc).
23592772	5	33	theme	PDAC	784:787	arg1	hyper-O-GlcNAcylation					789:809	PDAC hyper-O-GlcNAcylation	784:809	PDAC hyper-O-GlcNAcylation	784:809	PDAC hyper-O-GlcNAcylation was associated with elevation of OGT and reduction of the enzyme that removes O-GlcNAc (OGA).
23592772	9	34	theme	target	1417:1422	arg1	expression					1429:1438	target gene expression	1417:1438	target gene expression	1417:1438	Reducing hyper-O-GlcNAcylation decreased PDAC cell p65 activating phosphorylation (S536), nuclear translocation, NF-κB transcriptional activity, and target gene expression.
23592772	1	35	theme	Cancer	110:115	arg1	reprogramming					132:144	Cancer cell metabolic reprogramming	110:144	Cancer cell metabolic reprogramming	110:144	Cancer cell metabolic reprogramming includes a shift in energy production from oxidative phosphorylation to less efficient glycolysis even in the presence of oxygen (Warburg effect) and use of glutamine for increased biosynthetic needs.
23592772	12	36	from	activation	1940:1949	arg1	PDAC					1954:1957	PDAC	1954:1957	PDAC	1954:1957	Our data indicate that hyper-O-GlcNAcylation is anti-apoptotic and contributes to NF-κB oncogenic activation in PDAC.
23592772	10	37	theme	NF-κB	1653:1657	arg1	signaling					1659:1667	NF-κB signaling	1653:1667	NF-κB signaling	1653:1667	Conversely, mimicking PDAC hyper-O-GlcNAcylation through pharmacological inhibition of OGA suppressed suspension culture-induced apoptosis and increased IKKα and p65 O-GlcNAcylation, accompanied by activation of NF-κB signaling.
23592772	11	38	theme	p65	1688:1690	arg1	O-GlcNAcylation					1692:1706	reducing p65 O-GlcNAcylation	1679:1706	reducing p65 O-GlcNAcylation specifically by mutating two p65 O-GlcNAc sites (T322A and T352A)	1679:1772	Finally, reducing p65 O-GlcNAcylation specifically by mutating two p65 O-GlcNAc sites (T322A and T352A) attenuated the induction of PDAC cell anchorage-independent growth.
23592772	2	39	theme	hexosamine	437:446	arg1	HBP					470:472	HBP	470:472	HBP	470:472	This necessitates greatly increased glucose and glutamine uptake, both of which enter the hexosamine biosynthetic pathway (HBP).
23592772	2	39	theme	hexosamine	437:446	arg1	pathway					461:467	the hexosamine biosynthetic pathway	433:467	the hexosamine biosynthetic pathway (HBP)	433:473	This necessitates greatly increased glucose and glutamine uptake, both of which enter the hexosamine biosynthetic pathway (HBP).
23592772	5	40	theme	enzyme	869:874	arg1	elevation					831:839	elevation	831:839	elevation of OGT	831:846	PDAC hyper-O-GlcNAcylation was associated with elevation of OGT and reduction of the enzyme that removes O-GlcNAc (OGA).
23592772	5	40	theme	enzyme	869:874	arg1	reduction					852:860	reduction	852:860	reduction of the enzyme that removes O-GlcNAc (OGA)	852:902	PDAC hyper-O-GlcNAcylation was associated with elevation of OGT and reduction of the enzyme that removes O-GlcNAc (OGA).
23592772	6	41	theme	Reducing	905:912	arg1	hyper-O-GlcNAcylation					914:934	Reducing hyper-O-GlcNAcylation	905:934	Reducing hyper-O-GlcNAcylation	905:934	Reducing hyper-O-GlcNAcylation had no effect on non-transformed pancreatic epithelial cell growth, but inhibited PDAC cell proliferation, anchorage-independent growth, orthotopic tumor growth, and triggered apoptosis.
23592772	1	42	theme	metabolic	122:130	arg1	reprogramming					132:144	Cancer cell metabolic reprogramming	110:144	Cancer cell metabolic reprogramming	110:144	Cancer cell metabolic reprogramming includes a shift in energy production from oxidative phosphorylation to less efficient glycolysis even in the presence of oxygen (Warburg effect) and use of glutamine for increased biosynthetic needs.
23592772	10	43	dep	IKKα	1594:1597	arg1	O-GlcNAcylation					1607:1621	O-GlcNAcylation	1607:1621	O-GlcNAcylation	1607:1621	Conversely, mimicking PDAC hyper-O-GlcNAcylation through pharmacological inhibition of OGA suppressed suspension culture-induced apoptosis and increased IKKα and p65 O-GlcNAcylation, accompanied by activation of NF-κB signaling.
23592772	3	44	theme	end	484:486	arg1	product					488:494	The HBP end product UDP-N-acetylglucosamine (UDP-GlcNAc)	476:531	The HBP end product UDP-N-acetylglucosamine (UDP-GlcNAc)	476:531	The HBP end product UDP-N-acetylglucosamine (UDP-GlcNAc) is used in enzymatic post-translational modification of many cytosolic and nuclear proteins by O-linked β-N-acetylglucosamine (O-GlcNAc).
23592772	8	45	theme	NF-κB	1190:1194	arg1	subunit					1200:1206	NF-κB p65 subunit	1190:1206	NF-κB p65 subunit	1190:1206	The NF-κB p65 subunit and upstream kinases IKKα/IKKβ were O-GlcNAcylated in PDAC.
23592772	3	46	used	used	536:539	arg2	product					488:494	The HBP end product UDP-N-acetylglucosamine (UDP-GlcNAc)	476:531	The HBP end product UDP-N-acetylglucosamine (UDP-GlcNAc)	476:531	The HBP end product UDP-N-acetylglucosamine (UDP-GlcNAc) is used in enzymatic post-translational modification of many cytosolic and nuclear proteins by O-linked β-N-acetylglucosamine (O-GlcNAc).
23592772	2	47	theme	glutamine	395:403	arg1	uptake					405:410	greatly increased glucose and glutamine uptake	365:410	greatly increased glucose and glutamine uptake	365:410	This necessitates greatly increased glucose and glutamine uptake, both of which enter the hexosamine biosynthetic pathway (HBP).
23592772	8	48	theme	subunit	1200:1206	arg1	O-GlcNAcylated					1244:1257	O-GlcNAcylated	1244:1257	O-GlcNAcylated	1244:1257	The NF-κB p65 subunit and upstream kinases IKKα/IKKβ were O-GlcNAcylated in PDAC.
23592772	8	48	theme	subunit	1200:1206	arg1	IKKα/IKKβ					1229:1237	The NF-κB p65 subunit and upstream kinases IKKα/IKKβ	1186:1237	The NF-κB p65 subunit and upstream kinases IKKα/IKKβ	1186:1237	The NF-κB p65 subunit and upstream kinases IKKα/IKKβ were O-GlcNAcylated in PDAC.
23592772	6	49	theme	epithelial	980:989	arg1	growth					996:1001	non-transformed pancreatic epithelial cell growth	953:1001	non-transformed pancreatic epithelial cell growth	953:1001	Reducing hyper-O-GlcNAcylation had no effect on non-transformed pancreatic epithelial cell growth, but inhibited PDAC cell proliferation, anchorage-independent growth, orthotopic tumor growth, and triggered apoptosis.
23592772	11	50	theme	PDAC	1802:1805	arg1	growth					1834:1839	PDAC cell anchorage-independent growth	1802:1839	PDAC cell anchorage-independent growth	1802:1839	Finally, reducing p65 O-GlcNAcylation specifically by mutating two p65 O-GlcNAc sites (T322A and T352A) attenuated the induction of PDAC cell anchorage-independent growth.
23592772	2	51	theme	glucose	383:389	arg1	uptake					405:410	greatly increased glucose and glutamine uptake	365:410	greatly increased glucose and glutamine uptake	365:410	This necessitates greatly increased glucose and glutamine uptake, both of which enter the hexosamine biosynthetic pathway (HBP).
23592772	8	52	theme	upstream	1212:1219	arg1	kinases					1221:1227	upstream kinases	1212:1227	upstream kinases	1212:1227	The NF-κB p65 subunit and upstream kinases IKKα/IKKβ were O-GlcNAcylated in PDAC.
23592772	6	53	theme	non-transformed	953:967	arg1	growth					996:1001	non-transformed pancreatic epithelial cell growth	953:1001	non-transformed pancreatic epithelial cell growth	953:1001	Reducing hyper-O-GlcNAcylation had no effect on non-transformed pancreatic epithelial cell growth, but inhibited PDAC cell proliferation, anchorage-independent growth, orthotopic tumor growth, and triggered apoptosis.
23592772	9	54	theme	PDAC	1309:1312	arg1	S536					1351:1354	S536	1351:1354	S536	1351:1354	Reducing hyper-O-GlcNAcylation decreased PDAC cell p65 activating phosphorylation (S536), nuclear translocation, NF-κB transcriptional activity, and target gene expression.
23592772	9	54	theme	PDAC	1309:1312	arg1	phosphorylation					1334:1348	PDAC cell p65 activating phosphorylation	1309:1348	PDAC cell p65 activating phosphorylation (S536)	1309:1355	Reducing hyper-O-GlcNAcylation decreased PDAC cell p65 activating phosphorylation (S536), nuclear translocation, NF-κB transcriptional activity, and target gene expression.
23592772	3	55	theme	post-translational	554:571	arg1	modification					573:584	enzymatic post-translational modification	544:584	enzymatic post-translational modification of many cytosolic and nuclear proteins by O-linked β-N-acetylglucosamine (O-GlcNAc)	544:668	The HBP end product UDP-N-acetylglucosamine (UDP-GlcNAc) is used in enzymatic post-translational modification of many cytosolic and nuclear proteins by O-linked β-N-acetylglucosamine (O-GlcNAc).
23592772	7	56	theme	transcriptional	1160:1174	arg1	activity					1176:1183	oncogenic NF-κB transcriptional activity	1144:1183	oncogenic NF-κB transcriptional activity	1144:1183	PDAC is supported by oncogenic NF-κB transcriptional activity.
23592772	10	57	theme	pharmacological	1498:1512	arg1	inhibition					1514:1523	pharmacological inhibition	1498:1523	pharmacological inhibition of OGA	1498:1530	Conversely, mimicking PDAC hyper-O-GlcNAcylation through pharmacological inhibition of OGA suppressed suspension culture-induced apoptosis and increased IKKα and p65 O-GlcNAcylation, accompanied by activation of NF-κB signaling.
23592772	1	58	theme	oxidative	189:197	arg1	phosphorylation					199:213	oxidative phosphorylation	189:213	oxidative phosphorylation	189:213	Cancer cell metabolic reprogramming includes a shift in energy production from oxidative phosphorylation to less efficient glycolysis even in the presence of oxygen (Warburg effect) and use of glutamine for increased biosynthetic needs.
23592772	0	59	theme	NF-κB	67:71	arg1	activity					73:80	constitutive NF-κB activity	54:80	constitutive NF-κB activity in pancreatic cancer cells	54:107	Hyper-O-GlcNAcylation is anti-apoptotic and maintains constitutive NF-κB activity in pancreatic cancer cells.
23592772	11	60	theme	p65	1737:1739	arg1	T352A					1767:1771	T352A	1767:1771	T352A	1767:1771	Finally, reducing p65 O-GlcNAcylation specifically by mutating two p65 O-GlcNAc sites (T322A and T352A) attenuated the induction of PDAC cell anchorage-independent growth.
23592772	11	60	theme	p65	1737:1739	arg1	T322A					1757:1761	T322A	1757:1761	T322A	1757:1761	Finally, reducing p65 O-GlcNAcylation specifically by mutating two p65 O-GlcNAc sites (T322A and T352A) attenuated the induction of PDAC cell anchorage-independent growth.
23592772	11	60	theme	p65	1737:1739	arg1	sites					1750:1754	two p65 O-GlcNAc sites	1733:1754	two p65 O-GlcNAc sites (T322A and T352A)	1733:1772	Finally, reducing p65 O-GlcNAcylation specifically by mutating two p65 O-GlcNAc sites (T322A and T352A) attenuated the induction of PDAC cell anchorage-independent growth.
23592772	11	61	theme	anchorage-independent	1812:1832	arg1	growth					1834:1839	PDAC cell anchorage-independent growth	1802:1839	PDAC cell anchorage-independent growth	1802:1839	Finally, reducing p65 O-GlcNAcylation specifically by mutating two p65 O-GlcNAc sites (T322A and T352A) attenuated the induction of PDAC cell anchorage-independent growth.
23592772	7	62	theme	oncogenic	1144:1152	arg1	activity					1176:1183	oncogenic NF-κB transcriptional activity	1144:1183	oncogenic NF-κB transcriptional activity	1144:1183	PDAC is supported by oncogenic NF-κB transcriptional activity.
23592772	10	63	theme	culture-induced	1554:1568	arg1	apoptosis					1570:1578	suspension culture-induced apoptosis	1543:1578	suspension culture-induced apoptosis	1543:1578	Conversely, mimicking PDAC hyper-O-GlcNAcylation through pharmacological inhibition of OGA suppressed suspension culture-induced apoptosis and increased IKKα and p65 O-GlcNAcylation, accompanied by activation of NF-κB signaling.
23592772	3	64	theme	cytosolic	594:602	arg1	proteins					616:623	many cytosolic and nuclear proteins	589:623	many cytosolic and nuclear proteins	589:623	The HBP end product UDP-N-acetylglucosamine (UDP-GlcNAc) is used in enzymatic post-translational modification of many cytosolic and nuclear proteins by O-linked β-N-acetylglucosamine (O-GlcNAc).
23592772	12	65	theme	oncogenic	1930:1938	arg1	activation					1940:1949	NF-κB oncogenic activation	1924:1949	NF-κB oncogenic activation in PDAC	1924:1957	Our data indicate that hyper-O-GlcNAcylation is anti-apoptotic and contributes to NF-κB oncogenic activation in PDAC.
23592772	4	66	theme	HBP	699:701	arg1	flux					703:706	increased HBP flux	689:706	increased HBP flux	689:706	Here, we observed increased HBP flux and hyper-O-GlcNAcylation in human pancreatic ductal adenocarcinoma (PDAC).
23592772	10	67	theme	suspension	1543:1552	arg1	apoptosis					1570:1578	suspension culture-induced apoptosis	1543:1578	suspension culture-induced apoptosis	1543:1578	Conversely, mimicking PDAC hyper-O-GlcNAcylation through pharmacological inhibition of OGA suppressed suspension culture-induced apoptosis and increased IKKα and p65 O-GlcNAcylation, accompanied by activation of NF-κB signaling.
23592772	9	68	theme	p65	1319:1321	arg1	S536					1351:1354	S536	1351:1354	S536	1351:1354	Reducing hyper-O-GlcNAcylation decreased PDAC cell p65 activating phosphorylation (S536), nuclear translocation, NF-κB transcriptional activity, and target gene expression.
23592772	9	68	theme	p65	1319:1321	arg1	phosphorylation					1334:1348	PDAC cell p65 activating phosphorylation	1309:1348	PDAC cell p65 activating phosphorylation (S536)	1309:1355	Reducing hyper-O-GlcNAcylation decreased PDAC cell p65 activating phosphorylation (S536), nuclear translocation, NF-κB transcriptional activity, and target gene expression.
23592772	1	69	theme	efficient	223:231	arg1	glycolysis					233:242	less efficient glycolysis	218:242	less efficient glycolysis	218:242	Cancer cell metabolic reprogramming includes a shift in energy production from oxidative phosphorylation to less efficient glycolysis even in the presence of oxygen (Warburg effect) and use of glutamine for increased biosynthetic needs.
23592772	6	70	theme	PDAC	1018:1021	arg1	proliferation					1028:1040	PDAC cell proliferation	1018:1040	PDAC cell proliferation	1018:1040	Reducing hyper-O-GlcNAcylation had no effect on non-transformed pancreatic epithelial cell growth, but inhibited PDAC cell proliferation, anchorage-independent growth, orthotopic tumor growth, and triggered apoptosis.
23592772	6	71	contain	had	936:938	arg1	hyper-O-GlcNAcylation					914:934	Reducing hyper-O-GlcNAcylation	905:934	Reducing hyper-O-GlcNAcylation	905:934	Reducing hyper-O-GlcNAcylation had no effect on non-transformed pancreatic epithelial cell growth, but inhibited PDAC cell proliferation, anchorage-independent growth, orthotopic tumor growth, and triggered apoptosis.
23592772	6	71	contain	had	936:938	arg2	effect					943:948	no effect	940:948	no effect	940:948	Reducing hyper-O-GlcNAcylation had no effect on non-transformed pancreatic epithelial cell growth, but inhibited PDAC cell proliferation, anchorage-independent growth, orthotopic tumor growth, and triggered apoptosis.
23592772	3	72	theme	nuclear	608:614	arg1	proteins					616:623	many cytosolic and nuclear proteins	589:623	many cytosolic and nuclear proteins	589:623	The HBP end product UDP-N-acetylglucosamine (UDP-GlcNAc) is used in enzymatic post-translational modification of many cytosolic and nuclear proteins by O-linked β-N-acetylglucosamine (O-GlcNAc).
23592772	4	73	theme	pancreatic	743:752	arg1	PDAC					777:780	PDAC	777:780	PDAC	777:780	Here, we observed increased HBP flux and hyper-O-GlcNAcylation in human pancreatic ductal adenocarcinoma (PDAC).
23592772	4	73	theme	pancreatic	743:752	arg1	adenocarcinoma					761:774	human pancreatic ductal adenocarcinoma	737:774	human pancreatic ductal adenocarcinoma (PDAC)	737:781	Here, we observed increased HBP flux and hyper-O-GlcNAcylation in human pancreatic ductal adenocarcinoma (PDAC).
23592772	0	74	theme	pancreatic	85:94	arg1	cells					103:107	pancreatic cancer cells	85:107	pancreatic cancer cells	85:107	Hyper-O-GlcNAcylation is anti-apoptotic and maintains constitutive NF-κB activity in pancreatic cancer cells.
23592772	6	75	theme	tumor	1084:1088	arg1	growth					1090:1095	orthotopic tumor growth	1073:1095	orthotopic tumor growth	1073:1095	Reducing hyper-O-GlcNAcylation had no effect on non-transformed pancreatic epithelial cell growth, but inhibited PDAC cell proliferation, anchorage-independent growth, orthotopic tumor growth, and triggered apoptosis.
23592772	9	76	theme	NF-κB	1381:1385	arg1	activity					1403:1410	NF-κB transcriptional activity	1381:1410	NF-κB transcriptional activity	1381:1410	Reducing hyper-O-GlcNAcylation decreased PDAC cell p65 activating phosphorylation (S536), nuclear translocation, NF-κB transcriptional activity, and target gene expression.
23592772	1	77	from	phosphorylation	199:213	arg1	shift					157:161	a shift	155:161	a shift in energy production from oxidative phosphorylation to less efficient glycolysis	155:242	Cancer cell metabolic reprogramming includes a shift in energy production from oxidative phosphorylation to less efficient glycolysis even in the presence of oxygen (Warburg effect) and use of glutamine for increased biosynthetic needs.
23592772	1	78	dep	biosynthetic	327:338	arg1	needs					340:344	needs	340:344	needs	340:344	Cancer cell metabolic reprogramming includes a shift in energy production from oxidative phosphorylation to less efficient glycolysis even in the presence of oxygen (Warburg effect) and use of glutamine for increased biosynthetic needs.
23592772	6	79	theme	anchorage-independent	1043:1063	arg1	growth					1065:1070	anchorage-independent growth	1043:1070	anchorage-independent growth	1043:1070	Reducing hyper-O-GlcNAcylation had no effect on non-transformed pancreatic epithelial cell growth, but inhibited PDAC cell proliferation, anchorage-independent growth, orthotopic tumor growth, and triggered apoptosis.
23592772	0	80	from	activity	73:80	arg1	cells					103:107	pancreatic cancer cells	85:107	pancreatic cancer cells	85:107	Hyper-O-GlcNAcylation is anti-apoptotic and maintains constitutive NF-κB activity in pancreatic cancer cells.
23592772	9	81	theme	gene	1424:1427	arg1	expression					1429:1438	target gene expression	1417:1438	target gene expression	1417:1438	Reducing hyper-O-GlcNAcylation decreased PDAC cell p65 activating phosphorylation (S536), nuclear translocation, NF-κB transcriptional activity, and target gene expression.
23592772	1	82	from	shift	157:161	arg1	production					173:182	energy production	166:182	energy production	166:182	Cancer cell metabolic reprogramming includes a shift in energy production from oxidative phosphorylation to less efficient glycolysis even in the presence of oxygen (Warburg effect) and use of glutamine for increased biosynthetic needs.
23592772	1	83	theme	cell	117:120	arg1	reprogramming					132:144	Cancer cell metabolic reprogramming	110:144	Cancer cell metabolic reprogramming	110:144	Cancer cell metabolic reprogramming includes a shift in energy production from oxidative phosphorylation to less efficient glycolysis even in the presence of oxygen (Warburg effect) and use of glutamine for increased biosynthetic needs.
23592772	2	84	theme	biosynthetic	448:459	arg1	HBP					470:472	HBP	470:472	HBP	470:472	This necessitates greatly increased glucose and glutamine uptake, both of which enter the hexosamine biosynthetic pathway (HBP).
23592772	2	84	theme	biosynthetic	448:459	arg1	pathway					461:467	the hexosamine biosynthetic pathway	433:467	the hexosamine biosynthetic pathway (HBP)	433:473	This necessitates greatly increased glucose and glutamine uptake, both of which enter the hexosamine biosynthetic pathway (HBP).
23592772	3	85	theme	HBP	480:482	arg1	product					488:494	The HBP end product UDP-N-acetylglucosamine (UDP-GlcNAc)	476:531	The HBP end product UDP-N-acetylglucosamine (UDP-GlcNAc)	476:531	The HBP end product UDP-N-acetylglucosamine (UDP-GlcNAc) is used in enzymatic post-translational modification of many cytosolic and nuclear proteins by O-linked β-N-acetylglucosamine (O-GlcNAc).
23592772	0	86	theme	constitutive	54:65	arg1	activity					73:80	constitutive NF-κB activity	54:80	constitutive NF-κB activity in pancreatic cancer cells	54:107	Hyper-O-GlcNAcylation is anti-apoptotic and maintains constitutive NF-κB activity in pancreatic cancer cells.
23592772	1	87	theme	glutamine	303:311	arg1	oxygen					268:273	oxygen	268:273	oxygen (Warburg effect)	268:290	Cancer cell metabolic reprogramming includes a shift in energy production from oxidative phosphorylation to less efficient glycolysis even in the presence of oxygen (Warburg effect) and use of glutamine for increased biosynthetic needs.
23592772	1	87	theme	glutamine	303:311	arg1	effect					284:289	Warburg effect	276:289	Warburg effect	276:289	Cancer cell metabolic reprogramming includes a shift in energy production from oxidative phosphorylation to less efficient glycolysis even in the presence of oxygen (Warburg effect) and use of glutamine for increased biosynthetic needs.
23592772	1	87	theme	glutamine	303:311	arg1	use					296:298	use	296:298	use of glutamine for increased biosynthetic needs	296:344	Cancer cell metabolic reprogramming includes a shift in energy production from oxidative phosphorylation to less efficient glycolysis even in the presence of oxygen (Warburg effect) and use of glutamine for increased biosynthetic needs.
23592772	6	88	theme	triggered	1102:1110	arg1	apoptosis					1112:1120	triggered apoptosis	1102:1120	triggered apoptosis	1102:1120	Reducing hyper-O-GlcNAcylation had no effect on non-transformed pancreatic epithelial cell growth, but inhibited PDAC cell proliferation, anchorage-independent growth, orthotopic tumor growth, and triggered apoptosis.
23592772	5	89	theme	OGT	844:846	arg1	elevation					831:839	elevation	831:839	elevation of OGT	831:846	PDAC hyper-O-GlcNAcylation was associated with elevation of OGT and reduction of the enzyme that removes O-GlcNAc (OGA).
23592772	5	89	theme	OGT	844:846	arg1	reduction					852:860	reduction	852:860	reduction of the enzyme that removes O-GlcNAc (OGA)	852:902	PDAC hyper-O-GlcNAcylation was associated with elevation of OGT and reduction of the enzyme that removes O-GlcNAc (OGA).
23592772	3	90	link	O-linked	628:635	arg1	O-GlcNAc					660:667	O-GlcNAc	660:667	O-GlcNAc	660:667	The HBP end product UDP-N-acetylglucosamine (UDP-GlcNAc) is used in enzymatic post-translational modification of many cytosolic and nuclear proteins by O-linked β-N-acetylglucosamine (O-GlcNAc).
23592772	3	90	link	O-linked	628:635	arg1	β-N-acetylglucosamine					637:657	O-linked β-N-acetylglucosamine	628:657	O-linked β-N-acetylglucosamine (O-GlcNAc)	628:668	The HBP end product UDP-N-acetylglucosamine (UDP-GlcNAc) is used in enzymatic post-translational modification of many cytosolic and nuclear proteins by O-linked β-N-acetylglucosamine (O-GlcNAc).
23592772	11	91	theme	O-GlcNAc	1741:1748	arg1	T352A					1767:1771	T352A	1767:1771	T352A	1767:1771	Finally, reducing p65 O-GlcNAcylation specifically by mutating two p65 O-GlcNAc sites (T322A and T352A) attenuated the induction of PDAC cell anchorage-independent growth.
23592772	11	91	theme	O-GlcNAc	1741:1748	arg1	T322A					1757:1761	T322A	1757:1761	T322A	1757:1761	Finally, reducing p65 O-GlcNAcylation specifically by mutating two p65 O-GlcNAc sites (T322A and T352A) attenuated the induction of PDAC cell anchorage-independent growth.
23592772	11	91	theme	O-GlcNAc	1741:1748	arg1	sites					1750:1754	two p65 O-GlcNAc sites	1733:1754	two p65 O-GlcNAc sites (T322A and T352A)	1733:1772	Finally, reducing p65 O-GlcNAcylation specifically by mutating two p65 O-GlcNAc sites (T322A and T352A) attenuated the induction of PDAC cell anchorage-independent growth.
23592772	8	92	theme	p65	1196:1198	arg1	subunit					1200:1206	NF-κB p65 subunit	1190:1206	NF-κB p65 subunit	1190:1206	The NF-κB p65 subunit and upstream kinases IKKα/IKKβ were O-GlcNAcylated in PDAC.
23592772	8	93	from	O-GlcNAcylated	1244:1257	arg1	PDAC					1262:1265	PDAC	1262:1265	PDAC	1262:1265	The NF-κB p65 subunit and upstream kinases IKKα/IKKβ were O-GlcNAcylated in PDAC.
23592772	10	94	theme	signaling	1659:1667	arg1	activation					1639:1648	activation	1639:1648	activation of NF-κB signaling	1639:1667	Conversely, mimicking PDAC hyper-O-GlcNAcylation through pharmacological inhibition of OGA suppressed suspension culture-induced apoptosis and increased IKKα and p65 O-GlcNAcylation, accompanied by activation of NF-κB signaling.
23592772	10	95	theme	PDAC	1463:1466	arg1	hyper-O-GlcNAcylation					1468:1488	PDAC hyper-O-GlcNAcylation	1463:1488	PDAC hyper-O-GlcNAcylation	1463:1488	Conversely, mimicking PDAC hyper-O-GlcNAcylation through pharmacological inhibition of OGA suppressed suspension culture-induced apoptosis and increased IKKα and p65 O-GlcNAcylation, accompanied by activation of NF-κB signaling.
33086728	2	0	theme	endothelial	485:495	arg1	cells					497:501	endothelial cells	485:501	endothelial cells (ECs)	485:507	Herein, we investigated how NDPK-B is involved in the HBP in endothelial cells (ECs).
33086728	2	0	theme	endothelial	485:495	arg1	ECs					504:506	ECs	504:506	ECs	504:506	Herein, we investigated how NDPK-B is involved in the HBP in endothelial cells (ECs).
33086728	11	1	theme	Ang-2	1696:1700	arg1	O-GlcNAcylation					1652:1666	increased protein O-GlcNAcylation	1634:1666	increased protein O-GlcNAcylation	1634:1666	NDPK-B deficiency hence results in the activation of HBP and the suppression of OGA activity, leading to increased protein O-GlcNAcylation and further upregulation of Ang-2.
33086728	11	1	theme	Ang-2	1696:1700	arg1	upregulation					1680:1691	further upregulation	1672:1691	further upregulation of Ang-2	1672:1700	NDPK-B deficiency hence results in the activation of HBP and the suppression of OGA activity, leading to increased protein O-GlcNAcylation and further upregulation of Ang-2.
33086728	10	2	theme	NDPK-B	1476:1481	arg1	transphosphorylase					1424:1441	diphosphate (NTP/NDP) transphosphorylase	1402:1441	diphosphate (NTP/NDP) transphosphorylase	1402:1441	However, the nucleoside triphosphate to diphosphate (NTP/NDP) transphosphorylase and histidine kinase activity of NDPK-B were dispensable for protein O-GlcNAcylation.
33086728	10	2	theme	NDPK-B	1476:1481	arg1	activity					1464:1471	histidine kinase activity	1447:1471	histidine kinase activity	1447:1471	However, the nucleoside triphosphate to diphosphate (NTP/NDP) transphosphorylase and histidine kinase activity of NDPK-B were dispensable for protein O-GlcNAcylation.
33086728	6	3	theme	UDP-GlcNAc	894:903	arg1	levels					905:910	UDP-GlcNAc levels	894:910	UDP-GlcNAc levels	894:910	Our results show that NDPK-B depletion in ECs elevated UDP-GlcNAc levels and reduced NDPK activity, similar to high glucose (HG) treatment.
33086728	1	4	theme	previous	171:178	arg1	studies					180:186	Our previous studies	167:186	Our previous studies	167:186	Our previous studies identified that retinal endothelial damage caused by hyperglycemia or nucleoside diphosphate kinase-B (NDPK-B) deficiency is linked to elevation of angiopoietin-2 (Ang-2) and the activation of the hexosamine biosynthesis pathway (HBP).
33086728	7	5	dep	induced	1087:1093	arg1	whereas					1096:1102	whereas	1096:1102	whereas	1096:1102	Moreover, the expression and phosphorylation of glutamine:fructose-6-phosphate amidotransferase (GFAT) were induced, whereas OGA activity was suppressed.
33086728	11	6	theme	further	1672:1678	arg1	upregulation					1680:1691	further upregulation	1672:1691	further upregulation of Ang-2	1672:1700	NDPK-B deficiency hence results in the activation of HBP and the suppression of OGA activity, leading to increased protein O-GlcNAcylation and further upregulation of Ang-2.
33086728	8	7	theme	depleted	1236:1243	arg1	ECs					1245:1247	NDPK-B depleted ECs	1229:1247	NDPK-B depleted ECs	1229:1247	Furthermore, overall protein O-GlcNAcylation, along with O-GlcNAcylated Ang-2, was increased in NDPK-B depleted ECs.
33086728	4	8	theme	liquid	686:691	arg1	chromatography					693:706	Ultra-performance liquid chromatography	668:706	Ultra-performance liquid chromatography with Photodiode array detection	668:738	Nucleotide metabolism and O-GlcNAcylated proteins were assessed by UPLC-PDA (Ultra-performance liquid chromatography with Photodiode array detection) and immunoblot, respectively.
33086728	1	9	theme	NDPK-B	291:296	arg1	deficiency					299:308	nucleoside diphosphate kinase-B (NDPK-B) deficiency	258:308	nucleoside diphosphate kinase-B (NDPK-B) deficiency	258:308	Our previous studies identified that retinal endothelial damage caused by hyperglycemia or nucleoside diphosphate kinase-B (NDPK-B) deficiency is linked to elevation of angiopoietin-2 (Ang-2) and the activation of the hexosamine biosynthesis pathway (HBP).
33086728	0	10	theme	Biosynthesis	105:116	arg1	Pathway					118:124	the Hexosamine Biosynthesis Pathway	90:124	the Hexosamine Biosynthesis Pathway	90:124	Involvement of NDPK-B in Glucose Metabolism-Mediated Endothelial Damage via Activation of the Hexosamine Biosynthesis Pathway and Suppression of O-GlcNAcase Activity.
33086728	0	11	from	Involvement	0:10	arg1	Damage					65:70	Glucose Metabolism-Mediated Endothelial Damage	25:70	Glucose Metabolism-Mediated Endothelial Damage via Activation of the Hexosamine Biosynthesis Pathway and Suppression of O-GlcNAcase Activity	25:164	Involvement of NDPK-B in Glucose Metabolism-Mediated Endothelial Damage via Activation of the Hexosamine Biosynthesis Pathway and Suppression of O-GlcNAcase Activity.
33086728	8	12	dep	along	1179:1183	arg1	with					1185:1188	with	1185:1188	with	1185:1188	Furthermore, overall protein O-GlcNAcylation, along with O-GlcNAcylated Ang-2, was increased in NDPK-B depleted ECs.
33086728	10	13	theme	nucleoside	1375:1384	arg1	dispensable					1488:1498	dispensable	1488:1498	dispensable	1488:1498	However, the nucleoside triphosphate to diphosphate (NTP/NDP) transphosphorylase and histidine kinase activity of NDPK-B were dispensable for protein O-GlcNAcylation.
33086728	10	13	theme	nucleoside	1375:1384	arg1	triphosphate					1386:1397	the nucleoside triphosphate	1371:1397	the nucleoside triphosphate to diphosphate (NTP/NDP) transphosphorylase and histidine kinase activity of NDPK-B	1371:1481	However, the nucleoside triphosphate to diphosphate (NTP/NDP) transphosphorylase and histidine kinase activity of NDPK-B were dispensable for protein O-GlcNAcylation.
33086728	1	14	attach	linked	313:318	arg1	elevation					323:331	elevation	323:331	elevation of angiopoietin-2 (Ang-2)	323:357	Our previous studies identified that retinal endothelial damage caused by hyperglycemia or nucleoside diphosphate kinase-B (NDPK-B) deficiency is linked to elevation of angiopoietin-2 (Ang-2) and the activation of the hexosamine biosynthesis pathway (HBP).
33086728	1	14	attach	linked	313:318	arg1	activation					367:376	the activation	363:376	the activation of the hexosamine biosynthesis pathway (HBP)	363:421	Our previous studies identified that retinal endothelial damage caused by hyperglycemia or nucleoside diphosphate kinase-B (NDPK-B) deficiency is linked to elevation of angiopoietin-2 (Ang-2) and the activation of the hexosamine biosynthesis pathway (HBP).
33086728	1	14	attach	linked	313:318	arg2	damage					224:229	retinal endothelial damage	204:229	retinal endothelial damage caused by hyperglycemia or nucleoside diphosphate kinase-B (NDPK-B) deficiency	204:308	Our previous studies identified that retinal endothelial damage caused by hyperglycemia or nucleoside diphosphate kinase-B (NDPK-B) deficiency is linked to elevation of angiopoietin-2 (Ang-2) and the activation of the hexosamine biosynthesis pathway (HBP).
33086728	11	15	theme	protein	1644:1650	arg1	O-GlcNAcylation					1652:1666	increased protein O-GlcNAcylation	1634:1666	increased protein O-GlcNAcylation	1634:1666	NDPK-B deficiency hence results in the activation of HBP and the suppression of OGA activity, leading to increased protein O-GlcNAcylation and further upregulation of Ang-2.
33086728	0	16	theme	Hexosamine	94:103	arg1	Pathway					118:124	the Hexosamine Biosynthesis Pathway	90:124	the Hexosamine Biosynthesis Pathway	90:124	Involvement of NDPK-B in Glucose Metabolism-Mediated Endothelial Damage via Activation of the Hexosamine Biosynthesis Pathway and Suppression of O-GlcNAcase Activity.
33086728	4	17	with	chromatography	693:706	arg1	detection					730:738	Photodiode array detection	713:738	Photodiode array detection	713:738	Nucleotide metabolism and O-GlcNAcylated proteins were assessed by UPLC-PDA (Ultra-performance liquid chromatography with Photodiode array detection) and immunoblot, respectively.
33086728	7	18	theme	glutamine	1027:1035	arg1	phosphorylation					1008:1022	phosphorylation	1008:1022	phosphorylation	1008:1022	Moreover, the expression and phosphorylation of glutamine:fructose-6-phosphate amidotransferase (GFAT) were induced, whereas OGA activity was suppressed.
33086728	7	18	theme	glutamine	1027:1035	arg1	expression					993:1002	expression	993:1002	expression	993:1002	Moreover, the expression and phosphorylation of glutamine:fructose-6-phosphate amidotransferase (GFAT) were induced, whereas OGA activity was suppressed.
33086728	10	19	theme	diphosphate	1402:1412	arg1	transphosphorylase					1424:1441	diphosphate (NTP/NDP) transphosphorylase	1402:1441	diphosphate (NTP/NDP) transphosphorylase	1402:1441	However, the nucleoside triphosphate to diphosphate (NTP/NDP) transphosphorylase and histidine kinase activity of NDPK-B were dispensable for protein O-GlcNAcylation.
33086728	8	20	theme	O-GlcNAcylated	1190:1203	arg1	Ang-2					1205:1209	O-GlcNAcylated Ang-2	1190:1209	O-GlcNAcylated Ang-2	1190:1209	Furthermore, overall protein O-GlcNAcylation, along with O-GlcNAcylated Ang-2, was increased in NDPK-B depleted ECs.
33086728	9	21	theme	OGA	1328:1330	arg1	siRNA					1332:1336	OGA siRNA	1328:1336	OGA siRNA	1328:1336	Pharmacological elevation of protein O-GlcNAcylation using Thiamet G (TMG) or OGA siRNA increased Ang-2 levels.
33086728	7	22	theme	OGA	1104:1106	arg1	activity					1108:1115	OGA activity	1104:1115	OGA activity	1104:1115	Moreover, the expression and phosphorylation of glutamine:fructose-6-phosphate amidotransferase (GFAT) were induced, whereas OGA activity was suppressed.
33086728	0	23	theme	Pathway	118:124	arg1	Suppression					130:140	Suppression	130:140	Suppression of O-GlcNAcase Activity	130:164	Involvement of NDPK-B in Glucose Metabolism-Mediated Endothelial Damage via Activation of the Hexosamine Biosynthesis Pathway and Suppression of O-GlcNAcase Activity.
33086728	0	23	theme	Pathway	118:124	arg1	Activation					76:85	Activation	76:85	Activation of the Hexosamine Biosynthesis Pathway	76:124	Involvement of NDPK-B in Glucose Metabolism-Mediated Endothelial Damage via Activation of the Hexosamine Biosynthesis Pathway and Suppression of O-GlcNAcase Activity.
33086728	1	24	theme	hexosamine	385:394	arg1	HBP					418:420	HBP	418:420	HBP	418:420	Our previous studies identified that retinal endothelial damage caused by hyperglycemia or nucleoside diphosphate kinase-B (NDPK-B) deficiency is linked to elevation of angiopoietin-2 (Ang-2) and the activation of the hexosamine biosynthesis pathway (HBP).
33086728	1	24	theme	hexosamine	385:394	arg1	pathway					409:415	the hexosamine biosynthesis pathway	381:415	the hexosamine biosynthesis pathway (HBP)	381:421	Our previous studies identified that retinal endothelial damage caused by hyperglycemia or nucleoside diphosphate kinase-B (NDPK-B) deficiency is linked to elevation of angiopoietin-2 (Ang-2) and the activation of the hexosamine biosynthesis pathway (HBP).
33086728	5	25	theme	NDPK-B	788:793	arg1	Re-expression					771:783	Re-expression	771:783	Re-expression of NDPK-B	771:793	Re-expression of NDPK-B was achieved with recombinant adenoviruses.
33086728	10	26	theme	histidine	1447:1455	arg1	activity					1464:1471	histidine kinase activity	1447:1471	histidine kinase activity	1447:1471	However, the nucleoside triphosphate to diphosphate (NTP/NDP) transphosphorylase and histidine kinase activity of NDPK-B were dispensable for protein O-GlcNAcylation.
33086728	12	27	theme	HBP	1795:1797	arg1	modulation					1777:1786	the modulation	1773:1786	the modulation of the HBP	1773:1797	The data indicate a critical role of NDPK-B in endothelial damage via the modulation of the HBP.
33086728	5	28	theme	recombinant	813:823	arg1	adenoviruses					825:836	recombinant adenoviruses	813:836	recombinant adenoviruses	813:836	Re-expression of NDPK-B was achieved with recombinant adenoviruses.
33086728	1	29	theme	biosynthesis	396:407	arg1	HBP					418:420	HBP	418:420	HBP	418:420	Our previous studies identified that retinal endothelial damage caused by hyperglycemia or nucleoside diphosphate kinase-B (NDPK-B) deficiency is linked to elevation of angiopoietin-2 (Ang-2) and the activation of the hexosamine biosynthesis pathway (HBP).
33086728	1	29	theme	biosynthesis	396:407	arg1	pathway					409:415	the hexosamine biosynthesis pathway	381:415	the hexosamine biosynthesis pathway (HBP)	381:421	Our previous studies identified that retinal endothelial damage caused by hyperglycemia or nucleoside diphosphate kinase-B (NDPK-B) deficiency is linked to elevation of angiopoietin-2 (Ang-2) and the activation of the hexosamine biosynthesis pathway (HBP).
33086728	11	30	theme	OGA	1609:1611	arg1	activity					1613:1620	OGA activity	1609:1620	OGA activity	1609:1620	NDPK-B deficiency hence results in the activation of HBP and the suppression of OGA activity, leading to increased protein O-GlcNAcylation and further upregulation of Ang-2.
33086728	7	31	dep	glutamine	1027:1035	arg1	amidotransferase					1058:1073	fructose-6-phosphate amidotransferase	1037:1073	glutamine:fructose-6-phosphate amidotransferase (GFAT)	1027:1080	Moreover, the expression and phosphorylation of glutamine:fructose-6-phosphate amidotransferase (GFAT) were induced, whereas OGA activity was suppressed.
33086728	7	31	dep	glutamine	1027:1035	arg1	GFAT					1076:1079	GFAT	1076:1079	GFAT	1076:1079	Moreover, the expression and phosphorylation of glutamine:fructose-6-phosphate amidotransferase (GFAT) were induced, whereas OGA activity was suppressed.
33086728	1	32	theme	retinal	204:210	arg1	damage					224:229	retinal endothelial damage	204:229	retinal endothelial damage caused by hyperglycemia or nucleoside diphosphate kinase-B (NDPK-B) deficiency	204:308	Our previous studies identified that retinal endothelial damage caused by hyperglycemia or nucleoside diphosphate kinase-B (NDPK-B) deficiency is linked to elevation of angiopoietin-2 (Ang-2) and the activation of the hexosamine biosynthesis pathway (HBP).
33086728	6	33	from	depletion	868:876	arg1	ECs					881:883	ECs	881:883	ECs	881:883	Our results show that NDPK-B depletion in ECs elevated UDP-GlcNAc levels and reduced NDPK activity, similar to high glucose (HG) treatment.
33086728	9	34	theme	Ang-2	1348:1352	arg1	levels					1354:1359	Ang-2 levels	1348:1359	Ang-2 levels	1348:1359	Pharmacological elevation of protein O-GlcNAcylation using Thiamet G (TMG) or OGA siRNA increased Ang-2 levels.
33086728	9	35	theme	protein	1279:1285	arg1	O-GlcNAcylation					1287:1301	protein O-GlcNAcylation	1279:1301	protein O-GlcNAcylation	1279:1301	Pharmacological elevation of protein O-GlcNAcylation using Thiamet G (TMG) or OGA siRNA increased Ang-2 levels.
33086728	1	36	theme	endothelial	212:222	arg1	damage					224:229	retinal endothelial damage	204:229	retinal endothelial damage caused by hyperglycemia or nucleoside diphosphate kinase-B (NDPK-B) deficiency	204:308	Our previous studies identified that retinal endothelial damage caused by hyperglycemia or nucleoside diphosphate kinase-B (NDPK-B) deficiency is linked to elevation of angiopoietin-2 (Ang-2) and the activation of the hexosamine biosynthesis pathway (HBP).
33086728	12	37	theme	critical	1723:1730	arg1	role					1732:1735	a critical role	1721:1735	a critical role of NDPK-B in endothelial damage	1721:1767	The data indicate a critical role of NDPK-B in endothelial damage via the modulation of the HBP.
33086728	3	38	theme	O-GlcNAcase	539:549	arg1	activities					514:523	The activities	510:523	The activities of NDPK-B and O-GlcNAcase (OGA)	510:555	The activities of NDPK-B and O-GlcNAcase (OGA) were measured by in vitro assays.
33086728	10	39	theme	NTP/NDP	1415:1421	arg1	transphosphorylase					1424:1441	diphosphate (NTP/NDP) transphosphorylase	1402:1441	diphosphate (NTP/NDP) transphosphorylase	1402:1441	However, the nucleoside triphosphate to diphosphate (NTP/NDP) transphosphorylase and histidine kinase activity of NDPK-B were dispensable for protein O-GlcNAcylation.
33086728	6	40	theme	NDPK	924:927	arg1	activity					929:936	NDPK activity	924:936	NDPK activity	924:936	Our results show that NDPK-B depletion in ECs elevated UDP-GlcNAc levels and reduced NDPK activity, similar to high glucose (HG) treatment.
33086728	0	41	theme	NDPK-B	15:20	arg1	Involvement					0:10	Involvement	0:10	Involvement of NDPK-B in Glucose Metabolism-Mediated Endothelial Damage via Activation of the Hexosamine Biosynthesis Pathway and Suppression of O-GlcNAcase Activity.	0:165	Involvement of NDPK-B in Glucose Metabolism-Mediated Endothelial Damage via Activation of the Hexosamine Biosynthesis Pathway and Suppression of O-GlcNAcase Activity.
33086728	1	42	theme	pathway	409:415	arg1	elevation					323:331	elevation	323:331	elevation of angiopoietin-2 (Ang-2)	323:357	Our previous studies identified that retinal endothelial damage caused by hyperglycemia or nucleoside diphosphate kinase-B (NDPK-B) deficiency is linked to elevation of angiopoietin-2 (Ang-2) and the activation of the hexosamine biosynthesis pathway (HBP).
33086728	1	42	theme	pathway	409:415	arg1	activation					367:376	the activation	363:376	the activation of the hexosamine biosynthesis pathway (HBP)	363:421	Our previous studies identified that retinal endothelial damage caused by hyperglycemia or nucleoside diphosphate kinase-B (NDPK-B) deficiency is linked to elevation of angiopoietin-2 (Ang-2) and the activation of the hexosamine biosynthesis pathway (HBP).
33086728	7	43	dep	expression	993:1002	arg1	the					989:991	the	989:991	the	989:991	Moreover, the expression and phosphorylation of glutamine:fructose-6-phosphate amidotransferase (GFAT) were induced, whereas OGA activity was suppressed.
33086728	0	44	theme	Metabolism-Mediated	33:51	arg1	Damage					65:70	Glucose Metabolism-Mediated Endothelial Damage	25:70	Glucose Metabolism-Mediated Endothelial Damage via Activation of the Hexosamine Biosynthesis Pathway and Suppression of O-GlcNAcase Activity	25:164	Involvement of NDPK-B in Glucose Metabolism-Mediated Endothelial Damage via Activation of the Hexosamine Biosynthesis Pathway and Suppression of O-GlcNAcase Activity.
33086728	12	45	from	role	1732:1735	arg1	damage					1762:1767	endothelial damage	1750:1767	endothelial damage	1750:1767	The data indicate a critical role of NDPK-B in endothelial damage via the modulation of the HBP.
33086728	0	46	theme	Activity	157:164	arg1	Suppression					130:140	Suppression	130:140	Suppression of O-GlcNAcase Activity	130:164	Involvement of NDPK-B in Glucose Metabolism-Mediated Endothelial Damage via Activation of the Hexosamine Biosynthesis Pathway and Suppression of O-GlcNAcase Activity.
33086728	0	46	theme	Activity	157:164	arg1	Activation					76:85	Activation	76:85	Activation of the Hexosamine Biosynthesis Pathway	76:124	Involvement of NDPK-B in Glucose Metabolism-Mediated Endothelial Damage via Activation of the Hexosamine Biosynthesis Pathway and Suppression of O-GlcNAcase Activity.
33086728	9	47	theme	Pharmacological	1250:1264	arg1	elevation					1266:1274	Pharmacological elevation	1250:1274	Pharmacological elevation of protein O-GlcNAcylation using Thiamet G (TMG) or OGA siRNA	1250:1336	Pharmacological elevation of protein O-GlcNAcylation using Thiamet G (TMG) or OGA siRNA increased Ang-2 levels.
33086728	11	48	theme	HBP	1582:1584	arg1	suppression					1594:1604	the suppression	1590:1604	the suppression of OGA activity	1590:1620	NDPK-B deficiency hence results in the activation of HBP and the suppression of OGA activity, leading to increased protein O-GlcNAcylation and further upregulation of Ang-2.
33086728	11	48	theme	HBP	1582:1584	arg1	activation					1568:1577	the activation	1564:1577	the activation of HBP	1564:1584	NDPK-B deficiency hence results in the activation of HBP and the suppression of OGA activity, leading to increased protein O-GlcNAcylation and further upregulation of Ang-2.
33086728	3	49	dep	in	574:575	arg1	vitro					577:581	vitro	577:581	vitro	577:581	The activities of NDPK-B and O-GlcNAcase (OGA) were measured by in vitro assays.
33086728	0	50	theme	Glucose	25:31	arg1	Damage					65:70	Glucose Metabolism-Mediated Endothelial Damage	25:70	Glucose Metabolism-Mediated Endothelial Damage via Activation of the Hexosamine Biosynthesis Pathway and Suppression of O-GlcNAcase Activity	25:164	Involvement of NDPK-B in Glucose Metabolism-Mediated Endothelial Damage via Activation of the Hexosamine Biosynthesis Pathway and Suppression of O-GlcNAcase Activity.
33086728	0	51	theme	O-GlcNAcase	145:155	arg1	Activity					157:164	O-GlcNAcase Activity	145:164	O-GlcNAcase Activity	145:164	Involvement of NDPK-B in Glucose Metabolism-Mediated Endothelial Damage via Activation of the Hexosamine Biosynthesis Pathway and Suppression of O-GlcNAcase Activity.
33086728	8	52	theme	protein	1154:1160	arg1	O-GlcNAcylation					1162:1176	overall protein O-GlcNAcylation	1146:1176	overall protein O-GlcNAcylation	1146:1176	Furthermore, overall protein O-GlcNAcylation, along with O-GlcNAcylated Ang-2, was increased in NDPK-B depleted ECs.
33086728	3	53	theme	in	574:575	arg1	assays					583:588	in vitro assays	574:588	in vitro assays	574:588	The activities of NDPK-B and O-GlcNAcase (OGA) were measured by in vitro assays.
33086728	4	54	theme	O-GlcNAcylated	617:630	arg1	proteins					632:639	O-GlcNAcylated proteins	617:639	O-GlcNAcylated proteins	617:639	Nucleotide metabolism and O-GlcNAcylated proteins were assessed by UPLC-PDA (Ultra-performance liquid chromatography with Photodiode array detection) and immunoblot, respectively.
33086728	10	55	theme	kinase	1457:1462	arg1	activity					1464:1471	histidine kinase activity	1447:1471	histidine kinase activity	1447:1471	However, the nucleoside triphosphate to diphosphate (NTP/NDP) transphosphorylase and histidine kinase activity of NDPK-B were dispensable for protein O-GlcNAcylation.
33086728	1	56	theme	angiopoietin-2	336:349	arg1	elevation					323:331	elevation	323:331	elevation of angiopoietin-2 (Ang-2)	323:357	Our previous studies identified that retinal endothelial damage caused by hyperglycemia or nucleoside diphosphate kinase-B (NDPK-B) deficiency is linked to elevation of angiopoietin-2 (Ang-2) and the activation of the hexosamine biosynthesis pathway (HBP).
33086728	1	56	theme	angiopoietin-2	336:349	arg1	activation					367:376	the activation	363:376	the activation of the hexosamine biosynthesis pathway (HBP)	363:421	Our previous studies identified that retinal endothelial damage caused by hyperglycemia or nucleoside diphosphate kinase-B (NDPK-B) deficiency is linked to elevation of angiopoietin-2 (Ang-2) and the activation of the hexosamine biosynthesis pathway (HBP).
33086728	2	57	from	HBP	478:480	arg1	cells					497:501	endothelial cells	485:501	endothelial cells (ECs)	485:507	Herein, we investigated how NDPK-B is involved in the HBP in endothelial cells (ECs).
33086728	2	57	from	HBP	478:480	arg1	ECs					504:506	ECs	504:506	ECs	504:506	Herein, we investigated how NDPK-B is involved in the HBP in endothelial cells (ECs).
33086728	4	58	theme	Photodiode	713:722	arg1	detection					730:738	Photodiode array detection	713:738	Photodiode array detection	713:738	Nucleotide metabolism and O-GlcNAcylated proteins were assessed by UPLC-PDA (Ultra-performance liquid chromatography with Photodiode array detection) and immunoblot, respectively.
33086728	0	59	theme	Endothelial	53:63	arg1	Damage					65:70	Glucose Metabolism-Mediated Endothelial Damage	25:70	Glucose Metabolism-Mediated Endothelial Damage via Activation of the Hexosamine Biosynthesis Pathway and Suppression of O-GlcNAcase Activity	25:164	Involvement of NDPK-B in Glucose Metabolism-Mediated Endothelial Damage via Activation of the Hexosamine Biosynthesis Pathway and Suppression of O-GlcNAcase Activity.
33086728	6	60	theme	high	950:953	arg1	glucose					955:961	high glucose	950:961	high glucose (HG) treatment	950:976	Our results show that NDPK-B depletion in ECs elevated UDP-GlcNAc levels and reduced NDPK activity, similar to high glucose (HG) treatment.
33086728	6	60	theme	high	950:953	arg1	HG					964:965	HG	964:965	HG	964:965	Our results show that NDPK-B depletion in ECs elevated UDP-GlcNAc levels and reduced NDPK activity, similar to high glucose (HG) treatment.
33086728	6	61	theme	NDPK-B	861:866	arg1	depletion					868:876	NDPK-B depletion	861:876	NDPK-B depletion in ECs	861:883	Our results show that NDPK-B depletion in ECs elevated UDP-GlcNAc levels and reduced NDPK activity, similar to high glucose (HG) treatment.
33086728	11	62	theme	activity	1613:1620	arg1	suppression					1594:1604	the suppression	1590:1604	the suppression of OGA activity	1590:1620	NDPK-B deficiency hence results in the activation of HBP and the suppression of OGA activity, leading to increased protein O-GlcNAcylation and further upregulation of Ang-2.
33086728	11	62	theme	activity	1613:1620	arg1	activation					1568:1577	the activation	1564:1577	the activation of HBP	1564:1584	NDPK-B deficiency hence results in the activation of HBP and the suppression of OGA activity, leading to increased protein O-GlcNAcylation and further upregulation of Ang-2.
33086728	8	63	theme	NDPK-B	1229:1234	arg1	ECs					1245:1247	NDPK-B depleted ECs	1229:1247	NDPK-B depleted ECs	1229:1247	Furthermore, overall protein O-GlcNAcylation, along with O-GlcNAcylated Ang-2, was increased in NDPK-B depleted ECs.
33086728	11	64	theme	NDPK-B	1529:1534	arg1	deficiency					1536:1545	NDPK-B deficiency	1529:1545	NDPK-B deficiency	1529:1545	NDPK-B deficiency hence results in the activation of HBP and the suppression of OGA activity, leading to increased protein O-GlcNAcylation and further upregulation of Ang-2.
33086728	9	65	theme	O-GlcNAcylation	1287:1301	arg1	elevation					1266:1274	Pharmacological elevation	1250:1274	Pharmacological elevation of protein O-GlcNAcylation using Thiamet G (TMG) or OGA siRNA	1250:1336	Pharmacological elevation of protein O-GlcNAcylation using Thiamet G (TMG) or OGA siRNA increased Ang-2 levels.
33086728	4	66	dep	UPLC-PDA	658:665	arg1	chromatography					693:706	Ultra-performance liquid chromatography	668:706	Ultra-performance liquid chromatography with Photodiode array detection	668:738	Nucleotide metabolism and O-GlcNAcylated proteins were assessed by UPLC-PDA (Ultra-performance liquid chromatography with Photodiode array detection) and immunoblot, respectively.
33086728	8	67	gly	O-GlcNAcylation	1162:1176	arg1	ECs					1245:1247	NDPK-B depleted ECs	1229:1247	NDPK-B depleted ECs	1229:1247	Furthermore, overall protein O-GlcNAcylation, along with O-GlcNAcylated Ang-2, was increased in NDPK-B depleted ECs.
33086728	12	68	theme	NDPK-B	1740:1745	arg1	role					1732:1735	a critical role	1721:1735	a critical role of NDPK-B in endothelial damage	1721:1767	The data indicate a critical role of NDPK-B in endothelial damage via the modulation of the HBP.
33086728	7	69	theme	fructose-6-phosphate	1037:1056	arg1	amidotransferase					1058:1073	fructose-6-phosphate amidotransferase	1037:1073	glutamine:fructose-6-phosphate amidotransferase (GFAT)	1027:1080	Moreover, the expression and phosphorylation of glutamine:fructose-6-phosphate amidotransferase (GFAT) were induced, whereas OGA activity was suppressed.
33086728	7	69	theme	fructose-6-phosphate	1037:1056	arg1	GFAT					1076:1079	GFAT	1076:1079	GFAT	1076:1079	Moreover, the expression and phosphorylation of glutamine:fructose-6-phosphate amidotransferase (GFAT) were induced, whereas OGA activity was suppressed.
33086728	3	70	theme	NDPK-B	528:533	arg1	activities					514:523	The activities	510:523	The activities of NDPK-B and O-GlcNAcase (OGA)	510:555	The activities of NDPK-B and O-GlcNAcase (OGA) were measured by in vitro assays.
33086728	10	71	theme	protein	1504:1510	arg1	O-GlcNAcylation					1512:1526	protein O-GlcNAcylation	1504:1526	protein O-GlcNAcylation	1504:1526	However, the nucleoside triphosphate to diphosphate (NTP/NDP) transphosphorylase and histidine kinase activity of NDPK-B were dispensable for protein O-GlcNAcylation.
33086728	4	72	theme	array	724:728	arg1	detection					730:738	Photodiode array detection	713:738	Photodiode array detection	713:738	Nucleotide metabolism and O-GlcNAcylated proteins were assessed by UPLC-PDA (Ultra-performance liquid chromatography with Photodiode array detection) and immunoblot, respectively.
33086728	1	73	theme	nucleoside	258:267	arg1	deficiency					299:308	nucleoside diphosphate kinase-B (NDPK-B) deficiency	258:308	nucleoside diphosphate kinase-B (NDPK-B) deficiency	258:308	Our previous studies identified that retinal endothelial damage caused by hyperglycemia or nucleoside diphosphate kinase-B (NDPK-B) deficiency is linked to elevation of angiopoietin-2 (Ang-2) and the activation of the hexosamine biosynthesis pathway (HBP).
33086728	8	74	theme	overall	1146:1152	arg1	O-GlcNAcylation					1162:1176	overall protein O-GlcNAcylation	1146:1176	overall protein O-GlcNAcylation	1146:1176	Furthermore, overall protein O-GlcNAcylation, along with O-GlcNAcylated Ang-2, was increased in NDPK-B depleted ECs.
33086728	9	75	theme	Thiamet	1309:1315	arg1	TMG					1320:1322	TMG	1320:1322	TMG	1320:1322	Pharmacological elevation of protein O-GlcNAcylation using Thiamet G (TMG) or OGA siRNA increased Ang-2 levels.
33086728	9	75	theme	Thiamet	1309:1315	arg1	G					1317:1317	Thiamet G	1309:1317	Thiamet G (TMG)	1309:1323	Pharmacological elevation of protein O-GlcNAcylation using Thiamet G (TMG) or OGA siRNA increased Ang-2 levels.
33086728	4	76	theme	Nucleotide	591:600	arg1	metabolism					602:611	Nucleotide metabolism	591:611	Nucleotide metabolism	591:611	Nucleotide metabolism and O-GlcNAcylated proteins were assessed by UPLC-PDA (Ultra-performance liquid chromatography with Photodiode array detection) and immunoblot, respectively.
33086728	4	77	theme	Ultra-performance	668:684	arg1	chromatography					693:706	Ultra-performance liquid chromatography	668:706	Ultra-performance liquid chromatography with Photodiode array detection	668:738	Nucleotide metabolism and O-GlcNAcylated proteins were assessed by UPLC-PDA (Ultra-performance liquid chromatography with Photodiode array detection) and immunoblot, respectively.
33086728	12	78	theme	endothelial	1750:1760	arg1	damage					1762:1767	endothelial damage	1750:1767	endothelial damage	1750:1767	The data indicate a critical role of NDPK-B in endothelial damage via the modulation of the HBP.
33086728	1	79	theme	diphosphate	269:279	arg1	deficiency					299:308	nucleoside diphosphate kinase-B (NDPK-B) deficiency	258:308	nucleoside diphosphate kinase-B (NDPK-B) deficiency	258:308	Our previous studies identified that retinal endothelial damage caused by hyperglycemia or nucleoside diphosphate kinase-B (NDPK-B) deficiency is linked to elevation of angiopoietin-2 (Ang-2) and the activation of the hexosamine biosynthesis pathway (HBP).
33086728	6	80	theme	similar	939:945	arg1	activity					929:936	NDPK activity	924:936	NDPK activity	924:936	Our results show that NDPK-B depletion in ECs elevated UDP-GlcNAc levels and reduced NDPK activity, similar to high glucose (HG) treatment.
33086728	11	81	theme	increased	1634:1642	arg1	O-GlcNAcylation					1652:1666	increased protein O-GlcNAcylation	1634:1666	increased protein O-GlcNAcylation	1634:1666	NDPK-B deficiency hence results in the activation of HBP and the suppression of OGA activity, leading to increased protein O-GlcNAcylation and further upregulation of Ang-2.
33086728	6	82	theme	glucose	955:961	arg1	treatment					968:976	high glucose (HG) treatment	950:976	high glucose (HG) treatment	950:976	Our results show that NDPK-B depletion in ECs elevated UDP-GlcNAc levels and reduced NDPK activity, similar to high glucose (HG) treatment.
33086728	1	83	theme	kinase-B	281:288	arg1	deficiency					299:308	nucleoside diphosphate kinase-B (NDPK-B) deficiency	258:308	nucleoside diphosphate kinase-B (NDPK-B) deficiency	258:308	Our previous studies identified that retinal endothelial damage caused by hyperglycemia or nucleoside diphosphate kinase-B (NDPK-B) deficiency is linked to elevation of angiopoietin-2 (Ang-2) and the activation of the hexosamine biosynthesis pathway (HBP).
23271734	0	0	theme	major	61:65	arg1	protein					39:45	Z-band alternatively spliced PDZ motif protein	0:45	Z-band alternatively spliced PDZ motif protein (ZASP)	0:52	Z-band alternatively spliced PDZ motif protein (ZASP) is the major O-linked β-N-acetylglucosamine-substituted protein in human heart myofibrils.
23271734	0	0	theme	major	61:65	arg1	protein					110:116	the major O-linked β-N-acetylglucosamine-substituted protein	57:116	the major O-linked β-N-acetylglucosamine-substituted protein in human heart myofibrils	57:142	Z-band alternatively spliced PDZ motif protein (ZASP) is the major O-linked β-N-acetylglucosamine-substituted protein in human heart myofibrils.
23271734	3	1	theme	Z-band	729:734	arg1	protein					768:774	Z-band alternatively spliced PDZ motif protein	729:774	Z-band alternatively spliced PDZ motif protein	729:774	MALDI-MS/MS identified the 90-kDa band as the protein ZASP (Z-band alternatively spliced PDZ motif protein), a minor component of the Z-disc (about 1 per 400 α-actinin) important for myofibrillar development and mechanotransduction.
23271734	3	1	theme	Z-band	729:734	arg1	ZASP					723:726	the protein ZASP	711:726	the protein ZASP (Z-band alternatively spliced PDZ motif protein)	711:775	MALDI-MS/MS identified the 90-kDa band as the protein ZASP (Z-band alternatively spliced PDZ motif protein), a minor component of the Z-disc (about 1 per 400 α-actinin) important for myofibrillar development and mechanotransduction.
23271734	0	2	link	O-linked	67:74	arg1	protein					39:45	Z-band alternatively spliced PDZ motif protein	0:45	Z-band alternatively spliced PDZ motif protein (ZASP)	0:52	Z-band alternatively spliced PDZ motif protein (ZASP) is the major O-linked β-N-acetylglucosamine-substituted protein in human heart myofibrils.
23271734	0	2	link	O-linked	67:74	arg1	protein					110:116	the major O-linked β-N-acetylglucosamine-substituted protein	57:116	the major O-linked β-N-acetylglucosamine-substituted protein in human heart myofibrils	57:142	Z-band alternatively spliced PDZ motif protein (ZASP) is the major O-linked β-N-acetylglucosamine-substituted protein in human heart myofibrils.
23271734	1	3	theme	O-linked	156:163	arg1	modification					198:209	O-linked β-N-acetylglucosamine (O-GlcNAc) modification	156:209	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of contractile proteins in human heart	156:248	We studied O-linked β-N-acetylglucosamine (O-GlcNAc) modification of contractile proteins in human heart using SDS-PAGE and three detection methods: specific enzymatic conjugation of O-GlcNAc with UDP-N-azidoacetylgalactosamine (UDP-GalNAz) that is then linked to a tetramethylrhodamine fluorescent tag and CTD110.6 and RL2 monoclonal antibodies to O-GlcNAc.
23271734	5	4	theme	myectomy	1205:1212	arg1	samples					1183:1189	myectomy muscle samples	1167:1189	myectomy muscle samples (donor versus myectomy p < 0.05)	1167:1222	O-GlcNAcylation of ZASP increased in diseased heart, being 49 ± 5% of all O-GlcNAc in donor, 68 ± 9% in end-stage failing heart, and 76 ± 6% in myectomy muscle samples (donor versus myectomy p < 0.05).
23271734	5	4	theme	myectomy	1205:1212	arg1	<					1216:1216	donor versus myectomy p < 0.05	1192:1221	<	1216:1216	O-GlcNAcylation of ZASP increased in diseased heart, being 49 ± 5% of all O-GlcNAc in donor, 68 ± 9% in end-stage failing heart, and 76 ± 6% in myectomy muscle samples (donor versus myectomy p < 0.05).
23271734	2	5	theme	bands	588:592	arg1	bands					588:592	bands ~90 kDa	588:600	bands ~90 kDa	588:600	All three methods showed that O-GlcNAc modification was predominantly in a group of bands ~90 kDa that did not correspond to any of the major myofibrillar proteins.
23271734	2	5	theme	bands	588:592	arg1	group					579:583	a group	577:583	a group of bands ~90 kDa that did not correspond to any of the major myofibrillar proteins	577:666	All three methods showed that O-GlcNAc modification was predominantly in a group of bands ~90 kDa that did not correspond to any of the major myofibrillar proteins.
23271734	3	6	theme	protein	715:721	arg1	component					786:794	a minor component	778:794	a minor component of the Z-disc (about 1 per 400 α-actinin) important for myofibrillar development and mechanotransduction	778:899	MALDI-MS/MS identified the 90-kDa band as the protein ZASP (Z-band alternatively spliced PDZ motif protein), a minor component of the Z-disc (about 1 per 400 α-actinin) important for myofibrillar development and mechanotransduction.
23271734	3	6	theme	protein	715:721	arg1	protein					768:774	Z-band alternatively spliced PDZ motif protein	729:774	Z-band alternatively spliced PDZ motif protein	729:774	MALDI-MS/MS identified the 90-kDa band as the protein ZASP (Z-band alternatively spliced PDZ motif protein), a minor component of the Z-disc (about 1 per 400 α-actinin) important for myofibrillar development and mechanotransduction.
23271734	3	6	theme	protein	715:721	arg1	ZASP					723:726	the protein ZASP	711:726	the protein ZASP (Z-band alternatively spliced PDZ motif protein)	711:775	MALDI-MS/MS identified the 90-kDa band as the protein ZASP (Z-band alternatively spliced PDZ motif protein), a minor component of the Z-disc (about 1 per 400 α-actinin) important for myofibrillar development and mechanotransduction.
23271734	3	6	theme	protein	715:721	arg1	band					703:706	the 90-kDa band	692:706	the 90-kDa band	692:706	MALDI-MS/MS identified the 90-kDa band as the protein ZASP (Z-band alternatively spliced PDZ motif protein), a minor component of the Z-disc (about 1 per 400 α-actinin) important for myofibrillar development and mechanotransduction.
23271734	1	7	theme	monoclonal	469:478	arg1	antibodies					480:489	CTD110.6 and RL2 monoclonal antibodies	452:489	CTD110.6 and RL2 monoclonal antibodies to O-GlcNAc	452:501	We studied O-linked β-N-acetylglucosamine (O-GlcNAc) modification of contractile proteins in human heart using SDS-PAGE and three detection methods: specific enzymatic conjugation of O-GlcNAc with UDP-N-azidoacetylgalactosamine (UDP-GalNAz) that is then linked to a tetramethylrhodamine fluorescent tag and CTD110.6 and RL2 monoclonal antibodies to O-GlcNAc.
23271734	1	8	attach	linked	399:404	arg2	UDP-N-azidoacetylgalactosamine					342:371	UDP-N-azidoacetylgalactosamine	342:371	UDP-N-azidoacetylgalactosamine (UDP-GalNAz) that is then linked to a tetramethylrhodamine fluorescent tag and CTD110.6 and RL2 monoclonal antibodies to O-GlcNAc	342:501	We studied O-linked β-N-acetylglucosamine (O-GlcNAc) modification of contractile proteins in human heart using SDS-PAGE and three detection methods: specific enzymatic conjugation of O-GlcNAc with UDP-N-azidoacetylgalactosamine (UDP-GalNAz) that is then linked to a tetramethylrhodamine fluorescent tag and CTD110.6 and RL2 monoclonal antibodies to O-GlcNAc.
23271734	1	8	attach	linked	399:404	arg1	tag					444:446	a tetramethylrhodamine fluorescent tag	409:446	a tetramethylrhodamine fluorescent tag	409:446	We studied O-linked β-N-acetylglucosamine (O-GlcNAc) modification of contractile proteins in human heart using SDS-PAGE and three detection methods: specific enzymatic conjugation of O-GlcNAc with UDP-N-azidoacetylgalactosamine (UDP-GalNAz) that is then linked to a tetramethylrhodamine fluorescent tag and CTD110.6 and RL2 monoclonal antibodies to O-GlcNAc.
23271734	1	8	attach	linked	399:404	arg1	antibodies					480:489	CTD110.6 and RL2 monoclonal antibodies	452:489	CTD110.6 and RL2 monoclonal antibodies to O-GlcNAc	452:501	We studied O-linked β-N-acetylglucosamine (O-GlcNAc) modification of contractile proteins in human heart using SDS-PAGE and three detection methods: specific enzymatic conjugation of O-GlcNAc with UDP-N-azidoacetylgalactosamine (UDP-GalNAz) that is then linked to a tetramethylrhodamine fluorescent tag and CTD110.6 and RL2 monoclonal antibodies to O-GlcNAc.
23271734	1	8	attach	linked	399:404	arg2	UDP-GalNAz					374:383	UDP-GalNAz	374:383	UDP-GalNAz	374:383	We studied O-linked β-N-acetylglucosamine (O-GlcNAc) modification of contractile proteins in human heart using SDS-PAGE and three detection methods: specific enzymatic conjugation of O-GlcNAc with UDP-N-azidoacetylgalactosamine (UDP-GalNAz) that is then linked to a tetramethylrhodamine fluorescent tag and CTD110.6 and RL2 monoclonal antibodies to O-GlcNAc.
23271734	5	9	theme	p	1214:1214	arg1	samples					1183:1189	myectomy muscle samples	1167:1189	myectomy muscle samples (donor versus myectomy p < 0.05)	1167:1222	O-GlcNAcylation of ZASP increased in diseased heart, being 49 ± 5% of all O-GlcNAc in donor, 68 ± 9% in end-stage failing heart, and 76 ± 6% in myectomy muscle samples (donor versus myectomy p < 0.05).
23271734	5	9	theme	p	1214:1214	arg1	<					1216:1216	donor versus myectomy p < 0.05	1192:1221	<	1216:1216	O-GlcNAcylation of ZASP increased in diseased heart, being 49 ± 5% of all O-GlcNAc in donor, 68 ± 9% in end-stage failing heart, and 76 ± 6% in myectomy muscle samples (donor versus myectomy p < 0.05).
23271734	0	10	theme	β-N-acetylglucosamine-substituted	76:108	arg1	protein					39:45	Z-band alternatively spliced PDZ motif protein	0:45	Z-band alternatively spliced PDZ motif protein (ZASP)	0:52	Z-band alternatively spliced PDZ motif protein (ZASP) is the major O-linked β-N-acetylglucosamine-substituted protein in human heart myofibrils.
23271734	0	10	theme	β-N-acetylglucosamine-substituted	76:108	arg1	protein					110:116	the major O-linked β-N-acetylglucosamine-substituted protein	57:116	the major O-linked β-N-acetylglucosamine-substituted protein in human heart myofibrils	57:142	Z-band alternatively spliced PDZ motif protein (ZASP) is the major O-linked β-N-acetylglucosamine-substituted protein in human heart myofibrils.
23271734	1	11	theme	detection	275:283	arg1	methods					285:291	three detection methods	269:291	three detection methods: specific enzymatic conjugation of O-GlcNAc with UDP-N-azidoacetylgalactosamine (UDP-GalNAz) that is then linked to a tetramethylrhodamine fluorescent tag and CTD110.6 and RL2 monoclonal antibodies to O-GlcNAc	269:501	We studied O-linked β-N-acetylglucosamine (O-GlcNAc) modification of contractile proteins in human heart using SDS-PAGE and three detection methods: specific enzymatic conjugation of O-GlcNAc with UDP-N-azidoacetylgalactosamine (UDP-GalNAz) that is then linked to a tetramethylrhodamine fluorescent tag and CTD110.6 and RL2 monoclonal antibodies to O-GlcNAc.
23271734	0	12	theme	O-linked	67:74	arg1	protein					39:45	Z-band alternatively spliced PDZ motif protein	0:45	Z-band alternatively spliced PDZ motif protein (ZASP)	0:52	Z-band alternatively spliced PDZ motif protein (ZASP) is the major O-linked β-N-acetylglucosamine-substituted protein in human heart myofibrils.
23271734	0	12	theme	O-linked	67:74	arg1	protein					110:116	the major O-linked β-N-acetylglucosamine-substituted protein	57:116	the major O-linked β-N-acetylglucosamine-substituted protein in human heart myofibrils	57:142	Z-band alternatively spliced PDZ motif protein (ZASP) is the major O-linked β-N-acetylglucosamine-substituted protein in human heart myofibrils.
23271734	3	13	theme	PDZ	758:760	arg1	protein					768:774	Z-band alternatively spliced PDZ motif protein	729:774	Z-band alternatively spliced PDZ motif protein	729:774	MALDI-MS/MS identified the 90-kDa band as the protein ZASP (Z-band alternatively spliced PDZ motif protein), a minor component of the Z-disc (about 1 per 400 α-actinin) important for myofibrillar development and mechanotransduction.
23271734	3	13	theme	PDZ	758:760	arg1	ZASP					723:726	the protein ZASP	711:726	the protein ZASP (Z-band alternatively spliced PDZ motif protein)	711:775	MALDI-MS/MS identified the 90-kDa band as the protein ZASP (Z-band alternatively spliced PDZ motif protein), a minor component of the Z-disc (about 1 per 400 α-actinin) important for myofibrillar development and mechanotransduction.
23271734	3	14	theme	spliced	750:756	arg1	protein					768:774	Z-band alternatively spliced PDZ motif protein	729:774	Z-band alternatively spliced PDZ motif protein	729:774	MALDI-MS/MS identified the 90-kDa band as the protein ZASP (Z-band alternatively spliced PDZ motif protein), a minor component of the Z-disc (about 1 per 400 α-actinin) important for myofibrillar development and mechanotransduction.
23271734	3	14	theme	spliced	750:756	arg1	ZASP					723:726	the protein ZASP	711:726	the protein ZASP (Z-band alternatively spliced PDZ motif protein)	711:775	MALDI-MS/MS identified the 90-kDa band as the protein ZASP (Z-band alternatively spliced PDZ motif protein), a minor component of the Z-disc (about 1 per 400 α-actinin) important for myofibrillar development and mechanotransduction.
23271734	5	15	theme	myectomy	1167:1174	arg1	samples					1183:1189	myectomy muscle samples	1167:1189	myectomy muscle samples (donor versus myectomy p < 0.05)	1167:1222	O-GlcNAcylation of ZASP increased in diseased heart, being 49 ± 5% of all O-GlcNAc in donor, 68 ± 9% in end-stage failing heart, and 76 ± 6% in myectomy muscle samples (donor versus myectomy p < 0.05).
23271734	5	15	theme	myectomy	1167:1174	arg1	<					1216:1216	donor versus myectomy p < 0.05	1192:1221	<	1216:1216	O-GlcNAcylation of ZASP increased in diseased heart, being 49 ± 5% of all O-GlcNAc in donor, 68 ± 9% in end-stage failing heart, and 76 ± 6% in myectomy muscle samples (donor versus myectomy p < 0.05).
23271734	5	16	from	%	1088:1088	arg1	donor					1109:1113	donor	1109:1113	donor	1109:1113	O-GlcNAcylation of ZASP increased in diseased heart, being 49 ± 5% of all O-GlcNAc in donor, 68 ± 9% in end-stage failing heart, and 76 ± 6% in myectomy muscle samples (donor versus myectomy p < 0.05).
23271734	5	16	from	%	1088:1088	arg1	samples					1183:1189	myectomy muscle samples	1167:1189	myectomy muscle samples (donor versus myectomy p < 0.05)	1167:1222	O-GlcNAcylation of ZASP increased in diseased heart, being 49 ± 5% of all O-GlcNAc in donor, 68 ± 9% in end-stage failing heart, and 76 ± 6% in myectomy muscle samples (donor versus myectomy p < 0.05).
23271734	5	16	from	%	1088:1088	arg1	heart					1145:1149	end-stage failing heart	1127:1149	end-stage failing heart	1127:1149	O-GlcNAcylation of ZASP increased in diseased heart, being 49 ± 5% of all O-GlcNAc in donor, 68 ± 9% in end-stage failing heart, and 76 ± 6% in myectomy muscle samples (donor versus myectomy p < 0.05).
23271734	5	16	from	%	1088:1088	arg1	<					1216:1216	donor versus myectomy p < 0.05	1192:1221	<	1216:1216	O-GlcNAcylation of ZASP increased in diseased heart, being 49 ± 5% of all O-GlcNAc in donor, 68 ± 9% in end-stage failing heart, and 76 ± 6% in myectomy muscle samples (donor versus myectomy p < 0.05).
23271734	3	17	theme	motif	762:766	arg1	protein					768:774	Z-band alternatively spliced PDZ motif protein	729:774	Z-band alternatively spliced PDZ motif protein	729:774	MALDI-MS/MS identified the 90-kDa band as the protein ZASP (Z-band alternatively spliced PDZ motif protein), a minor component of the Z-disc (about 1 per 400 α-actinin) important for myofibrillar development and mechanotransduction.
23271734	3	17	theme	motif	762:766	arg1	ZASP					723:726	the protein ZASP	711:726	the protein ZASP (Z-band alternatively spliced PDZ motif protein)	711:775	MALDI-MS/MS identified the 90-kDa band as the protein ZASP (Z-band alternatively spliced PDZ motif protein), a minor component of the Z-disc (about 1 per 400 α-actinin) important for myofibrillar development and mechanotransduction.
23271734	2	18	dep	bands	588:592	arg1	kDa					598:600	~90 kDa	594:600	bands ~90 kDa	588:600	All three methods showed that O-GlcNAc modification was predominantly in a group of bands ~90 kDa that did not correspond to any of the major myofibrillar proteins.
23271734	6	19	theme	mouse	1276:1280	arg1	myofibrils					1288:1297	mouse heart myofibrils	1276:1297	mouse heart myofibrils	1276:1297	ZASP is only 22% of all O-GlcNAcylated proteins in mouse heart myofibrils.
23271734	2	20	theme	myofibrillar	646:657	arg1	proteins					659:666	the major myofibrillar proteins	636:666	the major myofibrillar proteins	636:666	All three methods showed that O-GlcNAc modification was predominantly in a group of bands ~90 kDa that did not correspond to any of the major myofibrillar proteins.
23271734	1	21	theme	O-GlcNAc	188:195	arg1	modification					198:209	O-linked β-N-acetylglucosamine (O-GlcNAc) modification	156:209	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of contractile proteins in human heart	156:248	We studied O-linked β-N-acetylglucosamine (O-GlcNAc) modification of contractile proteins in human heart using SDS-PAGE and three detection methods: specific enzymatic conjugation of O-GlcNAc with UDP-N-azidoacetylgalactosamine (UDP-GalNAz) that is then linked to a tetramethylrhodamine fluorescent tag and CTD110.6 and RL2 monoclonal antibodies to O-GlcNAc.
23271734	5	22	from	donor	1109:1113	arg1	%					1088:1088	49 ± 5%	1082:1088	49 ± 5% of all O-GlcNAc in donor	1082:1113	O-GlcNAcylation of ZASP increased in diseased heart, being 49 ± 5% of all O-GlcNAc in donor, 68 ± 9% in end-stage failing heart, and 76 ± 6% in myectomy muscle samples (donor versus myectomy p < 0.05).
23271734	5	22	from	donor	1109:1113	arg1	O-GlcNAc					1097:1104	all O-GlcNAc	1093:1104	all O-GlcNAc in donor	1093:1113	O-GlcNAcylation of ZASP increased in diseased heart, being 49 ± 5% of all O-GlcNAc in donor, 68 ± 9% in end-stage failing heart, and 76 ± 6% in myectomy muscle samples (donor versus myectomy p < 0.05).
23271734	5	22	from	donor	1109:1113	arg1	%					1162:1162	76 ± 6%	1156:1162	76 ± 6% in myectomy muscle samples (donor versus myectomy p < 0.05)	1156:1222	O-GlcNAcylation of ZASP increased in diseased heart, being 49 ± 5% of all O-GlcNAc in donor, 68 ± 9% in end-stage failing heart, and 76 ± 6% in myectomy muscle samples (donor versus myectomy p < 0.05).
23271734	5	22	from	donor	1109:1113	arg1	%					1122:1122	68 ± 9%	1116:1122	68 ± 9% in end-stage failing heart	1116:1149	O-GlcNAcylation of ZASP increased in diseased heart, being 49 ± 5% of all O-GlcNAc in donor, 68 ± 9% in end-stage failing heart, and 76 ± 6% in myectomy muscle samples (donor versus myectomy p < 0.05).
23271734	1	23	dep	methods	285:291	arg1	conjugation					313:323	specific enzymatic conjugation	294:323	three detection methods: specific enzymatic conjugation of O-GlcNAc with UDP-N-azidoacetylgalactosamine (UDP-GalNAz) that is then linked to a tetramethylrhodamine fluorescent tag and CTD110.6 and RL2 monoclonal antibodies to O-GlcNAc	269:501	We studied O-linked β-N-acetylglucosamine (O-GlcNAc) modification of contractile proteins in human heart using SDS-PAGE and three detection methods: specific enzymatic conjugation of O-GlcNAc with UDP-N-azidoacetylgalactosamine (UDP-GalNAz) that is then linked to a tetramethylrhodamine fluorescent tag and CTD110.6 and RL2 monoclonal antibodies to O-GlcNAc.
23271734	2	24	theme	major	640:644	arg1	proteins					659:666	the major myofibrillar proteins	636:666	the major myofibrillar proteins	636:666	All three methods showed that O-GlcNAc modification was predominantly in a group of bands ~90 kDa that did not correspond to any of the major myofibrillar proteins.
23271734	1	25	with	conjugation	313:323	arg1	UDP-GalNAz					374:383	UDP-GalNAz	374:383	UDP-GalNAz	374:383	We studied O-linked β-N-acetylglucosamine (O-GlcNAc) modification of contractile proteins in human heart using SDS-PAGE and three detection methods: specific enzymatic conjugation of O-GlcNAc with UDP-N-azidoacetylgalactosamine (UDP-GalNAz) that is then linked to a tetramethylrhodamine fluorescent tag and CTD110.6 and RL2 monoclonal antibodies to O-GlcNAc.
23271734	1	25	with	conjugation	313:323	arg1	UDP-N-azidoacetylgalactosamine					342:371	UDP-N-azidoacetylgalactosamine	342:371	UDP-N-azidoacetylgalactosamine (UDP-GalNAz) that is then linked to a tetramethylrhodamine fluorescent tag and CTD110.6 and RL2 monoclonal antibodies to O-GlcNAc	342:501	We studied O-linked β-N-acetylglucosamine (O-GlcNAc) modification of contractile proteins in human heart using SDS-PAGE and three detection methods: specific enzymatic conjugation of O-GlcNAc with UDP-N-azidoacetylgalactosamine (UDP-GalNAz) that is then linked to a tetramethylrhodamine fluorescent tag and CTD110.6 and RL2 monoclonal antibodies to O-GlcNAc.
23271734	5	26	theme	failing	1137:1143	arg1	heart					1145:1149	end-stage failing heart	1127:1149	end-stage failing heart	1127:1149	O-GlcNAcylation of ZASP increased in diseased heart, being 49 ± 5% of all O-GlcNAc in donor, 68 ± 9% in end-stage failing heart, and 76 ± 6% in myectomy muscle samples (donor versus myectomy p < 0.05).
23271734	0	27	theme	Z-band	0:5	arg1	protein					39:45	Z-band alternatively spliced PDZ motif protein	0:45	Z-band alternatively spliced PDZ motif protein (ZASP)	0:52	Z-band alternatively spliced PDZ motif protein (ZASP) is the major O-linked β-N-acetylglucosamine-substituted protein in human heart myofibrils.
23271734	0	27	theme	Z-band	0:5	arg1	protein					110:116	the major O-linked β-N-acetylglucosamine-substituted protein	57:116	the major O-linked β-N-acetylglucosamine-substituted protein in human heart myofibrils	57:142	Z-band alternatively spliced PDZ motif protein (ZASP) is the major O-linked β-N-acetylglucosamine-substituted protein in human heart myofibrils.
23271734	0	27	theme	Z-band	0:5	arg1	ZASP					48:51	ZASP	48:51	ZASP	48:51	Z-band alternatively spliced PDZ motif protein (ZASP) is the major O-linked β-N-acetylglucosamine-substituted protein in human heart myofibrils.
23271734	6	28	theme	proteins	1264:1271	arg1	%					1240:1240	only 22%	1233:1240	only 22% of all O-GlcNAcylated proteins in mouse heart myofibrils	1233:1297	ZASP is only 22% of all O-GlcNAcylated proteins in mouse heart myofibrils.
23271734	6	28	theme	proteins	1264:1271	arg1	proteins					1264:1271	all O-GlcNAcylated proteins	1245:1271	all O-GlcNAcylated proteins	1245:1271	ZASP is only 22% of all O-GlcNAcylated proteins in mouse heart myofibrils.
23271734	5	29	theme	±	1085:1085	arg1	%					1088:1088	49 ± 5%	1082:1088	49 ± 5% of all O-GlcNAc in donor	1082:1113	O-GlcNAcylation of ZASP increased in diseased heart, being 49 ± 5% of all O-GlcNAc in donor, 68 ± 9% in end-stage failing heart, and 76 ± 6% in myectomy muscle samples (donor versus myectomy p < 0.05).
23271734	5	29	theme	±	1085:1085	arg1	O-GlcNAc					1097:1104	all O-GlcNAc	1093:1104	all O-GlcNAc in donor	1093:1113	O-GlcNAcylation of ZASP increased in diseased heart, being 49 ± 5% of all O-GlcNAc in donor, 68 ± 9% in end-stage failing heart, and 76 ± 6% in myectomy muscle samples (donor versus myectomy p < 0.05).
23271734	6	30	theme	O-GlcNAcylated	1249:1262	arg1	proteins					1264:1271	all O-GlcNAcylated proteins	1245:1271	all O-GlcNAcylated proteins	1245:1271	ZASP is only 22% of all O-GlcNAcylated proteins in mouse heart myofibrils.
23271734	0	31	theme	PDZ	29:31	arg1	protein					39:45	Z-band alternatively spliced PDZ motif protein	0:45	Z-band alternatively spliced PDZ motif protein (ZASP)	0:52	Z-band alternatively spliced PDZ motif protein (ZASP) is the major O-linked β-N-acetylglucosamine-substituted protein in human heart myofibrils.
23271734	0	31	theme	PDZ	29:31	arg1	protein					110:116	the major O-linked β-N-acetylglucosamine-substituted protein	57:116	the major O-linked β-N-acetylglucosamine-substituted protein in human heart myofibrils	57:142	Z-band alternatively spliced PDZ motif protein (ZASP) is the major O-linked β-N-acetylglucosamine-substituted protein in human heart myofibrils.
23271734	0	31	theme	PDZ	29:31	arg1	ZASP					48:51	ZASP	48:51	ZASP	48:51	Z-band alternatively spliced PDZ motif protein (ZASP) is the major O-linked β-N-acetylglucosamine-substituted protein in human heart myofibrils.
23271734	1	32	theme	specific	294:301	arg1	conjugation					313:323	specific enzymatic conjugation	294:323	three detection methods: specific enzymatic conjugation of O-GlcNAc with UDP-N-azidoacetylgalactosamine (UDP-GalNAz) that is then linked to a tetramethylrhodamine fluorescent tag and CTD110.6 and RL2 monoclonal antibodies to O-GlcNAc	269:501	We studied O-linked β-N-acetylglucosamine (O-GlcNAc) modification of contractile proteins in human heart using SDS-PAGE and three detection methods: specific enzymatic conjugation of O-GlcNAc with UDP-N-azidoacetylgalactosamine (UDP-GalNAz) that is then linked to a tetramethylrhodamine fluorescent tag and CTD110.6 and RL2 monoclonal antibodies to O-GlcNAc.
23271734	1	33	link	O-linked	156:163	arg1	modification					198:209	O-linked β-N-acetylglucosamine (O-GlcNAc) modification	156:209	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of contractile proteins in human heart	156:248	We studied O-linked β-N-acetylglucosamine (O-GlcNAc) modification of contractile proteins in human heart using SDS-PAGE and three detection methods: specific enzymatic conjugation of O-GlcNAc with UDP-N-azidoacetylgalactosamine (UDP-GalNAz) that is then linked to a tetramethylrhodamine fluorescent tag and CTD110.6 and RL2 monoclonal antibodies to O-GlcNAc.
23271734	0	34	theme	spliced	21:27	arg1	protein					39:45	Z-band alternatively spliced PDZ motif protein	0:45	Z-band alternatively spliced PDZ motif protein (ZASP)	0:52	Z-band alternatively spliced PDZ motif protein (ZASP) is the major O-linked β-N-acetylglucosamine-substituted protein in human heart myofibrils.
23271734	0	34	theme	spliced	21:27	arg1	protein					110:116	the major O-linked β-N-acetylglucosamine-substituted protein	57:116	the major O-linked β-N-acetylglucosamine-substituted protein in human heart myofibrils	57:142	Z-band alternatively spliced PDZ motif protein (ZASP) is the major O-linked β-N-acetylglucosamine-substituted protein in human heart myofibrils.
23271734	0	34	theme	spliced	21:27	arg1	ZASP					48:51	ZASP	48:51	ZASP	48:51	Z-band alternatively spliced PDZ motif protein (ZASP) is the major O-linked β-N-acetylglucosamine-substituted protein in human heart myofibrils.
23271734	1	35	theme	enzymatic	303:311	arg1	conjugation					313:323	specific enzymatic conjugation	294:323	three detection methods: specific enzymatic conjugation of O-GlcNAc with UDP-N-azidoacetylgalactosamine (UDP-GalNAz) that is then linked to a tetramethylrhodamine fluorescent tag and CTD110.6 and RL2 monoclonal antibodies to O-GlcNAc	269:501	We studied O-linked β-N-acetylglucosamine (O-GlcNAc) modification of contractile proteins in human heart using SDS-PAGE and three detection methods: specific enzymatic conjugation of O-GlcNAc with UDP-N-azidoacetylgalactosamine (UDP-GalNAz) that is then linked to a tetramethylrhodamine fluorescent tag and CTD110.6 and RL2 monoclonal antibodies to O-GlcNAc.
23271734	0	36	theme	human	121:125	arg1	myofibrils					133:142	human heart myofibrils	121:142	human heart myofibrils	121:142	Z-band alternatively spliced PDZ motif protein (ZASP) is the major O-linked β-N-acetylglucosamine-substituted protein in human heart myofibrils.
23271734	5	37	from	%	1122:1122	arg1	donor					1109:1113	donor	1109:1113	donor	1109:1113	O-GlcNAcylation of ZASP increased in diseased heart, being 49 ± 5% of all O-GlcNAc in donor, 68 ± 9% in end-stage failing heart, and 76 ± 6% in myectomy muscle samples (donor versus myectomy p < 0.05).
23271734	5	37	from	%	1122:1122	arg1	samples					1183:1189	myectomy muscle samples	1167:1189	myectomy muscle samples (donor versus myectomy p < 0.05)	1167:1222	O-GlcNAcylation of ZASP increased in diseased heart, being 49 ± 5% of all O-GlcNAc in donor, 68 ± 9% in end-stage failing heart, and 76 ± 6% in myectomy muscle samples (donor versus myectomy p < 0.05).
23271734	5	37	from	%	1122:1122	arg1	heart					1145:1149	end-stage failing heart	1127:1149	end-stage failing heart	1127:1149	O-GlcNAcylation of ZASP increased in diseased heart, being 49 ± 5% of all O-GlcNAc in donor, 68 ± 9% in end-stage failing heart, and 76 ± 6% in myectomy muscle samples (donor versus myectomy p < 0.05).
23271734	5	37	from	%	1122:1122	arg1	<					1216:1216	donor versus myectomy p < 0.05	1192:1221	<	1216:1216	O-GlcNAcylation of ZASP increased in diseased heart, being 49 ± 5% of all O-GlcNAc in donor, 68 ± 9% in end-stage failing heart, and 76 ± 6% in myectomy muscle samples (donor versus myectomy p < 0.05).
23271734	1	38	theme	β-N-acetylglucosamine	165:185	arg1	modification					198:209	O-linked β-N-acetylglucosamine (O-GlcNAc) modification	156:209	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of contractile proteins in human heart	156:248	We studied O-linked β-N-acetylglucosamine (O-GlcNAc) modification of contractile proteins in human heart using SDS-PAGE and three detection methods: specific enzymatic conjugation of O-GlcNAc with UDP-N-azidoacetylgalactosamine (UDP-GalNAz) that is then linked to a tetramethylrhodamine fluorescent tag and CTD110.6 and RL2 monoclonal antibodies to O-GlcNAc.
23271734	6	39	theme	heart	1282:1286	arg1	myofibrils					1288:1297	mouse heart myofibrils	1276:1297	mouse heart myofibrils	1276:1297	ZASP is only 22% of all O-GlcNAcylated proteins in mouse heart myofibrils.
23271734	1	40	theme	contractile	214:224	arg1	proteins					226:233	contractile proteins	214:233	contractile proteins in human heart	214:248	We studied O-linked β-N-acetylglucosamine (O-GlcNAc) modification of contractile proteins in human heart using SDS-PAGE and three detection methods: specific enzymatic conjugation of O-GlcNAc with UDP-N-azidoacetylgalactosamine (UDP-GalNAz) that is then linked to a tetramethylrhodamine fluorescent tag and CTD110.6 and RL2 monoclonal antibodies to O-GlcNAc.
23271734	5	41	theme	±	1159:1159	arg1	O-GlcNAc					1097:1104	all O-GlcNAc	1093:1104	all O-GlcNAc in donor	1093:1113	O-GlcNAcylation of ZASP increased in diseased heart, being 49 ± 5% of all O-GlcNAc in donor, 68 ± 9% in end-stage failing heart, and 76 ± 6% in myectomy muscle samples (donor versus myectomy p < 0.05).
23271734	5	41	theme	±	1159:1159	arg1	%					1162:1162	76 ± 6%	1156:1162	76 ± 6% in myectomy muscle samples (donor versus myectomy p < 0.05)	1156:1222	O-GlcNAcylation of ZASP increased in diseased heart, being 49 ± 5% of all O-GlcNAc in donor, 68 ± 9% in end-stage failing heart, and 76 ± 6% in myectomy muscle samples (donor versus myectomy p < 0.05).
23271734	1	42	theme	tetramethylrhodamine	411:430	arg1	tag					444:446	a tetramethylrhodamine fluorescent tag	409:446	a tetramethylrhodamine fluorescent tag	409:446	We studied O-linked β-N-acetylglucosamine (O-GlcNAc) modification of contractile proteins in human heart using SDS-PAGE and three detection methods: specific enzymatic conjugation of O-GlcNAc with UDP-N-azidoacetylgalactosamine (UDP-GalNAz) that is then linked to a tetramethylrhodamine fluorescent tag and CTD110.6 and RL2 monoclonal antibodies to O-GlcNAc.
23271734	1	43	theme	proteins	226:233	arg1	modification					198:209	O-linked β-N-acetylglucosamine (O-GlcNAc) modification	156:209	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of contractile proteins in human heart	156:248	We studied O-linked β-N-acetylglucosamine (O-GlcNAc) modification of contractile proteins in human heart using SDS-PAGE and three detection methods: specific enzymatic conjugation of O-GlcNAc with UDP-N-azidoacetylgalactosamine (UDP-GalNAz) that is then linked to a tetramethylrhodamine fluorescent tag and CTD110.6 and RL2 monoclonal antibodies to O-GlcNAc.
23271734	0	44	theme	motif	33:37	arg1	protein					39:45	Z-band alternatively spliced PDZ motif protein	0:45	Z-band alternatively spliced PDZ motif protein (ZASP)	0:52	Z-band alternatively spliced PDZ motif protein (ZASP) is the major O-linked β-N-acetylglucosamine-substituted protein in human heart myofibrils.
23271734	0	44	theme	motif	33:37	arg1	protein					110:116	the major O-linked β-N-acetylglucosamine-substituted protein	57:116	the major O-linked β-N-acetylglucosamine-substituted protein in human heart myofibrils	57:142	Z-band alternatively spliced PDZ motif protein (ZASP) is the major O-linked β-N-acetylglucosamine-substituted protein in human heart myofibrils.
23271734	0	44	theme	motif	33:37	arg1	ZASP					48:51	ZASP	48:51	ZASP	48:51	Z-band alternatively spliced PDZ motif protein (ZASP) is the major O-linked β-N-acetylglucosamine-substituted protein in human heart myofibrils.
23271734	4	45	theme	immunofluorescence	992:1009	arg1	microscopy					1011:1020	immunofluorescence microscopy	992:1020	immunofluorescence microscopy	992:1020	This was confirmed by the co-localization of O-GlcNAc and ZASP in Western blotting and by immunofluorescence microscopy.
23271734	4	46	theme	O-GlcNAc	947:954	arg1	co-localization					928:942	the co-localization	924:942	the co-localization of O-GlcNAc and ZASP in Western blotting and by immunofluorescence microscopy	924:1020	This was confirmed by the co-localization of O-GlcNAc and ZASP in Western blotting and by immunofluorescence microscopy.
23271734	1	47	theme	fluorescent	432:442	arg1	tag					444:446	a tetramethylrhodamine fluorescent tag	409:446	a tetramethylrhodamine fluorescent tag	409:446	We studied O-linked β-N-acetylglucosamine (O-GlcNAc) modification of contractile proteins in human heart using SDS-PAGE and three detection methods: specific enzymatic conjugation of O-GlcNAc with UDP-N-azidoacetylgalactosamine (UDP-GalNAz) that is then linked to a tetramethylrhodamine fluorescent tag and CTD110.6 and RL2 monoclonal antibodies to O-GlcNAc.
23271734	5	48	from	O-GlcNAc	1097:1104	arg1	donor					1109:1113	donor	1109:1113	donor	1109:1113	O-GlcNAcylation of ZASP increased in diseased heart, being 49 ± 5% of all O-GlcNAc in donor, 68 ± 9% in end-stage failing heart, and 76 ± 6% in myectomy muscle samples (donor versus myectomy p < 0.05).
23271734	1	49	from	proteins	226:233	arg1	heart					244:248	human heart	238:248	human heart	238:248	We studied O-linked β-N-acetylglucosamine (O-GlcNAc) modification of contractile proteins in human heart using SDS-PAGE and three detection methods: specific enzymatic conjugation of O-GlcNAc with UDP-N-azidoacetylgalactosamine (UDP-GalNAz) that is then linked to a tetramethylrhodamine fluorescent tag and CTD110.6 and RL2 monoclonal antibodies to O-GlcNAc.
23271734	4	50	theme	Western	968:974	arg1	blotting					976:983	Western blotting	968:983	Western blotting	968:983	This was confirmed by the co-localization of O-GlcNAc and ZASP in Western blotting and by immunofluorescence microscopy.
23271734	1	51	theme	O-GlcNAc	328:335	arg1	conjugation					313:323	specific enzymatic conjugation	294:323	three detection methods: specific enzymatic conjugation of O-GlcNAc with UDP-N-azidoacetylgalactosamine (UDP-GalNAz) that is then linked to a tetramethylrhodamine fluorescent tag and CTD110.6 and RL2 monoclonal antibodies to O-GlcNAc	269:501	We studied O-linked β-N-acetylglucosamine (O-GlcNAc) modification of contractile proteins in human heart using SDS-PAGE and three detection methods: specific enzymatic conjugation of O-GlcNAc with UDP-N-azidoacetylgalactosamine (UDP-GalNAz) that is then linked to a tetramethylrhodamine fluorescent tag and CTD110.6 and RL2 monoclonal antibodies to O-GlcNAc.
23271734	5	52	theme	O-GlcNAc	1097:1104	arg1	%					1088:1088	49 ± 5%	1082:1088	49 ± 5% of all O-GlcNAc in donor	1082:1113	O-GlcNAcylation of ZASP increased in diseased heart, being 49 ± 5% of all O-GlcNAc in donor, 68 ± 9% in end-stage failing heart, and 76 ± 6% in myectomy muscle samples (donor versus myectomy p < 0.05).
23271734	5	52	theme	O-GlcNAc	1097:1104	arg1	O-GlcNAc					1097:1104	all O-GlcNAc	1093:1104	all O-GlcNAc in donor	1093:1113	O-GlcNAcylation of ZASP increased in diseased heart, being 49 ± 5% of all O-GlcNAc in donor, 68 ± 9% in end-stage failing heart, and 76 ± 6% in myectomy muscle samples (donor versus myectomy p < 0.05).
23271734	5	52	theme	O-GlcNAc	1097:1104	arg1	%					1162:1162	76 ± 6%	1156:1162	76 ± 6% in myectomy muscle samples (donor versus myectomy p < 0.05)	1156:1222	O-GlcNAcylation of ZASP increased in diseased heart, being 49 ± 5% of all O-GlcNAc in donor, 68 ± 9% in end-stage failing heart, and 76 ± 6% in myectomy muscle samples (donor versus myectomy p < 0.05).
23271734	5	52	theme	O-GlcNAc	1097:1104	arg1	%					1122:1122	68 ± 9%	1116:1122	68 ± 9% in end-stage failing heart	1116:1149	O-GlcNAcylation of ZASP increased in diseased heart, being 49 ± 5% of all O-GlcNAc in donor, 68 ± 9% in end-stage failing heart, and 76 ± 6% in myectomy muscle samples (donor versus myectomy p < 0.05).
23271734	4	53	from	co-localization	928:942	arg1	blotting					976:983	Western blotting	968:983	Western blotting	968:983	This was confirmed by the co-localization of O-GlcNAc and ZASP in Western blotting and by immunofluorescence microscopy.
23271734	5	54	theme	diseased	1060:1067	arg1	heart					1069:1073	diseased heart	1060:1073	diseased heart	1060:1073	O-GlcNAcylation of ZASP increased in diseased heart, being 49 ± 5% of all O-GlcNAc in donor, 68 ± 9% in end-stage failing heart, and 76 ± 6% in myectomy muscle samples (donor versus myectomy p < 0.05).
23271734	1	55	mod	modification	198:209	arg3	β-N-acetylglucosamine					165:185	O-linked β-N-acetylglucosamine (O-GlcNAc) modification	156:209	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of contractile proteins in human heart	156:248	We studied O-linked β-N-acetylglucosamine (O-GlcNAc) modification of contractile proteins in human heart using SDS-PAGE and three detection methods: specific enzymatic conjugation of O-GlcNAc with UDP-N-azidoacetylgalactosamine (UDP-GalNAz) that is then linked to a tetramethylrhodamine fluorescent tag and CTD110.6 and RL2 monoclonal antibodies to O-GlcNAc.
23271734	1	55	mod	modification	198:209	arg3	O-GlcNAc					188:195	O-linked β-N-acetylglucosamine (O-GlcNAc) modification	156:209	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of contractile proteins in human heart	156:248	We studied O-linked β-N-acetylglucosamine (O-GlcNAc) modification of contractile proteins in human heart using SDS-PAGE and three detection methods: specific enzymatic conjugation of O-GlcNAc with UDP-N-azidoacetylgalactosamine (UDP-GalNAz) that is then linked to a tetramethylrhodamine fluorescent tag and CTD110.6 and RL2 monoclonal antibodies to O-GlcNAc.
23271734	1	55	mod	modification	198:209	arg1	proteins					226:233	contractile proteins	214:233	contractile proteins in human heart	214:248	We studied O-linked β-N-acetylglucosamine (O-GlcNAc) modification of contractile proteins in human heart using SDS-PAGE and three detection methods: specific enzymatic conjugation of O-GlcNAc with UDP-N-azidoacetylgalactosamine (UDP-GalNAz) that is then linked to a tetramethylrhodamine fluorescent tag and CTD110.6 and RL2 monoclonal antibodies to O-GlcNAc.
23271734	5	56	from	%	1162:1162	arg1	donor					1109:1113	donor	1109:1113	donor	1109:1113	O-GlcNAcylation of ZASP increased in diseased heart, being 49 ± 5% of all O-GlcNAc in donor, 68 ± 9% in end-stage failing heart, and 76 ± 6% in myectomy muscle samples (donor versus myectomy p < 0.05).
23271734	5	56	from	%	1162:1162	arg1	samples					1183:1189	myectomy muscle samples	1167:1189	myectomy muscle samples (donor versus myectomy p < 0.05)	1167:1222	O-GlcNAcylation of ZASP increased in diseased heart, being 49 ± 5% of all O-GlcNAc in donor, 68 ± 9% in end-stage failing heart, and 76 ± 6% in myectomy muscle samples (donor versus myectomy p < 0.05).
23271734	5	56	from	%	1162:1162	arg1	heart					1145:1149	end-stage failing heart	1127:1149	end-stage failing heart	1127:1149	O-GlcNAcylation of ZASP increased in diseased heart, being 49 ± 5% of all O-GlcNAc in donor, 68 ± 9% in end-stage failing heart, and 76 ± 6% in myectomy muscle samples (donor versus myectomy p < 0.05).
23271734	5	56	from	%	1162:1162	arg1	<					1216:1216	donor versus myectomy p < 0.05	1192:1221	<	1216:1216	O-GlcNAcylation of ZASP increased in diseased heart, being 49 ± 5% of all O-GlcNAc in donor, 68 ± 9% in end-stage failing heart, and 76 ± 6% in myectomy muscle samples (donor versus myectomy p < 0.05).
23271734	3	57	theme	minor	780:784	arg1	component					786:794	a minor component	778:794	a minor component of the Z-disc (about 1 per 400 α-actinin) important for myofibrillar development and mechanotransduction	778:899	MALDI-MS/MS identified the 90-kDa band as the protein ZASP (Z-band alternatively spliced PDZ motif protein), a minor component of the Z-disc (about 1 per 400 α-actinin) important for myofibrillar development and mechanotransduction.
23271734	3	57	theme	minor	780:784	arg1	ZASP					723:726	the protein ZASP	711:726	the protein ZASP (Z-band alternatively spliced PDZ motif protein)	711:775	MALDI-MS/MS identified the 90-kDa band as the protein ZASP (Z-band alternatively spliced PDZ motif protein), a minor component of the Z-disc (about 1 per 400 α-actinin) important for myofibrillar development and mechanotransduction.
23271734	0	58	theme	heart	127:131	arg1	myofibrils					133:142	human heart myofibrils	121:142	human heart myofibrils	121:142	Z-band alternatively spliced PDZ motif protein (ZASP) is the major O-linked β-N-acetylglucosamine-substituted protein in human heart myofibrils.
23271734	1	59	theme	CTD110.6	452:459	arg1	antibodies					480:489	CTD110.6 and RL2 monoclonal antibodies	452:489	CTD110.6 and RL2 monoclonal antibodies to O-GlcNAc	452:501	We studied O-linked β-N-acetylglucosamine (O-GlcNAc) modification of contractile proteins in human heart using SDS-PAGE and three detection methods: specific enzymatic conjugation of O-GlcNAc with UDP-N-azidoacetylgalactosamine (UDP-GalNAz) that is then linked to a tetramethylrhodamine fluorescent tag and CTD110.6 and RL2 monoclonal antibodies to O-GlcNAc.
23271734	2	60	theme	~90	594:596	arg1	kDa					598:600	~90 kDa	594:600	bands ~90 kDa	588:600	All three methods showed that O-GlcNAc modification was predominantly in a group of bands ~90 kDa that did not correspond to any of the major myofibrillar proteins.
23271734	3	61	theme	myofibrillar	852:863	arg1	development					865:875	myofibrillar development	852:875	myofibrillar development	852:875	MALDI-MS/MS identified the 90-kDa band as the protein ZASP (Z-band alternatively spliced PDZ motif protein), a minor component of the Z-disc (about 1 per 400 α-actinin) important for myofibrillar development and mechanotransduction.
23271734	5	62	theme	ZASP	1042:1045	arg1	O-GlcNAcylation					1023:1037	O-GlcNAcylation	1023:1037	O-GlcNAcylation of ZASP	1023:1045	O-GlcNAcylation of ZASP increased in diseased heart, being 49 ± 5% of all O-GlcNAc in donor, 68 ± 9% in end-stage failing heart, and 76 ± 6% in myectomy muscle samples (donor versus myectomy p < 0.05).
23271734	0	63	from	protein	110:116	arg1	myofibrils					133:142	human heart myofibrils	121:142	human heart myofibrils	121:142	Z-band alternatively spliced PDZ motif protein (ZASP) is the major O-linked β-N-acetylglucosamine-substituted protein in human heart myofibrils.
23271734	1	64	theme	human	238:242	arg1	heart					244:248	human heart	238:248	human heart	238:248	We studied O-linked β-N-acetylglucosamine (O-GlcNAc) modification of contractile proteins in human heart using SDS-PAGE and three detection methods: specific enzymatic conjugation of O-GlcNAc with UDP-N-azidoacetylgalactosamine (UDP-GalNAz) that is then linked to a tetramethylrhodamine fluorescent tag and CTD110.6 and RL2 monoclonal antibodies to O-GlcNAc.
23271734	1	65	from	heart	244:248	arg1	modification					198:209	O-linked β-N-acetylglucosamine (O-GlcNAc) modification	156:209	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of contractile proteins in human heart	156:248	We studied O-linked β-N-acetylglucosamine (O-GlcNAc) modification of contractile proteins in human heart using SDS-PAGE and three detection methods: specific enzymatic conjugation of O-GlcNAc with UDP-N-azidoacetylgalactosamine (UDP-GalNAz) that is then linked to a tetramethylrhodamine fluorescent tag and CTD110.6 and RL2 monoclonal antibodies to O-GlcNAc.
23271734	3	66	theme	90-kDa	696:701	arg1	band					703:706	the 90-kDa band	692:706	the 90-kDa band	692:706	MALDI-MS/MS identified the 90-kDa band as the protein ZASP (Z-band alternatively spliced PDZ motif protein), a minor component of the Z-disc (about 1 per 400 α-actinin) important for myofibrillar development and mechanotransduction.
23271734	3	66	theme	90-kDa	696:701	arg1	ZASP					723:726	the protein ZASP	711:726	the protein ZASP (Z-band alternatively spliced PDZ motif protein)	711:775	MALDI-MS/MS identified the 90-kDa band as the protein ZASP (Z-band alternatively spliced PDZ motif protein), a minor component of the Z-disc (about 1 per 400 α-actinin) important for myofibrillar development and mechanotransduction.
23271734	3	67	theme	important	838:846	arg1	Z-disc					803:808	the Z-disc	799:808	the Z-disc (about 1 per 400 α-actinin) important for myofibrillar development and mechanotransduction	799:899	MALDI-MS/MS identified the 90-kDa band as the protein ZASP (Z-band alternatively spliced PDZ motif protein), a minor component of the Z-disc (about 1 per 400 α-actinin) important for myofibrillar development and mechanotransduction.
23271734	3	67	theme	important	838:846	arg1	α-actinin					827:835	about 1 per 400 α-actinin	811:835	about 1 per 400 α-actinin	811:835	MALDI-MS/MS identified the 90-kDa band as the protein ZASP (Z-band alternatively spliced PDZ motif protein), a minor component of the Z-disc (about 1 per 400 α-actinin) important for myofibrillar development and mechanotransduction.
23271734	1	68	theme	RL2	465:467	arg1	antibodies					480:489	CTD110.6 and RL2 monoclonal antibodies	452:489	CTD110.6 and RL2 monoclonal antibodies to O-GlcNAc	452:501	We studied O-linked β-N-acetylglucosamine (O-GlcNAc) modification of contractile proteins in human heart using SDS-PAGE and three detection methods: specific enzymatic conjugation of O-GlcNAc with UDP-N-azidoacetylgalactosamine (UDP-GalNAz) that is then linked to a tetramethylrhodamine fluorescent tag and CTD110.6 and RL2 monoclonal antibodies to O-GlcNAc.
23271734	6	69	from	%	1240:1240	arg1	myofibrils					1288:1297	mouse heart myofibrils	1276:1297	mouse heart myofibrils	1276:1297	ZASP is only 22% of all O-GlcNAcylated proteins in mouse heart myofibrils.
23271734	1	70	from	modification	198:209	arg1	heart					244:248	human heart	238:248	human heart	238:248	We studied O-linked β-N-acetylglucosamine (O-GlcNAc) modification of contractile proteins in human heart using SDS-PAGE and three detection methods: specific enzymatic conjugation of O-GlcNAc with UDP-N-azidoacetylgalactosamine (UDP-GalNAz) that is then linked to a tetramethylrhodamine fluorescent tag and CTD110.6 and RL2 monoclonal antibodies to O-GlcNAc.
23271734	5	71	theme	±	1119:1119	arg1	O-GlcNAc					1097:1104	all O-GlcNAc	1093:1104	all O-GlcNAc in donor	1093:1113	O-GlcNAcylation of ZASP increased in diseased heart, being 49 ± 5% of all O-GlcNAc in donor, 68 ± 9% in end-stage failing heart, and 76 ± 6% in myectomy muscle samples (donor versus myectomy p < 0.05).
23271734	5	71	theme	±	1119:1119	arg1	%					1122:1122	68 ± 9%	1116:1122	68 ± 9% in end-stage failing heart	1116:1149	O-GlcNAcylation of ZASP increased in diseased heart, being 49 ± 5% of all O-GlcNAc in donor, 68 ± 9% in end-stage failing heart, and 76 ± 6% in myectomy muscle samples (donor versus myectomy p < 0.05).
23271734	3	72	theme	Z-disc	803:808	arg1	component					786:794	a minor component	778:794	a minor component of the Z-disc (about 1 per 400 α-actinin) important for myofibrillar development and mechanotransduction	778:899	MALDI-MS/MS identified the 90-kDa band as the protein ZASP (Z-band alternatively spliced PDZ motif protein), a minor component of the Z-disc (about 1 per 400 α-actinin) important for myofibrillar development and mechanotransduction.
23271734	3	72	theme	Z-disc	803:808	arg1	ZASP					723:726	the protein ZASP	711:726	the protein ZASP (Z-band alternatively spliced PDZ motif protein)	711:775	MALDI-MS/MS identified the 90-kDa band as the protein ZASP (Z-band alternatively spliced PDZ motif protein), a minor component of the Z-disc (about 1 per 400 α-actinin) important for myofibrillar development and mechanotransduction.
23271734	2	73	theme	O-GlcNAc	534:541	arg1	modification					543:554	O-GlcNAc modification	534:554	O-GlcNAc modification	534:554	All three methods showed that O-GlcNAc modification was predominantly in a group of bands ~90 kDa that did not correspond to any of the major myofibrillar proteins.
23271734	5	74	theme	end-stage	1127:1135	arg1	heart					1145:1149	end-stage failing heart	1127:1149	end-stage failing heart	1127:1149	O-GlcNAcylation of ZASP increased in diseased heart, being 49 ± 5% of all O-GlcNAc in donor, 68 ± 9% in end-stage failing heart, and 76 ± 6% in myectomy muscle samples (donor versus myectomy p < 0.05).
23271734	5	75	theme	donor	1192:1196	arg1	samples					1183:1189	myectomy muscle samples	1167:1189	myectomy muscle samples (donor versus myectomy p < 0.05)	1167:1222	O-GlcNAcylation of ZASP increased in diseased heart, being 49 ± 5% of all O-GlcNAc in donor, 68 ± 9% in end-stage failing heart, and 76 ± 6% in myectomy muscle samples (donor versus myectomy p < 0.05).
23271734	5	75	theme	donor	1192:1196	arg1	<					1216:1216	donor versus myectomy p < 0.05	1192:1221	<	1216:1216	O-GlcNAcylation of ZASP increased in diseased heart, being 49 ± 5% of all O-GlcNAc in donor, 68 ± 9% in end-stage failing heart, and 76 ± 6% in myectomy muscle samples (donor versus myectomy p < 0.05).
23271734	5	76	theme	muscle	1176:1181	arg1	samples					1183:1189	myectomy muscle samples	1167:1189	myectomy muscle samples (donor versus myectomy p < 0.05)	1167:1222	O-GlcNAcylation of ZASP increased in diseased heart, being 49 ± 5% of all O-GlcNAc in donor, 68 ± 9% in end-stage failing heart, and 76 ± 6% in myectomy muscle samples (donor versus myectomy p < 0.05).
23271734	5	76	theme	muscle	1176:1181	arg1	<					1216:1216	donor versus myectomy p < 0.05	1192:1221	<	1216:1216	O-GlcNAcylation of ZASP increased in diseased heart, being 49 ± 5% of all O-GlcNAc in donor, 68 ± 9% in end-stage failing heart, and 76 ± 6% in myectomy muscle samples (donor versus myectomy p < 0.05).
23271734	4	77	theme	ZASP	960:963	arg1	co-localization					928:942	the co-localization	924:942	the co-localization of O-GlcNAc and ZASP in Western blotting and by immunofluorescence microscopy	924:1020	This was confirmed by the co-localization of O-GlcNAc and ZASP in Western blotting and by immunofluorescence microscopy.
36032089	6	0	from	production	1011:1020	arg1	RASFs					1031:1035	human RASFs	1025:1035	human RASFs	1025:1035	Pretreatment of RASFs with Thiamet G, an inhibitor of O-GlcNAcase, markedly increased the O-GlcNAc-modified proteins and concomitantly inhibited the IL-1β-induced IL-6 and IL-8 production in human RASFs in vitro.
36032089	8	1	with	autophosphorylation	1323:1341	arg1	kinase					1299:1304	TGF β-activated kinase 1	1283:1306	TGF β-activated kinase 1 (TAK1)	1283:1313	Immunoprecipitation analysis showed that PGG inhibited O-GlcNAcylation of TAB1 to reduce its association with TGF β-activated kinase 1 (TAK1) and its autophosphorylation, an essential signaling step in IL-1β-induced signaling pathways.
36032089	8	1	with	autophosphorylation	1323:1341	arg1	TAK1					1309:1312	TAK1	1309:1312	TAK1	1309:1312	Immunoprecipitation analysis showed that PGG inhibited O-GlcNAcylation of TAB1 to reduce its association with TGF β-activated kinase 1 (TAK1) and its autophosphorylation, an essential signaling step in IL-1β-induced signaling pathways.
36032089	5	2	theme	Human	709:713	arg1	tissues					724:730	Human synovial tissues	709:730	Human synovial tissues	709:730	Human synovial tissues and RASFs exhibited higher expression of O-GlcNAcylation compared to their non-diseased counterparts.
36032089	6	3	theme	O-GlcNAcase	888:898	arg1	G					869:869	Thiamet G	861:869	Thiamet G	861:869	Pretreatment of RASFs with Thiamet G, an inhibitor of O-GlcNAcase, markedly increased the O-GlcNAc-modified proteins and concomitantly inhibited the IL-1β-induced IL-6 and IL-8 production in human RASFs in vitro.
36032089	6	3	theme	O-GlcNAcase	888:898	arg1	inhibitor					875:883	an inhibitor	872:883	an inhibitor of O-GlcNAcase	872:898	Pretreatment of RASFs with Thiamet G, an inhibitor of O-GlcNAcase, markedly increased the O-GlcNAc-modified proteins and concomitantly inhibited the IL-1β-induced IL-6 and IL-8 production in human RASFs in vitro.
36032089	12	4	theme	therapeutic	2066:2076	arg1	efficacy					2078:2085	their therapeutic efficacy	2060:2085	their therapeutic efficacy	2060:2085	These findings suggest O-GlcNAcylation as a potential therapeutic target and provide the rationale for testing PGG or structurally similar molecule for their therapeutic efficacy.
36032089	3	5	link	patient-derived	500:514	arg1	RASFs					538:542	RASFs	538:542	RASFs	538:542	This study was designed to examine the role of O-GlcNAcylation in rheumatoid arthritis (RA) and its regulation using human RA patient-derived synovial fibroblasts (RASFs).
36032089	3	5	link	patient-derived	500:514	arg1	fibroblasts					525:535	human RA patient-derived synovial fibroblasts	491:535	human RA patient-derived synovial fibroblasts (RASFs)	491:543	This study was designed to examine the role of O-GlcNAcylation in rheumatoid arthritis (RA) and its regulation using human RA patient-derived synovial fibroblasts (RASFs).
36032089	6	6	theme	IL-1β-induced	983:995	arg1	IL-6					997:1000	IL-1β-induced IL-6	983:1000	IL-1β-induced IL-6	983:1000	Pretreatment of RASFs with Thiamet G, an inhibitor of O-GlcNAcase, markedly increased the O-GlcNAc-modified proteins and concomitantly inhibited the IL-1β-induced IL-6 and IL-8 production in human RASFs in vitro.
36032089	11	7	theme	TAK1	1742:1745	arg1	phosphorylation					1723:1737	the phosphorylation	1719:1737	the phosphorylation of TAK1 in the treated joints	1719:1767	PGG treatment reduced the phosphorylation of TAK1 in the treated joints compared to AIA joints, which correlated with the reduced disease severity and suppressed levels of serum IL-1β, GM-CSF, TNF-α, and RANKL.
36032089	8	8	theme	β-activated	1287:1297	arg1	kinase					1299:1304	TGF β-activated kinase 1	1283:1306	TGF β-activated kinase 1 (TAK1)	1283:1313	Immunoprecipitation analysis showed that PGG inhibited O-GlcNAcylation of TAB1 to reduce its association with TGF β-activated kinase 1 (TAK1) and its autophosphorylation, an essential signaling step in IL-1β-induced signaling pathways.
36032089	8	8	theme	β-activated	1287:1297	arg1	TAK1					1309:1312	TAK1	1309:1312	TAK1	1309:1312	Immunoprecipitation analysis showed that PGG inhibited O-GlcNAcylation of TAB1 to reduce its association with TGF β-activated kinase 1 (TAK1) and its autophosphorylation, an essential signaling step in IL-1β-induced signaling pathways.
36032089	11	9	theme	IL-1β	1875:1879	arg1	levels					1859:1864	levels	1859:1864	levels of serum IL-1β, GM-CSF, TNF-α, and RANKL	1859:1905	PGG treatment reduced the phosphorylation of TAK1 in the treated joints compared to AIA joints, which correlated with the reduced disease severity and suppressed levels of serum IL-1β, GM-CSF, TNF-α, and RANKL.
36032089	6	10	theme	Thiamet	861:867	arg1	G					869:869	Thiamet G	861:869	Thiamet G	861:869	Pretreatment of RASFs with Thiamet G, an inhibitor of O-GlcNAcase, markedly increased the O-GlcNAc-modified proteins and concomitantly inhibited the IL-1β-induced IL-6 and IL-8 production in human RASFs in vitro.
36032089	6	10	theme	Thiamet	861:867	arg1	inhibitor					875:883	an inhibitor	872:883	an inhibitor of O-GlcNAcase	872:898	Pretreatment of RASFs with Thiamet G, an inhibitor of O-GlcNAcase, markedly increased the O-GlcNAc-modified proteins and concomitantly inhibited the IL-1β-induced IL-6 and IL-8 production in human RASFs in vitro.
36032089	1	11	theme	cellular	240:247	arg1	responses					310:318	immune responses	303:318	embryonic development as well as immune responses	270:318	O-GlcNAcylation is a reversible post-translational modification that regulates numerous cellular processes, including embryonic development as well as immune responses.
36032089	1	11	theme	cellular	240:247	arg1	development					280:290	embryonic development	270:290	embryonic development as well as immune responses	270:318	O-GlcNAcylation is a reversible post-translational modification that regulates numerous cellular processes, including embryonic development as well as immune responses.
36032089	1	11	theme	cellular	240:247	arg1	processes					249:257	numerous cellular processes	231:257	numerous cellular processes	231:257	O-GlcNAcylation is a reversible post-translational modification that regulates numerous cellular processes, including embryonic development as well as immune responses.
36032089	8	12	theme	signaling	1357:1365	arg1	step					1367:1370	an essential signaling step	1344:1370	an essential signaling step in IL-1β-induced signaling pathways	1344:1406	Immunoprecipitation analysis showed that PGG inhibited O-GlcNAcylation of TAB1 to reduce its association with TGF β-activated kinase 1 (TAK1) and its autophosphorylation, an essential signaling step in IL-1β-induced signaling pathways.
36032089	8	12	theme	signaling	1357:1365	arg1	autophosphorylation					1323:1341	its autophosphorylation	1319:1341	its autophosphorylation	1319:1341	Immunoprecipitation analysis showed that PGG inhibited O-GlcNAcylation of TAB1 to reduce its association with TGF β-activated kinase 1 (TAK1) and its autophosphorylation, an essential signaling step in IL-1β-induced signaling pathways.
36032089	7	13	theme	dose-dependent	1150:1163	arg1	manner					1165:1170	a dose-dependent manner	1148:1170	a dose-dependent manner	1148:1170	Pretreatment of human RASFs with PGG (0.5-10 µM) abrogated IL-1β-induced IL-6 and IL-8 production in a dose-dependent manner.
36032089	11	14	theme	TNF-α	1890:1894	arg1	levels					1859:1864	levels	1859:1864	levels of serum IL-1β, GM-CSF, TNF-α, and RANKL	1859:1905	PGG treatment reduced the phosphorylation of TAK1 in the treated joints compared to AIA joints, which correlated with the reduced disease severity and suppressed levels of serum IL-1β, GM-CSF, TNF-α, and RANKL.
36032089	1	15	theme	embryonic	270:278	arg1	development					280:290	embryonic development	270:290	embryonic development as well as immune responses	270:318	O-GlcNAcylation is a reversible post-translational modification that regulates numerous cellular processes, including embryonic development as well as immune responses.
36032089	7	16	with	Pretreatment	1047:1058	arg1	PGG					1080:1082	PGG	1080:1082	PGG (0.5-10 µM)	1080:1094	Pretreatment of human RASFs with PGG (0.5-10 µM) abrogated IL-1β-induced IL-6 and IL-8 production in a dose-dependent manner.
36032089	7	16	with	Pretreatment	1047:1058	arg1	µM					1092:1093	0.5-10 µM	1085:1093	0.5-10 µM	1085:1093	Pretreatment of human RASFs with PGG (0.5-10 µM) abrogated IL-1β-induced IL-6 and IL-8 production in a dose-dependent manner.
36032089	8	17	theme	signaling	1389:1397	arg1	pathways					1399:1406	IL-1β-induced signaling pathways	1375:1406	IL-1β-induced signaling pathways	1375:1406	Immunoprecipitation analysis showed that PGG inhibited O-GlcNAcylation of TAB1 to reduce its association with TGF β-activated kinase 1 (TAK1) and its autophosphorylation, an essential signaling step in IL-1β-induced signaling pathways.
36032089	11	18	theme	GM-CSF	1882:1887	arg1	levels					1859:1864	levels	1859:1864	levels of serum IL-1β, GM-CSF, TNF-α, and RANKL	1859:1905	PGG treatment reduced the phosphorylation of TAK1 in the treated joints compared to AIA joints, which correlated with the reduced disease severity and suppressed levels of serum IL-1β, GM-CSF, TNF-α, and RANKL.
36032089	7	19	theme	IL-8	1129:1132	arg1	production					1134:1143	IL-1β-induced IL-6 and IL-8 production	1106:1143	IL-1β-induced IL-6 and IL-8 production	1106:1143	Pretreatment of human RASFs with PGG (0.5-10 µM) abrogated IL-1β-induced IL-6 and IL-8 production in a dose-dependent manner.
36032089	6	20	theme	human	1025:1029	arg1	RASFs					1031:1035	human RASFs	1025:1035	human RASFs	1025:1035	Pretreatment of RASFs with Thiamet G, an inhibitor of O-GlcNAcase, markedly increased the O-GlcNAc-modified proteins and concomitantly inhibited the IL-1β-induced IL-6 and IL-8 production in human RASFs in vitro.
36032089	11	21	theme	reduced	1819:1825	arg1	severity					1835:1842	the reduced disease severity	1815:1842	the reduced disease severity	1815:1842	PGG treatment reduced the phosphorylation of TAK1 in the treated joints compared to AIA joints, which correlated with the reduced disease severity and suppressed levels of serum IL-1β, GM-CSF, TNF-α, and RANKL.
36032089	7	22	theme	IL-6	1120:1123	arg1	production					1134:1143	IL-1β-induced IL-6 and IL-8 production	1106:1143	IL-1β-induced IL-6 and IL-8 production	1106:1143	Pretreatment of human RASFs with PGG (0.5-10 µM) abrogated IL-1β-induced IL-6 and IL-8 production in a dose-dependent manner.
36032089	0	23	theme	rheumatoid	68:77	arg1	arthritis					79:87	human rheumatoid arthritis	62:87	human rheumatoid arthritis	62:87	Penta-o-galloyl-beta-d-Glucose (PGG) inhibits inflammation in human rheumatoid arthritis synovial fibroblasts and rat adjuvant-induced arthritis model.
36032089	7	24	theme	RASFs	1069:1073	arg1	Pretreatment					1047:1058	Pretreatment	1047:1058	Pretreatment of human RASFs with PGG (0.5-10 µM)	1047:1094	Pretreatment of human RASFs with PGG (0.5-10 µM) abrogated IL-1β-induced IL-6 and IL-8 production in a dose-dependent manner.
36032089	1	25	theme	reversible	173:182	arg1	O-GlcNAcylation					152:166	O-GlcNAcylation	152:166	O-GlcNAcylation	152:166	O-GlcNAcylation is a reversible post-translational modification that regulates numerous cellular processes, including embryonic development as well as immune responses.
36032089	1	25	theme	reversible	173:182	arg1	modification					203:214	a reversible post-translational modification	171:214	a reversible post-translational modification that regulates numerous cellular processes, including embryonic development as well as immune responses	171:318	O-GlcNAcylation is a reversible post-translational modification that regulates numerous cellular processes, including embryonic development as well as immune responses.
36032089	5	26	theme	higher	752:757	arg1	expression					759:768	higher expression	752:768	higher expression of O-GlcNAcylation	752:787	Human synovial tissues and RASFs exhibited higher expression of O-GlcNAcylation compared to their non-diseased counterparts.
36032089	0	27	theme	synovial	89:96	arg1	fibroblasts					98:108	synovial fibroblasts	89:108	synovial fibroblasts	89:108	Penta-o-galloyl-beta-d-Glucose (PGG) inhibits inflammation in human rheumatoid arthritis synovial fibroblasts and rat adjuvant-induced arthritis model.
36032089	9	28	theme	Molecular	1409:1417	arg1	docking					1419:1425	Molecular docking	1409:1425	Molecular docking in silico studies	1409:1443	Molecular docking in silico studies shows that PGG occupies the C174 position, an ATP-binding site in the kinase domain to inhibit TAK1 kinase activity.
36032089	0	29	theme	adjuvant-induced	118:133	arg1	arthritis					135:143	rat adjuvant-induced arthritis	114:143	rat adjuvant-induced arthritis	114:143	Penta-o-galloyl-beta-d-Glucose (PGG) inhibits inflammation in human rheumatoid arthritis synovial fibroblasts and rat adjuvant-induced arthritis model.
36032089	8	30	with	association	1266:1276	arg1	kinase					1299:1304	TGF β-activated kinase 1	1283:1306	TGF β-activated kinase 1 (TAK1)	1283:1313	Immunoprecipitation analysis showed that PGG inhibited O-GlcNAcylation of TAB1 to reduce its association with TGF β-activated kinase 1 (TAK1) and its autophosphorylation, an essential signaling step in IL-1β-induced signaling pathways.
36032089	8	30	with	association	1266:1276	arg1	TAK1					1309:1312	TAK1	1309:1312	TAK1	1309:1312	Immunoprecipitation analysis showed that PGG inhibited O-GlcNAcylation of TAB1 to reduce its association with TGF β-activated kinase 1 (TAK1) and its autophosphorylation, an essential signaling step in IL-1β-induced signaling pathways.
36032089	5	31	theme	O-GlcNAcylation	773:787	arg1	expression					759:768	higher expression	752:768	higher expression of O-GlcNAcylation	752:787	Human synovial tissues and RASFs exhibited higher expression of O-GlcNAcylation compared to their non-diseased counterparts.
36032089	3	32	theme	patient-derived	500:514	arg1	RASFs					538:542	RASFs	538:542	RASFs	538:542	This study was designed to examine the role of O-GlcNAcylation in rheumatoid arthritis (RA) and its regulation using human RA patient-derived synovial fibroblasts (RASFs).
36032089	3	32	theme	patient-derived	500:514	arg1	fibroblasts					525:535	human RA patient-derived synovial fibroblasts	491:535	human RA patient-derived synovial fibroblasts (RASFs)	491:543	This study was designed to examine the role of O-GlcNAcylation in rheumatoid arthritis (RA) and its regulation using human RA patient-derived synovial fibroblasts (RASFs).
36032089	4	33	theme	potent	602:607	arg1	molecule					627:634	a potent anti-inflammatory molecule	600:634	a potent anti-inflammatory molecule	600:634	The efficacy of penta-O-galloyl-beta-D-glucose (PGG), a potent anti-inflammatory molecule, in regulating inflammatory processes in human RASFs was also evaluated.
36032089	4	33	theme	potent	602:607	arg1	penta-O-galloyl-beta-D-glucose					562:591	penta-O-galloyl-beta-D-glucose	562:591	penta-O-galloyl-beta-D-glucose (PGG)	562:597	The efficacy of penta-O-galloyl-beta-D-glucose (PGG), a potent anti-inflammatory molecule, in regulating inflammatory processes in human RASFs was also evaluated.
36032089	10	34	theme	PGG	1585:1587	arg1	administration					1567:1580	Oral administration	1562:1580	Oral administration of PGG (25 mg/kg/day) for 10 days from disease onset	1562:1633	Oral administration of PGG (25 mg/kg/day) for 10 days from disease onset significantly ameliorated rat adjuvant-induced (AIA) in rats.
36032089	11	35	theme	AIA	1781:1783	arg1	joints					1785:1790	AIA joints	1781:1790	AIA joints	1781:1790	PGG treatment reduced the phosphorylation of TAK1 in the treated joints compared to AIA joints, which correlated with the reduced disease severity and suppressed levels of serum IL-1β, GM-CSF, TNF-α, and RANKL.
36032089	3	36	theme	human	491:495	arg1	RASFs					538:542	RASFs	538:542	RASFs	538:542	This study was designed to examine the role of O-GlcNAcylation in rheumatoid arthritis (RA) and its regulation using human RA patient-derived synovial fibroblasts (RASFs).
36032089	3	36	theme	human	491:495	arg1	fibroblasts					525:535	human RA patient-derived synovial fibroblasts	491:535	human RA patient-derived synovial fibroblasts (RASFs)	491:543	This study was designed to examine the role of O-GlcNAcylation in rheumatoid arthritis (RA) and its regulation using human RA patient-derived synovial fibroblasts (RASFs).
36032089	8	37	theme	Immunoprecipitation	1173:1191	arg1	analysis					1193:1200	Immunoprecipitation analysis	1173:1200	Immunoprecipitation analysis	1173:1200	Immunoprecipitation analysis showed that PGG inhibited O-GlcNAcylation of TAB1 to reduce its association with TGF β-activated kinase 1 (TAK1) and its autophosphorylation, an essential signaling step in IL-1β-induced signaling pathways.
36032089	10	38	from	onset	1629:1633	arg1	days					1611:1614	10 days	1608:1614	10 days from disease onset	1608:1633	Oral administration of PGG (25 mg/kg/day) for 10 days from disease onset significantly ameliorated rat adjuvant-induced (AIA) in rats.
36032089	11	39	from	phosphorylation	1723:1737	arg1	joints					1762:1767	the treated joints	1750:1767	the treated joints	1750:1767	PGG treatment reduced the phosphorylation of TAK1 in the treated joints compared to AIA joints, which correlated with the reduced disease severity and suppressed levels of serum IL-1β, GM-CSF, TNF-α, and RANKL.
36032089	4	40	theme	penta-O-galloyl-beta-D-glucose	562:591	arg1	efficacy					550:557	The efficacy	546:557	The efficacy of penta-O-galloyl-beta-D-glucose (PGG), a potent anti-inflammatory molecule, in regulating inflammatory processes in human RASFs	546:687	The efficacy of penta-O-galloyl-beta-D-glucose (PGG), a potent anti-inflammatory molecule, in regulating inflammatory processes in human RASFs was also evaluated.
36032089	9	41	theme	C174	1473:1476	arg1	site					1503:1506	an ATP-binding site	1488:1506	an ATP-binding site in the kinase domain	1488:1527	Molecular docking in silico studies shows that PGG occupies the C174 position, an ATP-binding site in the kinase domain to inhibit TAK1 kinase activity.
36032089	9	41	theme	C174	1473:1476	arg1	position					1478:1485	the C174 position	1469:1485	the C174 position	1469:1485	Molecular docking in silico studies shows that PGG occupies the C174 position, an ATP-binding site in the kinase domain to inhibit TAK1 kinase activity.
36032089	9	42	from	site	1503:1506	arg1	domain					1522:1527	the kinase domain	1511:1527	the kinase domain	1511:1527	Molecular docking in silico studies shows that PGG occupies the C174 position, an ATP-binding site in the kinase domain to inhibit TAK1 kinase activity.
36032089	4	43	theme	inflammatory	651:662	arg1	processes					664:672	inflammatory processes	651:672	inflammatory processes	651:672	The efficacy of penta-O-galloyl-beta-D-glucose (PGG), a potent anti-inflammatory molecule, in regulating inflammatory processes in human RASFs was also evaluated.
36032089	6	44	with	Pretreatment	834:845	arg1	G					869:869	Thiamet G	861:869	Thiamet G	861:869	Pretreatment of RASFs with Thiamet G, an inhibitor of O-GlcNAcase, markedly increased the O-GlcNAc-modified proteins and concomitantly inhibited the IL-1β-induced IL-6 and IL-8 production in human RASFs in vitro.
36032089	6	44	with	Pretreatment	834:845	arg1	inhibitor					875:883	an inhibitor	872:883	an inhibitor of O-GlcNAcase	872:898	Pretreatment of RASFs with Thiamet G, an inhibitor of O-GlcNAcase, markedly increased the O-GlcNAc-modified proteins and concomitantly inhibited the IL-1β-induced IL-6 and IL-8 production in human RASFs in vitro.
36032089	9	45	theme	ATP-binding	1491:1501	arg1	site					1503:1506	an ATP-binding site	1488:1506	an ATP-binding site in the kinase domain	1488:1527	Molecular docking in silico studies shows that PGG occupies the C174 position, an ATP-binding site in the kinase domain to inhibit TAK1 kinase activity.
36032089	9	45	theme	ATP-binding	1491:1501	arg1	position					1478:1485	the C174 position	1469:1485	the C174 position	1469:1485	Molecular docking in silico studies shows that PGG occupies the C174 position, an ATP-binding site in the kinase domain to inhibit TAK1 kinase activity.
36032089	12	46	theme	similar	2039:2045	arg1	molecule					2047:2054	structurally similar molecule	2026:2054	structurally similar molecule	2026:2054	These findings suggest O-GlcNAcylation as a potential therapeutic target and provide the rationale for testing PGG or structurally similar molecule for their therapeutic efficacy.
36032089	1	47	theme	immune	303:308	arg1	responses					310:318	immune responses	303:318	embryonic development as well as immune responses	270:318	O-GlcNAcylation is a reversible post-translational modification that regulates numerous cellular processes, including embryonic development as well as immune responses.
36032089	8	48	theme	TAB1	1247:1250	arg1	O-GlcNAcylation					1228:1242	O-GlcNAcylation	1228:1242	O-GlcNAcylation of TAB1 to reduce its association with TGF β-activated kinase 1 (TAK1) and its autophosphorylation, an essential signaling step in IL-1β-induced signaling pathways	1228:1406	Immunoprecipitation analysis showed that PGG inhibited O-GlcNAcylation of TAB1 to reduce its association with TGF β-activated kinase 1 (TAK1) and its autophosphorylation, an essential signaling step in IL-1β-induced signaling pathways.
36032089	6	49	theme	IL-8	1006:1009	arg1	production					1011:1020	the IL-1β-induced IL-6 and IL-8 production	979:1020	the IL-1β-induced IL-6 and IL-8 production in human RASFs	979:1035	Pretreatment of RASFs with Thiamet G, an inhibitor of O-GlcNAcase, markedly increased the O-GlcNAc-modified proteins and concomitantly inhibited the IL-1β-induced IL-6 and IL-8 production in human RASFs in vitro.
36032089	5	50	theme	synovial	715:722	arg1	tissues					724:730	Human synovial tissues	709:730	Human synovial tissues	709:730	Human synovial tissues and RASFs exhibited higher expression of O-GlcNAcylation compared to their non-diseased counterparts.
36032089	9	51	theme	kinase	1515:1520	arg1	domain					1522:1527	the kinase domain	1511:1527	the kinase domain	1511:1527	Molecular docking in silico studies shows that PGG occupies the C174 position, an ATP-binding site in the kinase domain to inhibit TAK1 kinase activity.
36032089	6	52	theme	IL-6	997:1000	arg1	production					1011:1020	the IL-1β-induced IL-6 and IL-8 production	979:1020	the IL-1β-induced IL-6 and IL-8 production in human RASFs	979:1035	Pretreatment of RASFs with Thiamet G, an inhibitor of O-GlcNAcase, markedly increased the O-GlcNAc-modified proteins and concomitantly inhibited the IL-1β-induced IL-6 and IL-8 production in human RASFs in vitro.
36032089	11	53	theme	treated	1754:1760	arg1	joints					1762:1767	the treated joints	1750:1767	the treated joints	1750:1767	PGG treatment reduced the phosphorylation of TAK1 in the treated joints compared to AIA joints, which correlated with the reduced disease severity and suppressed levels of serum IL-1β, GM-CSF, TNF-α, and RANKL.
36032089	1	54	theme	numerous	231:238	arg1	responses					310:318	immune responses	303:318	embryonic development as well as immune responses	270:318	O-GlcNAcylation is a reversible post-translational modification that regulates numerous cellular processes, including embryonic development as well as immune responses.
36032089	1	54	theme	numerous	231:238	arg1	development					280:290	embryonic development	270:290	embryonic development as well as immune responses	270:318	O-GlcNAcylation is a reversible post-translational modification that regulates numerous cellular processes, including embryonic development as well as immune responses.
36032089	1	54	theme	numerous	231:238	arg1	processes					249:257	numerous cellular processes	231:257	numerous cellular processes	231:257	O-GlcNAcylation is a reversible post-translational modification that regulates numerous cellular processes, including embryonic development as well as immune responses.
36032089	9	55	theme	TAK1	1540:1543	arg1	activity					1552:1559	TAK1 kinase activity	1540:1559	TAK1 kinase activity	1540:1559	Molecular docking in silico studies shows that PGG occupies the C174 position, an ATP-binding site in the kinase domain to inhibit TAK1 kinase activity.
36032089	8	56	theme	TGF	1283:1285	arg1	kinase					1299:1304	TGF β-activated kinase 1	1283:1306	TGF β-activated kinase 1 (TAK1)	1283:1313	Immunoprecipitation analysis showed that PGG inhibited O-GlcNAcylation of TAB1 to reduce its association with TGF β-activated kinase 1 (TAK1) and its autophosphorylation, an essential signaling step in IL-1β-induced signaling pathways.
36032089	8	56	theme	TGF	1283:1285	arg1	TAK1					1309:1312	TAK1	1309:1312	TAK1	1309:1312	Immunoprecipitation analysis showed that PGG inhibited O-GlcNAcylation of TAB1 to reduce its association with TGF β-activated kinase 1 (TAK1) and its autophosphorylation, an essential signaling step in IL-1β-induced signaling pathways.
36032089	12	57	dep	potential	1952:1960	arg1	therapeutic					1962:1972	therapeutic	1962:1972	therapeutic	1962:1972	These findings suggest O-GlcNAcylation as a potential therapeutic target and provide the rationale for testing PGG or structurally similar molecule for their therapeutic efficacy.
36032089	9	58	from	docking	1419:1425	arg1	studies					1437:1443	silico studies	1430:1443	silico studies	1430:1443	Molecular docking in silico studies shows that PGG occupies the C174 position, an ATP-binding site in the kinase domain to inhibit TAK1 kinase activity.
36032089	8	59	theme	essential	1347:1355	arg1	step					1367:1370	an essential signaling step	1344:1370	an essential signaling step in IL-1β-induced signaling pathways	1344:1406	Immunoprecipitation analysis showed that PGG inhibited O-GlcNAcylation of TAB1 to reduce its association with TGF β-activated kinase 1 (TAK1) and its autophosphorylation, an essential signaling step in IL-1β-induced signaling pathways.
36032089	8	59	theme	essential	1347:1355	arg1	autophosphorylation					1323:1341	its autophosphorylation	1319:1341	its autophosphorylation	1319:1341	Immunoprecipitation analysis showed that PGG inhibited O-GlcNAcylation of TAB1 to reduce its association with TGF β-activated kinase 1 (TAK1) and its autophosphorylation, an essential signaling step in IL-1β-induced signaling pathways.
36032089	11	60	theme	serum	1869:1873	arg1	IL-1β					1875:1879	serum IL-1β	1869:1879	serum IL-1β	1869:1879	PGG treatment reduced the phosphorylation of TAK1 in the treated joints compared to AIA joints, which correlated with the reduced disease severity and suppressed levels of serum IL-1β, GM-CSF, TNF-α, and RANKL.
36032089	10	61	dep	adjuvant-induced	1665:1680	arg1	AIA					1683:1685	AIA	1683:1685	AIA	1683:1685	Oral administration of PGG (25 mg/kg/day) for 10 days from disease onset significantly ameliorated rat adjuvant-induced (AIA) in rats.
36032089	9	62	theme	kinase	1545:1550	arg1	activity					1552:1559	TAK1 kinase activity	1540:1559	TAK1 kinase activity	1540:1559	Molecular docking in silico studies shows that PGG occupies the C174 position, an ATP-binding site in the kinase domain to inhibit TAK1 kinase activity.
36032089	3	63	from	role	413:416	arg1	RA					462:463	RA	462:463	RA	462:463	This study was designed to examine the role of O-GlcNAcylation in rheumatoid arthritis (RA) and its regulation using human RA patient-derived synovial fibroblasts (RASFs).
36032089	3	63	from	role	413:416	arg1	arthritis					451:459	rheumatoid arthritis	440:459	rheumatoid arthritis (RA)	440:464	This study was designed to examine the role of O-GlcNAcylation in rheumatoid arthritis (RA) and its regulation using human RA patient-derived synovial fibroblasts (RASFs).
36032089	8	64	theme	IL-1β-induced	1375:1387	arg1	pathways					1399:1406	IL-1β-induced signaling pathways	1375:1406	IL-1β-induced signaling pathways	1375:1406	Immunoprecipitation analysis showed that PGG inhibited O-GlcNAcylation of TAB1 to reduce its association with TGF β-activated kinase 1 (TAK1) and its autophosphorylation, an essential signaling step in IL-1β-induced signaling pathways.
36032089	7	65	theme	IL-1β-induced	1106:1118	arg1	production					1134:1143	IL-1β-induced IL-6 and IL-8 production	1106:1143	IL-1β-induced IL-6 and IL-8 production	1106:1143	Pretreatment of human RASFs with PGG (0.5-10 µM) abrogated IL-1β-induced IL-6 and IL-8 production in a dose-dependent manner.
36032089	11	66	theme	disease	1827:1833	arg1	severity					1835:1842	the reduced disease severity	1815:1842	the reduced disease severity	1815:1842	PGG treatment reduced the phosphorylation of TAK1 in the treated joints compared to AIA joints, which correlated with the reduced disease severity and suppressed levels of serum IL-1β, GM-CSF, TNF-α, and RANKL.
36032089	0	67	theme	arthritis	79:87	arg1	model					145:149	human rheumatoid arthritis synovial fibroblasts and rat adjuvant-induced arthritis model	62:149	human rheumatoid arthritis synovial fibroblasts and rat adjuvant-induced arthritis model	62:149	Penta-o-galloyl-beta-d-Glucose (PGG) inhibits inflammation in human rheumatoid arthritis synovial fibroblasts and rat adjuvant-induced arthritis model.
36032089	8	68	from	step	1367:1370	arg1	pathways					1399:1406	IL-1β-induced signaling pathways	1375:1406	IL-1β-induced signaling pathways	1375:1406	Immunoprecipitation analysis showed that PGG inhibited O-GlcNAcylation of TAB1 to reduce its association with TGF β-activated kinase 1 (TAK1) and its autophosphorylation, an essential signaling step in IL-1β-induced signaling pathways.
36032089	2	69	from	role	334:337	arg1	inflammation					342:353	inflammation	342:353	inflammation	342:353	However, its role in inflammation remains ambiguous.
36032089	1	70	theme	post-translational	184:201	arg1	O-GlcNAcylation					152:166	O-GlcNAcylation	152:166	O-GlcNAcylation	152:166	O-GlcNAcylation is a reversible post-translational modification that regulates numerous cellular processes, including embryonic development as well as immune responses.
36032089	1	70	theme	post-translational	184:201	arg1	modification					203:214	a reversible post-translational modification	171:214	a reversible post-translational modification that regulates numerous cellular processes, including embryonic development as well as immune responses	171:318	O-GlcNAcylation is a reversible post-translational modification that regulates numerous cellular processes, including embryonic development as well as immune responses.
36032089	0	71	theme	rat	114:116	arg1	arthritis					135:143	rat adjuvant-induced arthritis	114:143	rat adjuvant-induced arthritis	114:143	Penta-o-galloyl-beta-d-Glucose (PGG) inhibits inflammation in human rheumatoid arthritis synovial fibroblasts and rat adjuvant-induced arthritis model.
36032089	7	72	theme	human	1063:1067	arg1	RASFs					1069:1073	human RASFs	1063:1073	human RASFs	1063:1073	Pretreatment of human RASFs with PGG (0.5-10 µM) abrogated IL-1β-induced IL-6 and IL-8 production in a dose-dependent manner.
36032089	0	73	theme	arthritis	135:143	arg1	model					145:149	human rheumatoid arthritis synovial fibroblasts and rat adjuvant-induced arthritis model	62:149	human rheumatoid arthritis synovial fibroblasts and rat adjuvant-induced arthritis model	62:149	Penta-o-galloyl-beta-d-Glucose (PGG) inhibits inflammation in human rheumatoid arthritis synovial fibroblasts and rat adjuvant-induced arthritis model.
36032089	12	74	theme	potential	1952:1960	arg1	target					1974:1979	a potential therapeutic target	1950:1979	a potential therapeutic target	1950:1979	These findings suggest O-GlcNAcylation as a potential therapeutic target and provide the rationale for testing PGG or structurally similar molecule for their therapeutic efficacy.
36032089	12	74	theme	potential	1952:1960	arg1	O-GlcNAcylation					1931:1945	O-GlcNAcylation	1931:1945	O-GlcNAcylation	1931:1945	These findings suggest O-GlcNAcylation as a potential therapeutic target and provide the rationale for testing PGG or structurally similar molecule for their therapeutic efficacy.
36032089	10	75	theme	Oral	1562:1565	arg1	administration					1567:1580	Oral administration	1562:1580	Oral administration of PGG (25 mg/kg/day) for 10 days from disease onset	1562:1633	Oral administration of PGG (25 mg/kg/day) for 10 days from disease onset significantly ameliorated rat adjuvant-induced (AIA) in rats.
36032089	5	76	theme	non-diseased	807:818	arg1	counterparts					820:831	their non-diseased counterparts	801:831	their non-diseased counterparts	801:831	Human synovial tissues and RASFs exhibited higher expression of O-GlcNAcylation compared to their non-diseased counterparts.
36032089	9	77	theme	silico	1430:1435	arg1	studies					1437:1443	silico studies	1430:1443	silico studies	1430:1443	Molecular docking in silico studies shows that PGG occupies the C174 position, an ATP-binding site in the kinase domain to inhibit TAK1 kinase activity.
36032089	3	78	theme	rheumatoid	440:449	arg1	RA					462:463	RA	462:463	RA	462:463	This study was designed to examine the role of O-GlcNAcylation in rheumatoid arthritis (RA) and its regulation using human RA patient-derived synovial fibroblasts (RASFs).
36032089	3	78	theme	rheumatoid	440:449	arg1	arthritis					451:459	rheumatoid arthritis	440:459	rheumatoid arthritis (RA)	440:464	This study was designed to examine the role of O-GlcNAcylation in rheumatoid arthritis (RA) and its regulation using human RA patient-derived synovial fibroblasts (RASFs).
36032089	0	79	dep	arthritis	79:87	arg1	fibroblasts					98:108	synovial fibroblasts	89:108	synovial fibroblasts	89:108	Penta-o-galloyl-beta-d-Glucose (PGG) inhibits inflammation in human rheumatoid arthritis synovial fibroblasts and rat adjuvant-induced arthritis model.
36032089	3	80	theme	O-GlcNAcylation	421:435	arg1	regulation					474:483	its regulation	470:483	its regulation using human RA patient-derived synovial fibroblasts (RASFs)	470:543	This study was designed to examine the role of O-GlcNAcylation in rheumatoid arthritis (RA) and its regulation using human RA patient-derived synovial fibroblasts (RASFs).
36032089	3	80	theme	O-GlcNAcylation	421:435	arg1	role					413:416	the role	409:416	the role of O-GlcNAcylation in rheumatoid arthritis (RA)	409:464	This study was designed to examine the role of O-GlcNAcylation in rheumatoid arthritis (RA) and its regulation using human RA patient-derived synovial fibroblasts (RASFs).
36032089	4	81	theme	anti-inflammatory	609:625	arg1	molecule					627:634	a potent anti-inflammatory molecule	600:634	a potent anti-inflammatory molecule	600:634	The efficacy of penta-O-galloyl-beta-D-glucose (PGG), a potent anti-inflammatory molecule, in regulating inflammatory processes in human RASFs was also evaluated.
36032089	4	81	theme	anti-inflammatory	609:625	arg1	penta-O-galloyl-beta-D-glucose					562:591	penta-O-galloyl-beta-D-glucose	562:591	penta-O-galloyl-beta-D-glucose (PGG)	562:597	The efficacy of penta-O-galloyl-beta-D-glucose (PGG), a potent anti-inflammatory molecule, in regulating inflammatory processes in human RASFs was also evaluated.
36032089	3	82	theme	synovial	516:523	arg1	RASFs					538:542	RASFs	538:542	RASFs	538:542	This study was designed to examine the role of O-GlcNAcylation in rheumatoid arthritis (RA) and its regulation using human RA patient-derived synovial fibroblasts (RASFs).
36032089	3	82	theme	synovial	516:523	arg1	fibroblasts					525:535	human RA patient-derived synovial fibroblasts	491:535	human RA patient-derived synovial fibroblasts (RASFs)	491:543	This study was designed to examine the role of O-GlcNAcylation in rheumatoid arthritis (RA) and its regulation using human RA patient-derived synovial fibroblasts (RASFs).
36032089	6	83	theme	RASFs	850:854	arg1	Pretreatment					834:845	Pretreatment	834:845	Pretreatment of RASFs with Thiamet G, an inhibitor of O-GlcNAcase,	834:899	Pretreatment of RASFs with Thiamet G, an inhibitor of O-GlcNAcase, markedly increased the O-GlcNAc-modified proteins and concomitantly inhibited the IL-1β-induced IL-6 and IL-8 production in human RASFs in vitro.
36032089	3	84	theme	RA	497:498	arg1	RASFs					538:542	RASFs	538:542	RASFs	538:542	This study was designed to examine the role of O-GlcNAcylation in rheumatoid arthritis (RA) and its regulation using human RA patient-derived synovial fibroblasts (RASFs).
36032089	3	84	theme	RA	497:498	arg1	fibroblasts					525:535	human RA patient-derived synovial fibroblasts	491:535	human RA patient-derived synovial fibroblasts (RASFs)	491:543	This study was designed to examine the role of O-GlcNAcylation in rheumatoid arthritis (RA) and its regulation using human RA patient-derived synovial fibroblasts (RASFs).
36032089	0	85	theme	human	62:66	arg1	arthritis					79:87	human rheumatoid arthritis	62:87	human rheumatoid arthritis	62:87	Penta-o-galloyl-beta-d-Glucose (PGG) inhibits inflammation in human rheumatoid arthritis synovial fibroblasts and rat adjuvant-induced arthritis model.
36032089	6	86	theme	O-GlcNAc-modified	924:940	arg1	proteins					942:949	the O-GlcNAc-modified proteins	920:949	the O-GlcNAc-modified proteins	920:949	Pretreatment of RASFs with Thiamet G, an inhibitor of O-GlcNAcase, markedly increased the O-GlcNAc-modified proteins and concomitantly inhibited the IL-1β-induced IL-6 and IL-8 production in human RASFs in vitro.
36032089	11	87	theme	PGG	1697:1699	arg1	treatment					1701:1709	PGG treatment	1697:1709	PGG treatment	1697:1709	PGG treatment reduced the phosphorylation of TAK1 in the treated joints compared to AIA joints, which correlated with the reduced disease severity and suppressed levels of serum IL-1β, GM-CSF, TNF-α, and RANKL.
36032089	11	88	theme	RANKL	1901:1905	arg1	levels					1859:1864	levels	1859:1864	levels of serum IL-1β, GM-CSF, TNF-α, and RANKL	1859:1905	PGG treatment reduced the phosphorylation of TAK1 in the treated joints compared to AIA joints, which correlated with the reduced disease severity and suppressed levels of serum IL-1β, GM-CSF, TNF-α, and RANKL.
36032089	4	89	theme	human	677:681	arg1	RASFs					683:687	human RASFs	677:687	human RASFs	677:687	The efficacy of penta-O-galloyl-beta-D-glucose (PGG), a potent anti-inflammatory molecule, in regulating inflammatory processes in human RASFs was also evaluated.
36032089	10	90	theme	disease	1621:1627	arg1	onset					1629:1633	disease onset	1621:1633	disease onset	1621:1633	Oral administration of PGG (25 mg/kg/day) for 10 days from disease onset significantly ameliorated rat adjuvant-induced (AIA) in rats.
36032089	3	91	from	regulation	474:483	arg1	RA					462:463	RA	462:463	RA	462:463	This study was designed to examine the role of O-GlcNAcylation in rheumatoid arthritis (RA) and its regulation using human RA patient-derived synovial fibroblasts (RASFs).
36032089	3	91	from	regulation	474:483	arg1	arthritis					451:459	rheumatoid arthritis	440:459	rheumatoid arthritis (RA)	440:464	This study was designed to examine the role of O-GlcNAcylation in rheumatoid arthritis (RA) and its regulation using human RA patient-derived synovial fibroblasts (RASFs).
25303527	7	0	dep	fasting	1155:1161	arg1	response					1143:1150	response	1143:1150	response	1143:1150	These data reveal adipose tissue browning as a highly dynamic physiological process under central control, in which O-GlcNAc signaling in AgRP neurons is essential for suppressing thermogenesis to conserve energy in response to fasting.
25303527	0	1	theme	fat	72:74	arg1	browning					54:61	browning	54:61	browning of white fat	54:74	O-GlcNAc transferase enables AgRP neurons to suppress browning of white fat.
25303527	6	2	theme	white	825:829	arg1	tissue					839:844	white adipose tissue	825:844	white adipose tissue browning	825:853	Genetic ablation of OGT in AgRP neurons inhibits neuronal excitability through the voltage-dependent potassium channel, promotes white adipose tissue browning, and protects mice against diet-induced obesity and insulin resistance.
25303527	6	3	theme	insulin	907:913	arg1	resistance					915:924	insulin resistance	907:924	insulin resistance	907:924	Genetic ablation of OGT in AgRP neurons inhibits neuronal excitability through the voltage-dependent potassium channel, promotes white adipose tissue browning, and protects mice against diet-induced obesity and insulin resistance.
25303527	4	4	theme	proteins	520:527	arg1	modification					480:491	O-linked β-N-acetylglucosamine (O-GlcNAc) modification	438:491	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of cytoplasmic and nuclear proteins	438:527	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of cytoplasmic and nuclear proteins regulates fundamental cellular processes.
25303527	7	5	theme	central	1017:1023	arg1	control					1025:1031	central control	1017:1031	central control	1017:1031	These data reveal adipose tissue browning as a highly dynamic physiological process under central control, in which O-GlcNAc signaling in AgRP neurons is essential for suppressing thermogenesis to conserve energy in response to fasting.
25303527	5	6	theme	O-GlcNAc	616:623	arg1	modification					625:636	O-GlcNAc modification	616:636	O-GlcNAc modification	616:636	The levels of O-GlcNAc transferase (OGT) and O-GlcNAc modification are enriched in AgRP neurons and are elevated by fasting.
25303527	3	7	theme	orexigenic	358:367	arg1	neurons					374:380	orexigenic AgRP neurons	358:380	orexigenic AgRP neurons	358:380	Here, we demonstrate that fasting and chemical-genetic activation of orexigenic AgRP neurons in the hypothalamus suppress the browning of white fat.
25303527	4	8	mod	modification	480:491	arg3	O-GlcNAc					470:477	O-linked β-N-acetylglucosamine (O-GlcNAc) modification	438:491	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of cytoplasmic and nuclear proteins	438:527	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of cytoplasmic and nuclear proteins regulates fundamental cellular processes.
25303527	4	8	mod	modification	480:491	arg1	proteins					520:527	cytoplasmic and nuclear proteins	496:527	cytoplasmic and nuclear proteins	496:527	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of cytoplasmic and nuclear proteins regulates fundamental cellular processes.
25303527	4	8	mod	modification	480:491	arg3	β-N-acetylglucosamine					447:467	O-linked β-N-acetylglucosamine (O-GlcNAc) modification	438:491	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of cytoplasmic and nuclear proteins	438:527	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of cytoplasmic and nuclear proteins regulates fundamental cellular processes.
25303527	5	9	theme	modification	625:636	arg1	levels					575:580	The levels	571:580	The levels of O-GlcNAc transferase (OGT) and O-GlcNAc modification	571:636	The levels of O-GlcNAc transferase (OGT) and O-GlcNAc modification are enriched in AgRP neurons and are elevated by fasting.
25303527	5	9	theme	modification	625:636	arg1	enriched					642:649	enriched	642:649	enriched	642:649	The levels of O-GlcNAc transferase (OGT) and O-GlcNAc modification are enriched in AgRP neurons and are elevated by fasting.
25303527	5	9	theme	modification	625:636	arg1	elevated					675:682	elevated	675:682	elevated	675:682	The levels of O-GlcNAc transferase (OGT) and O-GlcNAc modification are enriched in AgRP neurons and are elevated by fasting.
25303527	4	10	theme	O-linked	438:445	arg1	modification					480:491	O-linked β-N-acetylglucosamine (O-GlcNAc) modification	438:491	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of cytoplasmic and nuclear proteins	438:527	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of cytoplasmic and nuclear proteins regulates fundamental cellular processes.
25303527	6	11	theme	AgRP	723:726	arg1	neurons					728:734	AgRP neurons	723:734	AgRP neurons	723:734	Genetic ablation of OGT in AgRP neurons inhibits neuronal excitability through the voltage-dependent potassium channel, promotes white adipose tissue browning, and protects mice against diet-induced obesity and insulin resistance.
25303527	3	12	theme	chemical-genetic	327:342	arg1	activation					344:353	chemical-genetic activation	327:353	chemical-genetic activation of orexigenic AgRP neurons in the hypothalamus	327:400	Here, we demonstrate that fasting and chemical-genetic activation of orexigenic AgRP neurons in the hypothalamus suppress the browning of white fat.
25303527	6	13	theme	adipose	831:837	arg1	tissue					839:844	white adipose tissue	825:844	white adipose tissue browning	825:853	Genetic ablation of OGT in AgRP neurons inhibits neuronal excitability through the voltage-dependent potassium channel, promotes white adipose tissue browning, and protects mice against diet-induced obesity and insulin resistance.
25303527	1	14	theme	energy	148:153	arg1	metabolism					155:164	energy metabolism	148:164	energy metabolism	148:164	Induction of beige cells causes the browning of white fat and improves energy metabolism.
25303527	4	15	theme	cytoplasmic	496:506	arg1	proteins					520:527	cytoplasmic and nuclear proteins	496:527	cytoplasmic and nuclear proteins	496:527	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of cytoplasmic and nuclear proteins regulates fundamental cellular processes.
25303527	5	16	theme	transferase	594:604	arg1	levels					575:580	The levels	571:580	The levels of O-GlcNAc transferase (OGT) and O-GlcNAc modification	571:636	The levels of O-GlcNAc transferase (OGT) and O-GlcNAc modification are enriched in AgRP neurons and are elevated by fasting.
25303527	5	16	theme	transferase	594:604	arg1	enriched					642:649	enriched	642:649	enriched	642:649	The levels of O-GlcNAc transferase (OGT) and O-GlcNAc modification are enriched in AgRP neurons and are elevated by fasting.
25303527	5	16	theme	transferase	594:604	arg1	elevated					675:682	elevated	675:682	elevated	675:682	The levels of O-GlcNAc transferase (OGT) and O-GlcNAc modification are enriched in AgRP neurons and are elevated by fasting.
25303527	6	17	theme	OGT	716:718	arg1	ablation					704:711	Genetic ablation	696:711	Genetic ablation of OGT in AgRP neurons	696:734	Genetic ablation of OGT in AgRP neurons inhibits neuronal excitability through the voltage-dependent potassium channel, promotes white adipose tissue browning, and protects mice against diet-induced obesity and insulin resistance.
25303527	7	18	theme	physiological	989:1001	arg1	process					1003:1009	a highly dynamic physiological process	972:1009	a highly dynamic physiological process	972:1009	These data reveal adipose tissue browning as a highly dynamic physiological process under central control, in which O-GlcNAc signaling in AgRP neurons is essential for suppressing thermogenesis to conserve energy in response to fasting.
25303527	7	18	theme	physiological	989:1001	arg1	browning					960:967	adipose tissue browning	945:967	adipose tissue browning	945:967	These data reveal adipose tissue browning as a highly dynamic physiological process under central control, in which O-GlcNAc signaling in AgRP neurons is essential for suppressing thermogenesis to conserve energy in response to fasting.
25303527	5	19	theme	AgRP	654:657	arg1	neurons					659:665	AgRP neurons	654:665	AgRP neurons	654:665	The levels of O-GlcNAc transferase (OGT) and O-GlcNAc modification are enriched in AgRP neurons and are elevated by fasting.
25303527	7	20	theme	dynamic	981:987	arg1	process					1003:1009	a highly dynamic physiological process	972:1009	a highly dynamic physiological process	972:1009	These data reveal adipose tissue browning as a highly dynamic physiological process under central control, in which O-GlcNAc signaling in AgRP neurons is essential for suppressing thermogenesis to conserve energy in response to fasting.
25303527	7	20	theme	dynamic	981:987	arg1	browning					960:967	adipose tissue browning	945:967	adipose tissue browning	945:967	These data reveal adipose tissue browning as a highly dynamic physiological process under central control, in which O-GlcNAc signaling in AgRP neurons is essential for suppressing thermogenesis to conserve energy in response to fasting.
25303527	0	21	theme	O-GlcNAc	0:7	arg1	transferase					9:19	O-GlcNAc transferase	0:19	O-GlcNAc transferase	0:19	O-GlcNAc transferase enables AgRP neurons to suppress browning of white fat.
25303527	0	22	theme	AgRP	29:32	arg1	neurons					34:40	AgRP neurons	29:40	AgRP neurons	29:40	O-GlcNAc transferase enables AgRP neurons to suppress browning of white fat.
25303527	3	23	theme	white	427:431	arg1	fat					433:435	white fat	427:435	white fat	427:435	Here, we demonstrate that fasting and chemical-genetic activation of orexigenic AgRP neurons in the hypothalamus suppress the browning of white fat.
25303527	3	24	theme	AgRP	369:372	arg1	neurons					374:380	orexigenic AgRP neurons	358:380	orexigenic AgRP neurons	358:380	Here, we demonstrate that fasting and chemical-genetic activation of orexigenic AgRP neurons in the hypothalamus suppress the browning of white fat.
25303527	5	25	from	neurons	659:665	arg1	levels					575:580	The levels	571:580	The levels of O-GlcNAc transferase (OGT) and O-GlcNAc modification	571:636	The levels of O-GlcNAc transferase (OGT) and O-GlcNAc modification are enriched in AgRP neurons and are elevated by fasting.
25303527	5	25	from	neurons	659:665	arg1	enriched					642:649	enriched	642:649	enriched	642:649	The levels of O-GlcNAc transferase (OGT) and O-GlcNAc modification are enriched in AgRP neurons and are elevated by fasting.
25303527	5	25	from	neurons	659:665	arg1	elevated					675:682	elevated	675:682	elevated	675:682	The levels of O-GlcNAc transferase (OGT) and O-GlcNAc modification are enriched in AgRP neurons and are elevated by fasting.
25303527	1	26	theme	beige	90:94	arg1	cells					96:100	beige cells	90:100	beige cells	90:100	Induction of beige cells causes the browning of white fat and improves energy metabolism.
25303527	6	27	theme	Genetic	696:702	arg1	ablation					704:711	Genetic ablation	696:711	Genetic ablation of OGT in AgRP neurons	696:734	Genetic ablation of OGT in AgRP neurons inhibits neuronal excitability through the voltage-dependent potassium channel, promotes white adipose tissue browning, and protects mice against diet-induced obesity and insulin resistance.
25303527	7	28	theme	AgRP	1065:1068	arg1	neurons					1070:1076	AgRP neurons	1065:1076	AgRP neurons	1065:1076	These data reveal adipose tissue browning as a highly dynamic physiological process under central control, in which O-GlcNAc signaling in AgRP neurons is essential for suppressing thermogenesis to conserve energy in response to fasting.
25303527	3	29	theme	neurons	374:380	arg1	fasting					315:321	fasting	315:321	fasting	315:321	Here, we demonstrate that fasting and chemical-genetic activation of orexigenic AgRP neurons in the hypothalamus suppress the browning of white fat.
25303527	3	29	theme	neurons	374:380	arg1	activation					344:353	chemical-genetic activation	327:353	chemical-genetic activation of orexigenic AgRP neurons in the hypothalamus	327:400	Here, we demonstrate that fasting and chemical-genetic activation of orexigenic AgRP neurons in the hypothalamus suppress the browning of white fat.
25303527	5	30	from	enriched	642:649	arg1	neurons					659:665	AgRP neurons	654:665	AgRP neurons	654:665	The levels of O-GlcNAc transferase (OGT) and O-GlcNAc modification are enriched in AgRP neurons and are elevated by fasting.
25303527	4	31	theme	β-N-acetylglucosamine	447:467	arg1	modification					480:491	O-linked β-N-acetylglucosamine (O-GlcNAc) modification	438:491	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of cytoplasmic and nuclear proteins	438:527	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of cytoplasmic and nuclear proteins regulates fundamental cellular processes.
25303527	1	32	theme	cells	96:100	arg1	Induction					77:85	Induction	77:85	Induction of beige cells	77:100	Induction of beige cells causes the browning of white fat and improves energy metabolism.
25303527	7	33	from	signaling	1052:1060	arg1	neurons					1070:1076	AgRP neurons	1065:1076	AgRP neurons	1065:1076	These data reveal adipose tissue browning as a highly dynamic physiological process under central control, in which O-GlcNAc signaling in AgRP neurons is essential for suppressing thermogenesis to conserve energy in response to fasting.
25303527	3	34	from	activation	344:353	arg1	hypothalamus					389:400	the hypothalamus	385:400	the hypothalamus	385:400	Here, we demonstrate that fasting and chemical-genetic activation of orexigenic AgRP neurons in the hypothalamus suppress the browning of white fat.
25303527	2	35	theme	tissue	220:225	arg1	browning					227:234	adipose tissue browning	212:234	adipose tissue browning	212:234	However, the central mechanism that controls adipose tissue browning and its physiological relevance are largely unknown.
25303527	3	36	theme	fat	433:435	arg1	browning					415:422	the browning	411:422	the browning of white fat	411:435	Here, we demonstrate that fasting and chemical-genetic activation of orexigenic AgRP neurons in the hypothalamus suppress the browning of white fat.
25303527	4	37	theme	cellular	551:558	arg1	processes					560:568	fundamental cellular processes	539:568	fundamental cellular processes	539:568	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of cytoplasmic and nuclear proteins regulates fundamental cellular processes.
25303527	4	38	theme	O-GlcNAc	470:477	arg1	modification					480:491	O-linked β-N-acetylglucosamine (O-GlcNAc) modification	438:491	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of cytoplasmic and nuclear proteins	438:527	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of cytoplasmic and nuclear proteins regulates fundamental cellular processes.
25303527	2	39	theme	adipose	212:218	arg1	browning					227:234	adipose tissue browning	212:234	adipose tissue browning	212:234	However, the central mechanism that controls adipose tissue browning and its physiological relevance are largely unknown.
25303527	6	40	theme	potassium	797:805	arg1	channel					807:813	the voltage-dependent potassium channel	775:813	the voltage-dependent potassium channel	775:813	Genetic ablation of OGT in AgRP neurons inhibits neuronal excitability through the voltage-dependent potassium channel, promotes white adipose tissue browning, and protects mice against diet-induced obesity and insulin resistance.
25303527	4	41	theme	fundamental	539:549	arg1	processes					560:568	fundamental cellular processes	539:568	fundamental cellular processes	539:568	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of cytoplasmic and nuclear proteins regulates fundamental cellular processes.
25303527	6	42	theme	tissue	839:844	arg1	browning					846:853	white adipose tissue browning	825:853	white adipose tissue browning	825:853	Genetic ablation of OGT in AgRP neurons inhibits neuronal excitability through the voltage-dependent potassium channel, promotes white adipose tissue browning, and protects mice against diet-induced obesity and insulin resistance.
25303527	6	43	theme	diet-induced	882:893	arg1	obesity					895:901	diet-induced obesity	882:901	diet-induced obesity	882:901	Genetic ablation of OGT in AgRP neurons inhibits neuronal excitability through the voltage-dependent potassium channel, promotes white adipose tissue browning, and protects mice against diet-induced obesity and insulin resistance.
25303527	6	44	theme	voltage-dependent	779:795	arg1	channel					807:813	the voltage-dependent potassium channel	775:813	the voltage-dependent potassium channel	775:813	Genetic ablation of OGT in AgRP neurons inhibits neuronal excitability through the voltage-dependent potassium channel, promotes white adipose tissue browning, and protects mice against diet-induced obesity and insulin resistance.
25303527	7	45	theme	O-GlcNAc	1043:1050	arg1	signaling					1052:1060	O-GlcNAc signaling	1043:1060	O-GlcNAc signaling in AgRP neurons	1043:1076	These data reveal adipose tissue browning as a highly dynamic physiological process under central control, in which O-GlcNAc signaling in AgRP neurons is essential for suppressing thermogenesis to conserve energy in response to fasting.
25303527	7	46	theme	tissue	953:958	arg1	process					1003:1009	a highly dynamic physiological process	972:1009	a highly dynamic physiological process	972:1009	These data reveal adipose tissue browning as a highly dynamic physiological process under central control, in which O-GlcNAc signaling in AgRP neurons is essential for suppressing thermogenesis to conserve energy in response to fasting.
25303527	7	46	theme	tissue	953:958	arg1	browning					960:967	adipose tissue browning	945:967	adipose tissue browning	945:967	These data reveal adipose tissue browning as a highly dynamic physiological process under central control, in which O-GlcNAc signaling in AgRP neurons is essential for suppressing thermogenesis to conserve energy in response to fasting.
25303527	2	47	theme	central	180:186	arg1	unknown					280:286	unknown	280:286	unknown	280:286	However, the central mechanism that controls adipose tissue browning and its physiological relevance are largely unknown.
25303527	2	47	theme	central	180:186	arg1	mechanism					188:196	the central mechanism	176:196	the central mechanism that controls adipose tissue browning and its physiological relevance	176:266	However, the central mechanism that controls adipose tissue browning and its physiological relevance are largely unknown.
25303527	2	48	theme	physiological	244:256	arg1	relevance					258:266	its physiological relevance	240:266	its physiological relevance	240:266	However, the central mechanism that controls adipose tissue browning and its physiological relevance are largely unknown.
25303527	5	49	theme	O-GlcNAc	585:592	arg1	OGT					607:609	OGT	607:609	OGT	607:609	The levels of O-GlcNAc transferase (OGT) and O-GlcNAc modification are enriched in AgRP neurons and are elevated by fasting.
25303527	5	49	theme	O-GlcNAc	585:592	arg1	transferase					594:604	O-GlcNAc transferase	585:604	O-GlcNAc transferase (OGT)	585:610	The levels of O-GlcNAc transferase (OGT) and O-GlcNAc modification are enriched in AgRP neurons and are elevated by fasting.
25303527	6	50	from	ablation	704:711	arg1	neurons					728:734	AgRP neurons	723:734	AgRP neurons	723:734	Genetic ablation of OGT in AgRP neurons inhibits neuronal excitability through the voltage-dependent potassium channel, promotes white adipose tissue browning, and protects mice against diet-induced obesity and insulin resistance.
25303527	3	51	from	fasting	315:321	arg1	hypothalamus					389:400	the hypothalamus	385:400	the hypothalamus	385:400	Here, we demonstrate that fasting and chemical-genetic activation of orexigenic AgRP neurons in the hypothalamus suppress the browning of white fat.
25303527	7	52	from	process	1003:1009	arg1	essential					1081:1089	essential	1081:1089	essential	1081:1089	These data reveal adipose tissue browning as a highly dynamic physiological process under central control, in which O-GlcNAc signaling in AgRP neurons is essential for suppressing thermogenesis to conserve energy in response to fasting.
25303527	0	53	theme	white	66:70	arg1	fat					72:74	white fat	66:74	white fat	66:74	O-GlcNAc transferase enables AgRP neurons to suppress browning of white fat.
25303527	6	54	theme	neuronal	745:752	arg1	excitability					754:765	neuronal excitability	745:765	neuronal excitability	745:765	Genetic ablation of OGT in AgRP neurons inhibits neuronal excitability through the voltage-dependent potassium channel, promotes white adipose tissue browning, and protects mice against diet-induced obesity and insulin resistance.
25303527	1	55	theme	white	125:129	arg1	fat					131:133	white fat	125:133	white fat	125:133	Induction of beige cells causes the browning of white fat and improves energy metabolism.
25303527	7	56	theme	adipose	945:951	arg1	process					1003:1009	a highly dynamic physiological process	972:1009	a highly dynamic physiological process	972:1009	These data reveal adipose tissue browning as a highly dynamic physiological process under central control, in which O-GlcNAc signaling in AgRP neurons is essential for suppressing thermogenesis to conserve energy in response to fasting.
25303527	7	56	theme	adipose	945:951	arg1	browning					960:967	adipose tissue browning	945:967	adipose tissue browning	945:967	These data reveal adipose tissue browning as a highly dynamic physiological process under central control, in which O-GlcNAc signaling in AgRP neurons is essential for suppressing thermogenesis to conserve energy in response to fasting.
25303527	7	57	from	essential	1081:1089	arg1	process					1003:1009	a highly dynamic physiological process	972:1009	a highly dynamic physiological process	972:1009	These data reveal adipose tissue browning as a highly dynamic physiological process under central control, in which O-GlcNAc signaling in AgRP neurons is essential for suppressing thermogenesis to conserve energy in response to fasting.
25303527	7	57	from	essential	1081:1089	arg1	browning					960:967	adipose tissue browning	945:967	adipose tissue browning	945:967	These data reveal adipose tissue browning as a highly dynamic physiological process under central control, in which O-GlcNAc signaling in AgRP neurons is essential for suppressing thermogenesis to conserve energy in response to fasting.
25303527	4	58	theme	nuclear	512:518	arg1	proteins					520:527	cytoplasmic and nuclear proteins	496:527	cytoplasmic and nuclear proteins	496:527	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of cytoplasmic and nuclear proteins regulates fundamental cellular processes.
25303527	1	59	theme	fat	131:133	arg1	browning					113:120	the browning	109:120	the browning of white fat	109:133	Induction of beige cells causes the browning of white fat and improves energy metabolism.
25303527	4	60	link	O-linked	438:445	arg1	modification					480:491	O-linked β-N-acetylglucosamine (O-GlcNAc) modification	438:491	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of cytoplasmic and nuclear proteins	438:527	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of cytoplasmic and nuclear proteins regulates fundamental cellular processes.
21285374	0	0	theme	maturation	92:101	arg1	pathway					103:109	the host cell factor-1 maturation pathway	69:109	the host cell factor-1 maturation pathway	69:109	Crosstalk between O-GlcNAcylation and proteolytic cleavage regulates the host cell factor-1 maturation pathway.
21285374	10	1	theme	posttranslational	1539:1555	arg1	modifications					1557:1569	these posttranslational modifications	1533:1569	these posttranslational modifications	1533:1569	Together the data indicate that O-GlcNAcylation of HCF-1 is a signal for its proteolytic processing and reveal a unique crosstalk between these posttranslational modifications.
21285374	9	2	theme	infection	1384:1392	arg1	initiation					1364:1373	the initiation	1360:1373	the initiation of viral infection	1360:1392	Moreover, we show that OGT-mediated modulation of HCF-1 impacts the expression of the herpes simplex virus immediate-early genes, targets of HCF-1 during the initiation of viral infection.
21285374	1	3	theme	critical	145:152	arg1	roles					154:158	critical roles	145:158	critical roles	145:158	Host Cell Factor 1 (HCF-1) plays critical roles in regulating gene expression in a plethora of physiological processes.
21285374	0	4	theme	factor-1	83:90	arg1	pathway					103:109	the host cell factor-1 maturation pathway	69:109	the host cell factor-1 maturation pathway	69:109	Crosstalk between O-GlcNAcylation and proteolytic cleavage regulates the host cell factor-1 maturation pathway.
21285374	10	5	theme	HCF-1	1446:1450	arg1	signal					1457:1462	a signal	1455:1462	a signal for its proteolytic processing	1455:1493	Together the data indicate that O-GlcNAcylation of HCF-1 is a signal for its proteolytic processing and reveal a unique crosstalk between these posttranslational modifications.
21285374	10	5	theme	HCF-1	1446:1450	arg1	O-GlcNAcylation					1427:1441	O-GlcNAcylation	1427:1441	O-GlcNAcylation of HCF-1	1427:1450	Together the data indicate that O-GlcNAcylation of HCF-1 is a signal for its proteolytic processing and reveal a unique crosstalk between these posttranslational modifications.
21285374	9	6	theme	virus	1307:1311	arg1	targets					1336:1342	targets	1336:1342	targets of HCF-1	1336:1351	Moreover, we show that OGT-mediated modulation of HCF-1 impacts the expression of the herpes simplex virus immediate-early genes, targets of HCF-1 during the initiation of viral infection.
21285374	9	6	theme	virus	1307:1311	arg1	genes					1329:1333	the herpes simplex virus immediate-early genes	1288:1333	the herpes simplex virus immediate-early genes	1288:1333	Moreover, we show that OGT-mediated modulation of HCF-1 impacts the expression of the herpes simplex virus immediate-early genes, targets of HCF-1 during the initiation of viral infection.
21285374	4	7	theme	HCF-1	584:588	arg1	process					617:623	a regulated process	605:623	a regulated process	605:623	Here we report that HCF-1 proteolysis is a regulated process.
21285374	4	7	theme	HCF-1	584:588	arg1	proteolysis					590:600	HCF-1 proteolysis	584:600	HCF-1 proteolysis	584:600	Here we report that HCF-1 proteolysis is a regulated process.
21285374	9	8	theme	herpes	1292:1297	arg1	virus					1307:1311	herpes simplex virus	1292:1311	the herpes simplex virus immediate-early genes	1288:1333	Moreover, we show that OGT-mediated modulation of HCF-1 impacts the expression of the herpes simplex virus immediate-early genes, targets of HCF-1 during the initiation of viral infection.
21285374	9	9	theme	simplex	1299:1305	arg1	virus					1307:1311	herpes simplex virus	1292:1311	the herpes simplex virus immediate-early genes	1288:1333	Moreover, we show that OGT-mediated modulation of HCF-1 impacts the expression of the herpes simplex virus immediate-early genes, targets of HCF-1 during the initiation of viral infection.
21285374	5	10	theme	signaling	672:680	arg1	transferase					719:729	signaling enzyme O-linked-N-acetylglucosaminyl transferase	672:729	the signaling enzyme O-linked-N-acetylglucosaminyl transferase (OGT)	668:735	We demonstrate that a large proportion of the signaling enzyme O-linked-N-acetylglucosaminyl transferase (OGT) is complexed with HCF-1 and this interaction is essential for HCF-1 cleavage.
21285374	5	10	theme	signaling	672:680	arg1	OGT					732:734	OGT	732:734	OGT	732:734	We demonstrate that a large proportion of the signaling enzyme O-linked-N-acetylglucosaminyl transferase (OGT) is complexed with HCF-1 and this interaction is essential for HCF-1 cleavage.
21285374	8	11	theme	region	1169:1174	arg1	O-GlcNAcylation					1145:1159	the O-GlcNAcylation	1141:1159	the O-GlcNAcylation of this region	1141:1174	In contrast, although OGT also interacts with the basic domain in the HCF-1 amino-terminal subunit, neither the interaction nor the O-GlcNAcylation of this region are required for proteolysis.
21285374	3	12	theme	transcriptional	494:508	arg1	activity					510:517	its transcriptional activity	490:517	its transcriptional activity	490:517	Although the underlying mechanism remains enigmatic, proteolysis of HCF-1 regulates its transcriptional activity and is important for cell cycle progression.
21285374	3	13	theme	cell	540:543	arg1	progression					551:561	cell cycle progression	540:561	cell cycle progression	540:561	Although the underlying mechanism remains enigmatic, proteolysis of HCF-1 regulates its transcriptional activity and is important for cell cycle progression.
21285374	1	14	theme	gene	174:177	arg1	expression					179:188	gene expression	174:188	gene expression in a plethora of physiological processes	174:229	Host Cell Factor 1 (HCF-1) plays critical roles in regulating gene expression in a plethora of physiological processes.
21285374	11	15	theme	several	1660:1666	arg1	functions					1668:1676	several functions	1660:1676	several functions	1660:1676	Additionally, interactions of OGT with multiple HCF-1 domains may indicate that OGT has several functions in association with HCF-1.
21285374	9	16	theme	immediate-early	1313:1327	arg1	targets					1336:1342	targets	1336:1342	targets of HCF-1	1336:1351	Moreover, we show that OGT-mediated modulation of HCF-1 impacts the expression of the herpes simplex virus immediate-early genes, targets of HCF-1 during the initiation of viral infection.
21285374	9	16	theme	immediate-early	1313:1327	arg1	genes					1329:1333	the herpes simplex virus immediate-early genes	1288:1333	the herpes simplex virus immediate-early genes	1288:1333	Moreover, we show that OGT-mediated modulation of HCF-1 impacts the expression of the herpes simplex virus immediate-early genes, targets of HCF-1 during the initiation of viral infection.
21285374	7	17	theme	HCF-1	939:943	arg1	cleavage					945:952	HCF-1 cleavage	939:952	HCF-1 cleavage	939:952	We provide evidence indicating that OGT regulates HCF-1 cleavage via interaction with and O-GlcNAcylation of the HCF-1 PPD.
21285374	3	18	theme	cycle	545:549	arg1	progression					551:561	cell cycle progression	540:561	cell cycle progression	540:561	Although the underlying mechanism remains enigmatic, proteolysis of HCF-1 regulates its transcriptional activity and is important for cell cycle progression.
21285374	9	19	theme	genes	1329:1333	arg1	expression					1274:1283	the expression	1270:1283	the expression of the herpes simplex virus immediate-early genes, targets of HCF-1	1270:1351	Moreover, we show that OGT-mediated modulation of HCF-1 impacts the expression of the herpes simplex virus immediate-early genes, targets of HCF-1 during the initiation of viral infection.
21285374	8	20	theme	basic	1063:1067	arg1	domain					1069:1074	the basic domain	1059:1074	the basic domain in the HCF-1 amino-terminal subunit	1059:1110	In contrast, although OGT also interacts with the basic domain in the HCF-1 amino-terminal subunit, neither the interaction nor the O-GlcNAcylation of this region are required for proteolysis.
21285374	8	21	theme	amino-terminal	1089:1102	arg1	subunit					1104:1110	the HCF-1 amino-terminal subunit	1079:1110	the HCF-1 amino-terminal subunit	1079:1110	In contrast, although OGT also interacts with the basic domain in the HCF-1 amino-terminal subunit, neither the interaction nor the O-GlcNAcylation of this region are required for proteolysis.
21285374	3	22	theme	underlying	419:428	arg1	mechanism					430:438	the underlying mechanism	415:438	the underlying mechanism	415:438	Although the underlying mechanism remains enigmatic, proteolysis of HCF-1 regulates its transcriptional activity and is important for cell cycle progression.
21285374	5	23	theme	large	648:652	arg1	proportion					654:663	a large proportion	646:663	a large proportion of the signaling enzyme O-linked-N-acetylglucosaminyl transferase (OGT)	646:735	We demonstrate that a large proportion of the signaling enzyme O-linked-N-acetylglucosaminyl transferase (OGT) is complexed with HCF-1 and this interaction is essential for HCF-1 cleavage.
21285374	11	24	contain	has	1656:1658	arg1	OGT					1652:1654	OGT	1652:1654	OGT	1652:1654	Additionally, interactions of OGT with multiple HCF-1 domains may indicate that OGT has several functions in association with HCF-1.
21285374	11	24	contain	has	1656:1658	arg2	functions					1668:1676	several functions	1660:1676	several functions	1660:1676	Additionally, interactions of OGT with multiple HCF-1 domains may indicate that OGT has several functions in association with HCF-1.
21285374	2	25	dep	synthesized	247:257	arg1	cleaved					321:327	cleaved	321:327	proteolytically cleaved within a large middle region termed the proteolytic processing domain (PPD)	305:403	HCF-1 is first synthesized as a precursor, and subsequently specifically proteolytically cleaved within a large middle region termed the proteolytic processing domain (PPD).
21285374	1	26	theme	Host	112:115	arg1	Factor					122:127	Host Cell Factor 1	112:129	Host Cell Factor 1 (HCF-1)	112:137	Host Cell Factor 1 (HCF-1) plays critical roles in regulating gene expression in a plethora of physiological processes.
21285374	1	26	theme	Host	112:115	arg1	HCF-1					132:136	HCF-1	132:136	HCF-1	132:136	Host Cell Factor 1 (HCF-1) plays critical roles in regulating gene expression in a plethora of physiological processes.
21285374	7	27	theme	HCF-1	1002:1006	arg1	PPD					1008:1010	the HCF-1 PPD	998:1010	the HCF-1 PPD	998:1010	We provide evidence indicating that OGT regulates HCF-1 cleavage via interaction with and O-GlcNAcylation of the HCF-1 PPD.
21285374	11	28	with	interactions	1586:1597	arg1	domains					1626:1632	multiple HCF-1 domains	1611:1632	multiple HCF-1 domains	1611:1632	Additionally, interactions of OGT with multiple HCF-1 domains may indicate that OGT has several functions in association with HCF-1.
21285374	11	29	theme	OGT	1602:1604	arg1	interactions					1586:1597	interactions	1586:1597	interactions of OGT with multiple HCF-1 domains	1586:1632	Additionally, interactions of OGT with multiple HCF-1 domains may indicate that OGT has several functions in association with HCF-1.
21285374	1	30	theme	Cell	117:120	arg1	Factor					122:127	Host Cell Factor 1	112:129	Host Cell Factor 1 (HCF-1)	112:137	Host Cell Factor 1 (HCF-1) plays critical roles in regulating gene expression in a plethora of physiological processes.
21285374	1	30	theme	Cell	117:120	arg1	HCF-1					132:136	HCF-1	132:136	HCF-1	132:136	Host Cell Factor 1 (HCF-1) plays critical roles in regulating gene expression in a plethora of physiological processes.
21285374	3	31	theme	HCF-1	474:478	arg1	proteolysis					459:469	proteolysis	459:469	proteolysis of HCF-1	459:478	Although the underlying mechanism remains enigmatic, proteolysis of HCF-1 regulates its transcriptional activity and is important for cell cycle progression.
21285374	5	32	theme	HCF-1	799:803	arg1	cleavage					805:812	HCF-1 cleavage	799:812	HCF-1 cleavage	799:812	We demonstrate that a large proportion of the signaling enzyme O-linked-N-acetylglucosaminyl transferase (OGT) is complexed with HCF-1 and this interaction is essential for HCF-1 cleavage.
21285374	9	33	theme	HCF-1	1347:1351	arg1	targets					1336:1342	targets	1336:1342	targets of HCF-1	1336:1351	Moreover, we show that OGT-mediated modulation of HCF-1 impacts the expression of the herpes simplex virus immediate-early genes, targets of HCF-1 during the initiation of viral infection.
21285374	9	33	theme	HCF-1	1347:1351	arg1	genes					1329:1333	the herpes simplex virus immediate-early genes	1288:1333	the herpes simplex virus immediate-early genes	1288:1333	Moreover, we show that OGT-mediated modulation of HCF-1 impacts the expression of the herpes simplex virus immediate-early genes, targets of HCF-1 during the initiation of viral infection.
21285374	8	34	theme	HCF-1	1083:1087	arg1	subunit					1104:1110	the HCF-1 amino-terminal subunit	1079:1110	the HCF-1 amino-terminal subunit	1079:1110	In contrast, although OGT also interacts with the basic domain in the HCF-1 amino-terminal subunit, neither the interaction nor the O-GlcNAcylation of this region are required for proteolysis.
21285374	2	35	theme	processing	381:390	arg1	PPD					400:402	PPD	400:402	PPD	400:402	HCF-1 is first synthesized as a precursor, and subsequently specifically proteolytically cleaved within a large middle region termed the proteolytic processing domain (PPD).
21285374	2	35	theme	processing	381:390	arg1	domain					392:397	the proteolytic processing domain	365:397	the proteolytic processing domain (PPD)	365:403	HCF-1 is first synthesized as a precursor, and subsequently specifically proteolytically cleaved within a large middle region termed the proteolytic processing domain (PPD).
21285374	0	36	theme	proteolytic	38:48	arg1	cleavage					50:57	proteolytic cleavage	38:57	proteolytic cleavage	38:57	Crosstalk between O-GlcNAcylation and proteolytic cleavage regulates the host cell factor-1 maturation pathway.
21285374	10	37	theme	proteolytic	1472:1482	arg1	processing					1484:1493	its proteolytic processing	1468:1493	its proteolytic processing	1468:1493	Together the data indicate that O-GlcNAcylation of HCF-1 is a signal for its proteolytic processing and reveal a unique crosstalk between these posttranslational modifications.
21285374	9	38	theme	OGT-mediated	1229:1240	arg1	modulation					1242:1251	OGT-mediated modulation	1229:1251	OGT-mediated modulation of HCF-1	1229:1260	Moreover, we show that OGT-mediated modulation of HCF-1 impacts the expression of the herpes simplex virus immediate-early genes, targets of HCF-1 during the initiation of viral infection.
21285374	11	39	theme	multiple	1611:1618	arg1	domains					1626:1632	multiple HCF-1 domains	1611:1632	multiple HCF-1 domains	1611:1632	Additionally, interactions of OGT with multiple HCF-1 domains may indicate that OGT has several functions in association with HCF-1.
21285374	7	40	with	interaction	958:968	arg1	O-GlcNAcylation					979:993	and O-GlcNAcylation	975:993	O-GlcNAcylation	979:993	We provide evidence indicating that OGT regulates HCF-1 cleavage via interaction with and O-GlcNAcylation of the HCF-1 PPD.
21285374	5	41	theme	enzyme	682:687	arg1	transferase					719:729	signaling enzyme O-linked-N-acetylglucosaminyl transferase	672:729	the signaling enzyme O-linked-N-acetylglucosaminyl transferase (OGT)	668:735	We demonstrate that a large proportion of the signaling enzyme O-linked-N-acetylglucosaminyl transferase (OGT) is complexed with HCF-1 and this interaction is essential for HCF-1 cleavage.
21285374	5	41	theme	enzyme	682:687	arg1	OGT					732:734	OGT	732:734	OGT	732:734	We demonstrate that a large proportion of the signaling enzyme O-linked-N-acetylglucosaminyl transferase (OGT) is complexed with HCF-1 and this interaction is essential for HCF-1 cleavage.
21285374	10	42	theme	unique	1508:1513	arg1	crosstalk					1515:1523	a unique crosstalk	1506:1523	a unique crosstalk between these posttranslational modifications	1506:1569	Together the data indicate that O-GlcNAcylation of HCF-1 is a signal for its proteolytic processing and reveal a unique crosstalk between these posttranslational modifications.
21285374	2	43	theme	middle	344:349	arg1	region					351:356	a large middle region	336:356	a large middle region termed the proteolytic processing domain (PPD)	336:403	HCF-1 is first synthesized as a precursor, and subsequently specifically proteolytically cleaved within a large middle region termed the proteolytic processing domain (PPD).
21285374	4	44	theme	regulated	607:615	arg1	process					617:623	a regulated process	605:623	a regulated process	605:623	Here we report that HCF-1 proteolysis is a regulated process.
21285374	4	44	theme	regulated	607:615	arg1	proteolysis					590:600	HCF-1 proteolysis	584:600	HCF-1 proteolysis	584:600	Here we report that HCF-1 proteolysis is a regulated process.
21285374	5	45	theme	O-linked-N-acetylglucosaminyl	689:717	arg1	transferase					719:729	signaling enzyme O-linked-N-acetylglucosaminyl transferase	672:729	the signaling enzyme O-linked-N-acetylglucosaminyl transferase (OGT)	668:735	We demonstrate that a large proportion of the signaling enzyme O-linked-N-acetylglucosaminyl transferase (OGT) is complexed with HCF-1 and this interaction is essential for HCF-1 cleavage.
21285374	5	45	theme	O-linked-N-acetylglucosaminyl	689:717	arg1	OGT					732:734	OGT	732:734	OGT	732:734	We demonstrate that a large proportion of the signaling enzyme O-linked-N-acetylglucosaminyl transferase (OGT) is complexed with HCF-1 and this interaction is essential for HCF-1 cleavage.
21285374	7	46	theme	PPD	1008:1010	arg1	O-GlcNAcylation					979:993	and O-GlcNAcylation	975:993	O-GlcNAcylation	979:993	We provide evidence indicating that OGT regulates HCF-1 cleavage via interaction with and O-GlcNAcylation of the HCF-1 PPD.
21285374	2	47	theme	large	338:342	arg1	region					351:356	a large middle region	336:356	a large middle region termed the proteolytic processing domain (PPD)	336:403	HCF-1 is first synthesized as a precursor, and subsequently specifically proteolytically cleaved within a large middle region termed the proteolytic processing domain (PPD).
21285374	5	48	theme	transferase	719:729	arg1	proportion					654:663	a large proportion	646:663	a large proportion of the signaling enzyme O-linked-N-acetylglucosaminyl transferase (OGT)	646:735	We demonstrate that a large proportion of the signaling enzyme O-linked-N-acetylglucosaminyl transferase (OGT) is complexed with HCF-1 and this interaction is essential for HCF-1 cleavage.
21285374	9	49	theme	HCF-1	1256:1260	arg1	modulation					1242:1251	OGT-mediated modulation	1229:1251	OGT-mediated modulation of HCF-1	1229:1260	Moreover, we show that OGT-mediated modulation of HCF-1 impacts the expression of the herpes simplex virus immediate-early genes, targets of HCF-1 during the initiation of viral infection.
21285374	11	50	with	association	1681:1691	arg1	HCF-1					1698:1702	HCF-1	1698:1702	HCF-1	1698:1702	Additionally, interactions of OGT with multiple HCF-1 domains may indicate that OGT has several functions in association with HCF-1.
21285374	1	51	theme	physiological	207:219	arg1	processes					221:229	physiological processes	207:229	physiological processes	207:229	Host Cell Factor 1 (HCF-1) plays critical roles in regulating gene expression in a plethora of physiological processes.
21285374	8	52	gly	O-GlcNAcylation	1145:1159	arg1	contrast					1016:1023	contrast	1016:1023	contrast	1016:1023	In contrast, although OGT also interacts with the basic domain in the HCF-1 amino-terminal subunit, neither the interaction nor the O-GlcNAcylation of this region are required for proteolysis.
21285374	1	53	theme	processes	221:229	arg1	plethora					195:202	a plethora	193:202	a plethora of physiological processes	193:229	Host Cell Factor 1 (HCF-1) plays critical roles in regulating gene expression in a plethora of physiological processes.
21285374	0	54	theme	cell	78:81	arg1	pathway					103:109	the host cell factor-1 maturation pathway	69:109	the host cell factor-1 maturation pathway	69:109	Crosstalk between O-GlcNAcylation and proteolytic cleavage regulates the host cell factor-1 maturation pathway.
21285374	1	55	from	expression	179:188	arg1	plethora					195:202	a plethora	193:202	a plethora of physiological processes	193:229	Host Cell Factor 1 (HCF-1) plays critical roles in regulating gene expression in a plethora of physiological processes.
21285374	2	56	theme	proteolytic	369:379	arg1	PPD					400:402	PPD	400:402	PPD	400:402	HCF-1 is first synthesized as a precursor, and subsequently specifically proteolytically cleaved within a large middle region termed the proteolytic processing domain (PPD).
21285374	2	56	theme	proteolytic	369:379	arg1	domain					392:397	the proteolytic processing domain	365:397	the proteolytic processing domain (PPD)	365:403	HCF-1 is first synthesized as a precursor, and subsequently specifically proteolytically cleaved within a large middle region termed the proteolytic processing domain (PPD).
21285374	0	57	theme	host	73:76	arg1	pathway					103:109	the host cell factor-1 maturation pathway	69:109	the host cell factor-1 maturation pathway	69:109	Crosstalk between O-GlcNAcylation and proteolytic cleavage regulates the host cell factor-1 maturation pathway.
21285374	11	58	theme	HCF-1	1620:1624	arg1	domains					1626:1632	multiple HCF-1 domains	1611:1632	multiple HCF-1 domains	1611:1632	Additionally, interactions of OGT with multiple HCF-1 domains may indicate that OGT has several functions in association with HCF-1.
21285374	9	59	theme	viral	1378:1382	arg1	infection					1384:1392	viral infection	1378:1392	viral infection	1378:1392	Moreover, we show that OGT-mediated modulation of HCF-1 impacts the expression of the herpes simplex virus immediate-early genes, targets of HCF-1 during the initiation of viral infection.
21285374	8	60	from	domain	1069:1074	arg1	subunit					1104:1110	the HCF-1 amino-terminal subunit	1079:1110	the HCF-1 amino-terminal subunit	1079:1110	In contrast, although OGT also interacts with the basic domain in the HCF-1 amino-terminal subunit, neither the interaction nor the O-GlcNAcylation of this region are required for proteolysis.
22883232	3	0	theme	glucose	344:350	arg1	portion					333:339	A small portion	325:339	A small portion of glucose	325:350	A small portion of glucose metabolizes through the hexosamine biosynthetic pathway, which leads to O-linked β-N-acetylglucosamine (O-GlcNAc) modification of cytoplasmic and nuclear proteins.
22883232	5	1	theme	deubiquitinase	785:798	arg1	BAP1					800:803	the deubiquitinase BAP1	781:803	the deubiquitinase BAP1	781:803	HCF-1 recruits OGT to O-GlcNAcylate PGC-1α, and O-GlcNAcylation facilitates the binding of the deubiquitinase BAP1, thus protecting PGC-1α from degradation and promoting gluconeogenesis.
22883232	5	2	dep	facilitates	754:764	arg1	protecting					811:820	protecting	811:820	protecting PGC-1α from degradation	811:844	HCF-1 recruits OGT to O-GlcNAcylate PGC-1α, and O-GlcNAcylation facilitates the binding of the deubiquitinase BAP1, thus protecting PGC-1α from degradation and promoting gluconeogenesis.
22883232	5	2	dep	facilitates	754:764	arg1	promoting					850:858	promoting	850:858	promoting gluconeogenesis	850:874	HCF-1 recruits OGT to O-GlcNAcylate PGC-1α, and O-GlcNAcylation facilitates the binding of the deubiquitinase BAP1, thus protecting PGC-1α from degradation and promoting gluconeogenesis.
22883232	1	3	theme	inappropriate	162:174	arg1	gluconeogenesis					184:198	inappropriate hepatic gluconeogenesis	162:198	inappropriate hepatic gluconeogenesis	162:198	A major cause of hyperglycemia in diabetic patients is inappropriate hepatic gluconeogenesis.
22883232	1	3	theme	inappropriate	162:174	arg1	cause					115:119	A major cause	107:119	A major cause of hyperglycemia in diabetic patients	107:157	A major cause of hyperglycemia in diabetic patients is inappropriate hepatic gluconeogenesis.
22883232	6	4	theme	O-GlcNAcylation	957:971	arg1	regulation					936:945	the regulation	932:945	the regulation of PGC-1α O-GlcNAcylation and stability by the OGT/HCF-1 complex	932:1010	Glucose availability modulates gluconeogenesis through the regulation of PGC-1α O-GlcNAcylation and stability by the OGT/HCF-1 complex.
22883232	0	5	theme	PGC-1α	89:94	arg1	stability					96:104	PGC-1α stability	89:104	PGC-1α stability	89:104	O-GlcNAc transferase/host cell factor C1 complex regulates gluconeogenesis by modulating PGC-1α stability.
22883232	4	6	theme	broad	560:564	arg1	proteins					577:584	proteins	577:584	proteins associated with O-GlcNAc transferase (OGT), among which host cell factor C1 (HCF-1) is highly abundant	577:687	Using a proteomic approach, we identified a broad variety of proteins associated with O-GlcNAc transferase (OGT), among which host cell factor C1 (HCF-1) is highly abundant.
22883232	4	6	theme	broad	560:564	arg1	variety					566:572	a broad variety	558:572	a broad variety of proteins associated with O-GlcNAc transferase (OGT), among which host cell factor C1 (HCF-1) is highly abundant	558:687	Using a proteomic approach, we identified a broad variety of proteins associated with O-GlcNAc transferase (OGT), among which host cell factor C1 (HCF-1) is highly abundant.
22883232	7	7	theme	OGT	1034:1036	arg1	knockdown					1021:1029	Hepatic knockdown	1013:1029	Hepatic knockdown of OGT and HCF-1	1013:1046	Hepatic knockdown of OGT and HCF-1 improves glucose homeostasis in diabetic mice.
22883232	1	8	theme	hepatic	176:182	arg1	gluconeogenesis					184:198	inappropriate hepatic gluconeogenesis	162:198	inappropriate hepatic gluconeogenesis	162:198	A major cause of hyperglycemia in diabetic patients is inappropriate hepatic gluconeogenesis.
22883232	1	8	theme	hepatic	176:182	arg1	cause					115:119	A major cause	107:119	A major cause of hyperglycemia in diabetic patients	107:157	A major cause of hyperglycemia in diabetic patients is inappropriate hepatic gluconeogenesis.
22883232	3	9	theme	O-linked	424:431	arg1	modification					466:477	O-linked β-N-acetylglucosamine (O-GlcNAc) modification	424:477	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of cytoplasmic and nuclear proteins	424:513	A small portion of glucose metabolizes through the hexosamine biosynthetic pathway, which leads to O-linked β-N-acetylglucosamine (O-GlcNAc) modification of cytoplasmic and nuclear proteins.
22883232	4	10	theme	proteomic	524:532	arg1	approach					534:541	a proteomic approach	522:541	a proteomic approach	522:541	Using a proteomic approach, we identified a broad variety of proteins associated with O-GlcNAc transferase (OGT), among which host cell factor C1 (HCF-1) is highly abundant.
22883232	3	11	theme	hexosamine	376:385	arg1	pathway					400:406	the hexosamine biosynthetic pathway	372:406	the hexosamine biosynthetic pathway	372:406	A small portion of glucose metabolizes through the hexosamine biosynthetic pathway, which leads to O-linked β-N-acetylglucosamine (O-GlcNAc) modification of cytoplasmic and nuclear proteins.
22883232	6	12	theme	PGC-1α	950:955	arg1	O-GlcNAcylation					957:971	PGC-1α O-GlcNAcylation	950:971	PGC-1α O-GlcNAcylation	950:971	Glucose availability modulates gluconeogenesis through the regulation of PGC-1α O-GlcNAcylation and stability by the OGT/HCF-1 complex.
22883232	2	13	theme	posttranslational	292:308	arg1	modifications					310:322	various posttranslational modifications	284:322	various posttranslational modifications	284:322	PGC-1α is a master regulator of gluconeogenesis, and its activity is controlled by various posttranslational modifications.
22883232	3	14	theme	cytoplasmic	482:492	arg1	proteins					506:513	cytoplasmic and nuclear proteins	482:513	cytoplasmic and nuclear proteins	482:513	A small portion of glucose metabolizes through the hexosamine biosynthetic pathway, which leads to O-linked β-N-acetylglucosamine (O-GlcNAc) modification of cytoplasmic and nuclear proteins.
22883232	3	15	theme	biosynthetic	387:398	arg1	pathway					400:406	the hexosamine biosynthetic pathway	372:406	the hexosamine biosynthetic pathway	372:406	A small portion of glucose metabolizes through the hexosamine biosynthetic pathway, which leads to O-linked β-N-acetylglucosamine (O-GlcNAc) modification of cytoplasmic and nuclear proteins.
22883232	8	16	theme	OGT/HCF-1	1121:1129	arg1	complex					1131:1137	the OGT/HCF-1 complex	1117:1137	the OGT/HCF-1 complex	1117:1137	These findings define the OGT/HCF-1 complex as a glucose sensor and key regulator of gluconeogenesis, shedding light on new strategies for treating diabetes.
22883232	8	16	theme	OGT/HCF-1	1121:1129	arg1	sensor					1152:1157	a glucose sensor	1142:1157	a glucose sensor	1142:1157	These findings define the OGT/HCF-1 complex as a glucose sensor and key regulator of gluconeogenesis, shedding light on new strategies for treating diabetes.
22883232	2	17	theme	various	284:290	arg1	modifications					310:322	various posttranslational modifications	284:322	various posttranslational modifications	284:322	PGC-1α is a master regulator of gluconeogenesis, and its activity is controlled by various posttranslational modifications.
22883232	0	18	theme	transferase/host	9:24	arg1	complex					41:47	O-GlcNAc transferase/host cell factor C1 complex	0:47	O-GlcNAc transferase/host cell factor C1 complex	0:47	O-GlcNAc transferase/host cell factor C1 complex regulates gluconeogenesis by modulating PGC-1α stability.
22883232	5	19	theme	BAP1	800:803	arg1	binding					770:776	the binding	766:776	the binding of the deubiquitinase BAP1	766:803	HCF-1 recruits OGT to O-GlcNAcylate PGC-1α, and O-GlcNAcylation facilitates the binding of the deubiquitinase BAP1, thus protecting PGC-1α from degradation and promoting gluconeogenesis.
22883232	7	20	theme	Hepatic	1013:1019	arg1	knockdown					1021:1029	Hepatic knockdown	1013:1029	Hepatic knockdown of OGT and HCF-1	1013:1046	Hepatic knockdown of OGT and HCF-1 improves glucose homeostasis in diabetic mice.
22883232	0	21	theme	O-GlcNAc	0:7	arg1	complex					41:47	O-GlcNAc transferase/host cell factor C1 complex	0:47	O-GlcNAc transferase/host cell factor C1 complex	0:47	O-GlcNAc transferase/host cell factor C1 complex regulates gluconeogenesis by modulating PGC-1α stability.
22883232	4	22	theme	O-GlcNAc	602:609	arg1	OGT					624:626	OGT	624:626	OGT	624:626	Using a proteomic approach, we identified a broad variety of proteins associated with O-GlcNAc transferase (OGT), among which host cell factor C1 (HCF-1) is highly abundant.
22883232	4	22	theme	O-GlcNAc	602:609	arg1	transferase					611:621	O-GlcNAc transferase	602:621	O-GlcNAc transferase (OGT)	602:627	Using a proteomic approach, we identified a broad variety of proteins associated with O-GlcNAc transferase (OGT), among which host cell factor C1 (HCF-1) is highly abundant.
22883232	6	23	theme	OGT/HCF-1	994:1002	arg1	complex					1004:1010	the OGT/HCF-1 complex	990:1010	the OGT/HCF-1 complex	990:1010	Glucose availability modulates gluconeogenesis through the regulation of PGC-1α O-GlcNAcylation and stability by the OGT/HCF-1 complex.
22883232	8	24	theme	new	1215:1217	arg1	strategies					1219:1228	new strategies	1215:1228	new strategies for treating diabetes	1215:1250	These findings define the OGT/HCF-1 complex as a glucose sensor and key regulator of gluconeogenesis, shedding light on new strategies for treating diabetes.
22883232	7	25	from	homeostasis	1065:1075	arg1	mice					1089:1092	diabetic mice	1080:1092	diabetic mice	1080:1092	Hepatic knockdown of OGT and HCF-1 improves glucose homeostasis in diabetic mice.
22883232	0	26	theme	factor	31:36	arg1	complex					41:47	O-GlcNAc transferase/host cell factor C1 complex	0:47	O-GlcNAc transferase/host cell factor C1 complex	0:47	O-GlcNAc transferase/host cell factor C1 complex regulates gluconeogenesis by modulating PGC-1α stability.
22883232	5	27	theme	O-GlcNAcylate	712:724	arg1	PGC-1α					726:731	O-GlcNAcylate PGC-1α	712:731	O-GlcNAcylate PGC-1α	712:731	HCF-1 recruits OGT to O-GlcNAcylate PGC-1α, and O-GlcNAcylation facilitates the binding of the deubiquitinase BAP1, thus protecting PGC-1α from degradation and promoting gluconeogenesis.
22883232	1	28	theme	major	109:113	arg1	gluconeogenesis					184:198	inappropriate hepatic gluconeogenesis	162:198	inappropriate hepatic gluconeogenesis	162:198	A major cause of hyperglycemia in diabetic patients is inappropriate hepatic gluconeogenesis.
22883232	1	28	theme	major	109:113	arg1	cause					115:119	A major cause	107:119	A major cause of hyperglycemia in diabetic patients	107:157	A major cause of hyperglycemia in diabetic patients is inappropriate hepatic gluconeogenesis.
22883232	0	29	theme	cell	26:29	arg1	complex					41:47	O-GlcNAc transferase/host cell factor C1 complex	0:47	O-GlcNAc transferase/host cell factor C1 complex	0:47	O-GlcNAc transferase/host cell factor C1 complex regulates gluconeogenesis by modulating PGC-1α stability.
22883232	8	30	theme	glucose	1144:1150	arg1	complex					1131:1137	the OGT/HCF-1 complex	1117:1137	the OGT/HCF-1 complex	1117:1137	These findings define the OGT/HCF-1 complex as a glucose sensor and key regulator of gluconeogenesis, shedding light on new strategies for treating diabetes.
22883232	8	30	theme	glucose	1144:1150	arg1	sensor					1152:1157	a glucose sensor	1142:1157	a glucose sensor	1142:1157	These findings define the OGT/HCF-1 complex as a glucose sensor and key regulator of gluconeogenesis, shedding light on new strategies for treating diabetes.
22883232	3	31	theme	O-GlcNAc	456:463	arg1	modification					466:477	O-linked β-N-acetylglucosamine (O-GlcNAc) modification	424:477	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of cytoplasmic and nuclear proteins	424:513	A small portion of glucose metabolizes through the hexosamine biosynthetic pathway, which leads to O-linked β-N-acetylglucosamine (O-GlcNAc) modification of cytoplasmic and nuclear proteins.
22883232	8	32	theme	key	1163:1165	arg1	regulator					1167:1175	key regulator	1163:1175	key regulator	1163:1175	These findings define the OGT/HCF-1 complex as a glucose sensor and key regulator of gluconeogenesis, shedding light on new strategies for treating diabetes.
22883232	3	33	theme	nuclear	498:504	arg1	proteins					506:513	cytoplasmic and nuclear proteins	482:513	cytoplasmic and nuclear proteins	482:513	A small portion of glucose metabolizes through the hexosamine biosynthetic pathway, which leads to O-linked β-N-acetylglucosamine (O-GlcNAc) modification of cytoplasmic and nuclear proteins.
22883232	0	34	theme	C1	38:39	arg1	complex					41:47	O-GlcNAc transferase/host cell factor C1 complex	0:47	O-GlcNAc transferase/host cell factor C1 complex	0:47	O-GlcNAc transferase/host cell factor C1 complex regulates gluconeogenesis by modulating PGC-1α stability.
22883232	3	35	theme	proteins	506:513	arg1	modification					466:477	O-linked β-N-acetylglucosamine (O-GlcNAc) modification	424:477	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of cytoplasmic and nuclear proteins	424:513	A small portion of glucose metabolizes through the hexosamine biosynthetic pathway, which leads to O-linked β-N-acetylglucosamine (O-GlcNAc) modification of cytoplasmic and nuclear proteins.
22883232	3	36	theme	β-N-acetylglucosamine	433:453	arg1	modification					466:477	O-linked β-N-acetylglucosamine (O-GlcNAc) modification	424:477	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of cytoplasmic and nuclear proteins	424:513	A small portion of glucose metabolizes through the hexosamine biosynthetic pathway, which leads to O-linked β-N-acetylglucosamine (O-GlcNAc) modification of cytoplasmic and nuclear proteins.
22883232	6	37	theme	stability	977:985	arg1	regulation					936:945	the regulation	932:945	the regulation of PGC-1α O-GlcNAcylation and stability by the OGT/HCF-1 complex	932:1010	Glucose availability modulates gluconeogenesis through the regulation of PGC-1α O-GlcNAcylation and stability by the OGT/HCF-1 complex.
22883232	2	38	theme	gluconeogenesis	233:247	arg1	PGC-1α					201:206	PGC-1α	201:206	PGC-1α	201:206	PGC-1α is a master regulator of gluconeogenesis, and its activity is controlled by various posttranslational modifications.
22883232	2	38	theme	gluconeogenesis	233:247	arg1	regulator					220:228	a master regulator	211:228	a master regulator of gluconeogenesis	211:247	PGC-1α is a master regulator of gluconeogenesis, and its activity is controlled by various posttranslational modifications.
22883232	1	39	theme	hyperglycemia	124:136	arg1	gluconeogenesis					184:198	inappropriate hepatic gluconeogenesis	162:198	inappropriate hepatic gluconeogenesis	162:198	A major cause of hyperglycemia in diabetic patients is inappropriate hepatic gluconeogenesis.
22883232	1	39	theme	hyperglycemia	124:136	arg1	cause					115:119	A major cause	107:119	A major cause of hyperglycemia in diabetic patients	107:157	A major cause of hyperglycemia in diabetic patients is inappropriate hepatic gluconeogenesis.
22883232	4	40	theme	proteins	577:584	arg1	proteins					577:584	proteins	577:584	proteins associated with O-GlcNAc transferase (OGT), among which host cell factor C1 (HCF-1) is highly abundant	577:687	Using a proteomic approach, we identified a broad variety of proteins associated with O-GlcNAc transferase (OGT), among which host cell factor C1 (HCF-1) is highly abundant.
22883232	4	40	theme	proteins	577:584	arg1	variety					566:572	a broad variety	558:572	a broad variety of proteins associated with O-GlcNAc transferase (OGT), among which host cell factor C1 (HCF-1) is highly abundant	558:687	Using a proteomic approach, we identified a broad variety of proteins associated with O-GlcNAc transferase (OGT), among which host cell factor C1 (HCF-1) is highly abundant.
22883232	6	41	theme	Glucose	877:883	arg1	availability					885:896	Glucose availability	877:896	Glucose availability	877:896	Glucose availability modulates gluconeogenesis through the regulation of PGC-1α O-GlcNAcylation and stability by the OGT/HCF-1 complex.
22883232	7	42	theme	diabetic	1080:1087	arg1	mice					1089:1092	diabetic mice	1080:1092	diabetic mice	1080:1092	Hepatic knockdown of OGT and HCF-1 improves glucose homeostasis in diabetic mice.
22883232	1	43	from	cause	115:119	arg1	patients					150:157	diabetic patients	141:157	diabetic patients	141:157	A major cause of hyperglycemia in diabetic patients is inappropriate hepatic gluconeogenesis.
22883232	4	44	theme	host	642:645	arg1	HCF-1					663:667	HCF-1	663:667	HCF-1	663:667	Using a proteomic approach, we identified a broad variety of proteins associated with O-GlcNAc transferase (OGT), among which host cell factor C1 (HCF-1) is highly abundant.
22883232	4	44	theme	host	642:645	arg1	C1					659:660	host cell factor C1	642:660	host cell factor C1 (HCF-1)	642:668	Using a proteomic approach, we identified a broad variety of proteins associated with O-GlcNAc transferase (OGT), among which host cell factor C1 (HCF-1) is highly abundant.
22883232	3	45	theme	small	327:331	arg1	portion					333:339	A small portion	325:339	A small portion of glucose	325:350	A small portion of glucose metabolizes through the hexosamine biosynthetic pathway, which leads to O-linked β-N-acetylglucosamine (O-GlcNAc) modification of cytoplasmic and nuclear proteins.
22883232	2	46	theme	master	213:218	arg1	PGC-1α					201:206	PGC-1α	201:206	PGC-1α	201:206	PGC-1α is a master regulator of gluconeogenesis, and its activity is controlled by various posttranslational modifications.
22883232	2	46	theme	master	213:218	arg1	regulator					220:228	a master regulator	211:228	a master regulator of gluconeogenesis	211:247	PGC-1α is a master regulator of gluconeogenesis, and its activity is controlled by various posttranslational modifications.
22883232	7	47	theme	glucose	1057:1063	arg1	homeostasis					1065:1075	glucose homeostasis	1057:1075	glucose homeostasis in diabetic mice	1057:1092	Hepatic knockdown of OGT and HCF-1 improves glucose homeostasis in diabetic mice.
22883232	1	48	theme	diabetic	141:148	arg1	patients					150:157	diabetic patients	141:157	diabetic patients	141:157	A major cause of hyperglycemia in diabetic patients is inappropriate hepatic gluconeogenesis.
22883232	4	49	theme	factor	652:657	arg1	HCF-1					663:667	HCF-1	663:667	HCF-1	663:667	Using a proteomic approach, we identified a broad variety of proteins associated with O-GlcNAc transferase (OGT), among which host cell factor C1 (HCF-1) is highly abundant.
22883232	4	49	theme	factor	652:657	arg1	C1					659:660	host cell factor C1	642:660	host cell factor C1 (HCF-1)	642:668	Using a proteomic approach, we identified a broad variety of proteins associated with O-GlcNAc transferase (OGT), among which host cell factor C1 (HCF-1) is highly abundant.
22883232	3	50	link	O-linked	424:431	arg1	modification					466:477	O-linked β-N-acetylglucosamine (O-GlcNAc) modification	424:477	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of cytoplasmic and nuclear proteins	424:513	A small portion of glucose metabolizes through the hexosamine biosynthetic pathway, which leads to O-linked β-N-acetylglucosamine (O-GlcNAc) modification of cytoplasmic and nuclear proteins.
22883232	7	51	theme	HCF-1	1042:1046	arg1	knockdown					1021:1029	Hepatic knockdown	1013:1029	Hepatic knockdown of OGT and HCF-1	1013:1046	Hepatic knockdown of OGT and HCF-1 improves glucose homeostasis in diabetic mice.
22883232	3	52	mod	modification	466:477	arg1	proteins					506:513	cytoplasmic and nuclear proteins	482:513	cytoplasmic and nuclear proteins	482:513	A small portion of glucose metabolizes through the hexosamine biosynthetic pathway, which leads to O-linked β-N-acetylglucosamine (O-GlcNAc) modification of cytoplasmic and nuclear proteins.
22883232	3	52	mod	modification	466:477	arg3	β-N-acetylglucosamine					433:453	O-linked β-N-acetylglucosamine (O-GlcNAc) modification	424:477	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of cytoplasmic and nuclear proteins	424:513	A small portion of glucose metabolizes through the hexosamine biosynthetic pathway, which leads to O-linked β-N-acetylglucosamine (O-GlcNAc) modification of cytoplasmic and nuclear proteins.
22883232	3	52	mod	modification	466:477	arg3	O-GlcNAc					456:463	O-linked β-N-acetylglucosamine (O-GlcNAc) modification	424:477	O-linked β-N-acetylglucosamine (O-GlcNAc) modification of cytoplasmic and nuclear proteins	424:513	A small portion of glucose metabolizes through the hexosamine biosynthetic pathway, which leads to O-linked β-N-acetylglucosamine (O-GlcNAc) modification of cytoplasmic and nuclear proteins.
22883232	8	53	theme	gluconeogenesis	1180:1194	arg1	complex					1131:1137	the OGT/HCF-1 complex	1117:1137	the OGT/HCF-1 complex	1117:1137	These findings define the OGT/HCF-1 complex as a glucose sensor and key regulator of gluconeogenesis, shedding light on new strategies for treating diabetes.
22883232	8	53	theme	gluconeogenesis	1180:1194	arg1	sensor					1152:1157	a glucose sensor	1142:1157	a glucose sensor	1142:1157	These findings define the OGT/HCF-1 complex as a glucose sensor and key regulator of gluconeogenesis, shedding light on new strategies for treating diabetes.
22883232	8	53	theme	gluconeogenesis	1180:1194	arg1	regulator					1167:1175	key regulator	1163:1175	key regulator	1163:1175	These findings define the OGT/HCF-1 complex as a glucose sensor and key regulator of gluconeogenesis, shedding light on new strategies for treating diabetes.
22883232	4	54	theme	cell	647:650	arg1	HCF-1					663:667	HCF-1	663:667	HCF-1	663:667	Using a proteomic approach, we identified a broad variety of proteins associated with O-GlcNAc transferase (OGT), among which host cell factor C1 (HCF-1) is highly abundant.
22883232	4	54	theme	cell	647:650	arg1	C1					659:660	host cell factor C1	642:660	host cell factor C1 (HCF-1)	642:668	Using a proteomic approach, we identified a broad variety of proteins associated with O-GlcNAc transferase (OGT), among which host cell factor C1 (HCF-1) is highly abundant.
36604567	6	0	from	positioning	948:958	arg1	cells					980:984	hepatoma cells	971:984	hepatoma cells	971:984	However, O-GlcNAcylation of SPOP at Ser96 increases the nuclear positioning of SPOP in hepatoma cells, alleviating the ubiquitination of the Nogo-B protein, thereby promoting HCC progression in vitro and in vivo.
36604567	6	1	theme	Nogo-B	1025:1030	arg1	protein					1032:1038	the Nogo-B protein	1021:1038	the Nogo-B protein	1021:1038	However, O-GlcNAcylation of SPOP at Ser96 increases the nuclear positioning of SPOP in hepatoma cells, alleviating the ubiquitination of the Nogo-B protein, thereby promoting HCC progression in vitro and in vivo.
36604567	4	2	from	O-GlcNAcylated	568:581	arg1	HCC					548:550	HCC	548:550	HCC	548:550	Here, we show that, in HCC, SPOP is highly O-GlcNAcylated by O-GlcNAc transferase (OGT) at Ser96.
36604567	5	3	theme	N-terminal	836:845	arg1	motifs					876:881	its N-terminal SPOP-binding consensus (SBC) motifs	832:881	its N-terminal SPOP-binding consensus (SBC) motifs	832:881	In normal liver cells, the SPOP protein mainly localizes in the cytoplasm and mediates the ubiquitination of the oncoprotein neurite outgrowth inhibitor-B (Nogo-B) (also known as reticulon 4 B) by recognizing its N-terminal SPOP-binding consensus (SBC) motifs.
36604567	8	4	theme	novel	1355:1359	arg1	Nogo-B					1377:1382	Nogo-B	1377:1382	Nogo-B	1377:1382	Our findings reveal a novel post-translational modification of SPOP and identify a novel SPOP substrate, Nogo-B, in HCC.
36604567	8	4	theme	novel	1355:1359	arg1	substrate					1366:1374	a novel SPOP substrate	1353:1374	a novel SPOP substrate	1353:1374	Our findings reveal a novel post-translational modification of SPOP and identify a novel SPOP substrate, Nogo-B, in HCC.
36604567	5	5	dep	inhibitor-B	766:776	arg1	known					793:797	known	793:797	known as reticulon 4 B	793:814	In normal liver cells, the SPOP protein mainly localizes in the cytoplasm and mediates the ubiquitination of the oncoprotein neurite outgrowth inhibitor-B (Nogo-B) (also known as reticulon 4 B) by recognizing its N-terminal SPOP-binding consensus (SBC) motifs.
36604567	8	6	theme	SPOP	1361:1364	arg1	Nogo-B					1377:1382	Nogo-B	1377:1382	Nogo-B	1377:1382	Our findings reveal a novel post-translational modification of SPOP and identify a novel SPOP substrate, Nogo-B, in HCC.
36604567	8	6	theme	SPOP	1361:1364	arg1	substrate					1366:1374	a novel SPOP substrate	1353:1374	a novel SPOP substrate	1353:1374	Our findings reveal a novel post-translational modification of SPOP and identify a novel SPOP substrate, Nogo-B, in HCC.
36604567	2	7	dep	initiation	345:354	arg1	the					341:343	the	341:343	the	341:343	Speckle-type POZ protein (SPOP), an important substrate adaptor of cullin3-RING ubiquitin ligase, plays a key role in the initiation and development of various cancers.
36604567	7	8	theme	O-GlcNAcylation	1122:1136	arg1	ablation					1110:1117	ablation	1110:1117	ablation of O-GlcNAcylation by an S96A mutation	1110:1156	In addition, ablation of O-GlcNAcylation by an S96A mutation increased the cytoplasmic localization of SPOP, thereby inhibiting the Nogo-B/c-FLIP cascade and HCC progression.
36604567	9	9	theme	SPOP	1440:1443	arg1	O-GlcNAcylation					1421:1435	the hyper O-GlcNAcylation	1411:1435	the hyper O-GlcNAcylation of SPOP	1411:1443	Intervention with the hyper O-GlcNAcylation of SPOP may provide a novel strategy for HCC treatment.
36604567	5	10	theme	normal	626:631	arg1	cells					639:643	normal liver cells	626:643	normal liver cells	626:643	In normal liver cells, the SPOP protein mainly localizes in the cytoplasm and mediates the ubiquitination of the oncoprotein neurite outgrowth inhibitor-B (Nogo-B) (also known as reticulon 4 B) by recognizing its N-terminal SPOP-binding consensus (SBC) motifs.
36604567	7	11	theme	SPOP	1200:1203	arg1	localization					1184:1195	the cytoplasmic localization	1168:1195	the cytoplasmic localization of SPOP	1168:1203	In addition, ablation of O-GlcNAcylation by an S96A mutation increased the cytoplasmic localization of SPOP, thereby inhibiting the Nogo-B/c-FLIP cascade and HCC progression.
36604567	9	12	theme	hyper	1415:1419	arg1	O-GlcNAcylation					1421:1435	the hyper O-GlcNAcylation	1411:1435	the hyper O-GlcNAcylation of SPOP	1411:1443	Intervention with the hyper O-GlcNAcylation of SPOP may provide a novel strategy for HCC treatment.
36604567	6	13	from	Ser96	920:924	arg1	O-GlcNAcylation					893:907	O-GlcNAcylation	893:907	O-GlcNAcylation of SPOP at Ser96	893:924	However, O-GlcNAcylation of SPOP at Ser96 increases the nuclear positioning of SPOP in hepatoma cells, alleviating the ubiquitination of the Nogo-B protein, thereby promoting HCC progression in vitro and in vivo.
36604567	1	14	theme	elevated	88:95	arg1	target					215:220	a potential therapeutic target	191:220	a potential therapeutic target	191:220	Aberrantly elevated O-GlcNAcylation level is commonly observed in human cancer patients, and has been proposed as a potential therapeutic target.
36604567	1	14	theme	elevated	88:95	arg1	level					113:117	Aberrantly elevated O-GlcNAcylation level	77:117	Aberrantly elevated O-GlcNAcylation level	77:117	Aberrantly elevated O-GlcNAcylation level is commonly observed in human cancer patients, and has been proposed as a potential therapeutic target.
36604567	5	15	theme	reticulon	802:810	arg1	B					814:814	reticulon 4 B	802:814	reticulon 4 B	802:814	In normal liver cells, the SPOP protein mainly localizes in the cytoplasm and mediates the ubiquitination of the oncoprotein neurite outgrowth inhibitor-B (Nogo-B) (also known as reticulon 4 B) by recognizing its N-terminal SPOP-binding consensus (SBC) motifs.
36604567	5	16	theme	outgrowth	756:764	arg1	ubiquitination					714:727	the ubiquitination	710:727	the ubiquitination of the oncoprotein neurite outgrowth inhibitor-B (Nogo-B) (also known as reticulon 4 B)	710:815	In normal liver cells, the SPOP protein mainly localizes in the cytoplasm and mediates the ubiquitination of the oncoprotein neurite outgrowth inhibitor-B (Nogo-B) (also known as reticulon 4 B) by recognizing its N-terminal SPOP-binding consensus (SBC) motifs.
36604567	5	17	dep	outgrowth	756:764	arg1	Nogo-B					779:784	Nogo-B	779:784	Nogo-B	779:784	In normal liver cells, the SPOP protein mainly localizes in the cytoplasm and mediates the ubiquitination of the oncoprotein neurite outgrowth inhibitor-B (Nogo-B) (also known as reticulon 4 B) by recognizing its N-terminal SPOP-binding consensus (SBC) motifs.
36604567	5	17	dep	outgrowth	756:764	arg1	inhibitor-B					766:776	inhibitor-B	766:776	the oncoprotein neurite outgrowth inhibitor-B (Nogo-B) (also known as reticulon 4 B)	732:815	In normal liver cells, the SPOP protein mainly localizes in the cytoplasm and mediates the ubiquitination of the oncoprotein neurite outgrowth inhibitor-B (Nogo-B) (also known as reticulon 4 B) by recognizing its N-terminal SPOP-binding consensus (SBC) motifs.
36604567	1	18	theme	O-GlcNAcylation	97:111	arg1	target					215:220	a potential therapeutic target	191:220	a potential therapeutic target	191:220	Aberrantly elevated O-GlcNAcylation level is commonly observed in human cancer patients, and has been proposed as a potential therapeutic target.
36604567	1	18	theme	O-GlcNAcylation	97:111	arg1	level					113:117	Aberrantly elevated O-GlcNAcylation level	77:117	Aberrantly elevated O-GlcNAcylation level	77:117	Aberrantly elevated O-GlcNAcylation level is commonly observed in human cancer patients, and has been proposed as a potential therapeutic target.
36604567	2	19	theme	cancers	383:389	arg1	initiation					345:354	initiation	345:354	initiation	345:354	Speckle-type POZ protein (SPOP), an important substrate adaptor of cullin3-RING ubiquitin ligase, plays a key role in the initiation and development of various cancers.
36604567	2	19	theme	cancers	383:389	arg1	development					360:370	development	360:370	development	360:370	Speckle-type POZ protein (SPOP), an important substrate adaptor of cullin3-RING ubiquitin ligase, plays a key role in the initiation and development of various cancers.
36604567	4	20	from	HCC	548:550	arg1	O-GlcNAcylated					568:581	O-GlcNAcylated	568:581	O-GlcNAcylated	568:581	Here, we show that, in HCC, SPOP is highly O-GlcNAcylated by O-GlcNAc transferase (OGT) at Ser96.
36604567	8	21	theme	post-translational	1300:1317	arg1	modification					1319:1330	a novel post-translational modification	1292:1330	a novel post-translational modification of SPOP	1292:1338	Our findings reveal a novel post-translational modification of SPOP and identify a novel SPOP substrate, Nogo-B, in HCC.
36604567	4	22	from	Ser96	616:620	arg1	OGT					608:610	OGT	608:610	OGT	608:610	Here, we show that, in HCC, SPOP is highly O-GlcNAcylated by O-GlcNAc transferase (OGT) at Ser96.
36604567	4	22	from	Ser96	616:620	arg1	transferase					595:605	O-GlcNAc transferase	586:605	O-GlcNAc transferase (OGT) at Ser96	586:620	Here, we show that, in HCC, SPOP is highly O-GlcNAcylated by O-GlcNAc transferase (OGT) at Ser96.
36604567	2	23	theme	various	375:381	arg1	cancers					383:389	various cancers	375:389	various cancers	375:389	Speckle-type POZ protein (SPOP), an important substrate adaptor of cullin3-RING ubiquitin ligase, plays a key role in the initiation and development of various cancers.
36604567	6	24	theme	SPOP	912:915	arg1	O-GlcNAcylation					893:907	O-GlcNAcylation	893:907	O-GlcNAcylation of SPOP at Ser96	893:924	However, O-GlcNAcylation of SPOP at Ser96 increases the nuclear positioning of SPOP in hepatoma cells, alleviating the ubiquitination of the Nogo-B protein, thereby promoting HCC progression in vitro and in vivo.
36604567	8	25	theme	novel	1294:1298	arg1	modification					1319:1330	a novel post-translational modification	1292:1330	a novel post-translational modification of SPOP	1292:1338	Our findings reveal a novel post-translational modification of SPOP and identify a novel SPOP substrate, Nogo-B, in HCC.
36604567	1	26	theme	potential	193:201	arg1	target					215:220	a potential therapeutic target	191:220	a potential therapeutic target	191:220	Aberrantly elevated O-GlcNAcylation level is commonly observed in human cancer patients, and has been proposed as a potential therapeutic target.
36604567	1	26	theme	potential	193:201	arg1	level					113:117	Aberrantly elevated O-GlcNAcylation level	77:117	Aberrantly elevated O-GlcNAcylation level	77:117	Aberrantly elevated O-GlcNAcylation level is commonly observed in human cancer patients, and has been proposed as a potential therapeutic target.
36604567	5	27	theme	SPOP	650:653	arg1	protein					655:661	the SPOP protein	646:661	the SPOP protein	646:661	In normal liver cells, the SPOP protein mainly localizes in the cytoplasm and mediates the ubiquitination of the oncoprotein neurite outgrowth inhibitor-B (Nogo-B) (also known as reticulon 4 B) by recognizing its N-terminal SPOP-binding consensus (SBC) motifs.
36604567	2	28	theme	ligase	313:318	arg1	adaptor					279:285	an important substrate adaptor	256:285	an important substrate adaptor of cullin3-RING ubiquitin ligase	256:318	Speckle-type POZ protein (SPOP), an important substrate adaptor of cullin3-RING ubiquitin ligase, plays a key role in the initiation and development of various cancers.
36604567	2	28	theme	ligase	313:318	arg1	protein					240:246	Speckle-type POZ protein	223:246	Speckle-type POZ protein (SPOP)	223:253	Speckle-type POZ protein (SPOP), an important substrate adaptor of cullin3-RING ubiquitin ligase, plays a key role in the initiation and development of various cancers.
36604567	8	29	from	substrate	1366:1374	arg1	HCC					1388:1390	HCC	1388:1390	HCC	1388:1390	Our findings reveal a novel post-translational modification of SPOP and identify a novel SPOP substrate, Nogo-B, in HCC.
36604567	7	30	theme	Nogo-B/c-FLIP	1229:1241	arg1	cascade					1243:1249	the Nogo-B/c-FLIP cascade	1225:1249	the Nogo-B/c-FLIP cascade	1225:1249	In addition, ablation of O-GlcNAcylation by an S96A mutation increased the cytoplasmic localization of SPOP, thereby inhibiting the Nogo-B/c-FLIP cascade and HCC progression.
36604567	0	31	theme	SPOP	19:22	arg1	O-GlcNAcylation					0:14	O-GlcNAcylation	0:14	O-GlcNAcylation of SPOP	0:22	O-GlcNAcylation of SPOP promotes carcinogenesis in hepatocellular carcinoma.
36604567	9	32	theme	HCC	1478:1480	arg1	treatment					1482:1490	HCC treatment	1478:1490	HCC treatment	1478:1490	Intervention with the hyper O-GlcNAcylation of SPOP may provide a novel strategy for HCC treatment.
36604567	2	33	theme	ubiquitin	303:311	arg1	ligase					313:318	cullin3-RING ubiquitin ligase	290:318	cullin3-RING ubiquitin ligase	290:318	Speckle-type POZ protein (SPOP), an important substrate adaptor of cullin3-RING ubiquitin ligase, plays a key role in the initiation and development of various cancers.
36604567	9	34	theme	novel	1459:1463	arg1	strategy					1465:1472	a novel strategy	1457:1472	a novel strategy for HCC treatment	1457:1490	Intervention with the hyper O-GlcNAcylation of SPOP may provide a novel strategy for HCC treatment.
36604567	3	35	theme	hepatocellular	466:479	arg1	HCC					492:494	HCC	492:494	HCC	492:494	However, the regulatory mechanisms governing SPOP and its function during hepatocellular carcinoma (HCC) progression remain unclear.
36604567	3	35	theme	hepatocellular	466:479	arg1	carcinoma					481:489	hepatocellular carcinoma	466:489	hepatocellular carcinoma (HCC) progression	466:507	However, the regulatory mechanisms governing SPOP and its function during hepatocellular carcinoma (HCC) progression remain unclear.
36604567	5	36	theme	consensus	860:868	arg1	motifs					876:881	its N-terminal SPOP-binding consensus (SBC) motifs	832:881	its N-terminal SPOP-binding consensus (SBC) motifs	832:881	In normal liver cells, the SPOP protein mainly localizes in the cytoplasm and mediates the ubiquitination of the oncoprotein neurite outgrowth inhibitor-B (Nogo-B) (also known as reticulon 4 B) by recognizing its N-terminal SPOP-binding consensus (SBC) motifs.
36604567	6	37	theme	HCC	1059:1061	arg1	progression					1063:1073	HCC progression	1059:1073	HCC progression	1059:1073	However, O-GlcNAcylation of SPOP at Ser96 increases the nuclear positioning of SPOP in hepatoma cells, alleviating the ubiquitination of the Nogo-B protein, thereby promoting HCC progression in vitro and in vivo.
36604567	7	38	theme	HCC	1255:1257	arg1	progression					1259:1269	HCC progression	1255:1269	HCC progression	1255:1269	In addition, ablation of O-GlcNAcylation by an S96A mutation increased the cytoplasmic localization of SPOP, thereby inhibiting the Nogo-B/c-FLIP cascade and HCC progression.
36604567	6	39	theme	hepatoma	971:978	arg1	cells					980:984	hepatoma cells	971:984	hepatoma cells	971:984	However, O-GlcNAcylation of SPOP at Ser96 increases the nuclear positioning of SPOP in hepatoma cells, alleviating the ubiquitination of the Nogo-B protein, thereby promoting HCC progression in vitro and in vivo.
36604567	3	40	theme	regulatory	405:414	arg1	mechanisms					416:425	the regulatory mechanisms	401:425	the regulatory mechanisms governing SPOP and its function during hepatocellular carcinoma (HCC) progression	401:507	However, the regulatory mechanisms governing SPOP and its function during hepatocellular carcinoma (HCC) progression remain unclear.
36604567	5	41	theme	oncoprotein	736:746	arg1	outgrowth					756:764	the oncoprotein neurite outgrowth inhibitor-B (Nogo-B) (also known as reticulon 4 B)	732:815	the oncoprotein neurite outgrowth inhibitor-B (Nogo-B) (also known as reticulon 4 B)	732:815	In normal liver cells, the SPOP protein mainly localizes in the cytoplasm and mediates the ubiquitination of the oncoprotein neurite outgrowth inhibitor-B (Nogo-B) (also known as reticulon 4 B) by recognizing its N-terminal SPOP-binding consensus (SBC) motifs.
36604567	1	42	dep	potential	193:201	arg1	therapeutic					203:213	therapeutic	203:213	therapeutic	203:213	Aberrantly elevated O-GlcNAcylation level is commonly observed in human cancer patients, and has been proposed as a potential therapeutic target.
36604567	5	43	theme	neurite	748:754	arg1	outgrowth					756:764	the oncoprotein neurite outgrowth inhibitor-B (Nogo-B) (also known as reticulon 4 B)	732:815	the oncoprotein neurite outgrowth inhibitor-B (Nogo-B) (also known as reticulon 4 B)	732:815	In normal liver cells, the SPOP protein mainly localizes in the cytoplasm and mediates the ubiquitination of the oncoprotein neurite outgrowth inhibitor-B (Nogo-B) (also known as reticulon 4 B) by recognizing its N-terminal SPOP-binding consensus (SBC) motifs.
36604567	5	44	theme	liver	633:637	arg1	cells					639:643	normal liver cells	626:643	normal liver cells	626:643	In normal liver cells, the SPOP protein mainly localizes in the cytoplasm and mediates the ubiquitination of the oncoprotein neurite outgrowth inhibitor-B (Nogo-B) (also known as reticulon 4 B) by recognizing its N-terminal SPOP-binding consensus (SBC) motifs.
36604567	9	45	with	Intervention	1393:1404	arg1	O-GlcNAcylation					1421:1435	the hyper O-GlcNAcylation	1411:1435	the hyper O-GlcNAcylation of SPOP	1411:1443	Intervention with the hyper O-GlcNAcylation of SPOP may provide a novel strategy for HCC treatment.
36604567	5	46	theme	SPOP-binding	847:858	arg1	motifs					876:881	its N-terminal SPOP-binding consensus (SBC) motifs	832:881	its N-terminal SPOP-binding consensus (SBC) motifs	832:881	In normal liver cells, the SPOP protein mainly localizes in the cytoplasm and mediates the ubiquitination of the oncoprotein neurite outgrowth inhibitor-B (Nogo-B) (also known as reticulon 4 B) by recognizing its N-terminal SPOP-binding consensus (SBC) motifs.
36604567	0	47	theme	hepatocellular	51:64	arg1	carcinoma					66:74	hepatocellular carcinoma	51:74	hepatocellular carcinoma	51:74	O-GlcNAcylation of SPOP promotes carcinogenesis in hepatocellular carcinoma.
36604567	1	48	located	observed	131:138	arg2	target					215:220	a potential therapeutic target	191:220	a potential therapeutic target	191:220	Aberrantly elevated O-GlcNAcylation level is commonly observed in human cancer patients, and has been proposed as a potential therapeutic target.
36604567	1	48	located	observed	131:138	arg1	patients					156:163	human cancer patients	143:163	human cancer patients	143:163	Aberrantly elevated O-GlcNAcylation level is commonly observed in human cancer patients, and has been proposed as a potential therapeutic target.
36604567	1	48	located	observed	131:138	arg2	level					113:117	Aberrantly elevated O-GlcNAcylation level	77:117	Aberrantly elevated O-GlcNAcylation level	77:117	Aberrantly elevated O-GlcNAcylation level is commonly observed in human cancer patients, and has been proposed as a potential therapeutic target.
36604567	3	49	theme	carcinoma	481:489	arg1	progression					497:507	hepatocellular carcinoma (HCC) progression	466:507	hepatocellular carcinoma (HCC) progression	466:507	However, the regulatory mechanisms governing SPOP and its function during hepatocellular carcinoma (HCC) progression remain unclear.
36604567	2	50	theme	Speckle-type	223:234	arg1	SPOP					249:252	SPOP	249:252	SPOP	249:252	Speckle-type POZ protein (SPOP), an important substrate adaptor of cullin3-RING ubiquitin ligase, plays a key role in the initiation and development of various cancers.
36604567	2	50	theme	Speckle-type	223:234	arg1	protein					240:246	Speckle-type POZ protein	223:246	Speckle-type POZ protein (SPOP)	223:253	Speckle-type POZ protein (SPOP), an important substrate adaptor of cullin3-RING ubiquitin ligase, plays a key role in the initiation and development of various cancers.
36604567	2	50	theme	Speckle-type	223:234	arg1	adaptor					279:285	an important substrate adaptor	256:285	an important substrate adaptor of cullin3-RING ubiquitin ligase	256:318	Speckle-type POZ protein (SPOP), an important substrate adaptor of cullin3-RING ubiquitin ligase, plays a key role in the initiation and development of various cancers.
36604567	2	51	theme	POZ	236:238	arg1	SPOP					249:252	SPOP	249:252	SPOP	249:252	Speckle-type POZ protein (SPOP), an important substrate adaptor of cullin3-RING ubiquitin ligase, plays a key role in the initiation and development of various cancers.
36604567	2	51	theme	POZ	236:238	arg1	protein					240:246	Speckle-type POZ protein	223:246	Speckle-type POZ protein (SPOP)	223:253	Speckle-type POZ protein (SPOP), an important substrate adaptor of cullin3-RING ubiquitin ligase, plays a key role in the initiation and development of various cancers.
36604567	2	51	theme	POZ	236:238	arg1	adaptor					279:285	an important substrate adaptor	256:285	an important substrate adaptor of cullin3-RING ubiquitin ligase	256:318	Speckle-type POZ protein (SPOP), an important substrate adaptor of cullin3-RING ubiquitin ligase, plays a key role in the initiation and development of various cancers.
36604567	1	52	theme	human	143:147	arg1	patients					156:163	human cancer patients	143:163	human cancer patients	143:163	Aberrantly elevated O-GlcNAcylation level is commonly observed in human cancer patients, and has been proposed as a potential therapeutic target.
36604567	5	53	dep	known	793:797	arg1	also					788:791	also	788:791	also	788:791	In normal liver cells, the SPOP protein mainly localizes in the cytoplasm and mediates the ubiquitination of the oncoprotein neurite outgrowth inhibitor-B (Nogo-B) (also known as reticulon 4 B) by recognizing its N-terminal SPOP-binding consensus (SBC) motifs.
36604567	2	54	theme	important	259:267	arg1	adaptor					279:285	an important substrate adaptor	256:285	an important substrate adaptor of cullin3-RING ubiquitin ligase	256:318	Speckle-type POZ protein (SPOP), an important substrate adaptor of cullin3-RING ubiquitin ligase, plays a key role in the initiation and development of various cancers.
36604567	2	54	theme	important	259:267	arg1	protein					240:246	Speckle-type POZ protein	223:246	Speckle-type POZ protein (SPOP)	223:253	Speckle-type POZ protein (SPOP), an important substrate adaptor of cullin3-RING ubiquitin ligase, plays a key role in the initiation and development of various cancers.
36604567	8	55	theme	SPOP	1335:1338	arg1	modification					1319:1330	a novel post-translational modification	1292:1330	a novel post-translational modification of SPOP	1292:1338	Our findings reveal a novel post-translational modification of SPOP and identify a novel SPOP substrate, Nogo-B, in HCC.
36604567	1	56	theme	cancer	149:154	arg1	patients					156:163	human cancer patients	143:163	human cancer patients	143:163	Aberrantly elevated O-GlcNAcylation level is commonly observed in human cancer patients, and has been proposed as a potential therapeutic target.
36604567	6	57	theme	SPOP	963:966	arg1	positioning					948:958	the nuclear positioning	936:958	the nuclear positioning of SPOP in hepatoma cells	936:984	However, O-GlcNAcylation of SPOP at Ser96 increases the nuclear positioning of SPOP in hepatoma cells, alleviating the ubiquitination of the Nogo-B protein, thereby promoting HCC progression in vitro and in vivo.
36604567	2	58	theme	substrate	269:277	arg1	adaptor					279:285	an important substrate adaptor	256:285	an important substrate adaptor of cullin3-RING ubiquitin ligase	256:318	Speckle-type POZ protein (SPOP), an important substrate adaptor of cullin3-RING ubiquitin ligase, plays a key role in the initiation and development of various cancers.
36604567	2	58	theme	substrate	269:277	arg1	protein					240:246	Speckle-type POZ protein	223:246	Speckle-type POZ protein (SPOP)	223:253	Speckle-type POZ protein (SPOP), an important substrate adaptor of cullin3-RING ubiquitin ligase, plays a key role in the initiation and development of various cancers.
36604567	2	59	theme	cullin3-RING	290:301	arg1	ligase					313:318	cullin3-RING ubiquitin ligase	290:318	cullin3-RING ubiquitin ligase	290:318	Speckle-type POZ protein (SPOP), an important substrate adaptor of cullin3-RING ubiquitin ligase, plays a key role in the initiation and development of various cancers.
36604567	5	60	theme	SBC	871:873	arg1	motifs					876:881	its N-terminal SPOP-binding consensus (SBC) motifs	832:881	its N-terminal SPOP-binding consensus (SBC) motifs	832:881	In normal liver cells, the SPOP protein mainly localizes in the cytoplasm and mediates the ubiquitination of the oncoprotein neurite outgrowth inhibitor-B (Nogo-B) (also known as reticulon 4 B) by recognizing its N-terminal SPOP-binding consensus (SBC) motifs.
36604567	2	61	theme	key	329:331	arg1	role					333:336	a key role	327:336	a key role	327:336	Speckle-type POZ protein (SPOP), an important substrate adaptor of cullin3-RING ubiquitin ligase, plays a key role in the initiation and development of various cancers.
36604567	7	62	theme	S96A	1144:1147	arg1	mutation					1149:1156	an S96A mutation	1141:1156	an S96A mutation	1141:1156	In addition, ablation of O-GlcNAcylation by an S96A mutation increased the cytoplasmic localization of SPOP, thereby inhibiting the Nogo-B/c-FLIP cascade and HCC progression.
36604567	7	63	theme	cytoplasmic	1172:1182	arg1	localization					1184:1195	the cytoplasmic localization	1168:1195	the cytoplasmic localization of SPOP	1168:1203	In addition, ablation of O-GlcNAcylation by an S96A mutation increased the cytoplasmic localization of SPOP, thereby inhibiting the Nogo-B/c-FLIP cascade and HCC progression.
36604567	6	64	theme	nuclear	940:946	arg1	positioning					948:958	the nuclear positioning	936:958	the nuclear positioning of SPOP in hepatoma cells	936:984	However, O-GlcNAcylation of SPOP at Ser96 increases the nuclear positioning of SPOP in hepatoma cells, alleviating the ubiquitination of the Nogo-B protein, thereby promoting HCC progression in vitro and in vivo.
36604567	6	65	theme	protein	1032:1038	arg1	ubiquitination					1003:1016	the ubiquitination	999:1016	the ubiquitination of the Nogo-B protein	999:1038	However, O-GlcNAcylation of SPOP at Ser96 increases the nuclear positioning of SPOP in hepatoma cells, alleviating the ubiquitination of the Nogo-B protein, thereby promoting HCC progression in vitro and in vivo.
36604567	4	66	theme	O-GlcNAc	586:593	arg1	OGT					608:610	OGT	608:610	OGT	608:610	Here, we show that, in HCC, SPOP is highly O-GlcNAcylated by O-GlcNAc transferase (OGT) at Ser96.
36604567	4	66	theme	O-GlcNAc	586:593	arg1	transferase					595:605	O-GlcNAc transferase	586:605	O-GlcNAc transferase (OGT) at Ser96	586:620	Here, we show that, in HCC, SPOP is highly O-GlcNAcylated by O-GlcNAc transferase (OGT) at Ser96.
32357142	9	0	theme	apoptosis	1287:1295	arg1	inhibition					1297:1306	apoptosis inhibition	1287:1306	apoptosis inhibition	1287:1306	ACSL4 could be O-GlcNAcylated, and silencing of ACSL4 abolished the effects of O-GlcNAcylation on cell growth promotion and apoptosis inhibition.
32357142	5	1	dep	cell	702:705	arg1	proliferation					707:719	proliferation	707:719	proliferation	707:719	CCK-8, flow cytometry and in vivo tumour formation assays were performed to detect cell proliferation, apoptosis and tumorigenesis.
32357142	5	1	dep	cell	702:705	arg1	tumorigenesis					736:748	tumorigenesis	736:748	tumorigenesis	736:748	CCK-8, flow cytometry and in vivo tumour formation assays were performed to detect cell proliferation, apoptosis and tumorigenesis.
32357142	5	1	dep	cell	702:705	arg1	apoptosis					722:730	apoptosis	722:730	apoptosis	722:730	CCK-8, flow cytometry and in vivo tumour formation assays were performed to detect cell proliferation, apoptosis and tumorigenesis.
32357142	2	2	theme	HCC	334:336	arg1	progression					338:348	HCC progression	334:348	HCC progression	334:348	However, the molecular mechanisms underlying the role of ACSL4 in HCC progression remain largely unclear.
32357142	8	3	theme	mTOR	1105:1108	arg1	signalling					1110:1119	mTOR signalling	1105:1119	mTOR signalling	1105:1119	ACSL4 overexpression significantly promoted cell proliferation and tumorigenesis and inhibited cell apoptosis, whereas these effects were all obviously impaired when mTOR signalling was repressed or GLUT1 was downregulated.
32357142	4	4	theme	clinical	491:498	arg1	significance					500:511	The clinical significance	487:511	The clinical significance of ACSL4, O-GlcNAc and GLUT1 in HCC	487:547	The clinical significance of ACSL4, O-GlcNAc and GLUT1 in HCC was determined by Pearson chi-squared test and Kaplan-Meier analysis.
32357142	5	5	theme	flow	626:629	arg1	cytometry					631:639	flow cytometry	626:639	flow cytometry	626:639	CCK-8, flow cytometry and in vivo tumour formation assays were performed to detect cell proliferation, apoptosis and tumorigenesis.
32357142	2	6	from	role	317:320	arg1	progression					338:348	HCC progression	334:348	HCC progression	334:348	However, the molecular mechanisms underlying the role of ACSL4 in HCC progression remain largely unclear.
32357142	8	7	theme	cell	983:986	arg1	proliferation					988:1000	cell proliferation	983:1000	cell proliferation	983:1000	ACSL4 overexpression significantly promoted cell proliferation and tumorigenesis and inhibited cell apoptosis, whereas these effects were all obviously impaired when mTOR signalling was repressed or GLUT1 was downregulated.
32357142	5	8	theme	cytometry	631:639	arg1	assays					670:675	CCK-8, flow cytometry and in vivo tumour formation assays	619:675	CCK-8, flow cytometry and in vivo tumour formation assays	619:675	CCK-8, flow cytometry and in vivo tumour formation assays were performed to detect cell proliferation, apoptosis and tumorigenesis.
32357142	8	9	theme	ACSL4	939:943	arg1	overexpression					945:958	ACSL4 overexpression	939:958	ACSL4 overexpression	939:958	ACSL4 overexpression significantly promoted cell proliferation and tumorigenesis and inhibited cell apoptosis, whereas these effects were all obviously impaired when mTOR signalling was repressed or GLUT1 was downregulated.
32357142	7	10	theme	O-GlcNAc	848:855	arg1	levels					857:862	ACSL4, GLUT1 and O-GlcNAc levels	831:862	ACSL4, GLUT1 and O-GlcNAc levels	831:862	ACSL4, GLUT1 and O-GlcNAc levels were elevated in HCC tissues and predicted poor prognosis in HCC patients.
32357142	8	11	theme	cell	1034:1037	arg1	apoptosis					1039:1047	cell apoptosis	1034:1047	cell apoptosis	1034:1047	ACSL4 overexpression significantly promoted cell proliferation and tumorigenesis and inhibited cell apoptosis, whereas these effects were all obviously impaired when mTOR signalling was repressed or GLUT1 was downregulated.
32357142	1	12	theme	cell	248:251	arg1	proliferation					253:265	cell proliferation	248:265	cell proliferation	248:265	Acyl-CoA ligase 4 (ACSL4) has been reported to be overexpressed in hepatocellular carcinoma (HCC) and to enhance cell proliferation.
32357142	0	13	theme	hepatocellular	109:122	arg1	carcinoma					124:132	hepatocellular carcinoma	109:132	hepatocellular carcinoma	109:132	The positive feedback between ACSL4 expression and O-GlcNAcylation contributes to the growth and survival of hepatocellular carcinoma.
32357142	7	14	theme	HCC	925:927	arg1	patients					929:936	HCC patients	925:936	HCC patients	925:936	ACSL4, GLUT1 and O-GlcNAc levels were elevated in HCC tissues and predicted poor prognosis in HCC patients.
32357142	7	15	theme	GLUT1	838:842	arg1	levels					857:862	ACSL4, GLUT1 and O-GlcNAc levels	831:862	ACSL4, GLUT1 and O-GlcNAc levels	831:862	ACSL4, GLUT1 and O-GlcNAc levels were elevated in HCC tissues and predicted poor prognosis in HCC patients.
32357142	9	16	from	effects	1231:1237	arg1	inhibition					1297:1306	apoptosis inhibition	1287:1306	apoptosis inhibition	1287:1306	ACSL4 could be O-GlcNAcylated, and silencing of ACSL4 abolished the effects of O-GlcNAcylation on cell growth promotion and apoptosis inhibition.
32357142	9	16	from	effects	1231:1237	arg1	promotion					1273:1281	cell growth promotion	1261:1281	cell growth promotion	1261:1281	ACSL4 could be O-GlcNAcylated, and silencing of ACSL4 abolished the effects of O-GlcNAcylation on cell growth promotion and apoptosis inhibition.
32357142	7	17	theme	poor	907:910	arg1	prognosis					912:920	predicted poor prognosis	897:920	predicted poor prognosis in HCC patients	897:936	ACSL4, GLUT1 and O-GlcNAc levels were elevated in HCC tissues and predicted poor prognosis in HCC patients.
32357142	5	18	dep	in	645:646	arg1	vivo					648:651	vivo	648:651	vivo	648:651	CCK-8, flow cytometry and in vivo tumour formation assays were performed to detect cell proliferation, apoptosis and tumorigenesis.
32357142	0	19	theme	positive	4:11	arg1	feedback					13:20	The positive feedback	0:20	The positive feedback between ACSL4 expression and O-GlcNAcylation	0:65	The positive feedback between ACSL4 expression and O-GlcNAcylation contributes to the growth and survival of hepatocellular carcinoma.
32357142	7	20	theme	predicted	897:905	arg1	prognosis					912:920	predicted poor prognosis	897:920	predicted poor prognosis in HCC patients	897:936	ACSL4, GLUT1 and O-GlcNAc levels were elevated in HCC tissues and predicted poor prognosis in HCC patients.
32357142	7	21	theme	ACSL4	831:835	arg1	levels					857:862	ACSL4, GLUT1 and O-GlcNAc levels	831:862	ACSL4, GLUT1 and O-GlcNAc levels	831:862	ACSL4, GLUT1 and O-GlcNAc levels were elevated in HCC tissues and predicted poor prognosis in HCC patients.
32357142	5	22	theme	CCK-8	619:623	arg1	assays					670:675	CCK-8, flow cytometry and in vivo tumour formation assays	619:675	CCK-8, flow cytometry and in vivo tumour formation assays	619:675	CCK-8, flow cytometry and in vivo tumour formation assays were performed to detect cell proliferation, apoptosis and tumorigenesis.
32357142	9	23	theme	ACSL4	1211:1215	arg1	silencing					1198:1206	silencing	1198:1206	silencing of ACSL4	1198:1215	ACSL4 could be O-GlcNAcylated, and silencing of ACSL4 abolished the effects of O-GlcNAcylation on cell growth promotion and apoptosis inhibition.
32357142	8	24	dep	promoted	974:981	arg1	whereas					1050:1056	whereas	1050:1056	whereas	1050:1056	ACSL4 overexpression significantly promoted cell proliferation and tumorigenesis and inhibited cell apoptosis, whereas these effects were all obviously impaired when mTOR signalling was repressed or GLUT1 was downregulated.
32357142	6	25	used	used	769:772	arg2	technology					754:763	IP technology	751:763	IP technology	751:763	IP technology was used to evaluate the relationship between ACSL4 and O-GlcNAc.
32357142	4	26	theme	O-GlcNAc	523:530	arg1	significance					500:511	The clinical significance	487:511	The clinical significance of ACSL4, O-GlcNAc and GLUT1 in HCC	487:547	The clinical significance of ACSL4, O-GlcNAc and GLUT1 in HCC was determined by Pearson chi-squared test and Kaplan-Meier analysis.
32357142	6	27	theme	IP	751:752	arg1	technology					754:763	IP technology	751:763	IP technology	751:763	IP technology was used to evaluate the relationship between ACSL4 and O-GlcNAc.
32357142	2	28	theme	molecular	281:289	arg1	mechanisms					291:300	the molecular mechanisms	277:300	the molecular mechanisms underlying the role of ACSL4 in HCC progression	277:348	However, the molecular mechanisms underlying the role of ACSL4 in HCC progression remain largely unclear.
32357142	11	29	theme	ACSL4	1518:1522	arg1	expression					1524:1533	ACSL4 expression	1518:1533	ACSL4 expression	1518:1533	In turn, O-GlcNAcylation promotes HCC growth partially by increasing ACSL4 expression.
32357142	0	30	theme	carcinoma	124:132	arg1	survival					97:104	survival	97:104	survival	97:104	The positive feedback between ACSL4 expression and O-GlcNAcylation contributes to the growth and survival of hepatocellular carcinoma.
32357142	0	30	theme	carcinoma	124:132	arg1	growth					86:91	growth	86:91	growth	86:91	The positive feedback between ACSL4 expression and O-GlcNAcylation contributes to the growth and survival of hepatocellular carcinoma.
32357142	7	31	from	tissues	885:891	arg1	patients					929:936	HCC patients	925:936	HCC patients	925:936	ACSL4, GLUT1 and O-GlcNAc levels were elevated in HCC tissues and predicted poor prognosis in HCC patients.
32357142	4	32	theme	Kaplan-Meier	596:607	arg1	analysis					609:616	Kaplan-Meier analysis	596:616	Kaplan-Meier analysis	596:616	The clinical significance of ACSL4, O-GlcNAc and GLUT1 in HCC was determined by Pearson chi-squared test and Kaplan-Meier analysis.
32357142	4	33	theme	GLUT1	536:540	arg1	significance					500:511	The clinical significance	487:511	The clinical significance of ACSL4, O-GlcNAc and GLUT1 in HCC	487:547	The clinical significance of ACSL4, O-GlcNAc and GLUT1 in HCC was determined by Pearson chi-squared test and Kaplan-Meier analysis.
32357142	3	34	dep	investigate	392:402	arg1	whether					404:410	whether	404:410	whether	404:410	Here, we aimed to investigate whether and how O-GlcNAcylation and ACSL4 regulate each other and HCC progression.
32357142	11	35	theme	HCC	1483:1485	arg1	growth					1487:1492	HCC growth	1483:1492	HCC growth	1483:1492	In turn, O-GlcNAcylation promotes HCC growth partially by increasing ACSL4 expression.
32357142	0	36	theme	ACSL4	30:34	arg1	expression					36:45	ACSL4 expression	30:45	ACSL4 expression	30:45	The positive feedback between ACSL4 expression and O-GlcNAcylation contributes to the growth and survival of hepatocellular carcinoma.
32357142	3	37	dep	whether	404:410	arg1	regulate					446:453	regulate	446:453	regulate each other and HCC progression	446:484	Here, we aimed to investigate whether and how O-GlcNAcylation and ACSL4 regulate each other and HCC progression.
32357142	1	38	theme	hepatocellular	202:215	arg1	HCC					228:230	HCC	228:230	HCC	228:230	Acyl-CoA ligase 4 (ACSL4) has been reported to be overexpressed in hepatocellular carcinoma (HCC) and to enhance cell proliferation.
32357142	1	38	theme	hepatocellular	202:215	arg1	carcinoma					217:225	hepatocellular carcinoma	202:225	hepatocellular carcinoma (HCC)	202:231	Acyl-CoA ligase 4 (ACSL4) has been reported to be overexpressed in hepatocellular carcinoma (HCC) and to enhance cell proliferation.
32357142	5	39	theme	in	645:646	arg1	formation					660:668	in vivo tumour formation	645:668	in vivo tumour formation	645:668	CCK-8, flow cytometry and in vivo tumour formation assays were performed to detect cell proliferation, apoptosis and tumorigenesis.
32357142	9	40	theme	O-GlcNAcylation	1242:1256	arg1	effects					1231:1237	the effects	1227:1237	the effects of O-GlcNAcylation on cell growth promotion and apoptosis inhibition	1227:1306	ACSL4 could be O-GlcNAcylated, and silencing of ACSL4 abolished the effects of O-GlcNAcylation on cell growth promotion and apoptosis inhibition.
32357142	2	41	theme	ACSL4	325:329	arg1	role					317:320	the role	313:320	the role of ACSL4 in HCC progression	313:348	However, the molecular mechanisms underlying the role of ACSL4 in HCC progression remain largely unclear.
32357142	4	42	from	significance	500:511	arg1	HCC					545:547	HCC	545:547	HCC	545:547	The clinical significance of ACSL4, O-GlcNAc and GLUT1 in HCC was determined by Pearson chi-squared test and Kaplan-Meier analysis.
32357142	10	43	theme	GLUT1-mediated	1417:1430	arg1	O-GlcNAcylation					1432:1446	GLUT1-mediated O-GlcNAcylation	1417:1446	GLUT1-mediated O-GlcNAcylation	1417:1446	Collectively, this study demonstrates that ACSL4 contributes to the growth and survival of HCC by enhancing GLUT1-mediated O-GlcNAcylation.
32357142	3	44	theme	HCC	470:472	arg1	progression					474:484	HCC progression	470:484	HCC progression	470:484	Here, we aimed to investigate whether and how O-GlcNAcylation and ACSL4 regulate each other and HCC progression.
32357142	7	45	theme	HCC	881:883	arg1	tissues					885:891	HCC tissues	881:891	HCC tissues	881:891	ACSL4, GLUT1 and O-GlcNAc levels were elevated in HCC tissues and predicted poor prognosis in HCC patients.
32357142	4	46	theme	ACSL4	516:520	arg1	significance					500:511	The clinical significance	487:511	The clinical significance of ACSL4, O-GlcNAc and GLUT1 in HCC	487:547	The clinical significance of ACSL4, O-GlcNAc and GLUT1 in HCC was determined by Pearson chi-squared test and Kaplan-Meier analysis.
32357142	5	47	theme	tumour	653:658	arg1	formation					660:668	in vivo tumour formation	645:668	in vivo tumour formation	645:668	CCK-8, flow cytometry and in vivo tumour formation assays were performed to detect cell proliferation, apoptosis and tumorigenesis.
32357142	9	48	theme	cell	1261:1264	arg1	promotion					1273:1281	cell growth promotion	1261:1281	cell growth promotion	1261:1281	ACSL4 could be O-GlcNAcylated, and silencing of ACSL4 abolished the effects of O-GlcNAcylation on cell growth promotion and apoptosis inhibition.
32357142	10	49	theme	HCC	1400:1402	arg1	survival					1388:1395	survival	1388:1395	survival	1388:1395	Collectively, this study demonstrates that ACSL4 contributes to the growth and survival of HCC by enhancing GLUT1-mediated O-GlcNAcylation.
32357142	10	49	theme	HCC	1400:1402	arg1	growth					1377:1382	growth	1377:1382	growth	1377:1382	Collectively, this study demonstrates that ACSL4 contributes to the growth and survival of HCC by enhancing GLUT1-mediated O-GlcNAcylation.
32357142	1	50	theme	Acyl-CoA	135:142	arg1	ligase					144:149	Acyl-CoA ligase 4	135:151	Acyl-CoA ligase 4 (ACSL4)	135:159	Acyl-CoA ligase 4 (ACSL4) has been reported to be overexpressed in hepatocellular carcinoma (HCC) and to enhance cell proliferation.
32357142	1	50	theme	Acyl-CoA	135:142	arg1	ACSL4					154:158	ACSL4	154:158	ACSL4	154:158	Acyl-CoA ligase 4 (ACSL4) has been reported to be overexpressed in hepatocellular carcinoma (HCC) and to enhance cell proliferation.
32357142	4	51	theme	chi-squared	575:585	arg1	test					587:590	Pearson chi-squared test	567:590	Pearson chi-squared test	567:590	The clinical significance of ACSL4, O-GlcNAc and GLUT1 in HCC was determined by Pearson chi-squared test and Kaplan-Meier analysis.
32357142	5	52	theme	formation	660:668	arg1	assays					670:675	CCK-8, flow cytometry and in vivo tumour formation assays	619:675	CCK-8, flow cytometry and in vivo tumour formation assays	619:675	CCK-8, flow cytometry and in vivo tumour formation assays were performed to detect cell proliferation, apoptosis and tumorigenesis.
32357142	9	53	theme	growth	1266:1271	arg1	promotion					1273:1281	cell growth promotion	1261:1281	cell growth promotion	1261:1281	ACSL4 could be O-GlcNAcylated, and silencing of ACSL4 abolished the effects of O-GlcNAcylation on cell growth promotion and apoptosis inhibition.
32357142	7	54	from	prognosis	912:920	arg1	patients					929:936	HCC patients	925:936	HCC patients	925:936	ACSL4, GLUT1 and O-GlcNAc levels were elevated in HCC tissues and predicted poor prognosis in HCC patients.
32357142	4	55	theme	Pearson	567:573	arg1	test					587:590	Pearson chi-squared test	567:590	Pearson chi-squared test	567:590	The clinical significance of ACSL4, O-GlcNAc and GLUT1 in HCC was determined by Pearson chi-squared test and Kaplan-Meier analysis.
34065225	6	0	theme	ions	894:897	arg1	presence					851:858	presence	851:858	presence	851:858	Following automated glycopeptide assignment (Byonic) and evaluation of the presence and relative intensity of oxonium ions, we observed that, in particular, the ratio of the ions at m/z 144.066 and 138.055, respectively, could be used to discriminate between O-GlcNAcylated and O-GalNAcylated peptides, with concomitant relative quantification between the different cell lines.
34065225	6	0	theme	ions	894:897	arg1	intensity					873:881	relative intensity	864:881	relative intensity	864:881	Following automated glycopeptide assignment (Byonic) and evaluation of the presence and relative intensity of oxonium ions, we observed that, in particular, the ratio of the ions at m/z 144.066 and 138.055, respectively, could be used to discriminate between O-GlcNAcylated and O-GalNAcylated peptides, with concomitant relative quantification between the different cell lines.
34065225	6	1	theme	glycopeptide	796:807	arg1	Byonic					821:826	Byonic	821:826	Byonic	821:826	Following automated glycopeptide assignment (Byonic) and evaluation of the presence and relative intensity of oxonium ions, we observed that, in particular, the ratio of the ions at m/z 144.066 and 138.055, respectively, could be used to discriminate between O-GlcNAcylated and O-GalNAcylated peptides, with concomitant relative quantification between the different cell lines.
34065225	6	1	theme	glycopeptide	796:807	arg1	assignment					809:818	automated glycopeptide assignment	786:818	automated glycopeptide assignment (Byonic)	786:827	Following automated glycopeptide assignment (Byonic) and evaluation of the presence and relative intensity of oxonium ions, we observed that, in particular, the ratio of the ions at m/z 144.066 and 138.055, respectively, could be used to discriminate between O-GlcNAcylated and O-GalNAcylated peptides, with concomitant relative quantification between the different cell lines.
34065225	2	2	theme	glycopeptide	338:349	arg1	spectra					365:371	glycopeptide fragmentation spectra	338:371	glycopeptide fragmentation spectra	338:371	Recently, the characteristic pattern of oxonium ions in glycopeptide fragmentation spectra had been used to assign different sets of glycopeptides.
34065225	9	3	theme	use	1591:1593	arg1	application					1572:1582	broad application	1566:1582	broad application of the use of the relative intensities of oxonium ions	1566:1637	Overall, our study shows the potential of broad application of the use of the relative intensities of oxonium ions for the confident assignment of glycopeptides, even in complex proteomics datasets.
34065225	1	4	theme	related	262:268	arg1	glycosylation					248:260	glycosylation	248:260	glycosylation related to disease	248:279	Developments in mass spectrometry (MS)-based analyses of glycoproteins have been important to study changes in glycosylation related to disease.
34065225	5	5	used	used	636:639	arg2	we					633:634	we	633:634	we	633:634	For this purpose, we used tandem mass tag (TMT)-labeled samples from total cell lysates and secreted proteins from three different colorectal cancer cell lines.
34065225	6	6	theme	relative	864:871	arg1	intensity					873:881	relative intensity	864:881	relative intensity	864:881	Following automated glycopeptide assignment (Byonic) and evaluation of the presence and relative intensity of oxonium ions, we observed that, in particular, the ratio of the ions at m/z 144.066 and 138.055, respectively, could be used to discriminate between O-GlcNAcylated and O-GalNAcylated peptides, with concomitant relative quantification between the different cell lines.
34065225	6	7	theme	different	1132:1140	arg1	lines					1147:1151	the different cell lines	1128:1151	the different cell lines	1128:1151	Following automated glycopeptide assignment (Byonic) and evaluation of the presence and relative intensity of oxonium ions, we observed that, in particular, the ratio of the ions at m/z 144.066 and 138.055, respectively, could be used to discriminate between O-GlcNAcylated and O-GalNAcylated peptides, with concomitant relative quantification between the different cell lines.
34065225	6	8	theme	presence	851:858	arg1	Byonic					821:826	Byonic	821:826	Byonic	821:826	Following automated glycopeptide assignment (Byonic) and evaluation of the presence and relative intensity of oxonium ions, we observed that, in particular, the ratio of the ions at m/z 144.066 and 138.055, respectively, could be used to discriminate between O-GlcNAcylated and O-GalNAcylated peptides, with concomitant relative quantification between the different cell lines.
34065225	6	8	theme	presence	851:858	arg1	evaluation					833:842	evaluation	833:842	evaluation of the presence and relative intensity of oxonium ions	833:897	Following automated glycopeptide assignment (Byonic) and evaluation of the presence and relative intensity of oxonium ions, we observed that, in particular, the ratio of the ions at m/z 144.066 and 138.055, respectively, could be used to discriminate between O-GlcNAcylated and O-GalNAcylated peptides, with concomitant relative quantification between the different cell lines.
34065225	6	8	theme	presence	851:858	arg1	assignment					809:818	automated glycopeptide assignment	786:818	automated glycopeptide assignment (Byonic)	786:827	Following automated glycopeptide assignment (Byonic) and evaluation of the presence and relative intensity of oxonium ions, we observed that, in particular, the ratio of the ions at m/z 144.066 and 138.055, respectively, could be used to discriminate between O-GlcNAcylated and O-GalNAcylated peptides, with concomitant relative quantification between the different cell lines.
34065225	9	9	theme	intensities	1611:1621	arg1	use					1591:1593	the use	1587:1593	the use of the relative intensities of oxonium ions	1587:1637	Overall, our study shows the potential of broad application of the use of the relative intensities of oxonium ions for the confident assignment of glycopeptides, even in complex proteomics datasets.
34065225	1	10	gly	glycoproteins	194:206	arg1	glycoproteins					194:206	glycoproteins	194:206	glycoproteins	194:206	Developments in mass spectrometry (MS)-based analyses of glycoproteins have been important to study changes in glycosylation related to disease.
34065225	2	11	theme	characteristic	296:309	arg1	pattern					311:317	the characteristic pattern	292:317	the characteristic pattern of oxonium ions in glycopeptide fragmentation spectra	292:371	Recently, the characteristic pattern of oxonium ions in glycopeptide fragmentation spectra had been used to assign different sets of glycopeptides.
34065225	1	12	theme	-based	175:180	arg1	analyses					182:189	mass spectrometry (MS)-based analyses	153:189	mass spectrometry (MS)-based analyses of glycoproteins	153:206	Developments in mass spectrometry (MS)-based analyses of glycoproteins have been important to study changes in glycosylation related to disease.
34065225	9	13	theme	oxonium	1626:1632	arg1	ions					1634:1637	oxonium ions	1626:1637	oxonium ions	1626:1637	Overall, our study shows the potential of broad application of the use of the relative intensities of oxonium ions for the confident assignment of glycopeptides, even in complex proteomics datasets.
34065225	6	14	theme	relative	1096:1103	arg1	quantification					1105:1118	concomitant relative quantification	1084:1118	concomitant relative quantification between the different cell lines	1084:1151	Following automated glycopeptide assignment (Byonic) and evaluation of the presence and relative intensity of oxonium ions, we observed that, in particular, the ratio of the ions at m/z 144.066 and 138.055, respectively, could be used to discriminate between O-GlcNAcylated and O-GalNAcylated peptides, with concomitant relative quantification between the different cell lines.
34065225	9	15	gly	glycopeptides	1671:1683	arg2	glycopeptides					1671:1683	glycopeptides	1671:1683	glycopeptides	1671:1683	Overall, our study shows the potential of broad application of the use of the relative intensities of oxonium ions for the confident assignment of glycopeptides, even in complex proteomics datasets.
34065225	5	16	theme	total	684:688	arg1	lysates					695:701	total cell lysates	684:701	total cell lysates	684:701	For this purpose, we used tandem mass tag (TMT)-labeled samples from total cell lysates and secreted proteins from three different colorectal cancer cell lines.
34065225	6	17	gly	glycopeptide	796:807	arg2	glycopeptide					796:807	automated glycopeptide assignment	786:818	automated glycopeptide assignment (Byonic)	786:827	Following automated glycopeptide assignment (Byonic) and evaluation of the presence and relative intensity of oxonium ions, we observed that, in particular, the ratio of the ions at m/z 144.066 and 138.055, respectively, could be used to discriminate between O-GlcNAcylated and O-GalNAcylated peptides, with concomitant relative quantification between the different cell lines.
34065225	9	18	theme	confident	1647:1655	arg1	assignment					1657:1666	the confident assignment	1643:1666	the confident assignment of glycopeptides	1643:1683	Overall, our study shows the potential of broad application of the use of the relative intensities of oxonium ions for the confident assignment of glycopeptides, even in complex proteomics datasets.
34065225	4	19	used	used	569:572	arg2	information					550:560	such information	545:560	such information	545:560	Here, we thought to investigate how such information can be used to examine quantitative proteomics data.
34065225	5	20	from	proteins	716:723	arg1	samples					671:677	tandem mass tag (TMT)-labeled samples	641:677	tandem mass tag (TMT)-labeled samples from total cell lysates and secreted proteins from three different colorectal cancer cell lines	641:773	For this purpose, we used tandem mass tag (TMT)-labeled samples from total cell lysates and secreted proteins from three different colorectal cancer cell lines.
34065225	8	21	theme	modification	1415:1426	arg1	modification					1415:1426	modification	1415:1426	modification	1415:1426	Using a combination of multiple fragmentation methods, we then not only assigned the site of modification, but also showed different glycosylation between intracellular (ER-resident) and secreted AGR2.
34065225	8	21	theme	modification	1415:1426	arg1	site					1407:1410	the site	1403:1410	the site of modification	1403:1426	Using a combination of multiple fragmentation methods, we then not only assigned the site of modification, but also showed different glycosylation between intracellular (ER-resident) and secreted AGR2.
34065225	2	22	used	used	382:385	arg2	pattern					311:317	the characteristic pattern	292:317	the characteristic pattern of oxonium ions in glycopeptide fragmentation spectra	292:371	Recently, the characteristic pattern of oxonium ions in glycopeptide fragmentation spectra had been used to assign different sets of glycopeptides.
34065225	6	23	from	m/z	958:960	arg1	ratio					937:941	the ratio	933:941	the ratio of the ions at m/z 144.066 and 138.055	933:980	Following automated glycopeptide assignment (Byonic) and evaluation of the presence and relative intensity of oxonium ions, we observed that, in particular, the ratio of the ions at m/z 144.066 and 138.055, respectively, could be used to discriminate between O-GlcNAcylated and O-GalNAcylated peptides, with concomitant relative quantification between the different cell lines.
34065225	5	24	theme	different	736:744	arg1	lines					769:773	three different colorectal cancer cell lines	730:773	three different colorectal cancer cell lines	730:773	For this purpose, we used tandem mass tag (TMT)-labeled samples from total cell lysates and secreted proteins from three different colorectal cancer cell lines.
34065225	1	25	theme	spectrometry	158:169	arg1	analyses					182:189	mass spectrometry (MS)-based analyses	153:189	mass spectrometry (MS)-based analyses of glycoproteins	153:206	Developments in mass spectrometry (MS)-based analyses of glycoproteins have been important to study changes in glycosylation related to disease.
34065225	2	26	from	pattern	311:317	arg1	spectra					365:371	glycopeptide fragmentation spectra	338:371	glycopeptide fragmentation spectra	338:371	Recently, the characteristic pattern of oxonium ions in glycopeptide fragmentation spectra had been used to assign different sets of glycopeptides.
34065225	9	27	theme	proteomics	1702:1711	arg1	datasets					1713:1720	complex proteomics datasets	1694:1720	complex proteomics datasets	1694:1720	Overall, our study shows the potential of broad application of the use of the relative intensities of oxonium ions for the confident assignment of glycopeptides, even in complex proteomics datasets.
34065225	0	28	theme	Anterior	101:108	arg1	Protein					119:125	Anterior Gradient Protein 2	101:127	Anterior Gradient Protein 2 (AGR2)	101:134	Oxonium Ion Guided Analysis of Quantitative Proteomics Data Reveals Site-Specific O-Glycosylation of Anterior Gradient Protein 2 (AGR2).
34065225	0	28	theme	Anterior	101:108	arg1	AGR2					130:133	AGR2	130:133	AGR2	130:133	Oxonium Ion Guided Analysis of Quantitative Proteomics Data Reveals Site-Specific O-Glycosylation of Anterior Gradient Protein 2 (AGR2).
34065225	1	29	from	Developments	137:148	arg1	analyses					182:189	mass spectrometry (MS)-based analyses	153:189	mass spectrometry (MS)-based analyses of glycoproteins	153:206	Developments in mass spectrometry (MS)-based analyses of glycoproteins have been important to study changes in glycosylation related to disease.
34065225	5	30	theme	secreted	707:714	arg1	proteins					716:723	secreted proteins	707:723	secreted proteins	707:723	For this purpose, we used tandem mass tag (TMT)-labeled samples from total cell lysates and secreted proteins from three different colorectal cancer cell lines.
34065225	0	31	theme	Quantitative	31:42	arg1	Data					55:58	Quantitative Proteomics Data	31:58	Quantitative Proteomics Data	31:58	Oxonium Ion Guided Analysis of Quantitative Proteomics Data Reveals Site-Specific O-Glycosylation of Anterior Gradient Protein 2 (AGR2).
34065225	0	32	theme	Oxonium	0:6	arg1	Analysis					19:26	Oxonium Ion Guided Analysis	0:26	Oxonium Ion Guided Analysis of Quantitative Proteomics Data	0:58	Oxonium Ion Guided Analysis of Quantitative Proteomics Data Reveals Site-Specific O-Glycosylation of Anterior Gradient Protein 2 (AGR2).
34065225	7	33	gly	glycosylation	1258:1270	arg2	site					1272:1275	glycosylation site	1258:1275	glycosylation site	1258:1275	Among the O-GalNAcylated proteins, we also observed anterior gradient protein 2 (AGR2), a protein which glycosylation site and status was hitherto not well documented.
34065225	6	34	used	used	1006:1009	arg2	ratio					937:941	the ratio	933:941	the ratio of the ions at m/z 144.066 and 138.055	933:980	Following automated glycopeptide assignment (Byonic) and evaluation of the presence and relative intensity of oxonium ions, we observed that, in particular, the ratio of the ions at m/z 144.066 and 138.055, respectively, could be used to discriminate between O-GlcNAcylated and O-GalNAcylated peptides, with concomitant relative quantification between the different cell lines.
34065225	6	34	used	used	1006:1009	arg2	m/z					958:960	m/z 144.066 and 138.055	958:980	m/z	958:960	Following automated glycopeptide assignment (Byonic) and evaluation of the presence and relative intensity of oxonium ions, we observed that, in particular, the ratio of the ions at m/z 144.066 and 138.055, respectively, could be used to discriminate between O-GlcNAcylated and O-GalNAcylated peptides, with concomitant relative quantification between the different cell lines.
34065225	6	34	used	used	1006:1009	arg2	138.055					974:980	138.055	974:980	138.055	974:980	Following automated glycopeptide assignment (Byonic) and evaluation of the presence and relative intensity of oxonium ions, we observed that, in particular, the ratio of the ions at m/z 144.066 and 138.055, respectively, could be used to discriminate between O-GlcNAcylated and O-GalNAcylated peptides, with concomitant relative quantification between the different cell lines.
34065225	2	35	theme	glycopeptides	415:427	arg1	sets					407:410	different sets	397:410	different sets of glycopeptides	397:427	Recently, the characteristic pattern of oxonium ions in glycopeptide fragmentation spectra had been used to assign different sets of glycopeptides.
34065225	2	35	theme	glycopeptides	415:427	arg1	glycopeptides					415:427	glycopeptides	415:427	glycopeptides	415:427	Recently, the characteristic pattern of oxonium ions in glycopeptide fragmentation spectra had been used to assign different sets of glycopeptides.
34065225	0	36	theme	Guided	12:17	arg1	Analysis					19:26	Oxonium Ion Guided Analysis	0:26	Oxonium Ion Guided Analysis of Quantitative Proteomics Data	0:58	Oxonium Ion Guided Analysis of Quantitative Proteomics Data Reveals Site-Specific O-Glycosylation of Anterior Gradient Protein 2 (AGR2).
34065225	2	37	gly	glycopeptide	338:349	arg2	glycopeptide					338:349	glycopeptide fragmentation spectra	338:371	glycopeptide fragmentation spectra	338:371	Recently, the characteristic pattern of oxonium ions in glycopeptide fragmentation spectra had been used to assign different sets of glycopeptides.
34065225	5	38	theme	cancer	757:762	arg1	lines					769:773	three different colorectal cancer cell lines	730:773	three different colorectal cancer cell lines	730:773	For this purpose, we used tandem mass tag (TMT)-labeled samples from total cell lysates and secreted proteins from three different colorectal cancer cell lines.
34065225	8	39	theme	fragmentation	1354:1366	arg1	methods					1368:1374	multiple fragmentation methods	1345:1374	multiple fragmentation methods	1345:1374	Using a combination of multiple fragmentation methods, we then not only assigned the site of modification, but also showed different glycosylation between intracellular (ER-resident) and secreted AGR2.
34065225	0	40	theme	Proteomics	44:53	arg1	Data					55:58	Quantitative Proteomics Data	31:58	Quantitative Proteomics Data	31:58	Oxonium Ion Guided Analysis of Quantitative Proteomics Data Reveals Site-Specific O-Glycosylation of Anterior Gradient Protein 2 (AGR2).
34065225	2	41	theme	oxonium	322:328	arg1	ions					330:333	oxonium ions	322:333	oxonium ions	322:333	Recently, the characteristic pattern of oxonium ions in glycopeptide fragmentation spectra had been used to assign different sets of glycopeptides.
34065225	6	42	theme	O-GalNAcylated	1054:1067	arg1	peptides					1069:1076	O-GlcNAcylated and O-GalNAcylated peptides	1035:1076	O-GlcNAcylated and O-GalNAcylated peptides	1035:1076	Following automated glycopeptide assignment (Byonic) and evaluation of the presence and relative intensity of oxonium ions, we observed that, in particular, the ratio of the ions at m/z 144.066 and 138.055, respectively, could be used to discriminate between O-GlcNAcylated and O-GalNAcylated peptides, with concomitant relative quantification between the different cell lines.
34065225	6	43	dep	presence	851:858	arg1	the					847:849	the	847:849	the	847:849	Following automated glycopeptide assignment (Byonic) and evaluation of the presence and relative intensity of oxonium ions, we observed that, in particular, the ratio of the ions at m/z 144.066 and 138.055, respectively, could be used to discriminate between O-GlcNAcylated and O-GalNAcylated peptides, with concomitant relative quantification between the different cell lines.
34065225	2	44	theme	different	397:405	arg1	sets					407:410	different sets	397:410	different sets of glycopeptides	397:427	Recently, the characteristic pattern of oxonium ions in glycopeptide fragmentation spectra had been used to assign different sets of glycopeptides.
34065225	2	44	theme	different	397:405	arg1	glycopeptides					415:427	glycopeptides	415:427	glycopeptides	415:427	Recently, the characteristic pattern of oxonium ions in glycopeptide fragmentation spectra had been used to assign different sets of glycopeptides.
34065225	5	45	theme	cell	764:767	arg1	lines					769:773	three different colorectal cancer cell lines	730:773	three different colorectal cancer cell lines	730:773	For this purpose, we used tandem mass tag (TMT)-labeled samples from total cell lysates and secreted proteins from three different colorectal cancer cell lines.
34065225	9	46	theme	application	1572:1582	arg1	potential					1553:1561	the potential	1549:1561	the potential of broad application of the use of the relative intensities of oxonium ions for the confident assignment of glycopeptides	1549:1683	Overall, our study shows the potential of broad application of the use of the relative intensities of oxonium ions for the confident assignment of glycopeptides, even in complex proteomics datasets.
34065225	6	47	theme	O-GlcNAcylated	1035:1048	arg1	peptides					1069:1076	O-GlcNAcylated and O-GalNAcylated peptides	1035:1076	O-GlcNAcylated and O-GalNAcylated peptides	1035:1076	Following automated glycopeptide assignment (Byonic) and evaluation of the presence and relative intensity of oxonium ions, we observed that, in particular, the ratio of the ions at m/z 144.066 and 138.055, respectively, could be used to discriminate between O-GlcNAcylated and O-GalNAcylated peptides, with concomitant relative quantification between the different cell lines.
34065225	2	48	theme	fragmentation	351:363	arg1	spectra					365:371	glycopeptide fragmentation spectra	338:371	glycopeptide fragmentation spectra	338:371	Recently, the characteristic pattern of oxonium ions in glycopeptide fragmentation spectra had been used to assign different sets of glycopeptides.
34065225	6	49	theme	oxonium	886:892	arg1	ions					894:897	oxonium ions	886:897	oxonium ions	886:897	Following automated glycopeptide assignment (Byonic) and evaluation of the presence and relative intensity of oxonium ions, we observed that, in particular, the ratio of the ions at m/z 144.066 and 138.055, respectively, could be used to discriminate between O-GlcNAcylated and O-GalNAcylated peptides, with concomitant relative quantification between the different cell lines.
34065225	7	50	theme	anterior	1206:1213	arg1	protein					1244:1250	a protein	1242:1250	a protein which glycosylation site and status was hitherto not well documented	1242:1319	Among the O-GalNAcylated proteins, we also observed anterior gradient protein 2 (AGR2), a protein which glycosylation site and status was hitherto not well documented.
34065225	7	50	theme	anterior	1206:1213	arg1	protein					1224:1230	anterior gradient protein 2	1206:1232	anterior gradient protein 2 (AGR2)	1206:1239	Among the O-GalNAcylated proteins, we also observed anterior gradient protein 2 (AGR2), a protein which glycosylation site and status was hitherto not well documented.
34065225	7	50	theme	anterior	1206:1213	arg1	AGR2					1235:1238	AGR2	1235:1238	AGR2	1235:1238	Among the O-GalNAcylated proteins, we also observed anterior gradient protein 2 (AGR2), a protein which glycosylation site and status was hitherto not well documented.
34065225	5	51	theme	tandem	641:646	arg1	samples					671:677	tandem mass tag (TMT)-labeled samples	641:677	tandem mass tag (TMT)-labeled samples from total cell lysates and secreted proteins from three different colorectal cancer cell lines	641:773	For this purpose, we used tandem mass tag (TMT)-labeled samples from total cell lysates and secreted proteins from three different colorectal cancer cell lines.
34065225	6	52	theme	automated	786:794	arg1	Byonic					821:826	Byonic	821:826	Byonic	821:826	Following automated glycopeptide assignment (Byonic) and evaluation of the presence and relative intensity of oxonium ions, we observed that, in particular, the ratio of the ions at m/z 144.066 and 138.055, respectively, could be used to discriminate between O-GlcNAcylated and O-GalNAcylated peptides, with concomitant relative quantification between the different cell lines.
34065225	6	52	theme	automated	786:794	arg1	assignment					809:818	automated glycopeptide assignment	786:818	automated glycopeptide assignment (Byonic)	786:827	Following automated glycopeptide assignment (Byonic) and evaluation of the presence and relative intensity of oxonium ions, we observed that, in particular, the ratio of the ions at m/z 144.066 and 138.055, respectively, could be used to discriminate between O-GlcNAcylated and O-GalNAcylated peptides, with concomitant relative quantification between the different cell lines.
34065225	6	53	theme	intensity	873:881	arg1	Byonic					821:826	Byonic	821:826	Byonic	821:826	Following automated glycopeptide assignment (Byonic) and evaluation of the presence and relative intensity of oxonium ions, we observed that, in particular, the ratio of the ions at m/z 144.066 and 138.055, respectively, could be used to discriminate between O-GlcNAcylated and O-GalNAcylated peptides, with concomitant relative quantification between the different cell lines.
34065225	6	53	theme	intensity	873:881	arg1	evaluation					833:842	evaluation	833:842	evaluation of the presence and relative intensity of oxonium ions	833:897	Following automated glycopeptide assignment (Byonic) and evaluation of the presence and relative intensity of oxonium ions, we observed that, in particular, the ratio of the ions at m/z 144.066 and 138.055, respectively, could be used to discriminate between O-GlcNAcylated and O-GalNAcylated peptides, with concomitant relative quantification between the different cell lines.
34065225	6	53	theme	intensity	873:881	arg1	assignment					809:818	automated glycopeptide assignment	786:818	automated glycopeptide assignment (Byonic)	786:827	Following automated glycopeptide assignment (Byonic) and evaluation of the presence and relative intensity of oxonium ions, we observed that, in particular, the ratio of the ions at m/z 144.066 and 138.055, respectively, could be used to discriminate between O-GlcNAcylated and O-GalNAcylated peptides, with concomitant relative quantification between the different cell lines.
34065225	6	54	theme	cell	1142:1145	arg1	lines					1147:1151	the different cell lines	1128:1151	the different cell lines	1128:1151	Following automated glycopeptide assignment (Byonic) and evaluation of the presence and relative intensity of oxonium ions, we observed that, in particular, the ratio of the ions at m/z 144.066 and 138.055, respectively, could be used to discriminate between O-GlcNAcylated and O-GalNAcylated peptides, with concomitant relative quantification between the different cell lines.
34065225	9	55	theme	relative	1602:1609	arg1	intensities					1611:1621	the relative intensities	1598:1621	the relative intensities of oxonium ions	1598:1637	Overall, our study shows the potential of broad application of the use of the relative intensities of oxonium ions for the confident assignment of glycopeptides, even in complex proteomics datasets.
34065225	6	56	from	138.055	974:980	arg1	ratio					937:941	the ratio	933:941	the ratio of the ions at m/z 144.066 and 138.055	933:980	Following automated glycopeptide assignment (Byonic) and evaluation of the presence and relative intensity of oxonium ions, we observed that, in particular, the ratio of the ions at m/z 144.066 and 138.055, respectively, could be used to discriminate between O-GlcNAcylated and O-GalNAcylated peptides, with concomitant relative quantification between the different cell lines.
34065225	5	57	theme	-labeled	662:669	arg1	samples					671:677	tandem mass tag (TMT)-labeled samples	641:677	tandem mass tag (TMT)-labeled samples from total cell lysates and secreted proteins from three different colorectal cancer cell lines	641:773	For this purpose, we used tandem mass tag (TMT)-labeled samples from total cell lysates and secreted proteins from three different colorectal cancer cell lines.
34065225	9	58	theme	ions	1634:1637	arg1	intensities					1611:1621	the relative intensities	1598:1621	the relative intensities of oxonium ions	1598:1637	Overall, our study shows the potential of broad application of the use of the relative intensities of oxonium ions for the confident assignment of glycopeptides, even in complex proteomics datasets.
34065225	6	59	theme	concomitant	1084:1094	arg1	quantification					1105:1118	concomitant relative quantification	1084:1118	concomitant relative quantification between the different cell lines	1084:1151	Following automated glycopeptide assignment (Byonic) and evaluation of the presence and relative intensity of oxonium ions, we observed that, in particular, the ratio of the ions at m/z 144.066 and 138.055, respectively, could be used to discriminate between O-GlcNAcylated and O-GalNAcylated peptides, with concomitant relative quantification between the different cell lines.
34065225	1	60	from	changes	237:243	arg1	glycosylation					248:260	glycosylation	248:260	glycosylation related to disease	248:279	Developments in mass spectrometry (MS)-based analyses of glycoproteins have been important to study changes in glycosylation related to disease.
34065225	1	61	theme	glycoproteins	194:206	arg1	analyses					182:189	mass spectrometry (MS)-based analyses	153:189	mass spectrometry (MS)-based analyses of glycoproteins	153:206	Developments in mass spectrometry (MS)-based analyses of glycoproteins have been important to study changes in glycosylation related to disease.
34065225	5	62	theme	cell	690:693	arg1	lysates					695:701	total cell lysates	684:701	total cell lysates	684:701	For this purpose, we used tandem mass tag (TMT)-labeled samples from total cell lysates and secreted proteins from three different colorectal cancer cell lines.
34065225	5	63	from	lysates	695:701	arg1	samples					671:677	tandem mass tag (TMT)-labeled samples	641:677	tandem mass tag (TMT)-labeled samples from total cell lysates and secreted proteins from three different colorectal cancer cell lines	641:773	For this purpose, we used tandem mass tag (TMT)-labeled samples from total cell lysates and secreted proteins from three different colorectal cancer cell lines.
34065225	9	64	theme	glycopeptides	1671:1683	arg1	assignment					1657:1666	the confident assignment	1643:1666	the confident assignment of glycopeptides	1643:1683	Overall, our study shows the potential of broad application of the use of the relative intensities of oxonium ions for the confident assignment of glycopeptides, even in complex proteomics datasets.
34065225	0	65	theme	Site-Specific	68:80	arg1	O-Glycosylation					82:96	Site-Specific O-Glycosylation	68:96	Site-Specific O-Glycosylation of Anterior Gradient Protein 2 (AGR2)	68:134	Oxonium Ion Guided Analysis of Quantitative Proteomics Data Reveals Site-Specific O-Glycosylation of Anterior Gradient Protein 2 (AGR2).
34065225	7	66	theme	O-GalNAcylated	1164:1177	arg1	proteins					1179:1186	the O-GalNAcylated proteins	1160:1186	the O-GalNAcylated proteins	1160:1186	Among the O-GalNAcylated proteins, we also observed anterior gradient protein 2 (AGR2), a protein which glycosylation site and status was hitherto not well documented.
34065225	5	67	from	lines	769:773	arg1	lysates					695:701	total cell lysates	684:701	total cell lysates	684:701	For this purpose, we used tandem mass tag (TMT)-labeled samples from total cell lysates and secreted proteins from three different colorectal cancer cell lines.
34065225	5	67	from	lines	769:773	arg1	proteins					716:723	secreted proteins	707:723	secreted proteins	707:723	For this purpose, we used tandem mass tag (TMT)-labeled samples from total cell lysates and secreted proteins from three different colorectal cancer cell lines.
34065225	1	68	theme	mass	153:156	arg1	MS					172:173	MS	172:173	MS	172:173	Developments in mass spectrometry (MS)-based analyses of glycoproteins have been important to study changes in glycosylation related to disease.
34065225	1	68	theme	mass	153:156	arg1	spectrometry					158:169	mass spectrometry	153:169	mass spectrometry (MS)-based analyses of glycoproteins	153:206	Developments in mass spectrometry (MS)-based analyses of glycoproteins have been important to study changes in glycosylation related to disease.
34065225	6	69	theme	ions	950:953	arg1	ratio					937:941	the ratio	933:941	the ratio of the ions at m/z 144.066 and 138.055	933:980	Following automated glycopeptide assignment (Byonic) and evaluation of the presence and relative intensity of oxonium ions, we observed that, in particular, the ratio of the ions at m/z 144.066 and 138.055, respectively, could be used to discriminate between O-GlcNAcylated and O-GalNAcylated peptides, with concomitant relative quantification between the different cell lines.
34065225	9	70	theme	complex	1694:1700	arg1	datasets					1713:1720	complex proteomics datasets	1694:1720	complex proteomics datasets	1694:1720	Overall, our study shows the potential of broad application of the use of the relative intensities of oxonium ions for the confident assignment of glycopeptides, even in complex proteomics datasets.
34065225	8	71	theme	different	1445:1453	arg1	glycosylation					1455:1467	different glycosylation	1445:1467	different glycosylation between intracellular (ER-resident) and secreted AGR2	1445:1521	Using a combination of multiple fragmentation methods, we then not only assigned the site of modification, but also showed different glycosylation between intracellular (ER-resident) and secreted AGR2.
34065225	2	72	gly	glycopeptides	415:427	arg2	glycopeptides					415:427	glycopeptides	415:427	glycopeptides	415:427	Recently, the characteristic pattern of oxonium ions in glycopeptide fragmentation spectra had been used to assign different sets of glycopeptides.
34065225	0	73	theme	Gradient	110:117	arg1	Protein					119:125	Anterior Gradient Protein 2	101:127	Anterior Gradient Protein 2 (AGR2)	101:134	Oxonium Ion Guided Analysis of Quantitative Proteomics Data Reveals Site-Specific O-Glycosylation of Anterior Gradient Protein 2 (AGR2).
34065225	0	73	theme	Gradient	110:117	arg1	AGR2					130:133	AGR2	130:133	AGR2	130:133	Oxonium Ion Guided Analysis of Quantitative Proteomics Data Reveals Site-Specific O-Glycosylation of Anterior Gradient Protein 2 (AGR2).
34065225	0	74	gly	O-Glycosylation	82:96	arg1	Protein					119:125	Anterior Gradient Protein 2	101:127	Anterior Gradient Protein 2 (AGR2)	101:134	Oxonium Ion Guided Analysis of Quantitative Proteomics Data Reveals Site-Specific O-Glycosylation of Anterior Gradient Protein 2 (AGR2).
34065225	0	74	gly	O-Glycosylation	82:96	arg1	AGR2					130:133	AGR2	130:133	AGR2	130:133	Oxonium Ion Guided Analysis of Quantitative Proteomics Data Reveals Site-Specific O-Glycosylation of Anterior Gradient Protein 2 (AGR2).
34065225	4	75	theme	quantitative	585:596	arg1	data					609:612	quantitative proteomics data	585:612	quantitative proteomics data	585:612	Here, we thought to investigate how such information can be used to examine quantitative proteomics data.
34065225	0	76	theme	Ion	8:10	arg1	Analysis					19:26	Oxonium Ion Guided Analysis	0:26	Oxonium Ion Guided Analysis of Quantitative Proteomics Data	0:58	Oxonium Ion Guided Analysis of Quantitative Proteomics Data Reveals Site-Specific O-Glycosylation of Anterior Gradient Protein 2 (AGR2).
34065225	7	77	theme	glycosylation	1258:1270	arg1	site					1272:1275	glycosylation site	1258:1275	glycosylation site	1258:1275	Among the O-GalNAcylated proteins, we also observed anterior gradient protein 2 (AGR2), a protein which glycosylation site and status was hitherto not well documented.
34065225	4	78	theme	such	545:548	arg1	information					550:560	such information	545:560	such information	545:560	Here, we thought to investigate how such information can be used to examine quantitative proteomics data.
34065225	8	79	theme	secreted	1509:1516	arg1	AGR2					1518:1521	secreted AGR2	1509:1521	secreted AGR2	1509:1521	Using a combination of multiple fragmentation methods, we then not only assigned the site of modification, but also showed different glycosylation between intracellular (ER-resident) and secreted AGR2.
34065225	5	80	theme	colorectal	746:755	arg1	lines					769:773	three different colorectal cancer cell lines	730:773	three different colorectal cancer cell lines	730:773	For this purpose, we used tandem mass tag (TMT)-labeled samples from total cell lysates and secreted proteins from three different colorectal cancer cell lines.
34065225	0	81	theme	Protein	119:125	arg1	O-Glycosylation					82:96	Site-Specific O-Glycosylation	68:96	Site-Specific O-Glycosylation of Anterior Gradient Protein 2 (AGR2)	68:134	Oxonium Ion Guided Analysis of Quantitative Proteomics Data Reveals Site-Specific O-Glycosylation of Anterior Gradient Protein 2 (AGR2).
34065225	0	82	theme	Data	55:58	arg1	Analysis					19:26	Oxonium Ion Guided Analysis	0:26	Oxonium Ion Guided Analysis of Quantitative Proteomics Data	0:58	Oxonium Ion Guided Analysis of Quantitative Proteomics Data Reveals Site-Specific O-Glycosylation of Anterior Gradient Protein 2 (AGR2).
34065225	8	83	theme	multiple	1345:1352	arg1	methods					1368:1374	multiple fragmentation methods	1345:1374	multiple fragmentation methods	1345:1374	Using a combination of multiple fragmentation methods, we then not only assigned the site of modification, but also showed different glycosylation between intracellular (ER-resident) and secreted AGR2.
34065225	3	84	from	helpful	454:460	arg1	particular					433:442	particular	433:442	particular	433:442	In particular, this was helpful to discriminate between O-GalNAc and O-GlcNAc.
34065225	2	85	theme	ions	330:333	arg1	pattern					311:317	the characteristic pattern	292:317	the characteristic pattern of oxonium ions in glycopeptide fragmentation spectra	292:371	Recently, the characteristic pattern of oxonium ions in glycopeptide fragmentation spectra had been used to assign different sets of glycopeptides.
34065225	4	86	theme	proteomics	598:607	arg1	data					609:612	quantitative proteomics data	585:612	quantitative proteomics data	585:612	Here, we thought to investigate how such information can be used to examine quantitative proteomics data.
34065225	8	87	theme	methods	1368:1374	arg1	combination					1330:1340	a combination	1328:1340	a combination of multiple fragmentation methods	1328:1374	Using a combination of multiple fragmentation methods, we then not only assigned the site of modification, but also showed different glycosylation between intracellular (ER-resident) and secreted AGR2.
34065225	8	88	dep	intracellular	1477:1489	arg1	ER-resident					1492:1502	ER-resident	1492:1502	ER-resident	1492:1502	Using a combination of multiple fragmentation methods, we then not only assigned the site of modification, but also showed different glycosylation between intracellular (ER-resident) and secreted AGR2.
34065225	9	89	theme	broad	1566:1570	arg1	application					1572:1582	broad application	1566:1582	broad application of the use of the relative intensities of oxonium ions	1566:1637	Overall, our study shows the potential of broad application of the use of the relative intensities of oxonium ions for the confident assignment of glycopeptides, even in complex proteomics datasets.
34065225	7	90	theme	gradient	1215:1222	arg1	protein					1244:1250	a protein	1242:1250	a protein which glycosylation site and status was hitherto not well documented	1242:1319	Among the O-GalNAcylated proteins, we also observed anterior gradient protein 2 (AGR2), a protein which glycosylation site and status was hitherto not well documented.
34065225	7	90	theme	gradient	1215:1222	arg1	protein					1224:1230	anterior gradient protein 2	1206:1232	anterior gradient protein 2 (AGR2)	1206:1239	Among the O-GalNAcylated proteins, we also observed anterior gradient protein 2 (AGR2), a protein which glycosylation site and status was hitherto not well documented.
34065225	7	90	theme	gradient	1215:1222	arg1	AGR2					1235:1238	AGR2	1235:1238	AGR2	1235:1238	Among the O-GalNAcylated proteins, we also observed anterior gradient protein 2 (AGR2), a protein which glycosylation site and status was hitherto not well documented.
34065225	3	91	from	particular	433:442	arg1	helpful					454:460	helpful	454:460	helpful	454:460	In particular, this was helpful to discriminate between O-GalNAc and O-GlcNAc.
16434389	0	0	theme	kinase	87:92	arg1	identification					43:56	identification	43:56	Recombinant O-GlcNAc transferase isoforms: identification of O-GlcNAcase, yes tyrosine kinase, and tau as isoform-specific substrates.	0:133	Recombinant O-GlcNAc transferase isoforms: identification of O-GlcNAcase, yes tyrosine kinase, and tau as isoform-specific substrates.
16434389	7	1	theme	OGT	1163:1165	arg1	isoform					1152:1158	The short isoform	1142:1158	The short isoform of OGT (sOGT)	1142:1172	The short isoform of OGT (sOGT) did not glycosylate any of the substrates tested, although it retains a potentially active catalytic domain.
16434389	4	2	theme	tyrosine	855:862	arg1	yes					871:873	the Src-family tyrosine kinase yes	840:873	the Src-family tyrosine kinase yes	840:873	We expressed each of these OGT isoforms in a soluble form in Escherichia coli and have used them to identify novel targets including the Src-family tyrosine kinase yes and O-GlcNAc-ase.
16434389	0	3	theme	tyrosine	78:85	arg1	kinase					87:92	yes tyrosine kinase	74:92	yes tyrosine kinase	74:92	Recombinant O-GlcNAc transferase isoforms: identification of O-GlcNAcase, yes tyrosine kinase, and tau as isoform-specific substrates.
16434389	4	4	theme	Src-family	844:853	arg1	yes					871:873	the Src-family tyrosine kinase yes	840:873	the Src-family tyrosine kinase yes	840:873	We expressed each of these OGT isoforms in a soluble form in Escherichia coli and have used them to identify novel targets including the Src-family tyrosine kinase yes and O-GlcNAc-ase.
16434389	1	5	theme	variety	261:267	arg1	threonine					237:245	threonine	237:245	threonine	237:245	O-linked N-acetylglucosaminyltransferase (OGT) catalyzes the transfer of O-linked GlcNAc to serine or threonine residues of a variety of substrate proteins, including nuclear pore proteins, transcription factors, and proteins implicated in diabetes and neurodegenerative disorders.
16434389	1	5	theme	variety	261:267	arg1	serine					227:232	serine	227:232	serine	227:232	O-linked N-acetylglucosaminyltransferase (OGT) catalyzes the transfer of O-linked GlcNAc to serine or threonine residues of a variety of substrate proteins, including nuclear pore proteins, transcription factors, and proteins implicated in diabetes and neurodegenerative disorders.
16434389	8	6	theme	enzyme	1443:1448	arg1	isoforms					1427:1434	all active isoforms	1416:1434	all active isoforms of the enzyme	1416:1448	Our findings demonstrate the potential utility of recombinant OGT in identifying new targets and illustrate the necessity to examine all active isoforms of the enzyme.
16434389	1	7	link	O-linked	208:215	arg1	GlcNAc					217:222	O-linked GlcNAc	208:222	O-linked GlcNAc	208:222	O-linked N-acetylglucosaminyltransferase (OGT) catalyzes the transfer of O-linked GlcNAc to serine or threonine residues of a variety of substrate proteins, including nuclear pore proteins, transcription factors, and proteins implicated in diabetes and neurodegenerative disorders.
16434389	4	8	from	form	760:763	arg1	coli					780:783	Escherichia coli	768:783	Escherichia coli	768:783	We expressed each of these OGT isoforms in a soluble form in Escherichia coli and have used them to identify novel targets including the Src-family tyrosine kinase yes and O-GlcNAc-ase.
16434389	4	9	theme	soluble	752:758	arg1	form					760:763	a soluble form	750:763	a soluble form in Escherichia coli	750:783	We expressed each of these OGT isoforms in a soluble form in Escherichia coli and have used them to identify novel targets including the Src-family tyrosine kinase yes and O-GlcNAc-ase.
16434389	8	10	theme	potential	1312:1320	arg1	utility					1322:1328	the potential utility	1308:1328	the potential utility of recombinant OGT in identifying new targets	1308:1374	Our findings demonstrate the potential utility of recombinant OGT in identifying new targets and illustrate the necessity to examine all active isoforms of the enzyme.
16434389	5	11	mod	modified	1073:1080	arg1	tau					1052:1054	tau	1052:1054	tau	1052:1054	We demonstrate that some substrate proteins, such as Nup62 and casein kinase II, are glycosylated by both ncOGT and mOGT, while others such as O-GlcNAcase and tau are specifically modified by ncOGT.
16434389	5	11	mod	modified	1073:1080	arg1	others					1021:1026	others	1021:1026	others such as O-GlcNAcase and tau	1021:1054	We demonstrate that some substrate proteins, such as Nup62 and casein kinase II, are glycosylated by both ncOGT and mOGT, while others such as O-GlcNAcase and tau are specifically modified by ncOGT.
16434389	5	11	mod	modified	1073:1080	arg1	O-GlcNAcase					1036:1046	O-GlcNAcase	1036:1046	O-GlcNAcase	1036:1046	We demonstrate that some substrate proteins, such as Nup62 and casein kinase II, are glycosylated by both ncOGT and mOGT, while others such as O-GlcNAcase and tau are specifically modified by ncOGT.
16434389	5	11	mod	modified	1073:1080	arg3	ncOGT					1085:1089	ncOGT	1085:1089	ncOGT	1085:1089	We demonstrate that some substrate proteins, such as Nup62 and casein kinase II, are glycosylated by both ncOGT and mOGT, while others such as O-GlcNAcase and tau are specifically modified by ncOGT.
16434389	4	12	theme	kinase	864:869	arg1	yes					871:873	the Src-family tyrosine kinase yes	840:873	the Src-family tyrosine kinase yes	840:873	We expressed each of these OGT isoforms in a soluble form in Escherichia coli and have used them to identify novel targets including the Src-family tyrosine kinase yes and O-GlcNAc-ase.
16434389	9	13	theme	kinase	1484:1489	arg1	identification					1455:1468	The identification	1451:1468	The identification of a tyrosine kinase and O-GlcNAcase as OGT targets	1451:1520	The identification of a tyrosine kinase and O-GlcNAcase as OGT targets suggests the potential for OGT participation in numerous signal transduction cascades.
16434389	1	14	theme	substrate	272:280	arg1	proteins					315:322	nuclear pore proteins	302:322	nuclear pore proteins	302:322	O-linked N-acetylglucosaminyltransferase (OGT) catalyzes the transfer of O-linked GlcNAc to serine or threonine residues of a variety of substrate proteins, including nuclear pore proteins, transcription factors, and proteins implicated in diabetes and neurodegenerative disorders.
16434389	1	14	theme	substrate	272:280	arg1	proteins					282:289	substrate proteins	272:289	substrate proteins	272:289	O-linked N-acetylglucosaminyltransferase (OGT) catalyzes the transfer of O-linked GlcNAc to serine or threonine residues of a variety of substrate proteins, including nuclear pore proteins, transcription factors, and proteins implicated in diabetes and neurodegenerative disorders.
16434389	1	14	theme	substrate	272:280	arg1	proteins					352:359	proteins	352:359	proteins implicated in diabetes and neurodegenerative disorders	352:414	O-linked N-acetylglucosaminyltransferase (OGT) catalyzes the transfer of O-linked GlcNAc to serine or threonine residues of a variety of substrate proteins, including nuclear pore proteins, transcription factors, and proteins implicated in diabetes and neurodegenerative disorders.
16434389	1	14	theme	substrate	272:280	arg1	factors					339:345	transcription factors	325:345	transcription factors	325:345	O-linked N-acetylglucosaminyltransferase (OGT) catalyzes the transfer of O-linked GlcNAc to serine or threonine residues of a variety of substrate proteins, including nuclear pore proteins, transcription factors, and proteins implicated in diabetes and neurodegenerative disorders.
16434389	5	15	theme	casein	956:961	arg1	kinase					963:968	casein kinase II	956:971	casein kinase II	956:971	We demonstrate that some substrate proteins, such as Nup62 and casein kinase II, are glycosylated by both ncOGT and mOGT, while others such as O-GlcNAcase and tau are specifically modified by ncOGT.
16434389	7	16	theme	active	1258:1263	arg1	domain					1275:1280	a potentially active catalytic domain	1244:1280	a potentially active catalytic domain	1244:1280	The short isoform of OGT (sOGT) did not glycosylate any of the substrates tested, although it retains a potentially active catalytic domain.
16434389	0	17	theme	tau	99:101	arg1	identification					43:56	identification	43:56	Recombinant O-GlcNAc transferase isoforms: identification of O-GlcNAcase, yes tyrosine kinase, and tau as isoform-specific substrates.	0:133	Recombinant O-GlcNAc transferase isoforms: identification of O-GlcNAcase, yes tyrosine kinase, and tau as isoform-specific substrates.
16434389	2	18	dep	isoforms	458:465	arg1	isoforms					458:465	two nucleocytoplasmic isoforms	436:465	two nucleocytoplasmic isoforms of OGT (ncOGT and sOGT)	436:489	We have identified two nucleocytoplasmic isoforms of OGT (ncOGT and sOGT) and one isoform that localizes to the mitochondria (mOGT).
16434389	2	18	dep	isoforms	458:465	arg1	sOGT					485:488	sOGT	485:488	sOGT	485:488	We have identified two nucleocytoplasmic isoforms of OGT (ncOGT and sOGT) and one isoform that localizes to the mitochondria (mOGT).
16434389	2	18	dep	isoforms	458:465	arg1	ncOGT					475:479	ncOGT	475:479	ncOGT	475:479	We have identified two nucleocytoplasmic isoforms of OGT (ncOGT and sOGT) and one isoform that localizes to the mitochondria (mOGT).
16434389	2	19	theme	OGT	470:472	arg1	isoform					499:505	one isoform	495:505	one isoform that localizes to the mitochondria (mOGT)	495:547	We have identified two nucleocytoplasmic isoforms of OGT (ncOGT and sOGT) and one isoform that localizes to the mitochondria (mOGT).
16434389	2	19	theme	OGT	470:472	arg1	isoforms					458:465	two nucleocytoplasmic isoforms	436:465	two nucleocytoplasmic isoforms of OGT (ncOGT and sOGT)	436:489	We have identified two nucleocytoplasmic isoforms of OGT (ncOGT and sOGT) and one isoform that localizes to the mitochondria (mOGT).
16434389	2	19	theme	OGT	470:472	arg1	sOGT					485:488	sOGT	485:488	sOGT	485:488	We have identified two nucleocytoplasmic isoforms of OGT (ncOGT and sOGT) and one isoform that localizes to the mitochondria (mOGT).
16434389	2	19	theme	OGT	470:472	arg1	ncOGT					475:479	ncOGT	475:479	ncOGT	475:479	We have identified two nucleocytoplasmic isoforms of OGT (ncOGT and sOGT) and one isoform that localizes to the mitochondria (mOGT).
16434389	4	20	used	used	794:797	arg2	We					707:708	We	707:708	We	707:708	We expressed each of these OGT isoforms in a soluble form in Escherichia coli and have used them to identify novel targets including the Src-family tyrosine kinase yes and O-GlcNAc-ase.
16434389	7	21	theme	catalytic	1265:1273	arg1	domain					1275:1280	a potentially active catalytic domain	1244:1280	a potentially active catalytic domain	1244:1280	The short isoform of OGT (sOGT) did not glycosylate any of the substrates tested, although it retains a potentially active catalytic domain.
16434389	0	22	theme	O-GlcNAc	12:19	arg1	isoforms					33:40	Recombinant O-GlcNAc transferase isoforms	0:40	Recombinant O-GlcNAc transferase isoforms: identification of O-GlcNAcase, yes tyrosine kinase, and tau as isoform-specific substrates.	0:133	Recombinant O-GlcNAc transferase isoforms: identification of O-GlcNAcase, yes tyrosine kinase, and tau as isoform-specific substrates.
16434389	4	23	theme	OGT	734:736	arg1	isoforms					738:745	these OGT isoforms	728:745	these OGT isoforms	728:745	We expressed each of these OGT isoforms in a soluble form in Escherichia coli and have used them to identify novel targets including the Src-family tyrosine kinase yes and O-GlcNAc-ase.
16434389	0	24	theme	Recombinant	0:10	arg1	isoforms					33:40	Recombinant O-GlcNAc transferase isoforms	0:40	Recombinant O-GlcNAc transferase isoforms: identification of O-GlcNAcase, yes tyrosine kinase, and tau as isoform-specific substrates.	0:133	Recombinant O-GlcNAc transferase isoforms: identification of O-GlcNAcase, yes tyrosine kinase, and tau as isoform-specific substrates.
16434389	1	25	theme	proteins	282:289	arg1	variety					261:267	a variety	259:267	a variety of substrate proteins, including nuclear pore proteins, transcription factors, and proteins implicated in diabetes and neurodegenerative disorders	259:414	O-linked N-acetylglucosaminyltransferase (OGT) catalyzes the transfer of O-linked GlcNAc to serine or threonine residues of a variety of substrate proteins, including nuclear pore proteins, transcription factors, and proteins implicated in diabetes and neurodegenerative disorders.
16434389	1	25	theme	proteins	282:289	arg1	proteins					282:289	substrate proteins	272:289	substrate proteins	272:289	O-linked N-acetylglucosaminyltransferase (OGT) catalyzes the transfer of O-linked GlcNAc to serine or threonine residues of a variety of substrate proteins, including nuclear pore proteins, transcription factors, and proteins implicated in diabetes and neurodegenerative disorders.
16434389	1	25	theme	proteins	282:289	arg1	proteins					352:359	proteins	352:359	proteins implicated in diabetes and neurodegenerative disorders	352:414	O-linked N-acetylglucosaminyltransferase (OGT) catalyzes the transfer of O-linked GlcNAc to serine or threonine residues of a variety of substrate proteins, including nuclear pore proteins, transcription factors, and proteins implicated in diabetes and neurodegenerative disorders.
16434389	1	25	theme	proteins	282:289	arg1	factors					339:345	transcription factors	325:345	transcription factors	325:345	O-linked N-acetylglucosaminyltransferase (OGT) catalyzes the transfer of O-linked GlcNAc to serine or threonine residues of a variety of substrate proteins, including nuclear pore proteins, transcription factors, and proteins implicated in diabetes and neurodegenerative disorders.
16434389	1	25	theme	proteins	282:289	arg1	proteins					315:322	nuclear pore proteins	302:322	nuclear pore proteins	302:322	O-linked N-acetylglucosaminyltransferase (OGT) catalyzes the transfer of O-linked GlcNAc to serine or threonine residues of a variety of substrate proteins, including nuclear pore proteins, transcription factors, and proteins implicated in diabetes and neurodegenerative disorders.
16434389	9	26	theme	OGT	1510:1512	arg1	targets					1514:1520	OGT targets	1510:1520	OGT targets	1510:1520	The identification of a tyrosine kinase and O-GlcNAcase as OGT targets suggests the potential for OGT participation in numerous signal transduction cascades.
16434389	3	27	theme	repeat	653:658	arg1	motifs					660:665	tetratricopeptide repeat motifs	635:665	tetratricopeptide repeat motifs found at the N-terminus of each enzyme	635:704	These three isoforms contain identical catalytic regions but differ in the number of tetratricopeptide repeat motifs found at the N-terminus of each enzyme.
16434389	5	28	theme	substrate	918:926	arg1	proteins					928:935	some substrate proteins	913:935	some substrate proteins	913:935	We demonstrate that some substrate proteins, such as Nup62 and casein kinase II, are glycosylated by both ncOGT and mOGT, while others such as O-GlcNAcase and tau are specifically modified by ncOGT.
16434389	5	28	theme	substrate	918:926	arg1	Nup62					946:950	Nup62	946:950	Nup62	946:950	We demonstrate that some substrate proteins, such as Nup62 and casein kinase II, are glycosylated by both ncOGT and mOGT, while others such as O-GlcNAcase and tau are specifically modified by ncOGT.
16434389	5	28	theme	substrate	918:926	arg1	kinase					963:968	casein kinase II	956:971	casein kinase II	956:971	We demonstrate that some substrate proteins, such as Nup62 and casein kinase II, are glycosylated by both ncOGT and mOGT, while others such as O-GlcNAcase and tau are specifically modified by ncOGT.
16434389	1	29	theme	O-linked	208:215	arg1	GlcNAc					217:222	O-linked GlcNAc	208:222	O-linked GlcNAc	208:222	O-linked N-acetylglucosaminyltransferase (OGT) catalyzes the transfer of O-linked GlcNAc to serine or threonine residues of a variety of substrate proteins, including nuclear pore proteins, transcription factors, and proteins implicated in diabetes and neurodegenerative disorders.
16434389	0	30	theme	transferase	21:31	arg1	isoforms					33:40	Recombinant O-GlcNAc transferase isoforms	0:40	Recombinant O-GlcNAc transferase isoforms: identification of O-GlcNAcase, yes tyrosine kinase, and tau as isoform-specific substrates.	0:133	Recombinant O-GlcNAc transferase isoforms: identification of O-GlcNAcase, yes tyrosine kinase, and tau as isoform-specific substrates.
16434389	3	31	contain	contain	571:577	arg1	isoforms					562:569	These three isoforms	550:569	These three isoforms	550:569	These three isoforms contain identical catalytic regions but differ in the number of tetratricopeptide repeat motifs found at the N-terminus of each enzyme.
16434389	3	31	contain	contain	571:577	arg2	regions					599:605	identical catalytic regions	579:605	identical catalytic regions	579:605	These three isoforms contain identical catalytic regions but differ in the number of tetratricopeptide repeat motifs found at the N-terminus of each enzyme.
16434389	0	32	theme	isoform-specific	106:121	arg1	substrates					123:132	isoform-specific substrates	106:132	isoform-specific substrates	106:132	Recombinant O-GlcNAc transferase isoforms: identification of O-GlcNAcase, yes tyrosine kinase, and tau as isoform-specific substrates.
16434389	1	33	theme	neurodegenerative	388:404	arg1	disorders					406:414	neurodegenerative disorders	388:414	neurodegenerative disorders	388:414	O-linked N-acetylglucosaminyltransferase (OGT) catalyzes the transfer of O-linked GlcNAc to serine or threonine residues of a variety of substrate proteins, including nuclear pore proteins, transcription factors, and proteins implicated in diabetes and neurodegenerative disorders.
16434389	6	34	theme	yes	1096:1098	arg1	kinase					1100:1105	The yes kinase	1092:1105	The yes kinase	1092:1105	The yes kinase was specifically modified by mOGT.
16434389	1	35	theme	GlcNAc	217:222	arg1	transfer					196:203	the transfer	192:203	the transfer of O-linked GlcNAc to serine or threonine residues of a variety of substrate proteins, including nuclear pore proteins, transcription factors, and proteins implicated in diabetes and neurodegenerative disorders	192:414	O-linked N-acetylglucosaminyltransferase (OGT) catalyzes the transfer of O-linked GlcNAc to serine or threonine residues of a variety of substrate proteins, including nuclear pore proteins, transcription factors, and proteins implicated in diabetes and neurodegenerative disorders.
16434389	1	36	theme	nuclear	302:308	arg1	proteins					315:322	nuclear pore proteins	302:322	nuclear pore proteins	302:322	O-linked N-acetylglucosaminyltransferase (OGT) catalyzes the transfer of O-linked GlcNAc to serine or threonine residues of a variety of substrate proteins, including nuclear pore proteins, transcription factors, and proteins implicated in diabetes and neurodegenerative disorders.
16434389	3	37	theme	motifs	660:665	arg1	number					625:630	the number	621:630	the number of tetratricopeptide repeat motifs found at the N-terminus of each enzyme	621:704	These three isoforms contain identical catalytic regions but differ in the number of tetratricopeptide repeat motifs found at the N-terminus of each enzyme.
16434389	8	38	theme	recombinant	1333:1343	arg1	OGT					1345:1347	recombinant OGT	1333:1347	recombinant OGT	1333:1347	Our findings demonstrate the potential utility of recombinant OGT in identifying new targets and illustrate the necessity to examine all active isoforms of the enzyme.
16434389	1	39	theme	pore	310:313	arg1	proteins					315:322	nuclear pore proteins	302:322	nuclear pore proteins	302:322	O-linked N-acetylglucosaminyltransferase (OGT) catalyzes the transfer of O-linked GlcNAc to serine or threonine residues of a variety of substrate proteins, including nuclear pore proteins, transcription factors, and proteins implicated in diabetes and neurodegenerative disorders.
16434389	9	40	theme	transduction	1586:1597	arg1	cascades					1599:1606	numerous signal transduction cascades	1570:1606	numerous signal transduction cascades	1570:1606	The identification of a tyrosine kinase and O-GlcNAcase as OGT targets suggests the potential for OGT participation in numerous signal transduction cascades.
16434389	6	41	mod	modified	1124:1131	arg1	kinase					1100:1105	The yes kinase	1092:1105	The yes kinase	1092:1105	The yes kinase was specifically modified by mOGT.
16434389	6	41	mod	modified	1124:1131	arg3	mOGT					1136:1139	mOGT	1136:1139	mOGT	1136:1139	The yes kinase was specifically modified by mOGT.
16434389	7	42	theme	short	1146:1150	arg1	isoform					1152:1158	The short isoform	1142:1158	The short isoform of OGT (sOGT)	1142:1172	The short isoform of OGT (sOGT) did not glycosylate any of the substrates tested, although it retains a potentially active catalytic domain.
16434389	0	43	theme	O-GlcNAcase	61:71	arg1	identification					43:56	identification	43:56	Recombinant O-GlcNAc transferase isoforms: identification of O-GlcNAcase, yes tyrosine kinase, and tau as isoform-specific substrates.	0:133	Recombinant O-GlcNAc transferase isoforms: identification of O-GlcNAcase, yes tyrosine kinase, and tau as isoform-specific substrates.
16434389	3	44	theme	tetratricopeptide	635:651	arg1	motifs					660:665	tetratricopeptide repeat motifs	635:665	tetratricopeptide repeat motifs found at the N-terminus of each enzyme	635:704	These three isoforms contain identical catalytic regions but differ in the number of tetratricopeptide repeat motifs found at the N-terminus of each enzyme.
16434389	3	45	theme	identical	579:587	arg1	regions					599:605	identical catalytic regions	579:605	identical catalytic regions	579:605	These three isoforms contain identical catalytic regions but differ in the number of tetratricopeptide repeat motifs found at the N-terminus of each enzyme.
16434389	4	46	theme	novel	816:820	arg1	O-GlcNAc-ase					879:890	O-GlcNAc-ase	879:890	O-GlcNAc-ase	879:890	We expressed each of these OGT isoforms in a soluble form in Escherichia coli and have used them to identify novel targets including the Src-family tyrosine kinase yes and O-GlcNAc-ase.
16434389	4	46	theme	novel	816:820	arg1	targets					822:828	novel targets	816:828	novel targets including the Src-family tyrosine kinase yes and O-GlcNAc-ase	816:890	We expressed each of these OGT isoforms in a soluble form in Escherichia coli and have used them to identify novel targets including the Src-family tyrosine kinase yes and O-GlcNAc-ase.
16434389	4	46	theme	novel	816:820	arg1	yes					871:873	the Src-family tyrosine kinase yes	840:873	the Src-family tyrosine kinase yes	840:873	We expressed each of these OGT isoforms in a soluble form in Escherichia coli and have used them to identify novel targets including the Src-family tyrosine kinase yes and O-GlcNAc-ase.
16434389	1	47	link	O-linked	135:142	arg1	OGT					177:179	OGT	177:179	OGT	177:179	O-linked N-acetylglucosaminyltransferase (OGT) catalyzes the transfer of O-linked GlcNAc to serine or threonine residues of a variety of substrate proteins, including nuclear pore proteins, transcription factors, and proteins implicated in diabetes and neurodegenerative disorders.
16434389	1	47	link	O-linked	135:142	arg1	N-acetylglucosaminyltransferase					144:174	O-linked N-acetylglucosaminyltransferase	135:174	O-linked N-acetylglucosaminyltransferase (OGT)	135:180	O-linked N-acetylglucosaminyltransferase (OGT) catalyzes the transfer of O-linked GlcNAc to serine or threonine residues of a variety of substrate proteins, including nuclear pore proteins, transcription factors, and proteins implicated in diabetes and neurodegenerative disorders.
16434389	9	48	theme	tyrosine	1475:1482	arg1	kinase					1484:1489	a tyrosine kinase	1473:1489	a tyrosine kinase	1473:1489	The identification of a tyrosine kinase and O-GlcNAcase as OGT targets suggests the potential for OGT participation in numerous signal transduction cascades.
16434389	3	49	theme	catalytic	589:597	arg1	regions					599:605	identical catalytic regions	579:605	identical catalytic regions	579:605	These three isoforms contain identical catalytic regions but differ in the number of tetratricopeptide repeat motifs found at the N-terminus of each enzyme.
16434389	1	50	theme	transcription	325:337	arg1	factors					339:345	transcription factors	325:345	transcription factors	325:345	O-linked N-acetylglucosaminyltransferase (OGT) catalyzes the transfer of O-linked GlcNAc to serine or threonine residues of a variety of substrate proteins, including nuclear pore proteins, transcription factors, and proteins implicated in diabetes and neurodegenerative disorders.
16434389	8	51	theme	new	1364:1366	arg1	targets					1368:1374	new targets	1364:1374	new targets	1364:1374	Our findings demonstrate the potential utility of recombinant OGT in identifying new targets and illustrate the necessity to examine all active isoforms of the enzyme.
16434389	0	52	dep	isoforms	33:40	arg1	identification					43:56	identification	43:56	Recombinant O-GlcNAc transferase isoforms: identification of O-GlcNAcase, yes tyrosine kinase, and tau as isoform-specific substrates.	0:133	Recombinant O-GlcNAc transferase isoforms: identification of O-GlcNAcase, yes tyrosine kinase, and tau as isoform-specific substrates.
16434389	9	53	theme	signal	1579:1584	arg1	cascades					1599:1606	numerous signal transduction cascades	1570:1606	numerous signal transduction cascades	1570:1606	The identification of a tyrosine kinase and O-GlcNAcase as OGT targets suggests the potential for OGT participation in numerous signal transduction cascades.
16434389	7	54	gly	glycosylate	1182:1192	arg1	any					1194:1196	any	1194:1196	any	1194:1196	The short isoform of OGT (sOGT) did not glycosylate any of the substrates tested, although it retains a potentially active catalytic domain.
16434389	9	55	theme	O-GlcNAcase	1495:1505	arg1	identification					1455:1468	The identification	1451:1468	The identification of a tyrosine kinase and O-GlcNAcase as OGT targets	1451:1520	The identification of a tyrosine kinase and O-GlcNAcase as OGT targets suggests the potential for OGT participation in numerous signal transduction cascades.
16434389	1	56	dep	serine	227:232	arg1	residues					247:254	residues	247:254	residues	247:254	O-linked N-acetylglucosaminyltransferase (OGT) catalyzes the transfer of O-linked GlcNAc to serine or threonine residues of a variety of substrate proteins, including nuclear pore proteins, transcription factors, and proteins implicated in diabetes and neurodegenerative disorders.
16434389	1	57	theme	O-linked	135:142	arg1	OGT					177:179	OGT	177:179	OGT	177:179	O-linked N-acetylglucosaminyltransferase (OGT) catalyzes the transfer of O-linked GlcNAc to serine or threonine residues of a variety of substrate proteins, including nuclear pore proteins, transcription factors, and proteins implicated in diabetes and neurodegenerative disorders.
16434389	1	57	theme	O-linked	135:142	arg1	N-acetylglucosaminyltransferase					144:174	O-linked N-acetylglucosaminyltransferase	135:174	O-linked N-acetylglucosaminyltransferase (OGT)	135:180	O-linked N-acetylglucosaminyltransferase (OGT) catalyzes the transfer of O-linked GlcNAc to serine or threonine residues of a variety of substrate proteins, including nuclear pore proteins, transcription factors, and proteins implicated in diabetes and neurodegenerative disorders.
16434389	9	58	from	participation	1553:1565	arg1	cascades					1599:1606	numerous signal transduction cascades	1570:1606	numerous signal transduction cascades	1570:1606	The identification of a tyrosine kinase and O-GlcNAcase as OGT targets suggests the potential for OGT participation in numerous signal transduction cascades.
16434389	0	59	theme	yes	74:76	arg1	kinase					87:92	yes tyrosine kinase	74:92	yes tyrosine kinase	74:92	Recombinant O-GlcNAc transferase isoforms: identification of O-GlcNAcase, yes tyrosine kinase, and tau as isoform-specific substrates.
16434389	8	60	theme	active	1420:1425	arg1	isoforms					1427:1434	all active isoforms	1416:1434	all active isoforms of the enzyme	1416:1448	Our findings demonstrate the potential utility of recombinant OGT in identifying new targets and illustrate the necessity to examine all active isoforms of the enzyme.
16434389	9	61	theme	numerous	1570:1577	arg1	cascades					1599:1606	numerous signal transduction cascades	1570:1606	numerous signal transduction cascades	1570:1606	The identification of a tyrosine kinase and O-GlcNAcase as OGT targets suggests the potential for OGT participation in numerous signal transduction cascades.
16434389	2	62	theme	nucleocytoplasmic	440:456	arg1	isoforms					458:465	two nucleocytoplasmic isoforms	436:465	two nucleocytoplasmic isoforms of OGT (ncOGT and sOGT)	436:489	We have identified two nucleocytoplasmic isoforms of OGT (ncOGT and sOGT) and one isoform that localizes to the mitochondria (mOGT).
16434389	2	62	theme	nucleocytoplasmic	440:456	arg1	sOGT					485:488	sOGT	485:488	sOGT	485:488	We have identified two nucleocytoplasmic isoforms of OGT (ncOGT and sOGT) and one isoform that localizes to the mitochondria (mOGT).
16434389	2	62	theme	nucleocytoplasmic	440:456	arg1	ncOGT					475:479	ncOGT	475:479	ncOGT	475:479	We have identified two nucleocytoplasmic isoforms of OGT (ncOGT and sOGT) and one isoform that localizes to the mitochondria (mOGT).
16434389	8	63	theme	OGT	1345:1347	arg1	utility					1322:1328	the potential utility	1308:1328	the potential utility of recombinant OGT in identifying new targets	1308:1374	Our findings demonstrate the potential utility of recombinant OGT in identifying new targets and illustrate the necessity to examine all active isoforms of the enzyme.
16434389	5	64	gly	glycosylated	978:989	arg1	proteins					928:935	some substrate proteins	913:935	some substrate proteins	913:935	We demonstrate that some substrate proteins, such as Nup62 and casein kinase II, are glycosylated by both ncOGT and mOGT, while others such as O-GlcNAcase and tau are specifically modified by ncOGT.
16434389	5	64	gly	glycosylated	978:989	arg1	Nup62					946:950	Nup62	946:950	Nup62	946:950	We demonstrate that some substrate proteins, such as Nup62 and casein kinase II, are glycosylated by both ncOGT and mOGT, while others such as O-GlcNAcase and tau are specifically modified by ncOGT.
16434389	5	64	gly	glycosylated	978:989	arg1	kinase					963:968	casein kinase II	956:971	casein kinase II	956:971	We demonstrate that some substrate proteins, such as Nup62 and casein kinase II, are glycosylated by both ncOGT and mOGT, while others such as O-GlcNAcase and tau are specifically modified by ncOGT.
16434389	3	65	theme	enzyme	699:704	arg1	N-terminus					680:689	the N-terminus	676:689	the N-terminus of each enzyme	676:704	These three isoforms contain identical catalytic regions but differ in the number of tetratricopeptide repeat motifs found at the N-terminus of each enzyme.
16434389	3	66	located	found	667:671	arg2	motifs					660:665	tetratricopeptide repeat motifs	635:665	tetratricopeptide repeat motifs found at the N-terminus of each enzyme	635:704	These three isoforms contain identical catalytic regions but differ in the number of tetratricopeptide repeat motifs found at the N-terminus of each enzyme.
16434389	3	66	located	found	667:671	arg1	N-terminus					680:689	the N-terminus	676:689	the N-terminus of each enzyme	676:704	These three isoforms contain identical catalytic regions but differ in the number of tetratricopeptide repeat motifs found at the N-terminus of each enzyme.
16434389	9	67	theme	OGT	1549:1551	arg1	participation					1553:1565	OGT participation	1549:1565	OGT participation in numerous signal transduction cascades	1549:1606	The identification of a tyrosine kinase and O-GlcNAcase as OGT targets suggests the potential for OGT participation in numerous signal transduction cascades.
9756352	0	0	theme	recycling	89:97	arg1	dysfunction					99:109	synaptic vesicle recycling dysfunction	72:109	synaptic vesicle recycling dysfunction	72:109	Reduced O-glycosylated clathrin assembly protein AP180: implication for synaptic vesicle recycling dysfunction in Alzheimer's disease.
9756352	5	1	theme	synaptophysin	811:823	arg1	loss					803:806	a small loss	795:806	a small loss of synaptophysin	795:823	Furthermore, whereas the level of neurofilament (NF-M) remains relatively unchanged, another clathrin assembly protein, AP-2, is also reduced in AD along with a small loss of synaptophysin.
9756352	1	2	theme	crucial	223:229	arg1	role					231:234	a crucial role	221:234	a crucial role	221:234	Synapse loss is one of the neuropathologies in Alzheimer's disease (AD) that may play a crucial role in the mechanism of its distinct cognitive impairment and dementia.
9756352	0	3	theme	vesicle	81:87	arg1	dysfunction					99:109	synaptic vesicle recycling dysfunction	72:109	synaptic vesicle recycling dysfunction	72:109	Reduced O-glycosylated clathrin assembly protein AP180: implication for synaptic vesicle recycling dysfunction in Alzheimer's disease.
9756352	5	4	theme	neurofilament	670:682	arg1	level					661:665	the level	657:665	the level of neurofilament (NF-M)	657:689	Furthermore, whereas the level of neurofilament (NF-M) remains relatively unchanged, another clathrin assembly protein, AP-2, is also reduced in AD along with a small loss of synaptophysin.
9756352	2	5	gly	O-glycosylated	357:370	arg1	protein					390:396	O-glycosylated clathrin assembly protein AP180	357:402	O-glycosylated clathrin assembly protein AP180	357:402	In a previous study [18], a significant reduction of O-glycosylated clathrin assembly protein AP180 was observed in neocortex of AD.
9756352	4	6	theme	protein	611:617	arg1	level					596:600	the level	592:600	the level of AP180 protein	592:617	In this study we further determine that the O-GlcNAc/AP180 ratio is not changed, but the level of AP180 protein decreases in AD.
9756352	0	7	from	implication	56:66	arg1	disease					126:132	Alzheimer's disease	114:132	Alzheimer's disease	114:132	Reduced O-glycosylated clathrin assembly protein AP180: implication for synaptic vesicle recycling dysfunction in Alzheimer's disease.
9756352	4	8	theme	O-GlcNAc/AP180	551:564	arg1	ratio					566:570	the O-GlcNAc/AP180 ratio	547:570	the O-GlcNAc/AP180 ratio	547:570	In this study we further determine that the O-GlcNAc/AP180 ratio is not changed, but the level of AP180 protein decreases in AD.
9756352	6	9	from	pathology	914:922	arg1	AD					943:944	AD	943:944	AD	943:944	Our findings suggest that synaptic vesicle recycling dysfunction may be involved in the pathology of synapse loss in AD.
9756352	3	10	theme	tangles	498:504	arg1	density					471:477	the density	467:477	the density of neurofibrillary tangles	467:504	The reduction correlated with the density of neurofibrillary tangles.
9756352	1	11	theme	neuropathologies	162:177	arg1	one					151:153	one	151:153	one	151:153	Synapse loss is one of the neuropathologies in Alzheimer's disease (AD) that may play a crucial role in the mechanism of its distinct cognitive impairment and dementia.
9756352	1	11	theme	neuropathologies	162:177	arg1	neuropathologies					162:177	the neuropathologies	158:177	the neuropathologies in Alzheimer's disease (AD)	158:205	Synapse loss is one of the neuropathologies in Alzheimer's disease (AD) that may play a crucial role in the mechanism of its distinct cognitive impairment and dementia.
9756352	6	12	theme	synapse	927:933	arg1	loss					935:938	synapse loss	927:938	synapse loss	927:938	Our findings suggest that synaptic vesicle recycling dysfunction may be involved in the pathology of synapse loss in AD.
9756352	2	13	located	observed	408:415	arg1	neocortex					420:428	neocortex	420:428	neocortex of AD	420:434	In a previous study [18], a significant reduction of O-glycosylated clathrin assembly protein AP180 was observed in neocortex of AD.
9756352	2	13	located	observed	408:415	arg1	study					318:322	a previous study [18]	307:327	a previous study [18]	307:327	In a previous study [18], a significant reduction of O-glycosylated clathrin assembly protein AP180 was observed in neocortex of AD.
9756352	2	13	located	observed	408:415	arg2	reduction					344:352	a significant reduction	330:352	a significant reduction of O-glycosylated clathrin assembly protein AP180	330:402	In a previous study [18], a significant reduction of O-glycosylated clathrin assembly protein AP180 was observed in neocortex of AD.
9756352	0	14	theme	O-glycosylated	8:21	arg1	AP180					49:53	Reduced O-glycosylated clathrin assembly protein AP180	0:53	Reduced O-glycosylated clathrin assembly protein AP180: implication for synaptic vesicle recycling dysfunction in Alzheimer's disease.	0:133	Reduced O-glycosylated clathrin assembly protein AP180: implication for synaptic vesicle recycling dysfunction in Alzheimer's disease.
9756352	2	15	theme	significant	332:342	arg1	reduction					344:352	a significant reduction	330:352	a significant reduction of O-glycosylated clathrin assembly protein AP180	330:402	In a previous study [18], a significant reduction of O-glycosylated clathrin assembly protein AP180 was observed in neocortex of AD.
9756352	0	16	theme	Reduced	0:6	arg1	AP180					49:53	Reduced O-glycosylated clathrin assembly protein AP180	0:53	Reduced O-glycosylated clathrin assembly protein AP180: implication for synaptic vesicle recycling dysfunction in Alzheimer's disease.	0:133	Reduced O-glycosylated clathrin assembly protein AP180: implication for synaptic vesicle recycling dysfunction in Alzheimer's disease.
9756352	6	17	theme	synaptic	852:859	arg1	dysfunction					879:889	synaptic vesicle recycling dysfunction	852:889	synaptic vesicle recycling dysfunction	852:889	Our findings suggest that synaptic vesicle recycling dysfunction may be involved in the pathology of synapse loss in AD.
9756352	5	18	theme	small	797:801	arg1	loss					803:806	a small loss	795:806	a small loss of synaptophysin	795:823	Furthermore, whereas the level of neurofilament (NF-M) remains relatively unchanged, another clathrin assembly protein, AP-2, is also reduced in AD along with a small loss of synaptophysin.
9756352	0	19	theme	assembly	32:39	arg1	AP180					49:53	Reduced O-glycosylated clathrin assembly protein AP180	0:53	Reduced O-glycosylated clathrin assembly protein AP180: implication for synaptic vesicle recycling dysfunction in Alzheimer's disease.	0:133	Reduced O-glycosylated clathrin assembly protein AP180: implication for synaptic vesicle recycling dysfunction in Alzheimer's disease.
9756352	6	20	theme	loss	935:938	arg1	pathology					914:922	the pathology	910:922	the pathology of synapse loss in AD	910:944	Our findings suggest that synaptic vesicle recycling dysfunction may be involved in the pathology of synapse loss in AD.
9756352	2	21	theme	protein	390:396	arg1	reduction					344:352	a significant reduction	330:352	a significant reduction of O-glycosylated clathrin assembly protein AP180	330:402	In a previous study [18], a significant reduction of O-glycosylated clathrin assembly protein AP180 was observed in neocortex of AD.
9756352	0	22	theme	clathrin	23:30	arg1	AP180					49:53	Reduced O-glycosylated clathrin assembly protein AP180	0:53	Reduced O-glycosylated clathrin assembly protein AP180: implication for synaptic vesicle recycling dysfunction in Alzheimer's disease.	0:133	Reduced O-glycosylated clathrin assembly protein AP180: implication for synaptic vesicle recycling dysfunction in Alzheimer's disease.
9756352	2	23	theme	assembly	381:388	arg1	protein					390:396	O-glycosylated clathrin assembly protein AP180	357:402	O-glycosylated clathrin assembly protein AP180	357:402	In a previous study [18], a significant reduction of O-glycosylated clathrin assembly protein AP180 was observed in neocortex of AD.
9756352	1	24	theme	distinct	260:267	arg1	impairment					279:288	its distinct cognitive impairment	256:288	its distinct cognitive impairment	256:288	Synapse loss is one of the neuropathologies in Alzheimer's disease (AD) that may play a crucial role in the mechanism of its distinct cognitive impairment and dementia.
9756352	2	25	theme	clathrin	372:379	arg1	protein					390:396	O-glycosylated clathrin assembly protein AP180	357:402	O-glycosylated clathrin assembly protein AP180	357:402	In a previous study [18], a significant reduction of O-glycosylated clathrin assembly protein AP180 was observed in neocortex of AD.
9756352	0	26	theme	protein	41:47	arg1	AP180					49:53	Reduced O-glycosylated clathrin assembly protein AP180	0:53	Reduced O-glycosylated clathrin assembly protein AP180: implication for synaptic vesicle recycling dysfunction in Alzheimer's disease.	0:133	Reduced O-glycosylated clathrin assembly protein AP180: implication for synaptic vesicle recycling dysfunction in Alzheimer's disease.
9756352	1	27	theme	cognitive	269:277	arg1	impairment					279:288	its distinct cognitive impairment	256:288	its distinct cognitive impairment	256:288	Synapse loss is one of the neuropathologies in Alzheimer's disease (AD) that may play a crucial role in the mechanism of its distinct cognitive impairment and dementia.
9756352	2	28	theme	AD	433:434	arg1	neocortex					420:428	neocortex	420:428	neocortex of AD	420:434	In a previous study [18], a significant reduction of O-glycosylated clathrin assembly protein AP180 was observed in neocortex of AD.
9756352	0	29	gly	O-glycosylated	8:21	arg1	AP180					49:53	Reduced O-glycosylated clathrin assembly protein AP180	0:53	Reduced O-glycosylated clathrin assembly protein AP180: implication for synaptic vesicle recycling dysfunction in Alzheimer's disease.	0:133	Reduced O-glycosylated clathrin assembly protein AP180: implication for synaptic vesicle recycling dysfunction in Alzheimer's disease.
9756352	2	30	theme	O-glycosylated	357:370	arg1	protein					390:396	O-glycosylated clathrin assembly protein AP180	357:402	O-glycosylated clathrin assembly protein AP180	357:402	In a previous study [18], a significant reduction of O-glycosylated clathrin assembly protein AP180 was observed in neocortex of AD.
9756352	5	31	theme	assembly	738:745	arg1	AP-2					756:759	AP-2	756:759	AP-2	756:759	Furthermore, whereas the level of neurofilament (NF-M) remains relatively unchanged, another clathrin assembly protein, AP-2, is also reduced in AD along with a small loss of synaptophysin.
9756352	5	31	theme	assembly	738:745	arg1	protein					747:753	another clathrin assembly protein	721:753	another clathrin assembly protein	721:753	Furthermore, whereas the level of neurofilament (NF-M) remains relatively unchanged, another clathrin assembly protein, AP-2, is also reduced in AD along with a small loss of synaptophysin.
9756352	1	32	theme	impairment	279:288	arg1	mechanism					243:251	the mechanism	239:251	the mechanism of its distinct cognitive impairment and dementia	239:301	Synapse loss is one of the neuropathologies in Alzheimer's disease (AD) that may play a crucial role in the mechanism of its distinct cognitive impairment and dementia.
9756352	0	33	dep	AP180	49:53	arg1	implication					56:66	implication	56:66	Reduced O-glycosylated clathrin assembly protein AP180: implication for synaptic vesicle recycling dysfunction in Alzheimer's disease.	0:133	Reduced O-glycosylated clathrin assembly protein AP180: implication for synaptic vesicle recycling dysfunction in Alzheimer's disease.
9756352	2	34	theme	previous	309:316	arg1	study					318:322	a previous study [18]	307:327	a previous study [18]	307:327	In a previous study [18], a significant reduction of O-glycosylated clathrin assembly protein AP180 was observed in neocortex of AD.
9756352	6	35	theme	vesicle	861:867	arg1	dysfunction					879:889	synaptic vesicle recycling dysfunction	852:889	synaptic vesicle recycling dysfunction	852:889	Our findings suggest that synaptic vesicle recycling dysfunction may be involved in the pathology of synapse loss in AD.
9756352	1	36	theme	dementia	294:301	arg1	mechanism					243:251	the mechanism	239:251	the mechanism of its distinct cognitive impairment and dementia	239:301	Synapse loss is one of the neuropathologies in Alzheimer's disease (AD) that may play a crucial role in the mechanism of its distinct cognitive impairment and dementia.
9756352	1	37	theme	Synapse	135:141	arg1	loss					143:146	Synapse loss	135:146	Synapse loss	135:146	Synapse loss is one of the neuropathologies in Alzheimer's disease (AD) that may play a crucial role in the mechanism of its distinct cognitive impairment and dementia.
9756352	0	38	theme	synaptic	72:79	arg1	dysfunction					99:109	synaptic vesicle recycling dysfunction	72:109	synaptic vesicle recycling dysfunction	72:109	Reduced O-glycosylated clathrin assembly protein AP180: implication for synaptic vesicle recycling dysfunction in Alzheimer's disease.
9756352	5	39	theme	clathrin	729:736	arg1	AP-2					756:759	AP-2	756:759	AP-2	756:759	Furthermore, whereas the level of neurofilament (NF-M) remains relatively unchanged, another clathrin assembly protein, AP-2, is also reduced in AD along with a small loss of synaptophysin.
9756352	5	39	theme	clathrin	729:736	arg1	protein					747:753	another clathrin assembly protein	721:753	another clathrin assembly protein	721:753	Furthermore, whereas the level of neurofilament (NF-M) remains relatively unchanged, another clathrin assembly protein, AP-2, is also reduced in AD along with a small loss of synaptophysin.
9756352	3	40	theme	neurofibrillary	482:496	arg1	tangles					498:504	neurofibrillary tangles	482:504	neurofibrillary tangles	482:504	The reduction correlated with the density of neurofibrillary tangles.
9756352	6	41	theme	recycling	869:877	arg1	dysfunction					879:889	synaptic vesicle recycling dysfunction	852:889	synaptic vesicle recycling dysfunction	852:889	Our findings suggest that synaptic vesicle recycling dysfunction may be involved in the pathology of synapse loss in AD.
27566657	7	0	theme	metastatic	1199:1208	arg1	CRC					1210:1212	metastatic CRC	1199:1212	metastatic CRC	1199:1212	Importantly, elevated aberrant O-GlcNAcylation of EV proteins might serve as a potential biomarker of metastatic CRC.
27566657	3	1	theme	gel	543:545	arg1	electrophoresis					547:561	two-dimensional gel electrophoresis	527:561	two-dimensional gel electrophoresis	527:561	MATERIALS AND METHODS To investigate whether extracellular vesicles (EVs) carry secretory O-GlcNAc-modified proteins that were isolated from colorectal cancer (CRC) cells, two-dimensional gel electrophoresis followed with O-GlcNAc immunoblotting and liquid chromatography-tandem mass spectrometry (LC-MS/MS) were applied.
27566657	0	2	theme	Cancer	94:99	arg1	Cells					101:105	Metastatic Colorectal Cancer Cells	72:105	Metastatic Colorectal Cancer Cells	72:105	Elevated O-GlcNAcylation of Extracellular Vesicle Proteins Derived from Metastatic Colorectal Cancer Cells.
27566657	1	3	attach	attachment	153:162	arg2	threonine					181:189	threonine	181:189	threonine	181:189	BACKGROUND O-GlcNAcylation is a single sugar attachment of serine and/or threonine residues on intracellular proteins.
27566657	1	3	attach	attachment	153:162	arg2	serine					167:172	serine	167:172	serine	167:172	BACKGROUND O-GlcNAcylation is a single sugar attachment of serine and/or threonine residues on intracellular proteins.
27566657	1	3	attach	attachment	153:162	arg3	proteins					217:224	intracellular proteins	203:224	intracellular proteins	203:224	BACKGROUND O-GlcNAcylation is a single sugar attachment of serine and/or threonine residues on intracellular proteins.
27566657	4	4	dep	RESULTS	677:683	arg1	revealed					692:699	revealed	692:699	was revealed that the O-GlcNAc modification of many EV proteins was increased in metastatic cells	688:784	RESULTS It was revealed that the O-GlcNAc modification of many EV proteins was increased in metastatic cells.
27566657	1	5	theme	threonine	181:189	arg1	attachment					153:162	a single sugar attachment	138:162	a single sugar attachment of serine and/or threonine residues on intracellular proteins	138:224	BACKGROUND O-GlcNAcylation is a single sugar attachment of serine and/or threonine residues on intracellular proteins.
27566657	1	5	theme	threonine	181:189	arg1	O-GlcNAcylation					119:133	BACKGROUND O-GlcNAcylation	108:133	BACKGROUND O-GlcNAcylation	108:133	BACKGROUND O-GlcNAcylation is a single sugar attachment of serine and/or threonine residues on intracellular proteins.
27566657	1	6	from	attachment	153:162	arg1	proteins					217:224	intracellular proteins	203:224	intracellular proteins	203:224	BACKGROUND O-GlcNAcylation is a single sugar attachment of serine and/or threonine residues on intracellular proteins.
27566657	3	7	contain	carry	429:433	arg2	proteins					463:470	secretory O-GlcNAc-modified proteins	435:470	secretory O-GlcNAc-modified proteins that were isolated from colorectal cancer (CRC) cells	435:524	MATERIALS AND METHODS To investigate whether extracellular vesicles (EVs) carry secretory O-GlcNAc-modified proteins that were isolated from colorectal cancer (CRC) cells, two-dimensional gel electrophoresis followed with O-GlcNAc immunoblotting and liquid chromatography-tandem mass spectrometry (LC-MS/MS) were applied.
27566657	3	7	contain	carry	429:433	arg1	EVs					424:426	EVs	424:426	EVs	424:426	MATERIALS AND METHODS To investigate whether extracellular vesicles (EVs) carry secretory O-GlcNAc-modified proteins that were isolated from colorectal cancer (CRC) cells, two-dimensional gel electrophoresis followed with O-GlcNAc immunoblotting and liquid chromatography-tandem mass spectrometry (LC-MS/MS) were applied.
27566657	3	7	contain	carry	429:433	arg1	vesicles					414:421	extracellular vesicles	400:421	extracellular vesicles (EVs)	400:427	MATERIALS AND METHODS To investigate whether extracellular vesicles (EVs) carry secretory O-GlcNAc-modified proteins that were isolated from colorectal cancer (CRC) cells, two-dimensional gel electrophoresis followed with O-GlcNAc immunoblotting and liquid chromatography-tandem mass spectrometry (LC-MS/MS) were applied.
27566657	2	8	theme	underlying	309:318	arg1	mechanisms					320:329	the underlying mechanisms	305:329	the underlying mechanisms	305:329	Recent reports reveal that it can modify several secretory proteins; however, the underlying mechanisms are largely unexplored.
27566657	3	9	theme	mass	634:637	arg1	LC-MS/MS					653:660	LC-MS/MS	653:660	LC-MS/MS	653:660	MATERIALS AND METHODS To investigate whether extracellular vesicles (EVs) carry secretory O-GlcNAc-modified proteins that were isolated from colorectal cancer (CRC) cells, two-dimensional gel electrophoresis followed with O-GlcNAc immunoblotting and liquid chromatography-tandem mass spectrometry (LC-MS/MS) were applied.
27566657	3	9	theme	mass	634:637	arg1	spectrometry					639:650	liquid chromatography-tandem mass spectrometry	605:650	liquid chromatography-tandem mass spectrometry (LC-MS/MS)	605:661	MATERIALS AND METHODS To investigate whether extracellular vesicles (EVs) carry secretory O-GlcNAc-modified proteins that were isolated from colorectal cancer (CRC) cells, two-dimensional gel electrophoresis followed with O-GlcNAc immunoblotting and liquid chromatography-tandem mass spectrometry (LC-MS/MS) were applied.
27566657	3	10	theme	extracellular	400:412	arg1	EVs					424:426	EVs	424:426	EVs	424:426	MATERIALS AND METHODS To investigate whether extracellular vesicles (EVs) carry secretory O-GlcNAc-modified proteins that were isolated from colorectal cancer (CRC) cells, two-dimensional gel electrophoresis followed with O-GlcNAc immunoblotting and liquid chromatography-tandem mass spectrometry (LC-MS/MS) were applied.
27566657	3	10	theme	extracellular	400:412	arg1	vesicles					414:421	extracellular vesicles	400:421	extracellular vesicles (EVs)	400:427	MATERIALS AND METHODS To investigate whether extracellular vesicles (EVs) carry secretory O-GlcNAc-modified proteins that were isolated from colorectal cancer (CRC) cells, two-dimensional gel electrophoresis followed with O-GlcNAc immunoblotting and liquid chromatography-tandem mass spectrometry (LC-MS/MS) were applied.
27566657	3	11	theme	liquid	605:610	arg1	LC-MS/MS					653:660	LC-MS/MS	653:660	LC-MS/MS	653:660	MATERIALS AND METHODS To investigate whether extracellular vesicles (EVs) carry secretory O-GlcNAc-modified proteins that were isolated from colorectal cancer (CRC) cells, two-dimensional gel electrophoresis followed with O-GlcNAc immunoblotting and liquid chromatography-tandem mass spectrometry (LC-MS/MS) were applied.
27566657	3	11	theme	liquid	605:610	arg1	spectrometry					639:650	liquid chromatography-tandem mass spectrometry	605:650	liquid chromatography-tandem mass spectrometry (LC-MS/MS)	605:661	MATERIALS AND METHODS To investigate whether extracellular vesicles (EVs) carry secretory O-GlcNAc-modified proteins that were isolated from colorectal cancer (CRC) cells, two-dimensional gel electrophoresis followed with O-GlcNAc immunoblotting and liquid chromatography-tandem mass spectrometry (LC-MS/MS) were applied.
27566657	5	12	theme	cell	999:1002	arg1	line					1004:1007	metastatic CRC cell line	984:1007	metastatic CRC cell line	984:1007	Among these, transitional endoplasmic reticulum ATPase (TER ATPase) and RuVB-like1 were successfully confirmed for the O-GlcNAc modification in which the levels were significantly higher in EVs of metastatic CRC cell line.
27566657	5	13	theme	transitional	800:811	arg1	reticulum					825:833	transitional endoplasmic reticulum	800:833	transitional endoplasmic reticulum ATPase (TER ATPase)	800:853	Among these, transitional endoplasmic reticulum ATPase (TER ATPase) and RuVB-like1 were successfully confirmed for the O-GlcNAc modification in which the levels were significantly higher in EVs of metastatic CRC cell line.
27566657	3	14	theme	O-GlcNAc	577:584	arg1	immunoblotting					586:599	O-GlcNAc immunoblotting	577:599	O-GlcNAc immunoblotting	577:599	MATERIALS AND METHODS To investigate whether extracellular vesicles (EVs) carry secretory O-GlcNAc-modified proteins that were isolated from colorectal cancer (CRC) cells, two-dimensional gel electrophoresis followed with O-GlcNAc immunoblotting and liquid chromatography-tandem mass spectrometry (LC-MS/MS) were applied.
27566657	4	15	theme	EV	740:741	arg1	proteins					743:750	many EV proteins	735:750	many EV proteins	735:750	RESULTS It was revealed that the O-GlcNAc modification of many EV proteins was increased in metastatic cells.
27566657	5	16	theme	endoplasmic	813:823	arg1	reticulum					825:833	transitional endoplasmic reticulum	800:833	transitional endoplasmic reticulum ATPase (TER ATPase)	800:853	Among these, transitional endoplasmic reticulum ATPase (TER ATPase) and RuVB-like1 were successfully confirmed for the O-GlcNAc modification in which the levels were significantly higher in EVs of metastatic CRC cell line.
27566657	3	17	theme	O-GlcNAc-modified	445:461	arg1	proteins					463:470	secretory O-GlcNAc-modified proteins	435:470	secretory O-GlcNAc-modified proteins that were isolated from colorectal cancer (CRC) cells	435:524	MATERIALS AND METHODS To investigate whether extracellular vesicles (EVs) carry secretory O-GlcNAc-modified proteins that were isolated from colorectal cancer (CRC) cells, two-dimensional gel electrophoresis followed with O-GlcNAc immunoblotting and liquid chromatography-tandem mass spectrometry (LC-MS/MS) were applied.
27566657	5	18	theme	TER	843:845	arg1	ATPase					835:840	transitional endoplasmic reticulum ATPase	800:840	transitional endoplasmic reticulum ATPase (TER ATPase)	800:853	Among these, transitional endoplasmic reticulum ATPase (TER ATPase) and RuVB-like1 were successfully confirmed for the O-GlcNAc modification in which the levels were significantly higher in EVs of metastatic CRC cell line.
27566657	5	18	theme	TER	843:845	arg1	ATPase					847:852	TER ATPase	843:852	TER ATPase	843:852	Among these, transitional endoplasmic reticulum ATPase (TER ATPase) and RuVB-like1 were successfully confirmed for the O-GlcNAc modification in which the levels were significantly higher in EVs of metastatic CRC cell line.
27566657	3	19	attach	isolated	482:489	arg2	proteins					463:470	secretory O-GlcNAc-modified proteins	435:470	secretory O-GlcNAc-modified proteins that were isolated from colorectal cancer (CRC) cells	435:524	MATERIALS AND METHODS To investigate whether extracellular vesicles (EVs) carry secretory O-GlcNAc-modified proteins that were isolated from colorectal cancer (CRC) cells, two-dimensional gel electrophoresis followed with O-GlcNAc immunoblotting and liquid chromatography-tandem mass spectrometry (LC-MS/MS) were applied.
27566657	3	19	attach	isolated	482:489	arg1	cells					520:524	colorectal cancer (CRC) cells	496:524	colorectal cancer (CRC) cells	496:524	MATERIALS AND METHODS To investigate whether extracellular vesicles (EVs) carry secretory O-GlcNAc-modified proteins that were isolated from colorectal cancer (CRC) cells, two-dimensional gel electrophoresis followed with O-GlcNAc immunoblotting and liquid chromatography-tandem mass spectrometry (LC-MS/MS) were applied.
27566657	5	20	theme	line	1004:1007	arg1	EVs					977:979	EVs	977:979	EVs of metastatic CRC cell line	977:1007	Among these, transitional endoplasmic reticulum ATPase (TER ATPase) and RuVB-like1 were successfully confirmed for the O-GlcNAc modification in which the levels were significantly higher in EVs of metastatic CRC cell line.
27566657	1	21	theme	intracellular	203:215	arg1	proteins					217:224	intracellular proteins	203:224	intracellular proteins	203:224	BACKGROUND O-GlcNAcylation is a single sugar attachment of serine and/or threonine residues on intracellular proteins.
27566657	0	22	theme	Elevated	0:7	arg1	O-GlcNAcylation					9:23	Elevated O-GlcNAcylation	0:23	Elevated O-GlcNAcylation of Extracellular Vesicle Proteins	0:57	Elevated O-GlcNAcylation of Extracellular Vesicle Proteins Derived from Metastatic Colorectal Cancer Cells.
27566657	1	23	theme	BACKGROUND	108:117	arg1	attachment					153:162	a single sugar attachment	138:162	a single sugar attachment of serine and/or threonine residues on intracellular proteins	138:224	BACKGROUND O-GlcNAcylation is a single sugar attachment of serine and/or threonine residues on intracellular proteins.
27566657	1	23	theme	BACKGROUND	108:117	arg1	O-GlcNAcylation					119:133	BACKGROUND O-GlcNAcylation	108:133	BACKGROUND O-GlcNAcylation	108:133	BACKGROUND O-GlcNAcylation is a single sugar attachment of serine and/or threonine residues on intracellular proteins.
27566657	4	24	theme	many	735:738	arg1	proteins					743:750	many EV proteins	735:750	many EV proteins	735:750	RESULTS It was revealed that the O-GlcNAc modification of many EV proteins was increased in metastatic cells.
27566657	0	25	theme	Extracellular	28:40	arg1	Proteins					50:57	Extracellular Vesicle Proteins	28:57	Extracellular Vesicle Proteins	28:57	Elevated O-GlcNAcylation of Extracellular Vesicle Proteins Derived from Metastatic Colorectal Cancer Cells.
27566657	7	26	theme	proteins	1150:1157	arg1	O-GlcNAcylation					1128:1142	elevated aberrant O-GlcNAcylation	1110:1142	elevated aberrant O-GlcNAcylation of EV proteins	1110:1157	Importantly, elevated aberrant O-GlcNAcylation of EV proteins might serve as a potential biomarker of metastatic CRC.
27566657	7	26	theme	proteins	1150:1157	arg1	biomarker					1186:1194	a potential biomarker	1174:1194	a potential biomarker of metastatic CRC	1174:1212	Importantly, elevated aberrant O-GlcNAcylation of EV proteins might serve as a potential biomarker of metastatic CRC.
27566657	3	27	theme	chromatography-tandem	612:632	arg1	LC-MS/MS					653:660	LC-MS/MS	653:660	LC-MS/MS	653:660	MATERIALS AND METHODS To investigate whether extracellular vesicles (EVs) carry secretory O-GlcNAc-modified proteins that were isolated from colorectal cancer (CRC) cells, two-dimensional gel electrophoresis followed with O-GlcNAc immunoblotting and liquid chromatography-tandem mass spectrometry (LC-MS/MS) were applied.
27566657	3	27	theme	chromatography-tandem	612:632	arg1	spectrometry					639:650	liquid chromatography-tandem mass spectrometry	605:650	liquid chromatography-tandem mass spectrometry (LC-MS/MS)	605:661	MATERIALS AND METHODS To investigate whether extracellular vesicles (EVs) carry secretory O-GlcNAc-modified proteins that were isolated from colorectal cancer (CRC) cells, two-dimensional gel electrophoresis followed with O-GlcNAc immunoblotting and liquid chromatography-tandem mass spectrometry (LC-MS/MS) were applied.
27566657	3	28	dep	MATERIALS	355:363	arg1	investigate					380:390	investigate	380:390	investigate	380:390	MATERIALS AND METHODS To investigate whether extracellular vesicles (EVs) carry secretory O-GlcNAc-modified proteins that were isolated from colorectal cancer (CRC) cells, two-dimensional gel electrophoresis followed with O-GlcNAc immunoblotting and liquid chromatography-tandem mass spectrometry (LC-MS/MS) were applied.
27566657	1	29	dep	serine	167:172	arg1	residues					191:198	residues	191:198	residues	191:198	BACKGROUND O-GlcNAcylation is a single sugar attachment of serine and/or threonine residues on intracellular proteins.
27566657	5	30	theme	O-GlcNAc	906:913	arg1	modification					915:926	the O-GlcNAc modification	902:926	the O-GlcNAc modification in which the levels were significantly higher in EVs of metastatic CRC cell line	902:1007	Among these, transitional endoplasmic reticulum ATPase (TER ATPase) and RuVB-like1 were successfully confirmed for the O-GlcNAc modification in which the levels were significantly higher in EVs of metastatic CRC cell line.
27566657	0	31	theme	Proteins	50:57	arg1	O-GlcNAcylation					9:23	Elevated O-GlcNAcylation	0:23	Elevated O-GlcNAcylation of Extracellular Vesicle Proteins	0:57	Elevated O-GlcNAcylation of Extracellular Vesicle Proteins Derived from Metastatic Colorectal Cancer Cells.
27566657	3	32	theme	two-dimensional	527:541	arg1	electrophoresis					547:561	two-dimensional gel electrophoresis	527:561	two-dimensional gel electrophoresis	527:561	MATERIALS AND METHODS To investigate whether extracellular vesicles (EVs) carry secretory O-GlcNAc-modified proteins that were isolated from colorectal cancer (CRC) cells, two-dimensional gel electrophoresis followed with O-GlcNAc immunoblotting and liquid chromatography-tandem mass spectrometry (LC-MS/MS) were applied.
27566657	4	33	theme	O-GlcNAc	710:717	arg1	modification					719:730	the O-GlcNAc modification	706:730	the O-GlcNAc modification of many EV proteins	706:750	RESULTS It was revealed that the O-GlcNAc modification of many EV proteins was increased in metastatic cells.
27566657	5	34	theme	reticulum	825:833	arg1	ATPase					835:840	transitional endoplasmic reticulum ATPase	800:840	transitional endoplasmic reticulum ATPase (TER ATPase)	800:853	Among these, transitional endoplasmic reticulum ATPase (TER ATPase) and RuVB-like1 were successfully confirmed for the O-GlcNAc modification in which the levels were significantly higher in EVs of metastatic CRC cell line.
27566657	5	34	theme	reticulum	825:833	arg1	ATPase					847:852	TER ATPase	843:852	TER ATPase	843:852	Among these, transitional endoplasmic reticulum ATPase (TER ATPase) and RuVB-like1 were successfully confirmed for the O-GlcNAc modification in which the levels were significantly higher in EVs of metastatic CRC cell line.
27566657	3	35	theme	colorectal	496:505	arg1	cancer					507:512	colorectal cancer	496:512	colorectal cancer (CRC) cells	496:524	MATERIALS AND METHODS To investigate whether extracellular vesicles (EVs) carry secretory O-GlcNAc-modified proteins that were isolated from colorectal cancer (CRC) cells, two-dimensional gel electrophoresis followed with O-GlcNAc immunoblotting and liquid chromatography-tandem mass spectrometry (LC-MS/MS) were applied.
27566657	3	35	theme	colorectal	496:505	arg1	CRC					515:517	CRC	515:517	CRC	515:517	MATERIALS AND METHODS To investigate whether extracellular vesicles (EVs) carry secretory O-GlcNAc-modified proteins that were isolated from colorectal cancer (CRC) cells, two-dimensional gel electrophoresis followed with O-GlcNAc immunoblotting and liquid chromatography-tandem mass spectrometry (LC-MS/MS) were applied.
27566657	0	36	theme	Vesicle	42:48	arg1	Proteins					50:57	Extracellular Vesicle Proteins	28:57	Extracellular Vesicle Proteins	28:57	Elevated O-GlcNAcylation of Extracellular Vesicle Proteins Derived from Metastatic Colorectal Cancer Cells.
27566657	7	37	theme	EV	1147:1148	arg1	proteins					1150:1157	EV proteins	1147:1157	EV proteins	1147:1157	Importantly, elevated aberrant O-GlcNAcylation of EV proteins might serve as a potential biomarker of metastatic CRC.
27566657	5	38	theme	metastatic	984:993	arg1	line					1004:1007	metastatic CRC cell line	984:1007	metastatic CRC cell line	984:1007	Among these, transitional endoplasmic reticulum ATPase (TER ATPase) and RuVB-like1 were successfully confirmed for the O-GlcNAc modification in which the levels were significantly higher in EVs of metastatic CRC cell line.
27566657	3	39	theme	cancer	507:512	arg1	cells					520:524	colorectal cancer (CRC) cells	496:524	colorectal cancer (CRC) cells	496:524	MATERIALS AND METHODS To investigate whether extracellular vesicles (EVs) carry secretory O-GlcNAc-modified proteins that were isolated from colorectal cancer (CRC) cells, two-dimensional gel electrophoresis followed with O-GlcNAc immunoblotting and liquid chromatography-tandem mass spectrometry (LC-MS/MS) were applied.
27566657	7	40	theme	CRC	1210:1212	arg1	O-GlcNAcylation					1128:1142	elevated aberrant O-GlcNAcylation	1110:1142	elevated aberrant O-GlcNAcylation of EV proteins	1110:1157	Importantly, elevated aberrant O-GlcNAcylation of EV proteins might serve as a potential biomarker of metastatic CRC.
27566657	7	40	theme	CRC	1210:1212	arg1	biomarker					1186:1194	a potential biomarker	1174:1194	a potential biomarker of metastatic CRC	1174:1212	Importantly, elevated aberrant O-GlcNAcylation of EV proteins might serve as a potential biomarker of metastatic CRC.
27566657	7	41	theme	aberrant	1119:1126	arg1	O-GlcNAcylation					1128:1142	elevated aberrant O-GlcNAcylation	1110:1142	elevated aberrant O-GlcNAcylation of EV proteins	1110:1157	Importantly, elevated aberrant O-GlcNAcylation of EV proteins might serve as a potential biomarker of metastatic CRC.
27566657	7	41	theme	aberrant	1119:1126	arg1	biomarker					1186:1194	a potential biomarker	1174:1194	a potential biomarker of metastatic CRC	1174:1212	Importantly, elevated aberrant O-GlcNAcylation of EV proteins might serve as a potential biomarker of metastatic CRC.
27566657	6	42	dep	CONCLUSION	1010:1019	arg1	demonstrate					1033:1043	demonstrate	1033:1043	demonstrate that proteins carried by EVs are O-GlcNAc-modified	1033:1094	CONCLUSION These data, demonstrate that proteins carried by EVs are O-GlcNAc-modified.
27566657	3	43	theme	secretory	435:443	arg1	proteins					463:470	secretory O-GlcNAc-modified proteins	435:470	secretory O-GlcNAc-modified proteins that were isolated from colorectal cancer (CRC) cells	435:524	MATERIALS AND METHODS To investigate whether extracellular vesicles (EVs) carry secretory O-GlcNAc-modified proteins that were isolated from colorectal cancer (CRC) cells, two-dimensional gel electrophoresis followed with O-GlcNAc immunoblotting and liquid chromatography-tandem mass spectrometry (LC-MS/MS) were applied.
27566657	3	44	dep	investigate	380:390	arg1	followed					563:570	followed	563:570	followed with O-GlcNAc immunoblotting and liquid chromatography-tandem mass spectrometry (LC-MS/MS)	563:661	MATERIALS AND METHODS To investigate whether extracellular vesicles (EVs) carry secretory O-GlcNAc-modified proteins that were isolated from colorectal cancer (CRC) cells, two-dimensional gel electrophoresis followed with O-GlcNAc immunoblotting and liquid chromatography-tandem mass spectrometry (LC-MS/MS) were applied.
27566657	7	45	theme	potential	1176:1184	arg1	O-GlcNAcylation					1128:1142	elevated aberrant O-GlcNAcylation	1110:1142	elevated aberrant O-GlcNAcylation of EV proteins	1110:1157	Importantly, elevated aberrant O-GlcNAcylation of EV proteins might serve as a potential biomarker of metastatic CRC.
27566657	7	45	theme	potential	1176:1184	arg1	biomarker					1186:1194	a potential biomarker	1174:1194	a potential biomarker of metastatic CRC	1174:1212	Importantly, elevated aberrant O-GlcNAcylation of EV proteins might serve as a potential biomarker of metastatic CRC.
27566657	1	46	theme	single	140:145	arg1	attachment					153:162	a single sugar attachment	138:162	a single sugar attachment of serine and/or threonine residues on intracellular proteins	138:224	BACKGROUND O-GlcNAcylation is a single sugar attachment of serine and/or threonine residues on intracellular proteins.
27566657	1	46	theme	single	140:145	arg1	O-GlcNAcylation					119:133	BACKGROUND O-GlcNAcylation	108:133	BACKGROUND O-GlcNAcylation	108:133	BACKGROUND O-GlcNAcylation is a single sugar attachment of serine and/or threonine residues on intracellular proteins.
27566657	1	47	theme	sugar	147:151	arg1	attachment					153:162	a single sugar attachment	138:162	a single sugar attachment of serine and/or threonine residues on intracellular proteins	138:224	BACKGROUND O-GlcNAcylation is a single sugar attachment of serine and/or threonine residues on intracellular proteins.
27566657	1	47	theme	sugar	147:151	arg1	O-GlcNAcylation					119:133	BACKGROUND O-GlcNAcylation	108:133	BACKGROUND O-GlcNAcylation	108:133	BACKGROUND O-GlcNAcylation is a single sugar attachment of serine and/or threonine residues on intracellular proteins.
27566657	7	48	theme	elevated	1110:1117	arg1	O-GlcNAcylation					1128:1142	elevated aberrant O-GlcNAcylation	1110:1142	elevated aberrant O-GlcNAcylation of EV proteins	1110:1157	Importantly, elevated aberrant O-GlcNAcylation of EV proteins might serve as a potential biomarker of metastatic CRC.
27566657	7	48	theme	elevated	1110:1117	arg1	biomarker					1186:1194	a potential biomarker	1174:1194	a potential biomarker of metastatic CRC	1174:1212	Importantly, elevated aberrant O-GlcNAcylation of EV proteins might serve as a potential biomarker of metastatic CRC.
27566657	2	49	theme	Recent	227:232	arg1	reports					234:240	Recent reports	227:240	Recent reports	227:240	Recent reports reveal that it can modify several secretory proteins; however, the underlying mechanisms are largely unexplored.
27566657	4	50	theme	proteins	743:750	arg1	modification					719:730	the O-GlcNAc modification	706:730	the O-GlcNAc modification of many EV proteins	706:750	RESULTS It was revealed that the O-GlcNAc modification of many EV proteins was increased in metastatic cells.
27566657	5	51	theme	CRC	995:997	arg1	line					1004:1007	metastatic CRC cell line	984:1007	metastatic CRC cell line	984:1007	Among these, transitional endoplasmic reticulum ATPase (TER ATPase) and RuVB-like1 were successfully confirmed for the O-GlcNAc modification in which the levels were significantly higher in EVs of metastatic CRC cell line.
27566657	0	52	theme	Colorectal	83:92	arg1	Cells					101:105	Metastatic Colorectal Cancer Cells	72:105	Metastatic Colorectal Cancer Cells	72:105	Elevated O-GlcNAcylation of Extracellular Vesicle Proteins Derived from Metastatic Colorectal Cancer Cells.
27566657	2	53	theme	secretory	276:284	arg1	proteins					286:293	several secretory proteins	268:293	several secretory proteins	268:293	Recent reports reveal that it can modify several secretory proteins; however, the underlying mechanisms are largely unexplored.
27566657	0	54	theme	Metastatic	72:81	arg1	Cells					101:105	Metastatic Colorectal Cancer Cells	72:105	Metastatic Colorectal Cancer Cells	72:105	Elevated O-GlcNAcylation of Extracellular Vesicle Proteins Derived from Metastatic Colorectal Cancer Cells.
27566657	2	55	theme	several	268:274	arg1	proteins					286:293	several secretory proteins	268:293	several secretory proteins	268:293	Recent reports reveal that it can modify several secretory proteins; however, the underlying mechanisms are largely unexplored.
27566657	1	56	theme	serine	167:172	arg1	attachment					153:162	a single sugar attachment	138:162	a single sugar attachment of serine and/or threonine residues on intracellular proteins	138:224	BACKGROUND O-GlcNAcylation is a single sugar attachment of serine and/or threonine residues on intracellular proteins.
27566657	1	56	theme	serine	167:172	arg1	O-GlcNAcylation					119:133	BACKGROUND O-GlcNAcylation	108:133	BACKGROUND O-GlcNAcylation	108:133	BACKGROUND O-GlcNAcylation is a single sugar attachment of serine and/or threonine residues on intracellular proteins.
27566657	4	57	theme	metastatic	769:778	arg1	cells					780:784	metastatic cells	769:784	metastatic cells	769:784	RESULTS It was revealed that the O-GlcNAc modification of many EV proteins was increased in metastatic cells.
26136220	0	0	theme	Cell	97:100	arg1	Secretion					102:110	Breast Cancer Cell Secretion	83:110	Breast Cancer Cell Secretion	83:110	Proteomic Analysis Reveals Aberrant O-GlcNAcylation of Extracellular Proteins from Breast Cancer Cell Secretion.
26136220	12	1	theme	O-GlcNAcomic	1577:1588	arg1	study					1590:1594	CONCLUSION O-GlcNAcomic study	1566:1594	CONCLUSION O-GlcNAcomic study of the extracellular compartments	1566:1628	CONCLUSION O-GlcNAcomic study of the extracellular compartments reveals aberrant O-GlcNAc-secreted proteins, which may be of interest as potential biomarkers in breast cancer.
26136220	2	2	from	O-GlcNAcylation	341:355	arg1	aberrant					329:336	aberrant	329:336	aberrant	329:336	We have previously demonstrated that many cellular proteins were aberrant in O-GlcNAcylation in breast cancer tissues.
26136220	10	3	theme	TER	1371:1373	arg1	ATPase					1363:1368	transitional endoplasmic reticulum ATPase	1328:1368	transitional endoplasmic reticulum ATPase (TER ATPase)	1328:1381	Among these, transitional endoplasmic reticulum ATPase (TER ATPase) and heat-shock 70 kDa (HSP70) were confirmed to be O-GlcNAc-modified.
26136220	10	3	theme	TER	1371:1373	arg1	ATPase					1375:1380	TER ATPase	1371:1380	TER ATPase	1371:1380	Among these, transitional endoplasmic reticulum ATPase (TER ATPase) and heat-shock 70 kDa (HSP70) were confirmed to be O-GlcNAc-modified.
26136220	0	4	theme	Cancer	90:95	arg1	Secretion					102:110	Breast Cancer Cell Secretion	83:110	Breast Cancer Cell Secretion	83:110	Proteomic Analysis Reveals Aberrant O-GlcNAcylation of Extracellular Proteins from Breast Cancer Cell Secretion.
26136220	11	5	theme	O-GlcNAc-TER	1486:1497	arg1	levels					1457:1462	The levels	1453:1462	The levels of O-GlcNAc-HSP70 and O-GlcNAc-TER ATPase	1453:1504	The levels of O-GlcNAc-HSP70 and O-GlcNAc-TER ATPase were higher in SFM from MCF-7 cells than in that from HMEC.
26136220	11	5	theme	O-GlcNAc-TER	1486:1497	arg1	higher					1511:1516	higher	1511:1516	higher	1511:1516	The levels of O-GlcNAc-HSP70 and O-GlcNAc-TER ATPase were higher in SFM from MCF-7 cells than in that from HMEC.
26136220	12	6	from	biomarkers	1713:1722	arg1	cancer					1734:1739	breast cancer	1727:1739	breast cancer	1727:1739	CONCLUSION O-GlcNAcomic study of the extracellular compartments reveals aberrant O-GlcNAc-secreted proteins, which may be of interest as potential biomarkers in breast cancer.
26136220	6	7	theme	Mass	915:918	arg1	Spectrometry					920:931	Liquid Chromatography-tandem Mass Spectrometry	886:931	Liquid Chromatography-tandem Mass Spectrometry	886:931	O-GlcNAc-Modified proteins were identified using two-dimensional gel electrophoresis and Liquid Chromatography-tandem Mass Spectrometry.
26136220	9	8	theme	many	1206:1209	arg1	spots					1220:1224	many O-GlcNAc spots	1206:1224	many O-GlcNAc spots in MCF-7 secretions	1206:1244	Proteomic analysis revealed that many O-GlcNAc spots in MCF-7 secretions were abnormally increased in comparison to those in HMEC secretions.
26136220	4	9	dep	MATERIALS	518:526	arg1	proteins					572:579	Intracellular and extracellular proteins	540:579	MATERIALS AND METHODS Intracellular and extracellular proteins	518:579	MATERIALS AND METHODS Intracellular and extracellular proteins were prepared from cell lysates of breast cancer cells (MCF-7 and MDA-MB-231) and normal breast cells (HMEC) and from their serum-free media (SFM), respectively.
26136220	11	10	dep	O-GlcNAc-HSP70	1467:1480	arg1	ATPase					1499:1504	ATPase	1499:1504	ATPase	1499:1504	The levels of O-GlcNAc-HSP70 and O-GlcNAc-TER ATPase were higher in SFM from MCF-7 cells than in that from HMEC.
26136220	2	11	from	tissues	374:380	arg1	aberrant					329:336	aberrant	329:336	aberrant	329:336	We have previously demonstrated that many cellular proteins were aberrant in O-GlcNAcylation in breast cancer tissues.
26136220	10	12	theme	heat-shock	1387:1396	arg1	kDa					1401:1403	heat-shock 70 kDa	1387:1403	heat-shock 70 kDa (HSP70)	1387:1411	Among these, transitional endoplasmic reticulum ATPase (TER ATPase) and heat-shock 70 kDa (HSP70) were confirmed to be O-GlcNAc-modified.
26136220	10	12	theme	heat-shock	1387:1396	arg1	HSP70					1406:1410	HSP70	1406:1410	HSP70	1406:1410	Among these, transitional endoplasmic reticulum ATPase (TER ATPase) and heat-shock 70 kDa (HSP70) were confirmed to be O-GlcNAc-modified.
26136220	7	13	theme	cancer	1042:1047	arg1	cells					1049:1053	cancer cells	1042:1053	cancer cells	1042:1053	RESULTS O-GlcNAcylation level was significantly increased in the extracellular compartment of both types of cancer cells compared to normal cells.
26136220	4	14	theme	Intracellular	540:552	arg1	proteins					572:579	Intracellular and extracellular proteins	540:579	MATERIALS AND METHODS Intracellular and extracellular proteins	518:579	MATERIALS AND METHODS Intracellular and extracellular proteins were prepared from cell lysates of breast cancer cells (MCF-7 and MDA-MB-231) and normal breast cells (HMEC) and from their serum-free media (SFM), respectively.
26136220	6	15	theme	Liquid	886:891	arg1	Spectrometry					920:931	Liquid Chromatography-tandem Mass Spectrometry	886:931	Liquid Chromatography-tandem Mass Spectrometry	886:931	O-GlcNAc-Modified proteins were identified using two-dimensional gel electrophoresis and Liquid Chromatography-tandem Mass Spectrometry.
26136220	8	16	theme	O-GlcNAc	1096:1103	arg1	patterns					1105:1112	O-GlcNAc patterns	1096:1112	O-GlcNAc patterns	1096:1112	Interestingly, O-GlcNAc patterns differed between intracellular and extracellular proteins.
26136220	10	17	theme	reticulum	1353:1361	arg1	ATPase					1363:1368	transitional endoplasmic reticulum ATPase	1328:1368	transitional endoplasmic reticulum ATPase (TER ATPase)	1328:1381	Among these, transitional endoplasmic reticulum ATPase (TER ATPase) and heat-shock 70 kDa (HSP70) were confirmed to be O-GlcNAc-modified.
26136220	10	17	theme	reticulum	1353:1361	arg1	ATPase					1375:1380	TER ATPase	1371:1380	TER ATPase	1371:1380	Among these, transitional endoplasmic reticulum ATPase (TER ATPase) and heat-shock 70 kDa (HSP70) were confirmed to be O-GlcNAc-modified.
26136220	3	18	theme	present	390:396	arg1	study					398:402	the present study	386:402	the present study	386:402	In the present study, therefore, we investigated whether O-GlcNAc-modified proteins were abnormally secreted from breast cancer cells.
26136220	3	19	theme	breast	497:502	arg1	cells					511:515	breast cancer cells	497:515	breast cancer cells	497:515	In the present study, therefore, we investigated whether O-GlcNAc-modified proteins were abnormally secreted from breast cancer cells.
26136220	10	20	theme	transitional	1328:1339	arg1	reticulum					1353:1361	transitional endoplasmic reticulum	1328:1361	transitional endoplasmic reticulum ATPase (TER ATPase)	1328:1381	Among these, transitional endoplasmic reticulum ATPase (TER ATPase) and heat-shock 70 kDa (HSP70) were confirmed to be O-GlcNAc-modified.
26136220	4	21	theme	extracellular	558:570	arg1	proteins					572:579	Intracellular and extracellular proteins	540:579	MATERIALS AND METHODS Intracellular and extracellular proteins	518:579	MATERIALS AND METHODS Intracellular and extracellular proteins were prepared from cell lysates of breast cancer cells (MCF-7 and MDA-MB-231) and normal breast cells (HMEC) and from their serum-free media (SFM), respectively.
26136220	8	22	theme	intracellular	1131:1143	arg1	proteins					1163:1170	intracellular and extracellular proteins	1131:1170	intracellular and extracellular proteins	1131:1170	Interestingly, O-GlcNAc patterns differed between intracellular and extracellular proteins.
26136220	4	23	theme	normal	663:668	arg1	HMEC					684:687	HMEC	684:687	HMEC	684:687	MATERIALS AND METHODS Intracellular and extracellular proteins were prepared from cell lysates of breast cancer cells (MCF-7 and MDA-MB-231) and normal breast cells (HMEC) and from their serum-free media (SFM), respectively.
26136220	4	23	theme	normal	663:668	arg1	cells					677:681	normal breast cells	663:681	normal breast cells (HMEC)	663:688	MATERIALS AND METHODS Intracellular and extracellular proteins were prepared from cell lysates of breast cancer cells (MCF-7 and MDA-MB-231) and normal breast cells (HMEC) and from their serum-free media (SFM), respectively.
26136220	9	24	theme	MCF-7	1229:1233	arg1	secretions					1235:1244	MCF-7 secretions	1229:1244	MCF-7 secretions	1229:1244	Proteomic analysis revealed that many O-GlcNAc spots in MCF-7 secretions were abnormally increased in comparison to those in HMEC secretions.
26136220	1	25	theme	few	197:199	arg1	proteins					233:240	few extracellular O-GlcNAc-modified proteins	197:240	few extracellular O-GlcNAc-modified proteins	197:240	BACKGROUND O-GlcNAcylation is a unique intracellular protein modification; however, few extracellular O-GlcNAc-modified proteins have been discovered.
26136220	7	26	theme	normal	1067:1072	arg1	cells					1074:1078	normal cells	1067:1078	normal cells	1067:1078	RESULTS O-GlcNAcylation level was significantly increased in the extracellular compartment of both types of cancer cells compared to normal cells.
26136220	0	27	from	O-GlcNAcylation	36:50	arg1	Secretion					102:110	Breast Cancer Cell Secretion	83:110	Breast Cancer Cell Secretion	83:110	Proteomic Analysis Reveals Aberrant O-GlcNAcylation of Extracellular Proteins from Breast Cancer Cell Secretion.
26136220	8	28	theme	extracellular	1149:1161	arg1	proteins					1163:1170	intracellular and extracellular proteins	1131:1170	intracellular and extracellular proteins	1131:1170	Interestingly, O-GlcNAc patterns differed between intracellular and extracellular proteins.
26136220	6	29	theme	gel	862:864	arg1	electrophoresis					866:880	two-dimensional gel electrophoresis	846:880	two-dimensional gel electrophoresis	846:880	O-GlcNAc-Modified proteins were identified using two-dimensional gel electrophoresis and Liquid Chromatography-tandem Mass Spectrometry.
26136220	2	30	theme	cancer	367:372	arg1	tissues					374:380	breast cancer tissues	360:380	breast cancer tissues	360:380	We have previously demonstrated that many cellular proteins were aberrant in O-GlcNAcylation in breast cancer tissues.
26136220	1	31	theme	extracellular	201:213	arg1	proteins					233:240	few extracellular O-GlcNAc-modified proteins	197:240	few extracellular O-GlcNAc-modified proteins	197:240	BACKGROUND O-GlcNAcylation is a unique intracellular protein modification; however, few extracellular O-GlcNAc-modified proteins have been discovered.
26136220	0	32	theme	Proteomic	0:8	arg1	Analysis					10:17	Proteomic Analysis	0:17	Proteomic Analysis	0:17	Proteomic Analysis Reveals Aberrant O-GlcNAcylation of Extracellular Proteins from Breast Cancer Cell Secretion.
26136220	4	33	theme	cells	630:634	arg1	lysates					605:611	cell lysates	600:611	cell lysates of breast cancer cells (MCF-7 and MDA-MB-231) and normal breast cells (HMEC)	600:688	MATERIALS AND METHODS Intracellular and extracellular proteins were prepared from cell lysates of breast cancer cells (MCF-7 and MDA-MB-231) and normal breast cells (HMEC) and from their serum-free media (SFM), respectively.
26136220	6	34	theme	two-dimensional	846:860	arg1	electrophoresis					866:880	two-dimensional gel electrophoresis	846:880	two-dimensional gel electrophoresis	846:880	O-GlcNAc-Modified proteins were identified using two-dimensional gel electrophoresis and Liquid Chromatography-tandem Mass Spectrometry.
26136220	2	35	theme	breast	360:365	arg1	tissues					374:380	breast cancer tissues	360:380	breast cancer tissues	360:380	We have previously demonstrated that many cellular proteins were aberrant in O-GlcNAcylation in breast cancer tissues.
26136220	7	36	theme	RESULTS	934:940	arg1	level					958:962	RESULTS O-GlcNAcylation level	934:962	RESULTS O-GlcNAcylation level	934:962	RESULTS O-GlcNAcylation level was significantly increased in the extracellular compartment of both types of cancer cells compared to normal cells.
26136220	1	37	theme	O-GlcNAc-modified	215:231	arg1	proteins					233:240	few extracellular O-GlcNAc-modified proteins	197:240	few extracellular O-GlcNAc-modified proteins	197:240	BACKGROUND O-GlcNAcylation is a unique intracellular protein modification; however, few extracellular O-GlcNAc-modified proteins have been discovered.
26136220	0	38	theme	Aberrant	27:34	arg1	O-GlcNAcylation					36:50	Aberrant O-GlcNAcylation	27:50	Aberrant O-GlcNAcylation of Extracellular Proteins from Breast Cancer Cell Secretion	27:110	Proteomic Analysis Reveals Aberrant O-GlcNAcylation of Extracellular Proteins from Breast Cancer Cell Secretion.
26136220	4	39	theme	cancer	623:628	arg1	cells					630:634	breast cancer cells	616:634	breast cancer cells (MCF-7 and MDA-MB-231)	616:657	MATERIALS AND METHODS Intracellular and extracellular proteins were prepared from cell lysates of breast cancer cells (MCF-7 and MDA-MB-231) and normal breast cells (HMEC) and from their serum-free media (SFM), respectively.
26136220	4	39	theme	cancer	623:628	arg1	MDA-MB-231					647:656	MDA-MB-231	647:656	MDA-MB-231	647:656	MATERIALS AND METHODS Intracellular and extracellular proteins were prepared from cell lysates of breast cancer cells (MCF-7 and MDA-MB-231) and normal breast cells (HMEC) and from their serum-free media (SFM), respectively.
26136220	4	39	theme	cancer	623:628	arg1	MCF-7					637:641	MCF-7	637:641	MCF-7	637:641	MATERIALS AND METHODS Intracellular and extracellular proteins were prepared from cell lysates of breast cancer cells (MCF-7 and MDA-MB-231) and normal breast cells (HMEC) and from their serum-free media (SFM), respectively.
26136220	7	40	theme	cells	1049:1053	arg1	types					1033:1037	both types	1028:1037	both types of cancer cells	1028:1053	RESULTS O-GlcNAcylation level was significantly increased in the extracellular compartment of both types of cancer cells compared to normal cells.
26136220	1	41	theme	BACKGROUND	113:122	arg1	modification					174:185	a unique intracellular protein modification	143:185	a unique intracellular protein modification	143:185	BACKGROUND O-GlcNAcylation is a unique intracellular protein modification; however, few extracellular O-GlcNAc-modified proteins have been discovered.
26136220	1	41	theme	BACKGROUND	113:122	arg1	O-GlcNAcylation					124:138	BACKGROUND O-GlcNAcylation	113:138	BACKGROUND O-GlcNAcylation	113:138	BACKGROUND O-GlcNAcylation is a unique intracellular protein modification; however, few extracellular O-GlcNAc-modified proteins have been discovered.
26136220	7	42	theme	O-GlcNAcylation	942:956	arg1	level					958:962	RESULTS O-GlcNAcylation level	934:962	RESULTS O-GlcNAcylation level	934:962	RESULTS O-GlcNAcylation level was significantly increased in the extracellular compartment of both types of cancer cells compared to normal cells.
26136220	5	43	theme	O-GlcNAcylation	743:757	arg1	level					759:763	O-GlcNAcylation level	743:763	O-GlcNAcylation level	743:763	O-GlcNAcylation level was examined by immunoblotting.
26136220	11	44	from	cells	1536:1540	arg1	SFM					1521:1523	SFM	1521:1523	SFM from MCF-7 cells	1521:1540	The levels of O-GlcNAc-HSP70 and O-GlcNAc-TER ATPase were higher in SFM from MCF-7 cells than in that from HMEC.
26136220	12	45	theme	potential	1703:1711	arg1	biomarkers					1713:1722	potential biomarkers	1703:1722	potential biomarkers in breast cancer	1703:1739	CONCLUSION O-GlcNAcomic study of the extracellular compartments reveals aberrant O-GlcNAc-secreted proteins, which may be of interest as potential biomarkers in breast cancer.
26136220	12	46	theme	O-GlcNAc-secreted	1647:1663	arg1	proteins					1665:1672	aberrant O-GlcNAc-secreted proteins	1638:1672	aberrant O-GlcNAc-secreted proteins	1638:1672	CONCLUSION O-GlcNAcomic study of the extracellular compartments reveals aberrant O-GlcNAc-secreted proteins, which may be of interest as potential biomarkers in breast cancer.
26136220	12	47	theme	breast	1727:1732	arg1	cancer					1734:1739	breast cancer	1727:1739	breast cancer	1727:1739	CONCLUSION O-GlcNAcomic study of the extracellular compartments reveals aberrant O-GlcNAc-secreted proteins, which may be of interest as potential biomarkers in breast cancer.
26136220	4	48	theme	serum-free	705:714	arg1	SFM					723:725	SFM	723:725	SFM	723:725	MATERIALS AND METHODS Intracellular and extracellular proteins were prepared from cell lysates of breast cancer cells (MCF-7 and MDA-MB-231) and normal breast cells (HMEC) and from their serum-free media (SFM), respectively.
26136220	4	48	theme	serum-free	705:714	arg1	media					716:720	their serum-free media	699:720	their serum-free media (SFM)	699:726	MATERIALS AND METHODS Intracellular and extracellular proteins were prepared from cell lysates of breast cancer cells (MCF-7 and MDA-MB-231) and normal breast cells (HMEC) and from their serum-free media (SFM), respectively.
26136220	12	49	theme	CONCLUSION	1566:1575	arg1	study					1590:1594	CONCLUSION O-GlcNAcomic study	1566:1594	CONCLUSION O-GlcNAcomic study of the extracellular compartments	1566:1628	CONCLUSION O-GlcNAcomic study of the extracellular compartments reveals aberrant O-GlcNAc-secreted proteins, which may be of interest as potential biomarkers in breast cancer.
26136220	0	50	theme	Proteins	69:76	arg1	O-GlcNAcylation					36:50	Aberrant O-GlcNAcylation	27:50	Aberrant O-GlcNAcylation of Extracellular Proteins from Breast Cancer Cell Secretion	27:110	Proteomic Analysis Reveals Aberrant O-GlcNAcylation of Extracellular Proteins from Breast Cancer Cell Secretion.
26136220	4	51	theme	cell	600:603	arg1	lysates					605:611	cell lysates	600:611	cell lysates of breast cancer cells (MCF-7 and MDA-MB-231) and normal breast cells (HMEC)	600:688	MATERIALS AND METHODS Intracellular and extracellular proteins were prepared from cell lysates of breast cancer cells (MCF-7 and MDA-MB-231) and normal breast cells (HMEC) and from their serum-free media (SFM), respectively.
26136220	11	52	theme	MCF-7	1530:1534	arg1	cells					1536:1540	MCF-7 cells	1530:1540	MCF-7 cells	1530:1540	The levels of O-GlcNAc-HSP70 and O-GlcNAc-TER ATPase were higher in SFM from MCF-7 cells than in that from HMEC.
26136220	4	53	dep	cells	630:634	arg1	cells					630:634	breast cancer cells	616:634	breast cancer cells (MCF-7 and MDA-MB-231)	616:657	MATERIALS AND METHODS Intracellular and extracellular proteins were prepared from cell lysates of breast cancer cells (MCF-7 and MDA-MB-231) and normal breast cells (HMEC) and from their serum-free media (SFM), respectively.
26136220	4	53	dep	cells	630:634	arg1	MDA-MB-231					647:656	MDA-MB-231	647:656	MDA-MB-231	647:656	MATERIALS AND METHODS Intracellular and extracellular proteins were prepared from cell lysates of breast cancer cells (MCF-7 and MDA-MB-231) and normal breast cells (HMEC) and from their serum-free media (SFM), respectively.
26136220	4	53	dep	cells	630:634	arg1	MCF-7					637:641	MCF-7	637:641	MCF-7	637:641	MATERIALS AND METHODS Intracellular and extracellular proteins were prepared from cell lysates of breast cancer cells (MCF-7 and MDA-MB-231) and normal breast cells (HMEC) and from their serum-free media (SFM), respectively.
26136220	0	54	theme	Extracellular	55:67	arg1	Proteins					69:76	Extracellular Proteins	55:76	Extracellular Proteins from Breast Cancer Cell Secretion	55:110	Proteomic Analysis Reveals Aberrant O-GlcNAcylation of Extracellular Proteins from Breast Cancer Cell Secretion.
26136220	4	55	theme	breast	616:621	arg1	cells					630:634	breast cancer cells	616:634	breast cancer cells (MCF-7 and MDA-MB-231)	616:657	MATERIALS AND METHODS Intracellular and extracellular proteins were prepared from cell lysates of breast cancer cells (MCF-7 and MDA-MB-231) and normal breast cells (HMEC) and from their serum-free media (SFM), respectively.
26136220	4	55	theme	breast	616:621	arg1	MDA-MB-231					647:656	MDA-MB-231	647:656	MDA-MB-231	647:656	MATERIALS AND METHODS Intracellular and extracellular proteins were prepared from cell lysates of breast cancer cells (MCF-7 and MDA-MB-231) and normal breast cells (HMEC) and from their serum-free media (SFM), respectively.
26136220	4	55	theme	breast	616:621	arg1	MCF-7					637:641	MCF-7	637:641	MCF-7	637:641	MATERIALS AND METHODS Intracellular and extracellular proteins were prepared from cell lysates of breast cancer cells (MCF-7 and MDA-MB-231) and normal breast cells (HMEC) and from their serum-free media (SFM), respectively.
26136220	12	56	theme	compartments	1617:1628	arg1	study					1590:1594	CONCLUSION O-GlcNAcomic study	1566:1594	CONCLUSION O-GlcNAcomic study of the extracellular compartments	1566:1628	CONCLUSION O-GlcNAcomic study of the extracellular compartments reveals aberrant O-GlcNAc-secreted proteins, which may be of interest as potential biomarkers in breast cancer.
26136220	11	57	theme	O-GlcNAc-HSP70	1467:1480	arg1	levels					1457:1462	The levels	1453:1462	The levels of O-GlcNAc-HSP70 and O-GlcNAc-TER ATPase	1453:1504	The levels of O-GlcNAc-HSP70 and O-GlcNAc-TER ATPase were higher in SFM from MCF-7 cells than in that from HMEC.
26136220	11	57	theme	O-GlcNAc-HSP70	1467:1480	arg1	higher					1511:1516	higher	1511:1516	higher	1511:1516	The levels of O-GlcNAc-HSP70 and O-GlcNAc-TER ATPase were higher in SFM from MCF-7 cells than in that from HMEC.
26136220	7	58	theme	types	1033:1037	arg1	compartment					1013:1023	the extracellular compartment	995:1023	the extracellular compartment of both types of cancer cells	995:1053	RESULTS O-GlcNAcylation level was significantly increased in the extracellular compartment of both types of cancer cells compared to normal cells.
26136220	9	59	theme	O-GlcNAc	1211:1218	arg1	spots					1220:1224	many O-GlcNAc spots	1206:1224	many O-GlcNAc spots in MCF-7 secretions	1206:1244	Proteomic analysis revealed that many O-GlcNAc spots in MCF-7 secretions were abnormally increased in comparison to those in HMEC secretions.
26136220	12	60	theme	extracellular	1603:1615	arg1	compartments					1617:1628	the extracellular compartments	1599:1628	the extracellular compartments	1599:1628	CONCLUSION O-GlcNAcomic study of the extracellular compartments reveals aberrant O-GlcNAc-secreted proteins, which may be of interest as potential biomarkers in breast cancer.
26136220	2	61	theme	cellular	306:313	arg1	proteins					315:322	many cellular proteins	301:322	many cellular proteins	301:322	We have previously demonstrated that many cellular proteins were aberrant in O-GlcNAcylation in breast cancer tissues.
26136220	6	62	theme	Chromatography-tandem	893:913	arg1	Spectrometry					920:931	Liquid Chromatography-tandem Mass Spectrometry	886:931	Liquid Chromatography-tandem Mass Spectrometry	886:931	O-GlcNAc-Modified proteins were identified using two-dimensional gel electrophoresis and Liquid Chromatography-tandem Mass Spectrometry.
26136220	1	63	theme	unique	145:150	arg1	modification					174:185	a unique intracellular protein modification	143:185	a unique intracellular protein modification	143:185	BACKGROUND O-GlcNAcylation is a unique intracellular protein modification; however, few extracellular O-GlcNAc-modified proteins have been discovered.
26136220	1	63	theme	unique	145:150	arg1	O-GlcNAcylation					124:138	BACKGROUND O-GlcNAcylation	113:138	BACKGROUND O-GlcNAcylation	113:138	BACKGROUND O-GlcNAcylation is a unique intracellular protein modification; however, few extracellular O-GlcNAc-modified proteins have been discovered.
26136220	4	64	theme	breast	670:675	arg1	HMEC					684:687	HMEC	684:687	HMEC	684:687	MATERIALS AND METHODS Intracellular and extracellular proteins were prepared from cell lysates of breast cancer cells (MCF-7 and MDA-MB-231) and normal breast cells (HMEC) and from their serum-free media (SFM), respectively.
26136220	4	64	theme	breast	670:675	arg1	cells					677:681	normal breast cells	663:681	normal breast cells (HMEC)	663:688	MATERIALS AND METHODS Intracellular and extracellular proteins were prepared from cell lysates of breast cancer cells (MCF-7 and MDA-MB-231) and normal breast cells (HMEC) and from their serum-free media (SFM), respectively.
26136220	6	65	theme	O-GlcNAc-Modified	797:813	arg1	proteins					815:822	O-GlcNAc-Modified proteins	797:822	O-GlcNAc-Modified proteins	797:822	O-GlcNAc-Modified proteins were identified using two-dimensional gel electrophoresis and Liquid Chromatography-tandem Mass Spectrometry.
26136220	12	66	theme	aberrant	1638:1645	arg1	proteins					1665:1672	aberrant O-GlcNAc-secreted proteins	1638:1672	aberrant O-GlcNAc-secreted proteins	1638:1672	CONCLUSION O-GlcNAcomic study of the extracellular compartments reveals aberrant O-GlcNAc-secreted proteins, which may be of interest as potential biomarkers in breast cancer.
26136220	2	67	theme	many	301:304	arg1	proteins					315:322	many cellular proteins	301:322	many cellular proteins	301:322	We have previously demonstrated that many cellular proteins were aberrant in O-GlcNAcylation in breast cancer tissues.
26136220	9	68	theme	HMEC	1298:1301	arg1	secretions					1303:1312	HMEC secretions	1298:1312	HMEC secretions	1298:1312	Proteomic analysis revealed that many O-GlcNAc spots in MCF-7 secretions were abnormally increased in comparison to those in HMEC secretions.
26136220	1	69	theme	intracellular	152:164	arg1	modification					174:185	a unique intracellular protein modification	143:185	a unique intracellular protein modification	143:185	BACKGROUND O-GlcNAcylation is a unique intracellular protein modification; however, few extracellular O-GlcNAc-modified proteins have been discovered.
26136220	1	69	theme	intracellular	152:164	arg1	O-GlcNAcylation					124:138	BACKGROUND O-GlcNAcylation	113:138	BACKGROUND O-GlcNAcylation	113:138	BACKGROUND O-GlcNAcylation is a unique intracellular protein modification; however, few extracellular O-GlcNAc-modified proteins have been discovered.
26136220	9	70	theme	Proteomic	1173:1181	arg1	analysis					1183:1190	Proteomic analysis	1173:1190	Proteomic analysis	1173:1190	Proteomic analysis revealed that many O-GlcNAc spots in MCF-7 secretions were abnormally increased in comparison to those in HMEC secretions.
26136220	3	71	theme	cancer	504:509	arg1	cells					511:515	breast cancer cells	497:515	breast cancer cells	497:515	In the present study, therefore, we investigated whether O-GlcNAc-modified proteins were abnormally secreted from breast cancer cells.
26136220	0	72	theme	Breast	83:88	arg1	Cancer					90:95	Breast Cancer	83:95	Breast Cancer Cell Secretion	83:110	Proteomic Analysis Reveals Aberrant O-GlcNAcylation of Extracellular Proteins from Breast Cancer Cell Secretion.
26136220	0	73	from	Secretion	102:110	arg1	O-GlcNAcylation					36:50	Aberrant O-GlcNAcylation	27:50	Aberrant O-GlcNAcylation of Extracellular Proteins from Breast Cancer Cell Secretion	27:110	Proteomic Analysis Reveals Aberrant O-GlcNAcylation of Extracellular Proteins from Breast Cancer Cell Secretion.
26136220	0	73	from	Secretion	102:110	arg1	Proteins					69:76	Extracellular Proteins	55:76	Extracellular Proteins from Breast Cancer Cell Secretion	55:110	Proteomic Analysis Reveals Aberrant O-GlcNAcylation of Extracellular Proteins from Breast Cancer Cell Secretion.
26136220	9	74	from	spots	1220:1224	arg1	secretions					1235:1244	MCF-7 secretions	1229:1244	MCF-7 secretions	1229:1244	Proteomic analysis revealed that many O-GlcNAc spots in MCF-7 secretions were abnormally increased in comparison to those in HMEC secretions.
26136220	1	75	theme	protein	166:172	arg1	modification					174:185	a unique intracellular protein modification	143:185	a unique intracellular protein modification	143:185	BACKGROUND O-GlcNAcylation is a unique intracellular protein modification; however, few extracellular O-GlcNAc-modified proteins have been discovered.
26136220	1	75	theme	protein	166:172	arg1	O-GlcNAcylation					124:138	BACKGROUND O-GlcNAcylation	113:138	BACKGROUND O-GlcNAcylation	113:138	BACKGROUND O-GlcNAcylation is a unique intracellular protein modification; however, few extracellular O-GlcNAc-modified proteins have been discovered.
26136220	2	76	from	aberrant	329:336	arg1	tissues					374:380	breast cancer tissues	360:380	breast cancer tissues	360:380	We have previously demonstrated that many cellular proteins were aberrant in O-GlcNAcylation in breast cancer tissues.
26136220	2	76	from	aberrant	329:336	arg1	O-GlcNAcylation					341:355	O-GlcNAcylation	341:355	O-GlcNAcylation	341:355	We have previously demonstrated that many cellular proteins were aberrant in O-GlcNAcylation in breast cancer tissues.
26136220	3	77	theme	O-GlcNAc-modified	440:456	arg1	proteins					458:465	O-GlcNAc-modified proteins	440:465	O-GlcNAc-modified proteins	440:465	In the present study, therefore, we investigated whether O-GlcNAc-modified proteins were abnormally secreted from breast cancer cells.
26136220	10	78	theme	endoplasmic	1341:1351	arg1	reticulum					1353:1361	transitional endoplasmic reticulum	1328:1361	transitional endoplasmic reticulum ATPase (TER ATPase)	1328:1381	Among these, transitional endoplasmic reticulum ATPase (TER ATPase) and heat-shock 70 kDa (HSP70) were confirmed to be O-GlcNAc-modified.
26136220	7	79	theme	extracellular	999:1011	arg1	compartment					1013:1023	the extracellular compartment	995:1023	the extracellular compartment of both types of cancer cells	995:1053	RESULTS O-GlcNAcylation level was significantly increased in the extracellular compartment of both types of cancer cells compared to normal cells.
26136220	4	80	theme	cells	677:681	arg1	lysates					605:611	cell lysates	600:611	cell lysates of breast cancer cells (MCF-7 and MDA-MB-231) and normal breast cells (HMEC)	600:688	MATERIALS AND METHODS Intracellular and extracellular proteins were prepared from cell lysates of breast cancer cells (MCF-7 and MDA-MB-231) and normal breast cells (HMEC) and from their serum-free media (SFM), respectively.
30725225	5	0	theme	nearby	728:733	arg1	phosphorylation					735:749	nearby phosphorylation	728:749	nearby phosphorylation	728:749	The study of the missing part showed that nearby phosphorylation affects the de-O-GlcNAcylation by OGA, but not to the same extent as it affects the O-GlcNAcylation by OGT.
30725225	6	1	theme	phosphorylation	868:882	arg1	processes					907:915	Both the phosphorylation and de-phosphorylation processes	859:915	processes	907:915	Both the phosphorylation and de-phosphorylation processes were only slightly affected by the presence of an O-GlcNAc residue on a nearby serine.
30725225	4	2	theme	cross	674:678	arg1	talk					680:683	the cross talk	670:683	the cross talk	670:683	However, studying the effects of kinases and OGT without the reverse processes catalyzed by phosphatases and O-GlcNAcase (OGA) does not provide a complete picture of the cross talk.
30725225	4	3	theme	reverse	565:571	arg1	processes					573:581	the reverse processes	561:581	the reverse processes catalyzed by phosphatases and O-GlcNAcase (OGA)	561:629	However, studying the effects of kinases and OGT without the reverse processes catalyzed by phosphatases and O-GlcNAcase (OGA) does not provide a complete picture of the cross talk.
30725225	0	4	theme	ZO-3-derived	54:65	arg1	peptide					67:73	a ZO-3-derived peptide	52:73	a ZO-3-derived peptide	52:73	Study of cross talk between phosphatases and OGA on a ZO-3-derived peptide.
30725225	6	5	from	residue	976:982	arg1	serine					996:1001	a nearby serine	987:1001	a nearby serine	987:1001	Both the phosphorylation and de-phosphorylation processes were only slightly affected by the presence of an O-GlcNAc residue on a nearby serine.
30725225	1	6	theme	posttranslational	138:154	arg1	O-GlcNAcylation					76:90	O-GlcNAcylation	76:90	O-GlcNAcylation	76:90	O-GlcNAcylation, like phosphorylation, is a dynamic and rapid posttranslational modification which regulates many cellular processes.
30725225	1	6	theme	posttranslational	138:154	arg1	modification					156:167	a dynamic and rapid posttranslational modification	118:167	a dynamic and rapid posttranslational modification which regulates many cellular processes	118:207	O-GlcNAcylation, like phosphorylation, is a dynamic and rapid posttranslational modification which regulates many cellular processes.
30725225	0	7	from	Study	0:4	arg1	peptide					67:73	a ZO-3-derived peptide	52:73	a ZO-3-derived peptide	52:73	Study of cross talk between phosphatases and OGA on a ZO-3-derived peptide.
30725225	3	8	theme	peptide	359:365	arg1	system					373:378	a peptide model system	357:378	a peptide model system based on the ZO-3 protein	357:404	Indeed, by using a microarray with a peptide model system based on the ZO-3 protein, extensive cross talk between O-GlcNAcylation by OGT and phosphorylation by kinases was observed.
30725225	0	9	link	ZO-3-derived	54:65	arg1	peptide					67:73	a ZO-3-derived peptide	52:73	a ZO-3-derived peptide	52:73	Study of cross talk between phosphatases and OGA on a ZO-3-derived peptide.
30725225	1	10	theme	rapid	132:136	arg1	O-GlcNAcylation					76:90	O-GlcNAcylation	76:90	O-GlcNAcylation	76:90	O-GlcNAcylation, like phosphorylation, is a dynamic and rapid posttranslational modification which regulates many cellular processes.
30725225	1	10	theme	rapid	132:136	arg1	modification					156:167	a dynamic and rapid posttranslational modification	118:167	a dynamic and rapid posttranslational modification which regulates many cellular processes	118:207	O-GlcNAcylation, like phosphorylation, is a dynamic and rapid posttranslational modification which regulates many cellular processes.
30725225	2	11	from	Phosphorylation	210:224	arg1	threonine					278:286	threonine	278:286	threonine	278:286	Phosphorylation on tyrosine and O-GlcNAcylation on nearby serine or threonine residues may modulate each other.
30725225	2	11	from	Phosphorylation	210:224	arg1	O-GlcNAcylation					242:256	O-GlcNAcylation	242:256	O-GlcNAcylation	242:256	Phosphorylation on tyrosine and O-GlcNAcylation on nearby serine or threonine residues may modulate each other.
30725225	2	11	from	Phosphorylation	210:224	arg1	serine					268:273	nearby serine	261:273	nearby serine	261:273	Phosphorylation on tyrosine and O-GlcNAcylation on nearby serine or threonine residues may modulate each other.
30725225	2	11	from	Phosphorylation	210:224	arg1	tyrosine					229:236	tyrosine	229:236	tyrosine	229:236	Phosphorylation on tyrosine and O-GlcNAcylation on nearby serine or threonine residues may modulate each other.
30725225	4	12	theme	complete	650:657	arg1	picture					659:665	a complete picture	648:665	a complete picture of the cross talk	648:683	However, studying the effects of kinases and OGT without the reverse processes catalyzed by phosphatases and O-GlcNAcase (OGA) does not provide a complete picture of the cross talk.
30725225	5	13	theme	part	711:714	arg1	study					690:694	The study	686:694	The study of the missing part	686:714	The study of the missing part showed that nearby phosphorylation affects the de-O-GlcNAcylation by OGA, but not to the same extent as it affects the O-GlcNAcylation by OGT.
30725225	6	14	theme	O-GlcNAc	967:974	arg1	residue					976:982	an O-GlcNAc residue	964:982	an O-GlcNAc residue on a nearby serine	964:1001	Both the phosphorylation and de-phosphorylation processes were only slightly affected by the presence of an O-GlcNAc residue on a nearby serine.
30725225	5	15	theme	missing	703:709	arg1	part					711:714	the missing part	699:714	the missing part	699:714	The study of the missing part showed that nearby phosphorylation affects the de-O-GlcNAcylation by OGA, but not to the same extent as it affects the O-GlcNAcylation by OGT.
30725225	6	16	from	serine	996:1001	arg1	presence					952:959	the presence	948:959	the presence of an O-GlcNAc residue on a nearby serine	948:1001	Both the phosphorylation and de-phosphorylation processes were only slightly affected by the presence of an O-GlcNAc residue on a nearby serine.
30725225	3	17	theme	extensive	407:415	arg1	talk					423:426	extensive cross talk	407:426	extensive cross talk between O-GlcNAcylation by OGT and phosphorylation by kinases	407:488	Indeed, by using a microarray with a peptide model system based on the ZO-3 protein, extensive cross talk between O-GlcNAcylation by OGT and phosphorylation by kinases was observed.
30725225	3	18	theme	cross	417:421	arg1	talk					423:426	extensive cross talk	407:426	extensive cross talk between O-GlcNAcylation by OGT and phosphorylation by kinases	407:488	Indeed, by using a microarray with a peptide model system based on the ZO-3 protein, extensive cross talk between O-GlcNAcylation by OGT and phosphorylation by kinases was observed.
30725225	3	19	theme	model	367:371	arg1	system					373:378	a peptide model system	357:378	a peptide model system based on the ZO-3 protein	357:404	Indeed, by using a microarray with a peptide model system based on the ZO-3 protein, extensive cross talk between O-GlcNAcylation by OGT and phosphorylation by kinases was observed.
30725225	4	20	theme	kinases	537:543	arg1	effects					526:532	the effects	522:532	the effects of kinases and OGT	522:551	However, studying the effects of kinases and OGT without the reverse processes catalyzed by phosphatases and O-GlcNAcase (OGA) does not provide a complete picture of the cross talk.
30725225	1	21	theme	cellular	190:197	arg1	processes					199:207	many cellular processes	185:207	many cellular processes	185:207	O-GlcNAcylation, like phosphorylation, is a dynamic and rapid posttranslational modification which regulates many cellular processes.
30725225	0	22	theme	cross	9:13	arg1	talk					15:18	cross talk	9:18	cross talk between phosphatases and OGA	9:47	Study of cross talk between phosphatases and OGA on a ZO-3-derived peptide.
30725225	4	23	theme	OGT	549:551	arg1	effects					526:532	the effects	522:532	the effects of kinases and OGT	522:551	However, studying the effects of kinases and OGT without the reverse processes catalyzed by phosphatases and O-GlcNAcase (OGA) does not provide a complete picture of the cross talk.
30725225	3	24	with	microarray	341:350	arg1	system					373:378	a peptide model system	357:378	a peptide model system based on the ZO-3 protein	357:404	Indeed, by using a microarray with a peptide model system based on the ZO-3 protein, extensive cross talk between O-GlcNAcylation by OGT and phosphorylation by kinases was observed.
30725225	2	25	dep	serine	268:273	arg1	residues					288:295	residues	288:295	residues	288:295	Phosphorylation on tyrosine and O-GlcNAcylation on nearby serine or threonine residues may modulate each other.
30725225	5	26	theme	same	805:808	arg1	extent					810:815	the same extent	801:815	the same extent	801:815	The study of the missing part showed that nearby phosphorylation affects the de-O-GlcNAcylation by OGA, but not to the same extent as it affects the O-GlcNAcylation by OGT.
30725225	0	27	theme	talk	15:18	arg1	Study					0:4	Study	0:4	Study of cross talk between phosphatases and OGA on a ZO-3-derived peptide.	0:74	Study of cross talk between phosphatases and OGA on a ZO-3-derived peptide.
30725225	1	28	theme	many	185:188	arg1	processes					199:207	many cellular processes	185:207	many cellular processes	185:207	O-GlcNAcylation, like phosphorylation, is a dynamic and rapid posttranslational modification which regulates many cellular processes.
30725225	3	29	theme	ZO-3	393:396	arg1	protein					398:404	the ZO-3 protein	389:404	the ZO-3 protein	389:404	Indeed, by using a microarray with a peptide model system based on the ZO-3 protein, extensive cross talk between O-GlcNAcylation by OGT and phosphorylation by kinases was observed.
30725225	6	30	from	presence	952:959	arg1	serine					996:1001	a nearby serine	987:1001	a nearby serine	987:1001	Both the phosphorylation and de-phosphorylation processes were only slightly affected by the presence of an O-GlcNAc residue on a nearby serine.
30725225	4	31	theme	talk	680:683	arg1	picture					659:665	a complete picture	648:665	a complete picture of the cross talk	648:683	However, studying the effects of kinases and OGT without the reverse processes catalyzed by phosphatases and O-GlcNAcase (OGA) does not provide a complete picture of the cross talk.
30725225	6	32	theme	de-phosphorylation	888:905	arg1	processes					907:915	Both the phosphorylation and de-phosphorylation processes	859:915	processes	907:915	Both the phosphorylation and de-phosphorylation processes were only slightly affected by the presence of an O-GlcNAc residue on a nearby serine.
30725225	6	33	theme	nearby	989:994	arg1	serine					996:1001	a nearby serine	987:1001	a nearby serine	987:1001	Both the phosphorylation and de-phosphorylation processes were only slightly affected by the presence of an O-GlcNAc residue on a nearby serine.
30725225	2	34	theme	nearby	261:266	arg1	serine					268:273	nearby serine	261:273	nearby serine	261:273	Phosphorylation on tyrosine and O-GlcNAcylation on nearby serine or threonine residues may modulate each other.
30725225	1	35	theme	dynamic	120:126	arg1	O-GlcNAcylation					76:90	O-GlcNAcylation	76:90	O-GlcNAcylation	76:90	O-GlcNAcylation, like phosphorylation, is a dynamic and rapid posttranslational modification which regulates many cellular processes.
30725225	1	35	theme	dynamic	120:126	arg1	modification					156:167	a dynamic and rapid posttranslational modification	118:167	a dynamic and rapid posttranslational modification which regulates many cellular processes	118:207	O-GlcNAcylation, like phosphorylation, is a dynamic and rapid posttranslational modification which regulates many cellular processes.
30725225	6	36	theme	residue	976:982	arg1	presence					952:959	the presence	948:959	the presence of an O-GlcNAc residue on a nearby serine	948:1001	Both the phosphorylation and de-phosphorylation processes were only slightly affected by the presence of an O-GlcNAc residue on a nearby serine.
17882263	7	0	theme	nuclear	1025:1031	arg1	translocation					1033:1045	nuclear translocation	1025:1045	nuclear translocation of the transcription factors NFkappaB and NFAT	1025:1092	Moreover, kinetic experiments show that O-GlcNAc modification prominently increased shortly after activation of lymphoid cells and it might be required for nuclear translocation of the transcription factors NFkappaB and NFAT.
17882263	4	1	theme	T-cell	623:628	arg1	activation					630:639	T-cell activation	623:639	T-cell activation	623:639	This results in a reduction of IL-2 production consistent with prevention of T-cell activation.
17882263	5	2	theme	B	691:691	arg1	cells					693:697	B cells	691:697	B cells	691:697	OGT is also required for the early activation of B cells mediated by stimulation of the B-cell receptor.
17882263	0	3	from	Requirement	0:10	arg1	lymphocytes					60:70	lymphocytes	60:70	lymphocytes	60:70	Requirement for O-linked N-acetylglucosaminyltransferase in lymphocytes activation.
17882263	5	4	theme	cells	693:697	arg1	activation					677:686	the early activation	667:686	the early activation of B cells mediated by stimulation of the B-cell receptor	667:744	OGT is also required for the early activation of B cells mediated by stimulation of the B-cell receptor.
17882263	0	5	link	O-linked	16:23	arg1	N-acetylglucosaminyltransferase					25:55	O-linked N-acetylglucosaminyltransferase	16:55	O-linked N-acetylglucosaminyltransferase	16:55	Requirement for O-linked N-acetylglucosaminyltransferase in lymphocytes activation.
17882263	3	6	dep	factors	519:525	arg1	factors					519:525	the transcription factors NFAT and NFkappaB	501:543	the transcription factors NFAT and NFkappaB	501:543	SiRNA-mediated knockdown of OGT in T cells leads to an impaired activation of the transcription factors NFAT and NFkappaB.
17882263	3	6	dep	factors	519:525	arg1	NFkappaB					536:543	NFkappaB	536:543	NFkappaB	536:543	SiRNA-mediated knockdown of OGT in T cells leads to an impaired activation of the transcription factors NFAT and NFkappaB.
17882263	3	6	dep	factors	519:525	arg1	NFAT					527:530	NFAT	527:530	NFAT	527:530	SiRNA-mediated knockdown of OGT in T cells leads to an impaired activation of the transcription factors NFAT and NFkappaB.
17882263	7	7	theme	O-GlcNAc	909:916	arg1	modification					918:929	O-GlcNAc modification	909:929	O-GlcNAc modification	909:929	Moreover, kinetic experiments show that O-GlcNAc modification prominently increased shortly after activation of lymphoid cells and it might be required for nuclear translocation of the transcription factors NFkappaB and NFAT.
17882263	1	8	theme	various	319:325	arg1	stimuli					327:333	various stimuli	319:333	various stimuli	319:333	The dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc) by the O-linked N-acetylglucosaminyltransferase (OGT) is a regulatory post-translational modification that is responsive to various stimuli.
17882263	1	9	theme	dynamic	88:94	arg1	modification					96:107	The dynamic modification	84:107	The dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc) by the O-linked N-acetylglucosaminyltransferase (OGT)	84:247	The dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc) by the O-linked N-acetylglucosaminyltransferase (OGT) is a regulatory post-translational modification that is responsive to various stimuli.
17882263	1	9	theme	dynamic	88:94	arg1	modification					284:295	a regulatory post-translational modification	252:295	a regulatory post-translational modification that is responsive to various stimuli	252:333	The dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc) by the O-linked N-acetylglucosaminyltransferase (OGT) is a regulatory post-translational modification that is responsive to various stimuli.
17882263	1	9	theme	dynamic	88:94	arg1	responsive					305:314	responsive	305:314	responsive	305:314	The dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc) by the O-linked N-acetylglucosaminyltransferase (OGT) is a regulatory post-translational modification that is responsive to various stimuli.
17882263	2	10	dep	T-	390:391	arg1	activation					411:420	activation	411:420	activation	411:420	Here, we demonstrate that OGT is a central factor for T- and B-lymphocytes activation.
17882263	4	11	theme	activation	630:639	arg1	prevention					609:618	prevention	609:618	prevention of T-cell activation	609:639	This results in a reduction of IL-2 production consistent with prevention of T-cell activation.
17882263	4	12	with	consistent	593:602	arg1	prevention					609:618	prevention	609:618	prevention of T-cell activation	609:639	This results in a reduction of IL-2 production consistent with prevention of T-cell activation.
17882263	1	13	theme	O-linked	202:209	arg1	OGT					244:246	OGT	244:246	OGT	244:246	The dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc) by the O-linked N-acetylglucosaminyltransferase (OGT) is a regulatory post-translational modification that is responsive to various stimuli.
17882263	1	13	theme	O-linked	202:209	arg1	N-acetylglucosaminyltransferase					211:241	the O-linked N-acetylglucosaminyltransferase	198:241	the O-linked N-acetylglucosaminyltransferase (OGT)	198:247	The dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc) by the O-linked N-acetylglucosaminyltransferase (OGT) is a regulatory post-translational modification that is responsive to various stimuli.
17882263	3	14	from	knockdown	438:446	arg1	cells					460:464	T cells	458:464	T cells	458:464	SiRNA-mediated knockdown of OGT in T cells leads to an impaired activation of the transcription factors NFAT and NFkappaB.
17882263	7	15	theme	cells	990:994	arg1	activation					967:976	activation	967:976	activation of lymphoid cells	967:994	Moreover, kinetic experiments show that O-GlcNAc modification prominently increased shortly after activation of lymphoid cells and it might be required for nuclear translocation of the transcription factors NFkappaB and NFAT.
17882263	7	16	dep	factors	1068:1074	arg1	factors					1068:1074	the transcription factors NFkappaB and NFAT	1050:1092	the transcription factors NFkappaB and NFAT	1050:1092	Moreover, kinetic experiments show that O-GlcNAc modification prominently increased shortly after activation of lymphoid cells and it might be required for nuclear translocation of the transcription factors NFkappaB and NFAT.
17882263	7	16	dep	factors	1068:1074	arg1	NFAT					1089:1092	NFAT	1089:1092	NFAT	1089:1092	Moreover, kinetic experiments show that O-GlcNAc modification prominently increased shortly after activation of lymphoid cells and it might be required for nuclear translocation of the transcription factors NFkappaB and NFAT.
17882263	7	16	dep	factors	1068:1074	arg1	NFkappaB					1076:1083	NFkappaB	1076:1083	NFkappaB	1076:1083	Moreover, kinetic experiments show that O-GlcNAc modification prominently increased shortly after activation of lymphoid cells and it might be required for nuclear translocation of the transcription factors NFkappaB and NFAT.
17882263	3	17	theme	impaired	478:485	arg1	activation					487:496	an impaired activation	475:496	an impaired activation of the transcription factors NFAT and NFkappaB	475:543	SiRNA-mediated knockdown of OGT in T cells leads to an impaired activation of the transcription factors NFAT and NFkappaB.
17882263	1	18	link	O-linked	202:209	arg1	OGT					244:246	OGT	244:246	OGT	244:246	The dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc) by the O-linked N-acetylglucosaminyltransferase (OGT) is a regulatory post-translational modification that is responsive to various stimuli.
17882263	1	18	link	O-linked	202:209	arg1	N-acetylglucosaminyltransferase					211:241	the O-linked N-acetylglucosaminyltransferase	198:241	the O-linked N-acetylglucosaminyltransferase (OGT)	198:247	The dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc) by the O-linked N-acetylglucosaminyltransferase (OGT) is a regulatory post-translational modification that is responsive to various stimuli.
17882263	6	19	gly	glycosylated	813:824	arg1	NFAT					804:807	NFAT	804:807	NFkappaB as well as NFAT	784:807	Mechanistically, we demonstrate that NFkappaB as well as NFAT are glycosylated with O-GlcNAc after direct binding to OGT.
17882263	6	19	gly	glycosylated	813:824	arg1	NFkappaB					784:791	NFkappaB	784:791	NFkappaB as well as NFAT	784:807	Mechanistically, we demonstrate that NFkappaB as well as NFAT are glycosylated with O-GlcNAc after direct binding to OGT.
17882263	1	20	theme	nuclear	112:118	arg1	proteins					136:143	nuclear and cytoplasmic proteins	112:143	nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc)	112:193	The dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc) by the O-linked N-acetylglucosaminyltransferase (OGT) is a regulatory post-translational modification that is responsive to various stimuli.
17882263	7	21	theme	kinetic	879:885	arg1	experiments					887:897	kinetic experiments	879:897	kinetic experiments	879:897	Moreover, kinetic experiments show that O-GlcNAc modification prominently increased shortly after activation of lymphoid cells and it might be required for nuclear translocation of the transcription factors NFkappaB and NFAT.
17882263	1	22	with	proteins	136:143	arg1	beta-N-acetylglucosamine					159:182	O-linked beta-N-acetylglucosamine	150:182	O-linked beta-N-acetylglucosamine (O-GlcNAc)	150:193	The dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc) by the O-linked N-acetylglucosaminyltransferase (OGT) is a regulatory post-translational modification that is responsive to various stimuli.
17882263	1	22	with	proteins	136:143	arg1	O-GlcNAc					185:192	O-GlcNAc	185:192	O-GlcNAc	185:192	The dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc) by the O-linked N-acetylglucosaminyltransferase (OGT) is a regulatory post-translational modification that is responsive to various stimuli.
17882263	4	23	theme	consistent	593:602	arg1	reduction					564:572	a reduction	562:572	a reduction of IL-2 production consistent with prevention of T-cell activation	562:639	This results in a reduction of IL-2 production consistent with prevention of T-cell activation.
17882263	4	24	theme	production	582:591	arg1	reduction					564:572	a reduction	562:572	a reduction of IL-2 production consistent with prevention of T-cell activation	562:639	This results in a reduction of IL-2 production consistent with prevention of T-cell activation.
17882263	5	25	theme	B-cell	730:735	arg1	receptor					737:744	the B-cell receptor	726:744	the B-cell receptor	726:744	OGT is also required for the early activation of B cells mediated by stimulation of the B-cell receptor.
17882263	7	26	theme	lymphoid	981:988	arg1	cells					990:994	lymphoid cells	981:994	lymphoid cells	981:994	Moreover, kinetic experiments show that O-GlcNAc modification prominently increased shortly after activation of lymphoid cells and it might be required for nuclear translocation of the transcription factors NFkappaB and NFAT.
17882263	1	27	theme	cytoplasmic	124:134	arg1	proteins					136:143	nuclear and cytoplasmic proteins	112:143	nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc)	112:193	The dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc) by the O-linked N-acetylglucosaminyltransferase (OGT) is a regulatory post-translational modification that is responsive to various stimuli.
17882263	0	28	theme	O-linked	16:23	arg1	N-acetylglucosaminyltransferase					25:55	O-linked N-acetylglucosaminyltransferase	16:55	O-linked N-acetylglucosaminyltransferase	16:55	Requirement for O-linked N-acetylglucosaminyltransferase in lymphocytes activation.
17882263	5	29	theme	receptor	737:744	arg1	stimulation					711:721	stimulation	711:721	stimulation of the B-cell receptor	711:744	OGT is also required for the early activation of B cells mediated by stimulation of the B-cell receptor.
17882263	1	30	theme	proteins	136:143	arg1	modification					96:107	The dynamic modification	84:107	The dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc) by the O-linked N-acetylglucosaminyltransferase (OGT)	84:247	The dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc) by the O-linked N-acetylglucosaminyltransferase (OGT) is a regulatory post-translational modification that is responsive to various stimuli.
17882263	1	30	theme	proteins	136:143	arg1	modification					284:295	a regulatory post-translational modification	252:295	a regulatory post-translational modification that is responsive to various stimuli	252:333	The dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc) by the O-linked N-acetylglucosaminyltransferase (OGT) is a regulatory post-translational modification that is responsive to various stimuli.
17882263	1	30	theme	proteins	136:143	arg1	responsive					305:314	responsive	305:314	responsive	305:314	The dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc) by the O-linked N-acetylglucosaminyltransferase (OGT) is a regulatory post-translational modification that is responsive to various stimuli.
17882263	3	31	theme	transcription	505:517	arg1	factors					519:525	the transcription factors NFAT and NFkappaB	501:543	the transcription factors NFAT and NFkappaB	501:543	SiRNA-mediated knockdown of OGT in T cells leads to an impaired activation of the transcription factors NFAT and NFkappaB.
17882263	3	31	theme	transcription	505:517	arg1	NFkappaB					536:543	NFkappaB	536:543	NFkappaB	536:543	SiRNA-mediated knockdown of OGT in T cells leads to an impaired activation of the transcription factors NFAT and NFkappaB.
17882263	3	31	theme	transcription	505:517	arg1	NFAT					527:530	NFAT	527:530	NFAT	527:530	SiRNA-mediated knockdown of OGT in T cells leads to an impaired activation of the transcription factors NFAT and NFkappaB.
17882263	3	32	theme	T	458:458	arg1	cells					460:464	T cells	458:464	T cells	458:464	SiRNA-mediated knockdown of OGT in T cells leads to an impaired activation of the transcription factors NFAT and NFkappaB.
17882263	5	33	theme	early	671:675	arg1	activation					677:686	the early activation	667:686	the early activation of B cells mediated by stimulation of the B-cell receptor	667:744	OGT is also required for the early activation of B cells mediated by stimulation of the B-cell receptor.
17882263	0	34	dep	activation	72:81	arg1	Requirement					0:10	Requirement	0:10	Requirement for O-linked N-acetylglucosaminyltransferase in lymphocytes	0:70	Requirement for O-linked N-acetylglucosaminyltransferase in lymphocytes activation.
17882263	7	35	theme	factors	1068:1074	arg1	translocation					1033:1045	nuclear translocation	1025:1045	nuclear translocation of the transcription factors NFkappaB and NFAT	1025:1092	Moreover, kinetic experiments show that O-GlcNAc modification prominently increased shortly after activation of lymphoid cells and it might be required for nuclear translocation of the transcription factors NFkappaB and NFAT.
17882263	1	36	theme	regulatory	254:263	arg1	modification					96:107	The dynamic modification	84:107	The dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc) by the O-linked N-acetylglucosaminyltransferase (OGT)	84:247	The dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc) by the O-linked N-acetylglucosaminyltransferase (OGT) is a regulatory post-translational modification that is responsive to various stimuli.
17882263	1	36	theme	regulatory	254:263	arg1	modification					284:295	a regulatory post-translational modification	252:295	a regulatory post-translational modification that is responsive to various stimuli	252:333	The dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc) by the O-linked N-acetylglucosaminyltransferase (OGT) is a regulatory post-translational modification that is responsive to various stimuli.
17882263	1	36	theme	regulatory	254:263	arg1	responsive					305:314	responsive	305:314	responsive	305:314	The dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc) by the O-linked N-acetylglucosaminyltransferase (OGT) is a regulatory post-translational modification that is responsive to various stimuli.
17882263	3	37	theme	OGT	451:453	arg1	knockdown					438:446	SiRNA-mediated knockdown	423:446	SiRNA-mediated knockdown of OGT in T cells	423:464	SiRNA-mediated knockdown of OGT in T cells leads to an impaired activation of the transcription factors NFAT and NFkappaB.
17882263	4	38	theme	IL-2	577:580	arg1	production					582:591	IL-2 production	577:591	IL-2 production	577:591	This results in a reduction of IL-2 production consistent with prevention of T-cell activation.
17882263	1	39	theme	O-linked	150:157	arg1	beta-N-acetylglucosamine					159:182	O-linked beta-N-acetylglucosamine	150:182	O-linked beta-N-acetylglucosamine (O-GlcNAc)	150:193	The dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc) by the O-linked N-acetylglucosaminyltransferase (OGT) is a regulatory post-translational modification that is responsive to various stimuli.
17882263	1	39	theme	O-linked	150:157	arg1	O-GlcNAc					185:192	O-GlcNAc	185:192	O-GlcNAc	185:192	The dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc) by the O-linked N-acetylglucosaminyltransferase (OGT) is a regulatory post-translational modification that is responsive to various stimuli.
17882263	6	40	theme	direct	846:851	arg1	binding					853:859	direct binding	846:859	direct binding to OGT	846:866	Mechanistically, we demonstrate that NFkappaB as well as NFAT are glycosylated with O-GlcNAc after direct binding to OGT.
17882263	2	41	theme	central	371:377	arg1	factor					379:384	a central factor	369:384	a central factor for T- and B-lymphocytes activation	369:420	Here, we demonstrate that OGT is a central factor for T- and B-lymphocytes activation.
17882263	2	41	theme	central	371:377	arg1	OGT					362:364	OGT	362:364	OGT	362:364	Here, we demonstrate that OGT is a central factor for T- and B-lymphocytes activation.
17882263	1	42	theme	post-translational	265:282	arg1	modification					96:107	The dynamic modification	84:107	The dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc) by the O-linked N-acetylglucosaminyltransferase (OGT)	84:247	The dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc) by the O-linked N-acetylglucosaminyltransferase (OGT) is a regulatory post-translational modification that is responsive to various stimuli.
17882263	1	42	theme	post-translational	265:282	arg1	modification					284:295	a regulatory post-translational modification	252:295	a regulatory post-translational modification that is responsive to various stimuli	252:333	The dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc) by the O-linked N-acetylglucosaminyltransferase (OGT) is a regulatory post-translational modification that is responsive to various stimuli.
17882263	1	42	theme	post-translational	265:282	arg1	responsive					305:314	responsive	305:314	responsive	305:314	The dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc) by the O-linked N-acetylglucosaminyltransferase (OGT) is a regulatory post-translational modification that is responsive to various stimuli.
17882263	1	43	link	O-linked	150:157	arg1	beta-N-acetylglucosamine					159:182	O-linked beta-N-acetylglucosamine	150:182	O-linked beta-N-acetylglucosamine (O-GlcNAc)	150:193	The dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc) by the O-linked N-acetylglucosaminyltransferase (OGT) is a regulatory post-translational modification that is responsive to various stimuli.
17882263	1	43	link	O-linked	150:157	arg1	O-GlcNAc					185:192	O-GlcNAc	185:192	O-GlcNAc	185:192	The dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc) by the O-linked N-acetylglucosaminyltransferase (OGT) is a regulatory post-translational modification that is responsive to various stimuli.
17882263	3	44	theme	factors	519:525	arg1	activation					487:496	an impaired activation	475:496	an impaired activation of the transcription factors NFAT and NFkappaB	475:543	SiRNA-mediated knockdown of OGT in T cells leads to an impaired activation of the transcription factors NFAT and NFkappaB.
17882263	7	45	theme	transcription	1054:1066	arg1	factors					1068:1074	the transcription factors NFkappaB and NFAT	1050:1092	the transcription factors NFkappaB and NFAT	1050:1092	Moreover, kinetic experiments show that O-GlcNAc modification prominently increased shortly after activation of lymphoid cells and it might be required for nuclear translocation of the transcription factors NFkappaB and NFAT.
17882263	7	45	theme	transcription	1054:1066	arg1	NFAT					1089:1092	NFAT	1089:1092	NFAT	1089:1092	Moreover, kinetic experiments show that O-GlcNAc modification prominently increased shortly after activation of lymphoid cells and it might be required for nuclear translocation of the transcription factors NFkappaB and NFAT.
17882263	7	45	theme	transcription	1054:1066	arg1	NFkappaB					1076:1083	NFkappaB	1076:1083	NFkappaB	1076:1083	Moreover, kinetic experiments show that O-GlcNAc modification prominently increased shortly after activation of lymphoid cells and it might be required for nuclear translocation of the transcription factors NFkappaB and NFAT.
17882263	3	46	theme	SiRNA-mediated	423:436	arg1	knockdown					438:446	SiRNA-mediated knockdown	423:446	SiRNA-mediated knockdown of OGT in T cells	423:464	SiRNA-mediated knockdown of OGT in T cells leads to an impaired activation of the transcription factors NFAT and NFkappaB.
29507186	8	0	theme	SNARE	1104:1108	arg1	formation					1118:1126	SNARE complex formation	1104:1126	SNARE complex formation	1104:1126	These findings reveal a mechanism by which low levels of arsenic perturb proteostasis through inhibition of SNARE complex formation, providing a possible therapeutic target for disease intervention in the more than 200 million people exposed to unsafe levels of arsenic.
29507186	7	1	theme	SNAP29	838:843	arg1	Transfection					776:787	Transfection	776:787	Transfection of O-GlcNAcylation-defective, but not wild-type, SNAP29 into clustered regularly interspaced short palindromic repeat (CRISPR)-mediated SNAP29 knockout cells	776:945	Transfection of O-GlcNAcylation-defective, but not wild-type, SNAP29 into clustered regularly interspaced short palindromic repeat (CRISPR)-mediated SNAP29 knockout cells abolishes arsenic-mediated autophagy inhibition.
29507186	8	2	theme	disease	1173:1179	arg1	intervention					1181:1192	disease intervention	1173:1192	disease intervention	1173:1192	These findings reveal a mechanism by which low levels of arsenic perturb proteostasis through inhibition of SNARE complex formation, providing a possible therapeutic target for disease intervention in the more than 200 million people exposed to unsafe levels of arsenic.
29507186	4	3	theme	autophagosome-lysosome	432:453	arg1	fusion					455:460	autophagosome-lysosome fusion	432:460	autophagosome-lysosome fusion	432:460	Here we show that arsenic blocks autophagy by preventing autophagosome-lysosome fusion.
29507186	7	4	theme	wild-type	827:835	arg1	SNAP29					838:843	O-GlcNAcylation-defective, but not wild-type, SNAP29	792:843	O-GlcNAcylation-defective, but not wild-type, SNAP29	792:843	Transfection of O-GlcNAcylation-defective, but not wild-type, SNAP29 into clustered regularly interspaced short palindromic repeat (CRISPR)-mediated SNAP29 knockout cells abolishes arsenic-mediated autophagy inhibition.
29507186	3	5	dep	low	329:331	arg1	relevant					350:357	relevant	350:357	relevant	350:357	Previously, we demonstrated that arsenic dysregulated the autophagy pathway at low, environmentally relevant concentrations.
29507186	7	6	theme	O-GlcNAcylation-defective	792:816	arg1	SNAP29					838:843	O-GlcNAcylation-defective, but not wild-type, SNAP29	792:843	O-GlcNAcylation-defective, but not wild-type, SNAP29	792:843	Transfection of O-GlcNAcylation-defective, but not wild-type, SNAP29 into clustered regularly interspaced short palindromic repeat (CRISPR)-mediated SNAP29 knockout cells abolishes arsenic-mediated autophagy inhibition.
29507186	1	7	theme	Environmental	83:95	arg1	exposure					97:104	Environmental exposure	83:104	Environmental exposure to arsenic	83:115	Environmental exposure to arsenic is linked to adverse health effects, including cancer and diabetes.
29507186	5	8	theme	vesicle	567:573	arg1	fusion					575:580	vesicle fusion	567:580	vesicle fusion	567:580	Specifically, arsenic disrupts formation of the STX17-SNAP29-VAMP8 SNARE complex, where SNAP29 mediates vesicle fusion through bridging STX17-containing autophagosomes to VAMP8-bearing lysosomes.
29507186	8	9	dep	people	1223:1228	arg1	million					1215:1221	million	1215:1221	million	1215:1221	These findings reveal a mechanism by which low levels of arsenic perturb proteostasis through inhibition of SNARE complex formation, providing a possible therapeutic target for disease intervention in the more than 200 million people exposed to unsafe levels of arsenic.
29507186	0	10	theme	Arsenic-Induced	43:57	arg1	Dysfunction					70:80	Arsenic-Induced Autophagic Dysfunction	43:80	Arsenic-Induced Autophagic Dysfunction	43:80	Increased O-GlcNAcylation of SNAP29 Drives Arsenic-Induced Autophagic Dysfunction.
29507186	8	11	theme	therapeutic	1150:1160	arg1	target					1162:1167	a possible therapeutic target	1139:1167	a possible therapeutic target for disease intervention	1139:1192	These findings reveal a mechanism by which low levels of arsenic perturb proteostasis through inhibition of SNARE complex formation, providing a possible therapeutic target for disease intervention in the more than 200 million people exposed to unsafe levels of arsenic.
29507186	8	12	theme	possible	1141:1148	arg1	target					1162:1167	a possible therapeutic target	1139:1167	a possible therapeutic target for disease intervention	1139:1192	These findings reveal a mechanism by which low levels of arsenic perturb proteostasis through inhibition of SNARE complex formation, providing a possible therapeutic target for disease intervention in the more than 200 million people exposed to unsafe levels of arsenic.
29507186	0	13	theme	Increased	0:8	arg1	O-GlcNAcylation					10:24	Increased O-GlcNAcylation	0:24	Increased O-GlcNAcylation of SNAP29	0:34	Increased O-GlcNAcylation of SNAP29 Drives Arsenic-Induced Autophagic Dysfunction.
29507186	7	14	theme	SNAP29	925:930	arg1	cells					941:945	clustered regularly interspaced short palindromic repeat (CRISPR)-mediated SNAP29 knockout cells	850:945	clustered regularly interspaced short palindromic repeat (CRISPR)-mediated SNAP29 knockout cells	850:945	Transfection of O-GlcNAcylation-defective, but not wild-type, SNAP29 into clustered regularly interspaced short palindromic repeat (CRISPR)-mediated SNAP29 knockout cells abolishes arsenic-mediated autophagy inhibition.
29507186	5	15	theme	complex	536:542	arg1	formation					494:502	formation	494:502	formation of the STX17-SNAP29-VAMP8 SNARE complex	494:542	Specifically, arsenic disrupts formation of the STX17-SNAP29-VAMP8 SNARE complex, where SNAP29 mediates vesicle fusion through bridging STX17-containing autophagosomes to VAMP8-bearing lysosomes.
29507186	0	16	theme	SNAP29	29:34	arg1	O-GlcNAcylation					10:24	Increased O-GlcNAcylation	0:24	Increased O-GlcNAcylation of SNAP29	0:34	Increased O-GlcNAcylation of SNAP29 Drives Arsenic-Induced Autophagic Dysfunction.
29507186	7	17	theme	knockout	932:939	arg1	cells					941:945	clustered regularly interspaced short palindromic repeat (CRISPR)-mediated SNAP29 knockout cells	850:945	clustered regularly interspaced short palindromic repeat (CRISPR)-mediated SNAP29 knockout cells	850:945	Transfection of O-GlcNAcylation-defective, but not wild-type, SNAP29 into clustered regularly interspaced short palindromic repeat (CRISPR)-mediated SNAP29 knockout cells abolishes arsenic-mediated autophagy inhibition.
29507186	3	18	theme	autophagy	308:316	arg1	pathway					318:324	the autophagy pathway	304:324	the autophagy pathway	304:324	Previously, we demonstrated that arsenic dysregulated the autophagy pathway at low, environmentally relevant concentrations.
29507186	7	19	theme	autophagy	974:982	arg1	inhibition					984:993	arsenic-mediated autophagy inhibition	957:993	arsenic-mediated autophagy inhibition	957:993	Transfection of O-GlcNAcylation-defective, but not wild-type, SNAP29 into clustered regularly interspaced short palindromic repeat (CRISPR)-mediated SNAP29 knockout cells abolishes arsenic-mediated autophagy inhibition.
29507186	6	20	theme	complex	699:705	arg1	formation					707:715	SNARE complex formation	693:715	SNARE complex formation	693:715	Mechanistically, arsenic inhibits SNARE complex formation, at least in part, by enhancing O-GlcNAcylation of SNAP29.
29507186	7	21	theme	arsenic-mediated	957:972	arg1	inhibition					984:993	arsenic-mediated autophagy inhibition	957:993	arsenic-mediated autophagy inhibition	957:993	Transfection of O-GlcNAcylation-defective, but not wild-type, SNAP29 into clustered regularly interspaced short palindromic repeat (CRISPR)-mediated SNAP29 knockout cells abolishes arsenic-mediated autophagy inhibition.
29507186	6	22	theme	SNARE	693:697	arg1	formation					707:715	SNARE complex formation	693:715	SNARE complex formation	693:715	Mechanistically, arsenic inhibits SNARE complex formation, at least in part, by enhancing O-GlcNAcylation of SNAP29.
29507186	7	23	theme	-mediated	915:923	arg1	cells					941:945	clustered regularly interspaced short palindromic repeat (CRISPR)-mediated SNAP29 knockout cells	850:945	clustered regularly interspaced short palindromic repeat (CRISPR)-mediated SNAP29 knockout cells	850:945	Transfection of O-GlcNAcylation-defective, but not wild-type, SNAP29 into clustered regularly interspaced short palindromic repeat (CRISPR)-mediated SNAP29 knockout cells abolishes arsenic-mediated autophagy inhibition.
29507186	8	24	theme	unsafe	1241:1246	arg1	levels					1248:1253	unsafe levels	1241:1253	unsafe levels of arsenic	1241:1264	These findings reveal a mechanism by which low levels of arsenic perturb proteostasis through inhibition of SNARE complex formation, providing a possible therapeutic target for disease intervention in the more than 200 million people exposed to unsafe levels of arsenic.
29507186	2	25	theme	cellular	197:204	arg1	effects					206:212	Pleiotropic cellular effects	185:212	Pleiotropic cellular effects	185:212	Pleiotropic cellular effects are observed with arsenic exposure.
29507186	6	26	theme	SNAP29	768:773	arg1	O-GlcNAcylation					749:763	O-GlcNAcylation	749:763	O-GlcNAcylation of SNAP29	749:773	Mechanistically, arsenic inhibits SNARE complex formation, at least in part, by enhancing O-GlcNAcylation of SNAP29.
29507186	2	27	theme	Pleiotropic	185:195	arg1	effects					206:212	Pleiotropic cellular effects	185:212	Pleiotropic cellular effects	185:212	Pleiotropic cellular effects are observed with arsenic exposure.
29507186	5	28	theme	VAMP8-bearing	634:646	arg1	lysosomes					648:656	VAMP8-bearing lysosomes	634:656	VAMP8-bearing lysosomes	634:656	Specifically, arsenic disrupts formation of the STX17-SNAP29-VAMP8 SNARE complex, where SNAP29 mediates vesicle fusion through bridging STX17-containing autophagosomes to VAMP8-bearing lysosomes.
29507186	8	29	theme	arsenic	1053:1059	arg1	levels					1043:1048	low levels	1039:1048	low levels of arsenic	1039:1059	These findings reveal a mechanism by which low levels of arsenic perturb proteostasis through inhibition of SNARE complex formation, providing a possible therapeutic target for disease intervention in the more than 200 million people exposed to unsafe levels of arsenic.
29507186	1	30	theme	adverse	130:136	arg1	effects					145:151	adverse health effects	130:151	adverse health effects	130:151	Environmental exposure to arsenic is linked to adverse health effects, including cancer and diabetes.
29507186	1	30	theme	adverse	130:136	arg1	cancer					164:169	cancer	164:169	cancer	164:169	Environmental exposure to arsenic is linked to adverse health effects, including cancer and diabetes.
29507186	1	30	theme	adverse	130:136	arg1	diabetes					175:182	diabetes	175:182	diabetes	175:182	Environmental exposure to arsenic is linked to adverse health effects, including cancer and diabetes.
29507186	0	31	theme	Autophagic	59:68	arg1	Dysfunction					70:80	Arsenic-Induced Autophagic Dysfunction	43:80	Arsenic-Induced Autophagic Dysfunction	43:80	Increased O-GlcNAcylation of SNAP29 Drives Arsenic-Induced Autophagic Dysfunction.
29507186	7	32	theme	palindromic	888:898	arg1	CRISPR					908:913	CRISPR	908:913	CRISPR	908:913	Transfection of O-GlcNAcylation-defective, but not wild-type, SNAP29 into clustered regularly interspaced short palindromic repeat (CRISPR)-mediated SNAP29 knockout cells abolishes arsenic-mediated autophagy inhibition.
29507186	7	32	theme	palindromic	888:898	arg1	repeat					900:905	clustered regularly interspaced short palindromic repeat	850:905	clustered regularly interspaced short palindromic repeat (CRISPR)	850:914	Transfection of O-GlcNAcylation-defective, but not wild-type, SNAP29 into clustered regularly interspaced short palindromic repeat (CRISPR)-mediated SNAP29 knockout cells abolishes arsenic-mediated autophagy inhibition.
29507186	2	33	theme	arsenic	232:238	arg1	exposure					240:247	arsenic exposure	232:247	arsenic exposure	232:247	Pleiotropic cellular effects are observed with arsenic exposure.
29507186	8	34	theme	low	1039:1041	arg1	levels					1043:1048	low levels	1039:1048	low levels of arsenic	1039:1059	These findings reveal a mechanism by which low levels of arsenic perturb proteostasis through inhibition of SNARE complex formation, providing a possible therapeutic target for disease intervention in the more than 200 million people exposed to unsafe levels of arsenic.
29507186	1	35	theme	health	138:143	arg1	effects					145:151	adverse health effects	130:151	adverse health effects	130:151	Environmental exposure to arsenic is linked to adverse health effects, including cancer and diabetes.
29507186	1	35	theme	health	138:143	arg1	cancer					164:169	cancer	164:169	cancer	164:169	Environmental exposure to arsenic is linked to adverse health effects, including cancer and diabetes.
29507186	1	35	theme	health	138:143	arg1	diabetes					175:182	diabetes	175:182	diabetes	175:182	Environmental exposure to arsenic is linked to adverse health effects, including cancer and diabetes.
29507186	1	36	attach	linked	120:125	arg1	effects					145:151	adverse health effects	130:151	adverse health effects	130:151	Environmental exposure to arsenic is linked to adverse health effects, including cancer and diabetes.
29507186	1	36	attach	linked	120:125	arg1	cancer					164:169	cancer	164:169	cancer	164:169	Environmental exposure to arsenic is linked to adverse health effects, including cancer and diabetes.
29507186	1	36	attach	linked	120:125	arg1	diabetes					175:182	diabetes	175:182	diabetes	175:182	Environmental exposure to arsenic is linked to adverse health effects, including cancer and diabetes.
29507186	1	36	attach	linked	120:125	arg2	exposure					97:104	Environmental exposure	83:104	Environmental exposure to arsenic	83:115	Environmental exposure to arsenic is linked to adverse health effects, including cancer and diabetes.
29507186	8	37	theme	formation	1118:1126	arg1	inhibition					1090:1099	inhibition	1090:1099	inhibition of SNARE complex formation	1090:1126	These findings reveal a mechanism by which low levels of arsenic perturb proteostasis through inhibition of SNARE complex formation, providing a possible therapeutic target for disease intervention in the more than 200 million people exposed to unsafe levels of arsenic.
29507186	7	38	theme	interspaced	870:880	arg1	CRISPR					908:913	CRISPR	908:913	CRISPR	908:913	Transfection of O-GlcNAcylation-defective, but not wild-type, SNAP29 into clustered regularly interspaced short palindromic repeat (CRISPR)-mediated SNAP29 knockout cells abolishes arsenic-mediated autophagy inhibition.
29507186	7	38	theme	interspaced	870:880	arg1	repeat					900:905	clustered regularly interspaced short palindromic repeat	850:905	clustered regularly interspaced short palindromic repeat (CRISPR)	850:914	Transfection of O-GlcNAcylation-defective, but not wild-type, SNAP29 into clustered regularly interspaced short palindromic repeat (CRISPR)-mediated SNAP29 knockout cells abolishes arsenic-mediated autophagy inhibition.
29507186	3	39	theme	low	329:331	arg1	concentrations					359:372	low, environmentally relevant concentrations	329:372	low, environmentally relevant concentrations	329:372	Previously, we demonstrated that arsenic dysregulated the autophagy pathway at low, environmentally relevant concentrations.
29507186	5	40	theme	STX17-SNAP29-VAMP8	511:528	arg1	complex					536:542	the STX17-SNAP29-VAMP8 SNARE complex	507:542	the STX17-SNAP29-VAMP8 SNARE complex	507:542	Specifically, arsenic disrupts formation of the STX17-SNAP29-VAMP8 SNARE complex, where SNAP29 mediates vesicle fusion through bridging STX17-containing autophagosomes to VAMP8-bearing lysosomes.
29507186	7	41	theme	short	882:886	arg1	CRISPR					908:913	CRISPR	908:913	CRISPR	908:913	Transfection of O-GlcNAcylation-defective, but not wild-type, SNAP29 into clustered regularly interspaced short palindromic repeat (CRISPR)-mediated SNAP29 knockout cells abolishes arsenic-mediated autophagy inhibition.
29507186	7	41	theme	short	882:886	arg1	repeat					900:905	clustered regularly interspaced short palindromic repeat	850:905	clustered regularly interspaced short palindromic repeat (CRISPR)	850:914	Transfection of O-GlcNAcylation-defective, but not wild-type, SNAP29 into clustered regularly interspaced short palindromic repeat (CRISPR)-mediated SNAP29 knockout cells abolishes arsenic-mediated autophagy inhibition.
29507186	8	42	dep	million	1215:1221	arg1	200					1211:1213	200	1211:1213	200	1211:1213	These findings reveal a mechanism by which low levels of arsenic perturb proteostasis through inhibition of SNARE complex formation, providing a possible therapeutic target for disease intervention in the more than 200 million people exposed to unsafe levels of arsenic.
29507186	5	43	theme	STX17-containing	599:614	arg1	autophagosomes					616:629	STX17-containing autophagosomes	599:629	STX17-containing autophagosomes	599:629	Specifically, arsenic disrupts formation of the STX17-SNAP29-VAMP8 SNARE complex, where SNAP29 mediates vesicle fusion through bridging STX17-containing autophagosomes to VAMP8-bearing lysosomes.
29507186	5	44	theme	SNARE	530:534	arg1	complex					536:542	the STX17-SNAP29-VAMP8 SNARE complex	507:542	the STX17-SNAP29-VAMP8 SNARE complex	507:542	Specifically, arsenic disrupts formation of the STX17-SNAP29-VAMP8 SNARE complex, where SNAP29 mediates vesicle fusion through bridging STX17-containing autophagosomes to VAMP8-bearing lysosomes.
29507186	7	45	theme	clustered	850:858	arg1	CRISPR					908:913	CRISPR	908:913	CRISPR	908:913	Transfection of O-GlcNAcylation-defective, but not wild-type, SNAP29 into clustered regularly interspaced short palindromic repeat (CRISPR)-mediated SNAP29 knockout cells abolishes arsenic-mediated autophagy inhibition.
29507186	7	45	theme	clustered	850:858	arg1	repeat					900:905	clustered regularly interspaced short palindromic repeat	850:905	clustered regularly interspaced short palindromic repeat (CRISPR)	850:914	Transfection of O-GlcNAcylation-defective, but not wild-type, SNAP29 into clustered regularly interspaced short palindromic repeat (CRISPR)-mediated SNAP29 knockout cells abolishes arsenic-mediated autophagy inhibition.
29507186	8	46	theme	complex	1110:1116	arg1	formation					1118:1126	SNARE complex formation	1104:1126	SNARE complex formation	1104:1126	These findings reveal a mechanism by which low levels of arsenic perturb proteostasis through inhibition of SNARE complex formation, providing a possible therapeutic target for disease intervention in the more than 200 million people exposed to unsafe levels of arsenic.
29507186	8	47	theme	arsenic	1258:1264	arg1	levels					1248:1253	unsafe levels	1241:1253	unsafe levels of arsenic	1241:1264	These findings reveal a mechanism by which low levels of arsenic perturb proteostasis through inhibition of SNARE complex formation, providing a possible therapeutic target for disease intervention in the more than 200 million people exposed to unsafe levels of arsenic.
31346222	2	0	theme	tie2-TNF-α	564:573	arg1	model					592:596	a tie2-TNF-α transgenic mouse model	562:596	a tie2-TNF-α transgenic mouse model	562:596	Previously we have shown that endothelial activation induced by inflammation and hyperglycemia results in the endoplasmic reticulum (ER) stress-mediated intercellular junction alterations accompanied by visual deficits in a tie2-TNF-α transgenic mouse model.
31346222	7	1	theme	endothelial	1338:1348	arg1	function					1358:1365	the endothelial barrier function	1334:1365	the endothelial barrier function	1334:1365	Our findings suggest an essential role for ER stress and O-GlcNAcylation in altering the endothelial barrier function and reveal a potential therapeutic target in the treatment of DR.
31346222	4	2	theme	endothelial	961:971	arg1	integrity					981:989	retinal endothelial barrier integrity	953:989	retinal endothelial barrier integrity	953:989	We show that ER stress leads to GRP78 translocation to the plasma membrane, increased O-GlcNAcylation of proteins, particularly VE-Cadherin resulting in a defective complex partnering leading to the loss of retinal endothelial barrier integrity and increased transendothelial migration of monocytes.
31346222	1	3	theme	post-translational	174:191	arg1	O-GlcNAcylation					144:158	Increased O-GlcNAcylation	134:158	Increased O-GlcNAcylation	134:158	Increased O-GlcNAcylation, a well-known post-translational modification of proteins causally linked to various detrimental cellular functions in pathological conditions including diabetic retinopathy (DR).
31346222	1	3	theme	post-translational	174:191	arg1	modification					193:204	a well-known post-translational modification	161:204	a well-known post-translational modification of proteins	161:216	Increased O-GlcNAcylation, a well-known post-translational modification of proteins causally linked to various detrimental cellular functions in pathological conditions including diabetic retinopathy (DR).
31346222	7	4	theme	barrier	1350:1356	arg1	function					1358:1365	the endothelial barrier function	1334:1365	the endothelial barrier function	1334:1365	Our findings suggest an essential role for ER stress and O-GlcNAcylation in altering the endothelial barrier function and reveal a potential therapeutic target in the treatment of DR.
31346222	4	5	theme	retinal	953:959	arg1	integrity					981:989	retinal endothelial barrier integrity	953:989	retinal endothelial barrier integrity	953:989	We show that ER stress leads to GRP78 translocation to the plasma membrane, increased O-GlcNAcylation of proteins, particularly VE-Cadherin resulting in a defective complex partnering leading to the loss of retinal endothelial barrier integrity and increased transendothelial migration of monocytes.
31346222	1	6	theme	diabetic	313:320	arg1	DR					335:336	DR	335:336	DR	335:336	Increased O-GlcNAcylation, a well-known post-translational modification of proteins causally linked to various detrimental cellular functions in pathological conditions including diabetic retinopathy (DR).
31346222	1	6	theme	diabetic	313:320	arg1	retinopathy					322:332	diabetic retinopathy	313:332	diabetic retinopathy (DR)	313:337	Increased O-GlcNAcylation, a well-known post-translational modification of proteins causally linked to various detrimental cellular functions in pathological conditions including diabetic retinopathy (DR).
31346222	0	7	theme	stress-mediated	92:106	arg1	permeability					120:131	ER stress-mediated endothelial permeability	89:131	ER stress-mediated endothelial permeability	89:131	GRP78 translocation to the cell surface and O-GlcNAcylation of VE-Cadherin contribute to ER stress-mediated endothelial permeability.
31346222	4	8	theme	integrity	981:989	arg1	loss					945:948	the loss	941:948	the loss of retinal endothelial barrier integrity	941:989	We show that ER stress leads to GRP78 translocation to the plasma membrane, increased O-GlcNAcylation of proteins, particularly VE-Cadherin resulting in a defective complex partnering leading to the loss of retinal endothelial barrier integrity and increased transendothelial migration of monocytes.
31346222	4	9	theme	proteins	851:858	arg1	migration					1022:1030	increased transendothelial migration	995:1030	increased transendothelial migration of monocytes	995:1043	We show that ER stress leads to GRP78 translocation to the plasma membrane, increased O-GlcNAcylation of proteins, particularly VE-Cadherin resulting in a defective complex partnering leading to the loss of retinal endothelial barrier integrity and increased transendothelial migration of monocytes.
31346222	4	9	theme	proteins	851:858	arg1	O-GlcNAcylation					832:846	increased O-GlcNAcylation	822:846	increased O-GlcNAcylation of proteins, particularly VE-Cadherin resulting in a defective complex partnering leading to the loss of retinal endothelial barrier integrity	822:989	We show that ER stress leads to GRP78 translocation to the plasma membrane, increased O-GlcNAcylation of proteins, particularly VE-Cadherin resulting in a defective complex partnering leading to the loss of retinal endothelial barrier integrity and increased transendothelial migration of monocytes.
31346222	4	9	theme	proteins	851:858	arg1	translocation					784:796	GRP78 translocation	778:796	GRP78 translocation to the plasma membrane	778:819	We show that ER stress leads to GRP78 translocation to the plasma membrane, increased O-GlcNAcylation of proteins, particularly VE-Cadherin resulting in a defective complex partnering leading to the loss of retinal endothelial barrier integrity and increased transendothelial migration of monocytes.
31346222	0	10	theme	ER	89:90	arg1	permeability					120:131	ER stress-mediated endothelial permeability	89:131	ER stress-mediated endothelial permeability	89:131	GRP78 translocation to the cell surface and O-GlcNAcylation of VE-Cadherin contribute to ER stress-mediated endothelial permeability.
31346222	4	11	theme	barrier	973:979	arg1	integrity					981:989	retinal endothelial barrier integrity	953:989	retinal endothelial barrier integrity	953:989	We show that ER stress leads to GRP78 translocation to the plasma membrane, increased O-GlcNAcylation of proteins, particularly VE-Cadherin resulting in a defective complex partnering leading to the loss of retinal endothelial barrier integrity and increased transendothelial migration of monocytes.
31346222	4	12	theme	GRP78	778:782	arg1	translocation					784:796	GRP78 translocation	778:796	GRP78 translocation to the plasma membrane	778:819	We show that ER stress leads to GRP78 translocation to the plasma membrane, increased O-GlcNAcylation of proteins, particularly VE-Cadherin resulting in a defective complex partnering leading to the loss of retinal endothelial barrier integrity and increased transendothelial migration of monocytes.
31346222	7	13	theme	ER	1292:1293	arg1	stress					1295:1300	ER stress	1292:1300	ER stress	1292:1300	Our findings suggest an essential role for ER stress and O-GlcNAcylation in altering the endothelial barrier function and reveal a potential therapeutic target in the treatment of DR.
31346222	6	14	theme	ER	1163:1164	arg1	inhibitor					1173:1181	ER stress inhibitor	1163:1181	ER stress inhibitor	1163:1181	Interestingly, cells exposed to ER stress inhibitor, tauroursodeoxycholic acid partially mitigated all these effects.
31346222	6	14	theme	ER	1163:1164	arg1	acid					1205:1208	tauroursodeoxycholic acid	1184:1208	tauroursodeoxycholic acid	1184:1208	Interestingly, cells exposed to ER stress inhibitor, tauroursodeoxycholic acid partially mitigated all these effects.
31346222	2	15	dep	results	435:441	arg1	accompanied					528:538	accompanied	528:538	accompanied by visual deficits in a tie2-TNF-α transgenic mouse model	528:596	Previously we have shown that endothelial activation induced by inflammation and hyperglycemia results in the endoplasmic reticulum (ER) stress-mediated intercellular junction alterations accompanied by visual deficits in a tie2-TNF-α transgenic mouse model.
31346222	2	16	theme	reticulum	462:470	arg1	alterations					516:526	the endoplasmic reticulum (ER) stress-mediated intercellular junction alterations	446:526	the endoplasmic reticulum (ER) stress-mediated intercellular junction alterations	446:526	Previously we have shown that endothelial activation induced by inflammation and hyperglycemia results in the endoplasmic reticulum (ER) stress-mediated intercellular junction alterations accompanied by visual deficits in a tie2-TNF-α transgenic mouse model.
31346222	0	17	theme	endothelial	108:118	arg1	permeability					120:131	ER stress-mediated endothelial permeability	89:131	ER stress-mediated endothelial permeability	89:131	GRP78 translocation to the cell surface and O-GlcNAcylation of VE-Cadherin contribute to ER stress-mediated endothelial permeability.
31346222	7	18	from	target	1402:1407	arg1	treatment					1416:1424	the treatment	1412:1424	the treatment of DR	1412:1430	Our findings suggest an essential role for ER stress and O-GlcNAcylation in altering the endothelial barrier function and reveal a potential therapeutic target in the treatment of DR.
31346222	5	19	with	association	1065:1075	arg1	VE-Cadherin					1095:1105	the VE-Cadherin	1091:1105	the VE-Cadherin	1091:1105	We further show an association of GRP78 with the VE-Cadherin under these conditions.
31346222	1	20	theme	proteins	209:216	arg1	O-GlcNAcylation					144:158	Increased O-GlcNAcylation	134:158	Increased O-GlcNAcylation	134:158	Increased O-GlcNAcylation, a well-known post-translational modification of proteins causally linked to various detrimental cellular functions in pathological conditions including diabetic retinopathy (DR).
31346222	1	20	theme	proteins	209:216	arg1	modification					193:204	a well-known post-translational modification	161:204	a well-known post-translational modification of proteins	161:216	Increased O-GlcNAcylation, a well-known post-translational modification of proteins causally linked to various detrimental cellular functions in pathological conditions including diabetic retinopathy (DR).
31346222	2	21	from	deficits	550:557	arg1	model					592:596	a tie2-TNF-α transgenic mouse model	562:596	a tie2-TNF-α transgenic mouse model	562:596	Previously we have shown that endothelial activation induced by inflammation and hyperglycemia results in the endoplasmic reticulum (ER) stress-mediated intercellular junction alterations accompanied by visual deficits in a tie2-TNF-α transgenic mouse model.
31346222	0	22	theme	VE-Cadherin	63:73	arg1	translocation					6:18	GRP78 translocation	0:18	GRP78 translocation to the cell surface	0:38	GRP78 translocation to the cell surface and O-GlcNAcylation of VE-Cadherin contribute to ER stress-mediated endothelial permeability.
31346222	0	22	theme	VE-Cadherin	63:73	arg1	O-GlcNAcylation					44:58	O-GlcNAcylation	44:58	O-GlcNAcylation of VE-Cadherin	44:73	GRP78 translocation to the cell surface and O-GlcNAcylation of VE-Cadherin contribute to ER stress-mediated endothelial permeability.
31346222	4	23	theme	ER	759:760	arg1	stress					762:767	ER stress	759:767	ER stress	759:767	We show that ER stress leads to GRP78 translocation to the plasma membrane, increased O-GlcNAcylation of proteins, particularly VE-Cadherin resulting in a defective complex partnering leading to the loss of retinal endothelial barrier integrity and increased transendothelial migration of monocytes.
31346222	0	24	theme	GRP78	0:4	arg1	translocation					6:18	GRP78 translocation	0:18	GRP78 translocation to the cell surface	0:38	GRP78 translocation to the cell surface and O-GlcNAcylation of VE-Cadherin contribute to ER stress-mediated endothelial permeability.
31346222	3	25	theme	increased	644:652	arg1	stress					657:662	increased ER stress	644:662	increased ER stress via O-GlcNAcylation of VE-Cadherin	644:697	In this study, we tested the hypothesis that increased ER stress via O-GlcNAcylation of VE-Cadherin likely contribute to endothelial permeability.
31346222	2	26	theme	junction	507:514	arg1	alterations					516:526	the endoplasmic reticulum (ER) stress-mediated intercellular junction alterations	446:526	the endoplasmic reticulum (ER) stress-mediated intercellular junction alterations	446:526	Previously we have shown that endothelial activation induced by inflammation and hyperglycemia results in the endoplasmic reticulum (ER) stress-mediated intercellular junction alterations accompanied by visual deficits in a tie2-TNF-α transgenic mouse model.
31346222	6	27	theme	tauroursodeoxycholic	1184:1203	arg1	inhibitor					1173:1181	ER stress inhibitor	1163:1181	ER stress inhibitor	1163:1181	Interestingly, cells exposed to ER stress inhibitor, tauroursodeoxycholic acid partially mitigated all these effects.
31346222	6	27	theme	tauroursodeoxycholic	1184:1203	arg1	acid					1205:1208	tauroursodeoxycholic acid	1184:1208	tauroursodeoxycholic acid	1184:1208	Interestingly, cells exposed to ER stress inhibitor, tauroursodeoxycholic acid partially mitigated all these effects.
31346222	4	28	theme	monocytes	1035:1043	arg1	migration					1022:1030	increased transendothelial migration	995:1030	increased transendothelial migration of monocytes	995:1043	We show that ER stress leads to GRP78 translocation to the plasma membrane, increased O-GlcNAcylation of proteins, particularly VE-Cadherin resulting in a defective complex partnering leading to the loss of retinal endothelial barrier integrity and increased transendothelial migration of monocytes.
31346222	4	28	theme	monocytes	1035:1043	arg1	O-GlcNAcylation					832:846	increased O-GlcNAcylation	822:846	increased O-GlcNAcylation of proteins, particularly VE-Cadherin resulting in a defective complex partnering leading to the loss of retinal endothelial barrier integrity	822:989	We show that ER stress leads to GRP78 translocation to the plasma membrane, increased O-GlcNAcylation of proteins, particularly VE-Cadherin resulting in a defective complex partnering leading to the loss of retinal endothelial barrier integrity and increased transendothelial migration of monocytes.
31346222	4	28	theme	monocytes	1035:1043	arg1	translocation					784:796	GRP78 translocation	778:796	GRP78 translocation to the plasma membrane	778:819	We show that ER stress leads to GRP78 translocation to the plasma membrane, increased O-GlcNAcylation of proteins, particularly VE-Cadherin resulting in a defective complex partnering leading to the loss of retinal endothelial barrier integrity and increased transendothelial migration of monocytes.
31346222	7	29	dep	potential	1380:1388	arg1	therapeutic					1390:1400	therapeutic	1390:1400	therapeutic	1390:1400	Our findings suggest an essential role for ER stress and O-GlcNAcylation in altering the endothelial barrier function and reveal a potential therapeutic target in the treatment of DR.
31346222	2	30	theme	stress-mediated	477:491	arg1	alterations					516:526	the endoplasmic reticulum (ER) stress-mediated intercellular junction alterations	446:526	the endoplasmic reticulum (ER) stress-mediated intercellular junction alterations	446:526	Previously we have shown that endothelial activation induced by inflammation and hyperglycemia results in the endoplasmic reticulum (ER) stress-mediated intercellular junction alterations accompanied by visual deficits in a tie2-TNF-α transgenic mouse model.
31346222	2	31	theme	intercellular	493:505	arg1	alterations					516:526	the endoplasmic reticulum (ER) stress-mediated intercellular junction alterations	446:526	the endoplasmic reticulum (ER) stress-mediated intercellular junction alterations	446:526	Previously we have shown that endothelial activation induced by inflammation and hyperglycemia results in the endoplasmic reticulum (ER) stress-mediated intercellular junction alterations accompanied by visual deficits in a tie2-TNF-α transgenic mouse model.
31346222	4	32	theme	increased	822:830	arg1	O-GlcNAcylation					832:846	increased O-GlcNAcylation	822:846	increased O-GlcNAcylation of proteins, particularly VE-Cadherin resulting in a defective complex partnering leading to the loss of retinal endothelial barrier integrity	822:989	We show that ER stress leads to GRP78 translocation to the plasma membrane, increased O-GlcNAcylation of proteins, particularly VE-Cadherin resulting in a defective complex partnering leading to the loss of retinal endothelial barrier integrity and increased transendothelial migration of monocytes.
31346222	1	33	theme	various	237:243	arg1	functions					266:274	various detrimental cellular functions	237:274	various detrimental cellular functions in pathological conditions including diabetic retinopathy (DR)	237:337	Increased O-GlcNAcylation, a well-known post-translational modification of proteins causally linked to various detrimental cellular functions in pathological conditions including diabetic retinopathy (DR).
31346222	7	34	theme	essential	1273:1281	arg1	role					1283:1286	an essential role	1270:1286	an essential role for ER stress and O-GlcNAcylation in altering the endothelial barrier function	1270:1365	Our findings suggest an essential role for ER stress and O-GlcNAcylation in altering the endothelial barrier function and reveal a potential therapeutic target in the treatment of DR.
31346222	4	35	theme	complex	911:917	arg1	partnering					919:928	a defective complex partnering	899:928	a defective complex partnering leading to the loss of retinal endothelial barrier integrity	899:989	We show that ER stress leads to GRP78 translocation to the plasma membrane, increased O-GlcNAcylation of proteins, particularly VE-Cadherin resulting in a defective complex partnering leading to the loss of retinal endothelial barrier integrity and increased transendothelial migration of monocytes.
31346222	1	36	theme	detrimental	245:255	arg1	functions					266:274	various detrimental cellular functions	237:274	various detrimental cellular functions in pathological conditions including diabetic retinopathy (DR)	237:337	Increased O-GlcNAcylation, a well-known post-translational modification of proteins causally linked to various detrimental cellular functions in pathological conditions including diabetic retinopathy (DR).
31346222	0	37	theme	cell	27:30	arg1	surface					32:38	the cell surface	23:38	the cell surface	23:38	GRP78 translocation to the cell surface and O-GlcNAcylation of VE-Cadherin contribute to ER stress-mediated endothelial permeability.
31346222	1	38	attach	linked	227:232	arg2	modification					193:204	a well-known post-translational modification	161:204	a well-known post-translational modification of proteins	161:216	Increased O-GlcNAcylation, a well-known post-translational modification of proteins causally linked to various detrimental cellular functions in pathological conditions including diabetic retinopathy (DR).
31346222	1	38	attach	linked	227:232	arg1	functions					266:274	various detrimental cellular functions	237:274	various detrimental cellular functions in pathological conditions including diabetic retinopathy (DR)	237:337	Increased O-GlcNAcylation, a well-known post-translational modification of proteins causally linked to various detrimental cellular functions in pathological conditions including diabetic retinopathy (DR).
31346222	1	38	attach	linked	227:232	arg2	O-GlcNAcylation					144:158	Increased O-GlcNAcylation	134:158	Increased O-GlcNAcylation	134:158	Increased O-GlcNAcylation, a well-known post-translational modification of proteins causally linked to various detrimental cellular functions in pathological conditions including diabetic retinopathy (DR).
31346222	4	39	theme	defective	901:909	arg1	partnering					919:928	a defective complex partnering	899:928	a defective complex partnering leading to the loss of retinal endothelial barrier integrity	899:989	We show that ER stress leads to GRP78 translocation to the plasma membrane, increased O-GlcNAcylation of proteins, particularly VE-Cadherin resulting in a defective complex partnering leading to the loss of retinal endothelial barrier integrity and increased transendothelial migration of monocytes.
31346222	1	40	theme	cellular	257:264	arg1	functions					266:274	various detrimental cellular functions	237:274	various detrimental cellular functions in pathological conditions including diabetic retinopathy (DR)	237:337	Increased O-GlcNAcylation, a well-known post-translational modification of proteins causally linked to various detrimental cellular functions in pathological conditions including diabetic retinopathy (DR).
31346222	2	41	theme	visual	543:548	arg1	deficits					550:557	visual deficits	543:557	visual deficits in a tie2-TNF-α transgenic mouse model	543:596	Previously we have shown that endothelial activation induced by inflammation and hyperglycemia results in the endoplasmic reticulum (ER) stress-mediated intercellular junction alterations accompanied by visual deficits in a tie2-TNF-α transgenic mouse model.
31346222	4	42	theme	increased	995:1003	arg1	migration					1022:1030	increased transendothelial migration	995:1030	increased transendothelial migration of monocytes	995:1043	We show that ER stress leads to GRP78 translocation to the plasma membrane, increased O-GlcNAcylation of proteins, particularly VE-Cadherin resulting in a defective complex partnering leading to the loss of retinal endothelial barrier integrity and increased transendothelial migration of monocytes.
31346222	3	43	theme	endothelial	720:730	arg1	permeability					732:743	endothelial permeability	720:743	endothelial permeability	720:743	In this study, we tested the hypothesis that increased ER stress via O-GlcNAcylation of VE-Cadherin likely contribute to endothelial permeability.
31346222	3	44	theme	ER	654:655	arg1	stress					657:662	increased ER stress	644:662	increased ER stress via O-GlcNAcylation of VE-Cadherin	644:697	In this study, we tested the hypothesis that increased ER stress via O-GlcNAcylation of VE-Cadherin likely contribute to endothelial permeability.
31346222	1	45	theme	Increased	134:142	arg1	O-GlcNAcylation					144:158	Increased O-GlcNAcylation	134:158	Increased O-GlcNAcylation	134:158	Increased O-GlcNAcylation, a well-known post-translational modification of proteins causally linked to various detrimental cellular functions in pathological conditions including diabetic retinopathy (DR).
31346222	1	45	theme	Increased	134:142	arg1	modification					193:204	a well-known post-translational modification	161:204	a well-known post-translational modification of proteins	161:216	Increased O-GlcNAcylation, a well-known post-translational modification of proteins causally linked to various detrimental cellular functions in pathological conditions including diabetic retinopathy (DR).
31346222	1	46	from	functions	266:274	arg1	conditions					292:301	pathological conditions	279:301	pathological conditions including diabetic retinopathy (DR)	279:337	Increased O-GlcNAcylation, a well-known post-translational modification of proteins causally linked to various detrimental cellular functions in pathological conditions including diabetic retinopathy (DR).
31346222	1	46	from	functions	266:274	arg1	retinopathy					322:332	diabetic retinopathy	313:332	diabetic retinopathy (DR)	313:337	Increased O-GlcNAcylation, a well-known post-translational modification of proteins causally linked to various detrimental cellular functions in pathological conditions including diabetic retinopathy (DR).
31346222	4	47	theme	plasma	805:810	arg1	membrane					812:819	the plasma membrane	801:819	the plasma membrane	801:819	We show that ER stress leads to GRP78 translocation to the plasma membrane, increased O-GlcNAcylation of proteins, particularly VE-Cadherin resulting in a defective complex partnering leading to the loss of retinal endothelial barrier integrity and increased transendothelial migration of monocytes.
31346222	4	48	theme	transendothelial	1005:1020	arg1	migration					1022:1030	increased transendothelial migration	995:1030	increased transendothelial migration of monocytes	995:1043	We show that ER stress leads to GRP78 translocation to the plasma membrane, increased O-GlcNAcylation of proteins, particularly VE-Cadherin resulting in a defective complex partnering leading to the loss of retinal endothelial barrier integrity and increased transendothelial migration of monocytes.
31346222	2	49	theme	endothelial	370:380	arg1	activation					382:391	endothelial activation	370:391	endothelial activation induced by inflammation and hyperglycemia	370:433	Previously we have shown that endothelial activation induced by inflammation and hyperglycemia results in the endoplasmic reticulum (ER) stress-mediated intercellular junction alterations accompanied by visual deficits in a tie2-TNF-α transgenic mouse model.
31346222	2	50	theme	mouse	586:590	arg1	model					592:596	a tie2-TNF-α transgenic mouse model	562:596	a tie2-TNF-α transgenic mouse model	562:596	Previously we have shown that endothelial activation induced by inflammation and hyperglycemia results in the endoplasmic reticulum (ER) stress-mediated intercellular junction alterations accompanied by visual deficits in a tie2-TNF-α transgenic mouse model.
31346222	7	51	theme	DR	1429:1430	arg1	treatment					1416:1424	the treatment	1412:1424	the treatment of DR	1412:1430	Our findings suggest an essential role for ER stress and O-GlcNAcylation in altering the endothelial barrier function and reveal a potential therapeutic target in the treatment of DR.
31346222	6	52	theme	stress	1166:1171	arg1	inhibitor					1173:1181	ER stress inhibitor	1163:1181	ER stress inhibitor	1163:1181	Interestingly, cells exposed to ER stress inhibitor, tauroursodeoxycholic acid partially mitigated all these effects.
31346222	6	52	theme	stress	1166:1171	arg1	acid					1205:1208	tauroursodeoxycholic acid	1184:1208	tauroursodeoxycholic acid	1184:1208	Interestingly, cells exposed to ER stress inhibitor, tauroursodeoxycholic acid partially mitigated all these effects.
31346222	7	53	theme	potential	1380:1388	arg1	target					1402:1407	a potential therapeutic target	1378:1407	a potential therapeutic target in the treatment of DR	1378:1430	Our findings suggest an essential role for ER stress and O-GlcNAcylation in altering the endothelial barrier function and reveal a potential therapeutic target in the treatment of DR.
31346222	2	54	theme	endoplasmic	450:460	arg1	ER					473:474	ER	473:474	ER	473:474	Previously we have shown that endothelial activation induced by inflammation and hyperglycemia results in the endoplasmic reticulum (ER) stress-mediated intercellular junction alterations accompanied by visual deficits in a tie2-TNF-α transgenic mouse model.
31346222	2	54	theme	endoplasmic	450:460	arg1	reticulum					462:470	the endoplasmic reticulum	446:470	the endoplasmic reticulum (ER) stress-mediated intercellular junction alterations	446:526	Previously we have shown that endothelial activation induced by inflammation and hyperglycemia results in the endoplasmic reticulum (ER) stress-mediated intercellular junction alterations accompanied by visual deficits in a tie2-TNF-α transgenic mouse model.
31346222	1	55	theme	pathological	279:290	arg1	conditions					292:301	pathological conditions	279:301	pathological conditions including diabetic retinopathy (DR)	279:337	Increased O-GlcNAcylation, a well-known post-translational modification of proteins causally linked to various detrimental cellular functions in pathological conditions including diabetic retinopathy (DR).
31346222	1	55	theme	pathological	279:290	arg1	retinopathy					322:332	diabetic retinopathy	313:332	diabetic retinopathy (DR)	313:337	Increased O-GlcNAcylation, a well-known post-translational modification of proteins causally linked to various detrimental cellular functions in pathological conditions including diabetic retinopathy (DR).
31346222	2	56	theme	transgenic	575:584	arg1	model					592:596	a tie2-TNF-α transgenic mouse model	562:596	a tie2-TNF-α transgenic mouse model	562:596	Previously we have shown that endothelial activation induced by inflammation and hyperglycemia results in the endoplasmic reticulum (ER) stress-mediated intercellular junction alterations accompanied by visual deficits in a tie2-TNF-α transgenic mouse model.
31346222	5	57	theme	GRP78	1080:1084	arg1	association					1065:1075	an association	1062:1075	an association of GRP78 with the VE-Cadherin	1062:1105	We further show an association of GRP78 with the VE-Cadherin under these conditions.
31346222	3	58	theme	VE-Cadherin	687:697	arg1	O-GlcNAcylation					668:682	O-GlcNAcylation	668:682	O-GlcNAcylation of VE-Cadherin	668:697	In this study, we tested the hypothesis that increased ER stress via O-GlcNAcylation of VE-Cadherin likely contribute to endothelial permeability.
31346222	1	59	theme	well-known	163:172	arg1	O-GlcNAcylation					144:158	Increased O-GlcNAcylation	134:158	Increased O-GlcNAcylation	134:158	Increased O-GlcNAcylation, a well-known post-translational modification of proteins causally linked to various detrimental cellular functions in pathological conditions including diabetic retinopathy (DR).
31346222	1	59	theme	well-known	163:172	arg1	modification					193:204	a well-known post-translational modification	161:204	a well-known post-translational modification of proteins	161:216	Increased O-GlcNAcylation, a well-known post-translational modification of proteins causally linked to various detrimental cellular functions in pathological conditions including diabetic retinopathy (DR).
23524144	0	0	theme	E-cadherin	77:86	arg1	levels					88:93	E-cadherin levels	77:93	E-cadherin levels in ovarian cancer cells	77:117	A correlation between altered O-GlcNAcylation, migration and with changes in E-cadherin levels in ovarian cancer cells.
23524144	2	1	attach	linked	372:377	arg1	features					391:398	cellular features	382:398	cellular features relevant to metastasis	382:421	In recent years, the roles of O-GlcNAcylation in several human malignant tumors have been investigated, and O-GlcNAcylation was found to be linked to cellular features relevant to metastasis.
23524144	2	1	attach	linked	372:377	arg2	O-GlcNAcylation					340:354	O-GlcNAcylation	340:354	O-GlcNAcylation	340:354	In recent years, the roles of O-GlcNAcylation in several human malignant tumors have been investigated, and O-GlcNAcylation was found to be linked to cellular features relevant to metastasis.
23524144	7	2	theme	ovarian	1228:1234	arg1	migration					1248:1256	ovarian cancer cell migration	1228:1256	ovarian cancer cell migration	1228:1256	These results indicate that O-GlcNAcylation could enhance ovarian cancer cell migration and decrease the expression of E-cadherin.
23524144	4	3	theme	total	580:584	arg1	level					602:606	total O-GlcNAcylation level	580:606	total O-GlcNAcylation level	580:606	We found that total O-GlcNAcylation level was elevated in HO-8910PM cells compared to OVCAR3 cells.
23524144	1	4	theme	reversible	153:162	arg1	O-GlcNAcylation					120:134	O-GlcNAcylation	120:134	O-GlcNAcylation	120:134	O-GlcNAcylation is a dynamic and reversible posttranslational modification of nuclear and cytoplasmic proteins.
23524144	1	4	theme	reversible	153:162	arg1	modification					182:193	a dynamic and reversible posttranslational modification	139:193	a dynamic and reversible posttranslational modification of nuclear and cytoplasmic proteins	139:229	O-GlcNAcylation is a dynamic and reversible posttranslational modification of nuclear and cytoplasmic proteins.
23524144	3	5	from	effects	505:511	arg1	migration					555:563	ovarian cancer cell migration	535:563	ovarian cancer cell migration	535:563	In this study, we modeled four diverse ovarian cancer cells and investigated the effects of O-GlcNAcylation on ovarian cancer cell migration.
23524144	2	6	theme	malignant	295:303	arg1	tumors					305:310	several human malignant tumors	281:310	several human malignant tumors	281:310	In recent years, the roles of O-GlcNAcylation in several human malignant tumors have been investigated, and O-GlcNAcylation was found to be linked to cellular features relevant to metastasis.
23524144	6	7	theme	O-GlcNAcylated	1026:1039	arg1	protein					1041:1047	an O-GlcNAcylated protein	1023:1047	an O-GlcNAcylated protein in ovarian cancer cells	1023:1071	Furthermore, we also found that the expression of E-cadherin, an O-GlcNAcylated protein in ovarian cancer cells, was reduced by OGA inhibition in OVCAR3 cells and elevated by OGT silencing in HO-8910PM cells.
23524144	6	7	theme	O-GlcNAcylated	1026:1039	arg1	E-cadherin					1011:1020	E-cadherin	1011:1020	E-cadherin	1011:1020	Furthermore, we also found that the expression of E-cadherin, an O-GlcNAcylated protein in ovarian cancer cells, was reduced by OGA inhibition in OVCAR3 cells and elevated by OGT silencing in HO-8910PM cells.
23524144	3	8	theme	cell	550:553	arg1	migration					555:563	ovarian cancer cell migration	535:563	ovarian cancer cell migration	535:563	In this study, we modeled four diverse ovarian cancer cells and investigated the effects of O-GlcNAcylation on ovarian cancer cell migration.
23524144	2	9	theme	human	289:293	arg1	tumors					305:310	several human malignant tumors	281:310	several human malignant tumors	281:310	In recent years, the roles of O-GlcNAcylation in several human malignant tumors have been investigated, and O-GlcNAcylation was found to be linked to cellular features relevant to metastasis.
23524144	4	10	theme	O-GlcNAcylation	586:600	arg1	level					602:606	total O-GlcNAcylation level	580:606	total O-GlcNAcylation level	580:606	We found that total O-GlcNAcylation level was elevated in HO-8910PM cells compared to OVCAR3 cells.
23524144	0	11	theme	cancer	106:111	arg1	cells					113:117	ovarian cancer cells	98:117	ovarian cancer cells	98:117	A correlation between altered O-GlcNAcylation, migration and with changes in E-cadherin levels in ovarian cancer cells.
23524144	0	12	from	migration	47:55	arg1	levels					88:93	E-cadherin levels	77:93	E-cadherin levels in ovarian cancer cells	77:117	A correlation between altered O-GlcNAcylation, migration and with changes in E-cadherin levels in ovarian cancer cells.
23524144	3	13	theme	ovarian	463:469	arg1	cells					478:482	four diverse ovarian cancer cells	450:482	four diverse ovarian cancer cells	450:482	In this study, we modeled four diverse ovarian cancer cells and investigated the effects of O-GlcNAcylation on ovarian cancer cell migration.
23524144	2	14	theme	several	281:287	arg1	tumors					305:310	several human malignant tumors	281:310	several human malignant tumors	281:310	In recent years, the roles of O-GlcNAcylation in several human malignant tumors have been investigated, and O-GlcNAcylation was found to be linked to cellular features relevant to metastasis.
23524144	6	15	theme	cancer	1060:1065	arg1	cells					1067:1071	ovarian cancer cells	1052:1071	ovarian cancer cells	1052:1071	Furthermore, we also found that the expression of E-cadherin, an O-GlcNAcylated protein in ovarian cancer cells, was reduced by OGA inhibition in OVCAR3 cells and elevated by OGT silencing in HO-8910PM cells.
23524144	1	16	theme	posttranslational	164:180	arg1	O-GlcNAcylation					120:134	O-GlcNAcylation	120:134	O-GlcNAcylation	120:134	O-GlcNAcylation is a dynamic and reversible posttranslational modification of nuclear and cytoplasmic proteins.
23524144	1	16	theme	posttranslational	164:180	arg1	modification					182:193	a dynamic and reversible posttranslational modification	139:193	a dynamic and reversible posttranslational modification of nuclear and cytoplasmic proteins	139:229	O-GlcNAcylation is a dynamic and reversible posttranslational modification of nuclear and cytoplasmic proteins.
23524144	0	17	theme	ovarian	98:104	arg1	cells					113:117	ovarian cancer cells	98:117	ovarian cancer cells	98:117	A correlation between altered O-GlcNAcylation, migration and with changes in E-cadherin levels in ovarian cancer cells.
23524144	3	18	theme	ovarian	535:541	arg1	migration					555:563	ovarian cancer cell migration	535:563	ovarian cancer cell migration	535:563	In this study, we modeled four diverse ovarian cancer cells and investigated the effects of O-GlcNAcylation on ovarian cancer cell migration.
23524144	5	19	theme	OGA	749:751	arg1	inhibition					753:762	OGA inhibition	749:762	OGA inhibition	749:762	Additionally, through altering the total O-GlcNAcylation level by OGT silencing or OGA inhibition, we found that the migration of OVCAR3 cells was dramatically enhanced by PUGNAc and Thiamet G treatment, and the migration ability of HO-8910PM cells was significantly inhibited by OGT silencing.
23524144	5	20	theme	cells	803:807	arg1	migration					783:791	the migration	779:791	the migration of OVCAR3 cells	779:807	Additionally, through altering the total O-GlcNAcylation level by OGT silencing or OGA inhibition, we found that the migration of OVCAR3 cells was dramatically enhanced by PUGNAc and Thiamet G treatment, and the migration ability of HO-8910PM cells was significantly inhibited by OGT silencing.
23524144	0	21	from	O-GlcNAcylation	30:44	arg1	levels					88:93	E-cadherin levels	77:93	E-cadherin levels in ovarian cancer cells	77:117	A correlation between altered O-GlcNAcylation, migration and with changes in E-cadherin levels in ovarian cancer cells.
23524144	7	22	theme	cell	1243:1246	arg1	migration					1248:1256	ovarian cancer cell migration	1228:1256	ovarian cancer cell migration	1228:1256	These results indicate that O-GlcNAcylation could enhance ovarian cancer cell migration and decrease the expression of E-cadherin.
23524144	6	23	theme	OGT	1136:1138	arg1	silencing					1140:1148	OGT silencing	1136:1148	OGT silencing	1136:1148	Furthermore, we also found that the expression of E-cadherin, an O-GlcNAcylated protein in ovarian cancer cells, was reduced by OGA inhibition in OVCAR3 cells and elevated by OGT silencing in HO-8910PM cells.
23524144	2	24	theme	cellular	382:389	arg1	features					391:398	cellular features	382:398	cellular features relevant to metastasis	382:421	In recent years, the roles of O-GlcNAcylation in several human malignant tumors have been investigated, and O-GlcNAcylation was found to be linked to cellular features relevant to metastasis.
23524144	5	25	theme	G	857:857	arg1	treatment					859:867	Thiamet G treatment	849:867	Thiamet G treatment	849:867	Additionally, through altering the total O-GlcNAcylation level by OGT silencing or OGA inhibition, we found that the migration of OVCAR3 cells was dramatically enhanced by PUGNAc and Thiamet G treatment, and the migration ability of HO-8910PM cells was significantly inhibited by OGT silencing.
23524144	8	26	theme	potential	1368:1376	arg1	target					1378:1383	another potential target	1360:1383	another potential target for the therapy of ovarian cancer	1360:1417	Our studies also suggest that O-GlcNAcylation might become another potential target for the therapy of ovarian cancer.
23524144	2	27	from	roles	253:257	arg1	tumors					305:310	several human malignant tumors	281:310	several human malignant tumors	281:310	In recent years, the roles of O-GlcNAcylation in several human malignant tumors have been investigated, and O-GlcNAcylation was found to be linked to cellular features relevant to metastasis.
23524144	1	28	theme	nuclear	198:204	arg1	proteins					222:229	nuclear and cytoplasmic proteins	198:229	nuclear and cytoplasmic proteins	198:229	O-GlcNAcylation is a dynamic and reversible posttranslational modification of nuclear and cytoplasmic proteins.
23524144	0	29	theme	altered	22:28	arg1	O-GlcNAcylation					30:44	altered O-GlcNAcylation	22:44	altered O-GlcNAcylation	22:44	A correlation between altered O-GlcNAcylation, migration and with changes in E-cadherin levels in ovarian cancer cells.
23524144	5	30	theme	O-GlcNAcylation	707:721	arg1	level					723:727	the total O-GlcNAcylation level	697:727	the total O-GlcNAcylation level	697:727	Additionally, through altering the total O-GlcNAcylation level by OGT silencing or OGA inhibition, we found that the migration of OVCAR3 cells was dramatically enhanced by PUGNAc and Thiamet G treatment, and the migration ability of HO-8910PM cells was significantly inhibited by OGT silencing.
23524144	6	31	from	protein	1041:1047	arg1	cells					1067:1071	ovarian cancer cells	1052:1071	ovarian cancer cells	1052:1071	Furthermore, we also found that the expression of E-cadherin, an O-GlcNAcylated protein in ovarian cancer cells, was reduced by OGA inhibition in OVCAR3 cells and elevated by OGT silencing in HO-8910PM cells.
23524144	5	32	theme	OGT	946:948	arg1	silencing					950:958	OGT silencing	946:958	OGT silencing	946:958	Additionally, through altering the total O-GlcNAcylation level by OGT silencing or OGA inhibition, we found that the migration of OVCAR3 cells was dramatically enhanced by PUGNAc and Thiamet G treatment, and the migration ability of HO-8910PM cells was significantly inhibited by OGT silencing.
23524144	8	33	theme	cancer	1412:1417	arg1	therapy					1393:1399	the therapy	1389:1399	the therapy of ovarian cancer	1389:1417	Our studies also suggest that O-GlcNAcylation might become another potential target for the therapy of ovarian cancer.
23524144	3	34	theme	diverse	455:461	arg1	cells					478:482	four diverse ovarian cancer cells	450:482	four diverse ovarian cancer cells	450:482	In this study, we modeled four diverse ovarian cancer cells and investigated the effects of O-GlcNAcylation on ovarian cancer cell migration.
23524144	7	35	theme	cancer	1236:1241	arg1	migration					1248:1256	ovarian cancer cell migration	1228:1256	ovarian cancer cell migration	1228:1256	These results indicate that O-GlcNAcylation could enhance ovarian cancer cell migration and decrease the expression of E-cadherin.
23524144	1	36	theme	cytoplasmic	210:220	arg1	proteins					222:229	nuclear and cytoplasmic proteins	198:229	nuclear and cytoplasmic proteins	198:229	O-GlcNAcylation is a dynamic and reversible posttranslational modification of nuclear and cytoplasmic proteins.
23524144	7	37	theme	E-cadherin	1289:1298	arg1	expression					1275:1284	the expression	1271:1284	the expression of E-cadherin	1271:1298	These results indicate that O-GlcNAcylation could enhance ovarian cancer cell migration and decrease the expression of E-cadherin.
23524144	6	38	theme	OVCAR3	1107:1112	arg1	cells					1114:1118	OVCAR3 cells	1107:1118	OVCAR3 cells	1107:1118	Furthermore, we also found that the expression of E-cadherin, an O-GlcNAcylated protein in ovarian cancer cells, was reduced by OGA inhibition in OVCAR3 cells and elevated by OGT silencing in HO-8910PM cells.
23524144	4	39	theme	OVCAR3	652:657	arg1	cells					659:663	OVCAR3 cells	652:663	OVCAR3 cells	652:663	We found that total O-GlcNAcylation level was elevated in HO-8910PM cells compared to OVCAR3 cells.
23524144	6	40	theme	ovarian	1052:1058	arg1	cells					1067:1071	ovarian cancer cells	1052:1071	ovarian cancer cells	1052:1071	Furthermore, we also found that the expression of E-cadherin, an O-GlcNAcylated protein in ovarian cancer cells, was reduced by OGA inhibition in OVCAR3 cells and elevated by OGT silencing in HO-8910PM cells.
23524144	1	41	theme	proteins	222:229	arg1	O-GlcNAcylation					120:134	O-GlcNAcylation	120:134	O-GlcNAcylation	120:134	O-GlcNAcylation is a dynamic and reversible posttranslational modification of nuclear and cytoplasmic proteins.
23524144	1	41	theme	proteins	222:229	arg1	modification					182:193	a dynamic and reversible posttranslational modification	139:193	a dynamic and reversible posttranslational modification of nuclear and cytoplasmic proteins	139:229	O-GlcNAcylation is a dynamic and reversible posttranslational modification of nuclear and cytoplasmic proteins.
23524144	2	42	theme	relevant	400:407	arg1	features					391:398	cellular features	382:398	cellular features relevant to metastasis	382:421	In recent years, the roles of O-GlcNAcylation in several human malignant tumors have been investigated, and O-GlcNAcylation was found to be linked to cellular features relevant to metastasis.
23524144	5	43	theme	OGT	732:734	arg1	silencing					736:744	OGT silencing	732:744	OGT silencing	732:744	Additionally, through altering the total O-GlcNAcylation level by OGT silencing or OGA inhibition, we found that the migration of OVCAR3 cells was dramatically enhanced by PUGNAc and Thiamet G treatment, and the migration ability of HO-8910PM cells was significantly inhibited by OGT silencing.
23524144	0	44	from	changes	66:72	arg1	levels					88:93	E-cadherin levels	77:93	E-cadherin levels in ovarian cancer cells	77:117	A correlation between altered O-GlcNAcylation, migration and with changes in E-cadherin levels in ovarian cancer cells.
23524144	5	45	theme	Thiamet	849:855	arg1	treatment					859:867	Thiamet G treatment	849:867	Thiamet G treatment	849:867	Additionally, through altering the total O-GlcNAcylation level by OGT silencing or OGA inhibition, we found that the migration of OVCAR3 cells was dramatically enhanced by PUGNAc and Thiamet G treatment, and the migration ability of HO-8910PM cells was significantly inhibited by OGT silencing.
23524144	2	46	theme	recent	235:240	arg1	years					242:246	recent years	235:246	recent years	235:246	In recent years, the roles of O-GlcNAcylation in several human malignant tumors have been investigated, and O-GlcNAcylation was found to be linked to cellular features relevant to metastasis.
23524144	6	47	theme	OGA	1089:1091	arg1	inhibition					1093:1102	OGA inhibition	1089:1102	OGA inhibition	1089:1102	Furthermore, we also found that the expression of E-cadherin, an O-GlcNAcylated protein in ovarian cancer cells, was reduced by OGA inhibition in OVCAR3 cells and elevated by OGT silencing in HO-8910PM cells.
23524144	5	48	theme	HO-8910PM	899:907	arg1	cells					909:913	HO-8910PM cells	899:913	HO-8910PM cells	899:913	Additionally, through altering the total O-GlcNAcylation level by OGT silencing or OGA inhibition, we found that the migration of OVCAR3 cells was dramatically enhanced by PUGNAc and Thiamet G treatment, and the migration ability of HO-8910PM cells was significantly inhibited by OGT silencing.
23524144	5	49	theme	OVCAR3	796:801	arg1	cells					803:807	OVCAR3 cells	796:807	OVCAR3 cells	796:807	Additionally, through altering the total O-GlcNAcylation level by OGT silencing or OGA inhibition, we found that the migration of OVCAR3 cells was dramatically enhanced by PUGNAc and Thiamet G treatment, and the migration ability of HO-8910PM cells was significantly inhibited by OGT silencing.
23524144	6	50	theme	HO-8910PM	1153:1161	arg1	cells					1163:1167	HO-8910PM cells	1153:1167	HO-8910PM cells	1153:1167	Furthermore, we also found that the expression of E-cadherin, an O-GlcNAcylated protein in ovarian cancer cells, was reduced by OGA inhibition in OVCAR3 cells and elevated by OGT silencing in HO-8910PM cells.
23524144	8	51	theme	ovarian	1404:1410	arg1	cancer					1412:1417	ovarian cancer	1404:1417	ovarian cancer	1404:1417	Our studies also suggest that O-GlcNAcylation might become another potential target for the therapy of ovarian cancer.
23524144	5	52	theme	cells	909:913	arg1	ability					888:894	the migration ability	874:894	the migration ability of HO-8910PM cells	874:913	Additionally, through altering the total O-GlcNAcylation level by OGT silencing or OGA inhibition, we found that the migration of OVCAR3 cells was dramatically enhanced by PUGNAc and Thiamet G treatment, and the migration ability of HO-8910PM cells was significantly inhibited by OGT silencing.
23524144	2	53	theme	O-GlcNAcylation	262:276	arg1	roles					253:257	the roles	249:257	the roles of O-GlcNAcylation in several human malignant tumors	249:310	In recent years, the roles of O-GlcNAcylation in several human malignant tumors have been investigated, and O-GlcNAcylation was found to be linked to cellular features relevant to metastasis.
23524144	3	54	theme	cancer	471:476	arg1	cells					478:482	four diverse ovarian cancer cells	450:482	four diverse ovarian cancer cells	450:482	In this study, we modeled four diverse ovarian cancer cells and investigated the effects of O-GlcNAcylation on ovarian cancer cell migration.
23524144	5	55	theme	total	701:705	arg1	level					723:727	the total O-GlcNAcylation level	697:727	the total O-GlcNAcylation level	697:727	Additionally, through altering the total O-GlcNAcylation level by OGT silencing or OGA inhibition, we found that the migration of OVCAR3 cells was dramatically enhanced by PUGNAc and Thiamet G treatment, and the migration ability of HO-8910PM cells was significantly inhibited by OGT silencing.
23524144	3	56	theme	cancer	543:548	arg1	migration					555:563	ovarian cancer cell migration	535:563	ovarian cancer cell migration	535:563	In this study, we modeled four diverse ovarian cancer cells and investigated the effects of O-GlcNAcylation on ovarian cancer cell migration.
23524144	3	57	theme	O-GlcNAcylation	516:530	arg1	effects					505:511	the effects	501:511	the effects of O-GlcNAcylation on ovarian cancer cell migration	501:563	In this study, we modeled four diverse ovarian cancer cells and investigated the effects of O-GlcNAcylation on ovarian cancer cell migration.
23524144	6	58	theme	E-cadherin	1011:1020	arg1	expression					997:1006	the expression	993:1006	the expression of E-cadherin, an O-GlcNAcylated protein in ovarian cancer cells,	993:1072	Furthermore, we also found that the expression of E-cadherin, an O-GlcNAcylated protein in ovarian cancer cells, was reduced by OGA inhibition in OVCAR3 cells and elevated by OGT silencing in HO-8910PM cells.
23524144	0	59	from	levels	88:93	arg1	cells					113:117	ovarian cancer cells	98:117	ovarian cancer cells	98:117	A correlation between altered O-GlcNAcylation, migration and with changes in E-cadherin levels in ovarian cancer cells.
23524144	5	60	theme	migration	878:886	arg1	ability					888:894	the migration ability	874:894	the migration ability of HO-8910PM cells	874:913	Additionally, through altering the total O-GlcNAcylation level by OGT silencing or OGA inhibition, we found that the migration of OVCAR3 cells was dramatically enhanced by PUGNAc and Thiamet G treatment, and the migration ability of HO-8910PM cells was significantly inhibited by OGT silencing.
23524144	4	61	theme	HO-8910PM	624:632	arg1	cells					634:638	HO-8910PM cells	624:638	HO-8910PM cells	624:638	We found that total O-GlcNAcylation level was elevated in HO-8910PM cells compared to OVCAR3 cells.
23524144	0	62	theme	with	61:64	arg1	changes					66:72	changes	66:72	with changes	61:72	A correlation between altered O-GlcNAcylation, migration and with changes in E-cadherin levels in ovarian cancer cells.
23524144	1	63	theme	dynamic	141:147	arg1	O-GlcNAcylation					120:134	O-GlcNAcylation	120:134	O-GlcNAcylation	120:134	O-GlcNAcylation is a dynamic and reversible posttranslational modification of nuclear and cytoplasmic proteins.
23524144	1	63	theme	dynamic	141:147	arg1	modification					182:193	a dynamic and reversible posttranslational modification	139:193	a dynamic and reversible posttranslational modification of nuclear and cytoplasmic proteins	139:229	O-GlcNAcylation is a dynamic and reversible posttranslational modification of nuclear and cytoplasmic proteins.
22574218	5	0	theme	26S	815:817	arg1	proteasomes					819:829	26S proteasomes	815:829	26S proteasomes	815:829	Pharmacological and genetic activation of AMPK effectively suppresses 26S proteasomes in endothelial cells.
22574218	9	1	theme	physiological	1558:1570	arg1	AMPK					1538:1541	AMPK	1538:1541	AMPK	1538:1541	Taken together, we conclude that AMPK functions as a physiological suppressor of 26S proteasomes.
22574218	9	1	theme	physiological	1558:1570	arg1	suppressor					1572:1581	a physiological suppressor	1556:1581	a physiological suppressor of 26S proteasomes	1556:1600	Taken together, we conclude that AMPK functions as a physiological suppressor of 26S proteasomes.
22574218	4	2	theme	umbilical	557:565	arg1	exposed					693:699	exposed	693:699	being exposed to selective AMPK activators or inhibitors	687:742	26S proteasome assembly, activity, and O-GlcNAcylation of P700 were assayed in cultured human umbilical vein endothelial cells (HUVEC) and mouse aortas isolated from C57BL6 wild type and AMPKα2 knockout mice with or without being exposed to selective AMPK activators or inhibitors.
22574218	4	2	theme	umbilical	557:565	arg1	HUVEC					591:595	HUVEC	591:595	HUVEC	591:595	26S proteasome assembly, activity, and O-GlcNAcylation of P700 were assayed in cultured human umbilical vein endothelial cells (HUVEC) and mouse aortas isolated from C57BL6 wild type and AMPKα2 knockout mice with or without being exposed to selective AMPK activators or inhibitors.
22574218	4	2	theme	umbilical	557:565	arg1	with					671:674	with	671:674	with	671:674	26S proteasome assembly, activity, and O-GlcNAcylation of P700 were assayed in cultured human umbilical vein endothelial cells (HUVEC) and mouse aortas isolated from C57BL6 wild type and AMPKα2 knockout mice with or without being exposed to selective AMPK activators or inhibitors.
22574218	4	2	theme	umbilical	557:565	arg1	cells					584:588	cultured human umbilical vein endothelial cells	542:588	cultured human umbilical vein endothelial cells (HUVEC)	542:596	26S proteasome assembly, activity, and O-GlcNAcylation of P700 were assayed in cultured human umbilical vein endothelial cells (HUVEC) and mouse aortas isolated from C57BL6 wild type and AMPKα2 knockout mice with or without being exposed to selective AMPK activators or inhibitors.
22574218	3	3	theme	present	307:313	arg1	study					315:319	The present study	303:319	The present study	303:319	The present study was to investigate if AMP-activated protein kinase (AMPK) functions as a physiological suppressor of the 26S proteasome in endothelial cells.
22574218	1	4	theme	macromolecular	119:132	arg1	complex					148:154	a macromolecular multi-subunit complex	117:154	a macromolecular multi-subunit complex responsible for recognizing, unfolding, and ultimately destroying proteins	117:229	26S proteasome is a macromolecular multi-subunit complex responsible for recognizing, unfolding, and ultimately destroying proteins.
22574218	1	4	theme	macromolecular	119:132	arg1	proteasome					103:112	26S proteasome	99:112	26S proteasome	99:112	26S proteasome is a macromolecular multi-subunit complex responsible for recognizing, unfolding, and ultimately destroying proteins.
22574218	8	5	theme	elevated	1386:1393	arg1	activity					1410:1417	elevated 26S proteasome activity	1386:1417	elevated 26S proteasome activity	1386:1417	Finally, aortas from AMPK-KO vs wild type mice exhibit elevated 26S proteasome activity in parallel with decreased PA700/S10B O-GlcNAcylation and PA700/S10B-OGT association.
22574218	4	6	theme	human	551:555	arg1	exposed					693:699	exposed	693:699	being exposed to selective AMPK activators or inhibitors	687:742	26S proteasome assembly, activity, and O-GlcNAcylation of P700 were assayed in cultured human umbilical vein endothelial cells (HUVEC) and mouse aortas isolated from C57BL6 wild type and AMPKα2 knockout mice with or without being exposed to selective AMPK activators or inhibitors.
22574218	4	6	theme	human	551:555	arg1	HUVEC					591:595	HUVEC	591:595	HUVEC	591:595	26S proteasome assembly, activity, and O-GlcNAcylation of P700 were assayed in cultured human umbilical vein endothelial cells (HUVEC) and mouse aortas isolated from C57BL6 wild type and AMPKα2 knockout mice with or without being exposed to selective AMPK activators or inhibitors.
22574218	4	6	theme	human	551:555	arg1	with					671:674	with	671:674	with	671:674	26S proteasome assembly, activity, and O-GlcNAcylation of P700 were assayed in cultured human umbilical vein endothelial cells (HUVEC) and mouse aortas isolated from C57BL6 wild type and AMPKα2 knockout mice with or without being exposed to selective AMPK activators or inhibitors.
22574218	4	6	theme	human	551:555	arg1	cells					584:588	cultured human umbilical vein endothelial cells	542:588	cultured human umbilical vein endothelial cells (HUVEC)	542:596	26S proteasome assembly, activity, and O-GlcNAcylation of P700 were assayed in cultured human umbilical vein endothelial cells (HUVEC) and mouse aortas isolated from C57BL6 wild type and AMPKα2 knockout mice with or without being exposed to selective AMPK activators or inhibitors.
22574218	0	7	theme	O-GlcNAc	71:78	arg1	OGT					93:95	OGT	93:95	OGT	93:95	Regulation of the proteasome by AMPK in endothelial cells: the role of O-GlcNAc transferase (OGT).
22574218	0	7	theme	O-GlcNAc	71:78	arg1	transferase					80:90	O-GlcNAc transferase	71:90	O-GlcNAc transferase (OGT)	71:96	Regulation of the proteasome by AMPK in endothelial cells: the role of O-GlcNAc transferase (OGT).
22574218	0	8	from	Regulation	0:9	arg1	cells					52:56	endothelial cells	40:56	endothelial cells	40:56	Regulation of the proteasome by AMPK in endothelial cells: the role of O-GlcNAc transferase (OGT).
22574218	2	9	theme	proteasome	269:278	arg1	activity					280:287	26S proteasome activity	265:287	26S proteasome activity	265:287	It remains poorly understood how 26S proteasome activity is regulated.
22574218	8	10	theme	PA700/S10B	1446:1455	arg1	O-GlcNAcylation					1457:1471	decreased PA700/S10B O-GlcNAcylation	1436:1471	decreased PA700/S10B O-GlcNAcylation	1436:1471	Finally, aortas from AMPK-KO vs wild type mice exhibit elevated 26S proteasome activity in parallel with decreased PA700/S10B O-GlcNAcylation and PA700/S10B-OGT association.
22574218	4	11	theme	endothelial	572:582	arg1	exposed					693:699	exposed	693:699	being exposed to selective AMPK activators or inhibitors	687:742	26S proteasome assembly, activity, and O-GlcNAcylation of P700 were assayed in cultured human umbilical vein endothelial cells (HUVEC) and mouse aortas isolated from C57BL6 wild type and AMPKα2 knockout mice with or without being exposed to selective AMPK activators or inhibitors.
22574218	4	11	theme	endothelial	572:582	arg1	HUVEC					591:595	HUVEC	591:595	HUVEC	591:595	26S proteasome assembly, activity, and O-GlcNAcylation of P700 were assayed in cultured human umbilical vein endothelial cells (HUVEC) and mouse aortas isolated from C57BL6 wild type and AMPKα2 knockout mice with or without being exposed to selective AMPK activators or inhibitors.
22574218	4	11	theme	endothelial	572:582	arg1	with					671:674	with	671:674	with	671:674	26S proteasome assembly, activity, and O-GlcNAcylation of P700 were assayed in cultured human umbilical vein endothelial cells (HUVEC) and mouse aortas isolated from C57BL6 wild type and AMPKα2 knockout mice with or without being exposed to selective AMPK activators or inhibitors.
22574218	4	11	theme	endothelial	572:582	arg1	cells					584:588	cultured human umbilical vein endothelial cells	542:588	cultured human umbilical vein endothelial cells (HUVEC)	542:596	26S proteasome assembly, activity, and O-GlcNAcylation of P700 were assayed in cultured human umbilical vein endothelial cells (HUVEC) and mouse aortas isolated from C57BL6 wild type and AMPKα2 knockout mice with or without being exposed to selective AMPK activators or inhibitors.
22574218	3	12	theme	AMP-activated	343:355	arg1	AMPK					373:376	AMPK	373:376	AMPK	373:376	The present study was to investigate if AMP-activated protein kinase (AMPK) functions as a physiological suppressor of the 26S proteasome in endothelial cells.
22574218	3	12	theme	AMP-activated	343:355	arg1	kinase					365:370	AMP-activated protein kinase	343:370	AMP-activated protein kinase (AMPK)	343:377	The present study was to investigate if AMP-activated protein kinase (AMPK) functions as a physiological suppressor of the 26S proteasome in endothelial cells.
22574218	3	12	theme	AMP-activated	343:355	arg1	suppressor					408:417	a physiological suppressor	392:417	a physiological suppressor of the 26S proteasome in endothelial cells	392:460	The present study was to investigate if AMP-activated protein kinase (AMPK) functions as a physiological suppressor of the 26S proteasome in endothelial cells.
22574218	8	13	theme	AMPK-KO	1352:1358	arg1	mice					1373:1376	AMPK-KO vs wild type mice	1352:1376	AMPK-KO vs wild type mice	1352:1376	Finally, aortas from AMPK-KO vs wild type mice exhibit elevated 26S proteasome activity in parallel with decreased PA700/S10B O-GlcNAcylation and PA700/S10B-OGT association.
22574218	2	14	theme	26S	265:267	arg1	activity					280:287	26S proteasome activity	265:287	26S proteasome activity	265:287	It remains poorly understood how 26S proteasome activity is regulated.
22574218	4	15	theme	vein	567:570	arg1	exposed					693:699	exposed	693:699	being exposed to selective AMPK activators or inhibitors	687:742	26S proteasome assembly, activity, and O-GlcNAcylation of P700 were assayed in cultured human umbilical vein endothelial cells (HUVEC) and mouse aortas isolated from C57BL6 wild type and AMPKα2 knockout mice with or without being exposed to selective AMPK activators or inhibitors.
22574218	4	15	theme	vein	567:570	arg1	HUVEC					591:595	HUVEC	591:595	HUVEC	591:595	26S proteasome assembly, activity, and O-GlcNAcylation of P700 were assayed in cultured human umbilical vein endothelial cells (HUVEC) and mouse aortas isolated from C57BL6 wild type and AMPKα2 knockout mice with or without being exposed to selective AMPK activators or inhibitors.
22574218	4	15	theme	vein	567:570	arg1	with					671:674	with	671:674	with	671:674	26S proteasome assembly, activity, and O-GlcNAcylation of P700 were assayed in cultured human umbilical vein endothelial cells (HUVEC) and mouse aortas isolated from C57BL6 wild type and AMPKα2 knockout mice with or without being exposed to selective AMPK activators or inhibitors.
22574218	4	15	theme	vein	567:570	arg1	cells					584:588	cultured human umbilical vein endothelial cells	542:588	cultured human umbilical vein endothelial cells (HUVEC)	542:596	26S proteasome assembly, activity, and O-GlcNAcylation of P700 were assayed in cultured human umbilical vein endothelial cells (HUVEC) and mouse aortas isolated from C57BL6 wild type and AMPKα2 knockout mice with or without being exposed to selective AMPK activators or inhibitors.
22574218	4	16	theme	knockout	657:664	arg1	mice					666:669	C57BL6 wild type and AMPKα2 knockout mice	629:669	mice	666:669	26S proteasome assembly, activity, and O-GlcNAcylation of P700 were assayed in cultured human umbilical vein endothelial cells (HUVEC) and mouse aortas isolated from C57BL6 wild type and AMPKα2 knockout mice with or without being exposed to selective AMPK activators or inhibitors.
22574218	6	17	theme	AMPK	881:884	arg1	inactivation					865:876	inactivation	865:876	inactivation of AMPK	865:884	Conversely, inactivation of AMPK either pharmacologically or genetically increases 26S proteasome activity; furthermore, the inactivation decreases the O-GlcNAcylation of PA700/S10B (the regulatory complex in 26S proteasomes) and increases the assembly of 26S proteasomes.
22574218	7	18	theme	O-GlcNAcylated	1175:1188	arg1	PA700/S10B					1190:1199	O-GlcNAcylated PA700/S10B	1175:1199	O-GlcNAcylated PA700/S10B	1175:1199	In contrast, AMPK activation increases levels of O-GlcNAcylated PA700/S10B, likely through enhanced association of PA700 with O-GlcNAc transferase (OGT), the enzyme that catalyzes protein O-GlcNAcylation.
22574218	6	19	theme	26S	1062:1064	arg1	proteasomes					1066:1076	26S proteasomes	1062:1076	26S proteasomes	1062:1076	Conversely, inactivation of AMPK either pharmacologically or genetically increases 26S proteasome activity; furthermore, the inactivation decreases the O-GlcNAcylation of PA700/S10B (the regulatory complex in 26S proteasomes) and increases the assembly of 26S proteasomes.
22574218	8	20	theme	type	1368:1371	arg1	mice					1373:1376	AMPK-KO vs wild type mice	1352:1376	AMPK-KO vs wild type mice	1352:1376	Finally, aortas from AMPK-KO vs wild type mice exhibit elevated 26S proteasome activity in parallel with decreased PA700/S10B O-GlcNAcylation and PA700/S10B-OGT association.
22574218	1	21	theme	responsible	156:166	arg1	complex					148:154	a macromolecular multi-subunit complex	117:154	a macromolecular multi-subunit complex responsible for recognizing, unfolding, and ultimately destroying proteins	117:229	26S proteasome is a macromolecular multi-subunit complex responsible for recognizing, unfolding, and ultimately destroying proteins.
22574218	1	21	theme	responsible	156:166	arg1	proteasome					103:112	26S proteasome	99:112	26S proteasome	99:112	26S proteasome is a macromolecular multi-subunit complex responsible for recognizing, unfolding, and ultimately destroying proteins.
22574218	1	22	theme	multi-subunit	134:146	arg1	complex					148:154	a macromolecular multi-subunit complex	117:154	a macromolecular multi-subunit complex responsible for recognizing, unfolding, and ultimately destroying proteins	117:229	26S proteasome is a macromolecular multi-subunit complex responsible for recognizing, unfolding, and ultimately destroying proteins.
22574218	1	22	theme	multi-subunit	134:146	arg1	proteasome					103:112	26S proteasome	99:112	26S proteasome	99:112	26S proteasome is a macromolecular multi-subunit complex responsible for recognizing, unfolding, and ultimately destroying proteins.
22574218	0	23	theme	transferase	80:90	arg1	role					63:66	the role	59:66	Regulation of the proteasome by AMPK in endothelial cells: the role of O-GlcNAc transferase (OGT).	0:97	Regulation of the proteasome by AMPK in endothelial cells: the role of O-GlcNAc transferase (OGT).
22574218	4	24	theme	proteasome	467:476	arg1	assembly					478:485	26S proteasome assembly	463:485	26S proteasome assembly	463:485	26S proteasome assembly, activity, and O-GlcNAcylation of P700 were assayed in cultured human umbilical vein endothelial cells (HUVEC) and mouse aortas isolated from C57BL6 wild type and AMPKα2 knockout mice with or without being exposed to selective AMPK activators or inhibitors.
22574218	7	25	theme	AMPK	1139:1142	arg1	activation					1144:1153	AMPK activation	1139:1153	AMPK activation	1139:1153	In contrast, AMPK activation increases levels of O-GlcNAcylated PA700/S10B, likely through enhanced association of PA700 with O-GlcNAc transferase (OGT), the enzyme that catalyzes protein O-GlcNAcylation.
22574218	8	26	theme	wild	1363:1366	arg1	type					1368:1371	wild type	1363:1371	wild type	1363:1371	Finally, aortas from AMPK-KO vs wild type mice exhibit elevated 26S proteasome activity in parallel with decreased PA700/S10B O-GlcNAcylation and PA700/S10B-OGT association.
22574218	6	27	theme	proteasome	940:949	arg1	activity					951:958	26S proteasome activity	936:958	26S proteasome activity	936:958	Conversely, inactivation of AMPK either pharmacologically or genetically increases 26S proteasome activity; furthermore, the inactivation decreases the O-GlcNAcylation of PA700/S10B (the regulatory complex in 26S proteasomes) and increases the assembly of 26S proteasomes.
22574218	7	28	theme	PA700/S10B	1190:1199	arg1	levels					1165:1170	levels	1165:1170	levels of O-GlcNAcylated PA700/S10B	1165:1199	In contrast, AMPK activation increases levels of O-GlcNAcylated PA700/S10B, likely through enhanced association of PA700 with O-GlcNAc transferase (OGT), the enzyme that catalyzes protein O-GlcNAcylation.
22574218	4	29	theme	26S	463:465	arg1	proteasome					467:476	26S proteasome	463:476	26S proteasome assembly	463:485	26S proteasome assembly, activity, and O-GlcNAcylation of P700 were assayed in cultured human umbilical vein endothelial cells (HUVEC) and mouse aortas isolated from C57BL6 wild type and AMPKα2 knockout mice with or without being exposed to selective AMPK activators or inhibitors.
22574218	7	30	theme	PA700	1241:1245	arg1	association					1226:1236	enhanced association	1217:1236	enhanced association of PA700 with O-GlcNAc transferase (OGT), the enzyme that catalyzes protein O-GlcNAcylation	1217:1328	In contrast, AMPK activation increases levels of O-GlcNAcylated PA700/S10B, likely through enhanced association of PA700 with O-GlcNAc transferase (OGT), the enzyme that catalyzes protein O-GlcNAcylation.
22574218	6	31	from	complex	1051:1057	arg1	proteasomes					1066:1076	26S proteasomes	1062:1076	26S proteasomes	1062:1076	Conversely, inactivation of AMPK either pharmacologically or genetically increases 26S proteasome activity; furthermore, the inactivation decreases the O-GlcNAcylation of PA700/S10B (the regulatory complex in 26S proteasomes) and increases the assembly of 26S proteasomes.
22574218	6	32	dep	PA700/S10B	1024:1033	arg1	complex					1051:1057	the regulatory complex	1036:1057	the regulatory complex in 26S proteasomes	1036:1076	Conversely, inactivation of AMPK either pharmacologically or genetically increases 26S proteasome activity; furthermore, the inactivation decreases the O-GlcNAcylation of PA700/S10B (the regulatory complex in 26S proteasomes) and increases the assembly of 26S proteasomes.
22574218	3	33	theme	physiological	394:406	arg1	suppressor					408:417	a physiological suppressor	392:417	a physiological suppressor of the 26S proteasome in endothelial cells	392:460	The present study was to investigate if AMP-activated protein kinase (AMPK) functions as a physiological suppressor of the 26S proteasome in endothelial cells.
22574218	3	33	theme	physiological	394:406	arg1	kinase					365:370	AMP-activated protein kinase	343:370	AMP-activated protein kinase (AMPK)	343:377	The present study was to investigate if AMP-activated protein kinase (AMPK) functions as a physiological suppressor of the 26S proteasome in endothelial cells.
22574218	5	34	theme	AMPK	787:790	arg1	activation					773:782	Pharmacological and genetic activation	745:782	Pharmacological and genetic activation of AMPK	745:790	Pharmacological and genetic activation of AMPK effectively suppresses 26S proteasomes in endothelial cells.
22574218	8	35	with	parallel	1422:1429	arg1	association					1492:1502	PA700/S10B-OGT association	1477:1502	PA700/S10B-OGT association	1477:1502	Finally, aortas from AMPK-KO vs wild type mice exhibit elevated 26S proteasome activity in parallel with decreased PA700/S10B O-GlcNAcylation and PA700/S10B-OGT association.
22574218	8	35	with	parallel	1422:1429	arg1	O-GlcNAcylation					1457:1471	decreased PA700/S10B O-GlcNAcylation	1436:1471	decreased PA700/S10B O-GlcNAcylation	1436:1471	Finally, aortas from AMPK-KO vs wild type mice exhibit elevated 26S proteasome activity in parallel with decreased PA700/S10B O-GlcNAcylation and PA700/S10B-OGT association.
22574218	4	36	theme	wild	636:639	arg1	type					641:644	C57BL6 wild type and AMPKα2 knockout mice	629:669	type	641:644	26S proteasome assembly, activity, and O-GlcNAcylation of P700 were assayed in cultured human umbilical vein endothelial cells (HUVEC) and mouse aortas isolated from C57BL6 wild type and AMPKα2 knockout mice with or without being exposed to selective AMPK activators or inhibitors.
22574218	3	37	theme	protein	357:363	arg1	AMPK					373:376	AMPK	373:376	AMPK	373:376	The present study was to investigate if AMP-activated protein kinase (AMPK) functions as a physiological suppressor of the 26S proteasome in endothelial cells.
22574218	3	37	theme	protein	357:363	arg1	kinase					365:370	AMP-activated protein kinase	343:370	AMP-activated protein kinase (AMPK)	343:377	The present study was to investigate if AMP-activated protein kinase (AMPK) functions as a physiological suppressor of the 26S proteasome in endothelial cells.
22574218	3	37	theme	protein	357:363	arg1	suppressor					408:417	a physiological suppressor	392:417	a physiological suppressor of the 26S proteasome in endothelial cells	392:460	The present study was to investigate if AMP-activated protein kinase (AMPK) functions as a physiological suppressor of the 26S proteasome in endothelial cells.
22574218	4	38	theme	AMPK	714:717	arg1	activators					719:728	selective AMPK activators	704:728	selective AMPK activators	704:728	26S proteasome assembly, activity, and O-GlcNAcylation of P700 were assayed in cultured human umbilical vein endothelial cells (HUVEC) and mouse aortas isolated from C57BL6 wild type and AMPKα2 knockout mice with or without being exposed to selective AMPK activators or inhibitors.
22574218	4	39	theme	mouse	602:606	arg1	aortas					608:613	mouse aortas	602:613	mouse aortas	602:613	26S proteasome assembly, activity, and O-GlcNAcylation of P700 were assayed in cultured human umbilical vein endothelial cells (HUVEC) and mouse aortas isolated from C57BL6 wild type and AMPKα2 knockout mice with or without being exposed to selective AMPK activators or inhibitors.
22574218	3	40	from	suppressor	408:417	arg1	cells					456:460	endothelial cells	444:460	endothelial cells	444:460	The present study was to investigate if AMP-activated protein kinase (AMPK) functions as a physiological suppressor of the 26S proteasome in endothelial cells.
22574218	4	41	theme	cultured	542:549	arg1	exposed					693:699	exposed	693:699	being exposed to selective AMPK activators or inhibitors	687:742	26S proteasome assembly, activity, and O-GlcNAcylation of P700 were assayed in cultured human umbilical vein endothelial cells (HUVEC) and mouse aortas isolated from C57BL6 wild type and AMPKα2 knockout mice with or without being exposed to selective AMPK activators or inhibitors.
22574218	4	41	theme	cultured	542:549	arg1	HUVEC					591:595	HUVEC	591:595	HUVEC	591:595	26S proteasome assembly, activity, and O-GlcNAcylation of P700 were assayed in cultured human umbilical vein endothelial cells (HUVEC) and mouse aortas isolated from C57BL6 wild type and AMPKα2 knockout mice with or without being exposed to selective AMPK activators or inhibitors.
22574218	4	41	theme	cultured	542:549	arg1	with					671:674	with	671:674	with	671:674	26S proteasome assembly, activity, and O-GlcNAcylation of P700 were assayed in cultured human umbilical vein endothelial cells (HUVEC) and mouse aortas isolated from C57BL6 wild type and AMPKα2 knockout mice with or without being exposed to selective AMPK activators or inhibitors.
22574218	4	41	theme	cultured	542:549	arg1	cells					584:588	cultured human umbilical vein endothelial cells	542:588	cultured human umbilical vein endothelial cells (HUVEC)	542:596	26S proteasome assembly, activity, and O-GlcNAcylation of P700 were assayed in cultured human umbilical vein endothelial cells (HUVEC) and mouse aortas isolated from C57BL6 wild type and AMPKα2 knockout mice with or without being exposed to selective AMPK activators or inhibitors.
22574218	9	42	theme	proteasomes	1590:1600	arg1	AMPK					1538:1541	AMPK	1538:1541	AMPK	1538:1541	Taken together, we conclude that AMPK functions as a physiological suppressor of 26S proteasomes.
22574218	9	42	theme	proteasomes	1590:1600	arg1	suppressor					1572:1581	a physiological suppressor	1556:1581	a physiological suppressor of 26S proteasomes	1556:1600	Taken together, we conclude that AMPK functions as a physiological suppressor of 26S proteasomes.
22574218	8	43	theme	PA700/S10B-OGT	1477:1490	arg1	association					1492:1502	PA700/S10B-OGT association	1477:1502	PA700/S10B-OGT association	1477:1502	Finally, aortas from AMPK-KO vs wild type mice exhibit elevated 26S proteasome activity in parallel with decreased PA700/S10B O-GlcNAcylation and PA700/S10B-OGT association.
22574218	4	44	theme	selective	704:712	arg1	activators					719:728	selective AMPK activators	704:728	selective AMPK activators	704:728	26S proteasome assembly, activity, and O-GlcNAcylation of P700 were assayed in cultured human umbilical vein endothelial cells (HUVEC) and mouse aortas isolated from C57BL6 wild type and AMPKα2 knockout mice with or without being exposed to selective AMPK activators or inhibitors.
22574218	3	45	theme	endothelial	444:454	arg1	cells					456:460	endothelial cells	444:460	endothelial cells	444:460	The present study was to investigate if AMP-activated protein kinase (AMPK) functions as a physiological suppressor of the 26S proteasome in endothelial cells.
22574218	5	46	theme	Pharmacological	745:759	arg1	activation					773:782	Pharmacological and genetic activation	745:782	Pharmacological and genetic activation of AMPK	745:790	Pharmacological and genetic activation of AMPK effectively suppresses 26S proteasomes in endothelial cells.
22574218	7	47	theme	protein	1306:1312	arg1	O-GlcNAcylation					1314:1328	protein O-GlcNAcylation	1306:1328	protein O-GlcNAcylation	1306:1328	In contrast, AMPK activation increases levels of O-GlcNAcylated PA700/S10B, likely through enhanced association of PA700 with O-GlcNAc transferase (OGT), the enzyme that catalyzes protein O-GlcNAcylation.
22574218	8	48	from	mice	1373:1376	arg1	aortas					1340:1345	aortas	1340:1345	aortas from AMPK-KO vs wild type mice	1340:1376	Finally, aortas from AMPK-KO vs wild type mice exhibit elevated 26S proteasome activity in parallel with decreased PA700/S10B O-GlcNAcylation and PA700/S10B-OGT association.
22574218	4	49	dep	isolated	615:622	arg1	exposed					693:699	exposed	693:699	being exposed to selective AMPK activators or inhibitors	687:742	26S proteasome assembly, activity, and O-GlcNAcylation of P700 were assayed in cultured human umbilical vein endothelial cells (HUVEC) and mouse aortas isolated from C57BL6 wild type and AMPKα2 knockout mice with or without being exposed to selective AMPK activators or inhibitors.
22574218	4	49	dep	isolated	615:622	arg1	cells					584:588	cultured human umbilical vein endothelial cells	542:588	cultured human umbilical vein endothelial cells (HUVEC)	542:596	26S proteasome assembly, activity, and O-GlcNAcylation of P700 were assayed in cultured human umbilical vein endothelial cells (HUVEC) and mouse aortas isolated from C57BL6 wild type and AMPKα2 knockout mice with or without being exposed to selective AMPK activators or inhibitors.
22574218	4	49	dep	isolated	615:622	arg1	with					671:674	with	671:674	with	671:674	26S proteasome assembly, activity, and O-GlcNAcylation of P700 were assayed in cultured human umbilical vein endothelial cells (HUVEC) and mouse aortas isolated from C57BL6 wild type and AMPKα2 knockout mice with or without being exposed to selective AMPK activators or inhibitors.
22574218	3	50	theme	26S	426:428	arg1	proteasome					430:439	the 26S proteasome	422:439	the 26S proteasome	422:439	The present study was to investigate if AMP-activated protein kinase (AMPK) functions as a physiological suppressor of the 26S proteasome in endothelial cells.
22574218	4	51	theme	C57BL6	629:634	arg1	type					641:644	C57BL6 wild type and AMPKα2 knockout mice	629:669	type	641:644	26S proteasome assembly, activity, and O-GlcNAcylation of P700 were assayed in cultured human umbilical vein endothelial cells (HUVEC) and mouse aortas isolated from C57BL6 wild type and AMPKα2 knockout mice with or without being exposed to selective AMPK activators or inhibitors.
22574218	0	52	theme	proteasome	18:27	arg1	Regulation					0:9	Regulation	0:9	Regulation of the proteasome by AMPK in endothelial cells: the role of O-GlcNAc transferase (OGT).	0:97	Regulation of the proteasome by AMPK in endothelial cells: the role of O-GlcNAc transferase (OGT).
22574218	5	53	theme	endothelial	834:844	arg1	cells					846:850	endothelial cells	834:850	endothelial cells	834:850	Pharmacological and genetic activation of AMPK effectively suppresses 26S proteasomes in endothelial cells.
22574218	3	54	theme	proteasome	430:439	arg1	suppressor					408:417	a physiological suppressor	392:417	a physiological suppressor of the 26S proteasome in endothelial cells	392:460	The present study was to investigate if AMP-activated protein kinase (AMPK) functions as a physiological suppressor of the 26S proteasome in endothelial cells.
22574218	3	54	theme	proteasome	430:439	arg1	kinase					365:370	AMP-activated protein kinase	343:370	AMP-activated protein kinase (AMPK)	343:377	The present study was to investigate if AMP-activated protein kinase (AMPK) functions as a physiological suppressor of the 26S proteasome in endothelial cells.
22574218	0	55	theme	endothelial	40:50	arg1	cells					52:56	endothelial cells	40:56	endothelial cells	40:56	Regulation of the proteasome by AMPK in endothelial cells: the role of O-GlcNAc transferase (OGT).
22574218	7	56	theme	enhanced	1217:1224	arg1	association					1226:1236	enhanced association	1217:1236	enhanced association of PA700 with O-GlcNAc transferase (OGT), the enzyme that catalyzes protein O-GlcNAcylation	1217:1328	In contrast, AMPK activation increases levels of O-GlcNAcylated PA700/S10B, likely through enhanced association of PA700 with O-GlcNAc transferase (OGT), the enzyme that catalyzes protein O-GlcNAcylation.
22574218	7	57	theme	O-GlcNAc	1252:1259	arg1	OGT					1274:1276	OGT	1274:1276	OGT	1274:1276	In contrast, AMPK activation increases levels of O-GlcNAcylated PA700/S10B, likely through enhanced association of PA700 with O-GlcNAc transferase (OGT), the enzyme that catalyzes protein O-GlcNAcylation.
22574218	7	57	theme	O-GlcNAc	1252:1259	arg1	transferase					1261:1271	O-GlcNAc transferase	1252:1271	O-GlcNAc transferase (OGT)	1252:1277	In contrast, AMPK activation increases levels of O-GlcNAcylated PA700/S10B, likely through enhanced association of PA700 with O-GlcNAc transferase (OGT), the enzyme that catalyzes protein O-GlcNAcylation.
22574218	7	57	theme	O-GlcNAc	1252:1259	arg1	enzyme					1284:1289	the enzyme	1280:1289	the enzyme that catalyzes protein O-GlcNAcylation	1280:1328	In contrast, AMPK activation increases levels of O-GlcNAcylated PA700/S10B, likely through enhanced association of PA700 with O-GlcNAc transferase (OGT), the enzyme that catalyzes protein O-GlcNAcylation.
22574218	6	58	theme	proteasomes	1113:1123	arg1	assembly					1097:1104	the assembly	1093:1104	the assembly of 26S proteasomes	1093:1123	Conversely, inactivation of AMPK either pharmacologically or genetically increases 26S proteasome activity; furthermore, the inactivation decreases the O-GlcNAcylation of PA700/S10B (the regulatory complex in 26S proteasomes) and increases the assembly of 26S proteasomes.
22574218	4	59	theme	P700	521:524	arg1	activity					488:495	activity	488:495	activity	488:495	26S proteasome assembly, activity, and O-GlcNAcylation of P700 were assayed in cultured human umbilical vein endothelial cells (HUVEC) and mouse aortas isolated from C57BL6 wild type and AMPKα2 knockout mice with or without being exposed to selective AMPK activators or inhibitors.
22574218	4	59	theme	P700	521:524	arg1	O-GlcNAcylation					502:516	O-GlcNAcylation	502:516	O-GlcNAcylation	502:516	26S proteasome assembly, activity, and O-GlcNAcylation of P700 were assayed in cultured human umbilical vein endothelial cells (HUVEC) and mouse aortas isolated from C57BL6 wild type and AMPKα2 knockout mice with or without being exposed to selective AMPK activators or inhibitors.
22574218	4	59	theme	P700	521:524	arg1	assembly					478:485	26S proteasome assembly	463:485	26S proteasome assembly	463:485	26S proteasome assembly, activity, and O-GlcNAcylation of P700 were assayed in cultured human umbilical vein endothelial cells (HUVEC) and mouse aortas isolated from C57BL6 wild type and AMPKα2 knockout mice with or without being exposed to selective AMPK activators or inhibitors.
22574218	7	60	with	association	1226:1236	arg1	OGT					1274:1276	OGT	1274:1276	OGT	1274:1276	In contrast, AMPK activation increases levels of O-GlcNAcylated PA700/S10B, likely through enhanced association of PA700 with O-GlcNAc transferase (OGT), the enzyme that catalyzes protein O-GlcNAcylation.
22574218	7	60	with	association	1226:1236	arg1	transferase					1261:1271	O-GlcNAc transferase	1252:1271	O-GlcNAc transferase (OGT)	1252:1277	In contrast, AMPK activation increases levels of O-GlcNAcylated PA700/S10B, likely through enhanced association of PA700 with O-GlcNAc transferase (OGT), the enzyme that catalyzes protein O-GlcNAcylation.
22574218	7	60	with	association	1226:1236	arg1	enzyme					1284:1289	the enzyme	1280:1289	the enzyme that catalyzes protein O-GlcNAcylation	1280:1328	In contrast, AMPK activation increases levels of O-GlcNAcylated PA700/S10B, likely through enhanced association of PA700 with O-GlcNAc transferase (OGT), the enzyme that catalyzes protein O-GlcNAcylation.
22574218	6	61	theme	26S	936:938	arg1	activity					951:958	26S proteasome activity	936:958	26S proteasome activity	936:958	Conversely, inactivation of AMPK either pharmacologically or genetically increases 26S proteasome activity; furthermore, the inactivation decreases the O-GlcNAcylation of PA700/S10B (the regulatory complex in 26S proteasomes) and increases the assembly of 26S proteasomes.
22574218	8	62	theme	decreased	1436:1444	arg1	O-GlcNAcylation					1457:1471	decreased PA700/S10B O-GlcNAcylation	1436:1471	decreased PA700/S10B O-GlcNAcylation	1436:1471	Finally, aortas from AMPK-KO vs wild type mice exhibit elevated 26S proteasome activity in parallel with decreased PA700/S10B O-GlcNAcylation and PA700/S10B-OGT association.
22574218	8	63	theme	proteasome	1399:1408	arg1	activity					1410:1417	elevated 26S proteasome activity	1386:1417	elevated 26S proteasome activity	1386:1417	Finally, aortas from AMPK-KO vs wild type mice exhibit elevated 26S proteasome activity in parallel with decreased PA700/S10B O-GlcNAcylation and PA700/S10B-OGT association.
22574218	8	64	theme	26S	1395:1397	arg1	activity					1410:1417	elevated 26S proteasome activity	1386:1417	elevated 26S proteasome activity	1386:1417	Finally, aortas from AMPK-KO vs wild type mice exhibit elevated 26S proteasome activity in parallel with decreased PA700/S10B O-GlcNAcylation and PA700/S10B-OGT association.
22574218	6	65	theme	regulatory	1040:1049	arg1	complex					1051:1057	the regulatory complex	1036:1057	the regulatory complex in 26S proteasomes	1036:1076	Conversely, inactivation of AMPK either pharmacologically or genetically increases 26S proteasome activity; furthermore, the inactivation decreases the O-GlcNAcylation of PA700/S10B (the regulatory complex in 26S proteasomes) and increases the assembly of 26S proteasomes.
22574218	1	66	theme	26S	99:101	arg1	complex					148:154	a macromolecular multi-subunit complex	117:154	a macromolecular multi-subunit complex responsible for recognizing, unfolding, and ultimately destroying proteins	117:229	26S proteasome is a macromolecular multi-subunit complex responsible for recognizing, unfolding, and ultimately destroying proteins.
22574218	1	66	theme	26S	99:101	arg1	proteasome					103:112	26S proteasome	99:112	26S proteasome	99:112	26S proteasome is a macromolecular multi-subunit complex responsible for recognizing, unfolding, and ultimately destroying proteins.
22574218	4	67	attach	isolated	615:622	arg2	HUVEC					591:595	HUVEC	591:595	HUVEC	591:595	26S proteasome assembly, activity, and O-GlcNAcylation of P700 were assayed in cultured human umbilical vein endothelial cells (HUVEC) and mouse aortas isolated from C57BL6 wild type and AMPKα2 knockout mice with or without being exposed to selective AMPK activators or inhibitors.
22574218	4	67	attach	isolated	615:622	arg2	exposed					693:699	exposed	693:699	being exposed to selective AMPK activators or inhibitors	687:742	26S proteasome assembly, activity, and O-GlcNAcylation of P700 were assayed in cultured human umbilical vein endothelial cells (HUVEC) and mouse aortas isolated from C57BL6 wild type and AMPKα2 knockout mice with or without being exposed to selective AMPK activators or inhibitors.
22574218	4	67	attach	isolated	615:622	arg2	with					671:674	with	671:674	with	671:674	26S proteasome assembly, activity, and O-GlcNAcylation of P700 were assayed in cultured human umbilical vein endothelial cells (HUVEC) and mouse aortas isolated from C57BL6 wild type and AMPKα2 knockout mice with or without being exposed to selective AMPK activators or inhibitors.
22574218	4	67	attach	isolated	615:622	arg1	mice					666:669	C57BL6 wild type and AMPKα2 knockout mice	629:669	mice	666:669	26S proteasome assembly, activity, and O-GlcNAcylation of P700 were assayed in cultured human umbilical vein endothelial cells (HUVEC) and mouse aortas isolated from C57BL6 wild type and AMPKα2 knockout mice with or without being exposed to selective AMPK activators or inhibitors.
22574218	4	67	attach	isolated	615:622	arg2	cells					584:588	cultured human umbilical vein endothelial cells	542:588	cultured human umbilical vein endothelial cells (HUVEC)	542:596	26S proteasome assembly, activity, and O-GlcNAcylation of P700 were assayed in cultured human umbilical vein endothelial cells (HUVEC) and mouse aortas isolated from C57BL6 wild type and AMPKα2 knockout mice with or without being exposed to selective AMPK activators or inhibitors.
22574218	4	67	attach	isolated	615:622	arg1	type					641:644	C57BL6 wild type and AMPKα2 knockout mice	629:669	type	641:644	26S proteasome assembly, activity, and O-GlcNAcylation of P700 were assayed in cultured human umbilical vein endothelial cells (HUVEC) and mouse aortas isolated from C57BL6 wild type and AMPKα2 knockout mice with or without being exposed to selective AMPK activators or inhibitors.
22574218	4	68	gly	O-GlcNAcylation	502:516	arg1	aortas					608:613	mouse aortas	602:613	mouse aortas	602:613	26S proteasome assembly, activity, and O-GlcNAcylation of P700 were assayed in cultured human umbilical vein endothelial cells (HUVEC) and mouse aortas isolated from C57BL6 wild type and AMPKα2 knockout mice with or without being exposed to selective AMPK activators or inhibitors.
22574218	4	68	gly	O-GlcNAcylation	502:516	arg1	exposed					693:699	exposed	693:699	being exposed to selective AMPK activators or inhibitors	687:742	26S proteasome assembly, activity, and O-GlcNAcylation of P700 were assayed in cultured human umbilical vein endothelial cells (HUVEC) and mouse aortas isolated from C57BL6 wild type and AMPKα2 knockout mice with or without being exposed to selective AMPK activators or inhibitors.
22574218	4	68	gly	O-GlcNAcylation	502:516	arg1	HUVEC					591:595	HUVEC	591:595	HUVEC	591:595	26S proteasome assembly, activity, and O-GlcNAcylation of P700 were assayed in cultured human umbilical vein endothelial cells (HUVEC) and mouse aortas isolated from C57BL6 wild type and AMPKα2 knockout mice with or without being exposed to selective AMPK activators or inhibitors.
22574218	4	68	gly	O-GlcNAcylation	502:516	arg1	with					671:674	with	671:674	with	671:674	26S proteasome assembly, activity, and O-GlcNAcylation of P700 were assayed in cultured human umbilical vein endothelial cells (HUVEC) and mouse aortas isolated from C57BL6 wild type and AMPKα2 knockout mice with or without being exposed to selective AMPK activators or inhibitors.
22574218	4	68	gly	O-GlcNAcylation	502:516	arg1	cells					584:588	cultured human umbilical vein endothelial cells	542:588	cultured human umbilical vein endothelial cells (HUVEC)	542:596	26S proteasome assembly, activity, and O-GlcNAcylation of P700 were assayed in cultured human umbilical vein endothelial cells (HUVEC) and mouse aortas isolated from C57BL6 wild type and AMPKα2 knockout mice with or without being exposed to selective AMPK activators or inhibitors.
22574218	4	69	theme	AMPKα2	650:655	arg1	mice					666:669	C57BL6 wild type and AMPKα2 knockout mice	629:669	mice	666:669	26S proteasome assembly, activity, and O-GlcNAcylation of P700 were assayed in cultured human umbilical vein endothelial cells (HUVEC) and mouse aortas isolated from C57BL6 wild type and AMPKα2 knockout mice with or without being exposed to selective AMPK activators or inhibitors.
22574218	9	70	theme	26S	1586:1588	arg1	proteasomes					1590:1600	26S proteasomes	1586:1600	26S proteasomes	1586:1600	Taken together, we conclude that AMPK functions as a physiological suppressor of 26S proteasomes.
22574218	5	71	theme	genetic	765:771	arg1	activation					773:782	Pharmacological and genetic activation	745:782	Pharmacological and genetic activation of AMPK	745:790	Pharmacological and genetic activation of AMPK effectively suppresses 26S proteasomes in endothelial cells.
22574218	0	72	dep	Regulation	0:9	arg1	role					63:66	the role	59:66	Regulation of the proteasome by AMPK in endothelial cells: the role of O-GlcNAc transferase (OGT).	0:97	Regulation of the proteasome by AMPK in endothelial cells: the role of O-GlcNAc transferase (OGT).
22574218	6	73	theme	26S	1109:1111	arg1	proteasomes					1113:1123	26S proteasomes	1109:1123	26S proteasomes	1109:1123	Conversely, inactivation of AMPK either pharmacologically or genetically increases 26S proteasome activity; furthermore, the inactivation decreases the O-GlcNAcylation of PA700/S10B (the regulatory complex in 26S proteasomes) and increases the assembly of 26S proteasomes.
22574218	6	74	theme	PA700/S10B	1024:1033	arg1	O-GlcNAcylation					1005:1019	the O-GlcNAcylation	1001:1019	the O-GlcNAcylation of PA700/S10B (the regulatory complex in 26S proteasomes)	1001:1077	Conversely, inactivation of AMPK either pharmacologically or genetically increases 26S proteasome activity; furthermore, the inactivation decreases the O-GlcNAcylation of PA700/S10B (the regulatory complex in 26S proteasomes) and increases the assembly of 26S proteasomes.
27505673	0	0	theme	Survival	72:79	arg1	Mechanisms					81:90	c-MYC-Dependent Survival Mechanisms	56:90	c-MYC-Dependent Survival Mechanisms	56:90	Regulation of OGT by URI in Response to Glucose Confers c-MYC-Dependent Survival Mechanisms.
27505673	1	1	theme	nutrient	138:145	arg1	conditions					147:156	low nutrient conditions	134:156	low nutrient conditions	134:156	Cancer cells can adapt and survive under low nutrient conditions, but underlying mechanisms remain poorly explored.
27505673	0	2	theme	c-MYC-Dependent	56:70	arg1	Mechanisms					81:90	c-MYC-Dependent Survival Mechanisms	56:90	c-MYC-Dependent Survival Mechanisms	56:90	Regulation of OGT by URI in Response to Glucose Confers c-MYC-Dependent Survival Mechanisms.
27505673	4	3	theme	Low	504:506	arg1	activity					512:519	Low OGT activity	504:519	Low OGT activity	504:519	Low OGT activity reduces O-GlcNAcylation and promotes c-MYC degradation to maintain cell survival.
27505673	6	4	theme	liver	819:823	arg1	tumorigenesis					825:837	liver tumorigenesis	819:837	liver tumorigenesis in agreement with c-MYC oncogenic functions	819:881	Accordingly, mice expressing non-phosphorylatable URI (S371A) in hepatocytes exhibit high OGT activity and c-MYC stabilization, accelerating liver tumorigenesis in agreement with c-MYC oncogenic functions.
27505673	0	5	from	Regulation	0:9	arg1	Response					28:35	Response	28:35	Response to Glucose	28:46	Regulation of OGT by URI in Response to Glucose Confers c-MYC-Dependent Survival Mechanisms.
27505673	2	6	theme	co-chaperone	285:296	arg1	URI					298:300	the co-chaperone URI	281:300	the co-chaperone URI	281:300	We demonstrate here that glucose maintains a functional complex between the co-chaperone URI, PP1γ, and OGT, the enzyme catalyzing O-GlcNAcylation.
27505673	3	7	theme	OGT	488:490	arg1	inhibition					492:501	URI-mediated OGT inhibition	475:501	URI-mediated OGT inhibition	475:501	Glucose deprivation induces the activation of PKA, which phosphorylates URI at Ser-371, resulting in PP1γ release and URI-mediated OGT inhibition.
27505673	6	8	theme	non-phosphorylatable	707:726	arg1	S371A					733:737	S371A	733:737	S371A	733:737	Accordingly, mice expressing non-phosphorylatable URI (S371A) in hepatocytes exhibit high OGT activity and c-MYC stabilization, accelerating liver tumorigenesis in agreement with c-MYC oncogenic functions.
27505673	6	8	theme	non-phosphorylatable	707:726	arg1	URI					728:730	non-phosphorylatable URI	707:730	non-phosphorylatable URI (S371A) in hepatocytes	707:753	Accordingly, mice expressing non-phosphorylatable URI (S371A) in hepatocytes exhibit high OGT activity and c-MYC stabilization, accelerating liver tumorigenesis in agreement with c-MYC oncogenic functions.
27505673	4	9	theme	cell	588:591	arg1	survival					593:600	cell survival	588:600	cell survival	588:600	Low OGT activity reduces O-GlcNAcylation and promotes c-MYC degradation to maintain cell survival.
27505673	7	10	theme	glucose	983:989	arg1	fluctuations					991:1002	glucose fluctuations	983:1002	glucose fluctuations	983:1002	Our work uncovers that URI-regulated OGT confers c-MYC-dependent survival functions in response to glucose fluctuations.
27505673	6	11	theme	c-MYC	785:789	arg1	stabilization					791:803	c-MYC stabilization	785:803	c-MYC stabilization	785:803	Accordingly, mice expressing non-phosphorylatable URI (S371A) in hepatocytes exhibit high OGT activity and c-MYC stabilization, accelerating liver tumorigenesis in agreement with c-MYC oncogenic functions.
27505673	1	12	theme	underlying	163:172	arg1	mechanisms					174:183	underlying mechanisms	163:183	underlying mechanisms	163:183	Cancer cells can adapt and survive under low nutrient conditions, but underlying mechanisms remain poorly explored.
27505673	5	13	theme	PP1γ-bound	631:640	arg1	URI					642:644	PP1γ-bound URI	631:644	PP1γ-bound URI	631:644	In the presence of glucose, PP1γ-bound URI increases OGT and c-MYC levels.
27505673	7	14	theme	survival	949:956	arg1	functions					958:966	c-MYC-dependent survival functions	933:966	c-MYC-dependent survival functions	933:966	Our work uncovers that URI-regulated OGT confers c-MYC-dependent survival functions in response to glucose fluctuations.
27505673	3	15	theme	Glucose	357:363	arg1	deprivation					365:375	Glucose deprivation	357:375	Glucose deprivation	357:375	Glucose deprivation induces the activation of PKA, which phosphorylates URI at Ser-371, resulting in PP1γ release and URI-mediated OGT inhibition.
27505673	6	16	theme	OGT	768:770	arg1	activity					772:779	high OGT activity	763:779	high OGT activity	763:779	Accordingly, mice expressing non-phosphorylatable URI (S371A) in hepatocytes exhibit high OGT activity and c-MYC stabilization, accelerating liver tumorigenesis in agreement with c-MYC oncogenic functions.
27505673	1	17	theme	Cancer	93:98	arg1	cells					100:104	Cancer cells	93:104	Cancer cells	93:104	Cancer cells can adapt and survive under low nutrient conditions, but underlying mechanisms remain poorly explored.
27505673	0	18	theme	OGT	14:16	arg1	Regulation					0:9	Regulation	0:9	Regulation of OGT by URI in Response to Glucose	0:46	Regulation of OGT by URI in Response to Glucose Confers c-MYC-Dependent Survival Mechanisms.
27505673	3	19	theme	PKA	403:405	arg1	activation					389:398	the activation	385:398	the activation	385:398	Glucose deprivation induces the activation of PKA, which phosphorylates URI at Ser-371, resulting in PP1γ release and URI-mediated OGT inhibition.
27505673	4	20	theme	c-MYC	558:562	arg1	degradation					564:574	c-MYC degradation	558:574	c-MYC degradation to maintain cell survival	558:600	Low OGT activity reduces O-GlcNAcylation and promotes c-MYC degradation to maintain cell survival.
27505673	6	21	from	tumorigenesis	825:837	arg1	agreement					842:850	agreement	842:850	agreement with c-MYC oncogenic functions	842:881	Accordingly, mice expressing non-phosphorylatable URI (S371A) in hepatocytes exhibit high OGT activity and c-MYC stabilization, accelerating liver tumorigenesis in agreement with c-MYC oncogenic functions.
27505673	6	22	theme	oncogenic	863:871	arg1	functions					873:881	c-MYC oncogenic functions	857:881	c-MYC oncogenic functions	857:881	Accordingly, mice expressing non-phosphorylatable URI (S371A) in hepatocytes exhibit high OGT activity and c-MYC stabilization, accelerating liver tumorigenesis in agreement with c-MYC oncogenic functions.
27505673	6	23	theme	high	763:766	arg1	activity					772:779	high OGT activity	763:779	high OGT activity	763:779	Accordingly, mice expressing non-phosphorylatable URI (S371A) in hepatocytes exhibit high OGT activity and c-MYC stabilization, accelerating liver tumorigenesis in agreement with c-MYC oncogenic functions.
27505673	6	24	with	agreement	842:850	arg1	functions					873:881	c-MYC oncogenic functions	857:881	c-MYC oncogenic functions	857:881	Accordingly, mice expressing non-phosphorylatable URI (S371A) in hepatocytes exhibit high OGT activity and c-MYC stabilization, accelerating liver tumorigenesis in agreement with c-MYC oncogenic functions.
27505673	4	25	theme	OGT	508:510	arg1	activity					512:519	Low OGT activity	504:519	Low OGT activity	504:519	Low OGT activity reduces O-GlcNAcylation and promotes c-MYC degradation to maintain cell survival.
27505673	5	26	theme	c-MYC	664:668	arg1	levels					670:675	c-MYC levels	664:675	c-MYC levels	664:675	In the presence of glucose, PP1γ-bound URI increases OGT and c-MYC levels.
27505673	6	27	theme	c-MYC	857:861	arg1	functions					873:881	c-MYC oncogenic functions	857:881	c-MYC oncogenic functions	857:881	Accordingly, mice expressing non-phosphorylatable URI (S371A) in hepatocytes exhibit high OGT activity and c-MYC stabilization, accelerating liver tumorigenesis in agreement with c-MYC oncogenic functions.
27505673	5	28	dep	glucose	622:628	arg1	the					606:608	the	606:608	the	606:608	In the presence of glucose, PP1γ-bound URI increases OGT and c-MYC levels.
27505673	5	28	dep	glucose	622:628	arg1	presence					610:617	presence	610:617	presence	610:617	In the presence of glucose, PP1γ-bound URI increases OGT and c-MYC levels.
27505673	3	29	theme	URI-mediated	475:486	arg1	inhibition					492:501	URI-mediated OGT inhibition	475:501	URI-mediated OGT inhibition	475:501	Glucose deprivation induces the activation of PKA, which phosphorylates URI at Ser-371, resulting in PP1γ release and URI-mediated OGT inhibition.
27505673	2	30	theme	functional	254:263	arg1	complex					265:271	a functional complex	252:271	a functional complex between the co-chaperone URI, PP1γ, and OGT	252:315	We demonstrate here that glucose maintains a functional complex between the co-chaperone URI, PP1γ, and OGT, the enzyme catalyzing O-GlcNAcylation.
27505673	2	30	theme	functional	254:263	arg1	enzyme					322:327	the enzyme	318:327	the enzyme catalyzing O-GlcNAcylation	318:354	We demonstrate here that glucose maintains a functional complex between the co-chaperone URI, PP1γ, and OGT, the enzyme catalyzing O-GlcNAcylation.
27505673	3	31	theme	PP1γ	458:461	arg1	release					463:469	PP1γ release	458:469	PP1γ release	458:469	Glucose deprivation induces the activation of PKA, which phosphorylates URI at Ser-371, resulting in PP1γ release and URI-mediated OGT inhibition.
27505673	7	32	theme	c-MYC-dependent	933:947	arg1	functions					958:966	c-MYC-dependent survival functions	933:966	c-MYC-dependent survival functions	933:966	Our work uncovers that URI-regulated OGT confers c-MYC-dependent survival functions in response to glucose fluctuations.
27505673	6	33	from	URI	728:730	arg1	hepatocytes					743:753	hepatocytes	743:753	hepatocytes	743:753	Accordingly, mice expressing non-phosphorylatable URI (S371A) in hepatocytes exhibit high OGT activity and c-MYC stabilization, accelerating liver tumorigenesis in agreement with c-MYC oncogenic functions.
27505673	7	34	theme	URI-regulated	907:919	arg1	OGT					921:923	URI-regulated OGT	907:923	URI-regulated OGT	907:923	Our work uncovers that URI-regulated OGT confers c-MYC-dependent survival functions in response to glucose fluctuations.
27505673	1	35	theme	low	134:136	arg1	conditions					147:156	low nutrient conditions	134:156	low nutrient conditions	134:156	Cancer cells can adapt and survive under low nutrient conditions, but underlying mechanisms remain poorly explored.
32885474	0	0	theme	disrupted	84:92	arg1	homeostasis					102:112	disrupted calcium homeostasis	84:112	disrupted calcium homeostasis	84:112	Amyloid beta regulates ER exit sites formation through O-GlcNAcylation triggered by disrupted calcium homeostasis.
32885474	5	1	theme	COPII	724:728	arg1	vesicles					730:737	COPII vesicles	724:737	COPII vesicles	724:737	RESULTS In this study, we observed that disrupted calcium levels affected the formation of COPII vesicles in ERES through calcium-triggered O-GlcNAcylation of Sec31A.
32885474	8	2	theme	Golgi	1016:1020	arg1	fragmentation					1022:1034	Golgi fragmentation	1016:1034	Golgi fragmentation by Aβ	1016:1040	Golgi fragmentation by Aβ was rescued by up-regulation of O-GlcNAcylaion levels using Thiamet G (ThiG), an O-GlcNAcase inhibitor.
32885474	11	3	dep	SIGNIFICANCE	1492:1503	arg1	findings					1509:1516	The findings	1505:1516	SIGNIFICANCE The findings of this study	1492:1530	SIGNIFICANCE The findings of this study suggested that protection of ERES or Sec31 O-GlcNAcylation may offer a promising novel avenue for development of AD therapeutics.
32885474	8	4	theme	Thiamet	1102:1108	arg1	inhibitor					1135:1143	an O-GlcNAcase inhibitor	1120:1143	an O-GlcNAcase inhibitor	1120:1143	Golgi fragmentation by Aβ was rescued by up-regulation of O-GlcNAcylaion levels using Thiamet G (ThiG), an O-GlcNAcase inhibitor.
32885474	8	4	theme	Thiamet	1102:1108	arg1	ThiG					1113:1116	ThiG	1113:1116	ThiG	1113:1116	Golgi fragmentation by Aβ was rescued by up-regulation of O-GlcNAcylaion levels using Thiamet G (ThiG), an O-GlcNAcase inhibitor.
32885474	8	4	theme	Thiamet	1102:1108	arg1	G					1110:1110	Thiamet G	1102:1110	Thiamet G (ThiG)	1102:1117	Golgi fragmentation by Aβ was rescued by up-regulation of O-GlcNAcylaion levels using Thiamet G (ThiG), an O-GlcNAcase inhibitor.
32885474	4	5	theme	unique	540:545	arg1	O-GlcNAcylation					521:535	O-GlcNAcylation	521:535	O-GlcNAcylation	521:535	O-GlcNAcylation, a unique and dynamic protein glycosylation process, modulates the formation of COPII vesicles.
32885474	4	5	theme	unique	540:545	arg1	process					581:587	a unique and dynamic protein glycosylation process	538:587	a unique and dynamic protein glycosylation process	538:587	O-GlcNAcylation, a unique and dynamic protein glycosylation process, modulates the formation of COPII vesicles.
32885474	5	6	theme	vesicles	730:737	arg1	formation					711:719	the formation	707:719	the formation of COPII vesicles in ERES	707:745	RESULTS In this study, we observed that disrupted calcium levels affected the formation of COPII vesicles in ERES through calcium-triggered O-GlcNAcylation of Sec31A.
32885474	9	7	theme	COPII	1274:1278	arg1	vesicles					1280:1287	COPII vesicles	1274:1287	COPII vesicles	1274:1287	Additionally, we observed that the Golgi reassembly stacking proteins having a function in Golgi stacking showed attenuation at COPII vesicles following Aβ treatment.
32885474	3	8	from	sites	474:478	arg1	vesicles					454:461	coat protein complex II (COPII) vesicles	422:461	coat protein complex II (COPII) vesicles at ER exit sites (ERES)	422:485	Previously, we demonstrated that Sec31A, a main component for coat protein complex II (COPII) vesicles at ER exit sites (ERES), is modulated by O-GlcNAcylation.
32885474	2	9	theme	vesicles	350:357	arg1	trafficking					335:345	trafficking	335:345	trafficking	335:345	Calcium is required for the fusion and trafficking of vesicles.
32885474	2	9	theme	vesicles	350:357	arg1	fusion					324:329	fusion	324:329	fusion	324:329	Calcium is required for the fusion and trafficking of vesicles.
32885474	11	10	theme	study	1526:1530	arg1	SIGNIFICANCE					1492:1503	SIGNIFICANCE	1492:1503	SIGNIFICANCE The findings of this study	1492:1530	SIGNIFICANCE The findings of this study suggested that protection of ERES or Sec31 O-GlcNAcylation may offer a promising novel avenue for development of AD therapeutics.
32885474	10	11	theme	intracellular	1457:1469	arg1	homeostasis					1479:1489	intracellular calcium homeostasis	1457:1489	intracellular calcium homeostasis	1457:1489	CONCLUSIONS This study demonstrated that Aβ impaired Sec31A targeting to ERES through altered Sec31A O-GlcNAcylation triggered by disruption of intracellular calcium homeostasis.
32885474	5	12	theme	calcium	683:689	arg1	levels					691:696	disrupted calcium levels	673:696	disrupted calcium levels	673:696	RESULTS In this study, we observed that disrupted calcium levels affected the formation of COPII vesicles in ERES through calcium-triggered O-GlcNAcylation of Sec31A.
32885474	11	13	theme	Sec31	1569:1573	arg1	O-GlcNAcylation					1575:1589	Sec31 O-GlcNAcylation	1569:1589	Sec31 O-GlcNAcylation	1569:1589	SIGNIFICANCE The findings of this study suggested that protection of ERES or Sec31 O-GlcNAcylation may offer a promising novel avenue for development of AD therapeutics.
32885474	4	14	theme	vesicles	623:630	arg1	formation					604:612	the formation	600:612	the formation of COPII vesicles	600:630	O-GlcNAcylation, a unique and dynamic protein glycosylation process, modulates the formation of COPII vesicles.
32885474	4	15	theme	dynamic	551:557	arg1	O-GlcNAcylation					521:535	O-GlcNAcylation	521:535	O-GlcNAcylation	521:535	O-GlcNAcylation, a unique and dynamic protein glycosylation process, modulates the formation of COPII vesicles.
32885474	4	15	theme	dynamic	551:557	arg1	process					581:587	a unique and dynamic protein glycosylation process	538:587	a unique and dynamic protein glycosylation process	538:587	O-GlcNAcylation, a unique and dynamic protein glycosylation process, modulates the formation of COPII vesicles.
32885474	0	16	theme	calcium	94:100	arg1	homeostasis					102:112	disrupted calcium homeostasis	84:112	disrupted calcium homeostasis	84:112	Amyloid beta regulates ER exit sites formation through O-GlcNAcylation triggered by disrupted calcium homeostasis.
32885474	6	17	from	homeostasis	874:884	arg1	cells					928:932	neuronal cells	919:932	neuronal cells	919:932	Additionally, we found that Aβ impaired ERES through Aβ-disturbed calcium homeostasis and O-GlcNAcylation of Sec31A in neuronal cells.
32885474	3	18	theme	ER	466:467	arg1	ERES					481:484	ERES	481:484	ERES	481:484	Previously, we demonstrated that Sec31A, a main component for coat protein complex II (COPII) vesicles at ER exit sites (ERES), is modulated by O-GlcNAcylation.
32885474	3	18	theme	ER	466:467	arg1	sites					474:478	ER exit sites	466:478	ER exit sites (ERES)	466:485	Previously, we demonstrated that Sec31A, a main component for coat protein complex II (COPII) vesicles at ER exit sites (ERES), is modulated by O-GlcNAcylation.
32885474	11	19	theme	ERES	1561:1564	arg1	protection					1547:1556	protection	1547:1556	protection of ERES or Sec31 O-GlcNAcylation	1547:1589	SIGNIFICANCE The findings of this study suggested that protection of ERES or Sec31 O-GlcNAcylation may offer a promising novel avenue for development of AD therapeutics.
32885474	3	20	theme	protein	427:433	arg1	vesicles					454:461	coat protein complex II (COPII) vesicles	422:461	coat protein complex II (COPII) vesicles at ER exit sites (ERES)	422:485	Previously, we demonstrated that Sec31A, a main component for coat protein complex II (COPII) vesicles at ER exit sites (ERES), is modulated by O-GlcNAcylation.
32885474	6	21	theme	Aβ-disturbed	853:864	arg1	homeostasis					874:884	Aβ-disturbed calcium homeostasis	853:884	Aβ-disturbed calcium homeostasis	853:884	Additionally, we found that Aβ impaired ERES through Aβ-disturbed calcium homeostasis and O-GlcNAcylation of Sec31A in neuronal cells.
32885474	3	22	theme	main	403:406	arg1	Sec31A					393:398	Sec31A	393:398	Sec31A	393:398	Previously, we demonstrated that Sec31A, a main component for coat protein complex II (COPII) vesicles at ER exit sites (ERES), is modulated by O-GlcNAcylation.
32885474	3	22	theme	main	403:406	arg1	component					408:416	a main component	401:416	a main component for coat protein complex II (COPII) vesicles at ER exit sites (ERES)	401:485	Previously, we demonstrated that Sec31A, a main component for coat protein complex II (COPII) vesicles at ER exit sites (ERES), is modulated by O-GlcNAcylation.
32885474	4	23	theme	protein	559:565	arg1	O-GlcNAcylation					521:535	O-GlcNAcylation	521:535	O-GlcNAcylation	521:535	O-GlcNAcylation, a unique and dynamic protein glycosylation process, modulates the formation of COPII vesicles.
32885474	4	23	theme	protein	559:565	arg1	process					581:587	a unique and dynamic protein glycosylation process	538:587	a unique and dynamic protein glycosylation process	538:587	O-GlcNAcylation, a unique and dynamic protein glycosylation process, modulates the formation of COPII vesicles.
32885474	3	24	theme	complex	435:441	arg1	vesicles					454:461	coat protein complex II (COPII) vesicles	422:461	coat protein complex II (COPII) vesicles at ER exit sites (ERES)	422:485	Previously, we demonstrated that Sec31A, a main component for coat protein complex II (COPII) vesicles at ER exit sites (ERES), is modulated by O-GlcNAcylation.
32885474	10	25	theme	homeostasis	1479:1489	arg1	disruption					1443:1452	disruption	1443:1452	disruption of intracellular calcium homeostasis	1443:1489	CONCLUSIONS This study demonstrated that Aβ impaired Sec31A targeting to ERES through altered Sec31A O-GlcNAcylation triggered by disruption of intracellular calcium homeostasis.
32885474	9	26	theme	Golgi	1181:1185	arg1	reassembly					1187:1196	the Golgi reassembly	1177:1196	the Golgi reassembly stacking proteins having a function in Golgi stacking	1177:1250	Additionally, we observed that the Golgi reassembly stacking proteins having a function in Golgi stacking showed attenuation at COPII vesicles following Aβ treatment.
32885474	6	27	theme	calcium	866:872	arg1	homeostasis					874:884	Aβ-disturbed calcium homeostasis	853:884	Aβ-disturbed calcium homeostasis	853:884	Additionally, we found that Aβ impaired ERES through Aβ-disturbed calcium homeostasis and O-GlcNAcylation of Sec31A in neuronal cells.
32885474	0	28	theme	Amyloid	0:6	arg1	beta					8:11	Amyloid beta	0:11	Amyloid beta	0:11	Amyloid beta regulates ER exit sites formation through O-GlcNAcylation triggered by disrupted calcium homeostasis.
32885474	10	29	theme	calcium	1471:1477	arg1	homeostasis					1479:1489	intracellular calcium homeostasis	1457:1489	intracellular calcium homeostasis	1457:1489	CONCLUSIONS This study demonstrated that Aβ impaired Sec31A targeting to ERES through altered Sec31A O-GlcNAcylation triggered by disruption of intracellular calcium homeostasis.
32885474	10	30	theme	Sec31A	1407:1412	arg1	O-GlcNAcylation					1414:1428	altered Sec31A O-GlcNAcylation	1399:1428	altered Sec31A O-GlcNAcylation triggered by disruption of intracellular calcium homeostasis	1399:1489	CONCLUSIONS This study demonstrated that Aβ impaired Sec31A targeting to ERES through altered Sec31A O-GlcNAcylation triggered by disruption of intracellular calcium homeostasis.
32885474	2	31	dep	fusion	324:329	arg1	the					320:322	the	320:322	the	320:322	Calcium is required for the fusion and trafficking of vesicles.
32885474	9	32	from	vesicles	1280:1287	arg1	attenuation					1259:1269	attenuation	1259:1269	attenuation at COPII vesicles	1259:1287	Additionally, we observed that the Golgi reassembly stacking proteins having a function in Golgi stacking showed attenuation at COPII vesicles following Aβ treatment.
32885474	3	33	theme	coat	422:425	arg1	vesicles					454:461	coat protein complex II (COPII) vesicles	422:461	coat protein complex II (COPII) vesicles at ER exit sites (ERES)	422:485	Previously, we demonstrated that Sec31A, a main component for coat protein complex II (COPII) vesicles at ER exit sites (ERES), is modulated by O-GlcNAcylation.
32885474	0	34	theme	ER	23:24	arg1	sites					31:35	ER exit sites	23:35	ER exit sites formation	23:45	Amyloid beta regulates ER exit sites formation through O-GlcNAcylation triggered by disrupted calcium homeostasis.
32885474	11	35	theme	O-GlcNAcylation	1575:1589	arg1	protection					1547:1556	protection	1547:1556	protection of ERES or Sec31 O-GlcNAcylation	1547:1589	SIGNIFICANCE The findings of this study suggested that protection of ERES or Sec31 O-GlcNAcylation may offer a promising novel avenue for development of AD therapeutics.
32885474	10	36	theme	altered	1399:1405	arg1	O-GlcNAcylation					1414:1428	altered Sec31A O-GlcNAcylation	1399:1428	altered Sec31A O-GlcNAcylation triggered by disruption of intracellular calcium homeostasis	1399:1489	CONCLUSIONS This study demonstrated that Aβ impaired Sec31A targeting to ERES through altered Sec31A O-GlcNAcylation triggered by disruption of intracellular calcium homeostasis.
32885474	10	37	dep	CONCLUSIONS	1313:1323	arg1	demonstrated					1336:1347	demonstrated	1336:1347	demonstrated that Aβ impaired Sec31A targeting to ERES through altered Sec31A O-GlcNAcylation triggered by disruption of intracellular calcium homeostasis	1336:1489	CONCLUSIONS This study demonstrated that Aβ impaired Sec31A targeting to ERES through altered Sec31A O-GlcNAcylation triggered by disruption of intracellular calcium homeostasis.
32885474	3	38	theme	COPII	447:451	arg1	vesicles					454:461	coat protein complex II (COPII) vesicles	422:461	coat protein complex II (COPII) vesicles at ER exit sites (ERES)	422:485	Previously, we demonstrated that Sec31A, a main component for coat protein complex II (COPII) vesicles at ER exit sites (ERES), is modulated by O-GlcNAcylation.
32885474	11	39	theme	therapeutics	1648:1659	arg1	development					1630:1640	development	1630:1640	development of AD therapeutics	1630:1659	SIGNIFICANCE The findings of this study suggested that protection of ERES or Sec31 O-GlcNAcylation may offer a promising novel avenue for development of AD therapeutics.
32885474	11	40	theme	promising	1603:1611	arg1	avenue					1619:1624	a promising novel avenue	1601:1624	a promising novel avenue for development of AD therapeutics	1601:1659	SIGNIFICANCE The findings of this study suggested that protection of ERES or Sec31 O-GlcNAcylation may offer a promising novel avenue for development of AD therapeutics.
32885474	1	41	theme	BACKGROUND	115:124	arg1	INFORMATION					126:136	BACKGROUND INFORMATION	115:136	BACKGROUND INFORMATION Aberrant production of amyloid beta (Aβ)	115:177	BACKGROUND INFORMATION Aberrant production of amyloid beta (Aβ) causes disruption of intracellular calcium homeostasis, a crucial factor in the pathogenesis of Alzheimer's disease.
32885474	1	42	theme	calcium	214:220	arg1	factor					245:250	a crucial factor	235:250	a crucial factor in the pathogenesis of Alzheimer's disease	235:293	BACKGROUND INFORMATION Aberrant production of amyloid beta (Aβ) causes disruption of intracellular calcium homeostasis, a crucial factor in the pathogenesis of Alzheimer's disease.
32885474	1	42	theme	calcium	214:220	arg1	homeostasis					222:232	intracellular calcium homeostasis	200:232	intracellular calcium homeostasis	200:232	BACKGROUND INFORMATION Aberrant production of amyloid beta (Aβ) causes disruption of intracellular calcium homeostasis, a crucial factor in the pathogenesis of Alzheimer's disease.
32885474	0	43	theme	sites	31:35	arg1	formation					37:45	ER exit sites formation	23:45	ER exit sites formation	23:45	Amyloid beta regulates ER exit sites formation through O-GlcNAcylation triggered by disrupted calcium homeostasis.
32885474	3	44	theme	exit	469:472	arg1	ERES					481:484	ERES	481:484	ERES	481:484	Previously, we demonstrated that Sec31A, a main component for coat protein complex II (COPII) vesicles at ER exit sites (ERES), is modulated by O-GlcNAcylation.
32885474	3	44	theme	exit	469:472	arg1	sites					474:478	ER exit sites	466:478	ER exit sites (ERES)	466:485	Previously, we demonstrated that Sec31A, a main component for coat protein complex II (COPII) vesicles at ER exit sites (ERES), is modulated by O-GlcNAcylation.
32885474	8	45	theme	levels	1089:1094	arg1	up-regulation					1057:1069	up-regulation	1057:1069	up-regulation of O-GlcNAcylaion levels	1057:1094	Golgi fragmentation by Aβ was rescued by up-regulation of O-GlcNAcylaion levels using Thiamet G (ThiG), an O-GlcNAcase inhibitor.
32885474	3	46	theme	II	443:444	arg1	vesicles					454:461	coat protein complex II (COPII) vesicles	422:461	coat protein complex II (COPII) vesicles at ER exit sites (ERES)	422:485	Previously, we demonstrated that Sec31A, a main component for coat protein complex II (COPII) vesicles at ER exit sites (ERES), is modulated by O-GlcNAcylation.
32885474	1	47	theme	homeostasis	222:232	arg1	disruption					186:195	disruption	186:195	disruption of intracellular calcium homeostasis, a crucial factor in the pathogenesis of Alzheimer's disease	186:293	BACKGROUND INFORMATION Aberrant production of amyloid beta (Aβ) causes disruption of intracellular calcium homeostasis, a crucial factor in the pathogenesis of Alzheimer's disease.
32885474	0	48	theme	exit	26:29	arg1	sites					31:35	ER exit sites	23:35	ER exit sites formation	23:45	Amyloid beta regulates ER exit sites formation through O-GlcNAcylation triggered by disrupted calcium homeostasis.
32885474	5	49	theme	disrupted	673:681	arg1	levels					691:696	disrupted calcium levels	673:696	disrupted calcium levels	673:696	RESULTS In this study, we observed that disrupted calcium levels affected the formation of COPII vesicles in ERES through calcium-triggered O-GlcNAcylation of Sec31A.
32885474	11	50	theme	AD	1645:1646	arg1	therapeutics					1648:1659	AD therapeutics	1645:1659	AD therapeutics	1645:1659	SIGNIFICANCE The findings of this study suggested that protection of ERES or Sec31 O-GlcNAcylation may offer a promising novel avenue for development of AD therapeutics.
32885474	5	51	theme	Sec31A	792:797	arg1	O-GlcNAcylation					773:787	calcium-triggered O-GlcNAcylation	755:787	calcium-triggered O-GlcNAcylation of Sec31A	755:797	RESULTS In this study, we observed that disrupted calcium levels affected the formation of COPII vesicles in ERES through calcium-triggered O-GlcNAcylation of Sec31A.
32885474	1	52	from	factor	245:250	arg1	pathogenesis					259:270	the pathogenesis	255:270	the pathogenesis of Alzheimer's disease	255:293	BACKGROUND INFORMATION Aberrant production of amyloid beta (Aβ) causes disruption of intracellular calcium homeostasis, a crucial factor in the pathogenesis of Alzheimer's disease.
32885474	7	53	theme	Golgi	1009:1013	arg1	structure					996:1004	the ribbon-like structure	980:1004	the ribbon-like structure of Golgi	980:1013	Furthermore, we identified that Aβ disrupted the ribbon-like structure of Golgi.
32885474	1	54	theme	INFORMATION	126:136	arg1	production					147:156	BACKGROUND INFORMATION Aberrant production	115:156	BACKGROUND INFORMATION Aberrant production of amyloid beta (Aβ)	115:177	BACKGROUND INFORMATION Aberrant production of amyloid beta (Aβ) causes disruption of intracellular calcium homeostasis, a crucial factor in the pathogenesis of Alzheimer's disease.
32885474	5	55	theme	calcium-triggered	755:771	arg1	O-GlcNAcylation					773:787	calcium-triggered O-GlcNAcylation	755:787	calcium-triggered O-GlcNAcylation of Sec31A	755:797	RESULTS In this study, we observed that disrupted calcium levels affected the formation of COPII vesicles in ERES through calcium-triggered O-GlcNAcylation of Sec31A.
32885474	6	56	theme	neuronal	919:926	arg1	cells					928:932	neuronal cells	919:932	neuronal cells	919:932	Additionally, we found that Aβ impaired ERES through Aβ-disturbed calcium homeostasis and O-GlcNAcylation of Sec31A in neuronal cells.
32885474	7	57	theme	ribbon-like	984:994	arg1	structure					996:1004	the ribbon-like structure	980:1004	the ribbon-like structure of Golgi	980:1013	Furthermore, we identified that Aβ disrupted the ribbon-like structure of Golgi.
32885474	1	58	theme	Aberrant	138:145	arg1	production					147:156	BACKGROUND INFORMATION Aberrant production	115:156	BACKGROUND INFORMATION Aberrant production of amyloid beta (Aβ)	115:177	BACKGROUND INFORMATION Aberrant production of amyloid beta (Aβ) causes disruption of intracellular calcium homeostasis, a crucial factor in the pathogenesis of Alzheimer's disease.
32885474	9	59	from	function	1225:1232	arg1	stacking					1243:1250	Golgi stacking	1237:1250	Golgi stacking	1237:1250	Additionally, we observed that the Golgi reassembly stacking proteins having a function in Golgi stacking showed attenuation at COPII vesicles following Aβ treatment.
32885474	9	60	theme	Golgi	1237:1241	arg1	stacking					1243:1250	Golgi stacking	1237:1250	Golgi stacking	1237:1250	Additionally, we observed that the Golgi reassembly stacking proteins having a function in Golgi stacking showed attenuation at COPII vesicles following Aβ treatment.
32885474	11	61	theme	novel	1613:1617	arg1	avenue					1619:1624	a promising novel avenue	1601:1624	a promising novel avenue for development of AD therapeutics	1601:1659	SIGNIFICANCE The findings of this study suggested that protection of ERES or Sec31 O-GlcNAcylation may offer a promising novel avenue for development of AD therapeutics.
32885474	9	62	theme	Aβ	1299:1300	arg1	treatment					1302:1310	Aβ treatment	1299:1310	Aβ treatment	1299:1310	Additionally, we observed that the Golgi reassembly stacking proteins having a function in Golgi stacking showed attenuation at COPII vesicles following Aβ treatment.
32885474	4	63	theme	glycosylation	567:579	arg1	O-GlcNAcylation					521:535	O-GlcNAcylation	521:535	O-GlcNAcylation	521:535	O-GlcNAcylation, a unique and dynamic protein glycosylation process, modulates the formation of COPII vesicles.
32885474	4	63	theme	glycosylation	567:579	arg1	process					581:587	a unique and dynamic protein glycosylation process	538:587	a unique and dynamic protein glycosylation process	538:587	O-GlcNAcylation, a unique and dynamic protein glycosylation process, modulates the formation of COPII vesicles.
32885474	5	64	from	formation	711:719	arg1	ERES					742:745	ERES	742:745	ERES	742:745	RESULTS In this study, we observed that disrupted calcium levels affected the formation of COPII vesicles in ERES through calcium-triggered O-GlcNAcylation of Sec31A.
32885474	10	65	theme	Sec31A	1366:1371	arg1	targeting					1373:1381	Sec31A targeting	1366:1381	Sec31A targeting to ERES	1366:1389	CONCLUSIONS This study demonstrated that Aβ impaired Sec31A targeting to ERES through altered Sec31A O-GlcNAcylation triggered by disruption of intracellular calcium homeostasis.
32885474	9	66	contain	having	1216:1221	arg1	proteins					1207:1214	proteins	1207:1214	proteins having a function in Golgi stacking	1207:1250	Additionally, we observed that the Golgi reassembly stacking proteins having a function in Golgi stacking showed attenuation at COPII vesicles following Aβ treatment.
32885474	9	66	contain	having	1216:1221	arg2	function					1225:1232	a function	1223:1232	a function in Golgi stacking	1223:1250	Additionally, we observed that the Golgi reassembly stacking proteins having a function in Golgi stacking showed attenuation at COPII vesicles following Aβ treatment.
32885474	1	67	theme	crucial	237:243	arg1	factor					245:250	a crucial factor	235:250	a crucial factor in the pathogenesis of Alzheimer's disease	235:293	BACKGROUND INFORMATION Aberrant production of amyloid beta (Aβ) causes disruption of intracellular calcium homeostasis, a crucial factor in the pathogenesis of Alzheimer's disease.
32885474	1	67	theme	crucial	237:243	arg1	homeostasis					222:232	intracellular calcium homeostasis	200:232	intracellular calcium homeostasis	200:232	BACKGROUND INFORMATION Aberrant production of amyloid beta (Aβ) causes disruption of intracellular calcium homeostasis, a crucial factor in the pathogenesis of Alzheimer's disease.
32885474	6	68	from	O-GlcNAcylation	890:904	arg1	cells					928:932	neuronal cells	919:932	neuronal cells	919:932	Additionally, we found that Aβ impaired ERES through Aβ-disturbed calcium homeostasis and O-GlcNAcylation of Sec31A in neuronal cells.
32885474	1	69	theme	intracellular	200:212	arg1	factor					245:250	a crucial factor	235:250	a crucial factor in the pathogenesis of Alzheimer's disease	235:293	BACKGROUND INFORMATION Aberrant production of amyloid beta (Aβ) causes disruption of intracellular calcium homeostasis, a crucial factor in the pathogenesis of Alzheimer's disease.
32885474	1	69	theme	intracellular	200:212	arg1	homeostasis					222:232	intracellular calcium homeostasis	200:232	intracellular calcium homeostasis	200:232	BACKGROUND INFORMATION Aberrant production of amyloid beta (Aβ) causes disruption of intracellular calcium homeostasis, a crucial factor in the pathogenesis of Alzheimer's disease.
32885474	1	70	theme	amyloid	161:167	arg1	beta					169:172	amyloid beta	161:172	amyloid beta (Aβ)	161:177	BACKGROUND INFORMATION Aberrant production of amyloid beta (Aβ) causes disruption of intracellular calcium homeostasis, a crucial factor in the pathogenesis of Alzheimer's disease.
32885474	1	70	theme	amyloid	161:167	arg1	Aβ					175:176	Aβ	175:176	Aβ	175:176	BACKGROUND INFORMATION Aberrant production of amyloid beta (Aβ) causes disruption of intracellular calcium homeostasis, a crucial factor in the pathogenesis of Alzheimer's disease.
32885474	4	71	theme	COPII	617:621	arg1	vesicles					623:630	COPII vesicles	617:630	COPII vesicles	617:630	O-GlcNAcylation, a unique and dynamic protein glycosylation process, modulates the formation of COPII vesicles.
32885474	6	72	theme	Sec31A	909:914	arg1	O-GlcNAcylation					890:904	O-GlcNAcylation	890:904	O-GlcNAcylation	890:904	Additionally, we found that Aβ impaired ERES through Aβ-disturbed calcium homeostasis and O-GlcNAcylation of Sec31A in neuronal cells.
32885474	6	72	theme	Sec31A	909:914	arg1	homeostasis					874:884	Aβ-disturbed calcium homeostasis	853:884	Aβ-disturbed calcium homeostasis	853:884	Additionally, we found that Aβ impaired ERES through Aβ-disturbed calcium homeostasis and O-GlcNAcylation of Sec31A in neuronal cells.
32885474	5	73	dep	RESULTS	633:639	arg1	observed					659:666	observed	659:666	observed that disrupted calcium levels affected the formation of COPII vesicles in ERES through calcium-triggered O-GlcNAcylation of Sec31A	659:797	RESULTS In this study, we observed that disrupted calcium levels affected the formation of COPII vesicles in ERES through calcium-triggered O-GlcNAcylation of Sec31A.
32885474	1	74	theme	beta	169:172	arg1	production					147:156	BACKGROUND INFORMATION Aberrant production	115:156	BACKGROUND INFORMATION Aberrant production of amyloid beta (Aβ)	115:177	BACKGROUND INFORMATION Aberrant production of amyloid beta (Aβ) causes disruption of intracellular calcium homeostasis, a crucial factor in the pathogenesis of Alzheimer's disease.
32885474	8	75	theme	O-GlcNAcylaion	1074:1087	arg1	levels					1089:1094	O-GlcNAcylaion levels	1074:1094	O-GlcNAcylaion levels	1074:1094	Golgi fragmentation by Aβ was rescued by up-regulation of O-GlcNAcylaion levels using Thiamet G (ThiG), an O-GlcNAcase inhibitor.
32885474	8	76	theme	O-GlcNAcase	1123:1133	arg1	inhibitor					1135:1143	an O-GlcNAcase inhibitor	1120:1143	an O-GlcNAcase inhibitor	1120:1143	Golgi fragmentation by Aβ was rescued by up-regulation of O-GlcNAcylaion levels using Thiamet G (ThiG), an O-GlcNAcase inhibitor.
32885474	8	76	theme	O-GlcNAcase	1123:1133	arg1	G					1110:1110	Thiamet G	1102:1110	Thiamet G (ThiG)	1102:1117	Golgi fragmentation by Aβ was rescued by up-regulation of O-GlcNAcylaion levels using Thiamet G (ThiG), an O-GlcNAcase inhibitor.
30905621	10	0	from	p-STAT5	1077:1083	arg1	immunoprecipitate					1094:1110	STRA6 immunoprecipitate	1088:1110	STRA6 immunoprecipitate	1088:1110	RBP4, p-Try, p-JAK2, and p-STAT5 on STRA6 immunoprecipitate were reduced.
30905621	14	1	theme	CONCLUSIONS	1639:1649	arg1	O-GlcNAcylation					1651:1665	CONCLUSIONS O-GlcNAcylation	1639:1665	CONCLUSIONS O-GlcNAcylation	1639:1665	CONCLUSIONS O-GlcNAcylation significantly modified STRA6 and RALDH1, suppressed RBP4 binding activity, and disrupted retinol signals in the kidney of diabetes.
30905621	11	2	theme	HG-cultured	1270:1280	arg1	cells					1282:1286	HG-cultured cells	1270:1286	HG-cultured cells	1270:1286	Cellular retinol signals (CRBP1, LRAT, ADH, retinol, retinal, RA, RARα, RARγ and RXRα) remarkably decreased in kidneys of db/db, ob/ob mice and HG-cultured cells.
30905621	14	3	theme	RBP4	1719:1722	arg1	activity					1732:1739	RBP4 binding activity	1719:1739	RBP4 binding activity	1719:1739	CONCLUSIONS O-GlcNAcylation significantly modified STRA6 and RALDH1, suppressed RBP4 binding activity, and disrupted retinol signals in the kidney of diabetes.
30905621	6	4	theme	ELISA	636:640	arg1	concentrations					682:695	HPLC and ELISA for retinol, retinal, and retinoic acid concentrations	627:695	HPLC and ELISA for retinol, retinal, and retinoic acid concentrations	627:695	HPLC and ELISA for retinol, retinal, and retinoic acid concentrations were performed in vivo and vitro.
30905621	3	5	theme	STRA6-retinol	304:316	arg1	signals					318:324	STRA6-retinol signals	304:324	STRA6-retinol signals	304:324	Therefore, we investigated whether O-GlcNAcylation disrupted STRA6-retinol signals in diabetes.
30905621	13	6	theme	STRA6	1505:1509	arg1	O-GlcNAc-modification					1480:1500	O-GlcNAc-modification	1480:1500	O-GlcNAc-modification of STRA6 and RALDH1	1480:1520	OSMI-1, OGA transfection, and OGT silence reversed O-GlcNAc-modification of STRA6 and RALDH1, and rescued the decrease of retinol signals, and reversed the increase of TGFβ1 and collagen 1 in HG-treated cells.
30905621	7	7	with	binding	736:742	arg1	STRA6					749:753	STRA6	749:753	STRA6	749:753	RBP4 binding with STRA6 was measured in vitro.
30905621	13	8	theme	RALDH1	1515:1520	arg1	O-GlcNAc-modification					1480:1500	O-GlcNAc-modification	1480:1500	O-GlcNAc-modification of STRA6 and RALDH1	1480:1520	OSMI-1, OGA transfection, and OGT silence reversed O-GlcNAc-modification of STRA6 and RALDH1, and rescued the decrease of retinol signals, and reversed the increase of TGFβ1 and collagen 1 in HG-treated cells.
30905621	7	9	theme	RBP4	731:734	arg1	binding					736:742	RBP4 binding	731:742	RBP4 binding with STRA6	731:753	RBP4 binding with STRA6 was measured in vitro.
30905621	4	10	theme	mice	492:495	arg1	kidneys					465:471	kidneys	465:471	kidneys of db/db and ob/ob mice	465:495	METHODS Immunoprecipitation and proximity ligation assay were used to investigate O-GlcNAcylation of STRA6-retinol signals in kidneys of db/db and ob/ob mice.
30905621	12	11	theme	retinol	1391:1397	arg1	signals					1399:1405	retinol signals	1391:1405	retinol signals	1391:1405	TMG and OGT transfection induced O-GlcNAcylation of STRA6 and RALDH1, repressed RBP4-bound STRA6, and retinol signals in NG-cultured cells.
30905621	13	12	from	increase	1585:1592	arg1	cells					1632:1636	HG-treated cells	1621:1636	HG-treated cells	1621:1636	OSMI-1, OGA transfection, and OGT silence reversed O-GlcNAc-modification of STRA6 and RALDH1, and rescued the decrease of retinol signals, and reversed the increase of TGFβ1 and collagen 1 in HG-treated cells.
30905621	14	13	theme	binding	1724:1730	arg1	activity					1732:1739	RBP4 binding activity	1719:1739	RBP4 binding activity	1719:1739	CONCLUSIONS O-GlcNAcylation significantly modified STRA6 and RALDH1, suppressed RBP4 binding activity, and disrupted retinol signals in the kidney of diabetes.
30905621	6	14	theme	HPLC	627:630	arg1	concentrations					682:695	HPLC and ELISA for retinol, retinal, and retinoic acid concentrations	627:695	HPLC and ELISA for retinol, retinal, and retinoic acid concentrations	627:695	HPLC and ELISA for retinol, retinal, and retinoic acid concentrations were performed in vivo and vitro.
30905621	10	15	from	p-JAK2	1065:1070	arg1	immunoprecipitate					1094:1110	STRA6 immunoprecipitate	1088:1110	STRA6 immunoprecipitate	1088:1110	RBP4, p-Try, p-JAK2, and p-STAT5 on STRA6 immunoprecipitate were reduced.
30905621	1	16	theme	BACKGROUND	71:80	arg1	O-GlcNAcylation					82:96	BACKGROUND O-GlcNAcylation	71:96	BACKGROUND O-GlcNAcylation	71:96	BACKGROUND O-GlcNAcylation is an important mechanism of diabetic complication.
30905621	1	16	theme	BACKGROUND	71:80	arg1	mechanism					114:122	an important mechanism	101:122	an important mechanism of diabetic complication	101:147	BACKGROUND O-GlcNAcylation is an important mechanism of diabetic complication.
30905621	15	17	theme	GENERAL	1799:1805	arg1	SIGNIFICANCE					1807:1818	GENERAL SIGNIFICANCE	1799:1818	GENERAL SIGNIFICANCE	1799:1818	GENERAL SIGNIFICANCE This study first indicates that STRA6-retinol signals were directly disrupted by O-GlcNAcylation in diabetic kidney.
30905621	8	18	theme	OGA	890:892	arg1	treatment					845:853	treatment	845:853	treatment of TMG and OSMI-1	845:871	To verify whether O-GlcNAcylation disrupted STRA6-retinol signals, treatment of TMG and OSMI-1, transfection of OGA and OGT, and OGT siRNA were performed in HK-2 cells.
30905621	8	18	theme	OGA	890:892	arg1	siRNA					911:915	OGT siRNA	907:915	OGT siRNA	907:915	To verify whether O-GlcNAcylation disrupted STRA6-retinol signals, treatment of TMG and OSMI-1, transfection of OGA and OGT, and OGT siRNA were performed in HK-2 cells.
30905621	8	18	theme	OGA	890:892	arg1	transfection					874:885	transfection	874:885	transfection of OGA and OGT	874:900	To verify whether O-GlcNAcylation disrupted STRA6-retinol signals, treatment of TMG and OSMI-1, transfection of OGA and OGT, and OGT siRNA were performed in HK-2 cells.
30905621	2	19	theme	cell-physiological	181:198	arg1	functions					200:208	cell-physiological functions	181:208	cell-physiological functions	181:208	Retinoid homeostasis regulates cell-physiological functions through STRA6-retinol signaling.
30905621	12	20	theme	STRA6	1341:1345	arg1	O-GlcNAcylation					1322:1336	O-GlcNAcylation	1322:1336	O-GlcNAcylation of STRA6 and RALDH1	1322:1356	TMG and OGT transfection induced O-GlcNAcylation of STRA6 and RALDH1, repressed RBP4-bound STRA6, and retinol signals in NG-cultured cells.
30905621	12	20	theme	STRA6	1341:1345	arg1	STRA6					1380:1384	repressed RBP4-bound STRA6	1359:1384	repressed RBP4-bound STRA6	1359:1384	TMG and OGT transfection induced O-GlcNAcylation of STRA6 and RALDH1, repressed RBP4-bound STRA6, and retinol signals in NG-cultured cells.
30905621	12	20	theme	STRA6	1341:1345	arg1	signals					1399:1405	retinol signals	1391:1405	retinol signals	1391:1405	TMG and OGT transfection induced O-GlcNAcylation of STRA6 and RALDH1, repressed RBP4-bound STRA6, and retinol signals in NG-cultured cells.
30905621	4	21	theme	ligation	381:388	arg1	assay					390:394	proximity ligation assay	371:394	proximity ligation assay	371:394	METHODS Immunoprecipitation and proximity ligation assay were used to investigate O-GlcNAcylation of STRA6-retinol signals in kidneys of db/db and ob/ob mice.
30905621	4	21	theme	ligation	381:388	arg1	METHODS					339:345	METHODS Immunoprecipitation and proximity ligation assay	339:394	METHODS Immunoprecipitation and proximity ligation assay	339:394	METHODS Immunoprecipitation and proximity ligation assay were used to investigate O-GlcNAcylation of STRA6-retinol signals in kidneys of db/db and ob/ob mice.
30905621	11	22	theme	Cellular	1126:1133	arg1	RARα					1192:1195	RARα	1192:1195	RARα	1192:1195	Cellular retinol signals (CRBP1, LRAT, ADH, retinol, retinal, RA, RARα, RARγ and RXRα) remarkably decreased in kidneys of db/db, ob/ob mice and HG-cultured cells.
30905621	11	22	theme	Cellular	1126:1133	arg1	CRBP1					1152:1156	CRBP1	1152:1156	CRBP1	1152:1156	Cellular retinol signals (CRBP1, LRAT, ADH, retinol, retinal, RA, RARα, RARγ and RXRα) remarkably decreased in kidneys of db/db, ob/ob mice and HG-cultured cells.
30905621	11	22	theme	Cellular	1126:1133	arg1	retinol					1170:1176	retinol	1170:1176	retinol	1170:1176	Cellular retinol signals (CRBP1, LRAT, ADH, retinol, retinal, RA, RARα, RARγ and RXRα) remarkably decreased in kidneys of db/db, ob/ob mice and HG-cultured cells.
30905621	11	22	theme	Cellular	1126:1133	arg1	retinal					1179:1185	retinal	1179:1185	retinal	1179:1185	Cellular retinol signals (CRBP1, LRAT, ADH, retinol, retinal, RA, RARα, RARγ and RXRα) remarkably decreased in kidneys of db/db, ob/ob mice and HG-cultured cells.
30905621	11	22	theme	Cellular	1126:1133	arg1	RARγ					1198:1201	RARγ	1198:1201	RARγ	1198:1201	Cellular retinol signals (CRBP1, LRAT, ADH, retinol, retinal, RA, RARα, RARγ and RXRα) remarkably decreased in kidneys of db/db, ob/ob mice and HG-cultured cells.
30905621	11	22	theme	Cellular	1126:1133	arg1	LRAT					1159:1162	LRAT	1159:1162	LRAT	1159:1162	Cellular retinol signals (CRBP1, LRAT, ADH, retinol, retinal, RA, RARα, RARγ and RXRα) remarkably decreased in kidneys of db/db, ob/ob mice and HG-cultured cells.
30905621	11	22	theme	Cellular	1126:1133	arg1	RXRα					1207:1210	RXRα	1207:1210	RXRα	1207:1210	Cellular retinol signals (CRBP1, LRAT, ADH, retinol, retinal, RA, RARα, RARγ and RXRα) remarkably decreased in kidneys of db/db, ob/ob mice and HG-cultured cells.
30905621	11	22	theme	Cellular	1126:1133	arg1	ADH					1165:1167	ADH	1165:1167	ADH	1165:1167	Cellular retinol signals (CRBP1, LRAT, ADH, retinol, retinal, RA, RARα, RARγ and RXRα) remarkably decreased in kidneys of db/db, ob/ob mice and HG-cultured cells.
30905621	11	22	theme	Cellular	1126:1133	arg1	RA					1188:1189	RA	1188:1189	RA	1188:1189	Cellular retinol signals (CRBP1, LRAT, ADH, retinol, retinal, RA, RARα, RARγ and RXRα) remarkably decreased in kidneys of db/db, ob/ob mice and HG-cultured cells.
30905621	11	22	theme	Cellular	1126:1133	arg1	signals					1143:1149	Cellular retinol signals	1126:1149	Cellular retinol signals (CRBP1, LRAT, ADH, retinol, retinal, RA, RARα, RARγ and RXRα)	1126:1211	Cellular retinol signals (CRBP1, LRAT, ADH, retinol, retinal, RA, RARα, RARγ and RXRα) remarkably decreased in kidneys of db/db, ob/ob mice and HG-cultured cells.
30905621	9	23	theme	db/db	1030:1034	arg1	mice					1046:1049	db/db and ob/ob mice	1030:1049	db/db and ob/ob mice	1030:1049	RESULTS STRA6 and RALDH1 were highly O-GlcNAc-modified in glomeruli and tubules of db/db and ob/ob mice.
30905621	4	24	theme	db/db	476:480	arg1	mice					492:495	db/db and ob/ob mice	476:495	db/db and ob/ob mice	476:495	METHODS Immunoprecipitation and proximity ligation assay were used to investigate O-GlcNAcylation of STRA6-retinol signals in kidneys of db/db and ob/ob mice.
30905621	13	25	theme	TGFβ1	1597:1601	arg1	increase					1585:1592	the increase	1581:1592	the increase of TGFβ1 and collagen 1 in HG-treated cells	1581:1636	OSMI-1, OGA transfection, and OGT silence reversed O-GlcNAc-modification of STRA6 and RALDH1, and rescued the decrease of retinol signals, and reversed the increase of TGFβ1 and collagen 1 in HG-treated cells.
30905621	5	26	theme	collagen	609:616	arg1	level					620:624	collagen 1 level	609:624	collagen 1 level	609:624	Western blot and immunohistochemistry were done for STRA6/CRBP1/LRAT/RALDH1/RARs pathway, GFAT, OGT, TGFβ1 and collagen 1 level.
30905621	5	26	theme	collagen	609:616	arg1	pathway					579:585	STRA6/CRBP1/LRAT/RALDH1/RARs pathway	550:585	STRA6/CRBP1/LRAT/RALDH1/RARs pathway	550:585	Western blot and immunohistochemistry were done for STRA6/CRBP1/LRAT/RALDH1/RARs pathway, GFAT, OGT, TGFβ1 and collagen 1 level.
30905621	11	27	theme	retinol	1135:1141	arg1	RARα					1192:1195	RARα	1192:1195	RARα	1192:1195	Cellular retinol signals (CRBP1, LRAT, ADH, retinol, retinal, RA, RARα, RARγ and RXRα) remarkably decreased in kidneys of db/db, ob/ob mice and HG-cultured cells.
30905621	11	27	theme	retinol	1135:1141	arg1	CRBP1					1152:1156	CRBP1	1152:1156	CRBP1	1152:1156	Cellular retinol signals (CRBP1, LRAT, ADH, retinol, retinal, RA, RARα, RARγ and RXRα) remarkably decreased in kidneys of db/db, ob/ob mice and HG-cultured cells.
30905621	11	27	theme	retinol	1135:1141	arg1	retinol					1170:1176	retinol	1170:1176	retinol	1170:1176	Cellular retinol signals (CRBP1, LRAT, ADH, retinol, retinal, RA, RARα, RARγ and RXRα) remarkably decreased in kidneys of db/db, ob/ob mice and HG-cultured cells.
30905621	11	27	theme	retinol	1135:1141	arg1	retinal					1179:1185	retinal	1179:1185	retinal	1179:1185	Cellular retinol signals (CRBP1, LRAT, ADH, retinol, retinal, RA, RARα, RARγ and RXRα) remarkably decreased in kidneys of db/db, ob/ob mice and HG-cultured cells.
30905621	11	27	theme	retinol	1135:1141	arg1	RARγ					1198:1201	RARγ	1198:1201	RARγ	1198:1201	Cellular retinol signals (CRBP1, LRAT, ADH, retinol, retinal, RA, RARα, RARγ and RXRα) remarkably decreased in kidneys of db/db, ob/ob mice and HG-cultured cells.
30905621	11	27	theme	retinol	1135:1141	arg1	LRAT					1159:1162	LRAT	1159:1162	LRAT	1159:1162	Cellular retinol signals (CRBP1, LRAT, ADH, retinol, retinal, RA, RARα, RARγ and RXRα) remarkably decreased in kidneys of db/db, ob/ob mice and HG-cultured cells.
30905621	11	27	theme	retinol	1135:1141	arg1	RXRα					1207:1210	RXRα	1207:1210	RXRα	1207:1210	Cellular retinol signals (CRBP1, LRAT, ADH, retinol, retinal, RA, RARα, RARγ and RXRα) remarkably decreased in kidneys of db/db, ob/ob mice and HG-cultured cells.
30905621	11	27	theme	retinol	1135:1141	arg1	ADH					1165:1167	ADH	1165:1167	ADH	1165:1167	Cellular retinol signals (CRBP1, LRAT, ADH, retinol, retinal, RA, RARα, RARγ and RXRα) remarkably decreased in kidneys of db/db, ob/ob mice and HG-cultured cells.
30905621	11	27	theme	retinol	1135:1141	arg1	RA					1188:1189	RA	1188:1189	RA	1188:1189	Cellular retinol signals (CRBP1, LRAT, ADH, retinol, retinal, RA, RARα, RARγ and RXRα) remarkably decreased in kidneys of db/db, ob/ob mice and HG-cultured cells.
30905621	11	27	theme	retinol	1135:1141	arg1	signals					1143:1149	Cellular retinol signals	1126:1149	Cellular retinol signals (CRBP1, LRAT, ADH, retinol, retinal, RA, RARα, RARγ and RXRα)	1126:1211	Cellular retinol signals (CRBP1, LRAT, ADH, retinol, retinal, RA, RARα, RARγ and RXRα) remarkably decreased in kidneys of db/db, ob/ob mice and HG-cultured cells.
30905621	13	28	theme	collagen	1607:1614	arg1	increase					1585:1592	the increase	1581:1592	the increase of TGFβ1 and collagen 1 in HG-treated cells	1581:1636	OSMI-1, OGA transfection, and OGT silence reversed O-GlcNAc-modification of STRA6 and RALDH1, and rescued the decrease of retinol signals, and reversed the increase of TGFβ1 and collagen 1 in HG-treated cells.
30905621	14	29	theme	diabetes	1789:1796	arg1	kidney					1779:1784	the kidney	1775:1784	the kidney of diabetes	1775:1796	CONCLUSIONS O-GlcNAcylation significantly modified STRA6 and RALDH1, suppressed RBP4 binding activity, and disrupted retinol signals in the kidney of diabetes.
30905621	12	30	theme	RBP4-bound	1369:1378	arg1	STRA6					1380:1384	repressed RBP4-bound STRA6	1359:1384	repressed RBP4-bound STRA6	1359:1384	TMG and OGT transfection induced O-GlcNAcylation of STRA6 and RALDH1, repressed RBP4-bound STRA6, and retinol signals in NG-cultured cells.
30905621	12	31	theme	NG-cultured	1410:1420	arg1	cells					1422:1426	NG-cultured cells	1410:1426	NG-cultured cells	1410:1426	TMG and OGT transfection induced O-GlcNAcylation of STRA6 and RALDH1, repressed RBP4-bound STRA6, and retinol signals in NG-cultured cells.
30905621	12	32	theme	OGT	1297:1299	arg1	transfection					1301:1312	OGT transfection	1297:1312	OGT transfection	1297:1312	TMG and OGT transfection induced O-GlcNAcylation of STRA6 and RALDH1, repressed RBP4-bound STRA6, and retinol signals in NG-cultured cells.
30905621	9	33	theme	ob/ob	1040:1044	arg1	mice					1046:1049	db/db and ob/ob mice	1030:1049	db/db and ob/ob mice	1030:1049	RESULTS STRA6 and RALDH1 were highly O-GlcNAc-modified in glomeruli and tubules of db/db and ob/ob mice.
30905621	14	34	theme	retinol	1756:1762	arg1	signals					1764:1770	retinol signals	1756:1770	retinol signals in the kidney of diabetes	1756:1796	CONCLUSIONS O-GlcNAcylation significantly modified STRA6 and RALDH1, suppressed RBP4 binding activity, and disrupted retinol signals in the kidney of diabetes.
30905621	4	35	theme	ob/ob	486:490	arg1	mice					492:495	db/db and ob/ob mice	476:495	db/db and ob/ob mice	476:495	METHODS Immunoprecipitation and proximity ligation assay were used to investigate O-GlcNAcylation of STRA6-retinol signals in kidneys of db/db and ob/ob mice.
30905621	1	36	theme	important	104:112	arg1	O-GlcNAcylation					82:96	BACKGROUND O-GlcNAcylation	71:96	BACKGROUND O-GlcNAcylation	71:96	BACKGROUND O-GlcNAcylation is an important mechanism of diabetic complication.
30905621	1	36	theme	important	104:112	arg1	mechanism					114:122	an important mechanism	101:122	an important mechanism of diabetic complication	101:147	BACKGROUND O-GlcNAcylation is an important mechanism of diabetic complication.
30905621	15	37	theme	STRA6-retinol	1852:1864	arg1	signals					1866:1872	STRA6-retinol signals	1852:1872	STRA6-retinol signals	1852:1872	GENERAL SIGNIFICANCE This study first indicates that STRA6-retinol signals were directly disrupted by O-GlcNAcylation in diabetic kidney.
30905621	9	38	theme	mice	1046:1049	arg1	tubules					1019:1025	tubules	1019:1025	tubules	1019:1025	RESULTS STRA6 and RALDH1 were highly O-GlcNAc-modified in glomeruli and tubules of db/db and ob/ob mice.
30905621	9	38	theme	mice	1046:1049	arg1	glomeruli					1005:1013	glomeruli	1005:1013	glomeruli	1005:1013	RESULTS STRA6 and RALDH1 were highly O-GlcNAc-modified in glomeruli and tubules of db/db and ob/ob mice.
30905621	13	39	theme	HG-treated	1621:1630	arg1	cells					1632:1636	HG-treated cells	1621:1636	HG-treated cells	1621:1636	OSMI-1, OGA transfection, and OGT silence reversed O-GlcNAc-modification of STRA6 and RALDH1, and rescued the decrease of retinol signals, and reversed the increase of TGFβ1 and collagen 1 in HG-treated cells.
30905621	13	40	theme	retinol	1551:1557	arg1	signals					1559:1565	retinol signals	1551:1565	retinol signals	1551:1565	OSMI-1, OGA transfection, and OGT silence reversed O-GlcNAc-modification of STRA6 and RALDH1, and rescued the decrease of retinol signals, and reversed the increase of TGFβ1 and collagen 1 in HG-treated cells.
30905621	10	41	from	RBP4	1052:1055	arg1	immunoprecipitate					1094:1110	STRA6 immunoprecipitate	1088:1110	STRA6 immunoprecipitate	1088:1110	RBP4, p-Try, p-JAK2, and p-STAT5 on STRA6 immunoprecipitate were reduced.
30905621	0	42	theme	STRA6-retinol	25:37	arg1	signals					39:45	STRA6-retinol signals	25:45	STRA6-retinol signals	25:45	O-GlcNAcylation disrupts STRA6-retinol signals in kidneys of diabetes.
30905621	8	43	theme	STRA6-retinol	822:834	arg1	signals					836:842	STRA6-retinol signals	822:842	STRA6-retinol signals	822:842	To verify whether O-GlcNAcylation disrupted STRA6-retinol signals, treatment of TMG and OSMI-1, transfection of OGA and OGT, and OGT siRNA were performed in HK-2 cells.
30905621	13	44	theme	OGA	1437:1439	arg1	transfection					1441:1452	OGA transfection	1437:1452	OGA transfection	1437:1452	OSMI-1, OGA transfection, and OGT silence reversed O-GlcNAc-modification of STRA6 and RALDH1, and rescued the decrease of retinol signals, and reversed the increase of TGFβ1 and collagen 1 in HG-treated cells.
30905621	4	45	theme	proximity	371:379	arg1	assay					390:394	proximity ligation assay	371:394	proximity ligation assay	371:394	METHODS Immunoprecipitation and proximity ligation assay were used to investigate O-GlcNAcylation of STRA6-retinol signals in kidneys of db/db and ob/ob mice.
30905621	4	45	theme	proximity	371:379	arg1	METHODS					339:345	METHODS Immunoprecipitation and proximity ligation assay	339:394	METHODS Immunoprecipitation and proximity ligation assay	339:394	METHODS Immunoprecipitation and proximity ligation assay were used to investigate O-GlcNAcylation of STRA6-retinol signals in kidneys of db/db and ob/ob mice.
30905621	13	46	theme	OGT	1459:1461	arg1	silence					1463:1469	OGT silence	1459:1469	OGT silence	1459:1469	OSMI-1, OGA transfection, and OGT silence reversed O-GlcNAc-modification of STRA6 and RALDH1, and rescued the decrease of retinol signals, and reversed the increase of TGFβ1 and collagen 1 in HG-treated cells.
30905621	6	47	theme	retinoic	668:675	arg1	acid					677:680	retinoic acid	668:680	retinoic acid	668:680	HPLC and ELISA for retinol, retinal, and retinoic acid concentrations were performed in vivo and vitro.
30905621	8	48	theme	HK-2	935:938	arg1	cells					940:944	HK-2 cells	935:944	HK-2 cells	935:944	To verify whether O-GlcNAcylation disrupted STRA6-retinol signals, treatment of TMG and OSMI-1, transfection of OGA and OGT, and OGT siRNA were performed in HK-2 cells.
30905621	10	49	from	p-Try	1058:1062	arg1	immunoprecipitate					1094:1110	STRA6 immunoprecipitate	1088:1110	STRA6 immunoprecipitate	1088:1110	RBP4, p-Try, p-JAK2, and p-STAT5 on STRA6 immunoprecipitate were reduced.
30905621	2	50	theme	STRA6-retinol	218:230	arg1	signaling					232:240	STRA6-retinol signaling	218:240	STRA6-retinol signaling	218:240	Retinoid homeostasis regulates cell-physiological functions through STRA6-retinol signaling.
30905621	4	51	used	used	401:404	arg2	METHODS					339:345	METHODS Immunoprecipitation and proximity ligation assay	339:394	METHODS Immunoprecipitation and proximity ligation assay	339:394	METHODS Immunoprecipitation and proximity ligation assay were used to investigate O-GlcNAcylation of STRA6-retinol signals in kidneys of db/db and ob/ob mice.
30905621	4	51	used	used	401:404	arg2	assay					390:394	proximity ligation assay	371:394	proximity ligation assay	371:394	METHODS Immunoprecipitation and proximity ligation assay were used to investigate O-GlcNAcylation of STRA6-retinol signals in kidneys of db/db and ob/ob mice.
30905621	4	51	used	used	401:404	arg2	Immunoprecipitation					347:365	Immunoprecipitation	347:365	Immunoprecipitation	347:365	METHODS Immunoprecipitation and proximity ligation assay were used to investigate O-GlcNAcylation of STRA6-retinol signals in kidneys of db/db and ob/ob mice.
30905621	4	52	theme	signals	454:460	arg1	O-GlcNAcylation					421:435	O-GlcNAcylation	421:435	O-GlcNAcylation of STRA6-retinol signals in kidneys of db/db and ob/ob mice	421:495	METHODS Immunoprecipitation and proximity ligation assay were used to investigate O-GlcNAcylation of STRA6-retinol signals in kidneys of db/db and ob/ob mice.
30905621	0	53	theme	diabetes	61:68	arg1	kidneys					50:56	kidneys	50:56	kidneys of diabetes	50:68	O-GlcNAcylation disrupts STRA6-retinol signals in kidneys of diabetes.
30905621	9	54	from	tubules	1019:1025	arg1	O-GlcNAc-modified					984:1000	O-GlcNAc-modified	984:1000	O-GlcNAc-modified	984:1000	RESULTS STRA6 and RALDH1 were highly O-GlcNAc-modified in glomeruli and tubules of db/db and ob/ob mice.
30905621	4	55	theme	STRA6-retinol	440:452	arg1	signals					454:460	STRA6-retinol signals	440:460	STRA6-retinol signals	440:460	METHODS Immunoprecipitation and proximity ligation assay were used to investigate O-GlcNAcylation of STRA6-retinol signals in kidneys of db/db and ob/ob mice.
30905621	1	56	theme	diabetic	127:134	arg1	complication					136:147	diabetic complication	127:147	diabetic complication	127:147	BACKGROUND O-GlcNAcylation is an important mechanism of diabetic complication.
30905621	15	57	from	O-GlcNAcylation	1901:1915	arg1	kidney					1929:1934	diabetic kidney	1920:1934	diabetic kidney	1920:1934	GENERAL SIGNIFICANCE This study first indicates that STRA6-retinol signals were directly disrupted by O-GlcNAcylation in diabetic kidney.
30905621	11	58	theme	ob/ob	1255:1259	arg1	mice					1261:1264	ob/ob mice	1255:1264	ob/ob mice	1255:1264	Cellular retinol signals (CRBP1, LRAT, ADH, retinol, retinal, RA, RARα, RARγ and RXRα) remarkably decreased in kidneys of db/db, ob/ob mice and HG-cultured cells.
30905621	12	59	theme	RALDH1	1351:1356	arg1	O-GlcNAcylation					1322:1336	O-GlcNAcylation	1322:1336	O-GlcNAcylation of STRA6 and RALDH1	1322:1356	TMG and OGT transfection induced O-GlcNAcylation of STRA6 and RALDH1, repressed RBP4-bound STRA6, and retinol signals in NG-cultured cells.
30905621	12	59	theme	RALDH1	1351:1356	arg1	STRA6					1380:1384	repressed RBP4-bound STRA6	1359:1384	repressed RBP4-bound STRA6	1359:1384	TMG and OGT transfection induced O-GlcNAcylation of STRA6 and RALDH1, repressed RBP4-bound STRA6, and retinol signals in NG-cultured cells.
30905621	12	59	theme	RALDH1	1351:1356	arg1	signals					1399:1405	retinol signals	1391:1405	retinol signals	1391:1405	TMG and OGT transfection induced O-GlcNAcylation of STRA6 and RALDH1, repressed RBP4-bound STRA6, and retinol signals in NG-cultured cells.
30905621	1	60	theme	complication	136:147	arg1	O-GlcNAcylation					82:96	BACKGROUND O-GlcNAcylation	71:96	BACKGROUND O-GlcNAcylation	71:96	BACKGROUND O-GlcNAcylation is an important mechanism of diabetic complication.
30905621	1	60	theme	complication	136:147	arg1	mechanism					114:122	an important mechanism	101:122	an important mechanism of diabetic complication	101:147	BACKGROUND O-GlcNAcylation is an important mechanism of diabetic complication.
30905621	13	61	theme	signals	1559:1565	arg1	decrease					1539:1546	the decrease	1535:1546	the decrease of retinol signals	1535:1565	OSMI-1, OGA transfection, and OGT silence reversed O-GlcNAc-modification of STRA6 and RALDH1, and rescued the decrease of retinol signals, and reversed the increase of TGFβ1 and collagen 1 in HG-treated cells.
30905621	9	62	from	glomeruli	1005:1013	arg1	O-GlcNAc-modified					984:1000	O-GlcNAc-modified	984:1000	O-GlcNAc-modified	984:1000	RESULTS STRA6 and RALDH1 were highly O-GlcNAc-modified in glomeruli and tubules of db/db and ob/ob mice.
30905621	11	63	dep	signals	1143:1149	arg1	RARα					1192:1195	RARα	1192:1195	RARα	1192:1195	Cellular retinol signals (CRBP1, LRAT, ADH, retinol, retinal, RA, RARα, RARγ and RXRα) remarkably decreased in kidneys of db/db, ob/ob mice and HG-cultured cells.
30905621	11	63	dep	signals	1143:1149	arg1	CRBP1					1152:1156	CRBP1	1152:1156	CRBP1	1152:1156	Cellular retinol signals (CRBP1, LRAT, ADH, retinol, retinal, RA, RARα, RARγ and RXRα) remarkably decreased in kidneys of db/db, ob/ob mice and HG-cultured cells.
30905621	11	63	dep	signals	1143:1149	arg1	retinol					1170:1176	retinol	1170:1176	retinol	1170:1176	Cellular retinol signals (CRBP1, LRAT, ADH, retinol, retinal, RA, RARα, RARγ and RXRα) remarkably decreased in kidneys of db/db, ob/ob mice and HG-cultured cells.
30905621	11	63	dep	signals	1143:1149	arg1	retinal					1179:1185	retinal	1179:1185	retinal	1179:1185	Cellular retinol signals (CRBP1, LRAT, ADH, retinol, retinal, RA, RARα, RARγ and RXRα) remarkably decreased in kidneys of db/db, ob/ob mice and HG-cultured cells.
30905621	11	63	dep	signals	1143:1149	arg1	RARγ					1198:1201	RARγ	1198:1201	RARγ	1198:1201	Cellular retinol signals (CRBP1, LRAT, ADH, retinol, retinal, RA, RARα, RARγ and RXRα) remarkably decreased in kidneys of db/db, ob/ob mice and HG-cultured cells.
30905621	11	63	dep	signals	1143:1149	arg1	LRAT					1159:1162	LRAT	1159:1162	LRAT	1159:1162	Cellular retinol signals (CRBP1, LRAT, ADH, retinol, retinal, RA, RARα, RARγ and RXRα) remarkably decreased in kidneys of db/db, ob/ob mice and HG-cultured cells.
30905621	11	63	dep	signals	1143:1149	arg1	RXRα					1207:1210	RXRα	1207:1210	RXRα	1207:1210	Cellular retinol signals (CRBP1, LRAT, ADH, retinol, retinal, RA, RARα, RARγ and RXRα) remarkably decreased in kidneys of db/db, ob/ob mice and HG-cultured cells.
30905621	11	63	dep	signals	1143:1149	arg1	ADH					1165:1167	ADH	1165:1167	ADH	1165:1167	Cellular retinol signals (CRBP1, LRAT, ADH, retinol, retinal, RA, RARα, RARγ and RXRα) remarkably decreased in kidneys of db/db, ob/ob mice and HG-cultured cells.
30905621	11	63	dep	signals	1143:1149	arg1	RA					1188:1189	RA	1188:1189	RA	1188:1189	Cellular retinol signals (CRBP1, LRAT, ADH, retinol, retinal, RA, RARα, RARγ and RXRα) remarkably decreased in kidneys of db/db, ob/ob mice and HG-cultured cells.
30905621	11	63	dep	signals	1143:1149	arg1	signals					1143:1149	Cellular retinol signals	1126:1149	Cellular retinol signals (CRBP1, LRAT, ADH, retinol, retinal, RA, RARα, RARγ and RXRα)	1126:1211	Cellular retinol signals (CRBP1, LRAT, ADH, retinol, retinal, RA, RARα, RARγ and RXRα) remarkably decreased in kidneys of db/db, ob/ob mice and HG-cultured cells.
30905621	4	64	dep	METHODS	339:345	arg1	assay					390:394	proximity ligation assay	371:394	proximity ligation assay	371:394	METHODS Immunoprecipitation and proximity ligation assay were used to investigate O-GlcNAcylation of STRA6-retinol signals in kidneys of db/db and ob/ob mice.
30905621	4	64	dep	METHODS	339:345	arg1	METHODS					339:345	METHODS Immunoprecipitation and proximity ligation assay	339:394	METHODS Immunoprecipitation and proximity ligation assay	339:394	METHODS Immunoprecipitation and proximity ligation assay were used to investigate O-GlcNAcylation of STRA6-retinol signals in kidneys of db/db and ob/ob mice.
30905621	4	64	dep	METHODS	339:345	arg1	Immunoprecipitation					347:365	Immunoprecipitation	347:365	Immunoprecipitation	347:365	METHODS Immunoprecipitation and proximity ligation assay were used to investigate O-GlcNAcylation of STRA6-retinol signals in kidneys of db/db and ob/ob mice.
30905621	5	65	theme	STRA6/CRBP1/LRAT/RALDH1/RARs	550:577	arg1	OGT					594:596	OGT	594:596	OGT	594:596	Western blot and immunohistochemistry were done for STRA6/CRBP1/LRAT/RALDH1/RARs pathway, GFAT, OGT, TGFβ1 and collagen 1 level.
30905621	5	65	theme	STRA6/CRBP1/LRAT/RALDH1/RARs	550:577	arg1	level					620:624	collagen 1 level	609:624	collagen 1 level	609:624	Western blot and immunohistochemistry were done for STRA6/CRBP1/LRAT/RALDH1/RARs pathway, GFAT, OGT, TGFβ1 and collagen 1 level.
30905621	5	65	theme	STRA6/CRBP1/LRAT/RALDH1/RARs	550:577	arg1	pathway					579:585	STRA6/CRBP1/LRAT/RALDH1/RARs pathway	550:585	STRA6/CRBP1/LRAT/RALDH1/RARs pathway	550:585	Western blot and immunohistochemistry were done for STRA6/CRBP1/LRAT/RALDH1/RARs pathway, GFAT, OGT, TGFβ1 and collagen 1 level.
30905621	5	65	theme	STRA6/CRBP1/LRAT/RALDH1/RARs	550:577	arg1	GFAT					588:591	GFAT	588:591	GFAT	588:591	Western blot and immunohistochemistry were done for STRA6/CRBP1/LRAT/RALDH1/RARs pathway, GFAT, OGT, TGFβ1 and collagen 1 level.
30905621	5	65	theme	STRA6/CRBP1/LRAT/RALDH1/RARs	550:577	arg1	TGFβ1					599:603	TGFβ1	599:603	TGFβ1	599:603	Western blot and immunohistochemistry were done for STRA6/CRBP1/LRAT/RALDH1/RARs pathway, GFAT, OGT, TGFβ1 and collagen 1 level.
30905621	11	66	theme	db/db	1248:1252	arg1	cells					1282:1286	HG-cultured cells	1270:1286	HG-cultured cells	1270:1286	Cellular retinol signals (CRBP1, LRAT, ADH, retinol, retinal, RA, RARα, RARγ and RXRα) remarkably decreased in kidneys of db/db, ob/ob mice and HG-cultured cells.
30905621	11	66	theme	db/db	1248:1252	arg1	mice					1261:1264	ob/ob mice	1255:1264	ob/ob mice	1255:1264	Cellular retinol signals (CRBP1, LRAT, ADH, retinol, retinal, RA, RARα, RARγ and RXRα) remarkably decreased in kidneys of db/db, ob/ob mice and HG-cultured cells.
30905621	11	66	theme	db/db	1248:1252	arg1	kidneys					1237:1243	kidneys	1237:1243	kidneys of db/db	1237:1252	Cellular retinol signals (CRBP1, LRAT, ADH, retinol, retinal, RA, RARα, RARγ and RXRα) remarkably decreased in kidneys of db/db, ob/ob mice and HG-cultured cells.
30905621	10	67	theme	STRA6	1088:1092	arg1	immunoprecipitate					1094:1110	STRA6 immunoprecipitate	1088:1110	STRA6 immunoprecipitate	1088:1110	RBP4, p-Try, p-JAK2, and p-STAT5 on STRA6 immunoprecipitate were reduced.
30905621	4	68	from	O-GlcNAcylation	421:435	arg1	kidneys					465:471	kidneys	465:471	kidneys of db/db and ob/ob mice	465:495	METHODS Immunoprecipitation and proximity ligation assay were used to investigate O-GlcNAcylation of STRA6-retinol signals in kidneys of db/db and ob/ob mice.
30905621	8	69	theme	OGT	907:909	arg1	siRNA					911:915	OGT siRNA	907:915	OGT siRNA	907:915	To verify whether O-GlcNAcylation disrupted STRA6-retinol signals, treatment of TMG and OSMI-1, transfection of OGA and OGT, and OGT siRNA were performed in HK-2 cells.
30905621	8	70	theme	TMG	858:860	arg1	treatment					845:853	treatment	845:853	treatment of TMG and OSMI-1	845:871	To verify whether O-GlcNAcylation disrupted STRA6-retinol signals, treatment of TMG and OSMI-1, transfection of OGA and OGT, and OGT siRNA were performed in HK-2 cells.
30905621	8	70	theme	TMG	858:860	arg1	siRNA					911:915	OGT siRNA	907:915	OGT siRNA	907:915	To verify whether O-GlcNAcylation disrupted STRA6-retinol signals, treatment of TMG and OSMI-1, transfection of OGA and OGT, and OGT siRNA were performed in HK-2 cells.
30905621	8	70	theme	TMG	858:860	arg1	transfection					874:885	transfection	874:885	transfection of OGA and OGT	874:900	To verify whether O-GlcNAcylation disrupted STRA6-retinol signals, treatment of TMG and OSMI-1, transfection of OGA and OGT, and OGT siRNA were performed in HK-2 cells.
30905621	14	71	from	signals	1764:1770	arg1	kidney					1779:1784	the kidney	1775:1784	the kidney of diabetes	1775:1796	CONCLUSIONS O-GlcNAcylation significantly modified STRA6 and RALDH1, suppressed RBP4 binding activity, and disrupted retinol signals in the kidney of diabetes.
30905621	9	72	from	O-GlcNAc-modified	984:1000	arg1	tubules					1019:1025	tubules	1019:1025	tubules	1019:1025	RESULTS STRA6 and RALDH1 were highly O-GlcNAc-modified in glomeruli and tubules of db/db and ob/ob mice.
30905621	9	72	from	O-GlcNAc-modified	984:1000	arg1	glomeruli					1005:1013	glomeruli	1005:1013	glomeruli	1005:1013	RESULTS STRA6 and RALDH1 were highly O-GlcNAc-modified in glomeruli and tubules of db/db and ob/ob mice.
30905621	12	73	theme	repressed	1359:1367	arg1	STRA6					1380:1384	repressed RBP4-bound STRA6	1359:1384	repressed RBP4-bound STRA6	1359:1384	TMG and OGT transfection induced O-GlcNAcylation of STRA6 and RALDH1, repressed RBP4-bound STRA6, and retinol signals in NG-cultured cells.
30905621	8	74	theme	OGT	898:900	arg1	treatment					845:853	treatment	845:853	treatment of TMG and OSMI-1	845:871	To verify whether O-GlcNAcylation disrupted STRA6-retinol signals, treatment of TMG and OSMI-1, transfection of OGA and OGT, and OGT siRNA were performed in HK-2 cells.
30905621	8	74	theme	OGT	898:900	arg1	siRNA					911:915	OGT siRNA	907:915	OGT siRNA	907:915	To verify whether O-GlcNAcylation disrupted STRA6-retinol signals, treatment of TMG and OSMI-1, transfection of OGA and OGT, and OGT siRNA were performed in HK-2 cells.
30905621	8	74	theme	OGT	898:900	arg1	transfection					874:885	transfection	874:885	transfection of OGA and OGT	874:900	To verify whether O-GlcNAcylation disrupted STRA6-retinol signals, treatment of TMG and OSMI-1, transfection of OGA and OGT, and OGT siRNA were performed in HK-2 cells.
30905621	5	75	theme	Western	498:504	arg1	blot					506:509	Western blot	498:509	Western blot	498:509	Western blot and immunohistochemistry were done for STRA6/CRBP1/LRAT/RALDH1/RARs pathway, GFAT, OGT, TGFβ1 and collagen 1 level.
30905621	9	76	dep	RESULTS	947:953	arg1	RESULTS					947:953	RESULTS STRA6 and RALDH1	947:970	RESULTS STRA6 and RALDH1	947:970	RESULTS STRA6 and RALDH1 were highly O-GlcNAc-modified in glomeruli and tubules of db/db and ob/ob mice.
30905621	9	76	dep	RESULTS	947:953	arg1	RALDH1					965:970	RALDH1	965:970	RALDH1	965:970	RESULTS STRA6 and RALDH1 were highly O-GlcNAc-modified in glomeruli and tubules of db/db and ob/ob mice.
30905621	9	76	dep	RESULTS	947:953	arg1	STRA6					955:959	STRA6	955:959	STRA6	955:959	RESULTS STRA6 and RALDH1 were highly O-GlcNAc-modified in glomeruli and tubules of db/db and ob/ob mice.
30905621	2	77	theme	Retinoid	150:157	arg1	homeostasis					159:169	Retinoid homeostasis	150:169	Retinoid homeostasis	150:169	Retinoid homeostasis regulates cell-physiological functions through STRA6-retinol signaling.
30905621	15	78	theme	diabetic	1920:1927	arg1	kidney					1929:1934	diabetic kidney	1920:1934	diabetic kidney	1920:1934	GENERAL SIGNIFICANCE This study first indicates that STRA6-retinol signals were directly disrupted by O-GlcNAcylation in diabetic kidney.
30905621	8	79	theme	OSMI-1	866:871	arg1	treatment					845:853	treatment	845:853	treatment of TMG and OSMI-1	845:871	To verify whether O-GlcNAcylation disrupted STRA6-retinol signals, treatment of TMG and OSMI-1, transfection of OGA and OGT, and OGT siRNA were performed in HK-2 cells.
30905621	8	79	theme	OSMI-1	866:871	arg1	siRNA					911:915	OGT siRNA	907:915	OGT siRNA	907:915	To verify whether O-GlcNAcylation disrupted STRA6-retinol signals, treatment of TMG and OSMI-1, transfection of OGA and OGT, and OGT siRNA were performed in HK-2 cells.
30905621	8	79	theme	OSMI-1	866:871	arg1	transfection					874:885	transfection	874:885	transfection of OGA and OGT	874:900	To verify whether O-GlcNAcylation disrupted STRA6-retinol signals, treatment of TMG and OSMI-1, transfection of OGA and OGT, and OGT siRNA were performed in HK-2 cells.
28878262	0	0	theme	human	86:90	arg1	carcinoma					97:105	human lung carcinoma	86:105	human lung carcinoma	86:105	Hyper-O-GlcNAcylation induces cisplatin resistance via regulation of p53 and c-Myc in human lung carcinoma.
28878262	6	1	theme	proteasomal	1053:1063	arg1	degradation					1065:1075	subsequent proteasomal degradation	1042:1075	subsequent proteasomal degradation	1042:1075	By contrast, O-GlcNAcylation of c-Myc inhibits its ubiquitination and subsequent proteasomal degradation.
28878262	7	2	theme	CDDP-induced	1173:1184	arg1	apoptosis					1186:1194	CDDP-induced apoptosis	1173:1194	CDDP-induced apoptosis	1173:1194	Gene manipulation studies revealed that O-GlcNAcylation of p53/c-Myc is in part a regulator of CDDP-induced apoptosis.
28878262	5	3	theme	p53	789:791	arg1	O-GlcNAcylation					770:784	O-GlcNAcylation	770:784	O-GlcNAcylation of p53 under certain cellular contexts, i.e. high p53 activation,	770:850	Using co-immunoprecipitation and correlation analyses, we found that O-GlcNAcylation of p53 under certain cellular contexts, i.e. high p53 activation, promotes its ubiquitin-mediated proteasomal degradation, resulting in a gain of oncogenic and anti-apoptotic functions.
28878262	3	4	from	hyper-O-GlcNAcylation	399:419	arg1	cells					439:443	lung carcinoma cells	424:443	lung carcinoma cells	424:443	Here, we found that hyper-O-GlcNAcylation in lung carcinoma cells by O-GlcNAcase inhibition renders the cells to apoptosis resistance to cisplatin (CDDP).
28878262	7	5	theme	apoptosis	1186:1194	arg1	O-GlcNAcylation					1118:1132	O-GlcNAcylation	1118:1132	O-GlcNAcylation of p53/c-Myc	1118:1145	Gene manipulation studies revealed that O-GlcNAcylation of p53/c-Myc is in part a regulator of CDDP-induced apoptosis.
28878262	7	5	theme	apoptosis	1186:1194	arg1	regulator					1160:1168	a regulator	1158:1168	a regulator of CDDP-induced apoptosis	1158:1194	Gene manipulation studies revealed that O-GlcNAcylation of p53/c-Myc is in part a regulator of CDDP-induced apoptosis.
28878262	4	6	theme	status	693:698	arg1	independent					674:684	independent	674:684	independent	674:684	Profiling of various key regulatory proteins revealed an implication of either p53 or c-Myc in the apoptosis regulation by O-GlcNAcylation, independent of p53 status.
28878262	8	7	theme	CDDP	1224:1227	arg1	resistance					1229:1238	CDDP resistance	1224:1238	CDDP resistance by hyper-O-GlcNAcylation in lung carcinoma cells	1224:1287	Accordingly, we classified CDDP resistance by hyper-O-GlcNAcylation in lung carcinoma cells as either p53 or c-Myc dependence based on their molecular targets.
28878262	2	8	theme	O-GlcNAcylation	280:294	arg1	role					272:275	the role	268:275	the role of O-GlcNAcylation, a post-translational modification through HBP flux, in apoptosis	268:360	However, the role of O-GlcNAcylation, a post-translational modification through HBP flux, in apoptosis remains unclear.
28878262	9	9	theme	clinical	1495:1502	arg1	resistance					1509:1518	clinical drug resistance	1495:1518	clinical drug resistance	1495:1518	Together, our findings provide novel mechanisms for the regulation of lung cancer cell apoptosis that could be important in understanding clinical drug resistance and suggest O-GlcNAcylation as a potential target for cancer therapy.
28878262	0	10	theme	lung	92:95	arg1	carcinoma					97:105	human lung carcinoma	86:105	human lung carcinoma	86:105	Hyper-O-GlcNAcylation induces cisplatin resistance via regulation of p53 and c-Myc in human lung carcinoma.
28878262	9	11	theme	cancer	1432:1437	arg1	apoptosis					1444:1452	lung cancer cell apoptosis	1427:1452	lung cancer cell apoptosis	1427:1452	Together, our findings provide novel mechanisms for the regulation of lung cancer cell apoptosis that could be important in understanding clinical drug resistance and suggest O-GlcNAcylation as a potential target for cancer therapy.
28878262	5	12	theme	anti-apoptotic	946:959	arg1	functions					961:969	oncogenic and anti-apoptotic functions	932:969	oncogenic and anti-apoptotic functions	932:969	Using co-immunoprecipitation and correlation analyses, we found that O-GlcNAcylation of p53 under certain cellular contexts, i.e. high p53 activation, promotes its ubiquitin-mediated proteasomal degradation, resulting in a gain of oncogenic and anti-apoptotic functions.
28878262	8	13	theme	lung	1268:1271	arg1	cells					1283:1287	lung carcinoma cells	1268:1287	lung carcinoma cells	1268:1287	Accordingly, we classified CDDP resistance by hyper-O-GlcNAcylation in lung carcinoma cells as either p53 or c-Myc dependence based on their molecular targets.
28878262	5	14	theme	ubiquitin-mediated	865:882	arg1	degradation					896:906	its ubiquitin-mediated proteasomal degradation	861:906	its ubiquitin-mediated proteasomal degradation	861:906	Using co-immunoprecipitation and correlation analyses, we found that O-GlcNAcylation of p53 under certain cellular contexts, i.e. high p53 activation, promotes its ubiquitin-mediated proteasomal degradation, resulting in a gain of oncogenic and anti-apoptotic functions.
28878262	9	15	theme	drug	1504:1507	arg1	resistance					1509:1518	clinical drug resistance	1495:1518	clinical drug resistance	1495:1518	Together, our findings provide novel mechanisms for the regulation of lung cancer cell apoptosis that could be important in understanding clinical drug resistance and suggest O-GlcNAcylation as a potential target for cancer therapy.
28878262	0	16	from	regulation	55:64	arg1	carcinoma					97:105	human lung carcinoma	86:105	human lung carcinoma	86:105	Hyper-O-GlcNAcylation induces cisplatin resistance via regulation of p53 and c-Myc in human lung carcinoma.
28878262	9	17	theme	cancer	1574:1579	arg1	therapy					1581:1587	cancer therapy	1574:1587	cancer therapy	1574:1587	Together, our findings provide novel mechanisms for the regulation of lung cancer cell apoptosis that could be important in understanding clinical drug resistance and suggest O-GlcNAcylation as a potential target for cancer therapy.
28878262	5	18	theme	proteasomal	884:894	arg1	degradation					896:906	its ubiquitin-mediated proteasomal degradation	861:906	its ubiquitin-mediated proteasomal degradation	861:906	Using co-immunoprecipitation and correlation analyses, we found that O-GlcNAcylation of p53 under certain cellular contexts, i.e. high p53 activation, promotes its ubiquitin-mediated proteasomal degradation, resulting in a gain of oncogenic and anti-apoptotic functions.
28878262	6	19	theme	c-Myc	1004:1008	arg1	O-GlcNAcylation					985:999	O-GlcNAcylation	985:999	O-GlcNAcylation of c-Myc	985:1008	By contrast, O-GlcNAcylation of c-Myc inhibits its ubiquitination and subsequent proteasomal degradation.
28878262	5	20	theme	functions	961:969	arg1	gain					924:927	a gain	922:927	a gain of oncogenic and anti-apoptotic functions	922:969	Using co-immunoprecipitation and correlation analyses, we found that O-GlcNAcylation of p53 under certain cellular contexts, i.e. high p53 activation, promotes its ubiquitin-mediated proteasomal degradation, resulting in a gain of oncogenic and anti-apoptotic functions.
28878262	3	21	theme	lung	424:427	arg1	cells					439:443	lung carcinoma cells	424:443	lung carcinoma cells	424:443	Here, we found that hyper-O-GlcNAcylation in lung carcinoma cells by O-GlcNAcase inhibition renders the cells to apoptosis resistance to cisplatin (CDDP).
28878262	4	22	theme	key	555:557	arg1	proteins					570:577	various key regulatory proteins	547:577	various key regulatory proteins	547:577	Profiling of various key regulatory proteins revealed an implication of either p53 or c-Myc in the apoptosis regulation by O-GlcNAcylation, independent of p53 status.
28878262	1	23	from	metabolism	117:126	arg1	HBP					164:166	HBP	164:166	HBP	164:166	Aberrant metabolism in hexosamine biosynthetic pathway (HBP) has been observed in several cancers, affecting cellular signaling and tumor progression.
28878262	1	23	from	metabolism	117:126	arg1	pathway					155:161	hexosamine biosynthetic pathway	131:161	hexosamine biosynthetic pathway (HBP)	131:167	Aberrant metabolism in hexosamine biosynthetic pathway (HBP) has been observed in several cancers, affecting cellular signaling and tumor progression.
28878262	2	24	theme	post-translational	299:316	arg1	O-GlcNAcylation					280:294	O-GlcNAcylation	280:294	O-GlcNAcylation	280:294	However, the role of O-GlcNAcylation, a post-translational modification through HBP flux, in apoptosis remains unclear.
28878262	2	24	theme	post-translational	299:316	arg1	modification					318:329	a post-translational modification	297:329	a post-translational modification through HBP flux	297:346	However, the role of O-GlcNAcylation, a post-translational modification through HBP flux, in apoptosis remains unclear.
28878262	3	25	theme	carcinoma	429:437	arg1	cells					439:443	lung carcinoma cells	424:443	lung carcinoma cells	424:443	Here, we found that hyper-O-GlcNAcylation in lung carcinoma cells by O-GlcNAcase inhibition renders the cells to apoptosis resistance to cisplatin (CDDP).
28878262	5	26	theme	high	831:834	arg1	activation					840:849	high p53 activation	831:849	high p53 activation	831:849	Using co-immunoprecipitation and correlation analyses, we found that O-GlcNAcylation of p53 under certain cellular contexts, i.e. high p53 activation, promotes its ubiquitin-mediated proteasomal degradation, resulting in a gain of oncogenic and anti-apoptotic functions.
28878262	4	27	theme	various	547:553	arg1	proteins					570:577	various key regulatory proteins	547:577	various key regulatory proteins	547:577	Profiling of various key regulatory proteins revealed an implication of either p53 or c-Myc in the apoptosis regulation by O-GlcNAcylation, independent of p53 status.
28878262	8	28	dep	p53	1299:1301	arg1	dependence					1312:1321	dependence	1312:1321	dependence	1312:1321	Accordingly, we classified CDDP resistance by hyper-O-GlcNAcylation in lung carcinoma cells as either p53 or c-Myc dependence based on their molecular targets.
28878262	8	29	theme	carcinoma	1273:1281	arg1	cells					1283:1287	lung carcinoma cells	1268:1287	lung carcinoma cells	1268:1287	Accordingly, we classified CDDP resistance by hyper-O-GlcNAcylation in lung carcinoma cells as either p53 or c-Myc dependence based on their molecular targets.
28878262	1	30	theme	several	190:196	arg1	cancers					198:204	several cancers	190:204	several cancers	190:204	Aberrant metabolism in hexosamine biosynthetic pathway (HBP) has been observed in several cancers, affecting cellular signaling and tumor progression.
28878262	0	31	theme	cisplatin	30:38	arg1	resistance					40:49	cisplatin resistance	30:49	cisplatin resistance	30:49	Hyper-O-GlcNAcylation induces cisplatin resistance via regulation of p53 and c-Myc in human lung carcinoma.
28878262	4	32	theme	proteins	570:577	arg1	Profiling					534:542	Profiling	534:542	Profiling of various key regulatory proteins	534:577	Profiling of various key regulatory proteins revealed an implication of either p53 or c-Myc in the apoptosis regulation by O-GlcNAcylation, independent of p53 status.
28878262	7	33	theme	p53/c-Myc	1137:1145	arg1	O-GlcNAcylation					1118:1132	O-GlcNAcylation	1118:1132	O-GlcNAcylation of p53/c-Myc	1118:1145	Gene manipulation studies revealed that O-GlcNAcylation of p53/c-Myc is in part a regulator of CDDP-induced apoptosis.
28878262	7	33	theme	p53/c-Myc	1137:1145	arg1	regulator					1160:1168	a regulator	1158:1168	a regulator of CDDP-induced apoptosis	1158:1194	Gene manipulation studies revealed that O-GlcNAcylation of p53/c-Myc is in part a regulator of CDDP-induced apoptosis.
28878262	1	34	theme	Aberrant	108:115	arg1	metabolism					117:126	Aberrant metabolism	108:126	Aberrant metabolism in hexosamine biosynthetic pathway (HBP)	108:167	Aberrant metabolism in hexosamine biosynthetic pathway (HBP) has been observed in several cancers, affecting cellular signaling and tumor progression.
28878262	4	35	theme	regulatory	559:568	arg1	proteins					570:577	various key regulatory proteins	547:577	various key regulatory proteins	547:577	Profiling of various key regulatory proteins revealed an implication of either p53 or c-Myc in the apoptosis regulation by O-GlcNAcylation, independent of p53 status.
28878262	9	36	theme	potential	1553:1561	arg1	O-GlcNAcylation					1532:1546	O-GlcNAcylation	1532:1546	O-GlcNAcylation	1532:1546	Together, our findings provide novel mechanisms for the regulation of lung cancer cell apoptosis that could be important in understanding clinical drug resistance and suggest O-GlcNAcylation as a potential target for cancer therapy.
28878262	9	36	theme	potential	1553:1561	arg1	target					1563:1568	a potential target	1551:1568	a potential target for cancer therapy	1551:1587	Together, our findings provide novel mechanisms for the regulation of lung cancer cell apoptosis that could be important in understanding clinical drug resistance and suggest O-GlcNAcylation as a potential target for cancer therapy.
28878262	3	37	theme	O-GlcNAcase	448:458	arg1	inhibition					460:469	O-GlcNAcase inhibition	448:469	O-GlcNAcase inhibition	448:469	Here, we found that hyper-O-GlcNAcylation in lung carcinoma cells by O-GlcNAcase inhibition renders the cells to apoptosis resistance to cisplatin (CDDP).
28878262	5	38	theme	certain	799:805	arg1	contexts					816:823	certain cellular contexts	799:823	certain cellular contexts	799:823	Using co-immunoprecipitation and correlation analyses, we found that O-GlcNAcylation of p53 under certain cellular contexts, i.e. high p53 activation, promotes its ubiquitin-mediated proteasomal degradation, resulting in a gain of oncogenic and anti-apoptotic functions.
28878262	7	39	from	regulator	1160:1168	arg1	part					1153:1156	part	1153:1156	part	1153:1156	Gene manipulation studies revealed that O-GlcNAcylation of p53/c-Myc is in part a regulator of CDDP-induced apoptosis.
28878262	5	40	theme	correlation	734:744	arg1	analyses					746:753	correlation analyses	734:753	correlation analyses	734:753	Using co-immunoprecipitation and correlation analyses, we found that O-GlcNAcylation of p53 under certain cellular contexts, i.e. high p53 activation, promotes its ubiquitin-mediated proteasomal degradation, resulting in a gain of oncogenic and anti-apoptotic functions.
28878262	4	41	from	implication	591:601	arg1	regulation					643:652	the apoptosis regulation	629:652	the apoptosis regulation by O-GlcNAcylation	629:671	Profiling of various key regulatory proteins revealed an implication of either p53 or c-Myc in the apoptosis regulation by O-GlcNAcylation, independent of p53 status.
28878262	6	42	theme	subsequent	1042:1051	arg1	degradation					1065:1075	subsequent proteasomal degradation	1042:1075	subsequent proteasomal degradation	1042:1075	By contrast, O-GlcNAcylation of c-Myc inhibits its ubiquitination and subsequent proteasomal degradation.
28878262	4	43	theme	apoptosis	633:641	arg1	regulation					643:652	the apoptosis regulation	629:652	the apoptosis regulation by O-GlcNAcylation	629:671	Profiling of various key regulatory proteins revealed an implication of either p53 or c-Myc in the apoptosis regulation by O-GlcNAcylation, independent of p53 status.
28878262	0	44	theme	p53	69:71	arg1	regulation					55:64	regulation	55:64	regulation of p53 and c-Myc in human lung carcinoma	55:105	Hyper-O-GlcNAcylation induces cisplatin resistance via regulation of p53 and c-Myc in human lung carcinoma.
28878262	9	45	theme	lung	1427:1430	arg1	cancer					1432:1437	lung cancer	1427:1437	lung cancer cell apoptosis	1427:1452	Together, our findings provide novel mechanisms for the regulation of lung cancer cell apoptosis that could be important in understanding clinical drug resistance and suggest O-GlcNAcylation as a potential target for cancer therapy.
28878262	1	46	located	observed	178:185	arg1	cancers					198:204	several cancers	190:204	several cancers	190:204	Aberrant metabolism in hexosamine biosynthetic pathway (HBP) has been observed in several cancers, affecting cellular signaling and tumor progression.
28878262	1	46	located	observed	178:185	arg2	metabolism					117:126	Aberrant metabolism	108:126	Aberrant metabolism in hexosamine biosynthetic pathway (HBP)	108:167	Aberrant metabolism in hexosamine biosynthetic pathway (HBP) has been observed in several cancers, affecting cellular signaling and tumor progression.
28878262	9	47	theme	novel	1388:1392	arg1	mechanisms					1394:1403	novel mechanisms	1388:1403	novel mechanisms for the regulation of lung cancer cell apoptosis that could be important in understanding clinical drug resistance	1388:1518	Together, our findings provide novel mechanisms for the regulation of lung cancer cell apoptosis that could be important in understanding clinical drug resistance and suggest O-GlcNAcylation as a potential target for cancer therapy.
28878262	3	48	theme	apoptosis	492:500	arg1	resistance					502:511	apoptosis resistance	492:511	apoptosis resistance to cisplatin (CDDP)	492:531	Here, we found that hyper-O-GlcNAcylation in lung carcinoma cells by O-GlcNAcase inhibition renders the cells to apoptosis resistance to cisplatin (CDDP).
28878262	9	49	theme	cell	1439:1442	arg1	apoptosis					1444:1452	lung cancer cell apoptosis	1427:1452	lung cancer cell apoptosis	1427:1452	Together, our findings provide novel mechanisms for the regulation of lung cancer cell apoptosis that could be important in understanding clinical drug resistance and suggest O-GlcNAcylation as a potential target for cancer therapy.
28878262	5	50	theme	oncogenic	932:940	arg1	functions					961:969	oncogenic and anti-apoptotic functions	932:969	oncogenic and anti-apoptotic functions	932:969	Using co-immunoprecipitation and correlation analyses, we found that O-GlcNAcylation of p53 under certain cellular contexts, i.e. high p53 activation, promotes its ubiquitin-mediated proteasomal degradation, resulting in a gain of oncogenic and anti-apoptotic functions.
28878262	2	51	from	role	272:275	arg1	apoptosis					352:360	apoptosis	352:360	apoptosis	352:360	However, the role of O-GlcNAcylation, a post-translational modification through HBP flux, in apoptosis remains unclear.
28878262	9	52	theme	apoptosis	1444:1452	arg1	regulation					1413:1422	the regulation	1409:1422	the regulation of lung cancer cell apoptosis	1409:1452	Together, our findings provide novel mechanisms for the regulation of lung cancer cell apoptosis that could be important in understanding clinical drug resistance and suggest O-GlcNAcylation as a potential target for cancer therapy.
28878262	7	53	theme	Gene	1078:1081	arg1	studies					1096:1102	Gene manipulation studies	1078:1102	Gene manipulation studies	1078:1102	Gene manipulation studies revealed that O-GlcNAcylation of p53/c-Myc is in part a regulator of CDDP-induced apoptosis.
28878262	8	54	from	resistance	1229:1238	arg1	cells					1283:1287	lung carcinoma cells	1268:1287	lung carcinoma cells	1268:1287	Accordingly, we classified CDDP resistance by hyper-O-GlcNAcylation in lung carcinoma cells as either p53 or c-Myc dependence based on their molecular targets.
28878262	1	55	theme	hexosamine	131:140	arg1	HBP					164:166	HBP	164:166	HBP	164:166	Aberrant metabolism in hexosamine biosynthetic pathway (HBP) has been observed in several cancers, affecting cellular signaling and tumor progression.
28878262	1	55	theme	hexosamine	131:140	arg1	pathway					155:161	hexosamine biosynthetic pathway	131:161	hexosamine biosynthetic pathway (HBP)	131:167	Aberrant metabolism in hexosamine biosynthetic pathway (HBP) has been observed in several cancers, affecting cellular signaling and tumor progression.
28878262	1	56	theme	cellular	217:224	arg1	signaling					226:234	cellular signaling	217:234	cellular signaling	217:234	Aberrant metabolism in hexosamine biosynthetic pathway (HBP) has been observed in several cancers, affecting cellular signaling and tumor progression.
28878262	7	57	theme	manipulation	1083:1094	arg1	studies					1096:1102	Gene manipulation studies	1078:1102	Gene manipulation studies	1078:1102	Gene manipulation studies revealed that O-GlcNAcylation of p53/c-Myc is in part a regulator of CDDP-induced apoptosis.
28878262	1	58	theme	biosynthetic	142:153	arg1	HBP					164:166	HBP	164:166	HBP	164:166	Aberrant metabolism in hexosamine biosynthetic pathway (HBP) has been observed in several cancers, affecting cellular signaling and tumor progression.
28878262	1	58	theme	biosynthetic	142:153	arg1	pathway					155:161	hexosamine biosynthetic pathway	131:161	hexosamine biosynthetic pathway (HBP)	131:167	Aberrant metabolism in hexosamine biosynthetic pathway (HBP) has been observed in several cancers, affecting cellular signaling and tumor progression.
28878262	2	59	theme	HBP	339:341	arg1	flux					343:346	HBP flux	339:346	HBP flux	339:346	However, the role of O-GlcNAcylation, a post-translational modification through HBP flux, in apoptosis remains unclear.
28878262	0	60	theme	c-Myc	77:81	arg1	regulation					55:64	regulation	55:64	regulation of p53 and c-Myc in human lung carcinoma	55:105	Hyper-O-GlcNAcylation induces cisplatin resistance via regulation of p53 and c-Myc in human lung carcinoma.
28878262	8	61	theme	molecular	1338:1346	arg1	targets					1348:1354	their molecular targets	1332:1354	their molecular targets	1332:1354	Accordingly, we classified CDDP resistance by hyper-O-GlcNAcylation in lung carcinoma cells as either p53 or c-Myc dependence based on their molecular targets.
28878262	5	62	dep	activation	840:849	arg1	i.e.					826:829	i.e.	826:829	i.e.	826:829	Using co-immunoprecipitation and correlation analyses, we found that O-GlcNAcylation of p53 under certain cellular contexts, i.e. high p53 activation, promotes its ubiquitin-mediated proteasomal degradation, resulting in a gain of oncogenic and anti-apoptotic functions.
28878262	4	63	theme	p53	689:691	arg1	status					693:698	p53 status	689:698	p53 status	689:698	Profiling of various key regulatory proteins revealed an implication of either p53 or c-Myc in the apoptosis regulation by O-GlcNAcylation, independent of p53 status.
28878262	4	64	theme	c-Myc	620:624	arg1	implication					591:601	an implication	588:601	an implication of either p53 or c-Myc in the apoptosis regulation by O-GlcNAcylation	588:671	Profiling of various key regulatory proteins revealed an implication of either p53 or c-Myc in the apoptosis regulation by O-GlcNAcylation, independent of p53 status.
28878262	5	65	theme	cellular	807:814	arg1	contexts					816:823	certain cellular contexts	799:823	certain cellular contexts	799:823	Using co-immunoprecipitation and correlation analyses, we found that O-GlcNAcylation of p53 under certain cellular contexts, i.e. high p53 activation, promotes its ubiquitin-mediated proteasomal degradation, resulting in a gain of oncogenic and anti-apoptotic functions.
28878262	5	66	theme	p53	836:838	arg1	activation					840:849	high p53 activation	831:849	high p53 activation	831:849	Using co-immunoprecipitation and correlation analyses, we found that O-GlcNAcylation of p53 under certain cellular contexts, i.e. high p53 activation, promotes its ubiquitin-mediated proteasomal degradation, resulting in a gain of oncogenic and anti-apoptotic functions.
28878262	4	67	theme	p53	613:615	arg1	implication					591:601	an implication	588:601	an implication of either p53 or c-Myc in the apoptosis regulation by O-GlcNAcylation	588:671	Profiling of various key regulatory proteins revealed an implication of either p53 or c-Myc in the apoptosis regulation by O-GlcNAcylation, independent of p53 status.
28878262	1	68	theme	tumor	240:244	arg1	progression					246:256	tumor progression	240:256	tumor progression	240:256	Aberrant metabolism in hexosamine biosynthetic pathway (HBP) has been observed in several cancers, affecting cellular signaling and tumor progression.
36903375	3	0	theme	modification	464:475	arg1	proportion					441:450	the proportion	437:450	the proportion of O-GlcNAc modification	437:475	In this study, an OGT binding peptide (OBP)-tagged strategy for improving the proportion of O-GlcNAc modification was established successfully in E. coli.
36903375	10	1	theme	functional	1158:1167	arg1	research					1169:1176	further functional research	1150:1176	further functional research	1150:1176	These results indicated that the OBP-tagged strategy was a successful approach to improve the O-GlcNAcylation of a target protein for further functional research.
36903375	6	2	theme	P1Tau	710:714	arg1	level					701:705	the O-GlcNAc level	688:705	the O-GlcNAc level of P1Tau and TauP1	688:724	Compared with Tau, the O-GlcNAc level of P1Tau and TauP1 increased 4~6-fold.
36903375	10	3	theme	further	1150:1156	arg1	research					1169:1176	further functional research	1150:1176	further functional research	1150:1176	These results indicated that the OBP-tagged strategy was a successful approach to improve the O-GlcNAcylation of a target protein for further functional research.
36903375	2	4	theme	O-GlcNAc-modified	276:292	arg1	proteins					301:308	O-GlcNAc-modified target proteins	276:308	O-GlcNAc-modified target proteins	276:308	However, a large number of O-GlcNAc-modified target proteins are costly, inefficient, and complicated to prepare.
36903375	4	5	theme	target	553:558	arg1	Tau					568:570	target protein Tau	553:570	target protein Tau as tagged Tau	553:584	OBP (P1, P2, or P3) was fused with target protein Tau as tagged Tau.
36903375	2	6	theme	large	260:264	arg1	number					266:271	a large number	258:271	a large number of O-GlcNAc-modified target proteins	258:308	However, a large number of O-GlcNAc-modified target proteins are costly, inefficient, and complicated to prepare.
36903375	2	6	theme	large	260:264	arg1	costly					314:319	costly	314:319	costly	314:319	However, a large number of O-GlcNAc-modified target proteins are costly, inefficient, and complicated to prepare.
36903375	3	7	theme	OGT	381:383	arg1	peptide					393:399	OGT binding peptide	381:399	OGT binding peptide	381:399	In this study, an OGT binding peptide (OBP)-tagged strategy for improving the proportion of O-GlcNAc modification was established successfully in E. coli.
36903375	7	8	dep	P1Tau	760:764	arg1	the					756:758	the	756:758	the	756:758	Moreover, the P1Tau and TauP1 increased the O-GlcNAc-modified homogeneity.
36903375	10	9	theme	successful	1075:1084	arg1	approach					1086:1093	a successful approach	1073:1093	a successful approach to improve the O-GlcNAcylation of a target protein for further functional research	1073:1176	These results indicated that the OBP-tagged strategy was a successful approach to improve the O-GlcNAcylation of a target protein for further functional research.
36903375	10	9	theme	successful	1075:1084	arg1	strategy					1060:1067	the OBP-tagged strategy	1045:1067	the OBP-tagged strategy	1045:1067	These results indicated that the OBP-tagged strategy was a successful approach to improve the O-GlcNAcylation of a target protein for further functional research.
36903375	9	10	theme	O-GlcNAc	983:990	arg1	level					992:996	the O-GlcNAc level	979:996	the O-GlcNAc level of c-Myc and H2B	979:1013	This strategy was also used successfully to increase the O-GlcNAc level of c-Myc and H2B.
36903375	4	11	theme	tagged	575:580	arg1	Tau					582:584	tagged Tau	575:584	tagged Tau	575:584	OBP (P1, P2, or P3) was fused with target protein Tau as tagged Tau.
36903375	0	12	theme	Binding	4:10	arg1	Strategy					27:34	OGT Binding Peptide-Tagged Strategy	0:34	OGT Binding Peptide-Tagged Strategy	0:34	OGT Binding Peptide-Tagged Strategy Increases Protein O-GlcNAcylation Level in E. coli.
36903375	4	13	dep	OBP	518:520	arg1	P2					527:528	P2	527:528	P2	527:528	OBP (P1, P2, or P3) was fused with target protein Tau as tagged Tau.
36903375	4	13	dep	OBP	518:520	arg1	P3					534:535	P3	534:535	P3	534:535	OBP (P1, P2, or P3) was fused with target protein Tau as tagged Tau.
36903375	4	13	dep	OBP	518:520	arg1	P1					523:524	P1	523:524	P1	523:524	OBP (P1, P2, or P3) was fused with target protein Tau as tagged Tau.
36903375	0	14	theme	OGT	0:2	arg1	Strategy					27:34	OGT Binding Peptide-Tagged Strategy	0:34	OGT Binding Peptide-Tagged Strategy	0:34	OGT Binding Peptide-Tagged Strategy Increases Protein O-GlcNAcylation Level in E. coli.
36903375	2	15	theme	proteins	301:308	arg1	number					266:271	a large number	258:271	a large number of O-GlcNAc-modified target proteins	258:308	However, a large number of O-GlcNAc-modified target proteins are costly, inefficient, and complicated to prepare.
36903375	2	15	theme	proteins	301:308	arg1	costly					314:319	costly	314:319	costly	314:319	However, a large number of O-GlcNAc-modified target proteins are costly, inefficient, and complicated to prepare.
36903375	8	16	from	O-GlcNAcylation	830:844	arg1	P1Tau					849:853	P1Tau	849:853	P1Tau	849:853	The high O-GlcNAcylation on P1Tau resulted in a significantly slower aggregation rate than Tau in vitro.
36903375	6	17	theme	O-GlcNAc	692:699	arg1	level					701:705	the O-GlcNAc level	688:705	the O-GlcNAc level of P1Tau and TauP1	688:724	Compared with Tau, the O-GlcNAc level of P1Tau and TauP1 increased 4~6-fold.
36903375	2	18	theme	target	294:299	arg1	proteins					301:308	O-GlcNAc-modified target proteins	276:308	O-GlcNAc-modified target proteins	276:308	However, a large number of O-GlcNAc-modified target proteins are costly, inefficient, and complicated to prepare.
36903375	8	19	theme	slower	883:888	arg1	rate					902:905	a significantly slower aggregation rate	867:905	a significantly slower aggregation rate than Tau in vitro	867:923	The high O-GlcNAcylation on P1Tau resulted in a significantly slower aggregation rate than Tau in vitro.
36903375	1	20	theme	substrate	189:197	arg1	proteins					199:206	substrate proteins	189:206	substrate proteins	189:206	O-GlcNAcylation is a single glycosylation of GlcNAc mediated by OGT, which regulates the function of substrate proteins and is closely related to many diseases.
36903375	0	21	theme	Peptide-Tagged	12:25	arg1	Strategy					27:34	OGT Binding Peptide-Tagged Strategy	0:34	OGT Binding Peptide-Tagged Strategy	0:34	OGT Binding Peptide-Tagged Strategy Increases Protein O-GlcNAcylation Level in E. coli.
36903375	1	22	gly	glycosylation	116:128	arg1	GlcNAc					133:138	GlcNAc	133:138	GlcNAc mediated by OGT	133:154	O-GlcNAcylation is a single glycosylation of GlcNAc mediated by OGT, which regulates the function of substrate proteins and is closely related to many diseases.
36903375	1	23	theme	single	109:114	arg1	glycosylation					116:128	a single glycosylation	107:128	a single glycosylation	107:128	O-GlcNAcylation is a single glycosylation of GlcNAc mediated by OGT, which regulates the function of substrate proteins and is closely related to many diseases.
36903375	1	23	theme	single	109:114	arg1	related					223:229	related	223:229	related	223:229	O-GlcNAcylation is a single glycosylation of GlcNAc mediated by OGT, which regulates the function of substrate proteins and is closely related to many diseases.
36903375	1	23	theme	single	109:114	arg1	O-GlcNAcylation					88:102	O-GlcNAcylation	88:102	O-GlcNAcylation	88:102	O-GlcNAcylation is a single glycosylation of GlcNAc mediated by OGT, which regulates the function of substrate proteins and is closely related to many diseases.
36903375	1	24	theme	proteins	199:206	arg1	function					177:184	the function	173:184	the function of substrate proteins	173:206	O-GlcNAcylation is a single glycosylation of GlcNAc mediated by OGT, which regulates the function of substrate proteins and is closely related to many diseases.
36903375	0	25	theme	Protein	46:52	arg1	Level					70:74	Protein O-GlcNAcylation Level	46:74	Protein O-GlcNAcylation Level	46:74	OGT Binding Peptide-Tagged Strategy Increases Protein O-GlcNAcylation Level in E. coli.
36903375	9	26	theme	H2B	1011:1013	arg1	level					992:996	the O-GlcNAc level	979:996	the O-GlcNAc level of c-Myc and H2B	979:1013	This strategy was also used successfully to increase the O-GlcNAc level of c-Myc and H2B.
36903375	3	27	theme	-tagged	406:412	arg1	strategy					414:421	an OGT binding peptide (OBP)-tagged strategy	378:421	an OGT binding peptide (OBP)-tagged strategy for improving the proportion of O-GlcNAc modification	378:475	In this study, an OGT binding peptide (OBP)-tagged strategy for improving the proportion of O-GlcNAc modification was established successfully in E. coli.
36903375	3	28	theme	binding	385:391	arg1	peptide					393:399	OGT binding peptide	381:399	OGT binding peptide	381:399	In this study, an OGT binding peptide (OBP)-tagged strategy for improving the proportion of O-GlcNAc modification was established successfully in E. coli.
36903375	8	29	theme	high	825:828	arg1	O-GlcNAcylation					830:844	The high O-GlcNAcylation	821:844	The high O-GlcNAcylation on P1Tau	821:853	The high O-GlcNAcylation on P1Tau resulted in a significantly slower aggregation rate than Tau in vitro.
36903375	8	30	theme	aggregation	890:900	arg1	rate					902:905	a significantly slower aggregation rate	867:905	a significantly slower aggregation rate than Tau in vitro	867:923	The high O-GlcNAcylation on P1Tau resulted in a significantly slower aggregation rate than Tau in vitro.
36903375	10	31	theme	OBP-tagged	1049:1058	arg1	approach					1086:1093	a successful approach	1073:1093	a successful approach to improve the O-GlcNAcylation of a target protein for further functional research	1073:1176	These results indicated that the OBP-tagged strategy was a successful approach to improve the O-GlcNAcylation of a target protein for further functional research.
36903375	10	31	theme	OBP-tagged	1049:1058	arg1	strategy					1060:1067	the OBP-tagged strategy	1045:1067	the OBP-tagged strategy	1045:1067	These results indicated that the OBP-tagged strategy was a successful approach to improve the O-GlcNAcylation of a target protein for further functional research.
36903375	0	32	theme	O-GlcNAcylation	54:68	arg1	Level					70:74	Protein O-GlcNAcylation Level	46:74	Protein O-GlcNAcylation Level	46:74	OGT Binding Peptide-Tagged Strategy Increases Protein O-GlcNAcylation Level in E. coli.
36903375	5	33	theme	tagged	594:599	arg1	Tau					601:603	tagged Tau	594:603	tagged Tau	594:603	Tau or tagged Tau was co-constructed with OGT into a vector expressed in E. coli.
36903375	3	34	theme	O-GlcNAc	455:462	arg1	modification					464:475	O-GlcNAc modification	455:475	O-GlcNAc modification	455:475	In this study, an OGT binding peptide (OBP)-tagged strategy for improving the proportion of O-GlcNAc modification was established successfully in E. coli.
36903375	10	35	theme	protein	1138:1144	arg1	O-GlcNAcylation					1110:1124	the O-GlcNAcylation	1106:1124	the O-GlcNAcylation of a target protein for further functional research	1106:1176	These results indicated that the OBP-tagged strategy was a successful approach to improve the O-GlcNAcylation of a target protein for further functional research.
36903375	3	36	dep	-tagged	406:412	arg1	peptide					393:399	OGT binding peptide	381:399	OGT binding peptide	381:399	In this study, an OGT binding peptide (OBP)-tagged strategy for improving the proportion of O-GlcNAc modification was established successfully in E. coli.
36903375	1	37	theme	GlcNAc	133:138	arg1	glycosylation					116:128	a single glycosylation	107:128	a single glycosylation	107:128	O-GlcNAcylation is a single glycosylation of GlcNAc mediated by OGT, which regulates the function of substrate proteins and is closely related to many diseases.
36903375	1	37	theme	GlcNAc	133:138	arg1	related					223:229	related	223:229	related	223:229	O-GlcNAcylation is a single glycosylation of GlcNAc mediated by OGT, which regulates the function of substrate proteins and is closely related to many diseases.
36903375	1	37	theme	GlcNAc	133:138	arg1	O-GlcNAcylation					88:102	O-GlcNAcylation	88:102	O-GlcNAcylation	88:102	O-GlcNAcylation is a single glycosylation of GlcNAc mediated by OGT, which regulates the function of substrate proteins and is closely related to many diseases.
36903375	10	38	theme	target	1131:1136	arg1	protein					1138:1144	a target protein	1129:1144	a target protein	1129:1144	These results indicated that the OBP-tagged strategy was a successful approach to improve the O-GlcNAcylation of a target protein for further functional research.
36903375	6	39	theme	TauP1	720:724	arg1	level					701:705	the O-GlcNAc level	688:705	the O-GlcNAc level of P1Tau and TauP1	688:724	Compared with Tau, the O-GlcNAc level of P1Tau and TauP1 increased 4~6-fold.
36903375	9	40	theme	c-Myc	1001:1005	arg1	level					992:996	the O-GlcNAc level	979:996	the O-GlcNAc level of c-Myc and H2B	979:1013	This strategy was also used successfully to increase the O-GlcNAc level of c-Myc and H2B.
36903375	9	41	used	used	949:952	arg2	strategy					931:938	This strategy	926:938	This strategy	926:938	This strategy was also used successfully to increase the O-GlcNAc level of c-Myc and H2B.
36903375	4	42	theme	protein	560:566	arg1	Tau					568:570	target protein Tau	553:570	target protein Tau as tagged Tau	553:584	OBP (P1, P2, or P3) was fused with target protein Tau as tagged Tau.
36903375	7	43	theme	O-GlcNAc-modified	790:806	arg1	homogeneity					808:818	the O-GlcNAc-modified homogeneity	786:818	the O-GlcNAc-modified homogeneity	786:818	Moreover, the P1Tau and TauP1 increased the O-GlcNAc-modified homogeneity.
36903375	1	44	theme	many	234:237	arg1	diseases					239:246	many diseases	234:246	many diseases	234:246	O-GlcNAcylation is a single glycosylation of GlcNAc mediated by OGT, which regulates the function of substrate proteins and is closely related to many diseases.
32684624	2	0	with	association	357:367	arg1	signalling					382:391	calcium signalling	374:391	calcium signalling	374:391	Cell motility is a prerequisite for metastasis, the major cause of lung cancer death, yet its association with calcium signalling and underlying regulatory axis remains an unexplored area.
32684624	2	0	with	association	357:367	arg1	axis					419:422	underlying regulatory axis	397:422	underlying regulatory axis	397:422	Cell motility is a prerequisite for metastasis, the major cause of lung cancer death, yet its association with calcium signalling and underlying regulatory axis remains an unexplored area.
32684624	6	1	theme	TRPM7	935:939	arg1	Inhibition					921:930	Inhibition	921:930	Inhibition of TRPM7	921:939	Inhibition of TRPM7 suppresses cell motility in various NSCLC cell lines and patient-derived primary cells and attenuates experimental lung metastases.
32684624	7	2	theme	sensor	1178:1183	arg1	upstream					1101:1108	upstream	1101:1108	upstream	1101:1108	Mechanistically, TRPM7 acts upstream of O-GlcNAcylation, a post-translational modification and a crucial sensor for metabolic changes.
32684624	10	3	theme	TRPM7/O-GlcNAc	1494:1507	arg1	axis					1509:1512	TRPM7/O-GlcNAc axis	1494:1512	TRPM7/O-GlcNAc axis	1494:1512	CONCLUSIONS TRPM7/O-GlcNAc axis represents a potential novel target for lung cancer therapy that may overcome metastasis.
32684624	2	4	theme	death	342:346	arg1	cause					321:325	the major cause	311:325	the major cause of lung cancer death	311:346	Cell motility is a prerequisite for metastasis, the major cause of lung cancer death, yet its association with calcium signalling and underlying regulatory axis remains an unexplored area.
32684624	2	4	theme	death	342:346	arg1	metastasis					299:308	metastasis	299:308	metastasis	299:308	Cell motility is a prerequisite for metastasis, the major cause of lung cancer death, yet its association with calcium signalling and underlying regulatory axis remains an unexplored area.
32684624	3	5	theme	clinical	566:573	arg1	outcomes					575:582	clinical outcomes	566:582	clinical outcomes in non-small cell lung cancer (NSCLC)	566:620	METHODS Bioinformatics database analyses were employed to assess correlations between calcium influx channels and clinical outcomes in non-small cell lung cancer (NSCLC).
32684624	7	6	theme	modification	1151:1162	arg1	upstream					1101:1108	upstream	1101:1108	upstream	1101:1108	Mechanistically, TRPM7 acts upstream of O-GlcNAcylation, a post-translational modification and a crucial sensor for metabolic changes.
32684624	10	7	theme	potential	1527:1535	arg1	target					1543:1548	a potential novel target	1525:1548	a potential novel target for lung cancer therapy that may overcome metastasis	1525:1601	CONCLUSIONS TRPM7/O-GlcNAc axis represents a potential novel target for lung cancer therapy that may overcome metastasis.
32684624	1	8	theme	transduction	170:181	arg1	element					183:189	an essential signal transduction element	150:189	an essential signal transduction element that has been associated with aggressive behaviours in several cancers	150:260	BACKGROUND Calcium is an essential signal transduction element that has been associated with aggressive behaviours in several cancers.
32684624	1	8	theme	transduction	170:181	arg1	Calcium					139:145	BACKGROUND Calcium	128:145	BACKGROUND Calcium	128:145	BACKGROUND Calcium is an essential signal transduction element that has been associated with aggressive behaviours in several cancers.
32684624	5	9	dep	RESULTS	794:800	arg1	correlates					835:844	correlates	835:844	correlates well with the low survival rate of patients and high metastatic potential	835:918	RESULTS High expression of TRPM7 channel correlates well with the low survival rate of patients and high metastatic potential.
32684624	8	10	theme	TRPM7/O-GlcNAc	1299:1312	arg1	c-Myc					1257:1261	c-Myc	1257:1261	c-Myc	1257:1261	We reveal for the first time that caveolin-1 and c-Myc are favourable molecular targets of TRPM7/O-GlcNAc that regulates NSCLC motility.
32684624	8	10	theme	TRPM7/O-GlcNAc	1299:1312	arg1	caveolin-1					1242:1251	caveolin-1	1242:1251	caveolin-1	1242:1251	We reveal for the first time that caveolin-1 and c-Myc are favourable molecular targets of TRPM7/O-GlcNAc that regulates NSCLC motility.
32684624	8	10	theme	TRPM7/O-GlcNAc	1299:1312	arg1	targets					1288:1294	favourable molecular targets	1267:1294	favourable molecular targets of TRPM7/O-GlcNAc that regulates NSCLC motility	1267:1342	We reveal for the first time that caveolin-1 and c-Myc are favourable molecular targets of TRPM7/O-GlcNAc that regulates NSCLC motility.
32684624	6	11	link	patient-derived	998:1012	arg1	cells					1022:1026	patient-derived primary cells	998:1026	patient-derived primary cells	998:1026	Inhibition of TRPM7 suppresses cell motility in various NSCLC cell lines and patient-derived primary cells and attenuates experimental lung metastases.
32684624	7	12	theme	O-GlcNAcylation	1113:1127	arg1	upstream					1101:1108	upstream	1101:1108	upstream	1101:1108	Mechanistically, TRPM7 acts upstream of O-GlcNAcylation, a post-translational modification and a crucial sensor for metabolic changes.
32684624	4	13	from	roles	649:653	arg1	cell					677:680	cell migration and invasion	677:703	cell migration and invasion	677:703	Functional and regulatory roles of influx channels in cell migration and invasion were conducted and experimental lung metastasis was examined using in vivo live imaging.
32684624	6	14	theme	NSCLC	977:981	arg1	lines					988:992	various NSCLC cell lines	969:992	various NSCLC cell lines	969:992	Inhibition of TRPM7 suppresses cell motility in various NSCLC cell lines and patient-derived primary cells and attenuates experimental lung metastases.
32684624	4	15	theme	influx	658:663	arg1	channels					665:672	influx channels	658:672	influx channels	658:672	Functional and regulatory roles of influx channels in cell migration and invasion were conducted and experimental lung metastasis was examined using in vivo live imaging.
32684624	5	16	theme	survival	864:871	arg1	rate					873:876	the low survival rate	856:876	the low survival rate of patients and high metastatic potential	856:918	RESULTS High expression of TRPM7 channel correlates well with the low survival rate of patients and high metastatic potential.
32684624	8	17	theme	favourable	1267:1276	arg1	c-Myc					1257:1261	c-Myc	1257:1261	c-Myc	1257:1261	We reveal for the first time that caveolin-1 and c-Myc are favourable molecular targets of TRPM7/O-GlcNAc that regulates NSCLC motility.
32684624	8	17	theme	favourable	1267:1276	arg1	caveolin-1					1242:1251	caveolin-1	1242:1251	caveolin-1	1242:1251	We reveal for the first time that caveolin-1 and c-Myc are favourable molecular targets of TRPM7/O-GlcNAc that regulates NSCLC motility.
32684624	8	17	theme	favourable	1267:1276	arg1	targets					1288:1294	favourable molecular targets	1267:1294	favourable molecular targets of TRPM7/O-GlcNAc that regulates NSCLC motility	1267:1342	We reveal for the first time that caveolin-1 and c-Myc are favourable molecular targets of TRPM7/O-GlcNAc that regulates NSCLC motility.
32684624	4	18	theme	experimental	724:735	arg1	metastasis					742:751	experimental lung metastasis	724:751	experimental lung metastasis	724:751	Functional and regulatory roles of influx channels in cell migration and invasion were conducted and experimental lung metastasis was examined using in vivo live imaging.
32684624	6	19	theme	cell	952:955	arg1	motility					957:964	cell motility	952:964	cell motility in various NSCLC cell lines and patient-derived primary cells	952:1026	Inhibition of TRPM7 suppresses cell motility in various NSCLC cell lines and patient-derived primary cells and attenuates experimental lung metastases.
32684624	0	20	from	caveolin-1	98:107	arg1	carcinoma					117:125	lung carcinoma	112:125	lung carcinoma	112:125	A novel TRPM7/O-GlcNAc axis mediates tumour cell motility and metastasis by stabilising c-Myc and caveolin-1 in lung carcinoma.
32684624	1	21	from	behaviours	232:241	arg1	cancers					254:260	several cancers	246:260	several cancers	246:260	BACKGROUND Calcium is an essential signal transduction element that has been associated with aggressive behaviours in several cancers.
32684624	2	22	theme	Cell	263:266	arg1	prerequisite					282:293	a prerequisite	280:293	a prerequisite for metastasis, the major cause of lung cancer death	280:346	Cell motility is a prerequisite for metastasis, the major cause of lung cancer death, yet its association with calcium signalling and underlying regulatory axis remains an unexplored area.
32684624	2	22	theme	Cell	263:266	arg1	motility					268:275	Cell motility	263:275	Cell motility	263:275	Cell motility is a prerequisite for metastasis, the major cause of lung cancer death, yet its association with calcium signalling and underlying regulatory axis remains an unexplored area.
32684624	1	23	theme	BACKGROUND	128:137	arg1	element					183:189	an essential signal transduction element	150:189	an essential signal transduction element that has been associated with aggressive behaviours in several cancers	150:260	BACKGROUND Calcium is an essential signal transduction element that has been associated with aggressive behaviours in several cancers.
32684624	1	23	theme	BACKGROUND	128:137	arg1	Calcium					139:145	BACKGROUND Calcium	128:145	BACKGROUND Calcium	128:145	BACKGROUND Calcium is an essential signal transduction element that has been associated with aggressive behaviours in several cancers.
32684624	6	24	theme	lung	1056:1059	arg1	metastases					1061:1070	experimental lung metastases	1043:1070	experimental lung metastases	1043:1070	Inhibition of TRPM7 suppresses cell motility in various NSCLC cell lines and patient-derived primary cells and attenuates experimental lung metastases.
32684624	0	25	from	c-Myc	88:92	arg1	carcinoma					117:125	lung carcinoma	112:125	lung carcinoma	112:125	A novel TRPM7/O-GlcNAc axis mediates tumour cell motility and metastasis by stabilising c-Myc and caveolin-1 in lung carcinoma.
32684624	5	26	theme	metastatic	899:908	arg1	potential					910:918	high metastatic potential	894:918	high metastatic potential	894:918	RESULTS High expression of TRPM7 channel correlates well with the low survival rate of patients and high metastatic potential.
32684624	10	27	theme	lung	1554:1557	arg1	therapy					1566:1572	lung cancer therapy	1554:1572	lung cancer therapy	1554:1572	CONCLUSIONS TRPM7/O-GlcNAc axis represents a potential novel target for lung cancer therapy that may overcome metastasis.
32684624	3	28	from	channels	553:560	arg1	NSCLC					615:619	NSCLC	615:619	NSCLC	615:619	METHODS Bioinformatics database analyses were employed to assess correlations between calcium influx channels and clinical outcomes in non-small cell lung cancer (NSCLC).
32684624	3	28	from	channels	553:560	arg1	cancer					607:612	non-small cell lung cancer	587:612	non-small cell lung cancer (NSCLC)	587:620	METHODS Bioinformatics database analyses were employed to assess correlations between calcium influx channels and clinical outcomes in non-small cell lung cancer (NSCLC).
32684624	1	29	theme	essential	153:161	arg1	element					183:189	an essential signal transduction element	150:189	an essential signal transduction element that has been associated with aggressive behaviours in several cancers	150:260	BACKGROUND Calcium is an essential signal transduction element that has been associated with aggressive behaviours in several cancers.
32684624	1	29	theme	essential	153:161	arg1	Calcium					139:145	BACKGROUND Calcium	128:145	BACKGROUND Calcium	128:145	BACKGROUND Calcium is an essential signal transduction element that has been associated with aggressive behaviours in several cancers.
32684624	4	30	theme	live	780:783	arg1	imaging					785:791	in vivo live imaging	772:791	in vivo live imaging	772:791	Functional and regulatory roles of influx channels in cell migration and invasion were conducted and experimental lung metastasis was examined using in vivo live imaging.
32684624	6	31	theme	patient-derived	998:1012	arg1	cells					1022:1026	patient-derived primary cells	998:1026	patient-derived primary cells	998:1026	Inhibition of TRPM7 suppresses cell motility in various NSCLC cell lines and patient-derived primary cells and attenuates experimental lung metastases.
32684624	2	32	theme	regulatory	408:417	arg1	axis					419:422	underlying regulatory axis	397:422	underlying regulatory axis	397:422	Cell motility is a prerequisite for metastasis, the major cause of lung cancer death, yet its association with calcium signalling and underlying regulatory axis remains an unexplored area.
32684624	5	33	theme	channel	827:833	arg1	expression					807:816	High expression	802:816	High expression of TRPM7 channel	802:833	RESULTS High expression of TRPM7 channel correlates well with the low survival rate of patients and high metastatic potential.
32684624	4	34	theme	in	772:773	arg1	imaging					785:791	in vivo live imaging	772:791	in vivo live imaging	772:791	Functional and regulatory roles of influx channels in cell migration and invasion were conducted and experimental lung metastasis was examined using in vivo live imaging.
32684624	3	35	theme	Bioinformatics	460:473	arg1	analyses					484:491	METHODS Bioinformatics database analyses	452:491	METHODS Bioinformatics database analyses	452:491	METHODS Bioinformatics database analyses were employed to assess correlations between calcium influx channels and clinical outcomes in non-small cell lung cancer (NSCLC).
32684624	0	36	theme	TRPM7/O-GlcNAc	8:21	arg1	axis					23:26	A novel TRPM7/O-GlcNAc axis	0:26	A novel TRPM7/O-GlcNAc axis	0:26	A novel TRPM7/O-GlcNAc axis mediates tumour cell motility and metastasis by stabilising c-Myc and caveolin-1 in lung carcinoma.
32684624	2	37	theme	underlying	397:406	arg1	axis					419:422	underlying regulatory axis	397:422	underlying regulatory axis	397:422	Cell motility is a prerequisite for metastasis, the major cause of lung cancer death, yet its association with calcium signalling and underlying regulatory axis remains an unexplored area.
32684624	5	38	theme	High	802:805	arg1	expression					807:816	High expression	802:816	High expression of TRPM7 channel	802:833	RESULTS High expression of TRPM7 channel correlates well with the low survival rate of patients and high metastatic potential.
32684624	6	39	from	motility	957:964	arg1	cells					1022:1026	patient-derived primary cells	998:1026	patient-derived primary cells	998:1026	Inhibition of TRPM7 suppresses cell motility in various NSCLC cell lines and patient-derived primary cells and attenuates experimental lung metastases.
32684624	6	39	from	motility	957:964	arg1	lines					988:992	various NSCLC cell lines	969:992	various NSCLC cell lines	969:992	Inhibition of TRPM7 suppresses cell motility in various NSCLC cell lines and patient-derived primary cells and attenuates experimental lung metastases.
32684624	2	40	theme	cancer	335:340	arg1	death					342:346	lung cancer death	330:346	lung cancer death	330:346	Cell motility is a prerequisite for metastasis, the major cause of lung cancer death, yet its association with calcium signalling and underlying regulatory axis remains an unexplored area.
32684624	0	41	theme	cell	44:47	arg1	motility					49:56	tumour cell motility	37:56	tumour cell motility	37:56	A novel TRPM7/O-GlcNAc axis mediates tumour cell motility and metastasis by stabilising c-Myc and caveolin-1 in lung carcinoma.
32684624	1	42	theme	aggressive	221:230	arg1	behaviours					232:241	aggressive behaviours	221:241	aggressive behaviours in several cancers	221:260	BACKGROUND Calcium is an essential signal transduction element that has been associated with aggressive behaviours in several cancers.
32684624	4	43	dep	cell	677:680	arg1	invasion					696:703	invasion	696:703	invasion	696:703	Functional and regulatory roles of influx channels in cell migration and invasion were conducted and experimental lung metastasis was examined using in vivo live imaging.
32684624	4	43	dep	cell	677:680	arg1	migration					682:690	migration	682:690	migration	682:690	Functional and regulatory roles of influx channels in cell migration and invasion were conducted and experimental lung metastasis was examined using in vivo live imaging.
32684624	8	44	theme	molecular	1278:1286	arg1	c-Myc					1257:1261	c-Myc	1257:1261	c-Myc	1257:1261	We reveal for the first time that caveolin-1 and c-Myc are favourable molecular targets of TRPM7/O-GlcNAc that regulates NSCLC motility.
32684624	8	44	theme	molecular	1278:1286	arg1	caveolin-1					1242:1251	caveolin-1	1242:1251	caveolin-1	1242:1251	We reveal for the first time that caveolin-1 and c-Myc are favourable molecular targets of TRPM7/O-GlcNAc that regulates NSCLC motility.
32684624	8	44	theme	molecular	1278:1286	arg1	targets					1288:1294	favourable molecular targets	1267:1294	favourable molecular targets of TRPM7/O-GlcNAc that regulates NSCLC motility	1267:1342	We reveal for the first time that caveolin-1 and c-Myc are favourable molecular targets of TRPM7/O-GlcNAc that regulates NSCLC motility.
32684624	4	45	theme	Functional	623:632	arg1	roles					649:653	Functional and regulatory roles	623:653	Functional and regulatory roles of influx channels in cell migration and invasion	623:703	Functional and regulatory roles of influx channels in cell migration and invasion were conducted and experimental lung metastasis was examined using in vivo live imaging.
32684624	7	46	theme	crucial	1170:1176	arg1	sensor					1178:1183	a crucial sensor	1168:1183	a crucial sensor	1168:1183	Mechanistically, TRPM7 acts upstream of O-GlcNAcylation, a post-translational modification and a crucial sensor for metabolic changes.
32684624	10	47	dep	CONCLUSIONS	1482:1492	arg1	represents					1514:1523	represents	1514:1523	represents a potential novel target for lung cancer therapy that may overcome metastasis	1514:1601	CONCLUSIONS TRPM7/O-GlcNAc axis represents a potential novel target for lung cancer therapy that may overcome metastasis.
32684624	2	48	theme	major	315:319	arg1	cause					321:325	the major cause	311:325	the major cause of lung cancer death	311:346	Cell motility is a prerequisite for metastasis, the major cause of lung cancer death, yet its association with calcium signalling and underlying regulatory axis remains an unexplored area.
32684624	2	48	theme	major	315:319	arg1	metastasis					299:308	metastasis	299:308	metastasis	299:308	Cell motility is a prerequisite for metastasis, the major cause of lung cancer death, yet its association with calcium signalling and underlying regulatory axis remains an unexplored area.
32684624	7	49	theme	post-translational	1132:1149	arg1	modification					1151:1162	a post-translational modification	1130:1162	a post-translational modification	1130:1162	Mechanistically, TRPM7 acts upstream of O-GlcNAcylation, a post-translational modification and a crucial sensor for metabolic changes.
32684624	3	50	theme	influx	546:551	arg1	channels					553:560	calcium influx channels	538:560	calcium influx channels	538:560	METHODS Bioinformatics database analyses were employed to assess correlations between calcium influx channels and clinical outcomes in non-small cell lung cancer (NSCLC).
32684624	1	51	theme	signal	163:168	arg1	element					183:189	an essential signal transduction element	150:189	an essential signal transduction element that has been associated with aggressive behaviours in several cancers	150:260	BACKGROUND Calcium is an essential signal transduction element that has been associated with aggressive behaviours in several cancers.
32684624	1	51	theme	signal	163:168	arg1	Calcium					139:145	BACKGROUND Calcium	128:145	BACKGROUND Calcium	128:145	BACKGROUND Calcium is an essential signal transduction element that has been associated with aggressive behaviours in several cancers.
32684624	7	52	theme	metabolic	1189:1197	arg1	changes					1199:1205	metabolic changes	1189:1205	metabolic changes	1189:1205	Mechanistically, TRPM7 acts upstream of O-GlcNAcylation, a post-translational modification and a crucial sensor for metabolic changes.
32684624	4	53	theme	channels	665:672	arg1	roles					649:653	Functional and regulatory roles	623:653	Functional and regulatory roles of influx channels in cell migration and invasion	623:703	Functional and regulatory roles of influx channels in cell migration and invasion were conducted and experimental lung metastasis was examined using in vivo live imaging.
32684624	3	54	theme	non-small	587:595	arg1	NSCLC					615:619	NSCLC	615:619	NSCLC	615:619	METHODS Bioinformatics database analyses were employed to assess correlations between calcium influx channels and clinical outcomes in non-small cell lung cancer (NSCLC).
32684624	3	54	theme	non-small	587:595	arg1	cancer					607:612	non-small cell lung cancer	587:612	non-small cell lung cancer (NSCLC)	587:620	METHODS Bioinformatics database analyses were employed to assess correlations between calcium influx channels and clinical outcomes in non-small cell lung cancer (NSCLC).
32684624	5	55	theme	patients	881:888	arg1	rate					873:876	the low survival rate	856:876	the low survival rate of patients and high metastatic potential	856:918	RESULTS High expression of TRPM7 channel correlates well with the low survival rate of patients and high metastatic potential.
32684624	8	56	theme	first	1226:1230	arg1	time					1232:1235	the first time	1222:1235	the first time	1222:1235	We reveal for the first time that caveolin-1 and c-Myc are favourable molecular targets of TRPM7/O-GlcNAc that regulates NSCLC motility.
32684624	3	57	theme	cell	597:600	arg1	NSCLC					615:619	NSCLC	615:619	NSCLC	615:619	METHODS Bioinformatics database analyses were employed to assess correlations between calcium influx channels and clinical outcomes in non-small cell lung cancer (NSCLC).
32684624	3	57	theme	cell	597:600	arg1	cancer					607:612	non-small cell lung cancer	587:612	non-small cell lung cancer (NSCLC)	587:620	METHODS Bioinformatics database analyses were employed to assess correlations between calcium influx channels and clinical outcomes in non-small cell lung cancer (NSCLC).
32684624	6	58	theme	cell	983:986	arg1	lines					988:992	various NSCLC cell lines	969:992	various NSCLC cell lines	969:992	Inhibition of TRPM7 suppresses cell motility in various NSCLC cell lines and patient-derived primary cells and attenuates experimental lung metastases.
32684624	4	59	theme	regulatory	638:647	arg1	roles					649:653	Functional and regulatory roles	623:653	Functional and regulatory roles of influx channels in cell migration and invasion	623:703	Functional and regulatory roles of influx channels in cell migration and invasion were conducted and experimental lung metastasis was examined using in vivo live imaging.
32684624	5	60	theme	low	860:862	arg1	rate					873:876	the low survival rate	856:876	the low survival rate of patients and high metastatic potential	856:918	RESULTS High expression of TRPM7 channel correlates well with the low survival rate of patients and high metastatic potential.
32684624	6	61	theme	various	969:975	arg1	lines					988:992	various NSCLC cell lines	969:992	various NSCLC cell lines	969:992	Inhibition of TRPM7 suppresses cell motility in various NSCLC cell lines and patient-derived primary cells and attenuates experimental lung metastases.
32684624	8	62	theme	NSCLC	1329:1333	arg1	motility					1335:1342	NSCLC motility	1329:1342	NSCLC motility	1329:1342	We reveal for the first time that caveolin-1 and c-Myc are favourable molecular targets of TRPM7/O-GlcNAc that regulates NSCLC motility.
32684624	3	63	theme	lung	602:605	arg1	NSCLC					615:619	NSCLC	615:619	NSCLC	615:619	METHODS Bioinformatics database analyses were employed to assess correlations between calcium influx channels and clinical outcomes in non-small cell lung cancer (NSCLC).
32684624	3	63	theme	lung	602:605	arg1	cancer					607:612	non-small cell lung cancer	587:612	non-small cell lung cancer (NSCLC)	587:620	METHODS Bioinformatics database analyses were employed to assess correlations between calcium influx channels and clinical outcomes in non-small cell lung cancer (NSCLC).
32684624	4	64	dep	in	772:773	arg1	vivo					775:778	vivo	775:778	vivo	775:778	Functional and regulatory roles of influx channels in cell migration and invasion were conducted and experimental lung metastasis was examined using in vivo live imaging.
32684624	3	65	from	outcomes	575:582	arg1	NSCLC					615:619	NSCLC	615:619	NSCLC	615:619	METHODS Bioinformatics database analyses were employed to assess correlations between calcium influx channels and clinical outcomes in non-small cell lung cancer (NSCLC).
32684624	3	65	from	outcomes	575:582	arg1	cancer					607:612	non-small cell lung cancer	587:612	non-small cell lung cancer (NSCLC)	587:620	METHODS Bioinformatics database analyses were employed to assess correlations between calcium influx channels and clinical outcomes in non-small cell lung cancer (NSCLC).
32684624	4	66	theme	lung	737:740	arg1	metastasis					742:751	experimental lung metastasis	724:751	experimental lung metastasis	724:751	Functional and regulatory roles of influx channels in cell migration and invasion were conducted and experimental lung metastasis was examined using in vivo live imaging.
32684624	5	67	theme	high	894:897	arg1	potential					910:918	high metastatic potential	894:918	high metastatic potential	894:918	RESULTS High expression of TRPM7 channel correlates well with the low survival rate of patients and high metastatic potential.
32684624	6	68	theme	experimental	1043:1054	arg1	metastases					1061:1070	experimental lung metastases	1043:1070	experimental lung metastases	1043:1070	Inhibition of TRPM7 suppresses cell motility in various NSCLC cell lines and patient-derived primary cells and attenuates experimental lung metastases.
32684624	5	69	theme	potential	910:918	arg1	rate					873:876	the low survival rate	856:876	the low survival rate of patients and high metastatic potential	856:918	RESULTS High expression of TRPM7 channel correlates well with the low survival rate of patients and high metastatic potential.
32684624	0	70	theme	lung	112:115	arg1	carcinoma					117:125	lung carcinoma	112:125	lung carcinoma	112:125	A novel TRPM7/O-GlcNAc axis mediates tumour cell motility and metastasis by stabilising c-Myc and caveolin-1 in lung carcinoma.
32684624	9	71	theme	caveolin-1	1364:1373	arg1	O-GlcNAcylation					1345:1359	O-GlcNAcylation	1345:1359	O-GlcNAcylation of caveolin-1 and c-Myc	1345:1383	O-GlcNAcylation of caveolin-1 and c-Myc promotes protein stability by interfering with their ubiquitination and proteasomal degradation.
32684624	6	72	theme	primary	1014:1020	arg1	cells					1022:1026	patient-derived primary cells	998:1026	patient-derived primary cells	998:1026	Inhibition of TRPM7 suppresses cell motility in various NSCLC cell lines and patient-derived primary cells and attenuates experimental lung metastases.
32684624	10	73	theme	novel	1537:1541	arg1	target					1543:1548	a potential novel target	1525:1548	a potential novel target for lung cancer therapy that may overcome metastasis	1525:1601	CONCLUSIONS TRPM7/O-GlcNAc axis represents a potential novel target for lung cancer therapy that may overcome metastasis.
32684624	9	74	theme	c-Myc	1379:1383	arg1	O-GlcNAcylation					1345:1359	O-GlcNAcylation	1345:1359	O-GlcNAcylation of caveolin-1 and c-Myc	1345:1383	O-GlcNAcylation of caveolin-1 and c-Myc promotes protein stability by interfering with their ubiquitination and proteasomal degradation.
32684624	2	75	theme	calcium	374:380	arg1	signalling					382:391	calcium signalling	374:391	calcium signalling	374:391	Cell motility is a prerequisite for metastasis, the major cause of lung cancer death, yet its association with calcium signalling and underlying regulatory axis remains an unexplored area.
32684624	5	76	theme	TRPM7	821:825	arg1	channel					827:833	TRPM7 channel	821:833	TRPM7 channel	821:833	RESULTS High expression of TRPM7 channel correlates well with the low survival rate of patients and high metastatic potential.
32684624	9	77	theme	protein	1394:1400	arg1	stability					1402:1410	protein stability	1394:1410	protein stability	1394:1410	O-GlcNAcylation of caveolin-1 and c-Myc promotes protein stability by interfering with their ubiquitination and proteasomal degradation.
32684624	2	78	theme	unexplored	435:444	arg1	area					446:449	an unexplored area	432:449	an unexplored area	432:449	Cell motility is a prerequisite for metastasis, the major cause of lung cancer death, yet its association with calcium signalling and underlying regulatory axis remains an unexplored area.
32684624	10	79	theme	cancer	1559:1564	arg1	therapy					1566:1572	lung cancer therapy	1554:1572	lung cancer therapy	1554:1572	CONCLUSIONS TRPM7/O-GlcNAc axis represents a potential novel target for lung cancer therapy that may overcome metastasis.
32684624	3	80	theme	database	475:482	arg1	analyses					484:491	METHODS Bioinformatics database analyses	452:491	METHODS Bioinformatics database analyses	452:491	METHODS Bioinformatics database analyses were employed to assess correlations between calcium influx channels and clinical outcomes in non-small cell lung cancer (NSCLC).
32684624	0	81	theme	tumour	37:42	arg1	motility					49:56	tumour cell motility	37:56	tumour cell motility	37:56	A novel TRPM7/O-GlcNAc axis mediates tumour cell motility and metastasis by stabilising c-Myc and caveolin-1 in lung carcinoma.
32684624	3	82	theme	METHODS	452:458	arg1	analyses					484:491	METHODS Bioinformatics database analyses	452:491	METHODS Bioinformatics database analyses	452:491	METHODS Bioinformatics database analyses were employed to assess correlations between calcium influx channels and clinical outcomes in non-small cell lung cancer (NSCLC).
32684624	2	83	theme	lung	330:333	arg1	death					342:346	lung cancer death	330:346	lung cancer death	330:346	Cell motility is a prerequisite for metastasis, the major cause of lung cancer death, yet its association with calcium signalling and underlying regulatory axis remains an unexplored area.
32684624	9	84	theme	proteasomal	1457:1467	arg1	degradation					1469:1479	proteasomal degradation	1457:1479	proteasomal degradation	1457:1479	O-GlcNAcylation of caveolin-1 and c-Myc promotes protein stability by interfering with their ubiquitination and proteasomal degradation.
32684624	3	85	theme	calcium	538:544	arg1	channels					553:560	calcium influx channels	538:560	calcium influx channels	538:560	METHODS Bioinformatics database analyses were employed to assess correlations between calcium influx channels and clinical outcomes in non-small cell lung cancer (NSCLC).
32684624	0	86	theme	novel	2:6	arg1	axis					23:26	A novel TRPM7/O-GlcNAc axis	0:26	A novel TRPM7/O-GlcNAc axis	0:26	A novel TRPM7/O-GlcNAc axis mediates tumour cell motility and metastasis by stabilising c-Myc and caveolin-1 in lung carcinoma.
32684624	1	87	theme	several	246:252	arg1	cancers					254:260	several cancers	246:260	several cancers	246:260	BACKGROUND Calcium is an essential signal transduction element that has been associated with aggressive behaviours in several cancers.
20668475	6	0	theme	CLL	961:963	arg1	cells					965:969	CLL cells	961:969	CLL cells	961:969	Indolent and aggressive clinical behavior of CLL cells were found to correlate with higher and lower O-GlcNAc levels, respectively.
20668475	4	1	theme	pathway	722:728	arg1	substrates					730:739	hexosamine pathway substrates	711:739	hexosamine pathway substrates	711:739	O-GlcNAcylation in CLL cells increased following activation with cytokines and through toll-like receptors (TLRs), or after loading with hexosamine pathway substrates.
20668475	3	2	theme	proteins	534:541	arg1	levels					509:514	high levels	504:514	high levels of O-GlcNAcylated proteins, including p53, c-myc and Akt	504:571	In contrast to normal circulating and tonsillar B cells, CLL cells expressed high levels of O-GlcNAcylated proteins, including p53, c-myc and Akt.
20668475	5	3	theme	impaired	802:809	arg1	responses					821:829	impaired signaling responses	802:829	impaired signaling responses to TLR agonists, chemotherapeutic agents, B cell receptor crosslinking and mitogens	802:913	However, high baseline O-GlcNAc levels were associated with impaired signaling responses to TLR agonists, chemotherapeutic agents, B cell receptor crosslinking and mitogens.
20668475	7	4	theme	therapeutic	1179:1189	arg1	implications					1191:1202	therapeutic implications	1179:1202	therapeutic implications	1179:1202	These findings suggest that intracellular O-GlcNAcylation is associated with the pathogenesis of CLL, which could potentially have therapeutic implications.
20668475	4	5	theme	hexosamine	711:720	arg1	substrates					730:739	hexosamine pathway substrates	711:739	hexosamine pathway substrates	711:739	O-GlcNAcylation in CLL cells increased following activation with cytokines and through toll-like receptors (TLRs), or after loading with hexosamine pathway substrates.
20668475	5	6	theme	high	751:754	arg1	levels					774:779	high baseline O-GlcNAc levels	751:779	high baseline O-GlcNAc levels	751:779	However, high baseline O-GlcNAc levels were associated with impaired signaling responses to TLR agonists, chemotherapeutic agents, B cell receptor crosslinking and mitogens.
20668475	2	7	theme	lymphocytic	333:343	arg1	CLL					355:357	CLL	355:357	CLL	355:357	As aberrant responses to microenvironmental signals are a feature of chronic lymphocytic leukemia (CLL), O-GlcNAcylated protein levels were measured in primary CLL cells.
20668475	2	7	theme	lymphocytic	333:343	arg1	leukemia					345:352	chronic lymphocytic leukemia	325:352	chronic lymphocytic leukemia (CLL)	325:358	As aberrant responses to microenvironmental signals are a feature of chronic lymphocytic leukemia (CLL), O-GlcNAcylated protein levels were measured in primary CLL cells.
20668475	7	8	contain	have	1174:1177	arg2	implications					1191:1202	therapeutic implications	1179:1202	therapeutic implications	1179:1202	These findings suggest that intracellular O-GlcNAcylation is associated with the pathogenesis of CLL, which could potentially have therapeutic implications.
20668475	7	8	contain	have	1174:1177	arg1	pathogenesis					1129:1140	the pathogenesis	1125:1140	the pathogenesis	1125:1140	These findings suggest that intracellular O-GlcNAcylation is associated with the pathogenesis of CLL, which could potentially have therapeutic implications.
20668475	5	9	theme	baseline	756:763	arg1	levels					774:779	high baseline O-GlcNAc levels	751:779	high baseline O-GlcNAc levels	751:779	However, high baseline O-GlcNAc levels were associated with impaired signaling responses to TLR agonists, chemotherapeutic agents, B cell receptor crosslinking and mitogens.
20668475	6	10	theme	clinical	940:947	arg1	behavior					949:956	aggressive clinical behavior	929:956	aggressive clinical behavior	929:956	Indolent and aggressive clinical behavior of CLL cells were found to correlate with higher and lower O-GlcNAc levels, respectively.
20668475	2	11	theme	chronic	325:331	arg1	CLL					355:357	CLL	355:357	CLL	355:357	As aberrant responses to microenvironmental signals are a feature of chronic lymphocytic leukemia (CLL), O-GlcNAcylated protein levels were measured in primary CLL cells.
20668475	2	11	theme	chronic	325:331	arg1	leukemia					345:352	chronic lymphocytic leukemia	325:352	chronic lymphocytic leukemia (CLL)	325:358	As aberrant responses to microenvironmental signals are a feature of chronic lymphocytic leukemia (CLL), O-GlcNAcylated protein levels were measured in primary CLL cells.
20668475	6	12	theme	O-GlcNAc	1017:1024	arg1	levels					1026:1031	higher and lower O-GlcNAc levels	1000:1031	higher and lower O-GlcNAc levels	1000:1031	Indolent and aggressive clinical behavior of CLL cells were found to correlate with higher and lower O-GlcNAc levels, respectively.
20668475	5	13	theme	O-GlcNAc	765:772	arg1	levels					774:779	high baseline O-GlcNAc levels	751:779	high baseline O-GlcNAc levels	751:779	However, high baseline O-GlcNAc levels were associated with impaired signaling responses to TLR agonists, chemotherapeutic agents, B cell receptor crosslinking and mitogens.
20668475	6	14	theme	aggressive	929:938	arg1	behavior					949:956	aggressive clinical behavior	929:956	aggressive clinical behavior	929:956	Indolent and aggressive clinical behavior of CLL cells were found to correlate with higher and lower O-GlcNAc levels, respectively.
20668475	5	15	theme	B	873:873	arg1	crosslinking					889:900	B cell receptor crosslinking	873:900	B cell receptor crosslinking	873:900	However, high baseline O-GlcNAc levels were associated with impaired signaling responses to TLR agonists, chemotherapeutic agents, B cell receptor crosslinking and mitogens.
20668475	4	16	theme	toll-like	661:669	arg1	TLRs					682:685	TLRs	682:685	TLRs	682:685	O-GlcNAcylation in CLL cells increased following activation with cytokines and through toll-like receptors (TLRs), or after loading with hexosamine pathway substrates.
20668475	4	16	theme	toll-like	661:669	arg1	receptors					671:679	toll-like receptors	661:679	toll-like receptors (TLRs)	661:686	O-GlcNAcylation in CLL cells increased following activation with cytokines and through toll-like receptors (TLRs), or after loading with hexosamine pathway substrates.
20668475	3	17	theme	B	475:475	arg1	cells					477:481	normal circulating and tonsillar B cells	442:481	normal circulating and tonsillar B cells	442:481	In contrast to normal circulating and tonsillar B cells, CLL cells expressed high levels of O-GlcNAcylated proteins, including p53, c-myc and Akt.
20668475	5	18	theme	signaling	811:819	arg1	responses					821:829	impaired signaling responses	802:829	impaired signaling responses to TLR agonists, chemotherapeutic agents, B cell receptor crosslinking and mitogens	802:913	However, high baseline O-GlcNAc levels were associated with impaired signaling responses to TLR agonists, chemotherapeutic agents, B cell receptor crosslinking and mitogens.
20668475	0	19	theme	Aberrant	0:7	arg1	O-GlcNAcylation					9:23	Aberrant O-GlcNAcylation	0:23	Aberrant O-GlcNAcylation	0:23	Aberrant O-GlcNAcylation characterizes chronic lymphocytic leukemia.
20668475	4	20	with	loading	698:704	arg1	substrates					730:739	hexosamine pathway substrates	711:739	hexosamine pathway substrates	711:739	O-GlcNAcylation in CLL cells increased following activation with cytokines and through toll-like receptors (TLRs), or after loading with hexosamine pathway substrates.
20668475	1	21	theme	post-translational	109:126	arg1	modifications					128:140	O-linked N-Acetylglucosamine (O-GlcNAc) post-translational modifications	69:140	O-linked N-Acetylglucosamine (O-GlcNAc) post-translational modifications	69:140	O-linked N-Acetylglucosamine (O-GlcNAc) post-translational modifications originate from the activity of the hexosamine pathway, and are known to affect intracellular signaling processes.
20668475	6	22	theme	higher	1000:1005	arg1	levels					1026:1031	higher and lower O-GlcNAc levels	1000:1031	higher and lower O-GlcNAc levels	1000:1031	Indolent and aggressive clinical behavior of CLL cells were found to correlate with higher and lower O-GlcNAc levels, respectively.
20668475	1	23	link	O-linked	69:76	arg1	O-GlcNAc					99:106	O-GlcNAc	99:106	O-GlcNAc	99:106	O-linked N-Acetylglucosamine (O-GlcNAc) post-translational modifications originate from the activity of the hexosamine pathway, and are known to affect intracellular signaling processes.
20668475	1	23	link	O-linked	69:76	arg1	N-Acetylglucosamine					78:96	O-linked N-Acetylglucosamine	69:96	O-linked N-Acetylglucosamine (O-GlcNAc) post-translational modifications	69:140	O-linked N-Acetylglucosamine (O-GlcNAc) post-translational modifications originate from the activity of the hexosamine pathway, and are known to affect intracellular signaling processes.
20668475	6	24	theme	lower	1011:1015	arg1	levels					1026:1031	higher and lower O-GlcNAc levels	1000:1031	higher and lower O-GlcNAc levels	1000:1031	Indolent and aggressive clinical behavior of CLL cells were found to correlate with higher and lower O-GlcNAc levels, respectively.
20668475	7	25	theme	CLL	1145:1147	arg1	pathogenesis					1129:1140	the pathogenesis	1125:1140	the pathogenesis	1125:1140	These findings suggest that intracellular O-GlcNAcylation is associated with the pathogenesis of CLL, which could potentially have therapeutic implications.
20668475	2	26	theme	CLL	416:418	arg1	cells					420:424	primary CLL cells	408:424	primary CLL cells	408:424	As aberrant responses to microenvironmental signals are a feature of chronic lymphocytic leukemia (CLL), O-GlcNAcylated protein levels were measured in primary CLL cells.
20668475	0	27	theme	chronic	39:45	arg1	leukemia					59:66	chronic lymphocytic leukemia	39:66	chronic lymphocytic leukemia	39:66	Aberrant O-GlcNAcylation characterizes chronic lymphocytic leukemia.
20668475	5	28	theme	chemotherapeutic	848:863	arg1	agents					865:870	chemotherapeutic agents	848:870	chemotherapeutic agents	848:870	However, high baseline O-GlcNAc levels were associated with impaired signaling responses to TLR agonists, chemotherapeutic agents, B cell receptor crosslinking and mitogens.
20668475	1	29	theme	intracellular	221:233	arg1	processes					245:253	intracellular signaling processes	221:253	intracellular signaling processes	221:253	O-linked N-Acetylglucosamine (O-GlcNAc) post-translational modifications originate from the activity of the hexosamine pathway, and are known to affect intracellular signaling processes.
20668475	4	30	theme	CLL	593:595	arg1	cells					597:601	CLL cells	593:601	CLL cells	593:601	O-GlcNAcylation in CLL cells increased following activation with cytokines and through toll-like receptors (TLRs), or after loading with hexosamine pathway substrates.
20668475	2	31	theme	leukemia	345:352	arg1	responses					268:276	aberrant responses	259:276	aberrant responses to microenvironmental signals	259:306	As aberrant responses to microenvironmental signals are a feature of chronic lymphocytic leukemia (CLL), O-GlcNAcylated protein levels were measured in primary CLL cells.
20668475	2	31	theme	leukemia	345:352	arg1	feature					314:320	a feature	312:320	a feature of chronic lymphocytic leukemia (CLL)	312:358	As aberrant responses to microenvironmental signals are a feature of chronic lymphocytic leukemia (CLL), O-GlcNAcylated protein levels were measured in primary CLL cells.
20668475	1	32	theme	signaling	235:243	arg1	processes					245:253	intracellular signaling processes	221:253	intracellular signaling processes	221:253	O-linked N-Acetylglucosamine (O-GlcNAc) post-translational modifications originate from the activity of the hexosamine pathway, and are known to affect intracellular signaling processes.
20668475	3	33	theme	normal	442:447	arg1	cells					477:481	normal circulating and tonsillar B cells	442:481	normal circulating and tonsillar B cells	442:481	In contrast to normal circulating and tonsillar B cells, CLL cells expressed high levels of O-GlcNAcylated proteins, including p53, c-myc and Akt.
20668475	3	34	theme	O-GlcNAcylated	519:532	arg1	Akt					569:571	Akt	569:571	Akt	569:571	In contrast to normal circulating and tonsillar B cells, CLL cells expressed high levels of O-GlcNAcylated proteins, including p53, c-myc and Akt.
20668475	3	34	theme	O-GlcNAcylated	519:532	arg1	c-myc					559:563	c-myc	559:563	c-myc	559:563	In contrast to normal circulating and tonsillar B cells, CLL cells expressed high levels of O-GlcNAcylated proteins, including p53, c-myc and Akt.
20668475	3	34	theme	O-GlcNAcylated	519:532	arg1	proteins					534:541	O-GlcNAcylated proteins	519:541	O-GlcNAcylated proteins	519:541	In contrast to normal circulating and tonsillar B cells, CLL cells expressed high levels of O-GlcNAcylated proteins, including p53, c-myc and Akt.
20668475	3	34	theme	O-GlcNAcylated	519:532	arg1	p53					554:556	p53	554:556	p53	554:556	In contrast to normal circulating and tonsillar B cells, CLL cells expressed high levels of O-GlcNAcylated proteins, including p53, c-myc and Akt.
20668475	3	35	theme	tonsillar	465:473	arg1	cells					477:481	normal circulating and tonsillar B cells	442:481	normal circulating and tonsillar B cells	442:481	In contrast to normal circulating and tonsillar B cells, CLL cells expressed high levels of O-GlcNAcylated proteins, including p53, c-myc and Akt.
20668475	5	36	theme	cell	875:878	arg1	crosslinking					889:900	B cell receptor crosslinking	873:900	B cell receptor crosslinking	873:900	However, high baseline O-GlcNAc levels were associated with impaired signaling responses to TLR agonists, chemotherapeutic agents, B cell receptor crosslinking and mitogens.
20668475	0	37	theme	lymphocytic	47:57	arg1	leukemia					59:66	chronic lymphocytic leukemia	39:66	chronic lymphocytic leukemia	39:66	Aberrant O-GlcNAcylation characterizes chronic lymphocytic leukemia.
20668475	3	38	theme	circulating	449:459	arg1	cells					477:481	normal circulating and tonsillar B cells	442:481	normal circulating and tonsillar B cells	442:481	In contrast to normal circulating and tonsillar B cells, CLL cells expressed high levels of O-GlcNAcylated proteins, including p53, c-myc and Akt.
20668475	4	39	from	O-GlcNAcylation	574:588	arg1	cells					597:601	CLL cells	593:601	CLL cells	593:601	O-GlcNAcylation in CLL cells increased following activation with cytokines and through toll-like receptors (TLRs), or after loading with hexosamine pathway substrates.
20668475	3	40	theme	CLL	484:486	arg1	cells					488:492	CLL cells	484:492	CLL cells	484:492	In contrast to normal circulating and tonsillar B cells, CLL cells expressed high levels of O-GlcNAcylated proteins, including p53, c-myc and Akt.
20668475	2	41	theme	aberrant	259:266	arg1	responses					268:276	aberrant responses	259:276	aberrant responses to microenvironmental signals	259:306	As aberrant responses to microenvironmental signals are a feature of chronic lymphocytic leukemia (CLL), O-GlcNAcylated protein levels were measured in primary CLL cells.
20668475	2	41	theme	aberrant	259:266	arg1	feature					314:320	a feature	312:320	a feature of chronic lymphocytic leukemia (CLL)	312:358	As aberrant responses to microenvironmental signals are a feature of chronic lymphocytic leukemia (CLL), O-GlcNAcylated protein levels were measured in primary CLL cells.
20668475	5	42	theme	TLR	834:836	arg1	agonists					838:845	TLR agonists	834:845	TLR agonists	834:845	However, high baseline O-GlcNAc levels were associated with impaired signaling responses to TLR agonists, chemotherapeutic agents, B cell receptor crosslinking and mitogens.
20668475	3	43	dep	cells	477:481	arg1	contrast					430:437	contrast	430:437	contrast	430:437	In contrast to normal circulating and tonsillar B cells, CLL cells expressed high levels of O-GlcNAcylated proteins, including p53, c-myc and Akt.
20668475	2	44	theme	protein	376:382	arg1	levels					384:389	O-GlcNAcylated protein levels	361:389	O-GlcNAcylated protein levels	361:389	As aberrant responses to microenvironmental signals are a feature of chronic lymphocytic leukemia (CLL), O-GlcNAcylated protein levels were measured in primary CLL cells.
20668475	1	45	theme	O-linked	69:76	arg1	O-GlcNAc					99:106	O-GlcNAc	99:106	O-GlcNAc	99:106	O-linked N-Acetylglucosamine (O-GlcNAc) post-translational modifications originate from the activity of the hexosamine pathway, and are known to affect intracellular signaling processes.
20668475	1	45	theme	O-linked	69:76	arg1	N-Acetylglucosamine					78:96	O-linked N-Acetylglucosamine	69:96	O-linked N-Acetylglucosamine (O-GlcNAc) post-translational modifications	69:140	O-linked N-Acetylglucosamine (O-GlcNAc) post-translational modifications originate from the activity of the hexosamine pathway, and are known to affect intracellular signaling processes.
20668475	1	46	theme	hexosamine	177:186	arg1	pathway					188:194	the hexosamine pathway	173:194	the hexosamine pathway	173:194	O-linked N-Acetylglucosamine (O-GlcNAc) post-translational modifications originate from the activity of the hexosamine pathway, and are known to affect intracellular signaling processes.
20668475	4	47	with	activation	623:632	arg1	cytokines					639:647	cytokines	639:647	cytokines	639:647	O-GlcNAcylation in CLL cells increased following activation with cytokines and through toll-like receptors (TLRs), or after loading with hexosamine pathway substrates.
20668475	2	48	theme	O-GlcNAcylated	361:374	arg1	levels					384:389	O-GlcNAcylated protein levels	361:389	O-GlcNAcylated protein levels	361:389	As aberrant responses to microenvironmental signals are a feature of chronic lymphocytic leukemia (CLL), O-GlcNAcylated protein levels were measured in primary CLL cells.
20668475	7	49	theme	intracellular	1076:1088	arg1	O-GlcNAcylation					1090:1104	intracellular O-GlcNAcylation	1076:1104	intracellular O-GlcNAcylation	1076:1104	These findings suggest that intracellular O-GlcNAcylation is associated with the pathogenesis of CLL, which could potentially have therapeutic implications.
20668475	1	50	theme	N-Acetylglucosamine	78:96	arg1	modifications					128:140	O-linked N-Acetylglucosamine (O-GlcNAc) post-translational modifications	69:140	O-linked N-Acetylglucosamine (O-GlcNAc) post-translational modifications	69:140	O-linked N-Acetylglucosamine (O-GlcNAc) post-translational modifications originate from the activity of the hexosamine pathway, and are known to affect intracellular signaling processes.
20668475	3	51	theme	high	504:507	arg1	levels					509:514	high levels	504:514	high levels of O-GlcNAcylated proteins, including p53, c-myc and Akt	504:571	In contrast to normal circulating and tonsillar B cells, CLL cells expressed high levels of O-GlcNAcylated proteins, including p53, c-myc and Akt.
20668475	5	52	theme	receptor	880:887	arg1	crosslinking					889:900	B cell receptor crosslinking	873:900	B cell receptor crosslinking	873:900	However, high baseline O-GlcNAc levels were associated with impaired signaling responses to TLR agonists, chemotherapeutic agents, B cell receptor crosslinking and mitogens.
20668475	2	53	theme	primary	408:414	arg1	cells					420:424	primary CLL cells	408:424	primary CLL cells	408:424	As aberrant responses to microenvironmental signals are a feature of chronic lymphocytic leukemia (CLL), O-GlcNAcylated protein levels were measured in primary CLL cells.
20668475	6	54	theme	cells	965:969	arg1	Indolent					916:923	Indolent	916:923	Indolent	916:923	Indolent and aggressive clinical behavior of CLL cells were found to correlate with higher and lower O-GlcNAc levels, respectively.
20668475	6	54	theme	cells	965:969	arg1	behavior					949:956	aggressive clinical behavior	929:956	aggressive clinical behavior	929:956	Indolent and aggressive clinical behavior of CLL cells were found to correlate with higher and lower O-GlcNAc levels, respectively.
20668475	2	55	theme	microenvironmental	281:298	arg1	signals					300:306	microenvironmental signals	281:306	microenvironmental signals	281:306	As aberrant responses to microenvironmental signals are a feature of chronic lymphocytic leukemia (CLL), O-GlcNAcylated protein levels were measured in primary CLL cells.
20668475	1	56	theme	pathway	188:194	arg1	activity					161:168	the activity	157:168	the activity of the hexosamine pathway	157:194	O-linked N-Acetylglucosamine (O-GlcNAc) post-translational modifications originate from the activity of the hexosamine pathway, and are known to affect intracellular signaling processes.
33723378	7	0	theme	other	1256:1260	arg1	areas					1262:1266	potentially other areas	1244:1266	potentially other areas of sHSP biology	1244:1282	Our results have important implications for neurodegenerative diseases associated with amyloid formation and potentially other areas of sHSP biology.
33723378	7	1	theme	biology	1276:1282	arg1	areas					1262:1266	potentially other areas	1244:1266	potentially other areas of sHSP biology	1244:1282	Our results have important implications for neurodegenerative diseases associated with amyloid formation and potentially other areas of sHSP biology.
33723378	7	1	theme	biology	1276:1282	arg1	formation					1230:1238	amyloid formation	1222:1238	amyloid formation	1222:1238	Our results have important implications for neurodegenerative diseases associated with amyloid formation and potentially other areas of sHSP biology.
33723378	6	2	theme	sHSPs	1002:1006	arg1	modification					977:988	the modification	973:988	the modification of relevant sHSPs	973:1006	Finally, we found that, although O-GlcNAc levels are globally reduced in Alzheimer's disease brains, the modification of relevant sHSPs is either maintained or increased, which suggests a mechanism to maintain these potentially protective O-GlcNAc modifications.
33723378	0	3	theme	chaperone	79:87	arg1	activity					89:96	their anti-amyloid chaperone activity	60:96	their anti-amyloid chaperone activity	60:96	O-GlcNAc modification of small heat shock proteins enhances their anti-amyloid chaperone activity.
33723378	3	4	theme	important	520:528	arg1	proteins					483:490	certain small heat shock proteins	458:490	certain small heat shock proteins (sHSPs)	458:498	Here we used synthetic protein chemistry to discover that O-GlcNAc also activates the anti-amyloid activity of certain small heat shock proteins (sHSPs), a potentially more important modification event that can act broadly and substoichiometrically.
33723378	3	4	theme	important	520:528	arg1	event					543:547	a potentially more important modification event	501:547	a potentially more important modification event that can act broadly and substoichiometrically	501:594	Here we used synthetic protein chemistry to discover that O-GlcNAc also activates the anti-amyloid activity of certain small heat shock proteins (sHSPs), a potentially more important modification event that can act broadly and substoichiometrically.
33723378	6	5	theme	relevant	993:1000	arg1	sHSPs					1002:1006	relevant sHSPs	993:1006	relevant sHSPs	993:1006	Finally, we found that, although O-GlcNAc levels are globally reduced in Alzheimer's disease brains, the modification of relevant sHSPs is either maintained or increased, which suggests a mechanism to maintain these potentially protective O-GlcNAc modifications.
33723378	6	6	theme	O-GlcNAc	905:912	arg1	levels					914:919	O-GlcNAc levels	905:919	O-GlcNAc levels	905:919	Finally, we found that, although O-GlcNAc levels are globally reduced in Alzheimer's disease brains, the modification of relevant sHSPs is either maintained or increased, which suggests a mechanism to maintain these potentially protective O-GlcNAc modifications.
33723378	3	7	used	used	355:358	arg2	we					352:353	we	352:353	we	352:353	Here we used synthetic protein chemistry to discover that O-GlcNAc also activates the anti-amyloid activity of certain small heat shock proteins (sHSPs), a potentially more important modification event that can act broadly and substoichiometrically.
33723378	3	8	theme	modification	530:541	arg1	proteins					483:490	certain small heat shock proteins	458:490	certain small heat shock proteins (sHSPs)	458:498	Here we used synthetic protein chemistry to discover that O-GlcNAc also activates the anti-amyloid activity of certain small heat shock proteins (sHSPs), a potentially more important modification event that can act broadly and substoichiometrically.
33723378	3	8	theme	modification	530:541	arg1	event					543:547	a potentially more important modification event	501:547	a potentially more important modification event that can act broadly and substoichiometrically	501:594	Here we used synthetic protein chemistry to discover that O-GlcNAc also activates the anti-amyloid activity of certain small heat shock proteins (sHSPs), a potentially more important modification event that can act broadly and substoichiometrically.
33723378	2	9	mod	modification	290:301	arg3	O-GlcNAc					281:288	O-GlcNAc modification	281:301	O-GlcNAc modification of the amyloid-forming proteins themselves	281:344	Most of the previous studies in this area focused on O-GlcNAc modification of the amyloid-forming proteins themselves.
33723378	2	9	mod	modification	290:301	arg1	proteins					326:333	the amyloid-forming proteins	306:333	the amyloid-forming proteins themselves	306:344	Most of the previous studies in this area focused on O-GlcNAc modification of the amyloid-forming proteins themselves.
33723378	3	10	theme	synthetic	360:368	arg1	chemistry					378:386	synthetic protein chemistry	360:386	synthetic protein chemistry	360:386	Here we used synthetic protein chemistry to discover that O-GlcNAc also activates the anti-amyloid activity of certain small heat shock proteins (sHSPs), a potentially more important modification event that can act broadly and substoichiometrically.
33723378	2	11	theme	O-GlcNAc	281:288	arg1	modification					290:301	O-GlcNAc modification	281:301	O-GlcNAc modification of the amyloid-forming proteins themselves	281:344	Most of the previous studies in this area focused on O-GlcNAc modification of the amyloid-forming proteins themselves.
33723378	3	12	theme	small	466:470	arg1	proteins					483:490	certain small heat shock proteins	458:490	certain small heat shock proteins (sHSPs)	458:498	Here we used synthetic protein chemistry to discover that O-GlcNAc also activates the anti-amyloid activity of certain small heat shock proteins (sHSPs), a potentially more important modification event that can act broadly and substoichiometrically.
33723378	3	12	theme	small	466:470	arg1	event					543:547	a potentially more important modification event	501:547	a potentially more important modification event that can act broadly and substoichiometrically	501:594	Here we used synthetic protein chemistry to discover that O-GlcNAc also activates the anti-amyloid activity of certain small heat shock proteins (sHSPs), a potentially more important modification event that can act broadly and substoichiometrically.
33723378	3	12	theme	small	466:470	arg1	sHSPs					493:497	sHSPs	493:497	sHSPs	493:497	Here we used synthetic protein chemistry to discover that O-GlcNAc also activates the anti-amyloid activity of certain small heat shock proteins (sHSPs), a potentially more important modification event that can act broadly and substoichiometrically.
33723378	3	13	theme	protein	370:376	arg1	chemistry					378:386	synthetic protein chemistry	360:386	synthetic protein chemistry	360:386	Here we used synthetic protein chemistry to discover that O-GlcNAc also activates the anti-amyloid activity of certain small heat shock proteins (sHSPs), a potentially more important modification event that can act broadly and substoichiometrically.
33723378	3	14	theme	anti-amyloid	433:444	arg1	activity					446:453	the anti-amyloid activity	429:453	the anti-amyloid activity of certain small heat shock proteins (sHSPs), a potentially more important modification event that can act broadly and substoichiometrically	429:594	Here we used synthetic protein chemistry to discover that O-GlcNAc also activates the anti-amyloid activity of certain small heat shock proteins (sHSPs), a potentially more important modification event that can act broadly and substoichiometrically.
33723378	2	15	from	studies	249:255	arg1	area					265:268	this area	260:268	this area	260:268	Most of the previous studies in this area focused on O-GlcNAc modification of the amyloid-forming proteins themselves.
33723378	3	16	theme	heat	472:475	arg1	proteins					483:490	certain small heat shock proteins	458:490	certain small heat shock proteins (sHSPs)	458:498	Here we used synthetic protein chemistry to discover that O-GlcNAc also activates the anti-amyloid activity of certain small heat shock proteins (sHSPs), a potentially more important modification event that can act broadly and substoichiometrically.
33723378	3	16	theme	heat	472:475	arg1	event					543:547	a potentially more important modification event	501:547	a potentially more important modification event that can act broadly and substoichiometrically	501:594	Here we used synthetic protein chemistry to discover that O-GlcNAc also activates the anti-amyloid activity of certain small heat shock proteins (sHSPs), a potentially more important modification event that can act broadly and substoichiometrically.
33723378	3	16	theme	heat	472:475	arg1	sHSPs					493:497	sHSPs	493:497	sHSPs	493:497	Here we used synthetic protein chemistry to discover that O-GlcNAc also activates the anti-amyloid activity of certain small heat shock proteins (sHSPs), a potentially more important modification event that can act broadly and substoichiometrically.
33723378	0	17	theme	O-GlcNAc	0:7	arg1	modification					9:20	O-GlcNAc modification	0:20	O-GlcNAc modification of small heat shock proteins	0:49	O-GlcNAc modification of small heat shock proteins enhances their anti-amyloid chaperone activity.
33723378	2	18	theme	proteins	326:333	arg1	modification					290:301	O-GlcNAc modification	281:301	O-GlcNAc modification of the amyloid-forming proteins themselves	281:344	Most of the previous studies in this area focused on O-GlcNAc modification of the amyloid-forming proteins themselves.
33723378	3	19	theme	certain	458:464	arg1	proteins					483:490	certain small heat shock proteins	458:490	certain small heat shock proteins (sHSPs)	458:498	Here we used synthetic protein chemistry to discover that O-GlcNAc also activates the anti-amyloid activity of certain small heat shock proteins (sHSPs), a potentially more important modification event that can act broadly and substoichiometrically.
33723378	3	19	theme	certain	458:464	arg1	event					543:547	a potentially more important modification event	501:547	a potentially more important modification event that can act broadly and substoichiometrically	501:594	Here we used synthetic protein chemistry to discover that O-GlcNAc also activates the anti-amyloid activity of certain small heat shock proteins (sHSPs), a potentially more important modification event that can act broadly and substoichiometrically.
33723378	3	19	theme	certain	458:464	arg1	sHSPs					493:497	sHSPs	493:497	sHSPs	493:497	Here we used synthetic protein chemistry to discover that O-GlcNAc also activates the anti-amyloid activity of certain small heat shock proteins (sHSPs), a potentially more important modification event that can act broadly and substoichiometrically.
33723378	0	20	theme	small	25:29	arg1	proteins					42:49	small heat shock proteins	25:49	small heat shock proteins	25:49	O-GlcNAc modification of small heat shock proteins enhances their anti-amyloid chaperone activity.
33723378	2	21	theme	amyloid-forming	310:324	arg1	proteins					326:333	the amyloid-forming proteins	306:333	the amyloid-forming proteins themselves	306:344	Most of the previous studies in this area focused on O-GlcNAc modification of the amyloid-forming proteins themselves.
33723378	1	22	theme	protein	207:213	arg1	aggregation					215:225	protein aggregation	207:225	protein aggregation	207:225	A major role for the intracellular post-translational modification O-GlcNAc appears to be the inhibition of protein aggregation.
33723378	4	23	theme	α-synuclein	709:719	arg1	formation					691:699	the amyloid formation	679:699	the amyloid formation of both α-synuclein and Aβ(1-42)	679:732	More specifically, we found that O-GlcNAc increases the ability of sHSPs to block the amyloid formation of both α-synuclein and Aβ(1-42).
33723378	1	24	theme	aggregation	215:225	arg1	inhibition					193:202	the inhibition	189:202	the inhibition of protein aggregation	189:225	A major role for the intracellular post-translational modification O-GlcNAc appears to be the inhibition of protein aggregation.
33723378	1	24	theme	aggregation	215:225	arg1	role					107:110	A major role	99:110	A major role for the intracellular post-translational modification O-GlcNAc	99:173	A major role for the intracellular post-translational modification O-GlcNAc appears to be the inhibition of protein aggregation.
33723378	0	25	theme	shock	36:40	arg1	proteins					42:49	small heat shock proteins	25:49	small heat shock proteins	25:49	O-GlcNAc modification of small heat shock proteins enhances their anti-amyloid chaperone activity.
33723378	6	26	theme	disease	957:963	arg1	brains					965:970	Alzheimer's disease brains	945:970	Alzheimer's disease brains	945:970	Finally, we found that, although O-GlcNAc levels are globally reduced in Alzheimer's disease brains, the modification of relevant sHSPs is either maintained or increased, which suggests a mechanism to maintain these potentially protective O-GlcNAc modifications.
33723378	5	27	theme	substrate	853:861	arg1	binding					863:869	substrate binding	853:869	substrate binding	853:869	Mechanistically, we show that O-GlcNAc near the sHSP IXI-domain prevents its ability to intramolecularly compete with substrate binding.
33723378	4	28	theme	amyloid	683:689	arg1	formation					691:699	the amyloid formation	679:699	the amyloid formation of both α-synuclein and Aβ(1-42)	679:732	More specifically, we found that O-GlcNAc increases the ability of sHSPs to block the amyloid formation of both α-synuclein and Aβ(1-42).
33723378	3	29	theme	shock	477:481	arg1	proteins					483:490	certain small heat shock proteins	458:490	certain small heat shock proteins (sHSPs)	458:498	Here we used synthetic protein chemistry to discover that O-GlcNAc also activates the anti-amyloid activity of certain small heat shock proteins (sHSPs), a potentially more important modification event that can act broadly and substoichiometrically.
33723378	3	29	theme	shock	477:481	arg1	event					543:547	a potentially more important modification event	501:547	a potentially more important modification event that can act broadly and substoichiometrically	501:594	Here we used synthetic protein chemistry to discover that O-GlcNAc also activates the anti-amyloid activity of certain small heat shock proteins (sHSPs), a potentially more important modification event that can act broadly and substoichiometrically.
33723378	3	29	theme	shock	477:481	arg1	sHSPs					493:497	sHSPs	493:497	sHSPs	493:497	Here we used synthetic protein chemistry to discover that O-GlcNAc also activates the anti-amyloid activity of certain small heat shock proteins (sHSPs), a potentially more important modification event that can act broadly and substoichiometrically.
33723378	0	30	theme	heat	31:34	arg1	proteins					42:49	small heat shock proteins	25:49	small heat shock proteins	25:49	O-GlcNAc modification of small heat shock proteins enhances their anti-amyloid chaperone activity.
33723378	5	31	theme	sHSP	783:786	arg1	IXI-domain					788:797	the sHSP IXI-domain	779:797	the sHSP IXI-domain	779:797	Mechanistically, we show that O-GlcNAc near the sHSP IXI-domain prevents its ability to intramolecularly compete with substrate binding.
33723378	2	32	theme	previous	240:247	arg1	studies					249:255	the previous studies	236:255	the previous studies in this area	236:268	Most of the previous studies in this area focused on O-GlcNAc modification of the amyloid-forming proteins themselves.
33723378	3	33	theme	proteins	483:490	arg1	activity					446:453	the anti-amyloid activity	429:453	the anti-amyloid activity of certain small heat shock proteins (sHSPs), a potentially more important modification event that can act broadly and substoichiometrically	429:594	Here we used synthetic protein chemistry to discover that O-GlcNAc also activates the anti-amyloid activity of certain small heat shock proteins (sHSPs), a potentially more important modification event that can act broadly and substoichiometrically.
33723378	6	34	theme	O-GlcNAc	1111:1118	arg1	modifications					1120:1132	these potentially protective O-GlcNAc modifications	1082:1132	these potentially protective O-GlcNAc modifications	1082:1132	Finally, we found that, although O-GlcNAc levels are globally reduced in Alzheimer's disease brains, the modification of relevant sHSPs is either maintained or increased, which suggests a mechanism to maintain these potentially protective O-GlcNAc modifications.
33723378	0	35	theme	proteins	42:49	arg1	modification					9:20	O-GlcNAc modification	0:20	O-GlcNAc modification of small heat shock proteins	0:49	O-GlcNAc modification of small heat shock proteins enhances their anti-amyloid chaperone activity.
33723378	4	36	theme	Aβ	725:726	arg1	formation					691:699	the amyloid formation	679:699	the amyloid formation of both α-synuclein and Aβ(1-42)	679:732	More specifically, we found that O-GlcNAc increases the ability of sHSPs to block the amyloid formation of both α-synuclein and Aβ(1-42).
33723378	7	37	theme	neurodegenerative	1179:1195	arg1	diseases					1197:1204	neurodegenerative diseases	1179:1204	neurodegenerative diseases associated with amyloid formation and potentially other areas of sHSP biology	1179:1282	Our results have important implications for neurodegenerative diseases associated with amyloid formation and potentially other areas of sHSP biology.
33723378	7	38	theme	important	1152:1160	arg1	implications					1162:1173	important implications	1152:1173	important implications for neurodegenerative diseases associated with amyloid formation and potentially other areas of sHSP biology	1152:1282	Our results have important implications for neurodegenerative diseases associated with amyloid formation and potentially other areas of sHSP biology.
33723378	7	39	contain	have	1147:1150	arg2	implications					1162:1173	important implications	1152:1173	important implications for neurodegenerative diseases associated with amyloid formation and potentially other areas of sHSP biology	1152:1282	Our results have important implications for neurodegenerative diseases associated with amyloid formation and potentially other areas of sHSP biology.
33723378	7	39	contain	have	1147:1150	arg1	results					1139:1145	Our results	1135:1145	Our results	1135:1145	Our results have important implications for neurodegenerative diseases associated with amyloid formation and potentially other areas of sHSP biology.
33723378	1	40	theme	intracellular	120:132	arg1	O-GlcNAc					166:173	the intracellular post-translational modification O-GlcNAc	116:173	the intracellular post-translational modification O-GlcNAc	116:173	A major role for the intracellular post-translational modification O-GlcNAc appears to be the inhibition of protein aggregation.
33723378	1	41	theme	major	101:105	arg1	inhibition					193:202	the inhibition	189:202	the inhibition of protein aggregation	189:225	A major role for the intracellular post-translational modification O-GlcNAc appears to be the inhibition of protein aggregation.
33723378	1	41	theme	major	101:105	arg1	role					107:110	A major role	99:110	A major role for the intracellular post-translational modification O-GlcNAc	99:173	A major role for the intracellular post-translational modification O-GlcNAc appears to be the inhibition of protein aggregation.
33723378	1	42	theme	post-translational	134:151	arg1	O-GlcNAc					166:173	the intracellular post-translational modification O-GlcNAc	116:173	the intracellular post-translational modification O-GlcNAc	116:173	A major role for the intracellular post-translational modification O-GlcNAc appears to be the inhibition of protein aggregation.
33723378	0	43	theme	anti-amyloid	66:77	arg1	activity					89:96	their anti-amyloid chaperone activity	60:96	their anti-amyloid chaperone activity	60:96	O-GlcNAc modification of small heat shock proteins enhances their anti-amyloid chaperone activity.
33723378	4	44	theme	sHSPs	664:668	arg1	ability					653:659	the ability	649:659	the ability of sHSPs to block the amyloid formation of both α-synuclein and Aβ(1-42)	649:732	More specifically, we found that O-GlcNAc increases the ability of sHSPs to block the amyloid formation of both α-synuclein and Aβ(1-42).
33723378	1	45	theme	modification	153:164	arg1	O-GlcNAc					166:173	the intracellular post-translational modification O-GlcNAc	116:173	the intracellular post-translational modification O-GlcNAc	116:173	A major role for the intracellular post-translational modification O-GlcNAc appears to be the inhibition of protein aggregation.
33723378	7	46	theme	sHSP	1271:1274	arg1	biology					1276:1282	sHSP biology	1271:1282	sHSP biology	1271:1282	Our results have important implications for neurodegenerative diseases associated with amyloid formation and potentially other areas of sHSP biology.
33723378	7	47	theme	amyloid	1222:1228	arg1	formation					1230:1238	amyloid formation	1222:1238	amyloid formation	1222:1238	Our results have important implications for neurodegenerative diseases associated with amyloid formation and potentially other areas of sHSP biology.
33723378	6	48	theme	protective	1100:1109	arg1	modifications					1120:1132	these potentially protective O-GlcNAc modifications	1082:1132	these potentially protective O-GlcNAc modifications	1082:1132	Finally, we found that, although O-GlcNAc levels are globally reduced in Alzheimer's disease brains, the modification of relevant sHSPs is either maintained or increased, which suggests a mechanism to maintain these potentially protective O-GlcNAc modifications.
21300897	0	0	theme	salvage	122:128	arg1	pathway					130:136	the N-acetylgalactosamine salvage pathway	96:136	the N-acetylgalactosamine salvage pathway	96:136	Metabolic cross-talk allows labeling of O-linked beta-N-acetylglucosamine-modified proteins via the N-acetylgalactosamine salvage pathway.
21300897	7	1	theme	approaches	1375:1384	arg1	variety					1348:1354	a wide variety	1341:1354	a wide variety of future chemical approaches to identify, visualize, and characterize dynamic O-GlcNAc signaling	1341:1452	Our work provides a blueprint for a wide variety of future chemical approaches to identify, visualize, and characterize dynamic O-GlcNAc signaling.
21300897	7	1	theme	approaches	1375:1384	arg1	approaches					1375:1384	future chemical approaches	1359:1384	future chemical approaches	1359:1384	Our work provides a blueprint for a wide variety of future chemical approaches to identify, visualize, and characterize dynamic O-GlcNAc signaling.
21300897	2	2	theme	signaling	420:428	arg1	nature					401:406	the dynamic and posttranslational nature	367:406	the dynamic and posttranslational nature of O-GlcNAc signaling	367:428	Despite its broad functional significance, the dynamic and posttranslational nature of O-GlcNAc signaling makes it challenging to study using traditional molecular and cell biological techniques alone.
21300897	0	3	theme	N-acetylgalactosamine	100:120	arg1	pathway					130:136	the N-acetylgalactosamine salvage pathway	96:136	the N-acetylgalactosamine salvage pathway	96:136	Metabolic cross-talk allows labeling of O-linked beta-N-acetylglucosamine-modified proteins via the N-acetylgalactosamine salvage pathway.
21300897	2	4	theme	O-GlcNAc	411:418	arg1	signaling					420:428	O-GlcNAc signaling	411:428	O-GlcNAc signaling	411:428	Despite its broad functional significance, the dynamic and posttranslational nature of O-GlcNAc signaling makes it challenging to study using traditional molecular and cell biological techniques alone.
21300897	7	5	theme	future	1359:1364	arg1	approaches					1375:1384	future chemical approaches	1359:1384	future chemical approaches	1359:1384	Our work provides a blueprint for a wide variety of future chemical approaches to identify, visualize, and characterize dynamic O-GlcNAc signaling.
21300897	2	6	theme	functional	342:351	arg1	significance					353:364	its broad functional significance	332:364	its broad functional significance	332:364	Despite its broad functional significance, the dynamic and posttranslational nature of O-GlcNAc signaling makes it challenging to study using traditional molecular and cell biological techniques alone.
21300897	7	7	theme	dynamic	1427:1433	arg1	signaling					1444:1452	dynamic O-GlcNAc signaling	1427:1452	dynamic O-GlcNAc signaling	1427:1452	Our work provides a blueprint for a wide variety of future chemical approaches to identify, visualize, and characterize dynamic O-GlcNAc signaling.
21300897	2	8	theme	broad	336:340	arg1	significance					353:364	its broad functional significance	332:364	its broad functional significance	332:364	Despite its broad functional significance, the dynamic and posttranslational nature of O-GlcNAc signaling makes it challenging to study using traditional molecular and cell biological techniques alone.
21300897	3	9	theme	metabolic	547:555	arg1	cross-talk					557:566	metabolic cross-talk	547:566	metabolic cross-talk between the N-acetylgalactosamine salvage and O-GlcNAcylation pathways	547:637	Here, we report that metabolic cross-talk between the N-acetylgalactosamine salvage and O-GlcNAcylation pathways can be exploited for the tagging and identification of O-GlcNAcylated proteins.
21300897	4	10	theme	biosynthetic	806:817	arg1	enzymes					819:825	endogenous mammalian biosynthetic enzymes	785:825	endogenous mammalian biosynthetic enzymes	785:825	We found that N-azidoacetylgalactosamine (GalNAz) is converted by endogenous mammalian biosynthetic enzymes to UDP-GalNAz and then epimerized to UDP-N-azidoacetylglucosamine (GlcNAz).
21300897	6	11	used	used	1160:1163	arg2	we					1157:1158	we	1157:1158	we	1157:1158	In a proof-of-principle proteomics experiment, we used metabolic GalNAz labeling of human cells and a bioorthogonal chemical probe to affinity-purify and identify numerous O-GlcNAcylated proteins.
21300897	6	12	theme	cells	1200:1204	arg1	probe					1235:1239	a bioorthogonal chemical probe	1210:1239	a bioorthogonal chemical probe	1210:1239	In a proof-of-principle proteomics experiment, we used metabolic GalNAz labeling of human cells and a bioorthogonal chemical probe to affinity-purify and identify numerous O-GlcNAcylated proteins.
21300897	6	12	theme	cells	1200:1204	arg1	labeling					1182:1189	metabolic GalNAz labeling	1165:1189	metabolic GalNAz labeling of human cells	1165:1204	In a proof-of-principle proteomics experiment, we used metabolic GalNAz labeling of human cells and a bioorthogonal chemical probe to affinity-purify and identify numerous O-GlcNAcylated proteins.
21300897	3	13	theme	O-GlcNAcylation	614:628	arg1	pathways					630:637	the N-acetylgalactosamine salvage and O-GlcNAcylation pathways	576:637	pathways	630:637	Here, we report that metabolic cross-talk between the N-acetylgalactosamine salvage and O-GlcNAcylation pathways can be exploited for the tagging and identification of O-GlcNAcylated proteins.
21300897	6	14	theme	proteomics	1134:1143	arg1	experiment					1145:1154	a proof-of-principle proteomics experiment	1113:1154	a proof-of-principle proteomics experiment	1113:1154	In a proof-of-principle proteomics experiment, we used metabolic GalNAz labeling of human cells and a bioorthogonal chemical probe to affinity-purify and identify numerous O-GlcNAcylated proteins.
21300897	6	15	theme	O-GlcNAcylated	1282:1295	arg1	proteins					1297:1304	numerous O-GlcNAcylated proteins	1273:1304	numerous O-GlcNAcylated proteins	1273:1304	In a proof-of-principle proteomics experiment, we used metabolic GalNAz labeling of human cells and a bioorthogonal chemical probe to affinity-purify and identify numerous O-GlcNAcylated proteins.
21300897	5	16	theme	nucleotide-sugar	948:963	arg1	UDP-GlcNAz					932:941	UDP-GlcNAz	932:941	UDP-GlcNAz	932:941	O-GlcNAc transferase accepts UDP-GlcNAz as a nucleotide-sugar donor, appending an azidosugar onto its native substrates, which can then be detected by covalent labeling using azide-reactive chemical probes.
21300897	5	16	theme	nucleotide-sugar	948:963	arg1	donor					965:969	a nucleotide-sugar donor	946:969	a nucleotide-sugar donor	946:969	O-GlcNAc transferase accepts UDP-GlcNAz as a nucleotide-sugar donor, appending an azidosugar onto its native substrates, which can then be detected by covalent labeling using azide-reactive chemical probes.
21300897	1	17	theme	O-linked	225:232	arg1	β-N-acetylglucosamine					234:254	O-linked β-N-acetylglucosamine	225:254	O-linked β-N-acetylglucosamine (O-GlcNAc) to regulate their function, localization, and stability	225:321	Hundreds of mammalian nuclear and cytoplasmic proteins are reversibly glycosylated by O-linked β-N-acetylglucosamine (O-GlcNAc) to regulate their function, localization, and stability.
21300897	1	17	theme	O-linked	225:232	arg1	O-GlcNAc					257:264	O-GlcNAc	257:264	O-GlcNAc	257:264	Hundreds of mammalian nuclear and cytoplasmic proteins are reversibly glycosylated by O-linked β-N-acetylglucosamine (O-GlcNAc) to regulate their function, localization, and stability.
21300897	5	18	theme	O-GlcNAc	903:910	arg1	transferase					912:922	O-GlcNAc transferase	903:922	O-GlcNAc transferase	903:922	O-GlcNAc transferase accepts UDP-GlcNAz as a nucleotide-sugar donor, appending an azidosugar onto its native substrates, which can then be detected by covalent labeling using azide-reactive chemical probes.
21300897	2	19	theme	dynamic	371:377	arg1	nature					401:406	the dynamic and posttranslational nature	367:406	the dynamic and posttranslational nature of O-GlcNAc signaling	367:428	Despite its broad functional significance, the dynamic and posttranslational nature of O-GlcNAc signaling makes it challenging to study using traditional molecular and cell biological techniques alone.
21300897	7	20	theme	O-GlcNAc	1435:1442	arg1	signaling					1444:1452	dynamic O-GlcNAc signaling	1427:1452	dynamic O-GlcNAc signaling	1427:1452	Our work provides a blueprint for a wide variety of future chemical approaches to identify, visualize, and characterize dynamic O-GlcNAc signaling.
21300897	6	21	theme	bioorthogonal	1212:1224	arg1	probe					1235:1239	a bioorthogonal chemical probe	1210:1239	a bioorthogonal chemical probe	1210:1239	In a proof-of-principle proteomics experiment, we used metabolic GalNAz labeling of human cells and a bioorthogonal chemical probe to affinity-purify and identify numerous O-GlcNAcylated proteins.
21300897	0	22	theme	Metabolic	0:8	arg1	cross-talk					10:19	Metabolic cross-talk	0:19	Metabolic cross-talk	0:19	Metabolic cross-talk allows labeling of O-linked beta-N-acetylglucosamine-modified proteins via the N-acetylgalactosamine salvage pathway.
21300897	6	23	theme	proof-of-principle	1115:1132	arg1	experiment					1145:1154	a proof-of-principle proteomics experiment	1113:1154	a proof-of-principle proteomics experiment	1113:1154	In a proof-of-principle proteomics experiment, we used metabolic GalNAz labeling of human cells and a bioorthogonal chemical probe to affinity-purify and identify numerous O-GlcNAcylated proteins.
21300897	1	24	link	O-linked	225:232	arg1	β-N-acetylglucosamine					234:254	O-linked β-N-acetylglucosamine	225:254	O-linked β-N-acetylglucosamine (O-GlcNAc) to regulate their function, localization, and stability	225:321	Hundreds of mammalian nuclear and cytoplasmic proteins are reversibly glycosylated by O-linked β-N-acetylglucosamine (O-GlcNAc) to regulate their function, localization, and stability.
21300897	1	24	link	O-linked	225:232	arg1	O-GlcNAc					257:264	O-GlcNAc	257:264	O-GlcNAc	257:264	Hundreds of mammalian nuclear and cytoplasmic proteins are reversibly glycosylated by O-linked β-N-acetylglucosamine (O-GlcNAc) to regulate their function, localization, and stability.
21300897	0	25	link	O-linked	40:47	arg1	proteins					83:90	O-linked beta-N-acetylglucosamine-modified proteins	40:90	O-linked beta-N-acetylglucosamine-modified proteins	40:90	Metabolic cross-talk allows labeling of O-linked beta-N-acetylglucosamine-modified proteins via the N-acetylgalactosamine salvage pathway.
21300897	5	26	theme	azide-reactive	1078:1091	arg1	probes					1102:1107	azide-reactive chemical probes	1078:1107	azide-reactive chemical probes	1078:1107	O-GlcNAc transferase accepts UDP-GlcNAz as a nucleotide-sugar donor, appending an azidosugar onto its native substrates, which can then be detected by covalent labeling using azide-reactive chemical probes.
21300897	6	27	theme	chemical	1226:1233	arg1	probe					1235:1239	a bioorthogonal chemical probe	1210:1239	a bioorthogonal chemical probe	1210:1239	In a proof-of-principle proteomics experiment, we used metabolic GalNAz labeling of human cells and a bioorthogonal chemical probe to affinity-purify and identify numerous O-GlcNAcylated proteins.
21300897	5	28	theme	chemical	1093:1100	arg1	probes					1102:1107	azide-reactive chemical probes	1078:1107	azide-reactive chemical probes	1078:1107	O-GlcNAc transferase accepts UDP-GlcNAz as a nucleotide-sugar donor, appending an azidosugar onto its native substrates, which can then be detected by covalent labeling using azide-reactive chemical probes.
21300897	2	29	theme	biological	497:506	arg1	techniques					508:517	traditional molecular and cell biological techniques	466:517	traditional molecular and cell biological techniques alone	466:523	Despite its broad functional significance, the dynamic and posttranslational nature of O-GlcNAc signaling makes it challenging to study using traditional molecular and cell biological techniques alone.
21300897	3	30	theme	N-acetylgalactosamine	580:600	arg1	salvage					602:608	the N-acetylgalactosamine salvage and O-GlcNAcylation pathways	576:637	salvage	602:608	Here, we report that metabolic cross-talk between the N-acetylgalactosamine salvage and O-GlcNAcylation pathways can be exploited for the tagging and identification of O-GlcNAcylated proteins.
21300897	3	31	dep	tagging	664:670	arg1	the					660:662	the	660:662	the	660:662	Here, we report that metabolic cross-talk between the N-acetylgalactosamine salvage and O-GlcNAcylation pathways can be exploited for the tagging and identification of O-GlcNAcylated proteins.
21300897	4	32	theme	mammalian	796:804	arg1	enzymes					819:825	endogenous mammalian biosynthetic enzymes	785:825	endogenous mammalian biosynthetic enzymes	785:825	We found that N-azidoacetylgalactosamine (GalNAz) is converted by endogenous mammalian biosynthetic enzymes to UDP-GalNAz and then epimerized to UDP-N-azidoacetylglucosamine (GlcNAz).
21300897	0	33	theme	O-linked	40:47	arg1	proteins					83:90	O-linked beta-N-acetylglucosamine-modified proteins	40:90	O-linked beta-N-acetylglucosamine-modified proteins	40:90	Metabolic cross-talk allows labeling of O-linked beta-N-acetylglucosamine-modified proteins via the N-acetylgalactosamine salvage pathway.
21300897	6	34	theme	human	1194:1198	arg1	cells					1200:1204	human cells	1194:1204	human cells	1194:1204	In a proof-of-principle proteomics experiment, we used metabolic GalNAz labeling of human cells and a bioorthogonal chemical probe to affinity-purify and identify numerous O-GlcNAcylated proteins.
21300897	2	35	theme	molecular	478:486	arg1	techniques					508:517	traditional molecular and cell biological techniques	466:517	traditional molecular and cell biological techniques alone	466:523	Despite its broad functional significance, the dynamic and posttranslational nature of O-GlcNAc signaling makes it challenging to study using traditional molecular and cell biological techniques alone.
21300897	3	36	theme	O-GlcNAcylated	694:707	arg1	proteins					709:716	O-GlcNAcylated proteins	694:716	O-GlcNAcylated proteins	694:716	Here, we report that metabolic cross-talk between the N-acetylgalactosamine salvage and O-GlcNAcylation pathways can be exploited for the tagging and identification of O-GlcNAcylated proteins.
21300897	2	37	theme	traditional	466:476	arg1	techniques					508:517	traditional molecular and cell biological techniques	466:517	traditional molecular and cell biological techniques alone	466:523	Despite its broad functional significance, the dynamic and posttranslational nature of O-GlcNAc signaling makes it challenging to study using traditional molecular and cell biological techniques alone.
21300897	0	38	theme	proteins	83:90	arg1	labeling					28:35	labeling	28:35	labeling of O-linked beta-N-acetylglucosamine-modified proteins	28:90	Metabolic cross-talk allows labeling of O-linked beta-N-acetylglucosamine-modified proteins via the N-acetylgalactosamine salvage pathway.
21300897	7	39	dep	future	1359:1364	arg1	chemical					1366:1373	chemical	1366:1373	chemical	1366:1373	Our work provides a blueprint for a wide variety of future chemical approaches to identify, visualize, and characterize dynamic O-GlcNAc signaling.
21300897	1	40	theme	mammalian	151:159	arg1	proteins					185:192	mammalian nuclear and cytoplasmic proteins	151:192	mammalian nuclear and cytoplasmic proteins	151:192	Hundreds of mammalian nuclear and cytoplasmic proteins are reversibly glycosylated by O-linked β-N-acetylglucosamine (O-GlcNAc) to regulate their function, localization, and stability.
21300897	0	41	theme	beta-N-acetylglucosamine-modified	49:81	arg1	proteins					83:90	O-linked beta-N-acetylglucosamine-modified proteins	40:90	O-linked beta-N-acetylglucosamine-modified proteins	40:90	Metabolic cross-talk allows labeling of O-linked beta-N-acetylglucosamine-modified proteins via the N-acetylgalactosamine salvage pathway.
21300897	1	42	theme	nuclear	161:167	arg1	proteins					185:192	mammalian nuclear and cytoplasmic proteins	151:192	mammalian nuclear and cytoplasmic proteins	151:192	Hundreds of mammalian nuclear and cytoplasmic proteins are reversibly glycosylated by O-linked β-N-acetylglucosamine (O-GlcNAc) to regulate their function, localization, and stability.
21300897	1	43	gly	glycosylated	209:220	arg1	Hundreds					139:146	Hundreds	139:146	Hundreds of mammalian nuclear and cytoplasmic proteins	139:192	Hundreds of mammalian nuclear and cytoplasmic proteins are reversibly glycosylated by O-linked β-N-acetylglucosamine (O-GlcNAc) to regulate their function, localization, and stability.
21300897	6	44	theme	GalNAz	1175:1180	arg1	labeling					1182:1189	metabolic GalNAz labeling	1165:1189	metabolic GalNAz labeling of human cells	1165:1204	In a proof-of-principle proteomics experiment, we used metabolic GalNAz labeling of human cells and a bioorthogonal chemical probe to affinity-purify and identify numerous O-GlcNAcylated proteins.
21300897	2	45	theme	posttranslational	383:399	arg1	nature					401:406	the dynamic and posttranslational nature	367:406	the dynamic and posttranslational nature of O-GlcNAc signaling	367:428	Despite its broad functional significance, the dynamic and posttranslational nature of O-GlcNAc signaling makes it challenging to study using traditional molecular and cell biological techniques alone.
21300897	6	46	theme	numerous	1273:1280	arg1	proteins					1297:1304	numerous O-GlcNAcylated proteins	1273:1304	numerous O-GlcNAcylated proteins	1273:1304	In a proof-of-principle proteomics experiment, we used metabolic GalNAz labeling of human cells and a bioorthogonal chemical probe to affinity-purify and identify numerous O-GlcNAcylated proteins.
21300897	1	47	theme	cytoplasmic	173:183	arg1	proteins					185:192	mammalian nuclear and cytoplasmic proteins	151:192	mammalian nuclear and cytoplasmic proteins	151:192	Hundreds of mammalian nuclear and cytoplasmic proteins are reversibly glycosylated by O-linked β-N-acetylglucosamine (O-GlcNAc) to regulate their function, localization, and stability.
21300897	5	48	theme	covalent	1054:1061	arg1	labeling					1063:1070	covalent labeling	1054:1070	covalent labeling using azide-reactive chemical probes	1054:1107	O-GlcNAc transferase accepts UDP-GlcNAz as a nucleotide-sugar donor, appending an azidosugar onto its native substrates, which can then be detected by covalent labeling using azide-reactive chemical probes.
21300897	3	49	theme	proteins	709:716	arg1	identification					676:689	identification	676:689	identification	676:689	Here, we report that metabolic cross-talk between the N-acetylgalactosamine salvage and O-GlcNAcylation pathways can be exploited for the tagging and identification of O-GlcNAcylated proteins.
21300897	3	49	theme	proteins	709:716	arg1	tagging					664:670	tagging	664:670	tagging	664:670	Here, we report that metabolic cross-talk between the N-acetylgalactosamine salvage and O-GlcNAcylation pathways can be exploited for the tagging and identification of O-GlcNAcylated proteins.
21300897	1	50	theme	proteins	185:192	arg1	Hundreds					139:146	Hundreds	139:146	Hundreds of mammalian nuclear and cytoplasmic proteins	139:192	Hundreds of mammalian nuclear and cytoplasmic proteins are reversibly glycosylated by O-linked β-N-acetylglucosamine (O-GlcNAc) to regulate their function, localization, and stability.
21300897	5	51	theme	native	1005:1010	arg1	substrates					1012:1021	its native substrates	1001:1021	its native substrates	1001:1021	O-GlcNAc transferase accepts UDP-GlcNAz as a nucleotide-sugar donor, appending an azidosugar onto its native substrates, which can then be detected by covalent labeling using azide-reactive chemical probes.
21300897	6	52	theme	metabolic	1165:1173	arg1	labeling					1182:1189	metabolic GalNAz labeling	1165:1189	metabolic GalNAz labeling of human cells	1165:1204	In a proof-of-principle proteomics experiment, we used metabolic GalNAz labeling of human cells and a bioorthogonal chemical probe to affinity-purify and identify numerous O-GlcNAcylated proteins.
21300897	4	53	theme	endogenous	785:794	arg1	enzymes					819:825	endogenous mammalian biosynthetic enzymes	785:825	endogenous mammalian biosynthetic enzymes	785:825	We found that N-azidoacetylgalactosamine (GalNAz) is converted by endogenous mammalian biosynthetic enzymes to UDP-GalNAz and then epimerized to UDP-N-azidoacetylglucosamine (GlcNAz).
21300897	7	54	theme	wide	1343:1346	arg1	variety					1348:1354	a wide variety	1341:1354	a wide variety of future chemical approaches to identify, visualize, and characterize dynamic O-GlcNAc signaling	1341:1452	Our work provides a blueprint for a wide variety of future chemical approaches to identify, visualize, and characterize dynamic O-GlcNAc signaling.
21300897	7	54	theme	wide	1343:1346	arg1	approaches					1375:1384	future chemical approaches	1359:1384	future chemical approaches	1359:1384	Our work provides a blueprint for a wide variety of future chemical approaches to identify, visualize, and characterize dynamic O-GlcNAc signaling.
33731348	0	0	theme	ERα	83:85	arg1	glycosylation					87:99	ERα glycosylation	83:99	ERα glycosylation	83:99	GREB1: An evolutionarily conserved protein with a glycosyltransferase domain links ERα glycosylation and stability to cancer.
33731348	6	1	theme	bacteriophages	948:961	arg1	glycosyltransferases					924:943	DNA-modifying glycosyltransferases	910:943	DNA-modifying glycosyltransferases of bacteriophages and kinetoplastids	910:980	In summary, this study identifies GREB1, a protein with an evolutionarily conserved domain related to DNA-modifying glycosyltransferases of bacteriophages and kinetoplastids, as the first inducible and the only other (apart from OGT) O-GlcNAc glycosyltransferase in mammalian cytoplasm and ERα as its first substrate.
33731348	5	2	theme	ERα-null	793:800	arg1	mice					802:805	ERα-null mice	793:805	ERα-null mice	793:805	Mice lacking Greb1 exhibit growth and fertility defects reminiscent of phenotypes in ERα-null mice.
33731348	1	3	theme	temporal	166:173	arg1	ubiquitination					175:188	the temporal ubiquitination	162:188	the temporal ubiquitination of ERα	162:195	What covalent modifications control the temporal ubiquitination of ERα and hence the duration of its transcriptional activity remain poorly understood.
33731348	2	4	dep	residues	359:366	arg1	T553/S554					368:376	T553/S554	368:376	T553/S554	368:376	We show that GREB1, an ERα-inducible enzyme, catalyzes O-GlcNAcylation of ERα at residues T553/S554, which stabilizes ERα protein by inhibiting association with the ubiquitin ligase ZNF598.
33731348	4	5	theme	breast	616:621	arg1	cancer					623:628	ERα+ve breast cancer	609:628	ERα+ve breast cancer	609:628	Higher GREB1 expression in ERα+ve breast cancer is associated with greater survival in response to tamoxifen, an ERα agonist.
33731348	5	6	theme	fertility	746:754	arg1	defects					756:762	growth and fertility defects	735:762	growth and fertility defects reminiscent of phenotypes in ERα-null mice	735:805	Mice lacking Greb1 exhibit growth and fertility defects reminiscent of phenotypes in ERα-null mice.
33731348	6	7	theme	DNA-modifying	910:922	arg1	glycosyltransferases					924:943	DNA-modifying glycosyltransferases	910:943	DNA-modifying glycosyltransferases of bacteriophages and kinetoplastids	910:980	In summary, this study identifies GREB1, a protein with an evolutionarily conserved domain related to DNA-modifying glycosyltransferases of bacteriophages and kinetoplastids, as the first inducible and the only other (apart from OGT) O-GlcNAc glycosyltransferase in mammalian cytoplasm and ERα as its first substrate.
33731348	4	8	theme	ERα+ve	609:614	arg1	cancer					623:628	ERα+ve breast cancer	609:628	ERα+ve breast cancer	609:628	Higher GREB1 expression in ERα+ve breast cancer is associated with greater survival in response to tamoxifen, an ERα agonist.
33731348	3	9	theme	ERα	508:510	arg1	glycosylation					491:503	GREB1-mediated glycosylation	476:503	GREB1-mediated glycosylation of ERα	476:510	Loss of GREB1-mediated glycosylation of ERα results in reduced cellular ERα levels and insensitivity to estrogen.
33731348	4	10	theme	greater	649:655	arg1	survival					657:664	greater survival	649:664	greater survival in response to tamoxifen, an ERα agonist	649:705	Higher GREB1 expression in ERα+ve breast cancer is associated with greater survival in response to tamoxifen, an ERα agonist.
33731348	6	11	theme	mammalian	1074:1082	arg1	cytoplasm					1084:1092	mammalian cytoplasm	1074:1092	mammalian cytoplasm	1074:1092	In summary, this study identifies GREB1, a protein with an evolutionarily conserved domain related to DNA-modifying glycosyltransferases of bacteriophages and kinetoplastids, as the first inducible and the only other (apart from OGT) O-GlcNAc glycosyltransferase in mammalian cytoplasm and ERα as its first substrate.
33731348	4	12	from	expression	595:604	arg1	cancer					623:628	ERα+ve breast cancer	609:628	ERα+ve breast cancer	609:628	Higher GREB1 expression in ERα+ve breast cancer is associated with greater survival in response to tamoxifen, an ERα agonist.
33731348	6	13	theme	related	899:905	arg1	domain					892:897	an evolutionarily conserved domain	864:897	an evolutionarily conserved domain related to DNA-modifying glycosyltransferases of bacteriophages and kinetoplastids	864:980	In summary, this study identifies GREB1, a protein with an evolutionarily conserved domain related to DNA-modifying glycosyltransferases of bacteriophages and kinetoplastids, as the first inducible and the only other (apart from OGT) O-GlcNAc glycosyltransferase in mammalian cytoplasm and ERα as its first substrate.
33731348	2	14	from	residues	359:366	arg1	O-GlcNAcylation					333:347	O-GlcNAcylation	333:347	O-GlcNAcylation	333:347	We show that GREB1, an ERα-inducible enzyme, catalyzes O-GlcNAcylation of ERα at residues T553/S554, which stabilizes ERα protein by inhibiting association with the ubiquitin ligase ZNF598.
33731348	6	15	theme	first	1109:1113	arg1	substrate					1115:1123	its first substrate	1105:1123	its first substrate	1105:1123	In summary, this study identifies GREB1, a protein with an evolutionarily conserved domain related to DNA-modifying glycosyltransferases of bacteriophages and kinetoplastids, as the first inducible and the only other (apart from OGT) O-GlcNAc glycosyltransferase in mammalian cytoplasm and ERα as its first substrate.
33731348	2	16	theme	ERα	396:398	arg1	protein					400:406	ERα protein	396:406	ERα protein	396:406	We show that GREB1, an ERα-inducible enzyme, catalyzes O-GlcNAcylation of ERα at residues T553/S554, which stabilizes ERα protein by inhibiting association with the ubiquitin ligase ZNF598.
33731348	2	17	with	association	422:432	arg1	ligase					453:458	the ubiquitin ligase ZNF598	439:465	the ubiquitin ligase ZNF598	439:465	We show that GREB1, an ERα-inducible enzyme, catalyzes O-GlcNAcylation of ERα at residues T553/S554, which stabilizes ERα protein by inhibiting association with the ubiquitin ligase ZNF598.
33731348	1	18	theme	ERα	193:195	arg1	ubiquitination					175:188	the temporal ubiquitination	162:188	the temporal ubiquitination of ERα	162:195	What covalent modifications control the temporal ubiquitination of ERα and hence the duration of its transcriptional activity remain poorly understood.
33731348	1	18	theme	ERα	193:195	arg1	duration					211:218	hence the duration	201:218	hence the duration of its transcriptional activity	201:250	What covalent modifications control the temporal ubiquitination of ERα and hence the duration of its transcriptional activity remain poorly understood.
33731348	2	19	theme	ubiquitin	443:451	arg1	ligase					453:458	the ubiquitin ligase ZNF598	439:465	the ubiquitin ligase ZNF598	439:465	We show that GREB1, an ERα-inducible enzyme, catalyzes O-GlcNAcylation of ERα at residues T553/S554, which stabilizes ERα protein by inhibiting association with the ubiquitin ligase ZNF598.
33731348	2	20	theme	ERα-inducible	301:313	arg1	GREB1					291:295	GREB1	291:295	GREB1	291:295	We show that GREB1, an ERα-inducible enzyme, catalyzes O-GlcNAcylation of ERα at residues T553/S554, which stabilizes ERα protein by inhibiting association with the ubiquitin ligase ZNF598.
33731348	2	20	theme	ERα-inducible	301:313	arg1	enzyme					315:320	an ERα-inducible enzyme	298:320	an ERα-inducible enzyme	298:320	We show that GREB1, an ERα-inducible enzyme, catalyzes O-GlcNAcylation of ERα at residues T553/S554, which stabilizes ERα protein by inhibiting association with the ubiquitin ligase ZNF598.
33731348	4	21	theme	GREB1	589:593	arg1	expression					595:604	Higher GREB1 expression	582:604	Higher GREB1 expression in ERα+ve breast cancer	582:628	Higher GREB1 expression in ERα+ve breast cancer is associated with greater survival in response to tamoxifen, an ERα agonist.
33731348	6	22	theme	conserved	882:890	arg1	domain					892:897	an evolutionarily conserved domain	864:897	an evolutionarily conserved domain related to DNA-modifying glycosyltransferases of bacteriophages and kinetoplastids	864:980	In summary, this study identifies GREB1, a protein with an evolutionarily conserved domain related to DNA-modifying glycosyltransferases of bacteriophages and kinetoplastids, as the first inducible and the only other (apart from OGT) O-GlcNAc glycosyltransferase in mammalian cytoplasm and ERα as its first substrate.
33731348	3	23	gly	glycosylation	491:503	arg1	ERα					508:510	ERα	508:510	ERα	508:510	Loss of GREB1-mediated glycosylation of ERα results in reduced cellular ERα levels and insensitivity to estrogen.
33731348	4	24	from	survival	657:664	arg1	response					669:676	response	669:676	response to tamoxifen, an ERα agonist	669:705	Higher GREB1 expression in ERα+ve breast cancer is associated with greater survival in response to tamoxifen, an ERα agonist.
33731348	3	25	theme	GREB1-mediated	476:489	arg1	glycosylation					491:503	GREB1-mediated glycosylation	476:503	GREB1-mediated glycosylation of ERα	476:510	Loss of GREB1-mediated glycosylation of ERα results in reduced cellular ERα levels and insensitivity to estrogen.
33731348	4	26	theme	Higher	582:587	arg1	expression					595:604	Higher GREB1 expression	582:604	Higher GREB1 expression in ERα+ve breast cancer	582:628	Higher GREB1 expression in ERα+ve breast cancer is associated with greater survival in response to tamoxifen, an ERα agonist.
33731348	5	27	from	reminiscent	764:774	arg1	mice					802:805	ERα-null mice	793:805	ERα-null mice	793:805	Mice lacking Greb1 exhibit growth and fertility defects reminiscent of phenotypes in ERα-null mice.
33731348	6	28	with	protein	851:857	arg1	domain					892:897	an evolutionarily conserved domain	864:897	an evolutionarily conserved domain related to DNA-modifying glycosyltransferases of bacteriophages and kinetoplastids	864:980	In summary, this study identifies GREB1, a protein with an evolutionarily conserved domain related to DNA-modifying glycosyltransferases of bacteriophages and kinetoplastids, as the first inducible and the only other (apart from OGT) O-GlcNAc glycosyltransferase in mammalian cytoplasm and ERα as its first substrate.
33731348	0	29	theme	conserved	25:33	arg1	protein					35:41	An evolutionarily conserved protein	7:41	GREB1: An evolutionarily conserved protein with a glycosyltransferase domain	0:75	GREB1: An evolutionarily conserved protein with a glycosyltransferase domain links ERα glycosylation and stability to cancer.
33731348	5	30	theme	growth	735:740	arg1	defects					756:762	growth and fertility defects	735:762	growth and fertility defects reminiscent of phenotypes in ERα-null mice	735:805	Mice lacking Greb1 exhibit growth and fertility defects reminiscent of phenotypes in ERα-null mice.
33731348	5	31	dep	defects	756:762	arg1	reminiscent					764:774	reminiscent	764:774	growth and fertility defects reminiscent of phenotypes in ERα-null mice	735:805	Mice lacking Greb1 exhibit growth and fertility defects reminiscent of phenotypes in ERα-null mice.
33731348	5	32	theme	phenotypes	779:788	arg1	reminiscent					764:774	reminiscent	764:774	growth and fertility defects reminiscent of phenotypes in ERα-null mice	735:805	Mice lacking Greb1 exhibit growth and fertility defects reminiscent of phenotypes in ERα-null mice.
33731348	2	33	theme	ERα	352:354	arg1	O-GlcNAcylation					333:347	O-GlcNAcylation	333:347	O-GlcNAcylation	333:347	We show that GREB1, an ERα-inducible enzyme, catalyzes O-GlcNAcylation of ERα at residues T553/S554, which stabilizes ERα protein by inhibiting association with the ubiquitin ligase ZNF598.
33731348	6	34	dep	inducible	996:1004	arg1	glycosyltransferase					1051:1069	O-GlcNAc glycosyltransferase	1042:1069	O-GlcNAc glycosyltransferase	1042:1069	In summary, this study identifies GREB1, a protein with an evolutionarily conserved domain related to DNA-modifying glycosyltransferases of bacteriophages and kinetoplastids, as the first inducible and the only other (apart from OGT) O-GlcNAc glycosyltransferase in mammalian cytoplasm and ERα as its first substrate.
33731348	0	35	attach	links	77:81	arg2	GREB1					0:4	GREB1	0:4	GREB1: An evolutionarily conserved protein with a glycosyltransferase domain	0:75	GREB1: An evolutionarily conserved protein with a glycosyltransferase domain links ERα glycosylation and stability to cancer.
33731348	0	35	attach	links	77:81	arg1	cancer					118:123	cancer	118:123	cancer	118:123	GREB1: An evolutionarily conserved protein with a glycosyltransferase domain links ERα glycosylation and stability to cancer.
33731348	6	36	theme	kinetoplastids	967:980	arg1	glycosyltransferases					924:943	DNA-modifying glycosyltransferases	910:943	DNA-modifying glycosyltransferases of bacteriophages and kinetoplastids	910:980	In summary, this study identifies GREB1, a protein with an evolutionarily conserved domain related to DNA-modifying glycosyltransferases of bacteriophages and kinetoplastids, as the first inducible and the only other (apart from OGT) O-GlcNAc glycosyltransferase in mammalian cytoplasm and ERα as its first substrate.
33731348	3	37	theme	reduced	523:529	arg1	levels					544:549	reduced cellular ERα levels	523:549	reduced cellular ERα levels	523:549	Loss of GREB1-mediated glycosylation of ERα results in reduced cellular ERα levels and insensitivity to estrogen.
33731348	4	38	theme	ERα	695:697	arg1	tamoxifen					681:689	tamoxifen	681:689	tamoxifen	681:689	Higher GREB1 expression in ERα+ve breast cancer is associated with greater survival in response to tamoxifen, an ERα agonist.
33731348	4	38	theme	ERα	695:697	arg1	agonist					699:705	an ERα agonist	692:705	an ERα agonist	692:705	Higher GREB1 expression in ERα+ve breast cancer is associated with greater survival in response to tamoxifen, an ERα agonist.
33731348	3	39	theme	glycosylation	491:503	arg1	Loss					468:471	Loss	468:471	Loss of GREB1-mediated glycosylation of ERα	468:510	Loss of GREB1-mediated glycosylation of ERα results in reduced cellular ERα levels and insensitivity to estrogen.
33731348	1	40	dep	modifications	140:152	arg1	control					154:160	control	154:160	control the temporal ubiquitination of ERα and hence the duration of its transcriptional activity	154:250	What covalent modifications control the temporal ubiquitination of ERα and hence the duration of its transcriptional activity remain poorly understood.
33731348	6	41	theme	O-GlcNAc	1042:1049	arg1	glycosyltransferase					1051:1069	O-GlcNAc glycosyltransferase	1042:1069	O-GlcNAc glycosyltransferase	1042:1069	In summary, this study identifies GREB1, a protein with an evolutionarily conserved domain related to DNA-modifying glycosyltransferases of bacteriophages and kinetoplastids, as the first inducible and the only other (apart from OGT) O-GlcNAc glycosyltransferase in mammalian cytoplasm and ERα as its first substrate.
33731348	1	42	theme	covalent	131:138	arg1	modifications					140:152	covalent modifications	131:152	covalent modifications control the temporal ubiquitination of ERα and hence the duration of its transcriptional activity	131:250	What covalent modifications control the temporal ubiquitination of ERα and hence the duration of its transcriptional activity remain poorly understood.
33731348	1	43	theme	transcriptional	227:241	arg1	activity					243:250	its transcriptional activity	223:250	its transcriptional activity	223:250	What covalent modifications control the temporal ubiquitination of ERα and hence the duration of its transcriptional activity remain poorly understood.
33731348	3	44	theme	cellular	531:538	arg1	levels					544:549	reduced cellular ERα levels	523:549	reduced cellular ERα levels	523:549	Loss of GREB1-mediated glycosylation of ERα results in reduced cellular ERα levels and insensitivity to estrogen.
33731348	1	45	theme	activity	243:250	arg1	ubiquitination					175:188	the temporal ubiquitination	162:188	the temporal ubiquitination of ERα	162:195	What covalent modifications control the temporal ubiquitination of ERα and hence the duration of its transcriptional activity remain poorly understood.
33731348	1	45	theme	activity	243:250	arg1	duration					211:218	hence the duration	201:218	hence the duration of its transcriptional activity	201:250	What covalent modifications control the temporal ubiquitination of ERα and hence the duration of its transcriptional activity remain poorly understood.
33731348	0	46	theme	glycosyltransferase	50:68	arg1	domain					70:75	a glycosyltransferase domain	48:75	a glycosyltransferase domain	48:75	GREB1: An evolutionarily conserved protein with a glycosyltransferase domain links ERα glycosylation and stability to cancer.
33731348	0	47	dep	GREB1	0:4	arg1	protein					35:41	An evolutionarily conserved protein	7:41	GREB1: An evolutionarily conserved protein with a glycosyltransferase domain	0:75	GREB1: An evolutionarily conserved protein with a glycosyltransferase domain links ERα glycosylation and stability to cancer.
33731348	0	48	with	protein	35:41	arg1	domain					70:75	a glycosyltransferase domain	48:75	a glycosyltransferase domain	48:75	GREB1: An evolutionarily conserved protein with a glycosyltransferase domain links ERα glycosylation and stability to cancer.
33731348	3	49	theme	ERα	540:542	arg1	levels					544:549	reduced cellular ERα levels	523:549	reduced cellular ERα levels	523:549	Loss of GREB1-mediated glycosylation of ERα results in reduced cellular ERα levels and insensitivity to estrogen.
33909326	7	0	dep	RESULTS	1076:1082	arg1	XIST					1084:1087	XIST	1084:1087	XIST	1084:1087	RESULTS XIST and OGT were up-regulated in liver cancer tissues and cells, responsible for poor prognosis in patients with liver cancer, while miR-424-5p was down-regulated.
33909326	7	0	dep	RESULTS	1076:1082	arg1	RESULTS					1076:1082	RESULTS XIST and OGT	1076:1095	RESULTS XIST and OGT	1076:1095	RESULTS XIST and OGT were up-regulated in liver cancer tissues and cells, responsible for poor prognosis in patients with liver cancer, while miR-424-5p was down-regulated.
33909326	7	0	dep	RESULTS	1076:1082	arg1	OGT					1093:1095	OGT	1093:1095	OGT	1093:1095	RESULTS XIST and OGT were up-regulated in liver cancer tissues and cells, responsible for poor prognosis in patients with liver cancer, while miR-424-5p was down-regulated.
33909326	9	1	theme	cancer	1371:1376	arg1	cells					1378:1382	liver cancer cells	1365:1382	liver cancer cells	1365:1382	XIST silencing inhibited malignant phenotypes of liver cancer cells, while miR-424-5p down-regulation negated its effect.
33909326	1	2	theme	major	155:159	arg1	cancer					143:148	BACKGROUND Liver cancer	126:148	BACKGROUND Liver cancer	126:148	BACKGROUND Liver cancer is a major public health concern, but the mechanistic actions of biomarkers contributing to liver cancer remain to be determined.
33909326	1	2	theme	major	155:159	arg1	concern					175:181	a major public health concern	153:181	a major public health concern	153:181	BACKGROUND Liver cancer is a major public health concern, but the mechanistic actions of biomarkers contributing to liver cancer remain to be determined.
33909326	10	3	theme	OGT	1504:1506	arg1	expression					1508:1517	negatively regulating OGT expression	1482:1517	negatively regulating OGT expression	1482:1517	miR-424-5p suppressed RAF1 glycosylation by negatively regulating OGT expression and promoted its ubiquitination/degradation.
33909326	1	4	theme	public	161:166	arg1	cancer					143:148	BACKGROUND Liver cancer	126:148	BACKGROUND Liver cancer	126:148	BACKGROUND Liver cancer is a major public health concern, but the mechanistic actions of biomarkers contributing to liver cancer remain to be determined.
33909326	1	4	theme	public	161:166	arg1	concern					175:181	a major public health concern	153:181	a major public health concern	153:181	BACKGROUND Liver cancer is a major public health concern, but the mechanistic actions of biomarkers contributing to liver cancer remain to be determined.
33909326	5	5	from	effects	924:930	arg1	phenotypes					977:986	malignant phenotypes	967:986	malignant phenotypes	967:986	Then, gain- and loss-of-function assays were conducted to evaluate the effects of the XIST/miR-424-5p/OGT axis on malignant phenotypes.
33909326	9	6	theme	miR-424-5p	1391:1400	arg1	down-regulation					1402:1416	miR-424-5p down-regulation	1391:1416	miR-424-5p down-regulation	1391:1416	XIST silencing inhibited malignant phenotypes of liver cancer cells, while miR-424-5p down-regulation negated its effect.
33909326	6	7	theme	mouse	996:1000	arg1	model					1002:1006	A nude mouse model	989:1006	A nude mouse model of liver cancer	989:1022	A nude mouse model of liver cancer was further established for in vivo substantiation.
33909326	3	8	theme	liver	672:676	arg1	cells					685:689	liver cancer cells	672:689	liver cancer cells	672:689	METHODS Differentially expressed miRNAs and target genes related to liver cancer were predicted by bioinformatics analyses, and their expression was determined in liver tissues of patients with liver cancer and liver cancer cells.
33909326	11	9	theme	XIST	1577:1580	arg1	knockdown					1582:1590	XIST knockdown	1577:1590	XIST knockdown	1577:1590	Furthermore, XIST knockdown inhibited tumour growth and metastasis in nude mice, while ectopic OGT reversed its effect.
33909326	12	10	theme	XIST/miR-424-5p/OGT	1762:1780	arg1	interaction					1747:1757	the interaction	1743:1757	the interaction of XIST/miR-424-5p/OGT	1743:1780	CONCLUSION These results reveal a novel mechanism by which the interaction of XIST/miR-424-5p/OGT participates in the malignancy and metastasis of liver cancer.
33909326	12	11	theme	cancer	1837:1842	arg1	malignancy					1802:1811	malignancy	1802:1811	malignancy	1802:1811	CONCLUSION These results reveal a novel mechanism by which the interaction of XIST/miR-424-5p/OGT participates in the malignancy and metastasis of liver cancer.
33909326	12	11	theme	cancer	1837:1842	arg1	metastasis					1817:1826	metastasis	1817:1826	metastasis	1817:1826	CONCLUSION These results reveal a novel mechanism by which the interaction of XIST/miR-424-5p/OGT participates in the malignancy and metastasis of liver cancer.
33909326	7	12	theme	responsible	1150:1160	arg1	tissues					1131:1137	liver cancer tissues	1118:1137	liver cancer tissues	1118:1137	RESULTS XIST and OGT were up-regulated in liver cancer tissues and cells, responsible for poor prognosis in patients with liver cancer, while miR-424-5p was down-regulated.
33909326	9	13	theme	malignant	1341:1349	arg1	phenotypes					1351:1360	malignant phenotypes	1341:1360	malignant phenotypes of liver cancer cells	1341:1382	XIST silencing inhibited malignant phenotypes of liver cancer cells, while miR-424-5p down-regulation negated its effect.
33909326	3	14	theme	liver	529:533	arg1	cancer					535:540	liver cancer	529:540	liver cancer	529:540	METHODS Differentially expressed miRNAs and target genes related to liver cancer were predicted by bioinformatics analyses, and their expression was determined in liver tissues of patients with liver cancer and liver cancer cells.
33909326	3	15	with	patients	641:648	arg1	cells					685:689	liver cancer cells	672:689	liver cancer cells	672:689	METHODS Differentially expressed miRNAs and target genes related to liver cancer were predicted by bioinformatics analyses, and their expression was determined in liver tissues of patients with liver cancer and liver cancer cells.
33909326	3	15	with	patients	641:648	arg1	cancer					661:666	liver cancer	655:666	liver cancer	655:666	METHODS Differentially expressed miRNAs and target genes related to liver cancer were predicted by bioinformatics analyses, and their expression was determined in liver tissues of patients with liver cancer and liver cancer cells.
33909326	4	16	theme	RNA	696:698	arg1	RIP					721:723	RIP	721:723	RIP	721:723	The RNA immunoprecipitation (RIP), RNA pull-down and dual luciferase reporter assay were used to examine the binding affinity among XIST and miR-424-5p and OGT.
33909326	4	16	theme	RNA	696:698	arg1	immunoprecipitation					700:718	The RNA immunoprecipitation	692:718	The RNA immunoprecipitation (RIP)	692:724	The RNA immunoprecipitation (RIP), RNA pull-down and dual luciferase reporter assay were used to examine the binding affinity among XIST and miR-424-5p and OGT.
33909326	0	17	theme	cancer	118:123	arg1	progression					97:107	the progression	93:107	the progression of liver cancer	93:123	The crosstalk network of XIST/miR-424-5p/OGT mediates RAF1 glycosylation and participates in the progression of liver cancer.
33909326	6	18	theme	liver	1011:1015	arg1	cancer					1017:1022	liver cancer	1011:1022	liver cancer	1011:1022	A nude mouse model of liver cancer was further established for in vivo substantiation.
33909326	3	19	dep	METHODS	461:467	arg1	miRNAs					494:499	Differentially expressed miRNAs	469:499	Differentially expressed miRNAs	469:499	METHODS Differentially expressed miRNAs and target genes related to liver cancer were predicted by bioinformatics analyses, and their expression was determined in liver tissues of patients with liver cancer and liver cancer cells.
33909326	3	19	dep	METHODS	461:467	arg1	genes					512:516	target genes	505:516	target genes related to liver cancer	505:540	METHODS Differentially expressed miRNAs and target genes related to liver cancer were predicted by bioinformatics analyses, and their expression was determined in liver tissues of patients with liver cancer and liver cancer cells.
33909326	1	20	theme	health	168:173	arg1	cancer					143:148	BACKGROUND Liver cancer	126:148	BACKGROUND Liver cancer	126:148	BACKGROUND Liver cancer is a major public health concern, but the mechanistic actions of biomarkers contributing to liver cancer remain to be determined.
33909326	1	20	theme	health	168:173	arg1	concern					175:181	a major public health concern	153:181	a major public health concern	153:181	BACKGROUND Liver cancer is a major public health concern, but the mechanistic actions of biomarkers contributing to liver cancer remain to be determined.
33909326	0	21	theme	liver	112:116	arg1	cancer					118:123	liver cancer	112:123	liver cancer	112:123	The crosstalk network of XIST/miR-424-5p/OGT mediates RAF1 glycosylation and participates in the progression of liver cancer.
33909326	4	22	theme	binding	801:807	arg1	affinity					809:816	the binding affinity	797:816	the binding affinity among XIST and miR-424-5p and OGT	797:850	The RNA immunoprecipitation (RIP), RNA pull-down and dual luciferase reporter assay were used to examine the binding affinity among XIST and miR-424-5p and OGT.
33909326	11	23	theme	tumour	1602:1607	arg1	growth					1609:1614	tumour growth	1602:1614	tumour growth	1602:1614	Furthermore, XIST knockdown inhibited tumour growth and metastasis in nude mice, while ectopic OGT reversed its effect.
33909326	3	24	theme	related	518:524	arg1	genes					512:516	target genes	505:516	target genes related to liver cancer	505:540	METHODS Differentially expressed miRNAs and target genes related to liver cancer were predicted by bioinformatics analyses, and their expression was determined in liver tissues of patients with liver cancer and liver cancer cells.
33909326	4	25	used	used	781:784	arg2	immunoprecipitation					700:718	The RNA immunoprecipitation	692:718	The RNA immunoprecipitation (RIP)	692:724	The RNA immunoprecipitation (RIP), RNA pull-down and dual luciferase reporter assay were used to examine the binding affinity among XIST and miR-424-5p and OGT.
33909326	4	25	used	used	781:784	arg2	pull-down					731:739	pull-down	731:739	pull-down	731:739	The RNA immunoprecipitation (RIP), RNA pull-down and dual luciferase reporter assay were used to examine the binding affinity among XIST and miR-424-5p and OGT.
33909326	4	25	used	used	781:784	arg2	RIP					721:723	RIP	721:723	RIP	721:723	The RNA immunoprecipitation (RIP), RNA pull-down and dual luciferase reporter assay were used to examine the binding affinity among XIST and miR-424-5p and OGT.
33909326	4	25	used	used	781:784	arg2	assay					770:774	dual luciferase reporter assay	745:774	dual luciferase reporter assay	745:774	The RNA immunoprecipitation (RIP), RNA pull-down and dual luciferase reporter assay were used to examine the binding affinity among XIST and miR-424-5p and OGT.
33909326	0	26	theme	crosstalk	4:12	arg1	network					14:20	The crosstalk network	0:20	The crosstalk network of XIST/miR-424-5p/OGT	0:43	The crosstalk network of XIST/miR-424-5p/OGT mediates RAF1 glycosylation and participates in the progression of liver cancer.
33909326	10	27	theme	RAF1	1460:1463	arg1	glycosylation					1465:1477	RAF1 glycosylation	1460:1477	RAF1 glycosylation	1460:1477	miR-424-5p suppressed RAF1 glycosylation by negatively regulating OGT expression and promoted its ubiquitination/degradation.
33909326	2	28	from	cascade	334:340	arg1	cancer					453:458	liver cancer	447:458	liver cancer	447:458	In this study, we aimed to investigate the regulatory cascade of microRNA-424-5p (miR-424-5p), X-inactive-specific transcript (XIST) and O-GlcNAc transferase (OGT) in liver cancer.
33909326	6	29	theme	in	1052:1053	arg1	substantiation					1060:1073	in vivo substantiation	1052:1073	in vivo substantiation	1052:1073	A nude mouse model of liver cancer was further established for in vivo substantiation.
33909326	2	30	theme	transferase	426:436	arg1	cascade					334:340	the regulatory cascade	319:340	the regulatory cascade of microRNA-424-5p (miR-424-5p), X-inactive-specific transcript (XIST) and O-GlcNAc transferase (OGT) in liver cancer	319:458	In this study, we aimed to investigate the regulatory cascade of microRNA-424-5p (miR-424-5p), X-inactive-specific transcript (XIST) and O-GlcNAc transferase (OGT) in liver cancer.
33909326	7	31	theme	liver	1118:1122	arg1	tissues					1131:1137	liver cancer tissues	1118:1137	liver cancer tissues	1118:1137	RESULTS XIST and OGT were up-regulated in liver cancer tissues and cells, responsible for poor prognosis in patients with liver cancer, while miR-424-5p was down-regulated.
33909326	7	32	from	prognosis	1171:1179	arg1	patients					1184:1191	patients	1184:1191	patients with liver cancer	1184:1209	RESULTS XIST and OGT were up-regulated in liver cancer tissues and cells, responsible for poor prognosis in patients with liver cancer, while miR-424-5p was down-regulated.
33909326	2	33	theme	O-GlcNAc	417:424	arg1	transferase					426:436	O-GlcNAc transferase	417:436	O-GlcNAc transferase (OGT)	417:442	In this study, we aimed to investigate the regulatory cascade of microRNA-424-5p (miR-424-5p), X-inactive-specific transcript (XIST) and O-GlcNAc transferase (OGT) in liver cancer.
33909326	2	33	theme	O-GlcNAc	417:424	arg1	OGT					439:441	OGT	439:441	OGT	439:441	In this study, we aimed to investigate the regulatory cascade of microRNA-424-5p (miR-424-5p), X-inactive-specific transcript (XIST) and O-GlcNAc transferase (OGT) in liver cancer.
33909326	7	34	with	patients	1184:1191	arg1	cancer					1204:1209	liver cancer	1198:1209	liver cancer	1198:1209	RESULTS XIST and OGT were up-regulated in liver cancer tissues and cells, responsible for poor prognosis in patients with liver cancer, while miR-424-5p was down-regulated.
33909326	6	35	theme	cancer	1017:1022	arg1	model					1002:1006	A nude mouse model	989:1006	A nude mouse model of liver cancer	989:1022	A nude mouse model of liver cancer was further established for in vivo substantiation.
33909326	9	36	theme	XIST	1316:1319	arg1	silencing					1321:1329	XIST silencing	1316:1329	XIST silencing	1316:1329	XIST silencing inhibited malignant phenotypes of liver cancer cells, while miR-424-5p down-regulation negated its effect.
33909326	4	37	theme	dual	745:748	arg1	assay					770:774	dual luciferase reporter assay	745:774	dual luciferase reporter assay	745:774	The RNA immunoprecipitation (RIP), RNA pull-down and dual luciferase reporter assay were used to examine the binding affinity among XIST and miR-424-5p and OGT.
33909326	11	38	from	metastasis	1620:1629	arg1	mice					1639:1642	nude mice	1634:1642	nude mice	1634:1642	Furthermore, XIST knockdown inhibited tumour growth and metastasis in nude mice, while ectopic OGT reversed its effect.
33909326	5	39	theme	gain-	859:863	arg1	assays					886:891	gain- and loss-of-function assays	859:891	gain- and loss-of-function assays	859:891	Then, gain- and loss-of-function assays were conducted to evaluate the effects of the XIST/miR-424-5p/OGT axis on malignant phenotypes.
33909326	11	40	from	growth	1609:1614	arg1	mice					1639:1642	nude mice	1634:1642	nude mice	1634:1642	Furthermore, XIST knockdown inhibited tumour growth and metastasis in nude mice, while ectopic OGT reversed its effect.
33909326	1	41	theme	mechanistic	192:202	arg1	actions					204:210	the mechanistic actions	188:210	the mechanistic actions of biomarkers contributing to liver cancer	188:253	BACKGROUND Liver cancer is a major public health concern, but the mechanistic actions of biomarkers contributing to liver cancer remain to be determined.
33909326	2	42	theme	liver	447:451	arg1	cancer					453:458	liver cancer	447:458	liver cancer	447:458	In this study, we aimed to investigate the regulatory cascade of microRNA-424-5p (miR-424-5p), X-inactive-specific transcript (XIST) and O-GlcNAc transferase (OGT) in liver cancer.
33909326	5	43	theme	loss-of-function	869:884	arg1	assays					886:891	gain- and loss-of-function assays	859:891	gain- and loss-of-function assays	859:891	Then, gain- and loss-of-function assays were conducted to evaluate the effects of the XIST/miR-424-5p/OGT axis on malignant phenotypes.
33909326	10	44	theme	regulating	1493:1502	arg1	expression					1508:1517	negatively regulating OGT expression	1482:1517	negatively regulating OGT expression	1482:1517	miR-424-5p suppressed RAF1 glycosylation by negatively regulating OGT expression and promoted its ubiquitination/degradation.
33909326	12	45	dep	malignancy	1802:1811	arg1	the					1798:1800	the	1798:1800	the	1798:1800	CONCLUSION These results reveal a novel mechanism by which the interaction of XIST/miR-424-5p/OGT participates in the malignancy and metastasis of liver cancer.
33909326	2	46	theme	X-inactive-specific	375:393	arg1	XIST					407:410	XIST	407:410	XIST	407:410	In this study, we aimed to investigate the regulatory cascade of microRNA-424-5p (miR-424-5p), X-inactive-specific transcript (XIST) and O-GlcNAc transferase (OGT) in liver cancer.
33909326	2	46	theme	X-inactive-specific	375:393	arg1	transcript					395:404	X-inactive-specific transcript	375:404	X-inactive-specific transcript (XIST)	375:411	In this study, we aimed to investigate the regulatory cascade of microRNA-424-5p (miR-424-5p), X-inactive-specific transcript (XIST) and O-GlcNAc transferase (OGT) in liver cancer.
33909326	0	47	theme	XIST/miR-424-5p/OGT	25:43	arg1	network					14:20	The crosstalk network	0:20	The crosstalk network of XIST/miR-424-5p/OGT	0:43	The crosstalk network of XIST/miR-424-5p/OGT mediates RAF1 glycosylation and participates in the progression of liver cancer.
33909326	6	48	dep	in	1052:1053	arg1	vivo					1055:1058	vivo	1055:1058	vivo	1055:1058	A nude mouse model of liver cancer was further established for in vivo substantiation.
33909326	2	49	theme	transcript	395:404	arg1	cascade					334:340	the regulatory cascade	319:340	the regulatory cascade of microRNA-424-5p (miR-424-5p), X-inactive-specific transcript (XIST) and O-GlcNAc transferase (OGT) in liver cancer	319:458	In this study, we aimed to investigate the regulatory cascade of microRNA-424-5p (miR-424-5p), X-inactive-specific transcript (XIST) and O-GlcNAc transferase (OGT) in liver cancer.
33909326	3	50	theme	expressed	484:492	arg1	miRNAs					494:499	Differentially expressed miRNAs	469:499	Differentially expressed miRNAs	469:499	METHODS Differentially expressed miRNAs and target genes related to liver cancer were predicted by bioinformatics analyses, and their expression was determined in liver tissues of patients with liver cancer and liver cancer cells.
33909326	3	51	theme	liver	624:628	arg1	tissues					630:636	liver tissues	624:636	liver tissues of patients with liver cancer and liver cancer cells	624:689	METHODS Differentially expressed miRNAs and target genes related to liver cancer were predicted by bioinformatics analyses, and their expression was determined in liver tissues of patients with liver cancer and liver cancer cells.
33909326	3	52	theme	bioinformatics	560:573	arg1	analyses					575:582	bioinformatics analyses	560:582	bioinformatics analyses	560:582	METHODS Differentially expressed miRNAs and target genes related to liver cancer were predicted by bioinformatics analyses, and their expression was determined in liver tissues of patients with liver cancer and liver cancer cells.
33909326	11	53	theme	nude	1634:1637	arg1	mice					1639:1642	nude mice	1634:1642	nude mice	1634:1642	Furthermore, XIST knockdown inhibited tumour growth and metastasis in nude mice, while ectopic OGT reversed its effect.
33909326	2	54	theme	regulatory	323:332	arg1	cascade					334:340	the regulatory cascade	319:340	the regulatory cascade of microRNA-424-5p (miR-424-5p), X-inactive-specific transcript (XIST) and O-GlcNAc transferase (OGT) in liver cancer	319:458	In this study, we aimed to investigate the regulatory cascade of microRNA-424-5p (miR-424-5p), X-inactive-specific transcript (XIST) and O-GlcNAc transferase (OGT) in liver cancer.
33909326	0	55	theme	RAF1	54:57	arg1	glycosylation					59:71	RAF1 glycosylation	54:71	RAF1 glycosylation	54:71	The crosstalk network of XIST/miR-424-5p/OGT mediates RAF1 glycosylation and participates in the progression of liver cancer.
33909326	3	56	theme	liver	655:659	arg1	cancer					661:666	liver cancer	655:666	liver cancer	655:666	METHODS Differentially expressed miRNAs and target genes related to liver cancer were predicted by bioinformatics analyses, and their expression was determined in liver tissues of patients with liver cancer and liver cancer cells.
33909326	7	57	theme	poor	1166:1169	arg1	prognosis					1171:1179	poor prognosis	1166:1179	poor prognosis in patients with liver cancer	1166:1209	RESULTS XIST and OGT were up-regulated in liver cancer tissues and cells, responsible for poor prognosis in patients with liver cancer, while miR-424-5p was down-regulated.
33909326	1	58	theme	BACKGROUND	126:135	arg1	cancer					143:148	BACKGROUND Liver cancer	126:148	BACKGROUND Liver cancer	126:148	BACKGROUND Liver cancer is a major public health concern, but the mechanistic actions of biomarkers contributing to liver cancer remain to be determined.
33909326	1	58	theme	BACKGROUND	126:135	arg1	concern					175:181	a major public health concern	153:181	a major public health concern	153:181	BACKGROUND Liver cancer is a major public health concern, but the mechanistic actions of biomarkers contributing to liver cancer remain to be determined.
33909326	7	59	theme	cancer	1124:1129	arg1	tissues					1131:1137	liver cancer tissues	1118:1137	liver cancer tissues	1118:1137	RESULTS XIST and OGT were up-regulated in liver cancer tissues and cells, responsible for poor prognosis in patients with liver cancer, while miR-424-5p was down-regulated.
33909326	5	60	theme	axis	959:962	arg1	effects					924:930	the effects	920:930	the effects of the XIST/miR-424-5p/OGT axis on malignant phenotypes	920:986	Then, gain- and loss-of-function assays were conducted to evaluate the effects of the XIST/miR-424-5p/OGT axis on malignant phenotypes.
33909326	4	61	theme	reporter	761:768	arg1	assay					770:774	dual luciferase reporter assay	745:774	dual luciferase reporter assay	745:774	The RNA immunoprecipitation (RIP), RNA pull-down and dual luciferase reporter assay were used to examine the binding affinity among XIST and miR-424-5p and OGT.
33909326	1	62	theme	Liver	137:141	arg1	cancer					143:148	BACKGROUND Liver cancer	126:148	BACKGROUND Liver cancer	126:148	BACKGROUND Liver cancer is a major public health concern, but the mechanistic actions of biomarkers contributing to liver cancer remain to be determined.
33909326	1	62	theme	Liver	137:141	arg1	concern					175:181	a major public health concern	153:181	a major public health concern	153:181	BACKGROUND Liver cancer is a major public health concern, but the mechanistic actions of biomarkers contributing to liver cancer remain to be determined.
33909326	9	63	theme	liver	1365:1369	arg1	cells					1378:1382	liver cancer cells	1365:1382	liver cancer cells	1365:1382	XIST silencing inhibited malignant phenotypes of liver cancer cells, while miR-424-5p down-regulation negated its effect.
33909326	1	64	theme	biomarkers	215:224	arg1	actions					204:210	the mechanistic actions	188:210	the mechanistic actions of biomarkers contributing to liver cancer	188:253	BACKGROUND Liver cancer is a major public health concern, but the mechanistic actions of biomarkers contributing to liver cancer remain to be determined.
33909326	5	65	theme	XIST/miR-424-5p/OGT	939:957	arg1	axis					959:962	the XIST/miR-424-5p/OGT axis	935:962	the XIST/miR-424-5p/OGT axis	935:962	Then, gain- and loss-of-function assays were conducted to evaluate the effects of the XIST/miR-424-5p/OGT axis on malignant phenotypes.
33909326	3	66	theme	patients	641:648	arg1	tissues					630:636	liver tissues	624:636	liver tissues of patients with liver cancer and liver cancer cells	624:689	METHODS Differentially expressed miRNAs and target genes related to liver cancer were predicted by bioinformatics analyses, and their expression was determined in liver tissues of patients with liver cancer and liver cancer cells.
33909326	4	67	theme	luciferase	750:759	arg1	assay					770:774	dual luciferase reporter assay	745:774	dual luciferase reporter assay	745:774	The RNA immunoprecipitation (RIP), RNA pull-down and dual luciferase reporter assay were used to examine the binding affinity among XIST and miR-424-5p and OGT.
33909326	12	68	theme	liver	1831:1835	arg1	cancer					1837:1842	liver cancer	1831:1842	liver cancer	1831:1842	CONCLUSION These results reveal a novel mechanism by which the interaction of XIST/miR-424-5p/OGT participates in the malignancy and metastasis of liver cancer.
33909326	3	69	theme	target	505:510	arg1	genes					512:516	target genes	505:516	target genes related to liver cancer	505:540	METHODS Differentially expressed miRNAs and target genes related to liver cancer were predicted by bioinformatics analyses, and their expression was determined in liver tissues of patients with liver cancer and liver cancer cells.
33909326	8	70	theme	OGT	1300:1302	arg1	expression					1304:1313	OGT expression	1300:1313	OGT expression	1300:1313	XIST competitively bound to miR-424-5p to increase OGT expression.
33909326	6	71	theme	nude	991:994	arg1	model					1002:1006	A nude mouse model	989:1006	A nude mouse model of liver cancer	989:1022	A nude mouse model of liver cancer was further established for in vivo substantiation.
33909326	12	72	theme	novel	1718:1722	arg1	mechanism					1724:1732	a novel mechanism	1716:1732	a novel mechanism by which the interaction of XIST/miR-424-5p/OGT participates in the malignancy and metastasis of liver cancer	1716:1842	CONCLUSION These results reveal a novel mechanism by which the interaction of XIST/miR-424-5p/OGT participates in the malignancy and metastasis of liver cancer.
33909326	5	73	theme	malignant	967:975	arg1	phenotypes					977:986	malignant phenotypes	967:986	malignant phenotypes	967:986	Then, gain- and loss-of-function assays were conducted to evaluate the effects of the XIST/miR-424-5p/OGT axis on malignant phenotypes.
33909326	11	74	theme	ectopic	1651:1657	arg1	OGT					1659:1661	ectopic OGT	1651:1661	ectopic OGT	1651:1661	Furthermore, XIST knockdown inhibited tumour growth and metastasis in nude mice, while ectopic OGT reversed its effect.
33909326	9	75	theme	cells	1378:1382	arg1	phenotypes					1351:1360	malignant phenotypes	1341:1360	malignant phenotypes of liver cancer cells	1341:1382	XIST silencing inhibited malignant phenotypes of liver cancer cells, while miR-424-5p down-regulation negated its effect.
33909326	3	76	theme	cancer	678:683	arg1	cells					685:689	liver cancer cells	672:689	liver cancer cells	672:689	METHODS Differentially expressed miRNAs and target genes related to liver cancer were predicted by bioinformatics analyses, and their expression was determined in liver tissues of patients with liver cancer and liver cancer cells.
33909326	12	77	dep	CONCLUSION	1684:1693	arg1	reveal					1709:1714	reveal	1709:1714	reveal a novel mechanism by which the interaction of XIST/miR-424-5p/OGT participates in the malignancy and metastasis of liver cancer	1709:1842	CONCLUSION These results reveal a novel mechanism by which the interaction of XIST/miR-424-5p/OGT participates in the malignancy and metastasis of liver cancer.
33909326	2	78	theme	microRNA-424-5p	345:359	arg1	cascade					334:340	the regulatory cascade	319:340	the regulatory cascade of microRNA-424-5p (miR-424-5p), X-inactive-specific transcript (XIST) and O-GlcNAc transferase (OGT) in liver cancer	319:458	In this study, we aimed to investigate the regulatory cascade of microRNA-424-5p (miR-424-5p), X-inactive-specific transcript (XIST) and O-GlcNAc transferase (OGT) in liver cancer.
33909326	7	79	theme	liver	1198:1202	arg1	cancer					1204:1209	liver cancer	1198:1209	liver cancer	1198:1209	RESULTS XIST and OGT were up-regulated in liver cancer tissues and cells, responsible for poor prognosis in patients with liver cancer, while miR-424-5p was down-regulated.
33909326	1	80	theme	liver	242:246	arg1	cancer					248:253	liver cancer	242:253	liver cancer	242:253	BACKGROUND Liver cancer is a major public health concern, but the mechanistic actions of biomarkers contributing to liver cancer remain to be determined.
14985449	0	0	theme	gel	101:103	arg1	electrophoresis					105:119	two-dimensional gel electrophoresis	85:119	two-dimensional gel electrophoresis	85:119	Identification of O-linked N-acetylglucosamine proteins in rat skeletal muscle using two-dimensional gel electrophoresis and mass spectrometry.
14985449	6	1	from	decrease	1202:1209	arg1	level					1227:1231	the O-GlcNAc level	1214:1231	the O-GlcNAc level	1214:1231	A decrease in the O-GlcNAc level was measured in the slow postural soleus muscle after 14-day hindlimb unloading, a model of functional atrophy characterized by a decrease in the force of contraction.
14985449	7	2	theme	important	1475:1483	arg1	system					1496:1501	an important regulation system	1472:1501	an important regulation system in skeletal muscle physiology	1472:1531	These results strongly suggest that O-GlcNAc modification may serve as an important regulation system in skeletal muscle physiology.
14985449	7	2	theme	important	1475:1483	arg1	modification					1446:1457	O-GlcNAc modification	1437:1457	O-GlcNAc modification	1437:1457	These results strongly suggest that O-GlcNAc modification may serve as an important regulation system in skeletal muscle physiology.
14985449	5	3	dep	proteins	1169:1176	arg1	iii					1152:1154	iii	1152:1154	iii	1152:1154	These proteins can be classified in three main classes: i) proteins implicated in the signal transduction and in the translocation between the cytoplasm and the nucleus or structural proteins, ii) proteins of the glycolytic pathway and energetic metabolism, and iii) contractile proteins (myosin heavy chain).
14985449	0	4	theme	two-dimensional	85:99	arg1	electrophoresis					105:119	two-dimensional gel electrophoresis	85:119	two-dimensional gel electrophoresis	85:119	Identification of O-linked N-acetylglucosamine proteins in rat skeletal muscle using two-dimensional gel electrophoresis and mass spectrometry.
14985449	5	5	dep	proteins	949:956	arg1	i					946:946	i	946:946	i	946:946	These proteins can be classified in three main classes: i) proteins implicated in the signal transduction and in the translocation between the cytoplasm and the nucleus or structural proteins, ii) proteins of the glycolytic pathway and energetic metabolism, and iii) contractile proteins (myosin heavy chain).
14985449	3	6	theme	proteins	772:779	arg1	identification					736:749	the identification	732:749	the identification of O-GlcNAc-modified proteins in skeletal muscle using a proteomic approach	732:825	Because muscular contraction is both dependent on glucose metabolism and is highly regulated by phosphorylation/dephosphorylation processes, we decided to investigate the identification of O-GlcNAc-modified proteins in skeletal muscle using a proteomic approach.
14985449	0	7	from	Identification	0:13	arg1	muscle					72:77	rat skeletal muscle	59:77	rat skeletal muscle	59:77	Identification of O-linked N-acetylglucosamine proteins in rat skeletal muscle using two-dimensional gel electrophoresis and mass spectrometry.
14985449	0	8	link	O-linked	18:25	arg1	proteins					47:54	O-linked N-acetylglucosamine proteins	18:54	O-linked N-acetylglucosamine proteins in rat skeletal muscle	18:77	Identification of O-linked N-acetylglucosamine proteins in rat skeletal muscle using two-dimensional gel electrophoresis and mass spectrometry.
14985449	3	9	from	proteins	772:779	arg1	muscle					793:798	skeletal muscle	784:798	skeletal muscle using a proteomic approach	784:825	Because muscular contraction is both dependent on glucose metabolism and is highly regulated by phosphorylation/dephosphorylation processes, we decided to investigate the identification of O-GlcNAc-modified proteins in skeletal muscle using a proteomic approach.
14985449	5	10	dep	proteins	1087:1094	arg1	ii					1083:1084	ii	1083:1084	ii	1083:1084	These proteins can be classified in three main classes: i) proteins implicated in the signal transduction and in the translocation between the cytoplasm and the nucleus or structural proteins, ii) proteins of the glycolytic pathway and energetic metabolism, and iii) contractile proteins (myosin heavy chain).
14985449	6	11	theme	soleus	1267:1272	arg1	muscle					1274:1279	the slow postural soleus muscle	1249:1279	the slow postural soleus muscle	1249:1279	A decrease in the O-GlcNAc level was measured in the slow postural soleus muscle after 14-day hindlimb unloading, a model of functional atrophy characterized by a decrease in the force of contraction.
14985449	7	12	theme	O-GlcNAc	1437:1444	arg1	system					1496:1501	an important regulation system	1472:1501	an important regulation system in skeletal muscle physiology	1472:1531	These results strongly suggest that O-GlcNAc modification may serve as an important regulation system in skeletal muscle physiology.
14985449	7	12	theme	O-GlcNAc	1437:1444	arg1	modification					1446:1457	O-GlcNAc modification	1437:1457	O-GlcNAc modification	1437:1457	These results strongly suggest that O-GlcNAc modification may serve as an important regulation system in skeletal muscle physiology.
14985449	1	13	theme	regulatory	195:204	arg1	modification					225:236	a regulatory post-translational modification	193:236	a regulatory post-translational modification of nucleo-cytoplasmic proteins that has a complex interplay with phosphorylation	193:317	O-linked N-acetylglucosaminylation (O-GlcNAc) is a regulatory post-translational modification of nucleo-cytoplasmic proteins that has a complex interplay with phosphorylation.
14985449	1	13	theme	regulatory	195:204	arg1	N-acetylglucosaminylation					153:177	O-linked N-acetylglucosaminylation	144:177	O-linked N-acetylglucosaminylation (O-GlcNAc)	144:188	O-linked N-acetylglucosaminylation (O-GlcNAc) is a regulatory post-translational modification of nucleo-cytoplasmic proteins that has a complex interplay with phosphorylation.
14985449	0	14	theme	mass	125:128	arg1	spectrometry					130:141	mass spectrometry	125:141	mass spectrometry	125:141	Identification of O-linked N-acetylglucosamine proteins in rat skeletal muscle using two-dimensional gel electrophoresis and mass spectrometry.
14985449	5	15	dep	classes	937:943	arg1	proteins					1169:1176	contractile proteins	1157:1176	iii) contractile proteins (myosin heavy chain)	1152:1197	These proteins can be classified in three main classes: i) proteins implicated in the signal transduction and in the translocation between the cytoplasm and the nucleus or structural proteins, ii) proteins of the glycolytic pathway and energetic metabolism, and iii) contractile proteins (myosin heavy chain).
14985449	5	15	dep	classes	937:943	arg1	proteins					1087:1094	proteins	1087:1094	ii) proteins of the glycolytic pathway and energetic metabolism	1083:1145	These proteins can be classified in three main classes: i) proteins implicated in the signal transduction and in the translocation between the cytoplasm and the nucleus or structural proteins, ii) proteins of the glycolytic pathway and energetic metabolism, and iii) contractile proteins (myosin heavy chain).
14985449	5	15	dep	classes	937:943	arg1	chain					1192:1196	myosin heavy chain	1179:1196	myosin heavy chain	1179:1196	These proteins can be classified in three main classes: i) proteins implicated in the signal transduction and in the translocation between the cytoplasm and the nucleus or structural proteins, ii) proteins of the glycolytic pathway and energetic metabolism, and iii) contractile proteins (myosin heavy chain).
14985449	5	15	dep	classes	937:943	arg1	proteins					1073:1080	structural proteins	1062:1080	structural proteins	1062:1080	These proteins can be classified in three main classes: i) proteins implicated in the signal transduction and in the translocation between the cytoplasm and the nucleus or structural proteins, ii) proteins of the glycolytic pathway and energetic metabolism, and iii) contractile proteins (myosin heavy chain).
14985449	5	15	dep	classes	937:943	arg1	proteins					949:956	proteins	949:956	proteins implicated in the signal transduction and in the translocation between the cytoplasm and the nucleus	949:1057	These proteins can be classified in three main classes: i) proteins implicated in the signal transduction and in the translocation between the cytoplasm and the nucleus or structural proteins, ii) proteins of the glycolytic pathway and energetic metabolism, and iii) contractile proteins (myosin heavy chain).
14985449	5	16	theme	structural	1062:1071	arg1	proteins					1073:1080	structural proteins	1062:1080	structural proteins	1062:1080	These proteins can be classified in three main classes: i) proteins implicated in the signal transduction and in the translocation between the cytoplasm and the nucleus or structural proteins, ii) proteins of the glycolytic pathway and energetic metabolism, and iii) contractile proteins (myosin heavy chain).
14985449	3	17	from	identification	736:749	arg1	muscle					793:798	skeletal muscle	784:798	skeletal muscle using a proteomic approach	784:825	Because muscular contraction is both dependent on glucose metabolism and is highly regulated by phosphorylation/dephosphorylation processes, we decided to investigate the identification of O-GlcNAc-modified proteins in skeletal muscle using a proteomic approach.
14985449	1	18	theme	post-translational	206:223	arg1	modification					225:236	a regulatory post-translational modification	193:236	a regulatory post-translational modification of nucleo-cytoplasmic proteins that has a complex interplay with phosphorylation	193:317	O-linked N-acetylglucosaminylation (O-GlcNAc) is a regulatory post-translational modification of nucleo-cytoplasmic proteins that has a complex interplay with phosphorylation.
14985449	1	18	theme	post-translational	206:223	arg1	N-acetylglucosaminylation					153:177	O-linked N-acetylglucosaminylation	144:177	O-linked N-acetylglucosaminylation (O-GlcNAc)	144:188	O-linked N-acetylglucosaminylation (O-GlcNAc) is a regulatory post-translational modification of nucleo-cytoplasmic proteins that has a complex interplay with phosphorylation.
14985449	2	19	theme	cellular	539:546	arg1	fate					548:551	the cellular fate	535:551	the cellular fate of glucose	535:562	O-GlcNAc has been described as a nutritional sensor, the level of UDP-GlcNAc that serves as a donor for the uridine diphospho-N-acetylglucosamine:polypeptide beta-N-acetyl-glucosaminyltransferase being regulated by the cellular fate of glucose.
14985449	0	20	from	proteins	47:54	arg1	muscle					72:77	rat skeletal muscle	59:77	rat skeletal muscle	59:77	Identification of O-linked N-acetylglucosamine proteins in rat skeletal muscle using two-dimensional gel electrophoresis and mass spectrometry.
14985449	3	21	theme	phosphorylation/dephosphorylation	661:693	arg1	processes					695:703	phosphorylation/dephosphorylation processes	661:703	phosphorylation/dephosphorylation processes	661:703	Because muscular contraction is both dependent on glucose metabolism and is highly regulated by phosphorylation/dephosphorylation processes, we decided to investigate the identification of O-GlcNAc-modified proteins in skeletal muscle using a proteomic approach.
14985449	6	22	from	decrease	1363:1370	arg1	force					1379:1383	the force	1375:1383	the force of contraction	1375:1398	A decrease in the O-GlcNAc level was measured in the slow postural soleus muscle after 14-day hindlimb unloading, a model of functional atrophy characterized by a decrease in the force of contraction.
14985449	6	23	theme	atrophy	1336:1342	arg1	unloading					1303:1311	14-day hindlimb unloading	1287:1311	14-day hindlimb unloading	1287:1311	A decrease in the O-GlcNAc level was measured in the slow postural soleus muscle after 14-day hindlimb unloading, a model of functional atrophy characterized by a decrease in the force of contraction.
14985449	6	23	theme	atrophy	1336:1342	arg1	model					1316:1320	a model	1314:1320	a model of functional atrophy characterized by a decrease in the force of contraction	1314:1398	A decrease in the O-GlcNAc level was measured in the slow postural soleus muscle after 14-day hindlimb unloading, a model of functional atrophy characterized by a decrease in the force of contraction.
14985449	2	24	dep	level	377:381	arg1	beta-N-acetyl-glucosaminyltransferase					478:514	polypeptide beta-N-acetyl-glucosaminyltransferase	466:514	the level of UDP-GlcNAc that serves as a donor for the uridine diphospho-N-acetylglucosamine:polypeptide beta-N-acetyl-glucosaminyltransferase being regulated by the cellular fate of glucose	373:562	O-GlcNAc has been described as a nutritional sensor, the level of UDP-GlcNAc that serves as a donor for the uridine diphospho-N-acetylglucosamine:polypeptide beta-N-acetyl-glucosaminyltransferase being regulated by the cellular fate of glucose.
14985449	5	25	theme	heavy	1186:1190	arg1	proteins					1169:1176	contractile proteins	1157:1176	iii) contractile proteins (myosin heavy chain)	1152:1197	These proteins can be classified in three main classes: i) proteins implicated in the signal transduction and in the translocation between the cytoplasm and the nucleus or structural proteins, ii) proteins of the glycolytic pathway and energetic metabolism, and iii) contractile proteins (myosin heavy chain).
14985449	5	25	theme	heavy	1186:1190	arg1	chain					1192:1196	myosin heavy chain	1179:1196	myosin heavy chain	1179:1196	These proteins can be classified in three main classes: i) proteins implicated in the signal transduction and in the translocation between the cytoplasm and the nucleus or structural proteins, ii) proteins of the glycolytic pathway and energetic metabolism, and iii) contractile proteins (myosin heavy chain).
14985449	0	26	theme	N-acetylglucosamine	27:45	arg1	proteins					47:54	O-linked N-acetylglucosamine proteins	18:54	O-linked N-acetylglucosamine proteins in rat skeletal muscle	18:77	Identification of O-linked N-acetylglucosamine proteins in rat skeletal muscle using two-dimensional gel electrophoresis and mass spectrometry.
14985449	7	27	theme	muscle	1515:1520	arg1	physiology					1522:1531	skeletal muscle physiology	1506:1531	skeletal muscle physiology	1506:1531	These results strongly suggest that O-GlcNAc modification may serve as an important regulation system in skeletal muscle physiology.
14985449	6	28	theme	functional	1325:1334	arg1	atrophy					1336:1342	functional atrophy	1325:1342	functional atrophy characterized by a decrease in the force of contraction	1325:1398	A decrease in the O-GlcNAc level was measured in the slow postural soleus muscle after 14-day hindlimb unloading, a model of functional atrophy characterized by a decrease in the force of contraction.
14985449	1	29	theme	nucleo-cytoplasmic	241:258	arg1	proteins					260:267	nucleo-cytoplasmic proteins	241:267	nucleo-cytoplasmic proteins	241:267	O-linked N-acetylglucosaminylation (O-GlcNAc) is a regulatory post-translational modification of nucleo-cytoplasmic proteins that has a complex interplay with phosphorylation.
14985449	0	30	theme	O-linked	18:25	arg1	proteins					47:54	O-linked N-acetylglucosamine proteins	18:54	O-linked N-acetylglucosamine proteins in rat skeletal muscle	18:77	Identification of O-linked N-acetylglucosamine proteins in rat skeletal muscle using two-dimensional gel electrophoresis and mass spectrometry.
14985449	5	31	theme	myosin	1179:1184	arg1	proteins					1169:1176	contractile proteins	1157:1176	iii) contractile proteins (myosin heavy chain)	1152:1197	These proteins can be classified in three main classes: i) proteins implicated in the signal transduction and in the translocation between the cytoplasm and the nucleus or structural proteins, ii) proteins of the glycolytic pathway and energetic metabolism, and iii) contractile proteins (myosin heavy chain).
14985449	5	31	theme	myosin	1179:1184	arg1	chain					1192:1196	myosin heavy chain	1179:1196	myosin heavy chain	1179:1196	These proteins can be classified in three main classes: i) proteins implicated in the signal transduction and in the translocation between the cytoplasm and the nucleus or structural proteins, ii) proteins of the glycolytic pathway and energetic metabolism, and iii) contractile proteins (myosin heavy chain).
14985449	2	32	theme	nutritional	353:363	arg1	sensor					365:370	a nutritional sensor	351:370	a nutritional sensor	351:370	O-GlcNAc has been described as a nutritional sensor, the level of UDP-GlcNAc that serves as a donor for the uridine diphospho-N-acetylglucosamine:polypeptide beta-N-acetyl-glucosaminyltransferase being regulated by the cellular fate of glucose.
14985449	2	32	theme	nutritional	353:363	arg1	level					377:381	the level	373:381	the level of UDP-GlcNAc that serves as a donor for the uridine diphospho-N-acetylglucosamine:polypeptide beta-N-acetyl-glucosaminyltransferase being regulated by the cellular fate of glucose	373:562	O-GlcNAc has been described as a nutritional sensor, the level of UDP-GlcNAc that serves as a donor for the uridine diphospho-N-acetylglucosamine:polypeptide beta-N-acetyl-glucosaminyltransferase being regulated by the cellular fate of glucose.
14985449	2	32	theme	nutritional	353:363	arg1	O-GlcNAc					320:327	O-GlcNAc	320:327	O-GlcNAc	320:327	O-GlcNAc has been described as a nutritional sensor, the level of UDP-GlcNAc that serves as a donor for the uridine diphospho-N-acetylglucosamine:polypeptide beta-N-acetyl-glucosaminyltransferase being regulated by the cellular fate of glucose.
14985449	7	33	theme	skeletal	1506:1513	arg1	physiology					1522:1531	skeletal muscle physiology	1506:1531	skeletal muscle physiology	1506:1531	These results strongly suggest that O-GlcNAc modification may serve as an important regulation system in skeletal muscle physiology.
14985449	1	34	theme	proteins	260:267	arg1	modification					225:236	a regulatory post-translational modification	193:236	a regulatory post-translational modification of nucleo-cytoplasmic proteins that has a complex interplay with phosphorylation	193:317	O-linked N-acetylglucosaminylation (O-GlcNAc) is a regulatory post-translational modification of nucleo-cytoplasmic proteins that has a complex interplay with phosphorylation.
14985449	1	34	theme	proteins	260:267	arg1	N-acetylglucosaminylation					153:177	O-linked N-acetylglucosaminylation	144:177	O-linked N-acetylglucosaminylation (O-GlcNAc)	144:188	O-linked N-acetylglucosaminylation (O-GlcNAc) is a regulatory post-translational modification of nucleo-cytoplasmic proteins that has a complex interplay with phosphorylation.
14985449	2	35	theme	UDP-GlcNAc	386:395	arg1	sensor					365:370	a nutritional sensor	351:370	a nutritional sensor	351:370	O-GlcNAc has been described as a nutritional sensor, the level of UDP-GlcNAc that serves as a donor for the uridine diphospho-N-acetylglucosamine:polypeptide beta-N-acetyl-glucosaminyltransferase being regulated by the cellular fate of glucose.
14985449	2	35	theme	UDP-GlcNAc	386:395	arg1	level					377:381	the level	373:381	the level of UDP-GlcNAc that serves as a donor for the uridine diphospho-N-acetylglucosamine:polypeptide beta-N-acetyl-glucosaminyltransferase being regulated by the cellular fate of glucose	373:562	O-GlcNAc has been described as a nutritional sensor, the level of UDP-GlcNAc that serves as a donor for the uridine diphospho-N-acetylglucosamine:polypeptide beta-N-acetyl-glucosaminyltransferase being regulated by the cellular fate of glucose.
14985449	2	35	theme	UDP-GlcNAc	386:395	arg1	donor					414:418	a donor	412:418	a donor for the uridine diphospho-N-acetylglucosamine	412:464	O-GlcNAc has been described as a nutritional sensor, the level of UDP-GlcNAc that serves as a donor for the uridine diphospho-N-acetylglucosamine:polypeptide beta-N-acetyl-glucosaminyltransferase being regulated by the cellular fate of glucose.
14985449	3	36	theme	skeletal	784:791	arg1	muscle					793:798	skeletal muscle	784:798	skeletal muscle using a proteomic approach	784:825	Because muscular contraction is both dependent on glucose metabolism and is highly regulated by phosphorylation/dephosphorylation processes, we decided to investigate the identification of O-GlcNAc-modified proteins in skeletal muscle using a proteomic approach.
14985449	5	37	theme	metabolism	1136:1145	arg1	proteins					1169:1176	contractile proteins	1157:1176	iii) contractile proteins (myosin heavy chain)	1152:1197	These proteins can be classified in three main classes: i) proteins implicated in the signal transduction and in the translocation between the cytoplasm and the nucleus or structural proteins, ii) proteins of the glycolytic pathway and energetic metabolism, and iii) contractile proteins (myosin heavy chain).
14985449	5	37	theme	metabolism	1136:1145	arg1	proteins					1087:1094	proteins	1087:1094	ii) proteins of the glycolytic pathway and energetic metabolism	1083:1145	These proteins can be classified in three main classes: i) proteins implicated in the signal transduction and in the translocation between the cytoplasm and the nucleus or structural proteins, ii) proteins of the glycolytic pathway and energetic metabolism, and iii) contractile proteins (myosin heavy chain).
14985449	5	37	theme	metabolism	1136:1145	arg1	chain					1192:1196	myosin heavy chain	1179:1196	myosin heavy chain	1179:1196	These proteins can be classified in three main classes: i) proteins implicated in the signal transduction and in the translocation between the cytoplasm and the nucleus or structural proteins, ii) proteins of the glycolytic pathway and energetic metabolism, and iii) contractile proteins (myosin heavy chain).
14985449	5	37	theme	metabolism	1136:1145	arg1	proteins					1073:1080	structural proteins	1062:1080	structural proteins	1062:1080	These proteins can be classified in three main classes: i) proteins implicated in the signal transduction and in the translocation between the cytoplasm and the nucleus or structural proteins, ii) proteins of the glycolytic pathway and energetic metabolism, and iii) contractile proteins (myosin heavy chain).
14985449	5	37	theme	metabolism	1136:1145	arg1	proteins					949:956	proteins	949:956	proteins implicated in the signal transduction and in the translocation between the cytoplasm and the nucleus	949:1057	These proteins can be classified in three main classes: i) proteins implicated in the signal transduction and in the translocation between the cytoplasm and the nucleus or structural proteins, ii) proteins of the glycolytic pathway and energetic metabolism, and iii) contractile proteins (myosin heavy chain).
14985449	2	38	theme	polypeptide	466:476	arg1	beta-N-acetyl-glucosaminyltransferase					478:514	polypeptide beta-N-acetyl-glucosaminyltransferase	466:514	the level of UDP-GlcNAc that serves as a donor for the uridine diphospho-N-acetylglucosamine:polypeptide beta-N-acetyl-glucosaminyltransferase being regulated by the cellular fate of glucose	373:562	O-GlcNAc has been described as a nutritional sensor, the level of UDP-GlcNAc that serves as a donor for the uridine diphospho-N-acetylglucosamine:polypeptide beta-N-acetyl-glucosaminyltransferase being regulated by the cellular fate of glucose.
14985449	0	39	theme	proteins	47:54	arg1	Identification					0:13	Identification	0:13	Identification of O-linked N-acetylglucosamine proteins in rat skeletal muscle	0:77	Identification of O-linked N-acetylglucosamine proteins in rat skeletal muscle using two-dimensional gel electrophoresis and mass spectrometry.
14985449	2	40	theme	glucose	556:562	arg1	fate					548:551	the cellular fate	535:551	the cellular fate of glucose	535:562	O-GlcNAc has been described as a nutritional sensor, the level of UDP-GlcNAc that serves as a donor for the uridine diphospho-N-acetylglucosamine:polypeptide beta-N-acetyl-glucosaminyltransferase being regulated by the cellular fate of glucose.
14985449	3	41	theme	O-GlcNAc-modified	754:770	arg1	proteins					772:779	O-GlcNAc-modified proteins	754:779	O-GlcNAc-modified proteins in skeletal muscle using a proteomic approach	754:825	Because muscular contraction is both dependent on glucose metabolism and is highly regulated by phosphorylation/dephosphorylation processes, we decided to investigate the identification of O-GlcNAc-modified proteins in skeletal muscle using a proteomic approach.
14985449	7	42	theme	regulation	1485:1494	arg1	system					1496:1501	an important regulation system	1472:1501	an important regulation system in skeletal muscle physiology	1472:1531	These results strongly suggest that O-GlcNAc modification may serve as an important regulation system in skeletal muscle physiology.
14985449	7	42	theme	regulation	1485:1494	arg1	modification					1446:1457	O-GlcNAc modification	1437:1457	O-GlcNAc modification	1437:1457	These results strongly suggest that O-GlcNAc modification may serve as an important regulation system in skeletal muscle physiology.
14985449	5	43	theme	signal	976:981	arg1	transduction					983:994	the signal transduction	972:994	the signal transduction	972:994	These proteins can be classified in three main classes: i) proteins implicated in the signal transduction and in the translocation between the cytoplasm and the nucleus or structural proteins, ii) proteins of the glycolytic pathway and energetic metabolism, and iii) contractile proteins (myosin heavy chain).
14985449	0	44	theme	skeletal	63:70	arg1	muscle					72:77	rat skeletal muscle	59:77	rat skeletal muscle	59:77	Identification of O-linked N-acetylglucosamine proteins in rat skeletal muscle using two-dimensional gel electrophoresis and mass spectrometry.
14985449	0	45	from	muscle	72:77	arg1	Identification					0:13	Identification	0:13	Identification of O-linked N-acetylglucosamine proteins in rat skeletal muscle	0:77	Identification of O-linked N-acetylglucosamine proteins in rat skeletal muscle using two-dimensional gel electrophoresis and mass spectrometry.
14985449	0	46	theme	rat	59:61	arg1	muscle					72:77	rat skeletal muscle	59:77	rat skeletal muscle	59:77	Identification of O-linked N-acetylglucosamine proteins in rat skeletal muscle using two-dimensional gel electrophoresis and mass spectrometry.
14985449	1	47	contain	has	274:276	arg1	modification					225:236	a regulatory post-translational modification	193:236	a regulatory post-translational modification of nucleo-cytoplasmic proteins that has a complex interplay with phosphorylation	193:317	O-linked N-acetylglucosaminylation (O-GlcNAc) is a regulatory post-translational modification of nucleo-cytoplasmic proteins that has a complex interplay with phosphorylation.
14985449	1	47	contain	has	274:276	arg1	N-acetylglucosaminylation					153:177	O-linked N-acetylglucosaminylation	144:177	O-linked N-acetylglucosaminylation (O-GlcNAc)	144:188	O-linked N-acetylglucosaminylation (O-GlcNAc) is a regulatory post-translational modification of nucleo-cytoplasmic proteins that has a complex interplay with phosphorylation.
14985449	1	47	contain	has	274:276	arg2	interplay					288:296	a complex interplay	278:296	a complex interplay with phosphorylation	278:317	O-linked N-acetylglucosaminylation (O-GlcNAc) is a regulatory post-translational modification of nucleo-cytoplasmic proteins that has a complex interplay with phosphorylation.
14985449	5	48	theme	contractile	1157:1167	arg1	proteins					1169:1176	contractile proteins	1157:1176	iii) contractile proteins (myosin heavy chain)	1152:1197	These proteins can be classified in three main classes: i) proteins implicated in the signal transduction and in the translocation between the cytoplasm and the nucleus or structural proteins, ii) proteins of the glycolytic pathway and energetic metabolism, and iii) contractile proteins (myosin heavy chain).
14985449	5	48	theme	contractile	1157:1167	arg1	chain					1192:1196	myosin heavy chain	1179:1196	myosin heavy chain	1179:1196	These proteins can be classified in three main classes: i) proteins implicated in the signal transduction and in the translocation between the cytoplasm and the nucleus or structural proteins, ii) proteins of the glycolytic pathway and energetic metabolism, and iii) contractile proteins (myosin heavy chain).
14985449	1	49	theme	O-linked	144:151	arg1	N-acetylglucosaminylation					153:177	O-linked N-acetylglucosaminylation	144:177	O-linked N-acetylglucosaminylation (O-GlcNAc)	144:188	O-linked N-acetylglucosaminylation (O-GlcNAc) is a regulatory post-translational modification of nucleo-cytoplasmic proteins that has a complex interplay with phosphorylation.
14985449	1	49	theme	O-linked	144:151	arg1	modification					225:236	a regulatory post-translational modification	193:236	a regulatory post-translational modification of nucleo-cytoplasmic proteins that has a complex interplay with phosphorylation	193:317	O-linked N-acetylglucosaminylation (O-GlcNAc) is a regulatory post-translational modification of nucleo-cytoplasmic proteins that has a complex interplay with phosphorylation.
14985449	1	49	theme	O-linked	144:151	arg1	O-GlcNAc					180:187	O-GlcNAc	180:187	O-GlcNAc	180:187	O-linked N-acetylglucosaminylation (O-GlcNAc) is a regulatory post-translational modification of nucleo-cytoplasmic proteins that has a complex interplay with phosphorylation.
14985449	7	50	from	system	1496:1501	arg1	physiology					1522:1531	skeletal muscle physiology	1506:1531	skeletal muscle physiology	1506:1531	These results strongly suggest that O-GlcNAc modification may serve as an important regulation system in skeletal muscle physiology.
14985449	6	51	theme	14-day	1287:1292	arg1	unloading					1303:1311	14-day hindlimb unloading	1287:1311	14-day hindlimb unloading	1287:1311	A decrease in the O-GlcNAc level was measured in the slow postural soleus muscle after 14-day hindlimb unloading, a model of functional atrophy characterized by a decrease in the force of contraction.
14985449	6	51	theme	14-day	1287:1292	arg1	model					1316:1320	a model	1314:1320	a model of functional atrophy characterized by a decrease in the force of contraction	1314:1398	A decrease in the O-GlcNAc level was measured in the slow postural soleus muscle after 14-day hindlimb unloading, a model of functional atrophy characterized by a decrease in the force of contraction.
14985449	6	52	theme	contraction	1388:1398	arg1	force					1379:1383	the force	1375:1383	the force of contraction	1375:1398	A decrease in the O-GlcNAc level was measured in the slow postural soleus muscle after 14-day hindlimb unloading, a model of functional atrophy characterized by a decrease in the force of contraction.
14985449	3	53	theme	proteomic	808:816	arg1	approach					818:825	a proteomic approach	806:825	a proteomic approach	806:825	Because muscular contraction is both dependent on glucose metabolism and is highly regulated by phosphorylation/dephosphorylation processes, we decided to investigate the identification of O-GlcNAc-modified proteins in skeletal muscle using a proteomic approach.
14985449	5	54	theme	glycolytic	1103:1112	arg1	pathway					1114:1120	the glycolytic pathway	1099:1120	the glycolytic pathway	1099:1120	These proteins can be classified in three main classes: i) proteins implicated in the signal transduction and in the translocation between the cytoplasm and the nucleus or structural proteins, ii) proteins of the glycolytic pathway and energetic metabolism, and iii) contractile proteins (myosin heavy chain).
14985449	6	55	theme	O-GlcNAc	1218:1225	arg1	level					1227:1231	the O-GlcNAc level	1214:1231	the O-GlcNAc level	1214:1231	A decrease in the O-GlcNAc level was measured in the slow postural soleus muscle after 14-day hindlimb unloading, a model of functional atrophy characterized by a decrease in the force of contraction.
14985449	1	56	link	O-linked	144:151	arg1	N-acetylglucosaminylation					153:177	O-linked N-acetylglucosaminylation	144:177	O-linked N-acetylglucosaminylation (O-GlcNAc)	144:188	O-linked N-acetylglucosaminylation (O-GlcNAc) is a regulatory post-translational modification of nucleo-cytoplasmic proteins that has a complex interplay with phosphorylation.
14985449	1	56	link	O-linked	144:151	arg1	modification					225:236	a regulatory post-translational modification	193:236	a regulatory post-translational modification of nucleo-cytoplasmic proteins that has a complex interplay with phosphorylation	193:317	O-linked N-acetylglucosaminylation (O-GlcNAc) is a regulatory post-translational modification of nucleo-cytoplasmic proteins that has a complex interplay with phosphorylation.
14985449	1	56	link	O-linked	144:151	arg1	O-GlcNAc					180:187	O-GlcNAc	180:187	O-GlcNAc	180:187	O-linked N-acetylglucosaminylation (O-GlcNAc) is a regulatory post-translational modification of nucleo-cytoplasmic proteins that has a complex interplay with phosphorylation.
14985449	5	57	theme	pathway	1114:1120	arg1	proteins					1169:1176	contractile proteins	1157:1176	iii) contractile proteins (myosin heavy chain)	1152:1197	These proteins can be classified in three main classes: i) proteins implicated in the signal transduction and in the translocation between the cytoplasm and the nucleus or structural proteins, ii) proteins of the glycolytic pathway and energetic metabolism, and iii) contractile proteins (myosin heavy chain).
14985449	5	57	theme	pathway	1114:1120	arg1	proteins					1087:1094	proteins	1087:1094	ii) proteins of the glycolytic pathway and energetic metabolism	1083:1145	These proteins can be classified in three main classes: i) proteins implicated in the signal transduction and in the translocation between the cytoplasm and the nucleus or structural proteins, ii) proteins of the glycolytic pathway and energetic metabolism, and iii) contractile proteins (myosin heavy chain).
14985449	5	57	theme	pathway	1114:1120	arg1	chain					1192:1196	myosin heavy chain	1179:1196	myosin heavy chain	1179:1196	These proteins can be classified in three main classes: i) proteins implicated in the signal transduction and in the translocation between the cytoplasm and the nucleus or structural proteins, ii) proteins of the glycolytic pathway and energetic metabolism, and iii) contractile proteins (myosin heavy chain).
14985449	5	57	theme	pathway	1114:1120	arg1	proteins					1073:1080	structural proteins	1062:1080	structural proteins	1062:1080	These proteins can be classified in three main classes: i) proteins implicated in the signal transduction and in the translocation between the cytoplasm and the nucleus or structural proteins, ii) proteins of the glycolytic pathway and energetic metabolism, and iii) contractile proteins (myosin heavy chain).
14985449	5	57	theme	pathway	1114:1120	arg1	proteins					949:956	proteins	949:956	proteins implicated in the signal transduction and in the translocation between the cytoplasm and the nucleus	949:1057	These proteins can be classified in three main classes: i) proteins implicated in the signal transduction and in the translocation between the cytoplasm and the nucleus or structural proteins, ii) proteins of the glycolytic pathway and energetic metabolism, and iii) contractile proteins (myosin heavy chain).
14985449	1	58	with	interplay	288:296	arg1	phosphorylation					303:317	phosphorylation	303:317	phosphorylation	303:317	O-linked N-acetylglucosaminylation (O-GlcNAc) is a regulatory post-translational modification of nucleo-cytoplasmic proteins that has a complex interplay with phosphorylation.
14985449	3	59	theme	muscular	573:580	arg1	contraction					582:592	muscular contraction	573:592	muscular contraction	573:592	Because muscular contraction is both dependent on glucose metabolism and is highly regulated by phosphorylation/dephosphorylation processes, we decided to investigate the identification of O-GlcNAc-modified proteins in skeletal muscle using a proteomic approach.
14985449	1	60	theme	complex	280:286	arg1	interplay					288:296	a complex interplay	278:296	a complex interplay with phosphorylation	278:317	O-linked N-acetylglucosaminylation (O-GlcNAc) is a regulatory post-translational modification of nucleo-cytoplasmic proteins that has a complex interplay with phosphorylation.
14985449	3	61	from	muscle	793:798	arg1	identification					736:749	the identification	732:749	the identification of O-GlcNAc-modified proteins in skeletal muscle using a proteomic approach	732:825	Because muscular contraction is both dependent on glucose metabolism and is highly regulated by phosphorylation/dephosphorylation processes, we decided to investigate the identification of O-GlcNAc-modified proteins in skeletal muscle using a proteomic approach.
14985449	6	62	theme	hindlimb	1294:1301	arg1	unloading					1303:1311	14-day hindlimb unloading	1287:1311	14-day hindlimb unloading	1287:1311	A decrease in the O-GlcNAc level was measured in the slow postural soleus muscle after 14-day hindlimb unloading, a model of functional atrophy characterized by a decrease in the force of contraction.
14985449	6	62	theme	hindlimb	1294:1301	arg1	model					1316:1320	a model	1314:1320	a model of functional atrophy characterized by a decrease in the force of contraction	1314:1398	A decrease in the O-GlcNAc level was measured in the slow postural soleus muscle after 14-day hindlimb unloading, a model of functional atrophy characterized by a decrease in the force of contraction.
14985449	6	63	theme	postural	1258:1265	arg1	muscle					1274:1279	the slow postural soleus muscle	1249:1279	the slow postural soleus muscle	1249:1279	A decrease in the O-GlcNAc level was measured in the slow postural soleus muscle after 14-day hindlimb unloading, a model of functional atrophy characterized by a decrease in the force of contraction.
14985449	6	64	theme	slow	1253:1256	arg1	muscle					1274:1279	the slow postural soleus muscle	1249:1279	the slow postural soleus muscle	1249:1279	A decrease in the O-GlcNAc level was measured in the slow postural soleus muscle after 14-day hindlimb unloading, a model of functional atrophy characterized by a decrease in the force of contraction.
14985449	2	65	theme	uridine	428:434	arg1	diphospho-N-acetylglucosamine					436:464	the uridine diphospho-N-acetylglucosamine	424:464	the uridine diphospho-N-acetylglucosamine	424:464	O-GlcNAc has been described as a nutritional sensor, the level of UDP-GlcNAc that serves as a donor for the uridine diphospho-N-acetylglucosamine:polypeptide beta-N-acetyl-glucosaminyltransferase being regulated by the cellular fate of glucose.
14985449	5	66	theme	main	932:935	arg1	classes					937:943	three main classes	926:943	three main classes: i) proteins implicated in the signal transduction and in the translocation between the cytoplasm and the nucleus or structural proteins, ii) proteins of the glycolytic pathway and energetic metabolism, and iii) contractile proteins (myosin heavy chain)	926:1197	These proteins can be classified in three main classes: i) proteins implicated in the signal transduction and in the translocation between the cytoplasm and the nucleus or structural proteins, ii) proteins of the glycolytic pathway and energetic metabolism, and iii) contractile proteins (myosin heavy chain).
14985449	5	67	theme	energetic	1126:1134	arg1	metabolism					1136:1145	energetic metabolism	1126:1145	energetic metabolism	1126:1145	These proteins can be classified in three main classes: i) proteins implicated in the signal transduction and in the translocation between the cytoplasm and the nucleus or structural proteins, ii) proteins of the glycolytic pathway and energetic metabolism, and iii) contractile proteins (myosin heavy chain).
14985449	3	68	theme	glucose	615:621	arg1	metabolism					623:632	glucose metabolism	615:632	glucose metabolism	615:632	Because muscular contraction is both dependent on glucose metabolism and is highly regulated by phosphorylation/dephosphorylation processes, we decided to investigate the identification of O-GlcNAc-modified proteins in skeletal muscle using a proteomic approach.
18369606	1	0	link	O-linked	92:99	arg1	beta-N-acetylglucosamine					101:124	O-linked beta-N-acetylglucosamine	92:124	The O-linked beta-N-acetylglucosamine (O-GlcNAc) modification	88:148	The O-linked beta-N-acetylglucosamine (O-GlcNAc) modification is an abundant post-translational modification in eukaryotic cells.
18369606	1	0	link	O-linked	92:99	arg1	O-GlcNAc					127:134	O-GlcNAc	127:134	O-GlcNAc	127:134	The O-linked beta-N-acetylglucosamine (O-GlcNAc) modification is an abundant post-translational modification in eukaryotic cells.
18369606	4	1	theme	alkyne	722:727	arg1	group					729:733	an azido or alkyne group	710:733	group	729:733	Here we report a strategy based on the 1,3-dipolar cycloaddition, called click chemistry, between unnatural N-acetylglucosamine (GlcNAc) analogues (substituted with an azido or alkyne group) and the corresponding biotinylated probe to specifically detect, enrich and identify O-GlcNAc-modified proteins.
18369606	3	2	theme	most	533:536	arg1	cases					538:542	most cases	533:542	most cases	533:542	However the exact link between O-GlcNAc-modified proteins and their function in cells is largely undefined for most cases.
18369606	1	3	from	modification	184:195	arg1	cells					211:215	eukaryotic cells	200:215	eukaryotic cells	200:215	The O-linked beta-N-acetylglucosamine (O-GlcNAc) modification is an abundant post-translational modification in eukaryotic cells.
18369606	2	4	theme	many	289:292	arg1	proteins					318:325	many nuclear and cytoplasmic proteins	289:325	many nuclear and cytoplasmic proteins	289:325	This dynamic glycosylation plays a fundamental role in the activity of many nuclear and cytoplasmic proteins and is associated with pathologies like type II diabetes, Alzheimer's disease or some cancers.
18369606	4	5	theme	click	618:622	arg1	chemistry					624:632	click chemistry	618:632	click chemistry	618:632	Here we report a strategy based on the 1,3-dipolar cycloaddition, called click chemistry, between unnatural N-acetylglucosamine (GlcNAc) analogues (substituted with an azido or alkyne group) and the corresponding biotinylated probe to specifically detect, enrich and identify O-GlcNAc-modified proteins.
18369606	4	6	theme	biotinylated	758:769	arg1	probe					771:775	the corresponding biotinylated probe	740:775	the corresponding biotinylated probe to specifically detect, enrich and identify O-GlcNAc-modified proteins	740:846	Here we report a strategy based on the 1,3-dipolar cycloaddition, called click chemistry, between unnatural N-acetylglucosamine (GlcNAc) analogues (substituted with an azido or alkyne group) and the corresponding biotinylated probe to specifically detect, enrich and identify O-GlcNAc-modified proteins.
18369606	2	7	theme	proteins	318:325	arg1	activity					277:284	the activity	273:284	the activity of many nuclear and cytoplasmic proteins	273:325	This dynamic glycosylation plays a fundamental role in the activity of many nuclear and cytoplasmic proteins and is associated with pathologies like type II diabetes, Alzheimer's disease or some cancers.
18369606	2	8	theme	cytoplasmic	306:316	arg1	proteins					318:325	many nuclear and cytoplasmic proteins	289:325	many nuclear and cytoplasmic proteins	289:325	This dynamic glycosylation plays a fundamental role in the activity of many nuclear and cytoplasmic proteins and is associated with pathologies like type II diabetes, Alzheimer's disease or some cancers.
18369606	6	9	theme	cellular	1115:1122	arg1	model					1124:1128	an MCF-7 cellular model	1106:1128	an MCF-7 cellular model	1106:1128	Thanks to the biotin probe, affinity purification on streptavidin beads allowed us to identify 32 O-GlcNAc-azido-tagged proteins by LC-MS/MS analysis in an MCF-7 cellular model, 14 of which were previously unreported.
18369606	1	10	theme	eukaryotic	200:209	arg1	cells					211:215	eukaryotic cells	200:215	eukaryotic cells	200:215	The O-linked beta-N-acetylglucosamine (O-GlcNAc) modification is an abundant post-translational modification in eukaryotic cells.
18369606	3	11	theme	exact	434:438	arg1	undefined					519:527	undefined	519:527	undefined	519:527	However the exact link between O-GlcNAc-modified proteins and their function in cells is largely undefined for most cases.
18369606	3	11	theme	exact	434:438	arg1	link					440:443	the exact link	430:443	the exact link between O-GlcNAc-modified proteins and their function in cells	430:506	However the exact link between O-GlcNAc-modified proteins and their function in cells is largely undefined for most cases.
18369606	6	12	theme	model	1124:1128	arg1	14					1131:1132	14	1131:1132	14	1131:1132	Thanks to the biotin probe, affinity purification on streptavidin beads allowed us to identify 32 O-GlcNAc-azido-tagged proteins by LC-MS/MS analysis in an MCF-7 cellular model, 14 of which were previously unreported.
18369606	6	12	theme	model	1124:1128	arg1	model					1124:1128	an MCF-7 cellular model	1106:1128	an MCF-7 cellular model	1106:1128	Thanks to the biotin probe, affinity purification on streptavidin beads allowed us to identify 32 O-GlcNAc-azido-tagged proteins by LC-MS/MS analysis in an MCF-7 cellular model, 14 of which were previously unreported.
18369606	7	13	theme	click-chemistry-based	1208:1228	arg1	strategy					1230:1237	the click-chemistry-based strategy	1204:1237	the click-chemistry-based strategy combined with a proteomic approach to get further insight into the pattern of O-GlcNAc-modified proteins and the biological significance of this post-translational modification	1204:1414	This work illustrates the use of the click-chemistry-based strategy combined with a proteomic approach to get further insight into the pattern of O-GlcNAc-modified proteins and the biological significance of this post-translational modification.
18369606	1	14	theme	O-linked	92:99	arg1	beta-N-acetylglucosamine					101:124	O-linked beta-N-acetylglucosamine	92:124	The O-linked beta-N-acetylglucosamine (O-GlcNAc) modification	88:148	The O-linked beta-N-acetylglucosamine (O-GlcNAc) modification is an abundant post-translational modification in eukaryotic cells.
18369606	1	14	theme	O-linked	92:99	arg1	O-GlcNAc					127:134	O-GlcNAc	127:134	O-GlcNAc	127:134	The O-linked beta-N-acetylglucosamine (O-GlcNAc) modification is an abundant post-translational modification in eukaryotic cells.
18369606	5	15	theme	GlcNAc	918:923	arg1	analogue					906:913	only azido analogue	895:913	only azido analogue of GlcNAc	895:923	This bio-orthogonal conjugation confirms that only azido analogue of GlcNAc is metabolized by the cell.
18369606	7	16	theme	strategy	1230:1237	arg1	use					1197:1199	the use	1193:1199	the use of the click-chemistry-based strategy combined with a proteomic approach to get further insight into the pattern of O-GlcNAc-modified proteins and the biological significance of this post-translational modification	1193:1414	This work illustrates the use of the click-chemistry-based strategy combined with a proteomic approach to get further insight into the pattern of O-GlcNAc-modified proteins and the biological significance of this post-translational modification.
18369606	1	17	theme	beta-N-acetylglucosamine	101:124	arg1	modification					184:195	an abundant post-translational modification	153:195	an abundant post-translational modification in eukaryotic cells	153:215	The O-linked beta-N-acetylglucosamine (O-GlcNAc) modification is an abundant post-translational modification in eukaryotic cells.
18369606	1	17	theme	beta-N-acetylglucosamine	101:124	arg1	modification					137:148	The O-linked beta-N-acetylglucosamine (O-GlcNAc) modification	88:148	The O-linked beta-N-acetylglucosamine (O-GlcNAc) modification	88:148	The O-linked beta-N-acetylglucosamine (O-GlcNAc) modification is an abundant post-translational modification in eukaryotic cells.
18369606	3	18	theme	O-GlcNAc-modified	453:469	arg1	proteins					471:478	O-GlcNAc-modified proteins	453:478	O-GlcNAc-modified proteins	453:478	However the exact link between O-GlcNAc-modified proteins and their function in cells is largely undefined for most cases.
18369606	5	19	theme	bio-orthogonal	854:867	arg1	conjugation					869:879	This bio-orthogonal conjugation	849:879	This bio-orthogonal conjugation	849:879	This bio-orthogonal conjugation confirms that only azido analogue of GlcNAc is metabolized by the cell.
18369606	4	20	theme	corresponding	744:756	arg1	probe					771:775	the corresponding biotinylated probe	740:775	the corresponding biotinylated probe to specifically detect, enrich and identify O-GlcNAc-modified proteins	740:846	Here we report a strategy based on the 1,3-dipolar cycloaddition, called click chemistry, between unnatural N-acetylglucosamine (GlcNAc) analogues (substituted with an azido or alkyne group) and the corresponding biotinylated probe to specifically detect, enrich and identify O-GlcNAc-modified proteins.
18369606	0	21	theme	new	18:20	arg1	proteins					40:47	new O-GlcNAc modified proteins	18:47	new O-GlcNAc modified proteins	18:47	Identification of new O-GlcNAc modified proteins using a click-chemistry-based tagging.
18369606	4	22	theme	1,3-dipolar	584:594	arg1	cycloaddition					596:608	the 1,3-dipolar cycloaddition	580:608	the 1,3-dipolar cycloaddition	580:608	Here we report a strategy based on the 1,3-dipolar cycloaddition, called click chemistry, between unnatural N-acetylglucosamine (GlcNAc) analogues (substituted with an azido or alkyne group) and the corresponding biotinylated probe to specifically detect, enrich and identify O-GlcNAc-modified proteins.
18369606	6	23	from	purification	990:1001	arg1	beads					1019:1023	streptavidin beads	1006:1023	streptavidin beads	1006:1023	Thanks to the biotin probe, affinity purification on streptavidin beads allowed us to identify 32 O-GlcNAc-azido-tagged proteins by LC-MS/MS analysis in an MCF-7 cellular model, 14 of which were previously unreported.
18369606	4	24	theme	N-acetylglucosamine	653:671	arg1	analogues					682:690	unnatural N-acetylglucosamine (GlcNAc) analogues	643:690	unnatural N-acetylglucosamine (GlcNAc) analogues (substituted with an azido or alkyne group)	643:734	Here we report a strategy based on the 1,3-dipolar cycloaddition, called click chemistry, between unnatural N-acetylglucosamine (GlcNAc) analogues (substituted with an azido or alkyne group) and the corresponding biotinylated probe to specifically detect, enrich and identify O-GlcNAc-modified proteins.
18369606	0	25	theme	proteins	40:47	arg1	Identification					0:13	Identification	0:13	Identification of new O-GlcNAc modified proteins	0:47	Identification of new O-GlcNAc modified proteins using a click-chemistry-based tagging.
18369606	7	26	theme	biological	1352:1361	arg1	significance					1363:1374	the biological significance	1348:1374	the biological significance of this post-translational modification	1348:1414	This work illustrates the use of the click-chemistry-based strategy combined with a proteomic approach to get further insight into the pattern of O-GlcNAc-modified proteins and the biological significance of this post-translational modification.
18369606	6	27	theme	MCF-7	1109:1113	arg1	model					1124:1128	an MCF-7 cellular model	1106:1128	an MCF-7 cellular model	1106:1128	Thanks to the biotin probe, affinity purification on streptavidin beads allowed us to identify 32 O-GlcNAc-azido-tagged proteins by LC-MS/MS analysis in an MCF-7 cellular model, 14 of which were previously unreported.
18369606	4	28	theme	azido	713:717	arg1	group					729:733	an azido or alkyne group	710:733	group	729:733	Here we report a strategy based on the 1,3-dipolar cycloaddition, called click chemistry, between unnatural N-acetylglucosamine (GlcNAc) analogues (substituted with an azido or alkyne group) and the corresponding biotinylated probe to specifically detect, enrich and identify O-GlcNAc-modified proteins.
18369606	6	29	theme	affinity	981:988	arg1	purification					990:1001	affinity purification	981:1001	affinity purification on streptavidin beads	981:1023	Thanks to the biotin probe, affinity purification on streptavidin beads allowed us to identify 32 O-GlcNAc-azido-tagged proteins by LC-MS/MS analysis in an MCF-7 cellular model, 14 of which were previously unreported.
18369606	7	30	theme	modification	1403:1414	arg1	significance					1363:1374	the biological significance	1348:1374	the biological significance of this post-translational modification	1348:1414	This work illustrates the use of the click-chemistry-based strategy combined with a proteomic approach to get further insight into the pattern of O-GlcNAc-modified proteins and the biological significance of this post-translational modification.
18369606	7	30	theme	modification	1403:1414	arg1	pattern					1306:1312	the pattern	1302:1312	the pattern of O-GlcNAc-modified proteins	1302:1342	This work illustrates the use of the click-chemistry-based strategy combined with a proteomic approach to get further insight into the pattern of O-GlcNAc-modified proteins and the biological significance of this post-translational modification.
18369606	6	31	theme	O-GlcNAc-azido-tagged	1051:1071	arg1	proteins					1073:1080	32 O-GlcNAc-azido-tagged proteins	1048:1080	32 O-GlcNAc-azido-tagged proteins	1048:1080	Thanks to the biotin probe, affinity purification on streptavidin beads allowed us to identify 32 O-GlcNAc-azido-tagged proteins by LC-MS/MS analysis in an MCF-7 cellular model, 14 of which were previously unreported.
18369606	5	32	theme	azido	900:904	arg1	analogue					906:913	only azido analogue	895:913	only azido analogue of GlcNAc	895:923	This bio-orthogonal conjugation confirms that only azido analogue of GlcNAc is metabolized by the cell.
18369606	6	33	theme	LC-MS/MS	1085:1092	arg1	analysis					1094:1101	LC-MS/MS analysis	1085:1101	LC-MS/MS analysis	1085:1101	Thanks to the biotin probe, affinity purification on streptavidin beads allowed us to identify 32 O-GlcNAc-azido-tagged proteins by LC-MS/MS analysis in an MCF-7 cellular model, 14 of which were previously unreported.
18369606	6	34	theme	streptavidin	1006:1017	arg1	beads					1019:1023	streptavidin beads	1006:1023	streptavidin beads	1006:1023	Thanks to the biotin probe, affinity purification on streptavidin beads allowed us to identify 32 O-GlcNAc-azido-tagged proteins by LC-MS/MS analysis in an MCF-7 cellular model, 14 of which were previously unreported.
18369606	3	35	from	function	490:497	arg1	cells					502:506	cells	502:506	cells	502:506	However the exact link between O-GlcNAc-modified proteins and their function in cells is largely undefined for most cases.
18369606	7	36	theme	proteins	1335:1342	arg1	significance					1363:1374	the biological significance	1348:1374	the biological significance of this post-translational modification	1348:1414	This work illustrates the use of the click-chemistry-based strategy combined with a proteomic approach to get further insight into the pattern of O-GlcNAc-modified proteins and the biological significance of this post-translational modification.
18369606	7	36	theme	proteins	1335:1342	arg1	pattern					1306:1312	the pattern	1302:1312	the pattern of O-GlcNAc-modified proteins	1302:1342	This work illustrates the use of the click-chemistry-based strategy combined with a proteomic approach to get further insight into the pattern of O-GlcNAc-modified proteins and the biological significance of this post-translational modification.
18369606	7	37	theme	post-translational	1384:1401	arg1	modification					1403:1414	this post-translational modification	1379:1414	this post-translational modification	1379:1414	This work illustrates the use of the click-chemistry-based strategy combined with a proteomic approach to get further insight into the pattern of O-GlcNAc-modified proteins and the biological significance of this post-translational modification.
18369606	2	38	theme	fundamental	253:263	arg1	role					265:268	a fundamental role	251:268	a fundamental role	251:268	This dynamic glycosylation plays a fundamental role in the activity of many nuclear and cytoplasmic proteins and is associated with pathologies like type II diabetes, Alzheimer's disease or some cancers.
18369606	6	39	theme	biotin	967:972	arg1	probe					974:978	the biotin probe	963:978	the biotin probe	963:978	Thanks to the biotin probe, affinity purification on streptavidin beads allowed us to identify 32 O-GlcNAc-azido-tagged proteins by LC-MS/MS analysis in an MCF-7 cellular model, 14 of which were previously unreported.
18369606	2	40	theme	nuclear	294:300	arg1	proteins					318:325	many nuclear and cytoplasmic proteins	289:325	many nuclear and cytoplasmic proteins	289:325	This dynamic glycosylation plays a fundamental role in the activity of many nuclear and cytoplasmic proteins and is associated with pathologies like type II diabetes, Alzheimer's disease or some cancers.
18369606	2	41	theme	type	367:370	arg1	diabetes					375:382	type II diabetes	367:382	type II diabetes	367:382	This dynamic glycosylation plays a fundamental role in the activity of many nuclear and cytoplasmic proteins and is associated with pathologies like type II diabetes, Alzheimer's disease or some cancers.
18369606	0	42	dep	new	18:20	arg1	modified					31:38	modified	31:38	modified	31:38	Identification of new O-GlcNAc modified proteins using a click-chemistry-based tagging.
18369606	7	43	theme	O-GlcNAc-modified	1317:1333	arg1	proteins					1335:1342	O-GlcNAc-modified proteins	1317:1342	O-GlcNAc-modified proteins	1317:1342	This work illustrates the use of the click-chemistry-based strategy combined with a proteomic approach to get further insight into the pattern of O-GlcNAc-modified proteins and the biological significance of this post-translational modification.
18369606	8	44	dep	[figure	1417:1423	arg1	see					1426:1428	see	1426:1428	see text	1426:1433	[figure: see text]
18369606	2	45	theme	dynamic	223:229	arg1	glycosylation					231:243	This dynamic glycosylation	218:243	This dynamic glycosylation	218:243	This dynamic glycosylation plays a fundamental role in the activity of many nuclear and cytoplasmic proteins and is associated with pathologies like type II diabetes, Alzheimer's disease or some cancers.
18369606	1	46	theme	abundant	156:163	arg1	modification					184:195	an abundant post-translational modification	153:195	an abundant post-translational modification in eukaryotic cells	153:215	The O-linked beta-N-acetylglucosamine (O-GlcNAc) modification is an abundant post-translational modification in eukaryotic cells.
18369606	1	46	theme	abundant	156:163	arg1	modification					137:148	The O-linked beta-N-acetylglucosamine (O-GlcNAc) modification	88:148	The O-linked beta-N-acetylglucosamine (O-GlcNAc) modification	88:148	The O-linked beta-N-acetylglucosamine (O-GlcNAc) modification is an abundant post-translational modification in eukaryotic cells.
18369606	7	47	theme	further	1281:1287	arg1	insight					1289:1295	further insight	1281:1295	further insight into the pattern of O-GlcNAc-modified proteins and the biological significance of this post-translational modification	1281:1414	This work illustrates the use of the click-chemistry-based strategy combined with a proteomic approach to get further insight into the pattern of O-GlcNAc-modified proteins and the biological significance of this post-translational modification.
18369606	4	48	theme	unnatural	643:651	arg1	GlcNAc					674:679	GlcNAc	674:679	GlcNAc	674:679	Here we report a strategy based on the 1,3-dipolar cycloaddition, called click chemistry, between unnatural N-acetylglucosamine (GlcNAc) analogues (substituted with an azido or alkyne group) and the corresponding biotinylated probe to specifically detect, enrich and identify O-GlcNAc-modified proteins.
18369606	4	48	theme	unnatural	643:651	arg1	N-acetylglucosamine					653:671	unnatural N-acetylglucosamine	643:671	unnatural N-acetylglucosamine (GlcNAc) analogues (substituted with an azido or alkyne group)	643:734	Here we report a strategy based on the 1,3-dipolar cycloaddition, called click chemistry, between unnatural N-acetylglucosamine (GlcNAc) analogues (substituted with an azido or alkyne group) and the corresponding biotinylated probe to specifically detect, enrich and identify O-GlcNAc-modified proteins.
18369606	0	49	theme	click-chemistry-based	57:77	arg1	tagging					79:85	a click-chemistry-based tagging	55:85	a click-chemistry-based tagging	55:85	Identification of new O-GlcNAc modified proteins using a click-chemistry-based tagging.
18369606	4	50	theme	O-GlcNAc-modified	821:837	arg1	proteins					839:846	O-GlcNAc-modified proteins	821:846	O-GlcNAc-modified proteins	821:846	Here we report a strategy based on the 1,3-dipolar cycloaddition, called click chemistry, between unnatural N-acetylglucosamine (GlcNAc) analogues (substituted with an azido or alkyne group) and the corresponding biotinylated probe to specifically detect, enrich and identify O-GlcNAc-modified proteins.
18369606	3	51	from	proteins	471:478	arg1	cells					502:506	cells	502:506	cells	502:506	However the exact link between O-GlcNAc-modified proteins and their function in cells is largely undefined for most cases.
18369606	1	52	theme	post-translational	165:182	arg1	modification					184:195	an abundant post-translational modification	153:195	an abundant post-translational modification in eukaryotic cells	153:215	The O-linked beta-N-acetylglucosamine (O-GlcNAc) modification is an abundant post-translational modification in eukaryotic cells.
18369606	1	52	theme	post-translational	165:182	arg1	modification					137:148	The O-linked beta-N-acetylglucosamine (O-GlcNAc) modification	88:148	The O-linked beta-N-acetylglucosamine (O-GlcNAc) modification	88:148	The O-linked beta-N-acetylglucosamine (O-GlcNAc) modification is an abundant post-translational modification in eukaryotic cells.
18369606	7	53	theme	proteomic	1255:1263	arg1	approach					1265:1272	a proteomic approach	1253:1272	a proteomic approach to get further insight into the pattern of O-GlcNAc-modified proteins and the biological significance of this post-translational modification	1253:1414	This work illustrates the use of the click-chemistry-based strategy combined with a proteomic approach to get further insight into the pattern of O-GlcNAc-modified proteins and the biological significance of this post-translational modification.
23332158	8	0	theme	A/E	1210:1212	arg1	pathogens					1214:1222	A/E pathogens	1210:1222	A/E pathogens	1210:1222	These data identify GAPDH as a TRAF2 signaling cofactor and reveal a virulence strategy employed by A/E pathogens to inhibit NF-κB-dependent host innate immune responses.
23332158	6	1	theme	NF-κB	1004:1008	arg1	activation					1010:1019	NF-κB activation	1004:1019	NF-κB activation	1004:1019	NleB-mediated GAPDH O-GlcNAcylation disrupts the TRAF2-GAPDH interaction to suppress TRAF2 polyubiquitination and NF-κB activation.
23332158	0	2	with	effector	18:25	arg1	activity					52:59	glycosyltransferase activity	32:59	glycosyltransferase activity	32:59	NleB, a bacterial effector with glycosyltransferase activity, targets GAPDH function to inhibit NF-κB activation.
23332158	2	3	theme	type	329:332	arg1	system					348:353	type III secretion system	329:353	a highly conserved type III secretion system effector of A/E pathogens	310:379	NleB, a highly conserved type III secretion system effector of A/E pathogens, suppresses NF-κB activation, but the underlying mechanisms are unknown.
23332158	0	4	theme	GAPDH	70:74	arg1	function					76:83	GAPDH function	70:83	GAPDH function	70:83	NleB, a bacterial effector with glycosyltransferase activity, targets GAPDH function to inhibit NF-κB activation.
23332158	2	5	theme	conserved	319:327	arg1	NleB					304:307	NleB	304:307	NleB	304:307	NleB, a highly conserved type III secretion system effector of A/E pathogens, suppresses NF-κB activation, but the underlying mechanisms are unknown.
23332158	2	5	theme	conserved	319:327	arg1	effector					355:362	a highly conserved type III secretion system effector	310:362	a highly conserved type III secretion system effector of A/E pathogens	310:379	NleB, a highly conserved type III secretion system effector of A/E pathogens, suppresses NF-κB activation, but the underlying mechanisms are unknown.
23332158	3	6	theme	enzyme	493:498	arg1	protein					572:578	an NleB-interacting protein	552:578	an NleB-interacting protein	552:578	We identified the mammalian glycolysis enzyme glyceraldehyde 3-phosphate dehydrogenase (GAPDH) as an NleB-interacting protein.
23332158	3	6	theme	enzyme	493:498	arg1	GAPDH					542:546	GAPDH	542:546	GAPDH	542:546	We identified the mammalian glycolysis enzyme glyceraldehyde 3-phosphate dehydrogenase (GAPDH) as an NleB-interacting protein.
23332158	3	6	theme	enzyme	493:498	arg1	dehydrogenase					527:539	the mammalian glycolysis enzyme glyceraldehyde 3-phosphate dehydrogenase	468:539	the mammalian glycolysis enzyme glyceraldehyde 3-phosphate dehydrogenase (GAPDH)	468:547	We identified the mammalian glycolysis enzyme glyceraldehyde 3-phosphate dehydrogenase (GAPDH) as an NleB-interacting protein.
23332158	4	7	theme	TRAF2	746:750	arg1	polyubiquitination					752:769	TRAF2 polyubiquitination	746:769	TRAF2 polyubiquitination	746:769	Further, we discovered that GAPDH interacts with the TNF receptor-associated factor 2 (TRAF2), a protein required for TNF-α-mediated NF-κB activation, and regulates TRAF2 polyubiquitination.
23332158	7	8	theme	NleB	1034:1037	arg1	activity					1055:1062	Eliminating NleB O-GlcNAcylation activity	1022:1062	Eliminating NleB O-GlcNAcylation activity	1022:1062	Eliminating NleB O-GlcNAcylation activity attenuates C. rodentium colonization of mice.
23332158	3	9	theme	mammalian	472:480	arg1	protein					572:578	an NleB-interacting protein	552:578	an NleB-interacting protein	552:578	We identified the mammalian glycolysis enzyme glyceraldehyde 3-phosphate dehydrogenase (GAPDH) as an NleB-interacting protein.
23332158	3	9	theme	mammalian	472:480	arg1	GAPDH					542:546	GAPDH	542:546	GAPDH	542:546	We identified the mammalian glycolysis enzyme glyceraldehyde 3-phosphate dehydrogenase (GAPDH) as an NleB-interacting protein.
23332158	3	9	theme	mammalian	472:480	arg1	dehydrogenase					527:539	the mammalian glycolysis enzyme glyceraldehyde 3-phosphate dehydrogenase	468:539	the mammalian glycolysis enzyme glyceraldehyde 3-phosphate dehydrogenase (GAPDH)	468:547	We identified the mammalian glycolysis enzyme glyceraldehyde 3-phosphate dehydrogenase (GAPDH) as an NleB-interacting protein.
23332158	8	10	theme	NF-κB-dependent	1235:1249	arg1	responses					1270:1278	NF-κB-dependent host innate immune responses	1235:1278	NF-κB-dependent host innate immune responses	1235:1278	These data identify GAPDH as a TRAF2 signaling cofactor and reveal a virulence strategy employed by A/E pathogens to inhibit NF-κB-dependent host innate immune responses.
23332158	6	11	theme	GAPDH	904:908	arg1	O-GlcNAcylation					910:924	NleB-mediated GAPDH O-GlcNAcylation	890:924	NleB-mediated GAPDH O-GlcNAcylation	890:924	NleB-mediated GAPDH O-GlcNAcylation disrupts the TRAF2-GAPDH interaction to suppress TRAF2 polyubiquitination and NF-κB activation.
23332158	3	12	theme	3-phosphate	515:525	arg1	protein					572:578	an NleB-interacting protein	552:578	an NleB-interacting protein	552:578	We identified the mammalian glycolysis enzyme glyceraldehyde 3-phosphate dehydrogenase (GAPDH) as an NleB-interacting protein.
23332158	3	12	theme	3-phosphate	515:525	arg1	GAPDH					542:546	GAPDH	542:546	GAPDH	542:546	We identified the mammalian glycolysis enzyme glyceraldehyde 3-phosphate dehydrogenase (GAPDH) as an NleB-interacting protein.
23332158	3	12	theme	3-phosphate	515:525	arg1	dehydrogenase					527:539	the mammalian glycolysis enzyme glyceraldehyde 3-phosphate dehydrogenase	468:539	the mammalian glycolysis enzyme glyceraldehyde 3-phosphate dehydrogenase (GAPDH)	468:547	We identified the mammalian glycolysis enzyme glyceraldehyde 3-phosphate dehydrogenase (GAPDH) as an NleB-interacting protein.
23332158	8	13	theme	immune	1263:1268	arg1	responses					1270:1278	NF-κB-dependent host innate immune responses	1235:1278	NF-κB-dependent host innate immune responses	1235:1278	These data identify GAPDH as a TRAF2 signaling cofactor and reveal a virulence strategy employed by A/E pathogens to inhibit NF-κB-dependent host innate immune responses.
23332158	2	14	theme	A/E	367:369	arg1	pathogens					371:379	A/E pathogens	367:379	A/E pathogens	367:379	NleB, a highly conserved type III secretion system effector of A/E pathogens, suppresses NF-κB activation, but the underlying mechanisms are unknown.
23332158	0	15	theme	NF-κB	96:100	arg1	activation					102:111	NF-κB activation	96:111	NF-κB activation	96:111	NleB, a bacterial effector with glycosyltransferase activity, targets GAPDH function to inhibit NF-κB activation.
23332158	6	16	theme	NleB-mediated	890:902	arg1	O-GlcNAcylation					910:924	NleB-mediated GAPDH O-GlcNAcylation	890:924	NleB-mediated GAPDH O-GlcNAcylation	890:924	NleB-mediated GAPDH O-GlcNAcylation disrupts the TRAF2-GAPDH interaction to suppress TRAF2 polyubiquitination and NF-κB activation.
23332158	4	17	theme	receptor-associated	638:656	arg1	factor					658:663	the TNF receptor-associated factor 2	630:665	the TNF receptor-associated factor 2 (TRAF2)	630:673	Further, we discovered that GAPDH interacts with the TNF receptor-associated factor 2 (TRAF2), a protein required for TNF-α-mediated NF-κB activation, and regulates TRAF2 polyubiquitination.
23332158	4	17	theme	receptor-associated	638:656	arg1	TRAF2					668:672	TRAF2	668:672	TRAF2	668:672	Further, we discovered that GAPDH interacts with the TNF receptor-associated factor 2 (TRAF2), a protein required for TNF-α-mediated NF-κB activation, and regulates TRAF2 polyubiquitination.
23332158	4	17	theme	receptor-associated	638:656	arg1	protein					678:684	a protein	676:684	a protein required for TNF-α-mediated NF-κB activation	676:729	Further, we discovered that GAPDH interacts with the TNF receptor-associated factor 2 (TRAF2), a protein required for TNF-α-mediated NF-κB activation, and regulates TRAF2 polyubiquitination.
23332158	8	18	theme	innate	1256:1261	arg1	responses					1270:1278	NF-κB-dependent host innate immune responses	1235:1278	NF-κB-dependent host innate immune responses	1235:1278	These data identify GAPDH as a TRAF2 signaling cofactor and reveal a virulence strategy employed by A/E pathogens to inhibit NF-κB-dependent host innate immune responses.
23332158	8	19	theme	host	1251:1254	arg1	responses					1270:1278	NF-κB-dependent host innate immune responses	1235:1278	NF-κB-dependent host innate immune responses	1235:1278	These data identify GAPDH as a TRAF2 signaling cofactor and reveal a virulence strategy employed by A/E pathogens to inhibit NF-κB-dependent host innate immune responses.
23332158	3	20	theme	NleB-interacting	555:570	arg1	protein					572:578	an NleB-interacting protein	552:578	an NleB-interacting protein	552:578	We identified the mammalian glycolysis enzyme glyceraldehyde 3-phosphate dehydrogenase (GAPDH) as an NleB-interacting protein.
23332158	3	20	theme	NleB-interacting	555:570	arg1	dehydrogenase					527:539	the mammalian glycolysis enzyme glyceraldehyde 3-phosphate dehydrogenase	468:539	the mammalian glycolysis enzyme glyceraldehyde 3-phosphate dehydrogenase (GAPDH)	468:547	We identified the mammalian glycolysis enzyme glyceraldehyde 3-phosphate dehydrogenase (GAPDH) as an NleB-interacting protein.
23332158	0	21	theme	glycosyltransferase	32:50	arg1	activity					52:59	glycosyltransferase activity	32:59	glycosyltransferase activity	32:59	NleB, a bacterial effector with glycosyltransferase activity, targets GAPDH function to inhibit NF-κB activation.
23332158	2	22	theme	system	348:353	arg1	NleB					304:307	NleB	304:307	NleB	304:307	NleB, a highly conserved type III secretion system effector of A/E pathogens, suppresses NF-κB activation, but the underlying mechanisms are unknown.
23332158	2	22	theme	system	348:353	arg1	effector					355:362	a highly conserved type III secretion system effector	310:362	a highly conserved type III secretion system effector of A/E pathogens	310:379	NleB, a highly conserved type III secretion system effector of A/E pathogens, suppresses NF-κB activation, but the underlying mechanisms are unknown.
23332158	0	23	theme	bacterial	8:16	arg1	NleB					0:3	NleB	0:3	NleB	0:3	NleB, a bacterial effector with glycosyltransferase activity, targets GAPDH function to inhibit NF-κB activation.
23332158	0	23	theme	bacterial	8:16	arg1	effector					18:25	a bacterial effector	6:25	a bacterial effector with glycosyltransferase activity	6:59	NleB, a bacterial effector with glycosyltransferase activity, targets GAPDH function to inhibit NF-κB activation.
23332158	8	24	theme	TRAF2	1141:1145	arg1	cofactor					1157:1164	a TRAF2 signaling cofactor	1139:1164	a TRAF2 signaling cofactor	1139:1164	These data identify GAPDH as a TRAF2 signaling cofactor and reveal a virulence strategy employed by A/E pathogens to inhibit NF-κB-dependent host innate immune responses.
23332158	8	24	theme	TRAF2	1141:1145	arg1	GAPDH					1130:1134	GAPDH	1130:1134	GAPDH	1130:1134	These data identify GAPDH as a TRAF2 signaling cofactor and reveal a virulence strategy employed by A/E pathogens to inhibit NF-κB-dependent host innate immune responses.
23332158	2	25	theme	NF-κB	393:397	arg1	activation					399:408	NF-κB activation	393:408	NF-κB activation	393:408	NleB, a highly conserved type III secretion system effector of A/E pathogens, suppresses NF-κB activation, but the underlying mechanisms are unknown.
23332158	4	26	theme	NF-κB	714:718	arg1	activation					720:729	TNF-α-mediated NF-κB activation	699:729	TNF-α-mediated NF-κB activation	699:729	Further, we discovered that GAPDH interacts with the TNF receptor-associated factor 2 (TRAF2), a protein required for TNF-α-mediated NF-κB activation, and regulates TRAF2 polyubiquitination.
23332158	1	27	theme	natural	258:264	arg1	rodentium					293:301	the natural mouse pathogen Citrobacter rodentium	254:301	the natural mouse pathogen Citrobacter rodentium	254:301	Modulation of NF-κB-dependent responses is critical to the success of attaching/effacing (A/E) human pathogenic E. coli (EPEC and EHEC) and the natural mouse pathogen Citrobacter rodentium.
23332158	1	28	dep	coli	229:232	arg1	EHEC					244:247	EHEC	244:247	EHEC	244:247	Modulation of NF-κB-dependent responses is critical to the success of attaching/effacing (A/E) human pathogenic E. coli (EPEC and EHEC) and the natural mouse pathogen Citrobacter rodentium.
23332158	1	28	dep	coli	229:232	arg1	EPEC					235:238	EPEC	235:238	EPEC	235:238	Modulation of NF-κB-dependent responses is critical to the success of attaching/effacing (A/E) human pathogenic E. coli (EPEC and EHEC) and the natural mouse pathogen Citrobacter rodentium.
23332158	3	29	theme	glycolysis	482:491	arg1	protein					572:578	an NleB-interacting protein	552:578	an NleB-interacting protein	552:578	We identified the mammalian glycolysis enzyme glyceraldehyde 3-phosphate dehydrogenase (GAPDH) as an NleB-interacting protein.
23332158	3	29	theme	glycolysis	482:491	arg1	GAPDH					542:546	GAPDH	542:546	GAPDH	542:546	We identified the mammalian glycolysis enzyme glyceraldehyde 3-phosphate dehydrogenase (GAPDH) as an NleB-interacting protein.
23332158	3	29	theme	glycolysis	482:491	arg1	dehydrogenase					527:539	the mammalian glycolysis enzyme glyceraldehyde 3-phosphate dehydrogenase	468:539	the mammalian glycolysis enzyme glyceraldehyde 3-phosphate dehydrogenase (GAPDH)	468:547	We identified the mammalian glycolysis enzyme glyceraldehyde 3-phosphate dehydrogenase (GAPDH) as an NleB-interacting protein.
23332158	6	30	theme	TRAF2-GAPDH	939:949	arg1	interaction					951:961	the TRAF2-GAPDH interaction	935:961	the TRAF2-GAPDH interaction to suppress TRAF2 polyubiquitination and NF-κB activation	935:1019	NleB-mediated GAPDH O-GlcNAcylation disrupts the TRAF2-GAPDH interaction to suppress TRAF2 polyubiquitination and NF-κB activation.
23332158	1	31	theme	responses	144:152	arg1	Modulation					114:123	Modulation	114:123	Modulation of NF-κB-dependent responses	114:152	Modulation of NF-κB-dependent responses is critical to the success of attaching/effacing (A/E) human pathogenic E. coli (EPEC and EHEC) and the natural mouse pathogen Citrobacter rodentium.
23332158	1	32	theme	mouse	266:270	arg1	rodentium					293:301	the natural mouse pathogen Citrobacter rodentium	254:301	the natural mouse pathogen Citrobacter rodentium	254:301	Modulation of NF-κB-dependent responses is critical to the success of attaching/effacing (A/E) human pathogenic E. coli (EPEC and EHEC) and the natural mouse pathogen Citrobacter rodentium.
23332158	5	33	theme	O-GlcNAc	847:854	arg1	NleB					790:793	NleB	790:793	NleB	790:793	During infection, NleB functions as a translocated N-acetyl-D-glucosamine (O-GlcNAc) transferase that modifies GAPDH.
23332158	5	33	theme	O-GlcNAc	847:854	arg1	transferase					857:867	a translocated N-acetyl-D-glucosamine (O-GlcNAc) transferase	808:867	a translocated N-acetyl-D-glucosamine (O-GlcNAc) transferase that modifies GAPDH	808:887	During infection, NleB functions as a translocated N-acetyl-D-glucosamine (O-GlcNAc) transferase that modifies GAPDH.
23332158	4	34	theme	TNF	634:636	arg1	factor					658:663	the TNF receptor-associated factor 2	630:665	the TNF receptor-associated factor 2 (TRAF2)	630:673	Further, we discovered that GAPDH interacts with the TNF receptor-associated factor 2 (TRAF2), a protein required for TNF-α-mediated NF-κB activation, and regulates TRAF2 polyubiquitination.
23332158	4	34	theme	TNF	634:636	arg1	TRAF2					668:672	TRAF2	668:672	TRAF2	668:672	Further, we discovered that GAPDH interacts with the TNF receptor-associated factor 2 (TRAF2), a protein required for TNF-α-mediated NF-κB activation, and regulates TRAF2 polyubiquitination.
23332158	4	34	theme	TNF	634:636	arg1	protein					678:684	a protein	676:684	a protein required for TNF-α-mediated NF-κB activation	676:729	Further, we discovered that GAPDH interacts with the TNF receptor-associated factor 2 (TRAF2), a protein required for TNF-α-mediated NF-κB activation, and regulates TRAF2 polyubiquitination.
23332158	1	35	theme	pathogen	272:279	arg1	rodentium					293:301	the natural mouse pathogen Citrobacter rodentium	254:301	the natural mouse pathogen Citrobacter rodentium	254:301	Modulation of NF-κB-dependent responses is critical to the success of attaching/effacing (A/E) human pathogenic E. coli (EPEC and EHEC) and the natural mouse pathogen Citrobacter rodentium.
23332158	8	36	theme	signaling	1147:1155	arg1	cofactor					1157:1164	a TRAF2 signaling cofactor	1139:1164	a TRAF2 signaling cofactor	1139:1164	These data identify GAPDH as a TRAF2 signaling cofactor and reveal a virulence strategy employed by A/E pathogens to inhibit NF-κB-dependent host innate immune responses.
23332158	8	36	theme	signaling	1147:1155	arg1	GAPDH					1130:1134	GAPDH	1130:1134	GAPDH	1130:1134	These data identify GAPDH as a TRAF2 signaling cofactor and reveal a virulence strategy employed by A/E pathogens to inhibit NF-κB-dependent host innate immune responses.
23332158	1	37	dep	attaching/effacing	184:201	arg1	A/E					204:206	A/E	204:206	A/E	204:206	Modulation of NF-κB-dependent responses is critical to the success of attaching/effacing (A/E) human pathogenic E. coli (EPEC and EHEC) and the natural mouse pathogen Citrobacter rodentium.
23332158	7	38	theme	rodentium	1078:1086	arg1	colonization					1088:1099	C. rodentium colonization	1075:1099	C. rodentium colonization of mice	1075:1107	Eliminating NleB O-GlcNAcylation activity attenuates C. rodentium colonization of mice.
23332158	2	39	theme	pathogens	371:379	arg1	NleB					304:307	NleB	304:307	NleB	304:307	NleB, a highly conserved type III secretion system effector of A/E pathogens, suppresses NF-κB activation, but the underlying mechanisms are unknown.
23332158	2	39	theme	pathogens	371:379	arg1	effector					355:362	a highly conserved type III secretion system effector	310:362	a highly conserved type III secretion system effector of A/E pathogens	310:379	NleB, a highly conserved type III secretion system effector of A/E pathogens, suppresses NF-κB activation, but the underlying mechanisms are unknown.
23332158	1	40	theme	Citrobacter	281:291	arg1	rodentium					293:301	the natural mouse pathogen Citrobacter rodentium	254:301	the natural mouse pathogen Citrobacter rodentium	254:301	Modulation of NF-κB-dependent responses is critical to the success of attaching/effacing (A/E) human pathogenic E. coli (EPEC and EHEC) and the natural mouse pathogen Citrobacter rodentium.
23332158	2	41	theme	underlying	419:428	arg1	mechanisms					430:439	the underlying mechanisms	415:439	the underlying mechanisms	415:439	NleB, a highly conserved type III secretion system effector of A/E pathogens, suppresses NF-κB activation, but the underlying mechanisms are unknown.
23332158	2	41	theme	underlying	419:428	arg1	unknown					445:451	unknown	445:451	unknown	445:451	NleB, a highly conserved type III secretion system effector of A/E pathogens, suppresses NF-κB activation, but the underlying mechanisms are unknown.
23332158	1	42	theme	rodentium	293:301	arg1	success					173:179	the success	169:179	the success of attaching/effacing (A/E) human pathogenic E. coli (EPEC and EHEC) and the natural mouse pathogen Citrobacter rodentium	169:301	Modulation of NF-κB-dependent responses is critical to the success of attaching/effacing (A/E) human pathogenic E. coli (EPEC and EHEC) and the natural mouse pathogen Citrobacter rodentium.
23332158	8	43	theme	virulence	1179:1187	arg1	strategy					1189:1196	a virulence strategy	1177:1196	a virulence strategy employed by A/E pathogens to inhibit NF-κB-dependent host innate immune responses	1177:1278	These data identify GAPDH as a TRAF2 signaling cofactor and reveal a virulence strategy employed by A/E pathogens to inhibit NF-κB-dependent host innate immune responses.
23332158	7	44	theme	C.	1075:1076	arg1	colonization					1088:1099	C. rodentium colonization	1075:1099	C. rodentium colonization of mice	1075:1107	Eliminating NleB O-GlcNAcylation activity attenuates C. rodentium colonization of mice.
23332158	4	45	theme	TNF-α-mediated	699:712	arg1	activation					720:729	TNF-α-mediated NF-κB activation	699:729	TNF-α-mediated NF-κB activation	699:729	Further, we discovered that GAPDH interacts with the TNF receptor-associated factor 2 (TRAF2), a protein required for TNF-α-mediated NF-κB activation, and regulates TRAF2 polyubiquitination.
23332158	7	46	theme	mice	1104:1107	arg1	colonization					1088:1099	C. rodentium colonization	1075:1099	C. rodentium colonization of mice	1075:1107	Eliminating NleB O-GlcNAcylation activity attenuates C. rodentium colonization of mice.
23332158	7	47	theme	O-GlcNAcylation	1039:1053	arg1	activity					1055:1062	Eliminating NleB O-GlcNAcylation activity	1022:1062	Eliminating NleB O-GlcNAcylation activity	1022:1062	Eliminating NleB O-GlcNAcylation activity attenuates C. rodentium colonization of mice.
23332158	1	48	theme	NF-κB-dependent	128:142	arg1	responses					144:152	NF-κB-dependent responses	128:152	NF-κB-dependent responses	128:152	Modulation of NF-κB-dependent responses is critical to the success of attaching/effacing (A/E) human pathogenic E. coli (EPEC and EHEC) and the natural mouse pathogen Citrobacter rodentium.
23332158	5	49	theme	N-acetyl-D-glucosamine	823:844	arg1	NleB					790:793	NleB	790:793	NleB	790:793	During infection, NleB functions as a translocated N-acetyl-D-glucosamine (O-GlcNAc) transferase that modifies GAPDH.
23332158	5	49	theme	N-acetyl-D-glucosamine	823:844	arg1	transferase					857:867	a translocated N-acetyl-D-glucosamine (O-GlcNAc) transferase	808:867	a translocated N-acetyl-D-glucosamine (O-GlcNAc) transferase that modifies GAPDH	808:887	During infection, NleB functions as a translocated N-acetyl-D-glucosamine (O-GlcNAc) transferase that modifies GAPDH.
23332158	2	50	theme	secretion	338:346	arg1	system					348:353	type III secretion system	329:353	a highly conserved type III secretion system effector of A/E pathogens	310:379	NleB, a highly conserved type III secretion system effector of A/E pathogens, suppresses NF-κB activation, but the underlying mechanisms are unknown.
23332158	1	51	theme	coli	229:232	arg1	success					173:179	the success	169:179	the success of attaching/effacing (A/E) human pathogenic E. coli (EPEC and EHEC) and the natural mouse pathogen Citrobacter rodentium	169:301	Modulation of NF-κB-dependent responses is critical to the success of attaching/effacing (A/E) human pathogenic E. coli (EPEC and EHEC) and the natural mouse pathogen Citrobacter rodentium.
23332158	5	52	theme	translocated	810:821	arg1	NleB					790:793	NleB	790:793	NleB	790:793	During infection, NleB functions as a translocated N-acetyl-D-glucosamine (O-GlcNAc) transferase that modifies GAPDH.
23332158	5	52	theme	translocated	810:821	arg1	transferase					857:867	a translocated N-acetyl-D-glucosamine (O-GlcNAc) transferase	808:867	a translocated N-acetyl-D-glucosamine (O-GlcNAc) transferase that modifies GAPDH	808:887	During infection, NleB functions as a translocated N-acetyl-D-glucosamine (O-GlcNAc) transferase that modifies GAPDH.
23332158	7	53	theme	Eliminating	1022:1032	arg1	activity					1055:1062	Eliminating NleB O-GlcNAcylation activity	1022:1062	Eliminating NleB O-GlcNAcylation activity	1022:1062	Eliminating NleB O-GlcNAcylation activity attenuates C. rodentium colonization of mice.
23332158	3	54	theme	glyceraldehyde	500:513	arg1	protein					572:578	an NleB-interacting protein	552:578	an NleB-interacting protein	552:578	We identified the mammalian glycolysis enzyme glyceraldehyde 3-phosphate dehydrogenase (GAPDH) as an NleB-interacting protein.
23332158	3	54	theme	glyceraldehyde	500:513	arg1	GAPDH					542:546	GAPDH	542:546	GAPDH	542:546	We identified the mammalian glycolysis enzyme glyceraldehyde 3-phosphate dehydrogenase (GAPDH) as an NleB-interacting protein.
23332158	3	54	theme	glyceraldehyde	500:513	arg1	dehydrogenase					527:539	the mammalian glycolysis enzyme glyceraldehyde 3-phosphate dehydrogenase	468:539	the mammalian glycolysis enzyme glyceraldehyde 3-phosphate dehydrogenase (GAPDH)	468:547	We identified the mammalian glycolysis enzyme glyceraldehyde 3-phosphate dehydrogenase (GAPDH) as an NleB-interacting protein.
23332158	6	55	theme	TRAF2	975:979	arg1	polyubiquitination					981:998	TRAF2 polyubiquitination	975:998	TRAF2 polyubiquitination	975:998	NleB-mediated GAPDH O-GlcNAcylation disrupts the TRAF2-GAPDH interaction to suppress TRAF2 polyubiquitination and NF-κB activation.
11019912	8	0	theme	human	1588:1592	arg1	MHC					1602:1604	human class I MHC	1588:1604	human class I MHC of glycopeptides carrying terminal O-GlcNAc residues in vivo	1588:1665	Together, these data provide further evidence for the natural presentation by human class I MHC of glycopeptides carrying terminal O-GlcNAc residues in vivo.
11019912	1	1	theme	class	433:437	arg1	molecules					480:488	class I major histocompatibility complex (MHC) molecules	433:488	class I major histocompatibility complex (MHC) molecules	433:488	Previously, using synthetic glycopeptides carrying a natural cytosolic type of monosaccharide O-beta-linked N-acetylglucosamine (GlcNAc) glycosylation of serine residues, we have shown that glycopeptides act as suitable substrates for TAP-mediated transport into the endoplasmic reticulum (ER), and that they bind efficiently to class I major histocompatibility complex (MHC) molecules and can elicit glycopeptide-specific cytotoxic T-lymphocyte (CTL) responses in mice.
11019912	8	2	theme	in	1659:1660	arg1	residues					1650:1657	terminal O-GlcNAc residues	1632:1657	terminal O-GlcNAc residues in vivo	1632:1665	Together, these data provide further evidence for the natural presentation by human class I MHC of glycopeptides carrying terminal O-GlcNAc residues in vivo.
11019912	8	3	gly	glycopeptides	1609:1621	arg2	glycopeptides					1609:1621	glycopeptides	1609:1621	glycopeptides carrying terminal O-GlcNAc residues in vivo	1609:1665	Together, these data provide further evidence for the natural presentation by human class I MHC of glycopeptides carrying terminal O-GlcNAc residues in vivo.
11019912	8	4	theme	I	1600:1600	arg1	MHC					1602:1604	human class I MHC	1588:1604	human class I MHC of glycopeptides carrying terminal O-GlcNAc residues in vivo	1588:1665	Together, these data provide further evidence for the natural presentation by human class I MHC of glycopeptides carrying terminal O-GlcNAc residues in vivo.
11019912	1	5	theme	major	441:445	arg1	molecules					480:488	class I major histocompatibility complex (MHC) molecules	433:488	class I major histocompatibility complex (MHC) molecules	433:488	Previously, using synthetic glycopeptides carrying a natural cytosolic type of monosaccharide O-beta-linked N-acetylglucosamine (GlcNAc) glycosylation of serine residues, we have shown that glycopeptides act as suitable substrates for TAP-mediated transport into the endoplasmic reticulum (ER), and that they bind efficiently to class I major histocompatibility complex (MHC) molecules and can elicit glycopeptide-specific cytotoxic T-lymphocyte (CTL) responses in mice.
11019912	2	6	theme	human	629:633	arg1	molecules					647:655	human class I MHC molecules	629:655	human class I MHC molecules	629:655	Recently, we have reported that peptides presented by human class I MHC molecules in vivo encompass a small but significant amount of peptides which seem to be carrying O-beta-linked monosaccharide GlcNAc.
11019912	1	7	contain	carrying	146:153	arg2	type					175:178	a natural cytosolic type	155:178	a natural cytosolic type of monosaccharide O-beta-linked N-acetylglucosamine (GlcNAc) glycosylation of serine residues	155:272	Previously, using synthetic glycopeptides carrying a natural cytosolic type of monosaccharide O-beta-linked N-acetylglucosamine (GlcNAc) glycosylation of serine residues, we have shown that glycopeptides act as suitable substrates for TAP-mediated transport into the endoplasmic reticulum (ER), and that they bind efficiently to class I major histocompatibility complex (MHC) molecules and can elicit glycopeptide-specific cytotoxic T-lymphocyte (CTL) responses in mice.
11019912	1	7	contain	carrying	146:153	arg1	glycopeptides					132:144	synthetic glycopeptides	122:144	synthetic glycopeptides carrying a natural cytosolic type of monosaccharide O-beta-linked N-acetylglucosamine (GlcNAc) glycosylation of serine residues	122:272	Previously, using synthetic glycopeptides carrying a natural cytosolic type of monosaccharide O-beta-linked N-acetylglucosamine (GlcNAc) glycosylation of serine residues, we have shown that glycopeptides act as suitable substrates for TAP-mediated transport into the endoplasmic reticulum (ER), and that they bind efficiently to class I major histocompatibility complex (MHC) molecules and can elicit glycopeptide-specific cytotoxic T-lymphocyte (CTL) responses in mice.
11019912	1	8	theme	complex	466:472	arg1	molecules					480:488	class I major histocompatibility complex (MHC) molecules	433:488	class I major histocompatibility complex (MHC) molecules	433:488	Previously, using synthetic glycopeptides carrying a natural cytosolic type of monosaccharide O-beta-linked N-acetylglucosamine (GlcNAc) glycosylation of serine residues, we have shown that glycopeptides act as suitable substrates for TAP-mediated transport into the endoplasmic reticulum (ER), and that they bind efficiently to class I major histocompatibility complex (MHC) molecules and can elicit glycopeptide-specific cytotoxic T-lymphocyte (CTL) responses in mice.
11019912	7	9	theme	*	1410:1410	arg1	peptides					1424:1431	the HLA-A*0201-derived peptides	1401:1431	the HLA-A*0201-derived peptides which bind to the WGA lectin	1401:1460	Furthermore, using an enzymatic labeling procedure we present evidence that the HLA-A*0201-derived peptides which bind to the WGA lectin are glycosylated with terminal GlcNAc residues.
11019912	1	10	theme	MHC	475:477	arg1	molecules					480:488	class I major histocompatibility complex (MHC) molecules	433:488	class I major histocompatibility complex (MHC) molecules	433:488	Previously, using synthetic glycopeptides carrying a natural cytosolic type of monosaccharide O-beta-linked N-acetylglucosamine (GlcNAc) glycosylation of serine residues, we have shown that glycopeptides act as suitable substrates for TAP-mediated transport into the endoplasmic reticulum (ER), and that they bind efficiently to class I major histocompatibility complex (MHC) molecules and can elicit glycopeptide-specific cytotoxic T-lymphocyte (CTL) responses in mice.
11019912	1	11	theme	monosaccharide	183:196	arg1	N-acetylglucosamine					212:230	monosaccharide O-beta-linked N-acetylglucosamine	183:230	monosaccharide O-beta-linked N-acetylglucosamine (GlcNAc) glycosylation of serine residues	183:272	Previously, using synthetic glycopeptides carrying a natural cytosolic type of monosaccharide O-beta-linked N-acetylglucosamine (GlcNAc) glycosylation of serine residues, we have shown that glycopeptides act as suitable substrates for TAP-mediated transport into the endoplasmic reticulum (ER), and that they bind efficiently to class I major histocompatibility complex (MHC) molecules and can elicit glycopeptide-specific cytotoxic T-lymphocyte (CTL) responses in mice.
11019912	1	11	theme	monosaccharide	183:196	arg1	GlcNAc					233:238	GlcNAc	233:238	GlcNAc	233:238	Previously, using synthetic glycopeptides carrying a natural cytosolic type of monosaccharide O-beta-linked N-acetylglucosamine (GlcNAc) glycosylation of serine residues, we have shown that glycopeptides act as suitable substrates for TAP-mediated transport into the endoplasmic reticulum (ER), and that they bind efficiently to class I major histocompatibility complex (MHC) molecules and can elicit glycopeptide-specific cytotoxic T-lymphocyte (CTL) responses in mice.
11019912	7	12	theme	enzymatic	1347:1355	arg1	procedure					1366:1374	an enzymatic labeling procedure	1344:1374	an enzymatic labeling procedure	1344:1374	Furthermore, using an enzymatic labeling procedure we present evidence that the HLA-A*0201-derived peptides which bind to the WGA lectin are glycosylated with terminal GlcNAc residues.
11019912	6	13	theme	HLA-A	1299:1303	arg1	0201					1305:1308	HLA-A*0201	1299:1308	a HLA-A*0201 binding motif	1297:1322	It was found that the peptides derived from HLA-A*0201 which had been retained by the O-GlcNAc-binding lectin WGA did indeed carry a HLA-A*0201 binding motif.
11019912	1	14	theme	N-acetylglucosamine	212:230	arg1	glycosylation					241:253	monosaccharide O-beta-linked N-acetylglucosamine (GlcNAc) glycosylation	183:253	monosaccharide O-beta-linked N-acetylglucosamine (GlcNAc) glycosylation of serine residues	183:272	Previously, using synthetic glycopeptides carrying a natural cytosolic type of monosaccharide O-beta-linked N-acetylglucosamine (GlcNAc) glycosylation of serine residues, we have shown that glycopeptides act as suitable substrates for TAP-mediated transport into the endoplasmic reticulum (ER), and that they bind efficiently to class I major histocompatibility complex (MHC) molecules and can elicit glycopeptide-specific cytotoxic T-lymphocyte (CTL) responses in mice.
11019912	2	15	link	O-beta-linked	744:756	arg1	GlcNAc					773:778	O-beta-linked monosaccharide GlcNAc	744:778	O-beta-linked monosaccharide GlcNAc	744:778	Recently, we have reported that peptides presented by human class I MHC molecules in vivo encompass a small but significant amount of peptides which seem to be carrying O-beta-linked monosaccharide GlcNAc.
11019912	6	16	theme	*	1215:1215	arg1	0201					1216:1219	HLA-A*0201	1210:1219	HLA-A*0201 which had been retained by the O-GlcNAc-binding lectin WGA	1210:1278	It was found that the peptides derived from HLA-A*0201 which had been retained by the O-GlcNAc-binding lectin WGA did indeed carry a HLA-A*0201 binding motif.
11019912	2	17	theme	monosaccharide	758:771	arg1	GlcNAc					773:778	O-beta-linked monosaccharide GlcNAc	744:778	O-beta-linked monosaccharide GlcNAc	744:778	Recently, we have reported that peptides presented by human class I MHC molecules in vivo encompass a small but significant amount of peptides which seem to be carrying O-beta-linked monosaccharide GlcNAc.
11019912	7	18	gly	glycosylated	1466:1477	arg1	peptides					1424:1431	the HLA-A*0201-derived peptides	1401:1431	the HLA-A*0201-derived peptides which bind to the WGA lectin	1401:1460	Furthermore, using an enzymatic labeling procedure we present evidence that the HLA-A*0201-derived peptides which bind to the WGA lectin are glycosylated with terminal GlcNAc residues.
11019912	2	19	theme	significant	687:697	arg1	peptides					709:716	peptides	709:716	peptides which seem to be carrying O-beta-linked monosaccharide GlcNAc	709:778	Recently, we have reported that peptides presented by human class I MHC molecules in vivo encompass a small but significant amount of peptides which seem to be carrying O-beta-linked monosaccharide GlcNAc.
11019912	2	19	theme	significant	687:697	arg1	amount					699:704	a small but significant amount	675:704	a small but significant amount of peptides which seem to be carrying O-beta-linked monosaccharide GlcNAc	675:778	Recently, we have reported that peptides presented by human class I MHC molecules in vivo encompass a small but significant amount of peptides which seem to be carrying O-beta-linked monosaccharide GlcNAc.
11019912	6	20	attach	derived	1197:1203	arg1	0201					1216:1219	HLA-A*0201	1210:1219	HLA-A*0201 which had been retained by the O-GlcNAc-binding lectin WGA	1210:1278	It was found that the peptides derived from HLA-A*0201 which had been retained by the O-GlcNAc-binding lectin WGA did indeed carry a HLA-A*0201 binding motif.
11019912	6	20	attach	derived	1197:1203	arg2	peptides					1188:1195	the peptides	1184:1195	the peptides derived from HLA-A*0201 which had been retained by the O-GlcNAc-binding lectin WGA	1184:1278	It was found that the peptides derived from HLA-A*0201 which had been retained by the O-GlcNAc-binding lectin WGA did indeed carry a HLA-A*0201 binding motif.
11019912	1	21	gly	glycopeptides	132:144	arg2	glycopeptides					132:144	synthetic glycopeptides	122:144	synthetic glycopeptides carrying a natural cytosolic type of monosaccharide O-beta-linked N-acetylglucosamine (GlcNAc) glycosylation of serine residues	122:272	Previously, using synthetic glycopeptides carrying a natural cytosolic type of monosaccharide O-beta-linked N-acetylglucosamine (GlcNAc) glycosylation of serine residues, we have shown that glycopeptides act as suitable substrates for TAP-mediated transport into the endoplasmic reticulum (ER), and that they bind efficiently to class I major histocompatibility complex (MHC) molecules and can elicit glycopeptide-specific cytotoxic T-lymphocyte (CTL) responses in mice.
11019912	6	22	contain	carry	1291:1295	arg1	peptides					1188:1195	the peptides	1184:1195	the peptides derived from HLA-A*0201 which had been retained by the O-GlcNAc-binding lectin WGA	1184:1278	It was found that the peptides derived from HLA-A*0201 which had been retained by the O-GlcNAc-binding lectin WGA did indeed carry a HLA-A*0201 binding motif.
11019912	6	22	contain	carry	1291:1295	arg2	motif					1318:1322	a HLA-A*0201 binding motif	1297:1322	a HLA-A*0201 binding motif	1297:1322	It was found that the peptides derived from HLA-A*0201 which had been retained by the O-GlcNAc-binding lectin WGA did indeed carry a HLA-A*0201 binding motif.
11019912	2	23	theme	small	677:681	arg1	peptides					709:716	peptides	709:716	peptides which seem to be carrying O-beta-linked monosaccharide GlcNAc	709:778	Recently, we have reported that peptides presented by human class I MHC molecules in vivo encompass a small but significant amount of peptides which seem to be carrying O-beta-linked monosaccharide GlcNAc.
11019912	2	23	theme	small	677:681	arg1	amount					699:704	a small but significant amount	675:704	a small but significant amount of peptides which seem to be carrying O-beta-linked monosaccharide GlcNAc	675:778	Recently, we have reported that peptides presented by human class I MHC molecules in vivo encompass a small but significant amount of peptides which seem to be carrying O-beta-linked monosaccharide GlcNAc.
11019912	6	24	theme	lectin	1269:1274	arg1	WGA					1276:1278	the O-GlcNAc-binding lectin WGA	1248:1278	the O-GlcNAc-binding lectin WGA	1248:1278	It was found that the peptides derived from HLA-A*0201 which had been retained by the O-GlcNAc-binding lectin WGA did indeed carry a HLA-A*0201 binding motif.
11019912	1	25	theme	synthetic	122:130	arg1	glycopeptides					132:144	synthetic glycopeptides	122:144	synthetic glycopeptides carrying a natural cytosolic type of monosaccharide O-beta-linked N-acetylglucosamine (GlcNAc) glycosylation of serine residues	122:272	Previously, using synthetic glycopeptides carrying a natural cytosolic type of monosaccharide O-beta-linked N-acetylglucosamine (GlcNAc) glycosylation of serine residues, we have shown that glycopeptides act as suitable substrates for TAP-mediated transport into the endoplasmic reticulum (ER), and that they bind efficiently to class I major histocompatibility complex (MHC) molecules and can elicit glycopeptide-specific cytotoxic T-lymphocyte (CTL) responses in mice.
11019912	3	26	theme	glycosylated	836:847	arg1	peptides					849:856	glycosylated peptides	836:856	glycosylated peptides	836:856	In the present report we provide further evidence that glycosylated peptides are indeed presented by class I MHC molecules in vivo.
11019912	1	27	theme	TAP-mediated	339:350	arg1	transport					352:360	TAP-mediated transport	339:360	TAP-mediated transport into the endoplasmic reticulum (ER)	339:396	Previously, using synthetic glycopeptides carrying a natural cytosolic type of monosaccharide O-beta-linked N-acetylglucosamine (GlcNAc) glycosylation of serine residues, we have shown that glycopeptides act as suitable substrates for TAP-mediated transport into the endoplasmic reticulum (ER), and that they bind efficiently to class I major histocompatibility complex (MHC) molecules and can elicit glycopeptide-specific cytotoxic T-lymphocyte (CTL) responses in mice.
11019912	3	28	theme	class	882:886	arg1	molecules					894:902	class I MHC molecules	882:902	class I MHC molecules	882:902	In the present report we provide further evidence that glycosylated peptides are indeed presented by class I MHC molecules in vivo.
11019912	1	29	gly	glycosylation	241:253	arg1	residues					265:272	serine residues	258:272	serine residues	258:272	Previously, using synthetic glycopeptides carrying a natural cytosolic type of monosaccharide O-beta-linked N-acetylglucosamine (GlcNAc) glycosylation of serine residues, we have shown that glycopeptides act as suitable substrates for TAP-mediated transport into the endoplasmic reticulum (ER), and that they bind efficiently to class I major histocompatibility complex (MHC) molecules and can elicit glycopeptide-specific cytotoxic T-lymphocyte (CTL) responses in mice.
11019912	1	30	theme	natural	157:163	arg1	type					175:178	a natural cytosolic type	155:178	a natural cytosolic type of monosaccharide O-beta-linked N-acetylglucosamine (GlcNAc) glycosylation of serine residues	155:272	Previously, using synthetic glycopeptides carrying a natural cytosolic type of monosaccharide O-beta-linked N-acetylglucosamine (GlcNAc) glycosylation of serine residues, we have shown that glycopeptides act as suitable substrates for TAP-mediated transport into the endoplasmic reticulum (ER), and that they bind efficiently to class I major histocompatibility complex (MHC) molecules and can elicit glycopeptide-specific cytotoxic T-lymphocyte (CTL) responses in mice.
11019912	1	31	link	O-beta-linked	198:210	arg1	N-acetylglucosamine					212:230	monosaccharide O-beta-linked N-acetylglucosamine	183:230	monosaccharide O-beta-linked N-acetylglucosamine (GlcNAc) glycosylation of serine residues	183:272	Previously, using synthetic glycopeptides carrying a natural cytosolic type of monosaccharide O-beta-linked N-acetylglucosamine (GlcNAc) glycosylation of serine residues, we have shown that glycopeptides act as suitable substrates for TAP-mediated transport into the endoplasmic reticulum (ER), and that they bind efficiently to class I major histocompatibility complex (MHC) molecules and can elicit glycopeptide-specific cytotoxic T-lymphocyte (CTL) responses in mice.
11019912	1	31	link	O-beta-linked	198:210	arg1	GlcNAc					233:238	GlcNAc	233:238	GlcNAc	233:238	Previously, using synthetic glycopeptides carrying a natural cytosolic type of monosaccharide O-beta-linked N-acetylglucosamine (GlcNAc) glycosylation of serine residues, we have shown that glycopeptides act as suitable substrates for TAP-mediated transport into the endoplasmic reticulum (ER), and that they bind efficiently to class I major histocompatibility complex (MHC) molecules and can elicit glycopeptide-specific cytotoxic T-lymphocyte (CTL) responses in mice.
11019912	2	32	theme	MHC	643:645	arg1	molecules					647:655	human class I MHC molecules	629:655	human class I MHC molecules	629:655	Recently, we have reported that peptides presented by human class I MHC molecules in vivo encompass a small but significant amount of peptides which seem to be carrying O-beta-linked monosaccharide GlcNAc.
11019912	0	33	theme	glycopeptides	81:93	arg1	presentation					65:76	presentation	65:76	presentation of glycopeptides	65:93	Lectin purified human class I MHC-derived peptides: evidence for presentation of glycopeptides in vivo.
11019912	1	34	theme	endoplasmic	371:381	arg1	reticulum					383:391	the endoplasmic reticulum	367:391	the endoplasmic reticulum (ER)	367:396	Previously, using synthetic glycopeptides carrying a natural cytosolic type of monosaccharide O-beta-linked N-acetylglucosamine (GlcNAc) glycosylation of serine residues, we have shown that glycopeptides act as suitable substrates for TAP-mediated transport into the endoplasmic reticulum (ER), and that they bind efficiently to class I major histocompatibility complex (MHC) molecules and can elicit glycopeptide-specific cytotoxic T-lymphocyte (CTL) responses in mice.
11019912	1	34	theme	endoplasmic	371:381	arg1	ER					394:395	ER	394:395	ER	394:395	Previously, using synthetic glycopeptides carrying a natural cytosolic type of monosaccharide O-beta-linked N-acetylglucosamine (GlcNAc) glycosylation of serine residues, we have shown that glycopeptides act as suitable substrates for TAP-mediated transport into the endoplasmic reticulum (ER), and that they bind efficiently to class I major histocompatibility complex (MHC) molecules and can elicit glycopeptide-specific cytotoxic T-lymphocyte (CTL) responses in mice.
11019912	4	35	theme	*	946:946	arg1	0201					947:950	HLA-A*0201	941:950	HLA-A*0201	941:950	Thus, peptides derived from HLA-A*0201 were purified by wheat germ agglutinin (WGA) lectin affinity chromatography as previously described.
11019912	2	36	theme	class	635:639	arg1	molecules					647:655	human class I MHC molecules	629:655	human class I MHC molecules	629:655	Recently, we have reported that peptides presented by human class I MHC molecules in vivo encompass a small but significant amount of peptides which seem to be carrying O-beta-linked monosaccharide GlcNAc.
11019912	6	37	theme	0201	1305:1308	arg1	motif					1318:1322	a HLA-A*0201 binding motif	1297:1322	a HLA-A*0201 binding motif	1297:1322	It was found that the peptides derived from HLA-A*0201 which had been retained by the O-GlcNAc-binding lectin WGA did indeed carry a HLA-A*0201 binding motif.
11019912	3	38	theme	MHC	890:892	arg1	molecules					894:902	class I MHC molecules	882:902	class I MHC molecules	882:902	In the present report we provide further evidence that glycosylated peptides are indeed presented by class I MHC molecules in vivo.
11019912	4	39	theme	affinity	1004:1011	arg1	chromatography					1013:1026	wheat germ agglutinin (WGA) lectin affinity chromatography	969:1026	wheat germ agglutinin (WGA) lectin affinity chromatography	969:1026	Thus, peptides derived from HLA-A*0201 were purified by wheat germ agglutinin (WGA) lectin affinity chromatography as previously described.
11019912	3	40	gly	glycosylated	836:847	arg1	peptides					849:856	glycosylated peptides	836:856	glycosylated peptides	836:856	In the present report we provide further evidence that glycosylated peptides are indeed presented by class I MHC molecules in vivo.
11019912	0	41	theme	human	16:20	arg1	I					28:28	human class I	16:28	human class I MHC-derived peptides: evidence for presentation of glycopeptides in vivo	16:101	Lectin purified human class I MHC-derived peptides: evidence for presentation of glycopeptides in vivo.
11019912	7	42	theme	GlcNAc	1493:1498	arg1	residues					1500:1507	terminal GlcNAc residues	1484:1507	terminal GlcNAc residues	1484:1507	Furthermore, using an enzymatic labeling procedure we present evidence that the HLA-A*0201-derived peptides which bind to the WGA lectin are glycosylated with terminal GlcNAc residues.
11019912	4	43	theme	germ	975:978	arg1	agglutinin					980:989	wheat germ agglutinin	969:989	wheat germ agglutinin (WGA) lectin affinity chromatography	969:1026	Thus, peptides derived from HLA-A*0201 were purified by wheat germ agglutinin (WGA) lectin affinity chromatography as previously described.
11019912	4	43	theme	germ	975:978	arg1	WGA					992:994	WGA	992:994	WGA	992:994	Thus, peptides derived from HLA-A*0201 were purified by wheat germ agglutinin (WGA) lectin affinity chromatography as previously described.
11019912	5	44	theme	sequence	1126:1133	arg1	analysis					1135:1142	sequence analysis	1126:1142	sequence analysis	1126:1142	Subsequently, the peptides contained in the WGA-eluate were subjected to sequence analysis by Edman degradation.
11019912	0	45	dep	I	28:28	arg1	evidence					52:59	evidence	52:59	human class I MHC-derived peptides: evidence for presentation of glycopeptides in vivo	16:101	Lectin purified human class I MHC-derived peptides: evidence for presentation of glycopeptides in vivo.
11019912	0	45	dep	I	28:28	arg1	peptides					42:49	MHC-derived peptides	30:49	human class I MHC-derived peptides: evidence for presentation of glycopeptides in vivo	16:101	Lectin purified human class I MHC-derived peptides: evidence for presentation of glycopeptides in vivo.
11019912	8	46	theme	further	1539:1545	arg1	evidence					1547:1554	further evidence	1539:1554	further evidence for the natural presentation by human class I MHC of glycopeptides carrying terminal O-GlcNAc residues in vivo	1539:1665	Together, these data provide further evidence for the natural presentation by human class I MHC of glycopeptides carrying terminal O-GlcNAc residues in vivo.
11019912	7	47	theme	WGA	1451:1453	arg1	lectin					1455:1460	the WGA lectin	1447:1460	the WGA lectin	1447:1460	Furthermore, using an enzymatic labeling procedure we present evidence that the HLA-A*0201-derived peptides which bind to the WGA lectin are glycosylated with terminal GlcNAc residues.
11019912	4	48	attach	derived	928:934	arg2	peptides					919:926	peptides	919:926	peptides derived from HLA-A*0201	919:950	Thus, peptides derived from HLA-A*0201 were purified by wheat germ agglutinin (WGA) lectin affinity chromatography as previously described.
11019912	4	48	attach	derived	928:934	arg1	0201					947:950	HLA-A*0201	941:950	HLA-A*0201	941:950	Thus, peptides derived from HLA-A*0201 were purified by wheat germ agglutinin (WGA) lectin affinity chromatography as previously described.
11019912	1	49	theme	cytotoxic	527:535	arg1	CTL					551:553	CTL	551:553	CTL	551:553	Previously, using synthetic glycopeptides carrying a natural cytosolic type of monosaccharide O-beta-linked N-acetylglucosamine (GlcNAc) glycosylation of serine residues, we have shown that glycopeptides act as suitable substrates for TAP-mediated transport into the endoplasmic reticulum (ER), and that they bind efficiently to class I major histocompatibility complex (MHC) molecules and can elicit glycopeptide-specific cytotoxic T-lymphocyte (CTL) responses in mice.
11019912	1	49	theme	cytotoxic	527:535	arg1	T-lymphocyte					537:548	cytotoxic T-lymphocyte	527:548	glycopeptide-specific cytotoxic T-lymphocyte (CTL) responses	505:564	Previously, using synthetic glycopeptides carrying a natural cytosolic type of monosaccharide O-beta-linked N-acetylglucosamine (GlcNAc) glycosylation of serine residues, we have shown that glycopeptides act as suitable substrates for TAP-mediated transport into the endoplasmic reticulum (ER), and that they bind efficiently to class I major histocompatibility complex (MHC) molecules and can elicit glycopeptide-specific cytotoxic T-lymphocyte (CTL) responses in mice.
11019912	8	50	theme	glycopeptides	1609:1621	arg1	MHC					1602:1604	human class I MHC	1588:1604	human class I MHC of glycopeptides carrying terminal O-GlcNAc residues in vivo	1588:1665	Together, these data provide further evidence for the natural presentation by human class I MHC of glycopeptides carrying terminal O-GlcNAc residues in vivo.
11019912	8	51	theme	natural	1564:1570	arg1	presentation					1572:1583	the natural presentation	1560:1583	the natural presentation by human class I MHC of glycopeptides carrying terminal O-GlcNAc residues in vivo	1560:1665	Together, these data provide further evidence for the natural presentation by human class I MHC of glycopeptides carrying terminal O-GlcNAc residues in vivo.
11019912	6	52	theme	O-GlcNAc-binding	1252:1267	arg1	WGA					1276:1278	the O-GlcNAc-binding lectin WGA	1248:1278	the O-GlcNAc-binding lectin WGA	1248:1278	It was found that the peptides derived from HLA-A*0201 which had been retained by the O-GlcNAc-binding lectin WGA did indeed carry a HLA-A*0201 binding motif.
11019912	8	53	theme	terminal	1632:1639	arg1	residues					1650:1657	terminal O-GlcNAc residues	1632:1657	terminal O-GlcNAc residues in vivo	1632:1665	Together, these data provide further evidence for the natural presentation by human class I MHC of glycopeptides carrying terminal O-GlcNAc residues in vivo.
11019912	1	54	theme	residues	265:272	arg1	glycosylation					241:253	monosaccharide O-beta-linked N-acetylglucosamine (GlcNAc) glycosylation	183:253	monosaccharide O-beta-linked N-acetylglucosamine (GlcNAc) glycosylation of serine residues	183:272	Previously, using synthetic glycopeptides carrying a natural cytosolic type of monosaccharide O-beta-linked N-acetylglucosamine (GlcNAc) glycosylation of serine residues, we have shown that glycopeptides act as suitable substrates for TAP-mediated transport into the endoplasmic reticulum (ER), and that they bind efficiently to class I major histocompatibility complex (MHC) molecules and can elicit glycopeptide-specific cytotoxic T-lymphocyte (CTL) responses in mice.
11019912	7	55	theme	0201-derived	1411:1422	arg1	peptides					1424:1431	the HLA-A*0201-derived peptides	1401:1431	the HLA-A*0201-derived peptides which bind to the WGA lectin	1401:1460	Furthermore, using an enzymatic labeling procedure we present evidence that the HLA-A*0201-derived peptides which bind to the WGA lectin are glycosylated with terminal GlcNAc residues.
11019912	2	56	theme	O-beta-linked	744:756	arg1	GlcNAc					773:778	O-beta-linked monosaccharide GlcNAc	744:778	O-beta-linked monosaccharide GlcNAc	744:778	Recently, we have reported that peptides presented by human class I MHC molecules in vivo encompass a small but significant amount of peptides which seem to be carrying O-beta-linked monosaccharide GlcNAc.
11019912	8	57	theme	class	1594:1598	arg1	MHC					1602:1604	human class I MHC	1588:1604	human class I MHC of glycopeptides carrying terminal O-GlcNAc residues in vivo	1588:1665	Together, these data provide further evidence for the natural presentation by human class I MHC of glycopeptides carrying terminal O-GlcNAc residues in vivo.
11019912	1	58	theme	histocompatibility	447:464	arg1	molecules					480:488	class I major histocompatibility complex (MHC) molecules	433:488	class I major histocompatibility complex (MHC) molecules	433:488	Previously, using synthetic glycopeptides carrying a natural cytosolic type of monosaccharide O-beta-linked N-acetylglucosamine (GlcNAc) glycosylation of serine residues, we have shown that glycopeptides act as suitable substrates for TAP-mediated transport into the endoplasmic reticulum (ER), and that they bind efficiently to class I major histocompatibility complex (MHC) molecules and can elicit glycopeptide-specific cytotoxic T-lymphocyte (CTL) responses in mice.
11019912	1	59	theme	cytosolic	165:173	arg1	type					175:178	a natural cytosolic type	155:178	a natural cytosolic type of monosaccharide O-beta-linked N-acetylglucosamine (GlcNAc) glycosylation of serine residues	155:272	Previously, using synthetic glycopeptides carrying a natural cytosolic type of monosaccharide O-beta-linked N-acetylglucosamine (GlcNAc) glycosylation of serine residues, we have shown that glycopeptides act as suitable substrates for TAP-mediated transport into the endoplasmic reticulum (ER), and that they bind efficiently to class I major histocompatibility complex (MHC) molecules and can elicit glycopeptide-specific cytotoxic T-lymphocyte (CTL) responses in mice.
11019912	7	60	theme	HLA-A	1405:1409	arg1	peptides					1424:1431	the HLA-A*0201-derived peptides	1401:1431	the HLA-A*0201-derived peptides which bind to the WGA lectin	1401:1460	Furthermore, using an enzymatic labeling procedure we present evidence that the HLA-A*0201-derived peptides which bind to the WGA lectin are glycosylated with terminal GlcNAc residues.
11019912	7	61	link	0201-derived	1411:1422	arg1	peptides					1424:1431	the HLA-A*0201-derived peptides	1401:1431	the HLA-A*0201-derived peptides which bind to the WGA lectin	1401:1460	Furthermore, using an enzymatic labeling procedure we present evidence that the HLA-A*0201-derived peptides which bind to the WGA lectin are glycosylated with terminal GlcNAc residues.
11019912	0	62	link	MHC-derived	30:40	arg1	peptides					42:49	MHC-derived peptides	30:49	human class I MHC-derived peptides: evidence for presentation of glycopeptides in vivo	16:101	Lectin purified human class I MHC-derived peptides: evidence for presentation of glycopeptides in vivo.
11019912	6	63	theme	*	1304:1304	arg1	0201					1305:1308	HLA-A*0201	1299:1308	a HLA-A*0201 binding motif	1297:1322	It was found that the peptides derived from HLA-A*0201 which had been retained by the O-GlcNAc-binding lectin WGA did indeed carry a HLA-A*0201 binding motif.
11019912	1	64	theme	O-beta-linked	198:210	arg1	N-acetylglucosamine					212:230	monosaccharide O-beta-linked N-acetylglucosamine	183:230	monosaccharide O-beta-linked N-acetylglucosamine (GlcNAc) glycosylation of serine residues	183:272	Previously, using synthetic glycopeptides carrying a natural cytosolic type of monosaccharide O-beta-linked N-acetylglucosamine (GlcNAc) glycosylation of serine residues, we have shown that glycopeptides act as suitable substrates for TAP-mediated transport into the endoplasmic reticulum (ER), and that they bind efficiently to class I major histocompatibility complex (MHC) molecules and can elicit glycopeptide-specific cytotoxic T-lymphocyte (CTL) responses in mice.
11019912	1	64	theme	O-beta-linked	198:210	arg1	GlcNAc					233:238	GlcNAc	233:238	GlcNAc	233:238	Previously, using synthetic glycopeptides carrying a natural cytosolic type of monosaccharide O-beta-linked N-acetylglucosamine (GlcNAc) glycosylation of serine residues, we have shown that glycopeptides act as suitable substrates for TAP-mediated transport into the endoplasmic reticulum (ER), and that they bind efficiently to class I major histocompatibility complex (MHC) molecules and can elicit glycopeptide-specific cytotoxic T-lymphocyte (CTL) responses in mice.
11019912	7	65	theme	labeling	1357:1364	arg1	procedure					1366:1374	an enzymatic labeling procedure	1344:1374	an enzymatic labeling procedure	1344:1374	Furthermore, using an enzymatic labeling procedure we present evidence that the HLA-A*0201-derived peptides which bind to the WGA lectin are glycosylated with terminal GlcNAc residues.
11019912	6	66	theme	HLA-A	1210:1214	arg1	0201					1216:1219	HLA-A*0201	1210:1219	HLA-A*0201 which had been retained by the O-GlcNAc-binding lectin WGA	1210:1278	It was found that the peptides derived from HLA-A*0201 which had been retained by the O-GlcNAc-binding lectin WGA did indeed carry a HLA-A*0201 binding motif.
11019912	8	67	dep	in	1659:1660	arg1	vivo					1662:1665	vivo	1662:1665	vivo	1662:1665	Together, these data provide further evidence for the natural presentation by human class I MHC of glycopeptides carrying terminal O-GlcNAc residues in vivo.
11019912	7	68	dep	present	1379:1385	arg1	using					1338:1342	using	1338:1342	using an enzymatic labeling procedure	1338:1374	Furthermore, using an enzymatic labeling procedure we present evidence that the HLA-A*0201-derived peptides which bind to the WGA lectin are glycosylated with terminal GlcNAc residues.
11019912	8	69	contain	carrying	1623:1630	arg1	glycopeptides					1609:1621	glycopeptides	1609:1621	glycopeptides carrying terminal O-GlcNAc residues in vivo	1609:1665	Together, these data provide further evidence for the natural presentation by human class I MHC of glycopeptides carrying terminal O-GlcNAc residues in vivo.
11019912	8	69	contain	carrying	1623:1630	arg2	residues					1650:1657	terminal O-GlcNAc residues	1632:1657	terminal O-GlcNAc residues in vivo	1632:1665	Together, these data provide further evidence for the natural presentation by human class I MHC of glycopeptides carrying terminal O-GlcNAc residues in vivo.
11019912	1	70	gly	glycopeptides	294:306	arg2	responses					556:564	glycopeptide-specific cytotoxic T-lymphocyte (CTL) responses	505:564	glycopeptide-specific cytotoxic T-lymphocyte (CTL) responses	505:564	Previously, using synthetic glycopeptides carrying a natural cytosolic type of monosaccharide O-beta-linked N-acetylglucosamine (GlcNAc) glycosylation of serine residues, we have shown that glycopeptides act as suitable substrates for TAP-mediated transport into the endoplasmic reticulum (ER), and that they bind efficiently to class I major histocompatibility complex (MHC) molecules and can elicit glycopeptide-specific cytotoxic T-lymphocyte (CTL) responses in mice.
11019912	1	70	gly	glycopeptides	294:306	arg2	substrates					324:333	suitable substrates	315:333	suitable substrates for TAP-mediated transport into the endoplasmic reticulum (ER)	315:396	Previously, using synthetic glycopeptides carrying a natural cytosolic type of monosaccharide O-beta-linked N-acetylglucosamine (GlcNAc) glycosylation of serine residues, we have shown that glycopeptides act as suitable substrates for TAP-mediated transport into the endoplasmic reticulum (ER), and that they bind efficiently to class I major histocompatibility complex (MHC) molecules and can elicit glycopeptide-specific cytotoxic T-lymphocyte (CTL) responses in mice.
11019912	1	70	gly	glycopeptides	294:306	arg2	glycopeptides					294:306	glycopeptides	294:306	glycopeptides	294:306	Previously, using synthetic glycopeptides carrying a natural cytosolic type of monosaccharide O-beta-linked N-acetylglucosamine (GlcNAc) glycosylation of serine residues, we have shown that glycopeptides act as suitable substrates for TAP-mediated transport into the endoplasmic reticulum (ER), and that they bind efficiently to class I major histocompatibility complex (MHC) molecules and can elicit glycopeptide-specific cytotoxic T-lymphocyte (CTL) responses in mice.
11019912	2	71	theme	peptides	709:716	arg1	peptides					709:716	peptides	709:716	peptides which seem to be carrying O-beta-linked monosaccharide GlcNAc	709:778	Recently, we have reported that peptides presented by human class I MHC molecules in vivo encompass a small but significant amount of peptides which seem to be carrying O-beta-linked monosaccharide GlcNAc.
11019912	2	71	theme	peptides	709:716	arg1	amount					699:704	a small but significant amount	675:704	a small but significant amount of peptides which seem to be carrying O-beta-linked monosaccharide GlcNAc	675:778	Recently, we have reported that peptides presented by human class I MHC molecules in vivo encompass a small but significant amount of peptides which seem to be carrying O-beta-linked monosaccharide GlcNAc.
11019912	3	72	theme	present	788:794	arg1	report					796:801	the present report	784:801	the present report	784:801	In the present report we provide further evidence that glycosylated peptides are indeed presented by class I MHC molecules in vivo.
11019912	3	73	theme	I	888:888	arg1	molecules					894:902	class I MHC molecules	882:902	class I MHC molecules	882:902	In the present report we provide further evidence that glycosylated peptides are indeed presented by class I MHC molecules in vivo.
11019912	0	74	theme	in	95:96	arg1	evidence					52:59	evidence	52:59	human class I MHC-derived peptides: evidence for presentation of glycopeptides in vivo	16:101	Lectin purified human class I MHC-derived peptides: evidence for presentation of glycopeptides in vivo.
11019912	2	75	theme	I	641:641	arg1	molecules					647:655	human class I MHC molecules	629:655	human class I MHC molecules	629:655	Recently, we have reported that peptides presented by human class I MHC molecules in vivo encompass a small but significant amount of peptides which seem to be carrying O-beta-linked monosaccharide GlcNAc.
11019912	3	76	theme	further	814:820	arg1	evidence					822:829	further evidence that glycosylated peptides are indeed presented by class I MHC molecules in vivo	814:910	further evidence that glycosylated peptides are indeed presented by class I MHC molecules in vivo	814:910	In the present report we provide further evidence that glycosylated peptides are indeed presented by class I MHC molecules in vivo.
11019912	6	77	theme	binding	1310:1316	arg1	motif					1318:1322	a HLA-A*0201 binding motif	1297:1322	a HLA-A*0201 binding motif	1297:1322	It was found that the peptides derived from HLA-A*0201 which had been retained by the O-GlcNAc-binding lectin WGA did indeed carry a HLA-A*0201 binding motif.
11019912	0	78	dep	in	95:96	arg1	vivo					98:101	vivo	98:101	vivo	98:101	Lectin purified human class I MHC-derived peptides: evidence for presentation of glycopeptides in vivo.
11019912	4	79	theme	HLA-A	941:945	arg1	0201					947:950	HLA-A*0201	941:950	HLA-A*0201	941:950	Thus, peptides derived from HLA-A*0201 were purified by wheat germ agglutinin (WGA) lectin affinity chromatography as previously described.
11019912	0	80	gly	glycopeptides	81:93	arg2	glycopeptides					81:93	glycopeptides	81:93	glycopeptides	81:93	Lectin purified human class I MHC-derived peptides: evidence for presentation of glycopeptides in vivo.
11019912	0	81	theme	class	22:26	arg1	I					28:28	human class I	16:28	human class I MHC-derived peptides: evidence for presentation of glycopeptides in vivo	16:101	Lectin purified human class I MHC-derived peptides: evidence for presentation of glycopeptides in vivo.
11019912	4	82	theme	lectin	997:1002	arg1	chromatography					1013:1026	wheat germ agglutinin (WGA) lectin affinity chromatography	969:1026	wheat germ agglutinin (WGA) lectin affinity chromatography	969:1026	Thus, peptides derived from HLA-A*0201 were purified by wheat germ agglutinin (WGA) lectin affinity chromatography as previously described.
11019912	0	83	theme	MHC-derived	30:40	arg1	peptides					42:49	MHC-derived peptides	30:49	human class I MHC-derived peptides: evidence for presentation of glycopeptides in vivo	16:101	Lectin purified human class I MHC-derived peptides: evidence for presentation of glycopeptides in vivo.
11019912	4	84	theme	wheat	969:973	arg1	agglutinin					980:989	wheat germ agglutinin	969:989	wheat germ agglutinin (WGA) lectin affinity chromatography	969:1026	Thus, peptides derived from HLA-A*0201 were purified by wheat germ agglutinin (WGA) lectin affinity chromatography as previously described.
11019912	4	84	theme	wheat	969:973	arg1	WGA					992:994	WGA	992:994	WGA	992:994	Thus, peptides derived from HLA-A*0201 were purified by wheat germ agglutinin (WGA) lectin affinity chromatography as previously described.
11019912	1	85	theme	suitable	315:322	arg1	responses					556:564	glycopeptide-specific cytotoxic T-lymphocyte (CTL) responses	505:564	glycopeptide-specific cytotoxic T-lymphocyte (CTL) responses	505:564	Previously, using synthetic glycopeptides carrying a natural cytosolic type of monosaccharide O-beta-linked N-acetylglucosamine (GlcNAc) glycosylation of serine residues, we have shown that glycopeptides act as suitable substrates for TAP-mediated transport into the endoplasmic reticulum (ER), and that they bind efficiently to class I major histocompatibility complex (MHC) molecules and can elicit glycopeptide-specific cytotoxic T-lymphocyte (CTL) responses in mice.
11019912	1	85	theme	suitable	315:322	arg1	glycopeptides					294:306	glycopeptides	294:306	glycopeptides	294:306	Previously, using synthetic glycopeptides carrying a natural cytosolic type of monosaccharide O-beta-linked N-acetylglucosamine (GlcNAc) glycosylation of serine residues, we have shown that glycopeptides act as suitable substrates for TAP-mediated transport into the endoplasmic reticulum (ER), and that they bind efficiently to class I major histocompatibility complex (MHC) molecules and can elicit glycopeptide-specific cytotoxic T-lymphocyte (CTL) responses in mice.
11019912	1	85	theme	suitable	315:322	arg1	substrates					324:333	suitable substrates	315:333	suitable substrates for TAP-mediated transport into the endoplasmic reticulum (ER)	315:396	Previously, using synthetic glycopeptides carrying a natural cytosolic type of monosaccharide O-beta-linked N-acetylglucosamine (GlcNAc) glycosylation of serine residues, we have shown that glycopeptides act as suitable substrates for TAP-mediated transport into the endoplasmic reticulum (ER), and that they bind efficiently to class I major histocompatibility complex (MHC) molecules and can elicit glycopeptide-specific cytotoxic T-lymphocyte (CTL) responses in mice.
11019912	7	86	theme	terminal	1484:1491	arg1	residues					1500:1507	terminal GlcNAc residues	1484:1507	terminal GlcNAc residues	1484:1507	Furthermore, using an enzymatic labeling procedure we present evidence that the HLA-A*0201-derived peptides which bind to the WGA lectin are glycosylated with terminal GlcNAc residues.
11019912	4	87	theme	agglutinin	980:989	arg1	chromatography					1013:1026	wheat germ agglutinin (WGA) lectin affinity chromatography	969:1026	wheat germ agglutinin (WGA) lectin affinity chromatography	969:1026	Thus, peptides derived from HLA-A*0201 were purified by wheat germ agglutinin (WGA) lectin affinity chromatography as previously described.
11019912	5	88	theme	Edman	1147:1151	arg1	degradation					1153:1163	Edman degradation	1147:1163	Edman degradation	1147:1163	Subsequently, the peptides contained in the WGA-eluate were subjected to sequence analysis by Edman degradation.
11019912	1	89	theme	glycopeptide-specific	505:525	arg1	responses					556:564	glycopeptide-specific cytotoxic T-lymphocyte (CTL) responses	505:564	glycopeptide-specific cytotoxic T-lymphocyte (CTL) responses	505:564	Previously, using synthetic glycopeptides carrying a natural cytosolic type of monosaccharide O-beta-linked N-acetylglucosamine (GlcNAc) glycosylation of serine residues, we have shown that glycopeptides act as suitable substrates for TAP-mediated transport into the endoplasmic reticulum (ER), and that they bind efficiently to class I major histocompatibility complex (MHC) molecules and can elicit glycopeptide-specific cytotoxic T-lymphocyte (CTL) responses in mice.
11019912	1	89	theme	glycopeptide-specific	505:525	arg1	glycopeptides					294:306	glycopeptides	294:306	glycopeptides	294:306	Previously, using synthetic glycopeptides carrying a natural cytosolic type of monosaccharide O-beta-linked N-acetylglucosamine (GlcNAc) glycosylation of serine residues, we have shown that glycopeptides act as suitable substrates for TAP-mediated transport into the endoplasmic reticulum (ER), and that they bind efficiently to class I major histocompatibility complex (MHC) molecules and can elicit glycopeptide-specific cytotoxic T-lymphocyte (CTL) responses in mice.
11019912	1	89	theme	glycopeptide-specific	505:525	arg1	substrates					324:333	suitable substrates	315:333	suitable substrates for TAP-mediated transport into the endoplasmic reticulum (ER)	315:396	Previously, using synthetic glycopeptides carrying a natural cytosolic type of monosaccharide O-beta-linked N-acetylglucosamine (GlcNAc) glycosylation of serine residues, we have shown that glycopeptides act as suitable substrates for TAP-mediated transport into the endoplasmic reticulum (ER), and that they bind efficiently to class I major histocompatibility complex (MHC) molecules and can elicit glycopeptide-specific cytotoxic T-lymphocyte (CTL) responses in mice.
11019912	1	90	theme	glycosylation	241:253	arg1	type					175:178	a natural cytosolic type	155:178	a natural cytosolic type of monosaccharide O-beta-linked N-acetylglucosamine (GlcNAc) glycosylation of serine residues	155:272	Previously, using synthetic glycopeptides carrying a natural cytosolic type of monosaccharide O-beta-linked N-acetylglucosamine (GlcNAc) glycosylation of serine residues, we have shown that glycopeptides act as suitable substrates for TAP-mediated transport into the endoplasmic reticulum (ER), and that they bind efficiently to class I major histocompatibility complex (MHC) molecules and can elicit glycopeptide-specific cytotoxic T-lymphocyte (CTL) responses in mice.
11019912	1	91	theme	T-lymphocyte	537:548	arg1	responses					556:564	glycopeptide-specific cytotoxic T-lymphocyte (CTL) responses	505:564	glycopeptide-specific cytotoxic T-lymphocyte (CTL) responses	505:564	Previously, using synthetic glycopeptides carrying a natural cytosolic type of monosaccharide O-beta-linked N-acetylglucosamine (GlcNAc) glycosylation of serine residues, we have shown that glycopeptides act as suitable substrates for TAP-mediated transport into the endoplasmic reticulum (ER), and that they bind efficiently to class I major histocompatibility complex (MHC) molecules and can elicit glycopeptide-specific cytotoxic T-lymphocyte (CTL) responses in mice.
11019912	1	91	theme	T-lymphocyte	537:548	arg1	glycopeptides					294:306	glycopeptides	294:306	glycopeptides	294:306	Previously, using synthetic glycopeptides carrying a natural cytosolic type of monosaccharide O-beta-linked N-acetylglucosamine (GlcNAc) glycosylation of serine residues, we have shown that glycopeptides act as suitable substrates for TAP-mediated transport into the endoplasmic reticulum (ER), and that they bind efficiently to class I major histocompatibility complex (MHC) molecules and can elicit glycopeptide-specific cytotoxic T-lymphocyte (CTL) responses in mice.
11019912	1	91	theme	T-lymphocyte	537:548	arg1	substrates					324:333	suitable substrates	315:333	suitable substrates for TAP-mediated transport into the endoplasmic reticulum (ER)	315:396	Previously, using synthetic glycopeptides carrying a natural cytosolic type of monosaccharide O-beta-linked N-acetylglucosamine (GlcNAc) glycosylation of serine residues, we have shown that glycopeptides act as suitable substrates for TAP-mediated transport into the endoplasmic reticulum (ER), and that they bind efficiently to class I major histocompatibility complex (MHC) molecules and can elicit glycopeptide-specific cytotoxic T-lymphocyte (CTL) responses in mice.
11019912	8	92	theme	O-GlcNAc	1641:1648	arg1	residues					1650:1657	terminal O-GlcNAc residues	1632:1657	terminal O-GlcNAc residues in vivo	1632:1665	Together, these data provide further evidence for the natural presentation by human class I MHC of glycopeptides carrying terminal O-GlcNAc residues in vivo.
11019912	1	93	theme	serine	258:263	arg1	residues					265:272	serine residues	258:272	serine residues	258:272	Previously, using synthetic glycopeptides carrying a natural cytosolic type of monosaccharide O-beta-linked N-acetylglucosamine (GlcNAc) glycosylation of serine residues, we have shown that glycopeptides act as suitable substrates for TAP-mediated transport into the endoplasmic reticulum (ER), and that they bind efficiently to class I major histocompatibility complex (MHC) molecules and can elicit glycopeptide-specific cytotoxic T-lymphocyte (CTL) responses in mice.
25619971	0	0	theme	protein	85:91	arg1	production					93:102	O-GlcNAcylated recombinant protein production	58:102	O-GlcNAcylated recombinant protein production in E. coli	58:113	A highly effective and adjustable dual plasmid system for O-GlcNAcylated recombinant protein production in E. coli.
25619971	4	1	theme	compatible	660:669	arg1	system					684:689	a compatible dual plasmid system	658:689	a compatible dual plasmid system for coexpression of OGT	658:713	Here, we describe a compatible dual plasmid system for coexpression of OGT and its target substrate for O-GlcNAcylated protein production in E. coli.
25619971	4	2	from	production	767:776	arg1	coli					784:787	E. coli	781:787	E. coli	781:787	Here, we describe a compatible dual plasmid system for coexpression of OGT and its target substrate for O-GlcNAcylated protein production in E. coli.
25619971	1	3	theme	dynamic	149:155	arg1	modification					199:210	a ubiquitous, dynamic and reversible post-translational protein modification	135:210	a ubiquitous, dynamic and reversible post-translational protein modification in metazoans	135:223	O-GlcNAcylation is a ubiquitous, dynamic and reversible post-translational protein modification in metazoans, and it is catalysed and removed by O-GlcNAc transferase (OGT) and O-GlcNAcase, respectively.
25619971	1	3	theme	dynamic	149:155	arg1	O-GlcNAcylation					116:130	O-GlcNAcylation	116:130	O-GlcNAcylation	116:130	O-GlcNAcylation is a ubiquitous, dynamic and reversible post-translational protein modification in metazoans, and it is catalysed and removed by O-GlcNAc transferase (OGT) and O-GlcNAcase, respectively.
25619971	9	4	theme	adjustable	1344:1353	arg1	system					1379:1384	an adjustable compatible dual plasmid system	1341:1384	an adjustable compatible dual plasmid system that can effectively yield O-GlcNAcylated proteins in E. coli	1341:1446	Altogether, we established an adjustable compatible dual plasmid system that can effectively yield O-GlcNAcylated proteins in E. coli.
25619971	6	5	theme	isopropyl	975:983	arg1	vector					1053:1058	an isopropyl β-d-thiogalactopyranoside-inducible OGT target substrate expression vector	972:1058	an isopropyl β-d-thiogalactopyranoside-inducible OGT target substrate expression vector bearing a p15A origin	972:1080	This compatible dual plasmid system contains an arabinose-inducible OGT expression vector with a pUC origin and an isopropyl β-d-thiogalactopyranoside-inducible OGT target substrate expression vector bearing a p15A origin.
25619971	0	6	theme	recombinant	73:83	arg1	production					93:102	O-GlcNAcylated recombinant protein production	58:102	O-GlcNAcylated recombinant protein production in E. coli	58:113	A highly effective and adjustable dual plasmid system for O-GlcNAcylated recombinant protein production in E. coli.
25619971	6	7	theme	plasmid	881:887	arg1	system					889:894	This compatible dual plasmid system	860:894	This compatible dual plasmid system	860:894	This compatible dual plasmid system contains an arabinose-inducible OGT expression vector with a pUC origin and an isopropyl β-d-thiogalactopyranoside-inducible OGT target substrate expression vector bearing a p15A origin.
25619971	4	8	theme	dual	671:674	arg1	system					684:689	a compatible dual plasmid system	658:689	a compatible dual plasmid system for coexpression of OGT	658:713	Here, we describe a compatible dual plasmid system for coexpression of OGT and its target substrate for O-GlcNAcylated protein production in E. coli.
25619971	6	9	theme	dual	876:879	arg1	system					889:894	This compatible dual plasmid system	860:894	This compatible dual plasmid system	860:894	This compatible dual plasmid system contains an arabinose-inducible OGT expression vector with a pUC origin and an isopropyl β-d-thiogalactopyranoside-inducible OGT target substrate expression vector bearing a p15A origin.
25619971	7	10	theme	recombinant	1116:1126	arg1	proteins					1128:1135	recombinant proteins	1116:1135	recombinant proteins	1116:1135	The dual plasmid system produces recombinant proteins with varying O-GlcNAcylation levels by altering the inducer concentration.
25619971	1	11	theme	O-GlcNAc	261:268	arg1	OGT					283:285	OGT	283:285	OGT	283:285	O-GlcNAcylation is a ubiquitous, dynamic and reversible post-translational protein modification in metazoans, and it is catalysed and removed by O-GlcNAc transferase (OGT) and O-GlcNAcase, respectively.
25619971	1	11	theme	O-GlcNAc	261:268	arg1	transferase					270:280	O-GlcNAc transferase	261:280	O-GlcNAc transferase (OGT)	261:286	O-GlcNAcylation is a ubiquitous, dynamic and reversible post-translational protein modification in metazoans, and it is catalysed and removed by O-GlcNAc transferase (OGT) and O-GlcNAcase, respectively.
25619971	6	12	theme	compatible	865:874	arg1	system					889:894	This compatible dual plasmid system	860:894	This compatible dual plasmid system	860:894	This compatible dual plasmid system contains an arabinose-inducible OGT expression vector with a pUC origin and an isopropyl β-d-thiogalactopyranoside-inducible OGT target substrate expression vector bearing a p15A origin.
25619971	6	13	with	vector	943:948	arg1	origin					961:966	a pUC origin	955:966	a pUC origin	955:966	This compatible dual plasmid system contains an arabinose-inducible OGT expression vector with a pUC origin and an isopropyl β-d-thiogalactopyranoside-inducible OGT target substrate expression vector bearing a p15A origin.
25619971	4	14	theme	plasmid	676:682	arg1	system					684:689	a compatible dual plasmid system	658:689	a compatible dual plasmid system for coexpression of OGT	658:713	Here, we describe a compatible dual plasmid system for coexpression of OGT and its target substrate for O-GlcNAcylated protein production in E. coli.
25619971	9	15	theme	O-GlcNAcylated	1413:1426	arg1	proteins					1428:1435	O-GlcNAcylated proteins	1413:1435	O-GlcNAcylated proteins	1413:1435	Altogether, we established an adjustable compatible dual plasmid system that can effectively yield O-GlcNAcylated proteins in E. coli.
25619971	9	16	theme	compatible	1355:1364	arg1	system					1379:1384	an adjustable compatible dual plasmid system	1341:1384	an adjustable compatible dual plasmid system that can effectively yield O-GlcNAcylated proteins in E. coli	1341:1446	Altogether, we established an adjustable compatible dual plasmid system that can effectively yield O-GlcNAcylated proteins in E. coli.
25619971	8	17	theme	reported	1297:1304	arg1	system					1306:1311	the previously reported system	1282:1311	the previously reported system	1282:1311	More importantly, the O-GlcNAcylation efficiency was much higher than the previously reported system.
25619971	4	18	theme	protein	759:765	arg1	production					767:776	O-GlcNAcylated protein production	744:776	O-GlcNAcylated protein production in E. coli	744:787	Here, we describe a compatible dual plasmid system for coexpression of OGT and its target substrate for O-GlcNAcylated protein production in E. coli.
25619971	1	19	theme	reversible	161:170	arg1	modification					199:210	a ubiquitous, dynamic and reversible post-translational protein modification	135:210	a ubiquitous, dynamic and reversible post-translational protein modification in metazoans	135:223	O-GlcNAcylation is a ubiquitous, dynamic and reversible post-translational protein modification in metazoans, and it is catalysed and removed by O-GlcNAc transferase (OGT) and O-GlcNAcase, respectively.
25619971	1	19	theme	reversible	161:170	arg1	O-GlcNAcylation					116:130	O-GlcNAcylation	116:130	O-GlcNAcylation	116:130	O-GlcNAcylation is a ubiquitous, dynamic and reversible post-translational protein modification in metazoans, and it is catalysed and removed by O-GlcNAc transferase (OGT) and O-GlcNAcase, respectively.
25619971	3	20	theme	mammalian	403:411	arg1	OGT					413:415	mammalian OGT	403:415	mammalian OGT	403:415	It has been reported that coexpression of mammalian OGT with its target substrates in Escherichia coli produce O-GlcNAcylated recombinant proteins, but the plasmids used were not compatible, and the expression of both OGT and its target protein were induced by the same inducer.
25619971	9	21	theme	dual	1366:1369	arg1	system					1379:1384	an adjustable compatible dual plasmid system	1341:1384	an adjustable compatible dual plasmid system that can effectively yield O-GlcNAcylated proteins in E. coli	1341:1446	Altogether, we established an adjustable compatible dual plasmid system that can effectively yield O-GlcNAcylated proteins in E. coli.
25619971	0	22	theme	dual	34:37	arg1	system					47:52	A highly effective and adjustable dual plasmid system	0:52	A highly effective and adjustable dual plasmid system for O-GlcNAcylated recombinant protein production in E. coli	0:113	A highly effective and adjustable dual plasmid system for O-GlcNAcylated recombinant protein production in E. coli.
25619971	4	23	theme	O-GlcNAcylated	744:757	arg1	production					767:776	O-GlcNAcylated protein production	744:776	O-GlcNAcylated protein production in E. coli	744:787	Here, we describe a compatible dual plasmid system for coexpression of OGT and its target substrate for O-GlcNAcylated protein production in E. coli.
25619971	1	24	theme	post-translational	172:189	arg1	modification					199:210	a ubiquitous, dynamic and reversible post-translational protein modification	135:210	a ubiquitous, dynamic and reversible post-translational protein modification in metazoans	135:223	O-GlcNAcylation is a ubiquitous, dynamic and reversible post-translational protein modification in metazoans, and it is catalysed and removed by O-GlcNAc transferase (OGT) and O-GlcNAcase, respectively.
25619971	1	24	theme	post-translational	172:189	arg1	O-GlcNAcylation					116:130	O-GlcNAcylation	116:130	O-GlcNAcylation	116:130	O-GlcNAcylation is a ubiquitous, dynamic and reversible post-translational protein modification in metazoans, and it is catalysed and removed by O-GlcNAc transferase (OGT) and O-GlcNAcase, respectively.
25619971	9	25	theme	plasmid	1371:1377	arg1	system					1379:1384	an adjustable compatible dual plasmid system	1341:1384	an adjustable compatible dual plasmid system that can effectively yield O-GlcNAcylated proteins in E. coli	1341:1446	Altogether, we established an adjustable compatible dual plasmid system that can effectively yield O-GlcNAcylated proteins in E. coli.
25619971	7	26	theme	dual	1087:1090	arg1	system					1100:1105	The dual plasmid system	1083:1105	The dual plasmid system	1083:1105	The dual plasmid system produces recombinant proteins with varying O-GlcNAcylation levels by altering the inducer concentration.
25619971	1	27	theme	protein	191:197	arg1	modification					199:210	a ubiquitous, dynamic and reversible post-translational protein modification	135:210	a ubiquitous, dynamic and reversible post-translational protein modification in metazoans	135:223	O-GlcNAcylation is a ubiquitous, dynamic and reversible post-translational protein modification in metazoans, and it is catalysed and removed by O-GlcNAc transferase (OGT) and O-GlcNAcase, respectively.
25619971	1	27	theme	protein	191:197	arg1	O-GlcNAcylation					116:130	O-GlcNAcylation	116:130	O-GlcNAcylation	116:130	O-GlcNAcylation is a ubiquitous, dynamic and reversible post-translational protein modification in metazoans, and it is catalysed and removed by O-GlcNAc transferase (OGT) and O-GlcNAcase, respectively.
25619971	6	28	theme	pUC	957:959	arg1	origin					961:966	a pUC origin	955:966	a pUC origin	955:966	This compatible dual plasmid system contains an arabinose-inducible OGT expression vector with a pUC origin and an isopropyl β-d-thiogalactopyranoside-inducible OGT target substrate expression vector bearing a p15A origin.
25619971	7	29	theme	plasmid	1092:1098	arg1	system					1100:1105	The dual plasmid system	1083:1105	The dual plasmid system	1083:1105	The dual plasmid system produces recombinant proteins with varying O-GlcNAcylation levels by altering the inducer concentration.
25619971	4	30	theme	OGT	711:713	arg1	coexpression					695:706	coexpression	695:706	coexpression of OGT	695:713	Here, we describe a compatible dual plasmid system for coexpression of OGT and its target substrate for O-GlcNAcylated protein production in E. coli.
25619971	3	31	theme	target	426:431	arg1	substrates					433:442	its target substrates	422:442	its target substrates in Escherichia coli	422:462	It has been reported that coexpression of mammalian OGT with its target substrates in Escherichia coli produce O-GlcNAcylated recombinant proteins, but the plasmids used were not compatible, and the expression of both OGT and its target protein were induced by the same inducer.
25619971	4	32	theme	target	723:728	arg1	substrate					730:738	its target substrate	719:738	its target substrate for O-GlcNAcylated protein production in E. coli	719:787	Here, we describe a compatible dual plasmid system for coexpression of OGT and its target substrate for O-GlcNAcylated protein production in E. coli.
25619971	0	33	theme	effective	9:17	arg1	system					47:52	A highly effective and adjustable dual plasmid system	0:52	A highly effective and adjustable dual plasmid system for O-GlcNAcylated recombinant protein production in E. coli	0:113	A highly effective and adjustable dual plasmid system for O-GlcNAcylated recombinant protein production in E. coli.
25619971	3	34	with	coexpression	387:398	arg1	substrates					433:442	its target substrates	422:442	its target substrates in Escherichia coli	422:462	It has been reported that coexpression of mammalian OGT with its target substrates in Escherichia coli produce O-GlcNAcylated recombinant proteins, but the plasmids used were not compatible, and the expression of both OGT and its target protein were induced by the same inducer.
25619971	3	35	theme	O-GlcNAcylated	472:485	arg1	proteins					499:506	O-GlcNAcylated recombinant proteins	472:506	O-GlcNAcylated recombinant proteins	472:506	It has been reported that coexpression of mammalian OGT with its target substrates in Escherichia coli produce O-GlcNAcylated recombinant proteins, but the plasmids used were not compatible, and the expression of both OGT and its target protein were induced by the same inducer.
25619971	3	36	theme	OGT	413:415	arg1	coexpression					387:398	coexpression	387:398	coexpression of mammalian OGT with its target substrates in Escherichia coli	387:462	It has been reported that coexpression of mammalian OGT with its target substrates in Escherichia coli produce O-GlcNAcylated recombinant proteins, but the plasmids used were not compatible, and the expression of both OGT and its target protein were induced by the same inducer.
25619971	6	37	contain	contains	896:903	arg1	system					889:894	This compatible dual plasmid system	860:894	This compatible dual plasmid system	860:894	This compatible dual plasmid system contains an arabinose-inducible OGT expression vector with a pUC origin and an isopropyl β-d-thiogalactopyranoside-inducible OGT target substrate expression vector bearing a p15A origin.
25619971	6	37	contain	contains	896:903	arg2	vector					943:948	an arabinose-inducible OGT expression vector	905:948	an arabinose-inducible OGT expression vector with a pUC origin	905:966	This compatible dual plasmid system contains an arabinose-inducible OGT expression vector with a pUC origin and an isopropyl β-d-thiogalactopyranoside-inducible OGT target substrate expression vector bearing a p15A origin.
25619971	6	37	contain	contains	896:903	arg2	vector					1053:1058	an isopropyl β-d-thiogalactopyranoside-inducible OGT target substrate expression vector	972:1058	an isopropyl β-d-thiogalactopyranoside-inducible OGT target substrate expression vector bearing a p15A origin	972:1080	This compatible dual plasmid system contains an arabinose-inducible OGT expression vector with a pUC origin and an isopropyl β-d-thiogalactopyranoside-inducible OGT target substrate expression vector bearing a p15A origin.
25619971	0	38	theme	adjustable	23:32	arg1	system					47:52	A highly effective and adjustable dual plasmid system	0:52	A highly effective and adjustable dual plasmid system for O-GlcNAcylated recombinant protein production in E. coli	0:113	A highly effective and adjustable dual plasmid system for O-GlcNAcylated recombinant protein production in E. coli.
25619971	6	39	theme	expression	932:941	arg1	vector					943:948	an arabinose-inducible OGT expression vector	905:948	an arabinose-inducible OGT expression vector with a pUC origin	905:966	This compatible dual plasmid system contains an arabinose-inducible OGT expression vector with a pUC origin and an isopropyl β-d-thiogalactopyranoside-inducible OGT target substrate expression vector bearing a p15A origin.
25619971	8	40	theme	O-GlcNAcylation	1234:1248	arg1	efficiency					1250:1259	the O-GlcNAcylation efficiency	1230:1259	the O-GlcNAcylation efficiency	1230:1259	More importantly, the O-GlcNAcylation efficiency was much higher than the previously reported system.
25619971	8	40	theme	O-GlcNAcylation	1234:1248	arg1	higher					1270:1275	higher	1270:1275	higher	1270:1275	More importantly, the O-GlcNAcylation efficiency was much higher than the previously reported system.
25619971	3	41	theme	target	591:596	arg1	protein					598:604	its target protein	587:604	its target protein	587:604	It has been reported that coexpression of mammalian OGT with its target substrates in Escherichia coli produce O-GlcNAcylated recombinant proteins, but the plasmids used were not compatible, and the expression of both OGT and its target protein were induced by the same inducer.
25619971	6	42	theme	expression	1042:1051	arg1	vector					1053:1058	an isopropyl β-d-thiogalactopyranoside-inducible OGT target substrate expression vector	972:1058	an isopropyl β-d-thiogalactopyranoside-inducible OGT target substrate expression vector bearing a p15A origin	972:1080	This compatible dual plasmid system contains an arabinose-inducible OGT expression vector with a pUC origin and an isopropyl β-d-thiogalactopyranoside-inducible OGT target substrate expression vector bearing a p15A origin.
25619971	7	43	theme	O-GlcNAcylation	1150:1164	arg1	levels					1166:1171	O-GlcNAcylation levels	1150:1171	O-GlcNAcylation levels	1150:1171	The dual plasmid system produces recombinant proteins with varying O-GlcNAcylation levels by altering the inducer concentration.
25619971	6	44	theme	OGT	928:930	arg1	vector					943:948	an arabinose-inducible OGT expression vector	905:948	an arabinose-inducible OGT expression vector with a pUC origin	905:966	This compatible dual plasmid system contains an arabinose-inducible OGT expression vector with a pUC origin and an isopropyl β-d-thiogalactopyranoside-inducible OGT target substrate expression vector bearing a p15A origin.
25619971	3	45	theme	same	626:629	arg1	inducer					631:637	the same inducer	622:637	the same inducer	622:637	It has been reported that coexpression of mammalian OGT with its target substrates in Escherichia coli produce O-GlcNAcylated recombinant proteins, but the plasmids used were not compatible, and the expression of both OGT and its target protein were induced by the same inducer.
25619971	3	46	theme	OGT	579:581	arg1	expression					560:569	the expression	556:569	the expression of both OGT and its target protein	556:604	It has been reported that coexpression of mammalian OGT with its target substrates in Escherichia coli produce O-GlcNAcylated recombinant proteins, but the plasmids used were not compatible, and the expression of both OGT and its target protein were induced by the same inducer.
25619971	2	47	theme	OGT	347:349	arg1	activity					351:358	endogenous OGT activity	336:358	endogenous OGT activity	336:358	Prokaryotes lack endogenous OGT activity.
25619971	0	48	theme	plasmid	39:45	arg1	system					47:52	A highly effective and adjustable dual plasmid system	0:52	A highly effective and adjustable dual plasmid system for O-GlcNAcylated recombinant protein production in E. coli	0:113	A highly effective and adjustable dual plasmid system for O-GlcNAcylated recombinant protein production in E. coli.
25619971	6	49	theme	arabinose-inducible	908:926	arg1	vector					943:948	an arabinose-inducible OGT expression vector	905:948	an arabinose-inducible OGT expression vector with a pUC origin	905:966	This compatible dual plasmid system contains an arabinose-inducible OGT expression vector with a pUC origin and an isopropyl β-d-thiogalactopyranoside-inducible OGT target substrate expression vector bearing a p15A origin.
25619971	6	50	with	vector	1053:1058	arg1	origin					961:966	a pUC origin	955:966	a pUC origin	955:966	This compatible dual plasmid system contains an arabinose-inducible OGT expression vector with a pUC origin and an isopropyl β-d-thiogalactopyranoside-inducible OGT target substrate expression vector bearing a p15A origin.
25619971	2	51	theme	endogenous	336:345	arg1	activity					351:358	endogenous OGT activity	336:358	endogenous OGT activity	336:358	Prokaryotes lack endogenous OGT activity.
25619971	3	52	theme	recombinant	487:497	arg1	proteins					499:506	O-GlcNAcylated recombinant proteins	472:506	O-GlcNAcylated recombinant proteins	472:506	It has been reported that coexpression of mammalian OGT with its target substrates in Escherichia coli produce O-GlcNAcylated recombinant proteins, but the plasmids used were not compatible, and the expression of both OGT and its target protein were induced by the same inducer.
25619971	6	53	theme	substrate	1032:1040	arg1	vector					1053:1058	an isopropyl β-d-thiogalactopyranoside-inducible OGT target substrate expression vector	972:1058	an isopropyl β-d-thiogalactopyranoside-inducible OGT target substrate expression vector bearing a p15A origin	972:1080	This compatible dual plasmid system contains an arabinose-inducible OGT expression vector with a pUC origin and an isopropyl β-d-thiogalactopyranoside-inducible OGT target substrate expression vector bearing a p15A origin.
25619971	6	54	theme	p15A	1070:1073	arg1	origin					1075:1080	a p15A origin	1068:1080	a p15A origin	1068:1080	This compatible dual plasmid system contains an arabinose-inducible OGT expression vector with a pUC origin and an isopropyl β-d-thiogalactopyranoside-inducible OGT target substrate expression vector bearing a p15A origin.
25619971	6	55	theme	target	1025:1030	arg1	vector					1053:1058	an isopropyl β-d-thiogalactopyranoside-inducible OGT target substrate expression vector	972:1058	an isopropyl β-d-thiogalactopyranoside-inducible OGT target substrate expression vector bearing a p15A origin	972:1080	This compatible dual plasmid system contains an arabinose-inducible OGT expression vector with a pUC origin and an isopropyl β-d-thiogalactopyranoside-inducible OGT target substrate expression vector bearing a p15A origin.
25619971	0	56	theme	O-GlcNAcylated	58:71	arg1	production					93:102	O-GlcNAcylated recombinant protein production	58:102	O-GlcNAcylated recombinant protein production in E. coli	58:113	A highly effective and adjustable dual plasmid system for O-GlcNAcylated recombinant protein production in E. coli.
25619971	0	57	from	production	93:102	arg1	coli					110:113	E. coli	107:113	E. coli	107:113	A highly effective and adjustable dual plasmid system for O-GlcNAcylated recombinant protein production in E. coli.
25619971	3	58	theme	protein	598:604	arg1	expression					560:569	the expression	556:569	the expression of both OGT and its target protein	556:604	It has been reported that coexpression of mammalian OGT with its target substrates in Escherichia coli produce O-GlcNAcylated recombinant proteins, but the plasmids used were not compatible, and the expression of both OGT and its target protein were induced by the same inducer.
25619971	1	59	from	modification	199:210	arg1	metazoans					215:223	metazoans	215:223	metazoans	215:223	O-GlcNAcylation is a ubiquitous, dynamic and reversible post-translational protein modification in metazoans, and it is catalysed and removed by O-GlcNAc transferase (OGT) and O-GlcNAcase, respectively.
25619971	1	60	theme	ubiquitous	137:146	arg1	modification					199:210	a ubiquitous, dynamic and reversible post-translational protein modification	135:210	a ubiquitous, dynamic and reversible post-translational protein modification in metazoans	135:223	O-GlcNAcylation is a ubiquitous, dynamic and reversible post-translational protein modification in metazoans, and it is catalysed and removed by O-GlcNAc transferase (OGT) and O-GlcNAcase, respectively.
25619971	1	60	theme	ubiquitous	137:146	arg1	O-GlcNAcylation					116:130	O-GlcNAcylation	116:130	O-GlcNAcylation	116:130	O-GlcNAcylation is a ubiquitous, dynamic and reversible post-translational protein modification in metazoans, and it is catalysed and removed by O-GlcNAc transferase (OGT) and O-GlcNAcase, respectively.
25619971	5	61	theme	p53	836:838	arg1	protein					840:846	p53 protein	836:846	p53 protein	836:846	The approach was validated using the CKII and p53 protein as control.
25619971	6	62	theme	OGT	1021:1023	arg1	vector					1053:1058	an isopropyl β-d-thiogalactopyranoside-inducible OGT target substrate expression vector	972:1058	an isopropyl β-d-thiogalactopyranoside-inducible OGT target substrate expression vector bearing a p15A origin	972:1080	This compatible dual plasmid system contains an arabinose-inducible OGT expression vector with a pUC origin and an isopropyl β-d-thiogalactopyranoside-inducible OGT target substrate expression vector bearing a p15A origin.
25619971	7	63	theme	inducer	1189:1195	arg1	concentration					1197:1209	the inducer concentration	1185:1209	the inducer concentration	1185:1209	The dual plasmid system produces recombinant proteins with varying O-GlcNAcylation levels by altering the inducer concentration.
25619971	3	64	from	substrates	433:442	arg1	coli					459:462	Escherichia coli	447:462	Escherichia coli	447:462	It has been reported that coexpression of mammalian OGT with its target substrates in Escherichia coli produce O-GlcNAcylated recombinant proteins, but the plasmids used were not compatible, and the expression of both OGT and its target protein were induced by the same inducer.
25619971	6	65	theme	β-d-thiogalactopyranoside-inducible	985:1019	arg1	vector					1053:1058	an isopropyl β-d-thiogalactopyranoside-inducible OGT target substrate expression vector	972:1058	an isopropyl β-d-thiogalactopyranoside-inducible OGT target substrate expression vector bearing a p15A origin	972:1080	This compatible dual plasmid system contains an arabinose-inducible OGT expression vector with a pUC origin and an isopropyl β-d-thiogalactopyranoside-inducible OGT target substrate expression vector bearing a p15A origin.
30462203	0	0	theme	recombinant	82:92	arg1	protein					94:100	highly O-GlcNAcylated recombinant protein	60:100	highly O-GlcNAcylated recombinant protein	60:100	A widely compatible expression system for the production of highly O-GlcNAcylated recombinant protein in Escherichia coli.
30462203	1	1	theme	dynamic	159:165	arg1	modification					186:197	a ubiquitous and dynamic post-translational modification	142:197	a ubiquitous and dynamic post-translational modification	142:197	O-GlcNAcylation is a ubiquitous and dynamic post-translational modification on serine/threonine residues of nucleocytoplasmic proteins in metazoa, which plays a critical role in numerous physiological and pathological processes.
30462203	1	1	theme	dynamic	159:165	arg1	O-GlcNAcylation					123:137	O-GlcNAcylation	123:137	O-GlcNAcylation	123:137	O-GlcNAcylation is a ubiquitous and dynamic post-translational modification on serine/threonine residues of nucleocytoplasmic proteins in metazoa, which plays a critical role in numerous physiological and pathological processes.
30462203	7	2	theme	enzymatic	1637:1645	arg1	activity					1647:1654	enzymatic activity	1637:1654	enzymatic activity	1637:1654	This new expression system provides possibility for investigating the roles of O-GlcNAcylation in the enzymatic activity, protein-protein interaction and structure of OGT target proteins.
30462203	0	3	theme	O-GlcNAcylated	67:80	arg1	protein					94:100	highly O-GlcNAcylated recombinant protein	60:100	highly O-GlcNAcylated recombinant protein	60:100	A widely compatible expression system for the production of highly O-GlcNAcylated recombinant protein in Escherichia coli.
30462203	5	4	from	UDP-GlcNAc	1162:1171	arg1	coli					1179:1182	E. coli	1176:1182	E. coli	1176:1182	The results revealed that the expression of GlmM and GlmU increases the cellular concentration of UDP-GlcNAc in E. coli, which markedly enhanced the activity of the co-expressed OGT to its target proteins, such as H2B, p53 and TAB1.
30462203	1	5	theme	post-translational	167:184	arg1	modification					186:197	a ubiquitous and dynamic post-translational modification	142:197	a ubiquitous and dynamic post-translational modification	142:197	O-GlcNAcylation is a ubiquitous and dynamic post-translational modification on serine/threonine residues of nucleocytoplasmic proteins in metazoa, which plays a critical role in numerous physiological and pathological processes.
30462203	1	5	theme	post-translational	167:184	arg1	O-GlcNAcylation					123:137	O-GlcNAcylation	123:137	O-GlcNAcylation	123:137	O-GlcNAcylation is a ubiquitous and dynamic post-translational modification on serine/threonine residues of nucleocytoplasmic proteins in metazoa, which plays a critical role in numerous physiological and pathological processes.
30462203	1	6	theme	critical	284:291	arg1	role					293:296	a critical role	282:296	a critical role	282:296	O-GlcNAcylation is a ubiquitous and dynamic post-translational modification on serine/threonine residues of nucleocytoplasmic proteins in metazoa, which plays a critical role in numerous physiological and pathological processes.
30462203	6	7	dep	compatible	1333:1342	arg1	E.					1344:1345	E.	1344:1345	E.	1344:1345	Altogether, we established a widely compatible E. coli expression system for producing highly O-GlcNAcylated protein, which could be used for modifying OGT target proteins expressed by almost any commercial expression vectors in E. coli.
30462203	6	8	used	used	1430:1433	arg2	protein					1406:1412	highly O-GlcNAcylated protein	1384:1412	highly O-GlcNAcylated protein	1384:1412	Altogether, we established a widely compatible E. coli expression system for producing highly O-GlcNAcylated protein, which could be used for modifying OGT target proteins expressed by almost any commercial expression vectors in E. coli.
30462203	6	9	theme	compatible	1333:1342	arg1	system					1363:1368	a widely compatible E. coli expression system	1324:1368	a widely compatible E. coli expression system for producing highly O-GlcNAcylated protein, which could be used for modifying OGT target proteins expressed by almost any commercial expression vectors in E. coli	1324:1532	Altogether, we established a widely compatible E. coli expression system for producing highly O-GlcNAcylated protein, which could be used for modifying OGT target proteins expressed by almost any commercial expression vectors in E. coli.
30462203	2	10	from	O-GlcNAcylation	360:374	arg1	proteins					384:391	most proteins	379:391	most proteins	379:391	But the O-GlcNAcylation on most proteins is often substoichiometric, which hinders the functional study of the O-GlcNAcylation.
30462203	3	11	dep	coli	584:587	arg1	coli					593:596	E. coli	590:596	E. coli	590:596	This study aimed to improve the production of highly O-GlcNAcylated recombinant proteins in Escherichia coli (E. coli).
30462203	7	12	from	roles	1605:1609	arg1	structure					1689:1697	structure	1689:1697	structure	1689:1697	This new expression system provides possibility for investigating the roles of O-GlcNAcylation in the enzymatic activity, protein-protein interaction and structure of OGT target proteins.
30462203	7	12	from	roles	1605:1609	arg1	activity					1647:1654	enzymatic activity	1637:1654	enzymatic activity	1637:1654	This new expression system provides possibility for investigating the roles of O-GlcNAcylation in the enzymatic activity, protein-protein interaction and structure of OGT target proteins.
30462203	7	12	from	roles	1605:1609	arg1	interaction					1673:1683	protein-protein interaction	1657:1683	protein-protein interaction	1657:1683	This new expression system provides possibility for investigating the roles of O-GlcNAcylation in the enzymatic activity, protein-protein interaction and structure of OGT target proteins.
30462203	0	13	theme	protein	94:100	arg1	production					46:55	the production	42:55	the production of highly O-GlcNAcylated recombinant protein in Escherichia coli	42:120	A widely compatible expression system for the production of highly O-GlcNAcylated recombinant protein in Escherichia coli.
30462203	0	14	from	production	46:55	arg1	coli					117:120	Escherichia coli	105:120	Escherichia coli	105:120	A widely compatible expression system for the production of highly O-GlcNAcylated recombinant protein in Escherichia coli.
30462203	3	15	theme	proteins	560:567	arg1	production					512:521	the production	508:521	the production of highly O-GlcNAcylated recombinant proteins in Escherichia coli (E. coli)	508:597	This study aimed to improve the production of highly O-GlcNAcylated recombinant proteins in Escherichia coli (E. coli).
30462203	4	16	theme	key	766:768	arg1	GlmM					802:805	GlmM	802:805	GlmM	802:805	To achieve this goal, we constructed a bacterial artificial chromosome-based chloramphenicol-resistant expression vector co-expressing O-GlcNAc transferase (OGT) and key enzymes (phosphoglucose mutase, GlmM and N-acetylglucosamine-1-phosphate uridyltransferase, GlmU) of the uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) synthesis pathway in E. coli, which can effectively increase the O-GlcNAcylation of the OGT target protein expressed by another vector.
30462203	4	16	theme	key	766:768	arg1	enzymes					770:776	key enzymes	766:776	key enzymes (phosphoglucose mutase, GlmM and N-acetylglucosamine-1-phosphate uridyltransferase, GlmU)	766:866	To achieve this goal, we constructed a bacterial artificial chromosome-based chloramphenicol-resistant expression vector co-expressing O-GlcNAc transferase (OGT) and key enzymes (phosphoglucose mutase, GlmM and N-acetylglucosamine-1-phosphate uridyltransferase, GlmU) of the uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) synthesis pathway in E. coli, which can effectively increase the O-GlcNAcylation of the OGT target protein expressed by another vector.
30462203	4	16	theme	key	766:768	arg1	mutase					794:799	phosphoglucose mutase	779:799	phosphoglucose mutase	779:799	To achieve this goal, we constructed a bacterial artificial chromosome-based chloramphenicol-resistant expression vector co-expressing O-GlcNAc transferase (OGT) and key enzymes (phosphoglucose mutase, GlmM and N-acetylglucosamine-1-phosphate uridyltransferase, GlmU) of the uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) synthesis pathway in E. coli, which can effectively increase the O-GlcNAcylation of the OGT target protein expressed by another vector.
30462203	4	16	theme	key	766:768	arg1	uridyltransferase					843:859	N-acetylglucosamine-1-phosphate uridyltransferase	811:859	N-acetylglucosamine-1-phosphate uridyltransferase	811:859	To achieve this goal, we constructed a bacterial artificial chromosome-based chloramphenicol-resistant expression vector co-expressing O-GlcNAc transferase (OGT) and key enzymes (phosphoglucose mutase, GlmM and N-acetylglucosamine-1-phosphate uridyltransferase, GlmU) of the uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) synthesis pathway in E. coli, which can effectively increase the O-GlcNAcylation of the OGT target protein expressed by another vector.
30462203	4	17	theme	phosphoglucose	779:792	arg1	enzymes					770:776	key enzymes	766:776	key enzymes (phosphoglucose mutase, GlmM and N-acetylglucosamine-1-phosphate uridyltransferase, GlmU)	766:866	To achieve this goal, we constructed a bacterial artificial chromosome-based chloramphenicol-resistant expression vector co-expressing O-GlcNAc transferase (OGT) and key enzymes (phosphoglucose mutase, GlmM and N-acetylglucosamine-1-phosphate uridyltransferase, GlmU) of the uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) synthesis pathway in E. coli, which can effectively increase the O-GlcNAcylation of the OGT target protein expressed by another vector.
30462203	4	17	theme	phosphoglucose	779:792	arg1	mutase					794:799	phosphoglucose mutase	779:799	phosphoglucose mutase	779:799	To achieve this goal, we constructed a bacterial artificial chromosome-based chloramphenicol-resistant expression vector co-expressing O-GlcNAc transferase (OGT) and key enzymes (phosphoglucose mutase, GlmM and N-acetylglucosamine-1-phosphate uridyltransferase, GlmU) of the uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) synthesis pathway in E. coli, which can effectively increase the O-GlcNAcylation of the OGT target protein expressed by another vector.
30462203	4	18	theme	chloramphenicol-resistant	677:701	arg1	vector					714:719	a bacterial artificial chromosome-based chloramphenicol-resistant expression vector	637:719	a bacterial artificial chromosome-based chloramphenicol-resistant expression vector	637:719	To achieve this goal, we constructed a bacterial artificial chromosome-based chloramphenicol-resistant expression vector co-expressing O-GlcNAc transferase (OGT) and key enzymes (phosphoglucose mutase, GlmM and N-acetylglucosamine-1-phosphate uridyltransferase, GlmU) of the uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) synthesis pathway in E. coli, which can effectively increase the O-GlcNAcylation of the OGT target protein expressed by another vector.
30462203	2	19	theme	functional	439:448	arg1	study					450:454	the functional study	435:454	the functional study of the O-GlcNAcylation	435:477	But the O-GlcNAcylation on most proteins is often substoichiometric, which hinders the functional study of the O-GlcNAcylation.
30462203	6	20	dep	E.	1344:1345	arg1	coli					1347:1350	coli	1347:1350	coli	1347:1350	Altogether, we established a widely compatible E. coli expression system for producing highly O-GlcNAcylated protein, which could be used for modifying OGT target proteins expressed by almost any commercial expression vectors in E. coli.
30462203	7	21	theme	protein-protein	1657:1671	arg1	interaction					1673:1683	protein-protein interaction	1657:1683	protein-protein interaction	1657:1683	This new expression system provides possibility for investigating the roles of O-GlcNAcylation in the enzymatic activity, protein-protein interaction and structure of OGT target proteins.
30462203	4	22	theme	O-GlcNAc	735:742	arg1	transferase					744:754	O-GlcNAc transferase	735:754	O-GlcNAc transferase (OGT)	735:760	To achieve this goal, we constructed a bacterial artificial chromosome-based chloramphenicol-resistant expression vector co-expressing O-GlcNAc transferase (OGT) and key enzymes (phosphoglucose mutase, GlmM and N-acetylglucosamine-1-phosphate uridyltransferase, GlmU) of the uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) synthesis pathway in E. coli, which can effectively increase the O-GlcNAcylation of the OGT target protein expressed by another vector.
30462203	4	22	theme	O-GlcNAc	735:742	arg1	OGT					757:759	OGT	757:759	OGT	757:759	To achieve this goal, we constructed a bacterial artificial chromosome-based chloramphenicol-resistant expression vector co-expressing O-GlcNAc transferase (OGT) and key enzymes (phosphoglucose mutase, GlmM and N-acetylglucosamine-1-phosphate uridyltransferase, GlmU) of the uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) synthesis pathway in E. coli, which can effectively increase the O-GlcNAcylation of the OGT target protein expressed by another vector.
30462203	4	23	from	pathway	938:944	arg1	coli					952:955	E. coli	949:955	E. coli	949:955	To achieve this goal, we constructed a bacterial artificial chromosome-based chloramphenicol-resistant expression vector co-expressing O-GlcNAc transferase (OGT) and key enzymes (phosphoglucose mutase, GlmM and N-acetylglucosamine-1-phosphate uridyltransferase, GlmU) of the uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) synthesis pathway in E. coli, which can effectively increase the O-GlcNAcylation of the OGT target protein expressed by another vector.
30462203	5	24	theme	target	1253:1258	arg1	proteins					1260:1267	its target proteins	1249:1267	its target proteins	1249:1267	The results revealed that the expression of GlmM and GlmU increases the cellular concentration of UDP-GlcNAc in E. coli, which markedly enhanced the activity of the co-expressed OGT to its target proteins, such as H2B, p53 and TAB1.
30462203	5	24	theme	target	1253:1258	arg1	p53					1283:1285	p53	1283:1285	p53	1283:1285	The results revealed that the expression of GlmM and GlmU increases the cellular concentration of UDP-GlcNAc in E. coli, which markedly enhanced the activity of the co-expressed OGT to its target proteins, such as H2B, p53 and TAB1.
30462203	5	24	theme	target	1253:1258	arg1	H2B					1278:1280	H2B	1278:1280	H2B	1278:1280	The results revealed that the expression of GlmM and GlmU increases the cellular concentration of UDP-GlcNAc in E. coli, which markedly enhanced the activity of the co-expressed OGT to its target proteins, such as H2B, p53 and TAB1.
30462203	5	24	theme	target	1253:1258	arg1	TAB1					1291:1294	TAB1	1291:1294	TAB1	1291:1294	The results revealed that the expression of GlmM and GlmU increases the cellular concentration of UDP-GlcNAc in E. coli, which markedly enhanced the activity of the co-expressed OGT to its target proteins, such as H2B, p53 and TAB1.
30462203	1	25	theme	serine/threonine	202:217	arg1	residues					219:226	serine/threonine residues	202:226	serine/threonine residues of nucleocytoplasmic proteins in metazoa	202:267	O-GlcNAcylation is a ubiquitous and dynamic post-translational modification on serine/threonine residues of nucleocytoplasmic proteins in metazoa, which plays a critical role in numerous physiological and pathological processes.
30462203	1	25	theme	serine/threonine	202:217	arg1	proteins					249:256	nucleocytoplasmic proteins	231:256	nucleocytoplasmic proteins in metazoa	231:267	O-GlcNAcylation is a ubiquitous and dynamic post-translational modification on serine/threonine residues of nucleocytoplasmic proteins in metazoa, which plays a critical role in numerous physiological and pathological processes.
30462203	6	26	theme	expression	1504:1513	arg1	vectors					1515:1521	almost any commercial expression vectors	1482:1521	almost any commercial expression vectors	1482:1521	Altogether, we established a widely compatible E. coli expression system for producing highly O-GlcNAcylated protein, which could be used for modifying OGT target proteins expressed by almost any commercial expression vectors in E. coli.
30462203	1	27	theme	numerous	301:308	arg1	processes					341:349	numerous physiological and pathological processes	301:349	numerous physiological and pathological processes	301:349	O-GlcNAcylation is a ubiquitous and dynamic post-translational modification on serine/threonine residues of nucleocytoplasmic proteins in metazoa, which plays a critical role in numerous physiological and pathological processes.
30462203	4	28	dep	mutase	794:799	arg1	GlmU					862:865	GlmU	862:865	GlmU	862:865	To achieve this goal, we constructed a bacterial artificial chromosome-based chloramphenicol-resistant expression vector co-expressing O-GlcNAc transferase (OGT) and key enzymes (phosphoglucose mutase, GlmM and N-acetylglucosamine-1-phosphate uridyltransferase, GlmU) of the uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) synthesis pathway in E. coli, which can effectively increase the O-GlcNAcylation of the OGT target protein expressed by another vector.
30462203	7	29	theme	O-GlcNAcylation	1614:1628	arg1	roles					1605:1609	the roles	1601:1609	the roles of O-GlcNAcylation in the enzymatic activity, protein-protein interaction and structure of OGT target proteins	1601:1720	This new expression system provides possibility for investigating the roles of O-GlcNAcylation in the enzymatic activity, protein-protein interaction and structure of OGT target proteins.
30462203	0	30	theme	expression	20:29	arg1	system					31:36	A widely compatible expression system	0:36	A widely compatible expression system for the production of highly O-GlcNAcylated recombinant protein in Escherichia coli	0:120	A widely compatible expression system for the production of highly O-GlcNAcylated recombinant protein in Escherichia coli.
30462203	1	31	theme	physiological	310:322	arg1	processes					341:349	numerous physiological and pathological processes	301:349	numerous physiological and pathological processes	301:349	O-GlcNAcylation is a ubiquitous and dynamic post-translational modification on serine/threonine residues of nucleocytoplasmic proteins in metazoa, which plays a critical role in numerous physiological and pathological processes.
30462203	4	32	theme	OGT	1016:1018	arg1	protein					1027:1033	the OGT target protein	1012:1033	the OGT target protein expressed by another vector	1012:1061	To achieve this goal, we constructed a bacterial artificial chromosome-based chloramphenicol-resistant expression vector co-expressing O-GlcNAc transferase (OGT) and key enzymes (phosphoglucose mutase, GlmM and N-acetylglucosamine-1-phosphate uridyltransferase, GlmU) of the uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) synthesis pathway in E. coli, which can effectively increase the O-GlcNAcylation of the OGT target protein expressed by another vector.
30462203	5	33	theme	GlmM	1108:1111	arg1	expression					1094:1103	the expression	1090:1103	the expression of GlmM and GlmU	1090:1120	The results revealed that the expression of GlmM and GlmU increases the cellular concentration of UDP-GlcNAc in E. coli, which markedly enhanced the activity of the co-expressed OGT to its target proteins, such as H2B, p53 and TAB1.
30462203	2	34	theme	O-GlcNAcylation	463:477	arg1	study					450:454	the functional study	435:454	the functional study of the O-GlcNAcylation	435:477	But the O-GlcNAcylation on most proteins is often substoichiometric, which hinders the functional study of the O-GlcNAcylation.
30462203	0	35	theme	compatible	9:18	arg1	system					31:36	A widely compatible expression system	0:36	A widely compatible expression system for the production of highly O-GlcNAcylated recombinant protein in Escherichia coli	0:120	A widely compatible expression system for the production of highly O-GlcNAcylated recombinant protein in Escherichia coli.
30462203	7	36	theme	proteins	1713:1720	arg1	structure					1689:1697	structure	1689:1697	structure	1689:1697	This new expression system provides possibility for investigating the roles of O-GlcNAcylation in the enzymatic activity, protein-protein interaction and structure of OGT target proteins.
30462203	7	36	theme	proteins	1713:1720	arg1	activity					1647:1654	enzymatic activity	1637:1654	enzymatic activity	1637:1654	This new expression system provides possibility for investigating the roles of O-GlcNAcylation in the enzymatic activity, protein-protein interaction and structure of OGT target proteins.
30462203	7	36	theme	proteins	1713:1720	arg1	interaction					1673:1683	protein-protein interaction	1657:1683	protein-protein interaction	1657:1683	This new expression system provides possibility for investigating the roles of O-GlcNAcylation in the enzymatic activity, protein-protein interaction and structure of OGT target proteins.
30462203	5	37	theme	UDP-GlcNAc	1162:1171	arg1	concentration					1145:1157	the cellular concentration	1132:1157	the cellular concentration of UDP-GlcNAc in E. coli, which markedly enhanced the activity of the co-expressed OGT to its target proteins, such as H2B, p53 and TAB1	1132:1294	The results revealed that the expression of GlmM and GlmU increases the cellular concentration of UDP-GlcNAc in E. coli, which markedly enhanced the activity of the co-expressed OGT to its target proteins, such as H2B, p53 and TAB1.
30462203	3	38	theme	recombinant	548:558	arg1	proteins					560:567	highly O-GlcNAcylated recombinant proteins	526:567	highly O-GlcNAcylated recombinant proteins	526:567	This study aimed to improve the production of highly O-GlcNAcylated recombinant proteins in Escherichia coli (E. coli).
30462203	5	39	theme	GlmU	1117:1120	arg1	expression					1094:1103	the expression	1090:1103	the expression of GlmM and GlmU	1090:1120	The results revealed that the expression of GlmM and GlmU increases the cellular concentration of UDP-GlcNAc in E. coli, which markedly enhanced the activity of the co-expressed OGT to its target proteins, such as H2B, p53 and TAB1.
30462203	1	40	theme	nucleocytoplasmic	231:247	arg1	proteins					249:256	nucleocytoplasmic proteins	231:256	nucleocytoplasmic proteins in metazoa	231:267	O-GlcNAcylation is a ubiquitous and dynamic post-translational modification on serine/threonine residues of nucleocytoplasmic proteins in metazoa, which plays a critical role in numerous physiological and pathological processes.
30462203	1	41	theme	pathological	328:339	arg1	processes					341:349	numerous physiological and pathological processes	301:349	numerous physiological and pathological processes	301:349	O-GlcNAcylation is a ubiquitous and dynamic post-translational modification on serine/threonine residues of nucleocytoplasmic proteins in metazoa, which plays a critical role in numerous physiological and pathological processes.
30462203	4	42	theme	protein	1027:1033	arg1	O-GlcNAcylation					993:1007	the O-GlcNAcylation	989:1007	the O-GlcNAcylation of the OGT target protein expressed by another vector	989:1061	To achieve this goal, we constructed a bacterial artificial chromosome-based chloramphenicol-resistant expression vector co-expressing O-GlcNAc transferase (OGT) and key enzymes (phosphoglucose mutase, GlmM and N-acetylglucosamine-1-phosphate uridyltransferase, GlmU) of the uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) synthesis pathway in E. coli, which can effectively increase the O-GlcNAcylation of the OGT target protein expressed by another vector.
30462203	7	43	theme	target	1706:1711	arg1	proteins					1713:1720	OGT target proteins	1702:1720	OGT target proteins	1702:1720	This new expression system provides possibility for investigating the roles of O-GlcNAcylation in the enzymatic activity, protein-protein interaction and structure of OGT target proteins.
30462203	4	44	theme	UDP-GlcNAc	916:925	arg1	pathway					938:944	the uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) synthesis pathway	871:944	the uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) synthesis pathway in E. coli	871:955	To achieve this goal, we constructed a bacterial artificial chromosome-based chloramphenicol-resistant expression vector co-expressing O-GlcNAc transferase (OGT) and key enzymes (phosphoglucose mutase, GlmM and N-acetylglucosamine-1-phosphate uridyltransferase, GlmU) of the uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) synthesis pathway in E. coli, which can effectively increase the O-GlcNAcylation of the OGT target protein expressed by another vector.
30462203	1	45	theme	proteins	249:256	arg1	residues					219:226	serine/threonine residues	202:226	serine/threonine residues of nucleocytoplasmic proteins in metazoa	202:267	O-GlcNAcylation is a ubiquitous and dynamic post-translational modification on serine/threonine residues of nucleocytoplasmic proteins in metazoa, which plays a critical role in numerous physiological and pathological processes.
30462203	1	45	theme	proteins	249:256	arg1	proteins					249:256	nucleocytoplasmic proteins	231:256	nucleocytoplasmic proteins in metazoa	231:267	O-GlcNAcylation is a ubiquitous and dynamic post-translational modification on serine/threonine residues of nucleocytoplasmic proteins in metazoa, which plays a critical role in numerous physiological and pathological processes.
30462203	5	46	theme	co-expressed	1229:1240	arg1	OGT					1242:1244	the co-expressed OGT	1225:1244	the co-expressed OGT	1225:1244	The results revealed that the expression of GlmM and GlmU increases the cellular concentration of UDP-GlcNAc in E. coli, which markedly enhanced the activity of the co-expressed OGT to its target proteins, such as H2B, p53 and TAB1.
30462203	4	47	theme	target	1020:1025	arg1	protein					1027:1033	the OGT target protein	1012:1033	the OGT target protein expressed by another vector	1012:1061	To achieve this goal, we constructed a bacterial artificial chromosome-based chloramphenicol-resistant expression vector co-expressing O-GlcNAc transferase (OGT) and key enzymes (phosphoglucose mutase, GlmM and N-acetylglucosamine-1-phosphate uridyltransferase, GlmU) of the uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) synthesis pathway in E. coli, which can effectively increase the O-GlcNAcylation of the OGT target protein expressed by another vector.
30462203	6	48	theme	O-GlcNAcylated	1391:1404	arg1	protein					1406:1412	highly O-GlcNAcylated protein	1384:1412	highly O-GlcNAcylated protein	1384:1412	Altogether, we established a widely compatible E. coli expression system for producing highly O-GlcNAcylated protein, which could be used for modifying OGT target proteins expressed by almost any commercial expression vectors in E. coli.
30462203	6	49	theme	commercial	1493:1502	arg1	vectors					1515:1521	almost any commercial expression vectors	1482:1521	almost any commercial expression vectors	1482:1521	Altogether, we established a widely compatible E. coli expression system for producing highly O-GlcNAcylated protein, which could be used for modifying OGT target proteins expressed by almost any commercial expression vectors in E. coli.
30462203	1	50	from	proteins	249:256	arg1	metazoa					261:267	metazoa	261:267	metazoa	261:267	O-GlcNAcylation is a ubiquitous and dynamic post-translational modification on serine/threonine residues of nucleocytoplasmic proteins in metazoa, which plays a critical role in numerous physiological and pathological processes.
30462203	7	51	theme	OGT	1702:1704	arg1	proteins					1713:1720	OGT target proteins	1702:1720	OGT target proteins	1702:1720	This new expression system provides possibility for investigating the roles of O-GlcNAcylation in the enzymatic activity, protein-protein interaction and structure of OGT target proteins.
30462203	5	52	theme	OGT	1242:1244	arg1	activity					1213:1220	the activity	1209:1220	the activity of the co-expressed OGT to its target proteins, such as H2B, p53 and TAB1	1209:1294	The results revealed that the expression of GlmM and GlmU increases the cellular concentration of UDP-GlcNAc in E. coli, which markedly enhanced the activity of the co-expressed OGT to its target proteins, such as H2B, p53 and TAB1.
30462203	4	53	theme	synthesis	928:936	arg1	pathway					938:944	the uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) synthesis pathway	871:944	the uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) synthesis pathway in E. coli	871:955	To achieve this goal, we constructed a bacterial artificial chromosome-based chloramphenicol-resistant expression vector co-expressing O-GlcNAc transferase (OGT) and key enzymes (phosphoglucose mutase, GlmM and N-acetylglucosamine-1-phosphate uridyltransferase, GlmU) of the uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) synthesis pathway in E. coli, which can effectively increase the O-GlcNAcylation of the OGT target protein expressed by another vector.
30462203	3	54	theme	O-GlcNAcylated	533:546	arg1	proteins					560:567	highly O-GlcNAcylated recombinant proteins	526:567	highly O-GlcNAcylated recombinant proteins	526:567	This study aimed to improve the production of highly O-GlcNAcylated recombinant proteins in Escherichia coli (E. coli).
30462203	7	55	theme	new	1540:1542	arg1	system					1555:1560	This new expression system	1535:1560	This new expression system	1535:1560	This new expression system provides possibility for investigating the roles of O-GlcNAcylation in the enzymatic activity, protein-protein interaction and structure of OGT target proteins.
30462203	2	56	theme	most	379:382	arg1	proteins					384:391	most proteins	379:391	most proteins	379:391	But the O-GlcNAcylation on most proteins is often substoichiometric, which hinders the functional study of the O-GlcNAcylation.
30462203	4	57	theme	diphosphate	883:893	arg1	pathway					938:944	the uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) synthesis pathway	871:944	the uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) synthesis pathway in E. coli	871:955	To achieve this goal, we constructed a bacterial artificial chromosome-based chloramphenicol-resistant expression vector co-expressing O-GlcNAc transferase (OGT) and key enzymes (phosphoglucose mutase, GlmM and N-acetylglucosamine-1-phosphate uridyltransferase, GlmU) of the uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) synthesis pathway in E. coli, which can effectively increase the O-GlcNAcylation of the OGT target protein expressed by another vector.
30462203	1	58	from	metazoa	261:267	arg1	residues					219:226	serine/threonine residues	202:226	serine/threonine residues of nucleocytoplasmic proteins in metazoa	202:267	O-GlcNAcylation is a ubiquitous and dynamic post-translational modification on serine/threonine residues of nucleocytoplasmic proteins in metazoa, which plays a critical role in numerous physiological and pathological processes.
30462203	1	58	from	metazoa	261:267	arg1	proteins					249:256	nucleocytoplasmic proteins	231:256	nucleocytoplasmic proteins in metazoa	231:267	O-GlcNAcylation is a ubiquitous and dynamic post-translational modification on serine/threonine residues of nucleocytoplasmic proteins in metazoa, which plays a critical role in numerous physiological and pathological processes.
30462203	5	59	theme	cellular	1136:1143	arg1	concentration					1145:1157	the cellular concentration	1132:1157	the cellular concentration of UDP-GlcNAc in E. coli, which markedly enhanced the activity of the co-expressed OGT to its target proteins, such as H2B, p53 and TAB1	1132:1294	The results revealed that the expression of GlmM and GlmU increases the cellular concentration of UDP-GlcNAc in E. coli, which markedly enhanced the activity of the co-expressed OGT to its target proteins, such as H2B, p53 and TAB1.
30462203	4	60	theme	uridine	875:881	arg1	pathway					938:944	the uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) synthesis pathway	871:944	the uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) synthesis pathway in E. coli	871:955	To achieve this goal, we constructed a bacterial artificial chromosome-based chloramphenicol-resistant expression vector co-expressing O-GlcNAc transferase (OGT) and key enzymes (phosphoglucose mutase, GlmM and N-acetylglucosamine-1-phosphate uridyltransferase, GlmU) of the uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) synthesis pathway in E. coli, which can effectively increase the O-GlcNAcylation of the OGT target protein expressed by another vector.
30462203	3	61	from	production	512:521	arg1	coli					584:587	Escherichia coli	572:587	Escherichia coli (E. coli)	572:597	This study aimed to improve the production of highly O-GlcNAcylated recombinant proteins in Escherichia coli (E. coli).
30462203	4	62	theme	bacterial	639:647	arg1	vector					714:719	a bacterial artificial chromosome-based chloramphenicol-resistant expression vector	637:719	a bacterial artificial chromosome-based chloramphenicol-resistant expression vector	637:719	To achieve this goal, we constructed a bacterial artificial chromosome-based chloramphenicol-resistant expression vector co-expressing O-GlcNAc transferase (OGT) and key enzymes (phosphoglucose mutase, GlmM and N-acetylglucosamine-1-phosphate uridyltransferase, GlmU) of the uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) synthesis pathway in E. coli, which can effectively increase the O-GlcNAcylation of the OGT target protein expressed by another vector.
30462203	6	63	theme	expression	1352:1361	arg1	system					1363:1368	a widely compatible E. coli expression system	1324:1368	a widely compatible E. coli expression system for producing highly O-GlcNAcylated protein, which could be used for modifying OGT target proteins expressed by almost any commercial expression vectors in E. coli	1324:1532	Altogether, we established a widely compatible E. coli expression system for producing highly O-GlcNAcylated protein, which could be used for modifying OGT target proteins expressed by almost any commercial expression vectors in E. coli.
30462203	6	64	theme	target	1453:1458	arg1	proteins					1460:1467	OGT target proteins	1449:1467	OGT target proteins expressed by almost any commercial expression vectors in E. coli	1449:1532	Altogether, we established a widely compatible E. coli expression system for producing highly O-GlcNAcylated protein, which could be used for modifying OGT target proteins expressed by almost any commercial expression vectors in E. coli.
30462203	4	65	theme	N-acetylglucosamine-1-phosphate	811:841	arg1	uridyltransferase					843:859	N-acetylglucosamine-1-phosphate uridyltransferase	811:859	N-acetylglucosamine-1-phosphate uridyltransferase	811:859	To achieve this goal, we constructed a bacterial artificial chromosome-based chloramphenicol-resistant expression vector co-expressing O-GlcNAc transferase (OGT) and key enzymes (phosphoglucose mutase, GlmM and N-acetylglucosamine-1-phosphate uridyltransferase, GlmU) of the uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) synthesis pathway in E. coli, which can effectively increase the O-GlcNAcylation of the OGT target protein expressed by another vector.
30462203	4	65	theme	N-acetylglucosamine-1-phosphate	811:841	arg1	enzymes					770:776	key enzymes	766:776	key enzymes (phosphoglucose mutase, GlmM and N-acetylglucosamine-1-phosphate uridyltransferase, GlmU)	766:866	To achieve this goal, we constructed a bacterial artificial chromosome-based chloramphenicol-resistant expression vector co-expressing O-GlcNAc transferase (OGT) and key enzymes (phosphoglucose mutase, GlmM and N-acetylglucosamine-1-phosphate uridyltransferase, GlmU) of the uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) synthesis pathway in E. coli, which can effectively increase the O-GlcNAcylation of the OGT target protein expressed by another vector.
30462203	5	66	from	coli	1179:1182	arg1	concentration					1145:1157	the cellular concentration	1132:1157	the cellular concentration of UDP-GlcNAc in E. coli, which markedly enhanced the activity of the co-expressed OGT to its target proteins, such as H2B, p53 and TAB1	1132:1294	The results revealed that the expression of GlmM and GlmU increases the cellular concentration of UDP-GlcNAc in E. coli, which markedly enhanced the activity of the co-expressed OGT to its target proteins, such as H2B, p53 and TAB1.
30462203	6	67	theme	any	1489:1491	arg1	vectors					1515:1521	almost any commercial expression vectors	1482:1521	almost any commercial expression vectors	1482:1521	Altogether, we established a widely compatible E. coli expression system for producing highly O-GlcNAcylated protein, which could be used for modifying OGT target proteins expressed by almost any commercial expression vectors in E. coli.
30462203	5	68	from	concentration	1145:1157	arg1	coli					1179:1182	E. coli	1176:1182	E. coli	1176:1182	The results revealed that the expression of GlmM and GlmU increases the cellular concentration of UDP-GlcNAc in E. coli, which markedly enhanced the activity of the co-expressed OGT to its target proteins, such as H2B, p53 and TAB1.
30462203	7	69	dep	activity	1647:1654	arg1	the					1633:1635	the	1633:1635	the	1633:1635	This new expression system provides possibility for investigating the roles of O-GlcNAcylation in the enzymatic activity, protein-protein interaction and structure of OGT target proteins.
30462203	4	70	theme	N-acetylglucosamine	895:913	arg1	pathway					938:944	the uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) synthesis pathway	871:944	the uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) synthesis pathway in E. coli	871:955	To achieve this goal, we constructed a bacterial artificial chromosome-based chloramphenicol-resistant expression vector co-expressing O-GlcNAc transferase (OGT) and key enzymes (phosphoglucose mutase, GlmM and N-acetylglucosamine-1-phosphate uridyltransferase, GlmU) of the uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) synthesis pathway in E. coli, which can effectively increase the O-GlcNAcylation of the OGT target protein expressed by another vector.
30462203	1	71	from	residues	219:226	arg1	metazoa					261:267	metazoa	261:267	metazoa	261:267	O-GlcNAcylation is a ubiquitous and dynamic post-translational modification on serine/threonine residues of nucleocytoplasmic proteins in metazoa, which plays a critical role in numerous physiological and pathological processes.
30462203	1	72	theme	ubiquitous	144:153	arg1	modification					186:197	a ubiquitous and dynamic post-translational modification	142:197	a ubiquitous and dynamic post-translational modification	142:197	O-GlcNAcylation is a ubiquitous and dynamic post-translational modification on serine/threonine residues of nucleocytoplasmic proteins in metazoa, which plays a critical role in numerous physiological and pathological processes.
30462203	1	72	theme	ubiquitous	144:153	arg1	O-GlcNAcylation					123:137	O-GlcNAcylation	123:137	O-GlcNAcylation	123:137	O-GlcNAcylation is a ubiquitous and dynamic post-translational modification on serine/threonine residues of nucleocytoplasmic proteins in metazoa, which plays a critical role in numerous physiological and pathological processes.
30462203	4	73	theme	chromosome-based	660:675	arg1	vector					714:719	a bacterial artificial chromosome-based chloramphenicol-resistant expression vector	637:719	a bacterial artificial chromosome-based chloramphenicol-resistant expression vector	637:719	To achieve this goal, we constructed a bacterial artificial chromosome-based chloramphenicol-resistant expression vector co-expressing O-GlcNAc transferase (OGT) and key enzymes (phosphoglucose mutase, GlmM and N-acetylglucosamine-1-phosphate uridyltransferase, GlmU) of the uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) synthesis pathway in E. coli, which can effectively increase the O-GlcNAcylation of the OGT target protein expressed by another vector.
30462203	6	74	theme	OGT	1449:1451	arg1	proteins					1460:1467	OGT target proteins	1449:1467	OGT target proteins expressed by almost any commercial expression vectors in E. coli	1449:1532	Altogether, we established a widely compatible E. coli expression system for producing highly O-GlcNAcylated protein, which could be used for modifying OGT target proteins expressed by almost any commercial expression vectors in E. coli.
30462203	7	75	theme	expression	1544:1553	arg1	system					1555:1560	This new expression system	1535:1560	This new expression system	1535:1560	This new expression system provides possibility for investigating the roles of O-GlcNAcylation in the enzymatic activity, protein-protein interaction and structure of OGT target proteins.
30462203	4	76	theme	expression	703:712	arg1	vector					714:719	a bacterial artificial chromosome-based chloramphenicol-resistant expression vector	637:719	a bacterial artificial chromosome-based chloramphenicol-resistant expression vector	637:719	To achieve this goal, we constructed a bacterial artificial chromosome-based chloramphenicol-resistant expression vector co-expressing O-GlcNAc transferase (OGT) and key enzymes (phosphoglucose mutase, GlmM and N-acetylglucosamine-1-phosphate uridyltransferase, GlmU) of the uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) synthesis pathway in E. coli, which can effectively increase the O-GlcNAcylation of the OGT target protein expressed by another vector.
30462203	1	77	from	modification	186:197	arg1	residues					219:226	serine/threonine residues	202:226	serine/threonine residues of nucleocytoplasmic proteins in metazoa	202:267	O-GlcNAcylation is a ubiquitous and dynamic post-translational modification on serine/threonine residues of nucleocytoplasmic proteins in metazoa, which plays a critical role in numerous physiological and pathological processes.
30462203	1	77	from	modification	186:197	arg1	proteins					249:256	nucleocytoplasmic proteins	231:256	nucleocytoplasmic proteins in metazoa	231:267	O-GlcNAcylation is a ubiquitous and dynamic post-translational modification on serine/threonine residues of nucleocytoplasmic proteins in metazoa, which plays a critical role in numerous physiological and pathological processes.
30462203	4	78	theme	artificial	649:658	arg1	vector					714:719	a bacterial artificial chromosome-based chloramphenicol-resistant expression vector	637:719	a bacterial artificial chromosome-based chloramphenicol-resistant expression vector	637:719	To achieve this goal, we constructed a bacterial artificial chromosome-based chloramphenicol-resistant expression vector co-expressing O-GlcNAc transferase (OGT) and key enzymes (phosphoglucose mutase, GlmM and N-acetylglucosamine-1-phosphate uridyltransferase, GlmU) of the uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) synthesis pathway in E. coli, which can effectively increase the O-GlcNAcylation of the OGT target protein expressed by another vector.
35308201	6	0	theme	c-Myc	638:642	arg1	modification					622:633	the O-GlcNAc modification	609:633	the O-GlcNAc modification of c-Myc and thus the stabilization of c-Myc, which is required for HCC tumorigenesis	609:719	Mechanistically, SLC35B4 is important for the O-GlcNAc modification of c-Myc and thus the stabilization of c-Myc, which is required for HCC tumorigenesis.
35308201	3	1	theme	hepatocellular	326:339	arg1	carcinoma					341:349	hepatocellular carcinoma	326:349	hepatocellular carcinoma (HCC) tumorigenesis	326:369	The roles of SLC35B4 in hepatocellular carcinoma (HCC) tumorigenesis remain unknown.
35308201	3	1	theme	hepatocellular	326:339	arg1	HCC					352:354	HCC	352:354	HCC	352:354	The roles of SLC35B4 in hepatocellular carcinoma (HCC) tumorigenesis remain unknown.
35308201	4	2	theme	HCC	447:449	arg1	tissues					451:457	HCC tissues	447:457	HCC tissues	447:457	We find that the expression levels of SLC35B4 are higher in HCC tissues than adjacent non-tumor tissues.
35308201	4	3	theme	non-tumor	473:481	arg1	tissues					483:489	adjacent non-tumor tissues	464:489	adjacent non-tumor tissues	464:489	We find that the expression levels of SLC35B4 are higher in HCC tissues than adjacent non-tumor tissues.
35308201	4	4	theme	adjacent	464:471	arg1	tissues					483:489	adjacent non-tumor tissues	464:489	adjacent non-tumor tissues	464:489	We find that the expression levels of SLC35B4 are higher in HCC tissues than adjacent non-tumor tissues.
35308201	4	5	theme	expression	404:413	arg1	higher					437:442	higher	437:442	higher	437:442	We find that the expression levels of SLC35B4 are higher in HCC tissues than adjacent non-tumor tissues.
35308201	4	5	theme	expression	404:413	arg1	levels					415:420	the expression levels	400:420	the expression levels of SLC35B4	400:431	We find that the expression levels of SLC35B4 are higher in HCC tissues than adjacent non-tumor tissues.
35308201	6	6	theme	HCC	703:705	arg1	tumorigenesis					707:719	HCC tumorigenesis	703:719	HCC tumorigenesis	703:719	Mechanistically, SLC35B4 is important for the O-GlcNAc modification of c-Myc and thus the stabilization of c-Myc, which is required for HCC tumorigenesis.
35308201	0	7	from	O-GlcNAcylation	36:50	arg1	HCC					55:57	HCC	55:57	HCC	55:57	SLC35B4 Stabilizes c-MYC Protein by O-GlcNAcylation in HCC.
35308201	7	8	theme	therapeutic	756:766	arg1	target					768:773	a promising therapeutic target	744:773	a promising therapeutic target for treating HCC	744:790	Therefore, SLC35B4 is a promising therapeutic target for treating HCC.
35308201	7	8	theme	therapeutic	756:766	arg1	SLC35B4					733:739	SLC35B4	733:739	SLC35B4	733:739	Therefore, SLC35B4 is a promising therapeutic target for treating HCC.
35308201	6	9	theme	O-GlcNAc	613:620	arg1	modification					622:633	the O-GlcNAc modification	609:633	the O-GlcNAc modification of c-Myc and thus the stabilization of c-Myc, which is required for HCC tumorigenesis	609:719	Mechanistically, SLC35B4 is important for the O-GlcNAc modification of c-Myc and thus the stabilization of c-Myc, which is required for HCC tumorigenesis.
35308201	1	10	theme	sugar	76:80	arg1	substrate					82:90	a sugar substrate	74:90	a sugar substrate necessary for the O-GlcNAcylation of proteins	74:136	UDP-GlcNAc is a sugar substrate necessary for the O-GlcNAcylation of proteins.
35308201	1	10	theme	sugar	76:80	arg1	UDP-GlcNAc					60:69	UDP-GlcNAc	60:69	UDP-GlcNAc	60:69	UDP-GlcNAc is a sugar substrate necessary for the O-GlcNAcylation of proteins.
35308201	1	11	theme	necessary	92:100	arg1	substrate					82:90	a sugar substrate	74:90	a sugar substrate necessary for the O-GlcNAcylation of proteins	74:136	UDP-GlcNAc is a sugar substrate necessary for the O-GlcNAcylation of proteins.
35308201	1	11	theme	necessary	92:100	arg1	UDP-GlcNAc					60:69	UDP-GlcNAc	60:69	UDP-GlcNAc	60:69	UDP-GlcNAc is a sugar substrate necessary for the O-GlcNAcylation of proteins.
35308201	0	12	theme	c-MYC	19:23	arg1	Protein					25:31	c-MYC Protein	19:31	c-MYC Protein	19:31	SLC35B4 Stabilizes c-MYC Protein by O-GlcNAcylation in HCC.
35308201	2	13	theme	sugar	172:176	arg1	transporters					178:189	the nucleotide sugar transporters	157:189	the nucleotide sugar transporters that transport UDP-GlcNAc and UDP-xylose into the endoplasmic reticulum and Golgi apparatus for glycosylation	157:299	SLC35B4 is one of the nucleotide sugar transporters that transport UDP-GlcNAc and UDP-xylose into the endoplasmic reticulum and Golgi apparatus for glycosylation.
35308201	6	14	theme	c-Myc	674:678	arg1	c-Myc					638:642	c-Myc	638:642	c-Myc	638:642	Mechanistically, SLC35B4 is important for the O-GlcNAc modification of c-Myc and thus the stabilization of c-Myc, which is required for HCC tumorigenesis.
35308201	6	14	theme	c-Myc	674:678	arg1	stabilization					657:669	thus the stabilization	648:669	thus the stabilization of c-Myc, which is required for HCC tumorigenesis	648:719	Mechanistically, SLC35B4 is important for the O-GlcNAc modification of c-Myc and thus the stabilization of c-Myc, which is required for HCC tumorigenesis.
35308201	2	15	theme	nucleotide	161:170	arg1	transporters					178:189	the nucleotide sugar transporters	157:189	the nucleotide sugar transporters that transport UDP-GlcNAc and UDP-xylose into the endoplasmic reticulum and Golgi apparatus for glycosylation	157:299	SLC35B4 is one of the nucleotide sugar transporters that transport UDP-GlcNAc and UDP-xylose into the endoplasmic reticulum and Golgi apparatus for glycosylation.
35308201	5	16	dep	proliferation	521:533	arg1	the					517:519	the	517:519	the	517:519	SLC35B4 is important for the proliferation and tumorigenesis of HCC cells.
35308201	5	17	theme	HCC	556:558	arg1	cells					560:564	HCC cells	556:564	HCC cells	556:564	SLC35B4 is important for the proliferation and tumorigenesis of HCC cells.
35308201	3	18	theme	SLC35B4	315:321	arg1	roles					306:310	The roles	302:310	The roles of SLC35B4 in hepatocellular carcinoma (HCC) tumorigenesis	302:369	The roles of SLC35B4 in hepatocellular carcinoma (HCC) tumorigenesis remain unknown.
35308201	4	19	theme	SLC35B4	425:431	arg1	higher					437:442	higher	437:442	higher	437:442	We find that the expression levels of SLC35B4 are higher in HCC tissues than adjacent non-tumor tissues.
35308201	4	19	theme	SLC35B4	425:431	arg1	levels					415:420	the expression levels	400:420	the expression levels of SLC35B4	400:431	We find that the expression levels of SLC35B4 are higher in HCC tissues than adjacent non-tumor tissues.
35308201	5	20	theme	cells	560:564	arg1	tumorigenesis					539:551	tumorigenesis	539:551	tumorigenesis	539:551	SLC35B4 is important for the proliferation and tumorigenesis of HCC cells.
35308201	5	20	theme	cells	560:564	arg1	proliferation					521:533	proliferation	521:533	proliferation	521:533	SLC35B4 is important for the proliferation and tumorigenesis of HCC cells.
35308201	2	21	theme	Golgi	267:271	arg1	apparatus					273:281	Golgi apparatus	267:281	Golgi apparatus	267:281	SLC35B4 is one of the nucleotide sugar transporters that transport UDP-GlcNAc and UDP-xylose into the endoplasmic reticulum and Golgi apparatus for glycosylation.
35308201	6	22	theme	stabilization	657:669	arg1	modification					622:633	the O-GlcNAc modification	609:633	the O-GlcNAc modification of c-Myc and thus the stabilization of c-Myc, which is required for HCC tumorigenesis	609:719	Mechanistically, SLC35B4 is important for the O-GlcNAc modification of c-Myc and thus the stabilization of c-Myc, which is required for HCC tumorigenesis.
35308201	7	23	theme	promising	746:754	arg1	target					768:773	a promising therapeutic target	744:773	a promising therapeutic target for treating HCC	744:790	Therefore, SLC35B4 is a promising therapeutic target for treating HCC.
35308201	7	23	theme	promising	746:754	arg1	SLC35B4					733:739	SLC35B4	733:739	SLC35B4	733:739	Therefore, SLC35B4 is a promising therapeutic target for treating HCC.
35308201	1	24	theme	proteins	129:136	arg1	O-GlcNAcylation					110:124	the O-GlcNAcylation	106:124	the O-GlcNAcylation of proteins	106:136	UDP-GlcNAc is a sugar substrate necessary for the O-GlcNAcylation of proteins.
35308201	3	25	from	roles	306:310	arg1	tumorigenesis					357:369	hepatocellular carcinoma (HCC) tumorigenesis	326:369	hepatocellular carcinoma (HCC) tumorigenesis	326:369	The roles of SLC35B4 in hepatocellular carcinoma (HCC) tumorigenesis remain unknown.
35308201	3	26	theme	carcinoma	341:349	arg1	tumorigenesis					357:369	hepatocellular carcinoma (HCC) tumorigenesis	326:369	hepatocellular carcinoma (HCC) tumorigenesis	326:369	The roles of SLC35B4 in hepatocellular carcinoma (HCC) tumorigenesis remain unknown.
35308201	2	27	theme	transporters	178:189	arg1	transporters					178:189	the nucleotide sugar transporters	157:189	the nucleotide sugar transporters that transport UDP-GlcNAc and UDP-xylose into the endoplasmic reticulum and Golgi apparatus for glycosylation	157:299	SLC35B4 is one of the nucleotide sugar transporters that transport UDP-GlcNAc and UDP-xylose into the endoplasmic reticulum and Golgi apparatus for glycosylation.
35308201	2	27	theme	transporters	178:189	arg1	one					150:152	one	150:152	one	150:152	SLC35B4 is one of the nucleotide sugar transporters that transport UDP-GlcNAc and UDP-xylose into the endoplasmic reticulum and Golgi apparatus for glycosylation.
35308201	2	28	theme	endoplasmic	241:251	arg1	reticulum					253:261	the endoplasmic reticulum	237:261	the endoplasmic reticulum	237:261	SLC35B4 is one of the nucleotide sugar transporters that transport UDP-GlcNAc and UDP-xylose into the endoplasmic reticulum and Golgi apparatus for glycosylation.
33544938	0	0	theme	integrin	111:118	arg1	perturbation					120:131	integrin perturbation	111:131	integrin perturbation	111:131	Metabolic sensor O-GlcNAcylation regulates megakaryopoiesis and thrombopoiesis through c-Myc stabilization and integrin perturbation.
33544938	8	1	theme	novel	1636:1640	arg1	knowledge					1648:1656	a novel basic knowledge	1634:1656	a novel basic knowledge on the regulatory role of O-GlcNAcylation in megakaryopoiesis and thrombopoiesis that could be important in understanding hematologic disorders whose etiology are related to impaired platelet production and may have clinical applications toward an ex vivo platelet production for transfusion	1634:1948	Together, our findings provide a novel basic knowledge on the regulatory role of O-GlcNAcylation in megakaryopoiesis and thrombopoiesis that could be important in understanding hematologic disorders whose etiology are related to impaired platelet production and may have clinical applications toward an ex vivo platelet production for transfusion.
33544938	8	1	theme	novel	1636:1640	arg1	important					1753:1761	important	1753:1761	important	1753:1761	Together, our findings provide a novel basic knowledge on the regulatory role of O-GlcNAcylation in megakaryopoiesis and thrombopoiesis that could be important in understanding hematologic disorders whose etiology are related to impaired platelet production and may have clinical applications toward an ex vivo platelet production for transfusion.
33544938	4	2	theme	CD34+	781:785	arg1	progenitors					802:812	CD34+ CD41a+ MK-like progenitors	781:812	CD34+ CD41a+ MK-like progenitors	781:812	Inhibition of O-GlcNAc transferase (OGT) that catalyzes O-GlcNAcylation prolongedly decreases O-GlcNAcylation and induces the acquisition of CD34+ CD41a+ MK-like progenitors and its progeny CD34- CD41a+ /CD42b+ megakaryoblasts (MBs)/MKs from HSPCs, consequently resulting in increased CD41a+ and CD42b+ platelets.
33544938	8	3	theme	regulatory	1665:1674	arg1	role					1676:1679	the regulatory role	1661:1679	the regulatory role of O-GlcNAcylation in megakaryopoiesis and thrombopoiesis	1661:1737	Together, our findings provide a novel basic knowledge on the regulatory role of O-GlcNAcylation in megakaryopoiesis and thrombopoiesis that could be important in understanding hematologic disorders whose etiology are related to impaired platelet production and may have clinical applications toward an ex vivo platelet production for transfusion.
33544938	3	4	theme	differentiation	556:570	arg1	course					527:532	the course	523:532	the course of megakaryocyte (MK) differentiation	523:570	Here, we reveal for the first time that cellular O-GlcNAcylation levels decline along the course of megakaryocyte (MK) differentiation from human-derived hematopoietic stem and progenitor cells (HSPCs).
33544938	5	5	from	target	1058:1063	arg1	MBs/MKs					1087:1093	MBs/MKs	1087:1093	MBs/MKs	1087:1093	Using correlation and co-immunoprecipitation analyses, we further identify c-Myc as a direct downstream target of O-GlcNAcylation in MBs/MKs and provide compelling evidence on the regulation of platelets by novel O-GlcNAc/c-Myc axis.
33544938	7	6	theme	c-Myc	1354:1358	arg1	Depletion					1341:1349	Depletion	1341:1349	Depletion of c-Myc upon inhibition of OGT	1341:1381	Depletion of c-Myc upon inhibition of OGT promotes platelet formation in part through the perturbation of cell adhesion molecules, that is, integrin-α4 and integrin-β7, as advised by gene ontology and enrichment analysis for RNA sequencing and validated herein.
33544938	8	7	theme	impaired	1832:1839	arg1	production					1850:1859	impaired platelet production	1832:1859	impaired platelet production	1832:1859	Together, our findings provide a novel basic knowledge on the regulatory role of O-GlcNAcylation in megakaryopoiesis and thrombopoiesis that could be important in understanding hematologic disorders whose etiology are related to impaired platelet production and may have clinical applications toward an ex vivo platelet production for transfusion.
33544938	5	8	theme	co-immunoprecipitation	976:997	arg1	analyses					999:1006	correlation and co-immunoprecipitation analyses	960:1006	analyses	999:1006	Using correlation and co-immunoprecipitation analyses, we further identify c-Myc as a direct downstream target of O-GlcNAcylation in MBs/MKs and provide compelling evidence on the regulation of platelets by novel O-GlcNAc/c-Myc axis.
33544938	5	9	theme	downstream	1047:1056	arg1	target					1058:1063	a direct downstream target	1038:1063	a direct downstream target of O-GlcNAcylation in MBs/MKs	1038:1093	Using correlation and co-immunoprecipitation analyses, we further identify c-Myc as a direct downstream target of O-GlcNAcylation in MBs/MKs and provide compelling evidence on the regulation of platelets by novel O-GlcNAc/c-Myc axis.
33544938	5	9	theme	downstream	1047:1056	arg1	c-Myc					1029:1033	c-Myc	1029:1033	c-Myc	1029:1033	Using correlation and co-immunoprecipitation analyses, we further identify c-Myc as a direct downstream target of O-GlcNAcylation in MBs/MKs and provide compelling evidence on the regulation of platelets by novel O-GlcNAc/c-Myc axis.
33544938	4	10	theme	O-GlcNAc	654:661	arg1	OGT					676:678	OGT	676:678	OGT	676:678	Inhibition of O-GlcNAc transferase (OGT) that catalyzes O-GlcNAcylation prolongedly decreases O-GlcNAcylation and induces the acquisition of CD34+ CD41a+ MK-like progenitors and its progeny CD34- CD41a+ /CD42b+ megakaryoblasts (MBs)/MKs from HSPCs, consequently resulting in increased CD41a+ and CD42b+ platelets.
33544938	4	10	theme	O-GlcNAc	654:661	arg1	transferase					663:673	O-GlcNAc transferase	654:673	O-GlcNAc transferase (OGT) that catalyzes O-GlcNAcylation	654:710	Inhibition of O-GlcNAc transferase (OGT) that catalyzes O-GlcNAcylation prolongedly decreases O-GlcNAcylation and induces the acquisition of CD34+ CD41a+ MK-like progenitors and its progeny CD34- CD41a+ /CD42b+ megakaryoblasts (MBs)/MKs from HSPCs, consequently resulting in increased CD41a+ and CD42b+ platelets.
33544938	8	11	contain	have	1869:1872	arg1	etiology					1808:1815	etiology	1808:1815	etiology	1808:1815	Together, our findings provide a novel basic knowledge on the regulatory role of O-GlcNAcylation in megakaryopoiesis and thrombopoiesis that could be important in understanding hematologic disorders whose etiology are related to impaired platelet production and may have clinical applications toward an ex vivo platelet production for transfusion.
33544938	8	11	contain	have	1869:1872	arg2	applications					1883:1894	clinical applications	1874:1894	clinical applications	1874:1894	Together, our findings provide a novel basic knowledge on the regulatory role of O-GlcNAcylation in megakaryopoiesis and thrombopoiesis that could be important in understanding hematologic disorders whose etiology are related to impaired platelet production and may have clinical applications toward an ex vivo platelet production for transfusion.
33544938	2	12	theme	metabolic	340:348	arg1	modification					283:294	Posttranslational modification	265:294	Posttranslational modification of proteins via O-GlcNAcylation	265:326	Posttranslational modification of proteins via O-GlcNAcylation is an ideal metabolic sensor, but how it contributes to megakaryopoiesis and thrombopoiesis remains unknown.
33544938	2	12	theme	metabolic	340:348	arg1	sensor					350:355	an ideal metabolic sensor	331:355	an ideal metabolic sensor	331:355	Posttranslational modification of proteins via O-GlcNAcylation is an ideal metabolic sensor, but how it contributes to megakaryopoiesis and thrombopoiesis remains unknown.
33544938	3	13	theme	progenitor	614:623	arg1	cells					625:629	human-derived hematopoietic stem and progenitor cells	577:629	cells	625:629	Here, we reveal for the first time that cellular O-GlcNAcylation levels decline along the course of megakaryocyte (MK) differentiation from human-derived hematopoietic stem and progenitor cells (HSPCs).
33544938	1	14	theme	cells	172:176	arg1	regulator					201:209	an important regulator	188:209	an important regulator of self-renewal and lineage-specific differentiation	188:262	Metabolic state of hematopoietic stem cells (HSCs) is an important regulator of self-renewal and lineage-specific differentiation.
33544938	1	14	theme	cells	172:176	arg1	state					144:148	Metabolic state	134:148	Metabolic state of hematopoietic stem cells (HSCs)	134:183	Metabolic state of hematopoietic stem cells (HSCs) is an important regulator of self-renewal and lineage-specific differentiation.
33544938	4	15	theme	CD41a+	925:930	arg1	platelets					943:951	increased CD41a+ and CD42b+ platelets	915:951	increased CD41a+ and CD42b+ platelets	915:951	Inhibition of O-GlcNAc transferase (OGT) that catalyzes O-GlcNAcylation prolongedly decreases O-GlcNAcylation and induces the acquisition of CD34+ CD41a+ MK-like progenitors and its progeny CD34- CD41a+ /CD42b+ megakaryoblasts (MBs)/MKs from HSPCs, consequently resulting in increased CD41a+ and CD42b+ platelets.
33544938	8	16	dep	ex	1906:1907	arg1	vivo					1909:1912	vivo	1909:1912	vivo	1909:1912	Together, our findings provide a novel basic knowledge on the regulatory role of O-GlcNAcylation in megakaryopoiesis and thrombopoiesis that could be important in understanding hematologic disorders whose etiology are related to impaired platelet production and may have clinical applications toward an ex vivo platelet production for transfusion.
33544938	2	17	theme	ideal	334:338	arg1	modification					283:294	Posttranslational modification	265:294	Posttranslational modification of proteins via O-GlcNAcylation	265:326	Posttranslational modification of proteins via O-GlcNAcylation is an ideal metabolic sensor, but how it contributes to megakaryopoiesis and thrombopoiesis remains unknown.
33544938	2	17	theme	ideal	334:338	arg1	sensor					350:355	an ideal metabolic sensor	331:355	an ideal metabolic sensor	331:355	Posttranslational modification of proteins via O-GlcNAcylation is an ideal metabolic sensor, but how it contributes to megakaryopoiesis and thrombopoiesis remains unknown.
33544938	8	18	theme	clinical	1874:1881	arg1	applications					1883:1894	clinical applications	1874:1894	clinical applications	1874:1894	Together, our findings provide a novel basic knowledge on the regulatory role of O-GlcNAcylation in megakaryopoiesis and thrombopoiesis that could be important in understanding hematologic disorders whose etiology are related to impaired platelet production and may have clinical applications toward an ex vivo platelet production for transfusion.
33544938	3	19	theme	O-GlcNAcylation	486:500	arg1	levels					502:507	cellular O-GlcNAcylation levels	477:507	cellular O-GlcNAcylation levels	477:507	Here, we reveal for the first time that cellular O-GlcNAcylation levels decline along the course of megakaryocyte (MK) differentiation from human-derived hematopoietic stem and progenitor cells (HSPCs).
33544938	4	20	theme	increased	915:923	arg1	platelets					943:951	increased CD41a+ and CD42b+ platelets	915:951	increased CD41a+ and CD42b+ platelets	915:951	Inhibition of O-GlcNAc transferase (OGT) that catalyzes O-GlcNAcylation prolongedly decreases O-GlcNAcylation and induces the acquisition of CD34+ CD41a+ MK-like progenitors and its progeny CD34- CD41a+ /CD42b+ megakaryoblasts (MBs)/MKs from HSPCs, consequently resulting in increased CD41a+ and CD42b+ platelets.
33544938	6	21	theme	ubiquitin-mediated	1297:1314	arg1	degradation					1328:1338	its ubiquitin-mediated proteasomal degradation	1293:1338	its ubiquitin-mediated proteasomal degradation	1293:1338	Our data indicate that O-GlcNAcylation posttranslationally regulates c-Myc stability by interfering with its ubiquitin-mediated proteasomal degradation.
33544938	1	22	theme	important	191:199	arg1	regulator					201:209	an important regulator	188:209	an important regulator of self-renewal and lineage-specific differentiation	188:262	Metabolic state of hematopoietic stem cells (HSCs) is an important regulator of self-renewal and lineage-specific differentiation.
33544938	1	22	theme	important	191:199	arg1	state					144:148	Metabolic state	134:148	Metabolic state of hematopoietic stem cells (HSCs)	134:183	Metabolic state of hematopoietic stem cells (HSCs) is an important regulator of self-renewal and lineage-specific differentiation.
33544938	0	23	theme	sensor	10:15	arg1	O-GlcNAcylation					17:31	Metabolic sensor O-GlcNAcylation	0:31	Metabolic sensor O-GlcNAcylation	0:31	Metabolic sensor O-GlcNAcylation regulates megakaryopoiesis and thrombopoiesis through c-Myc stabilization and integrin perturbation.
33544938	4	24	theme	CD42b+	936:941	arg1	platelets					943:951	increased CD41a+ and CD42b+ platelets	915:951	increased CD41a+ and CD42b+ platelets	915:951	Inhibition of O-GlcNAc transferase (OGT) that catalyzes O-GlcNAcylation prolongedly decreases O-GlcNAcylation and induces the acquisition of CD34+ CD41a+ MK-like progenitors and its progeny CD34- CD41a+ /CD42b+ megakaryoblasts (MBs)/MKs from HSPCs, consequently resulting in increased CD41a+ and CD42b+ platelets.
33544938	7	25	theme	OGT	1379:1381	arg1	inhibition					1365:1374	inhibition	1365:1374	inhibition of OGT	1365:1381	Depletion of c-Myc upon inhibition of OGT promotes platelet formation in part through the perturbation of cell adhesion molecules, that is, integrin-α4 and integrin-β7, as advised by gene ontology and enrichment analysis for RNA sequencing and validated herein.
33544938	4	26	theme	progeny	822:828	arg1	acquisition					766:776	the acquisition	762:776	the acquisition of CD34+ CD41a+ MK-like progenitors and its progeny CD34- CD41a+ /CD42b+ megakaryoblasts (MBs)/MKs from HSPCs, consequently resulting in increased CD41a+ and CD42b+ platelets	762:951	Inhibition of O-GlcNAc transferase (OGT) that catalyzes O-GlcNAcylation prolongedly decreases O-GlcNAcylation and induces the acquisition of CD34+ CD41a+ MK-like progenitors and its progeny CD34- CD41a+ /CD42b+ megakaryoblasts (MBs)/MKs from HSPCs, consequently resulting in increased CD41a+ and CD42b+ platelets.
33544938	0	27	theme	Metabolic	0:8	arg1	O-GlcNAcylation					17:31	Metabolic sensor O-GlcNAcylation	0:31	Metabolic sensor O-GlcNAcylation	0:31	Metabolic sensor O-GlcNAcylation regulates megakaryopoiesis and thrombopoiesis through c-Myc stabilization and integrin perturbation.
33544938	4	28	theme	progenitors	802:812	arg1	acquisition					766:776	the acquisition	762:776	the acquisition of CD34+ CD41a+ MK-like progenitors and its progeny CD34- CD41a+ /CD42b+ megakaryoblasts (MBs)/MKs from HSPCs, consequently resulting in increased CD41a+ and CD42b+ platelets	762:951	Inhibition of O-GlcNAc transferase (OGT) that catalyzes O-GlcNAcylation prolongedly decreases O-GlcNAcylation and induces the acquisition of CD34+ CD41a+ MK-like progenitors and its progeny CD34- CD41a+ /CD42b+ megakaryoblasts (MBs)/MKs from HSPCs, consequently resulting in increased CD41a+ and CD42b+ platelets.
33544938	7	29	theme	cell	1447:1450	arg1	molecules					1461:1469	cell adhesion molecules	1447:1469	cell adhesion molecules	1447:1469	Depletion of c-Myc upon inhibition of OGT promotes platelet formation in part through the perturbation of cell adhesion molecules, that is, integrin-α4 and integrin-β7, as advised by gene ontology and enrichment analysis for RNA sequencing and validated herein.
33544938	3	30	theme	cellular	477:484	arg1	levels					502:507	cellular O-GlcNAcylation levels	477:507	cellular O-GlcNAcylation levels	477:507	Here, we reveal for the first time that cellular O-GlcNAcylation levels decline along the course of megakaryocyte (MK) differentiation from human-derived hematopoietic stem and progenitor cells (HSPCs).
33544938	8	31	theme	O-GlcNAcylation	1684:1698	arg1	role					1676:1679	the regulatory role	1661:1679	the regulatory role of O-GlcNAcylation in megakaryopoiesis and thrombopoiesis	1661:1737	Together, our findings provide a novel basic knowledge on the regulatory role of O-GlcNAcylation in megakaryopoiesis and thrombopoiesis that could be important in understanding hematologic disorders whose etiology are related to impaired platelet production and may have clinical applications toward an ex vivo platelet production for transfusion.
33544938	1	32	theme	Metabolic	134:142	arg1	regulator					201:209	an important regulator	188:209	an important regulator of self-renewal and lineage-specific differentiation	188:262	Metabolic state of hematopoietic stem cells (HSCs) is an important regulator of self-renewal and lineage-specific differentiation.
33544938	1	32	theme	Metabolic	134:142	arg1	state					144:148	Metabolic state	134:148	Metabolic state of hematopoietic stem cells (HSCs)	134:183	Metabolic state of hematopoietic stem cells (HSCs) is an important regulator of self-renewal and lineage-specific differentiation.
33544938	8	33	theme	ex	1906:1907	arg1	production					1923:1932	an ex vivo platelet production	1903:1932	an ex vivo platelet production for transfusion	1903:1948	Together, our findings provide a novel basic knowledge on the regulatory role of O-GlcNAcylation in megakaryopoiesis and thrombopoiesis that could be important in understanding hematologic disorders whose etiology are related to impaired platelet production and may have clinical applications toward an ex vivo platelet production for transfusion.
33544938	1	34	theme	self-renewal	214:225	arg1	differentiation					248:262	self-renewal and lineage-specific differentiation	214:262	self-renewal and lineage-specific differentiation	214:262	Metabolic state of hematopoietic stem cells (HSCs) is an important regulator of self-renewal and lineage-specific differentiation.
33544938	5	35	theme	novel	1161:1165	arg1	axis					1182:1185	novel O-GlcNAc/c-Myc axis	1161:1185	novel O-GlcNAc/c-Myc axis	1161:1185	Using correlation and co-immunoprecipitation analyses, we further identify c-Myc as a direct downstream target of O-GlcNAcylation in MBs/MKs and provide compelling evidence on the regulation of platelets by novel O-GlcNAc/c-Myc axis.
33544938	3	36	theme	hematopoietic	591:603	arg1	HSPCs					632:636	HSPCs	632:636	HSPCs	632:636	Here, we reveal for the first time that cellular O-GlcNAcylation levels decline along the course of megakaryocyte (MK) differentiation from human-derived hematopoietic stem and progenitor cells (HSPCs).
33544938	3	36	theme	hematopoietic	591:603	arg1	stem					605:608	human-derived hematopoietic stem and progenitor cells	577:629	stem	605:608	Here, we reveal for the first time that cellular O-GlcNAcylation levels decline along the course of megakaryocyte (MK) differentiation from human-derived hematopoietic stem and progenitor cells (HSPCs).
33544938	5	37	theme	O-GlcNAc/c-Myc	1167:1180	arg1	axis					1182:1185	novel O-GlcNAc/c-Myc axis	1161:1185	novel O-GlcNAc/c-Myc axis	1161:1185	Using correlation and co-immunoprecipitation analyses, we further identify c-Myc as a direct downstream target of O-GlcNAcylation in MBs/MKs and provide compelling evidence on the regulation of platelets by novel O-GlcNAc/c-Myc axis.
33544938	4	38	theme	CD34-	830:834	arg1	megakaryoblasts					851:865	CD34- CD41a+ /CD42b+ megakaryoblasts	830:865	CD34- CD41a+ /CD42b+ megakaryoblasts (MBs)	830:871	Inhibition of O-GlcNAc transferase (OGT) that catalyzes O-GlcNAcylation prolongedly decreases O-GlcNAcylation and induces the acquisition of CD34+ CD41a+ MK-like progenitors and its progeny CD34- CD41a+ /CD42b+ megakaryoblasts (MBs)/MKs from HSPCs, consequently resulting in increased CD41a+ and CD42b+ platelets.
33544938	4	38	theme	CD34-	830:834	arg1	MBs					868:870	MBs	868:870	MBs	868:870	Inhibition of O-GlcNAc transferase (OGT) that catalyzes O-GlcNAcylation prolongedly decreases O-GlcNAcylation and induces the acquisition of CD34+ CD41a+ MK-like progenitors and its progeny CD34- CD41a+ /CD42b+ megakaryoblasts (MBs)/MKs from HSPCs, consequently resulting in increased CD41a+ and CD42b+ platelets.
33544938	5	39	from	evidence	1118:1125	arg1	regulation					1134:1143	the regulation	1130:1143	the regulation of platelets by novel O-GlcNAc/c-Myc axis	1130:1185	Using correlation and co-immunoprecipitation analyses, we further identify c-Myc as a direct downstream target of O-GlcNAcylation in MBs/MKs and provide compelling evidence on the regulation of platelets by novel O-GlcNAc/c-Myc axis.
33544938	3	40	theme	first	461:465	arg1	time					467:470	the first time	457:470	the first time	457:470	Here, we reveal for the first time that cellular O-GlcNAcylation levels decline along the course of megakaryocyte (MK) differentiation from human-derived hematopoietic stem and progenitor cells (HSPCs).
33544938	4	41	theme	CD41a+	787:792	arg1	progenitors					802:812	CD34+ CD41a+ MK-like progenitors	781:812	CD34+ CD41a+ MK-like progenitors	781:812	Inhibition of O-GlcNAc transferase (OGT) that catalyzes O-GlcNAcylation prolongedly decreases O-GlcNAcylation and induces the acquisition of CD34+ CD41a+ MK-like progenitors and its progeny CD34- CD41a+ /CD42b+ megakaryoblasts (MBs)/MKs from HSPCs, consequently resulting in increased CD41a+ and CD42b+ platelets.
33544938	7	42	theme	adhesion	1452:1459	arg1	molecules					1461:1469	cell adhesion molecules	1447:1469	cell adhesion molecules	1447:1469	Depletion of c-Myc upon inhibition of OGT promotes platelet formation in part through the perturbation of cell adhesion molecules, that is, integrin-α4 and integrin-β7, as advised by gene ontology and enrichment analysis for RNA sequencing and validated herein.
33544938	6	43	theme	c-Myc	1257:1261	arg1	stability					1263:1271	c-Myc stability	1257:1271	c-Myc stability	1257:1271	Our data indicate that O-GlcNAcylation posttranslationally regulates c-Myc stability by interfering with its ubiquitin-mediated proteasomal degradation.
33544938	7	44	theme	gene	1524:1527	arg1	ontology					1529:1536	gene ontology	1524:1536	gene ontology	1524:1536	Depletion of c-Myc upon inhibition of OGT promotes platelet formation in part through the perturbation of cell adhesion molecules, that is, integrin-α4 and integrin-β7, as advised by gene ontology and enrichment analysis for RNA sequencing and validated herein.
33544938	5	45	theme	correlation	960:970	arg1	analyses					999:1006	correlation and co-immunoprecipitation analyses	960:1006	analyses	999:1006	Using correlation and co-immunoprecipitation analyses, we further identify c-Myc as a direct downstream target of O-GlcNAcylation in MBs/MKs and provide compelling evidence on the regulation of platelets by novel O-GlcNAc/c-Myc axis.
33544938	1	46	theme	lineage-specific	231:246	arg1	differentiation					248:262	self-renewal and lineage-specific differentiation	214:262	self-renewal and lineage-specific differentiation	214:262	Metabolic state of hematopoietic stem cells (HSCs) is an important regulator of self-renewal and lineage-specific differentiation.
33544938	8	47	from	role	1676:1679	arg1	megakaryopoiesis					1703:1718	megakaryopoiesis	1703:1718	megakaryopoiesis	1703:1718	Together, our findings provide a novel basic knowledge on the regulatory role of O-GlcNAcylation in megakaryopoiesis and thrombopoiesis that could be important in understanding hematologic disorders whose etiology are related to impaired platelet production and may have clinical applications toward an ex vivo platelet production for transfusion.
33544938	8	47	from	role	1676:1679	arg1	thrombopoiesis					1724:1737	thrombopoiesis	1724:1737	thrombopoiesis	1724:1737	Together, our findings provide a novel basic knowledge on the regulatory role of O-GlcNAcylation in megakaryopoiesis and thrombopoiesis that could be important in understanding hematologic disorders whose etiology are related to impaired platelet production and may have clinical applications toward an ex vivo platelet production for transfusion.
33544938	3	48	link	human-derived	577:589	arg1	HSPCs					632:636	HSPCs	632:636	HSPCs	632:636	Here, we reveal for the first time that cellular O-GlcNAcylation levels decline along the course of megakaryocyte (MK) differentiation from human-derived hematopoietic stem and progenitor cells (HSPCs).
33544938	3	48	link	human-derived	577:589	arg1	stem					605:608	human-derived hematopoietic stem and progenitor cells	577:629	stem	605:608	Here, we reveal for the first time that cellular O-GlcNAcylation levels decline along the course of megakaryocyte (MK) differentiation from human-derived hematopoietic stem and progenitor cells (HSPCs).
33544938	4	49	theme	/CD42b+	843:849	arg1	megakaryoblasts					851:865	CD34- CD41a+ /CD42b+ megakaryoblasts	830:865	CD34- CD41a+ /CD42b+ megakaryoblasts (MBs)	830:871	Inhibition of O-GlcNAc transferase (OGT) that catalyzes O-GlcNAcylation prolongedly decreases O-GlcNAcylation and induces the acquisition of CD34+ CD41a+ MK-like progenitors and its progeny CD34- CD41a+ /CD42b+ megakaryoblasts (MBs)/MKs from HSPCs, consequently resulting in increased CD41a+ and CD42b+ platelets.
33544938	4	49	theme	/CD42b+	843:849	arg1	MBs					868:870	MBs	868:870	MBs	868:870	Inhibition of O-GlcNAc transferase (OGT) that catalyzes O-GlcNAcylation prolongedly decreases O-GlcNAcylation and induces the acquisition of CD34+ CD41a+ MK-like progenitors and its progeny CD34- CD41a+ /CD42b+ megakaryoblasts (MBs)/MKs from HSPCs, consequently resulting in increased CD41a+ and CD42b+ platelets.
33544938	7	50	theme	ontology	1529:1536	arg1	analysis					1553:1560	gene ontology and enrichment analysis	1524:1560	gene ontology and enrichment analysis	1524:1560	Depletion of c-Myc upon inhibition of OGT promotes platelet formation in part through the perturbation of cell adhesion molecules, that is, integrin-α4 and integrin-β7, as advised by gene ontology and enrichment analysis for RNA sequencing and validated herein.
33544938	1	51	theme	differentiation	248:262	arg1	regulator					201:209	an important regulator	188:209	an important regulator of self-renewal and lineage-specific differentiation	188:262	Metabolic state of hematopoietic stem cells (HSCs) is an important regulator of self-renewal and lineage-specific differentiation.
33544938	1	51	theme	differentiation	248:262	arg1	state					144:148	Metabolic state	134:148	Metabolic state of hematopoietic stem cells (HSCs)	134:183	Metabolic state of hematopoietic stem cells (HSCs) is an important regulator of self-renewal and lineage-specific differentiation.
33544938	8	52	theme	platelet	1914:1921	arg1	production					1923:1932	an ex vivo platelet production	1903:1932	an ex vivo platelet production for transfusion	1903:1948	Together, our findings provide a novel basic knowledge on the regulatory role of O-GlcNAcylation in megakaryopoiesis and thrombopoiesis that could be important in understanding hematologic disorders whose etiology are related to impaired platelet production and may have clinical applications toward an ex vivo platelet production for transfusion.
33544938	2	53	theme	Posttranslational	265:281	arg1	modification					283:294	Posttranslational modification	265:294	Posttranslational modification of proteins via O-GlcNAcylation	265:326	Posttranslational modification of proteins via O-GlcNAcylation is an ideal metabolic sensor, but how it contributes to megakaryopoiesis and thrombopoiesis remains unknown.
33544938	2	53	theme	Posttranslational	265:281	arg1	sensor					350:355	an ideal metabolic sensor	331:355	an ideal metabolic sensor	331:355	Posttranslational modification of proteins via O-GlcNAcylation is an ideal metabolic sensor, but how it contributes to megakaryopoiesis and thrombopoiesis remains unknown.
33544938	8	54	from	knowledge	1648:1656	arg1	role					1676:1679	the regulatory role	1661:1679	the regulatory role of O-GlcNAcylation in megakaryopoiesis and thrombopoiesis	1661:1737	Together, our findings provide a novel basic knowledge on the regulatory role of O-GlcNAcylation in megakaryopoiesis and thrombopoiesis that could be important in understanding hematologic disorders whose etiology are related to impaired platelet production and may have clinical applications toward an ex vivo platelet production for transfusion.
33544938	4	55	theme	MK-like	794:800	arg1	progenitors					802:812	CD34+ CD41a+ MK-like progenitors	781:812	CD34+ CD41a+ MK-like progenitors	781:812	Inhibition of O-GlcNAc transferase (OGT) that catalyzes O-GlcNAcylation prolongedly decreases O-GlcNAcylation and induces the acquisition of CD34+ CD41a+ MK-like progenitors and its progeny CD34- CD41a+ /CD42b+ megakaryoblasts (MBs)/MKs from HSPCs, consequently resulting in increased CD41a+ and CD42b+ platelets.
33544938	5	56	theme	direct	1040:1045	arg1	target					1058:1063	a direct downstream target	1038:1063	a direct downstream target of O-GlcNAcylation in MBs/MKs	1038:1093	Using correlation and co-immunoprecipitation analyses, we further identify c-Myc as a direct downstream target of O-GlcNAcylation in MBs/MKs and provide compelling evidence on the regulation of platelets by novel O-GlcNAc/c-Myc axis.
33544938	5	56	theme	direct	1040:1045	arg1	c-Myc					1029:1033	c-Myc	1029:1033	c-Myc	1029:1033	Using correlation and co-immunoprecipitation analyses, we further identify c-Myc as a direct downstream target of O-GlcNAcylation in MBs/MKs and provide compelling evidence on the regulation of platelets by novel O-GlcNAc/c-Myc axis.
33544938	1	57	theme	hematopoietic	153:165	arg1	HSCs					179:182	HSCs	179:182	HSCs	179:182	Metabolic state of hematopoietic stem cells (HSCs) is an important regulator of self-renewal and lineage-specific differentiation.
33544938	1	57	theme	hematopoietic	153:165	arg1	cells					172:176	hematopoietic stem cells	153:176	hematopoietic stem cells (HSCs)	153:183	Metabolic state of hematopoietic stem cells (HSCs) is an important regulator of self-renewal and lineage-specific differentiation.
33544938	5	58	theme	compelling	1107:1116	arg1	evidence					1118:1125	compelling evidence	1107:1125	compelling evidence on the regulation of platelets by novel O-GlcNAc/c-Myc axis	1107:1185	Using correlation and co-immunoprecipitation analyses, we further identify c-Myc as a direct downstream target of O-GlcNAcylation in MBs/MKs and provide compelling evidence on the regulation of platelets by novel O-GlcNAc/c-Myc axis.
33544938	5	59	theme	platelets	1148:1156	arg1	regulation					1134:1143	the regulation	1130:1143	the regulation of platelets by novel O-GlcNAc/c-Myc axis	1130:1185	Using correlation and co-immunoprecipitation analyses, we further identify c-Myc as a direct downstream target of O-GlcNAcylation in MBs/MKs and provide compelling evidence on the regulation of platelets by novel O-GlcNAc/c-Myc axis.
33544938	7	60	theme	RNA	1566:1568	arg1	sequencing					1570:1579	RNA sequencing	1566:1579	RNA sequencing	1566:1579	Depletion of c-Myc upon inhibition of OGT promotes platelet formation in part through the perturbation of cell adhesion molecules, that is, integrin-α4 and integrin-β7, as advised by gene ontology and enrichment analysis for RNA sequencing and validated herein.
33544938	1	61	theme	stem	167:170	arg1	HSCs					179:182	HSCs	179:182	HSCs	179:182	Metabolic state of hematopoietic stem cells (HSCs) is an important regulator of self-renewal and lineage-specific differentiation.
33544938	1	61	theme	stem	167:170	arg1	cells					172:176	hematopoietic stem cells	153:176	hematopoietic stem cells (HSCs)	153:183	Metabolic state of hematopoietic stem cells (HSCs) is an important regulator of self-renewal and lineage-specific differentiation.
33544938	4	62	theme	CD41a+	836:841	arg1	megakaryoblasts					851:865	CD34- CD41a+ /CD42b+ megakaryoblasts	830:865	CD34- CD41a+ /CD42b+ megakaryoblasts (MBs)	830:871	Inhibition of O-GlcNAc transferase (OGT) that catalyzes O-GlcNAcylation prolongedly decreases O-GlcNAcylation and induces the acquisition of CD34+ CD41a+ MK-like progenitors and its progeny CD34- CD41a+ /CD42b+ megakaryoblasts (MBs)/MKs from HSPCs, consequently resulting in increased CD41a+ and CD42b+ platelets.
33544938	4	62	theme	CD41a+	836:841	arg1	MBs					868:870	MBs	868:870	MBs	868:870	Inhibition of O-GlcNAc transferase (OGT) that catalyzes O-GlcNAcylation prolongedly decreases O-GlcNAcylation and induces the acquisition of CD34+ CD41a+ MK-like progenitors and its progeny CD34- CD41a+ /CD42b+ megakaryoblasts (MBs)/MKs from HSPCs, consequently resulting in increased CD41a+ and CD42b+ platelets.
33544938	7	63	theme	enrichment	1542:1551	arg1	analysis					1553:1560	gene ontology and enrichment analysis	1524:1560	gene ontology and enrichment analysis	1524:1560	Depletion of c-Myc upon inhibition of OGT promotes platelet formation in part through the perturbation of cell adhesion molecules, that is, integrin-α4 and integrin-β7, as advised by gene ontology and enrichment analysis for RNA sequencing and validated herein.
33544938	3	64	theme	megakaryocyte	537:549	arg1	differentiation					556:570	megakaryocyte (MK) differentiation	537:570	megakaryocyte (MK) differentiation	537:570	Here, we reveal for the first time that cellular O-GlcNAcylation levels decline along the course of megakaryocyte (MK) differentiation from human-derived hematopoietic stem and progenitor cells (HSPCs).
33544938	8	65	theme	platelet	1841:1848	arg1	production					1850:1859	impaired platelet production	1832:1859	impaired platelet production	1832:1859	Together, our findings provide a novel basic knowledge on the regulatory role of O-GlcNAcylation in megakaryopoiesis and thrombopoiesis that could be important in understanding hematologic disorders whose etiology are related to impaired platelet production and may have clinical applications toward an ex vivo platelet production for transfusion.
33544938	4	66	theme	transferase	663:673	arg1	Inhibition					640:649	Inhibition	640:649	Inhibition of O-GlcNAc transferase (OGT) that catalyzes O-GlcNAcylation	640:710	Inhibition of O-GlcNAc transferase (OGT) that catalyzes O-GlcNAcylation prolongedly decreases O-GlcNAcylation and induces the acquisition of CD34+ CD41a+ MK-like progenitors and its progeny CD34- CD41a+ /CD42b+ megakaryoblasts (MBs)/MKs from HSPCs, consequently resulting in increased CD41a+ and CD42b+ platelets.
33544938	4	67	dep	progeny	822:828	arg1	/MKs					872:875	/MKs	872:875	/MKs	872:875	Inhibition of O-GlcNAc transferase (OGT) that catalyzes O-GlcNAcylation prolongedly decreases O-GlcNAcylation and induces the acquisition of CD34+ CD41a+ MK-like progenitors and its progeny CD34- CD41a+ /CD42b+ megakaryoblasts (MBs)/MKs from HSPCs, consequently resulting in increased CD41a+ and CD42b+ platelets.
33544938	5	68	theme	O-GlcNAcylation	1068:1082	arg1	target					1058:1063	a direct downstream target	1038:1063	a direct downstream target of O-GlcNAcylation in MBs/MKs	1038:1093	Using correlation and co-immunoprecipitation analyses, we further identify c-Myc as a direct downstream target of O-GlcNAcylation in MBs/MKs and provide compelling evidence on the regulation of platelets by novel O-GlcNAc/c-Myc axis.
33544938	5	68	theme	O-GlcNAcylation	1068:1082	arg1	c-Myc					1029:1033	c-Myc	1029:1033	c-Myc	1029:1033	Using correlation and co-immunoprecipitation analyses, we further identify c-Myc as a direct downstream target of O-GlcNAcylation in MBs/MKs and provide compelling evidence on the regulation of platelets by novel O-GlcNAc/c-Myc axis.
33544938	7	69	theme	molecules	1461:1469	arg1	perturbation					1431:1442	the perturbation	1427:1442	the perturbation of cell adhesion molecules, that is, integrin-α4 and integrin-β7, as advised by gene ontology and enrichment analysis for RNA sequencing and validated herein	1427:1600	Depletion of c-Myc upon inhibition of OGT promotes platelet formation in part through the perturbation of cell adhesion molecules, that is, integrin-α4 and integrin-β7, as advised by gene ontology and enrichment analysis for RNA sequencing and validated herein.
33544938	6	70	theme	proteasomal	1316:1326	arg1	degradation					1328:1338	its ubiquitin-mediated proteasomal degradation	1293:1338	its ubiquitin-mediated proteasomal degradation	1293:1338	Our data indicate that O-GlcNAcylation posttranslationally regulates c-Myc stability by interfering with its ubiquitin-mediated proteasomal degradation.
33544938	8	71	theme	hematologic	1780:1790	arg1	disorders					1792:1800	hematologic disorders	1780:1800	hematologic disorders whose etiology are related to impaired platelet production and may have clinical applications toward an ex vivo platelet production for transfusion	1780:1948	Together, our findings provide a novel basic knowledge on the regulatory role of O-GlcNAcylation in megakaryopoiesis and thrombopoiesis that could be important in understanding hematologic disorders whose etiology are related to impaired platelet production and may have clinical applications toward an ex vivo platelet production for transfusion.
33544938	0	72	theme	c-Myc	87:91	arg1	stabilization					93:105	c-Myc stabilization	87:105	c-Myc stabilization	87:105	Metabolic sensor O-GlcNAcylation regulates megakaryopoiesis and thrombopoiesis through c-Myc stabilization and integrin perturbation.
33544938	8	73	theme	basic	1642:1646	arg1	knowledge					1648:1656	a novel basic knowledge	1634:1656	a novel basic knowledge on the regulatory role of O-GlcNAcylation in megakaryopoiesis and thrombopoiesis that could be important in understanding hematologic disorders whose etiology are related to impaired platelet production and may have clinical applications toward an ex vivo platelet production for transfusion	1634:1948	Together, our findings provide a novel basic knowledge on the regulatory role of O-GlcNAcylation in megakaryopoiesis and thrombopoiesis that could be important in understanding hematologic disorders whose etiology are related to impaired platelet production and may have clinical applications toward an ex vivo platelet production for transfusion.
33544938	8	73	theme	basic	1642:1646	arg1	important					1753:1761	important	1753:1761	important	1753:1761	Together, our findings provide a novel basic knowledge on the regulatory role of O-GlcNAcylation in megakaryopoiesis and thrombopoiesis that could be important in understanding hematologic disorders whose etiology are related to impaired platelet production and may have clinical applications toward an ex vivo platelet production for transfusion.
33544938	2	74	theme	proteins	299:306	arg1	modification					283:294	Posttranslational modification	265:294	Posttranslational modification of proteins via O-GlcNAcylation	265:326	Posttranslational modification of proteins via O-GlcNAcylation is an ideal metabolic sensor, but how it contributes to megakaryopoiesis and thrombopoiesis remains unknown.
33544938	2	74	theme	proteins	299:306	arg1	sensor					350:355	an ideal metabolic sensor	331:355	an ideal metabolic sensor	331:355	Posttranslational modification of proteins via O-GlcNAcylation is an ideal metabolic sensor, but how it contributes to megakaryopoiesis and thrombopoiesis remains unknown.
33544938	3	75	theme	human-derived	577:589	arg1	HSPCs					632:636	HSPCs	632:636	HSPCs	632:636	Here, we reveal for the first time that cellular O-GlcNAcylation levels decline along the course of megakaryocyte (MK) differentiation from human-derived hematopoietic stem and progenitor cells (HSPCs).
33544938	3	75	theme	human-derived	577:589	arg1	stem					605:608	human-derived hematopoietic stem and progenitor cells	577:629	stem	605:608	Here, we reveal for the first time that cellular O-GlcNAcylation levels decline along the course of megakaryocyte (MK) differentiation from human-derived hematopoietic stem and progenitor cells (HSPCs).
33544938	7	76	theme	platelet	1392:1399	arg1	formation					1401:1409	platelet formation	1392:1409	platelet formation	1392:1409	Depletion of c-Myc upon inhibition of OGT promotes platelet formation in part through the perturbation of cell adhesion molecules, that is, integrin-α4 and integrin-β7, as advised by gene ontology and enrichment analysis for RNA sequencing and validated herein.
30086259	0	0	theme	sensitive	73:81	arg1	biochip					94:100	a sensitive microarray biochip	71:100	a sensitive microarray biochip	71:100	Parallel study on protein O-GlcNAcylation in prostate cancer cell with a sensitive microarray biochip.
30086259	7	1	theme	PC-3 cells	1222:1231	arg1	migration					1209:1217	migration	1209:1217	migration	1209:1217	In addition, the biological behaviors including proliferation and migration of PC-3 cells are also studied when OGA inhibitor Thiamet G is applied to elevate the total O-GlcNAcylation level.
30086259	7	1	theme	PC-3 cells	1222:1231	arg1	proliferation					1191:1203	proliferation	1191:1203	proliferation	1191:1203	In addition, the biological behaviors including proliferation and migration of PC-3 cells are also studied when OGA inhibitor Thiamet G is applied to elevate the total O-GlcNAcylation level.
30086259	0	2	from	study	9:13	arg1	O-GlcNAcylation					26:40	protein O-GlcNAcylation	18:40	protein O-GlcNAcylation	18:40	Parallel study on protein O-GlcNAcylation in prostate cancer cell with a sensitive microarray biochip.
30086259	0	2	from	study	9:13	arg1	cancer					54:59	prostate cancer	45:59	prostate cancer	45:59	Parallel study on protein O-GlcNAcylation in prostate cancer cell with a sensitive microarray biochip.
30086259	5	3	theme	overall	874:880	arg1	O-GlcNAcylation					882:896	the overall O-GlcNAcylation	870:896	the overall O-GlcNAcylation	870:896	The experimental results show that the overall O-GlcNAcylation and OGT expression level are obviously elevated in PC-3 as compared to RWPE-1.
30086259	1	4	theme	high-throughput	263:277	arg1	manner					279:284	high-throughput manner	263:284	high-throughput manner	263:284	Although a variety of approaches have been developed to analyze protein O-GlcNAcylation, efficient investigations on O-GlcNAcylation of proteins of interest in high-throughput manner are still in high demand to further explore its functionality.
30086259	3	5	theme	cancer	700:705	arg1	line					712:715	normal prostate epithelial cell (RWPE-1) and prostate cancer cell line	646:715	line	712:715	The developed array biochip is then utilized to parallelly analyze the O-GlcNAcylation of three oncogenic transcription factors C-Myc, NF-κB and p53 in normal prostate epithelial cell (RWPE-1) and prostate cancer cell line (PC-3).
30086259	0	6	theme	microarray	83:92	arg1	biochip					94:100	a sensitive microarray biochip	71:100	a sensitive microarray biochip	71:100	Parallel study on protein O-GlcNAcylation in prostate cancer cell with a sensitive microarray biochip.
30086259	3	7	theme	prostate	691:698	arg1	line					712:715	normal prostate epithelial cell (RWPE-1) and prostate cancer cell line	646:715	line	712:715	The developed array biochip is then utilized to parallelly analyze the O-GlcNAcylation of three oncogenic transcription factors C-Myc, NF-κB and p53 in normal prostate epithelial cell (RWPE-1) and prostate cancer cell line (PC-3).
30086259	6	8	from	O-GlcNAcylation	1011:1025	arg1	PC-3					1049:1052	PC-3	1049:1052	PC-3	1049:1052	The protein expression-normalized O-GlcNAcylation of C-Myc and NF-κB in PC-3 is significantly higher than that in RWPE-1, while opposite result is observed from p53.
30086259	4	9	theme	transferase	748:758	arg1	levels					729:734	The levels	725:734	The levels of O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA)	725:786	The levels of O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) are also monitored by the microarray platform.
30086259	5	10	theme	expression	906:915	arg1	level					917:921	OGT expression level	902:921	OGT expression level	902:921	The experimental results show that the overall O-GlcNAcylation and OGT expression level are obviously elevated in PC-3 as compared to RWPE-1.
30086259	7	11	theme	inhibitor	1259:1267	arg1	G					1277:1277	OGA inhibitor Thiamet G	1255:1277	OGA inhibitor Thiamet G	1255:1277	In addition, the biological behaviors including proliferation and migration of PC-3 cells are also studied when OGA inhibitor Thiamet G is applied to elevate the total O-GlcNAcylation level.
30086259	0	12	with	cell	61:64	arg1	biochip					94:100	a sensitive microarray biochip	71:100	a sensitive microarray biochip	71:100	Parallel study on protein O-GlcNAcylation in prostate cancer cell with a sensitive microarray biochip.
30086259	2	13	theme	microarray	391:400	arg1	platform					402:409	a powerful microarray platform	380:409	a powerful microarray platform for a sensitive, specific and high-throughput analysis of protein O-GlcNAcylation	380:491	In this work, we first develop a powerful microarray platform for a sensitive, specific and high-throughput analysis of protein O-GlcNAcylation.
30086259	7	14	theme	biological	1160:1169	arg1	behaviors					1171:1179	the biological behaviors	1156:1179	the biological behaviors including proliferation and migration of PC-3 cells	1156:1231	In addition, the biological behaviors including proliferation and migration of PC-3 cells are also studied when OGA inhibitor Thiamet G is applied to elevate the total O-GlcNAcylation level.
30086259	7	14	theme	biological	1160:1169	arg1	migration					1209:1217	migration	1209:1217	migration	1209:1217	In addition, the biological behaviors including proliferation and migration of PC-3 cells are also studied when OGA inhibitor Thiamet G is applied to elevate the total O-GlcNAcylation level.
30086259	7	14	theme	biological	1160:1169	arg1	proliferation					1191:1203	proliferation	1191:1203	proliferation	1191:1203	In addition, the biological behaviors including proliferation and migration of PC-3 cells are also studied when OGA inhibitor Thiamet G is applied to elevate the total O-GlcNAcylation level.
30086259	1	15	theme	protein	167:173	arg1	O-GlcNAcylation					175:189	protein O-GlcNAcylation	167:189	protein O-GlcNAcylation	167:189	Although a variety of approaches have been developed to analyze protein O-GlcNAcylation, efficient investigations on O-GlcNAcylation of proteins of interest in high-throughput manner are still in high demand to further explore its functionality.
30086259	2	16	theme	high-throughput	441:455	arg1	analysis					457:464	a sensitive, specific and high-throughput analysis	415:464	a sensitive, specific and high-throughput analysis of protein O-GlcNAcylation	415:491	In this work, we first develop a powerful microarray platform for a sensitive, specific and high-throughput analysis of protein O-GlcNAcylation.
30086259	7	17	theme	OGA	1255:1257	arg1	G					1277:1277	OGA inhibitor Thiamet G	1255:1277	OGA inhibitor Thiamet G	1255:1277	In addition, the biological behaviors including proliferation and migration of PC-3 cells are also studied when OGA inhibitor Thiamet G is applied to elevate the total O-GlcNAcylation level.
30086259	5	18	theme	experimental	839:850	arg1	results					852:858	The experimental results	835:858	The experimental results	835:858	The experimental results show that the overall O-GlcNAcylation and OGT expression level are obviously elevated in PC-3 as compared to RWPE-1.
30086259	0	19	theme	Parallel	0:7	arg1	study					9:13	Parallel study	0:13	Parallel study on protein O-GlcNAcylation in prostate cancer	0:59	Parallel study on protein O-GlcNAcylation in prostate cancer cell with a sensitive microarray biochip.
30086259	4	20	theme	microarray	814:823	arg1	platform					825:832	the microarray platform	810:832	the microarray platform	810:832	The levels of O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) are also monitored by the microarray platform.
30086259	3	21	theme	oncogenic	590:598	arg1	C-Myc					622:626	C-Myc	622:626	C-Myc	622:626	The developed array biochip is then utilized to parallelly analyze the O-GlcNAcylation of three oncogenic transcription factors C-Myc, NF-κB and p53 in normal prostate epithelial cell (RWPE-1) and prostate cancer cell line (PC-3).
30086259	3	21	theme	oncogenic	590:598	arg1	p53					639:641	p53	639:641	p53	639:641	The developed array biochip is then utilized to parallelly analyze the O-GlcNAcylation of three oncogenic transcription factors C-Myc, NF-κB and p53 in normal prostate epithelial cell (RWPE-1) and prostate cancer cell line (PC-3).
30086259	3	21	theme	oncogenic	590:598	arg1	factors					614:620	three oncogenic transcription factors C-Myc, NF-κB and p53	584:641	three oncogenic transcription factors C-Myc, NF-κB and p53	584:641	The developed array biochip is then utilized to parallelly analyze the O-GlcNAcylation of three oncogenic transcription factors C-Myc, NF-κB and p53 in normal prostate epithelial cell (RWPE-1) and prostate cancer cell line (PC-3).
30086259	3	21	theme	oncogenic	590:598	arg1	NF-κB					629:633	NF-κB	629:633	NF-κB	629:633	The developed array biochip is then utilized to parallelly analyze the O-GlcNAcylation of three oncogenic transcription factors C-Myc, NF-κB and p53 in normal prostate epithelial cell (RWPE-1) and prostate cancer cell line (PC-3).
30086259	0	22	theme	protein	18:24	arg1	O-GlcNAcylation					26:40	protein O-GlcNAcylation	18:40	protein O-GlcNAcylation	18:40	Parallel study on protein O-GlcNAcylation in prostate cancer cell with a sensitive microarray biochip.
30086259	1	23	from	manner	279:284	arg1	proteins					239:246	proteins	239:246	proteins of interest in high-throughput manner	239:284	Although a variety of approaches have been developed to analyze protein O-GlcNAcylation, efficient investigations on O-GlcNAcylation of proteins of interest in high-throughput manner are still in high demand to further explore its functionality.
30086259	4	24	theme	O-GlcNAc	739:746	arg1	OGT					761:763	OGT	761:763	OGT	761:763	The levels of O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) are also monitored by the microarray platform.
30086259	4	24	theme	O-GlcNAc	739:746	arg1	transferase					748:758	O-GlcNAc transferase	739:758	O-GlcNAc transferase (OGT)	739:764	The levels of O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) are also monitored by the microarray platform.
30086259	1	25	theme	efficient	192:200	arg1	investigations					202:215	efficient investigations	192:215	efficient investigations on O-GlcNAcylation of proteins of interest in high-throughput manner	192:284	Although a variety of approaches have been developed to analyze protein O-GlcNAcylation, efficient investigations on O-GlcNAcylation of proteins of interest in high-throughput manner are still in high demand to further explore its functionality.
30086259	1	26	theme	high	299:302	arg1	demand					304:309	high demand	299:309	high demand	299:309	Although a variety of approaches have been developed to analyze protein O-GlcNAcylation, efficient investigations on O-GlcNAcylation of proteins of interest in high-throughput manner are still in high demand to further explore its functionality.
30086259	5	27	gly	O-GlcNAcylation	882:896	arg1	PC-3					949:952	PC-3	949:952	PC-3	949:952	The experimental results show that the overall O-GlcNAcylation and OGT expression level are obviously elevated in PC-3 as compared to RWPE-1.
30086259	3	28	theme	epithelial	662:671	arg1	RWPE-1					679:684	normal prostate epithelial cell (RWPE-1) and prostate cancer cell line	646:715	RWPE-1	679:684	The developed array biochip is then utilized to parallelly analyze the O-GlcNAcylation of three oncogenic transcription factors C-Myc, NF-κB and p53 in normal prostate epithelial cell (RWPE-1) and prostate cancer cell line (PC-3).
30086259	3	28	theme	epithelial	662:671	arg1	PC-3					718:721	PC-3	718:721	PC-3	718:721	The developed array biochip is then utilized to parallelly analyze the O-GlcNAcylation of three oncogenic transcription factors C-Myc, NF-κB and p53 in normal prostate epithelial cell (RWPE-1) and prostate cancer cell line (PC-3).
30086259	6	29	theme	NF-κB	1040:1044	arg1	O-GlcNAcylation					1011:1025	The protein expression-normalized O-GlcNAcylation	977:1025	The protein expression-normalized O-GlcNAcylation of C-Myc and NF-κB in PC-3	977:1052	The protein expression-normalized O-GlcNAcylation of C-Myc and NF-κB in PC-3 is significantly higher than that in RWPE-1, while opposite result is observed from p53.
30086259	6	29	theme	NF-κB	1040:1044	arg1	higher					1071:1076	higher	1071:1076	higher	1071:1076	The protein expression-normalized O-GlcNAcylation of C-Myc and NF-κB in PC-3 is significantly higher than that in RWPE-1, while opposite result is observed from p53.
30086259	2	30	theme	O-GlcNAcylation	477:491	arg1	analysis					457:464	a sensitive, specific and high-throughput analysis	415:464	a sensitive, specific and high-throughput analysis of protein O-GlcNAcylation	415:491	In this work, we first develop a powerful microarray platform for a sensitive, specific and high-throughput analysis of protein O-GlcNAcylation.
30086259	6	31	theme	opposite	1105:1112	arg1	result					1114:1119	opposite result	1105:1119	opposite result	1105:1119	The protein expression-normalized O-GlcNAcylation of C-Myc and NF-κB in PC-3 is significantly higher than that in RWPE-1, while opposite result is observed from p53.
30086259	3	32	theme	cell	673:676	arg1	RWPE-1					679:684	normal prostate epithelial cell (RWPE-1) and prostate cancer cell line	646:715	RWPE-1	679:684	The developed array biochip is then utilized to parallelly analyze the O-GlcNAcylation of three oncogenic transcription factors C-Myc, NF-κB and p53 in normal prostate epithelial cell (RWPE-1) and prostate cancer cell line (PC-3).
30086259	3	32	theme	cell	673:676	arg1	PC-3					718:721	PC-3	718:721	PC-3	718:721	The developed array biochip is then utilized to parallelly analyze the O-GlcNAcylation of three oncogenic transcription factors C-Myc, NF-κB and p53 in normal prostate epithelial cell (RWPE-1) and prostate cancer cell line (PC-3).
30086259	2	33	theme	protein	469:475	arg1	O-GlcNAcylation					477:491	protein O-GlcNAcylation	469:491	protein O-GlcNAcylation	469:491	In this work, we first develop a powerful microarray platform for a sensitive, specific and high-throughput analysis of protein O-GlcNAcylation.
30086259	3	34	theme	normal	646:651	arg1	RWPE-1					679:684	normal prostate epithelial cell (RWPE-1) and prostate cancer cell line	646:715	RWPE-1	679:684	The developed array biochip is then utilized to parallelly analyze the O-GlcNAcylation of three oncogenic transcription factors C-Myc, NF-κB and p53 in normal prostate epithelial cell (RWPE-1) and prostate cancer cell line (PC-3).
30086259	3	34	theme	normal	646:651	arg1	PC-3					718:721	PC-3	718:721	PC-3	718:721	The developed array biochip is then utilized to parallelly analyze the O-GlcNAcylation of three oncogenic transcription factors C-Myc, NF-κB and p53 in normal prostate epithelial cell (RWPE-1) and prostate cancer cell line (PC-3).
30086259	2	35	theme	specific	428:435	arg1	analysis					457:464	a sensitive, specific and high-throughput analysis	415:464	a sensitive, specific and high-throughput analysis of protein O-GlcNAcylation	415:491	In this work, we first develop a powerful microarray platform for a sensitive, specific and high-throughput analysis of protein O-GlcNAcylation.
30086259	6	36	theme	C-Myc	1030:1034	arg1	O-GlcNAcylation					1011:1025	The protein expression-normalized O-GlcNAcylation	977:1025	The protein expression-normalized O-GlcNAcylation of C-Myc and NF-κB in PC-3	977:1052	The protein expression-normalized O-GlcNAcylation of C-Myc and NF-κB in PC-3 is significantly higher than that in RWPE-1, while opposite result is observed from p53.
30086259	6	36	theme	C-Myc	1030:1034	arg1	higher					1071:1076	higher	1071:1076	higher	1071:1076	The protein expression-normalized O-GlcNAcylation of C-Myc and NF-κB in PC-3 is significantly higher than that in RWPE-1, while opposite result is observed from p53.
30086259	3	37	dep	factors	614:620	arg1	C-Myc					622:626	C-Myc	622:626	C-Myc	622:626	The developed array biochip is then utilized to parallelly analyze the O-GlcNAcylation of three oncogenic transcription factors C-Myc, NF-κB and p53 in normal prostate epithelial cell (RWPE-1) and prostate cancer cell line (PC-3).
30086259	3	37	dep	factors	614:620	arg1	p53					639:641	p53	639:641	p53	639:641	The developed array biochip is then utilized to parallelly analyze the O-GlcNAcylation of three oncogenic transcription factors C-Myc, NF-κB and p53 in normal prostate epithelial cell (RWPE-1) and prostate cancer cell line (PC-3).
30086259	3	37	dep	factors	614:620	arg1	factors					614:620	three oncogenic transcription factors C-Myc, NF-κB and p53	584:641	three oncogenic transcription factors C-Myc, NF-κB and p53	584:641	The developed array biochip is then utilized to parallelly analyze the O-GlcNAcylation of three oncogenic transcription factors C-Myc, NF-κB and p53 in normal prostate epithelial cell (RWPE-1) and prostate cancer cell line (PC-3).
30086259	3	37	dep	factors	614:620	arg1	NF-κB					629:633	NF-κB	629:633	NF-κB	629:633	The developed array biochip is then utilized to parallelly analyze the O-GlcNAcylation of three oncogenic transcription factors C-Myc, NF-κB and p53 in normal prostate epithelial cell (RWPE-1) and prostate cancer cell line (PC-3).
30086259	3	38	theme	prostate	653:660	arg1	RWPE-1					679:684	normal prostate epithelial cell (RWPE-1) and prostate cancer cell line	646:715	RWPE-1	679:684	The developed array biochip is then utilized to parallelly analyze the O-GlcNAcylation of three oncogenic transcription factors C-Myc, NF-κB and p53 in normal prostate epithelial cell (RWPE-1) and prostate cancer cell line (PC-3).
30086259	3	38	theme	prostate	653:660	arg1	PC-3					718:721	PC-3	718:721	PC-3	718:721	The developed array biochip is then utilized to parallelly analyze the O-GlcNAcylation of three oncogenic transcription factors C-Myc, NF-κB and p53 in normal prostate epithelial cell (RWPE-1) and prostate cancer cell line (PC-3).
30086259	3	39	theme	transcription	600:612	arg1	C-Myc					622:626	C-Myc	622:626	C-Myc	622:626	The developed array biochip is then utilized to parallelly analyze the O-GlcNAcylation of three oncogenic transcription factors C-Myc, NF-κB and p53 in normal prostate epithelial cell (RWPE-1) and prostate cancer cell line (PC-3).
30086259	3	39	theme	transcription	600:612	arg1	p53					639:641	p53	639:641	p53	639:641	The developed array biochip is then utilized to parallelly analyze the O-GlcNAcylation of three oncogenic transcription factors C-Myc, NF-κB and p53 in normal prostate epithelial cell (RWPE-1) and prostate cancer cell line (PC-3).
30086259	3	39	theme	transcription	600:612	arg1	factors					614:620	three oncogenic transcription factors C-Myc, NF-κB and p53	584:641	three oncogenic transcription factors C-Myc, NF-κB and p53	584:641	The developed array biochip is then utilized to parallelly analyze the O-GlcNAcylation of three oncogenic transcription factors C-Myc, NF-κB and p53 in normal prostate epithelial cell (RWPE-1) and prostate cancer cell line (PC-3).
30086259	3	39	theme	transcription	600:612	arg1	NF-κB					629:633	NF-κB	629:633	NF-κB	629:633	The developed array biochip is then utilized to parallelly analyze the O-GlcNAcylation of three oncogenic transcription factors C-Myc, NF-κB and p53 in normal prostate epithelial cell (RWPE-1) and prostate cancer cell line (PC-3).
30086259	3	40	theme	developed	498:506	arg1	biochip					514:520	The developed array biochip	494:520	The developed array biochip	494:520	The developed array biochip is then utilized to parallelly analyze the O-GlcNAcylation of three oncogenic transcription factors C-Myc, NF-κB and p53 in normal prostate epithelial cell (RWPE-1) and prostate cancer cell line (PC-3).
30086259	0	41	theme	prostate	45:52	arg1	cancer					54:59	prostate cancer	45:59	prostate cancer	45:59	Parallel study on protein O-GlcNAcylation in prostate cancer cell with a sensitive microarray biochip.
30086259	1	42	from	interest	251:258	arg1	manner					279:284	high-throughput manner	263:284	high-throughput manner	263:284	Although a variety of approaches have been developed to analyze protein O-GlcNAcylation, efficient investigations on O-GlcNAcylation of proteins of interest in high-throughput manner are still in high demand to further explore its functionality.
30086259	3	43	theme	factors	614:620	arg1	O-GlcNAcylation					565:579	the O-GlcNAcylation	561:579	the O-GlcNAcylation of three oncogenic transcription factors C-Myc, NF-κB and p53 in normal prostate epithelial cell (RWPE-1) and prostate cancer cell line (PC-3)	561:722	The developed array biochip is then utilized to parallelly analyze the O-GlcNAcylation of three oncogenic transcription factors C-Myc, NF-κB and p53 in normal prostate epithelial cell (RWPE-1) and prostate cancer cell line (PC-3).
30086259	7	44	theme	O-GlcNAcylation	1311:1325	arg1	level					1327:1331	the total O-GlcNAcylation level	1301:1331	the total O-GlcNAcylation level	1301:1331	In addition, the biological behaviors including proliferation and migration of PC-3 cells are also studied when OGA inhibitor Thiamet G is applied to elevate the total O-GlcNAcylation level.
30086259	3	45	theme	array	508:512	arg1	biochip					514:520	The developed array biochip	494:520	The developed array biochip	494:520	The developed array biochip is then utilized to parallelly analyze the O-GlcNAcylation of three oncogenic transcription factors C-Myc, NF-κB and p53 in normal prostate epithelial cell (RWPE-1) and prostate cancer cell line (PC-3).
30086259	3	46	from	O-GlcNAcylation	565:579	arg1	RWPE-1					679:684	normal prostate epithelial cell (RWPE-1) and prostate cancer cell line	646:715	RWPE-1	679:684	The developed array biochip is then utilized to parallelly analyze the O-GlcNAcylation of three oncogenic transcription factors C-Myc, NF-κB and p53 in normal prostate epithelial cell (RWPE-1) and prostate cancer cell line (PC-3).
30086259	3	46	from	O-GlcNAcylation	565:579	arg1	line					712:715	normal prostate epithelial cell (RWPE-1) and prostate cancer cell line	646:715	line	712:715	The developed array biochip is then utilized to parallelly analyze the O-GlcNAcylation of three oncogenic transcription factors C-Myc, NF-κB and p53 in normal prostate epithelial cell (RWPE-1) and prostate cancer cell line (PC-3).
30086259	3	46	from	O-GlcNAcylation	565:579	arg1	PC-3					718:721	PC-3	718:721	PC-3	718:721	The developed array biochip is then utilized to parallelly analyze the O-GlcNAcylation of three oncogenic transcription factors C-Myc, NF-κB and p53 in normal prostate epithelial cell (RWPE-1) and prostate cancer cell line (PC-3).
30086259	7	47	theme	total	1305:1309	arg1	level					1327:1331	the total O-GlcNAcylation level	1301:1331	the total O-GlcNAcylation level	1301:1331	In addition, the biological behaviors including proliferation and migration of PC-3 cells are also studied when OGA inhibitor Thiamet G is applied to elevate the total O-GlcNAcylation level.
30086259	4	48	theme	O-GlcNAcase	770:780	arg1	levels					729:734	The levels	725:734	The levels of O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA)	725:786	The levels of O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) are also monitored by the microarray platform.
30086259	1	49	from	investigations	202:215	arg1	O-GlcNAcylation					220:234	O-GlcNAcylation	220:234	O-GlcNAcylation of proteins of interest in high-throughput manner	220:284	Although a variety of approaches have been developed to analyze protein O-GlcNAcylation, efficient investigations on O-GlcNAcylation of proteins of interest in high-throughput manner are still in high demand to further explore its functionality.
30086259	5	50	theme	OGT	902:904	arg1	level					917:921	OGT expression level	902:921	OGT expression level	902:921	The experimental results show that the overall O-GlcNAcylation and OGT expression level are obviously elevated in PC-3 as compared to RWPE-1.
30086259	1	51	from	proteins	239:246	arg1	manner					279:284	high-throughput manner	263:284	high-throughput manner	263:284	Although a variety of approaches have been developed to analyze protein O-GlcNAcylation, efficient investigations on O-GlcNAcylation of proteins of interest in high-throughput manner are still in high demand to further explore its functionality.
30086259	7	52	theme	Thiamet	1269:1275	arg1	G					1277:1277	OGA inhibitor Thiamet G	1255:1277	OGA inhibitor Thiamet G	1255:1277	In addition, the biological behaviors including proliferation and migration of PC-3 cells are also studied when OGA inhibitor Thiamet G is applied to elevate the total O-GlcNAcylation level.
30086259	1	53	theme	approaches	125:134	arg1	approaches					125:134	approaches	125:134	approaches	125:134	Although a variety of approaches have been developed to analyze protein O-GlcNAcylation, efficient investigations on O-GlcNAcylation of proteins of interest in high-throughput manner are still in high demand to further explore its functionality.
30086259	1	53	theme	approaches	125:134	arg1	variety					114:120	a variety	112:120	a variety of approaches	112:134	Although a variety of approaches have been developed to analyze protein O-GlcNAcylation, efficient investigations on O-GlcNAcylation of proteins of interest in high-throughput manner are still in high demand to further explore its functionality.
30086259	1	54	theme	proteins	239:246	arg1	O-GlcNAcylation					220:234	O-GlcNAcylation	220:234	O-GlcNAcylation of proteins of interest in high-throughput manner	220:284	Although a variety of approaches have been developed to analyze protein O-GlcNAcylation, efficient investigations on O-GlcNAcylation of proteins of interest in high-throughput manner are still in high demand to further explore its functionality.
30086259	3	55	used	utilized	530:537	arg2	biochip					514:520	The developed array biochip	494:520	The developed array biochip	494:520	The developed array biochip is then utilized to parallelly analyze the O-GlcNAcylation of three oncogenic transcription factors C-Myc, NF-κB and p53 in normal prostate epithelial cell (RWPE-1) and prostate cancer cell line (PC-3).
30086259	2	56	theme	sensitive	417:425	arg1	analysis					457:464	a sensitive, specific and high-throughput analysis	415:464	a sensitive, specific and high-throughput analysis of protein O-GlcNAcylation	415:491	In this work, we first develop a powerful microarray platform for a sensitive, specific and high-throughput analysis of protein O-GlcNAcylation.
30086259	2	57	theme	powerful	382:389	arg1	platform					402:409	a powerful microarray platform	380:409	a powerful microarray platform for a sensitive, specific and high-throughput analysis of protein O-GlcNAcylation	380:491	In this work, we first develop a powerful microarray platform for a sensitive, specific and high-throughput analysis of protein O-GlcNAcylation.
30086259	6	58	theme	expression-normalized	989:1009	arg1	O-GlcNAcylation					1011:1025	The protein expression-normalized O-GlcNAcylation	977:1025	The protein expression-normalized O-GlcNAcylation of C-Myc and NF-κB in PC-3	977:1052	The protein expression-normalized O-GlcNAcylation of C-Myc and NF-κB in PC-3 is significantly higher than that in RWPE-1, while opposite result is observed from p53.
30086259	6	58	theme	expression-normalized	989:1009	arg1	higher					1071:1076	higher	1071:1076	higher	1071:1076	The protein expression-normalized O-GlcNAcylation of C-Myc and NF-κB in PC-3 is significantly higher than that in RWPE-1, while opposite result is observed from p53.
30086259	3	59	theme	cell	707:710	arg1	line					712:715	normal prostate epithelial cell (RWPE-1) and prostate cancer cell line	646:715	line	712:715	The developed array biochip is then utilized to parallelly analyze the O-GlcNAcylation of three oncogenic transcription factors C-Myc, NF-κB and p53 in normal prostate epithelial cell (RWPE-1) and prostate cancer cell line (PC-3).
30086259	6	60	theme	protein	981:987	arg1	O-GlcNAcylation					1011:1025	The protein expression-normalized O-GlcNAcylation	977:1025	The protein expression-normalized O-GlcNAcylation of C-Myc and NF-κB in PC-3	977:1052	The protein expression-normalized O-GlcNAcylation of C-Myc and NF-κB in PC-3 is significantly higher than that in RWPE-1, while opposite result is observed from p53.
30086259	6	60	theme	protein	981:987	arg1	higher					1071:1076	higher	1071:1076	higher	1071:1076	The protein expression-normalized O-GlcNAcylation of C-Myc and NF-κB in PC-3 is significantly higher than that in RWPE-1, while opposite result is observed from p53.
30086259	1	61	theme	interest	251:258	arg1	proteins					239:246	proteins	239:246	proteins of interest in high-throughput manner	239:284	Although a variety of approaches have been developed to analyze protein O-GlcNAcylation, efficient investigations on O-GlcNAcylation of proteins of interest in high-throughput manner are still in high demand to further explore its functionality.
22665487	6	0	theme	sugar	758:762	arg1	UDP-N-acetylglucosamine					716:738	UDP-N-acetylglucosamine	716:738	UDP-N-acetylglucosamine (UDP-GlcNAc)	716:751	Here we show that TpeL preferably utilizes UDP-N-acetylglucosamine (UDP-GlcNAc) as a sugar donor.
22665487	6	0	theme	sugar	758:762	arg1	donor					764:768	a sugar donor	756:768	a sugar donor	756:768	Here we show that TpeL preferably utilizes UDP-N-acetylglucosamine (UDP-GlcNAc) as a sugar donor.
22665487	10	1	theme	extended	1256:1263	arg1	TpeL1-1779					1291:1300	TpeL1-1779	1291:1300	TpeL1-1779	1291:1300	A C-terminally extended TpeL full-length variant (TpeL1-1779) induces apoptosis in HeLa cells (most likely by mono-O-GlcNAcylation of Ras), and inhibits Ras signaling including Ras-Raf interaction and ERK activation.
22665487	10	1	theme	extended	1256:1263	arg1	variant					1282:1288	A C-terminally extended TpeL full-length variant	1241:1288	A C-terminally extended TpeL full-length variant (TpeL1-1779)	1241:1301	A C-terminally extended TpeL full-length variant (TpeL1-1779) induces apoptosis in HeLa cells (most likely by mono-O-GlcNAcylation of Ras), and inhibits Ras signaling including Ras-Raf interaction and ERK activation.
22665487	0	2	theme	mono-O-GlcNAcylation	84:103	arg1	consequences					68:79	consequences	68:79	consequences of mono-O-GlcNAcylation of Ras in living cells	68:126	Molecular characteristics of Clostridium perfringens TpeL toxin and consequences of mono-O-GlcNAcylation of Ras in living cells.
22665487	0	2	theme	mono-O-GlcNAcylation	84:103	arg1	characteristics					10:24	Molecular characteristics	0:24	Molecular characteristics of Clostridium perfringens TpeL toxin	0:62	Molecular characteristics of Clostridium perfringens TpeL toxin and consequences of mono-O-GlcNAcylation of Ras in living cells.
22665487	10	3	theme	C-terminally	1243:1254	arg1	TpeL1-1779					1291:1300	TpeL1-1779	1291:1300	TpeL1-1779	1291:1300	A C-terminally extended TpeL full-length variant (TpeL1-1779) induces apoptosis in HeLa cells (most likely by mono-O-GlcNAcylation of Ras), and inhibits Ras signaling including Ras-Raf interaction and ERK activation.
22665487	10	3	theme	C-terminally	1243:1254	arg1	variant					1282:1288	A C-terminally extended TpeL full-length variant	1241:1288	A C-terminally extended TpeL full-length variant (TpeL1-1779)	1241:1301	A C-terminally extended TpeL full-length variant (TpeL1-1779) induces apoptosis in HeLa cells (most likely by mono-O-GlcNAcylation of Ras), and inhibits Ras signaling including Ras-Raf interaction and ERK activation.
22665487	7	4	theme	TpeL	796:799	arg1	383					789:791	alanine 383	781:791	alanine 383 of TpeL	781:799	Change of alanine 383 of TpeL to isoleucine turns the sugar donor preference from UDP-GlcNAc to UDP-glucose.
22665487	1	5	theme	family	153:158	arg1	TpeL					129:132	TpeL	129:132	TpeL	129:132	TpeL is a member of the family of clostridial glucosylating toxins produced by Clostridium perfringens type A, B, and C strains.
22665487	1	5	theme	family	153:158	arg1	member					139:144	a member	137:144	a member of the family of clostridial glucosylating toxins produced by Clostridium perfringens type A, B, and C strains	137:255	TpeL is a member of the family of clostridial glucosylating toxins produced by Clostridium perfringens type A, B, and C strains.
22665487	12	6	theme	C-terminal	1646:1655	arg1	domain					1676:1681	a typical C-terminal polypeptide repeat domain	1636:1681	a typical C-terminal polypeptide repeat domain	1636:1681	TpeL is a glucosylating toxin, which modifies Ras and induces apoptosis in target cells without having a typical C-terminal polypeptide repeat domain.
22665487	9	7	theme	inositol	1115:1122	arg1	InsP					1142:1145	InsP(6)	1142:1148	InsP(6)	1142:1148	The toxin is autoproteolytically processed in the presence of inositol hexakisphosphate (InsP(6)) by an intrinsic cysteine protease domain, located next to the glucosyltransferase domain.
22665487	9	7	theme	inositol	1115:1122	arg1	hexakisphosphate					1124:1139	inositol hexakisphosphate	1115:1139	inositol hexakisphosphate (InsP(6))	1115:1149	The toxin is autoproteolytically processed in the presence of inositol hexakisphosphate (InsP(6)) by an intrinsic cysteine protease domain, located next to the glucosyltransferase domain.
22665487	5	8	dep	79	659:660	arg1	905-910					663:669	905-910	663:669	905-910	663:669	79, 905-910).
22665487	10	9	from	apoptosis	1311:1319	arg1	cells					1329:1333	HeLa cells	1324:1333	HeLa cells	1324:1333	A C-terminally extended TpeL full-length variant (TpeL1-1779) induces apoptosis in HeLa cells (most likely by mono-O-GlcNAcylation of Ras), and inhibits Ras signaling including Ras-Raf interaction and ERK activation.
22665487	10	10	theme	full-length	1270:1280	arg1	TpeL1-1779					1291:1300	TpeL1-1779	1291:1300	TpeL1-1779	1291:1300	A C-terminally extended TpeL full-length variant (TpeL1-1779) induces apoptosis in HeLa cells (most likely by mono-O-GlcNAcylation of Ras), and inhibits Ras signaling including Ras-Raf interaction and ERK activation.
22665487	10	10	theme	full-length	1270:1280	arg1	variant					1282:1288	A C-terminally extended TpeL full-length variant	1241:1288	A C-terminally extended TpeL full-length variant (TpeL1-1779)	1241:1301	A C-terminally extended TpeL full-length variant (TpeL1-1779) induces apoptosis in HeLa cells (most likely by mono-O-GlcNAcylation of Ras), and inhibits Ras signaling including Ras-Raf interaction and ERK activation.
22665487	1	11	theme	C	247:247	arg1	strains					249:255	Clostridium perfringens type A, B, and C strains	208:255	Clostridium perfringens type A, B, and C strains	208:255	TpeL is a member of the family of clostridial glucosylating toxins produced by Clostridium perfringens type A, B, and C strains.
22665487	0	12	theme	Ras	108:110	arg1	mono-O-GlcNAcylation					84:103	mono-O-GlcNAcylation	84:103	mono-O-GlcNAcylation of Ras in living cells	84:126	Molecular characteristics of Clostridium perfringens TpeL toxin and consequences of mono-O-GlcNAcylation of Ras in living cells.
22665487	9	13	theme	hexakisphosphate	1124:1139	arg1	presence					1103:1110	the presence	1099:1110	the presence of inositol hexakisphosphate (InsP(6))	1099:1149	The toxin is autoproteolytically processed in the presence of inositol hexakisphosphate (InsP(6)) by an intrinsic cysteine protease domain, located next to the glucosyltransferase domain.
22665487	7	14	theme	383	789:791	arg1	Change					771:776	Change	771:776	Change of alanine 383 of TpeL to isoleucine	771:813	Change of alanine 383 of TpeL to isoleucine turns the sugar donor preference from UDP-GlcNAc to UDP-glucose.
22665487	3	15	theme	by	495:496	arg1	mono-O-glucosylation					498:517	mono-O-glucosylation	498:517	mono-O-glucosylation	498:517	It was shown that the glucosyltransferase domain of TpeL modifies Ras in vitro by mono-O-glucosylation or mono-O-GlcNAcylation (Nagahama, M., Ohkubo, A., Oda, M., Kobayashi, K., Amimoto, K., Miyamoto, K., and Sakurai, J. (2011) Infect.
22665487	10	16	theme	Ras	1375:1377	arg1	mono-O-GlcNAcylation					1351:1370	mono-O-GlcNAcylation	1351:1370	mono-O-GlcNAcylation of Ras	1351:1377	A C-terminally extended TpeL full-length variant (TpeL1-1779) induces apoptosis in HeLa cells (most likely by mono-O-GlcNAcylation of Ras), and inhibits Ras signaling including Ras-Raf interaction and ERK activation.
22665487	3	17	dep	M.	554:555	arg1	2011					638:641	2011	638:641	Nagahama, M., Ohkubo, A., Oda, M., Kobayashi, K., Amimoto, K., Miyamoto, K., and Sakurai, J. (2011	544:641	It was shown that the glucosyltransferase domain of TpeL modifies Ras in vitro by mono-O-glucosylation or mono-O-GlcNAcylation (Nagahama, M., Ohkubo, A., Oda, M., Kobayashi, K., Amimoto, K., Miyamoto, K., and Sakurai, J. (2011) Infect.
22665487	0	18	theme	living	115:120	arg1	cells					122:126	living cells	115:126	living cells	115:126	Molecular characteristics of Clostridium perfringens TpeL toxin and consequences of mono-O-GlcNAcylation of Ras in living cells.
22665487	2	19	theme	target	395:400	arg1	binding					407:413	target cell binding	395:413	target cell binding	395:413	In contrast to other members of this toxin family, it lacks a C-terminal polypeptide repeat domain, which is suggested to be involved in target cell binding.
22665487	10	20	theme	ERK	1442:1444	arg1	activation					1446:1455	ERK activation	1442:1455	ERK activation	1442:1455	A C-terminally extended TpeL full-length variant (TpeL1-1779) induces apoptosis in HeLa cells (most likely by mono-O-GlcNAcylation of Ras), and inhibits Ras signaling including Ras-Raf interaction and ERK activation.
22665487	1	21	theme	clostridial	163:173	arg1	toxins					189:194	clostridial glucosylating toxins	163:194	clostridial glucosylating toxins produced by Clostridium perfringens type A, B, and C strains	163:255	TpeL is a member of the family of clostridial glucosylating toxins produced by Clostridium perfringens type A, B, and C strains.
22665487	2	22	theme	cell	402:405	arg1	binding					407:413	target cell binding	395:413	target cell binding	395:413	In contrast to other members of this toxin family, it lacks a C-terminal polypeptide repeat domain, which is suggested to be involved in target cell binding.
22665487	10	23	theme	Ras	1394:1396	arg1	signaling					1398:1406	Ras signaling	1394:1406	Ras signaling including Ras-Raf interaction and ERK activation	1394:1455	A C-terminally extended TpeL full-length variant (TpeL1-1779) induces apoptosis in HeLa cells (most likely by mono-O-GlcNAcylation of Ras), and inhibits Ras signaling including Ras-Raf interaction and ERK activation.
22665487	7	24	theme	alanine	781:787	arg1	383					789:791	alanine 383	781:791	alanine 383 of TpeL	781:799	Change of alanine 383 of TpeL to isoleucine turns the sugar donor preference from UDP-GlcNAc to UDP-glucose.
22665487	1	25	theme	glucosylating	175:187	arg1	toxins					189:194	clostridial glucosylating toxins	163:194	clostridial glucosylating toxins produced by Clostridium perfringens type A, B, and C strains	163:255	TpeL is a member of the family of clostridial glucosylating toxins produced by Clostridium perfringens type A, B, and C strains.
22665487	0	26	theme	Molecular	0:8	arg1	characteristics					10:24	Molecular characteristics	0:24	Molecular characteristics of Clostridium perfringens TpeL toxin	0:62	Molecular characteristics of Clostridium perfringens TpeL toxin and consequences of mono-O-GlcNAcylation of Ras in living cells.
22665487	8	27	theme	previous	895:902	arg1	studies					904:910	previous studies	895:910	previous studies	895:910	In contrast to previous studies, we show that Rac is a poor substrate in vitro and in vivo and requires 1-2 magnitudes higher toxin concentrations for modification by TpeL.
22665487	12	28	theme	glucosylating	1543:1555	arg1	TpeL					1533:1536	TpeL	1533:1536	TpeL	1533:1536	TpeL is a glucosylating toxin, which modifies Ras and induces apoptosis in target cells without having a typical C-terminal polypeptide repeat domain.
22665487	12	28	theme	glucosylating	1543:1555	arg1	toxin					1557:1561	a glucosylating toxin	1541:1561	a glucosylating toxin	1541:1561	TpeL is a glucosylating toxin, which modifies Ras and induces apoptosis in target cells without having a typical C-terminal polypeptide repeat domain.
22665487	1	29	theme	toxins	189:194	arg1	family					153:158	the family	149:158	the family of clostridial glucosylating toxins produced by Clostridium perfringens type A, B, and C strains	149:255	TpeL is a member of the family of clostridial glucosylating toxins produced by Clostridium perfringens type A, B, and C strains.
22665487	0	30	theme	Clostridium	29:39	arg1	toxin					58:62	Clostridium perfringens TpeL toxin	29:62	Clostridium perfringens TpeL toxin	29:62	Molecular characteristics of Clostridium perfringens TpeL toxin and consequences of mono-O-GlcNAcylation of Ras in living cells.
22665487	12	31	theme	repeat	1669:1674	arg1	domain					1676:1681	a typical C-terminal polypeptide repeat domain	1636:1681	a typical C-terminal polypeptide repeat domain	1636:1681	TpeL is a glucosylating toxin, which modifies Ras and induces apoptosis in target cells without having a typical C-terminal polypeptide repeat domain.
22665487	10	32	dep	induces	1303:1309	arg1	mono-O-GlcNAcylation					1351:1370	mono-O-GlcNAcylation	1351:1370	mono-O-GlcNAcylation of Ras	1351:1377	A C-terminally extended TpeL full-length variant (TpeL1-1779) induces apoptosis in HeLa cells (most likely by mono-O-GlcNAcylation of Ras), and inhibits Ras signaling including Ras-Raf interaction and ERK activation.
22665487	10	33	theme	TpeL	1265:1268	arg1	TpeL1-1779					1291:1300	TpeL1-1779	1291:1300	TpeL1-1779	1291:1300	A C-terminally extended TpeL full-length variant (TpeL1-1779) induces apoptosis in HeLa cells (most likely by mono-O-GlcNAcylation of Ras), and inhibits Ras signaling including Ras-Raf interaction and ERK activation.
22665487	10	33	theme	TpeL	1265:1268	arg1	variant					1282:1288	A C-terminally extended TpeL full-length variant	1241:1288	A C-terminally extended TpeL full-length variant (TpeL1-1779)	1241:1301	A C-terminally extended TpeL full-length variant (TpeL1-1779) induces apoptosis in HeLa cells (most likely by mono-O-GlcNAcylation of Ras), and inhibits Ras signaling including Ras-Raf interaction and ERK activation.
22665487	7	34	theme	sugar	825:829	arg1	preference					837:846	the sugar donor preference	821:846	the sugar donor preference from UDP-GlcNAc	821:862	Change of alanine 383 of TpeL to isoleucine turns the sugar donor preference from UDP-GlcNAc to UDP-glucose.
22665487	12	35	theme	polypeptide	1657:1667	arg1	domain					1676:1681	a typical C-terminal polypeptide repeat domain	1636:1681	a typical C-terminal polypeptide repeat domain	1636:1681	TpeL is a glucosylating toxin, which modifies Ras and induces apoptosis in target cells without having a typical C-terminal polypeptide repeat domain.
22665487	2	36	theme	other	273:277	arg1	members					279:285	other members	273:285	other members of this toxin family	273:306	In contrast to other members of this toxin family, it lacks a C-terminal polypeptide repeat domain, which is suggested to be involved in target cell binding.
22665487	3	37	theme	TpeL	468:471	arg1	TpeL					468:471	TpeL	468:471	TpeL	468:471	It was shown that the glucosyltransferase domain of TpeL modifies Ras in vitro by mono-O-glucosylation or mono-O-GlcNAcylation (Nagahama, M., Ohkubo, A., Oda, M., Kobayashi, K., Amimoto, K., Miyamoto, K., and Sakurai, J. (2011) Infect.
22665487	3	37	theme	TpeL	468:471	arg1	domain					458:463	the glucosyltransferase domain	434:463	the glucosyltransferase domain of TpeL	434:471	It was shown that the glucosyltransferase domain of TpeL modifies Ras in vitro by mono-O-glucosylation or mono-O-GlcNAcylation (Nagahama, M., Ohkubo, A., Oda, M., Kobayashi, K., Amimoto, K., Miyamoto, K., and Sakurai, J. (2011) Infect.
22665487	0	38	theme	TpeL	53:56	arg1	toxin					58:62	Clostridium perfringens TpeL toxin	29:62	Clostridium perfringens TpeL toxin	29:62	Molecular characteristics of Clostridium perfringens TpeL toxin and consequences of mono-O-GlcNAcylation of Ras in living cells.
22665487	11	39	from	signaling	1487:1495	arg1	cells					1526:1530	rat pheochromocytoma PC12 cells	1500:1530	rat pheochromocytoma PC12 cells	1500:1530	In addition, TpeL blocks Ras signaling in rat pheochromocytoma PC12 cells.
22665487	0	40	from	mono-O-GlcNAcylation	84:103	arg1	cells					122:126	living cells	115:126	living cells	115:126	Molecular characteristics of Clostridium perfringens TpeL toxin and consequences of mono-O-GlcNAcylation of Ras in living cells.
22665487	11	41	theme	rat	1500:1502	arg1	cells					1526:1530	rat pheochromocytoma PC12 cells	1500:1530	rat pheochromocytoma PC12 cells	1500:1530	In addition, TpeL blocks Ras signaling in rat pheochromocytoma PC12 cells.
22665487	2	42	theme	repeat	343:348	arg1	domain					350:355	a C-terminal polypeptide repeat domain	318:355	a C-terminal polypeptide repeat domain	318:355	In contrast to other members of this toxin family, it lacks a C-terminal polypeptide repeat domain, which is suggested to be involved in target cell binding.
22665487	1	43	theme	Clostridium	208:218	arg1	A					237:237	Clostridium perfringens type A	208:237	Clostridium perfringens type A	208:237	TpeL is a member of the family of clostridial glucosylating toxins produced by Clostridium perfringens type A, B, and C strains.
22665487	11	44	theme	Ras	1483:1485	arg1	signaling					1487:1495	Ras signaling	1483:1495	Ras signaling in rat pheochromocytoma PC12 cells	1483:1530	In addition, TpeL blocks Ras signaling in rat pheochromocytoma PC12 cells.
22665487	8	45	theme	toxin	1006:1010	arg1	concentrations					1012:1025	1-2 magnitudes higher toxin concentrations	984:1025	1-2 magnitudes higher toxin concentrations	984:1025	In contrast to previous studies, we show that Rac is a poor substrate in vitro and in vivo and requires 1-2 magnitudes higher toxin concentrations for modification by TpeL.
22665487	12	46	theme	target	1608:1613	arg1	cells					1615:1619	target cells	1608:1619	target cells	1608:1619	TpeL is a glucosylating toxin, which modifies Ras and induces apoptosis in target cells without having a typical C-terminal polypeptide repeat domain.
22665487	7	47	from	UDP-GlcNAc	853:862	arg1	preference					837:846	the sugar donor preference	821:846	the sugar donor preference from UDP-GlcNAc	821:862	Change of alanine 383 of TpeL to isoleucine turns the sugar donor preference from UDP-GlcNAc to UDP-glucose.
22665487	10	48	theme	Ras-Raf	1418:1424	arg1	interaction					1426:1436	Ras-Raf interaction	1418:1436	Ras-Raf interaction	1418:1436	A C-terminally extended TpeL full-length variant (TpeL1-1779) induces apoptosis in HeLa cells (most likely by mono-O-GlcNAcylation of Ras), and inhibits Ras signaling including Ras-Raf interaction and ERK activation.
22665487	9	49	theme	intrinsic	1157:1165	arg1	domain					1185:1190	an intrinsic cysteine protease domain	1154:1190	an intrinsic cysteine protease domain	1154:1190	The toxin is autoproteolytically processed in the presence of inositol hexakisphosphate (InsP(6)) by an intrinsic cysteine protease domain, located next to the glucosyltransferase domain.
22665487	10	50	theme	HeLa	1324:1327	arg1	cells					1329:1333	HeLa cells	1324:1333	HeLa cells	1324:1333	A C-terminally extended TpeL full-length variant (TpeL1-1779) induces apoptosis in HeLa cells (most likely by mono-O-GlcNAcylation of Ras), and inhibits Ras signaling including Ras-Raf interaction and ERK activation.
22665487	0	51	theme	toxin	58:62	arg1	consequences					68:79	consequences	68:79	consequences of mono-O-GlcNAcylation of Ras in living cells	68:126	Molecular characteristics of Clostridium perfringens TpeL toxin and consequences of mono-O-GlcNAcylation of Ras in living cells.
22665487	0	51	theme	toxin	58:62	arg1	characteristics					10:24	Molecular characteristics	0:24	Molecular characteristics of Clostridium perfringens TpeL toxin	0:62	Molecular characteristics of Clostridium perfringens TpeL toxin and consequences of mono-O-GlcNAcylation of Ras in living cells.
22665487	9	52	theme	cysteine	1167:1174	arg1	domain					1185:1190	an intrinsic cysteine protease domain	1154:1190	an intrinsic cysteine protease domain	1154:1190	The toxin is autoproteolytically processed in the presence of inositol hexakisphosphate (InsP(6)) by an intrinsic cysteine protease domain, located next to the glucosyltransferase domain.
22665487	0	53	from	cells	122:126	arg1	mono-O-GlcNAcylation					84:103	mono-O-GlcNAcylation	84:103	mono-O-GlcNAcylation of Ras in living cells	84:126	Molecular characteristics of Clostridium perfringens TpeL toxin and consequences of mono-O-GlcNAcylation of Ras in living cells.
22665487	7	54	theme	donor	831:835	arg1	preference					837:846	the sugar donor preference	821:846	the sugar donor preference from UDP-GlcNAc	821:862	Change of alanine 383 of TpeL to isoleucine turns the sugar donor preference from UDP-GlcNAc to UDP-glucose.
22665487	3	55	theme	glucosyltransferase	438:456	arg1	TpeL					468:471	TpeL	468:471	TpeL	468:471	It was shown that the glucosyltransferase domain of TpeL modifies Ras in vitro by mono-O-glucosylation or mono-O-GlcNAcylation (Nagahama, M., Ohkubo, A., Oda, M., Kobayashi, K., Amimoto, K., Miyamoto, K., and Sakurai, J. (2011) Infect.
22665487	3	55	theme	glucosyltransferase	438:456	arg1	domain					458:463	the glucosyltransferase domain	434:463	the glucosyltransferase domain of TpeL	434:471	It was shown that the glucosyltransferase domain of TpeL modifies Ras in vitro by mono-O-glucosylation or mono-O-GlcNAcylation (Nagahama, M., Ohkubo, A., Oda, M., Kobayashi, K., Amimoto, K., Miyamoto, K., and Sakurai, J. (2011) Infect.
22665487	9	56	theme	protease	1176:1183	arg1	domain					1185:1190	an intrinsic cysteine protease domain	1154:1190	an intrinsic cysteine protease domain	1154:1190	The toxin is autoproteolytically processed in the presence of inositol hexakisphosphate (InsP(6)) by an intrinsic cysteine protease domain, located next to the glucosyltransferase domain.
22665487	8	57	theme	poor	935:938	arg1	substrate					940:948	a poor substrate	933:948	a poor substrate	933:948	In contrast to previous studies, we show that Rac is a poor substrate in vitro and in vivo and requires 1-2 magnitudes higher toxin concentrations for modification by TpeL.
22665487	8	57	theme	poor	935:938	arg1	Rac					926:928	Rac	926:928	Rac	926:928	In contrast to previous studies, we show that Rac is a poor substrate in vitro and in vivo and requires 1-2 magnitudes higher toxin concentrations for modification by TpeL.
22665487	0	58	dep	Clostridium	29:39	arg1	perfringens					41:51	perfringens	41:51	perfringens	41:51	Molecular characteristics of Clostridium perfringens TpeL toxin and consequences of mono-O-GlcNAcylation of Ras in living cells.
22665487	1	59	dep	Clostridium	208:218	arg1	perfringens					220:230	perfringens	220:230	perfringens	220:230	TpeL is a member of the family of clostridial glucosylating toxins produced by Clostridium perfringens type A, B, and C strains.
22665487	11	60	theme	PC12	1521:1524	arg1	cells					1526:1530	rat pheochromocytoma PC12 cells	1500:1530	rat pheochromocytoma PC12 cells	1500:1530	In addition, TpeL blocks Ras signaling in rat pheochromocytoma PC12 cells.
22665487	2	61	theme	family	301:306	arg1	members					279:285	other members	273:285	other members of this toxin family	273:306	In contrast to other members of this toxin family, it lacks a C-terminal polypeptide repeat domain, which is suggested to be involved in target cell binding.
22665487	1	62	theme	type	232:235	arg1	A					237:237	Clostridium perfringens type A	208:237	Clostridium perfringens type A	208:237	TpeL is a member of the family of clostridial glucosylating toxins produced by Clostridium perfringens type A, B, and C strains.
22665487	12	63	theme	typical	1638:1644	arg1	domain					1676:1681	a typical C-terminal polypeptide repeat domain	1636:1681	a typical C-terminal polypeptide repeat domain	1636:1681	TpeL is a glucosylating toxin, which modifies Ras and induces apoptosis in target cells without having a typical C-terminal polypeptide repeat domain.
22665487	11	64	theme	pheochromocytoma	1504:1519	arg1	cells					1526:1530	rat pheochromocytoma PC12 cells	1500:1530	rat pheochromocytoma PC12 cells	1500:1530	In addition, TpeL blocks Ras signaling in rat pheochromocytoma PC12 cells.
22665487	2	65	theme	toxin	295:299	arg1	family					301:306	this toxin family	290:306	this toxin family	290:306	In contrast to other members of this toxin family, it lacks a C-terminal polypeptide repeat domain, which is suggested to be involved in target cell binding.
22665487	1	66	theme	A	237:237	arg1	strains					249:255	Clostridium perfringens type A, B, and C strains	208:255	Clostridium perfringens type A, B, and C strains	208:255	TpeL is a member of the family of clostridial glucosylating toxins produced by Clostridium perfringens type A, B, and C strains.
22665487	8	67	dep	studies	904:910	arg1	contrast					883:890	contrast	883:890	contrast	883:890	In contrast to previous studies, we show that Rac is a poor substrate in vitro and in vivo and requires 1-2 magnitudes higher toxin concentrations for modification by TpeL.
22665487	0	68	from	Ras	108:110	arg1	cells					122:126	living cells	115:126	living cells	115:126	Molecular characteristics of Clostridium perfringens TpeL toxin and consequences of mono-O-GlcNAcylation of Ras in living cells.
22665487	3	69	dep	mono-O-glucosylation	498:517	arg1	M.					554:555	M.	554:555	M.	554:555	It was shown that the glucosyltransferase domain of TpeL modifies Ras in vitro by mono-O-glucosylation or mono-O-GlcNAcylation (Nagahama, M., Ohkubo, A., Oda, M., Kobayashi, K., Amimoto, K., Miyamoto, K., and Sakurai, J. (2011) Infect.
22665487	3	69	dep	mono-O-glucosylation	498:517	arg1	Oda					570:572	Oda	570:572	Oda	570:572	It was shown that the glucosyltransferase domain of TpeL modifies Ras in vitro by mono-O-glucosylation or mono-O-GlcNAcylation (Nagahama, M., Ohkubo, A., Oda, M., Kobayashi, K., Amimoto, K., Miyamoto, K., and Sakurai, J. (2011) Infect.
22665487	3	69	dep	mono-O-glucosylation	498:517	arg1	K.					617:618	K.	617:618	K.	617:618	It was shown that the glucosyltransferase domain of TpeL modifies Ras in vitro by mono-O-glucosylation or mono-O-GlcNAcylation (Nagahama, M., Ohkubo, A., Oda, M., Kobayashi, K., Amimoto, K., Miyamoto, K., and Sakurai, J. (2011) Infect.
22665487	3	69	dep	mono-O-glucosylation	498:517	arg1	M.					575:576	M.	575:576	M.	575:576	It was shown that the glucosyltransferase domain of TpeL modifies Ras in vitro by mono-O-glucosylation or mono-O-GlcNAcylation (Nagahama, M., Ohkubo, A., Oda, M., Kobayashi, K., Amimoto, K., Miyamoto, K., and Sakurai, J. (2011) Infect.
22665487	3	69	dep	mono-O-glucosylation	498:517	arg1	Amimoto					594:600	Amimoto	594:600	Amimoto	594:600	It was shown that the glucosyltransferase domain of TpeL modifies Ras in vitro by mono-O-glucosylation or mono-O-GlcNAcylation (Nagahama, M., Ohkubo, A., Oda, M., Kobayashi, K., Amimoto, K., Miyamoto, K., and Sakurai, J. (2011) Infect.
22665487	3	69	dep	mono-O-glucosylation	498:517	arg1	K.					603:604	K.	603:604	K.	603:604	It was shown that the glucosyltransferase domain of TpeL modifies Ras in vitro by mono-O-glucosylation or mono-O-GlcNAcylation (Nagahama, M., Ohkubo, A., Oda, M., Kobayashi, K., Amimoto, K., Miyamoto, K., and Sakurai, J. (2011) Infect.
22665487	3	69	dep	mono-O-glucosylation	498:517	arg1	A.					566:567	A.	566:567	A.	566:567	It was shown that the glucosyltransferase domain of TpeL modifies Ras in vitro by mono-O-glucosylation or mono-O-GlcNAcylation (Nagahama, M., Ohkubo, A., Oda, M., Kobayashi, K., Amimoto, K., Miyamoto, K., and Sakurai, J. (2011) Infect.
22665487	3	69	dep	mono-O-glucosylation	498:517	arg1	Kobayashi					579:587	Kobayashi	579:587	Kobayashi	579:587	It was shown that the glucosyltransferase domain of TpeL modifies Ras in vitro by mono-O-glucosylation or mono-O-GlcNAcylation (Nagahama, M., Ohkubo, A., Oda, M., Kobayashi, K., Amimoto, K., Miyamoto, K., and Sakurai, J. (2011) Infect.
22665487	3	69	dep	mono-O-glucosylation	498:517	arg1	vitro					489:493	vitro by mono-O-glucosylation or mono-O-GlcNAcylation (Nagahama, M., Ohkubo, A., Oda, M., Kobayashi, K., Amimoto, K., Miyamoto, K., and Sakurai, J. (2011) Infect	489:649	vitro by mono-O-glucosylation or mono-O-GlcNAcylation (Nagahama, M., Ohkubo, A., Oda, M., Kobayashi, K., Amimoto, K., Miyamoto, K., and Sakurai, J. (2011) Infect	489:649	It was shown that the glucosyltransferase domain of TpeL modifies Ras in vitro by mono-O-glucosylation or mono-O-GlcNAcylation (Nagahama, M., Ohkubo, A., Oda, M., Kobayashi, K., Amimoto, K., Miyamoto, K., and Sakurai, J. (2011) Infect.
22665487	3	69	dep	mono-O-glucosylation	498:517	arg1	Infect					644:649	Infect	644:649	Infect	644:649	It was shown that the glucosyltransferase domain of TpeL modifies Ras in vitro by mono-O-glucosylation or mono-O-GlcNAcylation (Nagahama, M., Ohkubo, A., Oda, M., Kobayashi, K., Amimoto, K., Miyamoto, K., and Sakurai, J. (2011) Infect.
22665487	3	69	dep	mono-O-glucosylation	498:517	arg1	J					634:634	J	634:634	J	634:634	It was shown that the glucosyltransferase domain of TpeL modifies Ras in vitro by mono-O-glucosylation or mono-O-GlcNAcylation (Nagahama, M., Ohkubo, A., Oda, M., Kobayashi, K., Amimoto, K., Miyamoto, K., and Sakurai, J. (2011) Infect.
22665487	2	70	theme	polypeptide	331:341	arg1	domain					350:355	a C-terminal polypeptide repeat domain	318:355	a C-terminal polypeptide repeat domain	318:355	In contrast to other members of this toxin family, it lacks a C-terminal polypeptide repeat domain, which is suggested to be involved in target cell binding.
22665487	9	71	theme	located	1193:1199	arg1	domain					1185:1190	an intrinsic cysteine protease domain	1154:1190	an intrinsic cysteine protease domain	1154:1190	The toxin is autoproteolytically processed in the presence of inositol hexakisphosphate (InsP(6)) by an intrinsic cysteine protease domain, located next to the glucosyltransferase domain.
22665487	9	72	theme	glucosyltransferase	1213:1231	arg1	domain					1233:1238	the glucosyltransferase domain	1209:1238	the glucosyltransferase domain	1209:1238	The toxin is autoproteolytically processed in the presence of inositol hexakisphosphate (InsP(6)) by an intrinsic cysteine protease domain, located next to the glucosyltransferase domain.
22665487	8	73	theme	higher	999:1004	arg1	concentrations					1012:1025	1-2 magnitudes higher toxin concentrations	984:1025	1-2 magnitudes higher toxin concentrations	984:1025	In contrast to previous studies, we show that Rac is a poor substrate in vitro and in vivo and requires 1-2 magnitudes higher toxin concentrations for modification by TpeL.
22665487	2	74	theme	C-terminal	320:329	arg1	domain					350:355	a C-terminal polypeptide repeat domain	318:355	a C-terminal polypeptide repeat domain	318:355	In contrast to other members of this toxin family, it lacks a C-terminal polypeptide repeat domain, which is suggested to be involved in target cell binding.
22665487	3	75	from	Ras	482:484	arg1	mono-O-GlcNAcylation					522:541	mono-O-GlcNAcylation	522:541	mono-O-GlcNAcylation	522:541	It was shown that the glucosyltransferase domain of TpeL modifies Ras in vitro by mono-O-glucosylation or mono-O-GlcNAcylation (Nagahama, M., Ohkubo, A., Oda, M., Kobayashi, K., Amimoto, K., Miyamoto, K., and Sakurai, J. (2011) Infect.
22665487	3	75	from	Ras	482:484	arg1	mono-O-glucosylation					498:517	mono-O-glucosylation	498:517	mono-O-glucosylation	498:517	It was shown that the glucosyltransferase domain of TpeL modifies Ras in vitro by mono-O-glucosylation or mono-O-GlcNAcylation (Nagahama, M., Ohkubo, A., Oda, M., Kobayashi, K., Amimoto, K., Miyamoto, K., and Sakurai, J. (2011) Infect.
22665487	1	76	theme	B	240:240	arg1	strains					249:255	Clostridium perfringens type A, B, and C strains	208:255	Clostridium perfringens type A, B, and C strains	208:255	TpeL is a member of the family of clostridial glucosylating toxins produced by Clostridium perfringens type A, B, and C strains.
8639509	9	0	theme	small	1657:1661	arg1	protein					1674:1680	this small heat shock protein	1652:1680	this small heat shock protein	1652:1680	Metabolic pulse-chase labeling studies of U373-MG astroglioma cells indicated that turnover of the carbohydrate on alphaB-crystallin is not static but proceeds many-fold more rapidly than turnover of the protein backbone itself, consistent with a regulatory role for O-GlcNAc on this small heat shock protein.
8639509	9	1	theme	labeling	1395:1402	arg1	studies					1404:1410	Metabolic pulse-chase labeling studies	1373:1410	Metabolic pulse-chase labeling studies of U373-MG astroglioma cells	1373:1439	Metabolic pulse-chase labeling studies of U373-MG astroglioma cells indicated that turnover of the carbohydrate on alphaB-crystallin is not static but proceeds many-fold more rapidly than turnover of the protein backbone itself, consistent with a regulatory role for O-GlcNAc on this small heat shock protein.
8639509	2	2	theme	homologous	315:324	arg1	proteins					326:333	homologous proteins	315:333	homologous proteins	315:333	This highly conserved 20 kDa protein aggregates with homologous proteins, including alphaA-crystallin and the small heat shock protein HSP28, to form large heteromeric complexes.
8639509	2	2	theme	homologous	315:324	arg1	alphaA-crystallin					346:362	alphaA-crystallin	346:362	alphaA-crystallin	346:362	This highly conserved 20 kDa protein aggregates with homologous proteins, including alphaA-crystallin and the small heat shock protein HSP28, to form large heteromeric complexes.
8639509	2	2	theme	homologous	315:324	arg1	protein					389:395	the small heat shock protein HSP28	368:401	the small heat shock protein HSP28	368:401	This highly conserved 20 kDa protein aggregates with homologous proteins, including alphaA-crystallin and the small heat shock protein HSP28, to form large heteromeric complexes.
8639509	6	3	theme	Two-dimensional	970:984	arg1	electrophoresis					986:1000	Two-dimensional electrophoresis	970:1000	Two-dimensional electrophoresis of rat heart alphaB-crystallin	970:1031	Two-dimensional electrophoresis of rat heart alphaB-crystallin revealed two O-GlcNAcylated forms with mobilities corresponding to the unphosphorylated form (alphaB2) and an unidentified, slightly more acidic form.
8639509	3	4	theme	nuclear	671:677	arg1	proteins					695:702	nuclear and cytoplasmic proteins	671:702	nuclear and cytoplasmic proteins	671:702	Recently, Roquemore et al. (1992) have established that both phosphorylated and unphosphorylated forms of lens alphaB-crystallin are modified with O-linked N-acetylglucosamine, a dynamic posttranslational modification abundant on nuclear and cytoplasmic proteins.
8639509	9	5	theme	heat	1663:1666	arg1	protein					1674:1680	this small heat shock protein	1652:1680	this small heat shock protein	1652:1680	Metabolic pulse-chase labeling studies of U373-MG astroglioma cells indicated that turnover of the carbohydrate on alphaB-crystallin is not static but proceeds many-fold more rapidly than turnover of the protein backbone itself, consistent with a regulatory role for O-GlcNAc on this small heat shock protein.
8639509	5	6	theme	lens	866:869	arg1	alphaB-crystallin					871:887	lens alphaB-crystallin	866:887	lens alphaB-crystallin	866:887	We have further shown that this modification is not restricted to lens alphaB-crystallin but occurs on alphaB isolated from rat heart tissue and human astroglioma cells.
8639509	2	7	theme	kDa	287:289	arg1	protein					291:297	This highly conserved 20 kDa protein	262:297	This highly conserved 20 kDa protein	262:297	This highly conserved 20 kDa protein aggregates with homologous proteins, including alphaA-crystallin and the small heat shock protein HSP28, to form large heteromeric complexes.
8639509	4	8	theme	O-GlcNAcylation	757:771	arg1	O-GlcNAcylation					757:771	O-GlcNAcylation	757:771	O-GlcNAcylation	757:771	In this paper, we have identified the major site of O-GlcNAcylation on lens alphaB as Thr 170.
8639509	4	8	theme	O-GlcNAcylation	757:771	arg1	site					749:752	the major site	739:752	the major site of O-GlcNAcylation on lens alphaB	739:786	In this paper, we have identified the major site of O-GlcNAcylation on lens alphaB as Thr 170.
8639509	9	9	theme	shock	1668:1672	arg1	protein					1674:1680	this small heat shock protein	1652:1680	this small heat shock protein	1652:1680	Metabolic pulse-chase labeling studies of U373-MG astroglioma cells indicated that turnover of the carbohydrate on alphaB-crystallin is not static but proceeds many-fold more rapidly than turnover of the protein backbone itself, consistent with a regulatory role for O-GlcNAc on this small heat shock protein.
8639509	4	10	from	site	749:752	arg1	alphaB					781:786	lens alphaB	776:786	lens alphaB	776:786	In this paper, we have identified the major site of O-GlcNAcylation on lens alphaB as Thr 170.
8639509	3	11	mod	modified	574:581	arg3	N-acetylglucosamine					597:615	O-linked N-acetylglucosamine	588:615	O-linked N-acetylglucosamine	588:615	Recently, Roquemore et al. (1992) have established that both phosphorylated and unphosphorylated forms of lens alphaB-crystallin are modified with O-linked N-acetylglucosamine, a dynamic posttranslational modification abundant on nuclear and cytoplasmic proteins.
8639509	3	11	mod	modified	574:581	arg1	forms					538:542	both phosphorylated and unphosphorylated forms	497:542	both phosphorylated and unphosphorylated forms of lens alphaB-crystallin	497:568	Recently, Roquemore et al. (1992) have established that both phosphorylated and unphosphorylated forms of lens alphaB-crystallin are modified with O-linked N-acetylglucosamine, a dynamic posttranslational modification abundant on nuclear and cytoplasmic proteins.
8639509	3	11	mod	modified	574:581	arg3	modification					646:657	a dynamic posttranslational modification	618:657	a dynamic posttranslational modification abundant on nuclear and cytoplasmic proteins	618:702	Recently, Roquemore et al. (1992) have established that both phosphorylated and unphosphorylated forms of lens alphaB-crystallin are modified with O-linked N-acetylglucosamine, a dynamic posttranslational modification abundant on nuclear and cytoplasmic proteins.
8639509	5	12	theme	rat	924:926	arg1	tissue					934:939	rat heart tissue	924:939	rat heart tissue	924:939	We have further shown that this modification is not restricted to lens alphaB-crystallin but occurs on alphaB isolated from rat heart tissue and human astroglioma cells.
8639509	9	13	theme	cells	1435:1439	arg1	studies					1404:1410	Metabolic pulse-chase labeling studies	1373:1410	Metabolic pulse-chase labeling studies of U373-MG astroglioma cells	1373:1439	Metabolic pulse-chase labeling studies of U373-MG astroglioma cells indicated that turnover of the carbohydrate on alphaB-crystallin is not static but proceeds many-fold more rapidly than turnover of the protein backbone itself, consistent with a regulatory role for O-GlcNAc on this small heat shock protein.
8639509	9	14	theme	backbone	1585:1592	arg1	turnover					1561:1568	turnover	1561:1568	turnover of the protein backbone itself	1561:1599	Metabolic pulse-chase labeling studies of U373-MG astroglioma cells indicated that turnover of the carbohydrate on alphaB-crystallin is not static but proceeds many-fold more rapidly than turnover of the protein backbone itself, consistent with a regulatory role for O-GlcNAc on this small heat shock protein.
8639509	8	15	from	site	1300:1303	arg1	alphaB-crystallins					1308:1325	alphaB-crystallins	1308:1325	alphaB-crystallins from rat heart	1308:1340	The major O-GlcNAcylation site on alphaB-crystallins from rat heart also appears to be at Thr 170.
8639509	9	16	theme	carbohydrate	1472:1483	arg1	turnover					1456:1463	turnover	1456:1463	turnover of the carbohydrate on alphaB-crystallin	1456:1504	Metabolic pulse-chase labeling studies of U373-MG astroglioma cells indicated that turnover of the carbohydrate on alphaB-crystallin is not static but proceeds many-fold more rapidly than turnover of the protein backbone itself, consistent with a regulatory role for O-GlcNAc on this small heat shock protein.
8639509	7	17	theme	Phosphorylated	1184:1197	arg1	alphaB1					1218:1224	alphaB1	1218:1224	alphaB1	1218:1224	Phosphorylated alphaB-crystallin (alphaB1) was not detected in the rat heart preparation.
8639509	7	17	theme	Phosphorylated	1184:1197	arg1	alphaB-crystallin					1199:1215	Phosphorylated alphaB-crystallin	1184:1215	Phosphorylated alphaB-crystallin (alphaB1)	1184:1225	Phosphorylated alphaB-crystallin (alphaB1) was not detected in the rat heart preparation.
8639509	8	18	theme	O-GlcNAcylation	1284:1298	arg1	site					1300:1303	The major O-GlcNAcylation site	1274:1303	The major O-GlcNAcylation site on alphaB-crystallins from rat heart	1274:1340	The major O-GlcNAcylation site on alphaB-crystallins from rat heart also appears to be at Thr 170.
8639509	3	19	dep	Roquemore	451:459	arg1	al					464:465	Roquemore et al	451:465	Roquemore et al. (1992)	451:473	Recently, Roquemore et al. (1992) have established that both phosphorylated and unphosphorylated forms of lens alphaB-crystallin are modified with O-linked N-acetylglucosamine, a dynamic posttranslational modification abundant on nuclear and cytoplasmic proteins.
8639509	6	20	dep	unidentified	1143:1154	arg1	acidic					1171:1176	acidic	1171:1176	acidic	1171:1176	Two-dimensional electrophoresis of rat heart alphaB-crystallin revealed two O-GlcNAcylated forms with mobilities corresponding to the unphosphorylated form (alphaB2) and an unidentified, slightly more acidic form.
8639509	0	21	theme	shock	42:46	arg1	B-crystallin					62:73	the small heat shock protein alpha B-crystallin	27:73	the small heat shock protein alpha B-crystallin	27:73	Dynamic O-GlcNAcylation of the small heat shock protein alpha B-crystallin.
8639509	8	22	theme	rat	1332:1334	arg1	heart					1336:1340	rat heart	1332:1340	rat heart	1332:1340	The major O-GlcNAcylation site on alphaB-crystallins from rat heart also appears to be at Thr 170.
8639509	9	23	theme	U373-MG	1415:1421	arg1	cells					1435:1439	U373-MG astroglioma cells	1415:1439	U373-MG astroglioma cells	1415:1439	Metabolic pulse-chase labeling studies of U373-MG astroglioma cells indicated that turnover of the carbohydrate on alphaB-crystallin is not static but proceeds many-fold more rapidly than turnover of the protein backbone itself, consistent with a regulatory role for O-GlcNAc on this small heat shock protein.
8639509	5	24	theme	human	945:949	arg1	cells					963:967	human astroglioma cells	945:967	human astroglioma cells	945:967	We have further shown that this modification is not restricted to lens alphaB-crystallin but occurs on alphaB isolated from rat heart tissue and human astroglioma cells.
8639509	8	25	from	heart	1336:1340	arg1	alphaB-crystallins					1308:1325	alphaB-crystallins	1308:1325	alphaB-crystallins from rat heart	1308:1340	The major O-GlcNAcylation site on alphaB-crystallins from rat heart also appears to be at Thr 170.
8639509	2	26	theme	conserved	274:282	arg1	protein					291:297	This highly conserved 20 kDa protein	262:297	This highly conserved 20 kDa protein	262:297	This highly conserved 20 kDa protein aggregates with homologous proteins, including alphaA-crystallin and the small heat shock protein HSP28, to form large heteromeric complexes.
8639509	0	27	theme	Dynamic	0:6	arg1	O-GlcNAcylation					8:22	Dynamic O-GlcNAcylation	0:22	Dynamic O-GlcNAcylation of the small heat shock protein alpha B-crystallin.	0:74	Dynamic O-GlcNAcylation of the small heat shock protein alpha B-crystallin.
8639509	3	28	theme	unphosphorylated	521:536	arg1	forms					538:542	both phosphorylated and unphosphorylated forms	497:542	both phosphorylated and unphosphorylated forms of lens alphaB-crystallin	497:568	Recently, Roquemore et al. (1992) have established that both phosphorylated and unphosphorylated forms of lens alphaB-crystallin are modified with O-linked N-acetylglucosamine, a dynamic posttranslational modification abundant on nuclear and cytoplasmic proteins.
8639509	4	29	theme	major	743:747	arg1	O-GlcNAcylation					757:771	O-GlcNAcylation	757:771	O-GlcNAcylation	757:771	In this paper, we have identified the major site of O-GlcNAcylation on lens alphaB as Thr 170.
8639509	4	29	theme	major	743:747	arg1	site					749:752	the major site	739:752	the major site of O-GlcNAcylation on lens alphaB	739:786	In this paper, we have identified the major site of O-GlcNAcylation on lens alphaB as Thr 170.
8639509	3	30	theme	dynamic	620:626	arg1	modification					646:657	a dynamic posttranslational modification	618:657	a dynamic posttranslational modification abundant on nuclear and cytoplasmic proteins	618:702	Recently, Roquemore et al. (1992) have established that both phosphorylated and unphosphorylated forms of lens alphaB-crystallin are modified with O-linked N-acetylglucosamine, a dynamic posttranslational modification abundant on nuclear and cytoplasmic proteins.
8639509	3	30	theme	dynamic	620:626	arg1	N-acetylglucosamine					597:615	O-linked N-acetylglucosamine	588:615	O-linked N-acetylglucosamine	588:615	Recently, Roquemore et al. (1992) have established that both phosphorylated and unphosphorylated forms of lens alphaB-crystallin are modified with O-linked N-acetylglucosamine, a dynamic posttranslational modification abundant on nuclear and cytoplasmic proteins.
8639509	6	31	theme	unidentified	1143:1154	arg1	form					1178:1181	an unidentified, slightly more acidic form	1140:1181	an unidentified, slightly more acidic form	1140:1181	Two-dimensional electrophoresis of rat heart alphaB-crystallin revealed two O-GlcNAcylated forms with mobilities corresponding to the unphosphorylated form (alphaB2) and an unidentified, slightly more acidic form.
8639509	9	32	theme	Metabolic	1373:1381	arg1	studies					1404:1410	Metabolic pulse-chase labeling studies	1373:1410	Metabolic pulse-chase labeling studies of U373-MG astroglioma cells	1373:1439	Metabolic pulse-chase labeling studies of U373-MG astroglioma cells indicated that turnover of the carbohydrate on alphaB-crystallin is not static but proceeds many-fold more rapidly than turnover of the protein backbone itself, consistent with a regulatory role for O-GlcNAc on this small heat shock protein.
8639509	5	33	theme	heart	928:932	arg1	tissue					934:939	rat heart tissue	924:939	rat heart tissue	924:939	We have further shown that this modification is not restricted to lens alphaB-crystallin but occurs on alphaB isolated from rat heart tissue and human astroglioma cells.
8639509	3	34	link	O-linked	588:595	arg1	modification					646:657	a dynamic posttranslational modification	618:657	a dynamic posttranslational modification abundant on nuclear and cytoplasmic proteins	618:702	Recently, Roquemore et al. (1992) have established that both phosphorylated and unphosphorylated forms of lens alphaB-crystallin are modified with O-linked N-acetylglucosamine, a dynamic posttranslational modification abundant on nuclear and cytoplasmic proteins.
8639509	3	34	link	O-linked	588:595	arg1	N-acetylglucosamine					597:615	O-linked N-acetylglucosamine	588:615	O-linked N-acetylglucosamine	588:615	Recently, Roquemore et al. (1992) have established that both phosphorylated and unphosphorylated forms of lens alphaB-crystallin are modified with O-linked N-acetylglucosamine, a dynamic posttranslational modification abundant on nuclear and cytoplasmic proteins.
8639509	1	35	theme	nonlens	245:251	arg1	tissues					253:259	nonlens tissues	245:259	nonlens tissues	245:259	alphaB-Crystallin, originally described as a structural lens protein, is now known to be a member of the small heat shock protein family and is expressed in a number of nonlens tissues.
8639509	3	36	theme	phosphorylated	502:515	arg1	forms					538:542	both phosphorylated and unphosphorylated forms	497:542	both phosphorylated and unphosphorylated forms of lens alphaB-crystallin	497:568	Recently, Roquemore et al. (1992) have established that both phosphorylated and unphosphorylated forms of lens alphaB-crystallin are modified with O-linked N-acetylglucosamine, a dynamic posttranslational modification abundant on nuclear and cytoplasmic proteins.
8639509	2	37	theme	heteromeric	418:428	arg1	complexes					430:438	large heteromeric complexes	412:438	large heteromeric complexes	412:438	This highly conserved 20 kDa protein aggregates with homologous proteins, including alphaA-crystallin and the small heat shock protein HSP28, to form large heteromeric complexes.
8639509	2	38	theme	shock	383:387	arg1	protein					389:395	the small heat shock protein HSP28	368:401	the small heat shock protein HSP28	368:401	This highly conserved 20 kDa protein aggregates with homologous proteins, including alphaA-crystallin and the small heat shock protein HSP28, to form large heteromeric complexes.
8639509	0	39	theme	heat	37:40	arg1	B-crystallin					62:73	the small heat shock protein alpha B-crystallin	27:73	the small heat shock protein alpha B-crystallin	27:73	Dynamic O-GlcNAcylation of the small heat shock protein alpha B-crystallin.
8639509	1	40	theme	tissues	253:259	arg1	number					235:240	a number	233:240	a number of nonlens tissues	233:259	alphaB-Crystallin, originally described as a structural lens protein, is now known to be a member of the small heat shock protein family and is expressed in a number of nonlens tissues.
8639509	1	41	theme	small	181:185	arg1	family					206:211	the small heat shock protein family	177:211	the small heat shock protein family	177:211	alphaB-Crystallin, originally described as a structural lens protein, is now known to be a member of the small heat shock protein family and is expressed in a number of nonlens tissues.
8639509	3	42	theme	lens	547:550	arg1	alphaB-crystallin					552:568	lens alphaB-crystallin	547:568	lens alphaB-crystallin	547:568	Recently, Roquemore et al. (1992) have established that both phosphorylated and unphosphorylated forms of lens alphaB-crystallin are modified with O-linked N-acetylglucosamine, a dynamic posttranslational modification abundant on nuclear and cytoplasmic proteins.
8639509	2	43	theme	heat	378:381	arg1	protein					389:395	the small heat shock protein HSP28	368:401	the small heat shock protein HSP28	368:401	This highly conserved 20 kDa protein aggregates with homologous proteins, including alphaA-crystallin and the small heat shock protein HSP28, to form large heteromeric complexes.
8639509	0	44	theme	small	31:35	arg1	B-crystallin					62:73	the small heat shock protein alpha B-crystallin	27:73	the small heat shock protein alpha B-crystallin	27:73	Dynamic O-GlcNAcylation of the small heat shock protein alpha B-crystallin.
8639509	5	45	attach	isolated	910:917	arg2	alphaB					903:908	alphaB	903:908	alphaB isolated from rat heart tissue and human astroglioma cells	903:967	We have further shown that this modification is not restricted to lens alphaB-crystallin but occurs on alphaB isolated from rat heart tissue and human astroglioma cells.
8639509	5	45	attach	isolated	910:917	arg1	cells					963:967	human astroglioma cells	945:967	human astroglioma cells	945:967	We have further shown that this modification is not restricted to lens alphaB-crystallin but occurs on alphaB isolated from rat heart tissue and human astroglioma cells.
8639509	5	45	attach	isolated	910:917	arg1	tissue					934:939	rat heart tissue	924:939	rat heart tissue	924:939	We have further shown that this modification is not restricted to lens alphaB-crystallin but occurs on alphaB isolated from rat heart tissue and human astroglioma cells.
8639509	9	46	theme	astroglioma	1423:1433	arg1	cells					1435:1439	U373-MG astroglioma cells	1415:1439	U373-MG astroglioma cells	1415:1439	Metabolic pulse-chase labeling studies of U373-MG astroglioma cells indicated that turnover of the carbohydrate on alphaB-crystallin is not static but proceeds many-fold more rapidly than turnover of the protein backbone itself, consistent with a regulatory role for O-GlcNAc on this small heat shock protein.
8639509	8	47	theme	major	1278:1282	arg1	site					1300:1303	The major O-GlcNAcylation site	1274:1303	The major O-GlcNAcylation site on alphaB-crystallins from rat heart	1274:1340	The major O-GlcNAcylation site on alphaB-crystallins from rat heart also appears to be at Thr 170.
8639509	3	48	theme	alphaB-crystallin	552:568	arg1	forms					538:542	both phosphorylated and unphosphorylated forms	497:542	both phosphorylated and unphosphorylated forms of lens alphaB-crystallin	497:568	Recently, Roquemore et al. (1992) have established that both phosphorylated and unphosphorylated forms of lens alphaB-crystallin are modified with O-linked N-acetylglucosamine, a dynamic posttranslational modification abundant on nuclear and cytoplasmic proteins.
8639509	6	49	with	forms	1061:1065	arg1	mobilities					1072:1081	mobilities	1072:1081	mobilities corresponding to the unphosphorylated form (alphaB2) and an unidentified, slightly more acidic form	1072:1181	Two-dimensional electrophoresis of rat heart alphaB-crystallin revealed two O-GlcNAcylated forms with mobilities corresponding to the unphosphorylated form (alphaB2) and an unidentified, slightly more acidic form.
8639509	1	50	theme	heat	187:190	arg1	family					206:211	the small heat shock protein family	177:211	the small heat shock protein family	177:211	alphaB-Crystallin, originally described as a structural lens protein, is now known to be a member of the small heat shock protein family and is expressed in a number of nonlens tissues.
8639509	0	51	theme	protein	48:54	arg1	B-crystallin					62:73	the small heat shock protein alpha B-crystallin	27:73	the small heat shock protein alpha B-crystallin	27:73	Dynamic O-GlcNAcylation of the small heat shock protein alpha B-crystallin.
8639509	9	52	with	consistent	1602:1611	arg1	role					1631:1634	a regulatory role	1618:1634	a regulatory role for O-GlcNAc on this small heat shock protein	1618:1680	Metabolic pulse-chase labeling studies of U373-MG astroglioma cells indicated that turnover of the carbohydrate on alphaB-crystallin is not static but proceeds many-fold more rapidly than turnover of the protein backbone itself, consistent with a regulatory role for O-GlcNAc on this small heat shock protein.
8639509	6	53	theme	alphaB-crystallin	1015:1031	arg1	electrophoresis					986:1000	Two-dimensional electrophoresis	970:1000	Two-dimensional electrophoresis of rat heart alphaB-crystallin	970:1031	Two-dimensional electrophoresis of rat heart alphaB-crystallin revealed two O-GlcNAcylated forms with mobilities corresponding to the unphosphorylated form (alphaB2) and an unidentified, slightly more acidic form.
8639509	9	54	theme	regulatory	1620:1629	arg1	role					1631:1634	a regulatory role	1618:1634	a regulatory role for O-GlcNAc on this small heat shock protein	1618:1680	Metabolic pulse-chase labeling studies of U373-MG astroglioma cells indicated that turnover of the carbohydrate on alphaB-crystallin is not static but proceeds many-fold more rapidly than turnover of the protein backbone itself, consistent with a regulatory role for O-GlcNAc on this small heat shock protein.
8639509	9	55	from	role	1631:1634	arg1	protein					1674:1680	this small heat shock protein	1652:1680	this small heat shock protein	1652:1680	Metabolic pulse-chase labeling studies of U373-MG astroglioma cells indicated that turnover of the carbohydrate on alphaB-crystallin is not static but proceeds many-fold more rapidly than turnover of the protein backbone itself, consistent with a regulatory role for O-GlcNAc on this small heat shock protein.
8639509	2	56	theme	large	412:416	arg1	complexes					430:438	large heteromeric complexes	412:438	large heteromeric complexes	412:438	This highly conserved 20 kDa protein aggregates with homologous proteins, including alphaA-crystallin and the small heat shock protein HSP28, to form large heteromeric complexes.
8639509	3	57	theme	abundant	659:666	arg1	modification					646:657	a dynamic posttranslational modification	618:657	a dynamic posttranslational modification abundant on nuclear and cytoplasmic proteins	618:702	Recently, Roquemore et al. (1992) have established that both phosphorylated and unphosphorylated forms of lens alphaB-crystallin are modified with O-linked N-acetylglucosamine, a dynamic posttranslational modification abundant on nuclear and cytoplasmic proteins.
8639509	3	57	theme	abundant	659:666	arg1	N-acetylglucosamine					597:615	O-linked N-acetylglucosamine	588:615	O-linked N-acetylglucosamine	588:615	Recently, Roquemore et al. (1992) have established that both phosphorylated and unphosphorylated forms of lens alphaB-crystallin are modified with O-linked N-acetylglucosamine, a dynamic posttranslational modification abundant on nuclear and cytoplasmic proteins.
8639509	9	58	from	turnover	1456:1463	arg1	alphaB-crystallin					1488:1504	alphaB-crystallin	1488:1504	alphaB-crystallin	1488:1504	Metabolic pulse-chase labeling studies of U373-MG astroglioma cells indicated that turnover of the carbohydrate on alphaB-crystallin is not static but proceeds many-fold more rapidly than turnover of the protein backbone itself, consistent with a regulatory role for O-GlcNAc on this small heat shock protein.
8639509	1	59	theme	structural	121:130	arg1	protein					137:143	a structural lens protein	119:143	a structural lens protein	119:143	alphaB-Crystallin, originally described as a structural lens protein, is now known to be a member of the small heat shock protein family and is expressed in a number of nonlens tissues.
8639509	7	60	theme	heart	1255:1259	arg1	preparation					1261:1271	the rat heart preparation	1247:1271	the rat heart preparation	1247:1271	Phosphorylated alphaB-crystallin (alphaB1) was not detected in the rat heart preparation.
8639509	5	61	theme	astroglioma	951:961	arg1	cells					963:967	human astroglioma cells	945:967	human astroglioma cells	945:967	We have further shown that this modification is not restricted to lens alphaB-crystallin but occurs on alphaB isolated from rat heart tissue and human astroglioma cells.
8639509	6	62	theme	rat	1005:1007	arg1	alphaB-crystallin					1015:1031	rat heart alphaB-crystallin	1005:1031	rat heart alphaB-crystallin	1005:1031	Two-dimensional electrophoresis of rat heart alphaB-crystallin revealed two O-GlcNAcylated forms with mobilities corresponding to the unphosphorylated form (alphaB2) and an unidentified, slightly more acidic form.
8639509	1	63	theme	lens	132:135	arg1	protein					137:143	a structural lens protein	119:143	a structural lens protein	119:143	alphaB-Crystallin, originally described as a structural lens protein, is now known to be a member of the small heat shock protein family and is expressed in a number of nonlens tissues.
8639509	9	64	theme	pulse-chase	1383:1393	arg1	studies					1404:1410	Metabolic pulse-chase labeling studies	1373:1410	Metabolic pulse-chase labeling studies of U373-MG astroglioma cells	1373:1439	Metabolic pulse-chase labeling studies of U373-MG astroglioma cells indicated that turnover of the carbohydrate on alphaB-crystallin is not static but proceeds many-fold more rapidly than turnover of the protein backbone itself, consistent with a regulatory role for O-GlcNAc on this small heat shock protein.
8639509	1	65	theme	shock	192:196	arg1	family					206:211	the small heat shock protein family	177:211	the small heat shock protein family	177:211	alphaB-Crystallin, originally described as a structural lens protein, is now known to be a member of the small heat shock protein family and is expressed in a number of nonlens tissues.
8639509	9	66	theme	protein	1577:1583	arg1	backbone					1585:1592	the protein backbone itself	1573:1599	the protein backbone itself	1573:1599	Metabolic pulse-chase labeling studies of U373-MG astroglioma cells indicated that turnover of the carbohydrate on alphaB-crystallin is not static but proceeds many-fold more rapidly than turnover of the protein backbone itself, consistent with a regulatory role for O-GlcNAc on this small heat shock protein.
8639509	3	67	theme	posttranslational	628:644	arg1	modification					646:657	a dynamic posttranslational modification	618:657	a dynamic posttranslational modification abundant on nuclear and cytoplasmic proteins	618:702	Recently, Roquemore et al. (1992) have established that both phosphorylated and unphosphorylated forms of lens alphaB-crystallin are modified with O-linked N-acetylglucosamine, a dynamic posttranslational modification abundant on nuclear and cytoplasmic proteins.
8639509	3	67	theme	posttranslational	628:644	arg1	N-acetylglucosamine					597:615	O-linked N-acetylglucosamine	588:615	O-linked N-acetylglucosamine	588:615	Recently, Roquemore et al. (1992) have established that both phosphorylated and unphosphorylated forms of lens alphaB-crystallin are modified with O-linked N-acetylglucosamine, a dynamic posttranslational modification abundant on nuclear and cytoplasmic proteins.
8639509	3	68	theme	O-linked	588:595	arg1	modification					646:657	a dynamic posttranslational modification	618:657	a dynamic posttranslational modification abundant on nuclear and cytoplasmic proteins	618:702	Recently, Roquemore et al. (1992) have established that both phosphorylated and unphosphorylated forms of lens alphaB-crystallin are modified with O-linked N-acetylglucosamine, a dynamic posttranslational modification abundant on nuclear and cytoplasmic proteins.
8639509	3	68	theme	O-linked	588:595	arg1	N-acetylglucosamine					597:615	O-linked N-acetylglucosamine	588:615	O-linked N-acetylglucosamine	588:615	Recently, Roquemore et al. (1992) have established that both phosphorylated and unphosphorylated forms of lens alphaB-crystallin are modified with O-linked N-acetylglucosamine, a dynamic posttranslational modification abundant on nuclear and cytoplasmic proteins.
8639509	7	69	located	detected	1235:1242	arg2	alphaB1					1218:1224	alphaB1	1218:1224	alphaB1	1218:1224	Phosphorylated alphaB-crystallin (alphaB1) was not detected in the rat heart preparation.
8639509	7	69	located	detected	1235:1242	arg2	alphaB-crystallin					1199:1215	Phosphorylated alphaB-crystallin	1184:1215	Phosphorylated alphaB-crystallin (alphaB1)	1184:1225	Phosphorylated alphaB-crystallin (alphaB1) was not detected in the rat heart preparation.
8639509	7	69	located	detected	1235:1242	arg1	preparation					1261:1271	the rat heart preparation	1247:1271	the rat heart preparation	1247:1271	Phosphorylated alphaB-crystallin (alphaB1) was not detected in the rat heart preparation.
8639509	6	70	theme	unphosphorylated	1104:1119	arg1	alphaB2					1127:1133	alphaB2	1127:1133	alphaB2	1127:1133	Two-dimensional electrophoresis of rat heart alphaB-crystallin revealed two O-GlcNAcylated forms with mobilities corresponding to the unphosphorylated form (alphaB2) and an unidentified, slightly more acidic form.
8639509	6	70	theme	unphosphorylated	1104:1119	arg1	form					1121:1124	the unphosphorylated form	1100:1124	the unphosphorylated form (alphaB2)	1100:1134	Two-dimensional electrophoresis of rat heart alphaB-crystallin revealed two O-GlcNAcylated forms with mobilities corresponding to the unphosphorylated form (alphaB2) and an unidentified, slightly more acidic form.
8639509	1	71	theme	protein	198:204	arg1	family					206:211	the small heat shock protein family	177:211	the small heat shock protein family	177:211	alphaB-Crystallin, originally described as a structural lens protein, is now known to be a member of the small heat shock protein family and is expressed in a number of nonlens tissues.
8639509	0	72	theme	B-crystallin	62:73	arg1	O-GlcNAcylation					8:22	Dynamic O-GlcNAcylation	0:22	Dynamic O-GlcNAcylation of the small heat shock protein alpha B-crystallin.	0:74	Dynamic O-GlcNAcylation of the small heat shock protein alpha B-crystallin.
8639509	2	73	theme	small	372:376	arg1	protein					389:395	the small heat shock protein HSP28	368:401	the small heat shock protein HSP28	368:401	This highly conserved 20 kDa protein aggregates with homologous proteins, including alphaA-crystallin and the small heat shock protein HSP28, to form large heteromeric complexes.
8639509	6	74	theme	O-GlcNAcylated	1046:1059	arg1	forms					1061:1065	two O-GlcNAcylated forms	1042:1065	two O-GlcNAcylated forms with mobilities corresponding to the unphosphorylated form (alphaB2) and an unidentified, slightly more acidic form	1042:1181	Two-dimensional electrophoresis of rat heart alphaB-crystallin revealed two O-GlcNAcylated forms with mobilities corresponding to the unphosphorylated form (alphaB2) and an unidentified, slightly more acidic form.
8639509	7	75	theme	rat	1251:1253	arg1	preparation					1261:1271	the rat heart preparation	1247:1271	the rat heart preparation	1247:1271	Phosphorylated alphaB-crystallin (alphaB1) was not detected in the rat heart preparation.
8639509	1	76	theme	family	206:211	arg1	member					167:172	a member	165:172	a member of the small heat shock protein family	165:211	alphaB-Crystallin, originally described as a structural lens protein, is now known to be a member of the small heat shock protein family and is expressed in a number of nonlens tissues.
8639509	1	76	theme	family	206:211	arg1	alphaB-Crystallin					76:92	alphaB-Crystallin	76:92	alphaB-Crystallin	76:92	alphaB-Crystallin, originally described as a structural lens protein, is now known to be a member of the small heat shock protein family and is expressed in a number of nonlens tissues.
8639509	0	77	theme	alpha	56:60	arg1	B-crystallin					62:73	the small heat shock protein alpha B-crystallin	27:73	the small heat shock protein alpha B-crystallin	27:73	Dynamic O-GlcNAcylation of the small heat shock protein alpha B-crystallin.
8639509	3	78	theme	cytoplasmic	683:693	arg1	proteins					695:702	nuclear and cytoplasmic proteins	671:702	nuclear and cytoplasmic proteins	671:702	Recently, Roquemore et al. (1992) have established that both phosphorylated and unphosphorylated forms of lens alphaB-crystallin are modified with O-linked N-acetylglucosamine, a dynamic posttranslational modification abundant on nuclear and cytoplasmic proteins.
8639509	4	79	theme	lens	776:779	arg1	alphaB					781:786	lens alphaB	776:786	lens alphaB	776:786	In this paper, we have identified the major site of O-GlcNAcylation on lens alphaB as Thr 170.
8639509	6	80	theme	heart	1009:1013	arg1	alphaB-crystallin					1015:1031	rat heart alphaB-crystallin	1005:1031	rat heart alphaB-crystallin	1005:1031	Two-dimensional electrophoresis of rat heart alphaB-crystallin revealed two O-GlcNAcylated forms with mobilities corresponding to the unphosphorylated form (alphaB2) and an unidentified, slightly more acidic form.
20680651	7	0	theme	p107	893:896	arg1	pRB					872:874	pRB	872:874	pRB	872:874	Here we show that pRB, and the related p107 protein, are modified by O-linked β-N-acetylglucosamine (O-GlcNAc) in an in vitro transcription/translation system.
20680651	7	0	theme	p107	893:896	arg1	protein					898:904	and the related p107 protein	877:904	protein	898:904	Here we show that pRB, and the related p107 protein, are modified by O-linked β-N-acetylglucosamine (O-GlcNAc) in an in vitro transcription/translation system.
20680651	5	1	theme	histone	590:596	arg1	deacetylase					598:608	histone deacetylase	590:608	a histone deacetylase complex	588:616	pRB binds E2F-1 and represses transcription via recruitment of a histone deacetylase complex and by preventing co-activator complexes from binding E2F-1.
20680651	3	2	theme	family	353:358	arg1	members					360:366	the related p107 and p130 family members	327:366	the related p107 and p130 family members	327:366	One of the essential mechanisms by which pRB, and the related p107 and p130 family members, act is through its interactions with the E2F class of transcription factors.
20680651	5	3	theme	deacetylase	598:608	arg1	complex					610:616	a histone deacetylase complex	588:616	a histone deacetylase complex	588:616	pRB binds E2F-1 and represses transcription via recruitment of a histone deacetylase complex and by preventing co-activator complexes from binding E2F-1.
20680651	10	4	theme	dynamic	1322:1328	arg1	modification					1339:1350	dynamic O-GlcNAc modification	1322:1350	dynamic O-GlcNAc modification	1322:1350	These studies suggest that regulation of pRB function(s) may be controlled by dynamic O-GlcNAc modification, as well as phosphorylation.
20680651	5	5	theme	complex	610:616	arg1	recruitment					573:583	recruitment	573:583	recruitment of a histone deacetylase complex	573:616	pRB binds E2F-1 and represses transcription via recruitment of a histone deacetylase complex and by preventing co-activator complexes from binding E2F-1.
20680651	3	6	with	interactions	388:399	arg1	class					414:418	the E2F class	406:418	the E2F class of transcription factors	406:443	One of the essential mechanisms by which pRB, and the related p107 and p130 family members, act is through its interactions with the E2F class of transcription factors.
20680651	8	7	gly	glycosylated	1068:1079	arg1	G1					1084:1085	G1	1084:1085	G1 of the cell-cycle	1084:1103	Furthermore, we show in vivo that pRB is more heavily glycosylated in G1 of the cell-cycle when pRB is known to be in an active, hypophosphorylated state.
20680651	8	7	gly	glycosylated	1068:1079	arg2	pRB					1048:1050	pRB	1048:1050	pRB	1048:1050	Furthermore, we show in vivo that pRB is more heavily glycosylated in G1 of the cell-cycle when pRB is known to be in an active, hypophosphorylated state.
20680651	8	7	gly	glycosylated	1068:1079	arg1	pRB					1048:1050	pRB	1048:1050	pRB	1048:1050	Furthermore, we show in vivo that pRB is more heavily glycosylated in G1 of the cell-cycle when pRB is known to be in an active, hypophosphorylated state.
20680651	10	8	theme	O-GlcNAc	1330:1337	arg1	modification					1339:1350	dynamic O-GlcNAc modification	1322:1350	dynamic O-GlcNAc modification	1322:1350	These studies suggest that regulation of pRB function(s) may be controlled by dynamic O-GlcNAc modification, as well as phosphorylation.
20680651	6	9	theme	pRB	726:728	arg1	phosphorylation					707:721	phosphorylation	707:721	phosphorylation of pRB during mid- to late-G1	707:751	Current dogma suggests that phosphorylation of pRB during mid- to late-G1 leads to release of E2F-1 and E2F-1 dependent transcriptional activation of essential S-phase genes.
20680651	3	10	theme	p130	348:351	arg1	members					360:366	the related p107 and p130 family members	327:366	the related p107 and p130 family members	327:366	One of the essential mechanisms by which pRB, and the related p107 and p130 family members, act is through its interactions with the E2F class of transcription factors.
20680651	6	11	theme	transcriptional	799:813	arg1	activation					815:824	E2F-1 dependent transcriptional activation	783:824	E2F-1 dependent transcriptional activation of essential S-phase genes	783:851	Current dogma suggests that phosphorylation of pRB during mid- to late-G1 leads to release of E2F-1 and E2F-1 dependent transcriptional activation of essential S-phase genes.
20680651	3	12	theme	transcription	423:435	arg1	factors					437:443	transcription factors	423:443	transcription factors	423:443	One of the essential mechanisms by which pRB, and the related p107 and p130 family members, act is through its interactions with the E2F class of transcription factors.
20680651	0	13	theme	E2F-1	4:8	arg1	product					56:62	The E2F-1 associated retinoblastoma-susceptibility gene product	0:62	The E2F-1 associated retinoblastoma-susceptibility gene product	0:62	The E2F-1 associated retinoblastoma-susceptibility gene product is modified by O-GlcNAc.
20680651	5	14	theme	co-activator	636:647	arg1	complexes					649:657	co-activator complexes	636:657	co-activator complexes	636:657	pRB binds E2F-1 and represses transcription via recruitment of a histone deacetylase complex and by preventing co-activator complexes from binding E2F-1.
20680651	6	15	theme	dependent	789:797	arg1	activation					815:824	E2F-1 dependent transcriptional activation	783:824	E2F-1 dependent transcriptional activation of essential S-phase genes	783:851	Current dogma suggests that phosphorylation of pRB during mid- to late-G1 leads to release of E2F-1 and E2F-1 dependent transcriptional activation of essential S-phase genes.
20680651	1	16	theme	retinoblastoma-susceptibility	93:121	arg1	suppressor					163:172	a classical tumor suppressor	145:172	a classical tumor suppressor	145:172	The retinoblastoma-susceptibility gene product (pRB) is a classical tumor suppressor.
20680651	1	16	theme	retinoblastoma-susceptibility	93:121	arg1	pRB					137:139	pRB	137:139	pRB	137:139	The retinoblastoma-susceptibility gene product (pRB) is a classical tumor suppressor.
20680651	1	16	theme	retinoblastoma-susceptibility	93:121	arg1	product					128:134	The retinoblastoma-susceptibility gene product	89:134	The retinoblastoma-susceptibility gene product (pRB)	89:140	The retinoblastoma-susceptibility gene product (pRB) is a classical tumor suppressor.
20680651	3	17	theme	E2F	410:412	arg1	class					414:418	the E2F class	406:418	the E2F class of transcription factors	406:443	One of the essential mechanisms by which pRB, and the related p107 and p130 family members, act is through its interactions with the E2F class of transcription factors.
20680651	8	18	theme	hypophosphorylated	1143:1160	arg1	state					1162:1166	an active, hypophosphorylated state	1132:1166	state	1162:1166	Furthermore, we show in vivo that pRB is more heavily glycosylated in G1 of the cell-cycle when pRB is known to be in an active, hypophosphorylated state.
20680651	1	19	theme	gene	123:126	arg1	suppressor					163:172	a classical tumor suppressor	145:172	a classical tumor suppressor	145:172	The retinoblastoma-susceptibility gene product (pRB) is a classical tumor suppressor.
20680651	1	19	theme	gene	123:126	arg1	pRB					137:139	pRB	137:139	pRB	137:139	The retinoblastoma-susceptibility gene product (pRB) is a classical tumor suppressor.
20680651	1	19	theme	gene	123:126	arg1	product					128:134	The retinoblastoma-susceptibility gene product	89:134	The retinoblastoma-susceptibility gene product (pRB)	89:140	The retinoblastoma-susceptibility gene product (pRB) is a classical tumor suppressor.
20680651	7	20	dep	in	971:972	arg1	vitro					974:978	vitro	974:978	vitro	974:978	Here we show that pRB, and the related p107 protein, are modified by O-linked β-N-acetylglucosamine (O-GlcNAc) in an in vitro transcription/translation system.
20680651	0	21	theme	retinoblastoma-susceptibility	21:49	arg1	product					56:62	The E2F-1 associated retinoblastoma-susceptibility gene product	0:62	The E2F-1 associated retinoblastoma-susceptibility gene product	0:62	The E2F-1 associated retinoblastoma-susceptibility gene product is modified by O-GlcNAc.
20680651	0	22	mod	modified	67:74	arg1	product					56:62	The E2F-1 associated retinoblastoma-susceptibility gene product	0:62	The E2F-1 associated retinoblastoma-susceptibility gene product	0:62	The E2F-1 associated retinoblastoma-susceptibility gene product is modified by O-GlcNAc.
20680651	0	22	mod	modified	67:74	arg3	O-GlcNAc					79:86	O-GlcNAc	79:86	O-GlcNAc	79:86	The E2F-1 associated retinoblastoma-susceptibility gene product is modified by O-GlcNAc.
20680651	3	23	theme	essential	288:296	arg1	mechanisms					298:307	the essential mechanisms	284:307	the essential mechanisms by which pRB, and the related p107 and p130 family members, act	284:371	One of the essential mechanisms by which pRB, and the related p107 and p130 family members, act is through its interactions with the E2F class of transcription factors.
20680651	7	24	theme	O-linked	923:930	arg1	β-N-acetylglucosamine					932:952	O-linked β-N-acetylglucosamine	923:952	O-linked β-N-acetylglucosamine (O-GlcNAc) in an in vitro transcription/translation system	923:1011	Here we show that pRB, and the related p107 protein, are modified by O-linked β-N-acetylglucosamine (O-GlcNAc) in an in vitro transcription/translation system.
20680651	7	24	theme	O-linked	923:930	arg1	O-GlcNAc					955:962	O-GlcNAc	955:962	O-GlcNAc	955:962	Here we show that pRB, and the related p107 protein, are modified by O-linked β-N-acetylglucosamine (O-GlcNAc) in an in vitro transcription/translation system.
20680651	6	25	theme	S-phase	839:845	arg1	genes					847:851	essential S-phase genes	829:851	essential S-phase genes	829:851	Current dogma suggests that phosphorylation of pRB during mid- to late-G1 leads to release of E2F-1 and E2F-1 dependent transcriptional activation of essential S-phase genes.
20680651	0	26	theme	associated	10:19	arg1	product					56:62	The E2F-1 associated retinoblastoma-susceptibility gene product	0:62	The E2F-1 associated retinoblastoma-susceptibility gene product	0:62	The E2F-1 associated retinoblastoma-susceptibility gene product is modified by O-GlcNAc.
20680651	3	27	theme	mechanisms	298:307	arg1	mechanisms					298:307	the essential mechanisms	284:307	the essential mechanisms by which pRB, and the related p107 and p130 family members, act	284:371	One of the essential mechanisms by which pRB, and the related p107 and p130 family members, act is through its interactions with the E2F class of transcription factors.
20680651	3	27	theme	mechanisms	298:307	arg1	One					277:279	One	277:279	One	277:279	One of the essential mechanisms by which pRB, and the related p107 and p130 family members, act is through its interactions with the E2F class of transcription factors.
20680651	9	28	theme	E2F-1	1198:1202	arg1	pRB					1215:1217	E2F-1 associated pRB	1198:1217	E2F-1 associated pRB	1198:1217	Finally, we demonstrate that E2F-1 associated pRB is modified by O-GlcNAc.
20680651	7	29	mod	modified	911:918	arg3	O-GlcNAc					955:962	O-GlcNAc	955:962	O-GlcNAc	955:962	Here we show that pRB, and the related p107 protein, are modified by O-linked β-N-acetylglucosamine (O-GlcNAc) in an in vitro transcription/translation system.
20680651	7	29	mod	modified	911:918	arg3	β-N-acetylglucosamine					932:952	O-linked β-N-acetylglucosamine	923:952	O-linked β-N-acetylglucosamine (O-GlcNAc) in an in vitro transcription/translation system	923:1011	Here we show that pRB, and the related p107 protein, are modified by O-linked β-N-acetylglucosamine (O-GlcNAc) in an in vitro transcription/translation system.
20680651	7	29	mod	modified	911:918	arg1	pRB					872:874	pRB	872:874	pRB	872:874	Here we show that pRB, and the related p107 protein, are modified by O-linked β-N-acetylglucosamine (O-GlcNAc) in an in vitro transcription/translation system.
20680651	7	29	mod	modified	911:918	arg1	protein					898:904	and the related p107 protein	877:904	protein	898:904	Here we show that pRB, and the related p107 protein, are modified by O-linked β-N-acetylglucosamine (O-GlcNAc) in an in vitro transcription/translation system.
20680651	10	30	theme	function	1289:1296	arg1	s					1298:1298	pRB function(s)	1285:1299	pRB function(s)	1285:1299	These studies suggest that regulation of pRB function(s) may be controlled by dynamic O-GlcNAc modification, as well as phosphorylation.
20680651	9	31	theme	associated	1204:1213	arg1	pRB					1215:1217	E2F-1 associated pRB	1198:1217	E2F-1 associated pRB	1198:1217	Finally, we demonstrate that E2F-1 associated pRB is modified by O-GlcNAc.
20680651	6	32	theme	Current	679:685	arg1	dogma					687:691	Current dogma	679:691	Current dogma	679:691	Current dogma suggests that phosphorylation of pRB during mid- to late-G1 leads to release of E2F-1 and E2F-1 dependent transcriptional activation of essential S-phase genes.
20680651	3	33	theme	factors	437:443	arg1	class					414:418	the E2F class	406:418	the E2F class of transcription factors	406:443	One of the essential mechanisms by which pRB, and the related p107 and p130 family members, act is through its interactions with the E2F class of transcription factors.
20680651	0	34	theme	gene	51:54	arg1	product					56:62	The E2F-1 associated retinoblastoma-susceptibility gene product	0:62	The E2F-1 associated retinoblastoma-susceptibility gene product	0:62	The E2F-1 associated retinoblastoma-susceptibility gene product is modified by O-GlcNAc.
20680651	6	35	theme	E2F-1	773:777	arg1	release					762:768	release	762:768	release of E2F-1	762:777	Current dogma suggests that phosphorylation of pRB during mid- to late-G1 leads to release of E2F-1 and E2F-1 dependent transcriptional activation of essential S-phase genes.
20680651	6	35	theme	E2F-1	773:777	arg1	activation					815:824	E2F-1 dependent transcriptional activation	783:824	E2F-1 dependent transcriptional activation of essential S-phase genes	783:851	Current dogma suggests that phosphorylation of pRB during mid- to late-G1 leads to release of E2F-1 and E2F-1 dependent transcriptional activation of essential S-phase genes.
20680651	8	36	theme	active	1135:1140	arg1	state					1162:1166	an active, hypophosphorylated state	1132:1166	state	1162:1166	Furthermore, we show in vivo that pRB is more heavily glycosylated in G1 of the cell-cycle when pRB is known to be in an active, hypophosphorylated state.
20680651	8	37	theme	cell-cycle	1094:1103	arg1	G1					1084:1085	G1	1084:1085	G1 of the cell-cycle	1084:1103	Furthermore, we show in vivo that pRB is more heavily glycosylated in G1 of the cell-cycle when pRB is known to be in an active, hypophosphorylated state.
20680651	4	38	theme	E2F-1	446:450	arg1	transcription					452:464	E2F-1 transcription	446:464	E2F-1 transcription	446:464	E2F-1 transcription is necessary for entry into S-phase during the cell-cycle.
20680651	10	39	theme	s	1298:1298	arg1	regulation					1271:1280	regulation	1271:1280	regulation of pRB function(s)	1271:1299	These studies suggest that regulation of pRB function(s) may be controlled by dynamic O-GlcNAc modification, as well as phosphorylation.
20680651	2	40	theme	processes	210:218	arg1	differentiation					245:259	differentiation	245:259	differentiation	245:259	pRB regulates a number of cellular processes including proliferation, differentiation, and apoptosis.
20680651	2	40	theme	processes	210:218	arg1	apoptosis					266:274	apoptosis	266:274	apoptosis	266:274	pRB regulates a number of cellular processes including proliferation, differentiation, and apoptosis.
20680651	2	40	theme	processes	210:218	arg1	proliferation					230:242	proliferation	230:242	proliferation	230:242	pRB regulates a number of cellular processes including proliferation, differentiation, and apoptosis.
20680651	2	40	theme	processes	210:218	arg1	number					191:196	a number	189:196	a number of cellular processes including proliferation, differentiation, and apoptosis	189:274	pRB regulates a number of cellular processes including proliferation, differentiation, and apoptosis.
20680651	6	41	theme	essential	829:837	arg1	genes					847:851	essential S-phase genes	829:851	essential S-phase genes	829:851	Current dogma suggests that phosphorylation of pRB during mid- to late-G1 leads to release of E2F-1 and E2F-1 dependent transcriptional activation of essential S-phase genes.
20680651	7	42	from	β-N-acetylglucosamine	932:952	arg1	system					1006:1011	an in vitro transcription/translation system	968:1011	an in vitro transcription/translation system	968:1011	Here we show that pRB, and the related p107 protein, are modified by O-linked β-N-acetylglucosamine (O-GlcNAc) in an in vitro transcription/translation system.
20680651	9	43	mod	modified	1222:1229	arg1	pRB					1215:1217	E2F-1 associated pRB	1198:1217	E2F-1 associated pRB	1198:1217	Finally, we demonstrate that E2F-1 associated pRB is modified by O-GlcNAc.
20680651	9	43	mod	modified	1222:1229	arg3	O-GlcNAc					1234:1241	O-GlcNAc	1234:1241	O-GlcNAc	1234:1241	Finally, we demonstrate that E2F-1 associated pRB is modified by O-GlcNAc.
20680651	2	44	theme	cellular	201:208	arg1	differentiation					245:259	differentiation	245:259	differentiation	245:259	pRB regulates a number of cellular processes including proliferation, differentiation, and apoptosis.
20680651	2	44	theme	cellular	201:208	arg1	apoptosis					266:274	apoptosis	266:274	apoptosis	266:274	pRB regulates a number of cellular processes including proliferation, differentiation, and apoptosis.
20680651	2	44	theme	cellular	201:208	arg1	proliferation					230:242	proliferation	230:242	proliferation	230:242	pRB regulates a number of cellular processes including proliferation, differentiation, and apoptosis.
20680651	2	44	theme	cellular	201:208	arg1	processes					210:218	cellular processes	201:218	cellular processes including proliferation, differentiation, and apoptosis	201:274	pRB regulates a number of cellular processes including proliferation, differentiation, and apoptosis.
20680651	7	45	theme	transcription/translation	980:1004	arg1	system					1006:1011	an in vitro transcription/translation system	968:1011	an in vitro transcription/translation system	968:1011	Here we show that pRB, and the related p107 protein, are modified by O-linked β-N-acetylglucosamine (O-GlcNAc) in an in vitro transcription/translation system.
20680651	10	46	theme	pRB	1285:1287	arg1	s					1298:1298	pRB function(s)	1285:1299	pRB function(s)	1285:1299	These studies suggest that regulation of pRB function(s) may be controlled by dynamic O-GlcNAc modification, as well as phosphorylation.
20680651	7	47	link	O-linked	923:930	arg1	β-N-acetylglucosamine					932:952	O-linked β-N-acetylglucosamine	923:952	O-linked β-N-acetylglucosamine (O-GlcNAc) in an in vitro transcription/translation system	923:1011	Here we show that pRB, and the related p107 protein, are modified by O-linked β-N-acetylglucosamine (O-GlcNAc) in an in vitro transcription/translation system.
20680651	7	47	link	O-linked	923:930	arg1	O-GlcNAc					955:962	O-GlcNAc	955:962	O-GlcNAc	955:962	Here we show that pRB, and the related p107 protein, are modified by O-linked β-N-acetylglucosamine (O-GlcNAc) in an in vitro transcription/translation system.
20680651	3	48	theme	related	331:337	arg1	p107					339:342	the related p107	327:342	the related p107	327:342	One of the essential mechanisms by which pRB, and the related p107 and p130 family members, act is through its interactions with the E2F class of transcription factors.
20680651	6	49	theme	genes	847:851	arg1	release					762:768	release	762:768	release of E2F-1	762:777	Current dogma suggests that phosphorylation of pRB during mid- to late-G1 leads to release of E2F-1 and E2F-1 dependent transcriptional activation of essential S-phase genes.
20680651	6	49	theme	genes	847:851	arg1	activation					815:824	E2F-1 dependent transcriptional activation	783:824	E2F-1 dependent transcriptional activation of essential S-phase genes	783:851	Current dogma suggests that phosphorylation of pRB during mid- to late-G1 leads to release of E2F-1 and E2F-1 dependent transcriptional activation of essential S-phase genes.
20680651	1	50	theme	classical	147:155	arg1	product					128:134	The retinoblastoma-susceptibility gene product	89:134	The retinoblastoma-susceptibility gene product (pRB)	89:140	The retinoblastoma-susceptibility gene product (pRB) is a classical tumor suppressor.
20680651	1	50	theme	classical	147:155	arg1	suppressor					163:172	a classical tumor suppressor	145:172	a classical tumor suppressor	145:172	The retinoblastoma-susceptibility gene product (pRB) is a classical tumor suppressor.
20680651	3	51	theme	p107	339:342	arg1	members					360:366	the related p107 and p130 family members	327:366	the related p107 and p130 family members	327:366	One of the essential mechanisms by which pRB, and the related p107 and p130 family members, act is through its interactions with the E2F class of transcription factors.
20680651	7	52	theme	in	971:972	arg1	system					1006:1011	an in vitro transcription/translation system	968:1011	an in vitro transcription/translation system	968:1011	Here we show that pRB, and the related p107 protein, are modified by O-linked β-N-acetylglucosamine (O-GlcNAc) in an in vitro transcription/translation system.
20680651	1	53	theme	tumor	157:161	arg1	product					128:134	The retinoblastoma-susceptibility gene product	89:134	The retinoblastoma-susceptibility gene product (pRB)	89:140	The retinoblastoma-susceptibility gene product (pRB) is a classical tumor suppressor.
20680651	1	53	theme	tumor	157:161	arg1	suppressor					163:172	a classical tumor suppressor	145:172	a classical tumor suppressor	145:172	The retinoblastoma-susceptibility gene product (pRB) is a classical tumor suppressor.
20680651	7	54	theme	related	885:891	arg1	pRB					872:874	pRB	872:874	pRB	872:874	Here we show that pRB, and the related p107 protein, are modified by O-linked β-N-acetylglucosamine (O-GlcNAc) in an in vitro transcription/translation system.
20680651	7	54	theme	related	885:891	arg1	protein					898:904	and the related p107 protein	877:904	protein	898:904	Here we show that pRB, and the related p107 protein, are modified by O-linked β-N-acetylglucosamine (O-GlcNAc) in an in vitro transcription/translation system.
28929346	8	0	theme	breast	1440:1445	arg1	cancer					1447:1452	breast cancer	1440:1452	breast cancer	1440:1452	These data predict that under conditions where O-GlcNAc levels are high (breast cancer), PR, through an interaction with the modifying enzyme OGT, will exhibit increased O-GlcNAcylation and potentiated transcriptional activity.
28929346	8	0	theme	breast	1440:1445	arg1	levels					1423:1428	O-GlcNAc levels	1414:1428	O-GlcNAc levels	1414:1428	These data predict that under conditions where O-GlcNAc levels are high (breast cancer), PR, through an interaction with the modifying enzyme OGT, will exhibit increased O-GlcNAcylation and potentiated transcriptional activity.
28929346	9	1	theme	Therapeutic	1595:1605	arg1	strategies					1607:1616	Therapeutic strategies	1595:1616	Therapeutic strategies aimed at altering cellular O-GlcNAc levels	1595:1659	Therapeutic strategies aimed at altering cellular O-GlcNAc levels may have profound effects on PR transcriptional activity in breast cancer.
28929346	3	2	theme	nuclear	506:512	arg1	receptors					514:522	nuclear receptors	506:522	nuclear receptors	506:522	PR interacts with many different types of proteins, including transcriptional co-activators and co-repressors, transcription factors, nuclear receptors, and proteins that post-translationally modify PR (i.e., kinases and phosphatases).
28929346	3	2	theme	nuclear	506:512	arg1	co-repressors					468:480	co-repressors	468:480	co-repressors	468:480	PR interacts with many different types of proteins, including transcriptional co-activators and co-repressors, transcription factors, nuclear receptors, and proteins that post-translationally modify PR (i.e., kinases and phosphatases).
28929346	3	2	theme	nuclear	506:512	arg1	co-activators					450:462	transcriptional co-activators	434:462	transcriptional co-activators	434:462	PR interacts with many different types of proteins, including transcriptional co-activators and co-repressors, transcription factors, nuclear receptors, and proteins that post-translationally modify PR (i.e., kinases and phosphatases).
28929346	6	3	theme	O-GlcNAc	1127:1134	arg1	levels					1136:1141	O-GlcNAc levels	1127:1141	O-GlcNAc levels	1127:1141	Moreover, we show that O-GlcNAcylated PR is more transcriptionally active on PR-target genes, despite the observation that PR messenger RNA and protein levels are decreased when O-GlcNAc levels are high.
28929346	4	4	theme	target	832:837	arg1	proteins					839:846	target proteins	832:846	target proteins	832:846	Herein, we identify a novel interaction between PR and O-GlcNAc transferase (OGT), the enzyme that catalyzes the addition of a single N-acetylglucosamine sugar, referred to as O-GlcNAc, to acceptor serines and threonines in target proteins.
28929346	6	5	theme	PR	1072:1073	arg1	RNA					1085:1087	PR messenger RNA	1072:1087	PR messenger RNA	1072:1087	Moreover, we show that O-GlcNAcylated PR is more transcriptionally active on PR-target genes, despite the observation that PR messenger RNA and protein levels are decreased when O-GlcNAc levels are high.
28929346	3	6	theme	receptors	514:522	arg1	types					405:409	many different types	390:409	many different types of proteins, including transcriptional co-activators and co-repressors, transcription factors, nuclear receptors, and proteins that post-translationally modify PR (i.e., kinases and phosphatases)	390:605	PR interacts with many different types of proteins, including transcriptional co-activators and co-repressors, transcription factors, nuclear receptors, and proteins that post-translationally modify PR (i.e., kinases and phosphatases).
28929346	5	7	theme	post-translational	898:915	arg1	modification					917:928	the post-translational modification	894:928	the post-translational modification of PR by O-GlcNAc	894:946	This interaction between PR and OGT leads to the post-translational modification of PR by O-GlcNAc.
28929346	7	8	theme	breast	1172:1177	arg1	cancer					1179:1184	breast cancer	1172:1184	breast cancer	1172:1184	O-GlcNAcylation in breast cancer is clinically relevant, as we show that O-GlcNAc levels are higher in breast cancer as compared to matched normal tissues, and PR-positive breast cancers have higher levels of OGT.
28929346	7	9	theme	PR-positive	1313:1323	arg1	cancers					1332:1338	PR-positive breast cancers	1313:1338	PR-positive breast cancers	1313:1338	O-GlcNAcylation in breast cancer is clinically relevant, as we show that O-GlcNAc levels are higher in breast cancer as compared to matched normal tissues, and PR-positive breast cancers have higher levels of OGT.
28929346	7	10	theme	breast	1325:1330	arg1	cancers					1332:1338	PR-positive breast cancers	1313:1338	PR-positive breast cancers	1313:1338	O-GlcNAcylation in breast cancer is clinically relevant, as we show that O-GlcNAc levels are higher in breast cancer as compared to matched normal tissues, and PR-positive breast cancers have higher levels of OGT.
28929346	4	11	theme	single	735:740	arg1	sugar					762:766	a single N-acetylglucosamine sugar	733:766	a single N-acetylglucosamine sugar	733:766	Herein, we identify a novel interaction between PR and O-GlcNAc transferase (OGT), the enzyme that catalyzes the addition of a single N-acetylglucosamine sugar, referred to as O-GlcNAc, to acceptor serines and threonines in target proteins.
28929346	5	12	theme	PR	933:934	arg1	modification					917:928	the post-translational modification	894:928	the post-translational modification of PR by O-GlcNAc	894:946	This interaction between PR and OGT leads to the post-translational modification of PR by O-GlcNAc.
28929346	1	13	theme	trial	100:104	arg1	data					106:109	Emerging clinical trial data	82:109	Emerging clinical trial data	82:109	Emerging clinical trial data implicate progestins in the development of breast cancer.
28929346	6	14	theme	RNA	1085:1087	arg1	levels					1101:1106	PR messenger RNA and protein levels	1072:1106	PR messenger RNA and protein levels	1072:1106	Moreover, we show that O-GlcNAcylated PR is more transcriptionally active on PR-target genes, despite the observation that PR messenger RNA and protein levels are decreased when O-GlcNAc levels are high.
28929346	4	15	from	threonines	818:827	arg1	proteins					839:846	target proteins	832:846	target proteins	832:846	Herein, we identify a novel interaction between PR and O-GlcNAc transferase (OGT), the enzyme that catalyzes the addition of a single N-acetylglucosamine sugar, referred to as O-GlcNAc, to acceptor serines and threonines in target proteins.
28929346	1	16	theme	Emerging	82:89	arg1	data					106:109	Emerging clinical trial data	82:109	Emerging clinical trial data	82:109	Emerging clinical trial data implicate progestins in the development of breast cancer.
28929346	3	17	dep	kinases	581:587	arg1	i.e.					575:578	i.e.	575:578	i.e.	575:578	PR interacts with many different types of proteins, including transcriptional co-activators and co-repressors, transcription factors, nuclear receptors, and proteins that post-translationally modify PR (i.e., kinases and phosphatases).
28929346	7	18	contain	have	1340:1343	arg1	cancers					1332:1338	PR-positive breast cancers	1313:1338	PR-positive breast cancers	1313:1338	O-GlcNAcylation in breast cancer is clinically relevant, as we show that O-GlcNAc levels are higher in breast cancer as compared to matched normal tissues, and PR-positive breast cancers have higher levels of OGT.
28929346	7	18	contain	have	1340:1343	arg2	levels					1352:1357	higher levels	1345:1357	higher levels of OGT	1345:1364	O-GlcNAcylation in breast cancer is clinically relevant, as we show that O-GlcNAc levels are higher in breast cancer as compared to matched normal tissues, and PR-positive breast cancers have higher levels of OGT.
28929346	8	19	theme	O-GlcNAc	1414:1421	arg1	cancer					1447:1452	breast cancer	1440:1452	breast cancer	1440:1452	These data predict that under conditions where O-GlcNAc levels are high (breast cancer), PR, through an interaction with the modifying enzyme OGT, will exhibit increased O-GlcNAcylation and potentiated transcriptional activity.
28929346	8	19	theme	O-GlcNAc	1414:1421	arg1	levels					1423:1428	O-GlcNAc levels	1414:1428	O-GlcNAc levels	1414:1428	These data predict that under conditions where O-GlcNAc levels are high (breast cancer), PR, through an interaction with the modifying enzyme OGT, will exhibit increased O-GlcNAcylation and potentiated transcriptional activity.
28929346	8	20	theme	transcriptional	1569:1583	arg1	activity					1585:1592	potentiated transcriptional activity	1557:1592	potentiated transcriptional activity	1557:1592	These data predict that under conditions where O-GlcNAc levels are high (breast cancer), PR, through an interaction with the modifying enzyme OGT, will exhibit increased O-GlcNAcylation and potentiated transcriptional activity.
28929346	1	21	theme	clinical	91:98	arg1	data					106:109	Emerging clinical trial data	82:109	Emerging clinical trial data	82:109	Emerging clinical trial data implicate progestins in the development of breast cancer.
28929346	7	22	theme	OGT	1362:1364	arg1	levels					1352:1357	higher levels	1345:1357	higher levels of OGT	1345:1364	O-GlcNAcylation in breast cancer is clinically relevant, as we show that O-GlcNAc levels are higher in breast cancer as compared to matched normal tissues, and PR-positive breast cancers have higher levels of OGT.
28929346	4	23	from	serines	806:812	arg1	proteins					839:846	target proteins	832:846	target proteins	832:846	Herein, we identify a novel interaction between PR and O-GlcNAc transferase (OGT), the enzyme that catalyzes the addition of a single N-acetylglucosamine sugar, referred to as O-GlcNAc, to acceptor serines and threonines in target proteins.
28929346	9	24	theme	O-GlcNAc	1645:1652	arg1	levels					1654:1659	cellular O-GlcNAc levels	1636:1659	cellular O-GlcNAc levels	1636:1659	Therapeutic strategies aimed at altering cellular O-GlcNAc levels may have profound effects on PR transcriptional activity in breast cancer.
28929346	2	25	theme	nuclear	299:305	arg1	receptor					307:314	a steroid-activated nuclear receptor	279:314	a steroid-activated nuclear receptor	279:314	While the role for the progesterone receptor (PR) in this process remains controversial, it is clear that PR, a steroid-activated nuclear receptor, alters the transcriptional landscape of breast cancer.
28929346	2	25	theme	nuclear	299:305	arg1	PR					275:276	PR	275:276	PR	275:276	While the role for the progesterone receptor (PR) in this process remains controversial, it is clear that PR, a steroid-activated nuclear receptor, alters the transcriptional landscape of breast cancer.
28929346	4	26	theme	O-GlcNAc	663:670	arg1	OGT					685:687	OGT	685:687	OGT	685:687	Herein, we identify a novel interaction between PR and O-GlcNAc transferase (OGT), the enzyme that catalyzes the addition of a single N-acetylglucosamine sugar, referred to as O-GlcNAc, to acceptor serines and threonines in target proteins.
28929346	4	26	theme	O-GlcNAc	663:670	arg1	transferase					672:682	O-GlcNAc transferase	663:682	O-GlcNAc transferase (OGT)	663:688	Herein, we identify a novel interaction between PR and O-GlcNAc transferase (OGT), the enzyme that catalyzes the addition of a single N-acetylglucosamine sugar, referred to as O-GlcNAc, to acceptor serines and threonines in target proteins.
28929346	0	27	theme	O-GlcNAc-Dependent	0:17	arg1	Regulation					19:28	O-GlcNAc-Dependent Regulation	0:28	O-GlcNAc-Dependent Regulation of Progesterone Receptor	0:53	O-GlcNAc-Dependent Regulation of Progesterone Receptor Function in Breast Cancer.
28929346	2	28	theme	steroid-activated	281:297	arg1	receptor					307:314	a steroid-activated nuclear receptor	279:314	a steroid-activated nuclear receptor	279:314	While the role for the progesterone receptor (PR) in this process remains controversial, it is clear that PR, a steroid-activated nuclear receptor, alters the transcriptional landscape of breast cancer.
28929346	2	28	theme	steroid-activated	281:297	arg1	PR					275:276	PR	275:276	PR	275:276	While the role for the progesterone receptor (PR) in this process remains controversial, it is clear that PR, a steroid-activated nuclear receptor, alters the transcriptional landscape of breast cancer.
28929346	2	29	theme	cancer	364:369	arg1	landscape					344:352	the transcriptional landscape	324:352	the transcriptional landscape of breast cancer	324:369	While the role for the progesterone receptor (PR) in this process remains controversial, it is clear that PR, a steroid-activated nuclear receptor, alters the transcriptional landscape of breast cancer.
28929346	0	30	theme	Progesterone	33:44	arg1	Receptor					46:53	Progesterone Receptor	33:53	Progesterone Receptor	33:53	O-GlcNAc-Dependent Regulation of Progesterone Receptor Function in Breast Cancer.
28929346	8	31	dep	high	1434:1437	arg1	cancer					1447:1452	breast cancer	1440:1452	breast cancer	1440:1452	These data predict that under conditions where O-GlcNAc levels are high (breast cancer), PR, through an interaction with the modifying enzyme OGT, will exhibit increased O-GlcNAcylation and potentiated transcriptional activity.
28929346	8	31	dep	high	1434:1437	arg1	levels					1423:1428	O-GlcNAc levels	1414:1428	O-GlcNAc levels	1414:1428	These data predict that under conditions where O-GlcNAc levels are high (breast cancer), PR, through an interaction with the modifying enzyme OGT, will exhibit increased O-GlcNAcylation and potentiated transcriptional activity.
28929346	9	32	from	activity	1709:1716	arg1	cancer					1728:1733	breast cancer	1721:1733	breast cancer	1721:1733	Therapeutic strategies aimed at altering cellular O-GlcNAc levels may have profound effects on PR transcriptional activity in breast cancer.
28929346	6	33	theme	PR-target	1026:1034	arg1	genes					1036:1040	PR-target genes	1026:1040	PR-target genes	1026:1040	Moreover, we show that O-GlcNAcylated PR is more transcriptionally active on PR-target genes, despite the observation that PR messenger RNA and protein levels are decreased when O-GlcNAc levels are high.
28929346	8	34	theme	modifying	1492:1500	arg1	OGT					1509:1511	the modifying enzyme OGT	1488:1511	the modifying enzyme OGT	1488:1511	These data predict that under conditions where O-GlcNAc levels are high (breast cancer), PR, through an interaction with the modifying enzyme OGT, will exhibit increased O-GlcNAcylation and potentiated transcriptional activity.
28929346	3	35	theme	proteins	529:536	arg1	types					405:409	many different types	390:409	many different types of proteins, including transcriptional co-activators and co-repressors, transcription factors, nuclear receptors, and proteins that post-translationally modify PR (i.e., kinases and phosphatases)	390:605	PR interacts with many different types of proteins, including transcriptional co-activators and co-repressors, transcription factors, nuclear receptors, and proteins that post-translationally modify PR (i.e., kinases and phosphatases).
28929346	7	36	from	O-GlcNAcylation	1153:1167	arg1	cancer					1179:1184	breast cancer	1172:1184	breast cancer	1172:1184	O-GlcNAcylation in breast cancer is clinically relevant, as we show that O-GlcNAc levels are higher in breast cancer as compared to matched normal tissues, and PR-positive breast cancers have higher levels of OGT.
28929346	2	37	theme	transcriptional	328:342	arg1	landscape					344:352	the transcriptional landscape	324:352	the transcriptional landscape of breast cancer	324:369	While the role for the progesterone receptor (PR) in this process remains controversial, it is clear that PR, a steroid-activated nuclear receptor, alters the transcriptional landscape of breast cancer.
28929346	1	38	theme	breast	154:159	arg1	cancer					161:166	breast cancer	154:166	breast cancer	154:166	Emerging clinical trial data implicate progestins in the development of breast cancer.
28929346	3	39	theme	different	395:403	arg1	types					405:409	many different types	390:409	many different types of proteins, including transcriptional co-activators and co-repressors, transcription factors, nuclear receptors, and proteins that post-translationally modify PR (i.e., kinases and phosphatases)	390:605	PR interacts with many different types of proteins, including transcriptional co-activators and co-repressors, transcription factors, nuclear receptors, and proteins that post-translationally modify PR (i.e., kinases and phosphatases).
28929346	7	40	theme	breast	1256:1261	arg1	cancer					1263:1268	breast cancer	1256:1268	breast cancer	1256:1268	O-GlcNAcylation in breast cancer is clinically relevant, as we show that O-GlcNAc levels are higher in breast cancer as compared to matched normal tissues, and PR-positive breast cancers have higher levels of OGT.
28929346	9	41	theme	profound	1670:1677	arg1	effects					1679:1685	profound effects	1670:1685	profound effects	1670:1685	Therapeutic strategies aimed at altering cellular O-GlcNAc levels may have profound effects on PR transcriptional activity in breast cancer.
28929346	9	42	theme	cellular	1636:1643	arg1	levels					1654:1659	cellular O-GlcNAc levels	1636:1659	cellular O-GlcNAc levels	1636:1659	Therapeutic strategies aimed at altering cellular O-GlcNAc levels may have profound effects on PR transcriptional activity in breast cancer.
28929346	3	43	theme	proteins	414:421	arg1	types					405:409	many different types	390:409	many different types of proteins, including transcriptional co-activators and co-repressors, transcription factors, nuclear receptors, and proteins that post-translationally modify PR (i.e., kinases and phosphatases)	390:605	PR interacts with many different types of proteins, including transcriptional co-activators and co-repressors, transcription factors, nuclear receptors, and proteins that post-translationally modify PR (i.e., kinases and phosphatases).
28929346	3	44	theme	transcriptional	434:448	arg1	co-activators					450:462	transcriptional co-activators	434:462	transcriptional co-activators	434:462	PR interacts with many different types of proteins, including transcriptional co-activators and co-repressors, transcription factors, nuclear receptors, and proteins that post-translationally modify PR (i.e., kinases and phosphatases).
28929346	0	45	theme	Receptor	46:53	arg1	Regulation					19:28	O-GlcNAc-Dependent Regulation	0:28	O-GlcNAc-Dependent Regulation of Progesterone Receptor	0:53	O-GlcNAc-Dependent Regulation of Progesterone Receptor Function in Breast Cancer.
28929346	8	46	theme	potentiated	1557:1567	arg1	activity					1585:1592	potentiated transcriptional activity	1557:1592	potentiated transcriptional activity	1557:1592	These data predict that under conditions where O-GlcNAc levels are high (breast cancer), PR, through an interaction with the modifying enzyme OGT, will exhibit increased O-GlcNAcylation and potentiated transcriptional activity.
28929346	7	47	theme	matched	1285:1291	arg1	tissues					1300:1306	matched normal tissues	1285:1306	matched normal tissues	1285:1306	O-GlcNAcylation in breast cancer is clinically relevant, as we show that O-GlcNAc levels are higher in breast cancer as compared to matched normal tissues, and PR-positive breast cancers have higher levels of OGT.
28929346	3	48	dep	proteins	414:421	arg1	phosphatases					593:604	phosphatases	593:604	phosphatases	593:604	PR interacts with many different types of proteins, including transcriptional co-activators and co-repressors, transcription factors, nuclear receptors, and proteins that post-translationally modify PR (i.e., kinases and phosphatases).
28929346	3	48	dep	proteins	414:421	arg1	kinases					581:587	kinases	581:587	kinases	581:587	PR interacts with many different types of proteins, including transcriptional co-activators and co-repressors, transcription factors, nuclear receptors, and proteins that post-translationally modify PR (i.e., kinases and phosphatases).
28929346	4	49	theme	novel	630:634	arg1	interaction					636:646	a novel interaction	628:646	a novel interaction between PR and O-GlcNAc transferase (OGT), the enzyme that catalyzes the addition of a single N-acetylglucosamine sugar, referred to as O-GlcNAc, to acceptor serines and threonines in target proteins	628:846	Herein, we identify a novel interaction between PR and O-GlcNAc transferase (OGT), the enzyme that catalyzes the addition of a single N-acetylglucosamine sugar, referred to as O-GlcNAc, to acceptor serines and threonines in target proteins.
28929346	0	50	theme	Breast	67:72	arg1	Cancer					74:79	Breast Cancer	67:79	Breast Cancer	67:79	O-GlcNAc-Dependent Regulation of Progesterone Receptor Function in Breast Cancer.
28929346	8	51	theme	enzyme	1502:1507	arg1	OGT					1509:1511	the modifying enzyme OGT	1488:1511	the modifying enzyme OGT	1488:1511	These data predict that under conditions where O-GlcNAc levels are high (breast cancer), PR, through an interaction with the modifying enzyme OGT, will exhibit increased O-GlcNAcylation and potentiated transcriptional activity.
28929346	4	52	theme	acceptor	797:804	arg1	serines					806:812	serines	806:812	serines	806:812	Herein, we identify a novel interaction between PR and O-GlcNAc transferase (OGT), the enzyme that catalyzes the addition of a single N-acetylglucosamine sugar, referred to as O-GlcNAc, to acceptor serines and threonines in target proteins.
28929346	6	53	theme	messenger	1075:1083	arg1	RNA					1085:1087	PR messenger RNA	1072:1087	PR messenger RNA	1072:1087	Moreover, we show that O-GlcNAcylated PR is more transcriptionally active on PR-target genes, despite the observation that PR messenger RNA and protein levels are decreased when O-GlcNAc levels are high.
28929346	3	54	theme	factors	497:503	arg1	types					405:409	many different types	390:409	many different types of proteins, including transcriptional co-activators and co-repressors, transcription factors, nuclear receptors, and proteins that post-translationally modify PR (i.e., kinases and phosphatases)	390:605	PR interacts with many different types of proteins, including transcriptional co-activators and co-repressors, transcription factors, nuclear receptors, and proteins that post-translationally modify PR (i.e., kinases and phosphatases).
28929346	3	55	theme	many	390:393	arg1	types					405:409	many different types	390:409	many different types of proteins, including transcriptional co-activators and co-repressors, transcription factors, nuclear receptors, and proteins that post-translationally modify PR (i.e., kinases and phosphatases)	390:605	PR interacts with many different types of proteins, including transcriptional co-activators and co-repressors, transcription factors, nuclear receptors, and proteins that post-translationally modify PR (i.e., kinases and phosphatases).
28929346	9	56	theme	PR	1690:1691	arg1	activity					1709:1716	PR transcriptional activity	1690:1716	PR transcriptional activity in breast cancer	1690:1733	Therapeutic strategies aimed at altering cellular O-GlcNAc levels may have profound effects on PR transcriptional activity in breast cancer.
28929346	8	57	with	interaction	1471:1481	arg1	OGT					1509:1511	the modifying enzyme OGT	1488:1511	the modifying enzyme OGT	1488:1511	These data predict that under conditions where O-GlcNAc levels are high (breast cancer), PR, through an interaction with the modifying enzyme OGT, will exhibit increased O-GlcNAcylation and potentiated transcriptional activity.
28929346	6	58	theme	protein	1093:1099	arg1	levels					1101:1106	PR messenger RNA and protein levels	1072:1106	PR messenger RNA and protein levels	1072:1106	Moreover, we show that O-GlcNAcylated PR is more transcriptionally active on PR-target genes, despite the observation that PR messenger RNA and protein levels are decreased when O-GlcNAc levels are high.
28929346	9	59	theme	transcriptional	1693:1707	arg1	activity					1709:1716	PR transcriptional activity	1690:1716	PR transcriptional activity in breast cancer	1690:1733	Therapeutic strategies aimed at altering cellular O-GlcNAc levels may have profound effects on PR transcriptional activity in breast cancer.
28929346	7	60	theme	higher	1345:1350	arg1	levels					1352:1357	higher levels	1345:1357	higher levels of OGT	1345:1364	O-GlcNAcylation in breast cancer is clinically relevant, as we show that O-GlcNAc levels are higher in breast cancer as compared to matched normal tissues, and PR-positive breast cancers have higher levels of OGT.
28929346	7	61	theme	O-GlcNAc	1226:1233	arg1	levels					1235:1240	O-GlcNAc levels	1226:1240	O-GlcNAc levels	1226:1240	O-GlcNAcylation in breast cancer is clinically relevant, as we show that O-GlcNAc levels are higher in breast cancer as compared to matched normal tissues, and PR-positive breast cancers have higher levels of OGT.
28929346	8	62	theme	increased	1527:1535	arg1	O-GlcNAcylation					1537:1551	increased O-GlcNAcylation	1527:1551	increased O-GlcNAcylation	1527:1551	These data predict that under conditions where O-GlcNAc levels are high (breast cancer), PR, through an interaction with the modifying enzyme OGT, will exhibit increased O-GlcNAcylation and potentiated transcriptional activity.
28929346	4	63	theme	N-acetylglucosamine	742:760	arg1	sugar					762:766	a single N-acetylglucosamine sugar	733:766	a single N-acetylglucosamine sugar	733:766	Herein, we identify a novel interaction between PR and O-GlcNAc transferase (OGT), the enzyme that catalyzes the addition of a single N-acetylglucosamine sugar, referred to as O-GlcNAc, to acceptor serines and threonines in target proteins.
28929346	4	64	theme	sugar	762:766	arg1	addition					721:728	the addition	717:728	the addition of a single N-acetylglucosamine sugar, referred to as O-GlcNAc, to acceptor serines and threonines in target proteins	717:846	Herein, we identify a novel interaction between PR and O-GlcNAc transferase (OGT), the enzyme that catalyzes the addition of a single N-acetylglucosamine sugar, referred to as O-GlcNAc, to acceptor serines and threonines in target proteins.
28929346	3	65	theme	transcription	483:495	arg1	factors					497:503	transcription factors	483:503	transcription factors	483:503	PR interacts with many different types of proteins, including transcriptional co-activators and co-repressors, transcription factors, nuclear receptors, and proteins that post-translationally modify PR (i.e., kinases and phosphatases).
28929346	3	65	theme	transcription	483:495	arg1	co-activators					450:462	transcriptional co-activators	434:462	transcriptional co-activators	434:462	PR interacts with many different types of proteins, including transcriptional co-activators and co-repressors, transcription factors, nuclear receptors, and proteins that post-translationally modify PR (i.e., kinases and phosphatases).
28929346	3	65	theme	transcription	483:495	arg1	co-repressors					468:480	co-repressors	468:480	co-repressors	468:480	PR interacts with many different types of proteins, including transcriptional co-activators and co-repressors, transcription factors, nuclear receptors, and proteins that post-translationally modify PR (i.e., kinases and phosphatases).
28929346	9	66	contain	have	1665:1668	arg2	effects					1679:1685	profound effects	1670:1685	profound effects	1670:1685	Therapeutic strategies aimed at altering cellular O-GlcNAc levels may have profound effects on PR transcriptional activity in breast cancer.
28929346	9	66	contain	have	1665:1668	arg1	strategies					1607:1616	Therapeutic strategies	1595:1616	Therapeutic strategies aimed at altering cellular O-GlcNAc levels	1595:1659	Therapeutic strategies aimed at altering cellular O-GlcNAc levels may have profound effects on PR transcriptional activity in breast cancer.
28929346	2	67	from	role	179:182	arg1	process					227:233	this process	222:233	this process	222:233	While the role for the progesterone receptor (PR) in this process remains controversial, it is clear that PR, a steroid-activated nuclear receptor, alters the transcriptional landscape of breast cancer.
28929346	2	68	theme	progesterone	192:203	arg1	receptor					205:212	progesterone receptor	192:212	the progesterone receptor (PR)	188:217	While the role for the progesterone receptor (PR) in this process remains controversial, it is clear that PR, a steroid-activated nuclear receptor, alters the transcriptional landscape of breast cancer.
28929346	2	68	theme	progesterone	192:203	arg1	PR					215:216	PR	215:216	PR	215:216	While the role for the progesterone receptor (PR) in this process remains controversial, it is clear that PR, a steroid-activated nuclear receptor, alters the transcriptional landscape of breast cancer.
28929346	2	69	theme	breast	357:362	arg1	cancer					364:369	breast cancer	357:369	breast cancer	357:369	While the role for the progesterone receptor (PR) in this process remains controversial, it is clear that PR, a steroid-activated nuclear receptor, alters the transcriptional landscape of breast cancer.
28929346	7	70	theme	normal	1293:1298	arg1	tissues					1300:1306	matched normal tissues	1285:1306	matched normal tissues	1285:1306	O-GlcNAcylation in breast cancer is clinically relevant, as we show that O-GlcNAc levels are higher in breast cancer as compared to matched normal tissues, and PR-positive breast cancers have higher levels of OGT.
28929346	9	71	theme	breast	1721:1726	arg1	cancer					1728:1733	breast cancer	1721:1733	breast cancer	1721:1733	Therapeutic strategies aimed at altering cellular O-GlcNAc levels may have profound effects on PR transcriptional activity in breast cancer.
28929346	1	72	theme	cancer	161:166	arg1	development					139:149	the development	135:149	the development of breast cancer	135:166	Emerging clinical trial data implicate progestins in the development of breast cancer.
28929346	6	73	theme	O-GlcNAcylated	972:985	arg1	PR					987:988	O-GlcNAcylated PR	972:988	O-GlcNAcylated PR	972:988	Moreover, we show that O-GlcNAcylated PR is more transcriptionally active on PR-target genes, despite the observation that PR messenger RNA and protein levels are decreased when O-GlcNAc levels are high.
19944066	6	0	theme	diabetes	733:740	arg1	mellitus					742:749	diabetes mellitus	733:749	diabetes mellitus	733:749	Our findings suggest a crucial role for GPX1 and its O-GlcNAc modification in hyperglycemia and diabetes mellitus.
19944066	1	1	theme	cell	171:174	arg1	survival					176:183	cell survival	171:183	cell survival during oxidative stress	171:207	Hyperglycemia induces activation of glutathione peroxidase 1 (GPX1), an anti-oxidant enzyme essential for cell survival during oxidative stress.
19944066	5	2	theme	mouse	624:628	arg1	liver					630:634	the mouse liver	620:634	the mouse liver	620:634	We also demonstrate that pharmacological injection of the O-GlcNAcase inhibitor NTZ induces GPX1 activation in the mouse liver.
19944066	1	3	theme	glutathione	101:111	arg1	peroxidase					113:122	glutathione peroxidase 1	101:124	glutathione peroxidase 1 (GPX1)	101:131	Hyperglycemia induces activation of glutathione peroxidase 1 (GPX1), an anti-oxidant enzyme essential for cell survival during oxidative stress.
19944066	1	3	theme	glutathione	101:111	arg1	GPX1					127:130	GPX1	127:130	GPX1	127:130	Hyperglycemia induces activation of glutathione peroxidase 1 (GPX1), an anti-oxidant enzyme essential for cell survival during oxidative stress.
19944066	1	3	theme	glutathione	101:111	arg1	enzyme					150:155	an anti-oxidant enzyme	134:155	an anti-oxidant enzyme essential for cell survival during oxidative stress	134:207	Hyperglycemia induces activation of glutathione peroxidase 1 (GPX1), an anti-oxidant enzyme essential for cell survival during oxidative stress.
19944066	5	4	theme	NTZ	589:591	arg1	injection					550:558	pharmacological injection	534:558	pharmacological injection of the O-GlcNAcase inhibitor NTZ	534:591	We also demonstrate that pharmacological injection of the O-GlcNAcase inhibitor NTZ induces GPX1 activation in the mouse liver.
19944066	1	5	theme	peroxidase	113:122	arg1	activation					87:96	activation	87:96	activation of glutathione peroxidase 1 (GPX1), an anti-oxidant enzyme essential for cell survival during oxidative stress	87:207	Hyperglycemia induces activation of glutathione peroxidase 1 (GPX1), an anti-oxidant enzyme essential for cell survival during oxidative stress.
19944066	1	6	theme	oxidative	192:200	arg1	stress					202:207	oxidative stress	192:207	oxidative stress	192:207	Hyperglycemia induces activation of glutathione peroxidase 1 (GPX1), an anti-oxidant enzyme essential for cell survival during oxidative stress.
19944066	4	7	mod	modified	467:474	arg3	O-GlcNAc					481:488	O-GlcNAc	481:488	O-GlcNAc	481:488	GPX1 itself is modified with O-GlcNAc on its C-terminus.
19944066	4	7	mod	modified	467:474	arg1	GPX1					452:455	GPX1 itself	452:462	GPX1 itself	452:462	GPX1 itself is modified with O-GlcNAc on its C-terminus.
19944066	3	8	dep	c-Abl	429:433	arg1	kinases					443:449	kinases	443:449	kinases	443:449	Here, we report that hyperglycemia-induced protein glycosylation by O-linked N-acetylglucosamine (O-GlcNAc) is crucial for activation of GPX1 and for its binding to c-Abl and Arg kinases.
19944066	5	9	theme	GPX1	601:604	arg1	activation					606:615	GPX1 activation	601:615	GPX1 activation	601:615	We also demonstrate that pharmacological injection of the O-GlcNAcase inhibitor NTZ induces GPX1 activation in the mouse liver.
19944066	6	10	theme	O-GlcNAc	690:697	arg1	modification					699:710	its O-GlcNAc modification	686:710	its O-GlcNAc modification	686:710	Our findings suggest a crucial role for GPX1 and its O-GlcNAc modification in hyperglycemia and diabetes mellitus.
19944066	0	11	theme	GPX1	48:51	arg1	activation					53:62	hyperglycemia-induced GPX1 activation	26:62	hyperglycemia-induced GPX1 activation	26:62	O-GlcNAcylation regulates hyperglycemia-induced GPX1 activation.
19944066	3	12	theme	GPX1	401:404	arg1	activation					387:396	activation	387:396	activation of GPX1	387:404	Here, we report that hyperglycemia-induced protein glycosylation by O-linked N-acetylglucosamine (O-GlcNAc) is crucial for activation of GPX1 and for its binding to c-Abl and Arg kinases.
19944066	3	13	theme	hyperglycemia-induced	285:305	arg1	glycosylation					315:327	hyperglycemia-induced protein glycosylation	285:327	hyperglycemia-induced protein glycosylation by O-linked N-acetylglucosamine (O-GlcNAc)	285:370	Here, we report that hyperglycemia-induced protein glycosylation by O-linked N-acetylglucosamine (O-GlcNAc) is crucial for activation of GPX1 and for its binding to c-Abl and Arg kinases.
19944066	2	14	theme	activation	241:250	arg1	unclear					255:261	unclear	255:261	unclear	255:261	However, the mechanism of GPX1 activation is unclear.
19944066	2	14	theme	activation	241:250	arg1	mechanism					223:231	the mechanism	219:231	the mechanism of GPX1 activation	219:250	However, the mechanism of GPX1 activation is unclear.
19944066	2	15	theme	GPX1	236:239	arg1	activation					241:250	GPX1 activation	236:250	GPX1 activation	236:250	However, the mechanism of GPX1 activation is unclear.
19944066	3	16	theme	O-linked	332:339	arg1	O-GlcNAc					362:369	O-GlcNAc	362:369	O-GlcNAc	362:369	Here, we report that hyperglycemia-induced protein glycosylation by O-linked N-acetylglucosamine (O-GlcNAc) is crucial for activation of GPX1 and for its binding to c-Abl and Arg kinases.
19944066	3	16	theme	O-linked	332:339	arg1	N-acetylglucosamine					341:359	O-linked N-acetylglucosamine	332:359	O-linked N-acetylglucosamine (O-GlcNAc)	332:370	Here, we report that hyperglycemia-induced protein glycosylation by O-linked N-acetylglucosamine (O-GlcNAc) is crucial for activation of GPX1 and for its binding to c-Abl and Arg kinases.
19944066	6	17	from	role	668:671	arg1	hyperglycemia					715:727	hyperglycemia	715:727	hyperglycemia	715:727	Our findings suggest a crucial role for GPX1 and its O-GlcNAc modification in hyperglycemia and diabetes mellitus.
19944066	6	17	from	role	668:671	arg1	mellitus					742:749	diabetes mellitus	733:749	diabetes mellitus	733:749	Our findings suggest a crucial role for GPX1 and its O-GlcNAc modification in hyperglycemia and diabetes mellitus.
19944066	5	18	theme	O-GlcNAcase	567:577	arg1	NTZ					589:591	the O-GlcNAcase inhibitor NTZ	563:591	the O-GlcNAcase inhibitor NTZ	563:591	We also demonstrate that pharmacological injection of the O-GlcNAcase inhibitor NTZ induces GPX1 activation in the mouse liver.
19944066	3	19	theme	protein	307:313	arg1	glycosylation					315:327	hyperglycemia-induced protein glycosylation	285:327	hyperglycemia-induced protein glycosylation by O-linked N-acetylglucosamine (O-GlcNAc)	285:370	Here, we report that hyperglycemia-induced protein glycosylation by O-linked N-acetylglucosamine (O-GlcNAc) is crucial for activation of GPX1 and for its binding to c-Abl and Arg kinases.
19944066	5	20	theme	inhibitor	579:587	arg1	NTZ					589:591	the O-GlcNAcase inhibitor NTZ	563:591	the O-GlcNAcase inhibitor NTZ	563:591	We also demonstrate that pharmacological injection of the O-GlcNAcase inhibitor NTZ induces GPX1 activation in the mouse liver.
19944066	1	21	theme	anti-oxidant	137:148	arg1	enzyme					150:155	an anti-oxidant enzyme	134:155	an anti-oxidant enzyme essential for cell survival during oxidative stress	134:207	Hyperglycemia induces activation of glutathione peroxidase 1 (GPX1), an anti-oxidant enzyme essential for cell survival during oxidative stress.
19944066	1	21	theme	anti-oxidant	137:148	arg1	peroxidase					113:122	glutathione peroxidase 1	101:124	glutathione peroxidase 1 (GPX1)	101:131	Hyperglycemia induces activation of glutathione peroxidase 1 (GPX1), an anti-oxidant enzyme essential for cell survival during oxidative stress.
19944066	3	22	link	O-linked	332:339	arg1	O-GlcNAc					362:369	O-GlcNAc	362:369	O-GlcNAc	362:369	Here, we report that hyperglycemia-induced protein glycosylation by O-linked N-acetylglucosamine (O-GlcNAc) is crucial for activation of GPX1 and for its binding to c-Abl and Arg kinases.
19944066	3	22	link	O-linked	332:339	arg1	N-acetylglucosamine					341:359	O-linked N-acetylglucosamine	332:359	O-linked N-acetylglucosamine (O-GlcNAc)	332:370	Here, we report that hyperglycemia-induced protein glycosylation by O-linked N-acetylglucosamine (O-GlcNAc) is crucial for activation of GPX1 and for its binding to c-Abl and Arg kinases.
19944066	6	23	theme	crucial	660:666	arg1	role					668:671	a crucial role	658:671	a crucial role for GPX1 and its O-GlcNAc modification in hyperglycemia and diabetes mellitus	658:749	Our findings suggest a crucial role for GPX1 and its O-GlcNAc modification in hyperglycemia and diabetes mellitus.
19944066	1	24	theme	essential	157:165	arg1	enzyme					150:155	an anti-oxidant enzyme	134:155	an anti-oxidant enzyme essential for cell survival during oxidative stress	134:207	Hyperglycemia induces activation of glutathione peroxidase 1 (GPX1), an anti-oxidant enzyme essential for cell survival during oxidative stress.
19944066	1	24	theme	essential	157:165	arg1	peroxidase					113:122	glutathione peroxidase 1	101:124	glutathione peroxidase 1 (GPX1)	101:131	Hyperglycemia induces activation of glutathione peroxidase 1 (GPX1), an anti-oxidant enzyme essential for cell survival during oxidative stress.
19944066	0	25	theme	hyperglycemia-induced	26:46	arg1	activation					53:62	hyperglycemia-induced GPX1 activation	26:62	hyperglycemia-induced GPX1 activation	26:62	O-GlcNAcylation regulates hyperglycemia-induced GPX1 activation.
19944066	5	26	theme	pharmacological	534:548	arg1	injection					550:558	pharmacological injection	534:558	pharmacological injection of the O-GlcNAcase inhibitor NTZ	534:591	We also demonstrate that pharmacological injection of the O-GlcNAcase inhibitor NTZ induces GPX1 activation in the mouse liver.
22403705	8	0	theme	CTD110.6	1104:1111	arg1	reactivity					1090:1099	reactivity	1090:1099	reactivity of CTD110.6 to EGF-like module 1	1090:1132	Analysis of tandem modules of TSP-1 localized reactivity of CTD110.6 to EGF-like module 1.
22403705	3	1	located	found	378:382	arg2	O-β-GlcNAc					362:371	O-β-GlcNAc	362:371	O-β-GlcNAc	362:371	Previously, O-β-N-acetylglucosamine (O-β-GlcNAc) was found on a threonine in the loop between the fifth and sixth cysteines of the 20(th) epidermal growth factor (EGF)-like module of Drosophila Notch.
22403705	3	1	located	found	378:382	arg1	threonine					389:397	a threonine	387:397	a threonine in the loop between the fifth and sixth cysteines of the 20(th) epidermal growth factor (EGF)-like module of Drosophila Notch	387:523	Previously, O-β-N-acetylglucosamine (O-β-GlcNAc) was found on a threonine in the loop between the fifth and sixth cysteines of the 20(th) epidermal growth factor (EGF)-like module of Drosophila Notch.
22403705	3	1	located	found	378:382	arg2	O-β-N-acetylglucosamine					337:359	O-β-N-acetylglucosamine	337:359	O-β-N-acetylglucosamine (O-β-GlcNAc)	337:372	Previously, O-β-N-acetylglucosamine (O-β-GlcNAc) was found on a threonine in the loop between the fifth and sixth cysteines of the 20(th) epidermal growth factor (EGF)-like module of Drosophila Notch.
22403705	2	2	dep	fourth	286:291	arg1	O-β-N-acetylglucosaminylation					294:322	O-β-N-acetylglucosaminylation	294:322	a fourth: O-β-N-acetylglucosaminylation	284:322	We now describe a fourth: O-β-N-acetylglucosaminylation.
22403705	8	3	theme	modules	1063:1069	arg1	Analysis					1044:1051	Analysis	1044:1051	Analysis of tandem modules of TSP-1	1044:1078	Analysis of tandem modules of TSP-1 localized reactivity of CTD110.6 to EGF-like module 1.
22403705	0	4	theme	extracellular	65:77	arg1	protein					79:85	an animal extracellular protein	55:85	an animal extracellular protein	55:85	Modification of EGF-like module 1 of thrombospondin-1, an animal extracellular protein, by O-linked N-acetylglucosamine.
22403705	0	4	theme	extracellular	65:77	arg1	thrombospondin-1					37:52	thrombospondin-1	37:52	thrombospondin-1	37:52	Modification of EGF-like module 1 of thrombospondin-1, an animal extracellular protein, by O-linked N-acetylglucosamine.
22403705	6	5	theme	Antibody	853:860	arg1	reactivity					862:871	Antibody reactivity	853:871	Antibody reactivity	853:871	Antibody reactivity was diminished by treatment of TSP-1 with β-N-acetylhexosaminidase.
22403705	10	6	theme	+203-Da	1393:1399	arg1	modification					1401:1412	the +203-Da modification	1389:1412	the +203-Da modification	1389:1412	Mass spectrometric sequence analysis localized the +203-Da modification to Ser580 in the sequence (575)CPPGYSGNGIQC(586).
22403705	5	7	theme	anti-O-GlcNAc	829:841	arg1	antibody					843:850	the CTD110.6 anti-O-GlcNAc antibody	816:850	the CTD110.6 anti-O-GlcNAc antibody	816:850	TSP-1, which has a potentially modifiable serine in the loop, reacted in immuno-blots with the CTD110.6 anti-O-GlcNAc antibody.
22403705	8	8	theme	EGF-like	1116:1123	arg1	module					1125:1130	EGF-like module 1	1116:1132	EGF-like module 1	1116:1132	Analysis of tandem modules of TSP-1 localized reactivity of CTD110.6 to EGF-like module 1.
22403705	10	9	theme	sequence	1361:1368	arg1	analysis					1370:1377	Mass spectrometric sequence analysis	1342:1377	Mass spectrometric sequence analysis	1342:1377	Mass spectrometric sequence analysis localized the +203-Da modification to Ser580 in the sequence (575)CPPGYSGNGIQC(586).
22403705	9	10	theme	Top-down	1135:1142	arg1	analysis					1163:1170	Top-down mass spectrometric analysis	1135:1170	Top-down mass spectrometric analysis of EGF-like module 1	1135:1191	Top-down mass spectrometric analysis of EGF-like module 1 demonstrated the expected modifications with glucose (+162 Da) and xylose (+132 Da) separately from modification with N-acetyl hexosamine (+203 Da).
22403705	3	11	theme	Drosophila	508:517	arg1	Notch					519:523	Drosophila Notch	508:523	Drosophila Notch	508:523	Previously, O-β-N-acetylglucosamine (O-β-GlcNAc) was found on a threonine in the loop between the fifth and sixth cysteines of the 20(th) epidermal growth factor (EGF)-like module of Drosophila Notch.
22403705	6	12	with	treatment	891:899	arg1	β-N-acetylhexosaminidase					915:938	β-N-acetylhexosaminidase	915:938	β-N-acetylhexosaminidase	915:938	Antibody reactivity was diminished by treatment of TSP-1 with β-N-acetylhexosaminidase.
22403705	4	13	theme	Drosophila	554:563	arg1	sequence					576:583	the Drosophila Notch loop sequence	550:583	the Drosophila Notch loop sequence	550:583	A BLAST search based on the Drosophila Notch loop sequence identified a number of human EGF-like modules that contain a similar sequence, including EGF-like module 1 of TSP-1 and its homolog, TSP-2.
22403705	4	14	theme	homolog	709:715	arg1	module					683:688	EGF-like module 1	674:690	EGF-like module 1 of TSP-1 and its homolog, TSP-2	674:722	A BLAST search based on the Drosophila Notch loop sequence identified a number of human EGF-like modules that contain a similar sequence, including EGF-like module 1 of TSP-1 and its homolog, TSP-2.
22403705	9	15	theme	mass	1144:1147	arg1	analysis					1163:1170	Top-down mass spectrometric analysis	1135:1170	Top-down mass spectrometric analysis of EGF-like module 1	1135:1191	Top-down mass spectrometric analysis of EGF-like module 1 demonstrated the expected modifications with glucose (+162 Da) and xylose (+132 Da) separately from modification with N-acetyl hexosamine (+203 Da).
22403705	3	16	theme	Notch	519:523	arg1	module					498:503	the 20(th) epidermal growth factor (EGF)-like module	452:503	the 20(th) epidermal growth factor (EGF)-like module of Drosophila Notch	452:523	Previously, O-β-N-acetylglucosamine (O-β-GlcNAc) was found on a threonine in the loop between the fifth and sixth cysteines of the 20(th) epidermal growth factor (EGF)-like module of Drosophila Notch.
22403705	3	17	from	threonine	389:397	arg1	loop					406:409	the loop	402:409	the loop between the fifth and sixth cysteines of the 20(th) epidermal growth factor (EGF)-like module of Drosophila Notch	402:523	Previously, O-β-N-acetylglucosamine (O-β-GlcNAc) was found on a threonine in the loop between the fifth and sixth cysteines of the 20(th) epidermal growth factor (EGF)-like module of Drosophila Notch.
22403705	9	18	theme	spectrometric	1149:1161	arg1	analysis					1163:1170	Top-down mass spectrometric analysis	1135:1170	Top-down mass spectrometric analysis of EGF-like module 1	1135:1191	Top-down mass spectrometric analysis of EGF-like module 1 demonstrated the expected modifications with glucose (+162 Da) and xylose (+132 Da) separately from modification with N-acetyl hexosamine (+203 Da).
22403705	3	19	theme	module	498:503	arg1	cysteines					439:447	the fifth and sixth cysteines	419:447	the fifth and sixth cysteines of the 20(th) epidermal growth factor (EGF)-like module of Drosophila Notch	419:523	Previously, O-β-N-acetylglucosamine (O-β-GlcNAc) was found on a threonine in the loop between the fifth and sixth cysteines of the 20(th) epidermal growth factor (EGF)-like module of Drosophila Notch.
22403705	4	20	theme	modules	623:629	arg1	number					598:603	a number	596:603	a number of human EGF-like modules that contain a similar sequence, including EGF-like module 1 of TSP-1 and its homolog, TSP-2	596:722	A BLAST search based on the Drosophila Notch loop sequence identified a number of human EGF-like modules that contain a similar sequence, including EGF-like module 1 of TSP-1 and its homolog, TSP-2.
22403705	0	21	theme	O-linked	91:98	arg1	N-acetylglucosamine					100:118	O-linked N-acetylglucosamine	91:118	O-linked N-acetylglucosamine	91:118	Modification of EGF-like module 1 of thrombospondin-1, an animal extracellular protein, by O-linked N-acetylglucosamine.
22403705	11	22	theme	surface	1596:1602	arg1	proteins					1604:1611	cell surface proteins	1591:1611	cell surface proteins	1591:1611	These results demonstrate that O-β-N-acetylglucosaminylation can occur on secreted extracellular matrix proteins as well as on cell surface proteins.
22403705	4	23	theme	TSP-2	718:722	arg1	module					683:688	EGF-like module 1	674:690	EGF-like module 1 of TSP-1 and its homolog, TSP-2	674:722	A BLAST search based on the Drosophila Notch loop sequence identified a number of human EGF-like modules that contain a similar sequence, including EGF-like module 1 of TSP-1 and its homolog, TSP-2.
22403705	4	24	theme	EGF-like	614:621	arg1	modules					623:629	human EGF-like modules	608:629	human EGF-like modules that contain a similar sequence, including EGF-like module 1 of TSP-1 and its homolog, TSP-2	608:722	A BLAST search based on the Drosophila Notch loop sequence identified a number of human EGF-like modules that contain a similar sequence, including EGF-like module 1 of TSP-1 and its homolog, TSP-2.
22403705	6	25	theme	TSP-1	904:908	arg1	treatment					891:899	treatment	891:899	treatment of TSP-1 with β-N-acetylhexosaminidase	891:938	Antibody reactivity was diminished by treatment of TSP-1 with β-N-acetylhexosaminidase.
22403705	9	26	with	modification	1293:1304	arg1	hexosamine					1320:1329	N-acetyl hexosamine	1311:1329	N-acetyl hexosamine (+203 Da)	1311:1339	Top-down mass spectrometric analysis of EGF-like module 1 demonstrated the expected modifications with glucose (+162 Da) and xylose (+132 Da) separately from modification with N-acetyl hexosamine (+203 Da).
22403705	9	26	with	modification	1293:1304	arg1	Da					1337:1338	+203 Da	1332:1338	+203 Da	1332:1338	Top-down mass spectrometric analysis of EGF-like module 1 demonstrated the expected modifications with glucose (+162 Da) and xylose (+132 Da) separately from modification with N-acetyl hexosamine (+203 Da).
22403705	4	27	theme	TSP-1	695:699	arg1	module					683:688	EGF-like module 1	674:690	EGF-like module 1 of TSP-1 and its homolog, TSP-2	674:722	A BLAST search based on the Drosophila Notch loop sequence identified a number of human EGF-like modules that contain a similar sequence, including EGF-like module 1 of TSP-1 and its homolog, TSP-2.
22403705	9	28	theme	EGF-like	1175:1182	arg1	module					1184:1189	EGF-like module 1	1175:1191	EGF-like module 1	1175:1191	Top-down mass spectrometric analysis of EGF-like module 1 demonstrated the expected modifications with glucose (+162 Da) and xylose (+132 Da) separately from modification with N-acetyl hexosamine (+203 Da).
22403705	3	29	theme	sixth	433:437	arg1	cysteines					439:447	the fifth and sixth cysteines	419:447	the fifth and sixth cysteines of the 20(th) epidermal growth factor (EGF)-like module of Drosophila Notch	419:523	Previously, O-β-N-acetylglucosamine (O-β-GlcNAc) was found on a threonine in the loop between the fifth and sixth cysteines of the 20(th) epidermal growth factor (EGF)-like module of Drosophila Notch.
22403705	0	30	theme	module	25:30	arg1	Modification					0:11	Modification	0:11	Modification of EGF-like module 1 of thrombospondin-1, an animal extracellular protein, by O-linked N-acetylglucosamine.	0:119	Modification of EGF-like module 1 of thrombospondin-1, an animal extracellular protein, by O-linked N-acetylglucosamine.
22403705	10	31	theme	spectrometric	1347:1359	arg1	analysis					1370:1377	Mass spectrometric sequence analysis	1342:1377	Mass spectrometric sequence analysis	1342:1377	Mass spectrometric sequence analysis localized the +203-Da modification to Ser580 in the sequence (575)CPPGYSGNGIQC(586).
22403705	9	32	theme	module	1184:1189	arg1	analysis					1163:1170	Top-down mass spectrometric analysis	1135:1170	Top-down mass spectrometric analysis of EGF-like module 1	1135:1191	Top-down mass spectrometric analysis of EGF-like module 1 demonstrated the expected modifications with glucose (+162 Da) and xylose (+132 Da) separately from modification with N-acetyl hexosamine (+203 Da).
22403705	1	33	theme	unusual	178:184	arg1	O-fucosylation					231:244	O-fucosylation	231:244	O-fucosylation	231:244	Thrombospondin-1 (TSP-1) is known to be subject to three unusual carbohydrate modifications: C-mannosylation, O-fucosylation, and O-glucosylation.
22403705	1	33	theme	unusual	178:184	arg1	O-glucosylation					251:265	O-glucosylation	251:265	O-glucosylation	251:265	Thrombospondin-1 (TSP-1) is known to be subject to three unusual carbohydrate modifications: C-mannosylation, O-fucosylation, and O-glucosylation.
22403705	1	33	theme	unusual	178:184	arg1	C-mannosylation					214:228	C-mannosylation	214:228	C-mannosylation	214:228	Thrombospondin-1 (TSP-1) is known to be subject to three unusual carbohydrate modifications: C-mannosylation, O-fucosylation, and O-glucosylation.
22403705	1	33	theme	unusual	178:184	arg1	modifications					199:211	three unusual carbohydrate modifications	172:211	three unusual carbohydrate modifications: C-mannosylation, O-fucosylation, and O-glucosylation	172:265	Thrombospondin-1 (TSP-1) is known to be subject to three unusual carbohydrate modifications: C-mannosylation, O-fucosylation, and O-glucosylation.
22403705	0	34	theme	EGF-like	16:23	arg1	module					25:30	EGF-like module 1	16:32	EGF-like module 1 of thrombospondin-1, an animal extracellular protein,	16:86	Modification of EGF-like module 1 of thrombospondin-1, an animal extracellular protein, by O-linked N-acetylglucosamine.
22403705	3	35	dep	-like	492:496	arg1	factor					480:485	epidermal growth factor	463:485	epidermal growth factor	463:485	Previously, O-β-N-acetylglucosamine (O-β-GlcNAc) was found on a threonine in the loop between the fifth and sixth cysteines of the 20(th) epidermal growth factor (EGF)-like module of Drosophila Notch.
22403705	1	36	theme	carbohydrate	186:197	arg1	O-fucosylation					231:244	O-fucosylation	231:244	O-fucosylation	231:244	Thrombospondin-1 (TSP-1) is known to be subject to three unusual carbohydrate modifications: C-mannosylation, O-fucosylation, and O-glucosylation.
22403705	1	36	theme	carbohydrate	186:197	arg1	O-glucosylation					251:265	O-glucosylation	251:265	O-glucosylation	251:265	Thrombospondin-1 (TSP-1) is known to be subject to three unusual carbohydrate modifications: C-mannosylation, O-fucosylation, and O-glucosylation.
22403705	1	36	theme	carbohydrate	186:197	arg1	C-mannosylation					214:228	C-mannosylation	214:228	C-mannosylation	214:228	Thrombospondin-1 (TSP-1) is known to be subject to three unusual carbohydrate modifications: C-mannosylation, O-fucosylation, and O-glucosylation.
22403705	1	36	theme	carbohydrate	186:197	arg1	modifications					199:211	three unusual carbohydrate modifications	172:211	three unusual carbohydrate modifications: C-mannosylation, O-fucosylation, and O-glucosylation	172:265	Thrombospondin-1 (TSP-1) is known to be subject to three unusual carbohydrate modifications: C-mannosylation, O-fucosylation, and O-glucosylation.
22403705	4	37	theme	BLAST	528:532	arg1	search					534:539	A BLAST search	526:539	A BLAST search based on the Drosophila Notch loop sequence	526:583	A BLAST search based on the Drosophila Notch loop sequence identified a number of human EGF-like modules that contain a similar sequence, including EGF-like module 1 of TSP-1 and its homolog, TSP-2.
22403705	4	38	theme	human	608:612	arg1	modules					623:629	human EGF-like modules	608:629	human EGF-like modules that contain a similar sequence, including EGF-like module 1 of TSP-1 and its homolog, TSP-2	608:722	A BLAST search based on the Drosophila Notch loop sequence identified a number of human EGF-like modules that contain a similar sequence, including EGF-like module 1 of TSP-1 and its homolog, TSP-2.
22403705	3	39	theme	fifth	423:427	arg1	cysteines					439:447	the fifth and sixth cysteines	419:447	the fifth and sixth cysteines of the 20(th) epidermal growth factor (EGF)-like module of Drosophila Notch	419:523	Previously, O-β-N-acetylglucosamine (O-β-GlcNAc) was found on a threonine in the loop between the fifth and sixth cysteines of the 20(th) epidermal growth factor (EGF)-like module of Drosophila Notch.
22403705	10	40	theme	sequence	1431:1438	arg1	CPPGYSGNGIQC					1445:1456	the sequence (575)CPPGYSGNGIQC(586)	1427:1461	the sequence (575)CPPGYSGNGIQC(586)	1427:1461	Mass spectrometric sequence analysis localized the +203-Da modification to Ser580 in the sequence (575)CPPGYSGNGIQC(586).
22403705	11	41	theme	cell	1591:1594	arg1	proteins					1604:1611	cell surface proteins	1591:1611	cell surface proteins	1591:1611	These results demonstrate that O-β-N-acetylglucosaminylation can occur on secreted extracellular matrix proteins as well as on cell surface proteins.
22403705	5	42	theme	modifiable	756:765	arg1	serine					767:772	a potentially modifiable serine	742:772	a potentially modifiable serine	742:772	TSP-1, which has a potentially modifiable serine in the loop, reacted in immuno-blots with the CTD110.6 anti-O-GlcNAc antibody.
22403705	7	43	theme	modifiable	974:983	arg1	serine/threonine					985:1000	a potentially modifiable serine/threonine	960:1000	a potentially modifiable serine/threonine in the loop	960:1012	TSP-2, which lacks a potentially modifiable serine/threonine in the loop, did not react with CTD110.6.
22403705	7	44	from	serine/threonine	985:1000	arg1	loop					1009:1012	the loop	1005:1012	the loop	1005:1012	TSP-2, which lacks a potentially modifiable serine/threonine in the loop, did not react with CTD110.6.
22403705	9	45	theme	N-acetyl	1311:1318	arg1	hexosamine					1320:1329	N-acetyl hexosamine	1311:1329	N-acetyl hexosamine (+203 Da)	1311:1339	Top-down mass spectrometric analysis of EGF-like module 1 demonstrated the expected modifications with glucose (+162 Da) and xylose (+132 Da) separately from modification with N-acetyl hexosamine (+203 Da).
22403705	9	45	theme	N-acetyl	1311:1318	arg1	Da					1337:1338	+203 Da	1332:1338	+203 Da	1332:1338	Top-down mass spectrometric analysis of EGF-like module 1 demonstrated the expected modifications with glucose (+162 Da) and xylose (+132 Da) separately from modification with N-acetyl hexosamine (+203 Da).
22403705	5	46	with	immuno-blots	798:809	arg1	antibody					843:850	the CTD110.6 anti-O-GlcNAc antibody	816:850	the CTD110.6 anti-O-GlcNAc antibody	816:850	TSP-1, which has a potentially modifiable serine in the loop, reacted in immuno-blots with the CTD110.6 anti-O-GlcNAc antibody.
22403705	9	47	theme	expected	1210:1217	arg1	modifications					1219:1231	the expected modifications	1206:1231	the expected modifications	1206:1231	Top-down mass spectrometric analysis of EGF-like module 1 demonstrated the expected modifications with glucose (+162 Da) and xylose (+132 Da) separately from modification with N-acetyl hexosamine (+203 Da).
22403705	8	48	theme	TSP-1	1074:1078	arg1	modules					1063:1069	tandem modules	1056:1069	tandem modules of TSP-1	1056:1078	Analysis of tandem modules of TSP-1 localized reactivity of CTD110.6 to EGF-like module 1.
22403705	3	49	theme	growth	473:478	arg1	factor					480:485	epidermal growth factor	463:485	epidermal growth factor	463:485	Previously, O-β-N-acetylglucosamine (O-β-GlcNAc) was found on a threonine in the loop between the fifth and sixth cysteines of the 20(th) epidermal growth factor (EGF)-like module of Drosophila Notch.
22403705	0	50	theme	thrombospondin-1	37:52	arg1	module					25:30	EGF-like module 1	16:32	EGF-like module 1 of thrombospondin-1, an animal extracellular protein,	16:86	Modification of EGF-like module 1 of thrombospondin-1, an animal extracellular protein, by O-linked N-acetylglucosamine.
22403705	8	51	theme	tandem	1056:1061	arg1	modules					1063:1069	tandem modules	1056:1069	tandem modules of TSP-1	1056:1078	Analysis of tandem modules of TSP-1 localized reactivity of CTD110.6 to EGF-like module 1.
22403705	5	52	contain	has	738:740	arg2	serine					767:772	a potentially modifiable serine	742:772	a potentially modifiable serine	742:772	TSP-1, which has a potentially modifiable serine in the loop, reacted in immuno-blots with the CTD110.6 anti-O-GlcNAc antibody.
22403705	5	52	contain	has	738:740	arg1	TSP-1					725:729	TSP-1	725:729	TSP-1	725:729	TSP-1, which has a potentially modifiable serine in the loop, reacted in immuno-blots with the CTD110.6 anti-O-GlcNAc antibody.
22403705	10	53	theme	Mass	1342:1345	arg1	analysis					1370:1377	Mass spectrometric sequence analysis	1342:1377	Mass spectrometric sequence analysis	1342:1377	Mass spectrometric sequence analysis localized the +203-Da modification to Ser580 in the sequence (575)CPPGYSGNGIQC(586).
22403705	4	54	theme	EGF-like	674:681	arg1	module					683:688	EGF-like module 1	674:690	EGF-like module 1 of TSP-1 and its homolog, TSP-2	674:722	A BLAST search based on the Drosophila Notch loop sequence identified a number of human EGF-like modules that contain a similar sequence, including EGF-like module 1 of TSP-1 and its homolog, TSP-2.
22403705	4	55	contain	contain	636:642	arg1	modules					623:629	human EGF-like modules	608:629	human EGF-like modules that contain a similar sequence, including EGF-like module 1 of TSP-1 and its homolog, TSP-2	608:722	A BLAST search based on the Drosophila Notch loop sequence identified a number of human EGF-like modules that contain a similar sequence, including EGF-like module 1 of TSP-1 and its homolog, TSP-2.
22403705	4	55	contain	contain	636:642	arg2	sequence					654:661	a similar sequence	644:661	a similar sequence	644:661	A BLAST search based on the Drosophila Notch loop sequence identified a number of human EGF-like modules that contain a similar sequence, including EGF-like module 1 of TSP-1 and its homolog, TSP-2.
22403705	1	56	dep	modifications	199:211	arg1	O-fucosylation					231:244	O-fucosylation	231:244	O-fucosylation	231:244	Thrombospondin-1 (TSP-1) is known to be subject to three unusual carbohydrate modifications: C-mannosylation, O-fucosylation, and O-glucosylation.
22403705	1	56	dep	modifications	199:211	arg1	O-glucosylation					251:265	O-glucosylation	251:265	O-glucosylation	251:265	Thrombospondin-1 (TSP-1) is known to be subject to three unusual carbohydrate modifications: C-mannosylation, O-fucosylation, and O-glucosylation.
22403705	1	56	dep	modifications	199:211	arg1	C-mannosylation					214:228	C-mannosylation	214:228	C-mannosylation	214:228	Thrombospondin-1 (TSP-1) is known to be subject to three unusual carbohydrate modifications: C-mannosylation, O-fucosylation, and O-glucosylation.
22403705	1	56	dep	modifications	199:211	arg1	modifications					199:211	three unusual carbohydrate modifications	172:211	three unusual carbohydrate modifications: C-mannosylation, O-fucosylation, and O-glucosylation	172:265	Thrombospondin-1 (TSP-1) is known to be subject to three unusual carbohydrate modifications: C-mannosylation, O-fucosylation, and O-glucosylation.
22403705	11	57	theme	secreted	1538:1545	arg1	proteins					1568:1575	secreted extracellular matrix proteins	1538:1575	secreted extracellular matrix proteins	1538:1575	These results demonstrate that O-β-N-acetylglucosaminylation can occur on secreted extracellular matrix proteins as well as on cell surface proteins.
22403705	4	58	theme	loop	571:574	arg1	sequence					576:583	the Drosophila Notch loop sequence	550:583	the Drosophila Notch loop sequence	550:583	A BLAST search based on the Drosophila Notch loop sequence identified a number of human EGF-like modules that contain a similar sequence, including EGF-like module 1 of TSP-1 and its homolog, TSP-2.
22403705	11	59	theme	extracellular	1547:1559	arg1	proteins					1568:1575	secreted extracellular matrix proteins	1538:1575	secreted extracellular matrix proteins	1538:1575	These results demonstrate that O-β-N-acetylglucosaminylation can occur on secreted extracellular matrix proteins as well as on cell surface proteins.
22403705	3	60	theme	epidermal	463:471	arg1	factor					480:485	epidermal growth factor	463:485	epidermal growth factor	463:485	Previously, O-β-N-acetylglucosamine (O-β-GlcNAc) was found on a threonine in the loop between the fifth and sixth cysteines of the 20(th) epidermal growth factor (EGF)-like module of Drosophila Notch.
22403705	4	61	theme	Notch	565:569	arg1	sequence					576:583	the Drosophila Notch loop sequence	550:583	the Drosophila Notch loop sequence	550:583	A BLAST search based on the Drosophila Notch loop sequence identified a number of human EGF-like modules that contain a similar sequence, including EGF-like module 1 of TSP-1 and its homolog, TSP-2.
22403705	0	62	theme	animal	58:63	arg1	protein					79:85	an animal extracellular protein	55:85	an animal extracellular protein	55:85	Modification of EGF-like module 1 of thrombospondin-1, an animal extracellular protein, by O-linked N-acetylglucosamine.
22403705	0	62	theme	animal	58:63	arg1	thrombospondin-1					37:52	thrombospondin-1	37:52	thrombospondin-1	37:52	Modification of EGF-like module 1 of thrombospondin-1, an animal extracellular protein, by O-linked N-acetylglucosamine.
22403705	0	63	link	O-linked	91:98	arg1	N-acetylglucosamine					100:118	O-linked N-acetylglucosamine	91:118	O-linked N-acetylglucosamine	91:118	Modification of EGF-like module 1 of thrombospondin-1, an animal extracellular protein, by O-linked N-acetylglucosamine.
22403705	4	64	theme	similar	646:652	arg1	sequence					654:661	a similar sequence	644:661	a similar sequence	644:661	A BLAST search based on the Drosophila Notch loop sequence identified a number of human EGF-like modules that contain a similar sequence, including EGF-like module 1 of TSP-1 and its homolog, TSP-2.
22403705	11	65	theme	matrix	1561:1566	arg1	proteins					1568:1575	secreted extracellular matrix proteins	1538:1575	secreted extracellular matrix proteins	1538:1575	These results demonstrate that O-β-N-acetylglucosaminylation can occur on secreted extracellular matrix proteins as well as on cell surface proteins.
22403705	3	66	theme	-like	492:496	arg1	module					498:503	the 20(th) epidermal growth factor (EGF)-like module	452:503	the 20(th) epidermal growth factor (EGF)-like module of Drosophila Notch	452:523	Previously, O-β-N-acetylglucosamine (O-β-GlcNAc) was found on a threonine in the loop between the fifth and sixth cysteines of the 20(th) epidermal growth factor (EGF)-like module of Drosophila Notch.
24129563	0	0	from	death	24:28	arg1	cancer					44:49	pancreatic cancer	33:49	pancreatic cancer	33:49	Triptolide-induced cell death in pancreatic cancer is mediated by O-GlcNAc modification of transcription factor Sp1.
24129563	1	1	theme	prevalent	152:160	arg1	cause					177:181	the fourth most prevalent cancer-related cause	136:181	the fourth most prevalent cancer-related cause of death in the United States	136:211	Pancreatic cancer, the fourth most prevalent cancer-related cause of death in the United States, is a disease with a dismal survival rate of 5% 5 years after diagnosis.
24129563	1	1	theme	prevalent	152:160	arg1	cancer					128:133	Pancreatic cancer	117:133	Pancreatic cancer	117:133	Pancreatic cancer, the fourth most prevalent cancer-related cause of death in the United States, is a disease with a dismal survival rate of 5% 5 years after diagnosis.
24129563	3	2	from	expression	489:498	arg1	cells					537:541	pancreatic cancer cells	519:541	pancreatic cancer cells	519:541	A naturally derived compound, triptolide, and its water-soluble prodrug, Minnelide, down-regulate the expression of this protein in pancreatic cancer cells, thereby causing cell death.
24129563	0	3	mod	modification	75:86	arg3	O-GlcNAc					66:73	O-GlcNAc modification	66:86	O-GlcNAc modification of transcription factor Sp1	66:114	Triptolide-induced cell death in pancreatic cancer is mediated by O-GlcNAc modification of transcription factor Sp1.
24129563	0	3	mod	modification	75:86	arg1	Sp1					112:114	transcription factor Sp1	91:114	transcription factor Sp1	91:114	Triptolide-induced cell death in pancreatic cancer is mediated by O-GlcNAc modification of transcription factor Sp1.
24129563	6	4	theme	hexosamine	878:887	arg1	pathway					902:908	the hexosamine biosynthesis pathway	874:908	the hexosamine biosynthesis pathway	874:908	We further show that triptolide inhibits glycosylation of Sp1, inhibiting the hexosamine biosynthesis pathway, particularly the enzyme O-GlcNAc transferase.
24129563	6	4	theme	hexosamine	878:887	arg1	transferase					944:954	the enzyme O-GlcNAc transferase	924:954	particularly the enzyme O-GlcNAc transferase	911:954	We further show that triptolide inhibits glycosylation of Sp1, inhibiting the hexosamine biosynthesis pathway, particularly the enzyme O-GlcNAc transferase.
24129563	1	5	theme	cancer-related	162:175	arg1	cause					177:181	the fourth most prevalent cancer-related cause	136:181	the fourth most prevalent cancer-related cause of death in the United States	136:211	Pancreatic cancer, the fourth most prevalent cancer-related cause of death in the United States, is a disease with a dismal survival rate of 5% 5 years after diagnosis.
24129563	1	5	theme	cancer-related	162:175	arg1	cancer					128:133	Pancreatic cancer	117:133	Pancreatic cancer	117:133	Pancreatic cancer, the fourth most prevalent cancer-related cause of death in the United States, is a disease with a dismal survival rate of 5% 5 years after diagnosis.
24129563	1	6	theme	dismal	234:239	arg1	rate					250:253	a dismal survival rate	232:253	a dismal survival rate of 5% 5 years after diagnosis	232:283	Pancreatic cancer, the fourth most prevalent cancer-related cause of death in the United States, is a disease with a dismal survival rate of 5% 5 years after diagnosis.
24129563	0	7	theme	factor	105:110	arg1	Sp1					112:114	transcription factor Sp1	91:114	transcription factor Sp1	91:114	Triptolide-induced cell death in pancreatic cancer is mediated by O-GlcNAc modification of transcription factor Sp1.
24129563	5	8	from	decrease	741:748	arg1	glycosylation					753:765	glycosylation	753:765	glycosylation of the transcription factor Sp1	753:797	Our study shows that triptolide-induced down-regulation of HSP70 expression is associated with a decrease in glycosylation of the transcription factor Sp1.
24129563	7	9	theme	O-GlcNAc	971:978	arg1	transferase					980:990	O-GlcNAc transferase	971:990	O-GlcNAc transferase	971:990	Inhibition of O-GlcNAc transferase prevents nuclear localization of Sp1 and affects its DNA binding activity.
24129563	1	10	theme	survival	241:248	arg1	rate					250:253	a dismal survival rate	232:253	a dismal survival rate of 5% 5 years after diagnosis	232:283	Pancreatic cancer, the fourth most prevalent cancer-related cause of death in the United States, is a disease with a dismal survival rate of 5% 5 years after diagnosis.
24129563	0	11	theme	transcription	91:103	arg1	Sp1					112:114	transcription factor Sp1	91:114	transcription factor Sp1	91:114	Triptolide-induced cell death in pancreatic cancer is mediated by O-GlcNAc modification of transcription factor Sp1.
24129563	9	12	theme	Sp1	1285:1287	arg1	glycosylation					1268:1280	glycosylation	1268:1280	glycosylation	1268:1280	In this study, we evaluated the mechanism by which triptolide affects glycosylation of Sp1, which in turn affects downstream pathways controlling survival of pancreatic cancer cells.
24129563	2	13	theme	responsible	315:325	arg1	proteins					306:313	the survival proteins	293:313	the survival proteins responsible for its extraordinary ability to evade cell death	293:375	One of the survival proteins responsible for its extraordinary ability to evade cell death is HSP70.
24129563	8	14	theme	HSP70	1162:1166	arg1	inhibition					1139:1148	inhibition	1139:1148	inhibition of HSF1 and HSP70	1139:1166	This in turn down-regulates prosurvival pathways like NF-κB, leading to inhibition of HSF1 and HSP70 and eventually to cell death.
24129563	2	15	theme	survival	297:304	arg1	proteins					306:313	the survival proteins	293:313	the survival proteins responsible for its extraordinary ability to evade cell death	293:375	One of the survival proteins responsible for its extraordinary ability to evade cell death is HSP70.
24129563	0	16	theme	Sp1	112:114	arg1	modification					75:86	O-GlcNAc modification	66:86	O-GlcNAc modification of transcription factor Sp1	66:114	Triptolide-induced cell death in pancreatic cancer is mediated by O-GlcNAc modification of transcription factor Sp1.
24129563	1	17	dep	years	263:267	arg1	diagnosis					275:283	diagnosis	275:283	diagnosis	275:283	Pancreatic cancer, the fourth most prevalent cancer-related cause of death in the United States, is a disease with a dismal survival rate of 5% 5 years after diagnosis.
24129563	3	18	theme	water-soluble	437:449	arg1	Minnelide					460:468	Minnelide	460:468	Minnelide	460:468	A naturally derived compound, triptolide, and its water-soluble prodrug, Minnelide, down-regulate the expression of this protein in pancreatic cancer cells, thereby causing cell death.
24129563	3	18	theme	water-soluble	437:449	arg1	prodrug					451:457	its water-soluble prodrug	433:457	its water-soluble prodrug	433:457	A naturally derived compound, triptolide, and its water-soluble prodrug, Minnelide, down-regulate the expression of this protein in pancreatic cancer cells, thereby causing cell death.
24129563	3	19	theme	derived	399:405	arg1	triptolide					417:426	triptolide	417:426	triptolide	417:426	A naturally derived compound, triptolide, and its water-soluble prodrug, Minnelide, down-regulate the expression of this protein in pancreatic cancer cells, thereby causing cell death.
24129563	3	19	theme	derived	399:405	arg1	compound					407:414	A naturally derived compound	387:414	A naturally derived compound	387:414	A naturally derived compound, triptolide, and its water-soluble prodrug, Minnelide, down-regulate the expression of this protein in pancreatic cancer cells, thereby causing cell death.
24129563	0	20	theme	cell	19:22	arg1	death					24:28	Triptolide-induced cell death	0:28	Triptolide-induced cell death in pancreatic cancer	0:49	Triptolide-induced cell death in pancreatic cancer is mediated by O-GlcNAc modification of transcription factor Sp1.
24129563	5	21	theme	expression	709:718	arg1	down-regulation					684:698	triptolide-induced down-regulation	665:698	triptolide-induced down-regulation of HSP70 expression	665:718	Our study shows that triptolide-induced down-regulation of HSP70 expression is associated with a decrease in glycosylation of the transcription factor Sp1.
24129563	3	22	theme	pancreatic	519:528	arg1	cells					537:541	pancreatic cancer cells	519:541	pancreatic cancer cells	519:541	A naturally derived compound, triptolide, and its water-soluble prodrug, Minnelide, down-regulate the expression of this protein in pancreatic cancer cells, thereby causing cell death.
24129563	6	23	theme	Sp1	858:860	arg1	glycosylation					841:853	glycosylation	841:853	glycosylation of Sp1	841:860	We further show that triptolide inhibits glycosylation of Sp1, inhibiting the hexosamine biosynthesis pathway, particularly the enzyme O-GlcNAc transferase.
24129563	1	24	theme	death	186:190	arg1	cause					177:181	the fourth most prevalent cancer-related cause	136:181	the fourth most prevalent cancer-related cause of death in the United States	136:211	Pancreatic cancer, the fourth most prevalent cancer-related cause of death in the United States, is a disease with a dismal survival rate of 5% 5 years after diagnosis.
24129563	1	24	theme	death	186:190	arg1	cancer					128:133	Pancreatic cancer	117:133	Pancreatic cancer	117:133	Pancreatic cancer, the fourth most prevalent cancer-related cause of death in the United States, is a disease with a dismal survival rate of 5% 5 years after diagnosis.
24129563	0	25	theme	Triptolide-induced	0:17	arg1	death					24:28	Triptolide-induced cell death	0:28	Triptolide-induced cell death in pancreatic cancer	0:49	Triptolide-induced cell death in pancreatic cancer is mediated by O-GlcNAc modification of transcription factor Sp1.
24129563	3	26	link	derived	399:405	arg1	triptolide					417:426	triptolide	417:426	triptolide	417:426	A naturally derived compound, triptolide, and its water-soluble prodrug, Minnelide, down-regulate the expression of this protein in pancreatic cancer cells, thereby causing cell death.
24129563	3	26	link	derived	399:405	arg1	compound					407:414	A naturally derived compound	387:414	A naturally derived compound	387:414	A naturally derived compound, triptolide, and its water-soluble prodrug, Minnelide, down-regulate the expression of this protein in pancreatic cancer cells, thereby causing cell death.
24129563	3	27	theme	cancer	530:535	arg1	cells					537:541	pancreatic cancer cells	519:541	pancreatic cancer cells	519:541	A naturally derived compound, triptolide, and its water-soluble prodrug, Minnelide, down-regulate the expression of this protein in pancreatic cancer cells, thereby causing cell death.
24129563	2	28	theme	extraordinary	335:347	arg1	ability					349:355	its extraordinary ability to evade cell death	331:375	its extraordinary ability to evade cell death	331:375	One of the survival proteins responsible for its extraordinary ability to evade cell death is HSP70.
24129563	5	29	theme	transcription	774:786	arg1	Sp1					795:797	the transcription factor Sp1	770:797	the transcription factor Sp1	770:797	Our study shows that triptolide-induced down-regulation of HSP70 expression is associated with a decrease in glycosylation of the transcription factor Sp1.
24129563	5	30	gly	glycosylation	753:765	arg1	Sp1					795:797	the transcription factor Sp1	770:797	the transcription factor Sp1	770:797	Our study shows that triptolide-induced down-regulation of HSP70 expression is associated with a decrease in glycosylation of the transcription factor Sp1.
24129563	6	31	theme	O-GlcNAc	935:942	arg1	pathway					902:908	the hexosamine biosynthesis pathway	874:908	the hexosamine biosynthesis pathway	874:908	We further show that triptolide inhibits glycosylation of Sp1, inhibiting the hexosamine biosynthesis pathway, particularly the enzyme O-GlcNAc transferase.
24129563	6	31	theme	O-GlcNAc	935:942	arg1	transferase					944:954	the enzyme O-GlcNAc transferase	924:954	particularly the enzyme O-GlcNAc transferase	911:954	We further show that triptolide inhibits glycosylation of Sp1, inhibiting the hexosamine biosynthesis pathway, particularly the enzyme O-GlcNAc transferase.
24129563	3	32	theme	protein	508:514	arg1	expression					489:498	the expression	485:498	the expression of this protein in pancreatic cancer cells	485:541	A naturally derived compound, triptolide, and its water-soluble prodrug, Minnelide, down-regulate the expression of this protein in pancreatic cancer cells, thereby causing cell death.
24129563	5	33	theme	HSP70	703:707	arg1	expression					709:718	HSP70 expression	703:718	HSP70 expression	703:718	Our study shows that triptolide-induced down-regulation of HSP70 expression is associated with a decrease in glycosylation of the transcription factor Sp1.
24129563	5	34	theme	Sp1	795:797	arg1	glycosylation					753:765	glycosylation	753:765	glycosylation of the transcription factor Sp1	753:797	Our study shows that triptolide-induced down-regulation of HSP70 expression is associated with a decrease in glycosylation of the transcription factor Sp1.
24129563	5	35	theme	factor	788:793	arg1	Sp1					795:797	the transcription factor Sp1	770:797	the transcription factor Sp1	770:797	Our study shows that triptolide-induced down-regulation of HSP70 expression is associated with a decrease in glycosylation of the transcription factor Sp1.
24129563	1	36	theme	%	259:259	arg1	rate					250:253	a dismal survival rate	232:253	a dismal survival rate of 5% 5 years after diagnosis	232:283	Pancreatic cancer, the fourth most prevalent cancer-related cause of death in the United States, is a disease with a dismal survival rate of 5% 5 years after diagnosis.
24129563	2	37	theme	proteins	306:313	arg1	One					286:288	One	286:288	One	286:288	One of the survival proteins responsible for its extraordinary ability to evade cell death is HSP70.
24129563	2	37	theme	proteins	306:313	arg1	proteins					306:313	the survival proteins	293:313	the survival proteins responsible for its extraordinary ability to evade cell death	293:375	One of the survival proteins responsible for its extraordinary ability to evade cell death is HSP70.
24129563	1	38	theme	United	199:204	arg1	States					206:211	the United States	195:211	the United States	195:211	Pancreatic cancer, the fourth most prevalent cancer-related cause of death in the United States, is a disease with a dismal survival rate of 5% 5 years after diagnosis.
24129563	6	39	theme	enzyme	928:933	arg1	pathway					902:908	the hexosamine biosynthesis pathway	874:908	the hexosamine biosynthesis pathway	874:908	We further show that triptolide inhibits glycosylation of Sp1, inhibiting the hexosamine biosynthesis pathway, particularly the enzyme O-GlcNAc transferase.
24129563	6	39	theme	enzyme	928:933	arg1	transferase					944:954	the enzyme O-GlcNAc transferase	924:954	particularly the enzyme O-GlcNAc transferase	911:954	We further show that triptolide inhibits glycosylation of Sp1, inhibiting the hexosamine biosynthesis pathway, particularly the enzyme O-GlcNAc transferase.
24129563	7	40	theme	DNA	1045:1047	arg1	activity					1057:1064	its DNA binding activity	1041:1064	its DNA binding activity	1041:1064	Inhibition of O-GlcNAc transferase prevents nuclear localization of Sp1 and affects its DNA binding activity.
24129563	4	41	theme	triptolide	608:617	arg1	action					598:603	action	598:603	action of triptolide	598:617	However, the mechanism of action of triptolide has not been elucidated.
24129563	9	42	theme	downstream	1312:1321	arg1	pathways					1323:1330	downstream pathways	1312:1330	downstream pathways controlling survival of pancreatic cancer cells	1312:1378	In this study, we evaluated the mechanism by which triptolide affects glycosylation of Sp1, which in turn affects downstream pathways controlling survival of pancreatic cancer cells.
24129563	0	43	theme	pancreatic	33:42	arg1	cancer					44:49	pancreatic cancer	33:49	pancreatic cancer	33:49	Triptolide-induced cell death in pancreatic cancer is mediated by O-GlcNAc modification of transcription factor Sp1.
24129563	7	44	theme	binding	1049:1055	arg1	activity					1057:1064	its DNA binding activity	1041:1064	its DNA binding activity	1041:1064	Inhibition of O-GlcNAc transferase prevents nuclear localization of Sp1 and affects its DNA binding activity.
24129563	8	45	theme	cell	1186:1189	arg1	death					1191:1195	cell death	1186:1195	cell death	1186:1195	This in turn down-regulates prosurvival pathways like NF-κB, leading to inhibition of HSF1 and HSP70 and eventually to cell death.
24129563	2	46	theme	cell	366:369	arg1	death					371:375	cell death	366:375	cell death	366:375	One of the survival proteins responsible for its extraordinary ability to evade cell death is HSP70.
24129563	5	47	theme	triptolide-induced	665:682	arg1	down-regulation					684:698	triptolide-induced down-regulation	665:698	triptolide-induced down-regulation of HSP70 expression	665:718	Our study shows that triptolide-induced down-regulation of HSP70 expression is associated with a decrease in glycosylation of the transcription factor Sp1.
24129563	1	48	theme	Pancreatic	117:126	arg1	disease					219:225	a disease	217:225	a disease with a dismal survival rate of 5% 5 years after diagnosis	217:283	Pancreatic cancer, the fourth most prevalent cancer-related cause of death in the United States, is a disease with a dismal survival rate of 5% 5 years after diagnosis.
24129563	1	48	theme	Pancreatic	117:126	arg1	cause					177:181	the fourth most prevalent cancer-related cause	136:181	the fourth most prevalent cancer-related cause of death in the United States	136:211	Pancreatic cancer, the fourth most prevalent cancer-related cause of death in the United States, is a disease with a dismal survival rate of 5% 5 years after diagnosis.
24129563	1	48	theme	Pancreatic	117:126	arg1	cancer					128:133	Pancreatic cancer	117:133	Pancreatic cancer	117:133	Pancreatic cancer, the fourth most prevalent cancer-related cause of death in the United States, is a disease with a dismal survival rate of 5% 5 years after diagnosis.
24129563	8	49	theme	prosurvival	1095:1105	arg1	pathways					1107:1114	prosurvival pathways	1095:1114	prosurvival pathways	1095:1114	This in turn down-regulates prosurvival pathways like NF-κB, leading to inhibition of HSF1 and HSP70 and eventually to cell death.
24129563	9	50	theme	pancreatic	1356:1365	arg1	cells					1374:1378	pancreatic cancer cells	1356:1378	pancreatic cancer cells	1356:1378	In this study, we evaluated the mechanism by which triptolide affects glycosylation of Sp1, which in turn affects downstream pathways controlling survival of pancreatic cancer cells.
24129563	7	51	theme	Sp1	1025:1027	arg1	localization					1009:1020	nuclear localization	1001:1020	nuclear localization of Sp1	1001:1027	Inhibition of O-GlcNAc transferase prevents nuclear localization of Sp1 and affects its DNA binding activity.
24129563	7	52	theme	nuclear	1001:1007	arg1	localization					1009:1020	nuclear localization	1001:1020	nuclear localization of Sp1	1001:1027	Inhibition of O-GlcNAc transferase prevents nuclear localization of Sp1 and affects its DNA binding activity.
24129563	8	53	theme	HSF1	1153:1156	arg1	inhibition					1139:1148	inhibition	1139:1148	inhibition of HSF1 and HSP70	1139:1166	This in turn down-regulates prosurvival pathways like NF-κB, leading to inhibition of HSF1 and HSP70 and eventually to cell death.
24129563	1	54	with	disease	219:225	arg1	rate					250:253	a dismal survival rate	232:253	a dismal survival rate of 5% 5 years after diagnosis	232:283	Pancreatic cancer, the fourth most prevalent cancer-related cause of death in the United States, is a disease with a dismal survival rate of 5% 5 years after diagnosis.
24129563	9	55	gly	glycosylation	1268:1280	arg1	Sp1					1285:1287	Sp1	1285:1287	Sp1	1285:1287	In this study, we evaluated the mechanism by which triptolide affects glycosylation of Sp1, which in turn affects downstream pathways controlling survival of pancreatic cancer cells.
24129563	6	56	gly	glycosylation	841:853	arg1	Sp1					858:860	Sp1	858:860	Sp1	858:860	We further show that triptolide inhibits glycosylation of Sp1, inhibiting the hexosamine biosynthesis pathway, particularly the enzyme O-GlcNAc transferase.
24129563	9	57	theme	cells	1374:1378	arg1	survival					1344:1351	survival	1344:1351	survival of pancreatic cancer cells	1344:1378	In this study, we evaluated the mechanism by which triptolide affects glycosylation of Sp1, which in turn affects downstream pathways controlling survival of pancreatic cancer cells.
24129563	0	58	theme	O-GlcNAc	66:73	arg1	modification					75:86	O-GlcNAc modification	66:86	O-GlcNAc modification of transcription factor Sp1	66:114	Triptolide-induced cell death in pancreatic cancer is mediated by O-GlcNAc modification of transcription factor Sp1.
24129563	3	59	theme	cell	560:563	arg1	death					565:569	cell death	560:569	cell death	560:569	A naturally derived compound, triptolide, and its water-soluble prodrug, Minnelide, down-regulate the expression of this protein in pancreatic cancer cells, thereby causing cell death.
24129563	7	60	theme	transferase	980:990	arg1	Inhibition					957:966	Inhibition	957:966	Inhibition of O-GlcNAc transferase	957:990	Inhibition of O-GlcNAc transferase prevents nuclear localization of Sp1 and affects its DNA binding activity.
24129563	1	61	theme	fourth	140:145	arg1	cause					177:181	the fourth most prevalent cancer-related cause	136:181	the fourth most prevalent cancer-related cause of death in the United States	136:211	Pancreatic cancer, the fourth most prevalent cancer-related cause of death in the United States, is a disease with a dismal survival rate of 5% 5 years after diagnosis.
24129563	1	61	theme	fourth	140:145	arg1	cancer					128:133	Pancreatic cancer	117:133	Pancreatic cancer	117:133	Pancreatic cancer, the fourth most prevalent cancer-related cause of death in the United States, is a disease with a dismal survival rate of 5% 5 years after diagnosis.
24129563	4	62	theme	action	598:603	arg1	mechanism					585:593	the mechanism	581:593	the mechanism of action of triptolide	581:617	However, the mechanism of action of triptolide has not been elucidated.
24129563	6	63	theme	biosynthesis	889:900	arg1	pathway					902:908	the hexosamine biosynthesis pathway	874:908	the hexosamine biosynthesis pathway	874:908	We further show that triptolide inhibits glycosylation of Sp1, inhibiting the hexosamine biosynthesis pathway, particularly the enzyme O-GlcNAc transferase.
24129563	6	63	theme	biosynthesis	889:900	arg1	transferase					944:954	the enzyme O-GlcNAc transferase	924:954	particularly the enzyme O-GlcNAc transferase	911:954	We further show that triptolide inhibits glycosylation of Sp1, inhibiting the hexosamine biosynthesis pathway, particularly the enzyme O-GlcNAc transferase.
24129563	1	64	from	cause	177:181	arg1	States					206:211	the United States	195:211	the United States	195:211	Pancreatic cancer, the fourth most prevalent cancer-related cause of death in the United States, is a disease with a dismal survival rate of 5% 5 years after diagnosis.
24129563	9	65	theme	cancer	1367:1372	arg1	cells					1374:1378	pancreatic cancer cells	1356:1378	pancreatic cancer cells	1356:1378	In this study, we evaluated the mechanism by which triptolide affects glycosylation of Sp1, which in turn affects downstream pathways controlling survival of pancreatic cancer cells.
31394193	5	0	dep	c-Jun-S73A	763:772	arg1	form					796:799	a non-O-GlcNAcylated form	775:799	a non-O-GlcNAcylated form of c-Jun	775:808	Overexpression of c-Jun-WT with simultaneous PuGNAc treatment conversely inhibited erastin-induced ferroptosis, whereas overexpression of c-Jun-WT alone or overexpression of c-Jun-S73A (a non-O-GlcNAcylated form of c-Jun) with PuGNAc treatment did not exert a similar effect.
31394193	8	1	theme	positive	1202:1209	arg1	correlation					1211:1221	A positive correlation	1200:1221	A positive correlation between c-Jun O-GlcNAcylation and GSH	1200:1259	A positive correlation between c-Jun O-GlcNAcylation and GSH was observed in clinical samples.
31394193	0	2	from	synthesis	64:72	arg1	cancer					83:88	liver cancer	77:88	liver cancer	77:88	O-GlcNAcylated c-Jun antagonizes ferroptosis via inhibiting GSH synthesis in liver cancer.
31394193	7	3	theme	O-GlcNAcylated	1178:1191	arg1	c-Jun					1193:1197	O-GlcNAcylated c-Jun	1178:1197	O-GlcNAcylated c-Jun	1178:1197	In addition, overexpression of c-Jun-WT, but not its S73A mutant, induced PSAT1 and CBS transcription via directly binding to their promoter regions, suggesting that GSH synthesis is regulated by O-GlcNAcylated c-Jun.
31394193	5	4	theme	simultaneous	621:632	arg1	treatment					641:649	simultaneous PuGNAc treatment	621:649	simultaneous PuGNAc treatment	621:649	Overexpression of c-Jun-WT with simultaneous PuGNAc treatment conversely inhibited erastin-induced ferroptosis, whereas overexpression of c-Jun-WT alone or overexpression of c-Jun-S73A (a non-O-GlcNAcylated form of c-Jun) with PuGNAc treatment did not exert a similar effect.
31394193	7	5	theme	promoter	1114:1121	arg1	regions					1123:1129	their promoter regions	1108:1129	their promoter regions	1108:1129	In addition, overexpression of c-Jun-WT, but not its S73A mutant, induced PSAT1 and CBS transcription via directly binding to their promoter regions, suggesting that GSH synthesis is regulated by O-GlcNAcylated c-Jun.
31394193	7	6	theme	c-Jun-WT	1013:1020	arg1	overexpression					995:1008	overexpression	995:1008	overexpression of c-Jun-WT	995:1020	In addition, overexpression of c-Jun-WT, but not its S73A mutant, induced PSAT1 and CBS transcription via directly binding to their promoter regions, suggesting that GSH synthesis is regulated by O-GlcNAcylated c-Jun.
31394193	5	7	theme	PuGNAc	634:639	arg1	treatment					641:649	simultaneous PuGNAc treatment	621:649	simultaneous PuGNAc treatment	621:649	Overexpression of c-Jun-WT with simultaneous PuGNAc treatment conversely inhibited erastin-induced ferroptosis, whereas overexpression of c-Jun-WT alone or overexpression of c-Jun-S73A (a non-O-GlcNAcylated form of c-Jun) with PuGNAc treatment did not exert a similar effect.
31394193	6	8	theme	PuGNAc	964:969	arg1	treatment					971:979	simultaneous PuGNAc treatment	951:979	simultaneous PuGNAc treatment	951:979	GSH downregulation induced by erastin was restored by overexpression of c-Jun-WT with simultaneous PuGNAc treatment.
31394193	9	9	theme	obstructive	1344:1354	arg1	factor					1356:1361	an obstructive factor	1341:1361	an obstructive factor to ferroptosis	1341:1376	Collectively, O-GlcNAcylated c-Jun represents an obstructive factor to ferroptosis, and targeting O-GlcNAcylated c-Jun might be helpful for treating liver cancer.
31394193	4	10	theme	c-Jun	483:487	arg1	O-GlcNAcylation					464:478	O-GlcNAcylation	464:478	O-GlcNAcylation of c-Jun	464:487	Here, we observed that erastin suppressed the malignant phenotypes of liver cancer cells by inhibiting O-GlcNAcylation of c-Jun and further inhibited protein expression, transcription activity and nuclear accumulation of c-Jun.
31394193	5	11	theme	c-Jun-WT	727:734	arg1	overexpression					709:722	overexpression	709:722	overexpression of c-Jun-WT alone or overexpression of c-Jun-S73A (a non-O-GlcNAcylated form of c-Jun) with PuGNAc treatment	709:831	Overexpression of c-Jun-WT with simultaneous PuGNAc treatment conversely inhibited erastin-induced ferroptosis, whereas overexpression of c-Jun-WT alone or overexpression of c-Jun-S73A (a non-O-GlcNAcylated form of c-Jun) with PuGNAc treatment did not exert a similar effect.
31394193	4	12	theme	malignant	407:415	arg1	phenotypes					417:426	the malignant phenotypes	403:426	the malignant phenotypes of liver cancer cells	403:448	Here, we observed that erastin suppressed the malignant phenotypes of liver cancer cells by inhibiting O-GlcNAcylation of c-Jun and further inhibited protein expression, transcription activity and nuclear accumulation of c-Jun.
31394193	5	13	theme	c-Jun	804:808	arg1	form					796:799	a non-O-GlcNAcylated form	775:799	a non-O-GlcNAcylated form of c-Jun	775:808	Overexpression of c-Jun-WT with simultaneous PuGNAc treatment conversely inhibited erastin-induced ferroptosis, whereas overexpression of c-Jun-WT alone or overexpression of c-Jun-S73A (a non-O-GlcNAcylated form of c-Jun) with PuGNAc treatment did not exert a similar effect.
31394193	2	14	theme	liver	166:170	arg1	cells					179:183	liver cancer cells	166:183	liver cancer cells	166:183	Stimulating ferroptosis in liver cancer cells is a strategy to treat liver cancer.
31394193	3	15	theme	liver	248:252	arg1	cells					261:265	liver cancer cells	248:265	liver cancer cells	248:265	However, how to eradicate liver cancer cells through ferroptosis and the obstacles to inducing ferroptosis in liver cancer remain unclear.
31394193	5	16	theme	similar	849:855	arg1	effect					857:862	a similar effect	847:862	a similar effect	847:862	Overexpression of c-Jun-WT with simultaneous PuGNAc treatment conversely inhibited erastin-induced ferroptosis, whereas overexpression of c-Jun-WT alone or overexpression of c-Jun-S73A (a non-O-GlcNAcylated form of c-Jun) with PuGNAc treatment did not exert a similar effect.
31394193	3	17	theme	cancer	254:259	arg1	cells					261:265	liver cancer cells	248:265	liver cancer cells	248:265	However, how to eradicate liver cancer cells through ferroptosis and the obstacles to inducing ferroptosis in liver cancer remain unclear.
31394193	6	18	theme	c-Jun-WT	937:944	arg1	overexpression					919:932	overexpression	919:932	overexpression of c-Jun-WT with simultaneous PuGNAc treatment	919:979	GSH downregulation induced by erastin was restored by overexpression of c-Jun-WT with simultaneous PuGNAc treatment.
31394193	3	19	theme	liver	332:336	arg1	cancer					338:343	liver cancer	332:343	liver cancer	332:343	However, how to eradicate liver cancer cells through ferroptosis and the obstacles to inducing ferroptosis in liver cancer remain unclear.
31394193	9	20	theme	targeting	1383:1391	arg1	c-Jun					1408:1412	targeting O-GlcNAcylated c-Jun	1383:1412	targeting O-GlcNAcylated c-Jun	1383:1412	Collectively, O-GlcNAcylated c-Jun represents an obstructive factor to ferroptosis, and targeting O-GlcNAcylated c-Jun might be helpful for treating liver cancer.
31394193	6	21	theme	simultaneous	951:962	arg1	treatment					971:979	simultaneous PuGNAc treatment	951:979	simultaneous PuGNAc treatment	951:979	GSH downregulation induced by erastin was restored by overexpression of c-Jun-WT with simultaneous PuGNAc treatment.
31394193	0	22	theme	O-GlcNAcylated	0:13	arg1	c-Jun					15:19	O-GlcNAcylated c-Jun	0:19	O-GlcNAcylated c-Jun	0:19	O-GlcNAcylated c-Jun antagonizes ferroptosis via inhibiting GSH synthesis in liver cancer.
31394193	5	23	with	c-Jun-WT	607:614	arg1	treatment					641:649	simultaneous PuGNAc treatment	621:649	simultaneous PuGNAc treatment	621:649	Overexpression of c-Jun-WT with simultaneous PuGNAc treatment conversely inhibited erastin-induced ferroptosis, whereas overexpression of c-Jun-WT alone or overexpression of c-Jun-S73A (a non-O-GlcNAcylated form of c-Jun) with PuGNAc treatment did not exert a similar effect.
31394193	5	24	theme	c-Jun-WT	607:614	arg1	Overexpression					589:602	Overexpression	589:602	Overexpression of c-Jun-WT with simultaneous PuGNAc treatment	589:649	Overexpression of c-Jun-WT with simultaneous PuGNAc treatment conversely inhibited erastin-induced ferroptosis, whereas overexpression of c-Jun-WT alone or overexpression of c-Jun-S73A (a non-O-GlcNAcylated form of c-Jun) with PuGNAc treatment did not exert a similar effect.
31394193	7	25	theme	GSH	1148:1150	arg1	synthesis					1152:1160	GSH synthesis	1148:1160	GSH synthesis	1148:1160	In addition, overexpression of c-Jun-WT, but not its S73A mutant, induced PSAT1 and CBS transcription via directly binding to their promoter regions, suggesting that GSH synthesis is regulated by O-GlcNAcylated c-Jun.
31394193	6	26	with	overexpression	919:932	arg1	treatment					971:979	simultaneous PuGNAc treatment	951:979	simultaneous PuGNAc treatment	951:979	GSH downregulation induced by erastin was restored by overexpression of c-Jun-WT with simultaneous PuGNAc treatment.
31394193	5	27	theme	c-Jun-S73A	763:772	arg1	overexpression					745:758	overexpression	745:758	overexpression of c-Jun-S73A (a non-O-GlcNAcylated form of c-Jun) with PuGNAc treatment	745:831	Overexpression of c-Jun-WT with simultaneous PuGNAc treatment conversely inhibited erastin-induced ferroptosis, whereas overexpression of c-Jun-WT alone or overexpression of c-Jun-S73A (a non-O-GlcNAcylated form of c-Jun) with PuGNAc treatment did not exert a similar effect.
31394193	5	27	theme	c-Jun-S73A	763:772	arg1	c-Jun-WT					727:734	c-Jun-WT	727:734	c-Jun-WT alone	727:740	Overexpression of c-Jun-WT with simultaneous PuGNAc treatment conversely inhibited erastin-induced ferroptosis, whereas overexpression of c-Jun-WT alone or overexpression of c-Jun-S73A (a non-O-GlcNAcylated form of c-Jun) with PuGNAc treatment did not exert a similar effect.
31394193	8	28	located	observed	1265:1272	arg1	samples					1286:1292	clinical samples	1277:1292	clinical samples	1277:1292	A positive correlation between c-Jun O-GlcNAcylation and GSH was observed in clinical samples.
31394193	8	28	located	observed	1265:1272	arg2	correlation					1211:1221	A positive correlation	1200:1221	A positive correlation between c-Jun O-GlcNAcylation and GSH	1200:1259	A positive correlation between c-Jun O-GlcNAcylation and GSH was observed in clinical samples.
31394193	1	29	theme	metabolism-related	108:125	arg1	death					132:136	a metabolism-related cell death	106:136	a metabolism-related cell death	106:136	Ferroptosis is a metabolism-related cell death.
31394193	1	29	theme	metabolism-related	108:125	arg1	Ferroptosis					91:101	Ferroptosis	91:101	Ferroptosis	91:101	Ferroptosis is a metabolism-related cell death.
31394193	8	30	theme	clinical	1277:1284	arg1	samples					1286:1292	clinical samples	1277:1292	clinical samples	1277:1292	A positive correlation between c-Jun O-GlcNAcylation and GSH was observed in clinical samples.
31394193	4	31	theme	c-Jun	582:586	arg1	expression					519:528	protein expression	511:528	protein expression	511:528	Here, we observed that erastin suppressed the malignant phenotypes of liver cancer cells by inhibiting O-GlcNAcylation of c-Jun and further inhibited protein expression, transcription activity and nuclear accumulation of c-Jun.
31394193	4	31	theme	c-Jun	582:586	arg1	activity					545:552	transcription activity	531:552	transcription activity	531:552	Here, we observed that erastin suppressed the malignant phenotypes of liver cancer cells by inhibiting O-GlcNAcylation of c-Jun and further inhibited protein expression, transcription activity and nuclear accumulation of c-Jun.
31394193	4	31	theme	c-Jun	582:586	arg1	accumulation					566:577	nuclear accumulation	558:577	nuclear accumulation of c-Jun	558:586	Here, we observed that erastin suppressed the malignant phenotypes of liver cancer cells by inhibiting O-GlcNAcylation of c-Jun and further inhibited protein expression, transcription activity and nuclear accumulation of c-Jun.
31394193	9	32	theme	O-GlcNAcylated	1393:1406	arg1	c-Jun					1408:1412	targeting O-GlcNAcylated c-Jun	1383:1412	targeting O-GlcNAcylated c-Jun	1383:1412	Collectively, O-GlcNAcylated c-Jun represents an obstructive factor to ferroptosis, and targeting O-GlcNAcylated c-Jun might be helpful for treating liver cancer.
31394193	4	33	theme	cells	444:448	arg1	phenotypes					417:426	the malignant phenotypes	403:426	the malignant phenotypes of liver cancer cells	403:448	Here, we observed that erastin suppressed the malignant phenotypes of liver cancer cells by inhibiting O-GlcNAcylation of c-Jun and further inhibited protein expression, transcription activity and nuclear accumulation of c-Jun.
31394193	5	34	with	c-Jun-S73A	763:772	arg1	treatment					823:831	PuGNAc treatment	816:831	PuGNAc treatment	816:831	Overexpression of c-Jun-WT with simultaneous PuGNAc treatment conversely inhibited erastin-induced ferroptosis, whereas overexpression of c-Jun-WT alone or overexpression of c-Jun-S73A (a non-O-GlcNAcylated form of c-Jun) with PuGNAc treatment did not exert a similar effect.
31394193	2	35	from	ferroptosis	151:161	arg1	cells					179:183	liver cancer cells	166:183	liver cancer cells	166:183	Stimulating ferroptosis in liver cancer cells is a strategy to treat liver cancer.
31394193	9	36	theme	liver	1444:1448	arg1	cancer					1450:1455	liver cancer	1444:1455	liver cancer	1444:1455	Collectively, O-GlcNAcylated c-Jun represents an obstructive factor to ferroptosis, and targeting O-GlcNAcylated c-Jun might be helpful for treating liver cancer.
31394193	5	37	theme	non-O-GlcNAcylated	777:794	arg1	form					796:799	a non-O-GlcNAcylated form	775:799	a non-O-GlcNAcylated form of c-Jun	775:808	Overexpression of c-Jun-WT with simultaneous PuGNAc treatment conversely inhibited erastin-induced ferroptosis, whereas overexpression of c-Jun-WT alone or overexpression of c-Jun-S73A (a non-O-GlcNAcylated form of c-Jun) with PuGNAc treatment did not exert a similar effect.
31394193	9	38	theme	O-GlcNAcylated	1309:1322	arg1	c-Jun					1324:1328	O-GlcNAcylated c-Jun	1309:1328	O-GlcNAcylated c-Jun	1309:1328	Collectively, O-GlcNAcylated c-Jun represents an obstructive factor to ferroptosis, and targeting O-GlcNAcylated c-Jun might be helpful for treating liver cancer.
31394193	7	39	theme	CBS	1066:1068	arg1	transcription					1070:1082	CBS transcription	1066:1082	CBS transcription	1066:1082	In addition, overexpression of c-Jun-WT, but not its S73A mutant, induced PSAT1 and CBS transcription via directly binding to their promoter regions, suggesting that GSH synthesis is regulated by O-GlcNAcylated c-Jun.
31394193	8	40	theme	c-Jun	1231:1235	arg1	O-GlcNAcylation					1237:1251	c-Jun O-GlcNAcylation	1231:1251	c-Jun O-GlcNAcylation	1231:1251	A positive correlation between c-Jun O-GlcNAcylation and GSH was observed in clinical samples.
31394193	4	41	theme	transcription	531:543	arg1	activity					545:552	transcription activity	531:552	transcription activity	531:552	Here, we observed that erastin suppressed the malignant phenotypes of liver cancer cells by inhibiting O-GlcNAcylation of c-Jun and further inhibited protein expression, transcription activity and nuclear accumulation of c-Jun.
31394193	1	42	theme	cell	127:130	arg1	death					132:136	a metabolism-related cell death	106:136	a metabolism-related cell death	106:136	Ferroptosis is a metabolism-related cell death.
31394193	1	42	theme	cell	127:130	arg1	Ferroptosis					91:101	Ferroptosis	91:101	Ferroptosis	91:101	Ferroptosis is a metabolism-related cell death.
31394193	0	43	theme	GSH	60:62	arg1	synthesis					64:72	GSH synthesis	60:72	GSH synthesis in liver cancer	60:88	O-GlcNAcylated c-Jun antagonizes ferroptosis via inhibiting GSH synthesis in liver cancer.
31394193	4	44	theme	nuclear	558:564	arg1	accumulation					566:577	nuclear accumulation	558:577	nuclear accumulation of c-Jun	558:586	Here, we observed that erastin suppressed the malignant phenotypes of liver cancer cells by inhibiting O-GlcNAcylation of c-Jun and further inhibited protein expression, transcription activity and nuclear accumulation of c-Jun.
31394193	2	45	theme	Stimulating	139:149	arg1	strategy					190:197	a strategy	188:197	a strategy to treat liver cancer	188:219	Stimulating ferroptosis in liver cancer cells is a strategy to treat liver cancer.
31394193	2	45	theme	Stimulating	139:149	arg1	ferroptosis					151:161	Stimulating ferroptosis	139:161	Stimulating ferroptosis in liver cancer cells	139:183	Stimulating ferroptosis in liver cancer cells is a strategy to treat liver cancer.
31394193	5	46	theme	erastin-induced	672:686	arg1	ferroptosis					688:698	erastin-induced ferroptosis	672:698	erastin-induced ferroptosis	672:698	Overexpression of c-Jun-WT with simultaneous PuGNAc treatment conversely inhibited erastin-induced ferroptosis, whereas overexpression of c-Jun-WT alone or overexpression of c-Jun-S73A (a non-O-GlcNAcylated form of c-Jun) with PuGNAc treatment did not exert a similar effect.
31394193	5	47	theme	overexpression	745:758	arg1	overexpression					709:722	overexpression	709:722	overexpression of c-Jun-WT alone or overexpression of c-Jun-S73A (a non-O-GlcNAcylated form of c-Jun) with PuGNAc treatment	709:831	Overexpression of c-Jun-WT with simultaneous PuGNAc treatment conversely inhibited erastin-induced ferroptosis, whereas overexpression of c-Jun-WT alone or overexpression of c-Jun-S73A (a non-O-GlcNAcylated form of c-Jun) with PuGNAc treatment did not exert a similar effect.
31394193	2	48	theme	liver	208:212	arg1	cancer					214:219	liver cancer	208:219	liver cancer	208:219	Stimulating ferroptosis in liver cancer cells is a strategy to treat liver cancer.
31394193	6	49	theme	GSH	865:867	arg1	downregulation					869:882	GSH downregulation	865:882	GSH downregulation induced by erastin	865:901	GSH downregulation induced by erastin was restored by overexpression of c-Jun-WT with simultaneous PuGNAc treatment.
31394193	4	50	theme	cancer	437:442	arg1	cells					444:448	liver cancer cells	431:448	liver cancer cells	431:448	Here, we observed that erastin suppressed the malignant phenotypes of liver cancer cells by inhibiting O-GlcNAcylation of c-Jun and further inhibited protein expression, transcription activity and nuclear accumulation of c-Jun.
31394193	0	51	theme	liver	77:81	arg1	cancer					83:88	liver cancer	77:88	liver cancer	77:88	O-GlcNAcylated c-Jun antagonizes ferroptosis via inhibiting GSH synthesis in liver cancer.
31394193	4	52	theme	liver	431:435	arg1	cells					444:448	liver cancer cells	431:448	liver cancer cells	431:448	Here, we observed that erastin suppressed the malignant phenotypes of liver cancer cells by inhibiting O-GlcNAcylation of c-Jun and further inhibited protein expression, transcription activity and nuclear accumulation of c-Jun.
31394193	5	53	theme	PuGNAc	816:821	arg1	treatment					823:831	PuGNAc treatment	816:831	PuGNAc treatment	816:831	Overexpression of c-Jun-WT with simultaneous PuGNAc treatment conversely inhibited erastin-induced ferroptosis, whereas overexpression of c-Jun-WT alone or overexpression of c-Jun-S73A (a non-O-GlcNAcylated form of c-Jun) with PuGNAc treatment did not exert a similar effect.
31394193	4	54	theme	protein	511:517	arg1	expression					519:528	protein expression	511:528	protein expression	511:528	Here, we observed that erastin suppressed the malignant phenotypes of liver cancer cells by inhibiting O-GlcNAcylation of c-Jun and further inhibited protein expression, transcription activity and nuclear accumulation of c-Jun.
31394193	7	55	theme	S73A	1035:1038	arg1	mutant					1040:1045	its S73A mutant	1031:1045	its S73A mutant	1031:1045	In addition, overexpression of c-Jun-WT, but not its S73A mutant, induced PSAT1 and CBS transcription via directly binding to their promoter regions, suggesting that GSH synthesis is regulated by O-GlcNAcylated c-Jun.
31394193	2	56	theme	cancer	172:177	arg1	cells					179:183	liver cancer cells	166:183	liver cancer cells	166:183	Stimulating ferroptosis in liver cancer cells is a strategy to treat liver cancer.
26825459	5	0	theme	proteins	667:674	arg1	O-GlcNAcylation					641:655	enhanced O-GlcNAcylation	632:655	enhanced O-GlcNAcylation of target proteins	632:674	Mechanistically, AGER activated a hexosamine biosynthetic pathway, leading to enhanced O-GlcNAcylation of target proteins.
26825459	10	1	theme	blood	1225:1229	arg1	levels					1239:1244	high blood glucose levels	1220:1244	high blood glucose levels	1220:1244	In conclusion, AGER and its functions to stimulate O-GlcNAcylation are important during liver tumorigenesis, when high blood glucose levels are inadequately controlled.
26825459	8	2	theme	positive	888:895	arg1	loop					921:924	a positive autoregulatory feedback loop	886:924	a positive autoregulatory feedback loop that stimulates diabetic HCC	886:953	Thereby, a positive autoregulatory feedback loop that stimulates diabetic HCC was established.
26825459	10	3	theme	high	1220:1223	arg1	levels					1239:1244	high blood glucose levels	1220:1244	high blood glucose levels	1220:1244	In conclusion, AGER and its functions to stimulate O-GlcNAcylation are important during liver tumorigenesis, when high blood glucose levels are inadequately controlled.
26825459	3	4	theme	main	352:355	arg1	characteristics					357:371	the main characteristics	348:371	the main characteristics of diabetes	348:383	Here, we demonstrated that high glucose (HG), one of the main characteristics of diabetes, was capable of accelerating tumorigenesis in HCC cells.
26825459	3	5	from	tumorigenesis	414:426	arg1	cells					435:439	HCC cells	431:439	HCC cells	431:439	Here, we demonstrated that high glucose (HG), one of the main characteristics of diabetes, was capable of accelerating tumorigenesis in HCC cells.
26825459	0	6	theme	c-Jun	114:118	arg1	O-GlcNAcylation					95:109	AGER-Dependent O-GlcNAcylation	80:109	AGER-Dependent O-GlcNAcylation of c-Jun	80:118	High Glucose Stimulates Tumorigenesis in Hepatocellular Carcinoma Cells Through AGER-Dependent O-GlcNAcylation of c-Jun.
26825459	1	7	contain	has	187:189	arg1	HCC					182:184	HCC	182:184	HCC	182:184	Epidemiologic studies suggest that hepatocellular carcinoma (HCC) has a strong relationship with diabetes.
26825459	1	7	contain	has	187:189	arg1	carcinoma					171:179	hepatocellular carcinoma	156:179	hepatocellular carcinoma (HCC)	156:185	Epidemiologic studies suggest that hepatocellular carcinoma (HCC) has a strong relationship with diabetes.
26825459	1	7	contain	has	187:189	arg2	relationship					200:211	a strong relationship	191:211	a strong relationship with diabetes	191:225	Epidemiologic studies suggest that hepatocellular carcinoma (HCC) has a strong relationship with diabetes.
26825459	8	8	theme	feedback	912:919	arg1	loop					921:924	a positive autoregulatory feedback loop	886:924	a positive autoregulatory feedback loop that stimulates diabetic HCC	886:953	Thereby, a positive autoregulatory feedback loop that stimulates diabetic HCC was established.
26825459	5	9	theme	enhanced	632:639	arg1	O-GlcNAcylation					641:655	enhanced O-GlcNAcylation	632:655	enhanced O-GlcNAcylation of target proteins	632:674	Mechanistically, AGER activated a hexosamine biosynthetic pathway, leading to enhanced O-GlcNAcylation of target proteins.
26825459	8	10	theme	autoregulatory	897:910	arg1	loop					921:924	a positive autoregulatory feedback loop	886:924	a positive autoregulatory feedback loop that stimulates diabetic HCC	886:953	Thereby, a positive autoregulatory feedback loop that stimulates diabetic HCC was established.
26825459	10	11	from	conclusion	1109:1118	arg1	important					1177:1185	important	1177:1185	important	1177:1185	In conclusion, AGER and its functions to stimulate O-GlcNAcylation are important during liver tumorigenesis, when high blood glucose levels are inadequately controlled.
26825459	10	12	dep	functions	1134:1142	arg1	stimulate					1147:1155	stimulate	1147:1155	to stimulate O-GlcNAcylation	1144:1171	In conclusion, AGER and its functions to stimulate O-GlcNAcylation are important during liver tumorigenesis, when high blood glucose levels are inadequately controlled.
26825459	9	13	theme	Janus	1018:1022	arg1	kinase					1024:1029	Janus kinase	1018:1029	Janus kinase	1018:1029	Finally, we found that AG490, an inhibitor of Janus kinase, has the ability to impair AGER expression and its functions in HCC cells.
26825459	9	14	theme	HCC	1095:1097	arg1	cells					1099:1103	HCC cells	1095:1103	HCC cells	1095:1103	Finally, we found that AG490, an inhibitor of Janus kinase, has the ability to impair AGER expression and its functions in HCC cells.
26825459	1	15	theme	strong	193:198	arg1	relationship					200:211	a strong relationship	191:211	a strong relationship with diabetes	191:225	Epidemiologic studies suggest that hepatocellular carcinoma (HCC) has a strong relationship with diabetes.
26825459	0	16	theme	High	0:3	arg1	Glucose					5:11	High Glucose	0:11	High Glucose	0:11	High Glucose Stimulates Tumorigenesis in Hepatocellular Carcinoma Cells Through AGER-Dependent O-GlcNAcylation of c-Jun.
26825459	5	17	theme	target	660:665	arg1	proteins					667:674	target proteins	660:674	target proteins	660:674	Mechanistically, AGER activated a hexosamine biosynthetic pathway, leading to enhanced O-GlcNAcylation of target proteins.
26825459	5	18	theme	hexosamine	588:597	arg1	pathway					612:618	a hexosamine biosynthetic pathway	586:618	a hexosamine biosynthetic pathway	586:618	Mechanistically, AGER activated a hexosamine biosynthetic pathway, leading to enhanced O-GlcNAcylation of target proteins.
26825459	8	19	theme	diabetic	942:949	arg1	HCC					951:953	diabetic HCC	942:953	diabetic HCC	942:953	Thereby, a positive autoregulatory feedback loop that stimulates diabetic HCC was established.
26825459	3	20	theme	HCC	431:433	arg1	cells					435:439	HCC cells	431:439	HCC cells	431:439	Here, we demonstrated that high glucose (HG), one of the main characteristics of diabetes, was capable of accelerating tumorigenesis in HCC cells.
26825459	5	21	theme	biosynthetic	599:610	arg1	pathway					612:618	a hexosamine biosynthetic pathway	586:618	a hexosamine biosynthetic pathway	586:618	Mechanistically, AGER activated a hexosamine biosynthetic pathway, leading to enhanced O-GlcNAcylation of target proteins.
26825459	1	22	theme	Epidemiologic	121:133	arg1	studies					135:141	Epidemiologic studies	121:141	Epidemiologic studies	121:141	Epidemiologic studies suggest that hepatocellular carcinoma (HCC) has a strong relationship with diabetes.
26825459	6	23	from	Ser73	806:810	arg1	O-GlcNAcylation					771:785	O-GlcNAcylation	771:785	O-GlcNAcylation of this protein at Ser73	771:810	Notably, AGER was capable of increasing activity and stability of proto-oncoprotein c-Jun via O-GlcNAcylation of this protein at Ser73.
26825459	3	24	theme	diabetes	376:383	arg1	characteristics					357:371	the main characteristics	348:371	the main characteristics of diabetes	348:383	Here, we demonstrated that high glucose (HG), one of the main characteristics of diabetes, was capable of accelerating tumorigenesis in HCC cells.
26825459	10	25	from	important	1177:1185	arg1	conclusion					1109:1118	conclusion	1109:1118	conclusion	1109:1118	In conclusion, AGER and its functions to stimulate O-GlcNAcylation are important during liver tumorigenesis, when high blood glucose levels are inadequately controlled.
26825459	4	26	theme	glycosylation	451:463	arg1	AGER					496:499	AGER	496:499	AGER	496:499	Advanced glycosylation end product-specific receptor (AGER) was identified as a stimulator during this process.
26825459	4	26	theme	glycosylation	451:463	arg1	receptor					486:493	Advanced glycosylation end product-specific receptor	442:493	Advanced glycosylation end product-specific receptor (AGER)	442:500	Advanced glycosylation end product-specific receptor (AGER) was identified as a stimulator during this process.
26825459	4	26	theme	glycosylation	451:463	arg1	stimulator					522:531	a stimulator	520:531	a stimulator during this process	520:551	Advanced glycosylation end product-specific receptor (AGER) was identified as a stimulator during this process.
26825459	9	27	from	ability	1040:1046	arg1	cells					1099:1103	HCC cells	1095:1103	HCC cells	1095:1103	Finally, we found that AG490, an inhibitor of Janus kinase, has the ability to impair AGER expression and its functions in HCC cells.
26825459	0	28	theme	Hepatocellular	41:54	arg1	Cells					66:70	Hepatocellular Carcinoma Cells	41:70	Hepatocellular Carcinoma Cells	41:70	High Glucose Stimulates Tumorigenesis in Hepatocellular Carcinoma Cells Through AGER-Dependent O-GlcNAcylation of c-Jun.
26825459	4	29	theme	Advanced	442:449	arg1	AGER					496:499	AGER	496:499	AGER	496:499	Advanced glycosylation end product-specific receptor (AGER) was identified as a stimulator during this process.
26825459	4	29	theme	Advanced	442:449	arg1	receptor					486:493	Advanced glycosylation end product-specific receptor	442:493	Advanced glycosylation end product-specific receptor (AGER)	442:500	Advanced glycosylation end product-specific receptor (AGER) was identified as a stimulator during this process.
26825459	4	29	theme	Advanced	442:449	arg1	stimulator					522:531	a stimulator	520:531	a stimulator during this process	520:551	Advanced glycosylation end product-specific receptor (AGER) was identified as a stimulator during this process.
26825459	7	30	theme	AGER	857:860	arg1	transcription					862:874	AGER transcription	857:874	AGER transcription	857:874	Interestingly, c-Jun can conversely enhance AGER transcription.
26825459	9	31	theme	kinase	1024:1029	arg1	inhibitor					1005:1013	an inhibitor	1002:1013	an inhibitor of Janus kinase	1002:1029	Finally, we found that AG490, an inhibitor of Janus kinase, has the ability to impair AGER expression and its functions in HCC cells.
26825459	9	31	theme	kinase	1024:1029	arg1	AG490					995:999	AG490	995:999	AG490	995:999	Finally, we found that AG490, an inhibitor of Janus kinase, has the ability to impair AGER expression and its functions in HCC cells.
26825459	4	32	theme	product-specific	469:484	arg1	AGER					496:499	AGER	496:499	AGER	496:499	Advanced glycosylation end product-specific receptor (AGER) was identified as a stimulator during this process.
26825459	4	32	theme	product-specific	469:484	arg1	receptor					486:493	Advanced glycosylation end product-specific receptor	442:493	Advanced glycosylation end product-specific receptor (AGER)	442:500	Advanced glycosylation end product-specific receptor (AGER) was identified as a stimulator during this process.
26825459	4	32	theme	product-specific	469:484	arg1	stimulator					522:531	a stimulator	520:531	a stimulator during this process	520:551	Advanced glycosylation end product-specific receptor (AGER) was identified as a stimulator during this process.
26825459	2	33	theme	molecular	252:260	arg1	mechanisms					262:271	the underlying molecular mechanisms	237:271	the underlying molecular mechanisms	237:271	However, the underlying molecular mechanisms still remain unclear.
26825459	6	34	theme	protein	795:801	arg1	O-GlcNAcylation					771:785	O-GlcNAcylation	771:785	O-GlcNAcylation of this protein at Ser73	771:810	Notably, AGER was capable of increasing activity and stability of proto-oncoprotein c-Jun via O-GlcNAcylation of this protein at Ser73.
26825459	1	35	with	relationship	200:211	arg1	diabetes					218:225	diabetes	218:225	diabetes	218:225	Epidemiologic studies suggest that hepatocellular carcinoma (HCC) has a strong relationship with diabetes.
26825459	4	36	theme	end	465:467	arg1	AGER					496:499	AGER	496:499	AGER	496:499	Advanced glycosylation end product-specific receptor (AGER) was identified as a stimulator during this process.
26825459	4	36	theme	end	465:467	arg1	receptor					486:493	Advanced glycosylation end product-specific receptor	442:493	Advanced glycosylation end product-specific receptor (AGER)	442:500	Advanced glycosylation end product-specific receptor (AGER) was identified as a stimulator during this process.
26825459	4	36	theme	end	465:467	arg1	stimulator					522:531	a stimulator	520:531	a stimulator during this process	520:551	Advanced glycosylation end product-specific receptor (AGER) was identified as a stimulator during this process.
26825459	2	37	theme	underlying	241:250	arg1	mechanisms					262:271	the underlying molecular mechanisms	237:271	the underlying molecular mechanisms	237:271	However, the underlying molecular mechanisms still remain unclear.
26825459	0	38	theme	Carcinoma	56:64	arg1	Cells					66:70	Hepatocellular Carcinoma Cells	41:70	Hepatocellular Carcinoma Cells	41:70	High Glucose Stimulates Tumorigenesis in Hepatocellular Carcinoma Cells Through AGER-Dependent O-GlcNAcylation of c-Jun.
26825459	9	39	contain	has	1032:1034	arg1	inhibitor					1005:1013	an inhibitor	1002:1013	an inhibitor of Janus kinase	1002:1029	Finally, we found that AG490, an inhibitor of Janus kinase, has the ability to impair AGER expression and its functions in HCC cells.
26825459	9	39	contain	has	1032:1034	arg2	functions					1082:1090	its functions	1078:1090	its functions in HCC cells	1078:1103	Finally, we found that AG490, an inhibitor of Janus kinase, has the ability to impair AGER expression and its functions in HCC cells.
26825459	9	39	contain	has	1032:1034	arg2	ability					1040:1046	the ability	1036:1046	the ability to impair AGER expression	1036:1072	Finally, we found that AG490, an inhibitor of Janus kinase, has the ability to impair AGER expression and its functions in HCC cells.
26825459	9	39	contain	has	1032:1034	arg1	AG490					995:999	AG490	995:999	AG490	995:999	Finally, we found that AG490, an inhibitor of Janus kinase, has the ability to impair AGER expression and its functions in HCC cells.
26825459	1	40	theme	hepatocellular	156:169	arg1	HCC					182:184	HCC	182:184	HCC	182:184	Epidemiologic studies suggest that hepatocellular carcinoma (HCC) has a strong relationship with diabetes.
26825459	1	40	theme	hepatocellular	156:169	arg1	carcinoma					171:179	hepatocellular carcinoma	156:179	hepatocellular carcinoma (HCC)	156:185	Epidemiologic studies suggest that hepatocellular carcinoma (HCC) has a strong relationship with diabetes.
26825459	3	41	theme	high	322:325	arg1	HG					336:337	HG	336:337	HG	336:337	Here, we demonstrated that high glucose (HG), one of the main characteristics of diabetes, was capable of accelerating tumorigenesis in HCC cells.
26825459	3	41	theme	high	322:325	arg1	one					341:343	one	341:343	one	341:343	Here, we demonstrated that high glucose (HG), one of the main characteristics of diabetes, was capable of accelerating tumorigenesis in HCC cells.
26825459	3	41	theme	high	322:325	arg1	glucose					327:333	high glucose	322:333	high glucose (HG)	322:338	Here, we demonstrated that high glucose (HG), one of the main characteristics of diabetes, was capable of accelerating tumorigenesis in HCC cells.
26825459	3	41	theme	high	322:325	arg1	characteristics					357:371	the main characteristics	348:371	the main characteristics of diabetes	348:383	Here, we demonstrated that high glucose (HG), one of the main characteristics of diabetes, was capable of accelerating tumorigenesis in HCC cells.
26825459	10	42	theme	liver	1194:1198	arg1	tumorigenesis					1200:1212	liver tumorigenesis	1194:1212	liver tumorigenesis	1194:1212	In conclusion, AGER and its functions to stimulate O-GlcNAcylation are important during liver tumorigenesis, when high blood glucose levels are inadequately controlled.
26825459	0	43	theme	AGER-Dependent	80:93	arg1	O-GlcNAcylation					95:109	AGER-Dependent O-GlcNAcylation	80:109	AGER-Dependent O-GlcNAcylation of c-Jun	80:118	High Glucose Stimulates Tumorigenesis in Hepatocellular Carcinoma Cells Through AGER-Dependent O-GlcNAcylation of c-Jun.
26825459	9	44	from	functions	1082:1090	arg1	cells					1099:1103	HCC cells	1095:1103	HCC cells	1095:1103	Finally, we found that AG490, an inhibitor of Janus kinase, has the ability to impair AGER expression and its functions in HCC cells.
26825459	6	45	theme	c-Jun	761:765	arg1	activity					717:724	activity	717:724	activity	717:724	Notably, AGER was capable of increasing activity and stability of proto-oncoprotein c-Jun via O-GlcNAcylation of this protein at Ser73.
26825459	6	45	theme	c-Jun	761:765	arg1	stability					730:738	stability	730:738	stability	730:738	Notably, AGER was capable of increasing activity and stability of proto-oncoprotein c-Jun via O-GlcNAcylation of this protein at Ser73.
26825459	10	46	theme	glucose	1231:1237	arg1	levels					1239:1244	high blood glucose levels	1220:1244	high blood glucose levels	1220:1244	In conclusion, AGER and its functions to stimulate O-GlcNAcylation are important during liver tumorigenesis, when high blood glucose levels are inadequately controlled.
26825459	0	47	from	Tumorigenesis	24:36	arg1	Cells					66:70	Hepatocellular Carcinoma Cells	41:70	Hepatocellular Carcinoma Cells	41:70	High Glucose Stimulates Tumorigenesis in Hepatocellular Carcinoma Cells Through AGER-Dependent O-GlcNAcylation of c-Jun.
26825459	6	48	theme	proto-oncoprotein	743:759	arg1	c-Jun					761:765	proto-oncoprotein c-Jun	743:765	proto-oncoprotein c-Jun	743:765	Notably, AGER was capable of increasing activity and stability of proto-oncoprotein c-Jun via O-GlcNAcylation of this protein at Ser73.
26825459	9	49	theme	AGER	1058:1061	arg1	expression					1063:1072	AGER expression	1058:1072	AGER expression	1058:1072	Finally, we found that AG490, an inhibitor of Janus kinase, has the ability to impair AGER expression and its functions in HCC cells.
26825459	3	50	theme	characteristics	357:371	arg1	one					341:343	one	341:343	one	341:343	Here, we demonstrated that high glucose (HG), one of the main characteristics of diabetes, was capable of accelerating tumorigenesis in HCC cells.
26825459	3	50	theme	characteristics	357:371	arg1	glucose					327:333	high glucose	322:333	high glucose (HG)	322:338	Here, we demonstrated that high glucose (HG), one of the main characteristics of diabetes, was capable of accelerating tumorigenesis in HCC cells.
26825459	3	50	theme	characteristics	357:371	arg1	characteristics					357:371	the main characteristics	348:371	the main characteristics of diabetes	348:383	Here, we demonstrated that high glucose (HG), one of the main characteristics of diabetes, was capable of accelerating tumorigenesis in HCC cells.
27059955	8	0	from	K18-S30A	1294:1301	arg1	migration					1353:1361	cell migration	1348:1361	cell migration	1348:1361	Further to this, the K18 phosphomutant (K18-S33A) mimicked K18-S30A in its stability, filament organization, and cell migration.
27059955	8	0	from	K18-S30A	1294:1301	arg1	stability					1310:1318	its stability	1306:1318	its stability	1306:1318	Further to this, the K18 phosphomutant (K18-S33A) mimicked K18-S30A in its stability, filament organization, and cell migration.
27059955	8	0	from	K18-S30A	1294:1301	arg1	organization					1330:1341	filament organization	1321:1341	filament organization	1321:1341	Further to this, the K18 phosphomutant (K18-S33A) mimicked K18-S30A in its stability, filament organization, and cell migration.
27059955	11	1	theme	novel	1706:1710	arg1	interplay					1722:1730	a novel, positive interplay	1704:1730	a novel, positive interplay between O-GlcNAcylation and phosphorylation at adjacent sites on K18 to regulate its fundamental properties	1704:1838	Here we report a novel, positive interplay between O-GlcNAcylation and phosphorylation at adjacent sites on K18 to regulate its fundamental properties.
27059955	2	2	theme	phosphorylation	286:300	arg1	sites					331:335	The three O-GlcNAcylation (Ser(29), Ser(30), and Ser(48)) and two phosphorylation (Ser(33) and Ser(52)) serine sites	220:335	The three O-GlcNAcylation (Ser(29), Ser(30), and Ser(48)) and two phosphorylation (Ser(33) and Ser(52)) serine sites on K18	220:342	The three O-GlcNAcylation (Ser(29), Ser(30), and Ser(48)) and two phosphorylation (Ser(33) and Ser(52)) serine sites on K18 are well characterized.
27059955	9	3	from	Ser	1411:1413	arg1	O-GlcNAcylation					1392:1406	O-GlcNAcylation	1392:1406	O-GlcNAcylation at Ser(30)	1392:1417	These results indicate that O-GlcNAcylation at Ser(30) promotes phosphorylation at Ser(33) to regulate the functional properties of K18 and also impact cellular processes like migration.
27059955	9	4	theme	functional	1471:1480	arg1	properties					1482:1491	the functional properties	1467:1491	the functional properties of K18	1467:1498	These results indicate that O-GlcNAcylation at Ser(30) promotes phosphorylation at Ser(33) to regulate the functional properties of K18 and also impact cellular processes like migration.
27059955	1	5	dep	Keratins	103:110	arg1	K8/18					118:122	K8/18	118:122	K8/18	118:122	Keratins 8/18 (K8/18) are phosphoglycoproteins and form the major intermediate filament network of simple epithelia.
27059955	1	5	dep	Keratins	103:110	arg1	8/18					112:115	8/18	112:115	8/18	112:115	Keratins 8/18 (K8/18) are phosphoglycoproteins and form the major intermediate filament network of simple epithelia.
27059955	8	6	theme	cell	1348:1351	arg1	migration					1353:1361	cell migration	1348:1361	cell migration	1348:1361	Further to this, the K18 phosphomutant (K18-S33A) mimicked K18-S30A in its stability, filament organization, and cell migration.
27059955	2	7	from	sites	331:335	arg1	K18					340:342	K18	340:342	K18	340:342	The three O-GlcNAcylation (Ser(29), Ser(30), and Ser(48)) and two phosphorylation (Ser(33) and Ser(52)) serine sites on K18 are well characterized.
27059955	7	8	theme	K18	1230:1232	arg1	solubility					1216:1225	the solubility	1212:1225	the solubility of K18	1212:1232	Interestingly, K18-S30A mutants also showed loss of phosphorylation at Ser(33), a modification known to regulate the solubility of K18.
27059955	2	9	dep	phosphorylation	286:300	arg1	Ser					315:317	Ser(52)	315:321	Ser(52)	315:321	The three O-GlcNAcylation (Ser(29), Ser(30), and Ser(48)) and two phosphorylation (Ser(33) and Ser(52)) serine sites on K18 are well characterized.
27059955	2	9	dep	phosphorylation	286:300	arg1	Ser					303:305	Ser(33)	303:309	Ser(33)	303:309	The three O-GlcNAcylation (Ser(29), Ser(30), and Ser(48)) and two phosphorylation (Ser(33) and Ser(52)) serine sites on K18 are well characterized.
27059955	5	10	theme	site	843:846	arg1	s					848:848	the site(s)	839:849	the site(s) critical for regulating these functions	839:889	An immortalized hepatocyte cell line (HHL-17) stably expressing site-specific single, double, and triple O-GlcNAc and phosphomutants of K18 were used to identify the site(s) critical for regulating these functions.
27059955	11	11	dep	novel	1706:1710	arg1	positive					1713:1720	positive	1713:1720	positive	1713:1720	Here we report a novel, positive interplay between O-GlcNAcylation and phosphorylation at adjacent sites on K18 to regulate its fundamental properties.
27059955	6	12	theme	slower	1081:1086	arg1	migration					1088:1096	slower migration	1081:1096	slower migration	1081:1096	Keratin 18 mutants where O-GlcNAcylation at Ser(30) was abolished (K18-S30A) exhibited reduced phosphorylation induced solubility, increased stability, defective filament architecture, and slower migration.
27059955	6	13	theme	filament	1054:1061	arg1	architecture					1063:1074	defective filament architecture	1044:1074	defective filament architecture	1044:1074	Keratin 18 mutants where O-GlcNAcylation at Ser(30) was abolished (K18-S30A) exhibited reduced phosphorylation induced solubility, increased stability, defective filament architecture, and slower migration.
27059955	4	14	theme	functional	592:601	arg1	properties					603:612	the functional properties	588:612	the functional properties of K18	588:619	In this report, we investigated the site-specific interplay between these two modifications in regulating the functional properties of K18, like solubility, stability, and filament organization.
27059955	6	15	theme	induced	1003:1009	arg1	solubility					1011:1020	phosphorylation induced solubility	987:1020	phosphorylation induced solubility	987:1020	Keratin 18 mutants where O-GlcNAcylation at Ser(30) was abolished (K18-S30A) exhibited reduced phosphorylation induced solubility, increased stability, defective filament architecture, and slower migration.
27059955	9	16	theme	K18	1496:1498	arg1	properties					1482:1491	the functional properties	1467:1491	the functional properties of K18	1467:1498	These results indicate that O-GlcNAcylation at Ser(30) promotes phosphorylation at Ser(33) to regulate the functional properties of K18 and also impact cellular processes like migration.
27059955	6	17	theme	defective	1044:1052	arg1	architecture					1063:1074	defective filament architecture	1044:1074	defective filament architecture	1044:1074	Keratin 18 mutants where O-GlcNAcylation at Ser(30) was abolished (K18-S30A) exhibited reduced phosphorylation induced solubility, increased stability, defective filament architecture, and slower migration.
27059955	1	18	theme	intermediate	169:180	arg1	network					191:197	the major intermediate filament network	159:197	the major intermediate filament network of simple epithelia	159:217	Keratins 8/18 (K8/18) are phosphoglycoproteins and form the major intermediate filament network of simple epithelia.
27059955	10	19	from	O-GlcNAcylation	1551:1565	arg1	sites					1611:1615	the same or adjacent sites	1590:1615	the same or adjacent sites on most proteins	1590:1632	O-GlcNAcylation and phosphorylation on the same or adjacent sites on most proteins antagonize each other in regulating protein functions.
27059955	5	20	theme	critical	851:858	arg1	s					848:848	the site(s)	839:849	the site(s) critical for regulating these functions	839:889	An immortalized hepatocyte cell line (HHL-17) stably expressing site-specific single, double, and triple O-GlcNAc and phosphomutants of K18 were used to identify the site(s) critical for regulating these functions.
27059955	1	21	theme	filament	182:189	arg1	network					191:197	the major intermediate filament network	159:197	the major intermediate filament network of simple epithelia	159:217	Keratins 8/18 (K8/18) are phosphoglycoproteins and form the major intermediate filament network of simple epithelia.
27059955	10	22	theme	most	1620:1623	arg1	proteins					1625:1632	most proteins	1620:1632	most proteins	1620:1632	O-GlcNAcylation and phosphorylation on the same or adjacent sites on most proteins antagonize each other in regulating protein functions.
27059955	0	23	theme	Functional	0:9	arg1	Implications					11:22	Functional Implications	0:22	Functional Implications of O-GlcNAcylation-dependent Phosphorylation at a Proximal Site on Keratin 18.	0:101	Functional Implications of O-GlcNAcylation-dependent Phosphorylation at a Proximal Site on Keratin 18.
27059955	6	24	from	Ser	936:938	arg1	O-GlcNAcylation					917:931	O-GlcNAcylation	917:931	O-GlcNAcylation at Ser(30)	917:942	Keratin 18 mutants where O-GlcNAcylation at Ser(30) was abolished (K18-S30A) exhibited reduced phosphorylation induced solubility, increased stability, defective filament architecture, and slower migration.
27059955	3	25	theme	filament	459:466	arg1	organization					468:479	its filament organization	455:479	its filament organization	455:479	Both of these modifications have been reported to increase K18 solubility and regulate its filament organization.
27059955	9	26	from	Ser	1447:1449	arg1	phosphorylation					1428:1442	phosphorylation	1428:1442	phosphorylation at Ser(33) to regulate the functional properties of K18	1428:1498	These results indicate that O-GlcNAcylation at Ser(30) promotes phosphorylation at Ser(33) to regulate the functional properties of K18 and also impact cellular processes like migration.
27059955	0	27	theme	O-GlcNAcylation-dependent	27:51	arg1	Phosphorylation					53:67	O-GlcNAcylation-dependent Phosphorylation	27:67	O-GlcNAcylation-dependent Phosphorylation	27:67	Functional Implications of O-GlcNAcylation-dependent Phosphorylation at a Proximal Site on Keratin 18.
27059955	10	28	from	phosphorylation	1571:1585	arg1	sites					1611:1615	the same or adjacent sites	1590:1615	the same or adjacent sites on most proteins	1590:1632	O-GlcNAcylation and phosphorylation on the same or adjacent sites on most proteins antagonize each other in regulating protein functions.
27059955	9	29	theme	cellular	1516:1523	arg1	processes					1525:1533	cellular processes	1516:1533	cellular processes	1516:1533	These results indicate that O-GlcNAcylation at Ser(30) promotes phosphorylation at Ser(33) to regulate the functional properties of K18 and also impact cellular processes like migration.
27059955	2	30	dep	O-GlcNAcylation	230:244	arg1	Ser					256:258	Ser(30)	256:262	Ser(30)	256:262	The three O-GlcNAcylation (Ser(29), Ser(30), and Ser(48)) and two phosphorylation (Ser(33) and Ser(52)) serine sites on K18 are well characterized.
27059955	2	30	dep	O-GlcNAcylation	230:244	arg1	Ser					247:249	Ser(29)	247:253	Ser(29)	247:253	The three O-GlcNAcylation (Ser(29), Ser(30), and Ser(48)) and two phosphorylation (Ser(33) and Ser(52)) serine sites on K18 are well characterized.
27059955	2	30	dep	O-GlcNAcylation	230:244	arg1	Ser					269:271	Ser(48)	269:275	Ser(48)	269:275	The three O-GlcNAcylation (Ser(29), Ser(30), and Ser(48)) and two phosphorylation (Ser(33) and Ser(52)) serine sites on K18 are well characterized.
27059955	6	31	theme	increased	1023:1031	arg1	stability					1033:1041	increased stability	1023:1041	increased stability	1023:1041	Keratin 18 mutants where O-GlcNAcylation at Ser(30) was abolished (K18-S30A) exhibited reduced phosphorylation induced solubility, increased stability, defective filament architecture, and slower migration.
27059955	1	32	theme	major	163:167	arg1	network					191:197	the major intermediate filament network	159:197	the major intermediate filament network of simple epithelia	159:217	Keratins 8/18 (K8/18) are phosphoglycoproteins and form the major intermediate filament network of simple epithelia.
27059955	10	33	theme	same	1594:1597	arg1	sites					1611:1615	the same or adjacent sites	1590:1615	the same or adjacent sites on most proteins	1590:1632	O-GlcNAcylation and phosphorylation on the same or adjacent sites on most proteins antagonize each other in regulating protein functions.
27059955	1	34	theme	epithelia	209:217	arg1	network					191:197	the major intermediate filament network	159:197	the major intermediate filament network of simple epithelia	159:217	Keratins 8/18 (K8/18) are phosphoglycoproteins and form the major intermediate filament network of simple epithelia.
27059955	1	35	gly	phosphoglycoproteins	129:148	arg1	Keratins					103:110	Keratins 8/18 (K8/18)	103:123	Keratins 8/18 (K8/18)	103:123	Keratins 8/18 (K8/18) are phosphoglycoproteins and form the major intermediate filament network of simple epithelia.
27059955	1	35	gly	phosphoglycoproteins	129:148	arg1	phosphoglycoproteins					129:148	phosphoglycoproteins	129:148	phosphoglycoproteins	129:148	Keratins 8/18 (K8/18) are phosphoglycoproteins and form the major intermediate filament network of simple epithelia.
27059955	5	36	theme	site-specific	741:753	arg1	O-GlcNAc					782:789	site-specific single, double, and triple O-GlcNAc	741:789	site-specific single, double, and triple O-GlcNAc	741:789	An immortalized hepatocyte cell line (HHL-17) stably expressing site-specific single, double, and triple O-GlcNAc and phosphomutants of K18 were used to identify the site(s) critical for regulating these functions.
27059955	0	37	theme	Phosphorylation	53:67	arg1	Implications					11:22	Functional Implications	0:22	Functional Implications of O-GlcNAcylation-dependent Phosphorylation at a Proximal Site on Keratin 18.	0:101	Functional Implications of O-GlcNAcylation-dependent Phosphorylation at a Proximal Site on Keratin 18.
27059955	5	38	theme	immortalized	680:691	arg1	HHL-17					715:720	HHL-17	715:720	HHL-17	715:720	An immortalized hepatocyte cell line (HHL-17) stably expressing site-specific single, double, and triple O-GlcNAc and phosphomutants of K18 were used to identify the site(s) critical for regulating these functions.
27059955	5	38	theme	immortalized	680:691	arg1	line					709:712	An immortalized hepatocyte cell line	677:712	An immortalized hepatocyte cell line (HHL-17) stably expressing site-specific single, double, and triple O-GlcNAc	677:789	An immortalized hepatocyte cell line (HHL-17) stably expressing site-specific single, double, and triple O-GlcNAc and phosphomutants of K18 were used to identify the site(s) critical for regulating these functions.
27059955	2	39	theme	serine	324:329	arg1	sites					331:335	The three O-GlcNAcylation (Ser(29), Ser(30), and Ser(48)) and two phosphorylation (Ser(33) and Ser(52)) serine sites	220:335	The three O-GlcNAcylation (Ser(29), Ser(30), and Ser(48)) and two phosphorylation (Ser(33) and Ser(52)) serine sites on K18	220:342	The three O-GlcNAcylation (Ser(29), Ser(30), and Ser(48)) and two phosphorylation (Ser(33) and Ser(52)) serine sites on K18 are well characterized.
27059955	5	40	theme	single	755:760	arg1	O-GlcNAc					782:789	site-specific single, double, and triple O-GlcNAc	741:789	site-specific single, double, and triple O-GlcNAc	741:789	An immortalized hepatocyte cell line (HHL-17) stably expressing site-specific single, double, and triple O-GlcNAc and phosphomutants of K18 were used to identify the site(s) critical for regulating these functions.
27059955	0	41	theme	Proximal	74:81	arg1	Site					83:86	a Proximal Site	72:86	a Proximal Site on Keratin 18	72:100	Functional Implications of O-GlcNAcylation-dependent Phosphorylation at a Proximal Site on Keratin 18.
27059955	0	42	from	Site	83:86	arg1	Keratin					91:97	Keratin 18	91:100	Keratin 18	91:100	Functional Implications of O-GlcNAcylation-dependent Phosphorylation at a Proximal Site on Keratin 18.
27059955	0	42	from	Site	83:86	arg1	Implications					11:22	Functional Implications	0:22	Functional Implications of O-GlcNAcylation-dependent Phosphorylation at a Proximal Site on Keratin 18.	0:101	Functional Implications of O-GlcNAcylation-dependent Phosphorylation at a Proximal Site on Keratin 18.
27059955	2	43	theme	O-GlcNAcylation	230:244	arg1	sites					331:335	The three O-GlcNAcylation (Ser(29), Ser(30), and Ser(48)) and two phosphorylation (Ser(33) and Ser(52)) serine sites	220:335	The three O-GlcNAcylation (Ser(29), Ser(30), and Ser(48)) and two phosphorylation (Ser(33) and Ser(52)) serine sites on K18	220:342	The three O-GlcNAcylation (Ser(29), Ser(30), and Ser(48)) and two phosphorylation (Ser(33) and Ser(52)) serine sites on K18 are well characterized.
27059955	4	44	theme	K18	617:619	arg1	properties					603:612	the functional properties	588:612	the functional properties of K18	588:619	In this report, we investigated the site-specific interplay between these two modifications in regulating the functional properties of K18, like solubility, stability, and filament organization.
27059955	5	45	theme	cell	704:707	arg1	HHL-17					715:720	HHL-17	715:720	HHL-17	715:720	An immortalized hepatocyte cell line (HHL-17) stably expressing site-specific single, double, and triple O-GlcNAc and phosphomutants of K18 were used to identify the site(s) critical for regulating these functions.
27059955	5	45	theme	cell	704:707	arg1	line					709:712	An immortalized hepatocyte cell line	677:712	An immortalized hepatocyte cell line (HHL-17) stably expressing site-specific single, double, and triple O-GlcNAc	677:789	An immortalized hepatocyte cell line (HHL-17) stably expressing site-specific single, double, and triple O-GlcNAc and phosphomutants of K18 were used to identify the site(s) critical for regulating these functions.
27059955	8	46	theme	K18	1256:1258	arg1	K18-S33A					1275:1282	K18-S33A	1275:1282	K18-S33A	1275:1282	Further to this, the K18 phosphomutant (K18-S33A) mimicked K18-S30A in its stability, filament organization, and cell migration.
27059955	8	46	theme	K18	1256:1258	arg1	phosphomutant					1260:1272	the K18 phosphomutant	1252:1272	the K18 phosphomutant (K18-S33A)	1252:1283	Further to this, the K18 phosphomutant (K18-S33A) mimicked K18-S30A in its stability, filament organization, and cell migration.
27059955	11	47	theme	adjacent	1779:1786	arg1	sites					1788:1792	adjacent sites	1779:1792	adjacent sites on K18	1779:1799	Here we report a novel, positive interplay between O-GlcNAcylation and phosphorylation at adjacent sites on K18 to regulate its fundamental properties.
27059955	5	48	theme	K18	813:815	arg1	phosphomutants					795:808	phosphomutants	795:808	phosphomutants of K18	795:815	An immortalized hepatocyte cell line (HHL-17) stably expressing site-specific single, double, and triple O-GlcNAc and phosphomutants of K18 were used to identify the site(s) critical for regulating these functions.
27059955	5	48	theme	K18	813:815	arg1	HHL-17					715:720	HHL-17	715:720	HHL-17	715:720	An immortalized hepatocyte cell line (HHL-17) stably expressing site-specific single, double, and triple O-GlcNAc and phosphomutants of K18 were used to identify the site(s) critical for regulating these functions.
27059955	5	48	theme	K18	813:815	arg1	line					709:712	An immortalized hepatocyte cell line	677:712	An immortalized hepatocyte cell line (HHL-17) stably expressing site-specific single, double, and triple O-GlcNAc	677:789	An immortalized hepatocyte cell line (HHL-17) stably expressing site-specific single, double, and triple O-GlcNAc and phosphomutants of K18 were used to identify the site(s) critical for regulating these functions.
27059955	10	49	theme	adjacent	1602:1609	arg1	sites					1611:1615	the same or adjacent sites	1590:1615	the same or adjacent sites on most proteins	1590:1632	O-GlcNAcylation and phosphorylation on the same or adjacent sites on most proteins antagonize each other in regulating protein functions.
27059955	11	50	theme	fundamental	1817:1827	arg1	properties					1829:1838	its fundamental properties	1813:1838	its fundamental properties	1813:1838	Here we report a novel, positive interplay between O-GlcNAcylation and phosphorylation at adjacent sites on K18 to regulate its fundamental properties.
27059955	5	51	used	used	822:825	arg2	HHL-17					715:720	HHL-17	715:720	HHL-17	715:720	An immortalized hepatocyte cell line (HHL-17) stably expressing site-specific single, double, and triple O-GlcNAc and phosphomutants of K18 were used to identify the site(s) critical for regulating these functions.
27059955	5	51	used	used	822:825	arg2	phosphomutants					795:808	phosphomutants	795:808	phosphomutants of K18	795:815	An immortalized hepatocyte cell line (HHL-17) stably expressing site-specific single, double, and triple O-GlcNAc and phosphomutants of K18 were used to identify the site(s) critical for regulating these functions.
27059955	5	51	used	used	822:825	arg2	line					709:712	An immortalized hepatocyte cell line	677:712	An immortalized hepatocyte cell line (HHL-17) stably expressing site-specific single, double, and triple O-GlcNAc	677:789	An immortalized hepatocyte cell line (HHL-17) stably expressing site-specific single, double, and triple O-GlcNAc and phosphomutants of K18 were used to identify the site(s) critical for regulating these functions.
27059955	6	52	dep	abolished	948:956	arg1	K18-S30A					959:966	K18-S30A	959:966	K18-S30A	959:966	Keratin 18 mutants where O-GlcNAcylation at Ser(30) was abolished (K18-S30A) exhibited reduced phosphorylation induced solubility, increased stability, defective filament architecture, and slower migration.
27059955	6	53	theme	reduced	979:985	arg1	solubility					1011:1020	phosphorylation induced solubility	987:1020	phosphorylation induced solubility	987:1020	Keratin 18 mutants where O-GlcNAcylation at Ser(30) was abolished (K18-S30A) exhibited reduced phosphorylation induced solubility, increased stability, defective filament architecture, and slower migration.
27059955	11	54	from	sites	1788:1792	arg1	O-GlcNAcylation					1740:1754	O-GlcNAcylation	1740:1754	O-GlcNAcylation	1740:1754	Here we report a novel, positive interplay between O-GlcNAcylation and phosphorylation at adjacent sites on K18 to regulate its fundamental properties.
27059955	11	54	from	sites	1788:1792	arg1	K18					1797:1799	K18	1797:1799	K18	1797:1799	Here we report a novel, positive interplay between O-GlcNAcylation and phosphorylation at adjacent sites on K18 to regulate its fundamental properties.
27059955	11	54	from	sites	1788:1792	arg1	phosphorylation					1760:1774	phosphorylation	1760:1774	phosphorylation at adjacent sites on K18	1760:1799	Here we report a novel, positive interplay between O-GlcNAcylation and phosphorylation at adjacent sites on K18 to regulate its fundamental properties.
27059955	4	55	theme	filament	654:661	arg1	organization					663:674	filament organization	654:674	filament organization	654:674	In this report, we investigated the site-specific interplay between these two modifications in regulating the functional properties of K18, like solubility, stability, and filament organization.
27059955	7	56	theme	phosphorylation	1151:1165	arg1	loss					1143:1146	loss	1143:1146	loss of phosphorylation	1143:1165	Interestingly, K18-S30A mutants also showed loss of phosphorylation at Ser(33), a modification known to regulate the solubility of K18.
27059955	7	57	theme	K18-S30A	1114:1121	arg1	mutants					1123:1129	K18-S30A mutants	1114:1129	K18-S30A mutants	1114:1129	Interestingly, K18-S30A mutants also showed loss of phosphorylation at Ser(33), a modification known to regulate the solubility of K18.
27059955	8	58	theme	filament	1321:1328	arg1	organization					1330:1341	filament organization	1321:1341	filament organization	1321:1341	Further to this, the K18 phosphomutant (K18-S33A) mimicked K18-S30A in its stability, filament organization, and cell migration.
27059955	6	59	dep	induced	1003:1009	arg1	phosphorylation					987:1001	phosphorylation	987:1001	phosphorylation	987:1001	Keratin 18 mutants where O-GlcNAcylation at Ser(30) was abolished (K18-S30A) exhibited reduced phosphorylation induced solubility, increased stability, defective filament architecture, and slower migration.
27059955	1	60	theme	simple	202:207	arg1	epithelia					209:217	simple epithelia	202:217	simple epithelia	202:217	Keratins 8/18 (K8/18) are phosphoglycoproteins and form the major intermediate filament network of simple epithelia.
27059955	5	61	theme	triple	775:780	arg1	O-GlcNAc					782:789	site-specific single, double, and triple O-GlcNAc	741:789	site-specific single, double, and triple O-GlcNAc	741:789	An immortalized hepatocyte cell line (HHL-17) stably expressing site-specific single, double, and triple O-GlcNAc and phosphomutants of K18 were used to identify the site(s) critical for regulating these functions.
27059955	5	62	theme	double	763:768	arg1	O-GlcNAc					782:789	site-specific single, double, and triple O-GlcNAc	741:789	site-specific single, double, and triple O-GlcNAc	741:789	An immortalized hepatocyte cell line (HHL-17) stably expressing site-specific single, double, and triple O-GlcNAc and phosphomutants of K18 were used to identify the site(s) critical for regulating these functions.
27059955	6	63	theme	Keratin	892:898	arg1	mutants					903:909	Keratin 18 mutants	892:909	Keratin 18 mutants where O-GlcNAcylation at Ser(30) was abolished (K18-S30A)	892:967	Keratin 18 mutants where O-GlcNAcylation at Ser(30) was abolished (K18-S30A) exhibited reduced phosphorylation induced solubility, increased stability, defective filament architecture, and slower migration.
27059955	5	64	theme	hepatocyte	693:702	arg1	HHL-17					715:720	HHL-17	715:720	HHL-17	715:720	An immortalized hepatocyte cell line (HHL-17) stably expressing site-specific single, double, and triple O-GlcNAc and phosphomutants of K18 were used to identify the site(s) critical for regulating these functions.
27059955	5	64	theme	hepatocyte	693:702	arg1	line					709:712	An immortalized hepatocyte cell line	677:712	An immortalized hepatocyte cell line (HHL-17) stably expressing site-specific single, double, and triple O-GlcNAc	677:789	An immortalized hepatocyte cell line (HHL-17) stably expressing site-specific single, double, and triple O-GlcNAc and phosphomutants of K18 were used to identify the site(s) critical for regulating these functions.
27059955	3	65	theme	K18	427:429	arg1	solubility					431:440	K18 solubility	427:440	K18 solubility	427:440	Both of these modifications have been reported to increase K18 solubility and regulate its filament organization.
27059955	4	66	theme	site-specific	518:530	arg1	interplay					532:540	the site-specific interplay	514:540	the site-specific interplay between these two modifications in regulating the functional properties of K18	514:619	In this report, we investigated the site-specific interplay between these two modifications in regulating the functional properties of K18, like solubility, stability, and filament organization.
27059955	10	67	from	sites	1611:1615	arg1	proteins					1625:1632	most proteins	1620:1632	most proteins	1620:1632	O-GlcNAcylation and phosphorylation on the same or adjacent sites on most proteins antagonize each other in regulating protein functions.
27059955	10	68	theme	protein	1670:1676	arg1	functions					1678:1686	protein functions	1670:1686	protein functions	1670:1686	O-GlcNAcylation and phosphorylation on the same or adjacent sites on most proteins antagonize each other in regulating protein functions.
17084817	5	0	theme	proximal	832:839	arg1	sites					841:845	proximal sites	832:845	proximal sites	832:845	Therefore, regulation of protein Ser/Thr phosphorylation and glycosylation at proximal sites can be interdependent and provides a potential mechanism of counter regulation.
17084817	2	1	theme	amino	357:361	arg1	acids					363:367	K18 amino acids 40-56	353:373	K18 amino acids 40-56	353:373	We used in vitro phosphorylation and O-GlcNAcylation of wild-type, phospho-Ser52, glyco-Ser48, and Ser-to-Ala mutant 17mer peptides (K18 amino acids 40-56), which include the major K18 glycosylation (Ser48) and phosphorylation (Ser52) sites, to address whether each modification blocks the other.
17084817	2	1	theme	amino	357:361	arg1	peptides					343:350	wild-type, phospho-Ser52, glyco-Ser48, and Ser-to-Ala mutant 17mer peptides	276:350	wild-type, phospho-Ser52, glyco-Ser48, and Ser-to-Ala mutant 17mer peptides (K18 amino acids 40-56)	276:374	We used in vitro phosphorylation and O-GlcNAcylation of wild-type, phospho-Ser52, glyco-Ser48, and Ser-to-Ala mutant 17mer peptides (K18 amino acids 40-56), which include the major K18 glycosylation (Ser48) and phosphorylation (Ser52) sites, to address whether each modification blocks the other.
17084817	2	2	dep	acids	363:367	arg1	40-56					369:373	40-56	369:373	40-56	369:373	We used in vitro phosphorylation and O-GlcNAcylation of wild-type, phospho-Ser52, glyco-Ser48, and Ser-to-Ala mutant 17mer peptides (K18 amino acids 40-56), which include the major K18 glycosylation (Ser48) and phosphorylation (Ser52) sites, to address whether each modification blocks the other.
17084817	4	3	theme	modifications	739:751	arg1	reciprocity					695:705	the reciprocity	691:705	the reciprocity of these two post-translational modifications	691:751	Our findings support the reciprocity of these two post-translational modifications.
17084817	3	4	theme	glyco-K18	521:529	arg1	peptide					531:537	The glyco-K18 peptide	517:537	The glyco-K18 peptide	517:537	The glyco-K18 peptide blocks Ser52 phosphorylation by protein kinase C, an in vivo K18 kinase, while the phospho-K18 peptide blocks its O-GlcNAcylation.
17084817	2	5	theme	K18	353:355	arg1	acids					363:367	K18 amino acids 40-56	353:373	K18 amino acids 40-56	353:373	We used in vitro phosphorylation and O-GlcNAcylation of wild-type, phospho-Ser52, glyco-Ser48, and Ser-to-Ala mutant 17mer peptides (K18 amino acids 40-56), which include the major K18 glycosylation (Ser48) and phosphorylation (Ser52) sites, to address whether each modification blocks the other.
17084817	2	5	theme	K18	353:355	arg1	peptides					343:350	wild-type, phospho-Ser52, glyco-Ser48, and Ser-to-Ala mutant 17mer peptides	276:350	wild-type, phospho-Ser52, glyco-Ser48, and Ser-to-Ala mutant 17mer peptides (K18 amino acids 40-56)	276:374	We used in vitro phosphorylation and O-GlcNAcylation of wild-type, phospho-Ser52, glyco-Ser48, and Ser-to-Ala mutant 17mer peptides (K18 amino acids 40-56), which include the major K18 glycosylation (Ser48) and phosphorylation (Ser52) sites, to address whether each modification blocks the other.
17084817	5	6	theme	phosphorylation	795:809	arg1	regulation					765:774	regulation	765:774	regulation of protein Ser/Thr phosphorylation and glycosylation at proximal sites	765:845	Therefore, regulation of protein Ser/Thr phosphorylation and glycosylation at proximal sites can be interdependent and provides a potential mechanism of counter regulation.
17084817	5	7	dep	regulation	915:924	arg1	counter					907:913	counter	907:913	counter	907:913	Therefore, regulation of protein Ser/Thr phosphorylation and glycosylation at proximal sites can be interdependent and provides a potential mechanism of counter regulation.
17084817	5	8	theme	Ser/Thr	787:793	arg1	phosphorylation					795:809	protein Ser/Thr phosphorylation	779:809	protein Ser/Thr phosphorylation	779:809	Therefore, regulation of protein Ser/Thr phosphorylation and glycosylation at proximal sites can be interdependent and provides a potential mechanism of counter regulation.
17084817	2	9	theme	phosphorylation	431:445	arg1	Ser52					448:452	Ser52	448:452	Ser52	448:452	We used in vitro phosphorylation and O-GlcNAcylation of wild-type, phospho-Ser52, glyco-Ser48, and Ser-to-Ala mutant 17mer peptides (K18 amino acids 40-56), which include the major K18 glycosylation (Ser48) and phosphorylation (Ser52) sites, to address whether each modification blocks the other.
17084817	2	9	theme	phosphorylation	431:445	arg1	sites					455:459	the major K18 glycosylation (Ser48) and phosphorylation (Ser52) sites	391:459	sites	455:459	We used in vitro phosphorylation and O-GlcNAcylation of wild-type, phospho-Ser52, glyco-Ser48, and Ser-to-Ala mutant 17mer peptides (K18 amino acids 40-56), which include the major K18 glycosylation (Ser48) and phosphorylation (Ser52) sites, to address whether each modification blocks the other.
17084817	3	10	theme	Ser52	546:550	arg1	phosphorylation					552:566	Ser52 phosphorylation	546:566	Ser52 phosphorylation by protein kinase C, an in vivo K18 kinase	546:609	The glyco-K18 peptide blocks Ser52 phosphorylation by protein kinase C, an in vivo K18 kinase, while the phospho-K18 peptide blocks its O-GlcNAcylation.
17084817	2	11	dep	wild-type	276:284	arg1	mutant					330:335	mutant	330:335	mutant	330:335	We used in vitro phosphorylation and O-GlcNAcylation of wild-type, phospho-Ser52, glyco-Ser48, and Ser-to-Ala mutant 17mer peptides (K18 amino acids 40-56), which include the major K18 glycosylation (Ser48) and phosphorylation (Ser52) sites, to address whether each modification blocks the other.
17084817	0	12	theme	Reciprocal	0:9	arg1	O-GlcNAcylation					28:42	Reciprocal keratin 18 Ser48 O-GlcNAcylation	0:42	Reciprocal keratin 18 Ser48 O-GlcNAcylation	0:42	Reciprocal keratin 18 Ser48 O-GlcNAcylation and Ser52 phosphorylation using peptide analysis.
17084817	2	13	used	used	223:226	arg2	We					220:221	We	220:221	We	220:221	We used in vitro phosphorylation and O-GlcNAcylation of wild-type, phospho-Ser52, glyco-Ser48, and Ser-to-Ala mutant 17mer peptides (K18 amino acids 40-56), which include the major K18 glycosylation (Ser48) and phosphorylation (Ser52) sites, to address whether each modification blocks the other.
17084817	1	14	theme	independent	191:201	arg1	populations					207:217	independent K18 populations	191:217	independent K18 populations	191:217	Phosphorylation and O-GlcNAcylation of keratin 18 (K18) are highly dynamic and involve primarily independent K18 populations.
17084817	0	15	theme	Ser48	22:26	arg1	O-GlcNAcylation					28:42	Reciprocal keratin 18 Ser48 O-GlcNAcylation	0:42	Reciprocal keratin 18 Ser48 O-GlcNAcylation	0:42	Reciprocal keratin 18 Ser48 O-GlcNAcylation and Ser52 phosphorylation using peptide analysis.
17084817	4	16	theme	post-translational	720:737	arg1	modifications					739:751	these two post-translational modifications	710:751	these two post-translational modifications	710:751	Our findings support the reciprocity of these two post-translational modifications.
17084817	2	17	dep	in	228:229	arg1	vitro					231:235	vitro	231:235	vitro	231:235	We used in vitro phosphorylation and O-GlcNAcylation of wild-type, phospho-Ser52, glyco-Ser48, and Ser-to-Ala mutant 17mer peptides (K18 amino acids 40-56), which include the major K18 glycosylation (Ser48) and phosphorylation (Ser52) sites, to address whether each modification blocks the other.
17084817	3	18	dep	in	592:593	arg1	vivo					595:598	vivo	595:598	vivo	595:598	The glyco-K18 peptide blocks Ser52 phosphorylation by protein kinase C, an in vivo K18 kinase, while the phospho-K18 peptide blocks its O-GlcNAcylation.
17084817	3	19	theme	kinase	579:584	arg1	C					586:586	protein kinase C	571:586	protein kinase C	571:586	The glyco-K18 peptide blocks Ser52 phosphorylation by protein kinase C, an in vivo K18 kinase, while the phospho-K18 peptide blocks its O-GlcNAcylation.
17084817	3	19	theme	kinase	579:584	arg1	kinase					604:609	an in vivo K18 kinase	589:609	an in vivo K18 kinase	589:609	The glyco-K18 peptide blocks Ser52 phosphorylation by protein kinase C, an in vivo K18 kinase, while the phospho-K18 peptide blocks its O-GlcNAcylation.
17084817	2	20	theme	K18	401:403	arg1	Ser48					420:424	Ser48	420:424	Ser48	420:424	We used in vitro phosphorylation and O-GlcNAcylation of wild-type, phospho-Ser52, glyco-Ser48, and Ser-to-Ala mutant 17mer peptides (K18 amino acids 40-56), which include the major K18 glycosylation (Ser48) and phosphorylation (Ser52) sites, to address whether each modification blocks the other.
17084817	2	20	theme	K18	401:403	arg1	glycosylation					405:417	the major K18 glycosylation (Ser48) and phosphorylation (Ser52) sites	391:459	glycosylation	405:417	We used in vitro phosphorylation and O-GlcNAcylation of wild-type, phospho-Ser52, glyco-Ser48, and Ser-to-Ala mutant 17mer peptides (K18 amino acids 40-56), which include the major K18 glycosylation (Ser48) and phosphorylation (Ser52) sites, to address whether each modification blocks the other.
17084817	3	21	theme	K18	600:602	arg1	C					586:586	protein kinase C	571:586	protein kinase C	571:586	The glyco-K18 peptide blocks Ser52 phosphorylation by protein kinase C, an in vivo K18 kinase, while the phospho-K18 peptide blocks its O-GlcNAcylation.
17084817	3	21	theme	K18	600:602	arg1	kinase					604:609	an in vivo K18 kinase	589:609	an in vivo K18 kinase	589:609	The glyco-K18 peptide blocks Ser52 phosphorylation by protein kinase C, an in vivo K18 kinase, while the phospho-K18 peptide blocks its O-GlcNAcylation.
17084817	5	22	theme	glycosylation	815:827	arg1	regulation					765:774	regulation	765:774	regulation of protein Ser/Thr phosphorylation and glycosylation at proximal sites	765:845	Therefore, regulation of protein Ser/Thr phosphorylation and glycosylation at proximal sites can be interdependent and provides a potential mechanism of counter regulation.
17084817	2	23	theme	major	395:399	arg1	Ser48					420:424	Ser48	420:424	Ser48	420:424	We used in vitro phosphorylation and O-GlcNAcylation of wild-type, phospho-Ser52, glyco-Ser48, and Ser-to-Ala mutant 17mer peptides (K18 amino acids 40-56), which include the major K18 glycosylation (Ser48) and phosphorylation (Ser52) sites, to address whether each modification blocks the other.
17084817	2	23	theme	major	395:399	arg1	glycosylation					405:417	the major K18 glycosylation (Ser48) and phosphorylation (Ser52) sites	391:459	glycosylation	405:417	We used in vitro phosphorylation and O-GlcNAcylation of wild-type, phospho-Ser52, glyco-Ser48, and Ser-to-Ala mutant 17mer peptides (K18 amino acids 40-56), which include the major K18 glycosylation (Ser48) and phosphorylation (Ser52) sites, to address whether each modification blocks the other.
17084817	5	24	theme	protein	779:785	arg1	phosphorylation					795:809	protein Ser/Thr phosphorylation	779:809	protein Ser/Thr phosphorylation	779:809	Therefore, regulation of protein Ser/Thr phosphorylation and glycosylation at proximal sites can be interdependent and provides a potential mechanism of counter regulation.
17084817	2	25	theme	in	228:229	arg1	phosphorylation					237:251	in vitro phosphorylation	228:251	in vitro phosphorylation	228:251	We used in vitro phosphorylation and O-GlcNAcylation of wild-type, phospho-Ser52, glyco-Ser48, and Ser-to-Ala mutant 17mer peptides (K18 amino acids 40-56), which include the major K18 glycosylation (Ser48) and phosphorylation (Ser52) sites, to address whether each modification blocks the other.
17084817	1	26	theme	keratin	133:139	arg1	O-GlcNAcylation					114:128	O-GlcNAcylation	114:128	O-GlcNAcylation	114:128	Phosphorylation and O-GlcNAcylation of keratin 18 (K18) are highly dynamic and involve primarily independent K18 populations.
17084817	1	26	theme	keratin	133:139	arg1	Phosphorylation					94:108	Phosphorylation	94:108	Phosphorylation	94:108	Phosphorylation and O-GlcNAcylation of keratin 18 (K18) are highly dynamic and involve primarily independent K18 populations.
17084817	0	27	theme	Ser52	48:52	arg1	phosphorylation					54:68	Ser52 phosphorylation	48:68	Ser52 phosphorylation	48:68	Reciprocal keratin 18 Ser48 O-GlcNAcylation and Ser52 phosphorylation using peptide analysis.
17084817	3	28	theme	protein	571:577	arg1	C					586:586	protein kinase C	571:586	protein kinase C	571:586	The glyco-K18 peptide blocks Ser52 phosphorylation by protein kinase C, an in vivo K18 kinase, while the phospho-K18 peptide blocks its O-GlcNAcylation.
17084817	3	28	theme	protein	571:577	arg1	kinase					604:609	an in vivo K18 kinase	589:609	an in vivo K18 kinase	589:609	The glyco-K18 peptide blocks Ser52 phosphorylation by protein kinase C, an in vivo K18 kinase, while the phospho-K18 peptide blocks its O-GlcNAcylation.
17084817	3	29	theme	in	592:593	arg1	C					586:586	protein kinase C	571:586	protein kinase C	571:586	The glyco-K18 peptide blocks Ser52 phosphorylation by protein kinase C, an in vivo K18 kinase, while the phospho-K18 peptide blocks its O-GlcNAcylation.
17084817	3	29	theme	in	592:593	arg1	kinase					604:609	an in vivo K18 kinase	589:609	an in vivo K18 kinase	589:609	The glyco-K18 peptide blocks Ser52 phosphorylation by protein kinase C, an in vivo K18 kinase, while the phospho-K18 peptide blocks its O-GlcNAcylation.
17084817	2	30	theme	wild-type	276:284	arg1	acids					363:367	K18 amino acids 40-56	353:373	K18 amino acids 40-56	353:373	We used in vitro phosphorylation and O-GlcNAcylation of wild-type, phospho-Ser52, glyco-Ser48, and Ser-to-Ala mutant 17mer peptides (K18 amino acids 40-56), which include the major K18 glycosylation (Ser48) and phosphorylation (Ser52) sites, to address whether each modification blocks the other.
17084817	2	30	theme	wild-type	276:284	arg1	peptides					343:350	wild-type, phospho-Ser52, glyco-Ser48, and Ser-to-Ala mutant 17mer peptides	276:350	wild-type, phospho-Ser52, glyco-Ser48, and Ser-to-Ala mutant 17mer peptides (K18 amino acids 40-56)	276:374	We used in vitro phosphorylation and O-GlcNAcylation of wild-type, phospho-Ser52, glyco-Ser48, and Ser-to-Ala mutant 17mer peptides (K18 amino acids 40-56), which include the major K18 glycosylation (Ser48) and phosphorylation (Ser52) sites, to address whether each modification blocks the other.
17084817	5	31	from	sites	841:845	arg1	regulation					765:774	regulation	765:774	regulation of protein Ser/Thr phosphorylation and glycosylation at proximal sites	765:845	Therefore, regulation of protein Ser/Thr phosphorylation and glycosylation at proximal sites can be interdependent and provides a potential mechanism of counter regulation.
17084817	2	32	theme	peptides	343:350	arg1	O-GlcNAcylation					257:271	O-GlcNAcylation	257:271	O-GlcNAcylation	257:271	We used in vitro phosphorylation and O-GlcNAcylation of wild-type, phospho-Ser52, glyco-Ser48, and Ser-to-Ala mutant 17mer peptides (K18 amino acids 40-56), which include the major K18 glycosylation (Ser48) and phosphorylation (Ser52) sites, to address whether each modification blocks the other.
17084817	2	32	theme	peptides	343:350	arg1	phosphorylation					237:251	in vitro phosphorylation	228:251	in vitro phosphorylation	228:251	We used in vitro phosphorylation and O-GlcNAcylation of wild-type, phospho-Ser52, glyco-Ser48, and Ser-to-Ala mutant 17mer peptides (K18 amino acids 40-56), which include the major K18 glycosylation (Ser48) and phosphorylation (Ser52) sites, to address whether each modification blocks the other.
17084817	5	33	theme	regulation	915:924	arg1	mechanism					894:902	a potential mechanism	882:902	a potential mechanism of counter regulation	882:924	Therefore, regulation of protein Ser/Thr phosphorylation and glycosylation at proximal sites can be interdependent and provides a potential mechanism of counter regulation.
17084817	2	34	theme	17mer	337:341	arg1	acids					363:367	K18 amino acids 40-56	353:373	K18 amino acids 40-56	353:373	We used in vitro phosphorylation and O-GlcNAcylation of wild-type, phospho-Ser52, glyco-Ser48, and Ser-to-Ala mutant 17mer peptides (K18 amino acids 40-56), which include the major K18 glycosylation (Ser48) and phosphorylation (Ser52) sites, to address whether each modification blocks the other.
17084817	2	34	theme	17mer	337:341	arg1	peptides					343:350	wild-type, phospho-Ser52, glyco-Ser48, and Ser-to-Ala mutant 17mer peptides	276:350	wild-type, phospho-Ser52, glyco-Ser48, and Ser-to-Ala mutant 17mer peptides (K18 amino acids 40-56)	276:374	We used in vitro phosphorylation and O-GlcNAcylation of wild-type, phospho-Ser52, glyco-Ser48, and Ser-to-Ala mutant 17mer peptides (K18 amino acids 40-56), which include the major K18 glycosylation (Ser48) and phosphorylation (Ser52) sites, to address whether each modification blocks the other.
17084817	0	35	theme	peptide	76:82	arg1	analysis					84:91	peptide analysis	76:91	peptide analysis	76:91	Reciprocal keratin 18 Ser48 O-GlcNAcylation and Ser52 phosphorylation using peptide analysis.
17084817	3	36	theme	phospho-K18	622:632	arg1	peptide					634:640	the phospho-K18 peptide	618:640	the phospho-K18 peptide	618:640	The glyco-K18 peptide blocks Ser52 phosphorylation by protein kinase C, an in vivo K18 kinase, while the phospho-K18 peptide blocks its O-GlcNAcylation.
17084817	1	37	theme	K18	203:205	arg1	populations					207:217	independent K18 populations	191:217	independent K18 populations	191:217	Phosphorylation and O-GlcNAcylation of keratin 18 (K18) are highly dynamic and involve primarily independent K18 populations.
17084817	5	38	theme	potential	884:892	arg1	mechanism					894:902	a potential mechanism	882:902	a potential mechanism of counter regulation	882:924	Therefore, regulation of protein Ser/Thr phosphorylation and glycosylation at proximal sites can be interdependent and provides a potential mechanism of counter regulation.
17084817	0	39	theme	keratin	11:17	arg1	O-GlcNAcylation					28:42	Reciprocal keratin 18 Ser48 O-GlcNAcylation	0:42	Reciprocal keratin 18 Ser48 O-GlcNAcylation	0:42	Reciprocal keratin 18 Ser48 O-GlcNAcylation and Ser52 phosphorylation using peptide analysis.
9079710	0	0	theme	O-linked	73:80	arg1	N-acetylglucosamine					82:100	O-linked N-acetylglucosamine	73:100	O-linked N-acetylglucosamine	73:100	Mitotic arrest with nocodazole induces selective changes in the level of O-linked N-acetylglucosamine and accumulation of incompletely processed N-glycans on proteins from HT29 cells.
9079710	5	1	theme	colon	697:701	arg1	line					715:718	human colon cancer cell line	691:718	the human colon cancer cell line HT29	687:723	268, 4465-4472) have shown that mitotic arrest with microtubule-destabilizing agents such as nocodazole causes an increase in the O-GlcNAc levels on keratins in the human colon cancer cell line HT29.
9079710	9	2	theme	pore	1230:1233	arg1	protein					1235:1241	the nuclear pore protein	1218:1241	the nuclear pore protein p62	1218:1245	The levels of O-GlcNAc on other proteins, including the nuclear pore protein p62 and the transcription factor Sp1, are not significantly affected by this treatment.
9079710	5	3	dep	268	526:528	arg1	4465-4472					531:539	4465-4472	531:539	4465-4472	531:539	268, 4465-4472) have shown that mitotic arrest with microtubule-destabilizing agents such as nocodazole causes an increase in the O-GlcNAc levels on keratins in the human colon cancer cell line HT29.
9079710	0	4	from	cells	177:181	arg1	proteins					158:165	proteins	158:165	proteins from HT29 cells	158:181	Mitotic arrest with nocodazole induces selective changes in the level of O-linked N-acetylglucosamine and accumulation of incompletely processed N-glycans on proteins from HT29 cells.
9079710	5	5	theme	cancer	703:708	arg1	line					715:718	human colon cancer cell line	691:718	the human colon cancer cell line HT29	687:723	268, 4465-4472) have shown that mitotic arrest with microtubule-destabilizing agents such as nocodazole causes an increase in the O-GlcNAc levels on keratins in the human colon cancer cell line HT29.
9079710	6	6	theme	many	825:828	arg1	proteins					830:837	many proteins	825:837	many proteins	825:837	We have sought to determine whether this increase in glycosylation is a general (i.e. occurring on many proteins) or a limited (i.e. occurring only on the keratins) process.
9079710	5	7	theme	microtubule-destabilizing	578:602	arg1	agents					604:609	microtubule-destabilizing agents	578:609	microtubule-destabilizing agents such as nocodazole	578:628	268, 4465-4472) have shown that mitotic arrest with microtubule-destabilizing agents such as nocodazole causes an increase in the O-GlcNAc levels on keratins in the human colon cancer cell line HT29.
9079710	5	7	theme	microtubule-destabilizing	578:602	arg1	nocodazole					619:628	nocodazole	619:628	nocodazole	619:628	268, 4465-4472) have shown that mitotic arrest with microtubule-destabilizing agents such as nocodazole causes an increase in the O-GlcNAc levels on keratins in the human colon cancer cell line HT29.
9079710	12	8	gly	glycosylation	1717:1729	arg1	keratins					1738:1745	the keratins	1734:1745	the keratins	1734:1745	Potential mechanisms for this and the change in glycosylation of the keratins are discussed.
9079710	3	9	dep	Biol	514:517	arg1	M.					498:499	M.	498:499	M.	498:499	Previous workers (Chou, C. F., and Omary, M. B. (1993) J. Biol.
9079710	3	9	dep	Biol	514:517	arg1	F.					483:484	F.	483:484	F.	483:484	Previous workers (Chou, C. F., and Omary, M. B. (1993) J. Biol.
9079710	3	9	dep	Biol	514:517	arg1	workers					465:471	Previous workers	456:471	Previous workers (Chou, C. F., and Omary, M. B. (1993)	456:509	Previous workers (Chou, C. F., and Omary, M. B. (1993) J. Biol.
9079710	12	10	from	change	1707:1712	arg1	glycosylation					1717:1729	glycosylation	1717:1729	glycosylation of the keratins	1717:1745	Potential mechanisms for this and the change in glycosylation of the keratins are discussed.
9079710	10	11	theme	O-GlcNAc	1473:1480	arg1	removal					1462:1468	removal	1462:1468	removal	1462:1468	In agreement with these findings, nocodazole treatment caused no change in the activity of the enzymes responsible for addition or removal of O-GlcNAc as determined by direct in vitro assay.
9079710	10	11	theme	O-GlcNAc	1473:1480	arg1	addition					1450:1457	addition	1450:1457	addition	1450:1457	In agreement with these findings, nocodazole treatment caused no change in the activity of the enzymes responsible for addition or removal of O-GlcNAc as determined by direct in vitro assay.
9079710	8	12	from	changes	1092:1098	arg1	O-GlcNAc					1103:1110	O-GlcNAc	1103:1110	O-GlcNAc	1103:1110	Our results suggest that the changes in O-GlcNAc induced by nocodazole are selective for the keratins.
9079710	5	13	from	increase	640:647	arg1	keratins					675:682	keratins	675:682	keratins in the human colon cancer cell line HT29	675:723	268, 4465-4472) have shown that mitotic arrest with microtubule-destabilizing agents such as nocodazole causes an increase in the O-GlcNAc levels on keratins in the human colon cancer cell line HT29.
9079710	5	13	from	increase	640:647	arg1	levels					665:670	the O-GlcNAc levels	652:670	the O-GlcNAc levels on keratins in the human colon cancer cell line HT29	652:723	268, 4465-4472) have shown that mitotic arrest with microtubule-destabilizing agents such as nocodazole causes an increase in the O-GlcNAc levels on keratins in the human colon cancer cell line HT29.
9079710	0	14	theme	N-acetylglucosamine	82:100	arg1	level					64:68	the level	60:68	the level of O-linked N-acetylglucosamine	60:100	Mitotic arrest with nocodazole induces selective changes in the level of O-linked N-acetylglucosamine and accumulation of incompletely processed N-glycans on proteins from HT29 cells.
9079710	11	15	theme	GlcNAc	1631:1636	arg1	residues					1638:1645	terminal GlcNAc residues	1622:1645	terminal GlcNAc residues on numerous proteins	1622:1666	Interestingly, nocodazole treatment did cause a dramatic increase in modification of N-glycans with terminal GlcNAc residues on numerous proteins.
9079710	9	16	theme	factor	1269:1274	arg1	Sp1					1276:1278	the transcription factor Sp1	1251:1278	the transcription factor Sp1	1251:1278	The levels of O-GlcNAc on other proteins, including the nuclear pore protein p62 and the transcription factor Sp1, are not significantly affected by this treatment.
9079710	1	17	theme	nuclear	283:289	arg1	proteins					307:314	nuclear and cytoplasmic proteins	283:314	nuclear and cytoplasmic proteins	283:314	O-Linked N-acetylglucosamine (O-GlcNAc) is a ubiquitous and abundant protein modification found on nuclear and cytoplasmic proteins.
9079710	0	18	from	changes	49:55	arg1	level					64:68	the level	60:68	the level of O-linked N-acetylglucosamine	60:100	Mitotic arrest with nocodazole induces selective changes in the level of O-linked N-acetylglucosamine and accumulation of incompletely processed N-glycans on proteins from HT29 cells.
9079710	0	18	from	changes	49:55	arg1	proteins					158:165	proteins	158:165	proteins from HT29 cells	158:181	Mitotic arrest with nocodazole induces selective changes in the level of O-linked N-acetylglucosamine and accumulation of incompletely processed N-glycans on proteins from HT29 cells.
9079710	0	19	from	proteins	158:165	arg1	accumulation					106:117	accumulation	106:117	accumulation of incompletely processed N-glycans on proteins from HT29 cells	106:181	Mitotic arrest with nocodazole induces selective changes in the level of O-linked N-acetylglucosamine and accumulation of incompletely processed N-glycans on proteins from HT29 cells.
9079710	0	19	from	proteins	158:165	arg1	changes					49:55	selective changes	39:55	selective changes in the level of O-linked N-acetylglucosamine	39:100	Mitotic arrest with nocodazole induces selective changes in the level of O-linked N-acetylglucosamine and accumulation of incompletely processed N-glycans on proteins from HT29 cells.
9079710	9	20	theme	nuclear	1222:1228	arg1	protein					1235:1241	the nuclear pore protein	1218:1241	the nuclear pore protein p62	1218:1245	The levels of O-GlcNAc on other proteins, including the nuclear pore protein p62 and the transcription factor Sp1, are not significantly affected by this treatment.
9079710	5	21	theme	cell	710:713	arg1	line					715:718	human colon cancer cell line	691:718	the human colon cancer cell line HT29	687:723	268, 4465-4472) have shown that mitotic arrest with microtubule-destabilizing agents such as nocodazole causes an increase in the O-GlcNAc levels on keratins in the human colon cancer cell line HT29.
9079710	3	22	dep	F.	483:484	arg1	B					501:501	B	501:501	Chou, C. F., and Omary, M. B. (1993)	474:509	Previous workers (Chou, C. F., and Omary, M. B. (1993) J. Biol.
9079710	1	23	theme	O-Linked	184:191	arg1	N-acetylglucosamine					193:211	O-Linked N-acetylglucosamine	184:211	O-Linked N-acetylglucosamine (O-GlcNAc)	184:222	O-Linked N-acetylglucosamine (O-GlcNAc) is a ubiquitous and abundant protein modification found on nuclear and cytoplasmic proteins.
9079710	1	23	theme	O-Linked	184:191	arg1	modification					261:272	a ubiquitous and abundant protein modification	227:272	a ubiquitous and abundant protein modification found on nuclear and cytoplasmic proteins	227:314	O-Linked N-acetylglucosamine (O-GlcNAc) is a ubiquitous and abundant protein modification found on nuclear and cytoplasmic proteins.
9079710	1	23	theme	O-Linked	184:191	arg1	O-GlcNAc					214:221	O-GlcNAc	214:221	O-GlcNAc	214:221	O-Linked N-acetylglucosamine (O-GlcNAc) is a ubiquitous and abundant protein modification found on nuclear and cytoplasmic proteins.
9079710	10	24	theme	direct	1499:1504	arg1	assay					1515:1519	direct in vitro assay	1499:1519	direct in vitro assay	1499:1519	In agreement with these findings, nocodazole treatment caused no change in the activity of the enzymes responsible for addition or removal of O-GlcNAc as determined by direct in vitro assay.
9079710	6	25	theme	general	798:804	arg1	increase					767:774	this increase	762:774	this increase in glycosylation	762:791	We have sought to determine whether this increase in glycosylation is a general (i.e. occurring on many proteins) or a limited (i.e. occurring only on the keratins) process.
9079710	6	25	theme	general	798:804	arg1	process					891:897	a general (i.e. occurring on many proteins) or a limited (i.e. occurring only on the keratins) process	796:897	a general (i.e. occurring on many proteins) or a limited (i.e. occurring only on the keratins) process	796:897	We have sought to determine whether this increase in glycosylation is a general (i.e. occurring on many proteins) or a limited (i.e. occurring only on the keratins) process.
9079710	5	26	theme	mitotic	558:564	arg1	arrest					566:571	mitotic arrest	558:571	mitotic arrest with microtubule-destabilizing agents such as nocodazole	558:628	268, 4465-4472) have shown that mitotic arrest with microtubule-destabilizing agents such as nocodazole causes an increase in the O-GlcNAc levels on keratins in the human colon cancer cell line HT29.
9079710	2	27	theme	evidence	334:341	arg1	lines					325:329	Several lines	317:329	Several lines of evidence	317:341	Several lines of evidence suggest that it is a highly dynamic modification and that the levels of this sugar on proteins may be regulated.
9079710	11	28	theme	dramatic	1570:1577	arg1	increase					1579:1586	a dramatic increase	1568:1586	a dramatic increase in modification of N-glycans with terminal GlcNAc residues on numerous proteins	1568:1666	Interestingly, nocodazole treatment did cause a dramatic increase in modification of N-glycans with terminal GlcNAc residues on numerous proteins.
9079710	9	29	from	levels	1170:1175	arg1	proteins					1198:1205	other proteins	1192:1205	other proteins	1192:1205	The levels of O-GlcNAc on other proteins, including the nuclear pore protein p62 and the transcription factor Sp1, are not significantly affected by this treatment.
9079710	9	29	from	levels	1170:1175	arg1	protein					1235:1241	the nuclear pore protein	1218:1241	the nuclear pore protein p62	1218:1245	The levels of O-GlcNAc on other proteins, including the nuclear pore protein p62 and the transcription factor Sp1, are not significantly affected by this treatment.
9079710	9	29	from	levels	1170:1175	arg1	Sp1					1276:1278	the transcription factor Sp1	1251:1278	the transcription factor Sp1	1251:1278	The levels of O-GlcNAc on other proteins, including the nuclear pore protein p62 and the transcription factor Sp1, are not significantly affected by this treatment.
9079710	0	30	theme	Mitotic	0:6	arg1	arrest					8:13	Mitotic arrest	0:13	Mitotic arrest with nocodazole	0:29	Mitotic arrest with nocodazole induces selective changes in the level of O-linked N-acetylglucosamine and accumulation of incompletely processed N-glycans on proteins from HT29 cells.
9079710	10	31	theme	in	1506:1507	arg1	assay					1515:1519	direct in vitro assay	1499:1519	direct in vitro assay	1499:1519	In agreement with these findings, nocodazole treatment caused no change in the activity of the enzymes responsible for addition or removal of O-GlcNAc as determined by direct in vitro assay.
9079710	5	32	dep	line	715:718	arg1	HT29					720:723	HT29	720:723	the human colon cancer cell line HT29	687:723	268, 4465-4472) have shown that mitotic arrest with microtubule-destabilizing agents such as nocodazole causes an increase in the O-GlcNAc levels on keratins in the human colon cancer cell line HT29.
9079710	11	33	theme	terminal	1622:1629	arg1	residues					1638:1645	terminal GlcNAc residues	1622:1645	terminal GlcNAc residues on numerous proteins	1622:1666	Interestingly, nocodazole treatment did cause a dramatic increase in modification of N-glycans with terminal GlcNAc residues on numerous proteins.
9079710	10	34	with	agreement	1334:1342	arg1	findings					1355:1362	these findings	1349:1362	these findings	1349:1362	In agreement with these findings, nocodazole treatment caused no change in the activity of the enzymes responsible for addition or removal of O-GlcNAc as determined by direct in vitro assay.
9079710	10	35	dep	in	1506:1507	arg1	vitro					1509:1513	vitro	1509:1513	vitro	1509:1513	In agreement with these findings, nocodazole treatment caused no change in the activity of the enzymes responsible for addition or removal of O-GlcNAc as determined by direct in vitro assay.
9079710	1	36	theme	cytoplasmic	295:305	arg1	proteins					307:314	nuclear and cytoplasmic proteins	283:314	nuclear and cytoplasmic proteins	283:314	O-Linked N-acetylglucosamine (O-GlcNAc) is a ubiquitous and abundant protein modification found on nuclear and cytoplasmic proteins.
9079710	0	37	theme	processed	135:143	arg1	N-glycans					145:153	incompletely processed N-glycans	122:153	incompletely processed N-glycans on proteins from HT29 cells	122:181	Mitotic arrest with nocodazole induces selective changes in the level of O-linked N-acetylglucosamine and accumulation of incompletely processed N-glycans on proteins from HT29 cells.
9079710	12	38	theme	Potential	1669:1677	arg1	mechanisms					1679:1688	Potential mechanisms	1669:1688	Potential mechanisms for this	1669:1697	Potential mechanisms for this and the change in glycosylation of the keratins are discussed.
9079710	2	39	from	levels	405:410	arg1	proteins					429:436	proteins	429:436	proteins	429:436	Several lines of evidence suggest that it is a highly dynamic modification and that the levels of this sugar on proteins may be regulated.
9079710	5	40	from	keratins	675:682	arg1	line					715:718	human colon cancer cell line	691:718	the human colon cancer cell line HT29	687:723	268, 4465-4472) have shown that mitotic arrest with microtubule-destabilizing agents such as nocodazole causes an increase in the O-GlcNAc levels on keratins in the human colon cancer cell line HT29.
9079710	5	40	from	keratins	675:682	arg1	increase					640:647	an increase	637:647	an increase in the O-GlcNAc levels on keratins in the human colon cancer cell line HT29	637:723	268, 4465-4472) have shown that mitotic arrest with microtubule-destabilizing agents such as nocodazole causes an increase in the O-GlcNAc levels on keratins in the human colon cancer cell line HT29.
9079710	2	41	theme	Several	317:323	arg1	lines					325:329	Several lines	317:329	Several lines of evidence	317:341	Several lines of evidence suggest that it is a highly dynamic modification and that the levels of this sugar on proteins may be regulated.
9079710	11	42	with	modification	1591:1602	arg1	residues					1638:1645	terminal GlcNAc residues	1622:1645	terminal GlcNAc residues on numerous proteins	1622:1666	Interestingly, nocodazole treatment did cause a dramatic increase in modification of N-glycans with terminal GlcNAc residues on numerous proteins.
9079710	2	43	theme	sugar	420:424	arg1	levels					405:410	the levels	401:410	the levels of this sugar on proteins	401:436	Several lines of evidence suggest that it is a highly dynamic modification and that the levels of this sugar on proteins may be regulated.
9079710	0	44	theme	selective	39:47	arg1	changes					49:55	selective changes	39:55	selective changes in the level of O-linked N-acetylglucosamine	39:100	Mitotic arrest with nocodazole induces selective changes in the level of O-linked N-acetylglucosamine and accumulation of incompletely processed N-glycans on proteins from HT29 cells.
9079710	10	45	theme	nocodazole	1365:1374	arg1	treatment					1376:1384	nocodazole treatment	1365:1384	nocodazole treatment	1365:1384	In agreement with these findings, nocodazole treatment caused no change in the activity of the enzymes responsible for addition or removal of O-GlcNAc as determined by direct in vitro assay.
9079710	7	46	theme	microtubule-destabilizing	942:966	arg1	agents					968:973	the microtubule-destabilizing agents	938:973	the microtubule-destabilizing agents	938:973	A general increase would suggest that the microtubule-destabilizing agents were somehow affecting the enzymes responsible for addition and/or removal of O-GlcNAc.
9079710	9	47	theme	other	1192:1196	arg1	proteins					1198:1205	other proteins	1192:1205	other proteins	1192:1205	The levels of O-GlcNAc on other proteins, including the nuclear pore protein p62 and the transcription factor Sp1, are not significantly affected by this treatment.
9079710	9	47	theme	other	1192:1196	arg1	protein					1235:1241	the nuclear pore protein	1218:1241	the nuclear pore protein p62	1218:1245	The levels of O-GlcNAc on other proteins, including the nuclear pore protein p62 and the transcription factor Sp1, are not significantly affected by this treatment.
9079710	9	47	theme	other	1192:1196	arg1	Sp1					1276:1278	the transcription factor Sp1	1251:1278	the transcription factor Sp1	1251:1278	The levels of O-GlcNAc on other proteins, including the nuclear pore protein p62 and the transcription factor Sp1, are not significantly affected by this treatment.
9079710	6	48	dep	general	798:804	arg1	i.e.					807:810	i.e.	807:810	i.e.	807:810	We have sought to determine whether this increase in glycosylation is a general (i.e. occurring on many proteins) or a limited (i.e. occurring only on the keratins) process.
9079710	9	49	theme	transcription	1255:1267	arg1	Sp1					1276:1278	the transcription factor Sp1	1251:1278	the transcription factor Sp1	1251:1278	The levels of O-GlcNAc on other proteins, including the nuclear pore protein p62 and the transcription factor Sp1, are not significantly affected by this treatment.
9079710	0	50	theme	N-glycans	145:153	arg1	accumulation					106:117	accumulation	106:117	accumulation of incompletely processed N-glycans on proteins from HT29 cells	106:181	Mitotic arrest with nocodazole induces selective changes in the level of O-linked N-acetylglucosamine and accumulation of incompletely processed N-glycans on proteins from HT29 cells.
9079710	0	50	theme	N-glycans	145:153	arg1	changes					49:55	selective changes	39:55	selective changes in the level of O-linked N-acetylglucosamine	39:100	Mitotic arrest with nocodazole induces selective changes in the level of O-linked N-acetylglucosamine and accumulation of incompletely processed N-glycans on proteins from HT29 cells.
9079710	5	51	from	levels	665:670	arg1	keratins					675:682	keratins	675:682	keratins in the human colon cancer cell line HT29	675:723	268, 4465-4472) have shown that mitotic arrest with microtubule-destabilizing agents such as nocodazole causes an increase in the O-GlcNAc levels on keratins in the human colon cancer cell line HT29.
9079710	0	52	link	O-linked	73:80	arg1	N-acetylglucosamine					82:100	O-linked N-acetylglucosamine	73:100	O-linked N-acetylglucosamine	73:100	Mitotic arrest with nocodazole induces selective changes in the level of O-linked N-acetylglucosamine and accumulation of incompletely processed N-glycans on proteins from HT29 cells.
9079710	3	53	theme	Previous	456:463	arg1	M.					498:499	M.	498:499	M.	498:499	Previous workers (Chou, C. F., and Omary, M. B. (1993) J. Biol.
9079710	3	53	theme	Previous	456:463	arg1	F.					483:484	F.	483:484	F.	483:484	Previous workers (Chou, C. F., and Omary, M. B. (1993) J. Biol.
9079710	3	53	theme	Previous	456:463	arg1	workers					465:471	Previous workers	456:471	Previous workers (Chou, C. F., and Omary, M. B. (1993)	456:509	Previous workers (Chou, C. F., and Omary, M. B. (1993) J. Biol.
9079710	6	54	from	increase	767:774	arg1	glycosylation					779:791	glycosylation	779:791	glycosylation	779:791	We have sought to determine whether this increase in glycosylation is a general (i.e. occurring on many proteins) or a limited (i.e. occurring only on the keratins) process.
9079710	6	55	theme	limited	845:851	arg1	increase					767:774	this increase	762:774	this increase in glycosylation	762:791	We have sought to determine whether this increase in glycosylation is a general (i.e. occurring on many proteins) or a limited (i.e. occurring only on the keratins) process.
9079710	6	55	theme	limited	845:851	arg1	process					891:897	a general (i.e. occurring on many proteins) or a limited (i.e. occurring only on the keratins) process	796:897	a general (i.e. occurring on many proteins) or a limited (i.e. occurring only on the keratins) process	796:897	We have sought to determine whether this increase in glycosylation is a general (i.e. occurring on many proteins) or a limited (i.e. occurring only on the keratins) process.
9079710	11	56	from	residues	1638:1645	arg1	proteins					1659:1666	numerous proteins	1650:1666	numerous proteins	1650:1666	Interestingly, nocodazole treatment did cause a dramatic increase in modification of N-glycans with terminal GlcNAc residues on numerous proteins.
9079710	6	57	dep	limited	845:851	arg1	i.e.					854:857	i.e.	854:857	i.e. occurring only on the keratins	854:888	We have sought to determine whether this increase in glycosylation is a general (i.e. occurring on many proteins) or a limited (i.e. occurring only on the keratins) process.
9079710	11	58	from	increase	1579:1586	arg1	modification					1591:1602	modification	1591:1602	modification of N-glycans with terminal GlcNAc residues on numerous proteins	1591:1666	Interestingly, nocodazole treatment did cause a dramatic increase in modification of N-glycans with terminal GlcNAc residues on numerous proteins.
9079710	5	59	theme	O-GlcNAc	656:663	arg1	levels					665:670	the O-GlcNAc levels	652:670	the O-GlcNAc levels on keratins in the human colon cancer cell line HT29	652:723	268, 4465-4472) have shown that mitotic arrest with microtubule-destabilizing agents such as nocodazole causes an increase in the O-GlcNAc levels on keratins in the human colon cancer cell line HT29.
9079710	12	60	theme	keratins	1738:1745	arg1	glycosylation					1717:1729	glycosylation	1717:1729	glycosylation of the keratins	1717:1745	Potential mechanisms for this and the change in glycosylation of the keratins are discussed.
9079710	10	61	theme	responsible	1434:1444	arg1	enzymes					1426:1432	the enzymes	1422:1432	the enzymes responsible for addition or removal of O-GlcNAc	1422:1480	In agreement with these findings, nocodazole treatment caused no change in the activity of the enzymes responsible for addition or removal of O-GlcNAc as determined by direct in vitro assay.
9079710	7	62	theme	responsible	1010:1020	arg1	enzymes					1002:1008	the enzymes	998:1008	the enzymes responsible for addition and/or removal of O-GlcNAc	998:1060	A general increase would suggest that the microtubule-destabilizing agents were somehow affecting the enzymes responsible for addition and/or removal of O-GlcNAc.
9079710	0	63	with	arrest	8:13	arg1	nocodazole					20:29	nocodazole	20:29	nocodazole	20:29	Mitotic arrest with nocodazole induces selective changes in the level of O-linked N-acetylglucosamine and accumulation of incompletely processed N-glycans on proteins from HT29 cells.
9079710	5	64	with	arrest	566:571	arg1	agents					604:609	microtubule-destabilizing agents	578:609	microtubule-destabilizing agents such as nocodazole	578:628	268, 4465-4472) have shown that mitotic arrest with microtubule-destabilizing agents such as nocodazole causes an increase in the O-GlcNAc levels on keratins in the human colon cancer cell line HT29.
9079710	5	64	with	arrest	566:571	arg1	nocodazole					619:628	nocodazole	619:628	nocodazole	619:628	268, 4465-4472) have shown that mitotic arrest with microtubule-destabilizing agents such as nocodazole causes an increase in the O-GlcNAc levels on keratins in the human colon cancer cell line HT29.
9079710	9	65	dep	protein	1235:1241	arg1	p62					1243:1245	p62	1243:1245	the nuclear pore protein p62	1218:1245	The levels of O-GlcNAc on other proteins, including the nuclear pore protein p62 and the transcription factor Sp1, are not significantly affected by this treatment.
9079710	7	66	theme	O-GlcNAc	1053:1060	arg1	addition					1026:1033	addition	1026:1033	addition	1026:1033	A general increase would suggest that the microtubule-destabilizing agents were somehow affecting the enzymes responsible for addition and/or removal of O-GlcNAc.
9079710	0	67	from	accumulation	106:117	arg1	level					64:68	the level	60:68	the level of O-linked N-acetylglucosamine	60:100	Mitotic arrest with nocodazole induces selective changes in the level of O-linked N-acetylglucosamine and accumulation of incompletely processed N-glycans on proteins from HT29 cells.
9079710	0	67	from	accumulation	106:117	arg1	proteins					158:165	proteins	158:165	proteins from HT29 cells	158:181	Mitotic arrest with nocodazole induces selective changes in the level of O-linked N-acetylglucosamine and accumulation of incompletely processed N-glycans on proteins from HT29 cells.
9079710	1	68	located	found	274:278	arg1	proteins					307:314	nuclear and cytoplasmic proteins	283:314	nuclear and cytoplasmic proteins	283:314	O-Linked N-acetylglucosamine (O-GlcNAc) is a ubiquitous and abundant protein modification found on nuclear and cytoplasmic proteins.
9079710	1	68	located	found	274:278	arg2	modification					261:272	a ubiquitous and abundant protein modification	227:272	a ubiquitous and abundant protein modification found on nuclear and cytoplasmic proteins	227:314	O-Linked N-acetylglucosamine (O-GlcNAc) is a ubiquitous and abundant protein modification found on nuclear and cytoplasmic proteins.
9079710	1	68	located	found	274:278	arg2	N-acetylglucosamine					193:211	O-Linked N-acetylglucosamine	184:211	O-Linked N-acetylglucosamine (O-GlcNAc)	184:222	O-Linked N-acetylglucosamine (O-GlcNAc) is a ubiquitous and abundant protein modification found on nuclear and cytoplasmic proteins.
9079710	12	69	from	mechanisms	1679:1688	arg1	glycosylation					1717:1729	glycosylation	1717:1729	glycosylation of the keratins	1717:1745	Potential mechanisms for this and the change in glycosylation of the keratins are discussed.
9079710	1	70	theme	ubiquitous	229:238	arg1	N-acetylglucosamine					193:211	O-Linked N-acetylglucosamine	184:211	O-Linked N-acetylglucosamine (O-GlcNAc)	184:222	O-Linked N-acetylglucosamine (O-GlcNAc) is a ubiquitous and abundant protein modification found on nuclear and cytoplasmic proteins.
9079710	1	70	theme	ubiquitous	229:238	arg1	modification					261:272	a ubiquitous and abundant protein modification	227:272	a ubiquitous and abundant protein modification found on nuclear and cytoplasmic proteins	227:314	O-Linked N-acetylglucosamine (O-GlcNAc) is a ubiquitous and abundant protein modification found on nuclear and cytoplasmic proteins.
9079710	0	71	theme	HT29	172:175	arg1	cells					177:181	HT29 cells	172:181	HT29 cells	172:181	Mitotic arrest with nocodazole induces selective changes in the level of O-linked N-acetylglucosamine and accumulation of incompletely processed N-glycans on proteins from HT29 cells.
9079710	11	72	theme	N-glycans	1607:1615	arg1	modification					1591:1602	modification	1591:1602	modification of N-glycans with terminal GlcNAc residues on numerous proteins	1591:1666	Interestingly, nocodazole treatment did cause a dramatic increase in modification of N-glycans with terminal GlcNAc residues on numerous proteins.
9079710	7	73	theme	general	902:908	arg1	increase					910:917	A general increase	900:917	A general increase	900:917	A general increase would suggest that the microtubule-destabilizing agents were somehow affecting the enzymes responsible for addition and/or removal of O-GlcNAc.
9079710	0	74	from	N-glycans	145:153	arg1	proteins					158:165	proteins	158:165	proteins from HT29 cells	158:181	Mitotic arrest with nocodazole induces selective changes in the level of O-linked N-acetylglucosamine and accumulation of incompletely processed N-glycans on proteins from HT29 cells.
9079710	9	75	theme	O-GlcNAc	1180:1187	arg1	levels					1170:1175	The levels	1166:1175	The levels of O-GlcNAc on other proteins, including the nuclear pore protein p62 and the transcription factor Sp1,	1166:1279	The levels of O-GlcNAc on other proteins, including the nuclear pore protein p62 and the transcription factor Sp1, are not significantly affected by this treatment.
9079710	3	76	dep	workers	465:471	arg1	C.					480:481	C.	480:481	C.	480:481	Previous workers (Chou, C. F., and Omary, M. B. (1993) J. Biol.
9079710	3	76	dep	workers	465:471	arg1	M.					498:499	M.	498:499	M.	498:499	Previous workers (Chou, C. F., and Omary, M. B. (1993) J. Biol.
9079710	3	76	dep	workers	465:471	arg1	F.					483:484	F.	483:484	F.	483:484	Previous workers (Chou, C. F., and Omary, M. B. (1993) J. Biol.
9079710	3	76	dep	workers	465:471	arg1	workers					465:471	Previous workers	456:471	Previous workers (Chou, C. F., and Omary, M. B. (1993)	456:509	Previous workers (Chou, C. F., and Omary, M. B. (1993) J. Biol.
9079710	3	76	dep	workers	465:471	arg1	1993					505:508	1993	505:508	1993	505:508	Previous workers (Chou, C. F., and Omary, M. B. (1993) J. Biol.
9079710	10	77	theme	enzymes	1426:1432	arg1	activity					1410:1417	the activity	1406:1417	the activity of the enzymes responsible for addition or removal of O-GlcNAc	1406:1480	In agreement with these findings, nocodazole treatment caused no change in the activity of the enzymes responsible for addition or removal of O-GlcNAc as determined by direct in vitro assay.
9079710	11	78	theme	numerous	1650:1657	arg1	proteins					1659:1666	numerous proteins	1650:1666	numerous proteins	1650:1666	Interestingly, nocodazole treatment did cause a dramatic increase in modification of N-glycans with terminal GlcNAc residues on numerous proteins.
9079710	1	79	theme	abundant	244:251	arg1	N-acetylglucosamine					193:211	O-Linked N-acetylglucosamine	184:211	O-Linked N-acetylglucosamine (O-GlcNAc)	184:222	O-Linked N-acetylglucosamine (O-GlcNAc) is a ubiquitous and abundant protein modification found on nuclear and cytoplasmic proteins.
9079710	1	79	theme	abundant	244:251	arg1	modification					261:272	a ubiquitous and abundant protein modification	227:272	a ubiquitous and abundant protein modification found on nuclear and cytoplasmic proteins	227:314	O-Linked N-acetylglucosamine (O-GlcNAc) is a ubiquitous and abundant protein modification found on nuclear and cytoplasmic proteins.
9079710	5	80	theme	human	691:695	arg1	line					715:718	human colon cancer cell line	691:718	the human colon cancer cell line HT29	687:723	268, 4465-4472) have shown that mitotic arrest with microtubule-destabilizing agents such as nocodazole causes an increase in the O-GlcNAc levels on keratins in the human colon cancer cell line HT29.
9079710	11	81	theme	nocodazole	1537:1546	arg1	treatment					1548:1556	nocodazole treatment	1537:1556	nocodazole treatment	1537:1556	Interestingly, nocodazole treatment did cause a dramatic increase in modification of N-glycans with terminal GlcNAc residues on numerous proteins.
9079710	10	82	from	change	1396:1401	arg1	activity					1410:1417	the activity	1406:1417	the activity of the enzymes responsible for addition or removal of O-GlcNAc	1406:1480	In agreement with these findings, nocodazole treatment caused no change in the activity of the enzymes responsible for addition or removal of O-GlcNAc as determined by direct in vitro assay.
9079710	2	83	theme	dynamic	371:377	arg1	it					356:357	it	356:357	it	356:357	Several lines of evidence suggest that it is a highly dynamic modification and that the levels of this sugar on proteins may be regulated.
9079710	2	83	theme	dynamic	371:377	arg1	modification					379:390	a highly dynamic modification	362:390	a highly dynamic modification	362:390	Several lines of evidence suggest that it is a highly dynamic modification and that the levels of this sugar on proteins may be regulated.
9079710	1	84	theme	protein	253:259	arg1	N-acetylglucosamine					193:211	O-Linked N-acetylglucosamine	184:211	O-Linked N-acetylglucosamine (O-GlcNAc)	184:222	O-Linked N-acetylglucosamine (O-GlcNAc) is a ubiquitous and abundant protein modification found on nuclear and cytoplasmic proteins.
9079710	1	84	theme	protein	253:259	arg1	modification					261:272	a ubiquitous and abundant protein modification	227:272	a ubiquitous and abundant protein modification found on nuclear and cytoplasmic proteins	227:314	O-Linked N-acetylglucosamine (O-GlcNAc) is a ubiquitous and abundant protein modification found on nuclear and cytoplasmic proteins.
21105874	7	0	theme	expression	1319:1328	arg1	form					1291:1294	This O-GlcNAc-deficient form	1267:1294	This O-GlcNAc-deficient form	1267:1294	This O-GlcNAc-deficient form of Sp1-enhanced p75NTR expression, demonstrating that O-GlcNAcylation of Sp1 negatively regulates p75NTR expression.
21105874	1	1	theme	receptor	170:177	arg1	expression					139:148	Injury-induced expression	124:148	Injury-induced expression of p75 neurotrophin receptor (p75NTR) in the CNS	124:197	Injury-induced expression of p75 neurotrophin receptor (p75NTR) in the CNS induces neuronal apoptosis and prevents neuronal regrowth.
21105874	8	2	theme	stress-induced	1432:1445	arg1	decline					1447:1453	a stress-induced decline	1430:1453	a stress-induced decline in the O-GlcNAc content of Sp1	1430:1484	We conclude that a stress-induced decline in the O-GlcNAc content of Sp1 drives expression of p75NTR.
21105874	5	3	theme	RNAi-based	957:966	arg1	treatments					968:977	chemical and RNAi-based treatments	944:977	chemical and RNAi-based treatments that reduce cellular O-GlcNAcylation	944:1014	We demonstrate that chemical and RNAi-based treatments that reduce cellular O-GlcNAcylation facilitate p75NTR induction by hypo-osmolarity, directly linking protein O-GlcNAcylation to p75NTR induction.
21105874	0	4	theme	Sp1	98:100	arg1	factor					116:121	the Sp1 transcription factor	94:121	the Sp1 transcription factor	94:121	Stress-induced expression of the p75 neurotrophin receptor is regulated by O-GlcNAcylation of the Sp1 transcription factor.
21105874	4	5	theme	extracellular	803:815	arg1	hypo-osmolarity					817:831	extracellular hypo-osmolarity	803:831	extracellular hypo-osmolarity	803:831	We report that levels of O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT), the enzyme that mediates O-linked attachment of GlcNAc, are reduced by extracellular hypo-osmolarity and that global levels of protein O-GlcNAcylation and of Sp1 show a corresponding decline.
21105874	6	6	theme	target	1250:1255	arg1	residues					1257:1264	O-GlcNAc target residues	1241:1264	O-GlcNAc target residues	1241:1264	To determine if Sp1 O-GlcNAc content regulates p75NTR expression, we replaced endogenous Sp1 with a Sp1 mutated at O-GlcNAc target residues.
21105874	6	7	theme	O-GlcNAc	1241:1248	arg1	residues					1257:1264	O-GlcNAc target residues	1241:1264	O-GlcNAc target residues	1241:1264	To determine if Sp1 O-GlcNAc content regulates p75NTR expression, we replaced endogenous Sp1 with a Sp1 mutated at O-GlcNAc target residues.
21105874	4	8	link	O-linked	757:764	arg1	attachment					766:775	O-linked attachment	757:775	O-linked attachment of GlcNAc	757:785	We report that levels of O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT), the enzyme that mediates O-linked attachment of GlcNAc, are reduced by extracellular hypo-osmolarity and that global levels of protein O-GlcNAcylation and of Sp1 show a corresponding decline.
21105874	8	9	theme	O-GlcNAc	1462:1469	arg1	content					1471:1477	the O-GlcNAc content	1458:1477	the O-GlcNAc content of Sp1	1458:1484	We conclude that a stress-induced decline in the O-GlcNAc content of Sp1 drives expression of p75NTR.
21105874	5	10	theme	cellular	991:998	arg1	O-GlcNAcylation					1000:1014	cellular O-GlcNAcylation	991:1014	cellular O-GlcNAcylation	991:1014	We demonstrate that chemical and RNAi-based treatments that reduce cellular O-GlcNAcylation facilitate p75NTR induction by hypo-osmolarity, directly linking protein O-GlcNAcylation to p75NTR induction.
21105874	0	11	theme	factor	116:121	arg1	O-GlcNAcylation					75:89	O-GlcNAcylation	75:89	O-GlcNAcylation of the Sp1 transcription factor	75:121	Stress-induced expression of the p75 neurotrophin receptor is regulated by O-GlcNAcylation of the Sp1 transcription factor.
21105874	7	12	theme	Sp1	1369:1371	arg1	O-GlcNAcylation					1350:1364	O-GlcNAcylation	1350:1364	O-GlcNAcylation of Sp1	1350:1371	This O-GlcNAc-deficient form of Sp1-enhanced p75NTR expression, demonstrating that O-GlcNAcylation of Sp1 negatively regulates p75NTR expression.
21105874	4	13	theme	N-acetylglucosamine	682:700	arg1	enzyme					736:741	the enzyme	732:741	the enzyme that mediates O-linked attachment of GlcNAc	732:785	We report that levels of O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT), the enzyme that mediates O-linked attachment of GlcNAc, are reduced by extracellular hypo-osmolarity and that global levels of protein O-GlcNAcylation and of Sp1 show a corresponding decline.
21105874	4	13	theme	N-acetylglucosamine	682:700	arg1	OGT					726:728	OGT	726:728	OGT	726:728	We report that levels of O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT), the enzyme that mediates O-linked attachment of GlcNAc, are reduced by extracellular hypo-osmolarity and that global levels of protein O-GlcNAcylation and of Sp1 show a corresponding decline.
21105874	4	13	theme	N-acetylglucosamine	682:700	arg1	transferase					713:723	O-linked N-acetylglucosamine (O-GlcNAc) transferase	673:723	O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT)	673:729	We report that levels of O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT), the enzyme that mediates O-linked attachment of GlcNAc, are reduced by extracellular hypo-osmolarity and that global levels of protein O-GlcNAcylation and of Sp1 show a corresponding decline.
21105874	2	14	theme	p75NTR	299:304	arg1	expression					306:315	injury-induced p75NTR expression	284:315	injury-induced p75NTR expression	284:315	The mechanisms regulating injury-induced p75NTR expression are poorly characterized but previous studies have established that reductions in extracellular osmolarity which mimic cytotoxic edema induce p75NTR gene expression through pathways that activate the Sp1 transcription factor.
21105874	6	15	theme	Sp1	1142:1144	arg1	content					1155:1161	Sp1 O-GlcNAc content	1142:1161	Sp1 O-GlcNAc content	1142:1161	To determine if Sp1 O-GlcNAc content regulates p75NTR expression, we replaced endogenous Sp1 with a Sp1 mutated at O-GlcNAc target residues.
21105874	0	16	theme	transcription	102:114	arg1	factor					116:121	the Sp1 transcription factor	94:121	the Sp1 transcription factor	94:121	Stress-induced expression of the p75 neurotrophin receptor is regulated by O-GlcNAcylation of the Sp1 transcription factor.
21105874	4	17	theme	Sp1	890:892	arg1	levels					849:854	global levels	842:854	global levels of protein O-GlcNAcylation and of Sp1	842:892	We report that levels of O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT), the enzyme that mediates O-linked attachment of GlcNAc, are reduced by extracellular hypo-osmolarity and that global levels of protein O-GlcNAcylation and of Sp1 show a corresponding decline.
21105874	1	18	from	expression	139:148	arg1	CNS					195:197	the CNS	191:197	the CNS	191:197	Injury-induced expression of p75 neurotrophin receptor (p75NTR) in the CNS induces neuronal apoptosis and prevents neuronal regrowth.
21105874	2	19	theme	injury-induced	284:297	arg1	expression					306:315	injury-induced p75NTR expression	284:315	injury-induced p75NTR expression	284:315	The mechanisms regulating injury-induced p75NTR expression are poorly characterized but previous studies have established that reductions in extracellular osmolarity which mimic cytotoxic edema induce p75NTR gene expression through pathways that activate the Sp1 transcription factor.
21105874	2	20	theme	cytotoxic	436:444	arg1	edema					446:450	cytotoxic edema	436:450	cytotoxic edema	436:450	The mechanisms regulating injury-induced p75NTR expression are poorly characterized but previous studies have established that reductions in extracellular osmolarity which mimic cytotoxic edema induce p75NTR gene expression through pathways that activate the Sp1 transcription factor.
21105874	4	21	theme	corresponding	901:913	arg1	decline					915:921	a corresponding decline	899:921	a corresponding decline	899:921	We report that levels of O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT), the enzyme that mediates O-linked attachment of GlcNAc, are reduced by extracellular hypo-osmolarity and that global levels of protein O-GlcNAcylation and of Sp1 show a corresponding decline.
21105874	2	22	from	reductions	385:394	arg1	osmolarity					413:422	extracellular osmolarity	399:422	extracellular osmolarity	399:422	The mechanisms regulating injury-induced p75NTR expression are poorly characterized but previous studies have established that reductions in extracellular osmolarity which mimic cytotoxic edema induce p75NTR gene expression through pathways that activate the Sp1 transcription factor.
21105874	2	23	theme	previous	346:353	arg1	studies					355:361	previous studies	346:361	previous studies	346:361	The mechanisms regulating injury-induced p75NTR expression are poorly characterized but previous studies have established that reductions in extracellular osmolarity which mimic cytotoxic edema induce p75NTR gene expression through pathways that activate the Sp1 transcription factor.
21105874	7	24	theme	p75NTR	1394:1399	arg1	expression					1401:1410	p75NTR expression	1394:1410	p75NTR expression	1394:1410	This O-GlcNAc-deficient form of Sp1-enhanced p75NTR expression, demonstrating that O-GlcNAcylation of Sp1 negatively regulates p75NTR expression.
21105874	0	25	theme	Stress-induced	0:13	arg1	expression					15:24	Stress-induced expression	0:24	Stress-induced expression of the p75 neurotrophin receptor	0:57	Stress-induced expression of the p75 neurotrophin receptor is regulated by O-GlcNAcylation of the Sp1 transcription factor.
21105874	8	26	from	decline	1447:1453	arg1	content					1471:1477	the O-GlcNAc content	1458:1477	the O-GlcNAc content of Sp1	1458:1484	We conclude that a stress-induced decline in the O-GlcNAc content of Sp1 drives expression of p75NTR.
21105874	3	27	theme	p75NTR	629:634	arg1	expression					636:645	p75NTR expression	629:645	p75NTR expression	629:645	In this report, we examined how extracellular osmolarity converges on Sp1 to regulate p75NTR expression.
21105874	8	28	theme	Sp1	1482:1484	arg1	content					1471:1477	the O-GlcNAc content	1458:1477	the O-GlcNAc content of Sp1	1458:1484	We conclude that a stress-induced decline in the O-GlcNAc content of Sp1 drives expression of p75NTR.
21105874	6	29	theme	p75NTR	1173:1178	arg1	expression					1180:1189	p75NTR expression	1173:1189	p75NTR expression	1173:1189	To determine if Sp1 O-GlcNAc content regulates p75NTR expression, we replaced endogenous Sp1 with a Sp1 mutated at O-GlcNAc target residues.
21105874	5	30	theme	p75NTR	1027:1032	arg1	induction					1034:1042	p75NTR induction	1027:1042	p75NTR induction	1027:1042	We demonstrate that chemical and RNAi-based treatments that reduce cellular O-GlcNAcylation facilitate p75NTR induction by hypo-osmolarity, directly linking protein O-GlcNAcylation to p75NTR induction.
21105874	5	31	theme	p75NTR	1108:1113	arg1	induction					1115:1123	p75NTR induction	1108:1123	p75NTR induction	1108:1123	We demonstrate that chemical and RNAi-based treatments that reduce cellular O-GlcNAcylation facilitate p75NTR induction by hypo-osmolarity, directly linking protein O-GlcNAcylation to p75NTR induction.
21105874	6	32	theme	O-GlcNAc	1146:1153	arg1	content					1155:1161	Sp1 O-GlcNAc content	1142:1161	Sp1 O-GlcNAc content	1142:1161	To determine if Sp1 O-GlcNAc content regulates p75NTR expression, we replaced endogenous Sp1 with a Sp1 mutated at O-GlcNAc target residues.
21105874	4	33	theme	GlcNAc	780:785	arg1	attachment					766:775	O-linked attachment	757:775	O-linked attachment of GlcNAc	757:785	We report that levels of O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT), the enzyme that mediates O-linked attachment of GlcNAc, are reduced by extracellular hypo-osmolarity and that global levels of protein O-GlcNAcylation and of Sp1 show a corresponding decline.
21105874	3	34	theme	extracellular	575:587	arg1	osmolarity					589:598	extracellular osmolarity	575:598	extracellular osmolarity	575:598	In this report, we examined how extracellular osmolarity converges on Sp1 to regulate p75NTR expression.
21105874	4	35	link	O-linked	673:680	arg1	O-GlcNAc					703:710	O-GlcNAc	703:710	O-GlcNAc	703:710	We report that levels of O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT), the enzyme that mediates O-linked attachment of GlcNAc, are reduced by extracellular hypo-osmolarity and that global levels of protein O-GlcNAcylation and of Sp1 show a corresponding decline.
21105874	4	35	link	O-linked	673:680	arg1	N-acetylglucosamine					682:700	O-linked N-acetylglucosamine	673:700	O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT)	673:729	We report that levels of O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT), the enzyme that mediates O-linked attachment of GlcNAc, are reduced by extracellular hypo-osmolarity and that global levels of protein O-GlcNAcylation and of Sp1 show a corresponding decline.
21105874	2	36	theme	gene	466:469	arg1	expression					471:480	p75NTR gene expression	459:480	p75NTR gene expression	459:480	The mechanisms regulating injury-induced p75NTR expression are poorly characterized but previous studies have established that reductions in extracellular osmolarity which mimic cytotoxic edema induce p75NTR gene expression through pathways that activate the Sp1 transcription factor.
21105874	0	37	theme	neurotrophin	37:48	arg1	receptor					50:57	the p75 neurotrophin receptor	29:57	the p75 neurotrophin receptor	29:57	Stress-induced expression of the p75 neurotrophin receptor is regulated by O-GlcNAcylation of the Sp1 transcription factor.
21105874	1	38	theme	neuronal	207:214	arg1	apoptosis					216:224	neuronal apoptosis	207:224	neuronal apoptosis	207:224	Injury-induced expression of p75 neurotrophin receptor (p75NTR) in the CNS induces neuronal apoptosis and prevents neuronal regrowth.
21105874	4	39	theme	O-GlcNAcylation	867:881	arg1	levels					849:854	global levels	842:854	global levels of protein O-GlcNAcylation and of Sp1	842:892	We report that levels of O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT), the enzyme that mediates O-linked attachment of GlcNAc, are reduced by extracellular hypo-osmolarity and that global levels of protein O-GlcNAcylation and of Sp1 show a corresponding decline.
21105874	2	40	theme	p75NTR	459:464	arg1	expression					471:480	p75NTR gene expression	459:480	p75NTR gene expression	459:480	The mechanisms regulating injury-induced p75NTR expression are poorly characterized but previous studies have established that reductions in extracellular osmolarity which mimic cytotoxic edema induce p75NTR gene expression through pathways that activate the Sp1 transcription factor.
21105874	0	41	theme	p75	33:35	arg1	receptor					50:57	the p75 neurotrophin receptor	29:57	the p75 neurotrophin receptor	29:57	Stress-induced expression of the p75 neurotrophin receptor is regulated by O-GlcNAcylation of the Sp1 transcription factor.
21105874	2	42	theme	transcription	521:533	arg1	factor					535:540	the Sp1 transcription factor	513:540	the Sp1 transcription factor	513:540	The mechanisms regulating injury-induced p75NTR expression are poorly characterized but previous studies have established that reductions in extracellular osmolarity which mimic cytotoxic edema induce p75NTR gene expression through pathways that activate the Sp1 transcription factor.
21105874	4	43	theme	protein	859:865	arg1	O-GlcNAcylation					867:881	protein O-GlcNAcylation	859:881	protein O-GlcNAcylation	859:881	We report that levels of O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT), the enzyme that mediates O-linked attachment of GlcNAc, are reduced by extracellular hypo-osmolarity and that global levels of protein O-GlcNAcylation and of Sp1 show a corresponding decline.
21105874	2	44	theme	Sp1	517:519	arg1	factor					535:540	the Sp1 transcription factor	513:540	the Sp1 transcription factor	513:540	The mechanisms regulating injury-induced p75NTR expression are poorly characterized but previous studies have established that reductions in extracellular osmolarity which mimic cytotoxic edema induce p75NTR gene expression through pathways that activate the Sp1 transcription factor.
21105874	7	45	theme	Sp1-enhanced	1299:1310	arg1	expression					1319:1328	Sp1-enhanced p75NTR expression	1299:1328	Sp1-enhanced p75NTR expression	1299:1328	This O-GlcNAc-deficient form of Sp1-enhanced p75NTR expression, demonstrating that O-GlcNAcylation of Sp1 negatively regulates p75NTR expression.
21105874	6	46	theme	endogenous	1204:1213	arg1	Sp1					1215:1217	endogenous Sp1	1204:1217	endogenous Sp1	1204:1217	To determine if Sp1 O-GlcNAc content regulates p75NTR expression, we replaced endogenous Sp1 with a Sp1 mutated at O-GlcNAc target residues.
21105874	4	47	theme	O-linked	757:764	arg1	attachment					766:775	O-linked attachment	757:775	O-linked attachment of GlcNAc	757:785	We report that levels of O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT), the enzyme that mediates O-linked attachment of GlcNAc, are reduced by extracellular hypo-osmolarity and that global levels of protein O-GlcNAcylation and of Sp1 show a corresponding decline.
21105874	0	48	theme	receptor	50:57	arg1	expression					15:24	Stress-induced expression	0:24	Stress-induced expression of the p75 neurotrophin receptor	0:57	Stress-induced expression of the p75 neurotrophin receptor is regulated by O-GlcNAcylation of the Sp1 transcription factor.
21105874	1	49	theme	Injury-induced	124:137	arg1	expression					139:148	Injury-induced expression	124:148	Injury-induced expression of p75 neurotrophin receptor (p75NTR) in the CNS	124:197	Injury-induced expression of p75 neurotrophin receptor (p75NTR) in the CNS induces neuronal apoptosis and prevents neuronal regrowth.
21105874	4	50	theme	global	842:847	arg1	levels					849:854	global levels	842:854	global levels of protein O-GlcNAcylation and of Sp1	842:892	We report that levels of O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT), the enzyme that mediates O-linked attachment of GlcNAc, are reduced by extracellular hypo-osmolarity and that global levels of protein O-GlcNAcylation and of Sp1 show a corresponding decline.
21105874	8	51	theme	p75NTR	1507:1512	arg1	expression					1493:1502	expression	1493:1502	expression of p75NTR	1493:1512	We conclude that a stress-induced decline in the O-GlcNAc content of Sp1 drives expression of p75NTR.
21105874	5	52	theme	protein	1081:1087	arg1	O-GlcNAcylation					1089:1103	protein O-GlcNAcylation	1081:1103	protein O-GlcNAcylation	1081:1103	We demonstrate that chemical and RNAi-based treatments that reduce cellular O-GlcNAcylation facilitate p75NTR induction by hypo-osmolarity, directly linking protein O-GlcNAcylation to p75NTR induction.
21105874	1	53	theme	neurotrophin	157:168	arg1	p75NTR					180:185	p75NTR	180:185	p75NTR	180:185	Injury-induced expression of p75 neurotrophin receptor (p75NTR) in the CNS induces neuronal apoptosis and prevents neuronal regrowth.
21105874	1	53	theme	neurotrophin	157:168	arg1	receptor					170:177	p75 neurotrophin receptor	153:177	p75 neurotrophin receptor (p75NTR)	153:186	Injury-induced expression of p75 neurotrophin receptor (p75NTR) in the CNS induces neuronal apoptosis and prevents neuronal regrowth.
21105874	5	54	theme	chemical	944:951	arg1	treatments					968:977	chemical and RNAi-based treatments	944:977	chemical and RNAi-based treatments that reduce cellular O-GlcNAcylation	944:1014	We demonstrate that chemical and RNAi-based treatments that reduce cellular O-GlcNAcylation facilitate p75NTR induction by hypo-osmolarity, directly linking protein O-GlcNAcylation to p75NTR induction.
21105874	4	55	theme	O-linked	673:680	arg1	O-GlcNAc					703:710	O-GlcNAc	703:710	O-GlcNAc	703:710	We report that levels of O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT), the enzyme that mediates O-linked attachment of GlcNAc, are reduced by extracellular hypo-osmolarity and that global levels of protein O-GlcNAcylation and of Sp1 show a corresponding decline.
21105874	4	55	theme	O-linked	673:680	arg1	N-acetylglucosamine					682:700	O-linked N-acetylglucosamine	673:700	O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT)	673:729	We report that levels of O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT), the enzyme that mediates O-linked attachment of GlcNAc, are reduced by extracellular hypo-osmolarity and that global levels of protein O-GlcNAcylation and of Sp1 show a corresponding decline.
21105874	1	56	theme	p75	153:155	arg1	p75NTR					180:185	p75NTR	180:185	p75NTR	180:185	Injury-induced expression of p75 neurotrophin receptor (p75NTR) in the CNS induces neuronal apoptosis and prevents neuronal regrowth.
21105874	1	56	theme	p75	153:155	arg1	receptor					170:177	p75 neurotrophin receptor	153:177	p75 neurotrophin receptor (p75NTR)	153:186	Injury-induced expression of p75 neurotrophin receptor (p75NTR) in the CNS induces neuronal apoptosis and prevents neuronal regrowth.
21105874	4	57	theme	transferase	713:723	arg1	levels					663:668	levels	663:668	levels of O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT), the enzyme that mediates O-linked attachment of GlcNAc,	663:786	We report that levels of O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT), the enzyme that mediates O-linked attachment of GlcNAc, are reduced by extracellular hypo-osmolarity and that global levels of protein O-GlcNAcylation and of Sp1 show a corresponding decline.
21105874	1	58	theme	neuronal	239:246	arg1	regrowth					248:255	neuronal regrowth	239:255	neuronal regrowth	239:255	Injury-induced expression of p75 neurotrophin receptor (p75NTR) in the CNS induces neuronal apoptosis and prevents neuronal regrowth.
21105874	2	59	theme	extracellular	399:411	arg1	osmolarity					413:422	extracellular osmolarity	399:422	extracellular osmolarity	399:422	The mechanisms regulating injury-induced p75NTR expression are poorly characterized but previous studies have established that reductions in extracellular osmolarity which mimic cytotoxic edema induce p75NTR gene expression through pathways that activate the Sp1 transcription factor.
21105874	7	60	theme	O-GlcNAc-deficient	1272:1289	arg1	form					1291:1294	This O-GlcNAc-deficient form	1267:1294	This O-GlcNAc-deficient form	1267:1294	This O-GlcNAc-deficient form of Sp1-enhanced p75NTR expression, demonstrating that O-GlcNAcylation of Sp1 negatively regulates p75NTR expression.
21105874	7	61	theme	p75NTR	1312:1317	arg1	expression					1319:1328	Sp1-enhanced p75NTR expression	1299:1328	Sp1-enhanced p75NTR expression	1299:1328	This O-GlcNAc-deficient form of Sp1-enhanced p75NTR expression, demonstrating that O-GlcNAcylation of Sp1 negatively regulates p75NTR expression.
25352121	17	0	theme	DR	1924:1925	arg1	pathogenesis					1896:1907	the pathogenesis	1892:1907	the pathogenesis of preclinical DR through VEGF-A upregulation	1892:1953	This mechanism may be significant in the pathogenesis of preclinical DR through VEGF-A upregulation.
25352121	14	1	theme	OGT	1543:1545	arg1	depletion					1530:1538	Cellular depletion	1521:1538	Cellular depletion of OGT or Sp1 by shRNA	1521:1561	Cellular depletion of OGT or Sp1 by shRNA significantly abrogated glucose-induced changes in VEGF-A.
25352121	15	2	theme	Sp1	1697:1699	arg1	binding					1686:1692	binding	1686:1692	binding of Sp1 to the VEGF-A promoter	1686:1722	ChIP analysis showed that hyperglycemia significantly increased binding of Sp1 to the VEGF-A promoter.
25352121	8	3	theme	endothelial	989:999	arg1	factor-A					1008:1015	Vascular endothelial growth factor-A protein and transcript	980:1038	Vascular endothelial growth factor-A protein and transcript	980:1038	Vascular endothelial growth factor-A protein and transcript were measured in cells depleted of OGT or Sp1 by shRNA.
25352121	10	4	from	occupancy	1243:1251	arg1	promoter					1267:1274	the VEGF-A promoter	1256:1274	the VEGF-A promoter	1256:1274	Chromatin immunoprecipitation (ChIP) was used to assess Sp1 occupancy on the VEGF-A promoter.
25352121	7	5	theme	O-GlcNAc	891:898	arg1	OGT					913:915	OGT	913:915	OGT	913:915	Small molecule inhibitors of O-GlcNAc transferase (OGT) or O-GlcNAcase (OGA) were used to manipulate O-GlcNAc levels.
25352121	7	5	theme	O-GlcNAc	891:898	arg1	transferase					900:910	O-GlcNAc transferase	891:910	O-GlcNAc transferase (OGT)	891:916	Small molecule inhibitors of O-GlcNAc transferase (OGT) or O-GlcNAcase (OGA) were used to manipulate O-GlcNAc levels.
25352121	7	6	theme	Small	862:866	arg1	inhibitors					877:886	Small molecule inhibitors	862:886	Small molecule inhibitors of O-GlcNAc transferase (OGT) or O-GlcNAcase (OGA)	862:937	Small molecule inhibitors of O-GlcNAc transferase (OGT) or O-GlcNAcase (OGA) were used to manipulate O-GlcNAc levels.
25352121	5	7	from	effects	550:556	arg1	expression					591:600	Sp1-mediated expression	578:600	Sp1-mediated expression of VEGF-A in the retinal endothelium and pigment epithelium	578:660	This study investigated the effects of hyperglycemia on Sp1-mediated expression of VEGF-A in the retinal endothelium and pigment epithelium.
25352121	16	8	mod	modification	1809:1820	arg1	factor					1847:1852	the Sp1 transcription factor	1825:1852	the Sp1 transcription factor	1825:1852	CONCLUSIONS Hyperglycemia-driven VEGF-A production is mediated by elevated O-GlcNAc modification of the Sp1 transcription factor.
25352121	16	8	mod	modification	1809:1820	arg3	O-GlcNAc					1800:1807	elevated O-GlcNAc modification	1791:1820	elevated O-GlcNAc modification of the Sp1 transcription factor	1791:1852	CONCLUSIONS Hyperglycemia-driven VEGF-A production is mediated by elevated O-GlcNAc modification of the Sp1 transcription factor.
25352121	8	9	theme	growth	1001:1006	arg1	factor-A					1008:1015	Vascular endothelial growth factor-A protein and transcript	980:1038	Vascular endothelial growth factor-A protein and transcript	980:1038	Vascular endothelial growth factor-A protein and transcript were measured in cells depleted of OGT or Sp1 by shRNA.
25352121	17	10	from	significant	1877:1887	arg1	pathogenesis					1896:1907	the pathogenesis	1892:1907	the pathogenesis of preclinical DR through VEGF-A upregulation	1892:1953	This mechanism may be significant in the pathogenesis of preclinical DR through VEGF-A upregulation.
25352121	16	11	theme	O-GlcNAc	1800:1807	arg1	modification					1809:1820	elevated O-GlcNAc modification	1791:1820	elevated O-GlcNAc modification of the Sp1 transcription factor	1791:1852	CONCLUSIONS Hyperglycemia-driven VEGF-A production is mediated by elevated O-GlcNAc modification of the Sp1 transcription factor.
25352121	6	12	theme	retinal	708:714	arg1	ARPE-19					693:699	Hyperglycemia-exposed ARPE-19	671:699	Hyperglycemia-exposed ARPE-19 (human retinal pigment epithelial cells)	671:740	METHODS Hyperglycemia-exposed ARPE-19 (human retinal pigment epithelial cells) and TR-iBRB (rat retinal microendothelial cells) were assayed for levels of VEGF-A by qRT-PCR, Western blot, and ELISA.
25352121	6	12	theme	retinal	708:714	arg1	cells					735:739	human retinal pigment epithelial cells	702:739	human retinal pigment epithelial cells	702:739	METHODS Hyperglycemia-exposed ARPE-19 (human retinal pigment epithelial cells) and TR-iBRB (rat retinal microendothelial cells) were assayed for levels of VEGF-A by qRT-PCR, Western blot, and ELISA.
25352121	4	13	theme	glucose	457:463	arg1	concentration					465:477	glucose concentration	457:477	glucose concentration	457:477	The O-GlcNAc modification is driven by glucose concentration and has a profound effect on Sp1 activity.
25352121	10	14	theme	Sp1	1239:1241	arg1	occupancy					1243:1251	Sp1 occupancy	1239:1251	Sp1 occupancy on the VEGF-A promoter	1239:1274	Chromatin immunoprecipitation (ChIP) was used to assess Sp1 occupancy on the VEGF-A promoter.
25352121	0	15	theme	VEGF-A	81:86	arg1	upregulation					88:99	hyperglycemia-induced VEGF-A upregulation	59:99	hyperglycemia-induced VEGF-A upregulation in retinal cells	59:116	O-GlcNAc modification of transcription factor Sp1 mediates hyperglycemia-induced VEGF-A upregulation in retinal cells.
25352121	1	16	from	neovascularization	205:222	arg1	retinopathy					236:246	diabetic retinopathy	227:246	diabetic retinopathy	227:246	PURPOSE Proangiogenic protein VEGF-A contributes significantly to retinal lesions and neovascularization in diabetic retinopathy (DR).
25352121	1	17	theme	retinal	185:191	arg1	lesions					193:199	retinal lesions	185:199	retinal lesions	185:199	PURPOSE Proangiogenic protein VEGF-A contributes significantly to retinal lesions and neovascularization in diabetic retinopathy (DR).
25352121	11	18	theme	VEGF-A	1309:1314	arg1	activity					1325:1332	VEGF-A promoter activity	1309:1332	VEGF-A promoter activity	1309:1332	RESULTS Hyperglycemia increased VEGF-A promoter activity and upregulated VEGF-A transcript and protein.
25352121	6	19	theme	Hyperglycemia-exposed	671:691	arg1	ARPE-19					693:699	Hyperglycemia-exposed ARPE-19	671:699	Hyperglycemia-exposed ARPE-19 (human retinal pigment epithelial cells)	671:740	METHODS Hyperglycemia-exposed ARPE-19 (human retinal pigment epithelial cells) and TR-iBRB (rat retinal microendothelial cells) were assayed for levels of VEGF-A by qRT-PCR, Western blot, and ELISA.
25352121	6	19	theme	Hyperglycemia-exposed	671:691	arg1	cells					735:739	human retinal pigment epithelial cells	702:739	human retinal pigment epithelial cells	702:739	METHODS Hyperglycemia-exposed ARPE-19 (human retinal pigment epithelial cells) and TR-iBRB (rat retinal microendothelial cells) were assayed for levels of VEGF-A by qRT-PCR, Western blot, and ELISA.
25352121	6	19	theme	Hyperglycemia-exposed	671:691	arg1	METHODS					663:669	METHODS	663:669	METHODS Hyperglycemia-exposed ARPE-19 (human retinal pigment epithelial cells) and TR-iBRB (rat retinal microendothelial cells)	663:789	METHODS Hyperglycemia-exposed ARPE-19 (human retinal pigment epithelial cells) and TR-iBRB (rat retinal microendothelial cells) were assayed for levels of VEGF-A by qRT-PCR, Western blot, and ELISA.
25352121	1	20	from	lesions	193:199	arg1	retinopathy					236:246	diabetic retinopathy	227:246	diabetic retinopathy	227:246	PURPOSE Proangiogenic protein VEGF-A contributes significantly to retinal lesions and neovascularization in diabetic retinopathy (DR).
25352121	10	21	theme	VEGF-A	1260:1265	arg1	promoter					1267:1274	the VEGF-A promoter	1256:1274	the VEGF-A promoter	1256:1274	Chromatin immunoprecipitation (ChIP) was used to assess Sp1 occupancy on the VEGF-A promoter.
25352121	7	22	theme	O-GlcNAc	963:970	arg1	levels					972:977	O-GlcNAc levels	963:977	O-GlcNAc levels	963:977	Small molecule inhibitors of O-GlcNAc transferase (OGT) or O-GlcNAcase (OGA) were used to manipulate O-GlcNAc levels.
25352121	6	23	theme	rat	755:757	arg1	cells					784:788	rat retinal microendothelial cells	755:788	rat retinal microendothelial cells	755:788	METHODS Hyperglycemia-exposed ARPE-19 (human retinal pigment epithelial cells) and TR-iBRB (rat retinal microendothelial cells) were assayed for levels of VEGF-A by qRT-PCR, Western blot, and ELISA.
25352121	6	23	theme	rat	755:757	arg1	TR-iBRB					746:752	TR-iBRB	746:752	TR-iBRB (rat retinal microendothelial cells)	746:789	METHODS Hyperglycemia-exposed ARPE-19 (human retinal pigment epithelial cells) and TR-iBRB (rat retinal microendothelial cells) were assayed for levels of VEGF-A by qRT-PCR, Western blot, and ELISA.
25352121	16	24	theme	VEGF-A	1758:1763	arg1	production					1765:1774	Hyperglycemia-driven VEGF-A production	1737:1774	Hyperglycemia-driven VEGF-A production	1737:1774	CONCLUSIONS Hyperglycemia-driven VEGF-A production is mediated by elevated O-GlcNAc modification of the Sp1 transcription factor.
25352121	5	25	theme	VEGF-A	605:610	arg1	expression					591:600	Sp1-mediated expression	578:600	Sp1-mediated expression of VEGF-A in the retinal endothelium and pigment epithelium	578:660	This study investigated the effects of hyperglycemia on Sp1-mediated expression of VEGF-A in the retinal endothelium and pigment epithelium.
25352121	4	26	theme	Sp1	508:510	arg1	activity					512:519	Sp1 activity	508:519	Sp1 activity	508:519	The O-GlcNAc modification is driven by glucose concentration and has a profound effect on Sp1 activity.
25352121	9	27	theme	proximal	1100:1107	arg1	promoter					1116:1123	The proximal VEGF-A promoter	1096:1123	The proximal VEGF-A promoter	1096:1123	The proximal VEGF-A promoter was analyzed for glucose sensitivity by luciferase assay.
25352121	0	28	theme	O-GlcNAc	0:7	arg1	modification					9:20	O-GlcNAc modification	0:20	O-GlcNAc modification of transcription factor Sp1	0:48	O-GlcNAc modification of transcription factor Sp1 mediates hyperglycemia-induced VEGF-A upregulation in retinal cells.
25352121	7	29	used	used	944:947	arg2	inhibitors					877:886	Small molecule inhibitors	862:886	Small molecule inhibitors of O-GlcNAc transferase (OGT) or O-GlcNAcase (OGA)	862:937	Small molecule inhibitors of O-GlcNAc transferase (OGT) or O-GlcNAcase (OGA) were used to manipulate O-GlcNAc levels.
25352121	8	30	dep	factor-A	1008:1015	arg1	transcript					1029:1038	transcript	1029:1038	transcript	1029:1038	Vascular endothelial growth factor-A protein and transcript were measured in cells depleted of OGT or Sp1 by shRNA.
25352121	8	30	dep	factor-A	1008:1015	arg1	protein					1017:1023	protein	1017:1023	protein	1017:1023	Vascular endothelial growth factor-A protein and transcript were measured in cells depleted of OGT or Sp1 by shRNA.
25352121	17	31	theme	VEGF-A	1935:1940	arg1	upregulation					1942:1953	VEGF-A upregulation	1935:1953	VEGF-A upregulation	1935:1953	This mechanism may be significant in the pathogenesis of preclinical DR through VEGF-A upregulation.
25352121	1	32	theme	Proangiogenic	127:139	arg1	VEGF-A					149:154	PURPOSE Proangiogenic protein VEGF-A	119:154	PURPOSE Proangiogenic protein VEGF-A	119:154	PURPOSE Proangiogenic protein VEGF-A contributes significantly to retinal lesions and neovascularization in diabetic retinopathy (DR).
25352121	6	33	theme	epithelial	724:733	arg1	ARPE-19					693:699	Hyperglycemia-exposed ARPE-19	671:699	Hyperglycemia-exposed ARPE-19 (human retinal pigment epithelial cells)	671:740	METHODS Hyperglycemia-exposed ARPE-19 (human retinal pigment epithelial cells) and TR-iBRB (rat retinal microendothelial cells) were assayed for levels of VEGF-A by qRT-PCR, Western blot, and ELISA.
25352121	6	33	theme	epithelial	724:733	arg1	cells					735:739	human retinal pigment epithelial cells	702:739	human retinal pigment epithelial cells	702:739	METHODS Hyperglycemia-exposed ARPE-19 (human retinal pigment epithelial cells) and TR-iBRB (rat retinal microendothelial cells) were assayed for levels of VEGF-A by qRT-PCR, Western blot, and ELISA.
25352121	0	34	theme	factor	39:44	arg1	Sp1					46:48	transcription factor Sp1	25:48	transcription factor Sp1	25:48	O-GlcNAc modification of transcription factor Sp1 mediates hyperglycemia-induced VEGF-A upregulation in retinal cells.
25352121	10	35	theme	Chromatin	1183:1191	arg1	ChIP					1214:1217	ChIP	1214:1217	ChIP	1214:1217	Chromatin immunoprecipitation (ChIP) was used to assess Sp1 occupancy on the VEGF-A promoter.
25352121	10	35	theme	Chromatin	1183:1191	arg1	immunoprecipitation					1193:1211	Chromatin immunoprecipitation	1183:1211	Chromatin immunoprecipitation (ChIP)	1183:1218	Chromatin immunoprecipitation (ChIP) was used to assess Sp1 occupancy on the VEGF-A promoter.
25352121	3	36	dep	factor	382:387	arg1	protein					401:407	specificity protein 1	389:409	the transcription factor specificity protein 1 (Sp1)	364:415	The VEGF-A promoter is responsive to the transcription factor specificity protein 1 (Sp1).
25352121	3	36	dep	factor	382:387	arg1	Sp1					412:414	Sp1	412:414	Sp1	412:414	The VEGF-A promoter is responsive to the transcription factor specificity protein 1 (Sp1).
25352121	9	37	theme	glucose	1142:1148	arg1	sensitivity					1150:1160	glucose sensitivity	1142:1160	glucose sensitivity	1142:1160	The proximal VEGF-A promoter was analyzed for glucose sensitivity by luciferase assay.
25352121	13	38	theme	glucose-driven	1498:1511	arg1	VEGF-A					1513:1518	glucose-driven VEGF-A	1498:1518	glucose-driven VEGF-A	1498:1518	O-GlcNAc transferase inhibition abrogated glucose-driven VEGF-A.
25352121	17	39	from	pathogenesis	1896:1907	arg1	significant					1877:1887	significant	1877:1887	significant	1877:1887	This mechanism may be significant in the pathogenesis of preclinical DR through VEGF-A upregulation.
25352121	16	40	theme	Sp1	1829:1831	arg1	factor					1847:1852	the Sp1 transcription factor	1825:1852	the Sp1 transcription factor	1825:1852	CONCLUSIONS Hyperglycemia-driven VEGF-A production is mediated by elevated O-GlcNAc modification of the Sp1 transcription factor.
25352121	5	41	dep	endothelium	627:637	arg1	the					615:617	the	615:617	the	615:617	This study investigated the effects of hyperglycemia on Sp1-mediated expression of VEGF-A in the retinal endothelium and pigment epithelium.
25352121	13	42	theme	O-GlcNAc	1456:1463	arg1	inhibition					1477:1486	O-GlcNAc transferase inhibition	1456:1486	O-GlcNAc transferase inhibition	1456:1486	O-GlcNAc transferase inhibition abrogated glucose-driven VEGF-A.
25352121	16	43	theme	factor	1847:1852	arg1	modification					1809:1820	elevated O-GlcNAc modification	1791:1820	elevated O-GlcNAc modification of the Sp1 transcription factor	1791:1852	CONCLUSIONS Hyperglycemia-driven VEGF-A production is mediated by elevated O-GlcNAc modification of the Sp1 transcription factor.
25352121	8	44	theme	Vascular	980:987	arg1	factor-A					1008:1015	Vascular endothelial growth factor-A protein and transcript	980:1038	Vascular endothelial growth factor-A protein and transcript	980:1038	Vascular endothelial growth factor-A protein and transcript were measured in cells depleted of OGT or Sp1 by shRNA.
25352121	10	45	used	used	1224:1227	arg2	immunoprecipitation					1193:1211	Chromatin immunoprecipitation	1183:1211	Chromatin immunoprecipitation (ChIP)	1183:1218	Chromatin immunoprecipitation (ChIP) was used to assess Sp1 occupancy on the VEGF-A promoter.
25352121	10	45	used	used	1224:1227	arg2	ChIP					1214:1217	ChIP	1214:1217	ChIP	1214:1217	Chromatin immunoprecipitation (ChIP) was used to assess Sp1 occupancy on the VEGF-A promoter.
25352121	6	46	theme	microendothelial	767:782	arg1	cells					784:788	rat retinal microendothelial cells	755:788	rat retinal microendothelial cells	755:788	METHODS Hyperglycemia-exposed ARPE-19 (human retinal pigment epithelial cells) and TR-iBRB (rat retinal microendothelial cells) were assayed for levels of VEGF-A by qRT-PCR, Western blot, and ELISA.
25352121	6	46	theme	microendothelial	767:782	arg1	TR-iBRB					746:752	TR-iBRB	746:752	TR-iBRB (rat retinal microendothelial cells)	746:789	METHODS Hyperglycemia-exposed ARPE-19 (human retinal pigment epithelial cells) and TR-iBRB (rat retinal microendothelial cells) were assayed for levels of VEGF-A by qRT-PCR, Western blot, and ELISA.
25352121	16	47	dep	CONCLUSIONS	1725:1735	arg1	mediated					1779:1786	mediated	1779:1786	is mediated by elevated O-GlcNAc modification of the Sp1 transcription factor	1776:1852	CONCLUSIONS Hyperglycemia-driven VEGF-A production is mediated by elevated O-GlcNAc modification of the Sp1 transcription factor.
25352121	4	48	theme	O-GlcNAc	422:429	arg1	modification					431:442	The O-GlcNAc modification	418:442	The O-GlcNAc modification	418:442	The O-GlcNAc modification is driven by glucose concentration and has a profound effect on Sp1 activity.
25352121	14	49	theme	Cellular	1521:1528	arg1	depletion					1530:1538	Cellular depletion	1521:1538	Cellular depletion of OGT or Sp1 by shRNA	1521:1561	Cellular depletion of OGT or Sp1 by shRNA significantly abrogated glucose-induced changes in VEGF-A.
25352121	6	50	theme	Western	837:843	arg1	blot					845:848	Western blot	837:848	Western blot	837:848	METHODS Hyperglycemia-exposed ARPE-19 (human retinal pigment epithelial cells) and TR-iBRB (rat retinal microendothelial cells) were assayed for levels of VEGF-A by qRT-PCR, Western blot, and ELISA.
25352121	2	51	theme	retinal	312:318	arg1	cells					320:324	retinal cells	312:324	retinal cells	312:324	In preclinical DR, hyperglycemia can upregulate VEGF-A in retinal cells.
25352121	7	52	theme	transferase	900:910	arg1	inhibitors					877:886	Small molecule inhibitors	862:886	Small molecule inhibitors of O-GlcNAc transferase (OGT) or O-GlcNAcase (OGA)	862:937	Small molecule inhibitors of O-GlcNAc transferase (OGT) or O-GlcNAcase (OGA) were used to manipulate O-GlcNAc levels.
25352121	1	53	theme	diabetic	227:234	arg1	retinopathy					236:246	diabetic retinopathy	227:246	diabetic retinopathy	227:246	PURPOSE Proangiogenic protein VEGF-A contributes significantly to retinal lesions and neovascularization in diabetic retinopathy (DR).
25352121	12	54	theme	OGA	1406:1408	arg1	inhibitors					1410:1419	OGA inhibitors	1406:1419	OGA inhibitors	1406:1419	Elevation of O-GlcNAc by OGA inhibitors was sufficient to increase VEGF-A.
25352121	6	55	theme	VEGF-A	818:823	arg1	levels					808:813	levels	808:813	levels of VEGF-A	808:823	METHODS Hyperglycemia-exposed ARPE-19 (human retinal pigment epithelial cells) and TR-iBRB (rat retinal microendothelial cells) were assayed for levels of VEGF-A by qRT-PCR, Western blot, and ELISA.
25352121	7	56	theme	molecule	868:875	arg1	inhibitors					877:886	Small molecule inhibitors	862:886	Small molecule inhibitors of O-GlcNAc transferase (OGT) or O-GlcNAcase (OGA)	862:937	Small molecule inhibitors of O-GlcNAc transferase (OGT) or O-GlcNAcase (OGA) were used to manipulate O-GlcNAc levels.
25352121	5	57	from	expression	591:600	arg1	endothelium					627:637	retinal endothelium	619:637	retinal endothelium	619:637	This study investigated the effects of hyperglycemia on Sp1-mediated expression of VEGF-A in the retinal endothelium and pigment epithelium.
25352121	5	57	from	expression	591:600	arg1	epithelium					651:660	pigment epithelium	643:660	pigment epithelium	643:660	This study investigated the effects of hyperglycemia on Sp1-mediated expression of VEGF-A in the retinal endothelium and pigment epithelium.
25352121	0	58	from	upregulation	88:99	arg1	cells					112:116	retinal cells	104:116	retinal cells	104:116	O-GlcNAc modification of transcription factor Sp1 mediates hyperglycemia-induced VEGF-A upregulation in retinal cells.
25352121	6	59	dep	METHODS	663:669	arg1	METHODS					663:669	METHODS	663:669	METHODS Hyperglycemia-exposed ARPE-19 (human retinal pigment epithelial cells) and TR-iBRB (rat retinal microendothelial cells)	663:789	METHODS Hyperglycemia-exposed ARPE-19 (human retinal pigment epithelial cells) and TR-iBRB (rat retinal microendothelial cells) were assayed for levels of VEGF-A by qRT-PCR, Western blot, and ELISA.
25352121	6	59	dep	METHODS	663:669	arg1	ARPE-19					693:699	Hyperglycemia-exposed ARPE-19	671:699	Hyperglycemia-exposed ARPE-19 (human retinal pigment epithelial cells)	671:740	METHODS Hyperglycemia-exposed ARPE-19 (human retinal pigment epithelial cells) and TR-iBRB (rat retinal microendothelial cells) were assayed for levels of VEGF-A by qRT-PCR, Western blot, and ELISA.
25352121	6	59	dep	METHODS	663:669	arg1	cells					735:739	human retinal pigment epithelial cells	702:739	human retinal pigment epithelial cells	702:739	METHODS Hyperglycemia-exposed ARPE-19 (human retinal pigment epithelial cells) and TR-iBRB (rat retinal microendothelial cells) were assayed for levels of VEGF-A by qRT-PCR, Western blot, and ELISA.
25352121	6	59	dep	METHODS	663:669	arg1	TR-iBRB					746:752	TR-iBRB	746:752	TR-iBRB (rat retinal microendothelial cells)	746:789	METHODS Hyperglycemia-exposed ARPE-19 (human retinal pigment epithelial cells) and TR-iBRB (rat retinal microendothelial cells) were assayed for levels of VEGF-A by qRT-PCR, Western blot, and ELISA.
25352121	6	59	dep	METHODS	663:669	arg1	cells					784:788	rat retinal microendothelial cells	755:788	rat retinal microendothelial cells	755:788	METHODS Hyperglycemia-exposed ARPE-19 (human retinal pigment epithelial cells) and TR-iBRB (rat retinal microendothelial cells) were assayed for levels of VEGF-A by qRT-PCR, Western blot, and ELISA.
25352121	2	60	theme	preclinical	257:267	arg1	DR					269:270	preclinical DR	257:270	preclinical DR	257:270	In preclinical DR, hyperglycemia can upregulate VEGF-A in retinal cells.
25352121	5	61	theme	Sp1-mediated	578:589	arg1	expression					591:600	Sp1-mediated expression	578:600	Sp1-mediated expression of VEGF-A in the retinal endothelium and pigment epithelium	578:660	This study investigated the effects of hyperglycemia on Sp1-mediated expression of VEGF-A in the retinal endothelium and pigment epithelium.
25352121	1	62	theme	protein	141:147	arg1	VEGF-A					149:154	PURPOSE Proangiogenic protein VEGF-A	119:154	PURPOSE Proangiogenic protein VEGF-A	119:154	PURPOSE Proangiogenic protein VEGF-A contributes significantly to retinal lesions and neovascularization in diabetic retinopathy (DR).
25352121	12	63	theme	O-GlcNAc	1394:1401	arg1	Elevation					1381:1389	Elevation	1381:1389	Elevation of O-GlcNAc by OGA inhibitors	1381:1419	Elevation of O-GlcNAc by OGA inhibitors was sufficient to increase VEGF-A.
25352121	6	64	theme	pigment	716:722	arg1	ARPE-19					693:699	Hyperglycemia-exposed ARPE-19	671:699	Hyperglycemia-exposed ARPE-19 (human retinal pigment epithelial cells)	671:740	METHODS Hyperglycemia-exposed ARPE-19 (human retinal pigment epithelial cells) and TR-iBRB (rat retinal microendothelial cells) were assayed for levels of VEGF-A by qRT-PCR, Western blot, and ELISA.
25352121	6	64	theme	pigment	716:722	arg1	cells					735:739	human retinal pigment epithelial cells	702:739	human retinal pigment epithelial cells	702:739	METHODS Hyperglycemia-exposed ARPE-19 (human retinal pigment epithelial cells) and TR-iBRB (rat retinal microendothelial cells) were assayed for levels of VEGF-A by qRT-PCR, Western blot, and ELISA.
25352121	16	65	theme	elevated	1791:1798	arg1	modification					1809:1820	elevated O-GlcNAc modification	1791:1820	elevated O-GlcNAc modification of the Sp1 transcription factor	1791:1852	CONCLUSIONS Hyperglycemia-driven VEGF-A production is mediated by elevated O-GlcNAc modification of the Sp1 transcription factor.
25352121	3	66	theme	VEGF-A	331:336	arg1	responsive					350:359	responsive	350:359	responsive	350:359	The VEGF-A promoter is responsive to the transcription factor specificity protein 1 (Sp1).
25352121	3	66	theme	VEGF-A	331:336	arg1	promoter					338:345	The VEGF-A promoter	327:345	The VEGF-A promoter	327:345	The VEGF-A promoter is responsive to the transcription factor specificity protein 1 (Sp1).
25352121	6	67	theme	human	702:706	arg1	ARPE-19					693:699	Hyperglycemia-exposed ARPE-19	671:699	Hyperglycemia-exposed ARPE-19 (human retinal pigment epithelial cells)	671:740	METHODS Hyperglycemia-exposed ARPE-19 (human retinal pigment epithelial cells) and TR-iBRB (rat retinal microendothelial cells) were assayed for levels of VEGF-A by qRT-PCR, Western blot, and ELISA.
25352121	6	67	theme	human	702:706	arg1	cells					735:739	human retinal pigment epithelial cells	702:739	human retinal pigment epithelial cells	702:739	METHODS Hyperglycemia-exposed ARPE-19 (human retinal pigment epithelial cells) and TR-iBRB (rat retinal microendothelial cells) were assayed for levels of VEGF-A by qRT-PCR, Western blot, and ELISA.
25352121	3	68	theme	transcription	368:380	arg1	factor					382:387	the transcription factor specificity protein 1 (Sp1)	364:415	the transcription factor specificity protein 1 (Sp1)	364:415	The VEGF-A promoter is responsive to the transcription factor specificity protein 1 (Sp1).
25352121	0	69	theme	retinal	104:110	arg1	cells					112:116	retinal cells	104:116	retinal cells	104:116	O-GlcNAc modification of transcription factor Sp1 mediates hyperglycemia-induced VEGF-A upregulation in retinal cells.
25352121	5	70	theme	hyperglycemia	561:573	arg1	effects					550:556	the effects	546:556	the effects of hyperglycemia on Sp1-mediated expression of VEGF-A in the retinal endothelium and pigment epithelium	546:660	This study investigated the effects of hyperglycemia on Sp1-mediated expression of VEGF-A in the retinal endothelium and pigment epithelium.
25352121	11	71	theme	promoter	1316:1323	arg1	activity					1325:1332	VEGF-A promoter activity	1309:1332	VEGF-A promoter activity	1309:1332	RESULTS Hyperglycemia increased VEGF-A promoter activity and upregulated VEGF-A transcript and protein.
25352121	5	72	theme	pigment	643:649	arg1	epithelium					651:660	pigment epithelium	643:660	pigment epithelium	643:660	This study investigated the effects of hyperglycemia on Sp1-mediated expression of VEGF-A in the retinal endothelium and pigment epithelium.
25352121	9	73	theme	luciferase	1165:1174	arg1	assay					1176:1180	luciferase assay	1165:1180	luciferase assay	1165:1180	The proximal VEGF-A promoter was analyzed for glucose sensitivity by luciferase assay.
25352121	6	74	theme	retinal	759:765	arg1	cells					784:788	rat retinal microendothelial cells	755:788	rat retinal microendothelial cells	755:788	METHODS Hyperglycemia-exposed ARPE-19 (human retinal pigment epithelial cells) and TR-iBRB (rat retinal microendothelial cells) were assayed for levels of VEGF-A by qRT-PCR, Western blot, and ELISA.
25352121	6	74	theme	retinal	759:765	arg1	TR-iBRB					746:752	TR-iBRB	746:752	TR-iBRB (rat retinal microendothelial cells)	746:789	METHODS Hyperglycemia-exposed ARPE-19 (human retinal pigment epithelial cells) and TR-iBRB (rat retinal microendothelial cells) were assayed for levels of VEGF-A by qRT-PCR, Western blot, and ELISA.
25352121	3	75	theme	specificity	389:399	arg1	protein					401:407	specificity protein 1	389:409	the transcription factor specificity protein 1 (Sp1)	364:415	The VEGF-A promoter is responsive to the transcription factor specificity protein 1 (Sp1).
25352121	3	75	theme	specificity	389:399	arg1	Sp1					412:414	Sp1	412:414	Sp1	412:414	The VEGF-A promoter is responsive to the transcription factor specificity protein 1 (Sp1).
25352121	11	76	theme	VEGF-A	1350:1355	arg1	transcript					1357:1366	VEGF-A transcript	1350:1366	VEGF-A transcript	1350:1366	RESULTS Hyperglycemia increased VEGF-A promoter activity and upregulated VEGF-A transcript and protein.
25352121	16	77	theme	Hyperglycemia-driven	1737:1756	arg1	production					1765:1774	Hyperglycemia-driven VEGF-A production	1737:1774	Hyperglycemia-driven VEGF-A production	1737:1774	CONCLUSIONS Hyperglycemia-driven VEGF-A production is mediated by elevated O-GlcNAc modification of the Sp1 transcription factor.
25352121	14	78	theme	glucose-induced	1587:1601	arg1	changes					1603:1609	glucose-induced changes	1587:1609	glucose-induced changes in VEGF-A	1587:1619	Cellular depletion of OGT or Sp1 by shRNA significantly abrogated glucose-induced changes in VEGF-A.
25352121	9	79	theme	VEGF-A	1109:1114	arg1	promoter					1116:1123	The proximal VEGF-A promoter	1096:1123	The proximal VEGF-A promoter	1096:1123	The proximal VEGF-A promoter was analyzed for glucose sensitivity by luciferase assay.
25352121	0	80	theme	transcription	25:37	arg1	Sp1					46:48	transcription factor Sp1	25:48	transcription factor Sp1	25:48	O-GlcNAc modification of transcription factor Sp1 mediates hyperglycemia-induced VEGF-A upregulation in retinal cells.
25352121	5	81	theme	retinal	619:625	arg1	endothelium					627:637	retinal endothelium	619:637	retinal endothelium	619:637	This study investigated the effects of hyperglycemia on Sp1-mediated expression of VEGF-A in the retinal endothelium and pigment epithelium.
25352121	1	82	theme	PURPOSE	119:125	arg1	VEGF-A					149:154	PURPOSE Proangiogenic protein VEGF-A	119:154	PURPOSE Proangiogenic protein VEGF-A	119:154	PURPOSE Proangiogenic protein VEGF-A contributes significantly to retinal lesions and neovascularization in diabetic retinopathy (DR).
25352121	15	83	theme	ChIP	1622:1625	arg1	analysis					1627:1634	ChIP analysis	1622:1634	ChIP analysis	1622:1634	ChIP analysis showed that hyperglycemia significantly increased binding of Sp1 to the VEGF-A promoter.
25352121	14	84	from	changes	1603:1609	arg1	VEGF-A					1614:1619	VEGF-A	1614:1619	VEGF-A	1614:1619	Cellular depletion of OGT or Sp1 by shRNA significantly abrogated glucose-induced changes in VEGF-A.
25352121	0	85	theme	Sp1	46:48	arg1	modification					9:20	O-GlcNAc modification	0:20	O-GlcNAc modification of transcription factor Sp1	0:48	O-GlcNAc modification of transcription factor Sp1 mediates hyperglycemia-induced VEGF-A upregulation in retinal cells.
25352121	4	86	contain	has	483:485	arg2	effect					498:503	a profound effect	487:503	a profound effect	487:503	The O-GlcNAc modification is driven by glucose concentration and has a profound effect on Sp1 activity.
25352121	4	86	contain	has	483:485	arg1	modification					431:442	The O-GlcNAc modification	418:442	The O-GlcNAc modification	418:442	The O-GlcNAc modification is driven by glucose concentration and has a profound effect on Sp1 activity.
25352121	0	87	theme	hyperglycemia-induced	59:79	arg1	upregulation					88:99	hyperglycemia-induced VEGF-A upregulation	59:99	hyperglycemia-induced VEGF-A upregulation in retinal cells	59:116	O-GlcNAc modification of transcription factor Sp1 mediates hyperglycemia-induced VEGF-A upregulation in retinal cells.
25352121	11	88	theme	RESULTS	1277:1283	arg1	Hyperglycemia					1285:1297	RESULTS Hyperglycemia	1277:1297	RESULTS Hyperglycemia	1277:1297	RESULTS Hyperglycemia increased VEGF-A promoter activity and upregulated VEGF-A transcript and protein.
25352121	4	89	theme	profound	489:496	arg1	effect					498:503	a profound effect	487:503	a profound effect	487:503	The O-GlcNAc modification is driven by glucose concentration and has a profound effect on Sp1 activity.
25352121	17	90	theme	preclinical	1912:1922	arg1	DR					1924:1925	preclinical DR	1912:1925	preclinical DR	1912:1925	This mechanism may be significant in the pathogenesis of preclinical DR through VEGF-A upregulation.
25352121	15	91	theme	VEGF-A	1708:1713	arg1	promoter					1715:1722	the VEGF-A promoter	1704:1722	the VEGF-A promoter	1704:1722	ChIP analysis showed that hyperglycemia significantly increased binding of Sp1 to the VEGF-A promoter.
25352121	7	92	theme	O-GlcNAcase	921:931	arg1	inhibitors					877:886	Small molecule inhibitors	862:886	Small molecule inhibitors of O-GlcNAc transferase (OGT) or O-GlcNAcase (OGA)	862:937	Small molecule inhibitors of O-GlcNAc transferase (OGT) or O-GlcNAcase (OGA) were used to manipulate O-GlcNAc levels.
25352121	14	93	theme	Sp1	1550:1552	arg1	depletion					1530:1538	Cellular depletion	1521:1538	Cellular depletion of OGT or Sp1 by shRNA	1521:1561	Cellular depletion of OGT or Sp1 by shRNA significantly abrogated glucose-induced changes in VEGF-A.
25352121	13	94	theme	transferase	1465:1475	arg1	inhibition					1477:1486	O-GlcNAc transferase inhibition	1456:1486	O-GlcNAc transferase inhibition	1456:1486	O-GlcNAc transferase inhibition abrogated glucose-driven VEGF-A.
25352121	16	95	theme	transcription	1833:1845	arg1	factor					1847:1852	the Sp1 transcription factor	1825:1852	the Sp1 transcription factor	1825:1852	CONCLUSIONS Hyperglycemia-driven VEGF-A production is mediated by elevated O-GlcNAc modification of the Sp1 transcription factor.
17049555	0	0	from	association	20:30	arg1	cells					53:57	interphase cells	42:57	interphase cells	42:57	Increased chromatin association of Sp1 in interphase cells by PP2A-mediated dephosphorylations.
17049555	8	1	theme	general	1273:1279	arg1	feature					1281:1287	a general feature	1271:1287	a general feature of dividing cells	1271:1305	We propose that the coordinated dephosphorylation of several Sp1 residues, a general feature of dividing cells, is a required post-translational mechanism for Sp1-dependent transcription of genes related to cell division.
17049555	8	1	theme	general	1273:1279	arg1	dephosphorylation					1228:1244	the coordinated dephosphorylation	1212:1244	the coordinated dephosphorylation of several Sp1 residues	1212:1268	We propose that the coordinated dephosphorylation of several Sp1 residues, a general feature of dividing cells, is a required post-translational mechanism for Sp1-dependent transcription of genes related to cell division.
17049555	4	2	theme	antibody	616:623	arg1	Analysis					538:545	Analysis	538:545	Analysis of the expression of Sp1 point mutants	538:584	Analysis of the expression of Sp1 point mutants and use of a phospho-specific antibody enabled identification of serine 59 as a major target of PP2A during cell-cycle interphase.
17049555	4	2	theme	antibody	616:623	arg1	use					590:592	use	590:592	use of a phospho-specific antibody	590:623	Analysis of the expression of Sp1 point mutants and use of a phospho-specific antibody enabled identification of serine 59 as a major target of PP2A during cell-cycle interphase.
17049555	5	3	theme	Sp1	782:784	arg1	association					786:796	Sp1 association	782:796	Sp1 association with chromatin	782:811	Importantly, serine 59 dephosphorylation appeared to up-regulate Sp1 association with chromatin.
17049555	4	4	theme	expression	554:563	arg1	Analysis					538:545	Analysis	538:545	Analysis of the expression of Sp1 point mutants	538:584	Analysis of the expression of Sp1 point mutants and use of a phospho-specific antibody enabled identification of serine 59 as a major target of PP2A during cell-cycle interphase.
17049555	4	4	theme	expression	554:563	arg1	use					590:592	use	590:592	use of a phospho-specific antibody	590:623	Analysis of the expression of Sp1 point mutants and use of a phospho-specific antibody enabled identification of serine 59 as a major target of PP2A during cell-cycle interphase.
17049555	2	5	theme	transcriptional	326:340	arg1	activity					342:349	Sp1 transcriptional activity	322:349	Sp1 transcriptional activity	322:349	This event occurs concurrently with cell-cycle interphase and increases Sp1 transcriptional activity and in vitro affinity for DNA.
17049555	4	6	theme	cell-cycle	694:703	arg1	interphase					705:714	cell-cycle interphase	694:714	cell-cycle interphase	694:714	Analysis of the expression of Sp1 point mutants and use of a phospho-specific antibody enabled identification of serine 59 as a major target of PP2A during cell-cycle interphase.
17049555	7	7	theme	PP2A	1162:1165	arg1	target					1152:1157	another target	1144:1157	another target of PP2A	1144:1165	In addition, we demonstrated by phosphopeptide mapping that threonine 681, which belongs to the latter region, is another target of PP2A, yet unrelated to serine 59.
17049555	2	8	theme	Sp1	322:324	arg1	activity					342:349	Sp1 transcriptional activity	322:349	Sp1 transcriptional activity	322:349	This event occurs concurrently with cell-cycle interphase and increases Sp1 transcriptional activity and in vitro affinity for DNA.
17049555	8	9	theme	post-translational	1322:1339	arg1	dephosphorylation					1228:1244	the coordinated dephosphorylation	1212:1244	the coordinated dephosphorylation of several Sp1 residues	1212:1268	We propose that the coordinated dephosphorylation of several Sp1 residues, a general feature of dividing cells, is a required post-translational mechanism for Sp1-dependent transcription of genes related to cell division.
17049555	8	9	theme	post-translational	1322:1339	arg1	mechanism					1341:1349	a required post-translational mechanism	1311:1349	a required post-translational mechanism for Sp1-dependent transcription of genes related to cell division	1311:1415	We propose that the coordinated dephosphorylation of several Sp1 residues, a general feature of dividing cells, is a required post-translational mechanism for Sp1-dependent transcription of genes related to cell division.
17049555	8	10	theme	required	1313:1320	arg1	dephosphorylation					1228:1244	the coordinated dephosphorylation	1212:1244	the coordinated dephosphorylation of several Sp1 residues	1212:1268	We propose that the coordinated dephosphorylation of several Sp1 residues, a general feature of dividing cells, is a required post-translational mechanism for Sp1-dependent transcription of genes related to cell division.
17049555	8	10	theme	required	1313:1320	arg1	mechanism					1341:1349	a required post-translational mechanism	1311:1349	a required post-translational mechanism for Sp1-dependent transcription of genes related to cell division	1311:1415	We propose that the coordinated dephosphorylation of several Sp1 residues, a general feature of dividing cells, is a required post-translational mechanism for Sp1-dependent transcription of genes related to cell division.
17049555	7	11	dep	unrelated	1172:1180	arg1	target					1152:1157	another target	1144:1157	another target of PP2A	1144:1165	In addition, we demonstrated by phosphopeptide mapping that threonine 681, which belongs to the latter region, is another target of PP2A, yet unrelated to serine 59.
17049555	4	12	theme	major	666:670	arg1	identification					633:646	identification	633:646	identification of serine 59	633:659	Analysis of the expression of Sp1 point mutants and use of a phospho-specific antibody enabled identification of serine 59 as a major target of PP2A during cell-cycle interphase.
17049555	4	12	theme	major	666:670	arg1	target					672:677	a major target	664:677	a major target of PP2A	664:685	Analysis of the expression of Sp1 point mutants and use of a phospho-specific antibody enabled identification of serine 59 as a major target of PP2A during cell-cycle interphase.
17049555	8	13	theme	cell	1403:1406	arg1	division					1408:1415	cell division	1403:1415	cell division	1403:1415	We propose that the coordinated dephosphorylation of several Sp1 residues, a general feature of dividing cells, is a required post-translational mechanism for Sp1-dependent transcription of genes related to cell division.
17049555	3	14	theme	phosphorylated	472:485	arg1	counterparts					487:498	its phosphorylated counterparts	468:498	its phosphorylated counterparts from either resting or mitotic cells	468:535	We show here that dephosphorylated Sp1 is associated with chromatin more tightly than its phosphorylated counterparts from either resting or mitotic cells.
17049555	8	15	theme	residues	1261:1268	arg1	dephosphorylation					1228:1244	the coordinated dephosphorylation	1212:1244	the coordinated dephosphorylation of several Sp1 residues	1212:1268	We propose that the coordinated dephosphorylation of several Sp1 residues, a general feature of dividing cells, is a required post-translational mechanism for Sp1-dependent transcription of genes related to cell division.
17049555	8	15	theme	residues	1261:1268	arg1	feature					1281:1287	a general feature	1271:1287	a general feature of dividing cells	1271:1305	We propose that the coordinated dephosphorylation of several Sp1 residues, a general feature of dividing cells, is a required post-translational mechanism for Sp1-dependent transcription of genes related to cell division.
17049555	8	15	theme	residues	1261:1268	arg1	mechanism					1341:1349	a required post-translational mechanism	1311:1349	a required post-translational mechanism for Sp1-dependent transcription of genes related to cell division	1311:1415	We propose that the coordinated dephosphorylation of several Sp1 residues, a general feature of dividing cells, is a required post-translational mechanism for Sp1-dependent transcription of genes related to cell division.
17049555	0	16	theme	chromatin	10:18	arg1	association					20:30	chromatin association	10:30	chromatin association of Sp1 in interphase cells	10:57	Increased chromatin association of Sp1 in interphase cells by PP2A-mediated dephosphorylations.
17049555	3	17	from	cells	531:535	arg1	counterparts					487:498	its phosphorylated counterparts	468:498	its phosphorylated counterparts from either resting or mitotic cells	468:535	We show here that dephosphorylated Sp1 is associated with chromatin more tightly than its phosphorylated counterparts from either resting or mitotic cells.
17049555	1	18	theme	Sp1	96:98	arg1	dephosphorylation					100:116	Sp1 dephosphorylation	96:116	Sp1 dephosphorylation by phosphatase 2A	96:134	Sp1 dephosphorylation by phosphatase 2A is related to sustained cellular proliferation and is illustrated by an enhanced electrophoretic migration shift.
17049555	6	19	mod	modification	921:932	arg3	O-phosphate/O-GlcNAc					900:919	the reciprocal O-phosphate/O-GlcNAc modification	885:932	the reciprocal O-phosphate/O-GlcNAc modification of other residues, some of which are likely to belong to the Sp1 C-terminal DNA-binding domain	885:1027	Various studies suggested that this might occur through the control of the reciprocal O-phosphate/O-GlcNAc modification of other residues, some of which are likely to belong to the Sp1 C-terminal DNA-binding domain.
17049555	6	19	mod	modification	921:932	arg1	residues					943:950	other residues	937:950	other residues	937:950	Various studies suggested that this might occur through the control of the reciprocal O-phosphate/O-GlcNAc modification of other residues, some of which are likely to belong to the Sp1 C-terminal DNA-binding domain.
17049555	2	20	theme	in	355:356	arg1	affinity					364:371	in vitro affinity	355:371	in vitro affinity for DNA	355:379	This event occurs concurrently with cell-cycle interphase and increases Sp1 transcriptional activity and in vitro affinity for DNA.
17049555	8	21	theme	dividing	1292:1299	arg1	cells					1301:1305	dividing cells	1292:1305	dividing cells	1292:1305	We propose that the coordinated dephosphorylation of several Sp1 residues, a general feature of dividing cells, is a required post-translational mechanism for Sp1-dependent transcription of genes related to cell division.
17049555	6	22	theme	residues	943:950	arg1	modification					921:932	the reciprocal O-phosphate/O-GlcNAc modification	885:932	the reciprocal O-phosphate/O-GlcNAc modification of other residues, some of which are likely to belong to the Sp1 C-terminal DNA-binding domain	885:1027	Various studies suggested that this might occur through the control of the reciprocal O-phosphate/O-GlcNAc modification of other residues, some of which are likely to belong to the Sp1 C-terminal DNA-binding domain.
17049555	3	23	theme	dephosphorylated	400:415	arg1	Sp1					417:419	dephosphorylated Sp1	400:419	dephosphorylated Sp1	400:419	We show here that dephosphorylated Sp1 is associated with chromatin more tightly than its phosphorylated counterparts from either resting or mitotic cells.
17049555	7	24	theme	latter	1126:1131	arg1	region					1133:1138	the latter region	1122:1138	the latter region	1122:1138	In addition, we demonstrated by phosphopeptide mapping that threonine 681, which belongs to the latter region, is another target of PP2A, yet unrelated to serine 59.
17049555	1	25	theme	enhanced	208:215	arg1	shift					243:247	an enhanced electrophoretic migration shift	205:247	an enhanced electrophoretic migration shift	205:247	Sp1 dephosphorylation by phosphatase 2A is related to sustained cellular proliferation and is illustrated by an enhanced electrophoretic migration shift.
17049555	4	26	theme	phospho-specific	599:614	arg1	antibody					616:623	a phospho-specific antibody	597:623	a phospho-specific antibody	597:623	Analysis of the expression of Sp1 point mutants and use of a phospho-specific antibody enabled identification of serine 59 as a major target of PP2A during cell-cycle interphase.
17049555	6	27	theme	Various	814:820	arg1	studies					822:828	Various studies	814:828	Various studies	814:828	Various studies suggested that this might occur through the control of the reciprocal O-phosphate/O-GlcNAc modification of other residues, some of which are likely to belong to the Sp1 C-terminal DNA-binding domain.
17049555	1	28	theme	phosphatase	121:131	arg1	2A					133:134	phosphatase 2A	121:134	phosphatase 2A	121:134	Sp1 dephosphorylation by phosphatase 2A is related to sustained cellular proliferation and is illustrated by an enhanced electrophoretic migration shift.
17049555	1	29	theme	electrophoretic	217:231	arg1	shift					243:247	an enhanced electrophoretic migration shift	205:247	an enhanced electrophoretic migration shift	205:247	Sp1 dephosphorylation by phosphatase 2A is related to sustained cellular proliferation and is illustrated by an enhanced electrophoretic migration shift.
17049555	8	30	theme	Sp1	1257:1259	arg1	residues					1261:1268	several Sp1 residues	1249:1268	several Sp1 residues	1249:1268	We propose that the coordinated dephosphorylation of several Sp1 residues, a general feature of dividing cells, is a required post-translational mechanism for Sp1-dependent transcription of genes related to cell division.
17049555	4	31	theme	PP2A	682:685	arg1	identification					633:646	identification	633:646	identification of serine 59	633:659	Analysis of the expression of Sp1 point mutants and use of a phospho-specific antibody enabled identification of serine 59 as a major target of PP2A during cell-cycle interphase.
17049555	4	31	theme	PP2A	682:685	arg1	target					672:677	a major target	664:677	a major target of PP2A	664:685	Analysis of the expression of Sp1 point mutants and use of a phospho-specific antibody enabled identification of serine 59 as a major target of PP2A during cell-cycle interphase.
17049555	8	32	theme	Sp1-dependent	1355:1367	arg1	transcription					1369:1381	Sp1-dependent transcription	1355:1381	Sp1-dependent transcription of genes related to cell division	1355:1415	We propose that the coordinated dephosphorylation of several Sp1 residues, a general feature of dividing cells, is a required post-translational mechanism for Sp1-dependent transcription of genes related to cell division.
17049555	1	33	theme	migration	233:241	arg1	shift					243:247	an enhanced electrophoretic migration shift	205:247	an enhanced electrophoretic migration shift	205:247	Sp1 dephosphorylation by phosphatase 2A is related to sustained cellular proliferation and is illustrated by an enhanced electrophoretic migration shift.
17049555	0	34	theme	Sp1	35:37	arg1	association					20:30	chromatin association	10:30	chromatin association of Sp1 in interphase cells	10:57	Increased chromatin association of Sp1 in interphase cells by PP2A-mediated dephosphorylations.
17049555	4	35	theme	point	572:576	arg1	mutants					578:584	Sp1 point mutants	568:584	Sp1 point mutants	568:584	Analysis of the expression of Sp1 point mutants and use of a phospho-specific antibody enabled identification of serine 59 as a major target of PP2A during cell-cycle interphase.
17049555	8	36	theme	several	1249:1255	arg1	residues					1261:1268	several Sp1 residues	1249:1268	several Sp1 residues	1249:1268	We propose that the coordinated dephosphorylation of several Sp1 residues, a general feature of dividing cells, is a required post-translational mechanism for Sp1-dependent transcription of genes related to cell division.
17049555	6	37	theme	other	937:941	arg1	residues					943:950	other residues	937:950	other residues	937:950	Various studies suggested that this might occur through the control of the reciprocal O-phosphate/O-GlcNAc modification of other residues, some of which are likely to belong to the Sp1 C-terminal DNA-binding domain.
17049555	8	38	theme	coordinated	1216:1226	arg1	dephosphorylation					1228:1244	the coordinated dephosphorylation	1212:1244	the coordinated dephosphorylation of several Sp1 residues	1212:1268	We propose that the coordinated dephosphorylation of several Sp1 residues, a general feature of dividing cells, is a required post-translational mechanism for Sp1-dependent transcription of genes related to cell division.
17049555	8	38	theme	coordinated	1216:1226	arg1	feature					1281:1287	a general feature	1271:1287	a general feature of dividing cells	1271:1305	We propose that the coordinated dephosphorylation of several Sp1 residues, a general feature of dividing cells, is a required post-translational mechanism for Sp1-dependent transcription of genes related to cell division.
17049555	8	38	theme	coordinated	1216:1226	arg1	mechanism					1341:1349	a required post-translational mechanism	1311:1349	a required post-translational mechanism for Sp1-dependent transcription of genes related to cell division	1311:1415	We propose that the coordinated dephosphorylation of several Sp1 residues, a general feature of dividing cells, is a required post-translational mechanism for Sp1-dependent transcription of genes related to cell division.
17049555	4	39	theme	Sp1	568:570	arg1	mutants					578:584	Sp1 point mutants	568:584	Sp1 point mutants	568:584	Analysis of the expression of Sp1 point mutants and use of a phospho-specific antibody enabled identification of serine 59 as a major target of PP2A during cell-cycle interphase.
17049555	8	40	theme	related	1392:1398	arg1	genes					1386:1390	genes	1386:1390	genes related to cell division	1386:1415	We propose that the coordinated dephosphorylation of several Sp1 residues, a general feature of dividing cells, is a required post-translational mechanism for Sp1-dependent transcription of genes related to cell division.
17049555	7	41	theme	phosphopeptide	1062:1075	arg1	mapping					1077:1083	phosphopeptide mapping	1062:1083	phosphopeptide mapping	1062:1083	In addition, we demonstrated by phosphopeptide mapping that threonine 681, which belongs to the latter region, is another target of PP2A, yet unrelated to serine 59.
17049555	6	42	theme	DNA-binding	1010:1020	arg1	domain					1022:1027	the Sp1 C-terminal DNA-binding domain	991:1027	the Sp1 C-terminal DNA-binding domain	991:1027	Various studies suggested that this might occur through the control of the reciprocal O-phosphate/O-GlcNAc modification of other residues, some of which are likely to belong to the Sp1 C-terminal DNA-binding domain.
17049555	0	43	theme	interphase	42:51	arg1	cells					53:57	interphase cells	42:57	interphase cells	42:57	Increased chromatin association of Sp1 in interphase cells by PP2A-mediated dephosphorylations.
17049555	6	44	theme	Sp1	995:997	arg1	domain					1022:1027	the Sp1 C-terminal DNA-binding domain	991:1027	the Sp1 C-terminal DNA-binding domain	991:1027	Various studies suggested that this might occur through the control of the reciprocal O-phosphate/O-GlcNAc modification of other residues, some of which are likely to belong to the Sp1 C-terminal DNA-binding domain.
17049555	6	45	theme	modification	921:932	arg1	control					874:880	the control	870:880	the control of the reciprocal O-phosphate/O-GlcNAc modification of other residues, some of which are likely to belong to the Sp1 C-terminal DNA-binding domain	870:1027	Various studies suggested that this might occur through the control of the reciprocal O-phosphate/O-GlcNAc modification of other residues, some of which are likely to belong to the Sp1 C-terminal DNA-binding domain.
17049555	5	46	with	association	786:796	arg1	chromatin					803:811	chromatin	803:811	chromatin	803:811	Importantly, serine 59 dephosphorylation appeared to up-regulate Sp1 association with chromatin.
17049555	3	47	from	resting	512:518	arg1	counterparts					487:498	its phosphorylated counterparts	468:498	its phosphorylated counterparts from either resting or mitotic cells	468:535	We show here that dephosphorylated Sp1 is associated with chromatin more tightly than its phosphorylated counterparts from either resting or mitotic cells.
17049555	4	48	theme	mutants	578:584	arg1	expression					554:563	the expression	550:563	the expression of Sp1 point mutants	550:584	Analysis of the expression of Sp1 point mutants and use of a phospho-specific antibody enabled identification of serine 59 as a major target of PP2A during cell-cycle interphase.
17049555	5	49	theme	serine	730:735	arg1	dephosphorylation					740:756	serine 59 dephosphorylation	730:756	serine 59 dephosphorylation	730:756	Importantly, serine 59 dephosphorylation appeared to up-regulate Sp1 association with chromatin.
17049555	6	50	theme	O-phosphate/O-GlcNAc	900:919	arg1	modification					921:932	the reciprocal O-phosphate/O-GlcNAc modification	885:932	the reciprocal O-phosphate/O-GlcNAc modification of other residues, some of which are likely to belong to the Sp1 C-terminal DNA-binding domain	885:1027	Various studies suggested that this might occur through the control of the reciprocal O-phosphate/O-GlcNAc modification of other residues, some of which are likely to belong to the Sp1 C-terminal DNA-binding domain.
17049555	3	51	theme	mitotic	523:529	arg1	cells					531:535	mitotic cells	523:535	mitotic cells	523:535	We show here that dephosphorylated Sp1 is associated with chromatin more tightly than its phosphorylated counterparts from either resting or mitotic cells.
17049555	6	52	theme	reciprocal	889:898	arg1	modification					921:932	the reciprocal O-phosphate/O-GlcNAc modification	885:932	the reciprocal O-phosphate/O-GlcNAc modification of other residues, some of which are likely to belong to the Sp1 C-terminal DNA-binding domain	885:1027	Various studies suggested that this might occur through the control of the reciprocal O-phosphate/O-GlcNAc modification of other residues, some of which are likely to belong to the Sp1 C-terminal DNA-binding domain.
17049555	2	53	theme	cell-cycle	286:295	arg1	interphase					297:306	cell-cycle interphase	286:306	cell-cycle interphase	286:306	This event occurs concurrently with cell-cycle interphase and increases Sp1 transcriptional activity and in vitro affinity for DNA.
17049555	2	54	dep	in	355:356	arg1	vitro					358:362	vitro	358:362	vitro	358:362	This event occurs concurrently with cell-cycle interphase and increases Sp1 transcriptional activity and in vitro affinity for DNA.
17049555	8	55	theme	genes	1386:1390	arg1	transcription					1369:1381	Sp1-dependent transcription	1355:1381	Sp1-dependent transcription of genes related to cell division	1355:1415	We propose that the coordinated dephosphorylation of several Sp1 residues, a general feature of dividing cells, is a required post-translational mechanism for Sp1-dependent transcription of genes related to cell division.
17049555	4	56	theme	serine	651:656	arg1	identification					633:646	identification	633:646	identification of serine 59	633:659	Analysis of the expression of Sp1 point mutants and use of a phospho-specific antibody enabled identification of serine 59 as a major target of PP2A during cell-cycle interphase.
17049555	4	56	theme	serine	651:656	arg1	target					672:677	a major target	664:677	a major target of PP2A	664:685	Analysis of the expression of Sp1 point mutants and use of a phospho-specific antibody enabled identification of serine 59 as a major target of PP2A during cell-cycle interphase.
17049555	0	57	theme	PP2A-mediated	62:74	arg1	dephosphorylations					76:93	PP2A-mediated dephosphorylations	62:93	PP2A-mediated dephosphorylations	62:93	Increased chromatin association of Sp1 in interphase cells by PP2A-mediated dephosphorylations.
17049555	8	58	theme	cells	1301:1305	arg1	feature					1281:1287	a general feature	1271:1287	a general feature of dividing cells	1271:1305	We propose that the coordinated dephosphorylation of several Sp1 residues, a general feature of dividing cells, is a required post-translational mechanism for Sp1-dependent transcription of genes related to cell division.
17049555	8	58	theme	cells	1301:1305	arg1	dephosphorylation					1228:1244	the coordinated dephosphorylation	1212:1244	the coordinated dephosphorylation of several Sp1 residues	1212:1268	We propose that the coordinated dephosphorylation of several Sp1 residues, a general feature of dividing cells, is a required post-translational mechanism for Sp1-dependent transcription of genes related to cell division.
17049555	1	59	theme	sustained	150:158	arg1	proliferation					169:181	sustained cellular proliferation	150:181	sustained cellular proliferation	150:181	Sp1 dephosphorylation by phosphatase 2A is related to sustained cellular proliferation and is illustrated by an enhanced electrophoretic migration shift.
17049555	1	60	theme	cellular	160:167	arg1	proliferation					169:181	sustained cellular proliferation	150:181	sustained cellular proliferation	150:181	Sp1 dephosphorylation by phosphatase 2A is related to sustained cellular proliferation and is illustrated by an enhanced electrophoretic migration shift.
17049555	6	61	theme	C-terminal	999:1008	arg1	domain					1022:1027	the Sp1 C-terminal DNA-binding domain	991:1027	the Sp1 C-terminal DNA-binding domain	991:1027	Various studies suggested that this might occur through the control of the reciprocal O-phosphate/O-GlcNAc modification of other residues, some of which are likely to belong to the Sp1 C-terminal DNA-binding domain.
24553187	3	0	theme	cardiac	368:374	arg1	CF					389:390	CF	389:390	CF	389:390	The role that enhanced protein O-GlcNAcylation plays in modulating the phenotype of cardiac fibroblasts (CF) is unknown.
24553187	3	0	theme	cardiac	368:374	arg1	fibroblasts					376:386	cardiac fibroblasts	368:386	cardiac fibroblasts (CF)	368:391	The role that enhanced protein O-GlcNAcylation plays in modulating the phenotype of cardiac fibroblasts (CF) is unknown.
24553187	4	1	theme	high-glucose	489:500	arg1	media					514:518	normal glucose (NG; 5 mM glucose) or high-glucose (HG; 25 mM) media	452:518	normal glucose (NG; 5 mM glucose) or high-glucose (HG; 25 mM) media	452:518	To address this issue, rat CF were cultured in normal glucose (NG; 5 mM glucose) or high-glucose (HG; 25 mM) media for 48 h. Results demonstrate that CF cultured in HG have higher levels (~50%) of overall protein O-GlcNAcylation vs. NG cells.
24553187	6	2	from	evidence	917:924	arg1	cells					955:959	HG cells	952:959	HG cells	952:959	The nuclear transcription factor Sp1 and arginase II evidence excess O-GlcNAcylation in HG cells.
24553187	4	3	theme	cells	641:645	arg1	levels					585:590	higher levels	578:590	higher levels (~50%) of overall protein O-GlcNAcylation vs. NG cells	578:645	To address this issue, rat CF were cultured in normal glucose (NG; 5 mM glucose) or high-glucose (HG; 25 mM) media for 48 h. Results demonstrate that CF cultured in HG have higher levels (~50%) of overall protein O-GlcNAcylation vs. NG cells.
24553187	4	3	theme	cells	641:645	arg1	%					596:596	~50%	593:596	~50%	593:596	To address this issue, rat CF were cultured in normal glucose (NG; 5 mM glucose) or high-glucose (HG; 25 mM) media for 48 h. Results demonstrate that CF cultured in HG have higher levels (~50%) of overall protein O-GlcNAcylation vs. NG cells.
24553187	7	4	from	Expression	962:971	arg1	CF					976:977	CF	976:977	CF	976:977	Expression in CF of an adenovirus coding for the enzyme N-acetylglucosaminidase, which removes O-GlcNAc moieties from proteins, decreased Sp1 and arginase II O-GlcNAcylation and restored HG-induced perturbations in CF back to NG levels.
24553187	3	5	theme	fibroblasts	376:386	arg1	phenotype					355:363	the phenotype	351:363	the phenotype of cardiac fibroblasts (CF)	351:391	The role that enhanced protein O-GlcNAcylation plays in modulating the phenotype of cardiac fibroblasts (CF) is unknown.
24553187	4	6	theme	rat	428:430	arg1	CF					432:433	rat CF	428:433	rat CF	428:433	To address this issue, rat CF were cultured in normal glucose (NG; 5 mM glucose) or high-glucose (HG; 25 mM) media for 48 h. Results demonstrate that CF cultured in HG have higher levels (~50%) of overall protein O-GlcNAcylation vs. NG cells.
24553187	4	7	theme	NG	638:639	arg1	cells					641:645	overall protein O-GlcNAcylation vs. NG cells	602:645	overall protein O-GlcNAcylation vs. NG cells	602:645	To address this issue, rat CF were cultured in normal glucose (NG; 5 mM glucose) or high-glucose (HG; 25 mM) media for 48 h. Results demonstrate that CF cultured in HG have higher levels (~50%) of overall protein O-GlcNAcylation vs. NG cells.
24553187	4	8	theme	NG	468:469	arg1	glucose					459:465	normal glucose	452:465	normal glucose (NG; 5 mM glucose)	452:484	To address this issue, rat CF were cultured in normal glucose (NG; 5 mM glucose) or high-glucose (HG; 25 mM) media for 48 h. Results demonstrate that CF cultured in HG have higher levels (~50%) of overall protein O-GlcNAcylation vs. NG cells.
24553187	4	8	theme	NG	468:469	arg1	glucose					477:483	NG; 5 mM glucose	468:483	NG; 5 mM glucose	468:483	To address this issue, rat CF were cultured in normal glucose (NG; 5 mM glucose) or high-glucose (HG; 25 mM) media for 48 h. Results demonstrate that CF cultured in HG have higher levels (~50%) of overall protein O-GlcNAcylation vs. NG cells.
24553187	5	9	theme	collagen	666:673	arg1	synthesis					675:683	collagen synthesis	666:683	collagen synthesis	666:683	Key regulators of collagen synthesis such as transforming-growth factor-β1 (TGF-β1), SMADs 2/3, and SMAD 7 protein levels, including those of arginase I and II, were altered, leading to increases in collagen levels.
24553187	7	10	theme	NG	1188:1189	arg1	levels					1191:1196	NG levels	1188:1196	NG levels	1188:1196	Expression in CF of an adenovirus coding for the enzyme N-acetylglucosaminidase, which removes O-GlcNAc moieties from proteins, decreased Sp1 and arginase II O-GlcNAcylation and restored HG-induced perturbations in CF back to NG levels.
24553187	5	11	theme	synthesis	675:683	arg1	SMADs					733:737	SMADs 2/3	733:741	SMADs 2/3	733:741	Key regulators of collagen synthesis such as transforming-growth factor-β1 (TGF-β1), SMADs 2/3, and SMAD 7 protein levels, including those of arginase I and II, were altered, leading to increases in collagen levels.
24553187	5	11	theme	synthesis	675:683	arg1	SMAD					748:751	SMAD 7	748:753	SMAD 7	748:753	Key regulators of collagen synthesis such as transforming-growth factor-β1 (TGF-β1), SMADs 2/3, and SMAD 7 protein levels, including those of arginase I and II, were altered, leading to increases in collagen levels.
24553187	5	11	theme	synthesis	675:683	arg1	regulators					652:661	Key regulators	648:661	Key regulators	648:661	Key regulators of collagen synthesis such as transforming-growth factor-β1 (TGF-β1), SMADs 2/3, and SMAD 7 protein levels, including those of arginase I and II, were altered, leading to increases in collagen levels.
24553187	5	11	theme	synthesis	675:683	arg1	those					781:785	those	781:785	those	781:785	Key regulators of collagen synthesis such as transforming-growth factor-β1 (TGF-β1), SMADs 2/3, and SMAD 7 protein levels, including those of arginase I and II, were altered, leading to increases in collagen levels.
24553187	5	11	theme	synthesis	675:683	arg1	factor-β1					713:721	transforming-growth factor-β1	693:721	transforming-growth factor-β1 (TGF-β1)	693:730	Key regulators of collagen synthesis such as transforming-growth factor-β1 (TGF-β1), SMADs 2/3, and SMAD 7 protein levels, including those of arginase I and II, were altered, leading to increases in collagen levels.
24553187	7	12	theme	enzyme	1011:1016	arg1	N-acetylglucosaminidase					1018:1040	the enzyme N-acetylglucosaminidase	1007:1040	the enzyme N-acetylglucosaminidase	1007:1040	Expression in CF of an adenovirus coding for the enzyme N-acetylglucosaminidase, which removes O-GlcNAc moieties from proteins, decreased Sp1 and arginase II O-GlcNAcylation and restored HG-induced perturbations in CF back to NG levels.
24553187	6	13	theme	factor	890:895	arg1	Sp1					897:899	The nuclear transcription factor Sp1	864:899	The nuclear transcription factor Sp1	864:899	The nuclear transcription factor Sp1 and arginase II evidence excess O-GlcNAcylation in HG cells.
24553187	4	14	theme	mM	474:475	arg1	glucose					459:465	normal glucose	452:465	normal glucose (NG; 5 mM glucose)	452:484	To address this issue, rat CF were cultured in normal glucose (NG; 5 mM glucose) or high-glucose (HG; 25 mM) media for 48 h. Results demonstrate that CF cultured in HG have higher levels (~50%) of overall protein O-GlcNAcylation vs. NG cells.
24553187	4	14	theme	mM	474:475	arg1	glucose					477:483	NG; 5 mM glucose	468:483	NG; 5 mM glucose	468:483	To address this issue, rat CF were cultured in normal glucose (NG; 5 mM glucose) or high-glucose (HG; 25 mM) media for 48 h. Results demonstrate that CF cultured in HG have higher levels (~50%) of overall protein O-GlcNAcylation vs. NG cells.
24553187	8	15	theme	diabetes-induced	1288:1303	arg1	fibrosis					1313:1320	diabetes-induced cardiac fibrosis	1288:1320	diabetes-induced cardiac fibrosis	1288:1320	These findings may have important pathophysiological implications for the development of diabetes-induced cardiac fibrosis.
24553187	3	16	theme	enhanced	298:305	arg1	O-GlcNAcylation					315:329	enhanced protein O-GlcNAcylation	298:329	enhanced protein O-GlcNAcylation	298:329	The role that enhanced protein O-GlcNAcylation plays in modulating the phenotype of cardiac fibroblasts (CF) is unknown.
24553187	7	17	theme	arginase	1108:1115	arg1	O-GlcNAcylation					1120:1134	arginase II O-GlcNAcylation	1108:1134	arginase II O-GlcNAcylation	1108:1134	Expression in CF of an adenovirus coding for the enzyme N-acetylglucosaminidase, which removes O-GlcNAc moieties from proteins, decreased Sp1 and arginase II O-GlcNAcylation and restored HG-induced perturbations in CF back to NG levels.
24553187	5	18	theme	transforming-growth	693:711	arg1	factor-β1					713:721	transforming-growth factor-β1	693:721	transforming-growth factor-β1 (TGF-β1)	693:730	Key regulators of collagen synthesis such as transforming-growth factor-β1 (TGF-β1), SMADs 2/3, and SMAD 7 protein levels, including those of arginase I and II, were altered, leading to increases in collagen levels.
24553187	5	18	theme	transforming-growth	693:711	arg1	TGF-β1					724:729	TGF-β1	724:729	TGF-β1	724:729	Key regulators of collagen synthesis such as transforming-growth factor-β1 (TGF-β1), SMADs 2/3, and SMAD 7 protein levels, including those of arginase I and II, were altered, leading to increases in collagen levels.
24553187	1	19	theme	Excess	108:113	arg1	O-GlcNAcylation					139:153	Excess enzyme-mediated protein O-GlcNAcylation	108:153	Excess enzyme-mediated protein O-GlcNAcylation	108:153	Excess enzyme-mediated protein O-GlcNAcylation is known to occur with diabetes mellitus.
24553187	4	20	dep	h.	527:528	arg1	demonstrate					538:548	demonstrate	538:548	demonstrate that CF cultured in HG have higher levels (~50%) of overall protein O-GlcNAcylation vs. NG cells	538:645	To address this issue, rat CF were cultured in normal glucose (NG; 5 mM glucose) or high-glucose (HG; 25 mM) media for 48 h. Results demonstrate that CF cultured in HG have higher levels (~50%) of overall protein O-GlcNAcylation vs. NG cells.
24553187	4	21	theme	protein	610:616	arg1	O-GlcNAcylation					618:632	overall protein O-GlcNAcylation	602:632	overall protein O-GlcNAcylation	602:632	To address this issue, rat CF were cultured in normal glucose (NG; 5 mM glucose) or high-glucose (HG; 25 mM) media for 48 h. Results demonstrate that CF cultured in HG have higher levels (~50%) of overall protein O-GlcNAcylation vs. NG cells.
24553187	6	22	theme	transcription	876:888	arg1	Sp1					897:899	The nuclear transcription factor Sp1	864:899	The nuclear transcription factor Sp1	864:899	The nuclear transcription factor Sp1 and arginase II evidence excess O-GlcNAcylation in HG cells.
24553187	4	23	theme	normal	452:457	arg1	glucose					459:465	normal glucose	452:465	normal glucose (NG; 5 mM glucose)	452:484	To address this issue, rat CF were cultured in normal glucose (NG; 5 mM glucose) or high-glucose (HG; 25 mM) media for 48 h. Results demonstrate that CF cultured in HG have higher levels (~50%) of overall protein O-GlcNAcylation vs. NG cells.
24553187	4	23	theme	normal	452:457	arg1	glucose					477:483	NG; 5 mM glucose	468:483	NG; 5 mM glucose	468:483	To address this issue, rat CF were cultured in normal glucose (NG; 5 mM glucose) or high-glucose (HG; 25 mM) media for 48 h. Results demonstrate that CF cultured in HG have higher levels (~50%) of overall protein O-GlcNAcylation vs. NG cells.
24553187	1	24	theme	enzyme-mediated	115:129	arg1	O-GlcNAcylation					139:153	Excess enzyme-mediated protein O-GlcNAcylation	108:153	Excess enzyme-mediated protein O-GlcNAcylation	108:153	Excess enzyme-mediated protein O-GlcNAcylation is known to occur with diabetes mellitus.
24553187	4	25	theme	overall	602:608	arg1	O-GlcNAcylation					618:632	overall protein O-GlcNAcylation	602:632	overall protein O-GlcNAcylation	602:632	To address this issue, rat CF were cultured in normal glucose (NG; 5 mM glucose) or high-glucose (HG; 25 mM) media for 48 h. Results demonstrate that CF cultured in HG have higher levels (~50%) of overall protein O-GlcNAcylation vs. NG cells.
24553187	0	26	theme	protein	30:36	arg1	O-GlcNAcylation					38:52	high-glucose-induced protein O-GlcNAcylation	9:52	high-glucose-induced protein O-GlcNAcylation	9:52	Role for high-glucose-induced protein O-GlcNAcylation in stimulating cardiac fibroblast collagen synthesis.
24553187	6	27	theme	nuclear	868:874	arg1	Sp1					897:899	The nuclear transcription factor Sp1	864:899	The nuclear transcription factor Sp1	864:899	The nuclear transcription factor Sp1 and arginase II evidence excess O-GlcNAcylation in HG cells.
24553187	1	28	theme	protein	131:137	arg1	O-GlcNAcylation					139:153	Excess enzyme-mediated protein O-GlcNAcylation	108:153	Excess enzyme-mediated protein O-GlcNAcylation	108:153	Excess enzyme-mediated protein O-GlcNAcylation is known to occur with diabetes mellitus.
24553187	7	29	from	perturbations	1160:1172	arg1	CF					1177:1178	CF	1177:1178	CF	1177:1178	Expression in CF of an adenovirus coding for the enzyme N-acetylglucosaminidase, which removes O-GlcNAc moieties from proteins, decreased Sp1 and arginase II O-GlcNAcylation and restored HG-induced perturbations in CF back to NG levels.
24553187	5	30	theme	protein	755:761	arg1	levels					763:768	protein levels	755:768	protein levels	755:768	Key regulators of collagen synthesis such as transforming-growth factor-β1 (TGF-β1), SMADs 2/3, and SMAD 7 protein levels, including those of arginase I and II, were altered, leading to increases in collagen levels.
24553187	0	31	theme	high-glucose-induced	9:28	arg1	O-GlcNAcylation					38:52	high-glucose-induced protein O-GlcNAcylation	9:52	high-glucose-induced protein O-GlcNAcylation	9:52	Role for high-glucose-induced protein O-GlcNAcylation in stimulating cardiac fibroblast collagen synthesis.
24553187	5	32	theme	Key	648:650	arg1	SMADs					733:737	SMADs 2/3	733:741	SMADs 2/3	733:741	Key regulators of collagen synthesis such as transforming-growth factor-β1 (TGF-β1), SMADs 2/3, and SMAD 7 protein levels, including those of arginase I and II, were altered, leading to increases in collagen levels.
24553187	5	32	theme	Key	648:650	arg1	SMAD					748:751	SMAD 7	748:753	SMAD 7	748:753	Key regulators of collagen synthesis such as transforming-growth factor-β1 (TGF-β1), SMADs 2/3, and SMAD 7 protein levels, including those of arginase I and II, were altered, leading to increases in collagen levels.
24553187	5	32	theme	Key	648:650	arg1	regulators					652:661	Key regulators	648:661	Key regulators	648:661	Key regulators of collagen synthesis such as transforming-growth factor-β1 (TGF-β1), SMADs 2/3, and SMAD 7 protein levels, including those of arginase I and II, were altered, leading to increases in collagen levels.
24553187	5	32	theme	Key	648:650	arg1	those					781:785	those	781:785	those	781:785	Key regulators of collagen synthesis such as transforming-growth factor-β1 (TGF-β1), SMADs 2/3, and SMAD 7 protein levels, including those of arginase I and II, were altered, leading to increases in collagen levels.
24553187	5	32	theme	Key	648:650	arg1	factor-β1					713:721	transforming-growth factor-β1	693:721	transforming-growth factor-β1 (TGF-β1)	693:730	Key regulators of collagen synthesis such as transforming-growth factor-β1 (TGF-β1), SMADs 2/3, and SMAD 7 protein levels, including those of arginase I and II, were altered, leading to increases in collagen levels.
24553187	2	33	theme	diabetic	217:224	arg1	cardiomyopathy					226:239	diabetic cardiomyopathy	217:239	diabetic cardiomyopathy	217:239	A characteristic of diabetic cardiomyopathy is the development of myocardial fibrosis.
24553187	7	34	theme	adenovirus	985:994	arg1	Expression					962:971	Expression	962:971	Expression in CF of an adenovirus coding for the enzyme N-acetylglucosaminidase, which removes O-GlcNAc moieties from proteins,	962:1088	Expression in CF of an adenovirus coding for the enzyme N-acetylglucosaminidase, which removes O-GlcNAc moieties from proteins, decreased Sp1 and arginase II O-GlcNAcylation and restored HG-induced perturbations in CF back to NG levels.
24553187	7	35	theme	O-GlcNAc	1057:1064	arg1	moieties					1066:1073	O-GlcNAc moieties	1057:1073	O-GlcNAc moieties	1057:1073	Expression in CF of an adenovirus coding for the enzyme N-acetylglucosaminidase, which removes O-GlcNAc moieties from proteins, decreased Sp1 and arginase II O-GlcNAcylation and restored HG-induced perturbations in CF back to NG levels.
24553187	3	36	theme	protein	307:313	arg1	O-GlcNAcylation					315:329	enhanced protein O-GlcNAcylation	298:329	enhanced protein O-GlcNAcylation	298:329	The role that enhanced protein O-GlcNAcylation plays in modulating the phenotype of cardiac fibroblasts (CF) is unknown.
24553187	6	37	theme	HG	952:953	arg1	cells					955:959	HG cells	952:959	HG cells	952:959	The nuclear transcription factor Sp1 and arginase II evidence excess O-GlcNAcylation in HG cells.
24553187	4	38	theme	mM	510:511	arg1	HG					503:504	HG	503:504	HG; 25 mM	503:511	To address this issue, rat CF were cultured in normal glucose (NG; 5 mM glucose) or high-glucose (HG; 25 mM) media for 48 h. Results demonstrate that CF cultured in HG have higher levels (~50%) of overall protein O-GlcNAcylation vs. NG cells.
24553187	5	39	dep	factor-β1	713:721	arg1	levels					763:768	protein levels	755:768	protein levels	755:768	Key regulators of collagen synthesis such as transforming-growth factor-β1 (TGF-β1), SMADs 2/3, and SMAD 7 protein levels, including those of arginase I and II, were altered, leading to increases in collagen levels.
24553187	2	40	theme	fibrosis	274:281	arg1	characteristic					199:212	A characteristic	197:212	A characteristic of diabetic cardiomyopathy	197:239	A characteristic of diabetic cardiomyopathy is the development of myocardial fibrosis.
24553187	2	40	theme	fibrosis	274:281	arg1	development					248:258	the development	244:258	the development of myocardial fibrosis	244:281	A characteristic of diabetic cardiomyopathy is the development of myocardial fibrosis.
24553187	0	41	theme	cardiac	69:75	arg1	synthesis					97:105	cardiac fibroblast collagen synthesis	69:105	cardiac fibroblast collagen synthesis	69:105	Role for high-glucose-induced protein O-GlcNAcylation in stimulating cardiac fibroblast collagen synthesis.
24553187	4	42	theme	25	507:508	arg1	mM					510:511	mM	510:511	mM	510:511	To address this issue, rat CF were cultured in normal glucose (NG; 5 mM glucose) or high-glucose (HG; 25 mM) media for 48 h. Results demonstrate that CF cultured in HG have higher levels (~50%) of overall protein O-GlcNAcylation vs. NG cells.
24553187	8	43	theme	fibrosis	1313:1320	arg1	development					1273:1283	the development	1269:1283	the development of diabetes-induced cardiac fibrosis	1269:1320	These findings may have important pathophysiological implications for the development of diabetes-induced cardiac fibrosis.
24553187	7	44	theme	HG-induced	1149:1158	arg1	perturbations					1160:1172	HG-induced perturbations	1149:1172	HG-induced perturbations in CF	1149:1178	Expression in CF of an adenovirus coding for the enzyme N-acetylglucosaminidase, which removes O-GlcNAc moieties from proteins, decreased Sp1 and arginase II O-GlcNAcylation and restored HG-induced perturbations in CF back to NG levels.
24553187	2	45	theme	myocardial	263:272	arg1	fibrosis					274:281	myocardial fibrosis	263:281	myocardial fibrosis	263:281	A characteristic of diabetic cardiomyopathy is the development of myocardial fibrosis.
24553187	8	46	theme	cardiac	1305:1311	arg1	fibrosis					1313:1320	diabetes-induced cardiac fibrosis	1288:1320	diabetes-induced cardiac fibrosis	1288:1320	These findings may have important pathophysiological implications for the development of diabetes-induced cardiac fibrosis.
24553187	8	47	theme	important	1223:1231	arg1	implications					1252:1263	important pathophysiological implications	1223:1263	important pathophysiological implications	1223:1263	These findings may have important pathophysiological implications for the development of diabetes-induced cardiac fibrosis.
24553187	8	48	contain	have	1218:1221	arg2	implications					1252:1263	important pathophysiological implications	1223:1263	important pathophysiological implications	1223:1263	These findings may have important pathophysiological implications for the development of diabetes-induced cardiac fibrosis.
24553187	8	48	contain	have	1218:1221	arg1	findings					1205:1212	These findings	1199:1212	These findings	1199:1212	These findings may have important pathophysiological implications for the development of diabetes-induced cardiac fibrosis.
24553187	4	49	contain	have	573:576	arg1	CF					555:556	CF	555:556	CF cultured in HG	555:571	To address this issue, rat CF were cultured in normal glucose (NG; 5 mM glucose) or high-glucose (HG; 25 mM) media for 48 h. Results demonstrate that CF cultured in HG have higher levels (~50%) of overall protein O-GlcNAcylation vs. NG cells.
24553187	4	49	contain	have	573:576	arg2	levels					585:590	higher levels	578:590	higher levels (~50%) of overall protein O-GlcNAcylation vs. NG cells	578:645	To address this issue, rat CF were cultured in normal glucose (NG; 5 mM glucose) or high-glucose (HG; 25 mM) media for 48 h. Results demonstrate that CF cultured in HG have higher levels (~50%) of overall protein O-GlcNAcylation vs. NG cells.
24553187	4	49	contain	have	573:576	arg2	%					596:596	~50%	593:596	~50%	593:596	To address this issue, rat CF were cultured in normal glucose (NG; 5 mM glucose) or high-glucose (HG; 25 mM) media for 48 h. Results demonstrate that CF cultured in HG have higher levels (~50%) of overall protein O-GlcNAcylation vs. NG cells.
24553187	5	50	theme	collagen	847:854	arg1	levels					856:861	collagen levels	847:861	collagen levels	847:861	Key regulators of collagen synthesis such as transforming-growth factor-β1 (TGF-β1), SMADs 2/3, and SMAD 7 protein levels, including those of arginase I and II, were altered, leading to increases in collagen levels.
24553187	4	51	dep	glucose	459:465	arg1	HG					503:504	HG	503:504	HG; 25 mM	503:511	To address this issue, rat CF were cultured in normal glucose (NG; 5 mM glucose) or high-glucose (HG; 25 mM) media for 48 h. Results demonstrate that CF cultured in HG have higher levels (~50%) of overall protein O-GlcNAcylation vs. NG cells.
24553187	4	52	theme	glucose	459:465	arg1	media					514:518	normal glucose (NG; 5 mM glucose) or high-glucose (HG; 25 mM) media	452:518	normal glucose (NG; 5 mM glucose) or high-glucose (HG; 25 mM) media	452:518	To address this issue, rat CF were cultured in normal glucose (NG; 5 mM glucose) or high-glucose (HG; 25 mM) media for 48 h. Results demonstrate that CF cultured in HG have higher levels (~50%) of overall protein O-GlcNAcylation vs. NG cells.
24553187	1	53	theme	diabetes	178:185	arg1	mellitus					187:194	diabetes mellitus	178:194	diabetes mellitus	178:194	Excess enzyme-mediated protein O-GlcNAcylation is known to occur with diabetes mellitus.
24553187	5	54	from	increases	834:842	arg1	levels					856:861	collagen levels	847:861	collagen levels	847:861	Key regulators of collagen synthesis such as transforming-growth factor-β1 (TGF-β1), SMADs 2/3, and SMAD 7 protein levels, including those of arginase I and II, were altered, leading to increases in collagen levels.
24553187	6	55	theme	excess	926:931	arg1	O-GlcNAcylation					933:947	excess O-GlcNAcylation	926:947	excess O-GlcNAcylation	926:947	The nuclear transcription factor Sp1 and arginase II evidence excess O-GlcNAcylation in HG cells.
24553187	0	56	theme	collagen	88:95	arg1	synthesis					97:105	cardiac fibroblast collagen synthesis	69:105	cardiac fibroblast collagen synthesis	69:105	Role for high-glucose-induced protein O-GlcNAcylation in stimulating cardiac fibroblast collagen synthesis.
24553187	2	57	theme	cardiomyopathy	226:239	arg1	characteristic					199:212	A characteristic	197:212	A characteristic of diabetic cardiomyopathy	197:239	A characteristic of diabetic cardiomyopathy is the development of myocardial fibrosis.
24553187	2	57	theme	cardiomyopathy	226:239	arg1	development					248:258	the development	244:258	the development of myocardial fibrosis	244:281	A characteristic of diabetic cardiomyopathy is the development of myocardial fibrosis.
24553187	8	58	theme	pathophysiological	1233:1250	arg1	implications					1252:1263	important pathophysiological implications	1223:1263	important pathophysiological implications	1223:1263	These findings may have important pathophysiological implications for the development of diabetes-induced cardiac fibrosis.
24553187	4	59	theme	higher	578:583	arg1	levels					585:590	higher levels	578:590	higher levels (~50%) of overall protein O-GlcNAcylation vs. NG cells	578:645	To address this issue, rat CF were cultured in normal glucose (NG; 5 mM glucose) or high-glucose (HG; 25 mM) media for 48 h. Results demonstrate that CF cultured in HG have higher levels (~50%) of overall protein O-GlcNAcylation vs. NG cells.
24553187	4	59	theme	higher	578:583	arg1	%					596:596	~50%	593:596	~50%	593:596	To address this issue, rat CF were cultured in normal glucose (NG; 5 mM glucose) or high-glucose (HG; 25 mM) media for 48 h. Results demonstrate that CF cultured in HG have higher levels (~50%) of overall protein O-GlcNAcylation vs. NG cells.
24553187	0	60	theme	fibroblast	77:86	arg1	synthesis					97:105	cardiac fibroblast collagen synthesis	69:105	cardiac fibroblast collagen synthesis	69:105	Role for high-glucose-induced protein O-GlcNAcylation in stimulating cardiac fibroblast collagen synthesis.
24553187	4	61	theme	O-GlcNAcylation	618:632	arg1	cells					641:645	overall protein O-GlcNAcylation vs. NG cells	602:645	overall protein O-GlcNAcylation vs. NG cells	602:645	To address this issue, rat CF were cultured in normal glucose (NG; 5 mM glucose) or high-glucose (HG; 25 mM) media for 48 h. Results demonstrate that CF cultured in HG have higher levels (~50%) of overall protein O-GlcNAcylation vs. NG cells.
16027160	7	0	theme	cell	1168:1171	arg1	cycle					1173:1177	the cell cycle	1164:1177	the cell cycle	1164:1177	These data suggest that dynamic O-GlcNAc processing is a pivotal regulatory component of the cell cycle, controlling cell cycle progression by regulating mitotic phosphorylation, cyclin expression, and cell division.
16027160	1	1	theme	proteins	185:192	arg1	responsive					308:317	responsive	308:317	responsive	308:317	The dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc) is a regulatory post-translational modification that is rapidly responsive to morphogens, hormones, nutrients, and cellular stress.
16027160	1	1	theme	proteins	185:192	arg1	modification					145:156	The dynamic modification	133:156	The dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc)	133:242	The dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc) is a regulatory post-translational modification that is rapidly responsive to morphogens, hormones, nutrients, and cellular stress.
16027160	1	1	theme	proteins	185:192	arg1	modification					279:290	a regulatory post-translational modification	247:290	a regulatory post-translational modification that is rapidly responsive to morphogens, hormones, nutrients, and cellular stress	247:373	The dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc) is a regulatory post-translational modification that is rapidly responsive to morphogens, hormones, nutrients, and cellular stress.
16027160	0	2	theme	mitotic	96:102	arg1	progression					104:114	mitotic progression	96:114	mitotic progression	96:114	Perturbations in O-linked beta-N-acetylglucosamine protein modification cause severe defects in mitotic progression and cytokinesis.
16027160	5	3	with	phenotype	947:955	arg1	cytokinesis					969:979	faulty cytokinesis	962:979	faulty cytokinesis	962:979	Overexpression of the O-GlcNAc transferase, the enzyme that adds O-GlcNAc, results in a polyploid phenotype with faulty cytokinesis.
16027160	3	4	from	delays	538:543	arg1	phosphorylation					582:596	altered mitotic phosphorylation	566:596	altered mitotic phosphorylation	566:596	Increased O-GlcNAc (pharmacologically or genetically) results in growth defects linked to delays in G2/M progression, altered mitotic phosphorylation, and cyclin expression.
16027160	3	4	from	delays	538:543	arg1	expression					610:619	cyclin expression	603:619	cyclin expression	603:619	Increased O-GlcNAc (pharmacologically or genetically) results in growth defects linked to delays in G2/M progression, altered mitotic phosphorylation, and cyclin expression.
16027160	3	4	from	delays	538:543	arg1	progression					553:563	G2/M progression	548:563	G2/M progression	548:563	Increased O-GlcNAc (pharmacologically or genetically) results in growth defects linked to delays in G2/M progression, altered mitotic phosphorylation, and cyclin expression.
16027160	4	5	theme	nuclear	827:833	arg1	organization					835:846	nuclear organization	827:846	nuclear organization	827:846	Overexpression of O-GlcNAcase, the enzyme that removes O-GlcNAc, induces a mitotic exit phenotype accompanied by a delay in mitotic phosphorylation, altered cyclin expression, and pronounced disruption in nuclear organization.
16027160	7	6	theme	cyclin	1254:1259	arg1	expression					1261:1270	cyclin expression	1254:1270	cyclin expression	1254:1270	These data suggest that dynamic O-GlcNAc processing is a pivotal regulatory component of the cell cycle, controlling cell cycle progression by regulating mitotic phosphorylation, cyclin expression, and cell division.
16027160	0	7	from	Perturbations	0:12	arg1	modification					59:70	O-linked beta-N-acetylglucosamine protein modification	17:70	O-linked beta-N-acetylglucosamine protein modification	17:70	Perturbations in O-linked beta-N-acetylglucosamine protein modification cause severe defects in mitotic progression and cytokinesis.
16027160	0	8	link	O-linked	17:24	arg1	modification					59:70	O-linked beta-N-acetylglucosamine protein modification	17:70	O-linked beta-N-acetylglucosamine protein modification	17:70	Perturbations in O-linked beta-N-acetylglucosamine protein modification cause severe defects in mitotic progression and cytokinesis.
16027160	3	9	theme	mitotic	574:580	arg1	phosphorylation					582:596	altered mitotic phosphorylation	566:596	altered mitotic phosphorylation	566:596	Increased O-GlcNAc (pharmacologically or genetically) results in growth defects linked to delays in G2/M progression, altered mitotic phosphorylation, and cyclin expression.
16027160	4	10	theme	mitotic	697:703	arg1	phenotype					710:718	a mitotic exit phenotype	695:718	a mitotic exit phenotype accompanied by a delay in mitotic phosphorylation, altered cyclin expression, and pronounced disruption in nuclear organization	695:846	Overexpression of O-GlcNAcase, the enzyme that removes O-GlcNAc, induces a mitotic exit phenotype accompanied by a delay in mitotic phosphorylation, altered cyclin expression, and pronounced disruption in nuclear organization.
16027160	4	11	theme	O-GlcNAcase	640:650	arg1	Overexpression					622:635	Overexpression	622:635	Overexpression of O-GlcNAcase, the enzyme that removes O-GlcNAc,	622:685	Overexpression of O-GlcNAcase, the enzyme that removes O-GlcNAc, induces a mitotic exit phenotype accompanied by a delay in mitotic phosphorylation, altered cyclin expression, and pronounced disruption in nuclear organization.
16027160	4	12	theme	cyclin	779:784	arg1	expression					786:795	altered cyclin expression	771:795	altered cyclin expression	771:795	Overexpression of O-GlcNAcase, the enzyme that removes O-GlcNAc, induces a mitotic exit phenotype accompanied by a delay in mitotic phosphorylation, altered cyclin expression, and pronounced disruption in nuclear organization.
16027160	5	13	theme	polyploid	937:945	arg1	phenotype					947:955	a polyploid phenotype	935:955	a polyploid phenotype with faulty cytokinesis	935:979	Overexpression of the O-GlcNAc transferase, the enzyme that adds O-GlcNAc, results in a polyploid phenotype with faulty cytokinesis.
16027160	6	14	theme	mitotic	1035:1041	arg1	spindle					1043:1049	the mitotic spindle	1031:1049	the mitotic spindle	1031:1049	Notably, O-GlcNAc transferase is concentrated at the mitotic spindle and midbody at M phase.
16027160	4	15	theme	mitotic	746:752	arg1	phosphorylation					754:768	mitotic phosphorylation	746:768	mitotic phosphorylation	746:768	Overexpression of O-GlcNAcase, the enzyme that removes O-GlcNAc, induces a mitotic exit phenotype accompanied by a delay in mitotic phosphorylation, altered cyclin expression, and pronounced disruption in nuclear organization.
16027160	7	16	theme	regulatory	1140:1149	arg1	component					1151:1159	a pivotal regulatory component	1130:1159	a pivotal regulatory component of the cell cycle	1130:1177	These data suggest that dynamic O-GlcNAc processing is a pivotal regulatory component of the cell cycle, controlling cell cycle progression by regulating mitotic phosphorylation, cyclin expression, and cell division.
16027160	7	16	theme	regulatory	1140:1149	arg1	processing					1116:1125	dynamic O-GlcNAc processing	1099:1125	dynamic O-GlcNAc processing	1099:1125	These data suggest that dynamic O-GlcNAc processing is a pivotal regulatory component of the cell cycle, controlling cell cycle progression by regulating mitotic phosphorylation, cyclin expression, and cell division.
16027160	1	17	theme	O-linked	199:206	arg1	O-GlcNAc					234:241	O-GlcNAc	234:241	O-GlcNAc	234:241	The dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc) is a regulatory post-translational modification that is rapidly responsive to morphogens, hormones, nutrients, and cellular stress.
16027160	1	17	theme	O-linked	199:206	arg1	beta-N-acetylglucosamine					208:231	O-linked beta-N-acetylglucosamine	199:231	O-linked beta-N-acetylglucosamine (O-GlcNAc)	199:242	The dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc) is a regulatory post-translational modification that is rapidly responsive to morphogens, hormones, nutrients, and cellular stress.
16027160	3	18	theme	altered	566:572	arg1	phosphorylation					582:596	altered mitotic phosphorylation	566:596	altered mitotic phosphorylation	566:596	Increased O-GlcNAc (pharmacologically or genetically) results in growth defects linked to delays in G2/M progression, altered mitotic phosphorylation, and cyclin expression.
16027160	1	19	link	O-linked	199:206	arg1	O-GlcNAc					234:241	O-GlcNAc	234:241	O-GlcNAc	234:241	The dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc) is a regulatory post-translational modification that is rapidly responsive to morphogens, hormones, nutrients, and cellular stress.
16027160	1	19	link	O-linked	199:206	arg1	beta-N-acetylglucosamine					208:231	O-linked beta-N-acetylglucosamine	199:231	O-linked beta-N-acetylglucosamine (O-GlcNAc)	199:242	The dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc) is a regulatory post-translational modification that is rapidly responsive to morphogens, hormones, nutrients, and cellular stress.
16027160	4	20	from	expression	786:795	arg1	organization					835:846	nuclear organization	827:846	nuclear organization	827:846	Overexpression of O-GlcNAcase, the enzyme that removes O-GlcNAc, induces a mitotic exit phenotype accompanied by a delay in mitotic phosphorylation, altered cyclin expression, and pronounced disruption in nuclear organization.
16027160	3	21	theme	cyclin	603:608	arg1	expression					610:619	cyclin expression	603:619	cyclin expression	603:619	Increased O-GlcNAc (pharmacologically or genetically) results in growth defects linked to delays in G2/M progression, altered mitotic phosphorylation, and cyclin expression.
16027160	7	22	theme	mitotic	1229:1235	arg1	phosphorylation					1237:1251	mitotic phosphorylation	1229:1251	mitotic phosphorylation	1229:1251	These data suggest that dynamic O-GlcNAc processing is a pivotal regulatory component of the cell cycle, controlling cell cycle progression by regulating mitotic phosphorylation, cyclin expression, and cell division.
16027160	7	23	theme	cycle	1197:1201	arg1	progression					1203:1213	cell cycle progression	1192:1213	cell cycle progression	1192:1213	These data suggest that dynamic O-GlcNAc processing is a pivotal regulatory component of the cell cycle, controlling cell cycle progression by regulating mitotic phosphorylation, cyclin expression, and cell division.
16027160	1	24	with	modification	145:156	arg1	O-GlcNAc					234:241	O-GlcNAc	234:241	O-GlcNAc	234:241	The dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc) is a regulatory post-translational modification that is rapidly responsive to morphogens, hormones, nutrients, and cellular stress.
16027160	1	24	with	modification	145:156	arg1	beta-N-acetylglucosamine					208:231	O-linked beta-N-acetylglucosamine	199:231	O-linked beta-N-acetylglucosamine (O-GlcNAc)	199:242	The dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc) is a regulatory post-translational modification that is rapidly responsive to morphogens, hormones, nutrients, and cellular stress.
16027160	4	25	theme	altered	771:777	arg1	expression					786:795	altered cyclin expression	771:795	altered cyclin expression	771:795	Overexpression of O-GlcNAcase, the enzyme that removes O-GlcNAc, induces a mitotic exit phenotype accompanied by a delay in mitotic phosphorylation, altered cyclin expression, and pronounced disruption in nuclear organization.
16027160	2	26	theme	important	409:417	arg1	O-GlcNAc					394:401	O-GlcNAc	394:401	O-GlcNAc	394:401	Here we show that O-GlcNAc is an important regulator of the cell cycle.
16027160	2	26	theme	important	409:417	arg1	regulator					419:427	an important regulator	406:427	an important regulator of the cell cycle	406:445	Here we show that O-GlcNAc is an important regulator of the cell cycle.
16027160	0	27	theme	beta-N-acetylglucosamine	26:49	arg1	modification					59:70	O-linked beta-N-acetylglucosamine protein modification	17:70	O-linked beta-N-acetylglucosamine protein modification	17:70	Perturbations in O-linked beta-N-acetylglucosamine protein modification cause severe defects in mitotic progression and cytokinesis.
16027160	0	28	theme	O-linked	17:24	arg1	modification					59:70	O-linked beta-N-acetylglucosamine protein modification	17:70	O-linked beta-N-acetylglucosamine protein modification	17:70	Perturbations in O-linked beta-N-acetylglucosamine protein modification cause severe defects in mitotic progression and cytokinesis.
16027160	7	29	theme	cell	1192:1195	arg1	progression					1203:1213	cell cycle progression	1192:1213	cell cycle progression	1192:1213	These data suggest that dynamic O-GlcNAc processing is a pivotal regulatory component of the cell cycle, controlling cell cycle progression by regulating mitotic phosphorylation, cyclin expression, and cell division.
16027160	7	30	theme	dynamic	1099:1105	arg1	component					1151:1159	a pivotal regulatory component	1130:1159	a pivotal regulatory component of the cell cycle	1130:1177	These data suggest that dynamic O-GlcNAc processing is a pivotal regulatory component of the cell cycle, controlling cell cycle progression by regulating mitotic phosphorylation, cyclin expression, and cell division.
16027160	7	30	theme	dynamic	1099:1105	arg1	processing					1116:1125	dynamic O-GlcNAc processing	1099:1125	dynamic O-GlcNAc processing	1099:1125	These data suggest that dynamic O-GlcNAc processing is a pivotal regulatory component of the cell cycle, controlling cell cycle progression by regulating mitotic phosphorylation, cyclin expression, and cell division.
16027160	3	31	dep	O-GlcNAc	458:465	arg1	or					486:487	or	486:487	or	486:487	Increased O-GlcNAc (pharmacologically or genetically) results in growth defects linked to delays in G2/M progression, altered mitotic phosphorylation, and cyclin expression.
16027160	4	32	theme	exit	705:708	arg1	phenotype					710:718	a mitotic exit phenotype	695:718	a mitotic exit phenotype accompanied by a delay in mitotic phosphorylation, altered cyclin expression, and pronounced disruption in nuclear organization	695:846	Overexpression of O-GlcNAcase, the enzyme that removes O-GlcNAc, induces a mitotic exit phenotype accompanied by a delay in mitotic phosphorylation, altered cyclin expression, and pronounced disruption in nuclear organization.
16027160	2	33	theme	cycle	441:445	arg1	O-GlcNAc					394:401	O-GlcNAc	394:401	O-GlcNAc	394:401	Here we show that O-GlcNAc is an important regulator of the cell cycle.
16027160	2	33	theme	cycle	441:445	arg1	regulator					419:427	an important regulator	406:427	an important regulator of the cell cycle	406:445	Here we show that O-GlcNAc is an important regulator of the cell cycle.
16027160	0	34	theme	protein	51:57	arg1	modification					59:70	O-linked beta-N-acetylglucosamine protein modification	17:70	O-linked beta-N-acetylglucosamine protein modification	17:70	Perturbations in O-linked beta-N-acetylglucosamine protein modification cause severe defects in mitotic progression and cytokinesis.
16027160	3	35	theme	Increased	448:456	arg1	O-GlcNAc					458:465	Increased O-GlcNAc	448:465	Increased O-GlcNAc (pharmacologically or genetically)	448:500	Increased O-GlcNAc (pharmacologically or genetically) results in growth defects linked to delays in G2/M progression, altered mitotic phosphorylation, and cyclin expression.
16027160	5	36	theme	O-GlcNAc	871:878	arg1	enzyme					897:902	the enzyme	893:902	the enzyme that adds O-GlcNAc	893:921	Overexpression of the O-GlcNAc transferase, the enzyme that adds O-GlcNAc, results in a polyploid phenotype with faulty cytokinesis.
16027160	5	36	theme	O-GlcNAc	871:878	arg1	transferase					880:890	the O-GlcNAc transferase	867:890	the O-GlcNAc transferase	867:890	Overexpression of the O-GlcNAc transferase, the enzyme that adds O-GlcNAc, results in a polyploid phenotype with faulty cytokinesis.
16027160	1	37	theme	regulatory	249:258	arg1	responsive					308:317	responsive	308:317	responsive	308:317	The dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc) is a regulatory post-translational modification that is rapidly responsive to morphogens, hormones, nutrients, and cellular stress.
16027160	1	37	theme	regulatory	249:258	arg1	modification					279:290	a regulatory post-translational modification	247:290	a regulatory post-translational modification that is rapidly responsive to morphogens, hormones, nutrients, and cellular stress	247:373	The dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc) is a regulatory post-translational modification that is rapidly responsive to morphogens, hormones, nutrients, and cellular stress.
16027160	1	37	theme	regulatory	249:258	arg1	modification					145:156	The dynamic modification	133:156	The dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc)	133:242	The dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc) is a regulatory post-translational modification that is rapidly responsive to morphogens, hormones, nutrients, and cellular stress.
16027160	0	38	theme	severe	78:83	arg1	defects					85:91	severe defects	78:91	severe defects in mitotic progression and cytokinesis	78:130	Perturbations in O-linked beta-N-acetylglucosamine protein modification cause severe defects in mitotic progression and cytokinesis.
16027160	6	39	theme	O-GlcNAc	991:998	arg1	transferase					1000:1010	O-GlcNAc transferase	991:1010	O-GlcNAc transferase	991:1010	Notably, O-GlcNAc transferase is concentrated at the mitotic spindle and midbody at M phase.
16027160	0	40	from	defects	85:91	arg1	cytokinesis					120:130	cytokinesis	120:130	cytokinesis	120:130	Perturbations in O-linked beta-N-acetylglucosamine protein modification cause severe defects in mitotic progression and cytokinesis.
16027160	0	40	from	defects	85:91	arg1	progression					104:114	mitotic progression	96:114	mitotic progression	96:114	Perturbations in O-linked beta-N-acetylglucosamine protein modification cause severe defects in mitotic progression and cytokinesis.
16027160	1	41	theme	dynamic	137:143	arg1	responsive					308:317	responsive	308:317	responsive	308:317	The dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc) is a regulatory post-translational modification that is rapidly responsive to morphogens, hormones, nutrients, and cellular stress.
16027160	1	41	theme	dynamic	137:143	arg1	modification					145:156	The dynamic modification	133:156	The dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc)	133:242	The dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc) is a regulatory post-translational modification that is rapidly responsive to morphogens, hormones, nutrients, and cellular stress.
16027160	1	41	theme	dynamic	137:143	arg1	modification					279:290	a regulatory post-translational modification	247:290	a regulatory post-translational modification that is rapidly responsive to morphogens, hormones, nutrients, and cellular stress	247:373	The dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc) is a regulatory post-translational modification that is rapidly responsive to morphogens, hormones, nutrients, and cellular stress.
16027160	7	42	theme	O-GlcNAc	1107:1114	arg1	component					1151:1159	a pivotal regulatory component	1130:1159	a pivotal regulatory component of the cell cycle	1130:1177	These data suggest that dynamic O-GlcNAc processing is a pivotal regulatory component of the cell cycle, controlling cell cycle progression by regulating mitotic phosphorylation, cyclin expression, and cell division.
16027160	7	42	theme	O-GlcNAc	1107:1114	arg1	processing					1116:1125	dynamic O-GlcNAc processing	1099:1125	dynamic O-GlcNAc processing	1099:1125	These data suggest that dynamic O-GlcNAc processing is a pivotal regulatory component of the cell cycle, controlling cell cycle progression by regulating mitotic phosphorylation, cyclin expression, and cell division.
16027160	1	43	theme	cellular	359:366	arg1	stress					368:373	cellular stress	359:373	cellular stress	359:373	The dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc) is a regulatory post-translational modification that is rapidly responsive to morphogens, hormones, nutrients, and cellular stress.
16027160	7	44	theme	cycle	1173:1177	arg1	component					1151:1159	a pivotal regulatory component	1130:1159	a pivotal regulatory component of the cell cycle	1130:1177	These data suggest that dynamic O-GlcNAc processing is a pivotal regulatory component of the cell cycle, controlling cell cycle progression by regulating mitotic phosphorylation, cyclin expression, and cell division.
16027160	7	44	theme	cycle	1173:1177	arg1	processing					1116:1125	dynamic O-GlcNAc processing	1099:1125	dynamic O-GlcNAc processing	1099:1125	These data suggest that dynamic O-GlcNAc processing is a pivotal regulatory component of the cell cycle, controlling cell cycle progression by regulating mitotic phosphorylation, cyclin expression, and cell division.
16027160	5	45	theme	faulty	962:967	arg1	cytokinesis					969:979	faulty cytokinesis	962:979	faulty cytokinesis	962:979	Overexpression of the O-GlcNAc transferase, the enzyme that adds O-GlcNAc, results in a polyploid phenotype with faulty cytokinesis.
16027160	4	46	from	disruption	813:822	arg1	organization					835:846	nuclear organization	827:846	nuclear organization	827:846	Overexpression of O-GlcNAcase, the enzyme that removes O-GlcNAc, induces a mitotic exit phenotype accompanied by a delay in mitotic phosphorylation, altered cyclin expression, and pronounced disruption in nuclear organization.
16027160	3	47	theme	growth	513:518	arg1	defects					520:526	growth defects	513:526	growth defects linked to delays in G2/M progression, altered mitotic phosphorylation, and cyclin expression	513:619	Increased O-GlcNAc (pharmacologically or genetically) results in growth defects linked to delays in G2/M progression, altered mitotic phosphorylation, and cyclin expression.
16027160	4	48	from	phosphorylation	754:768	arg1	organization					835:846	nuclear organization	827:846	nuclear organization	827:846	Overexpression of O-GlcNAcase, the enzyme that removes O-GlcNAc, induces a mitotic exit phenotype accompanied by a delay in mitotic phosphorylation, altered cyclin expression, and pronounced disruption in nuclear organization.
16027160	1	49	theme	post-translational	260:277	arg1	responsive					308:317	responsive	308:317	responsive	308:317	The dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc) is a regulatory post-translational modification that is rapidly responsive to morphogens, hormones, nutrients, and cellular stress.
16027160	1	49	theme	post-translational	260:277	arg1	modification					279:290	a regulatory post-translational modification	247:290	a regulatory post-translational modification that is rapidly responsive to morphogens, hormones, nutrients, and cellular stress	247:373	The dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc) is a regulatory post-translational modification that is rapidly responsive to morphogens, hormones, nutrients, and cellular stress.
16027160	1	49	theme	post-translational	260:277	arg1	modification					145:156	The dynamic modification	133:156	The dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc)	133:242	The dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc) is a regulatory post-translational modification that is rapidly responsive to morphogens, hormones, nutrients, and cellular stress.
16027160	4	50	theme	pronounced	802:811	arg1	disruption					813:822	pronounced disruption	802:822	pronounced disruption in nuclear organization	802:846	Overexpression of O-GlcNAcase, the enzyme that removes O-GlcNAc, induces a mitotic exit phenotype accompanied by a delay in mitotic phosphorylation, altered cyclin expression, and pronounced disruption in nuclear organization.
16027160	1	51	theme	nuclear	161:167	arg1	proteins					185:192	nuclear and cytoplasmic proteins	161:192	nuclear and cytoplasmic proteins	161:192	The dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc) is a regulatory post-translational modification that is rapidly responsive to morphogens, hormones, nutrients, and cellular stress.
16027160	7	52	theme	pivotal	1132:1138	arg1	component					1151:1159	a pivotal regulatory component	1130:1159	a pivotal regulatory component of the cell cycle	1130:1177	These data suggest that dynamic O-GlcNAc processing is a pivotal regulatory component of the cell cycle, controlling cell cycle progression by regulating mitotic phosphorylation, cyclin expression, and cell division.
16027160	7	52	theme	pivotal	1132:1138	arg1	processing					1116:1125	dynamic O-GlcNAc processing	1099:1125	dynamic O-GlcNAc processing	1099:1125	These data suggest that dynamic O-GlcNAc processing is a pivotal regulatory component of the cell cycle, controlling cell cycle progression by regulating mitotic phosphorylation, cyclin expression, and cell division.
16027160	7	53	theme	cell	1277:1280	arg1	division					1282:1289	cell division	1277:1289	cell division	1277:1289	These data suggest that dynamic O-GlcNAc processing is a pivotal regulatory component of the cell cycle, controlling cell cycle progression by regulating mitotic phosphorylation, cyclin expression, and cell division.
16027160	2	54	theme	cell	436:439	arg1	cycle					441:445	the cell cycle	432:445	the cell cycle	432:445	Here we show that O-GlcNAc is an important regulator of the cell cycle.
16027160	3	55	attach	linked	528:533	arg1	delays					538:543	delays	538:543	delays in G2/M progression, altered mitotic phosphorylation, and cyclin expression	538:619	Increased O-GlcNAc (pharmacologically or genetically) results in growth defects linked to delays in G2/M progression, altered mitotic phosphorylation, and cyclin expression.
16027160	3	55	attach	linked	528:533	arg2	defects					520:526	growth defects	513:526	growth defects linked to delays in G2/M progression, altered mitotic phosphorylation, and cyclin expression	513:619	Increased O-GlcNAc (pharmacologically or genetically) results in growth defects linked to delays in G2/M progression, altered mitotic phosphorylation, and cyclin expression.
16027160	3	56	theme	G2/M	548:551	arg1	progression					553:563	G2/M progression	548:563	G2/M progression	548:563	Increased O-GlcNAc (pharmacologically or genetically) results in growth defects linked to delays in G2/M progression, altered mitotic phosphorylation, and cyclin expression.
16027160	6	57	theme	M	1066:1066	arg1	phase					1068:1072	M phase	1066:1072	M phase	1066:1072	Notably, O-GlcNAc transferase is concentrated at the mitotic spindle and midbody at M phase.
16027160	5	58	theme	transferase	880:890	arg1	Overexpression					849:862	Overexpression	849:862	Overexpression of the O-GlcNAc transferase, the enzyme that adds O-GlcNAc,	849:922	Overexpression of the O-GlcNAc transferase, the enzyme that adds O-GlcNAc, results in a polyploid phenotype with faulty cytokinesis.
16027160	1	59	theme	cytoplasmic	173:183	arg1	proteins					185:192	nuclear and cytoplasmic proteins	161:192	nuclear and cytoplasmic proteins	161:192	The dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine (O-GlcNAc) is a regulatory post-translational modification that is rapidly responsive to morphogens, hormones, nutrients, and cellular stress.
16027160	4	60	from	delay	737:741	arg1	expression					786:795	altered cyclin expression	771:795	altered cyclin expression	771:795	Overexpression of O-GlcNAcase, the enzyme that removes O-GlcNAc, induces a mitotic exit phenotype accompanied by a delay in mitotic phosphorylation, altered cyclin expression, and pronounced disruption in nuclear organization.
16027160	4	60	from	delay	737:741	arg1	disruption					813:822	pronounced disruption	802:822	pronounced disruption in nuclear organization	802:846	Overexpression of O-GlcNAcase, the enzyme that removes O-GlcNAc, induces a mitotic exit phenotype accompanied by a delay in mitotic phosphorylation, altered cyclin expression, and pronounced disruption in nuclear organization.
16027160	4	60	from	delay	737:741	arg1	phosphorylation					754:768	mitotic phosphorylation	746:768	mitotic phosphorylation	746:768	Overexpression of O-GlcNAcase, the enzyme that removes O-GlcNAc, induces a mitotic exit phenotype accompanied by a delay in mitotic phosphorylation, altered cyclin expression, and pronounced disruption in nuclear organization.
30106436	10	0	theme	SW620	1376:1380	arg1	cells					1382:1386	MCF-7, SW480, and SW620 cells	1358:1386	cells	1382:1386	Under anoikis resistance conditions performed by spheroid cultures, siOGT treatment decreased viability only in MCF-7, SW480, and SW620 cells.
30106436	13	1	theme	modification	1751:1762	arg1	level					1764:1768	its O-GlcNAc modification level	1738:1768	its O-GlcNAc modification level	1738:1768	Immunoblots revealed that the Hsp27 protein level was increased but its O-GlcNAc modification level was decreased in siOGT-treated cells.
30106436	2	2	theme	cancer	320:325	arg1	tissues					327:333	primary breast and colorectal cancer tissues	290:333	primary breast and colorectal cancer tissues	290:333	Previously, we reported that the O-GlcNAcylation level was increased in primary breast and colorectal cancer tissues.
30106436	11	3	theme	OGT	1401:1403	arg1	knockdown					1405:1413	OGT knockdown	1401:1413	OGT knockdown in MCF-7 cells	1401:1428	Among them, OGT knockdown in MCF-7 cells revealed a high inhibitory effect on colony and spheroid cultures.
30106436	6	4	theme	cancerous	863:871	arg1	cells					873:877	all cancerous cells	859:877	all cancerous cells	859:877	We found that the levels of O-GlcNAcylation and O-GlcNAc transferase (OGT), an O-GlcNAc catalyzing enzyme, were obviously increased in all cancerous cells, except SK-Hep1, when compared to normal cells.
30106436	6	5	theme	transferase	781:791	arg1	levels					742:747	the levels	738:747	the levels of O-GlcNAcylation and O-GlcNAc transferase (OGT), an O-GlcNAc catalyzing enzyme,	738:829	We found that the levels of O-GlcNAcylation and O-GlcNAc transferase (OGT), an O-GlcNAc catalyzing enzyme, were obviously increased in all cancerous cells, except SK-Hep1, when compared to normal cells.
30106436	1	6	theme	proteins	208:215	arg1	modification					178:189	a dynamic posttranslational modification	150:189	a dynamic posttranslational modification of nucleoplasmic proteins	150:215	O-GlcNAcylation is a dynamic posttranslational modification of nucleoplasmic proteins.
30106436	1	6	theme	proteins	208:215	arg1	O-GlcNAcylation					131:145	O-GlcNAcylation	131:145	O-GlcNAcylation	131:145	O-GlcNAcylation is a dynamic posttranslational modification of nucleoplasmic proteins.
30106436	15	7	theme	double	1897:1902	arg1	knockdown					1904:1912	double knockdown	1897:1912	double knockdown of OGT and Hsp27	1897:1929	Notably, double knockdown of OGT and Hsp27 showed a reversal in the inhibitory effect on colony and spheroid cultures.
30106436	16	8	theme	MCF-7	2136:2140	arg1	cells					2142:2146	MCF-7 cells	2136:2146	MCF-7 cells	2136:2146	Collectively, these results indicate that O-GlcNAcylation is required for anoikis resistance and anchorage-independent growth of MCF-7 cells.
30106436	4	9	from	roles	483:487	arg1	transformation					525:538	the malignant transformation	511:538	the malignant transformation of cancer cell lines	511:559	The aim of the present study was to investigate the roles of O-GlcNAcylation in the malignant transformation of cancer cell lines.
30106436	14	10	theme	cell	1867:1870	arg1	transformation					1872:1885	MCF-7 cell transformation	1861:1885	MCF-7 cell transformation	1861:1885	These changes were associated with the inhibition of MCF-7 cell transformation.
30106436	13	11	theme	Hsp27	1700:1704	arg1	level					1714:1718	the Hsp27 protein level	1696:1718	the Hsp27 protein level	1696:1718	Immunoblots revealed that the Hsp27 protein level was increased but its O-GlcNAc modification level was decreased in siOGT-treated cells.
30106436	9	12	theme	cells	1223:1227	arg1	cultures					1200:1207	soft agar cultures	1190:1207	soft agar cultures of all cancer cells	1190:1227	However, it inhibited anchorage-independent growth in soft agar cultures of all cancer cells, except SK-Hep1.
30106436	12	13	theme	heat	1572:1575	arg1	protein					1642:1648	the highest upregulated protein	1618:1648	the highest upregulated protein upon OGT knockdown	1618:1667	Using two-dimensional gel electrophoresis and mass spectrometric analysis, heat shock protein 27 (Hsp27) was found to be the highest upregulated protein upon OGT knockdown.
30106436	12	13	theme	heat	1572:1575	arg1	protein					1583:1589	heat shock protein 27	1572:1592	heat shock protein 27 (Hsp27)	1572:1600	Using two-dimensional gel electrophoresis and mass spectrometric analysis, heat shock protein 27 (Hsp27) was found to be the highest upregulated protein upon OGT knockdown.
30106436	12	13	theme	heat	1572:1575	arg1	Hsp27					1595:1599	Hsp27	1595:1599	Hsp27	1595:1599	Using two-dimensional gel electrophoresis and mass spectrometric analysis, heat shock protein 27 (Hsp27) was found to be the highest upregulated protein upon OGT knockdown.
30106436	4	14	theme	present	446:452	arg1	study					454:458	the present study	442:458	the present study	442:458	The aim of the present study was to investigate the roles of O-GlcNAcylation in the malignant transformation of cancer cell lines.
30106436	2	15	theme	primary	290:296	arg1	breast					298:303	primary breast	290:303	primary breast	290:303	Previously, we reported that the O-GlcNAcylation level was increased in primary breast and colorectal cancer tissues.
30106436	12	16	theme	electrophoresis	1523:1537	arg1	analysis					1562:1569	two-dimensional gel electrophoresis and mass spectrometric analysis	1503:1569	two-dimensional gel electrophoresis and mass spectrometric analysis	1503:1569	Using two-dimensional gel electrophoresis and mass spectrometric analysis, heat shock protein 27 (Hsp27) was found to be the highest upregulated protein upon OGT knockdown.
30106436	9	17	from	growth	1180:1185	arg1	cultures					1200:1207	soft agar cultures	1190:1207	soft agar cultures of all cancer cells	1190:1227	However, it inhibited anchorage-independent growth in soft agar cultures of all cancer cells, except SK-Hep1.
30106436	11	18	theme	inhibitory	1446:1455	arg1	effect					1457:1462	a high inhibitory effect	1439:1462	a high inhibitory effect on colony and spheroid cultures	1439:1494	Among them, OGT knockdown in MCF-7 cells revealed a high inhibitory effect on colony and spheroid cultures.
30106436	0	19	theme	cells	73:77	arg1	transformation					49:62	the malignant transformation	35:62	the malignant transformation of MCF-7 cells	35:77	Decreasing O-GlcNAcylation affects the malignant transformation of MCF-7 cells via Hsp27 expression and its O-GlcNAc modification.
30106436	5	20	theme	O-GlcNAcylation	562:576	arg1	level					578:582	O-GlcNAcylation level	562:582	O-GlcNAcylation level	562:582	O-GlcNAcylation level was examined in six cancer cell lines including breast (MCF-7 and MDA-MB-231), colorectal (SW480 and SW620), and liver (SK-Hep1 and HepG2).
30106436	1	21	theme	posttranslational	160:176	arg1	modification					178:189	a dynamic posttranslational modification	150:189	a dynamic posttranslational modification of nucleoplasmic proteins	150:215	O-GlcNAcylation is a dynamic posttranslational modification of nucleoplasmic proteins.
30106436	1	21	theme	posttranslational	160:176	arg1	O-GlcNAcylation					131:145	O-GlcNAcylation	131:145	O-GlcNAcylation	131:145	O-GlcNAcylation is a dynamic posttranslational modification of nucleoplasmic proteins.
30106436	12	22	theme	mass	1543:1546	arg1	spectrometric					1548:1560	mass spectrometric	1543:1560	mass spectrometric	1543:1560	Using two-dimensional gel electrophoresis and mass spectrometric analysis, heat shock protein 27 (Hsp27) was found to be the highest upregulated protein upon OGT knockdown.
30106436	3	23	theme	precise	349:355	arg1	roles					357:361	its precise roles	345:361	its precise roles in cancer development and progression	345:399	However, its precise roles in cancer development and progression are still largely unexplored.
30106436	0	24	theme	Hsp27	83:87	arg1	expression					89:98	Hsp27 expression	83:98	Hsp27 expression	83:98	Decreasing O-GlcNAcylation affects the malignant transformation of MCF-7 cells via Hsp27 expression and its O-GlcNAc modification.
30106436	7	25	theme	Reducing	927:934	arg1	O-GlcNAcylation					936:950	Reducing O-GlcNAcylation	927:950	Reducing O-GlcNAcylation using RNA interference against OGT	927:985	Reducing O-GlcNAcylation using RNA interference against OGT showed a marked reduction in OGT and O-GlcNAcylation levels.
30106436	4	26	theme	cancer	543:548	arg1	lines					555:559	cancer cell lines	543:559	cancer cell lines	543:559	The aim of the present study was to investigate the roles of O-GlcNAcylation in the malignant transformation of cancer cell lines.
30106436	15	27	theme	Hsp27	1925:1929	arg1	knockdown					1904:1912	double knockdown	1897:1912	double knockdown of OGT and Hsp27	1897:1929	Notably, double knockdown of OGT and Hsp27 showed a reversal in the inhibitory effect on colony and spheroid cultures.
30106436	10	28	theme	spheroid	1295:1302	arg1	cultures					1304:1311	spheroid cultures	1295:1311	spheroid cultures	1295:1311	Under anoikis resistance conditions performed by spheroid cultures, siOGT treatment decreased viability only in MCF-7, SW480, and SW620 cells.
30106436	12	29	theme	two-dimensional	1503:1517	arg1	electrophoresis					1523:1537	two-dimensional gel electrophoresis	1503:1537	two-dimensional gel electrophoresis	1503:1537	Using two-dimensional gel electrophoresis and mass spectrometric analysis, heat shock protein 27 (Hsp27) was found to be the highest upregulated protein upon OGT knockdown.
30106436	4	30	theme	O-GlcNAcylation	492:506	arg1	roles					483:487	the roles	479:487	the roles of O-GlcNAcylation in the malignant transformation of cancer cell lines	479:559	The aim of the present study was to investigate the roles of O-GlcNAcylation in the malignant transformation of cancer cell lines.
30106436	15	31	theme	OGT	1917:1919	arg1	knockdown					1904:1912	double knockdown	1897:1912	double knockdown of OGT and Hsp27	1897:1929	Notably, double knockdown of OGT and Hsp27 showed a reversal in the inhibitory effect on colony and spheroid cultures.
30106436	0	32	theme	O-GlcNAc	108:115	arg1	modification					117:128	its O-GlcNAc modification	104:128	its O-GlcNAc modification	104:128	Decreasing O-GlcNAcylation affects the malignant transformation of MCF-7 cells via Hsp27 expression and its O-GlcNAc modification.
30106436	5	33	theme	cancer	604:609	arg1	lines					616:620	six cancer cell lines	600:620	six cancer cell lines including breast (MCF-7 and MDA-MB-231), colorectal (SW480 and SW620), and liver (SK-Hep1 and HepG2)	600:721	O-GlcNAcylation level was examined in six cancer cell lines including breast (MCF-7 and MDA-MB-231), colorectal (SW480 and SW620), and liver (SK-Hep1 and HepG2).
30106436	5	33	theme	cancer	604:609	arg1	colorectal					663:672	colorectal	663:672	colorectal	663:672	O-GlcNAcylation level was examined in six cancer cell lines including breast (MCF-7 and MDA-MB-231), colorectal (SW480 and SW620), and liver (SK-Hep1 and HepG2).
30106436	5	33	theme	cancer	604:609	arg1	liver					697:701	liver	697:701	liver (SK-Hep1 and HepG2)	697:721	O-GlcNAcylation level was examined in six cancer cell lines including breast (MCF-7 and MDA-MB-231), colorectal (SW480 and SW620), and liver (SK-Hep1 and HepG2).
30106436	5	33	theme	cancer	604:609	arg1	breast					632:637	breast	632:637	breast (MCF-7 and MDA-MB-231)	632:660	O-GlcNAcylation level was examined in six cancer cell lines including breast (MCF-7 and MDA-MB-231), colorectal (SW480 and SW620), and liver (SK-Hep1 and HepG2).
30106436	12	34	theme	upregulated	1630:1640	arg1	protein					1642:1648	the highest upregulated protein	1618:1648	the highest upregulated protein upon OGT knockdown	1618:1667	Using two-dimensional gel electrophoresis and mass spectrometric analysis, heat shock protein 27 (Hsp27) was found to be the highest upregulated protein upon OGT knockdown.
30106436	12	34	theme	upregulated	1630:1640	arg1	protein					1583:1589	heat shock protein 27	1572:1592	heat shock protein 27 (Hsp27)	1572:1600	Using two-dimensional gel electrophoresis and mass spectrometric analysis, heat shock protein 27 (Hsp27) was found to be the highest upregulated protein upon OGT knockdown.
30106436	16	35	theme	anchorage-independent	2104:2124	arg1	growth					2126:2131	anchorage-independent growth	2104:2131	anchorage-independent growth	2104:2131	Collectively, these results indicate that O-GlcNAcylation is required for anoikis resistance and anchorage-independent growth of MCF-7 cells.
30106436	10	36	theme	anoikis	1252:1258	arg1	conditions					1271:1280	anoikis resistance conditions	1252:1280	anoikis resistance conditions performed by spheroid cultures	1252:1311	Under anoikis resistance conditions performed by spheroid cultures, siOGT treatment decreased viability only in MCF-7, SW480, and SW620 cells.
30106436	0	37	theme	Decreasing	0:9	arg1	O-GlcNAcylation					11:25	Decreasing O-GlcNAcylation	0:25	Decreasing O-GlcNAcylation	0:25	Decreasing O-GlcNAcylation affects the malignant transformation of MCF-7 cells via Hsp27 expression and its O-GlcNAc modification.
30106436	17	38	theme	Hsp27	2212:2216	arg1	expression					2226:2235	Hsp27 protein expression	2212:2235	Hsp27 protein expression	2212:2235	Blocking this glycosylation by OGT knockdown may regulate both Hsp27 protein expression and its O-GlcNAc modification levels.
30106436	18	39	theme	malignant	2315:2323	arg1	transformation					2325:2338	malignant transformation	2315:2338	malignant transformation	2315:2338	This alteration may play vital roles in malignant transformation.
30106436	0	40	theme	malignant	39:47	arg1	transformation					49:62	the malignant transformation	35:62	the malignant transformation of MCF-7 cells	35:77	Decreasing O-GlcNAcylation affects the malignant transformation of MCF-7 cells via Hsp27 expression and its O-GlcNAc modification.
30106436	4	41	theme	lines	555:559	arg1	transformation					525:538	the malignant transformation	511:538	the malignant transformation of cancer cell lines	511:559	The aim of the present study was to investigate the roles of O-GlcNAcylation in the malignant transformation of cancer cell lines.
30106436	15	42	theme	inhibitory	1956:1965	arg1	effect					1967:1972	the inhibitory effect	1952:1972	the inhibitory effect on colony and spheroid cultures	1952:2004	Notably, double knockdown of OGT and Hsp27 showed a reversal in the inhibitory effect on colony and spheroid cultures.
30106436	15	43	from	cultures	1997:2004	arg1	reversal					1940:1947	a reversal	1938:1947	a reversal in the inhibitory effect on colony and spheroid cultures	1938:2004	Notably, double knockdown of OGT and Hsp27 showed a reversal in the inhibitory effect on colony and spheroid cultures.
30106436	9	44	theme	soft	1190:1193	arg1	cultures					1200:1207	soft agar cultures	1190:1207	soft agar cultures of all cancer cells	1190:1227	However, it inhibited anchorage-independent growth in soft agar cultures of all cancer cells, except SK-Hep1.
30106436	10	45	theme	siOGT	1314:1318	arg1	treatment					1320:1328	siOGT treatment	1314:1328	siOGT treatment	1314:1328	Under anoikis resistance conditions performed by spheroid cultures, siOGT treatment decreased viability only in MCF-7, SW480, and SW620 cells.
30106436	8	46	theme	cell	1085:1088	arg1	growth					1090:1095	cell growth	1085:1095	cell growth under conventional monolayer cultures	1085:1133	Surprisingly, siOGT had no effect on cell growth under conventional monolayer cultures.
30106436	5	47	dep	breast	632:637	arg1	MDA-MB-231					650:659	MDA-MB-231	650:659	MDA-MB-231	650:659	O-GlcNAcylation level was examined in six cancer cell lines including breast (MCF-7 and MDA-MB-231), colorectal (SW480 and SW620), and liver (SK-Hep1 and HepG2).
30106436	5	47	dep	breast	632:637	arg1	MCF-7					640:644	MCF-7	640:644	MCF-7	640:644	O-GlcNAcylation level was examined in six cancer cell lines including breast (MCF-7 and MDA-MB-231), colorectal (SW480 and SW620), and liver (SK-Hep1 and HepG2).
30106436	10	48	theme	MCF-7	1358:1362	arg1	SW480					1365:1369	MCF-7, SW480, and SW620 cells	1358:1386	SW480	1365:1369	Under anoikis resistance conditions performed by spheroid cultures, siOGT treatment decreased viability only in MCF-7, SW480, and SW620 cells.
30106436	8	49	contain	had	1068:1070	arg1	siOGT					1062:1066	siOGT	1062:1066	siOGT	1062:1066	Surprisingly, siOGT had no effect on cell growth under conventional monolayer cultures.
30106436	8	49	contain	had	1068:1070	arg2	effect					1075:1080	no effect	1072:1080	no effect	1072:1080	Surprisingly, siOGT had no effect on cell growth under conventional monolayer cultures.
30106436	13	50	theme	siOGT-treated	1787:1799	arg1	cells					1801:1805	siOGT-treated cells	1787:1805	siOGT-treated cells	1787:1805	Immunoblots revealed that the Hsp27 protein level was increased but its O-GlcNAc modification level was decreased in siOGT-treated cells.
30106436	8	51	theme	monolayer	1116:1124	arg1	cultures					1126:1133	conventional monolayer cultures	1103:1133	conventional monolayer cultures	1103:1133	Surprisingly, siOGT had no effect on cell growth under conventional monolayer cultures.
30106436	13	52	theme	O-GlcNAc	1742:1749	arg1	level					1764:1768	its O-GlcNAc modification level	1738:1768	its O-GlcNAc modification level	1738:1768	Immunoblots revealed that the Hsp27 protein level was increased but its O-GlcNAc modification level was decreased in siOGT-treated cells.
30106436	9	53	theme	agar	1195:1198	arg1	cultures					1200:1207	soft agar cultures	1190:1207	soft agar cultures of all cancer cells	1190:1227	However, it inhibited anchorage-independent growth in soft agar cultures of all cancer cells, except SK-Hep1.
30106436	9	54	theme	anchorage-independent	1158:1178	arg1	growth					1180:1185	anchorage-independent growth	1158:1185	anchorage-independent growth in soft agar cultures of all cancer cells	1158:1227	However, it inhibited anchorage-independent growth in soft agar cultures of all cancer cells, except SK-Hep1.
30106436	2	55	theme	colorectal	309:318	arg1	cancer					320:325	colorectal cancer	309:325	colorectal cancer	309:325	Previously, we reported that the O-GlcNAcylation level was increased in primary breast and colorectal cancer tissues.
30106436	1	56	theme	nucleoplasmic	194:206	arg1	proteins					208:215	nucleoplasmic proteins	194:215	nucleoplasmic proteins	194:215	O-GlcNAcylation is a dynamic posttranslational modification of nucleoplasmic proteins.
30106436	6	57	theme	O-GlcNAc	772:779	arg1	OGT					794:796	OGT	794:796	OGT	794:796	We found that the levels of O-GlcNAcylation and O-GlcNAc transferase (OGT), an O-GlcNAc catalyzing enzyme, were obviously increased in all cancerous cells, except SK-Hep1, when compared to normal cells.
30106436	6	57	theme	O-GlcNAc	772:779	arg1	transferase					781:791	O-GlcNAc transferase	772:791	O-GlcNAc transferase (OGT)	772:797	We found that the levels of O-GlcNAcylation and O-GlcNAc transferase (OGT), an O-GlcNAc catalyzing enzyme, were obviously increased in all cancerous cells, except SK-Hep1, when compared to normal cells.
30106436	16	58	theme	cells	2142:2146	arg1	resistance					2089:2098	anoikis resistance	2081:2098	anoikis resistance	2081:2098	Collectively, these results indicate that O-GlcNAcylation is required for anoikis resistance and anchorage-independent growth of MCF-7 cells.
30106436	16	58	theme	cells	2142:2146	arg1	growth					2126:2131	anchorage-independent growth	2104:2131	anchorage-independent growth	2104:2131	Collectively, these results indicate that O-GlcNAcylation is required for anoikis resistance and anchorage-independent growth of MCF-7 cells.
30106436	6	59	theme	O-GlcNAcylation	752:766	arg1	levels					742:747	the levels	738:747	the levels of O-GlcNAcylation and O-GlcNAc transferase (OGT), an O-GlcNAc catalyzing enzyme,	738:829	We found that the levels of O-GlcNAcylation and O-GlcNAc transferase (OGT), an O-GlcNAc catalyzing enzyme, were obviously increased in all cancerous cells, except SK-Hep1, when compared to normal cells.
30106436	14	60	theme	transformation	1872:1885	arg1	inhibition					1847:1856	the inhibition	1843:1856	the inhibition of MCF-7 cell transformation	1843:1885	These changes were associated with the inhibition of MCF-7 cell transformation.
30106436	17	61	dep	expression	2226:2235	arg1	levels					2267:2272	levels	2267:2272	levels	2267:2272	Blocking this glycosylation by OGT knockdown may regulate both Hsp27 protein expression and its O-GlcNAc modification levels.
30106436	7	62	theme	O-GlcNAcylation	1024:1038	arg1	levels					1040:1045	OGT and O-GlcNAcylation levels	1016:1045	OGT and O-GlcNAcylation levels	1016:1045	Reducing O-GlcNAcylation using RNA interference against OGT showed a marked reduction in OGT and O-GlcNAcylation levels.
30106436	9	63	theme	cancer	1216:1221	arg1	cells					1223:1227	all cancer cells	1212:1227	all cancer cells	1212:1227	However, it inhibited anchorage-independent growth in soft agar cultures of all cancer cells, except SK-Hep1.
30106436	14	64	theme	MCF-7	1861:1865	arg1	transformation					1872:1885	MCF-7 cell transformation	1861:1885	MCF-7 cell transformation	1861:1885	These changes were associated with the inhibition of MCF-7 cell transformation.
30106436	6	65	theme	normal	913:918	arg1	cells					920:924	normal cells	913:924	normal cells	913:924	We found that the levels of O-GlcNAcylation and O-GlcNAc transferase (OGT), an O-GlcNAc catalyzing enzyme, were obviously increased in all cancerous cells, except SK-Hep1, when compared to normal cells.
30106436	13	66	theme	protein	1706:1712	arg1	level					1714:1718	the Hsp27 protein level	1696:1718	the Hsp27 protein level	1696:1718	Immunoblots revealed that the Hsp27 protein level was increased but its O-GlcNAc modification level was decreased in siOGT-treated cells.
30106436	7	67	theme	OGT	1016:1018	arg1	levels					1040:1045	OGT and O-GlcNAcylation levels	1016:1045	OGT and O-GlcNAcylation levels	1016:1045	Reducing O-GlcNAcylation using RNA interference against OGT showed a marked reduction in OGT and O-GlcNAcylation levels.
30106436	2	68	theme	O-GlcNAcylation	251:265	arg1	level					267:271	the O-GlcNAcylation level	247:271	the O-GlcNAcylation level	247:271	Previously, we reported that the O-GlcNAcylation level was increased in primary breast and colorectal cancer tissues.
30106436	7	69	theme	marked	996:1001	arg1	reduction					1003:1011	a marked reduction	994:1011	a marked reduction in OGT and O-GlcNAcylation levels	994:1045	Reducing O-GlcNAcylation using RNA interference against OGT showed a marked reduction in OGT and O-GlcNAcylation levels.
30106436	17	70	theme	O-GlcNAc	2245:2252	arg1	modification					2254:2265	its O-GlcNAc modification	2241:2265	its O-GlcNAc modification	2241:2265	Blocking this glycosylation by OGT knockdown may regulate both Hsp27 protein expression and its O-GlcNAc modification levels.
30106436	12	71	theme	shock	1577:1581	arg1	protein					1642:1648	the highest upregulated protein	1618:1648	the highest upregulated protein upon OGT knockdown	1618:1667	Using two-dimensional gel electrophoresis and mass spectrometric analysis, heat shock protein 27 (Hsp27) was found to be the highest upregulated protein upon OGT knockdown.
30106436	12	71	theme	shock	1577:1581	arg1	protein					1583:1589	heat shock protein 27	1572:1592	heat shock protein 27 (Hsp27)	1572:1600	Using two-dimensional gel electrophoresis and mass spectrometric analysis, heat shock protein 27 (Hsp27) was found to be the highest upregulated protein upon OGT knockdown.
30106436	12	71	theme	shock	1577:1581	arg1	Hsp27					1595:1599	Hsp27	1595:1599	Hsp27	1595:1599	Using two-dimensional gel electrophoresis and mass spectrometric analysis, heat shock protein 27 (Hsp27) was found to be the highest upregulated protein upon OGT knockdown.
30106436	4	72	theme	study	454:458	arg1	aim					435:437	The aim	431:437	The aim of the present study	431:458	The aim of the present study was to investigate the roles of O-GlcNAcylation in the malignant transformation of cancer cell lines.
30106436	15	73	from	reversal	1940:1947	arg1	cultures					1997:2004	colony and spheroid cultures	1977:2004	colony and spheroid cultures	1977:2004	Notably, double knockdown of OGT and Hsp27 showed a reversal in the inhibitory effect on colony and spheroid cultures.
30106436	15	73	from	reversal	1940:1947	arg1	effect					1967:1972	the inhibitory effect	1952:1972	the inhibitory effect on colony and spheroid cultures	1952:2004	Notably, double knockdown of OGT and Hsp27 showed a reversal in the inhibitory effect on colony and spheroid cultures.
30106436	3	74	from	roles	357:361	arg1	progression					389:399	progression	389:399	progression	389:399	However, its precise roles in cancer development and progression are still largely unexplored.
30106436	3	74	from	roles	357:361	arg1	development					373:383	cancer development	366:383	cancer development	366:383	However, its precise roles in cancer development and progression are still largely unexplored.
30106436	2	75	theme	breast	298:303	arg1	tissues					327:333	primary breast and colorectal cancer tissues	290:333	primary breast and colorectal cancer tissues	290:333	Previously, we reported that the O-GlcNAcylation level was increased in primary breast and colorectal cancer tissues.
30106436	11	76	theme	high	1441:1444	arg1	effect					1457:1462	a high inhibitory effect	1439:1462	a high inhibitory effect on colony and spheroid cultures	1439:1494	Among them, OGT knockdown in MCF-7 cells revealed a high inhibitory effect on colony and spheroid cultures.
30106436	1	77	theme	dynamic	152:158	arg1	modification					178:189	a dynamic posttranslational modification	150:189	a dynamic posttranslational modification of nucleoplasmic proteins	150:215	O-GlcNAcylation is a dynamic posttranslational modification of nucleoplasmic proteins.
30106436	1	77	theme	dynamic	152:158	arg1	O-GlcNAcylation					131:145	O-GlcNAcylation	131:145	O-GlcNAcylation	131:145	O-GlcNAcylation is a dynamic posttranslational modification of nucleoplasmic proteins.
30106436	12	78	theme	spectrometric	1548:1560	arg1	analysis					1562:1569	two-dimensional gel electrophoresis and mass spectrometric analysis	1503:1569	two-dimensional gel electrophoresis and mass spectrometric analysis	1503:1569	Using two-dimensional gel electrophoresis and mass spectrometric analysis, heat shock protein 27 (Hsp27) was found to be the highest upregulated protein upon OGT knockdown.
30106436	3	79	theme	cancer	366:371	arg1	development					373:383	cancer development	366:383	cancer development	366:383	However, its precise roles in cancer development and progression are still largely unexplored.
30106436	11	80	theme	spheroid	1478:1485	arg1	cultures					1487:1494	colony and spheroid cultures	1467:1494	colony and spheroid cultures	1467:1494	Among them, OGT knockdown in MCF-7 cells revealed a high inhibitory effect on colony and spheroid cultures.
30106436	15	81	from	effect	1967:1972	arg1	cultures					1997:2004	colony and spheroid cultures	1977:2004	colony and spheroid cultures	1977:2004	Notably, double knockdown of OGT and Hsp27 showed a reversal in the inhibitory effect on colony and spheroid cultures.
30106436	7	82	theme	RNA	958:960	arg1	interference					962:973	RNA interference	958:973	RNA interference	958:973	Reducing O-GlcNAcylation using RNA interference against OGT showed a marked reduction in OGT and O-GlcNAcylation levels.
30106436	4	83	theme	cell	550:553	arg1	lines					555:559	cancer cell lines	543:559	cancer cell lines	543:559	The aim of the present study was to investigate the roles of O-GlcNAcylation in the malignant transformation of cancer cell lines.
30106436	11	84	theme	colony	1467:1472	arg1	cultures					1487:1494	colony and spheroid cultures	1467:1494	colony and spheroid cultures	1467:1494	Among them, OGT knockdown in MCF-7 cells revealed a high inhibitory effect on colony and spheroid cultures.
30106436	12	85	theme	OGT	1655:1657	arg1	knockdown					1659:1667	OGT knockdown	1655:1667	OGT knockdown	1655:1667	Using two-dimensional gel electrophoresis and mass spectrometric analysis, heat shock protein 27 (Hsp27) was found to be the highest upregulated protein upon OGT knockdown.
30106436	12	86	theme	gel	1519:1521	arg1	electrophoresis					1523:1537	two-dimensional gel electrophoresis	1503:1537	two-dimensional gel electrophoresis	1503:1537	Using two-dimensional gel electrophoresis and mass spectrometric analysis, heat shock protein 27 (Hsp27) was found to be the highest upregulated protein upon OGT knockdown.
30106436	5	87	dep	liver	697:701	arg1	SK-Hep1					704:710	SK-Hep1	704:710	SK-Hep1	704:710	O-GlcNAcylation level was examined in six cancer cell lines including breast (MCF-7 and MDA-MB-231), colorectal (SW480 and SW620), and liver (SK-Hep1 and HepG2).
30106436	5	87	dep	liver	697:701	arg1	HepG2					716:720	HepG2	716:720	HepG2	716:720	O-GlcNAcylation level was examined in six cancer cell lines including breast (MCF-7 and MDA-MB-231), colorectal (SW480 and SW620), and liver (SK-Hep1 and HepG2).
30106436	17	88	theme	OGT	2180:2182	arg1	knockdown					2184:2192	OGT knockdown	2180:2192	OGT knockdown	2180:2192	Blocking this glycosylation by OGT knockdown may regulate both Hsp27 protein expression and its O-GlcNAc modification levels.
30106436	18	89	theme	vital	2300:2304	arg1	roles					2306:2310	vital roles	2300:2310	vital roles	2300:2310	This alteration may play vital roles in malignant transformation.
30106436	4	90	theme	malignant	515:523	arg1	transformation					525:538	the malignant transformation	511:538	the malignant transformation of cancer cell lines	511:559	The aim of the present study was to investigate the roles of O-GlcNAcylation in the malignant transformation of cancer cell lines.
30106436	16	91	theme	anoikis	2081:2087	arg1	resistance					2089:2098	anoikis resistance	2081:2098	anoikis resistance	2081:2098	Collectively, these results indicate that O-GlcNAcylation is required for anoikis resistance and anchorage-independent growth of MCF-7 cells.
30106436	10	92	theme	resistance	1260:1269	arg1	conditions					1271:1280	anoikis resistance conditions	1252:1280	anoikis resistance conditions performed by spheroid cultures	1252:1311	Under anoikis resistance conditions performed by spheroid cultures, siOGT treatment decreased viability only in MCF-7, SW480, and SW620 cells.
30106436	5	93	theme	cell	611:614	arg1	lines					616:620	six cancer cell lines	600:620	six cancer cell lines including breast (MCF-7 and MDA-MB-231), colorectal (SW480 and SW620), and liver (SK-Hep1 and HepG2)	600:721	O-GlcNAcylation level was examined in six cancer cell lines including breast (MCF-7 and MDA-MB-231), colorectal (SW480 and SW620), and liver (SK-Hep1 and HepG2).
30106436	5	93	theme	cell	611:614	arg1	colorectal					663:672	colorectal	663:672	colorectal	663:672	O-GlcNAcylation level was examined in six cancer cell lines including breast (MCF-7 and MDA-MB-231), colorectal (SW480 and SW620), and liver (SK-Hep1 and HepG2).
30106436	5	93	theme	cell	611:614	arg1	liver					697:701	liver	697:701	liver (SK-Hep1 and HepG2)	697:721	O-GlcNAcylation level was examined in six cancer cell lines including breast (MCF-7 and MDA-MB-231), colorectal (SW480 and SW620), and liver (SK-Hep1 and HepG2).
30106436	5	93	theme	cell	611:614	arg1	breast					632:637	breast	632:637	breast (MCF-7 and MDA-MB-231)	632:660	O-GlcNAcylation level was examined in six cancer cell lines including breast (MCF-7 and MDA-MB-231), colorectal (SW480 and SW620), and liver (SK-Hep1 and HepG2).
30106436	12	94	theme	highest	1622:1628	arg1	protein					1642:1648	the highest upregulated protein	1618:1648	the highest upregulated protein upon OGT knockdown	1618:1667	Using two-dimensional gel electrophoresis and mass spectrometric analysis, heat shock protein 27 (Hsp27) was found to be the highest upregulated protein upon OGT knockdown.
30106436	12	94	theme	highest	1622:1628	arg1	protein					1583:1589	heat shock protein 27	1572:1592	heat shock protein 27 (Hsp27)	1572:1600	Using two-dimensional gel electrophoresis and mass spectrometric analysis, heat shock protein 27 (Hsp27) was found to be the highest upregulated protein upon OGT knockdown.
30106436	11	95	from	effect	1457:1462	arg1	cultures					1487:1494	colony and spheroid cultures	1467:1494	colony and spheroid cultures	1467:1494	Among them, OGT knockdown in MCF-7 cells revealed a high inhibitory effect on colony and spheroid cultures.
30106436	15	96	theme	spheroid	1988:1995	arg1	cultures					1997:2004	colony and spheroid cultures	1977:2004	colony and spheroid cultures	1977:2004	Notably, double knockdown of OGT and Hsp27 showed a reversal in the inhibitory effect on colony and spheroid cultures.
30106436	17	97	theme	protein	2218:2224	arg1	expression					2226:2235	Hsp27 protein expression	2212:2235	Hsp27 protein expression	2212:2235	Blocking this glycosylation by OGT knockdown may regulate both Hsp27 protein expression and its O-GlcNAc modification levels.
30106436	11	98	theme	MCF-7	1418:1422	arg1	cells					1424:1428	MCF-7 cells	1418:1428	MCF-7 cells	1418:1428	Among them, OGT knockdown in MCF-7 cells revealed a high inhibitory effect on colony and spheroid cultures.
30106436	5	99	dep	colorectal	663:672	arg1	SW480					675:679	SW480	675:679	SW480	675:679	O-GlcNAcylation level was examined in six cancer cell lines including breast (MCF-7 and MDA-MB-231), colorectal (SW480 and SW620), and liver (SK-Hep1 and HepG2).
30106436	5	99	dep	colorectal	663:672	arg1	SW620					685:689	SW620	685:689	SW620	685:689	O-GlcNAcylation level was examined in six cancer cell lines including breast (MCF-7 and MDA-MB-231), colorectal (SW480 and SW620), and liver (SK-Hep1 and HepG2).
30106436	15	100	theme	colony	1977:1982	arg1	cultures					1997:2004	colony and spheroid cultures	1977:2004	colony and spheroid cultures	1977:2004	Notably, double knockdown of OGT and Hsp27 showed a reversal in the inhibitory effect on colony and spheroid cultures.
30106436	0	101	theme	MCF-7	67:71	arg1	cells					73:77	MCF-7 cells	67:77	MCF-7 cells	67:77	Decreasing O-GlcNAcylation affects the malignant transformation of MCF-7 cells via Hsp27 expression and its O-GlcNAc modification.
30106436	7	102	from	reduction	1003:1011	arg1	levels					1040:1045	OGT and O-GlcNAcylation levels	1016:1045	OGT and O-GlcNAcylation levels	1016:1045	Reducing O-GlcNAcylation using RNA interference against OGT showed a marked reduction in OGT and O-GlcNAcylation levels.
30106436	8	103	theme	conventional	1103:1114	arg1	cultures					1126:1133	conventional monolayer cultures	1103:1133	conventional monolayer cultures	1103:1133	Surprisingly, siOGT had no effect on cell growth under conventional monolayer cultures.
30106436	11	104	from	knockdown	1405:1413	arg1	cells					1424:1428	MCF-7 cells	1418:1428	MCF-7 cells	1418:1428	Among them, OGT knockdown in MCF-7 cells revealed a high inhibitory effect on colony and spheroid cultures.
22664592	4	0	theme	YinOYang	1047:1054	arg1	method					1060:1065	the YinOYang 1.2 method	1043:1065	the YinOYang 1.2 method	1043:1065	We observed that HSP27 was modified with O-GlcNAc glycosylation in HCC cells and report that at conserved Ser residues of HSP27, alternative phosphorylation and O-GlcNAc modification can be predicted by the YinOYang 1.2 method.
22664592	7	1	theme	subcellular	1560:1570	arg1	localization					1572:1583	its subcellular localization	1556:1583	its subcellular localization	1556:1583	Crosstalk or interplay between glycosylation and phosphorylation of HSP27 could regulate its subcellular localization and biological functions in liver cancer.
22664592	4	2	theme	alternative	969:979	arg1	phosphorylation					981:995	alternative phosphorylation	969:995	alternative phosphorylation	969:995	We observed that HSP27 was modified with O-GlcNAc glycosylation in HCC cells and report that at conserved Ser residues of HSP27, alternative phosphorylation and O-GlcNAc modification can be predicted by the YinOYang 1.2 method.
22664592	1	3	theme	dynamic	151:157	arg1	interplay					159:167	the dynamic interplay	147:167	the dynamic interplay between O-GlcNAcylation and O-phosphorylation	147:213	It has been reported that the dynamic interplay between O-GlcNAcylation and O-phosphorylation is responsible for altering the activity or localization of heat-shock proteins.
22664592	1	3	theme	dynamic	151:157	arg1	responsible					218:228	responsible	218:228	responsible	218:228	It has been reported that the dynamic interplay between O-GlcNAcylation and O-phosphorylation is responsible for altering the activity or localization of heat-shock proteins.
22664592	7	4	theme	HSP27	1535:1539	arg1	glycosylation					1498:1510	glycosylation	1498:1510	glycosylation	1498:1510	Crosstalk or interplay between glycosylation and phosphorylation of HSP27 could regulate its subcellular localization and biological functions in liver cancer.
22664592	7	4	theme	HSP27	1535:1539	arg1	phosphorylation					1516:1530	phosphorylation	1516:1530	phosphorylation of HSP27	1516:1539	Crosstalk or interplay between glycosylation and phosphorylation of HSP27 could regulate its subcellular localization and biological functions in liver cancer.
22664592	4	5	theme	Ser	946:948	arg1	residues					950:957	conserved Ser residues	936:957	conserved Ser residues of HSP27	936:966	We observed that HSP27 was modified with O-GlcNAc glycosylation in HCC cells and report that at conserved Ser residues of HSP27, alternative phosphorylation and O-GlcNAc modification can be predicted by the YinOYang 1.2 method.
22664592	4	5	theme	Ser	946:948	arg1	HSP27					962:966	HSP27	962:966	HSP27	962:966	We observed that HSP27 was modified with O-GlcNAc glycosylation in HCC cells and report that at conserved Ser residues of HSP27, alternative phosphorylation and O-GlcNAc modification can be predicted by the YinOYang 1.2 method.
22664592	5	6	theme	increased	1137:1145	arg1	import					1155:1160	increased nuclear import	1137:1160	increased nuclear import of HSP27-WT and HSP27-3D	1137:1185	Furthermore, after P79350 or combined SB203580 and PUGNAc treatment, increased nuclear import of HSP27-WT and HSP27-3D implied that the entry of HSP27 into the nucleus was not only correlated with phosphorylation, but also with O-GlcNAc glycosylation.
22664592	4	7	theme	O-GlcNAc	881:888	arg1	glycosylation					890:902	O-GlcNAc glycosylation	881:902	O-GlcNAc glycosylation in HCC cells	881:915	We observed that HSP27 was modified with O-GlcNAc glycosylation in HCC cells and report that at conserved Ser residues of HSP27, alternative phosphorylation and O-GlcNAc modification can be predicted by the YinOYang 1.2 method.
22664592	1	8	theme	heat-shock	275:284	arg1	proteins					286:293	heat-shock proteins	275:293	heat-shock proteins	275:293	It has been reported that the dynamic interplay between O-GlcNAcylation and O-phosphorylation is responsible for altering the activity or localization of heat-shock proteins.
22664592	4	9	theme	conserved	936:944	arg1	residues					950:957	conserved Ser residues	936:957	conserved Ser residues of HSP27	936:966	We observed that HSP27 was modified with O-GlcNAc glycosylation in HCC cells and report that at conserved Ser residues of HSP27, alternative phosphorylation and O-GlcNAc modification can be predicted by the YinOYang 1.2 method.
22664592	4	9	theme	conserved	936:944	arg1	HSP27					962:966	HSP27	962:966	HSP27	962:966	We observed that HSP27 was modified with O-GlcNAc glycosylation in HCC cells and report that at conserved Ser residues of HSP27, alternative phosphorylation and O-GlcNAc modification can be predicted by the YinOYang 1.2 method.
22664592	1	10	theme	proteins	286:293	arg1	activity					247:254	activity	247:254	activity	247:254	It has been reported that the dynamic interplay between O-GlcNAcylation and O-phosphorylation is responsible for altering the activity or localization of heat-shock proteins.
22664592	1	10	theme	proteins	286:293	arg1	localization					259:270	localization	259:270	localization	259:270	It has been reported that the dynamic interplay between O-GlcNAcylation and O-phosphorylation is responsible for altering the activity or localization of heat-shock proteins.
22664592	4	11	dep	report	921:926	arg1	predicted					1030:1038	predicted	1030:1038	can be predicted by the YinOYang 1.2 method	1023:1065	We observed that HSP27 was modified with O-GlcNAc glycosylation in HCC cells and report that at conserved Ser residues of HSP27, alternative phosphorylation and O-GlcNAc modification can be predicted by the YinOYang 1.2 method.
22664592	5	12	theme	combined	1097:1104	arg1	treatment					1126:1134	combined SB203580 and PUGNAc treatment	1097:1134	combined SB203580 and PUGNAc treatment	1097:1134	Furthermore, after P79350 or combined SB203580 and PUGNAc treatment, increased nuclear import of HSP27-WT and HSP27-3D implied that the entry of HSP27 into the nucleus was not only correlated with phosphorylation, but also with O-GlcNAc glycosylation.
22664592	2	13	theme	hepatocellular	419:432	arg1	cells					447:451	hepatocellular cancer (HCC) cells	419:451	hepatocellular cancer (HCC) cells	419:451	The aim of this study was to determine whether dynamic interplay between O-GlcNAcylation and O-phosphorylation of HSP27 in hepatocellular cancer (HCC) cells affect its entry into the nucleus.
22664592	5	14	theme	HSP27	1213:1217	arg1	entry					1204:1208	the entry	1200:1208	the entry of HSP27 into the nucleus	1200:1234	Furthermore, after P79350 or combined SB203580 and PUGNAc treatment, increased nuclear import of HSP27-WT and HSP27-3D implied that the entry of HSP27 into the nucleus was not only correlated with phosphorylation, but also with O-GlcNAc glycosylation.
22664592	3	15	theme	HSP27-3D	726:733	arg1	mutants					736:742	pseudophosphorylated (HSP27-3D) mutants	704:742	pseudophosphorylated (HSP27-3D) mutants	704:742	We demonstrate that the entry of HSP27 into the nucleus correlated with its phosphorylation through transfecting HCC cells with plasmids coding for wild-type HSP27 (HSP27-WT), its non-phosphorylatable (HSP27-3A) and pseudophosphorylated (HSP27-3D) mutants, however, not all of the endogenous or exogenous nuclear HSP27 was modified by phosphorylation.
22664592	4	16	theme	O-GlcNAc	1001:1008	arg1	modification					1010:1021	O-GlcNAc modification	1001:1021	O-GlcNAc modification	1001:1021	We observed that HSP27 was modified with O-GlcNAc glycosylation in HCC cells and report that at conserved Ser residues of HSP27, alternative phosphorylation and O-GlcNAc modification can be predicted by the YinOYang 1.2 method.
22664592	2	17	from	O-GlcNAcylation	369:383	arg1	cells					447:451	hepatocellular cancer (HCC) cells	419:451	hepatocellular cancer (HCC) cells	419:451	The aim of this study was to determine whether dynamic interplay between O-GlcNAcylation and O-phosphorylation of HSP27 in hepatocellular cancer (HCC) cells affect its entry into the nucleus.
22664592	0	18	dep	phosphorylation	77:91	arg1	glycosylation					106:118	glycosylation	106:118	glycosylation	106:118	Translocation of HSP27 into liver cancer cell nucleus may be associated with phosphorylation and O-GlcNAc glycosylation.
22664592	6	19	theme	HSP27	1406:1410	arg1	function					1412:1419	HSP27 function	1406:1419	HSP27 function	1406:1419	Collectively, O-GlcNAcylation of HSP27 in HCC cells may be a novel regulatory mode of HSP27 function, particularly for its entry into the nucleus.
22664592	4	20	mod	modified	867:874	arg3	glycosylation					890:902	O-GlcNAc glycosylation	881:902	O-GlcNAc glycosylation in HCC cells	881:915	We observed that HSP27 was modified with O-GlcNAc glycosylation in HCC cells and report that at conserved Ser residues of HSP27, alternative phosphorylation and O-GlcNAc modification can be predicted by the YinOYang 1.2 method.
22664592	4	20	mod	modified	867:874	arg1	HSP27					857:861	HSP27	857:861	HSP27	857:861	We observed that HSP27 was modified with O-GlcNAc glycosylation in HCC cells and report that at conserved Ser residues of HSP27, alternative phosphorylation and O-GlcNAc modification can be predicted by the YinOYang 1.2 method.
22664592	4	20	mod	modified	867:874	arg3	report					921:926	report	921:926	report	921:926	We observed that HSP27 was modified with O-GlcNAc glycosylation in HCC cells and report that at conserved Ser residues of HSP27, alternative phosphorylation and O-GlcNAc modification can be predicted by the YinOYang 1.2 method.
22664592	2	21	theme	HSP27	410:414	arg1	O-GlcNAcylation					369:383	O-GlcNAcylation	369:383	O-GlcNAcylation	369:383	The aim of this study was to determine whether dynamic interplay between O-GlcNAcylation and O-phosphorylation of HSP27 in hepatocellular cancer (HCC) cells affect its entry into the nucleus.
22664592	2	21	theme	HSP27	410:414	arg1	O-phosphorylation					389:405	O-phosphorylation	389:405	O-phosphorylation	389:405	The aim of this study was to determine whether dynamic interplay between O-GlcNAcylation and O-phosphorylation of HSP27 in hepatocellular cancer (HCC) cells affect its entry into the nucleus.
22664592	2	22	from	O-phosphorylation	389:405	arg1	cells					447:451	hepatocellular cancer (HCC) cells	419:451	hepatocellular cancer (HCC) cells	419:451	The aim of this study was to determine whether dynamic interplay between O-GlcNAcylation and O-phosphorylation of HSP27 in hepatocellular cancer (HCC) cells affect its entry into the nucleus.
22664592	3	23	mod	modified	811:818	arg1	HSP27					801:805	the endogenous or exogenous nuclear HSP27	765:805	the endogenous or exogenous nuclear HSP27	765:805	We demonstrate that the entry of HSP27 into the nucleus correlated with its phosphorylation through transfecting HCC cells with plasmids coding for wild-type HSP27 (HSP27-WT), its non-phosphorylatable (HSP27-3A) and pseudophosphorylated (HSP27-3D) mutants, however, not all of the endogenous or exogenous nuclear HSP27 was modified by phosphorylation.
22664592	3	23	mod	modified	811:818	arg1	all					758:760	all	758:760	all	758:760	We demonstrate that the entry of HSP27 into the nucleus correlated with its phosphorylation through transfecting HCC cells with plasmids coding for wild-type HSP27 (HSP27-WT), its non-phosphorylatable (HSP27-3A) and pseudophosphorylated (HSP27-3D) mutants, however, not all of the endogenous or exogenous nuclear HSP27 was modified by phosphorylation.
22664592	3	23	mod	modified	811:818	arg3	phosphorylation					823:837	phosphorylation	823:837	phosphorylation	823:837	We demonstrate that the entry of HSP27 into the nucleus correlated with its phosphorylation through transfecting HCC cells with plasmids coding for wild-type HSP27 (HSP27-WT), its non-phosphorylatable (HSP27-3A) and pseudophosphorylated (HSP27-3D) mutants, however, not all of the endogenous or exogenous nuclear HSP27 was modified by phosphorylation.
22664592	6	24	theme	HSP27	1353:1357	arg1	O-GlcNAcylation					1334:1348	O-GlcNAcylation	1334:1348	O-GlcNAcylation of HSP27 in HCC cells	1334:1370	Collectively, O-GlcNAcylation of HSP27 in HCC cells may be a novel regulatory mode of HSP27 function, particularly for its entry into the nucleus.
22664592	6	24	theme	HSP27	1353:1357	arg1	mode					1398:1401	a novel regulatory mode	1379:1401	a novel regulatory mode of HSP27 function	1379:1419	Collectively, O-GlcNAcylation of HSP27 in HCC cells may be a novel regulatory mode of HSP27 function, particularly for its entry into the nucleus.
22664592	2	25	theme	study	312:316	arg1	aim					300:302	The aim	296:302	The aim of this study	296:316	The aim of this study was to determine whether dynamic interplay between O-GlcNAcylation and O-phosphorylation of HSP27 in hepatocellular cancer (HCC) cells affect its entry into the nucleus.
22664592	5	26	theme	O-GlcNAc	1296:1303	arg1	glycosylation					1305:1317	O-GlcNAc glycosylation	1296:1317	O-GlcNAc glycosylation	1296:1317	Furthermore, after P79350 or combined SB203580 and PUGNAc treatment, increased nuclear import of HSP27-WT and HSP27-3D implied that the entry of HSP27 into the nucleus was not only correlated with phosphorylation, but also with O-GlcNAc glycosylation.
22664592	0	27	theme	HSP27	17:21	arg1	Translocation					0:12	Translocation	0:12	Translocation of HSP27 into liver cancer cell nucleus	0:52	Translocation of HSP27 into liver cancer cell nucleus may be associated with phosphorylation and O-GlcNAc glycosylation.
22664592	6	28	theme	regulatory	1387:1396	arg1	O-GlcNAcylation					1334:1348	O-GlcNAcylation	1334:1348	O-GlcNAcylation of HSP27 in HCC cells	1334:1370	Collectively, O-GlcNAcylation of HSP27 in HCC cells may be a novel regulatory mode of HSP27 function, particularly for its entry into the nucleus.
22664592	6	28	theme	regulatory	1387:1396	arg1	mode					1398:1401	a novel regulatory mode	1379:1401	a novel regulatory mode of HSP27 function	1379:1419	Collectively, O-GlcNAcylation of HSP27 in HCC cells may be a novel regulatory mode of HSP27 function, particularly for its entry into the nucleus.
22664592	1	29	dep	activity	247:254	arg1	the					243:245	the	243:245	the	243:245	It has been reported that the dynamic interplay between O-GlcNAcylation and O-phosphorylation is responsible for altering the activity or localization of heat-shock proteins.
22664592	2	30	theme	HCC	442:444	arg1	cells					447:451	hepatocellular cancer (HCC) cells	419:451	hepatocellular cancer (HCC) cells	419:451	The aim of this study was to determine whether dynamic interplay between O-GlcNAcylation and O-phosphorylation of HSP27 in hepatocellular cancer (HCC) cells affect its entry into the nucleus.
22664592	0	31	theme	cancer	34:39	arg1	nucleus					46:52	liver cancer cell nucleus	28:52	liver cancer cell nucleus	28:52	Translocation of HSP27 into liver cancer cell nucleus may be associated with phosphorylation and O-GlcNAc glycosylation.
22664592	6	32	from	O-GlcNAcylation	1334:1348	arg1	cells					1366:1370	HCC cells	1362:1370	HCC cells	1362:1370	Collectively, O-GlcNAcylation of HSP27 in HCC cells may be a novel regulatory mode of HSP27 function, particularly for its entry into the nucleus.
22664592	0	33	theme	liver	28:32	arg1	nucleus					46:52	liver cancer cell nucleus	28:52	liver cancer cell nucleus	28:52	Translocation of HSP27 into liver cancer cell nucleus may be associated with phosphorylation and O-GlcNAc glycosylation.
22664592	3	34	theme	endogenous	769:778	arg1	HSP27					801:805	the endogenous or exogenous nuclear HSP27	765:805	the endogenous or exogenous nuclear HSP27	765:805	We demonstrate that the entry of HSP27 into the nucleus correlated with its phosphorylation through transfecting HCC cells with plasmids coding for wild-type HSP27 (HSP27-WT), its non-phosphorylatable (HSP27-3A) and pseudophosphorylated (HSP27-3D) mutants, however, not all of the endogenous or exogenous nuclear HSP27 was modified by phosphorylation.
22664592	7	35	from	localization	1572:1583	arg1	cancer					1619:1624	liver cancer	1613:1624	liver cancer	1613:1624	Crosstalk or interplay between glycosylation and phosphorylation of HSP27 could regulate its subcellular localization and biological functions in liver cancer.
22664592	2	36	theme	cancer	434:439	arg1	cells					447:451	hepatocellular cancer (HCC) cells	419:451	hepatocellular cancer (HCC) cells	419:451	The aim of this study was to determine whether dynamic interplay between O-GlcNAcylation and O-phosphorylation of HSP27 in hepatocellular cancer (HCC) cells affect its entry into the nucleus.
22664592	5	37	theme	nuclear	1147:1153	arg1	import					1155:1160	increased nuclear import	1137:1160	increased nuclear import of HSP27-WT and HSP27-3D	1137:1185	Furthermore, after P79350 or combined SB203580 and PUGNAc treatment, increased nuclear import of HSP27-WT and HSP27-3D implied that the entry of HSP27 into the nucleus was not only correlated with phosphorylation, but also with O-GlcNAc glycosylation.
22664592	5	38	theme	HSP27-3D	1178:1185	arg1	import					1155:1160	increased nuclear import	1137:1160	increased nuclear import of HSP27-WT and HSP27-3D	1137:1185	Furthermore, after P79350 or combined SB203580 and PUGNAc treatment, increased nuclear import of HSP27-WT and HSP27-3D implied that the entry of HSP27 into the nucleus was not only correlated with phosphorylation, but also with O-GlcNAc glycosylation.
22664592	3	39	theme	HCC	601:603	arg1	cells					605:609	HCC cells	601:609	HCC cells	601:609	We demonstrate that the entry of HSP27 into the nucleus correlated with its phosphorylation through transfecting HCC cells with plasmids coding for wild-type HSP27 (HSP27-WT), its non-phosphorylatable (HSP27-3A) and pseudophosphorylated (HSP27-3D) mutants, however, not all of the endogenous or exogenous nuclear HSP27 was modified by phosphorylation.
22664592	5	40	theme	SB203580	1106:1113	arg1	treatment					1126:1134	combined SB203580 and PUGNAc treatment	1097:1134	combined SB203580 and PUGNAc treatment	1097:1134	Furthermore, after P79350 or combined SB203580 and PUGNAc treatment, increased nuclear import of HSP27-WT and HSP27-3D implied that the entry of HSP27 into the nucleus was not only correlated with phosphorylation, but also with O-GlcNAc glycosylation.
22664592	0	41	theme	cell	41:44	arg1	nucleus					46:52	liver cancer cell nucleus	28:52	liver cancer cell nucleus	28:52	Translocation of HSP27 into liver cancer cell nucleus may be associated with phosphorylation and O-GlcNAc glycosylation.
22664592	7	42	theme	liver	1613:1617	arg1	cancer					1619:1624	liver cancer	1613:1624	liver cancer	1613:1624	Crosstalk or interplay between glycosylation and phosphorylation of HSP27 could regulate its subcellular localization and biological functions in liver cancer.
22664592	5	43	theme	PUGNAc	1119:1124	arg1	treatment					1126:1134	combined SB203580 and PUGNAc treatment	1097:1134	combined SB203580 and PUGNAc treatment	1097:1134	Furthermore, after P79350 or combined SB203580 and PUGNAc treatment, increased nuclear import of HSP27-WT and HSP27-3D implied that the entry of HSP27 into the nucleus was not only correlated with phosphorylation, but also with O-GlcNAc glycosylation.
22664592	2	44	theme	dynamic	343:349	arg1	interplay					351:359	dynamic interplay	343:359	dynamic interplay between O-GlcNAcylation and O-phosphorylation of HSP27 in hepatocellular cancer (HCC) cells	343:451	The aim of this study was to determine whether dynamic interplay between O-GlcNAcylation and O-phosphorylation of HSP27 in hepatocellular cancer (HCC) cells affect its entry into the nucleus.
22664592	5	45	theme	HSP27-WT	1165:1172	arg1	import					1155:1160	increased nuclear import	1137:1160	increased nuclear import of HSP27-WT and HSP27-3D	1137:1185	Furthermore, after P79350 or combined SB203580 and PUGNAc treatment, increased nuclear import of HSP27-WT and HSP27-3D implied that the entry of HSP27 into the nucleus was not only correlated with phosphorylation, but also with O-GlcNAc glycosylation.
22664592	7	46	from	functions	1600:1608	arg1	cancer					1619:1624	liver cancer	1613:1624	liver cancer	1613:1624	Crosstalk or interplay between glycosylation and phosphorylation of HSP27 could regulate its subcellular localization and biological functions in liver cancer.
22664592	3	47	theme	wild-type	636:644	arg1	HSP27-WT					653:660	HSP27-WT	653:660	HSP27-WT	653:660	We demonstrate that the entry of HSP27 into the nucleus correlated with its phosphorylation through transfecting HCC cells with plasmids coding for wild-type HSP27 (HSP27-WT), its non-phosphorylatable (HSP27-3A) and pseudophosphorylated (HSP27-3D) mutants, however, not all of the endogenous or exogenous nuclear HSP27 was modified by phosphorylation.
22664592	3	47	theme	wild-type	636:644	arg1	HSP27					646:650	wild-type HSP27	636:650	wild-type HSP27 (HSP27-WT)	636:661	We demonstrate that the entry of HSP27 into the nucleus correlated with its phosphorylation through transfecting HCC cells with plasmids coding for wild-type HSP27 (HSP27-WT), its non-phosphorylatable (HSP27-3A) and pseudophosphorylated (HSP27-3D) mutants, however, not all of the endogenous or exogenous nuclear HSP27 was modified by phosphorylation.
22664592	7	48	gly	glycosylation	1498:1510	arg1	HSP27					1535:1539	HSP27	1535:1539	HSP27	1535:1539	Crosstalk or interplay between glycosylation and phosphorylation of HSP27 could regulate its subcellular localization and biological functions in liver cancer.
22664592	4	49	theme	HCC	907:909	arg1	cells					911:915	HCC cells	907:915	HCC cells	907:915	We observed that HSP27 was modified with O-GlcNAc glycosylation in HCC cells and report that at conserved Ser residues of HSP27, alternative phosphorylation and O-GlcNAc modification can be predicted by the YinOYang 1.2 method.
22664592	6	50	theme	HCC	1362:1364	arg1	cells					1366:1370	HCC cells	1362:1370	HCC cells	1362:1370	Collectively, O-GlcNAcylation of HSP27 in HCC cells may be a novel regulatory mode of HSP27 function, particularly for its entry into the nucleus.
22664592	6	51	theme	novel	1381:1385	arg1	O-GlcNAcylation					1334:1348	O-GlcNAcylation	1334:1348	O-GlcNAcylation of HSP27 in HCC cells	1334:1370	Collectively, O-GlcNAcylation of HSP27 in HCC cells may be a novel regulatory mode of HSP27 function, particularly for its entry into the nucleus.
22664592	6	51	theme	novel	1381:1385	arg1	mode					1398:1401	a novel regulatory mode	1379:1401	a novel regulatory mode of HSP27 function	1379:1419	Collectively, O-GlcNAcylation of HSP27 in HCC cells may be a novel regulatory mode of HSP27 function, particularly for its entry into the nucleus.
22664592	4	52	from	glycosylation	890:902	arg1	cells					911:915	HCC cells	907:915	HCC cells	907:915	We observed that HSP27 was modified with O-GlcNAc glycosylation in HCC cells and report that at conserved Ser residues of HSP27, alternative phosphorylation and O-GlcNAc modification can be predicted by the YinOYang 1.2 method.
22664592	7	53	theme	biological	1589:1598	arg1	functions					1600:1608	biological functions	1589:1608	biological functions	1589:1608	Crosstalk or interplay between glycosylation and phosphorylation of HSP27 could regulate its subcellular localization and biological functions in liver cancer.
22664592	3	54	theme	HSP27	521:525	arg1	entry					512:516	the entry	508:516	the entry of HSP27 into the nucleus	508:542	We demonstrate that the entry of HSP27 into the nucleus correlated with its phosphorylation through transfecting HCC cells with plasmids coding for wild-type HSP27 (HSP27-WT), its non-phosphorylatable (HSP27-3A) and pseudophosphorylated (HSP27-3D) mutants, however, not all of the endogenous or exogenous nuclear HSP27 was modified by phosphorylation.
22664592	3	55	theme	exogenous	783:791	arg1	HSP27					801:805	the endogenous or exogenous nuclear HSP27	765:805	the endogenous or exogenous nuclear HSP27	765:805	We demonstrate that the entry of HSP27 into the nucleus correlated with its phosphorylation through transfecting HCC cells with plasmids coding for wild-type HSP27 (HSP27-WT), its non-phosphorylatable (HSP27-3A) and pseudophosphorylated (HSP27-3D) mutants, however, not all of the endogenous or exogenous nuclear HSP27 was modified by phosphorylation.
22664592	4	56	theme	HSP27	962:966	arg1	residues					950:957	conserved Ser residues	936:957	conserved Ser residues of HSP27	936:966	We observed that HSP27 was modified with O-GlcNAc glycosylation in HCC cells and report that at conserved Ser residues of HSP27, alternative phosphorylation and O-GlcNAc modification can be predicted by the YinOYang 1.2 method.
22664592	4	56	theme	HSP27	962:966	arg1	HSP27					962:966	HSP27	962:966	HSP27	962:966	We observed that HSP27 was modified with O-GlcNAc glycosylation in HCC cells and report that at conserved Ser residues of HSP27, alternative phosphorylation and O-GlcNAc modification can be predicted by the YinOYang 1.2 method.
22664592	3	57	theme	pseudophosphorylated	704:723	arg1	mutants					736:742	pseudophosphorylated (HSP27-3D) mutants	704:742	pseudophosphorylated (HSP27-3D) mutants	704:742	We demonstrate that the entry of HSP27 into the nucleus correlated with its phosphorylation through transfecting HCC cells with plasmids coding for wild-type HSP27 (HSP27-WT), its non-phosphorylatable (HSP27-3A) and pseudophosphorylated (HSP27-3D) mutants, however, not all of the endogenous or exogenous nuclear HSP27 was modified by phosphorylation.
22664592	6	58	theme	function	1412:1419	arg1	O-GlcNAcylation					1334:1348	O-GlcNAcylation	1334:1348	O-GlcNAcylation of HSP27 in HCC cells	1334:1370	Collectively, O-GlcNAcylation of HSP27 in HCC cells may be a novel regulatory mode of HSP27 function, particularly for its entry into the nucleus.
22664592	6	58	theme	function	1412:1419	arg1	mode					1398:1401	a novel regulatory mode	1379:1401	a novel regulatory mode of HSP27 function	1379:1419	Collectively, O-GlcNAcylation of HSP27 in HCC cells may be a novel regulatory mode of HSP27 function, particularly for its entry into the nucleus.
22664592	4	59	gly	glycosylation	890:902	arg1	cells					911:915	HCC cells	907:915	HCC cells	907:915	We observed that HSP27 was modified with O-GlcNAc glycosylation in HCC cells and report that at conserved Ser residues of HSP27, alternative phosphorylation and O-GlcNAc modification can be predicted by the YinOYang 1.2 method.
22664592	3	60	theme	nuclear	793:799	arg1	HSP27					801:805	the endogenous or exogenous nuclear HSP27	765:805	the endogenous or exogenous nuclear HSP27	765:805	We demonstrate that the entry of HSP27 into the nucleus correlated with its phosphorylation through transfecting HCC cells with plasmids coding for wild-type HSP27 (HSP27-WT), its non-phosphorylatable (HSP27-3A) and pseudophosphorylated (HSP27-3D) mutants, however, not all of the endogenous or exogenous nuclear HSP27 was modified by phosphorylation.
22322011	7	0	from	non-detectable	1450:1463	arg1	lines					1506:1510	the non-metastatic breast cancer cell lines	1468:1510	the non-metastatic breast cancer cell lines	1468:1510	These glycoproteins were non-detectable in the non-metastatic breast cancer cell lines.
22322011	6	1	theme	protein	1283:1289	arg1	H1					1299:1300	heterogeneous nuclear ribonuclear protein (HnRNP) H1	1249:1300	heterogeneous nuclear ribonuclear protein (HnRNP) H1	1249:1300	HPA binding correlated with levels of integrin α6, transcription factors heterogeneous nuclear ribonuclear protein (HnRNP) H1, HnRNP D-like, HnRNP A2/B1 as well as heat shock protein 27 (Hsp27), glial fibrillary acidic protein and enolase 1 (ENO1).
22322011	6	1	theme	protein	1283:1289	arg1	D-like					1309:1314	D-like	1309:1314	D-like	1309:1314	HPA binding correlated with levels of integrin α6, transcription factors heterogeneous nuclear ribonuclear protein (HnRNP) H1, HnRNP D-like, HnRNP A2/B1 as well as heat shock protein 27 (Hsp27), glial fibrillary acidic protein and enolase 1 (ENO1).
22322011	6	1	theme	protein	1283:1289	arg1	HnRNP					1303:1307	HnRNP	1303:1307	HnRNP	1303:1307	HPA binding correlated with levels of integrin α6, transcription factors heterogeneous nuclear ribonuclear protein (HnRNP) H1, HnRNP D-like, HnRNP A2/B1 as well as heat shock protein 27 (Hsp27), glial fibrillary acidic protein and enolase 1 (ENO1).
22322011	4	2	theme	breast	866:871	arg1	metastasis					880:889	breast cancer metastasis	866:889	breast cancer metastasis	866:889	The intriguing observations from the CFG array led to this study, in which HPA-binding epitopes were localized and characterized in an in vitro model of breast cancer metastasis.
22322011	6	3	theme	nuclear	1263:1269	arg1	HnRNP					1292:1296	HnRNP	1292:1296	HnRNP	1292:1296	HPA binding correlated with levels of integrin α6, transcription factors heterogeneous nuclear ribonuclear protein (HnRNP) H1, HnRNP D-like, HnRNP A2/B1 as well as heat shock protein 27 (Hsp27), glial fibrillary acidic protein and enolase 1 (ENO1).
22322011	6	3	theme	nuclear	1263:1269	arg1	protein					1283:1289	nuclear ribonuclear protein	1263:1289	heterogeneous nuclear ribonuclear protein (HnRNP) H1	1249:1300	HPA binding correlated with levels of integrin α6, transcription factors heterogeneous nuclear ribonuclear protein (HnRNP) H1, HnRNP D-like, HnRNP A2/B1 as well as heat shock protein 27 (Hsp27), glial fibrillary acidic protein and enolase 1 (ENO1).
22322011	9	4	theme	Integrin	1613:1620	arg1	α6					1622:1623	Integrin α6	1613:1623	Integrin α6	1613:1623	Integrin α6 was the most abundant HPA glycoprotein in the breast cancer cells with a metastatic phenotype; this concurred with previous findings in colorectal cancer.
22322011	9	4	theme	Integrin	1613:1620	arg1	glycoprotein					1651:1662	the most abundant HPA glycoprotein	1629:1662	the most abundant HPA glycoprotein in the breast cancer cells with a metastatic phenotype	1629:1717	Integrin α6 was the most abundant HPA glycoprotein in the breast cancer cells with a metastatic phenotype; this concurred with previous findings in colorectal cancer.
22322011	10	5	theme	transcription	1856:1868	arg1	factors					1870:1876	O-GlcNAcylated transcription factors	1841:1876	O-GlcNAcylated transcription factors	1841:1876	This is the first report in which HPA has been shown to bind O-GlcNAcylated transcription factors.
22322011	6	6	theme	factors	1241:1247	arg1	levels					1204:1209	levels	1204:1209	levels of integrin α6, transcription factors heterogeneous nuclear ribonuclear protein (HnRNP) H1, HnRNP D-like, HnRNP A2/B1 as well as heat shock protein 27 (Hsp27), glial fibrillary acidic protein and enolase 1 (ENO1)	1204:1422	HPA binding correlated with levels of integrin α6, transcription factors heterogeneous nuclear ribonuclear protein (HnRNP) H1, HnRNP D-like, HnRNP A2/B1 as well as heat shock protein 27 (Hsp27), glial fibrillary acidic protein and enolase 1 (ENO1).
22322011	9	7	gly	glycoprotein	1651:1662	arg1	α6					1622:1623	Integrin α6	1613:1623	Integrin α6	1613:1623	Integrin α6 was the most abundant HPA glycoprotein in the breast cancer cells with a metastatic phenotype; this concurred with previous findings in colorectal cancer.
22322011	9	7	gly	glycoprotein	1651:1662	arg1	glycoprotein					1651:1662	the most abundant HPA glycoprotein	1629:1662	the most abundant HPA glycoprotein in the breast cancer cells with a metastatic phenotype	1629:1717	Integrin α6 was the most abundant HPA glycoprotein in the breast cancer cells with a metastatic phenotype; this concurred with previous findings in colorectal cancer.
22322011	4	8	theme	in	848:849	arg1	model					857:861	an in vitro model	845:861	an in vitro model of breast cancer metastasis	845:889	The intriguing observations from the CFG array led to this study, in which HPA-binding epitopes were localized and characterized in an in vitro model of breast cancer metastasis.
22322011	1	9	theme	Helix	193:197	arg1	agglutinin					207:216	the lectin Helix pomatia agglutinin	182:216	the lectin Helix pomatia agglutinin (HPA) in breast cancer	182:239	There has been considerable interest in understanding the epitopes that bind the lectin Helix pomatia agglutinin (HPA) in breast cancer as the lectin has been shown to identify glycosylation changes associated with the development of metastatic disease.
22322011	1	9	theme	Helix	193:197	arg1	HPA					219:221	HPA	219:221	HPA	219:221	There has been considerable interest in understanding the epitopes that bind the lectin Helix pomatia agglutinin (HPA) in breast cancer as the lectin has been shown to identify glycosylation changes associated with the development of metastatic disease.
22322011	1	10	theme	considerable	120:131	arg1	interest					133:140	considerable interest	120:140	considerable interest	120:140	There has been considerable interest in understanding the epitopes that bind the lectin Helix pomatia agglutinin (HPA) in breast cancer as the lectin has been shown to identify glycosylation changes associated with the development of metastatic disease.
22322011	9	11	theme	HPA	1647:1649	arg1	α6					1622:1623	Integrin α6	1613:1623	Integrin α6	1613:1623	Integrin α6 was the most abundant HPA glycoprotein in the breast cancer cells with a metastatic phenotype; this concurred with previous findings in colorectal cancer.
22322011	9	11	theme	HPA	1647:1649	arg1	glycoprotein					1651:1662	the most abundant HPA glycoprotein	1629:1662	the most abundant HPA glycoprotein in the breast cancer cells with a metastatic phenotype	1629:1717	Integrin α6 was the most abundant HPA glycoprotein in the breast cancer cells with a metastatic phenotype; this concurred with previous findings in colorectal cancer.
22322011	6	12	theme	α6	1223:1224	arg1	levels					1204:1209	levels	1204:1209	levels of integrin α6, transcription factors heterogeneous nuclear ribonuclear protein (HnRNP) H1, HnRNP D-like, HnRNP A2/B1 as well as heat shock protein 27 (Hsp27), glial fibrillary acidic protein and enolase 1 (ENO1)	1204:1422	HPA binding correlated with levels of integrin α6, transcription factors heterogeneous nuclear ribonuclear protein (HnRNP) H1, HnRNP D-like, HnRNP A2/B1 as well as heat shock protein 27 (Hsp27), glial fibrillary acidic protein and enolase 1 (ENO1).
22322011	5	13	theme	glycoproteomic	1054:1067	arg1	analysis					1069:1076	a glycoproteomic analysis	1052:1076	a glycoproteomic analysis based on 2-dimensional electrophoresis (2DE), western blotting and mass spectrometry	1052:1161	HMT3522 (benign disease), BT474 (primary cancer) and T47D/MCF7 (metastatic cancer) cells were assessed in confocal microscopy-based co-localization studies and a glycoproteomic analysis based on 2-dimensional electrophoresis (2DE), western blotting and mass spectrometry was adopted.
22322011	6	14	theme	fibrillary	1377:1386	arg1	protein					1395:1401	glial fibrillary acidic protein	1371:1401	glial fibrillary acidic protein	1371:1401	HPA binding correlated with levels of integrin α6, transcription factors heterogeneous nuclear ribonuclear protein (HnRNP) H1, HnRNP D-like, HnRNP A2/B1 as well as heat shock protein 27 (Hsp27), glial fibrillary acidic protein and enolase 1 (ENO1).
22322011	4	15	theme	metastasis	880:889	arg1	model					857:861	an in vitro model	845:861	an in vitro model of breast cancer metastasis	845:889	The intriguing observations from the CFG array led to this study, in which HPA-binding epitopes were localized and characterized in an in vitro model of breast cancer metastasis.
22322011	5	16	theme	confocal	998:1005	arg1	studies					1040:1046	confocal microscopy-based co-localization studies	998:1046	confocal microscopy-based co-localization studies	998:1046	HMT3522 (benign disease), BT474 (primary cancer) and T47D/MCF7 (metastatic cancer) cells were assessed in confocal microscopy-based co-localization studies and a glycoproteomic analysis based on 2-dimensional electrophoresis (2DE), western blotting and mass spectrometry was adopted.
22322011	5	17	theme	benign	901:906	arg1	HMT3522					892:898	HMT3522	892:898	HMT3522 (benign disease)	892:915	HMT3522 (benign disease), BT474 (primary cancer) and T47D/MCF7 (metastatic cancer) cells were assessed in confocal microscopy-based co-localization studies and a glycoproteomic analysis based on 2-dimensional electrophoresis (2DE), western blotting and mass spectrometry was adopted.
22322011	5	17	theme	benign	901:906	arg1	disease					908:914	benign disease	901:914	benign disease	901:914	HMT3522 (benign disease), BT474 (primary cancer) and T47D/MCF7 (metastatic cancer) cells were assessed in confocal microscopy-based co-localization studies and a glycoproteomic analysis based on 2-dimensional electrophoresis (2DE), western blotting and mass spectrometry was adopted.
22322011	9	18	theme	breast	1671:1676	arg1	cells					1685:1689	the breast cancer cells	1667:1689	the breast cancer cells	1667:1689	Integrin α6 was the most abundant HPA glycoprotein in the breast cancer cells with a metastatic phenotype; this concurred with previous findings in colorectal cancer.
22322011	5	19	theme	co-localization	1024:1038	arg1	studies					1040:1046	confocal microscopy-based co-localization studies	998:1046	confocal microscopy-based co-localization studies	998:1046	HMT3522 (benign disease), BT474 (primary cancer) and T47D/MCF7 (metastatic cancer) cells were assessed in confocal microscopy-based co-localization studies and a glycoproteomic analysis based on 2-dimensional electrophoresis (2DE), western blotting and mass spectrometry was adopted.
22322011	6	20	theme	protein	1351:1357	arg1	levels					1204:1209	levels	1204:1209	levels of integrin α6, transcription factors heterogeneous nuclear ribonuclear protein (HnRNP) H1, HnRNP D-like, HnRNP A2/B1 as well as heat shock protein 27 (Hsp27), glial fibrillary acidic protein and enolase 1 (ENO1)	1204:1422	HPA binding correlated with levels of integrin α6, transcription factors heterogeneous nuclear ribonuclear protein (HnRNP) H1, HnRNP D-like, HnRNP A2/B1 as well as heat shock protein 27 (Hsp27), glial fibrillary acidic protein and enolase 1 (ENO1).
22322011	0	21	theme	Helix	11:15	arg1	agglutinin					25:34	The lectin Helix pomatia agglutinin	0:34	The lectin Helix pomatia agglutinin	0:34	The lectin Helix pomatia agglutinin recognizes O-GlcNAc containing glycoproteins in human breast cancer.
22322011	2	22	theme	exposed	495:501	arg1	epitopes					506:513	exposed Tn epitopes	495:513	exposed Tn epitopes	495:513	HPA has previously been shown to recognize aberrant O-linked α-N-acetylgalactosamine (GalNAcα)/mucin glycosylation in cancer, including exposed Tn epitopes.
22322011	0	23	theme	human	84:88	arg1	cancer					97:102	human breast cancer	84:102	human breast cancer	84:102	The lectin Helix pomatia agglutinin recognizes O-GlcNAc containing glycoproteins in human breast cancer.
22322011	5	24	theme	HMT3522	892:898	arg1	cells					975:979	HMT3522 (benign disease), BT474 (primary cancer) and T47D/MCF7 (metastatic cancer) cells	892:979	HMT3522 (benign disease), BT474 (primary cancer) and T47D/MCF7 (metastatic cancer) cells	892:979	HMT3522 (benign disease), BT474 (primary cancer) and T47D/MCF7 (metastatic cancer) cells were assessed in confocal microscopy-based co-localization studies and a glycoproteomic analysis based on 2-dimensional electrophoresis (2DE), western blotting and mass spectrometry was adopted.
22322011	9	25	from	glycoprotein	1651:1662	arg1	cells					1685:1689	the breast cancer cells	1667:1689	the breast cancer cells	1667:1689	Integrin α6 was the most abundant HPA glycoprotein in the breast cancer cells with a metastatic phenotype; this concurred with previous findings in colorectal cancer.
22322011	1	26	theme	disease	350:356	arg1	development					324:334	the development	320:334	the development of metastatic disease	320:356	There has been considerable interest in understanding the epitopes that bind the lectin Helix pomatia agglutinin (HPA) in breast cancer as the lectin has been shown to identify glycosylation changes associated with the development of metastatic disease.
22322011	9	27	with	glycoprotein	1651:1662	arg1	phenotype					1709:1717	a metastatic phenotype	1696:1717	a metastatic phenotype	1696:1717	Integrin α6 was the most abundant HPA glycoprotein in the breast cancer cells with a metastatic phenotype; this concurred with previous findings in colorectal cancer.
22322011	6	28	theme	A2/B1	1323:1327	arg1	levels					1204:1209	levels	1204:1209	levels of integrin α6, transcription factors heterogeneous nuclear ribonuclear protein (HnRNP) H1, HnRNP D-like, HnRNP A2/B1 as well as heat shock protein 27 (Hsp27), glial fibrillary acidic protein and enolase 1 (ENO1)	1204:1422	HPA binding correlated with levels of integrin α6, transcription factors heterogeneous nuclear ribonuclear protein (HnRNP) H1, HnRNP D-like, HnRNP A2/B1 as well as heat shock protein 27 (Hsp27), glial fibrillary acidic protein and enolase 1 (ENO1).
22322011	5	29	theme	2-dimensional	1087:1099	arg1	2DE					1118:1120	2DE	1118:1120	2DE	1118:1120	HMT3522 (benign disease), BT474 (primary cancer) and T47D/MCF7 (metastatic cancer) cells were assessed in confocal microscopy-based co-localization studies and a glycoproteomic analysis based on 2-dimensional electrophoresis (2DE), western blotting and mass spectrometry was adopted.
22322011	5	29	theme	2-dimensional	1087:1099	arg1	electrophoresis					1101:1115	2-dimensional electrophoresis	1087:1115	2-dimensional electrophoresis (2DE)	1087:1121	HMT3522 (benign disease), BT474 (primary cancer) and T47D/MCF7 (metastatic cancer) cells were assessed in confocal microscopy-based co-localization studies and a glycoproteomic analysis based on 2-dimensional electrophoresis (2DE), western blotting and mass spectrometry was adopted.
22322011	4	30	from	array	754:758	arg1	observations					728:739	The intriguing observations	713:739	The intriguing observations from the CFG array	713:758	The intriguing observations from the CFG array led to this study, in which HPA-binding epitopes were localized and characterized in an in vitro model of breast cancer metastasis.
22322011	5	31	theme	T47D/MCF7	945:953	arg1	cells					975:979	HMT3522 (benign disease), BT474 (primary cancer) and T47D/MCF7 (metastatic cancer) cells	892:979	HMT3522 (benign disease), BT474 (primary cancer) and T47D/MCF7 (metastatic cancer) cells	892:979	HMT3522 (benign disease), BT474 (primary cancer) and T47D/MCF7 (metastatic cancer) cells were assessed in confocal microscopy-based co-localization studies and a glycoproteomic analysis based on 2-dimensional electrophoresis (2DE), western blotting and mass spectrometry was adopted.
22322011	11	32	theme	aggressive	1974:1983	arg1	phenotype					1996:2004	an aggressive metastatic phenotype	1971:2004	an aggressive metastatic phenotype	1971:2004	This class of proteins represents a new means by which HPA differentiates cancer cells with an aggressive metastatic phenotype.
22322011	2	33	theme	/mucin	453:458	arg1	glycosylation					460:472	aberrant O-linked α-N-acetylgalactosamine (GalNAcα)/mucin glycosylation	402:472	aberrant O-linked α-N-acetylgalactosamine (GalNAcα)/mucin glycosylation	402:472	HPA has previously been shown to recognize aberrant O-linked α-N-acetylgalactosamine (GalNAcα)/mucin glycosylation in cancer, including exposed Tn epitopes.
22322011	6	34	theme	acidic	1388:1393	arg1	protein					1395:1401	glial fibrillary acidic protein	1371:1401	glial fibrillary acidic protein	1371:1401	HPA binding correlated with levels of integrin α6, transcription factors heterogeneous nuclear ribonuclear protein (HnRNP) H1, HnRNP D-like, HnRNP A2/B1 as well as heat shock protein 27 (Hsp27), glial fibrillary acidic protein and enolase 1 (ENO1).
22322011	5	35	theme	BT474	918:922	arg1	cells					975:979	HMT3522 (benign disease), BT474 (primary cancer) and T47D/MCF7 (metastatic cancer) cells	892:979	HMT3522 (benign disease), BT474 (primary cancer) and T47D/MCF7 (metastatic cancer) cells	892:979	HMT3522 (benign disease), BT474 (primary cancer) and T47D/MCF7 (metastatic cancer) cells were assessed in confocal microscopy-based co-localization studies and a glycoproteomic analysis based on 2-dimensional electrophoresis (2DE), western blotting and mass spectrometry was adopted.
22322011	10	36	theme	first	1792:1796	arg1	report					1798:1803	the first report	1788:1803	the first report in which HPA has been shown to bind O-GlcNAcylated transcription factors	1788:1876	This is the first report in which HPA has been shown to bind O-GlcNAcylated transcription factors.
22322011	10	36	theme	first	1792:1796	arg1	This					1780:1783	This	1780:1783	This	1780:1783	This is the first report in which HPA has been shown to bind O-GlcNAcylated transcription factors.
22322011	2	37	theme	GalNAcα	445:451	arg1	glycosylation					460:472	aberrant O-linked α-N-acetylgalactosamine (GalNAcα)/mucin glycosylation	402:472	aberrant O-linked α-N-acetylgalactosamine (GalNAcα)/mucin glycosylation	402:472	HPA has previously been shown to recognize aberrant O-linked α-N-acetylgalactosamine (GalNAcα)/mucin glycosylation in cancer, including exposed Tn epitopes.
22322011	2	38	theme	α-N-acetylgalactosamine	420:442	arg1	glycosylation					460:472	aberrant O-linked α-N-acetylgalactosamine (GalNAcα)/mucin glycosylation	402:472	aberrant O-linked α-N-acetylgalactosamine (GalNAcα)/mucin glycosylation	402:472	HPA has previously been shown to recognize aberrant O-linked α-N-acetylgalactosamine (GalNAcα)/mucin glycosylation in cancer, including exposed Tn epitopes.
22322011	6	39	theme	glial	1371:1375	arg1	protein					1395:1401	glial fibrillary acidic protein	1371:1401	glial fibrillary acidic protein	1371:1401	HPA binding correlated with levels of integrin α6, transcription factors heterogeneous nuclear ribonuclear protein (HnRNP) H1, HnRNP D-like, HnRNP A2/B1 as well as heat shock protein 27 (Hsp27), glial fibrillary acidic protein and enolase 1 (ENO1).
22322011	7	40	from	lines	1506:1510	arg1	non-detectable					1450:1463	non-detectable	1450:1463	non-detectable	1450:1463	These glycoproteins were non-detectable in the non-metastatic breast cancer cell lines.
22322011	7	41	theme	breast	1487:1492	arg1	lines					1506:1510	the non-metastatic breast cancer cell lines	1468:1510	the non-metastatic breast cancer cell lines	1468:1510	These glycoproteins were non-detectable in the non-metastatic breast cancer cell lines.
22322011	5	42	theme	primary	925:931	arg1	BT474					918:922	BT474	918:922	BT474 (primary cancer)	918:939	HMT3522 (benign disease), BT474 (primary cancer) and T47D/MCF7 (metastatic cancer) cells were assessed in confocal microscopy-based co-localization studies and a glycoproteomic analysis based on 2-dimensional electrophoresis (2DE), western blotting and mass spectrometry was adopted.
22322011	5	42	theme	primary	925:931	arg1	cancer					933:938	primary cancer	925:938	primary cancer	925:938	HMT3522 (benign disease), BT474 (primary cancer) and T47D/MCF7 (metastatic cancer) cells were assessed in confocal microscopy-based co-localization studies and a glycoproteomic analysis based on 2-dimensional electrophoresis (2DE), western blotting and mass spectrometry was adopted.
22322011	9	43	theme	colorectal	1761:1770	arg1	cancer					1772:1777	colorectal cancer	1761:1777	colorectal cancer	1761:1777	Integrin α6 was the most abundant HPA glycoprotein in the breast cancer cells with a metastatic phenotype; this concurred with previous findings in colorectal cancer.
22322011	3	44	theme	CFG	662:664	arg1	data					667:670	functional glycomics (CFG) data	640:670	functional glycomics (CFG) data	640:670	However, recent glycan-array analysis reported that diverse epitopes are also recognized by the lectin, e.g. consortium for functional glycomics (CFG) data: GalNAcα1,3Gal; β-GalNAc; GlcNAcβ1,4Gal.
22322011	2	45	theme	aberrant	402:409	arg1	glycosylation					460:472	aberrant O-linked α-N-acetylgalactosamine (GalNAcα)/mucin glycosylation	402:472	aberrant O-linked α-N-acetylgalactosamine (GalNAcα)/mucin glycosylation	402:472	HPA has previously been shown to recognize aberrant O-linked α-N-acetylgalactosamine (GalNAcα)/mucin glycosylation in cancer, including exposed Tn epitopes.
22322011	1	46	theme	glycosylation	282:294	arg1	changes					296:302	glycosylation changes	282:302	glycosylation changes associated with the development of metastatic disease	282:356	There has been considerable interest in understanding the epitopes that bind the lectin Helix pomatia agglutinin (HPA) in breast cancer as the lectin has been shown to identify glycosylation changes associated with the development of metastatic disease.
22322011	5	47	theme	western	1124:1130	arg1	blotting					1132:1139	western blotting	1124:1139	western blotting	1124:1139	HMT3522 (benign disease), BT474 (primary cancer) and T47D/MCF7 (metastatic cancer) cells were assessed in confocal microscopy-based co-localization studies and a glycoproteomic analysis based on 2-dimensional electrophoresis (2DE), western blotting and mass spectrometry was adopted.
22322011	3	48	theme	glycomics	651:659	arg1	data					667:670	functional glycomics (CFG) data	640:670	functional glycomics (CFG) data	640:670	However, recent glycan-array analysis reported that diverse epitopes are also recognized by the lectin, e.g. consortium for functional glycomics (CFG) data: GalNAcα1,3Gal; β-GalNAc; GlcNAcβ1,4Gal.
22322011	0	49	theme	O-GlcNAc	47:54	arg1	glycoproteins					67:79	O-GlcNAc containing glycoproteins	47:79	O-GlcNAc containing glycoproteins	47:79	The lectin Helix pomatia agglutinin recognizes O-GlcNAc containing glycoproteins in human breast cancer.
22322011	8	50	theme	HnRNPs	1532:1537	arg1	recognition					1517:1527	The recognition	1513:1527	The recognition of HnRNPs, Hsp27 and ENO1 by HPA	1513:1560	The recognition of HnRNPs, Hsp27 and ENO1 by HPA correlated with O-GlcNAcylation of these proteins.
22322011	5	51	theme	metastatic	956:965	arg1	cancer					967:972	metastatic cancer	956:972	metastatic cancer	956:972	HMT3522 (benign disease), BT474 (primary cancer) and T47D/MCF7 (metastatic cancer) cells were assessed in confocal microscopy-based co-localization studies and a glycoproteomic analysis based on 2-dimensional electrophoresis (2DE), western blotting and mass spectrometry was adopted.
22322011	5	51	theme	metastatic	956:965	arg1	T47D/MCF7					945:953	T47D/MCF7	945:953	T47D/MCF7 (metastatic cancer)	945:973	HMT3522 (benign disease), BT474 (primary cancer) and T47D/MCF7 (metastatic cancer) cells were assessed in confocal microscopy-based co-localization studies and a glycoproteomic analysis based on 2-dimensional electrophoresis (2DE), western blotting and mass spectrometry was adopted.
22322011	8	52	theme	Hsp27	1540:1544	arg1	recognition					1517:1527	The recognition	1513:1527	The recognition of HnRNPs, Hsp27 and ENO1 by HPA	1513:1560	The recognition of HnRNPs, Hsp27 and ENO1 by HPA correlated with O-GlcNAcylation of these proteins.
22322011	2	53	link	O-linked	411:418	arg1	glycosylation					460:472	aberrant O-linked α-N-acetylgalactosamine (GalNAcα)/mucin glycosylation	402:472	aberrant O-linked α-N-acetylgalactosamine (GalNAcα)/mucin glycosylation	402:472	HPA has previously been shown to recognize aberrant O-linked α-N-acetylgalactosamine (GalNAcα)/mucin glycosylation in cancer, including exposed Tn epitopes.
22322011	4	54	theme	HPA-binding	788:798	arg1	epitopes					800:807	HPA-binding epitopes	788:807	HPA-binding epitopes	788:807	The intriguing observations from the CFG array led to this study, in which HPA-binding epitopes were localized and characterized in an in vitro model of breast cancer metastasis.
22322011	8	55	theme	proteins	1603:1610	arg1	O-GlcNAcylation					1578:1592	O-GlcNAcylation	1578:1592	O-GlcNAcylation of these proteins	1578:1610	The recognition of HnRNPs, Hsp27 and ENO1 by HPA correlated with O-GlcNAcylation of these proteins.
22322011	1	56	theme	breast	227:232	arg1	cancer					234:239	breast cancer	227:239	breast cancer	227:239	There has been considerable interest in understanding the epitopes that bind the lectin Helix pomatia agglutinin (HPA) in breast cancer as the lectin has been shown to identify glycosylation changes associated with the development of metastatic disease.
22322011	8	57	theme	ENO1	1550:1553	arg1	recognition					1517:1527	The recognition	1513:1527	The recognition of HnRNPs, Hsp27 and ENO1 by HPA	1513:1560	The recognition of HnRNPs, Hsp27 and ENO1 by HPA correlated with O-GlcNAcylation of these proteins.
22322011	6	58	theme	shock	1345:1349	arg1	protein					1351:1357	heat shock protein 27	1340:1360	heat shock protein 27 (Hsp27)	1340:1368	HPA binding correlated with levels of integrin α6, transcription factors heterogeneous nuclear ribonuclear protein (HnRNP) H1, HnRNP D-like, HnRNP A2/B1 as well as heat shock protein 27 (Hsp27), glial fibrillary acidic protein and enolase 1 (ENO1).
22322011	6	58	theme	shock	1345:1349	arg1	Hsp27					1363:1367	Hsp27	1363:1367	Hsp27	1363:1367	HPA binding correlated with levels of integrin α6, transcription factors heterogeneous nuclear ribonuclear protein (HnRNP) H1, HnRNP D-like, HnRNP A2/B1 as well as heat shock protein 27 (Hsp27), glial fibrillary acidic protein and enolase 1 (ENO1).
22322011	6	58	theme	shock	1345:1349	arg1	ENO1					1418:1421	ENO1	1418:1421	ENO1	1418:1421	HPA binding correlated with levels of integrin α6, transcription factors heterogeneous nuclear ribonuclear protein (HnRNP) H1, HnRNP D-like, HnRNP A2/B1 as well as heat shock protein 27 (Hsp27), glial fibrillary acidic protein and enolase 1 (ENO1).
22322011	10	59	theme	O-GlcNAcylated	1841:1854	arg1	factors					1870:1876	O-GlcNAcylated transcription factors	1841:1876	O-GlcNAcylated transcription factors	1841:1876	This is the first report in which HPA has been shown to bind O-GlcNAcylated transcription factors.
22322011	6	60	dep	factors	1241:1247	arg1	H1					1299:1300	heterogeneous nuclear ribonuclear protein (HnRNP) H1	1249:1300	heterogeneous nuclear ribonuclear protein (HnRNP) H1	1249:1300	HPA binding correlated with levels of integrin α6, transcription factors heterogeneous nuclear ribonuclear protein (HnRNP) H1, HnRNP D-like, HnRNP A2/B1 as well as heat shock protein 27 (Hsp27), glial fibrillary acidic protein and enolase 1 (ENO1).
22322011	6	60	dep	factors	1241:1247	arg1	D-like					1309:1314	D-like	1309:1314	D-like	1309:1314	HPA binding correlated with levels of integrin α6, transcription factors heterogeneous nuclear ribonuclear protein (HnRNP) H1, HnRNP D-like, HnRNP A2/B1 as well as heat shock protein 27 (Hsp27), glial fibrillary acidic protein and enolase 1 (ENO1).
22322011	6	60	dep	factors	1241:1247	arg1	HnRNP					1303:1307	HnRNP	1303:1307	HnRNP	1303:1307	HPA binding correlated with levels of integrin α6, transcription factors heterogeneous nuclear ribonuclear protein (HnRNP) H1, HnRNP D-like, HnRNP A2/B1 as well as heat shock protein 27 (Hsp27), glial fibrillary acidic protein and enolase 1 (ENO1).
22322011	6	61	theme	ribonuclear	1271:1281	arg1	HnRNP					1292:1296	HnRNP	1292:1296	HnRNP	1292:1296	HPA binding correlated with levels of integrin α6, transcription factors heterogeneous nuclear ribonuclear protein (HnRNP) H1, HnRNP D-like, HnRNP A2/B1 as well as heat shock protein 27 (Hsp27), glial fibrillary acidic protein and enolase 1 (ENO1).
22322011	6	61	theme	ribonuclear	1271:1281	arg1	protein					1283:1289	nuclear ribonuclear protein	1263:1289	heterogeneous nuclear ribonuclear protein (HnRNP) H1	1249:1300	HPA binding correlated with levels of integrin α6, transcription factors heterogeneous nuclear ribonuclear protein (HnRNP) H1, HnRNP D-like, HnRNP A2/B1 as well as heat shock protein 27 (Hsp27), glial fibrillary acidic protein and enolase 1 (ENO1).
22322011	9	62	from	findings	1749:1756	arg1	cancer					1772:1777	colorectal cancer	1761:1777	colorectal cancer	1761:1777	Integrin α6 was the most abundant HPA glycoprotein in the breast cancer cells with a metastatic phenotype; this concurred with previous findings in colorectal cancer.
22322011	6	63	theme	heterogeneous	1249:1261	arg1	H1					1299:1300	heterogeneous nuclear ribonuclear protein (HnRNP) H1	1249:1300	heterogeneous nuclear ribonuclear protein (HnRNP) H1	1249:1300	HPA binding correlated with levels of integrin α6, transcription factors heterogeneous nuclear ribonuclear protein (HnRNP) H1, HnRNP D-like, HnRNP A2/B1 as well as heat shock protein 27 (Hsp27), glial fibrillary acidic protein and enolase 1 (ENO1).
22322011	6	63	theme	heterogeneous	1249:1261	arg1	D-like					1309:1314	D-like	1309:1314	D-like	1309:1314	HPA binding correlated with levels of integrin α6, transcription factors heterogeneous nuclear ribonuclear protein (HnRNP) H1, HnRNP D-like, HnRNP A2/B1 as well as heat shock protein 27 (Hsp27), glial fibrillary acidic protein and enolase 1 (ENO1).
22322011	6	63	theme	heterogeneous	1249:1261	arg1	HnRNP					1303:1307	HnRNP	1303:1307	HnRNP	1303:1307	HPA binding correlated with levels of integrin α6, transcription factors heterogeneous nuclear ribonuclear protein (HnRNP) H1, HnRNP D-like, HnRNP A2/B1 as well as heat shock protein 27 (Hsp27), glial fibrillary acidic protein and enolase 1 (ENO1).
22322011	3	64	theme	glycan-array	532:543	arg1	analysis					545:552	recent glycan-array analysis	525:552	recent glycan-array analysis	525:552	However, recent glycan-array analysis reported that diverse epitopes are also recognized by the lectin, e.g. consortium for functional glycomics (CFG) data: GalNAcα1,3Gal; β-GalNAc; GlcNAcβ1,4Gal.
22322011	6	65	theme	heat	1340:1343	arg1	protein					1351:1357	heat shock protein 27	1340:1360	heat shock protein 27 (Hsp27)	1340:1368	HPA binding correlated with levels of integrin α6, transcription factors heterogeneous nuclear ribonuclear protein (HnRNP) H1, HnRNP D-like, HnRNP A2/B1 as well as heat shock protein 27 (Hsp27), glial fibrillary acidic protein and enolase 1 (ENO1).
22322011	6	65	theme	heat	1340:1343	arg1	Hsp27					1363:1367	Hsp27	1363:1367	Hsp27	1363:1367	HPA binding correlated with levels of integrin α6, transcription factors heterogeneous nuclear ribonuclear protein (HnRNP) H1, HnRNP D-like, HnRNP A2/B1 as well as heat shock protein 27 (Hsp27), glial fibrillary acidic protein and enolase 1 (ENO1).
22322011	6	65	theme	heat	1340:1343	arg1	ENO1					1418:1421	ENO1	1418:1421	ENO1	1418:1421	HPA binding correlated with levels of integrin α6, transcription factors heterogeneous nuclear ribonuclear protein (HnRNP) H1, HnRNP D-like, HnRNP A2/B1 as well as heat shock protein 27 (Hsp27), glial fibrillary acidic protein and enolase 1 (ENO1).
22322011	6	66	theme	transcription	1227:1239	arg1	factors					1241:1247	transcription factors	1227:1247	transcription factors heterogeneous nuclear ribonuclear protein (HnRNP) H1, HnRNP D-like	1227:1314	HPA binding correlated with levels of integrin α6, transcription factors heterogeneous nuclear ribonuclear protein (HnRNP) H1, HnRNP D-like, HnRNP A2/B1 as well as heat shock protein 27 (Hsp27), glial fibrillary acidic protein and enolase 1 (ENO1).
22322011	1	67	theme	lectin	186:191	arg1	agglutinin					207:216	the lectin Helix pomatia agglutinin	182:216	the lectin Helix pomatia agglutinin (HPA) in breast cancer	182:239	There has been considerable interest in understanding the epitopes that bind the lectin Helix pomatia agglutinin (HPA) in breast cancer as the lectin has been shown to identify glycosylation changes associated with the development of metastatic disease.
22322011	1	67	theme	lectin	186:191	arg1	HPA					219:221	HPA	219:221	HPA	219:221	There has been considerable interest in understanding the epitopes that bind the lectin Helix pomatia agglutinin (HPA) in breast cancer as the lectin has been shown to identify glycosylation changes associated with the development of metastatic disease.
22322011	6	68	theme	HnRNP	1317:1321	arg1	A2/B1					1323:1327	HnRNP A2/B1	1317:1327	HnRNP A2/B1	1317:1327	HPA binding correlated with levels of integrin α6, transcription factors heterogeneous nuclear ribonuclear protein (HnRNP) H1, HnRNP D-like, HnRNP A2/B1 as well as heat shock protein 27 (Hsp27), glial fibrillary acidic protein and enolase 1 (ENO1).
22322011	3	69	theme	diverse	568:574	arg1	epitopes					576:583	diverse epitopes	568:583	diverse epitopes	568:583	However, recent glycan-array analysis reported that diverse epitopes are also recognized by the lectin, e.g. consortium for functional glycomics (CFG) data: GalNAcα1,3Gal; β-GalNAc; GlcNAcβ1,4Gal.
22322011	1	70	theme	pomatia	199:205	arg1	agglutinin					207:216	the lectin Helix pomatia agglutinin	182:216	the lectin Helix pomatia agglutinin (HPA) in breast cancer	182:239	There has been considerable interest in understanding the epitopes that bind the lectin Helix pomatia agglutinin (HPA) in breast cancer as the lectin has been shown to identify glycosylation changes associated with the development of metastatic disease.
22322011	1	70	theme	pomatia	199:205	arg1	HPA					219:221	HPA	219:221	HPA	219:221	There has been considerable interest in understanding the epitopes that bind the lectin Helix pomatia agglutinin (HPA) in breast cancer as the lectin has been shown to identify glycosylation changes associated with the development of metastatic disease.
22322011	9	71	theme	abundant	1638:1645	arg1	α6					1622:1623	Integrin α6	1613:1623	Integrin α6	1613:1623	Integrin α6 was the most abundant HPA glycoprotein in the breast cancer cells with a metastatic phenotype; this concurred with previous findings in colorectal cancer.
22322011	9	71	theme	abundant	1638:1645	arg1	glycoprotein					1651:1662	the most abundant HPA glycoprotein	1629:1662	the most abundant HPA glycoprotein in the breast cancer cells with a metastatic phenotype	1629:1717	Integrin α6 was the most abundant HPA glycoprotein in the breast cancer cells with a metastatic phenotype; this concurred with previous findings in colorectal cancer.
22322011	3	72	dep	lectin	612:617	arg1	GlcNAcβ1,4Gal					698:710	GlcNAcβ1,4Gal	698:710	GlcNAcβ1,4Gal	698:710	However, recent glycan-array analysis reported that diverse epitopes are also recognized by the lectin, e.g. consortium for functional glycomics (CFG) data: GalNAcα1,3Gal; β-GalNAc; GlcNAcβ1,4Gal.
22322011	3	72	dep	lectin	612:617	arg1	β-GalNAc					688:695	β-GalNAc	688:695	β-GalNAc	688:695	However, recent glycan-array analysis reported that diverse epitopes are also recognized by the lectin, e.g. consortium for functional glycomics (CFG) data: GalNAcα1,3Gal; β-GalNAc; GlcNAcβ1,4Gal.
22322011	3	72	dep	lectin	612:617	arg1	GalNAcα1,3Gal					673:685	GalNAcα1,3Gal	673:685	GalNAcα1,3Gal	673:685	However, recent glycan-array analysis reported that diverse epitopes are also recognized by the lectin, e.g. consortium for functional glycomics (CFG) data: GalNAcα1,3Gal; β-GalNAc; GlcNAcβ1,4Gal.
22322011	11	73	theme	metastatic	1985:1994	arg1	phenotype					1996:2004	an aggressive metastatic phenotype	1971:2004	an aggressive metastatic phenotype	1971:2004	This class of proteins represents a new means by which HPA differentiates cancer cells with an aggressive metastatic phenotype.
22322011	6	74	theme	integrin	1214:1221	arg1	α6					1223:1224	integrin α6	1214:1224	integrin α6	1214:1224	HPA binding correlated with levels of integrin α6, transcription factors heterogeneous nuclear ribonuclear protein (HnRNP) H1, HnRNP D-like, HnRNP A2/B1 as well as heat shock protein 27 (Hsp27), glial fibrillary acidic protein and enolase 1 (ENO1).
22322011	4	75	theme	cancer	873:878	arg1	metastasis					880:889	breast cancer metastasis	866:889	breast cancer metastasis	866:889	The intriguing observations from the CFG array led to this study, in which HPA-binding epitopes were localized and characterized in an in vitro model of breast cancer metastasis.
22322011	5	76	theme	microscopy-based	1007:1022	arg1	studies					1040:1046	confocal microscopy-based co-localization studies	998:1046	confocal microscopy-based co-localization studies	998:1046	HMT3522 (benign disease), BT474 (primary cancer) and T47D/MCF7 (metastatic cancer) cells were assessed in confocal microscopy-based co-localization studies and a glycoproteomic analysis based on 2-dimensional electrophoresis (2DE), western blotting and mass spectrometry was adopted.
22322011	11	77	theme	new	1915:1917	arg1	means					1919:1923	a new means	1913:1923	a new means by which HPA differentiates cancer cells with an aggressive metastatic phenotype	1913:2004	This class of proteins represents a new means by which HPA differentiates cancer cells with an aggressive metastatic phenotype.
22322011	1	78	from	agglutinin	207:216	arg1	cancer					234:239	breast cancer	227:239	breast cancer	227:239	There has been considerable interest in understanding the epitopes that bind the lectin Helix pomatia agglutinin (HPA) in breast cancer as the lectin has been shown to identify glycosylation changes associated with the development of metastatic disease.
22322011	11	79	theme	cancer	1953:1958	arg1	cells					1960:1964	cancer cells	1953:1964	cancer cells	1953:1964	This class of proteins represents a new means by which HPA differentiates cancer cells with an aggressive metastatic phenotype.
22322011	9	80	theme	cancer	1678:1683	arg1	cells					1685:1689	the breast cancer cells	1667:1689	the breast cancer cells	1667:1689	Integrin α6 was the most abundant HPA glycoprotein in the breast cancer cells with a metastatic phenotype; this concurred with previous findings in colorectal cancer.
22322011	4	81	theme	intriguing	717:726	arg1	observations					728:739	The intriguing observations	713:739	The intriguing observations from the CFG array	713:758	The intriguing observations from the CFG array led to this study, in which HPA-binding epitopes were localized and characterized in an in vitro model of breast cancer metastasis.
22322011	7	82	gly	glycoproteins	1431:1443	arg1	glycoproteins					1431:1443	These glycoproteins	1425:1443	These glycoproteins	1425:1443	These glycoproteins were non-detectable in the non-metastatic breast cancer cell lines.
22322011	2	83	theme	Tn	503:504	arg1	epitopes					506:513	exposed Tn epitopes	495:513	exposed Tn epitopes	495:513	HPA has previously been shown to recognize aberrant O-linked α-N-acetylgalactosamine (GalNAcα)/mucin glycosylation in cancer, including exposed Tn epitopes.
22322011	6	84	theme	HPA	1176:1178	arg1	binding					1180:1186	HPA binding	1176:1186	HPA binding	1176:1186	HPA binding correlated with levels of integrin α6, transcription factors heterogeneous nuclear ribonuclear protein (HnRNP) H1, HnRNP D-like, HnRNP A2/B1 as well as heat shock protein 27 (Hsp27), glial fibrillary acidic protein and enolase 1 (ENO1).
22322011	0	85	theme	breast	90:95	arg1	cancer					97:102	human breast cancer	84:102	human breast cancer	84:102	The lectin Helix pomatia agglutinin recognizes O-GlcNAc containing glycoproteins in human breast cancer.
22322011	3	86	theme	e.g.	620:623	arg1	lectin					612:617	the lectin	608:617	the lectin	608:617	However, recent glycan-array analysis reported that diverse epitopes are also recognized by the lectin, e.g. consortium for functional glycomics (CFG) data: GalNAcα1,3Gal; β-GalNAc; GlcNAcβ1,4Gal.
22322011	3	86	theme	e.g.	620:623	arg1	consortium					625:634	e.g. consortium	620:634	e.g. consortium for functional glycomics (CFG) data	620:670	However, recent glycan-array analysis reported that diverse epitopes are also recognized by the lectin, e.g. consortium for functional glycomics (CFG) data: GalNAcα1,3Gal; β-GalNAc; GlcNAcβ1,4Gal.
22322011	9	87	theme	metastatic	1698:1707	arg1	phenotype					1709:1717	a metastatic phenotype	1696:1717	a metastatic phenotype	1696:1717	Integrin α6 was the most abundant HPA glycoprotein in the breast cancer cells with a metastatic phenotype; this concurred with previous findings in colorectal cancer.
22322011	1	88	theme	metastatic	339:348	arg1	disease					350:356	metastatic disease	339:356	metastatic disease	339:356	There has been considerable interest in understanding the epitopes that bind the lectin Helix pomatia agglutinin (HPA) in breast cancer as the lectin has been shown to identify glycosylation changes associated with the development of metastatic disease.
22322011	0	89	gly	glycoproteins	67:79	arg1	glycoproteins					67:79	O-GlcNAc containing glycoproteins	47:79	O-GlcNAc containing glycoproteins	47:79	The lectin Helix pomatia agglutinin recognizes O-GlcNAc containing glycoproteins in human breast cancer.
22322011	7	90	theme	cell	1501:1504	arg1	lines					1506:1510	the non-metastatic breast cancer cell lines	1468:1510	the non-metastatic breast cancer cell lines	1468:1510	These glycoproteins were non-detectable in the non-metastatic breast cancer cell lines.
22322011	0	91	theme	lectin	4:9	arg1	agglutinin					25:34	The lectin Helix pomatia agglutinin	0:34	The lectin Helix pomatia agglutinin	0:34	The lectin Helix pomatia agglutinin recognizes O-GlcNAc containing glycoproteins in human breast cancer.
22322011	9	92	theme	previous	1740:1747	arg1	findings					1749:1756	previous findings	1740:1756	previous findings in colorectal cancer	1740:1777	Integrin α6 was the most abundant HPA glycoprotein in the breast cancer cells with a metastatic phenotype; this concurred with previous findings in colorectal cancer.
22322011	0	93	theme	pomatia	17:23	arg1	agglutinin					25:34	The lectin Helix pomatia agglutinin	0:34	The lectin Helix pomatia agglutinin	0:34	The lectin Helix pomatia agglutinin recognizes O-GlcNAc containing glycoproteins in human breast cancer.
22322011	4	94	theme	CFG	750:752	arg1	array					754:758	the CFG array	746:758	the CFG array	746:758	The intriguing observations from the CFG array led to this study, in which HPA-binding epitopes were localized and characterized in an in vitro model of breast cancer metastasis.
22322011	2	95	theme	O-linked	411:418	arg1	glycosylation					460:472	aberrant O-linked α-N-acetylgalactosamine (GalNAcα)/mucin glycosylation	402:472	aberrant O-linked α-N-acetylgalactosamine (GalNAcα)/mucin glycosylation	402:472	HPA has previously been shown to recognize aberrant O-linked α-N-acetylgalactosamine (GalNAcα)/mucin glycosylation in cancer, including exposed Tn epitopes.
22322011	7	96	theme	cancer	1494:1499	arg1	lines					1506:1510	the non-metastatic breast cancer cell lines	1468:1510	the non-metastatic breast cancer cell lines	1468:1510	These glycoproteins were non-detectable in the non-metastatic breast cancer cell lines.
22322011	3	97	theme	functional	640:649	arg1	data					667:670	functional glycomics (CFG) data	640:670	functional glycomics (CFG) data	640:670	However, recent glycan-array analysis reported that diverse epitopes are also recognized by the lectin, e.g. consortium for functional glycomics (CFG) data: GalNAcα1,3Gal; β-GalNAc; GlcNAcβ1,4Gal.
22322011	0	98	theme	containing	56:65	arg1	glycoproteins					67:79	O-GlcNAc containing glycoproteins	47:79	O-GlcNAc containing glycoproteins	47:79	The lectin Helix pomatia agglutinin recognizes O-GlcNAc containing glycoproteins in human breast cancer.
22322011	7	99	theme	non-metastatic	1472:1485	arg1	lines					1506:1510	the non-metastatic breast cancer cell lines	1468:1510	the non-metastatic breast cancer cell lines	1468:1510	These glycoproteins were non-detectable in the non-metastatic breast cancer cell lines.
22322011	2	100	gly	glycosylation	460:472	arg1	cancer					477:482	cancer	477:482	cancer	477:482	HPA has previously been shown to recognize aberrant O-linked α-N-acetylgalactosamine (GalNAcα)/mucin glycosylation in cancer, including exposed Tn epitopes.
22322011	5	101	theme	mass	1145:1148	arg1	spectrometry					1150:1161	mass spectrometry	1145:1161	mass spectrometry	1145:1161	HMT3522 (benign disease), BT474 (primary cancer) and T47D/MCF7 (metastatic cancer) cells were assessed in confocal microscopy-based co-localization studies and a glycoproteomic analysis based on 2-dimensional electrophoresis (2DE), western blotting and mass spectrometry was adopted.
22322011	11	102	theme	proteins	1893:1900	arg1	class					1884:1888	This class	1879:1888	This class of proteins	1879:1900	This class of proteins represents a new means by which HPA differentiates cancer cells with an aggressive metastatic phenotype.
22322011	3	103	theme	recent	525:530	arg1	analysis					545:552	recent glycan-array analysis	525:552	recent glycan-array analysis	525:552	However, recent glycan-array analysis reported that diverse epitopes are also recognized by the lectin, e.g. consortium for functional glycomics (CFG) data: GalNAcα1,3Gal; β-GalNAc; GlcNAcβ1,4Gal.
22322011	4	104	located	localized	814:822	arg2	epitopes					800:807	HPA-binding epitopes	788:807	HPA-binding epitopes	788:807	The intriguing observations from the CFG array led to this study, in which HPA-binding epitopes were localized and characterized in an in vitro model of breast cancer metastasis.
22322011	4	104	located	localized	814:822	arg1	study					772:776	this study	767:776	this study	767:776	The intriguing observations from the CFG array led to this study, in which HPA-binding epitopes were localized and characterized in an in vitro model of breast cancer metastasis.
22322011	4	105	dep	in	848:849	arg1	vitro					851:855	vitro	851:855	vitro	851:855	The intriguing observations from the CFG array led to this study, in which HPA-binding epitopes were localized and characterized in an in vitro model of breast cancer metastasis.
34845374	0	0	theme	colorectal	85:94	arg1	cancer					96:101	colorectal cancer	85:101	colorectal cancer	85:101	Thymidylate synthase O-GlcNAcylation: a molecular mechanism of 5-FU sensitization in colorectal cancer.
34845374	8	1	theme	non-cancerous	840:852	arg1	cells					874:878	non-cancerous and cancerous colon cells	840:878	non-cancerous and cancerous colon cells	840:878	In vitro in non-cancerous and cancerous colon cells, we showed that 5-FU impacts O-GlcNAcylation by decreasing O-GlcNAc Transferase (OGT) expression both at mRNA and protein levels.
34845374	7	2	theme	decreased	721:729	arg1	O-GlcNAcylation					731:745	5-FU decreased O-GlcNAcylation	716:745	5-FU decreased O-GlcNAcylation	716:745	5-FU decreased O-GlcNAcylation and, reciprocally, elevation of O-GlcNAcylation was associated with TS increase.
34845374	11	3	theme	5-FU	1396:1399	arg1	sensitization					1405:1417	5-FU CRC sensitization	1396:1417	5-FU CRC sensitization	1396:1417	We reveal a crosstalk between O-GlcNAcylation and 5-FU metabolism in vitro and in vivo that converges to 5-FU CRC sensitization by stabilizing TS.
34845374	12	4	theme	5-FU-based	1479:1488	arg1	chemotherapy					1490:1501	5-FU-based chemotherapy	1479:1501	5-FU-based chemotherapy	1479:1501	Overall, our data propose that combining 5-FU-based chemotherapy with Thiamet-G could be a new way to enhance CRC response to 5-FU.
34845374	6	5	theme	OGA	622:624	arg1	5-FU					588:591	5-FU	588:591	combined 5-FU with Thiamet-G (O-GlcNAcase (OGA) inhibitor) treatment	579:646	In vivo, we observed that combined 5-FU with Thiamet-G (O-GlcNAcase (OGA) inhibitor) treatment had a synergistic inhibitory effect on grade and tumor progression.
34845374	6	5	theme	OGA	622:624	arg1	inhibitor					627:635	O-GlcNAcase (OGA) inhibitor	609:635	O-GlcNAcase (OGA) inhibitor	609:635	In vivo, we observed that combined 5-FU with Thiamet-G (O-GlcNAcase (OGA) inhibitor) treatment had a synergistic inhibitory effect on grade and tumor progression.
34845374	8	6	theme	cancerous	858:866	arg1	cells					874:878	non-cancerous and cancerous colon cells	840:878	non-cancerous and cancerous colon cells	840:878	In vitro in non-cancerous and cancerous colon cells, we showed that 5-FU impacts O-GlcNAcylation by decreasing O-GlcNAc Transferase (OGT) expression both at mRNA and protein levels.
34845374	11	7	theme	CRC	1401:1403	arg1	sensitization					1405:1417	5-FU CRC sensitization	1396:1417	5-FU CRC sensitization	1396:1417	We reveal a crosstalk between O-GlcNAcylation and 5-FU metabolism in vitro and in vivo that converges to 5-FU CRC sensitization by stabilizing TS.
34845374	7	8	theme	5-FU	716:719	arg1	O-GlcNAcylation					731:745	5-FU decreased O-GlcNAcylation	716:745	5-FU decreased O-GlcNAcylation	716:745	5-FU decreased O-GlcNAcylation and, reciprocally, elevation of O-GlcNAcylation was associated with TS increase.
34845374	0	9	from	mechanism	50:58	arg1	cancer					96:101	colorectal cancer	85:101	colorectal cancer	85:101	Thymidylate synthase O-GlcNAcylation: a molecular mechanism of 5-FU sensitization in colorectal cancer.
34845374	4	10	theme	TS	404:405	arg1	O-GlcNAcylation					407:421	TS O-GlcNAcylation	404:421	TS O-GlcNAcylation	404:421	TS O-GlcNAcylation was reported but not investigated yet.
34845374	2	11	from	role	237:240	arg1	response					258:265	chemotherapy response	245:265	chemotherapy response	245:265	Its role in chemotherapy response is poorly investigated.
34845374	12	12	theme	CRC	1548:1550	arg1	response					1552:1559	CRC response	1548:1559	CRC response to 5-FU	1548:1567	Overall, our data propose that combining 5-FU-based chemotherapy with Thiamet-G could be a new way to enhance CRC response to 5-FU.
34845374	6	13	theme	5-FU	588:591	arg1	treatment					638:646	combined 5-FU with Thiamet-G (O-GlcNAcase (OGA) inhibitor) treatment	579:646	combined 5-FU with Thiamet-G (O-GlcNAcase (OGA) inhibitor) treatment	579:646	In vivo, we observed that combined 5-FU with Thiamet-G (O-GlcNAcase (OGA) inhibitor) treatment had a synergistic inhibitory effect on grade and tumor progression.
34845374	10	14	from	role	1255:1258	arg1	degradation					1278:1288	TS proteasomal degradation	1263:1288	TS proteasomal degradation	1263:1288	Mass spectrometry, mutagenesis and structural studies mapped O-GlcNAcylated sites on T251 and T306 residues and deciphered their role in TS proteasomal degradation.
34845374	5	15	theme	CRC	519:521	arg1	sensitivity					523:533	5-FU CRC sensitivity	514:533	5-FU CRC sensitivity	514:533	We hypothesize that O-GlcNAcylation interferes with 5-FU CRC sensitivity by regulating TS.
34845374	0	16	theme	synthase	12:19	arg1	O-GlcNAcylation					21:35	Thymidylate synthase O-GlcNAcylation	0:35	Thymidylate synthase O-GlcNAcylation: a molecular mechanism of 5-FU sensitization in colorectal cancer.	0:102	Thymidylate synthase O-GlcNAcylation: a molecular mechanism of 5-FU sensitization in colorectal cancer.
34845374	10	17	theme	Mass	1126:1129	arg1	spectrometry					1131:1142	Mass spectrometry	1126:1142	Mass spectrometry	1126:1142	Mass spectrometry, mutagenesis and structural studies mapped O-GlcNAcylated sites on T251 and T306 residues and deciphered their role in TS proteasomal degradation.
34845374	8	18	theme	protein	994:1000	arg1	levels					1002:1007	mRNA and protein levels	985:1007	mRNA and protein levels	985:1007	In vitro in non-cancerous and cancerous colon cells, we showed that 5-FU impacts O-GlcNAcylation by decreasing O-GlcNAc Transferase (OGT) expression both at mRNA and protein levels.
34845374	9	19	theme	protein	1098:1104	arg1	level					1106:1110	TS protein level	1095:1110	TS protein level	1095:1110	Reciprocally, OGT knockdown decreased 5-FU-induced cancer cell apoptosis by reducing TS protein level and activity.
34845374	9	20	theme	cancer	1061:1066	arg1	apoptosis					1073:1081	5-FU-induced cancer cell apoptosis	1048:1081	5-FU-induced cancer cell apoptosis	1048:1081	Reciprocally, OGT knockdown decreased 5-FU-induced cancer cell apoptosis by reducing TS protein level and activity.
34845374	0	21	theme	Thymidylate	0:10	arg1	O-GlcNAcylation					21:35	Thymidylate synthase O-GlcNAcylation	0:35	Thymidylate synthase O-GlcNAcylation: a molecular mechanism of 5-FU sensitization in colorectal cancer.	0:102	Thymidylate synthase O-GlcNAcylation: a molecular mechanism of 5-FU sensitization in colorectal cancer.
34845374	7	22	theme	TS	815:816	arg1	increase					818:825	TS increase	815:825	TS increase	815:825	5-FU decreased O-GlcNAcylation and, reciprocally, elevation of O-GlcNAcylation was associated with TS increase.
34845374	9	23	theme	TS	1095:1096	arg1	level					1106:1110	TS protein level	1095:1110	TS protein level	1095:1110	Reciprocally, OGT knockdown decreased 5-FU-induced cancer cell apoptosis by reducing TS protein level and activity.
34845374	6	24	with	5-FU	588:591	arg1	Thiamet-G					598:606	Thiamet-G	598:606	Thiamet-G	598:606	In vivo, we observed that combined 5-FU with Thiamet-G (O-GlcNAcase (OGA) inhibitor) treatment had a synergistic inhibitory effect on grade and tumor progression.
34845374	3	25	theme	Thymidylate	377:387	arg1	TS					399:400	TS	399:400	TS	399:400	Standard treatment for colorectal cancer (CRC), 5-fluorouracil (5-FU), mainly targets Thymidylate Synthase (TS).
34845374	3	25	theme	Thymidylate	377:387	arg1	Synthase					389:396	Thymidylate Synthase	377:396	Thymidylate Synthase (TS)	377:401	Standard treatment for colorectal cancer (CRC), 5-fluorouracil (5-FU), mainly targets Thymidylate Synthase (TS).
34845374	10	26	from	sites	1202:1206	arg1	T306					1220:1223	T306	1220:1223	T306	1220:1223	Mass spectrometry, mutagenesis and structural studies mapped O-GlcNAcylated sites on T251 and T306 residues and deciphered their role in TS proteasomal degradation.
34845374	10	26	from	sites	1202:1206	arg1	T251					1211:1214	T251	1211:1214	T251	1211:1214	Mass spectrometry, mutagenesis and structural studies mapped O-GlcNAcylated sites on T251 and T306 residues and deciphered their role in TS proteasomal degradation.
34845374	8	27	theme	mRNA	985:988	arg1	levels					1002:1007	mRNA and protein levels	985:1007	mRNA and protein levels	985:1007	In vitro in non-cancerous and cancerous colon cells, we showed that 5-FU impacts O-GlcNAcylation by decreasing O-GlcNAc Transferase (OGT) expression both at mRNA and protein levels.
34845374	1	28	theme	tumor	214:218	arg1	progression					220:230	tumor progression	214:230	tumor progression	214:230	Alteration of O-GlcNAcylation, a dynamic posttranslational modification, is associated with tumorigenesis and tumor progression.
34845374	3	29	theme	colorectal	314:323	arg1	CRC					333:335	CRC	333:335	CRC	333:335	Standard treatment for colorectal cancer (CRC), 5-fluorouracil (5-FU), mainly targets Thymidylate Synthase (TS).
34845374	3	29	theme	colorectal	314:323	arg1	5-fluorouracil					339:352	5-fluorouracil	339:352	5-fluorouracil (5-FU)	339:359	Standard treatment for colorectal cancer (CRC), 5-fluorouracil (5-FU), mainly targets Thymidylate Synthase (TS).
34845374	3	29	theme	colorectal	314:323	arg1	cancer					325:330	colorectal cancer	314:330	colorectal cancer (CRC)	314:336	Standard treatment for colorectal cancer (CRC), 5-fluorouracil (5-FU), mainly targets Thymidylate Synthase (TS).
34845374	6	30	theme	inhibitory	666:675	arg1	effect					677:682	a synergistic inhibitory effect	652:682	a synergistic inhibitory effect	652:682	In vivo, we observed that combined 5-FU with Thiamet-G (O-GlcNAcase (OGA) inhibitor) treatment had a synergistic inhibitory effect on grade and tumor progression.
34845374	0	31	theme	molecular	40:48	arg1	mechanism					50:58	a molecular mechanism	38:58	Thymidylate synthase O-GlcNAcylation: a molecular mechanism of 5-FU sensitization in colorectal cancer.	0:102	Thymidylate synthase O-GlcNAcylation: a molecular mechanism of 5-FU sensitization in colorectal cancer.
34845374	6	32	theme	tumor	697:701	arg1	progression					703:713	tumor progression	697:713	tumor progression	697:713	In vivo, we observed that combined 5-FU with Thiamet-G (O-GlcNAcase (OGA) inhibitor) treatment had a synergistic inhibitory effect on grade and tumor progression.
34845374	3	33	theme	Standard	291:298	arg1	treatment					300:308	Standard treatment	291:308	Standard treatment for colorectal cancer (CRC), 5-fluorouracil (5-FU),	291:360	Standard treatment for colorectal cancer (CRC), 5-fluorouracil (5-FU), mainly targets Thymidylate Synthase (TS).
34845374	8	34	theme	colon	868:872	arg1	cells					874:878	non-cancerous and cancerous colon cells	840:878	non-cancerous and cancerous colon cells	840:878	In vitro in non-cancerous and cancerous colon cells, we showed that 5-FU impacts O-GlcNAcylation by decreasing O-GlcNAc Transferase (OGT) expression both at mRNA and protein levels.
34845374	9	35	theme	cell	1068:1071	arg1	apoptosis					1073:1081	5-FU-induced cancer cell apoptosis	1048:1081	5-FU-induced cancer cell apoptosis	1048:1081	Reciprocally, OGT knockdown decreased 5-FU-induced cancer cell apoptosis by reducing TS protein level and activity.
34845374	6	36	theme	synergistic	654:664	arg1	effect					677:682	a synergistic inhibitory effect	652:682	a synergistic inhibitory effect	652:682	In vivo, we observed that combined 5-FU with Thiamet-G (O-GlcNAcase (OGA) inhibitor) treatment had a synergistic inhibitory effect on grade and tumor progression.
34845374	6	37	theme	combined	579:586	arg1	treatment					638:646	combined 5-FU with Thiamet-G (O-GlcNAcase (OGA) inhibitor) treatment	579:646	combined 5-FU with Thiamet-G (O-GlcNAcase (OGA) inhibitor) treatment	579:646	In vivo, we observed that combined 5-FU with Thiamet-G (O-GlcNAcase (OGA) inhibitor) treatment had a synergistic inhibitory effect on grade and tumor progression.
34845374	7	38	theme	O-GlcNAcylation	779:793	arg1	elevation					766:774	elevation	766:774	elevation of O-GlcNAcylation	766:793	5-FU decreased O-GlcNAcylation and, reciprocally, elevation of O-GlcNAcylation was associated with TS increase.
34845374	7	38	theme	O-GlcNAcylation	779:793	arg1	O-GlcNAcylation					731:745	5-FU decreased O-GlcNAcylation	716:745	5-FU decreased O-GlcNAcylation	716:745	5-FU decreased O-GlcNAcylation and, reciprocally, elevation of O-GlcNAcylation was associated with TS increase.
34845374	11	39	dep	O-GlcNAcylation	1321:1335	arg1	metabolism					1346:1355	metabolism	1346:1355	metabolism	1346:1355	We reveal a crosstalk between O-GlcNAcylation and 5-FU metabolism in vitro and in vivo that converges to 5-FU CRC sensitization by stabilizing TS.
34845374	2	40	theme	chemotherapy	245:256	arg1	response					258:265	chemotherapy response	245:265	chemotherapy response	245:265	Its role in chemotherapy response is poorly investigated.
34845374	12	41	theme	new	1529:1531	arg1	way					1533:1535	a new way	1527:1535	a new way to enhance CRC response to 5-FU	1527:1567	Overall, our data propose that combining 5-FU-based chemotherapy with Thiamet-G could be a new way to enhance CRC response to 5-FU.
34845374	1	42	theme	O-GlcNAcylation	118:132	arg1	Alteration					104:113	Alteration	104:113	Alteration of O-GlcNAcylation, a dynamic posttranslational modification,	104:175	Alteration of O-GlcNAcylation, a dynamic posttranslational modification, is associated with tumorigenesis and tumor progression.
34845374	10	43	theme	structural	1161:1170	arg1	studies					1172:1178	structural studies	1161:1178	structural studies	1161:1178	Mass spectrometry, mutagenesis and structural studies mapped O-GlcNAcylated sites on T251 and T306 residues and deciphered their role in TS proteasomal degradation.
34845374	5	44	theme	5-FU	514:517	arg1	sensitivity					523:533	5-FU CRC sensitivity	514:533	5-FU CRC sensitivity	514:533	We hypothesize that O-GlcNAcylation interferes with 5-FU CRC sensitivity by regulating TS.
34845374	8	45	theme	Transferase	948:958	arg1	expression					966:975	O-GlcNAc Transferase (OGT) expression	939:975	O-GlcNAc Transferase (OGT) expression	939:975	In vitro in non-cancerous and cancerous colon cells, we showed that 5-FU impacts O-GlcNAcylation by decreasing O-GlcNAc Transferase (OGT) expression both at mRNA and protein levels.
34845374	8	46	theme	O-GlcNAc	939:946	arg1	OGT					961:963	OGT	961:963	OGT	961:963	In vitro in non-cancerous and cancerous colon cells, we showed that 5-FU impacts O-GlcNAcylation by decreasing O-GlcNAc Transferase (OGT) expression both at mRNA and protein levels.
34845374	8	46	theme	O-GlcNAc	939:946	arg1	Transferase					948:958	O-GlcNAc Transferase	939:958	O-GlcNAc Transferase (OGT) expression	939:975	In vitro in non-cancerous and cancerous colon cells, we showed that 5-FU impacts O-GlcNAcylation by decreasing O-GlcNAc Transferase (OGT) expression both at mRNA and protein levels.
34845374	9	47	theme	OGT	1024:1026	arg1	knockdown					1028:1036	OGT knockdown	1024:1036	OGT knockdown	1024:1036	Reciprocally, OGT knockdown decreased 5-FU-induced cancer cell apoptosis by reducing TS protein level and activity.
34845374	10	48	theme	proteasomal	1266:1276	arg1	degradation					1278:1288	TS proteasomal degradation	1263:1288	TS proteasomal degradation	1263:1288	Mass spectrometry, mutagenesis and structural studies mapped O-GlcNAcylated sites on T251 and T306 residues and deciphered their role in TS proteasomal degradation.
34845374	10	49	dep	T251	1211:1214	arg1	residues					1225:1232	residues	1225:1232	residues	1225:1232	Mass spectrometry, mutagenesis and structural studies mapped O-GlcNAcylated sites on T251 and T306 residues and deciphered their role in TS proteasomal degradation.
34845374	0	50	dep	O-GlcNAcylation	21:35	arg1	mechanism					50:58	a molecular mechanism	38:58	Thymidylate synthase O-GlcNAcylation: a molecular mechanism of 5-FU sensitization in colorectal cancer.	0:102	Thymidylate synthase O-GlcNAcylation: a molecular mechanism of 5-FU sensitization in colorectal cancer.
34845374	1	51	theme	dynamic	137:143	arg1	modification					163:174	a dynamic posttranslational modification	135:174	a dynamic posttranslational modification	135:174	Alteration of O-GlcNAcylation, a dynamic posttranslational modification, is associated with tumorigenesis and tumor progression.
34845374	1	51	theme	dynamic	137:143	arg1	O-GlcNAcylation					118:132	O-GlcNAcylation	118:132	O-GlcNAcylation	118:132	Alteration of O-GlcNAcylation, a dynamic posttranslational modification, is associated with tumorigenesis and tumor progression.
34845374	8	52	dep	levels	1002:1007	arg1	both					977:980	both	977:980	both	977:980	In vitro in non-cancerous and cancerous colon cells, we showed that 5-FU impacts O-GlcNAcylation by decreasing O-GlcNAc Transferase (OGT) expression both at mRNA and protein levels.
34845374	0	53	theme	sensitization	68:80	arg1	mechanism					50:58	a molecular mechanism	38:58	Thymidylate synthase O-GlcNAcylation: a molecular mechanism of 5-FU sensitization in colorectal cancer.	0:102	Thymidylate synthase O-GlcNAcylation: a molecular mechanism of 5-FU sensitization in colorectal cancer.
34845374	10	54	theme	TS	1263:1264	arg1	degradation					1278:1288	TS proteasomal degradation	1263:1288	TS proteasomal degradation	1263:1288	Mass spectrometry, mutagenesis and structural studies mapped O-GlcNAcylated sites on T251 and T306 residues and deciphered their role in TS proteasomal degradation.
34845374	1	55	theme	posttranslational	145:161	arg1	modification					163:174	a dynamic posttranslational modification	135:174	a dynamic posttranslational modification	135:174	Alteration of O-GlcNAcylation, a dynamic posttranslational modification, is associated with tumorigenesis and tumor progression.
34845374	1	55	theme	posttranslational	145:161	arg1	O-GlcNAcylation					118:132	O-GlcNAcylation	118:132	O-GlcNAcylation	118:132	Alteration of O-GlcNAcylation, a dynamic posttranslational modification, is associated with tumorigenesis and tumor progression.
34845374	0	56	theme	5-FU	63:66	arg1	sensitization					68:80	5-FU sensitization	63:80	5-FU sensitization	63:80	Thymidylate synthase O-GlcNAcylation: a molecular mechanism of 5-FU sensitization in colorectal cancer.
34845374	6	57	contain	had	648:650	arg1	treatment					638:646	combined 5-FU with Thiamet-G (O-GlcNAcase (OGA) inhibitor) treatment	579:646	combined 5-FU with Thiamet-G (O-GlcNAcase (OGA) inhibitor) treatment	579:646	In vivo, we observed that combined 5-FU with Thiamet-G (O-GlcNAcase (OGA) inhibitor) treatment had a synergistic inhibitory effect on grade and tumor progression.
34845374	6	57	contain	had	648:650	arg2	effect					677:682	a synergistic inhibitory effect	652:682	a synergistic inhibitory effect	652:682	In vivo, we observed that combined 5-FU with Thiamet-G (O-GlcNAcase (OGA) inhibitor) treatment had a synergistic inhibitory effect on grade and tumor progression.
34845374	6	58	theme	O-GlcNAcase	609:619	arg1	5-FU					588:591	5-FU	588:591	combined 5-FU with Thiamet-G (O-GlcNAcase (OGA) inhibitor) treatment	579:646	In vivo, we observed that combined 5-FU with Thiamet-G (O-GlcNAcase (OGA) inhibitor) treatment had a synergistic inhibitory effect on grade and tumor progression.
34845374	6	58	theme	O-GlcNAcase	609:619	arg1	inhibitor					627:635	O-GlcNAcase (OGA) inhibitor	609:635	O-GlcNAcase (OGA) inhibitor	609:635	In vivo, we observed that combined 5-FU with Thiamet-G (O-GlcNAcase (OGA) inhibitor) treatment had a synergistic inhibitory effect on grade and tumor progression.
34845374	9	59	theme	5-FU-induced	1048:1059	arg1	apoptosis					1073:1081	5-FU-induced cancer cell apoptosis	1048:1081	5-FU-induced cancer cell apoptosis	1048:1081	Reciprocally, OGT knockdown decreased 5-FU-induced cancer cell apoptosis by reducing TS protein level and activity.
34845374	10	60	theme	O-GlcNAcylated	1187:1200	arg1	sites					1202:1206	O-GlcNAcylated sites	1187:1206	O-GlcNAcylated sites on T251 and T306 residues	1187:1232	Mass spectrometry, mutagenesis and structural studies mapped O-GlcNAcylated sites on T251 and T306 residues and deciphered their role in TS proteasomal degradation.
29084613	4	0	theme	mouse	778:782	arg1	mESCs					806:810	mESCs	806:810	mESCs	806:810	In this study, by considering the similarity between the S40-type H2A and histone H2A variants, we explored the function of H2AS40Gc in mouse embryonic stem cells (mESCs).
29084613	4	0	theme	mouse	778:782	arg1	cells					799:803	mouse embryonic stem cells	778:803	mouse embryonic stem cells (mESCs)	778:811	In this study, by considering the similarity between the S40-type H2A and histone H2A variants, we explored the function of H2AS40Gc in mouse embryonic stem cells (mESCs).
29084613	12	1	from	experiment	1919:1928	arg1	mESCs					1952:1956	WT and S40A-mutant mESCs	1933:1956	WT and S40A-mutant mESCs	1933:1956	Co-immunoprecipitation experiment in WT and S40A-mutant mESCs revealed that H2AS40Gc physiologically bound to AcH2AZ at the initial phase upon DNA damage, followed by binding with γH2AX during the DNA damage repair process.
29084613	4	2	theme	stem	794:797	arg1	mESCs					806:810	mESCs	806:810	mESCs	806:810	In this study, by considering the similarity between the S40-type H2A and histone H2A variants, we explored the function of H2AS40Gc in mouse embryonic stem cells (mESCs).
29084613	4	2	theme	stem	794:797	arg1	cells					799:803	mouse embryonic stem cells	778:803	mouse embryonic stem cells (mESCs)	778:811	In this study, by considering the similarity between the S40-type H2A and histone H2A variants, we explored the function of H2AS40Gc in mouse embryonic stem cells (mESCs).
29084613	3	3	theme	globular	510:517	arg1	portion					561:567	a variable portion	550:567	a variable portion that distinguishes between the canonical and non-canonical H2A variants	550:639	H2A isoforms are consisted of S40 and alanine 40 (A40) type and this residue on H2A is located in the L1 of the globular domain, which is also known as a variable portion that distinguishes between the canonical and non-canonical H2A variants.
29084613	3	3	theme	globular	510:517	arg1	domain					519:524	the globular domain	506:524	the globular domain	506:524	H2A isoforms are consisted of S40 and alanine 40 (A40) type and this residue on H2A is located in the L1 of the globular domain, which is also known as a variable portion that distinguishes between the canonical and non-canonical H2A variants.
29084613	3	4	from	residue	467:473	arg1	H2A					478:480	H2A	478:480	H2A	478:480	H2A isoforms are consisted of S40 and alanine 40 (A40) type and this residue on H2A is located in the L1 of the globular domain, which is also known as a variable portion that distinguishes between the canonical and non-canonical H2A variants.
29084613	9	5	theme	A40	1456:1458	arg1	mutation					1460:1467	the S40 to A40 mutation	1445:1467	the S40 to A40 mutation (S40A-mutant)	1445:1481	Overexpression of the wild-type (WT) H2A3, but not the S40 to A40 mutation (S40A-mutant), protected the mESC genome against chemical-induced DNA damage.
29084613	9	5	theme	A40	1456:1458	arg1	S40A-mutant					1470:1480	S40A-mutant	1470:1480	S40A-mutant	1470:1480	Overexpression of the wild-type (WT) H2A3, but not the S40 to A40 mutation (S40A-mutant), protected the mESC genome against chemical-induced DNA damage.
29084613	2	6	theme	susceptible	237:247	arg1	isoforms					228:235	S40-type H2A isoforms	215:235	S40-type H2A isoforms susceptible to O-GlcNAcylation	215:266	S40-type H2A isoforms susceptible to O-GlcNAcylation are evolutionarily new and restricted to the viviparous animals; however, the biological function of H2AS40Gc is largely unknown.
29084613	4	7	theme	H2AS40Gc	766:773	arg1	function					754:761	the function	750:761	the function of H2AS40Gc	750:773	In this study, by considering the similarity between the S40-type H2A and histone H2A variants, we explored the function of H2AS40Gc in mouse embryonic stem cells (mESCs).
29084613	3	8	theme	domain	519:524	arg1	L1					500:501	the L1	496:501	the L1 of the globular domain, which is also known as a variable portion that distinguishes between the canonical and non-canonical H2A variants	496:639	H2A isoforms are consisted of S40 and alanine 40 (A40) type and this residue on H2A is located in the L1 of the globular domain, which is also known as a variable portion that distinguishes between the canonical and non-canonical H2A variants.
29084613	13	9	dep	CONCLUSIONS	2120:2130	arg1	suggest					2143:2149	suggest	2143:2149	suggest that H2AS40Gc functions to maintain genome integrity through the DNA repair mechanism in association with AcH2AZ and γH2AX	2143:2272	CONCLUSIONS These data suggest that H2AS40Gc functions to maintain genome integrity through the DNA repair mechanism in association with AcH2AZ and γH2AX.
29084613	10	10	from	mESCs	1696:1700	arg1	advanced					1660:1667	advanced	1660:1667	advanced	1660:1667	Furthermore, 3 h after the DNA damage treatment, the genome was almost recovered in WT mESCs, whereas the damage advanced further in the S40A-mutant mESCs, suggesting functions of H2AS40Gc in the DNA repair mechanism.
29084613	12	11	theme	Co-immunoprecipitation	1896:1917	arg1	experiment					1919:1928	Co-immunoprecipitation experiment	1896:1928	Co-immunoprecipitation experiment in WT and S40A-mutant mESCs	1896:1956	Co-immunoprecipitation experiment in WT and S40A-mutant mESCs revealed that H2AS40Gc physiologically bound to AcH2AZ at the initial phase upon DNA damage, followed by binding with γH2AX during the DNA damage repair process.
29084613	9	12	theme	mESC	1498:1501	arg1	genome					1503:1508	the mESC genome	1494:1508	the mESC genome	1494:1508	Overexpression of the wild-type (WT) H2A3, but not the S40 to A40 mutation (S40A-mutant), protected the mESC genome against chemical-induced DNA damage.
29084613	12	13	theme	damage	2097:2102	arg1	repair					2104:2109	DNA damage repair	2093:2109	the DNA damage repair process	2089:2117	Co-immunoprecipitation experiment in WT and S40A-mutant mESCs revealed that H2AS40Gc physiologically bound to AcH2AZ at the initial phase upon DNA damage, followed by binding with γH2AX during the DNA damage repair process.
29084613	10	14	theme	DNA	1743:1745	arg1	mechanism					1754:1762	the DNA repair mechanism	1739:1762	the DNA repair mechanism	1739:1762	Furthermore, 3 h after the DNA damage treatment, the genome was almost recovered in WT mESCs, whereas the damage advanced further in the S40A-mutant mESCs, suggesting functions of H2AS40Gc in the DNA repair mechanism.
29084613	10	15	theme	DNA	1574:1576	arg1	damage					1578:1583	the DNA damage	1570:1583	the DNA damage treatment	1570:1593	Furthermore, 3 h after the DNA damage treatment, the genome was almost recovered in WT mESCs, whereas the damage advanced further in the S40A-mutant mESCs, suggesting functions of H2AS40Gc in the DNA repair mechanism.
29084613	9	16	theme	S40	1449:1451	arg1	mutation					1460:1467	the S40 to A40 mutation	1445:1467	the S40 to A40 mutation (S40A-mutant)	1445:1481	Overexpression of the wild-type (WT) H2A3, but not the S40 to A40 mutation (S40A-mutant), protected the mESC genome against chemical-induced DNA damage.
29084613	9	16	theme	S40	1449:1451	arg1	S40A-mutant					1470:1480	S40A-mutant	1470:1480	S40A-mutant	1470:1480	Overexpression of the wild-type (WT) H2A3, but not the S40 to A40 mutation (S40A-mutant), protected the mESC genome against chemical-induced DNA damage.
29084613	11	17	theme	repair	1832:1837	arg1	Rad51					1870:1874	Rad51	1870:1874	Rad51	1870:1874	Furthermore, the S40A mutant prevented the accumulation of the DNA repair apparatus such as DNA-PKcs and Rad51 at the damage site.
29084613	11	17	theme	repair	1832:1837	arg1	apparatus					1839:1847	the DNA repair apparatus	1824:1847	the DNA repair apparatus such as DNA-PKcs and Rad51	1824:1874	Furthermore, the S40A mutant prevented the accumulation of the DNA repair apparatus such as DNA-PKcs and Rad51 at the damage site.
29084613	11	17	theme	repair	1832:1837	arg1	DNA-PKcs					1857:1864	DNA-PKcs	1857:1864	DNA-PKcs	1857:1864	Furthermore, the S40A mutant prevented the accumulation of the DNA repair apparatus such as DNA-PKcs and Rad51 at the damage site.
29084613	8	18	theme	damage	1285:1290	arg1	± 1.5 kb					1268:1275	± 1.5 kb	1268:1275	± 1.5 kb	1268:1275	H2AS40Gc was accumulated at the restricted area (± 1.5 kb) of DNA damage sites induced by CRISPR/CAS9 system in contrast to accumulation of γH2AX, which was widely scattered.
29084613	8	18	theme	damage	1285:1290	arg1	area					1262:1265	the restricted area	1247:1265	the restricted area (± 1.5 kb) of DNA damage sites induced by CRISPR/CAS9 system in contrast to accumulation of γH2AX, which was widely scattered	1247:1391	H2AS40Gc was accumulated at the restricted area (± 1.5 kb) of DNA damage sites induced by CRISPR/CAS9 system in contrast to accumulation of γH2AX, which was widely scattered.
29084613	7	19	theme	acetylated	1193:1202	arg1	AcH2AZ					1210:1215	AcH2AZ	1210:1215	AcH2AZ	1210:1215	Importantly, H2AS40Gc level increased owing to chemical-induced DNA damage, similar to phosphorylated H2AX (γH2AX) and acetylated H2AZ (AcH2AZ).
29084613	7	19	theme	acetylated	1193:1202	arg1	H2AZ					1204:1207	acetylated H2AZ	1193:1207	acetylated H2AZ (AcH2AZ)	1193:1216	Importantly, H2AS40Gc level increased owing to chemical-induced DNA damage, similar to phosphorylated H2AX (γH2AX) and acetylated H2AZ (AcH2AZ).
29084613	3	20	from	L1	500:501	arg1	located					485:491	located	485:491	located	485:491	H2A isoforms are consisted of S40 and alanine 40 (A40) type and this residue on H2A is located in the L1 of the globular domain, which is also known as a variable portion that distinguishes between the canonical and non-canonical H2A variants.
29084613	2	21	theme	H2A	224:226	arg1	isoforms					228:235	S40-type H2A isoforms	215:235	S40-type H2A isoforms susceptible to O-GlcNAcylation	215:266	S40-type H2A isoforms susceptible to O-GlcNAcylation are evolutionarily new and restricted to the viviparous animals; however, the biological function of H2AS40Gc is largely unknown.
29084613	1	22	from	serine	180:185	arg1	modification					164:175	a novel O-GlcNAc modification	147:175	a novel O-GlcNAc modification at serine 40 (S40) of H2A (H2AS40Gc)	147:212	BACKGROUND We have previously reported a novel O-GlcNAc modification at serine 40 (S40) of H2A (H2AS40Gc).
29084613	9	23	theme	DNA	1535:1537	arg1	damage					1539:1544	chemical-induced DNA damage	1518:1544	chemical-induced DNA damage	1518:1544	Overexpression of the wild-type (WT) H2A3, but not the S40 to A40 mutation (S40A-mutant), protected the mESC genome against chemical-induced DNA damage.
29084613	7	24	theme	similar	1150:1156	arg1	damage					1142:1147	chemical-induced DNA damage	1121:1147	chemical-induced DNA damage	1121:1147	Importantly, H2AS40Gc level increased owing to chemical-induced DNA damage, similar to phosphorylated H2AX (γH2AX) and acetylated H2AZ (AcH2AZ).
29084613	13	25	from	mechanism	2227:2235	arg1	association					2240:2250	association	2240:2250	association with AcH2AZ and γH2AX	2240:2272	CONCLUSIONS These data suggest that H2AS40Gc functions to maintain genome integrity through the DNA repair mechanism in association with AcH2AZ and γH2AX.
29084613	8	26	theme	CRISPR/CAS9	1309:1319	arg1	system					1321:1326	CRISPR/CAS9 system	1309:1326	CRISPR/CAS9 system	1309:1326	H2AS40Gc was accumulated at the restricted area (± 1.5 kb) of DNA damage sites induced by CRISPR/CAS9 system in contrast to accumulation of γH2AX, which was widely scattered.
29084613	11	27	theme	apparatus	1839:1847	arg1	accumulation					1808:1819	the accumulation	1804:1819	the accumulation of the DNA repair apparatus such as DNA-PKcs and Rad51	1804:1874	Furthermore, the S40A mutant prevented the accumulation of the DNA repair apparatus such as DNA-PKcs and Rad51 at the damage site.
29084613	10	28	from	functions	1714:1722	arg1	mechanism					1754:1762	the DNA repair mechanism	1739:1762	the DNA repair mechanism	1739:1762	Furthermore, 3 h after the DNA damage treatment, the genome was almost recovered in WT mESCs, whereas the damage advanced further in the S40A-mutant mESCs, suggesting functions of H2AS40Gc in the DNA repair mechanism.
29084613	1	29	theme	O-GlcNAc	155:162	arg1	modification					164:175	a novel O-GlcNAc modification	147:175	a novel O-GlcNAc modification at serine 40 (S40) of H2A (H2AS40Gc)	147:212	BACKGROUND We have previously reported a novel O-GlcNAc modification at serine 40 (S40) of H2A (H2AS40Gc).
29084613	0	30	with	association	65:75	arg1	γH2AX					101:105	γH2AX	101:105	γH2AX	101:105	H2A O-GlcNAcylation at serine 40 functions genomic protection in association with acetylated H2AZ or γH2AX.
29084613	0	30	with	association	65:75	arg1	H2AZ					93:96	H2AZ	93:96	H2AZ	93:96	H2A O-GlcNAcylation at serine 40 functions genomic protection in association with acetylated H2AZ or γH2AX.
29084613	5	31	theme	H2A	873:875	arg1	isoforms					877:884	the S40-type H2A isoforms	860:884	the S40-type H2A isoforms	860:884	RESULTS We found several similarities between the S40-type H2A isoforms and histone H2A variants such H2AZ and H2AX.
29084613	12	32	theme	initial	2020:2026	arg1	phase					2028:2032	the initial phase	2016:2032	the initial phase upon DNA damage	2016:2048	Co-immunoprecipitation experiment in WT and S40A-mutant mESCs revealed that H2AS40Gc physiologically bound to AcH2AZ at the initial phase upon DNA damage, followed by binding with γH2AX during the DNA damage repair process.
29084613	1	33	dep	BACKGROUND	108:117	arg1	reported					138:145	reported	138:145	have previously reported a novel O-GlcNAc modification at serine 40 (S40) of H2A (H2AS40Gc)	122:212	BACKGROUND We have previously reported a novel O-GlcNAc modification at serine 40 (S40) of H2A (H2AS40Gc).
29084613	2	34	theme	H2AS40Gc	369:376	arg1	unknown					389:395	unknown	389:395	unknown	389:395	S40-type H2A isoforms susceptible to O-GlcNAcylation are evolutionarily new and restricted to the viviparous animals; however, the biological function of H2AS40Gc is largely unknown.
29084613	2	34	theme	H2AS40Gc	369:376	arg1	function					357:364	the biological function	342:364	the biological function of H2AS40Gc	342:376	S40-type H2A isoforms susceptible to O-GlcNAcylation are evolutionarily new and restricted to the viviparous animals; however, the biological function of H2AS40Gc is largely unknown.
29084613	13	35	theme	DNA	2216:2218	arg1	mechanism					2227:2235	the DNA repair mechanism	2212:2235	the DNA repair mechanism in association with AcH2AZ and γH2AX	2212:2272	CONCLUSIONS These data suggest that H2AS40Gc functions to maintain genome integrity through the DNA repair mechanism in association with AcH2AZ and γH2AX.
29084613	3	36	theme	H2A	398:400	arg1	isoforms					402:409	H2A isoforms	398:409	H2A isoforms	398:409	H2A isoforms are consisted of S40 and alanine 40 (A40) type and this residue on H2A is located in the L1 of the globular domain, which is also known as a variable portion that distinguishes between the canonical and non-canonical H2A variants.
29084613	0	37	theme	H2A	0:2	arg1	O-GlcNAcylation					4:18	H2A O-GlcNAcylation	0:18	H2A O-GlcNAcylation at serine 40	0:31	H2A O-GlcNAcylation at serine 40 functions genomic protection in association with acetylated H2AZ or γH2AX.
29084613	6	38	theme	isoforms	952:959	arg1	mRNA					931:934	mRNA	931:934	mRNA of S40-type H2A isoforms (H2A1 N and H2A3)	931:977	mRNA of S40-type H2A isoforms (H2A1 N and H2A3) had a poly(A) tail and was produced throughout the cell cycle in contrast to that of A40-type.
29084613	13	39	theme	genome	2187:2192	arg1	integrity					2194:2202	genome integrity	2187:2202	genome integrity	2187:2202	CONCLUSIONS These data suggest that H2AS40Gc functions to maintain genome integrity through the DNA repair mechanism in association with AcH2AZ and γH2AX.
29084613	6	40	theme	S40-type	939:946	arg1	H2A3					973:976	H2A3	973:976	H2A3	973:976	mRNA of S40-type H2A isoforms (H2A1 N and H2A3) had a poly(A) tail and was produced throughout the cell cycle in contrast to that of A40-type.
29084613	6	40	theme	S40-type	939:946	arg1	H2A1 N					962:967	H2A1 N	962:967	H2A1 N	962:967	mRNA of S40-type H2A isoforms (H2A1 N and H2A3) had a poly(A) tail and was produced throughout the cell cycle in contrast to that of A40-type.
29084613	6	40	theme	S40-type	939:946	arg1	isoforms					952:959	S40-type H2A isoforms	939:959	S40-type H2A isoforms (H2A1 N and H2A3)	939:977	mRNA of S40-type H2A isoforms (H2A1 N and H2A3) had a poly(A) tail and was produced throughout the cell cycle in contrast to that of A40-type.
29084613	10	41	theme	WT	1631:1632	arg1	mESCs					1634:1638	WT mESCs	1631:1638	WT mESCs	1631:1638	Furthermore, 3 h after the DNA damage treatment, the genome was almost recovered in WT mESCs, whereas the damage advanced further in the S40A-mutant mESCs, suggesting functions of H2AS40Gc in the DNA repair mechanism.
29084613	12	42	theme	S40A-mutant	1940:1950	arg1	mESCs					1952:1956	WT and S40A-mutant mESCs	1933:1956	WT and S40A-mutant mESCs	1933:1956	Co-immunoprecipitation experiment in WT and S40A-mutant mESCs revealed that H2AS40Gc physiologically bound to AcH2AZ at the initial phase upon DNA damage, followed by binding with γH2AX during the DNA damage repair process.
29084613	9	43	theme	wild-type	1416:1424	arg1	H2A3					1431:1434	the wild-type (WT) H2A3	1412:1434	the wild-type (WT) H2A3	1412:1434	Overexpression of the wild-type (WT) H2A3, but not the S40 to A40 mutation (S40A-mutant), protected the mESC genome against chemical-induced DNA damage.
29084613	3	44	theme	variable	552:559	arg1	portion					561:567	a variable portion	550:567	a variable portion that distinguishes between the canonical and non-canonical H2A variants	550:639	H2A isoforms are consisted of S40 and alanine 40 (A40) type and this residue on H2A is located in the L1 of the globular domain, which is also known as a variable portion that distinguishes between the canonical and non-canonical H2A variants.
29084613	3	44	theme	variable	552:559	arg1	domain					519:524	the globular domain	506:524	the globular domain	506:524	H2A isoforms are consisted of S40 and alanine 40 (A40) type and this residue on H2A is located in the L1 of the globular domain, which is also known as a variable portion that distinguishes between the canonical and non-canonical H2A variants.
29084613	9	45	dep	mutation	1460:1467	arg1	to					1453:1454	to	1453:1454	to	1453:1454	Overexpression of the wild-type (WT) H2A3, but not the S40 to A40 mutation (S40A-mutant), protected the mESC genome against chemical-induced DNA damage.
29084613	6	46	theme	A	990:990	arg1	tail					993:996	a poly(A) tail	983:996	a poly(A) tail	983:996	mRNA of S40-type H2A isoforms (H2A1 N and H2A3) had a poly(A) tail and was produced throughout the cell cycle in contrast to that of A40-type.
29084613	3	47	theme	canonical	600:608	arg1	variants					632:639	the canonical and non-canonical H2A variants	596:639	the canonical and non-canonical H2A variants	596:639	H2A isoforms are consisted of S40 and alanine 40 (A40) type and this residue on H2A is located in the L1 of the globular domain, which is also known as a variable portion that distinguishes between the canonical and non-canonical H2A variants.
29084613	8	48	theme	restricted	1251:1260	arg1	± 1.5 kb					1268:1275	± 1.5 kb	1268:1275	± 1.5 kb	1268:1275	H2AS40Gc was accumulated at the restricted area (± 1.5 kb) of DNA damage sites induced by CRISPR/CAS9 system in contrast to accumulation of γH2AX, which was widely scattered.
29084613	8	48	theme	restricted	1251:1260	arg1	area					1262:1265	the restricted area	1247:1265	the restricted area (± 1.5 kb) of DNA damage sites induced by CRISPR/CAS9 system in contrast to accumulation of γH2AX, which was widely scattered	1247:1391	H2AS40Gc was accumulated at the restricted area (± 1.5 kb) of DNA damage sites induced by CRISPR/CAS9 system in contrast to accumulation of γH2AX, which was widely scattered.
29084613	1	49	theme	H2A	199:201	arg1	serine					180:185	serine 40	180:188	serine 40 (S40) of H2A (H2AS40Gc)	180:212	BACKGROUND We have previously reported a novel O-GlcNAc modification at serine 40 (S40) of H2A (H2AS40Gc).
29084613	1	49	theme	H2A	199:201	arg1	S40					191:193	S40	191:193	S40	191:193	BACKGROUND We have previously reported a novel O-GlcNAc modification at serine 40 (S40) of H2A (H2AS40Gc).
29084613	5	50	theme	H2A	898:900	arg1	variants					902:909	histone H2A variants	890:909	histone H2A variants	890:909	RESULTS We found several similarities between the S40-type H2A isoforms and histone H2A variants such H2AZ and H2AX.
29084613	6	51	theme	poly	985:988	arg1	tail					993:996	a poly(A) tail	983:996	a poly(A) tail	983:996	mRNA of S40-type H2A isoforms (H2A1 N and H2A3) had a poly(A) tail and was produced throughout the cell cycle in contrast to that of A40-type.
29084613	4	52	theme	H2A	724:726	arg1	variants					728:735	the S40-type H2A and histone H2A variants	695:735	the S40-type H2A and histone H2A variants	695:735	In this study, by considering the similarity between the S40-type H2A and histone H2A variants, we explored the function of H2AS40Gc in mouse embryonic stem cells (mESCs).
29084613	8	53	dep	accumulation	1343:1354	arg1	contrast					1331:1338	contrast	1331:1338	contrast	1331:1338	H2AS40Gc was accumulated at the restricted area (± 1.5 kb) of DNA damage sites induced by CRISPR/CAS9 system in contrast to accumulation of γH2AX, which was widely scattered.
29084613	7	54	theme	H2AS40Gc	1087:1094	arg1	level					1096:1100	H2AS40Gc level	1087:1100	H2AS40Gc level	1087:1100	Importantly, H2AS40Gc level increased owing to chemical-induced DNA damage, similar to phosphorylated H2AX (γH2AX) and acetylated H2AZ (AcH2AZ).
29084613	3	55	theme	non-canonical	614:626	arg1	variants					632:639	the canonical and non-canonical H2A variants	596:639	the canonical and non-canonical H2A variants	596:639	H2A isoforms are consisted of S40 and alanine 40 (A40) type and this residue on H2A is located in the L1 of the globular domain, which is also known as a variable portion that distinguishes between the canonical and non-canonical H2A variants.
29084613	4	56	theme	embryonic	784:792	arg1	mESCs					806:810	mESCs	806:810	mESCs	806:810	In this study, by considering the similarity between the S40-type H2A and histone H2A variants, we explored the function of H2AS40Gc in mouse embryonic stem cells (mESCs).
29084613	4	56	theme	embryonic	784:792	arg1	cells					799:803	mouse embryonic stem cells	778:803	mouse embryonic stem cells (mESCs)	778:811	In this study, by considering the similarity between the S40-type H2A and histone H2A variants, we explored the function of H2AS40Gc in mouse embryonic stem cells (mESCs).
29084613	6	57	theme	cell	1030:1033	arg1	cycle					1035:1039	the cell cycle	1026:1039	the cell cycle	1026:1039	mRNA of S40-type H2A isoforms (H2A1 N and H2A3) had a poly(A) tail and was produced throughout the cell cycle in contrast to that of A40-type.
29084613	0	58	theme	genomic	43:49	arg1	protection					51:60	genomic protection	43:60	genomic protection	43:60	H2A O-GlcNAcylation at serine 40 functions genomic protection in association with acetylated H2AZ or γH2AX.
29084613	10	59	theme	S40A-mutant	1684:1694	arg1	mESCs					1696:1700	the S40A-mutant mESCs	1680:1700	the S40A-mutant mESCs	1680:1700	Furthermore, 3 h after the DNA damage treatment, the genome was almost recovered in WT mESCs, whereas the damage advanced further in the S40A-mutant mESCs, suggesting functions of H2AS40Gc in the DNA repair mechanism.
29084613	10	60	from	advanced	1660:1667	arg1	mESCs					1696:1700	the S40A-mutant mESCs	1680:1700	the S40A-mutant mESCs	1680:1700	Furthermore, 3 h after the DNA damage treatment, the genome was almost recovered in WT mESCs, whereas the damage advanced further in the S40A-mutant mESCs, suggesting functions of H2AS40Gc in the DNA repair mechanism.
29084613	11	61	theme	damage	1883:1888	arg1	site					1890:1893	the damage site	1879:1893	the damage site	1879:1893	Furthermore, the S40A mutant prevented the accumulation of the DNA repair apparatus such as DNA-PKcs and Rad51 at the damage site.
29084613	9	62	dep	wild-type	1416:1424	arg1	WT					1427:1428	WT	1427:1428	WT	1427:1428	Overexpression of the wild-type (WT) H2A3, but not the S40 to A40 mutation (S40A-mutant), protected the mESC genome against chemical-induced DNA damage.
29084613	10	63	theme	H2AS40Gc	1727:1734	arg1	functions					1714:1722	functions	1714:1722	functions of H2AS40Gc in the DNA repair mechanism	1714:1762	Furthermore, 3 h after the DNA damage treatment, the genome was almost recovered in WT mESCs, whereas the damage advanced further in the S40A-mutant mESCs, suggesting functions of H2AS40Gc in the DNA repair mechanism.
29084613	11	64	theme	S40A	1782:1785	arg1	mutant					1787:1792	the S40A mutant	1778:1792	the S40A mutant	1778:1792	Furthermore, the S40A mutant prevented the accumulation of the DNA repair apparatus such as DNA-PKcs and Rad51 at the damage site.
29084613	3	65	located	located	485:491	arg1	L1					500:501	the L1	496:501	the L1 of the globular domain, which is also known as a variable portion that distinguishes between the canonical and non-canonical H2A variants	496:639	H2A isoforms are consisted of S40 and alanine 40 (A40) type and this residue on H2A is located in the L1 of the globular domain, which is also known as a variable portion that distinguishes between the canonical and non-canonical H2A variants.
29084613	3	65	located	located	485:491	arg2	residue					467:473	this residue	462:473	this residue on H2A	462:480	H2A isoforms are consisted of S40 and alanine 40 (A40) type and this residue on H2A is located in the L1 of the globular domain, which is also known as a variable portion that distinguishes between the canonical and non-canonical H2A variants.
29084613	11	66	theme	DNA	1828:1830	arg1	Rad51					1870:1874	Rad51	1870:1874	Rad51	1870:1874	Furthermore, the S40A mutant prevented the accumulation of the DNA repair apparatus such as DNA-PKcs and Rad51 at the damage site.
29084613	11	66	theme	DNA	1828:1830	arg1	apparatus					1839:1847	the DNA repair apparatus	1824:1847	the DNA repair apparatus such as DNA-PKcs and Rad51	1824:1874	Furthermore, the S40A mutant prevented the accumulation of the DNA repair apparatus such as DNA-PKcs and Rad51 at the damage site.
29084613	11	66	theme	DNA	1828:1830	arg1	DNA-PKcs					1857:1864	DNA-PKcs	1857:1864	DNA-PKcs	1857:1864	Furthermore, the S40A mutant prevented the accumulation of the DNA repair apparatus such as DNA-PKcs and Rad51 at the damage site.
29084613	12	67	theme	DNA	2093:2095	arg1	repair					2104:2109	DNA damage repair	2093:2109	the DNA damage repair process	2089:2117	Co-immunoprecipitation experiment in WT and S40A-mutant mESCs revealed that H2AS40Gc physiologically bound to AcH2AZ at the initial phase upon DNA damage, followed by binding with γH2AX during the DNA damage repair process.
29084613	7	68	theme	DNA	1138:1140	arg1	damage					1142:1147	chemical-induced DNA damage	1121:1147	chemical-induced DNA damage	1121:1147	Importantly, H2AS40Gc level increased owing to chemical-induced DNA damage, similar to phosphorylated H2AX (γH2AX) and acetylated H2AZ (AcH2AZ).
29084613	8	69	theme	DNA	1281:1283	arg1	damage					1285:1290	DNA damage sites	1281:1296	DNA damage sites induced by CRISPR/CAS9 system in contrast to accumulation of γH2AX, which was widely scattered	1281:1391	H2AS40Gc was accumulated at the restricted area (± 1.5 kb) of DNA damage sites induced by CRISPR/CAS9 system in contrast to accumulation of γH2AX, which was widely scattered.
29084613	10	70	theme	repair	1747:1752	arg1	mechanism					1754:1762	the DNA repair mechanism	1739:1762	the DNA repair mechanism	1739:1762	Furthermore, 3 h after the DNA damage treatment, the genome was almost recovered in WT mESCs, whereas the damage advanced further in the S40A-mutant mESCs, suggesting functions of H2AS40Gc in the DNA repair mechanism.
29084613	13	71	theme	repair	2220:2225	arg1	mechanism					2227:2235	the DNA repair mechanism	2212:2235	the DNA repair mechanism in association with AcH2AZ and γH2AX	2212:2272	CONCLUSIONS These data suggest that H2AS40Gc functions to maintain genome integrity through the DNA repair mechanism in association with AcH2AZ and γH2AX.
29084613	10	72	theme	damage	1578:1583	arg1	treatment					1585:1593	the DNA damage treatment	1570:1593	the DNA damage treatment	1570:1593	Furthermore, 3 h after the DNA damage treatment, the genome was almost recovered in WT mESCs, whereas the damage advanced further in the S40A-mutant mESCs, suggesting functions of H2AS40Gc in the DNA repair mechanism.
29084613	12	73	dep	bound	1997:2001	arg1	followed					2051:2058	followed	2051:2058	followed by binding with γH2AX during the DNA damage repair process	2051:2117	Co-immunoprecipitation experiment in WT and S40A-mutant mESCs revealed that H2AS40Gc physiologically bound to AcH2AZ at the initial phase upon DNA damage, followed by binding with γH2AX during the DNA damage repair process.
29084613	9	74	theme	chemical-induced	1518:1533	arg1	damage					1539:1544	chemical-induced DNA damage	1518:1544	chemical-induced DNA damage	1518:1544	Overexpression of the wild-type (WT) H2A3, but not the S40 to A40 mutation (S40A-mutant), protected the mESC genome against chemical-induced DNA damage.
29084613	6	75	contain	had	979:981	arg2	tail					993:996	a poly(A) tail	983:996	a poly(A) tail	983:996	mRNA of S40-type H2A isoforms (H2A1 N and H2A3) had a poly(A) tail and was produced throughout the cell cycle in contrast to that of A40-type.
29084613	6	75	contain	had	979:981	arg1	mRNA					931:934	mRNA	931:934	mRNA of S40-type H2A isoforms (H2A1 N and H2A3)	931:977	mRNA of S40-type H2A isoforms (H2A1 N and H2A3) had a poly(A) tail and was produced throughout the cell cycle in contrast to that of A40-type.
29084613	2	76	theme	S40-type	215:222	arg1	isoforms					228:235	S40-type H2A isoforms	215:235	S40-type H2A isoforms susceptible to O-GlcNAcylation	215:266	S40-type H2A isoforms susceptible to O-GlcNAcylation are evolutionarily new and restricted to the viviparous animals; however, the biological function of H2AS40Gc is largely unknown.
29084613	0	77	from	serine	23:28	arg1	O-GlcNAcylation					4:18	H2A O-GlcNAcylation	0:18	H2A O-GlcNAcylation at serine 40	0:31	H2A O-GlcNAcylation at serine 40 functions genomic protection in association with acetylated H2AZ or γH2AX.
29084613	0	78	theme	acetylated	82:91	arg1	H2AZ					93:96	H2AZ	93:96	H2AZ	93:96	H2A O-GlcNAcylation at serine 40 functions genomic protection in association with acetylated H2AZ or γH2AX.
29084613	1	79	theme	novel	149:153	arg1	modification					164:175	a novel O-GlcNAc modification	147:175	a novel O-GlcNAc modification at serine 40 (S40) of H2A (H2AS40Gc)	147:212	BACKGROUND We have previously reported a novel O-GlcNAc modification at serine 40 (S40) of H2A (H2AS40Gc).
29084613	3	80	from	located	485:491	arg1	L1					500:501	the L1	496:501	the L1 of the globular domain, which is also known as a variable portion that distinguishes between the canonical and non-canonical H2A variants	496:639	H2A isoforms are consisted of S40 and alanine 40 (A40) type and this residue on H2A is located in the L1 of the globular domain, which is also known as a variable portion that distinguishes between the canonical and non-canonical H2A variants.
29084613	9	81	theme	H2A3	1431:1434	arg1	Overexpression					1394:1407	Overexpression	1394:1407	Overexpression of the wild-type (WT) H2A3	1394:1434	Overexpression of the wild-type (WT) H2A3, but not the S40 to A40 mutation (S40A-mutant), protected the mESC genome against chemical-induced DNA damage.
29084613	5	82	theme	S40-type	864:871	arg1	isoforms					877:884	the S40-type H2A isoforms	860:884	the S40-type H2A isoforms	860:884	RESULTS We found several similarities between the S40-type H2A isoforms and histone H2A variants such H2AZ and H2AX.
29084613	8	83	theme	γH2AX	1359:1363	arg1	accumulation					1343:1354	accumulation	1343:1354	accumulation of γH2AX, which was widely scattered	1343:1391	H2AS40Gc was accumulated at the restricted area (± 1.5 kb) of DNA damage sites induced by CRISPR/CAS9 system in contrast to accumulation of γH2AX, which was widely scattered.
29084613	5	84	dep	RESULTS	814:820	arg1	found					825:829	found	825:829	found several similarities between the S40-type H2A isoforms and histone H2A variants such H2AZ and H2AX	825:928	RESULTS We found several similarities between the S40-type H2A isoforms and histone H2A variants such H2AZ and H2AX.
29084613	13	85	with	association	2240:2250	arg1	AcH2AZ					2257:2262	AcH2AZ	2257:2262	AcH2AZ	2257:2262	CONCLUSIONS These data suggest that H2AS40Gc functions to maintain genome integrity through the DNA repair mechanism in association with AcH2AZ and γH2AX.
29084613	13	85	with	association	2240:2250	arg1	γH2AX					2268:2272	γH2AX	2268:2272	γH2AX	2268:2272	CONCLUSIONS These data suggest that H2AS40Gc functions to maintain genome integrity through the DNA repair mechanism in association with AcH2AZ and γH2AX.
29084613	5	86	theme	several	831:837	arg1	similarities					839:850	several similarities	831:850	several similarities between the S40-type H2A isoforms and histone H2A variants	831:909	RESULTS We found several similarities between the S40-type H2A isoforms and histone H2A variants such H2AZ and H2AX.
29084613	7	87	theme	phosphorylated	1161:1174	arg1	H2AX					1176:1179	phosphorylated H2AX	1161:1179	phosphorylated H2AX (γH2AX)	1161:1187	Importantly, H2AS40Gc level increased owing to chemical-induced DNA damage, similar to phosphorylated H2AX (γH2AX) and acetylated H2AZ (AcH2AZ).
29084613	7	87	theme	phosphorylated	1161:1174	arg1	γH2AX					1182:1186	γH2AX	1182:1186	γH2AX	1182:1186	Importantly, H2AS40Gc level increased owing to chemical-induced DNA damage, similar to phosphorylated H2AX (γH2AX) and acetylated H2AZ (AcH2AZ).
29084613	6	88	dep	isoforms	952:959	arg1	H2A3					973:976	H2A3	973:976	H2A3	973:976	mRNA of S40-type H2A isoforms (H2A1 N and H2A3) had a poly(A) tail and was produced throughout the cell cycle in contrast to that of A40-type.
29084613	6	88	dep	isoforms	952:959	arg1	H2A1 N					962:967	H2A1 N	962:967	H2A1 N	962:967	mRNA of S40-type H2A isoforms (H2A1 N and H2A3) had a poly(A) tail and was produced throughout the cell cycle in contrast to that of A40-type.
29084613	6	88	dep	isoforms	952:959	arg1	isoforms					952:959	S40-type H2A isoforms	939:959	S40-type H2A isoforms (H2A1 N and H2A3)	939:977	mRNA of S40-type H2A isoforms (H2A1 N and H2A3) had a poly(A) tail and was produced throughout the cell cycle in contrast to that of A40-type.
29084613	2	89	theme	biological	346:355	arg1	unknown					389:395	unknown	389:395	unknown	389:395	S40-type H2A isoforms susceptible to O-GlcNAcylation are evolutionarily new and restricted to the viviparous animals; however, the biological function of H2AS40Gc is largely unknown.
29084613	2	89	theme	biological	346:355	arg1	function					357:364	the biological function	342:364	the biological function of H2AS40Gc	342:376	S40-type H2A isoforms susceptible to O-GlcNAcylation are evolutionarily new and restricted to the viviparous animals; however, the biological function of H2AS40Gc is largely unknown.
29084613	12	90	theme	WT	1933:1934	arg1	mESCs					1952:1956	WT and S40A-mutant mESCs	1933:1956	WT and S40A-mutant mESCs	1933:1956	Co-immunoprecipitation experiment in WT and S40A-mutant mESCs revealed that H2AS40Gc physiologically bound to AcH2AZ at the initial phase upon DNA damage, followed by binding with γH2AX during the DNA damage repair process.
29084613	6	91	theme	H2A	948:950	arg1	H2A3					973:976	H2A3	973:976	H2A3	973:976	mRNA of S40-type H2A isoforms (H2A1 N and H2A3) had a poly(A) tail and was produced throughout the cell cycle in contrast to that of A40-type.
29084613	6	91	theme	H2A	948:950	arg1	H2A1 N					962:967	H2A1 N	962:967	H2A1 N	962:967	mRNA of S40-type H2A isoforms (H2A1 N and H2A3) had a poly(A) tail and was produced throughout the cell cycle in contrast to that of A40-type.
29084613	6	91	theme	H2A	948:950	arg1	isoforms					952:959	S40-type H2A isoforms	939:959	S40-type H2A isoforms (H2A1 N and H2A3)	939:977	mRNA of S40-type H2A isoforms (H2A1 N and H2A3) had a poly(A) tail and was produced throughout the cell cycle in contrast to that of A40-type.
29084613	4	92	theme	S40-type	699:706	arg1	H2A					708:710	S40-type H2A	699:710	S40-type H2A	699:710	In this study, by considering the similarity between the S40-type H2A and histone H2A variants, we explored the function of H2AS40Gc in mouse embryonic stem cells (mESCs).
29084613	8	93	dep	damage	1285:1290	arg1	sites					1292:1296	sites	1292:1296	DNA damage sites induced by CRISPR/CAS9 system in contrast to accumulation of γH2AX, which was widely scattered	1281:1391	H2AS40Gc was accumulated at the restricted area (± 1.5 kb) of DNA damage sites induced by CRISPR/CAS9 system in contrast to accumulation of γH2AX, which was widely scattered.
29084613	12	94	theme	DNA	2039:2041	arg1	damage					2043:2048	DNA damage	2039:2048	DNA damage	2039:2048	Co-immunoprecipitation experiment in WT and S40A-mutant mESCs revealed that H2AS40Gc physiologically bound to AcH2AZ at the initial phase upon DNA damage, followed by binding with γH2AX during the DNA damage repair process.
29084613	7	95	theme	chemical-induced	1121:1136	arg1	damage					1142:1147	chemical-induced DNA damage	1121:1147	chemical-induced DNA damage	1121:1147	Importantly, H2AS40Gc level increased owing to chemical-induced DNA damage, similar to phosphorylated H2AX (γH2AX) and acetylated H2AZ (AcH2AZ).
29084613	12	96	theme	repair	2104:2109	arg1	process					2111:2117	the DNA damage repair process	2089:2117	the DNA damage repair process	2089:2117	Co-immunoprecipitation experiment in WT and S40A-mutant mESCs revealed that H2AS40Gc physiologically bound to AcH2AZ at the initial phase upon DNA damage, followed by binding with γH2AX during the DNA damage repair process.
29084613	2	97	theme	viviparous	313:322	arg1	animals					324:330	the viviparous animals	309:330	the viviparous animals	309:330	S40-type H2A isoforms susceptible to O-GlcNAcylation are evolutionarily new and restricted to the viviparous animals; however, the biological function of H2AS40Gc is largely unknown.
29084613	5	98	theme	histone	890:896	arg1	variants					902:909	histone H2A variants	890:909	histone H2A variants	890:909	RESULTS We found several similarities between the S40-type H2A isoforms and histone H2A variants such H2AZ and H2AX.
29084613	4	99	theme	H2A	708:710	arg1	variants					728:735	the S40-type H2A and histone H2A variants	695:735	the S40-type H2A and histone H2A variants	695:735	In this study, by considering the similarity between the S40-type H2A and histone H2A variants, we explored the function of H2AS40Gc in mouse embryonic stem cells (mESCs).
29084613	3	100	theme	H2A	628:630	arg1	variants					632:639	the canonical and non-canonical H2A variants	596:639	the canonical and non-canonical H2A variants	596:639	H2A isoforms are consisted of S40 and alanine 40 (A40) type and this residue on H2A is located in the L1 of the globular domain, which is also known as a variable portion that distinguishes between the canonical and non-canonical H2A variants.
29084613	4	101	theme	histone	716:722	arg1	H2A					724:726	histone H2A	716:726	histone H2A	716:726	In this study, by considering the similarity between the S40-type H2A and histone H2A variants, we explored the function of H2AS40Gc in mouse embryonic stem cells (mESCs).
21795679	0	0	link	O-linked	106:113	arg1	modification					135:146	O-linked N-acetylglucosamine modification	106:146	O-linked N-acetylglucosamine modification of transcription factors YY1 and SP1	106:183	Cellular content of UDP-N-acetylhexosamines controls hyaluronan synthase 2 expression and correlates with O-linked N-acetylglucosamine modification of transcription factors YY1 and SP1.
21795679	4	1	theme	gene	913:916	arg1	expression					895:904	expression	895:904	expression of the gene	895:916	Increasing UDP-HexNAc in HaCaT keratinocytes by adding glucosamine down-regulated HAS2 gene expression, whereas a decrease in UDP-HexNAc, realized by mannose treatment or siRNA for GFAT1 (glutamine:fructose-6-phosphate amidotransferase 1), enhanced expression of the gene.
21795679	6	2	theme	HAS2	1275:1278	arg1	expression					1280:1289	HAS2 expression	1275:1289	HAS2 expression	1275:1289	Instead, altered binding of SP1 and YY1 to the promoter correlated with cellular UDP-HexNAc content and inhibition of HAS2 expression.
21795679	1	3	theme	high	200:203	arg1	Hyaluronan					186:195	Hyaluronan	186:195	Hyaluronan	186:195	Hyaluronan, a high molecular mass polysaccharide on the vertebrate cell surface and extracellular matrix, is produced at the plasma membrane by hyaluronan synthases using UDP-GlcNAc and UDP-GlcUA as substrates.
21795679	1	3	theme	high	200:203	arg1	polysaccharide					220:233	a high molecular mass polysaccharide	198:233	a high molecular mass polysaccharide on the vertebrate cell surface and extracellular matrix	198:289	Hyaluronan, a high molecular mass polysaccharide on the vertebrate cell surface and extracellular matrix, is produced at the plasma membrane by hyaluronan synthases using UDP-GlcNAc and UDP-GlcUA as substrates.
21795679	9	4	theme	hyaluronan	1724:1733	arg1	synthesis					1735:1743	hyaluronan synthesis	1724:1743	hyaluronan synthesis that would result from cellular fluctuations of this substrate	1724:1806	Our data are consistent with the hypothesis that, by regulating the level of protein O-GlcNAc modifications, cellular UDP-HexNAc content controls HAS2 transcription and decreases the effects on hyaluronan synthesis that would result from cellular fluctuations of this substrate.
21795679	1	5	theme	mass	215:218	arg1	Hyaluronan					186:195	Hyaluronan	186:195	Hyaluronan	186:195	Hyaluronan, a high molecular mass polysaccharide on the vertebrate cell surface and extracellular matrix, is produced at the plasma membrane by hyaluronan synthases using UDP-GlcNAc and UDP-GlcUA as substrates.
21795679	1	5	theme	mass	215:218	arg1	polysaccharide					220:233	a high molecular mass polysaccharide	198:233	a high molecular mass polysaccharide on the vertebrate cell surface and extracellular matrix	198:289	Hyaluronan, a high molecular mass polysaccharide on the vertebrate cell surface and extracellular matrix, is produced at the plasma membrane by hyaluronan synthases using UDP-GlcNAc and UDP-GlcUA as substrates.
21795679	6	6	theme	altered	1166:1172	arg1	binding					1174:1180	altered binding	1166:1180	altered binding of SP1 and YY1 to the promoter	1166:1211	Instead, altered binding of SP1 and YY1 to the promoter correlated with cellular UDP-HexNAc content and inhibition of HAS2 expression.
21795679	0	7	theme	transcription	151:163	arg1	YY1					173:175	YY1	173:175	YY1	173:175	Cellular content of UDP-N-acetylhexosamines controls hyaluronan synthase 2 expression and correlates with O-linked N-acetylglucosamine modification of transcription factors YY1 and SP1.
21795679	0	7	theme	transcription	151:163	arg1	factors					165:171	transcription factors YY1 and SP1	151:183	transcription factors YY1 and SP1	151:183	Cellular content of UDP-N-acetylhexosamines controls hyaluronan synthase 2 expression and correlates with O-linked N-acetylglucosamine modification of transcription factors YY1 and SP1.
21795679	0	7	theme	transcription	151:163	arg1	SP1					181:183	SP1	181:183	SP1	181:183	Cellular content of UDP-N-acetylhexosamines controls hyaluronan synthase 2 expression and correlates with O-linked N-acetylglucosamine modification of transcription factors YY1 and SP1.
21795679	4	8	from	UDP-HexNAc	657:666	arg1	keratinocytes					677:689	HaCaT keratinocytes	671:689	HaCaT keratinocytes	671:689	Increasing UDP-HexNAc in HaCaT keratinocytes by adding glucosamine down-regulated HAS2 gene expression, whereas a decrease in UDP-HexNAc, realized by mannose treatment or siRNA for GFAT1 (glutamine:fructose-6-phosphate amidotransferase 1), enhanced expression of the gene.
21795679	4	9	theme	HaCaT	671:675	arg1	keratinocytes					677:689	HaCaT keratinocytes	671:689	HaCaT keratinocytes	671:689	Increasing UDP-HexNAc in HaCaT keratinocytes by adding glucosamine down-regulated HAS2 gene expression, whereas a decrease in UDP-HexNAc, realized by mannose treatment or siRNA for GFAT1 (glutamine:fructose-6-phosphate amidotransferase 1), enhanced expression of the gene.
21795679	5	10	theme	growth	1102:1107	arg1	factor					1109:1114	growth factor	1102:1114	growth factor	1102:1114	Tracing the UDP-HexNAc-initiated signal to the HAS2 promoter revealed no change in the binding of STAT3, NF-κB, and cAMP response element-binding protein, shown previously to mediate growth factor and cytokine signals on HAS2 expression.
21795679	3	11	theme	hyaluronan	622:631	arg1	HAS2					616:619	HAS2	616:619	HAS2 (hyaluronan synthase 2)	616:643	In this study, we show that the cellular level of UDP-HexNAc also controls hyaluronan synthesis by modulating the expression of HAS2 (hyaluronan synthase 2).
21795679	3	11	theme	hyaluronan	622:631	arg1	synthase					633:640	hyaluronan synthase 2	622:642	hyaluronan synthase 2	622:642	In this study, we show that the cellular level of UDP-HexNAc also controls hyaluronan synthesis by modulating the expression of HAS2 (hyaluronan synthase 2).
21795679	1	12	theme	vertebrate	242:251	arg1	surface					258:264	the vertebrate cell surface	238:264	the vertebrate cell surface	238:264	Hyaluronan, a high molecular mass polysaccharide on the vertebrate cell surface and extracellular matrix, is produced at the plasma membrane by hyaluronan synthases using UDP-GlcNAc and UDP-GlcUA as substrates.
21795679	9	13	theme	cellular	1768:1775	arg1	fluctuations					1777:1788	cellular fluctuations	1768:1788	cellular fluctuations of this substrate	1768:1806	Our data are consistent with the hypothesis that, by regulating the level of protein O-GlcNAc modifications, cellular UDP-HexNAc content controls HAS2 transcription and decreases the effects on hyaluronan synthesis that would result from cellular fluctuations of this substrate.
21795679	6	14	theme	UDP-HexNAc	1238:1247	arg1	content					1249:1255	cellular UDP-HexNAc content	1229:1255	cellular UDP-HexNAc content	1229:1255	Instead, altered binding of SP1 and YY1 to the promoter correlated with cellular UDP-HexNAc content and inhibition of HAS2 expression.
21795679	5	15	theme	protein	1065:1071	arg1	binding					1006:1012	the binding	1002:1012	the binding of STAT3, NF-κB, and cAMP response element-binding protein	1002:1071	Tracing the UDP-HexNAc-initiated signal to the HAS2 promoter revealed no change in the binding of STAT3, NF-κB, and cAMP response element-binding protein, shown previously to mediate growth factor and cytokine signals on HAS2 expression.
21795679	3	16	theme	HAS2	616:619	arg1	expression					602:611	the expression	598:611	the expression of HAS2 (hyaluronan synthase 2)	598:643	In this study, we show that the cellular level of UDP-HexNAc also controls hyaluronan synthesis by modulating the expression of HAS2 (hyaluronan synthase 2).
21795679	1	17	from	polysaccharide	220:233	arg1	surface					258:264	the vertebrate cell surface	238:264	the vertebrate cell surface	238:264	Hyaluronan, a high molecular mass polysaccharide on the vertebrate cell surface and extracellular matrix, is produced at the plasma membrane by hyaluronan synthases using UDP-GlcNAc and UDP-GlcUA as substrates.
21795679	1	17	from	polysaccharide	220:233	arg1	matrix					284:289	extracellular matrix	270:289	extracellular matrix	270:289	Hyaluronan, a high molecular mass polysaccharide on the vertebrate cell surface and extracellular matrix, is produced at the plasma membrane by hyaluronan synthases using UDP-GlcNAc and UDP-GlcUA as substrates.
21795679	8	18	theme	HAS2	1499:1502	arg1	expression					1504:1513	HAS2 expression	1499:1513	HAS2 expression	1499:1513	Reduced and increased levels of O-GlcNAc-modified SP1 and YY1 proteins were associated with stimulation or inhibition of HAS2 expression, respectively.
21795679	5	19	theme	HAS2	966:969	arg1	promoter					971:978	the HAS2 promoter	962:978	the HAS2 promoter	962:978	Tracing the UDP-HexNAc-initiated signal to the HAS2 promoter revealed no change in the binding of STAT3, NF-κB, and cAMP response element-binding protein, shown previously to mediate growth factor and cytokine signals on HAS2 expression.
21795679	9	20	theme	substrate	1798:1806	arg1	fluctuations					1777:1788	cellular fluctuations	1768:1788	cellular fluctuations of this substrate	1768:1806	Our data are consistent with the hypothesis that, by regulating the level of protein O-GlcNAc modifications, cellular UDP-HexNAc content controls HAS2 transcription and decreases the effects on hyaluronan synthesis that would result from cellular fluctuations of this substrate.
21795679	7	21	theme	HAS2	1361:1364	arg1	expression					1366:1375	HAS2 expression	1361:1375	HAS2 expression	1361:1375	siRNA silencing of YY1 and SP1 confirmed their inhibitory effects on HAS2 expression.
21795679	4	22	theme	HAS2	728:731	arg1	expression					738:747	HAS2 gene expression	728:747	HAS2 gene expression	728:747	Increasing UDP-HexNAc in HaCaT keratinocytes by adding glucosamine down-regulated HAS2 gene expression, whereas a decrease in UDP-HexNAc, realized by mannose treatment or siRNA for GFAT1 (glutamine:fructose-6-phosphate amidotransferase 1), enhanced expression of the gene.
21795679	5	23	theme	HAS2	1140:1143	arg1	expression					1145:1154	HAS2 expression	1140:1154	HAS2 expression	1140:1154	Tracing the UDP-HexNAc-initiated signal to the HAS2 promoter revealed no change in the binding of STAT3, NF-κB, and cAMP response element-binding protein, shown previously to mediate growth factor and cytokine signals on HAS2 expression.
21795679	5	24	theme	UDP-HexNAc-initiated	931:950	arg1	signal					952:957	the UDP-HexNAc-initiated signal	927:957	the UDP-HexNAc-initiated signal to the HAS2 promoter	927:978	Tracing the UDP-HexNAc-initiated signal to the HAS2 promoter revealed no change in the binding of STAT3, NF-κB, and cAMP response element-binding protein, shown previously to mediate growth factor and cytokine signals on HAS2 expression.
21795679	9	25	with	consistent	1543:1552	arg1	hypothesis					1563:1572	the hypothesis that, by regulating the level of protein O-GlcNAc modifications, cellular UDP-HexNAc content controls HAS2 transcription and decreases the effects on hyaluronan synthesis that would result from cellular fluctuations of this substrate	1559:1806	the hypothesis that, by regulating the level of protein O-GlcNAc modifications, cellular UDP-HexNAc content controls HAS2 transcription and decreases the effects on hyaluronan synthesis that would result from cellular fluctuations of this substrate	1559:1806	Our data are consistent with the hypothesis that, by regulating the level of protein O-GlcNAc modifications, cellular UDP-HexNAc content controls HAS2 transcription and decreases the effects on hyaluronan synthesis that would result from cellular fluctuations of this substrate.
21795679	4	26	theme	mannose	796:802	arg1	treatment					804:812	mannose treatment	796:812	mannose treatment	796:812	Increasing UDP-HexNAc in HaCaT keratinocytes by adding glucosamine down-regulated HAS2 gene expression, whereas a decrease in UDP-HexNAc, realized by mannose treatment or siRNA for GFAT1 (glutamine:fructose-6-phosphate amidotransferase 1), enhanced expression of the gene.
21795679	0	27	theme	O-linked	106:113	arg1	modification					135:146	O-linked N-acetylglucosamine modification	106:146	O-linked N-acetylglucosamine modification of transcription factors YY1 and SP1	106:183	Cellular content of UDP-N-acetylhexosamines controls hyaluronan synthase 2 expression and correlates with O-linked N-acetylglucosamine modification of transcription factors YY1 and SP1.
21795679	8	28	theme	Reduced	1378:1384	arg1	levels					1400:1405	Reduced and increased levels	1378:1405	Reduced and increased levels of O-GlcNAc-modified SP1 and YY1 proteins	1378:1447	Reduced and increased levels of O-GlcNAc-modified SP1 and YY1 proteins were associated with stimulation or inhibition of HAS2 expression, respectively.
21795679	2	29	theme	substrates	433:442	arg1	availability					401:412	The availability	397:412	The availability of these UDP-sugar substrates	397:442	The availability of these UDP-sugar substrates can limit the synthesis rate of hyaluronan.
21795679	4	30	dep	down-regulated	713:726	arg1	whereas					750:756	whereas	750:756	whereas	750:756	Increasing UDP-HexNAc in HaCaT keratinocytes by adding glucosamine down-regulated HAS2 gene expression, whereas a decrease in UDP-HexNAc, realized by mannose treatment or siRNA for GFAT1 (glutamine:fructose-6-phosphate amidotransferase 1), enhanced expression of the gene.
21795679	8	31	theme	increased	1390:1398	arg1	levels					1400:1405	Reduced and increased levels	1378:1405	Reduced and increased levels of O-GlcNAc-modified SP1 and YY1 proteins	1378:1447	Reduced and increased levels of O-GlcNAc-modified SP1 and YY1 proteins were associated with stimulation or inhibition of HAS2 expression, respectively.
21795679	0	32	theme	Cellular	0:7	arg1	content					9:15	Cellular content	0:15	Cellular content of UDP-N-acetylhexosamines	0:42	Cellular content of UDP-N-acetylhexosamines controls hyaluronan synthase 2 expression and correlates with O-linked N-acetylglucosamine modification of transcription factors YY1 and SP1.
21795679	7	33	theme	inhibitory	1339:1348	arg1	effects					1350:1356	their inhibitory effects	1333:1356	their inhibitory effects on HAS2 expression	1333:1375	siRNA silencing of YY1 and SP1 confirmed their inhibitory effects on HAS2 expression.
21795679	2	34	theme	synthesis	458:466	arg1	rate					468:471	the synthesis rate	454:471	the synthesis rate of hyaluronan	454:485	The availability of these UDP-sugar substrates can limit the synthesis rate of hyaluronan.
21795679	1	35	theme	plasma	311:316	arg1	membrane					318:325	the plasma membrane	307:325	the plasma membrane	307:325	Hyaluronan, a high molecular mass polysaccharide on the vertebrate cell surface and extracellular matrix, is produced at the plasma membrane by hyaluronan synthases using UDP-GlcNAc and UDP-GlcUA as substrates.
21795679	9	36	theme	protein	1607:1613	arg1	modifications					1624:1636	protein O-GlcNAc modifications	1607:1636	protein O-GlcNAc modifications	1607:1636	Our data are consistent with the hypothesis that, by regulating the level of protein O-GlcNAc modifications, cellular UDP-HexNAc content controls HAS2 transcription and decreases the effects on hyaluronan synthesis that would result from cellular fluctuations of this substrate.
21795679	8	37	theme	SP1	1428:1430	arg1	proteins					1440:1447	O-GlcNAc-modified SP1 and YY1 proteins	1410:1447	O-GlcNAc-modified SP1 and YY1 proteins	1410:1447	Reduced and increased levels of O-GlcNAc-modified SP1 and YY1 proteins were associated with stimulation or inhibition of HAS2 expression, respectively.
21795679	9	38	theme	modifications	1624:1636	arg1	level					1598:1602	the level	1594:1602	the level of protein O-GlcNAc modifications	1594:1636	Our data are consistent with the hypothesis that, by regulating the level of protein O-GlcNAc modifications, cellular UDP-HexNAc content controls HAS2 transcription and decreases the effects on hyaluronan synthesis that would result from cellular fluctuations of this substrate.
21795679	8	39	theme	YY1	1436:1438	arg1	proteins					1440:1447	O-GlcNAc-modified SP1 and YY1 proteins	1410:1447	O-GlcNAc-modified SP1 and YY1 proteins	1410:1447	Reduced and increased levels of O-GlcNAc-modified SP1 and YY1 proteins were associated with stimulation or inhibition of HAS2 expression, respectively.
21795679	0	40	theme	synthase	64:71	arg1	expression					75:84	hyaluronan synthase 2 expression	53:84	hyaluronan synthase 2 expression	53:84	Cellular content of UDP-N-acetylhexosamines controls hyaluronan synthase 2 expression and correlates with O-linked N-acetylglucosamine modification of transcription factors YY1 and SP1.
21795679	5	41	theme	element-binding	1049:1063	arg1	protein					1065:1071	cAMP response element-binding protein	1035:1071	cAMP response element-binding protein	1035:1071	Tracing the UDP-HexNAc-initiated signal to the HAS2 promoter revealed no change in the binding of STAT3, NF-κB, and cAMP response element-binding protein, shown previously to mediate growth factor and cytokine signals on HAS2 expression.
21795679	5	42	theme	cAMP	1035:1038	arg1	protein					1065:1071	cAMP response element-binding protein	1035:1071	cAMP response element-binding protein	1035:1071	Tracing the UDP-HexNAc-initiated signal to the HAS2 promoter revealed no change in the binding of STAT3, NF-κB, and cAMP response element-binding protein, shown previously to mediate growth factor and cytokine signals on HAS2 expression.
21795679	5	43	from	change	992:997	arg1	binding					1006:1012	the binding	1002:1012	the binding of STAT3, NF-κB, and cAMP response element-binding protein	1002:1071	Tracing the UDP-HexNAc-initiated signal to the HAS2 promoter revealed no change in the binding of STAT3, NF-κB, and cAMP response element-binding protein, shown previously to mediate growth factor and cytokine signals on HAS2 expression.
21795679	1	44	theme	cell	253:256	arg1	surface					258:264	the vertebrate cell surface	238:264	the vertebrate cell surface	238:264	Hyaluronan, a high molecular mass polysaccharide on the vertebrate cell surface and extracellular matrix, is produced at the plasma membrane by hyaluronan synthases using UDP-GlcNAc and UDP-GlcUA as substrates.
21795679	7	45	theme	siRNA	1292:1296	arg1	silencing					1298:1306	siRNA silencing	1292:1306	siRNA silencing of YY1 and SP1	1292:1321	siRNA silencing of YY1 and SP1 confirmed their inhibitory effects on HAS2 expression.
21795679	9	46	theme	HAS2	1676:1679	arg1	transcription					1681:1693	HAS2 transcription	1676:1693	HAS2 transcription	1676:1693	Our data are consistent with the hypothesis that, by regulating the level of protein O-GlcNAc modifications, cellular UDP-HexNAc content controls HAS2 transcription and decreases the effects on hyaluronan synthesis that would result from cellular fluctuations of this substrate.
21795679	7	47	from	effects	1350:1356	arg1	expression					1366:1375	HAS2 expression	1361:1375	HAS2 expression	1361:1375	siRNA silencing of YY1 and SP1 confirmed their inhibitory effects on HAS2 expression.
21795679	3	48	theme	cellular	520:527	arg1	level					529:533	the cellular level	516:533	the cellular level of UDP-HexNAc	516:547	In this study, we show that the cellular level of UDP-HexNAc also controls hyaluronan synthesis by modulating the expression of HAS2 (hyaluronan synthase 2).
21795679	3	49	theme	hyaluronan	563:572	arg1	synthesis					574:582	hyaluronan synthesis	563:582	hyaluronan synthesis	563:582	In this study, we show that the cellular level of UDP-HexNAc also controls hyaluronan synthesis by modulating the expression of HAS2 (hyaluronan synthase 2).
21795679	6	50	theme	YY1	1193:1195	arg1	binding					1174:1180	altered binding	1166:1180	altered binding of SP1 and YY1 to the promoter	1166:1211	Instead, altered binding of SP1 and YY1 to the promoter correlated with cellular UDP-HexNAc content and inhibition of HAS2 expression.
21795679	6	51	theme	expression	1280:1289	arg1	inhibition					1261:1270	inhibition	1261:1270	inhibition of HAS2 expression	1261:1289	Instead, altered binding of SP1 and YY1 to the promoter correlated with cellular UDP-HexNAc content and inhibition of HAS2 expression.
21795679	6	51	theme	expression	1280:1289	arg1	content					1249:1255	cellular UDP-HexNAc content	1229:1255	cellular UDP-HexNAc content	1229:1255	Instead, altered binding of SP1 and YY1 to the promoter correlated with cellular UDP-HexNAc content and inhibition of HAS2 expression.
21795679	6	52	theme	SP1	1185:1187	arg1	binding					1174:1180	altered binding	1166:1180	altered binding of SP1 and YY1 to the promoter	1166:1211	Instead, altered binding of SP1 and YY1 to the promoter correlated with cellular UDP-HexNAc content and inhibition of HAS2 expression.
21795679	1	53	theme	molecular	205:213	arg1	Hyaluronan					186:195	Hyaluronan	186:195	Hyaluronan	186:195	Hyaluronan, a high molecular mass polysaccharide on the vertebrate cell surface and extracellular matrix, is produced at the plasma membrane by hyaluronan synthases using UDP-GlcNAc and UDP-GlcUA as substrates.
21795679	1	53	theme	molecular	205:213	arg1	polysaccharide					220:233	a high molecular mass polysaccharide	198:233	a high molecular mass polysaccharide on the vertebrate cell surface and extracellular matrix	198:289	Hyaluronan, a high molecular mass polysaccharide on the vertebrate cell surface and extracellular matrix, is produced at the plasma membrane by hyaluronan synthases using UDP-GlcNAc and UDP-GlcUA as substrates.
21795679	0	54	theme	factors	165:171	arg1	modification					135:146	O-linked N-acetylglucosamine modification	106:146	O-linked N-acetylglucosamine modification of transcription factors YY1 and SP1	106:183	Cellular content of UDP-N-acetylhexosamines controls hyaluronan synthase 2 expression and correlates with O-linked N-acetylglucosamine modification of transcription factors YY1 and SP1.
21795679	9	55	theme	cellular	1639:1646	arg1	content					1659:1665	cellular UDP-HexNAc content	1639:1665	cellular UDP-HexNAc content	1639:1665	Our data are consistent with the hypothesis that, by regulating the level of protein O-GlcNAc modifications, cellular UDP-HexNAc content controls HAS2 transcription and decreases the effects on hyaluronan synthesis that would result from cellular fluctuations of this substrate.
21795679	9	56	from	effects	1713:1719	arg1	synthesis					1735:1743	hyaluronan synthesis	1724:1743	hyaluronan synthesis that would result from cellular fluctuations of this substrate	1724:1806	Our data are consistent with the hypothesis that, by regulating the level of protein O-GlcNAc modifications, cellular UDP-HexNAc content controls HAS2 transcription and decreases the effects on hyaluronan synthesis that would result from cellular fluctuations of this substrate.
21795679	5	57	theme	factor	1109:1114	arg1	signals					1129:1135	growth factor and cytokine signals	1102:1135	growth factor and cytokine signals on HAS2 expression	1102:1154	Tracing the UDP-HexNAc-initiated signal to the HAS2 promoter revealed no change in the binding of STAT3, NF-κB, and cAMP response element-binding protein, shown previously to mediate growth factor and cytokine signals on HAS2 expression.
21795679	4	58	dep	realized	784:791	arg1	glutamine					834:842	glutamine:fructose-6-phosphate amidotransferase 1	834:882	glutamine:fructose-6-phosphate amidotransferase 1	834:882	Increasing UDP-HexNAc in HaCaT keratinocytes by adding glucosamine down-regulated HAS2 gene expression, whereas a decrease in UDP-HexNAc, realized by mannose treatment or siRNA for GFAT1 (glutamine:fructose-6-phosphate amidotransferase 1), enhanced expression of the gene.
21795679	4	58	dep	realized	784:791	arg1	decrease					760:767	a decrease	758:767	a decrease	758:767	Increasing UDP-HexNAc in HaCaT keratinocytes by adding glucosamine down-regulated HAS2 gene expression, whereas a decrease in UDP-HexNAc, realized by mannose treatment or siRNA for GFAT1 (glutamine:fructose-6-phosphate amidotransferase 1), enhanced expression of the gene.
21795679	8	59	theme	expression	1504:1513	arg1	inhibition					1485:1494	inhibition	1485:1494	inhibition of HAS2 expression	1485:1513	Reduced and increased levels of O-GlcNAc-modified SP1 and YY1 proteins were associated with stimulation or inhibition of HAS2 expression, respectively.
21795679	8	59	theme	expression	1504:1513	arg1	stimulation					1470:1480	stimulation	1470:1480	stimulation	1470:1480	Reduced and increased levels of O-GlcNAc-modified SP1 and YY1 proteins were associated with stimulation or inhibition of HAS2 expression, respectively.
21795679	6	60	theme	cellular	1229:1236	arg1	content					1249:1255	cellular UDP-HexNAc content	1229:1255	cellular UDP-HexNAc content	1229:1255	Instead, altered binding of SP1 and YY1 to the promoter correlated with cellular UDP-HexNAc content and inhibition of HAS2 expression.
21795679	5	61	theme	STAT3	1017:1021	arg1	binding					1006:1012	the binding	1002:1012	the binding of STAT3, NF-κB, and cAMP response element-binding protein	1002:1071	Tracing the UDP-HexNAc-initiated signal to the HAS2 promoter revealed no change in the binding of STAT3, NF-κB, and cAMP response element-binding protein, shown previously to mediate growth factor and cytokine signals on HAS2 expression.
21795679	0	62	dep	factors	165:171	arg1	YY1					173:175	YY1	173:175	YY1	173:175	Cellular content of UDP-N-acetylhexosamines controls hyaluronan synthase 2 expression and correlates with O-linked N-acetylglucosamine modification of transcription factors YY1 and SP1.
21795679	0	62	dep	factors	165:171	arg1	factors					165:171	transcription factors YY1 and SP1	151:183	transcription factors YY1 and SP1	151:183	Cellular content of UDP-N-acetylhexosamines controls hyaluronan synthase 2 expression and correlates with O-linked N-acetylglucosamine modification of transcription factors YY1 and SP1.
21795679	0	62	dep	factors	165:171	arg1	SP1					181:183	SP1	181:183	SP1	181:183	Cellular content of UDP-N-acetylhexosamines controls hyaluronan synthase 2 expression and correlates with O-linked N-acetylglucosamine modification of transcription factors YY1 and SP1.
21795679	4	63	theme	gene	733:736	arg1	expression					738:747	HAS2 gene expression	728:747	HAS2 gene expression	728:747	Increasing UDP-HexNAc in HaCaT keratinocytes by adding glucosamine down-regulated HAS2 gene expression, whereas a decrease in UDP-HexNAc, realized by mannose treatment or siRNA for GFAT1 (glutamine:fructose-6-phosphate amidotransferase 1), enhanced expression of the gene.
21795679	0	64	theme	N-acetylglucosamine	115:133	arg1	modification					135:146	O-linked N-acetylglucosamine modification	106:146	O-linked N-acetylglucosamine modification of transcription factors YY1 and SP1	106:183	Cellular content of UDP-N-acetylhexosamines controls hyaluronan synthase 2 expression and correlates with O-linked N-acetylglucosamine modification of transcription factors YY1 and SP1.
21795679	5	65	theme	cytokine	1120:1127	arg1	signals					1129:1135	growth factor and cytokine signals	1102:1135	growth factor and cytokine signals on HAS2 expression	1102:1154	Tracing the UDP-HexNAc-initiated signal to the HAS2 promoter revealed no change in the binding of STAT3, NF-κB, and cAMP response element-binding protein, shown previously to mediate growth factor and cytokine signals on HAS2 expression.
21795679	2	66	theme	UDP-sugar	423:431	arg1	substrates					433:442	these UDP-sugar substrates	417:442	these UDP-sugar substrates	417:442	The availability of these UDP-sugar substrates can limit the synthesis rate of hyaluronan.
21795679	5	67	from	signals	1129:1135	arg1	expression					1145:1154	HAS2 expression	1140:1154	HAS2 expression	1140:1154	Tracing the UDP-HexNAc-initiated signal to the HAS2 promoter revealed no change in the binding of STAT3, NF-κB, and cAMP response element-binding protein, shown previously to mediate growth factor and cytokine signals on HAS2 expression.
21795679	2	68	theme	hyaluronan	476:485	arg1	rate					468:471	the synthesis rate	454:471	the synthesis rate of hyaluronan	454:485	The availability of these UDP-sugar substrates can limit the synthesis rate of hyaluronan.
21795679	0	69	theme	UDP-N-acetylhexosamines	20:42	arg1	content					9:15	Cellular content	0:15	Cellular content of UDP-N-acetylhexosamines	0:42	Cellular content of UDP-N-acetylhexosamines controls hyaluronan synthase 2 expression and correlates with O-linked N-acetylglucosamine modification of transcription factors YY1 and SP1.
21795679	7	70	theme	SP1	1319:1321	arg1	silencing					1298:1306	siRNA silencing	1292:1306	siRNA silencing of YY1 and SP1	1292:1321	siRNA silencing of YY1 and SP1 confirmed their inhibitory effects on HAS2 expression.
21795679	0	71	theme	hyaluronan	53:62	arg1	synthase					64:71	hyaluronan synthase 2	53:73	hyaluronan synthase 2 expression	53:84	Cellular content of UDP-N-acetylhexosamines controls hyaluronan synthase 2 expression and correlates with O-linked N-acetylglucosamine modification of transcription factors YY1 and SP1.
21795679	9	72	theme	O-GlcNAc	1615:1622	arg1	modifications					1624:1636	protein O-GlcNAc modifications	1607:1636	protein O-GlcNAc modifications	1607:1636	Our data are consistent with the hypothesis that, by regulating the level of protein O-GlcNAc modifications, cellular UDP-HexNAc content controls HAS2 transcription and decreases the effects on hyaluronan synthesis that would result from cellular fluctuations of this substrate.
21795679	7	73	theme	YY1	1311:1313	arg1	silencing					1298:1306	siRNA silencing	1292:1306	siRNA silencing of YY1 and SP1	1292:1321	siRNA silencing of YY1 and SP1 confirmed their inhibitory effects on HAS2 expression.
21795679	8	74	theme	O-GlcNAc-modified	1410:1426	arg1	proteins					1440:1447	O-GlcNAc-modified SP1 and YY1 proteins	1410:1447	O-GlcNAc-modified SP1 and YY1 proteins	1410:1447	Reduced and increased levels of O-GlcNAc-modified SP1 and YY1 proteins were associated with stimulation or inhibition of HAS2 expression, respectively.
21795679	1	75	theme	hyaluronan	330:339	arg1	synthases					341:349	hyaluronan synthases	330:349	hyaluronan synthases using UDP-GlcNAc and UDP-GlcUA as substrates	330:394	Hyaluronan, a high molecular mass polysaccharide on the vertebrate cell surface and extracellular matrix, is produced at the plasma membrane by hyaluronan synthases using UDP-GlcNAc and UDP-GlcUA as substrates.
21795679	5	76	theme	response	1040:1047	arg1	protein					1065:1071	cAMP response element-binding protein	1035:1071	cAMP response element-binding protein	1035:1071	Tracing the UDP-HexNAc-initiated signal to the HAS2 promoter revealed no change in the binding of STAT3, NF-κB, and cAMP response element-binding protein, shown previously to mediate growth factor and cytokine signals on HAS2 expression.
21795679	4	77	theme	fructose-6-phosphate	844:863	arg1	amidotransferase					865:880	fructose-6-phosphate amidotransferase 1	844:882	glutamine:fructose-6-phosphate amidotransferase 1	834:882	Increasing UDP-HexNAc in HaCaT keratinocytes by adding glucosamine down-regulated HAS2 gene expression, whereas a decrease in UDP-HexNAc, realized by mannose treatment or siRNA for GFAT1 (glutamine:fructose-6-phosphate amidotransferase 1), enhanced expression of the gene.
21795679	4	78	from	decrease	760:767	arg1	UDP-HexNAc					772:781	UDP-HexNAc	772:781	UDP-HexNAc	772:781	Increasing UDP-HexNAc in HaCaT keratinocytes by adding glucosamine down-regulated HAS2 gene expression, whereas a decrease in UDP-HexNAc, realized by mannose treatment or siRNA for GFAT1 (glutamine:fructose-6-phosphate amidotransferase 1), enhanced expression of the gene.
21795679	9	79	theme	UDP-HexNAc	1648:1657	arg1	content					1659:1665	cellular UDP-HexNAc content	1639:1665	cellular UDP-HexNAc content	1639:1665	Our data are consistent with the hypothesis that, by regulating the level of protein O-GlcNAc modifications, cellular UDP-HexNAc content controls HAS2 transcription and decreases the effects on hyaluronan synthesis that would result from cellular fluctuations of this substrate.
21795679	0	80	mod	modification	135:146	arg1	YY1					173:175	YY1	173:175	YY1	173:175	Cellular content of UDP-N-acetylhexosamines controls hyaluronan synthase 2 expression and correlates with O-linked N-acetylglucosamine modification of transcription factors YY1 and SP1.
21795679	0	80	mod	modification	135:146	arg1	factors					165:171	transcription factors YY1 and SP1	151:183	transcription factors YY1 and SP1	151:183	Cellular content of UDP-N-acetylhexosamines controls hyaluronan synthase 2 expression and correlates with O-linked N-acetylglucosamine modification of transcription factors YY1 and SP1.
21795679	0	80	mod	modification	135:146	arg1	SP1					181:183	SP1	181:183	SP1	181:183	Cellular content of UDP-N-acetylhexosamines controls hyaluronan synthase 2 expression and correlates with O-linked N-acetylglucosamine modification of transcription factors YY1 and SP1.
21795679	0	80	mod	modification	135:146	arg3	N-acetylglucosamine					115:133	O-linked N-acetylglucosamine modification	106:146	O-linked N-acetylglucosamine modification of transcription factors YY1 and SP1	106:183	Cellular content of UDP-N-acetylhexosamines controls hyaluronan synthase 2 expression and correlates with O-linked N-acetylglucosamine modification of transcription factors YY1 and SP1.
21795679	8	81	theme	proteins	1440:1447	arg1	levels					1400:1405	Reduced and increased levels	1378:1405	Reduced and increased levels of O-GlcNAc-modified SP1 and YY1 proteins	1378:1447	Reduced and increased levels of O-GlcNAc-modified SP1 and YY1 proteins were associated with stimulation or inhibition of HAS2 expression, respectively.
21795679	4	82	dep	glutamine	834:842	arg1	amidotransferase					865:880	fructose-6-phosphate amidotransferase 1	844:882	glutamine:fructose-6-phosphate amidotransferase 1	834:882	Increasing UDP-HexNAc in HaCaT keratinocytes by adding glucosamine down-regulated HAS2 gene expression, whereas a decrease in UDP-HexNAc, realized by mannose treatment or siRNA for GFAT1 (glutamine:fructose-6-phosphate amidotransferase 1), enhanced expression of the gene.
21795679	5	83	theme	NF-κB	1024:1028	arg1	binding					1006:1012	the binding	1002:1012	the binding of STAT3, NF-κB, and cAMP response element-binding protein	1002:1071	Tracing the UDP-HexNAc-initiated signal to the HAS2 promoter revealed no change in the binding of STAT3, NF-κB, and cAMP response element-binding protein, shown previously to mediate growth factor and cytokine signals on HAS2 expression.
21795679	3	84	theme	UDP-HexNAc	538:547	arg1	level					529:533	the cellular level	516:533	the cellular level of UDP-HexNAc	516:547	In this study, we show that the cellular level of UDP-HexNAc also controls hyaluronan synthesis by modulating the expression of HAS2 (hyaluronan synthase 2).
21795679	1	85	theme	extracellular	270:282	arg1	matrix					284:289	extracellular matrix	270:289	extracellular matrix	270:289	Hyaluronan, a high molecular mass polysaccharide on the vertebrate cell surface and extracellular matrix, is produced at the plasma membrane by hyaluronan synthases using UDP-GlcNAc and UDP-GlcUA as substrates.
9111324	5	0	theme	mM	773:774	arg1	glucosamine					776:786	5 mM glucosamine	771:786	5 mM glucosamine	771:786	We found that Sp1 becomes hyperglycosylated when cells are exposed to 5 mM glucosamine, whereas under glucose starvation, stimulation with cyclic AMP (cAMP) results in nearly complete deglycosylation of this protein.
9111324	7	1	theme	glucosamine	1211:1221	arg1	synthesis					1223:1231	glucosamine synthesis	1211:1231	glucosamine synthesis	1211:1231	Treatment of cells with glucose or glucosamine protects Sp1 from cAMP-mediated degradation, whereas blockade of glucosamine synthesis abrogates glucose but not glucosamine protection.
9111324	7	2	theme	cells	1112:1116	arg1	Treatment					1099:1107	Treatment	1099:1107	Treatment of cells with glucose or glucosamine	1099:1144	Treatment of cells with glucose or glucosamine protects Sp1 from cAMP-mediated degradation, whereas blockade of glucosamine synthesis abrogates glucose but not glucosamine protection.
9111324	4	3	dep	observation	468:478	arg1	regulated					525:533	regulated	525:533	can be regulated by glucose and glucosamine in vascular smooth muscle cells	518:592	Based on an earlier observation that growth factor gene transcription can be regulated by glucose and glucosamine in vascular smooth muscle cells, we determined whether Sp1 glycosylation could be regulated and if this modification altered Sp1 function.
9111324	7	4	theme	synthesis	1223:1231	arg1	blockade					1199:1206	blockade	1199:1206	blockade of glucosamine synthesis	1199:1231	Treatment of cells with glucose or glucosamine protects Sp1 from cAMP-mediated degradation, whereas blockade of glucosamine synthesis abrogates glucose but not glucosamine protection.
9111324	9	5	theme	O-GlcNAc	1420:1427	arg1	modification					1429:1440	The O-GlcNAc modification	1416:1440	The O-GlcNAc modification of Sp1	1416:1447	The O-GlcNAc modification of Sp1 may play a role as a nutritional checkpoint.
9111324	11	6	theme	reduced	1649:1655	arg1	transcription					1665:1677	reduced general transcription	1649:1677	reduced general transcription	1649:1677	This process could potentially result in reduced general transcription, thereby conserving nutrients.
9111324	2	7	theme	such	298:301	arg1	genes					303:307	such genes	298:307	such genes	298:307	Most growth factors and receptors are also encoded by such genes.
9111324	4	8	theme	growth	485:490	arg1	transcription					504:516	growth factor gene transcription	485:516	growth factor gene transcription	485:516	Based on an earlier observation that growth factor gene transcription can be regulated by glucose and glucosamine in vascular smooth muscle cells, we determined whether Sp1 glycosylation could be regulated and if this modification altered Sp1 function.
9111324	3	9	theme	covalent	344:351	arg1	linkage					353:359	covalent linkage	344:359	covalent linkage of the monosaccharide N-acetylglucosamine (O-GlcNAc) to serine and threonine residues	344:445	Sp1 is multiply O glycosylated by covalent linkage of the monosaccharide N-acetylglucosamine (O-GlcNAc) to serine and threonine residues.
9111324	5	10	theme	protein	909:915	arg1	deglycosylation					885:899	nearly complete deglycosylation	869:899	nearly complete deglycosylation of this protein	869:915	We found that Sp1 becomes hyperglycosylated when cells are exposed to 5 mM glucosamine, whereas under glucose starvation, stimulation with cyclic AMP (cAMP) results in nearly complete deglycosylation of this protein.
9111324	6	11	gly	hypoglycosylated	940:955	arg1	state					957:961	this hypoglycosylated state	935:961	this hypoglycosylated state	935:961	Correlating with this hypoglycosylated state, Sp1 is rapidly proteolytically degraded by an enzyme(s) that can be inhibited by specific proteasome inhibitors, lactacystin and LLnL.
9111324	6	12	theme	proteasome	1054:1063	arg1	LLnL					1093:1096	LLnL	1093:1096	LLnL	1093:1096	Correlating with this hypoglycosylated state, Sp1 is rapidly proteolytically degraded by an enzyme(s) that can be inhibited by specific proteasome inhibitors, lactacystin and LLnL.
9111324	6	12	theme	proteasome	1054:1063	arg1	lactacystin					1077:1087	lactacystin	1077:1087	lactacystin	1077:1087	Correlating with this hypoglycosylated state, Sp1 is rapidly proteolytically degraded by an enzyme(s) that can be inhibited by specific proteasome inhibitors, lactacystin and LLnL.
9111324	6	12	theme	proteasome	1054:1063	arg1	inhibitors					1065:1074	specific proteasome inhibitors	1045:1074	specific proteasome inhibitors	1045:1074	Correlating with this hypoglycosylated state, Sp1 is rapidly proteolytically degraded by an enzyme(s) that can be inhibited by specific proteasome inhibitors, lactacystin and LLnL.
9111324	9	13	theme	Sp1	1445:1447	arg1	modification					1429:1440	The O-GlcNAc modification	1416:1440	The O-GlcNAc modification of Sp1	1416:1447	The O-GlcNAc modification of Sp1 may play a role as a nutritional checkpoint.
9111324	4	14	theme	gene	499:502	arg1	transcription					504:516	growth factor gene transcription	485:516	growth factor gene transcription	485:516	Based on an earlier observation that growth factor gene transcription can be regulated by glucose and glucosamine in vascular smooth muscle cells, we determined whether Sp1 glycosylation could be regulated and if this modification altered Sp1 function.
9111324	6	15	theme	enzyme	1010:1015	arg1	s					1017:1017	an enzyme(s)	1007:1018	an enzyme(s) that can be inhibited by specific proteasome inhibitors, lactacystin and LLnL	1007:1096	Correlating with this hypoglycosylated state, Sp1 is rapidly proteolytically degraded by an enzyme(s) that can be inhibited by specific proteasome inhibitors, lactacystin and LLnL.
9111324	8	16	theme	transcription	1342:1354	arg1	factors					1356:1362	E2F transcription factors	1338:1362	E2F transcription factors	1338:1362	This effect on Sp1 is specific, in that the Stat-3 and E2F transcription factors did not undergo degradation under these conditions.
9111324	0	17	theme	O	8:8	arg1	glycosylation					10:22	Reduced O glycosylation	0:22	Reduced O glycosylation of Sp1	0:29	Reduced O glycosylation of Sp1 is associated with increased proteasome susceptibility.
9111324	4	18	theme	factor	492:497	arg1	transcription					504:516	growth factor gene transcription	485:516	growth factor gene transcription	485:516	Based on an earlier observation that growth factor gene transcription can be regulated by glucose and glucosamine in vascular smooth muscle cells, we determined whether Sp1 glycosylation could be regulated and if this modification altered Sp1 function.
9111324	3	19	dep	serine	417:422	arg1	residues					438:445	residues	438:445	residues	438:445	Sp1 is multiply O glycosylated by covalent linkage of the monosaccharide N-acetylglucosamine (O-GlcNAc) to serine and threonine residues.
9111324	5	20	dep	becomes	719:725	arg1	whereas					789:795	whereas	789:795	whereas	789:795	We found that Sp1 becomes hyperglycosylated when cells are exposed to 5 mM glucosamine, whereas under glucose starvation, stimulation with cyclic AMP (cAMP) results in nearly complete deglycosylation of this protein.
9111324	5	21	with	stimulation	823:833	arg1	cAMP					852:855	cAMP	852:855	cAMP	852:855	We found that Sp1 becomes hyperglycosylated when cells are exposed to 5 mM glucosamine, whereas under glucose starvation, stimulation with cyclic AMP (cAMP) results in nearly complete deglycosylation of this protein.
9111324	5	21	with	stimulation	823:833	arg1	AMP					847:849	cyclic AMP	840:849	cyclic AMP (cAMP)	840:856	We found that Sp1 becomes hyperglycosylated when cells are exposed to 5 mM glucosamine, whereas under glucose starvation, stimulation with cyclic AMP (cAMP) results in nearly complete deglycosylation of this protein.
9111324	10	22	theme	adequate	1512:1519	arg1	nutrition					1521:1529	adequate nutrition	1512:1529	adequate nutrition	1512:1529	In the absence of adequate nutrition, Sp1 becomes hypoglycosylated and thereby subject to proteasome degradation.
9111324	4	23	theme	Sp1	687:689	arg1	function					691:698	Sp1 function	687:698	Sp1 function	687:698	Based on an earlier observation that growth factor gene transcription can be regulated by glucose and glucosamine in vascular smooth muscle cells, we determined whether Sp1 glycosylation could be regulated and if this modification altered Sp1 function.
9111324	0	24	theme	Reduced	0:6	arg1	glycosylation					10:22	Reduced O glycosylation	0:22	Reduced O glycosylation of Sp1	0:29	Reduced O glycosylation of Sp1 is associated with increased proteasome susceptibility.
9111324	4	25	theme	vascular	565:572	arg1	cells					588:592	vascular smooth muscle cells	565:592	vascular smooth muscle cells	565:592	Based on an earlier observation that growth factor gene transcription can be regulated by glucose and glucosamine in vascular smooth muscle cells, we determined whether Sp1 glycosylation could be regulated and if this modification altered Sp1 function.
9111324	1	26	theme	TATA-less	193:201	arg1	proteins					234:241	housekeeping proteins	221:241	housekeeping proteins	221:241	Sp1 is a ubiquitously expressed transcription factor that is particularly important for the regulation of TATA-less genes that encode housekeeping proteins.
9111324	1	26	theme	TATA-less	193:201	arg1	genes					203:207	TATA-less genes	193:207	TATA-less genes that encode housekeeping proteins	193:241	Sp1 is a ubiquitously expressed transcription factor that is particularly important for the regulation of TATA-less genes that encode housekeeping proteins.
9111324	3	27	theme	monosaccharide	368:381	arg1	O-GlcNAc					404:411	O-GlcNAc	404:411	O-GlcNAc	404:411	Sp1 is multiply O glycosylated by covalent linkage of the monosaccharide N-acetylglucosamine (O-GlcNAc) to serine and threonine residues.
9111324	3	27	theme	monosaccharide	368:381	arg1	N-acetylglucosamine					383:401	the monosaccharide N-acetylglucosamine	364:401	the monosaccharide N-acetylglucosamine (O-GlcNAc)	364:412	Sp1 is multiply O glycosylated by covalent linkage of the monosaccharide N-acetylglucosamine (O-GlcNAc) to serine and threonine residues.
9111324	1	28	theme	genes	203:207	arg1	regulation					179:188	the regulation	175:188	the regulation of TATA-less genes that encode housekeeping proteins	175:241	Sp1 is a ubiquitously expressed transcription factor that is particularly important for the regulation of TATA-less genes that encode housekeeping proteins.
9111324	3	29	theme	N-acetylglucosamine	383:401	arg1	linkage					353:359	covalent linkage	344:359	covalent linkage of the monosaccharide N-acetylglucosamine (O-GlcNAc) to serine and threonine residues	344:445	Sp1 is multiply O glycosylated by covalent linkage of the monosaccharide N-acetylglucosamine (O-GlcNAc) to serine and threonine residues.
9111324	4	30	theme	muscle	581:586	arg1	cells					588:592	vascular smooth muscle cells	565:592	vascular smooth muscle cells	565:592	Based on an earlier observation that growth factor gene transcription can be regulated by glucose and glucosamine in vascular smooth muscle cells, we determined whether Sp1 glycosylation could be regulated and if this modification altered Sp1 function.
9111324	8	31	from	effect	1288:1293	arg1	Sp1					1298:1300	Sp1	1298:1300	Sp1	1298:1300	This effect on Sp1 is specific, in that the Stat-3 and E2F transcription factors did not undergo degradation under these conditions.
9111324	7	32	theme	glucosamine	1259:1269	arg1	protection					1271:1280	glucosamine protection	1259:1280	glucose but not glucosamine protection	1243:1280	Treatment of cells with glucose or glucosamine protects Sp1 from cAMP-mediated degradation, whereas blockade of glucosamine synthesis abrogates glucose but not glucosamine protection.
9111324	4	33	from	glucosamine	550:560	arg1	cells					588:592	vascular smooth muscle cells	565:592	vascular smooth muscle cells	565:592	Based on an earlier observation that growth factor gene transcription can be regulated by glucose and glucosamine in vascular smooth muscle cells, we determined whether Sp1 glycosylation could be regulated and if this modification altered Sp1 function.
9111324	4	34	theme	smooth	574:579	arg1	cells					588:592	vascular smooth muscle cells	565:592	vascular smooth muscle cells	565:592	Based on an earlier observation that growth factor gene transcription can be regulated by glucose and glucosamine in vascular smooth muscle cells, we determined whether Sp1 glycosylation could be regulated and if this modification altered Sp1 function.
9111324	3	35	dep	glycosylated	328:339	arg1	O					326:326	O	326:326	O	326:326	Sp1 is multiply O glycosylated by covalent linkage of the monosaccharide N-acetylglucosamine (O-GlcNAc) to serine and threonine residues.
9111324	2	36	theme	growth	249:254	arg1	factors					256:262	Most growth factors	244:262	Most growth factors	244:262	Most growth factors and receptors are also encoded by such genes.
9111324	6	37	theme	specific	1045:1052	arg1	LLnL					1093:1096	LLnL	1093:1096	LLnL	1093:1096	Correlating with this hypoglycosylated state, Sp1 is rapidly proteolytically degraded by an enzyme(s) that can be inhibited by specific proteasome inhibitors, lactacystin and LLnL.
9111324	6	37	theme	specific	1045:1052	arg1	lactacystin					1077:1087	lactacystin	1077:1087	lactacystin	1077:1087	Correlating with this hypoglycosylated state, Sp1 is rapidly proteolytically degraded by an enzyme(s) that can be inhibited by specific proteasome inhibitors, lactacystin and LLnL.
9111324	6	37	theme	specific	1045:1052	arg1	inhibitors					1065:1074	specific proteasome inhibitors	1045:1074	specific proteasome inhibitors	1045:1074	Correlating with this hypoglycosylated state, Sp1 is rapidly proteolytically degraded by an enzyme(s) that can be inhibited by specific proteasome inhibitors, lactacystin and LLnL.
9111324	0	38	theme	Sp1	27:29	arg1	glycosylation					10:22	Reduced O glycosylation	0:22	Reduced O glycosylation of Sp1	0:29	Reduced O glycosylation of Sp1 is associated with increased proteasome susceptibility.
9111324	2	39	theme	Most	244:247	arg1	factors					256:262	Most growth factors	244:262	Most growth factors	244:262	Most growth factors and receptors are also encoded by such genes.
9111324	1	40	theme	housekeeping	221:232	arg1	proteins					234:241	housekeeping proteins	221:241	housekeeping proteins	221:241	Sp1 is a ubiquitously expressed transcription factor that is particularly important for the regulation of TATA-less genes that encode housekeeping proteins.
9111324	1	40	theme	housekeeping	221:232	arg1	genes					203:207	TATA-less genes	193:207	TATA-less genes that encode housekeeping proteins	193:241	Sp1 is a ubiquitously expressed transcription factor that is particularly important for the regulation of TATA-less genes that encode housekeeping proteins.
9111324	4	41	from	glucose	538:544	arg1	cells					588:592	vascular smooth muscle cells	565:592	vascular smooth muscle cells	565:592	Based on an earlier observation that growth factor gene transcription can be regulated by glucose and glucosamine in vascular smooth muscle cells, we determined whether Sp1 glycosylation could be regulated and if this modification altered Sp1 function.
9111324	5	42	gly	deglycosylation	885:899	arg1	protein					909:915	this protein	904:915	this protein	904:915	We found that Sp1 becomes hyperglycosylated when cells are exposed to 5 mM glucosamine, whereas under glucose starvation, stimulation with cyclic AMP (cAMP) results in nearly complete deglycosylation of this protein.
9111324	4	43	theme	earlier	460:466	arg1	observation					468:478	an earlier observation	457:478	an earlier observation that growth factor gene transcription can be regulated by glucose and glucosamine in vascular smooth muscle cells	457:592	Based on an earlier observation that growth factor gene transcription can be regulated by glucose and glucosamine in vascular smooth muscle cells, we determined whether Sp1 glycosylation could be regulated and if this modification altered Sp1 function.
9111324	0	44	gly	glycosylation	10:22	arg1	Sp1					27:29	Sp1	27:29	Sp1	27:29	Reduced O glycosylation of Sp1 is associated with increased proteasome susceptibility.
9111324	7	45	with	Treatment	1099:1107	arg1	glucosamine					1134:1144	glucosamine	1134:1144	glucosamine	1134:1144	Treatment of cells with glucose or glucosamine protects Sp1 from cAMP-mediated degradation, whereas blockade of glucosamine synthesis abrogates glucose but not glucosamine protection.
9111324	7	45	with	Treatment	1099:1107	arg1	glucose					1123:1129	glucose	1123:1129	glucose	1123:1129	Treatment of cells with glucose or glucosamine protects Sp1 from cAMP-mediated degradation, whereas blockade of glucosamine synthesis abrogates glucose but not glucosamine protection.
9111324	1	46	theme	expressed	109:117	arg1	factor					133:138	a ubiquitously expressed transcription factor	94:138	a ubiquitously expressed transcription factor that is particularly important for the regulation of TATA-less genes that encode housekeeping proteins	94:241	Sp1 is a ubiquitously expressed transcription factor that is particularly important for the regulation of TATA-less genes that encode housekeeping proteins.
9111324	1	46	theme	expressed	109:117	arg1	important					161:169	important	161:169	important	161:169	Sp1 is a ubiquitously expressed transcription factor that is particularly important for the regulation of TATA-less genes that encode housekeeping proteins.
9111324	1	46	theme	expressed	109:117	arg1	Sp1					87:89	Sp1	87:89	Sp1	87:89	Sp1 is a ubiquitously expressed transcription factor that is particularly important for the regulation of TATA-less genes that encode housekeeping proteins.
9111324	5	47	theme	glucose	803:809	arg1	starvation					811:820	glucose starvation	803:820	glucose starvation	803:820	We found that Sp1 becomes hyperglycosylated when cells are exposed to 5 mM glucosamine, whereas under glucose starvation, stimulation with cyclic AMP (cAMP) results in nearly complete deglycosylation of this protein.
9111324	6	48	theme	hypoglycosylated	940:955	arg1	state					957:961	this hypoglycosylated state	935:961	this hypoglycosylated state	935:961	Correlating with this hypoglycosylated state, Sp1 is rapidly proteolytically degraded by an enzyme(s) that can be inhibited by specific proteasome inhibitors, lactacystin and LLnL.
9111324	3	49	gly	glycosylated	328:339	arg1	Sp1					310:312	Sp1	310:312	Sp1	310:312	Sp1 is multiply O glycosylated by covalent linkage of the monosaccharide N-acetylglucosamine (O-GlcNAc) to serine and threonine residues.
9111324	1	50	theme	transcription	119:131	arg1	factor					133:138	a ubiquitously expressed transcription factor	94:138	a ubiquitously expressed transcription factor that is particularly important for the regulation of TATA-less genes that encode housekeeping proteins	94:241	Sp1 is a ubiquitously expressed transcription factor that is particularly important for the regulation of TATA-less genes that encode housekeeping proteins.
9111324	1	50	theme	transcription	119:131	arg1	important					161:169	important	161:169	important	161:169	Sp1 is a ubiquitously expressed transcription factor that is particularly important for the regulation of TATA-less genes that encode housekeeping proteins.
9111324	1	50	theme	transcription	119:131	arg1	Sp1					87:89	Sp1	87:89	Sp1	87:89	Sp1 is a ubiquitously expressed transcription factor that is particularly important for the regulation of TATA-less genes that encode housekeeping proteins.
9111324	10	51	dep	nutrition	1521:1529	arg1	the					1497:1499	the	1497:1499	the	1497:1499	In the absence of adequate nutrition, Sp1 becomes hypoglycosylated and thereby subject to proteasome degradation.
9111324	10	51	dep	nutrition	1521:1529	arg1	absence					1501:1507	absence	1501:1507	absence	1501:1507	In the absence of adequate nutrition, Sp1 becomes hypoglycosylated and thereby subject to proteasome degradation.
9111324	5	52	theme	5	771:771	arg1	mM					773:774	mM	773:774	mM	773:774	We found that Sp1 becomes hyperglycosylated when cells are exposed to 5 mM glucosamine, whereas under glucose starvation, stimulation with cyclic AMP (cAMP) results in nearly complete deglycosylation of this protein.
9111324	4	53	theme	Sp1	617:619	arg1	glycosylation					621:633	Sp1 glycosylation	617:633	Sp1 glycosylation	617:633	Based on an earlier observation that growth factor gene transcription can be regulated by glucose and glucosamine in vascular smooth muscle cells, we determined whether Sp1 glycosylation could be regulated and if this modification altered Sp1 function.
9111324	8	54	theme	E2F	1338:1340	arg1	factors					1356:1362	E2F transcription factors	1338:1362	E2F transcription factors	1338:1362	This effect on Sp1 is specific, in that the Stat-3 and E2F transcription factors did not undergo degradation under these conditions.
9111324	0	55	theme	proteasome	60:69	arg1	susceptibility					71:84	increased proteasome susceptibility	50:84	increased proteasome susceptibility	50:84	Reduced O glycosylation of Sp1 is associated with increased proteasome susceptibility.
9111324	9	56	theme	nutritional	1470:1480	arg1	checkpoint					1482:1491	a nutritional checkpoint	1468:1491	a nutritional checkpoint	1468:1491	The O-GlcNAc modification of Sp1 may play a role as a nutritional checkpoint.
9111324	9	56	theme	nutritional	1470:1480	arg1	role					1460:1463	a role	1458:1463	a role	1458:1463	The O-GlcNAc modification of Sp1 may play a role as a nutritional checkpoint.
9111324	5	57	theme	cyclic	840:845	arg1	cAMP					852:855	cAMP	852:855	cAMP	852:855	We found that Sp1 becomes hyperglycosylated when cells are exposed to 5 mM glucosamine, whereas under glucose starvation, stimulation with cyclic AMP (cAMP) results in nearly complete deglycosylation of this protein.
9111324	5	57	theme	cyclic	840:845	arg1	AMP					847:849	cyclic AMP	840:849	cyclic AMP (cAMP)	840:856	We found that Sp1 becomes hyperglycosylated when cells are exposed to 5 mM glucosamine, whereas under glucose starvation, stimulation with cyclic AMP (cAMP) results in nearly complete deglycosylation of this protein.
9111324	5	58	theme	complete	876:883	arg1	deglycosylation					885:899	nearly complete deglycosylation	869:899	nearly complete deglycosylation of this protein	869:915	We found that Sp1 becomes hyperglycosylated when cells are exposed to 5 mM glucosamine, whereas under glucose starvation, stimulation with cyclic AMP (cAMP) results in nearly complete deglycosylation of this protein.
9111324	0	59	theme	increased	50:58	arg1	susceptibility					71:84	increased proteasome susceptibility	50:84	increased proteasome susceptibility	50:84	Reduced O glycosylation of Sp1 is associated with increased proteasome susceptibility.
9111324	11	60	theme	general	1657:1663	arg1	transcription					1665:1677	reduced general transcription	1649:1677	reduced general transcription	1649:1677	This process could potentially result in reduced general transcription, thereby conserving nutrients.
9111324	10	61	theme	proteasome	1584:1593	arg1	degradation					1595:1605	proteasome degradation	1584:1605	proteasome degradation	1584:1605	In the absence of adequate nutrition, Sp1 becomes hypoglycosylated and thereby subject to proteasome degradation.
9111324	7	62	theme	cAMP-mediated	1164:1176	arg1	degradation					1178:1188	cAMP-mediated degradation	1164:1188	cAMP-mediated degradation	1164:1188	Treatment of cells with glucose or glucosamine protects Sp1 from cAMP-mediated degradation, whereas blockade of glucosamine synthesis abrogates glucose but not glucosamine protection.
20699577	5	0	theme	target	852:857	arg1	promoters					859:867	the target promoters	848:867	the target promoters	848:867	Since these pairs of transcription factors bind the target promoters cooperatively and DNA binding of Sp1 alone is not affected by O-GlcNAc, our results imply that O-GlcNAc weakens the DNA binding of Sp1 and its cooperative binding partners by inhibiting stable interaction on DNA templates.
20699577	4	1	theme	O-GlcNAc	777:784	arg1	modification					786:797	elevated O-GlcNAc modification	768:797	elevated O-GlcNAc modification	768:797	Chromatin immunoprecipitation assays on cells in which O-GlcNAc was modulated pharmacologically revealed that Sp1-Oct1- and Sp1-Elf-1-paired occupancies of previously known target promoter regions were suppressed by elevated O-GlcNAc modification.
20699577	1	2	theme	eukaryotes	258:267	arg1	proteins					246:253	nucleocytoplasmic proteins	228:253	nucleocytoplasmic proteins of eukaryotes	228:267	O-Linked N-acetylglucosamine (O-GlcNAc), a single GlcNAc modification of proteins, is abundant in nucleocytoplasmic proteins of eukaryotes.
20699577	4	3	theme	elevated	768:775	arg1	modification					786:797	elevated O-GlcNAc modification	768:797	elevated O-GlcNAc modification	768:797	Chromatin immunoprecipitation assays on cells in which O-GlcNAc was modulated pharmacologically revealed that Sp1-Oct1- and Sp1-Elf-1-paired occupancies of previously known target promoter regions were suppressed by elevated O-GlcNAc modification.
20699577	0	4	link	O-linked	9:16	arg1	N-acetylglucosamine					18:36	Elevated O-linked N-acetylglucosamine	0:36	Elevated O-linked N-acetylglucosamine	0:36	Elevated O-linked N-acetylglucosamine correlated with reduced Sp1 cooperative DNA binding with its collaborating factors in vivo.
20699577	5	5	theme	partners	1032:1039	arg1	binding					989:995	the DNA binding	981:995	the DNA binding of Sp1 and its cooperative binding partners	981:1039	Since these pairs of transcription factors bind the target promoters cooperatively and DNA binding of Sp1 alone is not affected by O-GlcNAc, our results imply that O-GlcNAc weakens the DNA binding of Sp1 and its cooperative binding partners by inhibiting stable interaction on DNA templates.
20699577	4	6	theme	promoter	732:739	arg1	regions					741:747	previously known target promoter regions	708:747	previously known target promoter regions	708:747	Chromatin immunoprecipitation assays on cells in which O-GlcNAc was modulated pharmacologically revealed that Sp1-Oct1- and Sp1-Elf-1-paired occupancies of previously known target promoter regions were suppressed by elevated O-GlcNAc modification.
20699577	3	7	theme	cooperative	436:446	arg1	binding					448:454	cooperative binding	436:454	cooperative binding of Sp1 and its collaborating transcription factors, Oct1 and Elf-1, onto DNA templates	436:541	This study suggested the possibility that O-GlcNAc regulates cooperative binding of Sp1 and its collaborating transcription factors, Oct1 and Elf-1, onto DNA templates in vivo.
20699577	0	8	theme	collaborating	99:111	arg1	factors					113:119	its collaborating factors	95:119	its collaborating factors	95:119	Elevated O-linked N-acetylglucosamine correlated with reduced Sp1 cooperative DNA binding with its collaborating factors in vivo.
20699577	0	9	with	binding	82:88	arg1	factors					113:119	its collaborating factors	95:119	its collaborating factors	95:119	Elevated O-linked N-acetylglucosamine correlated with reduced Sp1 cooperative DNA binding with its collaborating factors in vivo.
20699577	5	10	theme	transcription	821:833	arg1	factors					835:841	transcription factors	821:841	transcription factors	821:841	Since these pairs of transcription factors bind the target promoters cooperatively and DNA binding of Sp1 alone is not affected by O-GlcNAc, our results imply that O-GlcNAc weakens the DNA binding of Sp1 and its cooperative binding partners by inhibiting stable interaction on DNA templates.
20699577	4	11	gly	occupancies	693:703	arg2	regions					741:747	previously known target promoter regions	708:747	previously known target promoter regions	708:747	Chromatin immunoprecipitation assays on cells in which O-GlcNAc was modulated pharmacologically revealed that Sp1-Oct1- and Sp1-Elf-1-paired occupancies of previously known target promoter regions were suppressed by elevated O-GlcNAc modification.
20699577	2	12	theme	regulator	299:307	arg1	proteins					309:316	Most nuclear transcriptional regulator proteins	270:316	Most nuclear transcriptional regulator proteins	270:316	Most nuclear transcriptional regulator proteins carry O-GlcNAc, implicating O-GlcNAc in gene regulation.
20699577	1	13	theme	single	173:178	arg1	modification					187:198	a single GlcNAc modification	171:198	a single GlcNAc modification of proteins	171:210	O-Linked N-acetylglucosamine (O-GlcNAc), a single GlcNAc modification of proteins, is abundant in nucleocytoplasmic proteins of eukaryotes.
20699577	1	13	theme	single	173:178	arg1	N-acetylglucosamine					139:157	O-Linked N-acetylglucosamine	130:157	O-Linked N-acetylglucosamine (O-GlcNAc)	130:168	O-Linked N-acetylglucosamine (O-GlcNAc), a single GlcNAc modification of proteins, is abundant in nucleocytoplasmic proteins of eukaryotes.
20699577	5	14	theme	factors	835:841	arg1	pairs					812:816	these pairs	806:816	these pairs of transcription factors	806:841	Since these pairs of transcription factors bind the target promoters cooperatively and DNA binding of Sp1 alone is not affected by O-GlcNAc, our results imply that O-GlcNAc weakens the DNA binding of Sp1 and its cooperative binding partners by inhibiting stable interaction on DNA templates.
20699577	2	15	theme	transcriptional	283:297	arg1	proteins					309:316	Most nuclear transcriptional regulator proteins	270:316	Most nuclear transcriptional regulator proteins	270:316	Most nuclear transcriptional regulator proteins carry O-GlcNAc, implicating O-GlcNAc in gene regulation.
20699577	5	16	from	interaction	1062:1072	arg1	templates					1081:1089	DNA templates	1077:1089	DNA templates	1077:1089	Since these pairs of transcription factors bind the target promoters cooperatively and DNA binding of Sp1 alone is not affected by O-GlcNAc, our results imply that O-GlcNAc weakens the DNA binding of Sp1 and its cooperative binding partners by inhibiting stable interaction on DNA templates.
20699577	1	17	theme	GlcNAc	180:185	arg1	modification					187:198	a single GlcNAc modification	171:198	a single GlcNAc modification of proteins	171:210	O-Linked N-acetylglucosamine (O-GlcNAc), a single GlcNAc modification of proteins, is abundant in nucleocytoplasmic proteins of eukaryotes.
20699577	1	17	theme	GlcNAc	180:185	arg1	N-acetylglucosamine					139:157	O-Linked N-acetylglucosamine	130:157	O-Linked N-acetylglucosamine (O-GlcNAc)	130:168	O-Linked N-acetylglucosamine (O-GlcNAc), a single GlcNAc modification of proteins, is abundant in nucleocytoplasmic proteins of eukaryotes.
20699577	0	18	theme	O-linked	9:16	arg1	N-acetylglucosamine					18:36	Elevated O-linked N-acetylglucosamine	0:36	Elevated O-linked N-acetylglucosamine	0:36	Elevated O-linked N-acetylglucosamine correlated with reduced Sp1 cooperative DNA binding with its collaborating factors in vivo.
20699577	4	19	theme	target	725:730	arg1	regions					741:747	previously known target promoter regions	708:747	previously known target promoter regions	708:747	Chromatin immunoprecipitation assays on cells in which O-GlcNAc was modulated pharmacologically revealed that Sp1-Oct1- and Sp1-Elf-1-paired occupancies of previously known target promoter regions were suppressed by elevated O-GlcNAc modification.
20699577	0	20	theme	Elevated	0:7	arg1	N-acetylglucosamine					18:36	Elevated O-linked N-acetylglucosamine	0:36	Elevated O-linked N-acetylglucosamine	0:36	Elevated O-linked N-acetylglucosamine correlated with reduced Sp1 cooperative DNA binding with its collaborating factors in vivo.
20699577	4	21	theme	regions	741:747	arg1	occupancies					693:703	Sp1-Oct1- and Sp1-Elf-1-paired occupancies	662:703	Sp1-Oct1- and Sp1-Elf-1-paired occupancies of previously known target promoter regions	662:747	Chromatin immunoprecipitation assays on cells in which O-GlcNAc was modulated pharmacologically revealed that Sp1-Oct1- and Sp1-Elf-1-paired occupancies of previously known target promoter regions were suppressed by elevated O-GlcNAc modification.
20699577	5	22	theme	Sp1	902:904	arg1	binding					891:897	DNA binding	887:897	DNA binding of Sp1 alone	887:910	Since these pairs of transcription factors bind the target promoters cooperatively and DNA binding of Sp1 alone is not affected by O-GlcNAc, our results imply that O-GlcNAc weakens the DNA binding of Sp1 and its cooperative binding partners by inhibiting stable interaction on DNA templates.
20699577	5	23	theme	DNA	887:889	arg1	binding					891:897	DNA binding	887:897	DNA binding of Sp1 alone	887:910	Since these pairs of transcription factors bind the target promoters cooperatively and DNA binding of Sp1 alone is not affected by O-GlcNAc, our results imply that O-GlcNAc weakens the DNA binding of Sp1 and its cooperative binding partners by inhibiting stable interaction on DNA templates.
20699577	1	24	theme	proteins	203:210	arg1	modification					187:198	a single GlcNAc modification	171:198	a single GlcNAc modification of proteins	171:210	O-Linked N-acetylglucosamine (O-GlcNAc), a single GlcNAc modification of proteins, is abundant in nucleocytoplasmic proteins of eukaryotes.
20699577	1	24	theme	proteins	203:210	arg1	N-acetylglucosamine					139:157	O-Linked N-acetylglucosamine	130:157	O-Linked N-acetylglucosamine (O-GlcNAc)	130:168	O-Linked N-acetylglucosamine (O-GlcNAc), a single GlcNAc modification of proteins, is abundant in nucleocytoplasmic proteins of eukaryotes.
20699577	3	25	theme	DNA	529:531	arg1	templates					533:541	DNA templates	529:541	DNA templates	529:541	This study suggested the possibility that O-GlcNAc regulates cooperative binding of Sp1 and its collaborating transcription factors, Oct1 and Elf-1, onto DNA templates in vivo.
20699577	0	26	theme	reduced	54:60	arg1	binding					82:88	reduced Sp1 cooperative DNA binding	54:88	reduced Sp1 cooperative DNA binding with its collaborating factors	54:119	Elevated O-linked N-acetylglucosamine correlated with reduced Sp1 cooperative DNA binding with its collaborating factors in vivo.
20699577	2	27	contain	carry	318:322	arg1	proteins					309:316	Most nuclear transcriptional regulator proteins	270:316	Most nuclear transcriptional regulator proteins	270:316	Most nuclear transcriptional regulator proteins carry O-GlcNAc, implicating O-GlcNAc in gene regulation.
20699577	2	27	contain	carry	318:322	arg2	O-GlcNAc					324:331	O-GlcNAc	324:331	O-GlcNAc	324:331	Most nuclear transcriptional regulator proteins carry O-GlcNAc, implicating O-GlcNAc in gene regulation.
20699577	4	28	theme	known	719:723	arg1	regions					741:747	previously known target promoter regions	708:747	previously known target promoter regions	708:747	Chromatin immunoprecipitation assays on cells in which O-GlcNAc was modulated pharmacologically revealed that Sp1-Oct1- and Sp1-Elf-1-paired occupancies of previously known target promoter regions were suppressed by elevated O-GlcNAc modification.
20699577	3	29	theme	factors	499:505	arg1	binding					448:454	cooperative binding	436:454	cooperative binding of Sp1 and its collaborating transcription factors, Oct1 and Elf-1, onto DNA templates	436:541	This study suggested the possibility that O-GlcNAc regulates cooperative binding of Sp1 and its collaborating transcription factors, Oct1 and Elf-1, onto DNA templates in vivo.
20699577	3	30	theme	Sp1	459:461	arg1	binding					448:454	cooperative binding	436:454	cooperative binding of Sp1 and its collaborating transcription factors, Oct1 and Elf-1, onto DNA templates	436:541	This study suggested the possibility that O-GlcNAc regulates cooperative binding of Sp1 and its collaborating transcription factors, Oct1 and Elf-1, onto DNA templates in vivo.
20699577	4	31	theme	immunoprecipitation	562:580	arg1	assays					582:587	Chromatin immunoprecipitation assays	552:587	Chromatin immunoprecipitation assays on cells in which O-GlcNAc was modulated pharmacologically	552:646	Chromatin immunoprecipitation assays on cells in which O-GlcNAc was modulated pharmacologically revealed that Sp1-Oct1- and Sp1-Elf-1-paired occupancies of previously known target promoter regions were suppressed by elevated O-GlcNAc modification.
20699577	4	32	from	assays	582:587	arg1	cells					592:596	cells	592:596	cells in which O-GlcNAc was modulated pharmacologically	592:646	Chromatin immunoprecipitation assays on cells in which O-GlcNAc was modulated pharmacologically revealed that Sp1-Oct1- and Sp1-Elf-1-paired occupancies of previously known target promoter regions were suppressed by elevated O-GlcNAc modification.
20699577	0	33	theme	cooperative	66:76	arg1	binding					82:88	reduced Sp1 cooperative DNA binding	54:88	reduced Sp1 cooperative DNA binding with its collaborating factors	54:119	Elevated O-linked N-acetylglucosamine correlated with reduced Sp1 cooperative DNA binding with its collaborating factors in vivo.
20699577	4	34	theme	Chromatin	552:560	arg1	assays					582:587	Chromatin immunoprecipitation assays	552:587	Chromatin immunoprecipitation assays on cells in which O-GlcNAc was modulated pharmacologically	552:646	Chromatin immunoprecipitation assays on cells in which O-GlcNAc was modulated pharmacologically revealed that Sp1-Oct1- and Sp1-Elf-1-paired occupancies of previously known target promoter regions were suppressed by elevated O-GlcNAc modification.
20699577	1	35	from	proteins	246:253	arg1	abundant					216:223	abundant	216:223	abundant	216:223	O-Linked N-acetylglucosamine (O-GlcNAc), a single GlcNAc modification of proteins, is abundant in nucleocytoplasmic proteins of eukaryotes.
20699577	3	36	theme	collaborating	471:483	arg1	Elf-1					517:521	Elf-1	517:521	Elf-1	517:521	This study suggested the possibility that O-GlcNAc regulates cooperative binding of Sp1 and its collaborating transcription factors, Oct1 and Elf-1, onto DNA templates in vivo.
20699577	3	36	theme	collaborating	471:483	arg1	Oct1					508:511	Oct1	508:511	Oct1	508:511	This study suggested the possibility that O-GlcNAc regulates cooperative binding of Sp1 and its collaborating transcription factors, Oct1 and Elf-1, onto DNA templates in vivo.
20699577	3	36	theme	collaborating	471:483	arg1	factors					499:505	its collaborating transcription factors	467:505	its collaborating transcription factors	467:505	This study suggested the possibility that O-GlcNAc regulates cooperative binding of Sp1 and its collaborating transcription factors, Oct1 and Elf-1, onto DNA templates in vivo.
20699577	1	37	from	abundant	216:223	arg1	proteins					246:253	nucleocytoplasmic proteins	228:253	nucleocytoplasmic proteins of eukaryotes	228:267	O-Linked N-acetylglucosamine (O-GlcNAc), a single GlcNAc modification of proteins, is abundant in nucleocytoplasmic proteins of eukaryotes.
20699577	5	38	theme	DNA	985:987	arg1	binding					989:995	the DNA binding	981:995	the DNA binding of Sp1 and its cooperative binding partners	981:1039	Since these pairs of transcription factors bind the target promoters cooperatively and DNA binding of Sp1 alone is not affected by O-GlcNAc, our results imply that O-GlcNAc weakens the DNA binding of Sp1 and its cooperative binding partners by inhibiting stable interaction on DNA templates.
20699577	0	39	theme	Sp1	62:64	arg1	binding					82:88	reduced Sp1 cooperative DNA binding	54:88	reduced Sp1 cooperative DNA binding with its collaborating factors	54:119	Elevated O-linked N-acetylglucosamine correlated with reduced Sp1 cooperative DNA binding with its collaborating factors in vivo.
20699577	1	40	mod	modification	187:198	arg3	GlcNAc					180:185	a single GlcNAc modification	171:198	a single GlcNAc modification of proteins	171:210	O-Linked N-acetylglucosamine (O-GlcNAc), a single GlcNAc modification of proteins, is abundant in nucleocytoplasmic proteins of eukaryotes.
20699577	1	40	mod	modification	187:198	arg1	proteins					203:210	proteins	203:210	proteins	203:210	O-Linked N-acetylglucosamine (O-GlcNAc), a single GlcNAc modification of proteins, is abundant in nucleocytoplasmic proteins of eukaryotes.
20699577	2	41	theme	nuclear	275:281	arg1	proteins					309:316	Most nuclear transcriptional regulator proteins	270:316	Most nuclear transcriptional regulator proteins	270:316	Most nuclear transcriptional regulator proteins carry O-GlcNAc, implicating O-GlcNAc in gene regulation.
20699577	2	42	theme	gene	358:361	arg1	regulation					363:372	gene regulation	358:372	gene regulation	358:372	Most nuclear transcriptional regulator proteins carry O-GlcNAc, implicating O-GlcNAc in gene regulation.
20699577	5	43	theme	cooperative	1012:1022	arg1	partners					1032:1039	its cooperative binding partners	1008:1039	its cooperative binding partners	1008:1039	Since these pairs of transcription factors bind the target promoters cooperatively and DNA binding of Sp1 alone is not affected by O-GlcNAc, our results imply that O-GlcNAc weakens the DNA binding of Sp1 and its cooperative binding partners by inhibiting stable interaction on DNA templates.
20699577	4	44	theme	Sp1-Oct1-	662:670	arg1	occupancies					693:703	Sp1-Oct1- and Sp1-Elf-1-paired occupancies	662:703	Sp1-Oct1- and Sp1-Elf-1-paired occupancies of previously known target promoter regions	662:747	Chromatin immunoprecipitation assays on cells in which O-GlcNAc was modulated pharmacologically revealed that Sp1-Oct1- and Sp1-Elf-1-paired occupancies of previously known target promoter regions were suppressed by elevated O-GlcNAc modification.
20699577	5	45	theme	stable	1055:1060	arg1	interaction					1062:1072	stable interaction	1055:1072	stable interaction on DNA templates	1055:1089	Since these pairs of transcription factors bind the target promoters cooperatively and DNA binding of Sp1 alone is not affected by O-GlcNAc, our results imply that O-GlcNAc weakens the DNA binding of Sp1 and its cooperative binding partners by inhibiting stable interaction on DNA templates.
20699577	2	46	theme	Most	270:273	arg1	proteins					309:316	Most nuclear transcriptional regulator proteins	270:316	Most nuclear transcriptional regulator proteins	270:316	Most nuclear transcriptional regulator proteins carry O-GlcNAc, implicating O-GlcNAc in gene regulation.
20699577	5	47	theme	Sp1	1000:1002	arg1	binding					989:995	the DNA binding	981:995	the DNA binding of Sp1 and its cooperative binding partners	981:1039	Since these pairs of transcription factors bind the target promoters cooperatively and DNA binding of Sp1 alone is not affected by O-GlcNAc, our results imply that O-GlcNAc weakens the DNA binding of Sp1 and its cooperative binding partners by inhibiting stable interaction on DNA templates.
20699577	1	48	theme	nucleocytoplasmic	228:244	arg1	proteins					246:253	nucleocytoplasmic proteins	228:253	nucleocytoplasmic proteins of eukaryotes	228:267	O-Linked N-acetylglucosamine (O-GlcNAc), a single GlcNAc modification of proteins, is abundant in nucleocytoplasmic proteins of eukaryotes.
20699577	3	49	theme	transcription	485:497	arg1	Elf-1					517:521	Elf-1	517:521	Elf-1	517:521	This study suggested the possibility that O-GlcNAc regulates cooperative binding of Sp1 and its collaborating transcription factors, Oct1 and Elf-1, onto DNA templates in vivo.
20699577	3	49	theme	transcription	485:497	arg1	Oct1					508:511	Oct1	508:511	Oct1	508:511	This study suggested the possibility that O-GlcNAc regulates cooperative binding of Sp1 and its collaborating transcription factors, Oct1 and Elf-1, onto DNA templates in vivo.
20699577	3	49	theme	transcription	485:497	arg1	factors					499:505	its collaborating transcription factors	467:505	its collaborating transcription factors	467:505	This study suggested the possibility that O-GlcNAc regulates cooperative binding of Sp1 and its collaborating transcription factors, Oct1 and Elf-1, onto DNA templates in vivo.
20699577	5	50	theme	DNA	1077:1079	arg1	templates					1081:1089	DNA templates	1077:1089	DNA templates	1077:1089	Since these pairs of transcription factors bind the target promoters cooperatively and DNA binding of Sp1 alone is not affected by O-GlcNAc, our results imply that O-GlcNAc weakens the DNA binding of Sp1 and its cooperative binding partners by inhibiting stable interaction on DNA templates.
20699577	5	51	theme	binding	1024:1030	arg1	partners					1032:1039	its cooperative binding partners	1008:1039	its cooperative binding partners	1008:1039	Since these pairs of transcription factors bind the target promoters cooperatively and DNA binding of Sp1 alone is not affected by O-GlcNAc, our results imply that O-GlcNAc weakens the DNA binding of Sp1 and its cooperative binding partners by inhibiting stable interaction on DNA templates.
20699577	1	52	theme	O-Linked	130:137	arg1	N-acetylglucosamine					139:157	O-Linked N-acetylglucosamine	130:157	O-Linked N-acetylglucosamine (O-GlcNAc)	130:168	O-Linked N-acetylglucosamine (O-GlcNAc), a single GlcNAc modification of proteins, is abundant in nucleocytoplasmic proteins of eukaryotes.
20699577	1	52	theme	O-Linked	130:137	arg1	modification					187:198	a single GlcNAc modification	171:198	a single GlcNAc modification of proteins	171:210	O-Linked N-acetylglucosamine (O-GlcNAc), a single GlcNAc modification of proteins, is abundant in nucleocytoplasmic proteins of eukaryotes.
20699577	1	52	theme	O-Linked	130:137	arg1	O-GlcNAc					160:167	O-GlcNAc	160:167	O-GlcNAc	160:167	O-Linked N-acetylglucosamine (O-GlcNAc), a single GlcNAc modification of proteins, is abundant in nucleocytoplasmic proteins of eukaryotes.
20699577	4	53	theme	Sp1-Elf-1-paired	676:691	arg1	occupancies					693:703	Sp1-Oct1- and Sp1-Elf-1-paired occupancies	662:703	Sp1-Oct1- and Sp1-Elf-1-paired occupancies of previously known target promoter regions	662:747	Chromatin immunoprecipitation assays on cells in which O-GlcNAc was modulated pharmacologically revealed that Sp1-Oct1- and Sp1-Elf-1-paired occupancies of previously known target promoter regions were suppressed by elevated O-GlcNAc modification.
20699577	0	54	theme	DNA	78:80	arg1	binding					82:88	reduced Sp1 cooperative DNA binding	54:88	reduced Sp1 cooperative DNA binding with its collaborating factors	54:119	Elevated O-linked N-acetylglucosamine correlated with reduced Sp1 cooperative DNA binding with its collaborating factors in vivo.
31847126	11	0	theme	similar	2310:2316	arg1	IPAH					2305:2308	IPAH	2305:2308	IPAH similar to control levels	2305:2334	Blocking OGT activity in these experiments, however, altered the vascular sprouting and de novo vascularization in IPAH similar to control levels when compared to controls.
31847126	3	1	theme	proliferation	705:717	arg1	regulation					675:684	the regulation	671:684	the regulation of cell signaling, proliferation, and metabolism	671:733	OGT is a cellular nutrient sensor that is essential in maintaining proper cell function through the regulation of cell signaling, proliferation, and metabolism.
31847126	6	2	theme	endothelial	1274:1284	arg1	VEGF					1301:1304	VEGF	1301:1304	VEGF	1301:1304	We showed that knockdown of OGT resulted in reduced vascular endothelial growth factor (VEGF) expression in IPAH primary isolated vascular cells.
31847126	6	2	theme	endothelial	1274:1284	arg1	factor					1293:1298	vascular endothelial growth factor	1265:1298	reduced vascular endothelial growth factor (VEGF) expression in IPAH primary isolated vascular cells	1257:1356	We showed that knockdown of OGT resulted in reduced vascular endothelial growth factor (VEGF) expression in IPAH primary isolated vascular cells.
31847126	11	3	dep	sprouting	2264:2272	arg1	the					2251:2253	the	2251:2253	the	2251:2253	Blocking OGT activity in these experiments, however, altered the vascular sprouting and de novo vascularization in IPAH similar to control levels when compared to controls.
31847126	10	4	from	model	2069:2073	arg1	Assessment					1924:1933	Assessment	1924:1933	Assessment of vascular sprouting from an in vitro 3D spheroid co-culture model using IPAH and control PAEC/PASMCs and an in vivo vascularization model using control and PAEC-embedded collagen implants	1924:2123	Assessment of vascular sprouting from an in vitro 3D spheroid co-culture model using IPAH and control PAEC/PASMCs and an in vivo vascularization model using control and PAEC-embedded collagen implants demonstrated higher vascularization in IPAH compared to control.
31847126	10	4	from	model	2069:2073	arg1	sprouting					1947:1955	vascular sprouting	1938:1955	vascular sprouting from an in vitro 3D spheroid co-culture model using IPAH and control PAEC/PASMCs and an in vivo vascularization model using control and PAEC-embedded collagen implants	1938:2123	Assessment of vascular sprouting from an in vitro 3D spheroid co-culture model using IPAH and control PAEC/PASMCs and an in vivo vascularization model using control and PAEC-embedded collagen implants demonstrated higher vascularization in IPAH compared to control.
31847126	13	5	theme	plexiform	2673:2681	arg1	lesions					2683:2689	plexiform lesions	2673:2689	plexiform lesions	2673:2689	These findings provide greater insight into the potential role that altered glucose uptake and metabolism may have on the angiogenic process and the development of plexiform lesions.
31847126	5	6	theme	NODSCID	1199:1205	arg1	mice					1207:1210	NODSCID mice	1199:1210	NODSCID mice	1199:1210	Primary isolated human control and IPAH patient PASMCs and pulmonary arterial endothelial cells (PAECs) were grown in the presence or absence of OGT inhibitors and subjected to biochemical assessments in monolayer cultures and tube formation assays, in vitro vascular sprouting 3D spheroid co-culture models, and de novo vascularization models in NODSCID mice.
31847126	12	7	theme	VEGF	2464:2467	arg1	expression					2469:2478	VEGF expression	2464:2478	VEGF expression	2464:2478	Our findings in this report are the first to describe a role for the OGT/O-GlcNAc axis in modulating VEGF expression and vascularization in IPAH.
31847126	5	8	from	models	1153:1158	arg1	mice					1207:1210	NODSCID mice	1199:1210	NODSCID mice	1199:1210	Primary isolated human control and IPAH patient PASMCs and pulmonary arterial endothelial cells (PAECs) were grown in the presence or absence of OGT inhibitors and subjected to biochemical assessments in monolayer cultures and tube formation assays, in vitro vascular sprouting 3D spheroid co-culture models, and de novo vascularization models in NODSCID mice.
31847126	11	9	dep	de	2278:2279	arg1	novo					2281:2284	novo	2281:2284	novo	2281:2284	Blocking OGT activity in these experiments, however, altered the vascular sprouting and de novo vascularization in IPAH similar to control levels when compared to controls.
31847126	13	10	theme	angiogenic	2631:2640	arg1	process					2642:2648	the angiogenic process	2627:2648	the angiogenic process	2627:2648	These findings provide greater insight into the potential role that altered glucose uptake and metabolism may have on the angiogenic process and the development of plexiform lesions.
31847126	7	11	theme	expression	1428:1437	arg1	stimulator					1409:1418	a known stimulator	1401:1418	a known stimulator of VEGF expression	1401:1437	In addition, specificity protein 1 (SP1), a known stimulator of VEGF expression, was shown to have higher O-GlcNAc levels in IPAH compared to control at physiological (5 mM) and high (25 mM) glucose concentrations, and knockdown resulted in decreased VEGF protein levels.
31847126	7	11	theme	expression	1428:1437	arg1	protein					1384:1390	specificity protein 1	1372:1392	specificity protein 1 (SP1)	1372:1398	In addition, specificity protein 1 (SP1), a known stimulator of VEGF expression, was shown to have higher O-GlcNAc levels in IPAH compared to control at physiological (5 mM) and high (25 mM) glucose concentrations, and knockdown resulted in decreased VEGF protein levels.
31847126	5	12	from	models	1189:1194	arg1	mice					1207:1210	NODSCID mice	1199:1210	NODSCID mice	1199:1210	Primary isolated human control and IPAH patient PASMCs and pulmonary arterial endothelial cells (PAECs) were grown in the presence or absence of OGT inhibitors and subjected to biochemical assessments in monolayer cultures and tube formation assays, in vitro vascular sprouting 3D spheroid co-culture models, and de novo vascularization models in NODSCID mice.
31847126	8	13	theme	human	1644:1648	arg1	PAECs					1655:1659	human IPAH PAECs	1644:1659	human IPAH PAECs	1644:1659	Furthermore, human IPAH PAECs demonstrated a significantly higher degree of capillary tube-like structures and increased length compared to control PAECs.
31847126	7	14	contain	have	1453:1456	arg1	protein					1384:1390	specificity protein 1	1372:1392	specificity protein 1 (SP1)	1372:1398	In addition, specificity protein 1 (SP1), a known stimulator of VEGF expression, was shown to have higher O-GlcNAc levels in IPAH compared to control at physiological (5 mM) and high (25 mM) glucose concentrations, and knockdown resulted in decreased VEGF protein levels.
31847126	7	14	contain	have	1453:1456	arg1	SP1					1395:1397	SP1	1395:1397	SP1	1395:1397	In addition, specificity protein 1 (SP1), a known stimulator of VEGF expression, was shown to have higher O-GlcNAc levels in IPAH compared to control at physiological (5 mM) and high (25 mM) glucose concentrations, and knockdown resulted in decreased VEGF protein levels.
31847126	7	14	contain	have	1453:1456	arg2	levels					1474:1479	higher O-GlcNAc levels	1458:1479	higher O-GlcNAc levels in IPAH compared to control at physiological (5 mM) and high (25 mM) glucose concentrations	1458:1571	In addition, specificity protein 1 (SP1), a known stimulator of VEGF expression, was shown to have higher O-GlcNAc levels in IPAH compared to control at physiological (5 mM) and high (25 mM) glucose concentrations, and knockdown resulted in decreased VEGF protein levels.
31847126	7	14	contain	have	1453:1456	arg1	stimulator					1409:1418	a known stimulator	1401:1418	a known stimulator of VEGF expression	1401:1437	In addition, specificity protein 1 (SP1), a known stimulator of VEGF expression, was shown to have higher O-GlcNAc levels in IPAH compared to control at physiological (5 mM) and high (25 mM) glucose concentrations, and knockdown resulted in decreased VEGF protein levels.
31847126	12	15	theme	OGT/O-GlcNAc	2432:2443	arg1	axis					2445:2448	the OGT/O-GlcNAc axis	2428:2448	the OGT/O-GlcNAc axis	2428:2448	Our findings in this report are the first to describe a role for the OGT/O-GlcNAc axis in modulating VEGF expression and vascularization in IPAH.
31847126	3	16	theme	nutrient	593:600	arg1	essential					617:625	essential	617:625	essential	617:625	OGT is a cellular nutrient sensor that is essential in maintaining proper cell function through the regulation of cell signaling, proliferation, and metabolism.
31847126	3	16	theme	nutrient	593:600	arg1	sensor					602:607	a cellular nutrient sensor	582:607	a cellular nutrient sensor that is essential in maintaining proper cell function through the regulation of cell signaling, proliferation, and metabolism	582:733	OGT is a cellular nutrient sensor that is essential in maintaining proper cell function through the regulation of cell signaling, proliferation, and metabolism.
31847126	3	16	theme	nutrient	593:600	arg1	OGT					575:577	OGT	575:577	OGT	575:577	OGT is a cellular nutrient sensor that is essential in maintaining proper cell function through the regulation of cell signaling, proliferation, and metabolism.
31847126	9	17	theme	structures	1870:1879	arg1	number					1850:1855	the number	1846:1855	the number of tube-like structures	1846:1879	Addition of an OGT inhibitor, OSMI-1, significantly reduced the number of tube-like structures and tube length similar to control levels.
31847126	9	17	theme	structures	1870:1879	arg1	length					1890:1895	tube length	1885:1895	tube length similar to control levels	1885:1921	Addition of an OGT inhibitor, OSMI-1, significantly reduced the number of tube-like structures and tube length similar to control levels.
31847126	10	18	from	vascularization	2145:2159	arg1	IPAH					2164:2167	IPAH	2164:2167	IPAH	2164:2167	Assessment of vascular sprouting from an in vitro 3D spheroid co-culture model using IPAH and control PAEC/PASMCs and an in vivo vascularization model using control and PAEC-embedded collagen implants demonstrated higher vascularization in IPAH compared to control.
31847126	6	19	theme	IPAH	1321:1324	arg1	cells					1352:1356	IPAH primary isolated vascular cells	1321:1356	IPAH primary isolated vascular cells	1321:1356	We showed that knockdown of OGT resulted in reduced vascular endothelial growth factor (VEGF) expression in IPAH primary isolated vascular cells.
31847126	7	20	theme	glucose	1550:1556	arg1	concentrations					1558:1571	physiological (5 mM) and high (25 mM) glucose concentrations	1512:1571	physiological (5 mM) and high (25 mM) glucose concentrations	1512:1571	In addition, specificity protein 1 (SP1), a known stimulator of VEGF expression, was shown to have higher O-GlcNAc levels in IPAH compared to control at physiological (5 mM) and high (25 mM) glucose concentrations, and knockdown resulted in decreased VEGF protein levels.
31847126	10	21	dep	in	1965:1966	arg1	vitro					1968:1972	vitro	1968:1972	vitro	1968:1972	Assessment of vascular sprouting from an in vitro 3D spheroid co-culture model using IPAH and control PAEC/PASMCs and an in vivo vascularization model using control and PAEC-embedded collagen implants demonstrated higher vascularization in IPAH compared to control.
31847126	9	22	theme	tube	1885:1888	arg1	length					1890:1895	tube length	1885:1895	tube length similar to control levels	1885:1921	Addition of an OGT inhibitor, OSMI-1, significantly reduced the number of tube-like structures and tube length similar to control levels.
31847126	5	23	theme	tube	1079:1082	arg1	assays					1094:1099	tube formation assays	1079:1099	tube formation assays	1079:1099	Primary isolated human control and IPAH patient PASMCs and pulmonary arterial endothelial cells (PAECs) were grown in the presence or absence of OGT inhibitors and subjected to biochemical assessments in monolayer cultures and tube formation assays, in vitro vascular sprouting 3D spheroid co-culture models, and de novo vascularization models in NODSCID mice.
31847126	4	24	from	dysfunction	831:841	arg1	IPAH					846:849	IPAH	846:849	IPAH	846:849	The aim of this study was to determine the role of OGT and O-GlcNAc in vascular and angiogenic dysfunction in IPAH.
31847126	5	25	theme	Primary	852:858	arg1	control					875:881	Primary isolated human control and IPAH patient PASMCs	852:905	control	875:881	Primary isolated human control and IPAH patient PASMCs and pulmonary arterial endothelial cells (PAECs) were grown in the presence or absence of OGT inhibitors and subjected to biochemical assessments in monolayer cultures and tube formation assays, in vitro vascular sprouting 3D spheroid co-culture models, and de novo vascularization models in NODSCID mice.
31847126	9	26	theme	similar	1897:1903	arg1	length					1890:1895	tube length	1885:1895	tube length similar to control levels	1885:1921	Addition of an OGT inhibitor, OSMI-1, significantly reduced the number of tube-like structures and tube length similar to control levels.
31847126	5	27	theme	biochemical	1029:1039	arg1	assessments					1041:1051	biochemical assessments	1029:1051	biochemical assessments in monolayer cultures and tube formation assays, in vitro vascular sprouting 3D spheroid co-culture models, and de novo vascularization models in NODSCID mice	1029:1210	Primary isolated human control and IPAH patient PASMCs and pulmonary arterial endothelial cells (PAECs) were grown in the presence or absence of OGT inhibitors and subjected to biochemical assessments in monolayer cultures and tube formation assays, in vitro vascular sprouting 3D spheroid co-culture models, and de novo vascularization models in NODSCID mice.
31847126	5	28	theme	arterial	921:928	arg1	PAECs					949:953	PAECs	949:953	PAECs	949:953	Primary isolated human control and IPAH patient PASMCs and pulmonary arterial endothelial cells (PAECs) were grown in the presence or absence of OGT inhibitors and subjected to biochemical assessments in monolayer cultures and tube formation assays, in vitro vascular sprouting 3D spheroid co-culture models, and de novo vascularization models in NODSCID mice.
31847126	5	28	theme	arterial	921:928	arg1	cells					942:946	pulmonary arterial endothelial cells	911:946	pulmonary arterial endothelial cells (PAECs)	911:954	Primary isolated human control and IPAH patient PASMCs and pulmonary arterial endothelial cells (PAECs) were grown in the presence or absence of OGT inhibitors and subjected to biochemical assessments in monolayer cultures and tube formation assays, in vitro vascular sprouting 3D spheroid co-culture models, and de novo vascularization models in NODSCID mice.
31847126	14	29	theme	OGT/O-GlcNAc	2723:2734	arg1	target					2772:2777	a potential therapeutic target	2748:2777	a potential therapeutic target for treating the angiogenic dysregulation that is present in IPAH	2748:2843	Therefore, we believe that the OGT/O-GlcNAc axis may be a potential therapeutic target for treating the angiogenic dysregulation that is present in IPAH.
31847126	14	29	theme	OGT/O-GlcNAc	2723:2734	arg1	axis					2736:2739	the OGT/O-GlcNAc axis	2719:2739	the OGT/O-GlcNAc axis	2719:2739	Therefore, we believe that the OGT/O-GlcNAc axis may be a potential therapeutic target for treating the angiogenic dysregulation that is present in IPAH.
31847126	9	30	theme	control	1908:1914	arg1	levels					1916:1921	control levels	1908:1921	control levels	1908:1921	Addition of an OGT inhibitor, OSMI-1, significantly reduced the number of tube-like structures and tube length similar to control levels.
31847126	6	31	theme	factor	1293:1298	arg1	expression					1307:1316	reduced vascular endothelial growth factor (VEGF) expression	1257:1316	reduced vascular endothelial growth factor (VEGF) expression in IPAH primary isolated vascular cells	1257:1356	We showed that knockdown of OGT resulted in reduced vascular endothelial growth factor (VEGF) expression in IPAH primary isolated vascular cells.
31847126	7	32	dep	physiological	1512:1524	arg1	mM					1529:1530	5 mM	1527:1530	5 mM	1527:1530	In addition, specificity protein 1 (SP1), a known stimulator of VEGF expression, was shown to have higher O-GlcNAc levels in IPAH compared to control at physiological (5 mM) and high (25 mM) glucose concentrations, and knockdown resulted in decreased VEGF protein levels.
31847126	3	33	theme	cell	649:652	arg1	function					654:661	proper cell function	642:661	proper cell function	642:661	OGT is a cellular nutrient sensor that is essential in maintaining proper cell function through the regulation of cell signaling, proliferation, and metabolism.
31847126	8	34	theme	tube-like	1717:1725	arg1	structures					1727:1736	capillary tube-like structures	1707:1736	capillary tube-like structures	1707:1736	Furthermore, human IPAH PAECs demonstrated a significantly higher degree of capillary tube-like structures and increased length compared to control PAECs.
31847126	2	35	theme	cell	539:542	arg1	proliferation					552:564	pulmonary arterial smooth muscle cell (PASMC) proliferation	506:564	pulmonary arterial smooth muscle cell (PASMC) proliferation	506:564	The serine/threonine hydroxyl-linked N-Acetylglucosamine (O-GlcNAc) transferase (OGT) has been shown to drive pulmonary arterial smooth muscle cell (PASMC) proliferation in IPAH.
31847126	10	36	theme	sprouting	1947:1955	arg1	Assessment					1924:1933	Assessment	1924:1933	Assessment of vascular sprouting from an in vitro 3D spheroid co-culture model using IPAH and control PAEC/PASMCs and an in vivo vascularization model using control and PAEC-embedded collagen implants	1924:2123	Assessment of vascular sprouting from an in vitro 3D spheroid co-culture model using IPAH and control PAEC/PASMCs and an in vivo vascularization model using control and PAEC-embedded collagen implants demonstrated higher vascularization in IPAH compared to control.
31847126	5	37	theme	vascular	1111:1118	arg1	models					1153:1158	in vitro vascular sprouting 3D spheroid co-culture models	1102:1158	in vitro vascular sprouting 3D spheroid co-culture models	1102:1158	Primary isolated human control and IPAH patient PASMCs and pulmonary arterial endothelial cells (PAECs) were grown in the presence or absence of OGT inhibitors and subjected to biochemical assessments in monolayer cultures and tube formation assays, in vitro vascular sprouting 3D spheroid co-culture models, and de novo vascularization models in NODSCID mice.
31847126	14	38	from	present	2829:2835	arg1	IPAH					2840:2843	IPAH	2840:2843	IPAH	2840:2843	Therefore, we believe that the OGT/O-GlcNAc axis may be a potential therapeutic target for treating the angiogenic dysregulation that is present in IPAH.
31847126	5	39	theme	patient	892:898	arg1	PASMCs					900:905	Primary isolated human control and IPAH patient PASMCs	852:905	PASMCs	900:905	Primary isolated human control and IPAH patient PASMCs and pulmonary arterial endothelial cells (PAECs) were grown in the presence or absence of OGT inhibitors and subjected to biochemical assessments in monolayer cultures and tube formation assays, in vitro vascular sprouting 3D spheroid co-culture models, and de novo vascularization models in NODSCID mice.
31847126	2	40	theme	smooth	525:530	arg1	proliferation					552:564	pulmonary arterial smooth muscle cell (PASMC) proliferation	506:564	pulmonary arterial smooth muscle cell (PASMC) proliferation	506:564	The serine/threonine hydroxyl-linked N-Acetylglucosamine (O-GlcNAc) transferase (OGT) has been shown to drive pulmonary arterial smooth muscle cell (PASMC) proliferation in IPAH.
31847126	1	41	theme	PAH	320:322	arg1	vasoconstriction					233:248	vasoconstriction	233:248	vasoconstriction	233:248	Idiopathic pulmonary arterial hypertension (IPAH) is considered a vasculopathy characterized by elevated pulmonary vascular resistance due to vasoconstriction and/or lung remodeling such as plexiform lesions, the hallmark of the PAH, as well as cell proliferation and vascular and angiogenic dysfunction.
31847126	1	41	theme	PAH	320:322	arg1	hallmark					304:311	the hallmark	300:311	the hallmark of the PAH	300:322	Idiopathic pulmonary arterial hypertension (IPAH) is considered a vasculopathy characterized by elevated pulmonary vascular resistance due to vasoconstriction and/or lung remodeling such as plexiform lesions, the hallmark of the PAH, as well as cell proliferation and vascular and angiogenic dysfunction.
31847126	10	42	theme	higher	2138:2143	arg1	vascularization					2145:2159	higher vascularization	2138:2159	higher vascularization in IPAH	2138:2167	Assessment of vascular sprouting from an in vitro 3D spheroid co-culture model using IPAH and control PAEC/PASMCs and an in vivo vascularization model using control and PAEC-embedded collagen implants demonstrated higher vascularization in IPAH compared to control.
31847126	10	43	theme	spheroid	1977:1984	arg1	model					1997:2001	an in vitro 3D spheroid co-culture model	1962:2001	an in vitro 3D spheroid co-culture model using IPAH and control PAEC/PASMCs	1962:2036	Assessment of vascular sprouting from an in vitro 3D spheroid co-culture model using IPAH and control PAEC/PASMCs and an in vivo vascularization model using control and PAEC-embedded collagen implants demonstrated higher vascularization in IPAH compared to control.
31847126	5	44	from	assessments	1041:1051	arg1	assays					1094:1099	tube formation assays	1079:1099	tube formation assays	1079:1099	Primary isolated human control and IPAH patient PASMCs and pulmonary arterial endothelial cells (PAECs) were grown in the presence or absence of OGT inhibitors and subjected to biochemical assessments in monolayer cultures and tube formation assays, in vitro vascular sprouting 3D spheroid co-culture models, and de novo vascularization models in NODSCID mice.
31847126	5	44	from	assessments	1041:1051	arg1	models					1153:1158	in vitro vascular sprouting 3D spheroid co-culture models	1102:1158	in vitro vascular sprouting 3D spheroid co-culture models	1102:1158	Primary isolated human control and IPAH patient PASMCs and pulmonary arterial endothelial cells (PAECs) were grown in the presence or absence of OGT inhibitors and subjected to biochemical assessments in monolayer cultures and tube formation assays, in vitro vascular sprouting 3D spheroid co-culture models, and de novo vascularization models in NODSCID mice.
31847126	5	44	from	assessments	1041:1051	arg1	cultures					1066:1073	monolayer cultures	1056:1073	monolayer cultures	1056:1073	Primary isolated human control and IPAH patient PASMCs and pulmonary arterial endothelial cells (PAECs) were grown in the presence or absence of OGT inhibitors and subjected to biochemical assessments in monolayer cultures and tube formation assays, in vitro vascular sprouting 3D spheroid co-culture models, and de novo vascularization models in NODSCID mice.
31847126	5	44	from	assessments	1041:1051	arg1	models					1189:1194	de novo vascularization models	1165:1194	de novo vascularization models in NODSCID mice	1165:1210	Primary isolated human control and IPAH patient PASMCs and pulmonary arterial endothelial cells (PAECs) were grown in the presence or absence of OGT inhibitors and subjected to biochemical assessments in monolayer cultures and tube formation assays, in vitro vascular sprouting 3D spheroid co-culture models, and de novo vascularization models in NODSCID mice.
31847126	1	45	theme	vascular	359:366	arg1	dysfunction					383:393	vascular and angiogenic dysfunction	359:393	vascular and angiogenic dysfunction	359:393	Idiopathic pulmonary arterial hypertension (IPAH) is considered a vasculopathy characterized by elevated pulmonary vascular resistance due to vasoconstriction and/or lung remodeling such as plexiform lesions, the hallmark of the PAH, as well as cell proliferation and vascular and angiogenic dysfunction.
31847126	1	46	theme	elevated	187:194	arg1	resistance					215:224	elevated pulmonary vascular resistance	187:224	elevated pulmonary vascular resistance due to vasoconstriction and/or lung remodeling such as plexiform lesions, the hallmark of the PAH, as well as cell proliferation and vascular and angiogenic dysfunction	187:393	Idiopathic pulmonary arterial hypertension (IPAH) is considered a vasculopathy characterized by elevated pulmonary vascular resistance due to vasoconstriction and/or lung remodeling such as plexiform lesions, the hallmark of the PAH, as well as cell proliferation and vascular and angiogenic dysfunction.
31847126	10	47	from	model	1997:2001	arg1	Assessment					1924:1933	Assessment	1924:1933	Assessment of vascular sprouting from an in vitro 3D spheroid co-culture model using IPAH and control PAEC/PASMCs and an in vivo vascularization model using control and PAEC-embedded collagen implants	1924:2123	Assessment of vascular sprouting from an in vitro 3D spheroid co-culture model using IPAH and control PAEC/PASMCs and an in vivo vascularization model using control and PAEC-embedded collagen implants demonstrated higher vascularization in IPAH compared to control.
31847126	10	47	from	model	1997:2001	arg1	sprouting					1947:1955	vascular sprouting	1938:1955	vascular sprouting from an in vitro 3D spheroid co-culture model using IPAH and control PAEC/PASMCs and an in vivo vascularization model using control and PAEC-embedded collagen implants	1938:2123	Assessment of vascular sprouting from an in vitro 3D spheroid co-culture model using IPAH and control PAEC/PASMCs and an in vivo vascularization model using control and PAEC-embedded collagen implants demonstrated higher vascularization in IPAH compared to control.
31847126	1	48	theme	angiogenic	372:381	arg1	dysfunction					383:393	vascular and angiogenic dysfunction	359:393	vascular and angiogenic dysfunction	359:393	Idiopathic pulmonary arterial hypertension (IPAH) is considered a vasculopathy characterized by elevated pulmonary vascular resistance due to vasoconstriction and/or lung remodeling such as plexiform lesions, the hallmark of the PAH, as well as cell proliferation and vascular and angiogenic dysfunction.
31847126	14	49	theme	angiogenic	2796:2805	arg1	present					2829:2835	present	2829:2835	present	2829:2835	Therefore, we believe that the OGT/O-GlcNAc axis may be a potential therapeutic target for treating the angiogenic dysregulation that is present in IPAH.
31847126	14	49	theme	angiogenic	2796:2805	arg1	dysregulation					2807:2819	the angiogenic dysregulation	2792:2819	the angiogenic dysregulation that is present in IPAH	2792:2843	Therefore, we believe that the OGT/O-GlcNAc axis may be a potential therapeutic target for treating the angiogenic dysregulation that is present in IPAH.
31847126	7	50	theme	protein	1615:1621	arg1	levels					1623:1628	decreased VEGF protein levels	1600:1628	decreased VEGF protein levels	1600:1628	In addition, specificity protein 1 (SP1), a known stimulator of VEGF expression, was shown to have higher O-GlcNAc levels in IPAH compared to control at physiological (5 mM) and high (25 mM) glucose concentrations, and knockdown resulted in decreased VEGF protein levels.
31847126	2	51	theme	PASMC	545:549	arg1	proliferation					552:564	pulmonary arterial smooth muscle cell (PASMC) proliferation	506:564	pulmonary arterial smooth muscle cell (PASMC) proliferation	506:564	The serine/threonine hydroxyl-linked N-Acetylglucosamine (O-GlcNAc) transferase (OGT) has been shown to drive pulmonary arterial smooth muscle cell (PASMC) proliferation in IPAH.
31847126	11	52	theme	control	2321:2327	arg1	levels					2329:2334	control levels	2321:2334	control levels	2321:2334	Blocking OGT activity in these experiments, however, altered the vascular sprouting and de novo vascularization in IPAH similar to control levels when compared to controls.
31847126	6	53	theme	isolated	1334:1341	arg1	cells					1352:1356	IPAH primary isolated vascular cells	1321:1356	IPAH primary isolated vascular cells	1321:1356	We showed that knockdown of OGT resulted in reduced vascular endothelial growth factor (VEGF) expression in IPAH primary isolated vascular cells.
31847126	5	54	theme	in	1102:1103	arg1	models					1153:1158	in vitro vascular sprouting 3D spheroid co-culture models	1102:1158	in vitro vascular sprouting 3D spheroid co-culture models	1102:1158	Primary isolated human control and IPAH patient PASMCs and pulmonary arterial endothelial cells (PAECs) were grown in the presence or absence of OGT inhibitors and subjected to biochemical assessments in monolayer cultures and tube formation assays, in vitro vascular sprouting 3D spheroid co-culture models, and de novo vascularization models in NODSCID mice.
31847126	1	55	theme	pulmonary	102:110	arg1	hypertension					121:132	Idiopathic pulmonary arterial hypertension	91:132	Idiopathic pulmonary arterial hypertension (IPAH)	91:139	Idiopathic pulmonary arterial hypertension (IPAH) is considered a vasculopathy characterized by elevated pulmonary vascular resistance due to vasoconstriction and/or lung remodeling such as plexiform lesions, the hallmark of the PAH, as well as cell proliferation and vascular and angiogenic dysfunction.
31847126	1	55	theme	pulmonary	102:110	arg1	IPAH					135:138	IPAH	135:138	IPAH	135:138	Idiopathic pulmonary arterial hypertension (IPAH) is considered a vasculopathy characterized by elevated pulmonary vascular resistance due to vasoconstriction and/or lung remodeling such as plexiform lesions, the hallmark of the PAH, as well as cell proliferation and vascular and angiogenic dysfunction.
31847126	7	56	theme	decreased	1600:1608	arg1	levels					1623:1628	decreased VEGF protein levels	1600:1628	decreased VEGF protein levels	1600:1628	In addition, specificity protein 1 (SP1), a known stimulator of VEGF expression, was shown to have higher O-GlcNAc levels in IPAH compared to control at physiological (5 mM) and high (25 mM) glucose concentrations, and knockdown resulted in decreased VEGF protein levels.
31847126	4	57	theme	study	752:756	arg1	aim					740:742	The aim	736:742	The aim of this study	736:756	The aim of this study was to determine the role of OGT and O-GlcNAc in vascular and angiogenic dysfunction in IPAH.
31847126	2	58	theme	hydroxyl-linked	417:431	arg1	N-Acetylglucosamine					433:451	The serine/threonine hydroxyl-linked N-Acetylglucosamine	396:451	The serine/threonine hydroxyl-linked N-Acetylglucosamine (O-GlcNAc) transferase (OGT)	396:480	The serine/threonine hydroxyl-linked N-Acetylglucosamine (O-GlcNAc) transferase (OGT) has been shown to drive pulmonary arterial smooth muscle cell (PASMC) proliferation in IPAH.
31847126	2	58	theme	hydroxyl-linked	417:431	arg1	O-GlcNAc					454:461	O-GlcNAc	454:461	O-GlcNAc	454:461	The serine/threonine hydroxyl-linked N-Acetylglucosamine (O-GlcNAc) transferase (OGT) has been shown to drive pulmonary arterial smooth muscle cell (PASMC) proliferation in IPAH.
31847126	0	59	theme	O-GlcNAc	0:7	arg1	Transferase					9:19	O-GlcNAc Transferase	0:19	O-GlcNAc Transferase	0:19	O-GlcNAc Transferase Regulates Angiogenesis in Idiopathic Pulmonary Arterial Hypertension.
31847126	5	60	theme	de	1165:1166	arg1	models					1189:1194	de novo vascularization models	1165:1194	de novo vascularization models in NODSCID mice	1165:1210	Primary isolated human control and IPAH patient PASMCs and pulmonary arterial endothelial cells (PAECs) were grown in the presence or absence of OGT inhibitors and subjected to biochemical assessments in monolayer cultures and tube formation assays, in vitro vascular sprouting 3D spheroid co-culture models, and de novo vascularization models in NODSCID mice.
31847126	10	61	from	Assessment	1924:1933	arg1	model					1997:2001	an in vitro 3D spheroid co-culture model	1962:2001	an in vitro 3D spheroid co-culture model using IPAH and control PAEC/PASMCs	1962:2036	Assessment of vascular sprouting from an in vitro 3D spheroid co-culture model using IPAH and control PAEC/PASMCs and an in vivo vascularization model using control and PAEC-embedded collagen implants demonstrated higher vascularization in IPAH compared to control.
31847126	10	61	from	Assessment	1924:1933	arg1	model					2069:2073	an in vivo vascularization model	2042:2073	an in vivo vascularization model using control and PAEC-embedded collagen implants	2042:2123	Assessment of vascular sprouting from an in vitro 3D spheroid co-culture model using IPAH and control PAEC/PASMCs and an in vivo vascularization model using control and PAEC-embedded collagen implants demonstrated higher vascularization in IPAH compared to control.
31847126	5	62	theme	vascularization	1173:1187	arg1	models					1189:1194	de novo vascularization models	1165:1194	de novo vascularization models in NODSCID mice	1165:1210	Primary isolated human control and IPAH patient PASMCs and pulmonary arterial endothelial cells (PAECs) were grown in the presence or absence of OGT inhibitors and subjected to biochemical assessments in monolayer cultures and tube formation assays, in vitro vascular sprouting 3D spheroid co-culture models, and de novo vascularization models in NODSCID mice.
31847126	2	63	theme	pulmonary	506:514	arg1	proliferation					552:564	pulmonary arterial smooth muscle cell (PASMC) proliferation	506:564	pulmonary arterial smooth muscle cell (PASMC) proliferation	506:564	The serine/threonine hydroxyl-linked N-Acetylglucosamine (O-GlcNAc) transferase (OGT) has been shown to drive pulmonary arterial smooth muscle cell (PASMC) proliferation in IPAH.
31847126	10	64	theme	co-culture	1986:1995	arg1	model					1997:2001	an in vitro 3D spheroid co-culture model	1962:2001	an in vitro 3D spheroid co-culture model using IPAH and control PAEC/PASMCs	1962:2036	Assessment of vascular sprouting from an in vitro 3D spheroid co-culture model using IPAH and control PAEC/PASMCs and an in vivo vascularization model using control and PAEC-embedded collagen implants demonstrated higher vascularization in IPAH compared to control.
31847126	5	65	theme	isolated	860:867	arg1	control					875:881	Primary isolated human control and IPAH patient PASMCs	852:905	control	875:881	Primary isolated human control and IPAH patient PASMCs and pulmonary arterial endothelial cells (PAECs) were grown in the presence or absence of OGT inhibitors and subjected to biochemical assessments in monolayer cultures and tube formation assays, in vitro vascular sprouting 3D spheroid co-culture models, and de novo vascularization models in NODSCID mice.
31847126	5	66	theme	co-culture	1142:1151	arg1	models					1153:1158	in vitro vascular sprouting 3D spheroid co-culture models	1102:1158	in vitro vascular sprouting 3D spheroid co-culture models	1102:1158	Primary isolated human control and IPAH patient PASMCs and pulmonary arterial endothelial cells (PAECs) were grown in the presence or absence of OGT inhibitors and subjected to biochemical assessments in monolayer cultures and tube formation assays, in vitro vascular sprouting 3D spheroid co-culture models, and de novo vascularization models in NODSCID mice.
31847126	14	67	located	present	2829:2835	arg2	dysregulation					2807:2819	the angiogenic dysregulation	2792:2819	the angiogenic dysregulation that is present in IPAH	2792:2843	Therefore, we believe that the OGT/O-GlcNAc axis may be a potential therapeutic target for treating the angiogenic dysregulation that is present in IPAH.
31847126	14	67	located	present	2829:2835	arg1	IPAH					2840:2843	IPAH	2840:2843	IPAH	2840:2843	Therefore, we believe that the OGT/O-GlcNAc axis may be a potential therapeutic target for treating the angiogenic dysregulation that is present in IPAH.
31847126	14	67	located	present	2829:2835	arg2	present					2829:2835	present	2829:2835	present	2829:2835	Therefore, we believe that the OGT/O-GlcNAc axis may be a potential therapeutic target for treating the angiogenic dysregulation that is present in IPAH.
31847126	0	68	theme	Pulmonary	58:66	arg1	Hypertension					77:88	Idiopathic Pulmonary Arterial Hypertension	47:88	Idiopathic Pulmonary Arterial Hypertension	47:88	O-GlcNAc Transferase Regulates Angiogenesis in Idiopathic Pulmonary Arterial Hypertension.
31847126	7	69	theme	O-GlcNAc	1465:1472	arg1	levels					1474:1479	higher O-GlcNAc levels	1458:1479	higher O-GlcNAc levels in IPAH compared to control at physiological (5 mM) and high (25 mM) glucose concentrations	1458:1571	In addition, specificity protein 1 (SP1), a known stimulator of VEGF expression, was shown to have higher O-GlcNAc levels in IPAH compared to control at physiological (5 mM) and high (25 mM) glucose concentrations, and knockdown resulted in decreased VEGF protein levels.
31847126	10	70	theme	IPAH	2009:2012	arg1	PAEC/PASMCs					2026:2036	IPAH and control PAEC/PASMCs	2009:2036	IPAH and control PAEC/PASMCs	2009:2036	Assessment of vascular sprouting from an in vitro 3D spheroid co-culture model using IPAH and control PAEC/PASMCs and an in vivo vascularization model using control and PAEC-embedded collagen implants demonstrated higher vascularization in IPAH compared to control.
31847126	10	71	dep	in	2045:2046	arg1	vivo					2048:2051	vivo	2048:2051	vivo	2048:2051	Assessment of vascular sprouting from an in vitro 3D spheroid co-culture model using IPAH and control PAEC/PASMCs and an in vivo vascularization model using control and PAEC-embedded collagen implants demonstrated higher vascularization in IPAH compared to control.
31847126	9	72	theme	OGT	1801:1803	arg1	OSMI-1					1816:1821	OSMI-1	1816:1821	OSMI-1	1816:1821	Addition of an OGT inhibitor, OSMI-1, significantly reduced the number of tube-like structures and tube length similar to control levels.
31847126	9	72	theme	OGT	1801:1803	arg1	inhibitor					1805:1813	an OGT inhibitor	1798:1813	an OGT inhibitor	1798:1813	Addition of an OGT inhibitor, OSMI-1, significantly reduced the number of tube-like structures and tube length similar to control levels.
31847126	3	73	theme	cell	689:692	arg1	signaling					694:702	cell signaling	689:702	cell signaling	689:702	OGT is a cellular nutrient sensor that is essential in maintaining proper cell function through the regulation of cell signaling, proliferation, and metabolism.
31847126	11	74	dep	altered	2243:2249	arg1	Blocking					2190:2197	Blocking	2190:2197	Blocking OGT activity in these experiments	2190:2231	Blocking OGT activity in these experiments, however, altered the vascular sprouting and de novo vascularization in IPAH similar to control levels when compared to controls.
31847126	1	75	theme	vascular	206:213	arg1	resistance					215:224	elevated pulmonary vascular resistance	187:224	elevated pulmonary vascular resistance due to vasoconstriction and/or lung remodeling such as plexiform lesions, the hallmark of the PAH, as well as cell proliferation and vascular and angiogenic dysfunction	187:393	Idiopathic pulmonary arterial hypertension (IPAH) is considered a vasculopathy characterized by elevated pulmonary vascular resistance due to vasoconstriction and/or lung remodeling such as plexiform lesions, the hallmark of the PAH, as well as cell proliferation and vascular and angiogenic dysfunction.
31847126	5	76	theme	OGT	997:999	arg1	inhibitors					1001:1010	OGT inhibitors	997:1010	OGT inhibitors	997:1010	Primary isolated human control and IPAH patient PASMCs and pulmonary arterial endothelial cells (PAECs) were grown in the presence or absence of OGT inhibitors and subjected to biochemical assessments in monolayer cultures and tube formation assays, in vitro vascular sprouting 3D spheroid co-culture models, and de novo vascularization models in NODSCID mice.
31847126	3	77	theme	metabolism	724:733	arg1	regulation					675:684	the regulation	671:684	the regulation of cell signaling, proliferation, and metabolism	671:733	OGT is a cellular nutrient sensor that is essential in maintaining proper cell function through the regulation of cell signaling, proliferation, and metabolism.
31847126	6	78	theme	growth	1286:1291	arg1	VEGF					1301:1304	VEGF	1301:1304	VEGF	1301:1304	We showed that knockdown of OGT resulted in reduced vascular endothelial growth factor (VEGF) expression in IPAH primary isolated vascular cells.
31847126	6	78	theme	growth	1286:1291	arg1	factor					1293:1298	vascular endothelial growth factor	1265:1298	reduced vascular endothelial growth factor (VEGF) expression in IPAH primary isolated vascular cells	1257:1356	We showed that knockdown of OGT resulted in reduced vascular endothelial growth factor (VEGF) expression in IPAH primary isolated vascular cells.
31847126	7	79	from	levels	1474:1479	arg1	IPAH					1484:1487	IPAH	1484:1487	IPAH compared to control at physiological (5 mM) and high (25 mM) glucose concentrations	1484:1571	In addition, specificity protein 1 (SP1), a known stimulator of VEGF expression, was shown to have higher O-GlcNAc levels in IPAH compared to control at physiological (5 mM) and high (25 mM) glucose concentrations, and knockdown resulted in decreased VEGF protein levels.
31847126	10	80	theme	control	2018:2024	arg1	PAEC/PASMCs					2026:2036	IPAH and control PAEC/PASMCs	2009:2036	IPAH and control PAEC/PASMCs	2009:2036	Assessment of vascular sprouting from an in vitro 3D spheroid co-culture model using IPAH and control PAEC/PASMCs and an in vivo vascularization model using control and PAEC-embedded collagen implants demonstrated higher vascularization in IPAH compared to control.
31847126	6	81	theme	vascular	1265:1272	arg1	VEGF					1301:1304	VEGF	1301:1304	VEGF	1301:1304	We showed that knockdown of OGT resulted in reduced vascular endothelial growth factor (VEGF) expression in IPAH primary isolated vascular cells.
31847126	6	81	theme	vascular	1265:1272	arg1	factor					1293:1298	vascular endothelial growth factor	1265:1298	reduced vascular endothelial growth factor (VEGF) expression in IPAH primary isolated vascular cells	1257:1356	We showed that knockdown of OGT resulted in reduced vascular endothelial growth factor (VEGF) expression in IPAH primary isolated vascular cells.
31847126	11	82	from	vascularization	2286:2300	arg1	IPAH					2305:2308	IPAH	2305:2308	IPAH similar to control levels	2305:2334	Blocking OGT activity in these experiments, however, altered the vascular sprouting and de novo vascularization in IPAH similar to control levels when compared to controls.
31847126	13	83	theme	lesions	2683:2689	arg1	process					2642:2648	the angiogenic process	2627:2648	the angiogenic process	2627:2648	These findings provide greater insight into the potential role that altered glucose uptake and metabolism may have on the angiogenic process and the development of plexiform lesions.
31847126	13	83	theme	lesions	2683:2689	arg1	development					2658:2668	the development	2654:2668	the development of plexiform lesions	2654:2689	These findings provide greater insight into the potential role that altered glucose uptake and metabolism may have on the angiogenic process and the development of plexiform lesions.
31847126	11	84	from	sprouting	2264:2272	arg1	IPAH					2305:2308	IPAH	2305:2308	IPAH similar to control levels	2305:2334	Blocking OGT activity in these experiments, however, altered the vascular sprouting and de novo vascularization in IPAH similar to control levels when compared to controls.
31847126	7	85	theme	VEGF	1423:1426	arg1	expression					1428:1437	VEGF expression	1423:1437	VEGF expression	1423:1437	In addition, specificity protein 1 (SP1), a known stimulator of VEGF expression, was shown to have higher O-GlcNAc levels in IPAH compared to control at physiological (5 mM) and high (25 mM) glucose concentrations, and knockdown resulted in decreased VEGF protein levels.
31847126	6	86	theme	reduced	1257:1263	arg1	expression					1307:1316	reduced vascular endothelial growth factor (VEGF) expression	1257:1316	reduced vascular endothelial growth factor (VEGF) expression in IPAH primary isolated vascular cells	1257:1356	We showed that knockdown of OGT resulted in reduced vascular endothelial growth factor (VEGF) expression in IPAH primary isolated vascular cells.
31847126	7	87	theme	known	1403:1407	arg1	stimulator					1409:1418	a known stimulator	1401:1418	a known stimulator of VEGF expression	1401:1437	In addition, specificity protein 1 (SP1), a known stimulator of VEGF expression, was shown to have higher O-GlcNAc levels in IPAH compared to control at physiological (5 mM) and high (25 mM) glucose concentrations, and knockdown resulted in decreased VEGF protein levels.
31847126	7	87	theme	known	1403:1407	arg1	protein					1384:1390	specificity protein 1	1372:1392	specificity protein 1 (SP1)	1372:1398	In addition, specificity protein 1 (SP1), a known stimulator of VEGF expression, was shown to have higher O-GlcNAc levels in IPAH compared to control at physiological (5 mM) and high (25 mM) glucose concentrations, and knockdown resulted in decreased VEGF protein levels.
31847126	10	88	theme	vascularization	2053:2067	arg1	model					2069:2073	an in vivo vascularization model	2042:2073	an in vivo vascularization model using control and PAEC-embedded collagen implants	2042:2123	Assessment of vascular sprouting from an in vitro 3D spheroid co-culture model using IPAH and control PAEC/PASMCs and an in vivo vascularization model using control and PAEC-embedded collagen implants demonstrated higher vascularization in IPAH compared to control.
31847126	1	89	theme	pulmonary	196:204	arg1	resistance					215:224	elevated pulmonary vascular resistance	187:224	elevated pulmonary vascular resistance due to vasoconstriction and/or lung remodeling such as plexiform lesions, the hallmark of the PAH, as well as cell proliferation and vascular and angiogenic dysfunction	187:393	Idiopathic pulmonary arterial hypertension (IPAH) is considered a vasculopathy characterized by elevated pulmonary vascular resistance due to vasoconstriction and/or lung remodeling such as plexiform lesions, the hallmark of the PAH, as well as cell proliferation and vascular and angiogenic dysfunction.
31847126	10	90	theme	in	2045:2046	arg1	model					2069:2073	an in vivo vascularization model	2042:2073	an in vivo vascularization model using control and PAEC-embedded collagen implants	2042:2123	Assessment of vascular sprouting from an in vitro 3D spheroid co-culture model using IPAH and control PAEC/PASMCs and an in vivo vascularization model using control and PAEC-embedded collagen implants demonstrated higher vascularization in IPAH compared to control.
31847126	6	91	theme	OGT	1241:1243	arg1	knockdown					1228:1236	knockdown	1228:1236	knockdown of OGT	1228:1243	We showed that knockdown of OGT resulted in reduced vascular endothelial growth factor (VEGF) expression in IPAH primary isolated vascular cells.
31847126	3	92	theme	cellular	584:591	arg1	essential					617:625	essential	617:625	essential	617:625	OGT is a cellular nutrient sensor that is essential in maintaining proper cell function through the regulation of cell signaling, proliferation, and metabolism.
31847126	3	92	theme	cellular	584:591	arg1	sensor					602:607	a cellular nutrient sensor	582:607	a cellular nutrient sensor that is essential in maintaining proper cell function through the regulation of cell signaling, proliferation, and metabolism	582:733	OGT is a cellular nutrient sensor that is essential in maintaining proper cell function through the regulation of cell signaling, proliferation, and metabolism.
31847126	3	92	theme	cellular	584:591	arg1	OGT					575:577	OGT	575:577	OGT	575:577	OGT is a cellular nutrient sensor that is essential in maintaining proper cell function through the regulation of cell signaling, proliferation, and metabolism.
31847126	5	93	theme	3D	1130:1131	arg1	models					1153:1158	in vitro vascular sprouting 3D spheroid co-culture models	1102:1158	in vitro vascular sprouting 3D spheroid co-culture models	1102:1158	Primary isolated human control and IPAH patient PASMCs and pulmonary arterial endothelial cells (PAECs) were grown in the presence or absence of OGT inhibitors and subjected to biochemical assessments in monolayer cultures and tube formation assays, in vitro vascular sprouting 3D spheroid co-culture models, and de novo vascularization models in NODSCID mice.
31847126	9	94	theme	tube-like	1860:1868	arg1	structures					1870:1879	tube-like structures	1860:1879	tube-like structures	1860:1879	Addition of an OGT inhibitor, OSMI-1, significantly reduced the number of tube-like structures and tube length similar to control levels.
31847126	6	95	theme	primary	1326:1332	arg1	cells					1352:1356	IPAH primary isolated vascular cells	1321:1356	IPAH primary isolated vascular cells	1321:1356	We showed that knockdown of OGT resulted in reduced vascular endothelial growth factor (VEGF) expression in IPAH primary isolated vascular cells.
31847126	8	96	theme	IPAH	1650:1653	arg1	PAECs					1655:1659	human IPAH PAECs	1644:1659	human IPAH PAECs	1644:1659	Furthermore, human IPAH PAECs demonstrated a significantly higher degree of capillary tube-like structures and increased length compared to control PAECs.
31847126	14	97	theme	potential	2750:2758	arg1	target					2772:2777	a potential therapeutic target	2748:2777	a potential therapeutic target for treating the angiogenic dysregulation that is present in IPAH	2748:2843	Therefore, we believe that the OGT/O-GlcNAc axis may be a potential therapeutic target for treating the angiogenic dysregulation that is present in IPAH.
31847126	14	97	theme	potential	2750:2758	arg1	axis					2736:2739	the OGT/O-GlcNAc axis	2719:2739	the OGT/O-GlcNAc axis	2719:2739	Therefore, we believe that the OGT/O-GlcNAc axis may be a potential therapeutic target for treating the angiogenic dysregulation that is present in IPAH.
31847126	14	98	from	IPAH	2840:2843	arg1	present					2829:2835	present	2829:2835	present	2829:2835	Therefore, we believe that the OGT/O-GlcNAc axis may be a potential therapeutic target for treating the angiogenic dysregulation that is present in IPAH.
31847126	14	98	from	IPAH	2840:2843	arg1	dysregulation					2807:2819	the angiogenic dysregulation	2792:2819	the angiogenic dysregulation that is present in IPAH	2792:2843	Therefore, we believe that the OGT/O-GlcNAc axis may be a potential therapeutic target for treating the angiogenic dysregulation that is present in IPAH.
31847126	11	99	theme	de	2278:2279	arg1	vascularization					2286:2300	de novo vascularization	2278:2300	de novo vascularization	2278:2300	Blocking OGT activity in these experiments, however, altered the vascular sprouting and de novo vascularization in IPAH similar to control levels when compared to controls.
31847126	7	100	theme	specificity	1372:1382	arg1	protein					1384:1390	specificity protein 1	1372:1392	specificity protein 1 (SP1)	1372:1398	In addition, specificity protein 1 (SP1), a known stimulator of VEGF expression, was shown to have higher O-GlcNAc levels in IPAH compared to control at physiological (5 mM) and high (25 mM) glucose concentrations, and knockdown resulted in decreased VEGF protein levels.
31847126	7	100	theme	specificity	1372:1382	arg1	SP1					1395:1397	SP1	1395:1397	SP1	1395:1397	In addition, specificity protein 1 (SP1), a known stimulator of VEGF expression, was shown to have higher O-GlcNAc levels in IPAH compared to control at physiological (5 mM) and high (25 mM) glucose concentrations, and knockdown resulted in decreased VEGF protein levels.
31847126	7	100	theme	specificity	1372:1382	arg1	stimulator					1409:1418	a known stimulator	1401:1418	a known stimulator of VEGF expression	1401:1437	In addition, specificity protein 1 (SP1), a known stimulator of VEGF expression, was shown to have higher O-GlcNAc levels in IPAH compared to control at physiological (5 mM) and high (25 mM) glucose concentrations, and knockdown resulted in decreased VEGF protein levels.
31847126	14	101	attach	present	2829:2835	arg2	dysregulation					2807:2819	the angiogenic dysregulation	2792:2819	the angiogenic dysregulation that is present in IPAH	2792:2843	Therefore, we believe that the OGT/O-GlcNAc axis may be a potential therapeutic target for treating the angiogenic dysregulation that is present in IPAH.
31847126	14	101	attach	present	2829:2835	arg1	IPAH					2840:2843	IPAH	2840:2843	IPAH	2840:2843	Therefore, we believe that the OGT/O-GlcNAc axis may be a potential therapeutic target for treating the angiogenic dysregulation that is present in IPAH.
31847126	14	101	attach	present	2829:2835	arg2	present					2829:2835	present	2829:2835	present	2829:2835	Therefore, we believe that the OGT/O-GlcNAc axis may be a potential therapeutic target for treating the angiogenic dysregulation that is present in IPAH.
31847126	5	102	theme	formation	1084:1092	arg1	assays					1094:1099	tube formation assays	1079:1099	tube formation assays	1079:1099	Primary isolated human control and IPAH patient PASMCs and pulmonary arterial endothelial cells (PAECs) were grown in the presence or absence of OGT inhibitors and subjected to biochemical assessments in monolayer cultures and tube formation assays, in vitro vascular sprouting 3D spheroid co-culture models, and de novo vascularization models in NODSCID mice.
31847126	5	103	theme	pulmonary	911:919	arg1	PAECs					949:953	PAECs	949:953	PAECs	949:953	Primary isolated human control and IPAH patient PASMCs and pulmonary arterial endothelial cells (PAECs) were grown in the presence or absence of OGT inhibitors and subjected to biochemical assessments in monolayer cultures and tube formation assays, in vitro vascular sprouting 3D spheroid co-culture models, and de novo vascularization models in NODSCID mice.
31847126	5	103	theme	pulmonary	911:919	arg1	cells					942:946	pulmonary arterial endothelial cells	911:946	pulmonary arterial endothelial cells (PAECs)	911:954	Primary isolated human control and IPAH patient PASMCs and pulmonary arterial endothelial cells (PAECs) were grown in the presence or absence of OGT inhibitors and subjected to biochemical assessments in monolayer cultures and tube formation assays, in vitro vascular sprouting 3D spheroid co-culture models, and de novo vascularization models in NODSCID mice.
31847126	7	104	theme	high	1537:1540	arg1	concentrations					1558:1571	physiological (5 mM) and high (25 mM) glucose concentrations	1512:1571	physiological (5 mM) and high (25 mM) glucose concentrations	1512:1571	In addition, specificity protein 1 (SP1), a known stimulator of VEGF expression, was shown to have higher O-GlcNAc levels in IPAH compared to control at physiological (5 mM) and high (25 mM) glucose concentrations, and knockdown resulted in decreased VEGF protein levels.
31847126	10	105	theme	collagen	2107:2114	arg1	implants					2116:2123	control and PAEC-embedded collagen implants	2081:2123	control and PAEC-embedded collagen implants	2081:2123	Assessment of vascular sprouting from an in vitro 3D spheroid co-culture model using IPAH and control PAEC/PASMCs and an in vivo vascularization model using control and PAEC-embedded collagen implants demonstrated higher vascularization in IPAH compared to control.
31847126	12	106	from	findings	2367:2374	arg1	report					2384:2389	this report	2379:2389	this report	2379:2389	Our findings in this report are the first to describe a role for the OGT/O-GlcNAc axis in modulating VEGF expression and vascularization in IPAH.
31847126	3	107	theme	proper	642:647	arg1	function					654:661	proper cell function	642:661	proper cell function	642:661	OGT is a cellular nutrient sensor that is essential in maintaining proper cell function through the regulation of cell signaling, proliferation, and metabolism.
31847126	5	108	theme	endothelial	930:940	arg1	PAECs					949:953	PAECs	949:953	PAECs	949:953	Primary isolated human control and IPAH patient PASMCs and pulmonary arterial endothelial cells (PAECs) were grown in the presence or absence of OGT inhibitors and subjected to biochemical assessments in monolayer cultures and tube formation assays, in vitro vascular sprouting 3D spheroid co-culture models, and de novo vascularization models in NODSCID mice.
31847126	5	108	theme	endothelial	930:940	arg1	cells					942:946	pulmonary arterial endothelial cells	911:946	pulmonary arterial endothelial cells (PAECs)	911:954	Primary isolated human control and IPAH patient PASMCs and pulmonary arterial endothelial cells (PAECs) were grown in the presence or absence of OGT inhibitors and subjected to biochemical assessments in monolayer cultures and tube formation assays, in vitro vascular sprouting 3D spheroid co-culture models, and de novo vascularization models in NODSCID mice.
31847126	10	109	theme	PAEC-embedded	2093:2105	arg1	implants					2116:2123	control and PAEC-embedded collagen implants	2081:2123	control and PAEC-embedded collagen implants	2081:2123	Assessment of vascular sprouting from an in vitro 3D spheroid co-culture model using IPAH and control PAEC/PASMCs and an in vivo vascularization model using control and PAEC-embedded collagen implants demonstrated higher vascularization in IPAH compared to control.
31847126	13	110	dep	role	2567:2570	arg1	have					2619:2622	have	2619:2622	may have on the angiogenic process and the development of plexiform lesions	2615:2689	These findings provide greater insight into the potential role that altered glucose uptake and metabolism may have on the angiogenic process and the development of plexiform lesions.
31847126	10	111	theme	control	2081:2087	arg1	implants					2116:2123	control and PAEC-embedded collagen implants	2081:2123	control and PAEC-embedded collagen implants	2081:2123	Assessment of vascular sprouting from an in vitro 3D spheroid co-culture model using IPAH and control PAEC/PASMCs and an in vivo vascularization model using control and PAEC-embedded collagen implants demonstrated higher vascularization in IPAH compared to control.
31847126	13	112	theme	glucose	2585:2591	arg1	uptake					2593:2598	altered glucose uptake	2577:2598	altered glucose uptake	2577:2598	These findings provide greater insight into the potential role that altered glucose uptake and metabolism may have on the angiogenic process and the development of plexiform lesions.
31847126	5	113	theme	monolayer	1056:1064	arg1	cultures					1066:1073	monolayer cultures	1056:1073	monolayer cultures	1056:1073	Primary isolated human control and IPAH patient PASMCs and pulmonary arterial endothelial cells (PAECs) were grown in the presence or absence of OGT inhibitors and subjected to biochemical assessments in monolayer cultures and tube formation assays, in vitro vascular sprouting 3D spheroid co-culture models, and de novo vascularization models in NODSCID mice.
31847126	8	114	theme	capillary	1707:1715	arg1	structures					1727:1736	capillary tube-like structures	1707:1736	capillary tube-like structures	1707:1736	Furthermore, human IPAH PAECs demonstrated a significantly higher degree of capillary tube-like structures and increased length compared to control PAECs.
31847126	5	115	theme	IPAH	887:890	arg1	PASMCs					900:905	Primary isolated human control and IPAH patient PASMCs	852:905	PASMCs	900:905	Primary isolated human control and IPAH patient PASMCs and pulmonary arterial endothelial cells (PAECs) were grown in the presence or absence of OGT inhibitors and subjected to biochemical assessments in monolayer cultures and tube formation assays, in vitro vascular sprouting 3D spheroid co-culture models, and de novo vascularization models in NODSCID mice.
31847126	2	116	theme	muscle	532:537	arg1	proliferation					552:564	pulmonary arterial smooth muscle cell (PASMC) proliferation	506:564	pulmonary arterial smooth muscle cell (PASMC) proliferation	506:564	The serine/threonine hydroxyl-linked N-Acetylglucosamine (O-GlcNAc) transferase (OGT) has been shown to drive pulmonary arterial smooth muscle cell (PASMC) proliferation in IPAH.
31847126	10	117	theme	vascular	1938:1945	arg1	sprouting					1947:1955	vascular sprouting	1938:1955	vascular sprouting from an in vitro 3D spheroid co-culture model using IPAH and control PAEC/PASMCs and an in vivo vascularization model using control and PAEC-embedded collagen implants	1938:2123	Assessment of vascular sprouting from an in vitro 3D spheroid co-culture model using IPAH and control PAEC/PASMCs and an in vivo vascularization model using control and PAEC-embedded collagen implants demonstrated higher vascularization in IPAH compared to control.
31847126	5	118	theme	sprouting	1120:1128	arg1	models					1153:1158	in vitro vascular sprouting 3D spheroid co-culture models	1102:1158	in vitro vascular sprouting 3D spheroid co-culture models	1102:1158	Primary isolated human control and IPAH patient PASMCs and pulmonary arterial endothelial cells (PAECs) were grown in the presence or absence of OGT inhibitors and subjected to biochemical assessments in monolayer cultures and tube formation assays, in vitro vascular sprouting 3D spheroid co-culture models, and de novo vascularization models in NODSCID mice.
31847126	8	119	theme	structures	1727:1736	arg1	degree					1697:1702	a significantly higher degree	1674:1702	a significantly higher degree of capillary tube-like structures	1674:1736	Furthermore, human IPAH PAECs demonstrated a significantly higher degree of capillary tube-like structures and increased length compared to control PAECs.
31847126	7	120	dep	high	1537:1540	arg1	mM					1546:1547	25 mM	1543:1547	25 mM	1543:1547	In addition, specificity protein 1 (SP1), a known stimulator of VEGF expression, was shown to have higher O-GlcNAc levels in IPAH compared to control at physiological (5 mM) and high (25 mM) glucose concentrations, and knockdown resulted in decreased VEGF protein levels.
31847126	7	121	theme	physiological	1512:1524	arg1	concentrations					1558:1571	physiological (5 mM) and high (25 mM) glucose concentrations	1512:1571	physiological (5 mM) and high (25 mM) glucose concentrations	1512:1571	In addition, specificity protein 1 (SP1), a known stimulator of VEGF expression, was shown to have higher O-GlcNAc levels in IPAH compared to control at physiological (5 mM) and high (25 mM) glucose concentrations, and knockdown resulted in decreased VEGF protein levels.
31847126	2	122	theme	arterial	516:523	arg1	proliferation					552:564	pulmonary arterial smooth muscle cell (PASMC) proliferation	506:564	pulmonary arterial smooth muscle cell (PASMC) proliferation	506:564	The serine/threonine hydroxyl-linked N-Acetylglucosamine (O-GlcNAc) transferase (OGT) has been shown to drive pulmonary arterial smooth muscle cell (PASMC) proliferation in IPAH.
31847126	5	123	dep	de	1165:1166	arg1	novo					1168:1171	novo	1168:1171	novo	1168:1171	Primary isolated human control and IPAH patient PASMCs and pulmonary arterial endothelial cells (PAECs) were grown in the presence or absence of OGT inhibitors and subjected to biochemical assessments in monolayer cultures and tube formation assays, in vitro vascular sprouting 3D spheroid co-culture models, and de novo vascularization models in NODSCID mice.
31847126	10	124	theme	3D	1974:1975	arg1	model					1997:2001	an in vitro 3D spheroid co-culture model	1962:2001	an in vitro 3D spheroid co-culture model using IPAH and control PAEC/PASMCs	1962:2036	Assessment of vascular sprouting from an in vitro 3D spheroid co-culture model using IPAH and control PAEC/PASMCs and an in vivo vascularization model using control and PAEC-embedded collagen implants demonstrated higher vascularization in IPAH compared to control.
31847126	13	125	theme	potential	2557:2565	arg1	role					2567:2570	the potential role	2553:2570	the potential role that altered glucose uptake and metabolism may have on the angiogenic process and the development of plexiform lesions	2553:2689	These findings provide greater insight into the potential role that altered glucose uptake and metabolism may have on the angiogenic process and the development of plexiform lesions.
31847126	5	126	theme	spheroid	1133:1140	arg1	models					1153:1158	in vitro vascular sprouting 3D spheroid co-culture models	1102:1158	in vitro vascular sprouting 3D spheroid co-culture models	1102:1158	Primary isolated human control and IPAH patient PASMCs and pulmonary arterial endothelial cells (PAECs) were grown in the presence or absence of OGT inhibitors and subjected to biochemical assessments in monolayer cultures and tube formation assays, in vitro vascular sprouting 3D spheroid co-culture models, and de novo vascularization models in NODSCID mice.
31847126	4	127	from	role	779:782	arg1	dysfunction					831:841	vascular and angiogenic dysfunction	807:841	dysfunction	831:841	The aim of this study was to determine the role of OGT and O-GlcNAc in vascular and angiogenic dysfunction in IPAH.
31847126	14	128	dep	potential	2750:2758	arg1	therapeutic					2760:2770	therapeutic	2760:2770	therapeutic	2760:2770	Therefore, we believe that the OGT/O-GlcNAc axis may be a potential therapeutic target for treating the angiogenic dysregulation that is present in IPAH.
31847126	10	129	theme	in	1965:1966	arg1	model					1997:2001	an in vitro 3D spheroid co-culture model	1962:2001	an in vitro 3D spheroid co-culture model using IPAH and control PAEC/PASMCs	1962:2036	Assessment of vascular sprouting from an in vitro 3D spheroid co-culture model using IPAH and control PAEC/PASMCs and an in vivo vascularization model using control and PAEC-embedded collagen implants demonstrated higher vascularization in IPAH compared to control.
31847126	5	130	from	cultures	1066:1073	arg1	mice					1207:1210	NODSCID mice	1199:1210	NODSCID mice	1199:1210	Primary isolated human control and IPAH patient PASMCs and pulmonary arterial endothelial cells (PAECs) were grown in the presence or absence of OGT inhibitors and subjected to biochemical assessments in monolayer cultures and tube formation assays, in vitro vascular sprouting 3D spheroid co-culture models, and de novo vascularization models in NODSCID mice.
31847126	1	131	theme	Idiopathic	91:100	arg1	hypertension					121:132	Idiopathic pulmonary arterial hypertension	91:132	Idiopathic pulmonary arterial hypertension (IPAH)	91:139	Idiopathic pulmonary arterial hypertension (IPAH) is considered a vasculopathy characterized by elevated pulmonary vascular resistance due to vasoconstriction and/or lung remodeling such as plexiform lesions, the hallmark of the PAH, as well as cell proliferation and vascular and angiogenic dysfunction.
31847126	1	131	theme	Idiopathic	91:100	arg1	IPAH					135:138	IPAH	135:138	IPAH	135:138	Idiopathic pulmonary arterial hypertension (IPAH) is considered a vasculopathy characterized by elevated pulmonary vascular resistance due to vasoconstriction and/or lung remodeling such as plexiform lesions, the hallmark of the PAH, as well as cell proliferation and vascular and angiogenic dysfunction.
31847126	11	132	theme	OGT	2199:2201	arg1	activity					2203:2210	OGT activity	2199:2210	OGT activity	2199:2210	Blocking OGT activity in these experiments, however, altered the vascular sprouting and de novo vascularization in IPAH similar to control levels when compared to controls.
31847126	6	133	theme	vascular	1343:1350	arg1	cells					1352:1356	IPAH primary isolated vascular cells	1321:1356	IPAH primary isolated vascular cells	1321:1356	We showed that knockdown of OGT resulted in reduced vascular endothelial growth factor (VEGF) expression in IPAH primary isolated vascular cells.
31847126	13	134	theme	greater	2532:2538	arg1	insight					2540:2546	greater insight	2532:2546	greater insight into the potential role that altered glucose uptake and metabolism may have on the angiogenic process and the development of plexiform lesions	2532:2689	These findings provide greater insight into the potential role that altered glucose uptake and metabolism may have on the angiogenic process and the development of plexiform lesions.
31847126	7	135	from	concentrations	1558:1571	arg1	control					1501:1507	control	1501:1507	control at physiological (5 mM) and high (25 mM) glucose concentrations	1501:1571	In addition, specificity protein 1 (SP1), a known stimulator of VEGF expression, was shown to have higher O-GlcNAc levels in IPAH compared to control at physiological (5 mM) and high (25 mM) glucose concentrations, and knockdown resulted in decreased VEGF protein levels.
31847126	8	136	theme	control	1771:1777	arg1	PAECs					1779:1783	control PAECs	1771:1783	control PAECs	1771:1783	Furthermore, human IPAH PAECs demonstrated a significantly higher degree of capillary tube-like structures and increased length compared to control PAECs.
31847126	1	137	theme	arterial	112:119	arg1	hypertension					121:132	Idiopathic pulmonary arterial hypertension	91:132	Idiopathic pulmonary arterial hypertension (IPAH)	91:139	Idiopathic pulmonary arterial hypertension (IPAH) is considered a vasculopathy characterized by elevated pulmonary vascular resistance due to vasoconstriction and/or lung remodeling such as plexiform lesions, the hallmark of the PAH, as well as cell proliferation and vascular and angiogenic dysfunction.
31847126	1	137	theme	arterial	112:119	arg1	IPAH					135:138	IPAH	135:138	IPAH	135:138	Idiopathic pulmonary arterial hypertension (IPAH) is considered a vasculopathy characterized by elevated pulmonary vascular resistance due to vasoconstriction and/or lung remodeling such as plexiform lesions, the hallmark of the PAH, as well as cell proliferation and vascular and angiogenic dysfunction.
31847126	7	138	theme	VEGF	1610:1613	arg1	levels					1623:1628	decreased VEGF protein levels	1600:1628	decreased VEGF protein levels	1600:1628	In addition, specificity protein 1 (SP1), a known stimulator of VEGF expression, was shown to have higher O-GlcNAc levels in IPAH compared to control at physiological (5 mM) and high (25 mM) glucose concentrations, and knockdown resulted in decreased VEGF protein levels.
31847126	7	139	theme	higher	1458:1463	arg1	levels					1474:1479	higher O-GlcNAc levels	1458:1479	higher O-GlcNAc levels in IPAH compared to control at physiological (5 mM) and high (25 mM) glucose concentrations	1458:1571	In addition, specificity protein 1 (SP1), a known stimulator of VEGF expression, was shown to have higher O-GlcNAc levels in IPAH compared to control at physiological (5 mM) and high (25 mM) glucose concentrations, and knockdown resulted in decreased VEGF protein levels.
31847126	2	140	theme	serine/threonine	400:415	arg1	N-Acetylglucosamine					433:451	The serine/threonine hydroxyl-linked N-Acetylglucosamine	396:451	The serine/threonine hydroxyl-linked N-Acetylglucosamine (O-GlcNAc) transferase (OGT)	396:480	The serine/threonine hydroxyl-linked N-Acetylglucosamine (O-GlcNAc) transferase (OGT) has been shown to drive pulmonary arterial smooth muscle cell (PASMC) proliferation in IPAH.
31847126	2	140	theme	serine/threonine	400:415	arg1	O-GlcNAc					454:461	O-GlcNAc	454:461	O-GlcNAc	454:461	The serine/threonine hydroxyl-linked N-Acetylglucosamine (O-GlcNAc) transferase (OGT) has been shown to drive pulmonary arterial smooth muscle cell (PASMC) proliferation in IPAH.
31847126	5	141	from	assays	1094:1099	arg1	mice					1207:1210	NODSCID mice	1199:1210	NODSCID mice	1199:1210	Primary isolated human control and IPAH patient PASMCs and pulmonary arterial endothelial cells (PAECs) were grown in the presence or absence of OGT inhibitors and subjected to biochemical assessments in monolayer cultures and tube formation assays, in vitro vascular sprouting 3D spheroid co-culture models, and de novo vascularization models in NODSCID mice.
31847126	6	142	from	expression	1307:1316	arg1	cells					1352:1356	IPAH primary isolated vascular cells	1321:1356	IPAH primary isolated vascular cells	1321:1356	We showed that knockdown of OGT resulted in reduced vascular endothelial growth factor (VEGF) expression in IPAH primary isolated vascular cells.
31847126	11	143	theme	vascular	2255:2262	arg1	sprouting					2264:2272	vascular sprouting	2255:2272	vascular sprouting	2255:2272	Blocking OGT activity in these experiments, however, altered the vascular sprouting and de novo vascularization in IPAH similar to control levels when compared to controls.
31847126	2	144	link	hydroxyl-linked	417:431	arg1	N-Acetylglucosamine					433:451	The serine/threonine hydroxyl-linked N-Acetylglucosamine	396:451	The serine/threonine hydroxyl-linked N-Acetylglucosamine (O-GlcNAc) transferase (OGT)	396:480	The serine/threonine hydroxyl-linked N-Acetylglucosamine (O-GlcNAc) transferase (OGT) has been shown to drive pulmonary arterial smooth muscle cell (PASMC) proliferation in IPAH.
31847126	2	144	link	hydroxyl-linked	417:431	arg1	O-GlcNAc					454:461	O-GlcNAc	454:461	O-GlcNAc	454:461	The serine/threonine hydroxyl-linked N-Acetylglucosamine (O-GlcNAc) transferase (OGT) has been shown to drive pulmonary arterial smooth muscle cell (PASMC) proliferation in IPAH.
31847126	5	145	theme	human	869:873	arg1	control					875:881	Primary isolated human control and IPAH patient PASMCs	852:905	control	875:881	Primary isolated human control and IPAH patient PASMCs and pulmonary arterial endothelial cells (PAECs) were grown in the presence or absence of OGT inhibitors and subjected to biochemical assessments in monolayer cultures and tube formation assays, in vitro vascular sprouting 3D spheroid co-culture models, and de novo vascularization models in NODSCID mice.
31847126	0	146	theme	Idiopathic	47:56	arg1	Hypertension					77:88	Idiopathic Pulmonary Arterial Hypertension	47:88	Idiopathic Pulmonary Arterial Hypertension	47:88	O-GlcNAc Transferase Regulates Angiogenesis in Idiopathic Pulmonary Arterial Hypertension.
31847126	5	147	theme	inhibitors	1001:1010	arg1	absence					986:992	absence	986:992	absence	986:992	Primary isolated human control and IPAH patient PASMCs and pulmonary arterial endothelial cells (PAECs) were grown in the presence or absence of OGT inhibitors and subjected to biochemical assessments in monolayer cultures and tube formation assays, in vitro vascular sprouting 3D spheroid co-culture models, and de novo vascularization models in NODSCID mice.
31847126	5	147	theme	inhibitors	1001:1010	arg1	presence					974:981	the presence	970:981	the presence	970:981	Primary isolated human control and IPAH patient PASMCs and pulmonary arterial endothelial cells (PAECs) were grown in the presence or absence of OGT inhibitors and subjected to biochemical assessments in monolayer cultures and tube formation assays, in vitro vascular sprouting 3D spheroid co-culture models, and de novo vascularization models in NODSCID mice.
31847126	9	148	theme	inhibitor	1805:1813	arg1	Addition					1786:1793	Addition	1786:1793	Addition of an OGT inhibitor, OSMI-1,	1786:1822	Addition of an OGT inhibitor, OSMI-1, significantly reduced the number of tube-like structures and tube length similar to control levels.
31847126	5	149	dep	in	1102:1103	arg1	vitro					1105:1109	vitro	1105:1109	vitro	1105:1109	Primary isolated human control and IPAH patient PASMCs and pulmonary arterial endothelial cells (PAECs) were grown in the presence or absence of OGT inhibitors and subjected to biochemical assessments in monolayer cultures and tube formation assays, in vitro vascular sprouting 3D spheroid co-culture models, and de novo vascularization models in NODSCID mice.
31847126	4	150	theme	vascular	807:814	arg1	dysfunction					831:841	vascular and angiogenic dysfunction	807:841	dysfunction	831:841	The aim of this study was to determine the role of OGT and O-GlcNAc in vascular and angiogenic dysfunction in IPAH.
31847126	13	151	theme	altered	2577:2583	arg1	uptake					2593:2598	altered glucose uptake	2577:2598	altered glucose uptake	2577:2598	These findings provide greater insight into the potential role that altered glucose uptake and metabolism may have on the angiogenic process and the development of plexiform lesions.
31847126	0	152	theme	Arterial	68:75	arg1	Hypertension					77:88	Idiopathic Pulmonary Arterial Hypertension	47:88	Idiopathic Pulmonary Arterial Hypertension	47:88	O-GlcNAc Transferase Regulates Angiogenesis in Idiopathic Pulmonary Arterial Hypertension.
31847126	12	153	from	vascularization	2484:2498	arg1	IPAH					2503:2506	IPAH	2503:2506	IPAH	2503:2506	Our findings in this report are the first to describe a role for the OGT/O-GlcNAc axis in modulating VEGF expression and vascularization in IPAH.
31847126	3	154	theme	signaling	694:702	arg1	regulation					675:684	the regulation	671:684	the regulation of cell signaling, proliferation, and metabolism	671:733	OGT is a cellular nutrient sensor that is essential in maintaining proper cell function through the regulation of cell signaling, proliferation, and metabolism.
31847126	4	155	theme	angiogenic	820:829	arg1	dysfunction					831:841	vascular and angiogenic dysfunction	807:841	dysfunction	831:841	The aim of this study was to determine the role of OGT and O-GlcNAc in vascular and angiogenic dysfunction in IPAH.
31847126	1	156	theme	cell	336:339	arg1	proliferation					341:353	cell proliferation	336:353	cell proliferation	336:353	Idiopathic pulmonary arterial hypertension (IPAH) is considered a vasculopathy characterized by elevated pulmonary vascular resistance due to vasoconstriction and/or lung remodeling such as plexiform lesions, the hallmark of the PAH, as well as cell proliferation and vascular and angiogenic dysfunction.
31847126	8	157	theme	higher	1690:1695	arg1	degree					1697:1702	a significantly higher degree	1674:1702	a significantly higher degree of capillary tube-like structures	1674:1736	Furthermore, human IPAH PAECs demonstrated a significantly higher degree of capillary tube-like structures and increased length compared to control PAECs.
31847126	12	158	from	expression	2469:2478	arg1	IPAH					2503:2506	IPAH	2503:2506	IPAH	2503:2506	Our findings in this report are the first to describe a role for the OGT/O-GlcNAc axis in modulating VEGF expression and vascularization in IPAH.
31847126	4	159	theme	OGT	787:789	arg1	role					779:782	the role	775:782	the role of OGT and O-GlcNAc in vascular and angiogenic dysfunction in IPAH	775:849	The aim of this study was to determine the role of OGT and O-GlcNAc in vascular and angiogenic dysfunction in IPAH.
31847126	1	160	theme	lung	257:260	arg1	remodeling					262:271	lung remodeling	257:271	lung remodeling	257:271	Idiopathic pulmonary arterial hypertension (IPAH) is considered a vasculopathy characterized by elevated pulmonary vascular resistance due to vasoconstriction and/or lung remodeling such as plexiform lesions, the hallmark of the PAH, as well as cell proliferation and vascular and angiogenic dysfunction.
31847126	2	161	theme	N-Acetylglucosamine	433:451	arg1	OGT					477:479	OGT	477:479	OGT	477:479	The serine/threonine hydroxyl-linked N-Acetylglucosamine (O-GlcNAc) transferase (OGT) has been shown to drive pulmonary arterial smooth muscle cell (PASMC) proliferation in IPAH.
31847126	2	161	theme	N-Acetylglucosamine	433:451	arg1	transferase					464:474	The serine/threonine hydroxyl-linked N-Acetylglucosamine (O-GlcNAc) transferase	396:474	The serine/threonine hydroxyl-linked N-Acetylglucosamine (O-GlcNAc) transferase (OGT)	396:480	The serine/threonine hydroxyl-linked N-Acetylglucosamine (O-GlcNAc) transferase (OGT) has been shown to drive pulmonary arterial smooth muscle cell (PASMC) proliferation in IPAH.
31847126	4	162	theme	O-GlcNAc	795:802	arg1	role					779:782	the role	775:782	the role of OGT and O-GlcNAc in vascular and angiogenic dysfunction in IPAH	775:849	The aim of this study was to determine the role of OGT and O-GlcNAc in vascular and angiogenic dysfunction in IPAH.
31847126	1	163	theme	plexiform	281:289	arg1	lesions					291:297	plexiform lesions	281:297	plexiform lesions	281:297	Idiopathic pulmonary arterial hypertension (IPAH) is considered a vasculopathy characterized by elevated pulmonary vascular resistance due to vasoconstriction and/or lung remodeling such as plexiform lesions, the hallmark of the PAH, as well as cell proliferation and vascular and angiogenic dysfunction.
16332679	6	0	theme	reciprocal	881:890	arg1	modifications					911:923	sequential and reciprocal post-translational modifications	866:923	sequential and reciprocal post-translational modifications of Sp1	866:930	Insulin elicited sequential and reciprocal post-translational modifications of Sp1.
16332679	2	1	theme	insulin-responsive	367:384	arg1	expression					386:395	constitutive and insulin-responsive expression	350:395	constitutive and insulin-responsive expression of the calmodulin gene (Majumdar, G., Harmon, A., Candelaria, R., Martinez-Hernandez, A., Raghow, R., and Solomon, S. S. (2003) Am	350:526	Sp1 is an obligatory transcription factor for constitutive and insulin-responsive expression of the calmodulin gene (Majumdar, G., Harmon, A., Candelaria, R., Martinez-Hernandez, A., Raghow, R., and Solomon, S. S. (2003) Am.
16332679	9	2	theme	Western	1382:1388	arg1	blot					1390:1393	Western blot	1382:1393	Western blot	1382:1393	Analyses of the total, O-GlcNAc-modified, or phosphorylated Sp1 by Western blot and mass spectrometry corroborated the sequential and reciprocal control of post-translational modifications of Sp1 in response to insulin.
16332679	12	3	theme	state	2007:2011	arg1	levels					2013:2018	the enhanced steady state levels	1987:2018	the enhanced steady state levels of calmodulin mRNA seen after insulin treatment	1987:2066	Later, changes in the steady state levels of phosphorylated Sp1 mimicked the enhanced steady state levels of calmodulin mRNA seen after insulin treatment.
16332679	6	4	theme	sequential	866:875	arg1	modifications					911:923	sequential and reciprocal post-translational modifications	866:923	sequential and reciprocal post-translational modifications of Sp1	866:930	Insulin elicited sequential and reciprocal post-translational modifications of Sp1.
16332679	7	5	gly	O-glycosylation	937:951	arg1	accumulation					976:987	its nuclear accumulation	964:987	its nuclear accumulation induced by insulin	964:1006	The O-glycosylation of Sp1 and its nuclear accumulation induced by insulin peaked early (approximately 30 min), followed by a steady decline of O-GlcNAc-modified Sp1 to negligible levels by 240 min.
16332679	7	5	gly	O-glycosylation	937:951	arg1	Sp1					956:958	Sp1	956:958	Sp1	956:958	The O-glycosylation of Sp1 and its nuclear accumulation induced by insulin peaked early (approximately 30 min), followed by a steady decline of O-GlcNAc-modified Sp1 to negligible levels by 240 min.
16332679	7	6	theme	O-GlcNAc-modified	1077:1093	arg1	Sp1					1095:1097	O-GlcNAc-modified Sp1	1077:1097	O-GlcNAc-modified Sp1	1077:1097	The O-glycosylation of Sp1 and its nuclear accumulation induced by insulin peaked early (approximately 30 min), followed by a steady decline of O-GlcNAc-modified Sp1 to negligible levels by 240 min.
16332679	10	7	with	Treatment	1535:1543	arg1	streptozotocin					1559:1572	streptozotocin	1559:1572	streptozotocin (a potent inhibitor of O-GlcNAcase)	1559:1608	Treatment of cells with streptozotocin (a potent inhibitor of O-GlcNAcase) led to hyperglycosylation of Sp1 that failed to be significantly phosphorylated.
16332679	10	8	theme	cells	1548:1552	arg1	Treatment					1535:1543	Treatment	1535:1543	Treatment of cells with streptozotocin (a potent inhibitor of O-GlcNAcase)	1535:1608	Treatment of cells with streptozotocin (a potent inhibitor of O-GlcNAcase) led to hyperglycosylation of Sp1 that failed to be significantly phosphorylated.
16332679	1	9	theme	Sp1	210:212	arg1	O-glycosylation					171:185	O-glycosylation	171:185	O-glycosylation	171:185	O-glycosylation and phosphorylation of Sp1 are thought to modulate the expression of a number of genes in normal and diabetic state.
16332679	1	9	theme	Sp1	210:212	arg1	phosphorylation					191:205	phosphorylation	191:205	phosphorylation	191:205	O-glycosylation and phosphorylation of Sp1 are thought to modulate the expression of a number of genes in normal and diabetic state.
16332679	8	10	theme	phosphorylated	1152:1165	arg1	Sp1					1167:1169	phosphorylated Sp1	1152:1169	phosphorylated Sp1	1152:1169	The accumulation of phosphorylated Sp1 in the nuclei of insulin-treated cells showed an opposite pattern, increasing steadily until reaching a maximum around 240 min after treatment.
16332679	8	11	theme	opposite	1220:1227	arg1	pattern					1229:1235	an opposite pattern	1217:1235	an opposite pattern	1217:1235	The accumulation of phosphorylated Sp1 in the nuclei of insulin-treated cells showed an opposite pattern, increasing steadily until reaching a maximum around 240 min after treatment.
16332679	2	12	theme	obligatory	314:323	arg1	factor					339:344	an obligatory transcription factor	311:344	an obligatory transcription factor for constitutive and insulin-responsive expression of the calmodulin gene (Majumdar, G., Harmon, A., Candelaria, R., Martinez-Hernandez, A., Raghow, R., and Solomon, S. S. (2003) Am	311:526	Sp1 is an obligatory transcription factor for constitutive and insulin-responsive expression of the calmodulin gene (Majumdar, G., Harmon, A., Candelaria, R., Martinez-Hernandez, A., Raghow, R., and Solomon, S. S. (2003) Am.
16332679	2	12	theme	obligatory	314:323	arg1	Sp1					304:306	Sp1	304:306	Sp1	304:306	Sp1 is an obligatory transcription factor for constitutive and insulin-responsive expression of the calmodulin gene (Majumdar, G., Harmon, A., Candelaria, R., Martinez-Hernandez, A., Raghow, R., and Solomon, S. S. (2003) Am.
16332679	5	13	theme	mass	830:833	arg1	spectrometry					835:846	flight mass spectrometry	823:846	flight mass spectrometry	823:846	Here we report the temporal dynamics of accumulation of total, O-GlcNAc-modified, and phosphorylated Sp1 in H-411E hepatoma cells by immunohistochemistry with monospecific antibodies, confocal microscopy, and matrix-assisted laser desorption and ionization-time of flight mass spectrometry.
16332679	12	14	theme	enhanced	1991:1998	arg1	levels					2013:2018	the enhanced steady state levels	1987:2018	the enhanced steady state levels of calmodulin mRNA seen after insulin treatment	1987:2066	Later, changes in the steady state levels of phosphorylated Sp1 mimicked the enhanced steady state levels of calmodulin mRNA seen after insulin treatment.
16332679	5	15	theme	O-GlcNAc-modified	621:637	arg1	Sp1					659:661	total, O-GlcNAc-modified, and phosphorylated Sp1	614:661	total, O-GlcNAc-modified, and phosphorylated Sp1	614:661	Here we report the temporal dynamics of accumulation of total, O-GlcNAc-modified, and phosphorylated Sp1 in H-411E hepatoma cells by immunohistochemistry with monospecific antibodies, confocal microscopy, and matrix-assisted laser desorption and ionization-time of flight mass spectrometry.
16332679	5	16	theme	laser	783:787	arg1	desorption					789:798	matrix-assisted laser desorption and ionization-time	767:818	desorption	789:798	Here we report the temporal dynamics of accumulation of total, O-GlcNAc-modified, and phosphorylated Sp1 in H-411E hepatoma cells by immunohistochemistry with monospecific antibodies, confocal microscopy, and matrix-assisted laser desorption and ionization-time of flight mass spectrometry.
16332679	0	17	from	phosphorylation	91:105	arg1	cells					164:168	liver cells	158:168	liver cells	158:168	Insulin dynamically regulates calmodulin gene expression by sequential o-glycosylation and phosphorylation of sp1 and its subcellular compartmentalization in liver cells.
16332679	0	18	theme	liver	158:162	arg1	cells					164:168	liver cells	158:168	liver cells	158:168	Insulin dynamically regulates calmodulin gene expression by sequential o-glycosylation and phosphorylation of sp1 and its subcellular compartmentalization in liver cells.
16332679	8	19	theme	insulin-treated	1188:1202	arg1	cells					1204:1208	insulin-treated cells	1188:1208	insulin-treated cells	1188:1208	The accumulation of phosphorylated Sp1 in the nuclei of insulin-treated cells showed an opposite pattern, increasing steadily until reaching a maximum around 240 min after treatment.
16332679	6	20	theme	Sp1	928:930	arg1	modifications					911:923	sequential and reciprocal post-translational modifications	866:923	sequential and reciprocal post-translational modifications of Sp1	866:930	Insulin elicited sequential and reciprocal post-translational modifications of Sp1.
16332679	0	21	from	o-glycosylation	71:85	arg1	cells					164:168	liver cells	158:168	liver cells	158:168	Insulin dynamically regulates calmodulin gene expression by sequential o-glycosylation and phosphorylation of sp1 and its subcellular compartmentalization in liver cells.
16332679	13	22	gly	O-glycosylation	2075:2089	arg1	Sp1					2094:2096	Sp1	2094:2096	Sp1	2094:2096	Thus, O-glycosylation of Sp1 appears to be critical for its localization into the nucleus, where it undergoes obligatory phosphorylation that is needed for Sp1 to activate calmodulin gene expression.
16332679	10	23	theme	O-GlcNAcase	1597:1607	arg1	inhibitor					1584:1592	a potent inhibitor	1575:1592	a potent inhibitor of O-GlcNAcase	1575:1607	Treatment of cells with streptozotocin (a potent inhibitor of O-GlcNAcase) led to hyperglycosylation of Sp1 that failed to be significantly phosphorylated.
16332679	5	24	theme	accumulation	598:609	arg1	dynamics					586:593	the temporal dynamics	573:593	the temporal dynamics of accumulation of total, O-GlcNAc-modified, and phosphorylated Sp1 in H-411E hepatoma cells by immunohistochemistry with monospecific antibodies, confocal microscopy, and matrix-assisted laser desorption and ionization-time of flight mass spectrometry	573:846	Here we report the temporal dynamics of accumulation of total, O-GlcNAc-modified, and phosphorylated Sp1 in H-411E hepatoma cells by immunohistochemistry with monospecific antibodies, confocal microscopy, and matrix-assisted laser desorption and ionization-time of flight mass spectrometry.
16332679	9	25	theme	post-translational	1471:1488	arg1	modifications					1490:1502	post-translational modifications	1471:1502	post-translational modifications of Sp1 in response to insulin	1471:1532	Analyses of the total, O-GlcNAc-modified, or phosphorylated Sp1 by Western blot and mass spectrometry corroborated the sequential and reciprocal control of post-translational modifications of Sp1 in response to insulin.
16332679	13	26	theme	gene	2252:2255	arg1	expression					2257:2266	calmodulin gene expression	2241:2266	calmodulin gene expression	2241:2266	Thus, O-glycosylation of Sp1 appears to be critical for its localization into the nucleus, where it undergoes obligatory phosphorylation that is needed for Sp1 to activate calmodulin gene expression.
16332679	5	27	theme	total	614:618	arg1	Sp1					659:661	total, O-GlcNAc-modified, and phosphorylated Sp1	614:661	total, O-GlcNAc-modified, and phosphorylated Sp1	614:661	Here we report the temporal dynamics of accumulation of total, O-GlcNAc-modified, and phosphorylated Sp1 in H-411E hepatoma cells by immunohistochemistry with monospecific antibodies, confocal microscopy, and matrix-assisted laser desorption and ionization-time of flight mass spectrometry.
16332679	10	28	gly	hyperglycosylation	1617:1634	arg1	Sp1					1639:1641	Sp1	1639:1641	Sp1	1639:1641	Treatment of cells with streptozotocin (a potent inhibitor of O-GlcNAcase) led to hyperglycosylation of Sp1 that failed to be significantly phosphorylated.
16332679	7	29	theme	nuclear	968:974	arg1	accumulation					976:987	its nuclear accumulation	964:987	its nuclear accumulation induced by insulin	964:1006	The O-glycosylation of Sp1 and its nuclear accumulation induced by insulin peaked early (approximately 30 min), followed by a steady decline of O-GlcNAc-modified Sp1 to negligible levels by 240 min.
16332679	0	30	from	sp1	110:112	arg1	cells					164:168	liver cells	158:168	liver cells	158:168	Insulin dynamically regulates calmodulin gene expression by sequential o-glycosylation and phosphorylation of sp1 and its subcellular compartmentalization in liver cells.
16332679	12	31	from	changes	1921:1927	arg1	levels					1949:1954	the steady state levels	1932:1954	the steady state levels of phosphorylated Sp1	1932:1976	Later, changes in the steady state levels of phosphorylated Sp1 mimicked the enhanced steady state levels of calmodulin mRNA seen after insulin treatment.
16332679	4	32	dep	285	541:543	arg1	E584-E591					546:554	E584-E591	546:554	E584-E591	546:554	285, E584-E591).
16332679	11	33	from	cytoplasm	1888:1896	arg1	translocation					1869:1881	its rapid translocation	1859:1881	its rapid translocation from cytoplasm to the nucleus	1859:1911	The mass spectrometry data indicated that a number of common serine residues of Sp1 undergo time-dependent, reciprocal O-glycosylation and phosphorylation, paralleling its rapid translocation from cytoplasm to the nucleus.
16332679	11	34	theme	serine	1752:1757	arg1	residues					1759:1766	common serine residues	1745:1766	common serine residues of Sp1	1745:1773	The mass spectrometry data indicated that a number of common serine residues of Sp1 undergo time-dependent, reciprocal O-glycosylation and phosphorylation, paralleling its rapid translocation from cytoplasm to the nucleus.
16332679	11	34	theme	serine	1752:1757	arg1	Sp1					1771:1773	Sp1	1771:1773	Sp1	1771:1773	The mass spectrometry data indicated that a number of common serine residues of Sp1 undergo time-dependent, reciprocal O-glycosylation and phosphorylation, paralleling its rapid translocation from cytoplasm to the nucleus.
16332679	0	35	theme	sp1	110:112	arg1	phosphorylation					91:105	phosphorylation	91:105	phosphorylation	91:105	Insulin dynamically regulates calmodulin gene expression by sequential o-glycosylation and phosphorylation of sp1 and its subcellular compartmentalization in liver cells.
16332679	0	35	theme	sp1	110:112	arg1	o-glycosylation					71:85	sequential o-glycosylation	60:85	sequential o-glycosylation	60:85	Insulin dynamically regulates calmodulin gene expression by sequential o-glycosylation and phosphorylation of sp1 and its subcellular compartmentalization in liver cells.
16332679	5	36	theme	H-411E	666:671	arg1	cells					682:686	H-411E hepatoma cells	666:686	H-411E hepatoma cells	666:686	Here we report the temporal dynamics of accumulation of total, O-GlcNAc-modified, and phosphorylated Sp1 in H-411E hepatoma cells by immunohistochemistry with monospecific antibodies, confocal microscopy, and matrix-assisted laser desorption and ionization-time of flight mass spectrometry.
16332679	7	37	dep	peaked	1008:1013	arg1	min					1039:1041	approximately 30 min	1022:1041	approximately 30 min	1022:1041	The O-glycosylation of Sp1 and its nuclear accumulation induced by insulin peaked early (approximately 30 min), followed by a steady decline of O-GlcNAc-modified Sp1 to negligible levels by 240 min.
16332679	7	37	dep	peaked	1008:1013	arg1	followed					1045:1052	followed	1045:1052	followed by a steady decline of O-GlcNAc-modified Sp1 to negligible levels by 240 min	1045:1129	The O-glycosylation of Sp1 and its nuclear accumulation induced by insulin peaked early (approximately 30 min), followed by a steady decline of O-GlcNAc-modified Sp1 to negligible levels by 240 min.
16332679	2	38	theme	gene	415:418	arg1	expression					386:395	constitutive and insulin-responsive expression	350:395	constitutive and insulin-responsive expression of the calmodulin gene (Majumdar, G., Harmon, A., Candelaria, R., Martinez-Hernandez, A., Raghow, R., and Solomon, S. S. (2003) Am	350:526	Sp1 is an obligatory transcription factor for constitutive and insulin-responsive expression of the calmodulin gene (Majumdar, G., Harmon, A., Candelaria, R., Martinez-Hernandez, A., Raghow, R., and Solomon, S. S. (2003) Am.
16332679	1	39	theme	diabetic	288:295	arg1	state					297:301	normal and diabetic state	277:301	normal and diabetic state	277:301	O-glycosylation and phosphorylation of Sp1 are thought to modulate the expression of a number of genes in normal and diabetic state.
16332679	5	40	with	desorption	789:798	arg1	antibodies					730:739	monospecific antibodies	717:739	monospecific antibodies	717:739	Here we report the temporal dynamics of accumulation of total, O-GlcNAc-modified, and phosphorylated Sp1 in H-411E hepatoma cells by immunohistochemistry with monospecific antibodies, confocal microscopy, and matrix-assisted laser desorption and ionization-time of flight mass spectrometry.
16332679	7	41	theme	accumulation	976:987	arg1	O-glycosylation					937:951	The O-glycosylation	933:951	The O-glycosylation of Sp1 and its nuclear accumulation induced by insulin	933:1006	The O-glycosylation of Sp1 and its nuclear accumulation induced by insulin peaked early (approximately 30 min), followed by a steady decline of O-GlcNAc-modified Sp1 to negligible levels by 240 min.
16332679	5	42	theme	spectrometry	835:846	arg1	desorption					789:798	matrix-assisted laser desorption and ionization-time	767:818	desorption	789:798	Here we report the temporal dynamics of accumulation of total, O-GlcNAc-modified, and phosphorylated Sp1 in H-411E hepatoma cells by immunohistochemistry with monospecific antibodies, confocal microscopy, and matrix-assisted laser desorption and ionization-time of flight mass spectrometry.
16332679	5	42	theme	spectrometry	835:846	arg1	microscopy					751:760	confocal microscopy	742:760	confocal microscopy	742:760	Here we report the temporal dynamics of accumulation of total, O-GlcNAc-modified, and phosphorylated Sp1 in H-411E hepatoma cells by immunohistochemistry with monospecific antibodies, confocal microscopy, and matrix-assisted laser desorption and ionization-time of flight mass spectrometry.
16332679	5	42	theme	spectrometry	835:846	arg1	ionization-time					804:818	matrix-assisted laser desorption and ionization-time	767:818	ionization-time	804:818	Here we report the temporal dynamics of accumulation of total, O-GlcNAc-modified, and phosphorylated Sp1 in H-411E hepatoma cells by immunohistochemistry with monospecific antibodies, confocal microscopy, and matrix-assisted laser desorption and ionization-time of flight mass spectrometry.
16332679	5	42	theme	spectrometry	835:846	arg1	immunohistochemistry					691:710	immunohistochemistry	691:710	immunohistochemistry with monospecific antibodies	691:739	Here we report the temporal dynamics of accumulation of total, O-GlcNAc-modified, and phosphorylated Sp1 in H-411E hepatoma cells by immunohistochemistry with monospecific antibodies, confocal microscopy, and matrix-assisted laser desorption and ionization-time of flight mass spectrometry.
16332679	11	43	theme	mass	1695:1698	arg1	spectrometry					1700:1711	mass spectrometry	1695:1711	The mass spectrometry data	1691:1716	The mass spectrometry data indicated that a number of common serine residues of Sp1 undergo time-dependent, reciprocal O-glycosylation and phosphorylation, paralleling its rapid translocation from cytoplasm to the nucleus.
16332679	2	44	dep	G.	431:432	arg1	Am					525:526	Am	525:526	Am	525:526	Sp1 is an obligatory transcription factor for constitutive and insulin-responsive expression of the calmodulin gene (Majumdar, G., Harmon, A., Candelaria, R., Martinez-Hernandez, A., Raghow, R., and Solomon, S. S. (2003) Am.
16332679	5	45	theme	monospecific	717:728	arg1	antibodies					730:739	monospecific antibodies	717:739	monospecific antibodies	717:739	Here we report the temporal dynamics of accumulation of total, O-GlcNAc-modified, and phosphorylated Sp1 in H-411E hepatoma cells by immunohistochemistry with monospecific antibodies, confocal microscopy, and matrix-assisted laser desorption and ionization-time of flight mass spectrometry.
16332679	0	46	theme	gene	41:44	arg1	expression					46:55	calmodulin gene expression	30:55	calmodulin gene expression	30:55	Insulin dynamically regulates calmodulin gene expression by sequential o-glycosylation and phosphorylation of sp1 and its subcellular compartmentalization in liver cells.
16332679	11	47	theme	rapid	1863:1867	arg1	translocation					1869:1881	its rapid translocation	1859:1881	its rapid translocation from cytoplasm to the nucleus	1859:1911	The mass spectrometry data indicated that a number of common serine residues of Sp1 undergo time-dependent, reciprocal O-glycosylation and phosphorylation, paralleling its rapid translocation from cytoplasm to the nucleus.
16332679	8	48	from	accumulation	1136:1147	arg1	nuclei					1178:1183	the nuclei	1174:1183	the nuclei of insulin-treated cells	1174:1208	The accumulation of phosphorylated Sp1 in the nuclei of insulin-treated cells showed an opposite pattern, increasing steadily until reaching a maximum around 240 min after treatment.
16332679	5	49	with	ionization-time	804:818	arg1	antibodies					730:739	monospecific antibodies	717:739	monospecific antibodies	717:739	Here we report the temporal dynamics of accumulation of total, O-GlcNAc-modified, and phosphorylated Sp1 in H-411E hepatoma cells by immunohistochemistry with monospecific antibodies, confocal microscopy, and matrix-assisted laser desorption and ionization-time of flight mass spectrometry.
16332679	2	50	dep	gene	415:418	arg1	R.					495:496	R.	495:496	R.	495:496	Sp1 is an obligatory transcription factor for constitutive and insulin-responsive expression of the calmodulin gene (Majumdar, G., Harmon, A., Candelaria, R., Martinez-Hernandez, A., Raghow, R., and Solomon, S. S. (2003) Am.
16332679	2	50	dep	gene	415:418	arg1	A.					443:444	A.	443:444	A.	443:444	Sp1 is an obligatory transcription factor for constitutive and insulin-responsive expression of the calmodulin gene (Majumdar, G., Harmon, A., Candelaria, R., Martinez-Hernandez, A., Raghow, R., and Solomon, S. S. (2003) Am.
16332679	2	50	dep	gene	415:418	arg1	2003					519:522	2003	519:522	2003	519:522	Sp1 is an obligatory transcription factor for constitutive and insulin-responsive expression of the calmodulin gene (Majumdar, G., Harmon, A., Candelaria, R., Martinez-Hernandez, A., Raghow, R., and Solomon, S. S. (2003) Am.
16332679	2	50	dep	gene	415:418	arg1	A.					483:484	A.	483:484	A.	483:484	Sp1 is an obligatory transcription factor for constitutive and insulin-responsive expression of the calmodulin gene (Majumdar, G., Harmon, A., Candelaria, R., Martinez-Hernandez, A., Raghow, R., and Solomon, S. S. (2003) Am.
16332679	2	50	dep	gene	415:418	arg1	G.					431:432	G.	431:432	G.	431:432	Sp1 is an obligatory transcription factor for constitutive and insulin-responsive expression of the calmodulin gene (Majumdar, G., Harmon, A., Candelaria, R., Martinez-Hernandez, A., Raghow, R., and Solomon, S. S. (2003) Am.
16332679	2	50	dep	gene	415:418	arg1	S.					512:513	S.	512:513	S.	512:513	Sp1 is an obligatory transcription factor for constitutive and insulin-responsive expression of the calmodulin gene (Majumdar, G., Harmon, A., Candelaria, R., Martinez-Hernandez, A., Raghow, R., and Solomon, S. S. (2003) Am.
16332679	2	50	dep	gene	415:418	arg1	R.					459:460	R.	459:460	R.	459:460	Sp1 is an obligatory transcription factor for constitutive and insulin-responsive expression of the calmodulin gene (Majumdar, G., Harmon, A., Candelaria, R., Martinez-Hernandez, A., Raghow, R., and Solomon, S. S. (2003) Am.
16332679	2	50	dep	gene	415:418	arg1	S					515:515	S	515:515	S	515:515	Sp1 is an obligatory transcription factor for constitutive and insulin-responsive expression of the calmodulin gene (Majumdar, G., Harmon, A., Candelaria, R., Martinez-Hernandez, A., Raghow, R., and Solomon, S. S. (2003) Am.
16332679	9	51	theme	phosphorylated	1360:1373	arg1	Sp1					1375:1377	the total, O-GlcNAc-modified, or phosphorylated Sp1	1327:1377	the total, O-GlcNAc-modified, or phosphorylated Sp1	1327:1377	Analyses of the total, O-GlcNAc-modified, or phosphorylated Sp1 by Western blot and mass spectrometry corroborated the sequential and reciprocal control of post-translational modifications of Sp1 in response to insulin.
16332679	0	52	theme	sequential	60:69	arg1	o-glycosylation					71:85	sequential o-glycosylation	60:85	sequential o-glycosylation	60:85	Insulin dynamically regulates calmodulin gene expression by sequential o-glycosylation and phosphorylation of sp1 and its subcellular compartmentalization in liver cells.
16332679	6	53	theme	post-translational	892:909	arg1	modifications					911:923	sequential and reciprocal post-translational modifications	866:923	sequential and reciprocal post-translational modifications of Sp1	866:930	Insulin elicited sequential and reciprocal post-translational modifications of Sp1.
16332679	5	54	from	dynamics	586:593	arg1	cells					682:686	H-411E hepatoma cells	666:686	H-411E hepatoma cells	666:686	Here we report the temporal dynamics of accumulation of total, O-GlcNAc-modified, and phosphorylated Sp1 in H-411E hepatoma cells by immunohistochemistry with monospecific antibodies, confocal microscopy, and matrix-assisted laser desorption and ionization-time of flight mass spectrometry.
16332679	7	55	theme	Sp1	1095:1097	arg1	decline					1066:1072	a steady decline	1057:1072	a steady decline of O-GlcNAc-modified Sp1 to negligible levels	1057:1118	The O-glycosylation of Sp1 and its nuclear accumulation induced by insulin peaked early (approximately 30 min), followed by a steady decline of O-GlcNAc-modified Sp1 to negligible levels by 240 min.
16332679	1	56	theme	genes	268:272	arg1	number					258:263	a number	256:263	a number of genes	256:272	O-glycosylation and phosphorylation of Sp1 are thought to modulate the expression of a number of genes in normal and diabetic state.
16332679	9	57	from	response	1514:1521	arg1	modifications					1490:1502	post-translational modifications	1471:1502	post-translational modifications of Sp1 in response to insulin	1471:1532	Analyses of the total, O-GlcNAc-modified, or phosphorylated Sp1 by Western blot and mass spectrometry corroborated the sequential and reciprocal control of post-translational modifications of Sp1 in response to insulin.
16332679	5	58	theme	temporal	577:584	arg1	dynamics					586:593	the temporal dynamics	573:593	the temporal dynamics of accumulation of total, O-GlcNAc-modified, and phosphorylated Sp1 in H-411E hepatoma cells by immunohistochemistry with monospecific antibodies, confocal microscopy, and matrix-assisted laser desorption and ionization-time of flight mass spectrometry	573:846	Here we report the temporal dynamics of accumulation of total, O-GlcNAc-modified, and phosphorylated Sp1 in H-411E hepatoma cells by immunohistochemistry with monospecific antibodies, confocal microscopy, and matrix-assisted laser desorption and ionization-time of flight mass spectrometry.
16332679	1	59	theme	normal	277:282	arg1	state					297:301	normal and diabetic state	277:301	normal and diabetic state	277:301	O-glycosylation and phosphorylation of Sp1 are thought to modulate the expression of a number of genes in normal and diabetic state.
16332679	12	60	theme	steady	2000:2005	arg1	levels					2013:2018	the enhanced steady state levels	1987:2018	the enhanced steady state levels of calmodulin mRNA seen after insulin treatment	1987:2066	Later, changes in the steady state levels of phosphorylated Sp1 mimicked the enhanced steady state levels of calmodulin mRNA seen after insulin treatment.
16332679	9	61	from	Sp1	1507:1509	arg1	response					1514:1521	response	1514:1521	response to insulin	1514:1532	Analyses of the total, O-GlcNAc-modified, or phosphorylated Sp1 by Western blot and mass spectrometry corroborated the sequential and reciprocal control of post-translational modifications of Sp1 in response to insulin.
16332679	7	62	theme	steady	1059:1064	arg1	decline					1066:1072	a steady decline	1057:1072	a steady decline of O-GlcNAc-modified Sp1 to negligible levels	1057:1118	The O-glycosylation of Sp1 and its nuclear accumulation induced by insulin peaked early (approximately 30 min), followed by a steady decline of O-GlcNAc-modified Sp1 to negligible levels by 240 min.
16332679	9	63	theme	mass	1399:1402	arg1	spectrometry					1404:1415	mass spectrometry	1399:1415	mass spectrometry	1399:1415	Analyses of the total, O-GlcNAc-modified, or phosphorylated Sp1 by Western blot and mass spectrometry corroborated the sequential and reciprocal control of post-translational modifications of Sp1 in response to insulin.
16332679	9	64	from	modifications	1490:1502	arg1	response					1514:1521	response	1514:1521	response to insulin	1514:1532	Analyses of the total, O-GlcNAc-modified, or phosphorylated Sp1 by Western blot and mass spectrometry corroborated the sequential and reciprocal control of post-translational modifications of Sp1 in response to insulin.
16332679	8	65	theme	cells	1204:1208	arg1	nuclei					1178:1183	the nuclei	1174:1183	the nuclei of insulin-treated cells	1174:1208	The accumulation of phosphorylated Sp1 in the nuclei of insulin-treated cells showed an opposite pattern, increasing steadily until reaching a maximum around 240 min after treatment.
16332679	13	66	theme	obligatory	2179:2188	arg1	phosphorylation					2190:2204	obligatory phosphorylation	2179:2204	obligatory phosphorylation that is needed for Sp1 to activate calmodulin gene expression	2179:2266	Thus, O-glycosylation of Sp1 appears to be critical for its localization into the nucleus, where it undergoes obligatory phosphorylation that is needed for Sp1 to activate calmodulin gene expression.
16332679	2	67	theme	transcription	325:337	arg1	factor					339:344	an obligatory transcription factor	311:344	an obligatory transcription factor for constitutive and insulin-responsive expression of the calmodulin gene (Majumdar, G., Harmon, A., Candelaria, R., Martinez-Hernandez, A., Raghow, R., and Solomon, S. S. (2003) Am	311:526	Sp1 is an obligatory transcription factor for constitutive and insulin-responsive expression of the calmodulin gene (Majumdar, G., Harmon, A., Candelaria, R., Martinez-Hernandez, A., Raghow, R., and Solomon, S. S. (2003) Am.
16332679	2	67	theme	transcription	325:337	arg1	Sp1					304:306	Sp1	304:306	Sp1	304:306	Sp1 is an obligatory transcription factor for constitutive and insulin-responsive expression of the calmodulin gene (Majumdar, G., Harmon, A., Candelaria, R., Martinez-Hernandez, A., Raghow, R., and Solomon, S. S. (2003) Am.
16332679	5	68	theme	flight	823:828	arg1	spectrometry					835:846	flight mass spectrometry	823:846	flight mass spectrometry	823:846	Here we report the temporal dynamics of accumulation of total, O-GlcNAc-modified, and phosphorylated Sp1 in H-411E hepatoma cells by immunohistochemistry with monospecific antibodies, confocal microscopy, and matrix-assisted laser desorption and ionization-time of flight mass spectrometry.
16332679	12	69	theme	Sp1	1974:1976	arg1	levels					1949:1954	the steady state levels	1932:1954	the steady state levels of phosphorylated Sp1	1932:1976	Later, changes in the steady state levels of phosphorylated Sp1 mimicked the enhanced steady state levels of calmodulin mRNA seen after insulin treatment.
16332679	10	70	theme	potent	1577:1582	arg1	inhibitor					1584:1592	a potent inhibitor	1575:1592	a potent inhibitor of O-GlcNAcase	1575:1607	Treatment of cells with streptozotocin (a potent inhibitor of O-GlcNAcase) led to hyperglycosylation of Sp1 that failed to be significantly phosphorylated.
16332679	9	71	theme	sequential	1434:1443	arg1	control					1460:1466	the sequential and reciprocal control	1430:1466	the sequential and reciprocal control of post-translational modifications of Sp1 in response to insulin	1430:1532	Analyses of the total, O-GlcNAc-modified, or phosphorylated Sp1 by Western blot and mass spectrometry corroborated the sequential and reciprocal control of post-translational modifications of Sp1 in response to insulin.
16332679	8	72	theme	Sp1	1167:1169	arg1	accumulation					1136:1147	The accumulation	1132:1147	The accumulation of phosphorylated Sp1 in the nuclei of insulin-treated cells	1132:1208	The accumulation of phosphorylated Sp1 in the nuclei of insulin-treated cells showed an opposite pattern, increasing steadily until reaching a maximum around 240 min after treatment.
16332679	5	73	with	microscopy	751:760	arg1	antibodies					730:739	monospecific antibodies	717:739	monospecific antibodies	717:739	Here we report the temporal dynamics of accumulation of total, O-GlcNAc-modified, and phosphorylated Sp1 in H-411E hepatoma cells by immunohistochemistry with monospecific antibodies, confocal microscopy, and matrix-assisted laser desorption and ionization-time of flight mass spectrometry.
16332679	11	74	theme	time-dependent	1783:1796	arg1	O-glycosylation					1810:1824	O-glycosylation	1810:1824	O-glycosylation	1810:1824	The mass spectrometry data indicated that a number of common serine residues of Sp1 undergo time-dependent, reciprocal O-glycosylation and phosphorylation, paralleling its rapid translocation from cytoplasm to the nucleus.
16332679	9	75	theme	reciprocal	1449:1458	arg1	control					1460:1466	the sequential and reciprocal control	1430:1466	the sequential and reciprocal control of post-translational modifications of Sp1 in response to insulin	1430:1532	Analyses of the total, O-GlcNAc-modified, or phosphorylated Sp1 by Western blot and mass spectrometry corroborated the sequential and reciprocal control of post-translational modifications of Sp1 in response to insulin.
16332679	12	76	theme	state	1943:1947	arg1	levels					1949:1954	the steady state levels	1932:1954	the steady state levels of phosphorylated Sp1	1932:1976	Later, changes in the steady state levels of phosphorylated Sp1 mimicked the enhanced steady state levels of calmodulin mRNA seen after insulin treatment.
16332679	1	77	gly	O-glycosylation	171:185	arg1	Sp1					210:212	Sp1	210:212	Sp1	210:212	O-glycosylation and phosphorylation of Sp1 are thought to modulate the expression of a number of genes in normal and diabetic state.
16332679	1	78	from	expression	242:251	arg1	state					297:301	normal and diabetic state	277:301	normal and diabetic state	277:301	O-glycosylation and phosphorylation of Sp1 are thought to modulate the expression of a number of genes in normal and diabetic state.
16332679	9	79	theme	modifications	1490:1502	arg1	control					1460:1466	the sequential and reciprocal control	1430:1466	the sequential and reciprocal control of post-translational modifications of Sp1 in response to insulin	1430:1532	Analyses of the total, O-GlcNAc-modified, or phosphorylated Sp1 by Western blot and mass spectrometry corroborated the sequential and reciprocal control of post-translational modifications of Sp1 in response to insulin.
16332679	5	80	with	immunohistochemistry	691:710	arg1	antibodies					730:739	monospecific antibodies	717:739	monospecific antibodies	717:739	Here we report the temporal dynamics of accumulation of total, O-GlcNAc-modified, and phosphorylated Sp1 in H-411E hepatoma cells by immunohistochemistry with monospecific antibodies, confocal microscopy, and matrix-assisted laser desorption and ionization-time of flight mass spectrometry.
16332679	11	81	theme	common	1745:1750	arg1	residues					1759:1766	common serine residues	1745:1766	common serine residues of Sp1	1745:1773	The mass spectrometry data indicated that a number of common serine residues of Sp1 undergo time-dependent, reciprocal O-glycosylation and phosphorylation, paralleling its rapid translocation from cytoplasm to the nucleus.
16332679	11	81	theme	common	1745:1750	arg1	Sp1					1771:1773	Sp1	1771:1773	Sp1	1771:1773	The mass spectrometry data indicated that a number of common serine residues of Sp1 undergo time-dependent, reciprocal O-glycosylation and phosphorylation, paralleling its rapid translocation from cytoplasm to the nucleus.
16332679	5	82	theme	hepatoma	673:680	arg1	cells					682:686	H-411E hepatoma cells	666:686	H-411E hepatoma cells	666:686	Here we report the temporal dynamics of accumulation of total, O-GlcNAc-modified, and phosphorylated Sp1 in H-411E hepatoma cells by immunohistochemistry with monospecific antibodies, confocal microscopy, and matrix-assisted laser desorption and ionization-time of flight mass spectrometry.
16332679	5	83	from	cells	682:686	arg1	dynamics					586:593	the temporal dynamics	573:593	the temporal dynamics of accumulation of total, O-GlcNAc-modified, and phosphorylated Sp1 in H-411E hepatoma cells by immunohistochemistry with monospecific antibodies, confocal microscopy, and matrix-assisted laser desorption and ionization-time of flight mass spectrometry	573:846	Here we report the temporal dynamics of accumulation of total, O-GlcNAc-modified, and phosphorylated Sp1 in H-411E hepatoma cells by immunohistochemistry with monospecific antibodies, confocal microscopy, and matrix-assisted laser desorption and ionization-time of flight mass spectrometry.
16332679	5	84	theme	matrix-assisted	767:781	arg1	desorption					789:798	matrix-assisted laser desorption and ionization-time	767:818	desorption	789:798	Here we report the temporal dynamics of accumulation of total, O-GlcNAc-modified, and phosphorylated Sp1 in H-411E hepatoma cells by immunohistochemistry with monospecific antibodies, confocal microscopy, and matrix-assisted laser desorption and ionization-time of flight mass spectrometry.
16332679	9	85	theme	Sp1	1507:1509	arg1	modifications					1490:1502	post-translational modifications	1471:1502	post-translational modifications of Sp1 in response to insulin	1471:1532	Analyses of the total, O-GlcNAc-modified, or phosphorylated Sp1 by Western blot and mass spectrometry corroborated the sequential and reciprocal control of post-translational modifications of Sp1 in response to insulin.
16332679	12	86	theme	insulin	2050:2056	arg1	treatment					2058:2066	insulin treatment	2050:2066	insulin treatment	2050:2066	Later, changes in the steady state levels of phosphorylated Sp1 mimicked the enhanced steady state levels of calmodulin mRNA seen after insulin treatment.
16332679	5	87	theme	Sp1	659:661	arg1	accumulation					598:609	accumulation	598:609	accumulation of total, O-GlcNAc-modified, and phosphorylated Sp1 in H-411E hepatoma cells	598:686	Here we report the temporal dynamics of accumulation of total, O-GlcNAc-modified, and phosphorylated Sp1 in H-411E hepatoma cells by immunohistochemistry with monospecific antibodies, confocal microscopy, and matrix-assisted laser desorption and ionization-time of flight mass spectrometry.
16332679	11	88	dep	time-dependent	1783:1796	arg1	reciprocal					1799:1808	reciprocal	1799:1808	reciprocal	1799:1808	The mass spectrometry data indicated that a number of common serine residues of Sp1 undergo time-dependent, reciprocal O-glycosylation and phosphorylation, paralleling its rapid translocation from cytoplasm to the nucleus.
16332679	0	89	theme	compartmentalization	134:153	arg1	phosphorylation					91:105	phosphorylation	91:105	phosphorylation	91:105	Insulin dynamically regulates calmodulin gene expression by sequential o-glycosylation and phosphorylation of sp1 and its subcellular compartmentalization in liver cells.
16332679	0	89	theme	compartmentalization	134:153	arg1	o-glycosylation					71:85	sequential o-glycosylation	60:85	sequential o-glycosylation	60:85	Insulin dynamically regulates calmodulin gene expression by sequential o-glycosylation and phosphorylation of sp1 and its subcellular compartmentalization in liver cells.
16332679	11	90	theme	Sp1	1771:1773	arg1	residues					1759:1766	common serine residues	1745:1766	common serine residues of Sp1	1745:1773	The mass spectrometry data indicated that a number of common serine residues of Sp1 undergo time-dependent, reciprocal O-glycosylation and phosphorylation, paralleling its rapid translocation from cytoplasm to the nucleus.
16332679	11	90	theme	Sp1	1771:1773	arg1	Sp1					1771:1773	Sp1	1771:1773	Sp1	1771:1773	The mass spectrometry data indicated that a number of common serine residues of Sp1 undergo time-dependent, reciprocal O-glycosylation and phosphorylation, paralleling its rapid translocation from cytoplasm to the nucleus.
16332679	5	91	theme	phosphorylated	644:657	arg1	Sp1					659:661	total, O-GlcNAc-modified, and phosphorylated Sp1	614:661	total, O-GlcNAc-modified, and phosphorylated Sp1	614:661	Here we report the temporal dynamics of accumulation of total, O-GlcNAc-modified, and phosphorylated Sp1 in H-411E hepatoma cells by immunohistochemistry with monospecific antibodies, confocal microscopy, and matrix-assisted laser desorption and ionization-time of flight mass spectrometry.
16332679	13	92	theme	Sp1	2094:2096	arg1	O-glycosylation					2075:2089	O-glycosylation	2075:2089	O-glycosylation of Sp1	2075:2096	Thus, O-glycosylation of Sp1 appears to be critical for its localization into the nucleus, where it undergoes obligatory phosphorylation that is needed for Sp1 to activate calmodulin gene expression.
16332679	12	93	theme	steady	1936:1941	arg1	levels					1949:1954	the steady state levels	1932:1954	the steady state levels of phosphorylated Sp1	1932:1976	Later, changes in the steady state levels of phosphorylated Sp1 mimicked the enhanced steady state levels of calmodulin mRNA seen after insulin treatment.
16332679	7	94	theme	Sp1	956:958	arg1	O-glycosylation					937:951	The O-glycosylation	933:951	The O-glycosylation of Sp1 and its nuclear accumulation induced by insulin	933:1006	The O-glycosylation of Sp1 and its nuclear accumulation induced by insulin peaked early (approximately 30 min), followed by a steady decline of O-GlcNAc-modified Sp1 to negligible levels by 240 min.
16332679	0	95	gly	o-glycosylation	71:85	arg1	compartmentalization					134:153	its subcellular compartmentalization	118:153	its subcellular compartmentalization	118:153	Insulin dynamically regulates calmodulin gene expression by sequential o-glycosylation and phosphorylation of sp1 and its subcellular compartmentalization in liver cells.
16332679	0	95	gly	o-glycosylation	71:85	arg1	sp1					110:112	sp1	110:112	sp1	110:112	Insulin dynamically regulates calmodulin gene expression by sequential o-glycosylation and phosphorylation of sp1 and its subcellular compartmentalization in liver cells.
16332679	11	96	theme	residues	1759:1766	arg1	number					1735:1740	a number	1733:1740	a number of common serine residues of Sp1	1733:1773	The mass spectrometry data indicated that a number of common serine residues of Sp1 undergo time-dependent, reciprocal O-glycosylation and phosphorylation, paralleling its rapid translocation from cytoplasm to the nucleus.
16332679	0	97	theme	subcellular	122:132	arg1	compartmentalization					134:153	its subcellular compartmentalization	118:153	its subcellular compartmentalization	118:153	Insulin dynamically regulates calmodulin gene expression by sequential o-glycosylation and phosphorylation of sp1 and its subcellular compartmentalization in liver cells.
16332679	0	98	from	compartmentalization	134:153	arg1	cells					164:168	liver cells	158:168	liver cells	158:168	Insulin dynamically regulates calmodulin gene expression by sequential o-glycosylation and phosphorylation of sp1 and its subcellular compartmentalization in liver cells.
16332679	10	99	theme	Sp1	1639:1641	arg1	hyperglycosylation					1617:1634	hyperglycosylation	1617:1634	hyperglycosylation of Sp1 that failed to be significantly phosphorylated	1617:1688	Treatment of cells with streptozotocin (a potent inhibitor of O-GlcNAcase) led to hyperglycosylation of Sp1 that failed to be significantly phosphorylated.
16332679	5	100	theme	confocal	742:749	arg1	microscopy					751:760	confocal microscopy	742:760	confocal microscopy	742:760	Here we report the temporal dynamics of accumulation of total, O-GlcNAc-modified, and phosphorylated Sp1 in H-411E hepatoma cells by immunohistochemistry with monospecific antibodies, confocal microscopy, and matrix-assisted laser desorption and ionization-time of flight mass spectrometry.
16332679	2	101	theme	calmodulin	404:413	arg1	gene					415:418	the calmodulin gene	400:418	the calmodulin gene (Majumdar, G., Harmon, A., Candelaria, R., Martinez-Hernandez, A., Raghow, R., and Solomon, S. S. (2003) Am	400:526	Sp1 is an obligatory transcription factor for constitutive and insulin-responsive expression of the calmodulin gene (Majumdar, G., Harmon, A., Candelaria, R., Martinez-Hernandez, A., Raghow, R., and Solomon, S. S. (2003) Am.
16332679	0	102	theme	calmodulin	30:39	arg1	expression					46:55	calmodulin gene expression	30:55	calmodulin gene expression	30:55	Insulin dynamically regulates calmodulin gene expression by sequential o-glycosylation and phosphorylation of sp1 and its subcellular compartmentalization in liver cells.
16332679	13	103	theme	calmodulin	2241:2250	arg1	expression					2257:2266	calmodulin gene expression	2241:2266	calmodulin gene expression	2241:2266	Thus, O-glycosylation of Sp1 appears to be critical for its localization into the nucleus, where it undergoes obligatory phosphorylation that is needed for Sp1 to activate calmodulin gene expression.
16332679	1	104	theme	number	258:263	arg1	expression					242:251	the expression	238:251	the expression of a number of genes in normal and diabetic state	238:301	O-glycosylation and phosphorylation of Sp1 are thought to modulate the expression of a number of genes in normal and diabetic state.
16332679	7	105	theme	negligible	1102:1111	arg1	levels					1113:1118	negligible levels	1102:1118	negligible levels	1102:1118	The O-glycosylation of Sp1 and its nuclear accumulation induced by insulin peaked early (approximately 30 min), followed by a steady decline of O-GlcNAc-modified Sp1 to negligible levels by 240 min.
16332679	9	106	theme	total	1331:1335	arg1	Sp1					1375:1377	the total, O-GlcNAc-modified, or phosphorylated Sp1	1327:1377	the total, O-GlcNAc-modified, or phosphorylated Sp1	1327:1377	Analyses of the total, O-GlcNAc-modified, or phosphorylated Sp1 by Western blot and mass spectrometry corroborated the sequential and reciprocal control of post-translational modifications of Sp1 in response to insulin.
16332679	12	107	theme	calmodulin	2023:2032	arg1	mRNA					2034:2037	calmodulin mRNA	2023:2037	calmodulin mRNA seen after insulin treatment	2023:2066	Later, changes in the steady state levels of phosphorylated Sp1 mimicked the enhanced steady state levels of calmodulin mRNA seen after insulin treatment.
16332679	10	108	dep	streptozotocin	1559:1572	arg1	inhibitor					1584:1592	a potent inhibitor	1575:1592	a potent inhibitor of O-GlcNAcase	1575:1607	Treatment of cells with streptozotocin (a potent inhibitor of O-GlcNAcase) led to hyperglycosylation of Sp1 that failed to be significantly phosphorylated.
16332679	11	109	gly	O-glycosylation	1810:1824	arg1	number					1735:1740	a number	1733:1740	a number of common serine residues of Sp1	1733:1773	The mass spectrometry data indicated that a number of common serine residues of Sp1 undergo time-dependent, reciprocal O-glycosylation and phosphorylation, paralleling its rapid translocation from cytoplasm to the nucleus.
16332679	2	110	theme	constitutive	350:361	arg1	expression					386:395	constitutive and insulin-responsive expression	350:395	constitutive and insulin-responsive expression of the calmodulin gene (Majumdar, G., Harmon, A., Candelaria, R., Martinez-Hernandez, A., Raghow, R., and Solomon, S. S. (2003) Am	350:526	Sp1 is an obligatory transcription factor for constitutive and insulin-responsive expression of the calmodulin gene (Majumdar, G., Harmon, A., Candelaria, R., Martinez-Hernandez, A., Raghow, R., and Solomon, S. S. (2003) Am.
16332679	9	111	theme	O-GlcNAc-modified	1338:1354	arg1	Sp1					1375:1377	the total, O-GlcNAc-modified, or phosphorylated Sp1	1327:1377	the total, O-GlcNAc-modified, or phosphorylated Sp1	1327:1377	Analyses of the total, O-GlcNAc-modified, or phosphorylated Sp1 by Western blot and mass spectrometry corroborated the sequential and reciprocal control of post-translational modifications of Sp1 in response to insulin.
16332679	0	112	from	cells	164:168	arg1	phosphorylation					91:105	phosphorylation	91:105	phosphorylation	91:105	Insulin dynamically regulates calmodulin gene expression by sequential o-glycosylation and phosphorylation of sp1 and its subcellular compartmentalization in liver cells.
16332679	0	112	from	cells	164:168	arg1	o-glycosylation					71:85	sequential o-glycosylation	60:85	sequential o-glycosylation	60:85	Insulin dynamically regulates calmodulin gene expression by sequential o-glycosylation and phosphorylation of sp1 and its subcellular compartmentalization in liver cells.
16332679	11	113	theme	spectrometry	1700:1711	arg1	data					1713:1716	The mass spectrometry data	1691:1716	The mass spectrometry data	1691:1716	The mass spectrometry data indicated that a number of common serine residues of Sp1 undergo time-dependent, reciprocal O-glycosylation and phosphorylation, paralleling its rapid translocation from cytoplasm to the nucleus.
16332679	12	114	theme	mRNA	2034:2037	arg1	levels					2013:2018	the enhanced steady state levels	1987:2018	the enhanced steady state levels of calmodulin mRNA seen after insulin treatment	1987:2066	Later, changes in the steady state levels of phosphorylated Sp1 mimicked the enhanced steady state levels of calmodulin mRNA seen after insulin treatment.
16332679	12	115	theme	phosphorylated	1959:1972	arg1	Sp1					1974:1976	phosphorylated Sp1	1959:1976	phosphorylated Sp1	1959:1976	Later, changes in the steady state levels of phosphorylated Sp1 mimicked the enhanced steady state levels of calmodulin mRNA seen after insulin treatment.
16332679	5	116	from	accumulation	598:609	arg1	cells					682:686	H-411E hepatoma cells	666:686	H-411E hepatoma cells	666:686	Here we report the temporal dynamics of accumulation of total, O-GlcNAc-modified, and phosphorylated Sp1 in H-411E hepatoma cells by immunohistochemistry with monospecific antibodies, confocal microscopy, and matrix-assisted laser desorption and ionization-time of flight mass spectrometry.
16332679	9	117	theme	Sp1	1375:1377	arg1	Analyses					1315:1322	Analyses	1315:1322	Analyses of the total, O-GlcNAc-modified, or phosphorylated Sp1 by Western blot and mass spectrometry	1315:1415	Analyses of the total, O-GlcNAc-modified, or phosphorylated Sp1 by Western blot and mass spectrometry corroborated the sequential and reciprocal control of post-translational modifications of Sp1 in response to insulin.
15158436	7	0	theme	70-kDa-heat	1158:1168	arg1	members					1184:1190	70-kDa-heat shock protein members	1158:1190	70-kDa-heat shock protein members	1158:1190	These results strongly suggest that O-GlcNAc influences protein stability through specific interaction with 70-kDa-heat shock protein members.
15158436	2	1	from	conformation	363:374	arg1	pathway					395:401	the proteasomal pathway	379:401	the proteasomal pathway	379:401	Considering that Hsp70 is a crucial component in the quality control of protein conformation in the proteasomal pathway, we investigated the possibility that Hsp70 physically interacts with O-GlcNAc proteins through a lectinic activity.
15158436	2	2	theme	proteasomal	383:393	arg1	pathway					395:401	the proteasomal pathway	379:401	the proteasomal pathway	379:401	Considering that Hsp70 is a crucial component in the quality control of protein conformation in the proteasomal pathway, we investigated the possibility that Hsp70 physically interacts with O-GlcNAc proteins through a lectinic activity.
15158436	7	3	theme	specific	1132:1139	arg1	interaction					1141:1151	specific interaction	1132:1151	specific interaction with 70-kDa-heat shock protein members	1132:1190	These results strongly suggest that O-GlcNAc influences protein stability through specific interaction with 70-kDa-heat shock protein members.
15158436	2	4	from	control	344:350	arg1	pathway					395:401	the proteasomal pathway	379:401	the proteasomal pathway	379:401	Considering that Hsp70 is a crucial component in the quality control of protein conformation in the proteasomal pathway, we investigated the possibility that Hsp70 physically interacts with O-GlcNAc proteins through a lectinic activity.
15158436	2	5	theme	crucial	311:317	arg1	component					319:327	a crucial component	309:327	a crucial component in the quality control of protein conformation in the proteasomal pathway	309:401	Considering that Hsp70 is a crucial component in the quality control of protein conformation in the proteasomal pathway, we investigated the possibility that Hsp70 physically interacts with O-GlcNAc proteins through a lectinic activity.
15158436	2	5	theme	crucial	311:317	arg1	Hsp70					300:304	Hsp70	300:304	Hsp70	300:304	Considering that Hsp70 is a crucial component in the quality control of protein conformation in the proteasomal pathway, we investigated the possibility that Hsp70 physically interacts with O-GlcNAc proteins through a lectinic activity.
15158436	1	6	theme	proteasomal	199:209	arg1	degradation					211:221	the proteasomal degradation	195:221	the proteasomal degradation	195:221	Numerous works demonstrated that the dynamic O-GlcNAc glycosylation could protect against the proteasomal degradation by modifying the target proteins and the proteasome itself.
15158436	0	7	theme	lectinic	49:56	arg1	activity					58:65	an adjustable lectinic activity	35:65	an adjustable lectinic activity towards O-linked N-acetylglucosamine	35:102	70-kDa-heat shock protein presents an adjustable lectinic activity towards O-linked N-acetylglucosamine.
15158436	2	8	from	pathway	395:401	arg1	control					344:350	the quality control	332:350	the quality control of protein conformation in the proteasomal pathway	332:401	Considering that Hsp70 is a crucial component in the quality control of protein conformation in the proteasomal pathway, we investigated the possibility that Hsp70 physically interacts with O-GlcNAc proteins through a lectinic activity.
15158436	0	9	theme	shock	12:16	arg1	protein					18:24	70-kDa-heat shock protein	0:24	70-kDa-heat shock protein	0:24	70-kDa-heat shock protein presents an adjustable lectinic activity towards O-linked N-acetylglucosamine.
15158436	1	10	theme	Numerous	105:112	arg1	works					114:118	Numerous works	105:118	Numerous works	105:118	Numerous works demonstrated that the dynamic O-GlcNAc glycosylation could protect against the proteasomal degradation by modifying the target proteins and the proteasome itself.
15158436	0	11	theme	70-kDa-heat	0:10	arg1	protein					18:24	70-kDa-heat shock protein	0:24	70-kDa-heat shock protein	0:24	70-kDa-heat shock protein presents an adjustable lectinic activity towards O-linked N-acetylglucosamine.
15158436	3	12	theme	O-GlcNAc	594:601	arg1	residues					603:610	O-GlcNAc residues	594:610	O-GlcNAc residues	594:610	First, we demonstrate that in HepG2 cells, Hsp70 can specifically bind to O-GlcNAc residues but also is itself modified by O-GlcNAc.
15158436	7	13	theme	protein	1106:1112	arg1	stability					1114:1122	protein stability	1106:1122	protein stability	1106:1122	These results strongly suggest that O-GlcNAc influences protein stability through specific interaction with 70-kDa-heat shock protein members.
15158436	5	14	theme	degrees	833:839	arg1	C					841:841	a 42 degrees C	828:841	a 42 degrees C thermic stress	828:856	On the other hand, a 42 degrees C thermic stress did not affect any of these features.
15158436	2	15	theme	quality	336:342	arg1	control					344:350	the quality control	332:350	the quality control of protein conformation in the proteasomal pathway	332:401	Considering that Hsp70 is a crucial component in the quality control of protein conformation in the proteasomal pathway, we investigated the possibility that Hsp70 physically interacts with O-GlcNAc proteins through a lectinic activity.
15158436	5	16	theme	thermic	843:849	arg1	stress					851:856	a 42 degrees C thermic stress	828:856	a 42 degrees C thermic stress	828:856	On the other hand, a 42 degrees C thermic stress did not affect any of these features.
15158436	2	17	theme	O-GlcNAc	473:480	arg1	proteins					482:489	O-GlcNAc proteins	473:489	O-GlcNAc proteins	473:489	Considering that Hsp70 is a crucial component in the quality control of protein conformation in the proteasomal pathway, we investigated the possibility that Hsp70 physically interacts with O-GlcNAc proteins through a lectinic activity.
15158436	3	18	theme	HepG2	550:554	arg1	cells					556:560	HepG2 cells	550:560	HepG2 cells	550:560	First, we demonstrate that in HepG2 cells, Hsp70 can specifically bind to O-GlcNAc residues but also is itself modified by O-GlcNAc.
15158436	1	19	theme	target	240:245	arg1	proteins					247:254	the target proteins	236:254	the target proteins	236:254	Numerous works demonstrated that the dynamic O-GlcNAc glycosylation could protect against the proteasomal degradation by modifying the target proteins and the proteasome itself.
15158436	0	20	theme	adjustable	38:47	arg1	activity					58:65	an adjustable lectinic activity	35:65	an adjustable lectinic activity towards O-linked N-acetylglucosamine	35:102	70-kDa-heat shock protein presents an adjustable lectinic activity towards O-linked N-acetylglucosamine.
15158436	4	21	theme	Hsp70	716:720	arg1	activity					731:738	Hsp70 lectinic activity	716:738	Hsp70 lectinic activity	716:738	Second, when cells were deprived of glucose (nutrient stress), Hsp70 lectinic activity markedly increased whereas its glycosylation dramatically decreased.
15158436	5	22	theme	other	816:820	arg1	hand					822:825	the other hand	812:825	the other hand	812:825	On the other hand, a 42 degrees C thermic stress did not affect any of these features.
15158436	7	23	theme	shock	1170:1174	arg1	members					1184:1190	70-kDa-heat shock protein members	1158:1190	70-kDa-heat shock protein members	1158:1190	These results strongly suggest that O-GlcNAc influences protein stability through specific interaction with 70-kDa-heat shock protein members.
15158436	6	24	theme	co-immunoprecipitating	945:966	arg1	proteins					936:943	O-GlcNAc modified proteins	918:943	O-GlcNAc modified proteins co-immunoprecipitating with Hsp70	918:977	Lastly, the nature of O-GlcNAc modified proteins co-immunoprecipitating with Hsp70 was similar for cells submitted to the thermic and to nutrient stress.
15158436	6	25	with	co-immunoprecipitating	945:966	arg1	Hsp70					973:977	Hsp70	973:977	Hsp70	973:977	Lastly, the nature of O-GlcNAc modified proteins co-immunoprecipitating with Hsp70 was similar for cells submitted to the thermic and to nutrient stress.
15158436	4	26	theme	lectinic	722:729	arg1	activity					731:738	Hsp70 lectinic activity	716:738	Hsp70 lectinic activity	716:738	Second, when cells were deprived of glucose (nutrient stress), Hsp70 lectinic activity markedly increased whereas its glycosylation dramatically decreased.
15158436	2	27	theme	lectinic	501:508	arg1	activity					510:517	a lectinic activity	499:517	a lectinic activity	499:517	Considering that Hsp70 is a crucial component in the quality control of protein conformation in the proteasomal pathway, we investigated the possibility that Hsp70 physically interacts with O-GlcNAc proteins through a lectinic activity.
15158436	6	28	theme	proteins	936:943	arg1	nature					908:913	the nature	904:913	the nature of O-GlcNAc modified proteins co-immunoprecipitating with Hsp70	904:977	Lastly, the nature of O-GlcNAc modified proteins co-immunoprecipitating with Hsp70 was similar for cells submitted to the thermic and to nutrient stress.
15158436	6	28	theme	proteins	936:943	arg1	similar					983:989	similar	983:989	similar	983:989	Lastly, the nature of O-GlcNAc modified proteins co-immunoprecipitating with Hsp70 was similar for cells submitted to the thermic and to nutrient stress.
15158436	0	29	link	O-linked	75:82	arg1	N-acetylglucosamine					84:102	O-linked N-acetylglucosamine	75:102	O-linked N-acetylglucosamine	75:102	70-kDa-heat shock protein presents an adjustable lectinic activity towards O-linked N-acetylglucosamine.
15158436	1	30	theme	dynamic	142:148	arg1	glycosylation					159:171	the dynamic O-GlcNAc glycosylation	138:171	the dynamic O-GlcNAc glycosylation	138:171	Numerous works demonstrated that the dynamic O-GlcNAc glycosylation could protect against the proteasomal degradation by modifying the target proteins and the proteasome itself.
15158436	6	31	theme	modified	927:934	arg1	proteins					936:943	O-GlcNAc modified proteins	918:943	O-GlcNAc modified proteins co-immunoprecipitating with Hsp70	918:977	Lastly, the nature of O-GlcNAc modified proteins co-immunoprecipitating with Hsp70 was similar for cells submitted to the thermic and to nutrient stress.
15158436	7	32	theme	protein	1176:1182	arg1	members					1184:1190	70-kDa-heat shock protein members	1158:1190	70-kDa-heat shock protein members	1158:1190	These results strongly suggest that O-GlcNAc influences protein stability through specific interaction with 70-kDa-heat shock protein members.
15158436	1	33	theme	O-GlcNAc	150:157	arg1	glycosylation					159:171	the dynamic O-GlcNAc glycosylation	138:171	the dynamic O-GlcNAc glycosylation	138:171	Numerous works demonstrated that the dynamic O-GlcNAc glycosylation could protect against the proteasomal degradation by modifying the target proteins and the proteasome itself.
15158436	6	34	theme	nutrient	1033:1040	arg1	stress					1042:1047	nutrient stress	1033:1047	nutrient stress	1033:1047	Lastly, the nature of O-GlcNAc modified proteins co-immunoprecipitating with Hsp70 was similar for cells submitted to the thermic and to nutrient stress.
15158436	5	35	theme	C	841:841	arg1	stress					851:856	a 42 degrees C thermic stress	828:856	a 42 degrees C thermic stress	828:856	On the other hand, a 42 degrees C thermic stress did not affect any of these features.
15158436	2	36	theme	protein	355:361	arg1	conformation					363:374	protein conformation	355:374	protein conformation in the proteasomal pathway	355:401	Considering that Hsp70 is a crucial component in the quality control of protein conformation in the proteasomal pathway, we investigated the possibility that Hsp70 physically interacts with O-GlcNAc proteins through a lectinic activity.
15158436	2	37	theme	conformation	363:374	arg1	control					344:350	the quality control	332:350	the quality control of protein conformation in the proteasomal pathway	332:401	Considering that Hsp70 is a crucial component in the quality control of protein conformation in the proteasomal pathway, we investigated the possibility that Hsp70 physically interacts with O-GlcNAc proteins through a lectinic activity.
15158436	0	38	theme	O-linked	75:82	arg1	N-acetylglucosamine					84:102	O-linked N-acetylglucosamine	75:102	O-linked N-acetylglucosamine	75:102	70-kDa-heat shock protein presents an adjustable lectinic activity towards O-linked N-acetylglucosamine.
15158436	7	39	with	interaction	1141:1151	arg1	members					1184:1190	70-kDa-heat shock protein members	1158:1190	70-kDa-heat shock protein members	1158:1190	These results strongly suggest that O-GlcNAc influences protein stability through specific interaction with 70-kDa-heat shock protein members.
15158436	2	40	from	component	319:327	arg1	control					344:350	the quality control	332:350	the quality control of protein conformation in the proteasomal pathway	332:401	Considering that Hsp70 is a crucial component in the quality control of protein conformation in the proteasomal pathway, we investigated the possibility that Hsp70 physically interacts with O-GlcNAc proteins through a lectinic activity.
15158436	4	41	dep	deprived	677:684	arg1	stress					707:712	nutrient stress	698:712	nutrient stress	698:712	Second, when cells were deprived of glucose (nutrient stress), Hsp70 lectinic activity markedly increased whereas its glycosylation dramatically decreased.
15158436	4	42	theme	nutrient	698:705	arg1	stress					707:712	nutrient stress	698:712	nutrient stress	698:712	Second, when cells were deprived of glucose (nutrient stress), Hsp70 lectinic activity markedly increased whereas its glycosylation dramatically decreased.
36888912	3	0	theme	inhibitor	774:782	arg1	G					792:792	the OGA inhibitor Thiamet G	766:792	the OGA inhibitor Thiamet G	766:792	The goal of the current study was to confirm tau O-GlcNAcylation at S400 as a pharmacodynamic readout of OGA inhibition in P301S transgenic mice overexpressing human tau and treated with the OGA inhibitor Thiamet G and to explore if additional O-GlcNAcylation sites on tau could be identified.
36888912	5	1	theme	O-GlcNAcylated	1171:1184	arg1	tau					1192:1194	in-house produced recombinant O-GlcNAcylated human tau	1141:1194	in-house produced recombinant O-GlcNAcylated human tau	1141:1194	Second, additional O-GlcNAc sites were identified in in-house produced recombinant O-GlcNAcylated human tau at relatively high concentrations, thereby facilitating collection of informative LC-MS data for identification of low-concentration O-GlcNAc-tryptic tau peptides in human transgenic mouse BH extracts.
36888912	5	2	theme	low-concentration	1311:1327	arg1	peptides					1350:1357	low-concentration O-GlcNAc-tryptic tau peptides	1311:1357	low-concentration O-GlcNAc-tryptic tau peptides in human transgenic mouse BH extracts	1311:1395	Second, additional O-GlcNAc sites were identified in in-house produced recombinant O-GlcNAcylated human tau at relatively high concentrations, thereby facilitating collection of informative LC-MS data for identification of low-concentration O-GlcNAc-tryptic tau peptides in human transgenic mouse BH extracts.
36888912	5	3	from	extracts	1388:1395	arg1	identification					1293:1306	identification	1293:1306	identification of low-concentration O-GlcNAc-tryptic tau peptides in human transgenic mouse BH extracts	1293:1395	Second, additional O-GlcNAc sites were identified in in-house produced recombinant O-GlcNAcylated human tau at relatively high concentrations, thereby facilitating collection of informative LC-MS data for identification of low-concentration O-GlcNAc-tryptic tau peptides in human transgenic mouse BH extracts.
36888912	4	4	from	S400	1035:1038	arg1	extracts					1078:1085	mouse brain homogenate (BH) extracts	1050:1085	mouse brain homogenate (BH) extracts	1050:1085	As a first step, an immunoprecipitation-liquid chromatography-mass spectrometry (IP-LC-MS) methodology was developed to monitor changes in O-GlcNAcylation around S400 of tau in mouse brain homogenate (BH) extracts.
36888912	4	5	theme	immunoprecipitation-liquid	893:918	arg1	IP-LC-MS					954:961	IP-LC-MS	954:961	IP-LC-MS	954:961	As a first step, an immunoprecipitation-liquid chromatography-mass spectrometry (IP-LC-MS) methodology was developed to monitor changes in O-GlcNAcylation around S400 of tau in mouse brain homogenate (BH) extracts.
36888912	4	5	theme	immunoprecipitation-liquid	893:918	arg1	spectrometry					940:951	immunoprecipitation-liquid chromatography-mass spectrometry	893:951	an immunoprecipitation-liquid chromatography-mass spectrometry (IP-LC-MS) methodology	890:974	As a first step, an immunoprecipitation-liquid chromatography-mass spectrometry (IP-LC-MS) methodology was developed to monitor changes in O-GlcNAcylation around S400 of tau in mouse brain homogenate (BH) extracts.
36888912	3	6	theme	Thiamet	784:790	arg1	G					792:792	the OGA inhibitor Thiamet G	766:792	the OGA inhibitor Thiamet G	766:792	The goal of the current study was to confirm tau O-GlcNAcylation at S400 as a pharmacodynamic readout of OGA inhibition in P301S transgenic mice overexpressing human tau and treated with the OGA inhibitor Thiamet G and to explore if additional O-GlcNAcylation sites on tau could be identified.
36888912	5	7	from	identification	1293:1306	arg1	extracts					1388:1395	human transgenic mouse BH extracts	1362:1395	human transgenic mouse BH extracts	1362:1395	Second, additional O-GlcNAc sites were identified in in-house produced recombinant O-GlcNAcylated human tau at relatively high concentrations, thereby facilitating collection of informative LC-MS data for identification of low-concentration O-GlcNAc-tryptic tau peptides in human transgenic mouse BH extracts.
36888912	4	8	theme	spectrometry	940:951	arg1	step					884:887	a first step	876:887	a first step	876:887	As a first step, an immunoprecipitation-liquid chromatography-mass spectrometry (IP-LC-MS) methodology was developed to monitor changes in O-GlcNAcylation around S400 of tau in mouse brain homogenate (BH) extracts.
36888912	4	8	theme	spectrometry	940:951	arg1	methodology					964:974	an immunoprecipitation-liquid chromatography-mass spectrometry (IP-LC-MS) methodology	890:974	an immunoprecipitation-liquid chromatography-mass spectrometry (IP-LC-MS) methodology	890:974	As a first step, an immunoprecipitation-liquid chromatography-mass spectrometry (IP-LC-MS) methodology was developed to monitor changes in O-GlcNAcylation around S400 of tau in mouse brain homogenate (BH) extracts.
36888912	3	9	theme	additional	812:821	arg1	sites					839:843	additional O-GlcNAcylation sites	812:843	additional O-GlcNAcylation sites on tau	812:850	The goal of the current study was to confirm tau O-GlcNAcylation at S400 as a pharmacodynamic readout of OGA inhibition in P301S transgenic mice overexpressing human tau and treated with the OGA inhibitor Thiamet G and to explore if additional O-GlcNAcylation sites on tau could be identified.
36888912	5	10	theme	in-house	1141:1148	arg1	tau					1192:1194	in-house produced recombinant O-GlcNAcylated human tau	1141:1194	in-house produced recombinant O-GlcNAcylated human tau	1141:1194	Second, additional O-GlcNAc sites were identified in in-house produced recombinant O-GlcNAcylated human tau at relatively high concentrations, thereby facilitating collection of informative LC-MS data for identification of low-concentration O-GlcNAc-tryptic tau peptides in human transgenic mouse BH extracts.
36888912	5	11	theme	recombinant	1159:1169	arg1	tau					1192:1194	in-house produced recombinant O-GlcNAcylated human tau	1141:1194	in-house produced recombinant O-GlcNAcylated human tau	1141:1194	Second, additional O-GlcNAc sites were identified in in-house produced recombinant O-GlcNAcylated human tau at relatively high concentrations, thereby facilitating collection of informative LC-MS data for identification of low-concentration O-GlcNAc-tryptic tau peptides in human transgenic mouse BH extracts.
36888912	6	12	theme	first	1429:1433	arg1	time					1435:1438	the first time	1425:1438	the first time	1425:1438	This strategy enabled, for the first time, identification of three low abundant N-terminal and mid-domain O-GlcNAc sites of tau (at S208, S191, and S184 or S185) in human transgenic mouse BH.
36888912	7	13	dep	doi	1638:1640	arg1	doi					1666:1668	doi	1666:1668	doi: 10.17632/jp57yk9469.1; doi: 10.17632/8n5j45dnd8.1; doi: 10.17632/h5vdrx4n3d.1	1638:1719	Data are openly available at data.mendeley.com (doi: 10.17632/jp57yk9469.1; doi: 10.17632/8n5j45dnd8.1; doi: 10.17632/h5vdrx4n3d.1).
36888912	7	13	dep	doi	1638:1640	arg1	10.17632/jp57yk9469.1					1643:1663	10.17632/jp57yk9469.1	1643:1663	10.17632/jp57yk9469.1	1643:1663	Data are openly available at data.mendeley.com (doi: 10.17632/jp57yk9469.1; doi: 10.17632/8n5j45dnd8.1; doi: 10.17632/h5vdrx4n3d.1).
36888912	7	13	dep	doi	1638:1640	arg1	10.17632/h5vdrx4n3d.1					1699:1719	10.17632/h5vdrx4n3d.1	1699:1719	10.17632/h5vdrx4n3d.1	1699:1719	Data are openly available at data.mendeley.com (doi: 10.17632/jp57yk9469.1; doi: 10.17632/8n5j45dnd8.1; doi: 10.17632/h5vdrx4n3d.1).
36888912	7	13	dep	doi	1638:1640	arg1	doi					1694:1696	doi	1694:1696	doi: 10.17632/jp57yk9469.1; doi: 10.17632/8n5j45dnd8.1; doi: 10.17632/h5vdrx4n3d.1	1638:1719	Data are openly available at data.mendeley.com (doi: 10.17632/jp57yk9469.1; doi: 10.17632/8n5j45dnd8.1; doi: 10.17632/h5vdrx4n3d.1).
36888912	7	13	dep	doi	1638:1640	arg1	10.17632/8n5j45dnd8.1					1671:1691	10.17632/8n5j45dnd8.1	1671:1691	10.17632/8n5j45dnd8.1	1671:1691	Data are openly available at data.mendeley.com (doi: 10.17632/jp57yk9469.1; doi: 10.17632/8n5j45dnd8.1; doi: 10.17632/h5vdrx4n3d.1).
36888912	2	14	used	used	501:504	arg2	Analysis					448:455	Analysis	448:455	Analysis of tau O-GlcNAcylation	448:478	Analysis of tau O-GlcNAcylation could potentially be used as a pharmacodynamic biomarker both in preclinical and clinical studies.
36888912	2	14	used	used	501:504	arg2	biomarker					527:535	a pharmacodynamic biomarker	509:535	a pharmacodynamic biomarker	509:535	Analysis of tau O-GlcNAcylation could potentially be used as a pharmacodynamic biomarker both in preclinical and clinical studies.
36888912	6	15	from	S208	1530:1533	arg1	tau					1522:1524	tau	1522:1524	tau (at S208, S191, and S184 or S185) in human transgenic mouse BH	1522:1587	This strategy enabled, for the first time, identification of three low abundant N-terminal and mid-domain O-GlcNAc sites of tau (at S208, S191, and S184 or S185) in human transgenic mouse BH.
36888912	6	15	from	S208	1530:1533	arg1	sites					1513:1517	abundant N-terminal and mid-domain O-GlcNAc sites	1469:1517	three low abundant N-terminal and mid-domain O-GlcNAc sites of tau (at S208, S191, and S184 or S185) in human transgenic mouse BH	1459:1587	This strategy enabled, for the first time, identification of three low abundant N-terminal and mid-domain O-GlcNAc sites of tau (at S208, S191, and S184 or S185) in human transgenic mouse BH.
36888912	4	16	theme	brain	1056:1060	arg1	extracts					1078:1085	mouse brain homogenate (BH) extracts	1050:1085	mouse brain homogenate (BH) extracts	1050:1085	As a first step, an immunoprecipitation-liquid chromatography-mass spectrometry (IP-LC-MS) methodology was developed to monitor changes in O-GlcNAcylation around S400 of tau in mouse brain homogenate (BH) extracts.
36888912	0	17	from	Readout	111:117	arg1	Mice					133:136	Transgenic Mice	122:136	Transgenic Mice Overexpressing Human Tau	122:161	IP-LC-MSMS Enables Identification of Three Tau O-GlcNAcylation Sites as O-GlcNAcase Inhibition Pharmacodynamic Readout in Transgenic Mice Overexpressing Human Tau.
36888912	6	18	theme	sites	1513:1517	arg1	identification					1441:1454	identification	1441:1454	identification of three low abundant N-terminal and mid-domain O-GlcNAc sites of tau (at S208, S191, and S184 or S185) in human transgenic mouse BH	1441:1587	This strategy enabled, for the first time, identification of three low abundant N-terminal and mid-domain O-GlcNAc sites of tau (at S208, S191, and S184 or S185) in human transgenic mouse BH.
36888912	5	19	theme	high	1210:1213	arg1	concentrations					1215:1228	relatively high concentrations	1199:1228	relatively high concentrations	1199:1228	Second, additional O-GlcNAc sites were identified in in-house produced recombinant O-GlcNAcylated human tau at relatively high concentrations, thereby facilitating collection of informative LC-MS data for identification of low-concentration O-GlcNAc-tryptic tau peptides in human transgenic mouse BH extracts.
36888912	3	20	theme	OGA	684:686	arg1	inhibition					688:697	OGA inhibition	684:697	OGA inhibition	684:697	The goal of the current study was to confirm tau O-GlcNAcylation at S400 as a pharmacodynamic readout of OGA inhibition in P301S transgenic mice overexpressing human tau and treated with the OGA inhibitor Thiamet G and to explore if additional O-GlcNAcylation sites on tau could be identified.
36888912	3	21	from	sites	839:843	arg1	tau					848:850	tau	848:850	tau	848:850	The goal of the current study was to confirm tau O-GlcNAcylation at S400 as a pharmacodynamic readout of OGA inhibition in P301S transgenic mice overexpressing human tau and treated with the OGA inhibitor Thiamet G and to explore if additional O-GlcNAcylation sites on tau could be identified.
36888912	5	22	theme	BH	1385:1386	arg1	extracts					1388:1395	human transgenic mouse BH extracts	1362:1395	human transgenic mouse BH extracts	1362:1395	Second, additional O-GlcNAc sites were identified in in-house produced recombinant O-GlcNAcylated human tau at relatively high concentrations, thereby facilitating collection of informative LC-MS data for identification of low-concentration O-GlcNAc-tryptic tau peptides in human transgenic mouse BH extracts.
36888912	0	23	theme	Inhibition	84:93	arg1	Readout					111:117	O-GlcNAcase Inhibition Pharmacodynamic Readout	72:117	O-GlcNAcase Inhibition Pharmacodynamic Readout in Transgenic Mice Overexpressing Human Tau	72:161	IP-LC-MSMS Enables Identification of Three Tau O-GlcNAcylation Sites as O-GlcNAcase Inhibition Pharmacodynamic Readout in Transgenic Mice Overexpressing Human Tau.
36888912	6	24	theme	N-terminal	1478:1487	arg1	tau					1522:1524	tau	1522:1524	tau (at S208, S191, and S184 or S185) in human transgenic mouse BH	1522:1587	This strategy enabled, for the first time, identification of three low abundant N-terminal and mid-domain O-GlcNAc sites of tau (at S208, S191, and S184 or S185) in human transgenic mouse BH.
36888912	6	24	theme	N-terminal	1478:1487	arg1	sites					1513:1517	abundant N-terminal and mid-domain O-GlcNAc sites	1469:1517	three low abundant N-terminal and mid-domain O-GlcNAc sites of tau (at S208, S191, and S184 or S185) in human transgenic mouse BH	1459:1587	This strategy enabled, for the first time, identification of three low abundant N-terminal and mid-domain O-GlcNAc sites of tau (at S208, S191, and S184 or S185) in human transgenic mouse BH.
36888912	5	25	theme	human	1186:1190	arg1	tau					1192:1194	in-house produced recombinant O-GlcNAcylated human tau	1141:1194	in-house produced recombinant O-GlcNAcylated human tau	1141:1194	Second, additional O-GlcNAc sites were identified in in-house produced recombinant O-GlcNAcylated human tau at relatively high concentrations, thereby facilitating collection of informative LC-MS data for identification of low-concentration O-GlcNAc-tryptic tau peptides in human transgenic mouse BH extracts.
36888912	2	26	theme	O-GlcNAcylation	464:478	arg1	Analysis					448:455	Analysis	448:455	Analysis of tau O-GlcNAcylation	448:478	Analysis of tau O-GlcNAcylation could potentially be used as a pharmacodynamic biomarker both in preclinical and clinical studies.
36888912	2	26	theme	O-GlcNAcylation	464:478	arg1	biomarker					527:535	a pharmacodynamic biomarker	509:535	a pharmacodynamic biomarker	509:535	Analysis of tau O-GlcNAcylation could potentially be used as a pharmacodynamic biomarker both in preclinical and clinical studies.
36888912	5	27	theme	tau	1346:1348	arg1	peptides					1350:1357	low-concentration O-GlcNAc-tryptic tau peptides	1311:1357	low-concentration O-GlcNAc-tryptic tau peptides in human transgenic mouse BH extracts	1311:1395	Second, additional O-GlcNAc sites were identified in in-house produced recombinant O-GlcNAcylated human tau at relatively high concentrations, thereby facilitating collection of informative LC-MS data for identification of low-concentration O-GlcNAc-tryptic tau peptides in human transgenic mouse BH extracts.
36888912	5	28	theme	LC-MS	1278:1282	arg1	data					1284:1287	informative LC-MS data	1266:1287	informative LC-MS data	1266:1287	Second, additional O-GlcNAc sites were identified in in-house produced recombinant O-GlcNAcylated human tau at relatively high concentrations, thereby facilitating collection of informative LC-MS data for identification of low-concentration O-GlcNAc-tryptic tau peptides in human transgenic mouse BH extracts.
36888912	6	29	from	BH	1586:1587	arg1	tau					1522:1524	tau	1522:1524	tau (at S208, S191, and S184 or S185) in human transgenic mouse BH	1522:1587	This strategy enabled, for the first time, identification of three low abundant N-terminal and mid-domain O-GlcNAc sites of tau (at S208, S191, and S184 or S185) in human transgenic mouse BH.
36888912	6	29	from	BH	1586:1587	arg1	sites					1513:1517	abundant N-terminal and mid-domain O-GlcNAc sites	1469:1517	three low abundant N-terminal and mid-domain O-GlcNAc sites of tau (at S208, S191, and S184 or S185) in human transgenic mouse BH	1459:1587	This strategy enabled, for the first time, identification of three low abundant N-terminal and mid-domain O-GlcNAc sites of tau (at S208, S191, and S184 or S185) in human transgenic mouse BH.
36888912	6	30	theme	mid-domain	1493:1502	arg1	tau					1522:1524	tau	1522:1524	tau (at S208, S191, and S184 or S185) in human transgenic mouse BH	1522:1587	This strategy enabled, for the first time, identification of three low abundant N-terminal and mid-domain O-GlcNAc sites of tau (at S208, S191, and S184 or S185) in human transgenic mouse BH.
36888912	6	30	theme	mid-domain	1493:1502	arg1	sites					1513:1517	abundant N-terminal and mid-domain O-GlcNAc sites	1469:1517	three low abundant N-terminal and mid-domain O-GlcNAc sites of tau (at S208, S191, and S184 or S185) in human transgenic mouse BH	1459:1587	This strategy enabled, for the first time, identification of three low abundant N-terminal and mid-domain O-GlcNAc sites of tau (at S208, S191, and S184 or S185) in human transgenic mouse BH.
36888912	1	31	theme	O-GlcNAc	352:359	arg1	OGA					372:374	OGA	372:374	OGA	372:374	O-β-linked N-acetylglucosaminylation (O-GlcNAcylation) modulates tau phosphorylation and aggregation: the pharmacological increase of tau O-GlcNAcylation upon treatment with inhibitors of O-GlcNAc hydrolase (OGA) constitutes a potential strategy to tackle neurodegenerative diseases.
36888912	1	31	theme	O-GlcNAc	352:359	arg1	hydrolase					361:369	O-GlcNAc hydrolase	352:369	O-GlcNAc hydrolase (OGA)	352:375	O-β-linked N-acetylglucosaminylation (O-GlcNAcylation) modulates tau phosphorylation and aggregation: the pharmacological increase of tau O-GlcNAcylation upon treatment with inhibitors of O-GlcNAc hydrolase (OGA) constitutes a potential strategy to tackle neurodegenerative diseases.
36888912	1	32	link	O-β-linked	164:173	arg1	N-acetylglucosaminylation					175:199	O-β-linked N-acetylglucosaminylation	164:199	O-β-linked N-acetylglucosaminylation (O-GlcNAcylation)	164:217	O-β-linked N-acetylglucosaminylation (O-GlcNAcylation) modulates tau phosphorylation and aggregation: the pharmacological increase of tau O-GlcNAcylation upon treatment with inhibitors of O-GlcNAc hydrolase (OGA) constitutes a potential strategy to tackle neurodegenerative diseases.
36888912	1	32	link	O-β-linked	164:173	arg1	O-GlcNAcylation					202:216	O-GlcNAcylation	202:216	O-GlcNAcylation	202:216	O-β-linked N-acetylglucosaminylation (O-GlcNAcylation) modulates tau phosphorylation and aggregation: the pharmacological increase of tau O-GlcNAcylation upon treatment with inhibitors of O-GlcNAc hydrolase (OGA) constitutes a potential strategy to tackle neurodegenerative diseases.
36888912	4	33	theme	first	878:882	arg1	step					884:887	a first step	876:887	a first step	876:887	As a first step, an immunoprecipitation-liquid chromatography-mass spectrometry (IP-LC-MS) methodology was developed to monitor changes in O-GlcNAcylation around S400 of tau in mouse brain homogenate (BH) extracts.
36888912	4	33	theme	first	878:882	arg1	methodology					964:974	an immunoprecipitation-liquid chromatography-mass spectrometry (IP-LC-MS) methodology	890:974	an immunoprecipitation-liquid chromatography-mass spectrometry (IP-LC-MS) methodology	890:974	As a first step, an immunoprecipitation-liquid chromatography-mass spectrometry (IP-LC-MS) methodology was developed to monitor changes in O-GlcNAcylation around S400 of tau in mouse brain homogenate (BH) extracts.
36888912	3	34	from	readout	673:679	arg1	mice					719:722	P301S transgenic mice	702:722	P301S transgenic mice overexpressing human tau and treated with the OGA inhibitor Thiamet G	702:792	The goal of the current study was to confirm tau O-GlcNAcylation at S400 as a pharmacodynamic readout of OGA inhibition in P301S transgenic mice overexpressing human tau and treated with the OGA inhibitor Thiamet G and to explore if additional O-GlcNAcylation sites on tau could be identified.
36888912	4	35	theme	BH	1074:1075	arg1	extracts					1078:1085	mouse brain homogenate (BH) extracts	1050:1085	mouse brain homogenate (BH) extracts	1050:1085	As a first step, an immunoprecipitation-liquid chromatography-mass spectrometry (IP-LC-MS) methodology was developed to monitor changes in O-GlcNAcylation around S400 of tau in mouse brain homogenate (BH) extracts.
36888912	1	36	with	treatment	323:331	arg1	inhibitors					338:347	inhibitors	338:347	inhibitors of O-GlcNAc hydrolase (OGA)	338:375	O-β-linked N-acetylglucosaminylation (O-GlcNAcylation) modulates tau phosphorylation and aggregation: the pharmacological increase of tau O-GlcNAcylation upon treatment with inhibitors of O-GlcNAc hydrolase (OGA) constitutes a potential strategy to tackle neurodegenerative diseases.
36888912	7	37	from	data.mendeley.com	1619:1635	arg1	available					1606:1614	available	1606:1614	available	1606:1614	Data are openly available at data.mendeley.com (doi: 10.17632/jp57yk9469.1; doi: 10.17632/8n5j45dnd8.1; doi: 10.17632/h5vdrx4n3d.1).
36888912	3	38	theme	transgenic	708:717	arg1	mice					719:722	P301S transgenic mice	702:722	P301S transgenic mice overexpressing human tau and treated with the OGA inhibitor Thiamet G	702:792	The goal of the current study was to confirm tau O-GlcNAcylation at S400 as a pharmacodynamic readout of OGA inhibition in P301S transgenic mice overexpressing human tau and treated with the OGA inhibitor Thiamet G and to explore if additional O-GlcNAcylation sites on tau could be identified.
36888912	6	39	theme	tau	1522:1524	arg1	tau					1522:1524	tau	1522:1524	tau (at S208, S191, and S184 or S185) in human transgenic mouse BH	1522:1587	This strategy enabled, for the first time, identification of three low abundant N-terminal and mid-domain O-GlcNAc sites of tau (at S208, S191, and S184 or S185) in human transgenic mouse BH.
36888912	6	39	theme	tau	1522:1524	arg1	sites					1513:1517	abundant N-terminal and mid-domain O-GlcNAc sites	1469:1517	three low abundant N-terminal and mid-domain O-GlcNAc sites of tau (at S208, S191, and S184 or S185) in human transgenic mouse BH	1459:1587	This strategy enabled, for the first time, identification of three low abundant N-terminal and mid-domain O-GlcNAc sites of tau (at S208, S191, and S184 or S185) in human transgenic mouse BH.
36888912	5	40	theme	O-GlcNAc	1107:1114	arg1	sites					1116:1120	additional O-GlcNAc sites	1096:1120	additional O-GlcNAc sites	1096:1120	Second, additional O-GlcNAc sites were identified in in-house produced recombinant O-GlcNAcylated human tau at relatively high concentrations, thereby facilitating collection of informative LC-MS data for identification of low-concentration O-GlcNAc-tryptic tau peptides in human transgenic mouse BH extracts.
36888912	6	41	theme	transgenic	1569:1578	arg1	BH					1586:1587	human transgenic mouse BH	1563:1587	human transgenic mouse BH	1563:1587	This strategy enabled, for the first time, identification of three low abundant N-terminal and mid-domain O-GlcNAc sites of tau (at S208, S191, and S184 or S185) in human transgenic mouse BH.
36888912	5	42	theme	peptides	1350:1357	arg1	identification					1293:1306	identification	1293:1306	identification of low-concentration O-GlcNAc-tryptic tau peptides in human transgenic mouse BH extracts	1293:1395	Second, additional O-GlcNAc sites were identified in in-house produced recombinant O-GlcNAcylated human tau at relatively high concentrations, thereby facilitating collection of informative LC-MS data for identification of low-concentration O-GlcNAc-tryptic tau peptides in human transgenic mouse BH extracts.
36888912	6	43	from	S184	1546:1549	arg1	tau					1522:1524	tau	1522:1524	tau (at S208, S191, and S184 or S185) in human transgenic mouse BH	1522:1587	This strategy enabled, for the first time, identification of three low abundant N-terminal and mid-domain O-GlcNAc sites of tau (at S208, S191, and S184 or S185) in human transgenic mouse BH.
36888912	6	43	from	S184	1546:1549	arg1	sites					1513:1517	abundant N-terminal and mid-domain O-GlcNAc sites	1469:1517	three low abundant N-terminal and mid-domain O-GlcNAc sites of tau (at S208, S191, and S184 or S185) in human transgenic mouse BH	1459:1587	This strategy enabled, for the first time, identification of three low abundant N-terminal and mid-domain O-GlcNAc sites of tau (at S208, S191, and S184 or S185) in human transgenic mouse BH.
36888912	5	44	theme	human	1362:1366	arg1	extracts					1388:1395	human transgenic mouse BH extracts	1362:1395	human transgenic mouse BH extracts	1362:1395	Second, additional O-GlcNAc sites were identified in in-house produced recombinant O-GlcNAcylated human tau at relatively high concentrations, thereby facilitating collection of informative LC-MS data for identification of low-concentration O-GlcNAc-tryptic tau peptides in human transgenic mouse BH extracts.
36888912	6	45	from	S185	1554:1557	arg1	tau					1522:1524	tau	1522:1524	tau (at S208, S191, and S184 or S185) in human transgenic mouse BH	1522:1587	This strategy enabled, for the first time, identification of three low abundant N-terminal and mid-domain O-GlcNAc sites of tau (at S208, S191, and S184 or S185) in human transgenic mouse BH.
36888912	6	45	from	S185	1554:1557	arg1	sites					1513:1517	abundant N-terminal and mid-domain O-GlcNAc sites	1469:1517	three low abundant N-terminal and mid-domain O-GlcNAc sites of tau (at S208, S191, and S184 or S185) in human transgenic mouse BH	1459:1587	This strategy enabled, for the first time, identification of three low abundant N-terminal and mid-domain O-GlcNAc sites of tau (at S208, S191, and S184 or S185) in human transgenic mouse BH.
36888912	6	46	theme	O-GlcNAc	1504:1511	arg1	tau					1522:1524	tau	1522:1524	tau (at S208, S191, and S184 or S185) in human transgenic mouse BH	1522:1587	This strategy enabled, for the first time, identification of three low abundant N-terminal and mid-domain O-GlcNAc sites of tau (at S208, S191, and S184 or S185) in human transgenic mouse BH.
36888912	6	46	theme	O-GlcNAc	1504:1511	arg1	sites					1513:1517	abundant N-terminal and mid-domain O-GlcNAc sites	1469:1517	three low abundant N-terminal and mid-domain O-GlcNAc sites of tau (at S208, S191, and S184 or S185) in human transgenic mouse BH	1459:1587	This strategy enabled, for the first time, identification of three low abundant N-terminal and mid-domain O-GlcNAc sites of tau (at S208, S191, and S184 or S185) in human transgenic mouse BH.
36888912	1	47	theme	O-GlcNAcylation	302:316	arg1	increase					286:293	the pharmacological increase	266:293	the pharmacological increase of tau O-GlcNAcylation upon treatment with inhibitors of O-GlcNAc hydrolase (OGA)	266:375	O-β-linked N-acetylglucosaminylation (O-GlcNAcylation) modulates tau phosphorylation and aggregation: the pharmacological increase of tau O-GlcNAcylation upon treatment with inhibitors of O-GlcNAc hydrolase (OGA) constitutes a potential strategy to tackle neurodegenerative diseases.
36888912	5	48	theme	O-GlcNAc-tryptic	1329:1344	arg1	peptides					1350:1357	low-concentration O-GlcNAc-tryptic tau peptides	1311:1357	low-concentration O-GlcNAc-tryptic tau peptides in human transgenic mouse BH extracts	1311:1395	Second, additional O-GlcNAc sites were identified in in-house produced recombinant O-GlcNAcylated human tau at relatively high concentrations, thereby facilitating collection of informative LC-MS data for identification of low-concentration O-GlcNAc-tryptic tau peptides in human transgenic mouse BH extracts.
36888912	3	49	theme	study	603:607	arg1	goal					583:586	The goal	579:586	The goal of the current study	579:607	The goal of the current study was to confirm tau O-GlcNAcylation at S400 as a pharmacodynamic readout of OGA inhibition in P301S transgenic mice overexpressing human tau and treated with the OGA inhibitor Thiamet G and to explore if additional O-GlcNAcylation sites on tau could be identified.
36888912	0	50	theme	O-GlcNAcylation	47:61	arg1	Sites					63:67	Three Tau O-GlcNAcylation Sites	37:67	Three Tau O-GlcNAcylation Sites	37:67	IP-LC-MSMS Enables Identification of Three Tau O-GlcNAcylation Sites as O-GlcNAcase Inhibition Pharmacodynamic Readout in Transgenic Mice Overexpressing Human Tau.
36888912	6	51	theme	low	1465:1467	arg1	tau					1522:1524	tau	1522:1524	tau (at S208, S191, and S184 or S185) in human transgenic mouse BH	1522:1587	This strategy enabled, for the first time, identification of three low abundant N-terminal and mid-domain O-GlcNAc sites of tau (at S208, S191, and S184 or S185) in human transgenic mouse BH.
36888912	6	51	theme	low	1465:1467	arg1	sites					1513:1517	abundant N-terminal and mid-domain O-GlcNAc sites	1469:1517	three low abundant N-terminal and mid-domain O-GlcNAc sites of tau (at S208, S191, and S184 or S185) in human transgenic mouse BH	1459:1587	This strategy enabled, for the first time, identification of three low abundant N-terminal and mid-domain O-GlcNAc sites of tau (at S208, S191, and S184 or S185) in human transgenic mouse BH.
36888912	2	52	theme	clinical	561:568	arg1	studies					570:576	preclinical and clinical studies	545:576	preclinical and clinical studies	545:576	Analysis of tau O-GlcNAcylation could potentially be used as a pharmacodynamic biomarker both in preclinical and clinical studies.
36888912	1	53	theme	tau	229:231	arg1	phosphorylation					233:247	tau phosphorylation	229:247	tau phosphorylation	229:247	O-β-linked N-acetylglucosaminylation (O-GlcNAcylation) modulates tau phosphorylation and aggregation: the pharmacological increase of tau O-GlcNAcylation upon treatment with inhibitors of O-GlcNAc hydrolase (OGA) constitutes a potential strategy to tackle neurodegenerative diseases.
36888912	4	54	theme	chromatography-mass	920:938	arg1	IP-LC-MS					954:961	IP-LC-MS	954:961	IP-LC-MS	954:961	As a first step, an immunoprecipitation-liquid chromatography-mass spectrometry (IP-LC-MS) methodology was developed to monitor changes in O-GlcNAcylation around S400 of tau in mouse brain homogenate (BH) extracts.
36888912	4	54	theme	chromatography-mass	920:938	arg1	spectrometry					940:951	immunoprecipitation-liquid chromatography-mass spectrometry	893:951	an immunoprecipitation-liquid chromatography-mass spectrometry (IP-LC-MS) methodology	890:974	As a first step, an immunoprecipitation-liquid chromatography-mass spectrometry (IP-LC-MS) methodology was developed to monitor changes in O-GlcNAcylation around S400 of tau in mouse brain homogenate (BH) extracts.
36888912	3	55	theme	O-GlcNAcylation	823:837	arg1	sites					839:843	additional O-GlcNAcylation sites	812:843	additional O-GlcNAcylation sites on tau	812:850	The goal of the current study was to confirm tau O-GlcNAcylation at S400 as a pharmacodynamic readout of OGA inhibition in P301S transgenic mice overexpressing human tau and treated with the OGA inhibitor Thiamet G and to explore if additional O-GlcNAcylation sites on tau could be identified.
36888912	0	56	theme	Human	153:157	arg1	Tau					159:161	Human Tau	153:161	Human Tau	153:161	IP-LC-MSMS Enables Identification of Three Tau O-GlcNAcylation Sites as O-GlcNAcase Inhibition Pharmacodynamic Readout in Transgenic Mice Overexpressing Human Tau.
36888912	3	57	theme	tau	624:626	arg1	O-GlcNAcylation					628:642	tau O-GlcNAcylation	624:642	tau O-GlcNAcylation	624:642	The goal of the current study was to confirm tau O-GlcNAcylation at S400 as a pharmacodynamic readout of OGA inhibition in P301S transgenic mice overexpressing human tau and treated with the OGA inhibitor Thiamet G and to explore if additional O-GlcNAcylation sites on tau could be identified.
36888912	3	57	theme	tau	624:626	arg1	readout					673:679	a pharmacodynamic readout	655:679	a pharmacodynamic readout of OGA inhibition in P301S transgenic mice overexpressing human tau and treated with the OGA inhibitor Thiamet G	655:792	The goal of the current study was to confirm tau O-GlcNAcylation at S400 as a pharmacodynamic readout of OGA inhibition in P301S transgenic mice overexpressing human tau and treated with the OGA inhibitor Thiamet G and to explore if additional O-GlcNAcylation sites on tau could be identified.
36888912	5	58	theme	produced	1150:1157	arg1	tau					1192:1194	in-house produced recombinant O-GlcNAcylated human tau	1141:1194	in-house produced recombinant O-GlcNAcylated human tau	1141:1194	Second, additional O-GlcNAc sites were identified in in-house produced recombinant O-GlcNAcylated human tau at relatively high concentrations, thereby facilitating collection of informative LC-MS data for identification of low-concentration O-GlcNAc-tryptic tau peptides in human transgenic mouse BH extracts.
36888912	3	59	theme	pharmacodynamic	657:671	arg1	O-GlcNAcylation					628:642	tau O-GlcNAcylation	624:642	tau O-GlcNAcylation	624:642	The goal of the current study was to confirm tau O-GlcNAcylation at S400 as a pharmacodynamic readout of OGA inhibition in P301S transgenic mice overexpressing human tau and treated with the OGA inhibitor Thiamet G and to explore if additional O-GlcNAcylation sites on tau could be identified.
36888912	3	59	theme	pharmacodynamic	657:671	arg1	readout					673:679	a pharmacodynamic readout	655:679	a pharmacodynamic readout of OGA inhibition in P301S transgenic mice overexpressing human tau and treated with the OGA inhibitor Thiamet G	655:792	The goal of the current study was to confirm tau O-GlcNAcylation at S400 as a pharmacodynamic readout of OGA inhibition in P301S transgenic mice overexpressing human tau and treated with the OGA inhibitor Thiamet G and to explore if additional O-GlcNAcylation sites on tau could be identified.
36888912	4	60	from	changes	1001:1007	arg1	O-GlcNAcylation					1012:1026	O-GlcNAcylation	1012:1026	O-GlcNAcylation	1012:1026	As a first step, an immunoprecipitation-liquid chromatography-mass spectrometry (IP-LC-MS) methodology was developed to monitor changes in O-GlcNAcylation around S400 of tau in mouse brain homogenate (BH) extracts.
36888912	5	61	from	peptides	1350:1357	arg1	extracts					1388:1395	human transgenic mouse BH extracts	1362:1395	human transgenic mouse BH extracts	1362:1395	Second, additional O-GlcNAc sites were identified in in-house produced recombinant O-GlcNAcylated human tau at relatively high concentrations, thereby facilitating collection of informative LC-MS data for identification of low-concentration O-GlcNAc-tryptic tau peptides in human transgenic mouse BH extracts.
36888912	6	62	from	tau	1522:1524	arg1	BH					1586:1587	human transgenic mouse BH	1563:1587	human transgenic mouse BH	1563:1587	This strategy enabled, for the first time, identification of three low abundant N-terminal and mid-domain O-GlcNAc sites of tau (at S208, S191, and S184 or S185) in human transgenic mouse BH.
36888912	3	63	theme	inhibition	688:697	arg1	O-GlcNAcylation					628:642	tau O-GlcNAcylation	624:642	tau O-GlcNAcylation	624:642	The goal of the current study was to confirm tau O-GlcNAcylation at S400 as a pharmacodynamic readout of OGA inhibition in P301S transgenic mice overexpressing human tau and treated with the OGA inhibitor Thiamet G and to explore if additional O-GlcNAcylation sites on tau could be identified.
36888912	3	63	theme	inhibition	688:697	arg1	readout					673:679	a pharmacodynamic readout	655:679	a pharmacodynamic readout of OGA inhibition in P301S transgenic mice overexpressing human tau and treated with the OGA inhibitor Thiamet G	655:792	The goal of the current study was to confirm tau O-GlcNAcylation at S400 as a pharmacodynamic readout of OGA inhibition in P301S transgenic mice overexpressing human tau and treated with the OGA inhibitor Thiamet G and to explore if additional O-GlcNAcylation sites on tau could be identified.
36888912	0	64	theme	O-GlcNAcase	72:82	arg1	Readout					111:117	O-GlcNAcase Inhibition Pharmacodynamic Readout	72:117	O-GlcNAcase Inhibition Pharmacodynamic Readout in Transgenic Mice Overexpressing Human Tau	72:161	IP-LC-MSMS Enables Identification of Three Tau O-GlcNAcylation Sites as O-GlcNAcase Inhibition Pharmacodynamic Readout in Transgenic Mice Overexpressing Human Tau.
36888912	1	65	theme	O-β-linked	164:173	arg1	N-acetylglucosaminylation					175:199	O-β-linked N-acetylglucosaminylation	164:199	O-β-linked N-acetylglucosaminylation (O-GlcNAcylation)	164:217	O-β-linked N-acetylglucosaminylation (O-GlcNAcylation) modulates tau phosphorylation and aggregation: the pharmacological increase of tau O-GlcNAcylation upon treatment with inhibitors of O-GlcNAc hydrolase (OGA) constitutes a potential strategy to tackle neurodegenerative diseases.
36888912	1	65	theme	O-β-linked	164:173	arg1	O-GlcNAcylation					202:216	O-GlcNAcylation	202:216	O-GlcNAcylation	202:216	O-β-linked N-acetylglucosaminylation (O-GlcNAcylation) modulates tau phosphorylation and aggregation: the pharmacological increase of tau O-GlcNAcylation upon treatment with inhibitors of O-GlcNAc hydrolase (OGA) constitutes a potential strategy to tackle neurodegenerative diseases.
36888912	4	66	theme	mouse	1050:1054	arg1	extracts					1078:1085	mouse brain homogenate (BH) extracts	1050:1085	mouse brain homogenate (BH) extracts	1050:1085	As a first step, an immunoprecipitation-liquid chromatography-mass spectrometry (IP-LC-MS) methodology was developed to monitor changes in O-GlcNAcylation around S400 of tau in mouse brain homogenate (BH) extracts.
36888912	1	67	theme	pharmacological	270:284	arg1	increase					286:293	the pharmacological increase	266:293	the pharmacological increase of tau O-GlcNAcylation upon treatment with inhibitors of O-GlcNAc hydrolase (OGA)	266:375	O-β-linked N-acetylglucosaminylation (O-GlcNAcylation) modulates tau phosphorylation and aggregation: the pharmacological increase of tau O-GlcNAcylation upon treatment with inhibitors of O-GlcNAc hydrolase (OGA) constitutes a potential strategy to tackle neurodegenerative diseases.
36888912	5	68	theme	mouse	1379:1383	arg1	extracts					1388:1395	human transgenic mouse BH extracts	1362:1395	human transgenic mouse BH extracts	1362:1395	Second, additional O-GlcNAc sites were identified in in-house produced recombinant O-GlcNAcylated human tau at relatively high concentrations, thereby facilitating collection of informative LC-MS data for identification of low-concentration O-GlcNAc-tryptic tau peptides in human transgenic mouse BH extracts.
36888912	0	69	theme	Pharmacodynamic	95:109	arg1	Readout					111:117	O-GlcNAcase Inhibition Pharmacodynamic Readout	72:117	O-GlcNAcase Inhibition Pharmacodynamic Readout in Transgenic Mice Overexpressing Human Tau	72:161	IP-LC-MSMS Enables Identification of Three Tau O-GlcNAcylation Sites as O-GlcNAcase Inhibition Pharmacodynamic Readout in Transgenic Mice Overexpressing Human Tau.
36888912	1	70	theme	potential	391:399	arg1	strategy					401:408	a potential strategy	389:408	a potential strategy to tackle neurodegenerative diseases	389:445	O-β-linked N-acetylglucosaminylation (O-GlcNAcylation) modulates tau phosphorylation and aggregation: the pharmacological increase of tau O-GlcNAcylation upon treatment with inhibitors of O-GlcNAc hydrolase (OGA) constitutes a potential strategy to tackle neurodegenerative diseases.
36888912	4	71	theme	homogenate	1062:1071	arg1	extracts					1078:1085	mouse brain homogenate (BH) extracts	1050:1085	mouse brain homogenate (BH) extracts	1050:1085	As a first step, an immunoprecipitation-liquid chromatography-mass spectrometry (IP-LC-MS) methodology was developed to monitor changes in O-GlcNAcylation around S400 of tau in mouse brain homogenate (BH) extracts.
36888912	6	72	from	S191	1536:1539	arg1	tau					1522:1524	tau	1522:1524	tau (at S208, S191, and S184 or S185) in human transgenic mouse BH	1522:1587	This strategy enabled, for the first time, identification of three low abundant N-terminal and mid-domain O-GlcNAc sites of tau (at S208, S191, and S184 or S185) in human transgenic mouse BH.
36888912	6	72	from	S191	1536:1539	arg1	sites					1513:1517	abundant N-terminal and mid-domain O-GlcNAc sites	1469:1517	three low abundant N-terminal and mid-domain O-GlcNAc sites of tau (at S208, S191, and S184 or S185) in human transgenic mouse BH	1459:1587	This strategy enabled, for the first time, identification of three low abundant N-terminal and mid-domain O-GlcNAc sites of tau (at S208, S191, and S184 or S185) in human transgenic mouse BH.
36888912	6	73	from	sites	1513:1517	arg1	S185					1554:1557	S185	1554:1557	S185	1554:1557	This strategy enabled, for the first time, identification of three low abundant N-terminal and mid-domain O-GlcNAc sites of tau (at S208, S191, and S184 or S185) in human transgenic mouse BH.
36888912	6	73	from	sites	1513:1517	arg1	S191					1536:1539	S191	1536:1539	S191	1536:1539	This strategy enabled, for the first time, identification of three low abundant N-terminal and mid-domain O-GlcNAc sites of tau (at S208, S191, and S184 or S185) in human transgenic mouse BH.
36888912	6	73	from	sites	1513:1517	arg1	BH					1586:1587	human transgenic mouse BH	1563:1587	human transgenic mouse BH	1563:1587	This strategy enabled, for the first time, identification of three low abundant N-terminal and mid-domain O-GlcNAc sites of tau (at S208, S191, and S184 or S185) in human transgenic mouse BH.
36888912	6	73	from	sites	1513:1517	arg1	S208					1530:1533	S208	1530:1533	S208	1530:1533	This strategy enabled, for the first time, identification of three low abundant N-terminal and mid-domain O-GlcNAc sites of tau (at S208, S191, and S184 or S185) in human transgenic mouse BH.
36888912	6	73	from	sites	1513:1517	arg1	S184					1546:1549	S184	1546:1549	S184	1546:1549	This strategy enabled, for the first time, identification of three low abundant N-terminal and mid-domain O-GlcNAc sites of tau (at S208, S191, and S184 or S185) in human transgenic mouse BH.
36888912	6	74	theme	abundant	1469:1476	arg1	tau					1522:1524	tau	1522:1524	tau (at S208, S191, and S184 or S185) in human transgenic mouse BH	1522:1587	This strategy enabled, for the first time, identification of three low abundant N-terminal and mid-domain O-GlcNAc sites of tau (at S208, S191, and S184 or S185) in human transgenic mouse BH.
36888912	6	74	theme	abundant	1469:1476	arg1	sites					1513:1517	abundant N-terminal and mid-domain O-GlcNAc sites	1469:1517	three low abundant N-terminal and mid-domain O-GlcNAc sites of tau (at S208, S191, and S184 or S185) in human transgenic mouse BH	1459:1587	This strategy enabled, for the first time, identification of three low abundant N-terminal and mid-domain O-GlcNAc sites of tau (at S208, S191, and S184 or S185) in human transgenic mouse BH.
36888912	1	75	theme	neurodegenerative	420:436	arg1	diseases					438:445	neurodegenerative diseases	420:445	neurodegenerative diseases	420:445	O-β-linked N-acetylglucosaminylation (O-GlcNAcylation) modulates tau phosphorylation and aggregation: the pharmacological increase of tau O-GlcNAcylation upon treatment with inhibitors of O-GlcNAc hydrolase (OGA) constitutes a potential strategy to tackle neurodegenerative diseases.
36888912	4	76	theme	tau	1043:1045	arg1	S400					1035:1038	S400	1035:1038	S400 of tau in mouse brain homogenate (BH) extracts	1035:1085	As a first step, an immunoprecipitation-liquid chromatography-mass spectrometry (IP-LC-MS) methodology was developed to monitor changes in O-GlcNAcylation around S400 of tau in mouse brain homogenate (BH) extracts.
36888912	2	77	theme	tau	460:462	arg1	O-GlcNAcylation					464:478	tau O-GlcNAcylation	460:478	tau O-GlcNAcylation	460:478	Analysis of tau O-GlcNAcylation could potentially be used as a pharmacodynamic biomarker both in preclinical and clinical studies.
36888912	2	78	dep	biomarker	527:535	arg1	both					537:540	both	537:540	both	537:540	Analysis of tau O-GlcNAcylation could potentially be used as a pharmacodynamic biomarker both in preclinical and clinical studies.
36888912	2	79	theme	pharmacodynamic	511:525	arg1	Analysis					448:455	Analysis	448:455	Analysis of tau O-GlcNAcylation	448:478	Analysis of tau O-GlcNAcylation could potentially be used as a pharmacodynamic biomarker both in preclinical and clinical studies.
36888912	2	79	theme	pharmacodynamic	511:525	arg1	biomarker					527:535	a pharmacodynamic biomarker	509:535	a pharmacodynamic biomarker	509:535	Analysis of tau O-GlcNAcylation could potentially be used as a pharmacodynamic biomarker both in preclinical and clinical studies.
36888912	5	80	theme	data	1284:1287	arg1	collection					1252:1261	collection	1252:1261	collection of informative LC-MS data for identification of low-concentration O-GlcNAc-tryptic tau peptides in human transgenic mouse BH extracts	1252:1395	Second, additional O-GlcNAc sites were identified in in-house produced recombinant O-GlcNAcylated human tau at relatively high concentrations, thereby facilitating collection of informative LC-MS data for identification of low-concentration O-GlcNAc-tryptic tau peptides in human transgenic mouse BH extracts.
36888912	0	81	theme	Tau	43:45	arg1	Sites					63:67	Three Tau O-GlcNAcylation Sites	37:67	Three Tau O-GlcNAcylation Sites	37:67	IP-LC-MSMS Enables Identification of Three Tau O-GlcNAcylation Sites as O-GlcNAcase Inhibition Pharmacodynamic Readout in Transgenic Mice Overexpressing Human Tau.
36888912	1	82	theme	hydrolase	361:369	arg1	inhibitors					338:347	inhibitors	338:347	inhibitors of O-GlcNAc hydrolase (OGA)	338:375	O-β-linked N-acetylglucosaminylation (O-GlcNAcylation) modulates tau phosphorylation and aggregation: the pharmacological increase of tau O-GlcNAcylation upon treatment with inhibitors of O-GlcNAc hydrolase (OGA) constitutes a potential strategy to tackle neurodegenerative diseases.
36888912	2	83	theme	preclinical	545:555	arg1	studies					570:576	preclinical and clinical studies	545:576	preclinical and clinical studies	545:576	Analysis of tau O-GlcNAcylation could potentially be used as a pharmacodynamic biomarker both in preclinical and clinical studies.
36888912	3	84	theme	P301S	702:706	arg1	mice					719:722	P301S transgenic mice	702:722	P301S transgenic mice overexpressing human tau and treated with the OGA inhibitor Thiamet G	702:792	The goal of the current study was to confirm tau O-GlcNAcylation at S400 as a pharmacodynamic readout of OGA inhibition in P301S transgenic mice overexpressing human tau and treated with the OGA inhibitor Thiamet G and to explore if additional O-GlcNAcylation sites on tau could be identified.
36888912	3	85	dep	mice	719:722	arg1	overexpressing					724:737	overexpressing	724:737	overexpressing human tau	724:747	The goal of the current study was to confirm tau O-GlcNAcylation at S400 as a pharmacodynamic readout of OGA inhibition in P301S transgenic mice overexpressing human tau and treated with the OGA inhibitor Thiamet G and to explore if additional O-GlcNAcylation sites on tau could be identified.
36888912	3	85	dep	mice	719:722	arg1	treated					753:759	treated	753:759	treated with the OGA inhibitor Thiamet G	753:792	The goal of the current study was to confirm tau O-GlcNAcylation at S400 as a pharmacodynamic readout of OGA inhibition in P301S transgenic mice overexpressing human tau and treated with the OGA inhibitor Thiamet G and to explore if additional O-GlcNAcylation sites on tau could be identified.
36888912	0	86	theme	Transgenic	122:131	arg1	Mice					133:136	Transgenic Mice	122:136	Transgenic Mice Overexpressing Human Tau	122:161	IP-LC-MSMS Enables Identification of Three Tau O-GlcNAcylation Sites as O-GlcNAcase Inhibition Pharmacodynamic Readout in Transgenic Mice Overexpressing Human Tau.
36888912	0	87	theme	Sites	63:67	arg1	Identification					19:32	Identification	19:32	Identification of Three Tau O-GlcNAcylation Sites	19:67	IP-LC-MSMS Enables Identification of Three Tau O-GlcNAcylation Sites as O-GlcNAcase Inhibition Pharmacodynamic Readout in Transgenic Mice Overexpressing Human Tau.
36888912	5	88	theme	additional	1096:1105	arg1	sites					1116:1120	additional O-GlcNAc sites	1096:1120	additional O-GlcNAc sites	1096:1120	Second, additional O-GlcNAc sites were identified in in-house produced recombinant O-GlcNAcylated human tau at relatively high concentrations, thereby facilitating collection of informative LC-MS data for identification of low-concentration O-GlcNAc-tryptic tau peptides in human transgenic mouse BH extracts.
36888912	6	89	theme	mouse	1580:1584	arg1	BH					1586:1587	human transgenic mouse BH	1563:1587	human transgenic mouse BH	1563:1587	This strategy enabled, for the first time, identification of three low abundant N-terminal and mid-domain O-GlcNAc sites of tau (at S208, S191, and S184 or S185) in human transgenic mouse BH.
36888912	5	90	theme	informative	1266:1276	arg1	data					1284:1287	informative LC-MS data	1266:1287	informative LC-MS data	1266:1287	Second, additional O-GlcNAc sites were identified in in-house produced recombinant O-GlcNAcylated human tau at relatively high concentrations, thereby facilitating collection of informative LC-MS data for identification of low-concentration O-GlcNAc-tryptic tau peptides in human transgenic mouse BH extracts.
36888912	3	91	theme	human	739:743	arg1	tau					745:747	human tau	739:747	human tau	739:747	The goal of the current study was to confirm tau O-GlcNAcylation at S400 as a pharmacodynamic readout of OGA inhibition in P301S transgenic mice overexpressing human tau and treated with the OGA inhibitor Thiamet G and to explore if additional O-GlcNAcylation sites on tau could be identified.
36888912	6	92	theme	human	1563:1567	arg1	BH					1586:1587	human transgenic mouse BH	1563:1587	human transgenic mouse BH	1563:1587	This strategy enabled, for the first time, identification of three low abundant N-terminal and mid-domain O-GlcNAc sites of tau (at S208, S191, and S184 or S185) in human transgenic mouse BH.
36888912	7	93	dep	available	1606:1614	arg1	Data					1590:1593	Data	1590:1593	Data	1590:1593	Data are openly available at data.mendeley.com (doi: 10.17632/jp57yk9469.1; doi: 10.17632/8n5j45dnd8.1; doi: 10.17632/h5vdrx4n3d.1).
36888912	7	93	dep	available	1606:1614	arg1	doi					1638:1640	doi	1638:1640	doi: 10.17632/jp57yk9469.1; doi: 10.17632/8n5j45dnd8.1; doi: 10.17632/h5vdrx4n3d.1	1638:1719	Data are openly available at data.mendeley.com (doi: 10.17632/jp57yk9469.1; doi: 10.17632/8n5j45dnd8.1; doi: 10.17632/h5vdrx4n3d.1).
36888912	3	94	theme	OGA	770:772	arg1	G					792:792	the OGA inhibitor Thiamet G	766:792	the OGA inhibitor Thiamet G	766:792	The goal of the current study was to confirm tau O-GlcNAcylation at S400 as a pharmacodynamic readout of OGA inhibition in P301S transgenic mice overexpressing human tau and treated with the OGA inhibitor Thiamet G and to explore if additional O-GlcNAcylation sites on tau could be identified.
36888912	1	95	theme	tau	298:300	arg1	O-GlcNAcylation					302:316	tau O-GlcNAcylation	298:316	tau O-GlcNAcylation	298:316	O-β-linked N-acetylglucosaminylation (O-GlcNAcylation) modulates tau phosphorylation and aggregation: the pharmacological increase of tau O-GlcNAcylation upon treatment with inhibitors of O-GlcNAc hydrolase (OGA) constitutes a potential strategy to tackle neurodegenerative diseases.
36888912	3	96	theme	current	595:601	arg1	study					603:607	the current study	591:607	the current study	591:607	The goal of the current study was to confirm tau O-GlcNAcylation at S400 as a pharmacodynamic readout of OGA inhibition in P301S transgenic mice overexpressing human tau and treated with the OGA inhibitor Thiamet G and to explore if additional O-GlcNAcylation sites on tau could be identified.
36888912	5	97	theme	transgenic	1368:1377	arg1	extracts					1388:1395	human transgenic mouse BH extracts	1362:1395	human transgenic mouse BH extracts	1362:1395	Second, additional O-GlcNAc sites were identified in in-house produced recombinant O-GlcNAcylated human tau at relatively high concentrations, thereby facilitating collection of informative LC-MS data for identification of low-concentration O-GlcNAc-tryptic tau peptides in human transgenic mouse BH extracts.
32830957	4	0	theme	various	621:627	arg1	proteins					629:636	various proteins	621:636	various proteins that are known to be modified by O-GlcNAcylation including CK2, NOD2, SREBP1c, AKT1, PKM, and PFKFB3	621:737	The method is validated on various proteins that are known to be modified by O-GlcNAcylation including CK2, NOD2, SREBP1c, AKT1, PKM, and PFKFB3, and on the nuclear extract of HEK293 cells.
32830957	3	1	theme	modification	381:392	arg1	identification					354:367	the identification	350:367	the identification of O-GlcNAc modification via tandem glycan labeling	350:419	Here, we report a highly efficient method for the identification of O-GlcNAc modification via tandem glycan labeling, in which O-GlcNAc is first galactosylated and then sialylated with a fluorophore-conjugated sialic acid residue, therefore enabling highly sensitive fluorescent detection.
32830957	5	2	theme	metabolic	962:970	arg1	pathway					981:987	the metabolic O-GlcNAc pathway	958:987	the metabolic O-GlcNAc pathway	958:987	Using this method, we then report the evidence that hypoxia-inducible factor HIF1α is a potential target for O-GlcNAcylation, suggesting a possibly direct connection between the metabolic O-GlcNAc pathway and the hypoxia pathway.
32830957	4	3	mod	modified	659:666	arg3	O-GlcNAcylation					671:685	O-GlcNAcylation	671:685	O-GlcNAcylation including CK2, NOD2, SREBP1c, AKT1, PKM, and PFKFB3	671:737	The method is validated on various proteins that are known to be modified by O-GlcNAcylation including CK2, NOD2, SREBP1c, AKT1, PKM, and PFKFB3, and on the nuclear extract of HEK293 cells.
32830957	4	3	mod	modified	659:666	arg1	proteins					629:636	various proteins	621:636	various proteins that are known to be modified by O-GlcNAcylation including CK2, NOD2, SREBP1c, AKT1, PKM, and PFKFB3	621:737	The method is validated on various proteins that are known to be modified by O-GlcNAcylation including CK2, NOD2, SREBP1c, AKT1, PKM, and PFKFB3, and on the nuclear extract of HEK293 cells.
32830957	5	4	theme	O-GlcNAc	972:979	arg1	pathway					981:987	the metabolic O-GlcNAc pathway	958:987	the metabolic O-GlcNAc pathway	958:987	Using this method, we then report the evidence that hypoxia-inducible factor HIF1α is a potential target for O-GlcNAcylation, suggesting a possibly direct connection between the metabolic O-GlcNAc pathway and the hypoxia pathway.
32830957	3	5	theme	fluorescent	571:581	arg1	detection					583:591	highly sensitive fluorescent detection	554:591	highly sensitive fluorescent detection	554:591	Here, we report a highly efficient method for the identification of O-GlcNAc modification via tandem glycan labeling, in which O-GlcNAc is first galactosylated and then sialylated with a fluorophore-conjugated sialic acid residue, therefore enabling highly sensitive fluorescent detection.
32830957	1	6	theme	various	180:186	arg1	pathways					199:206	various regulatory pathways	180:206	various regulatory pathways	180:206	O-GlcNAcylation is a reversible serine/threonine glycosylation on cytosolic and nuclear proteins that are involved in various regulatory pathways.
32830957	1	7	gly	glycosylation	111:123	arg1	proteins					150:157	cytosolic and nuclear proteins	128:157	cytosolic and nuclear proteins that are involved in various regulatory pathways	128:206	O-GlcNAcylation is a reversible serine/threonine glycosylation on cytosolic and nuclear proteins that are involved in various regulatory pathways.
32830957	4	8	theme	HEK293	770:775	arg1	cells					777:781	HEK293 cells	770:781	HEK293 cells	770:781	The method is validated on various proteins that are known to be modified by O-GlcNAcylation including CK2, NOD2, SREBP1c, AKT1, PKM, and PFKFB3, and on the nuclear extract of HEK293 cells.
32830957	1	9	theme	regulatory	188:197	arg1	pathways					199:206	various regulatory pathways	180:206	various regulatory pathways	180:206	O-GlcNAcylation is a reversible serine/threonine glycosylation on cytosolic and nuclear proteins that are involved in various regulatory pathways.
32830957	1	10	theme	reversible	83:92	arg1	glycosylation					111:123	a reversible serine/threonine glycosylation	81:123	a reversible serine/threonine glycosylation on cytosolic and nuclear proteins that are involved in various regulatory pathways	81:206	O-GlcNAcylation is a reversible serine/threonine glycosylation on cytosolic and nuclear proteins that are involved in various regulatory pathways.
32830957	1	10	theme	reversible	83:92	arg1	O-GlcNAcylation					62:76	O-GlcNAcylation	62:76	O-GlcNAcylation	62:76	O-GlcNAcylation is a reversible serine/threonine glycosylation on cytosolic and nuclear proteins that are involved in various regulatory pathways.
32830957	0	11	theme	Fluorescent	0:10	arg1	Detection					12:20	Fluorescent Detection	0:20	Fluorescent Detection of O-GlcNAc via Tandem Glycan Labeling.	0:60	Fluorescent Detection of O-GlcNAc via Tandem Glycan Labeling.
32830957	1	12	theme	serine/threonine	94:109	arg1	glycosylation					111:123	a reversible serine/threonine glycosylation	81:123	a reversible serine/threonine glycosylation on cytosolic and nuclear proteins that are involved in various regulatory pathways	81:206	O-GlcNAcylation is a reversible serine/threonine glycosylation on cytosolic and nuclear proteins that are involved in various regulatory pathways.
32830957	1	12	theme	serine/threonine	94:109	arg1	O-GlcNAcylation					62:76	O-GlcNAcylation	62:76	O-GlcNAcylation	62:76	O-GlcNAcylation is a reversible serine/threonine glycosylation on cytosolic and nuclear proteins that are involved in various regulatory pathways.
32830957	3	13	theme	tandem	398:403	arg1	labeling					412:419	tandem glycan labeling	398:419	tandem glycan labeling	398:419	Here, we report a highly efficient method for the identification of O-GlcNAc modification via tandem glycan labeling, in which O-GlcNAc is first galactosylated and then sialylated with a fluorophore-conjugated sialic acid residue, therefore enabling highly sensitive fluorescent detection.
32830957	4	14	theme	nuclear	751:757	arg1	extract					759:765	the nuclear extract	747:765	the nuclear extract of HEK293 cells	747:781	The method is validated on various proteins that are known to be modified by O-GlcNAcylation including CK2, NOD2, SREBP1c, AKT1, PKM, and PFKFB3, and on the nuclear extract of HEK293 cells.
32830957	3	15	theme	glycan	405:410	arg1	labeling					412:419	tandem glycan labeling	398:419	tandem glycan labeling	398:419	Here, we report a highly efficient method for the identification of O-GlcNAc modification via tandem glycan labeling, in which O-GlcNAc is first galactosylated and then sialylated with a fluorophore-conjugated sialic acid residue, therefore enabling highly sensitive fluorescent detection.
32830957	4	16	theme	cells	777:781	arg1	extract					759:765	the nuclear extract	747:765	the nuclear extract of HEK293 cells	747:781	The method is validated on various proteins that are known to be modified by O-GlcNAcylation including CK2, NOD2, SREBP1c, AKT1, PKM, and PFKFB3, and on the nuclear extract of HEK293 cells.
32830957	3	17	theme	fluorophore-conjugated	491:512	arg1	residue					526:532	a fluorophore-conjugated sialic acid residue	489:532	a fluorophore-conjugated sialic acid residue	489:532	Here, we report a highly efficient method for the identification of O-GlcNAc modification via tandem glycan labeling, in which O-GlcNAc is first galactosylated and then sialylated with a fluorophore-conjugated sialic acid residue, therefore enabling highly sensitive fluorescent detection.
32830957	0	18	theme	Tandem	38:43	arg1	Labeling					52:59	Tandem Glycan Labeling	38:59	Tandem Glycan Labeling	38:59	Fluorescent Detection of O-GlcNAc via Tandem Glycan Labeling.
32830957	2	19	theme	O-GlcNAcylation	254:268	arg1	substrates					270:279	O-GlcNAcylation substrates	254:279	O-GlcNAcylation substrates	254:279	However, the detection and quantification of O-GlcNAcylation substrates have been challenging.
32830957	5	20	theme	factor	854:859	arg1	HIF1α					861:865	hypoxia-inducible factor HIF1α	836:865	hypoxia-inducible factor HIF1α	836:865	Using this method, we then report the evidence that hypoxia-inducible factor HIF1α is a potential target for O-GlcNAcylation, suggesting a possibly direct connection between the metabolic O-GlcNAc pathway and the hypoxia pathway.
32830957	5	20	theme	factor	854:859	arg1	target					882:887	a potential target	870:887	a potential target for O-GlcNAcylation	870:907	Using this method, we then report the evidence that hypoxia-inducible factor HIF1α is a potential target for O-GlcNAcylation, suggesting a possibly direct connection between the metabolic O-GlcNAc pathway and the hypoxia pathway.
32830957	0	21	theme	O-GlcNAc	25:32	arg1	Detection					12:20	Fluorescent Detection	0:20	Fluorescent Detection of O-GlcNAc via Tandem Glycan Labeling.	0:60	Fluorescent Detection of O-GlcNAc via Tandem Glycan Labeling.
32830957	3	22	theme	O-GlcNAc	372:379	arg1	modification					381:392	O-GlcNAc modification	372:392	O-GlcNAc modification	372:392	Here, we report a highly efficient method for the identification of O-GlcNAc modification via tandem glycan labeling, in which O-GlcNAc is first galactosylated and then sialylated with a fluorophore-conjugated sialic acid residue, therefore enabling highly sensitive fluorescent detection.
32830957	1	23	theme	cytosolic	128:136	arg1	proteins					150:157	cytosolic and nuclear proteins	128:157	cytosolic and nuclear proteins that are involved in various regulatory pathways	128:206	O-GlcNAcylation is a reversible serine/threonine glycosylation on cytosolic and nuclear proteins that are involved in various regulatory pathways.
32830957	0	24	theme	Glycan	45:50	arg1	Labeling					52:59	Tandem Glycan Labeling	38:59	Tandem Glycan Labeling	38:59	Fluorescent Detection of O-GlcNAc via Tandem Glycan Labeling.
32830957	3	25	theme	efficient	329:337	arg1	method					339:344	a highly efficient method	320:344	a highly efficient method	320:344	Here, we report a highly efficient method for the identification of O-GlcNAc modification via tandem glycan labeling, in which O-GlcNAc is first galactosylated and then sialylated with a fluorophore-conjugated sialic acid residue, therefore enabling highly sensitive fluorescent detection.
32830957	3	26	gly	sialylated	473:482	arg1	O-GlcNAc					431:438	O-GlcNAc	431:438	O-GlcNAc	431:438	Here, we report a highly efficient method for the identification of O-GlcNAc modification via tandem glycan labeling, in which O-GlcNAc is first galactosylated and then sialylated with a fluorophore-conjugated sialic acid residue, therefore enabling highly sensitive fluorescent detection.
32830957	1	27	from	glycosylation	111:123	arg1	proteins					150:157	cytosolic and nuclear proteins	128:157	cytosolic and nuclear proteins that are involved in various regulatory pathways	128:206	O-GlcNAcylation is a reversible serine/threonine glycosylation on cytosolic and nuclear proteins that are involved in various regulatory pathways.
32830957	5	28	theme	direct	932:937	arg1	connection					939:948	a possibly direct connection	921:948	a possibly direct connection between the metabolic O-GlcNAc pathway and the hypoxia pathway	921:1011	Using this method, we then report the evidence that hypoxia-inducible factor HIF1α is a potential target for O-GlcNAcylation, suggesting a possibly direct connection between the metabolic O-GlcNAc pathway and the hypoxia pathway.
32830957	1	29	theme	nuclear	142:148	arg1	proteins					150:157	cytosolic and nuclear proteins	128:157	cytosolic and nuclear proteins that are involved in various regulatory pathways	128:206	O-GlcNAcylation is a reversible serine/threonine glycosylation on cytosolic and nuclear proteins that are involved in various regulatory pathways.
32830957	5	30	theme	hypoxia	997:1003	arg1	pathway					1005:1011	the hypoxia pathway	993:1011	the hypoxia pathway	993:1011	Using this method, we then report the evidence that hypoxia-inducible factor HIF1α is a potential target for O-GlcNAcylation, suggesting a possibly direct connection between the metabolic O-GlcNAc pathway and the hypoxia pathway.
32830957	3	31	theme	acid	521:524	arg1	residue					526:532	a fluorophore-conjugated sialic acid residue	489:532	a fluorophore-conjugated sialic acid residue	489:532	Here, we report a highly efficient method for the identification of O-GlcNAc modification via tandem glycan labeling, in which O-GlcNAc is first galactosylated and then sialylated with a fluorophore-conjugated sialic acid residue, therefore enabling highly sensitive fluorescent detection.
32830957	3	32	theme	sialic	514:519	arg1	residue					526:532	a fluorophore-conjugated sialic acid residue	489:532	a fluorophore-conjugated sialic acid residue	489:532	Here, we report a highly efficient method for the identification of O-GlcNAc modification via tandem glycan labeling, in which O-GlcNAc is first galactosylated and then sialylated with a fluorophore-conjugated sialic acid residue, therefore enabling highly sensitive fluorescent detection.
32830957	5	33	theme	hypoxia-inducible	836:852	arg1	HIF1α					861:865	hypoxia-inducible factor HIF1α	836:865	hypoxia-inducible factor HIF1α	836:865	Using this method, we then report the evidence that hypoxia-inducible factor HIF1α is a potential target for O-GlcNAcylation, suggesting a possibly direct connection between the metabolic O-GlcNAc pathway and the hypoxia pathway.
32830957	5	33	theme	hypoxia-inducible	836:852	arg1	target					882:887	a potential target	870:887	a potential target for O-GlcNAcylation	870:907	Using this method, we then report the evidence that hypoxia-inducible factor HIF1α is a potential target for O-GlcNAcylation, suggesting a possibly direct connection between the metabolic O-GlcNAc pathway and the hypoxia pathway.
32830957	5	34	theme	potential	872:880	arg1	HIF1α					861:865	hypoxia-inducible factor HIF1α	836:865	hypoxia-inducible factor HIF1α	836:865	Using this method, we then report the evidence that hypoxia-inducible factor HIF1α is a potential target for O-GlcNAcylation, suggesting a possibly direct connection between the metabolic O-GlcNAc pathway and the hypoxia pathway.
32830957	5	34	theme	potential	872:880	arg1	target					882:887	a potential target	870:887	a potential target for O-GlcNAcylation	870:907	Using this method, we then report the evidence that hypoxia-inducible factor HIF1α is a potential target for O-GlcNAcylation, suggesting a possibly direct connection between the metabolic O-GlcNAc pathway and the hypoxia pathway.
32830957	2	35	dep	detection	222:230	arg1	the					218:220	the	218:220	the	218:220	However, the detection and quantification of O-GlcNAcylation substrates have been challenging.
32830957	2	36	theme	substrates	270:279	arg1	quantification					236:249	quantification	236:249	quantification	236:249	However, the detection and quantification of O-GlcNAcylation substrates have been challenging.
32830957	2	36	theme	substrates	270:279	arg1	detection					222:230	detection	222:230	detection	222:230	However, the detection and quantification of O-GlcNAcylation substrates have been challenging.
32830957	3	37	theme	sensitive	561:569	arg1	detection					583:591	highly sensitive fluorescent detection	554:591	highly sensitive fluorescent detection	554:591	Here, we report a highly efficient method for the identification of O-GlcNAc modification via tandem glycan labeling, in which O-GlcNAc is first galactosylated and then sialylated with a fluorophore-conjugated sialic acid residue, therefore enabling highly sensitive fluorescent detection.
26252736	3	0	theme	modifications	533:545	arg1	crosstalk					516:524	crosstalk	516:524	crosstalk of the modifications	516:545	Therefore, we explored crosstalk of the modifications by RNA interference against O-GlcNAc transferase (OGT) in colorectal cancer cells.
26252736	1	1	theme	post-translational	183:200	arg1	modification					202:213	a dynamic post-translational modification	173:213	a dynamic post-translational modification that has extensive crosstalk with phosphorylation either at the same or adjacent sites of various proteins	173:320	O-GlcNAcylation is a dynamic post-translational modification that has extensive crosstalk with phosphorylation either at the same or adjacent sites of various proteins.
26252736	1	1	theme	post-translational	183:200	arg1	O-GlcNAcylation					154:168	O-GlcNAcylation	154:168	O-GlcNAcylation	154:168	O-GlcNAcylation is a dynamic post-translational modification that has extensive crosstalk with phosphorylation either at the same or adjacent sites of various proteins.
26252736	4	2	theme	O-GlcNAc	719:726	arg1	phosphorylation					739:753	serine phosphorylation	732:753	serine phosphorylation of many proteins including serine hydroxymethyltransferase, cytokeratin-8, pyruvate kinase M2 (PKM2), heterogeneous nuclear ribonucleoprotein L, and lamin-B1	732:911	Two-dimensional immunoblotting and mass spectrometric analysis showed that the levels of O-GlcNAc and serine phosphorylation of many proteins including serine hydroxymethyltransferase, cytokeratin-8, pyruvate kinase M2 (PKM2), heterogeneous nuclear ribonucleoprotein L, and lamin-B1, were reduced in siOGT cells compared to siScramble cells.
26252736	4	2	theme	O-GlcNAc	719:726	arg1	levels					709:714	the levels	705:714	the levels of O-GlcNAc	705:726	Two-dimensional immunoblotting and mass spectrometric analysis showed that the levels of O-GlcNAc and serine phosphorylation of many proteins including serine hydroxymethyltransferase, cytokeratin-8, pyruvate kinase M2 (PKM2), heterogeneous nuclear ribonucleoprotein L, and lamin-B1, were reduced in siOGT cells compared to siScramble cells.
26252736	1	3	theme	extensive	224:232	arg1	crosstalk					234:242	extensive crosstalk	224:242	extensive crosstalk with phosphorylation either at the same or adjacent sites of various proteins	224:320	O-GlcNAcylation is a dynamic post-translational modification that has extensive crosstalk with phosphorylation either at the same or adjacent sites of various proteins.
26252736	9	4	dep	roles	1685:1689	arg1	regulating					1762:1771	regulating	1762:1771	regulating PKM2 activity and expression	1762:1800	These results suggested roles of O-GlcNAcylation in modulating serine phosphorylation, as well as in regulating PKM2 activity and expression.
26252736	9	4	dep	roles	1685:1689	arg1	modulating					1713:1722	modulating	1713:1722	modulating serine phosphorylation	1713:1745	These results suggested roles of O-GlcNAcylation in modulating serine phosphorylation, as well as in regulating PKM2 activity and expression.
26252736	0	5	theme	cancer	140:145	arg1	cells					147:151	colorectal cancer cells	129:151	colorectal cancer cells	129:151	Alteration of O-GlcNAcylation affects serine phosphorylation and regulates gene expression and activity of pyruvate kinase M2 in colorectal cancer cells.
26252736	8	6	theme	colorectal	1504:1513	arg1	SW620					1529:1533	SW620	1529:1533	SW620	1529:1533	Moreover, the metastatic colorectal cancer cells, SW620, had more O-GlcNAc-PKM2 and showed lower PKM2-specific activity compared to the non-metastatic colorectal cancer SW480 cells.
26252736	8	6	theme	colorectal	1504:1513	arg1	cells					1522:1526	the metastatic colorectal cancer cells	1489:1526	the metastatic colorectal cancer cells	1489:1526	Moreover, the metastatic colorectal cancer cells, SW620, had more O-GlcNAc-PKM2 and showed lower PKM2-specific activity compared to the non-metastatic colorectal cancer SW480 cells.
26252736	6	7	theme	expression	1277:1286	arg1	level					1288:1292	PKM2 expression level	1272:1292	PKM2 expression level	1272:1292	In addition, when global O-GlcNAcylation was enhanced by treating cells with Thiamet-G, PKM2 expression level was upregulated, but PKM2-specific activity was decreased.
26252736	4	8	theme	proteins	763:770	arg1	phosphorylation					739:753	serine phosphorylation	732:753	serine phosphorylation of many proteins including serine hydroxymethyltransferase, cytokeratin-8, pyruvate kinase M2 (PKM2), heterogeneous nuclear ribonucleoprotein L, and lamin-B1	732:911	Two-dimensional immunoblotting and mass spectrometric analysis showed that the levels of O-GlcNAc and serine phosphorylation of many proteins including serine hydroxymethyltransferase, cytokeratin-8, pyruvate kinase M2 (PKM2), heterogeneous nuclear ribonucleoprotein L, and lamin-B1, were reduced in siOGT cells compared to siScramble cells.
26252736	4	8	theme	proteins	763:770	arg1	levels					709:714	the levels	705:714	the levels of O-GlcNAc	705:726	Two-dimensional immunoblotting and mass spectrometric analysis showed that the levels of O-GlcNAc and serine phosphorylation of many proteins including serine hydroxymethyltransferase, cytokeratin-8, pyruvate kinase M2 (PKM2), heterogeneous nuclear ribonucleoprotein L, and lamin-B1, were reduced in siOGT cells compared to siScramble cells.
26252736	3	9	theme	cancer	616:621	arg1	cells					623:627	colorectal cancer cells	605:627	colorectal cancer cells	605:627	Therefore, we explored crosstalk of the modifications by RNA interference against O-GlcNAc transferase (OGT) in colorectal cancer cells.
26252736	7	10	theme	PKM2	1396:1399	arg1	level					1412:1416	PKM2 expression level	1396:1416	PKM2 expression level	1396:1416	On the other hand, in OGT knockdown cells, PKM2 expression level was downregulated, but PKM2-specific activity was increased.
26252736	4	11	theme	serine	782:787	arg1	hydroxymethyltransferase					789:812	serine hydroxymethyltransferase	782:812	serine hydroxymethyltransferase	782:812	Two-dimensional immunoblotting and mass spectrometric analysis showed that the levels of O-GlcNAc and serine phosphorylation of many proteins including serine hydroxymethyltransferase, cytokeratin-8, pyruvate kinase M2 (PKM2), heterogeneous nuclear ribonucleoprotein L, and lamin-B1, were reduced in siOGT cells compared to siScramble cells.
26252736	10	12	theme	PKM2	1844:1847	arg1	O-GlcNAcylation					1825:1839	O-GlcNAcylation	1825:1839	O-GlcNAcylation of PKM2	1825:1847	Interfering levels of O-GlcNAcylation of PKM2 may be a novel target in controlling cancer metabolism and tumorigenesis of colorectal cancer.
26252736	4	13	theme	serine	732:737	arg1	phosphorylation					739:753	serine phosphorylation	732:753	serine phosphorylation of many proteins including serine hydroxymethyltransferase, cytokeratin-8, pyruvate kinase M2 (PKM2), heterogeneous nuclear ribonucleoprotein L, and lamin-B1	732:911	Two-dimensional immunoblotting and mass spectrometric analysis showed that the levels of O-GlcNAc and serine phosphorylation of many proteins including serine hydroxymethyltransferase, cytokeratin-8, pyruvate kinase M2 (PKM2), heterogeneous nuclear ribonucleoprotein L, and lamin-B1, were reduced in siOGT cells compared to siScramble cells.
26252736	0	14	theme	gene	75:78	arg1	expression					80:89	gene expression	75:89	gene expression	75:89	Alteration of O-GlcNAcylation affects serine phosphorylation and regulates gene expression and activity of pyruvate kinase M2 in colorectal cancer cells.
26252736	0	15	from	expression	80:89	arg1	cells					147:151	colorectal cancer cells	129:151	colorectal cancer cells	129:151	Alteration of O-GlcNAcylation affects serine phosphorylation and regulates gene expression and activity of pyruvate kinase M2 in colorectal cancer cells.
26252736	4	16	theme	kinase	839:844	arg1	PKM2					850:853	PKM2	850:853	PKM2	850:853	Two-dimensional immunoblotting and mass spectrometric analysis showed that the levels of O-GlcNAc and serine phosphorylation of many proteins including serine hydroxymethyltransferase, cytokeratin-8, pyruvate kinase M2 (PKM2), heterogeneous nuclear ribonucleoprotein L, and lamin-B1, were reduced in siOGT cells compared to siScramble cells.
26252736	4	16	theme	kinase	839:844	arg1	M2					846:847	pyruvate kinase M2	830:847	pyruvate kinase M2 (PKM2)	830:854	Two-dimensional immunoblotting and mass spectrometric analysis showed that the levels of O-GlcNAc and serine phosphorylation of many proteins including serine hydroxymethyltransferase, cytokeratin-8, pyruvate kinase M2 (PKM2), heterogeneous nuclear ribonucleoprotein L, and lamin-B1, were reduced in siOGT cells compared to siScramble cells.
26252736	3	17	from	transferase	584:594	arg1	cells					623:627	colorectal cancer cells	605:627	colorectal cancer cells	605:627	Therefore, we explored crosstalk of the modifications by RNA interference against O-GlcNAc transferase (OGT) in colorectal cancer cells.
26252736	5	18	theme	O-GlcNAc	1030:1037	arg1	levels					1066:1071	O-GlcNAc and serine phosphorylation levels	1030:1071	O-GlcNAc and serine phosphorylation levels	1030:1071	In HT29 cells, immunoprecipitated PKM2 revealed decreased O-GlcNAc and serine phosphorylation levels after siOGT knockdown, but increased levels after treatment with Thiamet-G, an inhibitor of O-GlcNAcase (OGA).
26252736	0	19	theme	kinase	116:121	arg1	M2					123:124	pyruvate kinase M2	107:124	pyruvate kinase M2	107:124	Alteration of O-GlcNAcylation affects serine phosphorylation and regulates gene expression and activity of pyruvate kinase M2 in colorectal cancer cells.
26252736	5	20	theme	serine	1043:1048	arg1	phosphorylation					1050:1064	serine phosphorylation	1043:1064	serine phosphorylation	1043:1064	In HT29 cells, immunoprecipitated PKM2 revealed decreased O-GlcNAc and serine phosphorylation levels after siOGT knockdown, but increased levels after treatment with Thiamet-G, an inhibitor of O-GlcNAcase (OGA).
26252736	7	21	theme	knockdown	1379:1387	arg1	cells					1389:1393	OGT knockdown cells	1375:1393	OGT knockdown cells	1375:1393	On the other hand, in OGT knockdown cells, PKM2 expression level was downregulated, but PKM2-specific activity was increased.
26252736	8	22	theme	PKM2-specific	1576:1588	arg1	activity					1590:1597	lower PKM2-specific activity	1570:1597	lower PKM2-specific activity	1570:1597	Moreover, the metastatic colorectal cancer cells, SW620, had more O-GlcNAc-PKM2 and showed lower PKM2-specific activity compared to the non-metastatic colorectal cancer SW480 cells.
26252736	2	23	theme	colorectal	414:423	arg1	cancer					425:430	colorectal cancer	414:430	colorectal cancer	414:430	We have previously reported that O-GlcNAcylation level was increased in primary breast and colorectal cancer, but the interplay of the two modifications remains unclear.
26252736	5	24	theme	immunoprecipitated	987:1004	arg1	PKM2					1006:1009	immunoprecipitated PKM2	987:1009	immunoprecipitated PKM2	987:1009	In HT29 cells, immunoprecipitated PKM2 revealed decreased O-GlcNAc and serine phosphorylation levels after siOGT knockdown, but increased levels after treatment with Thiamet-G, an inhibitor of O-GlcNAcase (OGA).
26252736	0	25	theme	O-GlcNAcylation	14:28	arg1	Alteration					0:9	Alteration	0:9	Alteration of O-GlcNAcylation	0:28	Alteration of O-GlcNAcylation affects serine phosphorylation and regulates gene expression and activity of pyruvate kinase M2 in colorectal cancer cells.
26252736	1	26	theme	proteins	313:320	arg1	proteins					313:320	various proteins	305:320	various proteins	305:320	O-GlcNAcylation is a dynamic post-translational modification that has extensive crosstalk with phosphorylation either at the same or adjacent sites of various proteins.
26252736	1	26	theme	proteins	313:320	arg1	sites					296:300	the same or adjacent sites	275:300	the same or adjacent sites of various proteins	275:320	O-GlcNAcylation is a dynamic post-translational modification that has extensive crosstalk with phosphorylation either at the same or adjacent sites of various proteins.
26252736	4	27	theme	ribonucleoprotein	879:895	arg1	L					897:897	heterogeneous nuclear ribonucleoprotein L	857:897	heterogeneous nuclear ribonucleoprotein L	857:897	Two-dimensional immunoblotting and mass spectrometric analysis showed that the levels of O-GlcNAc and serine phosphorylation of many proteins including serine hydroxymethyltransferase, cytokeratin-8, pyruvate kinase M2 (PKM2), heterogeneous nuclear ribonucleoprotein L, and lamin-B1, were reduced in siOGT cells compared to siScramble cells.
26252736	0	28	theme	serine	38:43	arg1	phosphorylation					45:59	serine phosphorylation	38:59	serine phosphorylation	38:59	Alteration of O-GlcNAcylation affects serine phosphorylation and regulates gene expression and activity of pyruvate kinase M2 in colorectal cancer cells.
26252736	8	29	theme	colorectal	1630:1639	arg1	cancer					1641:1646	non-metastatic colorectal cancer	1615:1646	the non-metastatic colorectal cancer SW480 cells	1611:1658	Moreover, the metastatic colorectal cancer cells, SW620, had more O-GlcNAc-PKM2 and showed lower PKM2-specific activity compared to the non-metastatic colorectal cancer SW480 cells.
26252736	10	30	theme	colorectal	1925:1934	arg1	cancer					1936:1941	colorectal cancer	1925:1941	colorectal cancer	1925:1941	Interfering levels of O-GlcNAcylation of PKM2 may be a novel target in controlling cancer metabolism and tumorigenesis of colorectal cancer.
26252736	8	31	theme	SW480	1648:1652	arg1	cells					1654:1658	the non-metastatic colorectal cancer SW480 cells	1611:1658	the non-metastatic colorectal cancer SW480 cells	1611:1658	Moreover, the metastatic colorectal cancer cells, SW620, had more O-GlcNAc-PKM2 and showed lower PKM2-specific activity compared to the non-metastatic colorectal cancer SW480 cells.
26252736	2	32	theme	O-GlcNAcylation	356:370	arg1	level					372:376	O-GlcNAcylation level	356:376	O-GlcNAcylation level	356:376	We have previously reported that O-GlcNAcylation level was increased in primary breast and colorectal cancer, but the interplay of the two modifications remains unclear.
26252736	4	33	theme	Two-dimensional	630:644	arg1	immunoblotting					646:659	Two-dimensional immunoblotting and mass spectrometric analysis	630:691	immunoblotting	646:659	Two-dimensional immunoblotting and mass spectrometric analysis showed that the levels of O-GlcNAc and serine phosphorylation of many proteins including serine hydroxymethyltransferase, cytokeratin-8, pyruvate kinase M2 (PKM2), heterogeneous nuclear ribonucleoprotein L, and lamin-B1, were reduced in siOGT cells compared to siScramble cells.
26252736	1	34	contain	has	220:222	arg1	modification					202:213	a dynamic post-translational modification	173:213	a dynamic post-translational modification that has extensive crosstalk with phosphorylation either at the same or adjacent sites of various proteins	173:320	O-GlcNAcylation is a dynamic post-translational modification that has extensive crosstalk with phosphorylation either at the same or adjacent sites of various proteins.
26252736	1	34	contain	has	220:222	arg1	O-GlcNAcylation					154:168	O-GlcNAcylation	154:168	O-GlcNAcylation	154:168	O-GlcNAcylation is a dynamic post-translational modification that has extensive crosstalk with phosphorylation either at the same or adjacent sites of various proteins.
26252736	1	34	contain	has	220:222	arg2	crosstalk					234:242	extensive crosstalk	224:242	extensive crosstalk with phosphorylation either at the same or adjacent sites of various proteins	224:320	O-GlcNAcylation is a dynamic post-translational modification that has extensive crosstalk with phosphorylation either at the same or adjacent sites of various proteins.
26252736	4	35	theme	heterogeneous	857:869	arg1	ribonucleoprotein					879:895	heterogeneous nuclear ribonucleoprotein	857:895	heterogeneous nuclear ribonucleoprotein L	857:897	Two-dimensional immunoblotting and mass spectrometric analysis showed that the levels of O-GlcNAc and serine phosphorylation of many proteins including serine hydroxymethyltransferase, cytokeratin-8, pyruvate kinase M2 (PKM2), heterogeneous nuclear ribonucleoprotein L, and lamin-B1, were reduced in siOGT cells compared to siScramble cells.
26252736	5	36	theme	siOGT	1079:1083	arg1	knockdown					1085:1093	siOGT knockdown	1079:1093	siOGT knockdown	1079:1093	In HT29 cells, immunoprecipitated PKM2 revealed decreased O-GlcNAc and serine phosphorylation levels after siOGT knockdown, but increased levels after treatment with Thiamet-G, an inhibitor of O-GlcNAcase (OGA).
26252736	1	37	theme	same	279:282	arg1	proteins					313:320	various proteins	305:320	various proteins	305:320	O-GlcNAcylation is a dynamic post-translational modification that has extensive crosstalk with phosphorylation either at the same or adjacent sites of various proteins.
26252736	1	37	theme	same	279:282	arg1	sites					296:300	the same or adjacent sites	275:300	the same or adjacent sites of various proteins	275:320	O-GlcNAcylation is a dynamic post-translational modification that has extensive crosstalk with phosphorylation either at the same or adjacent sites of various proteins.
26252736	9	38	theme	serine	1724:1729	arg1	phosphorylation					1731:1745	serine phosphorylation	1724:1745	serine phosphorylation	1724:1745	These results suggested roles of O-GlcNAcylation in modulating serine phosphorylation, as well as in regulating PKM2 activity and expression.
26252736	3	39	theme	O-GlcNAc	575:582	arg1	OGT					597:599	OGT	597:599	OGT	597:599	Therefore, we explored crosstalk of the modifications by RNA interference against O-GlcNAc transferase (OGT) in colorectal cancer cells.
26252736	3	39	theme	O-GlcNAc	575:582	arg1	transferase					584:594	O-GlcNAc transferase	575:594	O-GlcNAc transferase (OGT) in colorectal cancer cells	575:627	Therefore, we explored crosstalk of the modifications by RNA interference against O-GlcNAc transferase (OGT) in colorectal cancer cells.
26252736	1	40	theme	adjacent	287:294	arg1	proteins					313:320	various proteins	305:320	various proteins	305:320	O-GlcNAcylation is a dynamic post-translational modification that has extensive crosstalk with phosphorylation either at the same or adjacent sites of various proteins.
26252736	1	40	theme	adjacent	287:294	arg1	sites					296:300	the same or adjacent sites	275:300	the same or adjacent sites of various proteins	275:320	O-GlcNAcylation is a dynamic post-translational modification that has extensive crosstalk with phosphorylation either at the same or adjacent sites of various proteins.
26252736	4	41	theme	siOGT	930:934	arg1	cells					936:940	siOGT cells	930:940	siOGT cells	930:940	Two-dimensional immunoblotting and mass spectrometric analysis showed that the levels of O-GlcNAc and serine phosphorylation of many proteins including serine hydroxymethyltransferase, cytokeratin-8, pyruvate kinase M2 (PKM2), heterogeneous nuclear ribonucleoprotein L, and lamin-B1, were reduced in siOGT cells compared to siScramble cells.
26252736	6	42	theme	PKM2-specific	1315:1327	arg1	activity					1329:1336	PKM2-specific activity	1315:1336	PKM2-specific activity	1315:1336	In addition, when global O-GlcNAcylation was enhanced by treating cells with Thiamet-G, PKM2 expression level was upregulated, but PKM2-specific activity was decreased.
26252736	10	43	theme	O-GlcNAcylation	1825:1839	arg1	target					1864:1869	a novel target	1856:1869	a novel target	1856:1869	Interfering levels of O-GlcNAcylation of PKM2 may be a novel target in controlling cancer metabolism and tumorigenesis of colorectal cancer.
26252736	10	43	theme	O-GlcNAcylation	1825:1839	arg1	levels					1815:1820	Interfering levels	1803:1820	Interfering levels of O-GlcNAcylation of PKM2	1803:1847	Interfering levels of O-GlcNAcylation of PKM2 may be a novel target in controlling cancer metabolism and tumorigenesis of colorectal cancer.
26252736	1	44	theme	dynamic	175:181	arg1	modification					202:213	a dynamic post-translational modification	173:213	a dynamic post-translational modification that has extensive crosstalk with phosphorylation either at the same or adjacent sites of various proteins	173:320	O-GlcNAcylation is a dynamic post-translational modification that has extensive crosstalk with phosphorylation either at the same or adjacent sites of various proteins.
26252736	1	44	theme	dynamic	175:181	arg1	O-GlcNAcylation					154:168	O-GlcNAcylation	154:168	O-GlcNAcylation	154:168	O-GlcNAcylation is a dynamic post-translational modification that has extensive crosstalk with phosphorylation either at the same or adjacent sites of various proteins.
26252736	10	45	theme	novel	1858:1862	arg1	target					1864:1869	a novel target	1856:1869	a novel target	1856:1869	Interfering levels of O-GlcNAcylation of PKM2 may be a novel target in controlling cancer metabolism and tumorigenesis of colorectal cancer.
26252736	10	45	theme	novel	1858:1862	arg1	levels					1815:1820	Interfering levels	1803:1820	Interfering levels of O-GlcNAcylation of PKM2	1803:1847	Interfering levels of O-GlcNAcylation of PKM2 may be a novel target in controlling cancer metabolism and tumorigenesis of colorectal cancer.
26252736	6	46	theme	global	1202:1207	arg1	O-GlcNAcylation					1209:1223	global O-GlcNAcylation	1202:1223	global O-GlcNAcylation	1202:1223	In addition, when global O-GlcNAcylation was enhanced by treating cells with Thiamet-G, PKM2 expression level was upregulated, but PKM2-specific activity was decreased.
26252736	0	47	theme	colorectal	129:138	arg1	cells					147:151	colorectal cancer cells	129:151	colorectal cancer cells	129:151	Alteration of O-GlcNAcylation affects serine phosphorylation and regulates gene expression and activity of pyruvate kinase M2 in colorectal cancer cells.
26252736	9	48	theme	PKM2	1773:1776	arg1	activity					1778:1785	PKM2 activity	1773:1785	PKM2 activity	1773:1785	These results suggested roles of O-GlcNAcylation in modulating serine phosphorylation, as well as in regulating PKM2 activity and expression.
26252736	0	49	from	activity	95:102	arg1	cells					147:151	colorectal cancer cells	129:151	colorectal cancer cells	129:151	Alteration of O-GlcNAcylation affects serine phosphorylation and regulates gene expression and activity of pyruvate kinase M2 in colorectal cancer cells.
26252736	7	50	theme	PKM2-specific	1441:1453	arg1	activity					1455:1462	PKM2-specific activity	1441:1462	PKM2-specific activity	1441:1462	On the other hand, in OGT knockdown cells, PKM2 expression level was downregulated, but PKM2-specific activity was increased.
26252736	8	51	contain	had	1536:1538	arg1	SW620					1529:1533	SW620	1529:1533	SW620	1529:1533	Moreover, the metastatic colorectal cancer cells, SW620, had more O-GlcNAc-PKM2 and showed lower PKM2-specific activity compared to the non-metastatic colorectal cancer SW480 cells.
26252736	8	51	contain	had	1536:1538	arg1	cells					1522:1526	the metastatic colorectal cancer cells	1489:1526	the metastatic colorectal cancer cells	1489:1526	Moreover, the metastatic colorectal cancer cells, SW620, had more O-GlcNAc-PKM2 and showed lower PKM2-specific activity compared to the non-metastatic colorectal cancer SW480 cells.
26252736	8	51	contain	had	1536:1538	arg2	O-GlcNAc-PKM2					1545:1557	more O-GlcNAc-PKM2	1540:1557	more O-GlcNAc-PKM2	1540:1557	Moreover, the metastatic colorectal cancer cells, SW620, had more O-GlcNAc-PKM2 and showed lower PKM2-specific activity compared to the non-metastatic colorectal cancer SW480 cells.
26252736	4	52	theme	spectrometric	670:682	arg1	analysis					684:691	Two-dimensional immunoblotting and mass spectrometric analysis	630:691	analysis	684:691	Two-dimensional immunoblotting and mass spectrometric analysis showed that the levels of O-GlcNAc and serine phosphorylation of many proteins including serine hydroxymethyltransferase, cytokeratin-8, pyruvate kinase M2 (PKM2), heterogeneous nuclear ribonucleoprotein L, and lamin-B1, were reduced in siOGT cells compared to siScramble cells.
26252736	10	53	theme	cancer	1886:1891	arg1	metabolism					1893:1902	cancer metabolism	1886:1902	cancer metabolism	1886:1902	Interfering levels of O-GlcNAcylation of PKM2 may be a novel target in controlling cancer metabolism and tumorigenesis of colorectal cancer.
26252736	8	54	theme	cancer	1515:1520	arg1	SW620					1529:1533	SW620	1529:1533	SW620	1529:1533	Moreover, the metastatic colorectal cancer cells, SW620, had more O-GlcNAc-PKM2 and showed lower PKM2-specific activity compared to the non-metastatic colorectal cancer SW480 cells.
26252736	8	54	theme	cancer	1515:1520	arg1	cells					1522:1526	the metastatic colorectal cancer cells	1489:1526	the metastatic colorectal cancer cells	1489:1526	Moreover, the metastatic colorectal cancer cells, SW620, had more O-GlcNAc-PKM2 and showed lower PKM2-specific activity compared to the non-metastatic colorectal cancer SW480 cells.
26252736	3	55	theme	colorectal	605:614	arg1	cells					623:627	colorectal cancer cells	605:627	colorectal cancer cells	605:627	Therefore, we explored crosstalk of the modifications by RNA interference against O-GlcNAc transferase (OGT) in colorectal cancer cells.
26252736	6	56	theme	PKM2	1272:1275	arg1	level					1288:1292	PKM2 expression level	1272:1292	PKM2 expression level	1272:1292	In addition, when global O-GlcNAcylation was enhanced by treating cells with Thiamet-G, PKM2 expression level was upregulated, but PKM2-specific activity was decreased.
26252736	4	57	theme	many	758:761	arg1	proteins					763:770	many proteins	758:770	many proteins including serine hydroxymethyltransferase, cytokeratin-8, pyruvate kinase M2 (PKM2), heterogeneous nuclear ribonucleoprotein L, and lamin-B1	758:911	Two-dimensional immunoblotting and mass spectrometric analysis showed that the levels of O-GlcNAc and serine phosphorylation of many proteins including serine hydroxymethyltransferase, cytokeratin-8, pyruvate kinase M2 (PKM2), heterogeneous nuclear ribonucleoprotein L, and lamin-B1, were reduced in siOGT cells compared to siScramble cells.
26252736	4	57	theme	many	758:761	arg1	lamin-B1					904:911	lamin-B1	904:911	lamin-B1	904:911	Two-dimensional immunoblotting and mass spectrometric analysis showed that the levels of O-GlcNAc and serine phosphorylation of many proteins including serine hydroxymethyltransferase, cytokeratin-8, pyruvate kinase M2 (PKM2), heterogeneous nuclear ribonucleoprotein L, and lamin-B1, were reduced in siOGT cells compared to siScramble cells.
26252736	4	57	theme	many	758:761	arg1	M2					846:847	pyruvate kinase M2	830:847	pyruvate kinase M2 (PKM2)	830:854	Two-dimensional immunoblotting and mass spectrometric analysis showed that the levels of O-GlcNAc and serine phosphorylation of many proteins including serine hydroxymethyltransferase, cytokeratin-8, pyruvate kinase M2 (PKM2), heterogeneous nuclear ribonucleoprotein L, and lamin-B1, were reduced in siOGT cells compared to siScramble cells.
26252736	4	57	theme	many	758:761	arg1	hydroxymethyltransferase					789:812	serine hydroxymethyltransferase	782:812	serine hydroxymethyltransferase	782:812	Two-dimensional immunoblotting and mass spectrometric analysis showed that the levels of O-GlcNAc and serine phosphorylation of many proteins including serine hydroxymethyltransferase, cytokeratin-8, pyruvate kinase M2 (PKM2), heterogeneous nuclear ribonucleoprotein L, and lamin-B1, were reduced in siOGT cells compared to siScramble cells.
26252736	4	57	theme	many	758:761	arg1	L					897:897	heterogeneous nuclear ribonucleoprotein L	857:897	heterogeneous nuclear ribonucleoprotein L	857:897	Two-dimensional immunoblotting and mass spectrometric analysis showed that the levels of O-GlcNAc and serine phosphorylation of many proteins including serine hydroxymethyltransferase, cytokeratin-8, pyruvate kinase M2 (PKM2), heterogeneous nuclear ribonucleoprotein L, and lamin-B1, were reduced in siOGT cells compared to siScramble cells.
26252736	4	57	theme	many	758:761	arg1	cytokeratin-8					815:827	cytokeratin-8	815:827	cytokeratin-8	815:827	Two-dimensional immunoblotting and mass spectrometric analysis showed that the levels of O-GlcNAc and serine phosphorylation of many proteins including serine hydroxymethyltransferase, cytokeratin-8, pyruvate kinase M2 (PKM2), heterogeneous nuclear ribonucleoprotein L, and lamin-B1, were reduced in siOGT cells compared to siScramble cells.
26252736	5	58	theme	HT29	975:978	arg1	cells					980:984	HT29 cells	975:984	HT29 cells	975:984	In HT29 cells, immunoprecipitated PKM2 revealed decreased O-GlcNAc and serine phosphorylation levels after siOGT knockdown, but increased levels after treatment with Thiamet-G, an inhibitor of O-GlcNAcase (OGA).
26252736	4	59	theme	siScramble	954:963	arg1	cells					965:969	siScramble cells	954:969	siScramble cells	954:969	Two-dimensional immunoblotting and mass spectrometric analysis showed that the levels of O-GlcNAc and serine phosphorylation of many proteins including serine hydroxymethyltransferase, cytokeratin-8, pyruvate kinase M2 (PKM2), heterogeneous nuclear ribonucleoprotein L, and lamin-B1, were reduced in siOGT cells compared to siScramble cells.
26252736	7	60	theme	expression	1401:1410	arg1	level					1412:1416	PKM2 expression level	1396:1416	PKM2 expression level	1396:1416	On the other hand, in OGT knockdown cells, PKM2 expression level was downregulated, but PKM2-specific activity was increased.
26252736	8	61	theme	more	1540:1543	arg1	O-GlcNAc-PKM2					1545:1557	more O-GlcNAc-PKM2	1540:1557	more O-GlcNAc-PKM2	1540:1557	Moreover, the metastatic colorectal cancer cells, SW620, had more O-GlcNAc-PKM2 and showed lower PKM2-specific activity compared to the non-metastatic colorectal cancer SW480 cells.
26252736	5	62	dep	revealed	1011:1018	arg1	decreased					1020:1028	decreased	1020:1028	decreased O-GlcNAc and serine phosphorylation levels after siOGT knockdown	1020:1093	In HT29 cells, immunoprecipitated PKM2 revealed decreased O-GlcNAc and serine phosphorylation levels after siOGT knockdown, but increased levels after treatment with Thiamet-G, an inhibitor of O-GlcNAcase (OGA).
26252736	5	62	dep	revealed	1011:1018	arg1	increased					1100:1108	increased	1100:1108	increased levels after treatment with Thiamet-G, an inhibitor of O-GlcNAcase (OGA)	1100:1181	In HT29 cells, immunoprecipitated PKM2 revealed decreased O-GlcNAc and serine phosphorylation levels after siOGT knockdown, but increased levels after treatment with Thiamet-G, an inhibitor of O-GlcNAcase (OGA).
26252736	8	63	theme	metastatic	1493:1502	arg1	SW620					1529:1533	SW620	1529:1533	SW620	1529:1533	Moreover, the metastatic colorectal cancer cells, SW620, had more O-GlcNAc-PKM2 and showed lower PKM2-specific activity compared to the non-metastatic colorectal cancer SW480 cells.
26252736	8	63	theme	metastatic	1493:1502	arg1	cells					1522:1526	the metastatic colorectal cancer cells	1489:1526	the metastatic colorectal cancer cells	1489:1526	Moreover, the metastatic colorectal cancer cells, SW620, had more O-GlcNAc-PKM2 and showed lower PKM2-specific activity compared to the non-metastatic colorectal cancer SW480 cells.
26252736	0	64	theme	pyruvate	107:114	arg1	M2					123:124	pyruvate kinase M2	107:124	pyruvate kinase M2	107:124	Alteration of O-GlcNAcylation affects serine phosphorylation and regulates gene expression and activity of pyruvate kinase M2 in colorectal cancer cells.
26252736	8	65	theme	lower	1570:1574	arg1	activity					1590:1597	lower PKM2-specific activity	1570:1597	lower PKM2-specific activity	1570:1597	Moreover, the metastatic colorectal cancer cells, SW620, had more O-GlcNAc-PKM2 and showed lower PKM2-specific activity compared to the non-metastatic colorectal cancer SW480 cells.
26252736	4	66	theme	pyruvate	830:837	arg1	PKM2					850:853	PKM2	850:853	PKM2	850:853	Two-dimensional immunoblotting and mass spectrometric analysis showed that the levels of O-GlcNAc and serine phosphorylation of many proteins including serine hydroxymethyltransferase, cytokeratin-8, pyruvate kinase M2 (PKM2), heterogeneous nuclear ribonucleoprotein L, and lamin-B1, were reduced in siOGT cells compared to siScramble cells.
26252736	4	66	theme	pyruvate	830:837	arg1	M2					846:847	pyruvate kinase M2	830:847	pyruvate kinase M2 (PKM2)	830:854	Two-dimensional immunoblotting and mass spectrometric analysis showed that the levels of O-GlcNAc and serine phosphorylation of many proteins including serine hydroxymethyltransferase, cytokeratin-8, pyruvate kinase M2 (PKM2), heterogeneous nuclear ribonucleoprotein L, and lamin-B1, were reduced in siOGT cells compared to siScramble cells.
26252736	5	67	with	treatment	1123:1131	arg1	Thiamet-G					1138:1146	Thiamet-G	1138:1146	Thiamet-G	1138:1146	In HT29 cells, immunoprecipitated PKM2 revealed decreased O-GlcNAc and serine phosphorylation levels after siOGT knockdown, but increased levels after treatment with Thiamet-G, an inhibitor of O-GlcNAcase (OGA).
26252736	5	67	with	treatment	1123:1131	arg1	inhibitor					1152:1160	an inhibitor	1149:1160	an inhibitor of O-GlcNAcase (OGA)	1149:1181	In HT29 cells, immunoprecipitated PKM2 revealed decreased O-GlcNAc and serine phosphorylation levels after siOGT knockdown, but increased levels after treatment with Thiamet-G, an inhibitor of O-GlcNAcase (OGA).
26252736	0	68	theme	M2	123:124	arg1	activity					95:102	activity	95:102	activity	95:102	Alteration of O-GlcNAcylation affects serine phosphorylation and regulates gene expression and activity of pyruvate kinase M2 in colorectal cancer cells.
26252736	0	68	theme	M2	123:124	arg1	expression					80:89	gene expression	75:89	gene expression	75:89	Alteration of O-GlcNAcylation affects serine phosphorylation and regulates gene expression and activity of pyruvate kinase M2 in colorectal cancer cells.
26252736	5	69	theme	O-GlcNAcase	1165:1175	arg1	Thiamet-G					1138:1146	Thiamet-G	1138:1146	Thiamet-G	1138:1146	In HT29 cells, immunoprecipitated PKM2 revealed decreased O-GlcNAc and serine phosphorylation levels after siOGT knockdown, but increased levels after treatment with Thiamet-G, an inhibitor of O-GlcNAcase (OGA).
26252736	5	69	theme	O-GlcNAcase	1165:1175	arg1	inhibitor					1152:1160	an inhibitor	1149:1160	an inhibitor of O-GlcNAcase (OGA)	1149:1181	In HT29 cells, immunoprecipitated PKM2 revealed decreased O-GlcNAc and serine phosphorylation levels after siOGT knockdown, but increased levels after treatment with Thiamet-G, an inhibitor of O-GlcNAcase (OGA).
26252736	7	70	theme	OGT	1375:1377	arg1	cells					1389:1393	OGT knockdown cells	1375:1393	OGT knockdown cells	1375:1393	On the other hand, in OGT knockdown cells, PKM2 expression level was downregulated, but PKM2-specific activity was increased.
26252736	2	71	theme	modifications	462:474	arg1	interplay					441:449	the interplay	437:449	the interplay of the two modifications	437:474	We have previously reported that O-GlcNAcylation level was increased in primary breast and colorectal cancer, but the interplay of the two modifications remains unclear.
26252736	1	72	theme	various	305:311	arg1	proteins					313:320	various proteins	305:320	various proteins	305:320	O-GlcNAcylation is a dynamic post-translational modification that has extensive crosstalk with phosphorylation either at the same or adjacent sites of various proteins.
26252736	1	73	with	crosstalk	234:242	arg1	phosphorylation					249:263	phosphorylation	249:263	phosphorylation	249:263	O-GlcNAcylation is a dynamic post-translational modification that has extensive crosstalk with phosphorylation either at the same or adjacent sites of various proteins.
26252736	7	74	theme	other	1360:1364	arg1	hand					1366:1369	the other hand	1356:1369	the other hand	1356:1369	On the other hand, in OGT knockdown cells, PKM2 expression level was downregulated, but PKM2-specific activity was increased.
26252736	8	75	theme	non-metastatic	1615:1628	arg1	cancer					1641:1646	non-metastatic colorectal cancer	1615:1646	the non-metastatic colorectal cancer SW480 cells	1611:1658	Moreover, the metastatic colorectal cancer cells, SW620, had more O-GlcNAc-PKM2 and showed lower PKM2-specific activity compared to the non-metastatic colorectal cancer SW480 cells.
26252736	8	76	theme	cancer	1641:1646	arg1	cells					1654:1658	the non-metastatic colorectal cancer SW480 cells	1611:1658	the non-metastatic colorectal cancer SW480 cells	1611:1658	Moreover, the metastatic colorectal cancer cells, SW620, had more O-GlcNAc-PKM2 and showed lower PKM2-specific activity compared to the non-metastatic colorectal cancer SW480 cells.
26252736	10	77	theme	cancer	1936:1941	arg1	tumorigenesis					1908:1920	tumorigenesis	1908:1920	tumorigenesis	1908:1920	Interfering levels of O-GlcNAcylation of PKM2 may be a novel target in controlling cancer metabolism and tumorigenesis of colorectal cancer.
26252736	10	77	theme	cancer	1936:1941	arg1	metabolism					1893:1902	cancer metabolism	1886:1902	cancer metabolism	1886:1902	Interfering levels of O-GlcNAcylation of PKM2 may be a novel target in controlling cancer metabolism and tumorigenesis of colorectal cancer.
26252736	4	78	theme	nuclear	871:877	arg1	ribonucleoprotein					879:895	heterogeneous nuclear ribonucleoprotein	857:895	heterogeneous nuclear ribonucleoprotein L	857:897	Two-dimensional immunoblotting and mass spectrometric analysis showed that the levels of O-GlcNAc and serine phosphorylation of many proteins including serine hydroxymethyltransferase, cytokeratin-8, pyruvate kinase M2 (PKM2), heterogeneous nuclear ribonucleoprotein L, and lamin-B1, were reduced in siOGT cells compared to siScramble cells.
26252736	2	79	theme	primary	395:401	arg1	breast					403:408	primary breast	395:408	primary breast	395:408	We have previously reported that O-GlcNAcylation level was increased in primary breast and colorectal cancer, but the interplay of the two modifications remains unclear.
26252736	1	80	dep	phosphorylation	249:263	arg1	either					265:270	either	265:270	either	265:270	O-GlcNAcylation is a dynamic post-translational modification that has extensive crosstalk with phosphorylation either at the same or adjacent sites of various proteins.
26252736	5	81	theme	phosphorylation	1050:1064	arg1	levels					1066:1071	O-GlcNAc and serine phosphorylation levels	1030:1071	O-GlcNAc and serine phosphorylation levels	1030:1071	In HT29 cells, immunoprecipitated PKM2 revealed decreased O-GlcNAc and serine phosphorylation levels after siOGT knockdown, but increased levels after treatment with Thiamet-G, an inhibitor of O-GlcNAcase (OGA).
26252736	3	82	theme	RNA	550:552	arg1	interference					554:565	RNA interference	550:565	RNA interference against O-GlcNAc transferase (OGT) in colorectal cancer cells	550:627	Therefore, we explored crosstalk of the modifications by RNA interference against O-GlcNAc transferase (OGT) in colorectal cancer cells.
26252736	9	83	theme	O-GlcNAcylation	1694:1708	arg1	roles					1685:1689	roles	1685:1689	roles of O-GlcNAcylation in modulating serine phosphorylation, as well as in regulating PKM2 activity and expression	1685:1800	These results suggested roles of O-GlcNAcylation in modulating serine phosphorylation, as well as in regulating PKM2 activity and expression.
26252736	4	84	theme	mass	665:668	arg1	analysis					684:691	Two-dimensional immunoblotting and mass spectrometric analysis	630:691	analysis	684:691	Two-dimensional immunoblotting and mass spectrometric analysis showed that the levels of O-GlcNAc and serine phosphorylation of many proteins including serine hydroxymethyltransferase, cytokeratin-8, pyruvate kinase M2 (PKM2), heterogeneous nuclear ribonucleoprotein L, and lamin-B1, were reduced in siOGT cells compared to siScramble cells.
26252736	10	85	theme	Interfering	1803:1813	arg1	target					1864:1869	a novel target	1856:1869	a novel target	1856:1869	Interfering levels of O-GlcNAcylation of PKM2 may be a novel target in controlling cancer metabolism and tumorigenesis of colorectal cancer.
26252736	10	85	theme	Interfering	1803:1813	arg1	levels					1815:1820	Interfering levels	1803:1820	Interfering levels of O-GlcNAcylation of PKM2	1803:1847	Interfering levels of O-GlcNAcylation of PKM2 may be a novel target in controlling cancer metabolism and tumorigenesis of colorectal cancer.
35931120	11	0	theme	EGF-dependent	1611:1623	arg1	phosphorylation					1630:1644	EGF-dependent Y976 phosphorylation	1611:1644	EGF-dependent Y976 phosphorylation	1611:1644	Together, we show EGF-dependent Y976 phosphorylation is critical for OGT-PKM2 interaction and propose that this posttranslational modification might be important for substrate selection by OGT.
35931120	7	1	theme	transferase	1110:1120	arg1	binding					1128:1134	O-GlcNAc transferase (OGT) binding	1101:1134	O-GlcNAc transferase (OGT) binding to PKM2	1101:1142	Here, we demonstrated that EGF promoted O-GlcNAc transferase (OGT) binding to PKM2 by stimulating OGT Y976 phosphorylation.
35931120	2	2	theme	multiple	359:366	arg1	cancer					399:404	lung cancer	394:404	lung cancer	394:404	Its receptor EGFR has been extensively explored as a therapeutic target against multiple types of cancers, such as lung cancer and glioblastoma.
35931120	2	2	theme	multiple	359:366	arg1	types					368:372	multiple types	359:372	multiple types	359:372	Its receptor EGFR has been extensively explored as a therapeutic target against multiple types of cancers, such as lung cancer and glioblastoma.
35931120	2	2	theme	multiple	359:366	arg1	glioblastoma					410:421	glioblastoma	410:421	glioblastoma	410:421	Its receptor EGFR has been extensively explored as a therapeutic target against multiple types of cancers, such as lung cancer and glioblastoma.
35931120	5	3	theme	PKM2	893:896	arg1	detetramerization					898:914	PKM2 detetramerization	893:914	PKM2 detetramerization	893:914	We previously showed that PKM2 T405/S406 O-GlcNAcylation, a critical mark important for PKM2 detetramerization and activity, was markedly upregulated by EGF.
35931120	7	4	theme	O-GlcNAc	1101:1108	arg1	OGT					1123:1125	OGT	1123:1125	OGT	1123:1125	Here, we demonstrated that EGF promoted O-GlcNAc transferase (OGT) binding to PKM2 by stimulating OGT Y976 phosphorylation.
35931120	7	4	theme	O-GlcNAc	1101:1108	arg1	transferase					1110:1120	O-GlcNAc transferase	1101:1120	O-GlcNAc transferase (OGT) binding to PKM2	1101:1142	Here, we demonstrated that EGF promoted O-GlcNAc transferase (OGT) binding to PKM2 by stimulating OGT Y976 phosphorylation.
35931120	9	5	from	PKM2	1349:1352	arg1	distinct					1335:1342	distinct	1335:1342	distinct	1335:1342	Moreover, distinct from PKM2, we observed that the association of additional phosphotyrosine-binding proteins with OGT was also enhanced when Y976 was phosphorylated.
35931120	9	6	theme	additional	1391:1400	arg1	proteins					1426:1433	additional phosphotyrosine-binding proteins	1391:1433	additional phosphotyrosine-binding proteins	1391:1433	Moreover, distinct from PKM2, we observed that the association of additional phosphotyrosine-binding proteins with OGT was also enhanced when Y976 was phosphorylated.
35931120	0	7	theme	subsequent	104:113	arg1	association					115:125	their subsequent association	98:125	their subsequent association	98:125	EGF promotes PKM2 O-GlcNAcylation by stimulating O-GlcNAc transferase phosphorylation at Y976 and their subsequent association.
35931120	3	8	theme	aerobic	555:561	arg1	glycolysis					563:572	aerobic glycolysis	555:572	aerobic glycolysis	555:572	Recent studies have established a connection between deregulated EGF signaling and metabolic reprogramming, especially rewiring in aerobic glycolysis, which is also known as the Warburg effect and recognized as a hallmark in cancer.
35931120	3	8	theme	aerobic	555:561	arg1	hallmark					637:644	a hallmark	635:644	a hallmark in cancer	635:654	Recent studies have established a connection between deregulated EGF signaling and metabolic reprogramming, especially rewiring in aerobic glycolysis, which is also known as the Warburg effect and recognized as a hallmark in cancer.
35931120	3	8	theme	aerobic	555:561	arg1	effect					610:615	the Warburg effect	598:615	the Warburg effect	598:615	Recent studies have established a connection between deregulated EGF signaling and metabolic reprogramming, especially rewiring in aerobic glycolysis, which is also known as the Warburg effect and recognized as a hallmark in cancer.
35931120	8	9	dep	found	1206:1210	arg1	upregulated					1260:1270	upregulated	1260:1270	upregulated	1260:1270	As a consequence, we found PKM2 O-GlcNAcylation and detetramerization were upregulated, leading to a significant decrease in PKM2 activity.
35931120	9	10	theme	phosphotyrosine-binding	1402:1424	arg1	proteins					1426:1433	additional phosphotyrosine-binding proteins	1391:1433	additional phosphotyrosine-binding proteins	1391:1433	Moreover, distinct from PKM2, we observed that the association of additional phosphotyrosine-binding proteins with OGT was also enhanced when Y976 was phosphorylated.
35931120	3	11	from	hallmark	637:644	arg1	cancer					649:654	cancer	649:654	cancer	649:654	Recent studies have established a connection between deregulated EGF signaling and metabolic reprogramming, especially rewiring in aerobic glycolysis, which is also known as the Warburg effect and recognized as a hallmark in cancer.
35931120	4	12	theme	glycolysis	739:748	arg1	step					731:734	the final step	721:734	the final step of glycolysis	721:748	Pyruvate kinase M2 (PKM2) is a rate-limiting enzyme controlling the final step of glycolysis and serves as a major regulator of the Warburg effect.
35931120	2	13	theme	receptor	283:290	arg1	EGFR					292:295	Its receptor EGFR	279:295	Its receptor EGFR	279:295	Its receptor EGFR has been extensively explored as a therapeutic target against multiple types of cancers, such as lung cancer and glioblastoma.
35931120	2	13	theme	receptor	283:290	arg1	target					344:349	a therapeutic target	330:349	a therapeutic target against multiple types of cancers, such as lung cancer and glioblastoma	330:421	Its receptor EGFR has been extensively explored as a therapeutic target against multiple types of cancers, such as lung cancer and glioblastoma.
35931120	9	14	theme	proteins	1426:1433	arg1	association					1376:1386	the association	1372:1386	the association of additional phosphotyrosine-binding proteins with OGT	1372:1442	Moreover, distinct from PKM2, we observed that the association of additional phosphotyrosine-binding proteins with OGT was also enhanced when Y976 was phosphorylated.
35931120	7	15	theme	Y976	1163:1166	arg1	phosphorylation					1168:1182	OGT Y976 phosphorylation	1159:1182	OGT Y976 phosphorylation	1159:1182	Here, we demonstrated that EGF promoted O-GlcNAc transferase (OGT) binding to PKM2 by stimulating OGT Y976 phosphorylation.
35931120	4	16	theme	rate-limiting	688:700	arg1	enzyme					702:707	a rate-limiting enzyme	686:707	a rate-limiting enzyme controlling the final step of glycolysis	686:748	Pyruvate kinase M2 (PKM2) is a rate-limiting enzyme controlling the final step of glycolysis and serves as a major regulator of the Warburg effect.
35931120	4	16	theme	rate-limiting	688:700	arg1	M2					673:674	Pyruvate kinase M2	657:674	Pyruvate kinase M2 (PKM2)	657:681	Pyruvate kinase M2 (PKM2) is a rate-limiting enzyme controlling the final step of glycolysis and serves as a major regulator of the Warburg effect.
35931120	4	17	theme	Pyruvate	657:664	arg1	regulator					772:780	a major regulator	764:780	a major regulator of the Warburg effect	764:802	Pyruvate kinase M2 (PKM2) is a rate-limiting enzyme controlling the final step of glycolysis and serves as a major regulator of the Warburg effect.
35931120	4	17	theme	Pyruvate	657:664	arg1	enzyme					702:707	a rate-limiting enzyme	686:707	a rate-limiting enzyme controlling the final step of glycolysis	686:748	Pyruvate kinase M2 (PKM2) is a rate-limiting enzyme controlling the final step of glycolysis and serves as a major regulator of the Warburg effect.
35931120	4	17	theme	Pyruvate	657:664	arg1	PKM2					677:680	PKM2	677:680	PKM2	677:680	Pyruvate kinase M2 (PKM2) is a rate-limiting enzyme controlling the final step of glycolysis and serves as a major regulator of the Warburg effect.
35931120	4	17	theme	Pyruvate	657:664	arg1	M2					673:674	Pyruvate kinase M2	657:674	Pyruvate kinase M2 (PKM2)	657:681	Pyruvate kinase M2 (PKM2) is a rate-limiting enzyme controlling the final step of glycolysis and serves as a major regulator of the Warburg effect.
35931120	11	18	theme	substrate	1759:1767	arg1	selection					1769:1777	substrate selection	1759:1777	substrate selection by OGT	1759:1784	Together, we show EGF-dependent Y976 phosphorylation is critical for OGT-PKM2 interaction and propose that this posttranslational modification might be important for substrate selection by OGT.
35931120	11	19	theme	Y976	1625:1628	arg1	phosphorylation					1630:1644	EGF-dependent Y976 phosphorylation	1611:1644	EGF-dependent Y976 phosphorylation	1611:1644	Together, we show EGF-dependent Y976 phosphorylation is critical for OGT-PKM2 interaction and propose that this posttranslational modification might be important for substrate selection by OGT.
35931120	5	20	theme	T405/S406	836:844	arg1	O-GlcNAcylation					846:860	PKM2 T405/S406 O-GlcNAcylation	831:860	PKM2 T405/S406 O-GlcNAcylation	831:860	We previously showed that PKM2 T405/S406 O-GlcNAcylation, a critical mark important for PKM2 detetramerization and activity, was markedly upregulated by EGF.
35931120	5	20	theme	T405/S406	836:844	arg1	critical					865:872	critical	865:872	critical	865:872	We previously showed that PKM2 T405/S406 O-GlcNAcylation, a critical mark important for PKM2 detetramerization and activity, was markedly upregulated by EGF.
35931120	11	21	theme	posttranslational	1705:1721	arg1	modification					1723:1734	this posttranslational modification	1700:1734	this posttranslational modification	1700:1734	Together, we show EGF-dependent Y976 phosphorylation is critical for OGT-PKM2 interaction and propose that this posttranslational modification might be important for substrate selection by OGT.
35931120	4	22	theme	final	725:729	arg1	step					731:734	the final step	721:734	the final step of glycolysis	721:748	Pyruvate kinase M2 (PKM2) is a rate-limiting enzyme controlling the final step of glycolysis and serves as a major regulator of the Warburg effect.
35931120	1	23	theme	most	172:175	arg1	factors					203:209	the most well-characterized growth factors	168:209	the most well-characterized growth factors	168:209	Epidermal growth factor (EGF) is one of the most well-characterized growth factors and plays a crucial role in cell proliferation and differentiation.
35931120	7	24	theme	OGT	1159:1161	arg1	phosphorylation					1168:1182	OGT Y976 phosphorylation	1159:1182	OGT Y976 phosphorylation	1159:1182	Here, we demonstrated that EGF promoted O-GlcNAc transferase (OGT) binding to PKM2 by stimulating OGT Y976 phosphorylation.
35931120	8	25	theme	PKM2	1212:1215	arg1	O-GlcNAcylation					1217:1231	PKM2 O-GlcNAcylation	1212:1231	PKM2 O-GlcNAcylation	1212:1231	As a consequence, we found PKM2 O-GlcNAcylation and detetramerization were upregulated, leading to a significant decrease in PKM2 activity.
35931120	8	25	theme	PKM2	1212:1215	arg1	consequence					1190:1200	a consequence	1188:1200	a consequence	1188:1200	As a consequence, we found PKM2 O-GlcNAcylation and detetramerization were upregulated, leading to a significant decrease in PKM2 activity.
35931120	8	25	theme	PKM2	1212:1215	arg1	detetramerization					1237:1253	detetramerization	1237:1253	detetramerization	1237:1253	As a consequence, we found PKM2 O-GlcNAcylation and detetramerization were upregulated, leading to a significant decrease in PKM2 activity.
35931120	2	26	theme	cancers	377:383	arg1	cancer					399:404	lung cancer	394:404	lung cancer	394:404	Its receptor EGFR has been extensively explored as a therapeutic target against multiple types of cancers, such as lung cancer and glioblastoma.
35931120	2	26	theme	cancers	377:383	arg1	types					368:372	multiple types	359:372	multiple types	359:372	Its receptor EGFR has been extensively explored as a therapeutic target against multiple types of cancers, such as lung cancer and glioblastoma.
35931120	2	26	theme	cancers	377:383	arg1	glioblastoma					410:421	glioblastoma	410:421	glioblastoma	410:421	Its receptor EGFR has been extensively explored as a therapeutic target against multiple types of cancers, such as lung cancer and glioblastoma.
35931120	8	27	theme	significant	1286:1296	arg1	decrease					1298:1305	a significant decrease	1284:1305	a significant decrease in PKM2 activity	1284:1322	As a consequence, we found PKM2 O-GlcNAcylation and detetramerization were upregulated, leading to a significant decrease in PKM2 activity.
35931120	8	28	from	decrease	1298:1305	arg1	activity					1315:1322	PKM2 activity	1310:1322	PKM2 activity	1310:1322	As a consequence, we found PKM2 O-GlcNAcylation and detetramerization were upregulated, leading to a significant decrease in PKM2 activity.
35931120	8	29	theme	PKM2	1310:1313	arg1	activity					1315:1322	PKM2 activity	1310:1322	PKM2 activity	1310:1322	As a consequence, we found PKM2 O-GlcNAcylation and detetramerization were upregulated, leading to a significant decrease in PKM2 activity.
35931120	1	30	theme	growth	196:201	arg1	factors					203:209	the most well-characterized growth factors	168:209	the most well-characterized growth factors	168:209	Epidermal growth factor (EGF) is one of the most well-characterized growth factors and plays a crucial role in cell proliferation and differentiation.
35931120	0	31	theme	PKM2	13:16	arg1	O-GlcNAcylation					18:32	PKM2 O-GlcNAcylation	13:32	PKM2 O-GlcNAcylation	13:32	EGF promotes PKM2 O-GlcNAcylation by stimulating O-GlcNAc transferase phosphorylation at Y976 and their subsequent association.
35931120	5	32	dep	critical	865:872	arg1	mark					874:877	mark	874:877	mark important for PKM2 detetramerization and activity	874:927	We previously showed that PKM2 T405/S406 O-GlcNAcylation, a critical mark important for PKM2 detetramerization and activity, was markedly upregulated by EGF.
35931120	1	33	theme	factors	203:209	arg1	factors					203:209	the most well-characterized growth factors	168:209	the most well-characterized growth factors	168:209	Epidermal growth factor (EGF) is one of the most well-characterized growth factors and plays a crucial role in cell proliferation and differentiation.
35931120	1	33	theme	factors	203:209	arg1	one					161:163	one	161:163	one	161:163	Epidermal growth factor (EGF) is one of the most well-characterized growth factors and plays a crucial role in cell proliferation and differentiation.
35931120	3	34	theme	metabolic	507:515	arg1	reprogramming					517:529	metabolic reprogramming	507:529	metabolic reprogramming	507:529	Recent studies have established a connection between deregulated EGF signaling and metabolic reprogramming, especially rewiring in aerobic glycolysis, which is also known as the Warburg effect and recognized as a hallmark in cancer.
35931120	2	35	theme	therapeutic	332:342	arg1	EGFR					292:295	Its receptor EGFR	279:295	Its receptor EGFR	279:295	Its receptor EGFR has been extensively explored as a therapeutic target against multiple types of cancers, such as lung cancer and glioblastoma.
35931120	2	35	theme	therapeutic	332:342	arg1	target					344:349	a therapeutic target	330:349	a therapeutic target against multiple types of cancers, such as lung cancer and glioblastoma	330:421	Its receptor EGFR has been extensively explored as a therapeutic target against multiple types of cancers, such as lung cancer and glioblastoma.
35931120	0	36	from	Y976	89:92	arg1	phosphorylation					70:84	O-GlcNAc transferase phosphorylation	49:84	O-GlcNAc transferase phosphorylation at Y976	49:92	EGF promotes PKM2 O-GlcNAcylation by stimulating O-GlcNAc transferase phosphorylation at Y976 and their subsequent association.
35931120	0	36	from	Y976	89:92	arg1	association					115:125	their subsequent association	98:125	their subsequent association	98:125	EGF promotes PKM2 O-GlcNAcylation by stimulating O-GlcNAc transferase phosphorylation at Y976 and their subsequent association.
35931120	4	37	theme	Warburg	789:795	arg1	effect					797:802	the Warburg effect	785:802	the Warburg effect	785:802	Pyruvate kinase M2 (PKM2) is a rate-limiting enzyme controlling the final step of glycolysis and serves as a major regulator of the Warburg effect.
35931120	3	38	theme	Recent	424:429	arg1	studies					431:437	Recent studies	424:437	Recent studies	424:437	Recent studies have established a connection between deregulated EGF signaling and metabolic reprogramming, especially rewiring in aerobic glycolysis, which is also known as the Warburg effect and recognized as a hallmark in cancer.
35931120	5	39	theme	PKM2	831:834	arg1	O-GlcNAcylation					846:860	PKM2 T405/S406 O-GlcNAcylation	831:860	PKM2 T405/S406 O-GlcNAcylation	831:860	We previously showed that PKM2 T405/S406 O-GlcNAcylation, a critical mark important for PKM2 detetramerization and activity, was markedly upregulated by EGF.
35931120	5	39	theme	PKM2	831:834	arg1	critical					865:872	critical	865:872	critical	865:872	We previously showed that PKM2 T405/S406 O-GlcNAcylation, a critical mark important for PKM2 detetramerization and activity, was markedly upregulated by EGF.
35931120	3	40	theme	Warburg	602:608	arg1	glycolysis					563:572	aerobic glycolysis	555:572	aerobic glycolysis	555:572	Recent studies have established a connection between deregulated EGF signaling and metabolic reprogramming, especially rewiring in aerobic glycolysis, which is also known as the Warburg effect and recognized as a hallmark in cancer.
35931120	3	40	theme	Warburg	602:608	arg1	effect					610:615	the Warburg effect	598:615	the Warburg effect	598:615	Recent studies have established a connection between deregulated EGF signaling and metabolic reprogramming, especially rewiring in aerobic glycolysis, which is also known as the Warburg effect and recognized as a hallmark in cancer.
35931120	2	41	theme	lung	394:397	arg1	cancer					399:404	lung cancer	394:404	lung cancer	394:404	Its receptor EGFR has been extensively explored as a therapeutic target against multiple types of cancers, such as lung cancer and glioblastoma.
35931120	0	42	theme	transferase	58:68	arg1	phosphorylation					70:84	O-GlcNAc transferase phosphorylation	49:84	O-GlcNAc transferase phosphorylation at Y976	49:92	EGF promotes PKM2 O-GlcNAcylation by stimulating O-GlcNAc transferase phosphorylation at Y976 and their subsequent association.
35931120	11	43	theme	OGT-PKM2	1662:1669	arg1	interaction					1671:1681	OGT-PKM2 interaction	1662:1681	OGT-PKM2 interaction	1662:1681	Together, we show EGF-dependent Y976 phosphorylation is critical for OGT-PKM2 interaction and propose that this posttranslational modification might be important for substrate selection by OGT.
35931120	1	44	theme	well-characterized	177:194	arg1	factors					203:209	the most well-characterized growth factors	168:209	the most well-characterized growth factors	168:209	Epidermal growth factor (EGF) is one of the most well-characterized growth factors and plays a crucial role in cell proliferation and differentiation.
35931120	1	45	theme	Epidermal	128:136	arg1	factor					145:150	Epidermal growth factor	128:150	Epidermal growth factor (EGF)	128:156	Epidermal growth factor (EGF) is one of the most well-characterized growth factors and plays a crucial role in cell proliferation and differentiation.
35931120	1	45	theme	Epidermal	128:136	arg1	EGF					153:155	EGF	153:155	EGF	153:155	Epidermal growth factor (EGF) is one of the most well-characterized growth factors and plays a crucial role in cell proliferation and differentiation.
35931120	0	46	theme	O-GlcNAc	49:56	arg1	phosphorylation					70:84	O-GlcNAc transferase phosphorylation	49:84	O-GlcNAc transferase phosphorylation at Y976	49:92	EGF promotes PKM2 O-GlcNAcylation by stimulating O-GlcNAc transferase phosphorylation at Y976 and their subsequent association.
35931120	4	47	theme	effect	797:802	arg1	regulator					772:780	a major regulator	764:780	a major regulator of the Warburg effect	764:802	Pyruvate kinase M2 (PKM2) is a rate-limiting enzyme controlling the final step of glycolysis and serves as a major regulator of the Warburg effect.
35931120	4	47	theme	effect	797:802	arg1	M2					673:674	Pyruvate kinase M2	657:674	Pyruvate kinase M2 (PKM2)	657:681	Pyruvate kinase M2 (PKM2) is a rate-limiting enzyme controlling the final step of glycolysis and serves as a major regulator of the Warburg effect.
35931120	1	48	theme	growth	138:143	arg1	factor					145:150	Epidermal growth factor	128:150	Epidermal growth factor (EGF)	128:156	Epidermal growth factor (EGF) is one of the most well-characterized growth factors and plays a crucial role in cell proliferation and differentiation.
35931120	1	48	theme	growth	138:143	arg1	EGF					153:155	EGF	153:155	EGF	153:155	Epidermal growth factor (EGF) is one of the most well-characterized growth factors and plays a crucial role in cell proliferation and differentiation.
35931120	4	49	theme	kinase	666:671	arg1	regulator					772:780	a major regulator	764:780	a major regulator of the Warburg effect	764:802	Pyruvate kinase M2 (PKM2) is a rate-limiting enzyme controlling the final step of glycolysis and serves as a major regulator of the Warburg effect.
35931120	4	49	theme	kinase	666:671	arg1	enzyme					702:707	a rate-limiting enzyme	686:707	a rate-limiting enzyme controlling the final step of glycolysis	686:748	Pyruvate kinase M2 (PKM2) is a rate-limiting enzyme controlling the final step of glycolysis and serves as a major regulator of the Warburg effect.
35931120	4	49	theme	kinase	666:671	arg1	PKM2					677:680	PKM2	677:680	PKM2	677:680	Pyruvate kinase M2 (PKM2) is a rate-limiting enzyme controlling the final step of glycolysis and serves as a major regulator of the Warburg effect.
35931120	4	49	theme	kinase	666:671	arg1	M2					673:674	Pyruvate kinase M2	657:674	Pyruvate kinase M2 (PKM2)	657:681	Pyruvate kinase M2 (PKM2) is a rate-limiting enzyme controlling the final step of glycolysis and serves as a major regulator of the Warburg effect.
35931120	4	50	theme	major	766:770	arg1	regulator					772:780	a major regulator	764:780	a major regulator of the Warburg effect	764:802	Pyruvate kinase M2 (PKM2) is a rate-limiting enzyme controlling the final step of glycolysis and serves as a major regulator of the Warburg effect.
35931120	4	50	theme	major	766:770	arg1	M2					673:674	Pyruvate kinase M2	657:674	Pyruvate kinase M2 (PKM2)	657:681	Pyruvate kinase M2 (PKM2) is a rate-limiting enzyme controlling the final step of glycolysis and serves as a major regulator of the Warburg effect.
35931120	3	51	theme	deregulated	477:487	arg1	signaling					493:501	deregulated EGF signaling	477:501	deregulated EGF signaling	477:501	Recent studies have established a connection between deregulated EGF signaling and metabolic reprogramming, especially rewiring in aerobic glycolysis, which is also known as the Warburg effect and recognized as a hallmark in cancer.
35931120	1	52	dep	cell	239:242	arg1	proliferation					244:256	proliferation	244:256	proliferation	244:256	Epidermal growth factor (EGF) is one of the most well-characterized growth factors and plays a crucial role in cell proliferation and differentiation.
35931120	1	52	dep	cell	239:242	arg1	differentiation					262:276	differentiation	262:276	differentiation	262:276	Epidermal growth factor (EGF) is one of the most well-characterized growth factors and plays a crucial role in cell proliferation and differentiation.
35931120	3	53	theme	EGF	489:491	arg1	signaling					493:501	deregulated EGF signaling	477:501	deregulated EGF signaling	477:501	Recent studies have established a connection between deregulated EGF signaling and metabolic reprogramming, especially rewiring in aerobic glycolysis, which is also known as the Warburg effect and recognized as a hallmark in cancer.
35931120	1	54	theme	crucial	223:229	arg1	role					231:234	a crucial role	221:234	a crucial role	221:234	Epidermal growth factor (EGF) is one of the most well-characterized growth factors and plays a crucial role in cell proliferation and differentiation.
35931120	6	55	theme	PKM2	1009:1012	arg1	O-GlcNAcylation					1014:1028	PKM2 O-GlcNAcylation	1009:1028	PKM2 O-GlcNAcylation	1009:1028	However, the mechanism by which EGF regulates PKM2 O-GlcNAcylation still remains uncharacterized.
35931120	9	56	with	association	1376:1386	arg1	OGT					1440:1442	OGT	1440:1442	OGT	1440:1442	Moreover, distinct from PKM2, we observed that the association of additional phosphotyrosine-binding proteins with OGT was also enhanced when Y976 was phosphorylated.
23110217	4	0	with	inhibitors	779:788	arg1	Thiamet-G					752:760	Thiamet-G	752:760	Thiamet-G	752:760	We increased the O-GlcNAcylation level on soleus biopsies performing an organ culture of soleus treated or not with PUGNAc or Thiamet-G, two O-GlcNAcase inhibitors.
23110217	4	0	with	inhibitors	779:788	arg1	PUGNAc					742:747	PUGNAc	742:747	PUGNAc	742:747	We increased the O-GlcNAcylation level on soleus biopsies performing an organ culture of soleus treated or not with PUGNAc or Thiamet-G, two O-GlcNAcase inhibitors.
23110217	8	1	theme	O-GlcNAc	1251:1258	arg1	level					1260:1264	O-GlcNAc level	1251:1264	O-GlcNAc level	1251:1264	We quantified the variation of O-GlcNAc level on all these identified proteins, and showed that several regulatory contractile proteins, predominantly fast isoforms, presented a drastic increase in their O-GlcNAc level.
23110217	2	2	from	particular	370:379	arg1	properties					396:405	contractile properties	384:405	contractile properties such as the calcium activation parameters	384:447	New insights suggest that O-GlcNAcylation might be involved in striated muscle physiology, in particular in contractile properties such as the calcium activation parameters.
23110217	2	2	from	particular	370:379	arg1	parameters					438:447	the calcium activation parameters	415:447	the calcium activation parameters	415:447	New insights suggest that O-GlcNAcylation might be involved in striated muscle physiology, in particular in contractile properties such as the calcium activation parameters.
23110217	4	3	theme	soleus	668:673	arg1	biopsies					675:682	soleus biopsies	668:682	soleus biopsies performing an organ culture of soleus treated or not with PUGNAc or Thiamet-G, two O-GlcNAcase inhibitors	668:788	We increased the O-GlcNAcylation level on soleus biopsies performing an organ culture of soleus treated or not with PUGNAc or Thiamet-G, two O-GlcNAcase inhibitors.
23110217	10	4	theme	contractile	1854:1864	arg1	activity					1866:1873	contractile activity	1854:1873	contractile activity of skeletal muscle	1854:1892	All these data strongly linked O-GlcNAcylation to the modulation of contractile activity of skeletal muscle.
23110217	9	5	theme	level	1526:1530	arg1	increase					1505:1512	an increase	1502:1512	an increase of O-GlcNAc level	1502:1530	Since the only slow isoform of contractile protein presenting an increase of O-GlcNAc level was MLC2, the effect of enhanced O-GlcNAcylation pattern on calcium activation parameters could involve the O-GlcNAcylation of sMLC2, without excluding that an unidentified O-GlcNAc proteins, such as TnC, could be potentially involved in this mechanism.
23110217	8	6	theme	regulatory	1324:1333	arg1	proteins					1347:1354	several regulatory contractile proteins	1316:1354	several regulatory contractile proteins	1316:1354	We quantified the variation of O-GlcNAc level on all these identified proteins, and showed that several regulatory contractile proteins, predominantly fast isoforms, presented a drastic increase in their O-GlcNAc level.
23110217	8	6	theme	regulatory	1324:1333	arg1	isoforms					1376:1383	predominantly fast isoforms	1357:1383	predominantly fast isoforms	1357:1383	We quantified the variation of O-GlcNAc level on all these identified proteins, and showed that several regulatory contractile proteins, predominantly fast isoforms, presented a drastic increase in their O-GlcNAc level.
23110217	0	7	theme	Increasing	0:9	arg1	level					27:31	Increasing O-GlcNAcylation level	0:31	Increasing O-GlcNAcylation level on organ culture of soleus	0:58	Increasing O-GlcNAcylation level on organ culture of soleus modulates the calcium activation parameters of muscle fibers.
23110217	10	8	theme	muscle	1887:1892	arg1	activity					1866:1873	contractile activity	1854:1873	contractile activity of skeletal muscle	1854:1892	All these data strongly linked O-GlcNAcylation to the modulation of contractile activity of skeletal muscle.
23110217	7	9	theme	troponin	1175:1182	arg1	T					1184:1184	troponin T	1175:1184	troponin T	1175:1184	We also characterized the O-GlcNAcylated contractile proteins using a proteomic approach, and identified among others troponin T and I as being O-GlcNAc modified.
23110217	7	9	theme	troponin	1175:1182	arg1	others					1168:1173	others troponin T and I	1168:1190	others troponin T and I	1168:1190	We also characterized the O-GlcNAcylated contractile proteins using a proteomic approach, and identified among others troponin T and I as being O-GlcNAc modified.
23110217	2	10	theme	muscle	348:353	arg1	physiology					355:364	striated muscle physiology	339:364	striated muscle physiology	339:364	New insights suggest that O-GlcNAcylation might be involved in striated muscle physiology, in particular in contractile properties such as the calcium activation parameters.
23110217	1	11	theme	regulated	234:242	arg1	interplay					244:252	a dynamic and highly regulated interplay	213:252	a dynamic and highly regulated interplay with phosphorylation	213:273	O-N-acetylglucosaminylation is a reversible post-translational modification which presents a dynamic and highly regulated interplay with phosphorylation.
23110217	6	12	theme	skinned	1039:1045	arg1	biopsies					1047:1054	skinned biopsies	1039:1054	skinned biopsies	1039:1054	Analysis of the glycoproteins pattern showed that this effect is solely due to O-GlcNAcylation of proteins extracted from skinned biopsies.
23110217	2	13	theme	New	276:278	arg1	insights					280:287	New insights	276:287	New insights	276:287	New insights suggest that O-GlcNAcylation might be involved in striated muscle physiology, in particular in contractile properties such as the calcium activation parameters.
23110217	9	14	theme	O-GlcNAcylation	1565:1579	arg1	pattern					1581:1587	enhanced O-GlcNAcylation pattern	1556:1587	enhanced O-GlcNAcylation pattern	1556:1587	Since the only slow isoform of contractile protein presenting an increase of O-GlcNAc level was MLC2, the effect of enhanced O-GlcNAcylation pattern on calcium activation parameters could involve the O-GlcNAcylation of sMLC2, without excluding that an unidentified O-GlcNAc proteins, such as TnC, could be potentially involved in this mechanism.
23110217	7	15	theme	contractile	1098:1108	arg1	proteins					1110:1117	the O-GlcNAcylated contractile proteins	1079:1117	the O-GlcNAcylated contractile proteins	1079:1117	We also characterized the O-GlcNAcylated contractile proteins using a proteomic approach, and identified among others troponin T and I as being O-GlcNAc modified.
23110217	8	16	theme	drastic	1398:1404	arg1	increase					1406:1413	a drastic increase	1396:1413	a drastic increase in their O-GlcNAc level	1396:1437	We quantified the variation of O-GlcNAc level on all these identified proteins, and showed that several regulatory contractile proteins, predominantly fast isoforms, presented a drastic increase in their O-GlcNAc level.
23110217	2	17	theme	striated	339:346	arg1	physiology					355:364	striated muscle physiology	339:364	striated muscle physiology	339:364	New insights suggest that O-GlcNAcylation might be involved in striated muscle physiology, in particular in contractile properties such as the calcium activation parameters.
23110217	9	18	theme	activation	1600:1609	arg1	parameters					1611:1620	calcium activation parameters	1592:1620	calcium activation parameters	1592:1620	Since the only slow isoform of contractile protein presenting an increase of O-GlcNAc level was MLC2, the effect of enhanced O-GlcNAcylation pattern on calcium activation parameters could involve the O-GlcNAcylation of sMLC2, without excluding that an unidentified O-GlcNAc proteins, such as TnC, could be potentially involved in this mechanism.
23110217	3	19	theme	T/pCa	605:609	arg1	relationships					611:623	T/pCa relationships	605:623	T/pCa relationships	605:623	By the inhibition of O-GlcNAcase, we investigated the effect of the increase of soleus O-GlcNAcylation level on the contractile properties by establishing T/pCa relationships.
23110217	1	20	theme	post-translational	166:183	arg1	modification					185:196	a reversible post-translational modification	153:196	a reversible post-translational modification which presents a dynamic and highly regulated interplay with phosphorylation	153:273	O-N-acetylglucosaminylation is a reversible post-translational modification which presents a dynamic and highly regulated interplay with phosphorylation.
23110217	1	20	theme	post-translational	166:183	arg1	O-N-acetylglucosaminylation					122:148	O-N-acetylglucosaminylation	122:148	O-N-acetylglucosaminylation	122:148	O-N-acetylglucosaminylation is a reversible post-translational modification which presents a dynamic and highly regulated interplay with phosphorylation.
23110217	0	21	from	level	27:31	arg1	culture					42:48	organ culture	36:48	organ culture of soleus	36:58	Increasing O-GlcNAcylation level on organ culture of soleus modulates the calcium activation parameters of muscle fibers.
23110217	8	22	theme	O-GlcNAc	1424:1431	arg1	level					1433:1437	their O-GlcNAc level	1418:1437	their O-GlcNAc level	1418:1437	We quantified the variation of O-GlcNAc level on all these identified proteins, and showed that several regulatory contractile proteins, predominantly fast isoforms, presented a drastic increase in their O-GlcNAc level.
23110217	0	23	theme	calcium	74:80	arg1	parameters					93:102	the calcium activation parameters	70:102	the calcium activation parameters of muscle fibers	70:119	Increasing O-GlcNAcylation level on organ culture of soleus modulates the calcium activation parameters of muscle fibers.
23110217	5	24	from	increase	857:864	arg1	fibers					909:914	slow soleus skinned fibers	889:914	slow soleus skinned fibers	889:914	The enhancement of O-GlcNAcylation pattern was associated with an increase of calcium affinity on slow soleus skinned fibers.
23110217	5	25	theme	pattern	826:832	arg1	enhancement					795:805	The enhancement	791:805	The enhancement of O-GlcNAcylation pattern	791:832	The enhancement of O-GlcNAcylation pattern was associated with an increase of calcium affinity on slow soleus skinned fibers.
23110217	5	26	theme	slow	889:892	arg1	fibers					909:914	slow soleus skinned fibers	889:914	slow soleus skinned fibers	889:914	The enhancement of O-GlcNAcylation pattern was associated with an increase of calcium affinity on slow soleus skinned fibers.
23110217	5	27	theme	skinned	901:907	arg1	fibers					909:914	slow soleus skinned fibers	889:914	slow soleus skinned fibers	889:914	The enhancement of O-GlcNAcylation pattern was associated with an increase of calcium affinity on slow soleus skinned fibers.
23110217	8	28	from	variation	1238:1246	arg1	proteins					1290:1297	all these identified proteins	1269:1297	all these identified proteins	1269:1297	We quantified the variation of O-GlcNAc level on all these identified proteins, and showed that several regulatory contractile proteins, predominantly fast isoforms, presented a drastic increase in their O-GlcNAc level.
23110217	10	29	attach	linked	1810:1815	arg1	modulation					1840:1849	the modulation	1836:1849	the modulation of contractile activity of skeletal muscle	1836:1892	All these data strongly linked O-GlcNAcylation to the modulation of contractile activity of skeletal muscle.
23110217	10	29	attach	linked	1810:1815	arg2	data					1796:1799	All these data	1786:1799	All these data	1786:1799	All these data strongly linked O-GlcNAcylation to the modulation of contractile activity of skeletal muscle.
23110217	6	30	gly	glycoproteins	933:945	arg1	glycoproteins					933:945	the glycoproteins pattern	929:953	the glycoproteins pattern	929:953	Analysis of the glycoproteins pattern showed that this effect is solely due to O-GlcNAcylation of proteins extracted from skinned biopsies.
23110217	0	31	theme	organ	36:40	arg1	culture					42:48	organ culture	36:48	organ culture of soleus	36:58	Increasing O-GlcNAcylation level on organ culture of soleus modulates the calcium activation parameters of muscle fibers.
23110217	9	32	theme	only	1450:1453	arg1	isoform					1460:1466	the only slow isoform	1446:1466	the only slow isoform of contractile protein presenting an increase of O-GlcNAc level	1446:1530	Since the only slow isoform of contractile protein presenting an increase of O-GlcNAc level was MLC2, the effect of enhanced O-GlcNAcylation pattern on calcium activation parameters could involve the O-GlcNAcylation of sMLC2, without excluding that an unidentified O-GlcNAc proteins, such as TnC, could be potentially involved in this mechanism.
23110217	9	32	theme	only	1450:1453	arg1	MLC2					1536:1539	MLC2	1536:1539	MLC2	1536:1539	Since the only slow isoform of contractile protein presenting an increase of O-GlcNAc level was MLC2, the effect of enhanced O-GlcNAcylation pattern on calcium activation parameters could involve the O-GlcNAcylation of sMLC2, without excluding that an unidentified O-GlcNAc proteins, such as TnC, could be potentially involved in this mechanism.
23110217	6	33	theme	glycoproteins	933:945	arg1	pattern					947:953	the glycoproteins pattern	929:953	the glycoproteins pattern	929:953	Analysis of the glycoproteins pattern showed that this effect is solely due to O-GlcNAcylation of proteins extracted from skinned biopsies.
23110217	9	34	theme	O-GlcNAc	1705:1712	arg1	proteins					1714:1721	an unidentified O-GlcNAc proteins	1689:1721	an unidentified O-GlcNAc proteins	1689:1721	Since the only slow isoform of contractile protein presenting an increase of O-GlcNAc level was MLC2, the effect of enhanced O-GlcNAcylation pattern on calcium activation parameters could involve the O-GlcNAcylation of sMLC2, without excluding that an unidentified O-GlcNAc proteins, such as TnC, could be potentially involved in this mechanism.
23110217	9	34	theme	O-GlcNAc	1705:1712	arg1	TnC					1732:1734	TnC	1732:1734	TnC	1732:1734	Since the only slow isoform of contractile protein presenting an increase of O-GlcNAc level was MLC2, the effect of enhanced O-GlcNAcylation pattern on calcium activation parameters could involve the O-GlcNAcylation of sMLC2, without excluding that an unidentified O-GlcNAc proteins, such as TnC, could be potentially involved in this mechanism.
23110217	3	35	theme	O-GlcNAcylation	537:551	arg1	level					553:557	soleus O-GlcNAcylation level	530:557	soleus O-GlcNAcylation level	530:557	By the inhibition of O-GlcNAcase, we investigated the effect of the increase of soleus O-GlcNAcylation level on the contractile properties by establishing T/pCa relationships.
23110217	5	36	theme	affinity	877:884	arg1	increase					857:864	an increase	854:864	an increase of calcium affinity on slow soleus skinned fibers	854:914	The enhancement of O-GlcNAcylation pattern was associated with an increase of calcium affinity on slow soleus skinned fibers.
23110217	9	37	from	effect	1546:1551	arg1	parameters					1611:1620	calcium activation parameters	1592:1620	calcium activation parameters	1592:1620	Since the only slow isoform of contractile protein presenting an increase of O-GlcNAc level was MLC2, the effect of enhanced O-GlcNAcylation pattern on calcium activation parameters could involve the O-GlcNAcylation of sMLC2, without excluding that an unidentified O-GlcNAc proteins, such as TnC, could be potentially involved in this mechanism.
23110217	9	38	theme	contractile	1471:1481	arg1	protein					1483:1489	contractile protein	1471:1489	contractile protein presenting an increase of O-GlcNAc level	1471:1530	Since the only slow isoform of contractile protein presenting an increase of O-GlcNAc level was MLC2, the effect of enhanced O-GlcNAcylation pattern on calcium activation parameters could involve the O-GlcNAcylation of sMLC2, without excluding that an unidentified O-GlcNAc proteins, such as TnC, could be potentially involved in this mechanism.
23110217	3	39	theme	contractile	566:576	arg1	properties					578:587	the contractile properties	562:587	the contractile properties	562:587	By the inhibition of O-GlcNAcase, we investigated the effect of the increase of soleus O-GlcNAcylation level on the contractile properties by establishing T/pCa relationships.
23110217	5	40	theme	calcium	869:875	arg1	affinity					877:884	calcium affinity	869:884	calcium affinity	869:884	The enhancement of O-GlcNAcylation pattern was associated with an increase of calcium affinity on slow soleus skinned fibers.
23110217	7	41	dep	others	1168:1173	arg1	I					1190:1190	I	1190:1190	I	1190:1190	We also characterized the O-GlcNAcylated contractile proteins using a proteomic approach, and identified among others troponin T and I as being O-GlcNAc modified.
23110217	7	41	dep	others	1168:1173	arg1	T					1184:1184	troponin T	1175:1184	troponin T	1175:1184	We also characterized the O-GlcNAcylated contractile proteins using a proteomic approach, and identified among others troponin T and I as being O-GlcNAc modified.
23110217	7	41	dep	others	1168:1173	arg1	others					1168:1173	others troponin T and I	1168:1190	others troponin T and I	1168:1190	We also characterized the O-GlcNAcylated contractile proteins using a proteomic approach, and identified among others troponin T and I as being O-GlcNAc modified.
23110217	4	42	theme	O-GlcNAcylation	643:657	arg1	level					659:663	the O-GlcNAcylation level	639:663	the O-GlcNAcylation level on soleus biopsies performing an organ culture of soleus treated or not with PUGNAc or Thiamet-G, two O-GlcNAcase inhibitors	639:788	We increased the O-GlcNAcylation level on soleus biopsies performing an organ culture of soleus treated or not with PUGNAc or Thiamet-G, two O-GlcNAcase inhibitors.
23110217	10	43	theme	activity	1866:1873	arg1	modulation					1840:1849	the modulation	1836:1849	the modulation of contractile activity of skeletal muscle	1836:1892	All these data strongly linked O-GlcNAcylation to the modulation of contractile activity of skeletal muscle.
23110217	9	44	theme	O-GlcNAc	1517:1524	arg1	level					1526:1530	O-GlcNAc level	1517:1530	O-GlcNAc level	1517:1530	Since the only slow isoform of contractile protein presenting an increase of O-GlcNAc level was MLC2, the effect of enhanced O-GlcNAcylation pattern on calcium activation parameters could involve the O-GlcNAcylation of sMLC2, without excluding that an unidentified O-GlcNAc proteins, such as TnC, could be potentially involved in this mechanism.
23110217	2	45	from	properties	396:405	arg1	particular					370:379	particular	370:379	particular	370:379	New insights suggest that O-GlcNAcylation might be involved in striated muscle physiology, in particular in contractile properties such as the calcium activation parameters.
23110217	8	46	theme	level	1260:1264	arg1	variation					1238:1246	the variation	1234:1246	the variation of O-GlcNAc level on all these identified proteins	1234:1297	We quantified the variation of O-GlcNAc level on all these identified proteins, and showed that several regulatory contractile proteins, predominantly fast isoforms, presented a drastic increase in their O-GlcNAc level.
23110217	8	47	theme	several	1316:1322	arg1	proteins					1347:1354	several regulatory contractile proteins	1316:1354	several regulatory contractile proteins	1316:1354	We quantified the variation of O-GlcNAc level on all these identified proteins, and showed that several regulatory contractile proteins, predominantly fast isoforms, presented a drastic increase in their O-GlcNAc level.
23110217	8	47	theme	several	1316:1322	arg1	isoforms					1376:1383	predominantly fast isoforms	1357:1383	predominantly fast isoforms	1357:1383	We quantified the variation of O-GlcNAc level on all these identified proteins, and showed that several regulatory contractile proteins, predominantly fast isoforms, presented a drastic increase in their O-GlcNAc level.
23110217	2	48	gly	O-GlcNAcylation	302:316	arg1	physiology					355:364	striated muscle physiology	339:364	striated muscle physiology	339:364	New insights suggest that O-GlcNAcylation might be involved in striated muscle physiology, in particular in contractile properties such as the calcium activation parameters.
23110217	2	48	gly	O-GlcNAcylation	302:316	arg1	particular					370:379	particular	370:379	particular	370:379	New insights suggest that O-GlcNAcylation might be involved in striated muscle physiology, in particular in contractile properties such as the calcium activation parameters.
23110217	1	49	theme	dynamic	215:221	arg1	interplay					244:252	a dynamic and highly regulated interplay	213:252	a dynamic and highly regulated interplay with phosphorylation	213:273	O-N-acetylglucosaminylation is a reversible post-translational modification which presents a dynamic and highly regulated interplay with phosphorylation.
23110217	8	50	theme	contractile	1335:1345	arg1	proteins					1347:1354	several regulatory contractile proteins	1316:1354	several regulatory contractile proteins	1316:1354	We quantified the variation of O-GlcNAc level on all these identified proteins, and showed that several regulatory contractile proteins, predominantly fast isoforms, presented a drastic increase in their O-GlcNAc level.
23110217	8	50	theme	contractile	1335:1345	arg1	isoforms					1376:1383	predominantly fast isoforms	1357:1383	predominantly fast isoforms	1357:1383	We quantified the variation of O-GlcNAc level on all these identified proteins, and showed that several regulatory contractile proteins, predominantly fast isoforms, presented a drastic increase in their O-GlcNAc level.
23110217	10	51	theme	skeletal	1878:1885	arg1	muscle					1887:1892	skeletal muscle	1878:1892	skeletal muscle	1878:1892	All these data strongly linked O-GlcNAcylation to the modulation of contractile activity of skeletal muscle.
23110217	8	52	theme	identified	1279:1288	arg1	proteins					1290:1297	all these identified proteins	1269:1297	all these identified proteins	1269:1297	We quantified the variation of O-GlcNAc level on all these identified proteins, and showed that several regulatory contractile proteins, predominantly fast isoforms, presented a drastic increase in their O-GlcNAc level.
23110217	2	53	theme	calcium	419:425	arg1	parameters					438:447	the calcium activation parameters	415:447	the calcium activation parameters	415:447	New insights suggest that O-GlcNAcylation might be involved in striated muscle physiology, in particular in contractile properties such as the calcium activation parameters.
23110217	2	54	theme	contractile	384:394	arg1	properties					396:405	contractile properties	384:405	contractile properties such as the calcium activation parameters	384:447	New insights suggest that O-GlcNAcylation might be involved in striated muscle physiology, in particular in contractile properties such as the calcium activation parameters.
23110217	2	54	theme	contractile	384:394	arg1	parameters					438:447	the calcium activation parameters	415:447	the calcium activation parameters	415:447	New insights suggest that O-GlcNAcylation might be involved in striated muscle physiology, in particular in contractile properties such as the calcium activation parameters.
23110217	9	55	theme	enhanced	1556:1563	arg1	pattern					1581:1587	enhanced O-GlcNAcylation pattern	1556:1587	enhanced O-GlcNAcylation pattern	1556:1587	Since the only slow isoform of contractile protein presenting an increase of O-GlcNAc level was MLC2, the effect of enhanced O-GlcNAcylation pattern on calcium activation parameters could involve the O-GlcNAcylation of sMLC2, without excluding that an unidentified O-GlcNAc proteins, such as TnC, could be potentially involved in this mechanism.
23110217	4	56	theme	soleus	715:720	arg1	culture					704:710	an organ culture	695:710	an organ culture of soleus treated or not with PUGNAc or Thiamet-G, two O-GlcNAcase inhibitors	695:788	We increased the O-GlcNAcylation level on soleus biopsies performing an organ culture of soleus treated or not with PUGNAc or Thiamet-G, two O-GlcNAcase inhibitors.
23110217	9	57	theme	pattern	1581:1587	arg1	effect					1546:1551	the effect	1542:1551	the effect of enhanced O-GlcNAcylation pattern on calcium activation parameters	1542:1620	Since the only slow isoform of contractile protein presenting an increase of O-GlcNAc level was MLC2, the effect of enhanced O-GlcNAcylation pattern on calcium activation parameters could involve the O-GlcNAcylation of sMLC2, without excluding that an unidentified O-GlcNAc proteins, such as TnC, could be potentially involved in this mechanism.
23110217	6	58	theme	proteins	1015:1022	arg1	O-GlcNAcylation					996:1010	O-GlcNAcylation	996:1010	O-GlcNAcylation of proteins extracted from skinned biopsies	996:1054	Analysis of the glycoproteins pattern showed that this effect is solely due to O-GlcNAcylation of proteins extracted from skinned biopsies.
23110217	4	59	theme	O-GlcNAcase	767:777	arg1	inhibitors					779:788	two O-GlcNAcase inhibitors	763:788	two O-GlcNAcase inhibitors	763:788	We increased the O-GlcNAcylation level on soleus biopsies performing an organ culture of soleus treated or not with PUGNAc or Thiamet-G, two O-GlcNAcase inhibitors.
23110217	7	60	theme	proteomic	1127:1135	arg1	approach					1137:1144	a proteomic approach	1125:1144	a proteomic approach	1125:1144	We also characterized the O-GlcNAcylated contractile proteins using a proteomic approach, and identified among others troponin T and I as being O-GlcNAc modified.
23110217	9	61	theme	calcium	1592:1598	arg1	parameters					1611:1620	calcium activation parameters	1592:1620	calcium activation parameters	1592:1620	Since the only slow isoform of contractile protein presenting an increase of O-GlcNAc level was MLC2, the effect of enhanced O-GlcNAcylation pattern on calcium activation parameters could involve the O-GlcNAcylation of sMLC2, without excluding that an unidentified O-GlcNAc proteins, such as TnC, could be potentially involved in this mechanism.
23110217	7	62	theme	O-GlcNAcylated	1083:1096	arg1	proteins					1110:1117	the O-GlcNAcylated contractile proteins	1079:1117	the O-GlcNAcylated contractile proteins	1079:1117	We also characterized the O-GlcNAcylated contractile proteins using a proteomic approach, and identified among others troponin T and I as being O-GlcNAc modified.
23110217	1	63	theme	reversible	155:164	arg1	modification					185:196	a reversible post-translational modification	153:196	a reversible post-translational modification which presents a dynamic and highly regulated interplay with phosphorylation	153:273	O-N-acetylglucosaminylation is a reversible post-translational modification which presents a dynamic and highly regulated interplay with phosphorylation.
23110217	1	63	theme	reversible	155:164	arg1	O-N-acetylglucosaminylation					122:148	O-N-acetylglucosaminylation	122:148	O-N-acetylglucosaminylation	122:148	O-N-acetylglucosaminylation is a reversible post-translational modification which presents a dynamic and highly regulated interplay with phosphorylation.
23110217	0	64	theme	activation	82:91	arg1	parameters					93:102	the calcium activation parameters	70:102	the calcium activation parameters of muscle fibers	70:119	Increasing O-GlcNAcylation level on organ culture of soleus modulates the calcium activation parameters of muscle fibers.
23110217	0	65	theme	fibers	114:119	arg1	parameters					93:102	the calcium activation parameters	70:102	the calcium activation parameters of muscle fibers	70:119	Increasing O-GlcNAcylation level on organ culture of soleus modulates the calcium activation parameters of muscle fibers.
23110217	9	66	theme	sMLC2	1659:1663	arg1	O-GlcNAcylation					1640:1654	the O-GlcNAcylation	1636:1654	the O-GlcNAcylation of sMLC2	1636:1663	Since the only slow isoform of contractile protein presenting an increase of O-GlcNAc level was MLC2, the effect of enhanced O-GlcNAcylation pattern on calcium activation parameters could involve the O-GlcNAcylation of sMLC2, without excluding that an unidentified O-GlcNAc proteins, such as TnC, could be potentially involved in this mechanism.
23110217	4	67	from	level	659:663	arg1	biopsies					675:682	soleus biopsies	668:682	soleus biopsies performing an organ culture of soleus treated or not with PUGNAc or Thiamet-G, two O-GlcNAcase inhibitors	668:788	We increased the O-GlcNAcylation level on soleus biopsies performing an organ culture of soleus treated or not with PUGNAc or Thiamet-G, two O-GlcNAcase inhibitors.
23110217	0	68	theme	O-GlcNAcylation	11:25	arg1	level					27:31	Increasing O-GlcNAcylation level	0:31	Increasing O-GlcNAcylation level on organ culture of soleus	0:58	Increasing O-GlcNAcylation level on organ culture of soleus modulates the calcium activation parameters of muscle fibers.
23110217	2	69	theme	activation	427:436	arg1	parameters					438:447	the calcium activation parameters	415:447	the calcium activation parameters	415:447	New insights suggest that O-GlcNAcylation might be involved in striated muscle physiology, in particular in contractile properties such as the calcium activation parameters.
23110217	5	70	theme	soleus	894:899	arg1	fibers					909:914	slow soleus skinned fibers	889:914	slow soleus skinned fibers	889:914	The enhancement of O-GlcNAcylation pattern was associated with an increase of calcium affinity on slow soleus skinned fibers.
23110217	1	71	with	interplay	244:252	arg1	phosphorylation					259:273	phosphorylation	259:273	phosphorylation	259:273	O-N-acetylglucosaminylation is a reversible post-translational modification which presents a dynamic and highly regulated interplay with phosphorylation.
23110217	8	72	from	increase	1406:1413	arg1	level					1433:1437	their O-GlcNAc level	1418:1437	their O-GlcNAc level	1418:1437	We quantified the variation of O-GlcNAc level on all these identified proteins, and showed that several regulatory contractile proteins, predominantly fast isoforms, presented a drastic increase in their O-GlcNAc level.
23110217	3	73	theme	increase	518:525	arg1	effect					504:509	the effect	500:509	the effect of the increase of soleus O-GlcNAcylation level on the contractile properties	500:587	By the inhibition of O-GlcNAcase, we investigated the effect of the increase of soleus O-GlcNAcylation level on the contractile properties by establishing T/pCa relationships.
23110217	6	74	theme	pattern	947:953	arg1	Analysis					917:924	Analysis	917:924	Analysis of the glycoproteins pattern	917:953	Analysis of the glycoproteins pattern showed that this effect is solely due to O-GlcNAcylation of proteins extracted from skinned biopsies.
23110217	9	75	theme	unidentified	1692:1703	arg1	proteins					1714:1721	an unidentified O-GlcNAc proteins	1689:1721	an unidentified O-GlcNAc proteins	1689:1721	Since the only slow isoform of contractile protein presenting an increase of O-GlcNAc level was MLC2, the effect of enhanced O-GlcNAcylation pattern on calcium activation parameters could involve the O-GlcNAcylation of sMLC2, without excluding that an unidentified O-GlcNAc proteins, such as TnC, could be potentially involved in this mechanism.
23110217	9	75	theme	unidentified	1692:1703	arg1	TnC					1732:1734	TnC	1732:1734	TnC	1732:1734	Since the only slow isoform of contractile protein presenting an increase of O-GlcNAc level was MLC2, the effect of enhanced O-GlcNAcylation pattern on calcium activation parameters could involve the O-GlcNAcylation of sMLC2, without excluding that an unidentified O-GlcNAc proteins, such as TnC, could be potentially involved in this mechanism.
23110217	3	76	theme	O-GlcNAcase	471:481	arg1	inhibition					457:466	the inhibition	453:466	the inhibition of O-GlcNAcase	453:481	By the inhibition of O-GlcNAcase, we investigated the effect of the increase of soleus O-GlcNAcylation level on the contractile properties by establishing T/pCa relationships.
23110217	3	77	from	effect	504:509	arg1	properties					578:587	the contractile properties	562:587	the contractile properties	562:587	By the inhibition of O-GlcNAcase, we investigated the effect of the increase of soleus O-GlcNAcylation level on the contractile properties by establishing T/pCa relationships.
23110217	0	78	theme	muscle	107:112	arg1	fibers					114:119	muscle fibers	107:119	muscle fibers	107:119	Increasing O-GlcNAcylation level on organ culture of soleus modulates the calcium activation parameters of muscle fibers.
23110217	0	79	theme	soleus	53:58	arg1	culture					42:48	organ culture	36:48	organ culture of soleus	36:58	Increasing O-GlcNAcylation level on organ culture of soleus modulates the calcium activation parameters of muscle fibers.
23110217	9	80	theme	slow	1455:1458	arg1	isoform					1460:1466	the only slow isoform	1446:1466	the only slow isoform of contractile protein presenting an increase of O-GlcNAc level	1446:1530	Since the only slow isoform of contractile protein presenting an increase of O-GlcNAc level was MLC2, the effect of enhanced O-GlcNAcylation pattern on calcium activation parameters could involve the O-GlcNAcylation of sMLC2, without excluding that an unidentified O-GlcNAc proteins, such as TnC, could be potentially involved in this mechanism.
23110217	9	80	theme	slow	1455:1458	arg1	MLC2					1536:1539	MLC2	1536:1539	MLC2	1536:1539	Since the only slow isoform of contractile protein presenting an increase of O-GlcNAc level was MLC2, the effect of enhanced O-GlcNAcylation pattern on calcium activation parameters could involve the O-GlcNAcylation of sMLC2, without excluding that an unidentified O-GlcNAc proteins, such as TnC, could be potentially involved in this mechanism.
23110217	3	81	theme	level	553:557	arg1	increase					518:525	the increase	514:525	the increase of soleus O-GlcNAcylation level	514:557	By the inhibition of O-GlcNAcase, we investigated the effect of the increase of soleus O-GlcNAcylation level on the contractile properties by establishing T/pCa relationships.
23110217	5	82	theme	O-GlcNAcylation	810:824	arg1	pattern					826:832	O-GlcNAcylation pattern	810:832	O-GlcNAcylation pattern	810:832	The enhancement of O-GlcNAcylation pattern was associated with an increase of calcium affinity on slow soleus skinned fibers.
23110217	3	83	theme	soleus	530:535	arg1	level					553:557	soleus O-GlcNAcylation level	530:557	soleus O-GlcNAcylation level	530:557	By the inhibition of O-GlcNAcase, we investigated the effect of the increase of soleus O-GlcNAcylation level on the contractile properties by establishing T/pCa relationships.
23110217	9	84	theme	protein	1483:1489	arg1	isoform					1460:1466	the only slow isoform	1446:1466	the only slow isoform of contractile protein presenting an increase of O-GlcNAc level	1446:1530	Since the only slow isoform of contractile protein presenting an increase of O-GlcNAc level was MLC2, the effect of enhanced O-GlcNAcylation pattern on calcium activation parameters could involve the O-GlcNAcylation of sMLC2, without excluding that an unidentified O-GlcNAc proteins, such as TnC, could be potentially involved in this mechanism.
23110217	9	84	theme	protein	1483:1489	arg1	MLC2					1536:1539	MLC2	1536:1539	MLC2	1536:1539	Since the only slow isoform of contractile protein presenting an increase of O-GlcNAc level was MLC2, the effect of enhanced O-GlcNAcylation pattern on calcium activation parameters could involve the O-GlcNAcylation of sMLC2, without excluding that an unidentified O-GlcNAc proteins, such as TnC, could be potentially involved in this mechanism.
23110217	8	85	theme	fast	1371:1374	arg1	proteins					1347:1354	several regulatory contractile proteins	1316:1354	several regulatory contractile proteins	1316:1354	We quantified the variation of O-GlcNAc level on all these identified proteins, and showed that several regulatory contractile proteins, predominantly fast isoforms, presented a drastic increase in their O-GlcNAc level.
23110217	8	85	theme	fast	1371:1374	arg1	isoforms					1376:1383	predominantly fast isoforms	1357:1383	predominantly fast isoforms	1357:1383	We quantified the variation of O-GlcNAc level on all these identified proteins, and showed that several regulatory contractile proteins, predominantly fast isoforms, presented a drastic increase in their O-GlcNAc level.
23110217	4	86	theme	organ	698:702	arg1	culture					704:710	an organ culture	695:710	an organ culture of soleus treated or not with PUGNAc or Thiamet-G, two O-GlcNAcase inhibitors	695:788	We increased the O-GlcNAcylation level on soleus biopsies performing an organ culture of soleus treated or not with PUGNAc or Thiamet-G, two O-GlcNAcase inhibitors.
31202709	7	0	theme	O-GlcNAc	1136:1143	arg1	expression					1107:1116	The expression	1103:1116	RESULTS The expression of ITGA5, OGT and O-GlcNAc	1095:1143	RESULTS The expression of ITGA5, OGT and O-GlcNAc were all elevated in CRC tissues and cells compared with the normal tissues and cells.
31202709	4	1	theme	western	801:807	arg1	blotting					809:816	western blotting	801:816	western blotting	801:816	METHODS The expression profiles of ITGA5, OGT and O-GlcNAc in CRC tissues and cells were detected by immunohistochemistry (IHC), RT-PCR and western blotting.
31202709	4	2	from	tissues	727:733	arg1	profiles					684:691	The expression profiles	669:691	The expression profiles of ITGA5, OGT and O-GlcNAc in CRC tissues and cells	669:743	METHODS The expression profiles of ITGA5, OGT and O-GlcNAc in CRC tissues and cells were detected by immunohistochemistry (IHC), RT-PCR and western blotting.
31202709	1	3	theme	integrins	148:156	arg1	family					158:163	integrins family	148:163	integrins family	148:163	BACKGROUND/OBJECTIVE Integrin α5 (ITGA5) as one member of integrins family, plays an important role in promoting cancer cell metastasis and invasion through inducing the communications among different cells or cells with extracellular matrix (ECM).
31202709	9	4	theme	PUGNAc + GlcNAc	1486:1500	arg1	treatment					1502:1510	PUGNAc + GlcNAc treatment	1486:1510	PUGNAc + GlcNAc treatment	1486:1510	Besides, PUGNAc, GlcN or PUGNAc + GlcNAc treatment increased ITGA5 protein expression in RKO and SW620 cells, as well as increased its protein stability via enhancing its O-GlcNAcylation.
31202709	0	5	theme	cancer	82:87	arg1	occurrence					41:50	occurrence	41:50	occurrence	41:50	O-GlcNAcylation of ITGA5 facilitates the occurrence and development of colorectal cancer.
31202709	0	5	theme	cancer	82:87	arg1	development					56:66	development	56:66	development	56:66	O-GlcNAcylation of ITGA5 facilitates the occurrence and development of colorectal cancer.
31202709	9	6	theme	protein	1528:1534	arg1	expression					1536:1545	ITGA5 protein expression	1522:1545	ITGA5 protein expression in RKO and SW620 cells	1522:1568	Besides, PUGNAc, GlcN or PUGNAc + GlcNAc treatment increased ITGA5 protein expression in RKO and SW620 cells, as well as increased its protein stability via enhancing its O-GlcNAcylation.
31202709	1	7	theme	family	158:163	arg1	member					138:143	one member	134:143	one member of integrins family	134:163	BACKGROUND/OBJECTIVE Integrin α5 (ITGA5) as one member of integrins family, plays an important role in promoting cancer cell metastasis and invasion through inducing the communications among different cells or cells with extracellular matrix (ECM).
31202709	6	8	theme	Immunoprecipitation	934:952	arg1	assays					1030:1035	Immunoprecipitation (IP), in vitro O-GlcNAcylation of ITGA5 and enzymatic labelling of O-GlcNAc assays	934:1035	Immunoprecipitation (IP), in vitro O-GlcNAcylation of ITGA5 and enzymatic labelling of O-GlcNAc assays	934:1035	Immunoprecipitation (IP), in vitro O-GlcNAcylation of ITGA5 and enzymatic labelling of O-GlcNAc assays were used to detect the O-GlcNAcylation of ITGA5 protein.
31202709	7	9	theme	OGT	1128:1130	arg1	expression					1107:1116	The expression	1103:1116	RESULTS The expression of ITGA5, OGT and O-GlcNAc	1095:1143	RESULTS The expression of ITGA5, OGT and O-GlcNAc were all elevated in CRC tissues and cells compared with the normal tissues and cells.
31202709	3	10	theme	CRC	644:646	arg1	progression					648:658	CRC progression	644:658	CRC progression	644:658	To this end, the current study was performed to explore the effects of O-GlcNAcylation on ITGA5 expression, as well as to probe the effects of ITGA5 O-GlcNAcylation on CRC progression.
31202709	8	11	theme	cell	1327:1330	arg1	apoptosis					1332:1340	decreased cell apoptosis	1317:1340	decreased cell apoptosis	1317:1340	Up-regulation of ITGA5 in CRC RKO cells enhanced cell growth and tumorigenesis while decreased cell apoptosis, while down-regulation of ITGA5 in CRC SW620 cells decreased cell growth and tumorigenesis and induced cell apoptosis.
31202709	4	12	theme	O-GlcNAc	711:718	arg1	profiles					684:691	The expression profiles	669:691	The expression profiles of ITGA5, OGT and O-GlcNAc in CRC tissues and cells	669:743	METHODS The expression profiles of ITGA5, OGT and O-GlcNAc in CRC tissues and cells were detected by immunohistochemistry (IHC), RT-PCR and western blotting.
31202709	4	13	theme	ITGA5	696:700	arg1	profiles					684:691	The expression profiles	669:691	The expression profiles of ITGA5, OGT and O-GlcNAc in CRC tissues and cells	669:743	METHODS The expression profiles of ITGA5, OGT and O-GlcNAc in CRC tissues and cells were detected by immunohistochemistry (IHC), RT-PCR and western blotting.
31202709	7	14	dep	RESULTS	1095:1101	arg1	expression					1107:1116	The expression	1103:1116	RESULTS The expression of ITGA5, OGT and O-GlcNAc	1095:1143	RESULTS The expression of ITGA5, OGT and O-GlcNAc were all elevated in CRC tissues and cells compared with the normal tissues and cells.
31202709	10	15	dep	CONCLUSION	1649:1658	arg1	makes					1692:1696	makes	1692:1696	makes clear that ITGA5 overexpression accelerates the progression of CRC, which is closely associated to its enhanced O-GlcNAcylation	1692:1824	CONCLUSION Collectively, the present study makes clear that ITGA5 overexpression accelerates the progression of CRC, which is closely associated to its enhanced O-GlcNAcylation.
31202709	4	16	from	O-GlcNAc	711:718	arg1	cells					739:743	cells	739:743	cells	739:743	METHODS The expression profiles of ITGA5, OGT and O-GlcNAc in CRC tissues and cells were detected by immunohistochemistry (IHC), RT-PCR and western blotting.
31202709	4	16	from	O-GlcNAc	711:718	arg1	tissues					727:733	CRC tissues	723:733	CRC tissues	723:733	METHODS The expression profiles of ITGA5, OGT and O-GlcNAc in CRC tissues and cells were detected by immunohistochemistry (IHC), RT-PCR and western blotting.
31202709	5	17	theme	flow	826:829	arg1	cytometry					831:839	flow cytometry	826:839	flow cytometry	826:839	CCK-8, flow cytometry and xenotransplantation assays were used to assess cell growth, apoptosis and tumorigenesis.
31202709	7	18	theme	ITGA5	1121:1125	arg1	expression					1107:1116	The expression	1103:1116	RESULTS The expression of ITGA5, OGT and O-GlcNAc	1095:1143	RESULTS The expression of ITGA5, OGT and O-GlcNAc were all elevated in CRC tissues and cells compared with the normal tissues and cells.
31202709	8	19	theme	cell	1445:1448	arg1	apoptosis					1450:1458	cell apoptosis	1445:1458	cell apoptosis	1445:1458	Up-regulation of ITGA5 in CRC RKO cells enhanced cell growth and tumorigenesis while decreased cell apoptosis, while down-regulation of ITGA5 in CRC SW620 cells decreased cell growth and tumorigenesis and induced cell apoptosis.
31202709	3	20	theme	current	493:499	arg1	study					501:505	the current study	489:505	the current study	489:505	To this end, the current study was performed to explore the effects of O-GlcNAcylation on ITGA5 expression, as well as to probe the effects of ITGA5 O-GlcNAcylation on CRC progression.
31202709	2	21	theme	colorectal	383:392	arg1	CRC					402:404	CRC	402:404	CRC	402:404	However, the mechanisms underlying ITGA5 in colorectal cancer (CRC) progression need to be explored, especially for its O-GlcNAcylation.
31202709	2	21	theme	colorectal	383:392	arg1	cancer					394:399	colorectal cancer	383:399	colorectal cancer (CRC) progression	383:417	However, the mechanisms underlying ITGA5 in colorectal cancer (CRC) progression need to be explored, especially for its O-GlcNAcylation.
31202709	8	22	from	Up-regulation	1232:1244	arg1	cells					1266:1270	CRC RKO cells	1258:1270	CRC RKO cells	1258:1270	Up-regulation of ITGA5 in CRC RKO cells enhanced cell growth and tumorigenesis while decreased cell apoptosis, while down-regulation of ITGA5 in CRC SW620 cells decreased cell growth and tumorigenesis and induced cell apoptosis.
31202709	5	23	theme	cytometry	831:839	arg1	assays					865:870	CCK-8, flow cytometry and xenotransplantation assays	819:870	CCK-8, flow cytometry and xenotransplantation assays	819:870	CCK-8, flow cytometry and xenotransplantation assays were used to assess cell growth, apoptosis and tumorigenesis.
31202709	7	24	theme	CRC	1166:1168	arg1	tissues					1170:1176	CRC tissues	1166:1176	CRC tissues	1166:1176	RESULTS The expression of ITGA5, OGT and O-GlcNAc were all elevated in CRC tissues and cells compared with the normal tissues and cells.
31202709	4	25	from	OGT	703:705	arg1	cells					739:743	cells	739:743	cells	739:743	METHODS The expression profiles of ITGA5, OGT and O-GlcNAc in CRC tissues and cells were detected by immunohistochemistry (IHC), RT-PCR and western blotting.
31202709	4	25	from	OGT	703:705	arg1	tissues					727:733	CRC tissues	723:733	CRC tissues	723:733	METHODS The expression profiles of ITGA5, OGT and O-GlcNAc in CRC tissues and cells were detected by immunohistochemistry (IHC), RT-PCR and western blotting.
31202709	8	26	theme	RKO	1262:1264	arg1	cells					1266:1270	CRC RKO cells	1258:1270	CRC RKO cells	1258:1270	Up-regulation of ITGA5 in CRC RKO cells enhanced cell growth and tumorigenesis while decreased cell apoptosis, while down-regulation of ITGA5 in CRC SW620 cells decreased cell growth and tumorigenesis and induced cell apoptosis.
31202709	6	27	theme	O-GlcNAc	1021:1028	arg1	Immunoprecipitation					934:952	Immunoprecipitation	934:952	Immunoprecipitation (IP)	934:957	Immunoprecipitation (IP), in vitro O-GlcNAcylation of ITGA5 and enzymatic labelling of O-GlcNAc assays were used to detect the O-GlcNAcylation of ITGA5 protein.
31202709	6	27	theme	O-GlcNAc	1021:1028	arg1	labelling					1008:1016	enzymatic labelling	998:1016	enzymatic labelling of O-GlcNAc	998:1028	Immunoprecipitation (IP), in vitro O-GlcNAcylation of ITGA5 and enzymatic labelling of O-GlcNAc assays were used to detect the O-GlcNAcylation of ITGA5 protein.
31202709	6	27	theme	O-GlcNAc	1021:1028	arg1	O-GlcNAcylation					969:983	in vitro O-GlcNAcylation	960:983	in vitro O-GlcNAcylation of ITGA5	960:992	Immunoprecipitation (IP), in vitro O-GlcNAcylation of ITGA5 and enzymatic labelling of O-GlcNAc assays were used to detect the O-GlcNAcylation of ITGA5 protein.
31202709	6	27	theme	O-GlcNAc	1021:1028	arg1	IP					955:956	IP	955:956	IP	955:956	Immunoprecipitation (IP), in vitro O-GlcNAcylation of ITGA5 and enzymatic labelling of O-GlcNAc assays were used to detect the O-GlcNAcylation of ITGA5 protein.
31202709	6	28	theme	labelling	1008:1016	arg1	assays					1030:1035	Immunoprecipitation (IP), in vitro O-GlcNAcylation of ITGA5 and enzymatic labelling of O-GlcNAc assays	934:1035	Immunoprecipitation (IP), in vitro O-GlcNAcylation of ITGA5 and enzymatic labelling of O-GlcNAc assays	934:1035	Immunoprecipitation (IP), in vitro O-GlcNAcylation of ITGA5 and enzymatic labelling of O-GlcNAc assays were used to detect the O-GlcNAcylation of ITGA5 protein.
31202709	3	29	from	effects	608:614	arg1	progression					648:658	CRC progression	644:658	CRC progression	644:658	To this end, the current study was performed to explore the effects of O-GlcNAcylation on ITGA5 expression, as well as to probe the effects of ITGA5 O-GlcNAcylation on CRC progression.
31202709	1	30	theme	BACKGROUND/OBJECTIVE	90:109	arg1	ITGA5					124:128	ITGA5	124:128	ITGA5	124:128	BACKGROUND/OBJECTIVE Integrin α5 (ITGA5) as one member of integrins family, plays an important role in promoting cancer cell metastasis and invasion through inducing the communications among different cells or cells with extracellular matrix (ECM).
31202709	1	30	theme	BACKGROUND/OBJECTIVE	90:109	arg1	α5					120:121	BACKGROUND/OBJECTIVE Integrin α5	90:121	BACKGROUND/OBJECTIVE Integrin α5 (ITGA5)	90:129	BACKGROUND/OBJECTIVE Integrin α5 (ITGA5) as one member of integrins family, plays an important role in promoting cancer cell metastasis and invasion through inducing the communications among different cells or cells with extracellular matrix (ECM).
31202709	6	31	theme	enzymatic	998:1006	arg1	labelling					1008:1016	enzymatic labelling	998:1016	enzymatic labelling of O-GlcNAc	998:1028	Immunoprecipitation (IP), in vitro O-GlcNAcylation of ITGA5 and enzymatic labelling of O-GlcNAc assays were used to detect the O-GlcNAcylation of ITGA5 protein.
31202709	8	32	theme	cell	1403:1406	arg1	growth					1408:1413	cell growth	1403:1413	cell growth	1403:1413	Up-regulation of ITGA5 in CRC RKO cells enhanced cell growth and tumorigenesis while decreased cell apoptosis, while down-regulation of ITGA5 in CRC SW620 cells decreased cell growth and tumorigenesis and induced cell apoptosis.
31202709	4	33	from	ITGA5	696:700	arg1	cells					739:743	cells	739:743	cells	739:743	METHODS The expression profiles of ITGA5, OGT and O-GlcNAc in CRC tissues and cells were detected by immunohistochemistry (IHC), RT-PCR and western blotting.
31202709	4	33	from	ITGA5	696:700	arg1	tissues					727:733	CRC tissues	723:733	CRC tissues	723:733	METHODS The expression profiles of ITGA5, OGT and O-GlcNAc in CRC tissues and cells were detected by immunohistochemistry (IHC), RT-PCR and western blotting.
31202709	1	34	theme	Integrin	111:118	arg1	ITGA5					124:128	ITGA5	124:128	ITGA5	124:128	BACKGROUND/OBJECTIVE Integrin α5 (ITGA5) as one member of integrins family, plays an important role in promoting cancer cell metastasis and invasion through inducing the communications among different cells or cells with extracellular matrix (ECM).
31202709	1	34	theme	Integrin	111:118	arg1	α5					120:121	BACKGROUND/OBJECTIVE Integrin α5	90:121	BACKGROUND/OBJECTIVE Integrin α5 (ITGA5)	90:129	BACKGROUND/OBJECTIVE Integrin α5 (ITGA5) as one member of integrins family, plays an important role in promoting cancer cell metastasis and invasion through inducing the communications among different cells or cells with extracellular matrix (ECM).
31202709	8	35	from	down-regulation	1349:1363	arg1	SW620 cells					1381:1391	CRC SW620 cells	1377:1391	CRC SW620 cells	1377:1391	Up-regulation of ITGA5 in CRC RKO cells enhanced cell growth and tumorigenesis while decreased cell apoptosis, while down-regulation of ITGA5 in CRC SW620 cells decreased cell growth and tumorigenesis and induced cell apoptosis.
31202709	1	36	theme	important	175:183	arg1	role					185:188	an important role	172:188	an important role	172:188	BACKGROUND/OBJECTIVE Integrin α5 (ITGA5) as one member of integrins family, plays an important role in promoting cancer cell metastasis and invasion through inducing the communications among different cells or cells with extracellular matrix (ECM).
31202709	8	37	theme	CRC	1377:1379	arg1	SW620 cells					1381:1391	CRC SW620 cells	1377:1391	CRC SW620 cells	1377:1391	Up-regulation of ITGA5 in CRC RKO cells enhanced cell growth and tumorigenesis while decreased cell apoptosis, while down-regulation of ITGA5 in CRC SW620 cells decreased cell growth and tumorigenesis and induced cell apoptosis.
31202709	1	38	theme	different	281:289	arg1	cells					291:295	different cells	281:295	different cells	281:295	BACKGROUND/OBJECTIVE Integrin α5 (ITGA5) as one member of integrins family, plays an important role in promoting cancer cell metastasis and invasion through inducing the communications among different cells or cells with extracellular matrix (ECM).
31202709	8	39	theme	decreased	1317:1325	arg1	apoptosis					1332:1340	decreased cell apoptosis	1317:1340	decreased cell apoptosis	1317:1340	Up-regulation of ITGA5 in CRC RKO cells enhanced cell growth and tumorigenesis while decreased cell apoptosis, while down-regulation of ITGA5 in CRC SW620 cells decreased cell growth and tumorigenesis and induced cell apoptosis.
31202709	4	40	theme	OGT	703:705	arg1	profiles					684:691	The expression profiles	669:691	The expression profiles of ITGA5, OGT and O-GlcNAc in CRC tissues and cells	669:743	METHODS The expression profiles of ITGA5, OGT and O-GlcNAc in CRC tissues and cells were detected by immunohistochemistry (IHC), RT-PCR and western blotting.
31202709	10	41	theme	CRC	1761:1763	arg1	progression					1746:1756	the progression	1742:1756	the progression	1742:1756	CONCLUSION Collectively, the present study makes clear that ITGA5 overexpression accelerates the progression of CRC, which is closely associated to its enhanced O-GlcNAcylation.
31202709	6	42	theme	ITGA5	988:992	arg1	Immunoprecipitation					934:952	Immunoprecipitation	934:952	Immunoprecipitation (IP)	934:957	Immunoprecipitation (IP), in vitro O-GlcNAcylation of ITGA5 and enzymatic labelling of O-GlcNAc assays were used to detect the O-GlcNAcylation of ITGA5 protein.
31202709	6	42	theme	ITGA5	988:992	arg1	labelling					1008:1016	enzymatic labelling	998:1016	enzymatic labelling of O-GlcNAc	998:1028	Immunoprecipitation (IP), in vitro O-GlcNAcylation of ITGA5 and enzymatic labelling of O-GlcNAc assays were used to detect the O-GlcNAcylation of ITGA5 protein.
31202709	6	42	theme	ITGA5	988:992	arg1	O-GlcNAcylation					969:983	in vitro O-GlcNAcylation	960:983	in vitro O-GlcNAcylation of ITGA5	960:992	Immunoprecipitation (IP), in vitro O-GlcNAcylation of ITGA5 and enzymatic labelling of O-GlcNAc assays were used to detect the O-GlcNAcylation of ITGA5 protein.
31202709	6	42	theme	ITGA5	988:992	arg1	IP					955:956	IP	955:956	IP	955:956	Immunoprecipitation (IP), in vitro O-GlcNAcylation of ITGA5 and enzymatic labelling of O-GlcNAc assays were used to detect the O-GlcNAcylation of ITGA5 protein.
31202709	0	43	theme	ITGA5	19:23	arg1	O-GlcNAcylation					0:14	O-GlcNAcylation	0:14	O-GlcNAcylation of ITGA5	0:23	O-GlcNAcylation of ITGA5 facilitates the occurrence and development of colorectal cancer.
31202709	10	44	theme	enhanced	1801:1808	arg1	O-GlcNAcylation					1810:1824	its enhanced O-GlcNAcylation	1797:1824	its enhanced O-GlcNAcylation	1797:1824	CONCLUSION Collectively, the present study makes clear that ITGA5 overexpression accelerates the progression of CRC, which is closely associated to its enhanced O-GlcNAcylation.
31202709	4	45	theme	CRC	723:725	arg1	tissues					727:733	CRC tissues	723:733	CRC tissues	723:733	METHODS The expression profiles of ITGA5, OGT and O-GlcNAc in CRC tissues and cells were detected by immunohistochemistry (IHC), RT-PCR and western blotting.
31202709	8	46	theme	ITGA5	1368:1372	arg1	down-regulation					1349:1363	down-regulation	1349:1363	down-regulation of ITGA5 in CRC SW620 cells	1349:1391	Up-regulation of ITGA5 in CRC RKO cells enhanced cell growth and tumorigenesis while decreased cell apoptosis, while down-regulation of ITGA5 in CRC SW620 cells decreased cell growth and tumorigenesis and induced cell apoptosis.
31202709	4	47	dep	METHODS	661:667	arg1	detected					750:757	detected	750:757	were detected by immunohistochemistry (IHC), RT-PCR and western blotting	745:816	METHODS The expression profiles of ITGA5, OGT and O-GlcNAc in CRC tissues and cells were detected by immunohistochemistry (IHC), RT-PCR and western blotting.
31202709	6	48	theme	protein	1086:1092	arg1	O-GlcNAcylation					1061:1075	the O-GlcNAcylation	1057:1075	the O-GlcNAcylation of ITGA5 protein	1057:1092	Immunoprecipitation (IP), in vitro O-GlcNAcylation of ITGA5 and enzymatic labelling of O-GlcNAc assays were used to detect the O-GlcNAcylation of ITGA5 protein.
31202709	10	49	theme	ITGA5	1709:1713	arg1	overexpression					1715:1728	ITGA5 overexpression	1709:1728	ITGA5 overexpression	1709:1728	CONCLUSION Collectively, the present study makes clear that ITGA5 overexpression accelerates the progression of CRC, which is closely associated to its enhanced O-GlcNAcylation.
31202709	7	50	theme	normal	1206:1211	arg1	tissues					1213:1219	the normal tissues	1202:1219	the normal tissues	1202:1219	RESULTS The expression of ITGA5, OGT and O-GlcNAc were all elevated in CRC tissues and cells compared with the normal tissues and cells.
31202709	9	51	theme	ITGA5	1522:1526	arg1	expression					1536:1545	ITGA5 protein expression	1522:1545	ITGA5 protein expression in RKO and SW620 cells	1522:1568	Besides, PUGNAc, GlcN or PUGNAc + GlcNAc treatment increased ITGA5 protein expression in RKO and SW620 cells, as well as increased its protein stability via enhancing its O-GlcNAcylation.
31202709	5	52	used	used	877:880	arg2	assays					865:870	CCK-8, flow cytometry and xenotransplantation assays	819:870	CCK-8, flow cytometry and xenotransplantation assays	819:870	CCK-8, flow cytometry and xenotransplantation assays were used to assess cell growth, apoptosis and tumorigenesis.
31202709	6	53	theme	O-GlcNAcylation	969:983	arg1	assays					1030:1035	Immunoprecipitation (IP), in vitro O-GlcNAcylation of ITGA5 and enzymatic labelling of O-GlcNAc assays	934:1035	Immunoprecipitation (IP), in vitro O-GlcNAcylation of ITGA5 and enzymatic labelling of O-GlcNAc assays	934:1035	Immunoprecipitation (IP), in vitro O-GlcNAcylation of ITGA5 and enzymatic labelling of O-GlcNAc assays were used to detect the O-GlcNAcylation of ITGA5 protein.
31202709	1	54	dep	cell	210:213	arg1	metastasis					215:224	metastasis	215:224	metastasis	215:224	BACKGROUND/OBJECTIVE Integrin α5 (ITGA5) as one member of integrins family, plays an important role in promoting cancer cell metastasis and invasion through inducing the communications among different cells or cells with extracellular matrix (ECM).
31202709	3	55	theme	ITGA5	566:570	arg1	expression					572:581	ITGA5 expression	566:581	ITGA5 expression	566:581	To this end, the current study was performed to explore the effects of O-GlcNAcylation on ITGA5 expression, as well as to probe the effects of ITGA5 O-GlcNAcylation on CRC progression.
31202709	1	56	theme	cancer	203:208	arg1	cell					210:213	cancer cell metastasis and invasion	203:237	cell	210:213	BACKGROUND/OBJECTIVE Integrin α5 (ITGA5) as one member of integrins family, plays an important role in promoting cancer cell metastasis and invasion through inducing the communications among different cells or cells with extracellular matrix (ECM).
31202709	8	57	theme	cell	1281:1284	arg1	growth					1286:1291	cell growth	1281:1291	cell growth	1281:1291	Up-regulation of ITGA5 in CRC RKO cells enhanced cell growth and tumorigenesis while decreased cell apoptosis, while down-regulation of ITGA5 in CRC SW620 cells decreased cell growth and tumorigenesis and induced cell apoptosis.
31202709	9	58	from	expression	1536:1545	arg1	SW620 cells					1558:1568	SW620 cells	1558:1568	SW620 cells	1558:1568	Besides, PUGNAc, GlcN or PUGNAc + GlcNAc treatment increased ITGA5 protein expression in RKO and SW620 cells, as well as increased its protein stability via enhancing its O-GlcNAcylation.
31202709	9	58	from	expression	1536:1545	arg1	RKO					1550:1552	RKO	1550:1552	RKO	1550:1552	Besides, PUGNAc, GlcN or PUGNAc + GlcNAc treatment increased ITGA5 protein expression in RKO and SW620 cells, as well as increased its protein stability via enhancing its O-GlcNAcylation.
31202709	0	59	dep	occurrence	41:50	arg1	the					37:39	the	37:39	the	37:39	O-GlcNAcylation of ITGA5 facilitates the occurrence and development of colorectal cancer.
31202709	6	60	dep	in	960:961	arg1	vitro					963:967	vitro	963:967	vitro	963:967	Immunoprecipitation (IP), in vitro O-GlcNAcylation of ITGA5 and enzymatic labelling of O-GlcNAc assays were used to detect the O-GlcNAcylation of ITGA5 protein.
31202709	1	61	theme	extracellular	311:323	arg1	ECM					333:335	ECM	333:335	ECM	333:335	BACKGROUND/OBJECTIVE Integrin α5 (ITGA5) as one member of integrins family, plays an important role in promoting cancer cell metastasis and invasion through inducing the communications among different cells or cells with extracellular matrix (ECM).
31202709	1	61	theme	extracellular	311:323	arg1	matrix					325:330	extracellular matrix	311:330	extracellular matrix (ECM)	311:336	BACKGROUND/OBJECTIVE Integrin α5 (ITGA5) as one member of integrins family, plays an important role in promoting cancer cell metastasis and invasion through inducing the communications among different cells or cells with extracellular matrix (ECM).
31202709	9	62	theme	protein	1596:1602	arg1	stability					1604:1612	its protein stability	1592:1612	its protein stability	1592:1612	Besides, PUGNAc, GlcN or PUGNAc + GlcNAc treatment increased ITGA5 protein expression in RKO and SW620 cells, as well as increased its protein stability via enhancing its O-GlcNAcylation.
31202709	3	63	theme	ITGA5	619:623	arg1	O-GlcNAcylation					625:639	ITGA5 O-GlcNAcylation	619:639	ITGA5 O-GlcNAcylation	619:639	To this end, the current study was performed to explore the effects of O-GlcNAcylation on ITGA5 expression, as well as to probe the effects of ITGA5 O-GlcNAcylation on CRC progression.
31202709	3	64	theme	O-GlcNAcylation	547:561	arg1	effects					536:542	the effects	532:542	the effects of O-GlcNAcylation on ITGA5 expression	532:581	To this end, the current study was performed to explore the effects of O-GlcNAcylation on ITGA5 expression, as well as to probe the effects of ITGA5 O-GlcNAcylation on CRC progression.
31202709	5	65	theme	xenotransplantation	845:863	arg1	assays					865:870	CCK-8, flow cytometry and xenotransplantation assays	819:870	CCK-8, flow cytometry and xenotransplantation assays	819:870	CCK-8, flow cytometry and xenotransplantation assays were used to assess cell growth, apoptosis and tumorigenesis.
31202709	4	66	from	profiles	684:691	arg1	cells					739:743	cells	739:743	cells	739:743	METHODS The expression profiles of ITGA5, OGT and O-GlcNAc in CRC tissues and cells were detected by immunohistochemistry (IHC), RT-PCR and western blotting.
31202709	4	66	from	profiles	684:691	arg1	tissues					727:733	CRC tissues	723:733	CRC tissues	723:733	METHODS The expression profiles of ITGA5, OGT and O-GlcNAc in CRC tissues and cells were detected by immunohistochemistry (IHC), RT-PCR and western blotting.
31202709	3	67	theme	O-GlcNAcylation	625:639	arg1	effects					608:614	the effects	604:614	the effects of ITGA5 O-GlcNAcylation on CRC progression	604:658	To this end, the current study was performed to explore the effects of O-GlcNAcylation on ITGA5 expression, as well as to probe the effects of ITGA5 O-GlcNAcylation on CRC progression.
31202709	6	68	used	used	1042:1045	arg2	assays					1030:1035	Immunoprecipitation (IP), in vitro O-GlcNAcylation of ITGA5 and enzymatic labelling of O-GlcNAc assays	934:1035	Immunoprecipitation (IP), in vitro O-GlcNAcylation of ITGA5 and enzymatic labelling of O-GlcNAc assays	934:1035	Immunoprecipitation (IP), in vitro O-GlcNAcylation of ITGA5 and enzymatic labelling of O-GlcNAc assays were used to detect the O-GlcNAcylation of ITGA5 protein.
31202709	6	69	theme	ITGA5	1080:1084	arg1	protein					1086:1092	ITGA5 protein	1080:1092	ITGA5 protein	1080:1092	Immunoprecipitation (IP), in vitro O-GlcNAcylation of ITGA5 and enzymatic labelling of O-GlcNAc assays were used to detect the O-GlcNAcylation of ITGA5 protein.
31202709	6	70	theme	in	960:961	arg1	O-GlcNAcylation					969:983	in vitro O-GlcNAcylation	960:983	in vitro O-GlcNAcylation of ITGA5	960:992	Immunoprecipitation (IP), in vitro O-GlcNAcylation of ITGA5 and enzymatic labelling of O-GlcNAc assays were used to detect the O-GlcNAcylation of ITGA5 protein.
31202709	10	71	theme	present	1678:1684	arg1	study					1686:1690	the present study	1674:1690	the present study	1674:1690	CONCLUSION Collectively, the present study makes clear that ITGA5 overexpression accelerates the progression of CRC, which is closely associated to its enhanced O-GlcNAcylation.
31202709	8	72	theme	CRC	1258:1260	arg1	cells					1266:1270	CRC RKO cells	1258:1270	CRC RKO cells	1258:1270	Up-regulation of ITGA5 in CRC RKO cells enhanced cell growth and tumorigenesis while decreased cell apoptosis, while down-regulation of ITGA5 in CRC SW620 cells decreased cell growth and tumorigenesis and induced cell apoptosis.
31202709	4	73	theme	expression	673:682	arg1	profiles					684:691	The expression profiles	669:691	The expression profiles of ITGA5, OGT and O-GlcNAc in CRC tissues and cells	669:743	METHODS The expression profiles of ITGA5, OGT and O-GlcNAc in CRC tissues and cells were detected by immunohistochemistry (IHC), RT-PCR and western blotting.
31202709	8	74	theme	ITGA5	1249:1253	arg1	Up-regulation					1232:1244	Up-regulation	1232:1244	Up-regulation of ITGA5 in CRC RKO cells	1232:1270	Up-regulation of ITGA5 in CRC RKO cells enhanced cell growth and tumorigenesis while decreased cell apoptosis, while down-regulation of ITGA5 in CRC SW620 cells decreased cell growth and tumorigenesis and induced cell apoptosis.
31202709	0	75	theme	colorectal	71:80	arg1	cancer					82:87	colorectal cancer	71:87	colorectal cancer	71:87	O-GlcNAcylation of ITGA5 facilitates the occurrence and development of colorectal cancer.
31202709	2	76	theme	cancer	394:399	arg1	progression					407:417	colorectal cancer (CRC) progression	383:417	colorectal cancer (CRC) progression	383:417	However, the mechanisms underlying ITGA5 in colorectal cancer (CRC) progression need to be explored, especially for its O-GlcNAcylation.
31202709	4	77	from	cells	739:743	arg1	profiles					684:691	The expression profiles	669:691	The expression profiles of ITGA5, OGT and O-GlcNAc in CRC tissues and cells	669:743	METHODS The expression profiles of ITGA5, OGT and O-GlcNAc in CRC tissues and cells were detected by immunohistochemistry (IHC), RT-PCR and western blotting.
31202709	5	78	theme	CCK-8	819:823	arg1	assays					865:870	CCK-8, flow cytometry and xenotransplantation assays	819:870	CCK-8, flow cytometry and xenotransplantation assays	819:870	CCK-8, flow cytometry and xenotransplantation assays were used to assess cell growth, apoptosis and tumorigenesis.
31202709	3	79	from	effects	536:542	arg1	expression					572:581	ITGA5 expression	566:581	ITGA5 expression	566:581	To this end, the current study was performed to explore the effects of O-GlcNAcylation on ITGA5 expression, as well as to probe the effects of ITGA5 O-GlcNAcylation on CRC progression.
31202709	5	80	dep	cell	892:895	arg1	tumorigenesis					919:931	tumorigenesis	919:931	tumorigenesis	919:931	CCK-8, flow cytometry and xenotransplantation assays were used to assess cell growth, apoptosis and tumorigenesis.
31202709	5	80	dep	cell	892:895	arg1	apoptosis					905:913	apoptosis	905:913	apoptosis	905:913	CCK-8, flow cytometry and xenotransplantation assays were used to assess cell growth, apoptosis and tumorigenesis.
31202709	5	80	dep	cell	892:895	arg1	growth					897:902	growth	897:902	growth	897:902	CCK-8, flow cytometry and xenotransplantation assays were used to assess cell growth, apoptosis and tumorigenesis.
28262738	8	0	theme	GFAT	1182:1185	arg1	induction					1169:1177	the induction	1165:1177	the induction of GFAT, O-GlcNAcylation and an increase of O-GlcNAcylated vimentin and vimentin expression	1165:1269	The glucose level that promoted migration/invasion was shown to be potentiated by the induction of GFAT, O-GlcNAcylation and an increase of O-GlcNAcylated vimentin and vimentin expression.
28262738	7	1	theme	amidotransferase	1020:1035	arg1	expressions					950:960	the expressions	946:960	the expressions of vimentin, hexokinase, glucosamine-fructose-6-phosphate amidotransferase (GFAT) and O-GlcNAc transferase of CCA cells	946:1080	Concomitantly, high glucose increased global O-GlcNAcylated proteins, the expressions of vimentin, hexokinase, glucosamine-fructose-6-phosphate amidotransferase (GFAT) and O-GlcNAc transferase of CCA cells.
28262738	7	1	theme	amidotransferase	1020:1035	arg1	proteins					936:943	global O-GlcNAcylated proteins	914:943	global O-GlcNAcylated proteins	914:943	Concomitantly, high glucose increased global O-GlcNAcylated proteins, the expressions of vimentin, hexokinase, glucosamine-fructose-6-phosphate amidotransferase (GFAT) and O-GlcNAc transferase of CCA cells.
28262738	1	2	theme	cells	165:169	arg1	utilization					130:140	Increased glucose utilization	112:140	Increased glucose utilization	112:140	Increased glucose utilization is a feature of cancer cells to support cell survival, proliferation, and metastasis.
28262738	1	2	theme	cells	165:169	arg1	feature					147:153	a feature	145:153	a feature of cancer cells to support cell survival, proliferation, and metastasis	145:225	Increased glucose utilization is a feature of cancer cells to support cell survival, proliferation, and metastasis.
28262738	7	3	theme	cells	1076:1080	arg1	GFAT					1038:1041	GFAT	1038:1041	GFAT	1038:1041	Concomitantly, high glucose increased global O-GlcNAcylated proteins, the expressions of vimentin, hexokinase, glucosamine-fructose-6-phosphate amidotransferase (GFAT) and O-GlcNAc transferase of CCA cells.
28262738	7	3	theme	cells	1076:1080	arg1	hexokinase					975:984	hexokinase	975:984	hexokinase	975:984	Concomitantly, high glucose increased global O-GlcNAcylated proteins, the expressions of vimentin, hexokinase, glucosamine-fructose-6-phosphate amidotransferase (GFAT) and O-GlcNAc transferase of CCA cells.
28262738	7	3	theme	cells	1076:1080	arg1	amidotransferase					1020:1035	glucosamine-fructose-6-phosphate amidotransferase	987:1035	glucosamine-fructose-6-phosphate amidotransferase (GFAT)	987:1042	Concomitantly, high glucose increased global O-GlcNAcylated proteins, the expressions of vimentin, hexokinase, glucosamine-fructose-6-phosphate amidotransferase (GFAT) and O-GlcNAc transferase of CCA cells.
28262738	7	3	theme	cells	1076:1080	arg1	vimentin					965:972	vimentin	965:972	vimentin	965:972	Concomitantly, high glucose increased global O-GlcNAcylated proteins, the expressions of vimentin, hexokinase, glucosamine-fructose-6-phosphate amidotransferase (GFAT) and O-GlcNAc transferase of CCA cells.
28262738	7	3	theme	cells	1076:1080	arg1	transferase					1057:1067	O-GlcNAc transferase	1048:1067	O-GlcNAc transferase of CCA cells	1048:1080	Concomitantly, high glucose increased global O-GlcNAcylated proteins, the expressions of vimentin, hexokinase, glucosamine-fructose-6-phosphate amidotransferase (GFAT) and O-GlcNAc transferase of CCA cells.
28262738	4	4	theme	normal	594:599	arg1	media					634:638	normal (5.6 mM) or high (25 mM) glucose media	594:638	normal (5.6 mM) or high (25 mM) glucose media	594:638	Two pairs each of the parental low metastatic and highly metastatic CCA sublines were cultured in normal (5.6 mM) or high (25 mM) glucose media.
28262738	0	5	theme	cells	85:89	arg1	aggressiveness					30:43	the aggressiveness	26:43	the aggressiveness of highly metastatic cholangiocarcinoma cells	26:89	High glucose levels boost the aggressiveness of highly metastatic cholangiocarcinoma cells via O-GlcNAcylation.
28262738	4	6	theme	low	527:529	arg1	sublines					568:575	the parental low metastatic and highly metastatic CCA sublines	514:575	the parental low metastatic and highly metastatic CCA sublines	514:575	Two pairs each of the parental low metastatic and highly metastatic CCA sublines were cultured in normal (5.6 mM) or high (25 mM) glucose media.
28262738	10	7	theme	O-GlcNAcylation	1499:1513	arg1	modulation					1485:1494	modulation	1485:1494	modulation of O-GlcNAcylation	1485:1513	Altogether, these results suggested the role of high glucose enhanced CCA metastasis via modulation of O-GlcNAcylation, through the expressions of GFAT and vimentin.
28262738	7	8	theme	hexokinase	975:984	arg1	expressions					950:960	the expressions	946:960	the expressions of vimentin, hexokinase, glucosamine-fructose-6-phosphate amidotransferase (GFAT) and O-GlcNAc transferase of CCA cells	946:1080	Concomitantly, high glucose increased global O-GlcNAcylated proteins, the expressions of vimentin, hexokinase, glucosamine-fructose-6-phosphate amidotransferase (GFAT) and O-GlcNAc transferase of CCA cells.
28262738	7	8	theme	hexokinase	975:984	arg1	proteins					936:943	global O-GlcNAcylated proteins	914:943	global O-GlcNAcylated proteins	914:943	Concomitantly, high glucose increased global O-GlcNAcylated proteins, the expressions of vimentin, hexokinase, glucosamine-fructose-6-phosphate amidotransferase (GFAT) and O-GlcNAc transferase of CCA cells.
28262738	9	9	theme	GFAT	1289:1292	arg1	inhibitor					1294:1302	a GFAT inhibitor	1287:1302	a GFAT inhibitor	1287:1302	Treatment with a GFAT inhibitor reduced global O-GlcNAcylated proteins, vimentin expression, and alleviated cell migration.
28262738	8	10	theme	O-GlcNAcylation	1188:1202	arg1	induction					1169:1177	the induction	1165:1177	the induction of GFAT, O-GlcNAcylation and an increase of O-GlcNAcylated vimentin and vimentin expression	1165:1269	The glucose level that promoted migration/invasion was shown to be potentiated by the induction of GFAT, O-GlcNAcylation and an increase of O-GlcNAcylated vimentin and vimentin expression.
28262738	4	11	theme	parental	518:525	arg1	sublines					568:575	the parental low metastatic and highly metastatic CCA sublines	514:575	the parental low metastatic and highly metastatic CCA sublines	514:575	Two pairs each of the parental low metastatic and highly metastatic CCA sublines were cultured in normal (5.6 mM) or high (25 mM) glucose media.
28262738	5	12	theme	migration	645:653	arg1	abilities					668:676	The migration and invasion abilities	641:676	The migration and invasion abilities	641:676	The migration and invasion abilities were determined and underlying mechanisms were explored.
28262738	7	13	theme	vimentin	965:972	arg1	expressions					950:960	the expressions	946:960	the expressions of vimentin, hexokinase, glucosamine-fructose-6-phosphate amidotransferase (GFAT) and O-GlcNAc transferase of CCA cells	946:1080	Concomitantly, high glucose increased global O-GlcNAcylated proteins, the expressions of vimentin, hexokinase, glucosamine-fructose-6-phosphate amidotransferase (GFAT) and O-GlcNAc transferase of CCA cells.
28262738	7	13	theme	vimentin	965:972	arg1	proteins					936:943	global O-GlcNAcylated proteins	914:943	global O-GlcNAcylated proteins	914:943	Concomitantly, high glucose increased global O-GlcNAcylated proteins, the expressions of vimentin, hexokinase, glucosamine-fructose-6-phosphate amidotransferase (GFAT) and O-GlcNAc transferase of CCA cells.
28262738	6	14	theme	cells	809:813	arg1	invasion					793:800	invasion	793:800	invasion	793:800	Results revealed that high glucose promoted migration and invasion of CCA cells that were more pronounced in the highly metastatic sublines.
28262738	6	14	theme	cells	809:813	arg1	migration					779:787	migration	779:787	migration	779:787	Results revealed that high glucose promoted migration and invasion of CCA cells that were more pronounced in the highly metastatic sublines.
28262738	10	15	theme	vimentin	1552:1559	arg1	expressions					1528:1538	the expressions	1524:1538	the expressions of GFAT and vimentin	1524:1559	Altogether, these results suggested the role of high glucose enhanced CCA metastasis via modulation of O-GlcNAcylation, through the expressions of GFAT and vimentin.
28262738	8	16	theme	glucose	1087:1093	arg1	level					1095:1099	The glucose level	1083:1099	The glucose level that promoted migration/invasion	1083:1132	The glucose level that promoted migration/invasion was shown to be potentiated by the induction of GFAT, O-GlcNAcylation and an increase of O-GlcNAcylated vimentin and vimentin expression.
28262738	6	17	theme	CCA	805:807	arg1	cells					809:813	CCA cells	805:813	CCA cells that were more pronounced in the highly metastatic sublines	805:873	Results revealed that high glucose promoted migration and invasion of CCA cells that were more pronounced in the highly metastatic sublines.
28262738	8	18	theme	O-GlcNAcylated	1223:1236	arg1	expression					1260:1269	O-GlcNAcylated vimentin and vimentin expression	1223:1269	O-GlcNAcylated vimentin and vimentin expression	1223:1269	The glucose level that promoted migration/invasion was shown to be potentiated by the induction of GFAT, O-GlcNAcylation and an increase of O-GlcNAcylated vimentin and vimentin expression.
28262738	8	19	theme	expression	1260:1269	arg1	O-GlcNAcylation					1188:1202	O-GlcNAcylation	1188:1202	O-GlcNAcylation	1188:1202	The glucose level that promoted migration/invasion was shown to be potentiated by the induction of GFAT, O-GlcNAcylation and an increase of O-GlcNAcylated vimentin and vimentin expression.
28262738	8	19	theme	expression	1260:1269	arg1	increase					1211:1218	an increase	1208:1218	an increase of O-GlcNAcylated vimentin and vimentin expression	1208:1269	The glucose level that promoted migration/invasion was shown to be potentiated by the induction of GFAT, O-GlcNAcylation and an increase of O-GlcNAcylated vimentin and vimentin expression.
28262738	8	19	theme	expression	1260:1269	arg1	GFAT					1182:1185	GFAT	1182:1185	GFAT	1182:1185	The glucose level that promoted migration/invasion was shown to be potentiated by the induction of GFAT, O-GlcNAcylation and an increase of O-GlcNAcylated vimentin and vimentin expression.
28262738	9	20	theme	alleviated	1369:1378	arg1	migration					1385:1393	alleviated cell migration	1369:1393	alleviated cell migration	1369:1393	Treatment with a GFAT inhibitor reduced global O-GlcNAcylated proteins, vimentin expression, and alleviated cell migration.
28262738	6	21	from	pronounced	830:839	arg1	sublines					866:873	the highly metastatic sublines	844:873	the highly metastatic sublines	844:873	Results revealed that high glucose promoted migration and invasion of CCA cells that were more pronounced in the highly metastatic sublines.
28262738	8	22	theme	increase	1211:1218	arg1	induction					1169:1177	the induction	1165:1177	the induction of GFAT, O-GlcNAcylation and an increase of O-GlcNAcylated vimentin and vimentin expression	1165:1269	The glucose level that promoted migration/invasion was shown to be potentiated by the induction of GFAT, O-GlcNAcylation and an increase of O-GlcNAcylated vimentin and vimentin expression.
28262738	3	23	theme	metastatic	460:469	arg1	potentials					471:480	metastatic potentials	460:480	metastatic potentials of CCA cells	460:493	This study was aimed to determine the effects of high glucose on protein O-GlcNAcylation and metastatic potentials of CCA cells.
28262738	0	24	theme	glucose	5:11	arg1	levels					13:18	High glucose levels	0:18	High glucose levels	0:18	High glucose levels boost the aggressiveness of highly metastatic cholangiocarcinoma cells via O-GlcNAcylation.
28262738	3	25	from	effects	405:411	arg1	O-GlcNAcylation					440:454	protein O-GlcNAcylation	432:454	protein O-GlcNAcylation	432:454	This study was aimed to determine the effects of high glucose on protein O-GlcNAcylation and metastatic potentials of CCA cells.
28262738	3	25	from	effects	405:411	arg1	potentials					471:480	metastatic potentials	460:480	metastatic potentials of CCA cells	460:493	This study was aimed to determine the effects of high glucose on protein O-GlcNAcylation and metastatic potentials of CCA cells.
28262738	10	26	dep	suggested	1422:1430	arg1	enhanced					1457:1464	enhanced	1457:1464	enhanced	1457:1464	Altogether, these results suggested the role of high glucose enhanced CCA metastasis via modulation of O-GlcNAcylation, through the expressions of GFAT and vimentin.
28262738	3	27	theme	protein	432:438	arg1	O-GlcNAcylation					440:454	protein O-GlcNAcylation	432:454	protein O-GlcNAcylation	432:454	This study was aimed to determine the effects of high glucose on protein O-GlcNAcylation and metastatic potentials of CCA cells.
28262738	0	28	theme	High	0:3	arg1	levels					13:18	High glucose levels	0:18	High glucose levels	0:18	High glucose levels boost the aggressiveness of highly metastatic cholangiocarcinoma cells via O-GlcNAcylation.
28262738	8	29	theme	vimentin	1251:1258	arg1	expression					1260:1269	O-GlcNAcylated vimentin and vimentin expression	1223:1269	O-GlcNAcylated vimentin and vimentin expression	1223:1269	The glucose level that promoted migration/invasion was shown to be potentiated by the induction of GFAT, O-GlcNAcylation and an increase of O-GlcNAcylated vimentin and vimentin expression.
28262738	10	30	theme	CCA	1466:1468	arg1	metastasis					1470:1479	CCA metastasis	1466:1479	CCA metastasis	1466:1479	Altogether, these results suggested the role of high glucose enhanced CCA metastasis via modulation of O-GlcNAcylation, through the expressions of GFAT and vimentin.
28262738	8	31	theme	vimentin	1238:1245	arg1	expression					1260:1269	O-GlcNAcylated vimentin and vimentin expression	1223:1269	O-GlcNAcylated vimentin and vimentin expression	1223:1269	The glucose level that promoted migration/invasion was shown to be potentiated by the induction of GFAT, O-GlcNAcylation and an increase of O-GlcNAcylated vimentin and vimentin expression.
28262738	4	32	theme	CCA	564:566	arg1	sublines					568:575	the parental low metastatic and highly metastatic CCA sublines	514:575	the parental low metastatic and highly metastatic CCA sublines	514:575	Two pairs each of the parental low metastatic and highly metastatic CCA sublines were cultured in normal (5.6 mM) or high (25 mM) glucose media.
28262738	1	33	theme	Increased	112:120	arg1	utilization					130:140	Increased glucose utilization	112:140	Increased glucose utilization	112:140	Increased glucose utilization is a feature of cancer cells to support cell survival, proliferation, and metastasis.
28262738	1	33	theme	Increased	112:120	arg1	feature					147:153	a feature	145:153	a feature of cancer cells to support cell survival, proliferation, and metastasis	145:225	Increased glucose utilization is a feature of cancer cells to support cell survival, proliferation, and metastasis.
28262738	10	34	theme	glucose	1449:1455	arg1	role					1436:1439	the role	1432:1439	the role of high glucose	1432:1455	Altogether, these results suggested the role of high glucose enhanced CCA metastasis via modulation of O-GlcNAcylation, through the expressions of GFAT and vimentin.
28262738	3	35	theme	CCA	485:487	arg1	cells					489:493	CCA cells	485:493	CCA cells	485:493	This study was aimed to determine the effects of high glucose on protein O-GlcNAcylation and metastatic potentials of CCA cells.
28262738	6	36	from	sublines	866:873	arg1	pronounced					830:839	pronounced	830:839	pronounced	830:839	Results revealed that high glucose promoted migration and invasion of CCA cells that were more pronounced in the highly metastatic sublines.
28262738	5	37	theme	underlying	698:707	arg1	mechanisms					709:718	underlying mechanisms	698:718	underlying mechanisms	698:718	The migration and invasion abilities were determined and underlying mechanisms were explored.
28262738	1	38	theme	glucose	122:128	arg1	utilization					130:140	Increased glucose utilization	112:140	Increased glucose utilization	112:140	Increased glucose utilization is a feature of cancer cells to support cell survival, proliferation, and metastasis.
28262738	1	38	theme	glucose	122:128	arg1	feature					147:153	a feature	145:153	a feature of cancer cells to support cell survival, proliferation, and metastasis	145:225	Increased glucose utilization is a feature of cancer cells to support cell survival, proliferation, and metastasis.
28262738	9	39	with	Treatment	1272:1280	arg1	inhibitor					1294:1302	a GFAT inhibitor	1287:1302	a GFAT inhibitor	1287:1302	Treatment with a GFAT inhibitor reduced global O-GlcNAcylated proteins, vimentin expression, and alleviated cell migration.
28262738	3	40	theme	cells	489:493	arg1	O-GlcNAcylation					440:454	protein O-GlcNAcylation	432:454	protein O-GlcNAcylation	432:454	This study was aimed to determine the effects of high glucose on protein O-GlcNAcylation and metastatic potentials of CCA cells.
28262738	3	40	theme	cells	489:493	arg1	potentials					471:480	metastatic potentials	460:480	metastatic potentials of CCA cells	460:493	This study was aimed to determine the effects of high glucose on protein O-GlcNAcylation and metastatic potentials of CCA cells.
28262738	3	41	theme	glucose	421:427	arg1	effects					405:411	the effects	401:411	the effects of high glucose on protein O-GlcNAcylation and metastatic potentials of CCA cells	401:493	This study was aimed to determine the effects of high glucose on protein O-GlcNAcylation and metastatic potentials of CCA cells.
28262738	10	42	theme	GFAT	1543:1546	arg1	expressions					1528:1538	the expressions	1524:1538	the expressions of GFAT and vimentin	1524:1559	Altogether, these results suggested the role of high glucose enhanced CCA metastasis via modulation of O-GlcNAcylation, through the expressions of GFAT and vimentin.
28262738	4	43	dep	normal	594:599	arg1	5.6 mM					602:607	5.6 mM	602:607	5.6 mM	602:607	Two pairs each of the parental low metastatic and highly metastatic CCA sublines were cultured in normal (5.6 mM) or high (25 mM) glucose media.
28262738	7	44	theme	O-GlcNAc	1048:1055	arg1	transferase					1057:1067	O-GlcNAc transferase	1048:1067	O-GlcNAc transferase of CCA cells	1048:1080	Concomitantly, high glucose increased global O-GlcNAcylated proteins, the expressions of vimentin, hexokinase, glucosamine-fructose-6-phosphate amidotransferase (GFAT) and O-GlcNAc transferase of CCA cells.
28262738	4	45	theme	glucose	626:632	arg1	media					634:638	normal (5.6 mM) or high (25 mM) glucose media	594:638	normal (5.6 mM) or high (25 mM) glucose media	594:638	Two pairs each of the parental low metastatic and highly metastatic CCA sublines were cultured in normal (5.6 mM) or high (25 mM) glucose media.
28262738	9	46	theme	O-GlcNAcylated	1319:1332	arg1	proteins					1334:1341	global O-GlcNAcylated proteins	1312:1341	global O-GlcNAcylated proteins	1312:1341	Treatment with a GFAT inhibitor reduced global O-GlcNAcylated proteins, vimentin expression, and alleviated cell migration.
28262738	4	47	theme	metastatic	531:540	arg1	sublines					568:575	the parental low metastatic and highly metastatic CCA sublines	514:575	the parental low metastatic and highly metastatic CCA sublines	514:575	Two pairs each of the parental low metastatic and highly metastatic CCA sublines were cultured in normal (5.6 mM) or high (25 mM) glucose media.
28262738	5	48	theme	invasion	659:666	arg1	abilities					668:676	The migration and invasion abilities	641:676	The migration and invasion abilities	641:676	The migration and invasion abilities were determined and underlying mechanisms were explored.
28262738	4	49	dep	pairs	500:504	arg1	sublines					568:575	the parental low metastatic and highly metastatic CCA sublines	514:575	the parental low metastatic and highly metastatic CCA sublines	514:575	Two pairs each of the parental low metastatic and highly metastatic CCA sublines were cultured in normal (5.6 mM) or high (25 mM) glucose media.
28262738	4	49	dep	pairs	500:504	arg1	each					506:509	each	506:509	each	506:509	Two pairs each of the parental low metastatic and highly metastatic CCA sublines were cultured in normal (5.6 mM) or high (25 mM) glucose media.
28262738	7	50	theme	transferase	1057:1067	arg1	expressions					950:960	the expressions	946:960	the expressions of vimentin, hexokinase, glucosamine-fructose-6-phosphate amidotransferase (GFAT) and O-GlcNAc transferase of CCA cells	946:1080	Concomitantly, high glucose increased global O-GlcNAcylated proteins, the expressions of vimentin, hexokinase, glucosamine-fructose-6-phosphate amidotransferase (GFAT) and O-GlcNAc transferase of CCA cells.
28262738	7	50	theme	transferase	1057:1067	arg1	proteins					936:943	global O-GlcNAcylated proteins	914:943	global O-GlcNAcylated proteins	914:943	Concomitantly, high glucose increased global O-GlcNAcylated proteins, the expressions of vimentin, hexokinase, glucosamine-fructose-6-phosphate amidotransferase (GFAT) and O-GlcNAc transferase of CCA cells.
28262738	3	51	theme	high	416:419	arg1	glucose					421:427	high glucose	416:427	high glucose	416:427	This study was aimed to determine the effects of high glucose on protein O-GlcNAcylation and metastatic potentials of CCA cells.
28262738	4	52	theme	metastatic	553:562	arg1	sublines					568:575	the parental low metastatic and highly metastatic CCA sublines	514:575	the parental low metastatic and highly metastatic CCA sublines	514:575	Two pairs each of the parental low metastatic and highly metastatic CCA sublines were cultured in normal (5.6 mM) or high (25 mM) glucose media.
28262738	1	53	dep	cell	182:185	arg1	survival					187:194	survival	187:194	survival	187:194	Increased glucose utilization is a feature of cancer cells to support cell survival, proliferation, and metastasis.
28262738	6	54	theme	high	757:760	arg1	glucose					762:768	high glucose	757:768	high glucose	757:768	Results revealed that high glucose promoted migration and invasion of CCA cells that were more pronounced in the highly metastatic sublines.
28262738	6	55	theme	metastatic	855:864	arg1	sublines					866:873	the highly metastatic sublines	844:873	the highly metastatic sublines	844:873	Results revealed that high glucose promoted migration and invasion of CCA cells that were more pronounced in the highly metastatic sublines.
28262738	7	56	theme	O-GlcNAcylated	921:934	arg1	expressions					950:960	the expressions	946:960	the expressions of vimentin, hexokinase, glucosamine-fructose-6-phosphate amidotransferase (GFAT) and O-GlcNAc transferase of CCA cells	946:1080	Concomitantly, high glucose increased global O-GlcNAcylated proteins, the expressions of vimentin, hexokinase, glucosamine-fructose-6-phosphate amidotransferase (GFAT) and O-GlcNAc transferase of CCA cells.
28262738	7	56	theme	O-GlcNAcylated	921:934	arg1	proteins					936:943	global O-GlcNAcylated proteins	914:943	global O-GlcNAcylated proteins	914:943	Concomitantly, high glucose increased global O-GlcNAcylated proteins, the expressions of vimentin, hexokinase, glucosamine-fructose-6-phosphate amidotransferase (GFAT) and O-GlcNAc transferase of CCA cells.
28262738	4	57	dep	high	613:616	arg1	25 mM					619:623	25 mM	619:623	25 mM	619:623	Two pairs each of the parental low metastatic and highly metastatic CCA sublines were cultured in normal (5.6 mM) or high (25 mM) glucose media.
28262738	2	58	theme	cancer	273:278	arg1	progression					280:290	cancer progression	273:290	cancer progression	273:290	An association between diabetes mellitus and cancer progression was previously demonstrated in cancers including cholangiocarcinoma (CCA).
28262738	10	59	theme	high	1444:1447	arg1	glucose					1449:1455	high glucose	1444:1455	high glucose	1444:1455	Altogether, these results suggested the role of high glucose enhanced CCA metastasis via modulation of O-GlcNAcylation, through the expressions of GFAT and vimentin.
28262738	7	60	theme	CCA	1072:1074	arg1	cells					1076:1080	CCA cells	1072:1080	CCA cells	1072:1080	Concomitantly, high glucose increased global O-GlcNAcylated proteins, the expressions of vimentin, hexokinase, glucosamine-fructose-6-phosphate amidotransferase (GFAT) and O-GlcNAc transferase of CCA cells.
28262738	9	61	theme	global	1312:1317	arg1	proteins					1334:1341	global O-GlcNAcylated proteins	1312:1341	global O-GlcNAcylated proteins	1312:1341	Treatment with a GFAT inhibitor reduced global O-GlcNAcylated proteins, vimentin expression, and alleviated cell migration.
28262738	0	62	theme	cholangiocarcinoma	66:83	arg1	cells					85:89	highly metastatic cholangiocarcinoma cells	48:89	highly metastatic cholangiocarcinoma cells	48:89	High glucose levels boost the aggressiveness of highly metastatic cholangiocarcinoma cells via O-GlcNAcylation.
28262738	9	63	theme	cell	1380:1383	arg1	migration					1385:1393	alleviated cell migration	1369:1393	alleviated cell migration	1369:1393	Treatment with a GFAT inhibitor reduced global O-GlcNAcylated proteins, vimentin expression, and alleviated cell migration.
28262738	7	64	theme	global	914:919	arg1	expressions					950:960	the expressions	946:960	the expressions of vimentin, hexokinase, glucosamine-fructose-6-phosphate amidotransferase (GFAT) and O-GlcNAc transferase of CCA cells	946:1080	Concomitantly, high glucose increased global O-GlcNAcylated proteins, the expressions of vimentin, hexokinase, glucosamine-fructose-6-phosphate amidotransferase (GFAT) and O-GlcNAc transferase of CCA cells.
28262738	7	64	theme	global	914:919	arg1	proteins					936:943	global O-GlcNAcylated proteins	914:943	global O-GlcNAcylated proteins	914:943	Concomitantly, high glucose increased global O-GlcNAcylated proteins, the expressions of vimentin, hexokinase, glucosamine-fructose-6-phosphate amidotransferase (GFAT) and O-GlcNAc transferase of CCA cells.
28262738	0	65	theme	metastatic	55:64	arg1	cells					85:89	highly metastatic cholangiocarcinoma cells	48:89	highly metastatic cholangiocarcinoma cells	48:89	High glucose levels boost the aggressiveness of highly metastatic cholangiocarcinoma cells via O-GlcNAcylation.
28262738	9	66	theme	vimentin	1344:1351	arg1	expression					1353:1362	vimentin expression	1344:1362	vimentin expression	1344:1362	Treatment with a GFAT inhibitor reduced global O-GlcNAcylated proteins, vimentin expression, and alleviated cell migration.
28262738	2	67	theme	diabetes	251:258	arg1	mellitus					260:267	diabetes mellitus	251:267	diabetes mellitus	251:267	An association between diabetes mellitus and cancer progression was previously demonstrated in cancers including cholangiocarcinoma (CCA).
28262738	7	68	theme	glucosamine-fructose-6-phosphate	987:1018	arg1	GFAT					1038:1041	GFAT	1038:1041	GFAT	1038:1041	Concomitantly, high glucose increased global O-GlcNAcylated proteins, the expressions of vimentin, hexokinase, glucosamine-fructose-6-phosphate amidotransferase (GFAT) and O-GlcNAc transferase of CCA cells.
28262738	7	68	theme	glucosamine-fructose-6-phosphate	987:1018	arg1	amidotransferase					1020:1035	glucosamine-fructose-6-phosphate amidotransferase	987:1035	glucosamine-fructose-6-phosphate amidotransferase (GFAT)	987:1042	Concomitantly, high glucose increased global O-GlcNAcylated proteins, the expressions of vimentin, hexokinase, glucosamine-fructose-6-phosphate amidotransferase (GFAT) and O-GlcNAc transferase of CCA cells.
28262738	1	69	theme	cancer	158:163	arg1	cells					165:169	cancer cells	158:169	cancer cells	158:169	Increased glucose utilization is a feature of cancer cells to support cell survival, proliferation, and metastasis.
28262738	7	70	theme	high	891:894	arg1	glucose					896:902	high glucose	891:902	high glucose	891:902	Concomitantly, high glucose increased global O-GlcNAcylated proteins, the expressions of vimentin, hexokinase, glucosamine-fructose-6-phosphate amidotransferase (GFAT) and O-GlcNAc transferase of CCA cells.
28262738	4	71	theme	high	613:616	arg1	media					634:638	normal (5.6 mM) or high (25 mM) glucose media	594:638	normal (5.6 mM) or high (25 mM) glucose media	594:638	Two pairs each of the parental low metastatic and highly metastatic CCA sublines were cultured in normal (5.6 mM) or high (25 mM) glucose media.
18653473	0	0	theme	cytoskeletal	100:111	arg1	vimentin					121:128	the cytoskeletal protein vimentin	96:128	the cytoskeletal protein vimentin	96:128	A mitotic GlcNAcylation/phosphorylation signaling complex alters the posttranslational state of the cytoskeletal protein vimentin.
18653473	3	1	theme	O-GlcNAc	513:520	arg1	transferase					522:532	O-GlcNAc transferase	513:532	O-GlcNAc transferase (OGT)	513:538	Here, we demonstrate that the enzymes responsible for O-GlcNAc cycling, O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) are in a transient complex at M phase with the mitotic kinase Aurora B and protein phosphatase 1.
18653473	3	1	theme	O-GlcNAc	513:520	arg1	enzymes					471:477	the enzymes	467:477	the enzymes responsible for O-GlcNAc cycling	467:510	Here, we demonstrate that the enzymes responsible for O-GlcNAc cycling, O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) are in a transient complex at M phase with the mitotic kinase Aurora B and protein phosphatase 1.
18653473	3	1	theme	O-GlcNAc	513:520	arg1	OGT					535:537	OGT	535:537	OGT	535:537	Here, we demonstrate that the enzymes responsible for O-GlcNAc cycling, O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) are in a transient complex at M phase with the mitotic kinase Aurora B and protein phosphatase 1.
18653473	1	2	theme	cell	278:281	arg1	stage					289:293	cell cycle stage	278:293	cell cycle stage	278:293	O-linked beta-N-acetylglucosamine (O-GlcNAc) is a highly dynamic intracellular protein modification responsive to stress, hormones, nutrients, and cell cycle stage.
18653473	7	3	theme	mitotic	1143:1149	arg1	phosphorylation					1151:1165	mitotic phosphorylation	1143:1165	mitotic phosphorylation on multiple sites	1143:1183	Overexpression of OGT or OGA led to defects in mitotic phosphorylation on multiple sites, whereas OGT overexpression increased mitotic GlcNAcylation of vimentin.
18653473	7	4	from	phosphorylation	1151:1165	arg1	sites					1179:1183	multiple sites	1170:1183	multiple sites	1170:1183	Overexpression of OGT or OGA led to defects in mitotic phosphorylation on multiple sites, whereas OGT overexpression increased mitotic GlcNAcylation of vimentin.
18653473	1	5	theme	dynamic	188:194	arg1	modification					218:229	a highly dynamic intracellular protein modification	179:229	a highly dynamic intracellular protein modification responsive to stress, hormones, nutrients, and cell cycle stage	179:293	O-linked beta-N-acetylglucosamine (O-GlcNAc) is a highly dynamic intracellular protein modification responsive to stress, hormones, nutrients, and cell cycle stage.
18653473	1	5	theme	dynamic	188:194	arg1	beta-N-acetylglucosamine					140:163	O-linked beta-N-acetylglucosamine	131:163	O-linked beta-N-acetylglucosamine (O-GlcNAc)	131:174	O-linked beta-N-acetylglucosamine (O-GlcNAc) is a highly dynamic intracellular protein modification responsive to stress, hormones, nutrients, and cell cycle stage.
18653473	1	6	theme	cycle	283:287	arg1	stage					289:293	cell cycle stage	278:293	cell cycle stage	278:293	O-linked beta-N-acetylglucosamine (O-GlcNAc) is a highly dynamic intracellular protein modification responsive to stress, hormones, nutrients, and cell cycle stage.
18653473	0	7	theme	vimentin	121:128	arg1	state					87:91	the posttranslational state	65:91	the posttranslational state of the cytoskeletal protein vimentin	65:128	A mitotic GlcNAcylation/phosphorylation signaling complex alters the posttranslational state of the cytoskeletal protein vimentin.
18653473	7	8	from	sites	1179:1183	arg1	defects					1132:1138	defects	1132:1138	defects in mitotic phosphorylation on multiple sites	1132:1183	Overexpression of OGT or OGA led to defects in mitotic phosphorylation on multiple sites, whereas OGT overexpression increased mitotic GlcNAcylation of vimentin.
18653473	0	9	theme	protein	113:119	arg1	vimentin					121:128	the cytoskeletal protein vimentin	96:128	the cytoskeletal protein vimentin	96:128	A mitotic GlcNAcylation/phosphorylation signaling complex alters the posttranslational state of the cytoskeletal protein vimentin.
18653473	2	10	theme	O-GlcNAc	311:318	arg1	addition					320:327	O-GlcNAc addition	311:327	O-GlcNAc addition	311:327	Alterations in O-GlcNAc addition or removal (cycling) impair cell cycle progression and cytokinesis, but the mechanisms are not well understood.
18653473	7	11	theme	OGA	1121:1123	arg1	Overexpression					1096:1109	Overexpression	1096:1109	Overexpression of OGT or OGA	1096:1123	Overexpression of OGT or OGA led to defects in mitotic phosphorylation on multiple sites, whereas OGT overexpression increased mitotic GlcNAcylation of vimentin.
18653473	5	12	theme	total	870:874	arg1	levels					885:890	the total cellular levels	866:890	the total cellular levels of O-GlcNAc	866:902	The complex was stable under Aurora inhibition; however, the total cellular levels of O-GlcNAc were increased and the localization of OGT was decreased at the midbody after Aurora inhibition.
18653473	8	13	theme	late	1303:1306	arg1	phosphorylation					1316:1330	vimentin late mitotic phosphorylation	1294:1330	vimentin late mitotic phosphorylation	1294:1330	OGA inhibition caused a decrease in vimentin late mitotic phosphorylation but increased GlcNAcylation.
18653473	3	14	from	phase	594:598	arg1	complex					581:587	a transient complex	569:587	a transient complex	569:587	Here, we demonstrate that the enzymes responsible for O-GlcNAc cycling, O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) are in a transient complex at M phase with the mitotic kinase Aurora B and protein phosphatase 1.
18653473	1	15	theme	intracellular	196:208	arg1	modification					218:229	a highly dynamic intracellular protein modification	179:229	a highly dynamic intracellular protein modification responsive to stress, hormones, nutrients, and cell cycle stage	179:293	O-linked beta-N-acetylglucosamine (O-GlcNAc) is a highly dynamic intracellular protein modification responsive to stress, hormones, nutrients, and cell cycle stage.
18653473	1	15	theme	intracellular	196:208	arg1	beta-N-acetylglucosamine					140:163	O-linked beta-N-acetylglucosamine	131:163	O-linked beta-N-acetylglucosamine (O-GlcNAc)	131:174	O-linked beta-N-acetylglucosamine (O-GlcNAc) is a highly dynamic intracellular protein modification responsive to stress, hormones, nutrients, and cell cycle stage.
18653473	5	16	theme	OGT	943:945	arg1	localization					927:938	the localization	923:938	the localization of OGT	923:945	The complex was stable under Aurora inhibition; however, the total cellular levels of O-GlcNAc were increased and the localization of OGT was decreased at the midbody after Aurora inhibition.
18653473	1	17	theme	protein	210:216	arg1	modification					218:229	a highly dynamic intracellular protein modification	179:229	a highly dynamic intracellular protein modification responsive to stress, hormones, nutrients, and cell cycle stage	179:293	O-linked beta-N-acetylglucosamine (O-GlcNAc) is a highly dynamic intracellular protein modification responsive to stress, hormones, nutrients, and cell cycle stage.
18653473	1	17	theme	protein	210:216	arg1	beta-N-acetylglucosamine					140:163	O-linked beta-N-acetylglucosamine	131:163	O-linked beta-N-acetylglucosamine (O-GlcNAc)	131:174	O-linked beta-N-acetylglucosamine (O-GlcNAc) is a highly dynamic intracellular protein modification responsive to stress, hormones, nutrients, and cell cycle stage.
18653473	0	18	theme	mitotic	2:8	arg1	complex					50:56	A mitotic GlcNAcylation/phosphorylation signaling complex	0:56	A mitotic GlcNAcylation/phosphorylation signaling complex	0:56	A mitotic GlcNAcylation/phosphorylation signaling complex alters the posttranslational state of the cytoskeletal protein vimentin.
18653473	5	19	theme	O-GlcNAc	895:902	arg1	levels					885:890	the total cellular levels	866:890	the total cellular levels of O-GlcNAc	866:902	The complex was stable under Aurora inhibition; however, the total cellular levels of O-GlcNAc were increased and the localization of OGT was decreased at the midbody after Aurora inhibition.
18653473	7	20	theme	OGT	1114:1116	arg1	Overexpression					1096:1109	Overexpression	1096:1109	Overexpression of OGT or OGA	1096:1123	Overexpression of OGT or OGA led to defects in mitotic phosphorylation on multiple sites, whereas OGT overexpression increased mitotic GlcNAcylation of vimentin.
18653473	5	21	theme	Aurora	838:843	arg1	inhibition					845:854	Aurora inhibition	838:854	Aurora inhibition	838:854	The complex was stable under Aurora inhibition; however, the total cellular levels of O-GlcNAc were increased and the localization of OGT was decreased at the midbody after Aurora inhibition.
18653473	8	22	theme	mitotic	1308:1314	arg1	phosphorylation					1316:1330	vimentin late mitotic phosphorylation	1294:1330	vimentin late mitotic phosphorylation	1294:1330	OGA inhibition caused a decrease in vimentin late mitotic phosphorylation but increased GlcNAcylation.
18653473	1	23	theme	responsive	231:240	arg1	modification					218:229	a highly dynamic intracellular protein modification	179:229	a highly dynamic intracellular protein modification responsive to stress, hormones, nutrients, and cell cycle stage	179:293	O-linked beta-N-acetylglucosamine (O-GlcNAc) is a highly dynamic intracellular protein modification responsive to stress, hormones, nutrients, and cell cycle stage.
18653473	1	23	theme	responsive	231:240	arg1	beta-N-acetylglucosamine					140:163	O-linked beta-N-acetylglucosamine	131:163	O-linked beta-N-acetylglucosamine (O-GlcNAc)	131:174	O-linked beta-N-acetylglucosamine (O-GlcNAc) is a highly dynamic intracellular protein modification responsive to stress, hormones, nutrients, and cell cycle stage.
18653473	0	24	theme	signaling	40:48	arg1	complex					50:56	A mitotic GlcNAcylation/phosphorylation signaling complex	0:56	A mitotic GlcNAcylation/phosphorylation signaling complex	0:56	A mitotic GlcNAcylation/phosphorylation signaling complex alters the posttranslational state of the cytoskeletal protein vimentin.
18653473	4	25	theme	mitotic	792:798	arg1	extract					800:806	a late mitotic extract	785:806	a late mitotic extract	785:806	OGT colocalized to the midbody during telophase with Aurora B. Furthermore, these proteins coprecipitated with each other in a late mitotic extract.
18653473	8	26	theme	OGA	1258:1260	arg1	inhibition					1262:1271	OGA inhibition	1258:1271	OGA inhibition	1258:1271	OGA inhibition caused a decrease in vimentin late mitotic phosphorylation but increased GlcNAcylation.
18653473	7	27	theme	vimentin	1248:1255	arg1	GlcNAcylation					1231:1243	mitotic GlcNAcylation	1223:1243	mitotic GlcNAcylation of vimentin	1223:1255	Overexpression of OGT or OGA led to defects in mitotic phosphorylation on multiple sites, whereas OGT overexpression increased mitotic GlcNAcylation of vimentin.
18653473	0	28	theme	GlcNAcylation/phosphorylation	10:38	arg1	complex					50:56	A mitotic GlcNAcylation/phosphorylation signaling complex	0:56	A mitotic GlcNAcylation/phosphorylation signaling complex	0:56	A mitotic GlcNAcylation/phosphorylation signaling complex alters the posttranslational state of the cytoskeletal protein vimentin.
18653473	9	29	theme	vimentin	1523:1530	arg1	status					1513:1518	the posttranslational status	1491:1518	the posttranslational status of vimentin	1491:1530	Together, these data demonstrate that the O-GlcNAc cycling enzymes associate with kinases and phosphatases at M phase to regulate the posttranslational status of vimentin.
18653473	3	30	theme	Aurora	624:629	arg1	B					631:631	the mitotic kinase Aurora B	605:631	the mitotic kinase Aurora B	605:631	Here, we demonstrate that the enzymes responsible for O-GlcNAc cycling, O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) are in a transient complex at M phase with the mitotic kinase Aurora B and protein phosphatase 1.
18653473	1	31	theme	O-linked	131:138	arg1	O-GlcNAc					166:173	O-GlcNAc	166:173	O-GlcNAc	166:173	O-linked beta-N-acetylglucosamine (O-GlcNAc) is a highly dynamic intracellular protein modification responsive to stress, hormones, nutrients, and cell cycle stage.
18653473	1	31	theme	O-linked	131:138	arg1	modification					218:229	a highly dynamic intracellular protein modification	179:229	a highly dynamic intracellular protein modification responsive to stress, hormones, nutrients, and cell cycle stage	179:293	O-linked beta-N-acetylglucosamine (O-GlcNAc) is a highly dynamic intracellular protein modification responsive to stress, hormones, nutrients, and cell cycle stage.
18653473	1	31	theme	O-linked	131:138	arg1	beta-N-acetylglucosamine					140:163	O-linked beta-N-acetylglucosamine	131:163	O-linked beta-N-acetylglucosamine (O-GlcNAc)	131:174	O-linked beta-N-acetylglucosamine (O-GlcNAc) is a highly dynamic intracellular protein modification responsive to stress, hormones, nutrients, and cell cycle stage.
18653473	9	32	theme	posttranslational	1495:1511	arg1	status					1513:1518	the posttranslational status	1491:1518	the posttranslational status of vimentin	1491:1530	Together, these data demonstrate that the O-GlcNAc cycling enzymes associate with kinases and phosphatases at M phase to regulate the posttranslational status of vimentin.
18653473	3	33	theme	responsible	479:489	arg1	O-GlcNAcase					544:554	O-GlcNAcase	544:554	O-GlcNAcase (OGA)	544:560	Here, we demonstrate that the enzymes responsible for O-GlcNAc cycling, O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) are in a transient complex at M phase with the mitotic kinase Aurora B and protein phosphatase 1.
18653473	3	33	theme	responsible	479:489	arg1	transferase					522:532	O-GlcNAc transferase	513:532	O-GlcNAc transferase (OGT)	513:538	Here, we demonstrate that the enzymes responsible for O-GlcNAc cycling, O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) are in a transient complex at M phase with the mitotic kinase Aurora B and protein phosphatase 1.
18653473	3	33	theme	responsible	479:489	arg1	enzymes					471:477	the enzymes	467:477	the enzymes responsible for O-GlcNAc cycling	467:510	Here, we demonstrate that the enzymes responsible for O-GlcNAc cycling, O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) are in a transient complex at M phase with the mitotic kinase Aurora B and protein phosphatase 1.
18653473	5	34	theme	cellular	876:883	arg1	levels					885:890	the total cellular levels	866:890	the total cellular levels of O-GlcNAc	866:902	The complex was stable under Aurora inhibition; however, the total cellular levels of O-GlcNAc were increased and the localization of OGT was decreased at the midbody after Aurora inhibition.
18653473	4	35	theme	late	787:790	arg1	extract					800:806	a late mitotic extract	785:806	a late mitotic extract	785:806	OGT colocalized to the midbody during telophase with Aurora B. Furthermore, these proteins coprecipitated with each other in a late mitotic extract.
18653473	6	36	theme	intermediate	1014:1025	arg1	protein					1036:1042	an intermediate filament protein	1011:1042	an intermediate filament protein	1011:1042	Vimentin, an intermediate filament protein, is an M phase substrate for both Aurora B and OGT.
18653473	6	36	theme	intermediate	1014:1025	arg1	Vimentin					1001:1008	Vimentin	1001:1008	Vimentin	1001:1008	Vimentin, an intermediate filament protein, is an M phase substrate for both Aurora B and OGT.
18653473	3	37	theme	mitotic	609:615	arg1	B					631:631	the mitotic kinase Aurora B	605:631	the mitotic kinase Aurora B	605:631	Here, we demonstrate that the enzymes responsible for O-GlcNAc cycling, O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) are in a transient complex at M phase with the mitotic kinase Aurora B and protein phosphatase 1.
18653473	6	38	theme	filament	1027:1034	arg1	protein					1036:1042	an intermediate filament protein	1011:1042	an intermediate filament protein	1011:1042	Vimentin, an intermediate filament protein, is an M phase substrate for both Aurora B and OGT.
18653473	6	38	theme	filament	1027:1034	arg1	Vimentin					1001:1008	Vimentin	1001:1008	Vimentin	1001:1008	Vimentin, an intermediate filament protein, is an M phase substrate for both Aurora B and OGT.
18653473	0	39	theme	posttranslational	69:85	arg1	state					87:91	the posttranslational state	65:91	the posttranslational state of the cytoskeletal protein vimentin	65:128	A mitotic GlcNAcylation/phosphorylation signaling complex alters the posttranslational state of the cytoskeletal protein vimentin.
18653473	9	40	theme	O-GlcNAc	1403:1410	arg1	enzymes					1420:1426	the O-GlcNAc cycling enzymes	1399:1426	the O-GlcNAc cycling enzymes	1399:1426	Together, these data demonstrate that the O-GlcNAc cycling enzymes associate with kinases and phosphatases at M phase to regulate the posttranslational status of vimentin.
18653473	3	41	theme	kinase	617:622	arg1	B					631:631	the mitotic kinase Aurora B	605:631	the mitotic kinase Aurora B	605:631	Here, we demonstrate that the enzymes responsible for O-GlcNAc cycling, O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) are in a transient complex at M phase with the mitotic kinase Aurora B and protein phosphatase 1.
18653473	5	42	theme	Aurora	982:987	arg1	inhibition					989:998	Aurora inhibition	982:998	Aurora inhibition	982:998	The complex was stable under Aurora inhibition; however, the total cellular levels of O-GlcNAc were increased and the localization of OGT was decreased at the midbody after Aurora inhibition.
18653473	2	43	theme	cycle	362:366	arg1	progression					368:378	cell cycle progression	357:378	cell cycle progression	357:378	Alterations in O-GlcNAc addition or removal (cycling) impair cell cycle progression and cytokinesis, but the mechanisms are not well understood.
18653473	3	44	theme	transient	571:579	arg1	complex					581:587	a transient complex	569:587	a transient complex	569:587	Here, we demonstrate that the enzymes responsible for O-GlcNAc cycling, O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) are in a transient complex at M phase with the mitotic kinase Aurora B and protein phosphatase 1.
18653473	8	45	from	decrease	1282:1289	arg1	phosphorylation					1316:1330	vimentin late mitotic phosphorylation	1294:1330	vimentin late mitotic phosphorylation	1294:1330	OGA inhibition caused a decrease in vimentin late mitotic phosphorylation but increased GlcNAcylation.
18653473	2	46	theme	cell	357:360	arg1	progression					368:378	cell cycle progression	357:378	cell cycle progression	357:378	Alterations in O-GlcNAc addition or removal (cycling) impair cell cycle progression and cytokinesis, but the mechanisms are not well understood.
18653473	7	47	theme	OGT	1194:1196	arg1	overexpression					1198:1211	OGT overexpression	1194:1211	OGT overexpression	1194:1211	Overexpression of OGT or OGA led to defects in mitotic phosphorylation on multiple sites, whereas OGT overexpression increased mitotic GlcNAcylation of vimentin.
18653473	2	48	from	Alterations	296:306	arg1	removal					332:338	removal	332:338	removal (cycling)	332:348	Alterations in O-GlcNAc addition or removal (cycling) impair cell cycle progression and cytokinesis, but the mechanisms are not well understood.
18653473	2	48	from	Alterations	296:306	arg1	addition					320:327	O-GlcNAc addition	311:327	O-GlcNAc addition	311:327	Alterations in O-GlcNAc addition or removal (cycling) impair cell cycle progression and cytokinesis, but the mechanisms are not well understood.
18653473	2	48	from	Alterations	296:306	arg1	cycling					341:347	cycling	341:347	cycling	341:347	Alterations in O-GlcNAc addition or removal (cycling) impair cell cycle progression and cytokinesis, but the mechanisms are not well understood.
18653473	8	49	theme	vimentin	1294:1301	arg1	phosphorylation					1316:1330	vimentin late mitotic phosphorylation	1294:1330	vimentin late mitotic phosphorylation	1294:1330	OGA inhibition caused a decrease in vimentin late mitotic phosphorylation but increased GlcNAcylation.
18653473	7	50	from	defects	1132:1138	arg1	phosphorylation					1151:1165	mitotic phosphorylation	1143:1165	mitotic phosphorylation on multiple sites	1143:1183	Overexpression of OGT or OGA led to defects in mitotic phosphorylation on multiple sites, whereas OGT overexpression increased mitotic GlcNAcylation of vimentin.
18653473	7	50	from	defects	1132:1138	arg1	sites					1179:1183	multiple sites	1170:1183	multiple sites	1170:1183	Overexpression of OGT or OGA led to defects in mitotic phosphorylation on multiple sites, whereas OGT overexpression increased mitotic GlcNAcylation of vimentin.
18653473	3	51	theme	O-GlcNAc	495:502	arg1	cycling					504:510	O-GlcNAc cycling	495:510	O-GlcNAc cycling	495:510	Here, we demonstrate that the enzymes responsible for O-GlcNAc cycling, O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) are in a transient complex at M phase with the mitotic kinase Aurora B and protein phosphatase 1.
18653473	6	52	theme	Aurora	1078:1083	arg1	B					1085:1085	Aurora B	1078:1085	Aurora B	1078:1085	Vimentin, an intermediate filament protein, is an M phase substrate for both Aurora B and OGT.
18653473	9	53	theme	M	1471:1471	arg1	phase					1473:1477	M phase	1471:1477	M phase	1471:1477	Together, these data demonstrate that the O-GlcNAc cycling enzymes associate with kinases and phosphatases at M phase to regulate the posttranslational status of vimentin.
18653473	3	54	theme	protein	637:643	arg1	phosphatase					645:655	protein phosphatase 1	637:657	protein phosphatase 1	637:657	Here, we demonstrate that the enzymes responsible for O-GlcNAc cycling, O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) are in a transient complex at M phase with the mitotic kinase Aurora B and protein phosphatase 1.
18653473	3	55	theme	M	592:592	arg1	phase					594:598	M phase	592:598	M phase with the mitotic kinase Aurora B and protein phosphatase 1	592:657	Here, we demonstrate that the enzymes responsible for O-GlcNAc cycling, O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) are in a transient complex at M phase with the mitotic kinase Aurora B and protein phosphatase 1.
18653473	6	56	theme	phase	1053:1057	arg1	Vimentin					1001:1008	Vimentin	1001:1008	Vimentin	1001:1008	Vimentin, an intermediate filament protein, is an M phase substrate for both Aurora B and OGT.
18653473	6	56	theme	phase	1053:1057	arg1	substrate					1059:1067	an M phase substrate	1048:1067	an M phase substrate for both Aurora B and OGT	1048:1093	Vimentin, an intermediate filament protein, is an M phase substrate for both Aurora B and OGT.
18653473	3	57	with	phase	594:598	arg1	B					631:631	the mitotic kinase Aurora B	605:631	the mitotic kinase Aurora B	605:631	Here, we demonstrate that the enzymes responsible for O-GlcNAc cycling, O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) are in a transient complex at M phase with the mitotic kinase Aurora B and protein phosphatase 1.
18653473	3	57	with	phase	594:598	arg1	phosphatase					645:655	protein phosphatase 1	637:657	protein phosphatase 1	637:657	Here, we demonstrate that the enzymes responsible for O-GlcNAc cycling, O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) are in a transient complex at M phase with the mitotic kinase Aurora B and protein phosphatase 1.
18653473	1	58	link	O-linked	131:138	arg1	O-GlcNAc					166:173	O-GlcNAc	166:173	O-GlcNAc	166:173	O-linked beta-N-acetylglucosamine (O-GlcNAc) is a highly dynamic intracellular protein modification responsive to stress, hormones, nutrients, and cell cycle stage.
18653473	1	58	link	O-linked	131:138	arg1	modification					218:229	a highly dynamic intracellular protein modification	179:229	a highly dynamic intracellular protein modification responsive to stress, hormones, nutrients, and cell cycle stage	179:293	O-linked beta-N-acetylglucosamine (O-GlcNAc) is a highly dynamic intracellular protein modification responsive to stress, hormones, nutrients, and cell cycle stage.
18653473	1	58	link	O-linked	131:138	arg1	beta-N-acetylglucosamine					140:163	O-linked beta-N-acetylglucosamine	131:163	O-linked beta-N-acetylglucosamine (O-GlcNAc)	131:174	O-linked beta-N-acetylglucosamine (O-GlcNAc) is a highly dynamic intracellular protein modification responsive to stress, hormones, nutrients, and cell cycle stage.
18653473	9	59	theme	cycling	1412:1418	arg1	enzymes					1420:1426	the O-GlcNAc cycling enzymes	1399:1426	the O-GlcNAc cycling enzymes	1399:1426	Together, these data demonstrate that the O-GlcNAc cycling enzymes associate with kinases and phosphatases at M phase to regulate the posttranslational status of vimentin.
18653473	7	60	theme	mitotic	1223:1229	arg1	GlcNAcylation					1231:1243	mitotic GlcNAcylation	1223:1243	mitotic GlcNAcylation of vimentin	1223:1255	Overexpression of OGT or OGA led to defects in mitotic phosphorylation on multiple sites, whereas OGT overexpression increased mitotic GlcNAcylation of vimentin.
18653473	6	61	theme	M	1051:1051	arg1	Vimentin					1001:1008	Vimentin	1001:1008	Vimentin	1001:1008	Vimentin, an intermediate filament protein, is an M phase substrate for both Aurora B and OGT.
18653473	6	61	theme	M	1051:1051	arg1	substrate					1059:1067	an M phase substrate	1048:1067	an M phase substrate for both Aurora B and OGT	1048:1093	Vimentin, an intermediate filament protein, is an M phase substrate for both Aurora B and OGT.
18653473	7	62	theme	multiple	1170:1177	arg1	sites					1179:1183	multiple sites	1170:1183	multiple sites	1170:1183	Overexpression of OGT or OGA led to defects in mitotic phosphorylation on multiple sites, whereas OGT overexpression increased mitotic GlcNAcylation of vimentin.
20661758	0	0	theme	biochemical	76:86	arg1	study					106:110	a biochemical and bioinformatic study	74:110	Direct evidence of O-GlcNAcylation in the apicomplexan Toxoplasma gondii: a biochemical and bioinformatic study.	0:111	Direct evidence of O-GlcNAcylation in the apicomplexan Toxoplasma gondii: a biochemical and bioinformatic study.
20661758	4	1	from	occurrence	833:842	arg1	falciparum					850:859	P. falciparum	847:859	P. falciparum	847:859	In this work, we directly prove the O-GlcNAcylation in T. gondii using antibodies specifically directed against the modification and we strongly suggest its occurrence in P. falciparum.
20661758	1	2	theme	apicomplexan	161:172	arg1	gondii					124:129	Toxoplasma gondii	113:129	Toxoplasma gondii	113:129	Toxoplasma gondii and Plasmodium falciparum are apicomplexan parasites responsible for serious diseases in humans.
20661758	1	2	theme	apicomplexan	161:172	arg1	falciparum					146:155	Plasmodium falciparum	135:155	Plasmodium falciparum	135:155	Toxoplasma gondii and Plasmodium falciparum are apicomplexan parasites responsible for serious diseases in humans.
20661758	1	2	theme	apicomplexan	161:172	arg1	parasites					174:182	apicomplexan parasites	161:182	apicomplexan parasites responsible for serious diseases in humans	161:225	Toxoplasma gondii and Plasmodium falciparum are apicomplexan parasites responsible for serious diseases in humans.
20661758	8	3	from	track	1420:1424	arg1	knowledge					1433:1441	the knowledge	1429:1441	the knowledge of apicomplexans' life cycle and pathogenic potential	1429:1495	Since the O-GlcNAcylation is implicated in many biological fundamental processes this study opens a new research track in the knowledge of apicomplexans' life cycle and pathogenic potential.
20661758	8	4	theme	many	1350:1353	arg1	processes					1378:1386	many biological fundamental processes	1350:1386	many biological fundamental processes	1350:1386	Since the O-GlcNAcylation is implicated in many biological fundamental processes this study opens a new research track in the knowledge of apicomplexans' life cycle and pathogenic potential.
20661758	0	5	from	evidence	7:14	arg1	gondii					66:71	the apicomplexan Toxoplasma gondii	38:71	the apicomplexan Toxoplasma gondii	38:71	Direct evidence of O-GlcNAcylation in the apicomplexan Toxoplasma gondii: a biochemical and bioinformatic study.
20661758	8	6	theme	fundamental	1366:1376	arg1	processes					1378:1386	many biological fundamental processes	1350:1386	many biological fundamental processes	1350:1386	Since the O-GlcNAcylation is implicated in many biological fundamental processes this study opens a new research track in the knowledge of apicomplexans' life cycle and pathogenic potential.
20661758	0	7	theme	bioinformatic	92:104	arg1	study					106:110	a biochemical and bioinformatic study	74:110	Direct evidence of O-GlcNAcylation in the apicomplexan Toxoplasma gondii: a biochemical and bioinformatic study.	0:111	Direct evidence of O-GlcNAcylation in the apicomplexan Toxoplasma gondii: a biochemical and bioinformatic study.
20661758	3	8	theme	O-GlcNAc	567:574	arg1	transferase					576:586	O-GlcNAc transferase	567:586	O-GlcNAc transferase	567:586	O-GlcNAcylation is a highly dynamic PTM-regulated by the ON and OFF enzymes: O-GlcNAc transferase and O-GlcNAcase-that can compete with phosphorylation but its function remains unclear.
20661758	4	9	from	O-GlcNAcylation	712:726	arg1	gondii					734:739	T. gondii	731:739	T. gondii using antibodies specifically directed against the modification	731:803	In this work, we directly prove the O-GlcNAcylation in T. gondii using antibodies specifically directed against the modification and we strongly suggest its occurrence in P. falciparum.
20661758	3	10	theme	dynamic	518:524	arg1	PTM-regulated					526:538	a highly dynamic PTM-regulated	509:538	a highly dynamic PTM-regulated by the ON and OFF enzymes	509:564	O-GlcNAcylation is a highly dynamic PTM-regulated by the ON and OFF enzymes: O-GlcNAc transferase and O-GlcNAcase-that can compete with phosphorylation but its function remains unclear.
20661758	3	10	theme	dynamic	518:524	arg1	O-GlcNAcylation					490:504	O-GlcNAcylation	490:504	O-GlcNAcylation	490:504	O-GlcNAcylation is a highly dynamic PTM-regulated by the ON and OFF enzymes: O-GlcNAc transferase and O-GlcNAcase-that can compete with phosphorylation but its function remains unclear.
20661758	3	11	dep	enzymes	558:564	arg1	OFF					554:556	OFF	554:556	OFF	554:556	O-GlcNAcylation is a highly dynamic PTM-regulated by the ON and OFF enzymes: O-GlcNAc transferase and O-GlcNAcase-that can compete with phosphorylation but its function remains unclear.
20661758	6	12	theme	human	1110:1114	arg1	fibroblast					1125:1134	human foreskin fibroblast	1110:1134	human foreskin fibroblast	1110:1134	Using anti-OGT antibodies we were able to detect the expression of the glycosyltransferase in T. gondii cultured both in human foreskin fibroblast and in Vero cells and report its putative sequence.
20661758	1	13	theme	responsible	184:194	arg1	gondii					124:129	Toxoplasma gondii	113:129	Toxoplasma gondii	113:129	Toxoplasma gondii and Plasmodium falciparum are apicomplexan parasites responsible for serious diseases in humans.
20661758	1	13	theme	responsible	184:194	arg1	falciparum					146:155	Plasmodium falciparum	135:155	Plasmodium falciparum	135:155	Toxoplasma gondii and Plasmodium falciparum are apicomplexan parasites responsible for serious diseases in humans.
20661758	1	13	theme	responsible	184:194	arg1	parasites					174:182	apicomplexan parasites	161:182	apicomplexan parasites responsible for serious diseases in humans	161:225	Toxoplasma gondii and Plasmodium falciparum are apicomplexan parasites responsible for serious diseases in humans.
20661758	7	14	theme	O-GlcNAcylation	1223:1237	arg1	presence					1211:1218	the presence	1207:1218	the presence of O-GlcNAcylation	1207:1237	For the first time the presence of O-GlcNAcylation is unequivocally shown in T. gondii and suspected in P. falciparum.
20661758	0	15	theme	Direct	0:5	arg1	evidence					7:14	Direct evidence	0:14	Direct evidence of O-GlcNAcylation in the apicomplexan Toxoplasma gondii: a biochemical and bioinformatic study.	0:111	Direct evidence of O-GlcNAcylation in the apicomplexan Toxoplasma gondii: a biochemical and bioinformatic study.
20661758	2	16	theme	these	399:403	arg1	few					392:394	few	392:394	few	392:394	Many studies have focused on the post-translational modifications (PTMs) found in the two protists including phosphorylation, acetylation or SUMOylation but only a few of these are concerned with the nuclear and cytosolic-specific glycosylation O-GlcNAcylation.
20661758	6	17	from	expression	1042:1051	arg1	gondii					1086:1091	T. gondii	1083:1091	T. gondii cultured both in human foreskin fibroblast and in Vero cells	1083:1152	Using anti-OGT antibodies we were able to detect the expression of the glycosyltransferase in T. gondii cultured both in human foreskin fibroblast and in Vero cells and report its putative sequence.
20661758	5	18	from	T.	978:979	arg1	O-GlcNAcylated					919:932	O-GlcNAcylated	919:932	O-GlcNAcylated	919:932	We found that the inducible 70 kDa-Heat Shock Protein is O-GlcNAcylated, or associated with an O-GlcNAc-partner, in T. gondii.
20661758	8	19	theme	research	1411:1418	arg1	track					1420:1424	a new research track	1405:1424	a new research track in the knowledge of apicomplexans' life cycle and pathogenic potential	1405:1495	Since the O-GlcNAcylation is implicated in many biological fundamental processes this study opens a new research track in the knowledge of apicomplexans' life cycle and pathogenic potential.
20661758	1	20	theme	serious	200:206	arg1	diseases					208:215	serious diseases	200:215	serious diseases in humans	200:225	Toxoplasma gondii and Plasmodium falciparum are apicomplexan parasites responsible for serious diseases in humans.
20661758	2	21	theme	glycosylation	459:471	arg1	O-GlcNAcylation					473:487	the nuclear and cytosolic-specific glycosylation O-GlcNAcylation	424:487	the nuclear and cytosolic-specific glycosylation O-GlcNAcylation	424:487	Many studies have focused on the post-translational modifications (PTMs) found in the two protists including phosphorylation, acetylation or SUMOylation but only a few of these are concerned with the nuclear and cytosolic-specific glycosylation O-GlcNAcylation.
20661758	8	22	theme	new	1407:1409	arg1	track					1420:1424	a new research track	1405:1424	a new research track in the knowledge of apicomplexans' life cycle and pathogenic potential	1405:1495	Since the O-GlcNAcylation is implicated in many biological fundamental processes this study opens a new research track in the knowledge of apicomplexans' life cycle and pathogenic potential.
20661758	2	23	theme	cytosolic-specific	440:457	arg1	O-GlcNAcylation					473:487	the nuclear and cytosolic-specific glycosylation O-GlcNAcylation	424:487	the nuclear and cytosolic-specific glycosylation O-GlcNAcylation	424:487	Many studies have focused on the post-translational modifications (PTMs) found in the two protists including phosphorylation, acetylation or SUMOylation but only a few of these are concerned with the nuclear and cytosolic-specific glycosylation O-GlcNAcylation.
20661758	0	24	dep	evidence	7:14	arg1	study					106:110	a biochemical and bioinformatic study	74:110	Direct evidence of O-GlcNAcylation in the apicomplexan Toxoplasma gondii: a biochemical and bioinformatic study.	0:111	Direct evidence of O-GlcNAcylation in the apicomplexan Toxoplasma gondii: a biochemical and bioinformatic study.
20661758	2	25	theme	nuclear	428:434	arg1	O-GlcNAcylation					473:487	the nuclear and cytosolic-specific glycosylation O-GlcNAcylation	424:487	the nuclear and cytosolic-specific glycosylation O-GlcNAcylation	424:487	Many studies have focused on the post-translational modifications (PTMs) found in the two protists including phosphorylation, acetylation or SUMOylation but only a few of these are concerned with the nuclear and cytosolic-specific glycosylation O-GlcNAcylation.
20661758	8	26	theme	potential	1487:1495	arg1	knowledge					1433:1441	the knowledge	1429:1441	the knowledge of apicomplexans' life cycle and pathogenic potential	1429:1495	Since the O-GlcNAcylation is implicated in many biological fundamental processes this study opens a new research track in the knowledge of apicomplexans' life cycle and pathogenic potential.
20661758	5	27	theme	inducible	880:888	arg1	Protein					908:914	the inducible 70 kDa-Heat Shock Protein	876:914	the inducible 70 kDa-Heat Shock Protein	876:914	We found that the inducible 70 kDa-Heat Shock Protein is O-GlcNAcylated, or associated with an O-GlcNAc-partner, in T. gondii.
20661758	8	28	theme	pathogenic	1476:1485	arg1	potential					1487:1495	pathogenic potential	1476:1495	pathogenic potential	1476:1495	Since the O-GlcNAcylation is implicated in many biological fundamental processes this study opens a new research track in the knowledge of apicomplexans' life cycle and pathogenic potential.
20661758	5	29	theme	70 kDa-Heat	890:900	arg1	Protein					908:914	the inducible 70 kDa-Heat Shock Protein	876:914	the inducible 70 kDa-Heat Shock Protein	876:914	We found that the inducible 70 kDa-Heat Shock Protein is O-GlcNAcylated, or associated with an O-GlcNAc-partner, in T. gondii.
20661758	2	30	located	found	301:305	arg2	PTMs					295:298	PTMs	295:298	PTMs	295:298	Many studies have focused on the post-translational modifications (PTMs) found in the two protists including phosphorylation, acetylation or SUMOylation but only a few of these are concerned with the nuclear and cytosolic-specific glycosylation O-GlcNAcylation.
20661758	2	30	located	found	301:305	arg1	protists					318:325	the two protists	310:325	the two protists including phosphorylation, acetylation or SUMOylation	310:379	Many studies have focused on the post-translational modifications (PTMs) found in the two protists including phosphorylation, acetylation or SUMOylation but only a few of these are concerned with the nuclear and cytosolic-specific glycosylation O-GlcNAcylation.
20661758	2	30	located	found	301:305	arg1	SUMOylation					369:379	SUMOylation	369:379	SUMOylation	369:379	Many studies have focused on the post-translational modifications (PTMs) found in the two protists including phosphorylation, acetylation or SUMOylation but only a few of these are concerned with the nuclear and cytosolic-specific glycosylation O-GlcNAcylation.
20661758	2	30	located	found	301:305	arg2	modifications					280:292	the post-translational modifications	257:292	the post-translational modifications (PTMs) found in the two protists including phosphorylation, acetylation or SUMOylation	257:379	Many studies have focused on the post-translational modifications (PTMs) found in the two protists including phosphorylation, acetylation or SUMOylation but only a few of these are concerned with the nuclear and cytosolic-specific glycosylation O-GlcNAcylation.
20661758	2	30	located	found	301:305	arg1	phosphorylation					337:351	phosphorylation	337:351	phosphorylation	337:351	Many studies have focused on the post-translational modifications (PTMs) found in the two protists including phosphorylation, acetylation or SUMOylation but only a few of these are concerned with the nuclear and cytosolic-specific glycosylation O-GlcNAcylation.
20661758	2	30	located	found	301:305	arg1	acetylation					354:364	acetylation	354:364	acetylation	354:364	Many studies have focused on the post-translational modifications (PTMs) found in the two protists including phosphorylation, acetylation or SUMOylation but only a few of these are concerned with the nuclear and cytosolic-specific glycosylation O-GlcNAcylation.
20661758	0	31	theme	O-GlcNAcylation	19:33	arg1	evidence					7:14	Direct evidence	0:14	Direct evidence of O-GlcNAcylation in the apicomplexan Toxoplasma gondii: a biochemical and bioinformatic study.	0:111	Direct evidence of O-GlcNAcylation in the apicomplexan Toxoplasma gondii: a biochemical and bioinformatic study.
20661758	5	32	theme	Shock	902:906	arg1	Protein					908:914	the inducible 70 kDa-Heat Shock Protein	876:914	the inducible 70 kDa-Heat Shock Protein	876:914	We found that the inducible 70 kDa-Heat Shock Protein is O-GlcNAcylated, or associated with an O-GlcNAc-partner, in T. gondii.
20661758	0	33	theme	Toxoplasma	55:64	arg1	gondii					66:71	the apicomplexan Toxoplasma gondii	38:71	the apicomplexan Toxoplasma gondii	38:71	Direct evidence of O-GlcNAcylation in the apicomplexan Toxoplasma gondii: a biochemical and bioinformatic study.
20661758	6	34	theme	anti-OGT	995:1002	arg1	antibodies					1004:1013	anti-OGT antibodies	995:1013	anti-OGT antibodies	995:1013	Using anti-OGT antibodies we were able to detect the expression of the glycosyltransferase in T. gondii cultured both in human foreskin fibroblast and in Vero cells and report its putative sequence.
20661758	1	35	theme	Toxoplasma	113:122	arg1	gondii					124:129	Toxoplasma gondii	113:129	Toxoplasma gondii	113:129	Toxoplasma gondii and Plasmodium falciparum are apicomplexan parasites responsible for serious diseases in humans.
20661758	1	35	theme	Toxoplasma	113:122	arg1	falciparum					146:155	Plasmodium falciparum	135:155	Plasmodium falciparum	135:155	Toxoplasma gondii and Plasmodium falciparum are apicomplexan parasites responsible for serious diseases in humans.
20661758	1	35	theme	Toxoplasma	113:122	arg1	parasites					174:182	apicomplexan parasites	161:182	apicomplexan parasites responsible for serious diseases in humans	161:225	Toxoplasma gondii and Plasmodium falciparum are apicomplexan parasites responsible for serious diseases in humans.
20661758	0	36	theme	apicomplexan	42:53	arg1	gondii					66:71	the apicomplexan Toxoplasma gondii	38:71	the apicomplexan Toxoplasma gondii	38:71	Direct evidence of O-GlcNAcylation in the apicomplexan Toxoplasma gondii: a biochemical and bioinformatic study.
20661758	2	37	theme	Many	228:231	arg1	studies					233:239	Many studies	228:239	Many studies	228:239	Many studies have focused on the post-translational modifications (PTMs) found in the two protists including phosphorylation, acetylation or SUMOylation but only a few of these are concerned with the nuclear and cytosolic-specific glycosylation O-GlcNAcylation.
20661758	7	38	theme	first	1196:1200	arg1	time					1202:1205	the first time	1192:1205	the first time	1192:1205	For the first time the presence of O-GlcNAcylation is unequivocally shown in T. gondii and suspected in P. falciparum.
20661758	8	39	theme	life	1461:1464	arg1	cycle					1466:1470	apicomplexans' life cycle	1446:1470	apicomplexans' life cycle	1446:1470	Since the O-GlcNAcylation is implicated in many biological fundamental processes this study opens a new research track in the knowledge of apicomplexans' life cycle and pathogenic potential.
20661758	6	40	dep	able	1023:1026	arg1	Using					989:993	Using	989:993	Using anti-OGT antibodies	989:1013	Using anti-OGT antibodies we were able to detect the expression of the glycosyltransferase in T. gondii cultured both in human foreskin fibroblast and in Vero cells and report its putative sequence.
20661758	5	41	from	O-GlcNAcylated	919:932	arg1	T.					978:979	T.	978:979	T.	978:979	We found that the inducible 70 kDa-Heat Shock Protein is O-GlcNAcylated, or associated with an O-GlcNAc-partner, in T. gondii.
20661758	1	42	theme	Plasmodium	135:144	arg1	gondii					124:129	Toxoplasma gondii	113:129	Toxoplasma gondii	113:129	Toxoplasma gondii and Plasmodium falciparum are apicomplexan parasites responsible for serious diseases in humans.
20661758	1	42	theme	Plasmodium	135:144	arg1	falciparum					146:155	Plasmodium falciparum	135:155	Plasmodium falciparum	135:155	Toxoplasma gondii and Plasmodium falciparum are apicomplexan parasites responsible for serious diseases in humans.
20661758	1	42	theme	Plasmodium	135:144	arg1	parasites					174:182	apicomplexan parasites	161:182	apicomplexan parasites responsible for serious diseases in humans	161:225	Toxoplasma gondii and Plasmodium falciparum are apicomplexan parasites responsible for serious diseases in humans.
20661758	6	43	theme	putative	1169:1176	arg1	sequence					1178:1185	its putative sequence	1165:1185	its putative sequence	1165:1185	Using anti-OGT antibodies we were able to detect the expression of the glycosyltransferase in T. gondii cultured both in human foreskin fibroblast and in Vero cells and report its putative sequence.
20661758	6	44	theme	glycosyltransferase	1060:1078	arg1	expression					1042:1051	the expression	1038:1051	the expression of the glycosyltransferase in T. gondii cultured both in human foreskin fibroblast and in Vero cells	1038:1152	Using anti-OGT antibodies we were able to detect the expression of the glycosyltransferase in T. gondii cultured both in human foreskin fibroblast and in Vero cells and report its putative sequence.
20661758	2	45	theme	post-translational	261:278	arg1	PTMs					295:298	PTMs	295:298	PTMs	295:298	Many studies have focused on the post-translational modifications (PTMs) found in the two protists including phosphorylation, acetylation or SUMOylation but only a few of these are concerned with the nuclear and cytosolic-specific glycosylation O-GlcNAcylation.
20661758	2	45	theme	post-translational	261:278	arg1	modifications					280:292	the post-translational modifications	257:292	the post-translational modifications (PTMs) found in the two protists including phosphorylation, acetylation or SUMOylation	257:379	Many studies have focused on the post-translational modifications (PTMs) found in the two protists including phosphorylation, acetylation or SUMOylation but only a few of these are concerned with the nuclear and cytosolic-specific glycosylation O-GlcNAcylation.
20661758	1	46	from	diseases	208:215	arg1	humans					220:225	humans	220:225	humans	220:225	Toxoplasma gondii and Plasmodium falciparum are apicomplexan parasites responsible for serious diseases in humans.
20661758	8	47	theme	biological	1355:1364	arg1	processes					1378:1386	many biological fundamental processes	1350:1386	many biological fundamental processes	1350:1386	Since the O-GlcNAcylation is implicated in many biological fundamental processes this study opens a new research track in the knowledge of apicomplexans' life cycle and pathogenic potential.
20661758	6	48	theme	foreskin	1116:1123	arg1	fibroblast					1125:1134	human foreskin fibroblast	1110:1134	human foreskin fibroblast	1110:1134	Using anti-OGT antibodies we were able to detect the expression of the glycosyltransferase in T. gondii cultured both in human foreskin fibroblast and in Vero cells and report its putative sequence.
20661758	8	49	gly	O-GlcNAcylation	1317:1331	arg1	processes					1378:1386	many biological fundamental processes	1350:1386	many biological fundamental processes	1350:1386	Since the O-GlcNAcylation is implicated in many biological fundamental processes this study opens a new research track in the knowledge of apicomplexans' life cycle and pathogenic potential.
20661758	8	50	theme	cycle	1466:1470	arg1	knowledge					1433:1441	the knowledge	1429:1441	the knowledge of apicomplexans' life cycle and pathogenic potential	1429:1495	Since the O-GlcNAcylation is implicated in many biological fundamental processes this study opens a new research track in the knowledge of apicomplexans' life cycle and pathogenic potential.
20661758	6	51	theme	Vero	1143:1146	arg1	cells					1148:1152	Vero cells	1143:1152	Vero cells	1143:1152	Using anti-OGT antibodies we were able to detect the expression of the glycosyltransferase in T. gondii cultured both in human foreskin fibroblast and in Vero cells and report its putative sequence.
19302979	3	0	theme	Sp1-NF-Y	557:564	arg1	activation					578:587	Sp1-NF-Y cooperative activation	557:587	Sp1-NF-Y cooperative activation of gene transcription	557:609	In the present study, we show that O-GlcNAc of Sp1 serine/threonine-rich region interrupts a physical interaction between Sp1 and NF-YA, thus inhibiting Sp1-NF-Y cooperative activation of gene transcription.
19302979	2	1	mod	modified	300:307	arg1	factor					281:286	Sp1 transcription factor	263:286	Sp1 transcription factor	263:286	Sp1 transcription factor is multiply modified by O-GlcNAc within its serine/threonine-rich region and glutamine-rich transactivation domain.
19302979	2	1	mod	modified	300:307	arg3	O-GlcNAc					312:319	O-GlcNAc	312:319	O-GlcNAc	312:319	Sp1 transcription factor is multiply modified by O-GlcNAc within its serine/threonine-rich region and glutamine-rich transactivation domain.
19302979	3	2	theme	transcription	597:609	arg1	activation					578:587	Sp1-NF-Y cooperative activation	557:587	Sp1-NF-Y cooperative activation of gene transcription	557:609	In the present study, we show that O-GlcNAc of Sp1 serine/threonine-rich region interrupts a physical interaction between Sp1 and NF-YA, thus inhibiting Sp1-NF-Y cooperative activation of gene transcription.
19302979	3	3	theme	present	411:417	arg1	study					419:423	the present study	407:423	the present study	407:423	In the present study, we show that O-GlcNAc of Sp1 serine/threonine-rich region interrupts a physical interaction between Sp1 and NF-YA, thus inhibiting Sp1-NF-Y cooperative activation of gene transcription.
19302979	1	4	theme	O-linked	61:68	arg1	N-acetylglucosamine					70:88	O-linked N-acetylglucosamine	61:88	O-linked N-acetylglucosamine (O-GlcNAc)	61:99	O-linked N-acetylglucosamine (O-GlcNAc), a monosaccharide N-acetylglucosamine addition on nucleocytoplasmic proteins, is abundant in transcription regulators and has been implicated in gene regulation.
19302979	1	4	theme	O-linked	61:68	arg1	addition					139:146	a monosaccharide N-acetylglucosamine addition	102:146	a monosaccharide N-acetylglucosamine addition on nucleocytoplasmic proteins	102:176	O-linked N-acetylglucosamine (O-GlcNAc), a monosaccharide N-acetylglucosamine addition on nucleocytoplasmic proteins, is abundant in transcription regulators and has been implicated in gene regulation.
19302979	1	4	theme	O-linked	61:68	arg1	O-GlcNAc					91:98	O-GlcNAc	91:98	O-GlcNAc	91:98	O-linked N-acetylglucosamine (O-GlcNAc), a monosaccharide N-acetylglucosamine addition on nucleocytoplasmic proteins, is abundant in transcription regulators and has been implicated in gene regulation.
19302979	3	5	theme	serine/threonine-rich	455:475	arg1	region					477:482	Sp1 serine/threonine-rich region	451:482	Sp1 serine/threonine-rich region	451:482	In the present study, we show that O-GlcNAc of Sp1 serine/threonine-rich region interrupts a physical interaction between Sp1 and NF-YA, thus inhibiting Sp1-NF-Y cooperative activation of gene transcription.
19302979	4	6	theme	transcription	749:761	arg1	proteins					774:781	transcription regulatory proteins	749:781	transcription regulatory proteins	749:781	Our results strengthen the notion that O-GlcNAc regulates gene transcription by modulating the protein-protein interaction network among transcription regulatory proteins.
19302979	1	7	link	O-linked	61:68	arg1	N-acetylglucosamine					70:88	O-linked N-acetylglucosamine	61:88	O-linked N-acetylglucosamine (O-GlcNAc)	61:99	O-linked N-acetylglucosamine (O-GlcNAc), a monosaccharide N-acetylglucosamine addition on nucleocytoplasmic proteins, is abundant in transcription regulators and has been implicated in gene regulation.
19302979	1	7	link	O-linked	61:68	arg1	addition					139:146	a monosaccharide N-acetylglucosamine addition	102:146	a monosaccharide N-acetylglucosamine addition on nucleocytoplasmic proteins	102:176	O-linked N-acetylglucosamine (O-GlcNAc), a monosaccharide N-acetylglucosamine addition on nucleocytoplasmic proteins, is abundant in transcription regulators and has been implicated in gene regulation.
19302979	1	7	link	O-linked	61:68	arg1	O-GlcNAc					91:98	O-GlcNAc	91:98	O-GlcNAc	91:98	O-linked N-acetylglucosamine (O-GlcNAc), a monosaccharide N-acetylglucosamine addition on nucleocytoplasmic proteins, is abundant in transcription regulators and has been implicated in gene regulation.
19302979	1	8	from	addition	139:146	arg1	proteins					169:176	nucleocytoplasmic proteins	151:176	nucleocytoplasmic proteins	151:176	O-linked N-acetylglucosamine (O-GlcNAc), a monosaccharide N-acetylglucosamine addition on nucleocytoplasmic proteins, is abundant in transcription regulators and has been implicated in gene regulation.
19302979	3	9	theme	gene	592:595	arg1	transcription					597:609	gene transcription	592:609	gene transcription	592:609	In the present study, we show that O-GlcNAc of Sp1 serine/threonine-rich region interrupts a physical interaction between Sp1 and NF-YA, thus inhibiting Sp1-NF-Y cooperative activation of gene transcription.
19302979	1	10	theme	transcription	194:206	arg1	regulators					208:217	transcription regulators	194:217	transcription regulators	194:217	O-linked N-acetylglucosamine (O-GlcNAc), a monosaccharide N-acetylglucosamine addition on nucleocytoplasmic proteins, is abundant in transcription regulators and has been implicated in gene regulation.
19302979	2	11	theme	serine/threonine-rich	332:352	arg1	region					354:359	its serine/threonine-rich region	328:359	its serine/threonine-rich region	328:359	Sp1 transcription factor is multiply modified by O-GlcNAc within its serine/threonine-rich region and glutamine-rich transactivation domain.
19302979	3	12	theme	region	477:482	arg1	O-GlcNAc					439:446	O-GlcNAc	439:446	O-GlcNAc of Sp1 serine/threonine-rich region	439:482	In the present study, we show that O-GlcNAc of Sp1 serine/threonine-rich region interrupts a physical interaction between Sp1 and NF-YA, thus inhibiting Sp1-NF-Y cooperative activation of gene transcription.
19302979	4	13	theme	protein-protein	707:721	arg1	network					735:741	the protein-protein interaction network	703:741	the protein-protein interaction network among transcription regulatory proteins	703:781	Our results strengthen the notion that O-GlcNAc regulates gene transcription by modulating the protein-protein interaction network among transcription regulatory proteins.
19302979	0	14	theme	Sp1	19:21	arg1	O-GlcNAcylation					0:14	O-GlcNAcylation	0:14	O-GlcNAcylation of Sp1	0:21	O-GlcNAcylation of Sp1 interrupts Sp1 interaction with NF-Y.
19302979	3	15	theme	cooperative	566:576	arg1	activation					578:587	Sp1-NF-Y cooperative activation	557:587	Sp1-NF-Y cooperative activation of gene transcription	557:609	In the present study, we show that O-GlcNAc of Sp1 serine/threonine-rich region interrupts a physical interaction between Sp1 and NF-YA, thus inhibiting Sp1-NF-Y cooperative activation of gene transcription.
19302979	2	16	theme	transactivation	380:394	arg1	domain					396:401	glutamine-rich transactivation domain	365:401	glutamine-rich transactivation domain	365:401	Sp1 transcription factor is multiply modified by O-GlcNAc within its serine/threonine-rich region and glutamine-rich transactivation domain.
19302979	4	17	theme	regulatory	763:772	arg1	proteins					774:781	transcription regulatory proteins	749:781	transcription regulatory proteins	749:781	Our results strengthen the notion that O-GlcNAc regulates gene transcription by modulating the protein-protein interaction network among transcription regulatory proteins.
19302979	3	18	theme	physical	497:504	arg1	interaction					506:516	a physical interaction	495:516	a physical interaction between Sp1 and NF-YA	495:538	In the present study, we show that O-GlcNAc of Sp1 serine/threonine-rich region interrupts a physical interaction between Sp1 and NF-YA, thus inhibiting Sp1-NF-Y cooperative activation of gene transcription.
19302979	0	19	theme	Sp1	34:36	arg1	interaction					38:48	Sp1 interaction	34:48	Sp1 interaction with NF-Y	34:58	O-GlcNAcylation of Sp1 interrupts Sp1 interaction with NF-Y.
19302979	3	20	theme	Sp1	451:453	arg1	region					477:482	Sp1 serine/threonine-rich region	451:482	Sp1 serine/threonine-rich region	451:482	In the present study, we show that O-GlcNAc of Sp1 serine/threonine-rich region interrupts a physical interaction between Sp1 and NF-YA, thus inhibiting Sp1-NF-Y cooperative activation of gene transcription.
19302979	4	21	theme	interaction	723:733	arg1	network					735:741	the protein-protein interaction network	703:741	the protein-protein interaction network among transcription regulatory proteins	703:781	Our results strengthen the notion that O-GlcNAc regulates gene transcription by modulating the protein-protein interaction network among transcription regulatory proteins.
19302979	1	22	theme	monosaccharide	104:117	arg1	addition					139:146	a monosaccharide N-acetylglucosamine addition	102:146	a monosaccharide N-acetylglucosamine addition on nucleocytoplasmic proteins	102:176	O-linked N-acetylglucosamine (O-GlcNAc), a monosaccharide N-acetylglucosamine addition on nucleocytoplasmic proteins, is abundant in transcription regulators and has been implicated in gene regulation.
19302979	1	22	theme	monosaccharide	104:117	arg1	N-acetylglucosamine					70:88	O-linked N-acetylglucosamine	61:88	O-linked N-acetylglucosamine (O-GlcNAc)	61:99	O-linked N-acetylglucosamine (O-GlcNAc), a monosaccharide N-acetylglucosamine addition on nucleocytoplasmic proteins, is abundant in transcription regulators and has been implicated in gene regulation.
19302979	4	23	theme	gene	670:673	arg1	transcription					675:687	gene transcription	670:687	gene transcription	670:687	Our results strengthen the notion that O-GlcNAc regulates gene transcription by modulating the protein-protein interaction network among transcription regulatory proteins.
19302979	1	24	theme	N-acetylglucosamine	119:137	arg1	addition					139:146	a monosaccharide N-acetylglucosamine addition	102:146	a monosaccharide N-acetylglucosamine addition on nucleocytoplasmic proteins	102:176	O-linked N-acetylglucosamine (O-GlcNAc), a monosaccharide N-acetylglucosamine addition on nucleocytoplasmic proteins, is abundant in transcription regulators and has been implicated in gene regulation.
19302979	1	24	theme	N-acetylglucosamine	119:137	arg1	N-acetylglucosamine					70:88	O-linked N-acetylglucosamine	61:88	O-linked N-acetylglucosamine (O-GlcNAc)	61:99	O-linked N-acetylglucosamine (O-GlcNAc), a monosaccharide N-acetylglucosamine addition on nucleocytoplasmic proteins, is abundant in transcription regulators and has been implicated in gene regulation.
19302979	2	25	theme	glutamine-rich	365:378	arg1	domain					396:401	glutamine-rich transactivation domain	365:401	glutamine-rich transactivation domain	365:401	Sp1 transcription factor is multiply modified by O-GlcNAc within its serine/threonine-rich region and glutamine-rich transactivation domain.
19302979	0	26	with	interaction	38:48	arg1	NF-Y					55:58	NF-Y	55:58	NF-Y	55:58	O-GlcNAcylation of Sp1 interrupts Sp1 interaction with NF-Y.
19302979	1	27	theme	gene	246:249	arg1	regulation					251:260	gene regulation	246:260	gene regulation	246:260	O-linked N-acetylglucosamine (O-GlcNAc), a monosaccharide N-acetylglucosamine addition on nucleocytoplasmic proteins, is abundant in transcription regulators and has been implicated in gene regulation.
19302979	2	28	theme	transcription	267:279	arg1	factor					281:286	Sp1 transcription factor	263:286	Sp1 transcription factor	263:286	Sp1 transcription factor is multiply modified by O-GlcNAc within its serine/threonine-rich region and glutamine-rich transactivation domain.
19302979	1	29	from	regulators	208:217	arg1	abundant					182:189	abundant	182:189	abundant	182:189	O-linked N-acetylglucosamine (O-GlcNAc), a monosaccharide N-acetylglucosamine addition on nucleocytoplasmic proteins, is abundant in transcription regulators and has been implicated in gene regulation.
19302979	1	30	theme	nucleocytoplasmic	151:167	arg1	proteins					169:176	nucleocytoplasmic proteins	151:176	nucleocytoplasmic proteins	151:176	O-linked N-acetylglucosamine (O-GlcNAc), a monosaccharide N-acetylglucosamine addition on nucleocytoplasmic proteins, is abundant in transcription regulators and has been implicated in gene regulation.
19302979	2	31	theme	Sp1	263:265	arg1	factor					281:286	Sp1 transcription factor	263:286	Sp1 transcription factor	263:286	Sp1 transcription factor is multiply modified by O-GlcNAc within its serine/threonine-rich region and glutamine-rich transactivation domain.
19302979	1	32	from	abundant	182:189	arg1	regulators					208:217	transcription regulators	194:217	transcription regulators	194:217	O-linked N-acetylglucosamine (O-GlcNAc), a monosaccharide N-acetylglucosamine addition on nucleocytoplasmic proteins, is abundant in transcription regulators and has been implicated in gene regulation.
17614351	4	0	theme	expressing	570:579	arg1	cells					581:585	expressing cells	570:585	The antisense mRNA glutaminase expressing cells	539:585	The antisense mRNA glutaminase expressing cells, named ORF19, presented a 50% lower proliferation rate than parental cells, showing a more differentiated phenotype.
17614351	10	1	theme	proteins	1503:1510	arg1	detection					1471:1479	the detection	1467:1479	the detection of two new OGT target proteins: the chaperonin TCP-1 theta and the oncogene Ets-related protein isoform 7	1467:1585	Proteome analysis of O-glycosylated proteins permitted the detection of two new OGT target proteins: the chaperonin TCP-1 theta and the oncogene Ets-related protein isoform 7.
17614351	6	2	theme	protein	879:885	arg1	O-glycosylation					887:901	the overall cellular protein O-glycosylation	858:901	the overall cellular protein O-glycosylation	858:901	Although the overall cellular protein O-glycosylation did not change, the O-glycosylation status of several key proteins was altered.
17614351	3	3	theme	O-glycosylation	522:536	arg1	pattern					503:509	the pattern	499:509	the pattern of protein O-glycosylation	499:536	We have carried out the antisense L-type glutaminase inhibition in human MCF7 breast cancer cells, in order to study its effect on the hexosamine pathway and the pattern of protein O-glycosylation.
17614351	3	3	theme	O-glycosylation	522:536	arg1	effect					462:467	its effect	458:467	its effect on the hexosamine pathway	458:493	We have carried out the antisense L-type glutaminase inhibition in human MCF7 breast cancer cells, in order to study its effect on the hexosamine pathway and the pattern of protein O-glycosylation.
17614351	9	4	theme	Sp1	1382:1384	arg1	activity					1402:1409	a higher Sp1 transcriptional activity	1373:1409	a higher Sp1 transcriptional activity	1373:1409	These changes were accompanied by a higher Sp1 transcriptional activity.
17614351	8	5	from	increase	1188:1195	arg1	ratio					1250:1254	the ratio	1246:1254	the ratio of O-glycosylated to total protein for both Sp1 and the Rpt2 proteasome component	1246:1336	Inhibition of glutaminase also provoked a 10-fold increase in Sp1 expression, and a significant decrease in the ratio of O-glycosylated to total protein for both Sp1 and the Rpt2 proteasome component.
17614351	8	5	from	increase	1188:1195	arg1	expression					1204:1213	Sp1 expression	1200:1213	Sp1 expression	1200:1213	Inhibition of glutaminase also provoked a 10-fold increase in Sp1 expression, and a significant decrease in the ratio of O-glycosylated to total protein for both Sp1 and the Rpt2 proteasome component.
17614351	10	6	theme	TCP-1	1528:1532	arg1	theta					1534:1538	the chaperonin TCP-1 theta	1513:1538	the chaperonin TCP-1 theta	1513:1538	Proteome analysis of O-glycosylated proteins permitted the detection of two new OGT target proteins: the chaperonin TCP-1 theta and the oncogene Ets-related protein isoform 7.
17614351	10	6	theme	TCP-1	1528:1532	arg1	proteins					1503:1510	two new OGT target proteins	1484:1510	two new OGT target proteins: the chaperonin TCP-1 theta and the oncogene Ets-related protein isoform 7	1484:1585	Proteome analysis of O-glycosylated proteins permitted the detection of two new OGT target proteins: the chaperonin TCP-1 theta and the oncogene Ets-related protein isoform 7.
17614351	5	7	theme	hexosamine	829:838	arg1	pathway					840:846	the hexosamine pathway	825:846	the hexosamine pathway	825:846	ORF19 cells had an 80% reduction in glutamine:fructose-6-P amidotransferase activity, which is the rate-limiting step of the hexosamine pathway.
17614351	8	8	theme	glutaminase	1152:1162	arg1	Inhibition					1138:1147	Inhibition	1138:1147	Inhibition of glutaminase	1138:1162	Inhibition of glutaminase also provoked a 10-fold increase in Sp1 expression, and a significant decrease in the ratio of O-glycosylated to total protein for both Sp1 and the Rpt2 proteasome component.
17614351	4	9	theme	parental	647:654	arg1	cells					656:660	parental cells	647:660	parental cells	647:660	The antisense mRNA glutaminase expressing cells, named ORF19, presented a 50% lower proliferation rate than parental cells, showing a more differentiated phenotype.
17614351	10	10	theme	protein	1569:1575	arg1	proteins					1503:1510	two new OGT target proteins	1484:1510	two new OGT target proteins: the chaperonin TCP-1 theta and the oncogene Ets-related protein isoform 7	1484:1585	Proteome analysis of O-glycosylated proteins permitted the detection of two new OGT target proteins: the chaperonin TCP-1 theta and the oncogene Ets-related protein isoform 7.
17614351	10	10	theme	protein	1569:1575	arg1	isoform					1577:1583	the oncogene Ets-related protein isoform 7	1544:1585	the oncogene Ets-related protein isoform 7	1544:1585	Proteome analysis of O-glycosylated proteins permitted the detection of two new OGT target proteins: the chaperonin TCP-1 theta and the oncogene Ets-related protein isoform 7.
17614351	2	11	theme	glutamine	302:310	arg1	consumption					312:322	glutamine consumption	302:322	glutamine consumption	302:322	Glutaminase is the main glutamine-utilizing enzyme in these cells, and its activity correlates with glutamine consumption and growth rate.
17614351	6	12	theme	several	949:955	arg1	proteins					961:968	several key proteins	949:968	several key proteins	949:968	Although the overall cellular protein O-glycosylation did not change, the O-glycosylation status of several key proteins was altered.
17614351	8	13	theme	significant	1222:1232	arg1	decrease					1234:1241	a significant decrease	1220:1241	a significant decrease in the ratio of O-glycosylated to total protein for both Sp1 and the Rpt2 proteasome component	1220:1336	Inhibition of glutaminase also provoked a 10-fold increase in Sp1 expression, and a significant decrease in the ratio of O-glycosylated to total protein for both Sp1 and the Rpt2 proteasome component.
17614351	10	14	theme	oncogene	1548:1555	arg1	proteins					1503:1510	two new OGT target proteins	1484:1510	two new OGT target proteins: the chaperonin TCP-1 theta and the oncogene Ets-related protein isoform 7	1484:1585	Proteome analysis of O-glycosylated proteins permitted the detection of two new OGT target proteins: the chaperonin TCP-1 theta and the oncogene Ets-related protein isoform 7.
17614351	10	14	theme	oncogene	1548:1555	arg1	isoform					1577:1583	the oncogene Ets-related protein isoform 7	1544:1585	the oncogene Ets-related protein isoform 7	1544:1585	Proteome analysis of O-glycosylated proteins permitted the detection of two new OGT target proteins: the chaperonin TCP-1 theta and the oncogene Ets-related protein isoform 7.
17614351	11	15	theme	cell	1755:1758	arg1	states					1741:1746	the nutritional and energetic states	1711:1746	the nutritional and energetic states of the cell	1711:1758	Taken together, our results support the hexosamine pathway and the O-glycosylation of proteins being a sensor mechanism of the nutritional and energetic states of the cell.
17614351	5	16	theme	rate-limiting	803:815	arg1	step					817:820	the rate-limiting step	799:820	the rate-limiting step of the hexosamine pathway	799:846	ORF19 cells had an 80% reduction in glutamine:fructose-6-P amidotransferase activity, which is the rate-limiting step of the hexosamine pathway.
17614351	5	16	theme	rate-limiting	803:815	arg1	reduction					727:735	an 80% reduction	720:735	an 80% reduction	720:735	ORF19 cells had an 80% reduction in glutamine:fructose-6-P amidotransferase activity, which is the rate-limiting step of the hexosamine pathway.
17614351	8	17	theme	10-fold	1180:1186	arg1	increase					1188:1195	a 10-fold increase	1178:1195	a 10-fold increase in Sp1 expression	1178:1213	Inhibition of glutaminase also provoked a 10-fold increase in Sp1 expression, and a significant decrease in the ratio of O-glycosylated to total protein for both Sp1 and the Rpt2 proteasome component.
17614351	4	18	theme	lower	617:621	arg1	rate					637:640	a 50% lower proliferation rate	611:640	a 50% lower proliferation rate than parental cells	611:660	The antisense mRNA glutaminase expressing cells, named ORF19, presented a 50% lower proliferation rate than parental cells, showing a more differentiated phenotype.
17614351	2	19	theme	main	221:224	arg1	enzyme					246:251	the main glutamine-utilizing enzyme	217:251	the main glutamine-utilizing enzyme in these cells	217:266	Glutaminase is the main glutamine-utilizing enzyme in these cells, and its activity correlates with glutamine consumption and growth rate.
17614351	2	19	theme	main	221:224	arg1	Glutaminase					202:212	Glutaminase	202:212	Glutaminase	202:212	Glutaminase is the main glutamine-utilizing enzyme in these cells, and its activity correlates with glutamine consumption and growth rate.
17614351	7	20	theme	O-GlcNAc	1002:1009	arg1	enzyme					1034:1039	the enzyme	1030:1039	the enzyme that links N-acetylglucosamine to proteins	1030:1082	O-glycosylation of O-GlcNAc transferase (OGT), the enzyme that links N-acetylglucosamine to proteins, was fivefold lower in ORF19 than in wild type cells.
17614351	7	20	theme	O-GlcNAc	1002:1009	arg1	OGT					1024:1026	OGT	1024:1026	OGT	1024:1026	O-glycosylation of O-GlcNAc transferase (OGT), the enzyme that links N-acetylglucosamine to proteins, was fivefold lower in ORF19 than in wild type cells.
17614351	7	20	theme	O-GlcNAc	1002:1009	arg1	transferase					1011:1021	O-GlcNAc transferase	1002:1021	O-GlcNAc transferase (OGT)	1002:1027	O-glycosylation of O-GlcNAc transferase (OGT), the enzyme that links N-acetylglucosamine to proteins, was fivefold lower in ORF19 than in wild type cells.
17614351	4	21	theme	differentiated	678:691	arg1	phenotype					693:701	a more differentiated phenotype	671:701	a more differentiated phenotype	671:701	The antisense mRNA glutaminase expressing cells, named ORF19, presented a 50% lower proliferation rate than parental cells, showing a more differentiated phenotype.
17614351	10	22	dep	proteins	1503:1510	arg1	theta					1534:1538	the chaperonin TCP-1 theta	1513:1538	the chaperonin TCP-1 theta	1513:1538	Proteome analysis of O-glycosylated proteins permitted the detection of two new OGT target proteins: the chaperonin TCP-1 theta and the oncogene Ets-related protein isoform 7.
17614351	10	22	dep	proteins	1503:1510	arg1	proteins					1503:1510	two new OGT target proteins	1484:1510	two new OGT target proteins: the chaperonin TCP-1 theta and the oncogene Ets-related protein isoform 7	1484:1585	Proteome analysis of O-glycosylated proteins permitted the detection of two new OGT target proteins: the chaperonin TCP-1 theta and the oncogene Ets-related protein isoform 7.
17614351	10	22	dep	proteins	1503:1510	arg1	isoform					1577:1583	the oncogene Ets-related protein isoform 7	1544:1585	the oncogene Ets-related protein isoform 7	1544:1585	Proteome analysis of O-glycosylated proteins permitted the detection of two new OGT target proteins: the chaperonin TCP-1 theta and the oncogene Ets-related protein isoform 7.
17614351	5	23	from	reduction	727:735	arg1	activity					780:787	glutamine:fructose-6-P amidotransferase activity	740:787	glutamine:fructose-6-P amidotransferase activity	740:787	ORF19 cells had an 80% reduction in glutamine:fructose-6-P amidotransferase activity, which is the rate-limiting step of the hexosamine pathway.
17614351	8	24	theme	O-glycosylated	1259:1272	arg1	ratio					1250:1254	the ratio	1246:1254	the ratio of O-glycosylated to total protein for both Sp1 and the Rpt2 proteasome component	1246:1336	Inhibition of glutaminase also provoked a 10-fold increase in Sp1 expression, and a significant decrease in the ratio of O-glycosylated to total protein for both Sp1 and the Rpt2 proteasome component.
17614351	11	25	theme	nutritional	1715:1725	arg1	states					1741:1746	the nutritional and energetic states	1711:1746	the nutritional and energetic states of the cell	1711:1758	Taken together, our results support the hexosamine pathway and the O-glycosylation of proteins being a sensor mechanism of the nutritional and energetic states of the cell.
17614351	10	26	theme	new	1488:1490	arg1	theta					1534:1538	the chaperonin TCP-1 theta	1513:1538	the chaperonin TCP-1 theta	1513:1538	Proteome analysis of O-glycosylated proteins permitted the detection of two new OGT target proteins: the chaperonin TCP-1 theta and the oncogene Ets-related protein isoform 7.
17614351	10	26	theme	new	1488:1490	arg1	proteins					1503:1510	two new OGT target proteins	1484:1510	two new OGT target proteins: the chaperonin TCP-1 theta and the oncogene Ets-related protein isoform 7	1484:1585	Proteome analysis of O-glycosylated proteins permitted the detection of two new OGT target proteins: the chaperonin TCP-1 theta and the oncogene Ets-related protein isoform 7.
17614351	10	26	theme	new	1488:1490	arg1	isoform					1577:1583	the oncogene Ets-related protein isoform 7	1544:1585	the oncogene Ets-related protein isoform 7	1544:1585	Proteome analysis of O-glycosylated proteins permitted the detection of two new OGT target proteins: the chaperonin TCP-1 theta and the oncogene Ets-related protein isoform 7.
17614351	0	27	from	pathway	95:101	arg1	cells					120:124	breast cancer cells	106:124	breast cancer cells	106:124	Antisense glutaminase inhibition modifies the O-GlcNAc pattern and flux through the hexosamine pathway in breast cancer cells.
17614351	8	28	theme	total	1277:1281	arg1	protein					1283:1289	total protein	1277:1289	total protein for both Sp1 and the Rpt2 proteasome component	1277:1336	Inhibition of glutaminase also provoked a 10-fold increase in Sp1 expression, and a significant decrease in the ratio of O-glycosylated to total protein for both Sp1 and the Rpt2 proteasome component.
17614351	5	29	theme	%	725:725	arg1	step					817:820	the rate-limiting step	799:820	the rate-limiting step of the hexosamine pathway	799:846	ORF19 cells had an 80% reduction in glutamine:fructose-6-P amidotransferase activity, which is the rate-limiting step of the hexosamine pathway.
17614351	5	29	theme	%	725:725	arg1	reduction					727:735	an 80% reduction	720:735	an 80% reduction	720:735	ORF19 cells had an 80% reduction in glutamine:fructose-6-P amidotransferase activity, which is the rate-limiting step of the hexosamine pathway.
17614351	3	30	from	inhibition	394:403	arg1	cells					433:437	human MCF7 breast cancer cells	408:437	human MCF7 breast cancer cells	408:437	We have carried out the antisense L-type glutaminase inhibition in human MCF7 breast cancer cells, in order to study its effect on the hexosamine pathway and the pattern of protein O-glycosylation.
17614351	10	31	theme	Proteome	1412:1419	arg1	analysis					1421:1428	Proteome analysis	1412:1428	Proteome analysis of O-glycosylated proteins	1412:1455	Proteome analysis of O-glycosylated proteins permitted the detection of two new OGT target proteins: the chaperonin TCP-1 theta and the oncogene Ets-related protein isoform 7.
17614351	11	32	gly	O-glycosylation	1655:1669	arg1	proteins					1674:1681	proteins	1674:1681	proteins	1674:1681	Taken together, our results support the hexosamine pathway and the O-glycosylation of proteins being a sensor mechanism of the nutritional and energetic states of the cell.
17614351	11	33	theme	energetic	1731:1739	arg1	states					1741:1746	the nutritional and energetic states	1711:1746	the nutritional and energetic states of the cell	1711:1758	Taken together, our results support the hexosamine pathway and the O-glycosylation of proteins being a sensor mechanism of the nutritional and energetic states of the cell.
17614351	6	34	theme	proteins	961:968	arg1	status					939:944	the O-glycosylation status	919:944	the O-glycosylation status of several key proteins	919:968	Although the overall cellular protein O-glycosylation did not change, the O-glycosylation status of several key proteins was altered.
17614351	5	35	contain	had	716:718	arg2	reduction					727:735	an 80% reduction	720:735	an 80% reduction	720:735	ORF19 cells had an 80% reduction in glutamine:fructose-6-P amidotransferase activity, which is the rate-limiting step of the hexosamine pathway.
17614351	5	35	contain	had	716:718	arg1	cells					710:714	ORF19 cells	704:714	ORF19 cells	704:714	ORF19 cells had an 80% reduction in glutamine:fructose-6-P amidotransferase activity, which is the rate-limiting step of the hexosamine pathway.
17614351	5	35	contain	had	716:718	arg2	step					817:820	the rate-limiting step	799:820	the rate-limiting step of the hexosamine pathway	799:846	ORF19 cells had an 80% reduction in glutamine:fructose-6-P amidotransferase activity, which is the rate-limiting step of the hexosamine pathway.
17614351	10	36	theme	proteins	1448:1455	arg1	analysis					1421:1428	Proteome analysis	1412:1428	Proteome analysis of O-glycosylated proteins	1412:1455	Proteome analysis of O-glycosylated proteins permitted the detection of two new OGT target proteins: the chaperonin TCP-1 theta and the oncogene Ets-related protein isoform 7.
17614351	0	37	theme	breast	106:111	arg1	cells					120:124	breast cancer cells	106:124	breast cancer cells	106:124	Antisense glutaminase inhibition modifies the O-GlcNAc pattern and flux through the hexosamine pathway in breast cancer cells.
17614351	0	38	theme	O-GlcNAc	46:53	arg1	pattern					55:61	the O-GlcNAc pattern	42:61	the O-GlcNAc pattern	42:61	Antisense glutaminase inhibition modifies the O-GlcNAc pattern and flux through the hexosamine pathway in breast cancer cells.
17614351	3	39	theme	L-type	375:380	arg1	inhibition					394:403	the antisense L-type glutaminase inhibition	361:403	the antisense L-type glutaminase inhibition in human MCF7 breast cancer cells	361:437	We have carried out the antisense L-type glutaminase inhibition in human MCF7 breast cancer cells, in order to study its effect on the hexosamine pathway and the pattern of protein O-glycosylation.
17614351	8	40	theme	proteasome	1317:1326	arg1	component					1328:1336	the Rpt2 proteasome component	1308:1336	the Rpt2 proteasome component	1308:1336	Inhibition of glutaminase also provoked a 10-fold increase in Sp1 expression, and a significant decrease in the ratio of O-glycosylated to total protein for both Sp1 and the Rpt2 proteasome component.
17614351	6	41	theme	overall	862:868	arg1	O-glycosylation					887:901	the overall cellular protein O-glycosylation	858:901	the overall cellular protein O-glycosylation	858:901	Although the overall cellular protein O-glycosylation did not change, the O-glycosylation status of several key proteins was altered.
17614351	3	42	theme	breast	419:424	arg1	cells					433:437	human MCF7 breast cancer cells	408:437	human MCF7 breast cancer cells	408:437	We have carried out the antisense L-type glutaminase inhibition in human MCF7 breast cancer cells, in order to study its effect on the hexosamine pathway and the pattern of protein O-glycosylation.
17614351	0	43	theme	Antisense	0:8	arg1	inhibition					22:31	Antisense glutaminase inhibition	0:31	Antisense glutaminase inhibition	0:31	Antisense glutaminase inhibition modifies the O-GlcNAc pattern and flux through the hexosamine pathway in breast cancer cells.
17614351	3	44	gly	O-glycosylation	522:536	arg1	hexosamine					476:485	the hexosamine pathway	472:493	the hexosamine pathway	472:493	We have carried out the antisense L-type glutaminase inhibition in human MCF7 breast cancer cells, in order to study its effect on the hexosamine pathway and the pattern of protein O-glycosylation.
17614351	3	45	theme	human	408:412	arg1	cells					433:437	human MCF7 breast cancer cells	408:437	human MCF7 breast cancer cells	408:437	We have carried out the antisense L-type glutaminase inhibition in human MCF7 breast cancer cells, in order to study its effect on the hexosamine pathway and the pattern of protein O-glycosylation.
17614351	4	46	theme	antisense	543:551	arg1	glutaminase					558:568	The antisense mRNA glutaminase	539:568	The antisense mRNA glutaminase expressing cells	539:585	The antisense mRNA glutaminase expressing cells, named ORF19, presented a 50% lower proliferation rate than parental cells, showing a more differentiated phenotype.
17614351	11	47	theme	proteins	1674:1681	arg1	pathway					1639:1645	the hexosamine pathway	1624:1645	the hexosamine pathway	1624:1645	Taken together, our results support the hexosamine pathway and the O-glycosylation of proteins being a sensor mechanism of the nutritional and energetic states of the cell.
17614351	11	47	theme	proteins	1674:1681	arg1	O-glycosylation					1655:1669	the O-glycosylation	1651:1669	the O-glycosylation of proteins	1651:1681	Taken together, our results support the hexosamine pathway and the O-glycosylation of proteins being a sensor mechanism of the nutritional and energetic states of the cell.
17614351	7	48	theme	wild	1121:1124	arg1	cells					1131:1135	wild type cells	1121:1135	wild type cells	1121:1135	O-glycosylation of O-GlcNAc transferase (OGT), the enzyme that links N-acetylglucosamine to proteins, was fivefold lower in ORF19 than in wild type cells.
17614351	10	49	theme	target	1496:1501	arg1	theta					1534:1538	the chaperonin TCP-1 theta	1513:1538	the chaperonin TCP-1 theta	1513:1538	Proteome analysis of O-glycosylated proteins permitted the detection of two new OGT target proteins: the chaperonin TCP-1 theta and the oncogene Ets-related protein isoform 7.
17614351	10	49	theme	target	1496:1501	arg1	proteins					1503:1510	two new OGT target proteins	1484:1510	two new OGT target proteins: the chaperonin TCP-1 theta and the oncogene Ets-related protein isoform 7	1484:1585	Proteome analysis of O-glycosylated proteins permitted the detection of two new OGT target proteins: the chaperonin TCP-1 theta and the oncogene Ets-related protein isoform 7.
17614351	10	49	theme	target	1496:1501	arg1	isoform					1577:1583	the oncogene Ets-related protein isoform 7	1544:1585	the oncogene Ets-related protein isoform 7	1544:1585	Proteome analysis of O-glycosylated proteins permitted the detection of two new OGT target proteins: the chaperonin TCP-1 theta and the oncogene Ets-related protein isoform 7.
17614351	5	50	theme	amidotransferase	763:778	arg1	activity					780:787	glutamine:fructose-6-P amidotransferase activity	740:787	glutamine:fructose-6-P amidotransferase activity	740:787	ORF19 cells had an 80% reduction in glutamine:fructose-6-P amidotransferase activity, which is the rate-limiting step of the hexosamine pathway.
17614351	10	51	gly	O-glycosylated	1433:1446	arg1	proteins					1448:1455	O-glycosylated proteins	1433:1455	O-glycosylated proteins	1433:1455	Proteome analysis of O-glycosylated proteins permitted the detection of two new OGT target proteins: the chaperonin TCP-1 theta and the oncogene Ets-related protein isoform 7.
17614351	7	52	gly	O-glycosylation	983:997	arg1	enzyme					1034:1039	the enzyme	1030:1039	the enzyme that links N-acetylglucosamine to proteins	1030:1082	O-glycosylation of O-GlcNAc transferase (OGT), the enzyme that links N-acetylglucosamine to proteins, was fivefold lower in ORF19 than in wild type cells.
17614351	7	52	gly	O-glycosylation	983:997	arg1	OGT					1024:1026	OGT	1024:1026	OGT	1024:1026	O-glycosylation of O-GlcNAc transferase (OGT), the enzyme that links N-acetylglucosamine to proteins, was fivefold lower in ORF19 than in wild type cells.
17614351	7	52	gly	O-glycosylation	983:997	arg1	transferase					1011:1021	O-GlcNAc transferase	1002:1021	O-GlcNAc transferase (OGT)	1002:1027	O-glycosylation of O-GlcNAc transferase (OGT), the enzyme that links N-acetylglucosamine to proteins, was fivefold lower in ORF19 than in wild type cells.
17614351	3	53	dep	carried	349:355	arg1	out					357:359	out	357:359	out	357:359	We have carried out the antisense L-type glutaminase inhibition in human MCF7 breast cancer cells, in order to study its effect on the hexosamine pathway and the pattern of protein O-glycosylation.
17614351	2	54	theme	growth	328:333	arg1	rate					335:338	growth rate	328:338	growth rate	328:338	Glutaminase is the main glutamine-utilizing enzyme in these cells, and its activity correlates with glutamine consumption and growth rate.
17614351	10	55	theme	chaperonin	1517:1526	arg1	theta					1534:1538	the chaperonin TCP-1 theta	1513:1538	the chaperonin TCP-1 theta	1513:1538	Proteome analysis of O-glycosylated proteins permitted the detection of two new OGT target proteins: the chaperonin TCP-1 theta and the oncogene Ets-related protein isoform 7.
17614351	10	55	theme	chaperonin	1517:1526	arg1	proteins					1503:1510	two new OGT target proteins	1484:1510	two new OGT target proteins: the chaperonin TCP-1 theta and the oncogene Ets-related protein isoform 7	1484:1585	Proteome analysis of O-glycosylated proteins permitted the detection of two new OGT target proteins: the chaperonin TCP-1 theta and the oncogene Ets-related protein isoform 7.
17614351	4	56	theme	proliferation	623:635	arg1	rate					637:640	a 50% lower proliferation rate	611:640	a 50% lower proliferation rate than parental cells	611:660	The antisense mRNA glutaminase expressing cells, named ORF19, presented a 50% lower proliferation rate than parental cells, showing a more differentiated phenotype.
17614351	3	57	theme	hexosamine	476:485	arg1	pathway					487:493	the hexosamine pathway	472:493	the hexosamine pathway	472:493	We have carried out the antisense L-type glutaminase inhibition in human MCF7 breast cancer cells, in order to study its effect on the hexosamine pathway and the pattern of protein O-glycosylation.
17614351	6	58	gly	O-glycosylation	923:937	arg1	proteins					961:968	several key proteins	949:968	several key proteins	949:968	Although the overall cellular protein O-glycosylation did not change, the O-glycosylation status of several key proteins was altered.
17614351	3	59	theme	protein	514:520	arg1	O-glycosylation					522:536	protein O-glycosylation	514:536	protein O-glycosylation	514:536	We have carried out the antisense L-type glutaminase inhibition in human MCF7 breast cancer cells, in order to study its effect on the hexosamine pathway and the pattern of protein O-glycosylation.
17614351	9	60	theme	higher	1375:1380	arg1	activity					1402:1409	a higher Sp1 transcriptional activity	1373:1409	a higher Sp1 transcriptional activity	1373:1409	These changes were accompanied by a higher Sp1 transcriptional activity.
17614351	6	61	theme	cellular	870:877	arg1	O-glycosylation					887:901	the overall cellular protein O-glycosylation	858:901	the overall cellular protein O-glycosylation	858:901	Although the overall cellular protein O-glycosylation did not change, the O-glycosylation status of several key proteins was altered.
17614351	9	62	theme	transcriptional	1386:1400	arg1	activity					1402:1409	a higher Sp1 transcriptional activity	1373:1409	a higher Sp1 transcriptional activity	1373:1409	These changes were accompanied by a higher Sp1 transcriptional activity.
17614351	8	63	theme	Sp1	1200:1202	arg1	expression					1204:1213	Sp1 expression	1200:1213	Sp1 expression	1200:1213	Inhibition of glutaminase also provoked a 10-fold increase in Sp1 expression, and a significant decrease in the ratio of O-glycosylated to total protein for both Sp1 and the Rpt2 proteasome component.
17614351	11	64	theme	hexosamine	1628:1637	arg1	pathway					1639:1645	the hexosamine pathway	1624:1645	the hexosamine pathway	1624:1645	Taken together, our results support the hexosamine pathway and the O-glycosylation of proteins being a sensor mechanism of the nutritional and energetic states of the cell.
17614351	3	65	from	effect	462:467	arg1	pathway					487:493	the hexosamine pathway	472:493	the hexosamine pathway	472:493	We have carried out the antisense L-type glutaminase inhibition in human MCF7 breast cancer cells, in order to study its effect on the hexosamine pathway and the pattern of protein O-glycosylation.
17614351	5	66	theme	pathway	840:846	arg1	step					817:820	the rate-limiting step	799:820	the rate-limiting step of the hexosamine pathway	799:846	ORF19 cells had an 80% reduction in glutamine:fructose-6-P amidotransferase activity, which is the rate-limiting step of the hexosamine pathway.
17614351	5	66	theme	pathway	840:846	arg1	reduction					727:735	an 80% reduction	720:735	an 80% reduction	720:735	ORF19 cells had an 80% reduction in glutamine:fructose-6-P amidotransferase activity, which is the rate-limiting step of the hexosamine pathway.
17614351	6	67	theme	key	957:959	arg1	proteins					961:968	several key proteins	949:968	several key proteins	949:968	Although the overall cellular protein O-glycosylation did not change, the O-glycosylation status of several key proteins was altered.
17614351	7	68	attach	links	1046:1050	arg1	proteins					1075:1082	proteins	1075:1082	proteins	1075:1082	O-glycosylation of O-GlcNAc transferase (OGT), the enzyme that links N-acetylglucosamine to proteins, was fivefold lower in ORF19 than in wild type cells.
17614351	7	68	attach	links	1046:1050	arg2	transferase					1011:1021	O-GlcNAc transferase	1002:1021	O-GlcNAc transferase (OGT)	1002:1027	O-glycosylation of O-GlcNAc transferase (OGT), the enzyme that links N-acetylglucosamine to proteins, was fivefold lower in ORF19 than in wild type cells.
17614351	7	68	attach	links	1046:1050	arg2	enzyme					1034:1039	the enzyme	1030:1039	the enzyme that links N-acetylglucosamine to proteins	1030:1082	O-glycosylation of O-GlcNAc transferase (OGT), the enzyme that links N-acetylglucosamine to proteins, was fivefold lower in ORF19 than in wild type cells.
17614351	10	69	theme	Ets-related	1557:1567	arg1	proteins					1503:1510	two new OGT target proteins	1484:1510	two new OGT target proteins: the chaperonin TCP-1 theta and the oncogene Ets-related protein isoform 7	1484:1585	Proteome analysis of O-glycosylated proteins permitted the detection of two new OGT target proteins: the chaperonin TCP-1 theta and the oncogene Ets-related protein isoform 7.
17614351	10	69	theme	Ets-related	1557:1567	arg1	isoform					1577:1583	the oncogene Ets-related protein isoform 7	1544:1585	the oncogene Ets-related protein isoform 7	1544:1585	Proteome analysis of O-glycosylated proteins permitted the detection of two new OGT target proteins: the chaperonin TCP-1 theta and the oncogene Ets-related protein isoform 7.
17614351	1	70	theme	dividing	186:193	arg1	cells					195:199	rapidly dividing cells	178:199	rapidly dividing cells	178:199	Glutamine behaves as a key nutrient for tumors and rapidly dividing cells.
17614351	2	71	theme	glutamine-utilizing	226:244	arg1	enzyme					246:251	the main glutamine-utilizing enzyme	217:251	the main glutamine-utilizing enzyme in these cells	217:266	Glutaminase is the main glutamine-utilizing enzyme in these cells, and its activity correlates with glutamine consumption and growth rate.
17614351	2	71	theme	glutamine-utilizing	226:244	arg1	Glutaminase					202:212	Glutaminase	202:212	Glutaminase	202:212	Glutaminase is the main glutamine-utilizing enzyme in these cells, and its activity correlates with glutamine consumption and growth rate.
17614351	6	72	theme	O-glycosylation	923:937	arg1	status					939:944	the O-glycosylation status	919:944	the O-glycosylation status of several key proteins	919:968	Although the overall cellular protein O-glycosylation did not change, the O-glycosylation status of several key proteins was altered.
17614351	4	73	dep	glutaminase	558:568	arg1	cells					581:585	expressing cells	570:585	The antisense mRNA glutaminase expressing cells	539:585	The antisense mRNA glutaminase expressing cells, named ORF19, presented a 50% lower proliferation rate than parental cells, showing a more differentiated phenotype.
17614351	7	74	theme	transferase	1011:1021	arg1	O-glycosylation					983:997	O-glycosylation	983:997	O-glycosylation of O-GlcNAc transferase (OGT), the enzyme that links N-acetylglucosamine to proteins,	983:1083	O-glycosylation of O-GlcNAc transferase (OGT), the enzyme that links N-acetylglucosamine to proteins, was fivefold lower in ORF19 than in wild type cells.
17614351	5	75	theme	80	723:724	arg1	%					725:725	%	725:725	%	725:725	ORF19 cells had an 80% reduction in glutamine:fructose-6-P amidotransferase activity, which is the rate-limiting step of the hexosamine pathway.
17614351	8	76	from	decrease	1234:1241	arg1	ratio					1250:1254	the ratio	1246:1254	the ratio of O-glycosylated to total protein for both Sp1 and the Rpt2 proteasome component	1246:1336	Inhibition of glutaminase also provoked a 10-fold increase in Sp1 expression, and a significant decrease in the ratio of O-glycosylated to total protein for both Sp1 and the Rpt2 proteasome component.
17614351	8	76	from	decrease	1234:1241	arg1	expression					1204:1213	Sp1 expression	1200:1213	Sp1 expression	1200:1213	Inhibition of glutaminase also provoked a 10-fold increase in Sp1 expression, and a significant decrease in the ratio of O-glycosylated to total protein for both Sp1 and the Rpt2 proteasome component.
17614351	3	77	from	pattern	503:509	arg1	pathway					487:493	the hexosamine pathway	472:493	the hexosamine pathway	472:493	We have carried out the antisense L-type glutaminase inhibition in human MCF7 breast cancer cells, in order to study its effect on the hexosamine pathway and the pattern of protein O-glycosylation.
17614351	0	78	theme	hexosamine	84:93	arg1	pathway					95:101	the hexosamine pathway	80:101	the hexosamine pathway in breast cancer cells	80:124	Antisense glutaminase inhibition modifies the O-GlcNAc pattern and flux through the hexosamine pathway in breast cancer cells.
17614351	1	79	theme	key	150:152	arg1	nutrient					154:161	a key nutrient	148:161	a key nutrient for tumors and rapidly dividing cells	148:199	Glutamine behaves as a key nutrient for tumors and rapidly dividing cells.
17614351	5	80	theme	ORF19	704:708	arg1	cells					710:714	ORF19 cells	704:714	ORF19 cells	704:714	ORF19 cells had an 80% reduction in glutamine:fructose-6-P amidotransferase activity, which is the rate-limiting step of the hexosamine pathway.
17614351	11	81	theme	states	1741:1746	arg1	mechanism					1698:1706	a sensor mechanism	1689:1706	a sensor mechanism of the nutritional and energetic states of the cell	1689:1758	Taken together, our results support the hexosamine pathway and the O-glycosylation of proteins being a sensor mechanism of the nutritional and energetic states of the cell.
17614351	0	82	theme	cancer	113:118	arg1	cells					120:124	breast cancer cells	106:124	breast cancer cells	106:124	Antisense glutaminase inhibition modifies the O-GlcNAc pattern and flux through the hexosamine pathway in breast cancer cells.
17614351	10	83	theme	O-glycosylated	1433:1446	arg1	proteins					1448:1455	O-glycosylated proteins	1433:1455	O-glycosylated proteins	1433:1455	Proteome analysis of O-glycosylated proteins permitted the detection of two new OGT target proteins: the chaperonin TCP-1 theta and the oncogene Ets-related protein isoform 7.
17614351	0	84	theme	glutaminase	10:20	arg1	inhibition					22:31	Antisense glutaminase inhibition	0:31	Antisense glutaminase inhibition	0:31	Antisense glutaminase inhibition modifies the O-GlcNAc pattern and flux through the hexosamine pathway in breast cancer cells.
17614351	3	85	theme	glutaminase	382:392	arg1	inhibition					394:403	the antisense L-type glutaminase inhibition	361:403	the antisense L-type glutaminase inhibition in human MCF7 breast cancer cells	361:437	We have carried out the antisense L-type glutaminase inhibition in human MCF7 breast cancer cells, in order to study its effect on the hexosamine pathway and the pattern of protein O-glycosylation.
17614351	8	86	theme	Rpt2	1312:1315	arg1	component					1328:1336	the Rpt2 proteasome component	1308:1336	the Rpt2 proteasome component	1308:1336	Inhibition of glutaminase also provoked a 10-fold increase in Sp1 expression, and a significant decrease in the ratio of O-glycosylated to total protein for both Sp1 and the Rpt2 proteasome component.
17614351	3	87	theme	cancer	426:431	arg1	cells					433:437	human MCF7 breast cancer cells	408:437	human MCF7 breast cancer cells	408:437	We have carried out the antisense L-type glutaminase inhibition in human MCF7 breast cancer cells, in order to study its effect on the hexosamine pathway and the pattern of protein O-glycosylation.
17614351	7	88	theme	type	1126:1129	arg1	cells					1131:1135	wild type cells	1121:1135	wild type cells	1121:1135	O-glycosylation of O-GlcNAc transferase (OGT), the enzyme that links N-acetylglucosamine to proteins, was fivefold lower in ORF19 than in wild type cells.
17614351	2	89	from	enzyme	246:251	arg1	cells					262:266	these cells	256:266	these cells	256:266	Glutaminase is the main glutamine-utilizing enzyme in these cells, and its activity correlates with glutamine consumption and growth rate.
17614351	3	90	theme	antisense	365:373	arg1	inhibition					394:403	the antisense L-type glutaminase inhibition	361:403	the antisense L-type glutaminase inhibition in human MCF7 breast cancer cells	361:437	We have carried out the antisense L-type glutaminase inhibition in human MCF7 breast cancer cells, in order to study its effect on the hexosamine pathway and the pattern of protein O-glycosylation.
17614351	4	91	theme	mRNA	553:556	arg1	glutaminase					558:568	The antisense mRNA glutaminase	539:568	The antisense mRNA glutaminase expressing cells	539:585	The antisense mRNA glutaminase expressing cells, named ORF19, presented a 50% lower proliferation rate than parental cells, showing a more differentiated phenotype.
17614351	5	92	theme	glutamine	740:748	arg1	amidotransferase					763:778	glutamine:fructose-6-P amidotransferase	740:778	glutamine:fructose-6-P amidotransferase activity	740:787	ORF19 cells had an 80% reduction in glutamine:fructose-6-P amidotransferase activity, which is the rate-limiting step of the hexosamine pathway.
17614351	3	93	theme	MCF7	414:417	arg1	cells					433:437	human MCF7 breast cancer cells	408:437	human MCF7 breast cancer cells	408:437	We have carried out the antisense L-type glutaminase inhibition in human MCF7 breast cancer cells, in order to study its effect on the hexosamine pathway and the pattern of protein O-glycosylation.
17614351	5	94	theme	fructose-6-P	750:761	arg1	amidotransferase					763:778	glutamine:fructose-6-P amidotransferase	740:778	glutamine:fructose-6-P amidotransferase activity	740:787	ORF19 cells had an 80% reduction in glutamine:fructose-6-P amidotransferase activity, which is the rate-limiting step of the hexosamine pathway.
17614351	10	95	theme	OGT	1492:1494	arg1	theta					1534:1538	the chaperonin TCP-1 theta	1513:1538	the chaperonin TCP-1 theta	1513:1538	Proteome analysis of O-glycosylated proteins permitted the detection of two new OGT target proteins: the chaperonin TCP-1 theta and the oncogene Ets-related protein isoform 7.
17614351	10	95	theme	OGT	1492:1494	arg1	proteins					1503:1510	two new OGT target proteins	1484:1510	two new OGT target proteins: the chaperonin TCP-1 theta and the oncogene Ets-related protein isoform 7	1484:1585	Proteome analysis of O-glycosylated proteins permitted the detection of two new OGT target proteins: the chaperonin TCP-1 theta and the oncogene Ets-related protein isoform 7.
17614351	10	95	theme	OGT	1492:1494	arg1	isoform					1577:1583	the oncogene Ets-related protein isoform 7	1544:1585	the oncogene Ets-related protein isoform 7	1544:1585	Proteome analysis of O-glycosylated proteins permitted the detection of two new OGT target proteins: the chaperonin TCP-1 theta and the oncogene Ets-related protein isoform 7.
17614351	11	96	theme	sensor	1691:1696	arg1	mechanism					1698:1706	a sensor mechanism	1689:1706	a sensor mechanism of the nutritional and energetic states of the cell	1689:1758	Taken together, our results support the hexosamine pathway and the O-glycosylation of proteins being a sensor mechanism of the nutritional and energetic states of the cell.
9452489	2	0	theme	in	587:588	arg1	te					565:566	O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbama te	498:566	O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbama te (PUGNAc)	498:575	In this study we have demonstrated that O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbama te (PUGNAc), a potent in vitro inhibitor of the enzyme responsible for the removal of O-GlcNAc from proteins (peptide O-GlcNAc-beta-N-acetylglucosaminidase), can be used to increase O-GlcNAc levels on nuclear and cytoplasmic proteins in vivo.
9452489	2	0	theme	in	587:588	arg1	inhibitor					596:604	a potent in vitro inhibitor	578:604	a potent in vitro inhibitor of the enzyme responsible for the removal of O-GlcNAc from proteins (peptide O-GlcNAc-beta-N-acetylglucosaminidase)	578:720	In this study we have demonstrated that O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbama te (PUGNAc), a potent in vitro inhibitor of the enzyme responsible for the removal of O-GlcNAc from proteins (peptide O-GlcNAc-beta-N-acetylglucosaminidase), can be used to increase O-GlcNAc levels on nuclear and cytoplasmic proteins in vivo.
9452489	7	1	theme	transcription	1528:1540	arg1	Sp1					1549:1551	the transcription factor Sp1	1524:1551	the transcription factor Sp1	1524:1551	Interestingly, we demonstrated that an increase in O-GlcNAc levels on the transcription factor Sp1 resulted in a reciprocal decrease in its level of phosphorylation, supporting the hypothesis that O-GlcNAc competes with phosphate on some proteins.
9452489	2	2	dep	in	587:588	arg1	vitro					590:594	vitro	590:594	vitro	590:594	In this study we have demonstrated that O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbama te (PUGNAc), a potent in vitro inhibitor of the enzyme responsible for the removal of O-GlcNAc from proteins (peptide O-GlcNAc-beta-N-acetylglucosaminidase), can be used to increase O-GlcNAc levels on nuclear and cytoplasmic proteins in vivo.
9452489	2	3	theme	potent	580:585	arg1	te					565:566	O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbama te	498:566	O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbama te (PUGNAc)	498:575	In this study we have demonstrated that O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbama te (PUGNAc), a potent in vitro inhibitor of the enzyme responsible for the removal of O-GlcNAc from proteins (peptide O-GlcNAc-beta-N-acetylglucosaminidase), can be used to increase O-GlcNAc levels on nuclear and cytoplasmic proteins in vivo.
9452489	2	3	theme	potent	580:585	arg1	inhibitor					596:604	a potent in vitro inhibitor	578:604	a potent in vitro inhibitor of the enzyme responsible for the removal of O-GlcNAc from proteins (peptide O-GlcNAc-beta-N-acetylglucosaminidase)	578:720	In this study we have demonstrated that O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbama te (PUGNAc), a potent in vitro inhibitor of the enzyme responsible for the removal of O-GlcNAc from proteins (peptide O-GlcNAc-beta-N-acetylglucosaminidase), can be used to increase O-GlcNAc levels on nuclear and cytoplasmic proteins in vivo.
9452489	3	4	from	levels	875:880	arg1	HT29					915:918	HT29	915:918	HT29	915:918	Overall, PUGNAc caused approximately a 2-fold increase in O-GlcNAc levels in the human colon cancer cells, HT29, although the effects on individual proteins varied.
9452489	3	4	from	levels	875:880	arg1	cells					908:912	the human colon cancer cells	885:912	the human colon cancer cells	885:912	Overall, PUGNAc caused approximately a 2-fold increase in O-GlcNAc levels in the human colon cancer cells, HT29, although the effects on individual proteins varied.
9452489	8	5	theme	O-GlcNAc	1851:1858	arg1	extent					1841:1846	the extent	1837:1846	the extent of O-GlcNAc on cellular proteins	1837:1879	These studies demonstrate that PUGNAc is an effective inhibitor of O-GlcNAc turnover within cells and can be used to selectively alter the extent of O-GlcNAc on cellular proteins.
9452489	1	6	theme	O-Linked	230:237	arg1	O-GlcNAc					260:267	O-GlcNAc	260:267	O-GlcNAc	260:267	O-Linked N-acetylglucosamine (O-GlcNAc) is a ubiquitous and abundant post-translational modification found on nuclear and cytoplasmic proteins and is thought to be a dynamically regulated modification much like phosphorylation.
9452489	1	6	theme	O-Linked	230:237	arg1	modification					318:329	a ubiquitous and abundant post-translational modification	273:329	a ubiquitous and abundant post-translational modification found on nuclear and cytoplasmic proteins	273:371	O-Linked N-acetylglucosamine (O-GlcNAc) is a ubiquitous and abundant post-translational modification found on nuclear and cytoplasmic proteins and is thought to be a dynamically regulated modification much like phosphorylation.
9452489	1	6	theme	O-Linked	230:237	arg1	N-acetylglucosamine					239:257	O-Linked N-acetylglucosamine	230:257	O-Linked N-acetylglucosamine (O-GlcNAc)	230:268	O-Linked N-acetylglucosamine (O-GlcNAc) is a ubiquitous and abundant post-translational modification found on nuclear and cytoplasmic proteins and is thought to be a dynamically regulated modification much like phosphorylation.
9452489	1	6	theme	O-Linked	230:237	arg1	modification					418:429	a dynamically regulated modification	394:429	a dynamically regulated modification	394:429	O-Linked N-acetylglucosamine (O-GlcNAc) is a ubiquitous and abundant post-translational modification found on nuclear and cytoplasmic proteins and is thought to be a dynamically regulated modification much like phosphorylation.
9452489	1	7	theme	nuclear	340:346	arg1	proteins					364:371	nuclear and cytoplasmic proteins	340:371	nuclear and cytoplasmic proteins	340:371	O-Linked N-acetylglucosamine (O-GlcNAc) is a ubiquitous and abundant post-translational modification found on nuclear and cytoplasmic proteins and is thought to be a dynamically regulated modification much like phosphorylation.
9452489	2	8	theme	responsible	620:630	arg1	enzyme					613:618	the enzyme	609:618	the enzyme responsible for the removal of O-GlcNAc from proteins (peptide O-GlcNAc-beta-N-acetylglucosaminidase)	609:720	In this study we have demonstrated that O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbama te (PUGNAc), a potent in vitro inhibitor of the enzyme responsible for the removal of O-GlcNAc from proteins (peptide O-GlcNAc-beta-N-acetylglucosaminidase), can be used to increase O-GlcNAc levels on nuclear and cytoplasmic proteins in vivo.
9452489	0	9	from	Modulation	0:9	arg1	proteins					77:84	nuclear and cytoplasmic proteins	53:84	nuclear and cytoplasmic proteins	53:84	Modulation of O-linked N-acetylglucosamine levels on nuclear and cytoplasmic proteins in vivo using the peptide O-GlcNAc-beta-N-acetylglucosaminidase inhibitor O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate.
9452489	0	10	link	O-linked	14:21	arg1	levels					43:48	O-linked N-acetylglucosamine levels	14:48	O-linked N-acetylglucosamine levels	14:48	Modulation of O-linked N-acetylglucosamine levels on nuclear and cytoplasmic proteins in vivo using the peptide O-GlcNAc-beta-N-acetylglucosaminidase inhibitor O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate.
9452489	8	11	theme	cellular	1863:1870	arg1	proteins					1872:1879	cellular proteins	1863:1879	cellular proteins	1863:1879	These studies demonstrate that PUGNAc is an effective inhibitor of O-GlcNAc turnover within cells and can be used to selectively alter the extent of O-GlcNAc on cellular proteins.
9452489	2	12	theme	enzyme	613:618	arg1	te					565:566	O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbama te	498:566	O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbama te (PUGNAc)	498:575	In this study we have demonstrated that O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbama te (PUGNAc), a potent in vitro inhibitor of the enzyme responsible for the removal of O-GlcNAc from proteins (peptide O-GlcNAc-beta-N-acetylglucosaminidase), can be used to increase O-GlcNAc levels on nuclear and cytoplasmic proteins in vivo.
9452489	2	12	theme	enzyme	613:618	arg1	inhibitor					596:604	a potent in vitro inhibitor	578:604	a potent in vitro inhibitor of the enzyme responsible for the removal of O-GlcNAc from proteins (peptide O-GlcNAc-beta-N-acetylglucosaminidase)	578:720	In this study we have demonstrated that O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbama te (PUGNAc), a potent in vitro inhibitor of the enzyme responsible for the removal of O-GlcNAc from proteins (peptide O-GlcNAc-beta-N-acetylglucosaminidase), can be used to increase O-GlcNAc levels on nuclear and cytoplasmic proteins in vivo.
9452489	5	13	theme	HeLa	1306:1309	arg1	cells					1311:1315	HeLa cells	1306:1315	HeLa cells	1306:1315	O-GlcNAc levels in other cell lines tested (NIH 3T3, CV-1, and HeLa) were also affected by PUGNAc, although the effects on HeLa cells were minimal.
9452489	2	14	theme	peptide	675:681	arg1	proteins					665:672	proteins	665:672	proteins (peptide O-GlcNAc-beta-N-acetylglucosaminidase)	665:720	In this study we have demonstrated that O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbama te (PUGNAc), a potent in vitro inhibitor of the enzyme responsible for the removal of O-GlcNAc from proteins (peptide O-GlcNAc-beta-N-acetylglucosaminidase), can be used to increase O-GlcNAc levels on nuclear and cytoplasmic proteins in vivo.
9452489	2	14	theme	peptide	675:681	arg1	O-GlcNAc-beta-N-acetylglucosaminidase					683:719	peptide O-GlcNAc-beta-N-acetylglucosaminidase	675:719	peptide O-GlcNAc-beta-N-acetylglucosaminidase	675:719	In this study we have demonstrated that O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbama te (PUGNAc), a potent in vitro inhibitor of the enzyme responsible for the removal of O-GlcNAc from proteins (peptide O-GlcNAc-beta-N-acetylglucosaminidase), can be used to increase O-GlcNAc levels on nuclear and cytoplasmic proteins in vivo.
9452489	2	15	theme	O-GlcNAc	747:754	arg1	levels					756:761	O-GlcNAc levels	747:761	O-GlcNAc levels on nuclear and cytoplasmic proteins	747:797	In this study we have demonstrated that O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbama te (PUGNAc), a potent in vitro inhibitor of the enzyme responsible for the removal of O-GlcNAc from proteins (peptide O-GlcNAc-beta-N-acetylglucosaminidase), can be used to increase O-GlcNAc levels on nuclear and cytoplasmic proteins in vivo.
9452489	1	16	theme	cytoplasmic	352:362	arg1	proteins					364:371	nuclear and cytoplasmic proteins	340:371	nuclear and cytoplasmic proteins	340:371	O-Linked N-acetylglucosamine (O-GlcNAc) is a ubiquitous and abundant post-translational modification found on nuclear and cytoplasmic proteins and is thought to be a dynamically regulated modification much like phosphorylation.
9452489	0	17	theme	O-GlcNAc-beta-N-acetylglucosaminidase	112:148	arg1	inhibitor					150:158	the peptide O-GlcNAc-beta-N-acetylglucosaminidase inhibitor	100:158	the peptide O-GlcNAc-beta-N-acetylglucosaminidase inhibitor O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate	100:227	Modulation of O-linked N-acetylglucosamine levels on nuclear and cytoplasmic proteins in vivo using the peptide O-GlcNAc-beta-N-acetylglucosaminidase inhibitor O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate.
9452489	7	18	theme	O-GlcNAc	1505:1512	arg1	levels					1514:1519	O-GlcNAc levels	1505:1519	O-GlcNAc levels on the transcription factor Sp1	1505:1551	Interestingly, we demonstrated that an increase in O-GlcNAc levels on the transcription factor Sp1 resulted in a reciprocal decrease in its level of phosphorylation, supporting the hypothesis that O-GlcNAc competes with phosphate on some proteins.
9452489	8	19	theme	effective	1746:1754	arg1	PUGNAc					1733:1738	PUGNAc	1733:1738	PUGNAc	1733:1738	These studies demonstrate that PUGNAc is an effective inhibitor of O-GlcNAc turnover within cells and can be used to selectively alter the extent of O-GlcNAc on cellular proteins.
9452489	8	19	theme	effective	1746:1754	arg1	inhibitor					1756:1764	an effective inhibitor	1743:1764	an effective inhibitor of O-GlcNAc turnover	1743:1785	These studies demonstrate that PUGNAc is an effective inhibitor of O-GlcNAc turnover within cells and can be used to selectively alter the extent of O-GlcNAc on cellular proteins.
9452489	5	20	theme	other	1202:1206	arg1	HeLa					1246:1249	HeLa	1246:1249	HeLa	1246:1249	O-GlcNAc levels in other cell lines tested (NIH 3T3, CV-1, and HeLa) were also affected by PUGNAc, although the effects on HeLa cells were minimal.
9452489	5	20	theme	other	1202:1206	arg1	3T3					1231:1233	NIH 3T3	1227:1233	NIH 3T3	1227:1233	O-GlcNAc levels in other cell lines tested (NIH 3T3, CV-1, and HeLa) were also affected by PUGNAc, although the effects on HeLa cells were minimal.
9452489	5	20	theme	other	1202:1206	arg1	lines					1213:1217	other cell lines	1202:1217	other cell lines tested (NIH 3T3, CV-1, and HeLa)	1202:1250	O-GlcNAc levels in other cell lines tested (NIH 3T3, CV-1, and HeLa) were also affected by PUGNAc, although the effects on HeLa cells were minimal.
9452489	5	20	theme	other	1202:1206	arg1	CV-1					1236:1239	CV-1	1236:1239	CV-1	1236:1239	O-GlcNAc levels in other cell lines tested (NIH 3T3, CV-1, and HeLa) were also affected by PUGNAc, although the effects on HeLa cells were minimal.
9452489	0	21	theme	peptide	104:110	arg1	inhibitor					150:158	the peptide O-GlcNAc-beta-N-acetylglucosaminidase inhibitor	100:158	the peptide O-GlcNAc-beta-N-acetylglucosaminidase inhibitor O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate	100:227	Modulation of O-linked N-acetylglucosamine levels on nuclear and cytoplasmic proteins in vivo using the peptide O-GlcNAc-beta-N-acetylglucosaminidase inhibitor O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate.
9452489	7	22	from	levels	1514:1519	arg1	Sp1					1549:1551	the transcription factor Sp1	1524:1551	the transcription factor Sp1	1524:1551	Interestingly, we demonstrated that an increase in O-GlcNAc levels on the transcription factor Sp1 resulted in a reciprocal decrease in its level of phosphorylation, supporting the hypothesis that O-GlcNAc competes with phosphate on some proteins.
9452489	7	23	from	increase	1493:1500	arg1	Sp1					1549:1551	the transcription factor Sp1	1524:1551	the transcription factor Sp1	1524:1551	Interestingly, we demonstrated that an increase in O-GlcNAc levels on the transcription factor Sp1 resulted in a reciprocal decrease in its level of phosphorylation, supporting the hypothesis that O-GlcNAc competes with phosphate on some proteins.
9452489	7	23	from	increase	1493:1500	arg1	levels					1514:1519	O-GlcNAc levels	1505:1519	O-GlcNAc levels on the transcription factor Sp1	1505:1551	Interestingly, we demonstrated that an increase in O-GlcNAc levels on the transcription factor Sp1 resulted in a reciprocal decrease in its level of phosphorylation, supporting the hypothesis that O-GlcNAc competes with phosphate on some proteins.
9452489	8	24	theme	O-GlcNAc	1769:1776	arg1	turnover					1778:1785	O-GlcNAc turnover	1769:1785	O-GlcNAc turnover	1769:1785	These studies demonstrate that PUGNAc is an effective inhibitor of O-GlcNAc turnover within cells and can be used to selectively alter the extent of O-GlcNAc on cellular proteins.
9452489	6	25	theme	growth	1407:1412	arg1	rate					1414:1417	the growth rate	1403:1417	the growth rate of any of the cell lines examined	1403:1451	At the concentrations tested, PUGNAc was non-toxic and had no affect on the growth rate of any of the cell lines examined.
9452489	6	26	theme	any	1422:1424	arg1	rate					1414:1417	the growth rate	1403:1417	the growth rate of any of the cell lines examined	1403:1451	At the concentrations tested, PUGNAc was non-toxic and had no affect on the growth rate of any of the cell lines examined.
9452489	3	27	from	increase	854:861	arg1	levels					875:880	O-GlcNAc levels	866:880	O-GlcNAc levels in the human colon cancer cells, HT29	866:918	Overall, PUGNAc caused approximately a 2-fold increase in O-GlcNAc levels in the human colon cancer cells, HT29, although the effects on individual proteins varied.
9452489	2	28	theme	cytoplasmic	778:788	arg1	proteins					790:797	nuclear and cytoplasmic proteins	766:797	nuclear and cytoplasmic proteins	766:797	In this study we have demonstrated that O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbama te (PUGNAc), a potent in vitro inhibitor of the enzyme responsible for the removal of O-GlcNAc from proteins (peptide O-GlcNAc-beta-N-acetylglucosaminidase), can be used to increase O-GlcNAc levels on nuclear and cytoplasmic proteins in vivo.
9452489	7	29	from	decrease	1578:1585	arg1	level					1594:1598	its level	1590:1598	its level of phosphorylation	1590:1617	Interestingly, we demonstrated that an increase in O-GlcNAc levels on the transcription factor Sp1 resulted in a reciprocal decrease in its level of phosphorylation, supporting the hypothesis that O-GlcNAc competes with phosphate on some proteins.
9452489	4	30	theme	UDP-GlcNAc	1133:1142	arg1	levels					1144:1149	UDP-GlcNAc levels	1133:1149	UDP-GlcNAc levels	1133:1149	The increase appeared to be the result of the direct inhibition of the peptide O-GlcNAc-beta-N-acetylglucosaminidase since neither the O-GlcNAc transferase nor UDP-GlcNAc levels were affected by the treatment.
9452489	6	31	from	concentrations	1338:1351	arg1	non-toxic					1372:1380	non-toxic	1372:1380	non-toxic	1372:1380	At the concentrations tested, PUGNAc was non-toxic and had no affect on the growth rate of any of the cell lines examined.
9452489	3	32	from	effects	934:940	arg1	proteins					956:963	individual proteins	945:963	individual proteins	945:963	Overall, PUGNAc caused approximately a 2-fold increase in O-GlcNAc levels in the human colon cancer cells, HT29, although the effects on individual proteins varied.
9452489	0	33	theme	N-acetylglucosamine	23:41	arg1	levels					43:48	O-linked N-acetylglucosamine levels	14:48	O-linked N-acetylglucosamine levels	14:48	Modulation of O-linked N-acetylglucosamine levels on nuclear and cytoplasmic proteins in vivo using the peptide O-GlcNAc-beta-N-acetylglucosaminidase inhibitor O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate.
9452489	2	34	theme	nuclear	766:772	arg1	proteins					790:797	nuclear and cytoplasmic proteins	766:797	nuclear and cytoplasmic proteins	766:797	In this study we have demonstrated that O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbama te (PUGNAc), a potent in vitro inhibitor of the enzyme responsible for the removal of O-GlcNAc from proteins (peptide O-GlcNAc-beta-N-acetylglucosaminidase), can be used to increase O-GlcNAc levels on nuclear and cytoplasmic proteins in vivo.
9452489	8	35	theme	turnover	1778:1785	arg1	PUGNAc					1733:1738	PUGNAc	1733:1738	PUGNAc	1733:1738	These studies demonstrate that PUGNAc is an effective inhibitor of O-GlcNAc turnover within cells and can be used to selectively alter the extent of O-GlcNAc on cellular proteins.
9452489	8	35	theme	turnover	1778:1785	arg1	inhibitor					1756:1764	an effective inhibitor	1743:1764	an effective inhibitor of O-GlcNAc turnover	1743:1785	These studies demonstrate that PUGNAc is an effective inhibitor of O-GlcNAc turnover within cells and can be used to selectively alter the extent of O-GlcNAc on cellular proteins.
9452489	2	36	theme	2-acetamido-2-deoxy-D-glucopyranosylidene	501:541	arg1	te					565:566	O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbama te	498:566	O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbama te (PUGNAc)	498:575	In this study we have demonstrated that O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbama te (PUGNAc), a potent in vitro inhibitor of the enzyme responsible for the removal of O-GlcNAc from proteins (peptide O-GlcNAc-beta-N-acetylglucosaminidase), can be used to increase O-GlcNAc levels on nuclear and cytoplasmic proteins in vivo.
9452489	2	36	theme	2-acetamido-2-deoxy-D-glucopyranosylidene	501:541	arg1	inhibitor					596:604	a potent in vitro inhibitor	578:604	a potent in vitro inhibitor of the enzyme responsible for the removal of O-GlcNAc from proteins (peptide O-GlcNAc-beta-N-acetylglucosaminidase)	578:720	In this study we have demonstrated that O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbama te (PUGNAc), a potent in vitro inhibitor of the enzyme responsible for the removal of O-GlcNAc from proteins (peptide O-GlcNAc-beta-N-acetylglucosaminidase), can be used to increase O-GlcNAc levels on nuclear and cytoplasmic proteins in vivo.
9452489	2	36	theme	2-acetamido-2-deoxy-D-glucopyranosylidene	501:541	arg1	PUGNAc					569:574	PUGNAc	569:574	PUGNAc	569:574	In this study we have demonstrated that O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbama te (PUGNAc), a potent in vitro inhibitor of the enzyme responsible for the removal of O-GlcNAc from proteins (peptide O-GlcNAc-beta-N-acetylglucosaminidase), can be used to increase O-GlcNAc levels on nuclear and cytoplasmic proteins in vivo.
9452489	0	37	theme	O-linked	14:21	arg1	levels					43:48	O-linked N-acetylglucosamine levels	14:48	O-linked N-acetylglucosamine levels	14:48	Modulation of O-linked N-acetylglucosamine levels on nuclear and cytoplasmic proteins in vivo using the peptide O-GlcNAc-beta-N-acetylglucosaminidase inhibitor O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate.
9452489	2	38	used	used	730:733	arg2	inhibitor					596:604	a potent in vitro inhibitor	578:604	a potent in vitro inhibitor of the enzyme responsible for the removal of O-GlcNAc from proteins (peptide O-GlcNAc-beta-N-acetylglucosaminidase)	578:720	In this study we have demonstrated that O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbama te (PUGNAc), a potent in vitro inhibitor of the enzyme responsible for the removal of O-GlcNAc from proteins (peptide O-GlcNAc-beta-N-acetylglucosaminidase), can be used to increase O-GlcNAc levels on nuclear and cytoplasmic proteins in vivo.
9452489	2	38	used	used	730:733	arg2	PUGNAc					569:574	PUGNAc	569:574	PUGNAc	569:574	In this study we have demonstrated that O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbama te (PUGNAc), a potent in vitro inhibitor of the enzyme responsible for the removal of O-GlcNAc from proteins (peptide O-GlcNAc-beta-N-acetylglucosaminidase), can be used to increase O-GlcNAc levels on nuclear and cytoplasmic proteins in vivo.
9452489	2	38	used	used	730:733	arg2	te					565:566	O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbama te	498:566	O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbama te (PUGNAc)	498:575	In this study we have demonstrated that O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbama te (PUGNAc), a potent in vitro inhibitor of the enzyme responsible for the removal of O-GlcNAc from proteins (peptide O-GlcNAc-beta-N-acetylglucosaminidase), can be used to increase O-GlcNAc levels on nuclear and cytoplasmic proteins in vivo.
9452489	5	39	theme	O-GlcNAc	1183:1190	arg1	levels					1192:1197	O-GlcNAc levels	1183:1197	O-GlcNAc levels in other cell lines tested (NIH 3T3, CV-1, and HeLa)	1183:1250	O-GlcNAc levels in other cell lines tested (NIH 3T3, CV-1, and HeLa) were also affected by PUGNAc, although the effects on HeLa cells were minimal.
9452489	8	40	from	extent	1841:1846	arg1	proteins					1872:1879	cellular proteins	1863:1879	cellular proteins	1863:1879	These studies demonstrate that PUGNAc is an effective inhibitor of O-GlcNAc turnover within cells and can be used to selectively alter the extent of O-GlcNAc on cellular proteins.
9452489	4	41	theme	O-GlcNAc	1108:1115	arg1	transferase					1117:1127	the O-GlcNAc transferase	1104:1127	the O-GlcNAc transferase	1104:1127	The increase appeared to be the result of the direct inhibition of the peptide O-GlcNAc-beta-N-acetylglucosaminidase since neither the O-GlcNAc transferase nor UDP-GlcNAc levels were affected by the treatment.
9452489	3	42	theme	2-fold	847:852	arg1	increase					854:861	approximately a 2-fold increase	831:861	approximately a 2-fold increase in O-GlcNAc levels in the human colon cancer cells, HT29	831:918	Overall, PUGNAc caused approximately a 2-fold increase in O-GlcNAc levels in the human colon cancer cells, HT29, although the effects on individual proteins varied.
9452489	4	43	theme	direct	1019:1024	arg1	inhibition					1026:1035	the direct inhibition	1015:1035	the direct inhibition of the peptide O-GlcNAc-beta-N-acetylglucosaminidase	1015:1088	The increase appeared to be the result of the direct inhibition of the peptide O-GlcNAc-beta-N-acetylglucosaminidase since neither the O-GlcNAc transferase nor UDP-GlcNAc levels were affected by the treatment.
9452489	1	44	theme	ubiquitous	275:284	arg1	modification					318:329	a ubiquitous and abundant post-translational modification	273:329	a ubiquitous and abundant post-translational modification found on nuclear and cytoplasmic proteins	273:371	O-Linked N-acetylglucosamine (O-GlcNAc) is a ubiquitous and abundant post-translational modification found on nuclear and cytoplasmic proteins and is thought to be a dynamically regulated modification much like phosphorylation.
9452489	1	44	theme	ubiquitous	275:284	arg1	N-acetylglucosamine					239:257	O-Linked N-acetylglucosamine	230:257	O-Linked N-acetylglucosamine (O-GlcNAc)	230:268	O-Linked N-acetylglucosamine (O-GlcNAc) is a ubiquitous and abundant post-translational modification found on nuclear and cytoplasmic proteins and is thought to be a dynamically regulated modification much like phosphorylation.
9452489	2	45	theme	O-	498:499	arg1	te					565:566	O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbama te	498:566	O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbama te (PUGNAc)	498:575	In this study we have demonstrated that O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbama te (PUGNAc), a potent in vitro inhibitor of the enzyme responsible for the removal of O-GlcNAc from proteins (peptide O-GlcNAc-beta-N-acetylglucosaminidase), can be used to increase O-GlcNAc levels on nuclear and cytoplasmic proteins in vivo.
9452489	2	45	theme	O-	498:499	arg1	inhibitor					596:604	a potent in vitro inhibitor	578:604	a potent in vitro inhibitor of the enzyme responsible for the removal of O-GlcNAc from proteins (peptide O-GlcNAc-beta-N-acetylglucosaminidase)	578:720	In this study we have demonstrated that O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbama te (PUGNAc), a potent in vitro inhibitor of the enzyme responsible for the removal of O-GlcNAc from proteins (peptide O-GlcNAc-beta-N-acetylglucosaminidase), can be used to increase O-GlcNAc levels on nuclear and cytoplasmic proteins in vivo.
9452489	2	45	theme	O-	498:499	arg1	PUGNAc					569:574	PUGNAc	569:574	PUGNAc	569:574	In this study we have demonstrated that O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbama te (PUGNAc), a potent in vitro inhibitor of the enzyme responsible for the removal of O-GlcNAc from proteins (peptide O-GlcNAc-beta-N-acetylglucosaminidase), can be used to increase O-GlcNAc levels on nuclear and cytoplasmic proteins in vivo.
9452489	0	46	theme	levels	43:48	arg1	Modulation					0:9	Modulation	0:9	Modulation of O-linked N-acetylglucosamine levels on nuclear and cytoplasmic proteins in vivo	0:92	Modulation of O-linked N-acetylglucosamine levels on nuclear and cytoplasmic proteins in vivo using the peptide O-GlcNAc-beta-N-acetylglucosaminidase inhibitor O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate.
9452489	5	47	dep	tested	1219:1224	arg1	HeLa					1246:1249	HeLa	1246:1249	HeLa	1246:1249	O-GlcNAc levels in other cell lines tested (NIH 3T3, CV-1, and HeLa) were also affected by PUGNAc, although the effects on HeLa cells were minimal.
9452489	5	47	dep	tested	1219:1224	arg1	3T3					1231:1233	NIH 3T3	1227:1233	NIH 3T3	1227:1233	O-GlcNAc levels in other cell lines tested (NIH 3T3, CV-1, and HeLa) were also affected by PUGNAc, although the effects on HeLa cells were minimal.
9452489	5	47	dep	tested	1219:1224	arg1	lines					1213:1217	other cell lines	1202:1217	other cell lines tested (NIH 3T3, CV-1, and HeLa)	1202:1250	O-GlcNAc levels in other cell lines tested (NIH 3T3, CV-1, and HeLa) were also affected by PUGNAc, although the effects on HeLa cells were minimal.
9452489	5	47	dep	tested	1219:1224	arg1	CV-1					1236:1239	CV-1	1236:1239	CV-1	1236:1239	O-GlcNAc levels in other cell lines tested (NIH 3T3, CV-1, and HeLa) were also affected by PUGNAc, although the effects on HeLa cells were minimal.
9452489	7	48	theme	phosphorylation	1603:1617	arg1	level					1594:1598	its level	1590:1598	its level of phosphorylation	1590:1617	Interestingly, we demonstrated that an increase in O-GlcNAc levels on the transcription factor Sp1 resulted in a reciprocal decrease in its level of phosphorylation, supporting the hypothesis that O-GlcNAc competes with phosphate on some proteins.
9452489	2	49	theme	amino-N-phenylcarbama	543:563	arg1	te					565:566	O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbama te	498:566	O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbama te (PUGNAc)	498:575	In this study we have demonstrated that O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbama te (PUGNAc), a potent in vitro inhibitor of the enzyme responsible for the removal of O-GlcNAc from proteins (peptide O-GlcNAc-beta-N-acetylglucosaminidase), can be used to increase O-GlcNAc levels on nuclear and cytoplasmic proteins in vivo.
9452489	2	49	theme	amino-N-phenylcarbama	543:563	arg1	inhibitor					596:604	a potent in vitro inhibitor	578:604	a potent in vitro inhibitor of the enzyme responsible for the removal of O-GlcNAc from proteins (peptide O-GlcNAc-beta-N-acetylglucosaminidase)	578:720	In this study we have demonstrated that O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbama te (PUGNAc), a potent in vitro inhibitor of the enzyme responsible for the removal of O-GlcNAc from proteins (peptide O-GlcNAc-beta-N-acetylglucosaminidase), can be used to increase O-GlcNAc levels on nuclear and cytoplasmic proteins in vivo.
9452489	2	49	theme	amino-N-phenylcarbama	543:563	arg1	PUGNAc					569:574	PUGNAc	569:574	PUGNAc	569:574	In this study we have demonstrated that O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbama te (PUGNAc), a potent in vitro inhibitor of the enzyme responsible for the removal of O-GlcNAc from proteins (peptide O-GlcNAc-beta-N-acetylglucosaminidase), can be used to increase O-GlcNAc levels on nuclear and cytoplasmic proteins in vivo.
9452489	5	50	from	levels	1192:1197	arg1	HeLa					1246:1249	HeLa	1246:1249	HeLa	1246:1249	O-GlcNAc levels in other cell lines tested (NIH 3T3, CV-1, and HeLa) were also affected by PUGNAc, although the effects on HeLa cells were minimal.
9452489	5	50	from	levels	1192:1197	arg1	3T3					1231:1233	NIH 3T3	1227:1233	NIH 3T3	1227:1233	O-GlcNAc levels in other cell lines tested (NIH 3T3, CV-1, and HeLa) were also affected by PUGNAc, although the effects on HeLa cells were minimal.
9452489	5	50	from	levels	1192:1197	arg1	lines					1213:1217	other cell lines	1202:1217	other cell lines tested (NIH 3T3, CV-1, and HeLa)	1202:1250	O-GlcNAc levels in other cell lines tested (NIH 3T3, CV-1, and HeLa) were also affected by PUGNAc, although the effects on HeLa cells were minimal.
9452489	5	50	from	levels	1192:1197	arg1	CV-1					1236:1239	CV-1	1236:1239	CV-1	1236:1239	O-GlcNAc levels in other cell lines tested (NIH 3T3, CV-1, and HeLa) were also affected by PUGNAc, although the effects on HeLa cells were minimal.
9452489	4	51	theme	inhibition	1026:1035	arg1	result					1005:1010	the result	1001:1010	the result of the direct inhibition of the peptide O-GlcNAc-beta-N-acetylglucosaminidase	1001:1088	The increase appeared to be the result of the direct inhibition of the peptide O-GlcNAc-beta-N-acetylglucosaminidase since neither the O-GlcNAc transferase nor UDP-GlcNAc levels were affected by the treatment.
9452489	4	51	theme	inhibition	1026:1035	arg1	increase					977:984	The increase	973:984	The increase	973:984	The increase appeared to be the result of the direct inhibition of the peptide O-GlcNAc-beta-N-acetylglucosaminidase since neither the O-GlcNAc transferase nor UDP-GlcNAc levels were affected by the treatment.
9452489	0	52	theme	amino-N-phenylcarbamate	205:227	arg1	inhibitor					150:158	the peptide O-GlcNAc-beta-N-acetylglucosaminidase inhibitor	100:158	the peptide O-GlcNAc-beta-N-acetylglucosaminidase inhibitor O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate	100:227	Modulation of O-linked N-acetylglucosamine levels on nuclear and cytoplasmic proteins in vivo using the peptide O-GlcNAc-beta-N-acetylglucosaminidase inhibitor O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate.
9452489	4	53	theme	peptide	1044:1050	arg1	O-GlcNAc-beta-N-acetylglucosaminidase					1052:1088	the peptide O-GlcNAc-beta-N-acetylglucosaminidase	1040:1088	the peptide O-GlcNAc-beta-N-acetylglucosaminidase	1040:1088	The increase appeared to be the result of the direct inhibition of the peptide O-GlcNAc-beta-N-acetylglucosaminidase since neither the O-GlcNAc transferase nor UDP-GlcNAc levels were affected by the treatment.
9452489	1	54	located	found	331:335	arg2	N-acetylglucosamine					239:257	O-Linked N-acetylglucosamine	230:257	O-Linked N-acetylglucosamine (O-GlcNAc)	230:268	O-Linked N-acetylglucosamine (O-GlcNAc) is a ubiquitous and abundant post-translational modification found on nuclear and cytoplasmic proteins and is thought to be a dynamically regulated modification much like phosphorylation.
9452489	1	54	located	found	331:335	arg1	proteins					364:371	nuclear and cytoplasmic proteins	340:371	nuclear and cytoplasmic proteins	340:371	O-Linked N-acetylglucosamine (O-GlcNAc) is a ubiquitous and abundant post-translational modification found on nuclear and cytoplasmic proteins and is thought to be a dynamically regulated modification much like phosphorylation.
9452489	1	54	located	found	331:335	arg2	modification					318:329	a ubiquitous and abundant post-translational modification	273:329	a ubiquitous and abundant post-translational modification found on nuclear and cytoplasmic proteins	273:371	O-Linked N-acetylglucosamine (O-GlcNAc) is a ubiquitous and abundant post-translational modification found on nuclear and cytoplasmic proteins and is thought to be a dynamically regulated modification much like phosphorylation.
9452489	7	55	theme	reciprocal	1567:1576	arg1	decrease					1578:1585	a reciprocal decrease	1565:1585	a reciprocal decrease in its level of phosphorylation	1565:1617	Interestingly, we demonstrated that an increase in O-GlcNAc levels on the transcription factor Sp1 resulted in a reciprocal decrease in its level of phosphorylation, supporting the hypothesis that O-GlcNAc competes with phosphate on some proteins.
9452489	0	56	theme	nuclear	53:59	arg1	proteins					77:84	nuclear and cytoplasmic proteins	53:84	nuclear and cytoplasmic proteins	53:84	Modulation of O-linked N-acetylglucosamine levels on nuclear and cytoplasmic proteins in vivo using the peptide O-GlcNAc-beta-N-acetylglucosaminidase inhibitor O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate.
9452489	3	57	theme	O-GlcNAc	866:873	arg1	levels					875:880	O-GlcNAc levels	866:880	O-GlcNAc levels in the human colon cancer cells, HT29	866:918	Overall, PUGNAc caused approximately a 2-fold increase in O-GlcNAc levels in the human colon cancer cells, HT29, although the effects on individual proteins varied.
9452489	5	58	theme	NIH	1227:1229	arg1	3T3					1231:1233	NIH 3T3	1227:1233	NIH 3T3	1227:1233	O-GlcNAc levels in other cell lines tested (NIH 3T3, CV-1, and HeLa) were also affected by PUGNAc, although the effects on HeLa cells were minimal.
9452489	5	58	theme	NIH	1227:1229	arg1	lines					1213:1217	other cell lines	1202:1217	other cell lines tested (NIH 3T3, CV-1, and HeLa)	1202:1250	O-GlcNAc levels in other cell lines tested (NIH 3T3, CV-1, and HeLa) were also affected by PUGNAc, although the effects on HeLa cells were minimal.
9452489	5	59	theme	cell	1208:1211	arg1	HeLa					1246:1249	HeLa	1246:1249	HeLa	1246:1249	O-GlcNAc levels in other cell lines tested (NIH 3T3, CV-1, and HeLa) were also affected by PUGNAc, although the effects on HeLa cells were minimal.
9452489	5	59	theme	cell	1208:1211	arg1	3T3					1231:1233	NIH 3T3	1227:1233	NIH 3T3	1227:1233	O-GlcNAc levels in other cell lines tested (NIH 3T3, CV-1, and HeLa) were also affected by PUGNAc, although the effects on HeLa cells were minimal.
9452489	5	59	theme	cell	1208:1211	arg1	lines					1213:1217	other cell lines	1202:1217	other cell lines tested (NIH 3T3, CV-1, and HeLa)	1202:1250	O-GlcNAc levels in other cell lines tested (NIH 3T3, CV-1, and HeLa) were also affected by PUGNAc, although the effects on HeLa cells were minimal.
9452489	5	59	theme	cell	1208:1211	arg1	CV-1					1236:1239	CV-1	1236:1239	CV-1	1236:1239	O-GlcNAc levels in other cell lines tested (NIH 3T3, CV-1, and HeLa) were also affected by PUGNAc, although the effects on HeLa cells were minimal.
9452489	2	60	from	proteins	665:672	arg1	removal					640:646	the removal	636:646	the removal of O-GlcNAc from proteins (peptide O-GlcNAc-beta-N-acetylglucosaminidase)	636:720	In this study we have demonstrated that O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbama te (PUGNAc), a potent in vitro inhibitor of the enzyme responsible for the removal of O-GlcNAc from proteins (peptide O-GlcNAc-beta-N-acetylglucosaminidase), can be used to increase O-GlcNAc levels on nuclear and cytoplasmic proteins in vivo.
9452489	6	61	contain	had	1386:1388	arg1	PUGNAc					1361:1366	PUGNAc	1361:1366	PUGNAc	1361:1366	At the concentrations tested, PUGNAc was non-toxic and had no affect on the growth rate of any of the cell lines examined.
9452489	6	61	contain	had	1386:1388	arg2	affect					1393:1398	no affect	1390:1398	no affect	1390:1398	At the concentrations tested, PUGNAc was non-toxic and had no affect on the growth rate of any of the cell lines examined.
9452489	5	62	from	effects	1295:1301	arg1	cells					1311:1315	HeLa cells	1306:1315	HeLa cells	1306:1315	O-GlcNAc levels in other cell lines tested (NIH 3T3, CV-1, and HeLa) were also affected by PUGNAc, although the effects on HeLa cells were minimal.
9452489	3	63	theme	individual	945:954	arg1	proteins					956:963	individual proteins	945:963	individual proteins	945:963	Overall, PUGNAc caused approximately a 2-fold increase in O-GlcNAc levels in the human colon cancer cells, HT29, although the effects on individual proteins varied.
9452489	1	64	theme	abundant	290:297	arg1	modification					318:329	a ubiquitous and abundant post-translational modification	273:329	a ubiquitous and abundant post-translational modification found on nuclear and cytoplasmic proteins	273:371	O-Linked N-acetylglucosamine (O-GlcNAc) is a ubiquitous and abundant post-translational modification found on nuclear and cytoplasmic proteins and is thought to be a dynamically regulated modification much like phosphorylation.
9452489	1	64	theme	abundant	290:297	arg1	N-acetylglucosamine					239:257	O-Linked N-acetylglucosamine	230:257	O-Linked N-acetylglucosamine (O-GlcNAc)	230:268	O-Linked N-acetylglucosamine (O-GlcNAc) is a ubiquitous and abundant post-translational modification found on nuclear and cytoplasmic proteins and is thought to be a dynamically regulated modification much like phosphorylation.
9452489	2	65	theme	O-GlcNAc	651:658	arg1	removal					640:646	the removal	636:646	the removal of O-GlcNAc from proteins (peptide O-GlcNAc-beta-N-acetylglucosaminidase)	636:720	In this study we have demonstrated that O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbama te (PUGNAc), a potent in vitro inhibitor of the enzyme responsible for the removal of O-GlcNAc from proteins (peptide O-GlcNAc-beta-N-acetylglucosaminidase), can be used to increase O-GlcNAc levels on nuclear and cytoplasmic proteins in vivo.
9452489	7	66	theme	factor	1542:1547	arg1	Sp1					1549:1551	the transcription factor Sp1	1524:1551	the transcription factor Sp1	1524:1551	Interestingly, we demonstrated that an increase in O-GlcNAc levels on the transcription factor Sp1 resulted in a reciprocal decrease in its level of phosphorylation, supporting the hypothesis that O-GlcNAc competes with phosphate on some proteins.
9452489	6	67	theme	cell	1433:1436	arg1	lines					1438:1442	the cell lines	1429:1442	the cell lines examined	1429:1451	At the concentrations tested, PUGNAc was non-toxic and had no affect on the growth rate of any of the cell lines examined.
9452489	2	68	from	levels	756:761	arg1	proteins					790:797	nuclear and cytoplasmic proteins	766:797	nuclear and cytoplasmic proteins	766:797	In this study we have demonstrated that O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbama te (PUGNAc), a potent in vitro inhibitor of the enzyme responsible for the removal of O-GlcNAc from proteins (peptide O-GlcNAc-beta-N-acetylglucosaminidase), can be used to increase O-GlcNAc levels on nuclear and cytoplasmic proteins in vivo.
9452489	1	69	theme	post-translational	299:316	arg1	modification					318:329	a ubiquitous and abundant post-translational modification	273:329	a ubiquitous and abundant post-translational modification found on nuclear and cytoplasmic proteins	273:371	O-Linked N-acetylglucosamine (O-GlcNAc) is a ubiquitous and abundant post-translational modification found on nuclear and cytoplasmic proteins and is thought to be a dynamically regulated modification much like phosphorylation.
9452489	1	69	theme	post-translational	299:316	arg1	N-acetylglucosamine					239:257	O-Linked N-acetylglucosamine	230:257	O-Linked N-acetylglucosamine (O-GlcNAc)	230:268	O-Linked N-acetylglucosamine (O-GlcNAc) is a ubiquitous and abundant post-translational modification found on nuclear and cytoplasmic proteins and is thought to be a dynamically regulated modification much like phosphorylation.
9452489	4	70	theme	O-GlcNAc-beta-N-acetylglucosaminidase	1052:1088	arg1	inhibition					1026:1035	the direct inhibition	1015:1035	the direct inhibition of the peptide O-GlcNAc-beta-N-acetylglucosaminidase	1015:1088	The increase appeared to be the result of the direct inhibition of the peptide O-GlcNAc-beta-N-acetylglucosaminidase since neither the O-GlcNAc transferase nor UDP-GlcNAc levels were affected by the treatment.
9452489	8	71	used	used	1811:1814	arg2	PUGNAc					1733:1738	PUGNAc	1733:1738	PUGNAc	1733:1738	These studies demonstrate that PUGNAc is an effective inhibitor of O-GlcNAc turnover within cells and can be used to selectively alter the extent of O-GlcNAc on cellular proteins.
9452489	8	71	used	used	1811:1814	arg2	inhibitor					1756:1764	an effective inhibitor	1743:1764	an effective inhibitor of O-GlcNAc turnover	1743:1785	These studies demonstrate that PUGNAc is an effective inhibitor of O-GlcNAc turnover within cells and can be used to selectively alter the extent of O-GlcNAc on cellular proteins.
9452489	7	72	from	Sp1	1549:1551	arg1	increase					1493:1500	an increase	1490:1500	an increase in O-GlcNAc levels on the transcription factor Sp1	1490:1551	Interestingly, we demonstrated that an increase in O-GlcNAc levels on the transcription factor Sp1 resulted in a reciprocal decrease in its level of phosphorylation, supporting the hypothesis that O-GlcNAc competes with phosphate on some proteins.
9452489	3	73	theme	human	889:893	arg1	HT29					915:918	HT29	915:918	HT29	915:918	Overall, PUGNAc caused approximately a 2-fold increase in O-GlcNAc levels in the human colon cancer cells, HT29, although the effects on individual proteins varied.
9452489	3	73	theme	human	889:893	arg1	cells					908:912	the human colon cancer cells	885:912	the human colon cancer cells	885:912	Overall, PUGNAc caused approximately a 2-fold increase in O-GlcNAc levels in the human colon cancer cells, HT29, although the effects on individual proteins varied.
9452489	0	74	theme	cytoplasmic	65:75	arg1	proteins					77:84	nuclear and cytoplasmic proteins	53:84	nuclear and cytoplasmic proteins	53:84	Modulation of O-linked N-acetylglucosamine levels on nuclear and cytoplasmic proteins in vivo using the peptide O-GlcNAc-beta-N-acetylglucosaminidase inhibitor O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate.
9452489	1	75	theme	regulated	408:416	arg1	N-acetylglucosamine					239:257	O-Linked N-acetylglucosamine	230:257	O-Linked N-acetylglucosamine (O-GlcNAc)	230:268	O-Linked N-acetylglucosamine (O-GlcNAc) is a ubiquitous and abundant post-translational modification found on nuclear and cytoplasmic proteins and is thought to be a dynamically regulated modification much like phosphorylation.
9452489	1	75	theme	regulated	408:416	arg1	modification					418:429	a dynamically regulated modification	394:429	a dynamically regulated modification	394:429	O-Linked N-acetylglucosamine (O-GlcNAc) is a ubiquitous and abundant post-translational modification found on nuclear and cytoplasmic proteins and is thought to be a dynamically regulated modification much like phosphorylation.
9452489	3	76	theme	cancer	901:906	arg1	HT29					915:918	HT29	915:918	HT29	915:918	Overall, PUGNAc caused approximately a 2-fold increase in O-GlcNAc levels in the human colon cancer cells, HT29, although the effects on individual proteins varied.
9452489	3	76	theme	cancer	901:906	arg1	cells					908:912	the human colon cancer cells	885:912	the human colon cancer cells	885:912	Overall, PUGNAc caused approximately a 2-fold increase in O-GlcNAc levels in the human colon cancer cells, HT29, although the effects on individual proteins varied.
9452489	3	77	theme	colon	895:899	arg1	HT29					915:918	HT29	915:918	HT29	915:918	Overall, PUGNAc caused approximately a 2-fold increase in O-GlcNAc levels in the human colon cancer cells, HT29, although the effects on individual proteins varied.
9452489	3	77	theme	colon	895:899	arg1	cells					908:912	the human colon cancer cells	885:912	the human colon cancer cells	885:912	Overall, PUGNAc caused approximately a 2-fold increase in O-GlcNAc levels in the human colon cancer cells, HT29, although the effects on individual proteins varied.
23013401	8	0	from	regulator	1339:1347	arg1	control					1356:1362	the control	1352:1362	the control of NCT genes	1352:1375	Taken together, these results suggest that Sp1 could be a key regulator in the control of NCT genes and that reactive oxygen species-mediated alteration in Sp1 stability may be responsible for the generalized repression of those genes, leading to formation of the senescence-dependent functional nuclear barrier, resulting in subsequent hyporesponsiveness to external signals.
23013401	8	1	theme	generalized	1474:1484	arg1	repression					1486:1495	the generalized repression	1470:1495	the generalized repression of those genes	1470:1510	Taken together, these results suggest that Sp1 could be a key regulator in the control of NCT genes and that reactive oxygen species-mediated alteration in Sp1 stability may be responsible for the generalized repression of those genes, leading to formation of the senescence-dependent functional nuclear barrier, resulting in subsequent hyporesponsiveness to external signals.
23013401	5	2	theme	senescent	989:997	arg1	HDFs					999:1002	senescent HDFs	989:1002	senescent HDFs	989:1002	In addition, epidermal growth factor stimulation-induced p-ERK1/2 nuclear translocation and Elk-1 phosphorylation were severely impaired by Sp1 depletion in young HDFs; Sp1 overexpression restored the nuclear translocation of p-ERK1/2 in senescent HDFs.
23013401	1	3	theme	apoptotic	170:178	arg1	stimuli					180:186	apoptotic stimuli	170:186	apoptotic stimuli	170:186	Hyporesponsiveness to external signals, such as growth factors and apoptotic stimuli, is a cardinal feature of cellular senescence.
23013401	8	4	theme	barrier	1581:1587	arg1	formation					1524:1532	formation	1524:1532	formation of the senescence-dependent functional nuclear barrier, resulting in subsequent hyporesponsiveness to external signals	1524:1651	Taken together, these results suggest that Sp1 could be a key regulator in the control of NCT genes and that reactive oxygen species-mediated alteration in Sp1 stability may be responsible for the generalized repression of those genes, leading to formation of the senescence-dependent functional nuclear barrier, resulting in subsequent hyporesponsiveness to external signals.
23013401	8	5	theme	key	1335:1337	arg1	regulator					1339:1347	a key regulator	1333:1347	a key regulator	1333:1347	Taken together, these results suggest that Sp1 could be a key regulator in the control of NCT genes and that reactive oxygen species-mediated alteration in Sp1 stability may be responsible for the generalized repression of those genes, leading to formation of the senescence-dependent functional nuclear barrier, resulting in subsequent hyporesponsiveness to external signals.
23013401	8	5	theme	key	1335:1337	arg1	Sp1					1320:1322	Sp1	1320:1322	Sp1	1320:1322	Taken together, these results suggest that Sp1 could be a key regulator in the control of NCT genes and that reactive oxygen species-mediated alteration in Sp1 stability may be responsible for the generalized repression of those genes, leading to formation of the senescence-dependent functional nuclear barrier, resulting in subsequent hyporesponsiveness to external signals.
23013401	8	6	theme	oxygen	1395:1400	arg1	alteration					1419:1428	reactive oxygen species-mediated alteration	1386:1428	reactive oxygen species-mediated alteration in Sp1 stability	1386:1445	Taken together, these results suggest that Sp1 could be a key regulator in the control of NCT genes and that reactive oxygen species-mediated alteration in Sp1 stability may be responsible for the generalized repression of those genes, leading to formation of the senescence-dependent functional nuclear barrier, resulting in subsequent hyporesponsiveness to external signals.
23013401	6	7	theme	H	1093:1093	arg1	O					1098:1098	H(2) O(2)	1093:1101	H(2) O(2) treatment	1093:1111	Furthermore, we observed that Sp1 protein levels were decreased in senescent cells, and H(2) O(2) treatment decreased Sp1 levels in a proteasome-dependent manner.
23013401	5	8	from	translocation	960:972	arg1	HDFs					999:1002	senescent HDFs	989:1002	senescent HDFs	989:1002	In addition, epidermal growth factor stimulation-induced p-ERK1/2 nuclear translocation and Elk-1 phosphorylation were severely impaired by Sp1 depletion in young HDFs; Sp1 overexpression restored the nuclear translocation of p-ERK1/2 in senescent HDFs.
23013401	8	9	theme	functional	1562:1571	arg1	barrier					1581:1587	the senescence-dependent functional nuclear barrier	1537:1587	the senescence-dependent functional nuclear barrier	1537:1587	Taken together, these results suggest that Sp1 could be a key regulator in the control of NCT genes and that reactive oxygen species-mediated alteration in Sp1 stability may be responsible for the generalized repression of those genes, leading to formation of the senescence-dependent functional nuclear barrier, resulting in subsequent hyporesponsiveness to external signals.
23013401	8	10	theme	reactive	1386:1393	arg1	alteration					1419:1428	reactive oxygen species-mediated alteration	1386:1428	reactive oxygen species-mediated alteration in Sp1 stability	1386:1445	Taken together, these results suggest that Sp1 could be a key regulator in the control of NCT genes and that reactive oxygen species-mediated alteration in Sp1 stability may be responsible for the generalized repression of those genes, leading to formation of the senescence-dependent functional nuclear barrier, resulting in subsequent hyporesponsiveness to external signals.
23013401	2	11	theme	trafficking	320:330	arg1	genes					346:350	nucleocytoplasmic trafficking (NCT)-related genes	302:350	nucleocytoplasmic trafficking (NCT)-related genes	302:350	We previously reported that an aging-dependent marked reduction in nucleocytoplasmic trafficking (NCT)-related genes could be responsible for this phenomenon.
23013401	7	12	theme	senescent	1221:1229	arg1	cells					1231:1235	senescent cells	1221:1235	senescent cells	1221:1235	In addition, O-GlcNAcylation of Sp1 was decreased in senescent cells as well as in H(2) O(2) -treated cells.
23013401	2	13	theme	nucleocytoplasmic	302:318	arg1	NCT					333:335	NCT	333:335	NCT	333:335	We previously reported that an aging-dependent marked reduction in nucleocytoplasmic trafficking (NCT)-related genes could be responsible for this phenomenon.
23013401	2	13	theme	nucleocytoplasmic	302:318	arg1	trafficking					320:330	nucleocytoplasmic trafficking	302:330	nucleocytoplasmic trafficking (NCT)-related genes	302:350	We previously reported that an aging-dependent marked reduction in nucleocytoplasmic trafficking (NCT)-related genes could be responsible for this phenomenon.
23013401	5	14	theme	Sp1	920:922	arg1	overexpression					924:937	Sp1 overexpression	920:937	Sp1 overexpression	920:937	In addition, epidermal growth factor stimulation-induced p-ERK1/2 nuclear translocation and Elk-1 phosphorylation were severely impaired by Sp1 depletion in young HDFs; Sp1 overexpression restored the nuclear translocation of p-ERK1/2 in senescent HDFs.
23013401	5	15	theme	young	908:912	arg1	HDFs					914:917	young HDFs	908:917	young HDFs	908:917	In addition, epidermal growth factor stimulation-induced p-ERK1/2 nuclear translocation and Elk-1 phosphorylation were severely impaired by Sp1 depletion in young HDFs; Sp1 overexpression restored the nuclear translocation of p-ERK1/2 in senescent HDFs.
23013401	5	16	theme	growth	774:779	arg1	factor					781:786	epidermal growth factor	764:786	epidermal growth factor	764:786	In addition, epidermal growth factor stimulation-induced p-ERK1/2 nuclear translocation and Elk-1 phosphorylation were severely impaired by Sp1 depletion in young HDFs; Sp1 overexpression restored the nuclear translocation of p-ERK1/2 in senescent HDFs.
23013401	5	17	theme	p-ERK1/2	977:984	arg1	translocation					960:972	the nuclear translocation	948:972	the nuclear translocation of p-ERK1/2 in senescent HDFs	948:1002	In addition, epidermal growth factor stimulation-induced p-ERK1/2 nuclear translocation and Elk-1 phosphorylation were severely impaired by Sp1 depletion in young HDFs; Sp1 overexpression restored the nuclear translocation of p-ERK1/2 in senescent HDFs.
23013401	8	18	theme	subsequent	1603:1612	arg1	hyporesponsiveness					1614:1631	subsequent hyporesponsiveness	1603:1631	subsequent hyporesponsiveness to external signals	1603:1651	Taken together, these results suggest that Sp1 could be a key regulator in the control of NCT genes and that reactive oxygen species-mediated alteration in Sp1 stability may be responsible for the generalized repression of those genes, leading to formation of the senescence-dependent functional nuclear barrier, resulting in subsequent hyporesponsiveness to external signals.
23013401	7	19	theme	O	1256:1256	arg1	cells					1270:1274	H(2) O(2) -treated cells	1251:1274	H(2) O(2) -treated cells	1251:1274	In addition, O-GlcNAcylation of Sp1 was decreased in senescent cells as well as in H(2) O(2) -treated cells.
23013401	8	20	theme	Sp1	1433:1435	arg1	stability					1437:1445	Sp1 stability	1433:1445	Sp1 stability	1433:1445	Taken together, these results suggest that Sp1 could be a key regulator in the control of NCT genes and that reactive oxygen species-mediated alteration in Sp1 stability may be responsible for the generalized repression of those genes, leading to formation of the senescence-dependent functional nuclear barrier, resulting in subsequent hyporesponsiveness to external signals.
23013401	4	21	theme	Sp1	597:599	arg1	knockdown					601:609	Sp1 knockdown	597:609	Sp1 knockdown	597:609	Sp1 knockdown led to a reduction of those genes in young human diploid fibroblast cells (HDF); Sp1 overexpression induced those genes in senescent cells.
23013401	8	22	theme	external	1636:1643	arg1	signals					1645:1651	external signals	1636:1651	external signals	1636:1651	Taken together, these results suggest that Sp1 could be a key regulator in the control of NCT genes and that reactive oxygen species-mediated alteration in Sp1 stability may be responsible for the generalized repression of those genes, leading to formation of the senescence-dependent functional nuclear barrier, resulting in subsequent hyporesponsiveness to external signals.
23013401	4	23	theme	genes	639:643	arg1	reduction					620:628	a reduction	618:628	a reduction of those genes in young human diploid fibroblast cells (HDF)	618:689	Sp1 knockdown led to a reduction of those genes in young human diploid fibroblast cells (HDF); Sp1 overexpression induced those genes in senescent cells.
23013401	0	24	theme	transcription	4:16	arg1	responsible					32:42	responsible	32:42	responsible	32:42	The transcription factor Sp1 is responsible for aging-dependent altered nucleocytoplasmic trafficking.
23013401	0	24	theme	transcription	4:16	arg1	Sp1					25:27	The transcription factor Sp1	0:27	The transcription factor Sp1	0:27	The transcription factor Sp1 is responsible for aging-dependent altered nucleocytoplasmic trafficking.
23013401	2	25	theme	-related	337:344	arg1	genes					346:350	nucleocytoplasmic trafficking (NCT)-related genes	302:350	nucleocytoplasmic trafficking (NCT)-related genes	302:350	We previously reported that an aging-dependent marked reduction in nucleocytoplasmic trafficking (NCT)-related genes could be responsible for this phenomenon.
23013401	8	26	theme	species-mediated	1402:1417	arg1	alteration					1419:1428	reactive oxygen species-mediated alteration	1386:1428	reactive oxygen species-mediated alteration in Sp1 stability	1386:1445	Taken together, these results suggest that Sp1 could be a key regulator in the control of NCT genes and that reactive oxygen species-mediated alteration in Sp1 stability may be responsible for the generalized repression of those genes, leading to formation of the senescence-dependent functional nuclear barrier, resulting in subsequent hyporesponsiveness to external signals.
23013401	4	27	theme	human	654:658	arg1	cells					679:683	young human diploid fibroblast cells	648:683	young human diploid fibroblast cells (HDF)	648:689	Sp1 knockdown led to a reduction of those genes in young human diploid fibroblast cells (HDF); Sp1 overexpression induced those genes in senescent cells.
23013401	4	27	theme	human	654:658	arg1	HDF					686:688	HDF	686:688	HDF	686:688	Sp1 knockdown led to a reduction of those genes in young human diploid fibroblast cells (HDF); Sp1 overexpression induced those genes in senescent cells.
23013401	8	28	theme	NCT	1367:1369	arg1	genes					1371:1375	NCT genes	1367:1375	NCT genes	1367:1375	Taken together, these results suggest that Sp1 could be a key regulator in the control of NCT genes and that reactive oxygen species-mediated alteration in Sp1 stability may be responsible for the generalized repression of those genes, leading to formation of the senescence-dependent functional nuclear barrier, resulting in subsequent hyporesponsiveness to external signals.
23013401	7	29	gly	O-GlcNAcylation	1181:1195	arg1	cells					1231:1235	senescent cells	1221:1235	senescent cells	1221:1235	In addition, O-GlcNAcylation of Sp1 was decreased in senescent cells as well as in H(2) O(2) -treated cells.
23013401	7	29	gly	O-GlcNAcylation	1181:1195	arg1	cells					1270:1274	H(2) O(2) -treated cells	1251:1274	H(2) O(2) -treated cells	1251:1274	In addition, O-GlcNAcylation of Sp1 was decreased in senescent cells as well as in H(2) O(2) -treated cells.
23013401	7	29	gly	O-GlcNAcylation	1181:1195	arg1	addition					1171:1178	addition	1171:1178	addition	1171:1178	In addition, O-GlcNAcylation of Sp1 was decreased in senescent cells as well as in H(2) O(2) -treated cells.
23013401	4	30	theme	senescent	734:742	arg1	cells					744:748	senescent cells	734:748	senescent cells	734:748	Sp1 knockdown led to a reduction of those genes in young human diploid fibroblast cells (HDF); Sp1 overexpression induced those genes in senescent cells.
23013401	3	31	theme	transcription	444:456	arg1	factor					458:463	the transcription factor	440:463	the transcription factor	440:463	In searching for the mechanism, we identified the transcription factor, Sp1, as a common regulator of NCT genes, including various nucleoporins, importins, exportins, and Ran GTPase cycle-related genes.
23013401	3	31	theme	transcription	444:456	arg1	regulator					483:491	a common regulator	474:491	a common regulator of NCT genes, including various nucleoporins, importins, exportins, and Ran GTPase cycle-related genes	474:594	In searching for the mechanism, we identified the transcription factor, Sp1, as a common regulator of NCT genes, including various nucleoporins, importins, exportins, and Ran GTPase cycle-related genes.
23013401	3	31	theme	transcription	444:456	arg1	Sp1					466:468	Sp1	466:468	Sp1	466:468	In searching for the mechanism, we identified the transcription factor, Sp1, as a common regulator of NCT genes, including various nucleoporins, importins, exportins, and Ran GTPase cycle-related genes.
23013401	5	32	theme	stimulation-induced	788:806	arg1	translocation					825:837	epidermal growth factor stimulation-induced p-ERK1/2 nuclear translocation	764:837	epidermal growth factor stimulation-induced p-ERK1/2 nuclear translocation	764:837	In addition, epidermal growth factor stimulation-induced p-ERK1/2 nuclear translocation and Elk-1 phosphorylation were severely impaired by Sp1 depletion in young HDFs; Sp1 overexpression restored the nuclear translocation of p-ERK1/2 in senescent HDFs.
23013401	1	33	theme	external	125:132	arg1	stimuli					180:186	apoptotic stimuli	170:186	apoptotic stimuli	170:186	Hyporesponsiveness to external signals, such as growth factors and apoptotic stimuli, is a cardinal feature of cellular senescence.
23013401	1	33	theme	external	125:132	arg1	factors					158:164	growth factors	151:164	growth factors	151:164	Hyporesponsiveness to external signals, such as growth factors and apoptotic stimuli, is a cardinal feature of cellular senescence.
23013401	1	33	theme	external	125:132	arg1	signals					134:140	external signals	125:140	external signals	125:140	Hyporesponsiveness to external signals, such as growth factors and apoptotic stimuli, is a cardinal feature of cellular senescence.
23013401	5	34	theme	nuclear	817:823	arg1	translocation					825:837	epidermal growth factor stimulation-induced p-ERK1/2 nuclear translocation	764:837	epidermal growth factor stimulation-induced p-ERK1/2 nuclear translocation	764:837	In addition, epidermal growth factor stimulation-induced p-ERK1/2 nuclear translocation and Elk-1 phosphorylation were severely impaired by Sp1 depletion in young HDFs; Sp1 overexpression restored the nuclear translocation of p-ERK1/2 in senescent HDFs.
23013401	0	35	theme	factor	18:23	arg1	responsible					32:42	responsible	32:42	responsible	32:42	The transcription factor Sp1 is responsible for aging-dependent altered nucleocytoplasmic trafficking.
23013401	0	35	theme	factor	18:23	arg1	Sp1					25:27	The transcription factor Sp1	0:27	The transcription factor Sp1	0:27	The transcription factor Sp1 is responsible for aging-dependent altered nucleocytoplasmic trafficking.
23013401	5	36	theme	nuclear	952:958	arg1	translocation					960:972	the nuclear translocation	948:972	the nuclear translocation of p-ERK1/2 in senescent HDFs	948:1002	In addition, epidermal growth factor stimulation-induced p-ERK1/2 nuclear translocation and Elk-1 phosphorylation were severely impaired by Sp1 depletion in young HDFs; Sp1 overexpression restored the nuclear translocation of p-ERK1/2 in senescent HDFs.
23013401	4	37	from	reduction	620:628	arg1	cells					679:683	young human diploid fibroblast cells	648:683	young human diploid fibroblast cells (HDF)	648:689	Sp1 knockdown led to a reduction of those genes in young human diploid fibroblast cells (HDF); Sp1 overexpression induced those genes in senescent cells.
23013401	4	37	from	reduction	620:628	arg1	HDF					686:688	HDF	686:688	HDF	686:688	Sp1 knockdown led to a reduction of those genes in young human diploid fibroblast cells (HDF); Sp1 overexpression induced those genes in senescent cells.
23013401	3	38	theme	genes	500:504	arg1	factor					458:463	the transcription factor	440:463	the transcription factor	440:463	In searching for the mechanism, we identified the transcription factor, Sp1, as a common regulator of NCT genes, including various nucleoporins, importins, exportins, and Ran GTPase cycle-related genes.
23013401	3	38	theme	genes	500:504	arg1	regulator					483:491	a common regulator	474:491	a common regulator of NCT genes, including various nucleoporins, importins, exportins, and Ran GTPase cycle-related genes	474:594	In searching for the mechanism, we identified the transcription factor, Sp1, as a common regulator of NCT genes, including various nucleoporins, importins, exportins, and Ran GTPase cycle-related genes.
23013401	6	39	theme	O	1098:1098	arg1	treatment					1103:1111	H(2) O(2) treatment	1093:1111	H(2) O(2) treatment	1093:1111	Furthermore, we observed that Sp1 protein levels were decreased in senescent cells, and H(2) O(2) treatment decreased Sp1 levels in a proteasome-dependent manner.
23013401	6	40	theme	protein	1039:1045	arg1	levels					1047:1052	Sp1 protein levels	1035:1052	Sp1 protein levels	1035:1052	Furthermore, we observed that Sp1 protein levels were decreased in senescent cells, and H(2) O(2) treatment decreased Sp1 levels in a proteasome-dependent manner.
23013401	1	41	theme	cardinal	194:201	arg1	Hyporesponsiveness					103:120	Hyporesponsiveness	103:120	Hyporesponsiveness to external signals, such as growth factors and apoptotic stimuli,	103:187	Hyporesponsiveness to external signals, such as growth factors and apoptotic stimuli, is a cardinal feature of cellular senescence.
23013401	1	41	theme	cardinal	194:201	arg1	feature					203:209	a cardinal feature	192:209	a cardinal feature of cellular senescence	192:232	Hyporesponsiveness to external signals, such as growth factors and apoptotic stimuli, is a cardinal feature of cellular senescence.
23013401	1	42	theme	cellular	214:221	arg1	senescence					223:232	cellular senescence	214:232	cellular senescence	214:232	Hyporesponsiveness to external signals, such as growth factors and apoptotic stimuli, is a cardinal feature of cellular senescence.
23013401	5	43	theme	Elk-1	843:847	arg1	phosphorylation					849:863	Elk-1 phosphorylation	843:863	Elk-1 phosphorylation	843:863	In addition, epidermal growth factor stimulation-induced p-ERK1/2 nuclear translocation and Elk-1 phosphorylation were severely impaired by Sp1 depletion in young HDFs; Sp1 overexpression restored the nuclear translocation of p-ERK1/2 in senescent HDFs.
23013401	1	44	theme	senescence	223:232	arg1	Hyporesponsiveness					103:120	Hyporesponsiveness	103:120	Hyporesponsiveness to external signals, such as growth factors and apoptotic stimuli,	103:187	Hyporesponsiveness to external signals, such as growth factors and apoptotic stimuli, is a cardinal feature of cellular senescence.
23013401	1	44	theme	senescence	223:232	arg1	feature					203:209	a cardinal feature	192:209	a cardinal feature of cellular senescence	192:232	Hyporesponsiveness to external signals, such as growth factors and apoptotic stimuli, is a cardinal feature of cellular senescence.
23013401	0	45	theme	aging-dependent	48:62	arg1	trafficking					90:100	aging-dependent altered nucleocytoplasmic trafficking	48:100	aging-dependent altered nucleocytoplasmic trafficking	48:100	The transcription factor Sp1 is responsible for aging-dependent altered nucleocytoplasmic trafficking.
23013401	6	46	theme	Sp1	1035:1037	arg1	levels					1047:1052	Sp1 protein levels	1035:1052	Sp1 protein levels	1035:1052	Furthermore, we observed that Sp1 protein levels were decreased in senescent cells, and H(2) O(2) treatment decreased Sp1 levels in a proteasome-dependent manner.
23013401	3	47	theme	GTPase	569:574	arg1	genes					590:594	GTPase cycle-related genes	569:594	GTPase cycle-related genes	569:594	In searching for the mechanism, we identified the transcription factor, Sp1, as a common regulator of NCT genes, including various nucleoporins, importins, exportins, and Ran GTPase cycle-related genes.
23013401	3	48	dep	nucleoporins	525:536	arg1	genes					590:594	GTPase cycle-related genes	569:594	GTPase cycle-related genes	569:594	In searching for the mechanism, we identified the transcription factor, Sp1, as a common regulator of NCT genes, including various nucleoporins, importins, exportins, and Ran GTPase cycle-related genes.
23013401	5	49	theme	epidermal	764:772	arg1	factor					781:786	epidermal growth factor	764:786	epidermal growth factor	764:786	In addition, epidermal growth factor stimulation-induced p-ERK1/2 nuclear translocation and Elk-1 phosphorylation were severely impaired by Sp1 depletion in young HDFs; Sp1 overexpression restored the nuclear translocation of p-ERK1/2 in senescent HDFs.
23013401	8	50	from	alteration	1419:1428	arg1	stability					1437:1445	Sp1 stability	1433:1445	Sp1 stability	1433:1445	Taken together, these results suggest that Sp1 could be a key regulator in the control of NCT genes and that reactive oxygen species-mediated alteration in Sp1 stability may be responsible for the generalized repression of those genes, leading to formation of the senescence-dependent functional nuclear barrier, resulting in subsequent hyporesponsiveness to external signals.
23013401	3	51	theme	cycle-related	576:588	arg1	genes					590:594	GTPase cycle-related genes	569:594	GTPase cycle-related genes	569:594	In searching for the mechanism, we identified the transcription factor, Sp1, as a common regulator of NCT genes, including various nucleoporins, importins, exportins, and Ran GTPase cycle-related genes.
23013401	3	52	theme	NCT	496:498	arg1	importins					539:547	importins	539:547	importins	539:547	In searching for the mechanism, we identified the transcription factor, Sp1, as a common regulator of NCT genes, including various nucleoporins, importins, exportins, and Ran GTPase cycle-related genes.
23013401	3	52	theme	NCT	496:498	arg1	nucleoporins					525:536	various nucleoporins	517:536	various nucleoporins	517:536	In searching for the mechanism, we identified the transcription factor, Sp1, as a common regulator of NCT genes, including various nucleoporins, importins, exportins, and Ran GTPase cycle-related genes.
23013401	3	52	theme	NCT	496:498	arg1	exportins					550:558	exportins	550:558	exportins	550:558	In searching for the mechanism, we identified the transcription factor, Sp1, as a common regulator of NCT genes, including various nucleoporins, importins, exportins, and Ran GTPase cycle-related genes.
23013401	3	52	theme	NCT	496:498	arg1	genes					500:504	NCT genes	496:504	NCT genes	496:504	In searching for the mechanism, we identified the transcription factor, Sp1, as a common regulator of NCT genes, including various nucleoporins, importins, exportins, and Ran GTPase cycle-related genes.
23013401	3	52	theme	NCT	496:498	arg1	Ran					565:567	Ran	565:567	Ran	565:567	In searching for the mechanism, we identified the transcription factor, Sp1, as a common regulator of NCT genes, including various nucleoporins, importins, exportins, and Ran GTPase cycle-related genes.
23013401	8	53	theme	senescence-dependent	1541:1560	arg1	barrier					1581:1587	the senescence-dependent functional nuclear barrier	1537:1587	the senescence-dependent functional nuclear barrier	1537:1587	Taken together, these results suggest that Sp1 could be a key regulator in the control of NCT genes and that reactive oxygen species-mediated alteration in Sp1 stability may be responsible for the generalized repression of those genes, leading to formation of the senescence-dependent functional nuclear barrier, resulting in subsequent hyporesponsiveness to external signals.
23013401	6	54	theme	proteasome-dependent	1139:1158	arg1	manner					1160:1165	a proteasome-dependent manner	1137:1165	a proteasome-dependent manner	1137:1165	Furthermore, we observed that Sp1 protein levels were decreased in senescent cells, and H(2) O(2) treatment decreased Sp1 levels in a proteasome-dependent manner.
23013401	4	55	theme	young	648:652	arg1	cells					679:683	young human diploid fibroblast cells	648:683	young human diploid fibroblast cells (HDF)	648:689	Sp1 knockdown led to a reduction of those genes in young human diploid fibroblast cells (HDF); Sp1 overexpression induced those genes in senescent cells.
23013401	4	55	theme	young	648:652	arg1	HDF					686:688	HDF	686:688	HDF	686:688	Sp1 knockdown led to a reduction of those genes in young human diploid fibroblast cells (HDF); Sp1 overexpression induced those genes in senescent cells.
23013401	2	56	theme	marked	282:287	arg1	reduction					289:297	an aging-dependent marked reduction	263:297	an aging-dependent marked reduction in nucleocytoplasmic trafficking (NCT)-related genes	263:350	We previously reported that an aging-dependent marked reduction in nucleocytoplasmic trafficking (NCT)-related genes could be responsible for this phenomenon.
23013401	2	56	theme	marked	282:287	arg1	responsible					361:371	responsible	361:371	responsible	361:371	We previously reported that an aging-dependent marked reduction in nucleocytoplasmic trafficking (NCT)-related genes could be responsible for this phenomenon.
23013401	4	57	theme	diploid	660:666	arg1	cells					679:683	young human diploid fibroblast cells	648:683	young human diploid fibroblast cells (HDF)	648:689	Sp1 knockdown led to a reduction of those genes in young human diploid fibroblast cells (HDF); Sp1 overexpression induced those genes in senescent cells.
23013401	4	57	theme	diploid	660:666	arg1	HDF					686:688	HDF	686:688	HDF	686:688	Sp1 knockdown led to a reduction of those genes in young human diploid fibroblast cells (HDF); Sp1 overexpression induced those genes in senescent cells.
23013401	3	58	theme	common	476:481	arg1	factor					458:463	the transcription factor	440:463	the transcription factor	440:463	In searching for the mechanism, we identified the transcription factor, Sp1, as a common regulator of NCT genes, including various nucleoporins, importins, exportins, and Ran GTPase cycle-related genes.
23013401	3	58	theme	common	476:481	arg1	regulator					483:491	a common regulator	474:491	a common regulator of NCT genes, including various nucleoporins, importins, exportins, and Ran GTPase cycle-related genes	474:594	In searching for the mechanism, we identified the transcription factor, Sp1, as a common regulator of NCT genes, including various nucleoporins, importins, exportins, and Ran GTPase cycle-related genes.
23013401	2	59	from	reduction	289:297	arg1	genes					346:350	nucleocytoplasmic trafficking (NCT)-related genes	302:350	nucleocytoplasmic trafficking (NCT)-related genes	302:350	We previously reported that an aging-dependent marked reduction in nucleocytoplasmic trafficking (NCT)-related genes could be responsible for this phenomenon.
23013401	6	60	theme	Sp1	1123:1125	arg1	levels					1127:1132	Sp1 levels	1123:1132	Sp1 levels	1123:1132	Furthermore, we observed that Sp1 protein levels were decreased in senescent cells, and H(2) O(2) treatment decreased Sp1 levels in a proteasome-dependent manner.
23013401	8	61	theme	genes	1371:1375	arg1	control					1356:1362	the control	1352:1362	the control of NCT genes	1352:1375	Taken together, these results suggest that Sp1 could be a key regulator in the control of NCT genes and that reactive oxygen species-mediated alteration in Sp1 stability may be responsible for the generalized repression of those genes, leading to formation of the senescence-dependent functional nuclear barrier, resulting in subsequent hyporesponsiveness to external signals.
23013401	2	62	theme	aging-dependent	266:280	arg1	reduction					289:297	an aging-dependent marked reduction	263:297	an aging-dependent marked reduction in nucleocytoplasmic trafficking (NCT)-related genes	263:350	We previously reported that an aging-dependent marked reduction in nucleocytoplasmic trafficking (NCT)-related genes could be responsible for this phenomenon.
23013401	2	62	theme	aging-dependent	266:280	arg1	responsible					361:371	responsible	361:371	responsible	361:371	We previously reported that an aging-dependent marked reduction in nucleocytoplasmic trafficking (NCT)-related genes could be responsible for this phenomenon.
23013401	1	63	theme	growth	151:156	arg1	factors					158:164	growth factors	151:164	growth factors	151:164	Hyporesponsiveness to external signals, such as growth factors and apoptotic stimuli, is a cardinal feature of cellular senescence.
23013401	8	64	theme	nuclear	1573:1579	arg1	barrier					1581:1587	the senescence-dependent functional nuclear barrier	1537:1587	the senescence-dependent functional nuclear barrier	1537:1587	Taken together, these results suggest that Sp1 could be a key regulator in the control of NCT genes and that reactive oxygen species-mediated alteration in Sp1 stability may be responsible for the generalized repression of those genes, leading to formation of the senescence-dependent functional nuclear barrier, resulting in subsequent hyporesponsiveness to external signals.
23013401	4	65	theme	Sp1	692:694	arg1	overexpression					696:709	Sp1 overexpression	692:709	Sp1 overexpression	692:709	Sp1 knockdown led to a reduction of those genes in young human diploid fibroblast cells (HDF); Sp1 overexpression induced those genes in senescent cells.
23013401	0	66	theme	nucleocytoplasmic	72:88	arg1	trafficking					90:100	aging-dependent altered nucleocytoplasmic trafficking	48:100	aging-dependent altered nucleocytoplasmic trafficking	48:100	The transcription factor Sp1 is responsible for aging-dependent altered nucleocytoplasmic trafficking.
23013401	5	67	theme	Sp1	891:893	arg1	depletion					895:903	Sp1 depletion	891:903	Sp1 depletion	891:903	In addition, epidermal growth factor stimulation-induced p-ERK1/2 nuclear translocation and Elk-1 phosphorylation were severely impaired by Sp1 depletion in young HDFs; Sp1 overexpression restored the nuclear translocation of p-ERK1/2 in senescent HDFs.
23013401	7	68	theme	H	1251:1251	arg1	O					1256:1256	H(2) O(2)	1251:1259	H(2) O(2) -treated cells	1251:1274	In addition, O-GlcNAcylation of Sp1 was decreased in senescent cells as well as in H(2) O(2) -treated cells.
23013401	4	69	theme	fibroblast	668:677	arg1	cells					679:683	young human diploid fibroblast cells	648:683	young human diploid fibroblast cells (HDF)	648:689	Sp1 knockdown led to a reduction of those genes in young human diploid fibroblast cells (HDF); Sp1 overexpression induced those genes in senescent cells.
23013401	4	69	theme	fibroblast	668:677	arg1	HDF					686:688	HDF	686:688	HDF	686:688	Sp1 knockdown led to a reduction of those genes in young human diploid fibroblast cells (HDF); Sp1 overexpression induced those genes in senescent cells.
23013401	6	70	theme	senescent	1072:1080	arg1	cells					1082:1086	senescent cells	1072:1086	senescent cells	1072:1086	Furthermore, we observed that Sp1 protein levels were decreased in senescent cells, and H(2) O(2) treatment decreased Sp1 levels in a proteasome-dependent manner.
23013401	0	71	theme	altered	64:70	arg1	trafficking					90:100	aging-dependent altered nucleocytoplasmic trafficking	48:100	aging-dependent altered nucleocytoplasmic trafficking	48:100	The transcription factor Sp1 is responsible for aging-dependent altered nucleocytoplasmic trafficking.
23013401	7	72	theme	-treated	1261:1268	arg1	cells					1270:1274	H(2) O(2) -treated cells	1251:1274	H(2) O(2) -treated cells	1251:1274	In addition, O-GlcNAcylation of Sp1 was decreased in senescent cells as well as in H(2) O(2) -treated cells.
23013401	5	73	theme	p-ERK1/2	808:815	arg1	translocation					825:837	epidermal growth factor stimulation-induced p-ERK1/2 nuclear translocation	764:837	epidermal growth factor stimulation-induced p-ERK1/2 nuclear translocation	764:837	In addition, epidermal growth factor stimulation-induced p-ERK1/2 nuclear translocation and Elk-1 phosphorylation were severely impaired by Sp1 depletion in young HDFs; Sp1 overexpression restored the nuclear translocation of p-ERK1/2 in senescent HDFs.
23013401	3	74	theme	various	517:523	arg1	nucleoporins					525:536	various nucleoporins	517:536	various nucleoporins	517:536	In searching for the mechanism, we identified the transcription factor, Sp1, as a common regulator of NCT genes, including various nucleoporins, importins, exportins, and Ran GTPase cycle-related genes.
23013401	7	75	theme	Sp1	1200:1202	arg1	O-GlcNAcylation					1181:1195	O-GlcNAcylation	1181:1195	O-GlcNAcylation of Sp1	1181:1202	In addition, O-GlcNAcylation of Sp1 was decreased in senescent cells as well as in H(2) O(2) -treated cells.
23013401	8	76	theme	genes	1506:1510	arg1	repression					1486:1495	the generalized repression	1470:1495	the generalized repression of those genes	1470:1510	Taken together, these results suggest that Sp1 could be a key regulator in the control of NCT genes and that reactive oxygen species-mediated alteration in Sp1 stability may be responsible for the generalized repression of those genes, leading to formation of the senescence-dependent functional nuclear barrier, resulting in subsequent hyporesponsiveness to external signals.
21526146	12	0	theme	deprivation	2161:2171	arg1	conditions					2173:2182	stress and deprivation conditions	2150:2182	conditions	2173:2182	We also suggest that the repression of mature N-linked glycoproteins due to increased levels of N-GlcNAc(2)-modified proteins is a newly recognized pathway for effective use of sugar under stress and deprivation conditions.
21526146	2	1	link	O-linked	363:370	arg1	transferase					394:404	O-linked β-N-acetylglucosamine transferase	363:404	O-linked β-N-acetylglucosamine transferase (OGT)	363:410	O-GlcNAc modification is reversibly regulated by O-linked β-N-acetylglucosamine transferase (OGT) and β-D-N-acetylglucosaminase (O-GlcNAcase).
21526146	2	1	link	O-linked	363:370	arg1	OGT					407:409	OGT	407:409	OGT	407:409	O-GlcNAc modification is reversibly regulated by O-linked β-N-acetylglucosamine transferase (OGT) and β-D-N-acetylglucosaminase (O-GlcNAcase).
21526146	1	2	theme	β-N-acetylglucosamine	187:207	arg1	glycosylation					220:232	O-linked β-N-acetylglucosamine (O-GlcNAc) glycosylation	178:232	O-linked β-N-acetylglucosamine (O-GlcNAc) glycosylation	178:232	Modification of serine and threonine residues in proteins by O-linked β-N-acetylglucosamine (O-GlcNAc) glycosylation is a feature of many cellular responses to the nutritional state and to stress.
21526146	1	3	theme	nutritional	281:291	arg1	state					293:297	the nutritional state	277:297	the nutritional state	277:297	Modification of serine and threonine residues in proteins by O-linked β-N-acetylglucosamine (O-GlcNAc) glycosylation is a feature of many cellular responses to the nutritional state and to stress.
21526146	12	4	theme	mature	2000:2005	arg1	glycoproteins					2016:2028	mature N-linked glycoproteins	2000:2028	mature N-linked glycoproteins	2000:2028	We also suggest that the repression of mature N-linked glycoproteins due to increased levels of N-GlcNAc(2)-modified proteins is a newly recognized pathway for effective use of sugar under stress and deprivation conditions.
21526146	11	5	theme	proteins	1824:1831	arg1	status					1814:1819	the glycosylation status	1796:1819	the glycosylation status of proteins previously classified as O-GlcNAc-modified proteins according to their reactivity with CTD110.6 antibodies	1796:1938	We therefore propose that the glycosylation status of proteins previously classified as O-GlcNAc-modified proteins according to their reactivity with CTD110.6 antibodies must be re-examined.
21526146	13	6	theme	proteins	2288:2295	arg1	roles					2258:2262	the physiological and pathological roles	2223:2262	the physiological and pathological roles of N-GlcNAc(2)-modified proteins	2223:2295	Further research is needed to clarify the physiological and pathological roles of N-GlcNAc(2)-modified proteins.
21526146	9	7	theme	ALG1	1524:1527	arg1	ts-mutant					1511:1519	a ts-mutant	1509:1519	a ts-mutant of ALG1 that could not add a mannose residue to dolichol-PP-GlcNAc(2)	1509:1589	Furthermore, CTD110.6 antibodies reacted with N-GlcNAc(2)-modified glycoproteins produced by a yeast strain with a ts-mutant of ALG1 that could not add a mannose residue to dolichol-PP-GlcNAc(2).
21526146	7	8	with	treatment	1217:1225	arg1	tunicamycin					1232:1242	tunicamycin	1232:1242	tunicamycin	1232:1242	We found that this induced glycosylation was not regulated by OGT and O-GlcNAcase, unlike typical O-GlcNAcylation, and it was inhibited by treatment with tunicamycin, an N-glycosylation inhibitor.
21526146	7	8	with	treatment	1217:1225	arg1	inhibitor					1264:1272	an N-glycosylation inhibitor	1245:1272	an N-glycosylation inhibitor	1245:1272	We found that this induced glycosylation was not regulated by OGT and O-GlcNAcase, unlike typical O-GlcNAcylation, and it was inhibited by treatment with tunicamycin, an N-glycosylation inhibitor.
21526146	10	9	theme	-modified	1633:1641	arg1	glycoproteins					1643:1655	N-GlcNAc(2)-modified glycoproteins	1622:1655	N-GlcNAc(2)-modified glycoproteins	1622:1655	Our results demonstrated that N-GlcNAc(2)-modified glycoproteins were induced under glucose deprivation and that they cross-reacted with the O-GlcNAc-specific antibody CTD110.6.
21526146	6	10	theme	increased	921:929	arg1	modification					1024:1035	modification	1024:1035	modification by N-GlcNAc(2), rather than by O-GlcNAc	1024:1075	Here we show that the increased glycosylation induced by glucose deprivation and detected by CTD110.6 antibodies is actually modification by N-GlcNAc(2), rather than by O-GlcNAc.
21526146	6	10	theme	increased	921:929	arg1	glycosylation					931:943	the increased glycosylation	917:943	the increased glycosylation induced by glucose deprivation and detected by CTD110.6 antibodies	917:1010	Here we show that the increased glycosylation induced by glucose deprivation and detected by CTD110.6 antibodies is actually modification by N-GlcNAc(2), rather than by O-GlcNAc.
21526146	4	11	theme	glucose	756:762	arg1	deprivation					764:774	glucose deprivation	756:774	glucose deprivation	756:774	Immunoblot analysis using the O-GlcNAc-specific antibody CTD110.6 has indicated that glucose deprivation increases protein O-GlcNAcylation in some cancer cells.
21526146	4	12	theme	Immunoblot	671:680	arg1	analysis					682:689	Immunoblot analysis	671:689	Immunoblot analysis using the O-GlcNAc-specific antibody CTD110.6	671:735	Immunoblot analysis using the O-GlcNAc-specific antibody CTD110.6 has indicated that glucose deprivation increases protein O-GlcNAcylation in some cancer cells.
21526146	12	13	gly	glycoproteins	2016:2028	arg1	glycoproteins					2016:2028	mature N-linked glycoproteins	2000:2028	mature N-linked glycoproteins	2000:2028	We also suggest that the repression of mature N-linked glycoproteins due to increased levels of N-GlcNAc(2)-modified proteins is a newly recognized pathway for effective use of sugar under stress and deprivation conditions.
21526146	12	14	theme	-modified	2068:2076	arg1	proteins					2078:2085	N-GlcNAc(2)-modified proteins	2057:2085	N-GlcNAc(2)-modified proteins	2057:2085	We also suggest that the repression of mature N-linked glycoproteins due to increased levels of N-GlcNAc(2)-modified proteins is a newly recognized pathway for effective use of sugar under stress and deprivation conditions.
21526146	2	15	theme	O-GlcNAc	314:321	arg1	modification					323:334	O-GlcNAc modification	314:334	O-GlcNAc modification	314:334	O-GlcNAc modification is reversibly regulated by O-linked β-N-acetylglucosamine transferase (OGT) and β-D-N-acetylglucosaminase (O-GlcNAcase).
21526146	12	16	theme	glycoproteins	2016:2028	arg1	repression					1986:1995	the repression	1982:1995	the repression of mature N-linked glycoproteins due to increased levels of N-GlcNAc(2)-modified proteins	1982:2085	We also suggest that the repression of mature N-linked glycoproteins due to increased levels of N-GlcNAc(2)-modified proteins is a newly recognized pathway for effective use of sugar under stress and deprivation conditions.
21526146	12	16	theme	glycoproteins	2016:2028	arg1	pathway					2109:2115	a newly recognized pathway	2090:2115	a newly recognized pathway for effective use of sugar	2090:2142	We also suggest that the repression of mature N-linked glycoproteins due to increased levels of N-GlcNAc(2)-modified proteins is a newly recognized pathway for effective use of sugar under stress and deprivation conditions.
21526146	8	17	theme	-modified	1371:1379	arg1	glycoproteins					1381:1393	N-GlcNAc(2)-modified glycoproteins	1360:1393	N-GlcNAc(2)-modified glycoproteins	1360:1393	Proteomics analysis showed that proteins modified by this induced glycosylation were N-GlcNAc(2)-modified glycoproteins.
21526146	12	18	theme	sugar	2138:2142	arg1	use					2131:2133	effective use	2121:2133	effective use of sugar	2121:2142	We also suggest that the repression of mature N-linked glycoproteins due to increased levels of N-GlcNAc(2)-modified proteins is a newly recognized pathway for effective use of sugar under stress and deprivation conditions.
21526146	12	19	theme	increased	2037:2045	arg1	levels					2047:2052	increased levels	2037:2052	increased levels of N-GlcNAc(2)-modified proteins	2037:2085	We also suggest that the repression of mature N-linked glycoproteins due to increased levels of N-GlcNAc(2)-modified proteins is a newly recognized pathway for effective use of sugar under stress and deprivation conditions.
21526146	9	20	gly	glycoproteins	1463:1475	arg1	glycoproteins					1463:1475	N-GlcNAc(2)-modified glycoproteins	1442:1475	N-GlcNAc(2)-modified glycoproteins produced by a yeast strain with a ts-mutant of ALG1 that could not add a mannose residue to dolichol-PP-GlcNAc(2)	1442:1589	Furthermore, CTD110.6 antibodies reacted with N-GlcNAc(2)-modified glycoproteins produced by a yeast strain with a ts-mutant of ALG1 that could not add a mannose residue to dolichol-PP-GlcNAc(2).
21526146	12	21	link	N-linked	2007:2014	arg1	glycoproteins					2016:2028	mature N-linked glycoproteins	2000:2028	mature N-linked glycoproteins	2000:2028	We also suggest that the repression of mature N-linked glycoproteins due to increased levels of N-GlcNAc(2)-modified proteins is a newly recognized pathway for effective use of sugar under stress and deprivation conditions.
21526146	1	22	theme	O-GlcNAc	210:217	arg1	glycosylation					220:232	O-linked β-N-acetylglucosamine (O-GlcNAc) glycosylation	178:232	O-linked β-N-acetylglucosamine (O-GlcNAc) glycosylation	178:232	Modification of serine and threonine residues in proteins by O-linked β-N-acetylglucosamine (O-GlcNAc) glycosylation is a feature of many cellular responses to the nutritional state and to stress.
21526146	5	23	theme	paradoxical	854:864	arg1	phenomenon					866:875	this paradoxical phenomenon	849:875	this paradoxical phenomenon	849:875	The mechanism of this paradoxical phenomenon has remained unclear.
21526146	13	24	theme	Further	2185:2191	arg1	research					2193:2200	Further research	2185:2200	Further research	2185:2200	Further research is needed to clarify the physiological and pathological roles of N-GlcNAc(2)-modified proteins.
21526146	12	25	theme	proteins	2078:2085	arg1	levels					2047:2052	increased levels	2037:2052	increased levels of N-GlcNAc(2)-modified proteins	2037:2085	We also suggest that the repression of mature N-linked glycoproteins due to increased levels of N-GlcNAc(2)-modified proteins is a newly recognized pathway for effective use of sugar under stress and deprivation conditions.
21526146	3	26	theme	OGT	607:609	arg1	concentration					511:523	the concentration	507:523	the concentration	507:523	O-GlcNAc modification of proteins is dependent on the concentration of uridine 5'-diphospho-N-acetylglucosamine (UDP-GlcNAc), which is a substrate of OGT and is synthesized via the hexosamine biosynthetic pathway.
21526146	3	26	theme	OGT	607:609	arg1	substrate					594:602	a substrate	592:602	a substrate of OGT	592:609	O-GlcNAc modification of proteins is dependent on the concentration of uridine 5'-diphospho-N-acetylglucosamine (UDP-GlcNAc), which is a substrate of OGT and is synthesized via the hexosamine biosynthetic pathway.
21526146	11	27	theme	CTD110.6	1920:1927	arg1	antibodies					1929:1938	CTD110.6 antibodies	1920:1938	CTD110.6 antibodies	1920:1938	We therefore propose that the glycosylation status of proteins previously classified as O-GlcNAc-modified proteins according to their reactivity with CTD110.6 antibodies must be re-examined.
21526146	3	28	mod	modification	466:477	arg3	O-GlcNAc					457:464	O-GlcNAc modification	457:477	O-GlcNAc modification of proteins	457:489	O-GlcNAc modification of proteins is dependent on the concentration of uridine 5'-diphospho-N-acetylglucosamine (UDP-GlcNAc), which is a substrate of OGT and is synthesized via the hexosamine biosynthetic pathway.
21526146	3	28	mod	modification	466:477	arg1	proteins					482:489	proteins	482:489	proteins	482:489	O-GlcNAc modification of proteins is dependent on the concentration of uridine 5'-diphospho-N-acetylglucosamine (UDP-GlcNAc), which is a substrate of OGT and is synthesized via the hexosamine biosynthetic pathway.
21526146	12	29	theme	recognized	2098:2107	arg1	repression					1986:1995	the repression	1982:1995	the repression of mature N-linked glycoproteins due to increased levels of N-GlcNAc(2)-modified proteins	1982:2085	We also suggest that the repression of mature N-linked glycoproteins due to increased levels of N-GlcNAc(2)-modified proteins is a newly recognized pathway for effective use of sugar under stress and deprivation conditions.
21526146	12	29	theme	recognized	2098:2107	arg1	pathway					2109:2115	a newly recognized pathway	2090:2115	a newly recognized pathway for effective use of sugar	2090:2142	We also suggest that the repression of mature N-linked glycoproteins due to increased levels of N-GlcNAc(2)-modified proteins is a newly recognized pathway for effective use of sugar under stress and deprivation conditions.
21526146	11	30	gly	glycosylation	1800:1812	arg1	proteins					1824:1831	proteins	1824:1831	proteins previously classified as O-GlcNAc-modified proteins according to their reactivity with CTD110.6 antibodies	1824:1938	We therefore propose that the glycosylation status of proteins previously classified as O-GlcNAc-modified proteins according to their reactivity with CTD110.6 antibodies must be re-examined.
21526146	1	31	from	proteins	166:173	arg1	feature					239:245	a feature	237:245	a feature of many cellular responses to the nutritional state and to stress	237:311	Modification of serine and threonine residues in proteins by O-linked β-N-acetylglucosamine (O-GlcNAc) glycosylation is a feature of many cellular responses to the nutritional state and to stress.
21526146	1	31	from	proteins	166:173	arg1	Modification					117:128	Modification	117:128	Modification of serine and threonine residues in proteins by O-linked β-N-acetylglucosamine (O-GlcNAc) glycosylation	117:232	Modification of serine and threonine residues in proteins by O-linked β-N-acetylglucosamine (O-GlcNAc) glycosylation is a feature of many cellular responses to the nutritional state and to stress.
21526146	0	32	theme	O-GlcNAc-specific	0:16	arg1	antibody					18:25	O-GlcNAc-specific antibody CTD110.6	0:34	O-GlcNAc-specific antibody CTD110.6	0:34	O-GlcNAc-specific antibody CTD110.6 cross-reacts with N-GlcNAc2-modified proteins induced under glucose deprivation.
21526146	7	33	theme	N-glycosylation	1248:1262	arg1	tunicamycin					1232:1242	tunicamycin	1232:1242	tunicamycin	1232:1242	We found that this induced glycosylation was not regulated by OGT and O-GlcNAcase, unlike typical O-GlcNAcylation, and it was inhibited by treatment with tunicamycin, an N-glycosylation inhibitor.
21526146	7	33	theme	N-glycosylation	1248:1262	arg1	inhibitor					1264:1272	an N-glycosylation inhibitor	1245:1272	an N-glycosylation inhibitor	1245:1272	We found that this induced glycosylation was not regulated by OGT and O-GlcNAcase, unlike typical O-GlcNAcylation, and it was inhibited by treatment with tunicamycin, an N-glycosylation inhibitor.
21526146	1	34	from	threonine	144:152	arg1	proteins					166:173	proteins	166:173	proteins	166:173	Modification of serine and threonine residues in proteins by O-linked β-N-acetylglucosamine (O-GlcNAc) glycosylation is a feature of many cellular responses to the nutritional state and to stress.
21526146	3	35	theme	hexosamine	638:647	arg1	pathway					662:668	the hexosamine biosynthetic pathway	634:668	the hexosamine biosynthetic pathway	634:668	O-GlcNAc modification of proteins is dependent on the concentration of uridine 5'-diphospho-N-acetylglucosamine (UDP-GlcNAc), which is a substrate of OGT and is synthesized via the hexosamine biosynthetic pathway.
21526146	9	36	theme	mannose	1550:1556	arg1	residue					1558:1564	a mannose residue	1548:1564	a mannose residue	1548:1564	Furthermore, CTD110.6 antibodies reacted with N-GlcNAc(2)-modified glycoproteins produced by a yeast strain with a ts-mutant of ALG1 that could not add a mannose residue to dolichol-PP-GlcNAc(2).
21526146	8	37	theme	Proteomics	1275:1284	arg1	analysis					1286:1293	Proteomics analysis	1275:1293	Proteomics analysis	1275:1293	Proteomics analysis showed that proteins modified by this induced glycosylation were N-GlcNAc(2)-modified glycoproteins.
21526146	7	38	theme	typical	1168:1174	arg1	O-GlcNAcylation					1176:1190	typical O-GlcNAcylation	1168:1190	typical O-GlcNAcylation	1168:1190	We found that this induced glycosylation was not regulated by OGT and O-GlcNAcase, unlike typical O-GlcNAcylation, and it was inhibited by treatment with tunicamycin, an N-glycosylation inhibitor.
21526146	1	39	theme	serine	133:138	arg1	feature					239:245	a feature	237:245	a feature of many cellular responses to the nutritional state and to stress	237:311	Modification of serine and threonine residues in proteins by O-linked β-N-acetylglucosamine (O-GlcNAc) glycosylation is a feature of many cellular responses to the nutritional state and to stress.
21526146	1	39	theme	serine	133:138	arg1	Modification					117:128	Modification	117:128	Modification of serine and threonine residues in proteins by O-linked β-N-acetylglucosamine (O-GlcNAc) glycosylation	117:232	Modification of serine and threonine residues in proteins by O-linked β-N-acetylglucosamine (O-GlcNAc) glycosylation is a feature of many cellular responses to the nutritional state and to stress.
21526146	3	40	theme	uridine	528:534	arg1	UDP-GlcNAc					570:579	UDP-GlcNAc	570:579	UDP-GlcNAc	570:579	O-GlcNAc modification of proteins is dependent on the concentration of uridine 5'-diphospho-N-acetylglucosamine (UDP-GlcNAc), which is a substrate of OGT and is synthesized via the hexosamine biosynthetic pathway.
21526146	3	40	theme	uridine	528:534	arg1	5'-diphospho-N-acetylglucosamine					536:567	uridine 5'-diphospho-N-acetylglucosamine	528:567	uridine 5'-diphospho-N-acetylglucosamine (UDP-GlcNAc)	528:580	O-GlcNAc modification of proteins is dependent on the concentration of uridine 5'-diphospho-N-acetylglucosamine (UDP-GlcNAc), which is a substrate of OGT and is synthesized via the hexosamine biosynthetic pathway.
21526146	10	41	theme	glucose	1676:1682	arg1	deprivation					1684:1694	glucose deprivation	1676:1694	glucose deprivation	1676:1694	Our results demonstrated that N-GlcNAc(2)-modified glycoproteins were induced under glucose deprivation and that they cross-reacted with the O-GlcNAc-specific antibody CTD110.6.
21526146	9	42	theme	-modified	1453:1461	arg1	glycoproteins					1463:1475	N-GlcNAc(2)-modified glycoproteins	1442:1475	N-GlcNAc(2)-modified glycoproteins produced by a yeast strain with a ts-mutant of ALG1 that could not add a mannose residue to dolichol-PP-GlcNAc(2)	1442:1589	Furthermore, CTD110.6 antibodies reacted with N-GlcNAc(2)-modified glycoproteins produced by a yeast strain with a ts-mutant of ALG1 that could not add a mannose residue to dolichol-PP-GlcNAc(2).
21526146	12	43	theme	stress	2150:2155	arg1	conditions					2173:2182	stress and deprivation conditions	2150:2182	conditions	2173:2182	We also suggest that the repression of mature N-linked glycoproteins due to increased levels of N-GlcNAc(2)-modified proteins is a newly recognized pathway for effective use of sugar under stress and deprivation conditions.
21526146	6	44	dep	glycosylation	931:943	arg1	detected					980:987	detected	980:987	detected by CTD110.6 antibodies	980:1010	Here we show that the increased glycosylation induced by glucose deprivation and detected by CTD110.6 antibodies is actually modification by N-GlcNAc(2), rather than by O-GlcNAc.
21526146	6	44	dep	glycosylation	931:943	arg1	induced					945:951	induced	945:951	induced by glucose deprivation	945:974	Here we show that the increased glycosylation induced by glucose deprivation and detected by CTD110.6 antibodies is actually modification by N-GlcNAc(2), rather than by O-GlcNAc.
21526146	3	45	theme	5'-diphospho-N-acetylglucosamine	536:567	arg1	concentration					511:523	the concentration	507:523	the concentration	507:523	O-GlcNAc modification of proteins is dependent on the concentration of uridine 5'-diphospho-N-acetylglucosamine (UDP-GlcNAc), which is a substrate of OGT and is synthesized via the hexosamine biosynthetic pathway.
21526146	3	45	theme	5'-diphospho-N-acetylglucosamine	536:567	arg1	substrate					594:602	a substrate	592:602	a substrate of OGT	592:609	O-GlcNAc modification of proteins is dependent on the concentration of uridine 5'-diphospho-N-acetylglucosamine (UDP-GlcNAc), which is a substrate of OGT and is synthesized via the hexosamine biosynthetic pathway.
21526146	0	46	theme	N-GlcNAc2-modified	54:71	arg1	proteins					73:80	N-GlcNAc2-modified proteins	54:80	N-GlcNAc2-modified proteins induced under glucose deprivation	54:114	O-GlcNAc-specific antibody CTD110.6 cross-reacts with N-GlcNAc2-modified proteins induced under glucose deprivation.
21526146	5	47	theme	phenomenon	866:875	arg1	mechanism					836:844	The mechanism	832:844	The mechanism of this paradoxical phenomenon	832:875	The mechanism of this paradoxical phenomenon has remained unclear.
21526146	10	48	theme	O-GlcNAc-specific	1733:1749	arg1	antibody					1751:1758	the O-GlcNAc-specific antibody CTD110.6	1729:1767	the O-GlcNAc-specific antibody CTD110.6	1729:1767	Our results demonstrated that N-GlcNAc(2)-modified glycoproteins were induced under glucose deprivation and that they cross-reacted with the O-GlcNAc-specific antibody CTD110.6.
21526146	3	49	theme	proteins	482:489	arg1	modification					466:477	O-GlcNAc modification	457:477	O-GlcNAc modification of proteins	457:489	O-GlcNAc modification of proteins is dependent on the concentration of uridine 5'-diphospho-N-acetylglucosamine (UDP-GlcNAc), which is a substrate of OGT and is synthesized via the hexosamine biosynthetic pathway.
21526146	1	50	link	O-linked	178:185	arg1	glycosylation					220:232	O-linked β-N-acetylglucosamine (O-GlcNAc) glycosylation	178:232	O-linked β-N-acetylglucosamine (O-GlcNAc) glycosylation	178:232	Modification of serine and threonine residues in proteins by O-linked β-N-acetylglucosamine (O-GlcNAc) glycosylation is a feature of many cellular responses to the nutritional state and to stress.
21526146	11	51	theme	O-GlcNAc-modified	1858:1874	arg1	proteins					1876:1883	O-GlcNAc-modified proteins	1858:1883	O-GlcNAc-modified proteins according to their reactivity with CTD110.6 antibodies	1858:1938	We therefore propose that the glycosylation status of proteins previously classified as O-GlcNAc-modified proteins according to their reactivity with CTD110.6 antibodies must be re-examined.
21526146	1	52	theme	many	250:253	arg1	responses					264:272	many cellular responses	250:272	many cellular responses to the nutritional state and to stress	250:311	Modification of serine and threonine residues in proteins by O-linked β-N-acetylglucosamine (O-GlcNAc) glycosylation is a feature of many cellular responses to the nutritional state and to stress.
21526146	3	53	theme	O-GlcNAc	457:464	arg1	modification					466:477	O-GlcNAc modification	457:477	O-GlcNAc modification of proteins	457:489	O-GlcNAc modification of proteins is dependent on the concentration of uridine 5'-diphospho-N-acetylglucosamine (UDP-GlcNAc), which is a substrate of OGT and is synthesized via the hexosamine biosynthetic pathway.
21526146	11	54	theme	glycosylation	1800:1812	arg1	status					1814:1819	the glycosylation status	1796:1819	the glycosylation status of proteins previously classified as O-GlcNAc-modified proteins according to their reactivity with CTD110.6 antibodies	1796:1938	We therefore propose that the glycosylation status of proteins previously classified as O-GlcNAc-modified proteins according to their reactivity with CTD110.6 antibodies must be re-examined.
21526146	3	55	theme	biosynthetic	649:660	arg1	pathway					662:668	the hexosamine biosynthetic pathway	634:668	the hexosamine biosynthetic pathway	634:668	O-GlcNAc modification of proteins is dependent on the concentration of uridine 5'-diphospho-N-acetylglucosamine (UDP-GlcNAc), which is a substrate of OGT and is synthesized via the hexosamine biosynthetic pathway.
21526146	11	56	with	reactivity	1904:1913	arg1	antibodies					1929:1938	CTD110.6 antibodies	1920:1938	CTD110.6 antibodies	1920:1938	We therefore propose that the glycosylation status of proteins previously classified as O-GlcNAc-modified proteins according to their reactivity with CTD110.6 antibodies must be re-examined.
21526146	1	57	theme	threonine	144:152	arg1	feature					239:245	a feature	237:245	a feature of many cellular responses to the nutritional state and to stress	237:311	Modification of serine and threonine residues in proteins by O-linked β-N-acetylglucosamine (O-GlcNAc) glycosylation is a feature of many cellular responses to the nutritional state and to stress.
21526146	1	57	theme	threonine	144:152	arg1	Modification					117:128	Modification	117:128	Modification of serine and threonine residues in proteins by O-linked β-N-acetylglucosamine (O-GlcNAc) glycosylation	117:232	Modification of serine and threonine residues in proteins by O-linked β-N-acetylglucosamine (O-GlcNAc) glycosylation is a feature of many cellular responses to the nutritional state and to stress.
21526146	8	58	theme	induced	1333:1339	arg1	glycosylation					1341:1353	this induced glycosylation	1328:1353	this induced glycosylation	1328:1353	Proteomics analysis showed that proteins modified by this induced glycosylation were N-GlcNAc(2)-modified glycoproteins.
21526146	12	59	theme	N-linked	2007:2014	arg1	glycoproteins					2016:2028	mature N-linked glycoproteins	2000:2028	mature N-linked glycoproteins	2000:2028	We also suggest that the repression of mature N-linked glycoproteins due to increased levels of N-GlcNAc(2)-modified proteins is a newly recognized pathway for effective use of sugar under stress and deprivation conditions.
21526146	13	60	theme	physiological	2227:2239	arg1	roles					2258:2262	the physiological and pathological roles	2223:2262	the physiological and pathological roles of N-GlcNAc(2)-modified proteins	2223:2295	Further research is needed to clarify the physiological and pathological roles of N-GlcNAc(2)-modified proteins.
21526146	10	61	gly	glycoproteins	1643:1655	arg1	glycoproteins					1643:1655	N-GlcNAc(2)-modified glycoproteins	1622:1655	N-GlcNAc(2)-modified glycoproteins	1622:1655	Our results demonstrated that N-GlcNAc(2)-modified glycoproteins were induced under glucose deprivation and that they cross-reacted with the O-GlcNAc-specific antibody CTD110.6.
21526146	4	62	theme	cancer	818:823	arg1	cells					825:829	some cancer cells	813:829	some cancer cells	813:829	Immunoblot analysis using the O-GlcNAc-specific antibody CTD110.6 has indicated that glucose deprivation increases protein O-GlcNAcylation in some cancer cells.
21526146	1	63	from	serine	133:138	arg1	proteins					166:173	proteins	166:173	proteins	166:173	Modification of serine and threonine residues in proteins by O-linked β-N-acetylglucosamine (O-GlcNAc) glycosylation is a feature of many cellular responses to the nutritional state and to stress.
21526146	9	64	theme	yeast	1491:1495	arg1	strain					1497:1502	a yeast strain	1489:1502	a yeast strain with a ts-mutant of ALG1 that could not add a mannose residue to dolichol-PP-GlcNAc(2)	1489:1589	Furthermore, CTD110.6 antibodies reacted with N-GlcNAc(2)-modified glycoproteins produced by a yeast strain with a ts-mutant of ALG1 that could not add a mannose residue to dolichol-PP-GlcNAc(2).
21526146	6	65	theme	glucose	956:962	arg1	deprivation					964:974	glucose deprivation	956:974	glucose deprivation	956:974	Here we show that the increased glycosylation induced by glucose deprivation and detected by CTD110.6 antibodies is actually modification by N-GlcNAc(2), rather than by O-GlcNAc.
21526146	4	66	theme	protein	786:792	arg1	O-GlcNAcylation					794:808	protein O-GlcNAcylation	786:808	protein O-GlcNAcylation	786:808	Immunoblot analysis using the O-GlcNAc-specific antibody CTD110.6 has indicated that glucose deprivation increases protein O-GlcNAcylation in some cancer cells.
21526146	2	67	theme	β-N-acetylglucosamine	372:392	arg1	transferase					394:404	O-linked β-N-acetylglucosamine transferase	363:404	O-linked β-N-acetylglucosamine transferase (OGT)	363:410	O-GlcNAc modification is reversibly regulated by O-linked β-N-acetylglucosamine transferase (OGT) and β-D-N-acetylglucosaminase (O-GlcNAcase).
21526146	2	67	theme	β-N-acetylglucosamine	372:392	arg1	OGT					407:409	OGT	407:409	OGT	407:409	O-GlcNAc modification is reversibly regulated by O-linked β-N-acetylglucosamine transferase (OGT) and β-D-N-acetylglucosaminase (O-GlcNAcase).
21526146	1	68	theme	cellular	255:262	arg1	responses					264:272	many cellular responses	250:272	many cellular responses to the nutritional state and to stress	250:311	Modification of serine and threonine residues in proteins by O-linked β-N-acetylglucosamine (O-GlcNAc) glycosylation is a feature of many cellular responses to the nutritional state and to stress.
21526146	8	69	gly	glycoproteins	1381:1393	arg1	glycoproteins					1381:1393	N-GlcNAc(2)-modified glycoproteins	1360:1393	N-GlcNAc(2)-modified glycoproteins	1360:1393	Proteomics analysis showed that proteins modified by this induced glycosylation were N-GlcNAc(2)-modified glycoproteins.
21526146	2	70	theme	O-linked	363:370	arg1	transferase					394:404	O-linked β-N-acetylglucosamine transferase	363:404	O-linked β-N-acetylglucosamine transferase (OGT)	363:410	O-GlcNAc modification is reversibly regulated by O-linked β-N-acetylglucosamine transferase (OGT) and β-D-N-acetylglucosaminase (O-GlcNAcase).
21526146	2	70	theme	O-linked	363:370	arg1	OGT					407:409	OGT	407:409	OGT	407:409	O-GlcNAc modification is reversibly regulated by O-linked β-N-acetylglucosamine transferase (OGT) and β-D-N-acetylglucosaminase (O-GlcNAcase).
21526146	1	71	from	Modification	117:128	arg1	proteins					166:173	proteins	166:173	proteins	166:173	Modification of serine and threonine residues in proteins by O-linked β-N-acetylglucosamine (O-GlcNAc) glycosylation is a feature of many cellular responses to the nutritional state and to stress.
21526146	1	72	theme	responses	264:272	arg1	feature					239:245	a feature	237:245	a feature of many cellular responses to the nutritional state and to stress	237:311	Modification of serine and threonine residues in proteins by O-linked β-N-acetylglucosamine (O-GlcNAc) glycosylation is a feature of many cellular responses to the nutritional state and to stress.
21526146	1	72	theme	responses	264:272	arg1	Modification					117:128	Modification	117:128	Modification of serine and threonine residues in proteins by O-linked β-N-acetylglucosamine (O-GlcNAc) glycosylation	117:232	Modification of serine and threonine residues in proteins by O-linked β-N-acetylglucosamine (O-GlcNAc) glycosylation is a feature of many cellular responses to the nutritional state and to stress.
21526146	0	73	theme	glucose	96:102	arg1	deprivation					104:114	glucose deprivation	96:114	glucose deprivation	96:114	O-GlcNAc-specific antibody CTD110.6 cross-reacts with N-GlcNAc2-modified proteins induced under glucose deprivation.
21526146	13	74	theme	pathological	2245:2256	arg1	roles					2258:2262	the physiological and pathological roles	2223:2262	the physiological and pathological roles of N-GlcNAc(2)-modified proteins	2223:2295	Further research is needed to clarify the physiological and pathological roles of N-GlcNAc(2)-modified proteins.
21526146	7	75	theme	induced	1097:1103	arg1	glycosylation					1105:1117	this induced glycosylation	1092:1117	this induced glycosylation	1092:1117	We found that this induced glycosylation was not regulated by OGT and O-GlcNAcase, unlike typical O-GlcNAcylation, and it was inhibited by treatment with tunicamycin, an N-glycosylation inhibitor.
21526146	1	76	dep	serine	133:138	arg1	residues					154:161	residues	154:161	residues	154:161	Modification of serine and threonine residues in proteins by O-linked β-N-acetylglucosamine (O-GlcNAc) glycosylation is a feature of many cellular responses to the nutritional state and to stress.
21526146	4	77	theme	O-GlcNAc-specific	701:717	arg1	antibody					719:726	the O-GlcNAc-specific antibody CTD110.6	697:735	the O-GlcNAc-specific antibody CTD110.6	697:735	Immunoblot analysis using the O-GlcNAc-specific antibody CTD110.6 has indicated that glucose deprivation increases protein O-GlcNAcylation in some cancer cells.
21526146	13	78	theme	-modified	2278:2286	arg1	proteins					2288:2295	N-GlcNAc(2)-modified proteins	2267:2295	N-GlcNAc(2)-modified proteins	2267:2295	Further research is needed to clarify the physiological and pathological roles of N-GlcNAc(2)-modified proteins.
21526146	9	79	with	strain	1497:1502	arg1	ts-mutant					1511:1519	a ts-mutant	1509:1519	a ts-mutant of ALG1 that could not add a mannose residue to dolichol-PP-GlcNAc(2)	1509:1589	Furthermore, CTD110.6 antibodies reacted with N-GlcNAc(2)-modified glycoproteins produced by a yeast strain with a ts-mutant of ALG1 that could not add a mannose residue to dolichol-PP-GlcNAc(2).
21526146	1	80	theme	O-linked	178:185	arg1	glycosylation					220:232	O-linked β-N-acetylglucosamine (O-GlcNAc) glycosylation	178:232	O-linked β-N-acetylglucosamine (O-GlcNAc) glycosylation	178:232	Modification of serine and threonine residues in proteins by O-linked β-N-acetylglucosamine (O-GlcNAc) glycosylation is a feature of many cellular responses to the nutritional state and to stress.
21526146	12	81	theme	effective	2121:2129	arg1	use					2131:2133	effective use	2121:2133	effective use of sugar	2121:2142	We also suggest that the repression of mature N-linked glycoproteins due to increased levels of N-GlcNAc(2)-modified proteins is a newly recognized pathway for effective use of sugar under stress and deprivation conditions.
24141704	0	0	theme	Gq	78:79	arg1	deamidation					63:73	deamidation	63:73	deamidation	63:73	A bacterial toxin catalyzing tyrosine glycosylation of Rho and deamidation of Gq and Gi proteins.
24141704	0	0	theme	Gq	78:79	arg1	Rho					55:57	Rho	55:57	Rho	55:57	A bacterial toxin catalyzing tyrosine glycosylation of Rho and deamidation of Gq and Gi proteins.
24141704	5	1	theme	smallest	779:786	arg1	toxin					808:812	the smallest glycosyltransferase toxin	775:812	the smallest glycosyltransferase toxin known	775:818	The crystal structure of the PaTox glycosyltransferase domain in complex with UDP-GlcNAc determined at 1.8-Å resolution represents a canonical GT-A fold and is the smallest glycosyltransferase toxin known.
24141704	5	2	theme	glycosyltransferase	650:668	arg1	domain					670:675	the PaTox glycosyltransferase domain	640:675	the PaTox glycosyltransferase domain in complex with UDP-GlcNAc	640:702	The crystal structure of the PaTox glycosyltransferase domain in complex with UDP-GlcNAc determined at 1.8-Å resolution represents a canonical GT-A fold and is the smallest glycosyltransferase toxin known.
24141704	4	3	with	interaction	468:478	arg1	effectors					496:504	downstream effectors	485:504	downstream effectors	485:504	Tyrosine glycosylation inhibits Rho activation and prevents interaction with downstream effectors, resulting in actin disassembly, inhibition of phagocytosis and toxicity toward insects and mammalian cells.
24141704	7	4	theme	PaTox	926:930	arg1	PaTox					926:930	PaTox	926:930	PaTox	926:930	The glutamine-deamidase domain of PaTox blocks GTP hydrolysis of heterotrimeric Gαq/11 and Gαi proteins, thereby activating RhoA.
24141704	7	4	theme	PaTox	926:930	arg1	domain					916:921	The glutamine-deamidase domain	892:921	The glutamine-deamidase domain of PaTox	892:930	The glutamine-deamidase domain of PaTox blocks GTP hydrolysis of heterotrimeric Gαq/11 and Gαi proteins, thereby activating RhoA.
24141704	5	5	theme	glycosyltransferase	788:806	arg1	toxin					808:812	the smallest glycosyltransferase toxin	775:812	the smallest glycosyltransferase toxin known	775:818	The crystal structure of the PaTox glycosyltransferase domain in complex with UDP-GlcNAc determined at 1.8-Å resolution represents a canonical GT-A fold and is the smallest glycosyltransferase toxin known.
24141704	5	6	theme	domain	670:675	arg1	structure					627:635	The crystal structure	615:635	The crystal structure of the PaTox glycosyltransferase domain in complex with UDP-GlcNAc determined at 1.8-Å resolution	615:733	The crystal structure of the PaTox glycosyltransferase domain in complex with UDP-GlcNAc determined at 1.8-Å resolution represents a canonical GT-A fold and is the smallest glycosyltransferase toxin known.
24141704	1	7	from	pathogen	155:162	arg1	humans					167:172	humans	167:172	humans	167:172	Entomopathogenic Photorhabdus asymbiotica is an emerging pathogen in humans.
24141704	7	8	theme	glutamine-deamidase	896:914	arg1	PaTox					926:930	PaTox	926:930	PaTox	926:930	The glutamine-deamidase domain of PaTox blocks GTP hydrolysis of heterotrimeric Gαq/11 and Gαi proteins, thereby activating RhoA.
24141704	7	8	theme	glutamine-deamidase	896:914	arg1	domain					916:921	The glutamine-deamidase domain	892:921	The glutamine-deamidase domain of PaTox	892:930	The glutamine-deamidase domain of PaTox blocks GTP hydrolysis of heterotrimeric Gαq/11 and Gαi proteins, thereby activating RhoA.
24141704	0	9	theme	Gi	85:86	arg1	deamidation					63:73	deamidation	63:73	deamidation	63:73	A bacterial toxin catalyzing tyrosine glycosylation of Rho and deamidation of Gq and Gi proteins.
24141704	0	9	theme	Gi	85:86	arg1	Rho					55:57	Rho	55:57	Rho	55:57	A bacterial toxin catalyzing tyrosine glycosylation of Rho and deamidation of Gq and Gi proteins.
24141704	7	10	theme	Gαi	983:985	arg1	proteins					987:994	heterotrimeric Gαq/11 and Gαi proteins	957:994	heterotrimeric Gαq/11 and Gαi proteins	957:994	The glutamine-deamidase domain of PaTox blocks GTP hydrolysis of heterotrimeric Gαq/11 and Gαi proteins, thereby activating RhoA.
24141704	8	11	theme	bidirectional	1069:1081	arg1	manner					1083:1088	a bidirectional manner	1067:1088	a bidirectional manner	1067:1088	Thus, PaTox hijacks host GTPase signaling in a bidirectional manner by deamidation-induced activation and glycosylation-induced inactivation of GTPases.
24141704	6	12	theme	H-NMR	824:828	arg1	analysis					830:837	H-NMR analysis	824:837	H-NMR analysis	824:837	(1)H-NMR analysis identifies PaTox as a retaining glycosyltransferase.
24141704	4	13	theme	mammalian	598:606	arg1	cells					608:612	mammalian cells	598:612	mammalian cells	598:612	Tyrosine glycosylation inhibits Rho activation and prevents interaction with downstream effectors, resulting in actin disassembly, inhibition of phagocytosis and toxicity toward insects and mammalian cells.
24141704	5	14	theme	GT-A	758:761	arg1	fold					763:766	a canonical GT-A fold	746:766	a canonical GT-A fold	746:766	The crystal structure of the PaTox glycosyltransferase domain in complex with UDP-GlcNAc determined at 1.8-Å resolution represents a canonical GT-A fold and is the smallest glycosyltransferase toxin known.
24141704	7	15	theme	proteins	987:994	arg1	hydrolysis					943:952	GTP hydrolysis	939:952	GTP hydrolysis of heterotrimeric Gαq/11 and Gαi proteins	939:994	The glutamine-deamidase domain of PaTox blocks GTP hydrolysis of heterotrimeric Gαq/11 and Gαi proteins, thereby activating RhoA.
24141704	5	16	with	complex	680:686	arg1	UDP-GlcNAc					693:702	UDP-GlcNAc	693:702	UDP-GlcNAc	693:702	The crystal structure of the PaTox glycosyltransferase domain in complex with UDP-GlcNAc determined at 1.8-Å resolution represents a canonical GT-A fold and is the smallest glycosyltransferase toxin known.
24141704	5	17	theme	crystal	619:625	arg1	structure					627:635	The crystal structure	615:635	The crystal structure of the PaTox glycosyltransferase domain in complex with UDP-GlcNAc determined at 1.8-Å resolution	615:733	The crystal structure of the PaTox glycosyltransferase domain in complex with UDP-GlcNAc determined at 1.8-Å resolution represents a canonical GT-A fold and is the smallest glycosyltransferase toxin known.
24141704	4	18	theme	downstream	485:494	arg1	effectors					496:504	downstream effectors	485:504	downstream effectors	485:504	Tyrosine glycosylation inhibits Rho activation and prevents interaction with downstream effectors, resulting in actin disassembly, inhibition of phagocytosis and toxicity toward insects and mammalian cells.
24141704	3	19	theme	GTPases	353:359	arg1	Y32					322:324	Y32	322:324	Y32	322:324	PaTox mono-O-glycosylates Y32 (or Y34) of eukaryotic Rho GTPases by using UDP-N-acetylglucosamine (UDP-GlcNAc).
24141704	3	19	theme	GTPases	353:359	arg1	Y34					330:332	Y34	330:332	Y34	330:332	PaTox mono-O-glycosylates Y32 (or Y34) of eukaryotic Rho GTPases by using UDP-N-acetylglucosamine (UDP-GlcNAc).
24141704	4	20	theme	phagocytosis	553:564	arg1	inhibition					539:548	inhibition	539:548	inhibition of phagocytosis	539:564	Tyrosine glycosylation inhibits Rho activation and prevents interaction with downstream effectors, resulting in actin disassembly, inhibition of phagocytosis and toxicity toward insects and mammalian cells.
24141704	4	20	theme	phagocytosis	553:564	arg1	disassembly					526:536	actin disassembly	520:536	actin disassembly	520:536	Tyrosine glycosylation inhibits Rho activation and prevents interaction with downstream effectors, resulting in actin disassembly, inhibition of phagocytosis and toxicity toward insects and mammalian cells.
24141704	4	20	theme	phagocytosis	553:564	arg1	toxicity					570:577	toxicity	570:577	toxicity toward insects and mammalian cells	570:612	Tyrosine glycosylation inhibits Rho activation and prevents interaction with downstream effectors, resulting in actin disassembly, inhibition of phagocytosis and toxicity toward insects and mammalian cells.
24141704	0	21	dep	Gq	78:79	arg1	proteins					88:95	proteins	88:95	proteins	88:95	A bacterial toxin catalyzing tyrosine glycosylation of Rho and deamidation of Gq and Gi proteins.
24141704	8	22	theme	glycosylation-induced	1128:1148	arg1	inactivation					1150:1161	glycosylation-induced inactivation	1128:1161	glycosylation-induced inactivation	1128:1161	Thus, PaTox hijacks host GTPase signaling in a bidirectional manner by deamidation-induced activation and glycosylation-induced inactivation of GTPases.
24141704	2	23	contain	contains	241:248	arg1	toxin					220:224	a P. asymbiotica protein toxin	195:224	a P. asymbiotica protein toxin (PaTox)	195:232	Here, we identified a P. asymbiotica protein toxin (PaTox), which contains a glycosyltransferase and a deamidase domain.
24141704	2	23	contain	contains	241:248	arg2	domain					288:293	a deamidase domain	276:293	a deamidase domain	276:293	Here, we identified a P. asymbiotica protein toxin (PaTox), which contains a glycosyltransferase and a deamidase domain.
24141704	2	23	contain	contains	241:248	arg1	PaTox					227:231	PaTox	227:231	PaTox	227:231	Here, we identified a P. asymbiotica protein toxin (PaTox), which contains a glycosyltransferase and a deamidase domain.
24141704	2	23	contain	contains	241:248	arg2	glycosyltransferase					252:270	a glycosyltransferase	250:270	a glycosyltransferase	250:270	Here, we identified a P. asymbiotica protein toxin (PaTox), which contains a glycosyltransferase and a deamidase domain.
24141704	5	24	theme	PaTox	644:648	arg1	domain					670:675	the PaTox glycosyltransferase domain	640:675	the PaTox glycosyltransferase domain in complex with UDP-GlcNAc	640:702	The crystal structure of the PaTox glycosyltransferase domain in complex with UDP-GlcNAc determined at 1.8-Å resolution represents a canonical GT-A fold and is the smallest glycosyltransferase toxin known.
24141704	7	25	theme	heterotrimeric	957:970	arg1	proteins					987:994	heterotrimeric Gαq/11 and Gαi proteins	957:994	heterotrimeric Gαq/11 and Gαi proteins	957:994	The glutamine-deamidase domain of PaTox blocks GTP hydrolysis of heterotrimeric Gαq/11 and Gαi proteins, thereby activating RhoA.
24141704	5	26	theme	canonical	748:756	arg1	fold					763:766	a canonical GT-A fold	746:766	a canonical GT-A fold	746:766	The crystal structure of the PaTox glycosyltransferase domain in complex with UDP-GlcNAc determined at 1.8-Å resolution represents a canonical GT-A fold and is the smallest glycosyltransferase toxin known.
24141704	8	27	theme	GTPase	1047:1052	arg1	signaling					1054:1062	host GTPase signaling	1042:1062	host GTPase signaling	1042:1062	Thus, PaTox hijacks host GTPase signaling in a bidirectional manner by deamidation-induced activation and glycosylation-induced inactivation of GTPases.
24141704	3	28	theme	eukaryotic	338:347	arg1	GTPases					353:359	eukaryotic Rho GTPases	338:359	eukaryotic Rho GTPases	338:359	PaTox mono-O-glycosylates Y32 (or Y34) of eukaryotic Rho GTPases by using UDP-N-acetylglucosamine (UDP-GlcNAc).
24141704	6	29	dep	identifies	839:848	arg1	1					822:822	1	822:822	1	822:822	(1)H-NMR analysis identifies PaTox as a retaining glycosyltransferase.
24141704	5	30	theme	1.8-Å	718:722	arg1	resolution					724:733	1.8-Å resolution	718:733	1.8-Å resolution	718:733	The crystal structure of the PaTox glycosyltransferase domain in complex with UDP-GlcNAc determined at 1.8-Å resolution represents a canonical GT-A fold and is the smallest glycosyltransferase toxin known.
24141704	7	31	theme	Gαq/11	972:977	arg1	proteins					987:994	heterotrimeric Gαq/11 and Gαi proteins	957:994	heterotrimeric Gαq/11 and Gαi proteins	957:994	The glutamine-deamidase domain of PaTox blocks GTP hydrolysis of heterotrimeric Gαq/11 and Gαi proteins, thereby activating RhoA.
24141704	2	32	theme	deamidase	278:286	arg1	domain					288:293	a deamidase domain	276:293	a deamidase domain	276:293	Here, we identified a P. asymbiotica protein toxin (PaTox), which contains a glycosyltransferase and a deamidase domain.
24141704	3	33	theme	Rho	349:351	arg1	GTPases					353:359	eukaryotic Rho GTPases	338:359	eukaryotic Rho GTPases	338:359	PaTox mono-O-glycosylates Y32 (or Y34) of eukaryotic Rho GTPases by using UDP-N-acetylglucosamine (UDP-GlcNAc).
24141704	5	34	from	structure	627:635	arg1	complex					680:686	complex	680:686	complex with UDP-GlcNAc	680:702	The crystal structure of the PaTox glycosyltransferase domain in complex with UDP-GlcNAc determined at 1.8-Å resolution represents a canonical GT-A fold and is the smallest glycosyltransferase toxin known.
24141704	4	35	theme	Rho	440:442	arg1	activation					444:453	Rho activation	440:453	Rho activation	440:453	Tyrosine glycosylation inhibits Rho activation and prevents interaction with downstream effectors, resulting in actin disassembly, inhibition of phagocytosis and toxicity toward insects and mammalian cells.
24141704	0	36	theme	tyrosine	29:36	arg1	glycosylation					38:50	tyrosine glycosylation	29:50	tyrosine glycosylation of Rho and deamidation of Gq and Gi proteins	29:95	A bacterial toxin catalyzing tyrosine glycosylation of Rho and deamidation of Gq and Gi proteins.
24141704	8	37	theme	host	1042:1045	arg1	signaling					1054:1062	host GTPase signaling	1042:1062	host GTPase signaling	1042:1062	Thus, PaTox hijacks host GTPase signaling in a bidirectional manner by deamidation-induced activation and glycosylation-induced inactivation of GTPases.
24141704	0	38	theme	Rho	55:57	arg1	glycosylation					38:50	tyrosine glycosylation	29:50	tyrosine glycosylation of Rho and deamidation of Gq and Gi proteins	29:95	A bacterial toxin catalyzing tyrosine glycosylation of Rho and deamidation of Gq and Gi proteins.
24141704	4	39	theme	actin	520:524	arg1	disassembly					526:536	actin disassembly	520:536	actin disassembly	520:536	Tyrosine glycosylation inhibits Rho activation and prevents interaction with downstream effectors, resulting in actin disassembly, inhibition of phagocytosis and toxicity toward insects and mammalian cells.
24141704	6	40	theme	retaining	861:869	arg1	glycosyltransferase					871:889	a retaining glycosyltransferase	859:889	a retaining glycosyltransferase	859:889	(1)H-NMR analysis identifies PaTox as a retaining glycosyltransferase.
24141704	6	40	theme	retaining	861:869	arg1	PaTox					850:854	PaTox	850:854	PaTox	850:854	(1)H-NMR analysis identifies PaTox as a retaining glycosyltransferase.
24141704	2	41	theme	protein	212:218	arg1	toxin					220:224	a P. asymbiotica protein toxin	195:224	a P. asymbiotica protein toxin (PaTox)	195:232	Here, we identified a P. asymbiotica protein toxin (PaTox), which contains a glycosyltransferase and a deamidase domain.
24141704	2	41	theme	protein	212:218	arg1	PaTox					227:231	PaTox	227:231	PaTox	227:231	Here, we identified a P. asymbiotica protein toxin (PaTox), which contains a glycosyltransferase and a deamidase domain.
24141704	1	42	theme	Entomopathogenic	98:113	arg1	asymbiotica					128:138	Entomopathogenic Photorhabdus asymbiotica	98:138	Entomopathogenic Photorhabdus asymbiotica	98:138	Entomopathogenic Photorhabdus asymbiotica is an emerging pathogen in humans.
24141704	1	42	theme	Entomopathogenic	98:113	arg1	pathogen					155:162	an emerging pathogen	143:162	an emerging pathogen in humans	143:172	Entomopathogenic Photorhabdus asymbiotica is an emerging pathogen in humans.
24141704	8	43	theme	GTPases	1166:1172	arg1	inactivation					1150:1161	glycosylation-induced inactivation	1128:1161	glycosylation-induced inactivation	1128:1161	Thus, PaTox hijacks host GTPase signaling in a bidirectional manner by deamidation-induced activation and glycosylation-induced inactivation of GTPases.
24141704	8	43	theme	GTPases	1166:1172	arg1	activation					1113:1122	deamidation-induced activation	1093:1122	deamidation-induced activation	1093:1122	Thus, PaTox hijacks host GTPase signaling in a bidirectional manner by deamidation-induced activation and glycosylation-induced inactivation of GTPases.
24141704	2	44	theme	P.	197:198	arg1	toxin					220:224	a P. asymbiotica protein toxin	195:224	a P. asymbiotica protein toxin (PaTox)	195:232	Here, we identified a P. asymbiotica protein toxin (PaTox), which contains a glycosyltransferase and a deamidase domain.
24141704	2	44	theme	P.	197:198	arg1	PaTox					227:231	PaTox	227:231	PaTox	227:231	Here, we identified a P. asymbiotica protein toxin (PaTox), which contains a glycosyltransferase and a deamidase domain.
24141704	1	45	theme	Photorhabdus	115:126	arg1	asymbiotica					128:138	Entomopathogenic Photorhabdus asymbiotica	98:138	Entomopathogenic Photorhabdus asymbiotica	98:138	Entomopathogenic Photorhabdus asymbiotica is an emerging pathogen in humans.
24141704	1	45	theme	Photorhabdus	115:126	arg1	pathogen					155:162	an emerging pathogen	143:162	an emerging pathogen in humans	143:172	Entomopathogenic Photorhabdus asymbiotica is an emerging pathogen in humans.
24141704	5	46	from	domain	670:675	arg1	complex					680:686	complex	680:686	complex with UDP-GlcNAc	680:702	The crystal structure of the PaTox glycosyltransferase domain in complex with UDP-GlcNAc determined at 1.8-Å resolution represents a canonical GT-A fold and is the smallest glycosyltransferase toxin known.
24141704	3	47	gly	mono-O-glycosylates	302:320	arg1	Y32					322:324	Y32	322:324	Y32	322:324	PaTox mono-O-glycosylates Y32 (or Y34) of eukaryotic Rho GTPases by using UDP-N-acetylglucosamine (UDP-GlcNAc).
24141704	3	47	gly	mono-O-glycosylates	302:320	arg1	Y34					330:332	Y34	330:332	Y34	330:332	PaTox mono-O-glycosylates Y32 (or Y34) of eukaryotic Rho GTPases by using UDP-N-acetylglucosamine (UDP-GlcNAc).
24141704	0	48	gly	glycosylation	38:50	arg1	deamidation					63:73	deamidation	63:73	deamidation	63:73	A bacterial toxin catalyzing tyrosine glycosylation of Rho and deamidation of Gq and Gi proteins.
24141704	0	48	gly	glycosylation	38:50	arg1	Rho					55:57	Rho	55:57	Rho	55:57	A bacterial toxin catalyzing tyrosine glycosylation of Rho and deamidation of Gq and Gi proteins.
24141704	1	49	theme	emerging	146:153	arg1	asymbiotica					128:138	Entomopathogenic Photorhabdus asymbiotica	98:138	Entomopathogenic Photorhabdus asymbiotica	98:138	Entomopathogenic Photorhabdus asymbiotica is an emerging pathogen in humans.
24141704	1	49	theme	emerging	146:153	arg1	pathogen					155:162	an emerging pathogen	143:162	an emerging pathogen in humans	143:172	Entomopathogenic Photorhabdus asymbiotica is an emerging pathogen in humans.
24141704	8	50	theme	deamidation-induced	1093:1111	arg1	activation					1113:1122	deamidation-induced activation	1093:1122	deamidation-induced activation	1093:1122	Thus, PaTox hijacks host GTPase signaling in a bidirectional manner by deamidation-induced activation and glycosylation-induced inactivation of GTPases.
24141704	0	51	theme	deamidation	63:73	arg1	glycosylation					38:50	tyrosine glycosylation	29:50	tyrosine glycosylation of Rho and deamidation of Gq and Gi proteins	29:95	A bacterial toxin catalyzing tyrosine glycosylation of Rho and deamidation of Gq and Gi proteins.
24141704	4	52	theme	Tyrosine	408:415	arg1	glycosylation					417:429	Tyrosine glycosylation	408:429	Tyrosine glycosylation	408:429	Tyrosine glycosylation inhibits Rho activation and prevents interaction with downstream effectors, resulting in actin disassembly, inhibition of phagocytosis and toxicity toward insects and mammalian cells.
24141704	7	53	theme	GTP	939:941	arg1	hydrolysis					943:952	GTP hydrolysis	939:952	GTP hydrolysis of heterotrimeric Gαq/11 and Gαi proteins	939:994	The glutamine-deamidase domain of PaTox blocks GTP hydrolysis of heterotrimeric Gαq/11 and Gαi proteins, thereby activating RhoA.
24141704	2	54	dep	P.	197:198	arg1	asymbiotica					200:210	asymbiotica	200:210	asymbiotica	200:210	Here, we identified a P. asymbiotica protein toxin (PaTox), which contains a glycosyltransferase and a deamidase domain.
24141704	0	55	theme	bacterial	2:10	arg1	toxin					12:16	A bacterial toxin	0:16	A bacterial toxin	0:16	A bacterial toxin catalyzing tyrosine glycosylation of Rho and deamidation of Gq and Gi proteins.
24141704	5	56	from	complex	680:686	arg1	structure					627:635	The crystal structure	615:635	The crystal structure of the PaTox glycosyltransferase domain in complex with UDP-GlcNAc determined at 1.8-Å resolution	615:733	The crystal structure of the PaTox glycosyltransferase domain in complex with UDP-GlcNAc determined at 1.8-Å resolution represents a canonical GT-A fold and is the smallest glycosyltransferase toxin known.
36796536	6	0	theme	Ezrin	814:818	arg1	O-GlcNAcylation					820:834	Ezrin O-GlcNAcylation	814:834	Ezrin O-GlcNAcylation	814:834	Our data further show that Ezrin O-GlcNAcylation promotes its localization to the cell cortex, thereby stimulating the membrane-cytoskeleton interaction needed for efficient phagocytosis.
36796536	1	1	theme	nutrient	170:177	arg1	modification					131:142	a post-translational modification	110:142	a post-translational modification that serves as a cellular nutrient sensor and participates in multiple physiological and pathological processes	110:254	O-GlcNAcylation is a post-translational modification that serves as a cellular nutrient sensor and participates in multiple physiological and pathological processes.
36796536	1	1	theme	nutrient	170:177	arg1	sensor					179:184	a cellular nutrient sensor	159:184	a cellular nutrient sensor	159:184	O-GlcNAcylation is a post-translational modification that serves as a cellular nutrient sensor and participates in multiple physiological and pathological processes.
36796536	6	2	theme	efficient	951:959	arg1	phagocytosis					961:972	efficient phagocytosis	951:972	efficient phagocytosis	951:972	Our data further show that Ezrin O-GlcNAcylation promotes its localization to the cell cortex, thereby stimulating the membrane-cytoskeleton interaction needed for efficient phagocytosis.
36796536	7	3	theme	unrecognized	1012:1023	arg1	role					1025:1028	a previously unrecognized role	999:1028	a previously unrecognized role for protein O-GlcNAcylation in phagocytosis with important implications in both health and diseases	999:1128	These findings identify a previously unrecognized role for protein O-GlcNAcylation in phagocytosis with important implications in both health and diseases.
36796536	6	4	theme	membrane-cytoskeleton	906:926	arg1	interaction					928:938	the membrane-cytoskeleton interaction	902:938	the membrane-cytoskeleton interaction needed for efficient phagocytosis	902:972	Our data further show that Ezrin O-GlcNAcylation promotes its localization to the cell cortex, thereby stimulating the membrane-cytoskeleton interaction needed for efficient phagocytosis.
36796536	4	5	theme	O-GlcNAcylation	526:540	arg1	transferase					481:491	O-GlcNAc transferase	472:491	O-GlcNAc transferase	472:491	Knockout of O-GlcNAc transferase or pharmacological inhibition of O-GlcNAcylation dramatically blocks phagocytosis, resulting in the disruption of retinal structure and function.
36796536	4	5	theme	O-GlcNAcylation	526:540	arg1	inhibition					512:521	pharmacological inhibition	496:521	pharmacological inhibition of O-GlcNAcylation	496:540	Knockout of O-GlcNAc transferase or pharmacological inhibition of O-GlcNAcylation dramatically blocks phagocytosis, resulting in the disruption of retinal structure and function.
36796536	7	6	from	role	1025:1028	arg1	phagocytosis					1061:1072	phagocytosis	1061:1072	phagocytosis with important implications in both health and diseases	1061:1128	These findings identify a previously unrecognized role for protein O-GlcNAcylation in phagocytosis with important implications in both health and diseases.
36796536	3	7	theme	rapid	381:385	arg1	increase					387:394	a rapid increase	379:394	a rapid increase in protein O-GlcNAcylation in response to phagocytotic stimuli	379:457	Here, we demonstrate a rapid increase in protein O-GlcNAcylation in response to phagocytotic stimuli.
36796536	7	8	with	phagocytosis	1061:1072	arg1	implications					1089:1100	important implications	1079:1100	important implications in both health and diseases	1079:1128	These findings identify a previously unrecognized role for protein O-GlcNAcylation in phagocytosis with important implications in both health and diseases.
36796536	5	9	theme	membrane-cytoskeleton	716:736	arg1	protein					745:751	a membrane-cytoskeleton linker protein	714:751	a membrane-cytoskeleton linker protein	714:751	Mechanistic studies reveal that O-GlcNAc transferase interacts with Ezrin, a membrane-cytoskeleton linker protein, to catalyze its O-GlcNAcylation.
36796536	5	9	theme	membrane-cytoskeleton	716:736	arg1	Ezrin					707:711	Ezrin	707:711	Ezrin	707:711	Mechanistic studies reveal that O-GlcNAc transferase interacts with Ezrin, a membrane-cytoskeleton linker protein, to catalyze its O-GlcNAcylation.
36796536	7	10	theme	important	1079:1087	arg1	implications					1089:1100	important implications	1079:1100	important implications in both health and diseases	1079:1128	These findings identify a previously unrecognized role for protein O-GlcNAcylation in phagocytosis with important implications in both health and diseases.
36796536	2	11	gly	O-GlcNAcylation	295:309	arg1	regulation					330:339	the regulation	326:339	the regulation of phagocytosis	326:355	However, it remains uncertain whether O-GlcNAcylation is involved in the regulation of phagocytosis.
36796536	4	12	theme	function	629:636	arg1	disruption					593:602	the disruption	589:602	the disruption of retinal structure and function	589:636	Knockout of O-GlcNAc transferase or pharmacological inhibition of O-GlcNAcylation dramatically blocks phagocytosis, resulting in the disruption of retinal structure and function.
36796536	5	13	theme	linker	738:743	arg1	protein					745:751	a membrane-cytoskeleton linker protein	714:751	a membrane-cytoskeleton linker protein	714:751	Mechanistic studies reveal that O-GlcNAc transferase interacts with Ezrin, a membrane-cytoskeleton linker protein, to catalyze its O-GlcNAcylation.
36796536	5	13	theme	linker	738:743	arg1	Ezrin					707:711	Ezrin	707:711	Ezrin	707:711	Mechanistic studies reveal that O-GlcNAc transferase interacts with Ezrin, a membrane-cytoskeleton linker protein, to catalyze its O-GlcNAcylation.
36796536	2	14	theme	phagocytosis	344:355	arg1	regulation					330:339	the regulation	326:339	the regulation of phagocytosis	326:355	However, it remains uncertain whether O-GlcNAcylation is involved in the regulation of phagocytosis.
36796536	1	15	theme	multiple	206:213	arg1	processes					246:254	multiple physiological and pathological processes	206:254	multiple physiological and pathological processes	206:254	O-GlcNAcylation is a post-translational modification that serves as a cellular nutrient sensor and participates in multiple physiological and pathological processes.
36796536	3	16	theme	protein	399:405	arg1	O-GlcNAcylation					407:421	protein O-GlcNAcylation	399:421	protein O-GlcNAcylation	399:421	Here, we demonstrate a rapid increase in protein O-GlcNAcylation in response to phagocytotic stimuli.
36796536	5	17	theme	O-GlcNAc	671:678	arg1	transferase					680:690	O-GlcNAc transferase	671:690	O-GlcNAc transferase	671:690	Mechanistic studies reveal that O-GlcNAc transferase interacts with Ezrin, a membrane-cytoskeleton linker protein, to catalyze its O-GlcNAcylation.
36796536	1	18	theme	physiological	215:227	arg1	processes					246:254	multiple physiological and pathological processes	206:254	multiple physiological and pathological processes	206:254	O-GlcNAcylation is a post-translational modification that serves as a cellular nutrient sensor and participates in multiple physiological and pathological processes.
36796536	4	19	theme	pharmacological	496:510	arg1	inhibition					512:521	pharmacological inhibition	496:521	pharmacological inhibition of O-GlcNAcylation	496:540	Knockout of O-GlcNAc transferase or pharmacological inhibition of O-GlcNAcylation dramatically blocks phagocytosis, resulting in the disruption of retinal structure and function.
36796536	1	20	theme	post-translational	112:129	arg1	modification					131:142	a post-translational modification	110:142	a post-translational modification that serves as a cellular nutrient sensor and participates in multiple physiological and pathological processes	110:254	O-GlcNAcylation is a post-translational modification that serves as a cellular nutrient sensor and participates in multiple physiological and pathological processes.
36796536	1	20	theme	post-translational	112:129	arg1	O-GlcNAcylation					91:105	O-GlcNAcylation	91:105	O-GlcNAcylation	91:105	O-GlcNAcylation is a post-translational modification that serves as a cellular nutrient sensor and participates in multiple physiological and pathological processes.
36796536	1	20	theme	post-translational	112:129	arg1	sensor					179:184	a cellular nutrient sensor	159:184	a cellular nutrient sensor	159:184	O-GlcNAcylation is a post-translational modification that serves as a cellular nutrient sensor and participates in multiple physiological and pathological processes.
36796536	0	21	theme	Ezrin	52:56	arg1	localization					58:69	Ezrin localization	52:69	Ezrin localization	52:69	O-GlcNAcylation regulates phagocytosis by promoting Ezrin localization at the cell cortex.
36796536	1	22	theme	pathological	233:244	arg1	processes					246:254	multiple physiological and pathological processes	206:254	multiple physiological and pathological processes	206:254	O-GlcNAcylation is a post-translational modification that serves as a cellular nutrient sensor and participates in multiple physiological and pathological processes.
36796536	3	23	from	increase	387:394	arg1	response					426:433	response	426:433	response to phagocytotic stimuli	426:457	Here, we demonstrate a rapid increase in protein O-GlcNAcylation in response to phagocytotic stimuli.
36796536	3	23	from	increase	387:394	arg1	O-GlcNAcylation					407:421	protein O-GlcNAcylation	399:421	protein O-GlcNAcylation	399:421	Here, we demonstrate a rapid increase in protein O-GlcNAcylation in response to phagocytotic stimuli.
36796536	6	24	theme	cell	869:872	arg1	cortex					874:879	the cell cortex	865:879	the cell cortex	865:879	Our data further show that Ezrin O-GlcNAcylation promotes its localization to the cell cortex, thereby stimulating the membrane-cytoskeleton interaction needed for efficient phagocytosis.
36796536	4	25	theme	inhibition	512:521	arg1	Knockout					460:467	Knockout	460:467	Knockout	460:467	Knockout of O-GlcNAc transferase or pharmacological inhibition of O-GlcNAcylation dramatically blocks phagocytosis, resulting in the disruption of retinal structure and function.
36796536	3	26	theme	phagocytotic	438:449	arg1	stimuli					451:457	phagocytotic stimuli	438:457	phagocytotic stimuli	438:457	Here, we demonstrate a rapid increase in protein O-GlcNAcylation in response to phagocytotic stimuli.
36796536	4	27	theme	structure	615:623	arg1	disruption					593:602	the disruption	589:602	the disruption of retinal structure and function	589:636	Knockout of O-GlcNAc transferase or pharmacological inhibition of O-GlcNAcylation dramatically blocks phagocytosis, resulting in the disruption of retinal structure and function.
36796536	4	28	theme	retinal	607:613	arg1	structure					615:623	retinal structure	607:623	retinal structure	607:623	Knockout of O-GlcNAc transferase or pharmacological inhibition of O-GlcNAcylation dramatically blocks phagocytosis, resulting in the disruption of retinal structure and function.
36796536	5	29	theme	Mechanistic	639:649	arg1	studies					651:657	Mechanistic studies	639:657	Mechanistic studies	639:657	Mechanistic studies reveal that O-GlcNAc transferase interacts with Ezrin, a membrane-cytoskeleton linker protein, to catalyze its O-GlcNAcylation.
36796536	7	30	from	implications	1089:1100	arg1	health					1110:1115	health	1110:1115	health	1110:1115	These findings identify a previously unrecognized role for protein O-GlcNAcylation in phagocytosis with important implications in both health and diseases.
36796536	7	30	from	implications	1089:1100	arg1	diseases					1121:1128	diseases	1121:1128	diseases	1121:1128	These findings identify a previously unrecognized role for protein O-GlcNAcylation in phagocytosis with important implications in both health and diseases.
36796536	4	31	theme	transferase	481:491	arg1	Knockout					460:467	Knockout	460:467	Knockout	460:467	Knockout of O-GlcNAc transferase or pharmacological inhibition of O-GlcNAcylation dramatically blocks phagocytosis, resulting in the disruption of retinal structure and function.
36796536	7	32	theme	protein	1034:1040	arg1	O-GlcNAcylation					1042:1056	protein O-GlcNAcylation	1034:1056	protein O-GlcNAcylation	1034:1056	These findings identify a previously unrecognized role for protein O-GlcNAcylation in phagocytosis with important implications in both health and diseases.
36796536	0	33	theme	cell	78:81	arg1	cortex					83:88	the cell cortex	74:88	the cell cortex	74:88	O-GlcNAcylation regulates phagocytosis by promoting Ezrin localization at the cell cortex.
36796536	4	34	theme	O-GlcNAc	472:479	arg1	transferase					481:491	O-GlcNAc transferase	472:491	O-GlcNAc transferase	472:491	Knockout of O-GlcNAc transferase or pharmacological inhibition of O-GlcNAcylation dramatically blocks phagocytosis, resulting in the disruption of retinal structure and function.
36796536	1	35	theme	cellular	161:168	arg1	modification					131:142	a post-translational modification	110:142	a post-translational modification that serves as a cellular nutrient sensor and participates in multiple physiological and pathological processes	110:254	O-GlcNAcylation is a post-translational modification that serves as a cellular nutrient sensor and participates in multiple physiological and pathological processes.
36796536	1	35	theme	cellular	161:168	arg1	sensor					179:184	a cellular nutrient sensor	159:184	a cellular nutrient sensor	159:184	O-GlcNAcylation is a post-translational modification that serves as a cellular nutrient sensor and participates in multiple physiological and pathological processes.
24140293	4	0	from	expression	664:673	arg1	coli					681:684	E. coli	678:684	E. coli	678:684	Recombinant expression in E. coli is an advantageous approach, but only small quantities of insoluble O-GlcNAc-modified protein were produced.
24140293	4	1	theme	insoluble	744:752	arg1	protein					772:778	insoluble O-GlcNAc-modified protein	744:778	insoluble O-GlcNAc-modified protein	744:778	Recombinant expression in E. coli is an advantageous approach, but only small quantities of insoluble O-GlcNAc-modified protein were produced.
24140293	3	2	from	co-expression	431:443	arg1	coli					506:509	Escherichia coli	494:509	Escherichia coli	494:509	Recombinant co-expression of substrate protein and O-GlcNAc transferase in Escherichia coli was used to produce O-GlcNAc-modified domains of human cAMP responsive element-binding protein (CREB1) and Abelson tyrosine-kinase 2 (ABL2).
24140293	1	3	theme	important	178:186	arg1	modification					159:170	The O-linked β-N-acetylglucosamine (O-GlcNAc) post-translational modification	94:170	The O-linked β-N-acetylglucosamine (O-GlcNAc) post-translational modification	94:170	The O-linked β-N-acetylglucosamine (O-GlcNAc) post-translational modification is an important, regulatory modification of cytosolic and nuclear enzymes.
24140293	1	3	theme	important	178:186	arg1	modification					200:211	an important, regulatory modification	175:211	an important, regulatory modification of cytosolic and nuclear enzymes	175:244	The O-linked β-N-acetylglucosamine (O-GlcNAc) post-translational modification is an important, regulatory modification of cytosolic and nuclear enzymes.
24140293	6	4	theme	protein	1090:1096	arg1	yields					1062:1067	the yields	1058:1067	the yields of O-GlcNAc-modified protein	1058:1096	With the inhibitor present, the yields of O-GlcNAc-modified protein increased.
24140293	0	5	theme	proteins	84:91	arg1	production					30:39	the in vivo production	18:39	the in vivo production of O-linked β-N-acetylglucosamine-modified proteins	18:91	E. coli sabotages the in vivo production of O-linked β-N-acetylglucosamine-modified proteins.
24140293	3	6	theme	cAMP	566:569	arg1	CREB1					607:611	CREB1	607:611	CREB1	607:611	Recombinant co-expression of substrate protein and O-GlcNAc transferase in Escherichia coli was used to produce O-GlcNAc-modified domains of human cAMP responsive element-binding protein (CREB1) and Abelson tyrosine-kinase 2 (ABL2).
24140293	3	6	theme	cAMP	566:569	arg1	protein					598:604	human cAMP responsive element-binding protein	560:604	human cAMP responsive element-binding protein (CREB1)	560:612	Recombinant co-expression of substrate protein and O-GlcNAc transferase in Escherichia coli was used to produce O-GlcNAc-modified domains of human cAMP responsive element-binding protein (CREB1) and Abelson tyrosine-kinase 2 (ABL2).
24140293	6	7	theme	O-GlcNAc-modified	1072:1088	arg1	protein					1090:1096	O-GlcNAc-modified protein	1072:1096	O-GlcNAc-modified protein	1072:1096	With the inhibitor present, the yields of O-GlcNAc-modified protein increased.
24140293	8	8	theme	β-N-acetylglucosaminidase	1265:1289	arg1	identity					1237:1244	The identity	1233:1244	The identity of the interfering β-N-acetylglucosaminidase	1233:1289	The identity of the interfering β-N-acetylglucosaminidase was confirmed by testing a nagZ knockout strain.
24140293	9	9	theme	recycle	1422:1428	arg1	peptidoglycan					1430:1442	recycle peptidoglycan	1422:1442	recycle peptidoglycan	1422:1442	In E. coli, NagZ natively cleaves the GlcNAc-β1,4-N-acetylmuramic acid linkage to recycle peptidoglycan in the cytoplasm and cleaves the GlcNAc-β-O-linkage of foreign O-GlcNAc-modified proteins in vivo, sabotaging the recombinant co-expression system.
24140293	4	10	theme	small	724:728	arg1	quantities					730:739	only small quantities	719:739	only small quantities of insoluble O-GlcNAc-modified protein	719:778	Recombinant expression in E. coli is an advantageous approach, but only small quantities of insoluble O-GlcNAc-modified protein were produced.
24140293	3	11	theme	Abelson	618:624	arg1	tyrosine-kinase					626:640	Abelson tyrosine-kinase 2	618:642	Abelson tyrosine-kinase 2 (ABL2)	618:649	Recombinant co-expression of substrate protein and O-GlcNAc transferase in Escherichia coli was used to produce O-GlcNAc-modified domains of human cAMP responsive element-binding protein (CREB1) and Abelson tyrosine-kinase 2 (ABL2).
24140293	3	11	theme	Abelson	618:624	arg1	ABL2					645:648	ABL2	645:648	ABL2	645:648	Recombinant co-expression of substrate protein and O-GlcNAc transferase in Escherichia coli was used to produce O-GlcNAc-modified domains of human cAMP responsive element-binding protein (CREB1) and Abelson tyrosine-kinase 2 (ABL2).
24140293	9	12	theme	co-expression	1570:1582	arg1	system					1584:1589	the recombinant co-expression system	1554:1589	the recombinant co-expression system	1554:1589	In E. coli, NagZ natively cleaves the GlcNAc-β1,4-N-acetylmuramic acid linkage to recycle peptidoglycan in the cytoplasm and cleaves the GlcNAc-β-O-linkage of foreign O-GlcNAc-modified proteins in vivo, sabotaging the recombinant co-expression system.
24140293	2	13	theme	sufficient	353:362	arg1	quantities					364:373	sufficient quantities	353:373	sufficient quantities	353:373	To date, no 3-dimensional structures of O-GlcNAc-modified proteins exist due to difficulties in producing sufficient quantities with either in vitro or in vivo techniques.
24140293	3	14	theme	human	560:564	arg1	CREB1					607:611	CREB1	607:611	CREB1	607:611	Recombinant co-expression of substrate protein and O-GlcNAc transferase in Escherichia coli was used to produce O-GlcNAc-modified domains of human cAMP responsive element-binding protein (CREB1) and Abelson tyrosine-kinase 2 (ABL2).
24140293	3	14	theme	human	560:564	arg1	protein					598:604	human cAMP responsive element-binding protein	560:604	human cAMP responsive element-binding protein (CREB1)	560:612	Recombinant co-expression of substrate protein and O-GlcNAc transferase in Escherichia coli was used to produce O-GlcNAc-modified domains of human cAMP responsive element-binding protein (CREB1) and Abelson tyrosine-kinase 2 (ABL2).
24140293	9	15	theme	foreign	1499:1505	arg1	proteins					1525:1532	foreign O-GlcNAc-modified proteins	1499:1532	foreign O-GlcNAc-modified proteins	1499:1532	In E. coli, NagZ natively cleaves the GlcNAc-β1,4-N-acetylmuramic acid linkage to recycle peptidoglycan in the cytoplasm and cleaves the GlcNAc-β-O-linkage of foreign O-GlcNAc-modified proteins in vivo, sabotaging the recombinant co-expression system.
24140293	3	16	theme	O-GlcNAc-modified	531:547	arg1	domains					549:555	O-GlcNAc-modified domains	531:555	O-GlcNAc-modified domains of human cAMP responsive element-binding protein (CREB1) and Abelson tyrosine-kinase 2 (ABL2)	531:649	Recombinant co-expression of substrate protein and O-GlcNAc transferase in Escherichia coli was used to produce O-GlcNAc-modified domains of human cAMP responsive element-binding protein (CREB1) and Abelson tyrosine-kinase 2 (ABL2).
24140293	3	16	theme	O-GlcNAc-modified	531:547	arg1	protein					598:604	human cAMP responsive element-binding protein	560:604	human cAMP responsive element-binding protein (CREB1)	560:612	Recombinant co-expression of substrate protein and O-GlcNAc transferase in Escherichia coli was used to produce O-GlcNAc-modified domains of human cAMP responsive element-binding protein (CREB1) and Abelson tyrosine-kinase 2 (ABL2).
24140293	3	16	theme	O-GlcNAc-modified	531:547	arg1	tyrosine-kinase					626:640	Abelson tyrosine-kinase 2	618:642	Abelson tyrosine-kinase 2 (ABL2)	618:649	Recombinant co-expression of substrate protein and O-GlcNAc transferase in Escherichia coli was used to produce O-GlcNAc-modified domains of human cAMP responsive element-binding protein (CREB1) and Abelson tyrosine-kinase 2 (ABL2).
24140293	5	17	theme	β-N-acetylglucosaminidase	802:826	arg1	inhibitor					828:836	β-N-acetylglucosaminidase inhibitor	802:836	β-N-acetylglucosaminidase inhibitor	802:836	Adding β-N-acetylglucosaminidase inhibitor, O-(2-acetamido-2-dexoy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), to the culture media provided the first evidence that an E. coli enzyme cleaves O-GlcNAc from proteins in vivo.
24140293	2	18	theme	in	387:388	arg1	techniques					407:416	either in vitro or in vivo techniques	380:416	either in vitro or in vivo techniques	380:416	To date, no 3-dimensional structures of O-GlcNAc-modified proteins exist due to difficulties in producing sufficient quantities with either in vitro or in vivo techniques.
24140293	3	19	theme	protein	598:604	arg1	domains					549:555	O-GlcNAc-modified domains	531:555	O-GlcNAc-modified domains of human cAMP responsive element-binding protein (CREB1) and Abelson tyrosine-kinase 2 (ABL2)	531:649	Recombinant co-expression of substrate protein and O-GlcNAc transferase in Escherichia coli was used to produce O-GlcNAc-modified domains of human cAMP responsive element-binding protein (CREB1) and Abelson tyrosine-kinase 2 (ABL2).
24140293	3	19	theme	protein	598:604	arg1	protein					598:604	human cAMP responsive element-binding protein	560:604	human cAMP responsive element-binding protein (CREB1)	560:612	Recombinant co-expression of substrate protein and O-GlcNAc transferase in Escherichia coli was used to produce O-GlcNAc-modified domains of human cAMP responsive element-binding protein (CREB1) and Abelson tyrosine-kinase 2 (ABL2).
24140293	3	19	theme	protein	598:604	arg1	tyrosine-kinase					626:640	Abelson tyrosine-kinase 2	618:642	Abelson tyrosine-kinase 2 (ABL2)	618:649	Recombinant co-expression of substrate protein and O-GlcNAc transferase in Escherichia coli was used to produce O-GlcNAc-modified domains of human cAMP responsive element-binding protein (CREB1) and Abelson tyrosine-kinase 2 (ABL2).
24140293	5	20	theme	first	952:956	arg1	evidence					958:965	the first evidence that an E. coli enzyme cleaves O-GlcNAc from proteins in vivo	948:1027	the first evidence that an E. coli enzyme cleaves O-GlcNAc from proteins in vivo	948:1027	Adding β-N-acetylglucosaminidase inhibitor, O-(2-acetamido-2-dexoy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), to the culture media provided the first evidence that an E. coli enzyme cleaves O-GlcNAc from proteins in vivo.
24140293	7	21	theme	synthetic	1196:1204	arg1	O-GlcNAc-peptide					1206:1221	a synthetic O-GlcNAc-peptide	1194:1221	a synthetic O-GlcNAc-peptide	1194:1221	The E. coli β-N-acetylglucosaminidase was isolated and shown to cleave O-GlcNAc from a synthetic O-GlcNAc-peptide in vitro.
24140293	5	22	from	proteins	1012:1019	arg1	O-GlcNAc					998:1005	O-GlcNAc	998:1005	O-GlcNAc from proteins	998:1019	Adding β-N-acetylglucosaminidase inhibitor, O-(2-acetamido-2-dexoy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), to the culture media provided the first evidence that an E. coli enzyme cleaves O-GlcNAc from proteins in vivo.
24140293	2	23	theme	proteins	305:312	arg1	structures					273:282	no 3-dimensional structures	256:282	no 3-dimensional structures of O-GlcNAc-modified proteins	256:312	To date, no 3-dimensional structures of O-GlcNAc-modified proteins exist due to difficulties in producing sufficient quantities with either in vitro or in vivo techniques.
24140293	3	24	theme	Recombinant	419:429	arg1	co-expression					431:443	Recombinant co-expression	419:443	Recombinant co-expression of substrate protein and O-GlcNAc transferase in Escherichia coli	419:509	Recombinant co-expression of substrate protein and O-GlcNAc transferase in Escherichia coli was used to produce O-GlcNAc-modified domains of human cAMP responsive element-binding protein (CREB1) and Abelson tyrosine-kinase 2 (ABL2).
24140293	1	25	link	O-linked	98:105	arg1	modification					159:170	The O-linked β-N-acetylglucosamine (O-GlcNAc) post-translational modification	94:170	The O-linked β-N-acetylglucosamine (O-GlcNAc) post-translational modification	94:170	The O-linked β-N-acetylglucosamine (O-GlcNAc) post-translational modification is an important, regulatory modification of cytosolic and nuclear enzymes.
24140293	1	25	link	O-linked	98:105	arg1	modification					200:211	an important, regulatory modification	175:211	an important, regulatory modification of cytosolic and nuclear enzymes	175:244	The O-linked β-N-acetylglucosamine (O-GlcNAc) post-translational modification is an important, regulatory modification of cytosolic and nuclear enzymes.
24140293	1	26	dep	important	178:186	arg1	regulatory					189:198	regulatory	189:198	regulatory	189:198	The O-linked β-N-acetylglucosamine (O-GlcNAc) post-translational modification is an important, regulatory modification of cytosolic and nuclear enzymes.
24140293	7	27	dep	E.	1113:1114	arg1	coli					1116:1119	coli	1116:1119	coli	1116:1119	The E. coli β-N-acetylglucosaminidase was isolated and shown to cleave O-GlcNAc from a synthetic O-GlcNAc-peptide in vitro.
24140293	3	28	theme	O-GlcNAc	470:477	arg1	transferase					479:489	O-GlcNAc transferase	470:489	O-GlcNAc transferase	470:489	Recombinant co-expression of substrate protein and O-GlcNAc transferase in Escherichia coli was used to produce O-GlcNAc-modified domains of human cAMP responsive element-binding protein (CREB1) and Abelson tyrosine-kinase 2 (ABL2).
24140293	5	29	dep	amino-N-phenylcarbamate	884:906	arg1	PUGNAc					909:914	PUGNAc	909:914	PUGNAc	909:914	Adding β-N-acetylglucosaminidase inhibitor, O-(2-acetamido-2-dexoy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), to the culture media provided the first evidence that an E. coli enzyme cleaves O-GlcNAc from proteins in vivo.
24140293	1	30	theme	O-linked	98:105	arg1	modification					159:170	The O-linked β-N-acetylglucosamine (O-GlcNAc) post-translational modification	94:170	The O-linked β-N-acetylglucosamine (O-GlcNAc) post-translational modification	94:170	The O-linked β-N-acetylglucosamine (O-GlcNAc) post-translational modification is an important, regulatory modification of cytosolic and nuclear enzymes.
24140293	1	30	theme	O-linked	98:105	arg1	modification					200:211	an important, regulatory modification	175:211	an important, regulatory modification of cytosolic and nuclear enzymes	175:244	The O-linked β-N-acetylglucosamine (O-GlcNAc) post-translational modification is an important, regulatory modification of cytosolic and nuclear enzymes.
24140293	1	31	theme	cytosolic	216:224	arg1	enzymes					238:244	cytosolic and nuclear enzymes	216:244	cytosolic and nuclear enzymes	216:244	The O-linked β-N-acetylglucosamine (O-GlcNAc) post-translational modification is an important, regulatory modification of cytosolic and nuclear enzymes.
24140293	8	32	theme	nagZ	1318:1321	arg1	strain					1332:1337	a nagZ knockout strain	1316:1337	a nagZ knockout strain	1316:1337	The identity of the interfering β-N-acetylglucosaminidase was confirmed by testing a nagZ knockout strain.
24140293	1	33	theme	β-N-acetylglucosamine	107:127	arg1	modification					159:170	The O-linked β-N-acetylglucosamine (O-GlcNAc) post-translational modification	94:170	The O-linked β-N-acetylglucosamine (O-GlcNAc) post-translational modification	94:170	The O-linked β-N-acetylglucosamine (O-GlcNAc) post-translational modification is an important, regulatory modification of cytosolic and nuclear enzymes.
24140293	1	33	theme	β-N-acetylglucosamine	107:127	arg1	modification					200:211	an important, regulatory modification	175:211	an important, regulatory modification of cytosolic and nuclear enzymes	175:244	The O-linked β-N-acetylglucosamine (O-GlcNAc) post-translational modification is an important, regulatory modification of cytosolic and nuclear enzymes.
24140293	5	34	theme	culture	925:931	arg1	media					933:937	the culture media	921:937	the culture media	921:937	Adding β-N-acetylglucosaminidase inhibitor, O-(2-acetamido-2-dexoy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), to the culture media provided the first evidence that an E. coli enzyme cleaves O-GlcNAc from proteins in vivo.
24140293	3	35	used	used	515:518	arg2	co-expression					431:443	Recombinant co-expression	419:443	Recombinant co-expression of substrate protein and O-GlcNAc transferase in Escherichia coli	419:509	Recombinant co-expression of substrate protein and O-GlcNAc transferase in Escherichia coli was used to produce O-GlcNAc-modified domains of human cAMP responsive element-binding protein (CREB1) and Abelson tyrosine-kinase 2 (ABL2).
24140293	1	36	theme	nuclear	230:236	arg1	enzymes					238:244	cytosolic and nuclear enzymes	216:244	cytosolic and nuclear enzymes	216:244	The O-linked β-N-acetylglucosamine (O-GlcNAc) post-translational modification is an important, regulatory modification of cytosolic and nuclear enzymes.
24140293	3	37	theme	protein	458:464	arg1	co-expression					431:443	Recombinant co-expression	419:443	Recombinant co-expression of substrate protein and O-GlcNAc transferase in Escherichia coli	419:509	Recombinant co-expression of substrate protein and O-GlcNAc transferase in Escherichia coli was used to produce O-GlcNAc-modified domains of human cAMP responsive element-binding protein (CREB1) and Abelson tyrosine-kinase 2 (ABL2).
24140293	6	38	theme	inhibitor	1039:1047	arg1	present					1049:1055	the inhibitor present	1035:1055	the inhibitor present	1035:1055	With the inhibitor present, the yields of O-GlcNAc-modified protein increased.
24140293	4	39	theme	advantageous	692:703	arg1	expression					664:673	Recombinant expression	652:673	Recombinant expression in E. coli	652:684	Recombinant expression in E. coli is an advantageous approach, but only small quantities of insoluble O-GlcNAc-modified protein were produced.
24140293	4	39	theme	advantageous	692:703	arg1	approach					705:712	an advantageous approach	689:712	an advantageous approach	689:712	Recombinant expression in E. coli is an advantageous approach, but only small quantities of insoluble O-GlcNAc-modified protein were produced.
24140293	3	40	theme	transferase	479:489	arg1	co-expression					431:443	Recombinant co-expression	419:443	Recombinant co-expression of substrate protein and O-GlcNAc transferase in Escherichia coli	419:509	Recombinant co-expression of substrate protein and O-GlcNAc transferase in Escherichia coli was used to produce O-GlcNAc-modified domains of human cAMP responsive element-binding protein (CREB1) and Abelson tyrosine-kinase 2 (ABL2).
24140293	1	41	theme	enzymes	238:244	arg1	modification					159:170	The O-linked β-N-acetylglucosamine (O-GlcNAc) post-translational modification	94:170	The O-linked β-N-acetylglucosamine (O-GlcNAc) post-translational modification	94:170	The O-linked β-N-acetylglucosamine (O-GlcNAc) post-translational modification is an important, regulatory modification of cytosolic and nuclear enzymes.
24140293	1	41	theme	enzymes	238:244	arg1	modification					200:211	an important, regulatory modification	175:211	an important, regulatory modification of cytosolic and nuclear enzymes	175:244	The O-linked β-N-acetylglucosamine (O-GlcNAc) post-translational modification is an important, regulatory modification of cytosolic and nuclear enzymes.
24140293	0	42	theme	in	22:23	arg1	production					30:39	the in vivo production	18:39	the in vivo production of O-linked β-N-acetylglucosamine-modified proteins	18:91	E. coli sabotages the in vivo production of O-linked β-N-acetylglucosamine-modified proteins.
24140293	5	43	theme	amino-N-phenylcarbamate	884:906	arg1	inhibitor					828:836	β-N-acetylglucosaminidase inhibitor	802:836	β-N-acetylglucosaminidase inhibitor	802:836	Adding β-N-acetylglucosaminidase inhibitor, O-(2-acetamido-2-dexoy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), to the culture media provided the first evidence that an E. coli enzyme cleaves O-GlcNAc from proteins in vivo.
24140293	9	44	theme	proteins	1525:1532	arg1	GlcNAc-β-O-linkage					1477:1494	the GlcNAc-β-O-linkage	1473:1494	the GlcNAc-β-O-linkage of foreign O-GlcNAc-modified proteins	1473:1532	In E. coli, NagZ natively cleaves the GlcNAc-β1,4-N-acetylmuramic acid linkage to recycle peptidoglycan in the cytoplasm and cleaves the GlcNAc-β-O-linkage of foreign O-GlcNAc-modified proteins in vivo, sabotaging the recombinant co-expression system.
24140293	9	45	theme	GlcNAc-β1,4-N-acetylmuramic	1378:1404	arg1	linkage					1411:1417	the GlcNAc-β1,4-N-acetylmuramic acid linkage	1374:1417	the GlcNAc-β1,4-N-acetylmuramic acid linkage to recycle peptidoglycan	1374:1442	In E. coli, NagZ natively cleaves the GlcNAc-β1,4-N-acetylmuramic acid linkage to recycle peptidoglycan in the cytoplasm and cleaves the GlcNAc-β-O-linkage of foreign O-GlcNAc-modified proteins in vivo, sabotaging the recombinant co-expression system.
24140293	5	46	theme	E.	975:976	arg1	enzyme					983:988	an E. coli enzyme	972:988	an E. coli enzyme	972:988	Adding β-N-acetylglucosaminidase inhibitor, O-(2-acetamido-2-dexoy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), to the culture media provided the first evidence that an E. coli enzyme cleaves O-GlcNAc from proteins in vivo.
24140293	8	47	theme	knockout	1323:1330	arg1	strain					1332:1337	a nagZ knockout strain	1316:1337	a nagZ knockout strain	1316:1337	The identity of the interfering β-N-acetylglucosaminidase was confirmed by testing a nagZ knockout strain.
24140293	7	48	theme	E.	1113:1114	arg1	β-N-acetylglucosaminidase					1121:1145	The E. coli β-N-acetylglucosaminidase	1109:1145	The E. coli β-N-acetylglucosaminidase	1109:1145	The E. coli β-N-acetylglucosaminidase was isolated and shown to cleave O-GlcNAc from a synthetic O-GlcNAc-peptide in vitro.
24140293	1	49	theme	O-GlcNAc	130:137	arg1	modification					159:170	The O-linked β-N-acetylglucosamine (O-GlcNAc) post-translational modification	94:170	The O-linked β-N-acetylglucosamine (O-GlcNAc) post-translational modification	94:170	The O-linked β-N-acetylglucosamine (O-GlcNAc) post-translational modification is an important, regulatory modification of cytosolic and nuclear enzymes.
24140293	1	49	theme	O-GlcNAc	130:137	arg1	modification					200:211	an important, regulatory modification	175:211	an important, regulatory modification of cytosolic and nuclear enzymes	175:244	The O-linked β-N-acetylglucosamine (O-GlcNAc) post-translational modification is an important, regulatory modification of cytosolic and nuclear enzymes.
24140293	3	50	theme	substrate	448:456	arg1	protein					458:464	substrate protein	448:464	substrate protein	448:464	Recombinant co-expression of substrate protein and O-GlcNAc transferase in Escherichia coli was used to produce O-GlcNAc-modified domains of human cAMP responsive element-binding protein (CREB1) and Abelson tyrosine-kinase 2 (ABL2).
24140293	9	51	theme	O-GlcNAc-modified	1507:1523	arg1	proteins					1525:1532	foreign O-GlcNAc-modified proteins	1499:1532	foreign O-GlcNAc-modified proteins	1499:1532	In E. coli, NagZ natively cleaves the GlcNAc-β1,4-N-acetylmuramic acid linkage to recycle peptidoglycan in the cytoplasm and cleaves the GlcNAc-β-O-linkage of foreign O-GlcNAc-modified proteins in vivo, sabotaging the recombinant co-expression system.
24140293	0	52	dep	in	22:23	arg1	vivo					25:28	vivo	25:28	vivo	25:28	E. coli sabotages the in vivo production of O-linked β-N-acetylglucosamine-modified proteins.
24140293	4	53	theme	O-GlcNAc-modified	754:770	arg1	protein					772:778	insoluble O-GlcNAc-modified protein	744:778	insoluble O-GlcNAc-modified protein	744:778	Recombinant expression in E. coli is an advantageous approach, but only small quantities of insoluble O-GlcNAc-modified protein were produced.
24140293	3	54	theme	tyrosine-kinase	626:640	arg1	domains					549:555	O-GlcNAc-modified domains	531:555	O-GlcNAc-modified domains of human cAMP responsive element-binding protein (CREB1) and Abelson tyrosine-kinase 2 (ABL2)	531:649	Recombinant co-expression of substrate protein and O-GlcNAc transferase in Escherichia coli was used to produce O-GlcNAc-modified domains of human cAMP responsive element-binding protein (CREB1) and Abelson tyrosine-kinase 2 (ABL2).
24140293	3	54	theme	tyrosine-kinase	626:640	arg1	protein					598:604	human cAMP responsive element-binding protein	560:604	human cAMP responsive element-binding protein (CREB1)	560:612	Recombinant co-expression of substrate protein and O-GlcNAc transferase in Escherichia coli was used to produce O-GlcNAc-modified domains of human cAMP responsive element-binding protein (CREB1) and Abelson tyrosine-kinase 2 (ABL2).
24140293	3	54	theme	tyrosine-kinase	626:640	arg1	tyrosine-kinase					626:640	Abelson tyrosine-kinase 2	618:642	Abelson tyrosine-kinase 2 (ABL2)	618:649	Recombinant co-expression of substrate protein and O-GlcNAc transferase in Escherichia coli was used to produce O-GlcNAc-modified domains of human cAMP responsive element-binding protein (CREB1) and Abelson tyrosine-kinase 2 (ABL2).
24140293	4	55	theme	protein	772:778	arg1	quantities					730:739	only small quantities	719:739	only small quantities of insoluble O-GlcNAc-modified protein	719:778	Recombinant expression in E. coli is an advantageous approach, but only small quantities of insoluble O-GlcNAc-modified protein were produced.
24140293	2	56	theme	O-GlcNAc-modified	287:303	arg1	proteins					305:312	O-GlcNAc-modified proteins	287:312	O-GlcNAc-modified proteins	287:312	To date, no 3-dimensional structures of O-GlcNAc-modified proteins exist due to difficulties in producing sufficient quantities with either in vitro or in vivo techniques.
24140293	0	57	link	O-linked	44:51	arg1	proteins					84:91	O-linked β-N-acetylglucosamine-modified proteins	44:91	O-linked β-N-acetylglucosamine-modified proteins	44:91	E. coli sabotages the in vivo production of O-linked β-N-acetylglucosamine-modified proteins.
24140293	1	58	theme	post-translational	140:157	arg1	modification					159:170	The O-linked β-N-acetylglucosamine (O-GlcNAc) post-translational modification	94:170	The O-linked β-N-acetylglucosamine (O-GlcNAc) post-translational modification	94:170	The O-linked β-N-acetylglucosamine (O-GlcNAc) post-translational modification is an important, regulatory modification of cytosolic and nuclear enzymes.
24140293	1	58	theme	post-translational	140:157	arg1	modification					200:211	an important, regulatory modification	175:211	an important, regulatory modification of cytosolic and nuclear enzymes	175:244	The O-linked β-N-acetylglucosamine (O-GlcNAc) post-translational modification is an important, regulatory modification of cytosolic and nuclear enzymes.
24140293	2	59	dep	in	387:388	arg1	vitro					390:394	vitro	390:394	vitro	390:394	To date, no 3-dimensional structures of O-GlcNAc-modified proteins exist due to difficulties in producing sufficient quantities with either in vitro or in vivo techniques.
24140293	2	60	dep	in	399:400	arg1	vivo					402:405	vivo	402:405	vivo	402:405	To date, no 3-dimensional structures of O-GlcNAc-modified proteins exist due to difficulties in producing sufficient quantities with either in vitro or in vivo techniques.
24140293	9	61	theme	recombinant	1558:1568	arg1	system					1584:1589	the recombinant co-expression system	1554:1589	the recombinant co-expression system	1554:1589	In E. coli, NagZ natively cleaves the GlcNAc-β1,4-N-acetylmuramic acid linkage to recycle peptidoglycan in the cytoplasm and cleaves the GlcNAc-β-O-linkage of foreign O-GlcNAc-modified proteins in vivo, sabotaging the recombinant co-expression system.
24140293	3	62	theme	element-binding	582:596	arg1	CREB1					607:611	CREB1	607:611	CREB1	607:611	Recombinant co-expression of substrate protein and O-GlcNAc transferase in Escherichia coli was used to produce O-GlcNAc-modified domains of human cAMP responsive element-binding protein (CREB1) and Abelson tyrosine-kinase 2 (ABL2).
24140293	3	62	theme	element-binding	582:596	arg1	protein					598:604	human cAMP responsive element-binding protein	560:604	human cAMP responsive element-binding protein (CREB1)	560:612	Recombinant co-expression of substrate protein and O-GlcNAc transferase in Escherichia coli was used to produce O-GlcNAc-modified domains of human cAMP responsive element-binding protein (CREB1) and Abelson tyrosine-kinase 2 (ABL2).
24140293	4	63	theme	Recombinant	652:662	arg1	expression					664:673	Recombinant expression	652:673	Recombinant expression in E. coli	652:684	Recombinant expression in E. coli is an advantageous approach, but only small quantities of insoluble O-GlcNAc-modified protein were produced.
24140293	4	63	theme	Recombinant	652:662	arg1	approach					705:712	an advantageous approach	689:712	an advantageous approach	689:712	Recombinant expression in E. coli is an advantageous approach, but only small quantities of insoluble O-GlcNAc-modified protein were produced.
24140293	0	64	theme	β-N-acetylglucosamine-modified	53:82	arg1	proteins					84:91	O-linked β-N-acetylglucosamine-modified proteins	44:91	O-linked β-N-acetylglucosamine-modified proteins	44:91	E. coli sabotages the in vivo production of O-linked β-N-acetylglucosamine-modified proteins.
24140293	5	65	dep	E.	975:976	arg1	coli					978:981	coli	978:981	coli	978:981	Adding β-N-acetylglucosaminidase inhibitor, O-(2-acetamido-2-dexoy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), to the culture media provided the first evidence that an E. coli enzyme cleaves O-GlcNAc from proteins in vivo.
24140293	3	66	theme	responsive	571:580	arg1	CREB1					607:611	CREB1	607:611	CREB1	607:611	Recombinant co-expression of substrate protein and O-GlcNAc transferase in Escherichia coli was used to produce O-GlcNAc-modified domains of human cAMP responsive element-binding protein (CREB1) and Abelson tyrosine-kinase 2 (ABL2).
24140293	3	66	theme	responsive	571:580	arg1	protein					598:604	human cAMP responsive element-binding protein	560:604	human cAMP responsive element-binding protein (CREB1)	560:612	Recombinant co-expression of substrate protein and O-GlcNAc transferase in Escherichia coli was used to produce O-GlcNAc-modified domains of human cAMP responsive element-binding protein (CREB1) and Abelson tyrosine-kinase 2 (ABL2).
24140293	0	67	theme	O-linked	44:51	arg1	proteins					84:91	O-linked β-N-acetylglucosamine-modified proteins	44:91	O-linked β-N-acetylglucosamine-modified proteins	44:91	E. coli sabotages the in vivo production of O-linked β-N-acetylglucosamine-modified proteins.
24140293	9	68	theme	acid	1406:1409	arg1	linkage					1411:1417	the GlcNAc-β1,4-N-acetylmuramic acid linkage	1374:1417	the GlcNAc-β1,4-N-acetylmuramic acid linkage to recycle peptidoglycan	1374:1442	In E. coli, NagZ natively cleaves the GlcNAc-β1,4-N-acetylmuramic acid linkage to recycle peptidoglycan in the cytoplasm and cleaves the GlcNAc-β-O-linkage of foreign O-GlcNAc-modified proteins in vivo, sabotaging the recombinant co-expression system.
24140293	2	69	theme	3-dimensional	259:271	arg1	structures					273:282	no 3-dimensional structures	256:282	no 3-dimensional structures of O-GlcNAc-modified proteins	256:312	To date, no 3-dimensional structures of O-GlcNAc-modified proteins exist due to difficulties in producing sufficient quantities with either in vitro or in vivo techniques.
24140293	2	70	theme	in	399:400	arg1	techniques					407:416	either in vitro or in vivo techniques	380:416	either in vitro or in vivo techniques	380:416	To date, no 3-dimensional structures of O-GlcNAc-modified proteins exist due to difficulties in producing sufficient quantities with either in vitro or in vivo techniques.
24140293	8	71	theme	interfering	1253:1263	arg1	β-N-acetylglucosaminidase					1265:1289	the interfering β-N-acetylglucosaminidase	1249:1289	the interfering β-N-acetylglucosaminidase	1249:1289	The identity of the interfering β-N-acetylglucosaminidase was confirmed by testing a nagZ knockout strain.
18057713	7	0	theme	CREB	1544:1547	arg1	import					1519:1524	the nuclear import	1507:1524	the nuclear import of O-GlcNAcylated CREB	1507:1547	In addition, PUGNAc increased the nuclear import of O-GlcNAcylated CREB.
18057713	2	1	theme	present	312:318	arg1	study					320:324	the present study	308:324	the present study	308:324	In the present study, we found that treatment of HuH-7 human hepatoma cells with high glucose or the protein O-N-acetylglucosaminidase (O-GlcNAcase) inhibitor O-(2-acetoamide-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc) increased the cell surface expression of E-selectin.
18057713	4	2	theme	expression	908:917	arg1	vector					919:924	A expression vector	906:924	a protein kinase A expression vector pFC-PKA that enhances the phosphorylation of CRE binding protein (CREB)	889:996	Enhanced CRE promoter activities in HuH-7 cells treated with dibutyryl cAMP or co-transfected with a protein kinase A expression vector pFC-PKA that enhances the phosphorylation of CRE binding protein (CREB) were suppressed by PUGNAc.
18057713	4	3	theme	protein	983:989	arg1	phosphorylation					952:966	the phosphorylation	948:966	the phosphorylation of CRE binding protein (CREB)	948:996	Enhanced CRE promoter activities in HuH-7 cells treated with dibutyryl cAMP or co-transfected with a protein kinase A expression vector pFC-PKA that enhances the phosphorylation of CRE binding protein (CREB) were suppressed by PUGNAc.
18057713	7	4	theme	nuclear	1511:1517	arg1	import					1519:1524	the nuclear import	1507:1524	the nuclear import of O-GlcNAcylated CREB	1507:1547	In addition, PUGNAc increased the nuclear import of O-GlcNAcylated CREB.
18057713	0	5	theme	E-selectin	134:143	arg1	expression					145:154	E-selectin expression	134:154	E-selectin expression on HuH-7 human hepatoma cells	134:184	Protein O-N-acetylglucosaminylation modulates promoter activities of cyclic AMP response element and activator protein 1 and enhances E-selectin expression on HuH-7 human hepatoma cells.
18057713	6	6	theme	protein	1336:1342	arg1	O-GlcNAcylation					1344:1358	protein O-GlcNAcylation	1336:1358	protein O-GlcNAcylation	1336:1358	Immuno-blotting using an anti-O-GlcNAc antibody revealed that high glucose and PUGNAc accelerated protein O-GlcNAcylation and that there were substantial differences in the O-GlcNAcylated proteins in the cytoplasmic and nuclear fractions.
18057713	8	7	from	expression	1731:1740	arg1	hepatocytes					1745:1755	hepatocytes	1745:1755	hepatocytes	1745:1755	These results suggest that protein O-GlcNAcylation modulates the promoter activities of E-selectin gene, suppression of CRE and enhancement of AP-1, and enhances E-selectin protein expression on hepatocytes.
18057713	5	8	theme	mitogen-activated	1127:1143	arg1	kinase					1167:1172	a mitogen-activated protein kinase kinase kinase	1125:1172	a mitogen-activated protein kinase kinase kinase expression vector pFC-MEKK that enhances c-Jun phosphorylation	1125:1235	In contrast, PUGNAc further increased the enhanced AP-1 promoter activity in cells transfected with a mitogen-activated protein kinase kinase kinase expression vector pFC-MEKK that enhances c-Jun phosphorylation.
18057713	0	9	theme	promoter	46:53	arg1	activities					55:64	promoter activities	46:64	promoter activities of cyclic AMP response element and activator protein 1	46:119	Protein O-N-acetylglucosaminylation modulates promoter activities of cyclic AMP response element and activator protein 1 and enhances E-selectin expression on HuH-7 human hepatoma cells.
18057713	8	10	theme	protein	1577:1583	arg1	O-GlcNAcylation					1585:1599	protein O-GlcNAcylation	1577:1599	protein O-GlcNAcylation	1577:1599	These results suggest that protein O-GlcNAcylation modulates the promoter activities of E-selectin gene, suppression of CRE and enhancement of AP-1, and enhances E-selectin protein expression on hepatocytes.
18057713	0	11	theme	human	165:169	arg1	cells					180:184	HuH-7 human hepatoma cells	159:184	HuH-7 human hepatoma cells	159:184	Protein O-N-acetylglucosaminylation modulates promoter activities of cyclic AMP response element and activator protein 1 and enhances E-selectin expression on HuH-7 human hepatoma cells.
18057713	4	12	theme	CRE	971:973	arg1	protein					983:989	CRE binding protein	971:989	CRE binding protein (CREB)	971:996	Enhanced CRE promoter activities in HuH-7 cells treated with dibutyryl cAMP or co-transfected with a protein kinase A expression vector pFC-PKA that enhances the phosphorylation of CRE binding protein (CREB) were suppressed by PUGNAc.
18057713	4	12	theme	CRE	971:973	arg1	CREB					992:995	CREB	992:995	CREB	992:995	Enhanced CRE promoter activities in HuH-7 cells treated with dibutyryl cAMP or co-transfected with a protein kinase A expression vector pFC-PKA that enhances the phosphorylation of CRE binding protein (CREB) were suppressed by PUGNAc.
18057713	3	13	theme	cyclic	706:711	arg1	element					726:732	the cyclic AMP response element	702:732	the cyclic AMP response element (CRE)	702:738	A dual luciferase reporter assay indicated that high glucose and PUGNAc suppressed promoter activities of the cyclic AMP response element (CRE) and enhanced those of activator protein 1 (AP-1).
18057713	3	13	theme	cyclic	706:711	arg1	CRE					735:737	CRE	735:737	CRE	735:737	A dual luciferase reporter assay indicated that high glucose and PUGNAc suppressed promoter activities of the cyclic AMP response element (CRE) and enhanced those of activator protein 1 (AP-1).
18057713	8	14	theme	promoter	1615:1622	arg1	activities					1624:1633	the promoter activities	1611:1633	the promoter activities of E-selectin gene, suppression of CRE and enhancement of AP-1	1611:1696	These results suggest that protein O-GlcNAcylation modulates the promoter activities of E-selectin gene, suppression of CRE and enhancement of AP-1, and enhances E-selectin protein expression on hepatocytes.
18057713	0	15	theme	response	80:87	arg1	element					89:95	cyclic AMP response element	69:95	cyclic AMP response element	69:95	Protein O-N-acetylglucosaminylation modulates promoter activities of cyclic AMP response element and activator protein 1 and enhances E-selectin expression on HuH-7 human hepatoma cells.
18057713	5	16	theme	vector	1185:1190	arg1	pFC-MEKK					1192:1199	a mitogen-activated protein kinase kinase kinase expression vector pFC-MEKK	1125:1199	a mitogen-activated protein kinase kinase kinase expression vector pFC-MEKK that enhances c-Jun phosphorylation	1125:1235	In contrast, PUGNAc further increased the enhanced AP-1 promoter activity in cells transfected with a mitogen-activated protein kinase kinase kinase expression vector pFC-MEKK that enhances c-Jun phosphorylation.
18057713	2	17	theme	cell	557:560	arg1	expression					570:579	the cell surface expression	553:579	the cell surface expression of E-selectin	553:593	In the present study, we found that treatment of HuH-7 human hepatoma cells with high glucose or the protein O-N-acetylglucosaminidase (O-GlcNAcase) inhibitor O-(2-acetoamide-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc) increased the cell surface expression of E-selectin.
18057713	8	18	theme	gene	1649:1652	arg1	activities					1624:1633	the promoter activities	1611:1633	the promoter activities of E-selectin gene, suppression of CRE and enhancement of AP-1	1611:1696	These results suggest that protein O-GlcNAcylation modulates the promoter activities of E-selectin gene, suppression of CRE and enhancement of AP-1, and enhances E-selectin protein expression on hepatocytes.
18057713	0	19	theme	protein	111:117	arg1	activities					55:64	promoter activities	46:64	promoter activities of cyclic AMP response element and activator protein 1	46:119	Protein O-N-acetylglucosaminylation modulates promoter activities of cyclic AMP response element and activator protein 1 and enhances E-selectin expression on HuH-7 human hepatoma cells.
18057713	5	20	theme	kinase	1153:1158	arg1	kinase					1167:1172	a mitogen-activated protein kinase kinase kinase	1125:1172	a mitogen-activated protein kinase kinase kinase expression vector pFC-MEKK that enhances c-Jun phosphorylation	1125:1235	In contrast, PUGNAc further increased the enhanced AP-1 promoter activity in cells transfected with a mitogen-activated protein kinase kinase kinase expression vector pFC-MEKK that enhances c-Jun phosphorylation.
18057713	2	21	with	treatment	341:349	arg1	PUGNAc					535:540	PUGNAc	535:540	PUGNAc	535:540	In the present study, we found that treatment of HuH-7 human hepatoma cells with high glucose or the protein O-N-acetylglucosaminidase (O-GlcNAcase) inhibitor O-(2-acetoamide-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc) increased the cell surface expression of E-selectin.
18057713	2	21	with	treatment	341:349	arg1	amino-N-phenylcarbamate					510:532	the protein O-N-acetylglucosaminidase (O-GlcNAcase) inhibitor O-(2-acetoamide-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate	402:532	the protein O-N-acetylglucosaminidase (O-GlcNAcase) inhibitor O-(2-acetoamide-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc)	402:541	In the present study, we found that treatment of HuH-7 human hepatoma cells with high glucose or the protein O-N-acetylglucosaminidase (O-GlcNAcase) inhibitor O-(2-acetoamide-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc) increased the cell surface expression of E-selectin.
18057713	2	21	with	treatment	341:349	arg1	glucose					391:397	high glucose	386:397	high glucose	386:397	In the present study, we found that treatment of HuH-7 human hepatoma cells with high glucose or the protein O-N-acetylglucosaminidase (O-GlcNAcase) inhibitor O-(2-acetoamide-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc) increased the cell surface expression of E-selectin.
18057713	2	22	theme	E-selectin	584:593	arg1	expression					570:579	the cell surface expression	553:579	the cell surface expression of E-selectin	553:593	In the present study, we found that treatment of HuH-7 human hepatoma cells with high glucose or the protein O-N-acetylglucosaminidase (O-GlcNAcase) inhibitor O-(2-acetoamide-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc) increased the cell surface expression of E-selectin.
18057713	8	23	theme	suppression	1655:1665	arg1	activities					1624:1633	the promoter activities	1611:1633	the promoter activities of E-selectin gene, suppression of CRE and enhancement of AP-1	1611:1696	These results suggest that protein O-GlcNAcylation modulates the promoter activities of E-selectin gene, suppression of CRE and enhancement of AP-1, and enhances E-selectin protein expression on hepatocytes.
18057713	5	24	theme	kinase	1167:1172	arg1	pFC-MEKK					1192:1199	a mitogen-activated protein kinase kinase kinase expression vector pFC-MEKK	1125:1199	a mitogen-activated protein kinase kinase kinase expression vector pFC-MEKK that enhances c-Jun phosphorylation	1125:1235	In contrast, PUGNAc further increased the enhanced AP-1 promoter activity in cells transfected with a mitogen-activated protein kinase kinase kinase expression vector pFC-MEKK that enhances c-Jun phosphorylation.
18057713	8	25	theme	CRE	1670:1672	arg1	gene					1649:1652	E-selectin gene	1638:1652	E-selectin gene	1638:1652	These results suggest that protein O-GlcNAcylation modulates the promoter activities of E-selectin gene, suppression of CRE and enhancement of AP-1, and enhances E-selectin protein expression on hepatocytes.
18057713	8	25	theme	CRE	1670:1672	arg1	enhancement					1678:1688	enhancement	1678:1688	enhancement of AP-1	1678:1696	These results suggest that protein O-GlcNAcylation modulates the promoter activities of E-selectin gene, suppression of CRE and enhancement of AP-1, and enhances E-selectin protein expression on hepatocytes.
18057713	8	25	theme	CRE	1670:1672	arg1	suppression					1655:1665	suppression	1655:1665	suppression of CRE	1655:1672	These results suggest that protein O-GlcNAcylation modulates the promoter activities of E-selectin gene, suppression of CRE and enhancement of AP-1, and enhances E-selectin protein expression on hepatocytes.
18057713	4	26	theme	Enhanced	790:797	arg1	activities					812:821	Enhanced CRE promoter activities	790:821	Enhanced CRE promoter activities in HuH-7 cells treated with dibutyryl cAMP or co-transfected with a protein kinase A expression vector pFC-PKA that enhances the phosphorylation of CRE binding protein (CREB)	790:996	Enhanced CRE promoter activities in HuH-7 cells treated with dibutyryl cAMP or co-transfected with a protein kinase A expression vector pFC-PKA that enhances the phosphorylation of CRE binding protein (CREB) were suppressed by PUGNAc.
18057713	2	27	theme	protein	406:412	arg1	PUGNAc					535:540	PUGNAc	535:540	PUGNAc	535:540	In the present study, we found that treatment of HuH-7 human hepatoma cells with high glucose or the protein O-N-acetylglucosaminidase (O-GlcNAcase) inhibitor O-(2-acetoamide-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc) increased the cell surface expression of E-selectin.
18057713	2	27	theme	protein	406:412	arg1	amino-N-phenylcarbamate					510:532	the protein O-N-acetylglucosaminidase (O-GlcNAcase) inhibitor O-(2-acetoamide-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate	402:532	the protein O-N-acetylglucosaminidase (O-GlcNAcase) inhibitor O-(2-acetoamide-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc)	402:541	In the present study, we found that treatment of HuH-7 human hepatoma cells with high glucose or the protein O-N-acetylglucosaminidase (O-GlcNAcase) inhibitor O-(2-acetoamide-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc) increased the cell surface expression of E-selectin.
18057713	0	28	theme	Protein	0:6	arg1	O-N-acetylglucosaminylation					8:34	Protein O-N-acetylglucosaminylation	0:34	Protein O-N-acetylglucosaminylation	0:34	Protein O-N-acetylglucosaminylation modulates promoter activities of cyclic AMP response element and activator protein 1 and enhances E-selectin expression on HuH-7 human hepatoma cells.
18057713	2	29	theme	2-acetoamide-2-deoxy-D-glucopyranosylidene	467:508	arg1	PUGNAc					535:540	PUGNAc	535:540	PUGNAc	535:540	In the present study, we found that treatment of HuH-7 human hepatoma cells with high glucose or the protein O-N-acetylglucosaminidase (O-GlcNAcase) inhibitor O-(2-acetoamide-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc) increased the cell surface expression of E-selectin.
18057713	2	29	theme	2-acetoamide-2-deoxy-D-glucopyranosylidene	467:508	arg1	amino-N-phenylcarbamate					510:532	the protein O-N-acetylglucosaminidase (O-GlcNAcase) inhibitor O-(2-acetoamide-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate	402:532	the protein O-N-acetylglucosaminidase (O-GlcNAcase) inhibitor O-(2-acetoamide-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc)	402:541	In the present study, we found that treatment of HuH-7 human hepatoma cells with high glucose or the protein O-N-acetylglucosaminidase (O-GlcNAcase) inhibitor O-(2-acetoamide-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc) increased the cell surface expression of E-selectin.
18057713	8	30	theme	enhancement	1678:1688	arg1	activities					1624:1633	the promoter activities	1611:1633	the promoter activities of E-selectin gene, suppression of CRE and enhancement of AP-1	1611:1696	These results suggest that protein O-GlcNAcylation modulates the promoter activities of E-selectin gene, suppression of CRE and enhancement of AP-1, and enhances E-selectin protein expression on hepatocytes.
18057713	4	31	theme	promoter	803:810	arg1	activities					812:821	Enhanced CRE promoter activities	790:821	Enhanced CRE promoter activities in HuH-7 cells treated with dibutyryl cAMP or co-transfected with a protein kinase A expression vector pFC-PKA that enhances the phosphorylation of CRE binding protein (CREB)	790:996	Enhanced CRE promoter activities in HuH-7 cells treated with dibutyryl cAMP or co-transfected with a protein kinase A expression vector pFC-PKA that enhances the phosphorylation of CRE binding protein (CREB) were suppressed by PUGNAc.
18057713	2	32	theme	O-	464:465	arg1	PUGNAc					535:540	PUGNAc	535:540	PUGNAc	535:540	In the present study, we found that treatment of HuH-7 human hepatoma cells with high glucose or the protein O-N-acetylglucosaminidase (O-GlcNAcase) inhibitor O-(2-acetoamide-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc) increased the cell surface expression of E-selectin.
18057713	2	32	theme	O-	464:465	arg1	amino-N-phenylcarbamate					510:532	the protein O-N-acetylglucosaminidase (O-GlcNAcase) inhibitor O-(2-acetoamide-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate	402:532	the protein O-N-acetylglucosaminidase (O-GlcNAcase) inhibitor O-(2-acetoamide-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc)	402:541	In the present study, we found that treatment of HuH-7 human hepatoma cells with high glucose or the protein O-N-acetylglucosaminidase (O-GlcNAcase) inhibitor O-(2-acetoamide-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc) increased the cell surface expression of E-selectin.
18057713	8	33	theme	AP-1	1693:1696	arg1	gene					1649:1652	E-selectin gene	1638:1652	E-selectin gene	1638:1652	These results suggest that protein O-GlcNAcylation modulates the promoter activities of E-selectin gene, suppression of CRE and enhancement of AP-1, and enhances E-selectin protein expression on hepatocytes.
18057713	8	33	theme	AP-1	1693:1696	arg1	enhancement					1678:1688	enhancement	1678:1688	enhancement of AP-1	1678:1696	These results suggest that protein O-GlcNAcylation modulates the promoter activities of E-selectin gene, suppression of CRE and enhancement of AP-1, and enhances E-selectin protein expression on hepatocytes.
18057713	8	33	theme	AP-1	1693:1696	arg1	suppression					1655:1665	suppression	1655:1665	suppression of CRE	1655:1672	These results suggest that protein O-GlcNAcylation modulates the promoter activities of E-selectin gene, suppression of CRE and enhancement of AP-1, and enhances E-selectin protein expression on hepatocytes.
18057713	5	34	theme	c-Jun	1215:1219	arg1	phosphorylation					1221:1235	c-Jun phosphorylation	1215:1235	c-Jun phosphorylation	1215:1235	In contrast, PUGNAc further increased the enhanced AP-1 promoter activity in cells transfected with a mitogen-activated protein kinase kinase kinase expression vector pFC-MEKK that enhances c-Jun phosphorylation.
18057713	5	35	theme	enhanced	1067:1074	arg1	activity					1090:1097	the enhanced AP-1 promoter activity	1063:1097	the enhanced AP-1 promoter activity	1063:1097	In contrast, PUGNAc further increased the enhanced AP-1 promoter activity in cells transfected with a mitogen-activated protein kinase kinase kinase expression vector pFC-MEKK that enhances c-Jun phosphorylation.
18057713	3	36	theme	response	717:724	arg1	element					726:732	the cyclic AMP response element	702:732	the cyclic AMP response element (CRE)	702:738	A dual luciferase reporter assay indicated that high glucose and PUGNAc suppressed promoter activities of the cyclic AMP response element (CRE) and enhanced those of activator protein 1 (AP-1).
18057713	3	36	theme	response	717:724	arg1	CRE					735:737	CRE	735:737	CRE	735:737	A dual luciferase reporter assay indicated that high glucose and PUGNAc suppressed promoter activities of the cyclic AMP response element (CRE) and enhanced those of activator protein 1 (AP-1).
18057713	2	37	theme	cells	375:379	arg1	treatment					341:349	treatment	341:349	treatment of HuH-7 human hepatoma cells with high glucose or the protein O-N-acetylglucosaminidase (O-GlcNAcase) inhibitor O-(2-acetoamide-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc)	341:541	In the present study, we found that treatment of HuH-7 human hepatoma cells with high glucose or the protein O-N-acetylglucosaminidase (O-GlcNAcase) inhibitor O-(2-acetoamide-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc) increased the cell surface expression of E-selectin.
18057713	0	38	theme	cyclic	69:74	arg1	element					89:95	cyclic AMP response element	69:95	cyclic AMP response element	69:95	Protein O-N-acetylglucosaminylation modulates promoter activities of cyclic AMP response element and activator protein 1 and enhances E-selectin expression on HuH-7 human hepatoma cells.
18057713	5	39	theme	promoter	1081:1088	arg1	activity					1090:1097	the enhanced AP-1 promoter activity	1063:1097	the enhanced AP-1 promoter activity	1063:1097	In contrast, PUGNAc further increased the enhanced AP-1 promoter activity in cells transfected with a mitogen-activated protein kinase kinase kinase expression vector pFC-MEKK that enhances c-Jun phosphorylation.
18057713	8	40	theme	E-selectin	1712:1721	arg1	expression					1731:1740	E-selectin protein expression	1712:1740	E-selectin protein expression on hepatocytes	1712:1755	These results suggest that protein O-GlcNAcylation modulates the promoter activities of E-selectin gene, suppression of CRE and enhancement of AP-1, and enhances E-selectin protein expression on hepatocytes.
18057713	2	41	theme	human	360:364	arg1	cells					375:379	HuH-7 human hepatoma cells	354:379	HuH-7 human hepatoma cells	354:379	In the present study, we found that treatment of HuH-7 human hepatoma cells with high glucose or the protein O-N-acetylglucosaminidase (O-GlcNAcase) inhibitor O-(2-acetoamide-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc) increased the cell surface expression of E-selectin.
18057713	1	42	theme	proteins	261:268	arg1	O-GlcNAcylation					241:255	O-GlcNAcylation	241:255	O-GlcNAcylation	241:255	High glucose accelerates O-N-acetylglucosaminylation (O-GlcNAcylation) of proteins and causes diabetic complications.
18057713	1	42	theme	proteins	261:268	arg1	O-N-acetylglucosaminylation					212:238	O-N-acetylglucosaminylation	212:238	O-N-acetylglucosaminylation (O-GlcNAcylation) of proteins	212:268	High glucose accelerates O-N-acetylglucosaminylation (O-GlcNAcylation) of proteins and causes diabetic complications.
18057713	3	43	theme	luciferase	603:612	arg1	assay					623:627	A dual luciferase reporter assay	596:627	A dual luciferase reporter assay	596:627	A dual luciferase reporter assay indicated that high glucose and PUGNAc suppressed promoter activities of the cyclic AMP response element (CRE) and enhanced those of activator protein 1 (AP-1).
18057713	2	44	theme	high	386:389	arg1	glucose					391:397	high glucose	386:397	high glucose	386:397	In the present study, we found that treatment of HuH-7 human hepatoma cells with high glucose or the protein O-N-acetylglucosaminidase (O-GlcNAcase) inhibitor O-(2-acetoamide-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc) increased the cell surface expression of E-selectin.
18057713	1	45	theme	diabetic	281:288	arg1	complications					290:302	diabetic complications	281:302	diabetic complications	281:302	High glucose accelerates O-N-acetylglucosaminylation (O-GlcNAcylation) of proteins and causes diabetic complications.
18057713	4	46	theme	vector	919:924	arg1	pFC-PKA					926:932	A expression vector pFC-PKA	906:932	a protein kinase A expression vector pFC-PKA that enhances the phosphorylation of CRE binding protein (CREB)	889:996	Enhanced CRE promoter activities in HuH-7 cells treated with dibutyryl cAMP or co-transfected with a protein kinase A expression vector pFC-PKA that enhances the phosphorylation of CRE binding protein (CREB) were suppressed by PUGNAc.
18057713	6	47	theme	substantial	1380:1390	arg1	differences					1392:1402	substantial differences	1380:1402	substantial differences in the O-GlcNAcylated proteins in the cytoplasmic and nuclear fractions	1380:1474	Immuno-blotting using an anti-O-GlcNAc antibody revealed that high glucose and PUGNAc accelerated protein O-GlcNAcylation and that there were substantial differences in the O-GlcNAcylated proteins in the cytoplasmic and nuclear fractions.
18057713	3	48	theme	reporter	614:621	arg1	assay					623:627	A dual luciferase reporter assay	596:627	A dual luciferase reporter assay	596:627	A dual luciferase reporter assay indicated that high glucose and PUGNAc suppressed promoter activities of the cyclic AMP response element (CRE) and enhanced those of activator protein 1 (AP-1).
18057713	6	49	theme	anti-O-GlcNAc	1263:1275	arg1	antibody					1277:1284	an anti-O-GlcNAc antibody	1260:1284	an anti-O-GlcNAc antibody	1260:1284	Immuno-blotting using an anti-O-GlcNAc antibody revealed that high glucose and PUGNAc accelerated protein O-GlcNAcylation and that there were substantial differences in the O-GlcNAcylated proteins in the cytoplasmic and nuclear fractions.
18057713	3	50	theme	dual	598:601	arg1	assay					623:627	A dual luciferase reporter assay	596:627	A dual luciferase reporter assay	596:627	A dual luciferase reporter assay indicated that high glucose and PUGNAc suppressed promoter activities of the cyclic AMP response element (CRE) and enhanced those of activator protein 1 (AP-1).
18057713	1	51	theme	High	187:190	arg1	glucose					192:198	High glucose	187:198	High glucose	187:198	High glucose accelerates O-N-acetylglucosaminylation (O-GlcNAcylation) of proteins and causes diabetic complications.
18057713	4	52	theme	protein	891:897	arg1	kinase					899:904	a protein kinase	889:904	a protein kinase A expression vector pFC-PKA that enhances the phosphorylation of CRE binding protein (CREB)	889:996	Enhanced CRE promoter activities in HuH-7 cells treated with dibutyryl cAMP or co-transfected with a protein kinase A expression vector pFC-PKA that enhances the phosphorylation of CRE binding protein (CREB) were suppressed by PUGNAc.
18057713	3	53	theme	high	644:647	arg1	glucose					649:655	high glucose	644:655	high glucose	644:655	A dual luciferase reporter assay indicated that high glucose and PUGNAc suppressed promoter activities of the cyclic AMP response element (CRE) and enhanced those of activator protein 1 (AP-1).
18057713	7	54	theme	O-GlcNAcylated	1529:1542	arg1	CREB					1544:1547	O-GlcNAcylated CREB	1529:1547	O-GlcNAcylated CREB	1529:1547	In addition, PUGNAc increased the nuclear import of O-GlcNAcylated CREB.
18057713	6	55	theme	nuclear	1458:1464	arg1	fractions					1466:1474	the cytoplasmic and nuclear fractions	1438:1474	the cytoplasmic and nuclear fractions	1438:1474	Immuno-blotting using an anti-O-GlcNAc antibody revealed that high glucose and PUGNAc accelerated protein O-GlcNAcylation and that there were substantial differences in the O-GlcNAcylated proteins in the cytoplasmic and nuclear fractions.
18057713	4	56	theme	binding	975:981	arg1	protein					983:989	CRE binding protein	971:989	CRE binding protein (CREB)	971:996	Enhanced CRE promoter activities in HuH-7 cells treated with dibutyryl cAMP or co-transfected with a protein kinase A expression vector pFC-PKA that enhances the phosphorylation of CRE binding protein (CREB) were suppressed by PUGNAc.
18057713	4	56	theme	binding	975:981	arg1	CREB					992:995	CREB	992:995	CREB	992:995	Enhanced CRE promoter activities in HuH-7 cells treated with dibutyryl cAMP or co-transfected with a protein kinase A expression vector pFC-PKA that enhances the phosphorylation of CRE binding protein (CREB) were suppressed by PUGNAc.
18057713	6	57	theme	cytoplasmic	1442:1452	arg1	fractions					1466:1474	the cytoplasmic and nuclear fractions	1438:1474	the cytoplasmic and nuclear fractions	1438:1474	Immuno-blotting using an anti-O-GlcNAc antibody revealed that high glucose and PUGNAc accelerated protein O-GlcNAcylation and that there were substantial differences in the O-GlcNAcylated proteins in the cytoplasmic and nuclear fractions.
18057713	0	58	theme	hepatoma	171:178	arg1	cells					180:184	HuH-7 human hepatoma cells	159:184	HuH-7 human hepatoma cells	159:184	Protein O-N-acetylglucosaminylation modulates promoter activities of cyclic AMP response element and activator protein 1 and enhances E-selectin expression on HuH-7 human hepatoma cells.
18057713	5	59	theme	protein	1145:1151	arg1	kinase					1167:1172	a mitogen-activated protein kinase kinase kinase	1125:1172	a mitogen-activated protein kinase kinase kinase expression vector pFC-MEKK that enhances c-Jun phosphorylation	1125:1235	In contrast, PUGNAc further increased the enhanced AP-1 promoter activity in cells transfected with a mitogen-activated protein kinase kinase kinase expression vector pFC-MEKK that enhances c-Jun phosphorylation.
18057713	6	60	theme	O-GlcNAcylated	1411:1424	arg1	proteins					1426:1433	the O-GlcNAcylated proteins	1407:1433	the O-GlcNAcylated proteins	1407:1433	Immuno-blotting using an anti-O-GlcNAc antibody revealed that high glucose and PUGNAc accelerated protein O-GlcNAcylation and that there were substantial differences in the O-GlcNAcylated proteins in the cytoplasmic and nuclear fractions.
18057713	6	61	theme	high	1300:1303	arg1	glucose					1305:1311	high glucose	1300:1311	high glucose	1300:1311	Immuno-blotting using an anti-O-GlcNAc antibody revealed that high glucose and PUGNAc accelerated protein O-GlcNAcylation and that there were substantial differences in the O-GlcNAcylated proteins in the cytoplasmic and nuclear fractions.
18057713	0	62	theme	element	89:95	arg1	activities					55:64	promoter activities	46:64	promoter activities of cyclic AMP response element and activator protein 1	46:119	Protein O-N-acetylglucosaminylation modulates promoter activities of cyclic AMP response element and activator protein 1 and enhances E-selectin expression on HuH-7 human hepatoma cells.
18057713	4	63	dep	cells	832:836	arg1	co-transfected					869:882	co-transfected	869:882	co-transfected with a protein kinase A expression vector pFC-PKA that enhances the phosphorylation of CRE binding protein (CREB)	869:996	Enhanced CRE promoter activities in HuH-7 cells treated with dibutyryl cAMP or co-transfected with a protein kinase A expression vector pFC-PKA that enhances the phosphorylation of CRE binding protein (CREB) were suppressed by PUGNAc.
18057713	4	63	dep	cells	832:836	arg1	treated					838:844	treated	838:844	treated with dibutyryl cAMP	838:864	Enhanced CRE promoter activities in HuH-7 cells treated with dibutyryl cAMP or co-transfected with a protein kinase A expression vector pFC-PKA that enhances the phosphorylation of CRE binding protein (CREB) were suppressed by PUGNAc.
18057713	2	64	theme	surface	562:568	arg1	expression					570:579	the cell surface expression	553:579	the cell surface expression of E-selectin	553:593	In the present study, we found that treatment of HuH-7 human hepatoma cells with high glucose or the protein O-N-acetylglucosaminidase (O-GlcNAcase) inhibitor O-(2-acetoamide-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc) increased the cell surface expression of E-selectin.
18057713	8	65	theme	E-selectin	1638:1647	arg1	gene					1649:1652	E-selectin gene	1638:1652	E-selectin gene	1638:1652	These results suggest that protein O-GlcNAcylation modulates the promoter activities of E-selectin gene, suppression of CRE and enhancement of AP-1, and enhances E-selectin protein expression on hepatocytes.
18057713	0	66	theme	activator	101:109	arg1	protein					111:117	activator protein 1	101:119	activator protein 1	101:119	Protein O-N-acetylglucosaminylation modulates promoter activities of cyclic AMP response element and activator protein 1 and enhances E-selectin expression on HuH-7 human hepatoma cells.
18057713	5	67	theme	kinase	1160:1165	arg1	kinase					1167:1172	a mitogen-activated protein kinase kinase kinase	1125:1172	a mitogen-activated protein kinase kinase kinase expression vector pFC-MEKK that enhances c-Jun phosphorylation	1125:1235	In contrast, PUGNAc further increased the enhanced AP-1 promoter activity in cells transfected with a mitogen-activated protein kinase kinase kinase expression vector pFC-MEKK that enhances c-Jun phosphorylation.
18057713	4	68	from	activities	812:821	arg1	cells					832:836	HuH-7 cells	826:836	HuH-7 cells treated with dibutyryl cAMP or co-transfected with a protein kinase A expression vector pFC-PKA that enhances the phosphorylation of CRE binding protein (CREB)	826:996	Enhanced CRE promoter activities in HuH-7 cells treated with dibutyryl cAMP or co-transfected with a protein kinase A expression vector pFC-PKA that enhances the phosphorylation of CRE binding protein (CREB) were suppressed by PUGNAc.
18057713	4	69	theme	HuH-7	826:830	arg1	cells					832:836	HuH-7 cells	826:836	HuH-7 cells treated with dibutyryl cAMP or co-transfected with a protein kinase A expression vector pFC-PKA that enhances the phosphorylation of CRE binding protein (CREB)	826:996	Enhanced CRE promoter activities in HuH-7 cells treated with dibutyryl cAMP or co-transfected with a protein kinase A expression vector pFC-PKA that enhances the phosphorylation of CRE binding protein (CREB) were suppressed by PUGNAc.
18057713	2	70	theme	O-N-acetylglucosaminidase	414:438	arg1	PUGNAc					535:540	PUGNAc	535:540	PUGNAc	535:540	In the present study, we found that treatment of HuH-7 human hepatoma cells with high glucose or the protein O-N-acetylglucosaminidase (O-GlcNAcase) inhibitor O-(2-acetoamide-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc) increased the cell surface expression of E-selectin.
18057713	2	70	theme	O-N-acetylglucosaminidase	414:438	arg1	amino-N-phenylcarbamate					510:532	the protein O-N-acetylglucosaminidase (O-GlcNAcase) inhibitor O-(2-acetoamide-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate	402:532	the protein O-N-acetylglucosaminidase (O-GlcNAcase) inhibitor O-(2-acetoamide-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc)	402:541	In the present study, we found that treatment of HuH-7 human hepatoma cells with high glucose or the protein O-N-acetylglucosaminidase (O-GlcNAcase) inhibitor O-(2-acetoamide-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc) increased the cell surface expression of E-selectin.
18057713	5	71	theme	expression	1174:1183	arg1	pFC-MEKK					1192:1199	a mitogen-activated protein kinase kinase kinase expression vector pFC-MEKK	1125:1199	a mitogen-activated protein kinase kinase kinase expression vector pFC-MEKK that enhances c-Jun phosphorylation	1125:1235	In contrast, PUGNAc further increased the enhanced AP-1 promoter activity in cells transfected with a mitogen-activated protein kinase kinase kinase expression vector pFC-MEKK that enhances c-Jun phosphorylation.
18057713	0	72	theme	HuH-7	159:163	arg1	cells					180:184	HuH-7 human hepatoma cells	159:184	HuH-7 human hepatoma cells	159:184	Protein O-N-acetylglucosaminylation modulates promoter activities of cyclic AMP response element and activator protein 1 and enhances E-selectin expression on HuH-7 human hepatoma cells.
18057713	4	73	dep	kinase	899:904	arg1	pFC-PKA					926:932	A expression vector pFC-PKA	906:932	a protein kinase A expression vector pFC-PKA that enhances the phosphorylation of CRE binding protein (CREB)	889:996	Enhanced CRE promoter activities in HuH-7 cells treated with dibutyryl cAMP or co-transfected with a protein kinase A expression vector pFC-PKA that enhances the phosphorylation of CRE binding protein (CREB) were suppressed by PUGNAc.
18057713	3	74	theme	element	726:732	arg1	activities					688:697	promoter activities	679:697	promoter activities of the cyclic AMP response element (CRE)	679:738	A dual luciferase reporter assay indicated that high glucose and PUGNAc suppressed promoter activities of the cyclic AMP response element (CRE) and enhanced those of activator protein 1 (AP-1).
18057713	4	75	theme	CRE	799:801	arg1	activities					812:821	Enhanced CRE promoter activities	790:821	Enhanced CRE promoter activities in HuH-7 cells treated with dibutyryl cAMP or co-transfected with a protein kinase A expression vector pFC-PKA that enhances the phosphorylation of CRE binding protein (CREB)	790:996	Enhanced CRE promoter activities in HuH-7 cells treated with dibutyryl cAMP or co-transfected with a protein kinase A expression vector pFC-PKA that enhances the phosphorylation of CRE binding protein (CREB) were suppressed by PUGNAc.
18057713	2	76	theme	inhibitor	454:462	arg1	PUGNAc					535:540	PUGNAc	535:540	PUGNAc	535:540	In the present study, we found that treatment of HuH-7 human hepatoma cells with high glucose or the protein O-N-acetylglucosaminidase (O-GlcNAcase) inhibitor O-(2-acetoamide-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc) increased the cell surface expression of E-selectin.
18057713	2	76	theme	inhibitor	454:462	arg1	amino-N-phenylcarbamate					510:532	the protein O-N-acetylglucosaminidase (O-GlcNAcase) inhibitor O-(2-acetoamide-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate	402:532	the protein O-N-acetylglucosaminidase (O-GlcNAcase) inhibitor O-(2-acetoamide-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc)	402:541	In the present study, we found that treatment of HuH-7 human hepatoma cells with high glucose or the protein O-N-acetylglucosaminidase (O-GlcNAcase) inhibitor O-(2-acetoamide-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc) increased the cell surface expression of E-selectin.
18057713	3	77	theme	AMP	713:715	arg1	element					726:732	the cyclic AMP response element	702:732	the cyclic AMP response element (CRE)	702:738	A dual luciferase reporter assay indicated that high glucose and PUGNAc suppressed promoter activities of the cyclic AMP response element (CRE) and enhanced those of activator protein 1 (AP-1).
18057713	3	77	theme	AMP	713:715	arg1	CRE					735:737	CRE	735:737	CRE	735:737	A dual luciferase reporter assay indicated that high glucose and PUGNAc suppressed promoter activities of the cyclic AMP response element (CRE) and enhanced those of activator protein 1 (AP-1).
18057713	2	78	theme	O-GlcNAcase	441:451	arg1	PUGNAc					535:540	PUGNAc	535:540	PUGNAc	535:540	In the present study, we found that treatment of HuH-7 human hepatoma cells with high glucose or the protein O-N-acetylglucosaminidase (O-GlcNAcase) inhibitor O-(2-acetoamide-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc) increased the cell surface expression of E-selectin.
18057713	2	78	theme	O-GlcNAcase	441:451	arg1	amino-N-phenylcarbamate					510:532	the protein O-N-acetylglucosaminidase (O-GlcNAcase) inhibitor O-(2-acetoamide-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate	402:532	the protein O-N-acetylglucosaminidase (O-GlcNAcase) inhibitor O-(2-acetoamide-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc)	402:541	In the present study, we found that treatment of HuH-7 human hepatoma cells with high glucose or the protein O-N-acetylglucosaminidase (O-GlcNAcase) inhibitor O-(2-acetoamide-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc) increased the cell surface expression of E-selectin.
18057713	0	79	theme	AMP	76:78	arg1	element					89:95	cyclic AMP response element	69:95	cyclic AMP response element	69:95	Protein O-N-acetylglucosaminylation modulates promoter activities of cyclic AMP response element and activator protein 1 and enhances E-selectin expression on HuH-7 human hepatoma cells.
18057713	5	80	theme	AP-1	1076:1079	arg1	activity					1090:1097	the enhanced AP-1 promoter activity	1063:1097	the enhanced AP-1 promoter activity	1063:1097	In contrast, PUGNAc further increased the enhanced AP-1 promoter activity in cells transfected with a mitogen-activated protein kinase kinase kinase expression vector pFC-MEKK that enhances c-Jun phosphorylation.
18057713	8	81	theme	protein	1723:1729	arg1	expression					1731:1740	E-selectin protein expression	1712:1740	E-selectin protein expression on hepatocytes	1712:1755	These results suggest that protein O-GlcNAcylation modulates the promoter activities of E-selectin gene, suppression of CRE and enhancement of AP-1, and enhances E-selectin protein expression on hepatocytes.
18057713	2	82	theme	hepatoma	366:373	arg1	cells					375:379	HuH-7 human hepatoma cells	354:379	HuH-7 human hepatoma cells	354:379	In the present study, we found that treatment of HuH-7 human hepatoma cells with high glucose or the protein O-N-acetylglucosaminidase (O-GlcNAcase) inhibitor O-(2-acetoamide-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc) increased the cell surface expression of E-selectin.
18057713	3	83	theme	promoter	679:686	arg1	activities					688:697	promoter activities	679:697	promoter activities of the cyclic AMP response element (CRE)	679:738	A dual luciferase reporter assay indicated that high glucose and PUGNAc suppressed promoter activities of the cyclic AMP response element (CRE) and enhanced those of activator protein 1 (AP-1).
18057713	2	84	theme	HuH-7	354:358	arg1	cells					375:379	HuH-7 human hepatoma cells	354:379	HuH-7 human hepatoma cells	354:379	In the present study, we found that treatment of HuH-7 human hepatoma cells with high glucose or the protein O-N-acetylglucosaminidase (O-GlcNAcase) inhibitor O-(2-acetoamide-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc) increased the cell surface expression of E-selectin.
18057713	0	85	from	expression	145:154	arg1	cells					180:184	HuH-7 human hepatoma cells	159:184	HuH-7 human hepatoma cells	159:184	Protein O-N-acetylglucosaminylation modulates promoter activities of cyclic AMP response element and activator protein 1 and enhances E-selectin expression on HuH-7 human hepatoma cells.
18057713	3	86	theme	activator	762:770	arg1	protein					772:778	activator protein 1	762:780	activator protein 1 (AP-1)	762:787	A dual luciferase reporter assay indicated that high glucose and PUGNAc suppressed promoter activities of the cyclic AMP response element (CRE) and enhanced those of activator protein 1 (AP-1).
18057713	3	86	theme	activator	762:770	arg1	AP-1					783:786	AP-1	783:786	AP-1	783:786	A dual luciferase reporter assay indicated that high glucose and PUGNAc suppressed promoter activities of the cyclic AMP response element (CRE) and enhanced those of activator protein 1 (AP-1).
18057713	4	87	theme	dibutyryl	851:859	arg1	cAMP					861:864	dibutyryl cAMP	851:864	dibutyryl cAMP	851:864	Enhanced CRE promoter activities in HuH-7 cells treated with dibutyryl cAMP or co-transfected with a protein kinase A expression vector pFC-PKA that enhances the phosphorylation of CRE binding protein (CREB) were suppressed by PUGNAc.
18057713	6	88	from	differences	1392:1402	arg1	proteins					1426:1433	the O-GlcNAcylated proteins	1407:1433	the O-GlcNAcylated proteins	1407:1433	Immuno-blotting using an anti-O-GlcNAc antibody revealed that high glucose and PUGNAc accelerated protein O-GlcNAcylation and that there were substantial differences in the O-GlcNAcylated proteins in the cytoplasmic and nuclear fractions.
18057713	6	88	from	differences	1392:1402	arg1	fractions					1466:1474	the cytoplasmic and nuclear fractions	1438:1474	the cytoplasmic and nuclear fractions	1438:1474	Immuno-blotting using an anti-O-GlcNAc antibody revealed that high glucose and PUGNAc accelerated protein O-GlcNAcylation and that there were substantial differences in the O-GlcNAcylated proteins in the cytoplasmic and nuclear fractions.
32375037	5	0	theme	type	1201:1204	arg1	diabetes					1208:1215	type 2 diabetes	1201:1215	type 2 diabetes	1201:1215	This study reveals an important physiological role for β cell O-GlcNAcylation in sensing and responding to obesity, with therapeutic implications for managing the relationship between type 2 diabetes and its most common risk factor.
32375037	1	1	theme	increased	150:158	arg1	demand					170:175	increased metabolic demand	150:175	increased metabolic demand	150:175	During early obesity, pancreatic β cells compensate for increased metabolic demand through a transient phase of insulin hypersecretion that stabilizes blood glucose and forestalls diabetic progression.
32375037	2	2	theme	protein	383:389	arg1	modification					391:402	a nutrient-responsive post-translational protein modification	342:402	a nutrient-responsive post-translational protein modification regulated by O-GlcNAc transferase (OGT)	342:442	We find evidence that β cell O-GlcNAcylation, a nutrient-responsive post-translational protein modification regulated by O-GlcNAc transferase (OGT), is critical for coupling hyperlipidemia to β cell functional adaptation during this compensatory prediabetic phase.
32375037	2	2	theme	protein	383:389	arg1	O-GlcNAcylation					325:339	β cell O-GlcNAcylation	318:339	β cell O-GlcNAcylation	318:339	We find evidence that β cell O-GlcNAcylation, a nutrient-responsive post-translational protein modification regulated by O-GlcNAc transferase (OGT), is critical for coupling hyperlipidemia to β cell functional adaptation during this compensatory prediabetic phase.
32375037	5	3	theme	important	1039:1047	arg1	role					1063:1066	an important physiological role	1036:1066	an important physiological role for β cell O-GlcNAcylation in sensing and responding to obesity	1036:1130	This study reveals an important physiological role for β cell O-GlcNAcylation in sensing and responding to obesity, with therapeutic implications for managing the relationship between type 2 diabetes and its most common risk factor.
32375037	5	4	theme	β	1072:1072	arg1	O-GlcNAcylation					1079:1093	β cell O-GlcNAcylation	1072:1093	β cell O-GlcNAcylation	1072:1093	This study reveals an important physiological role for β cell O-GlcNAcylation in sensing and responding to obesity, with therapeutic implications for managing the relationship between type 2 diabetes and its most common risk factor.
32375037	3	5	theme	hyperinsulinemic	743:758	arg1	responses					760:768	hyperinsulinemic responses	743:768	hyperinsulinemic responses to lipids, in vivo and in vitro	743:800	In mice, islet O-GlcNAcylation rises and falls in tandem with the timeline of secretory potentiation during high-fat feeding while genetic models of β-cell-specific OGT loss abolish hyperinsulinemic responses to lipids, in vivo and in vitro.
32375037	4	6	theme	endoplasmic	819:829	arg1	ER					842:843	ER	842:843	ER	842:843	We identify the endoplasmic reticulum (ER) Ca2+ ATPase SERCA2 as a β cell O-GlcNAcylated protein in mice and humans that is able to rescue palmitate-stimulated insulin secretion through pharmacological activation.
32375037	4	6	theme	endoplasmic	819:829	arg1	reticulum					831:839	endoplasmic reticulum	819:839	the endoplasmic reticulum (ER) Ca2+ ATPase SERCA2	815:863	We identify the endoplasmic reticulum (ER) Ca2+ ATPase SERCA2 as a β cell O-GlcNAcylated protein in mice and humans that is able to rescue palmitate-stimulated insulin secretion through pharmacological activation.
32375037	1	7	theme	diabetic	274:281	arg1	progression					283:293	diabetic progression	274:293	diabetic progression	274:293	During early obesity, pancreatic β cells compensate for increased metabolic demand through a transient phase of insulin hypersecretion that stabilizes blood glucose and forestalls diabetic progression.
32375037	4	8	theme	pharmacological	989:1003	arg1	activation					1005:1014	pharmacological activation	989:1014	pharmacological activation	989:1014	We identify the endoplasmic reticulum (ER) Ca2+ ATPase SERCA2 as a β cell O-GlcNAcylated protein in mice and humans that is able to rescue palmitate-stimulated insulin secretion through pharmacological activation.
32375037	4	9	from	protein	892:898	arg1	humans					912:917	humans	912:917	humans	912:917	We identify the endoplasmic reticulum (ER) Ca2+ ATPase SERCA2 as a β cell O-GlcNAcylated protein in mice and humans that is able to rescue palmitate-stimulated insulin secretion through pharmacological activation.
32375037	4	9	from	protein	892:898	arg1	mice					903:906	mice	903:906	mice	903:906	We identify the endoplasmic reticulum (ER) Ca2+ ATPase SERCA2 as a β cell O-GlcNAcylated protein in mice and humans that is able to rescue palmitate-stimulated insulin secretion through pharmacological activation.
32375037	4	10	theme	O-GlcNAcylated	877:890	arg1	protein					892:898	a β cell O-GlcNAcylated protein	868:898	a β cell O-GlcNAcylated protein in mice and humans that is able to rescue palmitate-stimulated insulin secretion through pharmacological activation	868:1014	We identify the endoplasmic reticulum (ER) Ca2+ ATPase SERCA2 as a β cell O-GlcNAcylated protein in mice and humans that is able to rescue palmitate-stimulated insulin secretion through pharmacological activation.
32375037	4	10	theme	O-GlcNAcylated	877:890	arg1	SERCA2					858:863	the endoplasmic reticulum (ER) Ca2+ ATPase SERCA2	815:863	the endoplasmic reticulum (ER) Ca2+ ATPase SERCA2	815:863	We identify the endoplasmic reticulum (ER) Ca2+ ATPase SERCA2 as a β cell O-GlcNAcylated protein in mice and humans that is able to rescue palmitate-stimulated insulin secretion through pharmacological activation.
32375037	5	11	dep	important	1039:1047	arg1	physiological					1049:1061	physiological	1049:1061	physiological	1049:1061	This study reveals an important physiological role for β cell O-GlcNAcylation in sensing and responding to obesity, with therapeutic implications for managing the relationship between type 2 diabetes and its most common risk factor.
32375037	4	12	theme	cell	872:875	arg1	protein					892:898	a β cell O-GlcNAcylated protein	868:898	a β cell O-GlcNAcylated protein in mice and humans that is able to rescue palmitate-stimulated insulin secretion through pharmacological activation	868:1014	We identify the endoplasmic reticulum (ER) Ca2+ ATPase SERCA2 as a β cell O-GlcNAcylated protein in mice and humans that is able to rescue palmitate-stimulated insulin secretion through pharmacological activation.
32375037	4	12	theme	cell	872:875	arg1	SERCA2					858:863	the endoplasmic reticulum (ER) Ca2+ ATPase SERCA2	815:863	the endoplasmic reticulum (ER) Ca2+ ATPase SERCA2	815:863	We identify the endoplasmic reticulum (ER) Ca2+ ATPase SERCA2 as a β cell O-GlcNAcylated protein in mice and humans that is able to rescue palmitate-stimulated insulin secretion through pharmacological activation.
32375037	3	13	theme	islet	570:574	arg1	O-GlcNAcylation					576:590	islet O-GlcNAcylation	570:590	islet O-GlcNAcylation	570:590	In mice, islet O-GlcNAcylation rises and falls in tandem with the timeline of secretory potentiation during high-fat feeding while genetic models of β-cell-specific OGT loss abolish hyperinsulinemic responses to lipids, in vivo and in vitro.
32375037	0	14	theme	Secretion	68:76	arg1	Potentiation					44:55	Lipid Potentiation	38:55	Lipid Potentiation of Insulin Secretion through SERCA2	38:91	Islet O-GlcNAcylation Is Required for Lipid Potentiation of Insulin Secretion through SERCA2.
32375037	5	15	theme	common	1230:1235	arg1	factor					1242:1247	its most common risk factor	1221:1247	its most common risk factor	1221:1247	This study reveals an important physiological role for β cell O-GlcNAcylation in sensing and responding to obesity, with therapeutic implications for managing the relationship between type 2 diabetes and its most common risk factor.
32375037	0	16	theme	Islet	0:4	arg1	O-GlcNAcylation					6:20	Islet O-GlcNAcylation	0:20	Islet O-GlcNAcylation	0:20	Islet O-GlcNAcylation Is Required for Lipid Potentiation of Insulin Secretion through SERCA2.
32375037	5	17	theme	risk	1237:1240	arg1	factor					1242:1247	its most common risk factor	1221:1247	its most common risk factor	1221:1247	This study reveals an important physiological role for β cell O-GlcNAcylation in sensing and responding to obesity, with therapeutic implications for managing the relationship between type 2 diabetes and its most common risk factor.
32375037	2	18	theme	cell	320:323	arg1	modification					391:402	a nutrient-responsive post-translational protein modification	342:402	a nutrient-responsive post-translational protein modification regulated by O-GlcNAc transferase (OGT)	342:442	We find evidence that β cell O-GlcNAcylation, a nutrient-responsive post-translational protein modification regulated by O-GlcNAc transferase (OGT), is critical for coupling hyperlipidemia to β cell functional adaptation during this compensatory prediabetic phase.
32375037	2	18	theme	cell	320:323	arg1	O-GlcNAcylation					325:339	β cell O-GlcNAcylation	318:339	β cell O-GlcNAcylation	318:339	We find evidence that β cell O-GlcNAcylation, a nutrient-responsive post-translational protein modification regulated by O-GlcNAc transferase (OGT), is critical for coupling hyperlipidemia to β cell functional adaptation during this compensatory prediabetic phase.
32375037	1	19	theme	transient	187:195	arg1	phase					197:201	a transient phase	185:201	a transient phase of insulin hypersecretion that stabilizes blood glucose and forestalls diabetic progression	185:293	During early obesity, pancreatic β cells compensate for increased metabolic demand through a transient phase of insulin hypersecretion that stabilizes blood glucose and forestalls diabetic progression.
32375037	2	20	theme	coupling	461:468	arg1	hyperlipidemia					470:483	coupling hyperlipidemia	461:483	coupling hyperlipidemia	461:483	We find evidence that β cell O-GlcNAcylation, a nutrient-responsive post-translational protein modification regulated by O-GlcNAc transferase (OGT), is critical for coupling hyperlipidemia to β cell functional adaptation during this compensatory prediabetic phase.
32375037	4	21	theme	ATPase	851:856	arg1	protein					892:898	a β cell O-GlcNAcylated protein	868:898	a β cell O-GlcNAcylated protein in mice and humans that is able to rescue palmitate-stimulated insulin secretion through pharmacological activation	868:1014	We identify the endoplasmic reticulum (ER) Ca2+ ATPase SERCA2 as a β cell O-GlcNAcylated protein in mice and humans that is able to rescue palmitate-stimulated insulin secretion through pharmacological activation.
32375037	4	21	theme	ATPase	851:856	arg1	SERCA2					858:863	the endoplasmic reticulum (ER) Ca2+ ATPase SERCA2	815:863	the endoplasmic reticulum (ER) Ca2+ ATPase SERCA2	815:863	We identify the endoplasmic reticulum (ER) Ca2+ ATPase SERCA2 as a β cell O-GlcNAcylated protein in mice and humans that is able to rescue palmitate-stimulated insulin secretion through pharmacological activation.
32375037	4	22	theme	insulin	963:969	arg1	secretion					971:979	palmitate-stimulated insulin secretion	942:979	palmitate-stimulated insulin secretion	942:979	We identify the endoplasmic reticulum (ER) Ca2+ ATPase SERCA2 as a β cell O-GlcNAcylated protein in mice and humans that is able to rescue palmitate-stimulated insulin secretion through pharmacological activation.
32375037	2	23	theme	β	318:318	arg1	modification					391:402	a nutrient-responsive post-translational protein modification	342:402	a nutrient-responsive post-translational protein modification regulated by O-GlcNAc transferase (OGT)	342:442	We find evidence that β cell O-GlcNAcylation, a nutrient-responsive post-translational protein modification regulated by O-GlcNAc transferase (OGT), is critical for coupling hyperlipidemia to β cell functional adaptation during this compensatory prediabetic phase.
32375037	2	23	theme	β	318:318	arg1	O-GlcNAcylation					325:339	β cell O-GlcNAcylation	318:339	β cell O-GlcNAcylation	318:339	We find evidence that β cell O-GlcNAcylation, a nutrient-responsive post-translational protein modification regulated by O-GlcNAc transferase (OGT), is critical for coupling hyperlipidemia to β cell functional adaptation during this compensatory prediabetic phase.
32375037	3	24	with	tandem	611:616	arg1	timeline					627:634	the timeline	623:634	the timeline of secretory potentiation during high-fat feeding	623:684	In mice, islet O-GlcNAcylation rises and falls in tandem with the timeline of secretory potentiation during high-fat feeding while genetic models of β-cell-specific OGT loss abolish hyperinsulinemic responses to lipids, in vivo and in vitro.
32375037	4	25	theme	palmitate-stimulated	942:961	arg1	secretion					971:979	palmitate-stimulated insulin secretion	942:979	palmitate-stimulated insulin secretion	942:979	We identify the endoplasmic reticulum (ER) Ca2+ ATPase SERCA2 as a β cell O-GlcNAcylated protein in mice and humans that is able to rescue palmitate-stimulated insulin secretion through pharmacological activation.
32375037	3	26	theme	genetic	692:698	arg1	models					700:705	genetic models	692:705	genetic models of β-cell-specific OGT loss	692:733	In mice, islet O-GlcNAcylation rises and falls in tandem with the timeline of secretory potentiation during high-fat feeding while genetic models of β-cell-specific OGT loss abolish hyperinsulinemic responses to lipids, in vivo and in vitro.
32375037	1	27	theme	metabolic	160:168	arg1	demand					170:175	increased metabolic demand	150:175	increased metabolic demand	150:175	During early obesity, pancreatic β cells compensate for increased metabolic demand through a transient phase of insulin hypersecretion that stabilizes blood glucose and forestalls diabetic progression.
32375037	0	28	theme	Lipid	38:42	arg1	Potentiation					44:55	Lipid Potentiation	38:55	Lipid Potentiation of Insulin Secretion through SERCA2	38:91	Islet O-GlcNAcylation Is Required for Lipid Potentiation of Insulin Secretion through SERCA2.
32375037	2	29	theme	nutrient-responsive	344:362	arg1	modification					391:402	a nutrient-responsive post-translational protein modification	342:402	a nutrient-responsive post-translational protein modification regulated by O-GlcNAc transferase (OGT)	342:442	We find evidence that β cell O-GlcNAcylation, a nutrient-responsive post-translational protein modification regulated by O-GlcNAc transferase (OGT), is critical for coupling hyperlipidemia to β cell functional adaptation during this compensatory prediabetic phase.
32375037	2	29	theme	nutrient-responsive	344:362	arg1	O-GlcNAcylation					325:339	β cell O-GlcNAcylation	318:339	β cell O-GlcNAcylation	318:339	We find evidence that β cell O-GlcNAcylation, a nutrient-responsive post-translational protein modification regulated by O-GlcNAc transferase (OGT), is critical for coupling hyperlipidemia to β cell functional adaptation during this compensatory prediabetic phase.
32375037	5	30	theme	cell	1074:1077	arg1	O-GlcNAcylation					1079:1093	β cell O-GlcNAcylation	1072:1093	β cell O-GlcNAcylation	1072:1093	This study reveals an important physiological role for β cell O-GlcNAcylation in sensing and responding to obesity, with therapeutic implications for managing the relationship between type 2 diabetes and its most common risk factor.
32375037	2	31	theme	O-GlcNAc	417:424	arg1	OGT					439:441	OGT	439:441	OGT	439:441	We find evidence that β cell O-GlcNAcylation, a nutrient-responsive post-translational protein modification regulated by O-GlcNAc transferase (OGT), is critical for coupling hyperlipidemia to β cell functional adaptation during this compensatory prediabetic phase.
32375037	2	31	theme	O-GlcNAc	417:424	arg1	transferase					426:436	O-GlcNAc transferase	417:436	O-GlcNAc transferase (OGT)	417:442	We find evidence that β cell O-GlcNAcylation, a nutrient-responsive post-translational protein modification regulated by O-GlcNAc transferase (OGT), is critical for coupling hyperlipidemia to β cell functional adaptation during this compensatory prediabetic phase.
32375037	1	32	theme	insulin	206:212	arg1	hypersecretion					214:227	insulin hypersecretion	206:227	insulin hypersecretion	206:227	During early obesity, pancreatic β cells compensate for increased metabolic demand through a transient phase of insulin hypersecretion that stabilizes blood glucose and forestalls diabetic progression.
32375037	2	33	theme	functional	495:504	arg1	adaptation					506:515	cell functional adaptation	490:515	cell functional adaptation	490:515	We find evidence that β cell O-GlcNAcylation, a nutrient-responsive post-translational protein modification regulated by O-GlcNAc transferase (OGT), is critical for coupling hyperlipidemia to β cell functional adaptation during this compensatory prediabetic phase.
32375037	5	34	theme	therapeutic	1138:1148	arg1	implications					1150:1161	therapeutic implications	1138:1161	therapeutic implications for managing the relationship between type 2 diabetes and its most common risk factor	1138:1247	This study reveals an important physiological role for β cell O-GlcNAcylation in sensing and responding to obesity, with therapeutic implications for managing the relationship between type 2 diabetes and its most common risk factor.
32375037	1	35	theme	hypersecretion	214:227	arg1	phase					197:201	a transient phase	185:201	a transient phase of insulin hypersecretion that stabilizes blood glucose and forestalls diabetic progression	185:293	During early obesity, pancreatic β cells compensate for increased metabolic demand through a transient phase of insulin hypersecretion that stabilizes blood glucose and forestalls diabetic progression.
32375037	2	36	theme	cell	490:493	arg1	adaptation					506:515	cell functional adaptation	490:515	cell functional adaptation	490:515	We find evidence that β cell O-GlcNAcylation, a nutrient-responsive post-translational protein modification regulated by O-GlcNAc transferase (OGT), is critical for coupling hyperlipidemia to β cell functional adaptation during this compensatory prediabetic phase.
32375037	0	37	theme	Insulin	60:66	arg1	Secretion					68:76	Insulin Secretion	60:76	Insulin Secretion through SERCA2	60:91	Islet O-GlcNAcylation Is Required for Lipid Potentiation of Insulin Secretion through SERCA2.
32375037	4	38	theme	β	870:870	arg1	protein					892:898	a β cell O-GlcNAcylated protein	868:898	a β cell O-GlcNAcylated protein in mice and humans that is able to rescue palmitate-stimulated insulin secretion through pharmacological activation	868:1014	We identify the endoplasmic reticulum (ER) Ca2+ ATPase SERCA2 as a β cell O-GlcNAcylated protein in mice and humans that is able to rescue palmitate-stimulated insulin secretion through pharmacological activation.
32375037	4	38	theme	β	870:870	arg1	SERCA2					858:863	the endoplasmic reticulum (ER) Ca2+ ATPase SERCA2	815:863	the endoplasmic reticulum (ER) Ca2+ ATPase SERCA2	815:863	We identify the endoplasmic reticulum (ER) Ca2+ ATPase SERCA2 as a β cell O-GlcNAcylated protein in mice and humans that is able to rescue palmitate-stimulated insulin secretion through pharmacological activation.
32375037	2	39	theme	post-translational	364:381	arg1	modification					391:402	a nutrient-responsive post-translational protein modification	342:402	a nutrient-responsive post-translational protein modification regulated by O-GlcNAc transferase (OGT)	342:442	We find evidence that β cell O-GlcNAcylation, a nutrient-responsive post-translational protein modification regulated by O-GlcNAc transferase (OGT), is critical for coupling hyperlipidemia to β cell functional adaptation during this compensatory prediabetic phase.
32375037	2	39	theme	post-translational	364:381	arg1	O-GlcNAcylation					325:339	β cell O-GlcNAcylation	318:339	β cell O-GlcNAcylation	318:339	We find evidence that β cell O-GlcNAcylation, a nutrient-responsive post-translational protein modification regulated by O-GlcNAc transferase (OGT), is critical for coupling hyperlipidemia to β cell functional adaptation during this compensatory prediabetic phase.
32375037	3	40	theme	OGT	726:728	arg1	loss					730:733	β-cell-specific OGT loss	710:733	β-cell-specific OGT loss	710:733	In mice, islet O-GlcNAcylation rises and falls in tandem with the timeline of secretory potentiation during high-fat feeding while genetic models of β-cell-specific OGT loss abolish hyperinsulinemic responses to lipids, in vivo and in vitro.
32375037	1	41	theme	pancreatic	116:125	arg1	cells					129:133	pancreatic β cells	116:133	pancreatic β cells	116:133	During early obesity, pancreatic β cells compensate for increased metabolic demand through a transient phase of insulin hypersecretion that stabilizes blood glucose and forestalls diabetic progression.
32375037	4	42	theme	Ca2+	846:849	arg1	protein					892:898	a β cell O-GlcNAcylated protein	868:898	a β cell O-GlcNAcylated protein in mice and humans that is able to rescue palmitate-stimulated insulin secretion through pharmacological activation	868:1014	We identify the endoplasmic reticulum (ER) Ca2+ ATPase SERCA2 as a β cell O-GlcNAcylated protein in mice and humans that is able to rescue palmitate-stimulated insulin secretion through pharmacological activation.
32375037	4	42	theme	Ca2+	846:849	arg1	SERCA2					858:863	the endoplasmic reticulum (ER) Ca2+ ATPase SERCA2	815:863	the endoplasmic reticulum (ER) Ca2+ ATPase SERCA2	815:863	We identify the endoplasmic reticulum (ER) Ca2+ ATPase SERCA2 as a β cell O-GlcNAcylated protein in mice and humans that is able to rescue palmitate-stimulated insulin secretion through pharmacological activation.
32375037	3	43	theme	loss	730:733	arg1	models					700:705	genetic models	692:705	genetic models of β-cell-specific OGT loss	692:733	In mice, islet O-GlcNAcylation rises and falls in tandem with the timeline of secretory potentiation during high-fat feeding while genetic models of β-cell-specific OGT loss abolish hyperinsulinemic responses to lipids, in vivo and in vitro.
32375037	1	44	theme	β	127:127	arg1	cells					129:133	pancreatic β cells	116:133	pancreatic β cells	116:133	During early obesity, pancreatic β cells compensate for increased metabolic demand through a transient phase of insulin hypersecretion that stabilizes blood glucose and forestalls diabetic progression.
32375037	1	45	theme	early	101:105	arg1	obesity					107:113	early obesity	101:113	early obesity	101:113	During early obesity, pancreatic β cells compensate for increased metabolic demand through a transient phase of insulin hypersecretion that stabilizes blood glucose and forestalls diabetic progression.
32375037	4	46	theme	reticulum	831:839	arg1	protein					892:898	a β cell O-GlcNAcylated protein	868:898	a β cell O-GlcNAcylated protein in mice and humans that is able to rescue palmitate-stimulated insulin secretion through pharmacological activation	868:1014	We identify the endoplasmic reticulum (ER) Ca2+ ATPase SERCA2 as a β cell O-GlcNAcylated protein in mice and humans that is able to rescue palmitate-stimulated insulin secretion through pharmacological activation.
32375037	4	46	theme	reticulum	831:839	arg1	SERCA2					858:863	the endoplasmic reticulum (ER) Ca2+ ATPase SERCA2	815:863	the endoplasmic reticulum (ER) Ca2+ ATPase SERCA2	815:863	We identify the endoplasmic reticulum (ER) Ca2+ ATPase SERCA2 as a β cell O-GlcNAcylated protein in mice and humans that is able to rescue palmitate-stimulated insulin secretion through pharmacological activation.
32375037	3	47	theme	high-fat	669:676	arg1	feeding					678:684	high-fat feeding	669:684	high-fat feeding	669:684	In mice, islet O-GlcNAcylation rises and falls in tandem with the timeline of secretory potentiation during high-fat feeding while genetic models of β-cell-specific OGT loss abolish hyperinsulinemic responses to lipids, in vivo and in vitro.
32375037	2	48	theme	prediabetic	542:552	arg1	phase					554:558	this compensatory prediabetic phase	524:558	this compensatory prediabetic phase	524:558	We find evidence that β cell O-GlcNAcylation, a nutrient-responsive post-translational protein modification regulated by O-GlcNAc transferase (OGT), is critical for coupling hyperlipidemia to β cell functional adaptation during this compensatory prediabetic phase.
32375037	3	49	theme	β-cell-specific	710:724	arg1	loss					730:733	β-cell-specific OGT loss	710:733	β-cell-specific OGT loss	710:733	In mice, islet O-GlcNAcylation rises and falls in tandem with the timeline of secretory potentiation during high-fat feeding while genetic models of β-cell-specific OGT loss abolish hyperinsulinemic responses to lipids, in vivo and in vitro.
32375037	3	50	theme	secretory	639:647	arg1	potentiation					649:660	secretory potentiation	639:660	secretory potentiation	639:660	In mice, islet O-GlcNAcylation rises and falls in tandem with the timeline of secretory potentiation during high-fat feeding while genetic models of β-cell-specific OGT loss abolish hyperinsulinemic responses to lipids, in vivo and in vitro.
32375037	1	51	theme	blood	245:249	arg1	glucose					251:257	blood glucose	245:257	blood glucose	245:257	During early obesity, pancreatic β cells compensate for increased metabolic demand through a transient phase of insulin hypersecretion that stabilizes blood glucose and forestalls diabetic progression.
32375037	2	52	theme	compensatory	529:540	arg1	phase					554:558	this compensatory prediabetic phase	524:558	this compensatory prediabetic phase	524:558	We find evidence that β cell O-GlcNAcylation, a nutrient-responsive post-translational protein modification regulated by O-GlcNAc transferase (OGT), is critical for coupling hyperlipidemia to β cell functional adaptation during this compensatory prediabetic phase.
32375037	3	53	theme	potentiation	649:660	arg1	timeline					627:634	the timeline	623:634	the timeline of secretory potentiation during high-fat feeding	623:684	In mice, islet O-GlcNAcylation rises and falls in tandem with the timeline of secretory potentiation during high-fat feeding while genetic models of β-cell-specific OGT loss abolish hyperinsulinemic responses to lipids, in vivo and in vitro.
30484950	0	0	theme	catcinogenic	101:112	arg1	function					114:121	potential catcinogenic function	91:121	potential catcinogenic function	91:121	O-GlcNAcylation promotes colorectal cancer progression by regulating protein stability and potential catcinogenic function of DDX5.
30484950	7	1	theme	pathway	968:974	arg1	activation					930:939	activation	930:939	activation of the AKT/mTOR signalling pathway	930:974	The OGT-DDX5 axis affects colorectal cancer progression mainly by regulating activation of the AKT/mTOR signalling pathway.
30484950	7	2	theme	OGT-DDX5	857:864	arg1	axis					866:869	The OGT-DDX5 axis	853:869	The OGT-DDX5 axis	853:869	The OGT-DDX5 axis affects colorectal cancer progression mainly by regulating activation of the AKT/mTOR signalling pathway.
30484950	5	3	from	OGT	687:689	arg1	enzyme					739:744	the only known enzyme	724:744	the only known enzyme that catalyses O-GlcNAcylation in humans	724:785	Here we show that DDX5 interacts directly with OGT in the SW480 cell line, which is the only known enzyme that catalyses O-GlcNAcylation in humans.
30484950	5	3	from	OGT	687:689	arg1	line					709:712	the SW480 cell line	694:712	the SW480 cell line	694:712	Here we show that DDX5 interacts directly with OGT in the SW480 cell line, which is the only known enzyme that catalyses O-GlcNAcylation in humans.
30484950	0	4	theme	potential	91:99	arg1	function					114:121	potential catcinogenic function	91:121	potential catcinogenic function	91:121	O-GlcNAcylation promotes colorectal cancer progression by regulating protein stability and potential catcinogenic function of DDX5.
30484950	9	5	theme	OGT-DDX5	1310:1317	arg1	axis					1319:1322	the OGT-DDX5 axis	1306:1322	the OGT-DDX5 axis	1306:1322	This study not only reveals the novel functional of O-GlcNAcylation in regulating DDX5, but also reveals the carcinogenic effect of the OGT-DDX5 axis in colorectal cancer.
30484950	7	6	theme	AKT/mTOR	948:955	arg1	pathway					968:974	the AKT/mTOR signalling pathway	944:974	the AKT/mTOR signalling pathway	944:974	The OGT-DDX5 axis affects colorectal cancer progression mainly by regulating activation of the AKT/mTOR signalling pathway.
30484950	4	7	mod	modification	592:603	arg1	DDX5					618:621	DDX5	618:621	DDX5	618:621	Although it was known DDX5 protein could be regulated by post-translational modification (PTM), how O-GlcNAcylation modification regulated of DDX5 remains unclear.
30484950	4	7	mod	modification	592:603	arg3	O-GlcNAcylation					576:590	O-GlcNAcylation modification regulated	576:613	O-GlcNAcylation modification regulated of DDX5	576:621	Although it was known DDX5 protein could be regulated by post-translational modification (PTM), how O-GlcNAcylation modification regulated of DDX5 remains unclear.
30484950	9	8	theme	axis	1319:1322	arg1	effect					1296:1301	the carcinogenic effect	1279:1301	the carcinogenic effect of the OGT-DDX5 axis in colorectal cancer	1279:1343	This study not only reveals the novel functional of O-GlcNAcylation in regulating DDX5, but also reveals the carcinogenic effect of the OGT-DDX5 axis in colorectal cancer.
30484950	8	9	theme	OGT-mediated	1022:1033	arg1	O-GlcNAcylation					1035:1049	OGT-mediated O-GlcNAcylation	1022:1049	OGT-mediated O-GlcNAcylation	1022:1049	Taken together, these results indicated that OGT-mediated O-GlcNAcylation stabilizes DDX5, promoting activation of the AKT/mTOR signalling pathway, thus accelerating colorectal cancer progression.
30484950	5	10	theme	cell	704:707	arg1	enzyme					739:744	the only known enzyme	724:744	the only known enzyme that catalyses O-GlcNAcylation in humans	724:785	Here we show that DDX5 interacts directly with OGT in the SW480 cell line, which is the only known enzyme that catalyses O-GlcNAcylation in humans.
30484950	5	10	theme	cell	704:707	arg1	line					709:712	the SW480 cell line	694:712	the SW480 cell line	694:712	Here we show that DDX5 interacts directly with OGT in the SW480 cell line, which is the only known enzyme that catalyses O-GlcNAcylation in humans.
30484950	0	11	theme	DDX5	126:129	arg1	stability					77:85	protein stability	69:85	protein stability	69:85	O-GlcNAcylation promotes colorectal cancer progression by regulating protein stability and potential catcinogenic function of DDX5.
30484950	0	11	theme	DDX5	126:129	arg1	function					114:121	potential catcinogenic function	91:121	potential catcinogenic function	91:121	O-GlcNAcylation promotes colorectal cancer progression by regulating protein stability and potential catcinogenic function of DDX5.
30484950	9	12	theme	colorectal	1327:1336	arg1	cancer					1338:1343	colorectal cancer	1327:1343	colorectal cancer	1327:1343	This study not only reveals the novel functional of O-GlcNAcylation in regulating DDX5, but also reveals the carcinogenic effect of the OGT-DDX5 axis in colorectal cancer.
30484950	1	13	theme	key	163:165	arg1	player					167:172	a key player	161:172	a key player in RNA metabolism	161:190	The RNA helicase p68 (DDX5), a key player in RNA metabolism, belongs to the DEAD box family and is involved in the development of colorectal cancer.
30484950	1	13	theme	key	163:165	arg1	p68					149:151	The RNA helicase p68	132:151	The RNA helicase p68 (DDX5)	132:158	The RNA helicase p68 (DDX5), a key player in RNA metabolism, belongs to the DEAD box family and is involved in the development of colorectal cancer.
30484950	5	14	from	O-GlcNAcylation	761:775	arg1	humans					780:785	humans	780:785	humans	780:785	Here we show that DDX5 interacts directly with OGT in the SW480 cell line, which is the only known enzyme that catalyses O-GlcNAcylation in humans.
30484950	3	15	theme	DDX5	378:381	arg1	level					391:395	DDX5 protein level	378:395	DDX5 protein level	378:395	In addition, DDX5 protein level is significantly positively correlated with the expression of O-GlcNAcylation.
30484950	9	16	theme	O-GlcNAcylation	1226:1240	arg1	functional					1212:1221	functional	1212:1221	functional	1212:1221	This study not only reveals the novel functional of O-GlcNAcylation in regulating DDX5, but also reveals the carcinogenic effect of the OGT-DDX5 axis in colorectal cancer.
30484950	3	17	theme	protein	383:389	arg1	level					391:395	DDX5 protein level	378:395	DDX5 protein level	378:395	In addition, DDX5 protein level is significantly positively correlated with the expression of O-GlcNAcylation.
30484950	0	18	theme	cancer	36:41	arg1	progression					43:53	colorectal cancer progression	25:53	colorectal cancer progression	25:53	O-GlcNAcylation promotes colorectal cancer progression by regulating protein stability and potential catcinogenic function of DDX5.
30484950	2	19	gly	O-GlcNAcylation	310:324	arg1	cancer					357:362	colorectal cancer	346:362	colorectal cancer	346:362	Here, we found both DDX5 and O-GlcNAcylation are up-regulated in colorectal cancer.
30484950	1	20	theme	RNA	177:179	arg1	metabolism					181:190	RNA metabolism	177:190	RNA metabolism	177:190	The RNA helicase p68 (DDX5), a key player in RNA metabolism, belongs to the DEAD box family and is involved in the development of colorectal cancer.
30484950	0	21	theme	colorectal	25:34	arg1	progression					43:53	colorectal cancer progression	25:53	colorectal cancer progression	25:53	O-GlcNAcylation promotes colorectal cancer progression by regulating protein stability and potential catcinogenic function of DDX5.
30484950	4	22	theme	post-translational	533:550	arg1	PTM					566:568	PTM	566:568	PTM	566:568	Although it was known DDX5 protein could be regulated by post-translational modification (PTM), how O-GlcNAcylation modification regulated of DDX5 remains unclear.
30484950	4	22	theme	post-translational	533:550	arg1	modification					552:563	post-translational modification	533:563	post-translational modification (PTM)	533:569	Although it was known DDX5 protein could be regulated by post-translational modification (PTM), how O-GlcNAcylation modification regulated of DDX5 remains unclear.
30484950	6	23	theme	protein	834:840	arg1	stability					842:850	DDX5 protein stability	829:850	DDX5 protein stability	829:850	Meanwhile, O-GlcNAcylation could promote DDX5 protein stability.
30484950	4	24	theme	regulated	605:613	arg1	modification					592:603	O-GlcNAcylation modification regulated	576:613	O-GlcNAcylation modification regulated of DDX5	576:621	Although it was known DDX5 protein could be regulated by post-translational modification (PTM), how O-GlcNAcylation modification regulated of DDX5 remains unclear.
30484950	3	25	theme	O-GlcNAcylation	459:473	arg1	expression					445:454	the expression	441:454	the expression of O-GlcNAcylation	441:473	In addition, DDX5 protein level is significantly positively correlated with the expression of O-GlcNAcylation.
30484950	8	26	theme	AKT/mTOR	1096:1103	arg1	pathway					1116:1122	the AKT/mTOR signalling pathway	1092:1122	the AKT/mTOR signalling pathway	1092:1122	Taken together, these results indicated that OGT-mediated O-GlcNAcylation stabilizes DDX5, promoting activation of the AKT/mTOR signalling pathway, thus accelerating colorectal cancer progression.
30484950	6	27	theme	DDX5	829:832	arg1	stability					842:850	DDX5 protein stability	829:850	DDX5 protein stability	829:850	Meanwhile, O-GlcNAcylation could promote DDX5 protein stability.
30484950	5	28	theme	known	733:737	arg1	enzyme					739:744	the only known enzyme	724:744	the only known enzyme that catalyses O-GlcNAcylation in humans	724:785	Here we show that DDX5 interacts directly with OGT in the SW480 cell line, which is the only known enzyme that catalyses O-GlcNAcylation in humans.
30484950	5	28	theme	known	733:737	arg1	line					709:712	the SW480 cell line	694:712	the SW480 cell line	694:712	Here we show that DDX5 interacts directly with OGT in the SW480 cell line, which is the only known enzyme that catalyses O-GlcNAcylation in humans.
30484950	1	29	theme	colorectal	262:271	arg1	cancer					273:278	colorectal cancer	262:278	colorectal cancer	262:278	The RNA helicase p68 (DDX5), a key player in RNA metabolism, belongs to the DEAD box family and is involved in the development of colorectal cancer.
30484950	8	30	theme	cancer	1154:1159	arg1	progression					1161:1171	colorectal cancer progression	1143:1171	colorectal cancer progression	1143:1171	Taken together, these results indicated that OGT-mediated O-GlcNAcylation stabilizes DDX5, promoting activation of the AKT/mTOR signalling pathway, thus accelerating colorectal cancer progression.
30484950	4	31	theme	DDX5	618:621	arg1	modification					592:603	O-GlcNAcylation modification regulated	576:613	O-GlcNAcylation modification regulated of DDX5	576:621	Although it was known DDX5 protein could be regulated by post-translational modification (PTM), how O-GlcNAcylation modification regulated of DDX5 remains unclear.
30484950	0	32	theme	protein	69:75	arg1	stability					77:85	protein stability	69:85	protein stability	69:85	O-GlcNAcylation promotes colorectal cancer progression by regulating protein stability and potential catcinogenic function of DDX5.
30484950	1	33	theme	cancer	273:278	arg1	development					247:257	the development	243:257	the development of colorectal cancer	243:278	The RNA helicase p68 (DDX5), a key player in RNA metabolism, belongs to the DEAD box family and is involved in the development of colorectal cancer.
30484950	8	34	theme	pathway	1116:1122	arg1	activation					1078:1087	activation	1078:1087	activation of the AKT/mTOR signalling pathway	1078:1122	Taken together, these results indicated that OGT-mediated O-GlcNAcylation stabilizes DDX5, promoting activation of the AKT/mTOR signalling pathway, thus accelerating colorectal cancer progression.
30484950	4	35	theme	DDX5	498:501	arg1	protein					503:509	DDX5 protein	498:509	DDX5 protein	498:509	Although it was known DDX5 protein could be regulated by post-translational modification (PTM), how O-GlcNAcylation modification regulated of DDX5 remains unclear.
30484950	8	36	theme	signalling	1105:1114	arg1	pathway					1116:1122	the AKT/mTOR signalling pathway	1092:1122	the AKT/mTOR signalling pathway	1092:1122	Taken together, these results indicated that OGT-mediated O-GlcNAcylation stabilizes DDX5, promoting activation of the AKT/mTOR signalling pathway, thus accelerating colorectal cancer progression.
30484950	1	37	theme	RNA	136:138	arg1	player					167:172	a key player	161:172	a key player in RNA metabolism	161:190	The RNA helicase p68 (DDX5), a key player in RNA metabolism, belongs to the DEAD box family and is involved in the development of colorectal cancer.
30484950	1	37	theme	RNA	136:138	arg1	DDX5					154:157	DDX5	154:157	DDX5	154:157	The RNA helicase p68 (DDX5), a key player in RNA metabolism, belongs to the DEAD box family and is involved in the development of colorectal cancer.
30484950	1	37	theme	RNA	136:138	arg1	p68					149:151	The RNA helicase p68	132:151	The RNA helicase p68 (DDX5)	132:158	The RNA helicase p68 (DDX5), a key player in RNA metabolism, belongs to the DEAD box family and is involved in the development of colorectal cancer.
30484950	7	38	theme	colorectal	879:888	arg1	progression					897:907	colorectal cancer progression	879:907	colorectal cancer progression	879:907	The OGT-DDX5 axis affects colorectal cancer progression mainly by regulating activation of the AKT/mTOR signalling pathway.
30484950	1	39	theme	helicase	140:147	arg1	player					167:172	a key player	161:172	a key player in RNA metabolism	161:190	The RNA helicase p68 (DDX5), a key player in RNA metabolism, belongs to the DEAD box family and is involved in the development of colorectal cancer.
30484950	1	39	theme	helicase	140:147	arg1	DDX5					154:157	DDX5	154:157	DDX5	154:157	The RNA helicase p68 (DDX5), a key player in RNA metabolism, belongs to the DEAD box family and is involved in the development of colorectal cancer.
30484950	1	39	theme	helicase	140:147	arg1	p68					149:151	The RNA helicase p68	132:151	The RNA helicase p68 (DDX5)	132:158	The RNA helicase p68 (DDX5), a key player in RNA metabolism, belongs to the DEAD box family and is involved in the development of colorectal cancer.
30484950	7	40	theme	cancer	890:895	arg1	progression					897:907	colorectal cancer progression	879:907	colorectal cancer progression	879:907	The OGT-DDX5 axis affects colorectal cancer progression mainly by regulating activation of the AKT/mTOR signalling pathway.
30484950	1	41	from	player	167:172	arg1	metabolism					181:190	RNA metabolism	177:190	RNA metabolism	177:190	The RNA helicase p68 (DDX5), a key player in RNA metabolism, belongs to the DEAD box family and is involved in the development of colorectal cancer.
30484950	8	42	theme	colorectal	1143:1152	arg1	cancer					1154:1159	colorectal cancer	1143:1159	colorectal cancer progression	1143:1171	Taken together, these results indicated that OGT-mediated O-GlcNAcylation stabilizes DDX5, promoting activation of the AKT/mTOR signalling pathway, thus accelerating colorectal cancer progression.
30484950	9	43	theme	carcinogenic	1283:1294	arg1	effect					1296:1301	the carcinogenic effect	1279:1301	the carcinogenic effect of the OGT-DDX5 axis in colorectal cancer	1279:1343	This study not only reveals the novel functional of O-GlcNAcylation in regulating DDX5, but also reveals the carcinogenic effect of the OGT-DDX5 axis in colorectal cancer.
30484950	2	44	theme	colorectal	346:355	arg1	cancer					357:362	colorectal cancer	346:362	colorectal cancer	346:362	Here, we found both DDX5 and O-GlcNAcylation are up-regulated in colorectal cancer.
30484950	1	45	theme	DEAD	208:211	arg1	family					217:222	the DEAD box family	204:222	the DEAD box family	204:222	The RNA helicase p68 (DDX5), a key player in RNA metabolism, belongs to the DEAD box family and is involved in the development of colorectal cancer.
30484950	9	46	from	effect	1296:1301	arg1	cancer					1338:1343	colorectal cancer	1327:1343	colorectal cancer	1327:1343	This study not only reveals the novel functional of O-GlcNAcylation in regulating DDX5, but also reveals the carcinogenic effect of the OGT-DDX5 axis in colorectal cancer.
30484950	1	47	theme	box	213:215	arg1	family					217:222	the DEAD box family	204:222	the DEAD box family	204:222	The RNA helicase p68 (DDX5), a key player in RNA metabolism, belongs to the DEAD box family and is involved in the development of colorectal cancer.
30484950	7	48	theme	signalling	957:966	arg1	pathway					968:974	the AKT/mTOR signalling pathway	944:974	the AKT/mTOR signalling pathway	944:974	The OGT-DDX5 axis affects colorectal cancer progression mainly by regulating activation of the AKT/mTOR signalling pathway.
30484950	4	49	theme	O-GlcNAcylation	576:590	arg1	modification					592:603	O-GlcNAcylation modification regulated	576:613	O-GlcNAcylation modification regulated of DDX5	576:621	Although it was known DDX5 protein could be regulated by post-translational modification (PTM), how O-GlcNAcylation modification regulated of DDX5 remains unclear.
35183508	7	0	from	changes	1126:1132	arg1	levels					1146:1151	O-GlcNAc levels	1137:1151	O-GlcNAc levels	1137:1151	In this study, we also show that galectin 3 secretion is sensitive to changes in O-GlcNAc levels.
35183508	1	1	theme	nutrient	198:205	arg1	sensing					207:213	nutrient sensing	198:213	nutrient sensing	198:213	Endomembrane glycosylation and cytoplasmic O-GlcNAcylation each play essential roles in nutrient sensing, and characteristic changes in glycan patterns have been described in disease states such as diabetes and cancer.
35183508	2	2	from	changes	335:341	arg1	glycosylation					346:358	glycosylation	346:358	glycosylation	346:358	These changes in glycosylation have important functional roles and can drive disease progression.
35183508	6	3	theme	O-GlcNAc	1034:1041	arg1	transferase					1043:1053	O-GlcNAc transferase	1034:1053	O-GlcNAc transferase	1034:1053	Originating in the cytoplasm, galectins are predicted substrates for O-GlcNAc addition and removal; and as we have shown, galectin 3 is a substrate for O-GlcNAc transferase.
35183508	9	4	theme	galectin	1361:1368	arg1	secretion					1372:1380	galectin 3 secretion	1361:1380	galectin 3 secretion	1361:1380	We observed dramatic alterations in galectin 3 secretion in response to nutrient conditions, which were dependent on dynamic O-GlcNAcylation.
35183508	7	5	theme	O-GlcNAc	1137:1144	arg1	levels					1146:1151	O-GlcNAc levels	1137:1151	O-GlcNAc levels	1137:1151	In this study, we also show that galectin 3 secretion is sensitive to changes in O-GlcNAc levels.
35183508	1	6	dep	play	174:177	arg1	each					169:172	each	169:172	each	169:172	Endomembrane glycosylation and cytoplasmic O-GlcNAcylation each play essential roles in nutrient sensing, and characteristic changes in glycan patterns have been described in disease states such as diabetes and cancer.
35183508	4	7	theme	characterized	642:654	arg1	mechanism					679:687	a poorly characterized nonclassical secretory mechanism	633:687	a poorly characterized nonclassical secretory mechanism	633:687	Galectins are proteins that bind glycans and that are secreted by a poorly characterized nonclassical secretory mechanism.
35183508	8	8	theme	Western	1198:1204	arg1	blotting					1206:1213	Western blotting	1198:1213	Western blotting	1198:1213	We determined using immunoprecipitation and Western blotting that there is a significant difference in O-GlcNAcylation status between cytoplasmic and secreted galectin 3.
35183508	2	9	theme	important	365:373	arg1	roles					386:390	important functional roles	365:390	important functional roles	365:390	These changes in glycosylation have important functional roles and can drive disease progression.
35183508	5	10	theme	numerous	800:807	arg1	endocytosis					863:873	clathrin-independent endocytosis	842:873	clathrin-independent endocytosis (CIE)	842:879	Once outside the cell, galectins bind to the terminal galactose residues of cell surface glycans and modulate numerous extracellular functions, such as clathrin-independent endocytosis (CIE).
35183508	5	10	theme	numerous	800:807	arg1	functions					823:831	numerous extracellular functions	800:831	numerous extracellular functions	800:831	Once outside the cell, galectins bind to the terminal galactose residues of cell surface glycans and modulate numerous extracellular functions, such as clathrin-independent endocytosis (CIE).
35183508	1	11	theme	characteristic	220:233	arg1	changes					235:241	characteristic changes	220:241	characteristic changes in glycan patterns	220:260	Endomembrane glycosylation and cytoplasmic O-GlcNAcylation each play essential roles in nutrient sensing, and characteristic changes in glycan patterns have been described in disease states such as diabetes and cancer.
35183508	10	12	theme	nutrient-sensing	1734:1749	arg1	information					1751:1761	nutrient-sensing information	1734:1761	nutrient-sensing information coded in cell surface glycosylation	1734:1797	Importantly, we showed that these O-GlcNAc-driven alterations in galectin 3 secretion also facilitated changes in CIE. These results indicate that dynamic O-GlcNAcylation of galectin 3 plays a role in modulating its secretion and can tune its function in transducing nutrient-sensing information coded in cell surface glycosylation into biological effects.
35183508	5	13	theme	extracellular	809:821	arg1	endocytosis					863:873	clathrin-independent endocytosis	842:873	clathrin-independent endocytosis (CIE)	842:879	Once outside the cell, galectins bind to the terminal galactose residues of cell surface glycans and modulate numerous extracellular functions, such as clathrin-independent endocytosis (CIE).
35183508	5	13	theme	extracellular	809:821	arg1	functions					823:831	numerous extracellular functions	800:831	numerous extracellular functions	800:831	Once outside the cell, galectins bind to the terminal galactose residues of cell surface glycans and modulate numerous extracellular functions, such as clathrin-independent endocytosis (CIE).
35183508	8	14	theme	O-GlcNAcylation	1257:1271	arg1	status					1273:1278	O-GlcNAcylation status	1257:1278	O-GlcNAcylation status	1257:1278	We determined using immunoprecipitation and Western blotting that there is a significant difference in O-GlcNAcylation status between cytoplasmic and secreted galectin 3.
35183508	10	15	theme	surface	1777:1783	arg1	glycosylation					1785:1797	cell surface glycosylation	1772:1797	cell surface glycosylation	1772:1797	Importantly, we showed that these O-GlcNAc-driven alterations in galectin 3 secretion also facilitated changes in CIE. These results indicate that dynamic O-GlcNAcylation of galectin 3 plays a role in modulating its secretion and can tune its function in transducing nutrient-sensing information coded in cell surface glycosylation into biological effects.
35183508	8	16	theme	cytoplasmic	1288:1298	arg1	galectin					1313:1320	cytoplasmic and secreted galectin 3	1288:1322	cytoplasmic and secreted galectin 3	1288:1322	We determined using immunoprecipitation and Western blotting that there is a significant difference in O-GlcNAcylation status between cytoplasmic and secreted galectin 3.
35183508	6	17	theme	O-GlcNAc	951:958	arg1	addition					960:967	O-GlcNAc addition	951:967	O-GlcNAc addition	951:967	Originating in the cytoplasm, galectins are predicted substrates for O-GlcNAc addition and removal; and as we have shown, galectin 3 is a substrate for O-GlcNAc transferase.
35183508	9	18	dep	conditions	1406:1415	arg1	response					1385:1392	response	1385:1392	response	1385:1392	We observed dramatic alterations in galectin 3 secretion in response to nutrient conditions, which were dependent on dynamic O-GlcNAcylation.
35183508	1	19	theme	Endomembrane	110:121	arg1	glycosylation					123:135	Endomembrane glycosylation	110:135	Endomembrane glycosylation	110:135	Endomembrane glycosylation and cytoplasmic O-GlcNAcylation each play essential roles in nutrient sensing, and characteristic changes in glycan patterns have been described in disease states such as diabetes and cancer.
35183508	3	20	theme	molecular	462:470	arg1	mechanisms					472:481	the molecular mechanisms	458:481	the molecular mechanisms underlying how these signals are integrated and transduced into biological effects	458:564	However, little is known about the molecular mechanisms underlying how these signals are integrated and transduced into biological effects.
35183508	0	21	theme	Nutrient-responsive	0:18	arg1	O-GlcNAcylation					20:34	Nutrient-responsive O-GlcNAcylation	0:34	Nutrient-responsive O-GlcNAcylation	0:34	Nutrient-responsive O-GlcNAcylation dynamically modulates the secretion of glycan-binding protein galectin 3.
35183508	10	22	theme	galectin	1532:1539	arg1	secretion					1543:1551	galectin 3 secretion	1532:1551	galectin 3 secretion	1532:1551	Importantly, we showed that these O-GlcNAc-driven alterations in galectin 3 secretion also facilitated changes in CIE. These results indicate that dynamic O-GlcNAcylation of galectin 3 plays a role in modulating its secretion and can tune its function in transducing nutrient-sensing information coded in cell surface glycosylation into biological effects.
35183508	9	23	theme	dramatic	1337:1344	arg1	alterations					1346:1356	dramatic alterations	1337:1356	dramatic alterations in galectin 3 secretion	1337:1380	We observed dramatic alterations in galectin 3 secretion in response to nutrient conditions, which were dependent on dynamic O-GlcNAcylation.
35183508	8	24	theme	secreted	1304:1311	arg1	galectin					1313:1320	cytoplasmic and secreted galectin 3	1288:1322	cytoplasmic and secreted galectin 3	1288:1322	We determined using immunoprecipitation and Western blotting that there is a significant difference in O-GlcNAcylation status between cytoplasmic and secreted galectin 3.
35183508	9	25	theme	nutrient	1397:1404	arg1	conditions					1406:1415	nutrient conditions	1397:1415	nutrient conditions	1397:1415	We observed dramatic alterations in galectin 3 secretion in response to nutrient conditions, which were dependent on dynamic O-GlcNAcylation.
35183508	10	26	theme	O-GlcNAc-driven	1501:1515	arg1	alterations					1517:1527	these O-GlcNAc-driven alterations	1495:1527	these O-GlcNAc-driven alterations in galectin 3 secretion	1495:1551	Importantly, we showed that these O-GlcNAc-driven alterations in galectin 3 secretion also facilitated changes in CIE. These results indicate that dynamic O-GlcNAcylation of galectin 3 plays a role in modulating its secretion and can tune its function in transducing nutrient-sensing information coded in cell surface glycosylation into biological effects.
35183508	10	27	theme	cell	1772:1775	arg1	glycosylation					1785:1797	cell surface glycosylation	1772:1797	cell surface glycosylation	1772:1797	Importantly, we showed that these O-GlcNAc-driven alterations in galectin 3 secretion also facilitated changes in CIE. These results indicate that dynamic O-GlcNAcylation of galectin 3 plays a role in modulating its secretion and can tune its function in transducing nutrient-sensing information coded in cell surface glycosylation into biological effects.
35183508	8	28	theme	significant	1231:1241	arg1	difference					1243:1252	a significant difference	1229:1252	a significant difference in O-GlcNAcylation status between cytoplasmic and secreted galectin 3	1229:1322	We determined using immunoprecipitation and Western blotting that there is a significant difference in O-GlcNAcylation status between cytoplasmic and secreted galectin 3.
35183508	7	29	theme	galectin	1089:1096	arg1	secretion					1100:1108	galectin 3 secretion	1089:1108	galectin 3 secretion	1089:1108	In this study, we also show that galectin 3 secretion is sensitive to changes in O-GlcNAc levels.
35183508	5	30	theme	cell	766:769	arg1	glycans					779:785	cell surface glycans	766:785	cell surface glycans	766:785	Once outside the cell, galectins bind to the terminal galactose residues of cell surface glycans and modulate numerous extracellular functions, such as clathrin-independent endocytosis (CIE).
35183508	1	31	theme	cytoplasmic	141:151	arg1	O-GlcNAcylation					153:167	cytoplasmic O-GlcNAcylation	141:167	cytoplasmic O-GlcNAcylation	141:167	Endomembrane glycosylation and cytoplasmic O-GlcNAcylation each play essential roles in nutrient sensing, and characteristic changes in glycan patterns have been described in disease states such as diabetes and cancer.
35183508	1	32	theme	glycan	246:251	arg1	patterns					253:260	glycan patterns	246:260	glycan patterns	246:260	Endomembrane glycosylation and cytoplasmic O-GlcNAcylation each play essential roles in nutrient sensing, and characteristic changes in glycan patterns have been described in disease states such as diabetes and cancer.
35183508	5	33	theme	clathrin-independent	842:861	arg1	CIE					876:878	CIE	876:878	CIE	876:878	Once outside the cell, galectins bind to the terminal galactose residues of cell surface glycans and modulate numerous extracellular functions, such as clathrin-independent endocytosis (CIE).
35183508	5	33	theme	clathrin-independent	842:861	arg1	endocytosis					863:873	clathrin-independent endocytosis	842:873	clathrin-independent endocytosis (CIE)	842:879	Once outside the cell, galectins bind to the terminal galactose residues of cell surface glycans and modulate numerous extracellular functions, such as clathrin-independent endocytosis (CIE).
35183508	10	34	from	alterations	1517:1527	arg1	secretion					1543:1551	galectin 3 secretion	1532:1551	galectin 3 secretion	1532:1551	Importantly, we showed that these O-GlcNAc-driven alterations in galectin 3 secretion also facilitated changes in CIE. These results indicate that dynamic O-GlcNAcylation of galectin 3 plays a role in modulating its secretion and can tune its function in transducing nutrient-sensing information coded in cell surface glycosylation into biological effects.
35183508	5	35	theme	surface	771:777	arg1	glycans					779:785	cell surface glycans	766:785	cell surface glycans	766:785	Once outside the cell, galectins bind to the terminal galactose residues of cell surface glycans and modulate numerous extracellular functions, such as clathrin-independent endocytosis (CIE).
35183508	5	36	theme	glycans	779:785	arg1	residues					754:761	the terminal galactose residues	731:761	the terminal galactose residues of cell surface glycans	731:785	Once outside the cell, galectins bind to the terminal galactose residues of cell surface glycans and modulate numerous extracellular functions, such as clathrin-independent endocytosis (CIE).
35183508	5	36	theme	glycans	779:785	arg1	glycans					779:785	cell surface glycans	766:785	cell surface glycans	766:785	Once outside the cell, galectins bind to the terminal galactose residues of cell surface glycans and modulate numerous extracellular functions, such as clathrin-independent endocytosis (CIE).
35183508	6	37	theme	predicted	926:934	arg1	galectins					912:920	galectins	912:920	galectins	912:920	Originating in the cytoplasm, galectins are predicted substrates for O-GlcNAc addition and removal; and as we have shown, galectin 3 is a substrate for O-GlcNAc transferase.
35183508	6	37	theme	predicted	926:934	arg1	substrates					936:945	predicted substrates	926:945	predicted substrates for O-GlcNAc addition and removal	926:979	Originating in the cytoplasm, galectins are predicted substrates for O-GlcNAc addition and removal; and as we have shown, galectin 3 is a substrate for O-GlcNAc transferase.
35183508	10	38	theme	galectin	1641:1648	arg1	O-GlcNAcylation					1622:1636	dynamic O-GlcNAcylation	1614:1636	dynamic O-GlcNAcylation of galectin 3	1614:1650	Importantly, we showed that these O-GlcNAc-driven alterations in galectin 3 secretion also facilitated changes in CIE. These results indicate that dynamic O-GlcNAcylation of galectin 3 plays a role in modulating its secretion and can tune its function in transducing nutrient-sensing information coded in cell surface glycosylation into biological effects.
35183508	0	39	theme	glycan-binding	75:88	arg1	galectin					98:105	glycan-binding protein galectin 3	75:107	glycan-binding protein galectin 3	75:107	Nutrient-responsive O-GlcNAcylation dynamically modulates the secretion of glycan-binding protein galectin 3.
35183508	10	40	theme	biological	1804:1813	arg1	effects					1815:1821	biological effects	1804:1821	biological effects	1804:1821	Importantly, we showed that these O-GlcNAc-driven alterations in galectin 3 secretion also facilitated changes in CIE. These results indicate that dynamic O-GlcNAcylation of galectin 3 plays a role in modulating its secretion and can tune its function in transducing nutrient-sensing information coded in cell surface glycosylation into biological effects.
35183508	9	41	from	alterations	1346:1356	arg1	secretion					1372:1380	galectin 3 secretion	1361:1380	galectin 3 secretion	1361:1380	We observed dramatic alterations in galectin 3 secretion in response to nutrient conditions, which were dependent on dynamic O-GlcNAcylation.
35183508	5	42	theme	terminal	735:742	arg1	residues					754:761	the terminal galactose residues	731:761	the terminal galactose residues of cell surface glycans	731:785	Once outside the cell, galectins bind to the terminal galactose residues of cell surface glycans and modulate numerous extracellular functions, such as clathrin-independent endocytosis (CIE).
35183508	5	42	theme	terminal	735:742	arg1	glycans					779:785	cell surface glycans	766:785	cell surface glycans	766:785	Once outside the cell, galectins bind to the terminal galactose residues of cell surface glycans and modulate numerous extracellular functions, such as clathrin-independent endocytosis (CIE).
35183508	3	43	theme	biological	547:556	arg1	effects					558:564	biological effects	547:564	biological effects	547:564	However, little is known about the molecular mechanisms underlying how these signals are integrated and transduced into biological effects.
35183508	2	44	contain	have	360:363	arg1	changes					335:341	These changes	329:341	These changes in glycosylation	329:358	These changes in glycosylation have important functional roles and can drive disease progression.
35183508	2	44	contain	have	360:363	arg2	roles					386:390	important functional roles	365:390	important functional roles	365:390	These changes in glycosylation have important functional roles and can drive disease progression.
35183508	5	45	theme	galactose	744:752	arg1	residues					754:761	the terminal galactose residues	731:761	the terminal galactose residues of cell surface glycans	731:785	Once outside the cell, galectins bind to the terminal galactose residues of cell surface glycans and modulate numerous extracellular functions, such as clathrin-independent endocytosis (CIE).
35183508	5	45	theme	galactose	744:752	arg1	glycans					779:785	cell surface glycans	766:785	cell surface glycans	766:785	Once outside the cell, galectins bind to the terminal galactose residues of cell surface glycans and modulate numerous extracellular functions, such as clathrin-independent endocytosis (CIE).
35183508	2	46	theme	functional	375:384	arg1	roles					386:390	important functional roles	365:390	important functional roles	365:390	These changes in glycosylation have important functional roles and can drive disease progression.
35183508	9	47	theme	dynamic	1442:1448	arg1	O-GlcNAcylation					1450:1464	dynamic O-GlcNAcylation	1442:1464	dynamic O-GlcNAcylation	1442:1464	We observed dramatic alterations in galectin 3 secretion in response to nutrient conditions, which were dependent on dynamic O-GlcNAcylation.
35183508	4	48	theme	secretory	669:677	arg1	mechanism					679:687	a poorly characterized nonclassical secretory mechanism	633:687	a poorly characterized nonclassical secretory mechanism	633:687	Galectins are proteins that bind glycans and that are secreted by a poorly characterized nonclassical secretory mechanism.
35183508	1	49	theme	essential	179:187	arg1	roles					189:193	essential roles	179:193	essential roles	179:193	Endomembrane glycosylation and cytoplasmic O-GlcNAcylation each play essential roles in nutrient sensing, and characteristic changes in glycan patterns have been described in disease states such as diabetes and cancer.
35183508	4	50	theme	nonclassical	656:667	arg1	mechanism					679:687	a poorly characterized nonclassical secretory mechanism	633:687	a poorly characterized nonclassical secretory mechanism	633:687	Galectins are proteins that bind glycans and that are secreted by a poorly characterized nonclassical secretory mechanism.
35183508	0	51	theme	galectin	98:105	arg1	secretion					62:70	the secretion	58:70	the secretion of glycan-binding protein galectin 3	58:107	Nutrient-responsive O-GlcNAcylation dynamically modulates the secretion of glycan-binding protein galectin 3.
35183508	1	52	from	changes	235:241	arg1	patterns					253:260	glycan patterns	246:260	glycan patterns	246:260	Endomembrane glycosylation and cytoplasmic O-GlcNAcylation each play essential roles in nutrient sensing, and characteristic changes in glycan patterns have been described in disease states such as diabetes and cancer.
35183508	10	53	theme	dynamic	1614:1620	arg1	O-GlcNAcylation					1622:1636	dynamic O-GlcNAcylation	1614:1636	dynamic O-GlcNAcylation of galectin 3	1614:1650	Importantly, we showed that these O-GlcNAc-driven alterations in galectin 3 secretion also facilitated changes in CIE. These results indicate that dynamic O-GlcNAcylation of galectin 3 plays a role in modulating its secretion and can tune its function in transducing nutrient-sensing information coded in cell surface glycosylation into biological effects.
35183508	0	54	theme	protein	90:96	arg1	galectin					98:105	glycan-binding protein galectin 3	75:107	glycan-binding protein galectin 3	75:107	Nutrient-responsive O-GlcNAcylation dynamically modulates the secretion of glycan-binding protein galectin 3.
35183508	8	55	from	difference	1243:1252	arg1	status					1273:1278	O-GlcNAcylation status	1257:1278	O-GlcNAcylation status	1257:1278	We determined using immunoprecipitation and Western blotting that there is a significant difference in O-GlcNAcylation status between cytoplasmic and secreted galectin 3.
35183508	2	56	theme	disease	406:412	arg1	progression					414:424	disease progression	406:424	disease progression	406:424	These changes in glycosylation have important functional roles and can drive disease progression.
35183508	1	57	theme	disease	285:291	arg1	cancer					321:326	cancer	321:326	cancer	321:326	Endomembrane glycosylation and cytoplasmic O-GlcNAcylation each play essential roles in nutrient sensing, and characteristic changes in glycan patterns have been described in disease states such as diabetes and cancer.
35183508	1	57	theme	disease	285:291	arg1	states					293:298	disease states	285:298	disease states such as diabetes and cancer	285:326	Endomembrane glycosylation and cytoplasmic O-GlcNAcylation each play essential roles in nutrient sensing, and characteristic changes in glycan patterns have been described in disease states such as diabetes and cancer.
35183508	1	57	theme	disease	285:291	arg1	diabetes					308:315	diabetes	308:315	diabetes	308:315	Endomembrane glycosylation and cytoplasmic O-GlcNAcylation each play essential roles in nutrient sensing, and characteristic changes in glycan patterns have been described in disease states such as diabetes and cancer.
36089631	7	0	theme	O-GlcNAc	1205:1212	arg1	level					1214:1218	O-GlcNAc level	1205:1218	O-GlcNAc level	1205:1218	Immunoprecipitation analysis showed that O-GlcNAc level was decreased by LG in both VEGFR1, 2, but a de-O-GlcNAc glycosylase inhibitor restored the O-GlcNAc levels.
36089631	8	1	theme	proteasome	1465:1474	arg1	MG132					1487:1491	MG132	1487:1491	MG132	1487:1491	This inhibitor also abolished the LG-induced increase in VEGFR2 protein, whereas this effect was not disappeared in the presence of the proteasome inhibitor, MG132.
36089631	8	1	theme	proteasome	1465:1474	arg1	inhibitor					1476:1484	the proteasome inhibitor	1461:1484	the proteasome inhibitor	1461:1484	This inhibitor also abolished the LG-induced increase in VEGFR2 protein, whereas this effect was not disappeared in the presence of the proteasome inhibitor, MG132.
36089631	2	2	from	effects	420:426	arg1	neovascularization					448:465	neovascularization	448:465	neovascularization	448:465	Not only hypoxia, ischemia also induces the deficiency of glucose, yet its effects on VEGFR signal and neovascularization have seldom been studied.
36089631	2	2	from	effects	420:426	arg1	signal					437:442	VEGFR signal	431:442	VEGFR signal	431:442	Not only hypoxia, ischemia also induces the deficiency of glucose, yet its effects on VEGFR signal and neovascularization have seldom been studied.
36089631	1	3	theme	endothelial	169:179	arg1	VEGFRs					206:211	VEGFRs	206:211	VEGFRs	206:211	PURPOSE Vascular endothelial growth factor receptors (VEGFRs) have been demonstrated to play a critical role in ischemic retinal diseases, as VEGFRs mediate hypoxia-induced neovascularization.
36089631	1	3	theme	endothelial	169:179	arg1	receptors					195:203	PURPOSE Vascular endothelial growth factor receptors	152:203	PURPOSE Vascular endothelial growth factor receptors (VEGFRs)	152:212	PURPOSE Vascular endothelial growth factor receptors (VEGFRs) have been demonstrated to play a critical role in ischemic retinal diseases, as VEGFRs mediate hypoxia-induced neovascularization.
36089631	0	4	theme	cells	76:80	arg1	proliferation					38:50	the proliferation	34:50	the proliferation of vascular endothelial cells	34:80	A relatively low glucose promotes the proliferation of vascular endothelial cells by suppressing VEGFR2 O-GlcNAcylation and its proteasome degradation.
36089631	1	5	theme	growth	181:186	arg1	VEGFRs					206:211	VEGFRs	206:211	VEGFRs	206:211	PURPOSE Vascular endothelial growth factor receptors (VEGFRs) have been demonstrated to play a critical role in ischemic retinal diseases, as VEGFRs mediate hypoxia-induced neovascularization.
36089631	1	5	theme	growth	181:186	arg1	receptors					195:203	PURPOSE Vascular endothelial growth factor receptors	152:203	PURPOSE Vascular endothelial growth factor receptors (VEGFRs)	152:212	PURPOSE Vascular endothelial growth factor receptors (VEGFRs) have been demonstrated to play a critical role in ischemic retinal diseases, as VEGFRs mediate hypoxia-induced neovascularization.
36089631	6	6	theme	3	974:974	arg1	VEGFR1					963:968	VEGFR1	963:968	VEGFR1	963:968	RESULTS LG (2.8 mmol/L) treatment induced mRNA and protein levels of VEGFR1, 2, 3 even in the presence of the protein synthesis inhibitor, cycloheximide (CHX), suggesting that the increase in VEGFR proteins is partially associated with post-translational modifications.
36089631	0	7	theme	VEGFR2	97:102	arg1	O-GlcNAcylation					104:118	VEGFR2 O-GlcNAcylation	97:118	VEGFR2 O-GlcNAcylation	97:118	A relatively low glucose promotes the proliferation of vascular endothelial cells by suppressing VEGFR2 O-GlcNAcylation and its proteasome degradation.
36089631	9	8	theme	Similar	1494:1500	arg1	results					1502:1508	Similar results	1494:1508	Similar results	1494:1508	Similar results were also observed under OGD condition.
36089631	7	9	theme	de-O-GlcNAc	1265:1275	arg1	inhibitor					1289:1297	a de-O-GlcNAc glycosylase inhibitor	1263:1297	a de-O-GlcNAc glycosylase inhibitor	1263:1297	Immunoprecipitation analysis showed that O-GlcNAc level was decreased by LG in both VEGFR1, 2, but a de-O-GlcNAc glycosylase inhibitor restored the O-GlcNAc levels.
36089631	5	10	used	used	853:856	arg2	viability					819:827	Cell viability	814:827	Cell viability	814:827	Cell viability and apoptosis rate were used to evaluate cell growth characters.
36089631	5	10	used	used	853:856	arg2	rate					843:846	apoptosis rate	833:846	apoptosis rate	833:846	Cell viability and apoptosis rate were used to evaluate cell growth characters.
36089631	4	11	theme	low	764:766	arg1	oxygen					776:781	oxygen	776:781	oxygen	776:781	METHODS In this study, we treated human retinal microvascular endothelial cells with low glucose (LG) alone or in combination with low oxygen (oxygen and glucose deprivation, OGD).
36089631	4	11	theme	low	764:766	arg1	deprivation					795:805	glucose deprivation	787:805	glucose deprivation	787:805	METHODS In this study, we treated human retinal microvascular endothelial cells with low glucose (LG) alone or in combination with low oxygen (oxygen and glucose deprivation, OGD).
36089631	4	11	theme	low	764:766	arg1	oxygen					768:773	low oxygen	764:773	low oxygen (oxygen and glucose deprivation, OGD)	764:811	METHODS In this study, we treated human retinal microvascular endothelial cells with low glucose (LG) alone or in combination with low oxygen (oxygen and glucose deprivation, OGD).
36089631	1	12	theme	ischemic	264:271	arg1	diseases					281:288	ischemic retinal diseases	264:288	ischemic retinal diseases	264:288	PURPOSE Vascular endothelial growth factor receptors (VEGFRs) have been demonstrated to play a critical role in ischemic retinal diseases, as VEGFRs mediate hypoxia-induced neovascularization.
36089631	10	13	theme	VEGFR2	1550:1555	arg1	knockdown					1557:1565	VEGFR2 knockdown	1550:1565	VEGFR2 knockdown	1550:1565	VEGFR2 knockdown more significantly retarded the growth of hRMECs and HUVECs than VEGFR1, 3 knockdown under LG and OGD conditions.
36089631	6	14	theme	LG	902:903	arg1	treatment					918:926	RESULTS LG (2.8 mmol/L) treatment	894:926	RESULTS LG (2.8 mmol/L) treatment	894:926	RESULTS LG (2.8 mmol/L) treatment induced mRNA and protein levels of VEGFR1, 2, 3 even in the presence of the protein synthesis inhibitor, cycloheximide (CHX), suggesting that the increase in VEGFR proteins is partially associated with post-translational modifications.
36089631	4	15	dep	oxygen	776:781	arg1	OGD					808:810	OGD	808:810	OGD	808:810	METHODS In this study, we treated human retinal microvascular endothelial cells with low glucose (LG) alone or in combination with low oxygen (oxygen and glucose deprivation, OGD).
36089631	1	16	theme	retinal	273:279	arg1	diseases					281:288	ischemic retinal diseases	264:288	ischemic retinal diseases	264:288	PURPOSE Vascular endothelial growth factor receptors (VEGFRs) have been demonstrated to play a critical role in ischemic retinal diseases, as VEGFRs mediate hypoxia-induced neovascularization.
36089631	7	17	theme	Immunoprecipitation	1164:1182	arg1	analysis					1184:1191	Immunoprecipitation analysis	1164:1191	Immunoprecipitation analysis	1164:1191	Immunoprecipitation analysis showed that O-GlcNAc level was decreased by LG in both VEGFR1, 2, but a de-O-GlcNAc glycosylase inhibitor restored the O-GlcNAc levels.
36089631	6	18	theme	RESULTS	894:900	arg1	2.8 mmol/L					906:915	2.8 mmol/L	906:915	2.8 mmol/L	906:915	RESULTS LG (2.8 mmol/L) treatment induced mRNA and protein levels of VEGFR1, 2, 3 even in the presence of the protein synthesis inhibitor, cycloheximide (CHX), suggesting that the increase in VEGFR proteins is partially associated with post-translational modifications.
36089631	6	18	theme	RESULTS	894:900	arg1	LG					902:903	RESULTS LG	894:903	RESULTS LG (2.8 mmol/L) treatment	894:926	RESULTS LG (2.8 mmol/L) treatment induced mRNA and protein levels of VEGFR1, 2, 3 even in the presence of the protein synthesis inhibitor, cycloheximide (CHX), suggesting that the increase in VEGFR proteins is partially associated with post-translational modifications.
36089631	7	19	theme	glycosylase	1277:1287	arg1	inhibitor					1289:1297	a de-O-GlcNAc glycosylase inhibitor	1263:1297	a de-O-GlcNAc glycosylase inhibitor	1263:1297	Immunoprecipitation analysis showed that O-GlcNAc level was decreased by LG in both VEGFR1, 2, but a de-O-GlcNAc glycosylase inhibitor restored the O-GlcNAc levels.
36089631	4	20	theme	glucose	787:793	arg1	deprivation					795:805	glucose deprivation	787:805	glucose deprivation	787:805	METHODS In this study, we treated human retinal microvascular endothelial cells with low glucose (LG) alone or in combination with low oxygen (oxygen and glucose deprivation, OGD).
36089631	4	20	theme	glucose	787:793	arg1	oxygen					768:773	low oxygen	764:773	low oxygen (oxygen and glucose deprivation, OGD)	764:811	METHODS In this study, we treated human retinal microvascular endothelial cells with low glucose (LG) alone or in combination with low oxygen (oxygen and glucose deprivation, OGD).
36089631	1	21	theme	factor	188:193	arg1	VEGFRs					206:211	VEGFRs	206:211	VEGFRs	206:211	PURPOSE Vascular endothelial growth factor receptors (VEGFRs) have been demonstrated to play a critical role in ischemic retinal diseases, as VEGFRs mediate hypoxia-induced neovascularization.
36089631	1	21	theme	factor	188:193	arg1	receptors					195:203	PURPOSE Vascular endothelial growth factor receptors	152:203	PURPOSE Vascular endothelial growth factor receptors (VEGFRs)	152:212	PURPOSE Vascular endothelial growth factor receptors (VEGFRs) have been demonstrated to play a critical role in ischemic retinal diseases, as VEGFRs mediate hypoxia-induced neovascularization.
36089631	6	22	theme	2	971:971	arg1	VEGFR1					963:968	VEGFR1	963:968	VEGFR1	963:968	RESULTS LG (2.8 mmol/L) treatment induced mRNA and protein levels of VEGFR1, 2, 3 even in the presence of the protein synthesis inhibitor, cycloheximide (CHX), suggesting that the increase in VEGFR proteins is partially associated with post-translational modifications.
36089631	9	23	theme	OGD	1535:1537	arg1	condition					1539:1547	OGD condition	1535:1547	OGD condition	1535:1547	Similar results were also observed under OGD condition.
36089631	2	24	theme	glucose	403:409	arg1	deficiency					389:398	the deficiency	385:398	the deficiency of glucose	385:409	Not only hypoxia, ischemia also induces the deficiency of glucose, yet its effects on VEGFR signal and neovascularization have seldom been studied.
36089631	8	25	from	increase	1374:1381	arg1	protein					1393:1399	VEGFR2 protein	1386:1399	VEGFR2 protein	1386:1399	This inhibitor also abolished the LG-induced increase in VEGFR2 protein, whereas this effect was not disappeared in the presence of the proteasome inhibitor, MG132.
36089631	5	26	theme	cell	870:873	arg1	characters					882:891	cell growth characters	870:891	cell growth characters	870:891	Cell viability and apoptosis rate were used to evaluate cell growth characters.
36089631	5	27	theme	Cell	814:817	arg1	viability					819:827	Cell viability	814:827	Cell viability	814:827	Cell viability and apoptosis rate were used to evaluate cell growth characters.
36089631	5	28	theme	growth	875:880	arg1	characters					882:891	cell growth characters	870:891	cell growth characters	870:891	Cell viability and apoptosis rate were used to evaluate cell growth characters.
36089631	6	29	theme	VEGFR1	963:968	arg1	levels					953:958	mRNA and protein levels	936:958	mRNA and protein levels of VEGFR1, 2, 3	936:974	RESULTS LG (2.8 mmol/L) treatment induced mRNA and protein levels of VEGFR1, 2, 3 even in the presence of the protein synthesis inhibitor, cycloheximide (CHX), suggesting that the increase in VEGFR proteins is partially associated with post-translational modifications.
36089631	0	30	theme	proteasome	128:137	arg1	degradation					139:149	its proteasome degradation	124:149	its proteasome degradation	124:149	A relatively low glucose promotes the proliferation of vascular endothelial cells by suppressing VEGFR2 O-GlcNAcylation and its proteasome degradation.
36089631	6	31	theme	protein	1004:1010	arg1	cycloheximide					1033:1045	cycloheximide	1033:1045	cycloheximide (CHX)	1033:1051	RESULTS LG (2.8 mmol/L) treatment induced mRNA and protein levels of VEGFR1, 2, 3 even in the presence of the protein synthesis inhibitor, cycloheximide (CHX), suggesting that the increase in VEGFR proteins is partially associated with post-translational modifications.
36089631	6	31	theme	protein	1004:1010	arg1	inhibitor					1022:1030	the protein synthesis inhibitor	1000:1030	the protein synthesis inhibitor	1000:1030	RESULTS LG (2.8 mmol/L) treatment induced mRNA and protein levels of VEGFR1, 2, 3 even in the presence of the protein synthesis inhibitor, cycloheximide (CHX), suggesting that the increase in VEGFR proteins is partially associated with post-translational modifications.
36089631	5	32	theme	apoptosis	833:841	arg1	rate					843:846	apoptosis rate	833:846	apoptosis rate	833:846	Cell viability and apoptosis rate were used to evaluate cell growth characters.
36089631	2	33	theme	VEGFR	431:435	arg1	signal					437:442	VEGFR signal	431:442	VEGFR signal	431:442	Not only hypoxia, ischemia also induces the deficiency of glucose, yet its effects on VEGFR signal and neovascularization have seldom been studied.
36089631	6	34	theme	post-translational	1130:1147	arg1	modifications					1149:1161	post-translational modifications	1130:1161	post-translational modifications	1130:1161	RESULTS LG (2.8 mmol/L) treatment induced mRNA and protein levels of VEGFR1, 2, 3 even in the presence of the protein synthesis inhibitor, cycloheximide (CHX), suggesting that the increase in VEGFR proteins is partially associated with post-translational modifications.
36089631	4	35	dep	METHODS	633:639	arg1	treated					659:665	treated	659:665	treated human retinal microvascular endothelial cells with low glucose (LG) alone or in combination with low oxygen (oxygen and glucose deprivation, OGD)	659:811	METHODS In this study, we treated human retinal microvascular endothelial cells with low glucose (LG) alone or in combination with low oxygen (oxygen and glucose deprivation, OGD).
36089631	3	36	theme	glucose	582:588	arg1	deficiency					590:599	glucose deficiency	582:599	glucose deficiency	582:599	Bioinformatics analysis predicted that VEGFRs may be regulated by O-GlcNAcylation, while glucose deficiency influences the O-GlcNAcylation.
36089631	6	37	theme	synthesis	1012:1020	arg1	cycloheximide					1033:1045	cycloheximide	1033:1045	cycloheximide (CHX)	1033:1051	RESULTS LG (2.8 mmol/L) treatment induced mRNA and protein levels of VEGFR1, 2, 3 even in the presence of the protein synthesis inhibitor, cycloheximide (CHX), suggesting that the increase in VEGFR proteins is partially associated with post-translational modifications.
36089631	6	37	theme	synthesis	1012:1020	arg1	inhibitor					1022:1030	the protein synthesis inhibitor	1000:1030	the protein synthesis inhibitor	1000:1030	RESULTS LG (2.8 mmol/L) treatment induced mRNA and protein levels of VEGFR1, 2, 3 even in the presence of the protein synthesis inhibitor, cycloheximide (CHX), suggesting that the increase in VEGFR proteins is partially associated with post-translational modifications.
36089631	11	38	theme	proteasome	1779:1788	arg1	degradation					1790:1800	its proteasome degradation	1775:1800	its proteasome degradation	1775:1800	CONCLUSIONS A relatively low glucose suppressed O-GlcNAcylation in VEGFR2, whereby inhibiting its proteasome degradation; up-regulated VEGFR2 promoted the proliferation of vascular endothelial cells under ischemic condition.
36089631	11	39	theme	vascular	1853:1860	arg1	cells					1874:1878	vascular endothelial cells	1853:1878	vascular endothelial cells	1853:1878	CONCLUSIONS A relatively low glucose suppressed O-GlcNAcylation in VEGFR2, whereby inhibiting its proteasome degradation; up-regulated VEGFR2 promoted the proliferation of vascular endothelial cells under ischemic condition.
36089631	4	40	with	cells	707:711	arg1	LG					731:732	LG	731:732	LG	731:732	METHODS In this study, we treated human retinal microvascular endothelial cells with low glucose (LG) alone or in combination with low oxygen (oxygen and glucose deprivation, OGD).
36089631	4	40	with	cells	707:711	arg1	glucose					722:728	low glucose	718:728	low glucose (LG) alone or in combination with low oxygen (oxygen and glucose deprivation, OGD)	718:811	METHODS In this study, we treated human retinal microvascular endothelial cells with low glucose (LG) alone or in combination with low oxygen (oxygen and glucose deprivation, OGD).
36089631	10	41	theme	LG	1658:1659	arg1	conditions					1669:1678	LG and OGD conditions	1658:1678	LG and OGD conditions	1658:1678	VEGFR2 knockdown more significantly retarded the growth of hRMECs and HUVECs than VEGFR1, 3 knockdown under LG and OGD conditions.
36089631	10	42	theme	HUVECs	1620:1625	arg1	growth					1599:1604	the growth	1595:1604	the growth of hRMECs and HUVECs	1595:1625	VEGFR2 knockdown more significantly retarded the growth of hRMECs and HUVECs than VEGFR1, 3 knockdown under LG and OGD conditions.
36089631	4	43	theme	retinal	673:679	arg1	cells					707:711	human retinal microvascular endothelial cells	667:711	human retinal microvascular endothelial cells with low glucose (LG) alone or in combination with low oxygen (oxygen and glucose deprivation, OGD)	667:811	METHODS In this study, we treated human retinal microvascular endothelial cells with low glucose (LG) alone or in combination with low oxygen (oxygen and glucose deprivation, OGD).
36089631	4	44	theme	endothelial	695:705	arg1	cells					707:711	human retinal microvascular endothelial cells	667:711	human retinal microvascular endothelial cells with low glucose (LG) alone or in combination with low oxygen (oxygen and glucose deprivation, OGD)	667:811	METHODS In this study, we treated human retinal microvascular endothelial cells with low glucose (LG) alone or in combination with low oxygen (oxygen and glucose deprivation, OGD).
36089631	6	45	theme	protein	945:951	arg1	levels					953:958	mRNA and protein levels	936:958	mRNA and protein levels of VEGFR1, 2, 3	936:974	RESULTS LG (2.8 mmol/L) treatment induced mRNA and protein levels of VEGFR1, 2, 3 even in the presence of the protein synthesis inhibitor, cycloheximide (CHX), suggesting that the increase in VEGFR proteins is partially associated with post-translational modifications.
36089631	10	46	theme	hRMECs	1609:1614	arg1	growth					1599:1604	the growth	1595:1604	the growth of hRMECs and HUVECs	1595:1625	VEGFR2 knockdown more significantly retarded the growth of hRMECs and HUVECs than VEGFR1, 3 knockdown under LG and OGD conditions.
36089631	6	47	from	increase	1074:1081	arg1	proteins					1092:1099	VEGFR proteins	1086:1099	VEGFR proteins	1086:1099	RESULTS LG (2.8 mmol/L) treatment induced mRNA and protein levels of VEGFR1, 2, 3 even in the presence of the protein synthesis inhibitor, cycloheximide (CHX), suggesting that the increase in VEGFR proteins is partially associated with post-translational modifications.
36089631	4	48	theme	human	667:671	arg1	cells					707:711	human retinal microvascular endothelial cells	667:711	human retinal microvascular endothelial cells with low glucose (LG) alone or in combination with low oxygen (oxygen and glucose deprivation, OGD)	667:811	METHODS In this study, we treated human retinal microvascular endothelial cells with low glucose (LG) alone or in combination with low oxygen (oxygen and glucose deprivation, OGD).
36089631	1	49	theme	hypoxia-induced	309:323	arg1	neovascularization					325:342	hypoxia-induced neovascularization	309:342	hypoxia-induced neovascularization	309:342	PURPOSE Vascular endothelial growth factor receptors (VEGFRs) have been demonstrated to play a critical role in ischemic retinal diseases, as VEGFRs mediate hypoxia-induced neovascularization.
36089631	11	50	theme	ischemic	1886:1893	arg1	condition					1895:1903	ischemic condition	1886:1903	ischemic condition	1886:1903	CONCLUSIONS A relatively low glucose suppressed O-GlcNAcylation in VEGFR2, whereby inhibiting its proteasome degradation; up-regulated VEGFR2 promoted the proliferation of vascular endothelial cells under ischemic condition.
36089631	6	51	theme	VEGFR	1086:1090	arg1	proteins					1092:1099	VEGFR proteins	1086:1099	VEGFR proteins	1086:1099	RESULTS LG (2.8 mmol/L) treatment induced mRNA and protein levels of VEGFR1, 2, 3 even in the presence of the protein synthesis inhibitor, cycloheximide (CHX), suggesting that the increase in VEGFR proteins is partially associated with post-translational modifications.
36089631	6	52	theme	mRNA	936:939	arg1	levels					953:958	mRNA and protein levels	936:958	mRNA and protein levels of VEGFR1, 2, 3	936:974	RESULTS LG (2.8 mmol/L) treatment induced mRNA and protein levels of VEGFR1, 2, 3 even in the presence of the protein synthesis inhibitor, cycloheximide (CHX), suggesting that the increase in VEGFR proteins is partially associated with post-translational modifications.
36089631	8	53	theme	VEGFR2	1386:1391	arg1	protein					1393:1399	VEGFR2 protein	1386:1399	VEGFR2 protein	1386:1399	This inhibitor also abolished the LG-induced increase in VEGFR2 protein, whereas this effect was not disappeared in the presence of the proteasome inhibitor, MG132.
36089631	7	54	theme	O-GlcNAc	1312:1319	arg1	levels					1321:1326	the O-GlcNAc levels	1308:1326	the O-GlcNAc levels	1308:1326	Immunoprecipitation analysis showed that O-GlcNAc level was decreased by LG in both VEGFR1, 2, but a de-O-GlcNAc glycosylase inhibitor restored the O-GlcNAc levels.
36089631	11	55	theme	endothelial	1862:1872	arg1	cells					1874:1878	vascular endothelial cells	1853:1878	vascular endothelial cells	1853:1878	CONCLUSIONS A relatively low glucose suppressed O-GlcNAcylation in VEGFR2, whereby inhibiting its proteasome degradation; up-regulated VEGFR2 promoted the proliferation of vascular endothelial cells under ischemic condition.
36089631	4	56	with	combination	747:757	arg1	oxygen					776:781	oxygen	776:781	oxygen	776:781	METHODS In this study, we treated human retinal microvascular endothelial cells with low glucose (LG) alone or in combination with low oxygen (oxygen and glucose deprivation, OGD).
36089631	4	56	with	combination	747:757	arg1	deprivation					795:805	glucose deprivation	787:805	glucose deprivation	787:805	METHODS In this study, we treated human retinal microvascular endothelial cells with low glucose (LG) alone or in combination with low oxygen (oxygen and glucose deprivation, OGD).
36089631	4	56	with	combination	747:757	arg1	oxygen					768:773	low oxygen	764:773	low oxygen (oxygen and glucose deprivation, OGD)	764:811	METHODS In this study, we treated human retinal microvascular endothelial cells with low glucose (LG) alone or in combination with low oxygen (oxygen and glucose deprivation, OGD).
36089631	11	57	from	O-GlcNAcylation	1729:1743	arg1	VEGFR2					1748:1753	VEGFR2	1748:1753	VEGFR2	1748:1753	CONCLUSIONS A relatively low glucose suppressed O-GlcNAcylation in VEGFR2, whereby inhibiting its proteasome degradation; up-regulated VEGFR2 promoted the proliferation of vascular endothelial cells under ischemic condition.
36089631	11	58	theme	low	1706:1708	arg1	O-GlcNAcylation					1729:1743	A relatively low glucose suppressed O-GlcNAcylation	1693:1743	A relatively low glucose suppressed O-GlcNAcylation	1693:1743	CONCLUSIONS A relatively low glucose suppressed O-GlcNAcylation in VEGFR2, whereby inhibiting its proteasome degradation; up-regulated VEGFR2 promoted the proliferation of vascular endothelial cells under ischemic condition.
36089631	11	59	theme	cells	1874:1878	arg1	proliferation					1836:1848	the proliferation	1832:1848	the proliferation of vascular endothelial cells	1832:1878	CONCLUSIONS A relatively low glucose suppressed O-GlcNAcylation in VEGFR2, whereby inhibiting its proteasome degradation; up-regulated VEGFR2 promoted the proliferation of vascular endothelial cells under ischemic condition.
36089631	4	60	theme	low	718:720	arg1	LG					731:732	LG	731:732	LG	731:732	METHODS In this study, we treated human retinal microvascular endothelial cells with low glucose (LG) alone or in combination with low oxygen (oxygen and glucose deprivation, OGD).
36089631	4	60	theme	low	718:720	arg1	glucose					722:728	low glucose	718:728	low glucose (LG) alone or in combination with low oxygen (oxygen and glucose deprivation, OGD)	718:811	METHODS In this study, we treated human retinal microvascular endothelial cells with low glucose (LG) alone or in combination with low oxygen (oxygen and glucose deprivation, OGD).
36089631	10	61	theme	OGD	1665:1667	arg1	conditions					1669:1678	LG and OGD conditions	1658:1678	LG and OGD conditions	1658:1678	VEGFR2 knockdown more significantly retarded the growth of hRMECs and HUVECs than VEGFR1, 3 knockdown under LG and OGD conditions.
36089631	8	62	theme	LG-induced	1363:1372	arg1	increase					1374:1381	the LG-induced increase	1359:1381	the LG-induced increase in VEGFR2 protein	1359:1399	This inhibitor also abolished the LG-induced increase in VEGFR2 protein, whereas this effect was not disappeared in the presence of the proteasome inhibitor, MG132.
36089631	7	63	dep	VEGFR1	1248:1253	arg1	both					1243:1246	both	1243:1246	both	1243:1246	Immunoprecipitation analysis showed that O-GlcNAc level was decreased by LG in both VEGFR1, 2, but a de-O-GlcNAc glycosylase inhibitor restored the O-GlcNAc levels.
36089631	7	63	dep	VEGFR1	1248:1253	arg1	2					1256:1256	2	1256:1256	2	1256:1256	Immunoprecipitation analysis showed that O-GlcNAc level was decreased by LG in both VEGFR1, 2, but a de-O-GlcNAc glycosylase inhibitor restored the O-GlcNAc levels.
36089631	3	64	theme	Bioinformatics	493:506	arg1	analysis					508:515	Bioinformatics analysis	493:515	Bioinformatics analysis	493:515	Bioinformatics analysis predicted that VEGFRs may be regulated by O-GlcNAcylation, while glucose deficiency influences the O-GlcNAcylation.
36089631	11	65	theme	up-regulated	1803:1814	arg1	VEGFR2					1816:1821	up-regulated VEGFR2	1803:1821	up-regulated VEGFR2	1803:1821	CONCLUSIONS A relatively low glucose suppressed O-GlcNAcylation in VEGFR2, whereby inhibiting its proteasome degradation; up-regulated VEGFR2 promoted the proliferation of vascular endothelial cells under ischemic condition.
36089631	0	66	theme	endothelial	64:74	arg1	cells					76:80	vascular endothelial cells	55:80	vascular endothelial cells	55:80	A relatively low glucose promotes the proliferation of vascular endothelial cells by suppressing VEGFR2 O-GlcNAcylation and its proteasome degradation.
36089631	11	67	theme	suppressed	1718:1727	arg1	O-GlcNAcylation					1729:1743	A relatively low glucose suppressed O-GlcNAcylation	1693:1743	A relatively low glucose suppressed O-GlcNAcylation	1693:1743	CONCLUSIONS A relatively low glucose suppressed O-GlcNAcylation in VEGFR2, whereby inhibiting its proteasome degradation; up-regulated VEGFR2 promoted the proliferation of vascular endothelial cells under ischemic condition.
36089631	6	68	theme	inhibitor	1022:1030	arg1	presence					988:995	the presence	984:995	the presence of the protein synthesis inhibitor, cycloheximide (CHX)	984:1051	RESULTS LG (2.8 mmol/L) treatment induced mRNA and protein levels of VEGFR1, 2, 3 even in the presence of the protein synthesis inhibitor, cycloheximide (CHX), suggesting that the increase in VEGFR proteins is partially associated with post-translational modifications.
36089631	1	69	theme	PURPOSE	152:158	arg1	VEGFRs					206:211	VEGFRs	206:211	VEGFRs	206:211	PURPOSE Vascular endothelial growth factor receptors (VEGFRs) have been demonstrated to play a critical role in ischemic retinal diseases, as VEGFRs mediate hypoxia-induced neovascularization.
36089631	1	69	theme	PURPOSE	152:158	arg1	receptors					195:203	PURPOSE Vascular endothelial growth factor receptors	152:203	PURPOSE Vascular endothelial growth factor receptors (VEGFRs)	152:212	PURPOSE Vascular endothelial growth factor receptors (VEGFRs) have been demonstrated to play a critical role in ischemic retinal diseases, as VEGFRs mediate hypoxia-induced neovascularization.
36089631	4	70	theme	microvascular	681:693	arg1	cells					707:711	human retinal microvascular endothelial cells	667:711	human retinal microvascular endothelial cells with low glucose (LG) alone or in combination with low oxygen (oxygen and glucose deprivation, OGD)	667:811	METHODS In this study, we treated human retinal microvascular endothelial cells with low glucose (LG) alone or in combination with low oxygen (oxygen and glucose deprivation, OGD).
36089631	11	71	theme	glucose	1710:1716	arg1	O-GlcNAcylation					1729:1743	A relatively low glucose suppressed O-GlcNAcylation	1693:1743	A relatively low glucose suppressed O-GlcNAcylation	1693:1743	CONCLUSIONS A relatively low glucose suppressed O-GlcNAcylation in VEGFR2, whereby inhibiting its proteasome degradation; up-regulated VEGFR2 promoted the proliferation of vascular endothelial cells under ischemic condition.
36089631	0	72	theme	vascular	55:62	arg1	cells					76:80	vascular endothelial cells	55:80	vascular endothelial cells	55:80	A relatively low glucose promotes the proliferation of vascular endothelial cells by suppressing VEGFR2 O-GlcNAcylation and its proteasome degradation.
36089631	8	73	theme	inhibitor	1476:1484	arg1	presence					1449:1456	the presence	1445:1456	the presence of the proteasome inhibitor, MG132	1445:1491	This inhibitor also abolished the LG-induced increase in VEGFR2 protein, whereas this effect was not disappeared in the presence of the proteasome inhibitor, MG132.
36089631	0	74	theme	low	13:15	arg1	glucose					17:23	A relatively low glucose	0:23	A relatively low glucose	0:23	A relatively low glucose promotes the proliferation of vascular endothelial cells by suppressing VEGFR2 O-GlcNAcylation and its proteasome degradation.
36089631	1	75	theme	Vascular	160:167	arg1	VEGFRs					206:211	VEGFRs	206:211	VEGFRs	206:211	PURPOSE Vascular endothelial growth factor receptors (VEGFRs) have been demonstrated to play a critical role in ischemic retinal diseases, as VEGFRs mediate hypoxia-induced neovascularization.
36089631	1	75	theme	Vascular	160:167	arg1	receptors					195:203	PURPOSE Vascular endothelial growth factor receptors	152:203	PURPOSE Vascular endothelial growth factor receptors (VEGFRs)	152:212	PURPOSE Vascular endothelial growth factor receptors (VEGFRs) have been demonstrated to play a critical role in ischemic retinal diseases, as VEGFRs mediate hypoxia-induced neovascularization.
36089631	1	76	theme	critical	247:254	arg1	role					256:259	a critical role	245:259	a critical role	245:259	PURPOSE Vascular endothelial growth factor receptors (VEGFRs) have been demonstrated to play a critical role in ischemic retinal diseases, as VEGFRs mediate hypoxia-induced neovascularization.
35467332	0	0	from	Erasing	12:18	arg1	Alpha					48:52	Casein Kinase 2 Alpha	32:52	Casein Kinase 2 Alpha	32:52	Writing and Erasing O-GlcNAc on Casein Kinase 2 Alpha Alters the Phosphoproteome.
35467332	1	1	theme	phosphorylation	154:168	arg1	pathways					180:187	phosphorylation signaling pathways	154:187	phosphorylation signaling pathways	154:187	O-GlcNAc is an essential carbohydrate modification that intersects with phosphorylation signaling pathways via crosstalk on protein substrates or by direct modification of the kinases that write the phosphate modification.
35467332	1	2	theme	kinases	258:264	arg1	modification					238:249	direct modification	231:249	direct modification of the kinases that write the phosphate modification	231:302	O-GlcNAc is an essential carbohydrate modification that intersects with phosphorylation signaling pathways via crosstalk on protein substrates or by direct modification of the kinases that write the phosphate modification.
35467332	3	3	theme	tagged	661:666	arg1	CK2α					668:671	a tagged CK2α	659:671	a tagged CK2α to measure the effects on the phosphoproteome in cells	659:726	Here, we apply complementary targeted O-GlcNAc editors, nanobody-OGT and -splitOGA, to selectively write and erase O-GlcNAc from a tagged CK2α to measure the effects on the phosphoproteome in cells.
35467332	1	4	theme	signaling	170:178	arg1	pathways					180:187	phosphorylation signaling pathways	154:187	phosphorylation signaling pathways	154:187	O-GlcNAc is an essential carbohydrate modification that intersects with phosphorylation signaling pathways via crosstalk on protein substrates or by direct modification of the kinases that write the phosphate modification.
35467332	7	5	theme	future	1155:1160	arg1	studies					1162:1168	future studies	1155:1168	future studies on the crosstalk between O-GlcNAc and phosphorylation	1155:1222	These data will propel future studies on the crosstalk between O-GlcNAc and phosphorylation.
35467332	0	6	from	Writing	0:6	arg1	Alpha					48:52	Casein Kinase 2 Alpha	32:52	Casein Kinase 2 Alpha	32:52	Writing and Erasing O-GlcNAc on Casein Kinase 2 Alpha Alters the Phosphoproteome.
35467332	2	7	theme	Casein	305:310	arg1	subunit					349:355	the catalytic subunit	335:355	the catalytic subunit of the ubiquitously expressed and constitutively active kinase CK2	335:422	Casein kinase 2 alpha (CK2α), the catalytic subunit of the ubiquitously expressed and constitutively active kinase CK2, is modified by O-GlcNAc, but the effect of this modification on the phosphoproteome in cells is unknown.
35467332	2	7	theme	Casein	305:310	arg1	CK2α					328:331	CK2α	328:331	CK2α	328:331	Casein kinase 2 alpha (CK2α), the catalytic subunit of the ubiquitously expressed and constitutively active kinase CK2, is modified by O-GlcNAc, but the effect of this modification on the phosphoproteome in cells is unknown.
35467332	2	7	theme	Casein	305:310	arg1	alpha					321:325	Casein kinase 2 alpha	305:325	Casein kinase 2 alpha (CK2α)	305:332	Casein kinase 2 alpha (CK2α), the catalytic subunit of the ubiquitously expressed and constitutively active kinase CK2, is modified by O-GlcNAc, but the effect of this modification on the phosphoproteome in cells is unknown.
35467332	2	8	theme	kinase	312:317	arg1	subunit					349:355	the catalytic subunit	335:355	the catalytic subunit of the ubiquitously expressed and constitutively active kinase CK2	335:422	Casein kinase 2 alpha (CK2α), the catalytic subunit of the ubiquitously expressed and constitutively active kinase CK2, is modified by O-GlcNAc, but the effect of this modification on the phosphoproteome in cells is unknown.
35467332	2	8	theme	kinase	312:317	arg1	CK2α					328:331	CK2α	328:331	CK2α	328:331	Casein kinase 2 alpha (CK2α), the catalytic subunit of the ubiquitously expressed and constitutively active kinase CK2, is modified by O-GlcNAc, but the effect of this modification on the phosphoproteome in cells is unknown.
35467332	2	8	theme	kinase	312:317	arg1	alpha					321:325	Casein kinase 2 alpha	305:325	Casein kinase 2 alpha (CK2α)	305:332	Casein kinase 2 alpha (CK2α), the catalytic subunit of the ubiquitously expressed and constitutively active kinase CK2, is modified by O-GlcNAc, but the effect of this modification on the phosphoproteome in cells is unknown.
35467332	3	9	from	phosphoproteome	703:717	arg1	cells					722:726	cells	722:726	cells	722:726	Here, we apply complementary targeted O-GlcNAc editors, nanobody-OGT and -splitOGA, to selectively write and erase O-GlcNAc from a tagged CK2α to measure the effects on the phosphoproteome in cells.
35467332	5	10	theme	quantitative	810:821	arg1	phosphoproteomics					823:839	quantitative phosphoproteomics	810:839	quantitative phosphoproteomics	810:839	Using quantitative phosphoproteomics, we report 51 phosphoproteins whose enrichment changes as a function of editing O-GlcNAc on CK2α, including HDAC1, HDAC2, ENSA, SMARCAD1, and PABPN1.
35467332	2	11	from	effect	458:463	arg1	phosphoproteome					493:507	the phosphoproteome	489:507	the phosphoproteome in cells	489:516	Casein kinase 2 alpha (CK2α), the catalytic subunit of the ubiquitously expressed and constitutively active kinase CK2, is modified by O-GlcNAc, but the effect of this modification on the phosphoproteome in cells is unknown.
35467332	6	12	from	phosphosites	1000:1011	arg1	HDAC1					1016:1020	HDAC1 Ser393	1016:1027	HDAC1 Ser393	1016:1027	Specific phosphosites on HDAC1 Ser393 and HDAC2 Ser394, both reported CK2 substrates, are significantly enhanced by O-GlcNAcylation of CK2α.
35467332	6	12	from	phosphosites	1000:1011	arg1	HDAC2					1033:1037	HDAC2 Ser394	1033:1044	HDAC2 Ser394	1033:1044	Specific phosphosites on HDAC1 Ser393 and HDAC2 Ser394, both reported CK2 substrates, are significantly enhanced by O-GlcNAcylation of CK2α.
35467332	6	13	theme	CK2α	1126:1129	arg1	O-GlcNAcylation					1107:1121	O-GlcNAcylation	1107:1121	O-GlcNAcylation of CK2α	1107:1129	Specific phosphosites on HDAC1 Ser393 and HDAC2 Ser394, both reported CK2 substrates, are significantly enhanced by O-GlcNAcylation of CK2α.
35467332	4	14	gly	glycosite	785:793	arg2	glycosite					785:793	the Ser347 glycosite	774:793	the Ser347 glycosite on CK2α	774:801	These tools effectively and selectively edit the Ser347 glycosite on CK2α.
35467332	5	15	theme	O-GlcNAc	921:928	arg1	function					901:908	a function	899:908	a function of editing O-GlcNAc on CK2α, including HDAC1, HDAC2, ENSA, SMARCAD1, and PABPN1	899:988	Using quantitative phosphoproteomics, we report 51 phosphoproteins whose enrichment changes as a function of editing O-GlcNAc on CK2α, including HDAC1, HDAC2, ENSA, SMARCAD1, and PABPN1.
35467332	2	16	theme	expressed	377:385	arg1	CK2					420:422	the ubiquitously expressed and constitutively active kinase CK2	360:422	the ubiquitously expressed and constitutively active kinase CK2	360:422	Casein kinase 2 alpha (CK2α), the catalytic subunit of the ubiquitously expressed and constitutively active kinase CK2, is modified by O-GlcNAc, but the effect of this modification on the phosphoproteome in cells is unknown.
35467332	3	17	from	effects	688:694	arg1	phosphoproteome					703:717	the phosphoproteome	699:717	the phosphoproteome in cells	699:726	Here, we apply complementary targeted O-GlcNAc editors, nanobody-OGT and -splitOGA, to selectively write and erase O-GlcNAc from a tagged CK2α to measure the effects on the phosphoproteome in cells.
35467332	1	18	theme	phosphate	281:289	arg1	modification					291:302	the phosphate modification	277:302	the phosphate modification	277:302	O-GlcNAc is an essential carbohydrate modification that intersects with phosphorylation signaling pathways via crosstalk on protein substrates or by direct modification of the kinases that write the phosphate modification.
35467332	3	19	theme	complementary	545:557	arg1	editors					577:583	complementary targeted O-GlcNAc editors	545:583	complementary targeted O-GlcNAc editors	545:583	Here, we apply complementary targeted O-GlcNAc editors, nanobody-OGT and -splitOGA, to selectively write and erase O-GlcNAc from a tagged CK2α to measure the effects on the phosphoproteome in cells.
35467332	3	19	theme	complementary	545:557	arg1	-splitOGA					603:611	-splitOGA	603:611	-splitOGA	603:611	Here, we apply complementary targeted O-GlcNAc editors, nanobody-OGT and -splitOGA, to selectively write and erase O-GlcNAc from a tagged CK2α to measure the effects on the phosphoproteome in cells.
35467332	3	19	theme	complementary	545:557	arg1	nanobody-OGT					586:597	nanobody-OGT	586:597	nanobody-OGT	586:597	Here, we apply complementary targeted O-GlcNAc editors, nanobody-OGT and -splitOGA, to selectively write and erase O-GlcNAc from a tagged CK2α to measure the effects on the phosphoproteome in cells.
35467332	2	20	mod	modified	428:435	arg1	subunit					349:355	the catalytic subunit	335:355	the catalytic subunit of the ubiquitously expressed and constitutively active kinase CK2	335:422	Casein kinase 2 alpha (CK2α), the catalytic subunit of the ubiquitously expressed and constitutively active kinase CK2, is modified by O-GlcNAc, but the effect of this modification on the phosphoproteome in cells is unknown.
35467332	2	20	mod	modified	428:435	arg1	CK2α					328:331	CK2α	328:331	CK2α	328:331	Casein kinase 2 alpha (CK2α), the catalytic subunit of the ubiquitously expressed and constitutively active kinase CK2, is modified by O-GlcNAc, but the effect of this modification on the phosphoproteome in cells is unknown.
35467332	2	20	mod	modified	428:435	arg1	alpha					321:325	Casein kinase 2 alpha	305:325	Casein kinase 2 alpha (CK2α)	305:332	Casein kinase 2 alpha (CK2α), the catalytic subunit of the ubiquitously expressed and constitutively active kinase CK2, is modified by O-GlcNAc, but the effect of this modification on the phosphoproteome in cells is unknown.
35467332	2	20	mod	modified	428:435	arg3	O-GlcNAc					440:447	O-GlcNAc	440:447	O-GlcNAc	440:447	Casein kinase 2 alpha (CK2α), the catalytic subunit of the ubiquitously expressed and constitutively active kinase CK2, is modified by O-GlcNAc, but the effect of this modification on the phosphoproteome in cells is unknown.
35467332	5	21	from	function	901:908	arg1	CK2α					933:936	CK2α	933:936	CK2α	933:936	Using quantitative phosphoproteomics, we report 51 phosphoproteins whose enrichment changes as a function of editing O-GlcNAc on CK2α, including HDAC1, HDAC2, ENSA, SMARCAD1, and PABPN1.
35467332	1	22	theme	protein	206:212	arg1	substrates					214:223	protein substrates	206:223	protein substrates	206:223	O-GlcNAc is an essential carbohydrate modification that intersects with phosphorylation signaling pathways via crosstalk on protein substrates or by direct modification of the kinases that write the phosphate modification.
35467332	2	23	theme	catalytic	339:347	arg1	subunit					349:355	the catalytic subunit	335:355	the catalytic subunit of the ubiquitously expressed and constitutively active kinase CK2	335:422	Casein kinase 2 alpha (CK2α), the catalytic subunit of the ubiquitously expressed and constitutively active kinase CK2, is modified by O-GlcNAc, but the effect of this modification on the phosphoproteome in cells is unknown.
35467332	2	23	theme	catalytic	339:347	arg1	alpha					321:325	Casein kinase 2 alpha	305:325	Casein kinase 2 alpha (CK2α)	305:332	Casein kinase 2 alpha (CK2α), the catalytic subunit of the ubiquitously expressed and constitutively active kinase CK2, is modified by O-GlcNAc, but the effect of this modification on the phosphoproteome in cells is unknown.
35467332	2	24	theme	CK2	420:422	arg1	subunit					349:355	the catalytic subunit	335:355	the catalytic subunit of the ubiquitously expressed and constitutively active kinase CK2	335:422	Casein kinase 2 alpha (CK2α), the catalytic subunit of the ubiquitously expressed and constitutively active kinase CK2, is modified by O-GlcNAc, but the effect of this modification on the phosphoproteome in cells is unknown.
35467332	2	24	theme	CK2	420:422	arg1	alpha					321:325	Casein kinase 2 alpha	305:325	Casein kinase 2 alpha (CK2α)	305:332	Casein kinase 2 alpha (CK2α), the catalytic subunit of the ubiquitously expressed and constitutively active kinase CK2, is modified by O-GlcNAc, but the effect of this modification on the phosphoproteome in cells is unknown.
35467332	0	25	theme	Casein	32:37	arg1	Kinase					39:44	Casein Kinase 2	32:46	Casein Kinase 2 Alpha	32:52	Writing and Erasing O-GlcNAc on Casein Kinase 2 Alpha Alters the Phosphoproteome.
35467332	2	26	theme	kinase	413:418	arg1	CK2					420:422	the ubiquitously expressed and constitutively active kinase CK2	360:422	the ubiquitously expressed and constitutively active kinase CK2	360:422	Casein kinase 2 alpha (CK2α), the catalytic subunit of the ubiquitously expressed and constitutively active kinase CK2, is modified by O-GlcNAc, but the effect of this modification on the phosphoproteome in cells is unknown.
35467332	3	27	from	CK2α	668:671	arg1	O-GlcNAc					645:652	O-GlcNAc	645:652	O-GlcNAc from a tagged CK2α to measure the effects on the phosphoproteome in cells	645:726	Here, we apply complementary targeted O-GlcNAc editors, nanobody-OGT and -splitOGA, to selectively write and erase O-GlcNAc from a tagged CK2α to measure the effects on the phosphoproteome in cells.
35467332	2	28	theme	active	406:411	arg1	CK2					420:422	the ubiquitously expressed and constitutively active kinase CK2	360:422	the ubiquitously expressed and constitutively active kinase CK2	360:422	Casein kinase 2 alpha (CK2α), the catalytic subunit of the ubiquitously expressed and constitutively active kinase CK2, is modified by O-GlcNAc, but the effect of this modification on the phosphoproteome in cells is unknown.
35467332	7	29	from	studies	1162:1168	arg1	crosstalk					1177:1185	the crosstalk	1173:1185	the crosstalk between O-GlcNAc and phosphorylation	1173:1222	These data will propel future studies on the crosstalk between O-GlcNAc and phosphorylation.
35467332	3	30	theme	targeted	559:566	arg1	editors					577:583	complementary targeted O-GlcNAc editors	545:583	complementary targeted O-GlcNAc editors	545:583	Here, we apply complementary targeted O-GlcNAc editors, nanobody-OGT and -splitOGA, to selectively write and erase O-GlcNAc from a tagged CK2α to measure the effects on the phosphoproteome in cells.
35467332	3	30	theme	targeted	559:566	arg1	-splitOGA					603:611	-splitOGA	603:611	-splitOGA	603:611	Here, we apply complementary targeted O-GlcNAc editors, nanobody-OGT and -splitOGA, to selectively write and erase O-GlcNAc from a tagged CK2α to measure the effects on the phosphoproteome in cells.
35467332	3	30	theme	targeted	559:566	arg1	nanobody-OGT					586:597	nanobody-OGT	586:597	nanobody-OGT	586:597	Here, we apply complementary targeted O-GlcNAc editors, nanobody-OGT and -splitOGA, to selectively write and erase O-GlcNAc from a tagged CK2α to measure the effects on the phosphoproteome in cells.
35467332	1	31	theme	essential	97:105	arg1	modification					120:131	an essential carbohydrate modification	94:131	an essential carbohydrate modification that intersects with phosphorylation signaling pathways via crosstalk on protein substrates or by direct modification of the kinases that write the phosphate modification	94:302	O-GlcNAc is an essential carbohydrate modification that intersects with phosphorylation signaling pathways via crosstalk on protein substrates or by direct modification of the kinases that write the phosphate modification.
35467332	1	31	theme	essential	97:105	arg1	O-GlcNAc					82:89	O-GlcNAc	82:89	O-GlcNAc	82:89	O-GlcNAc is an essential carbohydrate modification that intersects with phosphorylation signaling pathways via crosstalk on protein substrates or by direct modification of the kinases that write the phosphate modification.
35467332	0	32	theme	Kinase	39:44	arg1	Alpha					48:52	Casein Kinase 2 Alpha	32:52	Casein Kinase 2 Alpha	32:52	Writing and Erasing O-GlcNAc on Casein Kinase 2 Alpha Alters the Phosphoproteome.
35467332	2	33	from	phosphoproteome	493:507	arg1	cells					512:516	cells	512:516	cells	512:516	Casein kinase 2 alpha (CK2α), the catalytic subunit of the ubiquitously expressed and constitutively active kinase CK2, is modified by O-GlcNAc, but the effect of this modification on the phosphoproteome in cells is unknown.
35467332	3	34	theme	O-GlcNAc	568:575	arg1	editors					577:583	complementary targeted O-GlcNAc editors	545:583	complementary targeted O-GlcNAc editors	545:583	Here, we apply complementary targeted O-GlcNAc editors, nanobody-OGT and -splitOGA, to selectively write and erase O-GlcNAc from a tagged CK2α to measure the effects on the phosphoproteome in cells.
35467332	3	34	theme	O-GlcNAc	568:575	arg1	-splitOGA					603:611	-splitOGA	603:611	-splitOGA	603:611	Here, we apply complementary targeted O-GlcNAc editors, nanobody-OGT and -splitOGA, to selectively write and erase O-GlcNAc from a tagged CK2α to measure the effects on the phosphoproteome in cells.
35467332	3	34	theme	O-GlcNAc	568:575	arg1	nanobody-OGT					586:597	nanobody-OGT	586:597	nanobody-OGT	586:597	Here, we apply complementary targeted O-GlcNAc editors, nanobody-OGT and -splitOGA, to selectively write and erase O-GlcNAc from a tagged CK2α to measure the effects on the phosphoproteome in cells.
35467332	1	35	theme	carbohydrate	107:118	arg1	modification					120:131	an essential carbohydrate modification	94:131	an essential carbohydrate modification that intersects with phosphorylation signaling pathways via crosstalk on protein substrates or by direct modification of the kinases that write the phosphate modification	94:302	O-GlcNAc is an essential carbohydrate modification that intersects with phosphorylation signaling pathways via crosstalk on protein substrates or by direct modification of the kinases that write the phosphate modification.
35467332	1	35	theme	carbohydrate	107:118	arg1	O-GlcNAc					82:89	O-GlcNAc	82:89	O-GlcNAc	82:89	O-GlcNAc is an essential carbohydrate modification that intersects with phosphorylation signaling pathways via crosstalk on protein substrates or by direct modification of the kinases that write the phosphate modification.
35467332	4	36	from	glycosite	785:793	arg1	CK2α					798:801	CK2α	798:801	CK2α	798:801	These tools effectively and selectively edit the Ser347 glycosite on CK2α.
35467332	1	37	theme	direct	231:236	arg1	modification					238:249	direct modification	231:249	direct modification of the kinases that write the phosphate modification	231:302	O-GlcNAc is an essential carbohydrate modification that intersects with phosphorylation signaling pathways via crosstalk on protein substrates or by direct modification of the kinases that write the phosphate modification.
35467332	1	38	from	crosstalk	193:201	arg1	substrates					214:223	protein substrates	206:223	protein substrates	206:223	O-GlcNAc is an essential carbohydrate modification that intersects with phosphorylation signaling pathways via crosstalk on protein substrates or by direct modification of the kinases that write the phosphate modification.
35467332	5	39	theme	editing	913:919	arg1	O-GlcNAc					921:928	editing O-GlcNAc	913:928	editing O-GlcNAc	913:928	Using quantitative phosphoproteomics, we report 51 phosphoproteins whose enrichment changes as a function of editing O-GlcNAc on CK2α, including HDAC1, HDAC2, ENSA, SMARCAD1, and PABPN1.
35467332	6	40	theme	Specific	991:998	arg1	phosphosites					1000:1011	Specific phosphosites	991:1011	Specific phosphosites on HDAC1 Ser393 and HDAC2 Ser394	991:1044	Specific phosphosites on HDAC1 Ser393 and HDAC2 Ser394, both reported CK2 substrates, are significantly enhanced by O-GlcNAcylation of CK2α.
35467332	6	40	theme	Specific	991:998	arg1	both					1047:1050	both	1047:1050	both	1047:1050	Specific phosphosites on HDAC1 Ser393 and HDAC2 Ser394, both reported CK2 substrates, are significantly enhanced by O-GlcNAcylation of CK2α.
35467332	4	41	theme	Ser347	778:783	arg1	glycosite					785:793	the Ser347 glycosite	774:793	the Ser347 glycosite on CK2α	774:801	These tools effectively and selectively edit the Ser347 glycosite on CK2α.
35467332	2	42	theme	modification	473:484	arg1	unknown					521:527	unknown	521:527	unknown	521:527	Casein kinase 2 alpha (CK2α), the catalytic subunit of the ubiquitously expressed and constitutively active kinase CK2, is modified by O-GlcNAc, but the effect of this modification on the phosphoproteome in cells is unknown.
35467332	2	42	theme	modification	473:484	arg1	effect					458:463	the effect	454:463	the effect of this modification on the phosphoproteome in cells	454:516	Casein kinase 2 alpha (CK2α), the catalytic subunit of the ubiquitously expressed and constitutively active kinase CK2, is modified by O-GlcNAc, but the effect of this modification on the phosphoproteome in cells is unknown.
35467332	0	43	dep	Writing	0:6	arg1	O-GlcNAc					20:27	O-GlcNAc	20:27	O-GlcNAc	20:27	Writing and Erasing O-GlcNAc on Casein Kinase 2 Alpha Alters the Phosphoproteome.
30237463	7	0	theme	O-GlcNAcylation	1189:1203	arg1	effects					1155:1161	the effects	1151:1161	the effects of Rab3A and its aberrant O-GlcNAcylation on HCC metastasis	1151:1221	Further experiments revealed that O-GlcNAcylation on Rab3A was key for attenuating Rab3A-mediated effects by regulating its GTP-binding activity, and verified the effects of Rab3A and its aberrant O-GlcNAcylation on HCC metastasis in vitro and in vivo.
30237463	3	1	theme	mRNA	488:491	arg1	levels					505:510	upregulated mRNA and protein levels	476:510	upregulated mRNA and protein levels of Rab3A in most tumor tissues	476:541	To investigate the potential roles of Rab3A in HCC progression, we first determined Rab3A levels in HCC tissues and observed upregulated mRNA and protein levels of Rab3A in most tumor tissues.
30237463	4	2	theme	in	553:554	arg1	data					562:565	in vitro data	553:565	in vitro data	553:565	However, in vitro data showed that decreasing Rab3A in most HCC cell lines conferred no significant effects and overexpressing Rab3A in PLC/PRF/5 cells even inhibited migration and invasion.
30237463	5	3	from	upregulation	750:761	arg1	patients					779:786	HCC patients	775:786	HCC patients	775:786	Meanwhile, the upregulation of Rab3A in HCC patients did not correlate with metastasis or overall survival of HCC patients.
30237463	8	4	theme	mitochondria	1316:1327	arg1	mtOXPHOS					1356:1363	mtOXPHOS	1356:1363	mtOXPHOS	1356:1363	We also found that Rab3A and its O-GlcNAcylation had opposite roles in mitochondria oxidative phosphorylation (mtOXPHOS), and their functions on HCC metastasis were partially depended on their effects on metabolic reprogramming.
30237463	8	4	theme	mitochondria	1316:1327	arg1	phosphorylation					1339:1353	mitochondria oxidative phosphorylation	1316:1353	mitochondria oxidative phosphorylation (mtOXPHOS)	1316:1364	We also found that Rab3A and its O-GlcNAcylation had opposite roles in mitochondria oxidative phosphorylation (mtOXPHOS), and their functions on HCC metastasis were partially depended on their effects on metabolic reprogramming.
30237463	5	5	theme	Rab3A	766:770	arg1	Meanwhile					735:743	Meanwhile	735:743	Meanwhile	735:743	Meanwhile, the upregulation of Rab3A in HCC patients did not correlate with metastasis or overall survival of HCC patients.
30237463	5	5	theme	Rab3A	766:770	arg1	upregulation					750:761	the upregulation	746:761	the upregulation of Rab3A in HCC patients	746:786	Meanwhile, the upregulation of Rab3A in HCC patients did not correlate with metastasis or overall survival of HCC patients.
30237463	0	6	theme	hepatocellular	109:122	arg1	carcinoma					124:132	hepatocellular carcinoma	109:132	hepatocellular carcinoma	109:132	O-GlcNAcylation on Rab3A attenuates its effects on mitochondrial oxidative phosphorylation and metastasis in hepatocellular carcinoma.
30237463	0	7	from	O-GlcNAcylation	0:14	arg1	Rab3A					19:23	Rab3A	19:23	Rab3A	19:23	O-GlcNAcylation on Rab3A attenuates its effects on mitochondrial oxidative phosphorylation and metastasis in hepatocellular carcinoma.
30237463	3	8	theme	Rab3A	389:393	arg1	roles					380:384	the potential roles	366:384	the potential roles of Rab3A in HCC progression	366:412	To investigate the potential roles of Rab3A in HCC progression, we first determined Rab3A levels in HCC tissues and observed upregulated mRNA and protein levels of Rab3A in most tumor tissues.
30237463	7	9	theme	aberrant	1180:1187	arg1	O-GlcNAcylation					1189:1203	its aberrant O-GlcNAcylation	1176:1203	its aberrant O-GlcNAcylation	1176:1203	Further experiments revealed that O-GlcNAcylation on Rab3A was key for attenuating Rab3A-mediated effects by regulating its GTP-binding activity, and verified the effects of Rab3A and its aberrant O-GlcNAcylation on HCC metastasis in vitro and in vivo.
30237463	3	10	theme	most	524:527	arg1	tissues					535:541	most tumor tissues	524:541	most tumor tissues	524:541	To investigate the potential roles of Rab3A in HCC progression, we first determined Rab3A levels in HCC tissues and observed upregulated mRNA and protein levels of Rab3A in most tumor tissues.
30237463	2	11	theme	Rab3A	283:287	arg1	roles					274:278	the roles	270:278	the roles of Rab3A in hepatocellular carcinoma (HCC)	270:321	Although the functions of Rab3A have been reported in several cancers, the roles of Rab3A in hepatocellular carcinoma (HCC) have never been determined.
30237463	8	12	from	functions	1377:1385	arg1	HCC					1390:1392	HCC	1390:1392	HCC	1390:1392	We also found that Rab3A and its O-GlcNAcylation had opposite roles in mitochondria oxidative phosphorylation (mtOXPHOS), and their functions on HCC metastasis were partially depended on their effects on metabolic reprogramming.
30237463	7	13	theme	Rab3A	1166:1170	arg1	effects					1155:1161	the effects	1151:1161	the effects of Rab3A and its aberrant O-GlcNAcylation on HCC metastasis	1151:1221	Further experiments revealed that O-GlcNAcylation on Rab3A was key for attenuating Rab3A-mediated effects by regulating its GTP-binding activity, and verified the effects of Rab3A and its aberrant O-GlcNAcylation on HCC metastasis in vitro and in vivo.
30237463	3	14	theme	HCC	451:453	arg1	tissues					455:461	HCC tissues	451:461	HCC tissues	451:461	To investigate the potential roles of Rab3A in HCC progression, we first determined Rab3A levels in HCC tissues and observed upregulated mRNA and protein levels of Rab3A in most tumor tissues.
30237463	8	15	theme	oxidative	1329:1337	arg1	mtOXPHOS					1356:1363	mtOXPHOS	1356:1363	mtOXPHOS	1356:1363	We also found that Rab3A and its O-GlcNAcylation had opposite roles in mitochondria oxidative phosphorylation (mtOXPHOS), and their functions on HCC metastasis were partially depended on their effects on metabolic reprogramming.
30237463	8	15	theme	oxidative	1329:1337	arg1	phosphorylation					1339:1353	mitochondria oxidative phosphorylation	1316:1353	mitochondria oxidative phosphorylation (mtOXPHOS)	1316:1364	We also found that Rab3A and its O-GlcNAcylation had opposite roles in mitochondria oxidative phosphorylation (mtOXPHOS), and their functions on HCC metastasis were partially depended on their effects on metabolic reprogramming.
30237463	5	16	theme	overall	825:831	arg1	survival					833:840	overall survival	825:840	overall survival	825:840	Meanwhile, the upregulation of Rab3A in HCC patients did not correlate with metastasis or overall survival of HCC patients.
30237463	7	17	theme	GTP-binding	1116:1126	arg1	activity					1128:1135	its GTP-binding activity	1112:1135	its GTP-binding activity	1112:1135	Further experiments revealed that O-GlcNAcylation on Rab3A was key for attenuating Rab3A-mediated effects by regulating its GTP-binding activity, and verified the effects of Rab3A and its aberrant O-GlcNAcylation on HCC metastasis in vitro and in vivo.
30237463	0	18	from	effects	40:46	arg1	metastasis					95:104	metastasis	95:104	metastasis	95:104	O-GlcNAcylation on Rab3A attenuates its effects on mitochondrial oxidative phosphorylation and metastasis in hepatocellular carcinoma.
30237463	0	18	from	effects	40:46	arg1	phosphorylation					75:89	mitochondrial oxidative phosphorylation	51:89	mitochondrial oxidative phosphorylation	51:89	O-GlcNAcylation on Rab3A attenuates its effects on mitochondrial oxidative phosphorylation and metastasis in hepatocellular carcinoma.
30237463	7	19	theme	Rab3A-mediated	1075:1088	arg1	effects					1090:1096	Rab3A-mediated effects	1075:1096	Rab3A-mediated effects	1075:1096	Further experiments revealed that O-GlcNAcylation on Rab3A was key for attenuating Rab3A-mediated effects by regulating its GTP-binding activity, and verified the effects of Rab3A and its aberrant O-GlcNAcylation on HCC metastasis in vitro and in vivo.
30237463	3	20	theme	Rab3A	515:519	arg1	levels					505:510	upregulated mRNA and protein levels	476:510	upregulated mRNA and protein levels of Rab3A in most tumor tissues	476:541	To investigate the potential roles of Rab3A in HCC progression, we first determined Rab3A levels in HCC tissues and observed upregulated mRNA and protein levels of Rab3A in most tumor tissues.
30237463	5	21	theme	HCC	775:777	arg1	patients					779:786	HCC patients	775:786	HCC patients	775:786	Meanwhile, the upregulation of Rab3A in HCC patients did not correlate with metastasis or overall survival of HCC patients.
30237463	8	22	from	effects	1438:1444	arg1	reprogramming					1459:1471	metabolic reprogramming	1449:1471	metabolic reprogramming	1449:1471	We also found that Rab3A and its O-GlcNAcylation had opposite roles in mitochondria oxidative phosphorylation (mtOXPHOS), and their functions on HCC metastasis were partially depended on their effects on metabolic reprogramming.
30237463	4	23	theme	significant	632:642	arg1	effects					644:650	no significant effects	629:650	no significant effects	629:650	However, in vitro data showed that decreasing Rab3A in most HCC cell lines conferred no significant effects and overexpressing Rab3A in PLC/PRF/5 cells even inhibited migration and invasion.
30237463	8	24	theme	metabolic	1449:1457	arg1	reprogramming					1459:1471	metabolic reprogramming	1449:1471	metabolic reprogramming	1449:1471	We also found that Rab3A and its O-GlcNAcylation had opposite roles in mitochondria oxidative phosphorylation (mtOXPHOS), and their functions on HCC metastasis were partially depended on their effects on metabolic reprogramming.
30237463	5	25	theme	HCC	845:847	arg1	patients					849:856	HCC patients	845:856	HCC patients	845:856	Meanwhile, the upregulation of Rab3A in HCC patients did not correlate with metastasis or overall survival of HCC patients.
30237463	8	26	contain	had	1294:1296	arg1	Rab3A					1264:1268	Rab3A	1264:1268	Rab3A	1264:1268	We also found that Rab3A and its O-GlcNAcylation had opposite roles in mitochondria oxidative phosphorylation (mtOXPHOS), and their functions on HCC metastasis were partially depended on their effects on metabolic reprogramming.
30237463	8	26	contain	had	1294:1296	arg2	roles					1307:1311	opposite roles	1298:1311	opposite roles in mitochondria oxidative phosphorylation (mtOXPHOS)	1298:1364	We also found that Rab3A and its O-GlcNAcylation had opposite roles in mitochondria oxidative phosphorylation (mtOXPHOS), and their functions on HCC metastasis were partially depended on their effects on metabolic reprogramming.
30237463	8	26	contain	had	1294:1296	arg1	O-GlcNAcylation					1278:1292	its O-GlcNAcylation	1274:1292	its O-GlcNAcylation	1274:1292	We also found that Rab3A and its O-GlcNAcylation had opposite roles in mitochondria oxidative phosphorylation (mtOXPHOS), and their functions on HCC metastasis were partially depended on their effects on metabolic reprogramming.
30237463	3	27	from	levels	505:510	arg1	tissues					535:541	most tumor tissues	524:541	most tumor tissues	524:541	To investigate the potential roles of Rab3A in HCC progression, we first determined Rab3A levels in HCC tissues and observed upregulated mRNA and protein levels of Rab3A in most tumor tissues.
30237463	3	28	theme	tumor	529:533	arg1	tissues					535:541	most tumor tissues	524:541	most tumor tissues	524:541	To investigate the potential roles of Rab3A in HCC progression, we first determined Rab3A levels in HCC tissues and observed upregulated mRNA and protein levels of Rab3A in most tumor tissues.
30237463	4	29	theme	most	599:602	arg1	lines					613:617	most HCC cell lines	599:617	most HCC cell lines conferred no significant effects	599:650	However, in vitro data showed that decreasing Rab3A in most HCC cell lines conferred no significant effects and overexpressing Rab3A in PLC/PRF/5 cells even inhibited migration and invasion.
30237463	3	30	theme	potential	370:378	arg1	roles					380:384	the potential roles	366:384	the potential roles of Rab3A in HCC progression	366:412	To investigate the potential roles of Rab3A in HCC progression, we first determined Rab3A levels in HCC tissues and observed upregulated mRNA and protein levels of Rab3A in most tumor tissues.
30237463	0	31	from	metastasis	95:104	arg1	carcinoma					124:132	hepatocellular carcinoma	109:132	hepatocellular carcinoma	109:132	O-GlcNAcylation on Rab3A attenuates its effects on mitochondrial oxidative phosphorylation and metastasis in hepatocellular carcinoma.
30237463	2	32	theme	hepatocellular	292:305	arg1	carcinoma					307:315	hepatocellular carcinoma	292:315	hepatocellular carcinoma (HCC)	292:321	Although the functions of Rab3A have been reported in several cancers, the roles of Rab3A in hepatocellular carcinoma (HCC) have never been determined.
30237463	2	32	theme	hepatocellular	292:305	arg1	HCC					318:320	HCC	318:320	HCC	318:320	Although the functions of Rab3A have been reported in several cancers, the roles of Rab3A in hepatocellular carcinoma (HCC) have never been determined.
30237463	1	33	theme	Ras-like	152:159	arg1	GTPase					161:166	a small Ras-like GTPase	144:166	a small Ras-like GTPase critical for membrane traffic	144:196	Rab3A is a small Ras-like GTPase critical for membrane traffic.
30237463	1	33	theme	Ras-like	152:159	arg1	Rab3A					135:139	Rab3A	135:139	Rab3A	135:139	Rab3A is a small Ras-like GTPase critical for membrane traffic.
30237463	3	34	theme	HCC	398:400	arg1	progression					402:412	HCC progression	398:412	HCC progression	398:412	To investigate the potential roles of Rab3A in HCC progression, we first determined Rab3A levels in HCC tissues and observed upregulated mRNA and protein levels of Rab3A in most tumor tissues.
30237463	8	35	dep	metastasis were	1394:1408	arg1	depended					1420:1427	depended	1420:1427	metastasis were partially depended on their effects on metabolic reprogramming	1394:1471	We also found that Rab3A and its O-GlcNAcylation had opposite roles in mitochondria oxidative phosphorylation (mtOXPHOS), and their functions on HCC metastasis were partially depended on their effects on metabolic reprogramming.
30237463	4	36	dep	in	553:554	arg1	vitro					556:560	vitro	556:560	vitro	556:560	However, in vitro data showed that decreasing Rab3A in most HCC cell lines conferred no significant effects and overexpressing Rab3A in PLC/PRF/5 cells even inhibited migration and invasion.
30237463	4	37	theme	cell	608:611	arg1	lines					613:617	most HCC cell lines	599:617	most HCC cell lines conferred no significant effects	599:650	However, in vitro data showed that decreasing Rab3A in most HCC cell lines conferred no significant effects and overexpressing Rab3A in PLC/PRF/5 cells even inhibited migration and invasion.
30237463	3	38	theme	Rab3A	435:439	arg1	levels					441:446	Rab3A levels	435:446	Rab3A levels in HCC tissues	435:461	To investigate the potential roles of Rab3A in HCC progression, we first determined Rab3A levels in HCC tissues and observed upregulated mRNA and protein levels of Rab3A in most tumor tissues.
30237463	6	39	theme	metastatic	915:924	arg1	suppressor					926:935	metastatic suppressor	915:935	metastatic suppressor	915:935	These contradict data suggested that Rab3A might act as metastatic suppressor and its effects might be attenuated in most HCC cells.
30237463	0	40	from	phosphorylation	75:89	arg1	carcinoma					124:132	hepatocellular carcinoma	109:132	hepatocellular carcinoma	109:132	O-GlcNAcylation on Rab3A attenuates its effects on mitochondrial oxidative phosphorylation and metastasis in hepatocellular carcinoma.
30237463	3	41	from	roles	380:384	arg1	progression					402:412	HCC progression	398:412	HCC progression	398:412	To investigate the potential roles of Rab3A in HCC progression, we first determined Rab3A levels in HCC tissues and observed upregulated mRNA and protein levels of Rab3A in most tumor tissues.
30237463	0	42	theme	mitochondrial	51:63	arg1	phosphorylation					75:89	mitochondrial oxidative phosphorylation	51:89	mitochondrial oxidative phosphorylation	51:89	O-GlcNAcylation on Rab3A attenuates its effects on mitochondrial oxidative phosphorylation and metastasis in hepatocellular carcinoma.
30237463	5	43	theme	patients	849:856	arg1	metastasis					811:820	metastasis	811:820	metastasis	811:820	Meanwhile, the upregulation of Rab3A in HCC patients did not correlate with metastasis or overall survival of HCC patients.
30237463	5	43	theme	patients	849:856	arg1	survival					833:840	overall survival	825:840	overall survival	825:840	Meanwhile, the upregulation of Rab3A in HCC patients did not correlate with metastasis or overall survival of HCC patients.
30237463	1	44	dep	membrane	181:188	arg1	traffic					190:196	traffic	190:196	traffic	190:196	Rab3A is a small Ras-like GTPase critical for membrane traffic.
30237463	3	45	from	levels	441:446	arg1	tissues					455:461	HCC tissues	451:461	HCC tissues	451:461	To investigate the potential roles of Rab3A in HCC progression, we first determined Rab3A levels in HCC tissues and observed upregulated mRNA and protein levels of Rab3A in most tumor tissues.
30237463	4	46	theme	PLC/PRF/5	680:688	arg1	cells					690:694	PLC/PRF/5 cells	680:694	PLC/PRF/5 cells	680:694	However, in vitro data showed that decreasing Rab3A in most HCC cell lines conferred no significant effects and overexpressing Rab3A in PLC/PRF/5 cells even inhibited migration and invasion.
30237463	2	47	theme	Rab3A	225:229	arg1	functions					212:220	the functions	208:220	the functions of Rab3A	208:229	Although the functions of Rab3A have been reported in several cancers, the roles of Rab3A in hepatocellular carcinoma (HCC) have never been determined.
30237463	3	48	theme	upregulated	476:486	arg1	levels					505:510	upregulated mRNA and protein levels	476:510	upregulated mRNA and protein levels of Rab3A in most tumor tissues	476:541	To investigate the potential roles of Rab3A in HCC progression, we first determined Rab3A levels in HCC tissues and observed upregulated mRNA and protein levels of Rab3A in most tumor tissues.
30237463	7	49	theme	Further	992:998	arg1	experiments					1000:1010	Further experiments	992:1010	Further experiments	992:1010	Further experiments revealed that O-GlcNAcylation on Rab3A was key for attenuating Rab3A-mediated effects by regulating its GTP-binding activity, and verified the effects of Rab3A and its aberrant O-GlcNAcylation on HCC metastasis in vitro and in vivo.
30237463	2	50	from	roles	274:278	arg1	carcinoma					307:315	hepatocellular carcinoma	292:315	hepatocellular carcinoma (HCC)	292:321	Although the functions of Rab3A have been reported in several cancers, the roles of Rab3A in hepatocellular carcinoma (HCC) have never been determined.
30237463	2	50	from	roles	274:278	arg1	HCC					318:320	HCC	318:320	HCC	318:320	Although the functions of Rab3A have been reported in several cancers, the roles of Rab3A in hepatocellular carcinoma (HCC) have never been determined.
30237463	7	51	from	effects	1155:1161	arg1	metastasis					1212:1221	HCC metastasis	1208:1221	HCC metastasis	1208:1221	Further experiments revealed that O-GlcNAcylation on Rab3A was key for attenuating Rab3A-mediated effects by regulating its GTP-binding activity, and verified the effects of Rab3A and its aberrant O-GlcNAcylation on HCC metastasis in vitro and in vivo.
30237463	1	52	theme	small	146:150	arg1	GTPase					161:166	a small Ras-like GTPase	144:166	a small Ras-like GTPase critical for membrane traffic	144:196	Rab3A is a small Ras-like GTPase critical for membrane traffic.
30237463	1	52	theme	small	146:150	arg1	Rab3A					135:139	Rab3A	135:139	Rab3A	135:139	Rab3A is a small Ras-like GTPase critical for membrane traffic.
30237463	8	53	theme	opposite	1298:1305	arg1	roles					1307:1311	opposite roles	1298:1311	opposite roles in mitochondria oxidative phosphorylation (mtOXPHOS)	1298:1364	We also found that Rab3A and its O-GlcNAcylation had opposite roles in mitochondria oxidative phosphorylation (mtOXPHOS), and their functions on HCC metastasis were partially depended on their effects on metabolic reprogramming.
30237463	7	54	theme	HCC	1208:1210	arg1	metastasis					1212:1221	HCC metastasis	1208:1221	HCC metastasis	1208:1221	Further experiments revealed that O-GlcNAcylation on Rab3A was key for attenuating Rab3A-mediated effects by regulating its GTP-binding activity, and verified the effects of Rab3A and its aberrant O-GlcNAcylation on HCC metastasis in vitro and in vivo.
30237463	4	55	theme	HCC	604:606	arg1	lines					613:617	most HCC cell lines	599:617	most HCC cell lines conferred no significant effects	599:650	However, in vitro data showed that decreasing Rab3A in most HCC cell lines conferred no significant effects and overexpressing Rab3A in PLC/PRF/5 cells even inhibited migration and invasion.
30237463	3	56	theme	protein	497:503	arg1	levels					505:510	upregulated mRNA and protein levels	476:510	upregulated mRNA and protein levels of Rab3A in most tumor tissues	476:541	To investigate the potential roles of Rab3A in HCC progression, we first determined Rab3A levels in HCC tissues and observed upregulated mRNA and protein levels of Rab3A in most tumor tissues.
30237463	8	57	from	roles	1307:1311	arg1	mtOXPHOS					1356:1363	mtOXPHOS	1356:1363	mtOXPHOS	1356:1363	We also found that Rab3A and its O-GlcNAcylation had opposite roles in mitochondria oxidative phosphorylation (mtOXPHOS), and their functions on HCC metastasis were partially depended on their effects on metabolic reprogramming.
30237463	8	57	from	roles	1307:1311	arg1	phosphorylation					1339:1353	mitochondria oxidative phosphorylation	1316:1353	mitochondria oxidative phosphorylation (mtOXPHOS)	1316:1364	We also found that Rab3A and its O-GlcNAcylation had opposite roles in mitochondria oxidative phosphorylation (mtOXPHOS), and their functions on HCC metastasis were partially depended on their effects on metabolic reprogramming.
30237463	6	58	theme	HCC	981:983	arg1	cells					985:989	most HCC cells	976:989	most HCC cells	976:989	These contradict data suggested that Rab3A might act as metastatic suppressor and its effects might be attenuated in most HCC cells.
30237463	0	59	theme	oxidative	65:73	arg1	phosphorylation					75:89	mitochondrial oxidative phosphorylation	51:89	mitochondrial oxidative phosphorylation	51:89	O-GlcNAcylation on Rab3A attenuates its effects on mitochondrial oxidative phosphorylation and metastasis in hepatocellular carcinoma.
30237463	1	60	theme	critical	168:175	arg1	GTPase					161:166	a small Ras-like GTPase	144:166	a small Ras-like GTPase critical for membrane traffic	144:196	Rab3A is a small Ras-like GTPase critical for membrane traffic.
30237463	1	60	theme	critical	168:175	arg1	Rab3A					135:139	Rab3A	135:139	Rab3A	135:139	Rab3A is a small Ras-like GTPase critical for membrane traffic.
30237463	2	61	theme	several	253:259	arg1	cancers					261:267	several cancers	253:267	several cancers	253:267	Although the functions of Rab3A have been reported in several cancers, the roles of Rab3A in hepatocellular carcinoma (HCC) have never been determined.
30237463	7	62	from	O-GlcNAcylation	1026:1040	arg1	Rab3A					1045:1049	Rab3A	1045:1049	Rab3A	1045:1049	Further experiments revealed that O-GlcNAcylation on Rab3A was key for attenuating Rab3A-mediated effects by regulating its GTP-binding activity, and verified the effects of Rab3A and its aberrant O-GlcNAcylation on HCC metastasis in vitro and in vivo.
30237463	6	63	theme	most	976:979	arg1	cells					985:989	most HCC cells	976:989	most HCC cells	976:989	These contradict data suggested that Rab3A might act as metastatic suppressor and its effects might be attenuated in most HCC cells.
18434435	3	0	theme	protective	323:332	arg1	O-GlcNAc					299:306	O-GlcNAc	299:306	O-GlcNAc	299:306	It has been recently speculated that O-GlcNAc could act as a protective signal against proteasomal degradation, both by modifying target substrates and/or by inhibiting the proteasome itself.
18434435	3	0	theme	protective	323:332	arg1	signal					334:339	a protective signal	321:339	a protective signal against proteasomal degradation	321:371	It has been recently speculated that O-GlcNAc could act as a protective signal against proteasomal degradation, both by modifying target substrates and/or by inhibiting the proteasome itself.
18434435	5	1	theme	ubiquitinated	660:672	arg1	proteins					674:681	ubiquitinated proteins	660:681	ubiquitinated proteins	660:681	First, we showed that the level of both modifications increased rapidly after thermal stress but, unlike ubiquitinated proteins, O-GlcNAc-modified proteins failed to be stabilized by inhibiting proteasome function.
18434435	5	2	theme	modifications	595:607	arg1	level					581:585	the level	577:585	the level of both modifications	577:607	First, we showed that the level of both modifications increased rapidly after thermal stress but, unlike ubiquitinated proteins, O-GlcNAc-modified proteins failed to be stabilized by inhibiting proteasome function.
18434435	5	3	theme	proteasome	749:758	arg1	function					760:767	proteasome function	749:767	proteasome function	749:767	First, we showed that the level of both modifications increased rapidly after thermal stress but, unlike ubiquitinated proteins, O-GlcNAc-modified proteins failed to be stabilized by inhibiting proteasome function.
18434435	10	4	theme	links	1510:1514	arg1	one					1492:1494	one	1492:1494	one	1492:1494	Altogether, these results show that O-GlcNAc and ubiquitin are not strictly antagonistic post-translational modifications, but rather that the former might regulate the latter, and also suggest that E1 could be one of the common links between the two pathways.
18434435	10	4	theme	links	1510:1514	arg1	links					1510:1514	the common links	1499:1514	the common links between the two pathways	1499:1539	Altogether, these results show that O-GlcNAc and ubiquitin are not strictly antagonistic post-translational modifications, but rather that the former might regulate the latter, and also suggest that E1 could be one of the common links between the two pathways.
18434435	9	5	theme	cell	1267:1270	arg1	culture					1272:1278	cell culture	1267:1278	cell culture	1267:1278	Finally, we demonstrated that the ubiquitin-activating enzyme E1 was O-GlcNAc modified and that its glycosylation and its interaction with Hsp70 varied according to the conditions of cell culture.
18434435	9	6	with	interaction	1206:1216	arg1	Hsp70					1223:1227	Hsp70	1223:1227	Hsp70	1223:1227	Finally, we demonstrated that the ubiquitin-activating enzyme E1 was O-GlcNAc modified and that its glycosylation and its interaction with Hsp70 varied according to the conditions of cell culture.
18434435	3	7	dep	act	314:316	arg1	inhibiting					420:429	inhibiting	420:429	inhibiting the proteasome itself	420:451	It has been recently speculated that O-GlcNAc could act as a protective signal against proteasomal degradation, both by modifying target substrates and/or by inhibiting the proteasome itself.
18434435	3	7	dep	act	314:316	arg1	modifying					382:390	modifying	382:390	modifying target substrates	382:408	It has been recently speculated that O-GlcNAc could act as a protective signal against proteasomal degradation, both by modifying target substrates and/or by inhibiting the proteasome itself.
18434435	10	8	theme	common	1503:1508	arg1	links					1510:1514	the common links	1499:1514	the common links between the two pathways	1499:1539	Altogether, these results show that O-GlcNAc and ubiquitin are not strictly antagonistic post-translational modifications, but rather that the former might regulate the latter, and also suggest that E1 could be one of the common links between the two pathways.
18434435	8	9	theme	cell	1062:1065	arg1	thermotolerance					1067:1081	moreover halved cell thermotolerance	1046:1081	moreover halved cell thermotolerance	1046:1081	Targeted-RNA interference of O-GlcNAc transferase also reduced ubiquitination and moreover halved cell thermotolerance.
18434435	5	10	theme	thermal	633:639	arg1	stress					641:646	thermal stress	633:646	thermal stress	633:646	First, we showed that the level of both modifications increased rapidly after thermal stress but, unlike ubiquitinated proteins, O-GlcNAc-modified proteins failed to be stabilized by inhibiting proteasome function.
18434435	8	11	theme	halved	1055:1060	arg1	thermotolerance					1067:1081	moreover halved cell thermotolerance	1046:1081	moreover halved cell thermotolerance	1046:1081	Targeted-RNA interference of O-GlcNAc transferase also reduced ubiquitination and moreover halved cell thermotolerance.
18434435	1	12	theme	past	74:77	arg1	decades					83:89	the past two decades	70:89	the past two decades	70:89	During the past two decades, O-GlcNAc modification of cytosolic and nuclear proteins has been intensively studied.
18434435	10	13	theme	post-translational	1370:1387	arg1	modifications					1389:1401	strictly antagonistic post-translational modifications	1348:1401	strictly antagonistic post-translational modifications	1348:1401	Altogether, these results show that O-GlcNAc and ubiquitin are not strictly antagonistic post-translational modifications, but rather that the former might regulate the latter, and also suggest that E1 could be one of the common links between the two pathways.
18434435	10	13	theme	post-translational	1370:1387	arg1	O-GlcNAc					1317:1324	O-GlcNAc	1317:1324	O-GlcNAc	1317:1324	Altogether, these results show that O-GlcNAc and ubiquitin are not strictly antagonistic post-translational modifications, but rather that the former might regulate the latter, and also suggest that E1 could be one of the common links between the two pathways.
18434435	10	13	theme	post-translational	1370:1387	arg1	ubiquitin					1330:1338	ubiquitin	1330:1338	ubiquitin	1330:1338	Altogether, these results show that O-GlcNAc and ubiquitin are not strictly antagonistic post-translational modifications, but rather that the former might regulate the latter, and also suggest that E1 could be one of the common links between the two pathways.
18434435	4	14	theme	putative	493:500	arg1	relation					502:509	the putative relation	489:509	the putative relation between O-GlcNAc and the ubiquitin pathway	489:552	In this work, we have investigated the putative relation between O-GlcNAc and the ubiquitin pathway.
18434435	10	15	theme	antagonistic	1357:1368	arg1	modifications					1389:1401	strictly antagonistic post-translational modifications	1348:1401	strictly antagonistic post-translational modifications	1348:1401	Altogether, these results show that O-GlcNAc and ubiquitin are not strictly antagonistic post-translational modifications, but rather that the former might regulate the latter, and also suggest that E1 could be one of the common links between the two pathways.
18434435	10	15	theme	antagonistic	1357:1368	arg1	O-GlcNAc					1317:1324	O-GlcNAc	1317:1324	O-GlcNAc	1317:1324	Altogether, these results show that O-GlcNAc and ubiquitin are not strictly antagonistic post-translational modifications, but rather that the former might regulate the latter, and also suggest that E1 could be one of the common links between the two pathways.
18434435	10	15	theme	antagonistic	1357:1368	arg1	ubiquitin					1330:1338	ubiquitin	1330:1338	ubiquitin	1330:1338	Altogether, these results show that O-GlcNAc and ubiquitin are not strictly antagonistic post-translational modifications, but rather that the former might regulate the latter, and also suggest that E1 could be one of the common links between the two pathways.
18434435	0	16	theme	Protein	0:6	arg1	ubiquitination					8:21	Protein ubiquitination	0:21	Protein ubiquitination	0:21	Protein ubiquitination is modulated by O-GlcNAc glycosylation.
18434435	7	17	theme	O-GlcNAc	868:875	arg1	levels					877:882	O-GlcNAc levels	868:882	O-GlcNAc levels	868:882	Inversely, when O-GlcNAc levels were reduced, using forskolin or glucose deprivation, ubiquitination decreased.
18434435	9	18	dep	enzyme	1139:1144	arg1	E1					1146:1147	E1	1146:1147	the ubiquitin-activating enzyme E1	1114:1147	Finally, we demonstrated that the ubiquitin-activating enzyme E1 was O-GlcNAc modified and that its glycosylation and its interaction with Hsp70 varied according to the conditions of cell culture.
18434435	1	19	theme	O-GlcNAc	92:99	arg1	modification					101:112	O-GlcNAc modification	92:112	O-GlcNAc modification of cytosolic and nuclear proteins	92:146	During the past two decades, O-GlcNAc modification of cytosolic and nuclear proteins has been intensively studied.
18434435	3	20	theme	target	392:397	arg1	substrates					399:408	target substrates	392:408	target substrates	392:408	It has been recently speculated that O-GlcNAc could act as a protective signal against proteasomal degradation, both by modifying target substrates and/or by inhibiting the proteasome itself.
18434435	9	21	theme	culture	1272:1278	arg1	conditions					1253:1262	the conditions	1249:1262	the conditions of cell culture	1249:1278	Finally, we demonstrated that the ubiquitin-activating enzyme E1 was O-GlcNAc modified and that its glycosylation and its interaction with Hsp70 varied according to the conditions of cell culture.
18434435	9	22	theme	ubiquitin-activating	1118:1137	arg1	enzyme					1139:1144	the ubiquitin-activating enzyme	1114:1144	the ubiquitin-activating enzyme E1	1114:1147	Finally, we demonstrated that the ubiquitin-activating enzyme E1 was O-GlcNAc modified and that its glycosylation and its interaction with Hsp70 varied according to the conditions of cell culture.
18434435	9	22	theme	ubiquitin-activating	1118:1137	arg1	modified					1162:1169	modified	1162:1169	modified	1162:1169	Finally, we demonstrated that the ubiquitin-activating enzyme E1 was O-GlcNAc modified and that its glycosylation and its interaction with Hsp70 varied according to the conditions of cell culture.
18434435	0	23	theme	O-GlcNAc	39:46	arg1	glycosylation					48:60	O-GlcNAc glycosylation	39:60	O-GlcNAc glycosylation	39:60	Protein ubiquitination is modulated by O-GlcNAc glycosylation.
18434435	4	24	theme	ubiquitin	536:544	arg1	pathway					546:552	the ubiquitin pathway	532:552	the ubiquitin pathway	532:552	In this work, we have investigated the putative relation between O-GlcNAc and the ubiquitin pathway.
18434435	5	25	theme	O-GlcNAc-modified	684:700	arg1	proteins					702:709	O-GlcNAc-modified proteins	684:709	O-GlcNAc-modified proteins	684:709	First, we showed that the level of both modifications increased rapidly after thermal stress but, unlike ubiquitinated proteins, O-GlcNAc-modified proteins failed to be stabilized by inhibiting proteasome function.
18434435	9	26	with	glycosylation	1184:1196	arg1	Hsp70					1223:1227	Hsp70	1223:1227	Hsp70	1223:1227	Finally, we demonstrated that the ubiquitin-activating enzyme E1 was O-GlcNAc modified and that its glycosylation and its interaction with Hsp70 varied according to the conditions of cell culture.
18434435	2	27	theme	modification	232:243	arg1	function					196:203	the function	192:203	the function of this post-translational modification	192:243	Nevertheless, the function of this post-translational modification remains unclear.
18434435	8	28	theme	Targeted-RNA	964:975	arg1	interference					977:988	Targeted-RNA interference	964:988	Targeted-RNA interference of O-GlcNAc transferase	964:1012	Targeted-RNA interference of O-GlcNAc transferase also reduced ubiquitination and moreover halved cell thermotolerance.
18434435	2	29	theme	post-translational	213:230	arg1	modification					232:243	this post-translational modification	208:243	this post-translational modification	208:243	Nevertheless, the function of this post-translational modification remains unclear.
18434435	8	30	theme	O-GlcNAc	993:1000	arg1	transferase					1002:1012	O-GlcNAc transferase	993:1012	O-GlcNAc transferase	993:1012	Targeted-RNA interference of O-GlcNAc transferase also reduced ubiquitination and moreover halved cell thermotolerance.
18434435	1	31	theme	cytosolic	117:125	arg1	proteins					139:146	cytosolic and nuclear proteins	117:146	cytosolic and nuclear proteins	117:146	During the past two decades, O-GlcNAc modification of cytosolic and nuclear proteins has been intensively studied.
18434435	1	32	mod	modification	101:112	arg3	O-GlcNAc					92:99	O-GlcNAc modification	92:112	O-GlcNAc modification of cytosolic and nuclear proteins	92:146	During the past two decades, O-GlcNAc modification of cytosolic and nuclear proteins has been intensively studied.
18434435	1	32	mod	modification	101:112	arg1	proteins					139:146	cytosolic and nuclear proteins	117:146	cytosolic and nuclear proteins	117:146	During the past two decades, O-GlcNAc modification of cytosolic and nuclear proteins has been intensively studied.
18434435	6	33	theme	O-GlcNAc	781:788	arg1	levels					790:795	Increasing O-GlcNAc levels	770:795	Increasing O-GlcNAc levels	770:795	Increasing O-GlcNAc levels, using glucosamine or PUGNAc, enhanced ubiquitination.
18434435	6	34	theme	Increasing	770:779	arg1	levels					790:795	Increasing O-GlcNAc levels	770:795	Increasing O-GlcNAc levels	770:795	Increasing O-GlcNAc levels, using glucosamine or PUGNAc, enhanced ubiquitination.
18434435	1	35	theme	nuclear	131:137	arg1	proteins					139:146	cytosolic and nuclear proteins	117:146	cytosolic and nuclear proteins	117:146	During the past two decades, O-GlcNAc modification of cytosolic and nuclear proteins has been intensively studied.
18434435	8	36	theme	transferase	1002:1012	arg1	interference					977:988	Targeted-RNA interference	964:988	Targeted-RNA interference of O-GlcNAc transferase	964:1012	Targeted-RNA interference of O-GlcNAc transferase also reduced ubiquitination and moreover halved cell thermotolerance.
18434435	1	37	theme	proteins	139:146	arg1	modification					101:112	O-GlcNAc modification	92:112	O-GlcNAc modification of cytosolic and nuclear proteins	92:146	During the past two decades, O-GlcNAc modification of cytosolic and nuclear proteins has been intensively studied.
18434435	3	38	theme	proteasomal	349:359	arg1	degradation					361:371	proteasomal degradation	349:371	proteasomal degradation	349:371	It has been recently speculated that O-GlcNAc could act as a protective signal against proteasomal degradation, both by modifying target substrates and/or by inhibiting the proteasome itself.
18434435	7	39	theme	glucose	917:923	arg1	deprivation					925:935	glucose deprivation	917:935	glucose deprivation	917:935	Inversely, when O-GlcNAc levels were reduced, using forskolin or glucose deprivation, ubiquitination decreased.
31235510	10	0	theme	RNA-binding	1129:1139	arg1	protein					1141:1147	RNA-binding protein	1129:1147	RNA-binding protein	1129:1147	Collectively, cav-1 is the first identified membranous protein that directly guides RNA-binding protein into EVs.
31235510	11	1	theme	innate	1302:1307	arg1	response					1316:1323	an innate immune response	1299:1323	an innate immune response	1299:1323	Our work delineates a novel mechanism by which oxidative stress compels epithelial cells to package and secrete specific miRNAs and elicits an innate immune response.
31235510	3	2	theme	plasma	475:480	arg1	membrane					482:489	the plasma membrane	471:489	the plasma membrane	471:489	We report that caveolin-1 (cav-1) is essential for sorting of selected miRNAs into microvesicles (MVs), a main type of EVs generated by outward budding of the plasma membrane.
31235510	3	3	theme	membrane	482:489	arg1	budding					460:466	outward budding	452:466	outward budding of the plasma membrane	452:489	We report that caveolin-1 (cav-1) is essential for sorting of selected miRNAs into microvesicles (MVs), a main type of EVs generated by outward budding of the plasma membrane.
31235510	11	4	theme	oxidative	1206:1214	arg1	stress					1216:1221	oxidative stress	1206:1221	oxidative stress compels epithelial cells	1206:1246	Our work delineates a novel mechanism by which oxidative stress compels epithelial cells to package and secrete specific miRNAs and elicits an innate immune response.
31235510	5	5	theme	cav-1/hnRNPA2B1	625:639	arg1	complex					641:647	The cav-1/hnRNPA2B1 complex	621:647	The cav-1/hnRNPA2B1 complex	621:647	The cav-1/hnRNPA2B1 complex subsequently traffics together into MVs.
31235510	11	6	theme	epithelial	1231:1240	arg1	cells					1242:1246	oxidative stress compels epithelial cells	1206:1246	oxidative stress compels epithelial cells	1206:1246	Our work delineates a novel mechanism by which oxidative stress compels epithelial cells to package and secrete specific miRNAs and elicits an innate immune response.
31235510	1	7	theme	intercellular	177:189	arg1	communications					191:204	intercellular communications	177:204	intercellular communications in response to noxious stimuli	177:235	Emerging evidence suggests that extracellular vesicle (EV)-containing miRNAs mediate intercellular communications in response to noxious stimuli.
31235510	9	8	theme	MV-containing	962:974	arg1	miR-17/93					1006:1014	MV-containing cav-1/hnRNPA2B1 complex-bound miR-17/93	962:1014	MV-containing cav-1/hnRNPA2B1 complex-bound miR-17/93	962:1014	MV-containing cav-1/hnRNPA2B1 complex-bound miR-17/93 activate tissue macrophages.
31235510	11	9	theme	stress	1216:1221	arg1	cells					1242:1246	oxidative stress compels epithelial cells	1206:1246	oxidative stress compels epithelial cells	1206:1246	Our work delineates a novel mechanism by which oxidative stress compels epithelial cells to package and secrete specific miRNAs and elicits an innate immune response.
31235510	6	10	theme	Oxidative	690:698	arg1	stress					700:705	Oxidative stress	690:705	Oxidative stress	690:705	Oxidative stress induces O-GlcNAcylation of hnRNPA2B1, resulting in a robustly altered hnRNPA2B1-bound miRNA repertoire.
31235510	3	11	theme	main	422:425	arg1	caveolin-1					331:340	caveolin-1	331:340	caveolin-1 (cav-1)	331:348	We report that caveolin-1 (cav-1) is essential for sorting of selected miRNAs into microvesicles (MVs), a main type of EVs generated by outward budding of the plasma membrane.
31235510	3	11	theme	main	422:425	arg1	type					427:430	a main type	420:430	a main type of EVs generated by outward budding of the plasma membrane	420:489	We report that caveolin-1 (cav-1) is essential for sorting of selected miRNAs into microvesicles (MVs), a main type of EVs generated by outward budding of the plasma membrane.
31235510	9	12	theme	cav-1/hnRNPA2B1	976:990	arg1	miR-17/93					1006:1014	MV-containing cav-1/hnRNPA2B1 complex-bound miR-17/93	962:1014	MV-containing cav-1/hnRNPA2B1 complex-bound miR-17/93	962:1014	MV-containing cav-1/hnRNPA2B1 complex-bound miR-17/93 activate tissue macrophages.
31235510	6	13	theme	miRNA	793:797	arg1	repertoire					799:808	a robustly altered hnRNPA2B1-bound miRNA repertoire	758:808	a robustly altered hnRNPA2B1-bound miRNA repertoire	758:808	Oxidative stress induces O-GlcNAcylation of hnRNPA2B1, resulting in a robustly altered hnRNPA2B1-bound miRNA repertoire.
31235510	2	14	theme	cellular	290:297	arg1	miRNAs					299:304	the cellular miRNAs	286:304	the cellular miRNAs	286:304	It remains unclear how a cell selectively sorts the cellular miRNAs into EVs.
31235510	7	15	theme	hnRNPA2B1	845:853	arg1	O-GlcNAcylation					855:869	hnRNPA2B1 O-GlcNAcylation	845:869	hnRNPA2B1 O-GlcNAcylation	845:869	Notably, cav-1 pY14 also promotes hnRNPA2B1 O-GlcNAcylation.
31235510	3	16	theme	miRNAs	387:392	arg1	sorting					367:373	sorting	367:373	sorting of selected miRNAs into microvesicles (MVs)	367:417	We report that caveolin-1 (cav-1) is essential for sorting of selected miRNAs into microvesicles (MVs), a main type of EVs generated by outward budding of the plasma membrane.
31235510	6	17	theme	hnRNPA2B1-bound	777:791	arg1	repertoire					799:808	a robustly altered hnRNPA2B1-bound miRNA repertoire	758:808	a robustly altered hnRNPA2B1-bound miRNA repertoire	758:808	Oxidative stress induces O-GlcNAcylation of hnRNPA2B1, resulting in a robustly altered hnRNPA2B1-bound miRNA repertoire.
31235510	10	18	theme	identified	1078:1087	arg1	cav-1					1059:1063	cav-1	1059:1063	cav-1	1059:1063	Collectively, cav-1 is the first identified membranous protein that directly guides RNA-binding protein into EVs.
31235510	10	18	theme	identified	1078:1087	arg1	protein					1100:1106	the first identified membranous protein	1068:1106	the first identified membranous protein that directly guides RNA-binding protein into EVs	1068:1156	Collectively, cav-1 is the first identified membranous protein that directly guides RNA-binding protein into EVs.
31235510	6	19	theme	altered	769:775	arg1	repertoire					799:808	a robustly altered hnRNPA2B1-bound miRNA repertoire	758:808	a robustly altered hnRNPA2B1-bound miRNA repertoire	758:808	Oxidative stress induces O-GlcNAcylation of hnRNPA2B1, resulting in a robustly altered hnRNPA2B1-bound miRNA repertoire.
31235510	8	20	theme	principal	911:919	arg1	recipient					921:929	the principal recipient	907:929	the principal recipient of epithelial MVs in the lung	907:959	Functionally, macrophages serve as the principal recipient of epithelial MVs in the lung.
31235510	8	20	theme	principal	911:919	arg1	macrophages					886:896	macrophages	886:896	macrophages	886:896	Functionally, macrophages serve as the principal recipient of epithelial MVs in the lung.
31235510	0	21	theme	microRNA	33:40	arg1	sorting					42:48	microRNA sorting	33:48	microRNA sorting into microvesicles after noxious stimuli	33:89	Caveolin-1 selectively regulates microRNA sorting into microvesicles after noxious stimuli.
31235510	11	22	theme	compels	1223:1229	arg1	cells					1242:1246	oxidative stress compels epithelial cells	1206:1246	oxidative stress compels epithelial cells	1206:1246	Our work delineates a novel mechanism by which oxidative stress compels epithelial cells to package and secrete specific miRNAs and elicits an innate immune response.
31235510	1	23	theme	noxious	221:227	arg1	stimuli					229:235	noxious stimuli	221:235	noxious stimuli	221:235	Emerging evidence suggests that extracellular vesicle (EV)-containing miRNAs mediate intercellular communications in response to noxious stimuli.
31235510	3	24	theme	selected	378:385	arg1	miRNAs					387:392	selected miRNAs	378:392	selected miRNAs	378:392	We report that caveolin-1 (cav-1) is essential for sorting of selected miRNAs into microvesicles (MVs), a main type of EVs generated by outward budding of the plasma membrane.
31235510	1	25	theme	extracellular	124:136	arg1	miRNAs					162:167	extracellular vesicle (EV)-containing miRNAs	124:167	extracellular vesicle (EV)-containing miRNAs	124:167	Emerging evidence suggests that extracellular vesicle (EV)-containing miRNAs mediate intercellular communications in response to noxious stimuli.
31235510	7	26	theme	cav-1	820:824	arg1	pY14					826:829	cav-1 pY14	820:829	cav-1 pY14	820:829	Notably, cav-1 pY14 also promotes hnRNPA2B1 O-GlcNAcylation.
31235510	4	27	theme	Y14	525:527	arg1	-phosphorylation					529:544	cav-1 tyrosine 14 (Y14)-phosphorylation	506:544	cav-1 tyrosine 14 (Y14)-phosphorylation	506:544	We found that cav-1 tyrosine 14 (Y14)-phosphorylation leads to interactions between cav-1 and hnRNPA2B1, an RNA-binding protein.
31235510	11	28	theme	specific	1271:1278	arg1	miRNAs					1280:1285	specific miRNAs	1271:1285	specific miRNAs	1271:1285	Our work delineates a novel mechanism by which oxidative stress compels epithelial cells to package and secrete specific miRNAs and elicits an innate immune response.
31235510	11	29	theme	novel	1181:1185	arg1	mechanism					1187:1195	a novel mechanism	1179:1195	a novel mechanism by which oxidative stress compels epithelial cells to package and secrete specific miRNAs	1179:1285	Our work delineates a novel mechanism by which oxidative stress compels epithelial cells to package and secrete specific miRNAs and elicits an innate immune response.
31235510	8	30	theme	MVs	945:947	arg1	recipient					921:929	the principal recipient	907:929	the principal recipient of epithelial MVs in the lung	907:959	Functionally, macrophages serve as the principal recipient of epithelial MVs in the lung.
31235510	8	30	theme	MVs	945:947	arg1	macrophages					886:896	macrophages	886:896	macrophages	886:896	Functionally, macrophages serve as the principal recipient of epithelial MVs in the lung.
31235510	4	31	theme	RNA-binding	600:610	arg1	cav-1					576:580	cav-1	576:580	cav-1	576:580	We found that cav-1 tyrosine 14 (Y14)-phosphorylation leads to interactions between cav-1 and hnRNPA2B1, an RNA-binding protein.
31235510	4	31	theme	RNA-binding	600:610	arg1	protein					612:618	an RNA-binding protein	597:618	an RNA-binding protein	597:618	We found that cav-1 tyrosine 14 (Y14)-phosphorylation leads to interactions between cav-1 and hnRNPA2B1, an RNA-binding protein.
31235510	11	32	theme	immune	1309:1314	arg1	response					1316:1323	an innate immune response	1299:1323	an innate immune response	1299:1323	Our work delineates a novel mechanism by which oxidative stress compels epithelial cells to package and secrete specific miRNAs and elicits an innate immune response.
31235510	8	33	theme	epithelial	934:943	arg1	MVs					945:947	epithelial MVs	934:947	epithelial MVs	934:947	Functionally, macrophages serve as the principal recipient of epithelial MVs in the lung.
31235510	4	34	theme	tyrosine	512:519	arg1	-phosphorylation					529:544	cav-1 tyrosine 14 (Y14)-phosphorylation	506:544	cav-1 tyrosine 14 (Y14)-phosphorylation	506:544	We found that cav-1 tyrosine 14 (Y14)-phosphorylation leads to interactions between cav-1 and hnRNPA2B1, an RNA-binding protein.
31235510	3	35	dep	essential	353:361	arg1	caveolin-1					331:340	caveolin-1	331:340	caveolin-1 (cav-1)	331:348	We report that caveolin-1 (cav-1) is essential for sorting of selected miRNAs into microvesicles (MVs), a main type of EVs generated by outward budding of the plasma membrane.
31235510	3	35	dep	essential	353:361	arg1	type					427:430	a main type	420:430	a main type of EVs generated by outward budding of the plasma membrane	420:489	We report that caveolin-1 (cav-1) is essential for sorting of selected miRNAs into microvesicles (MVs), a main type of EVs generated by outward budding of the plasma membrane.
31235510	4	36	theme	cav-1	506:510	arg1	-phosphorylation					529:544	cav-1 tyrosine 14 (Y14)-phosphorylation	506:544	cav-1 tyrosine 14 (Y14)-phosphorylation	506:544	We found that cav-1 tyrosine 14 (Y14)-phosphorylation leads to interactions between cav-1 and hnRNPA2B1, an RNA-binding protein.
31235510	3	37	theme	outward	452:458	arg1	budding					460:466	outward budding	452:466	outward budding of the plasma membrane	452:489	We report that caveolin-1 (cav-1) is essential for sorting of selected miRNAs into microvesicles (MVs), a main type of EVs generated by outward budding of the plasma membrane.
31235510	1	38	theme	Emerging	92:99	arg1	evidence					101:108	Emerging evidence	92:108	Emerging evidence	92:108	Emerging evidence suggests that extracellular vesicle (EV)-containing miRNAs mediate intercellular communications in response to noxious stimuli.
31235510	10	39	theme	membranous	1089:1098	arg1	cav-1					1059:1063	cav-1	1059:1063	cav-1	1059:1063	Collectively, cav-1 is the first identified membranous protein that directly guides RNA-binding protein into EVs.
31235510	10	39	theme	membranous	1089:1098	arg1	protein					1100:1106	the first identified membranous protein	1068:1106	the first identified membranous protein that directly guides RNA-binding protein into EVs	1068:1156	Collectively, cav-1 is the first identified membranous protein that directly guides RNA-binding protein into EVs.
31235510	8	40	from	recipient	921:929	arg1	lung					956:959	the lung	952:959	the lung	952:959	Functionally, macrophages serve as the principal recipient of epithelial MVs in the lung.
31235510	6	41	theme	hnRNPA2B1	734:742	arg1	O-GlcNAcylation					715:729	O-GlcNAcylation	715:729	O-GlcNAcylation of hnRNPA2B1	715:742	Oxidative stress induces O-GlcNAcylation of hnRNPA2B1, resulting in a robustly altered hnRNPA2B1-bound miRNA repertoire.
31235510	3	42	theme	EVs	435:437	arg1	caveolin-1					331:340	caveolin-1	331:340	caveolin-1 (cav-1)	331:348	We report that caveolin-1 (cav-1) is essential for sorting of selected miRNAs into microvesicles (MVs), a main type of EVs generated by outward budding of the plasma membrane.
31235510	3	42	theme	EVs	435:437	arg1	type					427:430	a main type	420:430	a main type of EVs generated by outward budding of the plasma membrane	420:489	We report that caveolin-1 (cav-1) is essential for sorting of selected miRNAs into microvesicles (MVs), a main type of EVs generated by outward budding of the plasma membrane.
31235510	1	43	theme	-containing	150:160	arg1	miRNAs					162:167	extracellular vesicle (EV)-containing miRNAs	124:167	extracellular vesicle (EV)-containing miRNAs	124:167	Emerging evidence suggests that extracellular vesicle (EV)-containing miRNAs mediate intercellular communications in response to noxious stimuli.
31235510	0	44	theme	noxious	75:81	arg1	stimuli					83:89	noxious stimuli	75:89	noxious stimuli	75:89	Caveolin-1 selectively regulates microRNA sorting into microvesicles after noxious stimuli.
31235510	9	45	theme	tissue	1025:1030	arg1	macrophages					1032:1042	tissue macrophages	1025:1042	tissue macrophages	1025:1042	MV-containing cav-1/hnRNPA2B1 complex-bound miR-17/93 activate tissue macrophages.
31235510	1	46	from	communications	191:204	arg1	response					209:216	response	209:216	response to noxious stimuli	209:235	Emerging evidence suggests that extracellular vesicle (EV)-containing miRNAs mediate intercellular communications in response to noxious stimuli.
31235510	9	47	theme	complex-bound	992:1004	arg1	miR-17/93					1006:1014	MV-containing cav-1/hnRNPA2B1 complex-bound miR-17/93	962:1014	MV-containing cav-1/hnRNPA2B1 complex-bound miR-17/93	962:1014	MV-containing cav-1/hnRNPA2B1 complex-bound miR-17/93 activate tissue macrophages.
30853214	5	0	theme	post-translational	770:787	arg1	modification					789:800	This post-translational modification	765:800	This post-translational modification	765:800	This post-translational modification specifically compromises the ribonucleotide reductase (RNR) activity, leading to deficiency in dNTP pools, genomic DNA alterations with KRAS mutations, and cellular transformation.
30853214	4	1	theme	phosphofructokinase	707:725	arg1	activity					733:740	lower phosphofructokinase (PFK) activity	701:740	lower phosphofructokinase (PFK) activity than other cell types	701:762	Here, we show that under high-glucose conditions, cellular O-GlcNAcylation is significantly elevated in pancreatic cells that exhibit lower phosphofructokinase (PFK) activity than other cell types.
30853214	1	2	theme	earliest	152:159	arg1	mutations					134:142	KRAS mutations	129:142	KRAS mutations	129:142	KRAS mutations are the earliest events found in approximately 90% of pancreatic ductal adenocarcinomas (PDACs).
30853214	1	2	theme	earliest	152:159	arg1	events					161:166	the earliest events	148:166	the earliest events found in approximately 90% of pancreatic ductal adenocarcinomas (PDACs)	148:238	KRAS mutations are the earliest events found in approximately 90% of pancreatic ductal adenocarcinomas (PDACs).
30853214	5	3	with	alterations	921:931	arg1	mutations					943:951	KRAS mutations	938:951	KRAS mutations	938:951	This post-translational modification specifically compromises the ribonucleotide reductase (RNR) activity, leading to deficiency in dNTP pools, genomic DNA alterations with KRAS mutations, and cellular transformation.
30853214	5	4	theme	DNA	917:919	arg1	alterations					921:931	genomic DNA alterations	909:931	genomic DNA alterations with KRAS mutations	909:951	This post-translational modification specifically compromises the ribonucleotide reductase (RNR) activity, leading to deficiency in dNTP pools, genomic DNA alterations with KRAS mutations, and cellular transformation.
30853214	3	5	theme	direct	495:500	arg1	relationship					502:513	a direct relationship	493:513	a direct relationship between KRAS mutations and sugar metabolism	493:557	While abnormal carbohydrate metabolism is associated with a high risk of pancreatic cancer, it remains elusive whether a direct relationship between KRAS mutations and sugar metabolism exists.
30853214	5	6	from	alterations	921:931	arg1	pools					902:906	dNTP pools	897:906	dNTP pools	897:906	This post-translational modification specifically compromises the ribonucleotide reductase (RNR) activity, leading to deficiency in dNTP pools, genomic DNA alterations with KRAS mutations, and cellular transformation.
30853214	0	7	theme	KRAS	94:97	arg1	Mutation					99:106	KRAS Mutation	94:106	KRAS Mutation	94:106	High Glucose Triggers Nucleotide Imbalance through O-GlcNAcylation of Key Enzymes and Induces KRAS Mutation in Pancreatic Cells.
30853214	3	8	theme	sugar	542:546	arg1	metabolism					548:557	sugar metabolism	542:557	sugar metabolism	542:557	While abnormal carbohydrate metabolism is associated with a high risk of pancreatic cancer, it remains elusive whether a direct relationship between KRAS mutations and sugar metabolism exists.
30853214	5	9	with	transformation	967:980	arg1	mutations					943:951	KRAS mutations	938:951	KRAS mutations	938:951	This post-translational modification specifically compromises the ribonucleotide reductase (RNR) activity, leading to deficiency in dNTP pools, genomic DNA alterations with KRAS mutations, and cellular transformation.
30853214	0	10	theme	Pancreatic	111:120	arg1	Cells					122:126	Pancreatic Cells	111:126	Pancreatic Cells	111:126	High Glucose Triggers Nucleotide Imbalance through O-GlcNAcylation of Key Enzymes and Induces KRAS Mutation in Pancreatic Cells.
30853214	3	11	theme	high	434:437	arg1	risk					439:442	a high risk	432:442	a high risk of pancreatic cancer	432:463	While abnormal carbohydrate metabolism is associated with a high risk of pancreatic cancer, it remains elusive whether a direct relationship between KRAS mutations and sugar metabolism exists.
30853214	6	12	theme	mechanistic	1009:1019	arg1	link					1021:1024	a mechanistic link	1007:1024	a mechanistic link between a perturbed sugar metabolism and genomic instability that induces de novo oncogenic KRAS mutations preferentially in pancreatic cells	1007:1166	These results establish a mechanistic link between a perturbed sugar metabolism and genomic instability that induces de novo oncogenic KRAS mutations preferentially in pancreatic cells.
30853214	4	13	gly	O-GlcNAcylation	626:640	arg1	cells					682:686	pancreatic cells	671:686	pancreatic cells that exhibit lower phosphofructokinase (PFK) activity than other cell types	671:762	Here, we show that under high-glucose conditions, cellular O-GlcNAcylation is significantly elevated in pancreatic cells that exhibit lower phosphofructokinase (PFK) activity than other cell types.
30853214	0	14	theme	High	0:3	arg1	Glucose					5:11	High Glucose	0:11	High Glucose	0:11	High Glucose Triggers Nucleotide Imbalance through O-GlcNAcylation of Key Enzymes and Induces KRAS Mutation in Pancreatic Cells.
30853214	6	15	theme	oncogenic	1108:1116	arg1	mutations					1123:1131	de novo oncogenic KRAS mutations	1100:1131	de novo oncogenic KRAS mutations	1100:1131	These results establish a mechanistic link between a perturbed sugar metabolism and genomic instability that induces de novo oncogenic KRAS mutations preferentially in pancreatic cells.
30853214	5	16	theme	reductase	846:854	arg1	activity					862:869	the ribonucleotide reductase (RNR) activity	827:869	the ribonucleotide reductase (RNR) activity	827:869	This post-translational modification specifically compromises the ribonucleotide reductase (RNR) activity, leading to deficiency in dNTP pools, genomic DNA alterations with KRAS mutations, and cellular transformation.
30853214	4	17	theme	other	747:751	arg1	types					758:762	other cell types	747:762	other cell types	747:762	Here, we show that under high-glucose conditions, cellular O-GlcNAcylation is significantly elevated in pancreatic cells that exhibit lower phosphofructokinase (PFK) activity than other cell types.
30853214	5	18	theme	dNTP	897:900	arg1	pools					902:906	dNTP pools	897:906	dNTP pools	897:906	This post-translational modification specifically compromises the ribonucleotide reductase (RNR) activity, leading to deficiency in dNTP pools, genomic DNA alterations with KRAS mutations, and cellular transformation.
30853214	3	19	theme	abnormal	380:387	arg1	metabolism					402:411	abnormal carbohydrate metabolism	380:411	abnormal carbohydrate metabolism	380:411	While abnormal carbohydrate metabolism is associated with a high risk of pancreatic cancer, it remains elusive whether a direct relationship between KRAS mutations and sugar metabolism exists.
30853214	5	20	theme	cellular	958:965	arg1	transformation					967:980	cellular transformation	958:980	cellular transformation	958:980	This post-translational modification specifically compromises the ribonucleotide reductase (RNR) activity, leading to deficiency in dNTP pools, genomic DNA alterations with KRAS mutations, and cellular transformation.
30853214	4	21	theme	pancreatic	671:680	arg1	cells					682:686	pancreatic cells	671:686	pancreatic cells that exhibit lower phosphofructokinase (PFK) activity than other cell types	671:762	Here, we show that under high-glucose conditions, cellular O-GlcNAcylation is significantly elevated in pancreatic cells that exhibit lower phosphofructokinase (PFK) activity than other cell types.
30853214	0	22	theme	Nucleotide	22:31	arg1	Imbalance					33:41	Nucleotide Imbalance	22:41	Nucleotide Imbalance	22:41	High Glucose Triggers Nucleotide Imbalance through O-GlcNAcylation of Key Enzymes and Induces KRAS Mutation in Pancreatic Cells.
30853214	2	23	theme	KRAS	276:279	arg1	mutations					281:289	KRAS mutations	276:289	KRAS mutations	276:289	However, little is known as to why KRAS mutations preferentially occur in PDACs and what processes/factors generate these mutations.
30853214	3	24	theme	cancer	458:463	arg1	risk					439:442	a high risk	432:442	a high risk of pancreatic cancer	432:463	While abnormal carbohydrate metabolism is associated with a high risk of pancreatic cancer, it remains elusive whether a direct relationship between KRAS mutations and sugar metabolism exists.
30853214	6	25	dep	de	1100:1101	arg1	novo					1103:1106	novo	1103:1106	novo	1103:1106	These results establish a mechanistic link between a perturbed sugar metabolism and genomic instability that induces de novo oncogenic KRAS mutations preferentially in pancreatic cells.
30853214	4	26	theme	cell	753:756	arg1	types					758:762	other cell types	747:762	other cell types	747:762	Here, we show that under high-glucose conditions, cellular O-GlcNAcylation is significantly elevated in pancreatic cells that exhibit lower phosphofructokinase (PFK) activity than other cell types.
30853214	4	27	theme	cellular	617:624	arg1	O-GlcNAcylation					626:640	cellular O-GlcNAcylation	617:640	cellular O-GlcNAcylation	617:640	Here, we show that under high-glucose conditions, cellular O-GlcNAcylation is significantly elevated in pancreatic cells that exhibit lower phosphofructokinase (PFK) activity than other cell types.
30853214	1	28	located	found	168:172	arg2	events					161:166	the earliest events	148:166	the earliest events found in approximately 90% of pancreatic ductal adenocarcinomas (PDACs)	148:238	KRAS mutations are the earliest events found in approximately 90% of pancreatic ductal adenocarcinomas (PDACs).
30853214	1	28	located	found	168:172	arg1	PDACs					233:237	PDACs	233:237	PDACs	233:237	KRAS mutations are the earliest events found in approximately 90% of pancreatic ductal adenocarcinomas (PDACs).
30853214	1	28	located	found	168:172	arg1	adenocarcinomas					216:230	pancreatic ductal adenocarcinomas	198:230	pancreatic ductal adenocarcinomas (PDACs)	198:238	KRAS mutations are the earliest events found in approximately 90% of pancreatic ductal adenocarcinomas (PDACs).
30853214	1	28	located	found	168:172	arg2	mutations					134:142	KRAS mutations	129:142	KRAS mutations	129:142	KRAS mutations are the earliest events found in approximately 90% of pancreatic ductal adenocarcinomas (PDACs).
30853214	1	28	located	found	168:172	arg1	%					193:193	approximately 90%	177:193	approximately 90% of pancreatic ductal adenocarcinomas (PDACs)	177:238	KRAS mutations are the earliest events found in approximately 90% of pancreatic ductal adenocarcinomas (PDACs).
30853214	6	29	theme	de	1100:1101	arg1	mutations					1123:1131	de novo oncogenic KRAS mutations	1100:1131	de novo oncogenic KRAS mutations	1100:1131	These results establish a mechanistic link between a perturbed sugar metabolism and genomic instability that induces de novo oncogenic KRAS mutations preferentially in pancreatic cells.
30853214	1	30	theme	pancreatic	198:207	arg1	PDACs					233:237	PDACs	233:237	PDACs	233:237	KRAS mutations are the earliest events found in approximately 90% of pancreatic ductal adenocarcinomas (PDACs).
30853214	1	30	theme	pancreatic	198:207	arg1	adenocarcinomas					216:230	pancreatic ductal adenocarcinomas	198:230	pancreatic ductal adenocarcinomas (PDACs)	198:238	KRAS mutations are the earliest events found in approximately 90% of pancreatic ductal adenocarcinomas (PDACs).
30853214	6	31	theme	KRAS	1118:1121	arg1	mutations					1123:1131	de novo oncogenic KRAS mutations	1100:1131	de novo oncogenic KRAS mutations	1100:1131	These results establish a mechanistic link between a perturbed sugar metabolism and genomic instability that induces de novo oncogenic KRAS mutations preferentially in pancreatic cells.
30853214	3	32	theme	pancreatic	447:456	arg1	cancer					458:463	pancreatic cancer	447:463	pancreatic cancer	447:463	While abnormal carbohydrate metabolism is associated with a high risk of pancreatic cancer, it remains elusive whether a direct relationship between KRAS mutations and sugar metabolism exists.
30853214	3	33	theme	carbohydrate	389:400	arg1	metabolism					402:411	abnormal carbohydrate metabolism	380:411	abnormal carbohydrate metabolism	380:411	While abnormal carbohydrate metabolism is associated with a high risk of pancreatic cancer, it remains elusive whether a direct relationship between KRAS mutations and sugar metabolism exists.
30853214	6	34	theme	genomic	1067:1073	arg1	instability					1075:1085	genomic instability	1067:1085	genomic instability	1067:1085	These results establish a mechanistic link between a perturbed sugar metabolism and genomic instability that induces de novo oncogenic KRAS mutations preferentially in pancreatic cells.
30853214	3	35	dep	KRAS	523:526	arg1	mutations					528:536	mutations	528:536	mutations	528:536	While abnormal carbohydrate metabolism is associated with a high risk of pancreatic cancer, it remains elusive whether a direct relationship between KRAS mutations and sugar metabolism exists.
30853214	5	36	theme	ribonucleotide	831:844	arg1	RNR					857:859	RNR	857:859	RNR	857:859	This post-translational modification specifically compromises the ribonucleotide reductase (RNR) activity, leading to deficiency in dNTP pools, genomic DNA alterations with KRAS mutations, and cellular transformation.
30853214	5	36	theme	ribonucleotide	831:844	arg1	reductase					846:854	ribonucleotide reductase	831:854	the ribonucleotide reductase (RNR) activity	827:869	This post-translational modification specifically compromises the ribonucleotide reductase (RNR) activity, leading to deficiency in dNTP pools, genomic DNA alterations with KRAS mutations, and cellular transformation.
30853214	5	37	theme	KRAS	938:941	arg1	mutations					943:951	KRAS mutations	938:951	KRAS mutations	938:951	This post-translational modification specifically compromises the ribonucleotide reductase (RNR) activity, leading to deficiency in dNTP pools, genomic DNA alterations with KRAS mutations, and cellular transformation.
30853214	5	38	from	transformation	967:980	arg1	pools					902:906	dNTP pools	897:906	dNTP pools	897:906	This post-translational modification specifically compromises the ribonucleotide reductase (RNR) activity, leading to deficiency in dNTP pools, genomic DNA alterations with KRAS mutations, and cellular transformation.
30853214	5	39	with	deficiency	883:892	arg1	mutations					943:951	KRAS mutations	938:951	KRAS mutations	938:951	This post-translational modification specifically compromises the ribonucleotide reductase (RNR) activity, leading to deficiency in dNTP pools, genomic DNA alterations with KRAS mutations, and cellular transformation.
30853214	1	40	theme	KRAS	129:132	arg1	mutations					134:142	KRAS mutations	129:142	KRAS mutations	129:142	KRAS mutations are the earliest events found in approximately 90% of pancreatic ductal adenocarcinomas (PDACs).
30853214	1	40	theme	KRAS	129:132	arg1	events					161:166	the earliest events	148:166	the earliest events found in approximately 90% of pancreatic ductal adenocarcinomas (PDACs)	148:238	KRAS mutations are the earliest events found in approximately 90% of pancreatic ductal adenocarcinomas (PDACs).
30853214	4	41	theme	lower	701:705	arg1	activity					733:740	lower phosphofructokinase (PFK) activity	701:740	lower phosphofructokinase (PFK) activity than other cell types	701:762	Here, we show that under high-glucose conditions, cellular O-GlcNAcylation is significantly elevated in pancreatic cells that exhibit lower phosphofructokinase (PFK) activity than other cell types.
30853214	1	42	theme	adenocarcinomas	216:230	arg1	PDACs					233:237	PDACs	233:237	PDACs	233:237	KRAS mutations are the earliest events found in approximately 90% of pancreatic ductal adenocarcinomas (PDACs).
30853214	1	42	theme	adenocarcinomas	216:230	arg1	adenocarcinomas					216:230	pancreatic ductal adenocarcinomas	198:230	pancreatic ductal adenocarcinomas (PDACs)	198:238	KRAS mutations are the earliest events found in approximately 90% of pancreatic ductal adenocarcinomas (PDACs).
30853214	1	42	theme	adenocarcinomas	216:230	arg1	%					193:193	approximately 90%	177:193	approximately 90% of pancreatic ductal adenocarcinomas (PDACs)	177:238	KRAS mutations are the earliest events found in approximately 90% of pancreatic ductal adenocarcinomas (PDACs).
30853214	5	43	theme	genomic	909:915	arg1	alterations					921:931	genomic DNA alterations	909:931	genomic DNA alterations with KRAS mutations	909:951	This post-translational modification specifically compromises the ribonucleotide reductase (RNR) activity, leading to deficiency in dNTP pools, genomic DNA alterations with KRAS mutations, and cellular transformation.
30853214	0	44	theme	Enzymes	74:80	arg1	O-GlcNAcylation					51:65	O-GlcNAcylation	51:65	O-GlcNAcylation of Key Enzymes	51:80	High Glucose Triggers Nucleotide Imbalance through O-GlcNAcylation of Key Enzymes and Induces KRAS Mutation in Pancreatic Cells.
30853214	1	45	theme	ductal	209:214	arg1	PDACs					233:237	PDACs	233:237	PDACs	233:237	KRAS mutations are the earliest events found in approximately 90% of pancreatic ductal adenocarcinomas (PDACs).
30853214	1	45	theme	ductal	209:214	arg1	adenocarcinomas					216:230	pancreatic ductal adenocarcinomas	198:230	pancreatic ductal adenocarcinomas (PDACs)	198:238	KRAS mutations are the earliest events found in approximately 90% of pancreatic ductal adenocarcinomas (PDACs).
30853214	6	46	theme	pancreatic	1151:1160	arg1	cells					1162:1166	pancreatic cells	1151:1166	pancreatic cells	1151:1166	These results establish a mechanistic link between a perturbed sugar metabolism and genomic instability that induces de novo oncogenic KRAS mutations preferentially in pancreatic cells.
30853214	6	47	theme	sugar	1046:1050	arg1	metabolism					1052:1061	sugar metabolism	1046:1061	sugar metabolism	1046:1061	These results establish a mechanistic link between a perturbed sugar metabolism and genomic instability that induces de novo oncogenic KRAS mutations preferentially in pancreatic cells.
30853214	0	48	theme	Key	70:72	arg1	Enzymes					74:80	Key Enzymes	70:80	Key Enzymes	70:80	High Glucose Triggers Nucleotide Imbalance through O-GlcNAcylation of Key Enzymes and Induces KRAS Mutation in Pancreatic Cells.
30853214	5	49	from	deficiency	883:892	arg1	pools					902:906	dNTP pools	897:906	dNTP pools	897:906	This post-translational modification specifically compromises the ribonucleotide reductase (RNR) activity, leading to deficiency in dNTP pools, genomic DNA alterations with KRAS mutations, and cellular transformation.
30853214	4	50	theme	high-glucose	592:603	arg1	conditions					605:614	high-glucose conditions	592:614	high-glucose conditions	592:614	Here, we show that under high-glucose conditions, cellular O-GlcNAcylation is significantly elevated in pancreatic cells that exhibit lower phosphofructokinase (PFK) activity than other cell types.
30853214	6	51	theme	perturbed	1036:1044	arg1	metabolism					1052:1061	sugar metabolism	1046:1061	sugar metabolism	1046:1061	These results establish a mechanistic link between a perturbed sugar metabolism and genomic instability that induces de novo oncogenic KRAS mutations preferentially in pancreatic cells.
22605332	8	0	theme	unexpected	992:1001	arg1	roles					1003:1007	unexpected roles	992:1007	unexpected roles for both the CTD and O-GlcNAc in the regulation of transcription initiation in higher eukaryotes	992:1104	Our results define unexpected roles for both the CTD and O-GlcNAc in the regulation of transcription initiation in higher eukaryotes.
22605332	6	1	theme	RNA	787:789	arg1	polymerase					791:800	RNA polymerase II	787:803	RNA polymerase II occupancy at several B-cell promoters	787:841	OGT shRNA experiments showed that reduction of OGT causes a reduction in transcription and RNA polymerase II occupancy at several B-cell promoters.
22605332	1	2	theme	C-terminal	138:147	arg1	CTD					157:159	CTD	157:159	CTD	157:159	The RNA polymerase II C-terminal domain (CTD), which serves as a scaffold to recruit machinery involved in transcription, is modified post-translationally.
22605332	1	2	theme	C-terminal	138:147	arg1	domain					149:154	The RNA polymerase II C-terminal domain	116:154	The RNA polymerase II C-terminal domain (CTD)	116:160	The RNA polymerase II C-terminal domain (CTD), which serves as a scaffold to recruit machinery involved in transcription, is modified post-translationally.
22605332	1	2	theme	C-terminal	138:147	arg1	scaffold					181:188	a scaffold	179:188	a scaffold	179:188	The RNA polymerase II C-terminal domain (CTD), which serves as a scaffold to recruit machinery involved in transcription, is modified post-translationally.
22605332	0	3	from	Evidence	0:7	arg1	transcription					80:92	transcription	80:92	transcription in vitro and in vivo	80:113	Evidence of the involvement of O-GlcNAc-modified human RNA polymerase II CTD in transcription in vitro and in vivo.
22605332	3	4	dep	residues	462:469	arg1	5					471:471	5	471:471	5	471:471	We show that O-GlcNAc transferase (OGT) modified CTD serine residues 5 and 7.
22605332	3	4	dep	residues	462:469	arg1	7					477:477	7	477:477	7	477:477	We show that O-GlcNAc transferase (OGT) modified CTD serine residues 5 and 7.
22605332	8	5	theme	higher	1088:1093	arg1	eukaryotes					1095:1104	higher eukaryotes	1088:1104	higher eukaryotes	1088:1104	Our results define unexpected roles for both the CTD and O-GlcNAc in the regulation of transcription initiation in higher eukaryotes.
22605332	2	6	theme	polymerase	314:323	arg1	modification					294:305	the O-GlcNAc modification	281:305	the O-GlcNAc modification of RNA polymerase II CTD	281:330	Although the O-GlcNAc modification of RNA polymerase II CTD was documented in 1993, its functional significance remained obscure.
22605332	6	7	from	occupancy	805:813	arg1	transcription					769:781	transcription	769:781	transcription	769:781	OGT shRNA experiments showed that reduction of OGT causes a reduction in transcription and RNA polymerase II occupancy at several B-cell promoters.
22605332	7	8	theme	preinitiation	950:962	arg1	complex					964:970	the preinitiation complex	946:970	the preinitiation complex	946:970	These data suggest that the cycling of O-GlcNAc on and off of polymerase II occurs during assembly of the preinitiation complex.
22605332	8	9	from	roles	1003:1007	arg1	regulation					1046:1055	the regulation	1042:1055	the regulation of transcription initiation in higher eukaryotes	1042:1104	Our results define unexpected roles for both the CTD and O-GlcNAc in the regulation of transcription initiation in higher eukaryotes.
22605332	4	10	theme	OGA	507:509	arg1	inhibition					485:494	Drug inhibition	480:494	Drug inhibition of OGT and OGA (N-acetylglucosaminidase)	480:535	Drug inhibition of OGT and OGA (N-acetylglucosaminidase) blocked transcription during preinitiation complex assembly.
22605332	2	11	theme	O-GlcNAc	285:292	arg1	modification					294:305	the O-GlcNAc modification	281:305	the O-GlcNAc modification of RNA polymerase II CTD	281:330	Although the O-GlcNAc modification of RNA polymerase II CTD was documented in 1993, its functional significance remained obscure.
22605332	6	12	theme	polymerase	791:800	arg1	occupancy					805:813	RNA polymerase II occupancy	787:813	RNA polymerase II occupancy at several B-cell promoters	787:841	OGT shRNA experiments showed that reduction of OGT causes a reduction in transcription and RNA polymerase II occupancy at several B-cell promoters.
22605332	7	13	from	cycling	872:878	arg1	and					895:897	and	895:897	and	895:897	These data suggest that the cycling of O-GlcNAc on and off of polymerase II occurs during assembly of the preinitiation complex.
22605332	0	14	theme	involvement	16:26	arg1	Evidence					0:7	Evidence	0:7	Evidence of the involvement of O-GlcNAc-modified human RNA polymerase II CTD in transcription in vitro and in vivo.	0:114	Evidence of the involvement of O-GlcNAc-modified human RNA polymerase II CTD in transcription in vitro and in vivo.
22605332	4	15	theme	OGT	499:501	arg1	inhibition					485:494	Drug inhibition	480:494	Drug inhibition of OGT and OGA (N-acetylglucosaminidase)	480:535	Drug inhibition of OGT and OGA (N-acetylglucosaminidase) blocked transcription during preinitiation complex assembly.
22605332	6	16	theme	OGT	743:745	arg1	reduction					730:738	reduction	730:738	reduction of OGT	730:745	OGT shRNA experiments showed that reduction of OGT causes a reduction in transcription and RNA polymerase II occupancy at several B-cell promoters.
22605332	2	17	dep	polymerase	314:323	arg1	CTD					328:330	CTD	328:330	RNA polymerase II CTD	310:330	Although the O-GlcNAc modification of RNA polymerase II CTD was documented in 1993, its functional significance remained obscure.
22605332	6	18	from	promoters	833:841	arg1	occupancy					805:813	RNA polymerase II occupancy	787:813	RNA polymerase II occupancy at several B-cell promoters	787:841	OGT shRNA experiments showed that reduction of OGT causes a reduction in transcription and RNA polymerase II occupancy at several B-cell promoters.
22605332	6	18	from	promoters	833:841	arg1	reduction					756:764	a reduction	754:764	a reduction in transcription	754:781	OGT shRNA experiments showed that reduction of OGT causes a reduction in transcription and RNA polymerase II occupancy at several B-cell promoters.
22605332	0	19	dep	polymerase	59:68	arg1	CTD					73:75	CTD	73:75	O-GlcNAc-modified human RNA polymerase II CTD	31:75	Evidence of the involvement of O-GlcNAc-modified human RNA polymerase II CTD in transcription in vitro and in vivo.
22605332	0	20	theme	O-GlcNAc-modified	31:47	arg1	polymerase					59:68	O-GlcNAc-modified human RNA polymerase II CTD	31:75	O-GlcNAc-modified human RNA polymerase II CTD	31:75	Evidence of the involvement of O-GlcNAc-modified human RNA polymerase II CTD in transcription in vitro and in vivo.
22605332	3	21	theme	serine	455:460	arg1	residues					462:469	CTD serine residues 5 and 7	451:477	CTD serine residues 5 and 7	451:477	We show that O-GlcNAc transferase (OGT) modified CTD serine residues 5 and 7.
22605332	5	22	theme	preinitiation	673:685	arg1	complex					687:693	the preinitiation complex	669:693	the preinitiation complex	669:693	Polymerase II and OGT co-immunoprecipitated, and OGT is a component of the preinitiation complex.
22605332	6	23	from	reduction	756:764	arg1	transcription					769:781	transcription	769:781	transcription	769:781	OGT shRNA experiments showed that reduction of OGT causes a reduction in transcription and RNA polymerase II occupancy at several B-cell promoters.
22605332	3	24	theme	O-GlcNAc	415:422	arg1	transferase					424:434	O-GlcNAc transferase	415:434	O-GlcNAc transferase (OGT)	415:440	We show that O-GlcNAc transferase (OGT) modified CTD serine residues 5 and 7.
22605332	3	24	theme	O-GlcNAc	415:422	arg1	OGT					437:439	OGT	437:439	OGT	437:439	We show that O-GlcNAc transferase (OGT) modified CTD serine residues 5 and 7.
22605332	8	25	from	regulation	1046:1055	arg1	eukaryotes					1095:1104	higher eukaryotes	1088:1104	higher eukaryotes	1088:1104	Our results define unexpected roles for both the CTD and O-GlcNAc in the regulation of transcription initiation in higher eukaryotes.
22605332	4	26	theme	Drug	480:483	arg1	inhibition					485:494	Drug inhibition	480:494	Drug inhibition of OGT and OGA (N-acetylglucosaminidase)	480:535	Drug inhibition of OGT and OGA (N-acetylglucosaminidase) blocked transcription during preinitiation complex assembly.
22605332	5	27	theme	complex	687:693	arg1	OGT					647:649	OGT	647:649	OGT	647:649	Polymerase II and OGT co-immunoprecipitated, and OGT is a component of the preinitiation complex.
22605332	5	27	theme	complex	687:693	arg1	component					656:664	a component	654:664	a component of the preinitiation complex	654:693	Polymerase II and OGT co-immunoprecipitated, and OGT is a component of the preinitiation complex.
22605332	6	28	theme	B-cell	826:831	arg1	promoters					833:841	several B-cell promoters	818:841	several B-cell promoters	818:841	OGT shRNA experiments showed that reduction of OGT causes a reduction in transcription and RNA polymerase II occupancy at several B-cell promoters.
22605332	2	29	theme	functional	360:369	arg1	significance					371:382	its functional significance	356:382	its functional significance	356:382	Although the O-GlcNAc modification of RNA polymerase II CTD was documented in 1993, its functional significance remained obscure.
22605332	0	30	theme	RNA	55:57	arg1	polymerase					59:68	O-GlcNAc-modified human RNA polymerase II CTD	31:75	O-GlcNAc-modified human RNA polymerase II CTD	31:75	Evidence of the involvement of O-GlcNAc-modified human RNA polymerase II CTD in transcription in vitro and in vivo.
22605332	8	31	theme	transcription	1060:1072	arg1	initiation					1074:1083	transcription initiation	1060:1083	transcription initiation	1060:1083	Our results define unexpected roles for both the CTD and O-GlcNAc in the regulation of transcription initiation in higher eukaryotes.
22605332	6	32	theme	several	818:824	arg1	promoters					833:841	several B-cell promoters	818:841	several B-cell promoters	818:841	OGT shRNA experiments showed that reduction of OGT causes a reduction in transcription and RNA polymerase II occupancy at several B-cell promoters.
22605332	3	33	theme	CTD	451:453	arg1	residues					462:469	CTD serine residues 5 and 7	451:477	CTD serine residues 5 and 7	451:477	We show that O-GlcNAc transferase (OGT) modified CTD serine residues 5 and 7.
22605332	0	34	theme	human	49:53	arg1	polymerase					59:68	O-GlcNAc-modified human RNA polymerase II CTD	31:75	O-GlcNAc-modified human RNA polymerase II CTD	31:75	Evidence of the involvement of O-GlcNAc-modified human RNA polymerase II CTD in transcription in vitro and in vivo.
22605332	7	35	theme	complex	964:970	arg1	assembly					934:941	assembly	934:941	assembly of the preinitiation complex	934:970	These data suggest that the cycling of O-GlcNAc on and off of polymerase II occurs during assembly of the preinitiation complex.
22605332	2	36	theme	RNA	310:312	arg1	polymerase					314:323	RNA polymerase II CTD	310:330	RNA polymerase II CTD	310:330	Although the O-GlcNAc modification of RNA polymerase II CTD was documented in 1993, its functional significance remained obscure.
22605332	7	37	dep	polymerase	906:915	arg1	off					899:901	off	899:901	off	899:901	These data suggest that the cycling of O-GlcNAc on and off of polymerase II occurs during assembly of the preinitiation complex.
22605332	7	38	theme	O-GlcNAc	883:890	arg1	cycling					872:878	the cycling	868:878	the cycling of O-GlcNAc on and off of polymerase II	868:918	These data suggest that the cycling of O-GlcNAc on and off of polymerase II occurs during assembly of the preinitiation complex.
22605332	4	39	theme	preinitiation	566:578	arg1	complex					580:586	preinitiation complex	566:586	preinitiation complex assembly	566:595	Drug inhibition of OGT and OGA (N-acetylglucosaminidase) blocked transcription during preinitiation complex assembly.
22605332	8	40	theme	initiation	1074:1083	arg1	regulation					1046:1055	the regulation	1042:1055	the regulation of transcription initiation in higher eukaryotes	1042:1104	Our results define unexpected roles for both the CTD and O-GlcNAc in the regulation of transcription initiation in higher eukaryotes.
22605332	8	41	dep	CTD	1022:1024	arg1	the					1018:1020	the	1018:1020	the	1018:1020	Our results define unexpected roles for both the CTD and O-GlcNAc in the regulation of transcription initiation in higher eukaryotes.
22605332	0	42	from	transcription	80:92	arg1	Evidence					0:7	Evidence	0:7	Evidence of the involvement of O-GlcNAc-modified human RNA polymerase II CTD in transcription in vitro and in vivo.	0:114	Evidence of the involvement of O-GlcNAc-modified human RNA polymerase II CTD in transcription in vitro and in vivo.
22605332	6	43	theme	shRNA	700:704	arg1	experiments					706:716	OGT shRNA experiments	696:716	OGT shRNA experiments	696:716	OGT shRNA experiments showed that reduction of OGT causes a reduction in transcription and RNA polymerase II occupancy at several B-cell promoters.
22605332	1	44	theme	RNA	120:122	arg1	CTD					157:159	CTD	157:159	CTD	157:159	The RNA polymerase II C-terminal domain (CTD), which serves as a scaffold to recruit machinery involved in transcription, is modified post-translationally.
22605332	1	44	theme	RNA	120:122	arg1	domain					149:154	The RNA polymerase II C-terminal domain	116:154	The RNA polymerase II C-terminal domain (CTD)	116:160	The RNA polymerase II C-terminal domain (CTD), which serves as a scaffold to recruit machinery involved in transcription, is modified post-translationally.
22605332	1	44	theme	RNA	120:122	arg1	scaffold					181:188	a scaffold	179:188	a scaffold	179:188	The RNA polymerase II C-terminal domain (CTD), which serves as a scaffold to recruit machinery involved in transcription, is modified post-translationally.
22605332	0	45	theme	polymerase	59:68	arg1	involvement					16:26	the involvement	12:26	the involvement of O-GlcNAc-modified human RNA polymerase II CTD in transcription in vitro and in vivo	12:113	Evidence of the involvement of O-GlcNAc-modified human RNA polymerase II CTD in transcription in vitro and in vivo.
22605332	0	46	from	involvement	16:26	arg1	transcription					80:92	transcription	80:92	transcription in vitro and in vivo	80:113	Evidence of the involvement of O-GlcNAc-modified human RNA polymerase II CTD in transcription in vitro and in vivo.
22605332	6	47	theme	OGT	696:698	arg1	experiments					706:716	OGT shRNA experiments	696:716	OGT shRNA experiments	696:716	OGT shRNA experiments showed that reduction of OGT causes a reduction in transcription and RNA polymerase II occupancy at several B-cell promoters.
22605332	1	48	theme	polymerase	124:133	arg1	CTD					157:159	CTD	157:159	CTD	157:159	The RNA polymerase II C-terminal domain (CTD), which serves as a scaffold to recruit machinery involved in transcription, is modified post-translationally.
22605332	1	48	theme	polymerase	124:133	arg1	domain					149:154	The RNA polymerase II C-terminal domain	116:154	The RNA polymerase II C-terminal domain (CTD)	116:160	The RNA polymerase II C-terminal domain (CTD), which serves as a scaffold to recruit machinery involved in transcription, is modified post-translationally.
22605332	1	48	theme	polymerase	124:133	arg1	scaffold					181:188	a scaffold	179:188	a scaffold	179:188	The RNA polymerase II C-terminal domain (CTD), which serves as a scaffold to recruit machinery involved in transcription, is modified post-translationally.
22605332	4	49	theme	complex	580:586	arg1	assembly					588:595	preinitiation complex assembly	566:595	preinitiation complex assembly	566:595	Drug inhibition of OGT and OGA (N-acetylglucosaminidase) blocked transcription during preinitiation complex assembly.
22371499	6	0	theme	target	770:775	arg1	genes					777:781	target genes	770:781	target genes	770:781	The recruitment of OGT by GR leads to increased O-GlcNAcylation and decreased phosphorylation of RNA polymerase II on target genes.
22371499	7	1	theme	sensitive	918:926	arg1	lines					933:937	sensitive cell lines	918:937	sensitive cell lines	918:937	Functionally, overexpression of OGT enhances glucocorticoid-induced apoptosis in resistant cell lines while knockdown of OGT prevents sensitive cell lines from apoptosis.
22371499	8	2	theme	O-GlcNAc	1053:1060	arg1	function					1041:1048	the function	1037:1048	the function of O-GlcNAc in hormone signaling	1037:1081	These studies identify a molecular mechanism of GR transrepression, and highlight the function of O-GlcNAc in hormone signaling.
22371499	1	3	theme	gene	168:171	arg1	repression					173:182	gene repression	168:182	gene repression	168:182	Recruitment of O-GlcNAc transferase (OGT) to promoters plays an important role in gene repression.
22371499	6	4	theme	OGT	671:673	arg1	recruitment					656:666	The recruitment	652:666	The recruitment of OGT by GR	652:679	The recruitment of OGT by GR leads to increased O-GlcNAcylation and decreased phosphorylation of RNA polymerase II on target genes.
22371499	7	5	from	apoptosis	852:860	arg1	lines					880:884	resistant cell lines	865:884	resistant cell lines	865:884	Functionally, overexpression of OGT enhances glucocorticoid-induced apoptosis in resistant cell lines while knockdown of OGT prevents sensitive cell lines from apoptosis.
22371499	6	6	from	O-GlcNAcylation	700:714	arg1	genes					777:781	target genes	770:781	target genes	770:781	The recruitment of OGT by GR leads to increased O-GlcNAcylation and decreased phosphorylation of RNA polymerase II on target genes.
22371499	2	7	theme	molecular	301:309	arg1	mechanisms					311:320	the molecular mechanisms	297:320	the molecular mechanisms	297:320	Glucocorticoid signaling represses the transcriptional activities of NF-κB and AP-1 through direct binding, yet the molecular mechanisms remain to be elucidated.
22371499	8	8	theme	hormone	1065:1071	arg1	signaling					1073:1081	hormone signaling	1065:1081	hormone signaling	1065:1081	These studies identify a molecular mechanism of GR transrepression, and highlight the function of O-GlcNAc in hormone signaling.
22371499	0	9	theme	O-GlcNAc	0:7	arg1	transferase					9:19	O-GlcNAc transferase	0:19	O-GlcNAc transferase	0:19	O-GlcNAc transferase is involved in glucocorticoid receptor-mediated transrepression.
22371499	6	10	theme	RNA	749:751	arg1	polymerase					753:762	RNA polymerase II	749:765	RNA polymerase II	749:765	The recruitment of OGT by GR leads to increased O-GlcNAcylation and decreased phosphorylation of RNA polymerase II on target genes.
22371499	7	11	theme	cell	928:931	arg1	lines					933:937	sensitive cell lines	918:937	sensitive cell lines	918:937	Functionally, overexpression of OGT enhances glucocorticoid-induced apoptosis in resistant cell lines while knockdown of OGT prevents sensitive cell lines from apoptosis.
22371499	5	12	theme	RNA	609:611	arg1	interference					613:624	RNA interference	609:624	RNA interference	609:624	Overexpression of OGT potentiates the GR transrepression pathway, whereas depletion of endogenous OGT by RNA interference abolishes the repression.
22371499	1	13	theme	O-GlcNAc	101:108	arg1	OGT					123:125	OGT	123:125	OGT	123:125	Recruitment of O-GlcNAc transferase (OGT) to promoters plays an important role in gene repression.
22371499	1	13	theme	O-GlcNAc	101:108	arg1	transferase					110:120	O-GlcNAc transferase	101:120	O-GlcNAc transferase (OGT)	101:126	Recruitment of O-GlcNAc transferase (OGT) to promoters plays an important role in gene repression.
22371499	5	14	theme	GR	542:543	arg1	pathway					561:567	the GR transrepression pathway	538:567	the GR transrepression pathway	538:567	Overexpression of OGT potentiates the GR transrepression pathway, whereas depletion of endogenous OGT by RNA interference abolishes the repression.
22371499	8	15	theme	molecular	980:988	arg1	mechanism					990:998	a molecular mechanism	978:998	a molecular mechanism of GR transrepression	978:1020	These studies identify a molecular mechanism of GR transrepression, and highlight the function of O-GlcNAc in hormone signaling.
22371499	1	16	theme	transferase	110:120	arg1	Recruitment					86:96	Recruitment	86:96	Recruitment of O-GlcNAc transferase (OGT) to promoters	86:139	Recruitment of O-GlcNAc transferase (OGT) to promoters plays an important role in gene repression.
22371499	5	17	theme	transrepression	545:559	arg1	pathway					561:567	the GR transrepression pathway	538:567	the GR transrepression pathway	538:567	Overexpression of OGT potentiates the GR transrepression pathway, whereas depletion of endogenous OGT by RNA interference abolishes the repression.
22371499	3	18	theme	GR-mediated	400:410	arg1	transrepression					412:426	GR-mediated transrepression	400:426	GR-mediated transrepression	400:426	Here we report that OGT is an important component of GR-mediated transrepression.
22371499	7	19	theme	OGT	905:907	arg1	knockdown					892:900	knockdown	892:900	knockdown of OGT	892:907	Functionally, overexpression of OGT enhances glucocorticoid-induced apoptosis in resistant cell lines while knockdown of OGT prevents sensitive cell lines from apoptosis.
22371499	3	20	theme	important	377:385	arg1	OGT					367:369	OGT	367:369	OGT	367:369	Here we report that OGT is an important component of GR-mediated transrepression.
22371499	3	20	theme	important	377:385	arg1	component					387:395	an important component	374:395	an important component of GR-mediated transrepression	374:426	Here we report that OGT is an important component of GR-mediated transrepression.
22371499	8	21	from	function	1041:1048	arg1	signaling					1073:1081	hormone signaling	1065:1081	hormone signaling	1065:1081	These studies identify a molecular mechanism of GR transrepression, and highlight the function of O-GlcNAc in hormone signaling.
22371499	7	22	theme	resistant	865:873	arg1	lines					880:884	resistant cell lines	865:884	resistant cell lines	865:884	Functionally, overexpression of OGT enhances glucocorticoid-induced apoptosis in resistant cell lines while knockdown of OGT prevents sensitive cell lines from apoptosis.
22371499	5	23	dep	potentiates	526:536	arg1	whereas					570:576	whereas	570:576	whereas	570:576	Overexpression of OGT potentiates the GR transrepression pathway, whereas depletion of endogenous OGT by RNA interference abolishes the repression.
22371499	4	24	theme	multi-protein	470:482	arg1	complex					495:501	a multi-protein repression complex	468:501	a multi-protein repression complex	468:501	OGT associates with ligand-bound GR in a multi-protein repression complex.
22371499	6	25	from	phosphorylation	730:744	arg1	genes					777:781	target genes	770:781	target genes	770:781	The recruitment of OGT by GR leads to increased O-GlcNAcylation and decreased phosphorylation of RNA polymerase II on target genes.
22371499	6	26	theme	decreased	720:728	arg1	phosphorylation					730:744	decreased phosphorylation	720:744	decreased phosphorylation of RNA polymerase II on target genes	720:781	The recruitment of OGT by GR leads to increased O-GlcNAcylation and decreased phosphorylation of RNA polymerase II on target genes.
22371499	7	27	theme	cell	875:878	arg1	lines					880:884	resistant cell lines	865:884	resistant cell lines	865:884	Functionally, overexpression of OGT enhances glucocorticoid-induced apoptosis in resistant cell lines while knockdown of OGT prevents sensitive cell lines from apoptosis.
22371499	2	28	theme	Glucocorticoid	185:198	arg1	signaling					200:208	Glucocorticoid signaling	185:208	Glucocorticoid signaling	185:208	Glucocorticoid signaling represses the transcriptional activities of NF-κB and AP-1 through direct binding, yet the molecular mechanisms remain to be elucidated.
22371499	2	29	theme	AP-1	264:267	arg1	activities					240:249	the transcriptional activities	220:249	the transcriptional activities of NF-κB and AP-1	220:267	Glucocorticoid signaling represses the transcriptional activities of NF-κB and AP-1 through direct binding, yet the molecular mechanisms remain to be elucidated.
22371499	5	30	theme	OGT	522:524	arg1	Overexpression					504:517	Overexpression	504:517	Overexpression of OGT	504:524	Overexpression of OGT potentiates the GR transrepression pathway, whereas depletion of endogenous OGT by RNA interference abolishes the repression.
22371499	8	31	theme	GR	1003:1004	arg1	transrepression					1006:1020	GR transrepression	1003:1020	GR transrepression	1003:1020	These studies identify a molecular mechanism of GR transrepression, and highlight the function of O-GlcNAc in hormone signaling.
22371499	3	32	theme	transrepression	412:426	arg1	OGT					367:369	OGT	367:369	OGT	367:369	Here we report that OGT is an important component of GR-mediated transrepression.
22371499	3	32	theme	transrepression	412:426	arg1	component					387:395	an important component	374:395	an important component of GR-mediated transrepression	374:426	Here we report that OGT is an important component of GR-mediated transrepression.
22371499	4	33	theme	repression	484:493	arg1	complex					495:501	a multi-protein repression complex	468:501	a multi-protein repression complex	468:501	OGT associates with ligand-bound GR in a multi-protein repression complex.
22371499	2	34	theme	NF-κB	254:258	arg1	activities					240:249	the transcriptional activities	220:249	the transcriptional activities of NF-κB and AP-1	220:267	Glucocorticoid signaling represses the transcriptional activities of NF-κB and AP-1 through direct binding, yet the molecular mechanisms remain to be elucidated.
22371499	5	35	theme	endogenous	591:600	arg1	OGT					602:604	endogenous OGT	591:604	endogenous OGT	591:604	Overexpression of OGT potentiates the GR transrepression pathway, whereas depletion of endogenous OGT by RNA interference abolishes the repression.
22371499	0	36	theme	receptor-mediated	51:67	arg1	transrepression					69:83	glucocorticoid receptor-mediated transrepression	36:83	glucocorticoid receptor-mediated transrepression	36:83	O-GlcNAc transferase is involved in glucocorticoid receptor-mediated transrepression.
22371499	4	37	theme	ligand-bound	449:460	arg1	GR					462:463	ligand-bound GR	449:463	ligand-bound GR	449:463	OGT associates with ligand-bound GR in a multi-protein repression complex.
22371499	5	38	theme	OGT	602:604	arg1	depletion					578:586	depletion	578:586	depletion of endogenous OGT by RNA interference	578:624	Overexpression of OGT potentiates the GR transrepression pathway, whereas depletion of endogenous OGT by RNA interference abolishes the repression.
22371499	7	39	theme	glucocorticoid-induced	829:850	arg1	apoptosis					852:860	glucocorticoid-induced apoptosis	829:860	glucocorticoid-induced apoptosis in resistant cell lines	829:884	Functionally, overexpression of OGT enhances glucocorticoid-induced apoptosis in resistant cell lines while knockdown of OGT prevents sensitive cell lines from apoptosis.
22371499	2	40	theme	transcriptional	224:238	arg1	activities					240:249	the transcriptional activities	220:249	the transcriptional activities of NF-κB and AP-1	220:267	Glucocorticoid signaling represses the transcriptional activities of NF-κB and AP-1 through direct binding, yet the molecular mechanisms remain to be elucidated.
22371499	8	41	theme	transrepression	1006:1020	arg1	mechanism					990:998	a molecular mechanism	978:998	a molecular mechanism of GR transrepression	978:1020	These studies identify a molecular mechanism of GR transrepression, and highlight the function of O-GlcNAc in hormone signaling.
22371499	6	42	theme	increased	690:698	arg1	O-GlcNAcylation					700:714	increased O-GlcNAcylation	690:714	increased O-GlcNAcylation	690:714	The recruitment of OGT by GR leads to increased O-GlcNAcylation and decreased phosphorylation of RNA polymerase II on target genes.
22371499	6	43	theme	polymerase	753:762	arg1	phosphorylation					730:744	decreased phosphorylation	720:744	decreased phosphorylation of RNA polymerase II on target genes	720:781	The recruitment of OGT by GR leads to increased O-GlcNAcylation and decreased phosphorylation of RNA polymerase II on target genes.
22371499	6	43	theme	polymerase	753:762	arg1	O-GlcNAcylation					700:714	increased O-GlcNAcylation	690:714	increased O-GlcNAcylation	690:714	The recruitment of OGT by GR leads to increased O-GlcNAcylation and decreased phosphorylation of RNA polymerase II on target genes.
22371499	7	44	theme	OGT	816:818	arg1	overexpression					798:811	overexpression	798:811	overexpression of OGT	798:818	Functionally, overexpression of OGT enhances glucocorticoid-induced apoptosis in resistant cell lines while knockdown of OGT prevents sensitive cell lines from apoptosis.
22371499	2	45	theme	direct	277:282	arg1	binding					284:290	direct binding	277:290	direct binding	277:290	Glucocorticoid signaling represses the transcriptional activities of NF-κB and AP-1 through direct binding, yet the molecular mechanisms remain to be elucidated.
22371499	1	46	theme	important	150:158	arg1	role					160:163	an important role	147:163	an important role	147:163	Recruitment of O-GlcNAc transferase (OGT) to promoters plays an important role in gene repression.
36064721	4	0	theme	threonine	617:625	arg1	residues					627:634	specific threonine residues	608:634	specific threonine residues	608:634	Mechanistically, O-GlcNAcylation on specific threonine residues increased the catalytic efficiency for ammonia of carbamoyl phosphate synthetase 1 (CPS1), the rate-limiting enzyme in ureagenesis.
36064721	5	1	theme	O-GlcNAc from	831:843	arg1	proteins					845:852	O-GlcNAc from proteins	831:852	O-GlcNAc from proteins	831:852	Pharmacological inhibition of O-GlcNAcase, the enzyme removing O-GlcNAc from proteins, resulted in clinically relevant reductions of systemic ammonia in both genetic (hypomorphic mouse model of propionic acidemia) and acquired (thioacetamide-induced acute liver failure) mouse models of liver diseases.
36064721	2	2	theme	pathway	436:442	arg1	UDP-GlcNAc					381:390	substrate UDP-GlcNAc	371:390	substrate UDP-GlcNAc	371:390	Protein O-GlcNAcylation is a reversible and nutrient-sensitive post-translational modification using as substrate UDP-GlcNAc, the end-product of hexosamine biosynthesis pathway.
36064721	2	2	theme	pathway	436:442	arg1	end-product					397:407	the end-product	393:407	the end-product of hexosamine biosynthesis pathway	393:442	Protein O-GlcNAcylation is a reversible and nutrient-sensitive post-translational modification using as substrate UDP-GlcNAc, the end-product of hexosamine biosynthesis pathway.
36064721	6	3	theme	hepatic	1143:1149	arg1	O-GlcNAcylation					1151:1165	hepatic O-GlcNAcylation	1143:1165	hepatic O-GlcNAcylation of CPS1	1143:1173	In conclusion, by fine-tuned control of ammonia entry into ureagenesis, hepatic O-GlcNAcylation of CPS1 increases ammonia detoxification and is a novel target for therapy of hyperammonemia in both genetic and acquired diseases.
36064721	5	4	dep	genetic	926:932	arg1	model					953:957	hypomorphic mouse model	935:957	hypomorphic mouse model of propionic acidemia	935:979	Pharmacological inhibition of O-GlcNAcase, the enzyme removing O-GlcNAc from proteins, resulted in clinically relevant reductions of systemic ammonia in both genetic (hypomorphic mouse model of propionic acidemia) and acquired (thioacetamide-induced acute liver failure) mouse models of liver diseases.
36064721	5	4	dep	genetic	926:932	arg1	failure					1030:1036	thioacetamide-induced acute liver failure	996:1036	thioacetamide-induced acute liver failure	996:1036	Pharmacological inhibition of O-GlcNAcase, the enzyme removing O-GlcNAc from proteins, resulted in clinically relevant reductions of systemic ammonia in both genetic (hypomorphic mouse model of propionic acidemia) and acquired (thioacetamide-induced acute liver failure) mouse models of liver diseases.
36064721	6	5	theme	hyperammonemia	1245:1258	arg1	therapy					1234:1240	therapy	1234:1240	therapy of hyperammonemia in both genetic and acquired diseases	1234:1296	In conclusion, by fine-tuned control of ammonia entry into ureagenesis, hepatic O-GlcNAcylation of CPS1 increases ammonia detoxification and is a novel target for therapy of hyperammonemia in both genetic and acquired diseases.
36064721	2	6	theme	biosynthesis	423:434	arg1	pathway					436:442	hexosamine biosynthesis pathway	412:442	hexosamine biosynthesis pathway	412:442	Protein O-GlcNAcylation is a reversible and nutrient-sensitive post-translational modification using as substrate UDP-GlcNAc, the end-product of hexosamine biosynthesis pathway.
36064721	5	7	theme	O-GlcNAcase	798:808	arg1	inhibition					784:793	Pharmacological inhibition	768:793	Pharmacological inhibition of O-GlcNAcase, the enzyme removing O-GlcNAc from proteins,	768:853	Pharmacological inhibition of O-GlcNAcase, the enzyme removing O-GlcNAc from proteins, resulted in clinically relevant reductions of systemic ammonia in both genetic (hypomorphic mouse model of propionic acidemia) and acquired (thioacetamide-induced acute liver failure) mouse models of liver diseases.
36064721	5	8	theme	hypomorphic	935:945	arg1	model					953:957	hypomorphic mouse model	935:957	hypomorphic mouse model of propionic acidemia	935:979	Pharmacological inhibition of O-GlcNAcase, the enzyme removing O-GlcNAc from proteins, resulted in clinically relevant reductions of systemic ammonia in both genetic (hypomorphic mouse model of propionic acidemia) and acquired (thioacetamide-induced acute liver failure) mouse models of liver diseases.
36064721	6	9	theme	entry	1119:1123	arg1	control					1100:1106	fine-tuned control	1089:1106	fine-tuned control of ammonia entry into ureagenesis	1089:1140	In conclusion, by fine-tuned control of ammonia entry into ureagenesis, hepatic O-GlcNAcylation of CPS1 increases ammonia detoxification and is a novel target for therapy of hyperammonemia in both genetic and acquired diseases.
36064721	5	10	theme	relevant	878:885	arg1	reductions					887:896	clinically relevant reductions	867:896	clinically relevant reductions of systemic ammonia	867:916	Pharmacological inhibition of O-GlcNAcase, the enzyme removing O-GlcNAc from proteins, resulted in clinically relevant reductions of systemic ammonia in both genetic (hypomorphic mouse model of propionic acidemia) and acquired (thioacetamide-induced acute liver failure) mouse models of liver diseases.
36064721	2	11	theme	hexosamine	412:421	arg1	pathway					436:442	hexosamine biosynthesis pathway	412:442	hexosamine biosynthesis pathway	412:442	Protein O-GlcNAcylation is a reversible and nutrient-sensitive post-translational modification using as substrate UDP-GlcNAc, the end-product of hexosamine biosynthesis pathway.
36064721	2	12	theme	post-translational	330:347	arg1	modification					349:360	a reversible and nutrient-sensitive post-translational modification	294:360	a reversible and nutrient-sensitive post-translational modification using as substrate UDP-GlcNAc, the end-product of hexosamine biosynthesis pathway	294:442	Protein O-GlcNAcylation is a reversible and nutrient-sensitive post-translational modification using as substrate UDP-GlcNAc, the end-product of hexosamine biosynthesis pathway.
36064721	2	12	theme	post-translational	330:347	arg1	O-GlcNAcylation					275:289	Protein O-GlcNAcylation	267:289	Protein O-GlcNAcylation	267:289	Protein O-GlcNAcylation is a reversible and nutrient-sensitive post-translational modification using as substrate UDP-GlcNAc, the end-product of hexosamine biosynthesis pathway.
36064721	6	13	theme	novel	1217:1221	arg1	target					1223:1228	a novel target	1215:1228	a novel target for therapy of hyperammonemia in both genetic and acquired diseases	1215:1296	In conclusion, by fine-tuned control of ammonia entry into ureagenesis, hepatic O-GlcNAcylation of CPS1 increases ammonia detoxification and is a novel target for therapy of hyperammonemia in both genetic and acquired diseases.
36064721	5	14	theme	thioacetamide-induced	996:1016	arg1	failure					1030:1036	thioacetamide-induced acute liver failure	996:1036	thioacetamide-induced acute liver failure	996:1036	Pharmacological inhibition of O-GlcNAcase, the enzyme removing O-GlcNAc from proteins, resulted in clinically relevant reductions of systemic ammonia in both genetic (hypomorphic mouse model of propionic acidemia) and acquired (thioacetamide-induced acute liver failure) mouse models of liver diseases.
36064721	4	15	theme	specific	608:615	arg1	residues					627:634	specific threonine residues	608:634	specific threonine residues	608:634	Mechanistically, O-GlcNAcylation on specific threonine residues increased the catalytic efficiency for ammonia of carbamoyl phosphate synthetase 1 (CPS1), the rate-limiting enzyme in ureagenesis.
36064721	6	16	theme	genetic	1268:1274	arg1	diseases					1289:1296	both genetic and acquired diseases	1263:1296	both genetic and acquired diseases	1263:1296	In conclusion, by fine-tuned control of ammonia entry into ureagenesis, hepatic O-GlcNAcylation of CPS1 increases ammonia detoxification and is a novel target for therapy of hyperammonemia in both genetic and acquired diseases.
36064721	1	17	theme	Life-threatening	89:104	arg1	hyperammonemia					106:119	Life-threatening hyperammonemia	89:119	Life-threatening hyperammonemia	89:119	Life-threatening hyperammonemia occurs in both inherited and acquired liver diseases affecting ureagenesis, the main pathway for detoxification of neurotoxic ammonia in mammals.
36064721	1	18	theme	main	201:204	arg1	pathway					206:212	the main pathway	197:212	the main pathway for detoxification of neurotoxic ammonia in mammals	197:264	Life-threatening hyperammonemia occurs in both inherited and acquired liver diseases affecting ureagenesis, the main pathway for detoxification of neurotoxic ammonia in mammals.
36064721	1	18	theme	main	201:204	arg1	ureagenesis					184:194	ureagenesis	184:194	ureagenesis	184:194	Life-threatening hyperammonemia occurs in both inherited and acquired liver diseases affecting ureagenesis, the main pathway for detoxification of neurotoxic ammonia in mammals.
36064721	4	19	from	O-GlcNAcylation	589:603	arg1	residues					627:634	specific threonine residues	608:634	specific threonine residues	608:634	Mechanistically, O-GlcNAcylation on specific threonine residues increased the catalytic efficiency for ammonia of carbamoyl phosphate synthetase 1 (CPS1), the rate-limiting enzyme in ureagenesis.
36064721	5	20	theme	systemic	901:908	arg1	ammonia					910:916	systemic ammonia	901:916	systemic ammonia	901:916	Pharmacological inhibition of O-GlcNAcase, the enzyme removing O-GlcNAc from proteins, resulted in clinically relevant reductions of systemic ammonia in both genetic (hypomorphic mouse model of propionic acidemia) and acquired (thioacetamide-induced acute liver failure) mouse models of liver diseases.
36064721	5	21	theme	liver	1024:1028	arg1	failure					1030:1036	thioacetamide-induced acute liver failure	996:1036	thioacetamide-induced acute liver failure	996:1036	Pharmacological inhibition of O-GlcNAcase, the enzyme removing O-GlcNAc from proteins, resulted in clinically relevant reductions of systemic ammonia in both genetic (hypomorphic mouse model of propionic acidemia) and acquired (thioacetamide-induced acute liver failure) mouse models of liver diseases.
36064721	3	22	theme	increased	463:471	arg1	UDP-GlcNAc					479:488	increased liver UDP-GlcNAc	463:488	increased liver UDP-GlcNAc during hyperammonemia	463:510	Here we show that increased liver UDP-GlcNAc during hyperammonemia increases protein O-GlcNAcylation and enhances ureagenesis.
36064721	4	23	theme	carbamoyl	686:694	arg1	CPS1					720:723	CPS1	720:723	CPS1	720:723	Mechanistically, O-GlcNAcylation on specific threonine residues increased the catalytic efficiency for ammonia of carbamoyl phosphate synthetase 1 (CPS1), the rate-limiting enzyme in ureagenesis.
36064721	4	23	theme	carbamoyl	686:694	arg1	enzyme					745:750	the rate-limiting enzyme	727:750	the rate-limiting enzyme in ureagenesis	727:765	Mechanistically, O-GlcNAcylation on specific threonine residues increased the catalytic efficiency for ammonia of carbamoyl phosphate synthetase 1 (CPS1), the rate-limiting enzyme in ureagenesis.
36064721	4	23	theme	carbamoyl	686:694	arg1	synthetase					706:715	carbamoyl phosphate synthetase 1	686:717	carbamoyl phosphate synthetase 1 (CPS1)	686:724	Mechanistically, O-GlcNAcylation on specific threonine residues increased the catalytic efficiency for ammonia of carbamoyl phosphate synthetase 1 (CPS1), the rate-limiting enzyme in ureagenesis.
36064721	5	24	theme	Pharmacological	768:782	arg1	inhibition					784:793	Pharmacological inhibition	768:793	Pharmacological inhibition of O-GlcNAcase, the enzyme removing O-GlcNAc from proteins,	768:853	Pharmacological inhibition of O-GlcNAcase, the enzyme removing O-GlcNAc from proteins, resulted in clinically relevant reductions of systemic ammonia in both genetic (hypomorphic mouse model of propionic acidemia) and acquired (thioacetamide-induced acute liver failure) mouse models of liver diseases.
36064721	3	25	theme	protein	522:528	arg1	O-GlcNAcylation					530:544	protein O-GlcNAcylation	522:544	protein O-GlcNAcylation	522:544	Here we show that increased liver UDP-GlcNAc during hyperammonemia increases protein O-GlcNAcylation and enhances ureagenesis.
36064721	0	26	theme	catalytic	30:38	arg1	efficiency					40:49	CPS1 catalytic efficiency	25:49	CPS1 catalytic efficiency for ammonia	25:61	O-GlcNAcylation enhances CPS1 catalytic efficiency for ammonia and promotes ureagenesis.
36064721	6	27	theme	ammonia	1111:1117	arg1	entry					1119:1123	ammonia entry	1111:1123	ammonia entry into ureagenesis	1111:1140	In conclusion, by fine-tuned control of ammonia entry into ureagenesis, hepatic O-GlcNAcylation of CPS1 increases ammonia detoxification and is a novel target for therapy of hyperammonemia in both genetic and acquired diseases.
36064721	2	28	theme	substrate	371:379	arg1	UDP-GlcNAc					381:390	substrate UDP-GlcNAc	371:390	substrate UDP-GlcNAc	371:390	Protein O-GlcNAcylation is a reversible and nutrient-sensitive post-translational modification using as substrate UDP-GlcNAc, the end-product of hexosamine biosynthesis pathway.
36064721	2	28	theme	substrate	371:379	arg1	end-product					397:407	the end-product	393:407	the end-product of hexosamine biosynthesis pathway	393:442	Protein O-GlcNAcylation is a reversible and nutrient-sensitive post-translational modification using as substrate UDP-GlcNAc, the end-product of hexosamine biosynthesis pathway.
36064721	0	29	theme	CPS1	25:28	arg1	efficiency					40:49	CPS1 catalytic efficiency	25:49	CPS1 catalytic efficiency for ammonia	25:61	O-GlcNAcylation enhances CPS1 catalytic efficiency for ammonia and promotes ureagenesis.
36064721	4	30	theme	synthetase	706:715	arg1	ammonia					675:681	ammonia	675:681	ammonia of carbamoyl phosphate synthetase 1 (CPS1), the rate-limiting enzyme in ureagenesis	675:765	Mechanistically, O-GlcNAcylation on specific threonine residues increased the catalytic efficiency for ammonia of carbamoyl phosphate synthetase 1 (CPS1), the rate-limiting enzyme in ureagenesis.
36064721	5	31	theme	propionic	962:970	arg1	acidemia					972:979	propionic acidemia	962:979	propionic acidemia	962:979	Pharmacological inhibition of O-GlcNAcase, the enzyme removing O-GlcNAc from proteins, resulted in clinically relevant reductions of systemic ammonia in both genetic (hypomorphic mouse model of propionic acidemia) and acquired (thioacetamide-induced acute liver failure) mouse models of liver diseases.
36064721	5	32	theme	genetic	926:932	arg1	models					1045:1050	both genetic (hypomorphic mouse model of propionic acidemia) and acquired (thioacetamide-induced acute liver failure) mouse models	921:1050	both genetic (hypomorphic mouse model of propionic acidemia) and acquired (thioacetamide-induced acute liver failure) mouse models of liver diseases	921:1068	Pharmacological inhibition of O-GlcNAcase, the enzyme removing O-GlcNAc from proteins, resulted in clinically relevant reductions of systemic ammonia in both genetic (hypomorphic mouse model of propionic acidemia) and acquired (thioacetamide-induced acute liver failure) mouse models of liver diseases.
36064721	4	33	theme	phosphate	696:704	arg1	CPS1					720:723	CPS1	720:723	CPS1	720:723	Mechanistically, O-GlcNAcylation on specific threonine residues increased the catalytic efficiency for ammonia of carbamoyl phosphate synthetase 1 (CPS1), the rate-limiting enzyme in ureagenesis.
36064721	4	33	theme	phosphate	696:704	arg1	enzyme					745:750	the rate-limiting enzyme	727:750	the rate-limiting enzyme in ureagenesis	727:765	Mechanistically, O-GlcNAcylation on specific threonine residues increased the catalytic efficiency for ammonia of carbamoyl phosphate synthetase 1 (CPS1), the rate-limiting enzyme in ureagenesis.
36064721	4	33	theme	phosphate	696:704	arg1	synthetase					706:715	carbamoyl phosphate synthetase 1	686:717	carbamoyl phosphate synthetase 1 (CPS1)	686:724	Mechanistically, O-GlcNAcylation on specific threonine residues increased the catalytic efficiency for ammonia of carbamoyl phosphate synthetase 1 (CPS1), the rate-limiting enzyme in ureagenesis.
36064721	5	34	theme	acquired	986:993	arg1	models					1045:1050	both genetic (hypomorphic mouse model of propionic acidemia) and acquired (thioacetamide-induced acute liver failure) mouse models	921:1050	both genetic (hypomorphic mouse model of propionic acidemia) and acquired (thioacetamide-induced acute liver failure) mouse models of liver diseases	921:1068	Pharmacological inhibition of O-GlcNAcase, the enzyme removing O-GlcNAc from proteins, resulted in clinically relevant reductions of systemic ammonia in both genetic (hypomorphic mouse model of propionic acidemia) and acquired (thioacetamide-induced acute liver failure) mouse models of liver diseases.
36064721	1	35	theme	neurotoxic	236:245	arg1	mammals					258:264	neurotoxic ammonia in mammals	236:264	neurotoxic ammonia in mammals	236:264	Life-threatening hyperammonemia occurs in both inherited and acquired liver diseases affecting ureagenesis, the main pathway for detoxification of neurotoxic ammonia in mammals.
36064721	6	36	theme	fine-tuned	1089:1098	arg1	control					1100:1106	fine-tuned control	1089:1106	fine-tuned control of ammonia entry into ureagenesis	1089:1140	In conclusion, by fine-tuned control of ammonia entry into ureagenesis, hepatic O-GlcNAcylation of CPS1 increases ammonia detoxification and is a novel target for therapy of hyperammonemia in both genetic and acquired diseases.
36064721	2	37	theme	Protein	267:273	arg1	modification					349:360	a reversible and nutrient-sensitive post-translational modification	294:360	a reversible and nutrient-sensitive post-translational modification using as substrate UDP-GlcNAc, the end-product of hexosamine biosynthesis pathway	294:442	Protein O-GlcNAcylation is a reversible and nutrient-sensitive post-translational modification using as substrate UDP-GlcNAc, the end-product of hexosamine biosynthesis pathway.
36064721	2	37	theme	Protein	267:273	arg1	O-GlcNAcylation					275:289	Protein O-GlcNAcylation	267:289	Protein O-GlcNAcylation	267:289	Protein O-GlcNAcylation is a reversible and nutrient-sensitive post-translational modification using as substrate UDP-GlcNAc, the end-product of hexosamine biosynthesis pathway.
36064721	1	38	theme	ammonia in	247:256	arg1	mammals					258:264	neurotoxic ammonia in mammals	236:264	neurotoxic ammonia in mammals	236:264	Life-threatening hyperammonemia occurs in both inherited and acquired liver diseases affecting ureagenesis, the main pathway for detoxification of neurotoxic ammonia in mammals.
36064721	3	39	theme	liver	473:477	arg1	UDP-GlcNAc					479:488	increased liver UDP-GlcNAc	463:488	increased liver UDP-GlcNAc during hyperammonemia	463:510	Here we show that increased liver UDP-GlcNAc during hyperammonemia increases protein O-GlcNAcylation and enhances ureagenesis.
36064721	4	40	theme	catalytic	650:658	arg1	efficiency					660:669	the catalytic efficiency	646:669	the catalytic efficiency for ammonia of carbamoyl phosphate synthetase 1 (CPS1), the rate-limiting enzyme in ureagenesis	646:765	Mechanistically, O-GlcNAcylation on specific threonine residues increased the catalytic efficiency for ammonia of carbamoyl phosphate synthetase 1 (CPS1), the rate-limiting enzyme in ureagenesis.
36064721	1	41	theme	inherited	136:144	arg1	diseases					165:172	both inherited and acquired liver diseases	131:172	both inherited and acquired liver diseases affecting ureagenesis, the main pathway for detoxification of neurotoxic ammonia in mammals	131:264	Life-threatening hyperammonemia occurs in both inherited and acquired liver diseases affecting ureagenesis, the main pathway for detoxification of neurotoxic ammonia in mammals.
36064721	5	42	theme	mouse	947:951	arg1	model					953:957	hypomorphic mouse model	935:957	hypomorphic mouse model of propionic acidemia	935:979	Pharmacological inhibition of O-GlcNAcase, the enzyme removing O-GlcNAc from proteins, resulted in clinically relevant reductions of systemic ammonia in both genetic (hypomorphic mouse model of propionic acidemia) and acquired (thioacetamide-induced acute liver failure) mouse models of liver diseases.
36064721	5	43	theme	diseases	1061:1068	arg1	models					1045:1050	both genetic (hypomorphic mouse model of propionic acidemia) and acquired (thioacetamide-induced acute liver failure) mouse models	921:1050	both genetic (hypomorphic mouse model of propionic acidemia) and acquired (thioacetamide-induced acute liver failure) mouse models of liver diseases	921:1068	Pharmacological inhibition of O-GlcNAcase, the enzyme removing O-GlcNAc from proteins, resulted in clinically relevant reductions of systemic ammonia in both genetic (hypomorphic mouse model of propionic acidemia) and acquired (thioacetamide-induced acute liver failure) mouse models of liver diseases.
36064721	1	44	theme	acquired	150:157	arg1	diseases					165:172	both inherited and acquired liver diseases	131:172	both inherited and acquired liver diseases affecting ureagenesis, the main pathway for detoxification of neurotoxic ammonia in mammals	131:264	Life-threatening hyperammonemia occurs in both inherited and acquired liver diseases affecting ureagenesis, the main pathway for detoxification of neurotoxic ammonia in mammals.
36064721	1	45	theme	mammals	258:264	arg1	detoxification					218:231	detoxification	218:231	detoxification of neurotoxic ammonia in mammals	218:264	Life-threatening hyperammonemia occurs in both inherited and acquired liver diseases affecting ureagenesis, the main pathway for detoxification of neurotoxic ammonia in mammals.
36064721	2	46	theme	nutrient-sensitive	311:328	arg1	modification					349:360	a reversible and nutrient-sensitive post-translational modification	294:360	a reversible and nutrient-sensitive post-translational modification using as substrate UDP-GlcNAc, the end-product of hexosamine biosynthesis pathway	294:442	Protein O-GlcNAcylation is a reversible and nutrient-sensitive post-translational modification using as substrate UDP-GlcNAc, the end-product of hexosamine biosynthesis pathway.
36064721	2	46	theme	nutrient-sensitive	311:328	arg1	O-GlcNAcylation					275:289	Protein O-GlcNAcylation	267:289	Protein O-GlcNAcylation	267:289	Protein O-GlcNAcylation is a reversible and nutrient-sensitive post-translational modification using as substrate UDP-GlcNAc, the end-product of hexosamine biosynthesis pathway.
36064721	5	47	theme	liver	1055:1059	arg1	diseases					1061:1068	liver diseases	1055:1068	liver diseases	1055:1068	Pharmacological inhibition of O-GlcNAcase, the enzyme removing O-GlcNAc from proteins, resulted in clinically relevant reductions of systemic ammonia in both genetic (hypomorphic mouse model of propionic acidemia) and acquired (thioacetamide-induced acute liver failure) mouse models of liver diseases.
36064721	2	48	theme	reversible	296:305	arg1	modification					349:360	a reversible and nutrient-sensitive post-translational modification	294:360	a reversible and nutrient-sensitive post-translational modification using as substrate UDP-GlcNAc, the end-product of hexosamine biosynthesis pathway	294:442	Protein O-GlcNAcylation is a reversible and nutrient-sensitive post-translational modification using as substrate UDP-GlcNAc, the end-product of hexosamine biosynthesis pathway.
36064721	2	48	theme	reversible	296:305	arg1	O-GlcNAcylation					275:289	Protein O-GlcNAcylation	267:289	Protein O-GlcNAcylation	267:289	Protein O-GlcNAcylation is a reversible and nutrient-sensitive post-translational modification using as substrate UDP-GlcNAc, the end-product of hexosamine biosynthesis pathway.
36064721	1	49	theme	liver	159:163	arg1	diseases					165:172	both inherited and acquired liver diseases	131:172	both inherited and acquired liver diseases affecting ureagenesis, the main pathway for detoxification of neurotoxic ammonia in mammals	131:264	Life-threatening hyperammonemia occurs in both inherited and acquired liver diseases affecting ureagenesis, the main pathway for detoxification of neurotoxic ammonia in mammals.
36064721	6	50	theme	acquired	1280:1287	arg1	diseases					1289:1296	both genetic and acquired diseases	1263:1296	both genetic and acquired diseases	1263:1296	In conclusion, by fine-tuned control of ammonia entry into ureagenesis, hepatic O-GlcNAcylation of CPS1 increases ammonia detoxification and is a novel target for therapy of hyperammonemia in both genetic and acquired diseases.
36064721	6	51	theme	CPS1	1170:1173	arg1	O-GlcNAcylation					1151:1165	hepatic O-GlcNAcylation	1143:1165	hepatic O-GlcNAcylation of CPS1	1143:1173	In conclusion, by fine-tuned control of ammonia entry into ureagenesis, hepatic O-GlcNAcylation of CPS1 increases ammonia detoxification and is a novel target for therapy of hyperammonemia in both genetic and acquired diseases.
36064721	4	52	from	enzyme	745:750	arg1	ureagenesis					755:765	ureagenesis	755:765	ureagenesis	755:765	Mechanistically, O-GlcNAcylation on specific threonine residues increased the catalytic efficiency for ammonia of carbamoyl phosphate synthetase 1 (CPS1), the rate-limiting enzyme in ureagenesis.
36064721	6	53	theme	ammonia	1185:1191	arg1	detoxification					1193:1206	ammonia detoxification	1185:1206	ammonia detoxification	1185:1206	In conclusion, by fine-tuned control of ammonia entry into ureagenesis, hepatic O-GlcNAcylation of CPS1 increases ammonia detoxification and is a novel target for therapy of hyperammonemia in both genetic and acquired diseases.
36064721	6	54	from	therapy	1234:1240	arg1	diseases					1289:1296	both genetic and acquired diseases	1263:1296	both genetic and acquired diseases	1263:1296	In conclusion, by fine-tuned control of ammonia entry into ureagenesis, hepatic O-GlcNAcylation of CPS1 increases ammonia detoxification and is a novel target for therapy of hyperammonemia in both genetic and acquired diseases.
36064721	5	55	theme	acute	1018:1022	arg1	failure					1030:1036	thioacetamide-induced acute liver failure	996:1036	thioacetamide-induced acute liver failure	996:1036	Pharmacological inhibition of O-GlcNAcase, the enzyme removing O-GlcNAc from proteins, resulted in clinically relevant reductions of systemic ammonia in both genetic (hypomorphic mouse model of propionic acidemia) and acquired (thioacetamide-induced acute liver failure) mouse models of liver diseases.
36064721	5	56	theme	ammonia	910:916	arg1	reductions					887:896	clinically relevant reductions	867:896	clinically relevant reductions of systemic ammonia	867:916	Pharmacological inhibition of O-GlcNAcase, the enzyme removing O-GlcNAc from proteins, resulted in clinically relevant reductions of systemic ammonia in both genetic (hypomorphic mouse model of propionic acidemia) and acquired (thioacetamide-induced acute liver failure) mouse models of liver diseases.
36064721	5	57	theme	acidemia	972:979	arg1	model					953:957	hypomorphic mouse model	935:957	hypomorphic mouse model of propionic acidemia	935:979	Pharmacological inhibition of O-GlcNAcase, the enzyme removing O-GlcNAc from proteins, resulted in clinically relevant reductions of systemic ammonia in both genetic (hypomorphic mouse model of propionic acidemia) and acquired (thioacetamide-induced acute liver failure) mouse models of liver diseases.
36064721	5	58	theme	mouse	1039:1043	arg1	models					1045:1050	both genetic (hypomorphic mouse model of propionic acidemia) and acquired (thioacetamide-induced acute liver failure) mouse models	921:1050	both genetic (hypomorphic mouse model of propionic acidemia) and acquired (thioacetamide-induced acute liver failure) mouse models of liver diseases	921:1068	Pharmacological inhibition of O-GlcNAcase, the enzyme removing O-GlcNAc from proteins, resulted in clinically relevant reductions of systemic ammonia in both genetic (hypomorphic mouse model of propionic acidemia) and acquired (thioacetamide-induced acute liver failure) mouse models of liver diseases.
36064721	4	59	theme	rate-limiting	731:743	arg1	synthetase					706:715	carbamoyl phosphate synthetase 1	686:717	carbamoyl phosphate synthetase 1 (CPS1)	686:724	Mechanistically, O-GlcNAcylation on specific threonine residues increased the catalytic efficiency for ammonia of carbamoyl phosphate synthetase 1 (CPS1), the rate-limiting enzyme in ureagenesis.
36064721	4	59	theme	rate-limiting	731:743	arg1	enzyme					745:750	the rate-limiting enzyme	727:750	the rate-limiting enzyme in ureagenesis	727:765	Mechanistically, O-GlcNAcylation on specific threonine residues increased the catalytic efficiency for ammonia of carbamoyl phosphate synthetase 1 (CPS1), the rate-limiting enzyme in ureagenesis.
22687243	4	0	theme	neuronal	552:559	arg1	cells					561:565	neuronal cells	552:565	neuronal cells	552:565	In neuronal cells, O-GlcNAcylation regulated phosphorylation of AKT negatively, but had no effect on GSK-3β.
22687243	0	1	from	regulation	8:17	arg1	types					67:71	various types	59:71	various types of cells	59:80	Diverse regulation of AKT and GSK-3β by O-GlcNAcylation in various types of cells.
22687243	3	2	from	kinases	517:523	arg1	cells					542:546	hepatic HepG2 cells	528:546	hepatic HepG2 cells	528:546	Here, we demonstrate that O-GlcNAcylation regulated phosphorylation/activation of AKT and GSK-3β in different manners in kidney HEK-293FT cells, but did not affect these two kinases in hepatic HepG2 cells.
22687243	5	3	theme	type-specific	706:718	arg1	regulation					720:729	protein-specific and cell type-specific regulation	680:729	protein-specific and cell type-specific regulation of AKT and GSK-3β by O-GlcNAcylation	680:766	These results suggest protein-specific and cell type-specific regulation of AKT and GSK-3β by O-GlcNAcylation.
22687243	6	4	theme	type-specific	872:884	arg1	manner					886:891	a tissue- and cell type-specific manner	853:891	a tissue- and cell type-specific manner	853:891	Therefore, studies on the roles of AKT and GSK-3β O-GlcNAcylation should be done in a tissue- and cell type-specific manner.
22687243	2	5	theme	Recent	246:251	arg1	studies					253:259	Recent studies	246:259	Recent studies	246:259	Recent studies found that these two kinases are modified posttranslationally by O-GlcNAcylation.
22687243	1	6	theme	kinase	91:96	arg1	AKT					101:103	AKT	101:103	AKT	101:103	Protein kinase B (AKT) and glycogen synthase kinase-3β (GSK-3β) are major components of insulin-AKT signaling that plays crucial roles in various types of tissue.
22687243	1	6	theme	kinase	91:96	arg1	components					157:166	major components	151:166	major components of insulin-AKT signaling that plays crucial roles in various types of tissue	151:243	Protein kinase B (AKT) and glycogen synthase kinase-3β (GSK-3β) are major components of insulin-AKT signaling that plays crucial roles in various types of tissue.
22687243	1	6	theme	kinase	91:96	arg1	B					98:98	Protein kinase B	83:98	Protein kinase B (AKT)	83:104	Protein kinase B (AKT) and glycogen synthase kinase-3β (GSK-3β) are major components of insulin-AKT signaling that plays crucial roles in various types of tissue.
22687243	1	6	theme	kinase	91:96	arg1	synthase					119:126	glycogen synthase kinase-3β	110:136	glycogen synthase kinase-3β (GSK-3β)	110:145	Protein kinase B (AKT) and glycogen synthase kinase-3β (GSK-3β) are major components of insulin-AKT signaling that plays crucial roles in various types of tissue.
22687243	1	7	theme	various	221:227	arg1	types					229:233	various types	221:233	various types of tissue	221:243	Protein kinase B (AKT) and glycogen synthase kinase-3β (GSK-3β) are major components of insulin-AKT signaling that plays crucial roles in various types of tissue.
22687243	0	8	theme	cells	76:80	arg1	types					67:71	various types	59:71	various types of cells	59:80	Diverse regulation of AKT and GSK-3β by O-GlcNAcylation in various types of cells.
22687243	5	9	theme	AKT	734:736	arg1	regulation					720:729	protein-specific and cell type-specific regulation	680:729	protein-specific and cell type-specific regulation of AKT and GSK-3β by O-GlcNAcylation	680:766	These results suggest protein-specific and cell type-specific regulation of AKT and GSK-3β by O-GlcNAcylation.
22687243	6	10	theme	tissue-	855:861	arg1	manner					886:891	a tissue- and cell type-specific manner	853:891	a tissue- and cell type-specific manner	853:891	Therefore, studies on the roles of AKT and GSK-3β O-GlcNAcylation should be done in a tissue- and cell type-specific manner.
22687243	3	11	theme	GSK-3β	433:438	arg1	phosphorylation/activation					395:420	phosphorylation/activation	395:420	phosphorylation/activation of AKT and GSK-3β	395:438	Here, we demonstrate that O-GlcNAcylation regulated phosphorylation/activation of AKT and GSK-3β in different manners in kidney HEK-293FT cells, but did not affect these two kinases in hepatic HepG2 cells.
22687243	0	12	theme	Diverse	0:6	arg1	regulation					8:17	Diverse regulation	0:17	Diverse regulation of AKT and GSK-3β by O-GlcNAcylation in various types of cells.	0:81	Diverse regulation of AKT and GSK-3β by O-GlcNAcylation in various types of cells.
22687243	6	13	theme	AKT	804:806	arg1	roles					795:799	the roles	791:799	the roles of AKT and GSK-3β O-GlcNAcylation	791:833	Therefore, studies on the roles of AKT and GSK-3β O-GlcNAcylation should be done in a tissue- and cell type-specific manner.
22687243	3	14	theme	AKT	425:427	arg1	phosphorylation/activation					395:420	phosphorylation/activation	395:420	phosphorylation/activation of AKT and GSK-3β	395:438	Here, we demonstrate that O-GlcNAcylation regulated phosphorylation/activation of AKT and GSK-3β in different manners in kidney HEK-293FT cells, but did not affect these two kinases in hepatic HepG2 cells.
22687243	0	15	theme	AKT	22:24	arg1	regulation					8:17	Diverse regulation	0:17	Diverse regulation of AKT and GSK-3β by O-GlcNAcylation in various types of cells.	0:81	Diverse regulation of AKT and GSK-3β by O-GlcNAcylation in various types of cells.
22687243	1	16	theme	tissue	238:243	arg1	types					229:233	various types	221:233	various types of tissue	221:243	Protein kinase B (AKT) and glycogen synthase kinase-3β (GSK-3β) are major components of insulin-AKT signaling that plays crucial roles in various types of tissue.
22687243	1	17	theme	Protein	83:89	arg1	AKT					101:103	AKT	101:103	AKT	101:103	Protein kinase B (AKT) and glycogen synthase kinase-3β (GSK-3β) are major components of insulin-AKT signaling that plays crucial roles in various types of tissue.
22687243	1	17	theme	Protein	83:89	arg1	components					157:166	major components	151:166	major components of insulin-AKT signaling that plays crucial roles in various types of tissue	151:243	Protein kinase B (AKT) and glycogen synthase kinase-3β (GSK-3β) are major components of insulin-AKT signaling that plays crucial roles in various types of tissue.
22687243	1	17	theme	Protein	83:89	arg1	B					98:98	Protein kinase B	83:98	Protein kinase B (AKT)	83:104	Protein kinase B (AKT) and glycogen synthase kinase-3β (GSK-3β) are major components of insulin-AKT signaling that plays crucial roles in various types of tissue.
22687243	1	17	theme	Protein	83:89	arg1	synthase					119:126	glycogen synthase kinase-3β	110:136	glycogen synthase kinase-3β (GSK-3β)	110:145	Protein kinase B (AKT) and glycogen synthase kinase-3β (GSK-3β) are major components of insulin-AKT signaling that plays crucial roles in various types of tissue.
22687243	1	18	theme	major	151:155	arg1	components					157:166	major components	151:166	major components of insulin-AKT signaling that plays crucial roles in various types of tissue	151:243	Protein kinase B (AKT) and glycogen synthase kinase-3β (GSK-3β) are major components of insulin-AKT signaling that plays crucial roles in various types of tissue.
22687243	1	18	theme	major	151:155	arg1	B					98:98	Protein kinase B	83:98	Protein kinase B (AKT)	83:104	Protein kinase B (AKT) and glycogen synthase kinase-3β (GSK-3β) are major components of insulin-AKT signaling that plays crucial roles in various types of tissue.
22687243	1	18	theme	major	151:155	arg1	synthase					119:126	glycogen synthase kinase-3β	110:136	glycogen synthase kinase-3β (GSK-3β)	110:145	Protein kinase B (AKT) and glycogen synthase kinase-3β (GSK-3β) are major components of insulin-AKT signaling that plays crucial roles in various types of tissue.
22687243	5	19	theme	protein-specific	680:695	arg1	regulation					720:729	protein-specific and cell type-specific regulation	680:729	protein-specific and cell type-specific regulation of AKT and GSK-3β by O-GlcNAcylation	680:766	These results suggest protein-specific and cell type-specific regulation of AKT and GSK-3β by O-GlcNAcylation.
22687243	3	20	theme	HepG2	536:540	arg1	cells					542:546	hepatic HepG2 cells	528:546	hepatic HepG2 cells	528:546	Here, we demonstrate that O-GlcNAcylation regulated phosphorylation/activation of AKT and GSK-3β in different manners in kidney HEK-293FT cells, but did not affect these two kinases in hepatic HepG2 cells.
22687243	4	21	theme	AKT	613:615	arg1	phosphorylation					594:608	phosphorylation	594:608	phosphorylation of AKT	594:615	In neuronal cells, O-GlcNAcylation regulated phosphorylation of AKT negatively, but had no effect on GSK-3β.
22687243	0	22	theme	GSK-3β	30:35	arg1	regulation					8:17	Diverse regulation	0:17	Diverse regulation of AKT and GSK-3β by O-GlcNAcylation in various types of cells.	0:81	Diverse regulation of AKT and GSK-3β by O-GlcNAcylation in various types of cells.
22687243	6	23	from	studies	780:786	arg1	roles					795:799	the roles	791:799	the roles of AKT and GSK-3β O-GlcNAcylation	791:833	Therefore, studies on the roles of AKT and GSK-3β O-GlcNAcylation should be done in a tissue- and cell type-specific manner.
22687243	1	24	theme	insulin-AKT	171:181	arg1	signaling					183:191	insulin-AKT signaling	171:191	insulin-AKT signaling	171:191	Protein kinase B (AKT) and glycogen synthase kinase-3β (GSK-3β) are major components of insulin-AKT signaling that plays crucial roles in various types of tissue.
22687243	6	25	dep	AKT	804:806	arg1	O-GlcNAcylation					819:833	O-GlcNAcylation	819:833	O-GlcNAcylation	819:833	Therefore, studies on the roles of AKT and GSK-3β O-GlcNAcylation should be done in a tissue- and cell type-specific manner.
22687243	3	26	from	manners	453:459	arg1	cells					481:485	kidney HEK-293FT cells	464:485	kidney HEK-293FT cells	464:485	Here, we demonstrate that O-GlcNAcylation regulated phosphorylation/activation of AKT and GSK-3β in different manners in kidney HEK-293FT cells, but did not affect these two kinases in hepatic HepG2 cells.
22687243	6	27	theme	GSK-3β	812:817	arg1	roles					795:799	the roles	791:799	the roles of AKT and GSK-3β O-GlcNAcylation	791:833	Therefore, studies on the roles of AKT and GSK-3β O-GlcNAcylation should be done in a tissue- and cell type-specific manner.
22687243	3	28	theme	kidney	464:469	arg1	cells					481:485	kidney HEK-293FT cells	464:485	kidney HEK-293FT cells	464:485	Here, we demonstrate that O-GlcNAcylation regulated phosphorylation/activation of AKT and GSK-3β in different manners in kidney HEK-293FT cells, but did not affect these two kinases in hepatic HepG2 cells.
22687243	3	29	theme	hepatic	528:534	arg1	cells					542:546	hepatic HepG2 cells	528:546	hepatic HepG2 cells	528:546	Here, we demonstrate that O-GlcNAcylation regulated phosphorylation/activation of AKT and GSK-3β in different manners in kidney HEK-293FT cells, but did not affect these two kinases in hepatic HepG2 cells.
22687243	1	30	theme	signaling	183:191	arg1	components					157:166	major components	151:166	major components of insulin-AKT signaling that plays crucial roles in various types of tissue	151:243	Protein kinase B (AKT) and glycogen synthase kinase-3β (GSK-3β) are major components of insulin-AKT signaling that plays crucial roles in various types of tissue.
22687243	1	30	theme	signaling	183:191	arg1	B					98:98	Protein kinase B	83:98	Protein kinase B (AKT)	83:104	Protein kinase B (AKT) and glycogen synthase kinase-3β (GSK-3β) are major components of insulin-AKT signaling that plays crucial roles in various types of tissue.
22687243	1	30	theme	signaling	183:191	arg1	synthase					119:126	glycogen synthase kinase-3β	110:136	glycogen synthase kinase-3β (GSK-3β)	110:145	Protein kinase B (AKT) and glycogen synthase kinase-3β (GSK-3β) are major components of insulin-AKT signaling that plays crucial roles in various types of tissue.
22687243	4	31	contain	had	633:635	arg2	effect					640:645	no effect	637:645	no effect	637:645	In neuronal cells, O-GlcNAcylation regulated phosphorylation of AKT negatively, but had no effect on GSK-3β.
22687243	4	31	contain	had	633:635	arg1	O-GlcNAcylation					568:582	O-GlcNAcylation	568:582	O-GlcNAcylation	568:582	In neuronal cells, O-GlcNAcylation regulated phosphorylation of AKT negatively, but had no effect on GSK-3β.
22687243	3	32	theme	HEK-293FT	471:479	arg1	cells					481:485	kidney HEK-293FT cells	464:485	kidney HEK-293FT cells	464:485	Here, we demonstrate that O-GlcNAcylation regulated phosphorylation/activation of AKT and GSK-3β in different manners in kidney HEK-293FT cells, but did not affect these two kinases in hepatic HepG2 cells.
22687243	0	33	theme	various	59:65	arg1	types					67:71	various types	59:71	various types of cells	59:80	Diverse regulation of AKT and GSK-3β by O-GlcNAcylation in various types of cells.
22687243	3	34	theme	different	443:451	arg1	manners					453:459	different manners	443:459	different manners in kidney HEK-293FT cells	443:485	Here, we demonstrate that O-GlcNAcylation regulated phosphorylation/activation of AKT and GSK-3β in different manners in kidney HEK-293FT cells, but did not affect these two kinases in hepatic HepG2 cells.
22687243	2	35	mod	modified	294:301	arg1	kinases					282:288	these two kinases	272:288	these two kinases	272:288	Recent studies found that these two kinases are modified posttranslationally by O-GlcNAcylation.
22687243	2	35	mod	modified	294:301	arg3	O-GlcNAcylation					326:340	O-GlcNAcylation	326:340	O-GlcNAcylation	326:340	Recent studies found that these two kinases are modified posttranslationally by O-GlcNAcylation.
22687243	5	36	theme	GSK-3β	742:747	arg1	regulation					720:729	protein-specific and cell type-specific regulation	680:729	protein-specific and cell type-specific regulation of AKT and GSK-3β by O-GlcNAcylation	680:766	These results suggest protein-specific and cell type-specific regulation of AKT and GSK-3β by O-GlcNAcylation.
22687243	1	37	theme	glycogen	110:117	arg1	components					157:166	major components	151:166	major components of insulin-AKT signaling that plays crucial roles in various types of tissue	151:243	Protein kinase B (AKT) and glycogen synthase kinase-3β (GSK-3β) are major components of insulin-AKT signaling that plays crucial roles in various types of tissue.
22687243	1	37	theme	glycogen	110:117	arg1	B					98:98	Protein kinase B	83:98	Protein kinase B (AKT)	83:104	Protein kinase B (AKT) and glycogen synthase kinase-3β (GSK-3β) are major components of insulin-AKT signaling that plays crucial roles in various types of tissue.
22687243	1	37	theme	glycogen	110:117	arg1	synthase					119:126	glycogen synthase kinase-3β	110:136	glycogen synthase kinase-3β (GSK-3β)	110:145	Protein kinase B (AKT) and glycogen synthase kinase-3β (GSK-3β) are major components of insulin-AKT signaling that plays crucial roles in various types of tissue.
22687243	1	37	theme	glycogen	110:117	arg1	GSK-3β					139:144	GSK-3β	139:144	GSK-3β	139:144	Protein kinase B (AKT) and glycogen synthase kinase-3β (GSK-3β) are major components of insulin-AKT signaling that plays crucial roles in various types of tissue.
22687243	1	38	theme	crucial	204:210	arg1	roles					212:216	crucial roles	204:216	crucial roles	204:216	Protein kinase B (AKT) and glycogen synthase kinase-3β (GSK-3β) are major components of insulin-AKT signaling that plays crucial roles in various types of tissue.
29706631	0	0	theme	cell	93:96	arg1	chemoresistance					98:112	cancer cell chemoresistance	86:112	cancer cell chemoresistance	86:112	O-GlcNAc elevation through activation of the hexosamine biosynthetic pathway enhances cancer cell chemoresistance.
29706631	6	1	with	treatment	801:809	arg1	CPT					851:853	CPT	851:853	CPT	851:853	Acute treatment with doxorubicin (DOX) or camptothecin (CPT) induced O-GlcNAcylation through HBP activation.
29706631	6	1	with	treatment	801:809	arg1	DOX					829:831	DOX	829:831	DOX	829:831	Acute treatment with doxorubicin (DOX) or camptothecin (CPT) induced O-GlcNAcylation through HBP activation.
29706631	6	1	with	treatment	801:809	arg1	camptothecin					837:848	camptothecin	837:848	camptothecin (CPT)	837:854	Acute treatment with doxorubicin (DOX) or camptothecin (CPT) induced O-GlcNAcylation through HBP activation.
29706631	6	1	with	treatment	801:809	arg1	doxorubicin					816:826	doxorubicin	816:826	doxorubicin (DOX)	816:832	Acute treatment with doxorubicin (DOX) or camptothecin (CPT) induced O-GlcNAcylation through HBP activation.
29706631	0	2	theme	cancer	86:91	arg1	chemoresistance					98:112	cancer cell chemoresistance	86:112	cancer cell chemoresistance	86:112	O-GlcNAc elevation through activation of the hexosamine biosynthetic pathway enhances cancer cell chemoresistance.
29706631	8	3	theme	observed	1034:1041	arg1	elevation					1043:1051	the observed elevation	1030:1051	the observed elevation of cellular O-GlcNAcylation	1030:1079	Furthermore, the observed elevation of cellular O-GlcNAcylation led to activation of survival signalling pathways and chemoresistance in cancer cells.
29706631	8	4	theme	cellular	1056:1063	arg1	O-GlcNAcylation					1065:1079	cellular O-GlcNAcylation	1056:1079	cellular O-GlcNAcylation	1056:1079	Furthermore, the observed elevation of cellular O-GlcNAcylation led to activation of survival signalling pathways and chemoresistance in cancer cells.
29706631	4	5	theme	important	606:614	arg1	role					616:619	an important role	603:619	an important role	603:619	The results showed that the HBP has an important role in cancer cell chemoresistance by regulating O-GlcNAcylation.
29706631	5	6	theme	cancer	765:770	arg1	cells					772:776	cancer cells	765:776	cancer cells	765:776	An increase in the levels of O-GlcNAcylation indicates an increased resistance of cancer cells to chemotherapy.
29706631	10	7	theme	O-GlcNAcylation	1386:1400	arg1	role					1366:1369	the important role	1352:1369	the important role of the HBP and O-GlcNAcylation in regulating cancer chemoresistance	1352:1437	These results provide significant novel insights regarding the important role of the HBP and O-GlcNAcylation in regulating cancer chemoresistance.
29706631	7	8	theme	XBP1	980:983	arg1	axis					986:989	the AKT/X-box-binding protein 1 (XBP1) axis	947:989	the AKT/X-box-binding protein 1 (XBP1) axis	947:989	In fact, the chemotherapy agents activated the AKT/X-box-binding protein 1 (XBP1) axis and then induced the HBP.
29706631	3	9	theme	O-GlcNAcylation	479:493	arg1	role					471:474	the role	467:474	the role of O-GlcNAcylation in chemoresistance	467:512	Here we assessed the role of O-GlcNAcylation in chemoresistance and investigated the underlying cellular mechanisms.
29706631	5	10	theme	cells	772:776	arg1	resistance					751:760	an increased resistance	738:760	an increased resistance of cancer cells to chemotherapy	738:792	An increase in the levels of O-GlcNAcylation indicates an increased resistance of cancer cells to chemotherapy.
29706631	2	11	theme	post-translational	290:307	arg1	modification					309:320	a post-translational modification	288:320	a post-translational modification that is regulated by the hexosamine biosynthetic pathway (HBP) and has an important role in a wide range of cellular functions	288:447	O-GlcNAcylation is a post-translational modification that is regulated by the hexosamine biosynthetic pathway (HBP) and has an important role in a wide range of cellular functions.
29706631	2	11	theme	post-translational	290:307	arg1	O-GlcNAcylation					269:283	O-GlcNAcylation	269:283	O-GlcNAcylation	269:283	O-GlcNAcylation is a post-translational modification that is regulated by the hexosamine biosynthetic pathway (HBP) and has an important role in a wide range of cellular functions.
29706631	1	12	theme	cancer	177:182	arg1	therapy					184:190	cancer therapy	177:190	cancer therapy	177:190	Chemoresistance has become a major obstacle to the success of cancer therapy, but the mechanisms underlying chemoresistance are not yet fully understood.
29706631	8	13	theme	O-GlcNAcylation	1065:1079	arg1	elevation					1043:1051	the observed elevation	1030:1051	the observed elevation of cellular O-GlcNAcylation	1030:1079	Furthermore, the observed elevation of cellular O-GlcNAcylation led to activation of survival signalling pathways and chemoresistance in cancer cells.
29706631	9	14	theme	established	1239:1249	arg1	cells					1270:1274	both established and primary cancer cells	1234:1274	both established and primary cancer cells	1234:1274	Finally, suppression of O-GlcNAcylation reduced the resistance of both established and primary cancer cells to chemotherapy.
29706631	8	15	theme	pathways	1122:1129	arg1	chemoresistance					1135:1149	chemoresistance	1135:1149	chemoresistance in cancer cells	1135:1165	Furthermore, the observed elevation of cellular O-GlcNAcylation led to activation of survival signalling pathways and chemoresistance in cancer cells.
29706631	8	15	theme	pathways	1122:1129	arg1	activation					1088:1097	activation	1088:1097	activation of survival signalling pathways	1088:1129	Furthermore, the observed elevation of cellular O-GlcNAcylation led to activation of survival signalling pathways and chemoresistance in cancer cells.
29706631	1	16	theme	therapy	184:190	arg1	success					166:172	the success	162:172	the success of cancer therapy	162:190	Chemoresistance has become a major obstacle to the success of cancer therapy, but the mechanisms underlying chemoresistance are not yet fully understood.
29706631	2	17	contain	has	389:391	arg1	modification					309:320	a post-translational modification	288:320	a post-translational modification that is regulated by the hexosamine biosynthetic pathway (HBP) and has an important role in a wide range of cellular functions	288:447	O-GlcNAcylation is a post-translational modification that is regulated by the hexosamine biosynthetic pathway (HBP) and has an important role in a wide range of cellular functions.
29706631	2	17	contain	has	389:391	arg1	O-GlcNAcylation					269:283	O-GlcNAcylation	269:283	O-GlcNAcylation	269:283	O-GlcNAcylation is a post-translational modification that is regulated by the hexosamine biosynthetic pathway (HBP) and has an important role in a wide range of cellular functions.
29706631	2	17	contain	has	389:391	arg2	role					406:409	an important role	393:409	an important role	393:409	O-GlcNAcylation is a post-translational modification that is regulated by the hexosamine biosynthetic pathway (HBP) and has an important role in a wide range of cellular functions.
29706631	10	18	theme	HBP	1378:1380	arg1	role					1366:1369	the important role	1352:1369	the important role of the HBP and O-GlcNAcylation in regulating cancer chemoresistance	1352:1437	These results provide significant novel insights regarding the important role of the HBP and O-GlcNAcylation in regulating cancer chemoresistance.
29706631	10	19	theme	novel	1327:1331	arg1	insights					1333:1340	significant novel insights	1315:1340	significant novel insights regarding the important role of the HBP and O-GlcNAcylation in regulating cancer chemoresistance	1315:1437	These results provide significant novel insights regarding the important role of the HBP and O-GlcNAcylation in regulating cancer chemoresistance.
29706631	2	20	theme	important	396:404	arg1	role					406:409	an important role	393:409	an important role	393:409	O-GlcNAcylation is a post-translational modification that is regulated by the hexosamine biosynthetic pathway (HBP) and has an important role in a wide range of cellular functions.
29706631	0	21	theme	O-GlcNAc	0:7	arg1	elevation					9:17	O-GlcNAc elevation	0:17	O-GlcNAc elevation through activation of the hexosamine biosynthetic pathway	0:75	O-GlcNAc elevation through activation of the hexosamine biosynthetic pathway enhances cancer cell chemoresistance.
29706631	7	22	theme	AKT/X-box-binding	951:967	arg1	axis					986:989	the AKT/X-box-binding protein 1 (XBP1) axis	947:989	the AKT/X-box-binding protein 1 (XBP1) axis	947:989	In fact, the chemotherapy agents activated the AKT/X-box-binding protein 1 (XBP1) axis and then induced the HBP.
29706631	11	23	theme	chemotherapy	1523:1534	arg1	efficacy					1511:1518	the efficacy	1507:1518	the efficacy of chemotherapy	1507:1534	Thus, O-GlcNAc inhibition might offer a new strategy for improving the efficacy of chemotherapy.
29706631	2	24	theme	functions	439:447	arg1	range					421:425	a wide range	414:425	a wide range of cellular functions	414:447	O-GlcNAcylation is a post-translational modification that is regulated by the hexosamine biosynthetic pathway (HBP) and has an important role in a wide range of cellular functions.
29706631	9	25	theme	primary	1255:1261	arg1	cells					1270:1274	both established and primary cancer cells	1234:1274	both established and primary cancer cells	1234:1274	Finally, suppression of O-GlcNAcylation reduced the resistance of both established and primary cancer cells to chemotherapy.
29706631	8	26	theme	survival	1102:1109	arg1	pathways					1122:1129	survival signalling pathways	1102:1129	survival signalling pathways	1102:1129	Furthermore, the observed elevation of cellular O-GlcNAcylation led to activation of survival signalling pathways and chemoresistance in cancer cells.
29706631	7	27	theme	protein	969:975	arg1	axis					986:989	the AKT/X-box-binding protein 1 (XBP1) axis	947:989	the AKT/X-box-binding protein 1 (XBP1) axis	947:989	In fact, the chemotherapy agents activated the AKT/X-box-binding protein 1 (XBP1) axis and then induced the HBP.
29706631	10	28	dep	HBP	1378:1380	arg1	the					1374:1376	the	1374:1376	the	1374:1376	These results provide significant novel insights regarding the important role of the HBP and O-GlcNAcylation in regulating cancer chemoresistance.
29706631	2	29	theme	cellular	430:437	arg1	functions					439:447	cellular functions	430:447	cellular functions	430:447	O-GlcNAcylation is a post-translational modification that is regulated by the hexosamine biosynthetic pathway (HBP) and has an important role in a wide range of cellular functions.
29706631	3	30	theme	cellular	546:553	arg1	mechanisms					555:564	the underlying cellular mechanisms	531:564	the underlying cellular mechanisms	531:564	Here we assessed the role of O-GlcNAcylation in chemoresistance and investigated the underlying cellular mechanisms.
29706631	9	31	theme	cells	1270:1274	arg1	resistance					1220:1229	the resistance	1216:1229	the resistance of both established and primary cancer cells to chemotherapy	1216:1290	Finally, suppression of O-GlcNAcylation reduced the resistance of both established and primary cancer cells to chemotherapy.
29706631	5	32	theme	increased	741:749	arg1	resistance					751:760	an increased resistance	738:760	an increased resistance of cancer cells to chemotherapy	738:792	An increase in the levels of O-GlcNAcylation indicates an increased resistance of cancer cells to chemotherapy.
29706631	10	33	theme	important	1356:1364	arg1	role					1366:1369	the important role	1352:1369	the important role of the HBP and O-GlcNAcylation in regulating cancer chemoresistance	1352:1437	These results provide significant novel insights regarding the important role of the HBP and O-GlcNAcylation in regulating cancer chemoresistance.
29706631	2	34	theme	wide	416:419	arg1	range					421:425	a wide range	414:425	a wide range of cellular functions	414:447	O-GlcNAcylation is a post-translational modification that is regulated by the hexosamine biosynthetic pathway (HBP) and has an important role in a wide range of cellular functions.
29706631	5	35	from	increase	686:693	arg1	levels					702:707	the levels	698:707	the levels of O-GlcNAcylation	698:726	An increase in the levels of O-GlcNAcylation indicates an increased resistance of cancer cells to chemotherapy.
29706631	8	36	theme	signalling	1111:1120	arg1	pathways					1122:1129	survival signalling pathways	1102:1129	survival signalling pathways	1102:1129	Furthermore, the observed elevation of cellular O-GlcNAcylation led to activation of survival signalling pathways and chemoresistance in cancer cells.
29706631	6	37	theme	HBP	888:890	arg1	activation					892:901	HBP activation	888:901	HBP activation	888:901	Acute treatment with doxorubicin (DOX) or camptothecin (CPT) induced O-GlcNAcylation through HBP activation.
29706631	0	38	theme	biosynthetic	56:67	arg1	pathway					69:75	the hexosamine biosynthetic pathway	41:75	the hexosamine biosynthetic pathway	41:75	O-GlcNAc elevation through activation of the hexosamine biosynthetic pathway enhances cancer cell chemoresistance.
29706631	8	39	from	activation	1088:1097	arg1	cells					1161:1165	cancer cells	1154:1165	cancer cells	1154:1165	Furthermore, the observed elevation of cellular O-GlcNAcylation led to activation of survival signalling pathways and chemoresistance in cancer cells.
29706631	6	40	theme	Acute	795:799	arg1	treatment					801:809	Acute treatment	795:809	Acute treatment with doxorubicin (DOX) or camptothecin (CPT)	795:854	Acute treatment with doxorubicin (DOX) or camptothecin (CPT) induced O-GlcNAcylation through HBP activation.
29706631	0	41	theme	hexosamine	45:54	arg1	pathway					69:75	the hexosamine biosynthetic pathway	41:75	the hexosamine biosynthetic pathway	41:75	O-GlcNAc elevation through activation of the hexosamine biosynthetic pathway enhances cancer cell chemoresistance.
29706631	4	42	contain	has	599:601	arg1	HBP					595:597	the HBP	591:597	the HBP	591:597	The results showed that the HBP has an important role in cancer cell chemoresistance by regulating O-GlcNAcylation.
29706631	4	42	contain	has	599:601	arg2	role					616:619	an important role	603:619	an important role	603:619	The results showed that the HBP has an important role in cancer cell chemoresistance by regulating O-GlcNAcylation.
29706631	9	43	theme	cancer	1263:1268	arg1	cells					1270:1274	both established and primary cancer cells	1234:1274	both established and primary cancer cells	1234:1274	Finally, suppression of O-GlcNAcylation reduced the resistance of both established and primary cancer cells to chemotherapy.
29706631	8	44	theme	cancer	1154:1159	arg1	cells					1161:1165	cancer cells	1154:1165	cancer cells	1154:1165	Furthermore, the observed elevation of cellular O-GlcNAcylation led to activation of survival signalling pathways and chemoresistance in cancer cells.
29706631	3	45	from	role	471:474	arg1	chemoresistance					498:512	chemoresistance	498:512	chemoresistance	498:512	Here we assessed the role of O-GlcNAcylation in chemoresistance and investigated the underlying cellular mechanisms.
29706631	1	46	theme	major	144:148	arg1	obstacle					150:157	a major obstacle	142:157	a major obstacle to the success of cancer therapy	142:190	Chemoresistance has become a major obstacle to the success of cancer therapy, but the mechanisms underlying chemoresistance are not yet fully understood.
29706631	10	47	theme	cancer	1416:1421	arg1	chemoresistance					1423:1437	cancer chemoresistance	1416:1437	cancer chemoresistance	1416:1437	These results provide significant novel insights regarding the important role of the HBP and O-GlcNAcylation in regulating cancer chemoresistance.
29706631	8	48	from	chemoresistance	1135:1149	arg1	cells					1161:1165	cancer cells	1154:1165	cancer cells	1154:1165	Furthermore, the observed elevation of cellular O-GlcNAcylation led to activation of survival signalling pathways and chemoresistance in cancer cells.
29706631	5	49	theme	O-GlcNAcylation	712:726	arg1	levels					702:707	the levels	698:707	the levels of O-GlcNAcylation	698:726	An increase in the levels of O-GlcNAcylation indicates an increased resistance of cancer cells to chemotherapy.
29706631	11	50	theme	new	1480:1482	arg1	strategy					1484:1491	a new strategy	1478:1491	a new strategy for improving the efficacy of chemotherapy	1478:1534	Thus, O-GlcNAc inhibition might offer a new strategy for improving the efficacy of chemotherapy.
29706631	2	51	theme	hexosamine	347:356	arg1	pathway					371:377	the hexosamine biosynthetic pathway	343:377	the hexosamine biosynthetic pathway (HBP)	343:383	O-GlcNAcylation is a post-translational modification that is regulated by the hexosamine biosynthetic pathway (HBP) and has an important role in a wide range of cellular functions.
29706631	2	51	theme	hexosamine	347:356	arg1	HBP					380:382	HBP	380:382	HBP	380:382	O-GlcNAcylation is a post-translational modification that is regulated by the hexosamine biosynthetic pathway (HBP) and has an important role in a wide range of cellular functions.
29706631	7	52	theme	chemotherapy	917:928	arg1	agents					930:935	the chemotherapy agents	913:935	the chemotherapy agents	913:935	In fact, the chemotherapy agents activated the AKT/X-box-binding protein 1 (XBP1) axis and then induced the HBP.
29706631	2	53	theme	biosynthetic	358:369	arg1	pathway					371:377	the hexosamine biosynthetic pathway	343:377	the hexosamine biosynthetic pathway (HBP)	343:383	O-GlcNAcylation is a post-translational modification that is regulated by the hexosamine biosynthetic pathway (HBP) and has an important role in a wide range of cellular functions.
29706631	2	53	theme	biosynthetic	358:369	arg1	HBP					380:382	HBP	380:382	HBP	380:382	O-GlcNAcylation is a post-translational modification that is regulated by the hexosamine biosynthetic pathway (HBP) and has an important role in a wide range of cellular functions.
29706631	11	54	theme	O-GlcNAc	1446:1453	arg1	inhibition					1455:1464	O-GlcNAc inhibition	1446:1464	O-GlcNAc inhibition	1446:1464	Thus, O-GlcNAc inhibition might offer a new strategy for improving the efficacy of chemotherapy.
29706631	4	55	theme	cell	631:634	arg1	chemoresistance					636:650	cancer cell chemoresistance	624:650	cancer cell chemoresistance	624:650	The results showed that the HBP has an important role in cancer cell chemoresistance by regulating O-GlcNAcylation.
29706631	0	56	theme	pathway	69:75	arg1	activation					27:36	activation	27:36	activation of the hexosamine biosynthetic pathway	27:75	O-GlcNAc elevation through activation of the hexosamine biosynthetic pathway enhances cancer cell chemoresistance.
29706631	9	57	theme	O-GlcNAcylation	1192:1206	arg1	suppression					1177:1187	suppression	1177:1187	suppression of O-GlcNAcylation	1177:1206	Finally, suppression of O-GlcNAcylation reduced the resistance of both established and primary cancer cells to chemotherapy.
29706631	3	58	theme	underlying	535:544	arg1	mechanisms					555:564	the underlying cellular mechanisms	531:564	the underlying cellular mechanisms	531:564	Here we assessed the role of O-GlcNAcylation in chemoresistance and investigated the underlying cellular mechanisms.
29706631	10	59	theme	significant	1315:1325	arg1	insights					1333:1340	significant novel insights	1315:1340	significant novel insights regarding the important role of the HBP and O-GlcNAcylation in regulating cancer chemoresistance	1315:1437	These results provide significant novel insights regarding the important role of the HBP and O-GlcNAcylation in regulating cancer chemoresistance.
29706631	4	60	theme	cancer	624:629	arg1	chemoresistance					636:650	cancer cell chemoresistance	624:650	cancer cell chemoresistance	624:650	The results showed that the HBP has an important role in cancer cell chemoresistance by regulating O-GlcNAcylation.
18728220	4	0	theme	O-GlcNAc	493:500	arg1	effect					483:488	the effect	479:488	the effect of O-GlcNAc on hepatic Akt signaling at physiological concentrations of glucose	479:568	Here we investigated the effect of O-GlcNAc on hepatic Akt signaling at physiological concentrations of glucose.
18728220	5	1	theme	adenoviral-mediated	635:653	arg1	overexpression					655:668	adenoviral-mediated overexpression	635:668	adenoviral-mediated overexpression of O-GlcNAcase	635:683	In HepG2 cells cultured in 5 mM glucose, removal of O-GlcNAc by adenoviral-mediated overexpression of O-GlcNAcase increased Akt activity and phosphorylation.
18728220	9	2	theme	activator	1198:1206	arg1	3-kinase					1225:1232	its upstream activator phosphoinositide 3-kinase	1185:1232	its upstream activator phosphoinositide 3-kinase (PI 3-kinase)	1185:1246	The increased Akt activity was not a result of activation of its upstream activator phosphoinositide 3-kinase (PI 3-kinase).
18728220	9	2	theme	activator	1198:1206	arg1	3-kinase					1238:1245	PI 3-kinase	1235:1245	PI 3-kinase	1235:1245	The increased Akt activity was not a result of activation of its upstream activator phosphoinositide 3-kinase (PI 3-kinase).
18728220	2	3	theme	insulin	369:375	arg1	resistance					377:386	insulin resistance	369:386	insulin resistance	369:386	Numerous studies have demonstrated that, in hyperglycemic conditions, excessive glucose flux through this pathway contributes to the development of insulin resistance.
18728220	7	4	from	Overexpression	851:864	arg1	cells					890:894	HepG2 cells	884:894	HepG2 cells	884:894	Overexpression of O-GlcNAcase in HepG2 cells reduced the levels of Akt in sWGA precipitates.
18728220	4	5	theme	Akt	513:515	arg1	signaling					517:525	hepatic Akt signaling	505:525	hepatic Akt signaling at physiological concentrations of glucose	505:568	Here we investigated the effect of O-GlcNAc on hepatic Akt signaling at physiological concentrations of glucose.
18728220	5	6	theme	5	598:598	arg1	mM					600:601	mM	600:601	mM	600:601	In HepG2 cells cultured in 5 mM glucose, removal of O-GlcNAc by adenoviral-mediated overexpression of O-GlcNAcase increased Akt activity and phosphorylation.
18728220	1	7	theme	cytoplasmic	157:167	arg1	protein					169:175	nuclear and cytoplasmic protein	145:175	nuclear and cytoplasmic protein	145:175	The hexosamine biosynthesis pathway (HBP) regulates the posttranslational modification of nuclear and cytoplasmic protein by O-linked N-acetylglucosamine (O-GlcNAc).
18728220	10	8	theme	Akt	1405:1407	arg1	activity					1409:1416	Akt activity	1405:1416	Akt activity	1405:1416	Further demonstrating Akt regulation by O-GlcNAc, we found that overexpression of O-GlcNAcase in the livers of euglycemic mice also significantly increased Akt activity, resulting in increased phosphorylation of downstream targets and decreased mRNA for glucose-6-phosphatase.
18728220	0	9	from	Regulation	0:9	arg1	euglycemia					43:52	euglycemia	43:52	euglycemia	43:52	Regulation of Akt signaling by O-GlcNAc in euglycemia.
18728220	5	10	theme	mM	600:601	arg1	glucose					603:609	5 mM glucose	598:609	5 mM glucose	598:609	In HepG2 cells cultured in 5 mM glucose, removal of O-GlcNAc by adenoviral-mediated overexpression of O-GlcNAcase increased Akt activity and phosphorylation.
18728220	2	11	theme	glucose	301:307	arg1	flux					309:312	excessive glucose flux	291:312	excessive glucose flux through this pathway	291:333	Numerous studies have demonstrated that, in hyperglycemic conditions, excessive glucose flux through this pathway contributes to the development of insulin resistance.
18728220	11	12	theme	Akt	1579:1581	arg1	signaling					1583:1591	Akt signaling	1579:1591	Akt signaling in hepatic models	1579:1609	Together, these data suggest that O-GlcNAc regulates Akt signaling in hepatic models under euglycemic conditions.
18728220	5	13	theme	O-GlcNAcase	673:683	arg1	overexpression					655:668	adenoviral-mediated overexpression	635:668	adenoviral-mediated overexpression of O-GlcNAcase	635:683	In HepG2 cells cultured in 5 mM glucose, removal of O-GlcNAc by adenoviral-mediated overexpression of O-GlcNAcase increased Akt activity and phosphorylation.
18728220	11	14	theme	hepatic	1596:1602	arg1	models					1604:1609	hepatic models	1596:1609	hepatic models	1596:1609	Together, these data suggest that O-GlcNAc regulates Akt signaling in hepatic models under euglycemic conditions.
18728220	2	15	theme	excessive	291:299	arg1	flux					309:312	excessive glucose flux	291:312	excessive glucose flux through this pathway	291:333	Numerous studies have demonstrated that, in hyperglycemic conditions, excessive glucose flux through this pathway contributes to the development of insulin resistance.
18728220	10	16	theme	O-GlcNAcase	1331:1341	arg1	overexpression					1313:1326	overexpression	1313:1326	overexpression of O-GlcNAcase in the livers of euglycemic mice	1313:1374	Further demonstrating Akt regulation by O-GlcNAc, we found that overexpression of O-GlcNAcase in the livers of euglycemic mice also significantly increased Akt activity, resulting in increased phosphorylation of downstream targets and decreased mRNA for glucose-6-phosphatase.
18728220	9	17	theme	increased	1128:1136	arg1	activity					1142:1149	The increased Akt activity	1124:1149	The increased Akt activity	1124:1149	The increased Akt activity was not a result of activation of its upstream activator phosphoinositide 3-kinase (PI 3-kinase).
18728220	9	17	theme	increased	1128:1136	arg1	result					1161:1166	a result	1159:1166	a result of activation of its upstream activator phosphoinositide 3-kinase (PI 3-kinase)	1159:1246	The increased Akt activity was not a result of activation of its upstream activator phosphoinositide 3-kinase (PI 3-kinase).
18728220	3	18	from	role	393:396	arg1	euglycemia					412:421	euglycemia	412:421	euglycemia	412:421	The role of the HBP in euglycemia, however, remains largely unknown.
18728220	1	19	link	O-linked	180:187	arg1	O-GlcNAc					210:217	O-GlcNAc	210:217	O-GlcNAc	210:217	The hexosamine biosynthesis pathway (HBP) regulates the posttranslational modification of nuclear and cytoplasmic protein by O-linked N-acetylglucosamine (O-GlcNAc).
18728220	1	19	link	O-linked	180:187	arg1	N-acetylglucosamine					189:207	O-linked N-acetylglucosamine	180:207	O-linked N-acetylglucosamine (O-GlcNAc)	180:218	The hexosamine biosynthesis pathway (HBP) regulates the posttranslational modification of nuclear and cytoplasmic protein by O-linked N-acetylglucosamine (O-GlcNAc).
18728220	9	20	theme	PI	1235:1236	arg1	3-kinase					1225:1232	its upstream activator phosphoinositide 3-kinase	1185:1232	its upstream activator phosphoinositide 3-kinase (PI 3-kinase)	1185:1246	The increased Akt activity was not a result of activation of its upstream activator phosphoinositide 3-kinase (PI 3-kinase).
18728220	9	20	theme	PI	1235:1236	arg1	3-kinase					1238:1245	PI 3-kinase	1235:1245	PI 3-kinase	1235:1245	The increased Akt activity was not a result of activation of its upstream activator phosphoinositide 3-kinase (PI 3-kinase).
18728220	1	21	theme	hexosamine	59:68	arg1	HBP					92:94	HBP	92:94	HBP	92:94	The hexosamine biosynthesis pathway (HBP) regulates the posttranslational modification of nuclear and cytoplasmic protein by O-linked N-acetylglucosamine (O-GlcNAc).
18728220	1	21	theme	hexosamine	59:68	arg1	pathway					83:89	The hexosamine biosynthesis pathway	55:89	The hexosamine biosynthesis pathway (HBP)	55:95	The hexosamine biosynthesis pathway (HBP) regulates the posttranslational modification of nuclear and cytoplasmic protein by O-linked N-acetylglucosamine (O-GlcNAc).
18728220	7	22	theme	HepG2	884:888	arg1	cells					890:894	HepG2 cells	884:894	HepG2 cells	884:894	Overexpression of O-GlcNAcase in HepG2 cells reduced the levels of Akt in sWGA precipitates.
18728220	1	23	theme	protein	169:175	arg1	modification					129:140	the posttranslational modification	107:140	the posttranslational modification of nuclear and cytoplasmic protein	107:175	The hexosamine biosynthesis pathway (HBP) regulates the posttranslational modification of nuclear and cytoplasmic protein by O-linked N-acetylglucosamine (O-GlcNAc).
18728220	4	24	from	effect	483:488	arg1	signaling					517:525	hepatic Akt signaling	505:525	hepatic Akt signaling at physiological concentrations of glucose	505:568	Here we investigated the effect of O-GlcNAc on hepatic Akt signaling at physiological concentrations of glucose.
18728220	5	25	theme	HepG2	574:578	arg1	cells					580:584	HepG2 cells	574:584	HepG2 cells cultured in 5 mM glucose	574:609	In HepG2 cells cultured in 5 mM glucose, removal of O-GlcNAc by adenoviral-mediated overexpression of O-GlcNAcase increased Akt activity and phosphorylation.
18728220	1	26	theme	biosynthesis	70:81	arg1	HBP					92:94	HBP	92:94	HBP	92:94	The hexosamine biosynthesis pathway (HBP) regulates the posttranslational modification of nuclear and cytoplasmic protein by O-linked N-acetylglucosamine (O-GlcNAc).
18728220	1	26	theme	biosynthesis	70:81	arg1	pathway					83:89	The hexosamine biosynthesis pathway	55:89	The hexosamine biosynthesis pathway (HBP)	55:95	The hexosamine biosynthesis pathway (HBP) regulates the posttranslational modification of nuclear and cytoplasmic protein by O-linked N-acetylglucosamine (O-GlcNAc).
18728220	5	27	theme	O-GlcNAc	623:630	arg1	removal					612:618	removal	612:618	removal of O-GlcNAc by adenoviral-mediated overexpression of O-GlcNAcase	612:683	In HepG2 cells cultured in 5 mM glucose, removal of O-GlcNAc by adenoviral-mediated overexpression of O-GlcNAcase increased Akt activity and phosphorylation.
18728220	8	28	theme	Akt	1019:1021	arg1	substrates					1023:1032	Akt substrates	1019:1032	Akt substrates	1019:1032	The increased Akt activity was accompanied by increased phosphorylation of Akt substrates and reduced mRNA for glucose-6-phosphatase and phosphoenolpyruvate carboxykinase (PEPCK).
18728220	7	29	theme	O-GlcNAcase	869:879	arg1	Overexpression					851:864	Overexpression	851:864	Overexpression of O-GlcNAcase in HepG2 cells	851:894	Overexpression of O-GlcNAcase in HepG2 cells reduced the levels of Akt in sWGA precipitates.
18728220	1	30	theme	O-linked	180:187	arg1	O-GlcNAc					210:217	O-GlcNAc	210:217	O-GlcNAc	210:217	The hexosamine biosynthesis pathway (HBP) regulates the posttranslational modification of nuclear and cytoplasmic protein by O-linked N-acetylglucosamine (O-GlcNAc).
18728220	1	30	theme	O-linked	180:187	arg1	N-acetylglucosamine					189:207	O-linked N-acetylglucosamine	180:207	O-linked N-acetylglucosamine (O-GlcNAc)	180:218	The hexosamine biosynthesis pathway (HBP) regulates the posttranslational modification of nuclear and cytoplasmic protein by O-linked N-acetylglucosamine (O-GlcNAc).
18728220	4	31	theme	glucose	562:568	arg1	concentrations					544:557	physiological concentrations	530:557	physiological concentrations of glucose	530:568	Here we investigated the effect of O-GlcNAc on hepatic Akt signaling at physiological concentrations of glucose.
18728220	8	32	theme	reduced	1038:1044	arg1	mRNA					1046:1049	reduced mRNA	1038:1049	reduced mRNA for glucose-6-phosphatase and phosphoenolpyruvate carboxykinase (PEPCK)	1038:1121	The increased Akt activity was accompanied by increased phosphorylation of Akt substrates and reduced mRNA for glucose-6-phosphatase and phosphoenolpyruvate carboxykinase (PEPCK).
18728220	9	33	theme	Akt	1138:1140	arg1	activity					1142:1149	The increased Akt activity	1124:1149	The increased Akt activity	1124:1149	The increased Akt activity was not a result of activation of its upstream activator phosphoinositide 3-kinase (PI 3-kinase).
18728220	9	33	theme	Akt	1138:1140	arg1	result					1161:1166	a result	1159:1166	a result of activation of its upstream activator phosphoinositide 3-kinase (PI 3-kinase)	1159:1246	The increased Akt activity was not a result of activation of its upstream activator phosphoinositide 3-kinase (PI 3-kinase).
18728220	0	34	theme	signaling	18:26	arg1	Regulation					0:9	Regulation	0:9	Regulation of Akt signaling by O-GlcNAc in euglycemia.	0:53	Regulation of Akt signaling by O-GlcNAc in euglycemia.
18728220	10	35	theme	downstream	1461:1470	arg1	targets					1472:1478	downstream targets	1461:1478	downstream targets	1461:1478	Further demonstrating Akt regulation by O-GlcNAc, we found that overexpression of O-GlcNAcase in the livers of euglycemic mice also significantly increased Akt activity, resulting in increased phosphorylation of downstream targets and decreased mRNA for glucose-6-phosphatase.
18728220	6	36	theme	germ	792:795	arg1	sWGA					809:812	sWGA	809:812	sWGA	809:812	We also observed that Akt was recognized by succinylated wheat germ agglutinin (sWGA), which specifically binds O-GlcNAc.
18728220	6	36	theme	germ	792:795	arg1	agglutinin					797:806	succinylated wheat germ agglutinin	773:806	succinylated wheat germ agglutinin (sWGA)	773:813	We also observed that Akt was recognized by succinylated wheat germ agglutinin (sWGA), which specifically binds O-GlcNAc.
18728220	9	37	theme	3-kinase	1225:1232	arg1	activation					1171:1180	activation	1171:1180	activation of its upstream activator phosphoinositide 3-kinase (PI 3-kinase)	1171:1246	The increased Akt activity was not a result of activation of its upstream activator phosphoinositide 3-kinase (PI 3-kinase).
18728220	8	38	theme	increased	990:998	arg1	phosphorylation					1000:1014	increased phosphorylation	990:1014	increased phosphorylation of Akt substrates	990:1032	The increased Akt activity was accompanied by increased phosphorylation of Akt substrates and reduced mRNA for glucose-6-phosphatase and phosphoenolpyruvate carboxykinase (PEPCK).
18728220	0	39	theme	Akt	14:16	arg1	signaling					18:26	Akt signaling	14:26	Akt signaling	14:26	Regulation of Akt signaling by O-GlcNAc in euglycemia.
18728220	10	40	theme	mice	1371:1374	arg1	livers					1350:1355	the livers	1346:1355	the livers of euglycemic mice	1346:1374	Further demonstrating Akt regulation by O-GlcNAc, we found that overexpression of O-GlcNAcase in the livers of euglycemic mice also significantly increased Akt activity, resulting in increased phosphorylation of downstream targets and decreased mRNA for glucose-6-phosphatase.
18728220	10	41	theme	targets	1472:1478	arg1	phosphorylation					1442:1456	increased phosphorylation	1432:1456	increased phosphorylation of downstream targets	1432:1478	Further demonstrating Akt regulation by O-GlcNAc, we found that overexpression of O-GlcNAcase in the livers of euglycemic mice also significantly increased Akt activity, resulting in increased phosphorylation of downstream targets and decreased mRNA for glucose-6-phosphatase.
18728220	4	42	from	concentrations	544:557	arg1	signaling					517:525	hepatic Akt signaling	505:525	hepatic Akt signaling at physiological concentrations of glucose	505:568	Here we investigated the effect of O-GlcNAc on hepatic Akt signaling at physiological concentrations of glucose.
18728220	10	43	from	overexpression	1313:1326	arg1	livers					1350:1355	the livers	1346:1355	the livers of euglycemic mice	1346:1374	Further demonstrating Akt regulation by O-GlcNAc, we found that overexpression of O-GlcNAcase in the livers of euglycemic mice also significantly increased Akt activity, resulting in increased phosphorylation of downstream targets and decreased mRNA for glucose-6-phosphatase.
18728220	11	44	theme	euglycemic	1617:1626	arg1	conditions					1628:1637	euglycemic conditions	1617:1637	euglycemic conditions	1617:1637	Together, these data suggest that O-GlcNAc regulates Akt signaling in hepatic models under euglycemic conditions.
18728220	6	45	theme	wheat	786:790	arg1	sWGA					809:812	sWGA	809:812	sWGA	809:812	We also observed that Akt was recognized by succinylated wheat germ agglutinin (sWGA), which specifically binds O-GlcNAc.
18728220	6	45	theme	wheat	786:790	arg1	agglutinin					797:806	succinylated wheat germ agglutinin	773:806	succinylated wheat germ agglutinin (sWGA)	773:813	We also observed that Akt was recognized by succinylated wheat germ agglutinin (sWGA), which specifically binds O-GlcNAc.
18728220	11	46	from	signaling	1583:1591	arg1	models					1604:1609	hepatic models	1596:1609	hepatic models	1596:1609	Together, these data suggest that O-GlcNAc regulates Akt signaling in hepatic models under euglycemic conditions.
18728220	3	47	theme	HBP	405:407	arg1	role					393:396	The role	389:396	The role of the HBP in euglycemia	389:421	The role of the HBP in euglycemia, however, remains largely unknown.
18728220	6	48	theme	succinylated	773:784	arg1	sWGA					809:812	sWGA	809:812	sWGA	809:812	We also observed that Akt was recognized by succinylated wheat germ agglutinin (sWGA), which specifically binds O-GlcNAc.
18728220	6	48	theme	succinylated	773:784	arg1	agglutinin					797:806	succinylated wheat germ agglutinin	773:806	succinylated wheat germ agglutinin (sWGA)	773:813	We also observed that Akt was recognized by succinylated wheat germ agglutinin (sWGA), which specifically binds O-GlcNAc.
18728220	9	49	theme	phosphoinositide	1208:1223	arg1	3-kinase					1225:1232	its upstream activator phosphoinositide 3-kinase	1185:1232	its upstream activator phosphoinositide 3-kinase (PI 3-kinase)	1185:1246	The increased Akt activity was not a result of activation of its upstream activator phosphoinositide 3-kinase (PI 3-kinase).
18728220	9	49	theme	phosphoinositide	1208:1223	arg1	3-kinase					1238:1245	PI 3-kinase	1235:1245	PI 3-kinase	1235:1245	The increased Akt activity was not a result of activation of its upstream activator phosphoinositide 3-kinase (PI 3-kinase).
18728220	4	50	theme	hepatic	505:511	arg1	signaling					517:525	hepatic Akt signaling	505:525	hepatic Akt signaling at physiological concentrations of glucose	505:568	Here we investigated the effect of O-GlcNAc on hepatic Akt signaling at physiological concentrations of glucose.
18728220	10	51	theme	increased	1432:1440	arg1	phosphorylation					1442:1456	increased phosphorylation	1432:1456	increased phosphorylation of downstream targets	1432:1478	Further demonstrating Akt regulation by O-GlcNAc, we found that overexpression of O-GlcNAcase in the livers of euglycemic mice also significantly increased Akt activity, resulting in increased phosphorylation of downstream targets and decreased mRNA for glucose-6-phosphatase.
18728220	5	52	theme	Akt	695:697	arg1	activity					699:706	Akt activity	695:706	Akt activity	695:706	In HepG2 cells cultured in 5 mM glucose, removal of O-GlcNAc by adenoviral-mediated overexpression of O-GlcNAcase increased Akt activity and phosphorylation.
18728220	2	53	theme	Numerous	221:228	arg1	studies					230:236	Numerous studies	221:236	Numerous studies	221:236	Numerous studies have demonstrated that, in hyperglycemic conditions, excessive glucose flux through this pathway contributes to the development of insulin resistance.
18728220	8	54	theme	increased	948:956	arg1	activity					962:969	The increased Akt activity	944:969	The increased Akt activity	944:969	The increased Akt activity was accompanied by increased phosphorylation of Akt substrates and reduced mRNA for glucose-6-phosphatase and phosphoenolpyruvate carboxykinase (PEPCK).
18728220	8	55	theme	phosphoenolpyruvate	1081:1099	arg1	carboxykinase					1101:1113	phosphoenolpyruvate carboxykinase	1081:1113	phosphoenolpyruvate carboxykinase (PEPCK)	1081:1121	The increased Akt activity was accompanied by increased phosphorylation of Akt substrates and reduced mRNA for glucose-6-phosphatase and phosphoenolpyruvate carboxykinase (PEPCK).
18728220	8	55	theme	phosphoenolpyruvate	1081:1099	arg1	PEPCK					1116:1120	PEPCK	1116:1120	PEPCK	1116:1120	The increased Akt activity was accompanied by increased phosphorylation of Akt substrates and reduced mRNA for glucose-6-phosphatase and phosphoenolpyruvate carboxykinase (PEPCK).
18728220	4	56	theme	physiological	530:542	arg1	concentrations					544:557	physiological concentrations	530:557	physiological concentrations of glucose	530:568	Here we investigated the effect of O-GlcNAc on hepatic Akt signaling at physiological concentrations of glucose.
18728220	8	57	theme	substrates	1023:1032	arg1	phosphorylation					1000:1014	increased phosphorylation	990:1014	increased phosphorylation of Akt substrates	990:1032	The increased Akt activity was accompanied by increased phosphorylation of Akt substrates and reduced mRNA for glucose-6-phosphatase and phosphoenolpyruvate carboxykinase (PEPCK).
18728220	8	57	theme	substrates	1023:1032	arg1	mRNA					1046:1049	reduced mRNA	1038:1049	reduced mRNA for glucose-6-phosphatase and phosphoenolpyruvate carboxykinase (PEPCK)	1038:1121	The increased Akt activity was accompanied by increased phosphorylation of Akt substrates and reduced mRNA for glucose-6-phosphatase and phosphoenolpyruvate carboxykinase (PEPCK).
18728220	2	58	theme	hyperglycemic	265:277	arg1	conditions					279:288	hyperglycemic conditions	265:288	hyperglycemic conditions	265:288	Numerous studies have demonstrated that, in hyperglycemic conditions, excessive glucose flux through this pathway contributes to the development of insulin resistance.
18728220	9	59	theme	activation	1171:1180	arg1	activity					1142:1149	The increased Akt activity	1124:1149	The increased Akt activity	1124:1149	The increased Akt activity was not a result of activation of its upstream activator phosphoinositide 3-kinase (PI 3-kinase).
18728220	9	59	theme	activation	1171:1180	arg1	result					1161:1166	a result	1159:1166	a result of activation of its upstream activator phosphoinositide 3-kinase (PI 3-kinase)	1159:1246	The increased Akt activity was not a result of activation of its upstream activator phosphoinositide 3-kinase (PI 3-kinase).
18728220	1	60	theme	posttranslational	111:127	arg1	modification					129:140	the posttranslational modification	107:140	the posttranslational modification of nuclear and cytoplasmic protein	107:175	The hexosamine biosynthesis pathway (HBP) regulates the posttranslational modification of nuclear and cytoplasmic protein by O-linked N-acetylglucosamine (O-GlcNAc).
18728220	7	61	theme	sWGA	925:928	arg1	precipitates					930:941	sWGA precipitates	925:941	sWGA precipitates	925:941	Overexpression of O-GlcNAcase in HepG2 cells reduced the levels of Akt in sWGA precipitates.
18728220	7	62	from	levels	908:913	arg1	precipitates					930:941	sWGA precipitates	925:941	sWGA precipitates	925:941	Overexpression of O-GlcNAcase in HepG2 cells reduced the levels of Akt in sWGA precipitates.
18728220	1	63	theme	nuclear	145:151	arg1	protein					169:175	nuclear and cytoplasmic protein	145:175	nuclear and cytoplasmic protein	145:175	The hexosamine biosynthesis pathway (HBP) regulates the posttranslational modification of nuclear and cytoplasmic protein by O-linked N-acetylglucosamine (O-GlcNAc).
18728220	10	64	theme	Akt	1271:1273	arg1	regulation					1275:1284	Akt regulation	1271:1284	Akt regulation	1271:1284	Further demonstrating Akt regulation by O-GlcNAc, we found that overexpression of O-GlcNAcase in the livers of euglycemic mice also significantly increased Akt activity, resulting in increased phosphorylation of downstream targets and decreased mRNA for glucose-6-phosphatase.
18728220	10	65	theme	euglycemic	1360:1369	arg1	mice					1371:1374	euglycemic mice	1360:1374	euglycemic mice	1360:1374	Further demonstrating Akt regulation by O-GlcNAc, we found that overexpression of O-GlcNAcase in the livers of euglycemic mice also significantly increased Akt activity, resulting in increased phosphorylation of downstream targets and decreased mRNA for glucose-6-phosphatase.
18728220	8	66	theme	Akt	958:960	arg1	activity					962:969	The increased Akt activity	944:969	The increased Akt activity	944:969	The increased Akt activity was accompanied by increased phosphorylation of Akt substrates and reduced mRNA for glucose-6-phosphatase and phosphoenolpyruvate carboxykinase (PEPCK).
18728220	7	67	theme	Akt	918:920	arg1	levels					908:913	the levels	904:913	the levels of Akt in sWGA precipitates	904:941	Overexpression of O-GlcNAcase in HepG2 cells reduced the levels of Akt in sWGA precipitates.
18728220	9	68	theme	upstream	1189:1196	arg1	3-kinase					1225:1232	its upstream activator phosphoinositide 3-kinase	1185:1232	its upstream activator phosphoinositide 3-kinase (PI 3-kinase)	1185:1246	The increased Akt activity was not a result of activation of its upstream activator phosphoinositide 3-kinase (PI 3-kinase).
18728220	9	68	theme	upstream	1189:1196	arg1	3-kinase					1238:1245	PI 3-kinase	1235:1245	PI 3-kinase	1235:1245	The increased Akt activity was not a result of activation of its upstream activator phosphoinositide 3-kinase (PI 3-kinase).
18728220	2	69	theme	resistance	377:386	arg1	development					354:364	the development	350:364	the development of insulin resistance	350:386	Numerous studies have demonstrated that, in hyperglycemic conditions, excessive glucose flux through this pathway contributes to the development of insulin resistance.
16684529	0	0	theme	insulin-like	80:91	arg1	factor-1					100:107	insulin-like growth factor-1	80:107	insulin-like growth factor-1	80:107	Akt1 is dynamically modified with O-GlcNAc following treatments with PUGNAc and insulin-like growth factor-1.
16684529	1	1	theme	growth	150:155	arg1	factors					157:163	growth factors	150:163	growth factors subsequent to its phosphorylation on Thr308 and Ser473	150:218	The Ser/Thr kinase Akt1 is activated by growth factors subsequent to its phosphorylation on Thr308 and Ser473.
16684529	4	2	theme	O-GlcNAc-Akt1	595:607	arg1	levels					609:614	O-GlcNAc-Akt1 levels	595:614	O-GlcNAc-Akt1 levels	595:614	Treatment of cells with insulin-like growth factor-1 (IGF-1) also increased O-GlcNAc-Akt1 levels and increased Akt1 phosphorylation.
16684529	4	3	theme	cells	532:536	arg1	Treatment					519:527	Treatment	519:527	Treatment of cells with insulin-like growth factor-1 (IGF-1)	519:578	Treatment of cells with insulin-like growth factor-1 (IGF-1) also increased O-GlcNAc-Akt1 levels and increased Akt1 phosphorylation.
16684529	5	4	theme	induced	693:699	arg1	phosphorylation					706:720	IGF-1 induced Akt1 phosphorylation	687:720	IGF-1 induced Akt1 phosphorylation	687:720	PUGNAc treatment did not attenuate IGF-1 induced Akt1 phosphorylation.
16684529	3	5	theme	2-acetamido-2-deoxy-D-glucopyranosylidene	337:377	arg1	PUGNAc					404:409	PUGNAc	404:409	PUGNAc	404:409	Treatment of SH-SY5Y cells with O(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), which inhibits the enzymatic removal of O-GlcNAc from proteins, increased cytosolic O-GlcNAc-Akt1 levels.
16684529	3	5	theme	2-acetamido-2-deoxy-D-glucopyranosylidene	337:377	arg1	amino-N-phenylcarbamate					379:401	O(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate	335:401	O(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc)	335:410	Treatment of SH-SY5Y cells with O(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), which inhibits the enzymatic removal of O-GlcNAc from proteins, increased cytosolic O-GlcNAc-Akt1 levels.
16684529	5	6	theme	Akt1	701:704	arg1	phosphorylation					706:720	IGF-1 induced Akt1 phosphorylation	687:720	IGF-1 induced Akt1 phosphorylation	687:720	PUGNAc treatment did not attenuate IGF-1 induced Akt1 phosphorylation.
16684529	3	7	theme	O-GlcNAc-Akt1	497:509	arg1	levels					511:516	cytosolic O-GlcNAc-Akt1 levels	487:516	cytosolic O-GlcNAc-Akt1 levels	487:516	Treatment of SH-SY5Y cells with O(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), which inhibits the enzymatic removal of O-GlcNAc from proteins, increased cytosolic O-GlcNAc-Akt1 levels.
16684529	5	8	theme	PUGNAc	652:657	arg1	treatment					659:667	PUGNAc treatment	652:667	PUGNAc treatment	652:667	PUGNAc treatment did not attenuate IGF-1 induced Akt1 phosphorylation.
16684529	1	9	theme	subsequent	165:174	arg1	factors					157:163	growth factors	150:163	growth factors subsequent to its phosphorylation on Thr308 and Ser473	150:218	The Ser/Thr kinase Akt1 is activated by growth factors subsequent to its phosphorylation on Thr308 and Ser473.
16684529	3	10	theme	O	335:335	arg1	PUGNAc					404:409	PUGNAc	404:409	PUGNAc	404:409	Treatment of SH-SY5Y cells with O(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), which inhibits the enzymatic removal of O-GlcNAc from proteins, increased cytosolic O-GlcNAc-Akt1 levels.
16684529	3	10	theme	O	335:335	arg1	amino-N-phenylcarbamate					379:401	O(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate	335:401	O(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc)	335:410	Treatment of SH-SY5Y cells with O(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), which inhibits the enzymatic removal of O-GlcNAc from proteins, increased cytosolic O-GlcNAc-Akt1 levels.
16684529	2	11	mod	modified	279:286	arg1	Akt1					243:246	Akt1	243:246	Akt1	243:246	In the present study, Akt1 was found to be constitutively modified with O-GlcNAc.
16684529	2	11	mod	modified	279:286	arg3	O-GlcNAc					293:300	O-GlcNAc	293:300	O-GlcNAc	293:300	In the present study, Akt1 was found to be constitutively modified with O-GlcNAc.
16684529	3	12	theme	enzymatic	432:440	arg1	removal					442:448	the enzymatic removal	428:448	the enzymatic removal of O-GlcNAc from proteins	428:474	Treatment of SH-SY5Y cells with O(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), which inhibits the enzymatic removal of O-GlcNAc from proteins, increased cytosolic O-GlcNAc-Akt1 levels.
16684529	6	13	mod	modified	778:785	arg3	O-GlcNAc					792:799	O-GlcNAc	792:799	O-GlcNAc	792:799	These results indicate that Akt1 can be simultaneously modified with O-GlcNAc and phosphorylated.
16684529	6	13	mod	modified	778:785	arg1	Akt1					751:754	Akt1	751:754	Akt1	751:754	These results indicate that Akt1 can be simultaneously modified with O-GlcNAc and phosphorylated.
16684529	6	13	mod	modified	778:785	arg3	phosphorylated					805:818	phosphorylated	805:818	phosphorylated	805:818	These results indicate that Akt1 can be simultaneously modified with O-GlcNAc and phosphorylated.
16684529	7	14	theme	Akt1	873:876	arg1	accumulation					857:868	the nuclear accumulation	845:868	the nuclear accumulation of Akt1	845:876	However, PUGNAc induced the nuclear accumulation of Akt1 suggesting that the O-GlcNAc-modification on Akt1 may play a role in Akt1 nuclear localization.
16684529	0	15	theme	O-GlcNAc	34:41	arg1	treatments					53:62	O-GlcNAc following treatments	34:62	O-GlcNAc following treatments with PUGNAc and insulin-like growth factor-1	34:107	Akt1 is dynamically modified with O-GlcNAc following treatments with PUGNAc and insulin-like growth factor-1.
16684529	7	16	theme	nuclear	849:855	arg1	accumulation					857:868	the nuclear accumulation	845:868	the nuclear accumulation of Akt1	845:876	However, PUGNAc induced the nuclear accumulation of Akt1 suggesting that the O-GlcNAc-modification on Akt1 may play a role in Akt1 nuclear localization.
16684529	2	17	theme	present	228:234	arg1	study					236:240	the present study	224:240	the present study	224:240	In the present study, Akt1 was found to be constitutively modified with O-GlcNAc.
16684529	3	18	theme	O-GlcNAc	453:460	arg1	removal					442:448	the enzymatic removal	428:448	the enzymatic removal of O-GlcNAc from proteins	428:474	Treatment of SH-SY5Y cells with O(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), which inhibits the enzymatic removal of O-GlcNAc from proteins, increased cytosolic O-GlcNAc-Akt1 levels.
16684529	4	19	theme	insulin-like	543:554	arg1	IGF-1					573:577	IGF-1	573:577	IGF-1	573:577	Treatment of cells with insulin-like growth factor-1 (IGF-1) also increased O-GlcNAc-Akt1 levels and increased Akt1 phosphorylation.
16684529	4	19	theme	insulin-like	543:554	arg1	factor-1					563:570	insulin-like growth factor-1	543:570	insulin-like growth factor-1 (IGF-1)	543:578	Treatment of cells with insulin-like growth factor-1 (IGF-1) also increased O-GlcNAc-Akt1 levels and increased Akt1 phosphorylation.
16684529	0	20	mod	modified	20:27	arg3	treatments					53:62	O-GlcNAc following treatments	34:62	O-GlcNAc following treatments with PUGNAc and insulin-like growth factor-1	34:107	Akt1 is dynamically modified with O-GlcNAc following treatments with PUGNAc and insulin-like growth factor-1.
16684529	0	20	mod	modified	20:27	arg1	Akt1					0:3	Akt1	0:3	Akt1	0:3	Akt1 is dynamically modified with O-GlcNAc following treatments with PUGNAc and insulin-like growth factor-1.
16684529	1	21	theme	Ser/Thr	114:120	arg1	Akt1					129:132	The Ser/Thr kinase Akt1	110:132	The Ser/Thr kinase Akt1	110:132	The Ser/Thr kinase Akt1 is activated by growth factors subsequent to its phosphorylation on Thr308 and Ser473.
16684529	0	22	theme	following	43:51	arg1	treatments					53:62	O-GlcNAc following treatments	34:62	O-GlcNAc following treatments with PUGNAc and insulin-like growth factor-1	34:107	Akt1 is dynamically modified with O-GlcNAc following treatments with PUGNAc and insulin-like growth factor-1.
16684529	2	23	located	found	252:256	arg2	Akt1					243:246	Akt1	243:246	Akt1	243:246	In the present study, Akt1 was found to be constitutively modified with O-GlcNAc.
16684529	2	23	located	found	252:256	arg1	study					236:240	the present study	224:240	the present study	224:240	In the present study, Akt1 was found to be constitutively modified with O-GlcNAc.
16684529	3	24	from	proteins	467:474	arg1	removal					442:448	the enzymatic removal	428:448	the enzymatic removal of O-GlcNAc from proteins	428:474	Treatment of SH-SY5Y cells with O(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), which inhibits the enzymatic removal of O-GlcNAc from proteins, increased cytosolic O-GlcNAc-Akt1 levels.
16684529	1	25	theme	kinase	122:127	arg1	Akt1					129:132	The Ser/Thr kinase Akt1	110:132	The Ser/Thr kinase Akt1	110:132	The Ser/Thr kinase Akt1 is activated by growth factors subsequent to its phosphorylation on Thr308 and Ser473.
16684529	4	26	theme	growth	556:561	arg1	IGF-1					573:577	IGF-1	573:577	IGF-1	573:577	Treatment of cells with insulin-like growth factor-1 (IGF-1) also increased O-GlcNAc-Akt1 levels and increased Akt1 phosphorylation.
16684529	4	26	theme	growth	556:561	arg1	factor-1					563:570	insulin-like growth factor-1	543:570	insulin-like growth factor-1 (IGF-1)	543:578	Treatment of cells with insulin-like growth factor-1 (IGF-1) also increased O-GlcNAc-Akt1 levels and increased Akt1 phosphorylation.
16684529	7	27	from	O-GlcNAc-modification	898:918	arg1	Akt1					923:926	Akt1	923:926	Akt1	923:926	However, PUGNAc induced the nuclear accumulation of Akt1 suggesting that the O-GlcNAc-modification on Akt1 may play a role in Akt1 nuclear localization.
16684529	3	28	with	Treatment	303:311	arg1	PUGNAc					404:409	PUGNAc	404:409	PUGNAc	404:409	Treatment of SH-SY5Y cells with O(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), which inhibits the enzymatic removal of O-GlcNAc from proteins, increased cytosolic O-GlcNAc-Akt1 levels.
16684529	3	28	with	Treatment	303:311	arg1	amino-N-phenylcarbamate					379:401	O(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate	335:401	O(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc)	335:410	Treatment of SH-SY5Y cells with O(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), which inhibits the enzymatic removal of O-GlcNAc from proteins, increased cytosolic O-GlcNAc-Akt1 levels.
16684529	4	29	with	Treatment	519:527	arg1	IGF-1					573:577	IGF-1	573:577	IGF-1	573:577	Treatment of cells with insulin-like growth factor-1 (IGF-1) also increased O-GlcNAc-Akt1 levels and increased Akt1 phosphorylation.
16684529	4	29	with	Treatment	519:527	arg1	factor-1					563:570	insulin-like growth factor-1	543:570	insulin-like growth factor-1 (IGF-1)	543:578	Treatment of cells with insulin-like growth factor-1 (IGF-1) also increased O-GlcNAc-Akt1 levels and increased Akt1 phosphorylation.
16684529	4	30	theme	Akt1	630:633	arg1	phosphorylation					635:649	Akt1 phosphorylation	630:649	Akt1 phosphorylation	630:649	Treatment of cells with insulin-like growth factor-1 (IGF-1) also increased O-GlcNAc-Akt1 levels and increased Akt1 phosphorylation.
16684529	0	31	with	treatments	53:62	arg1	factor-1					100:107	insulin-like growth factor-1	80:107	insulin-like growth factor-1	80:107	Akt1 is dynamically modified with O-GlcNAc following treatments with PUGNAc and insulin-like growth factor-1.
16684529	0	31	with	treatments	53:62	arg1	PUGNAc					69:74	PUGNAc	69:74	PUGNAc	69:74	Akt1 is dynamically modified with O-GlcNAc following treatments with PUGNAc and insulin-like growth factor-1.
16684529	3	32	theme	cytosolic	487:495	arg1	levels					511:516	cytosolic O-GlcNAc-Akt1 levels	487:516	cytosolic O-GlcNAc-Akt1 levels	487:516	Treatment of SH-SY5Y cells with O(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), which inhibits the enzymatic removal of O-GlcNAc from proteins, increased cytosolic O-GlcNAc-Akt1 levels.
16684529	7	33	theme	Akt1	947:950	arg1	localization					960:971	Akt1 nuclear localization	947:971	Akt1 nuclear localization	947:971	However, PUGNAc induced the nuclear accumulation of Akt1 suggesting that the O-GlcNAc-modification on Akt1 may play a role in Akt1 nuclear localization.
16684529	3	34	theme	SH-SY5Y	316:322	arg1	cells					324:328	SH-SY5Y cells	316:328	SH-SY5Y cells	316:328	Treatment of SH-SY5Y cells with O(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), which inhibits the enzymatic removal of O-GlcNAc from proteins, increased cytosolic O-GlcNAc-Akt1 levels.
16684529	1	35	from	phosphorylation	183:197	arg1	Thr308					202:207	Thr308	202:207	Thr308	202:207	The Ser/Thr kinase Akt1 is activated by growth factors subsequent to its phosphorylation on Thr308 and Ser473.
16684529	1	35	from	phosphorylation	183:197	arg1	Ser473					213:218	Ser473	213:218	Ser473	213:218	The Ser/Thr kinase Akt1 is activated by growth factors subsequent to its phosphorylation on Thr308 and Ser473.
16684529	7	36	theme	nuclear	952:958	arg1	localization					960:971	Akt1 nuclear localization	947:971	Akt1 nuclear localization	947:971	However, PUGNAc induced the nuclear accumulation of Akt1 suggesting that the O-GlcNAc-modification on Akt1 may play a role in Akt1 nuclear localization.
16684529	3	37	theme	cells	324:328	arg1	Treatment					303:311	Treatment	303:311	Treatment	303:311	Treatment of SH-SY5Y cells with O(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate (PUGNAc), which inhibits the enzymatic removal of O-GlcNAc from proteins, increased cytosolic O-GlcNAc-Akt1 levels.
16684529	0	38	theme	growth	93:98	arg1	factor-1					100:107	insulin-like growth factor-1	80:107	insulin-like growth factor-1	80:107	Akt1 is dynamically modified with O-GlcNAc following treatments with PUGNAc and insulin-like growth factor-1.
30069701	0	0	theme	MCM-MCM	87:93	arg1	interactions					95:106	MCM-MCM interactions	87:106	MCM-MCM interactions	87:106	O-GlcNAc transferase associates with the MCM2-7 complex and its silencing destabilizes MCM-MCM interactions.
30069701	9	1	theme	MCM/MCM	1284:1290	arg1	interactions					1292:1303	MCM/MCM interactions	1284:1303	MCM/MCM interactions	1284:1303	In conclusion, OGT is a new partner of the MCM2-7 complex and O-GlcNAcylation homeostasis might regulate MCM2-7 complex by regulating the chromatin loading of MCM6 and MCM7 and stabilizing MCM/MCM interactions.
30069701	6	2	theme	several	812:818	arg1	subunits					824:831	several MCM subunits	812:831	several MCM subunits	812:831	Moreover, we identify stable interaction between OGT and several MCM subunits.
30069701	8	3	theme	MCM2/6	1028:1033	arg1	interactions					1046:1057	MCM2/6 and MCM4/7 interactions	1028:1057	MCM2/6 and MCM4/7 interactions	1028:1057	Finally, OGT silencing or OGA inhibition destabilizes MCM2/6 and MCM4/7 interactions in the chromatin-enriched fraction.
30069701	7	4	theme	MCM7	925:928	arg1	binding					899:905	the chromatin binding	885:905	the chromatin binding of MCM2, MCM6 and MCM7	885:928	We also show that down-regulation of OGT decreases the chromatin binding of MCM2, MCM6 and MCM7 without affecting their steady-state level.
30069701	7	5	theme	steady-state	954:965	arg1	level					967:971	their steady-state level	948:971	their steady-state level	948:971	We also show that down-regulation of OGT decreases the chromatin binding of MCM2, MCM6 and MCM7 without affecting their steady-state level.
30069701	7	6	theme	OGT	871:873	arg1	down-regulation					852:866	down-regulation	852:866	down-regulation of OGT	852:873	We also show that down-regulation of OGT decreases the chromatin binding of MCM2, MCM6 and MCM7 without affecting their steady-state level.
30069701	4	7	theme	MCM2-7	470:475	arg1	complex					477:483	the MCM2-7 complex	466:483	the MCM2-7 complex which is crucial for the initiation of DNA replication through its DNA helicase activity	466:572	These proteins belong to the MCM2-7 complex which is crucial for the initiation of DNA replication through its DNA helicase activity.
30069701	4	7	theme	MCM2-7	470:475	arg1	crucial					494:500	crucial	494:500	crucial	494:500	These proteins belong to the MCM2-7 complex which is crucial for the initiation of DNA replication through its DNA helicase activity.
30069701	3	8	dep	proteins	405:412	arg1	MCM7					435:438	MCM7	435:438	MCM7	435:438	We previously reported the O-GlcNAcylation of the minichromosome maintenance proteins MCM2, MCM3, MCM6 and MCM7.
30069701	3	8	dep	proteins	405:412	arg1	MCM6					426:429	MCM6	426:429	MCM6	426:429	We previously reported the O-GlcNAcylation of the minichromosome maintenance proteins MCM2, MCM3, MCM6 and MCM7.
30069701	3	8	dep	proteins	405:412	arg1	proteins					405:412	minichromosome maintenance proteins	378:412	the minichromosome maintenance proteins MCM2, MCM3, MCM6 and MCM7	374:438	We previously reported the O-GlcNAcylation of the minichromosome maintenance proteins MCM2, MCM3, MCM6 and MCM7.
30069701	3	8	dep	proteins	405:412	arg1	MCM3					420:423	MCM3	420:423	MCM3	420:423	We previously reported the O-GlcNAcylation of the minichromosome maintenance proteins MCM2, MCM3, MCM6 and MCM7.
30069701	3	8	dep	proteins	405:412	arg1	MCM2					414:417	MCM2	414:417	MCM2	414:417	We previously reported the O-GlcNAcylation of the minichromosome maintenance proteins MCM2, MCM3, MCM6 and MCM7.
30069701	0	9	theme	O-GlcNAc	0:7	arg1	transferase					9:19	O-GlcNAc transferase	0:19	O-GlcNAc transferase	0:19	O-GlcNAc transferase associates with the MCM2-7 complex and its silencing destabilizes MCM-MCM interactions.
30069701	5	10	theme	synchronized	729:740	arg1	cells					748:752	synchronized human cells	729:752	synchronized human cells	729:752	Here we show that the six subunits of MCM2-7 are O-GlcNAcylated and that O-GlcNAcylation of MCM proteins mainly occurs in the chromatin-bound fraction of synchronized human cells.
30069701	8	11	theme	OGT	983:985	arg1	silencing					987:995	OGT silencing	983:995	OGT silencing	983:995	Finally, OGT silencing or OGA inhibition destabilizes MCM2/6 and MCM4/7 interactions in the chromatin-enriched fraction.
30069701	5	12	theme	human	742:746	arg1	cells					748:752	synchronized human cells	729:752	synchronized human cells	729:752	Here we show that the six subunits of MCM2-7 are O-GlcNAcylated and that O-GlcNAcylation of MCM proteins mainly occurs in the chromatin-bound fraction of synchronized human cells.
30069701	8	13	theme	MCM4/7	1039:1044	arg1	interactions					1046:1057	MCM2/6 and MCM4/7 interactions	1028:1057	MCM2/6 and MCM4/7 interactions	1028:1057	Finally, OGT silencing or OGA inhibition destabilizes MCM2/6 and MCM4/7 interactions in the chromatin-enriched fraction.
30069701	9	14	theme	MCM2-7	1200:1205	arg1	complex					1207:1213	MCM2-7 complex	1200:1213	MCM2-7 complex	1200:1213	In conclusion, OGT is a new partner of the MCM2-7 complex and O-GlcNAcylation homeostasis might regulate MCM2-7 complex by regulating the chromatin loading of MCM6 and MCM7 and stabilizing MCM/MCM interactions.
30069701	2	15	theme	cycle	263:267	arg1	progression					269:279	cell cycle progression	258:279	cell cycle progression	258:279	The homeostasis of O-GlcNAc cycling is regulated during cell cycle progression and is essential for proper cellular division.
30069701	3	16	theme	maintenance	393:403	arg1	MCM7					435:438	MCM7	435:438	MCM7	435:438	We previously reported the O-GlcNAcylation of the minichromosome maintenance proteins MCM2, MCM3, MCM6 and MCM7.
30069701	3	16	theme	maintenance	393:403	arg1	MCM6					426:429	MCM6	426:429	MCM6	426:429	We previously reported the O-GlcNAcylation of the minichromosome maintenance proteins MCM2, MCM3, MCM6 and MCM7.
30069701	3	16	theme	maintenance	393:403	arg1	proteins					405:412	minichromosome maintenance proteins	378:412	the minichromosome maintenance proteins MCM2, MCM3, MCM6 and MCM7	374:438	We previously reported the O-GlcNAcylation of the minichromosome maintenance proteins MCM2, MCM3, MCM6 and MCM7.
30069701	3	16	theme	maintenance	393:403	arg1	MCM3					420:423	MCM3	420:423	MCM3	420:423	We previously reported the O-GlcNAcylation of the minichromosome maintenance proteins MCM2, MCM3, MCM6 and MCM7.
30069701	3	16	theme	maintenance	393:403	arg1	MCM2					414:417	MCM2	414:417	MCM2	414:417	We previously reported the O-GlcNAcylation of the minichromosome maintenance proteins MCM2, MCM3, MCM6 and MCM7.
30069701	5	17	theme	MCM2-7	613:618	arg1	subunits					601:608	the six subunits	593:608	the six subunits of MCM2-7	593:618	Here we show that the six subunits of MCM2-7 are O-GlcNAcylated and that O-GlcNAcylation of MCM proteins mainly occurs in the chromatin-bound fraction of synchronized human cells.
30069701	5	17	theme	MCM2-7	613:618	arg1	O-GlcNAcylated					624:637	O-GlcNAcylated	624:637	O-GlcNAcylated	624:637	Here we show that the six subunits of MCM2-7 are O-GlcNAcylated and that O-GlcNAcylation of MCM proteins mainly occurs in the chromatin-bound fraction of synchronized human cells.
30069701	6	18	theme	stable	777:782	arg1	interaction					784:794	stable interaction	777:794	stable interaction between OGT and several MCM subunits	777:831	Moreover, we identify stable interaction between OGT and several MCM subunits.
30069701	2	19	theme	cellular	309:316	arg1	division					318:325	proper cellular division	302:325	proper cellular division	302:325	The homeostasis of O-GlcNAc cycling is regulated during cell cycle progression and is essential for proper cellular division.
30069701	3	20	theme	proteins	405:412	arg1	O-GlcNAcylation					355:369	the O-GlcNAcylation	351:369	the O-GlcNAcylation of the minichromosome maintenance proteins MCM2, MCM3, MCM6 and MCM7	351:438	We previously reported the O-GlcNAcylation of the minichromosome maintenance proteins MCM2, MCM3, MCM6 and MCM7.
30069701	8	21	theme	OGA	1000:1002	arg1	inhibition					1004:1013	OGA inhibition	1000:1013	OGA inhibition	1000:1013	Finally, OGT silencing or OGA inhibition destabilizes MCM2/6 and MCM4/7 interactions in the chromatin-enriched fraction.
30069701	2	22	theme	proper	302:307	arg1	division					318:325	proper cellular division	302:325	proper cellular division	302:325	The homeostasis of O-GlcNAc cycling is regulated during cell cycle progression and is essential for proper cellular division.
30069701	7	23	theme	MCM6	916:919	arg1	binding					899:905	the chromatin binding	885:905	the chromatin binding of MCM2, MCM6 and MCM7	885:928	We also show that down-regulation of OGT decreases the chromatin binding of MCM2, MCM6 and MCM7 without affecting their steady-state level.
30069701	9	24	theme	O-GlcNAcylation	1157:1171	arg1	homeostasis					1173:1183	O-GlcNAcylation homeostasis	1157:1183	O-GlcNAcylation homeostasis	1157:1183	In conclusion, OGT is a new partner of the MCM2-7 complex and O-GlcNAcylation homeostasis might regulate MCM2-7 complex by regulating the chromatin loading of MCM6 and MCM7 and stabilizing MCM/MCM interactions.
30069701	9	25	from	partner	1123:1129	arg1	conclusion					1098:1107	conclusion	1098:1107	conclusion	1098:1107	In conclusion, OGT is a new partner of the MCM2-7 complex and O-GlcNAcylation homeostasis might regulate MCM2-7 complex by regulating the chromatin loading of MCM6 and MCM7 and stabilizing MCM/MCM interactions.
30069701	3	26	theme	minichromosome	378:391	arg1	MCM7					435:438	MCM7	435:438	MCM7	435:438	We previously reported the O-GlcNAcylation of the minichromosome maintenance proteins MCM2, MCM3, MCM6 and MCM7.
30069701	3	26	theme	minichromosome	378:391	arg1	MCM6					426:429	MCM6	426:429	MCM6	426:429	We previously reported the O-GlcNAcylation of the minichromosome maintenance proteins MCM2, MCM3, MCM6 and MCM7.
30069701	3	26	theme	minichromosome	378:391	arg1	proteins					405:412	minichromosome maintenance proteins	378:412	the minichromosome maintenance proteins MCM2, MCM3, MCM6 and MCM7	374:438	We previously reported the O-GlcNAcylation of the minichromosome maintenance proteins MCM2, MCM3, MCM6 and MCM7.
30069701	3	26	theme	minichromosome	378:391	arg1	MCM3					420:423	MCM3	420:423	MCM3	420:423	We previously reported the O-GlcNAcylation of the minichromosome maintenance proteins MCM2, MCM3, MCM6 and MCM7.
30069701	3	26	theme	minichromosome	378:391	arg1	MCM2					414:417	MCM2	414:417	MCM2	414:417	We previously reported the O-GlcNAcylation of the minichromosome maintenance proteins MCM2, MCM3, MCM6 and MCM7.
30069701	4	27	theme	helicase	556:563	arg1	activity					565:572	its DNA helicase activity	548:572	its DNA helicase activity	548:572	These proteins belong to the MCM2-7 complex which is crucial for the initiation of DNA replication through its DNA helicase activity.
30069701	8	28	theme	chromatin-enriched	1066:1083	arg1	fraction					1085:1092	the chromatin-enriched fraction	1062:1092	the chromatin-enriched fraction	1062:1092	Finally, OGT silencing or OGA inhibition destabilizes MCM2/6 and MCM4/7 interactions in the chromatin-enriched fraction.
30069701	0	29	theme	MCM2-7	41:46	arg1	complex					48:54	the MCM2-7 complex	37:54	the MCM2-7 complex	37:54	O-GlcNAc transferase associates with the MCM2-7 complex and its silencing destabilizes MCM-MCM interactions.
30069701	4	30	theme	DNA	552:554	arg1	activity					565:572	its DNA helicase activity	548:572	its DNA helicase activity	548:572	These proteins belong to the MCM2-7 complex which is crucial for the initiation of DNA replication through its DNA helicase activity.
30069701	9	31	theme	chromatin	1233:1241	arg1	loading					1243:1249	the chromatin loading	1229:1249	the chromatin loading of MCM6 and MCM7	1229:1266	In conclusion, OGT is a new partner of the MCM2-7 complex and O-GlcNAcylation homeostasis might regulate MCM2-7 complex by regulating the chromatin loading of MCM6 and MCM7 and stabilizing MCM/MCM interactions.
30069701	2	32	theme	cycling	230:236	arg1	homeostasis					206:216	The homeostasis	202:216	The homeostasis of O-GlcNAc cycling	202:236	The homeostasis of O-GlcNAc cycling is regulated during cell cycle progression and is essential for proper cellular division.
30069701	2	32	theme	cycling	230:236	arg1	essential					288:296	essential	288:296	essential	288:296	The homeostasis of O-GlcNAc cycling is regulated during cell cycle progression and is essential for proper cellular division.
30069701	5	33	theme	chromatin-bound	701:715	arg1	fraction					717:724	the chromatin-bound fraction	697:724	the chromatin-bound fraction of synchronized human cells	697:752	Here we show that the six subunits of MCM2-7 are O-GlcNAcylated and that O-GlcNAcylation of MCM proteins mainly occurs in the chromatin-bound fraction of synchronized human cells.
30069701	2	34	theme	O-GlcNAc	221:228	arg1	cycling					230:236	O-GlcNAc cycling	221:236	O-GlcNAc cycling	221:236	The homeostasis of O-GlcNAc cycling is regulated during cell cycle progression and is essential for proper cellular division.
30069701	9	35	theme	new	1119:1121	arg1	partner					1123:1129	a new partner	1117:1129	a new partner of the MCM2-7 complex	1117:1151	In conclusion, OGT is a new partner of the MCM2-7 complex and O-GlcNAcylation homeostasis might regulate MCM2-7 complex by regulating the chromatin loading of MCM6 and MCM7 and stabilizing MCM/MCM interactions.
30069701	9	35	theme	new	1119:1121	arg1	OGT					1110:1112	OGT	1110:1112	OGT	1110:1112	In conclusion, OGT is a new partner of the MCM2-7 complex and O-GlcNAcylation homeostasis might regulate MCM2-7 complex by regulating the chromatin loading of MCM6 and MCM7 and stabilizing MCM/MCM interactions.
30069701	1	36	theme	proteins	128:135	arg1	O-GlcNAcylation					109:123	O-GlcNAcylation	109:123	O-GlcNAcylation of proteins	109:135	O-GlcNAcylation of proteins is governed by O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA).
30069701	4	37	theme	replication	528:538	arg1	initiation					510:519	the initiation	506:519	the initiation of DNA replication through its DNA helicase activity	506:572	These proteins belong to the MCM2-7 complex which is crucial for the initiation of DNA replication through its DNA helicase activity.
30069701	5	38	theme	MCM	667:669	arg1	proteins					671:678	MCM proteins	667:678	MCM proteins	667:678	Here we show that the six subunits of MCM2-7 are O-GlcNAcylated and that O-GlcNAcylation of MCM proteins mainly occurs in the chromatin-bound fraction of synchronized human cells.
30069701	9	39	theme	MCM6	1254:1257	arg1	loading					1243:1249	the chromatin loading	1229:1249	the chromatin loading of MCM6 and MCM7	1229:1266	In conclusion, OGT is a new partner of the MCM2-7 complex and O-GlcNAcylation homeostasis might regulate MCM2-7 complex by regulating the chromatin loading of MCM6 and MCM7 and stabilizing MCM/MCM interactions.
30069701	4	40	theme	DNA	524:526	arg1	replication					528:538	DNA replication	524:538	DNA replication	524:538	These proteins belong to the MCM2-7 complex which is crucial for the initiation of DNA replication through its DNA helicase activity.
30069701	5	41	theme	proteins	671:678	arg1	O-GlcNAcylation					648:662	O-GlcNAcylation	648:662	O-GlcNAcylation of MCM proteins	648:678	Here we show that the six subunits of MCM2-7 are O-GlcNAcylated and that O-GlcNAcylation of MCM proteins mainly occurs in the chromatin-bound fraction of synchronized human cells.
30069701	2	42	theme	cell	258:261	arg1	progression					269:279	cell cycle progression	258:279	cell cycle progression	258:279	The homeostasis of O-GlcNAc cycling is regulated during cell cycle progression and is essential for proper cellular division.
30069701	7	43	theme	MCM2	910:913	arg1	binding					899:905	the chromatin binding	885:905	the chromatin binding of MCM2, MCM6 and MCM7	885:928	We also show that down-regulation of OGT decreases the chromatin binding of MCM2, MCM6 and MCM7 without affecting their steady-state level.
30069701	9	44	theme	MCM7	1263:1266	arg1	loading					1243:1249	the chromatin loading	1229:1249	the chromatin loading of MCM6 and MCM7	1229:1266	In conclusion, OGT is a new partner of the MCM2-7 complex and O-GlcNAcylation homeostasis might regulate MCM2-7 complex by regulating the chromatin loading of MCM6 and MCM7 and stabilizing MCM/MCM interactions.
30069701	7	45	theme	chromatin	889:897	arg1	binding					899:905	the chromatin binding	885:905	the chromatin binding of MCM2, MCM6 and MCM7	885:928	We also show that down-regulation of OGT decreases the chromatin binding of MCM2, MCM6 and MCM7 without affecting their steady-state level.
30069701	5	46	theme	cells	748:752	arg1	fraction					717:724	the chromatin-bound fraction	697:724	the chromatin-bound fraction of synchronized human cells	697:752	Here we show that the six subunits of MCM2-7 are O-GlcNAcylated and that O-GlcNAcylation of MCM proteins mainly occurs in the chromatin-bound fraction of synchronized human cells.
30069701	6	47	theme	MCM	820:822	arg1	subunits					824:831	several MCM subunits	812:831	several MCM subunits	812:831	Moreover, we identify stable interaction between OGT and several MCM subunits.
30069701	9	48	theme	MCM2-7	1138:1143	arg1	complex					1145:1151	the MCM2-7 complex	1134:1151	the MCM2-7 complex	1134:1151	In conclusion, OGT is a new partner of the MCM2-7 complex and O-GlcNAcylation homeostasis might regulate MCM2-7 complex by regulating the chromatin loading of MCM6 and MCM7 and stabilizing MCM/MCM interactions.
30069701	1	49	theme	O-GlcNAc	152:159	arg1	transferase					161:171	O-GlcNAc transferase	152:171	O-GlcNAc transferase (OGT)	152:177	O-GlcNAcylation of proteins is governed by O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA).
30069701	1	49	theme	O-GlcNAc	152:159	arg1	OGT					174:176	OGT	174:176	OGT	174:176	O-GlcNAcylation of proteins is governed by O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA).
30069701	9	50	theme	complex	1145:1151	arg1	partner					1123:1129	a new partner	1117:1129	a new partner of the MCM2-7 complex	1117:1151	In conclusion, OGT is a new partner of the MCM2-7 complex and O-GlcNAcylation homeostasis might regulate MCM2-7 complex by regulating the chromatin loading of MCM6 and MCM7 and stabilizing MCM/MCM interactions.
30069701	9	50	theme	complex	1145:1151	arg1	OGT					1110:1112	OGT	1110:1112	OGT	1110:1112	In conclusion, OGT is a new partner of the MCM2-7 complex and O-GlcNAcylation homeostasis might regulate MCM2-7 complex by regulating the chromatin loading of MCM6 and MCM7 and stabilizing MCM/MCM interactions.
12588874	3	0	theme	important	303:311	arg1	functions					313:321	important functions	303:321	important functions in DNA replication, protein synthesis, and cellular response to external stimuli	303:402	It regulates the expression of genes with important functions in DNA replication, protein synthesis, and cellular response to external stimuli during cell growth and differentiation.
12588874	4	1	theme	functions	483:491	arg1	variety					472:478	a variety	470:478	a variety of functions	470:491	How YY1 accomplishes such a variety of functions is unknown.
12588874	4	1	theme	functions	483:491	arg1	functions					483:491	functions	483:491	functions	483:491	How YY1 accomplishes such a variety of functions is unknown.
12588874	1	2	theme	wide	160:163	arg1	genes					195:199	cellular and viral genes	176:199	cellular and viral genes	176:199	YY1 is a zinc finger DNA-binding transcription factor that influences expression of a wide variety of cellular and viral genes.
12588874	1	2	theme	wide	160:163	arg1	variety					165:171	a wide variety	158:171	a wide variety of cellular and viral genes	158:199	YY1 is a zinc finger DNA-binding transcription factor that influences expression of a wide variety of cellular and viral genes.
12588874	9	3	theme	profound	1001:1008	arg1	effect					1010:1015	a profound effect	999:1015	a profound effect	999:1015	The ability of the O-glycosylation on YY1 to disrupt the complex with Rb leads us to propose that O-glycosylation might have a profound effect on cell cycle transitions that regulate the YY1-Rb heterodimerization and promote the activity of YY1.
12588874	10	4	theme	YY1-regulated	1166:1178	arg1	transcription					1180:1192	YY1-regulated transcription	1166:1192	YY1-regulated transcription	1166:1192	Our observations provide strong evidence that YY1-regulated transcription is very likely connected to the pathway of glucose metabolism that culminates in the O-GlcNAcylation on YY1, changing its function in transcription.
12588874	3	5	theme	protein	343:349	arg1	synthesis					351:359	protein synthesis	343:359	protein synthesis	343:359	It regulates the expression of genes with important functions in DNA replication, protein synthesis, and cellular response to external stimuli during cell growth and differentiation.
12588874	5	6	theme	cells	629:633	arg1	status					615:620	the differentiation status	595:620	the differentiation status of the cells	595:633	Here, we show that a subset of the nuclear YY1 appears to be O-GlcNAcylated regardless of the differentiation status of the cells.
12588874	8	7	theme	glycosylated	836:847	arg1	free					856:859	free	856:859	free	856:859	Upon dissociation from Rb, the glycosylated YY1 is free to bind DNA.
12588874	8	7	theme	glycosylated	836:847	arg1	YY1					849:851	the glycosylated YY1	832:851	the glycosylated YY1	832:851	Upon dissociation from Rb, the glycosylated YY1 is free to bind DNA.
12588874	6	8	link	O-linked	678:685	arg1	O-GlcNAcylation					714:728	O-GlcNAcylation	714:728	O-GlcNAcylation	714:728	We found that glucose strongly stimulates O-linked N-acetylglucosaminylation (O-GlcNAcylation) on YY1.
12588874	6	8	link	O-linked	678:685	arg1	N-acetylglucosaminylation					687:711	O-linked N-acetylglucosaminylation	678:711	O-linked N-acetylglucosaminylation (O-GlcNAcylation) on YY1	678:736	We found that glucose strongly stimulates O-linked N-acetylglucosaminylation (O-GlcNAcylation) on YY1.
12588874	9	9	theme	cell	1020:1023	arg1	transitions					1031:1041	cell cycle transitions	1020:1041	cell cycle transitions that regulate the YY1-Rb heterodimerization and promote the activity of YY1	1020:1117	The ability of the O-glycosylation on YY1 to disrupt the complex with Rb leads us to propose that O-glycosylation might have a profound effect on cell cycle transitions that regulate the YY1-Rb heterodimerization and promote the activity of YY1.
12588874	10	10	from	function	1316:1323	arg1	transcription					1328:1340	transcription	1328:1340	transcription	1328:1340	Our observations provide strong evidence that YY1-regulated transcription is very likely connected to the pathway of glucose metabolism that culminates in the O-GlcNAcylation on YY1, changing its function in transcription.
12588874	6	11	from	N-acetylglucosaminylation	687:711	arg1	YY1					734:736	YY1	734:736	YY1	734:736	We found that glucose strongly stimulates O-linked N-acetylglucosaminylation (O-GlcNAcylation) on YY1.
12588874	1	12	theme	cellular	176:183	arg1	genes					195:199	cellular and viral genes	176:199	cellular and viral genes	176:199	YY1 is a zinc finger DNA-binding transcription factor that influences expression of a wide variety of cellular and viral genes.
12588874	1	13	theme	variety	165:171	arg1	expression					144:153	expression	144:153	expression of a wide variety of cellular and viral genes	144:199	YY1 is a zinc finger DNA-binding transcription factor that influences expression of a wide variety of cellular and viral genes.
12588874	9	14	theme	cycle	1025:1029	arg1	transitions					1031:1041	cell cycle transitions	1020:1041	cell cycle transitions that regulate the YY1-Rb heterodimerization and promote the activity of YY1	1020:1117	The ability of the O-glycosylation on YY1 to disrupt the complex with Rb leads us to propose that O-glycosylation might have a profound effect on cell cycle transitions that regulate the YY1-Rb heterodimerization and promote the activity of YY1.
12588874	3	15	theme	cellular	366:373	arg1	response					375:382	cellular response	366:382	cellular response to external stimuli	366:402	It regulates the expression of genes with important functions in DNA replication, protein synthesis, and cellular response to external stimuli during cell growth and differentiation.
12588874	5	16	theme	differentiation	599:613	arg1	status					615:620	the differentiation status	595:620	the differentiation status of the cells	595:633	Here, we show that a subset of the nuclear YY1 appears to be O-GlcNAcylated regardless of the differentiation status of the cells.
12588874	5	17	theme	nuclear	540:546	arg1	YY1					548:550	the nuclear YY1	536:550	the nuclear YY1	536:550	Here, we show that a subset of the nuclear YY1 appears to be O-GlcNAcylated regardless of the differentiation status of the cells.
12588874	9	18	with	complex	931:937	arg1	Rb					944:945	Rb	944:945	Rb	944:945	The ability of the O-glycosylation on YY1 to disrupt the complex with Rb leads us to propose that O-glycosylation might have a profound effect on cell cycle transitions that regulate the YY1-Rb heterodimerization and promote the activity of YY1.
12588874	10	19	theme	glucose	1237:1243	arg1	metabolism					1245:1254	glucose metabolism	1237:1254	glucose metabolism	1237:1254	Our observations provide strong evidence that YY1-regulated transcription is very likely connected to the pathway of glucose metabolism that culminates in the O-GlcNAcylation on YY1, changing its function in transcription.
12588874	3	20	with	genes	292:296	arg1	functions					313:321	important functions	303:321	important functions in DNA replication, protein synthesis, and cellular response to external stimuli	303:402	It regulates the expression of genes with important functions in DNA replication, protein synthesis, and cellular response to external stimuli during cell growth and differentiation.
12588874	9	21	from	ability	878:884	arg1	YY1					912:914	YY1	912:914	YY1	912:914	The ability of the O-glycosylation on YY1 to disrupt the complex with Rb leads us to propose that O-glycosylation might have a profound effect on cell cycle transitions that regulate the YY1-Rb heterodimerization and promote the activity of YY1.
12588874	5	22	theme	YY1	548:550	arg1	O-GlcNAcylated					566:579	O-GlcNAcylated	566:579	O-GlcNAcylated	566:579	Here, we show that a subset of the nuclear YY1 appears to be O-GlcNAcylated regardless of the differentiation status of the cells.
12588874	5	22	theme	YY1	548:550	arg1	subset					526:531	a subset	524:531	a subset of the nuclear YY1	524:550	Here, we show that a subset of the nuclear YY1 appears to be O-GlcNAcylated regardless of the differentiation status of the cells.
12588874	1	23	theme	zinc	83:86	arg1	YY1					74:76	YY1	74:76	YY1	74:76	YY1 is a zinc finger DNA-binding transcription factor that influences expression of a wide variety of cellular and viral genes.
12588874	1	23	theme	zinc	83:86	arg1	factor					121:126	a zinc finger DNA-binding transcription factor	81:126	a zinc finger DNA-binding transcription factor that influences expression of a wide variety of cellular and viral genes	81:199	YY1 is a zinc finger DNA-binding transcription factor that influences expression of a wide variety of cellular and viral genes.
12588874	8	24	gly	glycosylated	836:847	arg1	free					856:859	free	856:859	free	856:859	Upon dissociation from Rb, the glycosylated YY1 is free to bind DNA.
12588874	8	24	gly	glycosylated	836:847	arg1	YY1					849:851	the glycosylated YY1	832:851	the glycosylated YY1	832:851	Upon dissociation from Rb, the glycosylated YY1 is free to bind DNA.
12588874	0	25	link	O-linked	20:27	arg1	N-acetylglucosaminylation					29:53	O-linked N-acetylglucosaminylation	20:53	O-linked N-acetylglucosaminylation (O-glcNAcylation)	20:71	YY1 is regulated by O-linked N-acetylglucosaminylation (O-glcNAcylation).
12588874	0	25	link	O-linked	20:27	arg1	O-glcNAcylation					56:70	O-glcNAcylation	56:70	O-glcNAcylation	56:70	YY1 is regulated by O-linked N-acetylglucosaminylation (O-glcNAcylation).
12588874	1	26	theme	finger	88:93	arg1	YY1					74:76	YY1	74:76	YY1	74:76	YY1 is a zinc finger DNA-binding transcription factor that influences expression of a wide variety of cellular and viral genes.
12588874	1	26	theme	finger	88:93	arg1	factor					121:126	a zinc finger DNA-binding transcription factor	81:126	a zinc finger DNA-binding transcription factor that influences expression of a wide variety of cellular and viral genes	81:199	YY1 is a zinc finger DNA-binding transcription factor that influences expression of a wide variety of cellular and viral genes.
12588874	1	27	theme	viral	189:193	arg1	genes					195:199	cellular and viral genes	176:199	cellular and viral genes	176:199	YY1 is a zinc finger DNA-binding transcription factor that influences expression of a wide variety of cellular and viral genes.
12588874	7	28	theme	retinoblastoma	776:789	arg1	protein					791:797	the retinoblastoma protein	772:797	the retinoblastoma protein (Rb)	772:802	Glycosylated YY1 no longer binds the retinoblastoma protein (Rb).
12588874	7	28	theme	retinoblastoma	776:789	arg1	Rb					800:801	Rb	800:801	Rb	800:801	Glycosylated YY1 no longer binds the retinoblastoma protein (Rb).
12588874	9	29	from	YY1	912:914	arg1	ability					878:884	The ability	874:884	The ability of the O-glycosylation on YY1 to disrupt the complex with Rb	874:945	The ability of the O-glycosylation on YY1 to disrupt the complex with Rb leads us to propose that O-glycosylation might have a profound effect on cell cycle transitions that regulate the YY1-Rb heterodimerization and promote the activity of YY1.
12588874	1	30	theme	DNA-binding	95:105	arg1	YY1					74:76	YY1	74:76	YY1	74:76	YY1 is a zinc finger DNA-binding transcription factor that influences expression of a wide variety of cellular and viral genes.
12588874	1	30	theme	DNA-binding	95:105	arg1	factor					121:126	a zinc finger DNA-binding transcription factor	81:126	a zinc finger DNA-binding transcription factor that influences expression of a wide variety of cellular and viral genes	81:199	YY1 is a zinc finger DNA-binding transcription factor that influences expression of a wide variety of cellular and viral genes.
12588874	1	31	theme	genes	195:199	arg1	genes					195:199	cellular and viral genes	176:199	cellular and viral genes	176:199	YY1 is a zinc finger DNA-binding transcription factor that influences expression of a wide variety of cellular and viral genes.
12588874	1	31	theme	genes	195:199	arg1	variety					165:171	a wide variety	158:171	a wide variety of cellular and viral genes	158:199	YY1 is a zinc finger DNA-binding transcription factor that influences expression of a wide variety of cellular and viral genes.
12588874	6	32	theme	O-linked	678:685	arg1	O-GlcNAcylation					714:728	O-GlcNAcylation	714:728	O-GlcNAcylation	714:728	We found that glucose strongly stimulates O-linked N-acetylglucosaminylation (O-GlcNAcylation) on YY1.
12588874	6	32	theme	O-linked	678:685	arg1	N-acetylglucosaminylation					687:711	O-linked N-acetylglucosaminylation	678:711	O-linked N-acetylglucosaminylation (O-GlcNAcylation) on YY1	678:736	We found that glucose strongly stimulates O-linked N-acetylglucosaminylation (O-GlcNAcylation) on YY1.
12588874	3	33	dep	cell	411:414	arg1	differentiation					427:441	differentiation	427:441	differentiation	427:441	It regulates the expression of genes with important functions in DNA replication, protein synthesis, and cellular response to external stimuli during cell growth and differentiation.
12588874	3	33	dep	cell	411:414	arg1	growth					416:421	growth	416:421	growth	416:421	It regulates the expression of genes with important functions in DNA replication, protein synthesis, and cellular response to external stimuli during cell growth and differentiation.
12588874	9	34	theme	YY1-Rb	1061:1066	arg1	heterodimerization					1068:1085	the YY1-Rb heterodimerization	1057:1085	the YY1-Rb heterodimerization	1057:1085	The ability of the O-glycosylation on YY1 to disrupt the complex with Rb leads us to propose that O-glycosylation might have a profound effect on cell cycle transitions that regulate the YY1-Rb heterodimerization and promote the activity of YY1.
12588874	0	35	theme	O-linked	20:27	arg1	N-acetylglucosaminylation					29:53	O-linked N-acetylglucosaminylation	20:53	O-linked N-acetylglucosaminylation (O-glcNAcylation)	20:71	YY1 is regulated by O-linked N-acetylglucosaminylation (O-glcNAcylation).
12588874	0	35	theme	O-linked	20:27	arg1	O-glcNAcylation					56:70	O-glcNAcylation	56:70	O-glcNAcylation	56:70	YY1 is regulated by O-linked N-acetylglucosaminylation (O-glcNAcylation).
12588874	9	36	dep	ability	878:884	arg1	disrupt					919:925	disrupt	919:925	to disrupt the complex with Rb	916:945	The ability of the O-glycosylation on YY1 to disrupt the complex with Rb leads us to propose that O-glycosylation might have a profound effect on cell cycle transitions that regulate the YY1-Rb heterodimerization and promote the activity of YY1.
12588874	9	37	from	O-glycosylation	893:907	arg1	YY1					912:914	YY1	912:914	YY1	912:914	The ability of the O-glycosylation on YY1 to disrupt the complex with Rb leads us to propose that O-glycosylation might have a profound effect on cell cycle transitions that regulate the YY1-Rb heterodimerization and promote the activity of YY1.
12588874	9	38	theme	O-glycosylation	893:907	arg1	ability					878:884	The ability	874:884	The ability of the O-glycosylation on YY1 to disrupt the complex with Rb	874:945	The ability of the O-glycosylation on YY1 to disrupt the complex with Rb leads us to propose that O-glycosylation might have a profound effect on cell cycle transitions that regulate the YY1-Rb heterodimerization and promote the activity of YY1.
12588874	3	39	theme	genes	292:296	arg1	expression					278:287	the expression	274:287	the expression of genes with important functions in DNA replication, protein synthesis, and cellular response to external stimuli	274:402	It regulates the expression of genes with important functions in DNA replication, protein synthesis, and cellular response to external stimuli during cell growth and differentiation.
12588874	1	40	theme	transcription	107:119	arg1	YY1					74:76	YY1	74:76	YY1	74:76	YY1 is a zinc finger DNA-binding transcription factor that influences expression of a wide variety of cellular and viral genes.
12588874	1	40	theme	transcription	107:119	arg1	factor					121:126	a zinc finger DNA-binding transcription factor	81:126	a zinc finger DNA-binding transcription factor that influences expression of a wide variety of cellular and viral genes	81:199	YY1 is a zinc finger DNA-binding transcription factor that influences expression of a wide variety of cellular and viral genes.
12588874	3	41	theme	external	387:394	arg1	stimuli					396:402	external stimuli	387:402	external stimuli	387:402	It regulates the expression of genes with important functions in DNA replication, protein synthesis, and cellular response to external stimuli during cell growth and differentiation.
12588874	3	42	from	functions	313:321	arg1	response					375:382	cellular response	366:382	cellular response to external stimuli	366:402	It regulates the expression of genes with important functions in DNA replication, protein synthesis, and cellular response to external stimuli during cell growth and differentiation.
12588874	3	42	from	functions	313:321	arg1	replication					330:340	DNA replication	326:340	DNA replication	326:340	It regulates the expression of genes with important functions in DNA replication, protein synthesis, and cellular response to external stimuli during cell growth and differentiation.
12588874	3	42	from	functions	313:321	arg1	synthesis					351:359	protein synthesis	343:359	protein synthesis	343:359	It regulates the expression of genes with important functions in DNA replication, protein synthesis, and cellular response to external stimuli during cell growth and differentiation.
12588874	2	43	theme	embryos	252:258	arg1	development					227:237	the development	223:237	the development of mammalian embryos	223:258	YY1 is essential for the development of mammalian embryos.
12588874	8	44	from	Rb	828:829	arg1	dissociation					810:821	dissociation	810:821	dissociation from Rb	810:829	Upon dissociation from Rb, the glycosylated YY1 is free to bind DNA.
12588874	7	45	theme	Glycosylated	739:750	arg1	YY1					752:754	Glycosylated YY1	739:754	Glycosylated YY1	739:754	Glycosylated YY1 no longer binds the retinoblastoma protein (Rb).
12588874	2	46	theme	mammalian	242:250	arg1	embryos					252:258	mammalian embryos	242:258	mammalian embryos	242:258	YY1 is essential for the development of mammalian embryos.
12588874	10	47	theme	metabolism	1245:1254	arg1	pathway					1226:1232	the pathway	1222:1232	the pathway of glucose metabolism that culminates in the O-GlcNAcylation on YY1, changing its function in transcription	1222:1340	Our observations provide strong evidence that YY1-regulated transcription is very likely connected to the pathway of glucose metabolism that culminates in the O-GlcNAcylation on YY1, changing its function in transcription.
12588874	9	48	contain	have	994:997	arg1	O-glycosylation					972:986	O-glycosylation	972:986	O-glycosylation	972:986	The ability of the O-glycosylation on YY1 to disrupt the complex with Rb leads us to propose that O-glycosylation might have a profound effect on cell cycle transitions that regulate the YY1-Rb heterodimerization and promote the activity of YY1.
12588874	9	48	contain	have	994:997	arg2	effect					1010:1015	a profound effect	999:1015	a profound effect	999:1015	The ability of the O-glycosylation on YY1 to disrupt the complex with Rb leads us to propose that O-glycosylation might have a profound effect on cell cycle transitions that regulate the YY1-Rb heterodimerization and promote the activity of YY1.
12588874	9	49	gly	O-glycosylation	893:907	arg1	YY1					912:914	YY1	912:914	YY1	912:914	The ability of the O-glycosylation on YY1 to disrupt the complex with Rb leads us to propose that O-glycosylation might have a profound effect on cell cycle transitions that regulate the YY1-Rb heterodimerization and promote the activity of YY1.
12588874	3	50	theme	DNA	326:328	arg1	replication					330:340	DNA replication	326:340	DNA replication	326:340	It regulates the expression of genes with important functions in DNA replication, protein synthesis, and cellular response to external stimuli during cell growth and differentiation.
12588874	10	51	from	O-GlcNAcylation	1279:1293	arg1	YY1					1298:1300	YY1	1298:1300	YY1	1298:1300	Our observations provide strong evidence that YY1-regulated transcription is very likely connected to the pathway of glucose metabolism that culminates in the O-GlcNAcylation on YY1, changing its function in transcription.
12588874	9	52	theme	YY1	1115:1117	arg1	activity					1103:1110	the activity	1099:1110	the activity of YY1	1099:1117	The ability of the O-glycosylation on YY1 to disrupt the complex with Rb leads us to propose that O-glycosylation might have a profound effect on cell cycle transitions that regulate the YY1-Rb heterodimerization and promote the activity of YY1.
12588874	10	53	theme	strong	1145:1150	arg1	evidence					1152:1159	strong evidence that YY1-regulated transcription is very likely connected to the pathway of glucose metabolism that culminates in the O-GlcNAcylation on YY1, changing its function in transcription	1145:1340	strong evidence that YY1-regulated transcription is very likely connected to the pathway of glucose metabolism that culminates in the O-GlcNAcylation on YY1, changing its function in transcription	1145:1340	Our observations provide strong evidence that YY1-regulated transcription is very likely connected to the pathway of glucose metabolism that culminates in the O-GlcNAcylation on YY1, changing its function in transcription.
26358770	5	0	theme	interaction	794:804	arg1	inhibition					773:782	inhibition	773:782	inhibition	773:782	Indeed, Aβ bound to ATP synthase directly and reduced the O-GlcNAcylation of ATP5A by inhibition of direct interaction between ATP5A and mitochondrial O-GlcNAc transferase, resulting in decreased ATP production and ATPase activity.
26358770	4	1	theme	Aβ-treated	669:678	arg1	cells					680:684	Aβ-treated cells	669:684	Aβ-treated cells	669:684	Here, we found that ATP synthase subunit α (ATP5A) was O-GlcNAcylated at Thr432 and ATP5A O-GlcNAcylation was decreased in the brains of AD patients and transgenic mouse model, as well as Aβ-treated cells.
26358770	5	2	theme	ATP	707:709	arg1	synthase					711:718	ATP synthase	707:718	ATP synthase	707:718	Indeed, Aβ bound to ATP synthase directly and reduced the O-GlcNAcylation of ATP5A by inhibition of direct interaction between ATP5A and mitochondrial O-GlcNAc transferase, resulting in decreased ATP production and ATPase activity.
26358770	4	3	theme	ATP5A	565:569	arg1	O-GlcNAcylation					571:585	ATP5A O-GlcNAcylation	565:585	ATP5A O-GlcNAcylation	565:585	Here, we found that ATP synthase subunit α (ATP5A) was O-GlcNAcylated at Thr432 and ATP5A O-GlcNAcylation was decreased in the brains of AD patients and transgenic mouse model, as well as Aβ-treated cells.
26358770	7	4	theme	Thr432	1224:1229	arg1	residue					1231:1237	Thr432 residue	1224:1237	Thr432 residue on ATP5A	1224:1246	These results indicate that Aβ-mediated reduction of ATP synthase activity in AD pathology results from direct binding between Aβ and ATP synthase and inhibition of O-GlcNAcylation of Thr432 residue on ATP5A.
26358770	7	5	from	ATP5A	1242:1246	arg1	O-GlcNAcylation					1205:1219	O-GlcNAcylation	1205:1219	O-GlcNAcylation of Thr432 residue on ATP5A	1205:1246	These results indicate that Aβ-mediated reduction of ATP synthase activity in AD pathology results from direct binding between Aβ and ATP synthase and inhibition of O-GlcNAcylation of Thr432 residue on ATP5A.
26358770	5	6	theme	ATP	883:885	arg1	production					887:896	decreased ATP production	873:896	decreased ATP production	873:896	Indeed, Aβ bound to ATP synthase directly and reduced the O-GlcNAcylation of ATP5A by inhibition of direct interaction between ATP5A and mitochondrial O-GlcNAc transferase, resulting in decreased ATP production and ATPase activity.
26358770	3	7	theme	adenosine	376:384	arg1	ATP					403:405	ATP	403:405	ATP	403:405	Mitochondrial adenosine 5'-triphosphate (ATP) synthase is a multiprotein complex that synthesizes ATP from ADP and Pi.
26358770	3	7	theme	adenosine	376:384	arg1	5'-triphosphate					386:400	Mitochondrial adenosine 5'-triphosphate	362:400	Mitochondrial adenosine 5'-triphosphate (ATP) synthase	362:415	Mitochondrial adenosine 5'-triphosphate (ATP) synthase is a multiprotein complex that synthesizes ATP from ADP and Pi.
26358770	4	8	theme	synthase	505:512	arg1	ATP5A					525:529	ATP5A	525:529	ATP5A	525:529	Here, we found that ATP synthase subunit α (ATP5A) was O-GlcNAcylated at Thr432 and ATP5A O-GlcNAcylation was decreased in the brains of AD patients and transgenic mouse model, as well as Aβ-treated cells.
26358770	4	8	theme	synthase	505:512	arg1	subunit					514:520	ATP synthase subunit α	501:522	ATP synthase subunit α (ATP5A)	501:530	Here, we found that ATP synthase subunit α (ATP5A) was O-GlcNAcylated at Thr432 and ATP5A O-GlcNAcylation was decreased in the brains of AD patients and transgenic mouse model, as well as Aβ-treated cells.
26358770	6	9	theme	Aβ-induced	979:988	arg1	impairment					990:999	the Aβ-induced impairment	975:999	the Aβ-induced impairment in ATP production and ATPase activity	975:1037	Furthermore, treatment of O-GlcNAcase inhibitor rescued the Aβ-induced impairment in ATP production and ATPase activity.
26358770	3	10	theme	5'-triphosphate	386:400	arg1	synthase					408:415	Mitochondrial adenosine 5'-triphosphate (ATP) synthase	362:415	Mitochondrial adenosine 5'-triphosphate (ATP) synthase	362:415	Mitochondrial adenosine 5'-triphosphate (ATP) synthase is a multiprotein complex that synthesizes ATP from ADP and Pi.
26358770	3	10	theme	5'-triphosphate	386:400	arg1	complex					435:441	a multiprotein complex	420:441	a multiprotein complex that synthesizes ATP from ADP and Pi	420:478	Mitochondrial adenosine 5'-triphosphate (ATP) synthase is a multiprotein complex that synthesizes ATP from ADP and Pi.
26358770	7	11	theme	AD	1118:1119	arg1	pathology					1121:1129	AD pathology	1118:1129	AD pathology	1118:1129	These results indicate that Aβ-mediated reduction of ATP synthase activity in AD pathology results from direct binding between Aβ and ATP synthase and inhibition of O-GlcNAcylation of Thr432 residue on ATP5A.
26358770	5	12	theme	decreased	873:881	arg1	production					887:896	decreased ATP production	873:896	decreased ATP production	873:896	Indeed, Aβ bound to ATP synthase directly and reduced the O-GlcNAcylation of ATP5A by inhibition of direct interaction between ATP5A and mitochondrial O-GlcNAc transferase, resulting in decreased ATP production and ATPase activity.
26358770	7	13	from	reduction	1080:1088	arg1	pathology					1121:1129	AD pathology	1118:1129	AD pathology	1118:1129	These results indicate that Aβ-mediated reduction of ATP synthase activity in AD pathology results from direct binding between Aβ and ATP synthase and inhibition of O-GlcNAcylation of Thr432 residue on ATP5A.
26358770	7	14	theme	synthase	1097:1104	arg1	activity					1106:1113	ATP synthase activity	1093:1113	ATP synthase activity	1093:1113	These results indicate that Aβ-mediated reduction of ATP synthase activity in AD pathology results from direct binding between Aβ and ATP synthase and inhibition of O-GlcNAcylation of Thr432 residue on ATP5A.
26358770	4	15	from	Thr432	554:559	arg1	O-GlcNAcylated					536:549	O-GlcNAcylated	536:549	O-GlcNAcylated	536:549	Here, we found that ATP synthase subunit α (ATP5A) was O-GlcNAcylated at Thr432 and ATP5A O-GlcNAcylation was decreased in the brains of AD patients and transgenic mouse model, as well as Aβ-treated cells.
26358770	4	16	theme	mouse	645:649	arg1	model					651:655	transgenic mouse model	634:655	transgenic mouse model	634:655	Here, we found that ATP synthase subunit α (ATP5A) was O-GlcNAcylated at Thr432 and ATP5A O-GlcNAcylation was decreased in the brains of AD patients and transgenic mouse model, as well as Aβ-treated cells.
26358770	3	17	theme	Mitochondrial	362:374	arg1	ATP					403:405	ATP	403:405	ATP	403:405	Mitochondrial adenosine 5'-triphosphate (ATP) synthase is a multiprotein complex that synthesizes ATP from ADP and Pi.
26358770	3	17	theme	Mitochondrial	362:374	arg1	5'-triphosphate					386:400	Mitochondrial adenosine 5'-triphosphate	362:400	Mitochondrial adenosine 5'-triphosphate (ATP) synthase	362:415	Mitochondrial adenosine 5'-triphosphate (ATP) synthase is a multiprotein complex that synthesizes ATP from ADP and Pi.
26358770	7	18	theme	activity	1106:1113	arg1	reduction					1080:1088	Aβ-mediated reduction	1068:1088	Aβ-mediated reduction of ATP synthase activity in AD pathology	1068:1129	These results indicate that Aβ-mediated reduction of ATP synthase activity in AD pathology results from direct binding between Aβ and ATP synthase and inhibition of O-GlcNAcylation of Thr432 residue on ATP5A.
26358770	2	19	from	role	253:256	arg1	disease					327:333	Alzheimer's disease	315:333	Alzheimer's disease (AD)	315:338	However, the role of O-GlcNAcylation in neurodegenerative diseases such as Alzheimer's disease (AD) is poorly understood.
26358770	2	19	from	role	253:256	arg1	diseases					298:305	neurodegenerative diseases	280:305	neurodegenerative diseases such as Alzheimer's disease (AD)	280:338	However, the role of O-GlcNAcylation in neurodegenerative diseases such as Alzheimer's disease (AD) is poorly understood.
26358770	1	20	theme	protein	177:183	arg1	glycosylations					185:198	the protein glycosylations	173:198	the protein glycosylations affecting various intracellular events	173:237	Glycosylation with O-linked β-N-acetylglucosamine (O-GlcNAc) is one of the protein glycosylations affecting various intracellular events.
26358770	0	21	theme	ATP	14:16	arg1	activity					27:34	Mitochondrial ATP synthase activity	0:34	Mitochondrial ATP synthase activity	0:34	Mitochondrial ATP synthase activity is impaired by suppressed O-GlcNAcylation in Alzheimer's disease.
26358770	7	22	theme	ATP	1174:1176	arg1	synthase					1178:1185	ATP synthase	1174:1185	ATP synthase	1174:1185	These results indicate that Aβ-mediated reduction of ATP synthase activity in AD pathology results from direct binding between Aβ and ATP synthase and inhibition of O-GlcNAcylation of Thr432 residue on ATP5A.
26358770	1	23	theme	glycosylations	185:198	arg1	glycosylations					185:198	the protein glycosylations	173:198	the protein glycosylations affecting various intracellular events	173:237	Glycosylation with O-linked β-N-acetylglucosamine (O-GlcNAc) is one of the protein glycosylations affecting various intracellular events.
26358770	1	23	theme	glycosylations	185:198	arg1	one					166:168	one	166:168	one	166:168	Glycosylation with O-linked β-N-acetylglucosamine (O-GlcNAc) is one of the protein glycosylations affecting various intracellular events.
26358770	0	24	theme	Mitochondrial	0:12	arg1	activity					27:34	Mitochondrial ATP synthase activity	0:34	Mitochondrial ATP synthase activity	0:34	Mitochondrial ATP synthase activity is impaired by suppressed O-GlcNAcylation in Alzheimer's disease.
26358770	6	25	from	impairment	990:999	arg1	production					1008:1017	ATP production	1004:1017	ATP production	1004:1017	Furthermore, treatment of O-GlcNAcase inhibitor rescued the Aβ-induced impairment in ATP production and ATPase activity.
26358770	6	25	from	impairment	990:999	arg1	activity					1030:1037	ATPase activity	1023:1037	ATPase activity	1023:1037	Furthermore, treatment of O-GlcNAcase inhibitor rescued the Aβ-induced impairment in ATP production and ATPase activity.
26358770	4	26	gly	O-GlcNAcylation	571:585	arg1	cells					680:684	Aβ-treated cells	669:684	Aβ-treated cells	669:684	Here, we found that ATP synthase subunit α (ATP5A) was O-GlcNAcylated at Thr432 and ATP5A O-GlcNAcylation was decreased in the brains of AD patients and transgenic mouse model, as well as Aβ-treated cells.
26358770	4	26	gly	O-GlcNAcylation	571:585	arg1	brains					608:613	the brains	604:613	the brains of AD patients and transgenic mouse model	604:655	Here, we found that ATP synthase subunit α (ATP5A) was O-GlcNAcylated at Thr432 and ATP5A O-GlcNAcylation was decreased in the brains of AD patients and transgenic mouse model, as well as Aβ-treated cells.
26358770	5	27	theme	O-GlcNAc	838:845	arg1	transferase					847:857	mitochondrial O-GlcNAc transferase	824:857	mitochondrial O-GlcNAc transferase	824:857	Indeed, Aβ bound to ATP synthase directly and reduced the O-GlcNAcylation of ATP5A by inhibition of direct interaction between ATP5A and mitochondrial O-GlcNAc transferase, resulting in decreased ATP production and ATPase activity.
26358770	4	28	theme	model	651:655	arg1	cells					680:684	Aβ-treated cells	669:684	Aβ-treated cells	669:684	Here, we found that ATP synthase subunit α (ATP5A) was O-GlcNAcylated at Thr432 and ATP5A O-GlcNAcylation was decreased in the brains of AD patients and transgenic mouse model, as well as Aβ-treated cells.
26358770	4	28	theme	model	651:655	arg1	brains					608:613	the brains	604:613	the brains of AD patients and transgenic mouse model	604:655	Here, we found that ATP synthase subunit α (ATP5A) was O-GlcNAcylated at Thr432 and ATP5A O-GlcNAcylation was decreased in the brains of AD patients and transgenic mouse model, as well as Aβ-treated cells.
26358770	6	29	theme	inhibitor	957:965	arg1	treatment					932:940	treatment	932:940	treatment of O-GlcNAcase inhibitor	932:965	Furthermore, treatment of O-GlcNAcase inhibitor rescued the Aβ-induced impairment in ATP production and ATPase activity.
26358770	7	30	theme	Aβ-mediated	1068:1078	arg1	reduction					1080:1088	Aβ-mediated reduction	1068:1088	Aβ-mediated reduction of ATP synthase activity in AD pathology	1068:1129	These results indicate that Aβ-mediated reduction of ATP synthase activity in AD pathology results from direct binding between Aβ and ATP synthase and inhibition of O-GlcNAcylation of Thr432 residue on ATP5A.
26358770	4	31	theme	AD	618:619	arg1	patients					621:628	AD patients	618:628	AD patients	618:628	Here, we found that ATP synthase subunit α (ATP5A) was O-GlcNAcylated at Thr432 and ATP5A O-GlcNAcylation was decreased in the brains of AD patients and transgenic mouse model, as well as Aβ-treated cells.
26358770	0	32	theme	synthase	18:25	arg1	activity					27:34	Mitochondrial ATP synthase activity	0:34	Mitochondrial ATP synthase activity	0:34	Mitochondrial ATP synthase activity is impaired by suppressed O-GlcNAcylation in Alzheimer's disease.
26358770	6	33	theme	O-GlcNAcase	945:955	arg1	inhibitor					957:965	O-GlcNAcase inhibitor	945:965	O-GlcNAcase inhibitor	945:965	Furthermore, treatment of O-GlcNAcase inhibitor rescued the Aβ-induced impairment in ATP production and ATPase activity.
26358770	1	34	theme	intracellular	218:230	arg1	events					232:237	various intracellular events	210:237	various intracellular events	210:237	Glycosylation with O-linked β-N-acetylglucosamine (O-GlcNAc) is one of the protein glycosylations affecting various intracellular events.
26358770	3	35	theme	multiprotein	422:433	arg1	synthase					408:415	Mitochondrial adenosine 5'-triphosphate (ATP) synthase	362:415	Mitochondrial adenosine 5'-triphosphate (ATP) synthase	362:415	Mitochondrial adenosine 5'-triphosphate (ATP) synthase is a multiprotein complex that synthesizes ATP from ADP and Pi.
26358770	3	35	theme	multiprotein	422:433	arg1	complex					435:441	a multiprotein complex	420:441	a multiprotein complex that synthesizes ATP from ADP and Pi	420:478	Mitochondrial adenosine 5'-triphosphate (ATP) synthase is a multiprotein complex that synthesizes ATP from ADP and Pi.
26358770	5	36	theme	mitochondrial	824:836	arg1	transferase					847:857	mitochondrial O-GlcNAc transferase	824:857	mitochondrial O-GlcNAc transferase	824:857	Indeed, Aβ bound to ATP synthase directly and reduced the O-GlcNAcylation of ATP5A by inhibition of direct interaction between ATP5A and mitochondrial O-GlcNAc transferase, resulting in decreased ATP production and ATPase activity.
26358770	7	37	theme	direct	1144:1149	arg1	binding					1151:1157	direct binding	1144:1157	direct binding between Aβ and ATP synthase	1144:1185	These results indicate that Aβ-mediated reduction of ATP synthase activity in AD pathology results from direct binding between Aβ and ATP synthase and inhibition of O-GlcNAcylation of Thr432 residue on ATP5A.
26358770	4	38	theme	patients	621:628	arg1	cells					680:684	Aβ-treated cells	669:684	Aβ-treated cells	669:684	Here, we found that ATP synthase subunit α (ATP5A) was O-GlcNAcylated at Thr432 and ATP5A O-GlcNAcylation was decreased in the brains of AD patients and transgenic mouse model, as well as Aβ-treated cells.
26358770	4	38	theme	patients	621:628	arg1	brains					608:613	the brains	604:613	the brains of AD patients and transgenic mouse model	604:655	Here, we found that ATP synthase subunit α (ATP5A) was O-GlcNAcylated at Thr432 and ATP5A O-GlcNAcylation was decreased in the brains of AD patients and transgenic mouse model, as well as Aβ-treated cells.
26358770	0	39	theme	suppressed	51:60	arg1	O-GlcNAcylation					62:76	suppressed O-GlcNAcylation	51:76	suppressed O-GlcNAcylation in Alzheimer's disease	51:99	Mitochondrial ATP synthase activity is impaired by suppressed O-GlcNAcylation in Alzheimer's disease.
26358770	7	40	from	O-GlcNAcylation	1205:1219	arg1	ATP5A					1242:1246	ATP5A	1242:1246	ATP5A	1242:1246	These results indicate that Aβ-mediated reduction of ATP synthase activity in AD pathology results from direct binding between Aβ and ATP synthase and inhibition of O-GlcNAcylation of Thr432 residue on ATP5A.
26358770	1	41	theme	O-linked	121:128	arg1	O-GlcNAc					153:160	O-GlcNAc	153:160	O-GlcNAc	153:160	Glycosylation with O-linked β-N-acetylglucosamine (O-GlcNAc) is one of the protein glycosylations affecting various intracellular events.
26358770	1	41	theme	O-linked	121:128	arg1	β-N-acetylglucosamine					130:150	O-linked β-N-acetylglucosamine	121:150	O-linked β-N-acetylglucosamine (O-GlcNAc)	121:161	Glycosylation with O-linked β-N-acetylglucosamine (O-GlcNAc) is one of the protein glycosylations affecting various intracellular events.
26358770	5	42	theme	ATP5A	764:768	arg1	O-GlcNAcylation					745:759	the O-GlcNAcylation	741:759	the O-GlcNAcylation of ATP5A	741:768	Indeed, Aβ bound to ATP synthase directly and reduced the O-GlcNAcylation of ATP5A by inhibition of direct interaction between ATP5A and mitochondrial O-GlcNAc transferase, resulting in decreased ATP production and ATPase activity.
26358770	7	43	theme	O-GlcNAcylation	1205:1219	arg1	binding					1151:1157	direct binding	1144:1157	direct binding between Aβ and ATP synthase	1144:1185	These results indicate that Aβ-mediated reduction of ATP synthase activity in AD pathology results from direct binding between Aβ and ATP synthase and inhibition of O-GlcNAcylation of Thr432 residue on ATP5A.
26358770	7	43	theme	O-GlcNAcylation	1205:1219	arg1	inhibition					1191:1200	inhibition	1191:1200	inhibition of O-GlcNAcylation of Thr432 residue on ATP5A	1191:1246	These results indicate that Aβ-mediated reduction of ATP synthase activity in AD pathology results from direct binding between Aβ and ATP synthase and inhibition of O-GlcNAcylation of Thr432 residue on ATP5A.
26358770	1	44	link	O-linked	121:128	arg1	O-GlcNAc					153:160	O-GlcNAc	153:160	O-GlcNAc	153:160	Glycosylation with O-linked β-N-acetylglucosamine (O-GlcNAc) is one of the protein glycosylations affecting various intracellular events.
26358770	1	44	link	O-linked	121:128	arg1	β-N-acetylglucosamine					130:150	O-linked β-N-acetylglucosamine	121:150	O-linked β-N-acetylglucosamine (O-GlcNAc)	121:161	Glycosylation with O-linked β-N-acetylglucosamine (O-GlcNAc) is one of the protein glycosylations affecting various intracellular events.
26358770	2	45	theme	neurodegenerative	280:296	arg1	disease					327:333	Alzheimer's disease	315:333	Alzheimer's disease (AD)	315:338	However, the role of O-GlcNAcylation in neurodegenerative diseases such as Alzheimer's disease (AD) is poorly understood.
26358770	2	45	theme	neurodegenerative	280:296	arg1	diseases					298:305	neurodegenerative diseases	280:305	neurodegenerative diseases such as Alzheimer's disease (AD)	280:338	However, the role of O-GlcNAcylation in neurodegenerative diseases such as Alzheimer's disease (AD) is poorly understood.
26358770	5	46	theme	ATPase	902:907	arg1	activity					909:916	ATPase activity	902:916	ATPase activity	902:916	Indeed, Aβ bound to ATP synthase directly and reduced the O-GlcNAcylation of ATP5A by inhibition of direct interaction between ATP5A and mitochondrial O-GlcNAc transferase, resulting in decreased ATP production and ATPase activity.
26358770	6	47	theme	ATPase	1023:1028	arg1	activity					1030:1037	ATPase activity	1023:1037	ATPase activity	1023:1037	Furthermore, treatment of O-GlcNAcase inhibitor rescued the Aβ-induced impairment in ATP production and ATPase activity.
26358770	7	48	from	residue	1231:1237	arg1	ATP5A					1242:1246	ATP5A	1242:1246	ATP5A	1242:1246	These results indicate that Aβ-mediated reduction of ATP synthase activity in AD pathology results from direct binding between Aβ and ATP synthase and inhibition of O-GlcNAcylation of Thr432 residue on ATP5A.
26358770	7	49	theme	ATP	1093:1095	arg1	activity					1106:1113	ATP synthase activity	1093:1113	ATP synthase activity	1093:1113	These results indicate that Aβ-mediated reduction of ATP synthase activity in AD pathology results from direct binding between Aβ and ATP synthase and inhibition of O-GlcNAcylation of Thr432 residue on ATP5A.
26358770	7	50	theme	residue	1231:1237	arg1	O-GlcNAcylation					1205:1219	O-GlcNAcylation	1205:1219	O-GlcNAcylation of Thr432 residue on ATP5A	1205:1246	These results indicate that Aβ-mediated reduction of ATP synthase activity in AD pathology results from direct binding between Aβ and ATP synthase and inhibition of O-GlcNAcylation of Thr432 residue on ATP5A.
26358770	2	51	theme	O-GlcNAcylation	261:275	arg1	role					253:256	the role	249:256	the role of O-GlcNAcylation in neurodegenerative diseases such as Alzheimer's disease (AD)	249:338	However, the role of O-GlcNAcylation in neurodegenerative diseases such as Alzheimer's disease (AD) is poorly understood.
26358770	1	52	theme	various	210:216	arg1	events					232:237	various intracellular events	210:237	various intracellular events	210:237	Glycosylation with O-linked β-N-acetylglucosamine (O-GlcNAc) is one of the protein glycosylations affecting various intracellular events.
26358770	4	53	theme	transgenic	634:643	arg1	model					651:655	transgenic mouse model	634:655	transgenic mouse model	634:655	Here, we found that ATP synthase subunit α (ATP5A) was O-GlcNAcylated at Thr432 and ATP5A O-GlcNAcylation was decreased in the brains of AD patients and transgenic mouse model, as well as Aβ-treated cells.
26358770	4	54	theme	ATP	501:503	arg1	ATP5A					525:529	ATP5A	525:529	ATP5A	525:529	Here, we found that ATP synthase subunit α (ATP5A) was O-GlcNAcylated at Thr432 and ATP5A O-GlcNAcylation was decreased in the brains of AD patients and transgenic mouse model, as well as Aβ-treated cells.
26358770	4	54	theme	ATP	501:503	arg1	subunit					514:520	ATP synthase subunit α	501:522	ATP synthase subunit α (ATP5A)	501:530	Here, we found that ATP synthase subunit α (ATP5A) was O-GlcNAcylated at Thr432 and ATP5A O-GlcNAcylation was decreased in the brains of AD patients and transgenic mouse model, as well as Aβ-treated cells.
26358770	5	55	theme	direct	787:792	arg1	interaction					794:804	direct interaction	787:804	direct interaction between ATP5A and mitochondrial O-GlcNAc transferase	787:857	Indeed, Aβ bound to ATP synthase directly and reduced the O-GlcNAcylation of ATP5A by inhibition of direct interaction between ATP5A and mitochondrial O-GlcNAc transferase, resulting in decreased ATP production and ATPase activity.
26358770	1	56	with	Glycosylation	102:114	arg1	O-GlcNAc					153:160	O-GlcNAc	153:160	O-GlcNAc	153:160	Glycosylation with O-linked β-N-acetylglucosamine (O-GlcNAc) is one of the protein glycosylations affecting various intracellular events.
26358770	1	56	with	Glycosylation	102:114	arg1	β-N-acetylglucosamine					130:150	O-linked β-N-acetylglucosamine	121:150	O-linked β-N-acetylglucosamine (O-GlcNAc)	121:161	Glycosylation with O-linked β-N-acetylglucosamine (O-GlcNAc) is one of the protein glycosylations affecting various intracellular events.
26358770	6	57	theme	ATP	1004:1006	arg1	production					1008:1017	ATP production	1004:1017	ATP production	1004:1017	Furthermore, treatment of O-GlcNAcase inhibitor rescued the Aβ-induced impairment in ATP production and ATPase activity.
32411667	0	0	theme	Proteins	105:112	arg1	Labeling					93:100	Metabolism-Dependent Background Labeling	61:100	Metabolism-Dependent Background Labeling of Proteins	61:112	O-Acetylated Chemical Reporters of Glycosylation Can Display Metabolism-Dependent Background Labeling of Proteins but Are Generally Reliable Tools for the Identification of Glycoproteins.
32411667	11	1	theme	proteins	1990:1997	arg1	identification					1959:1972	unbiased identification	1950:1972	unbiased identification of glycosylated proteins	1950:1997	However, these results also show that MCRs are still good tools for unbiased identification of glycosylated proteins, as long as complementary methods are employed for confirmation.
32411667	7	2	theme	intracellular	1327:1339	arg1	modifications					1350:1362	intracellular O-GlcNAc modifications	1327:1362	intracellular O-GlcNAc modifications using MCRs	1327:1373	Given the implications this result has for the identification of intracellular O-GlcNAc modifications using MCRs, we then performed a meta-analysis of the potential O-GlcNAcylated proteins identified by different techniques.
32411667	0	3	theme	Glycoproteins	173:185	arg1	Identification					155:168	the Identification	151:168	the Identification of Glycoproteins	151:185	O-Acetylated Chemical Reporters of Glycosylation Can Display Metabolism-Dependent Background Labeling of Proteins but Are Generally Reliable Tools for the Identification of Glycoproteins.
32411667	10	4	dep	cytosol	1861:1867	arg1	the					1857:1859	the	1857:1859	the	1857:1859	Together, these data indicate that the selective metabolism of certain MCRs is responsible for S-glycosylation of proteins in the cytosol and nucleus.
32411667	6	5	used	used	1124:1127	arg2	we					1121:1122	we	1121:1122	we	1121:1122	Additionally, we used isotope targeted glycoproteomics (IsoTaG) proteomics to show that essentially all of the Ac42AzMan labeling is on cysteine residues.
32411667	1	6	theme	Monosaccharide	188:201	arg1	analogs					203:209	Monosaccharide analogs	188:209	Monosaccharide analogs bearing bioorthogonal functionalities	188:247	Monosaccharide analogs bearing bioorthogonal functionalities, or metabolic chemical reporters (MCRs) of glycosylation, have been used for approximately two decades for the visualization and identification of different glycoproteins.
32411667	10	7	from	nucleus	1873:1879	arg1	S-glycosylation					1826:1840	S-glycosylation	1826:1840	S-glycosylation of proteins in the cytosol and nucleus	1826:1879	Together, these data indicate that the selective metabolism of certain MCRs is responsible for S-glycosylation of proteins in the cytosol and nucleus.
32411667	1	8	theme	glycosylation	292:304	arg1	MCRs					283:286	MCRs	283:286	MCRs	283:286	Monosaccharide analogs bearing bioorthogonal functionalities, or metabolic chemical reporters (MCRs) of glycosylation, have been used for approximately two decades for the visualization and identification of different glycoproteins.
32411667	1	8	theme	glycosylation	292:304	arg1	analogs					203:209	Monosaccharide analogs	188:209	Monosaccharide analogs bearing bioorthogonal functionalities	188:247	Monosaccharide analogs bearing bioorthogonal functionalities, or metabolic chemical reporters (MCRs) of glycosylation, have been used for approximately two decades for the visualization and identification of different glycoproteins.
32411667	1	8	theme	glycosylation	292:304	arg1	reporters					272:280	metabolic chemical reporters	253:280	metabolic chemical reporters (MCRs) of glycosylation	253:304	Monosaccharide analogs bearing bioorthogonal functionalities, or metabolic chemical reporters (MCRs) of glycosylation, have been used for approximately two decades for the visualization and identification of different glycoproteins.
32411667	7	9	theme	O-GlcNAcylated	1427:1440	arg1	proteins					1442:1449	the potential O-GlcNAcylated proteins	1413:1449	the potential O-GlcNAcylated proteins identified by different techniques	1413:1484	Given the implications this result has for the identification of intracellular O-GlcNAc modifications using MCRs, we then performed a meta-analysis of the potential O-GlcNAcylated proteins identified by different techniques.
32411667	10	10	theme	MCRs	1802:1805	arg1	responsible					1810:1820	responsible	1810:1820	responsible	1810:1820	Together, these data indicate that the selective metabolism of certain MCRs is responsible for S-glycosylation of proteins in the cytosol and nucleus.
32411667	10	10	theme	MCRs	1802:1805	arg1	metabolism					1780:1789	the selective metabolism	1766:1789	the selective metabolism of certain MCRs	1766:1805	Together, these data indicate that the selective metabolism of certain MCRs is responsible for S-glycosylation of proteins in the cytosol and nucleus.
32411667	6	11	theme	cysteine	1243:1250	arg1	residues					1252:1259	cysteine residues	1243:1259	cysteine residues	1243:1259	Additionally, we used isotope targeted glycoproteomics (IsoTaG) proteomics to show that essentially all of the Ac42AzMan labeling is on cysteine residues.
32411667	1	12	theme	different	396:404	arg1	glycoproteins					406:418	different glycoproteins	396:418	different glycoproteins	396:418	Monosaccharide analogs bearing bioorthogonal functionalities, or metabolic chemical reporters (MCRs) of glycosylation, have been used for approximately two decades for the visualization and identification of different glycoproteins.
32411667	10	13	theme	proteins	1845:1852	arg1	S-glycosylation					1826:1840	S-glycosylation	1826:1840	S-glycosylation of proteins in the cytosol and nucleus	1826:1879	Together, these data indicate that the selective metabolism of certain MCRs is responsible for S-glycosylation of proteins in the cytosol and nucleus.
32411667	7	14	theme	O-GlcNAc	1341:1348	arg1	modifications					1350:1362	intracellular O-GlcNAc modifications	1327:1362	intracellular O-GlcNAc modifications using MCRs	1327:1373	Given the implications this result has for the identification of intracellular O-GlcNAc modifications using MCRs, we then performed a meta-analysis of the potential O-GlcNAcylated proteins identified by different techniques.
32411667	9	15	theme	them	1704:1707	arg1	half					1696:1699	half	1696:1699	half of them	1696:1707	Finally, we randomly selected four proteins that had only been identified as O-GlcNAcylated by MCRs and showed that half of them were indeed modified.
32411667	10	16	theme	selective	1770:1778	arg1	responsible					1810:1820	responsible	1810:1820	responsible	1810:1820	Together, these data indicate that the selective metabolism of certain MCRs is responsible for S-glycosylation of proteins in the cytosol and nucleus.
32411667	10	16	theme	selective	1770:1778	arg1	metabolism					1780:1789	the selective metabolism	1766:1789	the selective metabolism of certain MCRs	1766:1805	Together, these data indicate that the selective metabolism of certain MCRs is responsible for S-glycosylation of proteins in the cytosol and nucleus.
32411667	0	17	theme	Reliable	132:139	arg1	Tools					141:145	Reliable Tools	132:145	Reliable Tools for the Identification of Glycoproteins	132:185	O-Acetylated Chemical Reporters of Glycosylation Can Display Metabolism-Dependent Background Labeling of Proteins but Are Generally Reliable Tools for the Identification of Glycoproteins.
32411667	1	18	theme	glycoproteins	406:418	arg1	identification					378:391	identification	378:391	identification	378:391	Monosaccharide analogs bearing bioorthogonal functionalities, or metabolic chemical reporters (MCRs) of glycosylation, have been used for approximately two decades for the visualization and identification of different glycoproteins.
32411667	1	18	theme	glycoproteins	406:418	arg1	visualization					360:372	visualization	360:372	visualization	360:372	Monosaccharide analogs bearing bioorthogonal functionalities, or metabolic chemical reporters (MCRs) of glycosylation, have been used for approximately two decades for the visualization and identification of different glycoproteins.
32411667	10	19	from	proteins	1845:1852	arg1	cytosol					1861:1867	cytosol	1861:1867	cytosol	1861:1867	Together, these data indicate that the selective metabolism of certain MCRs is responsible for S-glycosylation of proteins in the cytosol and nucleus.
32411667	10	19	from	proteins	1845:1852	arg1	nucleus					1873:1879	nucleus	1873:1879	nucleus	1873:1879	Together, these data indicate that the selective metabolism of certain MCRs is responsible for S-glycosylation of proteins in the cytosol and nucleus.
32411667	11	20	theme	complementary	2011:2023	arg1	methods					2025:2031	complementary methods	2011:2031	complementary methods	2011:2031	However, these results also show that MCRs are still good tools for unbiased identification of glycosylated proteins, as long as complementary methods are employed for confirmation.
32411667	5	21	theme	characterized	1043:1055	arg1	reporters					1057:1065	previously characterized reporters	1032:1065	previously characterized reporters of intracellular O-GlcNAc modification	1032:1104	We then characterized Ac42AzMan labeling and found that the vast majority of the labeling occurs on intracellular proteins but that this MCR is not converted to previously characterized reporters of intracellular O-GlcNAc modification.
32411667	6	22	theme	IsoTaG	1163:1168	arg1	proteomics					1171:1180	isotope targeted glycoproteomics (IsoTaG) proteomics	1129:1180	isotope targeted glycoproteomics (IsoTaG) proteomics	1129:1180	Additionally, we used isotope targeted glycoproteomics (IsoTaG) proteomics to show that essentially all of the Ac42AzMan labeling is on cysteine residues.
32411667	5	23	theme	vast	931:934	arg1	majority					936:943	the vast majority	927:943	the vast majority of the labeling	927:959	We then characterized Ac42AzMan labeling and found that the vast majority of the labeling occurs on intracellular proteins but that this MCR is not converted to previously characterized reporters of intracellular O-GlcNAc modification.
32411667	1	24	used	used	317:320	arg2	analogs					203:209	Monosaccharide analogs	188:209	Monosaccharide analogs bearing bioorthogonal functionalities	188:247	Monosaccharide analogs bearing bioorthogonal functionalities, or metabolic chemical reporters (MCRs) of glycosylation, have been used for approximately two decades for the visualization and identification of different glycoproteins.
32411667	1	24	used	used	317:320	arg2	MCRs					283:286	MCRs	283:286	MCRs	283:286	Monosaccharide analogs bearing bioorthogonal functionalities, or metabolic chemical reporters (MCRs) of glycosylation, have been used for approximately two decades for the visualization and identification of different glycoproteins.
32411667	1	24	used	used	317:320	arg2	reporters					272:280	metabolic chemical reporters	253:280	metabolic chemical reporters (MCRs) of glycosylation	253:304	Monosaccharide analogs bearing bioorthogonal functionalities, or metabolic chemical reporters (MCRs) of glycosylation, have been used for approximately two decades for the visualization and identification of different glycoproteins.
32411667	2	25	theme	proteomics	436:445	arg1	analyses					447:454	proteomics analyses	436:454	proteomics analyses	436:454	More recently, proteomics analyses have shown that per-O-acetylated MCRs can directly and chemically react with cysteine residues in lysates and potentially cells, drawing into question the physiological relevance of the labeling.
32411667	0	26	theme	Chemical	13:20	arg1	Reporters					22:30	O-Acetylated Chemical Reporters	0:30	O-Acetylated Chemical Reporters of Glycosylation	0:47	O-Acetylated Chemical Reporters of Glycosylation Can Display Metabolism-Dependent Background Labeling of Proteins but Are Generally Reliable Tools for the Identification of Glycoproteins.
32411667	4	27	theme	cell	817:820	arg1	lysates					822:828	cell lysates	817:828	cell lysates	817:828	However, the levels of background chemical-labeling of cell lysates by both reporters are low and identical.
32411667	1	28	theme	bioorthogonal	219:231	arg1	functionalities					233:247	bioorthogonal functionalities	219:247	bioorthogonal functionalities	219:247	Monosaccharide analogs bearing bioorthogonal functionalities, or metabolic chemical reporters (MCRs) of glycosylation, have been used for approximately two decades for the visualization and identification of different glycoproteins.
32411667	0	29	theme	O-Acetylated	0:11	arg1	Reporters					22:30	O-Acetylated Chemical Reporters	0:30	O-Acetylated Chemical Reporters of Glycosylation	0:47	O-Acetylated Chemical Reporters of Glycosylation Can Display Metabolism-Dependent Background Labeling of Proteins but Are Generally Reliable Tools for the Identification of Glycoproteins.
32411667	11	30	dep	long	2003:2006	arg1	employed					2037:2044	employed	2037:2044	are employed for confirmation	2033:2061	However, these results also show that MCRs are still good tools for unbiased identification of glycosylated proteins, as long as complementary methods are employed for confirmation.
32411667	1	31	gly	glycoproteins	406:418	arg1	glycoproteins					406:418	different glycoproteins	396:418	different glycoproteins	396:418	Monosaccharide analogs bearing bioorthogonal functionalities, or metabolic chemical reporters (MCRs) of glycosylation, have been used for approximately two decades for the visualization and identification of different glycoproteins.
32411667	5	32	theme	intracellular	971:983	arg1	proteins					985:992	intracellular proteins	971:992	intracellular proteins	971:992	We then characterized Ac42AzMan labeling and found that the vast majority of the labeling occurs on intracellular proteins but that this MCR is not converted to previously characterized reporters of intracellular O-GlcNAc modification.
32411667	5	33	theme	Ac42AzMan	893:901	arg1	labeling					903:910	Ac42AzMan labeling	893:910	Ac42AzMan labeling	893:910	We then characterized Ac42AzMan labeling and found that the vast majority of the labeling occurs on intracellular proteins but that this MCR is not converted to previously characterized reporters of intracellular O-GlcNAc modification.
32411667	2	34	theme	physiological	611:623	arg1	relevance					625:633	the physiological relevance	607:633	the physiological relevance of the labeling	607:649	More recently, proteomics analyses have shown that per-O-acetylated MCRs can directly and chemically react with cysteine residues in lysates and potentially cells, drawing into question the physiological relevance of the labeling.
32411667	7	35	theme	modifications	1350:1362	arg1	identification					1309:1322	the identification	1305:1322	the identification of intracellular O-GlcNAc modifications using MCRs	1305:1373	Given the implications this result has for the identification of intracellular O-GlcNAc modifications using MCRs, we then performed a meta-analysis of the potential O-GlcNAcylated proteins identified by different techniques.
32411667	6	36	theme	isotope	1129:1135	arg1	proteomics					1171:1180	isotope targeted glycoproteomics (IsoTaG) proteomics	1129:1180	isotope targeted glycoproteomics (IsoTaG) proteomics	1129:1180	Additionally, we used isotope targeted glycoproteomics (IsoTaG) proteomics to show that essentially all of the Ac42AzMan labeling is on cysteine residues.
32411667	2	37	theme	per-O-acetylated	472:487	arg1	MCRs					489:492	per-O-acetylated MCRs	472:492	per-O-acetylated MCRs	472:492	More recently, proteomics analyses have shown that per-O-acetylated MCRs can directly and chemically react with cysteine residues in lysates and potentially cells, drawing into question the physiological relevance of the labeling.
32411667	1	38	dep	visualization	360:372	arg1	the					356:358	the	356:358	the	356:358	Monosaccharide analogs bearing bioorthogonal functionalities, or metabolic chemical reporters (MCRs) of glycosylation, have been used for approximately two decades for the visualization and identification of different glycoproteins.
32411667	4	39	theme	lysates	822:828	arg1	chemical-labeling					796:812	background chemical-labeling	785:812	background chemical-labeling of cell lysates by both reporters	785:846	However, the levels of background chemical-labeling of cell lysates by both reporters are low and identical.
32411667	6	40	theme	targeted	1137:1144	arg1	proteomics					1171:1180	isotope targeted glycoproteomics (IsoTaG) proteomics	1129:1180	isotope targeted glycoproteomics (IsoTaG) proteomics	1129:1180	Additionally, we used isotope targeted glycoproteomics (IsoTaG) proteomics to show that essentially all of the Ac42AzMan labeling is on cysteine residues.
32411667	2	41	theme	cysteine	533:540	arg1	residues					542:549	cysteine residues	533:549	cysteine residues in lysates and potentially cells	533:582	More recently, proteomics analyses have shown that per-O-acetylated MCRs can directly and chemically react with cysteine residues in lysates and potentially cells, drawing into question the physiological relevance of the labeling.
32411667	2	42	from	residues	542:549	arg1	lysates					554:560	lysates	554:560	lysates	554:560	More recently, proteomics analyses have shown that per-O-acetylated MCRs can directly and chemically react with cysteine residues in lysates and potentially cells, drawing into question the physiological relevance of the labeling.
32411667	2	42	from	residues	542:549	arg1	cells					578:582	cells	578:582	cells	578:582	More recently, proteomics analyses have shown that per-O-acetylated MCRs can directly and chemically react with cysteine residues in lysates and potentially cells, drawing into question the physiological relevance of the labeling.
32411667	7	43	theme	potential	1417:1425	arg1	proteins					1442:1449	the potential O-GlcNAcylated proteins	1413:1449	the potential O-GlcNAcylated proteins identified by different techniques	1413:1484	Given the implications this result has for the identification of intracellular O-GlcNAc modifications using MCRs, we then performed a meta-analysis of the potential O-GlcNAcylated proteins identified by different techniques.
32411667	1	44	theme	metabolic	253:261	arg1	MCRs					283:286	MCRs	283:286	MCRs	283:286	Monosaccharide analogs bearing bioorthogonal functionalities, or metabolic chemical reporters (MCRs) of glycosylation, have been used for approximately two decades for the visualization and identification of different glycoproteins.
32411667	1	44	theme	metabolic	253:261	arg1	reporters					272:280	metabolic chemical reporters	253:280	metabolic chemical reporters (MCRs) of glycosylation	253:304	Monosaccharide analogs bearing bioorthogonal functionalities, or metabolic chemical reporters (MCRs) of glycosylation, have been used for approximately two decades for the visualization and identification of different glycoproteins.
32411667	0	45	theme	Glycosylation	35:47	arg1	Reporters					22:30	O-Acetylated Chemical Reporters	0:30	O-Acetylated Chemical Reporters of Glycosylation	0:47	O-Acetylated Chemical Reporters of Glycosylation Can Display Metabolism-Dependent Background Labeling of Proteins but Are Generally Reliable Tools for the Identification of Glycoproteins.
32411667	11	46	theme	glycosylated	1977:1988	arg1	proteins					1990:1997	glycosylated proteins	1977:1997	glycosylated proteins	1977:1997	However, these results also show that MCRs are still good tools for unbiased identification of glycosylated proteins, as long as complementary methods are employed for confirmation.
32411667	7	47	dep	implications	1272:1283	arg1	has					1297:1299	has	1297:1299	has for the identification of intracellular O-GlcNAc modifications using MCRs	1297:1373	Given the implications this result has for the identification of intracellular O-GlcNAc modifications using MCRs, we then performed a meta-analysis of the potential O-GlcNAcylated proteins identified by different techniques.
32411667	1	48	theme	chemical	263:270	arg1	MCRs					283:286	MCRs	283:286	MCRs	283:286	Monosaccharide analogs bearing bioorthogonal functionalities, or metabolic chemical reporters (MCRs) of glycosylation, have been used for approximately two decades for the visualization and identification of different glycoproteins.
32411667	1	48	theme	chemical	263:270	arg1	reporters					272:280	metabolic chemical reporters	253:280	metabolic chemical reporters (MCRs) of glycosylation	253:304	Monosaccharide analogs bearing bioorthogonal functionalities, or metabolic chemical reporters (MCRs) of glycosylation, have been used for approximately two decades for the visualization and identification of different glycoproteins.
32411667	0	49	theme	Metabolism-Dependent	61:80	arg1	Labeling					93:100	Metabolism-Dependent Background Labeling	61:100	Metabolism-Dependent Background Labeling of Proteins	61:112	O-Acetylated Chemical Reporters of Glycosylation Can Display Metabolism-Dependent Background Labeling of Proteins but Are Generally Reliable Tools for the Identification of Glycoproteins.
32411667	2	50	theme	labeling	642:649	arg1	relevance					625:633	the physiological relevance	607:633	the physiological relevance of the labeling	607:649	More recently, proteomics analyses have shown that per-O-acetylated MCRs can directly and chemically react with cysteine residues in lysates and potentially cells, drawing into question the physiological relevance of the labeling.
32411667	11	51	theme	unbiased	1950:1957	arg1	identification					1959:1972	unbiased identification	1950:1972	unbiased identification of glycosylated proteins	1950:1997	However, these results also show that MCRs are still good tools for unbiased identification of glycosylated proteins, as long as complementary methods are employed for confirmation.
32411667	8	52	theme	proteins	1513:1520	arg1	many					1501:1504	many	1501:1504	many	1501:1504	We found that many of the proteins identified by MCRs have also been found by other methods.
32411667	8	52	theme	proteins	1513:1520	arg1	proteins					1513:1520	the proteins	1509:1520	the proteins identified by MCRs	1509:1539	We found that many of the proteins identified by MCRs have also been found by other methods.
32411667	11	53	gly	glycosylated	1977:1988	arg1	proteins					1990:1997	glycosylated proteins	1977:1997	glycosylated proteins	1977:1997	However, these results also show that MCRs are still good tools for unbiased identification of glycosylated proteins, as long as complementary methods are employed for confirmation.
32411667	6	54	theme	Ac42AzMan	1218:1226	arg1	labeling					1228:1235	the Ac42AzMan labeling	1214:1235	the Ac42AzMan labeling	1214:1235	Additionally, we used isotope targeted glycoproteomics (IsoTaG) proteomics to show that essentially all of the Ac42AzMan labeling is on cysteine residues.
32411667	10	55	gly	S-glycosylation	1826:1840	arg1	proteins					1845:1852	proteins	1845:1852	proteins in the cytosol and nucleus	1845:1879	Together, these data indicate that the selective metabolism of certain MCRs is responsible for S-glycosylation of proteins in the cytosol and nucleus.
32411667	8	56	theme	other	1565:1569	arg1	methods					1571:1577	other methods	1565:1577	other methods	1565:1577	We found that many of the proteins identified by MCRs have also been found by other methods.
32411667	11	57	theme	good	1935:1938	arg1	MCRs					1920:1923	MCRs	1920:1923	MCRs	1920:1923	However, these results also show that MCRs are still good tools for unbiased identification of glycosylated proteins, as long as complementary methods are employed for confirmation.
32411667	11	57	theme	good	1935:1938	arg1	tools					1940:1944	good tools	1935:1944	good tools for unbiased identification of glycosylated proteins	1935:1997	However, these results also show that MCRs are still good tools for unbiased identification of glycosylated proteins, as long as complementary methods are employed for confirmation.
32411667	5	58	theme	modification	1093:1104	arg1	reporters					1057:1065	previously characterized reporters	1032:1065	previously characterized reporters of intracellular O-GlcNAc modification	1032:1104	We then characterized Ac42AzMan labeling and found that the vast majority of the labeling occurs on intracellular proteins but that this MCR is not converted to previously characterized reporters of intracellular O-GlcNAc modification.
32411667	7	59	theme	different	1465:1473	arg1	techniques					1475:1484	different techniques	1465:1484	different techniques	1465:1484	Given the implications this result has for the identification of intracellular O-GlcNAc modifications using MCRs, we then performed a meta-analysis of the potential O-GlcNAcylated proteins identified by different techniques.
32411667	3	60	theme	metabolism-dependent	675:694	arg1	labeling					696:703	robust metabolism-dependent labeling	668:703	robust metabolism-dependent labeling by Ac42AzMan but not the structurally similar Ac44AzGal	668:759	Here, we report robust metabolism-dependent labeling by Ac42AzMan but not the structurally similar Ac44AzGal.
32411667	4	61	theme	chemical-labeling	796:812	arg1	levels					775:780	the levels	771:780	the levels of background chemical-labeling of cell lysates by both reporters	771:846	However, the levels of background chemical-labeling of cell lysates by both reporters are low and identical.
32411667	4	61	theme	chemical-labeling	796:812	arg1	low					852:854	low	852:854	low	852:854	However, the levels of background chemical-labeling of cell lysates by both reporters are low and identical.
32411667	10	62	from	S-glycosylation	1826:1840	arg1	cytosol					1861:1867	cytosol	1861:1867	cytosol	1861:1867	Together, these data indicate that the selective metabolism of certain MCRs is responsible for S-glycosylation of proteins in the cytosol and nucleus.
32411667	10	62	from	S-glycosylation	1826:1840	arg1	nucleus					1873:1879	nucleus	1873:1879	nucleus	1873:1879	Together, these data indicate that the selective metabolism of certain MCRs is responsible for S-glycosylation of proteins in the cytosol and nucleus.
32411667	5	63	theme	intracellular	1070:1082	arg1	modification					1093:1104	intracellular O-GlcNAc modification	1070:1104	intracellular O-GlcNAc modification	1070:1104	We then characterized Ac42AzMan labeling and found that the vast majority of the labeling occurs on intracellular proteins but that this MCR is not converted to previously characterized reporters of intracellular O-GlcNAc modification.
32411667	4	64	theme	background	785:794	arg1	chemical-labeling					796:812	background chemical-labeling	785:812	background chemical-labeling of cell lysates by both reporters	785:846	However, the levels of background chemical-labeling of cell lysates by both reporters are low and identical.
32411667	5	65	theme	O-GlcNAc	1084:1091	arg1	modification					1093:1104	intracellular O-GlcNAc modification	1070:1104	intracellular O-GlcNAc modification	1070:1104	We then characterized Ac42AzMan labeling and found that the vast majority of the labeling occurs on intracellular proteins but that this MCR is not converted to previously characterized reporters of intracellular O-GlcNAc modification.
32411667	6	66	theme	glycoproteomics	1146:1160	arg1	proteomics					1171:1180	isotope targeted glycoproteomics (IsoTaG) proteomics	1129:1180	isotope targeted glycoproteomics (IsoTaG) proteomics	1129:1180	Additionally, we used isotope targeted glycoproteomics (IsoTaG) proteomics to show that essentially all of the Ac42AzMan labeling is on cysteine residues.
32411667	5	67	theme	labeling	952:959	arg1	majority					936:943	the vast majority	927:943	the vast majority of the labeling	927:959	We then characterized Ac42AzMan labeling and found that the vast majority of the labeling occurs on intracellular proteins but that this MCR is not converted to previously characterized reporters of intracellular O-GlcNAc modification.
32411667	7	68	theme	proteins	1442:1449	arg1	meta-analysis					1396:1408	a meta-analysis	1394:1408	a meta-analysis of the potential O-GlcNAcylated proteins identified by different techniques	1394:1484	Given the implications this result has for the identification of intracellular O-GlcNAc modifications using MCRs, we then performed a meta-analysis of the potential O-GlcNAcylated proteins identified by different techniques.
32411667	0	69	theme	Background	82:91	arg1	Labeling					93:100	Metabolism-Dependent Background Labeling	61:100	Metabolism-Dependent Background Labeling of Proteins	61:112	O-Acetylated Chemical Reporters of Glycosylation Can Display Metabolism-Dependent Background Labeling of Proteins but Are Generally Reliable Tools for the Identification of Glycoproteins.
32411667	3	70	theme	robust	668:673	arg1	labeling					696:703	robust metabolism-dependent labeling	668:703	robust metabolism-dependent labeling by Ac42AzMan but not the structurally similar Ac44AzGal	668:759	Here, we report robust metabolism-dependent labeling by Ac42AzMan but not the structurally similar Ac44AzGal.
32411667	10	71	from	cytosol	1861:1867	arg1	S-glycosylation					1826:1840	S-glycosylation	1826:1840	S-glycosylation of proteins in the cytosol and nucleus	1826:1879	Together, these data indicate that the selective metabolism of certain MCRs is responsible for S-glycosylation of proteins in the cytosol and nucleus.
32411667	10	72	theme	certain	1794:1800	arg1	MCRs					1802:1805	certain MCRs	1794:1805	certain MCRs	1794:1805	Together, these data indicate that the selective metabolism of certain MCRs is responsible for S-glycosylation of proteins in the cytosol and nucleus.
29771506	0	0	theme	O-GlcNAc	101:108	arg1	Transferase					110:120	O-GlcNAc Transferase	101:120	O-GlcNAc Transferase	101:120	The Metabolic Chemical Reporter 6-Azido-6-deoxy-glucose Further Reveals the Substrate Promiscuity of O-GlcNAc Transferase and Catalyzes the Discovery of Intracellular Protein Modification by O-Glucose.
29771506	2	1	theme	metabolism	533:542	arg1	investigation					507:519	the investigation	503:519	the investigation of cellular metabolism	503:542	More recently, however, they have begun to see utility for the investigation of cellular metabolism and the tolerance of biosynthetic enzymes and glycosyltransferases to different sugars.
29771506	5	2	with	consistent	933:942	arg1	modifications					958:970	O-GlcNAc modifications	949:970	O-GlcNAc modifications	949:970	Notably, the pattern of this labeling was consistent with O-GlcNAc modifications, suggesting that the enzyme O-GlcNAc transferase is quite promiscuous for its donor sugar substrates.
29771506	2	3	theme	different	614:622	arg1	sugars					624:629	different sugars	614:629	different sugars	614:629	More recently, however, they have begun to see utility for the investigation of cellular metabolism and the tolerance of biosynthetic enzymes and glycosyltransferases to different sugars.
29771506	7	4	from	modification	1468:1479	arg1	factor					1494:1499	host cell factor	1484:1499	host cell factor	1484:1499	Finally, we use proteomics to first identify several bona fide 6AzGlc-modifications in mammalian cells and then an endogenous O-glucose modification on host cell factor.
29771506	2	5	theme	cellular	524:531	arg1	metabolism					533:542	cellular metabolism	524:542	cellular metabolism	524:542	More recently, however, they have begun to see utility for the investigation of cellular metabolism and the tolerance of biosynthetic enzymes and glycosyltransferases to different sugars.
29771506	4	6	with	treatment	764:772	arg1	version					820:826	the per- O-acetylated version	798:826	the per- O-acetylated version of 6AzGlc	798:836	We show that treatment of mammalian cells with the per- O-acetylated version of 6AzGlc results in robust labeling of a variety of proteins.
29771506	2	7	theme	enzymes	578:584	arg1	utility					491:497	utility	491:497	utility for the investigation of cellular metabolism	491:542	More recently, however, they have begun to see utility for the investigation of cellular metabolism and the tolerance of biosynthetic enzymes and glycosyltransferases to different sugars.
29771506	2	7	theme	enzymes	578:584	arg1	tolerance					552:560	the tolerance	548:560	the tolerance of biosynthetic enzymes and glycosyltransferases to different sugars	548:629	More recently, however, they have begun to see utility for the investigation of cellular metabolism and the tolerance of biosynthetic enzymes and glycosyltransferases to different sugars.
29771506	0	8	theme	Transferase	110:120	arg1	Promiscuity					86:96	the Substrate Promiscuity	72:96	the Substrate Promiscuity of O-GlcNAc Transferase	72:120	The Metabolic Chemical Reporter 6-Azido-6-deoxy-glucose Further Reveals the Substrate Promiscuity of O-GlcNAc Transferase and Catalyzes the Discovery of Intracellular Protein Modification by O-Glucose.
29771506	1	9	used	used	338:341	arg2	reporters					221:229	Metabolic chemical reporters	202:229	Metabolic chemical reporters of glycosylation in combination with bioorthogonal reactions	202:290	Metabolic chemical reporters of glycosylation in combination with bioorthogonal reactions have been known for two decades and have been used by many different research laboratories for the identification and visualization of glycoconjugates.
29771506	7	10	theme	host	1484:1487	arg1	factor					1494:1499	host cell factor	1484:1499	host cell factor	1484:1499	Finally, we use proteomics to first identify several bona fide 6AzGlc-modifications in mammalian cells and then an endogenous O-glucose modification on host cell factor.
29771506	4	11	theme	O-acetylated	807:818	arg1	version					820:826	the per- O-acetylated version	798:826	the per- O-acetylated version of 6AzGlc	798:836	We show that treatment of mammalian cells with the per- O-acetylated version of 6AzGlc results in robust labeling of a variety of proteins.
29771506	8	12	theme	widespread	1700:1709	arg1	modification					1678:1689	intracellular O-glucose modification	1654:1689	intracellular O-glucose modification	1654:1689	These results support the conclusion that OGT can endogenously modify proteins with both N-acetyl-glucosamine and glucose, raising the possibility that intracellular O-glucose modification may be a widespread modification under certain conditions or in particular tissues.
29771506	8	12	theme	widespread	1700:1709	arg1	modification					1711:1722	a widespread modification	1698:1722	a widespread modification	1698:1722	These results support the conclusion that OGT can endogenously modify proteins with both N-acetyl-glucosamine and glucose, raising the possibility that intracellular O-glucose modification may be a widespread modification under certain conditions or in particular tissues.
29771506	7	13	theme	endogenous	1447:1456	arg1	modification					1468:1479	an endogenous O-glucose modification	1444:1479	an endogenous O-glucose modification on host cell factor	1444:1499	Finally, we use proteomics to first identify several bona fide 6AzGlc-modifications in mammalian cells and then an endogenous O-glucose modification on host cell factor.
29771506	4	14	theme	6AzGlc	831:836	arg1	version					820:826	the per- O-acetylated version	798:826	the per- O-acetylated version of 6AzGlc	798:836	We show that treatment of mammalian cells with the per- O-acetylated version of 6AzGlc results in robust labeling of a variety of proteins.
29771506	1	15	theme	Metabolic	202:210	arg1	reporters					221:229	Metabolic chemical reporters	202:229	Metabolic chemical reporters of glycosylation in combination with bioorthogonal reactions	202:290	Metabolic chemical reporters of glycosylation in combination with bioorthogonal reactions have been known for two decades and have been used by many different research laboratories for the identification and visualization of glycoconjugates.
29771506	7	16	theme	cell	1489:1492	arg1	factor					1494:1499	host cell factor	1484:1499	host cell factor	1484:1499	Finally, we use proteomics to first identify several bona fide 6AzGlc-modifications in mammalian cells and then an endogenous O-glucose modification on host cell factor.
29771506	4	17	theme	proteins	881:888	arg1	proteins					881:888	proteins	881:888	proteins	881:888	We show that treatment of mammalian cells with the per- O-acetylated version of 6AzGlc results in robust labeling of a variety of proteins.
29771506	4	17	theme	proteins	881:888	arg1	variety					870:876	a variety	868:876	a variety of proteins	868:888	We show that treatment of mammalian cells with the per- O-acetylated version of 6AzGlc results in robust labeling of a variety of proteins.
29771506	8	18	theme	intracellular	1654:1666	arg1	modification					1678:1689	intracellular O-glucose modification	1654:1689	intracellular O-glucose modification	1654:1689	These results support the conclusion that OGT can endogenously modify proteins with both N-acetyl-glucosamine and glucose, raising the possibility that intracellular O-glucose modification may be a widespread modification under certain conditions or in particular tissues.
29771506	8	18	theme	intracellular	1654:1666	arg1	modification					1711:1722	a widespread modification	1698:1722	a widespread modification	1698:1722	These results support the conclusion that OGT can endogenously modify proteins with both N-acetyl-glucosamine and glucose, raising the possibility that intracellular O-glucose modification may be a widespread modification under certain conditions or in particular tissues.
29771506	1	19	theme	chemical	212:219	arg1	reporters					221:229	Metabolic chemical reporters	202:229	Metabolic chemical reporters of glycosylation in combination with bioorthogonal reactions	202:290	Metabolic chemical reporters of glycosylation in combination with bioorthogonal reactions have been known for two decades and have been used by many different research laboratories for the identification and visualization of glycoconjugates.
29771506	0	20	theme	Metabolic	4:12	arg1	6-Azido-6-deoxy-glucose					32:54	The Metabolic Chemical Reporter 6-Azido-6-deoxy-glucose	0:54	The Metabolic Chemical Reporter 6-Azido-6-deoxy-glucose	0:54	The Metabolic Chemical Reporter 6-Azido-6-deoxy-glucose Further Reveals the Substrate Promiscuity of O-GlcNAc Transferase and Catalyzes the Discovery of Intracellular Protein Modification by O-Glucose.
29771506	1	21	theme	glycoconjugates	427:441	arg1	visualization					410:422	visualization	410:422	visualization	410:422	Metabolic chemical reporters of glycosylation in combination with bioorthogonal reactions have been known for two decades and have been used by many different research laboratories for the identification and visualization of glycoconjugates.
29771506	1	21	theme	glycoconjugates	427:441	arg1	identification					391:404	identification	391:404	identification	391:404	Metabolic chemical reporters of glycosylation in combination with bioorthogonal reactions have been known for two decades and have been used by many different research laboratories for the identification and visualization of glycoconjugates.
29771506	6	22	theme	donor	1211:1215	arg1	sugar					1217:1221	the UDP-6AzGlc donor sugar	1196:1221	the UDP-6AzGlc donor sugar	1196:1221	To confirm this possibility, we show that 6AzGlc-treatment results in the labeling of known O-GlcNAcylated proteins, that the UDP-6AzGlc donor sugar is indeed produced in living cells, and that recombinant OGT will accept UDP-6AzGlc as a substrate in vitro.
29771506	2	23	theme	glycosyltransferases	590:609	arg1	utility					491:497	utility	491:497	utility for the investigation of cellular metabolism	491:542	More recently, however, they have begun to see utility for the investigation of cellular metabolism and the tolerance of biosynthetic enzymes and glycosyltransferases to different sugars.
29771506	2	23	theme	glycosyltransferases	590:609	arg1	tolerance					552:560	the tolerance	548:560	the tolerance of biosynthetic enzymes and glycosyltransferases to different sugars	548:629	More recently, however, they have begun to see utility for the investigation of cellular metabolism and the tolerance of biosynthetic enzymes and glycosyltransferases to different sugars.
29771506	6	24	theme	living	1245:1250	arg1	cells					1252:1256	living cells	1245:1256	living cells	1245:1256	To confirm this possibility, we show that 6AzGlc-treatment results in the labeling of known O-GlcNAcylated proteins, that the UDP-6AzGlc donor sugar is indeed produced in living cells, and that recombinant OGT will accept UDP-6AzGlc as a substrate in vitro.
29771506	4	25	theme	cells	787:791	arg1	treatment					764:772	treatment	764:772	treatment of mammalian cells with the per- O-acetylated version of 6AzGlc	764:836	We show that treatment of mammalian cells with the per- O-acetylated version of 6AzGlc results in robust labeling of a variety of proteins.
29771506	7	26	from	6AzGlc-modifications	1395:1414	arg1	cells					1429:1433	mammalian cells	1419:1433	mammalian cells	1419:1433	Finally, we use proteomics to first identify several bona fide 6AzGlc-modifications in mammalian cells and then an endogenous O-glucose modification on host cell factor.
29771506	0	27	theme	Reporter	23:30	arg1	6-Azido-6-deoxy-glucose					32:54	The Metabolic Chemical Reporter 6-Azido-6-deoxy-glucose	0:54	The Metabolic Chemical Reporter 6-Azido-6-deoxy-glucose	0:54	The Metabolic Chemical Reporter 6-Azido-6-deoxy-glucose Further Reveals the Substrate Promiscuity of O-GlcNAc Transferase and Catalyzes the Discovery of Intracellular Protein Modification by O-Glucose.
29771506	1	28	dep	identification	391:404	arg1	the					387:389	the	387:389	the	387:389	Metabolic chemical reporters of glycosylation in combination with bioorthogonal reactions have been known for two decades and have been used by many different research laboratories for the identification and visualization of glycoconjugates.
29771506	1	29	with	combination	251:261	arg1	reactions					282:290	bioorthogonal reactions	268:290	bioorthogonal reactions	268:290	Metabolic chemical reporters of glycosylation in combination with bioorthogonal reactions have been known for two decades and have been used by many different research laboratories for the identification and visualization of glycoconjugates.
29771506	7	30	theme	several	1377:1383	arg1	6AzGlc-modifications					1395:1414	several bona fide 6AzGlc-modifications	1377:1414	several bona fide 6AzGlc-modifications in mammalian cells	1377:1433	Finally, we use proteomics to first identify several bona fide 6AzGlc-modifications in mammalian cells and then an endogenous O-glucose modification on host cell factor.
29771506	4	31	theme	per-	802:805	arg1	version					820:826	the per- O-acetylated version	798:826	the per- O-acetylated version of 6AzGlc	798:836	We show that treatment of mammalian cells with the per- O-acetylated version of 6AzGlc results in robust labeling of a variety of proteins.
29771506	7	32	dep	use	1344:1346	arg1	modification					1468:1479	an endogenous O-glucose modification	1444:1479	an endogenous O-glucose modification on host cell factor	1444:1499	Finally, we use proteomics to first identify several bona fide 6AzGlc-modifications in mammalian cells and then an endogenous O-glucose modification on host cell factor.
29771506	7	32	dep	use	1344:1346	arg1	identify					1368:1375	identify	1368:1375	to first identify several bona fide 6AzGlc-modifications in mammalian cells	1359:1433	Finally, we use proteomics to first identify several bona fide 6AzGlc-modifications in mammalian cells and then an endogenous O-glucose modification on host cell factor.
29771506	1	33	theme	glycosylation	234:246	arg1	reporters					221:229	Metabolic chemical reporters	202:229	Metabolic chemical reporters of glycosylation in combination with bioorthogonal reactions	202:290	Metabolic chemical reporters of glycosylation in combination with bioorthogonal reactions have been known for two decades and have been used by many different research laboratories for the identification and visualization of glycoconjugates.
29771506	0	34	theme	Chemical	14:21	arg1	6-Azido-6-deoxy-glucose					32:54	The Metabolic Chemical Reporter 6-Azido-6-deoxy-glucose	0:54	The Metabolic Chemical Reporter 6-Azido-6-deoxy-glucose	0:54	The Metabolic Chemical Reporter 6-Azido-6-deoxy-glucose Further Reveals the Substrate Promiscuity of O-GlcNAc Transferase and Catalyzes the Discovery of Intracellular Protein Modification by O-Glucose.
29771506	7	35	theme	O-glucose	1458:1466	arg1	modification					1468:1479	an endogenous O-glucose modification	1444:1479	an endogenous O-glucose modification on host cell factor	1444:1499	Finally, we use proteomics to first identify several bona fide 6AzGlc-modifications in mammalian cells and then an endogenous O-glucose modification on host cell factor.
29771506	3	36	theme	metabolic	689:697	arg1	6-azido-6-deoxy-glucose					717:739	the metabolic chemical reporter 6-azido-6-deoxy-glucose	685:739	the metabolic chemical reporter 6-azido-6-deoxy-glucose (6AzGlc)	685:748	Here, we take this concept one step further by using the metabolic chemical reporter 6-azido-6-deoxy-glucose (6AzGlc).
29771506	3	36	theme	metabolic	689:697	arg1	6AzGlc					742:747	6AzGlc	742:747	6AzGlc	742:747	Here, we take this concept one step further by using the metabolic chemical reporter 6-azido-6-deoxy-glucose (6AzGlc).
29771506	5	37	theme	O-GlcNAc	1000:1007	arg1	transferase					1009:1019	the enzyme O-GlcNAc transferase	989:1019	the enzyme O-GlcNAc transferase	989:1019	Notably, the pattern of this labeling was consistent with O-GlcNAc modifications, suggesting that the enzyme O-GlcNAc transferase is quite promiscuous for its donor sugar substrates.
29771506	5	37	theme	O-GlcNAc	1000:1007	arg1	promiscuous					1030:1040	promiscuous	1030:1040	promiscuous	1030:1040	Notably, the pattern of this labeling was consistent with O-GlcNAc modifications, suggesting that the enzyme O-GlcNAc transferase is quite promiscuous for its donor sugar substrates.
29771506	6	38	theme	UDP-6AzGlc	1200:1209	arg1	sugar					1217:1221	the UDP-6AzGlc donor sugar	1196:1221	the UDP-6AzGlc donor sugar	1196:1221	To confirm this possibility, we show that 6AzGlc-treatment results in the labeling of known O-GlcNAcylated proteins, that the UDP-6AzGlc donor sugar is indeed produced in living cells, and that recombinant OGT will accept UDP-6AzGlc as a substrate in vitro.
29771506	5	39	theme	sugar	1056:1060	arg1	substrates					1062:1071	its donor sugar substrates	1046:1071	its donor sugar substrates	1046:1071	Notably, the pattern of this labeling was consistent with O-GlcNAc modifications, suggesting that the enzyme O-GlcNAc transferase is quite promiscuous for its donor sugar substrates.
29771506	0	40	theme	Protein	167:173	arg1	Modification					175:186	Intracellular Protein Modification	153:186	Intracellular Protein Modification by O-Glucose	153:199	The Metabolic Chemical Reporter 6-Azido-6-deoxy-glucose Further Reveals the Substrate Promiscuity of O-GlcNAc Transferase and Catalyzes the Discovery of Intracellular Protein Modification by O-Glucose.
29771506	3	41	theme	chemical	699:706	arg1	6-azido-6-deoxy-glucose					717:739	the metabolic chemical reporter 6-azido-6-deoxy-glucose	685:739	the metabolic chemical reporter 6-azido-6-deoxy-glucose (6AzGlc)	685:748	Here, we take this concept one step further by using the metabolic chemical reporter 6-azido-6-deoxy-glucose (6AzGlc).
29771506	3	41	theme	chemical	699:706	arg1	6AzGlc					742:747	6AzGlc	742:747	6AzGlc	742:747	Here, we take this concept one step further by using the metabolic chemical reporter 6-azido-6-deoxy-glucose (6AzGlc).
29771506	7	42	theme	mammalian	1419:1427	arg1	cells					1429:1433	mammalian cells	1419:1433	mammalian cells	1419:1433	Finally, we use proteomics to first identify several bona fide 6AzGlc-modifications in mammalian cells and then an endogenous O-glucose modification on host cell factor.
29771506	7	43	dep	bona	1385:1388	arg1	fide					1390:1393	fide	1390:1393	fide	1390:1393	Finally, we use proteomics to first identify several bona fide 6AzGlc-modifications in mammalian cells and then an endogenous O-glucose modification on host cell factor.
29771506	0	44	theme	Intracellular	153:165	arg1	Modification					175:186	Intracellular Protein Modification	153:186	Intracellular Protein Modification by O-Glucose	153:199	The Metabolic Chemical Reporter 6-Azido-6-deoxy-glucose Further Reveals the Substrate Promiscuity of O-GlcNAc Transferase and Catalyzes the Discovery of Intracellular Protein Modification by O-Glucose.
29771506	6	45	theme	recombinant	1268:1278	arg1	OGT					1280:1282	recombinant OGT	1268:1282	recombinant OGT	1268:1282	To confirm this possibility, we show that 6AzGlc-treatment results in the labeling of known O-GlcNAcylated proteins, that the UDP-6AzGlc donor sugar is indeed produced in living cells, and that recombinant OGT will accept UDP-6AzGlc as a substrate in vitro.
29771506	1	46	theme	many	346:349	arg1	laboratories					370:381	many different research laboratories	346:381	many different research laboratories for the identification and visualization of glycoconjugates	346:441	Metabolic chemical reporters of glycosylation in combination with bioorthogonal reactions have been known for two decades and have been used by many different research laboratories for the identification and visualization of glycoconjugates.
29771506	8	47	from	modification	1711:1722	arg1	tissues					1766:1772	particular tissues	1755:1772	particular tissues	1755:1772	These results support the conclusion that OGT can endogenously modify proteins with both N-acetyl-glucosamine and glucose, raising the possibility that intracellular O-glucose modification may be a widespread modification under certain conditions or in particular tissues.
29771506	5	48	theme	O-GlcNAc	949:956	arg1	modifications					958:970	O-GlcNAc modifications	949:970	O-GlcNAc modifications	949:970	Notably, the pattern of this labeling was consistent with O-GlcNAc modifications, suggesting that the enzyme O-GlcNAc transferase is quite promiscuous for its donor sugar substrates.
29771506	1	49	theme	different	351:359	arg1	laboratories					370:381	many different research laboratories	346:381	many different research laboratories for the identification and visualization of glycoconjugates	346:441	Metabolic chemical reporters of glycosylation in combination with bioorthogonal reactions have been known for two decades and have been used by many different research laboratories for the identification and visualization of glycoconjugates.
29771506	0	50	theme	Modification	175:186	arg1	Discovery					140:148	the Discovery	136:148	the Discovery of Intracellular Protein Modification by O-Glucose	136:199	The Metabolic Chemical Reporter 6-Azido-6-deoxy-glucose Further Reveals the Substrate Promiscuity of O-GlcNAc Transferase and Catalyzes the Discovery of Intracellular Protein Modification by O-Glucose.
29771506	4	51	theme	variety	870:876	arg1	labeling					856:863	robust labeling	849:863	robust labeling of a variety of proteins	849:888	We show that treatment of mammalian cells with the per- O-acetylated version of 6AzGlc results in robust labeling of a variety of proteins.
29771506	6	52	theme	proteins	1181:1188	arg1	labeling					1148:1155	the labeling	1144:1155	the labeling of known O-GlcNAcylated proteins	1144:1188	To confirm this possibility, we show that 6AzGlc-treatment results in the labeling of known O-GlcNAcylated proteins, that the UDP-6AzGlc donor sugar is indeed produced in living cells, and that recombinant OGT will accept UDP-6AzGlc as a substrate in vitro.
29771506	8	53	theme	certain	1730:1736	arg1	conditions					1738:1747	certain conditions	1730:1747	certain conditions	1730:1747	These results support the conclusion that OGT can endogenously modify proteins with both N-acetyl-glucosamine and glucose, raising the possibility that intracellular O-glucose modification may be a widespread modification under certain conditions or in particular tissues.
29771506	1	54	theme	research	361:368	arg1	laboratories					370:381	many different research laboratories	346:381	many different research laboratories for the identification and visualization of glycoconjugates	346:441	Metabolic chemical reporters of glycosylation in combination with bioorthogonal reactions have been known for two decades and have been used by many different research laboratories for the identification and visualization of glycoconjugates.
29771506	7	55	theme	bona	1385:1388	arg1	6AzGlc-modifications					1395:1414	several bona fide 6AzGlc-modifications	1377:1414	several bona fide 6AzGlc-modifications in mammalian cells	1377:1433	Finally, we use proteomics to first identify several bona fide 6AzGlc-modifications in mammalian cells and then an endogenous O-glucose modification on host cell factor.
29771506	4	56	theme	mammalian	777:785	arg1	cells					787:791	mammalian cells	777:791	mammalian cells	777:791	We show that treatment of mammalian cells with the per- O-acetylated version of 6AzGlc results in robust labeling of a variety of proteins.
29771506	5	57	theme	enzyme	993:998	arg1	transferase					1009:1019	the enzyme O-GlcNAc transferase	989:1019	the enzyme O-GlcNAc transferase	989:1019	Notably, the pattern of this labeling was consistent with O-GlcNAc modifications, suggesting that the enzyme O-GlcNAc transferase is quite promiscuous for its donor sugar substrates.
29771506	5	57	theme	enzyme	993:998	arg1	promiscuous					1030:1040	promiscuous	1030:1040	promiscuous	1030:1040	Notably, the pattern of this labeling was consistent with O-GlcNAc modifications, suggesting that the enzyme O-GlcNAc transferase is quite promiscuous for its donor sugar substrates.
29771506	1	58	theme	bioorthogonal	268:280	arg1	reactions					282:290	bioorthogonal reactions	268:290	bioorthogonal reactions	268:290	Metabolic chemical reporters of glycosylation in combination with bioorthogonal reactions have been known for two decades and have been used by many different research laboratories for the identification and visualization of glycoconjugates.
29771506	3	59	theme	reporter	708:715	arg1	6-azido-6-deoxy-glucose					717:739	the metabolic chemical reporter 6-azido-6-deoxy-glucose	685:739	the metabolic chemical reporter 6-azido-6-deoxy-glucose (6AzGlc)	685:748	Here, we take this concept one step further by using the metabolic chemical reporter 6-azido-6-deoxy-glucose (6AzGlc).
29771506	3	59	theme	reporter	708:715	arg1	6AzGlc					742:747	6AzGlc	742:747	6AzGlc	742:747	Here, we take this concept one step further by using the metabolic chemical reporter 6-azido-6-deoxy-glucose (6AzGlc).
29771506	1	60	from	reporters	221:229	arg1	combination					251:261	combination	251:261	combination with bioorthogonal reactions	251:290	Metabolic chemical reporters of glycosylation in combination with bioorthogonal reactions have been known for two decades and have been used by many different research laboratories for the identification and visualization of glycoconjugates.
29771506	6	61	theme	known	1160:1164	arg1	proteins					1181:1188	known O-GlcNAcylated proteins	1160:1188	known O-GlcNAcylated proteins	1160:1188	To confirm this possibility, we show that 6AzGlc-treatment results in the labeling of known O-GlcNAcylated proteins, that the UDP-6AzGlc donor sugar is indeed produced in living cells, and that recombinant OGT will accept UDP-6AzGlc as a substrate in vitro.
29771506	6	62	theme	O-GlcNAcylated	1166:1179	arg1	proteins					1181:1188	known O-GlcNAcylated proteins	1160:1188	known O-GlcNAcylated proteins	1160:1188	To confirm this possibility, we show that 6AzGlc-treatment results in the labeling of known O-GlcNAcylated proteins, that the UDP-6AzGlc donor sugar is indeed produced in living cells, and that recombinant OGT will accept UDP-6AzGlc as a substrate in vitro.
29771506	8	63	with	proteins	1572:1579	arg1	glucose					1616:1622	glucose	1616:1622	glucose	1616:1622	These results support the conclusion that OGT can endogenously modify proteins with both N-acetyl-glucosamine and glucose, raising the possibility that intracellular O-glucose modification may be a widespread modification under certain conditions or in particular tissues.
29771506	8	63	with	proteins	1572:1579	arg1	N-acetyl-glucosamine					1591:1610	N-acetyl-glucosamine	1591:1610	N-acetyl-glucosamine	1591:1610	These results support the conclusion that OGT can endogenously modify proteins with both N-acetyl-glucosamine and glucose, raising the possibility that intracellular O-glucose modification may be a widespread modification under certain conditions or in particular tissues.
29771506	5	64	theme	donor	1050:1054	arg1	substrates					1062:1071	its donor sugar substrates	1046:1071	its donor sugar substrates	1046:1071	Notably, the pattern of this labeling was consistent with O-GlcNAc modifications, suggesting that the enzyme O-GlcNAc transferase is quite promiscuous for its donor sugar substrates.
29771506	5	65	theme	labeling	920:927	arg1	consistent					933:942	consistent	933:942	consistent	933:942	Notably, the pattern of this labeling was consistent with O-GlcNAc modifications, suggesting that the enzyme O-GlcNAc transferase is quite promiscuous for its donor sugar substrates.
29771506	5	65	theme	labeling	920:927	arg1	pattern					904:910	the pattern	900:910	the pattern of this labeling	900:927	Notably, the pattern of this labeling was consistent with O-GlcNAc modifications, suggesting that the enzyme O-GlcNAc transferase is quite promiscuous for its donor sugar substrates.
29771506	0	66	theme	Substrate	76:84	arg1	Promiscuity					86:96	the Substrate Promiscuity	72:96	the Substrate Promiscuity of O-GlcNAc Transferase	72:120	The Metabolic Chemical Reporter 6-Azido-6-deoxy-glucose Further Reveals the Substrate Promiscuity of O-GlcNAc Transferase and Catalyzes the Discovery of Intracellular Protein Modification by O-Glucose.
29771506	4	67	theme	robust	849:854	arg1	labeling					856:863	robust labeling	849:863	robust labeling of a variety of proteins	849:888	We show that treatment of mammalian cells with the per- O-acetylated version of 6AzGlc results in robust labeling of a variety of proteins.
29771506	8	68	theme	O-glucose	1668:1676	arg1	modification					1678:1689	intracellular O-glucose modification	1654:1689	intracellular O-glucose modification	1654:1689	These results support the conclusion that OGT can endogenously modify proteins with both N-acetyl-glucosamine and glucose, raising the possibility that intracellular O-glucose modification may be a widespread modification under certain conditions or in particular tissues.
29771506	8	68	theme	O-glucose	1668:1676	arg1	modification					1711:1722	a widespread modification	1698:1722	a widespread modification	1698:1722	These results support the conclusion that OGT can endogenously modify proteins with both N-acetyl-glucosamine and glucose, raising the possibility that intracellular O-glucose modification may be a widespread modification under certain conditions or in particular tissues.
29771506	8	69	theme	particular	1755:1764	arg1	tissues					1766:1772	particular tissues	1755:1772	particular tissues	1755:1772	These results support the conclusion that OGT can endogenously modify proteins with both N-acetyl-glucosamine and glucose, raising the possibility that intracellular O-glucose modification may be a widespread modification under certain conditions or in particular tissues.
29771506	2	70	theme	biosynthetic	565:576	arg1	enzymes					578:584	biosynthetic enzymes	565:584	biosynthetic enzymes	565:584	More recently, however, they have begun to see utility for the investigation of cellular metabolism and the tolerance of biosynthetic enzymes and glycosyltransferases to different sugars.
16732326	5	0	theme	representative	1226:1239	arg1	spectra					1218:1224	42 MS spectra	1212:1224	42 MS spectra representative of hnRNPH1, calreticulin and hnRNPA2/B1 in a peak explorer, which reveals a cytogenetic-specific PTM of beta-O-linked N-acetyl glucosamine (O-GlcNAc) of hnRNPH1 in AML patients with 11q23 translocation, an acetylation of calreticulin in t(8;21) translocation and methylation of hnRNPA2/B1 in patients with translocations of t(8;21) and inv(16)	1212:1583	Further, we analysed 42 MS spectra representative of hnRNPH1, calreticulin and hnRNPA2/B1 in a peak explorer, which reveals a cytogenetic-specific PTM of beta-O-linked N-acetyl glucosamine (O-GlcNAc) of hnRNPH1 in AML patients with 11q23 translocation, an acetylation of calreticulin in t(8;21) translocation and methylation of hnRNPA2/B1 in patients with translocations of t(8;21) and inv(16).
16732326	3	1	theme	spectrometry	796:807	arg1	electrophoresis					712:726	two-dimensional gel electrophoresis	692:726	two-dimensional gel electrophoresis	692:726	We performed this study using 42 AML patients diagnosed for various cytogenetic abnormalities based on two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionization time of flight mass spectrometry (MS) and MSMS tandem MS. We could identify significant differences in the proteome and PTM of peptides, later confirmed by other methods, between cytogenetic groups.
16732326	3	1	theme	spectrometry	796:807	arg1	MS.					830:832	MSMS tandem MS.	818:832	MSMS tandem MS.	818:832	We performed this study using 42 AML patients diagnosed for various cytogenetic abnormalities based on two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionization time of flight mass spectrometry (MS) and MSMS tandem MS. We could identify significant differences in the proteome and PTM of peptides, later confirmed by other methods, between cytogenetic groups.
16732326	3	1	theme	spectrometry	796:807	arg1	time					776:779	matrix-assisted laser desorption/ionization time	732:779	matrix-assisted laser desorption/ionization time of flight mass spectrometry (MS)	732:812	We performed this study using 42 AML patients diagnosed for various cytogenetic abnormalities based on two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionization time of flight mass spectrometry (MS) and MSMS tandem MS. We could identify significant differences in the proteome and PTM of peptides, later confirmed by other methods, between cytogenetic groups.
16732326	5	2	from	hnRNPH1	1244:1250	arg1	explorer					1291:1298	a peak explorer	1284:1298	a peak explorer	1284:1298	Further, we analysed 42 MS spectra representative of hnRNPH1, calreticulin and hnRNPA2/B1 in a peak explorer, which reveals a cytogenetic-specific PTM of beta-O-linked N-acetyl glucosamine (O-GlcNAc) of hnRNPH1 in AML patients with 11q23 translocation, an acetylation of calreticulin in t(8;21) translocation and methylation of hnRNPA2/B1 in patients with translocations of t(8;21) and inv(16).
16732326	1	3	theme	myeloid	166:172	arg1	AML					185:187	AML	185:187	AML	185:187	Acute myeloid leukaemia (AML) is characterized by specific cytogenetic aberrations that are strong determinants of prognostic outcome and therapeutic response.
16732326	1	3	theme	myeloid	166:172	arg1	leukaemia					174:182	Acute myeloid leukaemia	160:182	Acute myeloid leukaemia (AML)	160:188	Acute myeloid leukaemia (AML) is characterized by specific cytogenetic aberrations that are strong determinants of prognostic outcome and therapeutic response.
16732326	3	4	theme	cytogenetic	955:965	arg1	groups					967:972	cytogenetic groups	955:972	cytogenetic groups	955:972	We performed this study using 42 AML patients diagnosed for various cytogenetic abnormalities based on two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionization time of flight mass spectrometry (MS) and MSMS tandem MS. We could identify significant differences in the proteome and PTM of peptides, later confirmed by other methods, between cytogenetic groups.
16732326	3	5	theme	peptides	903:910	arg1	proteome					883:890	proteome	883:890	proteome	883:890	We performed this study using 42 AML patients diagnosed for various cytogenetic abnormalities based on two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionization time of flight mass spectrometry (MS) and MSMS tandem MS. We could identify significant differences in the proteome and PTM of peptides, later confirmed by other methods, between cytogenetic groups.
16732326	3	5	theme	peptides	903:910	arg1	PTM					896:898	PTM	896:898	PTM	896:898	We performed this study using 42 AML patients diagnosed for various cytogenetic abnormalities based on two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionization time of flight mass spectrometry (MS) and MSMS tandem MS. We could identify significant differences in the proteome and PTM of peptides, later confirmed by other methods, between cytogenetic groups.
16732326	2	6	theme	interaction	524:534	arg1	pathways					536:543	protein interaction pathways	516:543	protein interaction pathways	516:543	Because the pathological outcome of AML patients with cytogenetic abnormalities differs considerably, we hypothesized that their proteome may also differ specifically in their expression pattern, protein interaction pathways and post-translational modifications (PTM).
16732326	6	7	theme	new	1612:1614	arg1	thinking					1616:1623	a new thinking	1610:1623	a new thinking about AML pathogenesis	1610:1646	This report may lead to a new thinking about AML pathogenesis, as differences at PTM level could be used to distinguish different subtypes of AML.
16732326	2	8	theme	cytogenetic	374:384	arg1	abnormalities					386:398	cytogenetic abnormalities	374:398	cytogenetic abnormalities	374:398	Because the pathological outcome of AML patients with cytogenetic abnormalities differs considerably, we hypothesized that their proteome may also differ specifically in their expression pattern, protein interaction pathways and post-translational modifications (PTM).
16732326	5	9	theme	MS	1215:1216	arg1	spectra					1218:1224	42 MS spectra	1212:1224	42 MS spectra representative of hnRNPH1, calreticulin and hnRNPA2/B1 in a peak explorer, which reveals a cytogenetic-specific PTM of beta-O-linked N-acetyl glucosamine (O-GlcNAc) of hnRNPH1 in AML patients with 11q23 translocation, an acetylation of calreticulin in t(8;21) translocation and methylation of hnRNPA2/B1 in patients with translocations of t(8;21) and inv(16)	1212:1583	Further, we analysed 42 MS spectra representative of hnRNPH1, calreticulin and hnRNPA2/B1 in a peak explorer, which reveals a cytogenetic-specific PTM of beta-O-linked N-acetyl glucosamine (O-GlcNAc) of hnRNPH1 in AML patients with 11q23 translocation, an acetylation of calreticulin in t(8;21) translocation and methylation of hnRNPA2/B1 in patients with translocations of t(8;21) and inv(16).
16732326	3	10	theme	flight	784:789	arg1	MS					810:811	MS	810:811	MS	810:811	We performed this study using 42 AML patients diagnosed for various cytogenetic abnormalities based on two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionization time of flight mass spectrometry (MS) and MSMS tandem MS. We could identify significant differences in the proteome and PTM of peptides, later confirmed by other methods, between cytogenetic groups.
16732326	3	10	theme	flight	784:789	arg1	spectrometry					796:807	flight mass spectrometry	784:807	flight mass spectrometry (MS)	784:812	We performed this study using 42 AML patients diagnosed for various cytogenetic abnormalities based on two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionization time of flight mass spectrometry (MS) and MSMS tandem MS. We could identify significant differences in the proteome and PTM of peptides, later confirmed by other methods, between cytogenetic groups.
16732326	3	11	theme	AML	622:624	arg1	patients					626:633	42 AML patients	619:633	42 AML patients diagnosed for various cytogenetic abnormalities based on two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionization time of flight mass spectrometry (MS) and MSMS tandem MS. We could identify significant differences in the proteome and PTM of peptides, later confirmed by other methods, between cytogenetic groups	619:972	We performed this study using 42 AML patients diagnosed for various cytogenetic abnormalities based on two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionization time of flight mass spectrometry (MS) and MSMS tandem MS. We could identify significant differences in the proteome and PTM of peptides, later confirmed by other methods, between cytogenetic groups.
16732326	5	12	from	hnRNPA2/B1	1270:1279	arg1	explorer					1291:1298	a peak explorer	1284:1298	a peak explorer	1284:1298	Further, we analysed 42 MS spectra representative of hnRNPH1, calreticulin and hnRNPA2/B1 in a peak explorer, which reveals a cytogenetic-specific PTM of beta-O-linked N-acetyl glucosamine (O-GlcNAc) of hnRNPH1 in AML patients with 11q23 translocation, an acetylation of calreticulin in t(8;21) translocation and methylation of hnRNPA2/B1 in patients with translocations of t(8;21) and inv(16).
16732326	1	13	theme	prognostic	275:284	arg1	outcome					286:292	prognostic outcome	275:292	prognostic outcome	275:292	Acute myeloid leukaemia (AML) is characterized by specific cytogenetic aberrations that are strong determinants of prognostic outcome and therapeutic response.
16732326	5	14	theme	t	1565:1565	arg1	translocations					1547:1560	translocations	1547:1560	translocations of t(8;21) and inv(16)	1547:1583	Further, we analysed 42 MS spectra representative of hnRNPH1, calreticulin and hnRNPA2/B1 in a peak explorer, which reveals a cytogenetic-specific PTM of beta-O-linked N-acetyl glucosamine (O-GlcNAc) of hnRNPH1 in AML patients with 11q23 translocation, an acetylation of calreticulin in t(8;21) translocation and methylation of hnRNPA2/B1 in patients with translocations of t(8;21) and inv(16).
16732326	3	15	from	differences	864:874	arg1	proteome					883:890	proteome	883:890	proteome	883:890	We performed this study using 42 AML patients diagnosed for various cytogenetic abnormalities based on two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionization time of flight mass spectrometry (MS) and MSMS tandem MS. We could identify significant differences in the proteome and PTM of peptides, later confirmed by other methods, between cytogenetic groups.
16732326	3	15	from	differences	864:874	arg1	PTM					896:898	PTM	896:898	PTM	896:898	We performed this study using 42 AML patients diagnosed for various cytogenetic abnormalities based on two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionization time of flight mass spectrometry (MS) and MSMS tandem MS. We could identify significant differences in the proteome and PTM of peptides, later confirmed by other methods, between cytogenetic groups.
16732326	1	16	theme	outcome	286:292	arg1	aberrations					231:241	specific cytogenetic aberrations	210:241	specific cytogenetic aberrations that are strong determinants of prognostic outcome and therapeutic response	210:317	Acute myeloid leukaemia (AML) is characterized by specific cytogenetic aberrations that are strong determinants of prognostic outcome and therapeutic response.
16732326	1	16	theme	outcome	286:292	arg1	determinants					259:270	strong determinants	252:270	strong determinants of prognostic outcome and therapeutic response	252:317	Acute myeloid leukaemia (AML) is characterized by specific cytogenetic aberrations that are strong determinants of prognostic outcome and therapeutic response.
16732326	4	17	theme	regulating	1052:1061	arg1	networks					1063:1070	major regulating networks	1046:1070	major regulating networks	1046:1070	The interactome analysis based on computational bioinformatics reveals major regulating networks: MAPK8 and MYC for complex aberrant karyotype, TP53 for t(8;21), TP53-MYC-PRKAC for 11q23 and JUN and MYC for Inv(16).
16732326	5	18	from	methylation	1504:1514	arg1	patients					1533:1540	patients	1533:1540	patients with translocations of t(8;21) and inv(16)	1533:1583	Further, we analysed 42 MS spectra representative of hnRNPH1, calreticulin and hnRNPA2/B1 in a peak explorer, which reveals a cytogenetic-specific PTM of beta-O-linked N-acetyl glucosamine (O-GlcNAc) of hnRNPH1 in AML patients with 11q23 translocation, an acetylation of calreticulin in t(8;21) translocation and methylation of hnRNPA2/B1 in patients with translocations of t(8;21) and inv(16).
16732326	5	18	from	methylation	1504:1514	arg1	translocation					1486:1498	t(8;21) translocation	1478:1498	t(8;21) translocation	1478:1498	Further, we analysed 42 MS spectra representative of hnRNPH1, calreticulin and hnRNPA2/B1 in a peak explorer, which reveals a cytogenetic-specific PTM of beta-O-linked N-acetyl glucosamine (O-GlcNAc) of hnRNPH1 in AML patients with 11q23 translocation, an acetylation of calreticulin in t(8;21) translocation and methylation of hnRNPA2/B1 in patients with translocations of t(8;21) and inv(16).
16732326	5	19	theme	calreticulin	1462:1473	arg1	translocation					1429:1441	11q23 translocation	1423:1441	11q23 translocation	1423:1441	Further, we analysed 42 MS spectra representative of hnRNPH1, calreticulin and hnRNPA2/B1 in a peak explorer, which reveals a cytogenetic-specific PTM of beta-O-linked N-acetyl glucosamine (O-GlcNAc) of hnRNPH1 in AML patients with 11q23 translocation, an acetylation of calreticulin in t(8;21) translocation and methylation of hnRNPA2/B1 in patients with translocations of t(8;21) and inv(16).
16732326	5	19	theme	calreticulin	1462:1473	arg1	acetylation					1447:1457	an acetylation	1444:1457	an acetylation of calreticulin in t(8;21) translocation	1444:1498	Further, we analysed 42 MS spectra representative of hnRNPH1, calreticulin and hnRNPA2/B1 in a peak explorer, which reveals a cytogenetic-specific PTM of beta-O-linked N-acetyl glucosamine (O-GlcNAc) of hnRNPH1 in AML patients with 11q23 translocation, an acetylation of calreticulin in t(8;21) translocation and methylation of hnRNPA2/B1 in patients with translocations of t(8;21) and inv(16).
16732326	5	19	theme	calreticulin	1462:1473	arg1	methylation					1504:1514	methylation	1504:1514	methylation	1504:1514	Further, we analysed 42 MS spectra representative of hnRNPH1, calreticulin and hnRNPA2/B1 in a peak explorer, which reveals a cytogenetic-specific PTM of beta-O-linked N-acetyl glucosamine (O-GlcNAc) of hnRNPH1 in AML patients with 11q23 translocation, an acetylation of calreticulin in t(8;21) translocation and methylation of hnRNPA2/B1 in patients with translocations of t(8;21) and inv(16).
16732326	3	20	dep	time	776:779	arg1	identify					843:850	identify	843:850	could identify significant differences in the proteome and PTM of peptides, later confirmed by other methods, between cytogenetic groups	837:972	We performed this study using 42 AML patients diagnosed for various cytogenetic abnormalities based on two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionization time of flight mass spectrometry (MS) and MSMS tandem MS. We could identify significant differences in the proteome and PTM of peptides, later confirmed by other methods, between cytogenetic groups.
16732326	5	21	theme	beta-O-linked	1345:1357	arg1	O-GlcNAc					1381:1388	O-GlcNAc	1381:1388	O-GlcNAc	1381:1388	Further, we analysed 42 MS spectra representative of hnRNPH1, calreticulin and hnRNPA2/B1 in a peak explorer, which reveals a cytogenetic-specific PTM of beta-O-linked N-acetyl glucosamine (O-GlcNAc) of hnRNPH1 in AML patients with 11q23 translocation, an acetylation of calreticulin in t(8;21) translocation and methylation of hnRNPA2/B1 in patients with translocations of t(8;21) and inv(16).
16732326	5	21	theme	beta-O-linked	1345:1357	arg1	glucosamine					1368:1378	beta-O-linked N-acetyl glucosamine	1345:1378	beta-O-linked N-acetyl glucosamine (O-GlcNAc)	1345:1389	Further, we analysed 42 MS spectra representative of hnRNPH1, calreticulin and hnRNPA2/B1 in a peak explorer, which reveals a cytogenetic-specific PTM of beta-O-linked N-acetyl glucosamine (O-GlcNAc) of hnRNPH1 in AML patients with 11q23 translocation, an acetylation of calreticulin in t(8;21) translocation and methylation of hnRNPA2/B1 in patients with translocations of t(8;21) and inv(16).
16732326	6	22	used	used	1686:1689	arg2	level					1671:1675	PTM level	1667:1675	PTM level	1667:1675	This report may lead to a new thinking about AML pathogenesis, as differences at PTM level could be used to distinguish different subtypes of AML.
16732326	6	22	used	used	1686:1689	arg2	differences					1652:1662	differences	1652:1662	differences at PTM level	1652:1675	This report may lead to a new thinking about AML pathogenesis, as differences at PTM level could be used to distinguish different subtypes of AML.
16732326	2	23	theme	expression	496:505	arg1	pattern					507:513	their expression pattern	490:513	their expression pattern	490:513	Because the pathological outcome of AML patients with cytogenetic abnormalities differs considerably, we hypothesized that their proteome may also differ specifically in their expression pattern, protein interaction pathways and post-translational modifications (PTM).
16732326	5	24	theme	inv	1577:1579	arg1	translocations					1547:1560	translocations	1547:1560	translocations of t(8;21) and inv(16)	1547:1583	Further, we analysed 42 MS spectra representative of hnRNPH1, calreticulin and hnRNPA2/B1 in a peak explorer, which reveals a cytogenetic-specific PTM of beta-O-linked N-acetyl glucosamine (O-GlcNAc) of hnRNPH1 in AML patients with 11q23 translocation, an acetylation of calreticulin in t(8;21) translocation and methylation of hnRNPA2/B1 in patients with translocations of t(8;21) and inv(16).
16732326	5	25	theme	t	1478:1478	arg1	translocation					1486:1498	t(8;21) translocation	1478:1498	t(8;21) translocation	1478:1498	Further, we analysed 42 MS spectra representative of hnRNPH1, calreticulin and hnRNPA2/B1 in a peak explorer, which reveals a cytogenetic-specific PTM of beta-O-linked N-acetyl glucosamine (O-GlcNAc) of hnRNPH1 in AML patients with 11q23 translocation, an acetylation of calreticulin in t(8;21) translocation and methylation of hnRNPA2/B1 in patients with translocations of t(8;21) and inv(16).
16732326	4	26	theme	major	1046:1050	arg1	networks					1063:1070	major regulating networks	1046:1070	major regulating networks	1046:1070	The interactome analysis based on computational bioinformatics reveals major regulating networks: MAPK8 and MYC for complex aberrant karyotype, TP53 for t(8;21), TP53-MYC-PRKAC for 11q23 and JUN and MYC for Inv(16).
16732326	3	27	dep	proteome	883:890	arg1	the					879:881	the	879:881	the	879:881	We performed this study using 42 AML patients diagnosed for various cytogenetic abnormalities based on two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionization time of flight mass spectrometry (MS) and MSMS tandem MS. We could identify significant differences in the proteome and PTM of peptides, later confirmed by other methods, between cytogenetic groups.
16732326	6	28	theme	AML	1728:1730	arg1	subtypes					1716:1723	different subtypes	1706:1723	different subtypes of AML	1706:1730	This report may lead to a new thinking about AML pathogenesis, as differences at PTM level could be used to distinguish different subtypes of AML.
16732326	5	29	theme	peak	1286:1289	arg1	explorer					1291:1298	a peak explorer	1284:1298	a peak explorer	1284:1298	Further, we analysed 42 MS spectra representative of hnRNPH1, calreticulin and hnRNPA2/B1 in a peak explorer, which reveals a cytogenetic-specific PTM of beta-O-linked N-acetyl glucosamine (O-GlcNAc) of hnRNPH1 in AML patients with 11q23 translocation, an acetylation of calreticulin in t(8;21) translocation and methylation of hnRNPA2/B1 in patients with translocations of t(8;21) and inv(16).
16732326	5	30	link	beta-O-linked	1345:1357	arg1	O-GlcNAc					1381:1388	O-GlcNAc	1381:1388	O-GlcNAc	1381:1388	Further, we analysed 42 MS spectra representative of hnRNPH1, calreticulin and hnRNPA2/B1 in a peak explorer, which reveals a cytogenetic-specific PTM of beta-O-linked N-acetyl glucosamine (O-GlcNAc) of hnRNPH1 in AML patients with 11q23 translocation, an acetylation of calreticulin in t(8;21) translocation and methylation of hnRNPA2/B1 in patients with translocations of t(8;21) and inv(16).
16732326	5	30	link	beta-O-linked	1345:1357	arg1	glucosamine					1368:1378	beta-O-linked N-acetyl glucosamine	1345:1378	beta-O-linked N-acetyl glucosamine (O-GlcNAc)	1345:1389	Further, we analysed 42 MS spectra representative of hnRNPH1, calreticulin and hnRNPA2/B1 in a peak explorer, which reveals a cytogenetic-specific PTM of beta-O-linked N-acetyl glucosamine (O-GlcNAc) of hnRNPH1 in AML patients with 11q23 translocation, an acetylation of calreticulin in t(8;21) translocation and methylation of hnRNPA2/B1 in patients with translocations of t(8;21) and inv(16).
16732326	5	31	with	patients	1409:1416	arg1	translocation					1429:1441	11q23 translocation	1423:1441	11q23 translocation	1423:1441	Further, we analysed 42 MS spectra representative of hnRNPH1, calreticulin and hnRNPA2/B1 in a peak explorer, which reveals a cytogenetic-specific PTM of beta-O-linked N-acetyl glucosamine (O-GlcNAc) of hnRNPH1 in AML patients with 11q23 translocation, an acetylation of calreticulin in t(8;21) translocation and methylation of hnRNPA2/B1 in patients with translocations of t(8;21) and inv(16).
16732326	5	31	with	patients	1409:1416	arg1	acetylation					1447:1457	an acetylation	1444:1457	an acetylation of calreticulin in t(8;21) translocation	1444:1498	Further, we analysed 42 MS spectra representative of hnRNPH1, calreticulin and hnRNPA2/B1 in a peak explorer, which reveals a cytogenetic-specific PTM of beta-O-linked N-acetyl glucosamine (O-GlcNAc) of hnRNPH1 in AML patients with 11q23 translocation, an acetylation of calreticulin in t(8;21) translocation and methylation of hnRNPA2/B1 in patients with translocations of t(8;21) and inv(16).
16732326	5	31	with	patients	1409:1416	arg1	methylation					1504:1514	methylation	1504:1514	methylation	1504:1514	Further, we analysed 42 MS spectra representative of hnRNPH1, calreticulin and hnRNPA2/B1 in a peak explorer, which reveals a cytogenetic-specific PTM of beta-O-linked N-acetyl glucosamine (O-GlcNAc) of hnRNPH1 in AML patients with 11q23 translocation, an acetylation of calreticulin in t(8;21) translocation and methylation of hnRNPA2/B1 in patients with translocations of t(8;21) and inv(16).
16732326	6	32	from	level	1671:1675	arg1	differences					1652:1662	differences	1652:1662	differences at PTM level	1652:1675	This report may lead to a new thinking about AML pathogenesis, as differences at PTM level could be used to distinguish different subtypes of AML.
16732326	5	33	theme	glucosamine	1368:1378	arg1	PTM					1338:1340	a cytogenetic-specific PTM	1315:1340	a cytogenetic-specific PTM of beta-O-linked N-acetyl glucosamine (O-GlcNAc) of hnRNPH1	1315:1400	Further, we analysed 42 MS spectra representative of hnRNPH1, calreticulin and hnRNPA2/B1 in a peak explorer, which reveals a cytogenetic-specific PTM of beta-O-linked N-acetyl glucosamine (O-GlcNAc) of hnRNPH1 in AML patients with 11q23 translocation, an acetylation of calreticulin in t(8;21) translocation and methylation of hnRNPA2/B1 in patients with translocations of t(8;21) and inv(16).
16732326	5	34	with	patients	1533:1540	arg1	translocations					1547:1560	translocations	1547:1560	translocations of t(8;21) and inv(16)	1547:1583	Further, we analysed 42 MS spectra representative of hnRNPH1, calreticulin and hnRNPA2/B1 in a peak explorer, which reveals a cytogenetic-specific PTM of beta-O-linked N-acetyl glucosamine (O-GlcNAc) of hnRNPH1 in AML patients with 11q23 translocation, an acetylation of calreticulin in t(8;21) translocation and methylation of hnRNPA2/B1 in patients with translocations of t(8;21) and inv(16).
16732326	5	35	theme	hnRNPA2/B1	1270:1279	arg1	representative					1226:1239	representative	1226:1239	representative	1226:1239	Further, we analysed 42 MS spectra representative of hnRNPH1, calreticulin and hnRNPA2/B1 in a peak explorer, which reveals a cytogenetic-specific PTM of beta-O-linked N-acetyl glucosamine (O-GlcNAc) of hnRNPH1 in AML patients with 11q23 translocation, an acetylation of calreticulin in t(8;21) translocation and methylation of hnRNPA2/B1 in patients with translocations of t(8;21) and inv(16).
16732326	2	36	theme	pathological	332:343	arg1	outcome					345:351	the pathological outcome	328:351	the pathological outcome of AML patients with cytogenetic abnormalities	328:398	Because the pathological outcome of AML patients with cytogenetic abnormalities differs considerably, we hypothesized that their proteome may also differ specifically in their expression pattern, protein interaction pathways and post-translational modifications (PTM).
16732326	0	37	theme	myeloid	20:26	arg1	leukaemia					28:36	acute myeloid leukaemia	14:36	acute myeloid leukaemia	14:36	Proteomics of acute myeloid leukaemia: Cytogenetic risk groups differ specifically in their proteome, interactome and post-translational protein modifications.
16732326	1	38	theme	therapeutic	298:308	arg1	response					310:317	therapeutic response	298:317	therapeutic response	298:317	Acute myeloid leukaemia (AML) is characterized by specific cytogenetic aberrations that are strong determinants of prognostic outcome and therapeutic response.
16732326	0	39	theme	post-translational	118:135	arg1	modifications					145:157	post-translational protein modifications	118:157	post-translational protein modifications	118:157	Proteomics of acute myeloid leukaemia: Cytogenetic risk groups differ specifically in their proteome, interactome and post-translational protein modifications.
16732326	0	40	theme	acute	14:18	arg1	leukaemia					28:36	acute myeloid leukaemia	14:36	acute myeloid leukaemia	14:36	Proteomics of acute myeloid leukaemia: Cytogenetic risk groups differ specifically in their proteome, interactome and post-translational protein modifications.
16732326	1	41	theme	response	310:317	arg1	aberrations					231:241	specific cytogenetic aberrations	210:241	specific cytogenetic aberrations that are strong determinants of prognostic outcome and therapeutic response	210:317	Acute myeloid leukaemia (AML) is characterized by specific cytogenetic aberrations that are strong determinants of prognostic outcome and therapeutic response.
16732326	1	41	theme	response	310:317	arg1	determinants					259:270	strong determinants	252:270	strong determinants of prognostic outcome and therapeutic response	252:317	Acute myeloid leukaemia (AML) is characterized by specific cytogenetic aberrations that are strong determinants of prognostic outcome and therapeutic response.
16732326	5	42	from	acetylation	1447:1457	arg1	patients					1533:1540	patients	1533:1540	patients with translocations of t(8;21) and inv(16)	1533:1583	Further, we analysed 42 MS spectra representative of hnRNPH1, calreticulin and hnRNPA2/B1 in a peak explorer, which reveals a cytogenetic-specific PTM of beta-O-linked N-acetyl glucosamine (O-GlcNAc) of hnRNPH1 in AML patients with 11q23 translocation, an acetylation of calreticulin in t(8;21) translocation and methylation of hnRNPA2/B1 in patients with translocations of t(8;21) and inv(16).
16732326	5	42	from	acetylation	1447:1457	arg1	translocation					1486:1498	t(8;21) translocation	1478:1498	t(8;21) translocation	1478:1498	Further, we analysed 42 MS spectra representative of hnRNPH1, calreticulin and hnRNPA2/B1 in a peak explorer, which reveals a cytogenetic-specific PTM of beta-O-linked N-acetyl glucosamine (O-GlcNAc) of hnRNPH1 in AML patients with 11q23 translocation, an acetylation of calreticulin in t(8;21) translocation and methylation of hnRNPA2/B1 in patients with translocations of t(8;21) and inv(16).
16732326	5	43	theme	cytogenetic-specific	1317:1336	arg1	PTM					1338:1340	a cytogenetic-specific PTM	1315:1340	a cytogenetic-specific PTM of beta-O-linked N-acetyl glucosamine (O-GlcNAc) of hnRNPH1	1315:1400	Further, we analysed 42 MS spectra representative of hnRNPH1, calreticulin and hnRNPA2/B1 in a peak explorer, which reveals a cytogenetic-specific PTM of beta-O-linked N-acetyl glucosamine (O-GlcNAc) of hnRNPH1 in AML patients with 11q23 translocation, an acetylation of calreticulin in t(8;21) translocation and methylation of hnRNPA2/B1 in patients with translocations of t(8;21) and inv(16).
16732326	2	44	theme	protein	516:522	arg1	pathways					536:543	protein interaction pathways	516:543	protein interaction pathways	516:543	Because the pathological outcome of AML patients with cytogenetic abnormalities differs considerably, we hypothesized that their proteome may also differ specifically in their expression pattern, protein interaction pathways and post-translational modifications (PTM).
16732326	3	45	theme	tandem	823:828	arg1	MS.					830:832	MSMS tandem MS.	818:832	MSMS tandem MS.	818:832	We performed this study using 42 AML patients diagnosed for various cytogenetic abnormalities based on two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionization time of flight mass spectrometry (MS) and MSMS tandem MS. We could identify significant differences in the proteome and PTM of peptides, later confirmed by other methods, between cytogenetic groups.
16732326	4	46	theme	computational	1009:1021	arg1	bioinformatics					1023:1036	computational bioinformatics	1009:1036	computational bioinformatics	1009:1036	The interactome analysis based on computational bioinformatics reveals major regulating networks: MAPK8 and MYC for complex aberrant karyotype, TP53 for t(8;21), TP53-MYC-PRKAC for 11q23 and JUN and MYC for Inv(16).
16732326	6	47	theme	AML	1631:1633	arg1	pathogenesis					1635:1646	AML pathogenesis	1631:1646	AML pathogenesis	1631:1646	This report may lead to a new thinking about AML pathogenesis, as differences at PTM level could be used to distinguish different subtypes of AML.
16732326	1	48	theme	specific	210:217	arg1	aberrations					231:241	specific cytogenetic aberrations	210:241	specific cytogenetic aberrations that are strong determinants of prognostic outcome and therapeutic response	210:317	Acute myeloid leukaemia (AML) is characterized by specific cytogenetic aberrations that are strong determinants of prognostic outcome and therapeutic response.
16732326	1	48	theme	specific	210:217	arg1	determinants					259:270	strong determinants	252:270	strong determinants of prognostic outcome and therapeutic response	252:317	Acute myeloid leukaemia (AML) is characterized by specific cytogenetic aberrations that are strong determinants of prognostic outcome and therapeutic response.
16732326	0	49	theme	leukaemia	28:36	arg1	Proteomics					0:9	Proteomics	0:9	Proteomics of acute myeloid leukaemia: Cytogenetic risk groups differ specifically in their proteome, interactome and post-translational protein modifications.	0:158	Proteomics of acute myeloid leukaemia: Cytogenetic risk groups differ specifically in their proteome, interactome and post-translational protein modifications.
16732326	3	50	theme	significant	852:862	arg1	differences					864:874	significant differences	852:874	significant differences in the proteome and PTM of peptides, later confirmed by other methods, between cytogenetic groups	852:972	We performed this study using 42 AML patients diagnosed for various cytogenetic abnormalities based on two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionization time of flight mass spectrometry (MS) and MSMS tandem MS. We could identify significant differences in the proteome and PTM of peptides, later confirmed by other methods, between cytogenetic groups.
16732326	0	51	theme	protein	137:143	arg1	modifications					145:157	post-translational protein modifications	118:157	post-translational protein modifications	118:157	Proteomics of acute myeloid leukaemia: Cytogenetic risk groups differ specifically in their proteome, interactome and post-translational protein modifications.
16732326	3	52	theme	two-dimensional	692:706	arg1	electrophoresis					712:726	two-dimensional gel electrophoresis	692:726	two-dimensional gel electrophoresis	692:726	We performed this study using 42 AML patients diagnosed for various cytogenetic abnormalities based on two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionization time of flight mass spectrometry (MS) and MSMS tandem MS. We could identify significant differences in the proteome and PTM of peptides, later confirmed by other methods, between cytogenetic groups.
16732326	3	53	theme	various	649:655	arg1	abnormalities					669:681	various cytogenetic abnormalities	649:681	various cytogenetic abnormalities based on two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionization time of flight mass spectrometry (MS) and MSMS tandem MS. We could identify significant differences in the proteome and PTM of peptides, later confirmed by other methods, between cytogenetic groups	649:972	We performed this study using 42 AML patients diagnosed for various cytogenetic abnormalities based on two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionization time of flight mass spectrometry (MS) and MSMS tandem MS. We could identify significant differences in the proteome and PTM of peptides, later confirmed by other methods, between cytogenetic groups.
16732326	5	54	theme	hnRNPH1	1394:1400	arg1	PTM					1338:1340	a cytogenetic-specific PTM	1315:1340	a cytogenetic-specific PTM of beta-O-linked N-acetyl glucosamine (O-GlcNAc) of hnRNPH1	1315:1400	Further, we analysed 42 MS spectra representative of hnRNPH1, calreticulin and hnRNPA2/B1 in a peak explorer, which reveals a cytogenetic-specific PTM of beta-O-linked N-acetyl glucosamine (O-GlcNAc) of hnRNPH1 in AML patients with 11q23 translocation, an acetylation of calreticulin in t(8;21) translocation and methylation of hnRNPA2/B1 in patients with translocations of t(8;21) and inv(16).
16732326	1	55	theme	cytogenetic	219:229	arg1	aberrations					231:241	specific cytogenetic aberrations	210:241	specific cytogenetic aberrations that are strong determinants of prognostic outcome and therapeutic response	210:317	Acute myeloid leukaemia (AML) is characterized by specific cytogenetic aberrations that are strong determinants of prognostic outcome and therapeutic response.
16732326	1	55	theme	cytogenetic	219:229	arg1	determinants					259:270	strong determinants	252:270	strong determinants of prognostic outcome and therapeutic response	252:317	Acute myeloid leukaemia (AML) is characterized by specific cytogenetic aberrations that are strong determinants of prognostic outcome and therapeutic response.
16732326	0	56	theme	risk	51:54	arg1	groups					56:61	Cytogenetic risk groups	39:61	Cytogenetic risk groups	39:61	Proteomics of acute myeloid leukaemia: Cytogenetic risk groups differ specifically in their proteome, interactome and post-translational protein modifications.
16732326	6	57	theme	different	1706:1714	arg1	subtypes					1716:1723	different subtypes	1706:1723	different subtypes of AML	1706:1730	This report may lead to a new thinking about AML pathogenesis, as differences at PTM level could be used to distinguish different subtypes of AML.
16732326	2	58	with	patients	360:367	arg1	abnormalities					386:398	cytogenetic abnormalities	374:398	cytogenetic abnormalities	374:398	Because the pathological outcome of AML patients with cytogenetic abnormalities differs considerably, we hypothesized that their proteome may also differ specifically in their expression pattern, protein interaction pathways and post-translational modifications (PTM).
16732326	5	59	theme	calreticulin	1253:1264	arg1	representative					1226:1239	representative	1226:1239	representative	1226:1239	Further, we analysed 42 MS spectra representative of hnRNPH1, calreticulin and hnRNPA2/B1 in a peak explorer, which reveals a cytogenetic-specific PTM of beta-O-linked N-acetyl glucosamine (O-GlcNAc) of hnRNPH1 in AML patients with 11q23 translocation, an acetylation of calreticulin in t(8;21) translocation and methylation of hnRNPA2/B1 in patients with translocations of t(8;21) and inv(16).
16732326	0	60	theme	Cytogenetic	39:49	arg1	groups					56:61	Cytogenetic risk groups	39:61	Cytogenetic risk groups	39:61	Proteomics of acute myeloid leukaemia: Cytogenetic risk groups differ specifically in their proteome, interactome and post-translational protein modifications.
16732326	6	61	theme	PTM	1667:1669	arg1	level					1671:1675	PTM level	1667:1675	PTM level	1667:1675	This report may lead to a new thinking about AML pathogenesis, as differences at PTM level could be used to distinguish different subtypes of AML.
16732326	5	62	from	calreticulin	1253:1264	arg1	explorer					1291:1298	a peak explorer	1284:1298	a peak explorer	1284:1298	Further, we analysed 42 MS spectra representative of hnRNPH1, calreticulin and hnRNPA2/B1 in a peak explorer, which reveals a cytogenetic-specific PTM of beta-O-linked N-acetyl glucosamine (O-GlcNAc) of hnRNPH1 in AML patients with 11q23 translocation, an acetylation of calreticulin in t(8;21) translocation and methylation of hnRNPA2/B1 in patients with translocations of t(8;21) and inv(16).
16732326	3	63	theme	gel	708:710	arg1	electrophoresis					712:726	two-dimensional gel electrophoresis	692:726	two-dimensional gel electrophoresis	692:726	We performed this study using 42 AML patients diagnosed for various cytogenetic abnormalities based on two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionization time of flight mass spectrometry (MS) and MSMS tandem MS. We could identify significant differences in the proteome and PTM of peptides, later confirmed by other methods, between cytogenetic groups.
16732326	5	64	theme	AML	1405:1407	arg1	patients					1409:1416	AML patients	1405:1416	AML patients with 11q23 translocation, an acetylation of calreticulin in t(8;21) translocation and methylation of hnRNPA2/B1 in patients with translocations of t(8;21) and inv(16)	1405:1583	Further, we analysed 42 MS spectra representative of hnRNPH1, calreticulin and hnRNPA2/B1 in a peak explorer, which reveals a cytogenetic-specific PTM of beta-O-linked N-acetyl glucosamine (O-GlcNAc) of hnRNPH1 in AML patients with 11q23 translocation, an acetylation of calreticulin in t(8;21) translocation and methylation of hnRNPA2/B1 in patients with translocations of t(8;21) and inv(16).
16732326	2	65	theme	patients	360:367	arg1	outcome					345:351	the pathological outcome	328:351	the pathological outcome of AML patients with cytogenetic abnormalities	328:398	Because the pathological outcome of AML patients with cytogenetic abnormalities differs considerably, we hypothesized that their proteome may also differ specifically in their expression pattern, protein interaction pathways and post-translational modifications (PTM).
16732326	4	66	theme	complex	1091:1097	arg1	karyotype					1108:1116	complex aberrant karyotype	1091:1116	complex aberrant karyotype	1091:1116	The interactome analysis based on computational bioinformatics reveals major regulating networks: MAPK8 and MYC for complex aberrant karyotype, TP53 for t(8;21), TP53-MYC-PRKAC for 11q23 and JUN and MYC for Inv(16).
16732326	5	67	theme	hnRNPH1	1244:1250	arg1	representative					1226:1239	representative	1226:1239	representative	1226:1239	Further, we analysed 42 MS spectra representative of hnRNPH1, calreticulin and hnRNPA2/B1 in a peak explorer, which reveals a cytogenetic-specific PTM of beta-O-linked N-acetyl glucosamine (O-GlcNAc) of hnRNPH1 in AML patients with 11q23 translocation, an acetylation of calreticulin in t(8;21) translocation and methylation of hnRNPA2/B1 in patients with translocations of t(8;21) and inv(16).
16732326	4	68	theme	interactome	979:989	arg1	analysis					991:998	The interactome analysis	975:998	The interactome analysis based on computational bioinformatics	975:1036	The interactome analysis based on computational bioinformatics reveals major regulating networks: MAPK8 and MYC for complex aberrant karyotype, TP53 for t(8;21), TP53-MYC-PRKAC for 11q23 and JUN and MYC for Inv(16).
16732326	2	69	theme	AML	356:358	arg1	patients					360:367	AML patients	356:367	AML patients with cytogenetic abnormalities	356:398	Because the pathological outcome of AML patients with cytogenetic abnormalities differs considerably, we hypothesized that their proteome may also differ specifically in their expression pattern, protein interaction pathways and post-translational modifications (PTM).
16732326	3	70	theme	other	932:936	arg1	methods					938:944	other methods	932:944	other methods	932:944	We performed this study using 42 AML patients diagnosed for various cytogenetic abnormalities based on two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionization time of flight mass spectrometry (MS) and MSMS tandem MS. We could identify significant differences in the proteome and PTM of peptides, later confirmed by other methods, between cytogenetic groups.
16732326	5	71	theme	hnRNPA2/B1	1519:1528	arg1	translocation					1429:1441	11q23 translocation	1423:1441	11q23 translocation	1423:1441	Further, we analysed 42 MS spectra representative of hnRNPH1, calreticulin and hnRNPA2/B1 in a peak explorer, which reveals a cytogenetic-specific PTM of beta-O-linked N-acetyl glucosamine (O-GlcNAc) of hnRNPH1 in AML patients with 11q23 translocation, an acetylation of calreticulin in t(8;21) translocation and methylation of hnRNPA2/B1 in patients with translocations of t(8;21) and inv(16).
16732326	5	71	theme	hnRNPA2/B1	1519:1528	arg1	acetylation					1447:1457	an acetylation	1444:1457	an acetylation of calreticulin in t(8;21) translocation	1444:1498	Further, we analysed 42 MS spectra representative of hnRNPH1, calreticulin and hnRNPA2/B1 in a peak explorer, which reveals a cytogenetic-specific PTM of beta-O-linked N-acetyl glucosamine (O-GlcNAc) of hnRNPH1 in AML patients with 11q23 translocation, an acetylation of calreticulin in t(8;21) translocation and methylation of hnRNPA2/B1 in patients with translocations of t(8;21) and inv(16).
16732326	5	71	theme	hnRNPA2/B1	1519:1528	arg1	methylation					1504:1514	methylation	1504:1514	methylation	1504:1514	Further, we analysed 42 MS spectra representative of hnRNPH1, calreticulin and hnRNPA2/B1 in a peak explorer, which reveals a cytogenetic-specific PTM of beta-O-linked N-acetyl glucosamine (O-GlcNAc) of hnRNPH1 in AML patients with 11q23 translocation, an acetylation of calreticulin in t(8;21) translocation and methylation of hnRNPA2/B1 in patients with translocations of t(8;21) and inv(16).
16732326	3	72	theme	matrix-assisted	732:746	arg1	desorption/ionization					754:774	matrix-assisted laser desorption/ionization	732:774	matrix-assisted laser desorption/ionization time of flight mass spectrometry (MS)	732:812	We performed this study using 42 AML patients diagnosed for various cytogenetic abnormalities based on two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionization time of flight mass spectrometry (MS) and MSMS tandem MS. We could identify significant differences in the proteome and PTM of peptides, later confirmed by other methods, between cytogenetic groups.
16732326	3	73	theme	MSMS	818:821	arg1	MS.					830:832	MSMS tandem MS.	818:832	MSMS tandem MS.	818:832	We performed this study using 42 AML patients diagnosed for various cytogenetic abnormalities based on two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionization time of flight mass spectrometry (MS) and MSMS tandem MS. We could identify significant differences in the proteome and PTM of peptides, later confirmed by other methods, between cytogenetic groups.
16732326	5	74	theme	N-acetyl	1359:1366	arg1	O-GlcNAc					1381:1388	O-GlcNAc	1381:1388	O-GlcNAc	1381:1388	Further, we analysed 42 MS spectra representative of hnRNPH1, calreticulin and hnRNPA2/B1 in a peak explorer, which reveals a cytogenetic-specific PTM of beta-O-linked N-acetyl glucosamine (O-GlcNAc) of hnRNPH1 in AML patients with 11q23 translocation, an acetylation of calreticulin in t(8;21) translocation and methylation of hnRNPA2/B1 in patients with translocations of t(8;21) and inv(16).
16732326	5	74	theme	N-acetyl	1359:1366	arg1	glucosamine					1368:1378	beta-O-linked N-acetyl glucosamine	1345:1378	beta-O-linked N-acetyl glucosamine (O-GlcNAc)	1345:1389	Further, we analysed 42 MS spectra representative of hnRNPH1, calreticulin and hnRNPA2/B1 in a peak explorer, which reveals a cytogenetic-specific PTM of beta-O-linked N-acetyl glucosamine (O-GlcNAc) of hnRNPH1 in AML patients with 11q23 translocation, an acetylation of calreticulin in t(8;21) translocation and methylation of hnRNPA2/B1 in patients with translocations of t(8;21) and inv(16).
16732326	2	75	theme	post-translational	549:566	arg1	PTM					583:585	PTM	583:585	PTM	583:585	Because the pathological outcome of AML patients with cytogenetic abnormalities differs considerably, we hypothesized that their proteome may also differ specifically in their expression pattern, protein interaction pathways and post-translational modifications (PTM).
16732326	2	75	theme	post-translational	549:566	arg1	modifications					568:580	post-translational modifications	549:580	post-translational modifications (PTM)	549:586	Because the pathological outcome of AML patients with cytogenetic abnormalities differs considerably, we hypothesized that their proteome may also differ specifically in their expression pattern, protein interaction pathways and post-translational modifications (PTM).
16732326	3	76	theme	laser	748:752	arg1	desorption/ionization					754:774	matrix-assisted laser desorption/ionization	732:774	matrix-assisted laser desorption/ionization time of flight mass spectrometry (MS)	732:812	We performed this study using 42 AML patients diagnosed for various cytogenetic abnormalities based on two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionization time of flight mass spectrometry (MS) and MSMS tandem MS. We could identify significant differences in the proteome and PTM of peptides, later confirmed by other methods, between cytogenetic groups.
16732326	3	77	theme	cytogenetic	657:667	arg1	abnormalities					669:681	various cytogenetic abnormalities	649:681	various cytogenetic abnormalities based on two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionization time of flight mass spectrometry (MS) and MSMS tandem MS. We could identify significant differences in the proteome and PTM of peptides, later confirmed by other methods, between cytogenetic groups	649:972	We performed this study using 42 AML patients diagnosed for various cytogenetic abnormalities based on two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionization time of flight mass spectrometry (MS) and MSMS tandem MS. We could identify significant differences in the proteome and PTM of peptides, later confirmed by other methods, between cytogenetic groups.
16732326	3	78	theme	desorption/ionization	754:774	arg1	time					776:779	matrix-assisted laser desorption/ionization time	732:779	matrix-assisted laser desorption/ionization time of flight mass spectrometry (MS)	732:812	We performed this study using 42 AML patients diagnosed for various cytogenetic abnormalities based on two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionization time of flight mass spectrometry (MS) and MSMS tandem MS. We could identify significant differences in the proteome and PTM of peptides, later confirmed by other methods, between cytogenetic groups.
16732326	4	79	theme	aberrant	1099:1106	arg1	karyotype					1108:1116	complex aberrant karyotype	1091:1116	complex aberrant karyotype	1091:1116	The interactome analysis based on computational bioinformatics reveals major regulating networks: MAPK8 and MYC for complex aberrant karyotype, TP53 for t(8;21), TP53-MYC-PRKAC for 11q23 and JUN and MYC for Inv(16).
16732326	3	80	theme	mass	791:794	arg1	MS					810:811	MS	810:811	MS	810:811	We performed this study using 42 AML patients diagnosed for various cytogenetic abnormalities based on two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionization time of flight mass spectrometry (MS) and MSMS tandem MS. We could identify significant differences in the proteome and PTM of peptides, later confirmed by other methods, between cytogenetic groups.
16732326	3	80	theme	mass	791:794	arg1	spectrometry					796:807	flight mass spectrometry	784:807	flight mass spectrometry (MS)	784:812	We performed this study using 42 AML patients diagnosed for various cytogenetic abnormalities based on two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionization time of flight mass spectrometry (MS) and MSMS tandem MS. We could identify significant differences in the proteome and PTM of peptides, later confirmed by other methods, between cytogenetic groups.
16732326	0	81	dep	Proteomics	0:9	arg1	differ					63:68	differ	63:68	differ specifically in their proteome, interactome and post-translational protein modifications	63:157	Proteomics of acute myeloid leukaemia: Cytogenetic risk groups differ specifically in their proteome, interactome and post-translational protein modifications.
16732326	1	82	theme	Acute	160:164	arg1	AML					185:187	AML	185:187	AML	185:187	Acute myeloid leukaemia (AML) is characterized by specific cytogenetic aberrations that are strong determinants of prognostic outcome and therapeutic response.
16732326	1	82	theme	Acute	160:164	arg1	leukaemia					174:182	Acute myeloid leukaemia	160:182	Acute myeloid leukaemia (AML)	160:188	Acute myeloid leukaemia (AML) is characterized by specific cytogenetic aberrations that are strong determinants of prognostic outcome and therapeutic response.
16732326	1	83	theme	strong	252:257	arg1	aberrations					231:241	specific cytogenetic aberrations	210:241	specific cytogenetic aberrations that are strong determinants of prognostic outcome and therapeutic response	210:317	Acute myeloid leukaemia (AML) is characterized by specific cytogenetic aberrations that are strong determinants of prognostic outcome and therapeutic response.
16732326	1	83	theme	strong	252:257	arg1	determinants					259:270	strong determinants	252:270	strong determinants of prognostic outcome and therapeutic response	252:317	Acute myeloid leukaemia (AML) is characterized by specific cytogenetic aberrations that are strong determinants of prognostic outcome and therapeutic response.
24580054	7	0	theme	cell	1144:1147	arg1	lines					1149:1153	cell lines	1144:1153	cell lines	1144:1153	Our results demonstrate that protein microarray technology, combined with the target validation strategy we report, is useful for identifying biologically important OGT substrates, including substrates not present in most tissue types or cell lines.
24580054	6	1	theme	several	891:897	arg1	sites					899:903	several sites	891:903	several sites	891:903	We show that endogenous OTX2 from a medulloblastoma cell line is O-GlcNAcylated at several sites.
24580054	4	2	theme	mass	546:549	arg1	tagging					551:557	O-GlcNAc mass tagging	537:557	O-GlcNAc mass tagging	537:557	We also report a rapid method to validate OGT substrates that combines in vitro transcription-translation with O-GlcNAc mass tagging.
24580054	5	3	theme	brain	668:672	arg1	development					674:684	brain development	668:684	brain development	668:684	Among the validated new OGT targets is Orthodenticle homeobox 2 (OTX2), a transcription factor critical for brain development, which is primarily expressed only during early embryogenesis and in medulloblastomas, where it functions as an oncogene.
24580054	7	4	theme	target	984:989	arg1	strategy					1002:1009	the target validation strategy	980:1009	the target validation strategy we report	980:1019	Our results demonstrate that protein microarray technology, combined with the target validation strategy we report, is useful for identifying biologically important OGT substrates, including substrates not present in most tissue types or cell lines.
24580054	3	5	theme	microarray	368:377	arg1	approach					379:386	a microarray approach	366:386	a microarray approach	366:386	Here we demonstrate the utility of a microarray approach for discovering novel OGT substrates.
24580054	4	6	theme	O-GlcNAc	537:544	arg1	tagging					551:557	O-GlcNAc mass tagging	537:557	O-GlcNAc mass tagging	537:557	We also report a rapid method to validate OGT substrates that combines in vitro transcription-translation with O-GlcNAc mass tagging.
24580054	6	7	theme	endogenous	821:830	arg1	OTX2					832:835	endogenous OTX2	821:835	endogenous OTX2 from a medulloblastoma cell line	821:868	We show that endogenous OTX2 from a medulloblastoma cell line is O-GlcNAcylated at several sites.
24580054	3	8	theme	approach	379:386	arg1	utility					355:361	the utility	351:361	the utility of a microarray approach for discovering novel OGT substrates	351:423	Here we demonstrate the utility of a microarray approach for discovering novel OGT substrates.
24580054	0	9	theme	Microarray	0:9	arg1	discovery					11:19	Microarray discovery	0:19	Microarray discovery of new OGT substrates: the medulloblastoma oncogene OTX2	0:76	Microarray discovery of new OGT substrates: the medulloblastoma oncogene OTX2 is O-GlcNAcylated.
24580054	7	10	theme	most	1123:1126	arg1	types					1135:1139	most tissue types	1123:1139	most tissue types	1123:1139	Our results demonstrate that protein microarray technology, combined with the target validation strategy we report, is useful for identifying biologically important OGT substrates, including substrates not present in most tissue types or cell lines.
24580054	5	11	theme	transcription	634:646	arg1	factor					648:653	a transcription factor	632:653	a transcription factor critical for brain development, which is primarily expressed only during early embryogenesis and in medulloblastomas, where it functions as an oncogene	632:805	Among the validated new OGT targets is Orthodenticle homeobox 2 (OTX2), a transcription factor critical for brain development, which is primarily expressed only during early embryogenesis and in medulloblastomas, where it functions as an oncogene.
24580054	5	11	theme	transcription	634:646	arg1	homeobox					613:620	Orthodenticle homeobox 2	599:622	Orthodenticle homeobox 2 (OTX2)	599:629	Among the validated new OGT targets is Orthodenticle homeobox 2 (OTX2), a transcription factor critical for brain development, which is primarily expressed only during early embryogenesis and in medulloblastomas, where it functions as an oncogene.
24580054	2	12	theme	complex	278:284	arg1	biology					286:292	OGT's complex biology	272:292	OGT's complex biology	272:292	Understanding OGT's complex biology requires identifying its substrates.
24580054	3	13	theme	novel	404:408	arg1	substrates					414:423	novel OGT substrates	404:423	novel OGT substrates	404:423	Here we demonstrate the utility of a microarray approach for discovering novel OGT substrates.
24580054	4	14	theme	in	497:498	arg1	transcription-translation					506:530	in vitro transcription-translation	497:530	in vitro transcription-translation	497:530	We also report a rapid method to validate OGT substrates that combines in vitro transcription-translation with O-GlcNAc mass tagging.
24580054	7	15	theme	present	1112:1118	arg1	substrates					1097:1106	substrates	1097:1106	substrates not present in most tissue types or cell lines	1097:1153	Our results demonstrate that protein microarray technology, combined with the target validation strategy we report, is useful for identifying biologically important OGT substrates, including substrates not present in most tissue types or cell lines.
24580054	5	16	theme	Orthodenticle	599:611	arg1	homeobox					613:620	Orthodenticle homeobox 2	599:622	Orthodenticle homeobox 2 (OTX2)	599:629	Among the validated new OGT targets is Orthodenticle homeobox 2 (OTX2), a transcription factor critical for brain development, which is primarily expressed only during early embryogenesis and in medulloblastomas, where it functions as an oncogene.
24580054	5	16	theme	Orthodenticle	599:611	arg1	factor					648:653	a transcription factor	632:653	a transcription factor critical for brain development, which is primarily expressed only during early embryogenesis and in medulloblastomas, where it functions as an oncogene	632:805	Among the validated new OGT targets is Orthodenticle homeobox 2 (OTX2), a transcription factor critical for brain development, which is primarily expressed only during early embryogenesis and in medulloblastomas, where it functions as an oncogene.
24580054	5	16	theme	Orthodenticle	599:611	arg1	OTX2					625:628	OTX2	625:628	OTX2	625:628	Among the validated new OGT targets is Orthodenticle homeobox 2 (OTX2), a transcription factor critical for brain development, which is primarily expressed only during early embryogenesis and in medulloblastomas, where it functions as an oncogene.
24580054	3	17	theme	OGT	410:412	arg1	substrates					414:423	novel OGT substrates	404:423	novel OGT substrates	404:423	Here we demonstrate the utility of a microarray approach for discovering novel OGT substrates.
24580054	7	18	from	present	1112:1118	arg1	types					1135:1139	most tissue types	1123:1139	most tissue types	1123:1139	Our results demonstrate that protein microarray technology, combined with the target validation strategy we report, is useful for identifying biologically important OGT substrates, including substrates not present in most tissue types or cell lines.
24580054	7	18	from	present	1112:1118	arg1	lines					1149:1153	cell lines	1144:1153	cell lines	1144:1153	Our results demonstrate that protein microarray technology, combined with the target validation strategy we report, is useful for identifying biologically important OGT substrates, including substrates not present in most tissue types or cell lines.
24580054	5	19	theme	critical	655:662	arg1	factor					648:653	a transcription factor	632:653	a transcription factor critical for brain development, which is primarily expressed only during early embryogenesis and in medulloblastomas, where it functions as an oncogene	632:805	Among the validated new OGT targets is Orthodenticle homeobox 2 (OTX2), a transcription factor critical for brain development, which is primarily expressed only during early embryogenesis and in medulloblastomas, where it functions as an oncogene.
24580054	5	19	theme	critical	655:662	arg1	homeobox					613:620	Orthodenticle homeobox 2	599:622	Orthodenticle homeobox 2 (OTX2)	599:629	Among the validated new OGT targets is Orthodenticle homeobox 2 (OTX2), a transcription factor critical for brain development, which is primarily expressed only during early embryogenesis and in medulloblastomas, where it functions as an oncogene.
24580054	7	20	theme	microarray	943:952	arg1	technology					954:963	protein microarray technology	935:963	protein microarray technology	935:963	Our results demonstrate that protein microarray technology, combined with the target validation strategy we report, is useful for identifying biologically important OGT substrates, including substrates not present in most tissue types or cell lines.
24580054	6	21	from	line	865:868	arg1	OTX2					832:835	endogenous OTX2	821:835	endogenous OTX2 from a medulloblastoma cell line	821:868	We show that endogenous OTX2 from a medulloblastoma cell line is O-GlcNAcylated at several sites.
24580054	7	22	dep	strategy	1002:1009	arg1	report					1014:1019	report	1014:1019	report	1014:1019	Our results demonstrate that protein microarray technology, combined with the target validation strategy we report, is useful for identifying biologically important OGT substrates, including substrates not present in most tissue types or cell lines.
24580054	7	22	dep	strategy	1002:1009	arg1	we					1011:1012	we	1011:1012	we	1011:1012	Our results demonstrate that protein microarray technology, combined with the target validation strategy we report, is useful for identifying biologically important OGT substrates, including substrates not present in most tissue types or cell lines.
24580054	0	23	theme	new	24:26	arg1	substrates					32:41	new OGT substrates	24:41	new OGT substrates	24:41	Microarray discovery of new OGT substrates: the medulloblastoma oncogene OTX2 is O-GlcNAcylated.
24580054	4	24	dep	in	497:498	arg1	vitro					500:504	vitro	500:504	vitro	500:504	We also report a rapid method to validate OGT substrates that combines in vitro transcription-translation with O-GlcNAc mass tagging.
24580054	1	25	theme	O-GlcNAc	97:104	arg1	essential					174:182	essential	174:182	essential	174:182	O-GlcNAc transferase (OGT) is a serine/threonine glycosyltransferase that is essential for development and continues to be critically important throughout life.
24580054	1	25	theme	O-GlcNAc	97:104	arg1	important					231:239	important	231:239	important	231:239	O-GlcNAc transferase (OGT) is a serine/threonine glycosyltransferase that is essential for development and continues to be critically important throughout life.
24580054	1	25	theme	O-GlcNAc	97:104	arg1	glycosyltransferase					146:164	a serine/threonine glycosyltransferase	127:164	a serine/threonine glycosyltransferase that is essential for development and continues to be critically important throughout life	127:255	O-GlcNAc transferase (OGT) is a serine/threonine glycosyltransferase that is essential for development and continues to be critically important throughout life.
24580054	1	25	theme	O-GlcNAc	97:104	arg1	OGT					119:121	OGT	119:121	OGT	119:121	O-GlcNAc transferase (OGT) is a serine/threonine glycosyltransferase that is essential for development and continues to be critically important throughout life.
24580054	1	25	theme	O-GlcNAc	97:104	arg1	transferase					106:116	O-GlcNAc transferase	97:116	O-GlcNAc transferase (OGT)	97:122	O-GlcNAc transferase (OGT) is a serine/threonine glycosyltransferase that is essential for development and continues to be critically important throughout life.
24580054	0	26	theme	substrates	32:41	arg1	discovery					11:19	Microarray discovery	0:19	Microarray discovery of new OGT substrates: the medulloblastoma oncogene OTX2	0:76	Microarray discovery of new OGT substrates: the medulloblastoma oncogene OTX2 is O-GlcNAcylated.
24580054	5	27	theme	early	728:732	arg1	embryogenesis					734:746	early embryogenesis	728:746	early embryogenesis	728:746	Among the validated new OGT targets is Orthodenticle homeobox 2 (OTX2), a transcription factor critical for brain development, which is primarily expressed only during early embryogenesis and in medulloblastomas, where it functions as an oncogene.
24580054	0	28	theme	OGT	28:30	arg1	substrates					32:41	new OGT substrates	24:41	new OGT substrates	24:41	Microarray discovery of new OGT substrates: the medulloblastoma oncogene OTX2 is O-GlcNAcylated.
24580054	7	29	from	types	1135:1139	arg1	present					1112:1118	present	1112:1118	present	1112:1118	Our results demonstrate that protein microarray technology, combined with the target validation strategy we report, is useful for identifying biologically important OGT substrates, including substrates not present in most tissue types or cell lines.
24580054	5	30	theme	validated	570:578	arg1	targets					588:594	the validated new OGT targets	566:594	the validated new OGT targets	566:594	Among the validated new OGT targets is Orthodenticle homeobox 2 (OTX2), a transcription factor critical for brain development, which is primarily expressed only during early embryogenesis and in medulloblastomas, where it functions as an oncogene.
24580054	6	31	from	sites	899:903	arg1	O-GlcNAcylated					873:886	O-GlcNAcylated	873:886	O-GlcNAcylated	873:886	We show that endogenous OTX2 from a medulloblastoma cell line is O-GlcNAcylated at several sites.
24580054	7	32	theme	OGT	1071:1073	arg1	substrates					1075:1084	biologically important OGT substrates	1048:1084	biologically important OGT substrates	1048:1084	Our results demonstrate that protein microarray technology, combined with the target validation strategy we report, is useful for identifying biologically important OGT substrates, including substrates not present in most tissue types or cell lines.
24580054	7	32	theme	OGT	1071:1073	arg1	substrates					1097:1106	substrates	1097:1106	substrates not present in most tissue types or cell lines	1097:1153	Our results demonstrate that protein microarray technology, combined with the target validation strategy we report, is useful for identifying biologically important OGT substrates, including substrates not present in most tissue types or cell lines.
24580054	4	33	theme	OGT	468:470	arg1	substrates					472:481	OGT substrates	468:481	OGT substrates that combines in vitro transcription-translation with O-GlcNAc mass tagging	468:557	We also report a rapid method to validate OGT substrates that combines in vitro transcription-translation with O-GlcNAc mass tagging.
24580054	5	34	theme	new	580:582	arg1	targets					588:594	the validated new OGT targets	566:594	the validated new OGT targets	566:594	Among the validated new OGT targets is Orthodenticle homeobox 2 (OTX2), a transcription factor critical for brain development, which is primarily expressed only during early embryogenesis and in medulloblastomas, where it functions as an oncogene.
24580054	6	35	theme	cell	860:863	arg1	line					865:868	a medulloblastoma cell line	842:868	a medulloblastoma cell line	842:868	We show that endogenous OTX2 from a medulloblastoma cell line is O-GlcNAcylated at several sites.
24580054	7	36	theme	tissue	1128:1133	arg1	types					1135:1139	most tissue types	1123:1139	most tissue types	1123:1139	Our results demonstrate that protein microarray technology, combined with the target validation strategy we report, is useful for identifying biologically important OGT substrates, including substrates not present in most tissue types or cell lines.
24580054	5	37	theme	OGT	584:586	arg1	targets					588:594	the validated new OGT targets	566:594	the validated new OGT targets	566:594	Among the validated new OGT targets is Orthodenticle homeobox 2 (OTX2), a transcription factor critical for brain development, which is primarily expressed only during early embryogenesis and in medulloblastomas, where it functions as an oncogene.
24580054	7	38	from	lines	1149:1153	arg1	present					1112:1118	present	1112:1118	present	1112:1118	Our results demonstrate that protein microarray technology, combined with the target validation strategy we report, is useful for identifying biologically important OGT substrates, including substrates not present in most tissue types or cell lines.
24580054	6	39	theme	medulloblastoma	844:858	arg1	line					865:868	a medulloblastoma cell line	842:868	a medulloblastoma cell line	842:868	We show that endogenous OTX2 from a medulloblastoma cell line is O-GlcNAcylated at several sites.
24580054	7	40	theme	validation	991:1000	arg1	strategy					1002:1009	the target validation strategy	980:1009	the target validation strategy we report	980:1019	Our results demonstrate that protein microarray technology, combined with the target validation strategy we report, is useful for identifying biologically important OGT substrates, including substrates not present in most tissue types or cell lines.
24580054	7	41	theme	protein	935:941	arg1	technology					954:963	protein microarray technology	935:963	protein microarray technology	935:963	Our results demonstrate that protein microarray technology, combined with the target validation strategy we report, is useful for identifying biologically important OGT substrates, including substrates not present in most tissue types or cell lines.
24580054	7	42	theme	important	1061:1069	arg1	substrates					1075:1084	biologically important OGT substrates	1048:1084	biologically important OGT substrates	1048:1084	Our results demonstrate that protein microarray technology, combined with the target validation strategy we report, is useful for identifying biologically important OGT substrates, including substrates not present in most tissue types or cell lines.
24580054	7	42	theme	important	1061:1069	arg1	substrates					1097:1106	substrates	1097:1106	substrates not present in most tissue types or cell lines	1097:1153	Our results demonstrate that protein microarray technology, combined with the target validation strategy we report, is useful for identifying biologically important OGT substrates, including substrates not present in most tissue types or cell lines.
24580054	0	43	theme	oncogene	64:71	arg1	OTX2					73:76	the medulloblastoma oncogene OTX2	44:76	Microarray discovery of new OGT substrates: the medulloblastoma oncogene OTX2	0:76	Microarray discovery of new OGT substrates: the medulloblastoma oncogene OTX2 is O-GlcNAcylated.
24580054	4	44	theme	rapid	443:447	arg1	method					449:454	a rapid method	441:454	a rapid method to validate OGT substrates that combines in vitro transcription-translation with O-GlcNAc mass tagging	441:557	We also report a rapid method to validate OGT substrates that combines in vitro transcription-translation with O-GlcNAc mass tagging.
24580054	0	45	dep	discovery	11:19	arg1	OTX2					73:76	the medulloblastoma oncogene OTX2	44:76	Microarray discovery of new OGT substrates: the medulloblastoma oncogene OTX2	0:76	Microarray discovery of new OGT substrates: the medulloblastoma oncogene OTX2 is O-GlcNAcylated.
24580054	7	46	attach	present	1112:1118	arg2	substrates					1097:1106	substrates	1097:1106	substrates not present in most tissue types or cell lines	1097:1153	Our results demonstrate that protein microarray technology, combined with the target validation strategy we report, is useful for identifying biologically important OGT substrates, including substrates not present in most tissue types or cell lines.
24580054	7	46	attach	present	1112:1118	arg1	types					1135:1139	most tissue types	1123:1139	most tissue types	1123:1139	Our results demonstrate that protein microarray technology, combined with the target validation strategy we report, is useful for identifying biologically important OGT substrates, including substrates not present in most tissue types or cell lines.
24580054	7	46	attach	present	1112:1118	arg1	lines					1149:1153	cell lines	1144:1153	cell lines	1144:1153	Our results demonstrate that protein microarray technology, combined with the target validation strategy we report, is useful for identifying biologically important OGT substrates, including substrates not present in most tissue types or cell lines.
24580054	0	47	theme	medulloblastoma	48:62	arg1	OTX2					73:76	the medulloblastoma oncogene OTX2	44:76	Microarray discovery of new OGT substrates: the medulloblastoma oncogene OTX2	0:76	Microarray discovery of new OGT substrates: the medulloblastoma oncogene OTX2 is O-GlcNAcylated.
24580054	1	48	theme	serine/threonine	129:144	arg1	essential					174:182	essential	174:182	essential	174:182	O-GlcNAc transferase (OGT) is a serine/threonine glycosyltransferase that is essential for development and continues to be critically important throughout life.
24580054	1	48	theme	serine/threonine	129:144	arg1	glycosyltransferase					146:164	a serine/threonine glycosyltransferase	127:164	a serine/threonine glycosyltransferase that is essential for development and continues to be critically important throughout life	127:255	O-GlcNAc transferase (OGT) is a serine/threonine glycosyltransferase that is essential for development and continues to be critically important throughout life.
24580054	1	48	theme	serine/threonine	129:144	arg1	important					231:239	important	231:239	important	231:239	O-GlcNAc transferase (OGT) is a serine/threonine glycosyltransferase that is essential for development and continues to be critically important throughout life.
24580054	1	48	theme	serine/threonine	129:144	arg1	transferase					106:116	O-GlcNAc transferase	97:116	O-GlcNAc transferase (OGT)	97:122	O-GlcNAc transferase (OGT) is a serine/threonine glycosyltransferase that is essential for development and continues to be critically important throughout life.
21867680	4	0	theme	Tollip	816:821	arg1	expression					828:837	Tollip gene expression	816:837	Tollip gene expression	816:837	Elf-1 was identified as a transcription factor that negatively regulates Tollip gene expression.
21867680	1	1	theme	Intestinal	174:183	arg1	IECs					203:206	IECs	203:206	IECs	203:206	Intestinal epithelial cells (IECs) must be tolerant of the large number of commensal bacteria inhabiting the intestinal tract to avoid excessive inflammatory reactions.
21867680	1	1	theme	Intestinal	174:183	arg1	cells					196:200	Intestinal epithelial cells	174:200	Intestinal epithelial cells (IECs)	174:207	Intestinal epithelial cells (IECs) must be tolerant of the large number of commensal bacteria inhabiting the intestinal tract to avoid excessive inflammatory reactions.
21867680	1	2	theme	commensal	249:257	arg1	bacteria					259:266	commensal bacteria	249:266	commensal bacteria inhabiting the intestinal tract to avoid excessive inflammatory reactions	249:340	Intestinal epithelial cells (IECs) must be tolerant of the large number of commensal bacteria inhabiting the intestinal tract to avoid excessive inflammatory reactions.
21867680	1	3	theme	epithelial	185:194	arg1	IECs					203:206	IECs	203:206	IECs	203:206	Intestinal epithelial cells (IECs) must be tolerant of the large number of commensal bacteria inhabiting the intestinal tract to avoid excessive inflammatory reactions.
21867680	1	3	theme	epithelial	185:194	arg1	cells					196:200	Intestinal epithelial cells	174:200	Intestinal epithelial cells (IECs)	174:207	Intestinal epithelial cells (IECs) must be tolerant of the large number of commensal bacteria inhabiting the intestinal tract to avoid excessive inflammatory reactions.
21867680	1	4	theme	bacteria	259:266	arg1	number					239:244	the large number	229:244	the large number of commensal bacteria inhabiting the intestinal tract to avoid excessive inflammatory reactions	229:340	Intestinal epithelial cells (IECs) must be tolerant of the large number of commensal bacteria inhabiting the intestinal tract to avoid excessive inflammatory reactions.
21867680	0	5	theme	O-GlcNAcylation-dependent	93:117	arg1	translocation					127:139	impaired O-GlcNAcylation-dependent nuclear translocation	84:139	impaired O-GlcNAcylation-dependent nuclear translocation of the negative regulator Elf-1	84:171	Transcription of the Tollip gene is elevated in intestinal epithelial cells through impaired O-GlcNAcylation-dependent nuclear translocation of the negative regulator Elf-1.
21867680	3	6	theme	human	671:675	arg1	Caco-2					687:692	Caco-2	687:692	Caco-2	687:692	In this study, we analyzed the underlying mechanisms for elevated transcription of the Tollip gene in IECs using a human IEC line, Caco-2, and a human monocyte line, THP-1, as a control.
21867680	3	6	theme	human	671:675	arg1	line					681:684	a human IEC line	669:684	a human IEC line	669:684	In this study, we analyzed the underlying mechanisms for elevated transcription of the Tollip gene in IECs using a human IEC line, Caco-2, and a human monocyte line, THP-1, as a control.
21867680	3	6	theme	human	671:675	arg1	control					734:740	a control	732:740	a control	732:740	In this study, we analyzed the underlying mechanisms for elevated transcription of the Tollip gene in IECs using a human IEC line, Caco-2, and a human monocyte line, THP-1, as a control.
21867680	3	6	theme	human	671:675	arg1	line					716:719	a human monocyte line	699:719	a human monocyte line	699:719	In this study, we analyzed the underlying mechanisms for elevated transcription of the Tollip gene in IECs using a human IEC line, Caco-2, and a human monocyte line, THP-1, as a control.
21867680	5	7	theme	N-acetylglucosamine	912:930	arg1	modification					943:954	O-linked N-acetylglucosamine (O-GlcNAc) modification	903:954	O-linked N-acetylglucosamine (O-GlcNAc) modification	903:954	The transcription factor Elf-1 was localized in the nucleus by O-linked N-acetylglucosamine (O-GlcNAc) modification, whereas the unmodified form was detected only in the cytoplasm.
21867680	5	8	theme	O-linked	903:910	arg1	O-GlcNAc					933:940	O-GlcNAc	933:940	O-GlcNAc	933:940	The transcription factor Elf-1 was localized in the nucleus by O-linked N-acetylglucosamine (O-GlcNAc) modification, whereas the unmodified form was detected only in the cytoplasm.
21867680	5	8	theme	O-linked	903:910	arg1	N-acetylglucosamine					912:930	O-linked N-acetylglucosamine	903:930	O-linked N-acetylglucosamine (O-GlcNAc) modification	903:954	The transcription factor Elf-1 was localized in the nucleus by O-linked N-acetylglucosamine (O-GlcNAc) modification, whereas the unmodified form was detected only in the cytoplasm.
21867680	0	9	theme	impaired	84:91	arg1	translocation					127:139	impaired O-GlcNAcylation-dependent nuclear translocation	84:139	impaired O-GlcNAcylation-dependent nuclear translocation of the negative regulator Elf-1	84:171	Transcription of the Tollip gene is elevated in intestinal epithelial cells through impaired O-GlcNAcylation-dependent nuclear translocation of the negative regulator Elf-1.
21867680	4	10	theme	gene	823:826	arg1	expression					828:837	Tollip gene expression	816:837	Tollip gene expression	816:837	Elf-1 was identified as a transcription factor that negatively regulates Tollip gene expression.
21867680	7	11	theme	O-GlcNAc	1207:1214	arg1	modification					1216:1227	insufficient O-GlcNAc modification	1194:1227	insufficient O-GlcNAc modification	1194:1227	Collectively, the results indicate that insufficient O-GlcNAc modification prevents Elf-1-mediated transcriptional repression and thereby upregulates Tollip gene expression in IECs.
21867680	5	12	theme	transcription	844:856	arg1	Elf-1					865:869	The transcription factor Elf-1	840:869	The transcription factor Elf-1	840:869	The transcription factor Elf-1 was localized in the nucleus by O-linked N-acetylglucosamine (O-GlcNAc) modification, whereas the unmodified form was detected only in the cytoplasm.
21867680	7	13	theme	transcriptional	1253:1267	arg1	repression					1269:1278	Elf-1-mediated transcriptional repression	1238:1278	Elf-1-mediated transcriptional repression	1238:1278	Collectively, the results indicate that insufficient O-GlcNAc modification prevents Elf-1-mediated transcriptional repression and thereby upregulates Tollip gene expression in IECs.
21867680	6	14	theme	THP-1	1046:1050	arg1	cells					1052:1056	Caco-2 and THP-1 cells	1035:1056	Caco-2 and THP-1 cells	1035:1056	Comparison of Caco-2 and THP-1 cells revealed that O-GlcNAc modification of Elf-1 was significantly lower in IECs than in monocytes.
21867680	6	15	theme	Caco-2	1035:1040	arg1	cells					1052:1056	Caco-2 and THP-1 cells	1035:1056	Caco-2 and THP-1 cells	1035:1056	Comparison of Caco-2 and THP-1 cells revealed that O-GlcNAc modification of Elf-1 was significantly lower in IECs than in monocytes.
21867680	2	16	theme	receptor	412:419	arg1	signaling					421:429	Toll-like receptor signaling	402:429	Toll-like receptor signaling	402:429	Toll-interacting protein (Tollip), a negative regulator of Toll-like receptor signaling, is known to be expressed at high levels in IECs, and to thereby contribute to the hyporesponsiveness of IECs to commensals.
21867680	0	17	theme	nuclear	119:125	arg1	translocation					127:139	impaired O-GlcNAcylation-dependent nuclear translocation	84:139	impaired O-GlcNAcylation-dependent nuclear translocation of the negative regulator Elf-1	84:171	Transcription of the Tollip gene is elevated in intestinal epithelial cells through impaired O-GlcNAcylation-dependent nuclear translocation of the negative regulator Elf-1.
21867680	4	18	theme	transcription	769:781	arg1	Elf-1					743:747	Elf-1	743:747	Elf-1	743:747	Elf-1 was identified as a transcription factor that negatively regulates Tollip gene expression.
21867680	4	18	theme	transcription	769:781	arg1	factor					783:788	a transcription factor	767:788	a transcription factor that negatively regulates Tollip gene expression	767:837	Elf-1 was identified as a transcription factor that negatively regulates Tollip gene expression.
21867680	6	19	mod	modification	1081:1092	arg1	Elf-1					1097:1101	Elf-1	1097:1101	Elf-1	1097:1101	Comparison of Caco-2 and THP-1 cells revealed that O-GlcNAc modification of Elf-1 was significantly lower in IECs than in monocytes.
21867680	6	19	mod	modification	1081:1092	arg3	O-GlcNAc					1072:1079	O-GlcNAc modification	1072:1092	O-GlcNAc modification of Elf-1	1072:1101	Comparison of Caco-2 and THP-1 cells revealed that O-GlcNAc modification of Elf-1 was significantly lower in IECs than in monocytes.
21867680	2	20	theme	Toll-like	402:410	arg1	signaling					421:429	Toll-like receptor signaling	402:429	Toll-like receptor signaling	402:429	Toll-interacting protein (Tollip), a negative regulator of Toll-like receptor signaling, is known to be expressed at high levels in IECs, and to thereby contribute to the hyporesponsiveness of IECs to commensals.
21867680	3	21	theme	monocyte	707:714	arg1	THP-1					722:726	THP-1	722:726	THP-1	722:726	In this study, we analyzed the underlying mechanisms for elevated transcription of the Tollip gene in IECs using a human IEC line, Caco-2, and a human monocyte line, THP-1, as a control.
21867680	3	21	theme	monocyte	707:714	arg1	line					716:719	a human monocyte line	699:719	a human monocyte line	699:719	In this study, we analyzed the underlying mechanisms for elevated transcription of the Tollip gene in IECs using a human IEC line, Caco-2, and a human monocyte line, THP-1, as a control.
21867680	3	21	theme	monocyte	707:714	arg1	line					681:684	a human IEC line	669:684	a human IEC line	669:684	In this study, we analyzed the underlying mechanisms for elevated transcription of the Tollip gene in IECs using a human IEC line, Caco-2, and a human monocyte line, THP-1, as a control.
21867680	3	21	theme	monocyte	707:714	arg1	control					734:740	a control	732:740	a control	732:740	In this study, we analyzed the underlying mechanisms for elevated transcription of the Tollip gene in IECs using a human IEC line, Caco-2, and a human monocyte line, THP-1, as a control.
21867680	0	22	theme	regulator	157:165	arg1	Elf-1					167:171	the negative regulator Elf-1	144:171	the negative regulator Elf-1	144:171	Transcription of the Tollip gene is elevated in intestinal epithelial cells through impaired O-GlcNAcylation-dependent nuclear translocation of the negative regulator Elf-1.
21867680	1	23	theme	intestinal	283:292	arg1	tract					294:298	the intestinal tract	279:298	the intestinal tract to avoid excessive inflammatory reactions	279:340	Intestinal epithelial cells (IECs) must be tolerant of the large number of commensal bacteria inhabiting the intestinal tract to avoid excessive inflammatory reactions.
21867680	5	24	located	localized	875:883	arg1	nucleus					892:898	the nucleus	888:898	the nucleus	888:898	The transcription factor Elf-1 was localized in the nucleus by O-linked N-acetylglucosamine (O-GlcNAc) modification, whereas the unmodified form was detected only in the cytoplasm.
21867680	5	24	located	localized	875:883	arg2	Elf-1					865:869	The transcription factor Elf-1	840:869	The transcription factor Elf-1	840:869	The transcription factor Elf-1 was localized in the nucleus by O-linked N-acetylglucosamine (O-GlcNAc) modification, whereas the unmodified form was detected only in the cytoplasm.
21867680	0	25	theme	Tollip	21:26	arg1	gene					28:31	the Tollip gene	17:31	the Tollip gene	17:31	Transcription of the Tollip gene is elevated in intestinal epithelial cells through impaired O-GlcNAcylation-dependent nuclear translocation of the negative regulator Elf-1.
21867680	6	26	theme	Elf-1	1097:1101	arg1	modification					1081:1092	O-GlcNAc modification	1072:1092	O-GlcNAc modification of Elf-1	1072:1101	Comparison of Caco-2 and THP-1 cells revealed that O-GlcNAc modification of Elf-1 was significantly lower in IECs than in monocytes.
21867680	7	27	theme	Tollip	1304:1309	arg1	expression					1316:1325	Tollip gene expression	1304:1325	Tollip gene expression in IECs	1304:1333	Collectively, the results indicate that insufficient O-GlcNAc modification prevents Elf-1-mediated transcriptional repression and thereby upregulates Tollip gene expression in IECs.
21867680	5	28	theme	factor	858:863	arg1	Elf-1					865:869	The transcription factor Elf-1	840:869	The transcription factor Elf-1	840:869	The transcription factor Elf-1 was localized in the nucleus by O-linked N-acetylglucosamine (O-GlcNAc) modification, whereas the unmodified form was detected only in the cytoplasm.
21867680	7	29	theme	gene	1311:1314	arg1	expression					1316:1325	Tollip gene expression	1304:1325	Tollip gene expression in IECs	1304:1333	Collectively, the results indicate that insufficient O-GlcNAc modification prevents Elf-1-mediated transcriptional repression and thereby upregulates Tollip gene expression in IECs.
21867680	3	30	theme	human	701:705	arg1	THP-1					722:726	THP-1	722:726	THP-1	722:726	In this study, we analyzed the underlying mechanisms for elevated transcription of the Tollip gene in IECs using a human IEC line, Caco-2, and a human monocyte line, THP-1, as a control.
21867680	3	30	theme	human	701:705	arg1	line					716:719	a human monocyte line	699:719	a human monocyte line	699:719	In this study, we analyzed the underlying mechanisms for elevated transcription of the Tollip gene in IECs using a human IEC line, Caco-2, and a human monocyte line, THP-1, as a control.
21867680	3	30	theme	human	701:705	arg1	line					681:684	a human IEC line	669:684	a human IEC line	669:684	In this study, we analyzed the underlying mechanisms for elevated transcription of the Tollip gene in IECs using a human IEC line, Caco-2, and a human monocyte line, THP-1, as a control.
21867680	3	30	theme	human	701:705	arg1	control					734:740	a control	732:740	a control	732:740	In this study, we analyzed the underlying mechanisms for elevated transcription of the Tollip gene in IECs using a human IEC line, Caco-2, and a human monocyte line, THP-1, as a control.
21867680	2	31	theme	IECs	536:539	arg1	hyporesponsiveness					514:531	the hyporesponsiveness	510:531	the hyporesponsiveness of IECs to commensals	510:553	Toll-interacting protein (Tollip), a negative regulator of Toll-like receptor signaling, is known to be expressed at high levels in IECs, and to thereby contribute to the hyporesponsiveness of IECs to commensals.
21867680	3	32	theme	Tollip	643:648	arg1	gene					650:653	the Tollip gene	639:653	the Tollip gene	639:653	In this study, we analyzed the underlying mechanisms for elevated transcription of the Tollip gene in IECs using a human IEC line, Caco-2, and a human monocyte line, THP-1, as a control.
21867680	5	33	theme	unmodified	969:978	arg1	form					980:983	the unmodified form	965:983	the unmodified form	965:983	The transcription factor Elf-1 was localized in the nucleus by O-linked N-acetylglucosamine (O-GlcNAc) modification, whereas the unmodified form was detected only in the cytoplasm.
21867680	0	34	theme	gene	28:31	arg1	Transcription					0:12	Transcription	0:12	Transcription of the Tollip gene	0:31	Transcription of the Tollip gene is elevated in intestinal epithelial cells through impaired O-GlcNAcylation-dependent nuclear translocation of the negative regulator Elf-1.
21867680	1	35	theme	excessive	309:317	arg1	reactions					332:340	excessive inflammatory reactions	309:340	excessive inflammatory reactions	309:340	Intestinal epithelial cells (IECs) must be tolerant of the large number of commensal bacteria inhabiting the intestinal tract to avoid excessive inflammatory reactions.
21867680	0	36	theme	negative	148:155	arg1	Elf-1					167:171	the negative regulator Elf-1	144:171	the negative regulator Elf-1	144:171	Transcription of the Tollip gene is elevated in intestinal epithelial cells through impaired O-GlcNAcylation-dependent nuclear translocation of the negative regulator Elf-1.
21867680	5	37	located	detected	989:996	arg2	form					980:983	the unmodified form	965:983	the unmodified form	965:983	The transcription factor Elf-1 was localized in the nucleus by O-linked N-acetylglucosamine (O-GlcNAc) modification, whereas the unmodified form was detected only in the cytoplasm.
21867680	5	37	located	detected	989:996	arg1	cytoplasm					1010:1018	the cytoplasm	1006:1018	the cytoplasm	1006:1018	The transcription factor Elf-1 was localized in the nucleus by O-linked N-acetylglucosamine (O-GlcNAc) modification, whereas the unmodified form was detected only in the cytoplasm.
21867680	2	38	theme	signaling	421:429	arg1	regulator					389:397	a negative regulator	378:397	a negative regulator of Toll-like receptor signaling	378:429	Toll-interacting protein (Tollip), a negative regulator of Toll-like receptor signaling, is known to be expressed at high levels in IECs, and to thereby contribute to the hyporesponsiveness of IECs to commensals.
21867680	2	38	theme	signaling	421:429	arg1	protein					360:366	Toll-interacting protein	343:366	Toll-interacting protein (Tollip)	343:375	Toll-interacting protein (Tollip), a negative regulator of Toll-like receptor signaling, is known to be expressed at high levels in IECs, and to thereby contribute to the hyporesponsiveness of IECs to commensals.
21867680	1	39	theme	inflammatory	319:330	arg1	reactions					332:340	excessive inflammatory reactions	309:340	excessive inflammatory reactions	309:340	Intestinal epithelial cells (IECs) must be tolerant of the large number of commensal bacteria inhabiting the intestinal tract to avoid excessive inflammatory reactions.
21867680	5	40	link	O-linked	903:910	arg1	O-GlcNAc					933:940	O-GlcNAc	933:940	O-GlcNAc	933:940	The transcription factor Elf-1 was localized in the nucleus by O-linked N-acetylglucosamine (O-GlcNAc) modification, whereas the unmodified form was detected only in the cytoplasm.
21867680	5	40	link	O-linked	903:910	arg1	N-acetylglucosamine					912:930	O-linked N-acetylglucosamine	903:930	O-linked N-acetylglucosamine (O-GlcNAc) modification	903:954	The transcription factor Elf-1 was localized in the nucleus by O-linked N-acetylglucosamine (O-GlcNAc) modification, whereas the unmodified form was detected only in the cytoplasm.
21867680	2	41	theme	high	460:463	arg1	levels					465:470	high levels	460:470	high levels	460:470	Toll-interacting protein (Tollip), a negative regulator of Toll-like receptor signaling, is known to be expressed at high levels in IECs, and to thereby contribute to the hyporesponsiveness of IECs to commensals.
21867680	0	42	theme	Elf-1	167:171	arg1	translocation					127:139	impaired O-GlcNAcylation-dependent nuclear translocation	84:139	impaired O-GlcNAcylation-dependent nuclear translocation of the negative regulator Elf-1	84:171	Transcription of the Tollip gene is elevated in intestinal epithelial cells through impaired O-GlcNAcylation-dependent nuclear translocation of the negative regulator Elf-1.
21867680	3	43	from	transcription	622:634	arg1	IECs					658:661	IECs	658:661	IECs	658:661	In this study, we analyzed the underlying mechanisms for elevated transcription of the Tollip gene in IECs using a human IEC line, Caco-2, and a human monocyte line, THP-1, as a control.
21867680	6	44	theme	O-GlcNAc	1072:1079	arg1	modification					1081:1092	O-GlcNAc modification	1072:1092	O-GlcNAc modification of Elf-1	1072:1101	Comparison of Caco-2 and THP-1 cells revealed that O-GlcNAc modification of Elf-1 was significantly lower in IECs than in monocytes.
21867680	3	45	theme	gene	650:653	arg1	transcription					622:634	elevated transcription	613:634	elevated transcription of the Tollip gene in IECs	613:661	In this study, we analyzed the underlying mechanisms for elevated transcription of the Tollip gene in IECs using a human IEC line, Caco-2, and a human monocyte line, THP-1, as a control.
21867680	3	46	theme	elevated	613:620	arg1	transcription					622:634	elevated transcription	613:634	elevated transcription of the Tollip gene in IECs	613:661	In this study, we analyzed the underlying mechanisms for elevated transcription of the Tollip gene in IECs using a human IEC line, Caco-2, and a human monocyte line, THP-1, as a control.
21867680	7	47	from	expression	1316:1325	arg1	IECs					1330:1333	IECs	1330:1333	IECs	1330:1333	Collectively, the results indicate that insufficient O-GlcNAc modification prevents Elf-1-mediated transcriptional repression and thereby upregulates Tollip gene expression in IECs.
21867680	2	48	theme	Toll-interacting	343:358	arg1	regulator					389:397	a negative regulator	378:397	a negative regulator of Toll-like receptor signaling	378:429	Toll-interacting protein (Tollip), a negative regulator of Toll-like receptor signaling, is known to be expressed at high levels in IECs, and to thereby contribute to the hyporesponsiveness of IECs to commensals.
21867680	2	48	theme	Toll-interacting	343:358	arg1	Tollip					369:374	Tollip	369:374	Tollip	369:374	Toll-interacting protein (Tollip), a negative regulator of Toll-like receptor signaling, is known to be expressed at high levels in IECs, and to thereby contribute to the hyporesponsiveness of IECs to commensals.
21867680	2	48	theme	Toll-interacting	343:358	arg1	protein					360:366	Toll-interacting protein	343:366	Toll-interacting protein (Tollip)	343:375	Toll-interacting protein (Tollip), a negative regulator of Toll-like receptor signaling, is known to be expressed at high levels in IECs, and to thereby contribute to the hyporesponsiveness of IECs to commensals.
21867680	1	49	theme	large	233:237	arg1	number					239:244	the large number	229:244	the large number of commensal bacteria inhabiting the intestinal tract to avoid excessive inflammatory reactions	229:340	Intestinal epithelial cells (IECs) must be tolerant of the large number of commensal bacteria inhabiting the intestinal tract to avoid excessive inflammatory reactions.
21867680	0	50	theme	epithelial	59:68	arg1	cells					70:74	intestinal epithelial cells	48:74	intestinal epithelial cells	48:74	Transcription of the Tollip gene is elevated in intestinal epithelial cells through impaired O-GlcNAcylation-dependent nuclear translocation of the negative regulator Elf-1.
21867680	3	51	theme	underlying	587:596	arg1	mechanisms					598:607	the underlying mechanisms	583:607	the underlying mechanisms for elevated transcription of the Tollip gene in IECs	583:661	In this study, we analyzed the underlying mechanisms for elevated transcription of the Tollip gene in IECs using a human IEC line, Caco-2, and a human monocyte line, THP-1, as a control.
21867680	2	52	theme	negative	380:387	arg1	regulator					389:397	a negative regulator	378:397	a negative regulator of Toll-like receptor signaling	378:429	Toll-interacting protein (Tollip), a negative regulator of Toll-like receptor signaling, is known to be expressed at high levels in IECs, and to thereby contribute to the hyporesponsiveness of IECs to commensals.
21867680	2	52	theme	negative	380:387	arg1	protein					360:366	Toll-interacting protein	343:366	Toll-interacting protein (Tollip)	343:375	Toll-interacting protein (Tollip), a negative regulator of Toll-like receptor signaling, is known to be expressed at high levels in IECs, and to thereby contribute to the hyporesponsiveness of IECs to commensals.
21867680	1	53	theme	number	239:244	arg1	tolerant					217:224	tolerant	217:224	tolerant	217:224	Intestinal epithelial cells (IECs) must be tolerant of the large number of commensal bacteria inhabiting the intestinal tract to avoid excessive inflammatory reactions.
21867680	0	54	theme	intestinal	48:57	arg1	cells					70:74	intestinal epithelial cells	48:74	intestinal epithelial cells	48:74	Transcription of the Tollip gene is elevated in intestinal epithelial cells through impaired O-GlcNAcylation-dependent nuclear translocation of the negative regulator Elf-1.
21867680	3	55	theme	IEC	677:679	arg1	Caco-2					687:692	Caco-2	687:692	Caco-2	687:692	In this study, we analyzed the underlying mechanisms for elevated transcription of the Tollip gene in IECs using a human IEC line, Caco-2, and a human monocyte line, THP-1, as a control.
21867680	3	55	theme	IEC	677:679	arg1	line					681:684	a human IEC line	669:684	a human IEC line	669:684	In this study, we analyzed the underlying mechanisms for elevated transcription of the Tollip gene in IECs using a human IEC line, Caco-2, and a human monocyte line, THP-1, as a control.
21867680	3	55	theme	IEC	677:679	arg1	control					734:740	a control	732:740	a control	732:740	In this study, we analyzed the underlying mechanisms for elevated transcription of the Tollip gene in IECs using a human IEC line, Caco-2, and a human monocyte line, THP-1, as a control.
21867680	3	55	theme	IEC	677:679	arg1	line					716:719	a human monocyte line	699:719	a human monocyte line	699:719	In this study, we analyzed the underlying mechanisms for elevated transcription of the Tollip gene in IECs using a human IEC line, Caco-2, and a human monocyte line, THP-1, as a control.
21867680	7	56	theme	Elf-1-mediated	1238:1251	arg1	repression					1269:1278	Elf-1-mediated transcriptional repression	1238:1278	Elf-1-mediated transcriptional repression	1238:1278	Collectively, the results indicate that insufficient O-GlcNAc modification prevents Elf-1-mediated transcriptional repression and thereby upregulates Tollip gene expression in IECs.
21867680	6	57	theme	cells	1052:1056	arg1	Comparison					1021:1030	Comparison	1021:1030	Comparison of Caco-2 and THP-1 cells	1021:1056	Comparison of Caco-2 and THP-1 cells revealed that O-GlcNAc modification of Elf-1 was significantly lower in IECs than in monocytes.
21867680	7	58	theme	insufficient	1194:1205	arg1	modification					1216:1227	insufficient O-GlcNAc modification	1194:1227	insufficient O-GlcNAc modification	1194:1227	Collectively, the results indicate that insufficient O-GlcNAc modification prevents Elf-1-mediated transcriptional repression and thereby upregulates Tollip gene expression in IECs.
34608265	0	0	theme	cancer	59:64	arg1	metastasis					66:75	colorectal cancer metastasis	48:75	colorectal cancer metastasis	48:75	CEMIP, a novel adaptor protein of OGT, promotes colorectal cancer metastasis through glutamine metabolic reprogramming via reciprocal regulation of β-catenin.
34608265	6	1	theme	CEMIP	934:938	arg1	transcription					917:929	the transcription	913:929	the transcription of CEMIP	913:938	Furthermore, accumulated β-catenin in nucleus enhances the transcription of CEMIP to reciprocally regulate β-catenin and contributes to over-expression of glutaminase 1 and glutamine transporters (SLC1A5 and SLC38A2).
34608265	6	2	theme	glutaminase	1013:1023	arg1	SLC1A5					1055:1060	SLC1A5	1055:1060	SLC1A5	1055:1060	Furthermore, accumulated β-catenin in nucleus enhances the transcription of CEMIP to reciprocally regulate β-catenin and contributes to over-expression of glutaminase 1 and glutamine transporters (SLC1A5 and SLC38A2).
34608265	6	2	theme	glutaminase	1013:1023	arg1	SLC38A2					1066:1072	SLC38A2	1066:1072	SLC38A2	1066:1072	Furthermore, accumulated β-catenin in nucleus enhances the transcription of CEMIP to reciprocally regulate β-catenin and contributes to over-expression of glutaminase 1 and glutamine transporters (SLC1A5 and SLC38A2).
34608265	6	2	theme	glutaminase	1013:1023	arg1	over-expression					994:1008	over-expression	994:1008	over-expression of glutaminase 1	994:1025	Furthermore, accumulated β-catenin in nucleus enhances the transcription of CEMIP to reciprocally regulate β-catenin and contributes to over-expression of glutaminase 1 and glutamine transporters (SLC1A5 and SLC38A2).
34608265	6	2	theme	glutaminase	1013:1023	arg1	transporters					1041:1052	glutamine transporters	1031:1052	glutamine transporters (SLC1A5 and SLC38A2)	1031:1073	Furthermore, accumulated β-catenin in nucleus enhances the transcription of CEMIP to reciprocally regulate β-catenin and contributes to over-expression of glutaminase 1 and glutamine transporters (SLC1A5 and SLC38A2).
34608265	6	3	theme	glutamine	1031:1039	arg1	SLC38A2					1066:1072	SLC38A2	1066:1072	SLC38A2	1066:1072	Furthermore, accumulated β-catenin in nucleus enhances the transcription of CEMIP to reciprocally regulate β-catenin and contributes to over-expression of glutaminase 1 and glutamine transporters (SLC1A5 and SLC38A2).
34608265	6	3	theme	glutamine	1031:1039	arg1	SLC1A5					1055:1060	SLC1A5	1055:1060	SLC1A5	1055:1060	Furthermore, accumulated β-catenin in nucleus enhances the transcription of CEMIP to reciprocally regulate β-catenin and contributes to over-expression of glutaminase 1 and glutamine transporters (SLC1A5 and SLC38A2).
34608265	6	3	theme	glutamine	1031:1039	arg1	transporters					1041:1052	glutamine transporters	1031:1052	glutamine transporters (SLC1A5 and SLC38A2)	1031:1073	Furthermore, accumulated β-catenin in nucleus enhances the transcription of CEMIP to reciprocally regulate β-catenin and contributes to over-expression of glutaminase 1 and glutamine transporters (SLC1A5 and SLC38A2).
34608265	0	4	theme	colorectal	48:57	arg1	metastasis					66:75	colorectal cancer metastasis	48:75	colorectal cancer metastasis	48:75	CEMIP, a novel adaptor protein of OGT, promotes colorectal cancer metastasis through glutamine metabolic reprogramming via reciprocal regulation of β-catenin.
34608265	8	5	theme	reprogramming	1266:1278	arg1	importance					1232:1241	the importance	1228:1241	the importance of glutamine metabolic reprogramming in CEMIP-induced CRC metastasis	1228:1310	Collectively, this study reveals the importance of glutamine metabolic reprogramming in CEMIP-induced CRC metastasis, indicating the great potential of CEMIP and glutamine metabolism for CRC metastasis prevention.
34608265	8	6	theme	CRC	1382:1384	arg1	prevention					1397:1406	CRC metastasis prevention	1382:1406	CRC metastasis prevention	1382:1406	Collectively, this study reveals the importance of glutamine metabolic reprogramming in CEMIP-induced CRC metastasis, indicating the great potential of CEMIP and glutamine metabolism for CRC metastasis prevention.
34608265	8	7	theme	CRC	1297:1299	arg1	metastasis					1301:1310	CEMIP-induced CRC metastasis	1283:1310	CEMIP-induced CRC metastasis	1283:1310	Collectively, this study reveals the importance of glutamine metabolic reprogramming in CEMIP-induced CRC metastasis, indicating the great potential of CEMIP and glutamine metabolism for CRC metastasis prevention.
34608265	3	8	theme	intrinsic	349:357	arg1	reprogramming					329:341	Metabolic reprogramming	319:341	Metabolic reprogramming	319:341	Metabolic reprogramming is an intrinsic feature of cancer, which have complicated effects on cancer metastasis.
34608265	3	8	theme	intrinsic	349:357	arg1	feature					359:365	an intrinsic feature	346:365	an intrinsic feature	346:365	Metabolic reprogramming is an intrinsic feature of cancer, which have complicated effects on cancer metastasis.
34608265	5	9	from	O-GlcNAcylation	765:779	arg1	cytomembrane					844:855	cytomembrane	844:855	cytomembrane	844:855	Mechanistically, CEMIP interacts with OGT and β-catenin, which leads to elevated O-GlcNAcylation of β-catenin and enhanced β-catenin nuclear translocation from cytomembrane.
34608265	3	10	contain	have	384:387	arg2	effects					401:407	complicated effects	389:407	complicated effects	389:407	Metabolic reprogramming is an intrinsic feature of cancer, which have complicated effects on cancer metastasis.
34608265	3	10	contain	have	384:387	arg1	reprogramming					329:341	Metabolic reprogramming	319:341	Metabolic reprogramming	319:341	Metabolic reprogramming is an intrinsic feature of cancer, which have complicated effects on cancer metastasis.
34608265	3	10	contain	have	384:387	arg1	feature					359:365	an intrinsic feature	346:365	an intrinsic feature	346:365	Metabolic reprogramming is an intrinsic feature of cancer, which have complicated effects on cancer metastasis.
34608265	4	11	theme	adaptor	569:575	arg1	protein					477:483	a novel metastasis-related protein	450:483	a novel metastasis-related protein	450:483	Here, we find that a novel metastasis-related protein, cell migration-inducing and hyaluronan-binding protein (CEMIP), can act as a novel adaptor protein of O-GlcNAc transferase (OGT) to promote CRC metastasis through glutamine metabolic reprogramming.
34608265	4	11	theme	adaptor	569:575	arg1	protein					577:583	a novel adaptor protein	561:583	a novel adaptor protein of O-GlcNAc transferase (OGT)	561:613	Here, we find that a novel metastasis-related protein, cell migration-inducing and hyaluronan-binding protein (CEMIP), can act as a novel adaptor protein of O-GlcNAc transferase (OGT) to promote CRC metastasis through glutamine metabolic reprogramming.
34608265	4	12	theme	novel	452:456	arg1	protein					477:483	a novel metastasis-related protein	450:483	a novel metastasis-related protein	450:483	Here, we find that a novel metastasis-related protein, cell migration-inducing and hyaluronan-binding protein (CEMIP), can act as a novel adaptor protein of O-GlcNAc transferase (OGT) to promote CRC metastasis through glutamine metabolic reprogramming.
34608265	4	12	theme	novel	452:456	arg1	migration-inducing					491:508	migration-inducing	491:508	migration-inducing	491:508	Here, we find that a novel metastasis-related protein, cell migration-inducing and hyaluronan-binding protein (CEMIP), can act as a novel adaptor protein of O-GlcNAc transferase (OGT) to promote CRC metastasis through glutamine metabolic reprogramming.
34608265	4	12	theme	novel	452:456	arg1	protein					533:539	cell migration-inducing and hyaluronan-binding protein	486:539	protein	533:539	Here, we find that a novel metastasis-related protein, cell migration-inducing and hyaluronan-binding protein (CEMIP), can act as a novel adaptor protein of O-GlcNAc transferase (OGT) to promote CRC metastasis through glutamine metabolic reprogramming.
34608265	4	12	theme	novel	452:456	arg1	protein					577:583	a novel adaptor protein	561:583	a novel adaptor protein of O-GlcNAc transferase (OGT)	561:613	Here, we find that a novel metastasis-related protein, cell migration-inducing and hyaluronan-binding protein (CEMIP), can act as a novel adaptor protein of O-GlcNAc transferase (OGT) to promote CRC metastasis through glutamine metabolic reprogramming.
34608265	8	13	theme	metastasis	1386:1395	arg1	prevention					1397:1406	CRC metastasis prevention	1382:1406	CRC metastasis prevention	1382:1406	Collectively, this study reveals the importance of glutamine metabolic reprogramming in CEMIP-induced CRC metastasis, indicating the great potential of CEMIP and glutamine metabolism for CRC metastasis prevention.
34608265	4	14	theme	novel	563:567	arg1	protein					477:483	a novel metastasis-related protein	450:483	a novel metastasis-related protein	450:483	Here, we find that a novel metastasis-related protein, cell migration-inducing and hyaluronan-binding protein (CEMIP), can act as a novel adaptor protein of O-GlcNAc transferase (OGT) to promote CRC metastasis through glutamine metabolic reprogramming.
34608265	4	14	theme	novel	563:567	arg1	protein					577:583	a novel adaptor protein	561:583	a novel adaptor protein of O-GlcNAc transferase (OGT)	561:613	Here, we find that a novel metastasis-related protein, cell migration-inducing and hyaluronan-binding protein (CEMIP), can act as a novel adaptor protein of O-GlcNAc transferase (OGT) to promote CRC metastasis through glutamine metabolic reprogramming.
34608265	0	15	theme	metabolic	95:103	arg1	reprogramming					105:117	glutamine metabolic reprogramming	85:117	glutamine metabolic reprogramming	85:117	CEMIP, a novel adaptor protein of OGT, promotes colorectal cancer metastasis through glutamine metabolic reprogramming via reciprocal regulation of β-catenin.
34608265	6	16	dep	transporters	1041:1052	arg1	SLC38A2					1066:1072	SLC38A2	1066:1072	SLC38A2	1066:1072	Furthermore, accumulated β-catenin in nucleus enhances the transcription of CEMIP to reciprocally regulate β-catenin and contributes to over-expression of glutaminase 1 and glutamine transporters (SLC1A5 and SLC38A2).
34608265	6	16	dep	transporters	1041:1052	arg1	SLC1A5					1055:1060	SLC1A5	1055:1060	SLC1A5	1055:1060	Furthermore, accumulated β-catenin in nucleus enhances the transcription of CEMIP to reciprocally regulate β-catenin and contributes to over-expression of glutaminase 1 and glutamine transporters (SLC1A5 and SLC38A2).
34608265	6	16	dep	transporters	1041:1052	arg1	transporters					1041:1052	glutamine transporters	1031:1052	glutamine transporters (SLC1A5 and SLC38A2)	1031:1073	Furthermore, accumulated β-catenin in nucleus enhances the transcription of CEMIP to reciprocally regulate β-catenin and contributes to over-expression of glutaminase 1 and glutamine transporters (SLC1A5 and SLC38A2).
34608265	2	17	theme	molecular	257:265	arg1	mechanisms					267:276	the underlying molecular mechanisms	242:276	the underlying molecular mechanisms of CRC metastasis	242:294	However, the underlying molecular mechanisms of CRC metastasis are poorly understood.
34608265	3	18	theme	cancer	412:417	arg1	metastasis					419:428	cancer metastasis	412:428	cancer metastasis	412:428	Metabolic reprogramming is an intrinsic feature of cancer, which have complicated effects on cancer metastasis.
34608265	4	19	theme	CRC	626:628	arg1	metastasis					630:639	CRC metastasis	626:639	CRC metastasis	626:639	Here, we find that a novel metastasis-related protein, cell migration-inducing and hyaluronan-binding protein (CEMIP), can act as a novel adaptor protein of O-GlcNAc transferase (OGT) to promote CRC metastasis through glutamine metabolic reprogramming.
34608265	0	20	theme	glutamine	85:93	arg1	reprogramming					105:117	glutamine metabolic reprogramming	85:117	glutamine metabolic reprogramming	85:117	CEMIP, a novel adaptor protein of OGT, promotes colorectal cancer metastasis through glutamine metabolic reprogramming via reciprocal regulation of β-catenin.
34608265	8	21	theme	metabolic	1256:1264	arg1	reprogramming					1266:1278	glutamine metabolic reprogramming	1246:1278	glutamine metabolic reprogramming	1246:1278	Collectively, this study reveals the importance of glutamine metabolic reprogramming in CEMIP-induced CRC metastasis, indicating the great potential of CEMIP and glutamine metabolism for CRC metastasis prevention.
34608265	2	22	theme	underlying	246:255	arg1	mechanisms					267:276	the underlying molecular mechanisms	242:276	the underlying molecular mechanisms of CRC metastasis	242:294	However, the underlying molecular mechanisms of CRC metastasis are poorly understood.
34608265	8	23	theme	CEMIP-induced	1283:1295	arg1	metastasis					1301:1310	CEMIP-induced CRC metastasis	1283:1310	CEMIP-induced CRC metastasis	1283:1310	Collectively, this study reveals the importance of glutamine metabolic reprogramming in CEMIP-induced CRC metastasis, indicating the great potential of CEMIP and glutamine metabolism for CRC metastasis prevention.
34608265	4	24	theme	metastasis-related	458:475	arg1	protein					477:483	a novel metastasis-related protein	450:483	a novel metastasis-related protein	450:483	Here, we find that a novel metastasis-related protein, cell migration-inducing and hyaluronan-binding protein (CEMIP), can act as a novel adaptor protein of O-GlcNAc transferase (OGT) to promote CRC metastasis through glutamine metabolic reprogramming.
34608265	4	24	theme	metastasis-related	458:475	arg1	migration-inducing					491:508	migration-inducing	491:508	migration-inducing	491:508	Here, we find that a novel metastasis-related protein, cell migration-inducing and hyaluronan-binding protein (CEMIP), can act as a novel adaptor protein of O-GlcNAc transferase (OGT) to promote CRC metastasis through glutamine metabolic reprogramming.
34608265	4	24	theme	metastasis-related	458:475	arg1	protein					533:539	cell migration-inducing and hyaluronan-binding protein	486:539	protein	533:539	Here, we find that a novel metastasis-related protein, cell migration-inducing and hyaluronan-binding protein (CEMIP), can act as a novel adaptor protein of O-GlcNAc transferase (OGT) to promote CRC metastasis through glutamine metabolic reprogramming.
34608265	4	24	theme	metastasis-related	458:475	arg1	protein					577:583	a novel adaptor protein	561:583	a novel adaptor protein of O-GlcNAc transferase (OGT)	561:613	Here, we find that a novel metastasis-related protein, cell migration-inducing and hyaluronan-binding protein (CEMIP), can act as a novel adaptor protein of O-GlcNAc transferase (OGT) to promote CRC metastasis through glutamine metabolic reprogramming.
34608265	7	25	theme	glutamine	1114:1122	arg1	metabolism					1124:1133	glutamine metabolism	1114:1133	glutamine metabolism	1114:1133	Combinational inhibition of CEMIP and glutamine metabolism could dramatically attenuate the metastasis of CRC in vivo.
34608265	1	26	theme	leading	177:183	arg1	cause					185:189	the leading cause	173:189	the leading cause of colorectal cancer (CRC)-induced death	173:230	Metastasis is the leading cause of colorectal cancer (CRC)-induced death.
34608265	1	26	theme	leading	177:183	arg1	Metastasis					159:168	Metastasis	159:168	Metastasis	159:168	Metastasis is the leading cause of colorectal cancer (CRC)-induced death.
34608265	5	27	theme	enhanced	798:805	arg1	translocation					825:837	enhanced β-catenin nuclear translocation	798:837	enhanced β-catenin nuclear translocation from cytomembrane	798:855	Mechanistically, CEMIP interacts with OGT and β-catenin, which leads to elevated O-GlcNAcylation of β-catenin and enhanced β-catenin nuclear translocation from cytomembrane.
34608265	7	28	theme	metabolism	1124:1133	arg1	inhibition					1090:1099	Combinational inhibition	1076:1099	Combinational inhibition of CEMIP and glutamine metabolism	1076:1133	Combinational inhibition of CEMIP and glutamine metabolism could dramatically attenuate the metastasis of CRC in vivo.
34608265	8	29	from	importance	1232:1241	arg1	metastasis					1301:1310	CEMIP-induced CRC metastasis	1283:1310	CEMIP-induced CRC metastasis	1283:1310	Collectively, this study reveals the importance of glutamine metabolic reprogramming in CEMIP-induced CRC metastasis, indicating the great potential of CEMIP and glutamine metabolism for CRC metastasis prevention.
34608265	0	30	theme	novel	9:13	arg1	protein					23:29	a novel adaptor protein	7:29	a novel adaptor protein of OGT	7:36	CEMIP, a novel adaptor protein of OGT, promotes colorectal cancer metastasis through glutamine metabolic reprogramming via reciprocal regulation of β-catenin.
34608265	0	30	theme	novel	9:13	arg1	CEMIP					0:4	CEMIP	0:4	CEMIP	0:4	CEMIP, a novel adaptor protein of OGT, promotes colorectal cancer metastasis through glutamine metabolic reprogramming via reciprocal regulation of β-catenin.
34608265	7	31	theme	CEMIP	1104:1108	arg1	inhibition					1090:1099	Combinational inhibition	1076:1099	Combinational inhibition of CEMIP and glutamine metabolism	1076:1133	Combinational inhibition of CEMIP and glutamine metabolism could dramatically attenuate the metastasis of CRC in vivo.
34608265	2	32	theme	metastasis	285:294	arg1	mechanisms					267:276	the underlying molecular mechanisms	242:276	the underlying molecular mechanisms of CRC metastasis	242:294	However, the underlying molecular mechanisms of CRC metastasis are poorly understood.
34608265	5	33	theme	translocation	825:837	arg1	O-GlcNAcylation					765:779	elevated O-GlcNAcylation	756:779	elevated O-GlcNAcylation of β-catenin and enhanced β-catenin nuclear translocation from cytomembrane	756:855	Mechanistically, CEMIP interacts with OGT and β-catenin, which leads to elevated O-GlcNAcylation of β-catenin and enhanced β-catenin nuclear translocation from cytomembrane.
34608265	3	34	theme	cancer	370:375	arg1	reprogramming					329:341	Metabolic reprogramming	319:341	Metabolic reprogramming	319:341	Metabolic reprogramming is an intrinsic feature of cancer, which have complicated effects on cancer metastasis.
34608265	3	34	theme	cancer	370:375	arg1	feature					359:365	an intrinsic feature	346:365	an intrinsic feature	346:365	Metabolic reprogramming is an intrinsic feature of cancer, which have complicated effects on cancer metastasis.
34608265	1	35	dep	-induced	217:224	arg1	cancer					205:210	colorectal cancer	194:210	colorectal cancer	194:210	Metastasis is the leading cause of colorectal cancer (CRC)-induced death.
34608265	2	36	theme	CRC	281:283	arg1	metastasis					285:294	CRC metastasis	281:294	CRC metastasis	281:294	However, the underlying molecular mechanisms of CRC metastasis are poorly understood.
34608265	5	37	theme	β-catenin	784:792	arg1	O-GlcNAcylation					765:779	elevated O-GlcNAcylation	756:779	elevated O-GlcNAcylation of β-catenin and enhanced β-catenin nuclear translocation from cytomembrane	756:855	Mechanistically, CEMIP interacts with OGT and β-catenin, which leads to elevated O-GlcNAcylation of β-catenin and enhanced β-catenin nuclear translocation from cytomembrane.
34608265	1	38	theme	colorectal	194:203	arg1	cancer					205:210	colorectal cancer	194:210	colorectal cancer	194:210	Metastasis is the leading cause of colorectal cancer (CRC)-induced death.
34608265	5	39	theme	elevated	756:763	arg1	O-GlcNAcylation					765:779	elevated O-GlcNAcylation	756:779	elevated O-GlcNAcylation of β-catenin and enhanced β-catenin nuclear translocation from cytomembrane	756:855	Mechanistically, CEMIP interacts with OGT and β-catenin, which leads to elevated O-GlcNAcylation of β-catenin and enhanced β-catenin nuclear translocation from cytomembrane.
34608265	6	40	theme	accumulated	871:881	arg1	β-catenin					883:891	accumulated β-catenin	871:891	accumulated β-catenin in nucleus	871:902	Furthermore, accumulated β-catenin in nucleus enhances the transcription of CEMIP to reciprocally regulate β-catenin and contributes to over-expression of glutaminase 1 and glutamine transporters (SLC1A5 and SLC38A2).
34608265	6	41	from	β-catenin	883:891	arg1	nucleus					896:902	nucleus	896:902	nucleus	896:902	Furthermore, accumulated β-catenin in nucleus enhances the transcription of CEMIP to reciprocally regulate β-catenin and contributes to over-expression of glutaminase 1 and glutamine transporters (SLC1A5 and SLC38A2).
34608265	0	42	theme	adaptor	15:21	arg1	protein					23:29	a novel adaptor protein	7:29	a novel adaptor protein of OGT	7:36	CEMIP, a novel adaptor protein of OGT, promotes colorectal cancer metastasis through glutamine metabolic reprogramming via reciprocal regulation of β-catenin.
34608265	0	42	theme	adaptor	15:21	arg1	CEMIP					0:4	CEMIP	0:4	CEMIP	0:4	CEMIP, a novel adaptor protein of OGT, promotes colorectal cancer metastasis through glutamine metabolic reprogramming via reciprocal regulation of β-catenin.
34608265	0	43	theme	reciprocal	123:132	arg1	regulation					134:143	reciprocal regulation	123:143	reciprocal regulation of β-catenin	123:156	CEMIP, a novel adaptor protein of OGT, promotes colorectal cancer metastasis through glutamine metabolic reprogramming via reciprocal regulation of β-catenin.
34608265	4	44	theme	transferase	597:607	arg1	protein					477:483	a novel metastasis-related protein	450:483	a novel metastasis-related protein	450:483	Here, we find that a novel metastasis-related protein, cell migration-inducing and hyaluronan-binding protein (CEMIP), can act as a novel adaptor protein of O-GlcNAc transferase (OGT) to promote CRC metastasis through glutamine metabolic reprogramming.
34608265	4	44	theme	transferase	597:607	arg1	protein					577:583	a novel adaptor protein	561:583	a novel adaptor protein of O-GlcNAc transferase (OGT)	561:613	Here, we find that a novel metastasis-related protein, cell migration-inducing and hyaluronan-binding protein (CEMIP), can act as a novel adaptor protein of O-GlcNAc transferase (OGT) to promote CRC metastasis through glutamine metabolic reprogramming.
34608265	5	45	from	cytomembrane	844:855	arg1	translocation					825:837	enhanced β-catenin nuclear translocation	798:837	enhanced β-catenin nuclear translocation from cytomembrane	798:855	Mechanistically, CEMIP interacts with OGT and β-catenin, which leads to elevated O-GlcNAcylation of β-catenin and enhanced β-catenin nuclear translocation from cytomembrane.
34608265	5	45	from	cytomembrane	844:855	arg1	β-catenin					784:792	β-catenin	784:792	β-catenin	784:792	Mechanistically, CEMIP interacts with OGT and β-catenin, which leads to elevated O-GlcNAcylation of β-catenin and enhanced β-catenin nuclear translocation from cytomembrane.
34608265	5	45	from	cytomembrane	844:855	arg1	O-GlcNAcylation					765:779	elevated O-GlcNAcylation	756:779	elevated O-GlcNAcylation of β-catenin and enhanced β-catenin nuclear translocation from cytomembrane	756:855	Mechanistically, CEMIP interacts with OGT and β-catenin, which leads to elevated O-GlcNAcylation of β-catenin and enhanced β-catenin nuclear translocation from cytomembrane.
34608265	5	46	theme	β-catenin	807:815	arg1	translocation					825:837	enhanced β-catenin nuclear translocation	798:837	enhanced β-catenin nuclear translocation from cytomembrane	798:855	Mechanistically, CEMIP interacts with OGT and β-catenin, which leads to elevated O-GlcNAcylation of β-catenin and enhanced β-catenin nuclear translocation from cytomembrane.
34608265	0	47	theme	OGT	34:36	arg1	protein					23:29	a novel adaptor protein	7:29	a novel adaptor protein of OGT	7:36	CEMIP, a novel adaptor protein of OGT, promotes colorectal cancer metastasis through glutamine metabolic reprogramming via reciprocal regulation of β-catenin.
34608265	0	47	theme	OGT	34:36	arg1	CEMIP					0:4	CEMIP	0:4	CEMIP	0:4	CEMIP, a novel adaptor protein of OGT, promotes colorectal cancer metastasis through glutamine metabolic reprogramming via reciprocal regulation of β-catenin.
34608265	4	48	theme	hyaluronan-binding	514:531	arg1	protein					477:483	a novel metastasis-related protein	450:483	a novel metastasis-related protein	450:483	Here, we find that a novel metastasis-related protein, cell migration-inducing and hyaluronan-binding protein (CEMIP), can act as a novel adaptor protein of O-GlcNAc transferase (OGT) to promote CRC metastasis through glutamine metabolic reprogramming.
34608265	4	48	theme	hyaluronan-binding	514:531	arg1	protein					533:539	cell migration-inducing and hyaluronan-binding protein	486:539	protein	533:539	Here, we find that a novel metastasis-related protein, cell migration-inducing and hyaluronan-binding protein (CEMIP), can act as a novel adaptor protein of O-GlcNAc transferase (OGT) to promote CRC metastasis through glutamine metabolic reprogramming.
34608265	0	49	theme	β-catenin	148:156	arg1	regulation					134:143	reciprocal regulation	123:143	reciprocal regulation of β-catenin	123:156	CEMIP, a novel adaptor protein of OGT, promotes colorectal cancer metastasis through glutamine metabolic reprogramming via reciprocal regulation of β-catenin.
34608265	8	50	theme	CEMIP	1347:1351	arg1	potential					1334:1342	the great potential	1324:1342	the great potential of CEMIP and glutamine metabolism for CRC metastasis prevention	1324:1406	Collectively, this study reveals the importance of glutamine metabolic reprogramming in CEMIP-induced CRC metastasis, indicating the great potential of CEMIP and glutamine metabolism for CRC metastasis prevention.
34608265	3	51	theme	complicated	389:399	arg1	effects					401:407	complicated effects	389:407	complicated effects	389:407	Metabolic reprogramming is an intrinsic feature of cancer, which have complicated effects on cancer metastasis.
34608265	7	52	theme	Combinational	1076:1088	arg1	inhibition					1090:1099	Combinational inhibition	1076:1099	Combinational inhibition of CEMIP and glutamine metabolism	1076:1133	Combinational inhibition of CEMIP and glutamine metabolism could dramatically attenuate the metastasis of CRC in vivo.
34608265	8	53	theme	glutamine	1357:1365	arg1	metabolism					1367:1376	glutamine metabolism	1357:1376	glutamine metabolism	1357:1376	Collectively, this study reveals the importance of glutamine metabolic reprogramming in CEMIP-induced CRC metastasis, indicating the great potential of CEMIP and glutamine metabolism for CRC metastasis prevention.
34608265	5	54	theme	nuclear	817:823	arg1	translocation					825:837	enhanced β-catenin nuclear translocation	798:837	enhanced β-catenin nuclear translocation from cytomembrane	798:855	Mechanistically, CEMIP interacts with OGT and β-catenin, which leads to elevated O-GlcNAcylation of β-catenin and enhanced β-catenin nuclear translocation from cytomembrane.
34608265	8	55	theme	metabolism	1367:1376	arg1	potential					1334:1342	the great potential	1324:1342	the great potential of CEMIP and glutamine metabolism for CRC metastasis prevention	1324:1406	Collectively, this study reveals the importance of glutamine metabolic reprogramming in CEMIP-induced CRC metastasis, indicating the great potential of CEMIP and glutamine metabolism for CRC metastasis prevention.
34608265	8	56	theme	glutamine	1246:1254	arg1	reprogramming					1266:1278	glutamine metabolic reprogramming	1246:1278	glutamine metabolic reprogramming	1246:1278	Collectively, this study reveals the importance of glutamine metabolic reprogramming in CEMIP-induced CRC metastasis, indicating the great potential of CEMIP and glutamine metabolism for CRC metastasis prevention.
34608265	3	57	theme	Metabolic	319:327	arg1	reprogramming					329:341	Metabolic reprogramming	319:341	Metabolic reprogramming	319:341	Metabolic reprogramming is an intrinsic feature of cancer, which have complicated effects on cancer metastasis.
34608265	3	57	theme	Metabolic	319:327	arg1	feature					359:365	an intrinsic feature	346:365	an intrinsic feature	346:365	Metabolic reprogramming is an intrinsic feature of cancer, which have complicated effects on cancer metastasis.
34608265	8	58	theme	great	1328:1332	arg1	potential					1334:1342	the great potential	1324:1342	the great potential of CEMIP and glutamine metabolism for CRC metastasis prevention	1324:1406	Collectively, this study reveals the importance of glutamine metabolic reprogramming in CEMIP-induced CRC metastasis, indicating the great potential of CEMIP and glutamine metabolism for CRC metastasis prevention.
34608265	4	59	theme	metabolic	659:667	arg1	reprogramming					669:681	glutamine metabolic reprogramming	649:681	glutamine metabolic reprogramming	649:681	Here, we find that a novel metastasis-related protein, cell migration-inducing and hyaluronan-binding protein (CEMIP), can act as a novel adaptor protein of O-GlcNAc transferase (OGT) to promote CRC metastasis through glutamine metabolic reprogramming.
34608265	1	60	theme	-induced	217:224	arg1	death					226:230	colorectal cancer (CRC)-induced death	194:230	colorectal cancer (CRC)-induced death	194:230	Metastasis is the leading cause of colorectal cancer (CRC)-induced death.
34608265	7	61	theme	CRC	1182:1184	arg1	metastasis					1168:1177	the metastasis	1164:1177	the metastasis of CRC	1164:1184	Combinational inhibition of CEMIP and glutamine metabolism could dramatically attenuate the metastasis of CRC in vivo.
34608265	4	62	theme	O-GlcNAc	588:595	arg1	OGT					610:612	OGT	610:612	OGT	610:612	Here, we find that a novel metastasis-related protein, cell migration-inducing and hyaluronan-binding protein (CEMIP), can act as a novel adaptor protein of O-GlcNAc transferase (OGT) to promote CRC metastasis through glutamine metabolic reprogramming.
34608265	4	62	theme	O-GlcNAc	588:595	arg1	transferase					597:607	O-GlcNAc transferase	588:607	O-GlcNAc transferase (OGT)	588:613	Here, we find that a novel metastasis-related protein, cell migration-inducing and hyaluronan-binding protein (CEMIP), can act as a novel adaptor protein of O-GlcNAc transferase (OGT) to promote CRC metastasis through glutamine metabolic reprogramming.
34608265	4	63	theme	glutamine	649:657	arg1	reprogramming					669:681	glutamine metabolic reprogramming	649:681	glutamine metabolic reprogramming	649:681	Here, we find that a novel metastasis-related protein, cell migration-inducing and hyaluronan-binding protein (CEMIP), can act as a novel adaptor protein of O-GlcNAc transferase (OGT) to promote CRC metastasis through glutamine metabolic reprogramming.
34608265	1	64	theme	death	226:230	arg1	cause					185:189	the leading cause	173:189	the leading cause of colorectal cancer (CRC)-induced death	173:230	Metastasis is the leading cause of colorectal cancer (CRC)-induced death.
34608265	1	64	theme	death	226:230	arg1	Metastasis					159:168	Metastasis	159:168	Metastasis	159:168	Metastasis is the leading cause of colorectal cancer (CRC)-induced death.
32149084	6	0	theme	cell	1029:1032	arg1	apoptosis					1034:1042	triggered cell apoptosis	1019:1042	triggered cell apoptosis	1019:1042	Genetic silencing or pharmacological inhibition of the first and rate-limiting enzyme of the HBP, glutamine:fructose-6-phosphate amidotransferase 1 (GFAT1), inhibited PDAC cell proliferation, invasive capacity, and triggered cell apoptosis.
32149084	6	1	theme	HBP	897:899	arg1	glutamine					902:910	glutamine:fructose-6-phosphate amidotransferase 1 (GFAT1)	902:958	glutamine:fructose-6-phosphate amidotransferase 1 (GFAT1)	902:958	Genetic silencing or pharmacological inhibition of the first and rate-limiting enzyme of the HBP, glutamine:fructose-6-phosphate amidotransferase 1 (GFAT1), inhibited PDAC cell proliferation, invasive capacity, and triggered cell apoptosis.
32149084	6	1	theme	HBP	897:899	arg1	enzyme					883:888	the first and rate-limiting enzyme	855:888	the first and rate-limiting enzyme of the HBP	855:899	Genetic silencing or pharmacological inhibition of the first and rate-limiting enzyme of the HBP, glutamine:fructose-6-phosphate amidotransferase 1 (GFAT1), inhibited PDAC cell proliferation, invasive capacity, and triggered cell apoptosis.
32149084	8	2	theme	pharmacological	1163:1177	arg1	inhibition					1179:1188	pharmacological inhibition	1163:1188	pharmacological inhibition of GFAT1 with 6-diazo-5-oxo-l-norleucine (DON) or Azaserine	1163:1248	Moreover, similar antitumor effects were noticed by pharmacological inhibition of GFAT1 with 6-diazo-5-oxo-l-norleucine (DON) or Azaserine.
32149084	4	3	theme	prognostic	604:613	arg1	value					615:619	its prognostic value	600:619	its prognostic value across 33 types of human cancers	600:652	In this study, we analyzed the activity of the HBP and its prognostic value across 33 types of human cancers.
32149084	13	4	theme	higher	1783:1788	arg1	GFAT1/HBP/O-GlcNAcylation					1790:1814	higher GFAT1/HBP/O-GlcNAcylation	1783:1814	higher GFAT1/HBP/O-GlcNAcylation	1783:1814	Collectively, our findings indicate that higher GFAT1/HBP/O-GlcNAcylation exhibits tumor-promoting roles by maintaining β-catenin activity in PDAC.
32149084	6	5	theme	rate-limiting	869:881	arg1	glutamine					902:910	glutamine:fructose-6-phosphate amidotransferase 1 (GFAT1)	902:958	glutamine:fructose-6-phosphate amidotransferase 1 (GFAT1)	902:958	Genetic silencing or pharmacological inhibition of the first and rate-limiting enzyme of the HBP, glutamine:fructose-6-phosphate amidotransferase 1 (GFAT1), inhibited PDAC cell proliferation, invasive capacity, and triggered cell apoptosis.
32149084	6	5	theme	rate-limiting	869:881	arg1	enzyme					883:888	the first and rate-limiting enzyme	855:888	the first and rate-limiting enzyme of the HBP	855:899	Genetic silencing or pharmacological inhibition of the first and rate-limiting enzyme of the HBP, glutamine:fructose-6-phosphate amidotransferase 1 (GFAT1), inhibited PDAC cell proliferation, invasive capacity, and triggered cell apoptosis.
32149084	11	6	theme	genes	1577:1581	arg1	activity					1521:1528	β-catenin activity	1511:1528	β-catenin activity	1511:1528	TOP/FOP-Flash and real-time qPCR analysis showed that GFAT1 knockdown inhibited β-catenin activity and the transcription of its downstream target genes CCND1 and MYC.
32149084	11	6	theme	genes	1577:1581	arg1	transcription					1538:1550	the transcription	1534:1550	the transcription of its downstream target genes CCND1 and MYC	1534:1595	TOP/FOP-Flash and real-time qPCR analysis showed that GFAT1 knockdown inhibited β-catenin activity and the transcription of its downstream target genes CCND1 and MYC.
32149084	5	7	theme	higher	739:744	arg1	activity					750:757	higher HBP activity	739:757	higher HBP activity	739:757	Increased HBP activity was observed in pancreatic ductal adenocarcinoma (PDAC), and higher HBP activity predicted a poor prognosis in PDAC patients.
32149084	6	8	theme	fructose-6-phosphate	912:931	arg1	amidotransferase					933:948	fructose-6-phosphate amidotransferase 1	912:950	glutamine:fructose-6-phosphate amidotransferase 1 (GFAT1)	902:958	Genetic silencing or pharmacological inhibition of the first and rate-limiting enzyme of the HBP, glutamine:fructose-6-phosphate amidotransferase 1 (GFAT1), inhibited PDAC cell proliferation, invasive capacity, and triggered cell apoptosis.
32149084	6	8	theme	fructose-6-phosphate	912:931	arg1	GFAT1					953:957	GFAT1	953:957	GFAT1	953:957	Genetic silencing or pharmacological inhibition of the first and rate-limiting enzyme of the HBP, glutamine:fructose-6-phosphate amidotransferase 1 (GFAT1), inhibited PDAC cell proliferation, invasive capacity, and triggered cell apoptosis.
32149084	3	9	theme	tumors	434:439	arg1	spectrum					408:415	the spectrum	404:415	the spectrum of HBP-dependent tumors	404:439	However, the spectrum of HBP-dependent tumors and the mechanisms by which the HBP promotes tumor aggressiveness remain areas of active investigation.
32149084	3	9	theme	tumors	434:439	arg1	mechanisms					449:458	the mechanisms	445:458	the mechanisms by which the HBP promotes tumor aggressiveness	445:505	However, the spectrum of HBP-dependent tumors and the mechanisms by which the HBP promotes tumor aggressiveness remain areas of active investigation.
32149084	5	10	theme	HBP	746:748	arg1	activity					750:757	higher HBP activity	739:757	higher HBP activity	739:757	Increased HBP activity was observed in pancreatic ductal adenocarcinoma (PDAC), and higher HBP activity predicted a poor prognosis in PDAC patients.
32149084	12	11	theme	form	1633:1636	arg1	expression					1606:1615	Ectopic expression	1598:1615	Ectopic expression of a stabilized form of β-catenin	1598:1649	Ectopic expression of a stabilized form of β-catenin restored the suppressive roles of GFAT1 knockdown on PDAC cell proliferation and invasion.
32149084	12	12	theme	knockdown	1691:1699	arg1	roles					1676:1680	the suppressive roles	1660:1680	the suppressive roles of GFAT1 knockdown on PDAC cell proliferation and invasion	1660:1739	Ectopic expression of a stabilized form of β-catenin restored the suppressive roles of GFAT1 knockdown on PDAC cell proliferation and invasion.
32149084	3	13	theme	active	523:528	arg1	investigation					530:542	active investigation	523:542	active investigation	523:542	However, the spectrum of HBP-dependent tumors and the mechanisms by which the HBP promotes tumor aggressiveness remain areas of active investigation.
32149084	8	14	theme	GFAT1	1193:1197	arg1	inhibition					1179:1188	pharmacological inhibition	1163:1188	pharmacological inhibition of GFAT1 with 6-diazo-5-oxo-l-norleucine (DON) or Azaserine	1163:1248	Moreover, similar antitumor effects were noticed by pharmacological inhibition of GFAT1 with 6-diazo-5-oxo-l-norleucine (DON) or Azaserine.
32149084	7	15	theme	UDP-GlcNAc	1099:1108	arg1	addition					1087:1094	addition	1087:1094	addition of UDP-GlcNAc	1087:1108	Notably, these effects can be restored by addition of UDP-GlcNAc.
32149084	2	16	theme	diphosphate	302:312	arg1	N-acetylglucosamine					314:332	uridine diphosphate N-acetylglucosamine	294:332	uridine diphosphate N-acetylglucosamine (UDP-GlcNAc)	294:345	As a branch of glucose and metabolism, the hexosamine biosynthesis pathway (HBP) generates uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) and contributes to the O-GlcNAcylation process.
32149084	2	16	theme	diphosphate	302:312	arg1	branch					208:213	a branch	206:213	a branch of glucose and metabolism	206:239	As a branch of glucose and metabolism, the hexosamine biosynthesis pathway (HBP) generates uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) and contributes to the O-GlcNAcylation process.
32149084	2	16	theme	diphosphate	302:312	arg1	UDP-GlcNAc					335:344	UDP-GlcNAc	335:344	UDP-GlcNAc	335:344	As a branch of glucose and metabolism, the hexosamine biosynthesis pathway (HBP) generates uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) and contributes to the O-GlcNAcylation process.
32149084	11	17	theme	β-catenin	1511:1519	arg1	activity					1521:1528	β-catenin activity	1511:1528	β-catenin activity	1511:1528	TOP/FOP-Flash and real-time qPCR analysis showed that GFAT1 knockdown inhibited β-catenin activity and the transcription of its downstream target genes CCND1 and MYC.
32149084	6	18	theme	invasive	996:1003	arg1	capacity					1005:1012	invasive capacity	996:1012	invasive capacity	996:1012	Genetic silencing or pharmacological inhibition of the first and rate-limiting enzyme of the HBP, glutamine:fructose-6-phosphate amidotransferase 1 (GFAT1), inhibited PDAC cell proliferation, invasive capacity, and triggered cell apoptosis.
32149084	12	19	theme	Ectopic	1598:1604	arg1	expression					1606:1615	Ectopic expression	1598:1615	Ectopic expression of a stabilized form of β-catenin	1598:1649	Ectopic expression of a stabilized form of β-catenin restored the suppressive roles of GFAT1 knockdown on PDAC cell proliferation and invasion.
32149084	6	20	theme	Genetic	804:810	arg1	silencing					812:820	Genetic silencing	804:820	Genetic silencing	804:820	Genetic silencing or pharmacological inhibition of the first and rate-limiting enzyme of the HBP, glutamine:fructose-6-phosphate amidotransferase 1 (GFAT1), inhibited PDAC cell proliferation, invasive capacity, and triggered cell apoptosis.
32149084	1	21	theme	Reprogrammed	105:116	arg1	metabolism					140:149	Reprogrammed glucose and glutamine metabolism	105:149	Reprogrammed glucose and glutamine metabolism	105:149	Reprogrammed glucose and glutamine metabolism are essential for tumor initiation and development.
32149084	11	22	theme	GFAT1	1485:1489	arg1	knockdown					1491:1499	GFAT1 knockdown	1485:1499	GFAT1 knockdown	1485:1499	TOP/FOP-Flash and real-time qPCR analysis showed that GFAT1 knockdown inhibited β-catenin activity and the transcription of its downstream target genes CCND1 and MYC.
32149084	11	23	theme	qPCR	1459:1462	arg1	analysis					1464:1471	real-time qPCR analysis	1449:1471	real-time qPCR analysis	1449:1471	TOP/FOP-Flash and real-time qPCR analysis showed that GFAT1 knockdown inhibited β-catenin activity and the transcription of its downstream target genes CCND1 and MYC.
32149084	3	24	theme	HBP-dependent	420:432	arg1	tumors					434:439	HBP-dependent tumors	420:439	HBP-dependent tumors	420:439	However, the spectrum of HBP-dependent tumors and the mechanisms by which the HBP promotes tumor aggressiveness remain areas of active investigation.
32149084	6	25	theme	PDAC	971:974	arg1	proliferation					981:993	PDAC cell proliferation	971:993	PDAC cell proliferation	971:993	Genetic silencing or pharmacological inhibition of the first and rate-limiting enzyme of the HBP, glutamine:fructose-6-phosphate amidotransferase 1 (GFAT1), inhibited PDAC cell proliferation, invasive capacity, and triggered cell apoptosis.
32149084	5	26	theme	Increased	655:663	arg1	activity					669:676	Increased HBP activity	655:676	Increased HBP activity	655:676	Increased HBP activity was observed in pancreatic ductal adenocarcinoma (PDAC), and higher HBP activity predicted a poor prognosis in PDAC patients.
32149084	1	27	theme	glucose	118:124	arg1	metabolism					140:149	Reprogrammed glucose and glutamine metabolism	105:149	Reprogrammed glucose and glutamine metabolism	105:149	Reprogrammed glucose and glutamine metabolism are essential for tumor initiation and development.
32149084	0	28	theme	GFAT1/HBP/O-GlcNAcylation	0:24	arg1	Axis					26:29	GFAT1/HBP/O-GlcNAcylation Axis	0:29	GFAT1/HBP/O-GlcNAcylation Axis	0:29	GFAT1/HBP/O-GlcNAcylation Axis Regulates β-Catenin Activity to Promote Pancreatic Cancer Aggressiveness.
32149084	5	29	theme	HBP	665:667	arg1	activity					669:676	Increased HBP activity	655:676	Increased HBP activity	655:676	Increased HBP activity was observed in pancreatic ductal adenocarcinoma (PDAC), and higher HBP activity predicted a poor prognosis in PDAC patients.
32149084	8	30	with	inhibition	1179:1188	arg1	DON					1232:1234	DON	1232:1234	DON	1232:1234	Moreover, similar antitumor effects were noticed by pharmacological inhibition of GFAT1 with 6-diazo-5-oxo-l-norleucine (DON) or Azaserine.
32149084	8	30	with	inhibition	1179:1188	arg1	Azaserine					1240:1248	Azaserine	1240:1248	Azaserine	1240:1248	Moreover, similar antitumor effects were noticed by pharmacological inhibition of GFAT1 with 6-diazo-5-oxo-l-norleucine (DON) or Azaserine.
32149084	8	30	with	inhibition	1179:1188	arg1	6-diazo-5-oxo-l-norleucine					1204:1229	6-diazo-5-oxo-l-norleucine	1204:1229	6-diazo-5-oxo-l-norleucine (DON)	1204:1235	Moreover, similar antitumor effects were noticed by pharmacological inhibition of GFAT1 with 6-diazo-5-oxo-l-norleucine (DON) or Azaserine.
32149084	9	31	theme	oncogenic	1273:1281	arg1	activity					1313:1320	oncogenic Wnt/β-catenin transcriptional activity	1273:1320	oncogenic Wnt/β-catenin transcriptional activity	1273:1320	PDAC is maintained by oncogenic Wnt/β-catenin transcriptional activity.
32149084	12	32	theme	PDAC	1704:1707	arg1	cell					1709:1712	PDAC cell proliferation and invasion	1704:1739	PDAC cell proliferation and invasion	1704:1739	Ectopic expression of a stabilized form of β-catenin restored the suppressive roles of GFAT1 knockdown on PDAC cell proliferation and invasion.
32149084	11	33	dep	genes	1577:1581	arg1	CCND1					1583:1587	CCND1	1583:1587	CCND1	1583:1587	TOP/FOP-Flash and real-time qPCR analysis showed that GFAT1 knockdown inhibited β-catenin activity and the transcription of its downstream target genes CCND1 and MYC.
32149084	11	33	dep	genes	1577:1581	arg1	genes					1577:1581	its downstream target genes	1555:1581	its downstream target genes CCND1 and MYC	1555:1595	TOP/FOP-Flash and real-time qPCR analysis showed that GFAT1 knockdown inhibited β-catenin activity and the transcription of its downstream target genes CCND1 and MYC.
32149084	11	33	dep	genes	1577:1581	arg1	MYC					1593:1595	MYC	1593:1595	MYC	1593:1595	TOP/FOP-Flash and real-time qPCR analysis showed that GFAT1 knockdown inhibited β-catenin activity and the transcription of its downstream target genes CCND1 and MYC.
32149084	0	34	theme	β-Catenin	41:49	arg1	Activity					51:58	β-Catenin Activity	41:58	β-Catenin Activity	41:58	GFAT1/HBP/O-GlcNAcylation Axis Regulates β-Catenin Activity to Promote Pancreatic Cancer Aggressiveness.
32149084	12	35	theme	GFAT1	1685:1689	arg1	knockdown					1691:1699	GFAT1 knockdown	1685:1699	GFAT1 knockdown	1685:1699	Ectopic expression of a stabilized form of β-catenin restored the suppressive roles of GFAT1 knockdown on PDAC cell proliferation and invasion.
32149084	1	36	theme	glutamine	130:138	arg1	metabolism					140:149	Reprogrammed glucose and glutamine metabolism	105:149	Reprogrammed glucose and glutamine metabolism	105:149	Reprogrammed glucose and glutamine metabolism are essential for tumor initiation and development.
32149084	10	37	theme	β-catenin	1363:1371	arg1	expression					1373:1382	β-catenin expression	1363:1382	β-catenin expression	1363:1382	Our data showed that GFAT1 can regulate β-catenin expression via modulation of the O-GlcNAcylation process.
32149084	6	38	theme	cell	976:979	arg1	proliferation					981:993	PDAC cell proliferation	971:993	PDAC cell proliferation	971:993	Genetic silencing or pharmacological inhibition of the first and rate-limiting enzyme of the HBP, glutamine:fructose-6-phosphate amidotransferase 1 (GFAT1), inhibited PDAC cell proliferation, invasive capacity, and triggered cell apoptosis.
32149084	4	39	theme	cancers	646:652	arg1	types					631:635	33 types	628:635	33 types of human cancers	628:652	In this study, we analyzed the activity of the HBP and its prognostic value across 33 types of human cancers.
32149084	5	40	theme	PDAC	789:792	arg1	patients					794:801	PDAC patients	789:801	PDAC patients	789:801	Increased HBP activity was observed in pancreatic ductal adenocarcinoma (PDAC), and higher HBP activity predicted a poor prognosis in PDAC patients.
32149084	4	41	theme	HBP	592:594	arg1	value					615:619	its prognostic value	600:619	its prognostic value across 33 types of human cancers	600:652	In this study, we analyzed the activity of the HBP and its prognostic value across 33 types of human cancers.
32149084	4	41	theme	HBP	592:594	arg1	activity					576:583	the activity	572:583	the activity of the HBP	572:594	In this study, we analyzed the activity of the HBP and its prognostic value across 33 types of human cancers.
32149084	3	42	theme	tumor	486:490	arg1	aggressiveness					492:505	tumor aggressiveness	486:505	tumor aggressiveness	486:505	However, the spectrum of HBP-dependent tumors and the mechanisms by which the HBP promotes tumor aggressiveness remain areas of active investigation.
32149084	13	43	from	activity	1872:1879	arg1	PDAC					1884:1887	PDAC	1884:1887	PDAC	1884:1887	Collectively, our findings indicate that higher GFAT1/HBP/O-GlcNAcylation exhibits tumor-promoting roles by maintaining β-catenin activity in PDAC.
32149084	12	44	from	roles	1676:1680	arg1	cell					1709:1712	PDAC cell proliferation and invasion	1704:1739	PDAC cell proliferation and invasion	1704:1739	Ectopic expression of a stabilized form of β-catenin restored the suppressive roles of GFAT1 knockdown on PDAC cell proliferation and invasion.
32149084	6	45	theme	enzyme	883:888	arg1	silencing					812:820	Genetic silencing	804:820	Genetic silencing	804:820	Genetic silencing or pharmacological inhibition of the first and rate-limiting enzyme of the HBP, glutamine:fructose-6-phosphate amidotransferase 1 (GFAT1), inhibited PDAC cell proliferation, invasive capacity, and triggered cell apoptosis.
32149084	6	45	theme	enzyme	883:888	arg1	inhibition					841:850	pharmacological inhibition	825:850	pharmacological inhibition of the first and rate-limiting enzyme of the HBP, glutamine:fructose-6-phosphate amidotransferase 1 (GFAT1),	825:959	Genetic silencing or pharmacological inhibition of the first and rate-limiting enzyme of the HBP, glutamine:fructose-6-phosphate amidotransferase 1 (GFAT1), inhibited PDAC cell proliferation, invasive capacity, and triggered cell apoptosis.
32149084	2	46	theme	biosynthesis	257:268	arg1	HBP					279:281	HBP	279:281	HBP	279:281	As a branch of glucose and metabolism, the hexosamine biosynthesis pathway (HBP) generates uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) and contributes to the O-GlcNAcylation process.
32149084	2	46	theme	biosynthesis	257:268	arg1	pathway					270:276	the hexosamine biosynthesis pathway	242:276	the hexosamine biosynthesis pathway (HBP)	242:282	As a branch of glucose and metabolism, the hexosamine biosynthesis pathway (HBP) generates uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) and contributes to the O-GlcNAcylation process.
32149084	0	47	theme	Pancreatic	71:80	arg1	Aggressiveness					89:102	Pancreatic Cancer Aggressiveness	71:102	Pancreatic Cancer Aggressiveness	71:102	GFAT1/HBP/O-GlcNAcylation Axis Regulates β-Catenin Activity to Promote Pancreatic Cancer Aggressiveness.
32149084	12	48	theme	β-catenin	1641:1649	arg1	form					1633:1636	a stabilized form	1620:1636	a stabilized form of β-catenin	1620:1649	Ectopic expression of a stabilized form of β-catenin restored the suppressive roles of GFAT1 knockdown on PDAC cell proliferation and invasion.
32149084	5	49	theme	pancreatic	694:703	arg1	adenocarcinoma					712:725	pancreatic ductal adenocarcinoma	694:725	pancreatic ductal adenocarcinoma (PDAC)	694:732	Increased HBP activity was observed in pancreatic ductal adenocarcinoma (PDAC), and higher HBP activity predicted a poor prognosis in PDAC patients.
32149084	5	49	theme	pancreatic	694:703	arg1	PDAC					728:731	PDAC	728:731	PDAC	728:731	Increased HBP activity was observed in pancreatic ductal adenocarcinoma (PDAC), and higher HBP activity predicted a poor prognosis in PDAC patients.
32149084	5	50	theme	poor	771:774	arg1	prognosis					776:784	a poor prognosis	769:784	a poor prognosis in PDAC patients	769:801	Increased HBP activity was observed in pancreatic ductal adenocarcinoma (PDAC), and higher HBP activity predicted a poor prognosis in PDAC patients.
32149084	2	51	theme	hexosamine	246:255	arg1	HBP					279:281	HBP	279:281	HBP	279:281	As a branch of glucose and metabolism, the hexosamine biosynthesis pathway (HBP) generates uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) and contributes to the O-GlcNAcylation process.
32149084	2	51	theme	hexosamine	246:255	arg1	pathway					270:276	the hexosamine biosynthesis pathway	242:276	the hexosamine biosynthesis pathway (HBP)	242:282	As a branch of glucose and metabolism, the hexosamine biosynthesis pathway (HBP) generates uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) and contributes to the O-GlcNAcylation process.
32149084	12	52	dep	cell	1709:1712	arg1	invasion					1732:1739	invasion	1732:1739	invasion	1732:1739	Ectopic expression of a stabilized form of β-catenin restored the suppressive roles of GFAT1 knockdown on PDAC cell proliferation and invasion.
32149084	12	52	dep	cell	1709:1712	arg1	proliferation					1714:1726	proliferation	1714:1726	proliferation	1714:1726	Ectopic expression of a stabilized form of β-catenin restored the suppressive roles of GFAT1 knockdown on PDAC cell proliferation and invasion.
32149084	3	53	theme	investigation	530:542	arg1	areas					514:518	areas	514:518	areas of active investigation	514:542	However, the spectrum of HBP-dependent tumors and the mechanisms by which the HBP promotes tumor aggressiveness remain areas of active investigation.
32149084	12	54	theme	suppressive	1664:1674	arg1	roles					1676:1680	the suppressive roles	1660:1680	the suppressive roles of GFAT1 knockdown on PDAC cell proliferation and invasion	1660:1739	Ectopic expression of a stabilized form of β-catenin restored the suppressive roles of GFAT1 knockdown on PDAC cell proliferation and invasion.
32149084	5	55	theme	ductal	705:710	arg1	adenocarcinoma					712:725	pancreatic ductal adenocarcinoma	694:725	pancreatic ductal adenocarcinoma (PDAC)	694:732	Increased HBP activity was observed in pancreatic ductal adenocarcinoma (PDAC), and higher HBP activity predicted a poor prognosis in PDAC patients.
32149084	5	55	theme	ductal	705:710	arg1	PDAC					728:731	PDAC	728:731	PDAC	728:731	Increased HBP activity was observed in pancreatic ductal adenocarcinoma (PDAC), and higher HBP activity predicted a poor prognosis in PDAC patients.
32149084	5	56	from	prognosis	776:784	arg1	patients					794:801	PDAC patients	789:801	PDAC patients	789:801	Increased HBP activity was observed in pancreatic ductal adenocarcinoma (PDAC), and higher HBP activity predicted a poor prognosis in PDAC patients.
32149084	6	57	theme	first	859:863	arg1	glutamine					902:910	glutamine:fructose-6-phosphate amidotransferase 1 (GFAT1)	902:958	glutamine:fructose-6-phosphate amidotransferase 1 (GFAT1)	902:958	Genetic silencing or pharmacological inhibition of the first and rate-limiting enzyme of the HBP, glutamine:fructose-6-phosphate amidotransferase 1 (GFAT1), inhibited PDAC cell proliferation, invasive capacity, and triggered cell apoptosis.
32149084	6	57	theme	first	859:863	arg1	enzyme					883:888	the first and rate-limiting enzyme	855:888	the first and rate-limiting enzyme of the HBP	855:899	Genetic silencing or pharmacological inhibition of the first and rate-limiting enzyme of the HBP, glutamine:fructose-6-phosphate amidotransferase 1 (GFAT1), inhibited PDAC cell proliferation, invasive capacity, and triggered cell apoptosis.
32149084	2	58	theme	O-GlcNAcylation	370:384	arg1	process					386:392	the O-GlcNAcylation process	366:392	the O-GlcNAcylation process	366:392	As a branch of glucose and metabolism, the hexosamine biosynthesis pathway (HBP) generates uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) and contributes to the O-GlcNAcylation process.
32149084	11	59	theme	downstream	1559:1568	arg1	CCND1					1583:1587	CCND1	1583:1587	CCND1	1583:1587	TOP/FOP-Flash and real-time qPCR analysis showed that GFAT1 knockdown inhibited β-catenin activity and the transcription of its downstream target genes CCND1 and MYC.
32149084	11	59	theme	downstream	1559:1568	arg1	genes					1577:1581	its downstream target genes	1555:1581	its downstream target genes CCND1 and MYC	1555:1595	TOP/FOP-Flash and real-time qPCR analysis showed that GFAT1 knockdown inhibited β-catenin activity and the transcription of its downstream target genes CCND1 and MYC.
32149084	11	59	theme	downstream	1559:1568	arg1	MYC					1593:1595	MYC	1593:1595	MYC	1593:1595	TOP/FOP-Flash and real-time qPCR analysis showed that GFAT1 knockdown inhibited β-catenin activity and the transcription of its downstream target genes CCND1 and MYC.
32149084	8	60	theme	antitumor	1129:1137	arg1	effects					1139:1145	similar antitumor effects	1121:1145	similar antitumor effects	1121:1145	Moreover, similar antitumor effects were noticed by pharmacological inhibition of GFAT1 with 6-diazo-5-oxo-l-norleucine (DON) or Azaserine.
32149084	2	61	theme	metabolism	230:239	arg1	branch					208:213	a branch	206:213	a branch of glucose and metabolism	206:239	As a branch of glucose and metabolism, the hexosamine biosynthesis pathway (HBP) generates uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) and contributes to the O-GlcNAcylation process.
32149084	2	61	theme	metabolism	230:239	arg1	N-acetylglucosamine					314:332	uridine diphosphate N-acetylglucosamine	294:332	uridine diphosphate N-acetylglucosamine (UDP-GlcNAc)	294:345	As a branch of glucose and metabolism, the hexosamine biosynthesis pathway (HBP) generates uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) and contributes to the O-GlcNAcylation process.
32149084	6	62	theme	pharmacological	825:839	arg1	inhibition					841:850	pharmacological inhibition	825:850	pharmacological inhibition of the first and rate-limiting enzyme of the HBP, glutamine:fructose-6-phosphate amidotransferase 1 (GFAT1),	825:959	Genetic silencing or pharmacological inhibition of the first and rate-limiting enzyme of the HBP, glutamine:fructose-6-phosphate amidotransferase 1 (GFAT1), inhibited PDAC cell proliferation, invasive capacity, and triggered cell apoptosis.
32149084	11	63	theme	target	1570:1575	arg1	CCND1					1583:1587	CCND1	1583:1587	CCND1	1583:1587	TOP/FOP-Flash and real-time qPCR analysis showed that GFAT1 knockdown inhibited β-catenin activity and the transcription of its downstream target genes CCND1 and MYC.
32149084	11	63	theme	target	1570:1575	arg1	genes					1577:1581	its downstream target genes	1555:1581	its downstream target genes CCND1 and MYC	1555:1595	TOP/FOP-Flash and real-time qPCR analysis showed that GFAT1 knockdown inhibited β-catenin activity and the transcription of its downstream target genes CCND1 and MYC.
32149084	11	63	theme	target	1570:1575	arg1	MYC					1593:1595	MYC	1593:1595	MYC	1593:1595	TOP/FOP-Flash and real-time qPCR analysis showed that GFAT1 knockdown inhibited β-catenin activity and the transcription of its downstream target genes CCND1 and MYC.
32149084	12	64	theme	stabilized	1622:1631	arg1	form					1633:1636	a stabilized form	1620:1636	a stabilized form of β-catenin	1620:1649	Ectopic expression of a stabilized form of β-catenin restored the suppressive roles of GFAT1 knockdown on PDAC cell proliferation and invasion.
32149084	2	65	theme	uridine	294:300	arg1	N-acetylglucosamine					314:332	uridine diphosphate N-acetylglucosamine	294:332	uridine diphosphate N-acetylglucosamine (UDP-GlcNAc)	294:345	As a branch of glucose and metabolism, the hexosamine biosynthesis pathway (HBP) generates uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) and contributes to the O-GlcNAcylation process.
32149084	2	65	theme	uridine	294:300	arg1	branch					208:213	a branch	206:213	a branch of glucose and metabolism	206:239	As a branch of glucose and metabolism, the hexosamine biosynthesis pathway (HBP) generates uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) and contributes to the O-GlcNAcylation process.
32149084	2	65	theme	uridine	294:300	arg1	UDP-GlcNAc					335:344	UDP-GlcNAc	335:344	UDP-GlcNAc	335:344	As a branch of glucose and metabolism, the hexosamine biosynthesis pathway (HBP) generates uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) and contributes to the O-GlcNAcylation process.
32149084	9	66	theme	transcriptional	1297:1311	arg1	activity					1313:1320	oncogenic Wnt/β-catenin transcriptional activity	1273:1320	oncogenic Wnt/β-catenin transcriptional activity	1273:1320	PDAC is maintained by oncogenic Wnt/β-catenin transcriptional activity.
32149084	11	67	theme	real-time	1449:1457	arg1	analysis					1464:1471	real-time qPCR analysis	1449:1471	real-time qPCR analysis	1449:1471	TOP/FOP-Flash and real-time qPCR analysis showed that GFAT1 knockdown inhibited β-catenin activity and the transcription of its downstream target genes CCND1 and MYC.
32149084	10	68	theme	process	1422:1428	arg1	modulation					1388:1397	modulation	1388:1397	modulation of the O-GlcNAcylation process	1388:1428	Our data showed that GFAT1 can regulate β-catenin expression via modulation of the O-GlcNAcylation process.
32149084	1	69	theme	tumor	169:173	arg1	initiation					175:184	tumor initiation	169:184	tumor initiation	169:184	Reprogrammed glucose and glutamine metabolism are essential for tumor initiation and development.
32149084	2	70	theme	glucose	218:224	arg1	branch					208:213	a branch	206:213	a branch of glucose and metabolism	206:239	As a branch of glucose and metabolism, the hexosamine biosynthesis pathway (HBP) generates uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) and contributes to the O-GlcNAcylation process.
32149084	2	70	theme	glucose	218:224	arg1	N-acetylglucosamine					314:332	uridine diphosphate N-acetylglucosamine	294:332	uridine diphosphate N-acetylglucosamine (UDP-GlcNAc)	294:345	As a branch of glucose and metabolism, the hexosamine biosynthesis pathway (HBP) generates uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) and contributes to the O-GlcNAcylation process.
32149084	10	71	theme	O-GlcNAcylation	1406:1420	arg1	process					1422:1428	the O-GlcNAcylation process	1402:1428	the O-GlcNAcylation process	1402:1428	Our data showed that GFAT1 can regulate β-catenin expression via modulation of the O-GlcNAcylation process.
32149084	9	72	theme	Wnt/β-catenin	1283:1295	arg1	activity					1313:1320	oncogenic Wnt/β-catenin transcriptional activity	1273:1320	oncogenic Wnt/β-catenin transcriptional activity	1273:1320	PDAC is maintained by oncogenic Wnt/β-catenin transcriptional activity.
32149084	5	73	located	observed	682:689	arg1	adenocarcinoma					712:725	pancreatic ductal adenocarcinoma	694:725	pancreatic ductal adenocarcinoma (PDAC)	694:732	Increased HBP activity was observed in pancreatic ductal adenocarcinoma (PDAC), and higher HBP activity predicted a poor prognosis in PDAC patients.
32149084	5	73	located	observed	682:689	arg2	activity					669:676	Increased HBP activity	655:676	Increased HBP activity	655:676	Increased HBP activity was observed in pancreatic ductal adenocarcinoma (PDAC), and higher HBP activity predicted a poor prognosis in PDAC patients.
32149084	5	73	located	observed	682:689	arg1	PDAC					728:731	PDAC	728:731	PDAC	728:731	Increased HBP activity was observed in pancreatic ductal adenocarcinoma (PDAC), and higher HBP activity predicted a poor prognosis in PDAC patients.
32149084	4	74	theme	human	640:644	arg1	cancers					646:652	human cancers	640:652	human cancers	640:652	In this study, we analyzed the activity of the HBP and its prognostic value across 33 types of human cancers.
32149084	0	75	theme	Cancer	82:87	arg1	Aggressiveness					89:102	Pancreatic Cancer Aggressiveness	71:102	Pancreatic Cancer Aggressiveness	71:102	GFAT1/HBP/O-GlcNAcylation Axis Regulates β-Catenin Activity to Promote Pancreatic Cancer Aggressiveness.
32149084	13	76	theme	tumor-promoting	1825:1839	arg1	roles					1841:1845	tumor-promoting roles	1825:1845	tumor-promoting roles	1825:1845	Collectively, our findings indicate that higher GFAT1/HBP/O-GlcNAcylation exhibits tumor-promoting roles by maintaining β-catenin activity in PDAC.
32149084	6	77	dep	glutamine	902:910	arg1	amidotransferase					933:948	fructose-6-phosphate amidotransferase 1	912:950	glutamine:fructose-6-phosphate amidotransferase 1 (GFAT1)	902:958	Genetic silencing or pharmacological inhibition of the first and rate-limiting enzyme of the HBP, glutamine:fructose-6-phosphate amidotransferase 1 (GFAT1), inhibited PDAC cell proliferation, invasive capacity, and triggered cell apoptosis.
32149084	6	77	dep	glutamine	902:910	arg1	GFAT1					953:957	GFAT1	953:957	GFAT1	953:957	Genetic silencing or pharmacological inhibition of the first and rate-limiting enzyme of the HBP, glutamine:fructose-6-phosphate amidotransferase 1 (GFAT1), inhibited PDAC cell proliferation, invasive capacity, and triggered cell apoptosis.
32149084	13	78	theme	β-catenin	1862:1870	arg1	activity					1872:1879	β-catenin activity	1862:1879	β-catenin activity in PDAC	1862:1887	Collectively, our findings indicate that higher GFAT1/HBP/O-GlcNAcylation exhibits tumor-promoting roles by maintaining β-catenin activity in PDAC.
32149084	8	79	theme	similar	1121:1127	arg1	effects					1139:1145	similar antitumor effects	1121:1145	similar antitumor effects	1121:1145	Moreover, similar antitumor effects were noticed by pharmacological inhibition of GFAT1 with 6-diazo-5-oxo-l-norleucine (DON) or Azaserine.
32149084	6	80	theme	triggered	1019:1027	arg1	apoptosis					1034:1042	triggered cell apoptosis	1019:1042	triggered cell apoptosis	1019:1042	Genetic silencing or pharmacological inhibition of the first and rate-limiting enzyme of the HBP, glutamine:fructose-6-phosphate amidotransferase 1 (GFAT1), inhibited PDAC cell proliferation, invasive capacity, and triggered cell apoptosis.
33019562	2	0	theme	key-regulator	373:385	arg1	β-catenin					387:395	the cell cycle key-regulator β-catenin	358:395	the cell cycle key-regulator β-catenin	358:395	We developed an original tool, enabling labeling and visualization of the cell cycle key-regulator β-catenin in its O-GlcNAcylated form, based on intramolecular Förster resonance energy transfer (FRET) technology in cells.
33019562	4	1	theme	HeLa	872:875	arg1	cells					877:881	HeLa cells	872:881	HeLa cells	872:881	We validated this technology by imaging the O-GlcNAcylation status of β-catenin in HeLa cells.
33019562	2	2	theme	cycle	367:371	arg1	β-catenin					387:395	the cell cycle key-regulator β-catenin	358:395	the cell cycle key-regulator β-catenin	358:395	We developed an original tool, enabling labeling and visualization of the cell cycle key-regulator β-catenin in its O-GlcNAcylated form, based on intramolecular Förster resonance energy transfer (FRET) technology in cells.
33019562	2	3	from	transfer	474:481	arg1	cells					504:508	cells	504:508	cells	504:508	We developed an original tool, enabling labeling and visualization of the cell cycle key-regulator β-catenin in its O-GlcNAcylated form, based on intramolecular Förster resonance energy transfer (FRET) technology in cells.
33019562	2	4	from	visualization	341:353	arg1	form					419:422	its O-GlcNAcylated form	400:422	its O-GlcNAcylated form	400:422	We developed an original tool, enabling labeling and visualization of the cell cycle key-regulator β-catenin in its O-GlcNAcylated form, based on intramolecular Förster resonance energy transfer (FRET) technology in cells.
33019562	2	5	from	labeling	328:335	arg1	form					419:422	its O-GlcNAcylated form	400:422	its O-GlcNAcylated form	400:422	We developed an original tool, enabling labeling and visualization of the cell cycle key-regulator β-catenin in its O-GlcNAcylated form, based on intramolecular Förster resonance energy transfer (FRET) technology in cells.
33019562	5	6	from	changes	888:894	arg1	O-GlcNAcylation					899:913	O-GlcNAcylation	899:913	O-GlcNAcylation of β-catenin	899:926	The changes in O-GlcNAcylation of β-catenin were varied by perturbing global cellular O-GlcNAc levels with the inhibitors of O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA).
33019562	2	7	theme	original	304:311	arg1	tool					313:316	an original tool	301:316	an original tool	301:316	We developed an original tool, enabling labeling and visualization of the cell cycle key-regulator β-catenin in its O-GlcNAcylated form, based on intramolecular Förster resonance energy transfer (FRET) technology in cells.
33019562	5	8	theme	β-catenin	918:926	arg1	O-GlcNAcylation					899:913	O-GlcNAcylation	899:913	O-GlcNAcylation of β-catenin	899:926	The changes in O-GlcNAcylation of β-catenin were varied by perturbing global cellular O-GlcNAc levels with the inhibitors of O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA).
33019562	3	9	theme	reporter	549:556	arg1	strategy					558:565	a bioorthogonal chemical reporter strategy	524:565	a bioorthogonal chemical reporter strategy based on the dual-labeling of β-catenin with a green fluorescent protein (GFP) for protein sequence combined with a chemically-clicked imaging probe for PTM	524:722	We opted for a bioorthogonal chemical reporter strategy based on the dual-labeling of β-catenin with a green fluorescent protein (GFP) for protein sequence combined with a chemically-clicked imaging probe for PTM, resulting in a fast and easy to monitor qualitative FRET assay.
33019562	6	10	theme	glycosylation	1157:1169	arg1	kind					1149:1152	any kind	1145:1152	any kind of glycosylation	1145:1169	Finally, we provided a flowchart demonstrating how this technology is transposable to any kind of glycosylation.
33019562	4	11	from	status	849:854	arg1	cells					877:881	HeLa cells	872:881	HeLa cells	872:881	We validated this technology by imaging the O-GlcNAcylation status of β-catenin in HeLa cells.
33019562	2	12	theme	O-GlcNAcylated	404:417	arg1	form					419:422	its O-GlcNAcylated form	400:422	its O-GlcNAcylated form	400:422	We developed an original tool, enabling labeling and visualization of the cell cycle key-regulator β-catenin in its O-GlcNAcylated form, based on intramolecular Förster resonance energy transfer (FRET) technology in cells.
33019562	2	13	dep	transfer	474:481	arg1	technology					490:499	technology	490:499	intramolecular Förster resonance energy transfer (FRET) technology in cells	434:508	We developed an original tool, enabling labeling and visualization of the cell cycle key-regulator β-catenin in its O-GlcNAcylated form, based on intramolecular Förster resonance energy transfer (FRET) technology in cells.
33019562	3	14	theme	β-catenin	597:605	arg1	dual-labeling					580:592	dual-labeling	580:592	dual-labeling	580:592	We opted for a bioorthogonal chemical reporter strategy based on the dual-labeling of β-catenin with a green fluorescent protein (GFP) for protein sequence combined with a chemically-clicked imaging probe for PTM, resulting in a fast and easy to monitor qualitative FRET assay.
33019562	2	15	theme	energy	467:472	arg1	transfer					474:481	intramolecular Förster resonance energy transfer	434:481	intramolecular Förster resonance energy transfer (FRET) technology in cells	434:508	We developed an original tool, enabling labeling and visualization of the cell cycle key-regulator β-catenin in its O-GlcNAcylated form, based on intramolecular Förster resonance energy transfer (FRET) technology in cells.
33019562	2	15	theme	energy	467:472	arg1	FRET					484:487	FRET	484:487	FRET	484:487	We developed an original tool, enabling labeling and visualization of the cell cycle key-regulator β-catenin in its O-GlcNAcylated form, based on intramolecular Förster resonance energy transfer (FRET) technology in cells.
33019562	2	16	from	β-catenin	387:395	arg1	form					419:422	its O-GlcNAcylated form	400:422	its O-GlcNAcylated form	400:422	We developed an original tool, enabling labeling and visualization of the cell cycle key-regulator β-catenin in its O-GlcNAcylated form, based on intramolecular Förster resonance energy transfer (FRET) technology in cells.
33019562	1	17	theme	glycosylation	117:129	arg1	changes					131:137	glycosylation changes	117:137	glycosylation changes	117:137	Monitoring glycosylation changes within cells upon response to stimuli remains challenging because of the complexity of this large family of post-translational modifications (PTMs).
33019562	2	18	theme	Förster	449:455	arg1	transfer					474:481	intramolecular Förster resonance energy transfer	434:481	intramolecular Förster resonance energy transfer (FRET) technology in cells	434:508	We developed an original tool, enabling labeling and visualization of the cell cycle key-regulator β-catenin in its O-GlcNAcylated form, based on intramolecular Förster resonance energy transfer (FRET) technology in cells.
33019562	2	18	theme	Förster	449:455	arg1	FRET					484:487	FRET	484:487	FRET	484:487	We developed an original tool, enabling labeling and visualization of the cell cycle key-regulator β-catenin in its O-GlcNAcylated form, based on intramolecular Förster resonance energy transfer (FRET) technology in cells.
33019562	2	19	theme	resonance	457:465	arg1	transfer					474:481	intramolecular Förster resonance energy transfer	434:481	intramolecular Förster resonance energy transfer (FRET) technology in cells	434:508	We developed an original tool, enabling labeling and visualization of the cell cycle key-regulator β-catenin in its O-GlcNAcylated form, based on intramolecular Förster resonance energy transfer (FRET) technology in cells.
33019562	2	19	theme	resonance	457:465	arg1	FRET					484:487	FRET	484:487	FRET	484:487	We developed an original tool, enabling labeling and visualization of the cell cycle key-regulator β-catenin in its O-GlcNAcylated form, based on intramolecular Förster resonance energy transfer (FRET) technology in cells.
33019562	5	20	theme	global	954:959	arg1	levels					979:984	global cellular O-GlcNAc levels	954:984	global cellular O-GlcNAc levels	954:984	The changes in O-GlcNAcylation of β-catenin were varied by perturbing global cellular O-GlcNAc levels with the inhibitors of O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA).
33019562	5	21	theme	O-GlcNAc	970:977	arg1	levels					979:984	global cellular O-GlcNAc levels	954:984	global cellular O-GlcNAc levels	954:984	The changes in O-GlcNAcylation of β-catenin were varied by perturbing global cellular O-GlcNAc levels with the inhibitors of O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA).
33019562	2	22	theme	intramolecular	434:447	arg1	transfer					474:481	intramolecular Förster resonance energy transfer	434:481	intramolecular Förster resonance energy transfer (FRET) technology in cells	434:508	We developed an original tool, enabling labeling and visualization of the cell cycle key-regulator β-catenin in its O-GlcNAcylated form, based on intramolecular Förster resonance energy transfer (FRET) technology in cells.
33019562	2	22	theme	intramolecular	434:447	arg1	FRET					484:487	FRET	484:487	FRET	484:487	We developed an original tool, enabling labeling and visualization of the cell cycle key-regulator β-catenin in its O-GlcNAcylated form, based on intramolecular Förster resonance energy transfer (FRET) technology in cells.
33019562	0	23	theme	O-GlcNAcylation	37:51	arg1	Potential					14:22	the Potential	10:22	the Potential of β-Catenin O-GlcNAcylation	10:51	Exploring the Potential of β-Catenin O-GlcNAcylation by Using Fluorescence-Based Engineering and Imaging.
33019562	3	24	theme	green	614:618	arg1	GFP					641:643	GFP	641:643	GFP	641:643	We opted for a bioorthogonal chemical reporter strategy based on the dual-labeling of β-catenin with a green fluorescent protein (GFP) for protein sequence combined with a chemically-clicked imaging probe for PTM, resulting in a fast and easy to monitor qualitative FRET assay.
33019562	3	24	theme	green	614:618	arg1	protein					632:638	a green fluorescent protein	612:638	a green fluorescent protein (GFP) for protein sequence combined with a chemically-clicked imaging probe for PTM	612:722	We opted for a bioorthogonal chemical reporter strategy based on the dual-labeling of β-catenin with a green fluorescent protein (GFP) for protein sequence combined with a chemically-clicked imaging probe for PTM, resulting in a fast and easy to monitor qualitative FRET assay.
33019562	1	25	theme	large	231:235	arg1	family					237:242	this large family	226:242	this large family of post-translational modifications (PTMs)	226:285	Monitoring glycosylation changes within cells upon response to stimuli remains challenging because of the complexity of this large family of post-translational modifications (PTMs).
33019562	0	26	theme	β-Catenin	27:35	arg1	O-GlcNAcylation					37:51	β-Catenin O-GlcNAcylation	27:51	β-Catenin O-GlcNAcylation	27:51	Exploring the Potential of β-Catenin O-GlcNAcylation by Using Fluorescence-Based Engineering and Imaging.
33019562	3	27	theme	fluorescent	620:630	arg1	GFP					641:643	GFP	641:643	GFP	641:643	We opted for a bioorthogonal chemical reporter strategy based on the dual-labeling of β-catenin with a green fluorescent protein (GFP) for protein sequence combined with a chemically-clicked imaging probe for PTM, resulting in a fast and easy to monitor qualitative FRET assay.
33019562	3	27	theme	fluorescent	620:630	arg1	protein					632:638	a green fluorescent protein	612:638	a green fluorescent protein (GFP) for protein sequence combined with a chemically-clicked imaging probe for PTM	612:722	We opted for a bioorthogonal chemical reporter strategy based on the dual-labeling of β-catenin with a green fluorescent protein (GFP) for protein sequence combined with a chemically-clicked imaging probe for PTM, resulting in a fast and easy to monitor qualitative FRET assay.
33019562	1	28	theme	family	237:242	arg1	complexity					212:221	the complexity	208:221	the complexity of this large family of post-translational modifications (PTMs)	208:285	Monitoring glycosylation changes within cells upon response to stimuli remains challenging because of the complexity of this large family of post-translational modifications (PTMs).
33019562	3	29	theme	protein	650:656	arg1	sequence					658:665	protein sequence	650:665	protein sequence combined with a chemically-clicked imaging probe for PTM	650:722	We opted for a bioorthogonal chemical reporter strategy based on the dual-labeling of β-catenin with a green fluorescent protein (GFP) for protein sequence combined with a chemically-clicked imaging probe for PTM, resulting in a fast and easy to monitor qualitative FRET assay.
33019562	4	30	theme	O-GlcNAcylation	833:847	arg1	status					849:854	the O-GlcNAcylation status	829:854	the O-GlcNAcylation status of β-catenin in HeLa cells	829:881	We validated this technology by imaging the O-GlcNAcylation status of β-catenin in HeLa cells.
33019562	4	31	theme	β-catenin	859:867	arg1	status					849:854	the O-GlcNAcylation status	829:854	the O-GlcNAcylation status of β-catenin in HeLa cells	829:881	We validated this technology by imaging the O-GlcNAcylation status of β-catenin in HeLa cells.
33019562	2	32	theme	cell	362:365	arg1	β-catenin					387:395	the cell cycle key-regulator β-catenin	358:395	the cell cycle key-regulator β-catenin	358:395	We developed an original tool, enabling labeling and visualization of the cell cycle key-regulator β-catenin in its O-GlcNAcylated form, based on intramolecular Förster resonance energy transfer (FRET) technology in cells.
33019562	3	33	theme	qualitative	765:775	arg1	assay					782:786	qualitative FRET assay	765:786	qualitative FRET assay	765:786	We opted for a bioorthogonal chemical reporter strategy based on the dual-labeling of β-catenin with a green fluorescent protein (GFP) for protein sequence combined with a chemically-clicked imaging probe for PTM, resulting in a fast and easy to monitor qualitative FRET assay.
33019562	3	34	theme	chemically-clicked	683:700	arg1	probe					710:714	a chemically-clicked imaging probe	681:714	a chemically-clicked imaging probe for PTM	681:722	We opted for a bioorthogonal chemical reporter strategy based on the dual-labeling of β-catenin with a green fluorescent protein (GFP) for protein sequence combined with a chemically-clicked imaging probe for PTM, resulting in a fast and easy to monitor qualitative FRET assay.
33019562	5	35	theme	O-GlcNAcase	1040:1050	arg1	inhibitors					995:1004	the inhibitors	991:1004	the inhibitors of O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA)	991:1056	The changes in O-GlcNAcylation of β-catenin were varied by perturbing global cellular O-GlcNAc levels with the inhibitors of O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA).
33019562	3	36	theme	FRET	777:780	arg1	assay					782:786	qualitative FRET assay	765:786	qualitative FRET assay	765:786	We opted for a bioorthogonal chemical reporter strategy based on the dual-labeling of β-catenin with a green fluorescent protein (GFP) for protein sequence combined with a chemically-clicked imaging probe for PTM, resulting in a fast and easy to monitor qualitative FRET assay.
33019562	3	37	theme	imaging	702:708	arg1	probe					710:714	a chemically-clicked imaging probe	681:714	a chemically-clicked imaging probe for PTM	681:722	We opted for a bioorthogonal chemical reporter strategy based on the dual-labeling of β-catenin with a green fluorescent protein (GFP) for protein sequence combined with a chemically-clicked imaging probe for PTM, resulting in a fast and easy to monitor qualitative FRET assay.
33019562	2	38	from	form	419:422	arg1	visualization					341:353	visualization	341:353	visualization of the cell cycle key-regulator β-catenin in its O-GlcNAcylated form, based on intramolecular Förster resonance energy transfer (FRET) technology in cells	341:508	We developed an original tool, enabling labeling and visualization of the cell cycle key-regulator β-catenin in its O-GlcNAcylated form, based on intramolecular Förster resonance energy transfer (FRET) technology in cells.
33019562	2	38	from	form	419:422	arg1	labeling					328:335	labeling	328:335	labeling	328:335	We developed an original tool, enabling labeling and visualization of the cell cycle key-regulator β-catenin in its O-GlcNAcylated form, based on intramolecular Förster resonance energy transfer (FRET) technology in cells.
33019562	5	39	theme	cellular	961:968	arg1	levels					979:984	global cellular O-GlcNAc levels	954:984	global cellular O-GlcNAc levels	954:984	The changes in O-GlcNAcylation of β-catenin were varied by perturbing global cellular O-GlcNAc levels with the inhibitors of O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA).
33019562	5	40	theme	O-GlcNAc	1009:1016	arg1	transferase					1018:1028	O-GlcNAc transferase	1009:1028	O-GlcNAc transferase (OGT)	1009:1034	The changes in O-GlcNAcylation of β-catenin were varied by perturbing global cellular O-GlcNAc levels with the inhibitors of O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA).
33019562	5	40	theme	O-GlcNAc	1009:1016	arg1	OGT					1031:1033	OGT	1031:1033	OGT	1031:1033	The changes in O-GlcNAcylation of β-catenin were varied by perturbing global cellular O-GlcNAc levels with the inhibitors of O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA).
33019562	3	41	theme	chemical	540:547	arg1	strategy					558:565	a bioorthogonal chemical reporter strategy	524:565	a bioorthogonal chemical reporter strategy based on the dual-labeling of β-catenin with a green fluorescent protein (GFP) for protein sequence combined with a chemically-clicked imaging probe for PTM	524:722	We opted for a bioorthogonal chemical reporter strategy based on the dual-labeling of β-catenin with a green fluorescent protein (GFP) for protein sequence combined with a chemically-clicked imaging probe for PTM, resulting in a fast and easy to monitor qualitative FRET assay.
33019562	1	42	theme	post-translational	247:264	arg1	modifications					266:278	post-translational modifications	247:278	post-translational modifications (PTMs)	247:285	Monitoring glycosylation changes within cells upon response to stimuli remains challenging because of the complexity of this large family of post-translational modifications (PTMs).
33019562	1	42	theme	post-translational	247:264	arg1	PTMs					281:284	PTMs	281:284	PTMs	281:284	Monitoring glycosylation changes within cells upon response to stimuli remains challenging because of the complexity of this large family of post-translational modifications (PTMs).
33019562	5	43	theme	transferase	1018:1028	arg1	inhibitors					995:1004	the inhibitors	991:1004	the inhibitors of O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA)	991:1056	The changes in O-GlcNAcylation of β-catenin were varied by perturbing global cellular O-GlcNAc levels with the inhibitors of O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA).
33019562	3	44	theme	bioorthogonal	526:538	arg1	strategy					558:565	a bioorthogonal chemical reporter strategy	524:565	a bioorthogonal chemical reporter strategy based on the dual-labeling of β-catenin with a green fluorescent protein (GFP) for protein sequence combined with a chemically-clicked imaging probe for PTM	524:722	We opted for a bioorthogonal chemical reporter strategy based on the dual-labeling of β-catenin with a green fluorescent protein (GFP) for protein sequence combined with a chemically-clicked imaging probe for PTM, resulting in a fast and easy to monitor qualitative FRET assay.
33019562	1	45	theme	modifications	266:278	arg1	family					237:242	this large family	226:242	this large family of post-translational modifications (PTMs)	226:285	Monitoring glycosylation changes within cells upon response to stimuli remains challenging because of the complexity of this large family of post-translational modifications (PTMs).
33019562	0	46	theme	Fluorescence-Based	62:79	arg1	Engineering					81:91	Engineering	81:91	Engineering	81:91	Exploring the Potential of β-Catenin O-GlcNAcylation by Using Fluorescence-Based Engineering and Imaging.
33019562	3	47	with	β-catenin	597:605	arg1	GFP					641:643	GFP	641:643	GFP	641:643	We opted for a bioorthogonal chemical reporter strategy based on the dual-labeling of β-catenin with a green fluorescent protein (GFP) for protein sequence combined with a chemically-clicked imaging probe for PTM, resulting in a fast and easy to monitor qualitative FRET assay.
33019562	3	47	with	β-catenin	597:605	arg1	protein					632:638	a green fluorescent protein	612:638	a green fluorescent protein (GFP) for protein sequence combined with a chemically-clicked imaging probe for PTM	612:722	We opted for a bioorthogonal chemical reporter strategy based on the dual-labeling of β-catenin with a green fluorescent protein (GFP) for protein sequence combined with a chemically-clicked imaging probe for PTM, resulting in a fast and easy to monitor qualitative FRET assay.
33019562	2	48	theme	β-catenin	387:395	arg1	visualization					341:353	visualization	341:353	visualization of the cell cycle key-regulator β-catenin in its O-GlcNAcylated form, based on intramolecular Förster resonance energy transfer (FRET) technology in cells	341:508	We developed an original tool, enabling labeling and visualization of the cell cycle key-regulator β-catenin in its O-GlcNAcylated form, based on intramolecular Förster resonance energy transfer (FRET) technology in cells.
33019562	2	48	theme	β-catenin	387:395	arg1	labeling					328:335	labeling	328:335	labeling	328:335	We developed an original tool, enabling labeling and visualization of the cell cycle key-regulator β-catenin in its O-GlcNAcylated form, based on intramolecular Förster resonance energy transfer (FRET) technology in cells.
26488919	3	0	theme	O-GlcNAc	522:529	arg1	moiety					531:536	the O-GlcNAc moiety	518:536	the O-GlcNAc moiety	518:536	Herein, we report the development of a FLIM-FRET-based strategy, which exploits the spatial proximity of the O-GlcNAc moiety and the attaching protein, for protein-specific imaging of O-GlcNAcylation in single cells.
26488919	6	1	from	state	997:1001	arg1	cells					1030:1034	the cells	1026:1034	the cells	1026:1034	We envision that the FLIM-FRET strategy will be broadly applicable to probe the O-GlcNAcylation state of various proteins in the cells.
26488919	0	2	from	Imaging	17:23	arg1	Cells					54:58	Single Cells	47:58	Single Cells	47:58	Protein-Specific Imaging of O-GlcNAcylation in Single Cells.
26488919	3	3	theme	moiety	531:536	arg1	proximity					505:513	the spatial proximity	493:513	the spatial proximity of the O-GlcNAc moiety and the attaching protein	493:562	Herein, we report the development of a FLIM-FRET-based strategy, which exploits the spatial proximity of the O-GlcNAc moiety and the attaching protein, for protein-specific imaging of O-GlcNAcylation in single cells.
26488919	2	4	theme	important	281:289	arg1	glycosylation					291:303	this important glycosylation	276:303	this important glycosylation	276:303	However, the ubiquity of this important glycosylation makes it highly challenging to probe the O-GlcNAcylation state of a specific protein at the cellular level.
26488919	5	5	theme	tau	764:766	arg1	O-GlcNAcylation					768:782	tau O-GlcNAcylation	764:782	tau O-GlcNAcylation	764:782	Furthermore, the changes in tau O-GlcNAcylation were monitored when the overall cellular O-GlcNAc was pharmacologically altered by using the OGT and OGA inhibitors.
26488919	6	6	theme	FLIM-FRET	922:930	arg1	strategy					932:939	the FLIM-FRET strategy	918:939	the FLIM-FRET strategy	918:939	We envision that the FLIM-FRET strategy will be broadly applicable to probe the O-GlcNAcylation state of various proteins in the cells.
26488919	6	6	theme	FLIM-FRET	922:930	arg1	applicable					957:966	applicable	957:966	applicable	957:966	We envision that the FLIM-FRET strategy will be broadly applicable to probe the O-GlcNAcylation state of various proteins in the cells.
26488919	5	7	theme	OGT	877:879	arg1	inhibitors					889:898	the OGT and OGA inhibitors	873:898	the OGT and OGA inhibitors	873:898	Furthermore, the changes in tau O-GlcNAcylation were monitored when the overall cellular O-GlcNAc was pharmacologically altered by using the OGT and OGA inhibitors.
26488919	1	8	theme	intracellular	74:86	arg1	proteins					88:95	intracellular proteins	74:95	intracellular proteins	74:95	Thousands of intracellular proteins are post-translationally modified with O-GlcNAc, and O-GlcNAcylation impacts the function of modified proteins and mediates diverse biological processes.
26488919	1	9	theme	modified	190:197	arg1	proteins					199:206	modified proteins	190:206	modified proteins	190:206	Thousands of intracellular proteins are post-translationally modified with O-GlcNAc, and O-GlcNAcylation impacts the function of modified proteins and mediates diverse biological processes.
26488919	5	10	theme	overall	808:814	arg1	O-GlcNAc					825:832	the overall cellular O-GlcNAc	804:832	the overall cellular O-GlcNAc	804:832	Furthermore, the changes in tau O-GlcNAcylation were monitored when the overall cellular O-GlcNAc was pharmacologically altered by using the OGT and OGA inhibitors.
26488919	1	11	theme	proteins	88:95	arg1	Thousands					61:69	Thousands	61:69	Thousands of intracellular proteins	61:95	Thousands of intracellular proteins are post-translationally modified with O-GlcNAc, and O-GlcNAcylation impacts the function of modified proteins and mediates diverse biological processes.
26488919	1	12	theme	proteins	199:206	arg1	function					178:185	the function	174:185	the function of modified proteins	174:206	Thousands of intracellular proteins are post-translationally modified with O-GlcNAc, and O-GlcNAcylation impacts the function of modified proteins and mediates diverse biological processes.
26488919	2	13	theme	O-GlcNAcylation	346:360	arg1	state					362:366	the O-GlcNAcylation state	342:366	the O-GlcNAcylation state of a specific protein at the cellular level	342:410	However, the ubiquity of this important glycosylation makes it highly challenging to probe the O-GlcNAcylation state of a specific protein at the cellular level.
26488919	0	14	theme	Protein-Specific	0:15	arg1	Imaging					17:23	Protein-Specific Imaging	0:23	Protein-Specific Imaging of O-GlcNAcylation in Single Cells	0:58	Protein-Specific Imaging of O-GlcNAcylation in Single Cells.
26488919	6	15	theme	proteins	1014:1021	arg1	state					997:1001	the O-GlcNAcylation state	977:1001	the O-GlcNAcylation state of various proteins in the cells	977:1034	We envision that the FLIM-FRET strategy will be broadly applicable to probe the O-GlcNAcylation state of various proteins in the cells.
26488919	3	16	theme	O-GlcNAcylation	597:611	arg1	imaging					586:592	protein-specific imaging	569:592	protein-specific imaging of O-GlcNAcylation in single cells	569:627	Herein, we report the development of a FLIM-FRET-based strategy, which exploits the spatial proximity of the O-GlcNAc moiety and the attaching protein, for protein-specific imaging of O-GlcNAcylation in single cells.
26488919	4	17	theme	tau	700:702	arg1	state					691:695	the O-GlcNAcylation state	671:695	the O-GlcNAcylation state of tau and β-catenin	671:716	We demonstrated this strategy by imaging the O-GlcNAcylation state of tau and β-catenin inside the cells.
26488919	0	18	theme	O-GlcNAcylation	28:42	arg1	Imaging					17:23	Protein-Specific Imaging	0:23	Protein-Specific Imaging of O-GlcNAcylation in Single Cells	0:58	Protein-Specific Imaging of O-GlcNAcylation in Single Cells.
26488919	6	19	theme	various	1006:1012	arg1	proteins					1014:1021	various proteins	1006:1021	various proteins	1006:1021	We envision that the FLIM-FRET strategy will be broadly applicable to probe the O-GlcNAcylation state of various proteins in the cells.
26488919	3	20	theme	protein-specific	569:584	arg1	imaging					586:592	protein-specific imaging	569:592	protein-specific imaging of O-GlcNAcylation in single cells	569:627	Herein, we report the development of a FLIM-FRET-based strategy, which exploits the spatial proximity of the O-GlcNAc moiety and the attaching protein, for protein-specific imaging of O-GlcNAcylation in single cells.
26488919	1	21	theme	diverse	221:227	arg1	processes					240:248	diverse biological processes	221:248	diverse biological processes	221:248	Thousands of intracellular proteins are post-translationally modified with O-GlcNAc, and O-GlcNAcylation impacts the function of modified proteins and mediates diverse biological processes.
26488919	3	22	theme	attaching	546:554	arg1	protein					556:562	the attaching protein	542:562	the attaching protein	542:562	Herein, we report the development of a FLIM-FRET-based strategy, which exploits the spatial proximity of the O-GlcNAc moiety and the attaching protein, for protein-specific imaging of O-GlcNAcylation in single cells.
26488919	2	23	theme	protein	382:388	arg1	state					362:366	the O-GlcNAcylation state	342:366	the O-GlcNAcylation state of a specific protein at the cellular level	342:410	However, the ubiquity of this important glycosylation makes it highly challenging to probe the O-GlcNAcylation state of a specific protein at the cellular level.
26488919	1	24	theme	biological	229:238	arg1	processes					240:248	diverse biological processes	221:248	diverse biological processes	221:248	Thousands of intracellular proteins are post-translationally modified with O-GlcNAc, and O-GlcNAcylation impacts the function of modified proteins and mediates diverse biological processes.
26488919	0	25	theme	Single	47:52	arg1	Cells					54:58	Single Cells	47:58	Single Cells	47:58	Protein-Specific Imaging of O-GlcNAcylation in Single Cells.
26488919	4	26	theme	O-GlcNAcylation	675:689	arg1	state					691:695	the O-GlcNAcylation state	671:695	the O-GlcNAcylation state of tau and β-catenin	671:716	We demonstrated this strategy by imaging the O-GlcNAcylation state of tau and β-catenin inside the cells.
26488919	3	27	theme	FLIM-FRET-based	452:466	arg1	strategy					468:475	a FLIM-FRET-based strategy	450:475	a FLIM-FRET-based strategy	450:475	Herein, we report the development of a FLIM-FRET-based strategy, which exploits the spatial proximity of the O-GlcNAc moiety and the attaching protein, for protein-specific imaging of O-GlcNAcylation in single cells.
26488919	6	28	theme	O-GlcNAcylation	981:995	arg1	state					997:1001	the O-GlcNAcylation state	977:1001	the O-GlcNAcylation state of various proteins in the cells	977:1034	We envision that the FLIM-FRET strategy will be broadly applicable to probe the O-GlcNAcylation state of various proteins in the cells.
26488919	5	29	theme	cellular	816:823	arg1	O-GlcNAc					825:832	the overall cellular O-GlcNAc	804:832	the overall cellular O-GlcNAc	804:832	Furthermore, the changes in tau O-GlcNAcylation were monitored when the overall cellular O-GlcNAc was pharmacologically altered by using the OGT and OGA inhibitors.
26488919	5	30	from	changes	753:759	arg1	O-GlcNAcylation					768:782	tau O-GlcNAcylation	764:782	tau O-GlcNAcylation	764:782	Furthermore, the changes in tau O-GlcNAcylation were monitored when the overall cellular O-GlcNAc was pharmacologically altered by using the OGT and OGA inhibitors.
26488919	5	31	theme	OGA	885:887	arg1	inhibitors					889:898	the OGT and OGA inhibitors	873:898	the OGT and OGA inhibitors	873:898	Furthermore, the changes in tau O-GlcNAcylation were monitored when the overall cellular O-GlcNAc was pharmacologically altered by using the OGT and OGA inhibitors.
26488919	4	32	dep	imaging	663:669	arg1	inside					718:723	inside	718:723	imaging the O-GlcNAcylation state of tau and β-catenin inside the cells	663:733	We demonstrated this strategy by imaging the O-GlcNAcylation state of tau and β-catenin inside the cells.
26488919	2	33	from	level	406:410	arg1	state					362:366	the O-GlcNAcylation state	342:366	the O-GlcNAcylation state of a specific protein at the cellular level	342:410	However, the ubiquity of this important glycosylation makes it highly challenging to probe the O-GlcNAcylation state of a specific protein at the cellular level.
26488919	2	34	theme	specific	373:380	arg1	protein					382:388	a specific protein	371:388	a specific protein	371:388	However, the ubiquity of this important glycosylation makes it highly challenging to probe the O-GlcNAcylation state of a specific protein at the cellular level.
26488919	3	35	theme	single	616:621	arg1	cells					623:627	single cells	616:627	single cells	616:627	Herein, we report the development of a FLIM-FRET-based strategy, which exploits the spatial proximity of the O-GlcNAc moiety and the attaching protein, for protein-specific imaging of O-GlcNAcylation in single cells.
26488919	2	36	theme	glycosylation	291:303	arg1	ubiquity					264:271	the ubiquity	260:271	the ubiquity of this important glycosylation	260:303	However, the ubiquity of this important glycosylation makes it highly challenging to probe the O-GlcNAcylation state of a specific protein at the cellular level.
26488919	3	37	theme	spatial	497:503	arg1	proximity					505:513	the spatial proximity	493:513	the spatial proximity of the O-GlcNAc moiety and the attaching protein	493:562	Herein, we report the development of a FLIM-FRET-based strategy, which exploits the spatial proximity of the O-GlcNAc moiety and the attaching protein, for protein-specific imaging of O-GlcNAcylation in single cells.
26488919	3	38	from	imaging	586:592	arg1	cells					623:627	single cells	616:627	single cells	616:627	Herein, we report the development of a FLIM-FRET-based strategy, which exploits the spatial proximity of the O-GlcNAc moiety and the attaching protein, for protein-specific imaging of O-GlcNAcylation in single cells.
26488919	3	39	theme	protein	556:562	arg1	proximity					505:513	the spatial proximity	493:513	the spatial proximity of the O-GlcNAc moiety and the attaching protein	493:562	Herein, we report the development of a FLIM-FRET-based strategy, which exploits the spatial proximity of the O-GlcNAc moiety and the attaching protein, for protein-specific imaging of O-GlcNAcylation in single cells.
26488919	1	40	mod	modified	122:129	arg3	O-GlcNAc					136:143	O-GlcNAc	136:143	O-GlcNAc	136:143	Thousands of intracellular proteins are post-translationally modified with O-GlcNAc, and O-GlcNAcylation impacts the function of modified proteins and mediates diverse biological processes.
26488919	1	40	mod	modified	122:129	arg1	Thousands					61:69	Thousands	61:69	Thousands of intracellular proteins	61:95	Thousands of intracellular proteins are post-translationally modified with O-GlcNAc, and O-GlcNAcylation impacts the function of modified proteins and mediates diverse biological processes.
26488919	2	41	theme	cellular	397:404	arg1	level					406:410	the cellular level	393:410	the cellular level	393:410	However, the ubiquity of this important glycosylation makes it highly challenging to probe the O-GlcNAcylation state of a specific protein at the cellular level.
26488919	3	42	theme	strategy	468:475	arg1	development					435:445	the development	431:445	the development of a FLIM-FRET-based strategy, which exploits the spatial proximity of the O-GlcNAc moiety and the attaching protein, for protein-specific imaging of O-GlcNAcylation in single cells	431:627	Herein, we report the development of a FLIM-FRET-based strategy, which exploits the spatial proximity of the O-GlcNAc moiety and the attaching protein, for protein-specific imaging of O-GlcNAcylation in single cells.
26488919	4	43	theme	β-catenin	708:716	arg1	state					691:695	the O-GlcNAcylation state	671:695	the O-GlcNAcylation state of tau and β-catenin	671:716	We demonstrated this strategy by imaging the O-GlcNAcylation state of tau and β-catenin inside the cells.
18586027	3	0	theme	beta-catenin	378:389	arg1	localization					362:373	the nuclear localization	350:373	the nuclear localization of beta-catenin	350:389	Phosphorylation of beta-catenin controls its intracellular expression but mechanism/s that regulates the nuclear localization of beta-catenin is unknown.
18586027	8	1	theme	reporter	1113:1120	arg1	assay					1122:1126	TOPFlash reporter assay	1104:1126	TOPFlash reporter assay	1104:1126	TOPFlash reporter assay and mRNA expressions of beta-catenin's target genes indicate that O-GlcNAcylation of beta-catenin results in a decrease in its transcriptional activity.
18586027	6	2	theme	minimal	768:774	arg1	O-GlcNAcylated					834:847	O-GlcNAcylated	834:847	O-GlcNAcylated	834:847	The total nuclear levels of beta-catenin are higher in the CaP cells than PNT1A but only a minimal fraction of the nuclear beta-catenin in the CaP cells are O-GlcNAcylated.
18586027	6	2	theme	minimal	768:774	arg1	fraction					776:783	only a minimal fraction	761:783	only a minimal fraction of the nuclear beta-catenin in the CaP cells	761:828	The total nuclear levels of beta-catenin are higher in the CaP cells than PNT1A but only a minimal fraction of the nuclear beta-catenin in the CaP cells are O-GlcNAcylated.
18586027	7	3	from	decrease	1049:1056	arg1	levels					1065:1070	the levels	1061:1070	the levels of beta-catenin in the nucleus	1061:1101	Increasing the levels of O-GlcNAcylated beta-catenin in the CaP cells with PUGNAc (O- (2-acetamido-2-deoxy-d-gluco-pyranosylidene) amino-N-phenylcarbamate) treatment is associated with a progressive decrease in the levels of beta-catenin in the nucleus.
18586027	4	4	gly	glycosylation	432:444	arg1	beta-catenin					467:478	beta-catenin	467:478	beta-catenin	467:478	We demonstrate that O-GlcNAc glycosylation (O-GlcNAcylation) of beta-catenin negatively regulates its levels in the nucleus.
18586027	3	5	theme	beta-catenin	268:279	arg1	Phosphorylation					249:263	Phosphorylation	249:263	Phosphorylation of beta-catenin	249:279	Phosphorylation of beta-catenin controls its intracellular expression but mechanism/s that regulates the nuclear localization of beta-catenin is unknown.
18586027	4	6	theme	beta-catenin	467:478	arg1	O-GlcNAcylation					447:461	O-GlcNAcylation	447:461	O-GlcNAcylation	447:461	We demonstrate that O-GlcNAc glycosylation (O-GlcNAcylation) of beta-catenin negatively regulates its levels in the nucleus.
18586027	4	6	theme	beta-catenin	467:478	arg1	glycosylation					432:444	O-GlcNAc glycosylation	423:444	O-GlcNAc glycosylation (O-GlcNAcylation) of beta-catenin	423:478	We demonstrate that O-GlcNAc glycosylation (O-GlcNAcylation) of beta-catenin negatively regulates its levels in the nucleus.
18586027	9	7	theme	novel	1293:1297	arg1	modification					1299:1310	a novel modification	1291:1310	a novel modification of beta-catenin that regulates its nuclear localization and transcriptional function	1291:1395	We define a novel modification of beta-catenin that regulates its nuclear localization and transcriptional function.
18586027	6	8	theme	nuclear	687:693	arg1	levels					695:700	The total nuclear levels	677:700	The total nuclear levels of beta-catenin	677:716	The total nuclear levels of beta-catenin are higher in the CaP cells than PNT1A but only a minimal fraction of the nuclear beta-catenin in the CaP cells are O-GlcNAcylated.
18586027	6	8	theme	nuclear	687:693	arg1	higher					722:727	higher	722:727	higher	722:727	The total nuclear levels of beta-catenin are higher in the CaP cells than PNT1A but only a minimal fraction of the nuclear beta-catenin in the CaP cells are O-GlcNAcylated.
18586027	5	9	contain	have	571:574	arg1	PNT1A					564:568	PNT1A	564:568	PNT1A	564:568	We show that normal prostate cells (PNT1A) have significantly higher amounts of O-GlcNAcylated beta-catenin compared to prostate cancer (CaP) cells.
18586027	5	9	contain	have	571:574	arg2	beta-catenin					623:634	O-GlcNAcylated beta-catenin	608:634	O-GlcNAcylated beta-catenin	608:634	We show that normal prostate cells (PNT1A) have significantly higher amounts of O-GlcNAcylated beta-catenin compared to prostate cancer (CaP) cells.
18586027	5	9	contain	have	571:574	arg1	cells					557:561	normal prostate cells	541:561	normal prostate cells (PNT1A)	541:569	We show that normal prostate cells (PNT1A) have significantly higher amounts of O-GlcNAcylated beta-catenin compared to prostate cancer (CaP) cells.
18586027	5	9	contain	have	571:574	arg2	amounts					597:603	significantly higher amounts	576:603	significantly higher amounts of O-GlcNAcylated beta-catenin	576:634	We show that normal prostate cells (PNT1A) have significantly higher amounts of O-GlcNAcylated beta-catenin compared to prostate cancer (CaP) cells.
18586027	6	10	theme	total	681:685	arg1	levels					695:700	The total nuclear levels	677:700	The total nuclear levels of beta-catenin	677:716	The total nuclear levels of beta-catenin are higher in the CaP cells than PNT1A but only a minimal fraction of the nuclear beta-catenin in the CaP cells are O-GlcNAcylated.
18586027	6	10	theme	total	681:685	arg1	higher					722:727	higher	722:727	higher	722:727	The total nuclear levels of beta-catenin are higher in the CaP cells than PNT1A but only a minimal fraction of the nuclear beta-catenin in the CaP cells are O-GlcNAcylated.
18586027	6	11	theme	CaP	736:738	arg1	cells					740:744	the CaP cells	732:744	the CaP cells	732:744	The total nuclear levels of beta-catenin are higher in the CaP cells than PNT1A but only a minimal fraction of the nuclear beta-catenin in the CaP cells are O-GlcNAcylated.
18586027	6	12	from	beta-catenin	800:811	arg1	cells					824:828	the CaP cells	816:828	the CaP cells	816:828	The total nuclear levels of beta-catenin are higher in the CaP cells than PNT1A but only a minimal fraction of the nuclear beta-catenin in the CaP cells are O-GlcNAcylated.
18586027	3	13	theme	intracellular	294:306	arg1	expression					308:317	its intracellular expression	290:317	its intracellular expression	290:317	Phosphorylation of beta-catenin controls its intracellular expression but mechanism/s that regulates the nuclear localization of beta-catenin is unknown.
18586027	7	14	theme	progressive	1037:1047	arg1	decrease					1049:1056	a progressive decrease	1035:1056	a progressive decrease in the levels of beta-catenin in the nucleus	1035:1101	Increasing the levels of O-GlcNAcylated beta-catenin in the CaP cells with PUGNAc (O- (2-acetamido-2-deoxy-d-gluco-pyranosylidene) amino-N-phenylcarbamate) treatment is associated with a progressive decrease in the levels of beta-catenin in the nucleus.
18586027	8	15	theme	transcriptional	1255:1269	arg1	activity					1271:1278	its transcriptional activity	1251:1278	its transcriptional activity	1251:1278	TOPFlash reporter assay and mRNA expressions of beta-catenin's target genes indicate that O-GlcNAcylation of beta-catenin results in a decrease in its transcriptional activity.
18586027	8	16	theme	mRNA	1132:1135	arg1	expressions					1137:1147	mRNA expressions	1132:1147	mRNA expressions of beta-catenin	1132:1163	TOPFlash reporter assay and mRNA expressions of beta-catenin's target genes indicate that O-GlcNAcylation of beta-catenin results in a decrease in its transcriptional activity.
18586027	5	17	theme	prostate	648:655	arg1	CaP					665:667	CaP	665:667	CaP	665:667	We show that normal prostate cells (PNT1A) have significantly higher amounts of O-GlcNAcylated beta-catenin compared to prostate cancer (CaP) cells.
18586027	5	17	theme	prostate	648:655	arg1	cancer					657:662	prostate cancer	648:662	prostate cancer (CaP) cells	648:674	We show that normal prostate cells (PNT1A) have significantly higher amounts of O-GlcNAcylated beta-catenin compared to prostate cancer (CaP) cells.
18586027	7	18	theme	beta-catenin	1075:1086	arg1	levels					1065:1070	the levels	1061:1070	the levels of beta-catenin in the nucleus	1061:1101	Increasing the levels of O-GlcNAcylated beta-catenin in the CaP cells with PUGNAc (O- (2-acetamido-2-deoxy-d-gluco-pyranosylidene) amino-N-phenylcarbamate) treatment is associated with a progressive decrease in the levels of beta-catenin in the nucleus.
18586027	7	19	from	levels	1065:1070	arg1	nucleus					1095:1101	the nucleus	1091:1101	the nucleus	1091:1101	Increasing the levels of O-GlcNAcylated beta-catenin in the CaP cells with PUGNAc (O- (2-acetamido-2-deoxy-d-gluco-pyranosylidene) amino-N-phenylcarbamate) treatment is associated with a progressive decrease in the levels of beta-catenin in the nucleus.
18586027	8	20	theme	beta-catenin	1152:1163	arg1	assay					1122:1126	TOPFlash reporter assay	1104:1126	TOPFlash reporter assay	1104:1126	TOPFlash reporter assay and mRNA expressions of beta-catenin's target genes indicate that O-GlcNAcylation of beta-catenin results in a decrease in its transcriptional activity.
18586027	8	20	theme	beta-catenin	1152:1163	arg1	expressions					1137:1147	mRNA expressions	1132:1147	mRNA expressions of beta-catenin	1132:1163	TOPFlash reporter assay and mRNA expressions of beta-catenin's target genes indicate that O-GlcNAcylation of beta-catenin results in a decrease in its transcriptional activity.
18586027	5	21	theme	cancer	657:662	arg1	cells					670:674	prostate cancer (CaP) cells	648:674	prostate cancer (CaP) cells	648:674	We show that normal prostate cells (PNT1A) have significantly higher amounts of O-GlcNAcylated beta-catenin compared to prostate cancer (CaP) cells.
18586027	7	22	theme	CaP	910:912	arg1	cells					914:918	the CaP cells	906:918	the CaP cells	906:918	Increasing the levels of O-GlcNAcylated beta-catenin in the CaP cells with PUGNAc (O- (2-acetamido-2-deoxy-d-gluco-pyranosylidene) amino-N-phenylcarbamate) treatment is associated with a progressive decrease in the levels of beta-catenin in the nucleus.
18586027	7	23	from	levels	865:870	arg1	cells					914:918	the CaP cells	906:918	the CaP cells	906:918	Increasing the levels of O-GlcNAcylated beta-catenin in the CaP cells with PUGNAc (O- (2-acetamido-2-deoxy-d-gluco-pyranosylidene) amino-N-phenylcarbamate) treatment is associated with a progressive decrease in the levels of beta-catenin in the nucleus.
18586027	7	24	theme	beta-catenin	890:901	arg1	levels					865:870	the levels	861:870	the levels of O-GlcNAcylated beta-catenin in the CaP cells	861:918	Increasing the levels of O-GlcNAcylated beta-catenin in the CaP cells with PUGNAc (O- (2-acetamido-2-deoxy-d-gluco-pyranosylidene) amino-N-phenylcarbamate) treatment is associated with a progressive decrease in the levels of beta-catenin in the nucleus.
18586027	8	25	theme	TOPFlash	1104:1111	arg1	assay					1122:1126	TOPFlash reporter assay	1104:1126	TOPFlash reporter assay	1104:1126	TOPFlash reporter assay and mRNA expressions of beta-catenin's target genes indicate that O-GlcNAcylation of beta-catenin results in a decrease in its transcriptional activity.
18586027	8	26	theme	target	1167:1172	arg1	genes					1174:1178	TOPFlash reporter assay and mRNA expressions of beta-catenin's target genes	1104:1178	TOPFlash reporter assay and mRNA expressions of beta-catenin's target genes	1104:1178	TOPFlash reporter assay and mRNA expressions of beta-catenin's target genes indicate that O-GlcNAcylation of beta-catenin results in a decrease in its transcriptional activity.
18586027	6	27	theme	CaP	820:822	arg1	cells					824:828	the CaP cells	816:828	the CaP cells	816:828	The total nuclear levels of beta-catenin are higher in the CaP cells than PNT1A but only a minimal fraction of the nuclear beta-catenin in the CaP cells are O-GlcNAcylated.
18586027	5	28	theme	normal	541:546	arg1	PNT1A					564:568	PNT1A	564:568	PNT1A	564:568	We show that normal prostate cells (PNT1A) have significantly higher amounts of O-GlcNAcylated beta-catenin compared to prostate cancer (CaP) cells.
18586027	5	28	theme	normal	541:546	arg1	cells					557:561	normal prostate cells	541:561	normal prostate cells (PNT1A)	541:569	We show that normal prostate cells (PNT1A) have significantly higher amounts of O-GlcNAcylated beta-catenin compared to prostate cancer (CaP) cells.
18586027	6	29	from	cells	824:828	arg1	O-GlcNAcylated					834:847	O-GlcNAcylated	834:847	O-GlcNAcylated	834:847	The total nuclear levels of beta-catenin are higher in the CaP cells than PNT1A but only a minimal fraction of the nuclear beta-catenin in the CaP cells are O-GlcNAcylated.
18586027	6	29	from	cells	824:828	arg1	fraction					776:783	only a minimal fraction	761:783	only a minimal fraction of the nuclear beta-catenin in the CaP cells	761:828	The total nuclear levels of beta-catenin are higher in the CaP cells than PNT1A but only a minimal fraction of the nuclear beta-catenin in the CaP cells are O-GlcNAcylated.
18586027	0	30	theme	beta-catenin	26:37	arg1	O-GlcNAc-glycosylation					0:21	O-GlcNAc-glycosylation	0:21	O-GlcNAc-glycosylation of beta-catenin	0:37	O-GlcNAc-glycosylation of beta-catenin regulates its nuclear localization and transcriptional activity.
18586027	6	31	theme	beta-catenin	800:811	arg1	O-GlcNAcylated					834:847	O-GlcNAcylated	834:847	O-GlcNAcylated	834:847	The total nuclear levels of beta-catenin are higher in the CaP cells than PNT1A but only a minimal fraction of the nuclear beta-catenin in the CaP cells are O-GlcNAcylated.
18586027	6	31	theme	beta-catenin	800:811	arg1	fraction					776:783	only a minimal fraction	761:783	only a minimal fraction of the nuclear beta-catenin in the CaP cells	761:828	The total nuclear levels of beta-catenin are higher in the CaP cells than PNT1A but only a minimal fraction of the nuclear beta-catenin in the CaP cells are O-GlcNAcylated.
18586027	8	32	from	decrease	1239:1246	arg1	activity					1271:1278	its transcriptional activity	1251:1278	its transcriptional activity	1251:1278	TOPFlash reporter assay and mRNA expressions of beta-catenin's target genes indicate that O-GlcNAcylation of beta-catenin results in a decrease in its transcriptional activity.
18586027	5	33	theme	prostate	548:555	arg1	PNT1A					564:568	PNT1A	564:568	PNT1A	564:568	We show that normal prostate cells (PNT1A) have significantly higher amounts of O-GlcNAcylated beta-catenin compared to prostate cancer (CaP) cells.
18586027	5	33	theme	prostate	548:555	arg1	cells					557:561	normal prostate cells	541:561	normal prostate cells (PNT1A)	541:569	We show that normal prostate cells (PNT1A) have significantly higher amounts of O-GlcNAcylated beta-catenin compared to prostate cancer (CaP) cells.
18586027	6	34	from	fraction	776:783	arg1	cells					824:828	the CaP cells	816:828	the CaP cells	816:828	The total nuclear levels of beta-catenin are higher in the CaP cells than PNT1A but only a minimal fraction of the nuclear beta-catenin in the CaP cells are O-GlcNAcylated.
18586027	0	35	theme	nuclear	53:59	arg1	localization					61:72	its nuclear localization	49:72	its nuclear localization	49:72	O-GlcNAc-glycosylation of beta-catenin regulates its nuclear localization and transcriptional activity.
18586027	7	36	dep	associated	1019:1028	arg1	Increasing					850:859	Increasing	850:859	Increasing the levels of O-GlcNAcylated beta-catenin in the CaP cells with PUGNAc (O- (2-acetamido-2-deoxy-d-gluco-pyranosylidene) amino-N-phenylcarbamate)	850:1004	Increasing the levels of O-GlcNAcylated beta-catenin in the CaP cells with PUGNAc (O- (2-acetamido-2-deoxy-d-gluco-pyranosylidene) amino-N-phenylcarbamate) treatment is associated with a progressive decrease in the levels of beta-catenin in the nucleus.
18586027	0	37	gly	O-GlcNAc-glycosylation	0:21	arg1	beta-catenin					26:37	beta-catenin	26:37	beta-catenin	26:37	O-GlcNAc-glycosylation of beta-catenin regulates its nuclear localization and transcriptional activity.
18586027	7	38	theme	O-GlcNAcylated	875:888	arg1	beta-catenin					890:901	O-GlcNAcylated beta-catenin	875:901	O-GlcNAcylated beta-catenin	875:901	Increasing the levels of O-GlcNAcylated beta-catenin in the CaP cells with PUGNAc (O- (2-acetamido-2-deoxy-d-gluco-pyranosylidene) amino-N-phenylcarbamate) treatment is associated with a progressive decrease in the levels of beta-catenin in the nucleus.
18586027	5	39	theme	O-GlcNAcylated	608:621	arg1	beta-catenin					623:634	O-GlcNAcylated beta-catenin	608:634	O-GlcNAcylated beta-catenin	608:634	We show that normal prostate cells (PNT1A) have significantly higher amounts of O-GlcNAcylated beta-catenin compared to prostate cancer (CaP) cells.
18586027	2	40	theme	latter	192:197	arg1	role					199:202	The latter role	188:202	The latter role	188:202	The latter role is associated with its oncogenic properties.
18586027	5	41	theme	beta-catenin	623:634	arg1	amounts					597:603	significantly higher amounts	576:603	significantly higher amounts of O-GlcNAcylated beta-catenin	576:634	We show that normal prostate cells (PNT1A) have significantly higher amounts of O-GlcNAcylated beta-catenin compared to prostate cancer (CaP) cells.
18586027	5	41	theme	beta-catenin	623:634	arg1	beta-catenin					623:634	O-GlcNAcylated beta-catenin	608:634	O-GlcNAcylated beta-catenin	608:634	We show that normal prostate cells (PNT1A) have significantly higher amounts of O-GlcNAcylated beta-catenin compared to prostate cancer (CaP) cells.
18586027	1	42	theme	intracellular	133:145	arg1	adhesion					147:154	intracellular adhesion	133:154	intracellular adhesion	133:154	Beta-catenin plays a role in intracellular adhesion and regulating gene expression.
18586027	9	43	theme	nuclear	1347:1353	arg1	localization					1355:1366	its nuclear localization	1343:1366	its nuclear localization	1343:1366	We define a novel modification of beta-catenin that regulates its nuclear localization and transcriptional function.
18586027	4	44	theme	O-GlcNAc	423:430	arg1	O-GlcNAcylation					447:461	O-GlcNAcylation	447:461	O-GlcNAcylation	447:461	We demonstrate that O-GlcNAc glycosylation (O-GlcNAcylation) of beta-catenin negatively regulates its levels in the nucleus.
18586027	4	44	theme	O-GlcNAc	423:430	arg1	glycosylation					432:444	O-GlcNAc glycosylation	423:444	O-GlcNAc glycosylation (O-GlcNAcylation) of beta-catenin	423:478	We demonstrate that O-GlcNAc glycosylation (O-GlcNAcylation) of beta-catenin negatively regulates its levels in the nucleus.
18586027	9	45	theme	beta-catenin	1315:1326	arg1	modification					1299:1310	a novel modification	1291:1310	a novel modification of beta-catenin that regulates its nuclear localization and transcriptional function	1291:1395	We define a novel modification of beta-catenin that regulates its nuclear localization and transcriptional function.
18586027	8	46	theme	beta-catenin	1213:1224	arg1	O-GlcNAcylation					1194:1208	O-GlcNAcylation	1194:1208	O-GlcNAcylation of beta-catenin	1194:1224	TOPFlash reporter assay and mRNA expressions of beta-catenin's target genes indicate that O-GlcNAcylation of beta-catenin results in a decrease in its transcriptional activity.
18586027	2	47	theme	oncogenic	227:235	arg1	properties					237:246	its oncogenic properties	223:246	its oncogenic properties	223:246	The latter role is associated with its oncogenic properties.
18586027	6	48	theme	nuclear	792:798	arg1	beta-catenin					800:811	the nuclear beta-catenin	788:811	the nuclear beta-catenin in the CaP cells	788:828	The total nuclear levels of beta-catenin are higher in the CaP cells than PNT1A but only a minimal fraction of the nuclear beta-catenin in the CaP cells are O-GlcNAcylated.
18586027	3	49	theme	nuclear	354:360	arg1	localization					362:373	the nuclear localization	350:373	the nuclear localization of beta-catenin	350:389	Phosphorylation of beta-catenin controls its intracellular expression but mechanism/s that regulates the nuclear localization of beta-catenin is unknown.
18586027	9	50	theme	transcriptional	1372:1386	arg1	function					1388:1395	transcriptional function	1372:1395	transcriptional function	1372:1395	We define a novel modification of beta-catenin that regulates its nuclear localization and transcriptional function.
18586027	1	51	theme	regulating	160:169	arg1	expression					176:185	regulating gene expression	160:185	regulating gene expression	160:185	Beta-catenin plays a role in intracellular adhesion and regulating gene expression.
18586027	7	52	theme	2-acetamido-2-deoxy-d-gluco-pyranosylidene	937:978	arg1	PUGNAc					925:930	PUGNAc	925:930	PUGNAc (O- (2-acetamido-2-deoxy-d-gluco-pyranosylidene) amino-N-phenylcarbamate)	925:1004	Increasing the levels of O-GlcNAcylated beta-catenin in the CaP cells with PUGNAc (O- (2-acetamido-2-deoxy-d-gluco-pyranosylidene) amino-N-phenylcarbamate) treatment is associated with a progressive decrease in the levels of beta-catenin in the nucleus.
18586027	7	52	theme	2-acetamido-2-deoxy-d-gluco-pyranosylidene	937:978	arg1	amino-N-phenylcarbamate					981:1003	O- (2-acetamido-2-deoxy-d-gluco-pyranosylidene) amino-N-phenylcarbamate	933:1003	O- (2-acetamido-2-deoxy-d-gluco-pyranosylidene) amino-N-phenylcarbamate	933:1003	Increasing the levels of O-GlcNAcylated beta-catenin in the CaP cells with PUGNAc (O- (2-acetamido-2-deoxy-d-gluco-pyranosylidene) amino-N-phenylcarbamate) treatment is associated with a progressive decrease in the levels of beta-catenin in the nucleus.
18586027	5	53	theme	higher	590:595	arg1	amounts					597:603	significantly higher amounts	576:603	significantly higher amounts of O-GlcNAcylated beta-catenin	576:634	We show that normal prostate cells (PNT1A) have significantly higher amounts of O-GlcNAcylated beta-catenin compared to prostate cancer (CaP) cells.
18586027	5	53	theme	higher	590:595	arg1	beta-catenin					623:634	O-GlcNAcylated beta-catenin	608:634	O-GlcNAcylated beta-catenin	608:634	We show that normal prostate cells (PNT1A) have significantly higher amounts of O-GlcNAcylated beta-catenin compared to prostate cancer (CaP) cells.
18586027	1	54	theme	gene	171:174	arg1	expression					176:185	regulating gene expression	160:185	regulating gene expression	160:185	Beta-catenin plays a role in intracellular adhesion and regulating gene expression.
18586027	6	55	theme	beta-catenin	705:716	arg1	levels					695:700	The total nuclear levels	677:700	The total nuclear levels of beta-catenin	677:716	The total nuclear levels of beta-catenin are higher in the CaP cells than PNT1A but only a minimal fraction of the nuclear beta-catenin in the CaP cells are O-GlcNAcylated.
18586027	6	55	theme	beta-catenin	705:716	arg1	higher					722:727	higher	722:727	higher	722:727	The total nuclear levels of beta-catenin are higher in the CaP cells than PNT1A but only a minimal fraction of the nuclear beta-catenin in the CaP cells are O-GlcNAcylated.
18586027	0	56	theme	transcriptional	78:92	arg1	activity					94:101	transcriptional activity	78:101	transcriptional activity	78:101	O-GlcNAc-glycosylation of beta-catenin regulates its nuclear localization and transcriptional activity.
18586027	7	57	theme	O-	933:934	arg1	PUGNAc					925:930	PUGNAc	925:930	PUGNAc (O- (2-acetamido-2-deoxy-d-gluco-pyranosylidene) amino-N-phenylcarbamate)	925:1004	Increasing the levels of O-GlcNAcylated beta-catenin in the CaP cells with PUGNAc (O- (2-acetamido-2-deoxy-d-gluco-pyranosylidene) amino-N-phenylcarbamate) treatment is associated with a progressive decrease in the levels of beta-catenin in the nucleus.
18586027	7	57	theme	O-	933:934	arg1	amino-N-phenylcarbamate					981:1003	O- (2-acetamido-2-deoxy-d-gluco-pyranosylidene) amino-N-phenylcarbamate	933:1003	O- (2-acetamido-2-deoxy-d-gluco-pyranosylidene) amino-N-phenylcarbamate	933:1003	Increasing the levels of O-GlcNAcylated beta-catenin in the CaP cells with PUGNAc (O- (2-acetamido-2-deoxy-d-gluco-pyranosylidene) amino-N-phenylcarbamate) treatment is associated with a progressive decrease in the levels of beta-catenin in the nucleus.
23552487	8	0	theme	cell	1243:1246	arg1	proliferation					1248:1260	cell proliferation	1243:1260	cell proliferation	1243:1260	Furthermore, blocking OGT activity using the potent inhibitor Ac-5SGlcNAc prevented serum-stimulated cyclin D1 synthesis and slightly delayed cell proliferation.
23552487	7	1	theme	HeLa	1056:1059	arg1	cells					1061:1065	exponentially proliferating HeLa cells	1028:1065	exponentially proliferating HeLa cells	1028:1065	Moreover, β-catenin-2XFLAG was heavily O-GlcNAcylated in exponentially proliferating HeLa cells when compared to confluent cells.
23552487	4	2	theme	major	742:746	arg1	OGT					721:723	OGT	721:723	OGT	721:723	Co-immunoprecipitation experiments performed upon serum stimulation showed a progressive interaction between OGT and β-catenin, a major factor in the regulation of cell cycle.
23552487	4	2	theme	major	742:746	arg1	factor					748:753	a major factor	740:753	a major factor in the regulation of cell cycle	740:785	Co-immunoprecipitation experiments performed upon serum stimulation showed a progressive interaction between OGT and β-catenin, a major factor in the regulation of cell cycle.
23552487	9	3	dep	PI3K	1355:1358	arg1	activation					1369:1378	activation	1369:1378	activation	1369:1378	At last, interfering with OGT expression (siOGT) blocked cyclin D1 expression and decreased PI3K and MAPK activation.
23552487	0	4	theme	D	79:79	arg1	expression					81:90	cyclin D expression	72:90	cyclin D expression	72:90	Serum-stimulated cell cycle entry promotes ncOGT synthesis required for cyclin D expression.
23552487	1	5	theme	unique	149:154	arg1	enzyme					182:187	a unique and universally expressed enzyme	147:187	a unique and universally expressed enzyme catalyzing O-GlcNAcylation of thousands of proteins	147:239	Nuclear and cytoplasmic O-GlcNAc transferase (OGT) is a unique and universally expressed enzyme catalyzing O-GlcNAcylation of thousands of proteins.
23552487	1	5	theme	unique	149:154	arg1	transferase					126:136	O-GlcNAc transferase	117:136	Nuclear and cytoplasmic O-GlcNAc transferase (OGT)	93:142	Nuclear and cytoplasmic O-GlcNAc transferase (OGT) is a unique and universally expressed enzyme catalyzing O-GlcNAcylation of thousands of proteins.
23552487	9	6	theme	cyclin	1320:1325	arg1	D1					1327:1328	cyclin D1	1320:1328	cyclin D1 expression	1320:1339	At last, interfering with OGT expression (siOGT) blocked cyclin D1 expression and decreased PI3K and MAPK activation.
23552487	10	7	theme	OGT	1451:1453	arg1	expression					1414:1423	expression	1414:1423	expression	1414:1423	Together, our data indicate that expression and catalytic activity of OGT are necessary and essential for G0/G1 transition.
23552487	10	7	theme	OGT	1451:1453	arg1	activity					1439:1446	catalytic activity	1429:1446	catalytic activity	1429:1446	Together, our data indicate that expression and catalytic activity of OGT are necessary and essential for G0/G1 transition.
23552487	4	8	theme	cycle	781:785	arg1	regulation					762:771	the regulation	758:771	the regulation of cell cycle	758:785	Co-immunoprecipitation experiments performed upon serum stimulation showed a progressive interaction between OGT and β-catenin, a major factor in the regulation of cell cycle.
23552487	4	9	theme	Co-immunoprecipitation	612:633	arg1	experiments					635:645	Co-immunoprecipitation experiments	612:645	Co-immunoprecipitation experiments performed upon serum stimulation	612:678	Co-immunoprecipitation experiments performed upon serum stimulation showed a progressive interaction between OGT and β-catenin, a major factor in the regulation of cell cycle.
23552487	4	10	theme	cell	776:779	arg1	cycle					781:785	cell cycle	776:785	cell cycle	776:785	Co-immunoprecipitation experiments performed upon serum stimulation showed a progressive interaction between OGT and β-catenin, a major factor in the regulation of cell cycle.
23552487	6	11	theme	β-catenin-2XFLAG	917:932	arg1	status					903:908	the O-GlcNAcylation status	883:908	the O-GlcNAcylation status of the β-catenin-2XFLAG	883:932	In these cells, the O-GlcNAcylation status of the β-catenin-2XFLAG was increased following stimulation.
23552487	3	12	theme	MCF7	480:483	arg1	cells					485:489	starved MCF7 cells	472:489	starved MCF7 cells reincubated with serum	472:512	We first demonstrated that starved MCF7 cells reincubated with serum quickly induced a significant OGT increase concomitantly to activation of PI3K and MAPK pathways.
23552487	2	13	theme	intracellular	284:296	arg1	processes					298:306	many crucial intracellular processes	271:306	many crucial intracellular processes	271:306	Although OGT interferes with many crucial intracellular processes, including cell cycle, only few studies have focused on elucidating the precise role of the glycosyltransferase during cell cycle entry.
23552487	2	13	theme	intracellular	284:296	arg1	cycle					324:328	cell cycle	319:328	cell cycle	319:328	Although OGT interferes with many crucial intracellular processes, including cell cycle, only few studies have focused on elucidating the precise role of the glycosyltransferase during cell cycle entry.
23552487	7	14	from	cells	1061:1065	arg1	O-GlcNAcylated					1010:1023	O-GlcNAcylated	1010:1023	O-GlcNAcylated	1010:1023	Moreover, β-catenin-2XFLAG was heavily O-GlcNAcylated in exponentially proliferating HeLa cells when compared to confluent cells.
23552487	8	15	theme	OGT	1123:1125	arg1	activity					1127:1134	OGT activity	1123:1134	OGT activity using the potent inhibitor Ac-5SGlcNAc	1123:1173	Furthermore, blocking OGT activity using the potent inhibitor Ac-5SGlcNAc prevented serum-stimulated cyclin D1 synthesis and slightly delayed cell proliferation.
23552487	2	16	theme	crucial	276:282	arg1	processes					298:306	many crucial intracellular processes	271:306	many crucial intracellular processes	271:306	Although OGT interferes with many crucial intracellular processes, including cell cycle, only few studies have focused on elucidating the precise role of the glycosyltransferase during cell cycle entry.
23552487	2	16	theme	crucial	276:282	arg1	cycle					324:328	cell cycle	319:328	cell cycle	319:328	Although OGT interferes with many crucial intracellular processes, including cell cycle, only few studies have focused on elucidating the precise role of the glycosyltransferase during cell cycle entry.
23552487	0	17	theme	cell	17:20	arg1	entry					28:32	Serum-stimulated cell cycle entry	0:32	Serum-stimulated cell cycle entry	0:32	Serum-stimulated cell cycle entry promotes ncOGT synthesis required for cyclin D expression.
23552487	5	18	located	observed	812:819	arg2	expression					792:801	OGT expression	788:801	OGT expression	788:801	OGT expression was also observed in starved HeLa cells reincubated with serum.
23552487	5	18	located	observed	812:819	arg1	cells					837:841	starved HeLa cells	824:841	starved HeLa cells reincubated with serum	824:864	OGT expression was also observed in starved HeLa cells reincubated with serum.
23552487	3	19	theme	PI3K	588:591	arg1	pathways					602:609	PI3K and MAPK pathways	588:609	PI3K and MAPK pathways	588:609	We first demonstrated that starved MCF7 cells reincubated with serum quickly induced a significant OGT increase concomitantly to activation of PI3K and MAPK pathways.
23552487	1	20	theme	expressed	172:180	arg1	enzyme					182:187	a unique and universally expressed enzyme	147:187	a unique and universally expressed enzyme catalyzing O-GlcNAcylation of thousands of proteins	147:239	Nuclear and cytoplasmic O-GlcNAc transferase (OGT) is a unique and universally expressed enzyme catalyzing O-GlcNAcylation of thousands of proteins.
23552487	1	20	theme	expressed	172:180	arg1	transferase					126:136	O-GlcNAc transferase	117:136	Nuclear and cytoplasmic O-GlcNAc transferase (OGT)	93:142	Nuclear and cytoplasmic O-GlcNAc transferase (OGT) is a unique and universally expressed enzyme catalyzing O-GlcNAcylation of thousands of proteins.
23552487	0	21	theme	Serum-stimulated	0:15	arg1	entry					28:32	Serum-stimulated cell cycle entry	0:32	Serum-stimulated cell cycle entry	0:32	Serum-stimulated cell cycle entry promotes ncOGT synthesis required for cyclin D expression.
23552487	1	22	theme	Nuclear	93:99	arg1	OGT					139:141	OGT	139:141	OGT	139:141	Nuclear and cytoplasmic O-GlcNAc transferase (OGT) is a unique and universally expressed enzyme catalyzing O-GlcNAcylation of thousands of proteins.
23552487	1	22	theme	Nuclear	93:99	arg1	transferase					126:136	O-GlcNAc transferase	117:136	Nuclear and cytoplasmic O-GlcNAc transferase (OGT)	93:142	Nuclear and cytoplasmic O-GlcNAc transferase (OGT) is a unique and universally expressed enzyme catalyzing O-GlcNAcylation of thousands of proteins.
23552487	1	22	theme	Nuclear	93:99	arg1	enzyme					182:187	a unique and universally expressed enzyme	147:187	a unique and universally expressed enzyme catalyzing O-GlcNAcylation of thousands of proteins	147:239	Nuclear and cytoplasmic O-GlcNAc transferase (OGT) is a unique and universally expressed enzyme catalyzing O-GlcNAcylation of thousands of proteins.
23552487	2	23	theme	precise	380:386	arg1	role					388:391	the precise role	376:391	the precise role of the glycosyltransferase during cell cycle entry	376:442	Although OGT interferes with many crucial intracellular processes, including cell cycle, only few studies have focused on elucidating the precise role of the glycosyltransferase during cell cycle entry.
23552487	8	24	theme	inhibitor	1153:1161	arg1	Ac-5SGlcNAc					1163:1173	the potent inhibitor Ac-5SGlcNAc	1142:1173	the potent inhibitor Ac-5SGlcNAc	1142:1173	Furthermore, blocking OGT activity using the potent inhibitor Ac-5SGlcNAc prevented serum-stimulated cyclin D1 synthesis and slightly delayed cell proliferation.
23552487	9	25	theme	OGT	1289:1291	arg1	siOGT					1305:1309	siOGT	1305:1309	siOGT	1305:1309	At last, interfering with OGT expression (siOGT) blocked cyclin D1 expression and decreased PI3K and MAPK activation.
23552487	9	25	theme	OGT	1289:1291	arg1	expression					1293:1302	OGT expression	1289:1302	OGT expression (siOGT)	1289:1310	At last, interfering with OGT expression (siOGT) blocked cyclin D1 expression and decreased PI3K and MAPK activation.
23552487	2	26	theme	cell	319:322	arg1	cycle					324:328	cell cycle	319:328	cell cycle	319:328	Although OGT interferes with many crucial intracellular processes, including cell cycle, only few studies have focused on elucidating the precise role of the glycosyltransferase during cell cycle entry.
23552487	2	27	theme	cycle	432:436	arg1	entry					438:442	cell cycle entry	427:442	cell cycle entry	427:442	Although OGT interferes with many crucial intracellular processes, including cell cycle, only few studies have focused on elucidating the precise role of the glycosyltransferase during cell cycle entry.
23552487	0	28	theme	cycle	22:26	arg1	entry					28:32	Serum-stimulated cell cycle entry	0:32	Serum-stimulated cell cycle entry	0:32	Serum-stimulated cell cycle entry promotes ncOGT synthesis required for cyclin D expression.
23552487	3	29	theme	OGT	544:546	arg1	increase					548:555	a significant OGT increase	530:555	a significant OGT increase	530:555	We first demonstrated that starved MCF7 cells reincubated with serum quickly induced a significant OGT increase concomitantly to activation of PI3K and MAPK pathways.
23552487	1	30	theme	cytoplasmic	105:115	arg1	OGT					139:141	OGT	139:141	OGT	139:141	Nuclear and cytoplasmic O-GlcNAc transferase (OGT) is a unique and universally expressed enzyme catalyzing O-GlcNAcylation of thousands of proteins.
23552487	1	30	theme	cytoplasmic	105:115	arg1	transferase					126:136	O-GlcNAc transferase	117:136	Nuclear and cytoplasmic O-GlcNAc transferase (OGT)	93:142	Nuclear and cytoplasmic O-GlcNAc transferase (OGT) is a unique and universally expressed enzyme catalyzing O-GlcNAcylation of thousands of proteins.
23552487	1	30	theme	cytoplasmic	105:115	arg1	enzyme					182:187	a unique and universally expressed enzyme	147:187	a unique and universally expressed enzyme catalyzing O-GlcNAcylation of thousands of proteins	147:239	Nuclear and cytoplasmic O-GlcNAc transferase (OGT) is a unique and universally expressed enzyme catalyzing O-GlcNAcylation of thousands of proteins.
23552487	2	31	theme	cell	427:430	arg1	entry					438:442	cell cycle entry	427:442	cell cycle entry	427:442	Although OGT interferes with many crucial intracellular processes, including cell cycle, only few studies have focused on elucidating the precise role of the glycosyltransferase during cell cycle entry.
23552487	0	32	theme	ncOGT	43:47	arg1	synthesis					49:57	ncOGT synthesis	43:57	ncOGT synthesis required for cyclin D expression	43:90	Serum-stimulated cell cycle entry promotes ncOGT synthesis required for cyclin D expression.
23552487	6	33	theme	O-GlcNAcylation	887:901	arg1	status					903:908	the O-GlcNAcylation status	883:908	the O-GlcNAcylation status of the β-catenin-2XFLAG	883:932	In these cells, the O-GlcNAcylation status of the β-catenin-2XFLAG was increased following stimulation.
23552487	8	34	theme	potent	1146:1151	arg1	Ac-5SGlcNAc					1163:1173	the potent inhibitor Ac-5SGlcNAc	1142:1173	the potent inhibitor Ac-5SGlcNAc	1142:1173	Furthermore, blocking OGT activity using the potent inhibitor Ac-5SGlcNAc prevented serum-stimulated cyclin D1 synthesis and slightly delayed cell proliferation.
23552487	4	35	theme	progressive	689:699	arg1	interaction					701:711	a progressive interaction	687:711	a progressive interaction between OGT and β-catenin, a major factor in the regulation of cell cycle	687:785	Co-immunoprecipitation experiments performed upon serum stimulation showed a progressive interaction between OGT and β-catenin, a major factor in the regulation of cell cycle.
23552487	5	36	theme	OGT	788:790	arg1	expression					792:801	OGT expression	788:801	OGT expression	788:801	OGT expression was also observed in starved HeLa cells reincubated with serum.
23552487	9	37	theme	D1	1327:1328	arg1	expression					1330:1339	cyclin D1 expression	1320:1339	cyclin D1 expression	1320:1339	At last, interfering with OGT expression (siOGT) blocked cyclin D1 expression and decreased PI3K and MAPK activation.
23552487	7	38	theme	confluent	1084:1092	arg1	cells					1094:1098	confluent cells	1084:1098	confluent cells	1084:1098	Moreover, β-catenin-2XFLAG was heavily O-GlcNAcylated in exponentially proliferating HeLa cells when compared to confluent cells.
23552487	2	39	theme	glycosyltransferase	400:418	arg1	role					388:391	the precise role	376:391	the precise role of the glycosyltransferase during cell cycle entry	376:442	Although OGT interferes with many crucial intracellular processes, including cell cycle, only few studies have focused on elucidating the precise role of the glycosyltransferase during cell cycle entry.
23552487	5	40	theme	starved	824:830	arg1	cells					837:841	starved HeLa cells	824:841	starved HeLa cells reincubated with serum	824:864	OGT expression was also observed in starved HeLa cells reincubated with serum.
23552487	8	41	theme	cyclin	1202:1207	arg1	D1					1209:1210	cyclin D1	1202:1210	serum-stimulated cyclin D1 synthesis	1185:1220	Furthermore, blocking OGT activity using the potent inhibitor Ac-5SGlcNAc prevented serum-stimulated cyclin D1 synthesis and slightly delayed cell proliferation.
23552487	3	42	theme	MAPK	597:600	arg1	pathways					602:609	PI3K and MAPK pathways	588:609	PI3K and MAPK pathways	588:609	We first demonstrated that starved MCF7 cells reincubated with serum quickly induced a significant OGT increase concomitantly to activation of PI3K and MAPK pathways.
23552487	1	43	theme	O-GlcNAc	117:124	arg1	OGT					139:141	OGT	139:141	OGT	139:141	Nuclear and cytoplasmic O-GlcNAc transferase (OGT) is a unique and universally expressed enzyme catalyzing O-GlcNAcylation of thousands of proteins.
23552487	1	43	theme	O-GlcNAc	117:124	arg1	transferase					126:136	O-GlcNAc transferase	117:136	Nuclear and cytoplasmic O-GlcNAc transferase (OGT)	93:142	Nuclear and cytoplasmic O-GlcNAc transferase (OGT) is a unique and universally expressed enzyme catalyzing O-GlcNAcylation of thousands of proteins.
23552487	1	43	theme	O-GlcNAc	117:124	arg1	enzyme					182:187	a unique and universally expressed enzyme	147:187	a unique and universally expressed enzyme catalyzing O-GlcNAcylation of thousands of proteins	147:239	Nuclear and cytoplasmic O-GlcNAc transferase (OGT) is a unique and universally expressed enzyme catalyzing O-GlcNAcylation of thousands of proteins.
23552487	5	44	theme	HeLa	832:835	arg1	cells					837:841	starved HeLa cells	824:841	starved HeLa cells reincubated with serum	824:864	OGT expression was also observed in starved HeLa cells reincubated with serum.
23552487	8	45	theme	serum-stimulated	1185:1200	arg1	synthesis					1212:1220	serum-stimulated cyclin D1 synthesis	1185:1220	serum-stimulated cyclin D1 synthesis	1185:1220	Furthermore, blocking OGT activity using the potent inhibitor Ac-5SGlcNAc prevented serum-stimulated cyclin D1 synthesis and slightly delayed cell proliferation.
23552487	3	46	theme	pathways	602:609	arg1	activation					574:583	activation	574:583	activation of PI3K and MAPK pathways	574:609	We first demonstrated that starved MCF7 cells reincubated with serum quickly induced a significant OGT increase concomitantly to activation of PI3K and MAPK pathways.
23552487	10	47	theme	G0/G1	1487:1491	arg1	transition					1493:1502	G0/G1 transition	1487:1502	G0/G1 transition	1487:1502	Together, our data indicate that expression and catalytic activity of OGT are necessary and essential for G0/G1 transition.
23552487	2	48	theme	many	271:274	arg1	processes					298:306	many crucial intracellular processes	271:306	many crucial intracellular processes	271:306	Although OGT interferes with many crucial intracellular processes, including cell cycle, only few studies have focused on elucidating the precise role of the glycosyltransferase during cell cycle entry.
23552487	2	48	theme	many	271:274	arg1	cycle					324:328	cell cycle	319:328	cell cycle	319:328	Although OGT interferes with many crucial intracellular processes, including cell cycle, only few studies have focused on elucidating the precise role of the glycosyltransferase during cell cycle entry.
23552487	2	49	theme	few	336:338	arg1	studies					340:346	only few studies	331:346	only few studies	331:346	Although OGT interferes with many crucial intracellular processes, including cell cycle, only few studies have focused on elucidating the precise role of the glycosyltransferase during cell cycle entry.
23552487	8	50	theme	D1	1209:1210	arg1	synthesis					1212:1220	serum-stimulated cyclin D1 synthesis	1185:1220	serum-stimulated cyclin D1 synthesis	1185:1220	Furthermore, blocking OGT activity using the potent inhibitor Ac-5SGlcNAc prevented serum-stimulated cyclin D1 synthesis and slightly delayed cell proliferation.
23552487	10	51	theme	catalytic	1429:1437	arg1	activity					1439:1446	catalytic activity	1429:1446	catalytic activity	1429:1446	Together, our data indicate that expression and catalytic activity of OGT are necessary and essential for G0/G1 transition.
23552487	7	52	from	O-GlcNAcylated	1010:1023	arg1	cells					1061:1065	exponentially proliferating HeLa cells	1028:1065	exponentially proliferating HeLa cells	1028:1065	Moreover, β-catenin-2XFLAG was heavily O-GlcNAcylated in exponentially proliferating HeLa cells when compared to confluent cells.
23552487	1	53	theme	proteins	232:239	arg1	thousands					219:227	thousands	219:227	thousands of proteins	219:239	Nuclear and cytoplasmic O-GlcNAc transferase (OGT) is a unique and universally expressed enzyme catalyzing O-GlcNAcylation of thousands of proteins.
23552487	0	54	theme	cyclin	72:77	arg1	expression					81:90	cyclin D expression	72:90	cyclin D expression	72:90	Serum-stimulated cell cycle entry promotes ncOGT synthesis required for cyclin D expression.
23552487	1	55	theme	thousands	219:227	arg1	O-GlcNAcylation					200:214	O-GlcNAcylation	200:214	O-GlcNAcylation of thousands of proteins	200:239	Nuclear and cytoplasmic O-GlcNAc transferase (OGT) is a unique and universally expressed enzyme catalyzing O-GlcNAcylation of thousands of proteins.
23552487	3	56	theme	starved	472:478	arg1	cells					485:489	starved MCF7 cells	472:489	starved MCF7 cells reincubated with serum	472:512	We first demonstrated that starved MCF7 cells reincubated with serum quickly induced a significant OGT increase concomitantly to activation of PI3K and MAPK pathways.
23552487	4	57	from	factor	748:753	arg1	regulation					762:771	the regulation	758:771	the regulation of cell cycle	758:785	Co-immunoprecipitation experiments performed upon serum stimulation showed a progressive interaction between OGT and β-catenin, a major factor in the regulation of cell cycle.
23552487	4	58	theme	serum	662:666	arg1	stimulation					668:678	serum stimulation	662:678	serum stimulation	662:678	Co-immunoprecipitation experiments performed upon serum stimulation showed a progressive interaction between OGT and β-catenin, a major factor in the regulation of cell cycle.
23552487	7	59	theme	proliferating	1042:1054	arg1	cells					1061:1065	exponentially proliferating HeLa cells	1028:1065	exponentially proliferating HeLa cells	1028:1065	Moreover, β-catenin-2XFLAG was heavily O-GlcNAcylated in exponentially proliferating HeLa cells when compared to confluent cells.
23552487	3	60	theme	significant	532:542	arg1	increase					548:555	a significant OGT increase	530:555	a significant OGT increase	530:555	We first demonstrated that starved MCF7 cells reincubated with serum quickly induced a significant OGT increase concomitantly to activation of PI3K and MAPK pathways.
26923859	10	0	theme	β-catenin	1492:1500	arg1	expression					1465:1474	a higher expression	1456:1474	a higher expression of intranuclear β-catenin in high glucose medium	1456:1523	Subcellular fractionation experiments showed that AN3CA cells had a higher expression of intranuclear β-catenin in high glucose medium.
26923859	4	1	from	influence	475:483	arg1	pathway					533:539	the WNT/β-catenin pathway	515:539	the WNT/β-catenin pathway in EC	515:545	In the present study, we explored the influence of elevated glucose levels on the WNT/β-catenin pathway in EC.
26923859	5	2	theme	biosynthesis	645:656	arg1	HBP					667:669	HBP	667:669	HBP	667:669	Previous studies have suggested that elevated concentrations of glucose can drive the hexosamine biosynthesis pathway (HBP) flux, thereby enhancing the O-GlcNAc modification of proteins.
26923859	5	2	theme	biosynthesis	645:656	arg1	pathway					658:664	hexosamine biosynthesis pathway	634:664	the hexosamine biosynthesis pathway (HBP) flux	630:675	Previous studies have suggested that elevated concentrations of glucose can drive the hexosamine biosynthesis pathway (HBP) flux, thereby enhancing the O-GlcNAc modification of proteins.
26923859	2	3	theme	greater	274:280	arg1	levels					266:271	fasting glucose levels	250:271	fasting glucose levels (greater than 5.6mmol/L)	250:296	Associations between fasting glucose levels (greater than 5.6mmol/L) and the risk of cancer fatality have been reported.
26923859	2	3	theme	greater	274:280	arg1	5.6mmol/L					287:295	greater than 5.6mmol/L	274:295	greater than 5.6mmol/L	274:295	Associations between fasting glucose levels (greater than 5.6mmol/L) and the risk of cancer fatality have been reported.
26923859	12	4	theme	O-GlcNAcylation	1741:1755	arg1	level					1757:1761	the O-GlcNAcylation level	1737:1761	the O-GlcNAcylation level	1737:1761	In conclusion, elevated glucose levels, via HBP, increase the O-GlcNAcylation level, thereby inducing the over expression of β-catenin and subsequent transcription of the target genes in EC cells.
26923859	6	5	theme	cell	756:759	arg1	HEC-1-B					778:784	HEC-1-B	778:784	HEC-1-B	778:784	Here, we cultured EC cell lines, AN3CA and HEC-1-B, with various concentrations of glucose.
26923859	6	5	theme	cell	756:759	arg1	AN3CA					768:772	AN3CA	768:772	AN3CA	768:772	Here, we cultured EC cell lines, AN3CA and HEC-1-B, with various concentrations of glucose.
26923859	6	5	theme	cell	756:759	arg1	lines					761:765	EC cell lines	753:765	EC cell lines	753:765	Here, we cultured EC cell lines, AN3CA and HEC-1-B, with various concentrations of glucose.
26923859	4	6	from	pathway	533:539	arg1	EC					544:545	EC	544:545	EC	544:545	In the present study, we explored the influence of elevated glucose levels on the WNT/β-catenin pathway in EC.
26923859	7	7	theme	HBP	1018:1020	arg1	Azaserine					1034:1042	Azaserine	1034:1042	Azaserine	1034:1042	Results showed that when treated with high levels of glucose, both lines showed increased expression of β-catenin and O-GlcNAcylation levels; however, these effects could be abolished by the HBP inhibitors, Azaserine and 6-Diazo-5-oxo-l-norleucine, and be restored by glucosamine.
26923859	7	7	theme	HBP	1018:1020	arg1	inhibitors					1022:1031	the HBP inhibitors	1014:1031	the HBP inhibitors	1014:1031	Results showed that when treated with high levels of glucose, both lines showed increased expression of β-catenin and O-GlcNAcylation levels; however, these effects could be abolished by the HBP inhibitors, Azaserine and 6-Diazo-5-oxo-l-norleucine, and be restored by glucosamine.
26923859	7	7	theme	HBP	1018:1020	arg1	6-Diazo-5-oxo-l-norleucine					1048:1073	6-Diazo-5-oxo-l-norleucine	1048:1073	6-Diazo-5-oxo-l-norleucine	1048:1073	Results showed that when treated with high levels of glucose, both lines showed increased expression of β-catenin and O-GlcNAcylation levels; however, these effects could be abolished by the HBP inhibitors, Azaserine and 6-Diazo-5-oxo-l-norleucine, and be restored by glucosamine.
26923859	1	8	theme	common	181:186	arg1	malignancies					202:213	the most common gynecological malignancies	172:213	the most common gynecological malignancies in the world	172:226	Endometrial cancer (EC) is one of the most common gynecological malignancies in the world.
26923859	1	9	theme	malignancies	202:213	arg1	one					165:167	one	165:167	one	165:167	Endometrial cancer (EC) is one of the most common gynecological malignancies in the world.
26923859	1	9	theme	malignancies	202:213	arg1	malignancies					202:213	the most common gynecological malignancies	172:213	the most common gynecological malignancies in the world	172:226	Endometrial cancer (EC) is one of the most common gynecological malignancies in the world.
26923859	12	10	from	transcription	1829:1841	arg1	cells					1869:1873	EC cells	1866:1873	EC cells	1866:1873	In conclusion, elevated glucose levels, via HBP, increase the O-GlcNAcylation level, thereby inducing the over expression of β-catenin and subsequent transcription of the target genes in EC cells.
26923859	12	11	theme	elevated	1694:1701	arg1	levels					1711:1716	elevated glucose levels	1694:1716	elevated glucose levels	1694:1716	In conclusion, elevated glucose levels, via HBP, increase the O-GlcNAcylation level, thereby inducing the over expression of β-catenin and subsequent transcription of the target genes in EC cells.
26923859	2	12	theme	fasting	250:256	arg1	levels					266:271	fasting glucose levels	250:271	fasting glucose levels (greater than 5.6mmol/L)	250:296	Associations between fasting glucose levels (greater than 5.6mmol/L) and the risk of cancer fatality have been reported.
26923859	2	12	theme	fasting	250:256	arg1	5.6mmol/L					287:295	greater than 5.6mmol/L	274:295	greater than 5.6mmol/L	274:295	Associations between fasting glucose levels (greater than 5.6mmol/L) and the risk of cancer fatality have been reported.
26923859	1	13	theme	Endometrial	138:148	arg1	EC					158:159	EC	158:159	EC	158:159	Endometrial cancer (EC) is one of the most common gynecological malignancies in the world.
26923859	1	13	theme	Endometrial	138:148	arg1	cancer					150:155	Endometrial cancer	138:155	Endometrial cancer (EC)	138:160	Endometrial cancer (EC) is one of the most common gynecological malignancies in the world.
26923859	10	14	theme	Subcellular	1390:1400	arg1	experiments					1416:1426	Subcellular fractionation experiments	1390:1426	Subcellular fractionation experiments	1390:1426	Subcellular fractionation experiments showed that AN3CA cells had a higher expression of intranuclear β-catenin in high glucose medium.
26923859	7	15	theme	increased	907:915	arg1	expression					917:926	increased expression	907:926	increased expression of β-catenin and O-GlcNAcylation levels	907:966	Results showed that when treated with high levels of glucose, both lines showed increased expression of β-catenin and O-GlcNAcylation levels; however, these effects could be abolished by the HBP inhibitors, Azaserine and 6-Diazo-5-oxo-l-norleucine, and be restored by glucosamine.
26923859	0	16	theme	hexosamine	83:92	arg1	pathway					107:113	the hexosamine biosynthesis pathway	79:113	the hexosamine biosynthesis pathway	79:113	Elevated glucose levels impair the WNT/β-catenin pathway via the activation of the hexosamine biosynthesis pathway in endometrial cancer.
26923859	4	17	theme	present	444:450	arg1	study					452:456	the present study	440:456	the present study	440:456	In the present study, we explored the influence of elevated glucose levels on the WNT/β-catenin pathway in EC.
26923859	0	18	theme	pathway	107:113	arg1	activation					65:74	the activation	61:74	the activation of the hexosamine biosynthesis pathway in endometrial cancer	61:135	Elevated glucose levels impair the WNT/β-catenin pathway via the activation of the hexosamine biosynthesis pathway in endometrial cancer.
26923859	12	19	theme	EC	1866:1867	arg1	cells					1869:1873	EC cells	1866:1873	EC cells	1866:1873	In conclusion, elevated glucose levels, via HBP, increase the O-GlcNAcylation level, thereby inducing the over expression of β-catenin and subsequent transcription of the target genes in EC cells.
26923859	0	20	theme	Elevated	0:7	arg1	levels					17:22	Elevated glucose levels	0:22	Elevated glucose levels	0:22	Elevated glucose levels impair the WNT/β-catenin pathway via the activation of the hexosamine biosynthesis pathway in endometrial cancer.
26923859	5	21	theme	Previous	548:555	arg1	studies					557:563	Previous studies	548:563	Previous studies	548:563	Previous studies have suggested that elevated concentrations of glucose can drive the hexosamine biosynthesis pathway (HBP) flux, thereby enhancing the O-GlcNAc modification of proteins.
26923859	7	22	dep	β-catenin	931:939	arg1	levels					961:966	levels	961:966	levels	961:966	Results showed that when treated with high levels of glucose, both lines showed increased expression of β-catenin and O-GlcNAcylation levels; however, these effects could be abolished by the HBP inhibitors, Azaserine and 6-Diazo-5-oxo-l-norleucine, and be restored by glucosamine.
26923859	3	23	theme	glucose	387:393	arg1	disease					405:411	glucose metabolic disease	387:411	glucose metabolic disease	387:411	However, the underlying link between glucose metabolic disease and EC remains unclear.
26923859	9	24	theme	glucose	1302:1308	arg1	levels					1310:1315	elevated glucose levels	1293:1315	elevated glucose levels	1293:1315	The results suggest that elevated glucose levels increase β-catenin expression via the activation of the HBP in EC cells.
26923859	12	25	theme	genes	1857:1861	arg1	transcription					1829:1841	β-catenin and subsequent transcription	1804:1841	β-catenin and subsequent transcription of the target genes in EC cells	1804:1873	In conclusion, elevated glucose levels, via HBP, increase the O-GlcNAcylation level, thereby inducing the over expression of β-catenin and subsequent transcription of the target genes in EC cells.
26923859	4	26	theme	elevated	488:495	arg1	levels					505:510	elevated glucose levels	488:510	elevated glucose levels	488:510	In the present study, we explored the influence of elevated glucose levels on the WNT/β-catenin pathway in EC.
26923859	10	27	theme	intranuclear	1479:1490	arg1	β-catenin					1492:1500	intranuclear β-catenin	1479:1500	intranuclear β-catenin	1479:1500	Subcellular fractionation experiments showed that AN3CA cells had a higher expression of intranuclear β-catenin in high glucose medium.
26923859	2	28	theme	fatality	321:328	arg1	levels					266:271	fasting glucose levels	250:271	fasting glucose levels (greater than 5.6mmol/L)	250:296	Associations between fasting glucose levels (greater than 5.6mmol/L) and the risk of cancer fatality have been reported.
26923859	2	28	theme	fatality	321:328	arg1	risk					306:309	the risk	302:309	the risk of cancer fatality	302:328	Associations between fasting glucose levels (greater than 5.6mmol/L) and the risk of cancer fatality have been reported.
26923859	2	28	theme	fatality	321:328	arg1	5.6mmol/L					287:295	greater than 5.6mmol/L	274:295	greater than 5.6mmol/L	274:295	Associations between fasting glucose levels (greater than 5.6mmol/L) and the risk of cancer fatality have been reported.
26923859	9	29	from	activation	1355:1364	arg1	cells					1383:1387	EC cells	1380:1387	EC cells	1380:1387	The results suggest that elevated glucose levels increase β-catenin expression via the activation of the HBP in EC cells.
26923859	6	30	theme	various	792:798	arg1	concentrations					800:813	various concentrations	792:813	various concentrations of glucose	792:824	Here, we cultured EC cell lines, AN3CA and HEC-1-B, with various concentrations of glucose.
26923859	12	31	theme	β-catenin	1804:1812	arg1	transcription					1829:1841	β-catenin and subsequent transcription	1804:1841	β-catenin and subsequent transcription of the target genes in EC cells	1804:1873	In conclusion, elevated glucose levels, via HBP, increase the O-GlcNAcylation level, thereby inducing the over expression of β-catenin and subsequent transcription of the target genes in EC cells.
26923859	4	32	theme	levels	505:510	arg1	influence					475:483	the influence	471:483	the influence of elevated glucose levels on the WNT/β-catenin pathway in EC	471:545	In the present study, we explored the influence of elevated glucose levels on the WNT/β-catenin pathway in EC.
26923859	12	33	theme	transcription	1829:1841	arg1	expression					1790:1799	expression	1790:1799	expression of β-catenin and subsequent transcription of the target genes in EC cells	1790:1873	In conclusion, elevated glucose levels, via HBP, increase the O-GlcNAcylation level, thereby inducing the over expression of β-catenin and subsequent transcription of the target genes in EC cells.
26923859	10	34	theme	glucose	1510:1516	arg1	medium					1518:1523	high glucose medium	1505:1523	high glucose medium	1505:1523	Subcellular fractionation experiments showed that AN3CA cells had a higher expression of intranuclear β-catenin in high glucose medium.
26923859	11	35	theme	increased	1600:1608	arg1	expression					1610:1619	glucose-induced increased expression	1584:1619	glucose-induced increased expression of β-catenin	1584:1632	Furthermore, TOP/FOP-Flash and RT-PCR results showed that glucose-induced increased expression of β-catenin triggered the transcription of target genes.
26923859	5	36	theme	hexosamine	634:643	arg1	HBP					667:669	HBP	667:669	HBP	667:669	Previous studies have suggested that elevated concentrations of glucose can drive the hexosamine biosynthesis pathway (HBP) flux, thereby enhancing the O-GlcNAc modification of proteins.
26923859	5	36	theme	hexosamine	634:643	arg1	pathway					658:664	hexosamine biosynthesis pathway	634:664	the hexosamine biosynthesis pathway (HBP) flux	630:675	Previous studies have suggested that elevated concentrations of glucose can drive the hexosamine biosynthesis pathway (HBP) flux, thereby enhancing the O-GlcNAc modification of proteins.
26923859	2	37	theme	than	282:285	arg1	levels					266:271	fasting glucose levels	250:271	fasting glucose levels (greater than 5.6mmol/L)	250:296	Associations between fasting glucose levels (greater than 5.6mmol/L) and the risk of cancer fatality have been reported.
26923859	2	37	theme	than	282:285	arg1	5.6mmol/L					287:295	greater than 5.6mmol/L	274:295	greater than 5.6mmol/L	274:295	Associations between fasting glucose levels (greater than 5.6mmol/L) and the risk of cancer fatality have been reported.
26923859	9	38	theme	HBP	1373:1375	arg1	activation					1355:1364	the activation	1351:1364	the activation of the HBP in EC cells	1351:1387	The results suggest that elevated glucose levels increase β-catenin expression via the activation of the HBP in EC cells.
26923859	11	39	theme	target	1665:1670	arg1	genes					1672:1676	target genes	1665:1676	target genes	1665:1676	Furthermore, TOP/FOP-Flash and RT-PCR results showed that glucose-induced increased expression of β-catenin triggered the transcription of target genes.
26923859	9	40	theme	EC	1380:1381	arg1	cells					1383:1387	EC cells	1380:1387	EC cells	1380:1387	The results suggest that elevated glucose levels increase β-catenin expression via the activation of the HBP in EC cells.
26923859	8	41	theme	AN3CA	1121:1125	arg1	cells					1139:1143	the AN3CA and HEC-1-B cells	1117:1143	cells	1139:1143	Moreover the AN3CA and HEC-1-B cells that were cultured with or without PUGNAc, an inhibitor of the O-GlcNAcase, showed that PUGNAc increased β-catenin levels.
26923859	5	42	theme	glucose	612:618	arg1	concentrations					594:607	elevated concentrations	585:607	elevated concentrations of glucose	585:618	Previous studies have suggested that elevated concentrations of glucose can drive the hexosamine biosynthesis pathway (HBP) flux, thereby enhancing the O-GlcNAc modification of proteins.
26923859	6	43	theme	EC	753:754	arg1	HEC-1-B					778:784	HEC-1-B	778:784	HEC-1-B	778:784	Here, we cultured EC cell lines, AN3CA and HEC-1-B, with various concentrations of glucose.
26923859	6	43	theme	EC	753:754	arg1	AN3CA					768:772	AN3CA	768:772	AN3CA	768:772	Here, we cultured EC cell lines, AN3CA and HEC-1-B, with various concentrations of glucose.
26923859	6	43	theme	EC	753:754	arg1	lines					761:765	EC cell lines	753:765	EC cell lines	753:765	Here, we cultured EC cell lines, AN3CA and HEC-1-B, with various concentrations of glucose.
26923859	8	44	theme	HEC-1-B	1131:1137	arg1	cells					1139:1143	the AN3CA and HEC-1-B cells	1117:1143	cells	1139:1143	Moreover the AN3CA and HEC-1-B cells that were cultured with or without PUGNAc, an inhibitor of the O-GlcNAcase, showed that PUGNAc increased β-catenin levels.
26923859	1	45	theme	gynecological	188:200	arg1	malignancies					202:213	the most common gynecological malignancies	172:213	the most common gynecological malignancies in the world	172:226	Endometrial cancer (EC) is one of the most common gynecological malignancies in the world.
26923859	0	46	from	activation	65:74	arg1	cancer					130:135	endometrial cancer	118:135	endometrial cancer	118:135	Elevated glucose levels impair the WNT/β-catenin pathway via the activation of the hexosamine biosynthesis pathway in endometrial cancer.
26923859	8	47	theme	O-GlcNAcase	1208:1218	arg1	PUGNAc					1180:1185	PUGNAc	1180:1185	PUGNAc	1180:1185	Moreover the AN3CA and HEC-1-B cells that were cultured with or without PUGNAc, an inhibitor of the O-GlcNAcase, showed that PUGNAc increased β-catenin levels.
26923859	8	47	theme	O-GlcNAcase	1208:1218	arg1	inhibitor					1191:1199	an inhibitor	1188:1199	an inhibitor of the O-GlcNAcase	1188:1218	Moreover the AN3CA and HEC-1-B cells that were cultured with or without PUGNAc, an inhibitor of the O-GlcNAcase, showed that PUGNAc increased β-catenin levels.
26923859	5	48	theme	pathway	658:664	arg1	flux					672:675	the hexosamine biosynthesis pathway (HBP) flux	630:675	the hexosamine biosynthesis pathway (HBP) flux	630:675	Previous studies have suggested that elevated concentrations of glucose can drive the hexosamine biosynthesis pathway (HBP) flux, thereby enhancing the O-GlcNAc modification of proteins.
26923859	1	49	from	malignancies	202:213	arg1	world					222:226	the world	218:226	the world	218:226	Endometrial cancer (EC) is one of the most common gynecological malignancies in the world.
26923859	2	50	theme	glucose	258:264	arg1	levels					266:271	fasting glucose levels	250:271	fasting glucose levels (greater than 5.6mmol/L)	250:296	Associations between fasting glucose levels (greater than 5.6mmol/L) and the risk of cancer fatality have been reported.
26923859	2	50	theme	glucose	258:264	arg1	5.6mmol/L					287:295	greater than 5.6mmol/L	274:295	greater than 5.6mmol/L	274:295	Associations between fasting glucose levels (greater than 5.6mmol/L) and the risk of cancer fatality have been reported.
26923859	10	51	contain	had	1452:1454	arg2	expression					1465:1474	a higher expression	1456:1474	a higher expression of intranuclear β-catenin in high glucose medium	1456:1523	Subcellular fractionation experiments showed that AN3CA cells had a higher expression of intranuclear β-catenin in high glucose medium.
26923859	10	51	contain	had	1452:1454	arg1	cells					1446:1450	AN3CA cells	1440:1450	AN3CA cells	1440:1450	Subcellular fractionation experiments showed that AN3CA cells had a higher expression of intranuclear β-catenin in high glucose medium.
26923859	5	52	theme	proteins	725:732	arg1	modification					709:720	the O-GlcNAc modification	696:720	the O-GlcNAc modification of proteins	696:732	Previous studies have suggested that elevated concentrations of glucose can drive the hexosamine biosynthesis pathway (HBP) flux, thereby enhancing the O-GlcNAc modification of proteins.
26923859	7	53	theme	O-GlcNAcylation	945:959	arg1	expression					917:926	increased expression	907:926	increased expression of β-catenin and O-GlcNAcylation levels	907:966	Results showed that when treated with high levels of glucose, both lines showed increased expression of β-catenin and O-GlcNAcylation levels; however, these effects could be abolished by the HBP inhibitors, Azaserine and 6-Diazo-5-oxo-l-norleucine, and be restored by glucosamine.
26923859	12	54	theme	glucose	1703:1709	arg1	levels					1711:1716	elevated glucose levels	1694:1716	elevated glucose levels	1694:1716	In conclusion, elevated glucose levels, via HBP, increase the O-GlcNAcylation level, thereby inducing the over expression of β-catenin and subsequent transcription of the target genes in EC cells.
26923859	8	55	theme	β-catenin	1250:1258	arg1	levels					1260:1265	β-catenin levels	1250:1265	β-catenin levels	1250:1265	Moreover the AN3CA and HEC-1-B cells that were cultured with or without PUGNAc, an inhibitor of the O-GlcNAcase, showed that PUGNAc increased β-catenin levels.
26923859	5	56	theme	O-GlcNAc	700:707	arg1	modification					709:720	the O-GlcNAc modification	696:720	the O-GlcNAc modification of proteins	696:732	Previous studies have suggested that elevated concentrations of glucose can drive the hexosamine biosynthesis pathway (HBP) flux, thereby enhancing the O-GlcNAc modification of proteins.
26923859	7	57	theme	β-catenin	931:939	arg1	expression					917:926	increased expression	907:926	increased expression of β-catenin and O-GlcNAcylation levels	907:966	Results showed that when treated with high levels of glucose, both lines showed increased expression of β-catenin and O-GlcNAcylation levels; however, these effects could be abolished by the HBP inhibitors, Azaserine and 6-Diazo-5-oxo-l-norleucine, and be restored by glucosamine.
26923859	10	58	from	expression	1465:1474	arg1	medium					1518:1523	high glucose medium	1505:1523	high glucose medium	1505:1523	Subcellular fractionation experiments showed that AN3CA cells had a higher expression of intranuclear β-catenin in high glucose medium.
26923859	0	59	theme	endometrial	118:128	arg1	cancer					130:135	endometrial cancer	118:135	endometrial cancer	118:135	Elevated glucose levels impair the WNT/β-catenin pathway via the activation of the hexosamine biosynthesis pathway in endometrial cancer.
26923859	0	60	theme	biosynthesis	94:105	arg1	pathway					107:113	the hexosamine biosynthesis pathway	79:113	the hexosamine biosynthesis pathway	79:113	Elevated glucose levels impair the WNT/β-catenin pathway via the activation of the hexosamine biosynthesis pathway in endometrial cancer.
26923859	12	61	from	cells	1869:1873	arg1	expression					1790:1799	expression	1790:1799	expression of β-catenin and subsequent transcription of the target genes in EC cells	1790:1873	In conclusion, elevated glucose levels, via HBP, increase the O-GlcNAcylation level, thereby inducing the over expression of β-catenin and subsequent transcription of the target genes in EC cells.
26923859	5	62	theme	elevated	585:592	arg1	concentrations					594:607	elevated concentrations	585:607	elevated concentrations of glucose	585:618	Previous studies have suggested that elevated concentrations of glucose can drive the hexosamine biosynthesis pathway (HBP) flux, thereby enhancing the O-GlcNAc modification of proteins.
26923859	0	63	theme	glucose	9:15	arg1	levels					17:22	Elevated glucose levels	0:22	Elevated glucose levels	0:22	Elevated glucose levels impair the WNT/β-catenin pathway via the activation of the hexosamine biosynthesis pathway in endometrial cancer.
26923859	3	64	theme	underlying	363:372	arg1	link					374:377	the underlying link	359:377	the underlying link between glucose metabolic disease and EC	359:418	However, the underlying link between glucose metabolic disease and EC remains unclear.
26923859	4	65	theme	WNT/β-catenin	519:531	arg1	pathway					533:539	the WNT/β-catenin pathway	515:539	the WNT/β-catenin pathway in EC	515:545	In the present study, we explored the influence of elevated glucose levels on the WNT/β-catenin pathway in EC.
26923859	10	66	theme	fractionation	1402:1414	arg1	experiments					1416:1426	Subcellular fractionation experiments	1390:1426	Subcellular fractionation experiments	1390:1426	Subcellular fractionation experiments showed that AN3CA cells had a higher expression of intranuclear β-catenin in high glucose medium.
26923859	12	67	theme	target	1850:1855	arg1	genes					1857:1861	the target genes	1846:1861	the target genes	1846:1861	In conclusion, elevated glucose levels, via HBP, increase the O-GlcNAcylation level, thereby inducing the over expression of β-catenin and subsequent transcription of the target genes in EC cells.
26923859	7	68	theme	glucose	880:886	arg1	levels					870:875	high levels	865:875	high levels of glucose	865:886	Results showed that when treated with high levels of glucose, both lines showed increased expression of β-catenin and O-GlcNAcylation levels; however, these effects could be abolished by the HBP inhibitors, Azaserine and 6-Diazo-5-oxo-l-norleucine, and be restored by glucosamine.
26923859	0	69	theme	WNT/β-catenin	35:47	arg1	pathway					49:55	the WNT/β-catenin pathway	31:55	the WNT/β-catenin pathway	31:55	Elevated glucose levels impair the WNT/β-catenin pathway via the activation of the hexosamine biosynthesis pathway in endometrial cancer.
26923859	9	70	theme	elevated	1293:1300	arg1	levels					1310:1315	elevated glucose levels	1293:1315	elevated glucose levels	1293:1315	The results suggest that elevated glucose levels increase β-catenin expression via the activation of the HBP in EC cells.
26923859	6	71	theme	glucose	818:824	arg1	concentrations					800:813	various concentrations	792:813	various concentrations of glucose	792:824	Here, we cultured EC cell lines, AN3CA and HEC-1-B, with various concentrations of glucose.
26923859	3	72	theme	metabolic	395:403	arg1	disease					405:411	glucose metabolic disease	387:411	glucose metabolic disease	387:411	However, the underlying link between glucose metabolic disease and EC remains unclear.
26923859	4	73	theme	glucose	497:503	arg1	levels					505:510	elevated glucose levels	488:510	elevated glucose levels	488:510	In the present study, we explored the influence of elevated glucose levels on the WNT/β-catenin pathway in EC.
26923859	10	74	theme	AN3CA	1440:1444	arg1	cells					1446:1450	AN3CA cells	1440:1450	AN3CA cells	1440:1450	Subcellular fractionation experiments showed that AN3CA cells had a higher expression of intranuclear β-catenin in high glucose medium.
26923859	11	75	theme	genes	1672:1676	arg1	transcription					1648:1660	the transcription	1644:1660	the transcription of target genes	1644:1676	Furthermore, TOP/FOP-Flash and RT-PCR results showed that glucose-induced increased expression of β-catenin triggered the transcription of target genes.
26923859	11	76	theme	RT-PCR	1557:1562	arg1	results					1564:1570	TOP/FOP-Flash and RT-PCR results	1539:1570	TOP/FOP-Flash and RT-PCR results	1539:1570	Furthermore, TOP/FOP-Flash and RT-PCR results showed that glucose-induced increased expression of β-catenin triggered the transcription of target genes.
26923859	12	77	theme	subsequent	1818:1827	arg1	transcription					1829:1841	β-catenin and subsequent transcription	1804:1841	β-catenin and subsequent transcription of the target genes in EC cells	1804:1873	In conclusion, elevated glucose levels, via HBP, increase the O-GlcNAcylation level, thereby inducing the over expression of β-catenin and subsequent transcription of the target genes in EC cells.
26923859	11	78	theme	TOP/FOP-Flash	1539:1551	arg1	results					1564:1570	TOP/FOP-Flash and RT-PCR results	1539:1570	TOP/FOP-Flash and RT-PCR results	1539:1570	Furthermore, TOP/FOP-Flash and RT-PCR results showed that glucose-induced increased expression of β-catenin triggered the transcription of target genes.
26923859	2	79	theme	cancer	314:319	arg1	fatality					321:328	cancer fatality	314:328	cancer fatality	314:328	Associations between fasting glucose levels (greater than 5.6mmol/L) and the risk of cancer fatality have been reported.
26923859	7	80	theme	high	865:868	arg1	levels					870:875	high levels	865:875	high levels of glucose	865:886	Results showed that when treated with high levels of glucose, both lines showed increased expression of β-catenin and O-GlcNAcylation levels; however, these effects could be abolished by the HBP inhibitors, Azaserine and 6-Diazo-5-oxo-l-norleucine, and be restored by glucosamine.
26923859	9	81	theme	β-catenin	1326:1334	arg1	expression					1336:1345	β-catenin expression	1326:1345	β-catenin expression	1326:1345	The results suggest that elevated glucose levels increase β-catenin expression via the activation of the HBP in EC cells.
26923859	12	82	from	expression	1790:1799	arg1	cells					1869:1873	EC cells	1866:1873	EC cells	1866:1873	In conclusion, elevated glucose levels, via HBP, increase the O-GlcNAcylation level, thereby inducing the over expression of β-catenin and subsequent transcription of the target genes in EC cells.
26923859	10	83	theme	higher	1458:1463	arg1	expression					1465:1474	a higher expression	1456:1474	a higher expression of intranuclear β-catenin in high glucose medium	1456:1523	Subcellular fractionation experiments showed that AN3CA cells had a higher expression of intranuclear β-catenin in high glucose medium.
26923859	11	84	theme	glucose-induced	1584:1598	arg1	expression					1610:1619	glucose-induced increased expression	1584:1619	glucose-induced increased expression of β-catenin	1584:1632	Furthermore, TOP/FOP-Flash and RT-PCR results showed that glucose-induced increased expression of β-catenin triggered the transcription of target genes.
26923859	10	85	theme	high	1505:1508	arg1	medium					1518:1523	high glucose medium	1505:1523	high glucose medium	1505:1523	Subcellular fractionation experiments showed that AN3CA cells had a higher expression of intranuclear β-catenin in high glucose medium.
26923859	11	86	theme	β-catenin	1624:1632	arg1	expression					1610:1619	glucose-induced increased expression	1584:1619	glucose-induced increased expression of β-catenin	1584:1632	Furthermore, TOP/FOP-Flash and RT-PCR results showed that glucose-induced increased expression of β-catenin triggered the transcription of target genes.
31626249	0	0	from	inhibition	18:27	arg1	cells					56:60	cells	56:60	cells	56:60	Targeted covalent inhibition of O-GlcNAc transferase in cells.
31626249	4	1	theme	cellular	445:452	arg1	functions					458:466	cellular OGT functions	445:466	cellular OGT functions	445:466	This study provides a new strategy to interrogate cellular OGT functions and to investigate other glycosyltransferases.
31626249	0	2	from	cells	56:60	arg1	inhibition					18:27	covalent inhibition	9:27	covalent inhibition of O-GlcNAc transferase in cells	9:60	Targeted covalent inhibition of O-GlcNAc transferase in cells.
31626249	1	3	theme	O-GlcNAc	63:70	arg1	transferase					72:82	O-GlcNAc transferase	63:82	O-GlcNAc transferase (OGT)	63:88	O-GlcNAc transferase (OGT) glycosylates numerous proteins and is implicated in many diseases.
31626249	1	3	theme	O-GlcNAc	63:70	arg1	OGT					85:87	OGT	85:87	OGT	85:87	O-GlcNAc transferase (OGT) glycosylates numerous proteins and is implicated in many diseases.
31626249	1	4	gly	glycosylates	90:101	arg1	proteins					112:119	numerous proteins	103:119	numerous proteins	103:119	O-GlcNAc transferase (OGT) glycosylates numerous proteins and is implicated in many diseases.
31626249	0	5	from	transferase	41:51	arg1	cells					56:60	cells	56:60	cells	56:60	Targeted covalent inhibition of O-GlcNAc transferase in cells.
31626249	3	6	theme	similar	378:384	arg1	enzymes					386:392	other functionally similar enzymes	359:392	other functionally similar enzymes	359:392	We report the first targeted covalent inhibitor that predominantly reacts with OGT but does not affect other functionally similar enzymes.
31626249	3	7	theme	other	359:363	arg1	enzymes					386:392	other functionally similar enzymes	359:392	other functionally similar enzymes	359:392	We report the first targeted covalent inhibitor that predominantly reacts with OGT but does not affect other functionally similar enzymes.
31626249	3	8	theme	first	270:274	arg1	inhibitor					294:302	the first targeted covalent inhibitor	266:302	the first targeted covalent inhibitor that predominantly reacts with OGT but does not affect other functionally similar enzymes	266:392	We report the first targeted covalent inhibitor that predominantly reacts with OGT but does not affect other functionally similar enzymes.
31626249	2	9	theme	most	166:169	arg1	inhibitors					175:184	most OGT inhibitors	166:184	most OGT inhibitors	166:184	To date, most OGT inhibitors lack either sufficient potency or characterized specificity in cells.
31626249	1	10	theme	numerous	103:110	arg1	proteins					112:119	numerous proteins	103:119	numerous proteins	103:119	O-GlcNAc transferase (OGT) glycosylates numerous proteins and is implicated in many diseases.
31626249	0	11	theme	transferase	41:51	arg1	inhibition					18:27	covalent inhibition	9:27	covalent inhibition of O-GlcNAc transferase in cells	9:60	Targeted covalent inhibition of O-GlcNAc transferase in cells.
31626249	0	12	theme	O-GlcNAc	32:39	arg1	transferase					41:51	O-GlcNAc transferase	32:51	O-GlcNAc transferase in cells	32:60	Targeted covalent inhibition of O-GlcNAc transferase in cells.
31626249	4	13	theme	OGT	454:456	arg1	functions					458:466	cellular OGT functions	445:466	cellular OGT functions	445:466	This study provides a new strategy to interrogate cellular OGT functions and to investigate other glycosyltransferases.
31626249	4	14	theme	other	487:491	arg1	glycosyltransferases					493:512	other glycosyltransferases	487:512	other glycosyltransferases	487:512	This study provides a new strategy to interrogate cellular OGT functions and to investigate other glycosyltransferases.
31626249	4	15	theme	new	417:419	arg1	strategy					421:428	a new strategy	415:428	a new strategy to interrogate cellular OGT functions and to investigate other glycosyltransferases	415:512	This study provides a new strategy to interrogate cellular OGT functions and to investigate other glycosyltransferases.
31626249	2	16	theme	sufficient	198:207	arg1	potency					209:215	either sufficient potency	191:215	either sufficient potency	191:215	To date, most OGT inhibitors lack either sufficient potency or characterized specificity in cells.
31626249	3	17	theme	targeted	276:283	arg1	inhibitor					294:302	the first targeted covalent inhibitor	266:302	the first targeted covalent inhibitor that predominantly reacts with OGT but does not affect other functionally similar enzymes	266:392	We report the first targeted covalent inhibitor that predominantly reacts with OGT but does not affect other functionally similar enzymes.
31626249	3	18	theme	covalent	285:292	arg1	inhibitor					294:302	the first targeted covalent inhibitor	266:302	the first targeted covalent inhibitor that predominantly reacts with OGT but does not affect other functionally similar enzymes	266:392	We report the first targeted covalent inhibitor that predominantly reacts with OGT but does not affect other functionally similar enzymes.
31626249	1	19	theme	many	142:145	arg1	diseases					147:154	many diseases	142:154	many diseases	142:154	O-GlcNAc transferase (OGT) glycosylates numerous proteins and is implicated in many diseases.
31626249	4	20	dep	strategy	421:428	arg1	investigate					475:485	investigate	475:485	to investigate other glycosyltransferases	472:512	This study provides a new strategy to interrogate cellular OGT functions and to investigate other glycosyltransferases.
31626249	4	20	dep	strategy	421:428	arg1	interrogate					433:443	interrogate	433:443	to interrogate cellular OGT functions	430:466	This study provides a new strategy to interrogate cellular OGT functions and to investigate other glycosyltransferases.
31626249	2	21	theme	OGT	171:173	arg1	inhibitors					175:184	most OGT inhibitors	166:184	most OGT inhibitors	166:184	To date, most OGT inhibitors lack either sufficient potency or characterized specificity in cells.
31626249	0	22	theme	covalent	9:16	arg1	inhibition					18:27	covalent inhibition	9:27	covalent inhibition of O-GlcNAc transferase in cells	9:60	Targeted covalent inhibition of O-GlcNAc transferase in cells.
31753312	8	0	theme	peptides	1209:1216	arg1	effects					1172:1178	the effects	1168:1178	the effects of various O-GlcNAc modified peptides on wild-type α-synuclein aggregation	1168:1253	Here we discuss efforts to probe the effects of various O-GlcNAc modified peptides on wild-type α-synuclein aggregation.
31753312	1	1	theme	disease	170:176	arg1	protein					214:220	the Parkinson's disease (PD) associated α-synuclein (α-syn) protein	154:220	the Parkinson's disease (PD) associated α-synuclein (α-syn) protein	154:220	Numerous post-translational modifications (PTMs) of the Parkinson's disease (PD) associated α-synuclein (α-syn) protein have been recognised to play critical roles in disease aetiology.
31753312	8	2	theme	modified	1200:1207	arg1	peptides					1209:1216	various O-GlcNAc modified peptides	1183:1216	various O-GlcNAc modified peptides	1183:1216	Here we discuss efforts to probe the effects of various O-GlcNAc modified peptides on wild-type α-synuclein aggregation.
31753312	6	3	theme	substrates	954:963	arg1	thousands					932:940	thousands	932:940	thousands of acceptor substrates	932:963	However, targeting upstream cellular processes can lead to mechanism-based toxicity as the enzymes governing O-GlcNAc cycling modify thousands of acceptor substrates.
31753312	1	4	theme	critical	251:258	arg1	roles					260:264	critical roles	251:264	critical roles	251:264	Numerous post-translational modifications (PTMs) of the Parkinson's disease (PD) associated α-synuclein (α-syn) protein have been recognised to play critical roles in disease aetiology.
31753312	8	5	theme	wild-type	1221:1229	arg1	aggregation					1243:1253	wild-type α-synuclein aggregation	1221:1253	wild-type α-synuclein aggregation	1221:1253	Here we discuss efforts to probe the effects of various O-GlcNAc modified peptides on wild-type α-synuclein aggregation.
31753312	6	6	theme	acceptor	945:952	arg1	substrates					954:963	acceptor substrates	945:963	acceptor substrates	945:963	However, targeting upstream cellular processes can lead to mechanism-based toxicity as the enzymes governing O-GlcNAc cycling modify thousands of acceptor substrates.
31753312	7	7	theme	O-GlcNAc	1024:1031	arg1	effects					1013:1019	the protective effects	998:1019	the protective effects of O-GlcNAc	998:1031	Small glycopeptides that couple the protective effects of O-GlcNAc with the selectivity of recognition sequences may prove useful tools to modulate protein aggregation.
31753312	3	8	theme	protective	557:566	arg1	effects					568:574	protective effects	557:574	protective effects	557:574	Among the PTMs, enzymatic glycosylation with N-acetylglucosamine (GlcNAc) onto the protein's hydroxylated amino acid residues is reported to deliver protective effects against its pathogenic processing.
31753312	1	9	theme	Numerous	102:109	arg1	PTMs					145:148	PTMs	145:148	PTMs	145:148	Numerous post-translational modifications (PTMs) of the Parkinson's disease (PD) associated α-synuclein (α-syn) protein have been recognised to play critical roles in disease aetiology.
31753312	1	9	theme	Numerous	102:109	arg1	modifications					130:142	Numerous post-translational modifications	102:142	Numerous post-translational modifications (PTMs) of the Parkinson's disease (PD) associated α-synuclein (α-syn) protein	102:220	Numerous post-translational modifications (PTMs) of the Parkinson's disease (PD) associated α-synuclein (α-syn) protein have been recognised to play critical roles in disease aetiology.
31753312	0	10	from	effects	66:72	arg1	aggregation					89:99	α-synuclein aggregation	77:99	α-synuclein aggregation	77:99	O-GlcNAcylation of truncated NAC segment alters peptide-dependent effects on α-synuclein aggregation.
31753312	7	11	theme	protective	1002:1011	arg1	effects					1013:1019	the protective effects	998:1019	the protective effects of O-GlcNAc	998:1031	Small glycopeptides that couple the protective effects of O-GlcNAc with the selectivity of recognition sequences may prove useful tools to modulate protein aggregation.
31753312	3	12	theme	acid	520:523	arg1	residues					525:532	the protein's hydroxylated amino acid residues	487:532	the protein's hydroxylated amino acid residues	487:532	Among the PTMs, enzymatic glycosylation with N-acetylglucosamine (GlcNAc) onto the protein's hydroxylated amino acid residues is reported to deliver protective effects against its pathogenic processing.
31753312	6	13	theme	cellular	827:834	arg1	processes					836:844	targeting upstream cellular processes	808:844	targeting upstream cellular processes	808:844	However, targeting upstream cellular processes can lead to mechanism-based toxicity as the enzymes governing O-GlcNAc cycling modify thousands of acceptor substrates.
31753312	8	14	theme	α-synuclein	1231:1241	arg1	aggregation					1243:1253	wild-type α-synuclein aggregation	1221:1253	wild-type α-synuclein aggregation	1221:1253	Here we discuss efforts to probe the effects of various O-GlcNAc modified peptides on wild-type α-synuclein aggregation.
31753312	6	15	theme	targeting	808:816	arg1	processes					836:844	targeting upstream cellular processes	808:844	targeting upstream cellular processes	808:844	However, targeting upstream cellular processes can lead to mechanism-based toxicity as the enzymes governing O-GlcNAc cycling modify thousands of acceptor substrates.
31753312	6	16	theme	upstream	818:825	arg1	processes					836:844	targeting upstream cellular processes	808:844	targeting upstream cellular processes	808:844	However, targeting upstream cellular processes can lead to mechanism-based toxicity as the enzymes governing O-GlcNAc cycling modify thousands of acceptor substrates.
31753312	5	17	theme	PD	777:778	arg1	route					792:796	a PD therapeutic route	775:796	a PD therapeutic route	775:796	As such, manipulation of the protein's O-GlcNAcylation status has been proposed to offer a PD therapeutic route.
31753312	3	18	theme	pathogenic	588:597	arg1	processing					599:608	its pathogenic processing	584:608	its pathogenic processing	584:608	Among the PTMs, enzymatic glycosylation with N-acetylglucosamine (GlcNAc) onto the protein's hydroxylated amino acid residues is reported to deliver protective effects against its pathogenic processing.
31753312	1	19	theme	associated	183:192	arg1	protein					214:220	the Parkinson's disease (PD) associated α-synuclein (α-syn) protein	154:220	the Parkinson's disease (PD) associated α-synuclein (α-syn) protein	154:220	Numerous post-translational modifications (PTMs) of the Parkinson's disease (PD) associated α-synuclein (α-syn) protein have been recognised to play critical roles in disease aetiology.
31753312	1	20	theme	disease	269:275	arg1	aetiology					277:285	disease aetiology	269:285	disease aetiology	269:285	Numerous post-translational modifications (PTMs) of the Parkinson's disease (PD) associated α-synuclein (α-syn) protein have been recognised to play critical roles in disease aetiology.
31753312	1	21	theme	post-translational	111:128	arg1	PTMs					145:148	PTMs	145:148	PTMs	145:148	Numerous post-translational modifications (PTMs) of the Parkinson's disease (PD) associated α-synuclein (α-syn) protein have been recognised to play critical roles in disease aetiology.
31753312	1	21	theme	post-translational	111:128	arg1	modifications					130:142	Numerous post-translational modifications	102:142	Numerous post-translational modifications (PTMs) of the Parkinson's disease (PD) associated α-synuclein (α-syn) protein	102:220	Numerous post-translational modifications (PTMs) of the Parkinson's disease (PD) associated α-synuclein (α-syn) protein have been recognised to play critical roles in disease aetiology.
31753312	2	22	theme	disease	387:393	arg1	progression					395:405	disease progression	387:405	disease progression	387:405	Indeed, dysregulated phosphorylation and proteolysis are thought to modulate α-syn aggregation and disease progression.
31753312	0	23	theme	NAC	29:31	arg1	segment					33:39	truncated NAC segment	19:39	truncated NAC segment	19:39	O-GlcNAcylation of truncated NAC segment alters peptide-dependent effects on α-synuclein aggregation.
31753312	5	24	theme	O-GlcNAcylation	725:739	arg1	status					741:746	the protein's O-GlcNAcylation status	711:746	the protein's O-GlcNAcylation status	711:746	As such, manipulation of the protein's O-GlcNAcylation status has been proposed to offer a PD therapeutic route.
31753312	2	25	theme	dysregulated	296:307	arg1	phosphorylation					309:323	phosphorylation	309:323	phosphorylation	309:323	Indeed, dysregulated phosphorylation and proteolysis are thought to modulate α-syn aggregation and disease progression.
31753312	4	26	theme	pathogenic	660:669	arg1	self-assembly					671:683	its pathogenic self-assembly	656:683	its pathogenic self-assembly	656:683	This modification has been reported to alter its pathogenic self-assembly.
31753312	0	27	theme	truncated	19:27	arg1	segment					33:39	truncated NAC segment	19:39	truncated NAC segment	19:39	O-GlcNAcylation of truncated NAC segment alters peptide-dependent effects on α-synuclein aggregation.
31753312	5	28	theme	status	741:746	arg1	such					689:692	such	689:692	such	689:692	As such, manipulation of the protein's O-GlcNAcylation status has been proposed to offer a PD therapeutic route.
31753312	5	28	theme	status	741:746	arg1	manipulation					695:706	manipulation	695:706	manipulation of the protein's O-GlcNAcylation status	695:746	As such, manipulation of the protein's O-GlcNAcylation status has been proposed to offer a PD therapeutic route.
31753312	6	29	theme	O-GlcNAc	908:915	arg1	cycling					917:923	O-GlcNAc cycling	908:923	O-GlcNAc cycling	908:923	However, targeting upstream cellular processes can lead to mechanism-based toxicity as the enzymes governing O-GlcNAc cycling modify thousands of acceptor substrates.
31753312	1	30	theme	α-syn	207:211	arg1	protein					214:220	the Parkinson's disease (PD) associated α-synuclein (α-syn) protein	154:220	the Parkinson's disease (PD) associated α-synuclein (α-syn) protein	154:220	Numerous post-translational modifications (PTMs) of the Parkinson's disease (PD) associated α-synuclein (α-syn) protein have been recognised to play critical roles in disease aetiology.
31753312	7	31	theme	protein	1114:1120	arg1	aggregation					1122:1132	protein aggregation	1114:1132	protein aggregation	1114:1132	Small glycopeptides that couple the protective effects of O-GlcNAc with the selectivity of recognition sequences may prove useful tools to modulate protein aggregation.
31753312	1	32	theme	α-synuclein	194:204	arg1	protein					214:220	the Parkinson's disease (PD) associated α-synuclein (α-syn) protein	154:220	the Parkinson's disease (PD) associated α-synuclein (α-syn) protein	154:220	Numerous post-translational modifications (PTMs) of the Parkinson's disease (PD) associated α-synuclein (α-syn) protein have been recognised to play critical roles in disease aetiology.
31753312	0	33	theme	segment	33:39	arg1	O-GlcNAcylation					0:14	O-GlcNAcylation	0:14	O-GlcNAcylation of truncated NAC segment	0:39	O-GlcNAcylation of truncated NAC segment alters peptide-dependent effects on α-synuclein aggregation.
31753312	3	34	theme	enzymatic	424:432	arg1	glycosylation					434:446	enzymatic glycosylation	424:446	enzymatic glycosylation with N-acetylglucosamine (GlcNAc) onto the protein's hydroxylated amino acid residues	424:532	Among the PTMs, enzymatic glycosylation with N-acetylglucosamine (GlcNAc) onto the protein's hydroxylated amino acid residues is reported to deliver protective effects against its pathogenic processing.
31753312	8	35	from	effects	1172:1178	arg1	aggregation					1243:1253	wild-type α-synuclein aggregation	1221:1253	wild-type α-synuclein aggregation	1221:1253	Here we discuss efforts to probe the effects of various O-GlcNAc modified peptides on wild-type α-synuclein aggregation.
31753312	1	36	theme	protein	214:220	arg1	PTMs					145:148	PTMs	145:148	PTMs	145:148	Numerous post-translational modifications (PTMs) of the Parkinson's disease (PD) associated α-synuclein (α-syn) protein have been recognised to play critical roles in disease aetiology.
31753312	1	36	theme	protein	214:220	arg1	modifications					130:142	Numerous post-translational modifications	102:142	Numerous post-translational modifications (PTMs) of the Parkinson's disease (PD) associated α-synuclein (α-syn) protein	102:220	Numerous post-translational modifications (PTMs) of the Parkinson's disease (PD) associated α-synuclein (α-syn) protein have been recognised to play critical roles in disease aetiology.
31753312	3	37	with	glycosylation	434:446	arg1	N-acetylglucosamine					453:471	N-acetylglucosamine	453:471	N-acetylglucosamine (GlcNAc)	453:480	Among the PTMs, enzymatic glycosylation with N-acetylglucosamine (GlcNAc) onto the protein's hydroxylated amino acid residues is reported to deliver protective effects against its pathogenic processing.
31753312	3	37	with	glycosylation	434:446	arg1	GlcNAc					474:479	GlcNAc	474:479	GlcNAc	474:479	Among the PTMs, enzymatic glycosylation with N-acetylglucosamine (GlcNAc) onto the protein's hydroxylated amino acid residues is reported to deliver protective effects against its pathogenic processing.
31753312	8	38	theme	various	1183:1189	arg1	peptides					1209:1216	various O-GlcNAc modified peptides	1183:1216	various O-GlcNAc modified peptides	1183:1216	Here we discuss efforts to probe the effects of various O-GlcNAc modified peptides on wild-type α-synuclein aggregation.
31753312	3	39	theme	hydroxylated	501:512	arg1	residues					525:532	the protein's hydroxylated amino acid residues	487:532	the protein's hydroxylated amino acid residues	487:532	Among the PTMs, enzymatic glycosylation with N-acetylglucosamine (GlcNAc) onto the protein's hydroxylated amino acid residues is reported to deliver protective effects against its pathogenic processing.
31753312	0	40	theme	peptide-dependent	48:64	arg1	effects					66:72	peptide-dependent effects	48:72	peptide-dependent effects on α-synuclein aggregation	48:99	O-GlcNAcylation of truncated NAC segment alters peptide-dependent effects on α-synuclein aggregation.
31753312	7	41	theme	recognition	1057:1067	arg1	sequences					1069:1077	recognition sequences	1057:1077	recognition sequences	1057:1077	Small glycopeptides that couple the protective effects of O-GlcNAc with the selectivity of recognition sequences may prove useful tools to modulate protein aggregation.
31753312	3	42	theme	amino	514:518	arg1	residues					525:532	the protein's hydroxylated amino acid residues	487:532	the protein's hydroxylated amino acid residues	487:532	Among the PTMs, enzymatic glycosylation with N-acetylglucosamine (GlcNAc) onto the protein's hydroxylated amino acid residues is reported to deliver protective effects against its pathogenic processing.
31753312	7	43	theme	useful	1089:1094	arg1	tools					1096:1100	useful tools	1089:1100	useful tools	1089:1100	Small glycopeptides that couple the protective effects of O-GlcNAc with the selectivity of recognition sequences may prove useful tools to modulate protein aggregation.
31753312	7	44	theme	sequences	1069:1077	arg1	selectivity					1042:1052	the selectivity	1038:1052	the selectivity of recognition sequences	1038:1077	Small glycopeptides that couple the protective effects of O-GlcNAc with the selectivity of recognition sequences may prove useful tools to modulate protein aggregation.
31753312	7	45	theme	Small	966:970	arg1	glycopeptides					972:984	Small glycopeptides	966:984	Small glycopeptides that couple the protective effects of O-GlcNAc with the selectivity of recognition sequences	966:1077	Small glycopeptides that couple the protective effects of O-GlcNAc with the selectivity of recognition sequences may prove useful tools to modulate protein aggregation.
31753312	6	46	theme	mechanism-based	858:872	arg1	toxicity					874:881	mechanism-based toxicity	858:881	mechanism-based toxicity	858:881	However, targeting upstream cellular processes can lead to mechanism-based toxicity as the enzymes governing O-GlcNAc cycling modify thousands of acceptor substrates.
31753312	0	47	theme	α-synuclein	77:87	arg1	aggregation					89:99	α-synuclein aggregation	77:99	α-synuclein aggregation	77:99	O-GlcNAcylation of truncated NAC segment alters peptide-dependent effects on α-synuclein aggregation.
31753312	2	48	theme	α-syn	365:369	arg1	aggregation					371:381	α-syn aggregation	365:381	α-syn aggregation	365:381	Indeed, dysregulated phosphorylation and proteolysis are thought to modulate α-syn aggregation and disease progression.
31753312	5	49	theme	therapeutic	780:790	arg1	route					792:796	a PD therapeutic route	775:796	a PD therapeutic route	775:796	As such, manipulation of the protein's O-GlcNAcylation status has been proposed to offer a PD therapeutic route.
31753312	7	50	gly	glycopeptides	972:984	arg2	glycopeptides					972:984	Small glycopeptides	966:984	Small glycopeptides that couple the protective effects of O-GlcNAc with the selectivity of recognition sequences	966:1077	Small glycopeptides that couple the protective effects of O-GlcNAc with the selectivity of recognition sequences may prove useful tools to modulate protein aggregation.
28673834	9	0	from	progression/treatment	1287:1307	arg1	models					1342:1347	animal models	1335:1347	animal models	1335:1347	Our data warrant further studies on the role of O-GlcNAcylation in the progression/treatment of Parkinson's disease in animal models.
28673834	5	1	from	Ser87	801:805	arg1	O-GlcNAcylation					773:787	O-GlcNAcylation	773:787	O-GlcNAcylation at Thr72 or Ser87	773:805	O-GlcNAcylation at Thr72 or Ser87 suppresses the aggregation of α-synuclein.
28673834	5	2	theme	α-synuclein	837:847	arg1	aggregation					822:832	the aggregation	818:832	the aggregation of α-synuclein	818:847	O-GlcNAcylation at Thr72 or Ser87 suppresses the aggregation of α-synuclein.
28673834	1	3	theme	aberrant	262:269	arg1	aggregation					271:281	the aberrant aggregation	258:281	the aberrant aggregation	258:281	Neurodegenerative diseases including dementia with Lewy bodies, Lewy body variant of Alzheimer's disease, and Parkinson's disease are associated with the aberrant aggregation of α-synuclein, which is influenced by several post-translational modifications (PTMs).
28673834	9	4	theme	animal	1335:1340	arg1	models					1342:1347	animal models	1335:1347	animal models	1335:1347	Our data warrant further studies on the role of O-GlcNAcylation in the progression/treatment of Parkinson's disease in animal models.
28673834	8	5	theme	negative	1196:1203	arg1	oligomers					1205:1213	soluble SDS-resistant and Thioflavine T negative oligomers	1156:1213	soluble SDS-resistant and Thioflavine T negative oligomers	1156:1213	The O-GlcNAcylation inhibited α-synuclein aggregation and promoted the formation of soluble SDS-resistant and Thioflavine T negative oligomers.
28673834	5	6	from	Thr72	792:796	arg1	O-GlcNAcylation					773:787	O-GlcNAcylation	773:787	O-GlcNAcylation at Thr72 or Ser87	773:805	O-GlcNAcylation at Thr72 or Ser87 suppresses the aggregation of α-synuclein.
28673834	7	7	theme	O-GlcNAcylated	981:994	arg1	α-synuclein					996:1006	O-GlcNAcylated α-synuclein	981:1006	O-GlcNAcylated α-synuclein	981:1006	Here, we successfully generated O-GlcNAcylated α-synuclein by co-expressing a shorter form of OGT (sOGT) with α-synuclein.
28673834	1	8	theme	Neurodegenerative	108:124	arg1	diseases					126:133	Neurodegenerative diseases	108:133	Neurodegenerative diseases including dementia with Lewy bodies	108:169	Neurodegenerative diseases including dementia with Lewy bodies, Lewy body variant of Alzheimer's disease, and Parkinson's disease are associated with the aberrant aggregation of α-synuclein, which is influenced by several post-translational modifications (PTMs).
28673834	1	8	theme	Neurodegenerative	108:124	arg1	dementia					145:152	dementia	145:152	dementia	145:152	Neurodegenerative diseases including dementia with Lewy bodies, Lewy body variant of Alzheimer's disease, and Parkinson's disease are associated with the aberrant aggregation of α-synuclein, which is influenced by several post-translational modifications (PTMs).
28673834	1	9	theme	α-synuclein	286:296	arg1	aggregation					271:281	the aberrant aggregation	258:281	the aberrant aggregation	258:281	Neurodegenerative diseases including dementia with Lewy bodies, Lewy body variant of Alzheimer's disease, and Parkinson's disease are associated with the aberrant aggregation of α-synuclein, which is influenced by several post-translational modifications (PTMs).
28673834	6	10	theme	α-synuclein	902:912	arg1	O-GlcNAcylation					883:897	enzymatic O-GlcNAcylation	873:897	enzymatic O-GlcNAcylation of α-synuclein	873:912	However, the effect of enzymatic O-GlcNAcylation of α-synuclein at multiple residues is not clear.
28673834	9	11	theme	further	1233:1239	arg1	studies					1241:1247	further studies	1233:1247	further studies on the role of O-GlcNAcylation in the progression/treatment of Parkinson's disease in animal models	1233:1347	Our data warrant further studies on the role of O-GlcNAcylation in the progression/treatment of Parkinson's disease in animal models.
28673834	2	12	theme	important	410:418	arg1	role					420:423	an important role	407:423	an important role	407:423	O-GlcNAcylation is one PTM that has an important role in many fundamental processes.
28673834	7	13	with	OGT	1043:1045	arg1	α-synuclein					1059:1069	α-synuclein	1059:1069	α-synuclein	1059:1069	Here, we successfully generated O-GlcNAcylated α-synuclein by co-expressing a shorter form of OGT (sOGT) with α-synuclein.
28673834	3	14	from	residues	505:512	arg1	O-GlcNAcylation					460:474	The O-GlcNAcylation	456:474	The O-GlcNAcylation of endogenous α-synuclein at residues 53, 64, 72 and 87	456:530	The O-GlcNAcylation of endogenous α-synuclein at residues 53, 64, 72 and 87 has been reported in an unbiased mass spectrum analysis.
28673834	0	15	theme	Enzymatic	0:8	arg1	O-GlcNAcylation					10:24	Enzymatic O-GlcNAcylation	0:24	Enzymatic O-GlcNAcylation of α-synuclein	0:39	Enzymatic O-GlcNAcylation of α-synuclein reduces aggregation and increases SDS-resistant soluble oligomers.
28673834	6	16	from	residues	926:933	arg1	effect					863:868	the effect	859:868	the effect of enzymatic O-GlcNAcylation of α-synuclein at multiple residues	859:933	However, the effect of enzymatic O-GlcNAcylation of α-synuclein at multiple residues is not clear.
28673834	6	16	from	residues	926:933	arg1	clear					942:946	clear	942:946	clear	942:946	However, the effect of enzymatic O-GlcNAcylation of α-synuclein at multiple residues is not clear.
28673834	6	17	theme	O-GlcNAcylation	883:897	arg1	effect					863:868	the effect	859:868	the effect of enzymatic O-GlcNAcylation of α-synuclein at multiple residues	859:933	However, the effect of enzymatic O-GlcNAcylation of α-synuclein at multiple residues is not clear.
28673834	6	17	theme	O-GlcNAcylation	883:897	arg1	clear					942:946	clear	942:946	clear	942:946	However, the effect of enzymatic O-GlcNAcylation of α-synuclein at multiple residues is not clear.
28673834	4	18	from	residues	628:635	arg1	consequences					593:604	The consequences	589:604	The consequences of O-GlcNAcylation at residues 72 or 87	589:644	The consequences of O-GlcNAcylation at residues 72 or 87 have been studied by using a synthetic α-synuclein bearing O-GlcNAcylation at threonine residue 72 or serine 87, respectively.
28673834	3	19	theme	mass	565:568	arg1	analysis					579:586	an unbiased mass spectrum analysis	553:586	an unbiased mass spectrum analysis	553:586	The O-GlcNAcylation of endogenous α-synuclein at residues 53, 64, 72 and 87 has been reported in an unbiased mass spectrum analysis.
28673834	1	20	with	dementia	145:152	arg1	bodies					164:169	Lewy bodies	159:169	Lewy bodies	159:169	Neurodegenerative diseases including dementia with Lewy bodies, Lewy body variant of Alzheimer's disease, and Parkinson's disease are associated with the aberrant aggregation of α-synuclein, which is influenced by several post-translational modifications (PTMs).
28673834	3	21	theme	spectrum	570:577	arg1	analysis					579:586	an unbiased mass spectrum analysis	553:586	an unbiased mass spectrum analysis	553:586	The O-GlcNAcylation of endogenous α-synuclein at residues 53, 64, 72 and 87 has been reported in an unbiased mass spectrum analysis.
28673834	9	22	theme	O-GlcNAcylation	1264:1278	arg1	role					1256:1259	the role	1252:1259	the role of O-GlcNAcylation in the progression/treatment of Parkinson's disease in animal models	1252:1347	Our data warrant further studies on the role of O-GlcNAcylation in the progression/treatment of Parkinson's disease in animal models.
28673834	0	23	theme	α-synuclein	29:39	arg1	O-GlcNAcylation					10:24	Enzymatic O-GlcNAcylation	0:24	Enzymatic O-GlcNAcylation of α-synuclein	0:39	Enzymatic O-GlcNAcylation of α-synuclein reduces aggregation and increases SDS-resistant soluble oligomers.
28673834	8	24	theme	oligomers	1205:1213	arg1	formation					1143:1151	the formation	1139:1151	the formation of soluble SDS-resistant and Thioflavine T negative oligomers	1139:1213	The O-GlcNAcylation inhibited α-synuclein aggregation and promoted the formation of soluble SDS-resistant and Thioflavine T negative oligomers.
28673834	8	25	theme	α-synuclein	1102:1112	arg1	aggregation					1114:1124	α-synuclein aggregation	1102:1124	α-synuclein aggregation	1102:1124	The O-GlcNAcylation inhibited α-synuclein aggregation and promoted the formation of soluble SDS-resistant and Thioflavine T negative oligomers.
28673834	4	26	from	87	643:644	arg1	consequences					593:604	The consequences	589:604	The consequences of O-GlcNAcylation at residues 72 or 87	589:644	The consequences of O-GlcNAcylation at residues 72 or 87 have been studied by using a synthetic α-synuclein bearing O-GlcNAcylation at threonine residue 72 or serine 87, respectively.
28673834	3	27	theme	α-synuclein	490:500	arg1	O-GlcNAcylation					460:474	The O-GlcNAcylation	456:474	The O-GlcNAcylation of endogenous α-synuclein at residues 53, 64, 72 and 87	456:530	The O-GlcNAcylation of endogenous α-synuclein at residues 53, 64, 72 and 87 has been reported in an unbiased mass spectrum analysis.
28673834	8	28	theme	SDS-resistant	1164:1176	arg1	oligomers					1205:1213	soluble SDS-resistant and Thioflavine T negative oligomers	1156:1213	soluble SDS-resistant and Thioflavine T negative oligomers	1156:1213	The O-GlcNAcylation inhibited α-synuclein aggregation and promoted the formation of soluble SDS-resistant and Thioflavine T negative oligomers.
28673834	6	29	theme	enzymatic	873:881	arg1	O-GlcNAcylation					883:897	enzymatic O-GlcNAcylation	873:897	enzymatic O-GlcNAcylation of α-synuclein	873:912	However, the effect of enzymatic O-GlcNAcylation of α-synuclein at multiple residues is not clear.
28673834	3	30	theme	unbiased	556:563	arg1	analysis					579:586	an unbiased mass spectrum analysis	553:586	an unbiased mass spectrum analysis	553:586	The O-GlcNAcylation of endogenous α-synuclein at residues 53, 64, 72 and 87 has been reported in an unbiased mass spectrum analysis.
28673834	2	31	theme	many	428:431	arg1	processes					445:453	many fundamental processes	428:453	many fundamental processes	428:453	O-GlcNAcylation is one PTM that has an important role in many fundamental processes.
28673834	9	32	from	role	1256:1259	arg1	progression/treatment					1287:1307	the progression/treatment	1283:1307	the progression/treatment of Parkinson's disease in animal models	1283:1347	Our data warrant further studies on the role of O-GlcNAcylation in the progression/treatment of Parkinson's disease in animal models.
28673834	2	33	contain	has	403:405	arg2	role					420:423	an important role	407:423	an important role	407:423	O-GlcNAcylation is one PTM that has an important role in many fundamental processes.
28673834	2	33	contain	has	403:405	arg1	PTM					394:396	one PTM	390:396	one PTM that has an important role in many fundamental processes	390:453	O-GlcNAcylation is one PTM that has an important role in many fundamental processes.
28673834	4	34	theme	synthetic	675:683	arg1	α-synuclein					685:695	a synthetic α-synuclein	673:695	a synthetic α-synuclein bearing O-GlcNAcylation at threonine residue 72 or serine 87	673:756	The consequences of O-GlcNAcylation at residues 72 or 87 have been studied by using a synthetic α-synuclein bearing O-GlcNAcylation at threonine residue 72 or serine 87, respectively.
28673834	9	35	from	models	1342:1347	arg1	progression/treatment					1287:1307	the progression/treatment	1283:1307	the progression/treatment of Parkinson's disease in animal models	1283:1347	Our data warrant further studies on the role of O-GlcNAcylation in the progression/treatment of Parkinson's disease in animal models.
28673834	3	36	theme	endogenous	479:488	arg1	α-synuclein					490:500	endogenous α-synuclein	479:500	endogenous α-synuclein	479:500	The O-GlcNAcylation of endogenous α-synuclein at residues 53, 64, 72 and 87 has been reported in an unbiased mass spectrum analysis.
28673834	9	37	from	disease	1324:1330	arg1	models					1342:1347	animal models	1335:1347	animal models	1335:1347	Our data warrant further studies on the role of O-GlcNAcylation in the progression/treatment of Parkinson's disease in animal models.
28673834	1	38	theme	several	322:328	arg1	PTMs					364:367	PTMs	364:367	PTMs	364:367	Neurodegenerative diseases including dementia with Lewy bodies, Lewy body variant of Alzheimer's disease, and Parkinson's disease are associated with the aberrant aggregation of α-synuclein, which is influenced by several post-translational modifications (PTMs).
28673834	1	38	theme	several	322:328	arg1	modifications					349:361	several post-translational modifications	322:361	several post-translational modifications (PTMs)	322:368	Neurodegenerative diseases including dementia with Lewy bodies, Lewy body variant of Alzheimer's disease, and Parkinson's disease are associated with the aberrant aggregation of α-synuclein, which is influenced by several post-translational modifications (PTMs).
28673834	8	39	theme	soluble	1156:1162	arg1	oligomers					1205:1213	soluble SDS-resistant and Thioflavine T negative oligomers	1156:1213	soluble SDS-resistant and Thioflavine T negative oligomers	1156:1213	The O-GlcNAcylation inhibited α-synuclein aggregation and promoted the formation of soluble SDS-resistant and Thioflavine T negative oligomers.
28673834	7	40	theme	OGT	1043:1045	arg1	form					1035:1038	a shorter form	1025:1038	a shorter form of OGT (sOGT) with α-synuclein	1025:1069	Here, we successfully generated O-GlcNAcylated α-synuclein by co-expressing a shorter form of OGT (sOGT) with α-synuclein.
28673834	6	41	theme	multiple	917:924	arg1	residues					926:933	multiple residues	917:933	multiple residues	917:933	However, the effect of enzymatic O-GlcNAcylation of α-synuclein at multiple residues is not clear.
28673834	1	42	theme	post-translational	330:347	arg1	PTMs					364:367	PTMs	364:367	PTMs	364:367	Neurodegenerative diseases including dementia with Lewy bodies, Lewy body variant of Alzheimer's disease, and Parkinson's disease are associated with the aberrant aggregation of α-synuclein, which is influenced by several post-translational modifications (PTMs).
28673834	1	42	theme	post-translational	330:347	arg1	modifications					349:361	several post-translational modifications	322:361	several post-translational modifications (PTMs)	322:368	Neurodegenerative diseases including dementia with Lewy bodies, Lewy body variant of Alzheimer's disease, and Parkinson's disease are associated with the aberrant aggregation of α-synuclein, which is influenced by several post-translational modifications (PTMs).
28673834	7	43	theme	shorter	1027:1033	arg1	form					1035:1038	a shorter form	1025:1038	a shorter form of OGT (sOGT) with α-synuclein	1025:1069	Here, we successfully generated O-GlcNAcylated α-synuclein by co-expressing a shorter form of OGT (sOGT) with α-synuclein.
28673834	1	44	theme	Lewy	159:162	arg1	bodies					164:169	Lewy bodies	159:169	Lewy bodies	159:169	Neurodegenerative diseases including dementia with Lewy bodies, Lewy body variant of Alzheimer's disease, and Parkinson's disease are associated with the aberrant aggregation of α-synuclein, which is influenced by several post-translational modifications (PTMs).
28673834	3	45	gly	O-GlcNAcylation	460:474	arg1	analysis					579:586	an unbiased mass spectrum analysis	553:586	an unbiased mass spectrum analysis	553:586	The O-GlcNAcylation of endogenous α-synuclein at residues 53, 64, 72 and 87 has been reported in an unbiased mass spectrum analysis.
28673834	4	46	theme	residue	734:740	arg1	threonine					724:732	threonine residue 72	724:743	threonine residue 72	724:743	The consequences of O-GlcNAcylation at residues 72 or 87 have been studied by using a synthetic α-synuclein bearing O-GlcNAcylation at threonine residue 72 or serine 87, respectively.
28673834	4	47	theme	O-GlcNAcylation	609:623	arg1	consequences					593:604	The consequences	589:604	The consequences of O-GlcNAcylation at residues 72 or 87	589:644	The consequences of O-GlcNAcylation at residues 72 or 87 have been studied by using a synthetic α-synuclein bearing O-GlcNAcylation at threonine residue 72 or serine 87, respectively.
28673834	9	48	from	studies	1241:1247	arg1	role					1256:1259	the role	1252:1259	the role of O-GlcNAcylation in the progression/treatment of Parkinson's disease in animal models	1252:1347	Our data warrant further studies on the role of O-GlcNAcylation in the progression/treatment of Parkinson's disease in animal models.
28673834	0	49	theme	soluble	89:95	arg1	oligomers					97:105	SDS-resistant soluble oligomers	75:105	SDS-resistant soluble oligomers	75:105	Enzymatic O-GlcNAcylation of α-synuclein reduces aggregation and increases SDS-resistant soluble oligomers.
28673834	2	50	theme	fundamental	433:443	arg1	processes					445:453	many fundamental processes	428:453	many fundamental processes	428:453	O-GlcNAcylation is one PTM that has an important role in many fundamental processes.
28673834	1	51	theme	Lewy	172:175	arg1	variant					182:188	Lewy body variant	172:188	Lewy body variant of Alzheimer's disease	172:211	Neurodegenerative diseases including dementia with Lewy bodies, Lewy body variant of Alzheimer's disease, and Parkinson's disease are associated with the aberrant aggregation of α-synuclein, which is influenced by several post-translational modifications (PTMs).
28673834	0	52	theme	SDS-resistant	75:87	arg1	oligomers					97:105	SDS-resistant soluble oligomers	75:105	SDS-resistant soluble oligomers	75:105	Enzymatic O-GlcNAcylation of α-synuclein reduces aggregation and increases SDS-resistant soluble oligomers.
28673834	9	53	theme	disease	1324:1330	arg1	progression/treatment					1287:1307	the progression/treatment	1283:1307	the progression/treatment of Parkinson's disease in animal models	1283:1347	Our data warrant further studies on the role of O-GlcNAcylation in the progression/treatment of Parkinson's disease in animal models.
28673834	1	54	theme	body	177:180	arg1	variant					182:188	Lewy body variant	172:188	Lewy body variant of Alzheimer's disease	172:211	Neurodegenerative diseases including dementia with Lewy bodies, Lewy body variant of Alzheimer's disease, and Parkinson's disease are associated with the aberrant aggregation of α-synuclein, which is influenced by several post-translational modifications (PTMs).
30679801	11	0	theme	IDO	1513:1515	arg1	upregulation					1517:1528	IDO upregulation	1513:1528	STAT1 activity together with IDO upregulation	1484:1528	Inhibiting the responsible O-acetylglucosamine (O-GlcNAc) transferase abolishes STAT1 activity together with IDO upregulation.
30679801	10	1	theme	/signal	1212:1218	arg1	transducer					1220:1229	the Janus kinase (JAK)/signal transducer	1190:1229	the Janus kinase (JAK)/signal transducer	1190:1229	We identified the Janus kinase (JAK)/signal transducer and activator of transcription (STAT)1 pathway as a regulator of both glycolysis and IDO, and show that enhanced glucose turnover is linked to abundant STAT1 glycosylation.
30679801	10	1	theme	/signal	1212:1218	arg1	STAT					1263:1266	STAT	1263:1266	STAT	1263:1266	We identified the Janus kinase (JAK)/signal transducer and activator of transcription (STAT)1 pathway as a regulator of both glycolysis and IDO, and show that enhanced glucose turnover is linked to abundant STAT1 glycosylation.
30679801	6	2	theme	both	694:697	arg1	capable					683:689	capable	683:689	capable	683:689	MSCs are capable of both, high levels of glycolysis and of oxidative phosphorylation.
30679801	0	3	theme	STAT1	92:96	arg1	glycosylation					98:110	STAT1 glycosylation	92:110	STAT1 glycosylation	92:110	Inflammation-induced glycolytic switch controls suppressivity of mesenchymal stem cells via STAT1 glycosylation.
30679801	11	4	theme	STAT1	1484:1488	arg1	activity					1490:1497	STAT1 activity	1484:1497	STAT1 activity together with IDO upregulation	1484:1528	Inhibiting the responsible O-acetylglucosamine (O-GlcNAc) transferase abolishes STAT1 activity together with IDO upregulation.
30679801	1	5	theme	tissue	173:178	arg1	homeostasis					180:190	tissue homeostasis	173:190	tissue homeostasis	173:190	Mesenchymal stem cells (MSCs) represent key contributors to tissue homeostasis and promising therapeutics for hyperinflammatory conditions including graft-versus-host disease.
30679801	8	6	theme	inflammatory	962:973	arg1	MSC-licensing					975:987	inflammatory MSC-licensing	962:987	inflammatory MSC-licensing	962:987	We demonstrate that inflammatory MSC-licensing causes metabolic shifts including enhanced glycolysis and increased fatty acid oxidation.
30679801	12	7	theme	downstream	1635:1644	arg1	effects					1646:1652	downstream effects	1635:1652	downstream effects	1635:1652	Our data suggest that STAT1-O-GlcNAcylation increases its stability towards degradation thus sustaining downstream effects.
30679801	10	8	theme	IDO	1316:1318	arg1	pathway					1270:1276	the Janus kinase (JAK)/signal transducer and activator of transcription (STAT)1 pathway	1190:1276	the Janus kinase (JAK)/signal transducer and activator of transcription (STAT)1 pathway	1190:1276	We identified the Janus kinase (JAK)/signal transducer and activator of transcription (STAT)1 pathway as a regulator of both glycolysis and IDO, and show that enhanced glucose turnover is linked to abundant STAT1 glycosylation.
30679801	10	8	theme	IDO	1316:1318	arg1	regulator					1283:1291	a regulator	1281:1291	a regulator of both glycolysis and IDO	1281:1318	We identified the Janus kinase (JAK)/signal transducer and activator of transcription (STAT)1 pathway as a regulator of both glycolysis and IDO, and show that enhanced glucose turnover is linked to abundant STAT1 glycosylation.
30679801	3	9	theme	MSC-	434:437	arg1	"					448:448	MSC-"licensing"	434:448	MSC-"licensing"	434:448	The MSCs' functional response towards inflammatory cues is known as MSC-"licensing" and includes indoleamine 2,3-dioxygenase (IDO) upregulation.
30679801	3	9	theme	MSC-	434:437	arg1	response					387:394	The MSCs' functional response	366:394	The MSCs' functional response towards inflammatory cues	366:420	The MSCs' functional response towards inflammatory cues is known as MSC-"licensing" and includes indoleamine 2,3-dioxygenase (IDO) upregulation.
30679801	10	10	theme	transcription	1248:1260	arg1	activator					1235:1243	activator	1235:1243	activator	1235:1243	We identified the Janus kinase (JAK)/signal transducer and activator of transcription (STAT)1 pathway as a regulator of both glycolysis and IDO, and show that enhanced glucose turnover is linked to abundant STAT1 glycosylation.
30679801	10	10	theme	transcription	1248:1260	arg1	transducer					1220:1229	the Janus kinase (JAK)/signal transducer	1190:1229	the Janus kinase (JAK)/signal transducer	1190:1229	We identified the Janus kinase (JAK)/signal transducer and activator of transcription (STAT)1 pathway as a regulator of both glycolysis and IDO, and show that enhanced glucose turnover is linked to abundant STAT1 glycosylation.
30679801	10	10	theme	transcription	1248:1260	arg1	STAT					1263:1266	STAT	1263:1266	STAT	1263:1266	We identified the Janus kinase (JAK)/signal transducer and activator of transcription (STAT)1 pathway as a regulator of both glycolysis and IDO, and show that enhanced glucose turnover is linked to abundant STAT1 glycosylation.
30679801	8	11	theme	increased	1047:1055	arg1	oxidation					1068:1076	increased fatty acid oxidation	1047:1076	increased fatty acid oxidation	1047:1076	We demonstrate that inflammatory MSC-licensing causes metabolic shifts including enhanced glycolysis and increased fatty acid oxidation.
30679801	5	12	theme	Increasing	566:575	arg1	evidence					577:584	Increasing evidence	566:584	Increasing evidence	566:584	Increasing evidence suggests that several functions are (co-)determined by the cells' metabolic commitment.
30679801	10	13	theme	STAT1	1383:1387	arg1	glycosylation					1389:1401	abundant STAT1 glycosylation	1374:1401	abundant STAT1 glycosylation	1374:1401	We identified the Janus kinase (JAK)/signal transducer and activator of transcription (STAT)1 pathway as a regulator of both glycolysis and IDO, and show that enhanced glucose turnover is linked to abundant STAT1 glycosylation.
30679801	5	14	dep	determined	627:636	arg1	co-					623:625	co-	623:625	co-	623:625	Increasing evidence suggests that several functions are (co-)determined by the cells' metabolic commitment.
30679801	11	15	theme	O-acetylglucosamine	1431:1449	arg1	transferase					1462:1472	the responsible O-acetylglucosamine (O-GlcNAc) transferase	1415:1472	the responsible O-acetylglucosamine (O-GlcNAc) transferase	1415:1472	Inhibiting the responsible O-acetylglucosamine (O-GlcNAc) transferase abolishes STAT1 activity together with IDO upregulation.
30679801	2	16	theme	microenvironmental	338:355	arg1	signals					357:363	microenvironmental signals	338:363	microenvironmental signals	338:363	Their immunomodulatory effects are controlled by microenvironmental signals.
30679801	0	17	theme	mesenchymal	65:75	arg1	cells					82:86	mesenchymal stem cells	65:86	mesenchymal stem cells	65:86	Inflammation-induced glycolytic switch controls suppressivity of mesenchymal stem cells via STAT1 glycosylation.
30679801	10	18	theme	activator	1235:1243	arg1	pathway					1270:1276	the Janus kinase (JAK)/signal transducer and activator of transcription (STAT)1 pathway	1190:1276	the Janus kinase (JAK)/signal transducer and activator of transcription (STAT)1 pathway	1190:1276	We identified the Janus kinase (JAK)/signal transducer and activator of transcription (STAT)1 pathway as a regulator of both glycolysis and IDO, and show that enhanced glucose turnover is linked to abundant STAT1 glycosylation.
30679801	10	18	theme	activator	1235:1243	arg1	regulator					1283:1291	a regulator	1281:1291	a regulator of both glycolysis and IDO	1281:1318	We identified the Janus kinase (JAK)/signal transducer and activator of transcription (STAT)1 pathway as a regulator of both glycolysis and IDO, and show that enhanced glucose turnover is linked to abundant STAT1 glycosylation.
30679801	9	19	theme	IDO	1125:1127	arg1	upregulation					1129:1140	IDO upregulation	1125:1140	IDO upregulation	1125:1140	Yet, only interfering with glycolysis impacts IDO upregulation and impedes T-cell-suppressivity.
30679801	10	20	theme	glycolysis	1301:1310	arg1	pathway					1270:1276	the Janus kinase (JAK)/signal transducer and activator of transcription (STAT)1 pathway	1190:1276	the Janus kinase (JAK)/signal transducer and activator of transcription (STAT)1 pathway	1190:1276	We identified the Janus kinase (JAK)/signal transducer and activator of transcription (STAT)1 pathway as a regulator of both glycolysis and IDO, and show that enhanced glucose turnover is linked to abundant STAT1 glycosylation.
30679801	10	20	theme	glycolysis	1301:1310	arg1	regulator					1283:1291	a regulator	1281:1291	a regulator of both glycolysis and IDO	1281:1318	We identified the Janus kinase (JAK)/signal transducer and activator of transcription (STAT)1 pathway as a regulator of both glycolysis and IDO, and show that enhanced glucose turnover is linked to abundant STAT1 glycosylation.
30679801	0	21	theme	glycolytic	21:30	arg1	switch					32:37	Inflammation-induced glycolytic switch	0:37	Inflammation-induced glycolytic switch	0:37	Inflammation-induced glycolytic switch controls suppressivity of mesenchymal stem cells via STAT1 glycosylation.
30679801	11	22	dep	together	1499:1506	arg1	with					1508:1511	with	1508:1511	with	1508:1511	Inhibiting the responsible O-acetylglucosamine (O-GlcNAc) transferase abolishes STAT1 activity together with IDO upregulation.
30679801	13	23	theme	immunoregulatory	1739:1754	arg1	potency					1756:1762	the MSCs' immunoregulatory potency	1729:1762	the MSCs' immunoregulatory potency	1729:1762	This pathway could represent a target for interventions aiming to enhance the MSCs' immunoregulatory potency.
30679801	8	24	theme	metabolic	996:1004	arg1	oxidation					1068:1076	increased fatty acid oxidation	1047:1076	increased fatty acid oxidation	1047:1076	We demonstrate that inflammatory MSC-licensing causes metabolic shifts including enhanced glycolysis and increased fatty acid oxidation.
30679801	8	24	theme	metabolic	996:1004	arg1	shifts					1006:1011	metabolic shifts	996:1011	metabolic shifts including enhanced glycolysis and increased fatty acid oxidation	996:1076	We demonstrate that inflammatory MSC-licensing causes metabolic shifts including enhanced glycolysis and increased fatty acid oxidation.
30679801	8	24	theme	metabolic	996:1004	arg1	glycolysis					1032:1041	enhanced glycolysis	1023:1041	enhanced glycolysis	1023:1041	We demonstrate that inflammatory MSC-licensing causes metabolic shifts including enhanced glycolysis and increased fatty acid oxidation.
30679801	1	25	theme	promising	196:204	arg1	therapeutics					206:217	promising therapeutics	196:217	promising therapeutics for hyperinflammatory conditions including graft-versus-host disease	196:286	Mesenchymal stem cells (MSCs) represent key contributors to tissue homeostasis and promising therapeutics for hyperinflammatory conditions including graft-versus-host disease.
30679801	0	26	theme	Inflammation-induced	0:19	arg1	switch					32:37	Inflammation-induced glycolytic switch	0:37	Inflammation-induced glycolytic switch	0:37	Inflammation-induced glycolytic switch controls suppressivity of mesenchymal stem cells via STAT1 glycosylation.
30679801	11	27	theme	responsible	1419:1429	arg1	O-GlcNAc					1452:1459	O-GlcNAc	1452:1459	O-GlcNAc	1452:1459	Inhibiting the responsible O-acetylglucosamine (O-GlcNAc) transferase abolishes STAT1 activity together with IDO upregulation.
30679801	11	27	theme	responsible	1419:1429	arg1	O-acetylglucosamine					1431:1449	the responsible O-acetylglucosamine	1415:1449	the responsible O-acetylglucosamine (O-GlcNAc) transferase	1415:1472	Inhibiting the responsible O-acetylglucosamine (O-GlcNAc) transferase abolishes STAT1 activity together with IDO upregulation.
30679801	1	28	theme	Mesenchymal	113:123	arg1	MSCs					137:140	MSCs	137:140	MSCs	137:140	Mesenchymal stem cells (MSCs) represent key contributors to tissue homeostasis and promising therapeutics for hyperinflammatory conditions including graft-versus-host disease.
30679801	1	28	theme	Mesenchymal	113:123	arg1	cells					130:134	Mesenchymal stem cells	113:134	Mesenchymal stem cells (MSCs)	113:141	Mesenchymal stem cells (MSCs) represent key contributors to tissue homeostasis and promising therapeutics for hyperinflammatory conditions including graft-versus-host disease.
30679801	6	29	theme	phosphorylation	743:757	arg1	levels					705:710	high levels	700:710	high levels of glycolysis and of oxidative phosphorylation	700:757	MSCs are capable of both, high levels of glycolysis and of oxidative phosphorylation.
30679801	6	29	theme	phosphorylation	743:757	arg1	MSCs					674:677	MSCs	674:677	MSCs	674:677	MSCs are capable of both, high levels of glycolysis and of oxidative phosphorylation.
30679801	5	30	theme	metabolic	652:660	arg1	commitment					662:671	the cells' metabolic commitment	641:671	the cells' metabolic commitment	641:671	Increasing evidence suggests that several functions are (co-)determined by the cells' metabolic commitment.
30679801	1	31	theme	stem	125:128	arg1	MSCs					137:140	MSCs	137:140	MSCs	137:140	Mesenchymal stem cells (MSCs) represent key contributors to tissue homeostasis and promising therapeutics for hyperinflammatory conditions including graft-versus-host disease.
30679801	1	31	theme	stem	125:128	arg1	cells					130:134	Mesenchymal stem cells	113:134	Mesenchymal stem cells (MSCs)	113:141	Mesenchymal stem cells (MSCs) represent key contributors to tissue homeostasis and promising therapeutics for hyperinflammatory conditions including graft-versus-host disease.
30679801	6	32	theme	oxidative	733:741	arg1	phosphorylation					743:757	oxidative phosphorylation	733:757	oxidative phosphorylation	733:757	MSCs are capable of both, high levels of glycolysis and of oxidative phosphorylation.
30679801	3	33	theme	licensing	439:447	arg1	"					448:448	MSC-"licensing"	434:448	MSC-"licensing"	434:448	The MSCs' functional response towards inflammatory cues is known as MSC-"licensing" and includes indoleamine 2,3-dioxygenase (IDO) upregulation.
30679801	3	33	theme	licensing	439:447	arg1	response					387:394	The MSCs' functional response	366:394	The MSCs' functional response towards inflammatory cues	366:420	The MSCs' functional response towards inflammatory cues is known as MSC-"licensing" and includes indoleamine 2,3-dioxygenase (IDO) upregulation.
30679801	7	34	theme	metabolic	880:888	arg1	mechanisms					890:899	metabolic mechanisms	880:899	metabolic mechanisms controlling this process	880:924	Although several studies have addressed alterations of the immune regulatory phenotype elicited by inflammatory priming metabolic mechanisms controlling this process remain unknown.
30679801	7	35	theme	several	769:775	arg1	studies					777:783	several studies	769:783	several studies	769:783	Although several studies have addressed alterations of the immune regulatory phenotype elicited by inflammatory priming metabolic mechanisms controlling this process remain unknown.
30679801	1	36	theme	hyperinflammatory	223:239	arg1	conditions					241:250	hyperinflammatory conditions	223:250	hyperinflammatory conditions including graft-versus-host disease	223:286	Mesenchymal stem cells (MSCs) represent key contributors to tissue homeostasis and promising therapeutics for hyperinflammatory conditions including graft-versus-host disease.
30679801	1	36	theme	hyperinflammatory	223:239	arg1	disease					280:286	graft-versus-host disease	262:286	graft-versus-host disease	262:286	Mesenchymal stem cells (MSCs) represent key contributors to tissue homeostasis and promising therapeutics for hyperinflammatory conditions including graft-versus-host disease.
30679801	3	37	theme	2,3-dioxygenase	475:489	arg1	upregulation					497:508	indoleamine 2,3-dioxygenase (IDO) upregulation	463:508	indoleamine 2,3-dioxygenase (IDO) upregulation	463:508	The MSCs' functional response towards inflammatory cues is known as MSC-"licensing" and includes indoleamine 2,3-dioxygenase (IDO) upregulation.
30679801	7	38	theme	inflammatory	859:870	arg1	priming					872:878	inflammatory priming	859:878	inflammatory priming	859:878	Although several studies have addressed alterations of the immune regulatory phenotype elicited by inflammatory priming metabolic mechanisms controlling this process remain unknown.
30679801	8	39	theme	fatty	1057:1061	arg1	oxidation					1068:1076	increased fatty acid oxidation	1047:1076	increased fatty acid oxidation	1047:1076	We demonstrate that inflammatory MSC-licensing causes metabolic shifts including enhanced glycolysis and increased fatty acid oxidation.
30679801	0	40	theme	stem	77:80	arg1	cells					82:86	mesenchymal stem cells	65:86	mesenchymal stem cells	65:86	Inflammation-induced glycolytic switch controls suppressivity of mesenchymal stem cells via STAT1 glycosylation.
30679801	4	41	theme	tryptophan-depleting	520:539	arg1	IDO					541:543	tryptophan-depleting IDO	520:543	tryptophan-depleting IDO	520:543	MSCs use tryptophan-depleting IDO to suppress T-cells.
30679801	6	42	dep	capable	683:689	arg1	levels					705:710	high levels	700:710	high levels of glycolysis and of oxidative phosphorylation	700:757	MSCs are capable of both, high levels of glycolysis and of oxidative phosphorylation.
30679801	6	42	dep	capable	683:689	arg1	MSCs					674:677	MSCs	674:677	MSCs	674:677	MSCs are capable of both, high levels of glycolysis and of oxidative phosphorylation.
30679801	3	43	theme	indoleamine	463:473	arg1	IDO					492:494	IDO	492:494	IDO	492:494	The MSCs' functional response towards inflammatory cues is known as MSC-"licensing" and includes indoleamine 2,3-dioxygenase (IDO) upregulation.
30679801	3	43	theme	indoleamine	463:473	arg1	2,3-dioxygenase					475:489	indoleamine 2,3-dioxygenase	463:489	indoleamine 2,3-dioxygenase (IDO) upregulation	463:508	The MSCs' functional response towards inflammatory cues is known as MSC-"licensing" and includes indoleamine 2,3-dioxygenase (IDO) upregulation.
30679801	3	44	theme	functional	376:385	arg1	"					448:448	MSC-"licensing"	434:448	MSC-"licensing"	434:448	The MSCs' functional response towards inflammatory cues is known as MSC-"licensing" and includes indoleamine 2,3-dioxygenase (IDO) upregulation.
30679801	3	44	theme	functional	376:385	arg1	response					387:394	The MSCs' functional response	366:394	The MSCs' functional response towards inflammatory cues	366:420	The MSCs' functional response towards inflammatory cues is known as MSC-"licensing" and includes indoleamine 2,3-dioxygenase (IDO) upregulation.
30679801	8	45	theme	enhanced	1023:1030	arg1	glycolysis					1032:1041	enhanced glycolysis	1023:1041	enhanced glycolysis	1023:1041	We demonstrate that inflammatory MSC-licensing causes metabolic shifts including enhanced glycolysis and increased fatty acid oxidation.
30679801	6	46	theme	glycolysis	715:724	arg1	levels					705:710	high levels	700:710	high levels of glycolysis and of oxidative phosphorylation	700:757	MSCs are capable of both, high levels of glycolysis and of oxidative phosphorylation.
30679801	6	46	theme	glycolysis	715:724	arg1	MSCs					674:677	MSCs	674:677	MSCs	674:677	MSCs are capable of both, high levels of glycolysis and of oxidative phosphorylation.
30679801	10	47	attach	linked	1364:1369	arg2	turnover					1352:1359	enhanced glucose turnover	1335:1359	enhanced glucose turnover	1335:1359	We identified the Janus kinase (JAK)/signal transducer and activator of transcription (STAT)1 pathway as a regulator of both glycolysis and IDO, and show that enhanced glucose turnover is linked to abundant STAT1 glycosylation.
30679801	10	47	attach	linked	1364:1369	arg1	glycosylation					1389:1401	abundant STAT1 glycosylation	1374:1401	abundant STAT1 glycosylation	1374:1401	We identified the Janus kinase (JAK)/signal transducer and activator of transcription (STAT)1 pathway as a regulator of both glycolysis and IDO, and show that enhanced glucose turnover is linked to abundant STAT1 glycosylation.
30679801	10	48	theme	kinase	1200:1205	arg1	transducer					1220:1229	the Janus kinase (JAK)/signal transducer	1190:1229	the Janus kinase (JAK)/signal transducer	1190:1229	We identified the Janus kinase (JAK)/signal transducer and activator of transcription (STAT)1 pathway as a regulator of both glycolysis and IDO, and show that enhanced glucose turnover is linked to abundant STAT1 glycosylation.
30679801	10	48	theme	kinase	1200:1205	arg1	STAT					1263:1266	STAT	1263:1266	STAT	1263:1266	We identified the Janus kinase (JAK)/signal transducer and activator of transcription (STAT)1 pathway as a regulator of both glycolysis and IDO, and show that enhanced glucose turnover is linked to abundant STAT1 glycosylation.
30679801	8	49	theme	acid	1063:1066	arg1	oxidation					1068:1076	increased fatty acid oxidation	1047:1076	increased fatty acid oxidation	1047:1076	We demonstrate that inflammatory MSC-licensing causes metabolic shifts including enhanced glycolysis and increased fatty acid oxidation.
30679801	10	50	theme	glucose	1344:1350	arg1	turnover					1352:1359	enhanced glucose turnover	1335:1359	enhanced glucose turnover	1335:1359	We identified the Janus kinase (JAK)/signal transducer and activator of transcription (STAT)1 pathway as a regulator of both glycolysis and IDO, and show that enhanced glucose turnover is linked to abundant STAT1 glycosylation.
30679801	1	51	theme	graft-versus-host	262:278	arg1	disease					280:286	graft-versus-host disease	262:286	graft-versus-host disease	262:286	Mesenchymal stem cells (MSCs) represent key contributors to tissue homeostasis and promising therapeutics for hyperinflammatory conditions including graft-versus-host disease.
30679801	10	52	theme	Janus	1194:1198	arg1	JAK					1208:1210	JAK	1208:1210	JAK	1208:1210	We identified the Janus kinase (JAK)/signal transducer and activator of transcription (STAT)1 pathway as a regulator of both glycolysis and IDO, and show that enhanced glucose turnover is linked to abundant STAT1 glycosylation.
30679801	10	52	theme	Janus	1194:1198	arg1	kinase					1200:1205	Janus kinase	1194:1205	the Janus kinase (JAK)/signal transducer	1190:1229	We identified the Janus kinase (JAK)/signal transducer and activator of transcription (STAT)1 pathway as a regulator of both glycolysis and IDO, and show that enhanced glucose turnover is linked to abundant STAT1 glycosylation.
30679801	5	53	theme	several	600:606	arg1	functions					608:616	several functions	600:616	several functions	600:616	Increasing evidence suggests that several functions are (co-)determined by the cells' metabolic commitment.
30679801	10	54	theme	enhanced	1335:1342	arg1	turnover					1352:1359	enhanced glucose turnover	1335:1359	enhanced glucose turnover	1335:1359	We identified the Janus kinase (JAK)/signal transducer and activator of transcription (STAT)1 pathway as a regulator of both glycolysis and IDO, and show that enhanced glucose turnover is linked to abundant STAT1 glycosylation.
30679801	7	55	theme	phenotype	837:845	arg1	alterations					800:810	alterations	800:810	alterations of the immune regulatory phenotype elicited by inflammatory priming	800:878	Although several studies have addressed alterations of the immune regulatory phenotype elicited by inflammatory priming metabolic mechanisms controlling this process remain unknown.
30679801	3	56	theme	inflammatory	404:415	arg1	cues					417:420	inflammatory cues	404:420	inflammatory cues	404:420	The MSCs' functional response towards inflammatory cues is known as MSC-"licensing" and includes indoleamine 2,3-dioxygenase (IDO) upregulation.
30679801	1	57	theme	key	153:155	arg1	contributors					157:168	key contributors	153:168	key contributors to tissue homeostasis	153:190	Mesenchymal stem cells (MSCs) represent key contributors to tissue homeostasis and promising therapeutics for hyperinflammatory conditions including graft-versus-host disease.
30679801	6	58	theme	high	700:703	arg1	levels					705:710	high levels	700:710	high levels of glycolysis and of oxidative phosphorylation	700:757	MSCs are capable of both, high levels of glycolysis and of oxidative phosphorylation.
30679801	6	58	theme	high	700:703	arg1	MSCs					674:677	MSCs	674:677	MSCs	674:677	MSCs are capable of both, high levels of glycolysis and of oxidative phosphorylation.
30679801	0	59	theme	cells	82:86	arg1	suppressivity					48:60	suppressivity	48:60	suppressivity of mesenchymal stem cells	48:86	Inflammation-induced glycolytic switch controls suppressivity of mesenchymal stem cells via STAT1 glycosylation.
30679801	10	60	theme	transducer	1220:1229	arg1	pathway					1270:1276	the Janus kinase (JAK)/signal transducer and activator of transcription (STAT)1 pathway	1190:1276	the Janus kinase (JAK)/signal transducer and activator of transcription (STAT)1 pathway	1190:1276	We identified the Janus kinase (JAK)/signal transducer and activator of transcription (STAT)1 pathway as a regulator of both glycolysis and IDO, and show that enhanced glucose turnover is linked to abundant STAT1 glycosylation.
30679801	10	60	theme	transducer	1220:1229	arg1	regulator					1283:1291	a regulator	1281:1291	a regulator of both glycolysis and IDO	1281:1318	We identified the Janus kinase (JAK)/signal transducer and activator of transcription (STAT)1 pathway as a regulator of both glycolysis and IDO, and show that enhanced glucose turnover is linked to abundant STAT1 glycosylation.
30679801	2	61	theme	immunomodulatory	295:310	arg1	effects					312:318	Their immunomodulatory effects	289:318	Their immunomodulatory effects	289:318	Their immunomodulatory effects are controlled by microenvironmental signals.
30679801	7	62	theme	regulatory	826:835	arg1	phenotype					837:845	the immune regulatory phenotype	815:845	the immune regulatory phenotype elicited by inflammatory priming	815:878	Although several studies have addressed alterations of the immune regulatory phenotype elicited by inflammatory priming metabolic mechanisms controlling this process remain unknown.
30679801	10	63	theme	abundant	1374:1381	arg1	glycosylation					1389:1401	abundant STAT1 glycosylation	1374:1401	abundant STAT1 glycosylation	1374:1401	We identified the Janus kinase (JAK)/signal transducer and activator of transcription (STAT)1 pathway as a regulator of both glycolysis and IDO, and show that enhanced glucose turnover is linked to abundant STAT1 glycosylation.
30679801	7	64	theme	immune	819:824	arg1	phenotype					837:845	the immune regulatory phenotype	815:845	the immune regulatory phenotype elicited by inflammatory priming	815:878	Although several studies have addressed alterations of the immune regulatory phenotype elicited by inflammatory priming metabolic mechanisms controlling this process remain unknown.
32641986	5	0	theme	datasets	687:694	arg1	group					664:668	A group	662:668	A group of transcriptome datasets	662:694	Methods: A group of transcriptome datasets were downloaded and analyzed for the characterization of IFIT3 in PDAC.
32641986	5	0	theme	datasets	687:694	arg1	datasets					687:694	transcriptome datasets	673:694	transcriptome datasets	673:694	Methods: A group of transcriptome datasets were downloaded and analyzed for the characterization of IFIT3 in PDAC.
32641986	6	1	dep	in	935:936	arg1	vitro					938:942	vitro	938:942	vitro	938:942	Highly metastatic PDAC cell line L3.6pl and patient-derived primary cell TBO368 were used and IFIT3 knockdown and the corresponding knockin cells were established for in vitro studies.
32641986	10	2	theme	gemcitabine	1634:1644	arg1	treatments					1682:1691	gemcitabine, paclitaxel, and FOLFIRINOX regimen treatments	1634:1691	gemcitabine, paclitaxel, and FOLFIRINOX regimen treatments	1634:1691	Knockdown of IFIT3 attenuates the chemotherapy resistance of PDAC cells to gemcitabine, paclitaxel, and FOLFIRINOX regimen treatments, independent of individual chemotherapy regimens.
32641986	11	3	theme	IFIT3	1749:1753	arg1	overexpression					1755:1768	While IFIT3 overexpression	1743:1768	While IFIT3 overexpression	1743:1768	While IFIT3 overexpression was found to promote drug resistance.
32641986	7	4	theme	chemotherapy	1209:1220	arg1	resistance					1222:1231	chemotherapy resistance	1209:1231	chemotherapy resistance of PDAC	1209:1239	Chemotherapy-induced apoptosis, ROS production, confocal immunofluorescence, subcellular fractionation, chromatin-immunoprecipitation, co-immunoprecipitation and mass spectrometry analysis were determined to further explore the biological role of IFIT3 in chemotherapy resistance of PDAC.
32641986	5	5	from	characterization	733:748	arg1	PDAC					762:765	PDAC	762:765	PDAC	762:765	Methods: A group of transcriptome datasets were downloaded and analyzed for the characterization of IFIT3 in PDAC.
32641986	12	6	theme	protein	1907:1913	arg1	VDAC2					1915:1919	the mitochondrial channel protein VDAC2	1881:1919	the mitochondrial channel protein VDAC2	1881:1919	Co-immunoprecipitation identified a direct interaction between IFIT3 and the mitochondrial channel protein VDAC2, an important regulator of mitochondria-associated apoptosis.
32641986	12	6	theme	protein	1907:1913	arg1	regulator					1935:1943	an important regulator	1922:1943	an important regulator of mitochondria-associated apoptosis	1922:1980	Co-immunoprecipitation identified a direct interaction between IFIT3 and the mitochondrial channel protein VDAC2, an important regulator of mitochondria-associated apoptosis.
32641986	10	7	theme	regimen	1674:1680	arg1	treatments					1682:1691	gemcitabine, paclitaxel, and FOLFIRINOX regimen treatments	1634:1691	gemcitabine, paclitaxel, and FOLFIRINOX regimen treatments	1634:1691	Knockdown of IFIT3 attenuates the chemotherapy resistance of PDAC cells to gemcitabine, paclitaxel, and FOLFIRINOX regimen treatments, independent of individual chemotherapy regimens.
32641986	11	8	theme	drug	1791:1794	arg1	resistance					1796:1805	drug resistance	1791:1805	drug resistance	1791:1805	While IFIT3 overexpression was found to promote drug resistance.
32641986	5	9	theme	transcriptome	673:685	arg1	datasets					687:694	transcriptome datasets	673:694	transcriptome datasets	673:694	Methods: A group of transcriptome datasets were downloaded and analyzed for the characterization of IFIT3 in PDAC.
32641986	6	10	theme	primary	828:834	arg1	TBO368					841:846	patient-derived primary cell TBO368	812:846	patient-derived primary cell TBO368	812:846	Highly metastatic PDAC cell line L3.6pl and patient-derived primary cell TBO368 were used and IFIT3 knockdown and the corresponding knockin cells were established for in vitro studies.
32641986	2	11	theme	antiviral	299:307	arg1	functions					330:338	antiviral and pro-inflammatory functions	299:338	antiviral and pro-inflammatory functions	299:338	IFIT3 is an interferon-stimulated gene with antiviral and pro-inflammatory functions.
32641986	3	12	from	IFIT3	500:504	arg1	PDAC					537:540	PDAC	537:540	PDAC	537:540	Our previous work has shown that high expression of IFIT3 is correlated with poor survival in PDAC patients who receive chemotherapy suggesting a link between IFIT3 and chemotherapy resistance in PDAC.
32641986	6	13	used	used	853:856	arg2	TBO368					841:846	patient-derived primary cell TBO368	812:846	patient-derived primary cell TBO368	812:846	Highly metastatic PDAC cell line L3.6pl and patient-derived primary cell TBO368 were used and IFIT3 knockdown and the corresponding knockin cells were established for in vitro studies.
32641986	6	13	used	used	853:856	arg2	line					796:799	Highly metastatic PDAC cell line	768:799	Highly metastatic PDAC cell line L3.6pl	768:806	Highly metastatic PDAC cell line L3.6pl and patient-derived primary cell TBO368 were used and IFIT3 knockdown and the corresponding knockin cells were established for in vitro studies.
32641986	9	14	theme	apoptosis	1528:1536	arg1	regulation					1490:1499	the regulation	1486:1499	the regulation of mitochondria-associated apoptosis during chemotherapy	1486:1556	We further identify a crucial role for IFIT3 in the regulation of mitochondria-associated apoptosis during chemotherapy.
32641986	8	15	theme	transcriptome	1265:1277	arg1	data					1279:1282	PDAC transcriptome data	1260:1282	PDAC transcriptome data	1260:1282	Results: Based on PDAC transcriptome data, we show that IFIT3 expression is associated with the squamous molecular subtype of PDAC and an increase in inflammatory response and apoptosis pathways.
32641986	6	16	theme	knockin	900:906	arg1	cells					908:912	IFIT3 knockdown and the corresponding knockin cells	862:912	IFIT3 knockdown and the corresponding knockin cells	862:912	Highly metastatic PDAC cell line L3.6pl and patient-derived primary cell TBO368 were used and IFIT3 knockdown and the corresponding knockin cells were established for in vitro studies.
32641986	1	17	theme	cancers	194:200	arg1	worldwide					202:210	the most lethal cancers worldwide	178:210	the most lethal cancers worldwide	178:210	Pancreatic ductal adenocarcinoma (PDAC) is one of the most lethal cancers worldwide and effective therapy remains a challenge.
32641986	12	18	theme	mitochondrial	1885:1897	arg1	VDAC2					1915:1919	the mitochondrial channel protein VDAC2	1881:1919	the mitochondrial channel protein VDAC2	1881:1919	Co-immunoprecipitation identified a direct interaction between IFIT3 and the mitochondrial channel protein VDAC2, an important regulator of mitochondria-associated apoptosis.
32641986	12	18	theme	mitochondrial	1885:1897	arg1	regulator					1935:1943	an important regulator	1922:1943	an important regulator of mitochondria-associated apoptosis	1922:1980	Co-immunoprecipitation identified a direct interaction between IFIT3 and the mitochondrial channel protein VDAC2, an important regulator of mitochondria-associated apoptosis.
32641986	8	19	theme	squamous	1338:1345	arg1	subtype					1357:1363	the squamous molecular subtype	1334:1363	the squamous molecular subtype of PDAC	1334:1371	Results: Based on PDAC transcriptome data, we show that IFIT3 expression is associated with the squamous molecular subtype of PDAC and an increase in inflammatory response and apoptosis pathways.
32641986	2	20	theme	pro-inflammatory	313:328	arg1	functions					330:338	antiviral and pro-inflammatory functions	299:338	antiviral and pro-inflammatory functions	299:338	IFIT3 is an interferon-stimulated gene with antiviral and pro-inflammatory functions.
32641986	16	21	theme	Targeting	2392:2400	arg1	IFIT3/VDAC2					2402:2412	Targeting IFIT3/VDAC2	2392:2412	Targeting IFIT3/VDAC2	2392:2412	Targeting IFIT3/VDAC2 may represent a novel strategy to sensitize aggressive forms of pancreatic cancer to conventional chemotherapy regimens.
32641986	8	22	theme	IFIT3	1298:1302	arg1	expression					1304:1313	IFIT3 expression	1298:1313	IFIT3 expression	1298:1313	Results: Based on PDAC transcriptome data, we show that IFIT3 expression is associated with the squamous molecular subtype of PDAC and an increase in inflammatory response and apoptosis pathways.
32641986	0	23	from	modification	84:95	arg1	cancer					120:125	pancreatic cancer	109:125	pancreatic cancer	109:125	Inflammatory IFIT3 renders chemotherapy resistance by regulating post-translational modification of VDAC2 in pancreatic cancer.
32641986	8	24	theme	PDAC	1368:1371	arg1	increase					1380:1387	an increase	1377:1387	an increase in inflammatory response and apoptosis pathways	1377:1435	Results: Based on PDAC transcriptome data, we show that IFIT3 expression is associated with the squamous molecular subtype of PDAC and an increase in inflammatory response and apoptosis pathways.
32641986	8	24	theme	PDAC	1368:1371	arg1	subtype					1357:1363	the squamous molecular subtype	1334:1363	the squamous molecular subtype of PDAC	1334:1371	Results: Based on PDAC transcriptome data, we show that IFIT3 expression is associated with the squamous molecular subtype of PDAC and an increase in inflammatory response and apoptosis pathways.
32641986	10	25	theme	chemotherapy	1720:1731	arg1	regimens					1733:1740	individual chemotherapy regimens	1709:1740	individual chemotherapy regimens	1709:1740	Knockdown of IFIT3 attenuates the chemotherapy resistance of PDAC cells to gemcitabine, paclitaxel, and FOLFIRINOX regimen treatments, independent of individual chemotherapy regimens.
32641986	8	26	from	increase	1380:1387	arg1	pathways					1428:1435	apoptosis pathways	1418:1435	apoptosis pathways	1418:1435	Results: Based on PDAC transcriptome data, we show that IFIT3 expression is associated with the squamous molecular subtype of PDAC and an increase in inflammatory response and apoptosis pathways.
32641986	8	26	from	increase	1380:1387	arg1	response					1405:1412	inflammatory response	1392:1412	inflammatory response	1392:1412	Results: Based on PDAC transcriptome data, we show that IFIT3 expression is associated with the squamous molecular subtype of PDAC and an increase in inflammatory response and apoptosis pathways.
32641986	7	27	theme	mass	1115:1118	arg1	analysis					1133:1140	mass spectrometry analysis	1115:1140	mass spectrometry analysis	1115:1140	Chemotherapy-induced apoptosis, ROS production, confocal immunofluorescence, subcellular fractionation, chromatin-immunoprecipitation, co-immunoprecipitation and mass spectrometry analysis were determined to further explore the biological role of IFIT3 in chemotherapy resistance of PDAC.
32641986	8	28	from	subtype	1357:1363	arg1	pathways					1428:1435	apoptosis pathways	1418:1435	apoptosis pathways	1418:1435	Results: Based on PDAC transcriptome data, we show that IFIT3 expression is associated with the squamous molecular subtype of PDAC and an increase in inflammatory response and apoptosis pathways.
32641986	8	28	from	subtype	1357:1363	arg1	response					1405:1412	inflammatory response	1392:1412	inflammatory response	1392:1412	Results: Based on PDAC transcriptome data, we show that IFIT3 expression is associated with the squamous molecular subtype of PDAC and an increase in inflammatory response and apoptosis pathways.
32641986	2	29	with	gene	289:292	arg1	functions					330:338	antiviral and pro-inflammatory functions	299:338	antiviral and pro-inflammatory functions	299:338	IFIT3 is an interferon-stimulated gene with antiviral and pro-inflammatory functions.
32641986	13	30	theme	VDAC2	2125:2129	arg1	interaction					2110:2120	the interaction	2106:2120	the interaction of VDAC2 with O-GlcNAc transferase	2106:2155	It was subsequently found that IFIT3 regulates the post-translational modification-O-GlcNAcylation of VDAC2 by stabilizing the interaction of VDAC2 with O-GlcNAc transferase.
32641986	4	31	dep	role	562:565	arg1	the					552:554	the	552:554	the	552:554	However, the exact role and molecular mechanism of IFIT3 in chemotherapy resistance in PDAC has been unclear.
32641986	3	32	theme	previous	345:352	arg1	work					354:357	Our previous work	341:357	Our previous work	341:357	Our previous work has shown that high expression of IFIT3 is correlated with poor survival in PDAC patients who receive chemotherapy suggesting a link between IFIT3 and chemotherapy resistance in PDAC.
32641986	13	33	theme	VDAC2	2085:2089	arg1	modification-O-GlcNAcylation					2053:2080	the post-translational modification-O-GlcNAcylation	2030:2080	the post-translational modification-O-GlcNAcylation of VDAC2	2030:2089	It was subsequently found that IFIT3 regulates the post-translational modification-O-GlcNAcylation of VDAC2 by stabilizing the interaction of VDAC2 with O-GlcNAc transferase.
32641986	0	34	theme	VDAC2	100:104	arg1	modification					84:95	post-translational modification	65:95	post-translational modification of VDAC2 in pancreatic cancer	65:125	Inflammatory IFIT3 renders chemotherapy resistance by regulating post-translational modification of VDAC2 in pancreatic cancer.
32641986	7	35	theme	IFIT3	1200:1204	arg1	role					1192:1195	the biological role	1177:1195	the biological role of IFIT3 in chemotherapy resistance of PDAC	1177:1239	Chemotherapy-induced apoptosis, ROS production, confocal immunofluorescence, subcellular fractionation, chromatin-immunoprecipitation, co-immunoprecipitation and mass spectrometry analysis were determined to further explore the biological role of IFIT3 in chemotherapy resistance of PDAC.
32641986	8	36	theme	apoptosis	1418:1426	arg1	pathways					1428:1435	apoptosis pathways	1418:1435	apoptosis pathways	1418:1435	Results: Based on PDAC transcriptome data, we show that IFIT3 expression is associated with the squamous molecular subtype of PDAC and an increase in inflammatory response and apoptosis pathways.
32641986	0	37	theme	pancreatic	109:118	arg1	cancer					120:125	pancreatic cancer	109:125	pancreatic cancer	109:125	Inflammatory IFIT3 renders chemotherapy resistance by regulating post-translational modification of VDAC2 in pancreatic cancer.
32641986	7	38	theme	ROS	985:987	arg1	production					989:998	ROS production	985:998	ROS production	985:998	Chemotherapy-induced apoptosis, ROS production, confocal immunofluorescence, subcellular fractionation, chromatin-immunoprecipitation, co-immunoprecipitation and mass spectrometry analysis were determined to further explore the biological role of IFIT3 in chemotherapy resistance of PDAC.
32641986	15	39	theme	central	2304:2310	arg1	mechanism					2312:2320	a central mechanism	2302:2320	a central mechanism by which IFIT3 expression can affect chemotherapy resistance in PDAC	2302:2389	Conclusions: These results effectively demonstrate a central mechanism by which IFIT3 expression can affect chemotherapy resistance in PDAC.
32641986	10	40	theme	IFIT3	1572:1576	arg1	Knockdown					1559:1567	Knockdown	1559:1567	Knockdown of IFIT3	1559:1576	Knockdown of IFIT3 attenuates the chemotherapy resistance of PDAC cells to gemcitabine, paclitaxel, and FOLFIRINOX regimen treatments, independent of individual chemotherapy regimens.
32641986	16	41	theme	pancreatic	2478:2487	arg1	cancer					2489:2494	pancreatic cancer	2478:2494	pancreatic cancer	2478:2494	Targeting IFIT3/VDAC2 may represent a novel strategy to sensitize aggressive forms of pancreatic cancer to conventional chemotherapy regimens.
32641986	4	42	from	role	562:565	arg1	resistance					616:625	chemotherapy resistance	603:625	chemotherapy resistance in PDAC	603:633	However, the exact role and molecular mechanism of IFIT3 in chemotherapy resistance in PDAC has been unclear.
32641986	13	43	with	interaction	2110:2120	arg1	transferase					2145:2155	O-GlcNAc transferase	2136:2155	O-GlcNAc transferase	2136:2155	It was subsequently found that IFIT3 regulates the post-translational modification-O-GlcNAcylation of VDAC2 by stabilizing the interaction of VDAC2 with O-GlcNAc transferase.
32641986	4	44	from	mechanism	581:589	arg1	resistance					616:625	chemotherapy resistance	603:625	chemotherapy resistance in PDAC	603:633	However, the exact role and molecular mechanism of IFIT3 in chemotherapy resistance in PDAC has been unclear.
32641986	3	45	theme	IFIT3	393:397	arg1	expression					379:388	high expression	374:388	high expression of IFIT3	374:397	Our previous work has shown that high expression of IFIT3 is correlated with poor survival in PDAC patients who receive chemotherapy suggesting a link between IFIT3 and chemotherapy resistance in PDAC.
32641986	16	46	theme	chemotherapy	2512:2523	arg1	regimens					2525:2532	conventional chemotherapy regimens	2499:2532	conventional chemotherapy regimens	2499:2532	Targeting IFIT3/VDAC2 may represent a novel strategy to sensitize aggressive forms of pancreatic cancer to conventional chemotherapy regimens.
32641986	6	47	theme	corresponding	886:898	arg1	knockin					900:906	the corresponding knockin	882:906	the corresponding knockin	882:906	Highly metastatic PDAC cell line L3.6pl and patient-derived primary cell TBO368 were used and IFIT3 knockdown and the corresponding knockin cells were established for in vitro studies.
32641986	1	48	theme	Pancreatic	128:137	arg1	PDAC					162:165	PDAC	162:165	PDAC	162:165	Pancreatic ductal adenocarcinoma (PDAC) is one of the most lethal cancers worldwide and effective therapy remains a challenge.
32641986	1	48	theme	Pancreatic	128:137	arg1	adenocarcinoma					146:159	Pancreatic ductal adenocarcinoma	128:159	Pancreatic ductal adenocarcinoma (PDAC)	128:166	Pancreatic ductal adenocarcinoma (PDAC) is one of the most lethal cancers worldwide and effective therapy remains a challenge.
32641986	7	49	from	role	1192:1195	arg1	resistance					1222:1231	chemotherapy resistance	1209:1231	chemotherapy resistance of PDAC	1209:1239	Chemotherapy-induced apoptosis, ROS production, confocal immunofluorescence, subcellular fractionation, chromatin-immunoprecipitation, co-immunoprecipitation and mass spectrometry analysis were determined to further explore the biological role of IFIT3 in chemotherapy resistance of PDAC.
32641986	15	50	theme	chemotherapy	2359:2370	arg1	resistance					2372:2381	chemotherapy resistance	2359:2381	chemotherapy resistance in PDAC	2359:2389	Conclusions: These results effectively demonstrate a central mechanism by which IFIT3 expression can affect chemotherapy resistance in PDAC.
32641986	3	51	theme	poor	418:421	arg1	survival					423:430	poor survival	418:430	poor survival in PDAC patients who receive chemotherapy suggesting a link between IFIT3 and chemotherapy resistance in PDAC	418:540	Our previous work has shown that high expression of IFIT3 is correlated with poor survival in PDAC patients who receive chemotherapy suggesting a link between IFIT3 and chemotherapy resistance in PDAC.
32641986	6	52	theme	metastatic	775:784	arg1	line					796:799	Highly metastatic PDAC cell line	768:799	Highly metastatic PDAC cell line L3.6pl	768:806	Highly metastatic PDAC cell line L3.6pl and patient-derived primary cell TBO368 were used and IFIT3 knockdown and the corresponding knockin cells were established for in vitro studies.
32641986	3	53	theme	chemotherapy	510:521	arg1	resistance					523:532	chemotherapy resistance	510:532	chemotherapy resistance in PDAC	510:540	Our previous work has shown that high expression of IFIT3 is correlated with poor survival in PDAC patients who receive chemotherapy suggesting a link between IFIT3 and chemotherapy resistance in PDAC.
32641986	6	54	theme	IFIT3	862:866	arg1	knockdown					868:876	IFIT3 knockdown	862:876	IFIT3 knockdown	862:876	Highly metastatic PDAC cell line L3.6pl and patient-derived primary cell TBO368 were used and IFIT3 knockdown and the corresponding knockin cells were established for in vitro studies.
32641986	14	55	theme	Increased	2158:2166	arg1	O-GlcNAcylation					2168:2182	Increased O-GlcNAcylation	2158:2182	Increased O-GlcNAcylation of VDAC2	2158:2191	Increased O-GlcNAcylation of VDAC2 protected PDAC cells from chemotherapy induced apoptosis.
32641986	4	56	theme	exact	556:560	arg1	role					562:565	exact role	556:565	exact role	556:565	However, the exact role and molecular mechanism of IFIT3 in chemotherapy resistance in PDAC has been unclear.
32641986	10	57	theme	PDAC	1620:1623	arg1	cells					1625:1629	PDAC cells	1620:1629	PDAC cells	1620:1629	Knockdown of IFIT3 attenuates the chemotherapy resistance of PDAC cells to gemcitabine, paclitaxel, and FOLFIRINOX regimen treatments, independent of individual chemotherapy regimens.
32641986	9	58	theme	crucial	1460:1466	arg1	role					1468:1471	a crucial role	1458:1471	a crucial role for IFIT3 in the regulation of mitochondria-associated apoptosis during chemotherapy	1458:1556	We further identify a crucial role for IFIT3 in the regulation of mitochondria-associated apoptosis during chemotherapy.
32641986	9	59	from	role	1468:1471	arg1	regulation					1490:1499	the regulation	1486:1499	the regulation of mitochondria-associated apoptosis during chemotherapy	1486:1556	We further identify a crucial role for IFIT3 in the regulation of mitochondria-associated apoptosis during chemotherapy.
32641986	15	60	theme	IFIT3	2331:2335	arg1	expression					2337:2346	IFIT3 expression	2331:2346	IFIT3 expression	2331:2346	Conclusions: These results effectively demonstrate a central mechanism by which IFIT3 expression can affect chemotherapy resistance in PDAC.
32641986	16	61	theme	novel	2430:2434	arg1	strategy					2436:2443	a novel strategy	2428:2443	a novel strategy to sensitize aggressive forms of pancreatic cancer to conventional chemotherapy regimens	2428:2532	Targeting IFIT3/VDAC2 may represent a novel strategy to sensitize aggressive forms of pancreatic cancer to conventional chemotherapy regimens.
32641986	11	62	theme	While	1743:1747	arg1	overexpression					1755:1768	While IFIT3 overexpression	1743:1768	While IFIT3 overexpression	1743:1768	While IFIT3 overexpression was found to promote drug resistance.
32641986	6	63	link	patient-derived	812:826	arg1	TBO368					841:846	patient-derived primary cell TBO368	812:846	patient-derived primary cell TBO368	812:846	Highly metastatic PDAC cell line L3.6pl and patient-derived primary cell TBO368 were used and IFIT3 knockdown and the corresponding knockin cells were established for in vitro studies.
32641986	12	64	theme	mitochondria-associated	1948:1970	arg1	apoptosis					1972:1980	mitochondria-associated apoptosis	1948:1980	mitochondria-associated apoptosis	1948:1980	Co-immunoprecipitation identified a direct interaction between IFIT3 and the mitochondrial channel protein VDAC2, an important regulator of mitochondria-associated apoptosis.
32641986	6	65	theme	in	935:936	arg1	studies					944:950	in vitro studies	935:950	in vitro studies	935:950	Highly metastatic PDAC cell line L3.6pl and patient-derived primary cell TBO368 were used and IFIT3 knockdown and the corresponding knockin cells were established for in vitro studies.
32641986	4	66	theme	IFIT3	594:598	arg1	role					562:565	exact role	556:565	exact role	556:565	However, the exact role and molecular mechanism of IFIT3 in chemotherapy resistance in PDAC has been unclear.
32641986	4	66	theme	IFIT3	594:598	arg1	mechanism					581:589	molecular mechanism	571:589	molecular mechanism	571:589	However, the exact role and molecular mechanism of IFIT3 in chemotherapy resistance in PDAC has been unclear.
32641986	16	67	theme	aggressive	2458:2467	arg1	forms					2469:2473	aggressive forms	2458:2473	aggressive forms of pancreatic cancer	2458:2494	Targeting IFIT3/VDAC2 may represent a novel strategy to sensitize aggressive forms of pancreatic cancer to conventional chemotherapy regimens.
32641986	7	68	theme	subcellular	1030:1040	arg1	immunofluorescence					1010:1027	confocal immunofluorescence	1001:1027	confocal immunofluorescence	1001:1027	Chemotherapy-induced apoptosis, ROS production, confocal immunofluorescence, subcellular fractionation, chromatin-immunoprecipitation, co-immunoprecipitation and mass spectrometry analysis were determined to further explore the biological role of IFIT3 in chemotherapy resistance of PDAC.
32641986	7	68	theme	subcellular	1030:1040	arg1	fractionation					1042:1054	subcellular fractionation	1030:1054	subcellular fractionation	1030:1054	Chemotherapy-induced apoptosis, ROS production, confocal immunofluorescence, subcellular fractionation, chromatin-immunoprecipitation, co-immunoprecipitation and mass spectrometry analysis were determined to further explore the biological role of IFIT3 in chemotherapy resistance of PDAC.
32641986	6	69	theme	cell	836:839	arg1	TBO368					841:846	patient-derived primary cell TBO368	812:846	patient-derived primary cell TBO368	812:846	Highly metastatic PDAC cell line L3.6pl and patient-derived primary cell TBO368 were used and IFIT3 knockdown and the corresponding knockin cells were established for in vitro studies.
32641986	6	70	dep	line	796:799	arg1	L3.6pl					801:806	L3.6pl	801:806	Highly metastatic PDAC cell line L3.6pl	768:806	Highly metastatic PDAC cell line L3.6pl and patient-derived primary cell TBO368 were used and IFIT3 knockdown and the corresponding knockin cells were established for in vitro studies.
32641986	4	71	theme	chemotherapy	603:614	arg1	resistance					616:625	chemotherapy resistance	603:625	chemotherapy resistance in PDAC	603:633	However, the exact role and molecular mechanism of IFIT3 in chemotherapy resistance in PDAC has been unclear.
32641986	10	72	theme	FOLFIRINOX	1663:1672	arg1	regimen					1674:1680	FOLFIRINOX regimen	1663:1680	FOLFIRINOX regimen	1663:1680	Knockdown of IFIT3 attenuates the chemotherapy resistance of PDAC cells to gemcitabine, paclitaxel, and FOLFIRINOX regimen treatments, independent of individual chemotherapy regimens.
32641986	7	73	theme	biological	1181:1190	arg1	role					1192:1195	the biological role	1177:1195	the biological role of IFIT3 in chemotherapy resistance of PDAC	1177:1239	Chemotherapy-induced apoptosis, ROS production, confocal immunofluorescence, subcellular fractionation, chromatin-immunoprecipitation, co-immunoprecipitation and mass spectrometry analysis were determined to further explore the biological role of IFIT3 in chemotherapy resistance of PDAC.
32641986	6	74	theme	patient-derived	812:826	arg1	TBO368					841:846	patient-derived primary cell TBO368	812:846	patient-derived primary cell TBO368	812:846	Highly metastatic PDAC cell line L3.6pl and patient-derived primary cell TBO368 were used and IFIT3 knockdown and the corresponding knockin cells were established for in vitro studies.
32641986	9	75	theme	mitochondria-associated	1504:1526	arg1	apoptosis					1528:1536	mitochondria-associated apoptosis	1504:1536	mitochondria-associated apoptosis	1504:1536	We further identify a crucial role for IFIT3 in the regulation of mitochondria-associated apoptosis during chemotherapy.
32641986	10	76	theme	individual	1709:1718	arg1	regimens					1733:1740	individual chemotherapy regimens	1709:1740	individual chemotherapy regimens	1709:1740	Knockdown of IFIT3 attenuates the chemotherapy resistance of PDAC cells to gemcitabine, paclitaxel, and FOLFIRINOX regimen treatments, independent of individual chemotherapy regimens.
32641986	13	77	theme	O-GlcNAc	2136:2143	arg1	transferase					2145:2155	O-GlcNAc transferase	2136:2155	O-GlcNAc transferase	2136:2155	It was subsequently found that IFIT3 regulates the post-translational modification-O-GlcNAcylation of VDAC2 by stabilizing the interaction of VDAC2 with O-GlcNAc transferase.
32641986	14	78	dep	induced	2232:2238	arg1	chemotherapy					2219:2230	chemotherapy	2219:2230	chemotherapy	2219:2230	Increased O-GlcNAcylation of VDAC2 protected PDAC cells from chemotherapy induced apoptosis.
32641986	1	79	theme	lethal	187:192	arg1	worldwide					202:210	the most lethal cancers worldwide	178:210	the most lethal cancers worldwide	178:210	Pancreatic ductal adenocarcinoma (PDAC) is one of the most lethal cancers worldwide and effective therapy remains a challenge.
32641986	8	80	theme	PDAC	1260:1263	arg1	data					1279:1282	PDAC transcriptome data	1260:1282	PDAC transcriptome data	1260:1282	Results: Based on PDAC transcriptome data, we show that IFIT3 expression is associated with the squamous molecular subtype of PDAC and an increase in inflammatory response and apoptosis pathways.
32641986	12	81	theme	channel	1899:1905	arg1	VDAC2					1915:1919	the mitochondrial channel protein VDAC2	1881:1919	the mitochondrial channel protein VDAC2	1881:1919	Co-immunoprecipitation identified a direct interaction between IFIT3 and the mitochondrial channel protein VDAC2, an important regulator of mitochondria-associated apoptosis.
32641986	12	81	theme	channel	1899:1905	arg1	regulator					1935:1943	an important regulator	1922:1943	an important regulator of mitochondria-associated apoptosis	1922:1980	Co-immunoprecipitation identified a direct interaction between IFIT3 and the mitochondrial channel protein VDAC2, an important regulator of mitochondria-associated apoptosis.
32641986	10	82	theme	independent	1694:1704	arg1	treatments					1682:1691	gemcitabine, paclitaxel, and FOLFIRINOX regimen treatments	1634:1691	gemcitabine, paclitaxel, and FOLFIRINOX regimen treatments	1634:1691	Knockdown of IFIT3 attenuates the chemotherapy resistance of PDAC cells to gemcitabine, paclitaxel, and FOLFIRINOX regimen treatments, independent of individual chemotherapy regimens.
32641986	3	83	from	resistance	523:532	arg1	PDAC					537:540	PDAC	537:540	PDAC	537:540	Our previous work has shown that high expression of IFIT3 is correlated with poor survival in PDAC patients who receive chemotherapy suggesting a link between IFIT3 and chemotherapy resistance in PDAC.
32641986	1	84	theme	worldwide	202:210	arg1	one					171:173	one	171:173	one	171:173	Pancreatic ductal adenocarcinoma (PDAC) is one of the most lethal cancers worldwide and effective therapy remains a challenge.
32641986	1	84	theme	worldwide	202:210	arg1	worldwide					202:210	the most lethal cancers worldwide	178:210	the most lethal cancers worldwide	178:210	Pancreatic ductal adenocarcinoma (PDAC) is one of the most lethal cancers worldwide and effective therapy remains a challenge.
32641986	1	85	theme	effective	216:224	arg1	therapy					226:232	effective therapy	216:232	effective therapy	216:232	Pancreatic ductal adenocarcinoma (PDAC) is one of the most lethal cancers worldwide and effective therapy remains a challenge.
32641986	15	86	from	resistance	2372:2381	arg1	PDAC					2386:2389	PDAC	2386:2389	PDAC	2386:2389	Conclusions: These results effectively demonstrate a central mechanism by which IFIT3 expression can affect chemotherapy resistance in PDAC.
32641986	8	87	theme	molecular	1347:1355	arg1	subtype					1357:1363	the squamous molecular subtype	1334:1363	the squamous molecular subtype of PDAC	1334:1371	Results: Based on PDAC transcriptome data, we show that IFIT3 expression is associated with the squamous molecular subtype of PDAC and an increase in inflammatory response and apoptosis pathways.
32641986	10	88	theme	regimens	1733:1740	arg1	independent					1694:1704	independent	1694:1704	independent	1694:1704	Knockdown of IFIT3 attenuates the chemotherapy resistance of PDAC cells to gemcitabine, paclitaxel, and FOLFIRINOX regimen treatments, independent of individual chemotherapy regimens.
32641986	7	89	theme	spectrometry	1120:1131	arg1	analysis					1133:1140	mass spectrometry analysis	1115:1140	mass spectrometry analysis	1115:1140	Chemotherapy-induced apoptosis, ROS production, confocal immunofluorescence, subcellular fractionation, chromatin-immunoprecipitation, co-immunoprecipitation and mass spectrometry analysis were determined to further explore the biological role of IFIT3 in chemotherapy resistance of PDAC.
32641986	1	90	theme	ductal	139:144	arg1	PDAC					162:165	PDAC	162:165	PDAC	162:165	Pancreatic ductal adenocarcinoma (PDAC) is one of the most lethal cancers worldwide and effective therapy remains a challenge.
32641986	1	90	theme	ductal	139:144	arg1	adenocarcinoma					146:159	Pancreatic ductal adenocarcinoma	128:159	Pancreatic ductal adenocarcinoma (PDAC)	128:166	Pancreatic ductal adenocarcinoma (PDAC) is one of the most lethal cancers worldwide and effective therapy remains a challenge.
32641986	6	91	theme	cell	791:794	arg1	line					796:799	Highly metastatic PDAC cell line	768:799	Highly metastatic PDAC cell line L3.6pl	768:806	Highly metastatic PDAC cell line L3.6pl and patient-derived primary cell TBO368 were used and IFIT3 knockdown and the corresponding knockin cells were established for in vitro studies.
32641986	2	92	theme	interferon-stimulated	267:287	arg1	gene					289:292	an interferon-stimulated gene	264:292	an interferon-stimulated gene with antiviral and pro-inflammatory functions	264:338	IFIT3 is an interferon-stimulated gene with antiviral and pro-inflammatory functions.
32641986	2	92	theme	interferon-stimulated	267:287	arg1	IFIT3					255:259	IFIT3	255:259	IFIT3	255:259	IFIT3 is an interferon-stimulated gene with antiviral and pro-inflammatory functions.
32641986	12	93	theme	direct	1844:1849	arg1	interaction					1851:1861	a direct interaction	1842:1861	a direct interaction between IFIT3 and the mitochondrial channel protein VDAC2, an important regulator of mitochondria-associated apoptosis	1842:1980	Co-immunoprecipitation identified a direct interaction between IFIT3 and the mitochondrial channel protein VDAC2, an important regulator of mitochondria-associated apoptosis.
32641986	5	94	theme	IFIT3	753:757	arg1	characterization					733:748	the characterization	729:748	the characterization of IFIT3 in PDAC	729:765	Methods: A group of transcriptome datasets were downloaded and analyzed for the characterization of IFIT3 in PDAC.
32641986	3	95	from	survival	423:430	arg1	patients					440:447	PDAC patients	435:447	PDAC patients who receive chemotherapy suggesting a link between IFIT3 and chemotherapy resistance in PDAC	435:540	Our previous work has shown that high expression of IFIT3 is correlated with poor survival in PDAC patients who receive chemotherapy suggesting a link between IFIT3 and chemotherapy resistance in PDAC.
32641986	8	96	theme	inflammatory	1392:1403	arg1	response					1405:1412	inflammatory response	1392:1412	inflammatory response	1392:1412	Results: Based on PDAC transcriptome data, we show that IFIT3 expression is associated with the squamous molecular subtype of PDAC and an increase in inflammatory response and apoptosis pathways.
32641986	4	97	from	resistance	616:625	arg1	PDAC					630:633	PDAC	630:633	PDAC	630:633	However, the exact role and molecular mechanism of IFIT3 in chemotherapy resistance in PDAC has been unclear.
32641986	7	98	theme	confocal	1001:1008	arg1	chromatin-immunoprecipitation					1057:1085	chromatin-immunoprecipitation	1057:1085	chromatin-immunoprecipitation	1057:1085	Chemotherapy-induced apoptosis, ROS production, confocal immunofluorescence, subcellular fractionation, chromatin-immunoprecipitation, co-immunoprecipitation and mass spectrometry analysis were determined to further explore the biological role of IFIT3 in chemotherapy resistance of PDAC.
32641986	7	98	theme	confocal	1001:1008	arg1	immunofluorescence					1010:1027	confocal immunofluorescence	1001:1027	confocal immunofluorescence	1001:1027	Chemotherapy-induced apoptosis, ROS production, confocal immunofluorescence, subcellular fractionation, chromatin-immunoprecipitation, co-immunoprecipitation and mass spectrometry analysis were determined to further explore the biological role of IFIT3 in chemotherapy resistance of PDAC.
32641986	7	98	theme	confocal	1001:1008	arg1	fractionation					1042:1054	subcellular fractionation	1030:1054	subcellular fractionation	1030:1054	Chemotherapy-induced apoptosis, ROS production, confocal immunofluorescence, subcellular fractionation, chromatin-immunoprecipitation, co-immunoprecipitation and mass spectrometry analysis were determined to further explore the biological role of IFIT3 in chemotherapy resistance of PDAC.
32641986	0	99	theme	Inflammatory	0:11	arg1	IFIT3					13:17	Inflammatory IFIT3	0:17	Inflammatory IFIT3	0:17	Inflammatory IFIT3 renders chemotherapy resistance by regulating post-translational modification of VDAC2 in pancreatic cancer.
32641986	16	100	theme	cancer	2489:2494	arg1	forms					2469:2473	aggressive forms	2458:2473	aggressive forms of pancreatic cancer	2458:2494	Targeting IFIT3/VDAC2 may represent a novel strategy to sensitize aggressive forms of pancreatic cancer to conventional chemotherapy regimens.
32641986	14	101	theme	induced	2232:2238	arg1	apoptosis					2240:2248	chemotherapy induced apoptosis	2219:2248	chemotherapy induced apoptosis	2219:2248	Increased O-GlcNAcylation of VDAC2 protected PDAC cells from chemotherapy induced apoptosis.
32641986	3	102	theme	high	374:377	arg1	expression					379:388	high expression	374:388	high expression of IFIT3	374:397	Our previous work has shown that high expression of IFIT3 is correlated with poor survival in PDAC patients who receive chemotherapy suggesting a link between IFIT3 and chemotherapy resistance in PDAC.
32641986	13	103	theme	post-translational	2034:2051	arg1	modification-O-GlcNAcylation					2053:2080	the post-translational modification-O-GlcNAcylation	2030:2080	the post-translational modification-O-GlcNAcylation of VDAC2	2030:2089	It was subsequently found that IFIT3 regulates the post-translational modification-O-GlcNAcylation of VDAC2 by stabilizing the interaction of VDAC2 with O-GlcNAc transferase.
32641986	4	104	theme	molecular	571:579	arg1	mechanism					581:589	molecular mechanism	571:589	molecular mechanism	571:589	However, the exact role and molecular mechanism of IFIT3 in chemotherapy resistance in PDAC has been unclear.
32641986	0	105	theme	chemotherapy	27:38	arg1	resistance					40:49	chemotherapy resistance	27:49	chemotherapy resistance	27:49	Inflammatory IFIT3 renders chemotherapy resistance by regulating post-translational modification of VDAC2 in pancreatic cancer.
32641986	7	106	theme	Chemotherapy-induced	953:972	arg1	apoptosis					974:982	Chemotherapy-induced apoptosis	953:982	Chemotherapy-induced apoptosis	953:982	Chemotherapy-induced apoptosis, ROS production, confocal immunofluorescence, subcellular fractionation, chromatin-immunoprecipitation, co-immunoprecipitation and mass spectrometry analysis were determined to further explore the biological role of IFIT3 in chemotherapy resistance of PDAC.
32641986	14	107	theme	PDAC	2203:2206	arg1	cells					2208:2212	PDAC cells	2203:2212	PDAC cells	2203:2212	Increased O-GlcNAcylation of VDAC2 protected PDAC cells from chemotherapy induced apoptosis.
32641986	10	108	theme	chemotherapy	1593:1604	arg1	resistance					1606:1615	the chemotherapy resistance	1589:1615	the chemotherapy resistance of PDAC cells to gemcitabine, paclitaxel, and FOLFIRINOX regimen treatments, independent of individual chemotherapy regimens	1589:1740	Knockdown of IFIT3 attenuates the chemotherapy resistance of PDAC cells to gemcitabine, paclitaxel, and FOLFIRINOX regimen treatments, independent of individual chemotherapy regimens.
32641986	7	109	theme	PDAC	1236:1239	arg1	resistance					1222:1231	chemotherapy resistance	1209:1231	chemotherapy resistance of PDAC	1209:1239	Chemotherapy-induced apoptosis, ROS production, confocal immunofluorescence, subcellular fractionation, chromatin-immunoprecipitation, co-immunoprecipitation and mass spectrometry analysis were determined to further explore the biological role of IFIT3 in chemotherapy resistance of PDAC.
32641986	14	110	theme	VDAC2	2187:2191	arg1	O-GlcNAcylation					2168:2182	Increased O-GlcNAcylation	2158:2182	Increased O-GlcNAcylation of VDAC2	2158:2191	Increased O-GlcNAcylation of VDAC2 protected PDAC cells from chemotherapy induced apoptosis.
32641986	3	111	theme	PDAC	435:438	arg1	patients					440:447	PDAC patients	435:447	PDAC patients who receive chemotherapy suggesting a link between IFIT3 and chemotherapy resistance in PDAC	435:540	Our previous work has shown that high expression of IFIT3 is correlated with poor survival in PDAC patients who receive chemotherapy suggesting a link between IFIT3 and chemotherapy resistance in PDAC.
32641986	6	112	theme	PDAC	786:789	arg1	line					796:799	Highly metastatic PDAC cell line	768:799	Highly metastatic PDAC cell line L3.6pl	768:806	Highly metastatic PDAC cell line L3.6pl and patient-derived primary cell TBO368 were used and IFIT3 knockdown and the corresponding knockin cells were established for in vitro studies.
32641986	0	113	theme	post-translational	65:82	arg1	modification					84:95	post-translational modification	65:95	post-translational modification of VDAC2 in pancreatic cancer	65:125	Inflammatory IFIT3 renders chemotherapy resistance by regulating post-translational modification of VDAC2 in pancreatic cancer.
32641986	6	114	theme	knockdown	868:876	arg1	cells					908:912	IFIT3 knockdown and the corresponding knockin cells	862:912	IFIT3 knockdown and the corresponding knockin cells	862:912	Highly metastatic PDAC cell line L3.6pl and patient-derived primary cell TBO368 were used and IFIT3 knockdown and the corresponding knockin cells were established for in vitro studies.
32641986	12	115	theme	apoptosis	1972:1980	arg1	VDAC2					1915:1919	the mitochondrial channel protein VDAC2	1881:1919	the mitochondrial channel protein VDAC2	1881:1919	Co-immunoprecipitation identified a direct interaction between IFIT3 and the mitochondrial channel protein VDAC2, an important regulator of mitochondria-associated apoptosis.
32641986	12	115	theme	apoptosis	1972:1980	arg1	regulator					1935:1943	an important regulator	1922:1943	an important regulator of mitochondria-associated apoptosis	1922:1980	Co-immunoprecipitation identified a direct interaction between IFIT3 and the mitochondrial channel protein VDAC2, an important regulator of mitochondria-associated apoptosis.
32641986	10	116	theme	cells	1625:1629	arg1	resistance					1606:1615	the chemotherapy resistance	1589:1615	the chemotherapy resistance of PDAC cells to gemcitabine, paclitaxel, and FOLFIRINOX regimen treatments, independent of individual chemotherapy regimens	1589:1740	Knockdown of IFIT3 attenuates the chemotherapy resistance of PDAC cells to gemcitabine, paclitaxel, and FOLFIRINOX regimen treatments, independent of individual chemotherapy regimens.
32641986	16	117	theme	conventional	2499:2510	arg1	regimens					2525:2532	conventional chemotherapy regimens	2499:2532	conventional chemotherapy regimens	2499:2532	Targeting IFIT3/VDAC2 may represent a novel strategy to sensitize aggressive forms of pancreatic cancer to conventional chemotherapy regimens.
32641986	12	118	theme	important	1925:1933	arg1	VDAC2					1915:1919	the mitochondrial channel protein VDAC2	1881:1919	the mitochondrial channel protein VDAC2	1881:1919	Co-immunoprecipitation identified a direct interaction between IFIT3 and the mitochondrial channel protein VDAC2, an important regulator of mitochondria-associated apoptosis.
32641986	12	118	theme	important	1925:1933	arg1	regulator					1935:1943	an important regulator	1922:1943	an important regulator of mitochondria-associated apoptosis	1922:1980	Co-immunoprecipitation identified a direct interaction between IFIT3 and the mitochondrial channel protein VDAC2, an important regulator of mitochondria-associated apoptosis.
32641986	10	119	theme	paclitaxel	1647:1656	arg1	treatments					1682:1691	gemcitabine, paclitaxel, and FOLFIRINOX regimen treatments	1634:1691	gemcitabine, paclitaxel, and FOLFIRINOX regimen treatments	1634:1691	Knockdown of IFIT3 attenuates the chemotherapy resistance of PDAC cells to gemcitabine, paclitaxel, and FOLFIRINOX regimen treatments, independent of individual chemotherapy regimens.
29680296	4	0	theme	expression	475:484	arg1	level					486:490	low expression level	471:490	low expression level of miR-485-5p	471:504	In addition, low expression level of miR-485-5p is correlated with tumor progression and poor survival in CRC patients.
29680296	7	1	theme	O-GlcNAcylation	952:966	arg1	level					968:972	the O-GlcNAcylation level	948:972	the O-GlcNAcylation level of Bmi-1 by OGT	948:988	Mechanistically, OGT is a direct target of miR-485-5p, and miR-485-5p could inhibit the O-GlcNAcylation level of Bmi-1 by OGT.
29680296	1	2	theme	many	168:171	arg1	cancers					173:179	many cancers	168:179	many cancers	168:179	Emerging evidences showed that miRNAs are involved in the oncogenesis of many cancers.
29680296	4	3	theme	CRC	564:566	arg1	patients					568:575	CRC patients	564:575	CRC patients	564:575	In addition, low expression level of miR-485-5p is correlated with tumor progression and poor survival in CRC patients.
29680296	4	4	theme	miR-485-5p	495:504	arg1	level					486:490	low expression level	471:490	low expression level of miR-485-5p	471:504	In addition, low expression level of miR-485-5p is correlated with tumor progression and poor survival in CRC patients.
29680296	2	5	theme	further	343:349	arg1	study					351:355	further study	343:355	further study	343:355	Here, miRNA microarray analysis was performed to screen the significant miRNAs involved in the progression of colorectal cancer (CRC), miR-485-5p was chosen for further study.
29680296	6	6	theme	many	850:853	arg1	cancers					855:861	many cancers	850:861	many cancers	850:861	Moreover, our results showed that miR-485-5p inhibits cell proliferation by reducing Bmi-1 protein expression, which has been reported to control the proliferation of many cancers.
29680296	9	7	theme	CRC	1252:1254	arg1	growth					1256:1261	CRC growth	1252:1261	CRC growth	1252:1261	This may give insight into a novel mechanism and therapy of CRC growth.
29680296	2	8	theme	cancer	303:308	arg1	progression					277:287	the progression	273:287	the progression of colorectal cancer (CRC)	273:314	Here, miRNA microarray analysis was performed to screen the significant miRNAs involved in the progression of colorectal cancer (CRC), miR-485-5p was chosen for further study.
29680296	9	9	theme	growth	1256:1261	arg1	therapy					1241:1247	therapy	1241:1247	therapy of CRC growth	1241:1261	This may give insight into a novel mechanism and therapy of CRC growth.
29680296	9	9	theme	growth	1256:1261	arg1	mechanism					1227:1235	a novel mechanism	1219:1235	a novel mechanism	1219:1235	This may give insight into a novel mechanism and therapy of CRC growth.
29680296	5	10	theme	in	587:588	arg1	assays					608:613	in vitro and in vivo assays	587:613	in vitro and in vivo assays	587:613	Based on in vitro and in vivo assays, we found that miR-485-5p significantly inhibits CRC proliferation.
29680296	2	11	theme	colorectal	292:301	arg1	CRC					311:313	CRC	311:313	CRC	311:313	Here, miRNA microarray analysis was performed to screen the significant miRNAs involved in the progression of colorectal cancer (CRC), miR-485-5p was chosen for further study.
29680296	2	11	theme	colorectal	292:301	arg1	cancer					303:308	colorectal cancer	292:308	colorectal cancer (CRC)	292:314	Here, miRNA microarray analysis was performed to screen the significant miRNAs involved in the progression of colorectal cancer (CRC), miR-485-5p was chosen for further study.
29680296	3	12	theme	CRC	428:430	arg1	specimens					432:440	CRC specimens	428:440	CRC specimens	428:440	We found that the expression of miR-485-5p was significantly lower in CRC specimens and cell lines.
29680296	5	13	dep	in	600:601	arg1	vivo					603:606	vivo	603:606	vivo	603:606	Based on in vitro and in vivo assays, we found that miR-485-5p significantly inhibits CRC proliferation.
29680296	4	14	theme	low	471:473	arg1	level					486:490	low expression level	471:490	low expression level of miR-485-5p	471:504	In addition, low expression level of miR-485-5p is correlated with tumor progression and poor survival in CRC patients.
29680296	5	15	theme	in	600:601	arg1	assays					608:613	in vitro and in vivo assays	587:613	in vitro and in vivo assays	587:613	Based on in vitro and in vivo assays, we found that miR-485-5p significantly inhibits CRC proliferation.
29680296	6	16	theme	protein	774:780	arg1	expression					782:791	Bmi-1 protein expression	768:791	Bmi-1 protein expression	768:791	Moreover, our results showed that miR-485-5p inhibits cell proliferation by reducing Bmi-1 protein expression, which has been reported to control the proliferation of many cancers.
29680296	1	17	theme	Emerging	95:102	arg1	evidences					104:112	Emerging evidences	95:112	Emerging evidences	95:112	Emerging evidences showed that miRNAs are involved in the oncogenesis of many cancers.
29680296	4	18	from	survival	552:559	arg1	patients					568:575	CRC patients	564:575	CRC patients	564:575	In addition, low expression level of miR-485-5p is correlated with tumor progression and poor survival in CRC patients.
29680296	6	19	theme	cancers	855:861	arg1	proliferation					833:845	the proliferation	829:845	the proliferation of many cancers	829:861	Moreover, our results showed that miR-485-5p inhibits cell proliferation by reducing Bmi-1 protein expression, which has been reported to control the proliferation of many cancers.
29680296	6	20	theme	Bmi-1	768:772	arg1	expression					782:791	Bmi-1 protein expression	768:791	Bmi-1 protein expression	768:791	Moreover, our results showed that miR-485-5p inhibits cell proliferation by reducing Bmi-1 protein expression, which has been reported to control the proliferation of many cancers.
29680296	8	21	theme	Bmi-1	1163:1167	arg1	O-GlcNAcylation					1126:1140	the O-GlcNAcylation	1122:1140	the O-GlcNAcylation	1122:1140	Overall, these results suggested that as a tumor suppressor, miR-485-5p may regulate CRC cells proliferation, which could regulate the O-GlcNAcylation and the stability of Bmi-1 through targeting OGT.
29680296	8	21	theme	Bmi-1	1163:1167	arg1	stability					1150:1158	the stability	1146:1158	the stability of Bmi-1	1146:1167	Overall, these results suggested that as a tumor suppressor, miR-485-5p may regulate CRC cells proliferation, which could regulate the O-GlcNAcylation and the stability of Bmi-1 through targeting OGT.
29680296	4	22	from	progression	531:541	arg1	patients					568:575	CRC patients	564:575	CRC patients	564:575	In addition, low expression level of miR-485-5p is correlated with tumor progression and poor survival in CRC patients.
29680296	8	23	theme	tumor	1034:1038	arg1	proliferation					1086:1098	CRC cells proliferation	1076:1098	CRC cells proliferation	1076:1098	Overall, these results suggested that as a tumor suppressor, miR-485-5p may regulate CRC cells proliferation, which could regulate the O-GlcNAcylation and the stability of Bmi-1 through targeting OGT.
29680296	8	23	theme	tumor	1034:1038	arg1	suppressor					1040:1049	a tumor suppressor	1032:1049	a tumor suppressor	1032:1049	Overall, these results suggested that as a tumor suppressor, miR-485-5p may regulate CRC cells proliferation, which could regulate the O-GlcNAcylation and the stability of Bmi-1 through targeting OGT.
29680296	2	24	theme	miRNA	188:192	arg1	analysis					205:212	miRNA microarray analysis	188:212	miRNA microarray analysis	188:212	Here, miRNA microarray analysis was performed to screen the significant miRNAs involved in the progression of colorectal cancer (CRC), miR-485-5p was chosen for further study.
29680296	1	25	theme	cancers	173:179	arg1	oncogenesis					153:163	the oncogenesis	149:163	the oncogenesis of many cancers	149:179	Emerging evidences showed that miRNAs are involved in the oncogenesis of many cancers.
29680296	4	26	theme	poor	547:550	arg1	survival					552:559	poor survival	547:559	poor survival	547:559	In addition, low expression level of miR-485-5p is correlated with tumor progression and poor survival in CRC patients.
29680296	2	27	theme	significant	242:252	arg1	miRNAs					254:259	the significant miRNAs	238:259	the significant miRNAs involved in the progression of colorectal cancer (CRC)	238:314	Here, miRNA microarray analysis was performed to screen the significant miRNAs involved in the progression of colorectal cancer (CRC), miR-485-5p was chosen for further study.
29680296	0	28	theme	Bmi-1	43:47	arg1	O-GlcNAcylation					24:38	O-GlcNAcylation	24:38	O-GlcNAcylation of Bmi-1	24:47	MicroRNA-485-5p reduces O-GlcNAcylation of Bmi-1 and inhibits colorectal cancer proliferation.
29680296	3	29	theme	cell	446:449	arg1	lines					451:455	cell lines	446:455	cell lines	446:455	We found that the expression of miR-485-5p was significantly lower in CRC specimens and cell lines.
29680296	0	30	theme	colorectal	62:71	arg1	proliferation					80:92	colorectal cancer proliferation	62:92	colorectal cancer proliferation	62:92	MicroRNA-485-5p reduces O-GlcNAcylation of Bmi-1 and inhibits colorectal cancer proliferation.
29680296	6	31	theme	cell	737:740	arg1	proliferation					742:754	cell proliferation	737:754	cell proliferation	737:754	Moreover, our results showed that miR-485-5p inhibits cell proliferation by reducing Bmi-1 protein expression, which has been reported to control the proliferation of many cancers.
29680296	3	32	theme	miR-485-5p	390:399	arg1	lower					419:423	lower	419:423	lower	419:423	We found that the expression of miR-485-5p was significantly lower in CRC specimens and cell lines.
29680296	3	32	theme	miR-485-5p	390:399	arg1	expression					376:385	the expression	372:385	the expression of miR-485-5p	372:399	We found that the expression of miR-485-5p was significantly lower in CRC specimens and cell lines.
29680296	4	33	theme	tumor	525:529	arg1	progression					531:541	tumor progression	525:541	tumor progression	525:541	In addition, low expression level of miR-485-5p is correlated with tumor progression and poor survival in CRC patients.
29680296	7	34	theme	Bmi-1	977:981	arg1	level					968:972	the O-GlcNAcylation level	948:972	the O-GlcNAcylation level of Bmi-1 by OGT	948:988	Mechanistically, OGT is a direct target of miR-485-5p, and miR-485-5p could inhibit the O-GlcNAcylation level of Bmi-1 by OGT.
29680296	5	35	dep	in	587:588	arg1	vitro					590:594	vitro	590:594	vitro	590:594	Based on in vitro and in vivo assays, we found that miR-485-5p significantly inhibits CRC proliferation.
29680296	8	36	theme	cells	1080:1084	arg1	proliferation					1086:1098	CRC cells proliferation	1076:1098	CRC cells proliferation	1076:1098	Overall, these results suggested that as a tumor suppressor, miR-485-5p may regulate CRC cells proliferation, which could regulate the O-GlcNAcylation and the stability of Bmi-1 through targeting OGT.
29680296	8	36	theme	cells	1080:1084	arg1	suppressor					1040:1049	a tumor suppressor	1032:1049	a tumor suppressor	1032:1049	Overall, these results suggested that as a tumor suppressor, miR-485-5p may regulate CRC cells proliferation, which could regulate the O-GlcNAcylation and the stability of Bmi-1 through targeting OGT.
29680296	7	37	theme	miR-485-5p	907:916	arg1	target					897:902	a direct target	888:902	a direct target of miR-485-5p	888:916	Mechanistically, OGT is a direct target of miR-485-5p, and miR-485-5p could inhibit the O-GlcNAcylation level of Bmi-1 by OGT.
29680296	7	37	theme	miR-485-5p	907:916	arg1	OGT					881:883	OGT	881:883	OGT	881:883	Mechanistically, OGT is a direct target of miR-485-5p, and miR-485-5p could inhibit the O-GlcNAcylation level of Bmi-1 by OGT.
29680296	8	38	theme	CRC	1076:1078	arg1	cells					1080:1084	CRC cells	1076:1084	CRC cells proliferation	1076:1098	Overall, these results suggested that as a tumor suppressor, miR-485-5p may regulate CRC cells proliferation, which could regulate the O-GlcNAcylation and the stability of Bmi-1 through targeting OGT.
29680296	7	39	theme	direct	890:895	arg1	target					897:902	a direct target	888:902	a direct target of miR-485-5p	888:916	Mechanistically, OGT is a direct target of miR-485-5p, and miR-485-5p could inhibit the O-GlcNAcylation level of Bmi-1 by OGT.
29680296	7	39	theme	direct	890:895	arg1	OGT					881:883	OGT	881:883	OGT	881:883	Mechanistically, OGT is a direct target of miR-485-5p, and miR-485-5p could inhibit the O-GlcNAcylation level of Bmi-1 by OGT.
29680296	5	40	theme	CRC	664:666	arg1	proliferation					668:680	CRC proliferation	664:680	CRC proliferation	664:680	Based on in vitro and in vivo assays, we found that miR-485-5p significantly inhibits CRC proliferation.
29680296	9	41	theme	novel	1221:1225	arg1	mechanism					1227:1235	a novel mechanism	1219:1235	a novel mechanism	1219:1235	This may give insight into a novel mechanism and therapy of CRC growth.
29680296	2	42	theme	microarray	194:203	arg1	analysis					205:212	miRNA microarray analysis	188:212	miRNA microarray analysis	188:212	Here, miRNA microarray analysis was performed to screen the significant miRNAs involved in the progression of colorectal cancer (CRC), miR-485-5p was chosen for further study.
29680296	0	43	theme	cancer	73:78	arg1	proliferation					80:92	colorectal cancer proliferation	62:92	colorectal cancer proliferation	62:92	MicroRNA-485-5p reduces O-GlcNAcylation of Bmi-1 and inhibits colorectal cancer proliferation.
31019204	6	0	theme	expression	958:967	arg1	regulation					940:949	transcriptional regulation	924:949	transcriptional regulation of the expression of the key enzyme glutamine: fructose-6-phosphate amidotransferase (GFAT)	924:1041	In addition, we demonstrated that a differentiation factor for the mammary epithelium, CCAAT/enhancer-binding protein B (CEBPB), was involved in Nic-induced hyper-O-GlcNAcylation via transcriptional regulation of the expression of the key enzyme glutamine: fructose-6-phosphate amidotransferase (GFAT) and thus increased the flux through the hexosamine biosynthetic pathway (HBP).
31019204	7	1	theme	transcriptional	1163:1177	arg1	protein					1206:1212	transcriptional repressor C/EBP homologous protein	1163:1212	the transcriptional repressor C/EBP homologous protein (CHOP)	1159:1219	Finally, elevated O-GlcNAcylation of the transcriptional repressor C/EBP homologous protein (CHOP) suppressed its heterodimerization with CEBPB and facilitated the DNA-binding activity of CEBPB, further generating positive feedback that enhanced EMT upon Nic stimulation.
31019204	7	1	theme	transcriptional	1163:1177	arg1	CHOP					1215:1218	CHOP	1215:1218	CHOP	1215:1218	Finally, elevated O-GlcNAcylation of the transcriptional repressor C/EBP homologous protein (CHOP) suppressed its heterodimerization with CEBPB and facilitated the DNA-binding activity of CEBPB, further generating positive feedback that enhanced EMT upon Nic stimulation.
31019204	4	2	theme	cancer	579:584	arg1	cells					586:590	human breast cancer cells	566:590	human breast cancer cells	566:590	Herein, we found that cellular O-GlcNAcylation dramatically increased in human breast cancer cells with EMT activation induced by Nic.
31019204	0	3	theme	epithelial-mesenchymal	72:93	arg1	transition					95:104	epithelial-mesenchymal transition	72:104	epithelial-mesenchymal transition	72:104	Elevation of O-GlcNAc and GFAT expression by nicotine exposure promotes epithelial-mesenchymal transition and invasion in breast cancer cells.
31019204	3	4	from	alterations	372:382	arg1	O-GlcNAcylation					395:409	protein O-GlcNAcylation	387:409	protein O-GlcNAcylation in Nic-mediated tumorigenesis and malignization mechanisms	387:468	However, the alterations in protein O-GlcNAcylation in Nic-mediated tumorigenesis and malignization mechanisms are less well studied.
31019204	6	5	theme	fructose-6-phosphate	998:1017	arg1	GFAT					1037:1040	GFAT	1037:1040	GFAT	1037:1040	In addition, we demonstrated that a differentiation factor for the mammary epithelium, CCAAT/enhancer-binding protein B (CEBPB), was involved in Nic-induced hyper-O-GlcNAcylation via transcriptional regulation of the expression of the key enzyme glutamine: fructose-6-phosphate amidotransferase (GFAT) and thus increased the flux through the hexosamine biosynthetic pathway (HBP).
31019204	6	5	theme	fructose-6-phosphate	998:1017	arg1	amidotransferase					1019:1034	fructose-6-phosphate amidotransferase	998:1034	the key enzyme glutamine: fructose-6-phosphate amidotransferase (GFAT)	972:1041	In addition, we demonstrated that a differentiation factor for the mammary epithelium, CCAAT/enhancer-binding protein B (CEBPB), was involved in Nic-induced hyper-O-GlcNAcylation via transcriptional regulation of the expression of the key enzyme glutamine: fructose-6-phosphate amidotransferase (GFAT) and thus increased the flux through the hexosamine biosynthetic pathway (HBP).
31019204	7	6	theme	CEBPB	1310:1314	arg1	activity					1298:1305	the DNA-binding activity	1282:1305	the DNA-binding activity of CEBPB	1282:1314	Finally, elevated O-GlcNAcylation of the transcriptional repressor C/EBP homologous protein (CHOP) suppressed its heterodimerization with CEBPB and facilitated the DNA-binding activity of CEBPB, further generating positive feedback that enhanced EMT upon Nic stimulation.
31019204	4	7	theme	breast	572:577	arg1	cells					586:590	human breast cancer cells	566:590	human breast cancer cells	566:590	Herein, we found that cellular O-GlcNAcylation dramatically increased in human breast cancer cells with EMT activation induced by Nic.
31019204	5	8	theme	Nic-induced	675:685	arg1	activation					691:700	Nic-induced EMT activation	675:700	Nic-induced EMT activation	675:700	Elevated O-GlcNAcylation subsequently promoted Nic-induced EMT activation and increased cell migratory abbility.
31019204	6	9	theme	protein	851:857	arg1	factor					793:798	a differentiation factor	775:798	a differentiation factor for the mammary epithelium	775:825	In addition, we demonstrated that a differentiation factor for the mammary epithelium, CCAAT/enhancer-binding protein B (CEBPB), was involved in Nic-induced hyper-O-GlcNAcylation via transcriptional regulation of the expression of the key enzyme glutamine: fructose-6-phosphate amidotransferase (GFAT) and thus increased the flux through the hexosamine biosynthetic pathway (HBP).
31019204	6	9	theme	protein	851:857	arg1	CEBPB					862:866	CEBPB	862:866	CEBPB	862:866	In addition, we demonstrated that a differentiation factor for the mammary epithelium, CCAAT/enhancer-binding protein B (CEBPB), was involved in Nic-induced hyper-O-GlcNAcylation via transcriptional regulation of the expression of the key enzyme glutamine: fructose-6-phosphate amidotransferase (GFAT) and thus increased the flux through the hexosamine biosynthetic pathway (HBP).
31019204	6	9	theme	protein	851:857	arg1	B					859:859	CCAAT/enhancer-binding protein B	828:859	CCAAT/enhancer-binding protein B (CEBPB)	828:867	In addition, we demonstrated that a differentiation factor for the mammary epithelium, CCAAT/enhancer-binding protein B (CEBPB), was involved in Nic-induced hyper-O-GlcNAcylation via transcriptional regulation of the expression of the key enzyme glutamine: fructose-6-phosphate amidotransferase (GFAT) and thus increased the flux through the hexosamine biosynthetic pathway (HBP).
31019204	5	10	theme	EMT	687:689	arg1	activation					691:700	Nic-induced EMT activation	675:700	Nic-induced EMT activation	675:700	Elevated O-GlcNAcylation subsequently promoted Nic-induced EMT activation and increased cell migratory abbility.
31019204	6	11	theme	CCAAT/enhancer-binding	828:849	arg1	factor					793:798	a differentiation factor	775:798	a differentiation factor for the mammary epithelium	775:825	In addition, we demonstrated that a differentiation factor for the mammary epithelium, CCAAT/enhancer-binding protein B (CEBPB), was involved in Nic-induced hyper-O-GlcNAcylation via transcriptional regulation of the expression of the key enzyme glutamine: fructose-6-phosphate amidotransferase (GFAT) and thus increased the flux through the hexosamine biosynthetic pathway (HBP).
31019204	6	11	theme	CCAAT/enhancer-binding	828:849	arg1	CEBPB					862:866	CEBPB	862:866	CEBPB	862:866	In addition, we demonstrated that a differentiation factor for the mammary epithelium, CCAAT/enhancer-binding protein B (CEBPB), was involved in Nic-induced hyper-O-GlcNAcylation via transcriptional regulation of the expression of the key enzyme glutamine: fructose-6-phosphate amidotransferase (GFAT) and thus increased the flux through the hexosamine biosynthetic pathway (HBP).
31019204	6	11	theme	CCAAT/enhancer-binding	828:849	arg1	B					859:859	CCAAT/enhancer-binding protein B	828:859	CCAAT/enhancer-binding protein B (CEBPB)	828:867	In addition, we demonstrated that a differentiation factor for the mammary epithelium, CCAAT/enhancer-binding protein B (CEBPB), was involved in Nic-induced hyper-O-GlcNAcylation via transcriptional regulation of the expression of the key enzyme glutamine: fructose-6-phosphate amidotransferase (GFAT) and thus increased the flux through the hexosamine biosynthetic pathway (HBP).
31019204	2	12	theme	tobacco	261:267	arg1	component					248:256	an active component	238:256	an active component of tobacco	238:267	Nicotine (Nic), an active component of tobacco, has been found to induce epithelial-mesenchymal transition (EMT) in breast cancer cells.
31019204	2	12	theme	tobacco	261:267	arg1	Nicotine					222:229	Nicotine	222:229	Nicotine (Nic)	222:235	Nicotine (Nic), an active component of tobacco, has been found to induce epithelial-mesenchymal transition (EMT) in breast cancer cells.
31019204	7	13	theme	positive	1336:1343	arg1	feedback					1345:1352	positive feedback	1336:1352	positive feedback that enhanced EMT upon Nic stimulation	1336:1391	Finally, elevated O-GlcNAcylation of the transcriptional repressor C/EBP homologous protein (CHOP) suppressed its heterodimerization with CEBPB and facilitated the DNA-binding activity of CEBPB, further generating positive feedback that enhanced EMT upon Nic stimulation.
31019204	0	14	theme	breast	122:127	arg1	cells					136:140	breast cancer cells	122:140	breast cancer cells	122:140	Elevation of O-GlcNAc and GFAT expression by nicotine exposure promotes epithelial-mesenchymal transition and invasion in breast cancer cells.
31019204	6	15	theme	transcriptional	924:938	arg1	regulation					940:949	transcriptional regulation	924:949	transcriptional regulation of the expression of the key enzyme glutamine: fructose-6-phosphate amidotransferase (GFAT)	924:1041	In addition, we demonstrated that a differentiation factor for the mammary epithelium, CCAAT/enhancer-binding protein B (CEBPB), was involved in Nic-induced hyper-O-GlcNAcylation via transcriptional regulation of the expression of the key enzyme glutamine: fructose-6-phosphate amidotransferase (GFAT) and thus increased the flux through the hexosamine biosynthetic pathway (HBP).
31019204	7	16	theme	elevated	1131:1138	arg1	O-GlcNAcylation					1140:1154	elevated O-GlcNAcylation	1131:1154	elevated O-GlcNAcylation of the transcriptional repressor C/EBP homologous protein (CHOP)	1131:1219	Finally, elevated O-GlcNAcylation of the transcriptional repressor C/EBP homologous protein (CHOP) suppressed its heterodimerization with CEBPB and facilitated the DNA-binding activity of CEBPB, further generating positive feedback that enhanced EMT upon Nic stimulation.
31019204	7	17	theme	Nic	1377:1379	arg1	stimulation					1381:1391	Nic stimulation	1377:1391	Nic stimulation	1377:1391	Finally, elevated O-GlcNAcylation of the transcriptional repressor C/EBP homologous protein (CHOP) suppressed its heterodimerization with CEBPB and facilitated the DNA-binding activity of CEBPB, further generating positive feedback that enhanced EMT upon Nic stimulation.
31019204	7	18	theme	protein	1206:1212	arg1	O-GlcNAcylation					1140:1154	elevated O-GlcNAcylation	1131:1154	elevated O-GlcNAcylation of the transcriptional repressor C/EBP homologous protein (CHOP)	1131:1219	Finally, elevated O-GlcNAcylation of the transcriptional repressor C/EBP homologous protein (CHOP) suppressed its heterodimerization with CEBPB and facilitated the DNA-binding activity of CEBPB, further generating positive feedback that enhanced EMT upon Nic stimulation.
31019204	3	19	theme	Nic-mediated	414:425	arg1	mechanisms					459:468	Nic-mediated tumorigenesis and malignization mechanisms	414:468	Nic-mediated tumorigenesis and malignization mechanisms	414:468	However, the alterations in protein O-GlcNAcylation in Nic-mediated tumorigenesis and malignization mechanisms are less well studied.
31019204	5	20	theme	Elevated	628:635	arg1	O-GlcNAcylation					637:651	Elevated O-GlcNAcylation	628:651	Elevated O-GlcNAcylation	628:651	Elevated O-GlcNAcylation subsequently promoted Nic-induced EMT activation and increased cell migratory abbility.
31019204	6	21	theme	mammary	808:814	arg1	epithelium					816:825	the mammary epithelium	804:825	the mammary epithelium	804:825	In addition, we demonstrated that a differentiation factor for the mammary epithelium, CCAAT/enhancer-binding protein B (CEBPB), was involved in Nic-induced hyper-O-GlcNAcylation via transcriptional regulation of the expression of the key enzyme glutamine: fructose-6-phosphate amidotransferase (GFAT) and thus increased the flux through the hexosamine biosynthetic pathway (HBP).
31019204	3	22	theme	protein	387:393	arg1	O-GlcNAcylation					395:409	protein O-GlcNAcylation	387:409	protein O-GlcNAcylation in Nic-mediated tumorigenesis and malignization mechanisms	387:468	However, the alterations in protein O-GlcNAcylation in Nic-mediated tumorigenesis and malignization mechanisms are less well studied.
31019204	2	23	theme	cancer	345:350	arg1	cells					352:356	breast cancer cells	338:356	breast cancer cells	338:356	Nicotine (Nic), an active component of tobacco, has been found to induce epithelial-mesenchymal transition (EMT) in breast cancer cells.
31019204	5	24	theme	migratory	721:729	arg1	abbility					731:738	cell migratory abbility	716:738	cell migratory abbility	716:738	Elevated O-GlcNAcylation subsequently promoted Nic-induced EMT activation and increased cell migratory abbility.
31019204	8	25	theme	CEBPB/GFAT-induced	1472:1489	arg1	hyper-O-GlcNAcylation					1491:1511	CEBPB/GFAT-induced hyper-O-GlcNAcylation	1472:1511	CEBPB/GFAT-induced hyper-O-GlcNAcylation that plays a key role in EMT and smoking-mediated breast cancer progression	1472:1587	In conclusion, our results have revealed a new regulatory mechanism involving CEBPB/GFAT-induced hyper-O-GlcNAcylation that plays a key role in EMT and smoking-mediated breast cancer progression.
31019204	6	26	theme	hexosamine	1083:1092	arg1	HBP					1116:1118	HBP	1116:1118	HBP	1116:1118	In addition, we demonstrated that a differentiation factor for the mammary epithelium, CCAAT/enhancer-binding protein B (CEBPB), was involved in Nic-induced hyper-O-GlcNAcylation via transcriptional regulation of the expression of the key enzyme glutamine: fructose-6-phosphate amidotransferase (GFAT) and thus increased the flux through the hexosamine biosynthetic pathway (HBP).
31019204	6	26	theme	hexosamine	1083:1092	arg1	pathway					1107:1113	the hexosamine biosynthetic pathway	1079:1113	the hexosamine biosynthetic pathway (HBP)	1079:1119	In addition, we demonstrated that a differentiation factor for the mammary epithelium, CCAAT/enhancer-binding protein B (CEBPB), was involved in Nic-induced hyper-O-GlcNAcylation via transcriptional regulation of the expression of the key enzyme glutamine: fructose-6-phosphate amidotransferase (GFAT) and thus increased the flux through the hexosamine biosynthetic pathway (HBP).
31019204	3	27	theme	malignization	445:457	arg1	mechanisms					459:468	Nic-mediated tumorigenesis and malignization mechanisms	414:468	Nic-mediated tumorigenesis and malignization mechanisms	414:468	However, the alterations in protein O-GlcNAcylation in Nic-mediated tumorigenesis and malignization mechanisms are less well studied.
31019204	0	28	theme	O-GlcNAc	13:20	arg1	Elevation					0:8	Elevation	0:8	Elevation of O-GlcNAc and GFAT expression by nicotine exposure	0:61	Elevation of O-GlcNAc and GFAT expression by nicotine exposure promotes epithelial-mesenchymal transition and invasion in breast cancer cells.
31019204	4	29	theme	human	566:570	arg1	cells					586:590	human breast cancer cells	566:590	human breast cancer cells	566:590	Herein, we found that cellular O-GlcNAcylation dramatically increased in human breast cancer cells with EMT activation induced by Nic.
31019204	0	30	theme	cancer	129:134	arg1	cells					136:140	breast cancer cells	122:140	breast cancer cells	122:140	Elevation of O-GlcNAc and GFAT expression by nicotine exposure promotes epithelial-mesenchymal transition and invasion in breast cancer cells.
31019204	0	31	from	transition	95:104	arg1	cells					136:140	breast cancer cells	122:140	breast cancer cells	122:140	Elevation of O-GlcNAc and GFAT expression by nicotine exposure promotes epithelial-mesenchymal transition and invasion in breast cancer cells.
31019204	8	32	theme	new	1437:1439	arg1	mechanism					1452:1460	a new regulatory mechanism	1435:1460	a new regulatory mechanism involving CEBPB/GFAT-induced hyper-O-GlcNAcylation that plays a key role in EMT and smoking-mediated breast cancer progression	1435:1587	In conclusion, our results have revealed a new regulatory mechanism involving CEBPB/GFAT-induced hyper-O-GlcNAcylation that plays a key role in EMT and smoking-mediated breast cancer progression.
31019204	6	33	theme	biosynthetic	1094:1105	arg1	HBP					1116:1118	HBP	1116:1118	HBP	1116:1118	In addition, we demonstrated that a differentiation factor for the mammary epithelium, CCAAT/enhancer-binding protein B (CEBPB), was involved in Nic-induced hyper-O-GlcNAcylation via transcriptional regulation of the expression of the key enzyme glutamine: fructose-6-phosphate amidotransferase (GFAT) and thus increased the flux through the hexosamine biosynthetic pathway (HBP).
31019204	6	33	theme	biosynthetic	1094:1105	arg1	pathway					1107:1113	the hexosamine biosynthetic pathway	1079:1113	the hexosamine biosynthetic pathway (HBP)	1079:1119	In addition, we demonstrated that a differentiation factor for the mammary epithelium, CCAAT/enhancer-binding protein B (CEBPB), was involved in Nic-induced hyper-O-GlcNAcylation via transcriptional regulation of the expression of the key enzyme glutamine: fructose-6-phosphate amidotransferase (GFAT) and thus increased the flux through the hexosamine biosynthetic pathway (HBP).
31019204	0	34	theme	expression	31:40	arg1	Elevation					0:8	Elevation	0:8	Elevation of O-GlcNAc and GFAT expression by nicotine exposure	0:61	Elevation of O-GlcNAc and GFAT expression by nicotine exposure promotes epithelial-mesenchymal transition and invasion in breast cancer cells.
31019204	1	35	theme	breast	207:212	arg1	cancer					214:219	breast cancer	207:219	breast cancer	207:219	Cigarette smoking has been shown to be a carcinogenic factor in breast cancer.
31019204	7	36	with	heterodimerization	1236:1253	arg1	CEBPB					1260:1264	CEBPB	1260:1264	CEBPB	1260:1264	Finally, elevated O-GlcNAcylation of the transcriptional repressor C/EBP homologous protein (CHOP) suppressed its heterodimerization with CEBPB and facilitated the DNA-binding activity of CEBPB, further generating positive feedback that enhanced EMT upon Nic stimulation.
31019204	1	37	theme	carcinogenic	184:195	arg1	smoking					153:159	Cigarette smoking	143:159	Cigarette smoking	143:159	Cigarette smoking has been shown to be a carcinogenic factor in breast cancer.
31019204	1	37	theme	carcinogenic	184:195	arg1	factor					197:202	a carcinogenic factor	182:202	a carcinogenic factor in breast cancer	182:219	Cigarette smoking has been shown to be a carcinogenic factor in breast cancer.
31019204	3	38	theme	tumorigenesis	427:439	arg1	mechanisms					459:468	Nic-mediated tumorigenesis and malignization mechanisms	414:468	Nic-mediated tumorigenesis and malignization mechanisms	414:468	However, the alterations in protein O-GlcNAcylation in Nic-mediated tumorigenesis and malignization mechanisms are less well studied.
31019204	0	39	theme	GFAT	26:29	arg1	expression					31:40	GFAT expression	26:40	GFAT expression	26:40	Elevation of O-GlcNAc and GFAT expression by nicotine exposure promotes epithelial-mesenchymal transition and invasion in breast cancer cells.
31019204	6	40	theme	glutamine	987:995	arg1	expression					958:967	the expression	954:967	the expression of the key enzyme glutamine: fructose-6-phosphate amidotransferase (GFAT)	954:1041	In addition, we demonstrated that a differentiation factor for the mammary epithelium, CCAAT/enhancer-binding protein B (CEBPB), was involved in Nic-induced hyper-O-GlcNAcylation via transcriptional regulation of the expression of the key enzyme glutamine: fructose-6-phosphate amidotransferase (GFAT) and thus increased the flux through the hexosamine biosynthetic pathway (HBP).
31019204	6	41	dep	glutamine	987:995	arg1	GFAT					1037:1040	GFAT	1037:1040	GFAT	1037:1040	In addition, we demonstrated that a differentiation factor for the mammary epithelium, CCAAT/enhancer-binding protein B (CEBPB), was involved in Nic-induced hyper-O-GlcNAcylation via transcriptional regulation of the expression of the key enzyme glutamine: fructose-6-phosphate amidotransferase (GFAT) and thus increased the flux through the hexosamine biosynthetic pathway (HBP).
31019204	6	41	dep	glutamine	987:995	arg1	amidotransferase					1019:1034	fructose-6-phosphate amidotransferase	998:1034	the key enzyme glutamine: fructose-6-phosphate amidotransferase (GFAT)	972:1041	In addition, we demonstrated that a differentiation factor for the mammary epithelium, CCAAT/enhancer-binding protein B (CEBPB), was involved in Nic-induced hyper-O-GlcNAcylation via transcriptional regulation of the expression of the key enzyme glutamine: fructose-6-phosphate amidotransferase (GFAT) and thus increased the flux through the hexosamine biosynthetic pathway (HBP).
31019204	0	42	theme	nicotine	45:52	arg1	exposure					54:61	nicotine exposure	45:61	nicotine exposure	45:61	Elevation of O-GlcNAc and GFAT expression by nicotine exposure promotes epithelial-mesenchymal transition and invasion in breast cancer cells.
31019204	6	43	theme	enzyme	980:985	arg1	glutamine					987:995	the key enzyme glutamine: fructose-6-phosphate amidotransferase (GFAT)	972:1041	the key enzyme glutamine: fructose-6-phosphate amidotransferase (GFAT)	972:1041	In addition, we demonstrated that a differentiation factor for the mammary epithelium, CCAAT/enhancer-binding protein B (CEBPB), was involved in Nic-induced hyper-O-GlcNAcylation via transcriptional regulation of the expression of the key enzyme glutamine: fructose-6-phosphate amidotransferase (GFAT) and thus increased the flux through the hexosamine biosynthetic pathway (HBP).
31019204	6	44	theme	Nic-induced	886:896	arg1	hyper-O-GlcNAcylation					898:918	Nic-induced hyper-O-GlcNAcylation	886:918	Nic-induced hyper-O-GlcNAcylation	886:918	In addition, we demonstrated that a differentiation factor for the mammary epithelium, CCAAT/enhancer-binding protein B (CEBPB), was involved in Nic-induced hyper-O-GlcNAcylation via transcriptional regulation of the expression of the key enzyme glutamine: fructose-6-phosphate amidotransferase (GFAT) and thus increased the flux through the hexosamine biosynthetic pathway (HBP).
31019204	6	45	theme	differentiation	777:791	arg1	B					859:859	CCAAT/enhancer-binding protein B	828:859	CCAAT/enhancer-binding protein B (CEBPB)	828:867	In addition, we demonstrated that a differentiation factor for the mammary epithelium, CCAAT/enhancer-binding protein B (CEBPB), was involved in Nic-induced hyper-O-GlcNAcylation via transcriptional regulation of the expression of the key enzyme glutamine: fructose-6-phosphate amidotransferase (GFAT) and thus increased the flux through the hexosamine biosynthetic pathway (HBP).
31019204	6	45	theme	differentiation	777:791	arg1	factor					793:798	a differentiation factor	775:798	a differentiation factor for the mammary epithelium	775:825	In addition, we demonstrated that a differentiation factor for the mammary epithelium, CCAAT/enhancer-binding protein B (CEBPB), was involved in Nic-induced hyper-O-GlcNAcylation via transcriptional regulation of the expression of the key enzyme glutamine: fructose-6-phosphate amidotransferase (GFAT) and thus increased the flux through the hexosamine biosynthetic pathway (HBP).
31019204	7	46	theme	homologous	1195:1204	arg1	protein					1206:1212	transcriptional repressor C/EBP homologous protein	1163:1212	the transcriptional repressor C/EBP homologous protein (CHOP)	1159:1219	Finally, elevated O-GlcNAcylation of the transcriptional repressor C/EBP homologous protein (CHOP) suppressed its heterodimerization with CEBPB and facilitated the DNA-binding activity of CEBPB, further generating positive feedback that enhanced EMT upon Nic stimulation.
31019204	7	46	theme	homologous	1195:1204	arg1	CHOP					1215:1218	CHOP	1215:1218	CHOP	1215:1218	Finally, elevated O-GlcNAcylation of the transcriptional repressor C/EBP homologous protein (CHOP) suppressed its heterodimerization with CEBPB and facilitated the DNA-binding activity of CEBPB, further generating positive feedback that enhanced EMT upon Nic stimulation.
31019204	6	47	theme	key	976:978	arg1	glutamine					987:995	the key enzyme glutamine: fructose-6-phosphate amidotransferase (GFAT)	972:1041	the key enzyme glutamine: fructose-6-phosphate amidotransferase (GFAT)	972:1041	In addition, we demonstrated that a differentiation factor for the mammary epithelium, CCAAT/enhancer-binding protein B (CEBPB), was involved in Nic-induced hyper-O-GlcNAcylation via transcriptional regulation of the expression of the key enzyme glutamine: fructose-6-phosphate amidotransferase (GFAT) and thus increased the flux through the hexosamine biosynthetic pathway (HBP).
31019204	8	48	theme	breast	1563:1568	arg1	progression					1577:1587	smoking-mediated breast cancer progression	1546:1587	smoking-mediated breast cancer progression	1546:1587	In conclusion, our results have revealed a new regulatory mechanism involving CEBPB/GFAT-induced hyper-O-GlcNAcylation that plays a key role in EMT and smoking-mediated breast cancer progression.
31019204	7	49	theme	repressor	1179:1187	arg1	protein					1206:1212	transcriptional repressor C/EBP homologous protein	1163:1212	the transcriptional repressor C/EBP homologous protein (CHOP)	1159:1219	Finally, elevated O-GlcNAcylation of the transcriptional repressor C/EBP homologous protein (CHOP) suppressed its heterodimerization with CEBPB and facilitated the DNA-binding activity of CEBPB, further generating positive feedback that enhanced EMT upon Nic stimulation.
31019204	7	49	theme	repressor	1179:1187	arg1	CHOP					1215:1218	CHOP	1215:1218	CHOP	1215:1218	Finally, elevated O-GlcNAcylation of the transcriptional repressor C/EBP homologous protein (CHOP) suppressed its heterodimerization with CEBPB and facilitated the DNA-binding activity of CEBPB, further generating positive feedback that enhanced EMT upon Nic stimulation.
31019204	1	50	from	factor	197:202	arg1	cancer					214:219	breast cancer	207:219	breast cancer	207:219	Cigarette smoking has been shown to be a carcinogenic factor in breast cancer.
31019204	4	51	theme	cellular	515:522	arg1	O-GlcNAcylation					524:538	cellular O-GlcNAcylation	515:538	cellular O-GlcNAcylation	515:538	Herein, we found that cellular O-GlcNAcylation dramatically increased in human breast cancer cells with EMT activation induced by Nic.
31019204	8	52	theme	smoking-mediated	1546:1561	arg1	progression					1577:1587	smoking-mediated breast cancer progression	1546:1587	smoking-mediated breast cancer progression	1546:1587	In conclusion, our results have revealed a new regulatory mechanism involving CEBPB/GFAT-induced hyper-O-GlcNAcylation that plays a key role in EMT and smoking-mediated breast cancer progression.
31019204	2	53	theme	active	241:246	arg1	component					248:256	an active component	238:256	an active component of tobacco	238:267	Nicotine (Nic), an active component of tobacco, has been found to induce epithelial-mesenchymal transition (EMT) in breast cancer cells.
31019204	2	53	theme	active	241:246	arg1	Nicotine					222:229	Nicotine	222:229	Nicotine (Nic)	222:235	Nicotine (Nic), an active component of tobacco, has been found to induce epithelial-mesenchymal transition (EMT) in breast cancer cells.
31019204	2	54	theme	epithelial-mesenchymal	295:316	arg1	transition					318:327	epithelial-mesenchymal transition	295:327	epithelial-mesenchymal transition (EMT)	295:333	Nicotine (Nic), an active component of tobacco, has been found to induce epithelial-mesenchymal transition (EMT) in breast cancer cells.
31019204	2	54	theme	epithelial-mesenchymal	295:316	arg1	EMT					330:332	EMT	330:332	EMT	330:332	Nicotine (Nic), an active component of tobacco, has been found to induce epithelial-mesenchymal transition (EMT) in breast cancer cells.
31019204	8	55	theme	regulatory	1441:1450	arg1	mechanism					1452:1460	a new regulatory mechanism	1435:1460	a new regulatory mechanism involving CEBPB/GFAT-induced hyper-O-GlcNAcylation that plays a key role in EMT and smoking-mediated breast cancer progression	1435:1587	In conclusion, our results have revealed a new regulatory mechanism involving CEBPB/GFAT-induced hyper-O-GlcNAcylation that plays a key role in EMT and smoking-mediated breast cancer progression.
31019204	5	56	theme	cell	716:719	arg1	abbility					731:738	cell migratory abbility	716:738	cell migratory abbility	716:738	Elevated O-GlcNAcylation subsequently promoted Nic-induced EMT activation and increased cell migratory abbility.
31019204	0	57	from	invasion	110:117	arg1	cells					136:140	breast cancer cells	122:140	breast cancer cells	122:140	Elevation of O-GlcNAc and GFAT expression by nicotine exposure promotes epithelial-mesenchymal transition and invasion in breast cancer cells.
31019204	1	58	theme	Cigarette	143:151	arg1	factor					197:202	a carcinogenic factor	182:202	a carcinogenic factor in breast cancer	182:219	Cigarette smoking has been shown to be a carcinogenic factor in breast cancer.
31019204	1	58	theme	Cigarette	143:151	arg1	smoking					153:159	Cigarette smoking	143:159	Cigarette smoking	143:159	Cigarette smoking has been shown to be a carcinogenic factor in breast cancer.
31019204	4	59	theme	EMT	597:599	arg1	activation					601:610	EMT activation	597:610	EMT activation induced by Nic	597:625	Herein, we found that cellular O-GlcNAcylation dramatically increased in human breast cancer cells with EMT activation induced by Nic.
31019204	7	60	theme	DNA-binding	1286:1296	arg1	activity					1298:1305	the DNA-binding activity	1282:1305	the DNA-binding activity of CEBPB	1282:1314	Finally, elevated O-GlcNAcylation of the transcriptional repressor C/EBP homologous protein (CHOP) suppressed its heterodimerization with CEBPB and facilitated the DNA-binding activity of CEBPB, further generating positive feedback that enhanced EMT upon Nic stimulation.
31019204	8	61	theme	cancer	1570:1575	arg1	progression					1577:1587	smoking-mediated breast cancer progression	1546:1587	smoking-mediated breast cancer progression	1546:1587	In conclusion, our results have revealed a new regulatory mechanism involving CEBPB/GFAT-induced hyper-O-GlcNAcylation that plays a key role in EMT and smoking-mediated breast cancer progression.
31019204	8	62	theme	key	1526:1528	arg1	role					1530:1533	a key role	1524:1533	a key role	1524:1533	In conclusion, our results have revealed a new regulatory mechanism involving CEBPB/GFAT-induced hyper-O-GlcNAcylation that plays a key role in EMT and smoking-mediated breast cancer progression.
31019204	3	63	from	O-GlcNAcylation	395:409	arg1	mechanisms					459:468	Nic-mediated tumorigenesis and malignization mechanisms	414:468	Nic-mediated tumorigenesis and malignization mechanisms	414:468	However, the alterations in protein O-GlcNAcylation in Nic-mediated tumorigenesis and malignization mechanisms are less well studied.
31019204	2	64	theme	breast	338:343	arg1	cells					352:356	breast cancer cells	338:356	breast cancer cells	338:356	Nicotine (Nic), an active component of tobacco, has been found to induce epithelial-mesenchymal transition (EMT) in breast cancer cells.
31019204	7	65	theme	C/EBP	1189:1193	arg1	protein					1206:1212	transcriptional repressor C/EBP homologous protein	1163:1212	the transcriptional repressor C/EBP homologous protein (CHOP)	1159:1219	Finally, elevated O-GlcNAcylation of the transcriptional repressor C/EBP homologous protein (CHOP) suppressed its heterodimerization with CEBPB and facilitated the DNA-binding activity of CEBPB, further generating positive feedback that enhanced EMT upon Nic stimulation.
31019204	7	65	theme	C/EBP	1189:1193	arg1	CHOP					1215:1218	CHOP	1215:1218	CHOP	1215:1218	Finally, elevated O-GlcNAcylation of the transcriptional repressor C/EBP homologous protein (CHOP) suppressed its heterodimerization with CEBPB and facilitated the DNA-binding activity of CEBPB, further generating positive feedback that enhanced EMT upon Nic stimulation.
20676906	2	0	theme	stress	559:564	arg1	models					544:549	models	544:549	models of heat stress, oxidative stress, endoplasmic reticulum (ER) stress, hypoxia, ischemia reperfusion injury, and trauma hemorrhage	544:678	Numerous forms of cellular injury lead to elevated levels of O-GlcNAc in both in vivo and in vitro models, and elevation of O-GlcNAc levels before, or immediately after, the induction of cellular injury is protective in models of heat stress, oxidative stress, endoplasmic reticulum (ER) stress, hypoxia, ischemia reperfusion injury, and trauma hemorrhage.
20676906	2	1	theme	elevated	366:373	arg1	levels					375:380	elevated levels	366:380	elevated levels of O-GlcNAc in both in vivo and in vitro models, and elevation of O-GlcNAc levels before	366:469	Numerous forms of cellular injury lead to elevated levels of O-GlcNAc in both in vivo and in vitro models, and elevation of O-GlcNAc levels before, or immediately after, the induction of cellular injury is protective in models of heat stress, oxidative stress, endoplasmic reticulum (ER) stress, hypoxia, ischemia reperfusion injury, and trauma hemorrhage.
20676906	1	2	theme	dynamic	256:262	arg1	modification					297:308	a dynamic and essential post-translational modification	254:308	a dynamic and essential post-translational modification of metazoans	254:321	The modification of nuclear, mitochondrial, and cytoplasmic proteins by O-linked β-N-acetylglucosamine (O-GlcNAc) is a dynamic and essential post-translational modification of metazoans.
20676906	1	2	theme	dynamic	256:262	arg1	modification					141:152	The modification	137:152	The modification of nuclear, mitochondrial, and cytoplasmic proteins by O-linked β-N-acetylglucosamine (O-GlcNAc)	137:249	The modification of nuclear, mitochondrial, and cytoplasmic proteins by O-linked β-N-acetylglucosamine (O-GlcNAc) is a dynamic and essential post-translational modification of metazoans.
20676906	2	3	theme	oxidative	567:575	arg1	stress					577:582	oxidative stress	567:582	oxidative stress	567:582	Numerous forms of cellular injury lead to elevated levels of O-GlcNAc in both in vivo and in vitro models, and elevation of O-GlcNAc levels before, or immediately after, the induction of cellular injury is protective in models of heat stress, oxidative stress, endoplasmic reticulum (ER) stress, hypoxia, ischemia reperfusion injury, and trauma hemorrhage.
20676906	1	4	theme	essential	268:276	arg1	modification					297:308	a dynamic and essential post-translational modification	254:308	a dynamic and essential post-translational modification of metazoans	254:321	The modification of nuclear, mitochondrial, and cytoplasmic proteins by O-linked β-N-acetylglucosamine (O-GlcNAc) is a dynamic and essential post-translational modification of metazoans.
20676906	1	4	theme	essential	268:276	arg1	modification					141:152	The modification	137:152	The modification of nuclear, mitochondrial, and cytoplasmic proteins by O-linked β-N-acetylglucosamine (O-GlcNAc)	137:249	The modification of nuclear, mitochondrial, and cytoplasmic proteins by O-linked β-N-acetylglucosamine (O-GlcNAc) is a dynamic and essential post-translational modification of metazoans.
20676906	2	5	theme	ER	608:609	arg1	stress					612:617	endoplasmic reticulum (ER) stress	585:617	endoplasmic reticulum (ER) stress	585:617	Numerous forms of cellular injury lead to elevated levels of O-GlcNAc in both in vivo and in vitro models, and elevation of O-GlcNAc levels before, or immediately after, the induction of cellular injury is protective in models of heat stress, oxidative stress, endoplasmic reticulum (ER) stress, hypoxia, ischemia reperfusion injury, and trauma hemorrhage.
20676906	8	6	theme	cellular	1615:1622	arg1	stress					1624:1629	cellular stress	1615:1629	cellular stress	1615:1629	Supporting this hypothesis, we have shown that DNA-PK is O-GlcNAc modified in response to numerous forms of cellular stress.
20676906	7	7	theme	protein	1378:1384	arg1	kinase					1386:1391	double-stranded DNA-dependent protein kinase	1348:1391	double-stranded DNA-dependent protein kinase (PK)	1348:1396	Many of these proteins bind double-stranded DNA-dependent protein kinase (PK), or double-stranded DNA breaks, suggesting a role for O-GlcNAc in regulating DNA damage signaling or repair.
20676906	7	7	theme	protein	1378:1384	arg1	PK					1394:1395	PK	1394:1395	PK	1394:1395	Many of these proteins bind double-stranded DNA-dependent protein kinase (PK), or double-stranded DNA breaks, suggesting a role for O-GlcNAc in regulating DNA damage signaling or repair.
20676906	2	8	theme	reticulum	597:605	arg1	stress					612:617	endoplasmic reticulum (ER) stress	585:617	endoplasmic reticulum (ER) stress	585:617	Numerous forms of cellular injury lead to elevated levels of O-GlcNAc in both in vivo and in vitro models, and elevation of O-GlcNAc levels before, or immediately after, the induction of cellular injury is protective in models of heat stress, oxidative stress, endoplasmic reticulum (ER) stress, hypoxia, ischemia reperfusion injury, and trauma hemorrhage.
20676906	5	9	used	used	999:1002	arg2	we					991:992	we	991:992	we	991:992	In order to determine how O-GlcNAc modulates stress tolerance in these models we have used stable isotope labeling with amino acids in cell culture to determine the identity of proteins that undergo O-GlcNAcylation in response to heat shock.
20676906	1	10	theme	cytoplasmic	185:195	arg1	proteins					197:204	nuclear, mitochondrial, and cytoplasmic proteins	157:204	nuclear, mitochondrial, and cytoplasmic proteins	157:204	The modification of nuclear, mitochondrial, and cytoplasmic proteins by O-linked β-N-acetylglucosamine (O-GlcNAc) is a dynamic and essential post-translational modification of metazoans.
20676906	8	11	dep	forms	1606:1610	arg1	response					1585:1592	response	1585:1592	response	1585:1592	Supporting this hypothesis, we have shown that DNA-PK is O-GlcNAc modified in response to numerous forms of cellular stress.
20676906	4	12	theme	enhanced	864:871	arg1	survival					878:885	enhanced cell survival	864:885	enhanced cell survival	864:885	However, the molecular mechanism(s) by which O-GlcNAc regulates protein function leading to enhanced cell survival have not been identified.
20676906	0	13	theme	cellular	118:125	arg1	pathways					127:134	other cellular pathways	112:134	other cellular pathways	112:134	The dynamic stress-induced "O-GlcNAc-ome" highlights functions for O-GlcNAc in regulating DNA damage/repair and other cellular pathways.
20676906	7	14	dep	damage	1479:1484	arg1	signaling					1486:1494	signaling	1486:1494	signaling	1486:1494	Many of these proteins bind double-stranded DNA-dependent protein kinase (PK), or double-stranded DNA breaks, suggesting a role for O-GlcNAc in regulating DNA damage signaling or repair.
20676906	6	15	theme	diverse	1178:1184	arg1	functions					1186:1194	diverse functions	1178:1194	diverse functions	1178:1194	Numerous proteins with diverse functions were identified, including NF-90, RuvB-like 1 (Tip49α), RuvB-like 2 (Tip49β), and several COPII vesicle transport proteins.
20676906	5	16	theme	heat	1143:1146	arg1	shock					1148:1152	heat shock	1143:1152	heat shock	1143:1152	In order to determine how O-GlcNAc modulates stress tolerance in these models we have used stable isotope labeling with amino acids in cell culture to determine the identity of proteins that undergo O-GlcNAcylation in response to heat shock.
20676906	4	17	theme	protein	836:842	arg1	function					844:851	protein function	836:851	protein function leading to enhanced cell survival	836:885	However, the molecular mechanism(s) by which O-GlcNAc regulates protein function leading to enhanced cell survival have not been identified.
20676906	2	18	theme	trauma	662:667	arg1	hemorrhage					669:678	trauma hemorrhage	662:678	trauma hemorrhage	662:678	Numerous forms of cellular injury lead to elevated levels of O-GlcNAc in both in vivo and in vitro models, and elevation of O-GlcNAc levels before, or immediately after, the induction of cellular injury is protective in models of heat stress, oxidative stress, endoplasmic reticulum (ER) stress, hypoxia, ischemia reperfusion injury, and trauma hemorrhage.
20676906	3	19	theme	stress	755:760	arg1	response					762:769	the cellular stress response	742:769	the cellular stress response	742:769	Together, these data suggest that O-GlcNAc is a regulator of the cellular stress response.
20676906	6	20	theme	vesicle	1292:1298	arg1	proteins					1310:1317	several COPII vesicle transport proteins	1278:1317	several COPII vesicle transport proteins	1278:1317	Numerous proteins with diverse functions were identified, including NF-90, RuvB-like 1 (Tip49α), RuvB-like 2 (Tip49β), and several COPII vesicle transport proteins.
20676906	1	21	link	O-linked	209:216	arg1	O-GlcNAc					241:248	O-GlcNAc	241:248	O-GlcNAc	241:248	The modification of nuclear, mitochondrial, and cytoplasmic proteins by O-linked β-N-acetylglucosamine (O-GlcNAc) is a dynamic and essential post-translational modification of metazoans.
20676906	1	21	link	O-linked	209:216	arg1	β-N-acetylglucosamine					218:238	O-linked β-N-acetylglucosamine	209:238	O-linked β-N-acetylglucosamine (O-GlcNAc)	209:249	The modification of nuclear, mitochondrial, and cytoplasmic proteins by O-linked β-N-acetylglucosamine (O-GlcNAc) is a dynamic and essential post-translational modification of metazoans.
20676906	6	22	theme	several	1278:1284	arg1	proteins					1310:1317	several COPII vesicle transport proteins	1278:1317	several COPII vesicle transport proteins	1278:1317	Numerous proteins with diverse functions were identified, including NF-90, RuvB-like 1 (Tip49α), RuvB-like 2 (Tip49β), and several COPII vesicle transport proteins.
20676906	7	23	theme	DNA	1475:1477	arg1	damage					1479:1484	DNA damage signaling or repair	1475:1504	damage	1479:1484	Many of these proteins bind double-stranded DNA-dependent protein kinase (PK), or double-stranded DNA breaks, suggesting a role for O-GlcNAc in regulating DNA damage signaling or repair.
20676906	2	24	theme	cellular	511:518	arg1	injury					520:525	cellular injury	511:525	cellular injury	511:525	Numerous forms of cellular injury lead to elevated levels of O-GlcNAc in both in vivo and in vitro models, and elevation of O-GlcNAc levels before, or immediately after, the induction of cellular injury is protective in models of heat stress, oxidative stress, endoplasmic reticulum (ER) stress, hypoxia, ischemia reperfusion injury, and trauma hemorrhage.
20676906	2	25	from	elevation	435:443	arg1	models					423:428	both in vivo and in vitro models	397:428	both in vivo and in vitro models	397:428	Numerous forms of cellular injury lead to elevated levels of O-GlcNAc in both in vivo and in vitro models, and elevation of O-GlcNAc levels before, or immediately after, the induction of cellular injury is protective in models of heat stress, oxidative stress, endoplasmic reticulum (ER) stress, hypoxia, ischemia reperfusion injury, and trauma hemorrhage.
20676906	0	26	theme	DNA	90:92	arg1	damage/repair					94:106	DNA damage/repair	90:106	DNA damage/repair	90:106	The dynamic stress-induced "O-GlcNAc-ome" highlights functions for O-GlcNAc in regulating DNA damage/repair and other cellular pathways.
20676906	5	27	theme	amino	1033:1037	arg1	acids					1039:1043	amino acids	1033:1043	amino acids	1033:1043	In order to determine how O-GlcNAc modulates stress tolerance in these models we have used stable isotope labeling with amino acids in cell culture to determine the identity of proteins that undergo O-GlcNAcylation in response to heat shock.
20676906	2	28	theme	reperfusion	638:648	arg1	injury					650:655	ischemia reperfusion injury	629:655	ischemia reperfusion injury	629:655	Numerous forms of cellular injury lead to elevated levels of O-GlcNAc in both in vivo and in vitro models, and elevation of O-GlcNAc levels before, or immediately after, the induction of cellular injury is protective in models of heat stress, oxidative stress, endoplasmic reticulum (ER) stress, hypoxia, ischemia reperfusion injury, and trauma hemorrhage.
20676906	1	29	theme	post-translational	278:295	arg1	modification					297:308	a dynamic and essential post-translational modification	254:308	a dynamic and essential post-translational modification of metazoans	254:321	The modification of nuclear, mitochondrial, and cytoplasmic proteins by O-linked β-N-acetylglucosamine (O-GlcNAc) is a dynamic and essential post-translational modification of metazoans.
20676906	1	29	theme	post-translational	278:295	arg1	modification					141:152	The modification	137:152	The modification of nuclear, mitochondrial, and cytoplasmic proteins by O-linked β-N-acetylglucosamine (O-GlcNAc)	137:249	The modification of nuclear, mitochondrial, and cytoplasmic proteins by O-linked β-N-acetylglucosamine (O-GlcNAc) is a dynamic and essential post-translational modification of metazoans.
20676906	4	30	theme	mechanism	795:803	arg1	s					805:805	the molecular mechanism(s)	781:806	the molecular mechanism(s) by which O-GlcNAc regulates protein function leading to enhanced cell survival	781:885	However, the molecular mechanism(s) by which O-GlcNAc regulates protein function leading to enhanced cell survival have not been identified.
20676906	0	31	theme	stress-induced	12:25	arg1	"					40:40	The dynamic stress-induced "O-GlcNAc-ome"	0:40	The dynamic stress-induced "O-GlcNAc-ome"	0:40	The dynamic stress-induced "O-GlcNAc-ome" highlights functions for O-GlcNAc in regulating DNA damage/repair and other cellular pathways.
20676906	2	32	dep	in	414:415	arg1	vitro					417:421	vitro	417:421	vitro	417:421	Numerous forms of cellular injury lead to elevated levels of O-GlcNAc in both in vivo and in vitro models, and elevation of O-GlcNAc levels before, or immediately after, the induction of cellular injury is protective in models of heat stress, oxidative stress, endoplasmic reticulum (ER) stress, hypoxia, ischemia reperfusion injury, and trauma hemorrhage.
20676906	2	33	theme	in	414:415	arg1	models					423:428	both in vivo and in vitro models	397:428	both in vivo and in vitro models	397:428	Numerous forms of cellular injury lead to elevated levels of O-GlcNAc in both in vivo and in vitro models, and elevation of O-GlcNAc levels before, or immediately after, the induction of cellular injury is protective in models of heat stress, oxidative stress, endoplasmic reticulum (ER) stress, hypoxia, ischemia reperfusion injury, and trauma hemorrhage.
20676906	0	34	theme	O-GlcNAc-ome	28:39	arg1	"					40:40	The dynamic stress-induced "O-GlcNAc-ome"	0:40	The dynamic stress-induced "O-GlcNAc-ome"	0:40	The dynamic stress-induced "O-GlcNAc-ome" highlights functions for O-GlcNAc in regulating DNA damage/repair and other cellular pathways.
20676906	2	35	theme	levels	457:462	arg1	elevation					435:443	elevation	435:443	elevation	435:443	Numerous forms of cellular injury lead to elevated levels of O-GlcNAc in both in vivo and in vitro models, and elevation of O-GlcNAc levels before, or immediately after, the induction of cellular injury is protective in models of heat stress, oxidative stress, endoplasmic reticulum (ER) stress, hypoxia, ischemia reperfusion injury, and trauma hemorrhage.
20676906	2	35	theme	levels	457:462	arg1	O-GlcNAc					385:392	O-GlcNAc	385:392	O-GlcNAc in both in vivo and in vitro models	385:428	Numerous forms of cellular injury lead to elevated levels of O-GlcNAc in both in vivo and in vitro models, and elevation of O-GlcNAc levels before, or immediately after, the induction of cellular injury is protective in models of heat stress, oxidative stress, endoplasmic reticulum (ER) stress, hypoxia, ischemia reperfusion injury, and trauma hemorrhage.
20676906	5	36	theme	proteins	1090:1097	arg1	identity					1078:1085	the identity	1074:1085	the identity of proteins that undergo O-GlcNAcylation in response to heat shock	1074:1152	In order to determine how O-GlcNAc modulates stress tolerance in these models we have used stable isotope labeling with amino acids in cell culture to determine the identity of proteins that undergo O-GlcNAcylation in response to heat shock.
20676906	2	37	theme	injury	351:356	arg1	forms					333:337	Numerous forms	324:337	Numerous forms of cellular injury	324:356	Numerous forms of cellular injury lead to elevated levels of O-GlcNAc in both in vivo and in vitro models, and elevation of O-GlcNAc levels before, or immediately after, the induction of cellular injury is protective in models of heat stress, oxidative stress, endoplasmic reticulum (ER) stress, hypoxia, ischemia reperfusion injury, and trauma hemorrhage.
20676906	7	38	theme	double-stranded	1402:1416	arg1	breaks					1422:1427	double-stranded DNA breaks	1402:1427	double-stranded DNA breaks	1402:1427	Many of these proteins bind double-stranded DNA-dependent protein kinase (PK), or double-stranded DNA breaks, suggesting a role for O-GlcNAc in regulating DNA damage signaling or repair.
20676906	2	39	theme	O-GlcNAc	385:392	arg1	levels					375:380	elevated levels	366:380	elevated levels of O-GlcNAc in both in vivo and in vitro models, and elevation of O-GlcNAc levels before	366:469	Numerous forms of cellular injury lead to elevated levels of O-GlcNAc in both in vivo and in vitro models, and elevation of O-GlcNAc levels before, or immediately after, the induction of cellular injury is protective in models of heat stress, oxidative stress, endoplasmic reticulum (ER) stress, hypoxia, ischemia reperfusion injury, and trauma hemorrhage.
20676906	2	40	from	models	423:428	arg1	levels					375:380	elevated levels	366:380	elevated levels of O-GlcNAc in both in vivo and in vitro models, and elevation of O-GlcNAc levels before	366:469	Numerous forms of cellular injury lead to elevated levels of O-GlcNAc in both in vivo and in vitro models, and elevation of O-GlcNAc levels before, or immediately after, the induction of cellular injury is protective in models of heat stress, oxidative stress, endoplasmic reticulum (ER) stress, hypoxia, ischemia reperfusion injury, and trauma hemorrhage.
20676906	2	41	from	protective	530:539	arg1	models					544:549	models	544:549	models of heat stress, oxidative stress, endoplasmic reticulum (ER) stress, hypoxia, ischemia reperfusion injury, and trauma hemorrhage	544:678	Numerous forms of cellular injury lead to elevated levels of O-GlcNAc in both in vivo and in vitro models, and elevation of O-GlcNAc levels before, or immediately after, the induction of cellular injury is protective in models of heat stress, oxidative stress, endoplasmic reticulum (ER) stress, hypoxia, ischemia reperfusion injury, and trauma hemorrhage.
20676906	2	42	theme	stress	577:582	arg1	models					544:549	models	544:549	models of heat stress, oxidative stress, endoplasmic reticulum (ER) stress, hypoxia, ischemia reperfusion injury, and trauma hemorrhage	544:678	Numerous forms of cellular injury lead to elevated levels of O-GlcNAc in both in vivo and in vitro models, and elevation of O-GlcNAc levels before, or immediately after, the induction of cellular injury is protective in models of heat stress, oxidative stress, endoplasmic reticulum (ER) stress, hypoxia, ischemia reperfusion injury, and trauma hemorrhage.
20676906	2	43	from	models	544:549	arg1	protective					530:539	protective	530:539	protective	530:539	Numerous forms of cellular injury lead to elevated levels of O-GlcNAc in both in vivo and in vitro models, and elevation of O-GlcNAc levels before, or immediately after, the induction of cellular injury is protective in models of heat stress, oxidative stress, endoplasmic reticulum (ER) stress, hypoxia, ischemia reperfusion injury, and trauma hemorrhage.
20676906	2	43	from	models	544:549	arg1	induction					498:506	the induction	494:506	the induction of cellular injury	494:525	Numerous forms of cellular injury lead to elevated levels of O-GlcNAc in both in vivo and in vitro models, and elevation of O-GlcNAc levels before, or immediately after, the induction of cellular injury is protective in models of heat stress, oxidative stress, endoplasmic reticulum (ER) stress, hypoxia, ischemia reperfusion injury, and trauma hemorrhage.
20676906	7	44	theme	double-stranded	1348:1362	arg1	kinase					1386:1391	double-stranded DNA-dependent protein kinase	1348:1391	double-stranded DNA-dependent protein kinase (PK)	1348:1396	Many of these proteins bind double-stranded DNA-dependent protein kinase (PK), or double-stranded DNA breaks, suggesting a role for O-GlcNAc in regulating DNA damage signaling or repair.
20676906	7	44	theme	double-stranded	1348:1362	arg1	PK					1394:1395	PK	1394:1395	PK	1394:1395	Many of these proteins bind double-stranded DNA-dependent protein kinase (PK), or double-stranded DNA breaks, suggesting a role for O-GlcNAc in regulating DNA damage signaling or repair.
20676906	8	45	theme	numerous	1597:1604	arg1	forms					1606:1610	numerous forms	1597:1610	numerous forms of cellular stress	1597:1629	Supporting this hypothesis, we have shown that DNA-PK is O-GlcNAc modified in response to numerous forms of cellular stress.
20676906	1	46	theme	mitochondrial	166:178	arg1	proteins					197:204	nuclear, mitochondrial, and cytoplasmic proteins	157:204	nuclear, mitochondrial, and cytoplasmic proteins	157:204	The modification of nuclear, mitochondrial, and cytoplasmic proteins by O-linked β-N-acetylglucosamine (O-GlcNAc) is a dynamic and essential post-translational modification of metazoans.
20676906	2	47	theme	O-GlcNAc	448:455	arg1	levels					457:462	O-GlcNAc levels	448:462	O-GlcNAc levels	448:462	Numerous forms of cellular injury lead to elevated levels of O-GlcNAc in both in vivo and in vitro models, and elevation of O-GlcNAc levels before, or immediately after, the induction of cellular injury is protective in models of heat stress, oxidative stress, endoplasmic reticulum (ER) stress, hypoxia, ischemia reperfusion injury, and trauma hemorrhage.
20676906	7	48	theme	DNA-dependent	1364:1376	arg1	kinase					1386:1391	double-stranded DNA-dependent protein kinase	1348:1391	double-stranded DNA-dependent protein kinase (PK)	1348:1396	Many of these proteins bind double-stranded DNA-dependent protein kinase (PK), or double-stranded DNA breaks, suggesting a role for O-GlcNAc in regulating DNA damage signaling or repair.
20676906	7	48	theme	DNA-dependent	1364:1376	arg1	PK					1394:1395	PK	1394:1395	PK	1394:1395	Many of these proteins bind double-stranded DNA-dependent protein kinase (PK), or double-stranded DNA breaks, suggesting a role for O-GlcNAc in regulating DNA damage signaling or repair.
20676906	4	49	theme	molecular	785:793	arg1	s					805:805	the molecular mechanism(s)	781:806	the molecular mechanism(s) by which O-GlcNAc regulates protein function leading to enhanced cell survival	781:885	However, the molecular mechanism(s) by which O-GlcNAc regulates protein function leading to enhanced cell survival have not been identified.
20676906	2	50	from	levels	375:380	arg1	models					423:428	both in vivo and in vitro models	397:428	both in vivo and in vitro models	397:428	Numerous forms of cellular injury lead to elevated levels of O-GlcNAc in both in vivo and in vitro models, and elevation of O-GlcNAc levels before, or immediately after, the induction of cellular injury is protective in models of heat stress, oxidative stress, endoplasmic reticulum (ER) stress, hypoxia, ischemia reperfusion injury, and trauma hemorrhage.
20676906	7	51	theme	proteins	1334:1341	arg1	Many					1320:1323	Many	1320:1323	Many	1320:1323	Many of these proteins bind double-stranded DNA-dependent protein kinase (PK), or double-stranded DNA breaks, suggesting a role for O-GlcNAc in regulating DNA damage signaling or repair.
20676906	7	51	theme	proteins	1334:1341	arg1	proteins					1334:1341	these proteins	1328:1341	these proteins	1328:1341	Many of these proteins bind double-stranded DNA-dependent protein kinase (PK), or double-stranded DNA breaks, suggesting a role for O-GlcNAc in regulating DNA damage signaling or repair.
20676906	2	52	theme	endoplasmic	585:595	arg1	stress					612:617	endoplasmic reticulum (ER) stress	585:617	endoplasmic reticulum (ER) stress	585:617	Numerous forms of cellular injury lead to elevated levels of O-GlcNAc in both in vivo and in vitro models, and elevation of O-GlcNAc levels before, or immediately after, the induction of cellular injury is protective in models of heat stress, oxidative stress, endoplasmic reticulum (ER) stress, hypoxia, ischemia reperfusion injury, and trauma hemorrhage.
20676906	2	53	from	O-GlcNAc	385:392	arg1	models					423:428	both in vivo and in vitro models	397:428	both in vivo and in vitro models	397:428	Numerous forms of cellular injury lead to elevated levels of O-GlcNAc in both in vivo and in vitro models, and elevation of O-GlcNAc levels before, or immediately after, the induction of cellular injury is protective in models of heat stress, oxidative stress, endoplasmic reticulum (ER) stress, hypoxia, ischemia reperfusion injury, and trauma hemorrhage.
20676906	2	54	theme	Numerous	324:331	arg1	forms					333:337	Numerous forms	324:337	Numerous forms of cellular injury	324:356	Numerous forms of cellular injury lead to elevated levels of O-GlcNAc in both in vivo and in vitro models, and elevation of O-GlcNAc levels before, or immediately after, the induction of cellular injury is protective in models of heat stress, oxidative stress, endoplasmic reticulum (ER) stress, hypoxia, ischemia reperfusion injury, and trauma hemorrhage.
20676906	8	55	theme	stress	1624:1629	arg1	forms					1606:1610	numerous forms	1597:1610	numerous forms of cellular stress	1597:1629	Supporting this hypothesis, we have shown that DNA-PK is O-GlcNAc modified in response to numerous forms of cellular stress.
20676906	1	56	theme	proteins	197:204	arg1	modification					297:308	a dynamic and essential post-translational modification	254:308	a dynamic and essential post-translational modification of metazoans	254:321	The modification of nuclear, mitochondrial, and cytoplasmic proteins by O-linked β-N-acetylglucosamine (O-GlcNAc) is a dynamic and essential post-translational modification of metazoans.
20676906	1	56	theme	proteins	197:204	arg1	modification					141:152	The modification	137:152	The modification of nuclear, mitochondrial, and cytoplasmic proteins by O-linked β-N-acetylglucosamine (O-GlcNAc)	137:249	The modification of nuclear, mitochondrial, and cytoplasmic proteins by O-linked β-N-acetylglucosamine (O-GlcNAc) is a dynamic and essential post-translational modification of metazoans.
20676906	5	57	theme	isotope	1011:1017	arg1	labeling					1019:1026	stable isotope labeling	1004:1026	stable isotope labeling with amino acids in cell culture	1004:1059	In order to determine how O-GlcNAc modulates stress tolerance in these models we have used stable isotope labeling with amino acids in cell culture to determine the identity of proteins that undergo O-GlcNAcylation in response to heat shock.
20676906	1	58	theme	O-linked	209:216	arg1	O-GlcNAc					241:248	O-GlcNAc	241:248	O-GlcNAc	241:248	The modification of nuclear, mitochondrial, and cytoplasmic proteins by O-linked β-N-acetylglucosamine (O-GlcNAc) is a dynamic and essential post-translational modification of metazoans.
20676906	1	58	theme	O-linked	209:216	arg1	β-N-acetylglucosamine					218:238	O-linked β-N-acetylglucosamine	209:238	O-linked β-N-acetylglucosamine (O-GlcNAc)	209:249	The modification of nuclear, mitochondrial, and cytoplasmic proteins by O-linked β-N-acetylglucosamine (O-GlcNAc) is a dynamic and essential post-translational modification of metazoans.
20676906	4	59	theme	cell	873:876	arg1	survival					878:885	enhanced cell survival	864:885	enhanced cell survival	864:885	However, the molecular mechanism(s) by which O-GlcNAc regulates protein function leading to enhanced cell survival have not been identified.
20676906	2	60	theme	hemorrhage	669:678	arg1	models					544:549	models	544:549	models of heat stress, oxidative stress, endoplasmic reticulum (ER) stress, hypoxia, ischemia reperfusion injury, and trauma hemorrhage	544:678	Numerous forms of cellular injury lead to elevated levels of O-GlcNAc in both in vivo and in vitro models, and elevation of O-GlcNAc levels before, or immediately after, the induction of cellular injury is protective in models of heat stress, oxidative stress, endoplasmic reticulum (ER) stress, hypoxia, ischemia reperfusion injury, and trauma hemorrhage.
20676906	2	61	theme	heat	554:557	arg1	stress					559:564	heat stress	554:564	heat stress	554:564	Numerous forms of cellular injury lead to elevated levels of O-GlcNAc in both in vivo and in vitro models, and elevation of O-GlcNAc levels before, or immediately after, the induction of cellular injury is protective in models of heat stress, oxidative stress, endoplasmic reticulum (ER) stress, hypoxia, ischemia reperfusion injury, and trauma hemorrhage.
20676906	6	62	theme	Numerous	1155:1162	arg1	proteins					1164:1171	Numerous proteins	1155:1171	Numerous proteins with diverse functions	1155:1194	Numerous proteins with diverse functions were identified, including NF-90, RuvB-like 1 (Tip49α), RuvB-like 2 (Tip49β), and several COPII vesicle transport proteins.
20676906	6	63	with	proteins	1164:1171	arg1	functions					1186:1194	diverse functions	1178:1194	diverse functions	1178:1194	Numerous proteins with diverse functions were identified, including NF-90, RuvB-like 1 (Tip49α), RuvB-like 2 (Tip49β), and several COPII vesicle transport proteins.
20676906	3	64	theme	response	762:769	arg1	O-GlcNAc					715:722	O-GlcNAc	715:722	O-GlcNAc	715:722	Together, these data suggest that O-GlcNAc is a regulator of the cellular stress response.
20676906	3	64	theme	response	762:769	arg1	regulator					729:737	a regulator	727:737	a regulator of the cellular stress response	727:769	Together, these data suggest that O-GlcNAc is a regulator of the cellular stress response.
20676906	6	65	theme	transport	1300:1308	arg1	proteins					1310:1317	several COPII vesicle transport proteins	1278:1317	several COPII vesicle transport proteins	1278:1317	Numerous proteins with diverse functions were identified, including NF-90, RuvB-like 1 (Tip49α), RuvB-like 2 (Tip49β), and several COPII vesicle transport proteins.
20676906	3	66	theme	cellular	746:753	arg1	response					762:769	the cellular stress response	742:769	the cellular stress response	742:769	Together, these data suggest that O-GlcNAc is a regulator of the cellular stress response.
20676906	6	67	theme	COPII	1286:1290	arg1	proteins					1310:1317	several COPII vesicle transport proteins	1278:1317	several COPII vesicle transport proteins	1278:1317	Numerous proteins with diverse functions were identified, including NF-90, RuvB-like 1 (Tip49α), RuvB-like 2 (Tip49β), and several COPII vesicle transport proteins.
20676906	1	68	theme	nuclear	157:163	arg1	proteins					197:204	nuclear, mitochondrial, and cytoplasmic proteins	157:204	nuclear, mitochondrial, and cytoplasmic proteins	157:204	The modification of nuclear, mitochondrial, and cytoplasmic proteins by O-linked β-N-acetylglucosamine (O-GlcNAc) is a dynamic and essential post-translational modification of metazoans.
20676906	2	69	theme	hypoxia	620:626	arg1	models					544:549	models	544:549	models of heat stress, oxidative stress, endoplasmic reticulum (ER) stress, hypoxia, ischemia reperfusion injury, and trauma hemorrhage	544:678	Numerous forms of cellular injury lead to elevated levels of O-GlcNAc in both in vivo and in vitro models, and elevation of O-GlcNAc levels before, or immediately after, the induction of cellular injury is protective in models of heat stress, oxidative stress, endoplasmic reticulum (ER) stress, hypoxia, ischemia reperfusion injury, and trauma hemorrhage.
20676906	5	70	theme	stable	1004:1009	arg1	labeling					1019:1026	stable isotope labeling	1004:1026	stable isotope labeling with amino acids in cell culture	1004:1059	In order to determine how O-GlcNAc modulates stress tolerance in these models we have used stable isotope labeling with amino acids in cell culture to determine the identity of proteins that undergo O-GlcNAcylation in response to heat shock.
20676906	5	71	from	labeling	1019:1026	arg1	culture					1053:1059	cell culture	1048:1059	cell culture	1048:1059	In order to determine how O-GlcNAc modulates stress tolerance in these models we have used stable isotope labeling with amino acids in cell culture to determine the identity of proteins that undergo O-GlcNAcylation in response to heat shock.
20676906	2	72	theme	stress	612:617	arg1	models					544:549	models	544:549	models of heat stress, oxidative stress, endoplasmic reticulum (ER) stress, hypoxia, ischemia reperfusion injury, and trauma hemorrhage	544:678	Numerous forms of cellular injury lead to elevated levels of O-GlcNAc in both in vivo and in vitro models, and elevation of O-GlcNAc levels before, or immediately after, the induction of cellular injury is protective in models of heat stress, oxidative stress, endoplasmic reticulum (ER) stress, hypoxia, ischemia reperfusion injury, and trauma hemorrhage.
20676906	0	73	theme	other	112:116	arg1	pathways					127:134	other cellular pathways	112:134	other cellular pathways	112:134	The dynamic stress-induced "O-GlcNAc-ome" highlights functions for O-GlcNAc in regulating DNA damage/repair and other cellular pathways.
20676906	2	74	theme	injury	650:655	arg1	models					544:549	models	544:549	models of heat stress, oxidative stress, endoplasmic reticulum (ER) stress, hypoxia, ischemia reperfusion injury, and trauma hemorrhage	544:678	Numerous forms of cellular injury lead to elevated levels of O-GlcNAc in both in vivo and in vitro models, and elevation of O-GlcNAc levels before, or immediately after, the induction of cellular injury is protective in models of heat stress, oxidative stress, endoplasmic reticulum (ER) stress, hypoxia, ischemia reperfusion injury, and trauma hemorrhage.
20676906	2	75	theme	in	402:403	arg1	models					423:428	both in vivo and in vitro models	397:428	both in vivo and in vitro models	397:428	Numerous forms of cellular injury lead to elevated levels of O-GlcNAc in both in vivo and in vitro models, and elevation of O-GlcNAc levels before, or immediately after, the induction of cellular injury is protective in models of heat stress, oxidative stress, endoplasmic reticulum (ER) stress, hypoxia, ischemia reperfusion injury, and trauma hemorrhage.
20676906	0	76	theme	dynamic	4:10	arg1	"					40:40	The dynamic stress-induced "O-GlcNAc-ome"	0:40	The dynamic stress-induced "O-GlcNAc-ome"	0:40	The dynamic stress-induced "O-GlcNAc-ome" highlights functions for O-GlcNAc in regulating DNA damage/repair and other cellular pathways.
20676906	5	77	theme	cell	1048:1051	arg1	culture					1053:1059	cell culture	1048:1059	cell culture	1048:1059	In order to determine how O-GlcNAc modulates stress tolerance in these models we have used stable isotope labeling with amino acids in cell culture to determine the identity of proteins that undergo O-GlcNAcylation in response to heat shock.
20676906	2	78	theme	elevation	435:443	arg1	levels					375:380	elevated levels	366:380	elevated levels of O-GlcNAc in both in vivo and in vitro models, and elevation of O-GlcNAc levels before	366:469	Numerous forms of cellular injury lead to elevated levels of O-GlcNAc in both in vivo and in vitro models, and elevation of O-GlcNAc levels before, or immediately after, the induction of cellular injury is protective in models of heat stress, oxidative stress, endoplasmic reticulum (ER) stress, hypoxia, ischemia reperfusion injury, and trauma hemorrhage.
20676906	2	79	theme	ischemia	629:636	arg1	injury					650:655	ischemia reperfusion injury	629:655	ischemia reperfusion injury	629:655	Numerous forms of cellular injury lead to elevated levels of O-GlcNAc in both in vivo and in vitro models, and elevation of O-GlcNAc levels before, or immediately after, the induction of cellular injury is protective in models of heat stress, oxidative stress, endoplasmic reticulum (ER) stress, hypoxia, ischemia reperfusion injury, and trauma hemorrhage.
20676906	5	80	with	labeling	1019:1026	arg1	acids					1039:1043	amino acids	1033:1043	amino acids	1033:1043	In order to determine how O-GlcNAc modulates stress tolerance in these models we have used stable isotope labeling with amino acids in cell culture to determine the identity of proteins that undergo O-GlcNAcylation in response to heat shock.
20676906	1	81	theme	metazoans	313:321	arg1	modification					297:308	a dynamic and essential post-translational modification	254:308	a dynamic and essential post-translational modification of metazoans	254:321	The modification of nuclear, mitochondrial, and cytoplasmic proteins by O-linked β-N-acetylglucosamine (O-GlcNAc) is a dynamic and essential post-translational modification of metazoans.
20676906	1	81	theme	metazoans	313:321	arg1	modification					141:152	The modification	137:152	The modification of nuclear, mitochondrial, and cytoplasmic proteins by O-linked β-N-acetylglucosamine (O-GlcNAc)	137:249	The modification of nuclear, mitochondrial, and cytoplasmic proteins by O-linked β-N-acetylglucosamine (O-GlcNAc) is a dynamic and essential post-translational modification of metazoans.
20676906	5	82	theme	stress	958:963	arg1	tolerance					965:973	stress tolerance	958:973	stress tolerance	958:973	In order to determine how O-GlcNAc modulates stress tolerance in these models we have used stable isotope labeling with amino acids in cell culture to determine the identity of proteins that undergo O-GlcNAcylation in response to heat shock.
20676906	2	83	theme	injury	520:525	arg1	protective					530:539	protective	530:539	protective	530:539	Numerous forms of cellular injury lead to elevated levels of O-GlcNAc in both in vivo and in vitro models, and elevation of O-GlcNAc levels before, or immediately after, the induction of cellular injury is protective in models of heat stress, oxidative stress, endoplasmic reticulum (ER) stress, hypoxia, ischemia reperfusion injury, and trauma hemorrhage.
20676906	2	83	theme	injury	520:525	arg1	induction					498:506	the induction	494:506	the induction of cellular injury	494:525	Numerous forms of cellular injury lead to elevated levels of O-GlcNAc in both in vivo and in vitro models, and elevation of O-GlcNAc levels before, or immediately after, the induction of cellular injury is protective in models of heat stress, oxidative stress, endoplasmic reticulum (ER) stress, hypoxia, ischemia reperfusion injury, and trauma hemorrhage.
20676906	2	84	theme	cellular	342:349	arg1	injury					351:356	cellular injury	342:356	cellular injury	342:356	Numerous forms of cellular injury lead to elevated levels of O-GlcNAc in both in vivo and in vitro models, and elevation of O-GlcNAc levels before, or immediately after, the induction of cellular injury is protective in models of heat stress, oxidative stress, endoplasmic reticulum (ER) stress, hypoxia, ischemia reperfusion injury, and trauma hemorrhage.
20676906	7	85	theme	DNA	1418:1420	arg1	breaks					1422:1427	double-stranded DNA breaks	1402:1427	double-stranded DNA breaks	1402:1427	Many of these proteins bind double-stranded DNA-dependent protein kinase (PK), or double-stranded DNA breaks, suggesting a role for O-GlcNAc in regulating DNA damage signaling or repair.
20676906	2	86	dep	in	402:403	arg1	vivo					405:408	vivo	405:408	vivo	405:408	Numerous forms of cellular injury lead to elevated levels of O-GlcNAc in both in vivo and in vitro models, and elevation of O-GlcNAc levels before, or immediately after, the induction of cellular injury is protective in models of heat stress, oxidative stress, endoplasmic reticulum (ER) stress, hypoxia, ischemia reperfusion injury, and trauma hemorrhage.
23777819	5	0	theme	Nup62	794:798	arg1	knockdown					781:789	knockdown	781:789	knockdown of Nup62	781:798	Although Nup88, unlike Nup62, was not recognized by an anti-O-GlcNAc antibody or WGA-HRP, knockdown of Nup62 caused a reduction in Nup88 protein levels, suggesting that the observed decrease in Nup88 in OGT knocked-down cells is due to a decrease in Nup62.
23777819	3	1	from	significance	436:447	arg1	nucleoporins					473:484	nucleoporins	473:484	nucleoporins	473:484	However, the biological significance of this modification on nucleoporins remains obscure.
23777819	4	2	theme	protein	538:544	arg1	levels					546:551	Nup62 and Nup88 protein levels	522:551	Nup62 and Nup88 protein levels	522:551	Here we found that Nup62 and Nup88 protein levels were significantly decreased upon knockdown of O-GlcNAc transferase (OGT), which catalyzes the O-GlcNAcylation of intracellular proteins.
23777819	2	3	theme	monosaccharide	305:318	arg1	GlcNAc					343:348	GlcNAc	343:348	GlcNAc	343:348	Several nucleoporins are O-GlcNAcylated, which is a post-translational modification in which the monosaccharide β-N-acetylglucosamine (GlcNAc) is attached to serine or threonine residues within proteins.
23777819	2	3	theme	monosaccharide	305:318	arg1	β-N-acetylglucosamine					320:340	the monosaccharide β-N-acetylglucosamine	301:340	the monosaccharide β-N-acetylglucosamine (GlcNAc)	301:349	Several nucleoporins are O-GlcNAcylated, which is a post-translational modification in which the monosaccharide β-N-acetylglucosamine (GlcNAc) is attached to serine or threonine residues within proteins.
23777819	5	4	from	reduction	809:817	arg1	levels					836:841	Nup88 protein levels	822:841	Nup88 protein levels	822:841	Although Nup88, unlike Nup62, was not recognized by an anti-O-GlcNAc antibody or WGA-HRP, knockdown of Nup62 caused a reduction in Nup88 protein levels, suggesting that the observed decrease in Nup88 in OGT knocked-down cells is due to a decrease in Nup62.
23777819	7	5	theme	O-GlcNAcylated	1242:1255	arg1	Nup62					1257:1261	O-GlcNAcylated Nup62	1242:1261	O-GlcNAcylated Nup62	1242:1261	These results indicate that Nup62 protein levels are primarily maintained by O-GlcNAcylation and that Nup88 is quantitatively regulated through its interaction with O-GlcNAcylated Nup62.
23777819	0	6	theme	proteins	48:55	arg1	regulation					13:22	Quantitative regulation	0:22	Quantitative regulation of nuclear pore complex proteins by O-GlcNAcylation.	0:75	Quantitative regulation of nuclear pore complex proteins by O-GlcNAcylation.
23777819	4	7	theme	Nup62	522:526	arg1	levels					546:551	Nup62 and Nup88 protein levels	522:551	Nup62 and Nup88 protein levels	522:551	Here we found that Nup62 and Nup88 protein levels were significantly decreased upon knockdown of O-GlcNAc transferase (OGT), which catalyzes the O-GlcNAcylation of intracellular proteins.
23777819	5	8	from	decrease	929:936	arg1	Nup62					941:945	Nup62	941:945	Nup62	941:945	Although Nup88, unlike Nup62, was not recognized by an anti-O-GlcNAc antibody or WGA-HRP, knockdown of Nup62 caused a reduction in Nup88 protein levels, suggesting that the observed decrease in Nup88 in OGT knocked-down cells is due to a decrease in Nup62.
23777819	1	9	theme	nuclear	81:87	arg1	complex					94:100	The nuclear pore complex	77:100	The nuclear pore complex (NPC)	77:106	The nuclear pore complex (NPC) is a macromolecular assembly consisting of approximately 30 different proteins called nucleoporins.
23777819	1	9	theme	nuclear	81:87	arg1	assembly					128:135	a macromolecular assembly	111:135	a macromolecular assembly consisting of approximately 30 different proteins called nucleoporins	111:205	The nuclear pore complex (NPC) is a macromolecular assembly consisting of approximately 30 different proteins called nucleoporins.
23777819	1	9	theme	nuclear	81:87	arg1	NPC					103:105	NPC	103:105	NPC	103:105	The nuclear pore complex (NPC) is a macromolecular assembly consisting of approximately 30 different proteins called nucleoporins.
23777819	1	10	theme	different	168:176	arg1	proteins					178:185	approximately 30 different proteins	151:185	approximately 30 different proteins called nucleoporins	151:205	The nuclear pore complex (NPC) is a macromolecular assembly consisting of approximately 30 different proteins called nucleoporins.
23777819	5	11	theme	protein	828:834	arg1	levels					836:841	Nup88 protein levels	822:841	Nup88 protein levels	822:841	Although Nup88, unlike Nup62, was not recognized by an anti-O-GlcNAc antibody or WGA-HRP, knockdown of Nup62 caused a reduction in Nup88 protein levels, suggesting that the observed decrease in Nup88 in OGT knocked-down cells is due to a decrease in Nup62.
23777819	2	12	attach	attached	354:361	arg3	modification					279:290	a post-translational modification	258:290	a post-translational modification in which the monosaccharide β-N-acetylglucosamine (GlcNAc) is attached to serine or threonine residues within proteins	258:409	Several nucleoporins are O-GlcNAcylated, which is a post-translational modification in which the monosaccharide β-N-acetylglucosamine (GlcNAc) is attached to serine or threonine residues within proteins.
23777819	2	12	attach	attached	354:361	arg1	threonine					376:384	threonine	376:384	threonine	376:384	Several nucleoporins are O-GlcNAcylated, which is a post-translational modification in which the monosaccharide β-N-acetylglucosamine (GlcNAc) is attached to serine or threonine residues within proteins.
23777819	2	12	attach	attached	354:361	arg3	which					249:253	which	249:253	which	249:253	Several nucleoporins are O-GlcNAcylated, which is a post-translational modification in which the monosaccharide β-N-acetylglucosamine (GlcNAc) is attached to serine or threonine residues within proteins.
23777819	2	12	attach	attached	354:361	arg2	β-N-acetylglucosamine					320:340	the monosaccharide β-N-acetylglucosamine	301:340	the monosaccharide β-N-acetylglucosamine (GlcNAc)	301:349	Several nucleoporins are O-GlcNAcylated, which is a post-translational modification in which the monosaccharide β-N-acetylglucosamine (GlcNAc) is attached to serine or threonine residues within proteins.
23777819	2	12	attach	attached	354:361	arg2	GlcNAc					343:348	GlcNAc	343:348	GlcNAc	343:348	Several nucleoporins are O-GlcNAcylated, which is a post-translational modification in which the monosaccharide β-N-acetylglucosamine (GlcNAc) is attached to serine or threonine residues within proteins.
23777819	2	12	attach	attached	354:361	arg1	serine					366:371	serine	366:371	serine	366:371	Several nucleoporins are O-GlcNAcylated, which is a post-translational modification in which the monosaccharide β-N-acetylglucosamine (GlcNAc) is attached to serine or threonine residues within proteins.
23777819	7	13	theme	protein	1111:1117	arg1	levels					1119:1124	Nup62 protein levels	1105:1124	Nup62 protein levels	1105:1124	These results indicate that Nup62 protein levels are primarily maintained by O-GlcNAcylation and that Nup88 is quantitatively regulated through its interaction with O-GlcNAcylated Nup62.
23777819	1	14	theme	pore	89:92	arg1	complex					94:100	The nuclear pore complex	77:100	The nuclear pore complex (NPC)	77:106	The nuclear pore complex (NPC) is a macromolecular assembly consisting of approximately 30 different proteins called nucleoporins.
23777819	1	14	theme	pore	89:92	arg1	assembly					128:135	a macromolecular assembly	111:135	a macromolecular assembly consisting of approximately 30 different proteins called nucleoporins	111:205	The nuclear pore complex (NPC) is a macromolecular assembly consisting of approximately 30 different proteins called nucleoporins.
23777819	1	14	theme	pore	89:92	arg1	NPC					103:105	NPC	103:105	NPC	103:105	The nuclear pore complex (NPC) is a macromolecular assembly consisting of approximately 30 different proteins called nucleoporins.
23777819	0	15	theme	Quantitative	0:11	arg1	regulation					13:22	Quantitative regulation	0:22	Quantitative regulation of nuclear pore complex proteins by O-GlcNAcylation.	0:75	Quantitative regulation of nuclear pore complex proteins by O-GlcNAcylation.
23777819	3	16	theme	modification	457:468	arg1	significance					436:447	the biological significance	421:447	the biological significance of this modification on nucleoporins	421:484	However, the biological significance of this modification on nucleoporins remains obscure.
23777819	0	17	theme	nuclear	27:33	arg1	proteins					48:55	nuclear pore complex proteins	27:55	nuclear pore complex proteins	27:55	Quantitative regulation of nuclear pore complex proteins by O-GlcNAcylation.
23777819	2	18	dep	serine	366:371	arg1	residues					386:393	residues	386:393	residues	386:393	Several nucleoporins are O-GlcNAcylated, which is a post-translational modification in which the monosaccharide β-N-acetylglucosamine (GlcNAc) is attached to serine or threonine residues within proteins.
23777819	4	19	theme	intracellular	667:679	arg1	proteins					681:688	intracellular proteins	667:688	intracellular proteins	667:688	Here we found that Nup62 and Nup88 protein levels were significantly decreased upon knockdown of O-GlcNAc transferase (OGT), which catalyzes the O-GlcNAcylation of intracellular proteins.
23777819	4	20	theme	transferase	609:619	arg1	knockdown					587:595	knockdown	587:595	knockdown of O-GlcNAc transferase (OGT), which catalyzes the O-GlcNAcylation of intracellular proteins	587:688	Here we found that Nup62 and Nup88 protein levels were significantly decreased upon knockdown of O-GlcNAc transferase (OGT), which catalyzes the O-GlcNAcylation of intracellular proteins.
23777819	7	21	theme	Nup62	1105:1109	arg1	levels					1119:1124	Nup62 protein levels	1105:1124	Nup62 protein levels	1105:1124	These results indicate that Nup62 protein levels are primarily maintained by O-GlcNAcylation and that Nup88 is quantitatively regulated through its interaction with O-GlcNAcylated Nup62.
23777819	7	22	with	interaction	1225:1235	arg1	Nup62					1257:1261	O-GlcNAcylated Nup62	1242:1261	O-GlcNAcylated Nup62	1242:1261	These results indicate that Nup62 protein levels are primarily maintained by O-GlcNAcylation and that Nup88 is quantitatively regulated through its interaction with O-GlcNAcylated Nup62.
23777819	0	23	theme	complex	40:46	arg1	proteins					48:55	nuclear pore complex proteins	27:55	nuclear pore complex proteins	27:55	Quantitative regulation of nuclear pore complex proteins by O-GlcNAcylation.
23777819	4	24	theme	O-GlcNAc	600:607	arg1	OGT					622:624	OGT	622:624	OGT	622:624	Here we found that Nup62 and Nup88 protein levels were significantly decreased upon knockdown of O-GlcNAc transferase (OGT), which catalyzes the O-GlcNAcylation of intracellular proteins.
23777819	4	24	theme	O-GlcNAc	600:607	arg1	transferase					609:619	O-GlcNAc transferase	600:619	O-GlcNAc transferase (OGT)	600:625	Here we found that Nup62 and Nup88 protein levels were significantly decreased upon knockdown of O-GlcNAc transferase (OGT), which catalyzes the O-GlcNAcylation of intracellular proteins.
23777819	5	25	theme	OGT	894:896	arg1	cells					911:915	OGT knocked-down cells	894:915	OGT knocked-down cells	894:915	Although Nup88, unlike Nup62, was not recognized by an anti-O-GlcNAc antibody or WGA-HRP, knockdown of Nup62 caused a reduction in Nup88 protein levels, suggesting that the observed decrease in Nup88 in OGT knocked-down cells is due to a decrease in Nup62.
23777819	5	26	theme	observed	864:871	arg1	due					920:922	due	920:922	due	920:922	Although Nup88, unlike Nup62, was not recognized by an anti-O-GlcNAc antibody or WGA-HRP, knockdown of Nup62 caused a reduction in Nup88 protein levels, suggesting that the observed decrease in Nup88 in OGT knocked-down cells is due to a decrease in Nup62.
23777819	5	26	theme	observed	864:871	arg1	decrease					873:880	the observed decrease	860:880	the observed decrease in Nup88 in OGT knocked-down cells	860:915	Although Nup88, unlike Nup62, was not recognized by an anti-O-GlcNAc antibody or WGA-HRP, knockdown of Nup62 caused a reduction in Nup88 protein levels, suggesting that the observed decrease in Nup88 in OGT knocked-down cells is due to a decrease in Nup62.
23777819	0	27	theme	pore	35:38	arg1	proteins					48:55	nuclear pore complex proteins	27:55	nuclear pore complex proteins	27:55	Quantitative regulation of nuclear pore complex proteins by O-GlcNAcylation.
23777819	5	28	theme	anti-O-GlcNAc	746:758	arg1	antibody					760:767	an anti-O-GlcNAc antibody	743:767	an anti-O-GlcNAc antibody	743:767	Although Nup88, unlike Nup62, was not recognized by an anti-O-GlcNAc antibody or WGA-HRP, knockdown of Nup62 caused a reduction in Nup88 protein levels, suggesting that the observed decrease in Nup88 in OGT knocked-down cells is due to a decrease in Nup62.
23777819	4	29	theme	proteins	681:688	arg1	O-GlcNAcylation					648:662	the O-GlcNAcylation	644:662	the O-GlcNAcylation of intracellular proteins	644:688	Here we found that Nup62 and Nup88 protein levels were significantly decreased upon knockdown of O-GlcNAc transferase (OGT), which catalyzes the O-GlcNAcylation of intracellular proteins.
23777819	5	30	theme	Nup88	822:826	arg1	levels					836:841	Nup88 protein levels	822:841	Nup88 protein levels	822:841	Although Nup88, unlike Nup62, was not recognized by an anti-O-GlcNAc antibody or WGA-HRP, knockdown of Nup62 caused a reduction in Nup88 protein levels, suggesting that the observed decrease in Nup88 in OGT knocked-down cells is due to a decrease in Nup62.
23777819	5	31	from	decrease	873:880	arg1	Nup88					885:889	Nup88	885:889	Nup88	885:889	Although Nup88, unlike Nup62, was not recognized by an anti-O-GlcNAc antibody or WGA-HRP, knockdown of Nup62 caused a reduction in Nup88 protein levels, suggesting that the observed decrease in Nup88 in OGT knocked-down cells is due to a decrease in Nup62.
23777819	5	31	from	decrease	873:880	arg1	cells					911:915	OGT knocked-down cells	894:915	OGT knocked-down cells	894:915	Although Nup88, unlike Nup62, was not recognized by an anti-O-GlcNAc antibody or WGA-HRP, knockdown of Nup62 caused a reduction in Nup88 protein levels, suggesting that the observed decrease in Nup88 in OGT knocked-down cells is due to a decrease in Nup62.
23777819	3	32	theme	biological	425:434	arg1	significance					436:447	the biological significance	421:447	the biological significance of this modification on nucleoporins	421:484	However, the biological significance of this modification on nucleoporins remains obscure.
23777819	2	33	theme	Several	208:214	arg1	nucleoporins					216:227	Several nucleoporins	208:227	Several nucleoporins	208:227	Several nucleoporins are O-GlcNAcylated, which is a post-translational modification in which the monosaccharide β-N-acetylglucosamine (GlcNAc) is attached to serine or threonine residues within proteins.
23777819	2	34	theme	post-translational	260:277	arg1	which					249:253	which	249:253	which	249:253	Several nucleoporins are O-GlcNAcylated, which is a post-translational modification in which the monosaccharide β-N-acetylglucosamine (GlcNAc) is attached to serine or threonine residues within proteins.
23777819	2	34	theme	post-translational	260:277	arg1	modification					279:290	a post-translational modification	258:290	a post-translational modification in which the monosaccharide β-N-acetylglucosamine (GlcNAc) is attached to serine or threonine residues within proteins	258:409	Several nucleoporins are O-GlcNAcylated, which is a post-translational modification in which the monosaccharide β-N-acetylglucosamine (GlcNAc) is attached to serine or threonine residues within proteins.
23777819	1	35	theme	macromolecular	113:126	arg1	complex					94:100	The nuclear pore complex	77:100	The nuclear pore complex (NPC)	77:106	The nuclear pore complex (NPC) is a macromolecular assembly consisting of approximately 30 different proteins called nucleoporins.
23777819	1	35	theme	macromolecular	113:126	arg1	assembly					128:135	a macromolecular assembly	111:135	a macromolecular assembly consisting of approximately 30 different proteins called nucleoporins	111:205	The nuclear pore complex (NPC) is a macromolecular assembly consisting of approximately 30 different proteins called nucleoporins.
23777819	6	36	theme	non-O-GlcNAcylated	1051:1068	arg1	Nup62					1070:1074	non-O-GlcNAcylated Nup62	1051:1074	non-O-GlcNAcylated Nup62	1051:1074	Furthermore, we found that Nup88 was preferentially associated with O-GlcNAcylated Nup62 compared with non-O-GlcNAcylated Nup62.
23777819	5	37	theme	knocked-down	898:909	arg1	cells					911:915	OGT knocked-down cells	894:915	OGT knocked-down cells	894:915	Although Nup88, unlike Nup62, was not recognized by an anti-O-GlcNAc antibody or WGA-HRP, knockdown of Nup62 caused a reduction in Nup88 protein levels, suggesting that the observed decrease in Nup88 in OGT knocked-down cells is due to a decrease in Nup62.
23777819	4	38	theme	Nup88	532:536	arg1	levels					546:551	Nup62 and Nup88 protein levels	522:551	Nup62 and Nup88 protein levels	522:551	Here we found that Nup62 and Nup88 protein levels were significantly decreased upon knockdown of O-GlcNAc transferase (OGT), which catalyzes the O-GlcNAcylation of intracellular proteins.
23777819	6	39	theme	O-GlcNAcylated	1016:1029	arg1	Nup62					1031:1035	O-GlcNAcylated Nup62	1016:1035	O-GlcNAcylated Nup62	1016:1035	Furthermore, we found that Nup88 was preferentially associated with O-GlcNAcylated Nup62 compared with non-O-GlcNAcylated Nup62.
10926833	0	0	theme	protein	89:95	arg1	p62					97:99	nuclear pore protein p62	76:99	nuclear pore protein p62	76:99	Responsiveness of the state of O-linked N-acetylglucosamine modification of nuclear pore protein p62 to the extracellular glucose concentration.
10926833	6	1	theme	physiological	932:944	arg1	range					946:950	the physiological range	928:950	the physiological range	928:950	Furthermore, changes in glucose concentrations within the physiological range induced the O-GlcNAc modification in p62 in rat aortic smooth-muscle cells, indicating that this modification of p62 might occur in an intact animal.
10926833	6	2	theme	intact	1087:1092	arg1	animal					1094:1099	an intact animal	1084:1099	an intact animal	1084:1099	Furthermore, changes in glucose concentrations within the physiological range induced the O-GlcNAc modification in p62 in rat aortic smooth-muscle cells, indicating that this modification of p62 might occur in an intact animal.
10926833	2	3	from	effect	314:319	arg1	level					353:357	the level	349:357	the level of modification of nuclear pore protein p62	349:401	In the present study we investigated the effect of extracellular glucose on the level of modification of nuclear pore protein p62 by O-GlcNAc.
10926833	0	4	theme	pore	84:87	arg1	p62					97:99	nuclear pore protein p62	76:99	nuclear pore protein p62	76:99	Responsiveness of the state of O-linked N-acetylglucosamine modification of nuclear pore protein p62 to the extracellular glucose concentration.
10926833	7	5	theme	glucose	1139:1145	arg1	concentration					1147:1159	the ambient glucose concentration	1127:1159	the ambient glucose concentration	1127:1159	These results imply that the ambient glucose concentration has an impact on the level of O-GlcNAc modification of proteins such as p62, and that functional changes in some of these proteins might ensue.
10926833	7	6	contain	has	1161:1163	arg1	concentration					1147:1159	the ambient glucose concentration	1127:1159	the ambient glucose concentration	1127:1159	These results imply that the ambient glucose concentration has an impact on the level of O-GlcNAc modification of proteins such as p62, and that functional changes in some of these proteins might ensue.
10926833	7	6	contain	has	1161:1163	arg2	impact					1168:1173	an impact	1165:1173	an impact on the level of O-GlcNAc modification of proteins such as p62	1165:1235	These results imply that the ambient glucose concentration has an impact on the level of O-GlcNAc modification of proteins such as p62, and that functional changes in some of these proteins might ensue.
10926833	2	7	theme	modification	362:373	arg1	level					353:357	the level	349:357	the level of modification of nuclear pore protein p62	349:401	In the present study we investigated the effect of extracellular glucose on the level of modification of nuclear pore protein p62 by O-GlcNAc.
10926833	7	8	theme	ambient	1131:1137	arg1	concentration					1147:1159	the ambient glucose concentration	1127:1159	the ambient glucose concentration	1127:1159	These results imply that the ambient glucose concentration has an impact on the level of O-GlcNAc modification of proteins such as p62, and that functional changes in some of these proteins might ensue.
10926833	7	9	from	impact	1168:1173	arg1	level					1182:1186	the level	1178:1186	the level of O-GlcNAc modification of proteins such as p62	1178:1235	These results imply that the ambient glucose concentration has an impact on the level of O-GlcNAc modification of proteins such as p62, and that functional changes in some of these proteins might ensue.
10926833	3	10	with	modification	512:523	arg1	O-GlcNAc					537:544	O-GlcNAc	537:544	O-GlcNAc	537:544	We found that exposure of cells to a high concentration of glucose caused an increased level of modification of p62 with O-GlcNAc, whereas the modification of other proteins did not change detectably.
10926833	3	11	theme	modification	512:523	arg1	level					503:507	an increased level	490:507	an increased level of modification of p62 with O-GlcNAc	490:544	We found that exposure of cells to a high concentration of glucose caused an increased level of modification of p62 with O-GlcNAc, whereas the modification of other proteins did not change detectably.
10926833	6	12	theme	smooth-muscle	1007:1019	arg1	cells					1021:1025	rat aortic smooth-muscle cells	996:1025	rat aortic smooth-muscle cells	996:1025	Furthermore, changes in glucose concentrations within the physiological range induced the O-GlcNAc modification in p62 in rat aortic smooth-muscle cells, indicating that this modification of p62 might occur in an intact animal.
10926833	0	13	theme	p62	97:99	arg1	modification					60:71	O-linked N-acetylglucosamine modification	31:71	O-linked N-acetylglucosamine modification of nuclear pore protein p62	31:99	Responsiveness of the state of O-linked N-acetylglucosamine modification of nuclear pore protein p62 to the extracellular glucose concentration.
10926833	1	14	gly	glycoproteins	258:270	arg1	glycoproteins					258:270	nuclear pore glycoproteins	245:270	nuclear pore glycoproteins	245:270	O-linked N-acetylglucosamine (O-GlcNAc) modification has been described in many proteins, including nuclear pore glycoproteins.
10926833	4	15	mod	modification	640:651	arg3	O-GlcNAc					631:638	The increased O-GlcNAc modification	617:651	The increased O-GlcNAc modification of p62 in response to glucose	617:681	The increased O-GlcNAc modification of p62 in response to glucose required the metabolism of glucose to glucosamine.
10926833	4	15	mod	modification	640:651	arg1	p62					656:658	p62	656:658	p62	656:658	The increased O-GlcNAc modification of p62 in response to glucose required the metabolism of glucose to glucosamine.
10926833	6	16	theme	aortic	1000:1005	arg1	cells					1021:1025	rat aortic smooth-muscle cells	996:1025	rat aortic smooth-muscle cells	996:1025	Furthermore, changes in glucose concentrations within the physiological range induced the O-GlcNAc modification in p62 in rat aortic smooth-muscle cells, indicating that this modification of p62 might occur in an intact animal.
10926833	0	17	theme	extracellular	108:120	arg1	concentration					130:142	the extracellular glucose concentration	104:142	the extracellular glucose concentration	104:142	Responsiveness of the state of O-linked N-acetylglucosamine modification of nuclear pore protein p62 to the extracellular glucose concentration.
10926833	6	18	theme	glucose	898:904	arg1	concentrations					906:919	glucose concentrations	898:919	glucose concentrations within the physiological range	898:950	Furthermore, changes in glucose concentrations within the physiological range induced the O-GlcNAc modification in p62 in rat aortic smooth-muscle cells, indicating that this modification of p62 might occur in an intact animal.
10926833	4	19	theme	increased	621:629	arg1	modification					640:651	The increased O-GlcNAc modification	617:651	The increased O-GlcNAc modification of p62 in response to glucose	617:681	The increased O-GlcNAc modification of p62 in response to glucose required the metabolism of glucose to glucosamine.
10926833	3	20	theme	p62	528:530	arg1	modification					512:523	modification	512:523	modification of p62 with O-GlcNAc	512:544	We found that exposure of cells to a high concentration of glucose caused an increased level of modification of p62 with O-GlcNAc, whereas the modification of other proteins did not change detectably.
10926833	3	21	theme	cells	442:446	arg1	exposure					430:437	exposure	430:437	exposure of cells to a high concentration of glucose	430:481	We found that exposure of cells to a high concentration of glucose caused an increased level of modification of p62 with O-GlcNAc, whereas the modification of other proteins did not change detectably.
10926833	5	22	theme	increased	794:802	arg1	modification					813:824	increased O-GlcNAc modification	794:824	increased O-GlcNAc modification	794:824	The exposure of the cells to glucosamine itself also caused increased O-GlcNAc modification, whereas mannosamine and galactosamine did not.
10926833	7	23	from	changes	1258:1264	arg1	some					1269:1272	some	1269:1272	some	1269:1272	These results imply that the ambient glucose concentration has an impact on the level of O-GlcNAc modification of proteins such as p62, and that functional changes in some of these proteins might ensue.
10926833	7	23	from	changes	1258:1264	arg1	proteins					1283:1290	these proteins	1277:1290	these proteins	1277:1290	These results imply that the ambient glucose concentration has an impact on the level of O-GlcNAc modification of proteins such as p62, and that functional changes in some of these proteins might ensue.
10926833	2	24	theme	pore	386:389	arg1	p62					399:401	nuclear pore protein p62	378:401	nuclear pore protein p62	378:401	In the present study we investigated the effect of extracellular glucose on the level of modification of nuclear pore protein p62 by O-GlcNAc.
10926833	5	25	theme	O-GlcNAc	804:811	arg1	modification					813:824	increased O-GlcNAc modification	794:824	increased O-GlcNAc modification	794:824	The exposure of the cells to glucosamine itself also caused increased O-GlcNAc modification, whereas mannosamine and galactosamine did not.
10926833	2	26	theme	glucose	338:344	arg1	effect					314:319	the effect	310:319	the effect of extracellular glucose on the level of modification of nuclear pore protein p62	310:401	In the present study we investigated the effect of extracellular glucose on the level of modification of nuclear pore protein p62 by O-GlcNAc.
10926833	2	27	theme	p62	399:401	arg1	modification					362:373	modification	362:373	modification of nuclear pore protein p62	362:401	In the present study we investigated the effect of extracellular glucose on the level of modification of nuclear pore protein p62 by O-GlcNAc.
10926833	6	28	theme	rat	996:998	arg1	cells					1021:1025	rat aortic smooth-muscle cells	996:1025	rat aortic smooth-muscle cells	996:1025	Furthermore, changes in glucose concentrations within the physiological range induced the O-GlcNAc modification in p62 in rat aortic smooth-muscle cells, indicating that this modification of p62 might occur in an intact animal.
10926833	7	29	mod	modification	1200:1211	arg3	O-GlcNAc					1191:1198	O-GlcNAc modification	1191:1211	O-GlcNAc modification of proteins such as p62	1191:1235	These results imply that the ambient glucose concentration has an impact on the level of O-GlcNAc modification of proteins such as p62, and that functional changes in some of these proteins might ensue.
10926833	7	29	mod	modification	1200:1211	arg1	proteins					1216:1223	proteins	1216:1223	proteins such as p62	1216:1235	These results imply that the ambient glucose concentration has an impact on the level of O-GlcNAc modification of proteins such as p62, and that functional changes in some of these proteins might ensue.
10926833	7	29	mod	modification	1200:1211	arg1	p62					1233:1235	p62	1233:1235	p62	1233:1235	These results imply that the ambient glucose concentration has an impact on the level of O-GlcNAc modification of proteins such as p62, and that functional changes in some of these proteins might ensue.
10926833	0	30	link	O-linked	31:38	arg1	modification					60:71	O-linked N-acetylglucosamine modification	31:71	O-linked N-acetylglucosamine modification of nuclear pore protein p62	31:99	Responsiveness of the state of O-linked N-acetylglucosamine modification of nuclear pore protein p62 to the extracellular glucose concentration.
10926833	2	31	theme	extracellular	324:336	arg1	glucose					338:344	extracellular glucose	324:344	extracellular glucose	324:344	In the present study we investigated the effect of extracellular glucose on the level of modification of nuclear pore protein p62 by O-GlcNAc.
10926833	2	32	theme	protein	391:397	arg1	p62					399:401	nuclear pore protein p62	378:401	nuclear pore protein p62	378:401	In the present study we investigated the effect of extracellular glucose on the level of modification of nuclear pore protein p62 by O-GlcNAc.
10926833	0	33	theme	state	22:26	arg1	Responsiveness					0:13	Responsiveness	0:13	Responsiveness of the state of O-linked N-acetylglucosamine modification of nuclear pore protein p62 to the extracellular glucose concentration.	0:143	Responsiveness of the state of O-linked N-acetylglucosamine modification of nuclear pore protein p62 to the extracellular glucose concentration.
10926833	0	34	mod	modification	60:71	arg3	N-acetylglucosamine					40:58	O-linked N-acetylglucosamine modification	31:71	O-linked N-acetylglucosamine modification of nuclear pore protein p62	31:99	Responsiveness of the state of O-linked N-acetylglucosamine modification of nuclear pore protein p62 to the extracellular glucose concentration.
10926833	0	34	mod	modification	60:71	arg1	p62					97:99	nuclear pore protein p62	76:99	nuclear pore protein p62	76:99	Responsiveness of the state of O-linked N-acetylglucosamine modification of nuclear pore protein p62 to the extracellular glucose concentration.
10926833	6	35	from	p62	989:991	arg1	cells					1021:1025	rat aortic smooth-muscle cells	996:1025	rat aortic smooth-muscle cells	996:1025	Furthermore, changes in glucose concentrations within the physiological range induced the O-GlcNAc modification in p62 in rat aortic smooth-muscle cells, indicating that this modification of p62 might occur in an intact animal.
10926833	7	36	theme	functional	1247:1256	arg1	changes					1258:1264	functional changes	1247:1264	functional changes in some of these proteins	1247:1290	These results imply that the ambient glucose concentration has an impact on the level of O-GlcNAc modification of proteins such as p62, and that functional changes in some of these proteins might ensue.
10926833	4	37	from	modification	640:651	arg1	response					663:670	response	663:670	response to glucose	663:681	The increased O-GlcNAc modification of p62 in response to glucose required the metabolism of glucose to glucosamine.
10926833	4	38	theme	O-GlcNAc	631:638	arg1	modification					640:651	The increased O-GlcNAc modification	617:651	The increased O-GlcNAc modification of p62 in response to glucose	617:681	The increased O-GlcNAc modification of p62 in response to glucose required the metabolism of glucose to glucosamine.
10926833	0	39	theme	glucose	122:128	arg1	concentration					130:142	the extracellular glucose concentration	104:142	the extracellular glucose concentration	104:142	Responsiveness of the state of O-linked N-acetylglucosamine modification of nuclear pore protein p62 to the extracellular glucose concentration.
10926833	1	40	theme	many	220:223	arg1	glycoproteins					258:270	nuclear pore glycoproteins	245:270	nuclear pore glycoproteins	245:270	O-linked N-acetylglucosamine (O-GlcNAc) modification has been described in many proteins, including nuclear pore glycoproteins.
10926833	1	40	theme	many	220:223	arg1	proteins					225:232	many proteins	220:232	many proteins	220:232	O-linked N-acetylglucosamine (O-GlcNAc) modification has been described in many proteins, including nuclear pore glycoproteins.
10926833	0	41	theme	O-linked	31:38	arg1	modification					60:71	O-linked N-acetylglucosamine modification	31:71	O-linked N-acetylglucosamine modification of nuclear pore protein p62	31:99	Responsiveness of the state of O-linked N-acetylglucosamine modification of nuclear pore protein p62 to the extracellular glucose concentration.
10926833	7	42	theme	modification	1200:1211	arg1	level					1182:1186	the level	1178:1186	the level of O-GlcNAc modification of proteins such as p62	1178:1235	These results imply that the ambient glucose concentration has an impact on the level of O-GlcNAc modification of proteins such as p62, and that functional changes in some of these proteins might ensue.
10926833	6	43	theme	p62	1065:1067	arg1	modification					1049:1060	this modification	1044:1060	this modification of p62	1044:1067	Furthermore, changes in glucose concentrations within the physiological range induced the O-GlcNAc modification in p62 in rat aortic smooth-muscle cells, indicating that this modification of p62 might occur in an intact animal.
10926833	3	44	theme	high	453:456	arg1	concentration					458:470	a high concentration	451:470	a high concentration of glucose	451:481	We found that exposure of cells to a high concentration of glucose caused an increased level of modification of p62 with O-GlcNAc, whereas the modification of other proteins did not change detectably.
10926833	0	45	theme	modification	60:71	arg1	state					22:26	the state	18:26	the state of O-linked N-acetylglucosamine modification of nuclear pore protein p62	18:99	Responsiveness of the state of O-linked N-acetylglucosamine modification of nuclear pore protein p62 to the extracellular glucose concentration.
10926833	6	46	theme	O-GlcNAc	964:971	arg1	modification					973:984	the O-GlcNAc modification	960:984	the O-GlcNAc modification	960:984	Furthermore, changes in glucose concentrations within the physiological range induced the O-GlcNAc modification in p62 in rat aortic smooth-muscle cells, indicating that this modification of p62 might occur in an intact animal.
10926833	3	47	theme	other	575:579	arg1	proteins					581:588	other proteins	575:588	other proteins	575:588	We found that exposure of cells to a high concentration of glucose caused an increased level of modification of p62 with O-GlcNAc, whereas the modification of other proteins did not change detectably.
10926833	4	48	theme	glucose	710:716	arg1	metabolism					696:705	the metabolism	692:705	the metabolism of glucose to glucosamine	692:731	The increased O-GlcNAc modification of p62 in response to glucose required the metabolism of glucose to glucosamine.
10926833	0	49	theme	N-acetylglucosamine	40:58	arg1	modification					60:71	O-linked N-acetylglucosamine modification	31:71	O-linked N-acetylglucosamine modification of nuclear pore protein p62	31:99	Responsiveness of the state of O-linked N-acetylglucosamine modification of nuclear pore protein p62 to the extracellular glucose concentration.
10926833	1	50	link	O-linked	145:152	arg1	O-GlcNAc					175:182	O-GlcNAc	175:182	O-GlcNAc	175:182	O-linked N-acetylglucosamine (O-GlcNAc) modification has been described in many proteins, including nuclear pore glycoproteins.
10926833	1	50	link	O-linked	145:152	arg1	N-acetylglucosamine					154:172	O-linked N-acetylglucosamine	145:172	O-linked N-acetylglucosamine (O-GlcNAc) modification	145:196	O-linked N-acetylglucosamine (O-GlcNAc) modification has been described in many proteins, including nuclear pore glycoproteins.
10926833	3	51	theme	proteins	581:588	arg1	modification					559:570	the modification	555:570	the modification of other proteins	555:588	We found that exposure of cells to a high concentration of glucose caused an increased level of modification of p62 with O-GlcNAc, whereas the modification of other proteins did not change detectably.
10926833	7	52	theme	proteins	1216:1223	arg1	modification					1200:1211	O-GlcNAc modification	1191:1211	O-GlcNAc modification of proteins such as p62	1191:1235	These results imply that the ambient glucose concentration has an impact on the level of O-GlcNAc modification of proteins such as p62, and that functional changes in some of these proteins might ensue.
10926833	3	53	theme	increased	493:501	arg1	level					503:507	an increased level	490:507	an increased level of modification of p62 with O-GlcNAc	490:544	We found that exposure of cells to a high concentration of glucose caused an increased level of modification of p62 with O-GlcNAc, whereas the modification of other proteins did not change detectably.
10926833	2	54	theme	present	280:286	arg1	study					288:292	the present study	276:292	the present study	276:292	In the present study we investigated the effect of extracellular glucose on the level of modification of nuclear pore protein p62 by O-GlcNAc.
10926833	3	55	theme	glucose	475:481	arg1	concentration					458:470	a high concentration	451:470	a high concentration of glucose	451:481	We found that exposure of cells to a high concentration of glucose caused an increased level of modification of p62 with O-GlcNAc, whereas the modification of other proteins did not change detectably.
10926833	1	56	theme	O-linked	145:152	arg1	O-GlcNAc					175:182	O-GlcNAc	175:182	O-GlcNAc	175:182	O-linked N-acetylglucosamine (O-GlcNAc) modification has been described in many proteins, including nuclear pore glycoproteins.
10926833	1	56	theme	O-linked	145:152	arg1	N-acetylglucosamine					154:172	O-linked N-acetylglucosamine	145:172	O-linked N-acetylglucosamine (O-GlcNAc) modification	145:196	O-linked N-acetylglucosamine (O-GlcNAc) modification has been described in many proteins, including nuclear pore glycoproteins.
10926833	1	57	theme	nuclear	245:251	arg1	glycoproteins					258:270	nuclear pore glycoproteins	245:270	nuclear pore glycoproteins	245:270	O-linked N-acetylglucosamine (O-GlcNAc) modification has been described in many proteins, including nuclear pore glycoproteins.
10926833	0	58	theme	nuclear	76:82	arg1	p62					97:99	nuclear pore protein p62	76:99	nuclear pore protein p62	76:99	Responsiveness of the state of O-linked N-acetylglucosamine modification of nuclear pore protein p62 to the extracellular glucose concentration.
10926833	1	59	theme	N-acetylglucosamine	154:172	arg1	modification					185:196	O-linked N-acetylglucosamine (O-GlcNAc) modification	145:196	O-linked N-acetylglucosamine (O-GlcNAc) modification	145:196	O-linked N-acetylglucosamine (O-GlcNAc) modification has been described in many proteins, including nuclear pore glycoproteins.
10926833	4	60	theme	p62	656:658	arg1	modification					640:651	The increased O-GlcNAc modification	617:651	The increased O-GlcNAc modification of p62 in response to glucose	617:681	The increased O-GlcNAc modification of p62 in response to glucose required the metabolism of glucose to glucosamine.
10926833	1	61	theme	pore	253:256	arg1	glycoproteins					258:270	nuclear pore glycoproteins	245:270	nuclear pore glycoproteins	245:270	O-linked N-acetylglucosamine (O-GlcNAc) modification has been described in many proteins, including nuclear pore glycoproteins.
10926833	5	62	theme	cells	754:758	arg1	exposure					738:745	The exposure	734:745	The exposure of the cells to glucosamine itself	734:780	The exposure of the cells to glucosamine itself also caused increased O-GlcNAc modification, whereas mannosamine and galactosamine did not.
10926833	7	63	theme	O-GlcNAc	1191:1198	arg1	modification					1200:1211	O-GlcNAc modification	1191:1211	O-GlcNAc modification of proteins such as p62	1191:1235	These results imply that the ambient glucose concentration has an impact on the level of O-GlcNAc modification of proteins such as p62, and that functional changes in some of these proteins might ensue.
10926833	2	64	theme	nuclear	378:384	arg1	p62					399:401	nuclear pore protein p62	378:401	nuclear pore protein p62	378:401	In the present study we investigated the effect of extracellular glucose on the level of modification of nuclear pore protein p62 by O-GlcNAc.
10926833	6	65	from	changes	887:893	arg1	concentrations					906:919	glucose concentrations	898:919	glucose concentrations within the physiological range	898:950	Furthermore, changes in glucose concentrations within the physiological range induced the O-GlcNAc modification in p62 in rat aortic smooth-muscle cells, indicating that this modification of p62 might occur in an intact animal.
20041180	0	0	theme	nuclear	80:86	arg1	factors					98:104	target nuclear transport factors	73:104	target nuclear transport factors	73:104	Dissecting the signaling events that impact classical nuclear import and target nuclear transport factors.
20041180	9	1	theme	PI3	1324:1326	arg1	signaling					1335:1343	PI3 kinase signaling	1324:1343	PI3 kinase signaling	1324:1343	Our results demonstrate that MEK and PI3 kinase signaling as well as oxidative stress control nuclear trafficking and the localization of transport components.
20041180	10	2	theme	transport	1495:1503	arg1	distribution					1512:1523	transport factor distribution	1495:1523	transport factor distribution	1495:1523	Furthermore, stress not only induced changes in transport factor distribution, but also upregulated post-translational modification of transport factors.
20041180	7	3	theme	subcellular	1007:1017	arg1	distributions					1019:1031	the subcellular distributions	1003:1031	the subcellular distributions of importin-alpha, CAS, and nucleoporins Nup153 and Nup88	1003:1089	Using recently developed tools for image acquisition and analysis, the subcellular distributions of importin-alpha, CAS, and nucleoporins Nup153 and Nup88 were quantified in different cellular compartments.
20041180	11	4	theme	O-GlcNAc	1718:1725	arg1	modification					1727:1738	the O-GlcNAc modification	1714:1738	the O-GlcNAc modification of Nup153	1714:1748	Our results are consistent with the idea that the phosphorylation of importin-alpha, CAS, Nup153, and Nup88, and the O-GlcNAc modification of Nup153 increase when cells are exposed to oxidant.
20041180	1	5	theme	exposure	249:256	arg1	survival					229:236	the survival	225:236	the survival of oxidant exposure	225:256	BACKGROUND Signaling through MEK-->ERK1/2 and PI3 kinases is implicated in many aspects of cell physiology, including the survival of oxidant exposure.
20041180	0	6	theme	target	73:78	arg1	factors					98:104	target nuclear transport factors	73:104	target nuclear transport factors	73:104	Dissecting the signaling events that impact classical nuclear import and target nuclear transport factors.
20041180	9	7	theme	kinase	1328:1333	arg1	signaling					1335:1343	PI3 kinase signaling	1324:1343	PI3 kinase signaling	1324:1343	Our results demonstrate that MEK and PI3 kinase signaling as well as oxidative stress control nuclear trafficking and the localization of transport components.
20041180	12	8	theme	PI3	1965:1967	arg1	kinase					1969:1974	PI3 kinase	1965:1974	PI3 kinase signaling	1965:1984	CONCLUSIONS/SIGNIFICANCE Our studies defined the complex regulation of classical nuclear import and identified key transport factors that are targeted by stress, MEK, and PI3 kinase signaling.
20041180	10	9	from	changes	1484:1490	arg1	distribution					1512:1523	transport factor distribution	1495:1523	transport factor distribution	1495:1523	Furthermore, stress not only induced changes in transport factor distribution, but also upregulated post-translational modification of transport factors.
20041180	5	10	theme	classical	741:749	arg1	import					759:764	classical nuclear import	741:764	classical nuclear import	741:764	This treatment activated MEK-->ERK1/2 as well as PI3 kinase-->Akt cascades and triggered the inhibition of classical nuclear import.
20041180	6	11	theme	factors	927:933	arg1	localization					897:908	the localization	893:908	the localization of key transport factors	893:933	To define the molecular mechanisms that regulate nuclear transport, we examined whether MEK and PI3 kinase signaling affected the localization of key transport factors.
20041180	12	12	theme	CONCLUSIONS/SIGNIFICANCE	1794:1817	arg1	studies					1823:1829	CONCLUSIONS/SIGNIFICANCE Our studies	1794:1829	CONCLUSIONS/SIGNIFICANCE Our studies	1794:1829	CONCLUSIONS/SIGNIFICANCE Our studies defined the complex regulation of classical nuclear import and identified key transport factors that are targeted by stress, MEK, and PI3 kinase signaling.
20041180	2	13	theme	numerous	283:290	arg1	processes					329:337	numerous physiological and pathophysiological processes	283:337	numerous physiological and pathophysiological processes	283:337	Oxidants play a role in numerous physiological and pathophysiological processes, many of which rely on transport in and out of the nucleus.
20041180	2	14	theme	physiological	292:304	arg1	processes					329:337	numerous physiological and pathophysiological processes	283:337	numerous physiological and pathophysiological processes	283:337	Oxidants play a role in numerous physiological and pathophysiological processes, many of which rely on transport in and out of the nucleus.
20041180	0	15	theme	transport	88:96	arg1	factors					98:104	target nuclear transport factors	73:104	target nuclear transport factors	73:104	Dissecting the signaling events that impact classical nuclear import and target nuclear transport factors.
20041180	6	16	theme	transport	917:925	arg1	factors					927:933	key transport factors	913:933	key transport factors	913:933	To define the molecular mechanisms that regulate nuclear transport, we examined whether MEK and PI3 kinase signaling affected the localization of key transport factors.
20041180	11	17	theme	importin-alpha	1670:1683	arg1	phosphorylation					1651:1665	the phosphorylation	1647:1665	the phosphorylation of importin-alpha, CAS, Nup153, and Nup88	1647:1707	Our results are consistent with the idea that the phosphorylation of importin-alpha, CAS, Nup153, and Nup88, and the O-GlcNAc modification of Nup153 increase when cells are exposed to oxidant.
20041180	11	17	theme	importin-alpha	1670:1683	arg1	modification					1727:1738	the O-GlcNAc modification	1714:1738	the O-GlcNAc modification of Nup153	1714:1748	Our results are consistent with the idea that the phosphorylation of importin-alpha, CAS, Nup153, and Nup88, and the O-GlcNAc modification of Nup153 increase when cells are exposed to oxidant.
20041180	11	18	theme	CAS	1686:1688	arg1	phosphorylation					1651:1665	the phosphorylation	1647:1665	the phosphorylation of importin-alpha, CAS, Nup153, and Nup88	1647:1707	Our results are consistent with the idea that the phosphorylation of importin-alpha, CAS, Nup153, and Nup88, and the O-GlcNAc modification of Nup153 increase when cells are exposed to oxidant.
20041180	11	18	theme	CAS	1686:1688	arg1	modification					1727:1738	the O-GlcNAc modification	1714:1738	the O-GlcNAc modification of Nup153	1714:1748	Our results are consistent with the idea that the phosphorylation of importin-alpha, CAS, Nup153, and Nup88, and the O-GlcNAc modification of Nup153 increase when cells are exposed to oxidant.
20041180	12	19	theme	key	1905:1907	arg1	factors					1919:1925	key transport factors	1905:1925	key transport factors that are targeted by stress, MEK, and PI3 kinase signaling	1905:1984	CONCLUSIONS/SIGNIFICANCE Our studies defined the complex regulation of classical nuclear import and identified key transport factors that are targeted by stress, MEK, and PI3 kinase signaling.
20041180	12	20	theme	classical	1865:1873	arg1	import					1883:1888	classical nuclear import	1865:1888	classical nuclear import	1865:1888	CONCLUSIONS/SIGNIFICANCE Our studies defined the complex regulation of classical nuclear import and identified key transport factors that are targeted by stress, MEK, and PI3 kinase signaling.
20041180	5	21	theme	import	759:764	arg1	inhibition					727:736	the inhibition	723:736	the inhibition of classical nuclear import	723:764	This treatment activated MEK-->ERK1/2 as well as PI3 kinase-->Akt cascades and triggered the inhibition of classical nuclear import.
20041180	6	22	theme	key	913:915	arg1	factors					927:933	key transport factors	913:933	key transport factors	913:933	To define the molecular mechanisms that regulate nuclear transport, we examined whether MEK and PI3 kinase signaling affected the localization of key transport factors.
20041180	12	23	theme	import	1883:1888	arg1	regulation					1851:1860	the complex regulation	1839:1860	the complex regulation of classical nuclear import	1839:1888	CONCLUSIONS/SIGNIFICANCE Our studies defined the complex regulation of classical nuclear import and identified key transport factors that are targeted by stress, MEK, and PI3 kinase signaling.
20041180	8	24	theme	factors	1220:1226	arg1	localization					1194:1205	the localization	1190:1205	the localization of transport factors	1190:1226	These studies identified specific profiles for the localization of transport factors in the nucleus and cytoplasm, and at the nuclear envelope.
20041180	4	25	theme	METHODOLOGY/PRINCIPAL	478:498	arg1	FINDINGS					500:507	METHODOLOGY/PRINCIPAL FINDINGS	478:507	METHODOLOGY/PRINCIPAL FINDINGS	478:507	METHODOLOGY/PRINCIPAL FINDINGS To better understand the effect of stress on nucleocytoplasmic trafficking, we exposed cells to the oxidant diethyl maleate.
20041180	6	26	theme	nuclear	816:822	arg1	transport					824:832	nuclear transport	816:832	nuclear transport	816:832	To define the molecular mechanisms that regulate nuclear transport, we examined whether MEK and PI3 kinase signaling affected the localization of key transport factors.
20041180	1	27	theme	many	182:185	arg1	aspects					187:193	many aspects	182:193	many aspects	182:193	BACKGROUND Signaling through MEK-->ERK1/2 and PI3 kinases is implicated in many aspects of cell physiology, including the survival of oxidant exposure.
20041180	1	27	theme	many	182:185	arg1	survival					229:236	the survival	225:236	the survival of oxidant exposure	225:256	BACKGROUND Signaling through MEK-->ERK1/2 and PI3 kinases is implicated in many aspects of cell physiology, including the survival of oxidant exposure.
20041180	9	28	theme	oxidative	1356:1364	arg1	stress					1366:1371	oxidative stress	1356:1371	oxidative stress	1356:1371	Our results demonstrate that MEK and PI3 kinase signaling as well as oxidative stress control nuclear trafficking and the localization of transport components.
20041180	7	29	theme	different	1110:1118	arg1	compartments					1129:1140	different cellular compartments	1110:1140	different cellular compartments	1110:1140	Using recently developed tools for image acquisition and analysis, the subcellular distributions of importin-alpha, CAS, and nucleoporins Nup153 and Nup88 were quantified in different cellular compartments.
20041180	7	30	theme	image	971:975	arg1	acquisition					977:987	image acquisition	971:987	image acquisition	971:987	Using recently developed tools for image acquisition and analysis, the subcellular distributions of importin-alpha, CAS, and nucleoporins Nup153 and Nup88 were quantified in different cellular compartments.
20041180	2	31	theme	processes	329:337	arg1	many					340:343	many	340:343	many	340:343	Oxidants play a role in numerous physiological and pathophysiological processes, many of which rely on transport in and out of the nucleus.
20041180	2	31	theme	processes	329:337	arg1	processes					329:337	numerous physiological and pathophysiological processes	283:337	numerous physiological and pathophysiological processes	283:337	Oxidants play a role in numerous physiological and pathophysiological processes, many of which rely on transport in and out of the nucleus.
20041180	10	32	theme	factors	1592:1598	arg1	modification					1566:1577	post-translational modification	1547:1577	post-translational modification of transport factors	1547:1598	Furthermore, stress not only induced changes in transport factor distribution, but also upregulated post-translational modification of transport factors.
20041180	4	33	theme	nucleocytoplasmic	554:570	arg1	trafficking					572:582	nucleocytoplasmic trafficking	554:582	nucleocytoplasmic trafficking	554:582	METHODOLOGY/PRINCIPAL FINDINGS To better understand the effect of stress on nucleocytoplasmic trafficking, we exposed cells to the oxidant diethyl maleate.
20041180	7	34	theme	cellular	1120:1127	arg1	compartments					1129:1140	different cellular compartments	1110:1140	different cellular compartments	1110:1140	Using recently developed tools for image acquisition and analysis, the subcellular distributions of importin-alpha, CAS, and nucleoporins Nup153 and Nup88 were quantified in different cellular compartments.
20041180	7	35	theme	developed	951:959	arg1	tools					961:965	recently developed tools	942:965	recently developed tools for image acquisition and analysis	942:1000	Using recently developed tools for image acquisition and analysis, the subcellular distributions of importin-alpha, CAS, and nucleoporins Nup153 and Nup88 were quantified in different cellular compartments.
20041180	2	36	theme	pathophysiological	310:327	arg1	processes					329:337	numerous physiological and pathophysiological processes	283:337	numerous physiological and pathophysiological processes	283:337	Oxidants play a role in numerous physiological and pathophysiological processes, many of which rely on transport in and out of the nucleus.
20041180	3	37	theme	oxidative	412:420	arg1	stress					422:427	oxidative stress	412:427	oxidative stress	412:427	However, how oxidative stress impacts nuclear trafficking is not well defined.
20041180	12	38	theme	kinase	1969:1974	arg1	signaling					1976:1984	PI3 kinase signaling	1965:1984	PI3 kinase signaling	1965:1984	CONCLUSIONS/SIGNIFICANCE Our studies defined the complex regulation of classical nuclear import and identified key transport factors that are targeted by stress, MEK, and PI3 kinase signaling.
20041180	2	39	from	transport	362:370	arg1	and					375:377	and	375:377	and	375:377	Oxidants play a role in numerous physiological and pathophysiological processes, many of which rely on transport in and out of the nucleus.
20041180	7	40	dep	nucleoporins	1061:1072	arg1	Nup153					1074:1079	Nup153	1074:1079	Nup153	1074:1079	Using recently developed tools for image acquisition and analysis, the subcellular distributions of importin-alpha, CAS, and nucleoporins Nup153 and Nup88 were quantified in different cellular compartments.
20041180	7	40	dep	nucleoporins	1061:1072	arg1	nucleoporins					1061:1072	nucleoporins Nup153 and Nup88	1061:1089	nucleoporins Nup153 and Nup88	1061:1089	Using recently developed tools for image acquisition and analysis, the subcellular distributions of importin-alpha, CAS, and nucleoporins Nup153 and Nup88 were quantified in different cellular compartments.
20041180	7	40	dep	nucleoporins	1061:1072	arg1	Nup88					1085:1089	Nup88	1085:1089	Nup88	1085:1089	Using recently developed tools for image acquisition and analysis, the subcellular distributions of importin-alpha, CAS, and nucleoporins Nup153 and Nup88 were quantified in different cellular compartments.
20041180	10	41	theme	factor	1505:1510	arg1	distribution					1512:1523	transport factor distribution	1495:1523	transport factor distribution	1495:1523	Furthermore, stress not only induced changes in transport factor distribution, but also upregulated post-translational modification of transport factors.
20041180	1	42	theme	cell	198:201	arg1	physiology					203:212	cell physiology	198:212	cell physiology	198:212	BACKGROUND Signaling through MEK-->ERK1/2 and PI3 kinases is implicated in many aspects of cell physiology, including the survival of oxidant exposure.
20041180	0	43	theme	signaling	15:23	arg1	events					25:30	the signaling events	11:30	the signaling events that impact classical nuclear import and target nuclear transport factors	11:104	Dissecting the signaling events that impact classical nuclear import and target nuclear transport factors.
20041180	9	44	theme	nuclear	1381:1387	arg1	trafficking					1389:1399	nuclear trafficking	1381:1399	nuclear trafficking	1381:1399	Our results demonstrate that MEK and PI3 kinase signaling as well as oxidative stress control nuclear trafficking and the localization of transport components.
20041180	10	45	theme	post-translational	1547:1564	arg1	modification					1566:1577	post-translational modification	1547:1577	post-translational modification of transport factors	1547:1598	Furthermore, stress not only induced changes in transport factor distribution, but also upregulated post-translational modification of transport factors.
20041180	1	46	theme	BACKGROUND	107:116	arg1	Signaling					118:126	BACKGROUND Signaling	107:126	BACKGROUND Signaling through MEK-->ERK1/2 and PI3 kinases	107:163	BACKGROUND Signaling through MEK-->ERK1/2 and PI3 kinases is implicated in many aspects of cell physiology, including the survival of oxidant exposure.
20041180	1	47	theme	physiology	203:212	arg1	aspects					187:193	many aspects	182:193	many aspects	182:193	BACKGROUND Signaling through MEK-->ERK1/2 and PI3 kinases is implicated in many aspects of cell physiology, including the survival of oxidant exposure.
20041180	1	47	theme	physiology	203:212	arg1	survival					229:236	the survival	225:236	the survival of oxidant exposure	225:256	BACKGROUND Signaling through MEK-->ERK1/2 and PI3 kinases is implicated in many aspects of cell physiology, including the survival of oxidant exposure.
20041180	12	48	theme	complex	1843:1849	arg1	regulation					1851:1860	the complex regulation	1839:1860	the complex regulation of classical nuclear import	1839:1888	CONCLUSIONS/SIGNIFICANCE Our studies defined the complex regulation of classical nuclear import and identified key transport factors that are targeted by stress, MEK, and PI3 kinase signaling.
20041180	3	49	theme	nuclear	437:443	arg1	trafficking					445:455	nuclear trafficking	437:455	nuclear trafficking	437:455	However, how oxidative stress impacts nuclear trafficking is not well defined.
20041180	5	50	theme	nuclear	751:757	arg1	import					759:764	classical nuclear import	741:764	classical nuclear import	741:764	This treatment activated MEK-->ERK1/2 as well as PI3 kinase-->Akt cascades and triggered the inhibition of classical nuclear import.
20041180	2	51	dep	nucleus	390:396	arg1	out					379:381	out	379:381	out	379:381	Oxidants play a role in numerous physiological and pathophysiological processes, many of which rely on transport in and out of the nucleus.
20041180	6	52	theme	molecular	781:789	arg1	mechanisms					791:800	the molecular mechanisms	777:800	the molecular mechanisms that regulate nuclear transport	777:832	To define the molecular mechanisms that regulate nuclear transport, we examined whether MEK and PI3 kinase signaling affected the localization of key transport factors.
20041180	0	53	theme	nuclear	54:60	arg1	import					62:67	classical nuclear import	44:67	classical nuclear import	44:67	Dissecting the signaling events that impact classical nuclear import and target nuclear transport factors.
20041180	8	54	theme	transport	1210:1218	arg1	factors					1220:1226	transport factors	1210:1226	transport factors	1210:1226	These studies identified specific profiles for the localization of transport factors in the nucleus and cytoplasm, and at the nuclear envelope.
20041180	5	55	theme	PI3	683:685	arg1	cascades					700:707	PI3 kinase-->Akt cascades	683:707	MEK-->ERK1/2 as well as PI3 kinase-->Akt cascades	659:707	This treatment activated MEK-->ERK1/2 as well as PI3 kinase-->Akt cascades and triggered the inhibition of classical nuclear import.
20041180	6	56	theme	kinase	867:872	arg1	signaling					874:882	PI3 kinase signaling	863:882	PI3 kinase signaling	863:882	To define the molecular mechanisms that regulate nuclear transport, we examined whether MEK and PI3 kinase signaling affected the localization of key transport factors.
20041180	10	57	theme	transport	1582:1590	arg1	factors					1592:1598	transport factors	1582:1598	transport factors	1582:1598	Furthermore, stress not only induced changes in transport factor distribution, but also upregulated post-translational modification of transport factors.
20041180	0	58	theme	classical	44:52	arg1	import					62:67	classical nuclear import	44:67	classical nuclear import	44:67	Dissecting the signaling events that impact classical nuclear import and target nuclear transport factors.
20041180	4	59	theme	stress	544:549	arg1	effect					534:539	the effect	530:539	the effect of stress on nucleocytoplasmic trafficking	530:582	METHODOLOGY/PRINCIPAL FINDINGS To better understand the effect of stress on nucleocytoplasmic trafficking, we exposed cells to the oxidant diethyl maleate.
20041180	5	60	theme	kinase-->Akt	687:698	arg1	cascades					700:707	PI3 kinase-->Akt cascades	683:707	MEK-->ERK1/2 as well as PI3 kinase-->Akt cascades	659:707	This treatment activated MEK-->ERK1/2 as well as PI3 kinase-->Akt cascades and triggered the inhibition of classical nuclear import.
20041180	6	61	theme	PI3	863:865	arg1	signaling					874:882	PI3 kinase signaling	863:882	PI3 kinase signaling	863:882	To define the molecular mechanisms that regulate nuclear transport, we examined whether MEK and PI3 kinase signaling affected the localization of key transport factors.
20041180	7	62	theme	importin-alpha	1036:1049	arg1	distributions					1019:1031	the subcellular distributions	1003:1031	the subcellular distributions of importin-alpha, CAS, and nucleoporins Nup153 and Nup88	1003:1089	Using recently developed tools for image acquisition and analysis, the subcellular distributions of importin-alpha, CAS, and nucleoporins Nup153 and Nup88 were quantified in different cellular compartments.
20041180	11	63	with	consistent	1617:1626	arg1	idea					1637:1640	the idea that the phosphorylation of importin-alpha, CAS, Nup153, and Nup88, and the O-GlcNAc modification of Nup153 increase when cells are exposed to oxidant	1633:1791	the idea that the phosphorylation of importin-alpha, CAS, Nup153, and Nup88, and the O-GlcNAc modification of Nup153 increase when cells are exposed to oxidant	1633:1791	Our results are consistent with the idea that the phosphorylation of importin-alpha, CAS, Nup153, and Nup88, and the O-GlcNAc modification of Nup153 increase when cells are exposed to oxidant.
20041180	8	64	theme	specific	1168:1175	arg1	profiles					1177:1184	specific profiles	1168:1184	specific profiles for the localization of transport factors	1168:1226	These studies identified specific profiles for the localization of transport factors in the nucleus and cytoplasm, and at the nuclear envelope.
20041180	4	65	theme	oxidant	609:615	arg1	maleate					625:631	the oxidant diethyl maleate	605:631	the oxidant diethyl maleate	605:631	METHODOLOGY/PRINCIPAL FINDINGS To better understand the effect of stress on nucleocytoplasmic trafficking, we exposed cells to the oxidant diethyl maleate.
20041180	7	66	theme	nucleoporins	1061:1072	arg1	distributions					1019:1031	the subcellular distributions	1003:1031	the subcellular distributions of importin-alpha, CAS, and nucleoporins Nup153 and Nup88	1003:1089	Using recently developed tools for image acquisition and analysis, the subcellular distributions of importin-alpha, CAS, and nucleoporins Nup153 and Nup88 were quantified in different cellular compartments.
20041180	7	67	theme	CAS	1052:1054	arg1	distributions					1019:1031	the subcellular distributions	1003:1031	the subcellular distributions of importin-alpha, CAS, and nucleoporins Nup153 and Nup88	1003:1089	Using recently developed tools for image acquisition and analysis, the subcellular distributions of importin-alpha, CAS, and nucleoporins Nup153 and Nup88 were quantified in different cellular compartments.
20041180	9	68	theme	components	1435:1444	arg1	trafficking					1389:1399	nuclear trafficking	1381:1399	nuclear trafficking	1381:1399	Our results demonstrate that MEK and PI3 kinase signaling as well as oxidative stress control nuclear trafficking and the localization of transport components.
20041180	9	68	theme	components	1435:1444	arg1	localization					1409:1420	the localization	1405:1420	the localization of transport components	1405:1444	Our results demonstrate that MEK and PI3 kinase signaling as well as oxidative stress control nuclear trafficking and the localization of transport components.
20041180	12	69	theme	transport	1909:1917	arg1	factors					1919:1925	key transport factors	1905:1925	key transport factors that are targeted by stress, MEK, and PI3 kinase signaling	1905:1984	CONCLUSIONS/SIGNIFICANCE Our studies defined the complex regulation of classical nuclear import and identified key transport factors that are targeted by stress, MEK, and PI3 kinase signaling.
20041180	11	70	theme	Nup153	1691:1696	arg1	phosphorylation					1651:1665	the phosphorylation	1647:1665	the phosphorylation of importin-alpha, CAS, Nup153, and Nup88	1647:1707	Our results are consistent with the idea that the phosphorylation of importin-alpha, CAS, Nup153, and Nup88, and the O-GlcNAc modification of Nup153 increase when cells are exposed to oxidant.
20041180	11	70	theme	Nup153	1691:1696	arg1	modification					1727:1738	the O-GlcNAc modification	1714:1738	the O-GlcNAc modification of Nup153	1714:1748	Our results are consistent with the idea that the phosphorylation of importin-alpha, CAS, Nup153, and Nup88, and the O-GlcNAc modification of Nup153 increase when cells are exposed to oxidant.
20041180	1	71	theme	PI3	153:155	arg1	kinases					157:163	PI3 kinases	153:163	PI3 kinases	153:163	BACKGROUND Signaling through MEK-->ERK1/2 and PI3 kinases is implicated in many aspects of cell physiology, including the survival of oxidant exposure.
20041180	8	72	theme	nuclear	1269:1275	arg1	envelope					1277:1284	the nuclear envelope	1265:1284	the nuclear envelope	1265:1284	These studies identified specific profiles for the localization of transport factors in the nucleus and cytoplasm, and at the nuclear envelope.
20041180	4	73	from	effect	534:539	arg1	trafficking					572:582	nucleocytoplasmic trafficking	554:582	nucleocytoplasmic trafficking	554:582	METHODOLOGY/PRINCIPAL FINDINGS To better understand the effect of stress on nucleocytoplasmic trafficking, we exposed cells to the oxidant diethyl maleate.
20041180	11	74	theme	Nup88	1703:1707	arg1	phosphorylation					1651:1665	the phosphorylation	1647:1665	the phosphorylation of importin-alpha, CAS, Nup153, and Nup88	1647:1707	Our results are consistent with the idea that the phosphorylation of importin-alpha, CAS, Nup153, and Nup88, and the O-GlcNAc modification of Nup153 increase when cells are exposed to oxidant.
20041180	11	74	theme	Nup88	1703:1707	arg1	modification					1727:1738	the O-GlcNAc modification	1714:1738	the O-GlcNAc modification of Nup153	1714:1748	Our results are consistent with the idea that the phosphorylation of importin-alpha, CAS, Nup153, and Nup88, and the O-GlcNAc modification of Nup153 increase when cells are exposed to oxidant.
20041180	1	75	theme	oxidant	241:247	arg1	exposure					249:256	oxidant exposure	241:256	oxidant exposure	241:256	BACKGROUND Signaling through MEK-->ERK1/2 and PI3 kinases is implicated in many aspects of cell physiology, including the survival of oxidant exposure.
20041180	12	76	theme	nuclear	1875:1881	arg1	import					1883:1888	classical nuclear import	1865:1888	classical nuclear import	1865:1888	CONCLUSIONS/SIGNIFICANCE Our studies defined the complex regulation of classical nuclear import and identified key transport factors that are targeted by stress, MEK, and PI3 kinase signaling.
20041180	9	77	theme	transport	1425:1433	arg1	components					1435:1444	transport components	1425:1444	transport components	1425:1444	Our results demonstrate that MEK and PI3 kinase signaling as well as oxidative stress control nuclear trafficking and the localization of transport components.
20041180	11	78	theme	Nup153	1743:1748	arg1	phosphorylation					1651:1665	the phosphorylation	1647:1665	the phosphorylation of importin-alpha, CAS, Nup153, and Nup88	1647:1707	Our results are consistent with the idea that the phosphorylation of importin-alpha, CAS, Nup153, and Nup88, and the O-GlcNAc modification of Nup153 increase when cells are exposed to oxidant.
20041180	11	78	theme	Nup153	1743:1748	arg1	modification					1727:1738	the O-GlcNAc modification	1714:1738	the O-GlcNAc modification of Nup153	1714:1748	Our results are consistent with the idea that the phosphorylation of importin-alpha, CAS, Nup153, and Nup88, and the O-GlcNAc modification of Nup153 increase when cells are exposed to oxidant.
20041180	4	79	theme	diethyl	617:623	arg1	maleate					625:631	the oxidant diethyl maleate	605:631	the oxidant diethyl maleate	605:631	METHODOLOGY/PRINCIPAL FINDINGS To better understand the effect of stress on nucleocytoplasmic trafficking, we exposed cells to the oxidant diethyl maleate.
29196265	4	0	theme	mitotic	594:600	arg1	M1					573:574	Forkhead box M1	560:574	Forkhead box M1 (FOXM1)	560:582	Forkhead box M1 (FOXM1), a master mitotic transcription factor, has been implicated in all major hallmarks of cancer, and is wildly expressed in solid tumors.
29196265	4	0	theme	mitotic	594:600	arg1	factor					616:621	a master mitotic transcription factor	585:621	a master mitotic transcription factor	585:621	Forkhead box M1 (FOXM1), a master mitotic transcription factor, has been implicated in all major hallmarks of cancer, and is wildly expressed in solid tumors.
29196265	10	1	theme	cancer	1835:1840	arg1	due					1882:1884	due	1882:1884	due	1882:1884	Taken together, we suggest that high glucose and elevated O-GlcNAcylation stabilize FOXM1 protein by its reduced degradation via GSK-3β inactivation in MKN45 cells, suggesting that the higher risk of gastric cancer in diabetic patients could be partially due to O-GlcNAcylation-mediated FOXM1 stabilization.
29196265	10	1	theme	cancer	1835:1840	arg1	risk					1819:1822	the higher risk	1808:1822	the higher risk of gastric cancer in diabetic patients	1808:1861	Taken together, we suggest that high glucose and elevated O-GlcNAcylation stabilize FOXM1 protein by its reduced degradation via GSK-3β inactivation in MKN45 cells, suggesting that the higher risk of gastric cancer in diabetic patients could be partially due to O-GlcNAcylation-mediated FOXM1 stabilization.
29196265	4	2	theme	cancer	670:675	arg1	hallmarks					657:665	all major hallmarks	647:665	all major hallmarks of cancer	647:675	Forkhead box M1 (FOXM1), a master mitotic transcription factor, has been implicated in all major hallmarks of cancer, and is wildly expressed in solid tumors.
29196265	6	3	theme	FOXM1	1196:1200	arg1	ubiquitination					1202:1215	FOXM1 ubiquitination	1196:1215	FOXM1 ubiquitination	1196:1215	To investigate the molecular mechanisms by which FOXM1 protein expression is regulated by O-GlcNAcylation, the effect of high glucose and TMG on FOXM1 ubiquitination was examined in MKN45 cells.
29196265	10	4	theme	high	1659:1662	arg1	glucose					1664:1670	high glucose	1659:1670	high glucose	1659:1670	Taken together, we suggest that high glucose and elevated O-GlcNAcylation stabilize FOXM1 protein by its reduced degradation via GSK-3β inactivation in MKN45 cells, suggesting that the higher risk of gastric cancer in diabetic patients could be partially due to O-GlcNAcylation-mediated FOXM1 stabilization.
29196265	8	5	gly	O-GlcNAcylation	1380:1394	arg1	GSK-3β					1433:1438	GSK-3β	1433:1438	GSK-3β	1433:1438	However, the O-GlcNAcylation was not detected on FOXM1 but not on GSK-3β.
29196265	8	5	gly	O-GlcNAcylation	1380:1394	arg1	FOXM1					1416:1420	FOXM1	1416:1420	FOXM1	1416:1420	However, the O-GlcNAcylation was not detected on FOXM1 but not on GSK-3β.
29196265	9	6	theme	inhibitors	1600:1609	arg1	treatment					1580:1588	treatment	1580:1588	treatment of GSK-3β inhibitors in MKN45 cells	1580:1624	High glucose and TMG treatment increased phospho-serine 9 GSK-3β, an inactive form, and the degradation of FOXM1 protein was suppressed by treatment of GSK-3β inhibitors in MKN45 cells.
29196265	6	7	theme	protein	1106:1112	arg1	expression					1114:1123	FOXM1 protein expression	1100:1123	FOXM1 protein expression	1100:1123	To investigate the molecular mechanisms by which FOXM1 protein expression is regulated by O-GlcNAcylation, the effect of high glucose and TMG on FOXM1 ubiquitination was examined in MKN45 cells.
29196265	10	8	theme	FOXM1	1914:1918	arg1	stabilization					1920:1932	O-GlcNAcylation-mediated FOXM1 stabilization	1889:1932	O-GlcNAcylation-mediated FOXM1 stabilization	1889:1932	Taken together, we suggest that high glucose and elevated O-GlcNAcylation stabilize FOXM1 protein by its reduced degradation via GSK-3β inactivation in MKN45 cells, suggesting that the higher risk of gastric cancer in diabetic patients could be partially due to O-GlcNAcylation-mediated FOXM1 stabilization.
29196265	6	9	theme	TMG	1189:1191	arg1	effect					1162:1167	the effect	1158:1167	the effect of high glucose and TMG on FOXM1 ubiquitination	1158:1215	To investigate the molecular mechanisms by which FOXM1 protein expression is regulated by O-GlcNAcylation, the effect of high glucose and TMG on FOXM1 ubiquitination was examined in MKN45 cells.
29196265	10	10	theme	FOXM1	1711:1715	arg1	protein					1717:1723	FOXM1 protein	1711:1723	FOXM1 protein	1711:1723	Taken together, we suggest that high glucose and elevated O-GlcNAcylation stabilize FOXM1 protein by its reduced degradation via GSK-3β inactivation in MKN45 cells, suggesting that the higher risk of gastric cancer in diabetic patients could be partially due to O-GlcNAcylation-mediated FOXM1 stabilization.
29196265	5	11	theme	O-GlcNAc	852:859	arg1	hydrolase					861:869	O-GlcNAc hydrolase	852:869	O-GlcNAc hydrolase	852:869	Given that FOXM1 expression was reported to be elevated in gastric cancer, we examined the effect of high glucose or an inhibitor of O-GlcNAc hydrolase, Thiamet G (TMG), on FOXM1 protein expression in a human gastric cancer cell line, MKN45 cells, and confirmed that FOXM1 protein level and the cell proliferation were upregulated.
29196265	7	12	theme	high	1335:1338	arg1	glucose					1340:1346	high glucose	1335:1346	high glucose	1335:1346	As a result, the ubiquitination and degradation of FOXM1 protein were both suppressed by high glucose and TMG treatment.
29196265	0	13	theme	cell	126:129	arg1	MKN45 cells					137:147	MKN45 cells	137:147	MKN45 cells	137:147	Elevated O-GlcNAcylation stabilizes FOXM1 by its reduced degradation through GSK-3β inactivation in a human gastric carcinoma cell line, MKN45 cells.
29196265	0	13	theme	cell	126:129	arg1	line					131:134	a human gastric carcinoma cell line	100:134	a human gastric carcinoma cell line	100:134	Elevated O-GlcNAcylation stabilizes FOXM1 by its reduced degradation through GSK-3β inactivation in a human gastric carcinoma cell line, MKN45 cells.
29196265	5	14	theme	high	820:823	arg1	glucose					825:831	high glucose	820:831	high glucose	820:831	Given that FOXM1 expression was reported to be elevated in gastric cancer, we examined the effect of high glucose or an inhibitor of O-GlcNAc hydrolase, Thiamet G (TMG), on FOXM1 protein expression in a human gastric cancer cell line, MKN45 cells, and confirmed that FOXM1 protein level and the cell proliferation were upregulated.
29196265	0	15	from	inactivation	84:95	arg1	MKN45 cells					137:147	MKN45 cells	137:147	MKN45 cells	137:147	Elevated O-GlcNAcylation stabilizes FOXM1 by its reduced degradation through GSK-3β inactivation in a human gastric carcinoma cell line, MKN45 cells.
29196265	0	15	from	inactivation	84:95	arg1	line					131:134	a human gastric carcinoma cell line	100:134	a human gastric carcinoma cell line	100:134	Elevated O-GlcNAcylation stabilizes FOXM1 by its reduced degradation through GSK-3β inactivation in a human gastric carcinoma cell line, MKN45 cells.
29196265	5	16	theme	cell	1014:1017	arg1	proliferation					1019:1031	the cell proliferation	1010:1031	the cell proliferation	1010:1031	Given that FOXM1 expression was reported to be elevated in gastric cancer, we examined the effect of high glucose or an inhibitor of O-GlcNAc hydrolase, Thiamet G (TMG), on FOXM1 protein expression in a human gastric cancer cell line, MKN45 cells, and confirmed that FOXM1 protein level and the cell proliferation were upregulated.
29196265	2	17	theme	Elevated	264:271	arg1	O-GlcNAcylation					273:287	Elevated O-GlcNAcylation	264:287	Elevated O-GlcNAcylation	264:287	Elevated O-GlcNAcylation is a general feature of cancer and contributes to cancer progression, and recent studies indicate the contribution to increasing incidence of various types of cancer in diabetic patients.
29196265	2	17	theme	Elevated	264:271	arg1	feature					302:308	a general feature	292:308	a general feature of cancer	292:318	Elevated O-GlcNAcylation is a general feature of cancer and contributes to cancer progression, and recent studies indicate the contribution to increasing incidence of various types of cancer in diabetic patients.
29196265	1	18	theme	intracellular	239:251	arg1	signaling					253:261	intracellular signaling	239:261	intracellular signaling	239:261	O-GlcNAcylation is a dynamic post-translational modification of cytonuclear proteins for intracellular signaling.
29196265	9	19	from	treatment	1580:1588	arg1	MKN45 cells					1614:1624	MKN45 cells	1614:1624	MKN45 cells	1614:1624	High glucose and TMG treatment increased phospho-serine 9 GSK-3β, an inactive form, and the degradation of FOXM1 protein was suppressed by treatment of GSK-3β inhibitors in MKN45 cells.
29196265	6	20	theme	high	1172:1175	arg1	glucose					1177:1183	high glucose	1172:1183	high glucose	1172:1183	To investigate the molecular mechanisms by which FOXM1 protein expression is regulated by O-GlcNAcylation, the effect of high glucose and TMG on FOXM1 ubiquitination was examined in MKN45 cells.
29196265	7	21	theme	FOXM1	1297:1301	arg1	protein					1303:1309	FOXM1 protein	1297:1309	FOXM1 protein	1297:1309	As a result, the ubiquitination and degradation of FOXM1 protein were both suppressed by high glucose and TMG treatment.
29196265	5	22	theme	protein	992:998	arg1	level					1000:1004	FOXM1 protein level	986:1004	FOXM1 protein level	986:1004	Given that FOXM1 expression was reported to be elevated in gastric cancer, we examined the effect of high glucose or an inhibitor of O-GlcNAc hydrolase, Thiamet G (TMG), on FOXM1 protein expression in a human gastric cancer cell line, MKN45 cells, and confirmed that FOXM1 protein level and the cell proliferation were upregulated.
29196265	2	23	theme	general	294:300	arg1	O-GlcNAcylation					273:287	Elevated O-GlcNAcylation	264:287	Elevated O-GlcNAcylation	264:287	Elevated O-GlcNAcylation is a general feature of cancer and contributes to cancer progression, and recent studies indicate the contribution to increasing incidence of various types of cancer in diabetic patients.
29196265	2	23	theme	general	294:300	arg1	feature					302:308	a general feature	292:308	a general feature of cancer	292:318	Elevated O-GlcNAcylation is a general feature of cancer and contributes to cancer progression, and recent studies indicate the contribution to increasing incidence of various types of cancer in diabetic patients.
29196265	8	24	located	detected	1404:1411	arg1	FOXM1					1416:1420	FOXM1	1416:1420	FOXM1	1416:1420	However, the O-GlcNAcylation was not detected on FOXM1 but not on GSK-3β.
29196265	8	24	located	detected	1404:1411	arg2	O-GlcNAcylation					1380:1394	the O-GlcNAcylation	1376:1394	the O-GlcNAcylation	1376:1394	However, the O-GlcNAcylation was not detected on FOXM1 but not on GSK-3β.
29196265	9	25	theme	TMG	1458:1460	arg1	treatment					1462:1470	TMG treatment	1458:1470	TMG treatment	1458:1470	High glucose and TMG treatment increased phospho-serine 9 GSK-3β, an inactive form, and the degradation of FOXM1 protein was suppressed by treatment of GSK-3β inhibitors in MKN45 cells.
29196265	5	26	theme	FOXM1	730:734	arg1	expression					736:745	FOXM1 expression	730:745	FOXM1 expression	730:745	Given that FOXM1 expression was reported to be elevated in gastric cancer, we examined the effect of high glucose or an inhibitor of O-GlcNAc hydrolase, Thiamet G (TMG), on FOXM1 protein expression in a human gastric cancer cell line, MKN45 cells, and confirmed that FOXM1 protein level and the cell proliferation were upregulated.
29196265	2	27	theme	types	439:443	arg1	incidence					418:426	increasing incidence	407:426	increasing incidence of various types of cancer	407:453	Elevated O-GlcNAcylation is a general feature of cancer and contributes to cancer progression, and recent studies indicate the contribution to increasing incidence of various types of cancer in diabetic patients.
29196265	0	28	theme	gastric	108:114	arg1	MKN45 cells					137:147	MKN45 cells	137:147	MKN45 cells	137:147	Elevated O-GlcNAcylation stabilizes FOXM1 by its reduced degradation through GSK-3β inactivation in a human gastric carcinoma cell line, MKN45 cells.
29196265	0	28	theme	gastric	108:114	arg1	line					131:134	a human gastric carcinoma cell line	100:134	a human gastric carcinoma cell line	100:134	Elevated O-GlcNAcylation stabilizes FOXM1 by its reduced degradation through GSK-3β inactivation in a human gastric carcinoma cell line, MKN45 cells.
29196265	5	29	theme	gastric	928:934	arg1	line					948:951	a human gastric cancer cell line	920:951	a human gastric cancer cell line	920:951	Given that FOXM1 expression was reported to be elevated in gastric cancer, we examined the effect of high glucose or an inhibitor of O-GlcNAc hydrolase, Thiamet G (TMG), on FOXM1 protein expression in a human gastric cancer cell line, MKN45 cells, and confirmed that FOXM1 protein level and the cell proliferation were upregulated.
29196265	5	29	theme	gastric	928:934	arg1	MKN45 cells					954:964	MKN45 cells	954:964	MKN45 cells	954:964	Given that FOXM1 expression was reported to be elevated in gastric cancer, we examined the effect of high glucose or an inhibitor of O-GlcNAc hydrolase, Thiamet G (TMG), on FOXM1 protein expression in a human gastric cancer cell line, MKN45 cells, and confirmed that FOXM1 protein level and the cell proliferation were upregulated.
29196265	0	30	theme	Elevated	0:7	arg1	O-GlcNAcylation					9:23	Elevated O-GlcNAcylation	0:23	Elevated O-GlcNAcylation	0:23	Elevated O-GlcNAcylation stabilizes FOXM1 by its reduced degradation through GSK-3β inactivation in a human gastric carcinoma cell line, MKN45 cells.
29196265	5	31	theme	FOXM1	892:896	arg1	expression					906:915	FOXM1 protein expression	892:915	FOXM1 protein expression in a human gastric cancer cell line, MKN45 cells,	892:965	Given that FOXM1 expression was reported to be elevated in gastric cancer, we examined the effect of high glucose or an inhibitor of O-GlcNAc hydrolase, Thiamet G (TMG), on FOXM1 protein expression in a human gastric cancer cell line, MKN45 cells, and confirmed that FOXM1 protein level and the cell proliferation were upregulated.
29196265	2	32	theme	diabetic	458:465	arg1	patients					467:474	diabetic patients	458:474	diabetic patients	458:474	Elevated O-GlcNAcylation is a general feature of cancer and contributes to cancer progression, and recent studies indicate the contribution to increasing incidence of various types of cancer in diabetic patients.
29196265	9	33	theme	inactive	1510:1517	arg1	form					1519:1522	an inactive form	1507:1522	an inactive form	1507:1522	High glucose and TMG treatment increased phospho-serine 9 GSK-3β, an inactive form, and the degradation of FOXM1 protein was suppressed by treatment of GSK-3β inhibitors in MKN45 cells.
29196265	9	33	theme	inactive	1510:1517	arg1	GSK-3β					1499:1504	phospho-serine 9 GSK-3β	1482:1504	phospho-serine 9 GSK-3β	1482:1504	High glucose and TMG treatment increased phospho-serine 9 GSK-3β, an inactive form, and the degradation of FOXM1 protein was suppressed by treatment of GSK-3β inhibitors in MKN45 cells.
29196265	9	34	theme	High	1441:1444	arg1	glucose					1446:1452	High glucose	1441:1452	High glucose	1441:1452	High glucose and TMG treatment increased phospho-serine 9 GSK-3β, an inactive form, and the degradation of FOXM1 protein was suppressed by treatment of GSK-3β inhibitors in MKN45 cells.
29196265	2	35	theme	cancer	448:453	arg1	types					439:443	various types	431:443	various types of cancer	431:453	Elevated O-GlcNAcylation is a general feature of cancer and contributes to cancer progression, and recent studies indicate the contribution to increasing incidence of various types of cancer in diabetic patients.
29196265	5	36	theme	gastric	778:784	arg1	cancer					786:791	gastric cancer	778:791	gastric cancer	778:791	Given that FOXM1 expression was reported to be elevated in gastric cancer, we examined the effect of high glucose or an inhibitor of O-GlcNAc hydrolase, Thiamet G (TMG), on FOXM1 protein expression in a human gastric cancer cell line, MKN45 cells, and confirmed that FOXM1 protein level and the cell proliferation were upregulated.
29196265	4	37	theme	Forkhead	560:567	arg1	M1					573:574	Forkhead box M1	560:574	Forkhead box M1 (FOXM1)	560:582	Forkhead box M1 (FOXM1), a master mitotic transcription factor, has been implicated in all major hallmarks of cancer, and is wildly expressed in solid tumors.
29196265	4	37	theme	Forkhead	560:567	arg1	factor					616:621	a master mitotic transcription factor	585:621	a master mitotic transcription factor	585:621	Forkhead box M1 (FOXM1), a master mitotic transcription factor, has been implicated in all major hallmarks of cancer, and is wildly expressed in solid tumors.
29196265	4	37	theme	Forkhead	560:567	arg1	FOXM1					577:581	FOXM1	577:581	FOXM1	577:581	Forkhead box M1 (FOXM1), a master mitotic transcription factor, has been implicated in all major hallmarks of cancer, and is wildly expressed in solid tumors.
29196265	3	38	from	role	490:493	arg1	progression					523:533	tumor progression	517:533	tumor progression	517:533	However, the role of O-GlcNAcylation in tumor progression is not fully elucidated.
29196265	0	39	theme	reduced	49:55	arg1	degradation					57:67	its reduced degradation	45:67	its reduced degradation	45:67	Elevated O-GlcNAcylation stabilizes FOXM1 by its reduced degradation through GSK-3β inactivation in a human gastric carcinoma cell line, MKN45 cells.
29196265	6	40	theme	molecular	1070:1078	arg1	mechanisms					1080:1089	the molecular mechanisms	1066:1089	the molecular mechanisms by which FOXM1 protein expression is regulated by O-GlcNAcylation	1066:1155	To investigate the molecular mechanisms by which FOXM1 protein expression is regulated by O-GlcNAcylation, the effect of high glucose and TMG on FOXM1 ubiquitination was examined in MKN45 cells.
29196265	2	41	theme	recent	363:368	arg1	studies					370:376	recent studies	363:376	recent studies	363:376	Elevated O-GlcNAcylation is a general feature of cancer and contributes to cancer progression, and recent studies indicate the contribution to increasing incidence of various types of cancer in diabetic patients.
29196265	5	42	from	expression	906:915	arg1	line					948:951	a human gastric cancer cell line	920:951	a human gastric cancer cell line	920:951	Given that FOXM1 expression was reported to be elevated in gastric cancer, we examined the effect of high glucose or an inhibitor of O-GlcNAc hydrolase, Thiamet G (TMG), on FOXM1 protein expression in a human gastric cancer cell line, MKN45 cells, and confirmed that FOXM1 protein level and the cell proliferation were upregulated.
29196265	5	42	from	expression	906:915	arg1	MKN45 cells					954:964	MKN45 cells	954:964	MKN45 cells	954:964	Given that FOXM1 expression was reported to be elevated in gastric cancer, we examined the effect of high glucose or an inhibitor of O-GlcNAc hydrolase, Thiamet G (TMG), on FOXM1 protein expression in a human gastric cancer cell line, MKN45 cells, and confirmed that FOXM1 protein level and the cell proliferation were upregulated.
29196265	5	43	theme	cell	943:946	arg1	line					948:951	a human gastric cancer cell line	920:951	a human gastric cancer cell line	920:951	Given that FOXM1 expression was reported to be elevated in gastric cancer, we examined the effect of high glucose or an inhibitor of O-GlcNAc hydrolase, Thiamet G (TMG), on FOXM1 protein expression in a human gastric cancer cell line, MKN45 cells, and confirmed that FOXM1 protein level and the cell proliferation were upregulated.
29196265	5	43	theme	cell	943:946	arg1	MKN45 cells					954:964	MKN45 cells	954:964	MKN45 cells	954:964	Given that FOXM1 expression was reported to be elevated in gastric cancer, we examined the effect of high glucose or an inhibitor of O-GlcNAc hydrolase, Thiamet G (TMG), on FOXM1 protein expression in a human gastric cancer cell line, MKN45 cells, and confirmed that FOXM1 protein level and the cell proliferation were upregulated.
29196265	2	44	theme	increasing	407:416	arg1	incidence					418:426	increasing incidence	407:426	increasing incidence of various types of cancer	407:453	Elevated O-GlcNAcylation is a general feature of cancer and contributes to cancer progression, and recent studies indicate the contribution to increasing incidence of various types of cancer in diabetic patients.
29196265	1	45	theme	post-translational	179:196	arg1	modification					198:209	a dynamic post-translational modification	169:209	a dynamic post-translational modification of cytonuclear proteins for intracellular signaling	169:261	O-GlcNAcylation is a dynamic post-translational modification of cytonuclear proteins for intracellular signaling.
29196265	1	45	theme	post-translational	179:196	arg1	O-GlcNAcylation					150:164	O-GlcNAcylation	150:164	O-GlcNAcylation	150:164	O-GlcNAcylation is a dynamic post-translational modification of cytonuclear proteins for intracellular signaling.
29196265	9	46	theme	protein	1554:1560	arg1	degradation					1533:1543	the degradation	1529:1543	the degradation of FOXM1 protein	1529:1560	High glucose and TMG treatment increased phospho-serine 9 GSK-3β, an inactive form, and the degradation of FOXM1 protein was suppressed by treatment of GSK-3β inhibitors in MKN45 cells.
29196265	4	47	theme	master	587:592	arg1	M1					573:574	Forkhead box M1	560:574	Forkhead box M1 (FOXM1)	560:582	Forkhead box M1 (FOXM1), a master mitotic transcription factor, has been implicated in all major hallmarks of cancer, and is wildly expressed in solid tumors.
29196265	4	47	theme	master	587:592	arg1	factor					616:621	a master mitotic transcription factor	585:621	a master mitotic transcription factor	585:621	Forkhead box M1 (FOXM1), a master mitotic transcription factor, has been implicated in all major hallmarks of cancer, and is wildly expressed in solid tumors.
29196265	10	48	theme	gastric	1827:1833	arg1	cancer					1835:1840	gastric cancer	1827:1840	gastric cancer	1827:1840	Taken together, we suggest that high glucose and elevated O-GlcNAcylation stabilize FOXM1 protein by its reduced degradation via GSK-3β inactivation in MKN45 cells, suggesting that the higher risk of gastric cancer in diabetic patients could be partially due to O-GlcNAcylation-mediated FOXM1 stabilization.
29196265	10	49	theme	elevated	1676:1683	arg1	O-GlcNAcylation					1685:1699	elevated O-GlcNAcylation	1676:1699	elevated O-GlcNAcylation	1676:1699	Taken together, we suggest that high glucose and elevated O-GlcNAcylation stabilize FOXM1 protein by its reduced degradation via GSK-3β inactivation in MKN45 cells, suggesting that the higher risk of gastric cancer in diabetic patients could be partially due to O-GlcNAcylation-mediated FOXM1 stabilization.
29196265	4	50	theme	transcription	602:614	arg1	M1					573:574	Forkhead box M1	560:574	Forkhead box M1 (FOXM1)	560:582	Forkhead box M1 (FOXM1), a master mitotic transcription factor, has been implicated in all major hallmarks of cancer, and is wildly expressed in solid tumors.
29196265	4	50	theme	transcription	602:614	arg1	factor					616:621	a master mitotic transcription factor	585:621	a master mitotic transcription factor	585:621	Forkhead box M1 (FOXM1), a master mitotic transcription factor, has been implicated in all major hallmarks of cancer, and is wildly expressed in solid tumors.
29196265	5	51	theme	inhibitor	839:847	arg1	effect					810:815	the effect	806:815	the effect of high glucose or an inhibitor of O-GlcNAc hydrolase, Thiamet G (TMG), on FOXM1 protein expression in a human gastric cancer cell line, MKN45 cells,	806:965	Given that FOXM1 expression was reported to be elevated in gastric cancer, we examined the effect of high glucose or an inhibitor of O-GlcNAc hydrolase, Thiamet G (TMG), on FOXM1 protein expression in a human gastric cancer cell line, MKN45 cells, and confirmed that FOXM1 protein level and the cell proliferation were upregulated.
29196265	2	52	theme	cancer	313:318	arg1	O-GlcNAcylation					273:287	Elevated O-GlcNAcylation	264:287	Elevated O-GlcNAcylation	264:287	Elevated O-GlcNAcylation is a general feature of cancer and contributes to cancer progression, and recent studies indicate the contribution to increasing incidence of various types of cancer in diabetic patients.
29196265	2	52	theme	cancer	313:318	arg1	feature					302:308	a general feature	292:308	a general feature of cancer	292:318	Elevated O-GlcNAcylation is a general feature of cancer and contributes to cancer progression, and recent studies indicate the contribution to increasing incidence of various types of cancer in diabetic patients.
29196265	1	53	theme	dynamic	171:177	arg1	modification					198:209	a dynamic post-translational modification	169:209	a dynamic post-translational modification of cytonuclear proteins for intracellular signaling	169:261	O-GlcNAcylation is a dynamic post-translational modification of cytonuclear proteins for intracellular signaling.
29196265	1	53	theme	dynamic	171:177	arg1	O-GlcNAcylation					150:164	O-GlcNAcylation	150:164	O-GlcNAcylation	150:164	O-GlcNAcylation is a dynamic post-translational modification of cytonuclear proteins for intracellular signaling.
29196265	10	54	from	risk	1819:1822	arg1	patients					1854:1861	diabetic patients	1845:1861	diabetic patients	1845:1861	Taken together, we suggest that high glucose and elevated O-GlcNAcylation stabilize FOXM1 protein by its reduced degradation via GSK-3β inactivation in MKN45 cells, suggesting that the higher risk of gastric cancer in diabetic patients could be partially due to O-GlcNAcylation-mediated FOXM1 stabilization.
29196265	9	55	theme	GSK-3β	1593:1598	arg1	inhibitors					1600:1609	GSK-3β inhibitors	1593:1609	GSK-3β inhibitors in MKN45 cells	1593:1624	High glucose and TMG treatment increased phospho-serine 9 GSK-3β, an inactive form, and the degradation of FOXM1 protein was suppressed by treatment of GSK-3β inhibitors in MKN45 cells.
29196265	2	56	from	contribution	391:402	arg1	patients					467:474	diabetic patients	458:474	diabetic patients	458:474	Elevated O-GlcNAcylation is a general feature of cancer and contributes to cancer progression, and recent studies indicate the contribution to increasing incidence of various types of cancer in diabetic patients.
29196265	9	57	from	inhibitors	1600:1609	arg1	MKN45 cells					1614:1624	MKN45 cells	1614:1624	MKN45 cells	1614:1624	High glucose and TMG treatment increased phospho-serine 9 GSK-3β, an inactive form, and the degradation of FOXM1 protein was suppressed by treatment of GSK-3β inhibitors in MKN45 cells.
29196265	7	58	theme	TMG	1352:1354	arg1	treatment					1356:1364	TMG treatment	1352:1364	TMG treatment	1352:1364	As a result, the ubiquitination and degradation of FOXM1 protein were both suppressed by high glucose and TMG treatment.
29196265	10	59	theme	O-GlcNAcylation-mediated	1889:1912	arg1	stabilization					1920:1932	O-GlcNAcylation-mediated FOXM1 stabilization	1889:1932	O-GlcNAcylation-mediated FOXM1 stabilization	1889:1932	Taken together, we suggest that high glucose and elevated O-GlcNAcylation stabilize FOXM1 protein by its reduced degradation via GSK-3β inactivation in MKN45 cells, suggesting that the higher risk of gastric cancer in diabetic patients could be partially due to O-GlcNAcylation-mediated FOXM1 stabilization.
29196265	2	60	theme	cancer	339:344	arg1	progression					346:356	cancer progression	339:356	cancer progression	339:356	Elevated O-GlcNAcylation is a general feature of cancer and contributes to cancer progression, and recent studies indicate the contribution to increasing incidence of various types of cancer in diabetic patients.
29196265	1	61	theme	cytonuclear	214:224	arg1	proteins					226:233	cytonuclear proteins	214:233	cytonuclear proteins	214:233	O-GlcNAcylation is a dynamic post-translational modification of cytonuclear proteins for intracellular signaling.
29196265	6	62	theme	FOXM1	1100:1104	arg1	expression					1114:1123	FOXM1 protein expression	1100:1123	FOXM1 protein expression	1100:1123	To investigate the molecular mechanisms by which FOXM1 protein expression is regulated by O-GlcNAcylation, the effect of high glucose and TMG on FOXM1 ubiquitination was examined in MKN45 cells.
29196265	5	63	theme	glucose	825:831	arg1	effect					810:815	the effect	806:815	the effect of high glucose or an inhibitor of O-GlcNAc hydrolase, Thiamet G (TMG), on FOXM1 protein expression in a human gastric cancer cell line, MKN45 cells,	806:965	Given that FOXM1 expression was reported to be elevated in gastric cancer, we examined the effect of high glucose or an inhibitor of O-GlcNAc hydrolase, Thiamet G (TMG), on FOXM1 protein expression in a human gastric cancer cell line, MKN45 cells, and confirmed that FOXM1 protein level and the cell proliferation were upregulated.
29196265	6	64	theme	glucose	1177:1183	arg1	effect					1162:1167	the effect	1158:1167	the effect of high glucose and TMG on FOXM1 ubiquitination	1158:1215	To investigate the molecular mechanisms by which FOXM1 protein expression is regulated by O-GlcNAcylation, the effect of high glucose and TMG on FOXM1 ubiquitination was examined in MKN45 cells.
29196265	4	65	theme	major	651:655	arg1	hallmarks					657:665	all major hallmarks	647:665	all major hallmarks of cancer	647:675	Forkhead box M1 (FOXM1), a master mitotic transcription factor, has been implicated in all major hallmarks of cancer, and is wildly expressed in solid tumors.
29196265	4	66	theme	solid	705:709	arg1	tumors					711:716	solid tumors	705:716	solid tumors	705:716	Forkhead box M1 (FOXM1), a master mitotic transcription factor, has been implicated in all major hallmarks of cancer, and is wildly expressed in solid tumors.
29196265	5	67	theme	FOXM1	986:990	arg1	level					1000:1004	FOXM1 protein level	986:1004	FOXM1 protein level	986:1004	Given that FOXM1 expression was reported to be elevated in gastric cancer, we examined the effect of high glucose or an inhibitor of O-GlcNAc hydrolase, Thiamet G (TMG), on FOXM1 protein expression in a human gastric cancer cell line, MKN45 cells, and confirmed that FOXM1 protein level and the cell proliferation were upregulated.
29196265	7	68	theme	protein	1303:1309	arg1	degradation					1282:1292	degradation	1282:1292	degradation	1282:1292	As a result, the ubiquitination and degradation of FOXM1 protein were both suppressed by high glucose and TMG treatment.
29196265	7	68	theme	protein	1303:1309	arg1	result					1251:1256	a result	1249:1256	a result	1249:1256	As a result, the ubiquitination and degradation of FOXM1 protein were both suppressed by high glucose and TMG treatment.
29196265	7	68	theme	protein	1303:1309	arg1	ubiquitination					1263:1276	ubiquitination	1263:1276	ubiquitination	1263:1276	As a result, the ubiquitination and degradation of FOXM1 protein were both suppressed by high glucose and TMG treatment.
29196265	0	69	theme	GSK-3β	77:82	arg1	inactivation					84:95	GSK-3β inactivation	77:95	GSK-3β inactivation in a human gastric carcinoma cell line, MKN45 cells	77:147	Elevated O-GlcNAcylation stabilizes FOXM1 by its reduced degradation through GSK-3β inactivation in a human gastric carcinoma cell line, MKN45 cells.
29196265	10	70	theme	GSK-3β	1756:1761	arg1	inactivation					1763:1774	GSK-3β inactivation	1756:1774	GSK-3β inactivation in MKN45 cells	1756:1789	Taken together, we suggest that high glucose and elevated O-GlcNAcylation stabilize FOXM1 protein by its reduced degradation via GSK-3β inactivation in MKN45 cells, suggesting that the higher risk of gastric cancer in diabetic patients could be partially due to O-GlcNAcylation-mediated FOXM1 stabilization.
29196265	5	71	theme	hydrolase	861:869	arg1	glucose					825:831	high glucose	820:831	high glucose	820:831	Given that FOXM1 expression was reported to be elevated in gastric cancer, we examined the effect of high glucose or an inhibitor of O-GlcNAc hydrolase, Thiamet G (TMG), on FOXM1 protein expression in a human gastric cancer cell line, MKN45 cells, and confirmed that FOXM1 protein level and the cell proliferation were upregulated.
29196265	5	71	theme	hydrolase	861:869	arg1	inhibitor					839:847	an inhibitor	836:847	an inhibitor of O-GlcNAc hydrolase	836:869	Given that FOXM1 expression was reported to be elevated in gastric cancer, we examined the effect of high glucose or an inhibitor of O-GlcNAc hydrolase, Thiamet G (TMG), on FOXM1 protein expression in a human gastric cancer cell line, MKN45 cells, and confirmed that FOXM1 protein level and the cell proliferation were upregulated.
29196265	5	71	theme	hydrolase	861:869	arg1	G					880:880	Thiamet G	872:880	Thiamet G (TMG)	872:886	Given that FOXM1 expression was reported to be elevated in gastric cancer, we examined the effect of high glucose or an inhibitor of O-GlcNAc hydrolase, Thiamet G (TMG), on FOXM1 protein expression in a human gastric cancer cell line, MKN45 cells, and confirmed that FOXM1 protein level and the cell proliferation were upregulated.
29196265	5	72	theme	Thiamet	872:878	arg1	TMG					883:885	TMG	883:885	TMG	883:885	Given that FOXM1 expression was reported to be elevated in gastric cancer, we examined the effect of high glucose or an inhibitor of O-GlcNAc hydrolase, Thiamet G (TMG), on FOXM1 protein expression in a human gastric cancer cell line, MKN45 cells, and confirmed that FOXM1 protein level and the cell proliferation were upregulated.
29196265	5	72	theme	Thiamet	872:878	arg1	G					880:880	Thiamet G	872:880	Thiamet G (TMG)	872:886	Given that FOXM1 expression was reported to be elevated in gastric cancer, we examined the effect of high glucose or an inhibitor of O-GlcNAc hydrolase, Thiamet G (TMG), on FOXM1 protein expression in a human gastric cancer cell line, MKN45 cells, and confirmed that FOXM1 protein level and the cell proliferation were upregulated.
29196265	5	72	theme	Thiamet	872:878	arg1	inhibitor					839:847	an inhibitor	836:847	an inhibitor of O-GlcNAc hydrolase	836:869	Given that FOXM1 expression was reported to be elevated in gastric cancer, we examined the effect of high glucose or an inhibitor of O-GlcNAc hydrolase, Thiamet G (TMG), on FOXM1 protein expression in a human gastric cancer cell line, MKN45 cells, and confirmed that FOXM1 protein level and the cell proliferation were upregulated.
29196265	6	73	from	effect	1162:1167	arg1	ubiquitination					1202:1215	FOXM1 ubiquitination	1196:1215	FOXM1 ubiquitination	1196:1215	To investigate the molecular mechanisms by which FOXM1 protein expression is regulated by O-GlcNAcylation, the effect of high glucose and TMG on FOXM1 ubiquitination was examined in MKN45 cells.
29196265	0	74	theme	human	102:106	arg1	MKN45 cells					137:147	MKN45 cells	137:147	MKN45 cells	137:147	Elevated O-GlcNAcylation stabilizes FOXM1 by its reduced degradation through GSK-3β inactivation in a human gastric carcinoma cell line, MKN45 cells.
29196265	0	74	theme	human	102:106	arg1	line					131:134	a human gastric carcinoma cell line	100:134	a human gastric carcinoma cell line	100:134	Elevated O-GlcNAcylation stabilizes FOXM1 by its reduced degradation through GSK-3β inactivation in a human gastric carcinoma cell line, MKN45 cells.
29196265	9	75	from	MKN45 cells	1614:1624	arg1	treatment					1580:1588	treatment	1580:1588	treatment of GSK-3β inhibitors in MKN45 cells	1580:1624	High glucose and TMG treatment increased phospho-serine 9 GSK-3β, an inactive form, and the degradation of FOXM1 protein was suppressed by treatment of GSK-3β inhibitors in MKN45 cells.
29196265	0	76	theme	carcinoma	116:124	arg1	MKN45 cells					137:147	MKN45 cells	137:147	MKN45 cells	137:147	Elevated O-GlcNAcylation stabilizes FOXM1 by its reduced degradation through GSK-3β inactivation in a human gastric carcinoma cell line, MKN45 cells.
29196265	0	76	theme	carcinoma	116:124	arg1	line					131:134	a human gastric carcinoma cell line	100:134	a human gastric carcinoma cell line	100:134	Elevated O-GlcNAcylation stabilizes FOXM1 by its reduced degradation through GSK-3β inactivation in a human gastric carcinoma cell line, MKN45 cells.
29196265	5	77	from	effect	810:815	arg1	expression					906:915	FOXM1 protein expression	892:915	FOXM1 protein expression in a human gastric cancer cell line, MKN45 cells,	892:965	Given that FOXM1 expression was reported to be elevated in gastric cancer, we examined the effect of high glucose or an inhibitor of O-GlcNAc hydrolase, Thiamet G (TMG), on FOXM1 protein expression in a human gastric cancer cell line, MKN45 cells, and confirmed that FOXM1 protein level and the cell proliferation were upregulated.
29196265	1	78	theme	proteins	226:233	arg1	modification					198:209	a dynamic post-translational modification	169:209	a dynamic post-translational modification of cytonuclear proteins for intracellular signaling	169:261	O-GlcNAcylation is a dynamic post-translational modification of cytonuclear proteins for intracellular signaling.
29196265	1	78	theme	proteins	226:233	arg1	O-GlcNAcylation					150:164	O-GlcNAcylation	150:164	O-GlcNAcylation	150:164	O-GlcNAcylation is a dynamic post-translational modification of cytonuclear proteins for intracellular signaling.
29196265	5	79	theme	human	922:926	arg1	line					948:951	a human gastric cancer cell line	920:951	a human gastric cancer cell line	920:951	Given that FOXM1 expression was reported to be elevated in gastric cancer, we examined the effect of high glucose or an inhibitor of O-GlcNAc hydrolase, Thiamet G (TMG), on FOXM1 protein expression in a human gastric cancer cell line, MKN45 cells, and confirmed that FOXM1 protein level and the cell proliferation were upregulated.
29196265	5	79	theme	human	922:926	arg1	MKN45 cells					954:964	MKN45 cells	954:964	MKN45 cells	954:964	Given that FOXM1 expression was reported to be elevated in gastric cancer, we examined the effect of high glucose or an inhibitor of O-GlcNAc hydrolase, Thiamet G (TMG), on FOXM1 protein expression in a human gastric cancer cell line, MKN45 cells, and confirmed that FOXM1 protein level and the cell proliferation were upregulated.
29196265	2	80	theme	various	431:437	arg1	types					439:443	various types	431:443	various types of cancer	431:453	Elevated O-GlcNAcylation is a general feature of cancer and contributes to cancer progression, and recent studies indicate the contribution to increasing incidence of various types of cancer in diabetic patients.
29196265	5	81	theme	protein	898:904	arg1	expression					906:915	FOXM1 protein expression	892:915	FOXM1 protein expression in a human gastric cancer cell line, MKN45 cells,	892:965	Given that FOXM1 expression was reported to be elevated in gastric cancer, we examined the effect of high glucose or an inhibitor of O-GlcNAc hydrolase, Thiamet G (TMG), on FOXM1 protein expression in a human gastric cancer cell line, MKN45 cells, and confirmed that FOXM1 protein level and the cell proliferation were upregulated.
29196265	9	82	theme	phospho-serine	1482:1495	arg1	form					1519:1522	an inactive form	1507:1522	an inactive form	1507:1522	High glucose and TMG treatment increased phospho-serine 9 GSK-3β, an inactive form, and the degradation of FOXM1 protein was suppressed by treatment of GSK-3β inhibitors in MKN45 cells.
29196265	9	82	theme	phospho-serine	1482:1495	arg1	GSK-3β					1499:1504	phospho-serine 9 GSK-3β	1482:1504	phospho-serine 9 GSK-3β	1482:1504	High glucose and TMG treatment increased phospho-serine 9 GSK-3β, an inactive form, and the degradation of FOXM1 protein was suppressed by treatment of GSK-3β inhibitors in MKN45 cells.
29196265	3	83	theme	O-GlcNAcylation	498:512	arg1	role					490:493	the role	486:493	the role of O-GlcNAcylation in tumor progression	486:533	However, the role of O-GlcNAcylation in tumor progression is not fully elucidated.
29196265	10	84	from	inactivation	1763:1774	arg1	MKN45 cells					1779:1789	MKN45 cells	1779:1789	MKN45 cells	1779:1789	Taken together, we suggest that high glucose and elevated O-GlcNAcylation stabilize FOXM1 protein by its reduced degradation via GSK-3β inactivation in MKN45 cells, suggesting that the higher risk of gastric cancer in diabetic patients could be partially due to O-GlcNAcylation-mediated FOXM1 stabilization.
29196265	4	85	theme	box	569:571	arg1	M1					573:574	Forkhead box M1	560:574	Forkhead box M1 (FOXM1)	560:582	Forkhead box M1 (FOXM1), a master mitotic transcription factor, has been implicated in all major hallmarks of cancer, and is wildly expressed in solid tumors.
29196265	4	85	theme	box	569:571	arg1	factor					616:621	a master mitotic transcription factor	585:621	a master mitotic transcription factor	585:621	Forkhead box M1 (FOXM1), a master mitotic transcription factor, has been implicated in all major hallmarks of cancer, and is wildly expressed in solid tumors.
29196265	4	85	theme	box	569:571	arg1	FOXM1					577:581	FOXM1	577:581	FOXM1	577:581	Forkhead box M1 (FOXM1), a master mitotic transcription factor, has been implicated in all major hallmarks of cancer, and is wildly expressed in solid tumors.
29196265	7	86	dep	ubiquitination	1263:1276	arg1	the					1259:1261	the	1259:1261	the	1259:1261	As a result, the ubiquitination and degradation of FOXM1 protein were both suppressed by high glucose and TMG treatment.
29196265	5	87	theme	cancer	936:941	arg1	line					948:951	a human gastric cancer cell line	920:951	a human gastric cancer cell line	920:951	Given that FOXM1 expression was reported to be elevated in gastric cancer, we examined the effect of high glucose or an inhibitor of O-GlcNAc hydrolase, Thiamet G (TMG), on FOXM1 protein expression in a human gastric cancer cell line, MKN45 cells, and confirmed that FOXM1 protein level and the cell proliferation were upregulated.
29196265	5	87	theme	cancer	936:941	arg1	MKN45 cells					954:964	MKN45 cells	954:964	MKN45 cells	954:964	Given that FOXM1 expression was reported to be elevated in gastric cancer, we examined the effect of high glucose or an inhibitor of O-GlcNAc hydrolase, Thiamet G (TMG), on FOXM1 protein expression in a human gastric cancer cell line, MKN45 cells, and confirmed that FOXM1 protein level and the cell proliferation were upregulated.
29196265	10	88	theme	reduced	1732:1738	arg1	degradation					1740:1750	its reduced degradation	1728:1750	its reduced degradation via GSK-3β inactivation in MKN45 cells	1728:1789	Taken together, we suggest that high glucose and elevated O-GlcNAcylation stabilize FOXM1 protein by its reduced degradation via GSK-3β inactivation in MKN45 cells, suggesting that the higher risk of gastric cancer in diabetic patients could be partially due to O-GlcNAcylation-mediated FOXM1 stabilization.
29196265	10	89	theme	higher	1812:1817	arg1	due					1882:1884	due	1882:1884	due	1882:1884	Taken together, we suggest that high glucose and elevated O-GlcNAcylation stabilize FOXM1 protein by its reduced degradation via GSK-3β inactivation in MKN45 cells, suggesting that the higher risk of gastric cancer in diabetic patients could be partially due to O-GlcNAcylation-mediated FOXM1 stabilization.
29196265	10	89	theme	higher	1812:1817	arg1	risk					1819:1822	the higher risk	1808:1822	the higher risk of gastric cancer in diabetic patients	1808:1861	Taken together, we suggest that high glucose and elevated O-GlcNAcylation stabilize FOXM1 protein by its reduced degradation via GSK-3β inactivation in MKN45 cells, suggesting that the higher risk of gastric cancer in diabetic patients could be partially due to O-GlcNAcylation-mediated FOXM1 stabilization.
29196265	3	90	theme	tumor	517:521	arg1	progression					523:533	tumor progression	517:533	tumor progression	517:533	However, the role of O-GlcNAcylation in tumor progression is not fully elucidated.
29196265	9	91	theme	FOXM1	1548:1552	arg1	protein					1554:1560	FOXM1 protein	1548:1560	FOXM1 protein	1548:1560	High glucose and TMG treatment increased phospho-serine 9 GSK-3β, an inactive form, and the degradation of FOXM1 protein was suppressed by treatment of GSK-3β inhibitors in MKN45 cells.
29196265	10	92	theme	diabetic	1845:1852	arg1	patients					1854:1861	diabetic patients	1845:1861	diabetic patients	1845:1861	Taken together, we suggest that high glucose and elevated O-GlcNAcylation stabilize FOXM1 protein by its reduced degradation via GSK-3β inactivation in MKN45 cells, suggesting that the higher risk of gastric cancer in diabetic patients could be partially due to O-GlcNAcylation-mediated FOXM1 stabilization.
35164752	6	0	theme	CDK9	856:859	arg1	effects					871:877	short-term CDK9 inhibitor effects	845:877	short-term CDK9 inhibitor effects on O-GlcNAcylated proteins	845:904	METHODS We used comprehensive mass spectrometry profiling of short-term CDK9 inhibitor effects on O-GlcNAcylated proteins in an isogenic cell line system that models transition from PC to CRPC.
35164752	6	1	dep	METHODS	784:790	arg1	used					795:798	used	795:798	used comprehensive mass spectrometry profiling of short-term CDK9 inhibitor effects on O-GlcNAcylated proteins in an isogenic cell line system that models transition from PC to CRPC	795:975	METHODS We used comprehensive mass spectrometry profiling of short-term CDK9 inhibitor effects on O-GlcNAcylated proteins in an isogenic cell line system that models transition from PC to CRPC.
35164752	4	2	theme	combined	591:598	arg1	inhibition					600:609	combined inhibition	591:609	combined inhibition of OGT	591:616	We have shown that combined inhibition of OGT and the transcription elongation kinase CDK9 induce CRPC-selective anti-proliferative effects.
35164752	15	3	theme	OGT	1822:1824	arg1	activity					1826:1833	OGT activity	1822:1833	OGT activity	1822:1833	Mechanistically, OGT activity is required for MRE11 chromatin-loading in cells treated with CDK9 inhibitor.
35164752	10	4	dep	inhibition	1369:1378	arg1	response					1352:1359	response	1352:1359	response	1352:1359	More specifically, the activity of the DNA damage repair protein MRE11 is regulated in response to CDK9 inhibition in an OGT-dependent manner.
35164752	6	5	theme	spectrometry	819:830	arg1	profiling					832:840	comprehensive mass spectrometry profiling	800:840	comprehensive mass spectrometry profiling of short-term CDK9 inhibitor effects on O-GlcNAcylated proteins	800:904	METHODS We used comprehensive mass spectrometry profiling of short-term CDK9 inhibitor effects on O-GlcNAcylated proteins in an isogenic cell line system that models transition from PC to CRPC.
35164752	3	6	theme	prostate	548:555	arg1	cancer					557:562	castration-resistant prostate cancer	527:562	castration-resistant prostate cancer (CRPC)	527:569	However, a significant number of prostate cancer patients develop resistance against anti-androgens, and this incurable disease is termed castration-resistant prostate cancer (CRPC).
35164752	3	6	theme	prostate	548:555	arg1	CRPC					565:568	CRPC	565:568	CRPC	565:568	However, a significant number of prostate cancer patients develop resistance against anti-androgens, and this incurable disease is termed castration-resistant prostate cancer (CRPC).
35164752	6	7	theme	cell	921:924	arg1	system					931:936	an isogenic cell line system	909:936	an isogenic cell line system that models transition from PC to CRPC	909:975	METHODS We used comprehensive mass spectrometry profiling of short-term CDK9 inhibitor effects on O-GlcNAcylated proteins in an isogenic cell line system that models transition from PC to CRPC.
35164752	4	8	theme	anti-proliferative	685:702	arg1	effects					704:710	CRPC-selective anti-proliferative effects	670:710	CRPC-selective anti-proliferative effects	670:710	We have shown that combined inhibition of OGT and the transcription elongation kinase CDK9 induce CRPC-selective anti-proliferative effects.
35164752	6	9	from	proteins	897:904	arg1	profiling					832:840	comprehensive mass spectrometry profiling	800:840	comprehensive mass spectrometry profiling of short-term CDK9 inhibitor effects on O-GlcNAcylated proteins	800:904	METHODS We used comprehensive mass spectrometry profiling of short-term CDK9 inhibitor effects on O-GlcNAcylated proteins in an isogenic cell line system that models transition from PC to CRPC.
35164752	6	10	theme	comprehensive	800:812	arg1	profiling					832:840	comprehensive mass spectrometry profiling	800:840	comprehensive mass spectrometry profiling of short-term CDK9 inhibitor effects on O-GlcNAcylated proteins	800:904	METHODS We used comprehensive mass spectrometry profiling of short-term CDK9 inhibitor effects on O-GlcNAcylated proteins in an isogenic cell line system that models transition from PC to CRPC.
35164752	13	11	theme	CDK9	1586:1589	arg1	inhibition					1572:1581	Combined inhibition	1563:1581	Combined inhibition of CDK9 and OGT or MRE11	1563:1606	Combined inhibition of CDK9 and OGT or MRE11 further decreases RNA polymerase II activity, induces DNA damage signaling, and blocks the survival of prostate cancer cells.
35164752	1	12	theme	genomic	196:202	arg1	integrity					204:212	the genomic integrity	192:212	the genomic integrity	192:212	BACKGROUND Transcription, metabolism and DNA damage response are tightly regulated to preserve the genomic integrity, and O-GlcNAc transferase (OGT) is positioned to connect the three.
35164752	4	13	theme	transcription	626:638	arg1	CDK9					658:661	the transcription elongation kinase CDK9	622:661	the transcription elongation kinase CDK9	622:661	We have shown that combined inhibition of OGT and the transcription elongation kinase CDK9 induce CRPC-selective anti-proliferative effects.
35164752	9	14	theme	cancer	1251:1256	arg1	cells					1258:1262	prostate cancer cells	1242:1262	prostate cancer cells	1242:1262	RESULTS Inhibition of CDK9 results in an OGT-dependent remodeling of the proteome in prostate cancer cells.
35164752	13	15	theme	OGT	1595:1597	arg1	inhibition					1572:1581	Combined inhibition	1563:1581	Combined inhibition of CDK9 and OGT or MRE11	1563:1606	Combined inhibition of CDK9 and OGT or MRE11 further decreases RNA polymerase II activity, induces DNA damage signaling, and blocks the survival of prostate cancer cells.
35164752	4	16	theme	kinase	651:656	arg1	CDK9					658:661	the transcription elongation kinase CDK9	622:661	the transcription elongation kinase CDK9	622:661	We have shown that combined inhibition of OGT and the transcription elongation kinase CDK9 induce CRPC-selective anti-proliferative effects.
35164752	13	17	theme	cells	1727:1731	arg1	survival					1699:1706	the survival	1695:1706	the survival of prostate cancer cells	1695:1731	Combined inhibition of CDK9 and OGT or MRE11 further decreases RNA polymerase II activity, induces DNA damage signaling, and blocks the survival of prostate cancer cells.
35164752	5	18	theme	functional	734:743	arg1	basis					745:749	the functional basis	730:749	the functional basis for these combinatorial effects	730:781	Here, we explain the functional basis for these combinatorial effects.
35164752	1	19	theme	O-GlcNAc	219:226	arg1	OGT					241:243	OGT	241:243	OGT	241:243	BACKGROUND Transcription, metabolism and DNA damage response are tightly regulated to preserve the genomic integrity, and O-GlcNAc transferase (OGT) is positioned to connect the three.
35164752	1	19	theme	O-GlcNAc	219:226	arg1	transferase					228:238	O-GlcNAc transferase	219:238	O-GlcNAc transferase (OGT)	219:244	BACKGROUND Transcription, metabolism and DNA damage response are tightly regulated to preserve the genomic integrity, and O-GlcNAc transferase (OGT) is positioned to connect the three.
35164752	7	20	theme	CRPC	1073:1076	arg1	models					1078:1083	multiple CRPC models	1064:1083	multiple CRPC models	1064:1083	In addition, we used both ChIP-seq and RNA-seq profiling, and pulldown experiments in multiple CRPC models.
35164752	9	21	theme	OGT-dependent	1198:1210	arg1	remodeling					1212:1221	an OGT-dependent remodeling	1195:1221	an OGT-dependent remodeling of the proteome in prostate cancer cells	1195:1262	RESULTS Inhibition of CDK9 results in an OGT-dependent remodeling of the proteome in prostate cancer cells.
35164752	1	22	theme	damage	142:147	arg1	response					149:156	DNA damage response	138:156	DNA damage response	138:156	BACKGROUND Transcription, metabolism and DNA damage response are tightly regulated to preserve the genomic integrity, and O-GlcNAc transferase (OGT) is positioned to connect the three.
35164752	9	23	from	remodeling	1212:1221	arg1	cells					1258:1262	prostate cancer cells	1242:1262	prostate cancer cells	1242:1262	RESULTS Inhibition of CDK9 results in an OGT-dependent remodeling of the proteome in prostate cancer cells.
35164752	17	24	theme	damage	2212:2217	arg1	repair					2175:2180	the repair	2171:2180	the repair of CDK9 inhibitor-induced DNA damage	2171:2217	CONCLUSIONS Both OGT and MRE11 are essential for the repair of CDK9 inhibitor-induced DNA damage.
35164752	16	25	theme	activity	2057:2064	arg1	loss					2043:2046	the loss	2039:2046	the loss of MRE11 activity	2039:2064	Finally, we show that MRE11 and O-GlcNAc are enriched at the prostate cancer-specific small nucleotide polymorphic sites, and the loss of MRE11 activity results in a hyper-mutator phenotype in patient tumors.
35164752	0	26	theme	DNA	85:87	arg1	damage					89:94	DNA damage	85:94	DNA damage	85:94	O-GlcNAc transferase couples MRE11 to transcriptionally active chromatin to suppress DNA damage.
35164752	16	27	theme	hyper-mutator	2079:2091	arg1	phenotype					2093:2101	a hyper-mutator phenotype	2077:2101	a hyper-mutator phenotype in patient tumors	2077:2119	Finally, we show that MRE11 and O-GlcNAc are enriched at the prostate cancer-specific small nucleotide polymorphic sites, and the loss of MRE11 activity results in a hyper-mutator phenotype in patient tumors.
35164752	10	28	theme	DNA	1304:1306	arg1	repair					1315:1320	DNA damage repair	1304:1320	the DNA damage repair protein MRE11	1300:1334	More specifically, the activity of the DNA damage repair protein MRE11 is regulated in response to CDK9 inhibition in an OGT-dependent manner.
35164752	3	29	theme	prostate	422:429	arg1	patients					438:445	prostate cancer patients	422:445	prostate cancer patients	422:445	However, a significant number of prostate cancer patients develop resistance against anti-androgens, and this incurable disease is termed castration-resistant prostate cancer (CRPC).
35164752	5	30	theme	combinatorial	761:773	arg1	effects					775:781	these combinatorial effects	755:781	these combinatorial effects	755:781	Here, we explain the functional basis for these combinatorial effects.
35164752	7	31	used	used	994:997	arg2	we					991:992	we	991:992	we	991:992	In addition, we used both ChIP-seq and RNA-seq profiling, and pulldown experiments in multiple CRPC models.
35164752	6	32	from	profiling	832:840	arg1	proteins					897:904	O-GlcNAcylated proteins	882:904	O-GlcNAcylated proteins	882:904	METHODS We used comprehensive mass spectrometry profiling of short-term CDK9 inhibitor effects on O-GlcNAcylated proteins in an isogenic cell line system that models transition from PC to CRPC.
35164752	2	33	theme	disease	368:374	arg1	progression					376:386	disease progression	368:386	disease progression	368:386	Prostate cancer is the most common cancer in men, and androgen-ablation therapy halts disease progression.
35164752	0	34	theme	O-GlcNAc	0:7	arg1	transferase					9:19	O-GlcNAc transferase	0:19	O-GlcNAc transferase	0:19	O-GlcNAc transferase couples MRE11 to transcriptionally active chromatin to suppress DNA damage.
35164752	1	35	theme	BACKGROUND	97:106	arg1	Transcription					108:120	BACKGROUND Transcription	97:120	BACKGROUND Transcription	97:120	BACKGROUND Transcription, metabolism and DNA damage response are tightly regulated to preserve the genomic integrity, and O-GlcNAc transferase (OGT) is positioned to connect the three.
35164752	16	36	theme	polymorphic	2016:2026	arg1	sites					2028:2032	the prostate cancer-specific small nucleotide polymorphic sites	1970:2032	the prostate cancer-specific small nucleotide polymorphic sites	1970:2032	Finally, we show that MRE11 and O-GlcNAc are enriched at the prostate cancer-specific small nucleotide polymorphic sites, and the loss of MRE11 activity results in a hyper-mutator phenotype in patient tumors.
35164752	17	37	theme	CDK9	2185:2188	arg1	damage					2212:2217	CDK9 inhibitor-induced DNA damage	2185:2217	CDK9 inhibitor-induced DNA damage	2185:2217	CONCLUSIONS Both OGT and MRE11 are essential for the repair of CDK9 inhibitor-induced DNA damage.
35164752	10	38	theme	MRE11	1330:1334	arg1	activity					1288:1295	the activity	1284:1295	the activity of the DNA damage repair protein MRE11	1284:1334	More specifically, the activity of the DNA damage repair protein MRE11 is regulated in response to CDK9 inhibition in an OGT-dependent manner.
35164752	14	39	theme	normal	1782:1787	arg1	cells					1798:1802	normal prostate cells	1782:1802	normal prostate cells	1782:1802	These effects are seen in CRPC cells but not in normal prostate cells.
35164752	6	40	theme	isogenic	912:919	arg1	system					931:936	an isogenic cell line system	909:936	an isogenic cell line system that models transition from PC to CRPC	909:975	METHODS We used comprehensive mass spectrometry profiling of short-term CDK9 inhibitor effects on O-GlcNAcylated proteins in an isogenic cell line system that models transition from PC to CRPC.
35164752	16	41	theme	cancer-specific	1983:1997	arg1	sites					2028:2032	the prostate cancer-specific small nucleotide polymorphic sites	1970:2032	the prostate cancer-specific small nucleotide polymorphic sites	1970:2032	Finally, we show that MRE11 and O-GlcNAc are enriched at the prostate cancer-specific small nucleotide polymorphic sites, and the loss of MRE11 activity results in a hyper-mutator phenotype in patient tumors.
35164752	13	42	theme	DNA	1662:1664	arg1	damage					1666:1671	DNA damage	1662:1671	DNA damage signaling	1662:1681	Combined inhibition of CDK9 and OGT or MRE11 further decreases RNA polymerase II activity, induces DNA damage signaling, and blocks the survival of prostate cancer cells.
35164752	10	43	theme	repair	1315:1320	arg1	MRE11					1330:1334	the DNA damage repair protein MRE11	1300:1334	the DNA damage repair protein MRE11	1300:1334	More specifically, the activity of the DNA damage repair protein MRE11 is regulated in response to CDK9 inhibition in an OGT-dependent manner.
35164752	3	44	theme	patients	438:445	arg1	number					412:417	a significant number	398:417	a significant number of prostate cancer patients	398:445	However, a significant number of prostate cancer patients develop resistance against anti-androgens, and this incurable disease is termed castration-resistant prostate cancer (CRPC).
35164752	13	45	theme	RNA	1626:1628	arg1	polymerase					1630:1639	RNA polymerase II	1626:1642	RNA polymerase II activity	1626:1651	Combined inhibition of CDK9 and OGT or MRE11 further decreases RNA polymerase II activity, induces DNA damage signaling, and blocks the survival of prostate cancer cells.
35164752	6	46	theme	line	926:929	arg1	system					931:936	an isogenic cell line system	909:936	an isogenic cell line system that models transition from PC to CRPC	909:975	METHODS We used comprehensive mass spectrometry profiling of short-term CDK9 inhibitor effects on O-GlcNAcylated proteins in an isogenic cell line system that models transition from PC to CRPC.
35164752	0	47	theme	active	56:61	arg1	chromatin					63:71	transcriptionally active chromatin	38:71	transcriptionally active chromatin	38:71	O-GlcNAc transferase couples MRE11 to transcriptionally active chromatin to suppress DNA damage.
35164752	6	48	theme	O-GlcNAcylated	882:895	arg1	proteins					897:904	O-GlcNAcylated proteins	882:904	O-GlcNAcylated proteins	882:904	METHODS We used comprehensive mass spectrometry profiling of short-term CDK9 inhibitor effects on O-GlcNAcylated proteins in an isogenic cell line system that models transition from PC to CRPC.
35164752	8	49	theme	cancer	1133:1138	arg1	samples					1148:1154	prostate cancer patient samples	1124:1154	prostate cancer patient samples	1124:1154	Finally, we validated our findings in prostate cancer patient samples.
35164752	12	50	theme	mRNAs	1507:1511	arg1	expression					1493:1502	the expression	1489:1502	the expression of mRNAs whose genes are bound by both O-GlcNAc and MRE11	1489:1560	CDK9 inhibition does not decrease the expression of mRNAs whose genes are bound by both O-GlcNAc and MRE11.
35164752	9	51	theme	CDK9	1179:1182	arg1	Inhibition					1165:1174	RESULTS Inhibition	1157:1174	RESULTS Inhibition of CDK9	1157:1182	RESULTS Inhibition of CDK9 results in an OGT-dependent remodeling of the proteome in prostate cancer cells.
35164752	4	52	theme	OGT	614:616	arg1	CDK9					658:661	the transcription elongation kinase CDK9	622:661	the transcription elongation kinase CDK9	622:661	We have shown that combined inhibition of OGT and the transcription elongation kinase CDK9 induce CRPC-selective anti-proliferative effects.
35164752	4	52	theme	OGT	614:616	arg1	inhibition					600:609	combined inhibition	591:609	combined inhibition of OGT	591:616	We have shown that combined inhibition of OGT and the transcription elongation kinase CDK9 induce CRPC-selective anti-proliferative effects.
35164752	6	53	from	PC	966:967	arg1	transition					950:959	transition	950:959	transition from PC to CRPC	950:975	METHODS We used comprehensive mass spectrometry profiling of short-term CDK9 inhibitor effects on O-GlcNAcylated proteins in an isogenic cell line system that models transition from PC to CRPC.
35164752	15	54	from	chromatin-loading	1857:1873	arg1	cells					1878:1882	cells	1878:1882	cells treated with CDK9 inhibitor	1878:1910	Mechanistically, OGT activity is required for MRE11 chromatin-loading in cells treated with CDK9 inhibitor.
35164752	10	55	theme	CDK9	1364:1367	arg1	inhibition					1369:1378	CDK9 inhibition	1364:1378	CDK9 inhibition	1364:1378	More specifically, the activity of the DNA damage repair protein MRE11 is regulated in response to CDK9 inhibition in an OGT-dependent manner.
35164752	3	56	theme	incurable	499:507	arg1	disease					509:515	this incurable disease	494:515	this incurable disease	494:515	However, a significant number of prostate cancer patients develop resistance against anti-androgens, and this incurable disease is termed castration-resistant prostate cancer (CRPC).
35164752	2	57	from	cancer	317:322	arg1	men					327:329	men	327:329	men	327:329	Prostate cancer is the most common cancer in men, and androgen-ablation therapy halts disease progression.
35164752	18	58	theme	CDK9	2266:2269	arg1	adjuvant					2314:2321	adjuvant	2314:2321	adjuvant	2314:2321	Our study raises the possibility of targeting CDK9 to elicit DNA damage in CRPC setting as an adjuvant to other treatments.
35164752	18	58	theme	CDK9	2266:2269	arg1	possibility					2241:2251	the possibility	2237:2251	the possibility of targeting CDK9 to elicit DNA damage in CRPC setting	2237:2306	Our study raises the possibility of targeting CDK9 to elicit DNA damage in CRPC setting as an adjuvant to other treatments.
35164752	6	59	theme	mass	814:817	arg1	profiling					832:840	comprehensive mass spectrometry profiling	800:840	comprehensive mass spectrometry profiling of short-term CDK9 inhibitor effects on O-GlcNAcylated proteins	800:904	METHODS We used comprehensive mass spectrometry profiling of short-term CDK9 inhibitor effects on O-GlcNAcylated proteins in an isogenic cell line system that models transition from PC to CRPC.
35164752	6	60	theme	short-term	845:854	arg1	effects					871:877	short-term CDK9 inhibitor effects	845:877	short-term CDK9 inhibitor effects on O-GlcNAcylated proteins	845:904	METHODS We used comprehensive mass spectrometry profiling of short-term CDK9 inhibitor effects on O-GlcNAcylated proteins in an isogenic cell line system that models transition from PC to CRPC.
35164752	2	61	theme	Prostate	282:289	arg1	cancer					317:322	the most common cancer	301:322	the most common cancer in men	301:329	Prostate cancer is the most common cancer in men, and androgen-ablation therapy halts disease progression.
35164752	2	61	theme	Prostate	282:289	arg1	cancer					291:296	Prostate cancer	282:296	Prostate cancer	282:296	Prostate cancer is the most common cancer in men, and androgen-ablation therapy halts disease progression.
35164752	10	62	theme	OGT-dependent	1386:1398	arg1	manner					1400:1405	an OGT-dependent manner	1383:1405	an OGT-dependent manner	1383:1405	More specifically, the activity of the DNA damage repair protein MRE11 is regulated in response to CDK9 inhibition in an OGT-dependent manner.
35164752	3	63	theme	castration-resistant	527:546	arg1	cancer					557:562	castration-resistant prostate cancer	527:562	castration-resistant prostate cancer (CRPC)	527:569	However, a significant number of prostate cancer patients develop resistance against anti-androgens, and this incurable disease is termed castration-resistant prostate cancer (CRPC).
35164752	3	63	theme	castration-resistant	527:546	arg1	CRPC					565:568	CRPC	565:568	CRPC	565:568	However, a significant number of prostate cancer patients develop resistance against anti-androgens, and this incurable disease is termed castration-resistant prostate cancer (CRPC).
35164752	6	64	used	used	795:798	arg2	We					792:793	We	792:793	We	792:793	METHODS We used comprehensive mass spectrometry profiling of short-term CDK9 inhibitor effects on O-GlcNAcylated proteins in an isogenic cell line system that models transition from PC to CRPC.
35164752	12	65	theme	CDK9	1455:1458	arg1	inhibition					1460:1469	CDK9 inhibition	1455:1469	CDK9 inhibition	1455:1469	CDK9 inhibition does not decrease the expression of mRNAs whose genes are bound by both O-GlcNAc and MRE11.
35164752	16	66	theme	patient	2106:2112	arg1	tumors					2114:2119	patient tumors	2106:2119	patient tumors	2106:2119	Finally, we show that MRE11 and O-GlcNAc are enriched at the prostate cancer-specific small nucleotide polymorphic sites, and the loss of MRE11 activity results in a hyper-mutator phenotype in patient tumors.
35164752	15	67	theme	CDK9	1897:1900	arg1	inhibitor					1902:1910	CDK9 inhibitor	1897:1910	CDK9 inhibitor	1897:1910	Mechanistically, OGT activity is required for MRE11 chromatin-loading in cells treated with CDK9 inhibitor.
35164752	9	68	theme	proteome	1230:1237	arg1	remodeling					1212:1221	an OGT-dependent remodeling	1195:1221	an OGT-dependent remodeling of the proteome in prostate cancer cells	1195:1262	RESULTS Inhibition of CDK9 results in an OGT-dependent remodeling of the proteome in prostate cancer cells.
35164752	4	69	theme	CRPC-selective	670:683	arg1	effects					704:710	CRPC-selective anti-proliferative effects	670:710	CRPC-selective anti-proliferative effects	670:710	We have shown that combined inhibition of OGT and the transcription elongation kinase CDK9 induce CRPC-selective anti-proliferative effects.
35164752	9	70	theme	prostate	1242:1249	arg1	cells					1258:1262	prostate cancer cells	1242:1262	prostate cancer cells	1242:1262	RESULTS Inhibition of CDK9 results in an OGT-dependent remodeling of the proteome in prostate cancer cells.
35164752	13	71	theme	cancer	1720:1725	arg1	cells					1727:1731	prostate cancer cells	1711:1731	prostate cancer cells	1711:1731	Combined inhibition of CDK9 and OGT or MRE11 further decreases RNA polymerase II activity, induces DNA damage signaling, and blocks the survival of prostate cancer cells.
35164752	4	72	theme	elongation	640:649	arg1	CDK9					658:661	the transcription elongation kinase CDK9	622:661	the transcription elongation kinase CDK9	622:661	We have shown that combined inhibition of OGT and the transcription elongation kinase CDK9 induce CRPC-selective anti-proliferative effects.
35164752	15	73	theme	MRE11	1851:1855	arg1	chromatin-loading					1857:1873	MRE11 chromatin-loading	1851:1873	MRE11 chromatin-loading in cells treated with CDK9 inhibitor	1851:1910	Mechanistically, OGT activity is required for MRE11 chromatin-loading in cells treated with CDK9 inhibitor.
35164752	7	74	theme	multiple	1064:1071	arg1	models					1078:1083	multiple CRPC models	1064:1083	multiple CRPC models	1064:1083	In addition, we used both ChIP-seq and RNA-seq profiling, and pulldown experiments in multiple CRPC models.
35164752	13	75	theme	Combined	1563:1570	arg1	inhibition					1572:1581	Combined inhibition	1563:1581	Combined inhibition of CDK9 and OGT or MRE11	1563:1606	Combined inhibition of CDK9 and OGT or MRE11 further decreases RNA polymerase II activity, induces DNA damage signaling, and blocks the survival of prostate cancer cells.
35164752	7	76	theme	pulldown	1040:1047	arg1	experiments					1049:1059	pulldown experiments	1040:1059	pulldown experiments	1040:1059	In addition, we used both ChIP-seq and RNA-seq profiling, and pulldown experiments in multiple CRPC models.
35164752	18	77	theme	CRPC	2295:2298	arg1	setting					2300:2306	CRPC setting	2295:2306	CRPC setting	2295:2306	Our study raises the possibility of targeting CDK9 to elicit DNA damage in CRPC setting as an adjuvant to other treatments.
35164752	1	78	theme	DNA	138:140	arg1	damage					142:147	DNA damage	138:147	DNA damage response	138:156	BACKGROUND Transcription, metabolism and DNA damage response are tightly regulated to preserve the genomic integrity, and O-GlcNAc transferase (OGT) is positioned to connect the three.
35164752	18	79	theme	other	2326:2330	arg1	treatments					2332:2341	other treatments	2326:2341	other treatments	2326:2341	Our study raises the possibility of targeting CDK9 to elicit DNA damage in CRPC setting as an adjuvant to other treatments.
35164752	7	80	theme	RNA-seq	1017:1023	arg1	profiling					1025:1033	RNA-seq profiling	1017:1033	RNA-seq profiling	1017:1033	In addition, we used both ChIP-seq and RNA-seq profiling, and pulldown experiments in multiple CRPC models.
35164752	17	81	theme	DNA	2208:2210	arg1	damage					2212:2217	CDK9 inhibitor-induced DNA damage	2185:2217	CDK9 inhibitor-induced DNA damage	2185:2217	CONCLUSIONS Both OGT and MRE11 are essential for the repair of CDK9 inhibitor-induced DNA damage.
35164752	18	82	from	damage	2285:2290	arg1	setting					2300:2306	CRPC setting	2295:2306	CRPC setting	2295:2306	Our study raises the possibility of targeting CDK9 to elicit DNA damage in CRPC setting as an adjuvant to other treatments.
35164752	6	83	theme	effects	871:877	arg1	profiling					832:840	comprehensive mass spectrometry profiling	800:840	comprehensive mass spectrometry profiling of short-term CDK9 inhibitor effects on O-GlcNAcylated proteins	800:904	METHODS We used comprehensive mass spectrometry profiling of short-term CDK9 inhibitor effects on O-GlcNAcylated proteins in an isogenic cell line system that models transition from PC to CRPC.
35164752	16	84	theme	MRE11	2051:2055	arg1	activity					2057:2064	MRE11 activity	2051:2064	MRE11 activity	2051:2064	Finally, we show that MRE11 and O-GlcNAc are enriched at the prostate cancer-specific small nucleotide polymorphic sites, and the loss of MRE11 activity results in a hyper-mutator phenotype in patient tumors.
35164752	13	85	theme	prostate	1711:1718	arg1	cells					1727:1731	prostate cancer cells	1711:1731	prostate cancer cells	1711:1731	Combined inhibition of CDK9 and OGT or MRE11 further decreases RNA polymerase II activity, induces DNA damage signaling, and blocks the survival of prostate cancer cells.
35164752	10	86	theme	damage	1308:1313	arg1	repair					1315:1320	DNA damage repair	1304:1320	the DNA damage repair protein MRE11	1300:1334	More specifically, the activity of the DNA damage repair protein MRE11 is regulated in response to CDK9 inhibition in an OGT-dependent manner.
35164752	6	87	from	effects	871:877	arg1	proteins					897:904	O-GlcNAcylated proteins	882:904	O-GlcNAcylated proteins	882:904	METHODS We used comprehensive mass spectrometry profiling of short-term CDK9 inhibitor effects on O-GlcNAcylated proteins in an isogenic cell line system that models transition from PC to CRPC.
35164752	11	88	theme	O-GlcNAc-marked	1433:1447	arg1	loci					1449:1452	the O-GlcNAc-marked loci	1429:1452	the O-GlcNAc-marked loci	1429:1452	MRE11 is enriched at the O-GlcNAc-marked loci.
35164752	3	89	theme	cancer	431:436	arg1	patients					438:445	prostate cancer patients	422:445	prostate cancer patients	422:445	However, a significant number of prostate cancer patients develop resistance against anti-androgens, and this incurable disease is termed castration-resistant prostate cancer (CRPC).
35164752	16	90	theme	prostate	1974:1981	arg1	sites					2028:2032	the prostate cancer-specific small nucleotide polymorphic sites	1970:2032	the prostate cancer-specific small nucleotide polymorphic sites	1970:2032	Finally, we show that MRE11 and O-GlcNAc are enriched at the prostate cancer-specific small nucleotide polymorphic sites, and the loss of MRE11 activity results in a hyper-mutator phenotype in patient tumors.
35164752	18	91	theme	targeting	2256:2264	arg1	CDK9					2266:2269	targeting CDK9	2256:2269	targeting CDK9	2256:2269	Our study raises the possibility of targeting CDK9 to elicit DNA damage in CRPC setting as an adjuvant to other treatments.
35164752	14	92	theme	prostate	1789:1796	arg1	cells					1798:1802	normal prostate cells	1782:1802	normal prostate cells	1782:1802	These effects are seen in CRPC cells but not in normal prostate cells.
35164752	16	93	theme	small	1999:2003	arg1	sites					2028:2032	the prostate cancer-specific small nucleotide polymorphic sites	1970:2032	the prostate cancer-specific small nucleotide polymorphic sites	1970:2032	Finally, we show that MRE11 and O-GlcNAc are enriched at the prostate cancer-specific small nucleotide polymorphic sites, and the loss of MRE11 activity results in a hyper-mutator phenotype in patient tumors.
35164752	16	94	theme	nucleotide	2005:2014	arg1	sites					2028:2032	the prostate cancer-specific small nucleotide polymorphic sites	1970:2032	the prostate cancer-specific small nucleotide polymorphic sites	1970:2032	Finally, we show that MRE11 and O-GlcNAc are enriched at the prostate cancer-specific small nucleotide polymorphic sites, and the loss of MRE11 activity results in a hyper-mutator phenotype in patient tumors.
35164752	17	95	theme	inhibitor-induced	2190:2206	arg1	damage					2212:2217	CDK9 inhibitor-induced DNA damage	2185:2217	CDK9 inhibitor-induced DNA damage	2185:2217	CONCLUSIONS Both OGT and MRE11 are essential for the repair of CDK9 inhibitor-induced DNA damage.
35164752	10	96	theme	protein	1322:1328	arg1	MRE11					1330:1334	the DNA damage repair protein MRE11	1300:1334	the DNA damage repair protein MRE11	1300:1334	More specifically, the activity of the DNA damage repair protein MRE11 is regulated in response to CDK9 inhibition in an OGT-dependent manner.
35164752	18	97	theme	DNA	2281:2283	arg1	damage					2285:2290	DNA damage	2281:2290	DNA damage in CRPC setting	2281:2306	Our study raises the possibility of targeting CDK9 to elicit DNA damage in CRPC setting as an adjuvant to other treatments.
35164752	3	98	theme	significant	400:410	arg1	number					412:417	a significant number	398:417	a significant number of prostate cancer patients	398:445	However, a significant number of prostate cancer patients develop resistance against anti-androgens, and this incurable disease is termed castration-resistant prostate cancer (CRPC).
35164752	13	99	theme	damage	1666:1671	arg1	signaling					1673:1681	DNA damage signaling	1662:1681	DNA damage signaling	1662:1681	Combined inhibition of CDK9 and OGT or MRE11 further decreases RNA polymerase II activity, induces DNA damage signaling, and blocks the survival of prostate cancer cells.
35164752	16	100	from	phenotype	2093:2101	arg1	tumors					2114:2119	patient tumors	2106:2119	patient tumors	2106:2119	Finally, we show that MRE11 and O-GlcNAc are enriched at the prostate cancer-specific small nucleotide polymorphic sites, and the loss of MRE11 activity results in a hyper-mutator phenotype in patient tumors.
35164752	8	101	theme	prostate	1124:1131	arg1	samples					1148:1154	prostate cancer patient samples	1124:1154	prostate cancer patient samples	1124:1154	Finally, we validated our findings in prostate cancer patient samples.
35164752	13	102	theme	polymerase	1630:1639	arg1	activity					1644:1651	RNA polymerase II activity	1626:1651	RNA polymerase II activity	1626:1651	Combined inhibition of CDK9 and OGT or MRE11 further decreases RNA polymerase II activity, induces DNA damage signaling, and blocks the survival of prostate cancer cells.
35164752	9	103	theme	RESULTS	1157:1163	arg1	Inhibition					1165:1174	RESULTS Inhibition	1157:1174	RESULTS Inhibition of CDK9	1157:1182	RESULTS Inhibition of CDK9 results in an OGT-dependent remodeling of the proteome in prostate cancer cells.
35164752	14	104	theme	CRPC	1760:1763	arg1	cells					1765:1769	CRPC cells	1760:1769	CRPC cells	1760:1769	These effects are seen in CRPC cells but not in normal prostate cells.
35164752	8	105	theme	patient	1140:1146	arg1	samples					1148:1154	prostate cancer patient samples	1124:1154	prostate cancer patient samples	1124:1154	Finally, we validated our findings in prostate cancer patient samples.
35164752	2	106	theme	common	310:315	arg1	cancer					317:322	the most common cancer	301:322	the most common cancer in men	301:329	Prostate cancer is the most common cancer in men, and androgen-ablation therapy halts disease progression.
35164752	2	106	theme	common	310:315	arg1	cancer					291:296	Prostate cancer	282:296	Prostate cancer	282:296	Prostate cancer is the most common cancer in men, and androgen-ablation therapy halts disease progression.
35164752	6	107	theme	inhibitor	861:869	arg1	effects					871:877	short-term CDK9 inhibitor effects	845:877	short-term CDK9 inhibitor effects on O-GlcNAcylated proteins	845:904	METHODS We used comprehensive mass spectrometry profiling of short-term CDK9 inhibitor effects on O-GlcNAcylated proteins in an isogenic cell line system that models transition from PC to CRPC.
35164752	17	108	dep	CONCLUSIONS	2122:2132	arg1	OGT					2139:2141	OGT	2139:2141	OGT	2139:2141	CONCLUSIONS Both OGT and MRE11 are essential for the repair of CDK9 inhibitor-induced DNA damage.
35164752	17	108	dep	CONCLUSIONS	2122:2132	arg1	CONCLUSIONS					2122:2132	CONCLUSIONS Both OGT and MRE11	2122:2151	CONCLUSIONS Both OGT and MRE11	2122:2151	CONCLUSIONS Both OGT and MRE11 are essential for the repair of CDK9 inhibitor-induced DNA damage.
35164752	17	108	dep	CONCLUSIONS	2122:2132	arg1	MRE11					2147:2151	MRE11	2147:2151	MRE11	2147:2151	CONCLUSIONS Both OGT and MRE11 are essential for the repair of CDK9 inhibitor-induced DNA damage.
35164752	2	109	theme	androgen-ablation	336:352	arg1	therapy					354:360	androgen-ablation therapy	336:360	androgen-ablation therapy	336:360	Prostate cancer is the most common cancer in men, and androgen-ablation therapy halts disease progression.
26305326	7	0	theme	cleavage	842:849	arg1	site					851:854	the cleavage site	838:854	the cleavage site that is intimately involved in the cleavage reaction	838:907	The glutamate residue at the cleavage site that is intimately involved in the cleavage reaction specifically inhibits association with OGT and its bound cofactor UDP-GlcNAc.
26305326	6	1	theme	cleavage	752:759	arg1	signal					761:766	the HCF-1PRO-repeat cleavage signal	732:766	the HCF-1PRO-repeat cleavage signal	732:766	We show that the HCF-1PRO-repeat cleavage signal possesses particular OGT-binding properties.
26305326	2	2	theme	cycle	381:385	arg1	phases					353:358	distinct phases	344:358	distinct phases of the cell-division cycle	344:385	HCF-1 proteolysis results in two active, noncovalently associated HCF-1N and HCF-1C subunits that regulate distinct phases of the cell-division cycle.
26305326	4	3	theme	repeat	602:607	arg1	sequences					609:617	six highly conserved 26 amino acid repeat sequences	567:617	six highly conserved 26 amino acid repeat sequences called HCF-1PRO repeats	567:641	OGT cleaves HCF-1 at six highly conserved 26 amino acid repeat sequences called HCF-1PRO repeats.
26305326	4	3	theme	repeat	602:607	arg1	repeats					635:641	repeats	635:641	repeats	635:641	OGT cleaves HCF-1 at six highly conserved 26 amino acid repeat sequences called HCF-1PRO repeats.
26305326	4	3	theme	repeat	602:607	arg1	HCF-1PRO					626:633	HCF-1PRO	626:633	HCF-1PRO	626:633	OGT cleaves HCF-1 at six highly conserved 26 amino acid repeat sequences called HCF-1PRO repeats.
26305326	8	4	theme	nearby	1037:1042	arg1	sequence					1028:1035	a novel OGT-binding sequence	1008:1035	a novel OGT-binding sequence nearby the first HCF-1PRO-repeat cleavage signal that enhances cleavage	1008:1107	Further, we identify a novel OGT-binding sequence nearby the first HCF-1PRO-repeat cleavage signal that enhances cleavage.
26305326	1	5	theme	complex	143:149	arg1	process					162:168	a complex maturation process	141:168	a complex maturation process involving extensive O-GlcNAcylation and site-specific proteolysis	141:234	Human HCF-1 (also referred to as HCFC-1) is a transcriptional co-regulator that undergoes a complex maturation process involving extensive O-GlcNAcylation and site-specific proteolysis.
26305326	4	6	theme	acid	597:600	arg1	sequences					609:617	six highly conserved 26 amino acid repeat sequences	567:617	six highly conserved 26 amino acid repeat sequences called HCF-1PRO repeats	567:641	OGT cleaves HCF-1 at six highly conserved 26 amino acid repeat sequences called HCF-1PRO repeats.
26305326	4	6	theme	acid	597:600	arg1	repeats					635:641	repeats	635:641	repeats	635:641	OGT cleaves HCF-1 at six highly conserved 26 amino acid repeat sequences called HCF-1PRO repeats.
26305326	4	6	theme	acid	597:600	arg1	HCF-1PRO					626:633	HCF-1PRO	626:633	HCF-1PRO	626:633	OGT cleaves HCF-1 at six highly conserved 26 amino acid repeat sequences called HCF-1PRO repeats.
26305326	2	7	theme	cell-division	367:379	arg1	cycle					381:385	the cell-division cycle	363:385	the cell-division cycle	363:385	HCF-1 proteolysis results in two active, noncovalently associated HCF-1N and HCF-1C subunits that regulate distinct phases of the cell-division cycle.
26305326	9	8	theme	protease	1260:1267	arg1	activity					1269:1276	this unusual protease activity	1247:1276	this unusual protease activity	1247:1276	These results demonstrate that distinct OGT-binding sites in HCF-1 promote proteolysis, and provide novel insights into the mechanism of this unusual protease activity.
26305326	8	9	theme	novel	1010:1014	arg1	sequence					1028:1035	a novel OGT-binding sequence	1008:1035	a novel OGT-binding sequence nearby the first HCF-1PRO-repeat cleavage signal that enhances cleavage	1008:1107	Further, we identify a novel OGT-binding sequence nearby the first HCF-1PRO-repeat cleavage signal that enhances cleavage.
26305326	3	10	theme	HCF-1	388:392	arg1	O-GlcNAcylation					394:408	HCF-1 O-GlcNAcylation	388:408	HCF-1 O-GlcNAcylation	388:408	HCF-1 O-GlcNAcylation and site-specific proteolysis are both catalyzed by O-GlcNAc transferase (OGT), which thus displays an unusual dual enzymatic activity.
26305326	8	11	theme	first	1048:1052	arg1	signal					1079:1084	the first HCF-1PRO-repeat cleavage signal	1044:1084	the first HCF-1PRO-repeat cleavage signal that enhances cleavage	1044:1107	Further, we identify a novel OGT-binding sequence nearby the first HCF-1PRO-repeat cleavage signal that enhances cleavage.
26305326	2	12	theme	HCF-1N	303:308	arg1	subunits					321:328	two active, noncovalently associated HCF-1N and HCF-1C subunits	266:328	two active, noncovalently associated HCF-1N and HCF-1C subunits that regulate distinct phases of the cell-division cycle	266:385	HCF-1 proteolysis results in two active, noncovalently associated HCF-1N and HCF-1C subunits that regulate distinct phases of the cell-division cycle.
26305326	6	13	theme	HCF-1PRO-repeat	736:750	arg1	signal					761:766	the HCF-1PRO-repeat cleavage signal	732:766	the HCF-1PRO-repeat cleavage signal	732:766	We show that the HCF-1PRO-repeat cleavage signal possesses particular OGT-binding properties.
26305326	9	14	theme	OGT-binding	1150:1160	arg1	sites					1162:1166	distinct OGT-binding sites	1141:1166	distinct OGT-binding sites in HCF-1	1141:1175	These results demonstrate that distinct OGT-binding sites in HCF-1 promote proteolysis, and provide novel insights into the mechanism of this unusual protease activity.
26305326	1	15	theme	maturation	151:160	arg1	process					162:168	a complex maturation process	141:168	a complex maturation process involving extensive O-GlcNAcylation and site-specific proteolysis	141:234	Human HCF-1 (also referred to as HCFC-1) is a transcriptional co-regulator that undergoes a complex maturation process involving extensive O-GlcNAcylation and site-specific proteolysis.
26305326	7	16	from	site	851:854	arg1	residue					827:833	The glutamate residue	813:833	The glutamate residue at the cleavage site that is intimately involved in the cleavage reaction	813:907	The glutamate residue at the cleavage site that is intimately involved in the cleavage reaction specifically inhibits association with OGT and its bound cofactor UDP-GlcNAc.
26305326	8	17	theme	cleavage	1070:1077	arg1	signal					1079:1084	the first HCF-1PRO-repeat cleavage signal	1044:1084	the first HCF-1PRO-repeat cleavage signal that enhances cleavage	1044:1107	Further, we identify a novel OGT-binding sequence nearby the first HCF-1PRO-repeat cleavage signal that enhances cleavage.
26305326	7	18	theme	cleavage	891:898	arg1	reaction					900:907	the cleavage reaction	887:907	the cleavage reaction	887:907	The glutamate residue at the cleavage site that is intimately involved in the cleavage reaction specifically inhibits association with OGT and its bound cofactor UDP-GlcNAc.
26305326	0	19	theme	OGT-Binding	9:19	arg1	Sites					21:25	Distinct OGT-Binding Sites	0:25	Distinct OGT-Binding Sites	0:25	Distinct OGT-Binding Sites Promote HCF-1 Cleavage.
26305326	7	20	with	UDP-GlcNAc	975:984	arg1	OGT					948:950	OGT	948:950	OGT	948:950	The glutamate residue at the cleavage site that is intimately involved in the cleavage reaction specifically inhibits association with OGT and its bound cofactor UDP-GlcNAc.
26305326	3	21	dep	catalyzed	449:457	arg1	both					444:447	both	444:447	both	444:447	HCF-1 O-GlcNAcylation and site-specific proteolysis are both catalyzed by O-GlcNAc transferase (OGT), which thus displays an unusual dual enzymatic activity.
26305326	8	22	theme	HCF-1PRO-repeat	1054:1068	arg1	signal					1079:1084	the first HCF-1PRO-repeat cleavage signal	1044:1084	the first HCF-1PRO-repeat cleavage signal that enhances cleavage	1044:1107	Further, we identify a novel OGT-binding sequence nearby the first HCF-1PRO-repeat cleavage signal that enhances cleavage.
26305326	3	23	theme	O-GlcNAc	462:469	arg1	OGT					484:486	OGT	484:486	OGT	484:486	HCF-1 O-GlcNAcylation and site-specific proteolysis are both catalyzed by O-GlcNAc transferase (OGT), which thus displays an unusual dual enzymatic activity.
26305326	3	23	theme	O-GlcNAc	462:469	arg1	transferase					471:481	O-GlcNAc transferase	462:481	O-GlcNAc transferase (OGT)	462:487	HCF-1 O-GlcNAcylation and site-specific proteolysis are both catalyzed by O-GlcNAc transferase (OGT), which thus displays an unusual dual enzymatic activity.
26305326	0	24	theme	Distinct	0:7	arg1	Sites					21:25	Distinct OGT-Binding Sites	0:25	Distinct OGT-Binding Sites	0:25	Distinct OGT-Binding Sites Promote HCF-1 Cleavage.
26305326	4	25	theme	conserved	578:586	arg1	sequences					609:617	six highly conserved 26 amino acid repeat sequences	567:617	six highly conserved 26 amino acid repeat sequences called HCF-1PRO repeats	567:641	OGT cleaves HCF-1 at six highly conserved 26 amino acid repeat sequences called HCF-1PRO repeats.
26305326	4	25	theme	conserved	578:586	arg1	repeats					635:641	repeats	635:641	repeats	635:641	OGT cleaves HCF-1 at six highly conserved 26 amino acid repeat sequences called HCF-1PRO repeats.
26305326	4	25	theme	conserved	578:586	arg1	HCF-1PRO					626:633	HCF-1PRO	626:633	HCF-1PRO	626:633	OGT cleaves HCF-1 at six highly conserved 26 amino acid repeat sequences called HCF-1PRO repeats.
26305326	5	26	theme	substrate	669:677	arg1	requirements					679:690	the substrate requirements	665:690	the substrate requirements for OGT cleavage of HCF-1	665:716	Here we characterize the substrate requirements for OGT cleavage of HCF-1.
26305326	1	27	theme	extensive	180:188	arg1	O-GlcNAcylation					190:204	extensive O-GlcNAcylation	180:204	extensive O-GlcNAcylation	180:204	Human HCF-1 (also referred to as HCFC-1) is a transcriptional co-regulator that undergoes a complex maturation process involving extensive O-GlcNAcylation and site-specific proteolysis.
26305326	9	28	theme	unusual	1252:1258	arg1	activity					1269:1276	this unusual protease activity	1247:1276	this unusual protease activity	1247:1276	These results demonstrate that distinct OGT-binding sites in HCF-1 promote proteolysis, and provide novel insights into the mechanism of this unusual protease activity.
26305326	4	29	theme	amino	591:595	arg1	sequences					609:617	six highly conserved 26 amino acid repeat sequences	567:617	six highly conserved 26 amino acid repeat sequences called HCF-1PRO repeats	567:641	OGT cleaves HCF-1 at six highly conserved 26 amino acid repeat sequences called HCF-1PRO repeats.
26305326	4	29	theme	amino	591:595	arg1	repeats					635:641	repeats	635:641	repeats	635:641	OGT cleaves HCF-1 at six highly conserved 26 amino acid repeat sequences called HCF-1PRO repeats.
26305326	4	29	theme	amino	591:595	arg1	HCF-1PRO					626:633	HCF-1PRO	626:633	HCF-1PRO	626:633	OGT cleaves HCF-1 at six highly conserved 26 amino acid repeat sequences called HCF-1PRO repeats.
26305326	4	30	dep	called	619:624	arg1	sequences					609:617	six highly conserved 26 amino acid repeat sequences	567:617	six highly conserved 26 amino acid repeat sequences called HCF-1PRO repeats	567:641	OGT cleaves HCF-1 at six highly conserved 26 amino acid repeat sequences called HCF-1PRO repeats.
26305326	4	30	dep	called	619:624	arg1	repeats					635:641	repeats	635:641	repeats	635:641	OGT cleaves HCF-1 at six highly conserved 26 amino acid repeat sequences called HCF-1PRO repeats.
26305326	4	30	dep	called	619:624	arg1	HCF-1PRO					626:633	HCF-1PRO	626:633	HCF-1PRO	626:633	OGT cleaves HCF-1 at six highly conserved 26 amino acid repeat sequences called HCF-1PRO repeats.
26305326	2	31	theme	HCF-1C	314:319	arg1	subunits					321:328	two active, noncovalently associated HCF-1N and HCF-1C subunits	266:328	two active, noncovalently associated HCF-1N and HCF-1C subunits that regulate distinct phases of the cell-division cycle	266:385	HCF-1 proteolysis results in two active, noncovalently associated HCF-1N and HCF-1C subunits that regulate distinct phases of the cell-division cycle.
26305326	8	32	dep	nearby	1037:1042	arg1	signal					1079:1084	the first HCF-1PRO-repeat cleavage signal	1044:1084	the first HCF-1PRO-repeat cleavage signal that enhances cleavage	1044:1107	Further, we identify a novel OGT-binding sequence nearby the first HCF-1PRO-repeat cleavage signal that enhances cleavage.
26305326	3	33	theme	enzymatic	526:534	arg1	activity					536:543	an unusual dual enzymatic activity	510:543	an unusual dual enzymatic activity	510:543	HCF-1 O-GlcNAcylation and site-specific proteolysis are both catalyzed by O-GlcNAc transferase (OGT), which thus displays an unusual dual enzymatic activity.
26305326	3	34	theme	dual	521:524	arg1	activity					536:543	an unusual dual enzymatic activity	510:543	an unusual dual enzymatic activity	510:543	HCF-1 O-GlcNAcylation and site-specific proteolysis are both catalyzed by O-GlcNAc transferase (OGT), which thus displays an unusual dual enzymatic activity.
26305326	2	35	dep	active	270:275	arg1	associated					292:301	associated	292:301	associated	292:301	HCF-1 proteolysis results in two active, noncovalently associated HCF-1N and HCF-1C subunits that regulate distinct phases of the cell-division cycle.
26305326	1	36	theme	site-specific	210:222	arg1	proteolysis					224:234	site-specific proteolysis	210:234	site-specific proteolysis	210:234	Human HCF-1 (also referred to as HCFC-1) is a transcriptional co-regulator that undergoes a complex maturation process involving extensive O-GlcNAcylation and site-specific proteolysis.
26305326	0	37	theme	HCF-1	35:39	arg1	Cleavage					41:48	HCF-1 Cleavage	35:48	HCF-1 Cleavage	35:48	Distinct OGT-Binding Sites Promote HCF-1 Cleavage.
26305326	6	38	contain	possesses	768:776	arg2	properties					801:810	particular OGT-binding properties	778:810	particular OGT-binding properties	778:810	We show that the HCF-1PRO-repeat cleavage signal possesses particular OGT-binding properties.
26305326	6	38	contain	possesses	768:776	arg1	signal					761:766	the HCF-1PRO-repeat cleavage signal	732:766	the HCF-1PRO-repeat cleavage signal	732:766	We show that the HCF-1PRO-repeat cleavage signal possesses particular OGT-binding properties.
26305326	9	39	theme	activity	1269:1276	arg1	mechanism					1234:1242	the mechanism	1230:1242	the mechanism of this unusual protease activity	1230:1276	These results demonstrate that distinct OGT-binding sites in HCF-1 promote proteolysis, and provide novel insights into the mechanism of this unusual protease activity.
26305326	2	40	theme	HCF-1	237:241	arg1	proteolysis					243:253	HCF-1 proteolysis	237:253	HCF-1 proteolysis	237:253	HCF-1 proteolysis results in two active, noncovalently associated HCF-1N and HCF-1C subunits that regulate distinct phases of the cell-division cycle.
26305326	9	41	theme	novel	1210:1214	arg1	insights					1216:1223	novel insights	1210:1223	novel insights into the mechanism of this unusual protease activity	1210:1276	These results demonstrate that distinct OGT-binding sites in HCF-1 promote proteolysis, and provide novel insights into the mechanism of this unusual protease activity.
26305326	3	42	theme	unusual	513:519	arg1	activity					536:543	an unusual dual enzymatic activity	510:543	an unusual dual enzymatic activity	510:543	HCF-1 O-GlcNAcylation and site-specific proteolysis are both catalyzed by O-GlcNAc transferase (OGT), which thus displays an unusual dual enzymatic activity.
26305326	7	43	theme	glutamate	817:825	arg1	residue					827:833	The glutamate residue	813:833	The glutamate residue at the cleavage site that is intimately involved in the cleavage reaction	813:907	The glutamate residue at the cleavage site that is intimately involved in the cleavage reaction specifically inhibits association with OGT and its bound cofactor UDP-GlcNAc.
26305326	5	44	theme	HCF-1	712:716	arg1	cleavage					700:707	OGT cleavage	696:707	OGT cleavage of HCF-1	696:716	Here we characterize the substrate requirements for OGT cleavage of HCF-1.
26305326	5	45	theme	OGT	696:698	arg1	cleavage					700:707	OGT cleavage	696:707	OGT cleavage of HCF-1	696:716	Here we characterize the substrate requirements for OGT cleavage of HCF-1.
26305326	1	46	dep	referred	69:76	arg1	also					64:67	also	64:67	also	64:67	Human HCF-1 (also referred to as HCFC-1) is a transcriptional co-regulator that undergoes a complex maturation process involving extensive O-GlcNAcylation and site-specific proteolysis.
26305326	7	47	theme	cofactor	966:973	arg1	UDP-GlcNAc					975:984	its bound cofactor UDP-GlcNAc	956:984	its bound cofactor UDP-GlcNAc	956:984	The glutamate residue at the cleavage site that is intimately involved in the cleavage reaction specifically inhibits association with OGT and its bound cofactor UDP-GlcNAc.
26305326	9	48	from	sites	1162:1166	arg1	HCF-1					1171:1175	HCF-1	1171:1175	HCF-1	1171:1175	These results demonstrate that distinct OGT-binding sites in HCF-1 promote proteolysis, and provide novel insights into the mechanism of this unusual protease activity.
26305326	6	49	theme	OGT-binding	789:799	arg1	properties					801:810	particular OGT-binding properties	778:810	particular OGT-binding properties	778:810	We show that the HCF-1PRO-repeat cleavage signal possesses particular OGT-binding properties.
26305326	1	50	theme	transcriptional	97:111	arg1	HCF-1					57:61	Human HCF-1	51:61	Human HCF-1 (also referred to as HCFC-1)	51:90	Human HCF-1 (also referred to as HCFC-1) is a transcriptional co-regulator that undergoes a complex maturation process involving extensive O-GlcNAcylation and site-specific proteolysis.
26305326	1	50	theme	transcriptional	97:111	arg1	co-regulator					113:124	a transcriptional co-regulator	95:124	a transcriptional co-regulator that undergoes a complex maturation process involving extensive O-GlcNAcylation and site-specific proteolysis	95:234	Human HCF-1 (also referred to as HCFC-1) is a transcriptional co-regulator that undergoes a complex maturation process involving extensive O-GlcNAcylation and site-specific proteolysis.
26305326	2	51	theme	active	270:275	arg1	subunits					321:328	two active, noncovalently associated HCF-1N and HCF-1C subunits	266:328	two active, noncovalently associated HCF-1N and HCF-1C subunits that regulate distinct phases of the cell-division cycle	266:385	HCF-1 proteolysis results in two active, noncovalently associated HCF-1N and HCF-1C subunits that regulate distinct phases of the cell-division cycle.
26305326	6	52	theme	particular	778:787	arg1	properties					801:810	particular OGT-binding properties	778:810	particular OGT-binding properties	778:810	We show that the HCF-1PRO-repeat cleavage signal possesses particular OGT-binding properties.
26305326	2	53	theme	distinct	344:351	arg1	phases					353:358	distinct phases	344:358	distinct phases of the cell-division cycle	344:385	HCF-1 proteolysis results in two active, noncovalently associated HCF-1N and HCF-1C subunits that regulate distinct phases of the cell-division cycle.
26305326	1	54	dep	HCF-1	57:61	arg1	referred					69:76	referred	69:76	referred to as HCFC-1	69:89	Human HCF-1 (also referred to as HCFC-1) is a transcriptional co-regulator that undergoes a complex maturation process involving extensive O-GlcNAcylation and site-specific proteolysis.
26305326	9	55	theme	distinct	1141:1148	arg1	sites					1162:1166	distinct OGT-binding sites	1141:1166	distinct OGT-binding sites in HCF-1	1141:1175	These results demonstrate that distinct OGT-binding sites in HCF-1 promote proteolysis, and provide novel insights into the mechanism of this unusual protease activity.
26305326	7	56	theme	bound	960:964	arg1	UDP-GlcNAc					975:984	its bound cofactor UDP-GlcNAc	956:984	its bound cofactor UDP-GlcNAc	956:984	The glutamate residue at the cleavage site that is intimately involved in the cleavage reaction specifically inhibits association with OGT and its bound cofactor UDP-GlcNAc.
26305326	7	57	with	association	931:941	arg1	OGT					948:950	OGT	948:950	OGT	948:950	The glutamate residue at the cleavage site that is intimately involved in the cleavage reaction specifically inhibits association with OGT and its bound cofactor UDP-GlcNAc.
26305326	1	58	theme	Human	51:55	arg1	HCF-1					57:61	Human HCF-1	51:61	Human HCF-1 (also referred to as HCFC-1)	51:90	Human HCF-1 (also referred to as HCFC-1) is a transcriptional co-regulator that undergoes a complex maturation process involving extensive O-GlcNAcylation and site-specific proteolysis.
26305326	1	58	theme	Human	51:55	arg1	co-regulator					113:124	a transcriptional co-regulator	95:124	a transcriptional co-regulator that undergoes a complex maturation process involving extensive O-GlcNAcylation and site-specific proteolysis	95:234	Human HCF-1 (also referred to as HCFC-1) is a transcriptional co-regulator that undergoes a complex maturation process involving extensive O-GlcNAcylation and site-specific proteolysis.
26305326	8	59	theme	OGT-binding	1016:1026	arg1	sequence					1028:1035	a novel OGT-binding sequence	1008:1035	a novel OGT-binding sequence nearby the first HCF-1PRO-repeat cleavage signal that enhances cleavage	1008:1107	Further, we identify a novel OGT-binding sequence nearby the first HCF-1PRO-repeat cleavage signal that enhances cleavage.
26305326	3	60	theme	site-specific	414:426	arg1	proteolysis					428:438	site-specific proteolysis	414:438	site-specific proteolysis	414:438	HCF-1 O-GlcNAcylation and site-specific proteolysis are both catalyzed by O-GlcNAc transferase (OGT), which thus displays an unusual dual enzymatic activity.
33103664	1	0	theme	crucial	162:168	arg1	roles					170:174	crucial roles	162:174	crucial roles in metazoans	162:187	O-GlcNAcylation is an abundant and dynamic protein posttranslational modification (PTM), with crucial roles in metazoans.
33103664	2	1	theme	native	280:285	arg1	O-GlcNAcylation					287:301	native O-GlcNAcylation	280:301	native O-GlcNAcylation	280:301	Studies of this modification are hampered by the lack of convenient methods for detecting native O-GlcNAcylation.
33103664	0	2	theme	Native	0:5	arg1	detection					7:15	Native detection	0:15	Native detection of protein O-GlcNAcylation by gel electrophoresis.	0:66	Native detection of protein O-GlcNAcylation by gel electrophoresis.
33103664	1	3	theme	abundant	90:97	arg1	PTM					151:153	PTM	151:153	PTM	151:153	O-GlcNAcylation is an abundant and dynamic protein posttranslational modification (PTM), with crucial roles in metazoans.
33103664	1	3	theme	abundant	90:97	arg1	modification					137:148	an abundant and dynamic protein posttranslational modification	87:148	an abundant and dynamic protein posttranslational modification (PTM)	87:154	O-GlcNAcylation is an abundant and dynamic protein posttranslational modification (PTM), with crucial roles in metazoans.
33103664	1	3	theme	abundant	90:97	arg1	O-GlcNAcylation					68:82	O-GlcNAcylation	68:82	O-GlcNAcylation	68:82	O-GlcNAcylation is an abundant and dynamic protein posttranslational modification (PTM), with crucial roles in metazoans.
33103664	3	4	theme	Polyacrylamide	391:404	arg1	Electrophoresis					410:424	Polyacrylamide Gel Electrophoresis	391:424	Polyacrylamide Gel Electrophoresis (SOPAGE)	391:433	Here, we describe a novel gel-based approach, Separation of O-GlcNAcylated Proteins by Polyacrylamide Gel Electrophoresis (SOPAGE), which enables detection of O-GlcNAc levels and dynamics.
33103664	3	4	theme	Polyacrylamide	391:404	arg1	SOPAGE					427:432	SOPAGE	427:432	SOPAGE	427:432	Here, we describe a novel gel-based approach, Separation of O-GlcNAcylated Proteins by Polyacrylamide Gel Electrophoresis (SOPAGE), which enables detection of O-GlcNAc levels and dynamics.
33103664	1	5	with	modification	137:148	arg1	roles					170:174	crucial roles	162:174	crucial roles in metazoans	162:187	O-GlcNAcylation is an abundant and dynamic protein posttranslational modification (PTM), with crucial roles in metazoans.
33103664	0	6	theme	protein	20:26	arg1	O-GlcNAcylation					28:42	protein O-GlcNAcylation	20:42	protein O-GlcNAcylation	20:42	Native detection of protein O-GlcNAcylation by gel electrophoresis.
33103664	1	7	theme	dynamic	103:109	arg1	PTM					151:153	PTM	151:153	PTM	151:153	O-GlcNAcylation is an abundant and dynamic protein posttranslational modification (PTM), with crucial roles in metazoans.
33103664	1	7	theme	dynamic	103:109	arg1	modification					137:148	an abundant and dynamic protein posttranslational modification	87:148	an abundant and dynamic protein posttranslational modification (PTM)	87:154	O-GlcNAcylation is an abundant and dynamic protein posttranslational modification (PTM), with crucial roles in metazoans.
33103664	1	7	theme	dynamic	103:109	arg1	O-GlcNAcylation					68:82	O-GlcNAcylation	68:82	O-GlcNAcylation	68:82	O-GlcNAcylation is an abundant and dynamic protein posttranslational modification (PTM), with crucial roles in metazoans.
33103664	3	8	theme	O-GlcNAc	463:470	arg1	levels					472:477	O-GlcNAc levels	463:477	O-GlcNAc levels	463:477	Here, we describe a novel gel-based approach, Separation of O-GlcNAcylated Proteins by Polyacrylamide Gel Electrophoresis (SOPAGE), which enables detection of O-GlcNAc levels and dynamics.
33103664	3	9	theme	Proteins	379:386	arg1	Separation					350:359	Separation	350:359	Separation of O-GlcNAcylated Proteins by Polyacrylamide Gel Electrophoresis (SOPAGE)	350:433	Here, we describe a novel gel-based approach, Separation of O-GlcNAcylated Proteins by Polyacrylamide Gel Electrophoresis (SOPAGE), which enables detection of O-GlcNAc levels and dynamics.
33103664	3	9	theme	Proteins	379:386	arg1	approach					340:347	a novel gel-based approach	322:347	a novel gel-based approach	322:347	Here, we describe a novel gel-based approach, Separation of O-GlcNAcylated Proteins by Polyacrylamide Gel Electrophoresis (SOPAGE), which enables detection of O-GlcNAc levels and dynamics.
33103664	1	10	theme	protein	111:117	arg1	PTM					151:153	PTM	151:153	PTM	151:153	O-GlcNAcylation is an abundant and dynamic protein posttranslational modification (PTM), with crucial roles in metazoans.
33103664	1	10	theme	protein	111:117	arg1	modification					137:148	an abundant and dynamic protein posttranslational modification	87:148	an abundant and dynamic protein posttranslational modification (PTM)	87:154	O-GlcNAcylation is an abundant and dynamic protein posttranslational modification (PTM), with crucial roles in metazoans.
33103664	1	10	theme	protein	111:117	arg1	O-GlcNAcylation					68:82	O-GlcNAcylation	68:82	O-GlcNAcylation	68:82	O-GlcNAcylation is an abundant and dynamic protein posttranslational modification (PTM), with crucial roles in metazoans.
33103664	3	11	theme	levels	472:477	arg1	detection					450:458	detection	450:458	detection of O-GlcNAc levels and dynamics	450:490	Here, we describe a novel gel-based approach, Separation of O-GlcNAcylated Proteins by Polyacrylamide Gel Electrophoresis (SOPAGE), which enables detection of O-GlcNAc levels and dynamics.
33103664	0	12	theme	O-GlcNAcylation	28:42	arg1	detection					7:15	Native detection	0:15	Native detection of protein O-GlcNAcylation by gel electrophoresis.	0:66	Native detection of protein O-GlcNAcylation by gel electrophoresis.
33103664	3	13	theme	O-GlcNAcylated	364:377	arg1	Proteins					379:386	O-GlcNAcylated Proteins	364:386	O-GlcNAcylated Proteins	364:386	Here, we describe a novel gel-based approach, Separation of O-GlcNAcylated Proteins by Polyacrylamide Gel Electrophoresis (SOPAGE), which enables detection of O-GlcNAc levels and dynamics.
33103664	3	14	theme	Gel	406:408	arg1	Electrophoresis					410:424	Polyacrylamide Gel Electrophoresis	391:424	Polyacrylamide Gel Electrophoresis (SOPAGE)	391:433	Here, we describe a novel gel-based approach, Separation of O-GlcNAcylated Proteins by Polyacrylamide Gel Electrophoresis (SOPAGE), which enables detection of O-GlcNAc levels and dynamics.
33103664	3	14	theme	Gel	406:408	arg1	SOPAGE					427:432	SOPAGE	427:432	SOPAGE	427:432	Here, we describe a novel gel-based approach, Separation of O-GlcNAcylated Proteins by Polyacrylamide Gel Electrophoresis (SOPAGE), which enables detection of O-GlcNAc levels and dynamics.
33103664	1	15	theme	posttranslational	119:135	arg1	PTM					151:153	PTM	151:153	PTM	151:153	O-GlcNAcylation is an abundant and dynamic protein posttranslational modification (PTM), with crucial roles in metazoans.
33103664	1	15	theme	posttranslational	119:135	arg1	modification					137:148	an abundant and dynamic protein posttranslational modification	87:148	an abundant and dynamic protein posttranslational modification (PTM)	87:154	O-GlcNAcylation is an abundant and dynamic protein posttranslational modification (PTM), with crucial roles in metazoans.
33103664	1	15	theme	posttranslational	119:135	arg1	O-GlcNAcylation					68:82	O-GlcNAcylation	68:82	O-GlcNAcylation	68:82	O-GlcNAcylation is an abundant and dynamic protein posttranslational modification (PTM), with crucial roles in metazoans.
33103664	0	16	theme	gel	47:49	arg1	electrophoresis					51:65	gel electrophoresis	47:65	gel electrophoresis	47:65	Native detection of protein O-GlcNAcylation by gel electrophoresis.
33103664	2	17	theme	modification	206:217	arg1	Studies					190:196	Studies	190:196	Studies of this modification	190:217	Studies of this modification are hampered by the lack of convenient methods for detecting native O-GlcNAcylation.
33103664	2	18	theme	methods	258:264	arg1	lack					239:242	the lack	235:242	the lack of convenient methods for detecting native O-GlcNAcylation	235:301	Studies of this modification are hampered by the lack of convenient methods for detecting native O-GlcNAcylation.
33103664	2	19	theme	convenient	247:256	arg1	methods					258:264	convenient methods	247:264	convenient methods	247:264	Studies of this modification are hampered by the lack of convenient methods for detecting native O-GlcNAcylation.
33103664	3	20	theme	dynamics	483:490	arg1	detection					450:458	detection	450:458	detection of O-GlcNAc levels and dynamics	450:490	Here, we describe a novel gel-based approach, Separation of O-GlcNAcylated Proteins by Polyacrylamide Gel Electrophoresis (SOPAGE), which enables detection of O-GlcNAc levels and dynamics.
33103664	3	21	theme	novel	324:328	arg1	Separation					350:359	Separation	350:359	Separation of O-GlcNAcylated Proteins by Polyacrylamide Gel Electrophoresis (SOPAGE)	350:433	Here, we describe a novel gel-based approach, Separation of O-GlcNAcylated Proteins by Polyacrylamide Gel Electrophoresis (SOPAGE), which enables detection of O-GlcNAc levels and dynamics.
33103664	3	21	theme	novel	324:328	arg1	approach					340:347	a novel gel-based approach	322:347	a novel gel-based approach	322:347	Here, we describe a novel gel-based approach, Separation of O-GlcNAcylated Proteins by Polyacrylamide Gel Electrophoresis (SOPAGE), which enables detection of O-GlcNAc levels and dynamics.
33103664	3	22	theme	gel-based	330:338	arg1	Separation					350:359	Separation	350:359	Separation of O-GlcNAcylated Proteins by Polyacrylamide Gel Electrophoresis (SOPAGE)	350:433	Here, we describe a novel gel-based approach, Separation of O-GlcNAcylated Proteins by Polyacrylamide Gel Electrophoresis (SOPAGE), which enables detection of O-GlcNAc levels and dynamics.
33103664	3	22	theme	gel-based	330:338	arg1	approach					340:347	a novel gel-based approach	322:347	a novel gel-based approach	322:347	Here, we describe a novel gel-based approach, Separation of O-GlcNAcylated Proteins by Polyacrylamide Gel Electrophoresis (SOPAGE), which enables detection of O-GlcNAc levels and dynamics.
33103664	1	23	from	roles	170:174	arg1	metazoans					179:187	metazoans	179:187	metazoans	179:187	O-GlcNAcylation is an abundant and dynamic protein posttranslational modification (PTM), with crucial roles in metazoans.
32092778	1	0	contain	carry	165:169	arg3	species					207:213	species	207:213	species ranging from bacteria to humans	207:245	Glycosyltransferases carry out important cellular functions in species ranging from bacteria to humans.
32092778	1	0	contain	carry	165:169	arg2	functions					194:202	important cellular functions	175:202	important cellular functions	175:202	Glycosyltransferases carry out important cellular functions in species ranging from bacteria to humans.
32092778	1	0	contain	carry	165:169	arg1	Glycosyltransferases					144:163	Glycosyltransferases	144:163	Glycosyltransferases	144:163	Glycosyltransferases carry out important cellular functions in species ranging from bacteria to humans.
32092778	6	1	theme	other	1171:1175	arg1	enzymes					1192:1198	other group-transfer enzymes	1171:1198	other group-transfer enzymes	1171:1198	We believe this assay will prove valuable not only for the study of OGT, but also more widely as a general approach for the screening of glycosyltransferases and other group-transfer enzymes.
32092778	4	2	theme	inhibitors	844:853	arg1	analysis					809:816	detailed Michaelis-Menten kinetic analysis	775:816	detailed Michaelis-Menten kinetic analysis of various substrates and inhibitors	775:853	We validate the performance and accuracy of the assay using O-GlcNAc transferase (OGT) as a model system through detailed Michaelis-Menten kinetic analysis of various substrates and inhibitors.
32092778	3	3	theme	simple	567:572	arg1	measurements					587:598	simple fluorescence measurements	567:598	simple fluorescence measurements	567:598	Herein, we report a bead-based strategy to measure the group-transfer activity of glycosyltransferases sensitively using simple fluorescence measurements, without the need for coupled enzymes or secondary reactions.
32092778	4	4	theme	various	821:827	arg1	substrates					829:838	various substrates	821:838	various substrates	821:838	We validate the performance and accuracy of the assay using O-GlcNAc transferase (OGT) as a model system through detailed Michaelis-Menten kinetic analysis of various substrates and inhibitors.
32092778	6	5	theme	enzymes	1192:1198	arg1	screening					1133:1141	the screening	1129:1141	the screening of glycosyltransferases and other group-transfer enzymes	1129:1198	We believe this assay will prove valuable not only for the study of OGT, but also more widely as a general approach for the screening of glycosyltransferases and other group-transfer enzymes.
32092778	4	6	theme	Michaelis-Menten	784:799	arg1	analysis					809:816	detailed Michaelis-Menten kinetic analysis	775:816	detailed Michaelis-Menten kinetic analysis of various substrates and inhibitors	775:853	We validate the performance and accuracy of the assay using O-GlcNAc transferase (OGT) as a model system through detailed Michaelis-Menten kinetic analysis of various substrates and inhibitors.
32092778	6	7	theme	glycosyltransferases	1146:1165	arg1	screening					1133:1141	the screening	1129:1141	the screening of glycosyltransferases and other group-transfer enzymes	1129:1198	We believe this assay will prove valuable not only for the study of OGT, but also more widely as a general approach for the screening of glycosyltransferases and other group-transfer enzymes.
32092778	6	8	theme	group-transfer	1177:1190	arg1	enzymes					1192:1198	other group-transfer enzymes	1171:1198	other group-transfer enzymes	1171:1198	We believe this assay will prove valuable not only for the study of OGT, but also more widely as a general approach for the screening of glycosyltransferases and other group-transfer enzymes.
32092778	5	9	theme	high-throughput	902:916	arg1	screening					918:926	high-throughput screening	902:926	high-throughput screening	902:926	Optimization of this assay and application to high-throughput screening enabled screening for inhibitors of OGT, leading to a novel inhibitory scaffold.
32092778	2	10	theme	activity	308:315	arg1	assays					317:322	simple and robust activity assays	290:322	simple and robust activity assays that can be easily applied to high-throughput screening for inhibitors of these enzymes	290:410	Despite their essential roles in biology, simple and robust activity assays that can be easily applied to high-throughput screening for inhibitors of these enzymes have been challenging to develop.
32092778	5	11	theme	inhibitory	988:997	arg1	scaffold					999:1006	a novel inhibitory scaffold	980:1006	a novel inhibitory scaffold	980:1006	Optimization of this assay and application to high-throughput screening enabled screening for inhibitors of OGT, leading to a novel inhibitory scaffold.
32092778	0	12	theme	O-GlcNAc	122:129	arg1	Transferase					131:141	O-GlcNAc Transferase	122:141	O-GlcNAc Transferase	122:141	A Direct Fluorescent Activity Assay for Glycosyltransferases Enables Convenient High-Throughput Screening: Application to O-GlcNAc Transferase.
32092778	2	13	theme	robust	301:306	arg1	assays					317:322	simple and robust activity assays	290:322	simple and robust activity assays that can be easily applied to high-throughput screening for inhibitors of these enzymes	290:410	Despite their essential roles in biology, simple and robust activity assays that can be easily applied to high-throughput screening for inhibitors of these enzymes have been challenging to develop.
32092778	3	14	theme	bead-based	466:475	arg1	strategy					477:484	a bead-based strategy	464:484	a bead-based strategy to measure the group-transfer activity of glycosyltransferases sensitively using simple fluorescence measurements, without the need for coupled enzymes or secondary reactions	464:659	Herein, we report a bead-based strategy to measure the group-transfer activity of glycosyltransferases sensitively using simple fluorescence measurements, without the need for coupled enzymes or secondary reactions.
32092778	0	15	theme	Direct	2:7	arg1	Assay					30:34	A Direct Fluorescent Activity Assay	0:34	A Direct Fluorescent Activity Assay for Glycosyltransferases	0:59	A Direct Fluorescent Activity Assay for Glycosyltransferases Enables Convenient High-Throughput Screening: Application to O-GlcNAc Transferase.
32092778	3	16	theme	coupled	622:628	arg1	enzymes					630:636	coupled enzymes	622:636	coupled enzymes	622:636	Herein, we report a bead-based strategy to measure the group-transfer activity of glycosyltransferases sensitively using simple fluorescence measurements, without the need for coupled enzymes or secondary reactions.
32092778	2	17	from	roles	272:276	arg1	biology					281:287	biology	281:287	biology	281:287	Despite their essential roles in biology, simple and robust activity assays that can be easily applied to high-throughput screening for inhibitors of these enzymes have been challenging to develop.
32092778	5	18	theme	assay	877:881	arg1	Optimization					856:867	Optimization	856:867	Optimization of this assay	856:881	Optimization of this assay and application to high-throughput screening enabled screening for inhibitors of OGT, leading to a novel inhibitory scaffold.
32092778	5	18	theme	assay	877:881	arg1	application					887:897	application	887:897	application to high-throughput screening	887:926	Optimization of this assay and application to high-throughput screening enabled screening for inhibitors of OGT, leading to a novel inhibitory scaffold.
32092778	4	19	theme	detailed	775:782	arg1	analysis					809:816	detailed Michaelis-Menten kinetic analysis	775:816	detailed Michaelis-Menten kinetic analysis of various substrates and inhibitors	775:853	We validate the performance and accuracy of the assay using O-GlcNAc transferase (OGT) as a model system through detailed Michaelis-Menten kinetic analysis of various substrates and inhibitors.
32092778	4	20	theme	O-GlcNAc	722:729	arg1	system					760:765	a model system	752:765	a model system	752:765	We validate the performance and accuracy of the assay using O-GlcNAc transferase (OGT) as a model system through detailed Michaelis-Menten kinetic analysis of various substrates and inhibitors.
32092778	4	20	theme	O-GlcNAc	722:729	arg1	OGT					744:746	OGT	744:746	OGT	744:746	We validate the performance and accuracy of the assay using O-GlcNAc transferase (OGT) as a model system through detailed Michaelis-Menten kinetic analysis of various substrates and inhibitors.
32092778	4	20	theme	O-GlcNAc	722:729	arg1	transferase					731:741	O-GlcNAc transferase	722:741	O-GlcNAc transferase (OGT)	722:747	We validate the performance and accuracy of the assay using O-GlcNAc transferase (OGT) as a model system through detailed Michaelis-Menten kinetic analysis of various substrates and inhibitors.
32092778	0	21	theme	Activity	21:28	arg1	Assay					30:34	A Direct Fluorescent Activity Assay	0:34	A Direct Fluorescent Activity Assay for Glycosyltransferases	0:59	A Direct Fluorescent Activity Assay for Glycosyltransferases Enables Convenient High-Throughput Screening: Application to O-GlcNAc Transferase.
32092778	6	22	theme	general	1108:1114	arg1	approach					1116:1123	a general approach	1106:1123	a general approach for the screening of glycosyltransferases and other group-transfer enzymes	1106:1198	We believe this assay will prove valuable not only for the study of OGT, but also more widely as a general approach for the screening of glycosyltransferases and other group-transfer enzymes.
32092778	0	23	theme	Fluorescent	9:19	arg1	Assay					30:34	A Direct Fluorescent Activity Assay	0:34	A Direct Fluorescent Activity Assay for Glycosyltransferases	0:59	A Direct Fluorescent Activity Assay for Glycosyltransferases Enables Convenient High-Throughput Screening: Application to O-GlcNAc Transferase.
32092778	4	24	theme	kinetic	801:807	arg1	analysis					809:816	detailed Michaelis-Menten kinetic analysis	775:816	detailed Michaelis-Menten kinetic analysis of various substrates and inhibitors	775:853	We validate the performance and accuracy of the assay using O-GlcNAc transferase (OGT) as a model system through detailed Michaelis-Menten kinetic analysis of various substrates and inhibitors.
32092778	1	25	theme	important	175:183	arg1	functions					194:202	important cellular functions	175:202	important cellular functions	175:202	Glycosyltransferases carry out important cellular functions in species ranging from bacteria to humans.
32092778	5	26	theme	novel	982:986	arg1	scaffold					999:1006	a novel inhibitory scaffold	980:1006	a novel inhibitory scaffold	980:1006	Optimization of this assay and application to high-throughput screening enabled screening for inhibitors of OGT, leading to a novel inhibitory scaffold.
32092778	5	27	theme	OGT	964:966	arg1	inhibitors					950:959	inhibitors	950:959	inhibitors of OGT	950:966	Optimization of this assay and application to high-throughput screening enabled screening for inhibitors of OGT, leading to a novel inhibitory scaffold.
32092778	6	28	dep	believe	1012:1018	arg1	prove					1036:1040	prove	1036:1040	believe this assay will prove valuable not only for the study of OGT, but also more widely as a general approach for the screening of glycosyltransferases and other group-transfer enzymes	1012:1198	We believe this assay will prove valuable not only for the study of OGT, but also more widely as a general approach for the screening of glycosyltransferases and other group-transfer enzymes.
32092778	2	29	theme	essential	262:270	arg1	roles					272:276	their essential roles	256:276	their essential roles in biology	256:287	Despite their essential roles in biology, simple and robust activity assays that can be easily applied to high-throughput screening for inhibitors of these enzymes have been challenging to develop.
32092778	4	30	theme	model	754:758	arg1	system					760:765	a model system	752:765	a model system	752:765	We validate the performance and accuracy of the assay using O-GlcNAc transferase (OGT) as a model system through detailed Michaelis-Menten kinetic analysis of various substrates and inhibitors.
32092778	4	30	theme	model	754:758	arg1	transferase					731:741	O-GlcNAc transferase	722:741	O-GlcNAc transferase (OGT)	722:747	We validate the performance and accuracy of the assay using O-GlcNAc transferase (OGT) as a model system through detailed Michaelis-Menten kinetic analysis of various substrates and inhibitors.
32092778	4	31	dep	performance	678:688	arg1	the					674:676	the	674:676	the	674:676	We validate the performance and accuracy of the assay using O-GlcNAc transferase (OGT) as a model system through detailed Michaelis-Menten kinetic analysis of various substrates and inhibitors.
32092778	3	32	theme	secondary	641:649	arg1	reactions					651:659	secondary reactions	641:659	secondary reactions	641:659	Herein, we report a bead-based strategy to measure the group-transfer activity of glycosyltransferases sensitively using simple fluorescence measurements, without the need for coupled enzymes or secondary reactions.
32092778	3	33	theme	glycosyltransferases	528:547	arg1	activity					516:523	the group-transfer activity	497:523	the group-transfer activity of glycosyltransferases	497:547	Herein, we report a bead-based strategy to measure the group-transfer activity of glycosyltransferases sensitively using simple fluorescence measurements, without the need for coupled enzymes or secondary reactions.
32092778	6	34	theme	OGT	1077:1079	arg1	study					1068:1072	the study	1064:1072	the study of OGT	1064:1079	We believe this assay will prove valuable not only for the study of OGT, but also more widely as a general approach for the screening of glycosyltransferases and other group-transfer enzymes.
32092778	3	35	theme	group-transfer	501:514	arg1	activity					516:523	the group-transfer activity	497:523	the group-transfer activity of glycosyltransferases	497:547	Herein, we report a bead-based strategy to measure the group-transfer activity of glycosyltransferases sensitively using simple fluorescence measurements, without the need for coupled enzymes or secondary reactions.
32092778	4	36	theme	substrates	829:838	arg1	analysis					809:816	detailed Michaelis-Menten kinetic analysis	775:816	detailed Michaelis-Menten kinetic analysis of various substrates and inhibitors	775:853	We validate the performance and accuracy of the assay using O-GlcNAc transferase (OGT) as a model system through detailed Michaelis-Menten kinetic analysis of various substrates and inhibitors.
32092778	2	37	theme	simple	290:295	arg1	assays					317:322	simple and robust activity assays	290:322	simple and robust activity assays that can be easily applied to high-throughput screening for inhibitors of these enzymes	290:410	Despite their essential roles in biology, simple and robust activity assays that can be easily applied to high-throughput screening for inhibitors of these enzymes have been challenging to develop.
32092778	1	38	theme	cellular	185:192	arg1	functions					194:202	important cellular functions	175:202	important cellular functions	175:202	Glycosyltransferases carry out important cellular functions in species ranging from bacteria to humans.
32092778	2	39	theme	high-throughput	354:368	arg1	screening					370:378	high-throughput screening	354:378	high-throughput screening for inhibitors of these enzymes	354:410	Despite their essential roles in biology, simple and robust activity assays that can be easily applied to high-throughput screening for inhibitors of these enzymes have been challenging to develop.
32092778	0	40	theme	High-Throughput	80:94	arg1	Screening					96:104	Convenient High-Throughput Screening	69:104	Convenient High-Throughput Screening	69:104	A Direct Fluorescent Activity Assay for Glycosyltransferases Enables Convenient High-Throughput Screening: Application to O-GlcNAc Transferase.
32092778	2	41	theme	enzymes	404:410	arg1	inhibitors					384:393	inhibitors	384:393	inhibitors of these enzymes	384:410	Despite their essential roles in biology, simple and robust activity assays that can be easily applied to high-throughput screening for inhibitors of these enzymes have been challenging to develop.
32092778	4	42	theme	assay	710:714	arg1	accuracy					694:701	accuracy	694:701	accuracy	694:701	We validate the performance and accuracy of the assay using O-GlcNAc transferase (OGT) as a model system through detailed Michaelis-Menten kinetic analysis of various substrates and inhibitors.
32092778	4	42	theme	assay	710:714	arg1	performance					678:688	performance	678:688	performance	678:688	We validate the performance and accuracy of the assay using O-GlcNAc transferase (OGT) as a model system through detailed Michaelis-Menten kinetic analysis of various substrates and inhibitors.
32092778	0	43	theme	Convenient	69:78	arg1	Screening					96:104	Convenient High-Throughput Screening	69:104	Convenient High-Throughput Screening	69:104	A Direct Fluorescent Activity Assay for Glycosyltransferases Enables Convenient High-Throughput Screening: Application to O-GlcNAc Transferase.
32092778	3	44	theme	fluorescence	574:585	arg1	measurements					587:598	simple fluorescence measurements	567:598	simple fluorescence measurements	567:598	Herein, we report a bead-based strategy to measure the group-transfer activity of glycosyltransferases sensitively using simple fluorescence measurements, without the need for coupled enzymes or secondary reactions.
24563466	2	0	theme	cytoplasmic	516:526	arg1	proteins					547:554	nuclear, cytoplasmic, and mitochondrial proteins	507:554	nuclear, cytoplasmic, and mitochondrial proteins catalyzed exclusively by OGT	507:583	Similar to phosphorylation, catalyzed by kinases such as AMPK, O-GlcNAcylation is a highly dynamic Ser/Thr-specific post-translational modification of nuclear, cytoplasmic, and mitochondrial proteins catalyzed exclusively by OGT.
24563466	9	1	theme	AMPK	1702:1705	arg1	systems					1707:1713	the O-GlcNAc and AMPK systems	1685:1713	systems	1707:1713	We have demonstrated significant cross-talk between the O-GlcNAc and AMPK systems, suggesting OGT and AMPK may cooperatively regulate nutrient-sensitive intracellular processes that mediate cellular metabolism, growth, proliferation, and/or tissue function.
24563466	5	2	theme	acute	923:927	arg1	activation					929:938	acute activation	923:938	acute activation of AMPK	923:946	We show acute activation of AMPK alters the substrate selectivity of OGT in several cell lines and nuclear localization of OGT in C2C12 skeletal muscle myotubes.
24563466	8	3	dep	α-	1453:1454	arg1	the					1449:1451	the	1449:1451	the	1449:1451	Conversely, the α- and γ-subunits of AMPK are O-GlcNAcylated, O-GlcNAcylation of the γ1-subunit increases with AMPK activity, and acute inhibition of O-GlcNAc cycling disrupts activation of AMPK.
24563466	7	4	theme	Thr-444	1273:1279	arg1	phosphorylation					1254:1268	phosphorylation	1254:1268	phosphorylation of Thr-444	1254:1279	AMPK phosphorylates Thr-444 on OGT in vitro; phosphorylation of Thr-444 is tightly associated with AMPK activity and nuclear localization of OGT in myotubes, and phospho-mimetic T444E-OGT exhibits altered substrate selectivity.
24563466	2	5	theme	mitochondrial	533:545	arg1	proteins					547:554	nuclear, cytoplasmic, and mitochondrial proteins	507:554	nuclear, cytoplasmic, and mitochondrial proteins catalyzed exclusively by OGT	507:583	Similar to phosphorylation, catalyzed by kinases such as AMPK, O-GlcNAcylation is a highly dynamic Ser/Thr-specific post-translational modification of nuclear, cytoplasmic, and mitochondrial proteins catalyzed exclusively by OGT.
24563466	0	6	theme	AMP-activated	92:104	arg1	enzymes					52:58	two essential nutrient-sensitive enzymes	19:58	two essential nutrient-sensitive enzymes: O-GlcNAc transferase (OGT) and AMP-activated protein kinase (AMPK)	19:126	Cross-talk between two essential nutrient-sensitive enzymes: O-GlcNAc transferase (OGT) and AMP-activated protein kinase (AMPK).
24563466	0	6	theme	AMP-activated	92:104	arg1	AMPK					122:125	AMPK	122:125	AMPK	122:125	Cross-talk between two essential nutrient-sensitive enzymes: O-GlcNAc transferase (OGT) and AMP-activated protein kinase (AMPK).
24563466	0	6	theme	AMP-activated	92:104	arg1	kinase					114:119	AMP-activated protein kinase	92:119	AMP-activated protein kinase (AMPK)	92:126	Cross-talk between two essential nutrient-sensitive enzymes: O-GlcNAc transferase (OGT) and AMP-activated protein kinase (AMPK).
24563466	3	7	theme	metabolic	711:719	arg1	stress					721:726	metabolic stress	711:726	metabolic stress	711:726	OGT and AMPK target a multitude of intracellular proteins, with the net effect to protect cells from the damaging effects of metabolic stress.
24563466	7	8	theme	altered	1406:1412	arg1	selectivity					1424:1434	altered substrate selectivity	1406:1434	altered substrate selectivity	1406:1434	AMPK phosphorylates Thr-444 on OGT in vitro; phosphorylation of Thr-444 is tightly associated with AMPK activity and nuclear localization of OGT in myotubes, and phospho-mimetic T444E-OGT exhibits altered substrate selectivity.
24563466	5	9	theme	C2C12	1045:1049	arg1	myotubes					1067:1074	C2C12 skeletal muscle myotubes	1045:1074	C2C12 skeletal muscle myotubes	1045:1074	We show acute activation of AMPK alters the substrate selectivity of OGT in several cell lines and nuclear localization of OGT in C2C12 skeletal muscle myotubes.
24563466	5	10	theme	nuclear	1014:1020	arg1	localization					1022:1033	nuclear localization	1014:1033	nuclear localization of OGT in C2C12 skeletal muscle myotubes	1014:1074	We show acute activation of AMPK alters the substrate selectivity of OGT in several cell lines and nuclear localization of OGT in C2C12 skeletal muscle myotubes.
24563466	3	11	with	proteins	635:642	arg1	effect					658:663	the net effect	650:663	the net effect to protect cells from the damaging effects of metabolic stress	650:726	OGT and AMPK target a multitude of intracellular proteins, with the net effect to protect cells from the damaging effects of metabolic stress.
24563466	8	12	theme	acute	1567:1571	arg1	inhibition					1573:1582	acute inhibition	1567:1582	acute inhibition of O-GlcNAc cycling	1567:1602	Conversely, the α- and γ-subunits of AMPK are O-GlcNAcylated, O-GlcNAcylation of the γ1-subunit increases with AMPK activity, and acute inhibition of O-GlcNAc cycling disrupts activation of AMPK.
24563466	5	13	theme	several	991:997	arg1	lines					1004:1008	several cell lines	991:1008	several cell lines	991:1008	We show acute activation of AMPK alters the substrate selectivity of OGT in several cell lines and nuclear localization of OGT in C2C12 skeletal muscle myotubes.
24563466	4	14	theme	upstream	794:801	arg1	processes					828:836	upstream and downstream signaling processes	794:836	upstream and downstream signaling processes	794:836	Despite hundreds of studies demonstrating significant overlap in upstream and downstream signaling processes, no study has investigated if OGT and AMPK can directly regulate each other.
24563466	5	15	from	localization	1022:1033	arg1	myotubes					1067:1074	C2C12 skeletal muscle myotubes	1045:1074	C2C12 skeletal muscle myotubes	1045:1074	We show acute activation of AMPK alters the substrate selectivity of OGT in several cell lines and nuclear localization of OGT in C2C12 skeletal muscle myotubes.
24563466	5	15	from	localization	1022:1033	arg1	lines					1004:1008	several cell lines	991:1008	several cell lines	991:1008	We show acute activation of AMPK alters the substrate selectivity of OGT in several cell lines and nuclear localization of OGT in C2C12 skeletal muscle myotubes.
24563466	1	16	theme	metabolic	264:272	arg1	homeostasis					274:284	metabolic homeostasis	264:284	metabolic homeostasis	264:284	Nutrient-sensitive pathways regulate both O-GlcNAc transferase (OGT) and AMP-activated protein kinase (AMPK), cooperatively connecting metabolic homeostasis to regulation of numerous intracellular processes essential for life.
24563466	2	17	theme	proteins	547:554	arg1	modification					491:502	a highly dynamic Ser/Thr-specific post-translational modification	438:502	a highly dynamic Ser/Thr-specific post-translational modification of nuclear, cytoplasmic, and mitochondrial proteins catalyzed exclusively by OGT	438:583	Similar to phosphorylation, catalyzed by kinases such as AMPK, O-GlcNAcylation is a highly dynamic Ser/Thr-specific post-translational modification of nuclear, cytoplasmic, and mitochondrial proteins catalyzed exclusively by OGT.
24563466	2	17	theme	proteins	547:554	arg1	O-GlcNAcylation					419:433	Similar to phosphorylation, catalyzed by kinases such as AMPK, O-GlcNAcylation	356:433	Similar to phosphorylation, catalyzed by kinases such as AMPK, O-GlcNAcylation	356:433	Similar to phosphorylation, catalyzed by kinases such as AMPK, O-GlcNAcylation is a highly dynamic Ser/Thr-specific post-translational modification of nuclear, cytoplasmic, and mitochondrial proteins catalyzed exclusively by OGT.
24563466	7	18	theme	AMPK	1308:1311	arg1	activity					1313:1320	AMPK activity	1308:1320	AMPK activity	1308:1320	AMPK phosphorylates Thr-444 on OGT in vitro; phosphorylation of Thr-444 is tightly associated with AMPK activity and nuclear localization of OGT in myotubes, and phospho-mimetic T444E-OGT exhibits altered substrate selectivity.
24563466	6	19	from	Lys-9	1177:1181	arg1	histone					1186:1192	histone 3	1186:1194	histone 3 in myotubes	1186:1206	Nuclear localization of OGT affects O-GlcNAcylation of numerous nuclear proteins and acetylation of Lys-9 on histone 3 in myotubes.
24563466	4	20	theme	signaling	818:826	arg1	processes					828:836	upstream and downstream signaling processes	794:836	upstream and downstream signaling processes	794:836	Despite hundreds of studies demonstrating significant overlap in upstream and downstream signaling processes, no study has investigated if OGT and AMPK can directly regulate each other.
24563466	1	21	theme	O-GlcNAc	171:178	arg1	OGT					193:195	OGT	193:195	OGT	193:195	Nutrient-sensitive pathways regulate both O-GlcNAc transferase (OGT) and AMP-activated protein kinase (AMPK), cooperatively connecting metabolic homeostasis to regulation of numerous intracellular processes essential for life.
24563466	1	21	theme	O-GlcNAc	171:178	arg1	transferase					180:190	O-GlcNAc transferase	171:190	O-GlcNAc transferase (OGT)	171:196	Nutrient-sensitive pathways regulate both O-GlcNAc transferase (OGT) and AMP-activated protein kinase (AMPK), cooperatively connecting metabolic homeostasis to regulation of numerous intracellular processes essential for life.
24563466	0	22	theme	protein	106:112	arg1	enzymes					52:58	two essential nutrient-sensitive enzymes	19:58	two essential nutrient-sensitive enzymes: O-GlcNAc transferase (OGT) and AMP-activated protein kinase (AMPK)	19:126	Cross-talk between two essential nutrient-sensitive enzymes: O-GlcNAc transferase (OGT) and AMP-activated protein kinase (AMPK).
24563466	0	22	theme	protein	106:112	arg1	AMPK					122:125	AMPK	122:125	AMPK	122:125	Cross-talk between two essential nutrient-sensitive enzymes: O-GlcNAc transferase (OGT) and AMP-activated protein kinase (AMPK).
24563466	0	22	theme	protein	106:112	arg1	kinase					114:119	AMP-activated protein kinase	92:119	AMP-activated protein kinase (AMPK)	92:126	Cross-talk between two essential nutrient-sensitive enzymes: O-GlcNAc transferase (OGT) and AMP-activated protein kinase (AMPK).
24563466	4	23	theme	downstream	807:816	arg1	processes					828:836	upstream and downstream signaling processes	794:836	upstream and downstream signaling processes	794:836	Despite hundreds of studies demonstrating significant overlap in upstream and downstream signaling processes, no study has investigated if OGT and AMPK can directly regulate each other.
24563466	6	24	theme	OGT	1101:1103	arg1	localization					1085:1096	Nuclear localization	1077:1096	Nuclear localization of OGT	1077:1103	Nuclear localization of OGT affects O-GlcNAcylation of numerous nuclear proteins and acetylation of Lys-9 on histone 3 in myotubes.
24563466	2	25	theme	Ser/Thr-specific	455:470	arg1	modification					491:502	a highly dynamic Ser/Thr-specific post-translational modification	438:502	a highly dynamic Ser/Thr-specific post-translational modification of nuclear, cytoplasmic, and mitochondrial proteins catalyzed exclusively by OGT	438:583	Similar to phosphorylation, catalyzed by kinases such as AMPK, O-GlcNAcylation is a highly dynamic Ser/Thr-specific post-translational modification of nuclear, cytoplasmic, and mitochondrial proteins catalyzed exclusively by OGT.
24563466	2	25	theme	Ser/Thr-specific	455:470	arg1	O-GlcNAcylation					419:433	Similar to phosphorylation, catalyzed by kinases such as AMPK, O-GlcNAcylation	356:433	Similar to phosphorylation, catalyzed by kinases such as AMPK, O-GlcNAcylation	356:433	Similar to phosphorylation, catalyzed by kinases such as AMPK, O-GlcNAcylation is a highly dynamic Ser/Thr-specific post-translational modification of nuclear, cytoplasmic, and mitochondrial proteins catalyzed exclusively by OGT.
24563466	5	26	theme	substrate	959:967	arg1	selectivity					969:979	the substrate selectivity	955:979	the substrate selectivity of OGT in several cell lines	955:1008	We show acute activation of AMPK alters the substrate selectivity of OGT in several cell lines and nuclear localization of OGT in C2C12 skeletal muscle myotubes.
24563466	7	27	theme	OGT	1350:1352	arg1	localization					1334:1345	nuclear localization	1326:1345	nuclear localization of OGT in myotubes	1326:1364	AMPK phosphorylates Thr-444 on OGT in vitro; phosphorylation of Thr-444 is tightly associated with AMPK activity and nuclear localization of OGT in myotubes, and phospho-mimetic T444E-OGT exhibits altered substrate selectivity.
24563466	7	27	theme	OGT	1350:1352	arg1	activity					1313:1320	AMPK activity	1308:1320	AMPK activity	1308:1320	AMPK phosphorylates Thr-444 on OGT in vitro; phosphorylation of Thr-444 is tightly associated with AMPK activity and nuclear localization of OGT in myotubes, and phospho-mimetic T444E-OGT exhibits altered substrate selectivity.
24563466	2	28	theme	dynamic	447:453	arg1	modification					491:502	a highly dynamic Ser/Thr-specific post-translational modification	438:502	a highly dynamic Ser/Thr-specific post-translational modification of nuclear, cytoplasmic, and mitochondrial proteins catalyzed exclusively by OGT	438:583	Similar to phosphorylation, catalyzed by kinases such as AMPK, O-GlcNAcylation is a highly dynamic Ser/Thr-specific post-translational modification of nuclear, cytoplasmic, and mitochondrial proteins catalyzed exclusively by OGT.
24563466	2	28	theme	dynamic	447:453	arg1	O-GlcNAcylation					419:433	Similar to phosphorylation, catalyzed by kinases such as AMPK, O-GlcNAcylation	356:433	Similar to phosphorylation, catalyzed by kinases such as AMPK, O-GlcNAcylation	356:433	Similar to phosphorylation, catalyzed by kinases such as AMPK, O-GlcNAcylation is a highly dynamic Ser/Thr-specific post-translational modification of nuclear, cytoplasmic, and mitochondrial proteins catalyzed exclusively by OGT.
24563466	8	29	theme	cycling	1596:1602	arg1	inhibition					1573:1582	acute inhibition	1567:1582	acute inhibition of O-GlcNAc cycling	1567:1602	Conversely, the α- and γ-subunits of AMPK are O-GlcNAcylated, O-GlcNAcylation of the γ1-subunit increases with AMPK activity, and acute inhibition of O-GlcNAc cycling disrupts activation of AMPK.
24563466	8	30	theme	γ1-subunit	1522:1531	arg1	O-GlcNAcylation					1499:1513	O-GlcNAcylation	1499:1513	O-GlcNAcylation of the γ1-subunit	1499:1531	Conversely, the α- and γ-subunits of AMPK are O-GlcNAcylated, O-GlcNAcylation of the γ1-subunit increases with AMPK activity, and acute inhibition of O-GlcNAc cycling disrupts activation of AMPK.
24563466	5	31	theme	muscle	1060:1065	arg1	myotubes					1067:1074	C2C12 skeletal muscle myotubes	1045:1074	C2C12 skeletal muscle myotubes	1045:1074	We show acute activation of AMPK alters the substrate selectivity of OGT in several cell lines and nuclear localization of OGT in C2C12 skeletal muscle myotubes.
24563466	0	32	theme	essential	23:31	arg1	enzymes					52:58	two essential nutrient-sensitive enzymes	19:58	two essential nutrient-sensitive enzymes: O-GlcNAc transferase (OGT) and AMP-activated protein kinase (AMPK)	19:126	Cross-talk between two essential nutrient-sensitive enzymes: O-GlcNAc transferase (OGT) and AMP-activated protein kinase (AMPK).
24563466	0	32	theme	essential	23:31	arg1	transferase					70:80	O-GlcNAc transferase	61:80	O-GlcNAc transferase (OGT)	61:86	Cross-talk between two essential nutrient-sensitive enzymes: O-GlcNAc transferase (OGT) and AMP-activated protein kinase (AMPK).
24563466	0	32	theme	essential	23:31	arg1	kinase					114:119	AMP-activated protein kinase	92:119	AMP-activated protein kinase (AMPK)	92:126	Cross-talk between two essential nutrient-sensitive enzymes: O-GlcNAc transferase (OGT) and AMP-activated protein kinase (AMPK).
24563466	8	33	theme	O-GlcNAc	1587:1594	arg1	cycling					1596:1602	O-GlcNAc cycling	1587:1602	O-GlcNAc cycling	1587:1602	Conversely, the α- and γ-subunits of AMPK are O-GlcNAcylated, O-GlcNAcylation of the γ1-subunit increases with AMPK activity, and acute inhibition of O-GlcNAc cycling disrupts activation of AMPK.
24563466	6	34	theme	Lys-9	1177:1181	arg1	O-GlcNAcylation					1113:1127	O-GlcNAcylation	1113:1127	O-GlcNAcylation of numerous nuclear proteins	1113:1156	Nuclear localization of OGT affects O-GlcNAcylation of numerous nuclear proteins and acetylation of Lys-9 on histone 3 in myotubes.
24563466	6	34	theme	Lys-9	1177:1181	arg1	acetylation					1162:1172	acetylation	1162:1172	acetylation of Lys-9 on histone 3 in myotubes	1162:1206	Nuclear localization of OGT affects O-GlcNAcylation of numerous nuclear proteins and acetylation of Lys-9 on histone 3 in myotubes.
24563466	5	35	theme	OGT	1038:1040	arg1	localization					1022:1033	nuclear localization	1014:1033	nuclear localization of OGT in C2C12 skeletal muscle myotubes	1014:1074	We show acute activation of AMPK alters the substrate selectivity of OGT in several cell lines and nuclear localization of OGT in C2C12 skeletal muscle myotubes.
24563466	5	35	theme	OGT	1038:1040	arg1	selectivity					969:979	the substrate selectivity	955:979	the substrate selectivity of OGT in several cell lines	955:1008	We show acute activation of AMPK alters the substrate selectivity of OGT in several cell lines and nuclear localization of OGT in C2C12 skeletal muscle myotubes.
24563466	6	36	theme	Nuclear	1077:1083	arg1	localization					1085:1096	Nuclear localization	1077:1096	Nuclear localization of OGT	1077:1103	Nuclear localization of OGT affects O-GlcNAcylation of numerous nuclear proteins and acetylation of Lys-9 on histone 3 in myotubes.
24563466	9	37	theme	tissue	1874:1879	arg1	function					1881:1888	tissue function	1874:1888	tissue function	1874:1888	We have demonstrated significant cross-talk between the O-GlcNAc and AMPK systems, suggesting OGT and AMPK may cooperatively regulate nutrient-sensitive intracellular processes that mediate cellular metabolism, growth, proliferation, and/or tissue function.
24563466	5	38	theme	cell	999:1002	arg1	lines					1004:1008	several cell lines	991:1008	several cell lines	991:1008	We show acute activation of AMPK alters the substrate selectivity of OGT in several cell lines and nuclear localization of OGT in C2C12 skeletal muscle myotubes.
24563466	5	39	theme	OGT	984:986	arg1	localization					1022:1033	nuclear localization	1014:1033	nuclear localization of OGT in C2C12 skeletal muscle myotubes	1014:1074	We show acute activation of AMPK alters the substrate selectivity of OGT in several cell lines and nuclear localization of OGT in C2C12 skeletal muscle myotubes.
24563466	5	39	theme	OGT	984:986	arg1	selectivity					969:979	the substrate selectivity	955:979	the substrate selectivity of OGT in several cell lines	955:1008	We show acute activation of AMPK alters the substrate selectivity of OGT in several cell lines and nuclear localization of OGT in C2C12 skeletal muscle myotubes.
24563466	6	40	theme	nuclear	1141:1147	arg1	proteins					1149:1156	numerous nuclear proteins	1132:1156	numerous nuclear proteins	1132:1156	Nuclear localization of OGT affects O-GlcNAcylation of numerous nuclear proteins and acetylation of Lys-9 on histone 3 in myotubes.
24563466	2	41	theme	nuclear	507:513	arg1	proteins					547:554	nuclear, cytoplasmic, and mitochondrial proteins	507:554	nuclear, cytoplasmic, and mitochondrial proteins catalyzed exclusively by OGT	507:583	Similar to phosphorylation, catalyzed by kinases such as AMPK, O-GlcNAcylation is a highly dynamic Ser/Thr-specific post-translational modification of nuclear, cytoplasmic, and mitochondrial proteins catalyzed exclusively by OGT.
24563466	9	42	theme	O-GlcNAc	1689:1696	arg1	systems					1707:1713	the O-GlcNAc and AMPK systems	1685:1713	systems	1707:1713	We have demonstrated significant cross-talk between the O-GlcNAc and AMPK systems, suggesting OGT and AMPK may cooperatively regulate nutrient-sensitive intracellular processes that mediate cellular metabolism, growth, proliferation, and/or tissue function.
24563466	9	43	theme	nutrient-sensitive	1767:1784	arg1	processes					1800:1808	nutrient-sensitive intracellular processes	1767:1808	nutrient-sensitive intracellular processes that mediate cellular metabolism, growth, proliferation, and/or tissue function	1767:1888	We have demonstrated significant cross-talk between the O-GlcNAc and AMPK systems, suggesting OGT and AMPK may cooperatively regulate nutrient-sensitive intracellular processes that mediate cellular metabolism, growth, proliferation, and/or tissue function.
24563466	3	44	theme	intracellular	621:633	arg1	proteins					635:642	intracellular proteins	621:642	intracellular proteins	621:642	OGT and AMPK target a multitude of intracellular proteins, with the net effect to protect cells from the damaging effects of metabolic stress.
24563466	6	45	from	histone	1186:1192	arg1	myotubes					1199:1206	myotubes	1199:1206	myotubes	1199:1206	Nuclear localization of OGT affects O-GlcNAcylation of numerous nuclear proteins and acetylation of Lys-9 on histone 3 in myotubes.
24563466	6	45	from	histone	1186:1192	arg1	O-GlcNAcylation					1113:1127	O-GlcNAcylation	1113:1127	O-GlcNAcylation of numerous nuclear proteins	1113:1156	Nuclear localization of OGT affects O-GlcNAcylation of numerous nuclear proteins and acetylation of Lys-9 on histone 3 in myotubes.
24563466	6	45	from	histone	1186:1192	arg1	acetylation					1162:1172	acetylation	1162:1172	acetylation of Lys-9 on histone 3 in myotubes	1162:1206	Nuclear localization of OGT affects O-GlcNAcylation of numerous nuclear proteins and acetylation of Lys-9 on histone 3 in myotubes.
24563466	1	46	theme	AMP-activated	202:214	arg1	AMPK					232:235	AMPK	232:235	AMPK	232:235	Nutrient-sensitive pathways regulate both O-GlcNAc transferase (OGT) and AMP-activated protein kinase (AMPK), cooperatively connecting metabolic homeostasis to regulation of numerous intracellular processes essential for life.
24563466	1	46	theme	AMP-activated	202:214	arg1	kinase					224:229	AMP-activated protein kinase	202:229	AMP-activated protein kinase (AMPK)	202:236	Nutrient-sensitive pathways regulate both O-GlcNAc transferase (OGT) and AMP-activated protein kinase (AMPK), cooperatively connecting metabolic homeostasis to regulation of numerous intracellular processes essential for life.
24563466	0	47	theme	nutrient-sensitive	33:50	arg1	enzymes					52:58	two essential nutrient-sensitive enzymes	19:58	two essential nutrient-sensitive enzymes: O-GlcNAc transferase (OGT) and AMP-activated protein kinase (AMPK)	19:126	Cross-talk between two essential nutrient-sensitive enzymes: O-GlcNAc transferase (OGT) and AMP-activated protein kinase (AMPK).
24563466	0	47	theme	nutrient-sensitive	33:50	arg1	transferase					70:80	O-GlcNAc transferase	61:80	O-GlcNAc transferase (OGT)	61:86	Cross-talk between two essential nutrient-sensitive enzymes: O-GlcNAc transferase (OGT) and AMP-activated protein kinase (AMPK).
24563466	0	47	theme	nutrient-sensitive	33:50	arg1	kinase					114:119	AMP-activated protein kinase	92:119	AMP-activated protein kinase (AMPK)	92:126	Cross-talk between two essential nutrient-sensitive enzymes: O-GlcNAc transferase (OGT) and AMP-activated protein kinase (AMPK).
24563466	1	48	theme	numerous	303:310	arg1	processes					326:334	numerous intracellular processes	303:334	numerous intracellular processes essential for life	303:353	Nutrient-sensitive pathways regulate both O-GlcNAc transferase (OGT) and AMP-activated protein kinase (AMPK), cooperatively connecting metabolic homeostasis to regulation of numerous intracellular processes essential for life.
24563466	9	49	theme	intracellular	1786:1798	arg1	processes					1800:1808	nutrient-sensitive intracellular processes	1767:1808	nutrient-sensitive intracellular processes that mediate cellular metabolism, growth, proliferation, and/or tissue function	1767:1888	We have demonstrated significant cross-talk between the O-GlcNAc and AMPK systems, suggesting OGT and AMPK may cooperatively regulate nutrient-sensitive intracellular processes that mediate cellular metabolism, growth, proliferation, and/or tissue function.
24563466	3	50	theme	proteins	635:642	arg1	multitude					608:616	a multitude	606:616	a multitude of intracellular proteins, with the net effect to protect cells from the damaging effects of metabolic stress	606:726	OGT and AMPK target a multitude of intracellular proteins, with the net effect to protect cells from the damaging effects of metabolic stress.
24563466	7	51	theme	substrate	1414:1422	arg1	selectivity					1424:1434	altered substrate selectivity	1406:1434	altered substrate selectivity	1406:1434	AMPK phosphorylates Thr-444 on OGT in vitro; phosphorylation of Thr-444 is tightly associated with AMPK activity and nuclear localization of OGT in myotubes, and phospho-mimetic T444E-OGT exhibits altered substrate selectivity.
24563466	1	52	theme	protein	216:222	arg1	AMPK					232:235	AMPK	232:235	AMPK	232:235	Nutrient-sensitive pathways regulate both O-GlcNAc transferase (OGT) and AMP-activated protein kinase (AMPK), cooperatively connecting metabolic homeostasis to regulation of numerous intracellular processes essential for life.
24563466	1	52	theme	protein	216:222	arg1	kinase					224:229	AMP-activated protein kinase	202:229	AMP-activated protein kinase (AMPK)	202:236	Nutrient-sensitive pathways regulate both O-GlcNAc transferase (OGT) and AMP-activated protein kinase (AMPK), cooperatively connecting metabolic homeostasis to regulation of numerous intracellular processes essential for life.
24563466	0	53	theme	O-GlcNAc	61:68	arg1	OGT					83:85	OGT	83:85	OGT	83:85	Cross-talk between two essential nutrient-sensitive enzymes: O-GlcNAc transferase (OGT) and AMP-activated protein kinase (AMPK).
24563466	0	53	theme	O-GlcNAc	61:68	arg1	enzymes					52:58	two essential nutrient-sensitive enzymes	19:58	two essential nutrient-sensitive enzymes: O-GlcNAc transferase (OGT) and AMP-activated protein kinase (AMPK)	19:126	Cross-talk between two essential nutrient-sensitive enzymes: O-GlcNAc transferase (OGT) and AMP-activated protein kinase (AMPK).
24563466	0	53	theme	O-GlcNAc	61:68	arg1	transferase					70:80	O-GlcNAc transferase	61:80	O-GlcNAc transferase (OGT)	61:86	Cross-talk between two essential nutrient-sensitive enzymes: O-GlcNAc transferase (OGT) and AMP-activated protein kinase (AMPK).
24563466	1	54	theme	intracellular	312:324	arg1	processes					326:334	numerous intracellular processes	303:334	numerous intracellular processes essential for life	303:353	Nutrient-sensitive pathways regulate both O-GlcNAc transferase (OGT) and AMP-activated protein kinase (AMPK), cooperatively connecting metabolic homeostasis to regulation of numerous intracellular processes essential for life.
24563466	0	55	dep	enzymes	52:58	arg1	OGT					83:85	OGT	83:85	OGT	83:85	Cross-talk between two essential nutrient-sensitive enzymes: O-GlcNAc transferase (OGT) and AMP-activated protein kinase (AMPK).
24563466	0	55	dep	enzymes	52:58	arg1	enzymes					52:58	two essential nutrient-sensitive enzymes	19:58	two essential nutrient-sensitive enzymes: O-GlcNAc transferase (OGT) and AMP-activated protein kinase (AMPK)	19:126	Cross-talk between two essential nutrient-sensitive enzymes: O-GlcNAc transferase (OGT) and AMP-activated protein kinase (AMPK).
24563466	0	55	dep	enzymes	52:58	arg1	transferase					70:80	O-GlcNAc transferase	61:80	O-GlcNAc transferase (OGT)	61:86	Cross-talk between two essential nutrient-sensitive enzymes: O-GlcNAc transferase (OGT) and AMP-activated protein kinase (AMPK).
24563466	0	55	dep	enzymes	52:58	arg1	AMPK					122:125	AMPK	122:125	AMPK	122:125	Cross-talk between two essential nutrient-sensitive enzymes: O-GlcNAc transferase (OGT) and AMP-activated protein kinase (AMPK).
24563466	0	55	dep	enzymes	52:58	arg1	kinase					114:119	AMP-activated protein kinase	92:119	AMP-activated protein kinase (AMPK)	92:126	Cross-talk between two essential nutrient-sensitive enzymes: O-GlcNAc transferase (OGT) and AMP-activated protein kinase (AMPK).
24563466	2	56	theme	Similar	356:362	arg1	modification					491:502	a highly dynamic Ser/Thr-specific post-translational modification	438:502	a highly dynamic Ser/Thr-specific post-translational modification of nuclear, cytoplasmic, and mitochondrial proteins catalyzed exclusively by OGT	438:583	Similar to phosphorylation, catalyzed by kinases such as AMPK, O-GlcNAcylation is a highly dynamic Ser/Thr-specific post-translational modification of nuclear, cytoplasmic, and mitochondrial proteins catalyzed exclusively by OGT.
24563466	2	56	theme	Similar	356:362	arg1	O-GlcNAcylation					419:433	Similar to phosphorylation, catalyzed by kinases such as AMPK, O-GlcNAcylation	356:433	Similar to phosphorylation, catalyzed by kinases such as AMPK, O-GlcNAcylation	356:433	Similar to phosphorylation, catalyzed by kinases such as AMPK, O-GlcNAcylation is a highly dynamic Ser/Thr-specific post-translational modification of nuclear, cytoplasmic, and mitochondrial proteins catalyzed exclusively by OGT.
24563466	2	57	theme	post-translational	472:489	arg1	modification					491:502	a highly dynamic Ser/Thr-specific post-translational modification	438:502	a highly dynamic Ser/Thr-specific post-translational modification of nuclear, cytoplasmic, and mitochondrial proteins catalyzed exclusively by OGT	438:583	Similar to phosphorylation, catalyzed by kinases such as AMPK, O-GlcNAcylation is a highly dynamic Ser/Thr-specific post-translational modification of nuclear, cytoplasmic, and mitochondrial proteins catalyzed exclusively by OGT.
24563466	2	57	theme	post-translational	472:489	arg1	O-GlcNAcylation					419:433	Similar to phosphorylation, catalyzed by kinases such as AMPK, O-GlcNAcylation	356:433	Similar to phosphorylation, catalyzed by kinases such as AMPK, O-GlcNAcylation	356:433	Similar to phosphorylation, catalyzed by kinases such as AMPK, O-GlcNAcylation is a highly dynamic Ser/Thr-specific post-translational modification of nuclear, cytoplasmic, and mitochondrial proteins catalyzed exclusively by OGT.
24563466	1	58	theme	processes	326:334	arg1	regulation					289:298	regulation	289:298	regulation of numerous intracellular processes essential for life	289:353	Nutrient-sensitive pathways regulate both O-GlcNAc transferase (OGT) and AMP-activated protein kinase (AMPK), cooperatively connecting metabolic homeostasis to regulation of numerous intracellular processes essential for life.
24563466	8	59	theme	AMPK	1548:1551	arg1	activity					1553:1560	AMPK activity	1548:1560	AMPK activity	1548:1560	Conversely, the α- and γ-subunits of AMPK are O-GlcNAcylated, O-GlcNAcylation of the γ1-subunit increases with AMPK activity, and acute inhibition of O-GlcNAc cycling disrupts activation of AMPK.
24563466	3	60	theme	damaging	691:698	arg1	effects					700:706	the damaging effects	687:706	the damaging effects of metabolic stress	687:726	OGT and AMPK target a multitude of intracellular proteins, with the net effect to protect cells from the damaging effects of metabolic stress.
24563466	5	61	theme	skeletal	1051:1058	arg1	myotubes					1067:1074	C2C12 skeletal muscle myotubes	1045:1074	C2C12 skeletal muscle myotubes	1045:1074	We show acute activation of AMPK alters the substrate selectivity of OGT in several cell lines and nuclear localization of OGT in C2C12 skeletal muscle myotubes.
24563466	7	62	from	localization	1334:1345	arg1	myotubes					1357:1364	myotubes	1357:1364	myotubes	1357:1364	AMPK phosphorylates Thr-444 on OGT in vitro; phosphorylation of Thr-444 is tightly associated with AMPK activity and nuclear localization of OGT in myotubes, and phospho-mimetic T444E-OGT exhibits altered substrate selectivity.
24563466	5	63	theme	AMPK	943:946	arg1	activation					929:938	acute activation	923:938	acute activation of AMPK	923:946	We show acute activation of AMPK alters the substrate selectivity of OGT in several cell lines and nuclear localization of OGT in C2C12 skeletal muscle myotubes.
24563466	1	64	theme	essential	336:344	arg1	processes					326:334	numerous intracellular processes	303:334	numerous intracellular processes essential for life	303:353	Nutrient-sensitive pathways regulate both O-GlcNAc transferase (OGT) and AMP-activated protein kinase (AMPK), cooperatively connecting metabolic homeostasis to regulation of numerous intracellular processes essential for life.
24563466	9	65	theme	significant	1654:1664	arg1	cross-talk					1666:1675	significant cross-talk	1654:1675	significant cross-talk between the O-GlcNAc and AMPK systems	1654:1713	We have demonstrated significant cross-talk between the O-GlcNAc and AMPK systems, suggesting OGT and AMPK may cooperatively regulate nutrient-sensitive intracellular processes that mediate cellular metabolism, growth, proliferation, and/or tissue function.
24563466	5	66	dep	show	918:921	arg1	alters					948:953	alters	948:953	show acute activation of AMPK alters the substrate selectivity of OGT in several cell lines and nuclear localization of OGT in C2C12 skeletal muscle myotubes	918:1074	We show acute activation of AMPK alters the substrate selectivity of OGT in several cell lines and nuclear localization of OGT in C2C12 skeletal muscle myotubes.
24563466	6	67	from	acetylation	1162:1172	arg1	histone					1186:1192	histone 3	1186:1194	histone 3 in myotubes	1186:1206	Nuclear localization of OGT affects O-GlcNAcylation of numerous nuclear proteins and acetylation of Lys-9 on histone 3 in myotubes.
24563466	4	68	theme	studies	749:755	arg1	hundreds					737:744	hundreds	737:744	hundreds of studies demonstrating significant overlap in upstream and downstream signaling processes	737:836	Despite hundreds of studies demonstrating significant overlap in upstream and downstream signaling processes, no study has investigated if OGT and AMPK can directly regulate each other.
24563466	9	69	theme	cellular	1823:1830	arg1	metabolism					1832:1841	cellular metabolism	1823:1841	cellular metabolism	1823:1841	We have demonstrated significant cross-talk between the O-GlcNAc and AMPK systems, suggesting OGT and AMPK may cooperatively regulate nutrient-sensitive intracellular processes that mediate cellular metabolism, growth, proliferation, and/or tissue function.
24563466	3	70	theme	net	654:656	arg1	effect					658:663	the net effect	650:663	the net effect to protect cells from the damaging effects of metabolic stress	650:726	OGT and AMPK target a multitude of intracellular proteins, with the net effect to protect cells from the damaging effects of metabolic stress.
24563466	6	71	theme	proteins	1149:1156	arg1	O-GlcNAcylation					1113:1127	O-GlcNAcylation	1113:1127	O-GlcNAcylation of numerous nuclear proteins	1113:1156	Nuclear localization of OGT affects O-GlcNAcylation of numerous nuclear proteins and acetylation of Lys-9 on histone 3 in myotubes.
24563466	6	71	theme	proteins	1149:1156	arg1	acetylation					1162:1172	acetylation	1162:1172	acetylation of Lys-9 on histone 3 in myotubes	1162:1206	Nuclear localization of OGT affects O-GlcNAcylation of numerous nuclear proteins and acetylation of Lys-9 on histone 3 in myotubes.
24563466	7	72	from	activity	1313:1320	arg1	myotubes					1357:1364	myotubes	1357:1364	myotubes	1357:1364	AMPK phosphorylates Thr-444 on OGT in vitro; phosphorylation of Thr-444 is tightly associated with AMPK activity and nuclear localization of OGT in myotubes, and phospho-mimetic T444E-OGT exhibits altered substrate selectivity.
24563466	7	73	theme	nuclear	1326:1332	arg1	localization					1334:1345	nuclear localization	1326:1345	nuclear localization of OGT in myotubes	1326:1364	AMPK phosphorylates Thr-444 on OGT in vitro; phosphorylation of Thr-444 is tightly associated with AMPK activity and nuclear localization of OGT in myotubes, and phospho-mimetic T444E-OGT exhibits altered substrate selectivity.
24563466	8	74	theme	AMPK	1474:1477	arg1	α-					1453:1454	α-	1453:1454	α-	1453:1454	Conversely, the α- and γ-subunits of AMPK are O-GlcNAcylated, O-GlcNAcylation of the γ1-subunit increases with AMPK activity, and acute inhibition of O-GlcNAc cycling disrupts activation of AMPK.
24563466	6	75	from	O-GlcNAcylation	1113:1127	arg1	histone					1186:1192	histone 3	1186:1194	histone 3 in myotubes	1186:1206	Nuclear localization of OGT affects O-GlcNAcylation of numerous nuclear proteins and acetylation of Lys-9 on histone 3 in myotubes.
24563466	1	76	theme	Nutrient-sensitive	129:146	arg1	pathways					148:155	Nutrient-sensitive pathways	129:155	Nutrient-sensitive pathways	129:155	Nutrient-sensitive pathways regulate both O-GlcNAc transferase (OGT) and AMP-activated protein kinase (AMPK), cooperatively connecting metabolic homeostasis to regulation of numerous intracellular processes essential for life.
24563466	5	77	from	selectivity	969:979	arg1	myotubes					1067:1074	C2C12 skeletal muscle myotubes	1045:1074	C2C12 skeletal muscle myotubes	1045:1074	We show acute activation of AMPK alters the substrate selectivity of OGT in several cell lines and nuclear localization of OGT in C2C12 skeletal muscle myotubes.
24563466	5	77	from	selectivity	969:979	arg1	lines					1004:1008	several cell lines	991:1008	several cell lines	991:1008	We show acute activation of AMPK alters the substrate selectivity of OGT in several cell lines and nuclear localization of OGT in C2C12 skeletal muscle myotubes.
24563466	8	78	theme	AMPK	1627:1630	arg1	activation					1613:1622	activation	1613:1622	activation of AMPK	1613:1630	Conversely, the α- and γ-subunits of AMPK are O-GlcNAcylated, O-GlcNAcylation of the γ1-subunit increases with AMPK activity, and acute inhibition of O-GlcNAc cycling disrupts activation of AMPK.
24563466	3	79	theme	stress	721:726	arg1	effects					700:706	the damaging effects	687:706	the damaging effects of metabolic stress	687:726	OGT and AMPK target a multitude of intracellular proteins, with the net effect to protect cells from the damaging effects of metabolic stress.
24563466	7	80	theme	phospho-mimetic	1371:1385	arg1	T444E-OGT					1387:1395	phospho-mimetic T444E-OGT	1371:1395	phospho-mimetic T444E-OGT	1371:1395	AMPK phosphorylates Thr-444 on OGT in vitro; phosphorylation of Thr-444 is tightly associated with AMPK activity and nuclear localization of OGT in myotubes, and phospho-mimetic T444E-OGT exhibits altered substrate selectivity.
24563466	6	81	theme	numerous	1132:1139	arg1	proteins					1149:1156	numerous nuclear proteins	1132:1156	numerous nuclear proteins	1132:1156	Nuclear localization of OGT affects O-GlcNAcylation of numerous nuclear proteins and acetylation of Lys-9 on histone 3 in myotubes.
18174169	10	0	from	decrease	1592:1599	arg1	p					1632:1632	p = 0.03	1632:1639	p = 0.03	1632:1639	In addition, 12-h glucose deprivation leads to a 49% decrease in O-GlcNAcase protein levels (p = 0.03).
18174169	10	0	from	decrease	1592:1599	arg1	levels					1624:1629	O-GlcNAcase protein levels	1604:1629	O-GlcNAcase protein levels (p = 0.03)	1604:1640	In addition, 12-h glucose deprivation leads to a 49% decrease in O-GlcNAcase protein levels (p = 0.03).
18174169	6	1	theme	=	1126:1126	arg1	0.004					1128:1132	p = 0.004	1124:1132	p = 0.004	1124:1132	O-GlcNAcylation of glycogen synthase is significantly increased with glucose deprivation, and this O-GlcNAc increase contributes to a 60% decrease (p = 0.004) in glycogen synthase activity.
18174169	6	1	theme	=	1126:1126	arg1	decrease					1114:1121	a 60% decrease	1108:1121	a 60% decrease (p = 0.004) in glycogen synthase activity	1108:1163	O-GlcNAcylation of glycogen synthase is significantly increased with glucose deprivation, and this O-GlcNAc increase contributes to a 60% decrease (p = 0.004) in glycogen synthase activity.
18174169	10	2	theme	12-h	1552:1555	arg1	deprivation					1565:1575	12-h glucose deprivation	1552:1575	12-h glucose deprivation	1552:1575	In addition, 12-h glucose deprivation leads to a 49% decrease in O-GlcNAcase protein levels (p = 0.03).
18174169	10	3	theme	49	1588:1589	arg1	%					1590:1590	%	1590:1590	%	1590:1590	In addition, 12-h glucose deprivation leads to a 49% decrease in O-GlcNAcase protein levels (p = 0.03).
18174169	11	4	theme	increased	1660:1668	arg1	modification					1679:1690	increased O-GlcNAc modification	1660:1690	increased O-GlcNAc modification stimulated by glucose deprivation	1660:1724	We conclude that increased O-GlcNAc modification stimulated by glucose deprivation results from increased OGT and decreased O-GlcNAcase levels and that these changes affect cell metabolism, thus inactivating glycogen synthase.
18174169	10	5	theme	O-GlcNAcase	1604:1614	arg1	p					1632:1632	p = 0.03	1632:1639	p = 0.03	1632:1639	In addition, 12-h glucose deprivation leads to a 49% decrease in O-GlcNAcase protein levels (p = 0.03).
18174169	10	5	theme	O-GlcNAcase	1604:1614	arg1	levels					1624:1629	O-GlcNAcase protein levels	1604:1629	O-GlcNAcase protein levels (p = 0.03)	1604:1640	In addition, 12-h glucose deprivation leads to a 49% decrease in O-GlcNAcase protein levels (p = 0.03).
18174169	11	6	theme	cell	1816:1819	arg1	metabolism					1821:1830	cell metabolism	1816:1830	cell metabolism	1816:1830	We conclude that increased O-GlcNAc modification stimulated by glucose deprivation results from increased OGT and decreased O-GlcNAcase levels and that these changes affect cell metabolism, thus inactivating glycogen synthase.
18174169	2	7	theme	glucose	339:345	arg1	concentrations					347:360	glucose concentrations	339:360	glucose concentrations	339:360	Here we report on regulation of O-GlcNAcylation over a broad range of glucose concentrations.
18174169	5	8	theme	glucosamine	866:876	arg1	treatment					886:894	high glucose (20 mm) or glucosamine (10 mm) treatment	842:894	high glucose (20 mm) or glucosamine (10 mm) treatment	842:894	Some of the targets of glucose deprivation-induced O-GlcNAcylation are distinct from those modified in response to high glucose (20 mm) or glucosamine (10 mm) treatment, suggesting differential targeting with glucose deprivation and glucose excess.
18174169	6	9	theme	glycogen	995:1002	arg1	synthase					1004:1011	glycogen synthase	995:1011	glycogen synthase	995:1011	O-GlcNAcylation of glycogen synthase is significantly increased with glucose deprivation, and this O-GlcNAc increase contributes to a 60% decrease (p = 0.004) in glycogen synthase activity.
18174169	8	10	theme	O-linked	1327:1334	arg1	OGT					1369:1371	OGT	1369:1371	OGT	1369:1371	Rather, the mRNA for nucleocytoplasmic O-linked N-acetylglucosaminyltransferase (OGT) increases 3.4-fold within 6 h of glucose deprivation (p = 0.006).
18174169	8	10	theme	O-linked	1327:1334	arg1	N-acetylglucosaminyltransferase					1336:1366	nucleocytoplasmic O-linked N-acetylglucosaminyltransferase	1309:1366	nucleocytoplasmic O-linked N-acetylglucosaminyltransferase (OGT)	1309:1372	Rather, the mRNA for nucleocytoplasmic O-linked N-acetylglucosaminyltransferase (OGT) increases 3.4-fold within 6 h of glucose deprivation (p = 0.006).
18174169	5	11	theme	glucose	750:756	arg1	O-GlcNAcylation					778:792	glucose deprivation-induced O-GlcNAcylation	750:792	glucose deprivation-induced O-GlcNAcylation	750:792	Some of the targets of glucose deprivation-induced O-GlcNAcylation are distinct from those modified in response to high glucose (20 mm) or glucosamine (10 mm) treatment, suggesting differential targeting with glucose deprivation and glucose excess.
18174169	4	12	from	increase	621:628	arg1	modification					648:659	total O-GlcNAc modification	633:659	total O-GlcNAc modification	633:659	Beginning 12 h after treatment, glucose-deprived human hepatocellular carcinoma (HepG2) cells demonstrate a 7.8-fold increase in total O-GlcNAc modification compared with cells cultured in normal glucose (5 mm; p = 0.008).
18174169	9	13	theme	normal	1509:1514	arg1	cells					1532:1536	normal glucose-treated cells	1509:1536	normal glucose-treated cells	1509:1536	Within 12 h, OGT protein increases 1.7-fold (p = 0.01) compared with normal glucose-treated cells.
18174169	7	14	theme	Increased	1166:1174	arg1	modification					1185:1196	Increased O-GlcNAc modification	1166:1196	Increased O-GlcNAc modification	1166:1196	Increased O-GlcNAc modification is not mediated by increased UDP-GlcNAc, the rate-limiting substrate for O-GlcNAcylation.
18174169	11	15	theme	decreased	1757:1765	arg1	levels					1779:1784	decreased O-GlcNAcase levels	1757:1784	decreased O-GlcNAcase levels	1757:1784	We conclude that increased O-GlcNAc modification stimulated by glucose deprivation results from increased OGT and decreased O-GlcNAcase levels and that these changes affect cell metabolism, thus inactivating glycogen synthase.
18174169	2	16	theme	O-GlcNAcylation	301:315	arg1	regulation					287:296	regulation	287:296	regulation of O-GlcNAcylation	287:315	Here we report on regulation of O-GlcNAcylation over a broad range of glucose concentrations.
18174169	5	17	theme	glucose	960:966	arg1	excess					968:973	glucose excess	960:973	glucose excess	960:973	Some of the targets of glucose deprivation-induced O-GlcNAcylation are distinct from those modified in response to high glucose (20 mm) or glucosamine (10 mm) treatment, suggesting differential targeting with glucose deprivation and glucose excess.
18174169	0	18	mod	modification	40:51	arg1	proteins					56:63	proteins	56:63	proteins	56:63	Glucose deprivation stimulates O-GlcNAc modification of proteins through up-regulation of O-linked N-acetylglucosaminyltransferase.
18174169	0	18	mod	modification	40:51	arg3	O-GlcNAc					31:38	O-GlcNAc modification	31:51	O-GlcNAc modification of proteins	31:63	Glucose deprivation stimulates O-GlcNAc modification of proteins through up-regulation of O-linked N-acetylglucosaminyltransferase.
18174169	5	19	theme	differential	908:919	arg1	targeting					921:929	differential targeting	908:929	differential targeting with glucose deprivation and glucose excess	908:973	Some of the targets of glucose deprivation-induced O-GlcNAcylation are distinct from those modified in response to high glucose (20 mm) or glucosamine (10 mm) treatment, suggesting differential targeting with glucose deprivation and glucose excess.
18174169	4	20	theme	hepatocellular	559:572	arg1	cells					592:596	glucose-deprived human hepatocellular carcinoma (HepG2) cells	536:596	glucose-deprived human hepatocellular carcinoma (HepG2) cells	536:596	Beginning 12 h after treatment, glucose-deprived human hepatocellular carcinoma (HepG2) cells demonstrate a 7.8-fold increase in total O-GlcNAc modification compared with cells cultured in normal glucose (5 mm; p = 0.008).
18174169	5	21	with	targeting	921:929	arg1	deprivation					944:954	glucose deprivation	936:954	glucose deprivation	936:954	Some of the targets of glucose deprivation-induced O-GlcNAcylation are distinct from those modified in response to high glucose (20 mm) or glucosamine (10 mm) treatment, suggesting differential targeting with glucose deprivation and glucose excess.
18174169	5	21	with	targeting	921:929	arg1	excess					968:973	glucose excess	960:973	glucose excess	960:973	Some of the targets of glucose deprivation-induced O-GlcNAcylation are distinct from those modified in response to high glucose (20 mm) or glucosamine (10 mm) treatment, suggesting differential targeting with glucose deprivation and glucose excess.
18174169	0	22	theme	O-linked	90:97	arg1	N-acetylglucosaminyltransferase					99:129	O-linked N-acetylglucosaminyltransferase	90:129	O-linked N-acetylglucosaminyltransferase	90:129	Glucose deprivation stimulates O-GlcNAc modification of proteins through up-regulation of O-linked N-acetylglucosaminyltransferase.
18174169	1	23	theme	proteins	212:219	arg1	modification					196:207	a post-translational modification	175:207	a post-translational modification of proteins that functions as a nutrient sensing mechanism	175:266	O-Linked N-acetylglucosamine (O-GlcNAc) is a post-translational modification of proteins that functions as a nutrient sensing mechanism.
18174169	1	23	theme	proteins	212:219	arg1	mechanism					258:266	a nutrient sensing mechanism	239:266	a nutrient sensing mechanism	239:266	O-Linked N-acetylglucosamine (O-GlcNAc) is a post-translational modification of proteins that functions as a nutrient sensing mechanism.
18174169	1	23	theme	proteins	212:219	arg1	N-acetylglucosamine					141:159	O-Linked N-acetylglucosamine	132:159	O-Linked N-acetylglucosamine (O-GlcNAc)	132:170	O-Linked N-acetylglucosamine (O-GlcNAc) is a post-translational modification of proteins that functions as a nutrient sensing mechanism.
18174169	6	24	theme	glucose	1045:1051	arg1	deprivation					1053:1063	glucose deprivation	1045:1063	glucose deprivation	1045:1063	O-GlcNAcylation of glycogen synthase is significantly increased with glucose deprivation, and this O-GlcNAc increase contributes to a 60% decrease (p = 0.004) in glycogen synthase activity.
18174169	3	25	theme	O-GlcNAc	409:416	arg1	modification					418:429	O-GlcNAc modification	409:429	O-GlcNAc modification of a limited number of proteins	409:461	We have discovered a significant induction of O-GlcNAc modification of a limited number of proteins under conditions of glucose deprivation.
18174169	5	26	theme	O-GlcNAcylation	778:792	arg1	targets					739:745	the targets	735:745	the targets of glucose deprivation-induced O-GlcNAcylation	735:792	Some of the targets of glucose deprivation-induced O-GlcNAcylation are distinct from those modified in response to high glucose (20 mm) or glucosamine (10 mm) treatment, suggesting differential targeting with glucose deprivation and glucose excess.
18174169	8	27	theme	deprivation	1415:1425	arg1	h					1402:1402	6 h	1400:1402	6 h of glucose deprivation (p = 0.006)	1400:1437	Rather, the mRNA for nucleocytoplasmic O-linked N-acetylglucosaminyltransferase (OGT) increases 3.4-fold within 6 h of glucose deprivation (p = 0.006).
18174169	3	28	theme	deprivation	491:501	arg1	conditions					469:478	conditions	469:478	conditions of glucose deprivation	469:501	We have discovered a significant induction of O-GlcNAc modification of a limited number of proteins under conditions of glucose deprivation.
18174169	3	29	theme	limited	436:442	arg1	number					444:449	a limited number	434:449	a limited number of proteins	434:461	We have discovered a significant induction of O-GlcNAc modification of a limited number of proteins under conditions of glucose deprivation.
18174169	4	30	theme	glucose-deprived	536:551	arg1	cells					592:596	glucose-deprived human hepatocellular carcinoma (HepG2) cells	536:596	glucose-deprived human hepatocellular carcinoma (HepG2) cells	536:596	Beginning 12 h after treatment, glucose-deprived human hepatocellular carcinoma (HepG2) cells demonstrate a 7.8-fold increase in total O-GlcNAc modification compared with cells cultured in normal glucose (5 mm; p = 0.008).
18174169	0	31	theme	Glucose	0:6	arg1	deprivation					8:18	Glucose deprivation	0:18	Glucose deprivation	0:18	Glucose deprivation stimulates O-GlcNAc modification of proteins through up-regulation of O-linked N-acetylglucosaminyltransferase.
18174169	1	32	theme	O-Linked	132:139	arg1	modification					196:207	a post-translational modification	175:207	a post-translational modification of proteins that functions as a nutrient sensing mechanism	175:266	O-Linked N-acetylglucosamine (O-GlcNAc) is a post-translational modification of proteins that functions as a nutrient sensing mechanism.
18174169	1	32	theme	O-Linked	132:139	arg1	O-GlcNAc					162:169	O-GlcNAc	162:169	O-GlcNAc	162:169	O-Linked N-acetylglucosamine (O-GlcNAc) is a post-translational modification of proteins that functions as a nutrient sensing mechanism.
18174169	1	32	theme	O-Linked	132:139	arg1	N-acetylglucosamine					141:159	O-Linked N-acetylglucosamine	132:159	O-Linked N-acetylglucosamine (O-GlcNAc)	132:170	O-Linked N-acetylglucosamine (O-GlcNAc) is a post-translational modification of proteins that functions as a nutrient sensing mechanism.
18174169	6	33	theme	60	1110:1111	arg1	%					1112:1112	%	1112:1112	%	1112:1112	O-GlcNAcylation of glycogen synthase is significantly increased with glucose deprivation, and this O-GlcNAc increase contributes to a 60% decrease (p = 0.004) in glycogen synthase activity.
18174169	4	34	theme	7.8-fold	612:619	arg1	increase					621:628	a 7.8-fold increase	610:628	a 7.8-fold increase in total O-GlcNAc modification	610:659	Beginning 12 h after treatment, glucose-deprived human hepatocellular carcinoma (HepG2) cells demonstrate a 7.8-fold increase in total O-GlcNAc modification compared with cells cultured in normal glucose (5 mm; p = 0.008).
18174169	11	35	theme	glucose	1706:1712	arg1	deprivation					1714:1724	glucose deprivation	1706:1724	glucose deprivation	1706:1724	We conclude that increased O-GlcNAc modification stimulated by glucose deprivation results from increased OGT and decreased O-GlcNAcase levels and that these changes affect cell metabolism, thus inactivating glycogen synthase.
18174169	0	36	theme	proteins	56:63	arg1	modification					40:51	O-GlcNAc modification	31:51	O-GlcNAc modification of proteins	31:63	Glucose deprivation stimulates O-GlcNAc modification of proteins through up-regulation of O-linked N-acetylglucosaminyltransferase.
18174169	8	37	link	O-linked	1327:1334	arg1	OGT					1369:1371	OGT	1369:1371	OGT	1369:1371	Rather, the mRNA for nucleocytoplasmic O-linked N-acetylglucosaminyltransferase (OGT) increases 3.4-fold within 6 h of glucose deprivation (p = 0.006).
18174169	8	37	link	O-linked	1327:1334	arg1	N-acetylglucosaminyltransferase					1336:1366	nucleocytoplasmic O-linked N-acetylglucosaminyltransferase	1309:1366	nucleocytoplasmic O-linked N-acetylglucosaminyltransferase (OGT)	1309:1372	Rather, the mRNA for nucleocytoplasmic O-linked N-acetylglucosaminyltransferase (OGT) increases 3.4-fold within 6 h of glucose deprivation (p = 0.006).
18174169	6	38	theme	synthase	1147:1154	arg1	activity					1156:1163	glycogen synthase activity	1138:1163	glycogen synthase activity	1138:1163	O-GlcNAcylation of glycogen synthase is significantly increased with glucose deprivation, and this O-GlcNAc increase contributes to a 60% decrease (p = 0.004) in glycogen synthase activity.
18174169	11	39	theme	increased	1739:1747	arg1	OGT					1749:1751	increased OGT	1739:1751	increased OGT	1739:1751	We conclude that increased O-GlcNAc modification stimulated by glucose deprivation results from increased OGT and decreased O-GlcNAcase levels and that these changes affect cell metabolism, thus inactivating glycogen synthase.
18174169	4	40	dep	=	717:717	arg1	mm					711:712	5 mm	709:712	5 mm	709:712	Beginning 12 h after treatment, glucose-deprived human hepatocellular carcinoma (HepG2) cells demonstrate a 7.8-fold increase in total O-GlcNAc modification compared with cells cultured in normal glucose (5 mm; p = 0.008).
18174169	9	41	dep	=	1487:1487	arg1	0.01					1489:1492	0.01	1489:1492	0.01	1489:1492	Within 12 h, OGT protein increases 1.7-fold (p = 0.01) compared with normal glucose-treated cells.
18174169	10	42	theme	glucose	1557:1563	arg1	deprivation					1565:1575	12-h glucose deprivation	1552:1575	12-h glucose deprivation	1552:1575	In addition, 12-h glucose deprivation leads to a 49% decrease in O-GlcNAcase protein levels (p = 0.03).
18174169	7	43	theme	rate-limiting	1243:1255	arg1	substrate					1257:1265	the rate-limiting substrate	1239:1265	the rate-limiting substrate for O-GlcNAcylation	1239:1285	Increased O-GlcNAc modification is not mediated by increased UDP-GlcNAc, the rate-limiting substrate for O-GlcNAcylation.
18174169	7	43	theme	rate-limiting	1243:1255	arg1	UDP-GlcNAc					1227:1236	increased UDP-GlcNAc	1217:1236	increased UDP-GlcNAc	1217:1236	Increased O-GlcNAc modification is not mediated by increased UDP-GlcNAc, the rate-limiting substrate for O-GlcNAcylation.
18174169	6	44	theme	p	1124:1124	arg1	0.004					1128:1132	p = 0.004	1124:1132	p = 0.004	1124:1132	O-GlcNAcylation of glycogen synthase is significantly increased with glucose deprivation, and this O-GlcNAc increase contributes to a 60% decrease (p = 0.004) in glycogen synthase activity.
18174169	6	44	theme	p	1124:1124	arg1	decrease					1114:1121	a 60% decrease	1108:1121	a 60% decrease (p = 0.004) in glycogen synthase activity	1108:1163	O-GlcNAcylation of glycogen synthase is significantly increased with glucose deprivation, and this O-GlcNAc increase contributes to a 60% decrease (p = 0.004) in glycogen synthase activity.
18174169	4	45	theme	O-GlcNAc	639:646	arg1	modification					648:659	total O-GlcNAc modification	633:659	total O-GlcNAc modification	633:659	Beginning 12 h after treatment, glucose-deprived human hepatocellular carcinoma (HepG2) cells demonstrate a 7.8-fold increase in total O-GlcNAc modification compared with cells cultured in normal glucose (5 mm; p = 0.008).
18174169	10	46	theme	%	1590:1590	arg1	decrease					1592:1599	a 49% decrease	1586:1599	a 49% decrease in O-GlcNAcase protein levels (p = 0.03)	1586:1640	In addition, 12-h glucose deprivation leads to a 49% decrease in O-GlcNAcase protein levels (p = 0.03).
18174169	9	47	theme	OGT	1453:1455	arg1	protein					1457:1463	OGT protein	1453:1463	OGT protein	1453:1463	Within 12 h, OGT protein increases 1.7-fold (p = 0.01) compared with normal glucose-treated cells.
18174169	11	48	theme	O-GlcNAc	1670:1677	arg1	modification					1679:1690	increased O-GlcNAc modification	1660:1690	increased O-GlcNAc modification stimulated by glucose deprivation	1660:1724	We conclude that increased O-GlcNAc modification stimulated by glucose deprivation results from increased OGT and decreased O-GlcNAcase levels and that these changes affect cell metabolism, thus inactivating glycogen synthase.
18174169	6	49	from	decrease	1114:1121	arg1	activity					1156:1163	glycogen synthase activity	1138:1163	glycogen synthase activity	1138:1163	O-GlcNAcylation of glycogen synthase is significantly increased with glucose deprivation, and this O-GlcNAc increase contributes to a 60% decrease (p = 0.004) in glycogen synthase activity.
18174169	2	50	theme	broad	324:328	arg1	range					330:334	a broad range	322:334	a broad range of glucose concentrations	322:360	Here we report on regulation of O-GlcNAcylation over a broad range of glucose concentrations.
18174169	5	51	theme	glucose	847:853	arg1	treatment					886:894	high glucose (20 mm) or glucosamine (10 mm) treatment	842:894	high glucose (20 mm) or glucosamine (10 mm) treatment	842:894	Some of the targets of glucose deprivation-induced O-GlcNAcylation are distinct from those modified in response to high glucose (20 mm) or glucosamine (10 mm) treatment, suggesting differential targeting with glucose deprivation and glucose excess.
18174169	10	52	theme	protein	1616:1622	arg1	p					1632:1632	p = 0.03	1632:1639	p = 0.03	1632:1639	In addition, 12-h glucose deprivation leads to a 49% decrease in O-GlcNAcase protein levels (p = 0.03).
18174169	10	52	theme	protein	1616:1622	arg1	levels					1624:1629	O-GlcNAcase protein levels	1604:1629	O-GlcNAcase protein levels (p = 0.03)	1604:1640	In addition, 12-h glucose deprivation leads to a 49% decrease in O-GlcNAcase protein levels (p = 0.03).
18174169	3	53	mod	modification	418:429	arg1	number					444:449	a limited number	434:449	a limited number of proteins	434:461	We have discovered a significant induction of O-GlcNAc modification of a limited number of proteins under conditions of glucose deprivation.
18174169	3	53	mod	modification	418:429	arg3	O-GlcNAc					409:416	O-GlcNAc modification	409:429	O-GlcNAc modification of a limited number of proteins	409:461	We have discovered a significant induction of O-GlcNAc modification of a limited number of proteins under conditions of glucose deprivation.
18174169	2	54	theme	concentrations	347:360	arg1	range					330:334	a broad range	322:334	a broad range of glucose concentrations	322:360	Here we report on regulation of O-GlcNAcylation over a broad range of glucose concentrations.
18174169	1	55	theme	nutrient	241:248	arg1	modification					196:207	a post-translational modification	175:207	a post-translational modification of proteins that functions as a nutrient sensing mechanism	175:266	O-Linked N-acetylglucosamine (O-GlcNAc) is a post-translational modification of proteins that functions as a nutrient sensing mechanism.
18174169	1	55	theme	nutrient	241:248	arg1	mechanism					258:266	a nutrient sensing mechanism	239:266	a nutrient sensing mechanism	239:266	O-Linked N-acetylglucosamine (O-GlcNAc) is a post-translational modification of proteins that functions as a nutrient sensing mechanism.
18174169	6	56	theme	synthase	1004:1011	arg1	O-GlcNAcylation					976:990	O-GlcNAcylation	976:990	O-GlcNAcylation of glycogen synthase	976:1011	O-GlcNAcylation of glycogen synthase is significantly increased with glucose deprivation, and this O-GlcNAc increase contributes to a 60% decrease (p = 0.004) in glycogen synthase activity.
18174169	10	57	theme	=	1634:1634	arg1	p					1632:1632	p = 0.03	1632:1639	p = 0.03	1632:1639	In addition, 12-h glucose deprivation leads to a 49% decrease in O-GlcNAcase protein levels (p = 0.03).
18174169	10	57	theme	=	1634:1634	arg1	levels					1624:1629	O-GlcNAcase protein levels	1604:1629	O-GlcNAcase protein levels (p = 0.03)	1604:1640	In addition, 12-h glucose deprivation leads to a 49% decrease in O-GlcNAcase protein levels (p = 0.03).
18174169	8	58	theme	nucleocytoplasmic	1309:1325	arg1	OGT					1369:1371	OGT	1369:1371	OGT	1369:1371	Rather, the mRNA for nucleocytoplasmic O-linked N-acetylglucosaminyltransferase (OGT) increases 3.4-fold within 6 h of glucose deprivation (p = 0.006).
18174169	8	58	theme	nucleocytoplasmic	1309:1325	arg1	N-acetylglucosaminyltransferase					1336:1366	nucleocytoplasmic O-linked N-acetylglucosaminyltransferase	1309:1366	nucleocytoplasmic O-linked N-acetylglucosaminyltransferase (OGT)	1309:1372	Rather, the mRNA for nucleocytoplasmic O-linked N-acetylglucosaminyltransferase (OGT) increases 3.4-fold within 6 h of glucose deprivation (p = 0.006).
18174169	11	59	theme	glycogen	1851:1858	arg1	synthase					1860:1867	glycogen synthase	1851:1867	glycogen synthase	1851:1867	We conclude that increased O-GlcNAc modification stimulated by glucose deprivation results from increased OGT and decreased O-GlcNAcase levels and that these changes affect cell metabolism, thus inactivating glycogen synthase.
18174169	5	60	theme	glucose	936:942	arg1	deprivation					944:954	glucose deprivation	936:954	glucose deprivation	936:954	Some of the targets of glucose deprivation-induced O-GlcNAcylation are distinct from those modified in response to high glucose (20 mm) or glucosamine (10 mm) treatment, suggesting differential targeting with glucose deprivation and glucose excess.
18174169	9	61	theme	glucose-treated	1516:1530	arg1	cells					1532:1536	normal glucose-treated cells	1509:1536	normal glucose-treated cells	1509:1536	Within 12 h, OGT protein increases 1.7-fold (p = 0.01) compared with normal glucose-treated cells.
18174169	6	62	theme	O-GlcNAc	1075:1082	arg1	increase					1084:1091	this O-GlcNAc increase	1070:1091	this O-GlcNAc increase	1070:1091	O-GlcNAcylation of glycogen synthase is significantly increased with glucose deprivation, and this O-GlcNAc increase contributes to a 60% decrease (p = 0.004) in glycogen synthase activity.
18174169	11	63	theme	O-GlcNAcase	1767:1777	arg1	levels					1779:1784	decreased O-GlcNAcase levels	1757:1784	decreased O-GlcNAcase levels	1757:1784	We conclude that increased O-GlcNAc modification stimulated by glucose deprivation results from increased OGT and decreased O-GlcNAcase levels and that these changes affect cell metabolism, thus inactivating glycogen synthase.
18174169	5	64	from	those	812:816	arg1	distinct					798:805	distinct	798:805	distinct	798:805	Some of the targets of glucose deprivation-induced O-GlcNAcylation are distinct from those modified in response to high glucose (20 mm) or glucosamine (10 mm) treatment, suggesting differential targeting with glucose deprivation and glucose excess.
18174169	9	65	theme	=	1487:1487	arg1	p					1485:1485	p	1485:1485	p = 0.01	1485:1492	Within 12 h, OGT protein increases 1.7-fold (p = 0.01) compared with normal glucose-treated cells.
18174169	1	66	theme	post-translational	177:194	arg1	modification					196:207	a post-translational modification	175:207	a post-translational modification of proteins that functions as a nutrient sensing mechanism	175:266	O-Linked N-acetylglucosamine (O-GlcNAc) is a post-translational modification of proteins that functions as a nutrient sensing mechanism.
18174169	1	66	theme	post-translational	177:194	arg1	mechanism					258:266	a nutrient sensing mechanism	239:266	a nutrient sensing mechanism	239:266	O-Linked N-acetylglucosamine (O-GlcNAc) is a post-translational modification of proteins that functions as a nutrient sensing mechanism.
18174169	1	66	theme	post-translational	177:194	arg1	N-acetylglucosamine					141:159	O-Linked N-acetylglucosamine	132:159	O-Linked N-acetylglucosamine (O-GlcNAc)	132:170	O-Linked N-acetylglucosamine (O-GlcNAc) is a post-translational modification of proteins that functions as a nutrient sensing mechanism.
18174169	3	67	theme	significant	384:394	arg1	induction					396:404	a significant induction	382:404	a significant induction of O-GlcNAc modification of a limited number of proteins	382:461	We have discovered a significant induction of O-GlcNAc modification of a limited number of proteins under conditions of glucose deprivation.
18174169	4	68	theme	carcinoma	574:582	arg1	cells					592:596	glucose-deprived human hepatocellular carcinoma (HepG2) cells	536:596	glucose-deprived human hepatocellular carcinoma (HepG2) cells	536:596	Beginning 12 h after treatment, glucose-deprived human hepatocellular carcinoma (HepG2) cells demonstrate a 7.8-fold increase in total O-GlcNAc modification compared with cells cultured in normal glucose (5 mm; p = 0.008).
18174169	0	69	theme	N-acetylglucosaminyltransferase	99:129	arg1	up-regulation					73:85	up-regulation	73:85	up-regulation of O-linked N-acetylglucosaminyltransferase	73:129	Glucose deprivation stimulates O-GlcNAc modification of proteins through up-regulation of O-linked N-acetylglucosaminyltransferase.
18174169	4	70	theme	HepG2	585:589	arg1	cells					592:596	glucose-deprived human hepatocellular carcinoma (HepG2) cells	536:596	glucose-deprived human hepatocellular carcinoma (HepG2) cells	536:596	Beginning 12 h after treatment, glucose-deprived human hepatocellular carcinoma (HepG2) cells demonstrate a 7.8-fold increase in total O-GlcNAc modification compared with cells cultured in normal glucose (5 mm; p = 0.008).
18174169	5	71	theme	deprivation-induced	758:776	arg1	O-GlcNAcylation					778:792	glucose deprivation-induced O-GlcNAcylation	750:792	glucose deprivation-induced O-GlcNAcylation	750:792	Some of the targets of glucose deprivation-induced O-GlcNAcylation are distinct from those modified in response to high glucose (20 mm) or glucosamine (10 mm) treatment, suggesting differential targeting with glucose deprivation and glucose excess.
18174169	3	72	theme	modification	418:429	arg1	induction					396:404	a significant induction	382:404	a significant induction of O-GlcNAc modification of a limited number of proteins	382:461	We have discovered a significant induction of O-GlcNAc modification of a limited number of proteins under conditions of glucose deprivation.
18174169	7	73	theme	increased	1217:1225	arg1	substrate					1257:1265	the rate-limiting substrate	1239:1265	the rate-limiting substrate for O-GlcNAcylation	1239:1285	Increased O-GlcNAc modification is not mediated by increased UDP-GlcNAc, the rate-limiting substrate for O-GlcNAcylation.
18174169	7	73	theme	increased	1217:1225	arg1	UDP-GlcNAc					1227:1236	increased UDP-GlcNAc	1217:1236	increased UDP-GlcNAc	1217:1236	Increased O-GlcNAc modification is not mediated by increased UDP-GlcNAc, the rate-limiting substrate for O-GlcNAcylation.
18174169	1	74	theme	sensing	250:256	arg1	modification					196:207	a post-translational modification	175:207	a post-translational modification of proteins that functions as a nutrient sensing mechanism	175:266	O-Linked N-acetylglucosamine (O-GlcNAc) is a post-translational modification of proteins that functions as a nutrient sensing mechanism.
18174169	1	74	theme	sensing	250:256	arg1	mechanism					258:266	a nutrient sensing mechanism	239:266	a nutrient sensing mechanism	239:266	O-Linked N-acetylglucosamine (O-GlcNAc) is a post-translational modification of proteins that functions as a nutrient sensing mechanism.
18174169	4	75	theme	human	553:557	arg1	cells					592:596	glucose-deprived human hepatocellular carcinoma (HepG2) cells	536:596	glucose-deprived human hepatocellular carcinoma (HepG2) cells	536:596	Beginning 12 h after treatment, glucose-deprived human hepatocellular carcinoma (HepG2) cells demonstrate a 7.8-fold increase in total O-GlcNAc modification compared with cells cultured in normal glucose (5 mm; p = 0.008).
18174169	8	76	theme	glucose	1407:1413	arg1	p					1428:1428	p = 0.006	1428:1436	p = 0.006	1428:1436	Rather, the mRNA for nucleocytoplasmic O-linked N-acetylglucosaminyltransferase (OGT) increases 3.4-fold within 6 h of glucose deprivation (p = 0.006).
18174169	8	76	theme	glucose	1407:1413	arg1	deprivation					1415:1425	glucose deprivation	1407:1425	glucose deprivation (p = 0.006)	1407:1437	Rather, the mRNA for nucleocytoplasmic O-linked N-acetylglucosaminyltransferase (OGT) increases 3.4-fold within 6 h of glucose deprivation (p = 0.006).
18174169	6	77	theme	%	1112:1112	arg1	0.004					1128:1132	p = 0.004	1124:1132	p = 0.004	1124:1132	O-GlcNAcylation of glycogen synthase is significantly increased with glucose deprivation, and this O-GlcNAc increase contributes to a 60% decrease (p = 0.004) in glycogen synthase activity.
18174169	6	77	theme	%	1112:1112	arg1	decrease					1114:1121	a 60% decrease	1108:1121	a 60% decrease (p = 0.004) in glycogen synthase activity	1108:1163	O-GlcNAcylation of glycogen synthase is significantly increased with glucose deprivation, and this O-GlcNAc increase contributes to a 60% decrease (p = 0.004) in glycogen synthase activity.
18174169	3	78	theme	number	444:449	arg1	modification					418:429	O-GlcNAc modification	409:429	O-GlcNAc modification of a limited number of proteins	409:461	We have discovered a significant induction of O-GlcNAc modification of a limited number of proteins under conditions of glucose deprivation.
18174169	3	79	theme	glucose	483:489	arg1	deprivation					491:501	glucose deprivation	483:501	glucose deprivation	483:501	We have discovered a significant induction of O-GlcNAc modification of a limited number of proteins under conditions of glucose deprivation.
18174169	0	80	theme	O-GlcNAc	31:38	arg1	modification					40:51	O-GlcNAc modification	31:51	O-GlcNAc modification of proteins	31:63	Glucose deprivation stimulates O-GlcNAc modification of proteins through up-regulation of O-linked N-acetylglucosaminyltransferase.
18174169	4	81	theme	total	633:637	arg1	modification					648:659	total O-GlcNAc modification	633:659	total O-GlcNAc modification	633:659	Beginning 12 h after treatment, glucose-deprived human hepatocellular carcinoma (HepG2) cells demonstrate a 7.8-fold increase in total O-GlcNAc modification compared with cells cultured in normal glucose (5 mm; p = 0.008).
18174169	8	82	theme	=	1430:1430	arg1	p					1428:1428	p = 0.006	1428:1436	p = 0.006	1428:1436	Rather, the mRNA for nucleocytoplasmic O-linked N-acetylglucosaminyltransferase (OGT) increases 3.4-fold within 6 h of glucose deprivation (p = 0.006).
18174169	8	82	theme	=	1430:1430	arg1	deprivation					1415:1425	glucose deprivation	1407:1425	glucose deprivation (p = 0.006)	1407:1437	Rather, the mRNA for nucleocytoplasmic O-linked N-acetylglucosaminyltransferase (OGT) increases 3.4-fold within 6 h of glucose deprivation (p = 0.006).
18174169	7	83	theme	O-GlcNAc	1176:1183	arg1	modification					1185:1196	Increased O-GlcNAc modification	1166:1196	Increased O-GlcNAc modification	1166:1196	Increased O-GlcNAc modification is not mediated by increased UDP-GlcNAc, the rate-limiting substrate for O-GlcNAcylation.
18174169	5	84	theme	high	842:845	arg1	glucose					847:853	high glucose	842:853	high glucose (20 mm)	842:861	Some of the targets of glucose deprivation-induced O-GlcNAcylation are distinct from those modified in response to high glucose (20 mm) or glucosamine (10 mm) treatment, suggesting differential targeting with glucose deprivation and glucose excess.
18174169	5	84	theme	high	842:845	arg1	mm					859:860	20 mm	856:860	20 mm	856:860	Some of the targets of glucose deprivation-induced O-GlcNAcylation are distinct from those modified in response to high glucose (20 mm) or glucosamine (10 mm) treatment, suggesting differential targeting with glucose deprivation and glucose excess.
18174169	0	85	link	O-linked	90:97	arg1	N-acetylglucosaminyltransferase					99:129	O-linked N-acetylglucosaminyltransferase	90:129	O-linked N-acetylglucosaminyltransferase	90:129	Glucose deprivation stimulates O-GlcNAc modification of proteins through up-regulation of O-linked N-acetylglucosaminyltransferase.
18174169	3	86	theme	proteins	454:461	arg1	number					444:449	a limited number	434:449	a limited number of proteins	434:461	We have discovered a significant induction of O-GlcNAc modification of a limited number of proteins under conditions of glucose deprivation.
18174169	9	87	dep	1.7-fold	1475:1482	arg1	p					1485:1485	p	1485:1485	p = 0.01	1485:1492	Within 12 h, OGT protein increases 1.7-fold (p = 0.01) compared with normal glucose-treated cells.
18174169	6	88	theme	glycogen	1138:1145	arg1	activity					1156:1163	glycogen synthase activity	1138:1163	glycogen synthase activity	1138:1163	O-GlcNAcylation of glycogen synthase is significantly increased with glucose deprivation, and this O-GlcNAc increase contributes to a 60% decrease (p = 0.004) in glycogen synthase activity.
18174169	4	89	theme	normal	693:698	arg1	glucose					700:706	normal glucose	693:706	normal glucose	693:706	Beginning 12 h after treatment, glucose-deprived human hepatocellular carcinoma (HepG2) cells demonstrate a 7.8-fold increase in total O-GlcNAc modification compared with cells cultured in normal glucose (5 mm; p = 0.008).
19933273	8	0	from	sensor	1545:1550	arg1	lipid					1555:1559	lipid	1555:1559	lipid	1555:1559	Altogether, our results suggest that O-GlcNAcylation of LXR is a novel mechanism by which LXR acts as a glucose sensor affecting LXR-dependent gene expression, substantiating the crucial role of LXR as a nutritional sensor in lipid and glucose metabolism.
19933273	8	0	from	sensor	1545:1550	arg1	metabolism					1573:1582	glucose metabolism	1565:1582	glucose metabolism	1565:1582	Altogether, our results suggest that O-GlcNAcylation of LXR is a novel mechanism by which LXR acts as a glucose sensor affecting LXR-dependent gene expression, substantiating the crucial role of LXR as a nutritional sensor in lipid and glucose metabolism.
19933273	7	1	theme	activity	1227:1234	arg1	activation					1193:1202	LXR/retinoic acid receptor-dependent activation	1156:1202	LXR/retinoic acid receptor-dependent activation of luciferase reporter activity driven by the mouse SREBP-1c promoter via the hexosamine biosynthetic pathway in Huh7 cells	1156:1326	Furthermore, glucose increased LXR/retinoic acid receptor-dependent activation of luciferase reporter activity driven by the mouse SREBP-1c promoter via the hexosamine biosynthetic pathway in Huh7 cells.
19933273	3	2	theme	gene	535:538	arg1	specificity					540:550	target gene specificity	528:550	target gene specificity	528:550	LXRs are shown to be post-translationally modified by phosphorylation, acetylation, and sumoylation, affecting their target gene specificity, stability, and transactivating and transrepressional activity, respectively.
19933273	8	3	theme	nutritional	1533:1543	arg1	role					1516:1519	the crucial role	1504:1519	the crucial role of LXR	1504:1526	Altogether, our results suggest that O-GlcNAcylation of LXR is a novel mechanism by which LXR acts as a glucose sensor affecting LXR-dependent gene expression, substantiating the crucial role of LXR as a nutritional sensor in lipid and glucose metabolism.
19933273	8	3	theme	nutritional	1533:1543	arg1	sensor					1545:1550	a nutritional sensor	1531:1550	a nutritional sensor in lipid and glucose metabolism	1531:1582	Altogether, our results suggest that O-GlcNAcylation of LXR is a novel mechanism by which LXR acts as a glucose sensor affecting LXR-dependent gene expression, substantiating the crucial role of LXR as a nutritional sensor in lipid and glucose metabolism.
19933273	5	4	theme	increased	816:824	arg1	O-GlcNAcylation					843:857	increased hepatic LXRalpha O-GlcNAcylation	816:857	increased hepatic LXRalpha O-GlcNAcylation	816:857	Furthermore, we observed increased hepatic LXRalpha O-GlcNAcylation in vivo in refed mice and in streptozotocin-induced refed diabetic mice.
19933273	2	5	theme	glucose	372:378	arg1	homeostasis					380:390	glucose homeostasis	372:390	glucose homeostasis	372:390	The liver X receptors (LXRs) function as nutritional sensors for cholesterol-regulating lipid metabolism, glucose homeostasis, and inflammation.
19933273	2	6	theme	lipid	354:358	arg1	metabolism					360:369	cholesterol-regulating lipid metabolism	331:369	cholesterol-regulating lipid metabolism	331:369	The liver X receptors (LXRs) function as nutritional sensors for cholesterol-regulating lipid metabolism, glucose homeostasis, and inflammation.
19933273	6	7	from	induction	945:953	arg1	models					997:1002	both mouse models	986:1002	both mouse models	986:1002	Importantly, induction of LXRalpha O-GlcNAcylation in both mouse models was concomitant with increased expression of the lipogenic gene SREBP-1c (sterol regulatory element-binding protein 1c).
19933273	6	8	theme	O-GlcNAcylation	967:981	arg1	induction					945:953	induction	945:953	induction of LXRalpha O-GlcNAcylation in both mouse models	945:1002	Importantly, induction of LXRalpha O-GlcNAcylation in both mouse models was concomitant with increased expression of the lipogenic gene SREBP-1c (sterol regulatory element-binding protein 1c).
19933273	7	9	theme	luciferase	1207:1216	arg1	activity					1227:1234	luciferase reporter activity	1207:1234	luciferase reporter activity	1207:1234	Furthermore, glucose increased LXR/retinoic acid receptor-dependent activation of luciferase reporter activity driven by the mouse SREBP-1c promoter via the hexosamine biosynthetic pathway in Huh7 cells.
19933273	8	10	theme	glucose	1433:1439	arg1	sensor					1441:1446	a glucose sensor	1431:1446	a glucose sensor affecting LXR-dependent gene expression	1431:1486	Altogether, our results suggest that O-GlcNAcylation of LXR is a novel mechanism by which LXR acts as a glucose sensor affecting LXR-dependent gene expression, substantiating the crucial role of LXR as a nutritional sensor in lipid and glucose metabolism.
19933273	8	10	theme	glucose	1433:1439	arg1	LXR					1419:1421	LXR	1419:1421	LXR	1419:1421	Altogether, our results suggest that O-GlcNAcylation of LXR is a novel mechanism by which LXR acts as a glucose sensor affecting LXR-dependent gene expression, substantiating the crucial role of LXR as a nutritional sensor in lipid and glucose metabolism.
19933273	6	11	with	concomitant	1008:1018	arg1	expression					1035:1044	increased expression	1025:1044	increased expression of the lipogenic gene SREBP-1c (sterol regulatory element-binding protein 1c)	1025:1122	Importantly, induction of LXRalpha O-GlcNAcylation in both mouse models was concomitant with increased expression of the lipogenic gene SREBP-1c (sterol regulatory element-binding protein 1c).
19933273	4	12	theme	present	637:643	arg1	study					645:649	the present study	633:649	the present study	633:649	In the present study, we show for the first time that LXRalpha and LXRbeta are targets for glucose-hexosamine-derived O-GlcNAc modification in human Huh7 cells.
19933273	4	13	link	glucose-hexosamine-derived	721:746	arg1	modification					757:768	glucose-hexosamine-derived O-GlcNAc modification	721:768	glucose-hexosamine-derived O-GlcNAc modification in human Huh7 cells	721:788	In the present study, we show for the first time that LXRalpha and LXRbeta are targets for glucose-hexosamine-derived O-GlcNAc modification in human Huh7 cells.
19933273	6	14	theme	LXRalpha	958:965	arg1	O-GlcNAcylation					967:981	LXRalpha O-GlcNAcylation	958:981	LXRalpha O-GlcNAcylation	958:981	Importantly, induction of LXRalpha O-GlcNAcylation in both mouse models was concomitant with increased expression of the lipogenic gene SREBP-1c (sterol regulatory element-binding protein 1c).
19933273	7	15	theme	reporter	1218:1225	arg1	activity					1227:1234	luciferase reporter activity	1207:1234	luciferase reporter activity	1207:1234	Furthermore, glucose increased LXR/retinoic acid receptor-dependent activation of luciferase reporter activity driven by the mouse SREBP-1c promoter via the hexosamine biosynthetic pathway in Huh7 cells.
19933273	4	16	theme	glucose-hexosamine-derived	721:746	arg1	modification					757:768	glucose-hexosamine-derived O-GlcNAc modification	721:768	glucose-hexosamine-derived O-GlcNAc modification in human Huh7 cells	721:788	In the present study, we show for the first time that LXRalpha and LXRbeta are targets for glucose-hexosamine-derived O-GlcNAc modification in human Huh7 cells.
19933273	6	17	theme	lipogenic	1053:1061	arg1	SREBP-1c					1068:1075	the lipogenic gene SREBP-1c	1049:1075	the lipogenic gene SREBP-1c (sterol regulatory element-binding protein 1c)	1049:1122	Importantly, induction of LXRalpha O-GlcNAcylation in both mouse models was concomitant with increased expression of the lipogenic gene SREBP-1c (sterol regulatory element-binding protein 1c).
19933273	6	17	theme	lipogenic	1053:1061	arg1	protein					1112:1118	sterol regulatory element-binding protein 1c	1078:1121	sterol regulatory element-binding protein 1c	1078:1121	Importantly, induction of LXRalpha O-GlcNAcylation in both mouse models was concomitant with increased expression of the lipogenic gene SREBP-1c (sterol regulatory element-binding protein 1c).
19933273	7	18	theme	biosynthetic	1293:1304	arg1	pathway					1306:1312	the hexosamine biosynthetic pathway	1278:1312	the hexosamine biosynthetic pathway in Huh7 cells	1278:1326	Furthermore, glucose increased LXR/retinoic acid receptor-dependent activation of luciferase reporter activity driven by the mouse SREBP-1c promoter via the hexosamine biosynthetic pathway in Huh7 cells.
19933273	0	19	from	O-GlcNAc-modified	37:53	arg1	response					58:65	response	58:65	response to glucose	58:76	Nuclear receptor liver X receptor is O-GlcNAc-modified in response to glucose.
19933273	5	20	theme	diabetic	917:924	arg1	mice					926:929	streptozotocin-induced refed diabetic mice	888:929	streptozotocin-induced refed diabetic mice	888:929	Furthermore, we observed increased hepatic LXRalpha O-GlcNAcylation in vivo in refed mice and in streptozotocin-induced refed diabetic mice.
19933273	7	21	theme	mouse	1250:1254	arg1	promoter					1265:1272	the mouse SREBP-1c promoter	1246:1272	the mouse SREBP-1c promoter	1246:1272	Furthermore, glucose increased LXR/retinoic acid receptor-dependent activation of luciferase reporter activity driven by the mouse SREBP-1c promoter via the hexosamine biosynthetic pathway in Huh7 cells.
19933273	6	22	theme	element-binding	1096:1110	arg1	SREBP-1c					1068:1075	the lipogenic gene SREBP-1c	1049:1075	the lipogenic gene SREBP-1c (sterol regulatory element-binding protein 1c)	1049:1122	Importantly, induction of LXRalpha O-GlcNAcylation in both mouse models was concomitant with increased expression of the lipogenic gene SREBP-1c (sterol regulatory element-binding protein 1c).
19933273	6	22	theme	element-binding	1096:1110	arg1	protein					1112:1118	sterol regulatory element-binding protein 1c	1078:1121	sterol regulatory element-binding protein 1c	1078:1121	Importantly, induction of LXRalpha O-GlcNAcylation in both mouse models was concomitant with increased expression of the lipogenic gene SREBP-1c (sterol regulatory element-binding protein 1c).
19933273	8	23	theme	LXR	1385:1387	arg1	mechanism					1400:1408	a novel mechanism	1392:1408	a novel mechanism by which LXR acts as a glucose sensor affecting LXR-dependent gene expression, substantiating the crucial role of LXR as a nutritional sensor in lipid and glucose metabolism	1392:1582	Altogether, our results suggest that O-GlcNAcylation of LXR is a novel mechanism by which LXR acts as a glucose sensor affecting LXR-dependent gene expression, substantiating the crucial role of LXR as a nutritional sensor in lipid and glucose metabolism.
19933273	8	23	theme	LXR	1385:1387	arg1	O-GlcNAcylation					1366:1380	O-GlcNAcylation	1366:1380	O-GlcNAcylation of LXR	1366:1387	Altogether, our results suggest that O-GlcNAcylation of LXR is a novel mechanism by which LXR acts as a glucose sensor affecting LXR-dependent gene expression, substantiating the crucial role of LXR as a nutritional sensor in lipid and glucose metabolism.
19933273	0	24	theme	receptor	8:15	arg1	receptor					25:32	Nuclear receptor liver X receptor	0:32	Nuclear receptor liver X receptor	0:32	Nuclear receptor liver X receptor is O-GlcNAc-modified in response to glucose.
19933273	6	25	theme	increased	1025:1033	arg1	expression					1035:1044	increased expression	1025:1044	increased expression of the lipogenic gene SREBP-1c (sterol regulatory element-binding protein 1c)	1025:1122	Importantly, induction of LXRalpha O-GlcNAcylation in both mouse models was concomitant with increased expression of the lipogenic gene SREBP-1c (sterol regulatory element-binding protein 1c).
19933273	7	26	theme	acid	1169:1172	arg1	activation					1193:1202	LXR/retinoic acid receptor-dependent activation	1156:1202	LXR/retinoic acid receptor-dependent activation of luciferase reporter activity driven by the mouse SREBP-1c promoter via the hexosamine biosynthetic pathway in Huh7 cells	1156:1326	Furthermore, glucose increased LXR/retinoic acid receptor-dependent activation of luciferase reporter activity driven by the mouse SREBP-1c promoter via the hexosamine biosynthetic pathway in Huh7 cells.
19933273	1	27	theme	Post-translational	79:96	arg1	modification					98:109	Post-translational modification	79:109	Post-translational modification of nucleocytoplasmic proteins by O-linked beta-N-acetylglucosamine (O-GlcNAc)	79:187	Post-translational modification of nucleocytoplasmic proteins by O-linked beta-N-acetylglucosamine (O-GlcNAc) has for the last 25 years emerged as an essential glucose-sensing mechanism.
19933273	1	28	theme	last	201:204	arg1	years					209:213	the last 25 years	197:213	the last 25 years emerged as an essential glucose-sensing mechanism	197:263	Post-translational modification of nucleocytoplasmic proteins by O-linked beta-N-acetylglucosamine (O-GlcNAc) has for the last 25 years emerged as an essential glucose-sensing mechanism.
19933273	0	29	theme	Nuclear	0:6	arg1	receptor					25:32	Nuclear receptor liver X receptor	0:32	Nuclear receptor liver X receptor	0:32	Nuclear receptor liver X receptor is O-GlcNAc-modified in response to glucose.
19933273	7	30	theme	SREBP-1c	1256:1263	arg1	promoter					1265:1272	the mouse SREBP-1c promoter	1246:1272	the mouse SREBP-1c promoter	1246:1272	Furthermore, glucose increased LXR/retinoic acid receptor-dependent activation of luciferase reporter activity driven by the mouse SREBP-1c promoter via the hexosamine biosynthetic pathway in Huh7 cells.
19933273	7	31	theme	receptor-dependent	1174:1191	arg1	activation					1193:1202	LXR/retinoic acid receptor-dependent activation	1156:1202	LXR/retinoic acid receptor-dependent activation of luciferase reporter activity driven by the mouse SREBP-1c promoter via the hexosamine biosynthetic pathway in Huh7 cells	1156:1326	Furthermore, glucose increased LXR/retinoic acid receptor-dependent activation of luciferase reporter activity driven by the mouse SREBP-1c promoter via the hexosamine biosynthetic pathway in Huh7 cells.
19933273	4	32	theme	Huh7	779:782	arg1	cells					784:788	human Huh7 cells	773:788	human Huh7 cells	773:788	In the present study, we show for the first time that LXRalpha and LXRbeta are targets for glucose-hexosamine-derived O-GlcNAc modification in human Huh7 cells.
19933273	7	33	from	pathway	1306:1312	arg1	cells					1322:1326	Huh7 cells	1317:1326	Huh7 cells	1317:1326	Furthermore, glucose increased LXR/retinoic acid receptor-dependent activation of luciferase reporter activity driven by the mouse SREBP-1c promoter via the hexosamine biosynthetic pathway in Huh7 cells.
19933273	0	34	theme	X	23:23	arg1	receptor					25:32	Nuclear receptor liver X receptor	0:32	Nuclear receptor liver X receptor	0:32	Nuclear receptor liver X receptor is O-GlcNAc-modified in response to glucose.
19933273	2	35	theme	nutritional	307:317	arg1	sensors					319:325	nutritional sensors	307:325	nutritional sensors for cholesterol-regulating lipid metabolism, glucose homeostasis, and inflammation	307:408	The liver X receptors (LXRs) function as nutritional sensors for cholesterol-regulating lipid metabolism, glucose homeostasis, and inflammation.
19933273	2	35	theme	nutritional	307:317	arg1	receptors					278:286	The liver X receptors	266:286	The liver X receptors (LXRs)	266:293	The liver X receptors (LXRs) function as nutritional sensors for cholesterol-regulating lipid metabolism, glucose homeostasis, and inflammation.
19933273	0	36	theme	liver	17:21	arg1	receptor					25:32	Nuclear receptor liver X receptor	0:32	Nuclear receptor liver X receptor	0:32	Nuclear receptor liver X receptor is O-GlcNAc-modified in response to glucose.
19933273	7	37	theme	LXR/retinoic	1156:1167	arg1	activation					1193:1202	LXR/retinoic acid receptor-dependent activation	1156:1202	LXR/retinoic acid receptor-dependent activation of luciferase reporter activity driven by the mouse SREBP-1c promoter via the hexosamine biosynthetic pathway in Huh7 cells	1156:1326	Furthermore, glucose increased LXR/retinoic acid receptor-dependent activation of luciferase reporter activity driven by the mouse SREBP-1c promoter via the hexosamine biosynthetic pathway in Huh7 cells.
19933273	1	38	theme	nucleocytoplasmic	114:130	arg1	proteins					132:139	nucleocytoplasmic proteins	114:139	nucleocytoplasmic proteins	114:139	Post-translational modification of nucleocytoplasmic proteins by O-linked beta-N-acetylglucosamine (O-GlcNAc) has for the last 25 years emerged as an essential glucose-sensing mechanism.
19933273	8	39	theme	gene	1472:1475	arg1	expression					1477:1486	LXR-dependent gene expression	1458:1486	LXR-dependent gene expression	1458:1486	Altogether, our results suggest that O-GlcNAcylation of LXR is a novel mechanism by which LXR acts as a glucose sensor affecting LXR-dependent gene expression, substantiating the crucial role of LXR as a nutritional sensor in lipid and glucose metabolism.
19933273	5	40	theme	hepatic	826:832	arg1	O-GlcNAcylation					843:857	increased hepatic LXRalpha O-GlcNAcylation	816:857	increased hepatic LXRalpha O-GlcNAcylation	816:857	Furthermore, we observed increased hepatic LXRalpha O-GlcNAcylation in vivo in refed mice and in streptozotocin-induced refed diabetic mice.
19933273	4	41	theme	O-GlcNAc	748:755	arg1	modification					757:768	glucose-hexosamine-derived O-GlcNAc modification	721:768	glucose-hexosamine-derived O-GlcNAc modification in human Huh7 cells	721:788	In the present study, we show for the first time that LXRalpha and LXRbeta are targets for glucose-hexosamine-derived O-GlcNAc modification in human Huh7 cells.
19933273	7	42	theme	hexosamine	1282:1291	arg1	pathway					1306:1312	the hexosamine biosynthetic pathway	1278:1312	the hexosamine biosynthetic pathway in Huh7 cells	1278:1326	Furthermore, glucose increased LXR/retinoic acid receptor-dependent activation of luciferase reporter activity driven by the mouse SREBP-1c promoter via the hexosamine biosynthetic pathway in Huh7 cells.
19933273	5	43	theme	streptozotocin-induced	888:909	arg1	mice					926:929	streptozotocin-induced refed diabetic mice	888:929	streptozotocin-induced refed diabetic mice	888:929	Furthermore, we observed increased hepatic LXRalpha O-GlcNAcylation in vivo in refed mice and in streptozotocin-induced refed diabetic mice.
19933273	5	44	theme	LXRalpha	834:841	arg1	O-GlcNAcylation					843:857	increased hepatic LXRalpha O-GlcNAcylation	816:857	increased hepatic LXRalpha O-GlcNAcylation	816:857	Furthermore, we observed increased hepatic LXRalpha O-GlcNAcylation in vivo in refed mice and in streptozotocin-induced refed diabetic mice.
19933273	6	45	theme	SREBP-1c	1068:1075	arg1	expression					1035:1044	increased expression	1025:1044	increased expression of the lipogenic gene SREBP-1c (sterol regulatory element-binding protein 1c)	1025:1122	Importantly, induction of LXRalpha O-GlcNAcylation in both mouse models was concomitant with increased expression of the lipogenic gene SREBP-1c (sterol regulatory element-binding protein 1c).
19933273	5	46	theme	refed	870:874	arg1	mice					876:879	refed mice	870:879	refed mice	870:879	Furthermore, we observed increased hepatic LXRalpha O-GlcNAcylation in vivo in refed mice and in streptozotocin-induced refed diabetic mice.
19933273	4	47	theme	first	668:672	arg1	time					674:677	the first time	664:677	the first time	664:677	In the present study, we show for the first time that LXRalpha and LXRbeta are targets for glucose-hexosamine-derived O-GlcNAc modification in human Huh7 cells.
19933273	8	48	theme	novel	1394:1398	arg1	mechanism					1400:1408	a novel mechanism	1392:1408	a novel mechanism by which LXR acts as a glucose sensor affecting LXR-dependent gene expression, substantiating the crucial role of LXR as a nutritional sensor in lipid and glucose metabolism	1392:1582	Altogether, our results suggest that O-GlcNAcylation of LXR is a novel mechanism by which LXR acts as a glucose sensor affecting LXR-dependent gene expression, substantiating the crucial role of LXR as a nutritional sensor in lipid and glucose metabolism.
19933273	8	48	theme	novel	1394:1398	arg1	O-GlcNAcylation					1366:1380	O-GlcNAcylation	1366:1380	O-GlcNAcylation of LXR	1366:1387	Altogether, our results suggest that O-GlcNAcylation of LXR is a novel mechanism by which LXR acts as a glucose sensor affecting LXR-dependent gene expression, substantiating the crucial role of LXR as a nutritional sensor in lipid and glucose metabolism.
19933273	1	49	link	O-linked	144:151	arg1	O-GlcNAc					179:186	O-GlcNAc	179:186	O-GlcNAc	179:186	Post-translational modification of nucleocytoplasmic proteins by O-linked beta-N-acetylglucosamine (O-GlcNAc) has for the last 25 years emerged as an essential glucose-sensing mechanism.
19933273	1	49	link	O-linked	144:151	arg1	beta-N-acetylglucosamine					153:176	O-linked beta-N-acetylglucosamine	144:176	O-linked beta-N-acetylglucosamine (O-GlcNAc)	144:187	Post-translational modification of nucleocytoplasmic proteins by O-linked beta-N-acetylglucosamine (O-GlcNAc) has for the last 25 years emerged as an essential glucose-sensing mechanism.
19933273	0	50	from	response	58:65	arg1	O-GlcNAc-modified					37:53	O-GlcNAc-modified	37:53	O-GlcNAc-modified	37:53	Nuclear receptor liver X receptor is O-GlcNAc-modified in response to glucose.
19933273	8	51	theme	LXR-dependent	1458:1470	arg1	expression					1477:1486	LXR-dependent gene expression	1458:1486	LXR-dependent gene expression	1458:1486	Altogether, our results suggest that O-GlcNAcylation of LXR is a novel mechanism by which LXR acts as a glucose sensor affecting LXR-dependent gene expression, substantiating the crucial role of LXR as a nutritional sensor in lipid and glucose metabolism.
19933273	1	52	theme	proteins	132:139	arg1	modification					98:109	Post-translational modification	79:109	Post-translational modification of nucleocytoplasmic proteins by O-linked beta-N-acetylglucosamine (O-GlcNAc)	79:187	Post-translational modification of nucleocytoplasmic proteins by O-linked beta-N-acetylglucosamine (O-GlcNAc) has for the last 25 years emerged as an essential glucose-sensing mechanism.
19933273	8	53	theme	glucose	1565:1571	arg1	metabolism					1573:1582	glucose metabolism	1565:1582	glucose metabolism	1565:1582	Altogether, our results suggest that O-GlcNAcylation of LXR is a novel mechanism by which LXR acts as a glucose sensor affecting LXR-dependent gene expression, substantiating the crucial role of LXR as a nutritional sensor in lipid and glucose metabolism.
19933273	8	54	theme	crucial	1508:1514	arg1	role					1516:1519	the crucial role	1504:1519	the crucial role of LXR	1504:1526	Altogether, our results suggest that O-GlcNAcylation of LXR is a novel mechanism by which LXR acts as a glucose sensor affecting LXR-dependent gene expression, substantiating the crucial role of LXR as a nutritional sensor in lipid and glucose metabolism.
19933273	8	54	theme	crucial	1508:1514	arg1	sensor					1545:1550	a nutritional sensor	1531:1550	a nutritional sensor in lipid and glucose metabolism	1531:1582	Altogether, our results suggest that O-GlcNAcylation of LXR is a novel mechanism by which LXR acts as a glucose sensor affecting LXR-dependent gene expression, substantiating the crucial role of LXR as a nutritional sensor in lipid and glucose metabolism.
19933273	7	55	theme	Huh7	1317:1320	arg1	cells					1322:1326	Huh7 cells	1317:1326	Huh7 cells	1317:1326	Furthermore, glucose increased LXR/retinoic acid receptor-dependent activation of luciferase reporter activity driven by the mouse SREBP-1c promoter via the hexosamine biosynthetic pathway in Huh7 cells.
19933273	3	56	theme	target	528:533	arg1	specificity					540:550	target gene specificity	528:550	target gene specificity	528:550	LXRs are shown to be post-translationally modified by phosphorylation, acetylation, and sumoylation, affecting their target gene specificity, stability, and transactivating and transrepressional activity, respectively.
19933273	4	57	theme	human	773:777	arg1	cells					784:788	human Huh7 cells	773:788	human Huh7 cells	773:788	In the present study, we show for the first time that LXRalpha and LXRbeta are targets for glucose-hexosamine-derived O-GlcNAc modification in human Huh7 cells.
19933273	8	58	theme	LXR	1524:1526	arg1	role					1516:1519	the crucial role	1504:1519	the crucial role of LXR	1504:1526	Altogether, our results suggest that O-GlcNAcylation of LXR is a novel mechanism by which LXR acts as a glucose sensor affecting LXR-dependent gene expression, substantiating the crucial role of LXR as a nutritional sensor in lipid and glucose metabolism.
19933273	8	58	theme	LXR	1524:1526	arg1	sensor					1545:1550	a nutritional sensor	1531:1550	a nutritional sensor in lipid and glucose metabolism	1531:1582	Altogether, our results suggest that O-GlcNAcylation of LXR is a novel mechanism by which LXR acts as a glucose sensor affecting LXR-dependent gene expression, substantiating the crucial role of LXR as a nutritional sensor in lipid and glucose metabolism.
19933273	1	59	theme	O-linked	144:151	arg1	O-GlcNAc					179:186	O-GlcNAc	179:186	O-GlcNAc	179:186	Post-translational modification of nucleocytoplasmic proteins by O-linked beta-N-acetylglucosamine (O-GlcNAc) has for the last 25 years emerged as an essential glucose-sensing mechanism.
19933273	1	59	theme	O-linked	144:151	arg1	beta-N-acetylglucosamine					153:176	O-linked beta-N-acetylglucosamine	144:176	O-linked beta-N-acetylglucosamine (O-GlcNAc)	144:187	Post-translational modification of nucleocytoplasmic proteins by O-linked beta-N-acetylglucosamine (O-GlcNAc) has for the last 25 years emerged as an essential glucose-sensing mechanism.
19933273	3	60	theme	transrepressional	588:604	arg1	activity					606:613	transrepressional activity	588:613	transrepressional activity	588:613	LXRs are shown to be post-translationally modified by phosphorylation, acetylation, and sumoylation, affecting their target gene specificity, stability, and transactivating and transrepressional activity, respectively.
19933273	1	61	theme	essential	229:237	arg1	mechanism					255:263	an essential glucose-sensing mechanism	226:263	an essential glucose-sensing mechanism	226:263	Post-translational modification of nucleocytoplasmic proteins by O-linked beta-N-acetylglucosamine (O-GlcNAc) has for the last 25 years emerged as an essential glucose-sensing mechanism.
19933273	2	62	theme	X	276:276	arg1	sensors					319:325	nutritional sensors	307:325	nutritional sensors for cholesterol-regulating lipid metabolism, glucose homeostasis, and inflammation	307:408	The liver X receptors (LXRs) function as nutritional sensors for cholesterol-regulating lipid metabolism, glucose homeostasis, and inflammation.
19933273	2	62	theme	X	276:276	arg1	LXRs					289:292	LXRs	289:292	LXRs	289:292	The liver X receptors (LXRs) function as nutritional sensors for cholesterol-regulating lipid metabolism, glucose homeostasis, and inflammation.
19933273	2	62	theme	X	276:276	arg1	receptors					278:286	The liver X receptors	266:286	The liver X receptors (LXRs)	266:293	The liver X receptors (LXRs) function as nutritional sensors for cholesterol-regulating lipid metabolism, glucose homeostasis, and inflammation.
19933273	2	63	theme	cholesterol-regulating	331:352	arg1	metabolism					360:369	cholesterol-regulating lipid metabolism	331:369	cholesterol-regulating lipid metabolism	331:369	The liver X receptors (LXRs) function as nutritional sensors for cholesterol-regulating lipid metabolism, glucose homeostasis, and inflammation.
19933273	4	64	from	modification	757:768	arg1	cells					784:788	human Huh7 cells	773:788	human Huh7 cells	773:788	In the present study, we show for the first time that LXRalpha and LXRbeta are targets for glucose-hexosamine-derived O-GlcNAc modification in human Huh7 cells.
19933273	1	65	theme	glucose-sensing	239:253	arg1	mechanism					255:263	an essential glucose-sensing mechanism	226:263	an essential glucose-sensing mechanism	226:263	Post-translational modification of nucleocytoplasmic proteins by O-linked beta-N-acetylglucosamine (O-GlcNAc) has for the last 25 years emerged as an essential glucose-sensing mechanism.
19933273	5	66	theme	refed	911:915	arg1	mice					926:929	streptozotocin-induced refed diabetic mice	888:929	streptozotocin-induced refed diabetic mice	888:929	Furthermore, we observed increased hepatic LXRalpha O-GlcNAcylation in vivo in refed mice and in streptozotocin-induced refed diabetic mice.
19933273	2	67	theme	liver	270:274	arg1	sensors					319:325	nutritional sensors	307:325	nutritional sensors for cholesterol-regulating lipid metabolism, glucose homeostasis, and inflammation	307:408	The liver X receptors (LXRs) function as nutritional sensors for cholesterol-regulating lipid metabolism, glucose homeostasis, and inflammation.
19933273	2	67	theme	liver	270:274	arg1	LXRs					289:292	LXRs	289:292	LXRs	289:292	The liver X receptors (LXRs) function as nutritional sensors for cholesterol-regulating lipid metabolism, glucose homeostasis, and inflammation.
19933273	2	67	theme	liver	270:274	arg1	receptors					278:286	The liver X receptors	266:286	The liver X receptors (LXRs)	266:293	The liver X receptors (LXRs) function as nutritional sensors for cholesterol-regulating lipid metabolism, glucose homeostasis, and inflammation.
19933273	6	68	theme	regulatory	1085:1094	arg1	SREBP-1c					1068:1075	the lipogenic gene SREBP-1c	1049:1075	the lipogenic gene SREBP-1c (sterol regulatory element-binding protein 1c)	1049:1122	Importantly, induction of LXRalpha O-GlcNAcylation in both mouse models was concomitant with increased expression of the lipogenic gene SREBP-1c (sterol regulatory element-binding protein 1c).
19933273	6	68	theme	regulatory	1085:1094	arg1	protein					1112:1118	sterol regulatory element-binding protein 1c	1078:1121	sterol regulatory element-binding protein 1c	1078:1121	Importantly, induction of LXRalpha O-GlcNAcylation in both mouse models was concomitant with increased expression of the lipogenic gene SREBP-1c (sterol regulatory element-binding protein 1c).
19933273	6	69	theme	gene	1063:1066	arg1	SREBP-1c					1068:1075	the lipogenic gene SREBP-1c	1049:1075	the lipogenic gene SREBP-1c (sterol regulatory element-binding protein 1c)	1049:1122	Importantly, induction of LXRalpha O-GlcNAcylation in both mouse models was concomitant with increased expression of the lipogenic gene SREBP-1c (sterol regulatory element-binding protein 1c).
19933273	6	69	theme	gene	1063:1066	arg1	protein					1112:1118	sterol regulatory element-binding protein 1c	1078:1121	sterol regulatory element-binding protein 1c	1078:1121	Importantly, induction of LXRalpha O-GlcNAcylation in both mouse models was concomitant with increased expression of the lipogenic gene SREBP-1c (sterol regulatory element-binding protein 1c).
19933273	6	70	theme	mouse	991:995	arg1	models					997:1002	both mouse models	986:1002	both mouse models	986:1002	Importantly, induction of LXRalpha O-GlcNAcylation in both mouse models was concomitant with increased expression of the lipogenic gene SREBP-1c (sterol regulatory element-binding protein 1c).
19933273	3	71	mod	modified	453:460	arg1	LXRs					411:414	LXRs	411:414	LXRs	411:414	LXRs are shown to be post-translationally modified by phosphorylation, acetylation, and sumoylation, affecting their target gene specificity, stability, and transactivating and transrepressional activity, respectively.
19933273	3	71	mod	modified	453:460	arg3	sumoylation					499:509	sumoylation	499:509	sumoylation	499:509	LXRs are shown to be post-translationally modified by phosphorylation, acetylation, and sumoylation, affecting their target gene specificity, stability, and transactivating and transrepressional activity, respectively.
19933273	3	71	mod	modified	453:460	arg3	phosphorylation					465:479	phosphorylation	465:479	phosphorylation	465:479	LXRs are shown to be post-translationally modified by phosphorylation, acetylation, and sumoylation, affecting their target gene specificity, stability, and transactivating and transrepressional activity, respectively.
19933273	3	71	mod	modified	453:460	arg3	acetylation					482:492	acetylation	482:492	acetylation	482:492	LXRs are shown to be post-translationally modified by phosphorylation, acetylation, and sumoylation, affecting their target gene specificity, stability, and transactivating and transrepressional activity, respectively.
19933273	6	72	theme	sterol	1078:1083	arg1	SREBP-1c					1068:1075	the lipogenic gene SREBP-1c	1049:1075	the lipogenic gene SREBP-1c (sterol regulatory element-binding protein 1c)	1049:1122	Importantly, induction of LXRalpha O-GlcNAcylation in both mouse models was concomitant with increased expression of the lipogenic gene SREBP-1c (sterol regulatory element-binding protein 1c).
19933273	6	72	theme	sterol	1078:1083	arg1	protein					1112:1118	sterol regulatory element-binding protein 1c	1078:1121	sterol regulatory element-binding protein 1c	1078:1121	Importantly, induction of LXRalpha O-GlcNAcylation in both mouse models was concomitant with increased expression of the lipogenic gene SREBP-1c (sterol regulatory element-binding protein 1c).
28455227	0	0	theme	cancer	77:82	arg1	cells					84:88	breast cancer cells	70:88	breast cancer cells	70:88	Suppression of OGT by microRNA24 reduces FOXA1 stability and prevents breast cancer cells invasion.
28455227	2	1	theme	emerging	343:350	arg1	evidences					352:360	emerging evidences	343:360	emerging evidences	343:360	Although there are emerging evidences that OGT plays important roles in breast cancer metastasis, the underlying mechanism is not fully understood.
28455227	10	2	theme	breast	1278:1283	arg1	metastasis					1292:1301	breast cancer metastasis	1278:1301	breast cancer metastasis	1278:1301	These results also indicated that OGT might be a potential target for the diagnosis and therapy of breast cancer metastasis.
28455227	1	3	theme	cytosolic	222:230	arg1	proteins					244:251	cytosolic and nuclear proteins	222:251	cytosolic and nuclear proteins	222:251	O-GlcNAc transferase (OGT) catalyzes the addition of O-GlcNAc to certain serine or threonine residue on a wide variety of cytosolic and nuclear proteins and regulates cellular activities such as signaling and transcription.
28455227	0	4	theme	breast	70:75	arg1	cells					84:88	breast cancer cells	70:88	breast cancer cells	70:88	Suppression of OGT by microRNA24 reduces FOXA1 stability and prevents breast cancer cells invasion.
28455227	10	5	theme	potential	1228:1236	arg1	OGT					1213:1215	OGT	1213:1215	OGT	1213:1215	These results also indicated that OGT might be a potential target for the diagnosis and therapy of breast cancer metastasis.
28455227	10	5	theme	potential	1228:1236	arg1	target					1238:1243	a potential target	1226:1243	a potential target for the diagnosis and therapy of breast cancer metastasis	1226:1301	These results also indicated that OGT might be a potential target for the diagnosis and therapy of breast cancer metastasis.
28455227	8	6	theme	breast	1013:1018	arg1	cells					1027:1031	breast cancer cells	1013:1031	breast cancer cells invasion	1013:1040	Furthermore, our data showed that FOXA1 is subjected to O-GlcNAcylation, which instabilizes FOXA1 protein and promotes breast cancer cells invasion.
28455227	3	7	theme	OGT	525:527	arg1	up-regulation					508:520	up-regulation	508:520	up-regulation of OGT	508:527	In this study, we demonstrated that up-regulation of OGT correlates with breast cancer cells invasion.
28455227	1	8	theme	O-GlcNAc	100:107	arg1	OGT					122:124	OGT	122:124	OGT	122:124	O-GlcNAc transferase (OGT) catalyzes the addition of O-GlcNAc to certain serine or threonine residue on a wide variety of cytosolic and nuclear proteins and regulates cellular activities such as signaling and transcription.
28455227	1	8	theme	O-GlcNAc	100:107	arg1	transferase					109:119	O-GlcNAc transferase	100:119	O-GlcNAc transferase (OGT)	100:125	O-GlcNAc transferase (OGT) catalyzes the addition of O-GlcNAc to certain serine or threonine residue on a wide variety of cytosolic and nuclear proteins and regulates cellular activities such as signaling and transcription.
28455227	1	9	theme	nuclear	236:242	arg1	proteins					244:251	cytosolic and nuclear proteins	222:251	cytosolic and nuclear proteins	222:251	O-GlcNAc transferase (OGT) catalyzes the addition of O-GlcNAc to certain serine or threonine residue on a wide variety of cytosolic and nuclear proteins and regulates cellular activities such as signaling and transcription.
28455227	5	10	theme	microRNA24	715:724	arg1	OGT					674:676	OGT	674:676	OGT	674:676	OGT is further identified as a target of microRNA24 (miR24).
28455227	5	10	theme	microRNA24	715:724	arg1	target					705:710	a target	703:710	a target of microRNA24 (miR24)	703:732	OGT is further identified as a target of microRNA24 (miR24).
28455227	6	11	theme	cells	799:803	arg1	invasion					805:812	cells invasion	799:812	cells invasion	799:812	miR24 down-regulates OGT expression and subsequently suppresses cells invasion.
28455227	7	12	theme	invasion	873:880	arg1	repression					882:891	miR24-mediated invasion repression	858:891	miR24-mediated invasion repression	858:891	Re-expression of OGT significantly rescues miR24-mediated invasion repression.
28455227	1	13	theme	proteins	244:251	arg1	variety					211:217	a wide variety	204:217	a wide variety of cytosolic and nuclear proteins	204:251	O-GlcNAc transferase (OGT) catalyzes the addition of O-GlcNAc to certain serine or threonine residue on a wide variety of cytosolic and nuclear proteins and regulates cellular activities such as signaling and transcription.
28455227	1	13	theme	proteins	244:251	arg1	proteins					244:251	cytosolic and nuclear proteins	222:251	cytosolic and nuclear proteins	222:251	O-GlcNAc transferase (OGT) catalyzes the addition of O-GlcNAc to certain serine or threonine residue on a wide variety of cytosolic and nuclear proteins and regulates cellular activities such as signaling and transcription.
28455227	9	14	theme	breast	1103:1108	arg1	cells					1117:1121	breast cancer cells	1103:1121	breast cancer cells invasion	1103:1130	In conclusion, our results demonstrated that miR24 inhibits breast cancer cells invasion by targeting OGT and reducing FOXA1 stability.
28455227	1	15	theme	O-GlcNAc	153:160	arg1	addition					141:148	the addition	137:148	the addition of O-GlcNAc to certain serine or threonine residue	137:199	O-GlcNAc transferase (OGT) catalyzes the addition of O-GlcNAc to certain serine or threonine residue on a wide variety of cytosolic and nuclear proteins and regulates cellular activities such as signaling and transcription.
28455227	8	16	theme	cells	1027:1031	arg1	invasion					1033:1040	breast cancer cells invasion	1013:1040	breast cancer cells invasion	1013:1040	Furthermore, our data showed that FOXA1 is subjected to O-GlcNAcylation, which instabilizes FOXA1 protein and promotes breast cancer cells invasion.
28455227	4	17	theme	OGT	594:596	arg1	Over-expression					575:589	Over-expression	575:589	Over-expression of OGT	575:596	Over-expression of OGT stimulates cells invasion, while OGT silence exhibits the opposite effects.
28455227	9	18	theme	cancer	1110:1115	arg1	cells					1117:1121	breast cancer cells	1103:1121	breast cancer cells invasion	1103:1130	In conclusion, our results demonstrated that miR24 inhibits breast cancer cells invasion by targeting OGT and reducing FOXA1 stability.
28455227	2	19	theme	important	377:385	arg1	roles					387:391	important roles	377:391	important roles	377:391	Although there are emerging evidences that OGT plays important roles in breast cancer metastasis, the underlying mechanism is not fully understood.
28455227	8	20	theme	cancer	1020:1025	arg1	cells					1027:1031	breast cancer cells	1013:1031	breast cancer cells invasion	1013:1040	Furthermore, our data showed that FOXA1 is subjected to O-GlcNAcylation, which instabilizes FOXA1 protein and promotes breast cancer cells invasion.
28455227	3	21	theme	cancer	552:557	arg1	cells					559:563	breast cancer cells	545:563	breast cancer cells invasion	545:572	In this study, we demonstrated that up-regulation of OGT correlates with breast cancer cells invasion.
28455227	7	22	theme	miR24-mediated	858:871	arg1	repression					882:891	miR24-mediated invasion repression	858:891	miR24-mediated invasion repression	858:891	Re-expression of OGT significantly rescues miR24-mediated invasion repression.
28455227	1	23	theme	certain	165:171	arg1	serine					173:178	certain serine	165:178	certain serine	165:178	O-GlcNAc transferase (OGT) catalyzes the addition of O-GlcNAc to certain serine or threonine residue on a wide variety of cytosolic and nuclear proteins and regulates cellular activities such as signaling and transcription.
28455227	2	24	theme	underlying	426:435	arg1	mechanism					437:445	the underlying mechanism	422:445	the underlying mechanism	422:445	Although there are emerging evidences that OGT plays important roles in breast cancer metastasis, the underlying mechanism is not fully understood.
28455227	3	25	theme	cells	559:563	arg1	invasion					565:572	breast cancer cells invasion	545:572	breast cancer cells invasion	545:572	In this study, we demonstrated that up-regulation of OGT correlates with breast cancer cells invasion.
28455227	7	26	theme	OGT	832:834	arg1	Re-expression					815:827	Re-expression	815:827	Re-expression of OGT	815:834	Re-expression of OGT significantly rescues miR24-mediated invasion repression.
28455227	4	27	theme	opposite	656:663	arg1	effects					665:671	the opposite effects	652:671	the opposite effects	652:671	Over-expression of OGT stimulates cells invasion, while OGT silence exhibits the opposite effects.
28455227	6	28	theme	OGT	756:758	arg1	expression					760:769	OGT expression	756:769	OGT expression	756:769	miR24 down-regulates OGT expression and subsequently suppresses cells invasion.
28455227	0	29	theme	OGT	15:17	arg1	Suppression					0:10	Suppression	0:10	Suppression of OGT by microRNA24	0:31	Suppression of OGT by microRNA24 reduces FOXA1 stability and prevents breast cancer cells invasion.
28455227	1	30	theme	cellular	267:274	arg1	transcription					309:321	transcription	309:321	transcription	309:321	O-GlcNAc transferase (OGT) catalyzes the addition of O-GlcNAc to certain serine or threonine residue on a wide variety of cytosolic and nuclear proteins and regulates cellular activities such as signaling and transcription.
28455227	1	30	theme	cellular	267:274	arg1	activities					276:285	cellular activities	267:285	cellular activities such as signaling and transcription	267:321	O-GlcNAc transferase (OGT) catalyzes the addition of O-GlcNAc to certain serine or threonine residue on a wide variety of cytosolic and nuclear proteins and regulates cellular activities such as signaling and transcription.
28455227	1	30	theme	cellular	267:274	arg1	signaling					295:303	signaling	295:303	signaling	295:303	O-GlcNAc transferase (OGT) catalyzes the addition of O-GlcNAc to certain serine or threonine residue on a wide variety of cytosolic and nuclear proteins and regulates cellular activities such as signaling and transcription.
28455227	3	31	theme	breast	545:550	arg1	cells					559:563	breast cancer cells	545:563	breast cancer cells invasion	545:572	In this study, we demonstrated that up-regulation of OGT correlates with breast cancer cells invasion.
28455227	2	32	theme	cancer	403:408	arg1	metastasis					410:419	breast cancer metastasis	396:419	breast cancer metastasis	396:419	Although there are emerging evidences that OGT plays important roles in breast cancer metastasis, the underlying mechanism is not fully understood.
28455227	2	33	theme	breast	396:401	arg1	metastasis					410:419	breast cancer metastasis	396:419	breast cancer metastasis	396:419	Although there are emerging evidences that OGT plays important roles in breast cancer metastasis, the underlying mechanism is not fully understood.
28455227	9	34	theme	cells	1117:1121	arg1	invasion					1123:1130	breast cancer cells invasion	1103:1130	breast cancer cells invasion	1103:1130	In conclusion, our results demonstrated that miR24 inhibits breast cancer cells invasion by targeting OGT and reducing FOXA1 stability.
28455227	1	35	dep	serine	173:178	arg1	residue					193:199	residue	193:199	residue	193:199	O-GlcNAc transferase (OGT) catalyzes the addition of O-GlcNAc to certain serine or threonine residue on a wide variety of cytosolic and nuclear proteins and regulates cellular activities such as signaling and transcription.
28455227	4	36	theme	OGT	631:633	arg1	silence					635:641	OGT silence	631:641	OGT silence	631:641	Over-expression of OGT stimulates cells invasion, while OGT silence exhibits the opposite effects.
28455227	0	37	theme	FOXA1	41:45	arg1	stability					47:55	FOXA1 stability	41:55	FOXA1 stability	41:55	Suppression of OGT by microRNA24 reduces FOXA1 stability and prevents breast cancer cells invasion.
28455227	9	38	theme	FOXA1	1162:1166	arg1	stability					1168:1176	FOXA1 stability	1162:1176	FOXA1 stability	1162:1176	In conclusion, our results demonstrated that miR24 inhibits breast cancer cells invasion by targeting OGT and reducing FOXA1 stability.
28455227	10	39	dep	diagnosis	1253:1261	arg1	the					1249:1251	the	1249:1251	the	1249:1251	These results also indicated that OGT might be a potential target for the diagnosis and therapy of breast cancer metastasis.
28455227	10	40	theme	metastasis	1292:1301	arg1	diagnosis					1253:1261	diagnosis	1253:1261	diagnosis	1253:1261	These results also indicated that OGT might be a potential target for the diagnosis and therapy of breast cancer metastasis.
28455227	10	40	theme	metastasis	1292:1301	arg1	therapy					1267:1273	therapy	1267:1273	therapy	1267:1273	These results also indicated that OGT might be a potential target for the diagnosis and therapy of breast cancer metastasis.
28455227	1	41	theme	wide	206:209	arg1	variety					211:217	a wide variety	204:217	a wide variety of cytosolic and nuclear proteins	204:251	O-GlcNAc transferase (OGT) catalyzes the addition of O-GlcNAc to certain serine or threonine residue on a wide variety of cytosolic and nuclear proteins and regulates cellular activities such as signaling and transcription.
28455227	1	41	theme	wide	206:209	arg1	proteins					244:251	cytosolic and nuclear proteins	222:251	cytosolic and nuclear proteins	222:251	O-GlcNAc transferase (OGT) catalyzes the addition of O-GlcNAc to certain serine or threonine residue on a wide variety of cytosolic and nuclear proteins and regulates cellular activities such as signaling and transcription.
28455227	8	42	theme	FOXA1	986:990	arg1	protein					992:998	FOXA1 protein	986:998	FOXA1 protein	986:998	Furthermore, our data showed that FOXA1 is subjected to O-GlcNAcylation, which instabilizes FOXA1 protein and promotes breast cancer cells invasion.
28455227	10	43	theme	cancer	1285:1290	arg1	metastasis					1292:1301	breast cancer metastasis	1278:1301	breast cancer metastasis	1278:1301	These results also indicated that OGT might be a potential target for the diagnosis and therapy of breast cancer metastasis.
28455227	4	44	theme	cells	609:613	arg1	invasion					615:622	cells invasion	609:622	cells invasion	609:622	Over-expression of OGT stimulates cells invasion, while OGT silence exhibits the opposite effects.
24120863	1	0	theme	experimental	294:305	arg1	challenge					307:315	a significant experimental challenge	280:315	a significant experimental challenge	280:315	Protein modification by O-linked β-N-acetylglucosamine (O-GlcNAc) is a critical cell signaling modality, but identifying signal-specific O-GlcNAcylation events remains a significant experimental challenge.
24120863	0	1	theme	channel	101:107	arg1	O-GlcNAcylation					44:58	O-GlcNAcylation	44:58	O-GlcNAcylation of mitochondrial voltage-dependent anion channel 2	44:109	A chemical glycoproteomics platform reveals O-GlcNAcylation of mitochondrial voltage-dependent anion channel 2.
24120863	2	2	theme	O-GlcNAcylated	408:421	arg1	proteins					423:430	organelle- and stimulus-specific O-GlcNAcylated proteins	375:430	organelle- and stimulus-specific O-GlcNAcylated proteins	375:430	Here, we describe a method for visualizing and analyzing organelle- and stimulus-specific O-GlcNAcylated proteins and use it to identify the mitochondrial voltage-dependent anion channel 2 (VDAC2) as an O-GlcNAc substrate.
24120863	4	3	theme	wide	856:859	arg1	array					861:865	a wide array	854:865	a wide array of experimental contexts	854:890	More broadly, our method will enable the discovery of signal-specific O-GlcNAcylation events in a wide array of experimental contexts.
24120863	4	4	theme	events	844:849	arg1	discovery					799:807	the discovery	795:807	the discovery of signal-specific O-GlcNAcylation events in a wide array of experimental contexts	795:890	More broadly, our method will enable the discovery of signal-specific O-GlcNAcylation events in a wide array of experimental contexts.
24120863	4	5	theme	O-GlcNAcylation	828:842	arg1	events					844:849	signal-specific O-GlcNAcylation events	812:849	signal-specific O-GlcNAcylation events	812:849	More broadly, our method will enable the discovery of signal-specific O-GlcNAcylation events in a wide array of experimental contexts.
24120863	2	6	theme	stimulus-specific	390:406	arg1	proteins					423:430	organelle- and stimulus-specific O-GlcNAcylated proteins	375:430	organelle- and stimulus-specific O-GlcNAcylated proteins	375:430	Here, we describe a method for visualizing and analyzing organelle- and stimulus-specific O-GlcNAcylated proteins and use it to identify the mitochondrial voltage-dependent anion channel 2 (VDAC2) as an O-GlcNAc substrate.
24120863	3	7	theme	mitochondrial	569:581	arg1	dysfunction					583:593	dysfunction	583:593	dysfunction	583:593	VDAC2(-/-) cells resist the mitochondrial dysfunction and apoptosis caused by global O-GlcNAc perturbation, demonstrating a functional connection between O-GlcNAc signaling and mitochondrial physiology through VDAC2.
24120863	1	8	theme	cell	192:195	arg1	modality					207:214	a critical cell signaling modality	181:214	a critical cell signaling modality	181:214	Protein modification by O-linked β-N-acetylglucosamine (O-GlcNAc) is a critical cell signaling modality, but identifying signal-specific O-GlcNAcylation events remains a significant experimental challenge.
24120863	1	8	theme	cell	192:195	arg1	modification					120:131	Protein modification	112:131	Protein modification by O-linked β-N-acetylglucosamine (O-GlcNAc)	112:176	Protein modification by O-linked β-N-acetylglucosamine (O-GlcNAc) is a critical cell signaling modality, but identifying signal-specific O-GlcNAcylation events remains a significant experimental challenge.
24120863	1	9	theme	signaling	197:205	arg1	modality					207:214	a critical cell signaling modality	181:214	a critical cell signaling modality	181:214	Protein modification by O-linked β-N-acetylglucosamine (O-GlcNAc) is a critical cell signaling modality, but identifying signal-specific O-GlcNAcylation events remains a significant experimental challenge.
24120863	1	9	theme	signaling	197:205	arg1	modification					120:131	Protein modification	112:131	Protein modification by O-linked β-N-acetylglucosamine (O-GlcNAc)	112:176	Protein modification by O-linked β-N-acetylglucosamine (O-GlcNAc) is a critical cell signaling modality, but identifying signal-specific O-GlcNAcylation events remains a significant experimental challenge.
24120863	0	10	theme	chemical	2:9	arg1	platform					27:34	A chemical glycoproteomics platform	0:34	A chemical glycoproteomics platform	0:34	A chemical glycoproteomics platform reveals O-GlcNAcylation of mitochondrial voltage-dependent anion channel 2.
24120863	3	11	theme	global	619:624	arg1	perturbation					635:646	global O-GlcNAc perturbation	619:646	global O-GlcNAc perturbation	619:646	VDAC2(-/-) cells resist the mitochondrial dysfunction and apoptosis caused by global O-GlcNAc perturbation, demonstrating a functional connection between O-GlcNAc signaling and mitochondrial physiology through VDAC2.
24120863	1	12	theme	Protein	112:118	arg1	modality					207:214	a critical cell signaling modality	181:214	a critical cell signaling modality	181:214	Protein modification by O-linked β-N-acetylglucosamine (O-GlcNAc) is a critical cell signaling modality, but identifying signal-specific O-GlcNAcylation events remains a significant experimental challenge.
24120863	1	12	theme	Protein	112:118	arg1	modification					120:131	Protein modification	112:131	Protein modification by O-linked β-N-acetylglucosamine (O-GlcNAc)	112:176	Protein modification by O-linked β-N-acetylglucosamine (O-GlcNAc) is a critical cell signaling modality, but identifying signal-specific O-GlcNAcylation events remains a significant experimental challenge.
24120863	4	13	theme	signal-specific	812:826	arg1	events					844:849	signal-specific O-GlcNAcylation events	812:849	signal-specific O-GlcNAcylation events	812:849	More broadly, our method will enable the discovery of signal-specific O-GlcNAcylation events in a wide array of experimental contexts.
24120863	0	14	theme	glycoproteomics	11:25	arg1	platform					27:34	A chemical glycoproteomics platform	0:34	A chemical glycoproteomics platform	0:34	A chemical glycoproteomics platform reveals O-GlcNAcylation of mitochondrial voltage-dependent anion channel 2.
24120863	1	15	theme	critical	183:190	arg1	modality					207:214	a critical cell signaling modality	181:214	a critical cell signaling modality	181:214	Protein modification by O-linked β-N-acetylglucosamine (O-GlcNAc) is a critical cell signaling modality, but identifying signal-specific O-GlcNAcylation events remains a significant experimental challenge.
24120863	1	15	theme	critical	183:190	arg1	modification					120:131	Protein modification	112:131	Protein modification by O-linked β-N-acetylglucosamine (O-GlcNAc)	112:176	Protein modification by O-linked β-N-acetylglucosamine (O-GlcNAc) is a critical cell signaling modality, but identifying signal-specific O-GlcNAcylation events remains a significant experimental challenge.
24120863	2	16	theme	anion	491:495	arg1	VDAC2					508:512	VDAC2	508:512	VDAC2	508:512	Here, we describe a method for visualizing and analyzing organelle- and stimulus-specific O-GlcNAcylated proteins and use it to identify the mitochondrial voltage-dependent anion channel 2 (VDAC2) as an O-GlcNAc substrate.
24120863	2	16	theme	anion	491:495	arg1	substrate					530:538	an O-GlcNAc substrate	518:538	an O-GlcNAc substrate	518:538	Here, we describe a method for visualizing and analyzing organelle- and stimulus-specific O-GlcNAcylated proteins and use it to identify the mitochondrial voltage-dependent anion channel 2 (VDAC2) as an O-GlcNAc substrate.
24120863	2	16	theme	anion	491:495	arg1	channel					497:503	the mitochondrial voltage-dependent anion channel 2	455:505	the mitochondrial voltage-dependent anion channel 2 (VDAC2)	455:513	Here, we describe a method for visualizing and analyzing organelle- and stimulus-specific O-GlcNAcylated proteins and use it to identify the mitochondrial voltage-dependent anion channel 2 (VDAC2) as an O-GlcNAc substrate.
24120863	1	17	theme	signal-specific	233:247	arg1	events					265:270	signal-specific O-GlcNAcylation events	233:270	signal-specific O-GlcNAcylation events	233:270	Protein modification by O-linked β-N-acetylglucosamine (O-GlcNAc) is a critical cell signaling modality, but identifying signal-specific O-GlcNAcylation events remains a significant experimental challenge.
24120863	2	18	theme	voltage-dependent	473:489	arg1	VDAC2					508:512	VDAC2	508:512	VDAC2	508:512	Here, we describe a method for visualizing and analyzing organelle- and stimulus-specific O-GlcNAcylated proteins and use it to identify the mitochondrial voltage-dependent anion channel 2 (VDAC2) as an O-GlcNAc substrate.
24120863	2	18	theme	voltage-dependent	473:489	arg1	substrate					530:538	an O-GlcNAc substrate	518:538	an O-GlcNAc substrate	518:538	Here, we describe a method for visualizing and analyzing organelle- and stimulus-specific O-GlcNAcylated proteins and use it to identify the mitochondrial voltage-dependent anion channel 2 (VDAC2) as an O-GlcNAc substrate.
24120863	2	18	theme	voltage-dependent	473:489	arg1	channel					497:503	the mitochondrial voltage-dependent anion channel 2	455:505	the mitochondrial voltage-dependent anion channel 2 (VDAC2)	455:513	Here, we describe a method for visualizing and analyzing organelle- and stimulus-specific O-GlcNAcylated proteins and use it to identify the mitochondrial voltage-dependent anion channel 2 (VDAC2) as an O-GlcNAc substrate.
24120863	2	19	theme	O-GlcNAc	521:528	arg1	channel					497:503	the mitochondrial voltage-dependent anion channel 2	455:505	the mitochondrial voltage-dependent anion channel 2 (VDAC2)	455:513	Here, we describe a method for visualizing and analyzing organelle- and stimulus-specific O-GlcNAcylated proteins and use it to identify the mitochondrial voltage-dependent anion channel 2 (VDAC2) as an O-GlcNAc substrate.
24120863	2	19	theme	O-GlcNAc	521:528	arg1	substrate					530:538	an O-GlcNAc substrate	518:538	an O-GlcNAc substrate	518:538	Here, we describe a method for visualizing and analyzing organelle- and stimulus-specific O-GlcNAcylated proteins and use it to identify the mitochondrial voltage-dependent anion channel 2 (VDAC2) as an O-GlcNAc substrate.
24120863	3	20	theme	a functional	663:674	arg1	connection					676:685	a functional connection	663:685	a functional connection between O-GlcNAc signaling and mitochondrial physiology through VDAC2	663:755	VDAC2(-/-) cells resist the mitochondrial dysfunction and apoptosis caused by global O-GlcNAc perturbation, demonstrating a functional connection between O-GlcNAc signaling and mitochondrial physiology through VDAC2.
24120863	1	21	theme	O-GlcNAcylation	249:263	arg1	events					265:270	signal-specific O-GlcNAcylation events	233:270	signal-specific O-GlcNAcylation events	233:270	Protein modification by O-linked β-N-acetylglucosamine (O-GlcNAc) is a critical cell signaling modality, but identifying signal-specific O-GlcNAcylation events remains a significant experimental challenge.
24120863	0	22	theme	mitochondrial	63:75	arg1	channel					101:107	mitochondrial voltage-dependent anion channel 2	63:109	mitochondrial voltage-dependent anion channel 2	63:109	A chemical glycoproteomics platform reveals O-GlcNAcylation of mitochondrial voltage-dependent anion channel 2.
24120863	3	23	theme	mitochondrial	718:730	arg1	physiology					732:741	mitochondrial physiology	718:741	mitochondrial physiology	718:741	VDAC2(-/-) cells resist the mitochondrial dysfunction and apoptosis caused by global O-GlcNAc perturbation, demonstrating a functional connection between O-GlcNAc signaling and mitochondrial physiology through VDAC2.
24120863	1	24	theme	O-linked	136:143	arg1	O-GlcNAc					168:175	O-GlcNAc	168:175	O-GlcNAc	168:175	Protein modification by O-linked β-N-acetylglucosamine (O-GlcNAc) is a critical cell signaling modality, but identifying signal-specific O-GlcNAcylation events remains a significant experimental challenge.
24120863	1	24	theme	O-linked	136:143	arg1	β-N-acetylglucosamine					145:165	O-linked β-N-acetylglucosamine	136:165	O-linked β-N-acetylglucosamine (O-GlcNAc)	136:176	Protein modification by O-linked β-N-acetylglucosamine (O-GlcNAc) is a critical cell signaling modality, but identifying signal-specific O-GlcNAcylation events remains a significant experimental challenge.
24120863	3	25	dep	dysfunction	583:593	arg1	the					565:567	the	565:567	the	565:567	VDAC2(-/-) cells resist the mitochondrial dysfunction and apoptosis caused by global O-GlcNAc perturbation, demonstrating a functional connection between O-GlcNAc signaling and mitochondrial physiology through VDAC2.
24120863	1	26	link	O-linked	136:143	arg1	O-GlcNAc					168:175	O-GlcNAc	168:175	O-GlcNAc	168:175	Protein modification by O-linked β-N-acetylglucosamine (O-GlcNAc) is a critical cell signaling modality, but identifying signal-specific O-GlcNAcylation events remains a significant experimental challenge.
24120863	1	26	link	O-linked	136:143	arg1	β-N-acetylglucosamine					145:165	O-linked β-N-acetylglucosamine	136:165	O-linked β-N-acetylglucosamine (O-GlcNAc)	136:176	Protein modification by O-linked β-N-acetylglucosamine (O-GlcNAc) is a critical cell signaling modality, but identifying signal-specific O-GlcNAcylation events remains a significant experimental challenge.
24120863	4	27	theme	contexts	883:890	arg1	array					861:865	a wide array	854:865	a wide array of experimental contexts	854:890	More broadly, our method will enable the discovery of signal-specific O-GlcNAcylation events in a wide array of experimental contexts.
24120863	3	28	theme	O-GlcNAc	695:702	arg1	signaling					704:712	O-GlcNAc signaling	695:712	O-GlcNAc signaling	695:712	VDAC2(-/-) cells resist the mitochondrial dysfunction and apoptosis caused by global O-GlcNAc perturbation, demonstrating a functional connection between O-GlcNAc signaling and mitochondrial physiology through VDAC2.
24120863	2	29	theme	organelle-	375:384	arg1	proteins					423:430	organelle- and stimulus-specific O-GlcNAcylated proteins	375:430	organelle- and stimulus-specific O-GlcNAcylated proteins	375:430	Here, we describe a method for visualizing and analyzing organelle- and stimulus-specific O-GlcNAcylated proteins and use it to identify the mitochondrial voltage-dependent anion channel 2 (VDAC2) as an O-GlcNAc substrate.
24120863	4	30	from	discovery	799:807	arg1	array					861:865	a wide array	854:865	a wide array of experimental contexts	854:890	More broadly, our method will enable the discovery of signal-specific O-GlcNAcylation events in a wide array of experimental contexts.
24120863	4	31	theme	experimental	870:881	arg1	contexts					883:890	experimental contexts	870:890	experimental contexts	870:890	More broadly, our method will enable the discovery of signal-specific O-GlcNAcylation events in a wide array of experimental contexts.
24120863	3	32	theme	VDAC2	541:545	arg1	cells					552:556	VDAC2(-/-) cells	541:556	VDAC2(-/-) cells	541:556	VDAC2(-/-) cells resist the mitochondrial dysfunction and apoptosis caused by global O-GlcNAc perturbation, demonstrating a functional connection between O-GlcNAc signaling and mitochondrial physiology through VDAC2.
24120863	0	33	theme	anion	95:99	arg1	channel					101:107	mitochondrial voltage-dependent anion channel 2	63:109	mitochondrial voltage-dependent anion channel 2	63:109	A chemical glycoproteomics platform reveals O-GlcNAcylation of mitochondrial voltage-dependent anion channel 2.
24120863	2	34	theme	mitochondrial	459:471	arg1	VDAC2					508:512	VDAC2	508:512	VDAC2	508:512	Here, we describe a method for visualizing and analyzing organelle- and stimulus-specific O-GlcNAcylated proteins and use it to identify the mitochondrial voltage-dependent anion channel 2 (VDAC2) as an O-GlcNAc substrate.
24120863	2	34	theme	mitochondrial	459:471	arg1	substrate					530:538	an O-GlcNAc substrate	518:538	an O-GlcNAc substrate	518:538	Here, we describe a method for visualizing and analyzing organelle- and stimulus-specific O-GlcNAcylated proteins and use it to identify the mitochondrial voltage-dependent anion channel 2 (VDAC2) as an O-GlcNAc substrate.
24120863	2	34	theme	mitochondrial	459:471	arg1	channel					497:503	the mitochondrial voltage-dependent anion channel 2	455:505	the mitochondrial voltage-dependent anion channel 2 (VDAC2)	455:513	Here, we describe a method for visualizing and analyzing organelle- and stimulus-specific O-GlcNAcylated proteins and use it to identify the mitochondrial voltage-dependent anion channel 2 (VDAC2) as an O-GlcNAc substrate.
24120863	0	35	theme	voltage-dependent	77:93	arg1	channel					101:107	mitochondrial voltage-dependent anion channel 2	63:109	mitochondrial voltage-dependent anion channel 2	63:109	A chemical glycoproteomics platform reveals O-GlcNAcylation of mitochondrial voltage-dependent anion channel 2.
24120863	3	36	theme	O-GlcNAc	626:633	arg1	perturbation					635:646	global O-GlcNAc perturbation	619:646	global O-GlcNAc perturbation	619:646	VDAC2(-/-) cells resist the mitochondrial dysfunction and apoptosis caused by global O-GlcNAc perturbation, demonstrating a functional connection between O-GlcNAc signaling and mitochondrial physiology through VDAC2.
24120863	1	37	theme	significant	282:292	arg1	challenge					307:315	a significant experimental challenge	280:315	a significant experimental challenge	280:315	Protein modification by O-linked β-N-acetylglucosamine (O-GlcNAc) is a critical cell signaling modality, but identifying signal-specific O-GlcNAcylation events remains a significant experimental challenge.
34819616	9	0	theme	proper	1672:1677	arg1	development					1679:1689	the proper development	1668:1689	the proper development of ectodermal lineage cells	1668:1717	Our findings using the Sox2 T258A mutant suggest that Sox2 T258 O-GlcNAc has a positive effect on ESC self-renewal and plays an important role in the proper development of ectodermal lineage cells.
34819616	10	1	theme	cell	1780:1783	arg1	decisions					1790:1798	early cell fate decisions	1774:1798	early cell fate decisions	1774:1798	Overall, our study directly links O-GlcNAcylation and early cell fate decisions.
34819616	1	2	theme	modification	233:244	arg1	Sox2					113:116	Sox2	113:116	Sox2	113:116	Sox2 is a core transcription factor in embryonic stem cells (ESCs), and O-GlcNAcylation is a type of post-translational modification of nuclear-cytoplasmic proteins.
34819616	1	2	theme	modification	233:244	arg1	O-GlcNAcylation					185:199	O-GlcNAcylation	185:199	O-GlcNAcylation	185:199	Sox2 is a core transcription factor in embryonic stem cells (ESCs), and O-GlcNAcylation is a type of post-translational modification of nuclear-cytoplasmic proteins.
34819616	1	2	theme	modification	233:244	arg1	type					206:209	a type	204:209	a type of post-translational modification of nuclear-cytoplasmic proteins	204:276	Sox2 is a core transcription factor in embryonic stem cells (ESCs), and O-GlcNAcylation is a type of post-translational modification of nuclear-cytoplasmic proteins.
34819616	1	2	theme	modification	233:244	arg1	factor					142:147	a core transcription factor	121:147	a core transcription factor in embryonic stem cells (ESCs)	121:178	Sox2 is a core transcription factor in embryonic stem cells (ESCs), and O-GlcNAcylation is a type of post-translational modification of nuclear-cytoplasmic proteins.
34819616	9	3	contain	has	1595:1597	arg2	effect					1610:1615	a positive effect	1599:1615	a positive effect	1599:1615	Our findings using the Sox2 T258A mutant suggest that Sox2 T258 O-GlcNAc has a positive effect on ESC self-renewal and plays an important role in the proper development of ectodermal lineage cells.
34819616	9	3	contain	has	1595:1597	arg1	O-GlcNAc					1586:1593	Sox2 T258 O-GlcNAc	1576:1593	Sox2 T258 O-GlcNAc	1576:1593	Our findings using the Sox2 T258A mutant suggest that Sox2 T258 O-GlcNAc has a positive effect on ESC self-renewal and plays an important role in the proper development of ectodermal lineage cells.
34819616	1	4	theme	embryonic	152:160	arg1	ESCs					174:177	ESCs	174:177	ESCs	174:177	Sox2 is a core transcription factor in embryonic stem cells (ESCs), and O-GlcNAcylation is a type of post-translational modification of nuclear-cytoplasmic proteins.
34819616	1	4	theme	embryonic	152:160	arg1	cells					167:171	embryonic stem cells	152:171	embryonic stem cells (ESCs)	152:178	Sox2 is a core transcription factor in embryonic stem cells (ESCs), and O-GlcNAcylation is a type of post-translational modification of nuclear-cytoplasmic proteins.
34819616	9	5	theme	lineage	1705:1711	arg1	cells					1713:1717	ectodermal lineage cells	1694:1717	ectodermal lineage cells	1694:1717	Our findings using the Sox2 T258A mutant suggest that Sox2 T258 O-GlcNAc has a positive effect on ESC self-renewal and plays an important role in the proper development of ectodermal lineage cells.
34819616	5	6	theme	Sox2	796:799	arg1	mutation					807:814	the Sox2 T258A mutation	792:814	the Sox2 T258A mutation heterologously introduced using the CRISPR/Cas9 system	792:869	ESCs with the Sox2 T258A mutation heterologously introduced using the CRISPR/Cas9 system, designated E14-Sox2TA/WT, also exhibited reduced self-renewal.
34819616	0	7	theme	cells	106:110	arg1	fate					83:86	the self-renewal and early cell fate	51:86	the self-renewal and early cell fate of embryonic stem cells	51:110	O-GlcNAcylation of Sox2 at threonine 258 regulates the self-renewal and early cell fate of embryonic stem cells.
34819616	2	8	theme	Sox2	486:489	arg1	O-GlcNAcylation					491:505	Sox2 O-GlcNAcylation	486:505	Sox2 O-GlcNAcylation	486:505	Although both factors play important roles in the maintenance and differentiation of ESCs and the serine 248 (S248) and threonine 258 (T258) residues of Sox2 are modified by O-GlcNAcylation, the function of Sox2 O-GlcNAcylation is unclear.
34819616	8	9	theme	teratomas	1384:1392	arg1	sequencing					1370:1379	RNA sequencing	1366:1379	RNA sequencing of teratomas	1366:1392	RNA sequencing of teratomas revealed that genes related to brain development had generally downregulated expression in the E14-Sox2TA/WT-derived teratomas.
34819616	7	10	from	decrease	1211:1218	arg1	tissue					1234:1239	ectodermal tissue	1223:1239	ectodermal tissue	1223:1239	There was a significant decrease in ectodermal tissue and a marked increase in cartilage tissue in E14-Sox2TA/WT-derived teratomas compared with normal E14 ESC-derived teratomas.
34819616	7	10	from	decrease	1211:1218	arg1	tissue					1276:1281	cartilage tissue	1266:1281	cartilage tissue in E14-Sox2TA/WT-derived teratomas	1266:1316	There was a significant decrease in ectodermal tissue and a marked increase in cartilage tissue in E14-Sox2TA/WT-derived teratomas compared with normal E14 ESC-derived teratomas.
34819616	7	11	theme	E14	1339:1341	arg1	teratomas					1355:1363	normal E14 ESC-derived teratomas	1332:1363	normal E14 ESC-derived teratomas	1332:1363	There was a significant decrease in ectodermal tissue and a marked increase in cartilage tissue in E14-Sox2TA/WT-derived teratomas compared with normal E14 ESC-derived teratomas.
34819616	1	12	theme	core	123:126	arg1	Sox2					113:116	Sox2	113:116	Sox2	113:116	Sox2 is a core transcription factor in embryonic stem cells (ESCs), and O-GlcNAcylation is a type of post-translational modification of nuclear-cytoplasmic proteins.
34819616	1	12	theme	core	123:126	arg1	factor					142:147	a core transcription factor	121:147	a core transcription factor in embryonic stem cells (ESCs)	121:178	Sox2 is a core transcription factor in embryonic stem cells (ESCs), and O-GlcNAcylation is a type of post-translational modification of nuclear-cytoplasmic proteins.
34819616	8	13	from	expression	1471:1480	arg1	teratomas					1511:1519	the E14-Sox2TA/WT-derived teratomas	1485:1519	the E14-Sox2TA/WT-derived teratomas	1485:1519	RNA sequencing of teratomas revealed that genes related to brain development had generally downregulated expression in the E14-Sox2TA/WT-derived teratomas.
34819616	3	14	theme	Sox2	557:560	arg1	O-GlcNAcylation					538:552	O-GlcNAcylation	538:552	O-GlcNAcylation of Sox2 at T258	538:568	Here, we show that O-GlcNAcylation of Sox2 at T258 regulates mouse ESC self-renewal and early cell fate.
34819616	9	15	theme	T258A	1550:1554	arg1	mutant					1556:1561	the Sox2 T258A mutant	1541:1561	the Sox2 T258A mutant	1541:1561	Our findings using the Sox2 T258A mutant suggest that Sox2 T258 O-GlcNAc has a positive effect on ESC self-renewal and plays an important role in the proper development of ectodermal lineage cells.
34819616	0	16	theme	early	72:76	arg1	fate					83:86	the self-renewal and early cell fate	51:86	the self-renewal and early cell fate of embryonic stem cells	51:110	O-GlcNAcylation of Sox2 at threonine 258 regulates the self-renewal and early cell fate of embryonic stem cells.
34819616	6	17	theme	sequencing	939:948	arg1	analysis					950:957	RNA sequencing analysis	935:957	RNA sequencing analysis under self-renewal conditions	935:987	RNA sequencing analysis under self-renewal conditions showed that upregulated expression of early differentiation genes, rather than a downregulated expression of self-renewal genes, was responsible for the reduced self-renewal of E14-Sox2TA/WT cells.
34819616	9	18	theme	Sox2	1576:1579	arg1	O-GlcNAc					1586:1593	Sox2 T258 O-GlcNAc	1576:1593	Sox2 T258 O-GlcNAc	1576:1593	Our findings using the Sox2 T258A mutant suggest that Sox2 T258 O-GlcNAc has a positive effect on ESC self-renewal and plays an important role in the proper development of ectodermal lineage cells.
34819616	2	19	theme	serine	377:382	arg1	Sox2					432:435	Sox2	432:435	Sox2	432:435	Although both factors play important roles in the maintenance and differentiation of ESCs and the serine 248 (S248) and threonine 258 (T258) residues of Sox2 are modified by O-GlcNAcylation, the function of Sox2 O-GlcNAcylation is unclear.
34819616	2	19	theme	serine	377:382	arg1	residues					420:427	the serine 248 (S248) and threonine 258 (T258) residues	373:427	the serine 248 (S248) and threonine 258 (T258) residues of Sox2	373:435	Although both factors play important roles in the maintenance and differentiation of ESCs and the serine 248 (S248) and threonine 258 (T258) residues of Sox2 are modified by O-GlcNAcylation, the function of Sox2 O-GlcNAcylation is unclear.
34819616	0	20	theme	embryonic	91:99	arg1	cells					106:110	embryonic stem cells	91:110	embryonic stem cells	91:110	O-GlcNAcylation of Sox2 at threonine 258 regulates the self-renewal and early cell fate of embryonic stem cells.
34819616	7	21	theme	normal	1332:1337	arg1	teratomas					1355:1363	normal E14 ESC-derived teratomas	1332:1363	normal E14 ESC-derived teratomas	1332:1363	There was a significant decrease in ectodermal tissue and a marked increase in cartilage tissue in E14-Sox2TA/WT-derived teratomas compared with normal E14 ESC-derived teratomas.
34819616	0	22	from	threonine	27:35	arg1	O-GlcNAcylation					0:14	O-GlcNAcylation	0:14	O-GlcNAcylation of Sox2 at threonine 258	0:39	O-GlcNAcylation of Sox2 at threonine 258 regulates the self-renewal and early cell fate of embryonic stem cells.
34819616	3	23	from	T258	565:568	arg1	O-GlcNAcylation					538:552	O-GlcNAcylation	538:552	O-GlcNAcylation of Sox2 at T258	538:568	Here, we show that O-GlcNAcylation of Sox2 at T258 regulates mouse ESC self-renewal and early cell fate.
34819616	6	24	theme	early	1027:1031	arg1	genes					1049:1053	early differentiation genes	1027:1053	early differentiation genes	1027:1053	RNA sequencing analysis under self-renewal conditions showed that upregulated expression of early differentiation genes, rather than a downregulated expression of self-renewal genes, was responsible for the reduced self-renewal of E14-Sox2TA/WT cells.
34819616	2	25	theme	threonine	399:407	arg1	Sox2					432:435	Sox2	432:435	Sox2	432:435	Although both factors play important roles in the maintenance and differentiation of ESCs and the serine 248 (S248) and threonine 258 (T258) residues of Sox2 are modified by O-GlcNAcylation, the function of Sox2 O-GlcNAcylation is unclear.
34819616	2	25	theme	threonine	399:407	arg1	residues					420:427	the serine 248 (S248) and threonine 258 (T258) residues	373:427	the serine 248 (S248) and threonine 258 (T258) residues of Sox2	373:435	Although both factors play important roles in the maintenance and differentiation of ESCs and the serine 248 (S248) and threonine 258 (T258) residues of Sox2 are modified by O-GlcNAcylation, the function of Sox2 O-GlcNAcylation is unclear.
34819616	6	26	theme	cells	1180:1184	arg1	self-renewal					1150:1161	self-renewal	1150:1161	self-renewal	1150:1161	RNA sequencing analysis under self-renewal conditions showed that upregulated expression of early differentiation genes, rather than a downregulated expression of self-renewal genes, was responsible for the reduced self-renewal of E14-Sox2TA/WT cells.
34819616	4	27	theme	T258A	680:684	arg1	mutant					686:691	the Sox2 T258A mutant	671:691	the Sox2 T258A mutant	671:691	ESCs in which wild-type Sox2 was replaced with the Sox2 T258A mutant exhibited reduced self-renewal, whereas ESCs with the Sox2 S248A point mutation did not.
34819616	0	28	theme	Sox2	19:22	arg1	O-GlcNAcylation					0:14	O-GlcNAcylation	0:14	O-GlcNAcylation of Sox2 at threonine 258	0:39	O-GlcNAcylation of Sox2 at threonine 258 regulates the self-renewal and early cell fate of embryonic stem cells.
34819616	1	29	theme	proteins	269:276	arg1	modification					233:244	post-translational modification	214:244	post-translational modification of nuclear-cytoplasmic proteins	214:276	Sox2 is a core transcription factor in embryonic stem cells (ESCs), and O-GlcNAcylation is a type of post-translational modification of nuclear-cytoplasmic proteins.
34819616	7	30	theme	E14-Sox2TA/WT-derived	1286:1306	arg1	teratomas					1308:1316	E14-Sox2TA/WT-derived teratomas	1286:1316	E14-Sox2TA/WT-derived teratomas	1286:1316	There was a significant decrease in ectodermal tissue and a marked increase in cartilage tissue in E14-Sox2TA/WT-derived teratomas compared with normal E14 ESC-derived teratomas.
34819616	0	31	theme	self-renewal	55:66	arg1	fate					83:86	the self-renewal and early cell fate	51:86	the self-renewal and early cell fate of embryonic stem cells	51:110	O-GlcNAcylation of Sox2 at threonine 258 regulates the self-renewal and early cell fate of embryonic stem cells.
34819616	3	32	theme	self-renewal	590:601	arg1	fate					618:621	mouse ESC self-renewal and early cell fate	580:621	mouse ESC self-renewal and early cell fate	580:621	Here, we show that O-GlcNAcylation of Sox2 at T258 regulates mouse ESC self-renewal and early cell fate.
34819616	4	33	theme	Sox2	747:750	arg1	mutation					764:771	the Sox2 S248A point mutation	743:771	the Sox2 S248A point mutation	743:771	ESCs in which wild-type Sox2 was replaced with the Sox2 T258A mutant exhibited reduced self-renewal, whereas ESCs with the Sox2 S248A point mutation did not.
34819616	2	34	mod	modified	441:448	arg3	O-GlcNAcylation					453:467	O-GlcNAcylation	453:467	O-GlcNAcylation	453:467	Although both factors play important roles in the maintenance and differentiation of ESCs and the serine 248 (S248) and threonine 258 (T258) residues of Sox2 are modified by O-GlcNAcylation, the function of Sox2 O-GlcNAcylation is unclear.
34819616	2	34	mod	modified	441:448	arg1	Sox2					432:435	Sox2	432:435	Sox2	432:435	Although both factors play important roles in the maintenance and differentiation of ESCs and the serine 248 (S248) and threonine 258 (T258) residues of Sox2 are modified by O-GlcNAcylation, the function of Sox2 O-GlcNAcylation is unclear.
34819616	2	34	mod	modified	441:448	arg1	residues					420:427	the serine 248 (S248) and threonine 258 (T258) residues	373:427	the serine 248 (S248) and threonine 258 (T258) residues of Sox2	373:435	Although both factors play important roles in the maintenance and differentiation of ESCs and the serine 248 (S248) and threonine 258 (T258) residues of Sox2 are modified by O-GlcNAcylation, the function of Sox2 O-GlcNAcylation is unclear.
34819616	5	35	theme	T258A	801:805	arg1	mutation					807:814	the Sox2 T258A mutation	792:814	the Sox2 T258A mutation heterologously introduced using the CRISPR/Cas9 system	792:869	ESCs with the Sox2 T258A mutation heterologously introduced using the CRISPR/Cas9 system, designated E14-Sox2TA/WT, also exhibited reduced self-renewal.
34819616	3	36	theme	mouse	580:584	arg1	fate					618:621	mouse ESC self-renewal and early cell fate	580:621	mouse ESC self-renewal and early cell fate	580:621	Here, we show that O-GlcNAcylation of Sox2 at T258 regulates mouse ESC self-renewal and early cell fate.
34819616	4	37	theme	point	758:762	arg1	mutation					764:771	the Sox2 S248A point mutation	743:771	the Sox2 S248A point mutation	743:771	ESCs in which wild-type Sox2 was replaced with the Sox2 T258A mutant exhibited reduced self-renewal, whereas ESCs with the Sox2 S248A point mutation did not.
34819616	6	38	theme	self-renewal	1098:1109	arg1	genes					1111:1115	self-renewal genes	1098:1115	self-renewal genes	1098:1115	RNA sequencing analysis under self-renewal conditions showed that upregulated expression of early differentiation genes, rather than a downregulated expression of self-renewal genes, was responsible for the reduced self-renewal of E14-Sox2TA/WT cells.
34819616	6	39	theme	E14-Sox2TA/WT	1166:1178	arg1	cells					1180:1184	E14-Sox2TA/WT cells	1166:1184	E14-Sox2TA/WT cells	1166:1184	RNA sequencing analysis under self-renewal conditions showed that upregulated expression of early differentiation genes, rather than a downregulated expression of self-renewal genes, was responsible for the reduced self-renewal of E14-Sox2TA/WT cells.
34819616	5	40	with	ESCs	782:785	arg1	mutation					807:814	the Sox2 T258A mutation	792:814	the Sox2 T258A mutation heterologously introduced using the CRISPR/Cas9 system	792:869	ESCs with the Sox2 T258A mutation heterologously introduced using the CRISPR/Cas9 system, designated E14-Sox2TA/WT, also exhibited reduced self-renewal.
34819616	8	41	theme	brain	1425:1429	arg1	development					1431:1441	brain development	1425:1441	brain development	1425:1441	RNA sequencing of teratomas revealed that genes related to brain development had generally downregulated expression in the E14-Sox2TA/WT-derived teratomas.
34819616	7	42	theme	marked	1247:1252	arg1	increase					1254:1261	a marked increase	1245:1261	a marked increase in cartilage tissue in E14-Sox2TA/WT-derived teratomas	1245:1316	There was a significant decrease in ectodermal tissue and a marked increase in cartilage tissue in E14-Sox2TA/WT-derived teratomas compared with normal E14 ESC-derived teratomas.
34819616	3	43	theme	early	607:611	arg1	fate					618:621	mouse ESC self-renewal and early cell fate	580:621	mouse ESC self-renewal and early cell fate	580:621	Here, we show that O-GlcNAcylation of Sox2 at T258 regulates mouse ESC self-renewal and early cell fate.
34819616	7	44	theme	ectodermal	1223:1232	arg1	tissue					1234:1239	ectodermal tissue	1223:1239	ectodermal tissue	1223:1239	There was a significant decrease in ectodermal tissue and a marked increase in cartilage tissue in E14-Sox2TA/WT-derived teratomas compared with normal E14 ESC-derived teratomas.
34819616	8	45	theme	related	1414:1420	arg1	genes					1408:1412	genes	1408:1412	genes related to brain development	1408:1441	RNA sequencing of teratomas revealed that genes related to brain development had generally downregulated expression in the E14-Sox2TA/WT-derived teratomas.
34819616	10	46	theme	fate	1785:1788	arg1	decisions					1790:1798	early cell fate decisions	1774:1798	early cell fate decisions	1774:1798	Overall, our study directly links O-GlcNAcylation and early cell fate decisions.
34819616	1	47	theme	post-translational	214:231	arg1	modification					233:244	post-translational modification	214:244	post-translational modification of nuclear-cytoplasmic proteins	214:276	Sox2 is a core transcription factor in embryonic stem cells (ESCs), and O-GlcNAcylation is a type of post-translational modification of nuclear-cytoplasmic proteins.
34819616	7	48	link	E14-Sox2TA/WT-derived	1286:1306	arg1	teratomas					1308:1316	E14-Sox2TA/WT-derived teratomas	1286:1316	E14-Sox2TA/WT-derived teratomas	1286:1316	There was a significant decrease in ectodermal tissue and a marked increase in cartilage tissue in E14-Sox2TA/WT-derived teratomas compared with normal E14 ESC-derived teratomas.
34819616	4	49	dep	exhibited	693:701	arg1	reduced					703:709	reduced	703:709	exhibited reduced self-renewal	693:722	ESCs in which wild-type Sox2 was replaced with the Sox2 T258A mutant exhibited reduced self-renewal, whereas ESCs with the Sox2 S248A point mutation did not.
34819616	4	49	dep	exhibited	693:701	arg1	whereas					725:731	whereas	725:731	whereas	725:731	ESCs in which wild-type Sox2 was replaced with the Sox2 T258A mutant exhibited reduced self-renewal, whereas ESCs with the Sox2 S248A point mutation did not.
34819616	10	50	theme	early	1774:1778	arg1	decisions					1790:1798	early cell fate decisions	1774:1798	early cell fate decisions	1774:1798	Overall, our study directly links O-GlcNAcylation and early cell fate decisions.
34819616	9	51	theme	ectodermal	1694:1703	arg1	cells					1713:1717	ectodermal lineage cells	1694:1717	ectodermal lineage cells	1694:1717	Our findings using the Sox2 T258A mutant suggest that Sox2 T258 O-GlcNAc has a positive effect on ESC self-renewal and plays an important role in the proper development of ectodermal lineage cells.
34819616	1	52	theme	stem	162:165	arg1	ESCs					174:177	ESCs	174:177	ESCs	174:177	Sox2 is a core transcription factor in embryonic stem cells (ESCs), and O-GlcNAcylation is a type of post-translational modification of nuclear-cytoplasmic proteins.
34819616	1	52	theme	stem	162:165	arg1	cells					167:171	embryonic stem cells	152:171	embryonic stem cells (ESCs)	152:178	Sox2 is a core transcription factor in embryonic stem cells (ESCs), and O-GlcNAcylation is a type of post-translational modification of nuclear-cytoplasmic proteins.
34819616	9	53	theme	cells	1713:1717	arg1	development					1679:1689	the proper development	1668:1689	the proper development of ectodermal lineage cells	1668:1717	Our findings using the Sox2 T258A mutant suggest that Sox2 T258 O-GlcNAc has a positive effect on ESC self-renewal and plays an important role in the proper development of ectodermal lineage cells.
34819616	7	54	from	increase	1254:1261	arg1	tissue					1234:1239	ectodermal tissue	1223:1239	ectodermal tissue	1223:1239	There was a significant decrease in ectodermal tissue and a marked increase in cartilage tissue in E14-Sox2TA/WT-derived teratomas compared with normal E14 ESC-derived teratomas.
34819616	7	54	from	increase	1254:1261	arg1	tissue					1276:1281	cartilage tissue	1266:1281	cartilage tissue in E14-Sox2TA/WT-derived teratomas	1266:1316	There was a significant decrease in ectodermal tissue and a marked increase in cartilage tissue in E14-Sox2TA/WT-derived teratomas compared with normal E14 ESC-derived teratomas.
34819616	2	55	theme	O-GlcNAcylation	491:505	arg1	unclear					510:516	unclear	510:516	unclear	510:516	Although both factors play important roles in the maintenance and differentiation of ESCs and the serine 248 (S248) and threonine 258 (T258) residues of Sox2 are modified by O-GlcNAcylation, the function of Sox2 O-GlcNAcylation is unclear.
34819616	2	55	theme	O-GlcNAcylation	491:505	arg1	function					474:481	the function	470:481	the function of Sox2 O-GlcNAcylation	470:505	Although both factors play important roles in the maintenance and differentiation of ESCs and the serine 248 (S248) and threonine 258 (T258) residues of Sox2 are modified by O-GlcNAcylation, the function of Sox2 O-GlcNAcylation is unclear.
34819616	1	56	from	type	206:209	arg1	ESCs					174:177	ESCs	174:177	ESCs	174:177	Sox2 is a core transcription factor in embryonic stem cells (ESCs), and O-GlcNAcylation is a type of post-translational modification of nuclear-cytoplasmic proteins.
34819616	1	56	from	type	206:209	arg1	cells					167:171	embryonic stem cells	152:171	embryonic stem cells (ESCs)	152:178	Sox2 is a core transcription factor in embryonic stem cells (ESCs), and O-GlcNAcylation is a type of post-translational modification of nuclear-cytoplasmic proteins.
34819616	8	57	theme	E14-Sox2TA/WT-derived	1489:1509	arg1	teratomas					1511:1519	the E14-Sox2TA/WT-derived teratomas	1485:1519	the E14-Sox2TA/WT-derived teratomas	1485:1519	RNA sequencing of teratomas revealed that genes related to brain development had generally downregulated expression in the E14-Sox2TA/WT-derived teratomas.
34819616	4	58	theme	wild-type	638:646	arg1	Sox2					648:651	wild-type Sox2	638:651	wild-type Sox2	638:651	ESCs in which wild-type Sox2 was replaced with the Sox2 T258A mutant exhibited reduced self-renewal, whereas ESCs with the Sox2 S248A point mutation did not.
34819616	5	59	theme	CRISPR/Cas9	852:862	arg1	system					864:869	the CRISPR/Cas9 system	848:869	the CRISPR/Cas9 system	848:869	ESCs with the Sox2 T258A mutation heterologously introduced using the CRISPR/Cas9 system, designated E14-Sox2TA/WT, also exhibited reduced self-renewal.
34819616	5	60	dep	exhibited	903:911	arg1	reduced					913:919	reduced	913:919	exhibited reduced self-renewal	903:932	ESCs with the Sox2 T258A mutation heterologously introduced using the CRISPR/Cas9 system, designated E14-Sox2TA/WT, also exhibited reduced self-renewal.
34819616	7	61	theme	significant	1199:1209	arg1	decrease					1211:1218	a significant decrease	1197:1218	a significant decrease in ectodermal tissue	1197:1239	There was a significant decrease in ectodermal tissue and a marked increase in cartilage tissue in E14-Sox2TA/WT-derived teratomas compared with normal E14 ESC-derived teratomas.
34819616	9	62	theme	Sox2	1545:1548	arg1	mutant					1556:1561	the Sox2 T258A mutant	1541:1561	the Sox2 T258A mutant	1541:1561	Our findings using the Sox2 T258A mutant suggest that Sox2 T258 O-GlcNAc has a positive effect on ESC self-renewal and plays an important role in the proper development of ectodermal lineage cells.
34819616	6	63	theme	self-renewal	965:976	arg1	conditions					978:987	self-renewal conditions	965:987	self-renewal conditions	965:987	RNA sequencing analysis under self-renewal conditions showed that upregulated expression of early differentiation genes, rather than a downregulated expression of self-renewal genes, was responsible for the reduced self-renewal of E14-Sox2TA/WT cells.
34819616	7	64	theme	ESC-derived	1343:1353	arg1	teratomas					1355:1363	normal E14 ESC-derived teratomas	1332:1363	normal E14 ESC-derived teratomas	1332:1363	There was a significant decrease in ectodermal tissue and a marked increase in cartilage tissue in E14-Sox2TA/WT-derived teratomas compared with normal E14 ESC-derived teratomas.
34819616	0	65	theme	cell	78:81	arg1	fate					83:86	the self-renewal and early cell fate	51:86	the self-renewal and early cell fate of embryonic stem cells	51:110	O-GlcNAcylation of Sox2 at threonine 258 regulates the self-renewal and early cell fate of embryonic stem cells.
34819616	1	66	theme	transcription	128:140	arg1	Sox2					113:116	Sox2	113:116	Sox2	113:116	Sox2 is a core transcription factor in embryonic stem cells (ESCs), and O-GlcNAcylation is a type of post-translational modification of nuclear-cytoplasmic proteins.
34819616	1	66	theme	transcription	128:140	arg1	factor					142:147	a core transcription factor	121:147	a core transcription factor in embryonic stem cells (ESCs)	121:178	Sox2 is a core transcription factor in embryonic stem cells (ESCs), and O-GlcNAcylation is a type of post-translational modification of nuclear-cytoplasmic proteins.
34819616	2	67	theme	Sox2	432:435	arg1	Sox2					432:435	Sox2	432:435	Sox2	432:435	Although both factors play important roles in the maintenance and differentiation of ESCs and the serine 248 (S248) and threonine 258 (T258) residues of Sox2 are modified by O-GlcNAcylation, the function of Sox2 O-GlcNAcylation is unclear.
34819616	2	67	theme	Sox2	432:435	arg1	residues					420:427	the serine 248 (S248) and threonine 258 (T258) residues	373:427	the serine 248 (S248) and threonine 258 (T258) residues of Sox2	373:435	Although both factors play important roles in the maintenance and differentiation of ESCs and the serine 248 (S248) and threonine 258 (T258) residues of Sox2 are modified by O-GlcNAcylation, the function of Sox2 O-GlcNAcylation is unclear.
34819616	4	68	with	ESCs	733:736	arg1	mutation					764:771	the Sox2 S248A point mutation	743:771	the Sox2 S248A point mutation	743:771	ESCs in which wild-type Sox2 was replaced with the Sox2 T258A mutant exhibited reduced self-renewal, whereas ESCs with the Sox2 S248A point mutation did not.
34819616	1	69	from	factor	142:147	arg1	ESCs					174:177	ESCs	174:177	ESCs	174:177	Sox2 is a core transcription factor in embryonic stem cells (ESCs), and O-GlcNAcylation is a type of post-translational modification of nuclear-cytoplasmic proteins.
34819616	1	69	from	factor	142:147	arg1	cells					167:171	embryonic stem cells	152:171	embryonic stem cells (ESCs)	152:178	Sox2 is a core transcription factor in embryonic stem cells (ESCs), and O-GlcNAcylation is a type of post-translational modification of nuclear-cytoplasmic proteins.
34819616	6	70	theme	upregulated	1001:1011	arg1	expression					1013:1022	upregulated expression	1001:1022	upregulated expression of early differentiation genes	1001:1053	RNA sequencing analysis under self-renewal conditions showed that upregulated expression of early differentiation genes, rather than a downregulated expression of self-renewal genes, was responsible for the reduced self-renewal of E14-Sox2TA/WT cells.
34819616	6	71	theme	RNA	935:937	arg1	analysis					950:957	RNA sequencing analysis	935:957	RNA sequencing analysis under self-renewal conditions	935:987	RNA sequencing analysis under self-renewal conditions showed that upregulated expression of early differentiation genes, rather than a downregulated expression of self-renewal genes, was responsible for the reduced self-renewal of E14-Sox2TA/WT cells.
34819616	2	72	dep	maintenance	329:339	arg1	the					325:327	the	325:327	the	325:327	Although both factors play important roles in the maintenance and differentiation of ESCs and the serine 248 (S248) and threonine 258 (T258) residues of Sox2 are modified by O-GlcNAcylation, the function of Sox2 O-GlcNAcylation is unclear.
34819616	0	73	theme	stem	101:104	arg1	cells					106:110	embryonic stem cells	91:110	embryonic stem cells	91:110	O-GlcNAcylation of Sox2 at threonine 258 regulates the self-renewal and early cell fate of embryonic stem cells.
34819616	9	74	theme	T258	1581:1584	arg1	O-GlcNAc					1586:1593	Sox2 T258 O-GlcNAc	1576:1593	Sox2 T258 O-GlcNAc	1576:1593	Our findings using the Sox2 T258A mutant suggest that Sox2 T258 O-GlcNAc has a positive effect on ESC self-renewal and plays an important role in the proper development of ectodermal lineage cells.
34819616	6	75	theme	differentiation	1033:1047	arg1	genes					1049:1053	early differentiation genes	1027:1053	early differentiation genes	1027:1053	RNA sequencing analysis under self-renewal conditions showed that upregulated expression of early differentiation genes, rather than a downregulated expression of self-renewal genes, was responsible for the reduced self-renewal of E14-Sox2TA/WT cells.
34819616	7	76	link	ESC-derived	1343:1353	arg1	teratomas					1355:1363	normal E14 ESC-derived teratomas	1332:1363	normal E14 ESC-derived teratomas	1332:1363	There was a significant decrease in ectodermal tissue and a marked increase in cartilage tissue in E14-Sox2TA/WT-derived teratomas compared with normal E14 ESC-derived teratomas.
34819616	8	77	theme	RNA	1366:1368	arg1	sequencing					1370:1379	RNA sequencing	1366:1379	RNA sequencing of teratomas	1366:1392	RNA sequencing of teratomas revealed that genes related to brain development had generally downregulated expression in the E14-Sox2TA/WT-derived teratomas.
34819616	2	78	theme	ESCs	364:367	arg1	differentiation					345:359	differentiation	345:359	differentiation	345:359	Although both factors play important roles in the maintenance and differentiation of ESCs and the serine 248 (S248) and threonine 258 (T258) residues of Sox2 are modified by O-GlcNAcylation, the function of Sox2 O-GlcNAcylation is unclear.
34819616	2	78	theme	ESCs	364:367	arg1	maintenance					329:339	maintenance	329:339	maintenance	329:339	Although both factors play important roles in the maintenance and differentiation of ESCs and the serine 248 (S248) and threonine 258 (T258) residues of Sox2 are modified by O-GlcNAcylation, the function of Sox2 O-GlcNAcylation is unclear.
34819616	1	79	theme	nuclear-cytoplasmic	249:267	arg1	proteins					269:276	nuclear-cytoplasmic proteins	249:276	nuclear-cytoplasmic proteins	249:276	Sox2 is a core transcription factor in embryonic stem cells (ESCs), and O-GlcNAcylation is a type of post-translational modification of nuclear-cytoplasmic proteins.
34819616	9	80	theme	positive	1601:1608	arg1	effect					1610:1615	a positive effect	1599:1615	a positive effect	1599:1615	Our findings using the Sox2 T258A mutant suggest that Sox2 T258 O-GlcNAc has a positive effect on ESC self-renewal and plays an important role in the proper development of ectodermal lineage cells.
34819616	3	81	theme	ESC	586:588	arg1	fate					618:621	mouse ESC self-renewal and early cell fate	580:621	mouse ESC self-renewal and early cell fate	580:621	Here, we show that O-GlcNAcylation of Sox2 at T258 regulates mouse ESC self-renewal and early cell fate.
34819616	4	82	theme	Sox2	675:678	arg1	mutant					686:691	the Sox2 T258A mutant	671:691	the Sox2 T258A mutant	671:691	ESCs in which wild-type Sox2 was replaced with the Sox2 T258A mutant exhibited reduced self-renewal, whereas ESCs with the Sox2 S248A point mutation did not.
34819616	7	83	theme	cartilage	1266:1274	arg1	tissue					1276:1281	cartilage tissue	1266:1281	cartilage tissue in E14-Sox2TA/WT-derived teratomas	1266:1316	There was a significant decrease in ectodermal tissue and a marked increase in cartilage tissue in E14-Sox2TA/WT-derived teratomas compared with normal E14 ESC-derived teratomas.
34819616	9	84	theme	self-renewal	1624:1635	arg1	ESC					1620:1622	ESC self-renewal	1620:1635	ESC self-renewal	1620:1635	Our findings using the Sox2 T258A mutant suggest that Sox2 T258 O-GlcNAc has a positive effect on ESC self-renewal and plays an important role in the proper development of ectodermal lineage cells.
34819616	7	85	from	tissue	1276:1281	arg1	teratomas					1308:1316	E14-Sox2TA/WT-derived teratomas	1286:1316	E14-Sox2TA/WT-derived teratomas	1286:1316	There was a significant decrease in ectodermal tissue and a marked increase in cartilage tissue in E14-Sox2TA/WT-derived teratomas compared with normal E14 ESC-derived teratomas.
34819616	6	86	theme	genes	1111:1115	arg1	responsible					1122:1132	responsible	1122:1132	responsible	1122:1132	RNA sequencing analysis under self-renewal conditions showed that upregulated expression of early differentiation genes, rather than a downregulated expression of self-renewal genes, was responsible for the reduced self-renewal of E14-Sox2TA/WT cells.
34819616	6	86	theme	genes	1111:1115	arg1	expression					1084:1093	a downregulated expression	1068:1093	a downregulated expression of self-renewal genes	1068:1115	RNA sequencing analysis under self-renewal conditions showed that upregulated expression of early differentiation genes, rather than a downregulated expression of self-renewal genes, was responsible for the reduced self-renewal of E14-Sox2TA/WT cells.
34819616	3	87	theme	cell	613:616	arg1	fate					618:621	mouse ESC self-renewal and early cell fate	580:621	mouse ESC self-renewal and early cell fate	580:621	Here, we show that O-GlcNAcylation of Sox2 at T258 regulates mouse ESC self-renewal and early cell fate.
34819616	4	88	theme	S248A	752:756	arg1	mutation					764:771	the Sox2 S248A point mutation	743:771	the Sox2 S248A point mutation	743:771	ESCs in which wild-type Sox2 was replaced with the Sox2 T258A mutant exhibited reduced self-renewal, whereas ESCs with the Sox2 S248A point mutation did not.
34819616	2	89	theme	important	306:314	arg1	roles					316:320	important roles	306:320	important roles	306:320	Although both factors play important roles in the maintenance and differentiation of ESCs and the serine 248 (S248) and threonine 258 (T258) residues of Sox2 are modified by O-GlcNAcylation, the function of Sox2 O-GlcNAcylation is unclear.
34819616	9	90	theme	important	1650:1658	arg1	role					1660:1663	an important role	1647:1663	an important role	1647:1663	Our findings using the Sox2 T258A mutant suggest that Sox2 T258 O-GlcNAc has a positive effect on ESC self-renewal and plays an important role in the proper development of ectodermal lineage cells.
34819616	6	91	theme	downregulated	1070:1082	arg1	responsible					1122:1132	responsible	1122:1132	responsible	1122:1132	RNA sequencing analysis under self-renewal conditions showed that upregulated expression of early differentiation genes, rather than a downregulated expression of self-renewal genes, was responsible for the reduced self-renewal of E14-Sox2TA/WT cells.
34819616	6	91	theme	downregulated	1070:1082	arg1	expression					1084:1093	a downregulated expression	1068:1093	a downregulated expression of self-renewal genes	1068:1115	RNA sequencing analysis under self-renewal conditions showed that upregulated expression of early differentiation genes, rather than a downregulated expression of self-renewal genes, was responsible for the reduced self-renewal of E14-Sox2TA/WT cells.
34819616	6	92	theme	genes	1049:1053	arg1	expression					1013:1022	upregulated expression	1001:1022	upregulated expression of early differentiation genes	1001:1053	RNA sequencing analysis under self-renewal conditions showed that upregulated expression of early differentiation genes, rather than a downregulated expression of self-renewal genes, was responsible for the reduced self-renewal of E14-Sox2TA/WT cells.
34819616	8	93	link	E14-Sox2TA/WT-derived	1489:1509	arg1	teratomas					1511:1519	the E14-Sox2TA/WT-derived teratomas	1485:1519	the E14-Sox2TA/WT-derived teratomas	1485:1519	RNA sequencing of teratomas revealed that genes related to brain development had generally downregulated expression in the E14-Sox2TA/WT-derived teratomas.
31281487	2	0	from	instrumental	404:415	arg1	phenomena					437:445	these recurrence phenomena	420:445	these recurrence phenomena	420:445	Aberrant upregulation in the transcriptional activity of proteins involved in self-renewal like Sox2, Oct4 and Nanog is instrumental in these recurrence phenomena.
31281487	2	1	theme	proteins	341:348	arg1	activity					329:336	the transcriptional activity	309:336	the transcriptional activity of proteins involved in self-renewal like Sox2, Oct4 and Nanog	309:399	Aberrant upregulation in the transcriptional activity of proteins involved in self-renewal like Sox2, Oct4 and Nanog is instrumental in these recurrence phenomena.
31281487	5	2	theme	Sox2	713:716	arg1	glycosylation					696:708	glycosylation	696:708	glycosylation of Sox2 by O-GlcNAc transferase (OGT)	696:746	In the current study, we have studied the how glycosylation of Sox2 by O-GlcNAc transferase (OGT) can affect its transcriptional activity and thus regulate self-renewal in cancer.
31281487	9	3	theme	first	1221:1225	arg1	time					1227:1230	the first time	1217:1230	the first time	1217:1230	Results: Our study shows for the first time that in PDAC, glycosylation of Sox2 by OGT stabilizes it in the nucleus.
31281487	10	4	theme	Site	1305:1308	arg1	mutagenesis					1319:1329	Site directed mutagenesis	1305:1329	Site directed mutagenesis of this site (S246A)	1305:1350	Site directed mutagenesis of this site (S246A) prevents this modification.
31281487	3	5	theme	turned-on	479:487	arg1	"					488:488	"turned-on"	478:488	"turned-on" leading to activation of downstream genes those results in relapse of the tumor	478:568	In cancer, Sox2 is aberrantly "turned-on" leading to activation of downstream genes those results in relapse of the tumor.
31281487	2	6	from	upregulation	293:304	arg1	activity					329:336	the transcriptional activity	309:336	the transcriptional activity of proteins involved in self-renewal like Sox2, Oct4 and Nanog	309:399	Aberrant upregulation in the transcriptional activity of proteins involved in self-renewal like Sox2, Oct4 and Nanog is instrumental in these recurrence phenomena.
31281487	7	7	theme	PDAC	1103:1106	arg1	cells					1108:1112	PDAC cells	1103:1112	PDAC cells	1103:1112	Pancreatic tumor burden following inhibition of OGT in vivo was done by using small molecule inhibitor, OSMI, on subcutaneous implantation of PDAC cells.
31281487	6	8	theme	RNA-Seq	839:845	arg1	analysis					847:854	RNA-Seq analysis	839:854	RNA-Seq analysis of CRISPR-OGTi PDAC cells	839:880	Methods: RNA-Seq analysis of CRISPR-OGTi PDAC cells indicated a deregulation of differentiation and self-renewal pathways in PDAC.
31281487	5	9	from	cancer	822:827	arg1	self-renewal					806:817	self-renewal	806:817	self-renewal	806:817	In the current study, we have studied the how glycosylation of Sox2 by O-GlcNAc transferase (OGT) can affect its transcriptional activity and thus regulate self-renewal in cancer.
31281487	5	10	gly	glycosylation	696:708	arg1	Sox2					713:716	Sox2	713:716	Sox2	713:716	In the current study, we have studied the how glycosylation of Sox2 by O-GlcNAc transferase (OGT) can affect its transcriptional activity and thus regulate self-renewal in cancer.
31281487	12	11	theme	tumor	1581:1585	arg1	burden					1587:1592	decreased tumor burden	1571:1592	decreased tumor burden in PDAC	1571:1600	We also show that targeting OGT in vivo with a small molecule-inhibitor OSMI, results in decreased tumor burden in PDAC.
31281487	6	12	theme	pathways	943:950	arg1	deregulation					894:905	a deregulation	892:905	a deregulation of differentiation and self-renewal pathways in PDAC	892:958	Methods: RNA-Seq analysis of CRISPR-OGTi PDAC cells indicated a deregulation of differentiation and self-renewal pathways in PDAC.
31281487	12	13	dep	results	1560:1566	arg1	targeting					1500:1508	targeting	1500:1508	targeting OGT in vivo with a small molecule-inhibitor OSMI	1500:1557	We also show that targeting OGT in vivo with a small molecule-inhibitor OSMI, results in decreased tumor burden in PDAC.
31281487	9	14	gly	glycosylation	1246:1258	arg1	Sox2					1263:1266	Sox2	1263:1266	Sox2	1263:1266	Results: Our study shows for the first time that in PDAC, glycosylation of Sox2 by OGT stabilizes it in the nucleus.
31281487	3	15	from	"	488:488	arg1	cancer					451:456	cancer	451:456	cancer	451:456	In cancer, Sox2 is aberrantly "turned-on" leading to activation of downstream genes those results in relapse of the tumor.
31281487	3	16	theme	downstream	515:524	arg1	genes					526:530	downstream genes	515:530	downstream genes	515:530	In cancer, Sox2 is aberrantly "turned-on" leading to activation of downstream genes those results in relapse of the tumor.
31281487	13	17	theme	therapy	1737:1743	arg1	development					1716:1726	development	1716:1726	development of novel therapy	1716:1743	Conclusion: Understanding this mechanism of SOX2 regulation by its glycosylation is expected to pave the way for development of novel therapy that has the potential to eradicate the cells responsible for tumor-recurrence.
31281487	6	18	theme	self-renewal	930:941	arg1	pathways					943:950	differentiation and self-renewal pathways	910:950	differentiation and self-renewal pathways	910:950	Methods: RNA-Seq analysis of CRISPR-OGTi PDAC cells indicated a deregulation of differentiation and self-renewal pathways in PDAC.
31281487	8	19	theme	Sox2	1115:1118	arg1	assay					1129:1133	Sox2 activity assay	1115:1133	Sox2 activity assay	1115:1133	Sox2 activity assay was performed by Dual Luciferase Reporter Assay kit.
31281487	2	20	from	phenomena	437:445	arg1	instrumental					404:415	instrumental	404:415	instrumental	404:415	Aberrant upregulation in the transcriptional activity of proteins involved in self-renewal like Sox2, Oct4 and Nanog is instrumental in these recurrence phenomena.
31281487	7	21	theme	small	1039:1043	arg1	OSMI					1065:1068	OSMI	1065:1068	OSMI	1065:1068	Pancreatic tumor burden following inhibition of OGT in vivo was done by using small molecule inhibitor, OSMI, on subcutaneous implantation of PDAC cells.
31281487	7	21	theme	small	1039:1043	arg1	inhibitor					1054:1062	small molecule inhibitor	1039:1062	small molecule inhibitor	1039:1062	Pancreatic tumor burden following inhibition of OGT in vivo was done by using small molecule inhibitor, OSMI, on subcutaneous implantation of PDAC cells.
31281487	12	22	theme	molecule-inhibitor	1535:1552	arg1	OSMI					1554:1557	a small molecule-inhibitor OSMI	1527:1557	a small molecule-inhibitor OSMI	1527:1557	We also show that targeting OGT in vivo with a small molecule-inhibitor OSMI, results in decreased tumor burden in PDAC.
31281487	8	23	theme	Luciferase	1157:1166	arg1	kit					1183:1185	Dual Luciferase Reporter Assay kit	1152:1185	Dual Luciferase Reporter Assay kit	1152:1185	Sox2 activity assay was performed by Dual Luciferase Reporter Assay kit.
31281487	7	24	theme	molecule	1045:1052	arg1	OSMI					1065:1068	OSMI	1065:1068	OSMI	1065:1068	Pancreatic tumor burden following inhibition of OGT in vivo was done by using small molecule inhibitor, OSMI, on subcutaneous implantation of PDAC cells.
31281487	7	24	theme	molecule	1045:1052	arg1	inhibitor					1054:1062	small molecule inhibitor	1039:1062	small molecule inhibitor	1039:1062	Pancreatic tumor burden following inhibition of OGT in vivo was done by using small molecule inhibitor, OSMI, on subcutaneous implantation of PDAC cells.
31281487	8	25	theme	activity	1120:1127	arg1	assay					1129:1133	Sox2 activity assay	1115:1133	Sox2 activity assay	1115:1133	Sox2 activity assay was performed by Dual Luciferase Reporter Assay kit.
31281487	4	26	theme	Sox2	622:625	arg1	activity					610:617	the activity	606:617	the activity of Sox2 in PDAC	606:633	Molecular mechanisms that regulate the activity of Sox2 in PDAC are not known.
31281487	2	27	theme	recurrence	426:435	arg1	phenomena					437:445	these recurrence phenomena	420:445	these recurrence phenomena	420:445	Aberrant upregulation in the transcriptional activity of proteins involved in self-renewal like Sox2, Oct4 and Nanog is instrumental in these recurrence phenomena.
31281487	1	28	theme	tumor	266:270	arg1	recurrence					272:281	tumor recurrence	266:281	tumor recurrence	266:281	Pancreatic adenocarcinoma (PDAC) claims more than 90% of the patients diagnosed with the disease owing to its aggressive biology that is manifested by high rate of tumor recurrence.
31281487	10	29	theme	site	1339:1342	arg1	mutagenesis					1319:1329	Site directed mutagenesis	1305:1329	Site directed mutagenesis of this site (S246A)	1305:1350	Site directed mutagenesis of this site (S246A) prevents this modification.
31281487	1	30	theme	patients	163:170	arg1	patients					163:170	the patients	159:170	the patients diagnosed with the disease owing to its aggressive biology that is manifested by high rate of tumor recurrence	159:281	Pancreatic adenocarcinoma (PDAC) claims more than 90% of the patients diagnosed with the disease owing to its aggressive biology that is manifested by high rate of tumor recurrence.
31281487	1	30	theme	patients	163:170	arg1	%					154:154	more than 90%	142:154	more than 90% of the patients diagnosed with the disease owing to its aggressive biology that is manifested by high rate of tumor recurrence	142:281	Pancreatic adenocarcinoma (PDAC) claims more than 90% of the patients diagnosed with the disease owing to its aggressive biology that is manifested by high rate of tumor recurrence.
31281487	0	31	theme	O-GlcNAc	0:7	arg1	modification					9:20	O-GlcNAc modification	0:20	O-GlcNAc modification of Sox2	0:28	O-GlcNAc modification of Sox2 regulates self-renewal in pancreatic cancer by promoting its stability.
31281487	1	32	theme	high	253:256	arg1	rate					258:261	high rate	253:261	high rate of tumor recurrence	253:281	Pancreatic adenocarcinoma (PDAC) claims more than 90% of the patients diagnosed with the disease owing to its aggressive biology that is manifested by high rate of tumor recurrence.
31281487	2	33	theme	Aberrant	284:291	arg1	upregulation					293:304	Aberrant upregulation	284:304	Aberrant upregulation in the transcriptional activity of proteins involved in self-renewal like Sox2, Oct4 and Nanog	284:399	Aberrant upregulation in the transcriptional activity of proteins involved in self-renewal like Sox2, Oct4 and Nanog is instrumental in these recurrence phenomena.
31281487	13	34	theme	responsible	1791:1801	arg1	cells					1785:1789	the cells	1781:1789	the cells responsible for tumor-recurrence	1781:1822	Conclusion: Understanding this mechanism of SOX2 regulation by its glycosylation is expected to pave the way for development of novel therapy that has the potential to eradicate the cells responsible for tumor-recurrence.
31281487	0	35	theme	Sox2	25:28	arg1	modification					9:20	O-GlcNAc modification	0:20	O-GlcNAc modification of Sox2	0:28	O-GlcNAc modification of Sox2 regulates self-renewal in pancreatic cancer by promoting its stability.
31281487	6	36	theme	differentiation	910:924	arg1	pathways					943:950	differentiation and self-renewal pathways	910:950	differentiation and self-renewal pathways	910:950	Methods: RNA-Seq analysis of CRISPR-OGTi PDAC cells indicated a deregulation of differentiation and self-renewal pathways in PDAC.
31281487	10	37	theme	directed	1310:1317	arg1	mutagenesis					1319:1329	Site directed mutagenesis	1305:1329	Site directed mutagenesis of this site (S246A)	1305:1350	Site directed mutagenesis of this site (S246A) prevents this modification.
31281487	3	38	theme	genes	526:530	arg1	activation					501:510	activation	501:510	activation of downstream genes those results in relapse of the tumor	501:568	In cancer, Sox2 is aberrantly "turned-on" leading to activation of downstream genes those results in relapse of the tumor.
31281487	4	39	from	activity	610:617	arg1	PDAC					630:633	PDAC	630:633	PDAC	630:633	Molecular mechanisms that regulate the activity of Sox2 in PDAC are not known.
31281487	7	40	theme	cells	1108:1112	arg1	implantation					1087:1098	subcutaneous implantation	1074:1098	subcutaneous implantation of PDAC cells	1074:1112	Pancreatic tumor burden following inhibition of OGT in vivo was done by using small molecule inhibitor, OSMI, on subcutaneous implantation of PDAC cells.
31281487	9	41	theme	Sox2	1263:1266	arg1	glycosylation					1246:1258	glycosylation	1246:1258	glycosylation of Sox2 by OGT	1246:1273	Results: Our study shows for the first time that in PDAC, glycosylation of Sox2 by OGT stabilizes it in the nucleus.
31281487	5	42	theme	current	657:663	arg1	study					665:669	the current study	653:669	the current study	653:669	In the current study, we have studied the how glycosylation of Sox2 by O-GlcNAc transferase (OGT) can affect its transcriptional activity and thus regulate self-renewal in cancer.
31281487	6	43	from	deregulation	894:905	arg1	PDAC					955:958	PDAC	955:958	PDAC	955:958	Methods: RNA-Seq analysis of CRISPR-OGTi PDAC cells indicated a deregulation of differentiation and self-renewal pathways in PDAC.
31281487	5	44	theme	transcriptional	763:777	arg1	activity					779:786	its transcriptional activity	759:786	its transcriptional activity	759:786	In the current study, we have studied the how glycosylation of Sox2 by O-GlcNAc transferase (OGT) can affect its transcriptional activity and thus regulate self-renewal in cancer.
31281487	8	45	theme	Dual	1152:1155	arg1	kit					1183:1185	Dual Luciferase Reporter Assay kit	1152:1185	Dual Luciferase Reporter Assay kit	1152:1185	Sox2 activity assay was performed by Dual Luciferase Reporter Assay kit.
31281487	3	46	dep	activation	501:510	arg1	results					538:544	results	538:544	results in relapse of the tumor	538:568	In cancer, Sox2 is aberrantly "turned-on" leading to activation of downstream genes those results in relapse of the tumor.
31281487	7	47	theme	in	1013:1014	arg1	inhibition					995:1004	inhibition	995:1004	inhibition of OGT in vivo	995:1019	Pancreatic tumor burden following inhibition of OGT in vivo was done by using small molecule inhibitor, OSMI, on subcutaneous implantation of PDAC cells.
31281487	13	48	contain	has	1750:1752	arg2	potential					1758:1766	the potential to eradicate the cells responsible for tumor-recurrence	1754:1822	the potential to eradicate the cells responsible for tumor-recurrence	1754:1822	Conclusion: Understanding this mechanism of SOX2 regulation by its glycosylation is expected to pave the way for development of novel therapy that has the potential to eradicate the cells responsible for tumor-recurrence.
31281487	13	48	contain	has	1750:1752	arg1	way					1708:1710	the way	1704:1710	the way for development of novel therapy that has the potential to eradicate the cells responsible for tumor-recurrence	1704:1822	Conclusion: Understanding this mechanism of SOX2 regulation by its glycosylation is expected to pave the way for development of novel therapy that has the potential to eradicate the cells responsible for tumor-recurrence.
31281487	13	49	theme	novel	1731:1735	arg1	therapy					1737:1743	novel therapy	1731:1743	novel therapy	1731:1743	Conclusion: Understanding this mechanism of SOX2 regulation by its glycosylation is expected to pave the way for development of novel therapy that has the potential to eradicate the cells responsible for tumor-recurrence.
31281487	11	50	theme	tumors	1452:1457	arg1	initiation					1427:1436	initiation	1427:1436	initiation of pancreatic tumors	1427:1457	We further show that inhibition of OGT delayed initiation of pancreatic tumors by inhibition of Sox2.
31281487	5	51	theme	O-GlcNAc	721:728	arg1	transferase					730:740	O-GlcNAc transferase	721:740	O-GlcNAc transferase (OGT)	721:746	In the current study, we have studied the how glycosylation of Sox2 by O-GlcNAc transferase (OGT) can affect its transcriptional activity and thus regulate self-renewal in cancer.
31281487	5	51	theme	O-GlcNAc	721:728	arg1	OGT					743:745	OGT	743:745	OGT	743:745	In the current study, we have studied the how glycosylation of Sox2 by O-GlcNAc transferase (OGT) can affect its transcriptional activity and thus regulate self-renewal in cancer.
31281487	1	52	theme	recurrence	272:281	arg1	rate					258:261	high rate	253:261	high rate of tumor recurrence	253:281	Pancreatic adenocarcinoma (PDAC) claims more than 90% of the patients diagnosed with the disease owing to its aggressive biology that is manifested by high rate of tumor recurrence.
31281487	11	53	theme	pancreatic	1441:1450	arg1	tumors					1452:1457	pancreatic tumors	1441:1457	pancreatic tumors	1441:1457	We further show that inhibition of OGT delayed initiation of pancreatic tumors by inhibition of Sox2.
31281487	3	54	theme	tumor	564:568	arg1	relapse					549:555	relapse	549:555	relapse of the tumor	549:568	In cancer, Sox2 is aberrantly "turned-on" leading to activation of downstream genes those results in relapse of the tumor.
31281487	7	55	theme	tumor	972:976	arg1	burden					978:983	Pancreatic tumor burden	961:983	Pancreatic tumor burden following inhibition of OGT in vivo	961:1019	Pancreatic tumor burden following inhibition of OGT in vivo was done by using small molecule inhibitor, OSMI, on subcutaneous implantation of PDAC cells.
31281487	0	56	theme	pancreatic	56:65	arg1	cancer					67:72	pancreatic cancer	56:72	pancreatic cancer	56:72	O-GlcNAc modification of Sox2 regulates self-renewal in pancreatic cancer by promoting its stability.
31281487	5	57	dep	studied	680:686	arg1	regulate					797:804	regulate	797:804	regulate self-renewal in cancer	797:827	In the current study, we have studied the how glycosylation of Sox2 by O-GlcNAc transferase (OGT) can affect its transcriptional activity and thus regulate self-renewal in cancer.
31281487	5	57	dep	studied	680:686	arg1	affect					752:757	affect	752:757	can affect its transcriptional activity	748:786	In the current study, we have studied the how glycosylation of Sox2 by O-GlcNAc transferase (OGT) can affect its transcriptional activity and thus regulate self-renewal in cancer.
31281487	7	58	theme	subcutaneous	1074:1085	arg1	implantation					1087:1098	subcutaneous implantation	1074:1098	subcutaneous implantation of PDAC cells	1074:1112	Pancreatic tumor burden following inhibition of OGT in vivo was done by using small molecule inhibitor, OSMI, on subcutaneous implantation of PDAC cells.
31281487	6	59	theme	cells	876:880	arg1	analysis					847:854	RNA-Seq analysis	839:854	RNA-Seq analysis of CRISPR-OGTi PDAC cells	839:880	Methods: RNA-Seq analysis of CRISPR-OGTi PDAC cells indicated a deregulation of differentiation and self-renewal pathways in PDAC.
31281487	7	60	theme	OGT	1009:1011	arg1	inhibition					995:1004	inhibition	995:1004	inhibition of OGT in vivo	995:1019	Pancreatic tumor burden following inhibition of OGT in vivo was done by using small molecule inhibitor, OSMI, on subcutaneous implantation of PDAC cells.
31281487	2	61	theme	transcriptional	313:327	arg1	activity					329:336	the transcriptional activity	309:336	the transcriptional activity of proteins involved in self-renewal like Sox2, Oct4 and Nanog	309:399	Aberrant upregulation in the transcriptional activity of proteins involved in self-renewal like Sox2, Oct4 and Nanog is instrumental in these recurrence phenomena.
31281487	11	62	theme	Sox2	1476:1479	arg1	inhibition					1462:1471	inhibition	1462:1471	inhibition of Sox2	1462:1479	We further show that inhibition of OGT delayed initiation of pancreatic tumors by inhibition of Sox2.
31281487	6	63	theme	PDAC	871:874	arg1	cells					876:880	CRISPR-OGTi PDAC cells	859:880	CRISPR-OGTi PDAC cells	859:880	Methods: RNA-Seq analysis of CRISPR-OGTi PDAC cells indicated a deregulation of differentiation and self-renewal pathways in PDAC.
31281487	13	64	theme	SOX2	1647:1650	arg1	regulation					1652:1661	SOX2 regulation	1647:1661	SOX2 regulation	1647:1661	Conclusion: Understanding this mechanism of SOX2 regulation by its glycosylation is expected to pave the way for development of novel therapy that has the potential to eradicate the cells responsible for tumor-recurrence.
31281487	12	65	from	burden	1587:1592	arg1	PDAC					1597:1600	PDAC	1597:1600	PDAC	1597:1600	We also show that targeting OGT in vivo with a small molecule-inhibitor OSMI, results in decreased tumor burden in PDAC.
31281487	7	66	theme	Pancreatic	961:970	arg1	burden					978:983	Pancreatic tumor burden	961:983	Pancreatic tumor burden following inhibition of OGT in vivo	961:1019	Pancreatic tumor burden following inhibition of OGT in vivo was done by using small molecule inhibitor, OSMI, on subcutaneous implantation of PDAC cells.
31281487	1	67	theme	Pancreatic	102:111	arg1	PDAC					129:132	PDAC	129:132	PDAC	129:132	Pancreatic adenocarcinoma (PDAC) claims more than 90% of the patients diagnosed with the disease owing to its aggressive biology that is manifested by high rate of tumor recurrence.
31281487	1	67	theme	Pancreatic	102:111	arg1	adenocarcinoma					113:126	Pancreatic adenocarcinoma	102:126	Pancreatic adenocarcinoma (PDAC)	102:133	Pancreatic adenocarcinoma (PDAC) claims more than 90% of the patients diagnosed with the disease owing to its aggressive biology that is manifested by high rate of tumor recurrence.
31281487	4	68	theme	Molecular	571:579	arg1	mechanisms					581:590	Molecular mechanisms	571:590	Molecular mechanisms that regulate the activity of Sox2 in PDAC	571:633	Molecular mechanisms that regulate the activity of Sox2 in PDAC are not known.
31281487	5	69	from	self-renewal	806:817	arg1	cancer					822:827	cancer	822:827	cancer	822:827	In the current study, we have studied the how glycosylation of Sox2 by O-GlcNAc transferase (OGT) can affect its transcriptional activity and thus regulate self-renewal in cancer.
31281487	7	70	dep	in	1013:1014	arg1	vivo					1016:1019	vivo	1016:1019	vivo	1016:1019	Pancreatic tumor burden following inhibition of OGT in vivo was done by using small molecule inhibitor, OSMI, on subcutaneous implantation of PDAC cells.
31281487	12	71	theme	decreased	1571:1579	arg1	burden					1587:1592	decreased tumor burden	1571:1592	decreased tumor burden in PDAC	1571:1600	We also show that targeting OGT in vivo with a small molecule-inhibitor OSMI, results in decreased tumor burden in PDAC.
31281487	8	72	theme	Assay	1177:1181	arg1	kit					1183:1185	Dual Luciferase Reporter Assay kit	1152:1185	Dual Luciferase Reporter Assay kit	1152:1185	Sox2 activity assay was performed by Dual Luciferase Reporter Assay kit.
31281487	1	73	theme	aggressive	212:221	arg1	biology					223:229	its aggressive biology	208:229	its aggressive biology that is manifested by high rate of tumor recurrence	208:281	Pancreatic adenocarcinoma (PDAC) claims more than 90% of the patients diagnosed with the disease owing to its aggressive biology that is manifested by high rate of tumor recurrence.
31281487	8	74	theme	Reporter	1168:1175	arg1	kit					1183:1185	Dual Luciferase Reporter Assay kit	1152:1185	Dual Luciferase Reporter Assay kit	1152:1185	Sox2 activity assay was performed by Dual Luciferase Reporter Assay kit.
31281487	6	75	theme	CRISPR-OGTi	859:869	arg1	cells					876:880	CRISPR-OGTi PDAC cells	859:880	CRISPR-OGTi PDAC cells	859:880	Methods: RNA-Seq analysis of CRISPR-OGTi PDAC cells indicated a deregulation of differentiation and self-renewal pathways in PDAC.
31281487	12	76	theme	small	1529:1533	arg1	OSMI					1554:1557	a small molecule-inhibitor OSMI	1527:1557	a small molecule-inhibitor OSMI	1527:1557	We also show that targeting OGT in vivo with a small molecule-inhibitor OSMI, results in decreased tumor burden in PDAC.
31281487	11	77	theme	OGT	1415:1417	arg1	inhibition					1401:1410	inhibition	1401:1410	inhibition of OGT	1401:1417	We further show that inhibition of OGT delayed initiation of pancreatic tumors by inhibition of Sox2.
31281487	13	78	theme	regulation	1652:1661	arg1	mechanism					1634:1642	this mechanism	1629:1642	this mechanism of SOX2 regulation by its glycosylation	1629:1682	Conclusion: Understanding this mechanism of SOX2 regulation by its glycosylation is expected to pave the way for development of novel therapy that has the potential to eradicate the cells responsible for tumor-recurrence.
31779679	8	0	theme	western	1149:1155	arg1	blot					1157:1160	western blot	1149:1160	western blot	1149:1160	Cartilage endplate stem cells (CESCs) were induced with low-, normal-, and high-glucose medium for 21 days, and chondrogenic and osteogenic differentiations were measured by Q-PCR, western blot, and immunohistochemical staining.
31779679	8	1	theme	endplate	978:985	arg1	CESCs					999:1003	CESCs	999:1003	CESCs	999:1003	Cartilage endplate stem cells (CESCs) were induced with low-, normal-, and high-glucose medium for 21 days, and chondrogenic and osteogenic differentiations were measured by Q-PCR, western blot, and immunohistochemical staining.
31779679	8	1	theme	endplate	978:985	arg1	cells					992:996	Cartilage endplate stem cells	968:996	Cartilage endplate stem cells (CESCs)	968:1004	Cartilage endplate stem cells (CESCs) were induced with low-, normal-, and high-glucose medium for 21 days, and chondrogenic and osteogenic differentiations were measured by Q-PCR, western blot, and immunohistochemical staining.
31779679	6	2	from	calcification	748:760	arg1	DDD					765:767	DDD	765:767	DDD	765:767	We aimed to identify the molecular mechanisms of glucose in CEP calcification in DDD.
31779679	7	3	theme	osteogenesis	878:889	arg1	effects					848:854	the effects	844:854	the effects of chondrogenesis and osteogenesis of the CEP	844:900	METHODS We assessed normal and degenerated CEP tissues from patients, and the effects of chondrogenesis and osteogenesis of the CEP were determined by western blot and immunohistochemical staining.
31779679	13	4	theme	osteogenic	1843:1852	arg1	differentiation					1854:1868	osteogenic differentiation	1843:1868	osteogenic differentiation	1843:1868	CESC chondrogenic differentiation gradually decreased while osteogenic differentiation gradually increased from low- to high-glucose differentiation medium.
31779679	12	5	contain	had	1699:1701	arg1	RESULTS					1608:1614	RESULTS	1608:1614	RESULTS Degenerated CEPs from DDD patients	1608:1649	RESULTS Degenerated CEPs from DDD patients lost chondrogenesis, acquired osteogenesis, and had higher protein O-GlcNAcylation level compared to normal CEPs from LVF patients.
31779679	12	5	contain	had	1699:1701	arg2	level					1734:1738	higher protein O-GlcNAcylation level	1703:1738	higher protein O-GlcNAcylation level	1703:1738	RESULTS Degenerated CEPs from DDD patients lost chondrogenesis, acquired osteogenesis, and had higher protein O-GlcNAcylation level compared to normal CEPs from LVF patients.
31779679	11	6	theme	Runx2	1559:1563	arg1	genes					1541:1545	the downstream genes	1526:1545	the downstream genes of Sox9 and Runx2	1526:1563	The effects of O-GlcNAcylation on the downstream genes of Sox9 and Runx2 were determined by Q-PCR and western blot.
31779679	2	7	theme	endplate	293:300	arg1	microenvironment					259:274	The physiological low-glucose microenvironment	229:274	The physiological low-glucose microenvironment of the cartilage endplate (CEP)	229:306	The physiological low-glucose microenvironment of the cartilage endplate (CEP) is disrupted in DDD.
31779679	7	8	theme	chondrogenesis	859:872	arg1	effects					848:854	the effects	844:854	the effects of chondrogenesis and osteogenesis of the CEP	844:900	METHODS We assessed normal and degenerated CEP tissues from patients, and the effects of chondrogenesis and osteogenesis of the CEP were determined by western blot and immunohistochemical staining.
31779679	8	9	theme	immunohistochemical	1167:1185	arg1	staining					1187:1194	immunohistochemical staining	1167:1194	immunohistochemical staining	1167:1194	Cartilage endplate stem cells (CESCs) were induced with low-, normal-, and high-glucose medium for 21 days, and chondrogenic and osteogenic differentiations were measured by Q-PCR, western blot, and immunohistochemical staining.
31779679	11	10	theme	western	1594:1600	arg1	blot					1602:1605	western blot	1594:1605	western blot	1594:1605	The effects of O-GlcNAcylation on the downstream genes of Sox9 and Runx2 were determined by Q-PCR and western blot.
31779679	12	11	theme	LVF	1769:1771	arg1	patients					1773:1780	LVF patients	1769:1780	LVF patients	1769:1780	RESULTS Degenerated CEPs from DDD patients lost chondrogenesis, acquired osteogenesis, and had higher protein O-GlcNAcylation level compared to normal CEPs from LVF patients.
31779679	15	12	from	CESCs	2241:2245	arg1	O-GlcNAcylated					2208:2221	O-GlcNAcylated	2208:2221	O-GlcNAcylated	2208:2221	Interestingly, we found that Sox9 and Runx2 were O-GlcNAcylated in differentiated CESCs.
31779679	5	13	theme	CEP	648:650	arg1	degeneration					652:663	CEP degeneration	648:663	CEP degeneration	648:663	Mechanisms of DDD are incompletely understood but include CEP degeneration and calcification.
31779679	9	14	theme	low-glucose	1221:1231	arg1	medium					1250:1255	low-glucose and high-glucose medium	1221:1255	medium	1250:1255	CESCs were induced with low-glucose and high-glucose medium with or without Thiamet-G or DON for 21 days, and chondrogenic and osteogenic differentiations were measured by Q-PCR, western blot, and immunohistochemical staining.
31779679	0	15	theme	Runx2	140:144	arg1	O-GlcNAcylation					112:126	O-GlcNAcylation	112:126	O-GlcNAcylation of Sox9 and Runx2	112:144	Glucose regulates tissue-specific chondro-osteogenic differentiation of human cartilage endplate stem cells via O-GlcNAcylation of Sox9 and Runx2.
31779679	9	16	theme	high-glucose	1237:1248	arg1	medium					1250:1255	low-glucose and high-glucose medium	1221:1255	medium	1250:1255	CESCs were induced with low-glucose and high-glucose medium with or without Thiamet-G or DON for 21 days, and chondrogenic and osteogenic differentiations were measured by Q-PCR, western blot, and immunohistochemical staining.
31779679	14	17	theme	CESC	1972:1975	arg1	differentiation					1988:2002	CESC osteogenic differentiation	1972:2002	CESC osteogenic differentiation	1972:2002	Furthermore, Thiamet-G promoted CESC osteogenic differentiation and inhibited chondrogenic differentiation in low-glucose differentiation medium; however, DON acted opposite role in high-glucose differentiation medium.
31779679	17	18	theme	differentiation	2472:2486	arg1	potential					2488:2496	the chondrogenic and osteogenic differentiation potential	2440:2496	the chondrogenic and osteogenic differentiation potential of CESCs	2440:2505	CONCLUSIONS Our findings demonstrate the effect of glucose concentration on regulating the chondrogenic and osteogenic differentiation potential of CESCs and provide insight into the mechanism of how glucose concentration regulates Sox9 and Runx2 O-GlcNAcylation to affect the differentiation of CESCs, which may represent a target for CEP degeneration therapy.
31779679	13	19	theme	CESC	1783:1786	arg1	differentiation					1801:1815	CESC chondrogenic differentiation	1783:1815	CESC chondrogenic differentiation	1783:1815	CESC chondrogenic differentiation gradually decreased while osteogenic differentiation gradually increased from low- to high-glucose differentiation medium.
31779679	12	20	theme	normal	1752:1757	arg1	CEPs					1759:1762	normal CEPs	1752:1762	normal CEPs from LVF patients	1752:1780	RESULTS Degenerated CEPs from DDD patients lost chondrogenesis, acquired osteogenesis, and had higher protein O-GlcNAcylation level compared to normal CEPs from LVF patients.
31779679	12	21	theme	Degenerated	1616:1626	arg1	CEPs					1628:1631	Degenerated CEPs	1616:1631	Degenerated CEPs	1616:1631	RESULTS Degenerated CEPs from DDD patients lost chondrogenesis, acquired osteogenesis, and had higher protein O-GlcNAcylation level compared to normal CEPs from LVF patients.
31779679	11	22	theme	downstream	1530:1539	arg1	genes					1541:1545	the downstream genes	1526:1545	the downstream genes of Sox9 and Runx2	1526:1563	The effects of O-GlcNAcylation on the downstream genes of Sox9 and Runx2 were determined by Q-PCR and western blot.
31779679	0	23	theme	endplate	88:95	arg1	cells					102:106	human cartilage endplate stem cells	72:106	human cartilage endplate stem cells	72:106	Glucose regulates tissue-specific chondro-osteogenic differentiation of human cartilage endplate stem cells via O-GlcNAcylation of Sox9 and Runx2.
31779679	17	24	theme	CESCs	2649:2653	arg1	differentiation					2630:2644	the differentiation	2626:2644	the differentiation of CESCs, which may represent a target for CEP degeneration therapy	2626:2712	CONCLUSIONS Our findings demonstrate the effect of glucose concentration on regulating the chondrogenic and osteogenic differentiation potential of CESCs and provide insight into the mechanism of how glucose concentration regulates Sox9 and Runx2 O-GlcNAcylation to affect the differentiation of CESCs, which may represent a target for CEP degeneration therapy.
31779679	2	25	theme	physiological	233:245	arg1	microenvironment					259:274	The physiological low-glucose microenvironment	229:274	The physiological low-glucose microenvironment of the cartilage endplate (CEP)	229:306	The physiological low-glucose microenvironment of the cartilage endplate (CEP) is disrupted in DDD.
31779679	1	26	theme	disc	175:178	arg1	cause					205:209	a major cause	197:209	a major cause of low back pain	197:226	BACKGROUND The degenerative disc disease (DDD) is a major cause of low back pain.
31779679	1	26	theme	disc	175:178	arg1	DDD					189:191	DDD	189:191	DDD	189:191	BACKGROUND The degenerative disc disease (DDD) is a major cause of low back pain.
31779679	1	26	theme	disc	175:178	arg1	disease					180:186	The degenerative disc disease	158:186	The degenerative disc disease (DDD)	158:192	BACKGROUND The degenerative disc disease (DDD) is a major cause of low back pain.
31779679	12	27	theme	O-GlcNAcylation	1718:1732	arg1	level					1734:1738	higher protein O-GlcNAcylation level	1703:1738	higher protein O-GlcNAcylation level	1703:1738	RESULTS Degenerated CEPs from DDD patients lost chondrogenesis, acquired osteogenesis, and had higher protein O-GlcNAcylation level compared to normal CEPs from LVF patients.
31779679	0	28	theme	cells	102:106	arg1	differentiation					53:67	tissue-specific chondro-osteogenic differentiation	18:67	tissue-specific chondro-osteogenic differentiation of human cartilage endplate stem cells	18:106	Glucose regulates tissue-specific chondro-osteogenic differentiation of human cartilage endplate stem cells via O-GlcNAcylation of Sox9 and Runx2.
31779679	4	29	theme	O-GlcNAcase	484:494	arg1	Thiamet-G					455:463	Thiamet-G	455:463	Thiamet-G	455:463	Thiamet-G is an inhibitor of O-GlcNAcase for accumulating O-GlcNAcylated proteins while 6-diazo-5-oxo-L-norleucine (DON) inhibits HBP.
31779679	4	29	theme	O-GlcNAcase	484:494	arg1	inhibitor					471:479	an inhibitor	468:479	an inhibitor of O-GlcNAcase for accumulating O-GlcNAcylated proteins	468:535	Thiamet-G is an inhibitor of O-GlcNAcase for accumulating O-GlcNAcylated proteins while 6-diazo-5-oxo-L-norleucine (DON) inhibits HBP.
31779679	1	30	dep	BACKGROUND	147:156	arg1	cause					205:209	a major cause	197:209	a major cause of low back pain	197:226	BACKGROUND The degenerative disc disease (DDD) is a major cause of low back pain.
31779679	1	30	dep	BACKGROUND	147:156	arg1	disease					180:186	The degenerative disc disease	158:186	The degenerative disc disease (DDD)	158:192	BACKGROUND The degenerative disc disease (DDD) is a major cause of low back pain.
31779679	9	31	theme	chondrogenic	1307:1318	arg1	differentiations					1335:1350	chondrogenic and osteogenic differentiations	1307:1350	chondrogenic and osteogenic differentiations	1307:1350	CESCs were induced with low-glucose and high-glucose medium with or without Thiamet-G or DON for 21 days, and chondrogenic and osteogenic differentiations were measured by Q-PCR, western blot, and immunohistochemical staining.
31779679	0	32	theme	Sox9	131:134	arg1	O-GlcNAcylation					112:126	O-GlcNAcylation	112:126	O-GlcNAcylation of Sox9 and Runx2	112:144	Glucose regulates tissue-specific chondro-osteogenic differentiation of human cartilage endplate stem cells via O-GlcNAcylation of Sox9 and Runx2.
31779679	9	33	theme	osteogenic	1324:1333	arg1	differentiations					1335:1350	chondrogenic and osteogenic differentiations	1307:1350	chondrogenic and osteogenic differentiations	1307:1350	CESCs were induced with low-glucose and high-glucose medium with or without Thiamet-G or DON for 21 days, and chondrogenic and osteogenic differentiations were measured by Q-PCR, western blot, and immunohistochemical staining.
31779679	8	34	theme	high-glucose	1043:1054	arg1	medium					1056:1061	high-glucose medium	1043:1061	high-glucose medium	1043:1061	Cartilage endplate stem cells (CESCs) were induced with low-, normal-, and high-glucose medium for 21 days, and chondrogenic and osteogenic differentiations were measured by Q-PCR, western blot, and immunohistochemical staining.
31779679	7	35	theme	immunohistochemical	938:956	arg1	staining					958:965	immunohistochemical staining	938:965	immunohistochemical staining	938:965	METHODS We assessed normal and degenerated CEP tissues from patients, and the effects of chondrogenesis and osteogenesis of the CEP were determined by western blot and immunohistochemical staining.
31779679	14	36	theme	differentiation	2135:2149	arg1	medium					2151:2156	high-glucose differentiation medium	2122:2156	high-glucose differentiation medium	2122:2156	Furthermore, Thiamet-G promoted CESC osteogenic differentiation and inhibited chondrogenic differentiation in low-glucose differentiation medium; however, DON acted opposite role in high-glucose differentiation medium.
31779679	12	37	theme	higher	1703:1708	arg1	level					1734:1738	higher protein O-GlcNAcylation level	1703:1738	higher protein O-GlcNAcylation level	1703:1738	RESULTS Degenerated CEPs from DDD patients lost chondrogenesis, acquired osteogenesis, and had higher protein O-GlcNAcylation level compared to normal CEPs from LVF patients.
31779679	3	38	theme	biosynthetic	391:402	arg1	key					432:434	key	432:434	key	432:434	Glucose influences protein O-GlcNAcylation via the hexosamine biosynthetic pathway (HBP), which is the key to stem cell fate.
31779679	3	38	theme	biosynthetic	391:402	arg1	HBP					413:415	HBP	413:415	HBP	413:415	Glucose influences protein O-GlcNAcylation via the hexosamine biosynthetic pathway (HBP), which is the key to stem cell fate.
31779679	3	38	theme	biosynthetic	391:402	arg1	pathway					404:410	the hexosamine biosynthetic pathway	376:410	the hexosamine biosynthetic pathway (HBP)	376:416	Glucose influences protein O-GlcNAcylation via the hexosamine biosynthetic pathway (HBP), which is the key to stem cell fate.
31779679	13	39	theme	differentiation	1916:1930	arg1	medium					1932:1937	high-glucose differentiation medium	1903:1937	high-glucose differentiation medium	1903:1937	CESC chondrogenic differentiation gradually decreased while osteogenic differentiation gradually increased from low- to high-glucose differentiation medium.
31779679	3	40	theme	cell	444:447	arg1	fate					449:452	stem cell fate	439:452	stem cell fate	439:452	Glucose influences protein O-GlcNAcylation via the hexosamine biosynthetic pathway (HBP), which is the key to stem cell fate.
31779679	0	41	theme	tissue-specific	18:32	arg1	differentiation					53:67	tissue-specific chondro-osteogenic differentiation	18:67	tissue-specific chondro-osteogenic differentiation of human cartilage endplate stem cells	18:106	Glucose regulates tissue-specific chondro-osteogenic differentiation of human cartilage endplate stem cells via O-GlcNAcylation of Sox9 and Runx2.
31779679	7	42	theme	degenerated	801:811	arg1	tissues					817:823	normal and degenerated CEP tissues	790:823	normal and degenerated CEP tissues from patients	790:837	METHODS We assessed normal and degenerated CEP tissues from patients, and the effects of chondrogenesis and osteogenesis of the CEP were determined by western blot and immunohistochemical staining.
31779679	14	43	theme	opposite	2105:2112	arg1	role					2114:2117	opposite role	2105:2117	opposite role	2105:2117	Furthermore, Thiamet-G promoted CESC osteogenic differentiation and inhibited chondrogenic differentiation in low-glucose differentiation medium; however, DON acted opposite role in high-glucose differentiation medium.
31779679	7	44	from	patients	830:837	arg1	tissues					817:823	normal and degenerated CEP tissues	790:823	normal and degenerated CEP tissues from patients	790:837	METHODS We assessed normal and degenerated CEP tissues from patients, and the effects of chondrogenesis and osteogenesis of the CEP were determined by western blot and immunohistochemical staining.
31779679	7	45	theme	normal	790:795	arg1	tissues					817:823	normal and degenerated CEP tissues	790:823	normal and degenerated CEP tissues from patients	790:837	METHODS We assessed normal and degenerated CEP tissues from patients, and the effects of chondrogenesis and osteogenesis of the CEP were determined by western blot and immunohistochemical staining.
31779679	8	46	theme	chondrogenic	1080:1091	arg1	differentiations					1108:1123	chondrogenic and osteogenic differentiations	1080:1123	chondrogenic and osteogenic differentiations	1080:1123	Cartilage endplate stem cells (CESCs) were induced with low-, normal-, and high-glucose medium for 21 days, and chondrogenic and osteogenic differentiations were measured by Q-PCR, western blot, and immunohistochemical staining.
31779679	4	47	theme	accumulating	500:511	arg1	proteins					528:535	accumulating O-GlcNAcylated proteins	500:535	accumulating O-GlcNAcylated proteins	500:535	Thiamet-G is an inhibitor of O-GlcNAcase for accumulating O-GlcNAcylated proteins while 6-diazo-5-oxo-L-norleucine (DON) inhibits HBP.
31779679	0	48	theme	human	72:76	arg1	cells					102:106	human cartilage endplate stem cells	72:106	human cartilage endplate stem cells	72:106	Glucose regulates tissue-specific chondro-osteogenic differentiation of human cartilage endplate stem cells via O-GlcNAcylation of Sox9 and Runx2.
31779679	8	49	theme	osteogenic	1097:1106	arg1	differentiations					1108:1123	chondrogenic and osteogenic differentiations	1080:1123	chondrogenic and osteogenic differentiations	1080:1123	Cartilage endplate stem cells (CESCs) were induced with low-, normal-, and high-glucose medium for 21 days, and chondrogenic and osteogenic differentiations were measured by Q-PCR, western blot, and immunohistochemical staining.
31779679	7	50	theme	western	921:927	arg1	blot					929:932	western blot	921:932	western blot	921:932	METHODS We assessed normal and degenerated CEP tissues from patients, and the effects of chondrogenesis and osteogenesis of the CEP were determined by western blot and immunohistochemical staining.
31779679	8	51	theme	Cartilage	968:976	arg1	CESCs					999:1003	CESCs	999:1003	CESCs	999:1003	Cartilage endplate stem cells (CESCs) were induced with low-, normal-, and high-glucose medium for 21 days, and chondrogenic and osteogenic differentiations were measured by Q-PCR, western blot, and immunohistochemical staining.
31779679	8	51	theme	Cartilage	968:976	arg1	cells					992:996	Cartilage endplate stem cells	968:996	Cartilage endplate stem cells (CESCs)	968:1004	Cartilage endplate stem cells (CESCs) were induced with low-, normal-, and high-glucose medium for 21 days, and chondrogenic and osteogenic differentiations were measured by Q-PCR, western blot, and immunohistochemical staining.
31779679	6	52	theme	CEP	744:746	arg1	calcification					748:760	CEP calcification	744:760	CEP calcification in DDD	744:767	We aimed to identify the molecular mechanisms of glucose in CEP calcification in DDD.
31779679	14	53	theme	low-glucose	2050:2060	arg1	medium					2078:2083	low-glucose differentiation medium	2050:2083	low-glucose differentiation medium	2050:2083	Furthermore, Thiamet-G promoted CESC osteogenic differentiation and inhibited chondrogenic differentiation in low-glucose differentiation medium; however, DON acted opposite role in high-glucose differentiation medium.
31779679	8	54	theme	stem	987:990	arg1	CESCs					999:1003	CESCs	999:1003	CESCs	999:1003	Cartilage endplate stem cells (CESCs) were induced with low-, normal-, and high-glucose medium for 21 days, and chondrogenic and osteogenic differentiations were measured by Q-PCR, western blot, and immunohistochemical staining.
31779679	8	54	theme	stem	987:990	arg1	cells					992:996	Cartilage endplate stem cells	968:996	Cartilage endplate stem cells (CESCs)	968:1004	Cartilage endplate stem cells (CESCs) were induced with low-, normal-, and high-glucose medium for 21 days, and chondrogenic and osteogenic differentiations were measured by Q-PCR, western blot, and immunohistochemical staining.
31779679	16	55	theme	Sox9	2276:2279	arg1	O-GlcNAcylation					2257:2271	O-GlcNAcylation	2257:2271	O-GlcNAcylation of Sox9 and Runx2	2257:2289	Finally, O-GlcNAcylation of Sox9 and Runx2 decreased chondrogenesis and increased osteogenesis in CESCs.
31779679	17	56	theme	degeneration	2693:2704	arg1	therapy					2706:2712	CEP degeneration therapy	2689:2712	CEP degeneration therapy	2689:2712	CONCLUSIONS Our findings demonstrate the effect of glucose concentration on regulating the chondrogenic and osteogenic differentiation potential of CESCs and provide insight into the mechanism of how glucose concentration regulates Sox9 and Runx2 O-GlcNAcylation to affect the differentiation of CESCs, which may represent a target for CEP degeneration therapy.
31779679	6	57	theme	glucose	733:739	arg1	mechanisms					719:728	the molecular mechanisms	705:728	the molecular mechanisms of glucose in CEP calcification in DDD	705:767	We aimed to identify the molecular mechanisms of glucose in CEP calcification in DDD.
31779679	7	58	theme	CEP	898:900	arg1	osteogenesis					878:889	osteogenesis	878:889	osteogenesis	878:889	METHODS We assessed normal and degenerated CEP tissues from patients, and the effects of chondrogenesis and osteogenesis of the CEP were determined by western blot and immunohistochemical staining.
31779679	7	58	theme	CEP	898:900	arg1	chondrogenesis					859:872	chondrogenesis	859:872	chondrogenesis	859:872	METHODS We assessed normal and degenerated CEP tissues from patients, and the effects of chondrogenesis and osteogenesis of the CEP were determined by western blot and immunohistochemical staining.
31779679	15	59	from	O-GlcNAcylated	2208:2221	arg1	CESCs					2241:2245	differentiated CESCs	2226:2245	differentiated CESCs	2226:2245	Interestingly, we found that Sox9 and Runx2 were O-GlcNAcylated in differentiated CESCs.
31779679	17	60	theme	glucose	2553:2559	arg1	concentration					2561:2573	glucose concentration	2553:2573	glucose concentration	2553:2573	CONCLUSIONS Our findings demonstrate the effect of glucose concentration on regulating the chondrogenic and osteogenic differentiation potential of CESCs and provide insight into the mechanism of how glucose concentration regulates Sox9 and Runx2 O-GlcNAcylation to affect the differentiation of CESCs, which may represent a target for CEP degeneration therapy.
31779679	17	61	dep	CONCLUSIONS	2353:2363	arg1	provide					2511:2517	provide	2511:2517	provide insight into the mechanism of how glucose concentration regulates Sox9 and Runx2 O-GlcNAcylation to affect the differentiation of CESCs, which may represent a target for CEP degeneration therapy	2511:2712	CONCLUSIONS Our findings demonstrate the effect of glucose concentration on regulating the chondrogenic and osteogenic differentiation potential of CESCs and provide insight into the mechanism of how glucose concentration regulates Sox9 and Runx2 O-GlcNAcylation to affect the differentiation of CESCs, which may represent a target for CEP degeneration therapy.
31779679	17	61	dep	CONCLUSIONS	2353:2363	arg1	demonstrate					2378:2388	demonstrate	2378:2388	demonstrate the effect of glucose concentration on regulating the chondrogenic and osteogenic differentiation potential of CESCs	2378:2505	CONCLUSIONS Our findings demonstrate the effect of glucose concentration on regulating the chondrogenic and osteogenic differentiation potential of CESCs and provide insight into the mechanism of how glucose concentration regulates Sox9 and Runx2 O-GlcNAcylation to affect the differentiation of CESCs, which may represent a target for CEP degeneration therapy.
31779679	2	62	theme	cartilage	283:291	arg1	endplate					293:300	the cartilage endplate	279:300	the cartilage endplate (CEP)	279:306	The physiological low-glucose microenvironment of the cartilage endplate (CEP) is disrupted in DDD.
31779679	2	62	theme	cartilage	283:291	arg1	CEP					303:305	CEP	303:305	CEP	303:305	The physiological low-glucose microenvironment of the cartilage endplate (CEP) is disrupted in DDD.
31779679	6	63	from	mechanisms	719:728	arg1	calcification					748:760	CEP calcification	744:760	CEP calcification in DDD	744:767	We aimed to identify the molecular mechanisms of glucose in CEP calcification in DDD.
31779679	13	64	theme	chondrogenic	1788:1799	arg1	differentiation					1801:1815	CESC chondrogenic differentiation	1783:1815	CESC chondrogenic differentiation	1783:1815	CESC chondrogenic differentiation gradually decreased while osteogenic differentiation gradually increased from low- to high-glucose differentiation medium.
31779679	10	65	theme	Runx2	1433:1437	arg1	O-GlcNAcylation					1439:1453	Runx2 O-GlcNAcylation	1433:1453	Runx2 O-GlcNAcylation	1433:1453	Sox9 and Runx2 O-GlcNAcylation were measured by immunofluorescence.
31779679	14	66	from	differentiation	2031:2045	arg1	medium					2078:2083	low-glucose differentiation medium	2050:2083	low-glucose differentiation medium	2050:2083	Furthermore, Thiamet-G promoted CESC osteogenic differentiation and inhibited chondrogenic differentiation in low-glucose differentiation medium; however, DON acted opposite role in high-glucose differentiation medium.
31779679	14	67	theme	chondrogenic	2018:2029	arg1	differentiation					2031:2045	chondrogenic differentiation	2018:2045	chondrogenic differentiation in low-glucose differentiation medium	2018:2083	Furthermore, Thiamet-G promoted CESC osteogenic differentiation and inhibited chondrogenic differentiation in low-glucose differentiation medium; however, DON acted opposite role in high-glucose differentiation medium.
31779679	12	68	theme	DDD	1638:1640	arg1	patients					1642:1649	DDD patients	1638:1649	DDD patients	1638:1649	RESULTS Degenerated CEPs from DDD patients lost chondrogenesis, acquired osteogenesis, and had higher protein O-GlcNAcylation level compared to normal CEPs from LVF patients.
31779679	16	69	theme	Runx2	2285:2289	arg1	O-GlcNAcylation					2257:2271	O-GlcNAcylation	2257:2271	O-GlcNAcylation of Sox9 and Runx2	2257:2289	Finally, O-GlcNAcylation of Sox9 and Runx2 decreased chondrogenesis and increased osteogenesis in CESCs.
31779679	1	70	theme	major	199:203	arg1	cause					205:209	a major cause	197:209	a major cause of low back pain	197:226	BACKGROUND The degenerative disc disease (DDD) is a major cause of low back pain.
31779679	1	70	theme	major	199:203	arg1	disease					180:186	The degenerative disc disease	158:186	The degenerative disc disease (DDD)	158:192	BACKGROUND The degenerative disc disease (DDD) is a major cause of low back pain.
31779679	17	71	theme	chondrogenic	2444:2455	arg1	potential					2488:2496	the chondrogenic and osteogenic differentiation potential	2440:2496	the chondrogenic and osteogenic differentiation potential of CESCs	2440:2505	CONCLUSIONS Our findings demonstrate the effect of glucose concentration on regulating the chondrogenic and osteogenic differentiation potential of CESCs and provide insight into the mechanism of how glucose concentration regulates Sox9 and Runx2 O-GlcNAcylation to affect the differentiation of CESCs, which may represent a target for CEP degeneration therapy.
31779679	14	72	theme	osteogenic	1977:1986	arg1	differentiation					1988:2002	CESC osteogenic differentiation	1972:2002	CESC osteogenic differentiation	1972:2002	Furthermore, Thiamet-G promoted CESC osteogenic differentiation and inhibited chondrogenic differentiation in low-glucose differentiation medium; however, DON acted opposite role in high-glucose differentiation medium.
31779679	17	73	theme	osteogenic	2461:2470	arg1	potential					2488:2496	the chondrogenic and osteogenic differentiation potential	2440:2496	the chondrogenic and osteogenic differentiation potential of CESCs	2440:2505	CONCLUSIONS Our findings demonstrate the effect of glucose concentration on regulating the chondrogenic and osteogenic differentiation potential of CESCs and provide insight into the mechanism of how glucose concentration regulates Sox9 and Runx2 O-GlcNAcylation to affect the differentiation of CESCs, which may represent a target for CEP degeneration therapy.
31779679	16	74	theme	increased	2320:2328	arg1	osteogenesis					2330:2341	increased osteogenesis	2320:2341	increased osteogenesis	2320:2341	Finally, O-GlcNAcylation of Sox9 and Runx2 decreased chondrogenesis and increased osteogenesis in CESCs.
31779679	16	75	from	osteogenesis	2330:2341	arg1	CESCs					2346:2350	CESCs	2346:2350	CESCs	2346:2350	Finally, O-GlcNAcylation of Sox9 and Runx2 decreased chondrogenesis and increased osteogenesis in CESCs.
31779679	17	76	theme	glucose	2404:2410	arg1	concentration					2412:2424	glucose concentration	2404:2424	glucose concentration	2404:2424	CONCLUSIONS Our findings demonstrate the effect of glucose concentration on regulating the chondrogenic and osteogenic differentiation potential of CESCs and provide insight into the mechanism of how glucose concentration regulates Sox9 and Runx2 O-GlcNAcylation to affect the differentiation of CESCs, which may represent a target for CEP degeneration therapy.
31779679	17	77	theme	CESCs	2501:2505	arg1	potential					2488:2496	the chondrogenic and osteogenic differentiation potential	2440:2496	the chondrogenic and osteogenic differentiation potential of CESCs	2440:2505	CONCLUSIONS Our findings demonstrate the effect of glucose concentration on regulating the chondrogenic and osteogenic differentiation potential of CESCs and provide insight into the mechanism of how glucose concentration regulates Sox9 and Runx2 O-GlcNAcylation to affect the differentiation of CESCs, which may represent a target for CEP degeneration therapy.
31779679	11	78	theme	O-GlcNAcylation	1507:1521	arg1	effects					1496:1502	The effects	1492:1502	The effects of O-GlcNAcylation on the downstream genes of Sox9 and Runx2	1492:1563	The effects of O-GlcNAcylation on the downstream genes of Sox9 and Runx2 were determined by Q-PCR and western blot.
31779679	0	79	theme	stem	97:100	arg1	cells					102:106	human cartilage endplate stem cells	72:106	human cartilage endplate stem cells	72:106	Glucose regulates tissue-specific chondro-osteogenic differentiation of human cartilage endplate stem cells via O-GlcNAcylation of Sox9 and Runx2.
31779679	2	80	theme	low-glucose	247:257	arg1	microenvironment					259:274	The physiological low-glucose microenvironment	229:274	The physiological low-glucose microenvironment of the cartilage endplate (CEP)	229:306	The physiological low-glucose microenvironment of the cartilage endplate (CEP) is disrupted in DDD.
31779679	1	81	theme	degenerative	162:173	arg1	cause					205:209	a major cause	197:209	a major cause of low back pain	197:226	BACKGROUND The degenerative disc disease (DDD) is a major cause of low back pain.
31779679	1	81	theme	degenerative	162:173	arg1	DDD					189:191	DDD	189:191	DDD	189:191	BACKGROUND The degenerative disc disease (DDD) is a major cause of low back pain.
31779679	1	81	theme	degenerative	162:173	arg1	disease					180:186	The degenerative disc disease	158:186	The degenerative disc disease (DDD)	158:192	BACKGROUND The degenerative disc disease (DDD) is a major cause of low back pain.
31779679	11	82	theme	Sox9	1550:1553	arg1	genes					1541:1545	the downstream genes	1526:1545	the downstream genes of Sox9 and Runx2	1526:1563	The effects of O-GlcNAcylation on the downstream genes of Sox9 and Runx2 were determined by Q-PCR and western blot.
31779679	12	83	theme	protein	1710:1716	arg1	level					1734:1738	higher protein O-GlcNAcylation level	1703:1738	higher protein O-GlcNAcylation level	1703:1738	RESULTS Degenerated CEPs from DDD patients lost chondrogenesis, acquired osteogenesis, and had higher protein O-GlcNAcylation level compared to normal CEPs from LVF patients.
31779679	5	84	theme	DDD	604:606	arg1	Mechanisms					590:599	Mechanisms	590:599	Mechanisms of DDD	590:606	Mechanisms of DDD are incompletely understood but include CEP degeneration and calcification.
31779679	17	85	theme	concentration	2412:2424	arg1	effect					2394:2399	the effect	2390:2399	the effect of glucose concentration on regulating the chondrogenic and osteogenic differentiation potential of CESCs	2390:2505	CONCLUSIONS Our findings demonstrate the effect of glucose concentration on regulating the chondrogenic and osteogenic differentiation potential of CESCs and provide insight into the mechanism of how glucose concentration regulates Sox9 and Runx2 O-GlcNAcylation to affect the differentiation of CESCs, which may represent a target for CEP degeneration therapy.
31779679	3	86	theme	protein	348:354	arg1	O-GlcNAcylation					356:370	protein O-GlcNAcylation	348:370	protein O-GlcNAcylation	348:370	Glucose influences protein O-GlcNAcylation via the hexosamine biosynthetic pathway (HBP), which is the key to stem cell fate.
31779679	1	87	theme	pain	223:226	arg1	cause					205:209	a major cause	197:209	a major cause of low back pain	197:226	BACKGROUND The degenerative disc disease (DDD) is a major cause of low back pain.
31779679	1	87	theme	pain	223:226	arg1	disease					180:186	The degenerative disc disease	158:186	The degenerative disc disease (DDD)	158:192	BACKGROUND The degenerative disc disease (DDD) is a major cause of low back pain.
31779679	6	88	theme	molecular	709:717	arg1	mechanisms					719:728	the molecular mechanisms	705:728	the molecular mechanisms of glucose in CEP calcification in DDD	705:767	We aimed to identify the molecular mechanisms of glucose in CEP calcification in DDD.
31779679	14	89	theme	high-glucose	2122:2133	arg1	medium					2151:2156	high-glucose differentiation medium	2122:2156	high-glucose differentiation medium	2122:2156	Furthermore, Thiamet-G promoted CESC osteogenic differentiation and inhibited chondrogenic differentiation in low-glucose differentiation medium; however, DON acted opposite role in high-glucose differentiation medium.
31779679	13	90	theme	high-glucose	1903:1914	arg1	medium					1932:1937	high-glucose differentiation medium	1903:1937	high-glucose differentiation medium	1903:1937	CESC chondrogenic differentiation gradually decreased while osteogenic differentiation gradually increased from low- to high-glucose differentiation medium.
31779679	0	91	theme	chondro-osteogenic	34:51	arg1	differentiation					53:67	tissue-specific chondro-osteogenic differentiation	18:67	tissue-specific chondro-osteogenic differentiation of human cartilage endplate stem cells	18:106	Glucose regulates tissue-specific chondro-osteogenic differentiation of human cartilage endplate stem cells via O-GlcNAcylation of Sox9 and Runx2.
31779679	3	92	theme	hexosamine	380:389	arg1	key					432:434	key	432:434	key	432:434	Glucose influences protein O-GlcNAcylation via the hexosamine biosynthetic pathway (HBP), which is the key to stem cell fate.
31779679	3	92	theme	hexosamine	380:389	arg1	HBP					413:415	HBP	413:415	HBP	413:415	Glucose influences protein O-GlcNAcylation via the hexosamine biosynthetic pathway (HBP), which is the key to stem cell fate.
31779679	3	92	theme	hexosamine	380:389	arg1	pathway					404:410	the hexosamine biosynthetic pathway	376:410	the hexosamine biosynthetic pathway (HBP)	376:416	Glucose influences protein O-GlcNAcylation via the hexosamine biosynthetic pathway (HBP), which is the key to stem cell fate.
31779679	7	93	theme	CEP	813:815	arg1	tissues					817:823	normal and degenerated CEP tissues	790:823	normal and degenerated CEP tissues from patients	790:837	METHODS We assessed normal and degenerated CEP tissues from patients, and the effects of chondrogenesis and osteogenesis of the CEP were determined by western blot and immunohistochemical staining.
31779679	12	94	from	patients	1773:1780	arg1	CEPs					1759:1762	normal CEPs	1752:1762	normal CEPs from LVF patients	1752:1780	RESULTS Degenerated CEPs from DDD patients lost chondrogenesis, acquired osteogenesis, and had higher protein O-GlcNAcylation level compared to normal CEPs from LVF patients.
31779679	4	95	theme	O-GlcNAcylated	513:526	arg1	proteins					528:535	accumulating O-GlcNAcylated proteins	500:535	accumulating O-GlcNAcylated proteins	500:535	Thiamet-G is an inhibitor of O-GlcNAcase for accumulating O-GlcNAcylated proteins while 6-diazo-5-oxo-L-norleucine (DON) inhibits HBP.
31779679	3	96	theme	stem	439:442	arg1	fate					449:452	stem cell fate	439:452	stem cell fate	439:452	Glucose influences protein O-GlcNAcylation via the hexosamine biosynthetic pathway (HBP), which is the key to stem cell fate.
31779679	0	97	theme	cartilage	78:86	arg1	cells					102:106	human cartilage endplate stem cells	72:106	human cartilage endplate stem cells	72:106	Glucose regulates tissue-specific chondro-osteogenic differentiation of human cartilage endplate stem cells via O-GlcNAcylation of Sox9 and Runx2.
31779679	9	98	theme	western	1376:1382	arg1	blot					1384:1387	western blot	1376:1387	western blot	1376:1387	CESCs were induced with low-glucose and high-glucose medium with or without Thiamet-G or DON for 21 days, and chondrogenic and osteogenic differentiations were measured by Q-PCR, western blot, and immunohistochemical staining.
31779679	12	99	from	CEPs	1628:1631	arg1	RESULTS					1608:1614	RESULTS	1608:1614	RESULTS Degenerated CEPs from DDD patients	1608:1649	RESULTS Degenerated CEPs from DDD patients lost chondrogenesis, acquired osteogenesis, and had higher protein O-GlcNAcylation level compared to normal CEPs from LVF patients.
31779679	7	100	dep	METHODS	770:776	arg1	determined					907:916	determined	907:916	were determined by western blot and immunohistochemical staining	902:965	METHODS We assessed normal and degenerated CEP tissues from patients, and the effects of chondrogenesis and osteogenesis of the CEP were determined by western blot and immunohistochemical staining.
31779679	7	100	dep	METHODS	770:776	arg1	assessed					781:788	assessed	781:788	assessed normal and degenerated CEP tissues from patients	781:837	METHODS We assessed normal and degenerated CEP tissues from patients, and the effects of chondrogenesis and osteogenesis of the CEP were determined by western blot and immunohistochemical staining.
31779679	11	101	from	effects	1496:1502	arg1	genes					1541:1545	the downstream genes	1526:1545	the downstream genes of Sox9 and Runx2	1526:1563	The effects of O-GlcNAcylation on the downstream genes of Sox9 and Runx2 were determined by Q-PCR and western blot.
31779679	16	102	from	chondrogenesis	2301:2314	arg1	CESCs					2346:2350	CESCs	2346:2350	CESCs	2346:2350	Finally, O-GlcNAcylation of Sox9 and Runx2 decreased chondrogenesis and increased osteogenesis in CESCs.
31779679	15	103	theme	differentiated	2226:2239	arg1	CESCs					2241:2245	differentiated CESCs	2226:2245	differentiated CESCs	2226:2245	Interestingly, we found that Sox9 and Runx2 were O-GlcNAcylated in differentiated CESCs.
31779679	17	104	theme	Runx2	2594:2598	arg1	O-GlcNAcylation					2600:2614	Runx2 O-GlcNAcylation	2594:2614	Runx2 O-GlcNAcylation	2594:2614	CONCLUSIONS Our findings demonstrate the effect of glucose concentration on regulating the chondrogenic and osteogenic differentiation potential of CESCs and provide insight into the mechanism of how glucose concentration regulates Sox9 and Runx2 O-GlcNAcylation to affect the differentiation of CESCs, which may represent a target for CEP degeneration therapy.
31779679	9	105	theme	immunohistochemical	1394:1412	arg1	staining					1414:1421	immunohistochemical staining	1394:1421	immunohistochemical staining	1394:1421	CESCs were induced with low-glucose and high-glucose medium with or without Thiamet-G or DON for 21 days, and chondrogenic and osteogenic differentiations were measured by Q-PCR, western blot, and immunohistochemical staining.
31779679	1	106	theme	low	214:216	arg1	pain					223:226	low back pain	214:226	low back pain	214:226	BACKGROUND The degenerative disc disease (DDD) is a major cause of low back pain.
31779679	14	107	theme	differentiation	2062:2076	arg1	medium					2078:2083	low-glucose differentiation medium	2050:2083	low-glucose differentiation medium	2050:2083	Furthermore, Thiamet-G promoted CESC osteogenic differentiation and inhibited chondrogenic differentiation in low-glucose differentiation medium; however, DON acted opposite role in high-glucose differentiation medium.
31779679	17	108	theme	CEP	2689:2691	arg1	therapy					2706:2712	CEP degeneration therapy	2689:2712	CEP degeneration therapy	2689:2712	CONCLUSIONS Our findings demonstrate the effect of glucose concentration on regulating the chondrogenic and osteogenic differentiation potential of CESCs and provide insight into the mechanism of how glucose concentration regulates Sox9 and Runx2 O-GlcNAcylation to affect the differentiation of CESCs, which may represent a target for CEP degeneration therapy.
31779679	12	109	dep	CEPs	1628:1631	arg1	patients					1642:1649	DDD patients	1638:1649	DDD patients	1638:1649	RESULTS Degenerated CEPs from DDD patients lost chondrogenesis, acquired osteogenesis, and had higher protein O-GlcNAcylation level compared to normal CEPs from LVF patients.
27185461	0	0	theme	Synthase	89:96	arg1	Expression					58:67	the Expression	54:67	the Expression of Liver Fatty Acid Synthase	54:96	The Nutrient-Dependent O-GlcNAc Modification Controls the Expression of Liver Fatty Acid Synthase.
27185461	3	1	theme	key	491:493	arg1	enzymes					495:501	key enzymes	491:501	key enzymes such as FAS	491:513	Therefore, deciphering the molecular mechanisms governing the expression and function of key enzymes such as FAS is crucial.
27185461	3	1	theme	key	491:493	arg1	FAS					511:513	FAS	511:513	FAS	511:513	Therefore, deciphering the molecular mechanisms governing the expression and function of key enzymes such as FAS is crucial.
27185461	0	2	theme	Acid	84:87	arg1	Synthase					89:96	Liver Fatty Acid Synthase	72:96	Liver Fatty Acid Synthase	72:96	The Nutrient-Dependent O-GlcNAc Modification Controls the Expression of Liver Fatty Acid Synthase.
27185461	6	3	from	removal	1002:1008	arg1	mice					1034:1037	mice	1034:1037	mice intraperitoneally injected with the selective and potent O-GlcNAcase (OGA) inhibitor Thiamet-G	1034:1132	More importantly, inhibiting the removal of O-GlcNAc residues in mice intraperitoneally injected with the selective and potent O-GlcNAcase (OGA) inhibitor Thiamet-G increases FAS expression.
27185461	1	4	theme	de	146:147	arg1	lipogenesis					154:164	de novo lipogenesis	146:164	de novo lipogenesis	146:164	Liver Fatty Acid Synthase (FAS) is pivotal for de novo lipogenesis.
27185461	6	5	theme	O-GlcNAcase	1096:1106	arg1	Thiamet-G					1124:1132	the selective and potent O-GlcNAcase (OGA) inhibitor Thiamet-G	1071:1132	the selective and potent O-GlcNAcase (OGA) inhibitor Thiamet-G	1071:1132	More importantly, inhibiting the removal of O-GlcNAc residues in mice intraperitoneally injected with the selective and potent O-GlcNAcase (OGA) inhibitor Thiamet-G increases FAS expression.
27185461	3	6	dep	expression	464:473	arg1	the					460:462	the	460:462	the	460:462	Therefore, deciphering the molecular mechanisms governing the expression and function of key enzymes such as FAS is crucial.
27185461	4	7	dep	diseases	699:706	arg1	obesity					719:725	obesity	719:725	obesity	719:725	Herein, we link the availability of this lipogenic enzyme to the nutrient-dependent post-translational modification O-GlcNAc that is thought to be deregulated in metabolic diseases (diabetes, obesity, and metabolic syndrome).
27185461	4	7	dep	diseases	699:706	arg1	diabetes					709:716	diabetes	709:716	diabetes	709:716	Herein, we link the availability of this lipogenic enzyme to the nutrient-dependent post-translational modification O-GlcNAc that is thought to be deregulated in metabolic diseases (diabetes, obesity, and metabolic syndrome).
27185461	4	7	dep	diseases	699:706	arg1	diseases					699:706	metabolic diseases	689:706	metabolic diseases (diabetes, obesity, and metabolic syndrome)	689:750	Herein, we link the availability of this lipogenic enzyme to the nutrient-dependent post-translational modification O-GlcNAc that is thought to be deregulated in metabolic diseases (diabetes, obesity, and metabolic syndrome).
27185461	4	7	dep	diseases	699:706	arg1	syndrome					742:749	metabolic syndrome	732:749	metabolic syndrome	732:749	Herein, we link the availability of this lipogenic enzyme to the nutrient-dependent post-translational modification O-GlcNAc that is thought to be deregulated in metabolic diseases (diabetes, obesity, and metabolic syndrome).
27185461	10	8	theme	diseases	1777:1784	arg1	forms					1762:1766	diverse forms	1754:1766	diverse forms of liver diseases	1754:1784	Together, these results reveal a new type of regulation of FAS, linked to O-GlcNAcylation status, and advance our knowledge on deregulation of lipogenesis in diverse forms of liver diseases.
27185461	10	9	theme	liver	1771:1775	arg1	diseases					1777:1784	liver diseases	1771:1784	liver diseases	1771:1784	Together, these results reveal a new type of regulation of FAS, linked to O-GlcNAcylation status, and advance our knowledge on deregulation of lipogenesis in diverse forms of liver diseases.
27185461	10	10	attach	linked	1660:1665	arg2	type					1633:1636	a new type	1627:1636	a new type	1627:1636	Together, these results reveal a new type of regulation of FAS, linked to O-GlcNAcylation status, and advance our knowledge on deregulation of lipogenesis in diverse forms of liver diseases.
27185461	10	10	attach	linked	1660:1665	arg1	status					1686:1691	O-GlcNAcylation status	1670:1691	O-GlcNAcylation status	1670:1691	Together, these results reveal a new type of regulation of FAS, linked to O-GlcNAcylation status, and advance our knowledge on deregulation of lipogenesis in diverse forms of liver diseases.
27185461	4	11	theme	metabolic	689:697	arg1	obesity					719:725	obesity	719:725	obesity	719:725	Herein, we link the availability of this lipogenic enzyme to the nutrient-dependent post-translational modification O-GlcNAc that is thought to be deregulated in metabolic diseases (diabetes, obesity, and metabolic syndrome).
27185461	4	11	theme	metabolic	689:697	arg1	diabetes					709:716	diabetes	709:716	diabetes	709:716	Herein, we link the availability of this lipogenic enzyme to the nutrient-dependent post-translational modification O-GlcNAc that is thought to be deregulated in metabolic diseases (diabetes, obesity, and metabolic syndrome).
27185461	4	11	theme	metabolic	689:697	arg1	syndrome					742:749	metabolic syndrome	732:749	metabolic syndrome	732:749	Herein, we link the availability of this lipogenic enzyme to the nutrient-dependent post-translational modification O-GlcNAc that is thought to be deregulated in metabolic diseases (diabetes, obesity, and metabolic syndrome).
27185461	4	11	theme	metabolic	689:697	arg1	diseases					699:706	metabolic diseases	689:706	metabolic diseases (diabetes, obesity, and metabolic syndrome)	689:750	Herein, we link the availability of this lipogenic enzyme to the nutrient-dependent post-translational modification O-GlcNAc that is thought to be deregulated in metabolic diseases (diabetes, obesity, and metabolic syndrome).
27185461	7	12	theme	O-GlcNAc	1168:1175	arg1	OGT					1190:1192	OGT	1190:1192	OGT	1190:1192	FAS and O-GlcNAc transferase (OGT) physically interact, and FAS is O-GlcNAc modified.
27185461	7	12	theme	O-GlcNAc	1168:1175	arg1	transferase					1177:1187	O-GlcNAc transferase	1168:1187	O-GlcNAc transferase (OGT)	1168:1193	FAS and O-GlcNAc transferase (OGT) physically interact, and FAS is O-GlcNAc modified.
27185461	8	13	theme	line	1272:1275	arg1	Treatment					1246:1254	Treatment	1246:1254	Treatment of a liver cell line with drugs or nutrients that elevate the O-GlcNAcylation	1246:1332	Treatment of a liver cell line with drugs or nutrients that elevate the O-GlcNAcylation interferes with FAS expression.
27185461	8	14	theme	FAS	1350:1352	arg1	expression					1354:1363	FAS expression	1350:1363	FAS expression	1350:1363	Treatment of a liver cell line with drugs or nutrients that elevate the O-GlcNAcylation interferes with FAS expression.
27185461	10	15	theme	regulation	1641:1650	arg1	type					1633:1636	a new type	1627:1636	a new type	1627:1636	Together, these results reveal a new type of regulation of FAS, linked to O-GlcNAcylation status, and advance our knowledge on deregulation of lipogenesis in diverse forms of liver diseases.
27185461	9	16	theme	deubiquitinase	1430:1443	arg1	protease-2a					1464:1474	the deubiquitinase Ubiquitin-specific protease-2a	1426:1474	the deubiquitinase Ubiquitin-specific protease-2a (USP2A)	1426:1482	Inhibition of OGA increases the interaction between FAS and the deubiquitinase Ubiquitin-specific protease-2a (USP2A) in vivo and ex vivo, providing mechanistic insights into the control of FAS expression through O-GlcNAcylation.
27185461	9	16	theme	deubiquitinase	1430:1443	arg1	USP2A					1477:1481	USP2A	1477:1481	USP2A	1477:1481	Inhibition of OGA increases the interaction between FAS and the deubiquitinase Ubiquitin-specific protease-2a (USP2A) in vivo and ex vivo, providing mechanistic insights into the control of FAS expression through O-GlcNAcylation.
27185461	10	17	from	knowledge	1710:1718	arg1	deregulation					1723:1734	deregulation	1723:1734	deregulation of lipogenesis	1723:1749	Together, these results reveal a new type of regulation of FAS, linked to O-GlcNAcylation status, and advance our knowledge on deregulation of lipogenesis in diverse forms of liver diseases.
27185461	2	18	theme	pathologies	249:259	arg1	development					228:238	the development	224:238	the development of liver pathologies ranging from steatosis to nonalcoholic steatohepatitis (NASH) which can lead to cirrhosis and, less frequently, to hepatocellular carcinoma	224:399	Loss of control of this metabolic pathway contributes to the development of liver pathologies ranging from steatosis to nonalcoholic steatohepatitis (NASH) which can lead to cirrhosis and, less frequently, to hepatocellular carcinoma.
27185461	6	19	theme	potent	1089:1094	arg1	Thiamet-G					1124:1132	the selective and potent O-GlcNAcase (OGA) inhibitor Thiamet-G	1071:1132	the selective and potent O-GlcNAcase (OGA) inhibitor Thiamet-G	1071:1132	More importantly, inhibiting the removal of O-GlcNAc residues in mice intraperitoneally injected with the selective and potent O-GlcNAcase (OGA) inhibitor Thiamet-G increases FAS expression.
27185461	5	20	theme	ob/ob	853:857	arg1	mice					859:862	ob/ob mice	853:862	ob/ob mice	853:862	We demonstrate that expression and activity of liver FAS correlate with O-GlcNAcylation contents in ob/ob mice and in mice fed with a high-carbohydrate diet both in a transcription-dependent and -independent manner.
27185461	0	21	theme	Nutrient-Dependent	4:21	arg1	Modification					32:43	The Nutrient-Dependent O-GlcNAc Modification	0:43	The Nutrient-Dependent O-GlcNAc Modification	0:43	The Nutrient-Dependent O-GlcNAc Modification Controls the Expression of Liver Fatty Acid Synthase.
27185461	9	22	theme	FAS	1556:1558	arg1	expression					1560:1569	FAS expression	1556:1569	FAS expression through O-GlcNAcylation	1556:1593	Inhibition of OGA increases the interaction between FAS and the deubiquitinase Ubiquitin-specific protease-2a (USP2A) in vivo and ex vivo, providing mechanistic insights into the control of FAS expression through O-GlcNAcylation.
27185461	9	23	theme	expression	1560:1569	arg1	control					1545:1551	the control	1541:1551	the control of FAS expression through O-GlcNAcylation	1541:1593	Inhibition of OGA increases the interaction between FAS and the deubiquitinase Ubiquitin-specific protease-2a (USP2A) in vivo and ex vivo, providing mechanistic insights into the control of FAS expression through O-GlcNAcylation.
27185461	4	24	theme	O-GlcNAc	643:650	arg1	modification					630:641	the nutrient-dependent post-translational modification O-GlcNAc	588:650	the nutrient-dependent post-translational modification O-GlcNAc that is thought to be deregulated in metabolic diseases (diabetes, obesity, and metabolic syndrome)	588:750	Herein, we link the availability of this lipogenic enzyme to the nutrient-dependent post-translational modification O-GlcNAc that is thought to be deregulated in metabolic diseases (diabetes, obesity, and metabolic syndrome).
27185461	1	25	dep	de	146:147	arg1	novo					149:152	novo	149:152	novo	149:152	Liver Fatty Acid Synthase (FAS) is pivotal for de novo lipogenesis.
27185461	6	26	attach	removal	1002:1008	arg2	residues					1022:1029	O-GlcNAc residues	1013:1029	O-GlcNAc residues	1013:1029	More importantly, inhibiting the removal of O-GlcNAc residues in mice intraperitoneally injected with the selective and potent O-GlcNAcase (OGA) inhibitor Thiamet-G increases FAS expression.
27185461	6	26	attach	removal	1002:1008	arg3	mice					1034:1037	mice	1034:1037	mice intraperitoneally injected with the selective and potent O-GlcNAcase (OGA) inhibitor Thiamet-G	1034:1132	More importantly, inhibiting the removal of O-GlcNAc residues in mice intraperitoneally injected with the selective and potent O-GlcNAcase (OGA) inhibitor Thiamet-G increases FAS expression.
27185461	5	27	theme	O-GlcNAcylation	825:839	arg1	contents					841:848	O-GlcNAcylation contents	825:848	O-GlcNAcylation contents in ob/ob mice and in mice fed with a high-carbohydrate diet both in a transcription-dependent and -independent manner	825:966	We demonstrate that expression and activity of liver FAS correlate with O-GlcNAcylation contents in ob/ob mice and in mice fed with a high-carbohydrate diet both in a transcription-dependent and -independent manner.
27185461	10	28	theme	diverse	1754:1760	arg1	forms					1762:1766	diverse forms	1754:1766	diverse forms of liver diseases	1754:1784	Together, these results reveal a new type of regulation of FAS, linked to O-GlcNAcylation status, and advance our knowledge on deregulation of lipogenesis in diverse forms of liver diseases.
27185461	2	29	theme	nonalcoholic	287:298	arg1	NASH					317:320	NASH	317:320	NASH	317:320	Loss of control of this metabolic pathway contributes to the development of liver pathologies ranging from steatosis to nonalcoholic steatohepatitis (NASH) which can lead to cirrhosis and, less frequently, to hepatocellular carcinoma.
27185461	2	29	theme	nonalcoholic	287:298	arg1	steatohepatitis					300:314	nonalcoholic steatohepatitis	287:314	nonalcoholic steatohepatitis (NASH) which can lead to cirrhosis and, less frequently, to hepatocellular carcinoma	287:399	Loss of control of this metabolic pathway contributes to the development of liver pathologies ranging from steatosis to nonalcoholic steatohepatitis (NASH) which can lead to cirrhosis and, less frequently, to hepatocellular carcinoma.
27185461	4	30	theme	post-translational	611:628	arg1	modification					630:641	the nutrient-dependent post-translational modification O-GlcNAc	588:650	the nutrient-dependent post-translational modification O-GlcNAc that is thought to be deregulated in metabolic diseases (diabetes, obesity, and metabolic syndrome)	588:750	Herein, we link the availability of this lipogenic enzyme to the nutrient-dependent post-translational modification O-GlcNAc that is thought to be deregulated in metabolic diseases (diabetes, obesity, and metabolic syndrome).
27185461	1	31	theme	Liver	99:103	arg1	FAS					126:128	FAS	126:128	FAS	126:128	Liver Fatty Acid Synthase (FAS) is pivotal for de novo lipogenesis.
27185461	1	31	theme	Liver	99:103	arg1	Synthase					116:123	Liver Fatty Acid Synthase	99:123	Liver Fatty Acid Synthase (FAS)	99:129	Liver Fatty Acid Synthase (FAS) is pivotal for de novo lipogenesis.
27185461	10	32	theme	lipogenesis	1739:1749	arg1	deregulation					1723:1734	deregulation	1723:1734	deregulation of lipogenesis	1723:1749	Together, these results reveal a new type of regulation of FAS, linked to O-GlcNAcylation status, and advance our knowledge on deregulation of lipogenesis in diverse forms of liver diseases.
27185461	1	33	theme	Acid	111:114	arg1	FAS					126:128	FAS	126:128	FAS	126:128	Liver Fatty Acid Synthase (FAS) is pivotal for de novo lipogenesis.
27185461	1	33	theme	Acid	111:114	arg1	Synthase					116:123	Liver Fatty Acid Synthase	99:123	Liver Fatty Acid Synthase (FAS)	99:129	Liver Fatty Acid Synthase (FAS) is pivotal for de novo lipogenesis.
27185461	4	34	theme	nutrient-dependent	592:609	arg1	modification					630:641	the nutrient-dependent post-translational modification O-GlcNAc	588:650	the nutrient-dependent post-translational modification O-GlcNAc that is thought to be deregulated in metabolic diseases (diabetes, obesity, and metabolic syndrome)	588:750	Herein, we link the availability of this lipogenic enzyme to the nutrient-dependent post-translational modification O-GlcNAc that is thought to be deregulated in metabolic diseases (diabetes, obesity, and metabolic syndrome).
27185461	5	35	theme	-independent	948:959	arg1	manner					961:966	a transcription-dependent and -independent manner	918:966	a transcription-dependent and -independent manner	918:966	We demonstrate that expression and activity of liver FAS correlate with O-GlcNAcylation contents in ob/ob mice and in mice fed with a high-carbohydrate diet both in a transcription-dependent and -independent manner.
27185461	2	36	theme	hepatocellular	376:389	arg1	carcinoma					391:399	hepatocellular carcinoma	376:399	hepatocellular carcinoma	376:399	Loss of control of this metabolic pathway contributes to the development of liver pathologies ranging from steatosis to nonalcoholic steatohepatitis (NASH) which can lead to cirrhosis and, less frequently, to hepatocellular carcinoma.
27185461	5	37	dep	mice	859:862	arg1	both					910:913	both	910:913	both	910:913	We demonstrate that expression and activity of liver FAS correlate with O-GlcNAcylation contents in ob/ob mice and in mice fed with a high-carbohydrate diet both in a transcription-dependent and -independent manner.
27185461	3	38	theme	molecular	429:437	arg1	mechanisms					439:448	the molecular mechanisms	425:448	the molecular mechanisms governing the expression and function of key enzymes such as FAS	425:513	Therefore, deciphering the molecular mechanisms governing the expression and function of key enzymes such as FAS is crucial.
27185461	9	39	theme	OGA	1380:1382	arg1	Inhibition					1366:1375	Inhibition	1366:1375	Inhibition of OGA	1366:1382	Inhibition of OGA increases the interaction between FAS and the deubiquitinase Ubiquitin-specific protease-2a (USP2A) in vivo and ex vivo, providing mechanistic insights into the control of FAS expression through O-GlcNAcylation.
27185461	10	40	theme	new	1629:1631	arg1	type					1633:1636	a new type	1627:1636	a new type	1627:1636	Together, these results reveal a new type of regulation of FAS, linked to O-GlcNAcylation status, and advance our knowledge on deregulation of lipogenesis in diverse forms of liver diseases.
27185461	8	41	theme	cell	1267:1270	arg1	line					1272:1275	a liver cell line	1259:1275	a liver cell line	1259:1275	Treatment of a liver cell line with drugs or nutrients that elevate the O-GlcNAcylation interferes with FAS expression.
27185461	5	42	theme	liver	800:804	arg1	FAS					806:808	liver FAS	800:808	liver FAS	800:808	We demonstrate that expression and activity of liver FAS correlate with O-GlcNAcylation contents in ob/ob mice and in mice fed with a high-carbohydrate diet both in a transcription-dependent and -independent manner.
27185461	4	43	theme	metabolic	732:740	arg1	diseases					699:706	metabolic diseases	689:706	metabolic diseases (diabetes, obesity, and metabolic syndrome)	689:750	Herein, we link the availability of this lipogenic enzyme to the nutrient-dependent post-translational modification O-GlcNAc that is thought to be deregulated in metabolic diseases (diabetes, obesity, and metabolic syndrome).
27185461	4	43	theme	metabolic	732:740	arg1	syndrome					742:749	metabolic syndrome	732:749	metabolic syndrome	732:749	Herein, we link the availability of this lipogenic enzyme to the nutrient-dependent post-translational modification O-GlcNAc that is thought to be deregulated in metabolic diseases (diabetes, obesity, and metabolic syndrome).
27185461	9	44	theme	Ubiquitin-specific	1445:1462	arg1	protease-2a					1464:1474	the deubiquitinase Ubiquitin-specific protease-2a	1426:1474	the deubiquitinase Ubiquitin-specific protease-2a (USP2A)	1426:1482	Inhibition of OGA increases the interaction between FAS and the deubiquitinase Ubiquitin-specific protease-2a (USP2A) in vivo and ex vivo, providing mechanistic insights into the control of FAS expression through O-GlcNAcylation.
27185461	9	44	theme	Ubiquitin-specific	1445:1462	arg1	USP2A					1477:1481	USP2A	1477:1481	USP2A	1477:1481	Inhibition of OGA increases the interaction between FAS and the deubiquitinase Ubiquitin-specific protease-2a (USP2A) in vivo and ex vivo, providing mechanistic insights into the control of FAS expression through O-GlcNAcylation.
27185461	2	45	theme	pathway	201:207	arg1	control					175:181	control	175:181	control of this metabolic pathway	175:207	Loss of control of this metabolic pathway contributes to the development of liver pathologies ranging from steatosis to nonalcoholic steatohepatitis (NASH) which can lead to cirrhosis and, less frequently, to hepatocellular carcinoma.
27185461	5	46	from	contents	841:848	arg1	manner					961:966	a transcription-dependent and -independent manner	918:966	a transcription-dependent and -independent manner	918:966	We demonstrate that expression and activity of liver FAS correlate with O-GlcNAcylation contents in ob/ob mice and in mice fed with a high-carbohydrate diet both in a transcription-dependent and -independent manner.
27185461	5	46	from	contents	841:848	arg1	mice					859:862	ob/ob mice	853:862	ob/ob mice	853:862	We demonstrate that expression and activity of liver FAS correlate with O-GlcNAcylation contents in ob/ob mice and in mice fed with a high-carbohydrate diet both in a transcription-dependent and -independent manner.
27185461	5	46	from	contents	841:848	arg1	mice					871:874	mice	871:874	mice fed with a high-carbohydrate diet	871:908	We demonstrate that expression and activity of liver FAS correlate with O-GlcNAcylation contents in ob/ob mice and in mice fed with a high-carbohydrate diet both in a transcription-dependent and -independent manner.
27185461	5	47	theme	transcription-dependent	920:942	arg1	manner					961:966	a transcription-dependent and -independent manner	918:966	a transcription-dependent and -independent manner	918:966	We demonstrate that expression and activity of liver FAS correlate with O-GlcNAcylation contents in ob/ob mice and in mice fed with a high-carbohydrate diet both in a transcription-dependent and -independent manner.
27185461	8	48	with	Treatment	1246:1254	arg1	drugs					1282:1286	drugs	1282:1286	drugs	1282:1286	Treatment of a liver cell line with drugs or nutrients that elevate the O-GlcNAcylation interferes with FAS expression.
27185461	8	48	with	Treatment	1246:1254	arg1	nutrients					1291:1299	nutrients	1291:1299	nutrients	1291:1299	Treatment of a liver cell line with drugs or nutrients that elevate the O-GlcNAcylation interferes with FAS expression.
27185461	2	49	theme	metabolic	191:199	arg1	pathway					201:207	this metabolic pathway	186:207	this metabolic pathway	186:207	Loss of control of this metabolic pathway contributes to the development of liver pathologies ranging from steatosis to nonalcoholic steatohepatitis (NASH) which can lead to cirrhosis and, less frequently, to hepatocellular carcinoma.
27185461	3	50	theme	enzymes	495:501	arg1	function					479:486	function	479:486	function	479:486	Therefore, deciphering the molecular mechanisms governing the expression and function of key enzymes such as FAS is crucial.
27185461	3	50	theme	enzymes	495:501	arg1	expression					464:473	expression	464:473	expression	464:473	Therefore, deciphering the molecular mechanisms governing the expression and function of key enzymes such as FAS is crucial.
27185461	5	51	theme	high-carbohydrate	887:903	arg1	diet					905:908	a high-carbohydrate diet	885:908	a high-carbohydrate diet	885:908	We demonstrate that expression and activity of liver FAS correlate with O-GlcNAcylation contents in ob/ob mice and in mice fed with a high-carbohydrate diet both in a transcription-dependent and -independent manner.
27185461	2	52	theme	liver	243:247	arg1	pathologies					249:259	liver pathologies	243:259	liver pathologies ranging from steatosis to nonalcoholic steatohepatitis (NASH) which can lead to cirrhosis and, less frequently, to hepatocellular carcinoma	243:399	Loss of control of this metabolic pathway contributes to the development of liver pathologies ranging from steatosis to nonalcoholic steatohepatitis (NASH) which can lead to cirrhosis and, less frequently, to hepatocellular carcinoma.
27185461	6	53	theme	O-GlcNAc	1013:1020	arg1	residues					1022:1029	O-GlcNAc residues	1013:1029	O-GlcNAc residues	1013:1029	More importantly, inhibiting the removal of O-GlcNAc residues in mice intraperitoneally injected with the selective and potent O-GlcNAcase (OGA) inhibitor Thiamet-G increases FAS expression.
27185461	6	54	theme	inhibitor	1114:1122	arg1	Thiamet-G					1124:1132	the selective and potent O-GlcNAcase (OGA) inhibitor Thiamet-G	1071:1132	the selective and potent O-GlcNAcase (OGA) inhibitor Thiamet-G	1071:1132	More importantly, inhibiting the removal of O-GlcNAc residues in mice intraperitoneally injected with the selective and potent O-GlcNAcase (OGA) inhibitor Thiamet-G increases FAS expression.
27185461	1	55	theme	Fatty	105:109	arg1	FAS					126:128	FAS	126:128	FAS	126:128	Liver Fatty Acid Synthase (FAS) is pivotal for de novo lipogenesis.
27185461	1	55	theme	Fatty	105:109	arg1	Synthase					116:123	Liver Fatty Acid Synthase	99:123	Liver Fatty Acid Synthase (FAS)	99:129	Liver Fatty Acid Synthase (FAS) is pivotal for de novo lipogenesis.
27185461	4	56	theme	enzyme	578:583	arg1	availability					547:558	the availability	543:558	the availability of this lipogenic enzyme	543:583	Herein, we link the availability of this lipogenic enzyme to the nutrient-dependent post-translational modification O-GlcNAc that is thought to be deregulated in metabolic diseases (diabetes, obesity, and metabolic syndrome).
27185461	4	57	attach	link	538:541	arg1	modification					630:641	the nutrient-dependent post-translational modification O-GlcNAc	588:650	the nutrient-dependent post-translational modification O-GlcNAc that is thought to be deregulated in metabolic diseases (diabetes, obesity, and metabolic syndrome)	588:750	Herein, we link the availability of this lipogenic enzyme to the nutrient-dependent post-translational modification O-GlcNAc that is thought to be deregulated in metabolic diseases (diabetes, obesity, and metabolic syndrome).
27185461	4	57	attach	link	538:541	arg2	we					535:536	we	535:536	we	535:536	Herein, we link the availability of this lipogenic enzyme to the nutrient-dependent post-translational modification O-GlcNAc that is thought to be deregulated in metabolic diseases (diabetes, obesity, and metabolic syndrome).
27185461	2	58	theme	control	175:181	arg1	Loss					167:170	Loss	167:170	Loss of control of this metabolic pathway	167:207	Loss of control of this metabolic pathway contributes to the development of liver pathologies ranging from steatosis to nonalcoholic steatohepatitis (NASH) which can lead to cirrhosis and, less frequently, to hepatocellular carcinoma.
27185461	5	59	theme	FAS	806:808	arg1	expression					773:782	expression	773:782	expression	773:782	We demonstrate that expression and activity of liver FAS correlate with O-GlcNAcylation contents in ob/ob mice and in mice fed with a high-carbohydrate diet both in a transcription-dependent and -independent manner.
27185461	5	59	theme	FAS	806:808	arg1	activity					788:795	activity	788:795	activity of liver FAS	788:808	We demonstrate that expression and activity of liver FAS correlate with O-GlcNAcylation contents in ob/ob mice and in mice fed with a high-carbohydrate diet both in a transcription-dependent and -independent manner.
27185461	9	60	theme	mechanistic	1515:1525	arg1	insights					1527:1534	mechanistic insights	1515:1534	mechanistic insights into the control of FAS expression through O-GlcNAcylation	1515:1593	Inhibition of OGA increases the interaction between FAS and the deubiquitinase Ubiquitin-specific protease-2a (USP2A) in vivo and ex vivo, providing mechanistic insights into the control of FAS expression through O-GlcNAcylation.
27185461	4	61	theme	lipogenic	568:576	arg1	enzyme					578:583	this lipogenic enzyme	563:583	this lipogenic enzyme	563:583	Herein, we link the availability of this lipogenic enzyme to the nutrient-dependent post-translational modification O-GlcNAc that is thought to be deregulated in metabolic diseases (diabetes, obesity, and metabolic syndrome).
27185461	0	62	theme	Fatty	78:82	arg1	Synthase					89:96	Liver Fatty Acid Synthase	72:96	Liver Fatty Acid Synthase	72:96	The Nutrient-Dependent O-GlcNAc Modification Controls the Expression of Liver Fatty Acid Synthase.
27185461	8	63	theme	liver	1261:1265	arg1	line					1272:1275	a liver cell line	1259:1275	a liver cell line	1259:1275	Treatment of a liver cell line with drugs or nutrients that elevate the O-GlcNAcylation interferes with FAS expression.
27185461	10	64	theme	O-GlcNAcylation	1670:1684	arg1	status					1686:1691	O-GlcNAcylation status	1670:1691	O-GlcNAcylation status	1670:1691	Together, these results reveal a new type of regulation of FAS, linked to O-GlcNAcylation status, and advance our knowledge on deregulation of lipogenesis in diverse forms of liver diseases.
27185461	6	65	theme	OGA	1109:1111	arg1	Thiamet-G					1124:1132	the selective and potent O-GlcNAcase (OGA) inhibitor Thiamet-G	1071:1132	the selective and potent O-GlcNAcase (OGA) inhibitor Thiamet-G	1071:1132	More importantly, inhibiting the removal of O-GlcNAc residues in mice intraperitoneally injected with the selective and potent O-GlcNAcase (OGA) inhibitor Thiamet-G increases FAS expression.
27185461	6	66	theme	selective	1075:1083	arg1	Thiamet-G					1124:1132	the selective and potent O-GlcNAcase (OGA) inhibitor Thiamet-G	1071:1132	the selective and potent O-GlcNAcase (OGA) inhibitor Thiamet-G	1071:1132	More importantly, inhibiting the removal of O-GlcNAc residues in mice intraperitoneally injected with the selective and potent O-GlcNAcase (OGA) inhibitor Thiamet-G increases FAS expression.
27185461	10	67	theme	FAS	1655:1657	arg1	regulation					1641:1650	regulation	1641:1650	regulation of FAS	1641:1657	Together, these results reveal a new type of regulation of FAS, linked to O-GlcNAcylation status, and advance our knowledge on deregulation of lipogenesis in diverse forms of liver diseases.
27185461	0	68	theme	Liver	72:76	arg1	Synthase					89:96	Liver Fatty Acid Synthase	72:96	Liver Fatty Acid Synthase	72:96	The Nutrient-Dependent O-GlcNAc Modification Controls the Expression of Liver Fatty Acid Synthase.
27185461	6	69	theme	FAS	1144:1146	arg1	expression					1148:1157	FAS expression	1144:1157	FAS expression	1144:1157	More importantly, inhibiting the removal of O-GlcNAc residues in mice intraperitoneally injected with the selective and potent O-GlcNAcase (OGA) inhibitor Thiamet-G increases FAS expression.
27185461	0	70	theme	O-GlcNAc	23:30	arg1	Modification					32:43	The Nutrient-Dependent O-GlcNAc Modification	0:43	The Nutrient-Dependent O-GlcNAc Modification	0:43	The Nutrient-Dependent O-GlcNAc Modification Controls the Expression of Liver Fatty Acid Synthase.
27185461	6	71	theme	residues	1022:1029	arg1	removal					1002:1008	the removal	998:1008	the removal of O-GlcNAc residues in mice intraperitoneally injected with the selective and potent O-GlcNAcase (OGA) inhibitor Thiamet-G	998:1132	More importantly, inhibiting the removal of O-GlcNAc residues in mice intraperitoneally injected with the selective and potent O-GlcNAcase (OGA) inhibitor Thiamet-G increases FAS expression.
31705928	0	0	theme	cancer	77:82	arg1	metastasis					54:63	lymph node metastasis	43:63	lymph node metastasis	43:63	RACK1 promotes the invasive activities and lymph node metastasis of cervical cancer via galectin-1.
31705928	0	0	theme	cancer	77:82	arg1	activities					28:37	the invasive activities	15:37	the invasive activities	15:37	RACK1 promotes the invasive activities and lymph node metastasis of cervical cancer via galectin-1.
31705928	7	1	theme	lymph	1280:1284	arg1	metastasis					1291:1300	lymph node metastasis	1280:1300	lymph node metastasis	1280:1300	Together, our results demonstrate that RACK1 stimulates tumor invasion and lymph node metastasis of cervical cancer via galectin-1 and imply that targeting RACK1/galectin-1 axis provides promising means for cervical cancer treatment.
31705928	4	2	theme	galectin-1-induced	708:725	arg1	FAK					747:749	galectin-1-induced downstream MEK/ERK, FAK, and AKT signaling	708:768	FAK	747:749	Additionally, RACK1 also augmented galectin-1-induced downstream MEK/ERK, FAK, and AKT signaling via integrin-β1 in cervical cancer cells.
31705928	5	3	from	prognosis	1025:1033	arg1	cases					1054:1058	cervical cancer cases	1038:1058	cervical cancer cases	1038:1058	Tissue microarray confirmed that RACK1 was upregulated in squamous intraepithelial lesion and cancer, and RACK1 was positively correlated with invasion/metastasis phenotype, galectin-1 expression, and unfavorable prognosis in cervical cancer cases.
31705928	1	4	theme	node	256:259	arg1	metastasis					261:270	lymph node metastasis	250:270	lymph node metastasis of cervical cancer	250:289	Cervical cancer remains the first leading cause of cancer-related mortality among female reproductive system malignancies worldwide, and invasion and lymph node metastasis of cervical cancer represent the major reason for its poor prognosis.
31705928	0	5	theme	cervical	68:75	arg1	cancer					77:82	cervical cancer	68:82	cervical cancer	68:82	RACK1 promotes the invasive activities and lymph node metastasis of cervical cancer via galectin-1.
31705928	6	6	theme	increased	1109:1117	arg1	expression					1119:1128	increased expression	1109:1128	increased expression of RACK1	1109:1137	Human papillomavirus E6 oncogene contributes to increased expression of RACK1 via the enhancement of its O-GlcNAcylation and protein stability.
31705928	1	7	theme	cancer-related	151:164	arg1	mortality					166:174	cancer-related mortality	151:174	cancer-related mortality among female reproductive system malignancies worldwide	151:230	Cervical cancer remains the first leading cause of cancer-related mortality among female reproductive system malignancies worldwide, and invasion and lymph node metastasis of cervical cancer represent the major reason for its poor prognosis.
31705928	5	8	theme	cervical	1038:1045	arg1	cases					1054:1058	cervical cancer cases	1038:1058	cervical cancer cases	1038:1058	Tissue microarray confirmed that RACK1 was upregulated in squamous intraepithelial lesion and cancer, and RACK1 was positively correlated with invasion/metastasis phenotype, galectin-1 expression, and unfavorable prognosis in cervical cancer cases.
31705928	3	9	theme	Mechanism	554:562	arg1	studies					564:570	Mechanism studies	554:570	Mechanism studies	554:570	Mechanism studies revealed that RACK1 promoted the expression and secretion of galectin-1 by reducing miR-1275 levels.
31705928	7	10	theme	tumor	1261:1265	arg1	invasion					1267:1274	tumor invasion	1261:1274	tumor invasion	1261:1274	Together, our results demonstrate that RACK1 stimulates tumor invasion and lymph node metastasis of cervical cancer via galectin-1 and imply that targeting RACK1/galectin-1 axis provides promising means for cervical cancer treatment.
31705928	7	11	theme	cancer	1314:1319	arg1	invasion					1267:1274	tumor invasion	1261:1274	tumor invasion	1261:1274	Together, our results demonstrate that RACK1 stimulates tumor invasion and lymph node metastasis of cervical cancer via galectin-1 and imply that targeting RACK1/galectin-1 axis provides promising means for cervical cancer treatment.
31705928	7	11	theme	cancer	1314:1319	arg1	metastasis					1291:1300	lymph node metastasis	1280:1300	lymph node metastasis	1280:1300	Together, our results demonstrate that RACK1 stimulates tumor invasion and lymph node metastasis of cervical cancer via galectin-1 and imply that targeting RACK1/galectin-1 axis provides promising means for cervical cancer treatment.
31705928	7	12	theme	cervical	1305:1312	arg1	cancer					1314:1319	cervical cancer	1305:1319	cervical cancer	1305:1319	Together, our results demonstrate that RACK1 stimulates tumor invasion and lymph node metastasis of cervical cancer via galectin-1 and imply that targeting RACK1/galectin-1 axis provides promising means for cervical cancer treatment.
31705928	1	13	theme	cervical	275:282	arg1	cancer					284:289	cervical cancer	275:289	cervical cancer	275:289	Cervical cancer remains the first leading cause of cancer-related mortality among female reproductive system malignancies worldwide, and invasion and lymph node metastasis of cervical cancer represent the major reason for its poor prognosis.
31705928	6	14	theme	stability	1194:1202	arg1	enhancement					1147:1157	the enhancement	1143:1157	the enhancement of its O-GlcNAcylation and protein stability	1143:1202	Human papillomavirus E6 oncogene contributes to increased expression of RACK1 via the enhancement of its O-GlcNAcylation and protein stability.
31705928	7	15	theme	promising	1392:1400	arg1	means					1402:1406	promising means	1392:1406	promising means for cervical cancer treatment	1392:1436	Together, our results demonstrate that RACK1 stimulates tumor invasion and lymph node metastasis of cervical cancer via galectin-1 and imply that targeting RACK1/galectin-1 axis provides promising means for cervical cancer treatment.
31705928	4	16	theme	cervical	789:796	arg1	cells					805:809	cervical cancer cells	789:809	cervical cancer cells	789:809	Additionally, RACK1 also augmented galectin-1-induced downstream MEK/ERK, FAK, and AKT signaling via integrin-β1 in cervical cancer cells.
31705928	1	17	theme	mortality	166:174	arg1	cause					142:146	the first leading cause	124:146	the first leading cause of cancer-related mortality among female reproductive system malignancies worldwide	124:230	Cervical cancer remains the first leading cause of cancer-related mortality among female reproductive system malignancies worldwide, and invasion and lymph node metastasis of cervical cancer represent the major reason for its poor prognosis.
31705928	2	18	theme	node	496:499	arg1	metastasis					501:510	lymph node metastasis	490:510	lymph node metastasis in vivo	490:518	In this study, we found that RACK1 facilitated tumor cell invasion and lymphatic tube formation in vitro, as well as promoted lymphangiogenesis and lymph node metastasis in vivo in a galectin-1-dependent manner.
31705928	6	19	theme	RACK1	1133:1137	arg1	expression					1119:1128	increased expression	1109:1128	increased expression of RACK1	1109:1137	Human papillomavirus E6 oncogene contributes to increased expression of RACK1 via the enhancement of its O-GlcNAcylation and protein stability.
31705928	7	20	theme	node	1286:1289	arg1	metastasis					1291:1300	lymph node metastasis	1280:1300	lymph node metastasis	1280:1300	Together, our results demonstrate that RACK1 stimulates tumor invasion and lymph node metastasis of cervical cancer via galectin-1 and imply that targeting RACK1/galectin-1 axis provides promising means for cervical cancer treatment.
31705928	1	21	theme	female	182:187	arg1	system					202:207	female reproductive system	182:207	female reproductive system malignancies worldwide	182:230	Cervical cancer remains the first leading cause of cancer-related mortality among female reproductive system malignancies worldwide, and invasion and lymph node metastasis of cervical cancer represent the major reason for its poor prognosis.
31705928	1	22	theme	cancer	284:289	arg1	metastasis					261:270	lymph node metastasis	250:270	lymph node metastasis of cervical cancer	250:289	Cervical cancer remains the first leading cause of cancer-related mortality among female reproductive system malignancies worldwide, and invasion and lymph node metastasis of cervical cancer represent the major reason for its poor prognosis.
31705928	1	22	theme	cancer	284:289	arg1	invasion					237:244	invasion	237:244	invasion	237:244	Cervical cancer remains the first leading cause of cancer-related mortality among female reproductive system malignancies worldwide, and invasion and lymph node metastasis of cervical cancer represent the major reason for its poor prognosis.
31705928	5	23	theme	intraepithelial	879:893	arg1	lesion					895:900	squamous intraepithelial lesion and cancer	870:911	lesion	895:900	Tissue microarray confirmed that RACK1 was upregulated in squamous intraepithelial lesion and cancer, and RACK1 was positively correlated with invasion/metastasis phenotype, galectin-1 expression, and unfavorable prognosis in cervical cancer cases.
31705928	3	24	dep	expression	605:614	arg1	the					601:603	the	601:603	the	601:603	Mechanism studies revealed that RACK1 promoted the expression and secretion of galectin-1 by reducing miR-1275 levels.
31705928	1	25	theme	reproductive	189:200	arg1	system					202:207	female reproductive system	182:207	female reproductive system malignancies worldwide	182:230	Cervical cancer remains the first leading cause of cancer-related mortality among female reproductive system malignancies worldwide, and invasion and lymph node metastasis of cervical cancer represent the major reason for its poor prognosis.
31705928	0	26	theme	invasive	19:26	arg1	activities					28:37	the invasive activities	15:37	the invasive activities	15:37	RACK1 promotes the invasive activities and lymph node metastasis of cervical cancer via galectin-1.
31705928	5	27	theme	invasion/metastasis	955:973	arg1	phenotype					975:983	invasion/metastasis phenotype	955:983	invasion/metastasis phenotype	955:983	Tissue microarray confirmed that RACK1 was upregulated in squamous intraepithelial lesion and cancer, and RACK1 was positively correlated with invasion/metastasis phenotype, galectin-1 expression, and unfavorable prognosis in cervical cancer cases.
31705928	5	28	theme	galectin-1	986:995	arg1	expression					997:1006	galectin-1 expression	986:1006	galectin-1 expression	986:1006	Tissue microarray confirmed that RACK1 was upregulated in squamous intraepithelial lesion and cancer, and RACK1 was positively correlated with invasion/metastasis phenotype, galectin-1 expression, and unfavorable prognosis in cervical cancer cases.
31705928	1	29	theme	system	202:207	arg1	worldwide					222:230	female reproductive system malignancies worldwide	182:230	female reproductive system malignancies worldwide	182:230	Cervical cancer remains the first leading cause of cancer-related mortality among female reproductive system malignancies worldwide, and invasion and lymph node metastasis of cervical cancer represent the major reason for its poor prognosis.
31705928	2	30	theme	tube	423:426	arg1	formation					428:436	lymphatic tube formation	413:436	lymphatic tube formation	413:436	In this study, we found that RACK1 facilitated tumor cell invasion and lymphatic tube formation in vitro, as well as promoted lymphangiogenesis and lymph node metastasis in vivo in a galectin-1-dependent manner.
31705928	2	31	theme	galectin-1-dependent	525:544	arg1	manner					546:551	a galectin-1-dependent manner	523:551	a galectin-1-dependent manner	523:551	In this study, we found that RACK1 facilitated tumor cell invasion and lymphatic tube formation in vitro, as well as promoted lymphangiogenesis and lymph node metastasis in vivo in a galectin-1-dependent manner.
31705928	1	32	theme	Cervical	100:107	arg1	cancer					109:114	Cervical cancer	100:114	Cervical cancer	100:114	Cervical cancer remains the first leading cause of cancer-related mortality among female reproductive system malignancies worldwide, and invasion and lymph node metastasis of cervical cancer represent the major reason for its poor prognosis.
31705928	1	33	theme	malignancies	209:220	arg1	worldwide					222:230	female reproductive system malignancies worldwide	182:230	female reproductive system malignancies worldwide	182:230	Cervical cancer remains the first leading cause of cancer-related mortality among female reproductive system malignancies worldwide, and invasion and lymph node metastasis of cervical cancer represent the major reason for its poor prognosis.
31705928	1	34	theme	major	305:309	arg1	reason					311:316	the major reason	301:316	the major reason for its poor prognosis	301:339	Cervical cancer remains the first leading cause of cancer-related mortality among female reproductive system malignancies worldwide, and invasion and lymph node metastasis of cervical cancer represent the major reason for its poor prognosis.
31705928	3	35	theme	miR-1275	656:663	arg1	levels					665:670	miR-1275 levels	656:670	miR-1275 levels	656:670	Mechanism studies revealed that RACK1 promoted the expression and secretion of galectin-1 by reducing miR-1275 levels.
31705928	7	36	theme	RACK1/galectin-1	1361:1376	arg1	axis					1378:1381	targeting RACK1/galectin-1 axis	1351:1381	targeting RACK1/galectin-1 axis	1351:1381	Together, our results demonstrate that RACK1 stimulates tumor invasion and lymph node metastasis of cervical cancer via galectin-1 and imply that targeting RACK1/galectin-1 axis provides promising means for cervical cancer treatment.
31705928	2	37	theme	tumor	389:393	arg1	invasion					400:407	tumor cell invasion	389:407	tumor cell invasion	389:407	In this study, we found that RACK1 facilitated tumor cell invasion and lymphatic tube formation in vitro, as well as promoted lymphangiogenesis and lymph node metastasis in vivo in a galectin-1-dependent manner.
31705928	3	38	theme	galectin-1	633:642	arg1	secretion					620:628	secretion	620:628	secretion	620:628	Mechanism studies revealed that RACK1 promoted the expression and secretion of galectin-1 by reducing miR-1275 levels.
31705928	3	38	theme	galectin-1	633:642	arg1	expression					605:614	expression	605:614	expression	605:614	Mechanism studies revealed that RACK1 promoted the expression and secretion of galectin-1 by reducing miR-1275 levels.
31705928	2	39	theme	cell	395:398	arg1	invasion					400:407	tumor cell invasion	389:407	tumor cell invasion	389:407	In this study, we found that RACK1 facilitated tumor cell invasion and lymphatic tube formation in vitro, as well as promoted lymphangiogenesis and lymph node metastasis in vivo in a galectin-1-dependent manner.
31705928	0	40	theme	node	49:52	arg1	metastasis					54:63	lymph node metastasis	43:63	lymph node metastasis	43:63	RACK1 promotes the invasive activities and lymph node metastasis of cervical cancer via galectin-1.
31705928	5	41	theme	Tissue	812:817	arg1	microarray					819:828	Tissue microarray	812:828	Tissue microarray	812:828	Tissue microarray confirmed that RACK1 was upregulated in squamous intraepithelial lesion and cancer, and RACK1 was positively correlated with invasion/metastasis phenotype, galectin-1 expression, and unfavorable prognosis in cervical cancer cases.
31705928	5	42	theme	unfavorable	1013:1023	arg1	prognosis					1025:1033	unfavorable prognosis	1013:1033	unfavorable prognosis in cervical cancer cases	1013:1058	Tissue microarray confirmed that RACK1 was upregulated in squamous intraepithelial lesion and cancer, and RACK1 was positively correlated with invasion/metastasis phenotype, galectin-1 expression, and unfavorable prognosis in cervical cancer cases.
31705928	6	43	theme	protein	1186:1192	arg1	stability					1194:1202	protein stability	1186:1202	protein stability	1186:1202	Human papillomavirus E6 oncogene contributes to increased expression of RACK1 via the enhancement of its O-GlcNAcylation and protein stability.
31705928	4	44	theme	MEK/ERK	738:744	arg1	FAK					747:749	galectin-1-induced downstream MEK/ERK, FAK, and AKT signaling	708:768	FAK	747:749	Additionally, RACK1 also augmented galectin-1-induced downstream MEK/ERK, FAK, and AKT signaling via integrin-β1 in cervical cancer cells.
31705928	0	45	theme	lymph	43:47	arg1	metastasis					54:63	lymph node metastasis	43:63	lymph node metastasis	43:63	RACK1 promotes the invasive activities and lymph node metastasis of cervical cancer via galectin-1.
31705928	4	46	theme	downstream	727:736	arg1	FAK					747:749	galectin-1-induced downstream MEK/ERK, FAK, and AKT signaling	708:768	FAK	747:749	Additionally, RACK1 also augmented galectin-1-induced downstream MEK/ERK, FAK, and AKT signaling via integrin-β1 in cervical cancer cells.
31705928	1	47	theme	poor	326:329	arg1	prognosis					331:339	its poor prognosis	322:339	its poor prognosis	322:339	Cervical cancer remains the first leading cause of cancer-related mortality among female reproductive system malignancies worldwide, and invasion and lymph node metastasis of cervical cancer represent the major reason for its poor prognosis.
31705928	7	48	theme	cervical	1412:1419	arg1	treatment					1428:1436	cervical cancer treatment	1412:1436	cervical cancer treatment	1412:1436	Together, our results demonstrate that RACK1 stimulates tumor invasion and lymph node metastasis of cervical cancer via galectin-1 and imply that targeting RACK1/galectin-1 axis provides promising means for cervical cancer treatment.
31705928	5	49	from	expression	997:1006	arg1	cases					1054:1058	cervical cancer cases	1038:1058	cervical cancer cases	1038:1058	Tissue microarray confirmed that RACK1 was upregulated in squamous intraepithelial lesion and cancer, and RACK1 was positively correlated with invasion/metastasis phenotype, galectin-1 expression, and unfavorable prognosis in cervical cancer cases.
31705928	6	50	theme	E6	1082:1083	arg1	oncogene					1085:1092	Human papillomavirus E6 oncogene	1061:1092	Human papillomavirus E6 oncogene	1061:1092	Human papillomavirus E6 oncogene contributes to increased expression of RACK1 via the enhancement of its O-GlcNAcylation and protein stability.
31705928	7	51	theme	targeting	1351:1359	arg1	axis					1378:1381	targeting RACK1/galectin-1 axis	1351:1381	targeting RACK1/galectin-1 axis	1351:1381	Together, our results demonstrate that RACK1 stimulates tumor invasion and lymph node metastasis of cervical cancer via galectin-1 and imply that targeting RACK1/galectin-1 axis provides promising means for cervical cancer treatment.
31705928	4	52	theme	cancer	798:803	arg1	cells					805:809	cervical cancer cells	789:809	cervical cancer cells	789:809	Additionally, RACK1 also augmented galectin-1-induced downstream MEK/ERK, FAK, and AKT signaling via integrin-β1 in cervical cancer cells.
31705928	4	53	theme	AKT	756:758	arg1	signaling					760:768	galectin-1-induced downstream MEK/ERK, FAK, and AKT signaling	708:768	signaling	760:768	Additionally, RACK1 also augmented galectin-1-induced downstream MEK/ERK, FAK, and AKT signaling via integrin-β1 in cervical cancer cells.
31705928	1	54	theme	first	128:132	arg1	cause					142:146	the first leading cause	124:146	the first leading cause of cancer-related mortality among female reproductive system malignancies worldwide	124:230	Cervical cancer remains the first leading cause of cancer-related mortality among female reproductive system malignancies worldwide, and invasion and lymph node metastasis of cervical cancer represent the major reason for its poor prognosis.
31705928	5	55	from	phenotype	975:983	arg1	cases					1054:1058	cervical cancer cases	1038:1058	cervical cancer cases	1038:1058	Tissue microarray confirmed that RACK1 was upregulated in squamous intraepithelial lesion and cancer, and RACK1 was positively correlated with invasion/metastasis phenotype, galectin-1 expression, and unfavorable prognosis in cervical cancer cases.
31705928	6	56	theme	papillomavirus	1067:1080	arg1	oncogene					1085:1092	Human papillomavirus E6 oncogene	1061:1092	Human papillomavirus E6 oncogene	1061:1092	Human papillomavirus E6 oncogene contributes to increased expression of RACK1 via the enhancement of its O-GlcNAcylation and protein stability.
31705928	2	57	theme	lymph	490:494	arg1	node					496:499	lymph node	490:499	lymph node metastasis in vivo	490:518	In this study, we found that RACK1 facilitated tumor cell invasion and lymphatic tube formation in vitro, as well as promoted lymphangiogenesis and lymph node metastasis in vivo in a galectin-1-dependent manner.
31705928	5	58	theme	squamous	870:877	arg1	lesion					895:900	squamous intraepithelial lesion and cancer	870:911	lesion	895:900	Tissue microarray confirmed that RACK1 was upregulated in squamous intraepithelial lesion and cancer, and RACK1 was positively correlated with invasion/metastasis phenotype, galectin-1 expression, and unfavorable prognosis in cervical cancer cases.
31705928	5	59	theme	cancer	1047:1052	arg1	cases					1054:1058	cervical cancer cases	1038:1058	cervical cancer cases	1038:1058	Tissue microarray confirmed that RACK1 was upregulated in squamous intraepithelial lesion and cancer, and RACK1 was positively correlated with invasion/metastasis phenotype, galectin-1 expression, and unfavorable prognosis in cervical cancer cases.
31705928	2	60	theme	lymphatic	413:421	arg1	formation					428:436	lymphatic tube formation	413:436	lymphatic tube formation	413:436	In this study, we found that RACK1 facilitated tumor cell invasion and lymphatic tube formation in vitro, as well as promoted lymphangiogenesis and lymph node metastasis in vivo in a galectin-1-dependent manner.
31705928	1	61	theme	leading	134:140	arg1	cause					142:146	the first leading cause	124:146	the first leading cause of cancer-related mortality among female reproductive system malignancies worldwide	124:230	Cervical cancer remains the first leading cause of cancer-related mortality among female reproductive system malignancies worldwide, and invasion and lymph node metastasis of cervical cancer represent the major reason for its poor prognosis.
31705928	7	62	theme	cancer	1421:1426	arg1	treatment					1428:1436	cervical cancer treatment	1412:1436	cervical cancer treatment	1412:1436	Together, our results demonstrate that RACK1 stimulates tumor invasion and lymph node metastasis of cervical cancer via galectin-1 and imply that targeting RACK1/galectin-1 axis provides promising means for cervical cancer treatment.
31705928	6	63	theme	Human	1061:1065	arg1	oncogene					1085:1092	Human papillomavirus E6 oncogene	1061:1092	Human papillomavirus E6 oncogene	1061:1092	Human papillomavirus E6 oncogene contributes to increased expression of RACK1 via the enhancement of its O-GlcNAcylation and protein stability.
31705928	6	64	theme	O-GlcNAcylation	1166:1180	arg1	enhancement					1147:1157	the enhancement	1143:1157	the enhancement of its O-GlcNAcylation and protein stability	1143:1202	Human papillomavirus E6 oncogene contributes to increased expression of RACK1 via the enhancement of its O-GlcNAcylation and protein stability.
31705928	1	65	theme	lymph	250:254	arg1	metastasis					261:270	lymph node metastasis	250:270	lymph node metastasis of cervical cancer	250:289	Cervical cancer remains the first leading cause of cancer-related mortality among female reproductive system malignancies worldwide, and invasion and lymph node metastasis of cervical cancer represent the major reason for its poor prognosis.
27530921	1	0	theme	scaffold	155:162	arg1	GNB2L1					128:133	GNB2L1	128:133	GNB2L1	128:133	GNB2L1 is an intercellular scaffold protein of the Trp-Asp (WD) repeat protein family, and has been reported to play suppressive roles in the progression of gastric cancer.
27530921	1	0	theme	scaffold	155:162	arg1	protein					164:170	an intercellular scaffold protein	138:170	an intercellular scaffold protein of the Trp-Asp (WD) repeat protein family	138:212	GNB2L1 is an intercellular scaffold protein of the Trp-Asp (WD) repeat protein family, and has been reported to play suppressive roles in the progression of gastric cancer.
27530921	6	1	from	inhibition	1169:1178	arg1	metastasis					1198:1207	gastric tumour metastasis	1183:1207	gastric tumour metastasis	1183:1207	In summary, this study indicated the O-GlcNAcylation on GNB2L1 reversed its inhibition on gastric tumour metastasis via promoting its degradation.
27530921	5	2	with	GNB2L1	943:948	arg1	expression					959:968	OGT expression	955:968	OGT expression	955:968	In addition, the clinical data revealed the negative correlation of the protein level instead of the mRNA level of GNB2L1 with OGT expression, and showed that OGT reversed the inhibition of GNB2L1 on metastasis, and worsened the prognosis of GNB2L1(High) patients.
27530921	2	3	theme	regulatory	314:323	arg1	mechanisms					325:334	the regulatory mechanisms	310:334	the regulatory mechanisms of GNB2L1 in gastric cancer	310:362	However, the regulatory mechanisms of GNB2L1 in gastric cancer still remain largely elusive.
27530921	3	4	from	GNB2L1	490:495	arg1	cancer					529:534	gastric cancer	521:534	gastric cancer	521:534	In the present study, we found that OGT was capable to interact with GNB2L1 directly and modify GNB2L1 with O-GlcNAcylation in gastric cancer, and this O-GlcNAcylation hindered the inhibition of GNB2L1 on migration of gastric cancer cells.
27530921	5	5	theme	GNB2L1	1070:1075	arg1	patients					1083:1090	GNB2L1(High) patients	1070:1090	GNB2L1(High) patients	1070:1090	In addition, the clinical data revealed the negative correlation of the protein level instead of the mRNA level of GNB2L1 with OGT expression, and showed that OGT reversed the inhibition of GNB2L1 on metastasis, and worsened the prognosis of GNB2L1(High) patients.
27530921	4	6	from	cancer	732:737	arg1	degradation					674:684	the degradation	670:684	the degradation instead of the synthesis of GNB2L1 in gastric cancer	670:737	Moreover, O-GlcNAcylation regulated the degradation instead of the synthesis of GNB2L1 in gastric cancer, and our data suggested the O-GlcNAcylation on GNB2L1 influenced its stability directly.
27530921	4	7	theme	gastric	724:730	arg1	cancer					732:737	gastric cancer	724:737	gastric cancer	724:737	Moreover, O-GlcNAcylation regulated the degradation instead of the synthesis of GNB2L1 in gastric cancer, and our data suggested the O-GlcNAcylation on GNB2L1 influenced its stability directly.
27530921	4	8	theme	synthesis	701:709	arg1	degradation					674:684	the degradation	670:684	the degradation instead of the synthesis of GNB2L1 in gastric cancer	670:737	Moreover, O-GlcNAcylation regulated the degradation instead of the synthesis of GNB2L1 in gastric cancer, and our data suggested the O-GlcNAcylation on GNB2L1 influenced its stability directly.
27530921	6	9	theme	tumour	1191:1196	arg1	metastasis					1198:1207	gastric tumour metastasis	1183:1207	gastric tumour metastasis	1183:1207	In summary, this study indicated the O-GlcNAcylation on GNB2L1 reversed its inhibition on gastric tumour metastasis via promoting its degradation.
27530921	6	10	dep	indicated	1116:1124	arg1	reversed					1156:1163	reversed	1156:1163	indicated the O-GlcNAcylation on GNB2L1 reversed its inhibition on gastric tumour metastasis via promoting its degradation	1116:1237	In summary, this study indicated the O-GlcNAcylation on GNB2L1 reversed its inhibition on gastric tumour metastasis via promoting its degradation.
27530921	0	11	theme	Gastric	111:117	arg1	Tumours					119:125	Gastric Tumours	111:125	Gastric Tumours	111:125	O-GlcNAcylation of the Signaling Scaffold Protein, GNB2L1 Promotes its Degradation and Increases Metastasis of Gastric Tumours.
27530921	6	12	theme	gastric	1183:1189	arg1	metastasis					1198:1207	gastric tumour metastasis	1183:1207	gastric tumour metastasis	1183:1207	In summary, this study indicated the O-GlcNAcylation on GNB2L1 reversed its inhibition on gastric tumour metastasis via promoting its degradation.
27530921	5	13	theme	mRNA	929:932	arg1	level					934:938	the mRNA level	925:938	the protein level instead of the mRNA level of GNB2L1 with OGT expression	896:968	In addition, the clinical data revealed the negative correlation of the protein level instead of the mRNA level of GNB2L1 with OGT expression, and showed that OGT reversed the inhibition of GNB2L1 on metastasis, and worsened the prognosis of GNB2L1(High) patients.
27530921	2	14	theme	gastric	349:355	arg1	cancer					357:362	gastric cancer	349:362	gastric cancer	349:362	However, the regulatory mechanisms of GNB2L1 in gastric cancer still remain largely elusive.
27530921	3	15	theme	present	401:407	arg1	study					409:413	the present study	397:413	the present study	397:413	In the present study, we found that OGT was capable to interact with GNB2L1 directly and modify GNB2L1 with O-GlcNAcylation in gastric cancer, and this O-GlcNAcylation hindered the inhibition of GNB2L1 on migration of gastric cancer cells.
27530921	2	16	from	mechanisms	325:334	arg1	cancer					357:362	gastric cancer	349:362	gastric cancer	349:362	However, the regulatory mechanisms of GNB2L1 in gastric cancer still remain largely elusive.
27530921	5	17	theme	level	934:938	arg1	correlation					881:891	the negative correlation	868:891	the negative correlation of the protein level instead of the mRNA level of GNB2L1 with OGT expression	868:968	In addition, the clinical data revealed the negative correlation of the protein level instead of the mRNA level of GNB2L1 with OGT expression, and showed that OGT reversed the inhibition of GNB2L1 on metastasis, and worsened the prognosis of GNB2L1(High) patients.
27530921	3	18	from	inhibition	575:584	arg1	migration					599:607	migration	599:607	migration of gastric cancer cells	599:631	In the present study, we found that OGT was capable to interact with GNB2L1 directly and modify GNB2L1 with O-GlcNAcylation in gastric cancer, and this O-GlcNAcylation hindered the inhibition of GNB2L1 on migration of gastric cancer cells.
27530921	5	19	from	inhibition	1004:1013	arg1	metastasis					1028:1037	metastasis	1028:1037	metastasis	1028:1037	In addition, the clinical data revealed the negative correlation of the protein level instead of the mRNA level of GNB2L1 with OGT expression, and showed that OGT reversed the inhibition of GNB2L1 on metastasis, and worsened the prognosis of GNB2L1(High) patients.
27530921	3	20	theme	gastric	521:527	arg1	cancer					529:534	gastric cancer	521:534	gastric cancer	521:534	In the present study, we found that OGT was capable to interact with GNB2L1 directly and modify GNB2L1 with O-GlcNAcylation in gastric cancer, and this O-GlcNAcylation hindered the inhibition of GNB2L1 on migration of gastric cancer cells.
27530921	5	21	theme	patients	1083:1090	arg1	prognosis					1057:1065	the prognosis	1053:1065	the prognosis of GNB2L1(High) patients	1053:1090	In addition, the clinical data revealed the negative correlation of the protein level instead of the mRNA level of GNB2L1 with OGT expression, and showed that OGT reversed the inhibition of GNB2L1 on metastasis, and worsened the prognosis of GNB2L1(High) patients.
27530921	1	22	theme	Trp-Asp	179:185	arg1	family					207:212	the Trp-Asp (WD) repeat protein family	175:212	the Trp-Asp (WD) repeat protein family	175:212	GNB2L1 is an intercellular scaffold protein of the Trp-Asp (WD) repeat protein family, and has been reported to play suppressive roles in the progression of gastric cancer.
27530921	1	23	theme	suppressive	245:255	arg1	roles					257:261	suppressive roles	245:261	suppressive roles	245:261	GNB2L1 is an intercellular scaffold protein of the Trp-Asp (WD) repeat protein family, and has been reported to play suppressive roles in the progression of gastric cancer.
27530921	4	24	from	synthesis	701:709	arg1	cancer					732:737	gastric cancer	724:737	gastric cancer	724:737	Moreover, O-GlcNAcylation regulated the degradation instead of the synthesis of GNB2L1 in gastric cancer, and our data suggested the O-GlcNAcylation on GNB2L1 influenced its stability directly.
27530921	5	25	theme	protein	900:906	arg1	level					908:912	the protein level	896:912	the protein level instead of the mRNA level of GNB2L1 with OGT expression	896:968	In addition, the clinical data revealed the negative correlation of the protein level instead of the mRNA level of GNB2L1 with OGT expression, and showed that OGT reversed the inhibition of GNB2L1 on metastasis, and worsened the prognosis of GNB2L1(High) patients.
27530921	0	26	theme	Signaling	23:31	arg1	Protein					42:48	the Signaling Scaffold Protein	19:48	the Signaling Scaffold Protein	19:48	O-GlcNAcylation of the Signaling Scaffold Protein, GNB2L1 Promotes its Degradation and Increases Metastasis of Gastric Tumours.
27530921	0	26	theme	Signaling	23:31	arg1	GNB2L1					51:56	GNB2L1	51:56	GNB2L1	51:56	O-GlcNAcylation of the Signaling Scaffold Protein, GNB2L1 Promotes its Degradation and Increases Metastasis of Gastric Tumours.
27530921	4	27	theme	GNB2L1	714:719	arg1	synthesis					701:709	the synthesis	697:709	the synthesis of GNB2L1 in gastric cancer	697:737	Moreover, O-GlcNAcylation regulated the degradation instead of the synthesis of GNB2L1 in gastric cancer, and our data suggested the O-GlcNAcylation on GNB2L1 influenced its stability directly.
27530921	1	28	theme	WD	188:189	arg1	family					207:212	the Trp-Asp (WD) repeat protein family	175:212	the Trp-Asp (WD) repeat protein family	175:212	GNB2L1 is an intercellular scaffold protein of the Trp-Asp (WD) repeat protein family, and has been reported to play suppressive roles in the progression of gastric cancer.
27530921	0	29	theme	Tumours	119:125	arg1	Metastasis					97:106	Metastasis	97:106	Metastasis of Gastric Tumours	97:125	O-GlcNAcylation of the Signaling Scaffold Protein, GNB2L1 Promotes its Degradation and Increases Metastasis of Gastric Tumours.
27530921	0	30	theme	Protein	42:48	arg1	O-GlcNAcylation					0:14	O-GlcNAcylation	0:14	O-GlcNAcylation of the Signaling Scaffold Protein, GNB2L1	0:56	O-GlcNAcylation of the Signaling Scaffold Protein, GNB2L1 Promotes its Degradation and Increases Metastasis of Gastric Tumours.
27530921	5	31	theme	negative	872:879	arg1	correlation					881:891	the negative correlation	868:891	the negative correlation of the protein level instead of the mRNA level of GNB2L1 with OGT expression	868:968	In addition, the clinical data revealed the negative correlation of the protein level instead of the mRNA level of GNB2L1 with OGT expression, and showed that OGT reversed the inhibition of GNB2L1 on metastasis, and worsened the prognosis of GNB2L1(High) patients.
27530921	1	32	theme	repeat	192:197	arg1	family					207:212	the Trp-Asp (WD) repeat protein family	175:212	the Trp-Asp (WD) repeat protein family	175:212	GNB2L1 is an intercellular scaffold protein of the Trp-Asp (WD) repeat protein family, and has been reported to play suppressive roles in the progression of gastric cancer.
27530921	0	33	theme	Scaffold	33:40	arg1	Protein					42:48	the Signaling Scaffold Protein	19:48	the Signaling Scaffold Protein	19:48	O-GlcNAcylation of the Signaling Scaffold Protein, GNB2L1 Promotes its Degradation and Increases Metastasis of Gastric Tumours.
27530921	0	33	theme	Scaffold	33:40	arg1	GNB2L1					51:56	GNB2L1	51:56	GNB2L1	51:56	O-GlcNAcylation of the Signaling Scaffold Protein, GNB2L1 Promotes its Degradation and Increases Metastasis of Gastric Tumours.
27530921	3	34	theme	GNB2L1	589:594	arg1	inhibition					575:584	the inhibition	571:584	the inhibition of GNB2L1 on migration of gastric cancer cells	571:631	In the present study, we found that OGT was capable to interact with GNB2L1 directly and modify GNB2L1 with O-GlcNAcylation in gastric cancer, and this O-GlcNAcylation hindered the inhibition of GNB2L1 on migration of gastric cancer cells.
27530921	1	35	theme	protein	199:205	arg1	family					207:212	the Trp-Asp (WD) repeat protein family	175:212	the Trp-Asp (WD) repeat protein family	175:212	GNB2L1 is an intercellular scaffold protein of the Trp-Asp (WD) repeat protein family, and has been reported to play suppressive roles in the progression of gastric cancer.
27530921	3	36	with	GNB2L1	490:495	arg1	O-GlcNAcylation					502:516	O-GlcNAcylation	502:516	O-GlcNAcylation	502:516	In the present study, we found that OGT was capable to interact with GNB2L1 directly and modify GNB2L1 with O-GlcNAcylation in gastric cancer, and this O-GlcNAcylation hindered the inhibition of GNB2L1 on migration of gastric cancer cells.
27530921	5	37	theme	High	1077:1080	arg1	patients					1083:1090	GNB2L1(High) patients	1070:1090	GNB2L1(High) patients	1070:1090	In addition, the clinical data revealed the negative correlation of the protein level instead of the mRNA level of GNB2L1 with OGT expression, and showed that OGT reversed the inhibition of GNB2L1 on metastasis, and worsened the prognosis of GNB2L1(High) patients.
27530921	4	38	dep	suggested	753:761	arg1	influenced					793:802	influenced	793:802	suggested the O-GlcNAcylation on GNB2L1 influenced its stability directly	753:825	Moreover, O-GlcNAcylation regulated the degradation instead of the synthesis of GNB2L1 in gastric cancer, and our data suggested the O-GlcNAcylation on GNB2L1 influenced its stability directly.
27530921	1	39	theme	gastric	285:291	arg1	cancer					293:298	gastric cancer	285:298	gastric cancer	285:298	GNB2L1 is an intercellular scaffold protein of the Trp-Asp (WD) repeat protein family, and has been reported to play suppressive roles in the progression of gastric cancer.
27530921	3	40	theme	cells	627:631	arg1	migration					599:607	migration	599:607	migration of gastric cancer cells	599:631	In the present study, we found that OGT was capable to interact with GNB2L1 directly and modify GNB2L1 with O-GlcNAcylation in gastric cancer, and this O-GlcNAcylation hindered the inhibition of GNB2L1 on migration of gastric cancer cells.
27530921	4	41	from	O-GlcNAcylation	767:781	arg1	GNB2L1					786:791	GNB2L1	786:791	GNB2L1	786:791	Moreover, O-GlcNAcylation regulated the degradation instead of the synthesis of GNB2L1 in gastric cancer, and our data suggested the O-GlcNAcylation on GNB2L1 influenced its stability directly.
27530921	5	42	theme	GNB2L1	1018:1023	arg1	inhibition					1004:1013	the inhibition	1000:1013	the inhibition of GNB2L1 on metastasis	1000:1037	In addition, the clinical data revealed the negative correlation of the protein level instead of the mRNA level of GNB2L1 with OGT expression, and showed that OGT reversed the inhibition of GNB2L1 on metastasis, and worsened the prognosis of GNB2L1(High) patients.
27530921	1	43	theme	cancer	293:298	arg1	progression					270:280	the progression	266:280	the progression of gastric cancer	266:298	GNB2L1 is an intercellular scaffold protein of the Trp-Asp (WD) repeat protein family, and has been reported to play suppressive roles in the progression of gastric cancer.
27530921	5	44	theme	level	908:912	arg1	correlation					881:891	the negative correlation	868:891	the negative correlation of the protein level instead of the mRNA level of GNB2L1 with OGT expression	868:968	In addition, the clinical data revealed the negative correlation of the protein level instead of the mRNA level of GNB2L1 with OGT expression, and showed that OGT reversed the inhibition of GNB2L1 on metastasis, and worsened the prognosis of GNB2L1(High) patients.
27530921	1	45	theme	family	207:212	arg1	GNB2L1					128:133	GNB2L1	128:133	GNB2L1	128:133	GNB2L1 is an intercellular scaffold protein of the Trp-Asp (WD) repeat protein family, and has been reported to play suppressive roles in the progression of gastric cancer.
27530921	1	45	theme	family	207:212	arg1	protein					164:170	an intercellular scaffold protein	138:170	an intercellular scaffold protein of the Trp-Asp (WD) repeat protein family	138:212	GNB2L1 is an intercellular scaffold protein of the Trp-Asp (WD) repeat protein family, and has been reported to play suppressive roles in the progression of gastric cancer.
27530921	3	46	theme	gastric	612:618	arg1	cells					627:631	gastric cancer cells	612:631	gastric cancer cells	612:631	In the present study, we found that OGT was capable to interact with GNB2L1 directly and modify GNB2L1 with O-GlcNAcylation in gastric cancer, and this O-GlcNAcylation hindered the inhibition of GNB2L1 on migration of gastric cancer cells.
27530921	5	47	theme	GNB2L1	943:948	arg1	level					934:938	the mRNA level	925:938	the protein level instead of the mRNA level of GNB2L1 with OGT expression	896:968	In addition, the clinical data revealed the negative correlation of the protein level instead of the mRNA level of GNB2L1 with OGT expression, and showed that OGT reversed the inhibition of GNB2L1 on metastasis, and worsened the prognosis of GNB2L1(High) patients.
27530921	5	48	theme	clinical	845:852	arg1	data					854:857	the clinical data	841:857	the clinical data	841:857	In addition, the clinical data revealed the negative correlation of the protein level instead of the mRNA level of GNB2L1 with OGT expression, and showed that OGT reversed the inhibition of GNB2L1 on metastasis, and worsened the prognosis of GNB2L1(High) patients.
27530921	4	49	from	degradation	674:684	arg1	cancer					732:737	gastric cancer	724:737	gastric cancer	724:737	Moreover, O-GlcNAcylation regulated the degradation instead of the synthesis of GNB2L1 in gastric cancer, and our data suggested the O-GlcNAcylation on GNB2L1 influenced its stability directly.
27530921	3	50	theme	cancer	620:625	arg1	cells					627:631	gastric cancer cells	612:631	gastric cancer cells	612:631	In the present study, we found that OGT was capable to interact with GNB2L1 directly and modify GNB2L1 with O-GlcNAcylation in gastric cancer, and this O-GlcNAcylation hindered the inhibition of GNB2L1 on migration of gastric cancer cells.
27530921	2	51	theme	GNB2L1	339:344	arg1	mechanisms					325:334	the regulatory mechanisms	310:334	the regulatory mechanisms of GNB2L1 in gastric cancer	310:362	However, the regulatory mechanisms of GNB2L1 in gastric cancer still remain largely elusive.
27530921	6	52	from	O-GlcNAcylation	1130:1144	arg1	GNB2L1					1149:1154	GNB2L1	1149:1154	GNB2L1	1149:1154	In summary, this study indicated the O-GlcNAcylation on GNB2L1 reversed its inhibition on gastric tumour metastasis via promoting its degradation.
27530921	5	53	theme	OGT	955:957	arg1	expression					959:968	OGT expression	955:968	OGT expression	955:968	In addition, the clinical data revealed the negative correlation of the protein level instead of the mRNA level of GNB2L1 with OGT expression, and showed that OGT reversed the inhibition of GNB2L1 on metastasis, and worsened the prognosis of GNB2L1(High) patients.
27530921	1	54	theme	intercellular	141:153	arg1	GNB2L1					128:133	GNB2L1	128:133	GNB2L1	128:133	GNB2L1 is an intercellular scaffold protein of the Trp-Asp (WD) repeat protein family, and has been reported to play suppressive roles in the progression of gastric cancer.
27530921	1	54	theme	intercellular	141:153	arg1	protein					164:170	an intercellular scaffold protein	138:170	an intercellular scaffold protein of the Trp-Asp (WD) repeat protein family	138:212	GNB2L1 is an intercellular scaffold protein of the Trp-Asp (WD) repeat protein family, and has been reported to play suppressive roles in the progression of gastric cancer.
25778404	2	0	theme	Trichoplax	497:506	arg1	adhaerens					508:516	the placozoan Trichoplax adhaerens	483:516	the placozoan Trichoplax adhaerens	483:516	In a search for a reductionist model to study O-GlcNAc signaling, we discovered the presence of functional O-GlcNAc transferase (OGT), O-GlcNAcase (OGA), and nucleocytoplasmic protein O-GlcNAcylation in the most basal extant animal, the placozoan Trichoplax adhaerens.
25778404	2	0	theme	Trichoplax	497:506	arg1	animal					475:480	the most basal extant animal	453:480	the most basal extant animal	453:480	In a search for a reductionist model to study O-GlcNAc signaling, we discovered the presence of functional O-GlcNAc transferase (OGT), O-GlcNAcase (OGA), and nucleocytoplasmic protein O-GlcNAcylation in the most basal extant animal, the placozoan Trichoplax adhaerens.
25778404	2	1	theme	placozoan	487:495	arg1	adhaerens					508:516	the placozoan Trichoplax adhaerens	483:516	the placozoan Trichoplax adhaerens	483:516	In a search for a reductionist model to study O-GlcNAc signaling, we discovered the presence of functional O-GlcNAc transferase (OGT), O-GlcNAcase (OGA), and nucleocytoplasmic protein O-GlcNAcylation in the most basal extant animal, the placozoan Trichoplax adhaerens.
25778404	2	1	theme	placozoan	487:495	arg1	animal					475:480	the most basal extant animal	453:480	the most basal extant animal	453:480	In a search for a reductionist model to study O-GlcNAc signaling, we discovered the presence of functional O-GlcNAc transferase (OGT), O-GlcNAcase (OGA), and nucleocytoplasmic protein O-GlcNAcylation in the most basal extant animal, the placozoan Trichoplax adhaerens.
25778404	4	2	theme	signaling	757:765	arg1	acquisition					733:743	The acquisition	729:743	The acquisition of O-GlcNAc signaling by metazoa	729:776	The acquisition of O-GlcNAc signaling by metazoa may have facilitated the rapid and complex signaling mechanisms required for the evolution of multicellular organisms.
25778404	3	3	theme	Trichoplax	561:570	arg1	OGT/OGA					572:578	Trichoplax OGT/OGA	561:578	Trichoplax OGT/OGA	561:578	We show via enzymatic characterization of Trichoplax OGT/OGA and genetic rescue experiments in Drosophila melanogaster that these proteins possess activities/functions similar to their bilaterian counterparts.
25778404	2	4	from	presence	334:341	arg1	adhaerens					508:516	the placozoan Trichoplax adhaerens	483:516	the placozoan Trichoplax adhaerens	483:516	In a search for a reductionist model to study O-GlcNAc signaling, we discovered the presence of functional O-GlcNAc transferase (OGT), O-GlcNAcase (OGA), and nucleocytoplasmic protein O-GlcNAcylation in the most basal extant animal, the placozoan Trichoplax adhaerens.
25778404	2	4	from	presence	334:341	arg1	animal					475:480	the most basal extant animal	453:480	the most basal extant animal	453:480	In a search for a reductionist model to study O-GlcNAc signaling, we discovered the presence of functional O-GlcNAc transferase (OGT), O-GlcNAcase (OGA), and nucleocytoplasmic protein O-GlcNAcylation in the most basal extant animal, the placozoan Trichoplax adhaerens.
25778404	4	5	theme	rapid	803:807	arg1	mechanisms					831:840	the rapid and complex signaling mechanisms	799:840	the rapid and complex signaling mechanisms required for the evolution of multicellular organisms	799:894	The acquisition of O-GlcNAc signaling by metazoa may have facilitated the rapid and complex signaling mechanisms required for the evolution of multicellular organisms.
25778404	4	6	theme	signaling	821:829	arg1	mechanisms					831:840	the rapid and complex signaling mechanisms	799:840	the rapid and complex signaling mechanisms required for the evolution of multicellular organisms	799:894	The acquisition of O-GlcNAc signaling by metazoa may have facilitated the rapid and complex signaling mechanisms required for the evolution of multicellular organisms.
25778404	3	7	theme	OGT/OGA	572:578	arg1	characterization					541:556	enzymatic characterization	531:556	enzymatic characterization of Trichoplax OGT/OGA	531:578	We show via enzymatic characterization of Trichoplax OGT/OGA and genetic rescue experiments in Drosophila melanogaster that these proteins possess activities/functions similar to their bilaterian counterparts.
25778404	3	7	theme	OGT/OGA	572:578	arg1	experiments					599:609	genetic rescue experiments	584:609	genetic rescue experiments in Drosophila melanogaster	584:636	We show via enzymatic characterization of Trichoplax OGT/OGA and genetic rescue experiments in Drosophila melanogaster that these proteins possess activities/functions similar to their bilaterian counterparts.
25778404	0	8	contain	Possesses	40:48	arg2	System					72:77	a Functional O-GlcNAc System	50:77	a Functional O-GlcNAc System	50:77	The Early Metazoan Trichoplax adhaerens Possesses a Functional O-GlcNAc System.
25778404	0	8	contain	Possesses	40:48	arg1	adhaerens					30:38	The Early Metazoan Trichoplax adhaerens	0:38	The Early Metazoan Trichoplax adhaerens	0:38	The Early Metazoan Trichoplax adhaerens Possesses a Functional O-GlcNAc System.
25778404	1	9	theme	Protein	80:86	arg1	modification					149:160	a reversible post-translational signaling modification	107:160	a reversible post-translational signaling modification of nucleocytoplasmic proteins that is essential for embryonic development in bilateria	107:247	Protein O-GlcNAcylation is a reversible post-translational signaling modification of nucleocytoplasmic proteins that is essential for embryonic development in bilateria.
25778404	1	9	theme	Protein	80:86	arg1	essential					200:208	essential	200:208	essential	200:208	Protein O-GlcNAcylation is a reversible post-translational signaling modification of nucleocytoplasmic proteins that is essential for embryonic development in bilateria.
25778404	1	9	theme	Protein	80:86	arg1	O-GlcNAcylation					88:102	Protein O-GlcNAcylation	80:102	Protein O-GlcNAcylation	80:102	Protein O-GlcNAcylation is a reversible post-translational signaling modification of nucleocytoplasmic proteins that is essential for embryonic development in bilateria.
25778404	1	10	mod	modification	149:160	arg1	proteins					183:190	nucleocytoplasmic proteins	165:190	nucleocytoplasmic proteins	165:190	Protein O-GlcNAcylation is a reversible post-translational signaling modification of nucleocytoplasmic proteins that is essential for embryonic development in bilateria.
25778404	1	10	mod	modification	149:160	arg3	signaling					139:147	a reversible post-translational signaling modification	107:160	a reversible post-translational signaling modification of nucleocytoplasmic proteins that is essential for embryonic development in bilateria	107:247	Protein O-GlcNAcylation is a reversible post-translational signaling modification of nucleocytoplasmic proteins that is essential for embryonic development in bilateria.
25778404	0	11	theme	Early	4:8	arg1	adhaerens					30:38	The Early Metazoan Trichoplax adhaerens	0:38	The Early Metazoan Trichoplax adhaerens	0:38	The Early Metazoan Trichoplax adhaerens Possesses a Functional O-GlcNAc System.
25778404	3	12	theme	enzymatic	531:539	arg1	characterization					541:556	enzymatic characterization	531:556	enzymatic characterization of Trichoplax OGT/OGA	531:578	We show via enzymatic characterization of Trichoplax OGT/OGA and genetic rescue experiments in Drosophila melanogaster that these proteins possess activities/functions similar to their bilaterian counterparts.
25778404	3	13	theme	rescue	592:597	arg1	experiments					599:609	genetic rescue experiments	584:609	genetic rescue experiments in Drosophila melanogaster	584:636	We show via enzymatic characterization of Trichoplax OGT/OGA and genetic rescue experiments in Drosophila melanogaster that these proteins possess activities/functions similar to their bilaterian counterparts.
25778404	1	14	theme	embryonic	214:222	arg1	development					224:234	embryonic development	214:234	embryonic development in bilateria	214:247	Protein O-GlcNAcylation is a reversible post-translational signaling modification of nucleocytoplasmic proteins that is essential for embryonic development in bilateria.
25778404	2	15	attach	presence	334:341	arg2	O-GlcNAcylation					434:448	nucleocytoplasmic protein O-GlcNAcylation	408:448	nucleocytoplasmic protein O-GlcNAcylation	408:448	In a search for a reductionist model to study O-GlcNAc signaling, we discovered the presence of functional O-GlcNAc transferase (OGT), O-GlcNAcase (OGA), and nucleocytoplasmic protein O-GlcNAcylation in the most basal extant animal, the placozoan Trichoplax adhaerens.
25778404	2	15	attach	presence	334:341	arg2	OGA					398:400	OGA	398:400	OGA	398:400	In a search for a reductionist model to study O-GlcNAc signaling, we discovered the presence of functional O-GlcNAc transferase (OGT), O-GlcNAcase (OGA), and nucleocytoplasmic protein O-GlcNAcylation in the most basal extant animal, the placozoan Trichoplax adhaerens.
25778404	2	15	attach	presence	334:341	arg2	transferase					366:376	functional O-GlcNAc transferase	346:376	functional O-GlcNAc transferase (OGT)	346:382	In a search for a reductionist model to study O-GlcNAc signaling, we discovered the presence of functional O-GlcNAc transferase (OGT), O-GlcNAcase (OGA), and nucleocytoplasmic protein O-GlcNAcylation in the most basal extant animal, the placozoan Trichoplax adhaerens.
25778404	2	15	attach	presence	334:341	arg1	adhaerens					508:516	the placozoan Trichoplax adhaerens	483:516	the placozoan Trichoplax adhaerens	483:516	In a search for a reductionist model to study O-GlcNAc signaling, we discovered the presence of functional O-GlcNAc transferase (OGT), O-GlcNAcase (OGA), and nucleocytoplasmic protein O-GlcNAcylation in the most basal extant animal, the placozoan Trichoplax adhaerens.
25778404	2	15	attach	presence	334:341	arg2	OGT					379:381	OGT	379:381	OGT	379:381	In a search for a reductionist model to study O-GlcNAc signaling, we discovered the presence of functional O-GlcNAc transferase (OGT), O-GlcNAcase (OGA), and nucleocytoplasmic protein O-GlcNAcylation in the most basal extant animal, the placozoan Trichoplax adhaerens.
25778404	2	15	attach	presence	334:341	arg2	O-GlcNAcase					385:395	O-GlcNAcase	385:395	O-GlcNAcase (OGA)	385:401	In a search for a reductionist model to study O-GlcNAc signaling, we discovered the presence of functional O-GlcNAc transferase (OGT), O-GlcNAcase (OGA), and nucleocytoplasmic protein O-GlcNAcylation in the most basal extant animal, the placozoan Trichoplax adhaerens.
25778404	2	15	attach	presence	334:341	arg1	animal					475:480	the most basal extant animal	453:480	the most basal extant animal	453:480	In a search for a reductionist model to study O-GlcNAc signaling, we discovered the presence of functional O-GlcNAc transferase (OGT), O-GlcNAcase (OGA), and nucleocytoplasmic protein O-GlcNAcylation in the most basal extant animal, the placozoan Trichoplax adhaerens.
25778404	0	16	theme	Trichoplax	19:28	arg1	adhaerens					30:38	The Early Metazoan Trichoplax adhaerens	0:38	The Early Metazoan Trichoplax adhaerens	0:38	The Early Metazoan Trichoplax adhaerens Possesses a Functional O-GlcNAc System.
25778404	4	17	theme	complex	813:819	arg1	mechanisms					831:840	the rapid and complex signaling mechanisms	799:840	the rapid and complex signaling mechanisms required for the evolution of multicellular organisms	799:894	The acquisition of O-GlcNAc signaling by metazoa may have facilitated the rapid and complex signaling mechanisms required for the evolution of multicellular organisms.
25778404	2	18	theme	O-GlcNAcylation	434:448	arg1	presence					334:341	the presence	330:341	the presence of functional O-GlcNAc transferase (OGT), O-GlcNAcase (OGA), and nucleocytoplasmic protein O-GlcNAcylation in the most basal extant animal, the placozoan Trichoplax adhaerens	330:516	In a search for a reductionist model to study O-GlcNAc signaling, we discovered the presence of functional O-GlcNAc transferase (OGT), O-GlcNAcase (OGA), and nucleocytoplasmic protein O-GlcNAcylation in the most basal extant animal, the placozoan Trichoplax adhaerens.
25778404	0	19	theme	Metazoan	10:17	arg1	adhaerens					30:38	The Early Metazoan Trichoplax adhaerens	0:38	The Early Metazoan Trichoplax adhaerens	0:38	The Early Metazoan Trichoplax adhaerens Possesses a Functional O-GlcNAc System.
25778404	2	20	theme	O-GlcNAcase	385:395	arg1	presence					334:341	the presence	330:341	the presence of functional O-GlcNAc transferase (OGT), O-GlcNAcase (OGA), and nucleocytoplasmic protein O-GlcNAcylation in the most basal extant animal, the placozoan Trichoplax adhaerens	330:516	In a search for a reductionist model to study O-GlcNAc signaling, we discovered the presence of functional O-GlcNAc transferase (OGT), O-GlcNAcase (OGA), and nucleocytoplasmic protein O-GlcNAcylation in the most basal extant animal, the placozoan Trichoplax adhaerens.
25778404	1	21	theme	reversible	109:118	arg1	modification					149:160	a reversible post-translational signaling modification	107:160	a reversible post-translational signaling modification of nucleocytoplasmic proteins that is essential for embryonic development in bilateria	107:247	Protein O-GlcNAcylation is a reversible post-translational signaling modification of nucleocytoplasmic proteins that is essential for embryonic development in bilateria.
25778404	1	21	theme	reversible	109:118	arg1	essential					200:208	essential	200:208	essential	200:208	Protein O-GlcNAcylation is a reversible post-translational signaling modification of nucleocytoplasmic proteins that is essential for embryonic development in bilateria.
25778404	1	21	theme	reversible	109:118	arg1	O-GlcNAcylation					88:102	Protein O-GlcNAcylation	80:102	Protein O-GlcNAcylation	80:102	Protein O-GlcNAcylation is a reversible post-translational signaling modification of nucleocytoplasmic proteins that is essential for embryonic development in bilateria.
25778404	2	22	theme	protein	426:432	arg1	O-GlcNAcylation					434:448	nucleocytoplasmic protein O-GlcNAcylation	408:448	nucleocytoplasmic protein O-GlcNAcylation	408:448	In a search for a reductionist model to study O-GlcNAc signaling, we discovered the presence of functional O-GlcNAc transferase (OGT), O-GlcNAcase (OGA), and nucleocytoplasmic protein O-GlcNAcylation in the most basal extant animal, the placozoan Trichoplax adhaerens.
25778404	2	23	theme	transferase	366:376	arg1	presence					334:341	the presence	330:341	the presence of functional O-GlcNAc transferase (OGT), O-GlcNAcase (OGA), and nucleocytoplasmic protein O-GlcNAcylation in the most basal extant animal, the placozoan Trichoplax adhaerens	330:516	In a search for a reductionist model to study O-GlcNAc signaling, we discovered the presence of functional O-GlcNAc transferase (OGT), O-GlcNAcase (OGA), and nucleocytoplasmic protein O-GlcNAcylation in the most basal extant animal, the placozoan Trichoplax adhaerens.
25778404	3	24	theme	bilaterian	704:713	arg1	counterparts					715:726	their bilaterian counterparts	698:726	their bilaterian counterparts	698:726	We show via enzymatic characterization of Trichoplax OGT/OGA and genetic rescue experiments in Drosophila melanogaster that these proteins possess activities/functions similar to their bilaterian counterparts.
25778404	2	25	theme	nucleocytoplasmic	408:424	arg1	O-GlcNAcylation					434:448	nucleocytoplasmic protein O-GlcNAcylation	408:448	nucleocytoplasmic protein O-GlcNAcylation	408:448	In a search for a reductionist model to study O-GlcNAc signaling, we discovered the presence of functional O-GlcNAc transferase (OGT), O-GlcNAcase (OGA), and nucleocytoplasmic protein O-GlcNAcylation in the most basal extant animal, the placozoan Trichoplax adhaerens.
25778404	4	26	theme	O-GlcNAc	748:755	arg1	signaling					757:765	O-GlcNAc signaling	748:765	O-GlcNAc signaling	748:765	The acquisition of O-GlcNAc signaling by metazoa may have facilitated the rapid and complex signaling mechanisms required for the evolution of multicellular organisms.
25778404	3	27	theme	similar	687:693	arg1	activities/functions					666:685	activities/functions	666:685	activities/functions similar to their bilaterian counterparts	666:726	We show via enzymatic characterization of Trichoplax OGT/OGA and genetic rescue experiments in Drosophila melanogaster that these proteins possess activities/functions similar to their bilaterian counterparts.
25778404	4	28	theme	organisms	886:894	arg1	evolution					859:867	the evolution	855:867	the evolution of multicellular organisms	855:894	The acquisition of O-GlcNAc signaling by metazoa may have facilitated the rapid and complex signaling mechanisms required for the evolution of multicellular organisms.
25778404	0	29	theme	Functional	52:61	arg1	System					72:77	a Functional O-GlcNAc System	50:77	a Functional O-GlcNAc System	50:77	The Early Metazoan Trichoplax adhaerens Possesses a Functional O-GlcNAc System.
25778404	2	30	theme	basal	462:466	arg1	adhaerens					508:516	the placozoan Trichoplax adhaerens	483:516	the placozoan Trichoplax adhaerens	483:516	In a search for a reductionist model to study O-GlcNAc signaling, we discovered the presence of functional O-GlcNAc transferase (OGT), O-GlcNAcase (OGA), and nucleocytoplasmic protein O-GlcNAcylation in the most basal extant animal, the placozoan Trichoplax adhaerens.
25778404	2	30	theme	basal	462:466	arg1	animal					475:480	the most basal extant animal	453:480	the most basal extant animal	453:480	In a search for a reductionist model to study O-GlcNAc signaling, we discovered the presence of functional O-GlcNAc transferase (OGT), O-GlcNAcase (OGA), and nucleocytoplasmic protein O-GlcNAcylation in the most basal extant animal, the placozoan Trichoplax adhaerens.
25778404	1	31	theme	post-translational	120:137	arg1	modification					149:160	a reversible post-translational signaling modification	107:160	a reversible post-translational signaling modification of nucleocytoplasmic proteins that is essential for embryonic development in bilateria	107:247	Protein O-GlcNAcylation is a reversible post-translational signaling modification of nucleocytoplasmic proteins that is essential for embryonic development in bilateria.
25778404	1	31	theme	post-translational	120:137	arg1	essential					200:208	essential	200:208	essential	200:208	Protein O-GlcNAcylation is a reversible post-translational signaling modification of nucleocytoplasmic proteins that is essential for embryonic development in bilateria.
25778404	1	31	theme	post-translational	120:137	arg1	O-GlcNAcylation					88:102	Protein O-GlcNAcylation	80:102	Protein O-GlcNAcylation	80:102	Protein O-GlcNAcylation is a reversible post-translational signaling modification of nucleocytoplasmic proteins that is essential for embryonic development in bilateria.
25778404	2	32	theme	extant	468:473	arg1	adhaerens					508:516	the placozoan Trichoplax adhaerens	483:516	the placozoan Trichoplax adhaerens	483:516	In a search for a reductionist model to study O-GlcNAc signaling, we discovered the presence of functional O-GlcNAc transferase (OGT), O-GlcNAcase (OGA), and nucleocytoplasmic protein O-GlcNAcylation in the most basal extant animal, the placozoan Trichoplax adhaerens.
25778404	2	32	theme	extant	468:473	arg1	animal					475:480	the most basal extant animal	453:480	the most basal extant animal	453:480	In a search for a reductionist model to study O-GlcNAc signaling, we discovered the presence of functional O-GlcNAc transferase (OGT), O-GlcNAcase (OGA), and nucleocytoplasmic protein O-GlcNAcylation in the most basal extant animal, the placozoan Trichoplax adhaerens.
25778404	1	33	theme	signaling	139:147	arg1	modification					149:160	a reversible post-translational signaling modification	107:160	a reversible post-translational signaling modification of nucleocytoplasmic proteins that is essential for embryonic development in bilateria	107:247	Protein O-GlcNAcylation is a reversible post-translational signaling modification of nucleocytoplasmic proteins that is essential for embryonic development in bilateria.
25778404	1	33	theme	signaling	139:147	arg1	essential					200:208	essential	200:208	essential	200:208	Protein O-GlcNAcylation is a reversible post-translational signaling modification of nucleocytoplasmic proteins that is essential for embryonic development in bilateria.
25778404	1	33	theme	signaling	139:147	arg1	O-GlcNAcylation					88:102	Protein O-GlcNAcylation	80:102	Protein O-GlcNAcylation	80:102	Protein O-GlcNAcylation is a reversible post-translational signaling modification of nucleocytoplasmic proteins that is essential for embryonic development in bilateria.
25778404	2	34	theme	O-GlcNAc	357:364	arg1	transferase					366:376	functional O-GlcNAc transferase	346:376	functional O-GlcNAc transferase (OGT)	346:382	In a search for a reductionist model to study O-GlcNAc signaling, we discovered the presence of functional O-GlcNAc transferase (OGT), O-GlcNAcase (OGA), and nucleocytoplasmic protein O-GlcNAcylation in the most basal extant animal, the placozoan Trichoplax adhaerens.
25778404	2	34	theme	O-GlcNAc	357:364	arg1	OGT					379:381	OGT	379:381	OGT	379:381	In a search for a reductionist model to study O-GlcNAc signaling, we discovered the presence of functional O-GlcNAc transferase (OGT), O-GlcNAcase (OGA), and nucleocytoplasmic protein O-GlcNAcylation in the most basal extant animal, the placozoan Trichoplax adhaerens.
25778404	2	35	theme	O-GlcNAc	296:303	arg1	signaling					305:313	O-GlcNAc signaling	296:313	O-GlcNAc signaling	296:313	In a search for a reductionist model to study O-GlcNAc signaling, we discovered the presence of functional O-GlcNAc transferase (OGT), O-GlcNAcase (OGA), and nucleocytoplasmic protein O-GlcNAcylation in the most basal extant animal, the placozoan Trichoplax adhaerens.
25778404	2	36	theme	functional	346:355	arg1	transferase					366:376	functional O-GlcNAc transferase	346:376	functional O-GlcNAc transferase (OGT)	346:382	In a search for a reductionist model to study O-GlcNAc signaling, we discovered the presence of functional O-GlcNAc transferase (OGT), O-GlcNAcase (OGA), and nucleocytoplasmic protein O-GlcNAcylation in the most basal extant animal, the placozoan Trichoplax adhaerens.
25778404	2	36	theme	functional	346:355	arg1	OGT					379:381	OGT	379:381	OGT	379:381	In a search for a reductionist model to study O-GlcNAc signaling, we discovered the presence of functional O-GlcNAc transferase (OGT), O-GlcNAcase (OGA), and nucleocytoplasmic protein O-GlcNAcylation in the most basal extant animal, the placozoan Trichoplax adhaerens.
25778404	3	37	theme	genetic	584:590	arg1	experiments					599:609	genetic rescue experiments	584:609	genetic rescue experiments in Drosophila melanogaster	584:636	We show via enzymatic characterization of Trichoplax OGT/OGA and genetic rescue experiments in Drosophila melanogaster that these proteins possess activities/functions similar to their bilaterian counterparts.
25778404	4	38	theme	multicellular	872:884	arg1	organisms					886:894	multicellular organisms	872:894	multicellular organisms	872:894	The acquisition of O-GlcNAc signaling by metazoa may have facilitated the rapid and complex signaling mechanisms required for the evolution of multicellular organisms.
25778404	1	39	from	development	224:234	arg1	bilateria					239:247	bilateria	239:247	bilateria	239:247	Protein O-GlcNAcylation is a reversible post-translational signaling modification of nucleocytoplasmic proteins that is essential for embryonic development in bilateria.
25778404	1	40	theme	nucleocytoplasmic	165:181	arg1	proteins					183:190	nucleocytoplasmic proteins	165:190	nucleocytoplasmic proteins	165:190	Protein O-GlcNAcylation is a reversible post-translational signaling modification of nucleocytoplasmic proteins that is essential for embryonic development in bilateria.
25778404	3	41	from	experiments	599:609	arg1	melanogaster					625:636	Drosophila melanogaster	614:636	Drosophila melanogaster	614:636	We show via enzymatic characterization of Trichoplax OGT/OGA and genetic rescue experiments in Drosophila melanogaster that these proteins possess activities/functions similar to their bilaterian counterparts.
25778404	0	42	theme	O-GlcNAc	63:70	arg1	System					72:77	a Functional O-GlcNAc System	50:77	a Functional O-GlcNAc System	50:77	The Early Metazoan Trichoplax adhaerens Possesses a Functional O-GlcNAc System.
25778404	2	43	theme	reductionist	268:279	arg1	model					281:285	a reductionist model	266:285	a reductionist model	266:285	In a search for a reductionist model to study O-GlcNAc signaling, we discovered the presence of functional O-GlcNAc transferase (OGT), O-GlcNAcase (OGA), and nucleocytoplasmic protein O-GlcNAcylation in the most basal extant animal, the placozoan Trichoplax adhaerens.
25778404	1	44	theme	proteins	183:190	arg1	modification					149:160	a reversible post-translational signaling modification	107:160	a reversible post-translational signaling modification of nucleocytoplasmic proteins that is essential for embryonic development in bilateria	107:247	Protein O-GlcNAcylation is a reversible post-translational signaling modification of nucleocytoplasmic proteins that is essential for embryonic development in bilateria.
25778404	1	44	theme	proteins	183:190	arg1	essential					200:208	essential	200:208	essential	200:208	Protein O-GlcNAcylation is a reversible post-translational signaling modification of nucleocytoplasmic proteins that is essential for embryonic development in bilateria.
25778404	1	44	theme	proteins	183:190	arg1	O-GlcNAcylation					88:102	Protein O-GlcNAcylation	80:102	Protein O-GlcNAcylation	80:102	Protein O-GlcNAcylation is a reversible post-translational signaling modification of nucleocytoplasmic proteins that is essential for embryonic development in bilateria.
25778404	3	45	from	characterization	541:556	arg1	melanogaster					625:636	Drosophila melanogaster	614:636	Drosophila melanogaster	614:636	We show via enzymatic characterization of Trichoplax OGT/OGA and genetic rescue experiments in Drosophila melanogaster that these proteins possess activities/functions similar to their bilaterian counterparts.
25778404	3	46	contain	possess	658:664	arg2	activities/functions					666:685	activities/functions	666:685	activities/functions similar to their bilaterian counterparts	666:726	We show via enzymatic characterization of Trichoplax OGT/OGA and genetic rescue experiments in Drosophila melanogaster that these proteins possess activities/functions similar to their bilaterian counterparts.
25778404	3	46	contain	possess	658:664	arg1	proteins					649:656	these proteins	643:656	these proteins	643:656	We show via enzymatic characterization of Trichoplax OGT/OGA and genetic rescue experiments in Drosophila melanogaster that these proteins possess activities/functions similar to their bilaterian counterparts.
28298630	6	0	theme	twofold	828:834	arg1	proteins					880:887	518 twofold up-regulated and 811 twofold down-regulated proteins	824:887	518 twofold up-regulated and 811 twofold down-regulated proteins common to both AUY922 and ganetespib treatment	824:934	Our proteomic study quantified 518 twofold up-regulated and 811 twofold down-regulated proteins common to both AUY922 and ganetespib treatment.
28298630	2	1	theme	clinical	296:303	arg1	trials					314:319	clinical oncology trials	296:319	clinical oncology trials	296:319	Several HSP90 inhibitors have shown promising effects in clinical oncology trials.
28298630	8	2	from	histone	1296:1302	arg1	AUY922-					1436:1442	AUY922-	1436:1442	AUY922-	1436:1442	Furthermore, quantitative proteome studies identified 14 types of PTMs with 93 marks on the core histones, including 34 novel histone marks of butyrylation, citrullination, 2-hydroxyisobutyrylation, methylation, O-GlcNAcylation, propionylation, and succinylation in AUY922- and ganetespib-treated 5637 cells.
28298630	8	2	from	histone	1296:1302	arg1	cells					1472:1476	ganetespib-treated 5637 cells	1448:1476	ganetespib-treated 5637 cells	1448:1476	Furthermore, quantitative proteome studies identified 14 types of PTMs with 93 marks on the core histones, including 34 novel histone marks of butyrylation, citrullination, 2-hydroxyisobutyrylation, methylation, O-GlcNAcylation, propionylation, and succinylation in AUY922- and ganetespib-treated 5637 cells.
28298630	8	3	theme	butyrylation	1313:1324	arg1	histone					1296:1302	34 novel histone marks	1287:1308	34 novel histone marks of butyrylation, citrullination, 2-hydroxyisobutyrylation, methylation, O-GlcNAcylation, propionylation, and succinylation in AUY922- and ganetespib-treated 5637 cells	1287:1476	Furthermore, quantitative proteome studies identified 14 types of PTMs with 93 marks on the core histones, including 34 novel histone marks of butyrylation, citrullination, 2-hydroxyisobutyrylation, methylation, O-GlcNAcylation, propionylation, and succinylation in AUY922- and ganetespib-treated 5637 cells.
28298630	6	4	theme	proteomic	797:805	arg1	study					807:811	Our proteomic study	793:811	Our proteomic study	793:811	Our proteomic study quantified 518 twofold up-regulated and 811 twofold down-regulated proteins common to both AUY922 and ganetespib treatment.
28298630	9	5	theme	histone	1555:1561	arg1	PTMs					1563:1566	histone PTMs	1555:1566	histone PTMs	1555:1566	Together, this study outlines the association between proteomic changes and histone PTMs in response to HSP90 inhibitor treatment in bladder carcinoma cells, and thus intensifies the understanding of HSP90 inhibition-mediated bladder cancer therapeutics.
28298630	8	6	theme	citrullination	1327:1340	arg1	histone					1296:1302	34 novel histone marks	1287:1308	34 novel histone marks of butyrylation, citrullination, 2-hydroxyisobutyrylation, methylation, O-GlcNAcylation, propionylation, and succinylation in AUY922- and ganetespib-treated 5637 cells	1287:1476	Furthermore, quantitative proteome studies identified 14 types of PTMs with 93 marks on the core histones, including 34 novel histone marks of butyrylation, citrullination, 2-hydroxyisobutyrylation, methylation, O-GlcNAcylation, propionylation, and succinylation in AUY922- and ganetespib-treated 5637 cells.
28298630	8	7	theme	2-hydroxyisobutyrylation	1343:1366	arg1	histone					1296:1302	34 novel histone marks	1287:1308	34 novel histone marks of butyrylation, citrullination, 2-hydroxyisobutyrylation, methylation, O-GlcNAcylation, propionylation, and succinylation in AUY922- and ganetespib-treated 5637 cells	1287:1476	Furthermore, quantitative proteome studies identified 14 types of PTMs with 93 marks on the core histones, including 34 novel histone marks of butyrylation, citrullination, 2-hydroxyisobutyrylation, methylation, O-GlcNAcylation, propionylation, and succinylation in AUY922- and ganetespib-treated 5637 cells.
28298630	8	8	theme	novel	1290:1294	arg1	histone					1296:1302	34 novel histone marks	1287:1308	34 novel histone marks of butyrylation, citrullination, 2-hydroxyisobutyrylation, methylation, O-GlcNAcylation, propionylation, and succinylation in AUY922- and ganetespib-treated 5637 cells	1287:1476	Furthermore, quantitative proteome studies identified 14 types of PTMs with 93 marks on the core histones, including 34 novel histone marks of butyrylation, citrullination, 2-hydroxyisobutyrylation, methylation, O-GlcNAcylation, propionylation, and succinylation in AUY922- and ganetespib-treated 5637 cells.
28298630	8	9	theme	methylation	1369:1379	arg1	histone					1296:1302	34 novel histone marks	1287:1308	34 novel histone marks of butyrylation, citrullination, 2-hydroxyisobutyrylation, methylation, O-GlcNAcylation, propionylation, and succinylation in AUY922- and ganetespib-treated 5637 cells	1287:1476	Furthermore, quantitative proteome studies identified 14 types of PTMs with 93 marks on the core histones, including 34 novel histone marks of butyrylation, citrullination, 2-hydroxyisobutyrylation, methylation, O-GlcNAcylation, propionylation, and succinylation in AUY922- and ganetespib-treated 5637 cells.
28298630	5	10	theme	bladder	729:735	arg1	cells					749:753	bladder cancer 5637 cells	729:753	bladder cancer 5637 cells	729:753	We show that 5 HSP90 inhibitors (AUY922, ganetespib, SNX2112, AT13387, and CUDC305) potently inhibited the proliferation of bladder cancer 5637 cells in a dose- and time-dependent manner.
28298630	2	11	theme	Several	239:245	arg1	inhibitors					253:262	Several HSP90 inhibitors	239:262	Several HSP90 inhibitors	239:262	Several HSP90 inhibitors have shown promising effects in clinical oncology trials.
28298630	7	12	theme	signaling	1080:1088	arg1	pathways					1160:1167	cell death-associated pathways	1138:1167	cell death-associated pathways	1138:1167	Bioinformatic analyses revealed that those differentially expressed proteins were involved in multiple cellular processes and enzyme-regulated signaling pathways, including chromatin modifications and cell death-associated pathways.
28298630	7	12	theme	signaling	1080:1088	arg1	modifications					1120:1132	chromatin modifications	1110:1132	chromatin modifications	1110:1132	Bioinformatic analyses revealed that those differentially expressed proteins were involved in multiple cellular processes and enzyme-regulated signaling pathways, including chromatin modifications and cell death-associated pathways.
28298630	7	12	theme	signaling	1080:1088	arg1	pathways					1090:1097	enzyme-regulated signaling pathways	1063:1097	enzyme-regulated signaling pathways	1063:1097	Bioinformatic analyses revealed that those differentially expressed proteins were involved in multiple cellular processes and enzyme-regulated signaling pathways, including chromatin modifications and cell death-associated pathways.
28298630	1	13	theme	cancer	221:226	arg1	treatment					228:236	cancer treatment	221:236	cancer treatment	221:236	Heat shock protein 90 (HSP90) inhibition is an attractive strategy for cancer treatment.
28298630	4	14	theme	protein	480:486	arg1	expression					488:497	protein expression	480:497	protein expression	480:497	Here, we report a quantitative proteomic study that evaluates alterations in protein expression and histone post-translational modifications (PTMs) in bladder carcinoma in response to HSP90 inhibition.
28298630	8	15	theme	O-GlcNAcylation	1382:1396	arg1	histone					1296:1302	34 novel histone marks	1287:1308	34 novel histone marks of butyrylation, citrullination, 2-hydroxyisobutyrylation, methylation, O-GlcNAcylation, propionylation, and succinylation in AUY922- and ganetespib-treated 5637 cells	1287:1476	Furthermore, quantitative proteome studies identified 14 types of PTMs with 93 marks on the core histones, including 34 novel histone marks of butyrylation, citrullination, 2-hydroxyisobutyrylation, methylation, O-GlcNAcylation, propionylation, and succinylation in AUY922- and ganetespib-treated 5637 cells.
28298630	8	16	from	butyrylation	1313:1324	arg1	AUY922-					1436:1442	AUY922-	1436:1442	AUY922-	1436:1442	Furthermore, quantitative proteome studies identified 14 types of PTMs with 93 marks on the core histones, including 34 novel histone marks of butyrylation, citrullination, 2-hydroxyisobutyrylation, methylation, O-GlcNAcylation, propionylation, and succinylation in AUY922- and ganetespib-treated 5637 cells.
28298630	8	16	from	butyrylation	1313:1324	arg1	cells					1472:1476	ganetespib-treated 5637 cells	1448:1476	ganetespib-treated 5637 cells	1448:1476	Furthermore, quantitative proteome studies identified 14 types of PTMs with 93 marks on the core histones, including 34 novel histone marks of butyrylation, citrullination, 2-hydroxyisobutyrylation, methylation, O-GlcNAcylation, propionylation, and succinylation in AUY922- and ganetespib-treated 5637 cells.
28298630	4	17	theme	proteomic	434:442	arg1	study					444:448	a quantitative proteomic study	419:448	a quantitative proteomic study that evaluates alterations in protein expression and histone post-translational modifications (PTMs) in bladder carcinoma in response to HSP90 inhibition	419:602	Here, we report a quantitative proteomic study that evaluates alterations in protein expression and histone post-translational modifications (PTMs) in bladder carcinoma in response to HSP90 inhibition.
28298630	8	18	theme	propionylation	1399:1412	arg1	histone					1296:1302	34 novel histone marks	1287:1308	34 novel histone marks of butyrylation, citrullination, 2-hydroxyisobutyrylation, methylation, O-GlcNAcylation, propionylation, and succinylation in AUY922- and ganetespib-treated 5637 cells	1287:1476	Furthermore, quantitative proteome studies identified 14 types of PTMs with 93 marks on the core histones, including 34 novel histone marks of butyrylation, citrullination, 2-hydroxyisobutyrylation, methylation, O-GlcNAcylation, propionylation, and succinylation in AUY922- and ganetespib-treated 5637 cells.
28298630	7	19	theme	cellular	1040:1047	arg1	pathways					1160:1167	cell death-associated pathways	1138:1167	cell death-associated pathways	1138:1167	Bioinformatic analyses revealed that those differentially expressed proteins were involved in multiple cellular processes and enzyme-regulated signaling pathways, including chromatin modifications and cell death-associated pathways.
28298630	7	19	theme	cellular	1040:1047	arg1	processes					1049:1057	multiple cellular processes	1031:1057	multiple cellular processes	1031:1057	Bioinformatic analyses revealed that those differentially expressed proteins were involved in multiple cellular processes and enzyme-regulated signaling pathways, including chromatin modifications and cell death-associated pathways.
28298630	7	19	theme	cellular	1040:1047	arg1	modifications					1120:1132	chromatin modifications	1110:1132	chromatin modifications	1110:1132	Bioinformatic analyses revealed that those differentially expressed proteins were involved in multiple cellular processes and enzyme-regulated signaling pathways, including chromatin modifications and cell death-associated pathways.
28298630	1	20	theme	shock	155:159	arg1	protein					161:167	Heat shock protein 90	150:170	Heat shock protein 90 (HSP90) inhibition	150:189	Heat shock protein 90 (HSP90) inhibition is an attractive strategy for cancer treatment.
28298630	1	20	theme	shock	155:159	arg1	HSP90					173:177	HSP90	173:177	HSP90	173:177	Heat shock protein 90 (HSP90) inhibition is an attractive strategy for cancer treatment.
28298630	9	21	theme	bladder	1612:1618	arg1	cells					1630:1634	bladder carcinoma cells	1612:1634	bladder carcinoma cells	1612:1634	Together, this study outlines the association between proteomic changes and histone PTMs in response to HSP90 inhibitor treatment in bladder carcinoma cells, and thus intensifies the understanding of HSP90 inhibition-mediated bladder cancer therapeutics.
28298630	9	22	theme	inhibitor	1589:1597	arg1	treatment					1599:1607	HSP90 inhibitor treatment	1583:1607	HSP90 inhibitor treatment	1583:1607	Together, this study outlines the association between proteomic changes and histone PTMs in response to HSP90 inhibitor treatment in bladder carcinoma cells, and thus intensifies the understanding of HSP90 inhibition-mediated bladder cancer therapeutics.
28298630	8	23	from	2-hydroxyisobutyrylation	1343:1366	arg1	AUY922-					1436:1442	AUY922-	1436:1442	AUY922-	1436:1442	Furthermore, quantitative proteome studies identified 14 types of PTMs with 93 marks on the core histones, including 34 novel histone marks of butyrylation, citrullination, 2-hydroxyisobutyrylation, methylation, O-GlcNAcylation, propionylation, and succinylation in AUY922- and ganetespib-treated 5637 cells.
28298630	8	23	from	2-hydroxyisobutyrylation	1343:1366	arg1	cells					1472:1476	ganetespib-treated 5637 cells	1448:1476	ganetespib-treated 5637 cells	1448:1476	Furthermore, quantitative proteome studies identified 14 types of PTMs with 93 marks on the core histones, including 34 novel histone marks of butyrylation, citrullination, 2-hydroxyisobutyrylation, methylation, O-GlcNAcylation, propionylation, and succinylation in AUY922- and ganetespib-treated 5637 cells.
28298630	0	24	theme	shock	84:88	arg1	protein					90:96	heat shock protein 90	79:99	heat shock protein 90	79:99	Proteomic analysis of proteome and histone post-translational modifications in heat shock protein 90 inhibition-mediated bladder cancer therapeutics.
28298630	8	25	from	propionylation	1399:1412	arg1	AUY922-					1436:1442	AUY922-	1436:1442	AUY922-	1436:1442	Furthermore, quantitative proteome studies identified 14 types of PTMs with 93 marks on the core histones, including 34 novel histone marks of butyrylation, citrullination, 2-hydroxyisobutyrylation, methylation, O-GlcNAcylation, propionylation, and succinylation in AUY922- and ganetespib-treated 5637 cells.
28298630	8	25	from	propionylation	1399:1412	arg1	cells					1472:1476	ganetespib-treated 5637 cells	1448:1476	ganetespib-treated 5637 cells	1448:1476	Furthermore, quantitative proteome studies identified 14 types of PTMs with 93 marks on the core histones, including 34 novel histone marks of butyrylation, citrullination, 2-hydroxyisobutyrylation, methylation, O-GlcNAcylation, propionylation, and succinylation in AUY922- and ganetespib-treated 5637 cells.
28298630	3	26	theme	bladder	379:385	arg1	therapy					394:400	HSP90 inhibition-mediated bladder cancer therapy	353:400	HSP90 inhibition-mediated bladder cancer therapy	353:400	However, little is known about HSP90 inhibition-mediated bladder cancer therapy.
28298630	8	27	from	methylation	1369:1379	arg1	AUY922-					1436:1442	AUY922-	1436:1442	AUY922-	1436:1442	Furthermore, quantitative proteome studies identified 14 types of PTMs with 93 marks on the core histones, including 34 novel histone marks of butyrylation, citrullination, 2-hydroxyisobutyrylation, methylation, O-GlcNAcylation, propionylation, and succinylation in AUY922- and ganetespib-treated 5637 cells.
28298630	8	27	from	methylation	1369:1379	arg1	cells					1472:1476	ganetespib-treated 5637 cells	1448:1476	ganetespib-treated 5637 cells	1448:1476	Furthermore, quantitative proteome studies identified 14 types of PTMs with 93 marks on the core histones, including 34 novel histone marks of butyrylation, citrullination, 2-hydroxyisobutyrylation, methylation, O-GlcNAcylation, propionylation, and succinylation in AUY922- and ganetespib-treated 5637 cells.
28298630	7	28	theme	expressed	995:1003	arg1	proteins					1005:1012	those differentially expressed proteins	974:1012	those differentially expressed proteins	974:1012	Bioinformatic analyses revealed that those differentially expressed proteins were involved in multiple cellular processes and enzyme-regulated signaling pathways, including chromatin modifications and cell death-associated pathways.
28298630	9	29	theme	carcinoma	1620:1628	arg1	cells					1630:1634	bladder carcinoma cells	1612:1634	bladder carcinoma cells	1612:1634	Together, this study outlines the association between proteomic changes and histone PTMs in response to HSP90 inhibitor treatment in bladder carcinoma cells, and thus intensifies the understanding of HSP90 inhibition-mediated bladder cancer therapeutics.
28298630	3	30	theme	HSP90	353:357	arg1	therapy					394:400	HSP90 inhibition-mediated bladder cancer therapy	353:400	HSP90 inhibition-mediated bladder cancer therapy	353:400	However, little is known about HSP90 inhibition-mediated bladder cancer therapy.
28298630	0	31	theme	bladder	121:127	arg1	therapeutics					136:147	bladder cancer therapeutics	121:147	bladder cancer therapeutics	121:147	Proteomic analysis of proteome and histone post-translational modifications in heat shock protein 90 inhibition-mediated bladder cancer therapeutics.
28298630	4	32	theme	post-translational	511:528	arg1	PTMs					545:548	PTMs	545:548	PTMs	545:548	Here, we report a quantitative proteomic study that evaluates alterations in protein expression and histone post-translational modifications (PTMs) in bladder carcinoma in response to HSP90 inhibition.
28298630	4	32	theme	post-translational	511:528	arg1	modifications					530:542	histone post-translational modifications	503:542	histone post-translational modifications (PTMs) in bladder carcinoma in response to HSP90 inhibition	503:602	Here, we report a quantitative proteomic study that evaluates alterations in protein expression and histone post-translational modifications (PTMs) in bladder carcinoma in response to HSP90 inhibition.
28298630	0	33	theme	Proteomic	0:8	arg1	analysis					10:17	Proteomic analysis	0:17	Proteomic analysis of proteome and histone post-translational modifications in heat shock protein 90	0:99	Proteomic analysis of proteome and histone post-translational modifications in heat shock protein 90 inhibition-mediated bladder cancer therapeutics.
28298630	9	34	theme	inhibition-mediated	1685:1703	arg1	therapeutics					1720:1731	HSP90 inhibition-mediated bladder cancer therapeutics	1679:1731	HSP90 inhibition-mediated bladder cancer therapeutics	1679:1731	Together, this study outlines the association between proteomic changes and histone PTMs in response to HSP90 inhibitor treatment in bladder carcinoma cells, and thus intensifies the understanding of HSP90 inhibition-mediated bladder cancer therapeutics.
28298630	9	35	from	changes	1543:1549	arg1	response					1571:1578	response	1571:1578	response to HSP90 inhibitor treatment in bladder carcinoma cells	1571:1634	Together, this study outlines the association between proteomic changes and histone PTMs in response to HSP90 inhibitor treatment in bladder carcinoma cells, and thus intensifies the understanding of HSP90 inhibition-mediated bladder cancer therapeutics.
28298630	9	36	theme	cancer	1713:1718	arg1	therapeutics					1720:1731	HSP90 inhibition-mediated bladder cancer therapeutics	1679:1731	HSP90 inhibition-mediated bladder cancer therapeutics	1679:1731	Together, this study outlines the association between proteomic changes and histone PTMs in response to HSP90 inhibitor treatment in bladder carcinoma cells, and thus intensifies the understanding of HSP90 inhibition-mediated bladder cancer therapeutics.
28298630	4	37	theme	bladder	554:560	arg1	carcinoma					562:570	bladder carcinoma	554:570	bladder carcinoma	554:570	Here, we report a quantitative proteomic study that evaluates alterations in protein expression and histone post-translational modifications (PTMs) in bladder carcinoma in response to HSP90 inhibition.
28298630	0	38	theme	post-translational	43:60	arg1	modifications					62:74	histone post-translational modifications	35:74	histone post-translational modifications in heat shock protein 90	35:99	Proteomic analysis of proteome and histone post-translational modifications in heat shock protein 90 inhibition-mediated bladder cancer therapeutics.
28298630	8	39	theme	proteome	1196:1203	arg1	studies					1205:1211	quantitative proteome studies	1183:1211	quantitative proteome studies	1183:1211	Furthermore, quantitative proteome studies identified 14 types of PTMs with 93 marks on the core histones, including 34 novel histone marks of butyrylation, citrullination, 2-hydroxyisobutyrylation, methylation, O-GlcNAcylation, propionylation, and succinylation in AUY922- and ganetespib-treated 5637 cells.
28298630	9	40	from	response	1571:1578	arg1	cells					1630:1634	bladder carcinoma cells	1612:1634	bladder carcinoma cells	1612:1634	Together, this study outlines the association between proteomic changes and histone PTMs in response to HSP90 inhibitor treatment in bladder carcinoma cells, and thus intensifies the understanding of HSP90 inhibition-mediated bladder cancer therapeutics.
28298630	9	41	from	PTMs	1563:1566	arg1	response					1571:1578	response	1571:1578	response to HSP90 inhibitor treatment in bladder carcinoma cells	1571:1634	Together, this study outlines the association between proteomic changes and histone PTMs in response to HSP90 inhibitor treatment in bladder carcinoma cells, and thus intensifies the understanding of HSP90 inhibition-mediated bladder cancer therapeutics.
28298630	8	42	from	AUY922-	1436:1442	arg1	histone					1296:1302	34 novel histone marks	1287:1308	34 novel histone marks of butyrylation, citrullination, 2-hydroxyisobutyrylation, methylation, O-GlcNAcylation, propionylation, and succinylation in AUY922- and ganetespib-treated 5637 cells	1287:1476	Furthermore, quantitative proteome studies identified 14 types of PTMs with 93 marks on the core histones, including 34 novel histone marks of butyrylation, citrullination, 2-hydroxyisobutyrylation, methylation, O-GlcNAcylation, propionylation, and succinylation in AUY922- and ganetespib-treated 5637 cells.
28298630	8	43	theme	PTMs	1236:1239	arg1	types					1227:1231	14 types	1224:1231	14 types of PTMs	1224:1239	Furthermore, quantitative proteome studies identified 14 types of PTMs with 93 marks on the core histones, including 34 novel histone marks of butyrylation, citrullination, 2-hydroxyisobutyrylation, methylation, O-GlcNAcylation, propionylation, and succinylation in AUY922- and ganetespib-treated 5637 cells.
28298630	2	44	theme	oncology	305:312	arg1	trials					314:319	clinical oncology trials	296:319	clinical oncology trials	296:319	Several HSP90 inhibitors have shown promising effects in clinical oncology trials.
28298630	8	45	from	cells	1472:1476	arg1	histone					1296:1302	34 novel histone marks	1287:1308	34 novel histone marks of butyrylation, citrullination, 2-hydroxyisobutyrylation, methylation, O-GlcNAcylation, propionylation, and succinylation in AUY922- and ganetespib-treated 5637 cells	1287:1476	Furthermore, quantitative proteome studies identified 14 types of PTMs with 93 marks on the core histones, including 34 novel histone marks of butyrylation, citrullination, 2-hydroxyisobutyrylation, methylation, O-GlcNAcylation, propionylation, and succinylation in AUY922- and ganetespib-treated 5637 cells.
28298630	9	46	theme	proteomic	1533:1541	arg1	changes					1543:1549	proteomic changes	1533:1549	proteomic changes	1533:1549	Together, this study outlines the association between proteomic changes and histone PTMs in response to HSP90 inhibitor treatment in bladder carcinoma cells, and thus intensifies the understanding of HSP90 inhibition-mediated bladder cancer therapeutics.
28298630	6	47	theme	ganetespib	915:924	arg1	treatment					926:934	ganetespib treatment	915:934	ganetespib treatment	915:934	Our proteomic study quantified 518 twofold up-regulated and 811 twofold down-regulated proteins common to both AUY922 and ganetespib treatment.
28298630	4	48	theme	quantitative	421:432	arg1	study					444:448	a quantitative proteomic study	419:448	a quantitative proteomic study that evaluates alterations in protein expression and histone post-translational modifications (PTMs) in bladder carcinoma in response to HSP90 inhibition	419:602	Here, we report a quantitative proteomic study that evaluates alterations in protein expression and histone post-translational modifications (PTMs) in bladder carcinoma in response to HSP90 inhibition.
28298630	4	49	from	modifications	530:542	arg1	response					575:582	response	575:582	response to HSP90 inhibition	575:602	Here, we report a quantitative proteomic study that evaluates alterations in protein expression and histone post-translational modifications (PTMs) in bladder carcinoma in response to HSP90 inhibition.
28298630	4	49	from	modifications	530:542	arg1	carcinoma					562:570	bladder carcinoma	554:570	bladder carcinoma	554:570	Here, we report a quantitative proteomic study that evaluates alterations in protein expression and histone post-translational modifications (PTMs) in bladder carcinoma in response to HSP90 inhibition.
28298630	5	50	theme	time-dependent	770:783	arg1	manner					785:790	time-dependent manner	770:790	time-dependent manner	770:790	We show that 5 HSP90 inhibitors (AUY922, ganetespib, SNX2112, AT13387, and CUDC305) potently inhibited the proliferation of bladder cancer 5637 cells in a dose- and time-dependent manner.
28298630	8	51	theme	core	1262:1265	arg1	histone					1296:1302	34 novel histone marks	1287:1308	34 novel histone marks of butyrylation, citrullination, 2-hydroxyisobutyrylation, methylation, O-GlcNAcylation, propionylation, and succinylation in AUY922- and ganetespib-treated 5637 cells	1287:1476	Furthermore, quantitative proteome studies identified 14 types of PTMs with 93 marks on the core histones, including 34 novel histone marks of butyrylation, citrullination, 2-hydroxyisobutyrylation, methylation, O-GlcNAcylation, propionylation, and succinylation in AUY922- and ganetespib-treated 5637 cells.
28298630	8	51	theme	core	1262:1265	arg1	histones					1267:1274	the core histones	1258:1274	the core histones	1258:1274	Furthermore, quantitative proteome studies identified 14 types of PTMs with 93 marks on the core histones, including 34 novel histone marks of butyrylation, citrullination, 2-hydroxyisobutyrylation, methylation, O-GlcNAcylation, propionylation, and succinylation in AUY922- and ganetespib-treated 5637 cells.
28298630	4	52	from	expression	488:497	arg1	response					575:582	response	575:582	response to HSP90 inhibition	575:602	Here, we report a quantitative proteomic study that evaluates alterations in protein expression and histone post-translational modifications (PTMs) in bladder carcinoma in response to HSP90 inhibition.
28298630	4	52	from	expression	488:497	arg1	carcinoma					562:570	bladder carcinoma	554:570	bladder carcinoma	554:570	Here, we report a quantitative proteomic study that evaluates alterations in protein expression and histone post-translational modifications (PTMs) in bladder carcinoma in response to HSP90 inhibition.
28298630	5	53	theme	HSP90	620:624	arg1	inhibitors					626:635	5 HSP90 inhibitors	618:635	5 HSP90 inhibitors (AUY922, ganetespib, SNX2112, AT13387, and CUDC305)	618:687	We show that 5 HSP90 inhibitors (AUY922, ganetespib, SNX2112, AT13387, and CUDC305) potently inhibited the proliferation of bladder cancer 5637 cells in a dose- and time-dependent manner.
28298630	5	53	theme	HSP90	620:624	arg1	CUDC305					680:686	CUDC305	680:686	CUDC305	680:686	We show that 5 HSP90 inhibitors (AUY922, ganetespib, SNX2112, AT13387, and CUDC305) potently inhibited the proliferation of bladder cancer 5637 cells in a dose- and time-dependent manner.
28298630	5	53	theme	HSP90	620:624	arg1	AT13387					667:673	AT13387	667:673	AT13387	667:673	We show that 5 HSP90 inhibitors (AUY922, ganetespib, SNX2112, AT13387, and CUDC305) potently inhibited the proliferation of bladder cancer 5637 cells in a dose- and time-dependent manner.
28298630	1	54	theme	attractive	197:206	arg1	strategy					208:215	an attractive strategy	194:215	an attractive strategy for cancer treatment	194:236	Heat shock protein 90 (HSP90) inhibition is an attractive strategy for cancer treatment.
28298630	1	54	theme	attractive	197:206	arg1	inhibition					180:189	Heat shock protein 90 (HSP90) inhibition	150:189	Heat shock protein 90 (HSP90) inhibition	150:189	Heat shock protein 90 (HSP90) inhibition is an attractive strategy for cancer treatment.
28298630	0	55	from	protein	90:96	arg1	analysis					10:17	Proteomic analysis	0:17	Proteomic analysis of proteome and histone post-translational modifications in heat shock protein 90	0:99	Proteomic analysis of proteome and histone post-translational modifications in heat shock protein 90 inhibition-mediated bladder cancer therapeutics.
28298630	2	56	theme	HSP90	247:251	arg1	inhibitors					253:262	Several HSP90 inhibitors	239:262	Several HSP90 inhibitors	239:262	Several HSP90 inhibitors have shown promising effects in clinical oncology trials.
28298630	9	57	theme	HSP90	1583:1587	arg1	treatment					1599:1607	HSP90 inhibitor treatment	1583:1607	HSP90 inhibitor treatment	1583:1607	Together, this study outlines the association between proteomic changes and histone PTMs in response to HSP90 inhibitor treatment in bladder carcinoma cells, and thus intensifies the understanding of HSP90 inhibition-mediated bladder cancer therapeutics.
28298630	8	58	theme	34	1287:1288	arg1	histone					1296:1302	34 novel histone marks	1287:1308	34 novel histone marks of butyrylation, citrullination, 2-hydroxyisobutyrylation, methylation, O-GlcNAcylation, propionylation, and succinylation in AUY922- and ganetespib-treated 5637 cells	1287:1476	Furthermore, quantitative proteome studies identified 14 types of PTMs with 93 marks on the core histones, including 34 novel histone marks of butyrylation, citrullination, 2-hydroxyisobutyrylation, methylation, O-GlcNAcylation, propionylation, and succinylation in AUY922- and ganetespib-treated 5637 cells.
28298630	7	59	theme	chromatin	1110:1118	arg1	modifications					1120:1132	chromatin modifications	1110:1132	chromatin modifications	1110:1132	Bioinformatic analyses revealed that those differentially expressed proteins were involved in multiple cellular processes and enzyme-regulated signaling pathways, including chromatin modifications and cell death-associated pathways.
28298630	7	60	theme	death-associated	1143:1158	arg1	pathways					1160:1167	cell death-associated pathways	1138:1167	cell death-associated pathways	1138:1167	Bioinformatic analyses revealed that those differentially expressed proteins were involved in multiple cellular processes and enzyme-regulated signaling pathways, including chromatin modifications and cell death-associated pathways.
28298630	2	61	theme	promising	275:283	arg1	effects					285:291	promising effects	275:291	promising effects	275:291	Several HSP90 inhibitors have shown promising effects in clinical oncology trials.
28298630	7	62	theme	enzyme-regulated	1063:1078	arg1	pathways					1160:1167	cell death-associated pathways	1138:1167	cell death-associated pathways	1138:1167	Bioinformatic analyses revealed that those differentially expressed proteins were involved in multiple cellular processes and enzyme-regulated signaling pathways, including chromatin modifications and cell death-associated pathways.
28298630	7	62	theme	enzyme-regulated	1063:1078	arg1	modifications					1120:1132	chromatin modifications	1110:1132	chromatin modifications	1110:1132	Bioinformatic analyses revealed that those differentially expressed proteins were involved in multiple cellular processes and enzyme-regulated signaling pathways, including chromatin modifications and cell death-associated pathways.
28298630	7	62	theme	enzyme-regulated	1063:1078	arg1	pathways					1090:1097	enzyme-regulated signaling pathways	1063:1097	enzyme-regulated signaling pathways	1063:1097	Bioinformatic analyses revealed that those differentially expressed proteins were involved in multiple cellular processes and enzyme-regulated signaling pathways, including chromatin modifications and cell death-associated pathways.
28298630	1	63	theme	Heat	150:153	arg1	protein					161:167	Heat shock protein 90	150:170	Heat shock protein 90 (HSP90) inhibition	150:189	Heat shock protein 90 (HSP90) inhibition is an attractive strategy for cancer treatment.
28298630	1	63	theme	Heat	150:153	arg1	HSP90					173:177	HSP90	173:177	HSP90	173:177	Heat shock protein 90 (HSP90) inhibition is an attractive strategy for cancer treatment.
28298630	0	64	theme	heat	79:82	arg1	protein					90:96	heat shock protein 90	79:99	heat shock protein 90	79:99	Proteomic analysis of proteome and histone post-translational modifications in heat shock protein 90 inhibition-mediated bladder cancer therapeutics.
28298630	1	65	theme	protein	161:167	arg1	strategy					208:215	an attractive strategy	194:215	an attractive strategy for cancer treatment	194:236	Heat shock protein 90 (HSP90) inhibition is an attractive strategy for cancer treatment.
28298630	1	65	theme	protein	161:167	arg1	inhibition					180:189	Heat shock protein 90 (HSP90) inhibition	150:189	Heat shock protein 90 (HSP90) inhibition	150:189	Heat shock protein 90 (HSP90) inhibition is an attractive strategy for cancer treatment.
28298630	0	66	from	proteome	22:29	arg1	protein					90:96	heat shock protein 90	79:99	heat shock protein 90	79:99	Proteomic analysis of proteome and histone post-translational modifications in heat shock protein 90 inhibition-mediated bladder cancer therapeutics.
28298630	7	67	theme	multiple	1031:1038	arg1	pathways					1160:1167	cell death-associated pathways	1138:1167	cell death-associated pathways	1138:1167	Bioinformatic analyses revealed that those differentially expressed proteins were involved in multiple cellular processes and enzyme-regulated signaling pathways, including chromatin modifications and cell death-associated pathways.
28298630	7	67	theme	multiple	1031:1038	arg1	processes					1049:1057	multiple cellular processes	1031:1057	multiple cellular processes	1031:1057	Bioinformatic analyses revealed that those differentially expressed proteins were involved in multiple cellular processes and enzyme-regulated signaling pathways, including chromatin modifications and cell death-associated pathways.
28298630	7	67	theme	multiple	1031:1038	arg1	modifications					1120:1132	chromatin modifications	1110:1132	chromatin modifications	1110:1132	Bioinformatic analyses revealed that those differentially expressed proteins were involved in multiple cellular processes and enzyme-regulated signaling pathways, including chromatin modifications and cell death-associated pathways.
28298630	0	68	from	modifications	62:74	arg1	protein					90:96	heat shock protein 90	79:99	heat shock protein 90	79:99	Proteomic analysis of proteome and histone post-translational modifications in heat shock protein 90 inhibition-mediated bladder cancer therapeutics.
28298630	0	69	from	analysis	10:17	arg1	protein					90:96	heat shock protein 90	79:99	heat shock protein 90	79:99	Proteomic analysis of proteome and histone post-translational modifications in heat shock protein 90 inhibition-mediated bladder cancer therapeutics.
28298630	8	70	theme	succinylation	1419:1431	arg1	histone					1296:1302	34 novel histone marks	1287:1308	34 novel histone marks of butyrylation, citrullination, 2-hydroxyisobutyrylation, methylation, O-GlcNAcylation, propionylation, and succinylation in AUY922- and ganetespib-treated 5637 cells	1287:1476	Furthermore, quantitative proteome studies identified 14 types of PTMs with 93 marks on the core histones, including 34 novel histone marks of butyrylation, citrullination, 2-hydroxyisobutyrylation, methylation, O-GlcNAcylation, propionylation, and succinylation in AUY922- and ganetespib-treated 5637 cells.
28298630	5	71	theme	cancer	737:742	arg1	cells					749:753	bladder cancer 5637 cells	729:753	bladder cancer 5637 cells	729:753	We show that 5 HSP90 inhibitors (AUY922, ganetespib, SNX2112, AT13387, and CUDC305) potently inhibited the proliferation of bladder cancer 5637 cells in a dose- and time-dependent manner.
28298630	8	72	from	O-GlcNAcylation	1382:1396	arg1	AUY922-					1436:1442	AUY922-	1436:1442	AUY922-	1436:1442	Furthermore, quantitative proteome studies identified 14 types of PTMs with 93 marks on the core histones, including 34 novel histone marks of butyrylation, citrullination, 2-hydroxyisobutyrylation, methylation, O-GlcNAcylation, propionylation, and succinylation in AUY922- and ganetespib-treated 5637 cells.
28298630	8	72	from	O-GlcNAcylation	1382:1396	arg1	cells					1472:1476	ganetespib-treated 5637 cells	1448:1476	ganetespib-treated 5637 cells	1448:1476	Furthermore, quantitative proteome studies identified 14 types of PTMs with 93 marks on the core histones, including 34 novel histone marks of butyrylation, citrullination, 2-hydroxyisobutyrylation, methylation, O-GlcNAcylation, propionylation, and succinylation in AUY922- and ganetespib-treated 5637 cells.
28298630	3	73	theme	cancer	387:392	arg1	therapy					394:400	HSP90 inhibition-mediated bladder cancer therapy	353:400	HSP90 inhibition-mediated bladder cancer therapy	353:400	However, little is known about HSP90 inhibition-mediated bladder cancer therapy.
28298630	4	74	theme	histone	503:509	arg1	PTMs					545:548	PTMs	545:548	PTMs	545:548	Here, we report a quantitative proteomic study that evaluates alterations in protein expression and histone post-translational modifications (PTMs) in bladder carcinoma in response to HSP90 inhibition.
28298630	4	74	theme	histone	503:509	arg1	modifications					530:542	histone post-translational modifications	503:542	histone post-translational modifications (PTMs) in bladder carcinoma in response to HSP90 inhibition	503:602	Here, we report a quantitative proteomic study that evaluates alterations in protein expression and histone post-translational modifications (PTMs) in bladder carcinoma in response to HSP90 inhibition.
28298630	8	75	dep	93	1246:1247	arg1	marks					1249:1253	marks	1249:1253	marks on the core histones, including 34 novel histone marks of butyrylation, citrullination, 2-hydroxyisobutyrylation, methylation, O-GlcNAcylation, propionylation, and succinylation in AUY922- and ganetespib-treated 5637 cells	1249:1476	Furthermore, quantitative proteome studies identified 14 types of PTMs with 93 marks on the core histones, including 34 novel histone marks of butyrylation, citrullination, 2-hydroxyisobutyrylation, methylation, O-GlcNAcylation, propionylation, and succinylation in AUY922- and ganetespib-treated 5637 cells.
28298630	0	76	theme	cancer	129:134	arg1	therapeutics					136:147	bladder cancer therapeutics	121:147	bladder cancer therapeutics	121:147	Proteomic analysis of proteome and histone post-translational modifications in heat shock protein 90 inhibition-mediated bladder cancer therapeutics.
28298630	3	77	theme	inhibition-mediated	359:377	arg1	therapy					394:400	HSP90 inhibition-mediated bladder cancer therapy	353:400	HSP90 inhibition-mediated bladder cancer therapy	353:400	However, little is known about HSP90 inhibition-mediated bladder cancer therapy.
28298630	8	78	theme	ganetespib-treated	1448:1465	arg1	cells					1472:1476	ganetespib-treated 5637 cells	1448:1476	ganetespib-treated 5637 cells	1448:1476	Furthermore, quantitative proteome studies identified 14 types of PTMs with 93 marks on the core histones, including 34 novel histone marks of butyrylation, citrullination, 2-hydroxyisobutyrylation, methylation, O-GlcNAcylation, propionylation, and succinylation in AUY922- and ganetespib-treated 5637 cells.
28298630	5	79	theme	cells	749:753	arg1	proliferation					712:724	the proliferation	708:724	the proliferation of bladder cancer 5637 cells	708:753	We show that 5 HSP90 inhibitors (AUY922, ganetespib, SNX2112, AT13387, and CUDC305) potently inhibited the proliferation of bladder cancer 5637 cells in a dose- and time-dependent manner.
28298630	8	80	from	succinylation	1419:1431	arg1	AUY922-					1436:1442	AUY922-	1436:1442	AUY922-	1436:1442	Furthermore, quantitative proteome studies identified 14 types of PTMs with 93 marks on the core histones, including 34 novel histone marks of butyrylation, citrullination, 2-hydroxyisobutyrylation, methylation, O-GlcNAcylation, propionylation, and succinylation in AUY922- and ganetespib-treated 5637 cells.
28298630	8	80	from	succinylation	1419:1431	arg1	cells					1472:1476	ganetespib-treated 5637 cells	1448:1476	ganetespib-treated 5637 cells	1448:1476	Furthermore, quantitative proteome studies identified 14 types of PTMs with 93 marks on the core histones, including 34 novel histone marks of butyrylation, citrullination, 2-hydroxyisobutyrylation, methylation, O-GlcNAcylation, propionylation, and succinylation in AUY922- and ganetespib-treated 5637 cells.
28298630	9	81	theme	HSP90	1679:1683	arg1	therapeutics					1720:1731	HSP90 inhibition-mediated bladder cancer therapeutics	1679:1731	HSP90 inhibition-mediated bladder cancer therapeutics	1679:1731	Together, this study outlines the association between proteomic changes and histone PTMs in response to HSP90 inhibitor treatment in bladder carcinoma cells, and thus intensifies the understanding of HSP90 inhibition-mediated bladder cancer therapeutics.
28298630	4	82	theme	HSP90	587:591	arg1	inhibition					593:602	HSP90 inhibition	587:602	HSP90 inhibition	587:602	Here, we report a quantitative proteomic study that evaluates alterations in protein expression and histone post-translational modifications (PTMs) in bladder carcinoma in response to HSP90 inhibition.
28298630	0	83	theme	proteome	22:29	arg1	analysis					10:17	Proteomic analysis	0:17	Proteomic analysis of proteome and histone post-translational modifications in heat shock protein 90	0:99	Proteomic analysis of proteome and histone post-translational modifications in heat shock protein 90 inhibition-mediated bladder cancer therapeutics.
28298630	9	84	theme	bladder	1705:1711	arg1	therapeutics					1720:1731	HSP90 inhibition-mediated bladder cancer therapeutics	1679:1731	HSP90 inhibition-mediated bladder cancer therapeutics	1679:1731	Together, this study outlines the association between proteomic changes and histone PTMs in response to HSP90 inhibitor treatment in bladder carcinoma cells, and thus intensifies the understanding of HSP90 inhibition-mediated bladder cancer therapeutics.
28298630	8	85	dep	histone	1296:1302	arg1	marks					1304:1308	marks	1304:1308	marks	1304:1308	Furthermore, quantitative proteome studies identified 14 types of PTMs with 93 marks on the core histones, including 34 novel histone marks of butyrylation, citrullination, 2-hydroxyisobutyrylation, methylation, O-GlcNAcylation, propionylation, and succinylation in AUY922- and ganetespib-treated 5637 cells.
28298630	0	86	theme	histone	35:41	arg1	modifications					62:74	histone post-translational modifications	35:74	histone post-translational modifications in heat shock protein 90	35:99	Proteomic analysis of proteome and histone post-translational modifications in heat shock protein 90 inhibition-mediated bladder cancer therapeutics.
28298630	8	87	theme	quantitative	1183:1194	arg1	studies					1205:1211	quantitative proteome studies	1183:1211	quantitative proteome studies	1183:1211	Furthermore, quantitative proteome studies identified 14 types of PTMs with 93 marks on the core histones, including 34 novel histone marks of butyrylation, citrullination, 2-hydroxyisobutyrylation, methylation, O-GlcNAcylation, propionylation, and succinylation in AUY922- and ganetespib-treated 5637 cells.
28298630	6	88	theme	common	889:894	arg1	proteins					880:887	518 twofold up-regulated and 811 twofold down-regulated proteins	824:887	518 twofold up-regulated and 811 twofold down-regulated proteins common to both AUY922 and ganetespib treatment	824:934	Our proteomic study quantified 518 twofold up-regulated and 811 twofold down-regulated proteins common to both AUY922 and ganetespib treatment.
28298630	9	89	theme	therapeutics	1720:1731	arg1	understanding					1662:1674	the understanding	1658:1674	the understanding of HSP90 inhibition-mediated bladder cancer therapeutics	1658:1731	Together, this study outlines the association between proteomic changes and histone PTMs in response to HSP90 inhibitor treatment in bladder carcinoma cells, and thus intensifies the understanding of HSP90 inhibition-mediated bladder cancer therapeutics.
28298630	0	90	theme	modifications	62:74	arg1	analysis					10:17	Proteomic analysis	0:17	Proteomic analysis of proteome and histone post-translational modifications in heat shock protein 90	0:99	Proteomic analysis of proteome and histone post-translational modifications in heat shock protein 90 inhibition-mediated bladder cancer therapeutics.
28298630	6	91	theme	down-regulated	865:878	arg1	proteins					880:887	518 twofold up-regulated and 811 twofold down-regulated proteins	824:887	518 twofold up-regulated and 811 twofold down-regulated proteins common to both AUY922 and ganetespib treatment	824:934	Our proteomic study quantified 518 twofold up-regulated and 811 twofold down-regulated proteins common to both AUY922 and ganetespib treatment.
28298630	4	92	from	alterations	465:475	arg1	PTMs					545:548	PTMs	545:548	PTMs	545:548	Here, we report a quantitative proteomic study that evaluates alterations in protein expression and histone post-translational modifications (PTMs) in bladder carcinoma in response to HSP90 inhibition.
28298630	4	92	from	alterations	465:475	arg1	modifications					530:542	histone post-translational modifications	503:542	histone post-translational modifications (PTMs) in bladder carcinoma in response to HSP90 inhibition	503:602	Here, we report a quantitative proteomic study that evaluates alterations in protein expression and histone post-translational modifications (PTMs) in bladder carcinoma in response to HSP90 inhibition.
28298630	4	92	from	alterations	465:475	arg1	expression					488:497	protein expression	480:497	protein expression	480:497	Here, we report a quantitative proteomic study that evaluates alterations in protein expression and histone post-translational modifications (PTMs) in bladder carcinoma in response to HSP90 inhibition.
28298630	7	93	theme	Bioinformatic	937:949	arg1	analyses					951:958	Bioinformatic analyses	937:958	Bioinformatic analyses	937:958	Bioinformatic analyses revealed that those differentially expressed proteins were involved in multiple cellular processes and enzyme-regulated signaling pathways, including chromatin modifications and cell death-associated pathways.
28298630	8	94	from	citrullination	1327:1340	arg1	AUY922-					1436:1442	AUY922-	1436:1442	AUY922-	1436:1442	Furthermore, quantitative proteome studies identified 14 types of PTMs with 93 marks on the core histones, including 34 novel histone marks of butyrylation, citrullination, 2-hydroxyisobutyrylation, methylation, O-GlcNAcylation, propionylation, and succinylation in AUY922- and ganetespib-treated 5637 cells.
28298630	8	94	from	citrullination	1327:1340	arg1	cells					1472:1476	ganetespib-treated 5637 cells	1448:1476	ganetespib-treated 5637 cells	1448:1476	Furthermore, quantitative proteome studies identified 14 types of PTMs with 93 marks on the core histones, including 34 novel histone marks of butyrylation, citrullination, 2-hydroxyisobutyrylation, methylation, O-GlcNAcylation, propionylation, and succinylation in AUY922- and ganetespib-treated 5637 cells.
28298630	6	95	theme	up-regulated	836:847	arg1	proteins					880:887	518 twofold up-regulated and 811 twofold down-regulated proteins	824:887	518 twofold up-regulated and 811 twofold down-regulated proteins common to both AUY922 and ganetespib treatment	824:934	Our proteomic study quantified 518 twofold up-regulated and 811 twofold down-regulated proteins common to both AUY922 and ganetespib treatment.
28298630	5	96	dep	inhibitors	626:635	arg1	AT13387					667:673	AT13387	667:673	AT13387	667:673	We show that 5 HSP90 inhibitors (AUY922, ganetespib, SNX2112, AT13387, and CUDC305) potently inhibited the proliferation of bladder cancer 5637 cells in a dose- and time-dependent manner.
28298630	5	96	dep	inhibitors	626:635	arg1	CUDC305					680:686	CUDC305	680:686	CUDC305	680:686	We show that 5 HSP90 inhibitors (AUY922, ganetespib, SNX2112, AT13387, and CUDC305) potently inhibited the proliferation of bladder cancer 5637 cells in a dose- and time-dependent manner.
28298630	5	96	dep	inhibitors	626:635	arg1	inhibitors					626:635	5 HSP90 inhibitors	618:635	5 HSP90 inhibitors (AUY922, ganetespib, SNX2112, AT13387, and CUDC305)	618:687	We show that 5 HSP90 inhibitors (AUY922, ganetespib, SNX2112, AT13387, and CUDC305) potently inhibited the proliferation of bladder cancer 5637 cells in a dose- and time-dependent manner.
36357422	2	0	from	tail	413:416	arg1	introduction					341:352	the introduction	337:352	the introduction of the ß-N-acetylglucosamine (GlcNAc) moiety on histone H3 tail at position Ser10 and Thr32	337:444	One such PTM has been identified as serine and threonine glycosylation, the introduction of the ß-N-acetylglucosamine (GlcNAc) moiety on histone H3 tail at position Ser10 and Thr32.
36357422	6	1	theme	full	1023:1026	arg1	substrate					1056:1064	a substrate	1054:1064	a substrate for OGT	1054:1072	In addition, full length histone H3 was not a substrate for OGT.
36357422	6	1	theme	full	1023:1026	arg1	H3					1043:1044	full length histone H3	1023:1044	full length histone H3	1023:1044	In addition, full length histone H3 was not a substrate for OGT.
36357422	9	2	theme	H3	1623:1624	arg1	peptide					1631:1637	histone H3 tail peptide	1615:1637	histone H3 tail peptide	1615:1637	Overall, this work indicates that GlcNAcylation of histone H3 tail peptide in the presence of OGT does not occur in vitro.
36357422	5	3	dep	sites	986:990	arg1	Ser10					993:997	Ser10	993:997	Ser10	993:997	Our enzymatic assays with recombinantly expressed human OGT revealed that the unmodified and PTM-modified histone H3 tails are not substrates for OGT at both sites, Ser10 and Thr32.
36357422	5	3	dep	sites	986:990	arg1	sites					986:990	both sites	981:990	both sites	981:990	Our enzymatic assays with recombinantly expressed human OGT revealed that the unmodified and PTM-modified histone H3 tails are not substrates for OGT at both sites, Ser10 and Thr32.
36357422	5	3	dep	sites	986:990	arg1	Thr32					1003:1007	Thr32	1003:1007	Thr32	1003:1007	Our enzymatic assays with recombinantly expressed human OGT revealed that the unmodified and PTM-modified histone H3 tails are not substrates for OGT at both sites, Ser10 and Thr32.
36357422	1	4	theme	Posttranslational	75:91	arg1	modifications					93:105	Posttranslational modifications	75:105	Posttranslational modifications (PTMs) on histone tails	75:129	Posttranslational modifications (PTMs) on histone tails regulate eukaryotic gene expression by impacting the chromatin structure and by modulating interactions with other cellular proteins.
36357422	1	4	theme	Posttranslational	75:91	arg1	PTMs					108:111	PTMs	108:111	PTMs	108:111	Posttranslational modifications (PTMs) on histone tails regulate eukaryotic gene expression by impacting the chromatin structure and by modulating interactions with other cellular proteins.
36357422	9	5	theme	peptide	1631:1637	arg1	GlcNAcylation					1598:1610	GlcNAcylation	1598:1610	GlcNAcylation of histone H3 tail peptide in the presence of OGT	1598:1660	Overall, this work indicates that GlcNAcylation of histone H3 tail peptide in the presence of OGT does not occur in vitro.
36357422	4	6	theme	Conflicting	622:632	arg1	reports					634:640	Conflicting reports	622:640	Conflicting reports on histone tail GlcNAc modification in vivo	622:684	Conflicting reports on histone tail GlcNAc modification in vivo prompted us to investigate whether synthetic histone H3 tail peptides in conjunction with other PTMs are substrates for OGT and OGA in vitro.
36357422	1	7	theme	chromatin	184:192	arg1	structure					194:202	the chromatin structure	180:202	the chromatin structure	180:202	Posttranslational modifications (PTMs) on histone tails regulate eukaryotic gene expression by impacting the chromatin structure and by modulating interactions with other cellular proteins.
36357422	8	8	theme	histone	1383:1389	arg1	PCAF					1417:1420	PCAF	1417:1420	PCAF	1417:1420	We also show that the catalytic domains of human histone lysine methyltransferases G9a, GLP and SETD7 and histone lysine acetyltransferases PCAF and GCN5 do somewhat tolerate glycosylated H3Ser10 close to lysine residues that undergo methylation and acetylation reactions, respectively.
36357422	8	8	theme	histone	1383:1389	arg1	acetyltransferases					1398:1415	histone lysine acetyltransferases PCAF and GCN5	1383:1429	histone lysine acetyltransferases PCAF and GCN5	1383:1429	We also show that the catalytic domains of human histone lysine methyltransferases G9a, GLP and SETD7 and histone lysine acetyltransferases PCAF and GCN5 do somewhat tolerate glycosylated H3Ser10 close to lysine residues that undergo methylation and acetylation reactions, respectively.
36357422	8	8	theme	histone	1383:1389	arg1	GCN5					1426:1429	GCN5	1426:1429	GCN5	1426:1429	We also show that the catalytic domains of human histone lysine methyltransferases G9a, GLP and SETD7 and histone lysine acetyltransferases PCAF and GCN5 do somewhat tolerate glycosylated H3Ser10 close to lysine residues that undergo methylation and acetylation reactions, respectively.
36357422	2	9	dep	serine	301:306	arg1	glycosylation					322:334	glycosylation	322:334	glycosylation	322:334	One such PTM has been identified as serine and threonine glycosylation, the introduction of the ß-N-acetylglucosamine (GlcNAc) moiety on histone H3 tail at position Ser10 and Thr32.
36357422	5	10	theme	expressed	868:876	arg1	OGT					884:886	recombinantly expressed human OGT	854:886	recombinantly expressed human OGT	854:886	Our enzymatic assays with recombinantly expressed human OGT revealed that the unmodified and PTM-modified histone H3 tails are not substrates for OGT at both sites, Ser10 and Thr32.
36357422	8	11	theme	acetyltransferases	1398:1415	arg1	methyltransferases					1341:1358	human histone lysine methyltransferases G9a, GLP and SETD7	1320:1377	human histone lysine methyltransferases G9a, GLP and SETD7	1320:1377	We also show that the catalytic domains of human histone lysine methyltransferases G9a, GLP and SETD7 and histone lysine acetyltransferases PCAF and GCN5 do somewhat tolerate glycosylated H3Ser10 close to lysine residues that undergo methylation and acetylation reactions, respectively.
36357422	8	11	theme	acetyltransferases	1398:1415	arg1	domains					1309:1315	the catalytic domains	1295:1315	the catalytic domains of human histone lysine methyltransferases G9a, GLP and SETD7 and histone lysine acetyltransferases PCAF and GCN5	1295:1429	We also show that the catalytic domains of human histone lysine methyltransferases G9a, GLP and SETD7 and histone lysine acetyltransferases PCAF and GCN5 do somewhat tolerate glycosylated H3Ser10 close to lysine residues that undergo methylation and acetylation reactions, respectively.
36357422	8	11	theme	acetyltransferases	1398:1415	arg1	acetyltransferases					1398:1415	histone lysine acetyltransferases PCAF and GCN5	1383:1429	histone lysine acetyltransferases PCAF and GCN5	1383:1429	We also show that the catalytic domains of human histone lysine methyltransferases G9a, GLP and SETD7 and histone lysine acetyltransferases PCAF and GCN5 do somewhat tolerate glycosylated H3Ser10 close to lysine residues that undergo methylation and acetylation reactions, respectively.
36357422	1	12	theme	histone	117:123	arg1	tails					125:129	histone tails	117:129	histone tails	117:129	Posttranslational modifications (PTMs) on histone tails regulate eukaryotic gene expression by impacting the chromatin structure and by modulating interactions with other cellular proteins.
36357422	0	13	theme	H3	57:58	arg1	peptides					65:72	H3 tail peptides	57:72	H3 tail peptides	57:72	Investigation of in vitro histone H3 glycosylation using H3 tail peptides.
36357422	4	14	from	peptides	747:754	arg1	conjunction					759:769	conjunction	759:769	conjunction with other PTMs	759:785	Conflicting reports on histone tail GlcNAc modification in vivo prompted us to investigate whether synthetic histone H3 tail peptides in conjunction with other PTMs are substrates for OGT and OGA in vitro.
36357422	1	15	theme	eukaryotic	140:149	arg1	expression					156:165	eukaryotic gene expression	140:165	eukaryotic gene expression	140:165	Posttranslational modifications (PTMs) on histone tails regulate eukaryotic gene expression by impacting the chromatin structure and by modulating interactions with other cellular proteins.
36357422	2	16	from	position	421:428	arg1	introduction					341:352	the introduction	337:352	the introduction of the ß-N-acetylglucosamine (GlcNAc) moiety on histone H3 tail at position Ser10 and Thr32	337:444	One such PTM has been identified as serine and threonine glycosylation, the introduction of the ß-N-acetylglucosamine (GlcNAc) moiety on histone H3 tail at position Ser10 and Thr32.
36357422	5	17	with	assays	842:847	arg1	OGT					884:886	recombinantly expressed human OGT	854:886	recombinantly expressed human OGT	854:886	Our enzymatic assays with recombinantly expressed human OGT revealed that the unmodified and PTM-modified histone H3 tails are not substrates for OGT at both sites, Ser10 and Thr32.
36357422	4	18	theme	tail	653:656	arg1	modification					665:676	histone tail GlcNAc modification	645:676	histone tail GlcNAc modification	645:676	Conflicting reports on histone tail GlcNAc modification in vivo prompted us to investigate whether synthetic histone H3 tail peptides in conjunction with other PTMs are substrates for OGT and OGA in vitro.
36357422	4	19	with	conjunction	759:769	arg1	PTMs					782:785	other PTMs	776:785	other PTMs	776:785	Conflicting reports on histone tail GlcNAc modification in vivo prompted us to investigate whether synthetic histone H3 tail peptides in conjunction with other PTMs are substrates for OGT and OGA in vitro.
36357422	8	20	theme	glycosylated	1452:1463	arg1	H3Ser10					1465:1471	glycosylated H3Ser10	1452:1471	glycosylated H3Ser10 close to lysine residues that undergo methylation and acetylation reactions, respectively	1452:1561	We also show that the catalytic domains of human histone lysine methyltransferases G9a, GLP and SETD7 and histone lysine acetyltransferases PCAF and GCN5 do somewhat tolerate glycosylated H3Ser10 close to lysine residues that undergo methylation and acetylation reactions, respectively.
36357422	4	21	theme	synthetic	721:729	arg1	substrates					791:800	substrates	791:800	substrates for OGT and OGA in vitro	791:825	Conflicting reports on histone tail GlcNAc modification in vivo prompted us to investigate whether synthetic histone H3 tail peptides in conjunction with other PTMs are substrates for OGT and OGA in vitro.
36357422	4	21	theme	synthetic	721:729	arg1	peptides					747:754	synthetic histone H3 tail peptides	721:754	synthetic histone H3 tail peptides in conjunction with other PTMs	721:785	Conflicting reports on histone tail GlcNAc modification in vivo prompted us to investigate whether synthetic histone H3 tail peptides in conjunction with other PTMs are substrates for OGT and OGA in vitro.
36357422	5	22	theme	PTM-modified	921:932	arg1	tails					945:949	the unmodified and PTM-modified histone H3 tails	902:949	the unmodified and PTM-modified histone H3 tails	902:949	Our enzymatic assays with recombinantly expressed human OGT revealed that the unmodified and PTM-modified histone H3 tails are not substrates for OGT at both sites, Ser10 and Thr32.
36357422	5	22	theme	PTM-modified	921:932	arg1	substrates					959:968	substrates	959:968	substrates for OGT	959:976	Our enzymatic assays with recombinantly expressed human OGT revealed that the unmodified and PTM-modified histone H3 tails are not substrates for OGT at both sites, Ser10 and Thr32.
36357422	4	23	theme	H3	739:740	arg1	substrates					791:800	substrates	791:800	substrates for OGT and OGA in vitro	791:825	Conflicting reports on histone tail GlcNAc modification in vivo prompted us to investigate whether synthetic histone H3 tail peptides in conjunction with other PTMs are substrates for OGT and OGA in vitro.
36357422	4	23	theme	H3	739:740	arg1	peptides					747:754	synthetic histone H3 tail peptides	721:754	synthetic histone H3 tail peptides in conjunction with other PTMs	721:785	Conflicting reports on histone tail GlcNAc modification in vivo prompted us to investigate whether synthetic histone H3 tail peptides in conjunction with other PTMs are substrates for OGT and OGA in vitro.
36357422	2	24	dep	position	421:428	arg1	Ser10					430:434	Ser10	430:434	Ser10	430:434	One such PTM has been identified as serine and threonine glycosylation, the introduction of the ß-N-acetylglucosamine (GlcNAc) moiety on histone H3 tail at position Ser10 and Thr32.
36357422	5	25	theme	H3	942:943	arg1	tails					945:949	the unmodified and PTM-modified histone H3 tails	902:949	the unmodified and PTM-modified histone H3 tails	902:949	Our enzymatic assays with recombinantly expressed human OGT revealed that the unmodified and PTM-modified histone H3 tails are not substrates for OGT at both sites, Ser10 and Thr32.
36357422	5	25	theme	H3	942:943	arg1	substrates					959:968	substrates	959:968	substrates for OGT	959:976	Our enzymatic assays with recombinantly expressed human OGT revealed that the unmodified and PTM-modified histone H3 tails are not substrates for OGT at both sites, Ser10 and Thr32.
36357422	8	26	theme	lysine	1482:1487	arg1	residues					1489:1496	lysine residues	1482:1496	lysine residues that undergo methylation and acetylation reactions, respectively	1482:1561	We also show that the catalytic domains of human histone lysine methyltransferases G9a, GLP and SETD7 and histone lysine acetyltransferases PCAF and GCN5 do somewhat tolerate glycosylated H3Ser10 close to lysine residues that undergo methylation and acetylation reactions, respectively.
36357422	0	27	theme	tail	60:63	arg1	peptides					65:72	H3 tail peptides	57:72	H3 tail peptides	57:72	Investigation of in vitro histone H3 glycosylation using H3 tail peptides.
36357422	8	28	theme	catalytic	1299:1307	arg1	methyltransferases					1341:1358	human histone lysine methyltransferases G9a, GLP and SETD7	1320:1377	human histone lysine methyltransferases G9a, GLP and SETD7	1320:1377	We also show that the catalytic domains of human histone lysine methyltransferases G9a, GLP and SETD7 and histone lysine acetyltransferases PCAF and GCN5 do somewhat tolerate glycosylated H3Ser10 close to lysine residues that undergo methylation and acetylation reactions, respectively.
36357422	8	28	theme	catalytic	1299:1307	arg1	domains					1309:1315	the catalytic domains	1295:1315	the catalytic domains of human histone lysine methyltransferases G9a, GLP and SETD7 and histone lysine acetyltransferases PCAF and GCN5	1295:1429	We also show that the catalytic domains of human histone lysine methyltransferases G9a, GLP and SETD7 and histone lysine acetyltransferases PCAF and GCN5 do somewhat tolerate glycosylated H3Ser10 close to lysine residues that undergo methylation and acetylation reactions, respectively.
36357422	8	28	theme	catalytic	1299:1307	arg1	acetyltransferases					1398:1415	histone lysine acetyltransferases PCAF and GCN5	1383:1429	histone lysine acetyltransferases PCAF and GCN5	1383:1429	We also show that the catalytic domains of human histone lysine methyltransferases G9a, GLP and SETD7 and histone lysine acetyltransferases PCAF and GCN5 do somewhat tolerate glycosylated H3Ser10 close to lysine residues that undergo methylation and acetylation reactions, respectively.
36357422	7	29	theme	H3	1264:1265	arg1	peptides					1267:1274	deglycosylated histone H3 peptides	1241:1274	deglycosylated histone H3 peptides	1241:1274	Conversely, our work demonstrates that synthetic peptides containing the GlcNAc functionality at Ser10 are substrates for recombinantly expressed human OGA, yielding deglycosylated histone H3 peptides.
36357422	1	30	dep	regulate	131:138	arg1	impacting					170:178	impacting	170:178	impacting the chromatin structure	170:202	Posttranslational modifications (PTMs) on histone tails regulate eukaryotic gene expression by impacting the chromatin structure and by modulating interactions with other cellular proteins.
36357422	1	30	dep	regulate	131:138	arg1	modulating					211:220	modulating	211:220	modulating interactions with other cellular proteins	211:262	Posttranslational modifications (PTMs) on histone tails regulate eukaryotic gene expression by impacting the chromatin structure and by modulating interactions with other cellular proteins.
36357422	6	31	from	substrate	1056:1064	arg1	addition					1013:1020	addition	1013:1020	addition	1013:1020	In addition, full length histone H3 was not a substrate for OGT.
36357422	0	32	theme	in	17:18	arg1	glycosylation					37:49	in vitro histone H3 glycosylation	17:49	in vitro histone H3 glycosylation	17:49	Investigation of in vitro histone H3 glycosylation using H3 tail peptides.
36357422	5	33	theme	unmodified	906:915	arg1	tails					945:949	the unmodified and PTM-modified histone H3 tails	902:949	the unmodified and PTM-modified histone H3 tails	902:949	Our enzymatic assays with recombinantly expressed human OGT revealed that the unmodified and PTM-modified histone H3 tails are not substrates for OGT at both sites, Ser10 and Thr32.
36357422	5	33	theme	unmodified	906:915	arg1	substrates					959:968	substrates	959:968	substrates for OGT	959:976	Our enzymatic assays with recombinantly expressed human OGT revealed that the unmodified and PTM-modified histone H3 tails are not substrates for OGT at both sites, Ser10 and Thr32.
36357422	7	34	theme	deglycosylated	1241:1254	arg1	peptides					1267:1274	deglycosylated histone H3 peptides	1241:1274	deglycosylated histone H3 peptides	1241:1274	Conversely, our work demonstrates that synthetic peptides containing the GlcNAc functionality at Ser10 are substrates for recombinantly expressed human OGA, yielding deglycosylated histone H3 peptides.
36357422	8	35	theme	methylation	1511:1521	arg1	reactions					1539:1547	methylation and acetylation reactions	1511:1547	methylation and acetylation reactions	1511:1547	We also show that the catalytic domains of human histone lysine methyltransferases G9a, GLP and SETD7 and histone lysine acetyltransferases PCAF and GCN5 do somewhat tolerate glycosylated H3Ser10 close to lysine residues that undergo methylation and acetylation reactions, respectively.
36357422	8	36	theme	histone	1326:1332	arg1	SETD7					1373:1377	SETD7	1373:1377	SETD7	1373:1377	We also show that the catalytic domains of human histone lysine methyltransferases G9a, GLP and SETD7 and histone lysine acetyltransferases PCAF and GCN5 do somewhat tolerate glycosylated H3Ser10 close to lysine residues that undergo methylation and acetylation reactions, respectively.
36357422	8	36	theme	histone	1326:1332	arg1	methyltransferases					1341:1358	human histone lysine methyltransferases G9a, GLP and SETD7	1320:1377	human histone lysine methyltransferases G9a, GLP and SETD7	1320:1377	We also show that the catalytic domains of human histone lysine methyltransferases G9a, GLP and SETD7 and histone lysine acetyltransferases PCAF and GCN5 do somewhat tolerate glycosylated H3Ser10 close to lysine residues that undergo methylation and acetylation reactions, respectively.
36357422	8	36	theme	histone	1326:1332	arg1	GLP					1365:1367	GLP	1365:1367	GLP	1365:1367	We also show that the catalytic domains of human histone lysine methyltransferases G9a, GLP and SETD7 and histone lysine acetyltransferases PCAF and GCN5 do somewhat tolerate glycosylated H3Ser10 close to lysine residues that undergo methylation and acetylation reactions, respectively.
36357422	8	36	theme	histone	1326:1332	arg1	G9a					1360:1362	G9a	1360:1362	G9a	1360:1362	We also show that the catalytic domains of human histone lysine methyltransferases G9a, GLP and SETD7 and histone lysine acetyltransferases PCAF and GCN5 do somewhat tolerate glycosylated H3Ser10 close to lysine residues that undergo methylation and acetylation reactions, respectively.
36357422	2	37	theme	H3	410:411	arg1	tail					413:416	histone H3 tail	402:416	histone H3 tail	402:416	One such PTM has been identified as serine and threonine glycosylation, the introduction of the ß-N-acetylglucosamine (GlcNAc) moiety on histone H3 tail at position Ser10 and Thr32.
36357422	0	38	theme	histone	26:32	arg1	glycosylation					37:49	in vitro histone H3 glycosylation	17:49	in vitro histone H3 glycosylation	17:49	Investigation of in vitro histone H3 glycosylation using H3 tail peptides.
36357422	8	39	theme	acetylation	1527:1537	arg1	reactions					1539:1547	methylation and acetylation reactions	1511:1547	methylation and acetylation reactions	1511:1547	We also show that the catalytic domains of human histone lysine methyltransferases G9a, GLP and SETD7 and histone lysine acetyltransferases PCAF and GCN5 do somewhat tolerate glycosylated H3Ser10 close to lysine residues that undergo methylation and acetylation reactions, respectively.
36357422	8	40	theme	methyltransferases	1341:1358	arg1	methyltransferases					1341:1358	human histone lysine methyltransferases G9a, GLP and SETD7	1320:1377	human histone lysine methyltransferases G9a, GLP and SETD7	1320:1377	We also show that the catalytic domains of human histone lysine methyltransferases G9a, GLP and SETD7 and histone lysine acetyltransferases PCAF and GCN5 do somewhat tolerate glycosylated H3Ser10 close to lysine residues that undergo methylation and acetylation reactions, respectively.
36357422	8	40	theme	methyltransferases	1341:1358	arg1	domains					1309:1315	the catalytic domains	1295:1315	the catalytic domains of human histone lysine methyltransferases G9a, GLP and SETD7 and histone lysine acetyltransferases PCAF and GCN5	1295:1429	We also show that the catalytic domains of human histone lysine methyltransferases G9a, GLP and SETD7 and histone lysine acetyltransferases PCAF and GCN5 do somewhat tolerate glycosylated H3Ser10 close to lysine residues that undergo methylation and acetylation reactions, respectively.
36357422	8	40	theme	methyltransferases	1341:1358	arg1	acetyltransferases					1398:1415	histone lysine acetyltransferases PCAF and GCN5	1383:1429	histone lysine acetyltransferases PCAF and GCN5	1383:1429	We also show that the catalytic domains of human histone lysine methyltransferases G9a, GLP and SETD7 and histone lysine acetyltransferases PCAF and GCN5 do somewhat tolerate glycosylated H3Ser10 close to lysine residues that undergo methylation and acetylation reactions, respectively.
36357422	3	41	theme	moiety	478:483	arg1	addition					451:458	The addition	447:458	The addition of the ß-O-GlcNAc moiety on serine or threonine residues	447:515	The addition of the ß-O-GlcNAc moiety on serine or threonine residues is facilitated by the O-GlcNAc transferase (OGT), and can be removed by the action of O-GlcNAcase (OGA).
36357422	0	42	theme	glycosylation	37:49	arg1	Investigation					0:12	Investigation	0:12	Investigation of in vitro histone H3 glycosylation	0:49	Investigation of in vitro histone H3 glycosylation using H3 tail peptides.
36357422	7	43	theme	human	1221:1225	arg1	OGA					1227:1229	recombinantly expressed human OGA	1197:1229	recombinantly expressed human OGA	1197:1229	Conversely, our work demonstrates that synthetic peptides containing the GlcNAc functionality at Ser10 are substrates for recombinantly expressed human OGA, yielding deglycosylated histone H3 peptides.
36357422	0	44	dep	in	17:18	arg1	vitro					20:24	vitro	20:24	vitro	20:24	Investigation of in vitro histone H3 glycosylation using H3 tail peptides.
36357422	5	45	theme	enzymatic	832:840	arg1	assays					842:847	Our enzymatic assays	828:847	Our enzymatic assays with recombinantly expressed human OGT	828:886	Our enzymatic assays with recombinantly expressed human OGT revealed that the unmodified and PTM-modified histone H3 tails are not substrates for OGT at both sites, Ser10 and Thr32.
36357422	9	46	from	GlcNAcylation	1598:1610	arg1	presence					1646:1653	the presence	1642:1653	the presence of OGT	1642:1660	Overall, this work indicates that GlcNAcylation of histone H3 tail peptide in the presence of OGT does not occur in vitro.
36357422	7	47	contain	containing	1133:1142	arg2	functionality					1155:1167	the GlcNAc functionality	1144:1167	the GlcNAc functionality	1144:1167	Conversely, our work demonstrates that synthetic peptides containing the GlcNAc functionality at Ser10 are substrates for recombinantly expressed human OGA, yielding deglycosylated histone H3 peptides.
36357422	7	47	contain	containing	1133:1142	arg1	peptides					1124:1131	synthetic peptides	1114:1131	synthetic peptides containing the GlcNAc functionality at Ser10	1114:1176	Conversely, our work demonstrates that synthetic peptides containing the GlcNAc functionality at Ser10 are substrates for recombinantly expressed human OGA, yielding deglycosylated histone H3 peptides.
36357422	7	47	contain	containing	1133:1142	arg1	substrates					1182:1191	substrates	1182:1191	substrates for recombinantly expressed human OGA	1182:1229	Conversely, our work demonstrates that synthetic peptides containing the GlcNAc functionality at Ser10 are substrates for recombinantly expressed human OGA, yielding deglycosylated histone H3 peptides.
36357422	1	48	from	modifications	93:105	arg1	tails					125:129	histone tails	117:129	histone tails	117:129	Posttranslational modifications (PTMs) on histone tails regulate eukaryotic gene expression by impacting the chromatin structure and by modulating interactions with other cellular proteins.
36357422	1	49	theme	other	240:244	arg1	proteins					255:262	other cellular proteins	240:262	other cellular proteins	240:262	Posttranslational modifications (PTMs) on histone tails regulate eukaryotic gene expression by impacting the chromatin structure and by modulating interactions with other cellular proteins.
36357422	1	50	with	interactions	222:233	arg1	proteins					255:262	other cellular proteins	240:262	other cellular proteins	240:262	Posttranslational modifications (PTMs) on histone tails regulate eukaryotic gene expression by impacting the chromatin structure and by modulating interactions with other cellular proteins.
36357422	6	51	theme	length	1028:1033	arg1	substrate					1056:1064	a substrate	1054:1064	a substrate for OGT	1054:1072	In addition, full length histone H3 was not a substrate for OGT.
36357422	6	51	theme	length	1028:1033	arg1	H3					1043:1044	full length histone H3	1023:1044	full length histone H3	1023:1044	In addition, full length histone H3 was not a substrate for OGT.
36357422	4	52	theme	other	776:780	arg1	PTMs					782:785	other PTMs	776:785	other PTMs	776:785	Conflicting reports on histone tail GlcNAc modification in vivo prompted us to investigate whether synthetic histone H3 tail peptides in conjunction with other PTMs are substrates for OGT and OGA in vitro.
36357422	9	53	theme	histone	1615:1621	arg1	H3					1623:1624	histone H3	1615:1624	histone H3 tail peptide	1615:1637	Overall, this work indicates that GlcNAcylation of histone H3 tail peptide in the presence of OGT does not occur in vitro.
36357422	4	54	from	reports	634:640	arg1	modification					665:676	histone tail GlcNAc modification	645:676	histone tail GlcNAc modification	645:676	Conflicting reports on histone tail GlcNAc modification in vivo prompted us to investigate whether synthetic histone H3 tail peptides in conjunction with other PTMs are substrates for OGT and OGA in vitro.
36357422	9	55	theme	tail	1626:1629	arg1	peptide					1631:1637	histone H3 tail peptide	1615:1637	histone H3 tail peptide	1615:1637	Overall, this work indicates that GlcNAcylation of histone H3 tail peptide in the presence of OGT does not occur in vitro.
36357422	2	56	from	introduction	341:352	arg1	tail					413:416	histone H3 tail	402:416	histone H3 tail	402:416	One such PTM has been identified as serine and threonine glycosylation, the introduction of the ß-N-acetylglucosamine (GlcNAc) moiety on histone H3 tail at position Ser10 and Thr32.
36357422	2	57	dep	identified	287:296	arg1	introduction					341:352	the introduction	337:352	the introduction of the ß-N-acetylglucosamine (GlcNAc) moiety on histone H3 tail at position Ser10 and Thr32	337:444	One such PTM has been identified as serine and threonine glycosylation, the introduction of the ß-N-acetylglucosamine (GlcNAc) moiety on histone H3 tail at position Ser10 and Thr32.
36357422	3	58	theme	O-GlcNAc	539:546	arg1	transferase					548:558	O-GlcNAc transferase	539:558	the O-GlcNAc transferase (OGT)	535:564	The addition of the ß-O-GlcNAc moiety on serine or threonine residues is facilitated by the O-GlcNAc transferase (OGT), and can be removed by the action of O-GlcNAcase (OGA).
36357422	3	58	theme	O-GlcNAc	539:546	arg1	OGT					561:563	OGT	561:563	OGT	561:563	The addition of the ß-O-GlcNAc moiety on serine or threonine residues is facilitated by the O-GlcNAc transferase (OGT), and can be removed by the action of O-GlcNAcase (OGA).
36357422	9	59	theme	OGT	1658:1660	arg1	presence					1646:1653	the presence	1642:1653	the presence of OGT	1642:1660	Overall, this work indicates that GlcNAcylation of histone H3 tail peptide in the presence of OGT does not occur in vitro.
36357422	8	60	theme	lysine	1391:1396	arg1	PCAF					1417:1420	PCAF	1417:1420	PCAF	1417:1420	We also show that the catalytic domains of human histone lysine methyltransferases G9a, GLP and SETD7 and histone lysine acetyltransferases PCAF and GCN5 do somewhat tolerate glycosylated H3Ser10 close to lysine residues that undergo methylation and acetylation reactions, respectively.
36357422	8	60	theme	lysine	1391:1396	arg1	acetyltransferases					1398:1415	histone lysine acetyltransferases PCAF and GCN5	1383:1429	histone lysine acetyltransferases PCAF and GCN5	1383:1429	We also show that the catalytic domains of human histone lysine methyltransferases G9a, GLP and SETD7 and histone lysine acetyltransferases PCAF and GCN5 do somewhat tolerate glycosylated H3Ser10 close to lysine residues that undergo methylation and acetylation reactions, respectively.
36357422	8	60	theme	lysine	1391:1396	arg1	GCN5					1426:1429	GCN5	1426:1429	GCN5	1426:1429	We also show that the catalytic domains of human histone lysine methyltransferases G9a, GLP and SETD7 and histone lysine acetyltransferases PCAF and GCN5 do somewhat tolerate glycosylated H3Ser10 close to lysine residues that undergo methylation and acetylation reactions, respectively.
36357422	4	61	theme	GlcNAc	658:663	arg1	modification					665:676	histone tail GlcNAc modification	645:676	histone tail GlcNAc modification	645:676	Conflicting reports on histone tail GlcNAc modification in vivo prompted us to investigate whether synthetic histone H3 tail peptides in conjunction with other PTMs are substrates for OGT and OGA in vitro.
36357422	2	62	theme	such	269:272	arg1	serine					301:306	serine	301:306	serine	301:306	One such PTM has been identified as serine and threonine glycosylation, the introduction of the ß-N-acetylglucosamine (GlcNAc) moiety on histone H3 tail at position Ser10 and Thr32.
36357422	2	62	theme	such	269:272	arg1	PTM					274:276	One such PTM	265:276	One such PTM	265:276	One such PTM has been identified as serine and threonine glycosylation, the introduction of the ß-N-acetylglucosamine (GlcNAc) moiety on histone H3 tail at position Ser10 and Thr32.
36357422	2	62	theme	such	269:272	arg1	threonine					312:320	threonine	312:320	threonine	312:320	One such PTM has been identified as serine and threonine glycosylation, the introduction of the ß-N-acetylglucosamine (GlcNAc) moiety on histone H3 tail at position Ser10 and Thr32.
36357422	8	63	gly	glycosylated	1452:1463	arg1	H3Ser10					1465:1471	glycosylated H3Ser10	1452:1471	glycosylated H3Ser10 close to lysine residues that undergo methylation and acetylation reactions, respectively	1452:1561	We also show that the catalytic domains of human histone lysine methyltransferases G9a, GLP and SETD7 and histone lysine acetyltransferases PCAF and GCN5 do somewhat tolerate glycosylated H3Ser10 close to lysine residues that undergo methylation and acetylation reactions, respectively.
36357422	7	64	theme	GlcNAc	1148:1153	arg1	functionality					1155:1167	the GlcNAc functionality	1144:1167	the GlcNAc functionality	1144:1167	Conversely, our work demonstrates that synthetic peptides containing the GlcNAc functionality at Ser10 are substrates for recombinantly expressed human OGA, yielding deglycosylated histone H3 peptides.
36357422	8	65	dep	methyltransferases	1341:1358	arg1	SETD7					1373:1377	SETD7	1373:1377	SETD7	1373:1377	We also show that the catalytic domains of human histone lysine methyltransferases G9a, GLP and SETD7 and histone lysine acetyltransferases PCAF and GCN5 do somewhat tolerate glycosylated H3Ser10 close to lysine residues that undergo methylation and acetylation reactions, respectively.
36357422	8	65	dep	methyltransferases	1341:1358	arg1	methyltransferases					1341:1358	human histone lysine methyltransferases G9a, GLP and SETD7	1320:1377	human histone lysine methyltransferases G9a, GLP and SETD7	1320:1377	We also show that the catalytic domains of human histone lysine methyltransferases G9a, GLP and SETD7 and histone lysine acetyltransferases PCAF and GCN5 do somewhat tolerate glycosylated H3Ser10 close to lysine residues that undergo methylation and acetylation reactions, respectively.
36357422	8	65	dep	methyltransferases	1341:1358	arg1	GLP					1365:1367	GLP	1365:1367	GLP	1365:1367	We also show that the catalytic domains of human histone lysine methyltransferases G9a, GLP and SETD7 and histone lysine acetyltransferases PCAF and GCN5 do somewhat tolerate glycosylated H3Ser10 close to lysine residues that undergo methylation and acetylation reactions, respectively.
36357422	8	65	dep	methyltransferases	1341:1358	arg1	G9a					1360:1362	G9a	1360:1362	G9a	1360:1362	We also show that the catalytic domains of human histone lysine methyltransferases G9a, GLP and SETD7 and histone lysine acetyltransferases PCAF and GCN5 do somewhat tolerate glycosylated H3Ser10 close to lysine residues that undergo methylation and acetylation reactions, respectively.
36357422	5	66	from	sites	986:990	arg1	tails					945:949	the unmodified and PTM-modified histone H3 tails	902:949	the unmodified and PTM-modified histone H3 tails	902:949	Our enzymatic assays with recombinantly expressed human OGT revealed that the unmodified and PTM-modified histone H3 tails are not substrates for OGT at both sites, Ser10 and Thr32.
36357422	5	66	from	sites	986:990	arg1	substrates					959:968	substrates	959:968	substrates for OGT	959:976	Our enzymatic assays with recombinantly expressed human OGT revealed that the unmodified and PTM-modified histone H3 tails are not substrates for OGT at both sites, Ser10 and Thr32.
36357422	7	67	gly	deglycosylated	1241:1254	arg1	peptides					1267:1274	deglycosylated histone H3 peptides	1241:1274	deglycosylated histone H3 peptides	1241:1274	Conversely, our work demonstrates that synthetic peptides containing the GlcNAc functionality at Ser10 are substrates for recombinantly expressed human OGA, yielding deglycosylated histone H3 peptides.
36357422	1	68	theme	gene	151:154	arg1	expression					156:165	eukaryotic gene expression	140:165	eukaryotic gene expression	140:165	Posttranslational modifications (PTMs) on histone tails regulate eukaryotic gene expression by impacting the chromatin structure and by modulating interactions with other cellular proteins.
36357422	2	69	from	Thr32	440:444	arg1	introduction					341:352	the introduction	337:352	the introduction of the ß-N-acetylglucosamine (GlcNAc) moiety on histone H3 tail at position Ser10 and Thr32	337:444	One such PTM has been identified as serine and threonine glycosylation, the introduction of the ß-N-acetylglucosamine (GlcNAc) moiety on histone H3 tail at position Ser10 and Thr32.
36357422	4	70	theme	histone	645:651	arg1	modification					665:676	histone tail GlcNAc modification	645:676	histone tail GlcNAc modification	645:676	Conflicting reports on histone tail GlcNAc modification in vivo prompted us to investigate whether synthetic histone H3 tail peptides in conjunction with other PTMs are substrates for OGT and OGA in vitro.
36357422	7	71	theme	synthetic	1114:1122	arg1	peptides					1124:1131	synthetic peptides	1114:1131	synthetic peptides containing the GlcNAc functionality at Ser10	1114:1176	Conversely, our work demonstrates that synthetic peptides containing the GlcNAc functionality at Ser10 are substrates for recombinantly expressed human OGA, yielding deglycosylated histone H3 peptides.
36357422	7	71	theme	synthetic	1114:1122	arg1	substrates					1182:1191	substrates	1182:1191	substrates for recombinantly expressed human OGA	1182:1229	Conversely, our work demonstrates that synthetic peptides containing the GlcNAc functionality at Ser10 are substrates for recombinantly expressed human OGA, yielding deglycosylated histone H3 peptides.
36357422	5	72	theme	histone	934:940	arg1	H3					942:943	histone H3	934:943	the unmodified and PTM-modified histone H3 tails	902:949	Our enzymatic assays with recombinantly expressed human OGT revealed that the unmodified and PTM-modified histone H3 tails are not substrates for OGT at both sites, Ser10 and Thr32.
36357422	5	73	theme	human	878:882	arg1	OGT					884:886	recombinantly expressed human OGT	854:886	recombinantly expressed human OGT	854:886	Our enzymatic assays with recombinantly expressed human OGT revealed that the unmodified and PTM-modified histone H3 tails are not substrates for OGT at both sites, Ser10 and Thr32.
36357422	4	74	theme	histone	731:737	arg1	H3					739:740	histone H3	731:740	synthetic histone H3 tail peptides in conjunction with other PTMs	721:785	Conflicting reports on histone tail GlcNAc modification in vivo prompted us to investigate whether synthetic histone H3 tail peptides in conjunction with other PTMs are substrates for OGT and OGA in vitro.
36357422	2	75	theme	moiety	392:397	arg1	introduction					341:352	the introduction	337:352	the introduction of the ß-N-acetylglucosamine (GlcNAc) moiety on histone H3 tail at position Ser10 and Thr32	337:444	One such PTM has been identified as serine and threonine glycosylation, the introduction of the ß-N-acetylglucosamine (GlcNAc) moiety on histone H3 tail at position Ser10 and Thr32.
36357422	3	76	dep	serine	488:493	arg1	residues					508:515	residues	508:515	residues	508:515	The addition of the ß-O-GlcNAc moiety on serine or threonine residues is facilitated by the O-GlcNAc transferase (OGT), and can be removed by the action of O-GlcNAcase (OGA).
36357422	7	77	theme	histone	1256:1262	arg1	peptides					1267:1274	deglycosylated histone H3 peptides	1241:1274	deglycosylated histone H3 peptides	1241:1274	Conversely, our work demonstrates that synthetic peptides containing the GlcNAc functionality at Ser10 are substrates for recombinantly expressed human OGA, yielding deglycosylated histone H3 peptides.
36357422	3	78	theme	O-GlcNAcase	603:613	arg1	action					593:598	the action	589:598	the action of O-GlcNAcase (OGA)	589:619	The addition of the ß-O-GlcNAc moiety on serine or threonine residues is facilitated by the O-GlcNAc transferase (OGT), and can be removed by the action of O-GlcNAcase (OGA).
36357422	0	79	theme	H3	34:35	arg1	glycosylation					37:49	in vitro histone H3 glycosylation	17:49	in vitro histone H3 glycosylation	17:49	Investigation of in vitro histone H3 glycosylation using H3 tail peptides.
36357422	8	80	dep	acetyltransferases	1398:1415	arg1	PCAF					1417:1420	PCAF	1417:1420	PCAF	1417:1420	We also show that the catalytic domains of human histone lysine methyltransferases G9a, GLP and SETD7 and histone lysine acetyltransferases PCAF and GCN5 do somewhat tolerate glycosylated H3Ser10 close to lysine residues that undergo methylation and acetylation reactions, respectively.
36357422	8	80	dep	acetyltransferases	1398:1415	arg1	acetyltransferases					1398:1415	histone lysine acetyltransferases PCAF and GCN5	1383:1429	histone lysine acetyltransferases PCAF and GCN5	1383:1429	We also show that the catalytic domains of human histone lysine methyltransferases G9a, GLP and SETD7 and histone lysine acetyltransferases PCAF and GCN5 do somewhat tolerate glycosylated H3Ser10 close to lysine residues that undergo methylation and acetylation reactions, respectively.
36357422	8	80	dep	acetyltransferases	1398:1415	arg1	GCN5					1426:1429	GCN5	1426:1429	GCN5	1426:1429	We also show that the catalytic domains of human histone lysine methyltransferases G9a, GLP and SETD7 and histone lysine acetyltransferases PCAF and GCN5 do somewhat tolerate glycosylated H3Ser10 close to lysine residues that undergo methylation and acetylation reactions, respectively.
36357422	8	81	theme	human	1320:1324	arg1	SETD7					1373:1377	SETD7	1373:1377	SETD7	1373:1377	We also show that the catalytic domains of human histone lysine methyltransferases G9a, GLP and SETD7 and histone lysine acetyltransferases PCAF and GCN5 do somewhat tolerate glycosylated H3Ser10 close to lysine residues that undergo methylation and acetylation reactions, respectively.
36357422	8	81	theme	human	1320:1324	arg1	methyltransferases					1341:1358	human histone lysine methyltransferases G9a, GLP and SETD7	1320:1377	human histone lysine methyltransferases G9a, GLP and SETD7	1320:1377	We also show that the catalytic domains of human histone lysine methyltransferases G9a, GLP and SETD7 and histone lysine acetyltransferases PCAF and GCN5 do somewhat tolerate glycosylated H3Ser10 close to lysine residues that undergo methylation and acetylation reactions, respectively.
36357422	8	81	theme	human	1320:1324	arg1	GLP					1365:1367	GLP	1365:1367	GLP	1365:1367	We also show that the catalytic domains of human histone lysine methyltransferases G9a, GLP and SETD7 and histone lysine acetyltransferases PCAF and GCN5 do somewhat tolerate glycosylated H3Ser10 close to lysine residues that undergo methylation and acetylation reactions, respectively.
36357422	8	81	theme	human	1320:1324	arg1	G9a					1360:1362	G9a	1360:1362	G9a	1360:1362	We also show that the catalytic domains of human histone lysine methyltransferases G9a, GLP and SETD7 and histone lysine acetyltransferases PCAF and GCN5 do somewhat tolerate glycosylated H3Ser10 close to lysine residues that undergo methylation and acetylation reactions, respectively.
36357422	2	82	theme	histone	402:408	arg1	H3					410:411	histone H3	402:411	histone H3 tail	402:416	One such PTM has been identified as serine and threonine glycosylation, the introduction of the ß-N-acetylglucosamine (GlcNAc) moiety on histone H3 tail at position Ser10 and Thr32.
36357422	7	83	theme	expressed	1211:1219	arg1	OGA					1227:1229	recombinantly expressed human OGA	1197:1229	recombinantly expressed human OGA	1197:1229	Conversely, our work demonstrates that synthetic peptides containing the GlcNAc functionality at Ser10 are substrates for recombinantly expressed human OGA, yielding deglycosylated histone H3 peptides.
36357422	8	84	theme	lysine	1334:1339	arg1	SETD7					1373:1377	SETD7	1373:1377	SETD7	1373:1377	We also show that the catalytic domains of human histone lysine methyltransferases G9a, GLP and SETD7 and histone lysine acetyltransferases PCAF and GCN5 do somewhat tolerate glycosylated H3Ser10 close to lysine residues that undergo methylation and acetylation reactions, respectively.
36357422	8	84	theme	lysine	1334:1339	arg1	methyltransferases					1341:1358	human histone lysine methyltransferases G9a, GLP and SETD7	1320:1377	human histone lysine methyltransferases G9a, GLP and SETD7	1320:1377	We also show that the catalytic domains of human histone lysine methyltransferases G9a, GLP and SETD7 and histone lysine acetyltransferases PCAF and GCN5 do somewhat tolerate glycosylated H3Ser10 close to lysine residues that undergo methylation and acetylation reactions, respectively.
36357422	8	84	theme	lysine	1334:1339	arg1	GLP					1365:1367	GLP	1365:1367	GLP	1365:1367	We also show that the catalytic domains of human histone lysine methyltransferases G9a, GLP and SETD7 and histone lysine acetyltransferases PCAF and GCN5 do somewhat tolerate glycosylated H3Ser10 close to lysine residues that undergo methylation and acetylation reactions, respectively.
36357422	8	84	theme	lysine	1334:1339	arg1	G9a					1360:1362	G9a	1360:1362	G9a	1360:1362	We also show that the catalytic domains of human histone lysine methyltransferases G9a, GLP and SETD7 and histone lysine acetyltransferases PCAF and GCN5 do somewhat tolerate glycosylated H3Ser10 close to lysine residues that undergo methylation and acetylation reactions, respectively.
36357422	3	85	from	addition	451:458	arg1	threonine					498:506	threonine	498:506	threonine	498:506	The addition of the ß-O-GlcNAc moiety on serine or threonine residues is facilitated by the O-GlcNAc transferase (OGT), and can be removed by the action of O-GlcNAcase (OGA).
36357422	3	85	from	addition	451:458	arg1	serine					488:493	serine	488:493	serine	488:493	The addition of the ß-O-GlcNAc moiety on serine or threonine residues is facilitated by the O-GlcNAc transferase (OGT), and can be removed by the action of O-GlcNAcase (OGA).
36357422	2	86	from	moiety	392:397	arg1	tail					413:416	histone H3 tail	402:416	histone H3 tail	402:416	One such PTM has been identified as serine and threonine glycosylation, the introduction of the ß-N-acetylglucosamine (GlcNAc) moiety on histone H3 tail at position Ser10 and Thr32.
36357422	4	87	theme	tail	742:745	arg1	substrates					791:800	substrates	791:800	substrates for OGT and OGA in vitro	791:825	Conflicting reports on histone tail GlcNAc modification in vivo prompted us to investigate whether synthetic histone H3 tail peptides in conjunction with other PTMs are substrates for OGT and OGA in vitro.
36357422	4	87	theme	tail	742:745	arg1	peptides					747:754	synthetic histone H3 tail peptides	721:754	synthetic histone H3 tail peptides in conjunction with other PTMs	721:785	Conflicting reports on histone tail GlcNAc modification in vivo prompted us to investigate whether synthetic histone H3 tail peptides in conjunction with other PTMs are substrates for OGT and OGA in vitro.
36357422	3	88	theme	ß-O-GlcNAc	467:476	arg1	moiety					478:483	the ß-O-GlcNAc moiety	463:483	the ß-O-GlcNAc moiety	463:483	The addition of the ß-O-GlcNAc moiety on serine or threonine residues is facilitated by the O-GlcNAc transferase (OGT), and can be removed by the action of O-GlcNAcase (OGA).
36357422	6	89	theme	histone	1035:1041	arg1	substrate					1056:1064	a substrate	1054:1064	a substrate for OGT	1054:1072	In addition, full length histone H3 was not a substrate for OGT.
36357422	6	89	theme	histone	1035:1041	arg1	H3					1043:1044	full length histone H3	1023:1044	full length histone H3	1023:1044	In addition, full length histone H3 was not a substrate for OGT.
36357422	2	90	theme	ß-N-acetylglucosamine	361:381	arg1	moiety					392:397	the ß-N-acetylglucosamine (GlcNAc) moiety	357:397	the ß-N-acetylglucosamine (GlcNAc) moiety on histone H3 tail	357:416	One such PTM has been identified as serine and threonine glycosylation, the introduction of the ß-N-acetylglucosamine (GlcNAc) moiety on histone H3 tail at position Ser10 and Thr32.
36357422	2	90	theme	ß-N-acetylglucosamine	361:381	arg1	GlcNAc					384:389	GlcNAc	384:389	GlcNAc	384:389	One such PTM has been identified as serine and threonine glycosylation, the introduction of the ß-N-acetylglucosamine (GlcNAc) moiety on histone H3 tail at position Ser10 and Thr32.
36357422	1	91	theme	cellular	246:253	arg1	proteins					255:262	other cellular proteins	240:262	other cellular proteins	240:262	Posttranslational modifications (PTMs) on histone tails regulate eukaryotic gene expression by impacting the chromatin structure and by modulating interactions with other cellular proteins.
28861343	9	0	theme	diabetes-induced	1737:1752	arg1	neurodegeneration					1754:1770	diabetes-induced neurodegeneration	1737:1770	diabetes-induced neurodegeneration	1737:1770	Hence, O-GlcNAcylation may be a new object for the treatment of DR, and AE may have therapeutic possibility to prevent diabetes-induced neurodegeneration.
28861343	3	1	theme	O-GlcNAcylation	648:662	arg1	expression					541:550	the expression	537:550	the expression of O-GlcNAc transferase (OGT), N-acetyl-b-D-glucosaminidase (OGA), O-GlcNAcylated proteins, and O-GlcNAcylation of NF-κB	537:671	Two months after injection of streptozotocin or saline, the degree of cell death and the expression of O-GlcNAc transferase (OGT), N-acetyl-b-D-glucosaminidase (OGA), O-GlcNAcylated proteins, and O-GlcNAcylation of NF-κB were examined.
28861343	3	1	theme	O-GlcNAcylation	648:662	arg1	months					456:461	Two months	452:461	Two months after injection of streptozotocin or saline	452:505	Two months after injection of streptozotocin or saline, the degree of cell death and the expression of O-GlcNAc transferase (OGT), N-acetyl-b-D-glucosaminidase (OGA), O-GlcNAcylated proteins, and O-GlcNAcylation of NF-κB were examined.
28861343	3	1	theme	O-GlcNAcylation	648:662	arg1	degree					512:517	the degree	508:517	the degree of cell death	508:531	Two months after injection of streptozotocin or saline, the degree of cell death and the expression of O-GlcNAc transferase (OGT), N-acetyl-b-D-glucosaminidase (OGA), O-GlcNAcylated proteins, and O-GlcNAcylation of NF-κB were examined.
28861343	1	2	from	neurodegeneration	266:282	arg1	mice					296:299	diabetic mice	287:299	diabetic mice	287:299	AIM To investigate the role of O-GlcNAcylation of nuclear factor-kappa B (NF-κB) in retinal ganglion cell (RGC) death and analysedthe effect of Aralia elata (AE) on neurodegeneration in diabetic mice.
28861343	8	3	theme	RGC	1559:1561	arg1	apoptosis					1563:1571	diabetes-induced RGC apoptosis	1542:1571	diabetes-induced RGC apoptosis	1542:1571	CONCLUSION O-GlcNAcylation of NF-κB is concerned in neuronal degeneration and that AE prevents diabetes-induced RGC apoptosis via downregulation of NF-κB O-GlcNAcylation.
28861343	1	4	theme	Aralia	245:250	arg1	AE					259:260	AE	259:260	AE	259:260	AIM To investigate the role of O-GlcNAcylation of nuclear factor-kappa B (NF-κB) in retinal ganglion cell (RGC) death and analysedthe effect of Aralia elata (AE) on neurodegeneration in diabetic mice.
28861343	1	4	theme	Aralia	245:250	arg1	elata					252:256	Aralia elata	245:256	Aralia elata (AE)	245:261	AIM To investigate the role of O-GlcNAcylation of nuclear factor-kappa B (NF-κB) in retinal ganglion cell (RGC) death and analysedthe effect of Aralia elata (AE) on neurodegeneration in diabetic mice.
28861343	6	5	theme	protein	1111:1117	arg1	O-GlcNAcylation					1119:1133	protein O-GlcNAcylation	1111:1133	protein O-GlcNAcylation	1111:1133	Expression levels of protein O-GlcNAcylation and OGT were increased in diabetic retinas (P<0.0001 vs CTL), and the level of O-GlcNAcylation of the NF-κB p65 subunit was higher in diabetic retinas than in controls (P<0.0001 vs CTL).
28861343	5	6	from	caspase-3	989:997	arg1	thickness					787:795	the inner retinal thickness	769:795	the inner retinal thickness (P<0.001 vs CTL, P<0.01 vs DM)	769:826	The decrease in the inner retinal thickness (P<0.001 vs CTL, P<0.01 vs DM) and increases in RGCs with terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling (P<0.001 vs CTL, P<0.0001 vs DM), glial activation, and active caspase-3 (P<0.0001 vs CTL, P<0.0001 vs DM) were blocked in diabetic retinas of AE extract-fed mice.
28861343	5	6	from	caspase-3	989:997	arg1	increases					832:840	increases	832:840	increases in RGCs with terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling (P<0.001 vs CTL, P<0.0001 vs DM)	832:957	The decrease in the inner retinal thickness (P<0.001 vs CTL, P<0.01 vs DM) and increases in RGCs with terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling (P<0.001 vs CTL, P<0.0001 vs DM), glial activation, and active caspase-3 (P<0.0001 vs CTL, P<0.0001 vs DM) were blocked in diabetic retinas of AE extract-fed mice.
28861343	5	7	theme	retinal	779:785	arg1	thickness					787:795	the inner retinal thickness	769:795	the inner retinal thickness (P<0.001 vs CTL, P<0.01 vs DM)	769:826	The decrease in the inner retinal thickness (P<0.001 vs CTL, P<0.01 vs DM) and increases in RGCs with terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling (P<0.001 vs CTL, P<0.0001 vs DM), glial activation, and active caspase-3 (P<0.0001 vs CTL, P<0.0001 vs DM) were blocked in diabetic retinas of AE extract-fed mice.
28861343	5	8	with	RGCs	845:848	arg1	labelling					916:924	terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling	855:924	terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling (P<0.001 vs CTL, P<0.0001 vs DM)	855:957	The decrease in the inner retinal thickness (P<0.001 vs CTL, P<0.01 vs DM) and increases in RGCs with terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling (P<0.001 vs CTL, P<0.0001 vs DM), glial activation, and active caspase-3 (P<0.0001 vs CTL, P<0.0001 vs DM) were blocked in diabetic retinas of AE extract-fed mice.
28861343	3	9	theme	NF-κB	667:671	arg1	transferase					564:574	O-GlcNAc transferase	555:574	O-GlcNAc transferase (OGT)	555:580	Two months after injection of streptozotocin or saline, the degree of cell death and the expression of O-GlcNAc transferase (OGT), N-acetyl-b-D-glucosaminidase (OGA), O-GlcNAcylated proteins, and O-GlcNAcylation of NF-κB were examined.
28861343	3	9	theme	NF-κB	667:671	arg1	O-GlcNAcylation					648:662	O-GlcNAcylation	648:662	O-GlcNAcylation of NF-κB	648:671	Two months after injection of streptozotocin or saline, the degree of cell death and the expression of O-GlcNAc transferase (OGT), N-acetyl-b-D-glucosaminidase (OGA), O-GlcNAcylated proteins, and O-GlcNAcylation of NF-κB were examined.
28861343	3	9	theme	NF-κB	667:671	arg1	OGT					577:579	OGT	577:579	OGT	577:579	Two months after injection of streptozotocin or saline, the degree of cell death and the expression of O-GlcNAc transferase (OGT), N-acetyl-b-D-glucosaminidase (OGA), O-GlcNAcylated proteins, and O-GlcNAcylation of NF-κB were examined.
28861343	3	9	theme	NF-κB	667:671	arg1	proteins					634:641	O-GlcNAcylated proteins	619:641	O-GlcNAcylated proteins	619:641	Two months after injection of streptozotocin or saline, the degree of cell death and the expression of O-GlcNAc transferase (OGT), N-acetyl-b-D-glucosaminidase (OGA), O-GlcNAcylated proteins, and O-GlcNAcylation of NF-κB were examined.
28861343	3	9	theme	NF-κB	667:671	arg1	N-acetyl-b-D-glucosaminidase					583:610	N-acetyl-b-D-glucosaminidase	583:610	N-acetyl-b-D-glucosaminidase (OGA)	583:616	Two months after injection of streptozotocin or saline, the degree of cell death and the expression of O-GlcNAc transferase (OGT), N-acetyl-b-D-glucosaminidase (OGA), O-GlcNAcylated proteins, and O-GlcNAcylation of NF-κB were examined.
28861343	3	9	theme	NF-κB	667:671	arg1	OGA					613:615	OGA	613:615	OGA	613:615	Two months after injection of streptozotocin or saline, the degree of cell death and the expression of O-GlcNAc transferase (OGT), N-acetyl-b-D-glucosaminidase (OGA), O-GlcNAcylated proteins, and O-GlcNAcylation of NF-κB were examined.
28861343	7	10	dep	hyperglycemia	1415:1427	arg1	DM					1442:1443	DM	1442:1443	DM	1442:1443	AE extract downregulated O-GlcNAcylation of NF-κB and prevented neurodegeneration induced by hyperglycemia (P<0.0001 vs DM).
28861343	7	10	dep	hyperglycemia	1415:1427	arg1	P<0.0001					1430:1437	P<0.0001	1430:1437	P<0.0001	1430:1437	AE extract downregulated O-GlcNAcylation of NF-κB and prevented neurodegeneration induced by hyperglycemia (P<0.0001 vs DM).
28861343	8	11	theme	O-GlcNAcylation	1601:1615	arg1	downregulation					1577:1590	downregulation	1577:1590	downregulation of NF-κB O-GlcNAcylation	1577:1615	CONCLUSION O-GlcNAcylation of NF-κB is concerned in neuronal degeneration and that AE prevents diabetes-induced RGC apoptosis via downregulation of NF-κB O-GlcNAcylation.
28861343	1	12	theme	ganglion	193:200	arg1	RGC					208:210	RGC	208:210	RGC	208:210	AIM To investigate the role of O-GlcNAcylation of nuclear factor-kappa B (NF-κB) in retinal ganglion cell (RGC) death and analysedthe effect of Aralia elata (AE) on neurodegeneration in diabetic mice.
28861343	1	12	theme	ganglion	193:200	arg1	cell					202:205	retinal ganglion cell	185:205	retinal ganglion cell (RGC) death	185:217	AIM To investigate the role of O-GlcNAcylation of nuclear factor-kappa B (NF-κB) in retinal ganglion cell (RGC) death and analysedthe effect of Aralia elata (AE) on neurodegeneration in diabetic mice.
28861343	6	13	theme	Expression	1090:1099	arg1	levels					1101:1106	Expression levels	1090:1106	Expression levels of protein O-GlcNAcylation and OGT	1090:1141	Expression levels of protein O-GlcNAcylation and OGT were increased in diabetic retinas (P<0.0001 vs CTL), and the level of O-GlcNAcylation of the NF-κB p65 subunit was higher in diabetic retinas than in controls (P<0.0001 vs CTL).
28861343	1	14	from	effect	235:240	arg1	death					213:217	retinal ganglion cell (RGC) death	185:217	retinal ganglion cell (RGC) death	185:217	AIM To investigate the role of O-GlcNAcylation of nuclear factor-kappa B (NF-κB) in retinal ganglion cell (RGC) death and analysedthe effect of Aralia elata (AE) on neurodegeneration in diabetic mice.
28861343	1	14	from	effect	235:240	arg1	neurodegeneration					266:282	neurodegeneration	266:282	neurodegeneration in diabetic mice	266:299	AIM To investigate the role of O-GlcNAcylation of nuclear factor-kappa B (NF-κB) in retinal ganglion cell (RGC) death and analysedthe effect of Aralia elata (AE) on neurodegeneration in diabetic mice.
28861343	5	15	theme	glial	960:964	arg1	activation					966:975	glial activation	960:975	glial activation	960:975	The decrease in the inner retinal thickness (P<0.001 vs CTL, P<0.01 vs DM) and increases in RGCs with terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling (P<0.001 vs CTL, P<0.0001 vs DM), glial activation, and active caspase-3 (P<0.0001 vs CTL, P<0.0001 vs DM) were blocked in diabetic retinas of AE extract-fed mice.
28861343	6	16	theme	diabetic	1269:1276	arg1	retinas					1278:1284	diabetic retinas	1269:1284	diabetic retinas	1269:1284	Expression levels of protein O-GlcNAcylation and OGT were increased in diabetic retinas (P<0.0001 vs CTL), and the level of O-GlcNAcylation of the NF-κB p65 subunit was higher in diabetic retinas than in controls (P<0.0001 vs CTL).
28861343	3	17	theme	cell	522:525	arg1	death					527:531	cell death	522:531	cell death	522:531	Two months after injection of streptozotocin or saline, the degree of cell death and the expression of O-GlcNAc transferase (OGT), N-acetyl-b-D-glucosaminidase (OGA), O-GlcNAcylated proteins, and O-GlcNAcylation of NF-κB were examined.
28861343	3	18	theme	O-GlcNAc	555:562	arg1	OGT					577:579	OGT	577:579	OGT	577:579	Two months after injection of streptozotocin or saline, the degree of cell death and the expression of O-GlcNAc transferase (OGT), N-acetyl-b-D-glucosaminidase (OGA), O-GlcNAcylated proteins, and O-GlcNAcylation of NF-κB were examined.
28861343	3	18	theme	O-GlcNAc	555:562	arg1	transferase					564:574	O-GlcNAc transferase	555:574	O-GlcNAc transferase (OGT)	555:580	Two months after injection of streptozotocin or saline, the degree of cell death and the expression of O-GlcNAc transferase (OGT), N-acetyl-b-D-glucosaminidase (OGA), O-GlcNAcylated proteins, and O-GlcNAcylation of NF-κB were examined.
28861343	5	19	from	thickness	787:795	arg1	RGCs					845:848	RGCs	845:848	RGCs with terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling (P<0.001 vs CTL, P<0.0001 vs DM)	845:957	The decrease in the inner retinal thickness (P<0.001 vs CTL, P<0.01 vs DM) and increases in RGCs with terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling (P<0.001 vs CTL, P<0.0001 vs DM), glial activation, and active caspase-3 (P<0.0001 vs CTL, P<0.0001 vs DM) were blocked in diabetic retinas of AE extract-fed mice.
28861343	1	20	theme	O-GlcNAcylation	132:146	arg1	effect					235:240	analysedthe effect	223:240	analysedthe effect of Aralia elata (AE) on neurodegeneration in diabetic mice	223:299	AIM To investigate the role of O-GlcNAcylation of nuclear factor-kappa B (NF-κB) in retinal ganglion cell (RGC) death and analysedthe effect of Aralia elata (AE) on neurodegeneration in diabetic mice.
28861343	1	20	theme	O-GlcNAcylation	132:146	arg1	role					124:127	the role	120:127	the role of O-GlcNAcylation of nuclear factor-kappa B (NF-κB) in retinal ganglion cell (RGC) death	120:217	AIM To investigate the role of O-GlcNAcylation of nuclear factor-kappa B (NF-κB) in retinal ganglion cell (RGC) death and analysedthe effect of Aralia elata (AE) on neurodegeneration in diabetic mice.
28861343	0	21	theme	NF-κB	77:81	arg1	O-GlcNAcylation					58:72	O-GlcNAcylation	58:72	O-GlcNAcylation of NF-κB in diabetic mice	58:98	Aralia elata inhibits neurodegeneration by downregulating O-GlcNAcylation of NF-κB in diabetic mice.
28861343	1	22	theme	nuclear	151:157	arg1	NF-κB					175:179	NF-κB	175:179	NF-κB	175:179	AIM To investigate the role of O-GlcNAcylation of nuclear factor-kappa B (NF-κB) in retinal ganglion cell (RGC) death and analysedthe effect of Aralia elata (AE) on neurodegeneration in diabetic mice.
28861343	1	22	theme	nuclear	151:157	arg1	B					172:172	nuclear factor-kappa B	151:172	nuclear factor-kappa B (NF-κB)	151:180	AIM To investigate the role of O-GlcNAcylation of nuclear factor-kappa B (NF-κB) in retinal ganglion cell (RGC) death and analysedthe effect of Aralia elata (AE) on neurodegeneration in diabetic mice.
28861343	0	23	theme	diabetic	86:93	arg1	mice					95:98	diabetic mice	86:98	diabetic mice	86:98	Aralia elata inhibits neurodegeneration by downregulating O-GlcNAcylation of NF-κB in diabetic mice.
28861343	1	24	theme	B	172:172	arg1	O-GlcNAcylation					132:146	O-GlcNAcylation	132:146	O-GlcNAcylation of nuclear factor-kappa B (NF-κB)	132:180	AIM To investigate the role of O-GlcNAcylation of nuclear factor-kappa B (NF-κB) in retinal ganglion cell (RGC) death and analysedthe effect of Aralia elata (AE) on neurodegeneration in diabetic mice.
28861343	5	25	from	activation	966:975	arg1	thickness					787:795	the inner retinal thickness	769:795	the inner retinal thickness (P<0.001 vs CTL, P<0.01 vs DM)	769:826	The decrease in the inner retinal thickness (P<0.001 vs CTL, P<0.01 vs DM) and increases in RGCs with terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling (P<0.001 vs CTL, P<0.0001 vs DM), glial activation, and active caspase-3 (P<0.0001 vs CTL, P<0.0001 vs DM) were blocked in diabetic retinas of AE extract-fed mice.
28861343	5	25	from	activation	966:975	arg1	increases					832:840	increases	832:840	increases in RGCs with terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling (P<0.001 vs CTL, P<0.0001 vs DM)	832:957	The decrease in the inner retinal thickness (P<0.001 vs CTL, P<0.01 vs DM) and increases in RGCs with terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling (P<0.001 vs CTL, P<0.0001 vs DM), glial activation, and active caspase-3 (P<0.0001 vs CTL, P<0.0001 vs DM) were blocked in diabetic retinas of AE extract-fed mice.
28861343	5	26	theme	terminal	855:862	arg1	labelling					916:924	terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling	855:924	terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling (P<0.001 vs CTL, P<0.0001 vs DM)	855:957	The decrease in the inner retinal thickness (P<0.001 vs CTL, P<0.01 vs DM) and increases in RGCs with terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling (P<0.001 vs CTL, P<0.0001 vs DM), glial activation, and active caspase-3 (P<0.0001 vs CTL, P<0.0001 vs DM) were blocked in diabetic retinas of AE extract-fed mice.
28861343	0	27	from	O-GlcNAcylation	58:72	arg1	mice					95:98	diabetic mice	86:98	diabetic mice	86:98	Aralia elata inhibits neurodegeneration by downregulating O-GlcNAcylation of NF-κB in diabetic mice.
28861343	2	28	theme	AE	379:380	arg1	extract					382:388	AE extract	379:388	AE extract	379:388	METHODS C57BL/6mice with streptozotocin-induced diabetes were fed daily with AE extract or control (CTL) diet at the onset of diabetes mellitus (DM).
28861343	5	29	theme	AE	1069:1070	arg1	mice					1084:1087	AE extract-fed mice	1069:1087	AE extract-fed mice	1069:1087	The decrease in the inner retinal thickness (P<0.001 vs CTL, P<0.01 vs DM) and increases in RGCs with terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling (P<0.001 vs CTL, P<0.0001 vs DM), glial activation, and active caspase-3 (P<0.0001 vs CTL, P<0.0001 vs DM) were blocked in diabetic retinas of AE extract-fed mice.
28861343	5	30	theme	active	982:987	arg1	caspase-3					989:997	active caspase-3	982:997	active caspase-3 (P<0.0001 vs CTL, P<0.0001 vs DM)	982:1031	The decrease in the inner retinal thickness (P<0.001 vs CTL, P<0.01 vs DM) and increases in RGCs with terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling (P<0.001 vs CTL, P<0.0001 vs DM), glial activation, and active caspase-3 (P<0.0001 vs CTL, P<0.0001 vs DM) were blocked in diabetic retinas of AE extract-fed mice.
28861343	5	31	theme	transferase-mediated	881:900	arg1	labelling					916:924	terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling	855:924	terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling (P<0.001 vs CTL, P<0.0001 vs DM)	855:957	The decrease in the inner retinal thickness (P<0.001 vs CTL, P<0.01 vs DM) and increases in RGCs with terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling (P<0.001 vs CTL, P<0.0001 vs DM), glial activation, and active caspase-3 (P<0.0001 vs CTL, P<0.0001 vs DM) were blocked in diabetic retinas of AE extract-fed mice.
28861343	0	32	theme	Aralia	0:5	arg1	elata					7:11	Aralia elata	0:11	Aralia elata	0:11	Aralia elata inhibits neurodegeneration by downregulating O-GlcNAcylation of NF-κB in diabetic mice.
28861343	1	33	theme	elata	252:256	arg1	effect					235:240	analysedthe effect	223:240	analysedthe effect of Aralia elata (AE) on neurodegeneration in diabetic mice	223:299	AIM To investigate the role of O-GlcNAcylation of nuclear factor-kappa B (NF-κB) in retinal ganglion cell (RGC) death and analysedthe effect of Aralia elata (AE) on neurodegeneration in diabetic mice.
28861343	1	33	theme	elata	252:256	arg1	role					124:127	the role	120:127	the role of O-GlcNAcylation of nuclear factor-kappa B (NF-κB) in retinal ganglion cell (RGC) death	120:217	AIM To investigate the role of O-GlcNAcylation of nuclear factor-kappa B (NF-κB) in retinal ganglion cell (RGC) death and analysedthe effect of Aralia elata (AE) on neurodegeneration in diabetic mice.
28861343	5	34	dep	P<0.001	798:804	arg1	DM					824:825	DM	824:825	DM	824:825	The decrease in the inner retinal thickness (P<0.001 vs CTL, P<0.01 vs DM) and increases in RGCs with terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling (P<0.001 vs CTL, P<0.0001 vs DM), glial activation, and active caspase-3 (P<0.0001 vs CTL, P<0.0001 vs DM) were blocked in diabetic retinas of AE extract-fed mice.
28861343	5	34	dep	P<0.001	798:804	arg1	P<0.01					814:819	P<0.01	814:819	P<0.01	814:819	The decrease in the inner retinal thickness (P<0.001 vs CTL, P<0.01 vs DM) and increases in RGCs with terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling (P<0.001 vs CTL, P<0.0001 vs DM), glial activation, and active caspase-3 (P<0.0001 vs CTL, P<0.0001 vs DM) were blocked in diabetic retinas of AE extract-fed mice.
28861343	4	35	theme	diabetic	738:745	arg1	mice					747:750	diabetic mice	738:750	diabetic mice	738:750	RESULTS AE did not affect the metabolic status of diabetic mice.
28861343	7	36	theme	NF-κB	1366:1370	arg1	O-GlcNAcylation					1347:1361	O-GlcNAcylation	1347:1361	O-GlcNAcylation of NF-κB	1347:1370	AE extract downregulated O-GlcNAcylation of NF-κB and prevented neurodegeneration induced by hyperglycemia (P<0.0001 vs DM).
28861343	2	37	theme	diabetes	428:435	arg1	DM					447:448	DM	447:448	DM	447:448	METHODS C57BL/6mice with streptozotocin-induced diabetes were fed daily with AE extract or control (CTL) diet at the onset of diabetes mellitus (DM).
28861343	2	37	theme	diabetes	428:435	arg1	mellitus					437:444	diabetes mellitus	428:444	diabetes mellitus (DM)	428:449	METHODS C57BL/6mice with streptozotocin-induced diabetes were fed daily with AE extract or control (CTL) diet at the onset of diabetes mellitus (DM).
28861343	5	38	dep	P<0.0001	1000:1007	arg1	DM					1029:1030	DM	1029:1030	DM	1029:1030	The decrease in the inner retinal thickness (P<0.001 vs CTL, P<0.01 vs DM) and increases in RGCs with terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling (P<0.001 vs CTL, P<0.0001 vs DM), glial activation, and active caspase-3 (P<0.0001 vs CTL, P<0.0001 vs DM) were blocked in diabetic retinas of AE extract-fed mice.
28861343	5	38	dep	P<0.0001	1000:1007	arg1	P<0.0001					1017:1024	P<0.0001	1017:1024	P<0.0001	1017:1024	The decrease in the inner retinal thickness (P<0.001 vs CTL, P<0.01 vs DM) and increases in RGCs with terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling (P<0.001 vs CTL, P<0.0001 vs DM), glial activation, and active caspase-3 (P<0.0001 vs CTL, P<0.0001 vs DM) were blocked in diabetic retinas of AE extract-fed mice.
28861343	9	39	contain	have	1697:1700	arg1	AE					1690:1691	AE	1690:1691	AE	1690:1691	Hence, O-GlcNAcylation may be a new object for the treatment of DR, and AE may have therapeutic possibility to prevent diabetes-induced neurodegeneration.
28861343	9	39	contain	have	1697:1700	arg2	possibility					1714:1724	therapeutic possibility	1702:1724	therapeutic possibility	1702:1724	Hence, O-GlcNAcylation may be a new object for the treatment of DR, and AE may have therapeutic possibility to prevent diabetes-induced neurodegeneration.
28861343	5	40	dep	thickness	787:795	arg1	CTL					809:811	CTL	809:811	CTL	809:811	The decrease in the inner retinal thickness (P<0.001 vs CTL, P<0.01 vs DM) and increases in RGCs with terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling (P<0.001 vs CTL, P<0.0001 vs DM), glial activation, and active caspase-3 (P<0.0001 vs CTL, P<0.0001 vs DM) were blocked in diabetic retinas of AE extract-fed mice.
28861343	5	40	dep	thickness	787:795	arg1	P<0.001					798:804	P<0.001	798:804	P<0.001	798:804	The decrease in the inner retinal thickness (P<0.001 vs CTL, P<0.01 vs DM) and increases in RGCs with terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling (P<0.001 vs CTL, P<0.0001 vs DM), glial activation, and active caspase-3 (P<0.0001 vs CTL, P<0.0001 vs DM) were blocked in diabetic retinas of AE extract-fed mice.
28861343	6	41	theme	subunit	1247:1253	arg1	level					1205:1209	the level	1201:1209	the level of O-GlcNAcylation of the NF-κB p65 subunit	1201:1253	Expression levels of protein O-GlcNAcylation and OGT were increased in diabetic retinas (P<0.0001 vs CTL), and the level of O-GlcNAcylation of the NF-κB p65 subunit was higher in diabetic retinas than in controls (P<0.0001 vs CTL).
28861343	6	41	theme	subunit	1247:1253	arg1	higher					1259:1264	higher	1259:1264	higher	1259:1264	Expression levels of protein O-GlcNAcylation and OGT were increased in diabetic retinas (P<0.0001 vs CTL), and the level of O-GlcNAcylation of the NF-κB p65 subunit was higher in diabetic retinas than in controls (P<0.0001 vs CTL).
28861343	2	42	with	C57BL/6mice	310:320	arg1	diabetes					350:357	streptozotocin-induced diabetes	327:357	streptozotocin-induced diabetes	327:357	METHODS C57BL/6mice with streptozotocin-induced diabetes were fed daily with AE extract or control (CTL) diet at the onset of diabetes mellitus (DM).
28861343	5	43	dep	caspase-3	989:997	arg1	P<0.0001					1000:1007	P<0.0001	1000:1007	P<0.0001	1000:1007	The decrease in the inner retinal thickness (P<0.001 vs CTL, P<0.01 vs DM) and increases in RGCs with terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling (P<0.001 vs CTL, P<0.0001 vs DM), glial activation, and active caspase-3 (P<0.0001 vs CTL, P<0.0001 vs DM) were blocked in diabetic retinas of AE extract-fed mice.
28861343	5	43	dep	caspase-3	989:997	arg1	CTL					1012:1014	CTL	1012:1014	CTL	1012:1014	The decrease in the inner retinal thickness (P<0.001 vs CTL, P<0.01 vs DM) and increases in RGCs with terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling (P<0.001 vs CTL, P<0.0001 vs DM), glial activation, and active caspase-3 (P<0.0001 vs CTL, P<0.0001 vs DM) were blocked in diabetic retinas of AE extract-fed mice.
28861343	6	44	theme	NF-κB	1237:1241	arg1	subunit					1247:1253	the NF-κB p65 subunit	1233:1253	the NF-κB p65 subunit	1233:1253	Expression levels of protein O-GlcNAcylation and OGT were increased in diabetic retinas (P<0.0001 vs CTL), and the level of O-GlcNAcylation of the NF-κB p65 subunit was higher in diabetic retinas than in controls (P<0.0001 vs CTL).
28861343	5	45	theme	extract-fed	1072:1082	arg1	mice					1084:1087	AE extract-fed mice	1069:1087	AE extract-fed mice	1069:1087	The decrease in the inner retinal thickness (P<0.001 vs CTL, P<0.01 vs DM) and increases in RGCs with terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling (P<0.001 vs CTL, P<0.0001 vs DM), glial activation, and active caspase-3 (P<0.0001 vs CTL, P<0.0001 vs DM) were blocked in diabetic retinas of AE extract-fed mice.
28861343	5	46	theme	nick	907:910	arg1	labelling					916:924	terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling	855:924	terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling (P<0.001 vs CTL, P<0.0001 vs DM)	855:957	The decrease in the inner retinal thickness (P<0.001 vs CTL, P<0.01 vs DM) and increases in RGCs with terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling (P<0.001 vs CTL, P<0.0001 vs DM), glial activation, and active caspase-3 (P<0.0001 vs CTL, P<0.0001 vs DM) were blocked in diabetic retinas of AE extract-fed mice.
28861343	3	47	theme	N-acetyl-b-D-glucosaminidase	583:610	arg1	expression					541:550	the expression	537:550	the expression of O-GlcNAc transferase (OGT), N-acetyl-b-D-glucosaminidase (OGA), O-GlcNAcylated proteins, and O-GlcNAcylation of NF-κB	537:671	Two months after injection of streptozotocin or saline, the degree of cell death and the expression of O-GlcNAc transferase (OGT), N-acetyl-b-D-glucosaminidase (OGA), O-GlcNAcylated proteins, and O-GlcNAcylation of NF-κB were examined.
28861343	3	47	theme	N-acetyl-b-D-glucosaminidase	583:610	arg1	months					456:461	Two months	452:461	Two months after injection of streptozotocin or saline	452:505	Two months after injection of streptozotocin or saline, the degree of cell death and the expression of O-GlcNAc transferase (OGT), N-acetyl-b-D-glucosaminidase (OGA), O-GlcNAcylated proteins, and O-GlcNAcylation of NF-κB were examined.
28861343	3	47	theme	N-acetyl-b-D-glucosaminidase	583:610	arg1	degree					512:517	the degree	508:517	the degree of cell death	508:531	Two months after injection of streptozotocin or saline, the degree of cell death and the expression of O-GlcNAc transferase (OGT), N-acetyl-b-D-glucosaminidase (OGA), O-GlcNAcylated proteins, and O-GlcNAcylation of NF-κB were examined.
28861343	5	48	from	increases	832:840	arg1	RGCs					845:848	RGCs	845:848	RGCs with terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling (P<0.001 vs CTL, P<0.0001 vs DM)	845:957	The decrease in the inner retinal thickness (P<0.001 vs CTL, P<0.01 vs DM) and increases in RGCs with terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling (P<0.001 vs CTL, P<0.0001 vs DM), glial activation, and active caspase-3 (P<0.0001 vs CTL, P<0.0001 vs DM) were blocked in diabetic retinas of AE extract-fed mice.
28861343	3	49	theme	proteins	634:641	arg1	expression					541:550	the expression	537:550	the expression of O-GlcNAc transferase (OGT), N-acetyl-b-D-glucosaminidase (OGA), O-GlcNAcylated proteins, and O-GlcNAcylation of NF-κB	537:671	Two months after injection of streptozotocin or saline, the degree of cell death and the expression of O-GlcNAc transferase (OGT), N-acetyl-b-D-glucosaminidase (OGA), O-GlcNAcylated proteins, and O-GlcNAcylation of NF-κB were examined.
28861343	3	49	theme	proteins	634:641	arg1	months					456:461	Two months	452:461	Two months after injection of streptozotocin or saline	452:505	Two months after injection of streptozotocin or saline, the degree of cell death and the expression of O-GlcNAc transferase (OGT), N-acetyl-b-D-glucosaminidase (OGA), O-GlcNAcylated proteins, and O-GlcNAcylation of NF-κB were examined.
28861343	3	49	theme	proteins	634:641	arg1	degree					512:517	the degree	508:517	the degree of cell death	508:531	Two months after injection of streptozotocin or saline, the degree of cell death and the expression of O-GlcNAc transferase (OGT), N-acetyl-b-D-glucosaminidase (OGA), O-GlcNAcylated proteins, and O-GlcNAcylation of NF-κB were examined.
28861343	2	50	theme	streptozotocin-induced	327:348	arg1	diabetes					350:357	streptozotocin-induced diabetes	327:357	streptozotocin-induced diabetes	327:357	METHODS C57BL/6mice with streptozotocin-induced diabetes were fed daily with AE extract or control (CTL) diet at the onset of diabetes mellitus (DM).
28861343	1	51	theme	analysedthe	223:233	arg1	effect					235:240	analysedthe effect	223:240	analysedthe effect of Aralia elata (AE) on neurodegeneration in diabetic mice	223:299	AIM To investigate the role of O-GlcNAcylation of nuclear factor-kappa B (NF-κB) in retinal ganglion cell (RGC) death and analysedthe effect of Aralia elata (AE) on neurodegeneration in diabetic mice.
28861343	6	52	theme	OGT	1139:1141	arg1	levels					1101:1106	Expression levels	1090:1106	Expression levels of protein O-GlcNAcylation and OGT	1090:1141	Expression levels of protein O-GlcNAcylation and OGT were increased in diabetic retinas (P<0.0001 vs CTL), and the level of O-GlcNAcylation of the NF-κB p65 subunit was higher in diabetic retinas than in controls (P<0.0001 vs CTL).
28861343	3	53	theme	streptozotocin	482:495	arg1	injection					469:477	injection	469:477	injection of streptozotocin or saline	469:505	Two months after injection of streptozotocin or saline, the degree of cell death and the expression of O-GlcNAc transferase (OGT), N-acetyl-b-D-glucosaminidase (OGA), O-GlcNAcylated proteins, and O-GlcNAcylation of NF-κB were examined.
28861343	8	54	theme	NF-κB	1477:1481	arg1	O-GlcNAcylation					1458:1472	CONCLUSION O-GlcNAcylation	1447:1472	CONCLUSION O-GlcNAcylation of NF-κB	1447:1481	CONCLUSION O-GlcNAcylation of NF-κB is concerned in neuronal degeneration and that AE prevents diabetes-induced RGC apoptosis via downregulation of NF-κB O-GlcNAcylation.
28861343	6	55	theme	O-GlcNAcylation	1119:1133	arg1	levels					1101:1106	Expression levels	1090:1106	Expression levels of protein O-GlcNAcylation and OGT	1090:1141	Expression levels of protein O-GlcNAcylation and OGT were increased in diabetic retinas (P<0.0001 vs CTL), and the level of O-GlcNAcylation of the NF-κB p65 subunit was higher in diabetic retinas than in controls (P<0.0001 vs CTL).
28861343	8	56	theme	diabetes-induced	1542:1557	arg1	apoptosis					1563:1571	diabetes-induced RGC apoptosis	1542:1571	diabetes-induced RGC apoptosis	1542:1571	CONCLUSION O-GlcNAcylation of NF-κB is concerned in neuronal degeneration and that AE prevents diabetes-induced RGC apoptosis via downregulation of NF-κB O-GlcNAcylation.
28861343	5	57	theme	inner	773:777	arg1	thickness					787:795	the inner retinal thickness	769:795	the inner retinal thickness (P<0.001 vs CTL, P<0.01 vs DM)	769:826	The decrease in the inner retinal thickness (P<0.001 vs CTL, P<0.01 vs DM) and increases in RGCs with terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling (P<0.001 vs CTL, P<0.0001 vs DM), glial activation, and active caspase-3 (P<0.0001 vs CTL, P<0.0001 vs DM) were blocked in diabetic retinas of AE extract-fed mice.
28861343	5	58	theme	diabetic	1049:1056	arg1	retinas					1058:1064	diabetic retinas	1049:1064	diabetic retinas of AE extract-fed mice	1049:1087	The decrease in the inner retinal thickness (P<0.001 vs CTL, P<0.01 vs DM) and increases in RGCs with terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling (P<0.001 vs CTL, P<0.0001 vs DM), glial activation, and active caspase-3 (P<0.0001 vs CTL, P<0.0001 vs DM) were blocked in diabetic retinas of AE extract-fed mice.
28861343	3	59	theme	saline	500:505	arg1	injection					469:477	injection	469:477	injection of streptozotocin or saline	469:505	Two months after injection of streptozotocin or saline, the degree of cell death and the expression of O-GlcNAc transferase (OGT), N-acetyl-b-D-glucosaminidase (OGA), O-GlcNAcylated proteins, and O-GlcNAcylation of NF-κB were examined.
28861343	1	60	theme	retinal	185:191	arg1	RGC					208:210	RGC	208:210	RGC	208:210	AIM To investigate the role of O-GlcNAcylation of nuclear factor-kappa B (NF-κB) in retinal ganglion cell (RGC) death and analysedthe effect of Aralia elata (AE) on neurodegeneration in diabetic mice.
28861343	1	60	theme	retinal	185:191	arg1	cell					202:205	retinal ganglion cell	185:205	retinal ganglion cell (RGC) death	185:217	AIM To investigate the role of O-GlcNAcylation of nuclear factor-kappa B (NF-κB) in retinal ganglion cell (RGC) death and analysedthe effect of Aralia elata (AE) on neurodegeneration in diabetic mice.
28861343	6	61	dep	retinas	1170:1176	arg1	CTL					1191:1193	CTL	1191:1193	CTL	1191:1193	Expression levels of protein O-GlcNAcylation and OGT were increased in diabetic retinas (P<0.0001 vs CTL), and the level of O-GlcNAcylation of the NF-κB p65 subunit was higher in diabetic retinas than in controls (P<0.0001 vs CTL).
28861343	6	61	dep	retinas	1170:1176	arg1	P<0.0001					1179:1186	P<0.0001	1179:1186	P<0.0001	1179:1186	Expression levels of protein O-GlcNAcylation and OGT were increased in diabetic retinas (P<0.0001 vs CTL), and the level of O-GlcNAcylation of the NF-κB p65 subunit was higher in diabetic retinas than in controls (P<0.0001 vs CTL).
28861343	5	62	dep	labelling	916:924	arg1	P<0.001					927:933	P<0.001	927:933	P<0.001	927:933	The decrease in the inner retinal thickness (P<0.001 vs CTL, P<0.01 vs DM) and increases in RGCs with terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling (P<0.001 vs CTL, P<0.0001 vs DM), glial activation, and active caspase-3 (P<0.0001 vs CTL, P<0.0001 vs DM) were blocked in diabetic retinas of AE extract-fed mice.
28861343	5	62	dep	labelling	916:924	arg1	DM					955:956	DM	955:956	DM	955:956	The decrease in the inner retinal thickness (P<0.001 vs CTL, P<0.01 vs DM) and increases in RGCs with terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling (P<0.001 vs CTL, P<0.0001 vs DM), glial activation, and active caspase-3 (P<0.0001 vs CTL, P<0.0001 vs DM) were blocked in diabetic retinas of AE extract-fed mice.
28861343	5	62	dep	labelling	916:924	arg1	P<0.0001					943:950	P<0.0001	943:950	P<0.0001	943:950	The decrease in the inner retinal thickness (P<0.001 vs CTL, P<0.01 vs DM) and increases in RGCs with terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling (P<0.001 vs CTL, P<0.0001 vs DM), glial activation, and active caspase-3 (P<0.0001 vs CTL, P<0.0001 vs DM) were blocked in diabetic retinas of AE extract-fed mice.
28861343	5	62	dep	labelling	916:924	arg1	CTL					938:940	CTL	938:940	CTL	938:940	The decrease in the inner retinal thickness (P<0.001 vs CTL, P<0.01 vs DM) and increases in RGCs with terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling (P<0.001 vs CTL, P<0.0001 vs DM), glial activation, and active caspase-3 (P<0.0001 vs CTL, P<0.0001 vs DM) were blocked in diabetic retinas of AE extract-fed mice.
28861343	3	63	theme	death	527:531	arg1	expression					541:550	the expression	537:550	the expression of O-GlcNAc transferase (OGT), N-acetyl-b-D-glucosaminidase (OGA), O-GlcNAcylated proteins, and O-GlcNAcylation of NF-κB	537:671	Two months after injection of streptozotocin or saline, the degree of cell death and the expression of O-GlcNAc transferase (OGT), N-acetyl-b-D-glucosaminidase (OGA), O-GlcNAcylated proteins, and O-GlcNAcylation of NF-κB were examined.
28861343	3	63	theme	death	527:531	arg1	months					456:461	Two months	452:461	Two months after injection of streptozotocin or saline	452:505	Two months after injection of streptozotocin or saline, the degree of cell death and the expression of O-GlcNAc transferase (OGT), N-acetyl-b-D-glucosaminidase (OGA), O-GlcNAcylated proteins, and O-GlcNAcylation of NF-κB were examined.
28861343	3	63	theme	death	527:531	arg1	degree					512:517	the degree	508:517	the degree of cell death	508:531	Two months after injection of streptozotocin or saline, the degree of cell death and the expression of O-GlcNAc transferase (OGT), N-acetyl-b-D-glucosaminidase (OGA), O-GlcNAcylated proteins, and O-GlcNAcylation of NF-κB were examined.
28861343	8	64	theme	NF-κB	1595:1599	arg1	O-GlcNAcylation					1601:1615	NF-κB O-GlcNAcylation	1595:1615	NF-κB O-GlcNAcylation	1595:1615	CONCLUSION O-GlcNAcylation of NF-κB is concerned in neuronal degeneration and that AE prevents diabetes-induced RGC apoptosis via downregulation of NF-κB O-GlcNAcylation.
28861343	1	65	theme	cell	202:205	arg1	death					213:217	retinal ganglion cell (RGC) death	185:217	retinal ganglion cell (RGC) death	185:217	AIM To investigate the role of O-GlcNAcylation of nuclear factor-kappa B (NF-κB) in retinal ganglion cell (RGC) death and analysedthe effect of Aralia elata (AE) on neurodegeneration in diabetic mice.
28861343	6	66	theme	diabetic	1161:1168	arg1	retinas					1170:1176	diabetic retinas	1161:1176	diabetic retinas (P<0.0001 vs CTL)	1161:1194	Expression levels of protein O-GlcNAcylation and OGT were increased in diabetic retinas (P<0.0001 vs CTL), and the level of O-GlcNAcylation of the NF-κB p65 subunit was higher in diabetic retinas than in controls (P<0.0001 vs CTL).
28861343	5	67	theme	dUTP	902:905	arg1	labelling					916:924	terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling	855:924	terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling (P<0.001 vs CTL, P<0.0001 vs DM)	855:957	The decrease in the inner retinal thickness (P<0.001 vs CTL, P<0.01 vs DM) and increases in RGCs with terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling (P<0.001 vs CTL, P<0.0001 vs DM), glial activation, and active caspase-3 (P<0.0001 vs CTL, P<0.0001 vs DM) were blocked in diabetic retinas of AE extract-fed mice.
28861343	5	68	from	decrease	757:764	arg1	thickness					787:795	the inner retinal thickness	769:795	the inner retinal thickness (P<0.001 vs CTL, P<0.01 vs DM)	769:826	The decrease in the inner retinal thickness (P<0.001 vs CTL, P<0.01 vs DM) and increases in RGCs with terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling (P<0.001 vs CTL, P<0.0001 vs DM), glial activation, and active caspase-3 (P<0.0001 vs CTL, P<0.0001 vs DM) were blocked in diabetic retinas of AE extract-fed mice.
28861343	5	68	from	decrease	757:764	arg1	increases					832:840	increases	832:840	increases in RGCs with terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling (P<0.001 vs CTL, P<0.0001 vs DM)	832:957	The decrease in the inner retinal thickness (P<0.001 vs CTL, P<0.01 vs DM) and increases in RGCs with terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling (P<0.001 vs CTL, P<0.0001 vs DM), glial activation, and active caspase-3 (P<0.0001 vs CTL, P<0.0001 vs DM) were blocked in diabetic retinas of AE extract-fed mice.
28861343	6	69	theme	O-GlcNAcylation	1214:1228	arg1	level					1205:1209	the level	1201:1209	the level of O-GlcNAcylation of the NF-κB p65 subunit	1201:1253	Expression levels of protein O-GlcNAcylation and OGT were increased in diabetic retinas (P<0.0001 vs CTL), and the level of O-GlcNAcylation of the NF-κB p65 subunit was higher in diabetic retinas than in controls (P<0.0001 vs CTL).
28861343	6	69	theme	O-GlcNAcylation	1214:1228	arg1	higher					1259:1264	higher	1259:1264	higher	1259:1264	Expression levels of protein O-GlcNAcylation and OGT were increased in diabetic retinas (P<0.0001 vs CTL), and the level of O-GlcNAcylation of the NF-κB p65 subunit was higher in diabetic retinas than in controls (P<0.0001 vs CTL).
28861343	1	70	theme	factor-kappa	159:170	arg1	NF-κB					175:179	NF-κB	175:179	NF-κB	175:179	AIM To investigate the role of O-GlcNAcylation of nuclear factor-kappa B (NF-κB) in retinal ganglion cell (RGC) death and analysedthe effect of Aralia elata (AE) on neurodegeneration in diabetic mice.
28861343	1	70	theme	factor-kappa	159:170	arg1	B					172:172	nuclear factor-kappa B	151:172	nuclear factor-kappa B (NF-κB)	151:180	AIM To investigate the role of O-GlcNAcylation of nuclear factor-kappa B (NF-κB) in retinal ganglion cell (RGC) death and analysedthe effect of Aralia elata (AE) on neurodegeneration in diabetic mice.
28861343	2	71	theme	mellitus	437:444	arg1	onset					419:423	the onset	415:423	the onset of diabetes mellitus (DM)	415:449	METHODS C57BL/6mice with streptozotocin-induced diabetes were fed daily with AE extract or control (CTL) diet at the onset of diabetes mellitus (DM).
28861343	5	72	theme	deoxynucleotidyl	864:879	arg1	labelling					916:924	terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling	855:924	terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling (P<0.001 vs CTL, P<0.0001 vs DM)	855:957	The decrease in the inner retinal thickness (P<0.001 vs CTL, P<0.01 vs DM) and increases in RGCs with terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling (P<0.001 vs CTL, P<0.0001 vs DM), glial activation, and active caspase-3 (P<0.0001 vs CTL, P<0.0001 vs DM) were blocked in diabetic retinas of AE extract-fed mice.
28861343	9	73	theme	new	1650:1652	arg1	object					1654:1659	a new object	1648:1659	a new object for the treatment of DR	1648:1683	Hence, O-GlcNAcylation may be a new object for the treatment of DR, and AE may have therapeutic possibility to prevent diabetes-induced neurodegeneration.
28861343	9	73	theme	new	1650:1652	arg1	O-GlcNAcylation					1625:1639	O-GlcNAcylation	1625:1639	O-GlcNAcylation	1625:1639	Hence, O-GlcNAcylation may be a new object for the treatment of DR, and AE may have therapeutic possibility to prevent diabetes-induced neurodegeneration.
28861343	1	74	from	role	124:127	arg1	death					213:217	retinal ganglion cell (RGC) death	185:217	retinal ganglion cell (RGC) death	185:217	AIM To investigate the role of O-GlcNAcylation of nuclear factor-kappa B (NF-κB) in retinal ganglion cell (RGC) death and analysedthe effect of Aralia elata (AE) on neurodegeneration in diabetic mice.
28861343	1	74	from	role	124:127	arg1	neurodegeneration					266:282	neurodegeneration	266:282	neurodegeneration in diabetic mice	266:299	AIM To investigate the role of O-GlcNAcylation of nuclear factor-kappa B (NF-κB) in retinal ganglion cell (RGC) death and analysedthe effect of Aralia elata (AE) on neurodegeneration in diabetic mice.
28861343	2	75	theme	CTL	402:404	arg1	diet					407:410	control (CTL) diet	393:410	control (CTL) diet	393:410	METHODS C57BL/6mice with streptozotocin-induced diabetes were fed daily with AE extract or control (CTL) diet at the onset of diabetes mellitus (DM).
28861343	2	76	theme	control	393:399	arg1	diet					407:410	control (CTL) diet	393:410	control (CTL) diet	393:410	METHODS C57BL/6mice with streptozotocin-induced diabetes were fed daily with AE extract or control (CTL) diet at the onset of diabetes mellitus (DM).
28861343	8	77	theme	neuronal	1499:1506	arg1	degeneration					1508:1519	neuronal degeneration	1499:1519	neuronal degeneration	1499:1519	CONCLUSION O-GlcNAcylation of NF-κB is concerned in neuronal degeneration and that AE prevents diabetes-induced RGC apoptosis via downregulation of NF-κB O-GlcNAcylation.
28861343	9	78	theme	DR	1682:1683	arg1	treatment					1669:1677	the treatment	1665:1677	the treatment of DR	1665:1683	Hence, O-GlcNAcylation may be a new object for the treatment of DR, and AE may have therapeutic possibility to prevent diabetes-induced neurodegeneration.
28861343	3	79	theme	transferase	564:574	arg1	expression					541:550	the expression	537:550	the expression of O-GlcNAc transferase (OGT), N-acetyl-b-D-glucosaminidase (OGA), O-GlcNAcylated proteins, and O-GlcNAcylation of NF-κB	537:671	Two months after injection of streptozotocin or saline, the degree of cell death and the expression of O-GlcNAc transferase (OGT), N-acetyl-b-D-glucosaminidase (OGA), O-GlcNAcylated proteins, and O-GlcNAcylation of NF-κB were examined.
28861343	3	79	theme	transferase	564:574	arg1	months					456:461	Two months	452:461	Two months after injection of streptozotocin or saline	452:505	Two months after injection of streptozotocin or saline, the degree of cell death and the expression of O-GlcNAc transferase (OGT), N-acetyl-b-D-glucosaminidase (OGA), O-GlcNAcylated proteins, and O-GlcNAcylation of NF-κB were examined.
28861343	3	79	theme	transferase	564:574	arg1	degree					512:517	the degree	508:517	the degree of cell death	508:531	Two months after injection of streptozotocin or saline, the degree of cell death and the expression of O-GlcNAc transferase (OGT), N-acetyl-b-D-glucosaminidase (OGA), O-GlcNAcylated proteins, and O-GlcNAcylation of NF-κB were examined.
28861343	6	80	theme	p65	1243:1245	arg1	subunit					1247:1253	the NF-κB p65 subunit	1233:1253	the NF-κB p65 subunit	1233:1253	Expression levels of protein O-GlcNAcylation and OGT were increased in diabetic retinas (P<0.0001 vs CTL), and the level of O-GlcNAcylation of the NF-κB p65 subunit was higher in diabetic retinas than in controls (P<0.0001 vs CTL).
28861343	4	81	theme	mice	747:750	arg1	status					728:733	the metabolic status	714:733	the metabolic status of diabetic mice	714:750	RESULTS AE did not affect the metabolic status of diabetic mice.
28861343	2	82	theme	METHODS	302:308	arg1	C57BL/6mice					310:320	METHODS C57BL/6mice	302:320	METHODS C57BL/6mice with streptozotocin-induced diabetes	302:357	METHODS C57BL/6mice with streptozotocin-induced diabetes were fed daily with AE extract or control (CTL) diet at the onset of diabetes mellitus (DM).
28861343	1	83	theme	diabetic	287:294	arg1	mice					296:299	diabetic mice	287:299	diabetic mice	287:299	AIM To investigate the role of O-GlcNAcylation of nuclear factor-kappa B (NF-κB) in retinal ganglion cell (RGC) death and analysedthe effect of Aralia elata (AE) on neurodegeneration in diabetic mice.
28861343	8	84	gly	O-GlcNAcylation	1458:1472	arg1	degeneration					1508:1519	neuronal degeneration	1499:1519	neuronal degeneration	1499:1519	CONCLUSION O-GlcNAcylation of NF-κB is concerned in neuronal degeneration and that AE prevents diabetes-induced RGC apoptosis via downregulation of NF-κB O-GlcNAcylation.
28861343	6	85	dep	controls	1294:1301	arg1	CTL					1316:1318	CTL	1316:1318	CTL	1316:1318	Expression levels of protein O-GlcNAcylation and OGT were increased in diabetic retinas (P<0.0001 vs CTL), and the level of O-GlcNAcylation of the NF-κB p65 subunit was higher in diabetic retinas than in controls (P<0.0001 vs CTL).
28861343	6	85	dep	controls	1294:1301	arg1	P<0.0001					1304:1311	P<0.0001	1304:1311	P<0.0001	1304:1311	Expression levels of protein O-GlcNAcylation and OGT were increased in diabetic retinas (P<0.0001 vs CTL), and the level of O-GlcNAcylation of the NF-κB p65 subunit was higher in diabetic retinas than in controls (P<0.0001 vs CTL).
28861343	5	86	theme	mice	1084:1087	arg1	retinas					1058:1064	diabetic retinas	1049:1064	diabetic retinas of AE extract-fed mice	1049:1087	The decrease in the inner retinal thickness (P<0.001 vs CTL, P<0.01 vs DM) and increases in RGCs with terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling (P<0.001 vs CTL, P<0.0001 vs DM), glial activation, and active caspase-3 (P<0.0001 vs CTL, P<0.0001 vs DM) were blocked in diabetic retinas of AE extract-fed mice.
28861343	7	87	theme	AE	1322:1323	arg1	extract					1325:1331	AE extract	1322:1331	AE extract	1322:1331	AE extract downregulated O-GlcNAcylation of NF-κB and prevented neurodegeneration induced by hyperglycemia (P<0.0001 vs DM).
28861343	5	88	theme	end	912:914	arg1	labelling					916:924	terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling	855:924	terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling (P<0.001 vs CTL, P<0.0001 vs DM)	855:957	The decrease in the inner retinal thickness (P<0.001 vs CTL, P<0.01 vs DM) and increases in RGCs with terminal deoxynucleotidyl transferase-mediated dUTP nick end labelling (P<0.001 vs CTL, P<0.0001 vs DM), glial activation, and active caspase-3 (P<0.0001 vs CTL, P<0.0001 vs DM) were blocked in diabetic retinas of AE extract-fed mice.
28861343	9	89	theme	therapeutic	1702:1712	arg1	possibility					1714:1724	therapeutic possibility	1702:1724	therapeutic possibility	1702:1724	Hence, O-GlcNAcylation may be a new object for the treatment of DR, and AE may have therapeutic possibility to prevent diabetes-induced neurodegeneration.
28861343	8	90	theme	CONCLUSION	1447:1456	arg1	O-GlcNAcylation					1458:1472	CONCLUSION O-GlcNAcylation	1447:1472	CONCLUSION O-GlcNAcylation of NF-κB	1447:1481	CONCLUSION O-GlcNAcylation of NF-κB is concerned in neuronal degeneration and that AE prevents diabetes-induced RGC apoptosis via downregulation of NF-κB O-GlcNAcylation.
28861343	3	91	theme	O-GlcNAcylated	619:632	arg1	proteins					634:641	O-GlcNAcylated proteins	619:641	O-GlcNAcylated proteins	619:641	Two months after injection of streptozotocin or saline, the degree of cell death and the expression of O-GlcNAc transferase (OGT), N-acetyl-b-D-glucosaminidase (OGA), O-GlcNAcylated proteins, and O-GlcNAcylation of NF-κB were examined.
28861343	4	92	theme	metabolic	718:726	arg1	status					728:733	the metabolic status	714:733	the metabolic status of diabetic mice	714:750	RESULTS AE did not affect the metabolic status of diabetic mice.
27454154	0	0	theme	Chain	104:108	arg1	Reaction					110:117	Proximity Ligation Polymerase Chain Reaction	74:117	Proximity Ligation Polymerase Chain Reaction	74:117	Glyco-seek: Ultrasensitive Detection of Protein-Specific Glycosylation by Proximity Ligation Polymerase Chain Reaction.
27454154	4	1	from	attomoles	582:590	arg1	lysates					631:637	cell lysates	626:637	cell lysates	626:637	We show that Glyco-seek detects attomoles of glycoproteins of interest from cell lysates, with sensitivity several orders of magnitude higher than that of current techniques.
27454154	5	2	theme	factor	822:827	arg1	status					782:787	the O-GlcNAcylation status	762:787	the O-GlcNAcylation status of a low-abundance transcription factor from cell lysates	762:845	We used the method to directly assay the O-GlcNAcylation status of a low-abundance transcription factor from cell lysates without need for isolation or enrichment.
27454154	0	3	theme	Polymerase	93:102	arg1	Reaction					110:117	Proximity Ligation Polymerase Chain Reaction	74:117	Proximity Ligation Polymerase Chain Reaction	74:117	Glyco-seek: Ultrasensitive Detection of Protein-Specific Glycosylation by Proximity Ligation Polymerase Chain Reaction.
27454154	1	4	theme	Glyco-seek	179:188	arg1	"					189:189	Glyco-seek"	179:189	Glyco-seek"	179:189	We report a non-destructive biochemical technique, termed "Glyco-seek", for analysis of O-GlcNAcylated proteins.
27454154	3	5	theme	glycan-specific	407:421	arg1	assay					423:427	Our glycan-specific assay	403:427	Our glycan-specific assay	403:427	Our glycan-specific assay can be paired with traditional proximity ligation assays to simultaneously determine the change in total protein levels.
27454154	2	6	theme	chain	326:330	arg1	reaction					332:339	quantitative polymerase chain reaction	302:339	quantitative polymerase chain reaction	302:339	Glyco-seek combines chemoenzymatic labeling, proximity ligation, and quantitative polymerase chain reaction to detect O-GlcNAcylated proteins with ultrahigh sensitivity.
27454154	5	7	used	used	728:731	arg2	We					725:726	We	725:726	We	725:726	We used the method to directly assay the O-GlcNAcylation status of a low-abundance transcription factor from cell lysates without need for isolation or enrichment.
27454154	2	8	theme	polymerase	315:324	arg1	reaction					332:339	quantitative polymerase chain reaction	302:339	quantitative polymerase chain reaction	302:339	Glyco-seek combines chemoenzymatic labeling, proximity ligation, and quantitative polymerase chain reaction to detect O-GlcNAcylated proteins with ultrahigh sensitivity.
27454154	4	9	theme	several	657:663	arg1	orders					665:670	several orders	657:670	several orders of magnitude	657:683	We show that Glyco-seek detects attomoles of glycoproteins of interest from cell lysates, with sensitivity several orders of magnitude higher than that of current techniques.
27454154	5	10	theme	transcription	808:820	arg1	factor					822:827	a low-abundance transcription factor	792:827	a low-abundance transcription factor	792:827	We used the method to directly assay the O-GlcNAcylation status of a low-abundance transcription factor from cell lysates without need for isolation or enrichment.
27454154	3	11	theme	protein	534:540	arg1	levels					542:547	total protein levels	528:547	total protein levels	528:547	Our glycan-specific assay can be paired with traditional proximity ligation assays to simultaneously determine the change in total protein levels.
27454154	2	12	theme	quantitative	302:313	arg1	reaction					332:339	quantitative polymerase chain reaction	302:339	quantitative polymerase chain reaction	302:339	Glyco-seek combines chemoenzymatic labeling, proximity ligation, and quantitative polymerase chain reaction to detect O-GlcNAcylated proteins with ultrahigh sensitivity.
27454154	3	13	theme	proximity	460:468	arg1	assays					479:484	traditional proximity ligation assays	448:484	traditional proximity ligation assays	448:484	Our glycan-specific assay can be paired with traditional proximity ligation assays to simultaneously determine the change in total protein levels.
27454154	3	14	theme	ligation	470:477	arg1	assays					479:484	traditional proximity ligation assays	448:484	traditional proximity ligation assays	448:484	Our glycan-specific assay can be paired with traditional proximity ligation assays to simultaneously determine the change in total protein levels.
27454154	2	15	theme	O-GlcNAcylated	351:364	arg1	proteins					366:373	O-GlcNAcylated proteins	351:373	O-GlcNAcylated proteins with ultrahigh sensitivity	351:400	Glyco-seek combines chemoenzymatic labeling, proximity ligation, and quantitative polymerase chain reaction to detect O-GlcNAcylated proteins with ultrahigh sensitivity.
27454154	4	16	from	lysates	631:637	arg1	glycoproteins					595:607	glycoproteins	595:607	glycoproteins of interest from cell lysates	595:637	We show that Glyco-seek detects attomoles of glycoproteins of interest from cell lysates, with sensitivity several orders of magnitude higher than that of current techniques.
27454154	4	16	from	lysates	631:637	arg1	attomoles					582:590	attomoles	582:590	attomoles of glycoproteins of interest from cell lysates	582:637	We show that Glyco-seek detects attomoles of glycoproteins of interest from cell lysates, with sensitivity several orders of magnitude higher than that of current techniques.
27454154	4	17	theme	cell	626:629	arg1	lysates					631:637	cell lysates	626:637	cell lysates	626:637	We show that Glyco-seek detects attomoles of glycoproteins of interest from cell lysates, with sensitivity several orders of magnitude higher than that of current techniques.
27454154	3	18	with	paired	436:441	arg1	assays					479:484	traditional proximity ligation assays	448:484	traditional proximity ligation assays	448:484	Our glycan-specific assay can be paired with traditional proximity ligation assays to simultaneously determine the change in total protein levels.
27454154	3	19	theme	total	528:532	arg1	levels					542:547	total protein levels	528:547	total protein levels	528:547	Our glycan-specific assay can be paired with traditional proximity ligation assays to simultaneously determine the change in total protein levels.
27454154	0	20	theme	Ultrasensitive	12:25	arg1	Detection					27:35	Ultrasensitive Detection	12:35	Ultrasensitive Detection of Protein-Specific Glycosylation by Proximity Ligation Polymerase Chain Reaction	12:117	Glyco-seek: Ultrasensitive Detection of Protein-Specific Glycosylation by Proximity Ligation Polymerase Chain Reaction.
27454154	5	21	theme	O-GlcNAcylation	766:780	arg1	status					782:787	the O-GlcNAcylation status	762:787	the O-GlcNAcylation status of a low-abundance transcription factor from cell lysates	762:845	We used the method to directly assay the O-GlcNAcylation status of a low-abundance transcription factor from cell lysates without need for isolation or enrichment.
27454154	1	22	theme	O-GlcNAcylated	208:221	arg1	proteins					223:230	O-GlcNAcylated proteins	208:230	O-GlcNAcylated proteins	208:230	We report a non-destructive biochemical technique, termed "Glyco-seek", for analysis of O-GlcNAcylated proteins.
27454154	0	23	theme	Protein-Specific	40:55	arg1	Glycosylation					57:69	Protein-Specific Glycosylation	40:69	Protein-Specific Glycosylation	40:69	Glyco-seek: Ultrasensitive Detection of Protein-Specific Glycosylation by Proximity Ligation Polymerase Chain Reaction.
27454154	2	24	theme	ultrahigh	380:388	arg1	sensitivity					390:400	ultrahigh sensitivity	380:400	ultrahigh sensitivity	380:400	Glyco-seek combines chemoenzymatic labeling, proximity ligation, and quantitative polymerase chain reaction to detect O-GlcNAcylated proteins with ultrahigh sensitivity.
27454154	2	25	with	proteins	366:373	arg1	sensitivity					390:400	ultrahigh sensitivity	380:400	ultrahigh sensitivity	380:400	Glyco-seek combines chemoenzymatic labeling, proximity ligation, and quantitative polymerase chain reaction to detect O-GlcNAcylated proteins with ultrahigh sensitivity.
27454154	1	26	theme	proteins	223:230	arg1	analysis					196:203	analysis	196:203	analysis of O-GlcNAcylated proteins	196:230	We report a non-destructive biochemical technique, termed "Glyco-seek", for analysis of O-GlcNAcylated proteins.
27454154	4	27	theme	glycoproteins	595:607	arg1	attomoles					582:590	attomoles	582:590	attomoles of glycoproteins of interest from cell lysates	582:637	We show that Glyco-seek detects attomoles of glycoproteins of interest from cell lysates, with sensitivity several orders of magnitude higher than that of current techniques.
27454154	5	28	theme	low-abundance	794:806	arg1	factor					822:827	a low-abundance transcription factor	792:827	a low-abundance transcription factor	792:827	We used the method to directly assay the O-GlcNAcylation status of a low-abundance transcription factor from cell lysates without need for isolation or enrichment.
27454154	2	29	theme	chemoenzymatic	253:266	arg1	labeling					268:275	chemoenzymatic labeling	253:275	chemoenzymatic labeling	253:275	Glyco-seek combines chemoenzymatic labeling, proximity ligation, and quantitative polymerase chain reaction to detect O-GlcNAcylated proteins with ultrahigh sensitivity.
27454154	3	30	from	change	518:523	arg1	levels					542:547	total protein levels	528:547	total protein levels	528:547	Our glycan-specific assay can be paired with traditional proximity ligation assays to simultaneously determine the change in total protein levels.
27454154	4	31	theme	current	705:711	arg1	techniques					713:722	current techniques	705:722	current techniques	705:722	We show that Glyco-seek detects attomoles of glycoproteins of interest from cell lysates, with sensitivity several orders of magnitude higher than that of current techniques.
27454154	3	32	theme	traditional	448:458	arg1	assays					479:484	traditional proximity ligation assays	448:484	traditional proximity ligation assays	448:484	Our glycan-specific assay can be paired with traditional proximity ligation assays to simultaneously determine the change in total protein levels.
27454154	5	33	theme	cell	834:837	arg1	lysates					839:845	cell lysates	834:845	cell lysates	834:845	We used the method to directly assay the O-GlcNAcylation status of a low-abundance transcription factor from cell lysates without need for isolation or enrichment.
27454154	0	34	theme	Glycosylation	57:69	arg1	Detection					27:35	Ultrasensitive Detection	12:35	Ultrasensitive Detection of Protein-Specific Glycosylation by Proximity Ligation Polymerase Chain Reaction	12:117	Glyco-seek: Ultrasensitive Detection of Protein-Specific Glycosylation by Proximity Ligation Polymerase Chain Reaction.
27454154	4	35	theme	interest	612:619	arg1	glycoproteins					595:607	glycoproteins	595:607	glycoproteins of interest from cell lysates	595:637	We show that Glyco-seek detects attomoles of glycoproteins of interest from cell lysates, with sensitivity several orders of magnitude higher than that of current techniques.
27454154	5	36	from	lysates	839:845	arg1	status					782:787	the O-GlcNAcylation status	762:787	the O-GlcNAcylation status of a low-abundance transcription factor from cell lysates	762:845	We used the method to directly assay the O-GlcNAcylation status of a low-abundance transcription factor from cell lysates without need for isolation or enrichment.
27454154	1	37	theme	non-destructive	132:146	arg1	technique					160:168	a non-destructive biochemical technique	130:168	a non-destructive biochemical technique	130:168	We report a non-destructive biochemical technique, termed "Glyco-seek", for analysis of O-GlcNAcylated proteins.
27454154	0	38	dep	Detection	27:35	arg1	Glyco-seek					0:9	Glyco-seek	0:9	Glyco-seek	0:9	Glyco-seek: Ultrasensitive Detection of Protein-Specific Glycosylation by Proximity Ligation Polymerase Chain Reaction.
27454154	1	39	theme	biochemical	148:158	arg1	technique					160:168	a non-destructive biochemical technique	130:168	a non-destructive biochemical technique	130:168	We report a non-destructive biochemical technique, termed "Glyco-seek", for analysis of O-GlcNAcylated proteins.
27454154	4	40	theme	magnitude	675:683	arg1	orders					665:670	several orders	657:670	several orders of magnitude	657:683	We show that Glyco-seek detects attomoles of glycoproteins of interest from cell lysates, with sensitivity several orders of magnitude higher than that of current techniques.
27454154	0	41	theme	Ligation	84:91	arg1	Reaction					110:117	Proximity Ligation Polymerase Chain Reaction	74:117	Proximity Ligation Polymerase Chain Reaction	74:117	Glyco-seek: Ultrasensitive Detection of Protein-Specific Glycosylation by Proximity Ligation Polymerase Chain Reaction.
27454154	2	42	theme	proximity	278:286	arg1	ligation					288:295	proximity ligation	278:295	proximity ligation	278:295	Glyco-seek combines chemoenzymatic labeling, proximity ligation, and quantitative polymerase chain reaction to detect O-GlcNAcylated proteins with ultrahigh sensitivity.
27454154	4	43	gly	glycoproteins	595:607	arg1	glycoproteins					595:607	glycoproteins	595:607	glycoproteins of interest from cell lysates	595:637	We show that Glyco-seek detects attomoles of glycoproteins of interest from cell lysates, with sensitivity several orders of magnitude higher than that of current techniques.
27454154	0	44	theme	Proximity	74:82	arg1	Reaction					110:117	Proximity Ligation Polymerase Chain Reaction	74:117	Proximity Ligation Polymerase Chain Reaction	74:117	Glyco-seek: Ultrasensitive Detection of Protein-Specific Glycosylation by Proximity Ligation Polymerase Chain Reaction.
27454154	4	45	theme	higher	685:690	arg1	sensitivity					645:655	sensitivity	645:655	sensitivity several orders of magnitude higher than that of current techniques	645:722	We show that Glyco-seek detects attomoles of glycoproteins of interest from cell lysates, with sensitivity several orders of magnitude higher than that of current techniques.
28571750	5	0	theme	cell	940:943	arg1	lines					945:949	different cancer cell lines	923:949	different cancer cell lines	923:949	Herein we demonstrated the utility of an O-GlcNAcylated peptide array to examine O-GlcNAcase (OGA) activity and substrate specificity of both purified protein as well cell lysates of different cancer cell lines.
28571750	4	1	from	demand	613:618	arg1	cancer					732:737	cancer	732:737	cancer	732:737	There is a strong demand for efficient analytical techniques to better detect and investigate this abundant modification and its role in cancer.
28571750	1	2	theme	nuclear	250:256	arg1	proteins					274:281	nuclear and cytoplasmic proteins	250:281	nuclear and cytoplasmic proteins	250:281	O-GlcNAcylation is a post-translational modification resulting from the addition of an N-acetylglucosamine moiety to the hydroxyl groups of serine and threonine residues of nuclear and cytoplasmic proteins.
28571750	0	3	theme	peptide	57:63	arg1	microarray					65:74	a peptide microarray	55:74	a peptide microarray	55:74	Measuring O-GlcNAc cleavage by OGA and cell lysates on a peptide microarray.
28571750	5	4	theme	lines	945:949	arg1	specificity					862:872	substrate specificity	852:872	substrate specificity of both purified protein	852:897	Herein we demonstrated the utility of an O-GlcNAcylated peptide array to examine O-GlcNAcase (OGA) activity and substrate specificity of both purified protein as well cell lysates of different cancer cell lines.
28571750	5	4	theme	lines	945:949	arg1	activity					839:846	O-GlcNAcase (OGA) activity	821:846	O-GlcNAcase (OGA) activity	821:846	Herein we demonstrated the utility of an O-GlcNAcylated peptide array to examine O-GlcNAcase (OGA) activity and substrate specificity of both purified protein as well cell lysates of different cancer cell lines.
28571750	5	4	theme	lines	945:949	arg1	lysates					912:918	well cell lysates	902:918	well cell lysates of different cancer cell lines	902:949	Herein we demonstrated the utility of an O-GlcNAcylated peptide array to examine O-GlcNAcase (OGA) activity and substrate specificity of both purified protein as well cell lysates of different cancer cell lines.
28571750	7	5	from	useful	1214:1219	arg1	research					1231:1238	cancer research	1224:1238	cancer research	1224:1238	This suggests that the tool may be useful in cancer research and biomarker development.
28571750	7	5	from	useful	1214:1219	arg1	development					1254:1264	biomarker development	1244:1264	biomarker development	1244:1264	This suggests that the tool may be useful in cancer research and biomarker development.
28571750	7	6	theme	cancer	1224:1229	arg1	research					1231:1238	cancer research	1224:1238	cancer research	1224:1238	This suggests that the tool may be useful in cancer research and biomarker development.
28571750	1	7	theme	cytoplasmic	262:272	arg1	proteins					274:281	nuclear and cytoplasmic proteins	250:281	nuclear and cytoplasmic proteins	250:281	O-GlcNAcylation is a post-translational modification resulting from the addition of an N-acetylglucosamine moiety to the hydroxyl groups of serine and threonine residues of nuclear and cytoplasmic proteins.
28571750	5	8	theme	peptide	796:802	arg1	array					804:808	an O-GlcNAcylated peptide array	778:808	an O-GlcNAcylated peptide array	778:808	Herein we demonstrated the utility of an O-GlcNAcylated peptide array to examine O-GlcNAcase (OGA) activity and substrate specificity of both purified protein as well cell lysates of different cancer cell lines.
28571750	6	9	dep	thiamet	1053:1059	arg1	G.					1061:1062	G.	1061:1062	G.	1061:1062	Using this microarray, we clearly observed OGA activity and also inhibition thereof by OGA inhibitor thiamet G. Interestingly, different levels of OGA activity were observed of lysates derived from different cancer cell lines.
28571750	4	10	from	role	724:727	arg1	cancer					732:737	cancer	732:737	cancer	732:737	There is a strong demand for efficient analytical techniques to better detect and investigate this abundant modification and its role in cancer.
28571750	1	11	theme	proteins	274:281	arg1	threonine					228:236	threonine	228:236	threonine	228:236	O-GlcNAcylation is a post-translational modification resulting from the addition of an N-acetylglucosamine moiety to the hydroxyl groups of serine and threonine residues of nuclear and cytoplasmic proteins.
28571750	1	11	theme	proteins	274:281	arg1	serine					217:222	serine	217:222	serine	217:222	O-GlcNAcylation is a post-translational modification resulting from the addition of an N-acetylglucosamine moiety to the hydroxyl groups of serine and threonine residues of nuclear and cytoplasmic proteins.
28571750	5	12	theme	O-GlcNAcylated	781:794	arg1	array					804:808	an O-GlcNAcylated peptide array	778:808	an O-GlcNAcylated peptide array	778:808	Herein we demonstrated the utility of an O-GlcNAcylated peptide array to examine O-GlcNAcase (OGA) activity and substrate specificity of both purified protein as well cell lysates of different cancer cell lines.
28571750	5	13	theme	purified	882:889	arg1	protein					891:897	both purified protein	877:897	both purified protein	877:897	Herein we demonstrated the utility of an O-GlcNAcylated peptide array to examine O-GlcNAcase (OGA) activity and substrate specificity of both purified protein as well cell lysates of different cancer cell lines.
28571750	1	14	theme	N-acetylglucosamine	164:182	arg1	moiety					184:189	an N-acetylglucosamine moiety	161:189	an N-acetylglucosamine moiety	161:189	O-GlcNAcylation is a post-translational modification resulting from the addition of an N-acetylglucosamine moiety to the hydroxyl groups of serine and threonine residues of nuclear and cytoplasmic proteins.
28571750	4	15	theme	efficient	624:632	arg1	techniques					645:654	efficient analytical techniques	624:654	efficient analytical techniques to better detect and investigate this abundant modification	624:714	There is a strong demand for efficient analytical techniques to better detect and investigate this abundant modification and its role in cancer.
28571750	6	16	theme	cancer	1160:1165	arg1	lines					1172:1176	different cancer cell lines	1150:1176	different cancer cell lines	1150:1176	Using this microarray, we clearly observed OGA activity and also inhibition thereof by OGA inhibitor thiamet G. Interestingly, different levels of OGA activity were observed of lysates derived from different cancer cell lines.
28571750	3	17	theme	tumor	577:581	arg1	metastasis					583:592	tumor metastasis	577:592	tumor metastasis	577:592	Dysregulation of O-GlcNAcylation affects cell signaling, transcriptional regulation, cell cycle control and can e.g. lead to tumorigenesis and tumor metastasis.
28571750	1	18	theme	moiety	184:189	arg1	addition					149:156	the addition	145:156	the addition of an N-acetylglucosamine moiety to the hydroxyl groups of serine and threonine residues of nuclear and cytoplasmic proteins	145:281	O-GlcNAcylation is a post-translational modification resulting from the addition of an N-acetylglucosamine moiety to the hydroxyl groups of serine and threonine residues of nuclear and cytoplasmic proteins.
28571750	0	19	theme	O-GlcNAc	10:17	arg1	cleavage					19:26	O-GlcNAc cleavage	10:26	O-GlcNAc cleavage by OGA and cell lysates	10:50	Measuring O-GlcNAc cleavage by OGA and cell lysates on a peptide microarray.
28571750	5	20	theme	O-GlcNAcase	821:831	arg1	specificity					862:872	substrate specificity	852:872	substrate specificity of both purified protein	852:897	Herein we demonstrated the utility of an O-GlcNAcylated peptide array to examine O-GlcNAcase (OGA) activity and substrate specificity of both purified protein as well cell lysates of different cancer cell lines.
28571750	5	20	theme	O-GlcNAcase	821:831	arg1	activity					839:846	O-GlcNAcase (OGA) activity	821:846	O-GlcNAcase (OGA) activity	821:846	Herein we demonstrated the utility of an O-GlcNAcylated peptide array to examine O-GlcNAcase (OGA) activity and substrate specificity of both purified protein as well cell lysates of different cancer cell lines.
28571750	5	20	theme	O-GlcNAcase	821:831	arg1	lysates					912:918	well cell lysates	902:918	well cell lysates of different cancer cell lines	902:949	Herein we demonstrated the utility of an O-GlcNAcylated peptide array to examine O-GlcNAcase (OGA) activity and substrate specificity of both purified protein as well cell lysates of different cancer cell lines.
28571750	7	21	theme	biomarker	1244:1252	arg1	development					1254:1264	biomarker development	1244:1264	biomarker development	1244:1264	This suggests that the tool may be useful in cancer research and biomarker development.
28571750	6	22	theme	activity	1103:1110	arg1	levels					1089:1094	different levels	1079:1094	different levels of OGA activity	1079:1110	Using this microarray, we clearly observed OGA activity and also inhibition thereof by OGA inhibitor thiamet G. Interestingly, different levels of OGA activity were observed of lysates derived from different cancer cell lines.
28571750	5	23	theme	substrate	852:860	arg1	lysates					912:918	well cell lysates	902:918	well cell lysates of different cancer cell lines	902:949	Herein we demonstrated the utility of an O-GlcNAcylated peptide array to examine O-GlcNAcase (OGA) activity and substrate specificity of both purified protein as well cell lysates of different cancer cell lines.
28571750	5	23	theme	substrate	852:860	arg1	activity					839:846	O-GlcNAcase (OGA) activity	821:846	O-GlcNAcase (OGA) activity	821:846	Herein we demonstrated the utility of an O-GlcNAcylated peptide array to examine O-GlcNAcase (OGA) activity and substrate specificity of both purified protein as well cell lysates of different cancer cell lines.
28571750	5	23	theme	substrate	852:860	arg1	specificity					862:872	substrate specificity	852:872	substrate specificity of both purified protein	852:897	Herein we demonstrated the utility of an O-GlcNAcylated peptide array to examine O-GlcNAcase (OGA) activity and substrate specificity of both purified protein as well cell lysates of different cancer cell lines.
28571750	5	24	theme	well	902:905	arg1	specificity					862:872	substrate specificity	852:872	substrate specificity of both purified protein	852:897	Herein we demonstrated the utility of an O-GlcNAcylated peptide array to examine O-GlcNAcase (OGA) activity and substrate specificity of both purified protein as well cell lysates of different cancer cell lines.
28571750	5	24	theme	well	902:905	arg1	activity					839:846	O-GlcNAcase (OGA) activity	821:846	O-GlcNAcase (OGA) activity	821:846	Herein we demonstrated the utility of an O-GlcNAcylated peptide array to examine O-GlcNAcase (OGA) activity and substrate specificity of both purified protein as well cell lysates of different cancer cell lines.
28571750	5	24	theme	well	902:905	arg1	lysates					912:918	well cell lysates	902:918	well cell lysates of different cancer cell lines	902:949	Herein we demonstrated the utility of an O-GlcNAcylated peptide array to examine O-GlcNAcase (OGA) activity and substrate specificity of both purified protein as well cell lysates of different cancer cell lines.
28571750	6	25	theme	OGA	1039:1041	arg1	thiamet					1053:1059	OGA inhibitor thiamet G.	1039:1062	OGA inhibitor thiamet G.	1039:1062	Using this microarray, we clearly observed OGA activity and also inhibition thereof by OGA inhibitor thiamet G. Interestingly, different levels of OGA activity were observed of lysates derived from different cancer cell lines.
28571750	3	26	theme	cell	475:478	arg1	signaling					480:488	cell signaling	475:488	cell signaling	475:488	Dysregulation of O-GlcNAcylation affects cell signaling, transcriptional regulation, cell cycle control and can e.g. lead to tumorigenesis and tumor metastasis.
28571750	3	26	theme	cell	475:478	arg1	regulation					507:516	transcriptional regulation	491:516	transcriptional regulation	491:516	Dysregulation of O-GlcNAcylation affects cell signaling, transcriptional regulation, cell cycle control and can e.g. lead to tumorigenesis and tumor metastasis.
28571750	3	26	theme	cell	475:478	arg1	control					530:536	cell cycle control	519:536	cell cycle control	519:536	Dysregulation of O-GlcNAcylation affects cell signaling, transcriptional regulation, cell cycle control and can e.g. lead to tumorigenesis and tumor metastasis.
28571750	5	27	theme	protein	891:897	arg1	lysates					912:918	well cell lysates	902:918	well cell lysates of different cancer cell lines	902:949	Herein we demonstrated the utility of an O-GlcNAcylated peptide array to examine O-GlcNAcase (OGA) activity and substrate specificity of both purified protein as well cell lysates of different cancer cell lines.
28571750	5	27	theme	protein	891:897	arg1	activity					839:846	O-GlcNAcase (OGA) activity	821:846	O-GlcNAcase (OGA) activity	821:846	Herein we demonstrated the utility of an O-GlcNAcylated peptide array to examine O-GlcNAcase (OGA) activity and substrate specificity of both purified protein as well cell lysates of different cancer cell lines.
28571750	5	27	theme	protein	891:897	arg1	specificity					862:872	substrate specificity	852:872	substrate specificity of both purified protein	852:897	Herein we demonstrated the utility of an O-GlcNAcylated peptide array to examine O-GlcNAcase (OGA) activity and substrate specificity of both purified protein as well cell lysates of different cancer cell lines.
28571750	6	28	theme	different	1079:1087	arg1	levels					1089:1094	different levels	1079:1094	different levels of OGA activity	1079:1110	Using this microarray, we clearly observed OGA activity and also inhibition thereof by OGA inhibitor thiamet G. Interestingly, different levels of OGA activity were observed of lysates derived from different cancer cell lines.
28571750	1	29	theme	hydroxyl	198:205	arg1	groups					207:212	the hydroxyl groups	194:212	the hydroxyl groups of serine and threonine residues of nuclear and cytoplasmic proteins	194:281	O-GlcNAcylation is a post-translational modification resulting from the addition of an N-acetylglucosamine moiety to the hydroxyl groups of serine and threonine residues of nuclear and cytoplasmic proteins.
28571750	1	29	theme	hydroxyl	198:205	arg1	threonine					228:236	threonine	228:236	threonine	228:236	O-GlcNAcylation is a post-translational modification resulting from the addition of an N-acetylglucosamine moiety to the hydroxyl groups of serine and threonine residues of nuclear and cytoplasmic proteins.
28571750	1	29	theme	hydroxyl	198:205	arg1	serine					217:222	serine	217:222	serine	217:222	O-GlcNAcylation is a post-translational modification resulting from the addition of an N-acetylglucosamine moiety to the hydroxyl groups of serine and threonine residues of nuclear and cytoplasmic proteins.
28571750	4	30	theme	strong	606:611	arg1	demand					613:618	a strong demand	604:618	a strong demand for efficient analytical techniques to better detect and investigate this abundant modification	604:714	There is a strong demand for efficient analytical techniques to better detect and investigate this abundant modification and its role in cancer.
28571750	6	31	attach	derived	1137:1143	arg2	lysates					1129:1135	lysates	1129:1135	lysates derived from different cancer cell lines	1129:1176	Using this microarray, we clearly observed OGA activity and also inhibition thereof by OGA inhibitor thiamet G. Interestingly, different levels of OGA activity were observed of lysates derived from different cancer cell lines.
28571750	6	31	attach	derived	1137:1143	arg1	lines					1172:1176	different cancer cell lines	1150:1176	different cancer cell lines	1150:1176	Using this microarray, we clearly observed OGA activity and also inhibition thereof by OGA inhibitor thiamet G. Interestingly, different levels of OGA activity were observed of lysates derived from different cancer cell lines.
28571750	2	32	theme	O-GlcNAcylated	297:310	arg1	proteins					312:319	O-GlcNAcylated proteins	297:319	O-GlcNAcylated proteins	297:319	In addition, O-GlcNAcylated proteins can be phosphorylated, which suggests the possibility for crosstalk between O-GlcNAcylation and phosphorylation.
28571750	3	33	theme	cell	519:522	arg1	signaling					480:488	cell signaling	475:488	cell signaling	475:488	Dysregulation of O-GlcNAcylation affects cell signaling, transcriptional regulation, cell cycle control and can e.g. lead to tumorigenesis and tumor metastasis.
28571750	3	33	theme	cell	519:522	arg1	control					530:536	cell cycle control	519:536	cell cycle control	519:536	Dysregulation of O-GlcNAcylation affects cell signaling, transcriptional regulation, cell cycle control and can e.g. lead to tumorigenesis and tumor metastasis.
28571750	6	34	theme	OGA	995:997	arg1	activity					999:1006	OGA activity	995:1006	OGA activity	995:1006	Using this microarray, we clearly observed OGA activity and also inhibition thereof by OGA inhibitor thiamet G. Interestingly, different levels of OGA activity were observed of lysates derived from different cancer cell lines.
28571750	4	35	theme	abundant	694:701	arg1	modification					703:714	this abundant modification	689:714	this abundant modification	689:714	There is a strong demand for efficient analytical techniques to better detect and investigate this abundant modification and its role in cancer.
28571750	6	36	theme	OGA	1099:1101	arg1	activity					1103:1110	OGA activity	1099:1110	OGA activity	1099:1110	Using this microarray, we clearly observed OGA activity and also inhibition thereof by OGA inhibitor thiamet G. Interestingly, different levels of OGA activity were observed of lysates derived from different cancer cell lines.
28571750	3	37	theme	transcriptional	491:505	arg1	signaling					480:488	cell signaling	475:488	cell signaling	475:488	Dysregulation of O-GlcNAcylation affects cell signaling, transcriptional regulation, cell cycle control and can e.g. lead to tumorigenesis and tumor metastasis.
28571750	3	37	theme	transcriptional	491:505	arg1	regulation					507:516	transcriptional regulation	491:516	transcriptional regulation	491:516	Dysregulation of O-GlcNAcylation affects cell signaling, transcriptional regulation, cell cycle control and can e.g. lead to tumorigenesis and tumor metastasis.
28571750	3	38	theme	O-GlcNAcylation	451:465	arg1	Dysregulation					434:446	Dysregulation	434:446	Dysregulation of O-GlcNAcylation	434:465	Dysregulation of O-GlcNAcylation affects cell signaling, transcriptional regulation, cell cycle control and can e.g. lead to tumorigenesis and tumor metastasis.
28571750	5	39	theme	OGA	834:836	arg1	specificity					862:872	substrate specificity	852:872	substrate specificity of both purified protein	852:897	Herein we demonstrated the utility of an O-GlcNAcylated peptide array to examine O-GlcNAcase (OGA) activity and substrate specificity of both purified protein as well cell lysates of different cancer cell lines.
28571750	5	39	theme	OGA	834:836	arg1	activity					839:846	O-GlcNAcase (OGA) activity	821:846	O-GlcNAcase (OGA) activity	821:846	Herein we demonstrated the utility of an O-GlcNAcylated peptide array to examine O-GlcNAcase (OGA) activity and substrate specificity of both purified protein as well cell lysates of different cancer cell lines.
28571750	5	39	theme	OGA	834:836	arg1	lysates					912:918	well cell lysates	902:918	well cell lysates of different cancer cell lines	902:949	Herein we demonstrated the utility of an O-GlcNAcylated peptide array to examine O-GlcNAcase (OGA) activity and substrate specificity of both purified protein as well cell lysates of different cancer cell lines.
28571750	1	40	theme	serine	217:222	arg1	groups					207:212	the hydroxyl groups	194:212	the hydroxyl groups of serine and threonine residues of nuclear and cytoplasmic proteins	194:281	O-GlcNAcylation is a post-translational modification resulting from the addition of an N-acetylglucosamine moiety to the hydroxyl groups of serine and threonine residues of nuclear and cytoplasmic proteins.
28571750	1	40	theme	serine	217:222	arg1	threonine					228:236	threonine	228:236	threonine	228:236	O-GlcNAcylation is a post-translational modification resulting from the addition of an N-acetylglucosamine moiety to the hydroxyl groups of serine and threonine residues of nuclear and cytoplasmic proteins.
28571750	1	40	theme	serine	217:222	arg1	serine					217:222	serine	217:222	serine	217:222	O-GlcNAcylation is a post-translational modification resulting from the addition of an N-acetylglucosamine moiety to the hydroxyl groups of serine and threonine residues of nuclear and cytoplasmic proteins.
28571750	7	41	from	research	1231:1238	arg1	tool					1202:1205	the tool	1198:1205	the tool	1198:1205	This suggests that the tool may be useful in cancer research and biomarker development.
28571750	7	41	from	research	1231:1238	arg1	useful					1214:1219	useful	1214:1219	useful	1214:1219	This suggests that the tool may be useful in cancer research and biomarker development.
28571750	1	42	theme	post-translational	98:115	arg1	O-GlcNAcylation					77:91	O-GlcNAcylation	77:91	O-GlcNAcylation	77:91	O-GlcNAcylation is a post-translational modification resulting from the addition of an N-acetylglucosamine moiety to the hydroxyl groups of serine and threonine residues of nuclear and cytoplasmic proteins.
28571750	1	42	theme	post-translational	98:115	arg1	modification					117:128	a post-translational modification	96:128	a post-translational modification resulting from the addition of an N-acetylglucosamine moiety to the hydroxyl groups of serine and threonine residues of nuclear and cytoplasmic proteins	96:281	O-GlcNAcylation is a post-translational modification resulting from the addition of an N-acetylglucosamine moiety to the hydroxyl groups of serine and threonine residues of nuclear and cytoplasmic proteins.
28571750	0	43	theme	cell	39:42	arg1	lysates					44:50	cell lysates	39:50	cell lysates	39:50	Measuring O-GlcNAc cleavage by OGA and cell lysates on a peptide microarray.
28571750	6	44	theme	cell	1167:1170	arg1	lines					1172:1176	different cancer cell lines	1150:1176	different cancer cell lines	1150:1176	Using this microarray, we clearly observed OGA activity and also inhibition thereof by OGA inhibitor thiamet G. Interestingly, different levels of OGA activity were observed of lysates derived from different cancer cell lines.
28571750	3	45	theme	cycle	524:528	arg1	signaling					480:488	cell signaling	475:488	cell signaling	475:488	Dysregulation of O-GlcNAcylation affects cell signaling, transcriptional regulation, cell cycle control and can e.g. lead to tumorigenesis and tumor metastasis.
28571750	3	45	theme	cycle	524:528	arg1	control					530:536	cell cycle control	519:536	cell cycle control	519:536	Dysregulation of O-GlcNAcylation affects cell signaling, transcriptional regulation, cell cycle control and can e.g. lead to tumorigenesis and tumor metastasis.
28571750	7	46	from	development	1254:1264	arg1	tool					1202:1205	the tool	1198:1205	the tool	1198:1205	This suggests that the tool may be useful in cancer research and biomarker development.
28571750	7	46	from	development	1254:1264	arg1	useful					1214:1219	useful	1214:1219	useful	1214:1219	This suggests that the tool may be useful in cancer research and biomarker development.
28571750	1	47	dep	serine	217:222	arg1	residues					238:245	residues	238:245	residues	238:245	O-GlcNAcylation is a post-translational modification resulting from the addition of an N-acetylglucosamine moiety to the hydroxyl groups of serine and threonine residues of nuclear and cytoplasmic proteins.
28571750	6	48	theme	different	1150:1158	arg1	lines					1172:1176	different cancer cell lines	1150:1176	different cancer cell lines	1150:1176	Using this microarray, we clearly observed OGA activity and also inhibition thereof by OGA inhibitor thiamet G. Interestingly, different levels of OGA activity were observed of lysates derived from different cancer cell lines.
28571750	1	49	theme	threonine	228:236	arg1	groups					207:212	the hydroxyl groups	194:212	the hydroxyl groups of serine and threonine residues of nuclear and cytoplasmic proteins	194:281	O-GlcNAcylation is a post-translational modification resulting from the addition of an N-acetylglucosamine moiety to the hydroxyl groups of serine and threonine residues of nuclear and cytoplasmic proteins.
28571750	1	49	theme	threonine	228:236	arg1	threonine					228:236	threonine	228:236	threonine	228:236	O-GlcNAcylation is a post-translational modification resulting from the addition of an N-acetylglucosamine moiety to the hydroxyl groups of serine and threonine residues of nuclear and cytoplasmic proteins.
28571750	1	49	theme	threonine	228:236	arg1	serine					217:222	serine	217:222	serine	217:222	O-GlcNAcylation is a post-translational modification resulting from the addition of an N-acetylglucosamine moiety to the hydroxyl groups of serine and threonine residues of nuclear and cytoplasmic proteins.
28571750	5	50	theme	array	804:808	arg1	utility					767:773	the utility	763:773	the utility of an O-GlcNAcylated peptide array to examine O-GlcNAcase (OGA) activity and substrate specificity of both purified protein as well cell lysates of different cancer cell lines	763:949	Herein we demonstrated the utility of an O-GlcNAcylated peptide array to examine O-GlcNAcase (OGA) activity and substrate specificity of both purified protein as well cell lysates of different cancer cell lines.
28571750	4	51	dep	techniques	645:654	arg1	investigate					677:687	investigate	677:687	investigate this abundant modification	677:714	There is a strong demand for efficient analytical techniques to better detect and investigate this abundant modification and its role in cancer.
28571750	4	51	dep	techniques	645:654	arg1	detect					666:671	detect	666:671	detect	666:671	There is a strong demand for efficient analytical techniques to better detect and investigate this abundant modification and its role in cancer.
28571750	5	52	theme	different	923:931	arg1	lines					945:949	different cancer cell lines	923:949	different cancer cell lines	923:949	Herein we demonstrated the utility of an O-GlcNAcylated peptide array to examine O-GlcNAcase (OGA) activity and substrate specificity of both purified protein as well cell lysates of different cancer cell lines.
28571750	5	53	theme	cell	907:910	arg1	specificity					862:872	substrate specificity	852:872	substrate specificity of both purified protein	852:897	Herein we demonstrated the utility of an O-GlcNAcylated peptide array to examine O-GlcNAcase (OGA) activity and substrate specificity of both purified protein as well cell lysates of different cancer cell lines.
28571750	5	53	theme	cell	907:910	arg1	activity					839:846	O-GlcNAcase (OGA) activity	821:846	O-GlcNAcase (OGA) activity	821:846	Herein we demonstrated the utility of an O-GlcNAcylated peptide array to examine O-GlcNAcase (OGA) activity and substrate specificity of both purified protein as well cell lysates of different cancer cell lines.
28571750	5	53	theme	cell	907:910	arg1	lysates					912:918	well cell lysates	902:918	well cell lysates of different cancer cell lines	902:949	Herein we demonstrated the utility of an O-GlcNAcylated peptide array to examine O-GlcNAcase (OGA) activity and substrate specificity of both purified protein as well cell lysates of different cancer cell lines.
28571750	4	54	theme	analytical	634:643	arg1	techniques					645:654	efficient analytical techniques	624:654	efficient analytical techniques to better detect and investigate this abundant modification	624:714	There is a strong demand for efficient analytical techniques to better detect and investigate this abundant modification and its role in cancer.
28571750	5	55	theme	cancer	933:938	arg1	lines					945:949	different cancer cell lines	923:949	different cancer cell lines	923:949	Herein we demonstrated the utility of an O-GlcNAcylated peptide array to examine O-GlcNAcase (OGA) activity and substrate specificity of both purified protein as well cell lysates of different cancer cell lines.
28571750	6	56	theme	inhibitor	1043:1051	arg1	thiamet					1053:1059	OGA inhibitor thiamet G.	1039:1062	OGA inhibitor thiamet G.	1039:1062	Using this microarray, we clearly observed OGA activity and also inhibition thereof by OGA inhibitor thiamet G. Interestingly, different levels of OGA activity were observed of lysates derived from different cancer cell lines.
30002415	5	0	theme	Ang-2	747:751	arg1	mice					768:771	Ang-2 haplodeficient mice	747:771	Ang-2 haplodeficient mice	747:771	The crucial role of retinal Ang-2 in the initiation of vasoregression was verified by crossing NDPK-B deficient with Ang-2 haplodeficient mice.
30002415	4	1	from	importance	488:497	arg1	retinas					528:534	NDPK-B deficient retinas	511:534	NDPK-B deficient retinas	511:534	We therefore investigated the importance of Ang-2 in NDPK-B deficient retinas and characterized the mechanisms of Ang-2 upregulation upon NDPK-B depletion in cultured ECs.
30002415	12	2	theme	vascular	1442:1449	arg1	damage					1451:1456	NDPK-B associated vascular damage	1424:1456	NDPK-B associated vascular damage	1424:1456	Our data provide evidence for a central role of protein O-GlcNAcylation in NDPK-B associated vascular damage and point to the hexosamine pathway as an important target in retinal vasoregression.
30002415	0	3	theme	endothelial	85:95	arg1	damage					97:102	endothelial damage	85:102	endothelial damage	85:102	O-GlcNAcylation of FoxO1 mediates nucleoside diphosphate kinase B deficiency induced endothelial damage.
30002415	12	4	theme	hexosamine	1475:1484	arg1	pathway					1486:1492	the hexosamine pathway	1471:1492	the hexosamine pathway	1471:1492	Our data provide evidence for a central role of protein O-GlcNAcylation in NDPK-B associated vascular damage and point to the hexosamine pathway as an important target in retinal vasoregression.
30002415	5	5	theme	crucial	634:640	arg1	role					642:645	The crucial role	630:645	The crucial role of retinal Ang-2 in the initiation of vasoregression	630:698	The crucial role of retinal Ang-2 in the initiation of vasoregression was verified by crossing NDPK-B deficient with Ang-2 haplodeficient mice.
30002415	1	6	theme	protective	156:165	arg1	factor					167:172	a protective factor	154:172	a protective factor in the retinal vasculature	154:199	Nucleoside diphosphate kinase B (NDPK-B) acts as a protective factor in the retinal vasculature.
30002415	1	6	theme	protective	156:165	arg1	B					135:135	Nucleoside diphosphate kinase B	105:135	Nucleoside diphosphate kinase B (NDPK-B)	105:144	Nucleoside diphosphate kinase B (NDPK-B) acts as a protective factor in the retinal vasculature.
30002415	9	7	theme	increased	1044:1052	arg1	O-GlcNAcylation					1054:1068	An increased O-GlcNAcylation	1041:1068	An increased O-GlcNAcylation of FoxO1	1041:1077	An increased O-GlcNAcylation of FoxO1 was revealed upon NDPK-B depletion.
30002415	11	8	theme	NDPK-B	1292:1297	arg1	deficiency					1299:1308	NDPK-B deficiency	1292:1308	NDPK-B deficiency	1292:1308	In summary, we demonstrated that the upregulation of Ang-2 upon NDPK-B deficiency is driven by O-GlcNAcylation of FoxO1.
30002415	11	9	theme	Ang-2	1281:1285	arg1	upregulation					1265:1276	the upregulation	1261:1276	the upregulation of Ang-2 upon NDPK-B deficiency	1261:1308	In summary, we demonstrated that the upregulation of Ang-2 upon NDPK-B deficiency is driven by O-GlcNAcylation of FoxO1.
30002415	12	10	theme	retinal	1520:1526	arg1	vasoregression					1528:1541	retinal vasoregression	1520:1541	retinal vasoregression	1520:1541	Our data provide evidence for a central role of protein O-GlcNAcylation in NDPK-B associated vascular damage and point to the hexosamine pathway as an important target in retinal vasoregression.
30002415	12	11	theme	O-GlcNAcylation	1405:1419	arg1	role					1389:1392	a central role	1379:1392	a central role of protein O-GlcNAcylation in NDPK-B associated vascular damage	1379:1456	Our data provide evidence for a central role of protein O-GlcNAcylation in NDPK-B associated vascular damage and point to the hexosamine pathway as an important target in retinal vasoregression.
30002415	4	12	theme	Ang-2	572:576	arg1	upregulation					578:589	Ang-2 upregulation	572:589	Ang-2 upregulation	572:589	We therefore investigated the importance of Ang-2 in NDPK-B deficient retinas and characterized the mechanisms of Ang-2 upregulation upon NDPK-B depletion in cultured ECs.
30002415	6	13	theme	depleted	872:879	arg1	ECs					881:883	NDPK-B depleted ECs	865:883	NDPK-B depleted ECs	865:883	On the molecular level, FoxO1, a transcription factor regulating Ang-2, was upregulated in NDPK-B depleted ECs.
30002415	12	14	theme	protein	1397:1403	arg1	O-GlcNAcylation					1405:1419	protein O-GlcNAcylation	1397:1419	protein O-GlcNAcylation	1397:1419	Our data provide evidence for a central role of protein O-GlcNAcylation in NDPK-B associated vascular damage and point to the hexosamine pathway as an important target in retinal vasoregression.
30002415	8	15	located	found	1004:1008	arg2	FoxO1					994:998	Furthermore O-GlcNAcylated FoxO1	967:998	Furthermore O-GlcNAcylated FoxO1	967:998	Furthermore O-GlcNAcylated FoxO1 was found preferentially in the nucleus.
30002415	8	15	located	found	1004:1008	arg1	nucleus					1032:1038	the nucleus	1028:1038	the nucleus	1028:1038	Furthermore O-GlcNAcylated FoxO1 was found preferentially in the nucleus.
30002415	3	16	theme	retinal	328:334	arg1	vasoregression					336:349	retinal vasoregression	328:349	retinal vasoregression in DR	328:355	Angiopoetin 2 (Ang-2), an initiator of retinal vasoregression in DR, is upregulated in NDPK-B deficient retinas and in NDPK-B depleted endothelial cells (ECs) in vitro.
30002415	6	17	theme	NDPK-B	865:870	arg1	ECs					881:883	NDPK-B depleted ECs	865:883	NDPK-B depleted ECs	865:883	On the molecular level, FoxO1, a transcription factor regulating Ang-2, was upregulated in NDPK-B depleted ECs.
30002415	6	18	theme	molecular	781:789	arg1	level					791:795	the molecular level	777:795	the molecular level	777:795	On the molecular level, FoxO1, a transcription factor regulating Ang-2, was upregulated in NDPK-B depleted ECs.
30002415	10	19	theme	O-GlcNAcylation	1156:1170	arg1	depletion					1190:1198	protein O-GlcNAcylation normalized NDPK-B depletion	1148:1198	protein O-GlcNAcylation normalized NDPK-B depletion	1148:1198	In accordance, the inhibition of protein O-GlcNAcylation normalized NDPK-B depletion induced Ang-2 upregulation.
30002415	9	20	theme	FoxO1	1073:1077	arg1	O-GlcNAcylation					1054:1068	An increased O-GlcNAcylation	1041:1068	An increased O-GlcNAcylation of FoxO1	1041:1077	An increased O-GlcNAcylation of FoxO1 was revealed upon NDPK-B depletion.
30002415	3	21	theme	depleted	415:422	arg1	ECs					443:445	ECs	443:445	ECs	443:445	Angiopoetin 2 (Ang-2), an initiator of retinal vasoregression in DR, is upregulated in NDPK-B deficient retinas and in NDPK-B depleted endothelial cells (ECs) in vitro.
30002415	3	21	theme	depleted	415:422	arg1	cells					436:440	NDPK-B depleted endothelial cells	408:440	NDPK-B depleted endothelial cells (ECs)	408:446	Angiopoetin 2 (Ang-2), an initiator of retinal vasoregression in DR, is upregulated in NDPK-B deficient retinas and in NDPK-B depleted endothelial cells (ECs) in vitro.
30002415	3	22	theme	vasoregression	336:349	arg1	initiator					315:323	an initiator	312:323	an initiator of retinal vasoregression in DR	312:355	Angiopoetin 2 (Ang-2), an initiator of retinal vasoregression in DR, is upregulated in NDPK-B deficient retinas and in NDPK-B depleted endothelial cells (ECs) in vitro.
30002415	3	22	theme	vasoregression	336:349	arg1	Angiopoetin					289:299	Angiopoetin 2	289:301	Angiopoetin 2 (Ang-2)	289:309	Angiopoetin 2 (Ang-2), an initiator of retinal vasoregression in DR, is upregulated in NDPK-B deficient retinas and in NDPK-B depleted endothelial cells (ECs) in vitro.
30002415	10	23	theme	depletion	1190:1198	arg1	inhibition					1134:1143	the inhibition	1130:1143	the inhibition of protein O-GlcNAcylation normalized NDPK-B depletion	1130:1198	In accordance, the inhibition of protein O-GlcNAcylation normalized NDPK-B depletion induced Ang-2 upregulation.
30002415	3	24	theme	endothelial	424:434	arg1	ECs					443:445	ECs	443:445	ECs	443:445	Angiopoetin 2 (Ang-2), an initiator of retinal vasoregression in DR, is upregulated in NDPK-B deficient retinas and in NDPK-B depleted endothelial cells (ECs) in vitro.
30002415	3	24	theme	endothelial	424:434	arg1	cells					436:440	NDPK-B depleted endothelial cells	408:440	NDPK-B depleted endothelial cells (ECs)	408:446	Angiopoetin 2 (Ang-2), an initiator of retinal vasoregression in DR, is upregulated in NDPK-B deficient retinas and in NDPK-B depleted endothelial cells (ECs) in vitro.
30002415	5	25	theme	haplodeficient	753:766	arg1	mice					768:771	Ang-2 haplodeficient mice	747:771	Ang-2 haplodeficient mice	747:771	The crucial role of retinal Ang-2 in the initiation of vasoregression was verified by crossing NDPK-B deficient with Ang-2 haplodeficient mice.
30002415	8	26	theme	O-GlcNAcylated	979:992	arg1	FoxO1					994:998	Furthermore O-GlcNAcylated FoxO1	967:998	Furthermore O-GlcNAcylated FoxO1	967:998	Furthermore O-GlcNAcylated FoxO1 was found preferentially in the nucleus.
30002415	12	27	theme	central	1381:1387	arg1	role					1389:1392	a central role	1379:1392	a central role of protein O-GlcNAcylation in NDPK-B associated vascular damage	1379:1456	Our data provide evidence for a central role of protein O-GlcNAcylation in NDPK-B associated vascular damage and point to the hexosamine pathway as an important target in retinal vasoregression.
30002415	12	28	theme	associated	1431:1440	arg1	damage					1451:1456	NDPK-B associated vascular damage	1424:1456	NDPK-B associated vascular damage	1424:1456	Our data provide evidence for a central role of protein O-GlcNAcylation in NDPK-B associated vascular damage and point to the hexosamine pathway as an important target in retinal vasoregression.
30002415	7	29	theme	FoxO1	899:903	arg1	Knockdown					886:894	Knockdown	886:894	Knockdown of FoxO1	886:903	Knockdown of FoxO1 abolished the elevation of Ang-2 induced by NDPK-B depletion.
30002415	1	30	theme	Nucleoside	105:114	arg1	NDPK-B					138:143	NDPK-B	138:143	NDPK-B	138:143	Nucleoside diphosphate kinase B (NDPK-B) acts as a protective factor in the retinal vasculature.
30002415	1	30	theme	Nucleoside	105:114	arg1	B					135:135	Nucleoside diphosphate kinase B	105:135	Nucleoside diphosphate kinase B (NDPK-B)	105:144	Nucleoside diphosphate kinase B (NDPK-B) acts as a protective factor in the retinal vasculature.
30002415	1	30	theme	Nucleoside	105:114	arg1	factor					167:172	a protective factor	154:172	a protective factor in the retinal vasculature	154:199	Nucleoside diphosphate kinase B (NDPK-B) acts as a protective factor in the retinal vasculature.
30002415	0	31	theme	kinase	57:62	arg1	deficiency					66:75	nucleoside diphosphate kinase B deficiency	34:75	nucleoside diphosphate kinase B deficiency induced endothelial damage	34:102	O-GlcNAcylation of FoxO1 mediates nucleoside diphosphate kinase B deficiency induced endothelial damage.
30002415	1	32	theme	retinal	181:187	arg1	vasculature					189:199	the retinal vasculature	177:199	the retinal vasculature	177:199	Nucleoside diphosphate kinase B (NDPK-B) acts as a protective factor in the retinal vasculature.
30002415	4	33	theme	deficient	518:526	arg1	retinas					528:534	NDPK-B deficient retinas	511:534	NDPK-B deficient retinas	511:534	We therefore investigated the importance of Ang-2 in NDPK-B deficient retinas and characterized the mechanisms of Ang-2 upregulation upon NDPK-B depletion in cultured ECs.
30002415	10	34	theme	protein	1148:1154	arg1	O-GlcNAcylation					1156:1170	protein O-GlcNAcylation	1148:1170	protein O-GlcNAcylation normalized NDPK-B depletion	1148:1198	In accordance, the inhibition of protein O-GlcNAcylation normalized NDPK-B depletion induced Ang-2 upregulation.
30002415	7	35	theme	Ang-2	932:936	arg1	elevation					919:927	the elevation	915:927	the elevation of Ang-2 induced by NDPK-B depletion	915:964	Knockdown of FoxO1 abolished the elevation of Ang-2 induced by NDPK-B depletion.
30002415	1	36	theme	diphosphate	116:126	arg1	NDPK-B					138:143	NDPK-B	138:143	NDPK-B	138:143	Nucleoside diphosphate kinase B (NDPK-B) acts as a protective factor in the retinal vasculature.
30002415	1	36	theme	diphosphate	116:126	arg1	B					135:135	Nucleoside diphosphate kinase B	105:135	Nucleoside diphosphate kinase B (NDPK-B)	105:144	Nucleoside diphosphate kinase B (NDPK-B) acts as a protective factor in the retinal vasculature.
30002415	1	36	theme	diphosphate	116:126	arg1	factor					167:172	a protective factor	154:172	a protective factor in the retinal vasculature	154:199	Nucleoside diphosphate kinase B (NDPK-B) acts as a protective factor in the retinal vasculature.
30002415	9	37	theme	NDPK-B	1097:1102	arg1	depletion					1104:1112	NDPK-B depletion	1097:1112	NDPK-B depletion	1097:1112	An increased O-GlcNAcylation of FoxO1 was revealed upon NDPK-B depletion.
30002415	4	38	theme	cultured	616:623	arg1	ECs					625:627	cultured ECs	616:627	cultured ECs	616:627	We therefore investigated the importance of Ang-2 in NDPK-B deficient retinas and characterized the mechanisms of Ang-2 upregulation upon NDPK-B depletion in cultured ECs.
30002415	0	39	theme	FoxO1	19:23	arg1	O-GlcNAcylation					0:14	O-GlcNAcylation	0:14	O-GlcNAcylation of FoxO1	0:23	O-GlcNAcylation of FoxO1 mediates nucleoside diphosphate kinase B deficiency induced endothelial damage.
30002415	10	40	theme	Ang-2	1208:1212	arg1	upregulation					1214:1225	Ang-2 upregulation	1208:1225	Ang-2 upregulation	1208:1225	In accordance, the inhibition of protein O-GlcNAcylation normalized NDPK-B depletion induced Ang-2 upregulation.
30002415	12	41	theme	NDPK-B	1424:1429	arg1	damage					1451:1456	NDPK-B associated vascular damage	1424:1456	NDPK-B associated vascular damage	1424:1456	Our data provide evidence for a central role of protein O-GlcNAcylation in NDPK-B associated vascular damage and point to the hexosamine pathway as an important target in retinal vasoregression.
30002415	1	42	theme	kinase	128:133	arg1	NDPK-B					138:143	NDPK-B	138:143	NDPK-B	138:143	Nucleoside diphosphate kinase B (NDPK-B) acts as a protective factor in the retinal vasculature.
30002415	1	42	theme	kinase	128:133	arg1	B					135:135	Nucleoside diphosphate kinase B	105:135	Nucleoside diphosphate kinase B (NDPK-B)	105:144	Nucleoside diphosphate kinase B (NDPK-B) acts as a protective factor in the retinal vasculature.
30002415	1	42	theme	kinase	128:133	arg1	factor					167:172	a protective factor	154:172	a protective factor in the retinal vasculature	154:199	Nucleoside diphosphate kinase B (NDPK-B) acts as a protective factor in the retinal vasculature.
30002415	0	43	theme	diphosphate	45:55	arg1	kinase					57:62	nucleoside diphosphate kinase	34:62	nucleoside diphosphate kinase B deficiency induced endothelial damage	34:102	O-GlcNAcylation of FoxO1 mediates nucleoside diphosphate kinase B deficiency induced endothelial damage.
30002415	12	44	theme	important	1500:1508	arg1	target					1510:1515	an important target	1497:1515	an important target in retinal vasoregression	1497:1541	Our data provide evidence for a central role of protein O-GlcNAcylation in NDPK-B associated vascular damage and point to the hexosamine pathway as an important target in retinal vasoregression.
30002415	5	45	theme	vasoregression	685:698	arg1	initiation					671:680	the initiation	667:680	the initiation of vasoregression	667:698	The crucial role of retinal Ang-2 in the initiation of vasoregression was verified by crossing NDPK-B deficient with Ang-2 haplodeficient mice.
30002415	3	46	from	vasoregression	336:349	arg1	DR					354:355	DR	354:355	DR	354:355	Angiopoetin 2 (Ang-2), an initiator of retinal vasoregression in DR, is upregulated in NDPK-B deficient retinas and in NDPK-B depleted endothelial cells (ECs) in vitro.
30002415	0	47	theme	nucleoside	34:43	arg1	kinase					57:62	nucleoside diphosphate kinase	34:62	nucleoside diphosphate kinase B deficiency induced endothelial damage	34:102	O-GlcNAcylation of FoxO1 mediates nucleoside diphosphate kinase B deficiency induced endothelial damage.
30002415	4	48	theme	Ang-2	502:506	arg1	importance					488:497	the importance	484:497	the importance of Ang-2 in NDPK-B deficient retinas	484:534	We therefore investigated the importance of Ang-2 in NDPK-B deficient retinas and characterized the mechanisms of Ang-2 upregulation upon NDPK-B depletion in cultured ECs.
30002415	2	49	theme	retinal	229:235	arg1	vasoregression					237:250	retinal vasoregression	229:250	retinal vasoregression mimicking diabetic retinopathy (DR)	229:286	NDPK-B deficiency leads to retinal vasoregression mimicking diabetic retinopathy (DR).
30002415	5	50	theme	NDPK-B	725:730	arg1	deficient					732:740	NDPK-B deficient	725:740	NDPK-B deficient	725:740	The crucial role of retinal Ang-2 in the initiation of vasoregression was verified by crossing NDPK-B deficient with Ang-2 haplodeficient mice.
30002415	0	51	theme	B	64:64	arg1	deficiency					66:75	nucleoside diphosphate kinase B deficiency	34:75	nucleoside diphosphate kinase B deficiency induced endothelial damage	34:102	O-GlcNAcylation of FoxO1 mediates nucleoside diphosphate kinase B deficiency induced endothelial damage.
30002415	5	52	from	role	642:645	arg1	initiation					671:680	the initiation	667:680	the initiation of vasoregression	667:698	The crucial role of retinal Ang-2 in the initiation of vasoregression was verified by crossing NDPK-B deficient with Ang-2 haplodeficient mice.
30002415	5	53	theme	retinal	650:656	arg1	Ang-2					658:662	retinal Ang-2	650:662	retinal Ang-2	650:662	The crucial role of retinal Ang-2 in the initiation of vasoregression was verified by crossing NDPK-B deficient with Ang-2 haplodeficient mice.
30002415	3	54	from	DR	354:355	arg1	initiator					315:323	an initiator	312:323	an initiator of retinal vasoregression in DR	312:355	Angiopoetin 2 (Ang-2), an initiator of retinal vasoregression in DR, is upregulated in NDPK-B deficient retinas and in NDPK-B depleted endothelial cells (ECs) in vitro.
30002415	3	54	from	DR	354:355	arg1	Angiopoetin					289:299	Angiopoetin 2	289:301	Angiopoetin 2 (Ang-2)	289:309	Angiopoetin 2 (Ang-2), an initiator of retinal vasoregression in DR, is upregulated in NDPK-B deficient retinas and in NDPK-B depleted endothelial cells (ECs) in vitro.
30002415	3	55	dep	depleted	415:422	arg1	NDPK-B					408:413	NDPK-B	408:413	NDPK-B	408:413	Angiopoetin 2 (Ang-2), an initiator of retinal vasoregression in DR, is upregulated in NDPK-B deficient retinas and in NDPK-B depleted endothelial cells (ECs) in vitro.
30002415	3	56	theme	deficient	383:391	arg1	retinas					393:399	NDPK-B deficient retinas	376:399	NDPK-B deficient retinas	376:399	Angiopoetin 2 (Ang-2), an initiator of retinal vasoregression in DR, is upregulated in NDPK-B deficient retinas and in NDPK-B depleted endothelial cells (ECs) in vitro.
30002415	4	57	theme	NDPK-B	511:516	arg1	retinas					528:534	NDPK-B deficient retinas	511:534	NDPK-B deficient retinas	511:534	We therefore investigated the importance of Ang-2 in NDPK-B deficient retinas and characterized the mechanisms of Ang-2 upregulation upon NDPK-B depletion in cultured ECs.
30002415	5	58	theme	Ang-2	658:662	arg1	role					642:645	The crucial role	630:645	The crucial role of retinal Ang-2 in the initiation of vasoregression	630:698	The crucial role of retinal Ang-2 in the initiation of vasoregression was verified by crossing NDPK-B deficient with Ang-2 haplodeficient mice.
30002415	6	59	theme	transcription	807:819	arg1	factor					821:826	a transcription factor	805:826	a transcription factor regulating Ang-2	805:843	On the molecular level, FoxO1, a transcription factor regulating Ang-2, was upregulated in NDPK-B depleted ECs.
30002415	6	59	theme	transcription	807:819	arg1	FoxO1					798:802	FoxO1	798:802	FoxO1	798:802	On the molecular level, FoxO1, a transcription factor regulating Ang-2, was upregulated in NDPK-B depleted ECs.
30002415	2	60	theme	NDPK-B	202:207	arg1	deficiency					209:218	NDPK-B deficiency	202:218	NDPK-B deficiency	202:218	NDPK-B deficiency leads to retinal vasoregression mimicking diabetic retinopathy (DR).
30002415	7	61	theme	NDPK-B	949:954	arg1	depletion					956:964	NDPK-B depletion	949:964	NDPK-B depletion	949:964	Knockdown of FoxO1 abolished the elevation of Ang-2 induced by NDPK-B depletion.
30002415	11	62	theme	FoxO1	1342:1346	arg1	O-GlcNAcylation					1323:1337	O-GlcNAcylation	1323:1337	O-GlcNAcylation of FoxO1	1323:1346	In summary, we demonstrated that the upregulation of Ang-2 upon NDPK-B deficiency is driven by O-GlcNAcylation of FoxO1.
30002415	3	63	from	initiator	315:323	arg1	DR					354:355	DR	354:355	DR	354:355	Angiopoetin 2 (Ang-2), an initiator of retinal vasoregression in DR, is upregulated in NDPK-B deficient retinas and in NDPK-B depleted endothelial cells (ECs) in vitro.
30002415	12	64	from	role	1389:1392	arg1	damage					1451:1456	NDPK-B associated vascular damage	1424:1456	NDPK-B associated vascular damage	1424:1456	Our data provide evidence for a central role of protein O-GlcNAcylation in NDPK-B associated vascular damage and point to the hexosamine pathway as an important target in retinal vasoregression.
30002415	4	65	theme	upregulation	578:589	arg1	mechanisms					558:567	the mechanisms	554:567	the mechanisms of Ang-2 upregulation upon NDPK-B depletion in cultured ECs	554:627	We therefore investigated the importance of Ang-2 in NDPK-B deficient retinas and characterized the mechanisms of Ang-2 upregulation upon NDPK-B depletion in cultured ECs.
30002415	4	66	from	depletion	603:611	arg1	ECs					625:627	cultured ECs	616:627	cultured ECs	616:627	We therefore investigated the importance of Ang-2 in NDPK-B deficient retinas and characterized the mechanisms of Ang-2 upregulation upon NDPK-B depletion in cultured ECs.
30002415	2	67	theme	diabetic	262:269	arg1	DR					284:285	DR	284:285	DR	284:285	NDPK-B deficiency leads to retinal vasoregression mimicking diabetic retinopathy (DR).
30002415	2	67	theme	diabetic	262:269	arg1	retinopathy					271:281	diabetic retinopathy	262:281	diabetic retinopathy (DR)	262:286	NDPK-B deficiency leads to retinal vasoregression mimicking diabetic retinopathy (DR).
30002415	12	68	from	target	1510:1515	arg1	vasoregression					1528:1541	retinal vasoregression	1520:1541	retinal vasoregression	1520:1541	Our data provide evidence for a central role of protein O-GlcNAcylation in NDPK-B associated vascular damage and point to the hexosamine pathway as an important target in retinal vasoregression.
30002415	10	69	theme	NDPK-B	1183:1188	arg1	depletion					1190:1198	protein O-GlcNAcylation normalized NDPK-B depletion	1148:1198	protein O-GlcNAcylation normalized NDPK-B depletion	1148:1198	In accordance, the inhibition of protein O-GlcNAcylation normalized NDPK-B depletion induced Ang-2 upregulation.
30002415	3	70	theme	NDPK-B	376:381	arg1	retinas					393:399	NDPK-B deficient retinas	376:399	NDPK-B deficient retinas	376:399	Angiopoetin 2 (Ang-2), an initiator of retinal vasoregression in DR, is upregulated in NDPK-B deficient retinas and in NDPK-B depleted endothelial cells (ECs) in vitro.
30002415	10	71	theme	normalized	1172:1181	arg1	depletion					1190:1198	protein O-GlcNAcylation normalized NDPK-B depletion	1148:1198	protein O-GlcNAcylation normalized NDPK-B depletion	1148:1198	In accordance, the inhibition of protein O-GlcNAcylation normalized NDPK-B depletion induced Ang-2 upregulation.
30002415	1	72	from	factor	167:172	arg1	vasculature					189:199	the retinal vasculature	177:199	the retinal vasculature	177:199	Nucleoside diphosphate kinase B (NDPK-B) acts as a protective factor in the retinal vasculature.
30002415	4	73	theme	NDPK-B	596:601	arg1	depletion					603:611	NDPK-B depletion	596:611	NDPK-B depletion in cultured ECs	596:627	We therefore investigated the importance of Ang-2 in NDPK-B deficient retinas and characterized the mechanisms of Ang-2 upregulation upon NDPK-B depletion in cultured ECs.
26789264	5	0	theme	liver-specific	716:729	arg1	protein					750:756	a liver-specific fatty acid binding protein	714:756	a liver-specific fatty acid binding protein FABP1	714:762	We report that uridine administration was associated with O-GlcNAc modification of FOXO1, increased gluconeogenesis, reduced insulin signaling activity, and reduced expression of a liver-specific fatty acid binding protein FABP1.
26789264	5	1	theme	FOXO1	618:622	arg1	modification					602:613	O-GlcNAc modification	593:613	O-GlcNAc modification of FOXO1	593:622	We report that uridine administration was associated with O-GlcNAc modification of FOXO1, increased gluconeogenesis, reduced insulin signaling activity, and reduced expression of a liver-specific fatty acid binding protein FABP1.
26789264	5	2	theme	FABP1	758:762	arg1	expression					700:709	expression	700:709	expression of a liver-specific fatty acid binding protein FABP1	700:762	We report that uridine administration was associated with O-GlcNAc modification of FOXO1, increased gluconeogenesis, reduced insulin signaling activity, and reduced expression of a liver-specific fatty acid binding protein FABP1.
26789264	4	3	theme	C57BL/6J	520:527	arg1	mice					529:532	C57BL/6J mice	520:532	C57BL/6J mice	520:532	In this study, long-term effects of uridine on liver metabolism were examined in both HepG2 cell cultures and C57BL/6J mice.
26789264	7	4	theme	uridine	929:935	arg1	potentials					915:924	the therapeutic potentials	899:924	the therapeutic potentials of uridine	899:935	Our findings suggest that the therapeutic potentials of uridine should be designed for short-term acute administration.
26789264	6	5	theme	systemic	799:806	arg1	intolerance					816:826	systemic glucose intolerance	799:826	systemic glucose intolerance	799:826	Long-term uridine feeding induced systemic glucose intolerance and severe liver lipid accumulation in mice.
26789264	4	6	theme	long-term	425:433	arg1	effects					435:441	long-term effects	425:441	long-term effects of uridine on liver metabolism	425:472	In this study, long-term effects of uridine on liver metabolism were examined in both HepG2 cell cultures and C57BL/6J mice.
26789264	7	7	theme	therapeutic	903:913	arg1	potentials					915:924	the therapeutic potentials	899:924	the therapeutic potentials of uridine	899:935	Our findings suggest that the therapeutic potentials of uridine should be designed for short-term acute administration.
26789264	3	8	theme	precise	367:373	arg1	mechanism					375:383	the precise mechanism	363:383	the precise mechanism	363:383	Uridine has the ability to modulate liver metabolism; however, the precise mechanism has not been delineated.
26789264	6	9	theme	lipid	845:849	arg1	accumulation					851:862	severe liver lipid accumulation	832:862	severe liver lipid accumulation	832:862	Long-term uridine feeding induced systemic glucose intolerance and severe liver lipid accumulation in mice.
26789264	0	10	from	Liver	45:49	arg1	Mice					82:85	Mice	82:85	Mice	82:85	Chronic Uridine Administration Induces Fatty Liver and Pre-Diabetic Conditions in Mice.
26789264	6	11	theme	severe	832:837	arg1	accumulation					851:862	severe liver lipid accumulation	832:862	severe liver lipid accumulation	832:862	Long-term uridine feeding induced systemic glucose intolerance and severe liver lipid accumulation in mice.
26789264	6	12	theme	liver	839:843	arg1	accumulation					851:862	severe liver lipid accumulation	832:862	severe liver lipid accumulation	832:862	Long-term uridine feeding induced systemic glucose intolerance and severe liver lipid accumulation in mice.
26789264	0	13	theme	Uridine	8:14	arg1	Administration					16:29	Chronic Uridine Administration	0:29	Chronic Uridine Administration	0:29	Chronic Uridine Administration Induces Fatty Liver and Pre-Diabetic Conditions in Mice.
26789264	4	14	theme	HepG2	496:500	arg1	cultures					507:514	HepG2 cell cultures	496:514	HepG2 cell cultures	496:514	In this study, long-term effects of uridine on liver metabolism were examined in both HepG2 cell cultures and C57BL/6J mice.
26789264	5	15	theme	insulin	660:666	arg1	activity					678:685	insulin signaling activity	660:685	insulin signaling activity	660:685	We report that uridine administration was associated with O-GlcNAc modification of FOXO1, increased gluconeogenesis, reduced insulin signaling activity, and reduced expression of a liver-specific fatty acid binding protein FABP1.
26789264	5	16	mod	modification	602:613	arg3	O-GlcNAc					593:600	O-GlcNAc modification	593:613	O-GlcNAc modification of FOXO1	593:622	We report that uridine administration was associated with O-GlcNAc modification of FOXO1, increased gluconeogenesis, reduced insulin signaling activity, and reduced expression of a liver-specific fatty acid binding protein FABP1.
26789264	5	16	mod	modification	602:613	arg1	FOXO1					618:622	FOXO1	618:622	FOXO1	618:622	We report that uridine administration was associated with O-GlcNAc modification of FOXO1, increased gluconeogenesis, reduced insulin signaling activity, and reduced expression of a liver-specific fatty acid binding protein FABP1.
26789264	0	17	theme	Chronic	0:6	arg1	Administration					16:29	Chronic Uridine Administration	0:29	Chronic Uridine Administration	0:29	Chronic Uridine Administration Induces Fatty Liver and Pre-Diabetic Conditions in Mice.
26789264	5	18	theme	signaling	668:676	arg1	activity					678:685	insulin signaling activity	660:685	insulin signaling activity	660:685	We report that uridine administration was associated with O-GlcNAc modification of FOXO1, increased gluconeogenesis, reduced insulin signaling activity, and reduced expression of a liver-specific fatty acid binding protein FABP1.
26789264	3	19	contain	has	308:310	arg1	Uridine					300:306	Uridine	300:306	Uridine	300:306	Uridine has the ability to modulate liver metabolism; however, the precise mechanism has not been delineated.
26789264	3	19	contain	has	308:310	arg2	ability					316:322	the ability to modulate liver metabolism	312:351	the ability to modulate liver metabolism	312:351	Uridine has the ability to modulate liver metabolism; however, the precise mechanism has not been delineated.
26789264	4	20	theme	liver	457:461	arg1	metabolism					463:472	liver metabolism	457:472	liver metabolism	457:472	In this study, long-term effects of uridine on liver metabolism were examined in both HepG2 cell cultures and C57BL/6J mice.
26789264	5	21	theme	fatty	731:735	arg1	protein					750:756	a liver-specific fatty acid binding protein	714:756	a liver-specific fatty acid binding protein FABP1	714:762	We report that uridine administration was associated with O-GlcNAc modification of FOXO1, increased gluconeogenesis, reduced insulin signaling activity, and reduced expression of a liver-specific fatty acid binding protein FABP1.
26789264	5	22	theme	acid	737:740	arg1	protein					750:756	a liver-specific fatty acid binding protein	714:756	a liver-specific fatty acid binding protein FABP1	714:762	We report that uridine administration was associated with O-GlcNAc modification of FOXO1, increased gluconeogenesis, reduced insulin signaling activity, and reduced expression of a liver-specific fatty acid binding protein FABP1.
26789264	1	23	theme	pyrimidine	101:110	arg1	nucleoside					112:121	a pyrimidine nucleoside	99:121	a pyrimidine nucleoside that exerts restorative functions in tissues under stress	99:179	Uridine is a pyrimidine nucleoside that exerts restorative functions in tissues under stress.
26789264	1	23	theme	pyrimidine	101:110	arg1	Uridine					88:94	Uridine	88:94	Uridine	88:94	Uridine is a pyrimidine nucleoside that exerts restorative functions in tissues under stress.
26789264	5	24	theme	binding	742:748	arg1	protein					750:756	a liver-specific fatty acid binding protein	714:756	a liver-specific fatty acid binding protein FABP1	714:762	We report that uridine administration was associated with O-GlcNAc modification of FOXO1, increased gluconeogenesis, reduced insulin signaling activity, and reduced expression of a liver-specific fatty acid binding protein FABP1.
26789264	2	25	theme	Short-term	182:191	arg1	co-administration					193:209	Short-term co-administration	182:209	Short-term co-administration of uridine with multiple unrelated drugs	182:250	Short-term co-administration of uridine with multiple unrelated drugs prevents drug-induced liver lipid accumulation.
26789264	2	26	theme	drug-induced	261:272	arg1	accumulation					286:297	drug-induced liver lipid accumulation	261:297	drug-induced liver lipid accumulation	261:297	Short-term co-administration of uridine with multiple unrelated drugs prevents drug-induced liver lipid accumulation.
26789264	0	27	theme	Fatty	39:43	arg1	Liver					45:49	Fatty Liver	39:49	Fatty Liver	39:49	Chronic Uridine Administration Induces Fatty Liver and Pre-Diabetic Conditions in Mice.
26789264	5	28	theme	protein	750:756	arg1	FABP1					758:762	a liver-specific fatty acid binding protein FABP1	714:762	a liver-specific fatty acid binding protein FABP1	714:762	We report that uridine administration was associated with O-GlcNAc modification of FOXO1, increased gluconeogenesis, reduced insulin signaling activity, and reduced expression of a liver-specific fatty acid binding protein FABP1.
26789264	5	29	theme	uridine	550:556	arg1	administration					558:571	uridine administration	550:571	uridine administration	550:571	We report that uridine administration was associated with O-GlcNAc modification of FOXO1, increased gluconeogenesis, reduced insulin signaling activity, and reduced expression of a liver-specific fatty acid binding protein FABP1.
26789264	0	30	theme	Pre-Diabetic	55:66	arg1	Conditions					68:77	Pre-Diabetic Conditions	55:77	Pre-Diabetic Conditions	55:77	Chronic Uridine Administration Induces Fatty Liver and Pre-Diabetic Conditions in Mice.
26789264	3	31	theme	liver	336:340	arg1	metabolism					342:351	liver metabolism	336:351	liver metabolism	336:351	Uridine has the ability to modulate liver metabolism; however, the precise mechanism has not been delineated.
26789264	0	32	from	Conditions	68:77	arg1	Mice					82:85	Mice	82:85	Mice	82:85	Chronic Uridine Administration Induces Fatty Liver and Pre-Diabetic Conditions in Mice.
26789264	4	33	theme	cell	502:505	arg1	cultures					507:514	HepG2 cell cultures	496:514	HepG2 cell cultures	496:514	In this study, long-term effects of uridine on liver metabolism were examined in both HepG2 cell cultures and C57BL/6J mice.
26789264	2	34	theme	multiple	227:234	arg1	drugs					246:250	multiple unrelated drugs	227:250	multiple unrelated drugs	227:250	Short-term co-administration of uridine with multiple unrelated drugs prevents drug-induced liver lipid accumulation.
26789264	2	35	theme	unrelated	236:244	arg1	drugs					246:250	multiple unrelated drugs	227:250	multiple unrelated drugs	227:250	Short-term co-administration of uridine with multiple unrelated drugs prevents drug-induced liver lipid accumulation.
26789264	7	36	theme	short-term	960:969	arg1	administration					977:990	short-term acute administration	960:990	short-term acute administration	960:990	Our findings suggest that the therapeutic potentials of uridine should be designed for short-term acute administration.
26789264	2	37	with	co-administration	193:209	arg1	drugs					246:250	multiple unrelated drugs	227:250	multiple unrelated drugs	227:250	Short-term co-administration of uridine with multiple unrelated drugs prevents drug-induced liver lipid accumulation.
26789264	5	38	theme	O-GlcNAc	593:600	arg1	modification					602:613	O-GlcNAc modification	593:613	O-GlcNAc modification of FOXO1	593:622	We report that uridine administration was associated with O-GlcNAc modification of FOXO1, increased gluconeogenesis, reduced insulin signaling activity, and reduced expression of a liver-specific fatty acid binding protein FABP1.
26789264	4	39	from	effects	435:441	arg1	metabolism					463:472	liver metabolism	457:472	liver metabolism	457:472	In this study, long-term effects of uridine on liver metabolism were examined in both HepG2 cell cultures and C57BL/6J mice.
26789264	2	40	theme	uridine	214:220	arg1	co-administration					193:209	Short-term co-administration	182:209	Short-term co-administration of uridine with multiple unrelated drugs	182:250	Short-term co-administration of uridine with multiple unrelated drugs prevents drug-induced liver lipid accumulation.
26789264	6	41	theme	glucose	808:814	arg1	intolerance					816:826	systemic glucose intolerance	799:826	systemic glucose intolerance	799:826	Long-term uridine feeding induced systemic glucose intolerance and severe liver lipid accumulation in mice.
26789264	6	42	theme	uridine	775:781	arg1	feeding					783:789	Long-term uridine feeding	765:789	Long-term uridine feeding	765:789	Long-term uridine feeding induced systemic glucose intolerance and severe liver lipid accumulation in mice.
26789264	1	43	theme	restorative	135:145	arg1	functions					147:155	restorative functions	135:155	restorative functions	135:155	Uridine is a pyrimidine nucleoside that exerts restorative functions in tissues under stress.
26789264	4	44	theme	uridine	446:452	arg1	effects					435:441	long-term effects	425:441	long-term effects of uridine on liver metabolism	425:472	In this study, long-term effects of uridine on liver metabolism were examined in both HepG2 cell cultures and C57BL/6J mice.
26789264	2	45	theme	lipid	280:284	arg1	accumulation					286:297	drug-induced liver lipid accumulation	261:297	drug-induced liver lipid accumulation	261:297	Short-term co-administration of uridine with multiple unrelated drugs prevents drug-induced liver lipid accumulation.
26789264	6	46	theme	Long-term	765:773	arg1	feeding					783:789	Long-term uridine feeding	765:789	Long-term uridine feeding	765:789	Long-term uridine feeding induced systemic glucose intolerance and severe liver lipid accumulation in mice.
26789264	7	47	theme	acute	971:975	arg1	administration					977:990	short-term acute administration	960:990	short-term acute administration	960:990	Our findings suggest that the therapeutic potentials of uridine should be designed for short-term acute administration.
26789264	2	48	theme	liver	274:278	arg1	accumulation					286:297	drug-induced liver lipid accumulation	261:297	drug-induced liver lipid accumulation	261:297	Short-term co-administration of uridine with multiple unrelated drugs prevents drug-induced liver lipid accumulation.
32805318	8	0	theme	level	1364:1368	arg1	modulation					1370:1379	DNA-PKcs O-GlcNAcylation level modulation	1339:1379	DNA-PKcs O-GlcNAcylation level modulation	1339:1379	CONCLUSIONS DNA-PKcs Ser2056 phosphorylation is antagonistically linked to DNA-PKcs O-GlcNAcylation level modulation.
32805318	9	1	from	role	1423:1426	arg1	DDR					1471:1473	the DDR	1467:1473	the DDR	1467:1473	GENERAL SIGNIFICANCE Given the essential role of DNA-PKcs Ser2056 phosphorylation in the DDR, this study brings data about the role of cell O-GlcNAc level on genome integrity maintenance.
32805318	9	2	theme	Ser2056	1440:1446	arg1	phosphorylation					1448:1462	DNA-PKcs Ser2056 phosphorylation	1431:1462	DNA-PKcs Ser2056 phosphorylation	1431:1462	GENERAL SIGNIFICANCE Given the essential role of DNA-PKcs Ser2056 phosphorylation in the DDR, this study brings data about the role of cell O-GlcNAc level on genome integrity maintenance.
32805318	4	3	theme	HeLa	673:676	arg1	line					683:686	HeLa cell line	673:686	HeLa cell line	673:686	METHODS Using IP techniques, and HeLa cell line, we evaluated the effect of pharmacological or siOGT mediated O-GlcNAc level modulation on DNA-PKcs O-GlcNAcylation.
32805318	4	3	theme	HeLa	673:676	arg1	we					689:690	we	689:690	we	689:690	METHODS Using IP techniques, and HeLa cell line, we evaluated the effect of pharmacological or siOGT mediated O-GlcNAc level modulation on DNA-PKcs O-GlcNAcylation.
32805318	8	4	theme	DNA-PKcs	1339:1346	arg1	modulation					1370:1379	DNA-PKcs O-GlcNAcylation level modulation	1339:1379	DNA-PKcs O-GlcNAcylation level modulation	1339:1379	CONCLUSIONS DNA-PKcs Ser2056 phosphorylation is antagonistically linked to DNA-PKcs O-GlcNAcylation level modulation.
32805318	6	5	dep	RESULTS	928:934	arg1	We					936:937	We	936:937	We	936:937	RESULTS We show here that human DNA-PKcs is an O-GlcNAc modified protein and that this new PTM is responsive to the cell O-GlcNAcylation level modulation.
32805318	2	6	theme	multiple	333:340	arg1	phosphorylations					342:357	multiple phosphorylations	333:357	multiple phosphorylations	333:357	The activity of its catalytic subunit (DNA-PKcs) is regulated by multiple phosphorylations, like the Ser2056 one that impacts DSB end processing and telomeres integrity.
32805318	1	7	theme	repair	252:257	arg1	pathway					259:265	(NHEJ) double strand break (DSB) repair pathway	219:265	(NHEJ) double strand break (DSB) repair pathway	219:265	BACKGROUND DNA dependent Protein Kinase (DNA-PK) is an heterotrimeric complex regulating the Non Homologous End Joining (NHEJ) double strand break (DSB) repair pathway.
32805318	6	8	theme	level	1065:1069	arg1	modulation					1071:1080	the cell O-GlcNAcylation level modulation	1040:1080	the cell O-GlcNAcylation level modulation	1040:1080	RESULTS We show here that human DNA-PKcs is an O-GlcNAc modified protein and that this new PTM is responsive to the cell O-GlcNAcylation level modulation.
32805318	3	9	theme	related	505:511	arg1	PTM					492:494	PTM	492:494	PTM	492:494	O-GlcNAcylation is a post translational modification (PTM) closely related to phosphorylation and its implication in the modulation of DNA-PKcs activity during the DNA Damage Response (DDR) is unknown.
32805318	3	9	theme	related	505:511	arg1	modification					478:489	a post translational modification	457:489	a post translational modification (PTM) closely related to phosphorylation	457:530	O-GlcNAcylation is a post translational modification (PTM) closely related to phosphorylation and its implication in the modulation of DNA-PKcs activity during the DNA Damage Response (DDR) is unknown.
32805318	3	9	theme	related	505:511	arg1	O-GlcNAcylation					438:452	O-GlcNAcylation	438:452	O-GlcNAcylation	438:452	O-GlcNAcylation is a post translational modification (PTM) closely related to phosphorylation and its implication in the modulation of DNA-PKcs activity during the DNA Damage Response (DDR) is unknown.
32805318	3	10	from	implication	540:550	arg1	modulation					559:568	the modulation	555:568	the modulation of DNA-PKcs activity	555:589	O-GlcNAcylation is a post translational modification (PTM) closely related to phosphorylation and its implication in the modulation of DNA-PKcs activity during the DNA Damage Response (DDR) is unknown.
32805318	5	11	theme	modulators	916:925	arg1	effect					897:902	the effect	893:902	the effect of O-GlcNAc modulators	893:925	We used the RPA32 phosphorylation as a DNA-PKcs activity reporter substrate to evaluate the effect of O-GlcNAc modulators.
32805318	7	12	theme	DNA-PKcs	1238:1245	arg1	O-GlcNAcylation					1247:1261	DNA-PKcs O-GlcNAcylation	1238:1261	DNA-PKcs O-GlcNAcylation	1238:1261	Our findings reveal that DNA-PKcs hypo O-GlcNAcylation affects its kinase activity and that the bleomycin-induced Ser2056 phosphorylation, is modulated by DNA-PKcs O-GlcNAcylation.
32805318	4	13	theme	pharmacological	716:730	arg1	modulation					765:774	pharmacological or siOGT mediated O-GlcNAc level modulation	716:774	modulation	765:774	METHODS Using IP techniques, and HeLa cell line, we evaluated the effect of pharmacological or siOGT mediated O-GlcNAc level modulation on DNA-PKcs O-GlcNAcylation.
32805318	9	14	theme	essential	1413:1421	arg1	role					1423:1426	the essential role	1409:1426	the essential role of DNA-PKcs Ser2056 phosphorylation in the DDR	1409:1473	GENERAL SIGNIFICANCE Given the essential role of DNA-PKcs Ser2056 phosphorylation in the DDR, this study brings data about the role of cell O-GlcNAc level on genome integrity maintenance.
32805318	9	15	theme	genome	1540:1545	arg1	maintenance					1557:1567	genome integrity maintenance	1540:1567	genome integrity maintenance	1540:1567	GENERAL SIGNIFICANCE Given the essential role of DNA-PKcs Ser2056 phosphorylation in the DDR, this study brings data about the role of cell O-GlcNAc level on genome integrity maintenance.
32805318	3	16	theme	post	459:462	arg1	PTM					492:494	PTM	492:494	PTM	492:494	O-GlcNAcylation is a post translational modification (PTM) closely related to phosphorylation and its implication in the modulation of DNA-PKcs activity during the DNA Damage Response (DDR) is unknown.
32805318	3	16	theme	post	459:462	arg1	modification					478:489	a post translational modification	457:489	a post translational modification (PTM) closely related to phosphorylation	457:530	O-GlcNAcylation is a post translational modification (PTM) closely related to phosphorylation and its implication in the modulation of DNA-PKcs activity during the DNA Damage Response (DDR) is unknown.
32805318	3	16	theme	post	459:462	arg1	O-GlcNAcylation					438:452	O-GlcNAcylation	438:452	O-GlcNAcylation	438:452	O-GlcNAcylation is a post translational modification (PTM) closely related to phosphorylation and its implication in the modulation of DNA-PKcs activity during the DNA Damage Response (DDR) is unknown.
32805318	1	17	theme	BACKGROUND	99:108	arg1	complex					169:175	an heterotrimeric complex	151:175	an heterotrimeric complex regulating the Non Homologous End Joining (NHEJ) double strand break (DSB) repair pathway	151:265	BACKGROUND DNA dependent Protein Kinase (DNA-PK) is an heterotrimeric complex regulating the Non Homologous End Joining (NHEJ) double strand break (DSB) repair pathway.
32805318	1	17	theme	BACKGROUND	99:108	arg1	DNA-PK					140:145	DNA-PK	140:145	DNA-PK	140:145	BACKGROUND DNA dependent Protein Kinase (DNA-PK) is an heterotrimeric complex regulating the Non Homologous End Joining (NHEJ) double strand break (DSB) repair pathway.
32805318	1	17	theme	BACKGROUND	99:108	arg1	Kinase					132:137	BACKGROUND DNA dependent Protein Kinase	99:137	BACKGROUND DNA dependent Protein Kinase (DNA-PK)	99:146	BACKGROUND DNA dependent Protein Kinase (DNA-PK) is an heterotrimeric complex regulating the Non Homologous End Joining (NHEJ) double strand break (DSB) repair pathway.
32805318	4	18	theme	IP	654:655	arg1	techniques					657:666	IP techniques	654:666	IP techniques	654:666	METHODS Using IP techniques, and HeLa cell line, we evaluated the effect of pharmacological or siOGT mediated O-GlcNAc level modulation on DNA-PKcs O-GlcNAcylation.
32805318	1	19	theme	Non	192:194	arg1	End					207:209	the Non Homologous End	188:209	the Non Homologous End Joining (NHEJ) double strand break (DSB) repair pathway	188:265	BACKGROUND DNA dependent Protein Kinase (DNA-PK) is an heterotrimeric complex regulating the Non Homologous End Joining (NHEJ) double strand break (DSB) repair pathway.
32805318	1	20	theme	DNA	110:112	arg1	complex					169:175	an heterotrimeric complex	151:175	an heterotrimeric complex regulating the Non Homologous End Joining (NHEJ) double strand break (DSB) repair pathway	151:265	BACKGROUND DNA dependent Protein Kinase (DNA-PK) is an heterotrimeric complex regulating the Non Homologous End Joining (NHEJ) double strand break (DSB) repair pathway.
32805318	1	20	theme	DNA	110:112	arg1	DNA-PK					140:145	DNA-PK	140:145	DNA-PK	140:145	BACKGROUND DNA dependent Protein Kinase (DNA-PK) is an heterotrimeric complex regulating the Non Homologous End Joining (NHEJ) double strand break (DSB) repair pathway.
32805318	1	20	theme	DNA	110:112	arg1	Kinase					132:137	BACKGROUND DNA dependent Protein Kinase	99:137	BACKGROUND DNA dependent Protein Kinase (DNA-PK)	99:146	BACKGROUND DNA dependent Protein Kinase (DNA-PK) is an heterotrimeric complex regulating the Non Homologous End Joining (NHEJ) double strand break (DSB) repair pathway.
32805318	6	21	theme	O-GlcNAcylation	1049:1063	arg1	modulation					1071:1080	the cell O-GlcNAcylation level modulation	1040:1080	the cell O-GlcNAcylation level modulation	1040:1080	RESULTS We show here that human DNA-PKcs is an O-GlcNAc modified protein and that this new PTM is responsive to the cell O-GlcNAcylation level modulation.
32805318	1	22	theme	Homologous	196:205	arg1	End					207:209	the Non Homologous End	188:209	the Non Homologous End Joining (NHEJ) double strand break (DSB) repair pathway	188:265	BACKGROUND DNA dependent Protein Kinase (DNA-PK) is an heterotrimeric complex regulating the Non Homologous End Joining (NHEJ) double strand break (DSB) repair pathway.
32805318	0	23	theme	Ser2056	9:15	arg1	auto-phosphorylation					17:36	DNA-PKcs Ser2056 auto-phosphorylation	0:36	DNA-PKcs Ser2056 auto-phosphorylation	0:36	DNA-PKcs Ser2056 auto-phosphorylation is affected by an O-GlcNAcylation/phosphorylation interplay.
32805318	4	24	from	effect	706:711	arg1	O-GlcNAcylation					788:802	DNA-PKcs O-GlcNAcylation	779:802	DNA-PKcs O-GlcNAcylation	779:802	METHODS Using IP techniques, and HeLa cell line, we evaluated the effect of pharmacological or siOGT mediated O-GlcNAc level modulation on DNA-PKcs O-GlcNAcylation.
32805318	1	25	theme	dependent	114:122	arg1	complex					169:175	an heterotrimeric complex	151:175	an heterotrimeric complex regulating the Non Homologous End Joining (NHEJ) double strand break (DSB) repair pathway	151:265	BACKGROUND DNA dependent Protein Kinase (DNA-PK) is an heterotrimeric complex regulating the Non Homologous End Joining (NHEJ) double strand break (DSB) repair pathway.
32805318	1	25	theme	dependent	114:122	arg1	DNA-PK					140:145	DNA-PK	140:145	DNA-PK	140:145	BACKGROUND DNA dependent Protein Kinase (DNA-PK) is an heterotrimeric complex regulating the Non Homologous End Joining (NHEJ) double strand break (DSB) repair pathway.
32805318	1	25	theme	dependent	114:122	arg1	Kinase					132:137	BACKGROUND DNA dependent Protein Kinase	99:137	BACKGROUND DNA dependent Protein Kinase (DNA-PK)	99:146	BACKGROUND DNA dependent Protein Kinase (DNA-PK) is an heterotrimeric complex regulating the Non Homologous End Joining (NHEJ) double strand break (DSB) repair pathway.
32805318	2	26	theme	Ser2056	369:375	arg1	one					377:379	the Ser2056 one	365:379	the Ser2056 one that impacts DSB end processing and telomeres integrity	365:435	The activity of its catalytic subunit (DNA-PKcs) is regulated by multiple phosphorylations, like the Ser2056 one that impacts DSB end processing and telomeres integrity.
32805318	0	27	theme	DNA-PKcs	0:7	arg1	auto-phosphorylation					17:36	DNA-PKcs Ser2056 auto-phosphorylation	0:36	DNA-PKcs Ser2056 auto-phosphorylation	0:36	DNA-PKcs Ser2056 auto-phosphorylation is affected by an O-GlcNAcylation/phosphorylation interplay.
32805318	6	28	theme	human	954:958	arg1	protein					993:999	an O-GlcNAc modified protein	972:999	an O-GlcNAc modified protein	972:999	RESULTS We show here that human DNA-PKcs is an O-GlcNAc modified protein and that this new PTM is responsive to the cell O-GlcNAcylation level modulation.
32805318	6	28	theme	human	954:958	arg1	DNA-PKcs					960:967	human DNA-PKcs	954:967	human DNA-PKcs	954:967	RESULTS We show here that human DNA-PKcs is an O-GlcNAc modified protein and that this new PTM is responsive to the cell O-GlcNAcylation level modulation.
32805318	1	29	theme	Protein	124:130	arg1	complex					169:175	an heterotrimeric complex	151:175	an heterotrimeric complex regulating the Non Homologous End Joining (NHEJ) double strand break (DSB) repair pathway	151:265	BACKGROUND DNA dependent Protein Kinase (DNA-PK) is an heterotrimeric complex regulating the Non Homologous End Joining (NHEJ) double strand break (DSB) repair pathway.
32805318	1	29	theme	Protein	124:130	arg1	DNA-PK					140:145	DNA-PK	140:145	DNA-PK	140:145	BACKGROUND DNA dependent Protein Kinase (DNA-PK) is an heterotrimeric complex regulating the Non Homologous End Joining (NHEJ) double strand break (DSB) repair pathway.
32805318	1	29	theme	Protein	124:130	arg1	Kinase					132:137	BACKGROUND DNA dependent Protein Kinase	99:137	BACKGROUND DNA dependent Protein Kinase (DNA-PK)	99:146	BACKGROUND DNA dependent Protein Kinase (DNA-PK) is an heterotrimeric complex regulating the Non Homologous End Joining (NHEJ) double strand break (DSB) repair pathway.
32805318	5	30	theme	activity	853:860	arg1	phosphorylation					823:837	the RPA32 phosphorylation	813:837	the RPA32 phosphorylation	813:837	We used the RPA32 phosphorylation as a DNA-PKcs activity reporter substrate to evaluate the effect of O-GlcNAc modulators.
32805318	5	30	theme	activity	853:860	arg1	substrate					871:879	a DNA-PKcs activity reporter substrate	842:879	a DNA-PKcs activity reporter substrate	842:879	We used the RPA32 phosphorylation as a DNA-PKcs activity reporter substrate to evaluate the effect of O-GlcNAc modulators.
32805318	5	31	used	used	808:811	arg2	We					805:806	We	805:806	We	805:806	We used the RPA32 phosphorylation as a DNA-PKcs activity reporter substrate to evaluate the effect of O-GlcNAc modulators.
32805318	2	32	theme	subunit	298:304	arg1	activity					272:279	The activity	268:279	The activity of its catalytic subunit (DNA-PKcs)	268:315	The activity of its catalytic subunit (DNA-PKcs) is regulated by multiple phosphorylations, like the Ser2056 one that impacts DSB end processing and telomeres integrity.
32805318	8	33	dep	CONCLUSIONS	1264:1274	arg1	linked					1329:1334	linked	1329:1334	is antagonistically linked to DNA-PKcs O-GlcNAcylation level modulation	1309:1379	CONCLUSIONS DNA-PKcs Ser2056 phosphorylation is antagonistically linked to DNA-PKcs O-GlcNAcylation level modulation.
32805318	8	34	theme	DNA-PKcs	1276:1283	arg1	phosphorylation					1293:1307	DNA-PKcs Ser2056 phosphorylation	1276:1307	DNA-PKcs Ser2056 phosphorylation	1276:1307	CONCLUSIONS DNA-PKcs Ser2056 phosphorylation is antagonistically linked to DNA-PKcs O-GlcNAcylation level modulation.
32805318	7	35	theme	kinase	1150:1155	arg1	activity					1157:1164	its kinase activity	1146:1164	its kinase activity	1146:1164	Our findings reveal that DNA-PKcs hypo O-GlcNAcylation affects its kinase activity and that the bleomycin-induced Ser2056 phosphorylation, is modulated by DNA-PKcs O-GlcNAcylation.
32805318	4	36	theme	mediated	741:748	arg1	modulation					765:774	pharmacological or siOGT mediated O-GlcNAc level modulation	716:774	modulation	765:774	METHODS Using IP techniques, and HeLa cell line, we evaluated the effect of pharmacological or siOGT mediated O-GlcNAc level modulation on DNA-PKcs O-GlcNAcylation.
32805318	2	37	theme	catalytic	288:296	arg1	subunit					298:304	its catalytic subunit	284:304	its catalytic subunit (DNA-PKcs)	284:315	The activity of its catalytic subunit (DNA-PKcs) is regulated by multiple phosphorylations, like the Ser2056 one that impacts DSB end processing and telomeres integrity.
32805318	2	37	theme	catalytic	288:296	arg1	DNA-PKcs					307:314	DNA-PKcs	307:314	DNA-PKcs	307:314	The activity of its catalytic subunit (DNA-PKcs) is regulated by multiple phosphorylations, like the Ser2056 one that impacts DSB end processing and telomeres integrity.
32805318	2	38	theme	end	398:400	arg1	processing					402:411	DSB end processing	394:411	DSB end processing	394:411	The activity of its catalytic subunit (DNA-PKcs) is regulated by multiple phosphorylations, like the Ser2056 one that impacts DSB end processing and telomeres integrity.
32805318	7	39	theme	bleomycin-induced	1179:1195	arg1	phosphorylation					1205:1219	the bleomycin-induced Ser2056 phosphorylation	1175:1219	the bleomycin-induced Ser2056 phosphorylation	1175:1219	Our findings reveal that DNA-PKcs hypo O-GlcNAcylation affects its kinase activity and that the bleomycin-induced Ser2056 phosphorylation, is modulated by DNA-PKcs O-GlcNAcylation.
32805318	9	40	theme	level	1531:1535	arg1	role					1509:1512	the role	1505:1512	the role of cell O-GlcNAc level on genome integrity maintenance	1505:1567	GENERAL SIGNIFICANCE Given the essential role of DNA-PKcs Ser2056 phosphorylation in the DDR, this study brings data about the role of cell O-GlcNAc level on genome integrity maintenance.
32805318	8	41	attach	linked	1329:1334	arg2	phosphorylation					1293:1307	DNA-PKcs Ser2056 phosphorylation	1276:1307	DNA-PKcs Ser2056 phosphorylation	1276:1307	CONCLUSIONS DNA-PKcs Ser2056 phosphorylation is antagonistically linked to DNA-PKcs O-GlcNAcylation level modulation.
32805318	8	41	attach	linked	1329:1334	arg1	modulation					1370:1379	DNA-PKcs O-GlcNAcylation level modulation	1339:1379	DNA-PKcs O-GlcNAcylation level modulation	1339:1379	CONCLUSIONS DNA-PKcs Ser2056 phosphorylation is antagonistically linked to DNA-PKcs O-GlcNAcylation level modulation.
32805318	5	42	theme	RPA32	817:821	arg1	phosphorylation					823:837	the RPA32 phosphorylation	813:837	the RPA32 phosphorylation	813:837	We used the RPA32 phosphorylation as a DNA-PKcs activity reporter substrate to evaluate the effect of O-GlcNAc modulators.
32805318	5	42	theme	RPA32	817:821	arg1	substrate					871:879	a DNA-PKcs activity reporter substrate	842:879	a DNA-PKcs activity reporter substrate	842:879	We used the RPA32 phosphorylation as a DNA-PKcs activity reporter substrate to evaluate the effect of O-GlcNAc modulators.
32805318	8	43	theme	O-GlcNAcylation	1348:1362	arg1	modulation					1370:1379	DNA-PKcs O-GlcNAcylation level modulation	1339:1379	DNA-PKcs O-GlcNAcylation level modulation	1339:1379	CONCLUSIONS DNA-PKcs Ser2056 phosphorylation is antagonistically linked to DNA-PKcs O-GlcNAcylation level modulation.
32805318	2	44	theme	DSB	394:396	arg1	processing					402:411	DSB end processing	394:411	DSB end processing	394:411	The activity of its catalytic subunit (DNA-PKcs) is regulated by multiple phosphorylations, like the Ser2056 one that impacts DSB end processing and telomeres integrity.
32805318	6	45	theme	cell	1044:1047	arg1	modulation					1071:1080	the cell O-GlcNAcylation level modulation	1040:1080	the cell O-GlcNAcylation level modulation	1040:1080	RESULTS We show here that human DNA-PKcs is an O-GlcNAc modified protein and that this new PTM is responsive to the cell O-GlcNAcylation level modulation.
32805318	5	46	theme	DNA-PKcs	844:851	arg1	phosphorylation					823:837	the RPA32 phosphorylation	813:837	the RPA32 phosphorylation	813:837	We used the RPA32 phosphorylation as a DNA-PKcs activity reporter substrate to evaluate the effect of O-GlcNAc modulators.
32805318	5	46	theme	DNA-PKcs	844:851	arg1	substrate					871:879	a DNA-PKcs activity reporter substrate	842:879	a DNA-PKcs activity reporter substrate	842:879	We used the RPA32 phosphorylation as a DNA-PKcs activity reporter substrate to evaluate the effect of O-GlcNAc modulators.
32805318	4	47	theme	DNA-PKcs	779:786	arg1	O-GlcNAcylation					788:802	DNA-PKcs O-GlcNAcylation	779:802	DNA-PKcs O-GlcNAcylation	779:802	METHODS Using IP techniques, and HeLa cell line, we evaluated the effect of pharmacological or siOGT mediated O-GlcNAc level modulation on DNA-PKcs O-GlcNAcylation.
32805318	1	48	theme	double	226:231	arg1	DSB					247:249	DSB	247:249	DSB	247:249	BACKGROUND DNA dependent Protein Kinase (DNA-PK) is an heterotrimeric complex regulating the Non Homologous End Joining (NHEJ) double strand break (DSB) repair pathway.
32805318	1	48	theme	double	226:231	arg1	break					240:244	(NHEJ) double strand break	219:244	(NHEJ) double strand break (DSB) repair pathway	219:265	BACKGROUND DNA dependent Protein Kinase (DNA-PK) is an heterotrimeric complex regulating the Non Homologous End Joining (NHEJ) double strand break (DSB) repair pathway.
32805318	0	49	theme	O-GlcNAcylation/phosphorylation	56:86	arg1	interplay					88:96	an O-GlcNAcylation/phosphorylation interplay	53:96	an O-GlcNAcylation/phosphorylation interplay	53:96	DNA-PKcs Ser2056 auto-phosphorylation is affected by an O-GlcNAcylation/phosphorylation interplay.
32805318	5	50	theme	reporter	862:869	arg1	phosphorylation					823:837	the RPA32 phosphorylation	813:837	the RPA32 phosphorylation	813:837	We used the RPA32 phosphorylation as a DNA-PKcs activity reporter substrate to evaluate the effect of O-GlcNAc modulators.
32805318	5	50	theme	reporter	862:869	arg1	substrate					871:879	a DNA-PKcs activity reporter substrate	842:879	a DNA-PKcs activity reporter substrate	842:879	We used the RPA32 phosphorylation as a DNA-PKcs activity reporter substrate to evaluate the effect of O-GlcNAc modulators.
32805318	1	51	dep	break	240:244	arg1	NHEJ					220:223	NHEJ	220:223	NHEJ	220:223	BACKGROUND DNA dependent Protein Kinase (DNA-PK) is an heterotrimeric complex regulating the Non Homologous End Joining (NHEJ) double strand break (DSB) repair pathway.
32805318	3	52	theme	DNA-PKcs	573:580	arg1	activity					582:589	DNA-PKcs activity	573:589	DNA-PKcs activity	573:589	O-GlcNAcylation is a post translational modification (PTM) closely related to phosphorylation and its implication in the modulation of DNA-PKcs activity during the DNA Damage Response (DDR) is unknown.
32805318	9	53	theme	O-GlcNAc	1522:1529	arg1	level					1531:1535	cell O-GlcNAc level	1517:1535	cell O-GlcNAc level	1517:1535	GENERAL SIGNIFICANCE Given the essential role of DNA-PKcs Ser2056 phosphorylation in the DDR, this study brings data about the role of cell O-GlcNAc level on genome integrity maintenance.
32805318	7	54	theme	hypo	1117:1120	arg1	O-GlcNAcylation					1122:1136	DNA-PKcs hypo O-GlcNAcylation	1108:1136	DNA-PKcs hypo O-GlcNAcylation	1108:1136	Our findings reveal that DNA-PKcs hypo O-GlcNAcylation affects its kinase activity and that the bleomycin-induced Ser2056 phosphorylation, is modulated by DNA-PKcs O-GlcNAcylation.
32805318	3	55	theme	activity	582:589	arg1	modulation					559:568	the modulation	555:568	the modulation of DNA-PKcs activity	555:589	O-GlcNAcylation is a post translational modification (PTM) closely related to phosphorylation and its implication in the modulation of DNA-PKcs activity during the DNA Damage Response (DDR) is unknown.
32805318	7	56	theme	Ser2056	1197:1203	arg1	phosphorylation					1205:1219	the bleomycin-induced Ser2056 phosphorylation	1175:1219	the bleomycin-induced Ser2056 phosphorylation	1175:1219	Our findings reveal that DNA-PKcs hypo O-GlcNAcylation affects its kinase activity and that the bleomycin-induced Ser2056 phosphorylation, is modulated by DNA-PKcs O-GlcNAcylation.
32805318	4	57	theme	cell	678:681	arg1	line					683:686	HeLa cell line	673:686	HeLa cell line	673:686	METHODS Using IP techniques, and HeLa cell line, we evaluated the effect of pharmacological or siOGT mediated O-GlcNAc level modulation on DNA-PKcs O-GlcNAcylation.
32805318	4	57	theme	cell	678:681	arg1	we					689:690	we	689:690	we	689:690	METHODS Using IP techniques, and HeLa cell line, we evaluated the effect of pharmacological or siOGT mediated O-GlcNAc level modulation on DNA-PKcs O-GlcNAcylation.
32805318	4	58	theme	modulation	765:774	arg1	effect					706:711	the effect	702:711	the effect of pharmacological or siOGT mediated O-GlcNAc level modulation on DNA-PKcs O-GlcNAcylation	702:802	METHODS Using IP techniques, and HeLa cell line, we evaluated the effect of pharmacological or siOGT mediated O-GlcNAc level modulation on DNA-PKcs O-GlcNAcylation.
32805318	4	59	theme	level	759:763	arg1	modulation					765:774	pharmacological or siOGT mediated O-GlcNAc level modulation	716:774	modulation	765:774	METHODS Using IP techniques, and HeLa cell line, we evaluated the effect of pharmacological or siOGT mediated O-GlcNAc level modulation on DNA-PKcs O-GlcNAcylation.
32805318	9	60	from	role	1509:1512	arg1	maintenance					1557:1567	genome integrity maintenance	1540:1567	genome integrity maintenance	1540:1567	GENERAL SIGNIFICANCE Given the essential role of DNA-PKcs Ser2056 phosphorylation in the DDR, this study brings data about the role of cell O-GlcNAc level on genome integrity maintenance.
32805318	3	61	theme	translational	464:476	arg1	PTM					492:494	PTM	492:494	PTM	492:494	O-GlcNAcylation is a post translational modification (PTM) closely related to phosphorylation and its implication in the modulation of DNA-PKcs activity during the DNA Damage Response (DDR) is unknown.
32805318	3	61	theme	translational	464:476	arg1	modification					478:489	a post translational modification	457:489	a post translational modification (PTM) closely related to phosphorylation	457:530	O-GlcNAcylation is a post translational modification (PTM) closely related to phosphorylation and its implication in the modulation of DNA-PKcs activity during the DNA Damage Response (DDR) is unknown.
32805318	3	61	theme	translational	464:476	arg1	O-GlcNAcylation					438:452	O-GlcNAcylation	438:452	O-GlcNAcylation	438:452	O-GlcNAcylation is a post translational modification (PTM) closely related to phosphorylation and its implication in the modulation of DNA-PKcs activity during the DNA Damage Response (DDR) is unknown.
32805318	9	62	theme	DNA-PKcs	1431:1438	arg1	phosphorylation					1448:1462	DNA-PKcs Ser2056 phosphorylation	1431:1462	DNA-PKcs Ser2056 phosphorylation	1431:1462	GENERAL SIGNIFICANCE Given the essential role of DNA-PKcs Ser2056 phosphorylation in the DDR, this study brings data about the role of cell O-GlcNAc level on genome integrity maintenance.
32805318	1	63	theme	strand	233:238	arg1	DSB					247:249	DSB	247:249	DSB	247:249	BACKGROUND DNA dependent Protein Kinase (DNA-PK) is an heterotrimeric complex regulating the Non Homologous End Joining (NHEJ) double strand break (DSB) repair pathway.
32805318	1	63	theme	strand	233:238	arg1	break					240:244	(NHEJ) double strand break	219:244	(NHEJ) double strand break (DSB) repair pathway	219:265	BACKGROUND DNA dependent Protein Kinase (DNA-PK) is an heterotrimeric complex regulating the Non Homologous End Joining (NHEJ) double strand break (DSB) repair pathway.
32805318	4	64	theme	siOGT	735:739	arg1	modulation					765:774	pharmacological or siOGT mediated O-GlcNAc level modulation	716:774	modulation	765:774	METHODS Using IP techniques, and HeLa cell line, we evaluated the effect of pharmacological or siOGT mediated O-GlcNAc level modulation on DNA-PKcs O-GlcNAcylation.
32805318	4	65	theme	O-GlcNAc	750:757	arg1	modulation					765:774	pharmacological or siOGT mediated O-GlcNAc level modulation	716:774	modulation	765:774	METHODS Using IP techniques, and HeLa cell line, we evaluated the effect of pharmacological or siOGT mediated O-GlcNAc level modulation on DNA-PKcs O-GlcNAcylation.
32805318	9	66	theme	GENERAL	1382:1388	arg1	SIGNIFICANCE					1390:1401	GENERAL SIGNIFICANCE	1382:1401	GENERAL SIGNIFICANCE	1382:1401	GENERAL SIGNIFICANCE Given the essential role of DNA-PKcs Ser2056 phosphorylation in the DDR, this study brings data about the role of cell O-GlcNAc level on genome integrity maintenance.
32805318	5	67	theme	O-GlcNAc	907:914	arg1	modulators					916:925	O-GlcNAc modulators	907:925	O-GlcNAc modulators	907:925	We used the RPA32 phosphorylation as a DNA-PKcs activity reporter substrate to evaluate the effect of O-GlcNAc modulators.
32805318	1	68	theme	break	240:244	arg1	pathway					259:265	(NHEJ) double strand break (DSB) repair pathway	219:265	(NHEJ) double strand break (DSB) repair pathway	219:265	BACKGROUND DNA dependent Protein Kinase (DNA-PK) is an heterotrimeric complex regulating the Non Homologous End Joining (NHEJ) double strand break (DSB) repair pathway.
32805318	9	69	theme	cell	1517:1520	arg1	level					1531:1535	cell O-GlcNAc level	1517:1535	cell O-GlcNAc level	1517:1535	GENERAL SIGNIFICANCE Given the essential role of DNA-PKcs Ser2056 phosphorylation in the DDR, this study brings data about the role of cell O-GlcNAc level on genome integrity maintenance.
32805318	8	70	theme	Ser2056	1285:1291	arg1	phosphorylation					1293:1307	DNA-PKcs Ser2056 phosphorylation	1276:1307	DNA-PKcs Ser2056 phosphorylation	1276:1307	CONCLUSIONS DNA-PKcs Ser2056 phosphorylation is antagonistically linked to DNA-PKcs O-GlcNAcylation level modulation.
32805318	3	71	theme	DNA	602:604	arg1	Damage					606:611	the DNA Damage	598:611	the DNA Damage Response (DDR)	598:626	O-GlcNAcylation is a post translational modification (PTM) closely related to phosphorylation and its implication in the modulation of DNA-PKcs activity during the DNA Damage Response (DDR) is unknown.
32805318	9	72	theme	integrity	1547:1555	arg1	maintenance					1557:1567	genome integrity maintenance	1540:1567	genome integrity maintenance	1540:1567	GENERAL SIGNIFICANCE Given the essential role of DNA-PKcs Ser2056 phosphorylation in the DDR, this study brings data about the role of cell O-GlcNAc level on genome integrity maintenance.
32805318	1	73	theme	heterotrimeric	154:167	arg1	complex					169:175	an heterotrimeric complex	151:175	an heterotrimeric complex regulating the Non Homologous End Joining (NHEJ) double strand break (DSB) repair pathway	151:265	BACKGROUND DNA dependent Protein Kinase (DNA-PK) is an heterotrimeric complex regulating the Non Homologous End Joining (NHEJ) double strand break (DSB) repair pathway.
32805318	1	73	theme	heterotrimeric	154:167	arg1	Kinase					132:137	BACKGROUND DNA dependent Protein Kinase	99:137	BACKGROUND DNA dependent Protein Kinase (DNA-PK)	99:146	BACKGROUND DNA dependent Protein Kinase (DNA-PK) is an heterotrimeric complex regulating the Non Homologous End Joining (NHEJ) double strand break (DSB) repair pathway.
32805318	9	74	theme	phosphorylation	1448:1462	arg1	role					1423:1426	the essential role	1409:1426	the essential role of DNA-PKcs Ser2056 phosphorylation in the DDR	1409:1473	GENERAL SIGNIFICANCE Given the essential role of DNA-PKcs Ser2056 phosphorylation in the DDR, this study brings data about the role of cell O-GlcNAc level on genome integrity maintenance.
32805318	7	75	theme	DNA-PKcs	1108:1115	arg1	O-GlcNAcylation					1122:1136	DNA-PKcs hypo O-GlcNAcylation	1108:1136	DNA-PKcs hypo O-GlcNAcylation	1108:1136	Our findings reveal that DNA-PKcs hypo O-GlcNAcylation affects its kinase activity and that the bleomycin-induced Ser2056 phosphorylation, is modulated by DNA-PKcs O-GlcNAcylation.
32805318	9	76	dep	SIGNIFICANCE	1390:1401	arg1	role					1423:1426	the essential role	1409:1426	the essential role of DNA-PKcs Ser2056 phosphorylation in the DDR	1409:1473	GENERAL SIGNIFICANCE Given the essential role of DNA-PKcs Ser2056 phosphorylation in the DDR, this study brings data about the role of cell O-GlcNAc level on genome integrity maintenance.
32805318	3	77	theme	Damage	606:611	arg1	DDR					623:625	DDR	623:625	DDR	623:625	O-GlcNAcylation is a post translational modification (PTM) closely related to phosphorylation and its implication in the modulation of DNA-PKcs activity during the DNA Damage Response (DDR) is unknown.
32805318	3	77	theme	Damage	606:611	arg1	Response					613:620	the DNA Damage Response	598:620	the DNA Damage Response (DDR)	598:626	O-GlcNAcylation is a post translational modification (PTM) closely related to phosphorylation and its implication in the modulation of DNA-PKcs activity during the DNA Damage Response (DDR) is unknown.
32805318	6	78	theme	new	1015:1017	arg1	PTM					1019:1021	this new PTM	1010:1021	this new PTM	1010:1021	RESULTS We show here that human DNA-PKcs is an O-GlcNAc modified protein and that this new PTM is responsive to the cell O-GlcNAcylation level modulation.
32805318	6	79	theme	modified	984:991	arg1	protein					993:999	an O-GlcNAc modified protein	972:999	an O-GlcNAc modified protein	972:999	RESULTS We show here that human DNA-PKcs is an O-GlcNAc modified protein and that this new PTM is responsive to the cell O-GlcNAcylation level modulation.
32805318	6	79	theme	modified	984:991	arg1	DNA-PKcs					960:967	human DNA-PKcs	954:967	human DNA-PKcs	954:967	RESULTS We show here that human DNA-PKcs is an O-GlcNAc modified protein and that this new PTM is responsive to the cell O-GlcNAcylation level modulation.
19932102	3	0	theme	FOXO4-dependent	388:402	arg1	response					421:428	the FOXO4-dependent oxidative stress response	384:428	the FOXO4-dependent oxidative stress response	384:428	Here, we demonstrate that O-GlcNAcylation also contributes to the FOXO4-dependent oxidative stress response.
19932102	4	1	theme	peroxide	453:460	arg1	treatment					462:470	hydrogen peroxide treatment	444:470	hydrogen peroxide treatment of HEK293 cells	444:486	We show that hydrogen peroxide treatment of HEK293 cells increases FOXO4 association with OGT, the enzyme that adds O-GlcNAc to proteins, causing FOXO4 O-GlcNAcylation and enhanced transcriptional activity under acute oxidative stress.
19932102	4	2	theme	oxidative	649:657	arg1	stress					659:664	acute oxidative stress	643:664	acute oxidative stress	643:664	We show that hydrogen peroxide treatment of HEK293 cells increases FOXO4 association with OGT, the enzyme that adds O-GlcNAc to proteins, causing FOXO4 O-GlcNAcylation and enhanced transcriptional activity under acute oxidative stress.
19932102	3	3	theme	oxidative	404:412	arg1	response					421:428	the FOXO4-dependent oxidative stress response	384:428	the FOXO4-dependent oxidative stress response	384:428	Here, we demonstrate that O-GlcNAcylation also contributes to the FOXO4-dependent oxidative stress response.
19932102	5	4	theme	stress	725:730	arg1	conditions					732:741	stress conditions	725:741	stress conditions	725:741	O-GlcNAcylation is known to be protective for cells under stress conditions, including oxidative stress.
19932102	1	5	from	survival	144:151	arg1	response					156:163	response	156:163	response to oxidative stress	156:183	The FOXO4 transcription factor plays an important role in cell survival in response to oxidative stress.
19932102	4	6	theme	acute	643:647	arg1	stress					659:664	acute oxidative stress	643:664	acute oxidative stress	643:664	We show that hydrogen peroxide treatment of HEK293 cells increases FOXO4 association with OGT, the enzyme that adds O-GlcNAc to proteins, causing FOXO4 O-GlcNAcylation and enhanced transcriptional activity under acute oxidative stress.
19932102	4	7	theme	hydrogen	444:451	arg1	peroxide					453:460	hydrogen peroxide	444:460	hydrogen peroxide treatment of HEK293 cells	444:486	We show that hydrogen peroxide treatment of HEK293 cells increases FOXO4 association with OGT, the enzyme that adds O-GlcNAc to proteins, causing FOXO4 O-GlcNAcylation and enhanced transcriptional activity under acute oxidative stress.
19932102	1	8	theme	oxidative	168:176	arg1	stress					178:183	oxidative stress	168:183	oxidative stress	168:183	The FOXO4 transcription factor plays an important role in cell survival in response to oxidative stress.
19932102	1	9	theme	FOXO4	85:89	arg1	factor					105:110	The FOXO4 transcription factor	81:110	The FOXO4 transcription factor	81:110	The FOXO4 transcription factor plays an important role in cell survival in response to oxidative stress.
19932102	4	10	with	association	504:514	arg1	OGT					521:523	OGT	521:523	OGT	521:523	We show that hydrogen peroxide treatment of HEK293 cells increases FOXO4 association with OGT, the enzyme that adds O-GlcNAc to proteins, causing FOXO4 O-GlcNAcylation and enhanced transcriptional activity under acute oxidative stress.
19932102	4	10	with	association	504:514	arg1	enzyme					530:535	the enzyme	526:535	the enzyme that adds O-GlcNAc to proteins	526:566	We show that hydrogen peroxide treatment of HEK293 cells increases FOXO4 association with OGT, the enzyme that adds O-GlcNAc to proteins, causing FOXO4 O-GlcNAcylation and enhanced transcriptional activity under acute oxidative stress.
19932102	1	11	theme	transcription	91:103	arg1	factor					105:110	The FOXO4 transcription factor	81:110	The FOXO4 transcription factor	81:110	The FOXO4 transcription factor plays an important role in cell survival in response to oxidative stress.
19932102	0	12	theme	transcriptional	31:45	arg1	regulation					47:56	FOXO4 transcriptional regulation	25:56	FOXO4 transcriptional regulation	25:56	O-GlcNAcylation enhances FOXO4 transcriptional regulation in response to stress.
19932102	3	13	theme	stress	414:419	arg1	response					421:428	the FOXO4-dependent oxidative stress response	384:428	the FOXO4-dependent oxidative stress response	384:428	Here, we demonstrate that O-GlcNAcylation also contributes to the FOXO4-dependent oxidative stress response.
19932102	0	14	theme	FOXO4	25:29	arg1	regulation					47:56	FOXO4 transcriptional regulation	25:56	FOXO4 transcriptional regulation	25:56	O-GlcNAcylation enhances FOXO4 transcriptional regulation in response to stress.
19932102	4	15	theme	transcriptional	612:626	arg1	activity					628:635	enhanced transcriptional activity	603:635	enhanced transcriptional activity	603:635	We show that hydrogen peroxide treatment of HEK293 cells increases FOXO4 association with OGT, the enzyme that adds O-GlcNAc to proteins, causing FOXO4 O-GlcNAcylation and enhanced transcriptional activity under acute oxidative stress.
19932102	4	16	theme	FOXO4	498:502	arg1	association					504:514	FOXO4 association	498:514	FOXO4 association with OGT, the enzyme that adds O-GlcNAc to proteins	498:566	We show that hydrogen peroxide treatment of HEK293 cells increases FOXO4 association with OGT, the enzyme that adds O-GlcNAc to proteins, causing FOXO4 O-GlcNAcylation and enhanced transcriptional activity under acute oxidative stress.
19932102	4	17	theme	enhanced	603:610	arg1	activity					628:635	enhanced transcriptional activity	603:635	enhanced transcriptional activity	603:635	We show that hydrogen peroxide treatment of HEK293 cells increases FOXO4 association with OGT, the enzyme that adds O-GlcNAc to proteins, causing FOXO4 O-GlcNAcylation and enhanced transcriptional activity under acute oxidative stress.
19932102	2	18	theme	post-translational	229:246	arg1	ubiquitination					306:319	ubiquitination	306:319	ubiquitination	306:319	The regulation of FOXO4 is orchestrated by post-translational modifications including phosphorylation, acetylation, and ubiquitination.
19932102	2	18	theme	post-translational	229:246	arg1	phosphorylation					272:286	phosphorylation	272:286	phosphorylation	272:286	The regulation of FOXO4 is orchestrated by post-translational modifications including phosphorylation, acetylation, and ubiquitination.
19932102	2	18	theme	post-translational	229:246	arg1	modifications					248:260	post-translational modifications	229:260	post-translational modifications including phosphorylation, acetylation, and ubiquitination	229:319	The regulation of FOXO4 is orchestrated by post-translational modifications including phosphorylation, acetylation, and ubiquitination.
19932102	2	18	theme	post-translational	229:246	arg1	acetylation					289:299	acetylation	289:299	acetylation	289:299	The regulation of FOXO4 is orchestrated by post-translational modifications including phosphorylation, acetylation, and ubiquitination.
19932102	6	19	theme	protection	825:834	arg1	mechanism					791:799	a mechanism	789:799	a mechanism of FOXO4 anti-oxidative protection through O-GlcNAcylation	789:858	Our data provide a mechanism of FOXO4 anti-oxidative protection through O-GlcNAcylation.
19932102	1	20	theme	important	121:129	arg1	role					131:134	an important role	118:134	an important role	118:134	The FOXO4 transcription factor plays an important role in cell survival in response to oxidative stress.
19932102	4	21	theme	FOXO4	577:581	arg1	O-GlcNAcylation					583:597	FOXO4 O-GlcNAcylation	577:597	FOXO4 O-GlcNAcylation	577:597	We show that hydrogen peroxide treatment of HEK293 cells increases FOXO4 association with OGT, the enzyme that adds O-GlcNAc to proteins, causing FOXO4 O-GlcNAcylation and enhanced transcriptional activity under acute oxidative stress.
19932102	6	22	theme	anti-oxidative	810:823	arg1	protection					825:834	FOXO4 anti-oxidative protection	804:834	FOXO4 anti-oxidative protection	804:834	Our data provide a mechanism of FOXO4 anti-oxidative protection through O-GlcNAcylation.
19932102	2	23	theme	FOXO4	204:208	arg1	regulation					190:199	The regulation	186:199	The regulation of FOXO4	186:208	The regulation of FOXO4 is orchestrated by post-translational modifications including phosphorylation, acetylation, and ubiquitination.
19932102	6	24	theme	FOXO4	804:808	arg1	protection					825:834	FOXO4 anti-oxidative protection	804:834	FOXO4 anti-oxidative protection	804:834	Our data provide a mechanism of FOXO4 anti-oxidative protection through O-GlcNAcylation.
19932102	5	25	theme	oxidative	754:762	arg1	stress					764:769	oxidative stress	754:769	oxidative stress	754:769	O-GlcNAcylation is known to be protective for cells under stress conditions, including oxidative stress.
19932102	4	26	theme	cells	482:486	arg1	treatment					462:470	hydrogen peroxide treatment	444:470	hydrogen peroxide treatment of HEK293 cells	444:486	We show that hydrogen peroxide treatment of HEK293 cells increases FOXO4 association with OGT, the enzyme that adds O-GlcNAc to proteins, causing FOXO4 O-GlcNAcylation and enhanced transcriptional activity under acute oxidative stress.
19932102	1	27	theme	cell	139:142	arg1	survival					144:151	cell survival	139:151	cell survival in response to oxidative stress	139:183	The FOXO4 transcription factor plays an important role in cell survival in response to oxidative stress.
19932102	4	28	theme	HEK293	475:480	arg1	cells					482:486	HEK293 cells	475:486	HEK293 cells	475:486	We show that hydrogen peroxide treatment of HEK293 cells increases FOXO4 association with OGT, the enzyme that adds O-GlcNAc to proteins, causing FOXO4 O-GlcNAcylation and enhanced transcriptional activity under acute oxidative stress.
34487576	9	0	theme	in	1254:1255	arg1	growth					1268:1273	in vivo tumor growth	1254:1273	in vivo tumor growth	1254:1273	Melatonin treatment, inhibition of O-GlcNAcylation by OSMI-1, or mutation of key O-GlcNAc site strongly suppressed in vivo tumor growth.
34487576	1	1	theme	circadian	173:181	arg1	rhythm					183:188	circadian rhythm	173:188	circadian rhythm	173:188	Melatonin helps to maintain circadian rhythm, exerts anticancer activity, and plays key roles in regulation of glucose homeostasis and energy metabolism.
34487576	10	2	theme	CDK5	1416:1419	arg1	O-GlcNAcylation					1397:1411	O-GlcNAcylation	1397:1411	O-GlcNAcylation of CDK5	1397:1419	Our findings indicate that melatonin reduces proliferation and promotes apoptosis of bladder cancer cells by suppressing O-GlcNAcylation of CDK5.
34487576	1	3	theme	glucose	256:262	arg1	homeostasis					264:274	glucose homeostasis	256:274	glucose homeostasis	256:274	Melatonin helps to maintain circadian rhythm, exerts anticancer activity, and plays key roles in regulation of glucose homeostasis and energy metabolism.
34487576	4	4	theme	elevated	534:541	arg1	level					552:556	elevated O-GlcNAc level	534:556	elevated O-GlcNAc level in bladder cancer	534:574	In this study, elevated O-GlcNAc level in bladder cancer was inhibited by melatonin treatment.
34487576	5	5	theme	bladder	698:704	arg1	cells					713:717	bladder cancer cells	698:717	bladder cancer cells	698:717	Melatonin treatment inhibited proliferation and migration and enhanced apoptosis of bladder cancer cells.
34487576	2	6	theme	other	355:359	arg1	monosaccharides					361:375	other monosaccharides	355:375	other monosaccharides	355:375	Glycosylation, a form of metabolic flux from glucose or other monosaccharides, is a common post-translational modification.
34487576	9	7	theme	Melatonin	1139:1147	arg1	treatment					1149:1157	Melatonin treatment	1139:1157	Melatonin treatment	1139:1157	Melatonin treatment, inhibition of O-GlcNAcylation by OSMI-1, or mutation of key O-GlcNAc site strongly suppressed in vivo tumor growth.
34487576	1	8	theme	homeostasis	264:274	arg1	regulation					242:251	regulation	242:251	regulation of glucose homeostasis and energy metabolism	242:296	Melatonin helps to maintain circadian rhythm, exerts anticancer activity, and plays key roles in regulation of glucose homeostasis and energy metabolism.
34487576	5	9	theme	cancer	706:711	arg1	cells					713:717	bladder cancer cells	698:717	bladder cancer cells	698:717	Melatonin treatment inhibited proliferation and migration and enhanced apoptosis of bladder cancer cells.
34487576	8	10	theme	metabolic	1051:1059	arg1	flux					1061:1064	metabolic flux	1051:1064	metabolic flux from glucose to UDP-GlcNAc	1051:1091	The mechanism whereby melatonin suppressed O-GlcNAc level was based on decreased glucose uptake and metabolic flux from glucose to UDP-GlcNAc, and consequent reduction in CDK5 expression.
34487576	8	11	theme	O-GlcNAc	994:1001	arg1	level					1003:1007	O-GlcNAc level	994:1007	O-GlcNAc level	994:1007	The mechanism whereby melatonin suppressed O-GlcNAc level was based on decreased glucose uptake and metabolic flux from glucose to UDP-GlcNAc, and consequent reduction in CDK5 expression.
34487576	9	12	theme	site	1229:1232	arg1	mutation					1204:1211	mutation	1204:1211	mutation of key O-GlcNAc site	1204:1232	Melatonin treatment, inhibition of O-GlcNAcylation by OSMI-1, or mutation of key O-GlcNAc site strongly suppressed in vivo tumor growth.
34487576	9	12	theme	site	1229:1232	arg1	inhibition					1160:1169	inhibition	1160:1169	inhibition of O-GlcNAcylation by OSMI-1	1160:1198	Melatonin treatment, inhibition of O-GlcNAcylation by OSMI-1, or mutation of key O-GlcNAc site strongly suppressed in vivo tumor growth.
34487576	9	12	theme	site	1229:1232	arg1	treatment					1149:1157	Melatonin treatment	1139:1157	Melatonin treatment	1139:1157	Melatonin treatment, inhibition of O-GlcNAcylation by OSMI-1, or mutation of key O-GlcNAc site strongly suppressed in vivo tumor growth.
34487576	5	13	theme	cells	713:717	arg1	apoptosis					685:693	apoptosis	685:693	apoptosis of bladder cancer cells	685:717	Melatonin treatment inhibited proliferation and migration and enhanced apoptosis of bladder cancer cells.
34487576	6	14	from	reduction	748:756	arg1	expression					799:808	cyclin-dependent-like kinase 5 (CDK5) expression	761:808	cyclin-dependent-like kinase 5 (CDK5) expression	761:808	Proteomic analysis revealed reduction in cyclin-dependent-like kinase 5 (CDK5) expression by melatonin.
34487576	6	15	theme	kinase	783:788	arg1	expression					799:808	cyclin-dependent-like kinase 5 (CDK5) expression	761:808	cyclin-dependent-like kinase 5 (CDK5) expression	761:808	Proteomic analysis revealed reduction in cyclin-dependent-like kinase 5 (CDK5) expression by melatonin.
34487576	3	16	theme	cells	512:516	arg1	glycosylation					436:448	Dysregulated glycosylation	423:448	Dysregulated glycosylation	423:448	Dysregulated glycosylation, particularly O-GlcNAcylation, is often a biomarker of cancer cells.
34487576	3	16	theme	cells	512:516	arg1	biomarker					492:500	a biomarker	490:500	a biomarker of cancer cells	490:516	Dysregulated glycosylation, particularly O-GlcNAcylation, is often a biomarker of cancer cells.
34487576	0	17	theme	kinase	135:140	arg1	O-GlcNAcylation					94:108	O-GlcNAcylation	94:108	O-GlcNAcylation of cyclin-dependent-like kinase 5	94:142	Melatonin reduces proliferation and promotes apoptosis of bladder cancer cells by suppressing O-GlcNAcylation of cyclin-dependent-like kinase 5.
34487576	7	18	from	conformation	861:872	arg1	CDK5					903:906	CDK5	903:906	CDK5	903:906	O-GlcNAc modification determined the conformation of critical T-loop domain on CDK5 and further influenced the CDK5 stability.
34487576	2	19	from	glucose	344:350	arg1	Glycosylation					299:311	Glycosylation	299:311	Glycosylation	299:311	Glycosylation, a form of metabolic flux from glucose or other monosaccharides, is a common post-translational modification.
34487576	2	19	from	glucose	344:350	arg1	form					316:319	a form	314:319	a form of metabolic flux from glucose or other monosaccharides	314:375	Glycosylation, a form of metabolic flux from glucose or other monosaccharides, is a common post-translational modification.
34487576	2	19	from	glucose	344:350	arg1	flux					334:337	metabolic flux	324:337	metabolic flux from glucose or other monosaccharides	324:375	Glycosylation, a form of metabolic flux from glucose or other monosaccharides, is a common post-translational modification.
34487576	1	20	theme	anticancer	198:207	arg1	activity					209:216	anticancer activity	198:216	anticancer activity	198:216	Melatonin helps to maintain circadian rhythm, exerts anticancer activity, and plays key roles in regulation of glucose homeostasis and energy metabolism.
34487576	0	21	theme	cyclin-dependent-like	113:133	arg1	kinase					135:140	cyclin-dependent-like kinase 5	113:142	cyclin-dependent-like kinase 5	113:142	Melatonin reduces proliferation and promotes apoptosis of bladder cancer cells by suppressing O-GlcNAcylation of cyclin-dependent-like kinase 5.
34487576	7	22	theme	O-GlcNAc	824:831	arg1	modification					833:844	O-GlcNAc modification	824:844	O-GlcNAc modification	824:844	O-GlcNAc modification determined the conformation of critical T-loop domain on CDK5 and further influenced the CDK5 stability.
34487576	2	23	from	monosaccharides	361:375	arg1	Glycosylation					299:311	Glycosylation	299:311	Glycosylation	299:311	Glycosylation, a form of metabolic flux from glucose or other monosaccharides, is a common post-translational modification.
34487576	2	23	from	monosaccharides	361:375	arg1	form					316:319	a form	314:319	a form of metabolic flux from glucose or other monosaccharides	314:375	Glycosylation, a form of metabolic flux from glucose or other monosaccharides, is a common post-translational modification.
34487576	2	23	from	monosaccharides	361:375	arg1	flux					334:337	metabolic flux	324:337	metabolic flux from glucose or other monosaccharides	324:375	Glycosylation, a form of metabolic flux from glucose or other monosaccharides, is a common post-translational modification.
34487576	10	24	theme	cells	1376:1380	arg1	apoptosis					1348:1356	apoptosis	1348:1356	apoptosis of bladder cancer cells	1348:1380	Our findings indicate that melatonin reduces proliferation and promotes apoptosis of bladder cancer cells by suppressing O-GlcNAcylation of CDK5.
34487576	2	25	theme	post-translational	390:407	arg1	Glycosylation					299:311	Glycosylation	299:311	Glycosylation	299:311	Glycosylation, a form of metabolic flux from glucose or other monosaccharides, is a common post-translational modification.
34487576	2	25	theme	post-translational	390:407	arg1	modification					409:420	a common post-translational modification	381:420	a common post-translational modification	381:420	Glycosylation, a form of metabolic flux from glucose or other monosaccharides, is a common post-translational modification.
34487576	7	26	theme	critical	877:884	arg1	domain					893:898	critical T-loop domain	877:898	critical T-loop domain on CDK5	877:906	O-GlcNAc modification determined the conformation of critical T-loop domain on CDK5 and further influenced the CDK5 stability.
34487576	2	27	theme	metabolic	324:332	arg1	flux					334:337	metabolic flux	324:337	metabolic flux from glucose or other monosaccharides	324:375	Glycosylation, a form of metabolic flux from glucose or other monosaccharides, is a common post-translational modification.
34487576	9	28	theme	O-GlcNAcylation	1174:1188	arg1	mutation					1204:1211	mutation	1204:1211	mutation of key O-GlcNAc site	1204:1232	Melatonin treatment, inhibition of O-GlcNAcylation by OSMI-1, or mutation of key O-GlcNAc site strongly suppressed in vivo tumor growth.
34487576	9	28	theme	O-GlcNAcylation	1174:1188	arg1	inhibition					1160:1169	inhibition	1160:1169	inhibition of O-GlcNAcylation by OSMI-1	1160:1198	Melatonin treatment, inhibition of O-GlcNAcylation by OSMI-1, or mutation of key O-GlcNAc site strongly suppressed in vivo tumor growth.
34487576	9	28	theme	O-GlcNAcylation	1174:1188	arg1	treatment					1149:1157	Melatonin treatment	1139:1157	Melatonin treatment	1139:1157	Melatonin treatment, inhibition of O-GlcNAcylation by OSMI-1, or mutation of key O-GlcNAc site strongly suppressed in vivo tumor growth.
34487576	2	29	theme	common	383:388	arg1	Glycosylation					299:311	Glycosylation	299:311	Glycosylation	299:311	Glycosylation, a form of metabolic flux from glucose or other monosaccharides, is a common post-translational modification.
34487576	2	29	theme	common	383:388	arg1	modification					409:420	a common post-translational modification	381:420	a common post-translational modification	381:420	Glycosylation, a form of metabolic flux from glucose or other monosaccharides, is a common post-translational modification.
34487576	1	30	theme	metabolism	287:296	arg1	regulation					242:251	regulation	242:251	regulation of glucose homeostasis and energy metabolism	242:296	Melatonin helps to maintain circadian rhythm, exerts anticancer activity, and plays key roles in regulation of glucose homeostasis and energy metabolism.
34487576	10	31	theme	bladder	1361:1367	arg1	cells					1376:1380	bladder cancer cells	1361:1380	bladder cancer cells	1361:1380	Our findings indicate that melatonin reduces proliferation and promotes apoptosis of bladder cancer cells by suppressing O-GlcNAcylation of CDK5.
34487576	8	32	theme	consequent	1098:1107	arg1	reduction					1109:1117	consequent reduction	1098:1117	consequent reduction in CDK5 expression	1098:1136	The mechanism whereby melatonin suppressed O-GlcNAc level was based on decreased glucose uptake and metabolic flux from glucose to UDP-GlcNAc, and consequent reduction in CDK5 expression.
34487576	7	33	theme	T-loop	886:891	arg1	domain					893:898	critical T-loop domain	877:898	critical T-loop domain on CDK5	877:906	O-GlcNAc modification determined the conformation of critical T-loop domain on CDK5 and further influenced the CDK5 stability.
34487576	5	34	theme	Melatonin	614:622	arg1	treatment					624:632	Melatonin treatment	614:632	Melatonin treatment	614:632	Melatonin treatment inhibited proliferation and migration and enhanced apoptosis of bladder cancer cells.
34487576	4	35	from	level	552:556	arg1	cancer					569:574	bladder cancer	561:574	bladder cancer	561:574	In this study, elevated O-GlcNAc level in bladder cancer was inhibited by melatonin treatment.
34487576	9	36	dep	in	1254:1255	arg1	vivo					1257:1260	vivo	1257:1260	vivo	1257:1260	Melatonin treatment, inhibition of O-GlcNAcylation by OSMI-1, or mutation of key O-GlcNAc site strongly suppressed in vivo tumor growth.
34487576	8	37	from	reduction	1109:1117	arg1	expression					1127:1136	CDK5 expression	1122:1136	CDK5 expression	1122:1136	The mechanism whereby melatonin suppressed O-GlcNAc level was based on decreased glucose uptake and metabolic flux from glucose to UDP-GlcNAc, and consequent reduction in CDK5 expression.
34487576	6	38	theme	Proteomic	720:728	arg1	analysis					730:737	Proteomic analysis	720:737	Proteomic analysis	720:737	Proteomic analysis revealed reduction in cyclin-dependent-like kinase 5 (CDK5) expression by melatonin.
34487576	8	39	from	uptake	1040:1045	arg1	expression					1127:1136	CDK5 expression	1122:1136	CDK5 expression	1122:1136	The mechanism whereby melatonin suppressed O-GlcNAc level was based on decreased glucose uptake and metabolic flux from glucose to UDP-GlcNAc, and consequent reduction in CDK5 expression.
34487576	6	40	theme	cyclin-dependent-like	761:781	arg1	CDK5					793:796	CDK5	793:796	CDK5	793:796	Proteomic analysis revealed reduction in cyclin-dependent-like kinase 5 (CDK5) expression by melatonin.
34487576	6	40	theme	cyclin-dependent-like	761:781	arg1	kinase					783:788	cyclin-dependent-like kinase 5	761:790	cyclin-dependent-like kinase 5 (CDK5) expression	761:808	Proteomic analysis revealed reduction in cyclin-dependent-like kinase 5 (CDK5) expression by melatonin.
34487576	7	41	from	domain	893:898	arg1	CDK5					903:906	CDK5	903:906	CDK5	903:906	O-GlcNAc modification determined the conformation of critical T-loop domain on CDK5 and further influenced the CDK5 stability.
34487576	4	42	theme	melatonin	593:601	arg1	treatment					603:611	melatonin treatment	593:611	melatonin treatment	593:611	In this study, elevated O-GlcNAc level in bladder cancer was inhibited by melatonin treatment.
34487576	1	43	theme	key	229:231	arg1	roles					233:237	key roles	229:237	key roles	229:237	Melatonin helps to maintain circadian rhythm, exerts anticancer activity, and plays key roles in regulation of glucose homeostasis and energy metabolism.
34487576	0	44	theme	bladder	58:64	arg1	cells					73:77	bladder cancer cells	58:77	bladder cancer cells	58:77	Melatonin reduces proliferation and promotes apoptosis of bladder cancer cells by suppressing O-GlcNAcylation of cyclin-dependent-like kinase 5.
34487576	4	45	theme	O-GlcNAc	543:550	arg1	level					552:556	elevated O-GlcNAc level	534:556	elevated O-GlcNAc level in bladder cancer	534:574	In this study, elevated O-GlcNAc level in bladder cancer was inhibited by melatonin treatment.
34487576	7	46	from	CDK5	903:906	arg1	conformation					861:872	the conformation	857:872	the conformation of critical T-loop domain on CDK5	857:906	O-GlcNAc modification determined the conformation of critical T-loop domain on CDK5 and further influenced the CDK5 stability.
34487576	8	47	from	glucose	1071:1077	arg1	uptake					1040:1045	decreased glucose uptake	1022:1045	decreased glucose uptake	1022:1045	The mechanism whereby melatonin suppressed O-GlcNAc level was based on decreased glucose uptake and metabolic flux from glucose to UDP-GlcNAc, and consequent reduction in CDK5 expression.
34487576	8	47	from	glucose	1071:1077	arg1	reduction					1109:1117	consequent reduction	1098:1117	consequent reduction in CDK5 expression	1098:1136	The mechanism whereby melatonin suppressed O-GlcNAc level was based on decreased glucose uptake and metabolic flux from glucose to UDP-GlcNAc, and consequent reduction in CDK5 expression.
34487576	8	47	from	glucose	1071:1077	arg1	flux					1061:1064	metabolic flux	1051:1064	metabolic flux from glucose to UDP-GlcNAc	1051:1091	The mechanism whereby melatonin suppressed O-GlcNAc level was based on decreased glucose uptake and metabolic flux from glucose to UDP-GlcNAc, and consequent reduction in CDK5 expression.
34487576	3	48	theme	Dysregulated	423:434	arg1	biomarker					492:500	a biomarker	490:500	a biomarker of cancer cells	490:516	Dysregulated glycosylation, particularly O-GlcNAcylation, is often a biomarker of cancer cells.
34487576	3	48	theme	Dysregulated	423:434	arg1	glycosylation					436:448	Dysregulated glycosylation	423:448	Dysregulated glycosylation	423:448	Dysregulated glycosylation, particularly O-GlcNAcylation, is often a biomarker of cancer cells.
34487576	3	48	theme	Dysregulated	423:434	arg1	O-GlcNAcylation					464:478	O-GlcNAcylation	464:478	particularly O-GlcNAcylation	451:478	Dysregulated glycosylation, particularly O-GlcNAcylation, is often a biomarker of cancer cells.
34487576	4	49	theme	bladder	561:567	arg1	cancer					569:574	bladder cancer	561:574	bladder cancer	561:574	In this study, elevated O-GlcNAc level in bladder cancer was inhibited by melatonin treatment.
34487576	9	50	theme	key	1216:1218	arg1	site					1229:1232	key O-GlcNAc site	1216:1232	key O-GlcNAc site	1216:1232	Melatonin treatment, inhibition of O-GlcNAcylation by OSMI-1, or mutation of key O-GlcNAc site strongly suppressed in vivo tumor growth.
34487576	8	51	theme	CDK5	1122:1125	arg1	expression					1127:1136	CDK5 expression	1122:1136	CDK5 expression	1122:1136	The mechanism whereby melatonin suppressed O-GlcNAc level was based on decreased glucose uptake and metabolic flux from glucose to UDP-GlcNAc, and consequent reduction in CDK5 expression.
34487576	10	52	theme	cancer	1369:1374	arg1	cells					1376:1380	bladder cancer cells	1361:1380	bladder cancer cells	1361:1380	Our findings indicate that melatonin reduces proliferation and promotes apoptosis of bladder cancer cells by suppressing O-GlcNAcylation of CDK5.
34487576	9	53	theme	tumor	1262:1266	arg1	growth					1268:1273	in vivo tumor growth	1254:1273	in vivo tumor growth	1254:1273	Melatonin treatment, inhibition of O-GlcNAcylation by OSMI-1, or mutation of key O-GlcNAc site strongly suppressed in vivo tumor growth.
34487576	3	54	theme	cancer	505:510	arg1	cells					512:516	cancer cells	505:516	cancer cells	505:516	Dysregulated glycosylation, particularly O-GlcNAcylation, is often a biomarker of cancer cells.
34487576	9	55	theme	O-GlcNAc	1220:1227	arg1	site					1229:1232	key O-GlcNAc site	1216:1232	key O-GlcNAc site	1216:1232	Melatonin treatment, inhibition of O-GlcNAcylation by OSMI-1, or mutation of key O-GlcNAc site strongly suppressed in vivo tumor growth.
34487576	7	56	theme	domain	893:898	arg1	conformation					861:872	the conformation	857:872	the conformation of critical T-loop domain on CDK5	857:906	O-GlcNAc modification determined the conformation of critical T-loop domain on CDK5 and further influenced the CDK5 stability.
34487576	7	57	theme	CDK5	935:938	arg1	stability					940:948	the CDK5 stability	931:948	the CDK5 stability	931:948	O-GlcNAc modification determined the conformation of critical T-loop domain on CDK5 and further influenced the CDK5 stability.
34487576	8	58	theme	glucose	1032:1038	arg1	uptake					1040:1045	decreased glucose uptake	1022:1045	decreased glucose uptake	1022:1045	The mechanism whereby melatonin suppressed O-GlcNAc level was based on decreased glucose uptake and metabolic flux from glucose to UDP-GlcNAc, and consequent reduction in CDK5 expression.
34487576	2	59	theme	flux	334:337	arg1	Glycosylation					299:311	Glycosylation	299:311	Glycosylation	299:311	Glycosylation, a form of metabolic flux from glucose or other monosaccharides, is a common post-translational modification.
34487576	2	59	theme	flux	334:337	arg1	form					316:319	a form	314:319	a form of metabolic flux from glucose or other monosaccharides	314:375	Glycosylation, a form of metabolic flux from glucose or other monosaccharides, is a common post-translational modification.
34487576	1	60	theme	energy	280:285	arg1	metabolism					287:296	energy metabolism	280:296	energy metabolism	280:296	Melatonin helps to maintain circadian rhythm, exerts anticancer activity, and plays key roles in regulation of glucose homeostasis and energy metabolism.
34487576	8	61	from	flux	1061:1064	arg1	expression					1127:1136	CDK5 expression	1122:1136	CDK5 expression	1122:1136	The mechanism whereby melatonin suppressed O-GlcNAc level was based on decreased glucose uptake and metabolic flux from glucose to UDP-GlcNAc, and consequent reduction in CDK5 expression.
34487576	0	62	theme	cells	73:77	arg1	apoptosis					45:53	apoptosis	45:53	apoptosis of bladder cancer cells	45:77	Melatonin reduces proliferation and promotes apoptosis of bladder cancer cells by suppressing O-GlcNAcylation of cyclin-dependent-like kinase 5.
34487576	8	63	theme	decreased	1022:1030	arg1	uptake					1040:1045	decreased glucose uptake	1022:1045	decreased glucose uptake	1022:1045	The mechanism whereby melatonin suppressed O-GlcNAc level was based on decreased glucose uptake and metabolic flux from glucose to UDP-GlcNAc, and consequent reduction in CDK5 expression.
34487576	0	64	theme	cancer	66:71	arg1	cells					73:77	bladder cancer cells	58:77	bladder cancer cells	58:77	Melatonin reduces proliferation and promotes apoptosis of bladder cancer cells by suppressing O-GlcNAcylation of cyclin-dependent-like kinase 5.
34487576	2	65	from	form	316:319	arg1	glucose					344:350	glucose	344:350	glucose	344:350	Glycosylation, a form of metabolic flux from glucose or other monosaccharides, is a common post-translational modification.
34487576	2	65	from	form	316:319	arg1	monosaccharides					361:375	other monosaccharides	355:375	other monosaccharides	355:375	Glycosylation, a form of metabolic flux from glucose or other monosaccharides, is a common post-translational modification.
27316643	0	0	theme	Intracerebral	84:96	arg1	Hemorrhage					98:107	Intracerebral Hemorrhage	84:107	Intracerebral Hemorrhage	84:107	The O-GlcNAc Modification of CDK5 Involved in Neuronal Apoptosis Following In Vitro Intracerebral Hemorrhage.
27316643	6	1	theme	critical	967:974	arg1	functions					985:993	critical neuronal functions	967:993	critical neuronal functions	967:993	Our findings demonstrated a new role for O-glycosylation in neuronal apoptosis and provided a mechanistic understanding of how glycosylation contributes to critical neuronal functions.
27316643	3	2	from	roles	455:459	arg1	neurons					486:492	neurons	486:492	neurons	486:492	Here we expanded on the functional roles of CDK5 glycosylation in neurons.
27316643	5	3	theme	ICH	806:808	arg1	model					793:797	the cell model	784:797	the cell model of the ICH	784:808	Blocking glycosylation of CDK5 alters cellular function and increases neuronal apoptosis in the cell model of the ICH.
27316643	5	4	theme	Blocking	692:699	arg1	glycosylation					701:713	Blocking glycosylation	692:713	Blocking glycosylation of CDK5	692:721	Blocking glycosylation of CDK5 alters cellular function and increases neuronal apoptosis in the cell model of the ICH.
27316643	4	5	dep	activity	578:585	arg1	response					557:564	response	557:564	response	557:564	We showed that CDK5 was dynamically modified with O-GlcNAc in response to neuronal activity and that glycosylation represses CDK5-dependent apoptosis by impairing its association with p53 pathway.
27316643	6	6	theme	new	839:841	arg1	role					843:846	a new role	837:846	a new role for O-glycosylation in neuronal apoptosis	837:888	Our findings demonstrated a new role for O-glycosylation in neuronal apoptosis and provided a mechanistic understanding of how glycosylation contributes to critical neuronal functions.
27316643	2	7	theme	regulation	408:417	arg1	forms					399:403	additional forms	388:403	additional forms of regulation	388:417	Studies of CDK5 have focused on its phosphorylation, although the diversity of CDK5 functions in the brain suggests additional forms of regulation.
27316643	5	8	theme	cell	788:791	arg1	model					793:797	the cell model	784:797	the cell model of the ICH	784:808	Blocking glycosylation of CDK5 alters cellular function and increases neuronal apoptosis in the cell model of the ICH.
27316643	2	9	dep	brain	373:377	arg1	suggests					379:386	suggests	379:386	suggests additional forms of regulation	379:417	Studies of CDK5 have focused on its phosphorylation, although the diversity of CDK5 functions in the brain suggests additional forms of regulation.
27316643	0	10	theme	O-GlcNAc	4:11	arg1	Modification					13:24	The O-GlcNAc Modification	0:24	The O-GlcNAc Modification of CDK5	0:32	The O-GlcNAc Modification of CDK5 Involved in Neuronal Apoptosis Following In Vitro Intracerebral Hemorrhage.
27316643	4	11	theme	neuronal	569:576	arg1	activity					578:585	neuronal activity	569:585	neuronal activity	569:585	We showed that CDK5 was dynamically modified with O-GlcNAc in response to neuronal activity and that glycosylation represses CDK5-dependent apoptosis by impairing its association with p53 pathway.
27316643	7	12	theme	development	1116:1126	arg1	regulation					1059:1068	the regulation	1055:1068	the regulation of activity-dependent gene expression, neural development, and apoptosis	1055:1141	Moreover, we identified a previously unknown mechanism for the regulation of activity-dependent gene expression, neural development, and apoptosis.
27316643	5	13	gly	glycosylation	701:713	arg1	CDK5					718:721	CDK5	718:721	CDK5	718:721	Blocking glycosylation of CDK5 alters cellular function and increases neuronal apoptosis in the cell model of the ICH.
27316643	2	14	theme	additional	388:397	arg1	forms					399:403	additional forms	388:403	additional forms of regulation	388:417	Studies of CDK5 have focused on its phosphorylation, although the diversity of CDK5 functions in the brain suggests additional forms of regulation.
27316643	4	15	mod	modified	531:538	arg1	CDK5					510:513	CDK5	510:513	CDK5	510:513	We showed that CDK5 was dynamically modified with O-GlcNAc in response to neuronal activity and that glycosylation represses CDK5-dependent apoptosis by impairing its association with p53 pathway.
27316643	4	15	mod	modified	531:538	arg3	O-GlcNAc					545:552	O-GlcNAc	545:552	O-GlcNAc	545:552	We showed that CDK5 was dynamically modified with O-GlcNAc in response to neuronal activity and that glycosylation represses CDK5-dependent apoptosis by impairing its association with p53 pathway.
27316643	7	16	theme	apoptosis	1133:1141	arg1	regulation					1059:1068	the regulation	1055:1068	the regulation of activity-dependent gene expression, neural development, and apoptosis	1055:1141	Moreover, we identified a previously unknown mechanism for the regulation of activity-dependent gene expression, neural development, and apoptosis.
27316643	3	17	theme	glycosylation	469:481	arg1	roles					455:459	the functional roles	440:459	the functional roles of CDK5 glycosylation in neurons	440:492	Here we expanded on the functional roles of CDK5 glycosylation in neurons.
27316643	6	18	theme	mechanistic	905:915	arg1	understanding					917:929	a mechanistic understanding	903:929	a mechanistic understanding of how glycosylation contributes to critical neuronal functions	903:993	Our findings demonstrated a new role for O-glycosylation in neuronal apoptosis and provided a mechanistic understanding of how glycosylation contributes to critical neuronal functions.
27316643	1	19	theme	signaling	211:219	arg1	processes					221:229	signaling processes	211:229	signaling processes	211:229	Contrary to cell cycle-associated cyclin-dependent kinases, CDK5 is best known for its regulation of signaling processes in regulating mammalian CNS development.
27316643	2	20	theme	CDK5	351:354	arg1	diversity					338:346	the diversity	334:346	the diversity of CDK5	334:354	Studies of CDK5 have focused on its phosphorylation, although the diversity of CDK5 functions in the brain suggests additional forms of regulation.
27316643	1	21	theme	processes	221:229	arg1	regulation					197:206	its regulation	193:206	its regulation of signaling processes in regulating mammalian CNS development	193:269	Contrary to cell cycle-associated cyclin-dependent kinases, CDK5 is best known for its regulation of signaling processes in regulating mammalian CNS development.
27316643	6	22	from	role	843:846	arg1	apoptosis					880:888	neuronal apoptosis	871:888	neuronal apoptosis	871:888	Our findings demonstrated a new role for O-glycosylation in neuronal apoptosis and provided a mechanistic understanding of how glycosylation contributes to critical neuronal functions.
27316643	4	23	theme	p53	679:681	arg1	pathway					683:689	p53 pathway	679:689	p53 pathway	679:689	We showed that CDK5 was dynamically modified with O-GlcNAc in response to neuronal activity and that glycosylation represses CDK5-dependent apoptosis by impairing its association with p53 pathway.
27316643	0	24	theme	CDK5	29:32	arg1	Modification					13:24	The O-GlcNAc Modification	0:24	The O-GlcNAc Modification of CDK5	0:32	The O-GlcNAc Modification of CDK5 Involved in Neuronal Apoptosis Following In Vitro Intracerebral Hemorrhage.
27316643	5	25	theme	neuronal	762:769	arg1	apoptosis					771:779	neuronal apoptosis	762:779	neuronal apoptosis in the cell model of the ICH	762:808	Blocking glycosylation of CDK5 alters cellular function and increases neuronal apoptosis in the cell model of the ICH.
27316643	5	26	from	apoptosis	771:779	arg1	model					793:797	the cell model	784:797	the cell model of the ICH	784:808	Blocking glycosylation of CDK5 alters cellular function and increases neuronal apoptosis in the cell model of the ICH.
27316643	7	27	theme	activity-dependent	1073:1090	arg1	expression					1097:1106	activity-dependent gene expression	1073:1106	activity-dependent gene expression	1073:1106	Moreover, we identified a previously unknown mechanism for the regulation of activity-dependent gene expression, neural development, and apoptosis.
27316643	3	28	theme	CDK5	464:467	arg1	glycosylation					469:481	CDK5 glycosylation	464:481	CDK5 glycosylation	464:481	Here we expanded on the functional roles of CDK5 glycosylation in neurons.
27316643	0	29	theme	Neuronal	46:53	arg1	Apoptosis					55:63	Neuronal Apoptosis	46:63	Neuronal Apoptosis	46:63	The O-GlcNAc Modification of CDK5 Involved in Neuronal Apoptosis Following In Vitro Intracerebral Hemorrhage.
27316643	7	30	theme	neural	1109:1114	arg1	development					1116:1126	neural development	1109:1126	neural development	1109:1126	Moreover, we identified a previously unknown mechanism for the regulation of activity-dependent gene expression, neural development, and apoptosis.
27316643	3	31	theme	functional	444:453	arg1	roles					455:459	the functional roles	440:459	the functional roles of CDK5 glycosylation in neurons	440:492	Here we expanded on the functional roles of CDK5 glycosylation in neurons.
27316643	7	32	theme	gene	1092:1095	arg1	expression					1097:1106	activity-dependent gene expression	1073:1106	activity-dependent gene expression	1073:1106	Moreover, we identified a previously unknown mechanism for the regulation of activity-dependent gene expression, neural development, and apoptosis.
27316643	1	33	theme	cell	122:125	arg1	kinases					161:167	cell cycle-associated cyclin-dependent kinases	122:167	cell cycle-associated cyclin-dependent kinases	122:167	Contrary to cell cycle-associated cyclin-dependent kinases, CDK5 is best known for its regulation of signaling processes in regulating mammalian CNS development.
27316643	4	34	theme	CDK5-dependent	620:633	arg1	apoptosis					635:643	CDK5-dependent apoptosis	620:643	CDK5-dependent apoptosis	620:643	We showed that CDK5 was dynamically modified with O-GlcNAc in response to neuronal activity and that glycosylation represses CDK5-dependent apoptosis by impairing its association with p53 pathway.
27316643	5	35	theme	CDK5	718:721	arg1	glycosylation					701:713	Blocking glycosylation	692:713	Blocking glycosylation of CDK5	692:721	Blocking glycosylation of CDK5 alters cellular function and increases neuronal apoptosis in the cell model of the ICH.
27316643	1	36	theme	cycle-associated	127:142	arg1	kinases					161:167	cell cycle-associated cyclin-dependent kinases	122:167	cell cycle-associated cyclin-dependent kinases	122:167	Contrary to cell cycle-associated cyclin-dependent kinases, CDK5 is best known for its regulation of signaling processes in regulating mammalian CNS development.
27316643	7	37	theme	expression	1097:1106	arg1	regulation					1059:1068	the regulation	1055:1068	the regulation of activity-dependent gene expression, neural development, and apoptosis	1055:1141	Moreover, we identified a previously unknown mechanism for the regulation of activity-dependent gene expression, neural development, and apoptosis.
27316643	6	38	theme	neuronal	871:878	arg1	apoptosis					880:888	neuronal apoptosis	871:888	neuronal apoptosis	871:888	Our findings demonstrated a new role for O-glycosylation in neuronal apoptosis and provided a mechanistic understanding of how glycosylation contributes to critical neuronal functions.
27316643	2	39	theme	CDK5	283:286	arg1	Studies					272:278	Studies	272:278	Studies of CDK5	272:286	Studies of CDK5 have focused on its phosphorylation, although the diversity of CDK5 functions in the brain suggests additional forms of regulation.
27316643	1	40	theme	cyclin-dependent	144:159	arg1	kinases					161:167	cell cycle-associated cyclin-dependent kinases	122:167	cell cycle-associated cyclin-dependent kinases	122:167	Contrary to cell cycle-associated cyclin-dependent kinases, CDK5 is best known for its regulation of signaling processes in regulating mammalian CNS development.
27316643	5	41	theme	cellular	730:737	arg1	function					739:746	cellular function	730:746	cellular function	730:746	Blocking glycosylation of CDK5 alters cellular function and increases neuronal apoptosis in the cell model of the ICH.
27316643	4	42	with	association	662:672	arg1	pathway					683:689	p53 pathway	679:689	p53 pathway	679:689	We showed that CDK5 was dynamically modified with O-GlcNAc in response to neuronal activity and that glycosylation represses CDK5-dependent apoptosis by impairing its association with p53 pathway.
27316643	1	43	theme	mammalian	245:253	arg1	development					259:269	mammalian CNS development	245:269	mammalian CNS development	245:269	Contrary to cell cycle-associated cyclin-dependent kinases, CDK5 is best known for its regulation of signaling processes in regulating mammalian CNS development.
27316643	1	44	theme	CNS	255:257	arg1	development					259:269	mammalian CNS development	245:269	mammalian CNS development	245:269	Contrary to cell cycle-associated cyclin-dependent kinases, CDK5 is best known for its regulation of signaling processes in regulating mammalian CNS development.
27316643	6	45	theme	neuronal	976:983	arg1	functions					985:993	critical neuronal functions	967:993	critical neuronal functions	967:993	Our findings demonstrated a new role for O-glycosylation in neuronal apoptosis and provided a mechanistic understanding of how glycosylation contributes to critical neuronal functions.
27316643	7	46	theme	unknown	1033:1039	arg1	mechanism					1041:1049	a previously unknown mechanism	1020:1049	a previously unknown mechanism for the regulation of activity-dependent gene expression, neural development, and apoptosis	1020:1141	Moreover, we identified a previously unknown mechanism for the regulation of activity-dependent gene expression, neural development, and apoptosis.
19383152	2	0	attach	removal	380:386	arg2	O-GlcNAc					391:398	O-GlcNAc	391:398	O-GlcNAc	391:398	The enzymes O-GlcNAc Transferase (Ogt) and O-GlcNAcase (Oga) catalyze, respectively, the attachment and removal of O-GlcNAc to target proteins.
19383152	2	0	attach	removal	380:386	arg1	proteins					410:417	target proteins	403:417	target proteins	403:417	The enzymes O-GlcNAc Transferase (Ogt) and O-GlcNAcase (Oga) catalyze, respectively, the attachment and removal of O-GlcNAc to target proteins.
19383152	12	1	theme	spiel	1786:1790	arg1	ohne					1792:1795	the Pou5f1/Oct4 transcription factor spiel ohne grenzen	1749:1803	the Pou5f1/Oct4 transcription factor spiel ohne grenzen	1749:1803	The cytoskeletal defects resemble those previously reported for embryos lacking function of the Pou5f1/Oct4 transcription factor spiel ohne grenzen.
19383152	4	2	contain	has	657:659	arg2	roles					683:687	additional, unstudied roles	661:687	additional, unstudied roles	661:687	Complete loss of ogt function, however, is lethal to mouse embryonic stem cells, suggesting that the enzyme has additional, unstudied roles in development.
19383152	4	2	contain	has	657:659	arg1	enzyme					650:655	the enzyme	646:655	the enzyme	646:655	Complete loss of ogt function, however, is lethal to mouse embryonic stem cells, suggesting that the enzyme has additional, unstudied roles in development.
19383152	8	3	theme	reduced	1150:1156	arg1	brains					1158:1163	reduced brains	1150:1163	reduced brains at 24 hpf	1150:1173	Each of these treatments results in embryos with shortened body axes and reduced brains at 24 hpf.
19383152	2	4	attach	attachment	365:374	arg2	O-GlcNAc					391:398	O-GlcNAc	391:398	O-GlcNAc	391:398	The enzymes O-GlcNAc Transferase (Ogt) and O-GlcNAcase (Oga) catalyze, respectively, the attachment and removal of O-GlcNAc to target proteins.
19383152	2	4	attach	attachment	365:374	arg1	proteins					410:417	target proteins	403:417	target proteins	403:417	The enzymes O-GlcNAc Transferase (Ogt) and O-GlcNAcase (Oga) catalyze, respectively, the attachment and removal of O-GlcNAc to target proteins.
19383152	11	5	theme	actin	1581:1585	arg1	cytoskeleton					1593:1604	the microtubule and actin based cytoskeleton	1561:1604	cytoskeleton	1593:1604	Overexpression of Ogt and Oga delayed epiboly and caused a severe disorganization of the microtubule and actin based cytoskeleton in the extra-embryonic yolk syncytial layer (YSL).
19383152	13	6	theme	embryonic	1873:1881	arg1	cells					1888:1892	human embryonic stem cells	1867:1892	human embryonic stem cells	1867:1892	Consistent with this, Pou5f1/Oct4 is modified by O-GlcNAc in human embryonic stem cells.
19383152	2	7	dep	enzymes	280:286	arg1	enzymes					280:286	The enzymes	276:286	The enzymes O-GlcNAc Transferase (Ogt) and O-GlcNAcase (Oga)	276:335	The enzymes O-GlcNAc Transferase (Ogt) and O-GlcNAcase (Oga) catalyze, respectively, the attachment and removal of O-GlcNAc to target proteins.
19383152	2	7	dep	enzymes	280:286	arg1	Oga					332:334	Oga	332:334	Oga	332:334	The enzymes O-GlcNAc Transferase (Ogt) and O-GlcNAcase (Oga) catalyze, respectively, the attachment and removal of O-GlcNAc to target proteins.
19383152	2	7	dep	enzymes	280:286	arg1	Ogt					310:312	Ogt	310:312	Ogt	310:312	The enzymes O-GlcNAc Transferase (Ogt) and O-GlcNAcase (Oga) catalyze, respectively, the attachment and removal of O-GlcNAc to target proteins.
19383152	2	7	dep	enzymes	280:286	arg1	O-GlcNAcase					319:329	O-GlcNAcase	319:329	O-GlcNAcase (Oga)	319:335	The enzymes O-GlcNAc Transferase (Ogt) and O-GlcNAcase (Oga) catalyze, respectively, the attachment and removal of O-GlcNAc to target proteins.
19383152	2	7	dep	enzymes	280:286	arg1	Transferase					297:307	O-GlcNAc Transferase	288:307	O-GlcNAc Transferase (Ogt)	288:313	The enzymes O-GlcNAc Transferase (Ogt) and O-GlcNAcase (Oga) catalyze, respectively, the attachment and removal of O-GlcNAc to target proteins.
19383152	11	8	theme	syncytial	1634:1642	arg1	layer					1644:1648	the extra-embryonic yolk syncytial layer	1609:1648	the extra-embryonic yolk syncytial layer (YSL)	1609:1654	Overexpression of Ogt and Oga delayed epiboly and caused a severe disorganization of the microtubule and actin based cytoskeleton in the extra-embryonic yolk syncytial layer (YSL).
19383152	11	8	theme	syncytial	1634:1642	arg1	YSL					1651:1653	YSL	1651:1653	YSL	1651:1653	Overexpression of Ogt and Oga delayed epiboly and caused a severe disorganization of the microtubule and actin based cytoskeleton in the extra-embryonic yolk syncytial layer (YSL).
19383152	3	9	theme	transduction	527:538	arg1	pathway					540:546	the signal transduction pathway	516:546	the signal transduction pathway	516:546	In adult mice, Ogt and Oga attenuate the response to insulin by modifying several components of the signal transduction pathway.
19383152	6	10	theme	different	845:853	arg1	isoforms					865:872	six different enzymatic isoforms	841:872	six different enzymatic isoforms that are expressed maternally and zygotically	841:918	Zebrafish has two ogt genes, encoding six different enzymatic isoforms that are expressed maternally and zygotically.
19383152	10	11	theme	layers	1374:1379	arg1	derivatives					1348:1358	derivatives	1348:1358	derivatives of three germ layers	1348:1379	An extensive marker analysis indicates that derivatives of three germ layers are reduced to variable extents, and the embryos are severely disorganized after gastrulation.
19383152	4	12	theme	stem	618:621	arg1	cells					623:627	mouse embryonic stem cells	602:627	mouse embryonic stem cells	602:627	Complete loss of ogt function, however, is lethal to mouse embryonic stem cells, suggesting that the enzyme has additional, unstudied roles in development.
19383152	13	13	mod	modified	1843:1850	arg1	Pou5f1/Oct4					1828:1838	Pou5f1/Oct4	1828:1838	Pou5f1/Oct4	1828:1838	Consistent with this, Pou5f1/Oct4 is modified by O-GlcNAc in human embryonic stem cells.
19383152	13	13	mod	modified	1843:1850	arg3	O-GlcNAc					1855:1862	O-GlcNAc	1855:1862	O-GlcNAc	1855:1862	Consistent with this, Pou5f1/Oct4 is modified by O-GlcNAc in human embryonic stem cells.
19383152	9	14	theme	fewer	1196:1200	arg1	cells					1202:1206	23% fewer cells	1192:1206	23% fewer cells	1192:1206	The embryos had 23% fewer cells than controls, and displayed increased rates of cell death as early as the mid-gastrula stages.
19383152	1	15	theme	variety	231:237	arg1	activity					212:219	the activity	208:219	the activity of a wide variety of nuclear and cytoplasmic proteins	208:273	BACKGROUND The post-translational addition of the monosaccharide O-linked beta-N-acetylglucosamine (O-GlcNAc) regulates the activity of a wide variety of nuclear and cytoplasmic proteins.
19383152	1	16	theme	nuclear	242:248	arg1	proteins					266:273	nuclear and cytoplasmic proteins	242:273	nuclear and cytoplasmic proteins	242:273	BACKGROUND The post-translational addition of the monosaccharide O-linked beta-N-acetylglucosamine (O-GlcNAc) regulates the activity of a wide variety of nuclear and cytoplasmic proteins.
19383152	7	17	theme	zebrafish	999:1007	arg1	ogt					1009:1011	zebrafish ogt	999:1011	zebrafish ogt	999:1011	RESULTS We manipulated O-GlcNAc levels in zebrafish embryos by overexpressing zebrafish ogt, human oga or by injecting morpholinos against ogt transcripts.
19383152	7	17	theme	zebrafish	999:1007	arg1	oga					1020:1022	human oga	1014:1022	human oga	1014:1022	RESULTS We manipulated O-GlcNAc levels in zebrafish embryos by overexpressing zebrafish ogt, human oga or by injecting morpholinos against ogt transcripts.
19383152	1	18	theme	monosaccharide	138:151	arg1	O-GlcNAc					188:195	O-GlcNAc	188:195	O-GlcNAc	188:195	BACKGROUND The post-translational addition of the monosaccharide O-linked beta-N-acetylglucosamine (O-GlcNAc) regulates the activity of a wide variety of nuclear and cytoplasmic proteins.
19383152	1	18	theme	monosaccharide	138:151	arg1	beta-N-acetylglucosamine					162:185	the monosaccharide O-linked beta-N-acetylglucosamine	134:185	the monosaccharide O-linked beta-N-acetylglucosamine (O-GlcNAc)	134:196	BACKGROUND The post-translational addition of the monosaccharide O-linked beta-N-acetylglucosamine (O-GlcNAc) regulates the activity of a wide variety of nuclear and cytoplasmic proteins.
19383152	2	19	theme	O-GlcNAc	288:295	arg1	enzymes					280:286	The enzymes	276:286	The enzymes O-GlcNAc Transferase (Ogt) and O-GlcNAcase (Oga)	276:335	The enzymes O-GlcNAc Transferase (Ogt) and O-GlcNAcase (Oga) catalyze, respectively, the attachment and removal of O-GlcNAc to target proteins.
19383152	2	19	theme	O-GlcNAc	288:295	arg1	Ogt					310:312	Ogt	310:312	Ogt	310:312	The enzymes O-GlcNAc Transferase (Ogt) and O-GlcNAcase (Oga) catalyze, respectively, the attachment and removal of O-GlcNAc to target proteins.
19383152	2	19	theme	O-GlcNAc	288:295	arg1	Transferase					297:307	O-GlcNAc Transferase	288:307	O-GlcNAc Transferase (Ogt)	288:313	The enzymes O-GlcNAc Transferase (Ogt) and O-GlcNAcase (Oga) catalyze, respectively, the attachment and removal of O-GlcNAc to target proteins.
19383152	1	20	theme	beta-N-acetylglucosamine	162:185	arg1	addition					122:129	The post-translational addition	99:129	The post-translational addition of the monosaccharide O-linked beta-N-acetylglucosamine (O-GlcNAc)	99:196	BACKGROUND The post-translational addition of the monosaccharide O-linked beta-N-acetylglucosamine (O-GlcNAc) regulates the activity of a wide variety of nuclear and cytoplasmic proteins.
19383152	4	21	theme	additional	661:670	arg1	roles					683:687	additional, unstudied roles	661:687	additional, unstudied roles	661:687	Complete loss of ogt function, however, is lethal to mouse embryonic stem cells, suggesting that the enzyme has additional, unstudied roles in development.
19383152	0	22	theme	zebrafish	65:73	arg1	development					75:85	zebrafish development	65:85	zebrafish development	65:85	O-GlcNAc modifications regulate cell survival and epiboly during zebrafish development.
19383152	7	23	theme	zebrafish	963:971	arg1	embryos					973:979	zebrafish embryos	963:979	zebrafish embryos	963:979	RESULTS We manipulated O-GlcNAc levels in zebrafish embryos by overexpressing zebrafish ogt, human oga or by injecting morpholinos against ogt transcripts.
19383152	11	24	theme	Ogt	1494:1496	arg1	Overexpression					1476:1489	Overexpression	1476:1489	Overexpression of Ogt and Oga	1476:1504	Overexpression of Ogt and Oga delayed epiboly and caused a severe disorganization of the microtubule and actin based cytoskeleton in the extra-embryonic yolk syncytial layer (YSL).
19383152	9	25	theme	cell	1256:1259	arg1	death					1261:1265	cell death	1256:1265	cell death	1256:1265	The embryos had 23% fewer cells than controls, and displayed increased rates of cell death as early as the mid-gastrula stages.
19383152	5	26	used	utilized	713:720	arg2	We					705:706	We	705:706	We	705:706	We have utilized zebrafish as a model to determine role of O-GlcNAc modifications in development.
19383152	12	27	theme	cytoskeletal	1661:1672	arg1	defects					1674:1680	The cytoskeletal defects	1657:1680	The cytoskeletal defects	1657:1680	The cytoskeletal defects resemble those previously reported for embryos lacking function of the Pou5f1/Oct4 transcription factor spiel ohne grenzen.
19383152	10	28	theme	variable	1396:1403	arg1	extents					1405:1411	variable extents	1396:1411	variable extents	1396:1411	An extensive marker analysis indicates that derivatives of three germ layers are reduced to variable extents, and the embryos are severely disorganized after gastrulation.
19383152	2	29	dep	attachment	365:374	arg1	the					361:363	the	361:363	the	361:363	The enzymes O-GlcNAc Transferase (Ogt) and O-GlcNAcase (Oga) catalyze, respectively, the attachment and removal of O-GlcNAc to target proteins.
19383152	2	30	theme	target	403:408	arg1	proteins					410:417	target proteins	403:417	target proteins	403:417	The enzymes O-GlcNAc Transferase (Ogt) and O-GlcNAcase (Oga) catalyze, respectively, the attachment and removal of O-GlcNAc to target proteins.
19383152	8	31	with	brains	1158:1163	arg1	axes					1141:1144	shortened body axes	1126:1144	shortened body axes	1126:1144	Each of these treatments results in embryos with shortened body axes and reduced brains at 24 hpf.
19383152	2	32	theme	O-GlcNAc	391:398	arg1	attachment					365:374	attachment	365:374	attachment	365:374	The enzymes O-GlcNAc Transferase (Ogt) and O-GlcNAcase (Oga) catalyze, respectively, the attachment and removal of O-GlcNAc to target proteins.
19383152	2	32	theme	O-GlcNAc	391:398	arg1	removal					380:386	removal	380:386	removal	380:386	The enzymes O-GlcNAc Transferase (Ogt) and O-GlcNAcase (Oga) catalyze, respectively, the attachment and removal of O-GlcNAc to target proteins.
19383152	0	33	theme	O-GlcNAc	0:7	arg1	modifications					9:21	O-GlcNAc modifications	0:21	O-GlcNAc modifications	0:21	O-GlcNAc modifications regulate cell survival and epiboly during zebrafish development.
19383152	9	34	theme	mid-gastrula	1283:1294	arg1	stages					1296:1301	the mid-gastrula stages	1279:1301	the mid-gastrula stages	1279:1301	The embryos had 23% fewer cells than controls, and displayed increased rates of cell death as early as the mid-gastrula stages.
19383152	1	35	theme	post-translational	103:120	arg1	addition					122:129	The post-translational addition	99:129	The post-translational addition of the monosaccharide O-linked beta-N-acetylglucosamine (O-GlcNAc)	99:196	BACKGROUND The post-translational addition of the monosaccharide O-linked beta-N-acetylglucosamine (O-GlcNAc) regulates the activity of a wide variety of nuclear and cytoplasmic proteins.
19383152	4	36	theme	Complete	549:556	arg1	loss					558:561	Complete loss	549:561	Complete loss of ogt function	549:577	Complete loss of ogt function, however, is lethal to mouse embryonic stem cells, suggesting that the enzyme has additional, unstudied roles in development.
19383152	15	37	theme	Spiel	2123:2127	arg1	grenzen/Pou5f1					2134:2147	the transcription factor Spiel ohne grenzen/Pou5f1	2098:2147	the transcription factor Spiel ohne grenzen/Pou5f1	2098:2147	O-GlcNAc modifies the transcription factor Spiel ohne grenzen/Pou5f1 and may regulate its activity.
19383152	14	38	dep	CONCLUSION	1895:1904	arg1	conclude					1909:1916	conclude	1909:1916	conclude that O-GlcNAc modifications control the activity of proteins that regulate apoptosis and epiboly movements, but do not seem to regulate germ layer specification	1909:2077	CONCLUSION We conclude that O-GlcNAc modifications control the activity of proteins that regulate apoptosis and epiboly movements, but do not seem to regulate germ layer specification.
19383152	14	39	theme	germ	2054:2057	arg1	specification					2065:2077	germ layer specification	2054:2077	germ layer specification	2054:2077	CONCLUSION We conclude that O-GlcNAc modifications control the activity of proteins that regulate apoptosis and epiboly movements, but do not seem to regulate germ layer specification.
19383152	15	40	theme	ohne	2129:2132	arg1	grenzen/Pou5f1					2134:2147	the transcription factor Spiel ohne grenzen/Pou5f1	2098:2147	the transcription factor Spiel ohne grenzen/Pou5f1	2098:2147	O-GlcNAc modifies the transcription factor Spiel ohne grenzen/Pou5f1 and may regulate its activity.
19383152	1	41	link	O-linked	153:160	arg1	O-GlcNAc					188:195	O-GlcNAc	188:195	O-GlcNAc	188:195	BACKGROUND The post-translational addition of the monosaccharide O-linked beta-N-acetylglucosamine (O-GlcNAc) regulates the activity of a wide variety of nuclear and cytoplasmic proteins.
19383152	1	41	link	O-linked	153:160	arg1	beta-N-acetylglucosamine					162:185	the monosaccharide O-linked beta-N-acetylglucosamine	134:185	the monosaccharide O-linked beta-N-acetylglucosamine (O-GlcNAc)	134:196	BACKGROUND The post-translational addition of the monosaccharide O-linked beta-N-acetylglucosamine (O-GlcNAc) regulates the activity of a wide variety of nuclear and cytoplasmic proteins.
19383152	11	42	theme	microtubule	1565:1575	arg1	disorganization					1542:1556	a severe disorganization	1533:1556	a severe disorganization of the microtubule and actin based cytoskeleton	1533:1604	Overexpression of Ogt and Oga delayed epiboly and caused a severe disorganization of the microtubule and actin based cytoskeleton in the extra-embryonic yolk syncytial layer (YSL).
19383152	5	43	theme	O-GlcNAc	764:771	arg1	modifications					773:785	O-GlcNAc modifications	764:785	O-GlcNAc modifications	764:785	We have utilized zebrafish as a model to determine role of O-GlcNAc modifications in development.
19383152	6	44	theme	ogt	821:823	arg1	genes					825:829	two ogt genes	817:829	two ogt genes	817:829	Zebrafish has two ogt genes, encoding six different enzymatic isoforms that are expressed maternally and zygotically.
19383152	15	45	theme	factor	2116:2121	arg1	grenzen/Pou5f1					2134:2147	the transcription factor Spiel ohne grenzen/Pou5f1	2098:2147	the transcription factor Spiel ohne grenzen/Pou5f1	2098:2147	O-GlcNAc modifies the transcription factor Spiel ohne grenzen/Pou5f1 and may regulate its activity.
19383152	13	46	with	Consistent	1806:1815	arg1	this					1822:1825	this	1822:1825	this	1822:1825	Consistent with this, Pou5f1/Oct4 is modified by O-GlcNAc in human embryonic stem cells.
19383152	12	47	theme	factor	1779:1784	arg1	ohne					1792:1795	the Pou5f1/Oct4 transcription factor spiel ohne grenzen	1749:1803	the Pou5f1/Oct4 transcription factor spiel ohne grenzen	1749:1803	The cytoskeletal defects resemble those previously reported for embryos lacking function of the Pou5f1/Oct4 transcription factor spiel ohne grenzen.
19383152	11	48	theme	cytoskeleton	1593:1604	arg1	disorganization					1542:1556	a severe disorganization	1533:1556	a severe disorganization of the microtubule and actin based cytoskeleton	1533:1604	Overexpression of Ogt and Oga delayed epiboly and caused a severe disorganization of the microtubule and actin based cytoskeleton in the extra-embryonic yolk syncytial layer (YSL).
19383152	1	49	theme	proteins	266:273	arg1	proteins					266:273	nuclear and cytoplasmic proteins	242:273	nuclear and cytoplasmic proteins	242:273	BACKGROUND The post-translational addition of the monosaccharide O-linked beta-N-acetylglucosamine (O-GlcNAc) regulates the activity of a wide variety of nuclear and cytoplasmic proteins.
19383152	1	49	theme	proteins	266:273	arg1	variety					231:237	a wide variety	224:237	a wide variety of nuclear and cytoplasmic proteins	224:273	BACKGROUND The post-translational addition of the monosaccharide O-linked beta-N-acetylglucosamine (O-GlcNAc) regulates the activity of a wide variety of nuclear and cytoplasmic proteins.
19383152	12	50	theme	ohne	1792:1795	arg1	function					1737:1744	function	1737:1744	function of the Pou5f1/Oct4 transcription factor spiel ohne grenzen	1737:1803	The cytoskeletal defects resemble those previously reported for embryos lacking function of the Pou5f1/Oct4 transcription factor spiel ohne grenzen.
19383152	8	51	with	embryos	1113:1119	arg1	axes					1141:1144	shortened body axes	1126:1144	shortened body axes	1126:1144	Each of these treatments results in embryos with shortened body axes and reduced brains at 24 hpf.
19383152	11	52	theme	yolk	1629:1632	arg1	layer					1644:1648	the extra-embryonic yolk syncytial layer	1609:1648	the extra-embryonic yolk syncytial layer (YSL)	1609:1654	Overexpression of Ogt and Oga delayed epiboly and caused a severe disorganization of the microtubule and actin based cytoskeleton in the extra-embryonic yolk syncytial layer (YSL).
19383152	11	52	theme	yolk	1629:1632	arg1	YSL					1651:1653	YSL	1651:1653	YSL	1651:1653	Overexpression of Ogt and Oga delayed epiboly and caused a severe disorganization of the microtubule and actin based cytoskeleton in the extra-embryonic yolk syncytial layer (YSL).
19383152	10	53	theme	extensive	1307:1315	arg1	analysis					1324:1331	An extensive marker analysis	1304:1331	An extensive marker analysis	1304:1331	An extensive marker analysis indicates that derivatives of three germ layers are reduced to variable extents, and the embryos are severely disorganized after gastrulation.
19383152	3	54	theme	several	494:500	arg1	components					502:511	several components	494:511	several components of the signal transduction pathway	494:546	In adult mice, Ogt and Oga attenuate the response to insulin by modifying several components of the signal transduction pathway.
19383152	8	55	theme	body	1136:1139	arg1	axes					1141:1144	shortened body axes	1126:1144	shortened body axes	1126:1144	Each of these treatments results in embryos with shortened body axes and reduced brains at 24 hpf.
19383152	8	56	from	hpf	1171:1173	arg1	brains					1158:1163	reduced brains	1150:1163	reduced brains at 24 hpf	1150:1173	Each of these treatments results in embryos with shortened body axes and reduced brains at 24 hpf.
19383152	8	56	from	hpf	1171:1173	arg1	embryos					1113:1119	embryos	1113:1119	embryos with shortened body axes	1113:1144	Each of these treatments results in embryos with shortened body axes and reduced brains at 24 hpf.
19383152	4	57	theme	function	570:577	arg1	loss					558:561	Complete loss	549:561	Complete loss of ogt function	549:577	Complete loss of ogt function, however, is lethal to mouse embryonic stem cells, suggesting that the enzyme has additional, unstudied roles in development.
19383152	3	58	theme	pathway	540:546	arg1	components					502:511	several components	494:511	several components of the signal transduction pathway	494:546	In adult mice, Ogt and Oga attenuate the response to insulin by modifying several components of the signal transduction pathway.
19383152	9	59	contain	had	1188:1190	arg2	cells					1202:1206	23% fewer cells	1192:1206	23% fewer cells	1192:1206	The embryos had 23% fewer cells than controls, and displayed increased rates of cell death as early as the mid-gastrula stages.
19383152	9	59	contain	had	1188:1190	arg1	embryos					1180:1186	The embryos	1176:1186	The embryos	1176:1186	The embryos had 23% fewer cells than controls, and displayed increased rates of cell death as early as the mid-gastrula stages.
19383152	12	60	theme	Pou5f1/Oct4	1753:1763	arg1	ohne					1792:1795	the Pou5f1/Oct4 transcription factor spiel ohne grenzen	1749:1803	the Pou5f1/Oct4 transcription factor spiel ohne grenzen	1749:1803	The cytoskeletal defects resemble those previously reported for embryos lacking function of the Pou5f1/Oct4 transcription factor spiel ohne grenzen.
19383152	11	61	theme	Oga	1502:1504	arg1	Overexpression					1476:1489	Overexpression	1476:1489	Overexpression of Ogt and Oga	1476:1504	Overexpression of Ogt and Oga delayed epiboly and caused a severe disorganization of the microtubule and actin based cytoskeleton in the extra-embryonic yolk syncytial layer (YSL).
19383152	3	62	theme	signal	520:525	arg1	pathway					540:546	the signal transduction pathway	516:546	the signal transduction pathway	516:546	In adult mice, Ogt and Oga attenuate the response to insulin by modifying several components of the signal transduction pathway.
19383152	6	63	theme	enzymatic	855:863	arg1	isoforms					865:872	six different enzymatic isoforms	841:872	six different enzymatic isoforms that are expressed maternally and zygotically	841:918	Zebrafish has two ogt genes, encoding six different enzymatic isoforms that are expressed maternally and zygotically.
19383152	11	64	theme	severe	1535:1540	arg1	disorganization					1542:1556	a severe disorganization	1533:1556	a severe disorganization of the microtubule and actin based cytoskeleton	1533:1604	Overexpression of Ogt and Oga delayed epiboly and caused a severe disorganization of the microtubule and actin based cytoskeleton in the extra-embryonic yolk syncytial layer (YSL).
19383152	7	65	theme	ogt	1060:1062	arg1	transcripts					1064:1074	ogt transcripts	1060:1074	ogt transcripts	1060:1074	RESULTS We manipulated O-GlcNAc levels in zebrafish embryos by overexpressing zebrafish ogt, human oga or by injecting morpholinos against ogt transcripts.
19383152	10	66	theme	germ	1369:1372	arg1	layers					1374:1379	three germ layers	1363:1379	three germ layers	1363:1379	An extensive marker analysis indicates that derivatives of three germ layers are reduced to variable extents, and the embryos are severely disorganized after gastrulation.
19383152	1	67	theme	wide	226:229	arg1	proteins					266:273	nuclear and cytoplasmic proteins	242:273	nuclear and cytoplasmic proteins	242:273	BACKGROUND The post-translational addition of the monosaccharide O-linked beta-N-acetylglucosamine (O-GlcNAc) regulates the activity of a wide variety of nuclear and cytoplasmic proteins.
19383152	1	67	theme	wide	226:229	arg1	variety					231:237	a wide variety	224:237	a wide variety of nuclear and cytoplasmic proteins	224:273	BACKGROUND The post-translational addition of the monosaccharide O-linked beta-N-acetylglucosamine (O-GlcNAc) regulates the activity of a wide variety of nuclear and cytoplasmic proteins.
19383152	4	68	theme	embryonic	608:616	arg1	cells					623:627	mouse embryonic stem cells	602:627	mouse embryonic stem cells	602:627	Complete loss of ogt function, however, is lethal to mouse embryonic stem cells, suggesting that the enzyme has additional, unstudied roles in development.
19383152	13	69	theme	stem	1883:1886	arg1	cells					1888:1892	human embryonic stem cells	1867:1892	human embryonic stem cells	1867:1892	Consistent with this, Pou5f1/Oct4 is modified by O-GlcNAc in human embryonic stem cells.
19383152	7	70	theme	human	1014:1018	arg1	ogt					1009:1011	zebrafish ogt	999:1011	zebrafish ogt	999:1011	RESULTS We manipulated O-GlcNAc levels in zebrafish embryos by overexpressing zebrafish ogt, human oga or by injecting morpholinos against ogt transcripts.
19383152	7	70	theme	human	1014:1018	arg1	oga					1020:1022	human oga	1014:1022	human oga	1014:1022	RESULTS We manipulated O-GlcNAc levels in zebrafish embryos by overexpressing zebrafish ogt, human oga or by injecting morpholinos against ogt transcripts.
19383152	9	71	theme	death	1261:1265	arg1	rates					1247:1251	increased rates	1237:1251	increased rates of cell death	1237:1265	The embryos had 23% fewer cells than controls, and displayed increased rates of cell death as early as the mid-gastrula stages.
19383152	1	72	dep	BACKGROUND	88:97	arg1	regulates					198:206	regulates	198:206	regulates the activity of a wide variety of nuclear and cytoplasmic proteins	198:273	BACKGROUND The post-translational addition of the monosaccharide O-linked beta-N-acetylglucosamine (O-GlcNAc) regulates the activity of a wide variety of nuclear and cytoplasmic proteins.
19383152	7	73	dep	manipulated	932:942	arg1	injecting					1030:1038	injecting	1030:1038	injecting morpholinos against ogt transcripts	1030:1074	RESULTS We manipulated O-GlcNAc levels in zebrafish embryos by overexpressing zebrafish ogt, human oga or by injecting morpholinos against ogt transcripts.
19383152	7	73	dep	manipulated	932:942	arg1	overexpressing					984:997	overexpressing	984:997	overexpressing zebrafish ogt, human oga	984:1022	RESULTS We manipulated O-GlcNAc levels in zebrafish embryos by overexpressing zebrafish ogt, human oga or by injecting morpholinos against ogt transcripts.
19383152	1	74	theme	O-linked	153:160	arg1	O-GlcNAc					188:195	O-GlcNAc	188:195	O-GlcNAc	188:195	BACKGROUND The post-translational addition of the monosaccharide O-linked beta-N-acetylglucosamine (O-GlcNAc) regulates the activity of a wide variety of nuclear and cytoplasmic proteins.
19383152	1	74	theme	O-linked	153:160	arg1	beta-N-acetylglucosamine					162:185	the monosaccharide O-linked beta-N-acetylglucosamine	134:185	the monosaccharide O-linked beta-N-acetylglucosamine (O-GlcNAc)	134:196	BACKGROUND The post-translational addition of the monosaccharide O-linked beta-N-acetylglucosamine (O-GlcNAc) regulates the activity of a wide variety of nuclear and cytoplasmic proteins.
19383152	9	75	theme	increased	1237:1245	arg1	rates					1247:1251	increased rates	1237:1251	increased rates of cell death	1237:1265	The embryos had 23% fewer cells than controls, and displayed increased rates of cell death as early as the mid-gastrula stages.
19383152	6	76	contain	has	813:815	arg1	Zebrafish					803:811	Zebrafish	803:811	Zebrafish	803:811	Zebrafish has two ogt genes, encoding six different enzymatic isoforms that are expressed maternally and zygotically.
19383152	6	76	contain	has	813:815	arg2	genes					825:829	two ogt genes	817:829	two ogt genes	817:829	Zebrafish has two ogt genes, encoding six different enzymatic isoforms that are expressed maternally and zygotically.
19383152	13	77	theme	human	1867:1871	arg1	cells					1888:1892	human embryonic stem cells	1867:1892	human embryonic stem cells	1867:1892	Consistent with this, Pou5f1/Oct4 is modified by O-GlcNAc in human embryonic stem cells.
19383152	7	78	dep	RESULTS	921:927	arg1	manipulated					932:942	manipulated	932:942	manipulated O-GlcNAc levels in zebrafish embryos by overexpressing zebrafish ogt, human oga or by injecting morpholinos against ogt transcripts	932:1074	RESULTS We manipulated O-GlcNAc levels in zebrafish embryos by overexpressing zebrafish ogt, human oga or by injecting morpholinos against ogt transcripts.
19383152	5	79	from	role	756:759	arg1	development					790:800	development	790:800	development	790:800	We have utilized zebrafish as a model to determine role of O-GlcNAc modifications in development.
19383152	7	80	theme	O-GlcNAc	944:951	arg1	levels					953:958	O-GlcNAc levels	944:958	O-GlcNAc levels	944:958	RESULTS We manipulated O-GlcNAc levels in zebrafish embryos by overexpressing zebrafish ogt, human oga or by injecting morpholinos against ogt transcripts.
19383152	4	81	dep	additional	661:670	arg1	unstudied					673:681	unstudied	673:681	unstudied	673:681	Complete loss of ogt function, however, is lethal to mouse embryonic stem cells, suggesting that the enzyme has additional, unstudied roles in development.
19383152	5	82	theme	modifications	773:785	arg1	role					756:759	role	756:759	role of O-GlcNAc modifications in development	756:800	We have utilized zebrafish as a model to determine role of O-GlcNAc modifications in development.
19383152	4	83	theme	ogt	566:568	arg1	function					570:577	ogt function	566:577	ogt function	566:577	Complete loss of ogt function, however, is lethal to mouse embryonic stem cells, suggesting that the enzyme has additional, unstudied roles in development.
19383152	14	84	theme	layer	2059:2063	arg1	specification					2065:2077	germ layer specification	2054:2077	germ layer specification	2054:2077	CONCLUSION We conclude that O-GlcNAc modifications control the activity of proteins that regulate apoptosis and epiboly movements, but do not seem to regulate germ layer specification.
19383152	14	85	theme	proteins	1970:1977	arg1	activity					1958:1965	the activity	1954:1965	the activity of proteins that regulate apoptosis and epiboly movements	1954:2023	CONCLUSION We conclude that O-GlcNAc modifications control the activity of proteins that regulate apoptosis and epiboly movements, but do not seem to regulate germ layer specification.
19383152	3	86	theme	adult	423:427	arg1	mice					429:432	adult mice	423:432	adult mice	423:432	In adult mice, Ogt and Oga attenuate the response to insulin by modifying several components of the signal transduction pathway.
19383152	15	87	theme	transcription	2102:2114	arg1	grenzen/Pou5f1					2134:2147	the transcription factor Spiel ohne grenzen/Pou5f1	2098:2147	the transcription factor Spiel ohne grenzen/Pou5f1	2098:2147	O-GlcNAc modifies the transcription factor Spiel ohne grenzen/Pou5f1 and may regulate its activity.
19383152	0	88	dep	cell	32:35	arg1	survival					37:44	survival	37:44	survival	37:44	O-GlcNAc modifications regulate cell survival and epiboly during zebrafish development.
19383152	11	89	theme	based	1587:1591	arg1	cytoskeleton					1593:1604	the microtubule and actin based cytoskeleton	1561:1604	cytoskeleton	1593:1604	Overexpression of Ogt and Oga delayed epiboly and caused a severe disorganization of the microtubule and actin based cytoskeleton in the extra-embryonic yolk syncytial layer (YSL).
19383152	1	90	theme	cytoplasmic	254:264	arg1	proteins					266:273	nuclear and cytoplasmic proteins	242:273	nuclear and cytoplasmic proteins	242:273	BACKGROUND The post-translational addition of the monosaccharide O-linked beta-N-acetylglucosamine (O-GlcNAc) regulates the activity of a wide variety of nuclear and cytoplasmic proteins.
19383152	8	91	theme	shortened	1126:1134	arg1	axes					1141:1144	shortened body axes	1126:1144	shortened body axes	1126:1144	Each of these treatments results in embryos with shortened body axes and reduced brains at 24 hpf.
19383152	14	92	theme	O-GlcNAc	1923:1930	arg1	modifications					1932:1944	O-GlcNAc modifications	1923:1944	O-GlcNAc modifications	1923:1944	CONCLUSION We conclude that O-GlcNAc modifications control the activity of proteins that regulate apoptosis and epiboly movements, but do not seem to regulate germ layer specification.
19383152	12	93	theme	transcription	1765:1777	arg1	ohne					1792:1795	the Pou5f1/Oct4 transcription factor spiel ohne grenzen	1749:1803	the Pou5f1/Oct4 transcription factor spiel ohne grenzen	1749:1803	The cytoskeletal defects resemble those previously reported for embryos lacking function of the Pou5f1/Oct4 transcription factor spiel ohne grenzen.
19383152	4	94	theme	mouse	602:606	arg1	cells					623:627	mouse embryonic stem cells	602:627	mouse embryonic stem cells	602:627	Complete loss of ogt function, however, is lethal to mouse embryonic stem cells, suggesting that the enzyme has additional, unstudied roles in development.
19383152	11	95	theme	extra-embryonic	1613:1627	arg1	layer					1644:1648	the extra-embryonic yolk syncytial layer	1609:1648	the extra-embryonic yolk syncytial layer (YSL)	1609:1654	Overexpression of Ogt and Oga delayed epiboly and caused a severe disorganization of the microtubule and actin based cytoskeleton in the extra-embryonic yolk syncytial layer (YSL).
19383152	11	95	theme	extra-embryonic	1613:1627	arg1	YSL					1651:1653	YSL	1651:1653	YSL	1651:1653	Overexpression of Ogt and Oga delayed epiboly and caused a severe disorganization of the microtubule and actin based cytoskeleton in the extra-embryonic yolk syncytial layer (YSL).
19383152	10	96	theme	marker	1317:1322	arg1	analysis					1324:1331	An extensive marker analysis	1304:1331	An extensive marker analysis	1304:1331	An extensive marker analysis indicates that derivatives of three germ layers are reduced to variable extents, and the embryos are severely disorganized after gastrulation.
30793308	0	0	theme	FOXA1	78:82	arg1	O-GlcNAcylation					84:98	FOXA1 O-GlcNAcylation	78:98	FOXA1 O-GlcNAcylation	78:98	Resistance to bortezomib in breast cancer cells that downregulate Bim through FOXA1 O-GlcNAcylation.
30793308	9	1	dep	dysregulation	1341:1353	arg1	the					1327:1329	the	1327:1329	the	1327:1329	Our results have revealed a new regulatory mechanism that involves O-GlcNAc elevation mediated Bim deficiency, which plays a key role in the apoptotic dysregulation and BTZ resistance in breast cancer cells.
30793308	3	2	theme	breast	462:467	arg1	cancer					469:474	breast cancer	462:474	breast cancer	462:474	The molecular basis of BTZ resistance in breast cancer remains elusive.
30793308	4	3	theme	cellular	529:536	arg1	modification					547:558	cellular O-GlcNAc modification	529:558	cellular O-GlcNAc modification	529:558	In the present study, we found that cellular O-GlcNAc modification was dramatically elevated by BTZ treatment in intrinsic resistant MCF-7 and T47D cells, but not in sensitive MDA-MB-231 cells.
30793308	9	4	theme	key	1315:1317	arg1	role					1319:1322	a key role	1313:1322	a key role	1313:1322	Our results have revealed a new regulatory mechanism that involves O-GlcNAc elevation mediated Bim deficiency, which plays a key role in the apoptotic dysregulation and BTZ resistance in breast cancer cells.
30793308	2	5	with	trials	293:298	arg1	BTZ					305:307	BTZ	305:307	BTZ	305:307	Although clinical trials with BTZ have shown promising results for some types of cancers, but not for some others, including those of the breast.
30793308	9	6	theme	O-GlcNAc	1257:1264	arg1	elevation					1266:1274	O-GlcNAc elevation	1257:1274	O-GlcNAc elevation	1257:1274	Our results have revealed a new regulatory mechanism that involves O-GlcNAc elevation mediated Bim deficiency, which plays a key role in the apoptotic dysregulation and BTZ resistance in breast cancer cells.
30793308	0	7	from	Resistance	0:9	arg1	cells					42:46	breast cancer cells	28:46	breast cancer cells that downregulate Bim through FOXA1 O-GlcNAcylation	28:98	Resistance to bortezomib in breast cancer cells that downregulate Bim through FOXA1 O-GlcNAcylation.
30793308	7	8	theme	FOXA1	969:973	arg1	attenuation					975:985	FOXA1 attenuation	969:985	FOXA1 attenuation	969:985	Further, we demonstrated that FOXA1 attenuation was involved in transcriptional downregulation of proapoptotic Bim and thus suppressed breast cancer cell apoptosis.
30793308	2	9	theme	clinical	284:291	arg1	trials					293:298	clinical trials	284:298	clinical trials with BTZ	284:307	Although clinical trials with BTZ have shown promising results for some types of cancers, but not for some others, including those of the breast.
30793308	8	10	theme	resistant	1173:1181	arg1	cells					1183:1187	resistant cells	1173:1187	resistant cells	1173:1187	Finally, the combination of O-GlcNAc inhibitor L01 to BTZ sensitized resistant cells.
30793308	4	11	theme	O-GlcNAc	538:545	arg1	modification					547:558	cellular O-GlcNAc modification	529:558	cellular O-GlcNAc modification	529:558	In the present study, we found that cellular O-GlcNAc modification was dramatically elevated by BTZ treatment in intrinsic resistant MCF-7 and T47D cells, but not in sensitive MDA-MB-231 cells.
30793308	5	12	theme	progressive	689:699	arg1	increase					701:708	A progressive increase	687:708	A progressive increase in O-GlcNAcylation	687:727	A progressive increase in O-GlcNAcylation characterized the increased acquired resistance of MDA-MB-231-derived cells.
30793308	4	13	theme	sensitive	659:667	arg1	cells					680:684	sensitive MDA-MB-231 cells	659:684	sensitive MDA-MB-231 cells	659:684	In the present study, we found that cellular O-GlcNAc modification was dramatically elevated by BTZ treatment in intrinsic resistant MCF-7 and T47D cells, but not in sensitive MDA-MB-231 cells.
30793308	9	14	from	resistance	1363:1372	arg1	cells					1391:1395	breast cancer cells	1377:1395	breast cancer cells	1377:1395	Our results have revealed a new regulatory mechanism that involves O-GlcNAc elevation mediated Bim deficiency, which plays a key role in the apoptotic dysregulation and BTZ resistance in breast cancer cells.
30793308	4	15	theme	BTZ	589:591	arg1	treatment					593:601	BTZ treatment	589:601	BTZ treatment	589:601	In the present study, we found that cellular O-GlcNAc modification was dramatically elevated by BTZ treatment in intrinsic resistant MCF-7 and T47D cells, but not in sensitive MDA-MB-231 cells.
30793308	4	16	theme	T47D	636:639	arg1	cells					641:645	intrinsic resistant MCF-7 and T47D cells	606:645	cells	641:645	In the present study, we found that cellular O-GlcNAc modification was dramatically elevated by BTZ treatment in intrinsic resistant MCF-7 and T47D cells, but not in sensitive MDA-MB-231 cells.
30793308	6	17	theme	pioneer	883:889	arg1	FOXA1					898:902	breast cancer related pioneer factor FOXA1	861:902	breast cancer related pioneer factor FOXA1	861:902	We showed that elevated O-GlcNAc subsequently modified breast cancer related pioneer factor FOXA1 and reduced its protein stability.
30793308	5	18	theme	increased	747:755	arg1	resistance					766:775	the increased acquired resistance	743:775	the increased acquired resistance of MDA-MB-231-derived cells	743:803	A progressive increase in O-GlcNAcylation characterized the increased acquired resistance of MDA-MB-231-derived cells.
30793308	9	19	theme	new	1218:1220	arg1	mechanism					1233:1241	a new regulatory mechanism	1216:1241	a new regulatory mechanism that involves O-GlcNAc elevation mediated Bim deficiency, which plays a key role in the apoptotic dysregulation and BTZ resistance in breast cancer cells	1216:1395	Our results have revealed a new regulatory mechanism that involves O-GlcNAc elevation mediated Bim deficiency, which plays a key role in the apoptotic dysregulation and BTZ resistance in breast cancer cells.
30793308	9	20	from	dysregulation	1341:1353	arg1	cells					1391:1395	breast cancer cells	1377:1395	breast cancer cells	1377:1395	Our results have revealed a new regulatory mechanism that involves O-GlcNAc elevation mediated Bim deficiency, which plays a key role in the apoptotic dysregulation and BTZ resistance in breast cancer cells.
30793308	4	21	theme	resistant	616:624	arg1	MCF-7					626:630	intrinsic resistant MCF-7 and T47D cells	606:645	MCF-7	626:630	In the present study, we found that cellular O-GlcNAc modification was dramatically elevated by BTZ treatment in intrinsic resistant MCF-7 and T47D cells, but not in sensitive MDA-MB-231 cells.
30793308	5	22	theme	MDA-MB-231-derived	780:797	arg1	cells					799:803	MDA-MB-231-derived cells	780:803	MDA-MB-231-derived cells	780:803	A progressive increase in O-GlcNAcylation characterized the increased acquired resistance of MDA-MB-231-derived cells.
30793308	6	23	theme	related	875:881	arg1	FOXA1					898:902	breast cancer related pioneer factor FOXA1	861:902	breast cancer related pioneer factor FOXA1	861:902	We showed that elevated O-GlcNAc subsequently modified breast cancer related pioneer factor FOXA1 and reduced its protein stability.
30793308	9	24	theme	regulatory	1222:1231	arg1	mechanism					1233:1241	a new regulatory mechanism	1216:1241	a new regulatory mechanism that involves O-GlcNAc elevation mediated Bim deficiency, which plays a key role in the apoptotic dysregulation and BTZ resistance in breast cancer cells	1216:1395	Our results have revealed a new regulatory mechanism that involves O-GlcNAc elevation mediated Bim deficiency, which plays a key role in the apoptotic dysregulation and BTZ resistance in breast cancer cells.
30793308	6	25	theme	factor	891:896	arg1	FOXA1					898:902	breast cancer related pioneer factor FOXA1	861:902	breast cancer related pioneer factor FOXA1	861:902	We showed that elevated O-GlcNAc subsequently modified breast cancer related pioneer factor FOXA1 and reduced its protein stability.
30793308	1	26	theme	clinical	171:178	arg1	therapy					180:186	the clinical therapy	167:186	the clinical therapy	167:186	Bortezomib (BTZ), a well-established proteasome inhibitor used in the clinical therapy, leads the modulation of several biological alterations and in turn induces apoptosis.
30793308	5	27	theme	cells	799:803	arg1	resistance					766:775	the increased acquired resistance	743:775	the increased acquired resistance of MDA-MB-231-derived cells	743:803	A progressive increase in O-GlcNAcylation characterized the increased acquired resistance of MDA-MB-231-derived cells.
30793308	6	28	theme	breast	861:866	arg1	cancer					868:873	breast cancer	861:873	breast cancer	861:873	We showed that elevated O-GlcNAc subsequently modified breast cancer related pioneer factor FOXA1 and reduced its protein stability.
30793308	9	29	theme	BTZ	1359:1361	arg1	resistance					1363:1372	BTZ resistance	1359:1372	BTZ resistance	1359:1372	Our results have revealed a new regulatory mechanism that involves O-GlcNAc elevation mediated Bim deficiency, which plays a key role in the apoptotic dysregulation and BTZ resistance in breast cancer cells.
30793308	7	30	theme	cell	1088:1091	arg1	apoptosis					1093:1101	breast cancer cell apoptosis	1074:1101	breast cancer cell apoptosis	1074:1101	Further, we demonstrated that FOXA1 attenuation was involved in transcriptional downregulation of proapoptotic Bim and thus suppressed breast cancer cell apoptosis.
30793308	3	31	theme	molecular	425:433	arg1	basis					435:439	The molecular basis	421:439	The molecular basis of BTZ resistance in breast cancer	421:474	The molecular basis of BTZ resistance in breast cancer remains elusive.
30793308	1	32	theme	well-established	121:136	arg1	Bortezomib					101:110	Bortezomib	101:110	Bortezomib (BTZ)	101:116	Bortezomib (BTZ), a well-established proteasome inhibitor used in the clinical therapy, leads the modulation of several biological alterations and in turn induces apoptosis.
30793308	1	32	theme	well-established	121:136	arg1	inhibitor					149:157	a well-established proteasome inhibitor	119:157	a well-established proteasome inhibitor used in the clinical therapy	119:186	Bortezomib (BTZ), a well-established proteasome inhibitor used in the clinical therapy, leads the modulation of several biological alterations and in turn induces apoptosis.
30793308	0	33	theme	cancer	35:40	arg1	cells					42:46	breast cancer cells	28:46	breast cancer cells that downregulate Bim through FOXA1 O-GlcNAcylation	28:98	Resistance to bortezomib in breast cancer cells that downregulate Bim through FOXA1 O-GlcNAcylation.
30793308	7	34	theme	breast	1074:1079	arg1	cancer					1081:1086	breast cancer	1074:1086	breast cancer cell apoptosis	1074:1101	Further, we demonstrated that FOXA1 attenuation was involved in transcriptional downregulation of proapoptotic Bim and thus suppressed breast cancer cell apoptosis.
30793308	5	35	from	increase	701:708	arg1	O-GlcNAcylation					713:727	O-GlcNAcylation	713:727	O-GlcNAcylation	713:727	A progressive increase in O-GlcNAcylation characterized the increased acquired resistance of MDA-MB-231-derived cells.
30793308	4	36	theme	intrinsic	606:614	arg1	MCF-7					626:630	intrinsic resistant MCF-7 and T47D cells	606:645	MCF-7	626:630	In the present study, we found that cellular O-GlcNAc modification was dramatically elevated by BTZ treatment in intrinsic resistant MCF-7 and T47D cells, but not in sensitive MDA-MB-231 cells.
30793308	0	37	theme	breast	28:33	arg1	cells					42:46	breast cancer cells	28:46	breast cancer cells that downregulate Bim through FOXA1 O-GlcNAcylation	28:98	Resistance to bortezomib in breast cancer cells that downregulate Bim through FOXA1 O-GlcNAcylation.
30793308	9	38	theme	breast	1377:1382	arg1	cells					1391:1395	breast cancer cells	1377:1395	breast cancer cells	1377:1395	Our results have revealed a new regulatory mechanism that involves O-GlcNAc elevation mediated Bim deficiency, which plays a key role in the apoptotic dysregulation and BTZ resistance in breast cancer cells.
30793308	5	39	theme	acquired	757:764	arg1	resistance					766:775	the increased acquired resistance	743:775	the increased acquired resistance of MDA-MB-231-derived cells	743:803	A progressive increase in O-GlcNAcylation characterized the increased acquired resistance of MDA-MB-231-derived cells.
30793308	9	40	theme	cancer	1384:1389	arg1	cells					1391:1395	breast cancer cells	1377:1395	breast cancer cells	1377:1395	Our results have revealed a new regulatory mechanism that involves O-GlcNAc elevation mediated Bim deficiency, which plays a key role in the apoptotic dysregulation and BTZ resistance in breast cancer cells.
30793308	7	41	theme	proapoptotic	1037:1048	arg1	Bim					1050:1052	proapoptotic Bim	1037:1052	proapoptotic Bim	1037:1052	Further, we demonstrated that FOXA1 attenuation was involved in transcriptional downregulation of proapoptotic Bim and thus suppressed breast cancer cell apoptosis.
30793308	3	42	theme	resistance	448:457	arg1	basis					435:439	The molecular basis	421:439	The molecular basis of BTZ resistance in breast cancer	421:474	The molecular basis of BTZ resistance in breast cancer remains elusive.
30793308	7	43	theme	cancer	1081:1086	arg1	apoptosis					1093:1101	breast cancer cell apoptosis	1074:1101	breast cancer cell apoptosis	1074:1101	Further, we demonstrated that FOXA1 attenuation was involved in transcriptional downregulation of proapoptotic Bim and thus suppressed breast cancer cell apoptosis.
30793308	4	44	theme	present	500:506	arg1	study					508:512	the present study	496:512	the present study	496:512	In the present study, we found that cellular O-GlcNAc modification was dramatically elevated by BTZ treatment in intrinsic resistant MCF-7 and T47D cells, but not in sensitive MDA-MB-231 cells.
30793308	9	45	theme	Bim	1285:1287	arg1	deficiency					1289:1298	Bim deficiency	1285:1298	Bim deficiency	1285:1298	Our results have revealed a new regulatory mechanism that involves O-GlcNAc elevation mediated Bim deficiency, which plays a key role in the apoptotic dysregulation and BTZ resistance in breast cancer cells.
30793308	7	46	theme	transcriptional	1003:1017	arg1	downregulation					1019:1032	transcriptional downregulation	1003:1032	transcriptional downregulation of proapoptotic Bim	1003:1052	Further, we demonstrated that FOXA1 attenuation was involved in transcriptional downregulation of proapoptotic Bim and thus suppressed breast cancer cell apoptosis.
30793308	9	47	theme	apoptotic	1331:1339	arg1	dysregulation					1341:1353	apoptotic dysregulation	1331:1353	apoptotic dysregulation	1331:1353	Our results have revealed a new regulatory mechanism that involves O-GlcNAc elevation mediated Bim deficiency, which plays a key role in the apoptotic dysregulation and BTZ resistance in breast cancer cells.
30793308	7	48	theme	Bim	1050:1052	arg1	downregulation					1019:1032	transcriptional downregulation	1003:1032	transcriptional downregulation of proapoptotic Bim	1003:1052	Further, we demonstrated that FOXA1 attenuation was involved in transcriptional downregulation of proapoptotic Bim and thus suppressed breast cancer cell apoptosis.
30793308	6	49	theme	elevated	821:828	arg1	O-GlcNAc					830:837	elevated O-GlcNAc	821:837	elevated O-GlcNAc	821:837	We showed that elevated O-GlcNAc subsequently modified breast cancer related pioneer factor FOXA1 and reduced its protein stability.
30793308	3	50	from	basis	435:439	arg1	cancer					469:474	breast cancer	462:474	breast cancer	462:474	The molecular basis of BTZ resistance in breast cancer remains elusive.
30793308	2	51	theme	promising	320:328	arg1	results					330:336	promising results	320:336	promising results	320:336	Although clinical trials with BTZ have shown promising results for some types of cancers, but not for some others, including those of the breast.
30793308	2	51	theme	promising	320:328	arg1	those					400:404	those	400:404	those	400:404	Although clinical trials with BTZ have shown promising results for some types of cancers, but not for some others, including those of the breast.
30793308	8	52	theme	O-GlcNAc	1132:1139	arg1	L01					1151:1153	O-GlcNAc inhibitor L01	1132:1153	O-GlcNAc inhibitor L01	1132:1153	Finally, the combination of O-GlcNAc inhibitor L01 to BTZ sensitized resistant cells.
30793308	8	53	theme	inhibitor	1141:1149	arg1	L01					1151:1153	O-GlcNAc inhibitor L01	1132:1153	O-GlcNAc inhibitor L01	1132:1153	Finally, the combination of O-GlcNAc inhibitor L01 to BTZ sensitized resistant cells.
30793308	4	54	theme	MDA-MB-231	669:678	arg1	cells					680:684	sensitive MDA-MB-231 cells	659:684	sensitive MDA-MB-231 cells	659:684	In the present study, we found that cellular O-GlcNAc modification was dramatically elevated by BTZ treatment in intrinsic resistant MCF-7 and T47D cells, but not in sensitive MDA-MB-231 cells.
30793308	1	55	theme	several	213:219	arg1	alterations					232:242	several biological alterations	213:242	several biological alterations	213:242	Bortezomib (BTZ), a well-established proteasome inhibitor used in the clinical therapy, leads the modulation of several biological alterations and in turn induces apoptosis.
30793308	5	56	link	MDA-MB-231-derived	780:797	arg1	cells					799:803	MDA-MB-231-derived cells	780:803	MDA-MB-231-derived cells	780:803	A progressive increase in O-GlcNAcylation characterized the increased acquired resistance of MDA-MB-231-derived cells.
30793308	2	57	theme	cancers	356:362	arg1	types					347:351	some types	342:351	some types of cancers	342:362	Although clinical trials with BTZ have shown promising results for some types of cancers, but not for some others, including those of the breast.
30793308	3	58	theme	BTZ	444:446	arg1	resistance					448:457	BTZ resistance	444:457	BTZ resistance	444:457	The molecular basis of BTZ resistance in breast cancer remains elusive.
30793308	1	59	theme	biological	221:230	arg1	alterations					232:242	several biological alterations	213:242	several biological alterations	213:242	Bortezomib (BTZ), a well-established proteasome inhibitor used in the clinical therapy, leads the modulation of several biological alterations and in turn induces apoptosis.
30793308	8	60	theme	L01	1151:1153	arg1	combination					1117:1127	the combination	1113:1127	the combination of O-GlcNAc inhibitor L01 to BTZ	1113:1160	Finally, the combination of O-GlcNAc inhibitor L01 to BTZ sensitized resistant cells.
30793308	6	61	theme	protein	920:926	arg1	stability					928:936	its protein stability	916:936	its protein stability	916:936	We showed that elevated O-GlcNAc subsequently modified breast cancer related pioneer factor FOXA1 and reduced its protein stability.
30793308	1	62	dep	leads	189:193	arg1	induces					256:262	induces	256:262	induces apoptosis	256:272	Bortezomib (BTZ), a well-established proteasome inhibitor used in the clinical therapy, leads the modulation of several biological alterations and in turn induces apoptosis.
30793308	1	63	theme	proteasome	138:147	arg1	Bortezomib					101:110	Bortezomib	101:110	Bortezomib (BTZ)	101:116	Bortezomib (BTZ), a well-established proteasome inhibitor used in the clinical therapy, leads the modulation of several biological alterations and in turn induces apoptosis.
30793308	1	63	theme	proteasome	138:147	arg1	inhibitor					149:157	a well-established proteasome inhibitor	119:157	a well-established proteasome inhibitor used in the clinical therapy	119:186	Bortezomib (BTZ), a well-established proteasome inhibitor used in the clinical therapy, leads the modulation of several biological alterations and in turn induces apoptosis.
30793308	1	64	theme	alterations	232:242	arg1	modulation					199:208	the modulation	195:208	the modulation of several biological alterations	195:242	Bortezomib (BTZ), a well-established proteasome inhibitor used in the clinical therapy, leads the modulation of several biological alterations and in turn induces apoptosis.
29167312	9	0	theme	potential	1731:1739	arg1	utility					1741:1747	its potential utility	1727:1747	its potential utility as a safe and effective adjuvant for MCL	1727:1788	Remarkably, ketoconazole strongly enhances bortezomib-induced apoptosis in de novo bortezomib-resistant MCL cells and in patient-derived primary cells with minimal cytotoxic effect on normal peripheral blood mononuclear cells and hepatocytes, suggesting its potential utility as a safe and effective adjuvant for MCL.
29167312	3	1	theme	proteins	515:522	arg1	sensor					556:561	an ideal sensor	547:561	an ideal sensor for nutritional changes mediated by O-GlcNAc transferase (OGT)	547:624	Posttranslational modification of proteins via O-GlcNAcylation is an ideal sensor for nutritional changes mediated by O-GlcNAc transferase (OGT) and is removed by O-GlcNAcase (OGA).
29167312	3	1	theme	proteins	515:522	arg1	modification					499:510	Posttranslational modification	481:510	Posttranslational modification of proteins via O-GlcNAcylation	481:542	Posttranslational modification of proteins via O-GlcNAcylation is an ideal sensor for nutritional changes mediated by O-GlcNAc transferase (OGT) and is removed by O-GlcNAcase (OGA).
29167312	10	2	theme	novel	1822:1826	arg1	evidence					1828:1835	novel evidence that combination of bortezomib and ketoconazole or other OGA inhibitors may present a promising strategy for the treatment of drug-resistant MCL	1822:1980	novel evidence that combination of bortezomib and ketoconazole or other OGA inhibitors may present a promising strategy for the treatment of drug-resistant MCL	1822:1980	Together, our findings provide novel evidence that combination of bortezomib and ketoconazole or other OGA inhibitors may present a promising strategy for the treatment of drug-resistant MCL.
29167312	0	3	theme	Truncated	130:138	arg1	Bid					140:142	Truncated Bid	130:142	Truncated Bid	130:142	Inhibition of O-GlcNAcase Sensitizes Apoptosis and Reverses Bortezomib Resistance in Mantle Cell Lymphoma through Modification of Truncated Bid.
29167312	6	4	theme	sensitizing	1077:1087	arg1	effect					1089:1094	similar sensitizing effect	1069:1094	similar sensitizing effect	1069:1094	To identify the potential clinical candidates, we tested MCL response to drug-like OGA inhibitor, ketoconazole, and verified that it exerts similar sensitizing effect on bortezomib-induced apoptosis.
29167312	5	5	theme	MGEA5	831:835	arg1	interference					815:826	CRISPR interference	808:826	CRISPR interference of MGEA5 (encoding OGA)	808:850	CRISPR interference of MGEA5 (encoding OGA) validated the apoptosis sensitization by O-GlcNAcylation and OGA inhibition.
29167312	6	6	theme	clinical	955:962	arg1	candidates					964:973	the potential clinical candidates	941:973	the potential clinical candidates	941:973	To identify the potential clinical candidates, we tested MCL response to drug-like OGA inhibitor, ketoconazole, and verified that it exerts similar sensitizing effect on bortezomib-induced apoptosis.
29167312	10	7	theme	OGA	1894:1896	arg1	inhibitors					1898:1907	other OGA inhibitors	1888:1907	other OGA inhibitors	1888:1907	Together, our findings provide novel evidence that combination of bortezomib and ketoconazole or other OGA inhibitors may present a promising strategy for the treatment of drug-resistant MCL.
29167312	1	8	theme	aggressive	232:241	arg1	behaviors					243:251	numerous aggressive behaviors	223:251	numerous aggressive behaviors	223:251	Aberrant energy metabolism represents a hallmark of cancer and contributes to numerous aggressive behaviors of cancer cells, including cell death and survival.
29167312	1	8	theme	aggressive	232:241	arg1	survival					295:302	survival	295:302	survival	295:302	Aberrant energy metabolism represents a hallmark of cancer and contributes to numerous aggressive behaviors of cancer cells, including cell death and survival.
29167312	1	8	theme	aggressive	232:241	arg1	death					285:289	cell death	280:289	cell death	280:289	Aberrant energy metabolism represents a hallmark of cancer and contributes to numerous aggressive behaviors of cancer cells, including cell death and survival.
29167312	12	9	theme	©2017	2015:2019	arg1	AACR					2021:2024	©2017 AACR	2015:2024	©2017 AACR.	2015:2025	©2017 AACR.
29167312	0	10	from	Resistance	71:80	arg1	Lymphoma					97:104	Mantle Cell Lymphoma	85:104	Mantle Cell Lymphoma	85:104	Inhibition of O-GlcNAcase Sensitizes Apoptosis and Reverses Bortezomib Resistance in Mantle Cell Lymphoma through Modification of Truncated Bid.
29167312	6	11	theme	bortezomib-induced	1099:1116	arg1	apoptosis					1118:1126	bortezomib-induced apoptosis	1099:1126	bortezomib-induced apoptosis	1099:1126	To identify the potential clinical candidates, we tested MCL response to drug-like OGA inhibitor, ketoconazole, and verified that it exerts similar sensitizing effect on bortezomib-induced apoptosis.
29167312	3	12	theme	O-GlcNAc	599:606	arg1	transferase					608:618	O-GlcNAc transferase	599:618	O-GlcNAc transferase (OGT)	599:624	Posttranslational modification of proteins via O-GlcNAcylation is an ideal sensor for nutritional changes mediated by O-GlcNAc transferase (OGT) and is removed by O-GlcNAcase (OGA).
29167312	3	12	theme	O-GlcNAc	599:606	arg1	OGT					621:623	OGT	621:623	OGT	621:623	Posttranslational modification of proteins via O-GlcNAcylation is an ideal sensor for nutritional changes mediated by O-GlcNAc transferase (OGT) and is removed by O-GlcNAcase (OGA).
29167312	9	13	theme	bortezomib-resistant	1556:1575	arg1	cells					1581:1585	de novo bortezomib-resistant MCL cells	1548:1585	de novo bortezomib-resistant MCL cells	1548:1585	Remarkably, ketoconazole strongly enhances bortezomib-induced apoptosis in de novo bortezomib-resistant MCL cells and in patient-derived primary cells with minimal cytotoxic effect on normal peripheral blood mononuclear cells and hepatocytes, suggesting its potential utility as a safe and effective adjuvant for MCL.
29167312	1	14	theme	Aberrant	145:152	arg1	metabolism					161:170	Aberrant energy metabolism	145:170	Aberrant energy metabolism	145:170	Aberrant energy metabolism represents a hallmark of cancer and contributes to numerous aggressive behaviors of cancer cells, including cell death and survival.
29167312	9	15	from	effect	1647:1652	arg1	cells					1693:1697	normal peripheral blood mononuclear cells	1657:1697	normal peripheral blood mononuclear cells	1657:1697	Remarkably, ketoconazole strongly enhances bortezomib-induced apoptosis in de novo bortezomib-resistant MCL cells and in patient-derived primary cells with minimal cytotoxic effect on normal peripheral blood mononuclear cells and hepatocytes, suggesting its potential utility as a safe and effective adjuvant for MCL.
29167312	9	15	from	effect	1647:1652	arg1	hepatocytes					1703:1713	hepatocytes	1703:1713	hepatocytes	1703:1713	Remarkably, ketoconazole strongly enhances bortezomib-induced apoptosis in de novo bortezomib-resistant MCL cells and in patient-derived primary cells with minimal cytotoxic effect on normal peripheral blood mononuclear cells and hepatocytes, suggesting its potential utility as a safe and effective adjuvant for MCL.
29167312	4	16	theme	small-molecule	677:690	arg1	inhibitors					692:701	various small-molecule inhibitors	669:701	various small-molecule inhibitors of OGT and OGA	669:716	Using various small-molecule inhibitors of OGT and OGA, we found for the first time that O-GlcNAcylation potentiates MCL response to bortezomib.
29167312	6	17	theme	drug-like	1002:1010	arg1	ketoconazole					1027:1038	ketoconazole	1027:1038	ketoconazole	1027:1038	To identify the potential clinical candidates, we tested MCL response to drug-like OGA inhibitor, ketoconazole, and verified that it exerts similar sensitizing effect on bortezomib-induced apoptosis.
29167312	6	17	theme	drug-like	1002:1010	arg1	inhibitor					1016:1024	drug-like OGA inhibitor	1002:1024	drug-like OGA inhibitor	1002:1024	To identify the potential clinical candidates, we tested MCL response to drug-like OGA inhibitor, ketoconazole, and verified that it exerts similar sensitizing effect on bortezomib-induced apoptosis.
29167312	0	18	theme	Mantle	85:90	arg1	Lymphoma					97:104	Mantle Cell Lymphoma	85:104	Mantle Cell Lymphoma	85:104	Inhibition of O-GlcNAcase Sensitizes Apoptosis and Reverses Bortezomib Resistance in Mantle Cell Lymphoma through Modification of Truncated Bid.
29167312	9	19	theme	primary	1610:1616	arg1	cells					1618:1622	patient-derived primary cells	1594:1622	patient-derived primary cells with minimal cytotoxic effect on normal peripheral blood mononuclear cells and hepatocytes	1594:1713	Remarkably, ketoconazole strongly enhances bortezomib-induced apoptosis in de novo bortezomib-resistant MCL cells and in patient-derived primary cells with minimal cytotoxic effect on normal peripheral blood mononuclear cells and hepatocytes, suggesting its potential utility as a safe and effective adjuvant for MCL.
29167312	9	20	theme	cytotoxic	1637:1645	arg1	effect					1647:1652	minimal cytotoxic effect	1629:1652	minimal cytotoxic effect on normal peripheral blood mononuclear cells and hepatocytes	1629:1713	Remarkably, ketoconazole strongly enhances bortezomib-induced apoptosis in de novo bortezomib-resistant MCL cells and in patient-derived primary cells with minimal cytotoxic effect on normal peripheral blood mononuclear cells and hepatocytes, suggesting its potential utility as a safe and effective adjuvant for MCL.
29167312	2	21	theme	MCL	443:445	arg1	cells					447:451	MCL cells	443:451	MCL cells	443:451	Despite the poor prognosis of mantle cell lymphoma (MCL), due to the inevitable development of drug resistance, metabolic reprograming of MCL cells remains an unexplored area.
29167312	0	22	theme	O-GlcNAcase	14:24	arg1	Inhibition					0:9	Inhibition	0:9	Inhibition of O-GlcNAcase	0:24	Inhibition of O-GlcNAcase Sensitizes Apoptosis and Reverses Bortezomib Resistance in Mantle Cell Lymphoma through Modification of Truncated Bid.
29167312	9	23	theme	peripheral	1664:1673	arg1	cells					1693:1697	normal peripheral blood mononuclear cells	1657:1697	normal peripheral blood mononuclear cells	1657:1697	Remarkably, ketoconazole strongly enhances bortezomib-induced apoptosis in de novo bortezomib-resistant MCL cells and in patient-derived primary cells with minimal cytotoxic effect on normal peripheral blood mononuclear cells and hepatocytes, suggesting its potential utility as a safe and effective adjuvant for MCL.
29167312	1	24	theme	energy	154:159	arg1	metabolism					161:170	Aberrant energy metabolism	145:170	Aberrant energy metabolism	145:170	Aberrant energy metabolism represents a hallmark of cancer and contributes to numerous aggressive behaviors of cancer cells, including cell death and survival.
29167312	2	25	theme	unexplored	464:473	arg1	area					475:478	an unexplored area	461:478	an unexplored area	461:478	Despite the poor prognosis of mantle cell lymphoma (MCL), due to the inevitable development of drug resistance, metabolic reprograming of MCL cells remains an unexplored area.
29167312	8	26	theme	tBid	1424:1427	arg1	ubiquitination					1429:1442	tBid ubiquitination	1424:1442	tBid ubiquitination	1424:1442	Not only does ketoconazole potentiate tBid induction, but also increases tBid stability through O-GlcNAcylation that interferes with tBid ubiquitination and proteasomal degradation.
29167312	2	27	theme	drug	400:403	arg1	resistance					405:414	drug resistance	400:414	drug resistance	400:414	Despite the poor prognosis of mantle cell lymphoma (MCL), due to the inevitable development of drug resistance, metabolic reprograming of MCL cells remains an unexplored area.
29167312	9	28	theme	mononuclear	1681:1691	arg1	cells					1693:1697	normal peripheral blood mononuclear cells	1657:1697	normal peripheral blood mononuclear cells	1657:1697	Remarkably, ketoconazole strongly enhances bortezomib-induced apoptosis in de novo bortezomib-resistant MCL cells and in patient-derived primary cells with minimal cytotoxic effect on normal peripheral blood mononuclear cells and hepatocytes, suggesting its potential utility as a safe and effective adjuvant for MCL.
29167312	3	29	theme	Posttranslational	481:497	arg1	sensor					556:561	an ideal sensor	547:561	an ideal sensor for nutritional changes mediated by O-GlcNAc transferase (OGT)	547:624	Posttranslational modification of proteins via O-GlcNAcylation is an ideal sensor for nutritional changes mediated by O-GlcNAc transferase (OGT) and is removed by O-GlcNAcase (OGA).
29167312	3	29	theme	Posttranslational	481:497	arg1	modification					499:510	Posttranslational modification	481:510	Posttranslational modification of proteins via O-GlcNAcylation	481:542	Posttranslational modification of proteins via O-GlcNAcylation is an ideal sensor for nutritional changes mediated by O-GlcNAc transferase (OGT) and is removed by O-GlcNAcase (OGA).
29167312	7	30	theme	underlying	1153:1162	arg1	mechanisms					1174:1183	the underlying molecular mechanisms	1149:1183	the underlying molecular mechanisms	1149:1183	Investigations into the underlying molecular mechanisms reveal that bortezomib and ketoconazole act in concert to cause the accumulation of truncated Bid (tBid).
29167312	10	31	theme	MCL	1978:1980	arg1	treatment					1950:1958	the treatment	1946:1958	the treatment of drug-resistant MCL	1946:1980	Together, our findings provide novel evidence that combination of bortezomib and ketoconazole or other OGA inhibitors may present a promising strategy for the treatment of drug-resistant MCL.
29167312	4	32	theme	MCL	780:782	arg1	response					784:791	MCL response	780:791	MCL response to bortezomib	780:805	Using various small-molecule inhibitors of OGT and OGA, we found for the first time that O-GlcNAcylation potentiates MCL response to bortezomib.
29167312	2	33	theme	cell	342:345	arg1	lymphoma					347:354	mantle cell lymphoma	335:354	mantle cell lymphoma (MCL)	335:360	Despite the poor prognosis of mantle cell lymphoma (MCL), due to the inevitable development of drug resistance, metabolic reprograming of MCL cells remains an unexplored area.
29167312	2	33	theme	cell	342:345	arg1	MCL					357:359	MCL	357:359	MCL	357:359	Despite the poor prognosis of mantle cell lymphoma (MCL), due to the inevitable development of drug resistance, metabolic reprograming of MCL cells remains an unexplored area.
29167312	4	34	theme	various	669:675	arg1	inhibitors					692:701	various small-molecule inhibitors	669:701	various small-molecule inhibitors of OGT and OGA	669:716	Using various small-molecule inhibitors of OGT and OGA, we found for the first time that O-GlcNAcylation potentiates MCL response to bortezomib.
29167312	1	35	theme	cancer	256:261	arg1	cells					263:267	cancer cells	256:267	cancer cells	256:267	Aberrant energy metabolism represents a hallmark of cancer and contributes to numerous aggressive behaviors of cancer cells, including cell death and survival.
29167312	5	36	theme	OGA	913:915	arg1	inhibition					917:926	OGA inhibition	913:926	OGA inhibition	913:926	CRISPR interference of MGEA5 (encoding OGA) validated the apoptosis sensitization by O-GlcNAcylation and OGA inhibition.
29167312	7	37	theme	truncated	1269:1277	arg1	Bid					1279:1281	truncated Bid	1269:1281	truncated Bid (tBid)	1269:1288	Investigations into the underlying molecular mechanisms reveal that bortezomib and ketoconazole act in concert to cause the accumulation of truncated Bid (tBid).
29167312	7	37	theme	truncated	1269:1277	arg1	tBid					1284:1287	tBid	1284:1287	tBid	1284:1287	Investigations into the underlying molecular mechanisms reveal that bortezomib and ketoconazole act in concert to cause the accumulation of truncated Bid (tBid).
29167312	3	38	theme	ideal	550:554	arg1	sensor					556:561	an ideal sensor	547:561	an ideal sensor for nutritional changes mediated by O-GlcNAc transferase (OGT)	547:624	Posttranslational modification of proteins via O-GlcNAcylation is an ideal sensor for nutritional changes mediated by O-GlcNAc transferase (OGT) and is removed by O-GlcNAcase (OGA).
29167312	3	38	theme	ideal	550:554	arg1	modification					499:510	Posttranslational modification	481:510	Posttranslational modification of proteins via O-GlcNAcylation	481:542	Posttranslational modification of proteins via O-GlcNAcylation is an ideal sensor for nutritional changes mediated by O-GlcNAc transferase (OGT) and is removed by O-GlcNAcase (OGA).
29167312	1	39	theme	cell	280:283	arg1	death					285:289	cell death	280:289	cell death	280:289	Aberrant energy metabolism represents a hallmark of cancer and contributes to numerous aggressive behaviors of cancer cells, including cell death and survival.
29167312	10	40	theme	ketoconazole	1872:1883	arg1	combination					1842:1852	combination	1842:1852	combination of bortezomib and ketoconazole or other OGA inhibitors	1842:1907	Together, our findings provide novel evidence that combination of bortezomib and ketoconazole or other OGA inhibitors may present a promising strategy for the treatment of drug-resistant MCL.
29167312	1	41	theme	cancer	197:202	arg1	hallmark					185:192	a hallmark	183:192	a hallmark of cancer	183:202	Aberrant energy metabolism represents a hallmark of cancer and contributes to numerous aggressive behaviors of cancer cells, including cell death and survival.
29167312	0	42	theme	Bid	140:142	arg1	Modification					114:125	Modification	114:125	Modification of Truncated Bid	114:142	Inhibition of O-GlcNAcase Sensitizes Apoptosis and Reverses Bortezomib Resistance in Mantle Cell Lymphoma through Modification of Truncated Bid.
29167312	2	43	theme	poor	317:320	arg1	prognosis					322:330	the poor prognosis	313:330	the poor prognosis of mantle cell lymphoma (MCL)	313:360	Despite the poor prognosis of mantle cell lymphoma (MCL), due to the inevitable development of drug resistance, metabolic reprograming of MCL cells remains an unexplored area.
29167312	9	44	theme	bortezomib-induced	1516:1533	arg1	apoptosis					1535:1543	bortezomib-induced apoptosis	1516:1543	bortezomib-induced apoptosis in de novo bortezomib-resistant MCL cells and in patient-derived primary cells with minimal cytotoxic effect on normal peripheral blood mononuclear cells and hepatocytes	1516:1713	Remarkably, ketoconazole strongly enhances bortezomib-induced apoptosis in de novo bortezomib-resistant MCL cells and in patient-derived primary cells with minimal cytotoxic effect on normal peripheral blood mononuclear cells and hepatocytes, suggesting its potential utility as a safe and effective adjuvant for MCL.
29167312	10	45	theme	inhibitors	1898:1907	arg1	combination					1842:1852	combination	1842:1852	combination of bortezomib and ketoconazole or other OGA inhibitors	1842:1907	Together, our findings provide novel evidence that combination of bortezomib and ketoconazole or other OGA inhibitors may present a promising strategy for the treatment of drug-resistant MCL.
29167312	1	46	theme	numerous	223:230	arg1	behaviors					243:251	numerous aggressive behaviors	223:251	numerous aggressive behaviors	223:251	Aberrant energy metabolism represents a hallmark of cancer and contributes to numerous aggressive behaviors of cancer cells, including cell death and survival.
29167312	1	46	theme	numerous	223:230	arg1	survival					295:302	survival	295:302	survival	295:302	Aberrant energy metabolism represents a hallmark of cancer and contributes to numerous aggressive behaviors of cancer cells, including cell death and survival.
29167312	1	46	theme	numerous	223:230	arg1	death					285:289	cell death	280:289	cell death	280:289	Aberrant energy metabolism represents a hallmark of cancer and contributes to numerous aggressive behaviors of cancer cells, including cell death and survival.
29167312	6	47	theme	potential	945:953	arg1	candidates					964:973	the potential clinical candidates	941:973	the potential clinical candidates	941:973	To identify the potential clinical candidates, we tested MCL response to drug-like OGA inhibitor, ketoconazole, and verified that it exerts similar sensitizing effect on bortezomib-induced apoptosis.
29167312	9	48	with	cells	1618:1622	arg1	effect					1647:1652	minimal cytotoxic effect	1629:1652	minimal cytotoxic effect on normal peripheral blood mononuclear cells and hepatocytes	1629:1713	Remarkably, ketoconazole strongly enhances bortezomib-induced apoptosis in de novo bortezomib-resistant MCL cells and in patient-derived primary cells with minimal cytotoxic effect on normal peripheral blood mononuclear cells and hepatocytes, suggesting its potential utility as a safe and effective adjuvant for MCL.
29167312	10	49	theme	other	1888:1892	arg1	inhibitors					1898:1907	other OGA inhibitors	1888:1907	other OGA inhibitors	1888:1907	Together, our findings provide novel evidence that combination of bortezomib and ketoconazole or other OGA inhibitors may present a promising strategy for the treatment of drug-resistant MCL.
29167312	4	50	theme	OGT	706:708	arg1	inhibitors					692:701	various small-molecule inhibitors	669:701	various small-molecule inhibitors of OGT and OGA	669:716	Using various small-molecule inhibitors of OGT and OGA, we found for the first time that O-GlcNAcylation potentiates MCL response to bortezomib.
29167312	10	51	theme	promising	1923:1931	arg1	strategy					1933:1940	a promising strategy	1921:1940	a promising strategy for the treatment of drug-resistant MCL	1921:1980	Together, our findings provide novel evidence that combination of bortezomib and ketoconazole or other OGA inhibitors may present a promising strategy for the treatment of drug-resistant MCL.
29167312	9	52	theme	MCL	1577:1579	arg1	cells					1581:1585	de novo bortezomib-resistant MCL cells	1548:1585	de novo bortezomib-resistant MCL cells	1548:1585	Remarkably, ketoconazole strongly enhances bortezomib-induced apoptosis in de novo bortezomib-resistant MCL cells and in patient-derived primary cells with minimal cytotoxic effect on normal peripheral blood mononuclear cells and hepatocytes, suggesting its potential utility as a safe and effective adjuvant for MCL.
29167312	10	53	theme	bortezomib	1857:1866	arg1	combination					1842:1852	combination	1842:1852	combination of bortezomib and ketoconazole or other OGA inhibitors	1842:1907	Together, our findings provide novel evidence that combination of bortezomib and ketoconazole or other OGA inhibitors may present a promising strategy for the treatment of drug-resistant MCL.
29167312	4	54	theme	OGA	714:716	arg1	inhibitors					692:701	various small-molecule inhibitors	669:701	various small-molecule inhibitors of OGT and OGA	669:716	Using various small-molecule inhibitors of OGT and OGA, we found for the first time that O-GlcNAcylation potentiates MCL response to bortezomib.
29167312	5	55	theme	apoptosis	866:874	arg1	sensitization					876:888	the apoptosis sensitization	862:888	the apoptosis sensitization	862:888	CRISPR interference of MGEA5 (encoding OGA) validated the apoptosis sensitization by O-GlcNAcylation and OGA inhibition.
29167312	6	56	theme	OGA	1012:1014	arg1	ketoconazole					1027:1038	ketoconazole	1027:1038	ketoconazole	1027:1038	To identify the potential clinical candidates, we tested MCL response to drug-like OGA inhibitor, ketoconazole, and verified that it exerts similar sensitizing effect on bortezomib-induced apoptosis.
29167312	6	56	theme	OGA	1012:1014	arg1	inhibitor					1016:1024	drug-like OGA inhibitor	1002:1024	drug-like OGA inhibitor	1002:1024	To identify the potential clinical candidates, we tested MCL response to drug-like OGA inhibitor, ketoconazole, and verified that it exerts similar sensitizing effect on bortezomib-induced apoptosis.
29167312	8	57	theme	tBid	1329:1332	arg1	induction					1334:1342	tBid induction	1329:1342	tBid induction	1329:1342	Not only does ketoconazole potentiate tBid induction, but also increases tBid stability through O-GlcNAcylation that interferes with tBid ubiquitination and proteasomal degradation.
29167312	0	58	theme	Cell	92:95	arg1	Lymphoma					97:104	Mantle Cell Lymphoma	85:104	Mantle Cell Lymphoma	85:104	Inhibition of O-GlcNAcase Sensitizes Apoptosis and Reverses Bortezomib Resistance in Mantle Cell Lymphoma through Modification of Truncated Bid.
29167312	9	59	theme	patient-derived	1594:1608	arg1	cells					1618:1622	patient-derived primary cells	1594:1622	patient-derived primary cells with minimal cytotoxic effect on normal peripheral blood mononuclear cells and hepatocytes	1594:1713	Remarkably, ketoconazole strongly enhances bortezomib-induced apoptosis in de novo bortezomib-resistant MCL cells and in patient-derived primary cells with minimal cytotoxic effect on normal peripheral blood mononuclear cells and hepatocytes, suggesting its potential utility as a safe and effective adjuvant for MCL.
29167312	8	60	theme	proteasomal	1448:1458	arg1	degradation					1460:1470	proteasomal degradation	1448:1470	proteasomal degradation	1448:1470	Not only does ketoconazole potentiate tBid induction, but also increases tBid stability through O-GlcNAcylation that interferes with tBid ubiquitination and proteasomal degradation.
29167312	3	61	theme	nutritional	567:577	arg1	changes					579:585	nutritional changes	567:585	nutritional changes mediated by O-GlcNAc transferase (OGT)	567:624	Posttranslational modification of proteins via O-GlcNAcylation is an ideal sensor for nutritional changes mediated by O-GlcNAc transferase (OGT) and is removed by O-GlcNAcase (OGA).
29167312	6	62	theme	MCL	986:988	arg1	response					990:997	MCL response	986:997	MCL response to drug-like OGA inhibitor, ketoconazole,	986:1039	To identify the potential clinical candidates, we tested MCL response to drug-like OGA inhibitor, ketoconazole, and verified that it exerts similar sensitizing effect on bortezomib-induced apoptosis.
29167312	4	63	theme	first	736:740	arg1	time					742:745	the first time	732:745	the first time	732:745	Using various small-molecule inhibitors of OGT and OGA, we found for the first time that O-GlcNAcylation potentiates MCL response to bortezomib.
29167312	9	64	theme	minimal	1629:1635	arg1	effect					1647:1652	minimal cytotoxic effect	1629:1652	minimal cytotoxic effect on normal peripheral blood mononuclear cells and hepatocytes	1629:1713	Remarkably, ketoconazole strongly enhances bortezomib-induced apoptosis in de novo bortezomib-resistant MCL cells and in patient-derived primary cells with minimal cytotoxic effect on normal peripheral blood mononuclear cells and hepatocytes, suggesting its potential utility as a safe and effective adjuvant for MCL.
29167312	6	65	theme	similar	1069:1075	arg1	effect					1089:1094	similar sensitizing effect	1069:1094	similar sensitizing effect	1069:1094	To identify the potential clinical candidates, we tested MCL response to drug-like OGA inhibitor, ketoconazole, and verified that it exerts similar sensitizing effect on bortezomib-induced apoptosis.
29167312	8	66	theme	tBid	1364:1367	arg1	stability					1369:1377	tBid stability	1364:1377	tBid stability	1364:1377	Not only does ketoconazole potentiate tBid induction, but also increases tBid stability through O-GlcNAcylation that interferes with tBid ubiquitination and proteasomal degradation.
29167312	2	67	theme	inevitable	374:383	arg1	development					385:395	the inevitable development	370:395	the inevitable development of drug resistance	370:414	Despite the poor prognosis of mantle cell lymphoma (MCL), due to the inevitable development of drug resistance, metabolic reprograming of MCL cells remains an unexplored area.
29167312	5	68	theme	CRISPR	808:813	arg1	interference					815:826	CRISPR interference	808:826	CRISPR interference of MGEA5 (encoding OGA)	808:850	CRISPR interference of MGEA5 (encoding OGA) validated the apoptosis sensitization by O-GlcNAcylation and OGA inhibition.
29167312	9	69	link	patient-derived	1594:1608	arg1	cells					1618:1622	patient-derived primary cells	1594:1622	patient-derived primary cells with minimal cytotoxic effect on normal peripheral blood mononuclear cells and hepatocytes	1594:1713	Remarkably, ketoconazole strongly enhances bortezomib-induced apoptosis in de novo bortezomib-resistant MCL cells and in patient-derived primary cells with minimal cytotoxic effect on normal peripheral blood mononuclear cells and hepatocytes, suggesting its potential utility as a safe and effective adjuvant for MCL.
29167312	9	70	theme	normal	1657:1662	arg1	cells					1693:1697	normal peripheral blood mononuclear cells	1657:1697	normal peripheral blood mononuclear cells	1657:1697	Remarkably, ketoconazole strongly enhances bortezomib-induced apoptosis in de novo bortezomib-resistant MCL cells and in patient-derived primary cells with minimal cytotoxic effect on normal peripheral blood mononuclear cells and hepatocytes, suggesting its potential utility as a safe and effective adjuvant for MCL.
29167312	2	71	theme	metabolic	417:425	arg1	reprograming					427:438	metabolic reprograming	417:438	metabolic reprograming of MCL cells	417:451	Despite the poor prognosis of mantle cell lymphoma (MCL), due to the inevitable development of drug resistance, metabolic reprograming of MCL cells remains an unexplored area.
29167312	2	72	theme	resistance	405:414	arg1	development					385:395	the inevitable development	370:395	the inevitable development of drug resistance	370:414	Despite the poor prognosis of mantle cell lymphoma (MCL), due to the inevitable development of drug resistance, metabolic reprograming of MCL cells remains an unexplored area.
29167312	7	73	theme	molecular	1164:1172	arg1	mechanisms					1174:1183	the underlying molecular mechanisms	1149:1183	the underlying molecular mechanisms	1149:1183	Investigations into the underlying molecular mechanisms reveal that bortezomib and ketoconazole act in concert to cause the accumulation of truncated Bid (tBid).
29167312	9	74	theme	blood	1675:1679	arg1	cells					1693:1697	normal peripheral blood mononuclear cells	1657:1697	normal peripheral blood mononuclear cells	1657:1697	Remarkably, ketoconazole strongly enhances bortezomib-induced apoptosis in de novo bortezomib-resistant MCL cells and in patient-derived primary cells with minimal cytotoxic effect on normal peripheral blood mononuclear cells and hepatocytes, suggesting its potential utility as a safe and effective adjuvant for MCL.
29167312	0	75	theme	Bortezomib	60:69	arg1	Resistance					71:80	Bortezomib Resistance	60:80	Bortezomib Resistance in Mantle Cell Lymphoma	60:104	Inhibition of O-GlcNAcase Sensitizes Apoptosis and Reverses Bortezomib Resistance in Mantle Cell Lymphoma through Modification of Truncated Bid.
29167312	11	76	dep	Ther	1994:1997	arg1	2					2003:2003	2	2003:2003	2	2003:2003	Mol Cancer Ther; 17(2); 484-96.
29167312	11	76	dep	Ther	1994:1997	arg1	17					2000:2001	17	2000:2001	17	2000:2001	Mol Cancer Ther; 17(2); 484-96.
29167312	2	77	theme	cells	447:451	arg1	reprograming					427:438	metabolic reprograming	417:438	metabolic reprograming of MCL cells	417:451	Despite the poor prognosis of mantle cell lymphoma (MCL), due to the inevitable development of drug resistance, metabolic reprograming of MCL cells remains an unexplored area.
29167312	2	78	theme	lymphoma	347:354	arg1	prognosis					322:330	the poor prognosis	313:330	the poor prognosis of mantle cell lymphoma (MCL)	313:360	Despite the poor prognosis of mantle cell lymphoma (MCL), due to the inevitable development of drug resistance, metabolic reprograming of MCL cells remains an unexplored area.
29167312	11	79	dep	17	2000:2001	arg1	484-96					2007:2012	484-96	2007:2012	484-96	2007:2012	Mol Cancer Ther; 17(2); 484-96.
29167312	9	80	from	apoptosis	1535:1543	arg1	cells					1618:1622	patient-derived primary cells	1594:1622	patient-derived primary cells with minimal cytotoxic effect on normal peripheral blood mononuclear cells and hepatocytes	1594:1713	Remarkably, ketoconazole strongly enhances bortezomib-induced apoptosis in de novo bortezomib-resistant MCL cells and in patient-derived primary cells with minimal cytotoxic effect on normal peripheral blood mononuclear cells and hepatocytes, suggesting its potential utility as a safe and effective adjuvant for MCL.
29167312	9	80	from	apoptosis	1535:1543	arg1	cells					1581:1585	de novo bortezomib-resistant MCL cells	1548:1585	de novo bortezomib-resistant MCL cells	1548:1585	Remarkably, ketoconazole strongly enhances bortezomib-induced apoptosis in de novo bortezomib-resistant MCL cells and in patient-derived primary cells with minimal cytotoxic effect on normal peripheral blood mononuclear cells and hepatocytes, suggesting its potential utility as a safe and effective adjuvant for MCL.
29167312	10	81	theme	drug-resistant	1963:1976	arg1	MCL					1978:1980	drug-resistant MCL	1963:1980	drug-resistant MCL	1963:1980	Together, our findings provide novel evidence that combination of bortezomib and ketoconazole or other OGA inhibitors may present a promising strategy for the treatment of drug-resistant MCL.
29167312	9	82	dep	de	1548:1549	arg1	novo					1551:1554	novo	1551:1554	novo	1551:1554	Remarkably, ketoconazole strongly enhances bortezomib-induced apoptosis in de novo bortezomib-resistant MCL cells and in patient-derived primary cells with minimal cytotoxic effect on normal peripheral blood mononuclear cells and hepatocytes, suggesting its potential utility as a safe and effective adjuvant for MCL.
29167312	2	83	theme	mantle	335:340	arg1	lymphoma					347:354	mantle cell lymphoma	335:354	mantle cell lymphoma (MCL)	335:360	Despite the poor prognosis of mantle cell lymphoma (MCL), due to the inevitable development of drug resistance, metabolic reprograming of MCL cells remains an unexplored area.
29167312	2	83	theme	mantle	335:340	arg1	MCL					357:359	MCL	357:359	MCL	357:359	Despite the poor prognosis of mantle cell lymphoma (MCL), due to the inevitable development of drug resistance, metabolic reprograming of MCL cells remains an unexplored area.
29167312	9	84	theme	de	1548:1549	arg1	cells					1581:1585	de novo bortezomib-resistant MCL cells	1548:1585	de novo bortezomib-resistant MCL cells	1548:1585	Remarkably, ketoconazole strongly enhances bortezomib-induced apoptosis in de novo bortezomib-resistant MCL cells and in patient-derived primary cells with minimal cytotoxic effect on normal peripheral blood mononuclear cells and hepatocytes, suggesting its potential utility as a safe and effective adjuvant for MCL.
29167312	7	85	theme	Bid	1279:1281	arg1	accumulation					1253:1264	the accumulation	1249:1264	the accumulation of truncated Bid (tBid)	1249:1288	Investigations into the underlying molecular mechanisms reveal that bortezomib and ketoconazole act in concert to cause the accumulation of truncated Bid (tBid).
29167312	1	86	theme	cells	263:267	arg1	behaviors					243:251	numerous aggressive behaviors	223:251	numerous aggressive behaviors	223:251	Aberrant energy metabolism represents a hallmark of cancer and contributes to numerous aggressive behaviors of cancer cells, including cell death and survival.
29167312	1	86	theme	cells	263:267	arg1	survival					295:302	survival	295:302	survival	295:302	Aberrant energy metabolism represents a hallmark of cancer and contributes to numerous aggressive behaviors of cancer cells, including cell death and survival.
29167312	1	86	theme	cells	263:267	arg1	death					285:289	cell death	280:289	cell death	280:289	Aberrant energy metabolism represents a hallmark of cancer and contributes to numerous aggressive behaviors of cancer cells, including cell death and survival.
21224338	3	0	theme	Xanthi	616:621	arg1	cells					623:627	tobacco cv Xanthi cells	605:627	tobacco cv Xanthi cells	605:627	In this paper, a nuclear proteomics approach was followed to identify the binding partners for Nictaba in the nucleus and the cytoplasm of tobacco cv Xanthi cells.
21224338	2	1	theme	stress	304:309	arg1	treatment					340:348	jasmonate treatment	330:348	jasmonate treatment	330:348	Since tobacco lectin expression is only observed after the plant has been subjected to stress situations such as jasmonate treatment or insect attack, Nictaba is believed to act as a signaling protein involved in the stress physiology of the plant.
21224338	2	1	theme	stress	304:309	arg1	attack					360:365	insect attack	353:365	insect attack	353:365	Since tobacco lectin expression is only observed after the plant has been subjected to stress situations such as jasmonate treatment or insect attack, Nictaba is believed to act as a signaling protein involved in the stress physiology of the plant.
21224338	2	1	theme	stress	304:309	arg1	situations					311:320	stress situations	304:320	stress situations such as jasmonate treatment or insect attack	304:365	Since tobacco lectin expression is only observed after the plant has been subjected to stress situations such as jasmonate treatment or insect attack, Nictaba is believed to act as a signaling protein involved in the stress physiology of the plant.
21224338	1	2	theme	tobacco	202:208	arg1	cells					210:214	tobacco cells	202:214	tobacco cells	202:214	The tobacco (Nicotiana tabacum) agglutinin or Nictaba is a member of a novel class of plant lectins residing in the nucleus and the cytoplasm of tobacco cells.
21224338	1	3	theme	novel	128:132	arg1	class					134:138	a novel class	126:138	a novel class of plant lectins residing in the nucleus and the cytoplasm of tobacco cells	126:214	The tobacco (Nicotiana tabacum) agglutinin or Nictaba is a member of a novel class of plant lectins residing in the nucleus and the cytoplasm of tobacco cells.
21224338	8	4	from	proteins	1321:1328	arg1	nucleus					1348:1354	the plant cell nucleus	1333:1354	the plant cell nucleus	1333:1354	Since the lectin-histone interaction was shown to be carbohydrate dependent, it is proposed that Nictaba might fulfill a signaling role in response to stress by interacting with O-GlcNAcylated proteins in the plant cell nucleus.
21224338	1	5	theme	cells	210:214	arg1	cytoplasm					189:197	the cytoplasm	185:197	the cytoplasm of tobacco cells	185:214	The tobacco (Nicotiana tabacum) agglutinin or Nictaba is a member of a novel class of plant lectins residing in the nucleus and the cytoplasm of tobacco cells.
21224338	1	5	theme	cells	210:214	arg1	nucleus					173:179	the nucleus	169:179	the nucleus	169:179	The tobacco (Nicotiana tabacum) agglutinin or Nictaba is a member of a novel class of plant lectins residing in the nucleus and the cytoplasm of tobacco cells.
21224338	2	6	theme	plant	459:463	arg1	physiology					441:450	the stress physiology	430:450	the stress physiology of the plant	430:463	Since tobacco lectin expression is only observed after the plant has been subjected to stress situations such as jasmonate treatment or insect attack, Nictaba is believed to act as a signaling protein involved in the stress physiology of the plant.
21224338	3	7	theme	tobacco	605:611	arg1	cells					623:627	tobacco cv Xanthi cells	605:627	tobacco cv Xanthi cells	605:627	In this paper, a nuclear proteomics approach was followed to identify the binding partners for Nictaba in the nucleus and the cytoplasm of tobacco cv Xanthi cells.
21224338	3	8	theme	nuclear	483:489	arg1	approach					502:509	a nuclear proteomics approach	481:509	a nuclear proteomics approach	481:509	In this paper, a nuclear proteomics approach was followed to identify the binding partners for Nictaba in the nucleus and the cytoplasm of tobacco cv Xanthi cells.
21224338	5	9	theme	thymus	864:869	arg1	proteins					879:886	purified calf thymus histone proteins	850:886	purified calf thymus histone proteins	850:886	Binding of Nictaba with histone H2B was confirmed in vitro using affinity chromatography of purified calf thymus histone proteins on a Nictaba column.
21224338	1	10	theme	tobacco	61:67	arg1	tabacum					80:86	Nicotiana tabacum	70:86	Nicotiana tabacum	70:86	The tobacco (Nicotiana tabacum) agglutinin or Nictaba is a member of a novel class of plant lectins residing in the nucleus and the cytoplasm of tobacco cells.
21224338	1	10	theme	tobacco	61:67	arg1	Nictaba					103:109	Nictaba	103:109	Nictaba	103:109	The tobacco (Nicotiana tabacum) agglutinin or Nictaba is a member of a novel class of plant lectins residing in the nucleus and the cytoplasm of tobacco cells.
21224338	1	10	theme	tobacco	61:67	arg1	member					116:121	a member	114:121	a member of a novel class of plant lectins residing in the nucleus and the cytoplasm of tobacco cells	114:214	The tobacco (Nicotiana tabacum) agglutinin or Nictaba is a member of a novel class of plant lectins residing in the nucleus and the cytoplasm of tobacco cells.
21224338	1	10	theme	tobacco	61:67	arg1	agglutinin					89:98	The tobacco (Nicotiana tabacum) agglutinin	57:98	The tobacco (Nicotiana tabacum) agglutinin	57:98	The tobacco (Nicotiana tabacum) agglutinin or Nictaba is a member of a novel class of plant lectins residing in the nucleus and the cytoplasm of tobacco cells.
21224338	1	11	theme	plant	143:147	arg1	lectins					149:155	plant lectins	143:155	plant lectins	143:155	The tobacco (Nicotiana tabacum) agglutinin or Nictaba is a member of a novel class of plant lectins residing in the nucleus and the cytoplasm of tobacco cells.
21224338	1	12	theme	class	134:138	arg1	Nictaba					103:109	Nictaba	103:109	Nictaba	103:109	The tobacco (Nicotiana tabacum) agglutinin or Nictaba is a member of a novel class of plant lectins residing in the nucleus and the cytoplasm of tobacco cells.
21224338	1	12	theme	class	134:138	arg1	member					116:121	a member	114:121	a member of a novel class of plant lectins residing in the nucleus and the cytoplasm of tobacco cells	114:214	The tobacco (Nicotiana tabacum) agglutinin or Nictaba is a member of a novel class of plant lectins residing in the nucleus and the cytoplasm of tobacco cells.
21224338	1	12	theme	class	134:138	arg1	agglutinin					89:98	The tobacco (Nicotiana tabacum) agglutinin	57:98	The tobacco (Nicotiana tabacum) agglutinin	57:98	The tobacco (Nicotiana tabacum) agglutinin or Nictaba is a member of a novel class of plant lectins residing in the nucleus and the cytoplasm of tobacco cells.
21224338	7	13	theme	histone	1085:1091	arg1	proteins					1093:1100	the Nictaba-interacting histone proteins	1061:1100	the Nictaba-interacting histone proteins	1061:1100	Moreover, mass spectrometry analyses indicated that the Nictaba-interacting histone proteins are modified by O-GlcNAc.
21224338	3	14	theme	cells	623:627	arg1	nucleus					576:582	the nucleus	572:582	the nucleus	572:582	In this paper, a nuclear proteomics approach was followed to identify the binding partners for Nictaba in the nucleus and the cytoplasm of tobacco cv Xanthi cells.
21224338	3	14	theme	cells	623:627	arg1	cytoplasm					592:600	the cytoplasm	588:600	the cytoplasm	588:600	In this paper, a nuclear proteomics approach was followed to identify the binding partners for Nictaba in the nucleus and the cytoplasm of tobacco cv Xanthi cells.
21224338	6	15	theme	Nictaba-interacting	920:938	arg1	proteins					948:955	Nictaba-interacting histone proteins	920:955	Nictaba-interacting histone proteins	920:955	Elution of Nictaba-interacting histone proteins was achieved with 1 m N-acetylglucosamine (GlcNAc).
21224338	2	16	theme	tobacco	223:229	arg1	expression					238:247	tobacco lectin expression	223:247	tobacco lectin expression	223:247	Since tobacco lectin expression is only observed after the plant has been subjected to stress situations such as jasmonate treatment or insect attack, Nictaba is believed to act as a signaling protein involved in the stress physiology of the plant.
21224338	5	17	theme	histone	782:788	arg1	H2B					790:792	histone H2B	782:792	histone H2B	782:792	Binding of Nictaba with histone H2B was confirmed in vitro using affinity chromatography of purified calf thymus histone proteins on a Nictaba column.
21224338	1	18	theme	Nicotiana	70:78	arg1	tabacum					80:86	Nicotiana tabacum	70:86	Nicotiana tabacum	70:86	The tobacco (Nicotiana tabacum) agglutinin or Nictaba is a member of a novel class of plant lectins residing in the nucleus and the cytoplasm of tobacco cells.
21224338	1	18	theme	Nicotiana	70:78	arg1	agglutinin					89:98	The tobacco (Nicotiana tabacum) agglutinin	57:98	The tobacco (Nicotiana tabacum) agglutinin	57:98	The tobacco (Nicotiana tabacum) agglutinin or Nictaba is a member of a novel class of plant lectins residing in the nucleus and the cytoplasm of tobacco cells.
21224338	3	19	from	partners	548:555	arg1	nucleus					576:582	the nucleus	572:582	the nucleus	572:582	In this paper, a nuclear proteomics approach was followed to identify the binding partners for Nictaba in the nucleus and the cytoplasm of tobacco cv Xanthi cells.
21224338	3	19	from	partners	548:555	arg1	cytoplasm					592:600	the cytoplasm	588:600	the cytoplasm	588:600	In this paper, a nuclear proteomics approach was followed to identify the binding partners for Nictaba in the nucleus and the cytoplasm of tobacco cv Xanthi cells.
21224338	2	20	theme	jasmonate	330:338	arg1	treatment					340:348	jasmonate treatment	330:348	jasmonate treatment	330:348	Since tobacco lectin expression is only observed after the plant has been subjected to stress situations such as jasmonate treatment or insect attack, Nictaba is believed to act as a signaling protein involved in the stress physiology of the plant.
21224338	3	21	theme	proteomics	491:500	arg1	approach					502:509	a nuclear proteomics approach	481:509	a nuclear proteomics approach	481:509	In this paper, a nuclear proteomics approach was followed to identify the binding partners for Nictaba in the nucleus and the cytoplasm of tobacco cv Xanthi cells.
21224338	1	22	theme	lectins	149:155	arg1	class					134:138	a novel class	126:138	a novel class of plant lectins residing in the nucleus and the cytoplasm of tobacco cells	126:214	The tobacco (Nicotiana tabacum) agglutinin or Nictaba is a member of a novel class of plant lectins residing in the nucleus and the cytoplasm of tobacco cells.
21224338	0	23	theme	tobacco	19:25	arg1	lectin					27:32	the tobacco lectin	15:32	the tobacco lectin	15:32	Interaction of the tobacco lectin with histone proteins.
21224338	5	24	from	chromatography	832:845	arg1	column					901:906	a Nictaba column	891:906	a Nictaba column	891:906	Binding of Nictaba with histone H2B was confirmed in vitro using affinity chromatography of purified calf thymus histone proteins on a Nictaba column.
21224338	4	25	theme	pull-down	671:679	arg1	assays					681:686	pull-down assays	671:686	pull-down assays	671:686	Using lectin affinity chromatography and pull-down assays, it was shown that Nictaba interacts primarily with histone proteins.
21224338	7	26	theme	spectrometry	1024:1035	arg1	analyses					1037:1044	mass spectrometry analyses	1019:1044	mass spectrometry analyses	1019:1044	Moreover, mass spectrometry analyses indicated that the Nictaba-interacting histone proteins are modified by O-GlcNAc.
21224338	4	27	theme	affinity	643:650	arg1	chromatography					652:665	lectin affinity chromatography	636:665	lectin affinity chromatography	636:665	Using lectin affinity chromatography and pull-down assays, it was shown that Nictaba interacts primarily with histone proteins.
21224338	2	28	theme	lectin	231:236	arg1	expression					238:247	tobacco lectin expression	223:247	tobacco lectin expression	223:247	Since tobacco lectin expression is only observed after the plant has been subjected to stress situations such as jasmonate treatment or insect attack, Nictaba is believed to act as a signaling protein involved in the stress physiology of the plant.
21224338	5	29	theme	proteins	879:886	arg1	chromatography					832:845	affinity chromatography	823:845	affinity chromatography of purified calf thymus histone proteins on a Nictaba column	823:906	Binding of Nictaba with histone H2B was confirmed in vitro using affinity chromatography of purified calf thymus histone proteins on a Nictaba column.
21224338	6	30	theme	m	977:977	arg1	GlcNAc					1000:1005	GlcNAc	1000:1005	GlcNAc	1000:1005	Elution of Nictaba-interacting histone proteins was achieved with 1 m N-acetylglucosamine (GlcNAc).
21224338	6	30	theme	m	977:977	arg1	N-acetylglucosamine					979:997	1 m N-acetylglucosamine	975:997	1 m N-acetylglucosamine (GlcNAc)	975:1006	Elution of Nictaba-interacting histone proteins was achieved with 1 m N-acetylglucosamine (GlcNAc).
21224338	5	31	with	Binding	758:764	arg1	H2B					790:792	histone H2B	782:792	histone H2B	782:792	Binding of Nictaba with histone H2B was confirmed in vitro using affinity chromatography of purified calf thymus histone proteins on a Nictaba column.
21224338	8	32	theme	cell	1343:1346	arg1	nucleus					1348:1354	the plant cell nucleus	1333:1354	the plant cell nucleus	1333:1354	Since the lectin-histone interaction was shown to be carbohydrate dependent, it is proposed that Nictaba might fulfill a signaling role in response to stress by interacting with O-GlcNAcylated proteins in the plant cell nucleus.
21224338	6	33	theme	1	975:975	arg1	m					977:977	m	977:977	m	977:977	Elution of Nictaba-interacting histone proteins was achieved with 1 m N-acetylglucosamine (GlcNAc).
21224338	2	34	theme	signaling	400:408	arg1	Nictaba					368:374	Nictaba	368:374	Nictaba	368:374	Since tobacco lectin expression is only observed after the plant has been subjected to stress situations such as jasmonate treatment or insect attack, Nictaba is believed to act as a signaling protein involved in the stress physiology of the plant.
21224338	2	34	theme	signaling	400:408	arg1	protein					410:416	a signaling protein	398:416	a signaling protein involved in the stress physiology of the plant	398:463	Since tobacco lectin expression is only observed after the plant has been subjected to stress situations such as jasmonate treatment or insect attack, Nictaba is believed to act as a signaling protein involved in the stress physiology of the plant.
21224338	0	35	theme	lectin	27:32	arg1	Interaction					0:10	Interaction	0:10	Interaction of the tobacco lectin with histone proteins.	0:55	Interaction of the tobacco lectin with histone proteins.
21224338	8	36	theme	plant	1337:1341	arg1	nucleus					1348:1354	the plant cell nucleus	1333:1354	the plant cell nucleus	1333:1354	Since the lectin-histone interaction was shown to be carbohydrate dependent, it is proposed that Nictaba might fulfill a signaling role in response to stress by interacting with O-GlcNAcylated proteins in the plant cell nucleus.
21224338	5	37	theme	Nictaba	769:775	arg1	Binding					758:764	Binding	758:764	Binding of Nictaba with histone H2B	758:792	Binding of Nictaba with histone H2B was confirmed in vitro using affinity chromatography of purified calf thymus histone proteins on a Nictaba column.
21224338	2	38	theme	insect	353:358	arg1	attack					360:365	insect attack	353:365	insect attack	353:365	Since tobacco lectin expression is only observed after the plant has been subjected to stress situations such as jasmonate treatment or insect attack, Nictaba is believed to act as a signaling protein involved in the stress physiology of the plant.
21224338	7	39	theme	Nictaba-interacting	1065:1083	arg1	proteins					1093:1100	the Nictaba-interacting histone proteins	1061:1100	the Nictaba-interacting histone proteins	1061:1100	Moreover, mass spectrometry analyses indicated that the Nictaba-interacting histone proteins are modified by O-GlcNAc.
21224338	8	40	theme	O-GlcNAcylated	1306:1319	arg1	proteins					1321:1328	O-GlcNAcylated proteins	1306:1328	O-GlcNAcylated proteins in the plant cell nucleus	1306:1354	Since the lectin-histone interaction was shown to be carbohydrate dependent, it is proposed that Nictaba might fulfill a signaling role in response to stress by interacting with O-GlcNAcylated proteins in the plant cell nucleus.
21224338	5	41	theme	affinity	823:830	arg1	chromatography					832:845	affinity chromatography	823:845	affinity chromatography of purified calf thymus histone proteins on a Nictaba column	823:906	Binding of Nictaba with histone H2B was confirmed in vitro using affinity chromatography of purified calf thymus histone proteins on a Nictaba column.
21224338	0	42	theme	histone	39:45	arg1	proteins					47:54	histone proteins	39:54	histone proteins	39:54	Interaction of the tobacco lectin with histone proteins.
21224338	4	43	theme	histone	740:746	arg1	proteins					748:755	histone proteins	740:755	histone proteins	740:755	Using lectin affinity chromatography and pull-down assays, it was shown that Nictaba interacts primarily with histone proteins.
21224338	7	44	mod	modified	1106:1113	arg1	proteins					1093:1100	the Nictaba-interacting histone proteins	1061:1100	the Nictaba-interacting histone proteins	1061:1100	Moreover, mass spectrometry analyses indicated that the Nictaba-interacting histone proteins are modified by O-GlcNAc.
21224338	7	44	mod	modified	1106:1113	arg3	O-GlcNAc					1118:1125	O-GlcNAc	1118:1125	O-GlcNAc	1118:1125	Moreover, mass spectrometry analyses indicated that the Nictaba-interacting histone proteins are modified by O-GlcNAc.
21224338	5	45	theme	calf	859:862	arg1	proteins					879:886	purified calf thymus histone proteins	850:886	purified calf thymus histone proteins	850:886	Binding of Nictaba with histone H2B was confirmed in vitro using affinity chromatography of purified calf thymus histone proteins on a Nictaba column.
21224338	3	46	theme	binding	540:546	arg1	partners					548:555	the binding partners	536:555	the binding partners for Nictaba in the nucleus and the cytoplasm of tobacco cv Xanthi cells	536:627	In this paper, a nuclear proteomics approach was followed to identify the binding partners for Nictaba in the nucleus and the cytoplasm of tobacco cv Xanthi cells.
21224338	0	47	with	Interaction	0:10	arg1	proteins					47:54	histone proteins	39:54	histone proteins	39:54	Interaction of the tobacco lectin with histone proteins.
21224338	4	48	theme	lectin	636:641	arg1	chromatography					652:665	lectin affinity chromatography	636:665	lectin affinity chromatography	636:665	Using lectin affinity chromatography and pull-down assays, it was shown that Nictaba interacts primarily with histone proteins.
21224338	5	49	theme	histone	871:877	arg1	proteins					879:886	purified calf thymus histone proteins	850:886	purified calf thymus histone proteins	850:886	Binding of Nictaba with histone H2B was confirmed in vitro using affinity chromatography of purified calf thymus histone proteins on a Nictaba column.
21224338	5	50	theme	purified	850:857	arg1	proteins					879:886	purified calf thymus histone proteins	850:886	purified calf thymus histone proteins	850:886	Binding of Nictaba with histone H2B was confirmed in vitro using affinity chromatography of purified calf thymus histone proteins on a Nictaba column.
21224338	8	51	theme	signaling	1249:1257	arg1	role					1259:1262	a signaling role	1247:1262	a signaling role	1247:1262	Since the lectin-histone interaction was shown to be carbohydrate dependent, it is proposed that Nictaba might fulfill a signaling role in response to stress by interacting with O-GlcNAcylated proteins in the plant cell nucleus.
21224338	2	52	theme	stress	434:439	arg1	physiology					441:450	the stress physiology	430:450	the stress physiology of the plant	430:463	Since tobacco lectin expression is only observed after the plant has been subjected to stress situations such as jasmonate treatment or insect attack, Nictaba is believed to act as a signaling protein involved in the stress physiology of the plant.
21224338	5	53	theme	Nictaba	893:899	arg1	column					901:906	a Nictaba column	891:906	a Nictaba column	891:906	Binding of Nictaba with histone H2B was confirmed in vitro using affinity chromatography of purified calf thymus histone proteins on a Nictaba column.
21224338	6	54	theme	proteins	948:955	arg1	Elution					909:915	Elution	909:915	Elution of Nictaba-interacting histone proteins	909:955	Elution of Nictaba-interacting histone proteins was achieved with 1 m N-acetylglucosamine (GlcNAc).
21224338	3	55	theme	cv	613:614	arg1	cells					623:627	tobacco cv Xanthi cells	605:627	tobacco cv Xanthi cells	605:627	In this paper, a nuclear proteomics approach was followed to identify the binding partners for Nictaba in the nucleus and the cytoplasm of tobacco cv Xanthi cells.
21224338	8	56	theme	lectin-histone	1138:1151	arg1	interaction					1153:1163	the lectin-histone interaction	1134:1163	the lectin-histone interaction	1134:1163	Since the lectin-histone interaction was shown to be carbohydrate dependent, it is proposed that Nictaba might fulfill a signaling role in response to stress by interacting with O-GlcNAcylated proteins in the plant cell nucleus.
21224338	8	56	theme	lectin-histone	1138:1151	arg1	dependent					1194:1202	dependent	1194:1202	dependent	1194:1202	Since the lectin-histone interaction was shown to be carbohydrate dependent, it is proposed that Nictaba might fulfill a signaling role in response to stress by interacting with O-GlcNAcylated proteins in the plant cell nucleus.
21224338	7	57	theme	mass	1019:1022	arg1	analyses					1037:1044	mass spectrometry analyses	1019:1044	mass spectrometry analyses	1019:1044	Moreover, mass spectrometry analyses indicated that the Nictaba-interacting histone proteins are modified by O-GlcNAc.
21224338	6	58	theme	histone	940:946	arg1	proteins					948:955	Nictaba-interacting histone proteins	920:955	Nictaba-interacting histone proteins	920:955	Elution of Nictaba-interacting histone proteins was achieved with 1 m N-acetylglucosamine (GlcNAc).
24853093	5	0	theme	26S	631:633	arg1	activity					646:653	26S proteasome activity	631:653	26S proteasome activity	631:653	The 26S proteasome reporter protein levels, 26S proteasome activity, and the O-GlcNAcylation of Rpt2, a key subunit of the proteasome regulatory complex, were assayed in 26S proteasome reporter cells, human umbilical vein endothelial cells (HUVEC), and mouse aortic tissues isolated from 26S proteasome reporter and eNOS knockout mice.
24853093	6	1	theme	26S	1131:1133	arg1	accumulation					1163:1174	26S proteasome reporter protein accumulation	1131:1174	26S proteasome reporter protein accumulation	1131:1174	Like the other selective NO donors, NO derived from activated eNOS (by pharmacological and genetic approach) increased O-GlcNAc modification of Rpt2, reduced proteasome chymotrypsin-like activity, and caused 26S proteasome reporter protein accumulation.
24853093	4	2	theme	endothelial	568:578	arg1	cells					580:584	vascular endothelial cells	559:584	vascular endothelial cells	559:584	The aim of the present study was to establish the connection between endothelial NO and 26S proteasome functionality in vascular endothelial cells.
24853093	9	3	theme	OGT	1511:1513	arg1	knockdown					1515:1523	OGT knockdown	1511:1523	OGT knockdown	1511:1523	Consistently, adenoviral overexpression of O-GlcNAcase (OGA), the enzyme catalyzing the removal of the O-GlcNAc group, mimicked the effects of OGT knockdown.
24853093	6	4	mod	modification	1051:1062	arg1	Rpt2					1067:1070	Rpt2	1067:1070	Rpt2	1067:1070	Like the other selective NO donors, NO derived from activated eNOS (by pharmacological and genetic approach) increased O-GlcNAc modification of Rpt2, reduced proteasome chymotrypsin-like activity, and caused 26S proteasome reporter protein accumulation.
24853093	6	4	mod	modification	1051:1062	arg3	O-GlcNAc					1042:1049	O-GlcNAc modification	1042:1062	O-GlcNAc modification of Rpt2	1042:1070	Like the other selective NO donors, NO derived from activated eNOS (by pharmacological and genetic approach) increased O-GlcNAc modification of Rpt2, reduced proteasome chymotrypsin-like activity, and caused 26S proteasome reporter protein accumulation.
24853093	11	5	theme	26S	1844:1846	arg1	proteasome					1848:1857	the 26S proteasome	1840:1857	the 26S proteasome	1840:1857	In conclusion, the eNOS-derived NO functions as a physiological suppressor of the 26S proteasome in vascular endothelial cells.
24853093	5	6	theme	reporter	606:613	arg1	levels					623:628	The 26S proteasome reporter protein levels	587:628	The 26S proteasome reporter protein levels	587:628	The 26S proteasome reporter protein levels, 26S proteasome activity, and the O-GlcNAcylation of Rpt2, a key subunit of the proteasome regulatory complex, were assayed in 26S proteasome reporter cells, human umbilical vein endothelial cells (HUVEC), and mouse aortic tissues isolated from 26S proteasome reporter and eNOS knockout mice.
24853093	10	7	theme	Rpt2	1695:1698	arg1	O-GlcNAcylation					1700:1714	decreased Rpt2 O-GlcNAcylation	1685:1714	decreased Rpt2 O-GlcNAcylation	1685:1714	Finally, compared to eNOS wild type aortic tissues, 26S proteasome reporter mice lacking eNOS exhibited elevated 26S proteasome functionality in parallel with decreased Rpt2 O-GlcNAcylation, without changing the levels of Rpt2 protein.
24853093	9	8	theme	O-GlcNAcase	1411:1421	arg1	overexpression					1393:1406	adenoviral overexpression	1382:1406	adenoviral overexpression of O-GlcNAcase (OGA), the enzyme catalyzing the removal of the O-GlcNAc group,	1382:1485	Consistently, adenoviral overexpression of O-GlcNAcase (OGA), the enzyme catalyzing the removal of the O-GlcNAc group, mimicked the effects of OGT knockdown.
24853093	6	9	attach	derived	962:968	arg1	eNOS					985:988	activated eNOS	975:988	activated eNOS (by pharmacological and genetic approach)	975:1030	Like the other selective NO donors, NO derived from activated eNOS (by pharmacological and genetic approach) increased O-GlcNAc modification of Rpt2, reduced proteasome chymotrypsin-like activity, and caused 26S proteasome reporter protein accumulation.
24853093	6	9	attach	derived	962:968	arg2	NO					959:960	NO	959:960	NO derived from activated eNOS (by pharmacological and genetic approach)	959:1030	Like the other selective NO donors, NO derived from activated eNOS (by pharmacological and genetic approach) increased O-GlcNAc modification of Rpt2, reduced proteasome chymotrypsin-like activity, and caused 26S proteasome reporter protein accumulation.
24853093	6	10	theme	proteasome	1081:1090	arg1	activity					1110:1117	proteasome chymotrypsin-like activity	1081:1117	proteasome chymotrypsin-like activity	1081:1117	Like the other selective NO donors, NO derived from activated eNOS (by pharmacological and genetic approach) increased O-GlcNAc modification of Rpt2, reduced proteasome chymotrypsin-like activity, and caused 26S proteasome reporter protein accumulation.
24853093	5	11	theme	Rpt2	683:686	arg1	levels					623:628	The 26S proteasome reporter protein levels	587:628	The 26S proteasome reporter protein levels	587:628	The 26S proteasome reporter protein levels, 26S proteasome activity, and the O-GlcNAcylation of Rpt2, a key subunit of the proteasome regulatory complex, were assayed in 26S proteasome reporter cells, human umbilical vein endothelial cells (HUVEC), and mouse aortic tissues isolated from 26S proteasome reporter and eNOS knockout mice.
24853093	5	11	theme	Rpt2	683:686	arg1	O-GlcNAcylation					664:678	the O-GlcNAcylation	660:678	the O-GlcNAcylation of Rpt2, a key subunit of the proteasome regulatory complex,	660:739	The 26S proteasome reporter protein levels, 26S proteasome activity, and the O-GlcNAcylation of Rpt2, a key subunit of the proteasome regulatory complex, were assayed in 26S proteasome reporter cells, human umbilical vein endothelial cells (HUVEC), and mouse aortic tissues isolated from 26S proteasome reporter and eNOS knockout mice.
24853093	5	11	theme	Rpt2	683:686	arg1	activity					646:653	26S proteasome activity	631:653	26S proteasome activity	631:653	The 26S proteasome reporter protein levels, 26S proteasome activity, and the O-GlcNAcylation of Rpt2, a key subunit of the proteasome regulatory complex, were assayed in 26S proteasome reporter cells, human umbilical vein endothelial cells (HUVEC), and mouse aortic tissues isolated from 26S proteasome reporter and eNOS knockout mice.
24853093	5	12	theme	umbilical	794:802	arg1	HUVEC					828:832	HUVEC	828:832	HUVEC	828:832	The 26S proteasome reporter protein levels, 26S proteasome activity, and the O-GlcNAcylation of Rpt2, a key subunit of the proteasome regulatory complex, were assayed in 26S proteasome reporter cells, human umbilical vein endothelial cells (HUVEC), and mouse aortic tissues isolated from 26S proteasome reporter and eNOS knockout mice.
24853093	5	12	theme	umbilical	794:802	arg1	cells					821:825	human umbilical vein endothelial cells	788:825	human umbilical vein endothelial cells (HUVEC)	788:833	The 26S proteasome reporter protein levels, 26S proteasome activity, and the O-GlcNAcylation of Rpt2, a key subunit of the proteasome regulatory complex, were assayed in 26S proteasome reporter cells, human umbilical vein endothelial cells (HUVEC), and mouse aortic tissues isolated from 26S proteasome reporter and eNOS knockout mice.
24853093	8	13	theme	SiRNA	1236:1240	arg1	knockdown					1242:1250	SiRNA knockdown	1236:1250	SiRNA knockdown of O-GlcNAc transferase (OGT), the key enzyme that catalyzes protein O-GlcNAcylation,	1236:1336	SiRNA knockdown of O-GlcNAc transferase (OGT), the key enzyme that catalyzes protein O-GlcNAcylation, abolished NO-induced effects.
24853093	10	14	theme	aortic	1562:1567	arg1	tissues					1569:1575	eNOS wild type aortic tissues	1547:1575	eNOS wild type aortic tissues	1547:1575	Finally, compared to eNOS wild type aortic tissues, 26S proteasome reporter mice lacking eNOS exhibited elevated 26S proteasome functionality in parallel with decreased Rpt2 O-GlcNAcylation, without changing the levels of Rpt2 protein.
24853093	1	15	theme	endothelial	203:213	arg1	cells					215:219	vascular endothelial cells	194:219	vascular endothelial cells	194:219	The 26S proteasome plays a fundamental role in almost all eukaryotic cells, including vascular endothelial cells.
24853093	10	16	theme	wild	1552:1555	arg1	tissues					1569:1575	eNOS wild type aortic tissues	1547:1575	eNOS wild type aortic tissues	1547:1575	Finally, compared to eNOS wild type aortic tissues, 26S proteasome reporter mice lacking eNOS exhibited elevated 26S proteasome functionality in parallel with decreased Rpt2 O-GlcNAcylation, without changing the levels of Rpt2 protein.
24853093	10	17	theme	Rpt2	1748:1751	arg1	protein					1753:1759	Rpt2 protein	1748:1759	Rpt2 protein	1748:1759	Finally, compared to eNOS wild type aortic tissues, 26S proteasome reporter mice lacking eNOS exhibited elevated 26S proteasome functionality in parallel with decreased Rpt2 O-GlcNAcylation, without changing the levels of Rpt2 protein.
24853093	1	18	theme	26S	112:114	arg1	proteasome					116:125	The 26S proteasome	108:125	The 26S proteasome	108:125	The 26S proteasome plays a fundamental role in almost all eukaryotic cells, including vascular endothelial cells.
24853093	11	19	link	eNOS-derived	1781:1792	arg1	suppressor					1826:1835	a physiological suppressor	1810:1835	a physiological suppressor of the 26S proteasome in vascular endothelial cells	1810:1887	In conclusion, the eNOS-derived NO functions as a physiological suppressor of the 26S proteasome in vascular endothelial cells.
24853093	11	19	link	eNOS-derived	1781:1792	arg1	NO					1794:1795	the eNOS-derived NO	1777:1795	the eNOS-derived NO	1777:1795	In conclusion, the eNOS-derived NO functions as a physiological suppressor of the 26S proteasome in vascular endothelial cells.
24853093	8	20	theme	transferase	1264:1274	arg1	knockdown					1242:1250	SiRNA knockdown	1236:1250	SiRNA knockdown of O-GlcNAc transferase (OGT), the key enzyme that catalyzes protein O-GlcNAcylation,	1236:1336	SiRNA knockdown of O-GlcNAc transferase (OGT), the key enzyme that catalyzes protein O-GlcNAcylation, abolished NO-induced effects.
24853093	5	21	theme	26S	875:877	arg1	reporter					890:897	26S proteasome reporter and eNOS knockout mice	875:920	reporter	890:897	The 26S proteasome reporter protein levels, 26S proteasome activity, and the O-GlcNAcylation of Rpt2, a key subunit of the proteasome regulatory complex, were assayed in 26S proteasome reporter cells, human umbilical vein endothelial cells (HUVEC), and mouse aortic tissues isolated from 26S proteasome reporter and eNOS knockout mice.
24853093	3	22	theme	nitric	332:337	arg1	eNOS					360:363	eNOS	360:363	eNOS	360:363	Endothelial nitric oxide (NO) synthase (eNOS)-derived NO is known to be essential to maintain endothelial homeostasis.
24853093	3	22	theme	nitric	332:337	arg1	synthase					350:357	Endothelial nitric oxide (NO) synthase	320:357	Endothelial nitric oxide (NO) synthase (eNOS)-derived NO	320:375	Endothelial nitric oxide (NO) synthase (eNOS)-derived NO is known to be essential to maintain endothelial homeostasis.
24853093	6	23	theme	reporter	1146:1153	arg1	accumulation					1163:1174	26S proteasome reporter protein accumulation	1131:1174	26S proteasome reporter protein accumulation	1131:1174	Like the other selective NO donors, NO derived from activated eNOS (by pharmacological and genetic approach) increased O-GlcNAc modification of Rpt2, reduced proteasome chymotrypsin-like activity, and caused 26S proteasome reporter protein accumulation.
24853093	5	24	theme	regulatory	721:730	arg1	complex					732:738	the proteasome regulatory complex	706:738	the proteasome regulatory complex	706:738	The 26S proteasome reporter protein levels, 26S proteasome activity, and the O-GlcNAcylation of Rpt2, a key subunit of the proteasome regulatory complex, were assayed in 26S proteasome reporter cells, human umbilical vein endothelial cells (HUVEC), and mouse aortic tissues isolated from 26S proteasome reporter and eNOS knockout mice.
24853093	3	25	link	-derived	365:372	arg1	NO					374:375	Endothelial nitric oxide (NO) synthase (eNOS)-derived NO	320:375	Endothelial nitric oxide (NO) synthase (eNOS)-derived NO	320:375	Endothelial nitric oxide (NO) synthase (eNOS)-derived NO is known to be essential to maintain endothelial homeostasis.
24853093	9	26	theme	O-GlcNAc	1471:1478	arg1	group					1480:1484	the O-GlcNAc group	1467:1484	the O-GlcNAc group	1467:1484	Consistently, adenoviral overexpression of O-GlcNAcase (OGA), the enzyme catalyzing the removal of the O-GlcNAc group, mimicked the effects of OGT knockdown.
24853093	4	27	theme	study	462:466	arg1	aim					443:445	The aim	439:445	The aim of the present study	439:466	The aim of the present study was to establish the connection between endothelial NO and 26S proteasome functionality in vascular endothelial cells.
24853093	5	28	gly	O-GlcNAcylation	664:678	arg1	HUVEC					828:832	HUVEC	828:832	HUVEC	828:832	The 26S proteasome reporter protein levels, 26S proteasome activity, and the O-GlcNAcylation of Rpt2, a key subunit of the proteasome regulatory complex, were assayed in 26S proteasome reporter cells, human umbilical vein endothelial cells (HUVEC), and mouse aortic tissues isolated from 26S proteasome reporter and eNOS knockout mice.
24853093	5	28	gly	O-GlcNAcylation	664:678	arg1	cells					781:785	26S proteasome reporter cells	757:785	26S proteasome reporter cells	757:785	The 26S proteasome reporter protein levels, 26S proteasome activity, and the O-GlcNAcylation of Rpt2, a key subunit of the proteasome regulatory complex, were assayed in 26S proteasome reporter cells, human umbilical vein endothelial cells (HUVEC), and mouse aortic tissues isolated from 26S proteasome reporter and eNOS knockout mice.
24853093	5	28	gly	O-GlcNAcylation	664:678	arg1	tissues					853:859	mouse aortic tissues	840:859	mouse aortic tissues	840:859	The 26S proteasome reporter protein levels, 26S proteasome activity, and the O-GlcNAcylation of Rpt2, a key subunit of the proteasome regulatory complex, were assayed in 26S proteasome reporter cells, human umbilical vein endothelial cells (HUVEC), and mouse aortic tissues isolated from 26S proteasome reporter and eNOS knockout mice.
24853093	5	28	gly	O-GlcNAcylation	664:678	arg1	cells					821:825	human umbilical vein endothelial cells	788:825	human umbilical vein endothelial cells (HUVEC)	788:833	The 26S proteasome reporter protein levels, 26S proteasome activity, and the O-GlcNAcylation of Rpt2, a key subunit of the proteasome regulatory complex, were assayed in 26S proteasome reporter cells, human umbilical vein endothelial cells (HUVEC), and mouse aortic tissues isolated from 26S proteasome reporter and eNOS knockout mice.
24853093	0	29	theme	proteasomes	65:75	arg1	inhibitor					48:56	an endogenous inhibitor	34:56	an endogenous inhibitor of 26S proteasomes in vascular endothelial cells	34:105	Identification of nitric oxide as an endogenous inhibitor of 26S proteasomes in vascular endothelial cells.
24853093	5	30	theme	aortic	846:851	arg1	tissues					853:859	mouse aortic tissues	840:859	mouse aortic tissues	840:859	The 26S proteasome reporter protein levels, 26S proteasome activity, and the O-GlcNAcylation of Rpt2, a key subunit of the proteasome regulatory complex, were assayed in 26S proteasome reporter cells, human umbilical vein endothelial cells (HUVEC), and mouse aortic tissues isolated from 26S proteasome reporter and eNOS knockout mice.
24853093	6	31	theme	selective	938:946	arg1	donors					951:956	the other selective NO donors	928:956	the other selective NO donors	928:956	Like the other selective NO donors, NO derived from activated eNOS (by pharmacological and genetic approach) increased O-GlcNAc modification of Rpt2, reduced proteasome chymotrypsin-like activity, and caused 26S proteasome reporter protein accumulation.
24853093	11	32	from	suppressor	1826:1835	arg1	cells					1883:1887	vascular endothelial cells	1862:1887	vascular endothelial cells	1862:1887	In conclusion, the eNOS-derived NO functions as a physiological suppressor of the 26S proteasome in vascular endothelial cells.
24853093	8	33	theme	key	1287:1289	arg1	enzyme					1291:1296	the key enzyme	1283:1296	the key enzyme that catalyzes protein O-GlcNAcylation	1283:1335	SiRNA knockdown of O-GlcNAc transferase (OGT), the key enzyme that catalyzes protein O-GlcNAcylation, abolished NO-induced effects.
24853093	8	33	theme	key	1287:1289	arg1	transferase					1264:1274	O-GlcNAc transferase	1255:1274	O-GlcNAc transferase (OGT)	1255:1280	SiRNA knockdown of O-GlcNAc transferase (OGT), the key enzyme that catalyzes protein O-GlcNAcylation, abolished NO-induced effects.
24853093	0	34	theme	vascular	80:87	arg1	cells					101:105	vascular endothelial cells	80:105	vascular endothelial cells	80:105	Identification of nitric oxide as an endogenous inhibitor of 26S proteasomes in vascular endothelial cells.
24853093	10	35	theme	reporter	1593:1600	arg1	mice					1602:1605	26S proteasome reporter mice	1578:1605	26S proteasome reporter mice lacking eNOS	1578:1618	Finally, compared to eNOS wild type aortic tissues, 26S proteasome reporter mice lacking eNOS exhibited elevated 26S proteasome functionality in parallel with decreased Rpt2 O-GlcNAcylation, without changing the levels of Rpt2 protein.
24853093	0	36	theme	26S	61:63	arg1	proteasomes					65:75	26S proteasomes	61:75	26S proteasomes	61:75	Identification of nitric oxide as an endogenous inhibitor of 26S proteasomes in vascular endothelial cells.
24853093	8	37	theme	protein	1313:1319	arg1	O-GlcNAcylation					1321:1335	protein O-GlcNAcylation	1313:1335	protein O-GlcNAcylation	1313:1335	SiRNA knockdown of O-GlcNAc transferase (OGT), the key enzyme that catalyzes protein O-GlcNAcylation, abolished NO-induced effects.
24853093	10	38	theme	26S	1578:1580	arg1	mice					1602:1605	26S proteasome reporter mice	1578:1605	26S proteasome reporter mice lacking eNOS	1578:1618	Finally, compared to eNOS wild type aortic tissues, 26S proteasome reporter mice lacking eNOS exhibited elevated 26S proteasome functionality in parallel with decreased Rpt2 O-GlcNAcylation, without changing the levels of Rpt2 protein.
24853093	5	39	theme	reporter	772:779	arg1	cells					781:785	26S proteasome reporter cells	757:785	26S proteasome reporter cells	757:785	The 26S proteasome reporter protein levels, 26S proteasome activity, and the O-GlcNAcylation of Rpt2, a key subunit of the proteasome regulatory complex, were assayed in 26S proteasome reporter cells, human umbilical vein endothelial cells (HUVEC), and mouse aortic tissues isolated from 26S proteasome reporter and eNOS knockout mice.
24853093	9	40	theme	knockdown	1515:1523	arg1	effects					1500:1506	the effects	1496:1506	the effects of OGT knockdown	1496:1523	Consistently, adenoviral overexpression of O-GlcNAcase (OGA), the enzyme catalyzing the removal of the O-GlcNAc group, mimicked the effects of OGT knockdown.
24853093	0	41	theme	nitric	18:23	arg1	oxide					25:29	nitric oxide	18:29	nitric oxide	18:29	Identification of nitric oxide as an endogenous inhibitor of 26S proteasomes in vascular endothelial cells.
24853093	5	42	theme	eNOS	903:906	arg1	mice					917:920	26S proteasome reporter and eNOS knockout mice	875:920	mice	917:920	The 26S proteasome reporter protein levels, 26S proteasome activity, and the O-GlcNAcylation of Rpt2, a key subunit of the proteasome regulatory complex, were assayed in 26S proteasome reporter cells, human umbilical vein endothelial cells (HUVEC), and mouse aortic tissues isolated from 26S proteasome reporter and eNOS knockout mice.
24853093	4	43	theme	26S	527:529	arg1	proteasome					531:540	26S proteasome	527:540	26S proteasome	527:540	The aim of the present study was to establish the connection between endothelial NO and 26S proteasome functionality in vascular endothelial cells.
24853093	11	44	theme	endothelial	1871:1881	arg1	cells					1883:1887	vascular endothelial cells	1862:1887	vascular endothelial cells	1862:1887	In conclusion, the eNOS-derived NO functions as a physiological suppressor of the 26S proteasome in vascular endothelial cells.
24853093	8	45	theme	NO-induced	1348:1357	arg1	effects					1359:1365	NO-induced effects	1348:1365	NO-induced effects	1348:1365	SiRNA knockdown of O-GlcNAc transferase (OGT), the key enzyme that catalyzes protein O-GlcNAcylation, abolished NO-induced effects.
24853093	3	46	theme	endothelial	414:424	arg1	homeostasis					426:436	endothelial homeostasis	414:436	endothelial homeostasis	414:436	Endothelial nitric oxide (NO) synthase (eNOS)-derived NO is known to be essential to maintain endothelial homeostasis.
24853093	5	47	theme	26S	757:759	arg1	cells					781:785	26S proteasome reporter cells	757:785	26S proteasome reporter cells	757:785	The 26S proteasome reporter protein levels, 26S proteasome activity, and the O-GlcNAcylation of Rpt2, a key subunit of the proteasome regulatory complex, were assayed in 26S proteasome reporter cells, human umbilical vein endothelial cells (HUVEC), and mouse aortic tissues isolated from 26S proteasome reporter and eNOS knockout mice.
24853093	10	48	with	parallel	1671:1678	arg1	O-GlcNAcylation					1700:1714	decreased Rpt2 O-GlcNAcylation	1685:1714	decreased Rpt2 O-GlcNAcylation	1685:1714	Finally, compared to eNOS wild type aortic tissues, 26S proteasome reporter mice lacking eNOS exhibited elevated 26S proteasome functionality in parallel with decreased Rpt2 O-GlcNAcylation, without changing the levels of Rpt2 protein.
24853093	6	49	theme	Rpt2	1067:1070	arg1	modification					1051:1062	O-GlcNAc modification	1042:1062	O-GlcNAc modification of Rpt2	1042:1070	Like the other selective NO donors, NO derived from activated eNOS (by pharmacological and genetic approach) increased O-GlcNAc modification of Rpt2, reduced proteasome chymotrypsin-like activity, and caused 26S proteasome reporter protein accumulation.
24853093	10	50	theme	26S	1639:1641	arg1	proteasome					1643:1652	elevated 26S proteasome	1630:1652	elevated 26S proteasome functionality	1630:1666	Finally, compared to eNOS wild type aortic tissues, 26S proteasome reporter mice lacking eNOS exhibited elevated 26S proteasome functionality in parallel with decreased Rpt2 O-GlcNAcylation, without changing the levels of Rpt2 protein.
24853093	1	51	theme	fundamental	135:145	arg1	role					147:150	a fundamental role	133:150	a fundamental role	133:150	The 26S proteasome plays a fundamental role in almost all eukaryotic cells, including vascular endothelial cells.
24853093	10	52	theme	decreased	1685:1693	arg1	O-GlcNAcylation					1700:1714	decreased Rpt2 O-GlcNAcylation	1685:1714	decreased Rpt2 O-GlcNAcylation	1685:1714	Finally, compared to eNOS wild type aortic tissues, 26S proteasome reporter mice lacking eNOS exhibited elevated 26S proteasome functionality in parallel with decreased Rpt2 O-GlcNAcylation, without changing the levels of Rpt2 protein.
24853093	1	53	theme	all	162:164	arg1	cells					215:219	vascular endothelial cells	194:219	vascular endothelial cells	194:219	The 26S proteasome plays a fundamental role in almost all eukaryotic cells, including vascular endothelial cells.
24853093	1	53	theme	all	162:164	arg1	cells					177:181	almost all eukaryotic cells	155:181	almost all eukaryotic cells	155:181	The 26S proteasome plays a fundamental role in almost all eukaryotic cells, including vascular endothelial cells.
24853093	5	54	attach	isolated	861:868	arg1	mice					917:920	26S proteasome reporter and eNOS knockout mice	875:920	mice	917:920	The 26S proteasome reporter protein levels, 26S proteasome activity, and the O-GlcNAcylation of Rpt2, a key subunit of the proteasome regulatory complex, were assayed in 26S proteasome reporter cells, human umbilical vein endothelial cells (HUVEC), and mouse aortic tissues isolated from 26S proteasome reporter and eNOS knockout mice.
24853093	5	54	attach	isolated	861:868	arg2	cells					781:785	26S proteasome reporter cells	757:785	26S proteasome reporter cells	757:785	The 26S proteasome reporter protein levels, 26S proteasome activity, and the O-GlcNAcylation of Rpt2, a key subunit of the proteasome regulatory complex, were assayed in 26S proteasome reporter cells, human umbilical vein endothelial cells (HUVEC), and mouse aortic tissues isolated from 26S proteasome reporter and eNOS knockout mice.
24853093	5	54	attach	isolated	861:868	arg1	reporter					890:897	26S proteasome reporter and eNOS knockout mice	875:920	reporter	890:897	The 26S proteasome reporter protein levels, 26S proteasome activity, and the O-GlcNAcylation of Rpt2, a key subunit of the proteasome regulatory complex, were assayed in 26S proteasome reporter cells, human umbilical vein endothelial cells (HUVEC), and mouse aortic tissues isolated from 26S proteasome reporter and eNOS knockout mice.
24853093	11	55	theme	physiological	1812:1824	arg1	suppressor					1826:1835	a physiological suppressor	1810:1835	a physiological suppressor of the 26S proteasome in vascular endothelial cells	1810:1887	In conclusion, the eNOS-derived NO functions as a physiological suppressor of the 26S proteasome in vascular endothelial cells.
24853093	11	55	theme	physiological	1812:1824	arg1	NO					1794:1795	the eNOS-derived NO	1777:1795	the eNOS-derived NO	1777:1795	In conclusion, the eNOS-derived NO functions as a physiological suppressor of the 26S proteasome in vascular endothelial cells.
24853093	7	56	theme	eNOS	1205:1208	arg1	inactivation					1189:1200	inactivation	1189:1200	inactivation of eNOS	1189:1208	Conversely, inactivation of eNOS reversed all the effects.
24853093	5	57	theme	proteasome	635:644	arg1	activity					646:653	26S proteasome activity	631:653	26S proteasome activity	631:653	The 26S proteasome reporter protein levels, 26S proteasome activity, and the O-GlcNAcylation of Rpt2, a key subunit of the proteasome regulatory complex, were assayed in 26S proteasome reporter cells, human umbilical vein endothelial cells (HUVEC), and mouse aortic tissues isolated from 26S proteasome reporter and eNOS knockout mice.
24853093	9	58	theme	adenoviral	1382:1391	arg1	overexpression					1393:1406	adenoviral overexpression	1382:1406	adenoviral overexpression of O-GlcNAcase (OGA), the enzyme catalyzing the removal of the O-GlcNAc group,	1382:1485	Consistently, adenoviral overexpression of O-GlcNAcase (OGA), the enzyme catalyzing the removal of the O-GlcNAc group, mimicked the effects of OGT knockdown.
24853093	9	59	theme	group	1480:1484	arg1	removal					1456:1462	the removal	1452:1462	the removal of the O-GlcNAc group	1452:1484	Consistently, adenoviral overexpression of O-GlcNAcase (OGA), the enzyme catalyzing the removal of the O-GlcNAc group, mimicked the effects of OGT knockdown.
24853093	4	60	theme	vascular	559:566	arg1	cells					580:584	vascular endothelial cells	559:584	vascular endothelial cells	559:584	The aim of the present study was to establish the connection between endothelial NO and 26S proteasome functionality in vascular endothelial cells.
24853093	5	61	theme	proteasome	595:604	arg1	levels					623:628	The 26S proteasome reporter protein levels	587:628	The 26S proteasome reporter protein levels	587:628	The 26S proteasome reporter protein levels, 26S proteasome activity, and the O-GlcNAcylation of Rpt2, a key subunit of the proteasome regulatory complex, were assayed in 26S proteasome reporter cells, human umbilical vein endothelial cells (HUVEC), and mouse aortic tissues isolated from 26S proteasome reporter and eNOS knockout mice.
24853093	2	62	theme	proteasome	262:271	arg1	functionality					273:285	proteasome functionality	262:285	proteasome functionality	262:285	However, it remains largely unknown how proteasome functionality is regulated in the vasculature.
24853093	0	63	theme	endogenous	37:46	arg1	inhibitor					48:56	an endogenous inhibitor	34:56	an endogenous inhibitor of 26S proteasomes in vascular endothelial cells	34:105	Identification of nitric oxide as an endogenous inhibitor of 26S proteasomes in vascular endothelial cells.
24853093	10	64	theme	eNOS	1547:1550	arg1	tissues					1569:1575	eNOS wild type aortic tissues	1547:1575	eNOS wild type aortic tissues	1547:1575	Finally, compared to eNOS wild type aortic tissues, 26S proteasome reporter mice lacking eNOS exhibited elevated 26S proteasome functionality in parallel with decreased Rpt2 O-GlcNAcylation, without changing the levels of Rpt2 protein.
24853093	5	65	theme	protein	615:621	arg1	levels					623:628	The 26S proteasome reporter protein levels	587:628	The 26S proteasome reporter protein levels	587:628	The 26S proteasome reporter protein levels, 26S proteasome activity, and the O-GlcNAcylation of Rpt2, a key subunit of the proteasome regulatory complex, were assayed in 26S proteasome reporter cells, human umbilical vein endothelial cells (HUVEC), and mouse aortic tissues isolated from 26S proteasome reporter and eNOS knockout mice.
24853093	1	66	theme	eukaryotic	166:175	arg1	cells					215:219	vascular endothelial cells	194:219	vascular endothelial cells	194:219	The 26S proteasome plays a fundamental role in almost all eukaryotic cells, including vascular endothelial cells.
24853093	1	66	theme	eukaryotic	166:175	arg1	cells					177:181	almost all eukaryotic cells	155:181	almost all eukaryotic cells	155:181	The 26S proteasome plays a fundamental role in almost all eukaryotic cells, including vascular endothelial cells.
24853093	6	67	theme	chymotrypsin-like	1092:1108	arg1	activity					1110:1117	proteasome chymotrypsin-like activity	1081:1117	proteasome chymotrypsin-like activity	1081:1117	Like the other selective NO donors, NO derived from activated eNOS (by pharmacological and genetic approach) increased O-GlcNAc modification of Rpt2, reduced proteasome chymotrypsin-like activity, and caused 26S proteasome reporter protein accumulation.
24853093	5	68	theme	human	788:792	arg1	HUVEC					828:832	HUVEC	828:832	HUVEC	828:832	The 26S proteasome reporter protein levels, 26S proteasome activity, and the O-GlcNAcylation of Rpt2, a key subunit of the proteasome regulatory complex, were assayed in 26S proteasome reporter cells, human umbilical vein endothelial cells (HUVEC), and mouse aortic tissues isolated from 26S proteasome reporter and eNOS knockout mice.
24853093	5	68	theme	human	788:792	arg1	cells					821:825	human umbilical vein endothelial cells	788:825	human umbilical vein endothelial cells (HUVEC)	788:833	The 26S proteasome reporter protein levels, 26S proteasome activity, and the O-GlcNAcylation of Rpt2, a key subunit of the proteasome regulatory complex, were assayed in 26S proteasome reporter cells, human umbilical vein endothelial cells (HUVEC), and mouse aortic tissues isolated from 26S proteasome reporter and eNOS knockout mice.
24853093	5	69	theme	vein	804:807	arg1	HUVEC					828:832	HUVEC	828:832	HUVEC	828:832	The 26S proteasome reporter protein levels, 26S proteasome activity, and the O-GlcNAcylation of Rpt2, a key subunit of the proteasome regulatory complex, were assayed in 26S proteasome reporter cells, human umbilical vein endothelial cells (HUVEC), and mouse aortic tissues isolated from 26S proteasome reporter and eNOS knockout mice.
24853093	5	69	theme	vein	804:807	arg1	cells					821:825	human umbilical vein endothelial cells	788:825	human umbilical vein endothelial cells (HUVEC)	788:833	The 26S proteasome reporter protein levels, 26S proteasome activity, and the O-GlcNAcylation of Rpt2, a key subunit of the proteasome regulatory complex, were assayed in 26S proteasome reporter cells, human umbilical vein endothelial cells (HUVEC), and mouse aortic tissues isolated from 26S proteasome reporter and eNOS knockout mice.
24853093	10	70	theme	type	1557:1560	arg1	tissues					1569:1575	eNOS wild type aortic tissues	1547:1575	eNOS wild type aortic tissues	1547:1575	Finally, compared to eNOS wild type aortic tissues, 26S proteasome reporter mice lacking eNOS exhibited elevated 26S proteasome functionality in parallel with decreased Rpt2 O-GlcNAcylation, without changing the levels of Rpt2 protein.
24853093	5	71	theme	key	691:693	arg1	Rpt2					683:686	Rpt2	683:686	Rpt2	683:686	The 26S proteasome reporter protein levels, 26S proteasome activity, and the O-GlcNAcylation of Rpt2, a key subunit of the proteasome regulatory complex, were assayed in 26S proteasome reporter cells, human umbilical vein endothelial cells (HUVEC), and mouse aortic tissues isolated from 26S proteasome reporter and eNOS knockout mice.
24853093	5	71	theme	key	691:693	arg1	subunit					695:701	a key subunit	689:701	a key subunit of the proteasome regulatory complex	689:738	The 26S proteasome reporter protein levels, 26S proteasome activity, and the O-GlcNAcylation of Rpt2, a key subunit of the proteasome regulatory complex, were assayed in 26S proteasome reporter cells, human umbilical vein endothelial cells (HUVEC), and mouse aortic tissues isolated from 26S proteasome reporter and eNOS knockout mice.
24853093	10	72	theme	protein	1753:1759	arg1	levels					1738:1743	the levels	1734:1743	the levels of Rpt2 protein	1734:1759	Finally, compared to eNOS wild type aortic tissues, 26S proteasome reporter mice lacking eNOS exhibited elevated 26S proteasome functionality in parallel with decreased Rpt2 O-GlcNAcylation, without changing the levels of Rpt2 protein.
24853093	6	73	theme	protein	1155:1161	arg1	accumulation					1163:1174	26S proteasome reporter protein accumulation	1131:1174	26S proteasome reporter protein accumulation	1131:1174	Like the other selective NO donors, NO derived from activated eNOS (by pharmacological and genetic approach) increased O-GlcNAc modification of Rpt2, reduced proteasome chymotrypsin-like activity, and caused 26S proteasome reporter protein accumulation.
24853093	8	74	theme	O-GlcNAc	1255:1262	arg1	enzyme					1291:1296	the key enzyme	1283:1296	the key enzyme that catalyzes protein O-GlcNAcylation	1283:1335	SiRNA knockdown of O-GlcNAc transferase (OGT), the key enzyme that catalyzes protein O-GlcNAcylation, abolished NO-induced effects.
24853093	8	74	theme	O-GlcNAc	1255:1262	arg1	OGT					1277:1279	OGT	1277:1279	OGT	1277:1279	SiRNA knockdown of O-GlcNAc transferase (OGT), the key enzyme that catalyzes protein O-GlcNAcylation, abolished NO-induced effects.
24853093	8	74	theme	O-GlcNAc	1255:1262	arg1	transferase					1264:1274	O-GlcNAc transferase	1255:1274	O-GlcNAc transferase (OGT)	1255:1280	SiRNA knockdown of O-GlcNAc transferase (OGT), the key enzyme that catalyzes protein O-GlcNAcylation, abolished NO-induced effects.
24853093	5	75	theme	proteasome	710:719	arg1	complex					732:738	the proteasome regulatory complex	706:738	the proteasome regulatory complex	706:738	The 26S proteasome reporter protein levels, 26S proteasome activity, and the O-GlcNAcylation of Rpt2, a key subunit of the proteasome regulatory complex, were assayed in 26S proteasome reporter cells, human umbilical vein endothelial cells (HUVEC), and mouse aortic tissues isolated from 26S proteasome reporter and eNOS knockout mice.
24853093	3	76	theme	oxide	339:343	arg1	eNOS					360:363	eNOS	360:363	eNOS	360:363	Endothelial nitric oxide (NO) synthase (eNOS)-derived NO is known to be essential to maintain endothelial homeostasis.
24853093	3	76	theme	oxide	339:343	arg1	synthase					350:357	Endothelial nitric oxide (NO) synthase	320:357	Endothelial nitric oxide (NO) synthase (eNOS)-derived NO	320:375	Endothelial nitric oxide (NO) synthase (eNOS)-derived NO is known to be essential to maintain endothelial homeostasis.
24853093	6	77	theme	proteasome	1135:1144	arg1	accumulation					1163:1174	26S proteasome reporter protein accumulation	1131:1174	26S proteasome reporter protein accumulation	1131:1174	Like the other selective NO donors, NO derived from activated eNOS (by pharmacological and genetic approach) increased O-GlcNAc modification of Rpt2, reduced proteasome chymotrypsin-like activity, and caused 26S proteasome reporter protein accumulation.
24853093	5	78	theme	complex	732:738	arg1	Rpt2					683:686	Rpt2	683:686	Rpt2	683:686	The 26S proteasome reporter protein levels, 26S proteasome activity, and the O-GlcNAcylation of Rpt2, a key subunit of the proteasome regulatory complex, were assayed in 26S proteasome reporter cells, human umbilical vein endothelial cells (HUVEC), and mouse aortic tissues isolated from 26S proteasome reporter and eNOS knockout mice.
24853093	5	78	theme	complex	732:738	arg1	subunit					695:701	a key subunit	689:701	a key subunit of the proteasome regulatory complex	689:738	The 26S proteasome reporter protein levels, 26S proteasome activity, and the O-GlcNAcylation of Rpt2, a key subunit of the proteasome regulatory complex, were assayed in 26S proteasome reporter cells, human umbilical vein endothelial cells (HUVEC), and mouse aortic tissues isolated from 26S proteasome reporter and eNOS knockout mice.
24853093	5	79	theme	mouse	840:844	arg1	tissues					853:859	mouse aortic tissues	840:859	mouse aortic tissues	840:859	The 26S proteasome reporter protein levels, 26S proteasome activity, and the O-GlcNAcylation of Rpt2, a key subunit of the proteasome regulatory complex, were assayed in 26S proteasome reporter cells, human umbilical vein endothelial cells (HUVEC), and mouse aortic tissues isolated from 26S proteasome reporter and eNOS knockout mice.
24853093	6	80	theme	NO	948:949	arg1	donors					951:956	the other selective NO donors	928:956	the other selective NO donors	928:956	Like the other selective NO donors, NO derived from activated eNOS (by pharmacological and genetic approach) increased O-GlcNAc modification of Rpt2, reduced proteasome chymotrypsin-like activity, and caused 26S proteasome reporter protein accumulation.
24853093	3	81	theme	Endothelial	320:330	arg1	eNOS					360:363	eNOS	360:363	eNOS	360:363	Endothelial nitric oxide (NO) synthase (eNOS)-derived NO is known to be essential to maintain endothelial homeostasis.
24853093	3	81	theme	Endothelial	320:330	arg1	synthase					350:357	Endothelial nitric oxide (NO) synthase	320:357	Endothelial nitric oxide (NO) synthase (eNOS)-derived NO	320:375	Endothelial nitric oxide (NO) synthase (eNOS)-derived NO is known to be essential to maintain endothelial homeostasis.
24853093	0	82	theme	endothelial	89:99	arg1	cells					101:105	vascular endothelial cells	80:105	vascular endothelial cells	80:105	Identification of nitric oxide as an endogenous inhibitor of 26S proteasomes in vascular endothelial cells.
24853093	5	83	theme	knockout	908:915	arg1	mice					917:920	26S proteasome reporter and eNOS knockout mice	875:920	mice	917:920	The 26S proteasome reporter protein levels, 26S proteasome activity, and the O-GlcNAcylation of Rpt2, a key subunit of the proteasome regulatory complex, were assayed in 26S proteasome reporter cells, human umbilical vein endothelial cells (HUVEC), and mouse aortic tissues isolated from 26S proteasome reporter and eNOS knockout mice.
24853093	6	84	theme	other	932:936	arg1	donors					951:956	the other selective NO donors	928:956	the other selective NO donors	928:956	Like the other selective NO donors, NO derived from activated eNOS (by pharmacological and genetic approach) increased O-GlcNAc modification of Rpt2, reduced proteasome chymotrypsin-like activity, and caused 26S proteasome reporter protein accumulation.
24853093	3	85	theme	synthase	350:357	arg1	NO					374:375	Endothelial nitric oxide (NO) synthase (eNOS)-derived NO	320:375	Endothelial nitric oxide (NO) synthase (eNOS)-derived NO	320:375	Endothelial nitric oxide (NO) synthase (eNOS)-derived NO is known to be essential to maintain endothelial homeostasis.
24853093	0	86	from	inhibitor	48:56	arg1	cells					101:105	vascular endothelial cells	80:105	vascular endothelial cells	80:105	Identification of nitric oxide as an endogenous inhibitor of 26S proteasomes in vascular endothelial cells.
24853093	5	87	theme	26S	591:593	arg1	levels					623:628	The 26S proteasome reporter protein levels	587:628	The 26S proteasome reporter protein levels	587:628	The 26S proteasome reporter protein levels, 26S proteasome activity, and the O-GlcNAcylation of Rpt2, a key subunit of the proteasome regulatory complex, were assayed in 26S proteasome reporter cells, human umbilical vein endothelial cells (HUVEC), and mouse aortic tissues isolated from 26S proteasome reporter and eNOS knockout mice.
24853093	6	88	theme	genetic	1014:1020	arg1	approach					1022:1029	pharmacological and genetic approach	994:1029	pharmacological and genetic approach	994:1029	Like the other selective NO donors, NO derived from activated eNOS (by pharmacological and genetic approach) increased O-GlcNAc modification of Rpt2, reduced proteasome chymotrypsin-like activity, and caused 26S proteasome reporter protein accumulation.
24853093	3	89	theme	NO	346:347	arg1	eNOS					360:363	eNOS	360:363	eNOS	360:363	Endothelial nitric oxide (NO) synthase (eNOS)-derived NO is known to be essential to maintain endothelial homeostasis.
24853093	3	89	theme	NO	346:347	arg1	synthase					350:357	Endothelial nitric oxide (NO) synthase	320:357	Endothelial nitric oxide (NO) synthase (eNOS)-derived NO	320:375	Endothelial nitric oxide (NO) synthase (eNOS)-derived NO is known to be essential to maintain endothelial homeostasis.
24853093	4	90	theme	present	454:460	arg1	study					462:466	the present study	450:466	the present study	450:466	The aim of the present study was to establish the connection between endothelial NO and 26S proteasome functionality in vascular endothelial cells.
24853093	10	91	theme	proteasome	1582:1591	arg1	mice					1602:1605	26S proteasome reporter mice	1578:1605	26S proteasome reporter mice lacking eNOS	1578:1618	Finally, compared to eNOS wild type aortic tissues, 26S proteasome reporter mice lacking eNOS exhibited elevated 26S proteasome functionality in parallel with decreased Rpt2 O-GlcNAcylation, without changing the levels of Rpt2 protein.
24853093	5	92	theme	proteasome	761:770	arg1	cells					781:785	26S proteasome reporter cells	757:785	26S proteasome reporter cells	757:785	The 26S proteasome reporter protein levels, 26S proteasome activity, and the O-GlcNAcylation of Rpt2, a key subunit of the proteasome regulatory complex, were assayed in 26S proteasome reporter cells, human umbilical vein endothelial cells (HUVEC), and mouse aortic tissues isolated from 26S proteasome reporter and eNOS knockout mice.
24853093	4	93	dep	NO	520:521	arg1	functionality					542:554	functionality	542:554	functionality	542:554	The aim of the present study was to establish the connection between endothelial NO and 26S proteasome functionality in vascular endothelial cells.
24853093	5	94	theme	proteasome	879:888	arg1	reporter					890:897	26S proteasome reporter and eNOS knockout mice	875:920	reporter	890:897	The 26S proteasome reporter protein levels, 26S proteasome activity, and the O-GlcNAcylation of Rpt2, a key subunit of the proteasome regulatory complex, were assayed in 26S proteasome reporter cells, human umbilical vein endothelial cells (HUVEC), and mouse aortic tissues isolated from 26S proteasome reporter and eNOS knockout mice.
24853093	6	95	theme	pharmacological	994:1008	arg1	approach					1022:1029	pharmacological and genetic approach	994:1029	pharmacological and genetic approach	994:1029	Like the other selective NO donors, NO derived from activated eNOS (by pharmacological and genetic approach) increased O-GlcNAc modification of Rpt2, reduced proteasome chymotrypsin-like activity, and caused 26S proteasome reporter protein accumulation.
24853093	3	96	theme	-derived	365:372	arg1	NO					374:375	Endothelial nitric oxide (NO) synthase (eNOS)-derived NO	320:375	Endothelial nitric oxide (NO) synthase (eNOS)-derived NO	320:375	Endothelial nitric oxide (NO) synthase (eNOS)-derived NO is known to be essential to maintain endothelial homeostasis.
24853093	11	97	theme	proteasome	1848:1857	arg1	suppressor					1826:1835	a physiological suppressor	1810:1835	a physiological suppressor of the 26S proteasome in vascular endothelial cells	1810:1887	In conclusion, the eNOS-derived NO functions as a physiological suppressor of the 26S proteasome in vascular endothelial cells.
24853093	11	97	theme	proteasome	1848:1857	arg1	NO					1794:1795	the eNOS-derived NO	1777:1795	the eNOS-derived NO	1777:1795	In conclusion, the eNOS-derived NO functions as a physiological suppressor of the 26S proteasome in vascular endothelial cells.
24853093	0	98	theme	oxide	25:29	arg1	Identification					0:13	Identification	0:13	Identification of nitric oxide as an endogenous inhibitor of 26S proteasomes in vascular endothelial cells.	0:106	Identification of nitric oxide as an endogenous inhibitor of 26S proteasomes in vascular endothelial cells.
24853093	1	99	theme	vascular	194:201	arg1	cells					215:219	vascular endothelial cells	194:219	vascular endothelial cells	194:219	The 26S proteasome plays a fundamental role in almost all eukaryotic cells, including vascular endothelial cells.
24853093	6	100	theme	activated	975:983	arg1	eNOS					985:988	activated eNOS	975:988	activated eNOS (by pharmacological and genetic approach)	975:1030	Like the other selective NO donors, NO derived from activated eNOS (by pharmacological and genetic approach) increased O-GlcNAc modification of Rpt2, reduced proteasome chymotrypsin-like activity, and caused 26S proteasome reporter protein accumulation.
24853093	4	101	from	connection	489:498	arg1	cells					580:584	vascular endothelial cells	559:584	vascular endothelial cells	559:584	The aim of the present study was to establish the connection between endothelial NO and 26S proteasome functionality in vascular endothelial cells.
24853093	4	102	theme	endothelial	508:518	arg1	NO					520:521	endothelial NO	508:521	endothelial NO	508:521	The aim of the present study was to establish the connection between endothelial NO and 26S proteasome functionality in vascular endothelial cells.
24853093	10	103	theme	proteasome	1643:1652	arg1	functionality					1654:1666	elevated 26S proteasome functionality	1630:1666	elevated 26S proteasome functionality	1630:1666	Finally, compared to eNOS wild type aortic tissues, 26S proteasome reporter mice lacking eNOS exhibited elevated 26S proteasome functionality in parallel with decreased Rpt2 O-GlcNAcylation, without changing the levels of Rpt2 protein.
24853093	10	104	theme	elevated	1630:1637	arg1	proteasome					1643:1652	elevated 26S proteasome	1630:1652	elevated 26S proteasome functionality	1630:1666	Finally, compared to eNOS wild type aortic tissues, 26S proteasome reporter mice lacking eNOS exhibited elevated 26S proteasome functionality in parallel with decreased Rpt2 O-GlcNAcylation, without changing the levels of Rpt2 protein.
24853093	5	105	theme	endothelial	809:819	arg1	HUVEC					828:832	HUVEC	828:832	HUVEC	828:832	The 26S proteasome reporter protein levels, 26S proteasome activity, and the O-GlcNAcylation of Rpt2, a key subunit of the proteasome regulatory complex, were assayed in 26S proteasome reporter cells, human umbilical vein endothelial cells (HUVEC), and mouse aortic tissues isolated from 26S proteasome reporter and eNOS knockout mice.
24853093	5	105	theme	endothelial	809:819	arg1	cells					821:825	human umbilical vein endothelial cells	788:825	human umbilical vein endothelial cells (HUVEC)	788:833	The 26S proteasome reporter protein levels, 26S proteasome activity, and the O-GlcNAcylation of Rpt2, a key subunit of the proteasome regulatory complex, were assayed in 26S proteasome reporter cells, human umbilical vein endothelial cells (HUVEC), and mouse aortic tissues isolated from 26S proteasome reporter and eNOS knockout mice.
24853093	6	106	theme	O-GlcNAc	1042:1049	arg1	modification					1051:1062	O-GlcNAc modification	1042:1062	O-GlcNAc modification of Rpt2	1042:1070	Like the other selective NO donors, NO derived from activated eNOS (by pharmacological and genetic approach) increased O-GlcNAc modification of Rpt2, reduced proteasome chymotrypsin-like activity, and caused 26S proteasome reporter protein accumulation.
24853093	11	107	theme	vascular	1862:1869	arg1	cells					1883:1887	vascular endothelial cells	1862:1887	vascular endothelial cells	1862:1887	In conclusion, the eNOS-derived NO functions as a physiological suppressor of the 26S proteasome in vascular endothelial cells.
24853093	11	108	theme	eNOS-derived	1781:1792	arg1	suppressor					1826:1835	a physiological suppressor	1810:1835	a physiological suppressor of the 26S proteasome in vascular endothelial cells	1810:1887	In conclusion, the eNOS-derived NO functions as a physiological suppressor of the 26S proteasome in vascular endothelial cells.
24853093	11	108	theme	eNOS-derived	1781:1792	arg1	NO					1794:1795	the eNOS-derived NO	1777:1795	the eNOS-derived NO	1777:1795	In conclusion, the eNOS-derived NO functions as a physiological suppressor of the 26S proteasome in vascular endothelial cells.
25541949	0	0	theme	independent	71:81	arg1	SIRT1					64:68	SIRT1	64:68	SIRT1	64:68	Upregulation of Unc-51-like kinase 1 by nitric oxide stabilizes SIRT1, independent of autophagy.
25541949	3	1	theme	emerging	303:310	arg1	evidence					312:319	emerging evidence	303:319	emerging evidence	303:319	However, emerging evidence suggests that endothelial nitric oxide synthase (eNOS) positively regulates SIRT1 protein expression.
25541949	13	2	theme	subunit	1699:1705	arg1	Rpt2					1707:1710	proteasomal subunit Rpt2	1687:1710	proteasomal subunit Rpt2	1687:1710	Mechanistically, ULK1 negatively regulated 26S proteasome functionality, which was at least partly mediated by O-linked-GlcNAc transferase (OGT), probably by increased O-GlcNAc modification of proteasomal subunit Rpt2.
25541949	1	3	theme	vascular	134:141	arg1	health					143:148	the lifespan and vascular health	117:148	the lifespan and vascular health	117:148	SIRT1 is central to the lifespan and vascular health, but undergoes degradation that contributes to several medical conditions, including diabetes.
25541949	4	4	theme	functionality	494:506	arg1	inhibitor					466:474	an endogenous inhibitor	452:474	an endogenous inhibitor of 26S proteasome functionality with a cellular reporter system	452:538	We recently identified NO as an endogenous inhibitor of 26S proteasome functionality with a cellular reporter system.
25541949	4	4	theme	functionality	494:506	arg1	NO					446:447	NO	446:447	NO	446:447	We recently identified NO as an endogenous inhibitor of 26S proteasome functionality with a cellular reporter system.
25541949	4	5	theme	cellular	515:522	arg1	system					533:538	a cellular reporter system	513:538	a cellular reporter system	513:538	We recently identified NO as an endogenous inhibitor of 26S proteasome functionality with a cellular reporter system.
25541949	4	6	with	inhibitor	466:474	arg1	system					533:538	a cellular reporter system	513:538	a cellular reporter system	513:538	We recently identified NO as an endogenous inhibitor of 26S proteasome functionality with a cellular reporter system.
25541949	8	7	from	mice	1052:1055	arg1	MEF					1034:1036	MEF	1034:1036	MEF	1034:1036	NO also stabilized an autophagy-related protein unc-51 like kinase (ULK1), but did not restore SIRT1 protein levels in ULK1-siRNA-treated cells or in mouse embryonic fibroblasts (MEF) from Ulk1-/- mice.
25541949	8	7	from	mice	1052:1055	arg1	levels					964:969	SIRT1 protein levels	950:969	SIRT1 protein levels in ULK1-siRNA-treated cells or in mouse embryonic fibroblasts (MEF) from Ulk1-/- mice	950:1055	NO also stabilized an autophagy-related protein unc-51 like kinase (ULK1), but did not restore SIRT1 protein levels in ULK1-siRNA-treated cells or in mouse embryonic fibroblasts (MEF) from Ulk1-/- mice.
25541949	8	7	from	mice	1052:1055	arg1	fibroblasts					1021:1031	mouse embryonic fibroblasts	1005:1031	mouse embryonic fibroblasts (MEF) from Ulk1-/- mice	1005:1055	NO also stabilized an autophagy-related protein unc-51 like kinase (ULK1), but did not restore SIRT1 protein levels in ULK1-siRNA-treated cells or in mouse embryonic fibroblasts (MEF) from Ulk1-/- mice.
25541949	0	8	theme	autophagy	86:94	arg1	independent					71:81	independent	71:81	independent	71:81	Upregulation of Unc-51-like kinase 1 by nitric oxide stabilizes SIRT1, independent of autophagy.
25541949	13	9	theme	increased	1652:1660	arg1	modification					1671:1682	increased O-GlcNAc modification	1652:1682	increased O-GlcNAc modification of proteasomal subunit Rpt2	1652:1710	Mechanistically, ULK1 negatively regulated 26S proteasome functionality, which was at least partly mediated by O-linked-GlcNAc transferase (OGT), probably by increased O-GlcNAc modification of proteasomal subunit Rpt2.
25541949	9	10	theme	SIRT1	1112:1116	arg1	regulation					1098:1107	the NO regulation	1091:1107	the NO regulation of SIRT1	1091:1116	This suggests that ULK1 mediated the NO regulation of SIRT1.
25541949	13	11	mod	modification	1671:1682	arg3	O-GlcNAc					1662:1669	increased O-GlcNAc modification	1652:1682	increased O-GlcNAc modification of proteasomal subunit Rpt2	1652:1710	Mechanistically, ULK1 negatively regulated 26S proteasome functionality, which was at least partly mediated by O-linked-GlcNAc transferase (OGT), probably by increased O-GlcNAc modification of proteasomal subunit Rpt2.
25541949	13	11	mod	modification	1671:1682	arg1	Rpt2					1707:1710	proteasomal subunit Rpt2	1687:1710	proteasomal subunit Rpt2	1687:1710	Mechanistically, ULK1 negatively regulated 26S proteasome functionality, which was at least partly mediated by O-linked-GlcNAc transferase (OGT), probably by increased O-GlcNAc modification of proteasomal subunit Rpt2.
25541949	13	12	theme	26S	1537:1539	arg1	proteasome					1541:1550	26S proteasome	1537:1550	26S proteasome functionality	1537:1564	Mechanistically, ULK1 negatively regulated 26S proteasome functionality, which was at least partly mediated by O-linked-GlcNAc transferase (OGT), probably by increased O-GlcNAc modification of proteasomal subunit Rpt2.
25541949	10	13	theme	adenoviral	1132:1141	arg1	overexpression					1143:1156	adenoviral overexpression	1132:1156	adenoviral overexpression of ULK1	1132:1164	Furthermore, adenoviral overexpression of ULK1 increased SIRT1 protein expression, while ULK1 siRNA treatment decreased it.
25541949	8	14	theme	ULK1-siRNA-treated	974:991	arg1	cells					993:997	ULK1-siRNA-treated cells	974:997	ULK1-siRNA-treated cells	974:997	NO also stabilized an autophagy-related protein unc-51 like kinase (ULK1), but did not restore SIRT1 protein levels in ULK1-siRNA-treated cells or in mouse embryonic fibroblasts (MEF) from Ulk1-/- mice.
25541949	5	15	theme	SIRT1	605:609	arg1	breakdown					619:627	SIRT1 protein breakdown	605:627	SIRT1 protein breakdown	605:627	Here we extended this finding to a novel pathway that regulates SIRT1 protein breakdown.
25541949	7	16	theme	mRNA	819:822	arg1	expression					824:833	mRNA expression	819:833	mRNA expression	819:833	Similarly, NO enhanced SIRT1 protein, but not mRNA expression, in CHX-free cells.
25541949	3	17	theme	endothelial	335:345	arg1	eNOS					370:373	eNOS	370:373	eNOS	370:373	However, emerging evidence suggests that endothelial nitric oxide synthase (eNOS) positively regulates SIRT1 protein expression.
25541949	3	17	theme	endothelial	335:345	arg1	synthase					360:367	endothelial nitric oxide synthase	335:367	endothelial nitric oxide synthase (eNOS)	335:374	However, emerging evidence suggests that endothelial nitric oxide synthase (eNOS) positively regulates SIRT1 protein expression.
25541949	5	18	theme	protein	611:617	arg1	breakdown					619:627	SIRT1 protein breakdown	605:627	SIRT1 protein breakdown	605:627	Here we extended this finding to a novel pathway that regulates SIRT1 protein breakdown.
25541949	6	19	theme	NO	692:693	arg1	NONOate					680:686	NONOate	680:686	NONOate	680:686	In cycloheximide (CHX)-treated endothelial cells, NONOate, an NO donor, and A23187, an eNOS activator, significantly stabilized SIRT1 protein.
25541949	6	19	theme	NO	692:693	arg1	donor					695:699	an NO donor	689:699	an NO donor	689:699	In cycloheximide (CHX)-treated endothelial cells, NONOate, an NO donor, and A23187, an eNOS activator, significantly stabilized SIRT1 protein.
25541949	0	20	theme	nitric	40:45	arg1	oxide					47:51	nitric oxide	40:51	nitric oxide	40:51	Upregulation of Unc-51-like kinase 1 by nitric oxide stabilizes SIRT1, independent of autophagy.
25541949	4	21	theme	proteasome	483:492	arg1	functionality					494:506	26S proteasome functionality	479:506	26S proteasome functionality	479:506	We recently identified NO as an endogenous inhibitor of 26S proteasome functionality with a cellular reporter system.
25541949	14	22	dep	downregulated	1923:1935	arg1	heart					1947:1951	heart	1947:1951	heart	1947:1951	The NO-ULK1-SIRT1 axis was likely operative in the whole animal: both ULK1 and SIRT1 protein levels were significantly reduced in tissue homogenates in eNOS-knockout mice (lung) and in db/db mice where eNOS is downregulated (lung and heart).
25541949	14	22	dep	downregulated	1923:1935	arg1	lung					1938:1941	lung	1938:1941	lung	1938:1941	The NO-ULK1-SIRT1 axis was likely operative in the whole animal: both ULK1 and SIRT1 protein levels were significantly reduced in tissue homogenates in eNOS-knockout mice (lung) and in db/db mice where eNOS is downregulated (lung and heart).
25541949	14	23	theme	eNOS-knockout	1865:1877	arg1	lung					1885:1888	lung	1885:1888	lung	1885:1888	The NO-ULK1-SIRT1 axis was likely operative in the whole animal: both ULK1 and SIRT1 protein levels were significantly reduced in tissue homogenates in eNOS-knockout mice (lung) and in db/db mice where eNOS is downregulated (lung and heart).
25541949	14	23	theme	eNOS-knockout	1865:1877	arg1	mice					1879:1882	eNOS-knockout mice	1865:1882	eNOS-knockout mice (lung)	1865:1889	The NO-ULK1-SIRT1 axis was likely operative in the whole animal: both ULK1 and SIRT1 protein levels were significantly reduced in tissue homogenates in eNOS-knockout mice (lung) and in db/db mice where eNOS is downregulated (lung and heart).
25541949	13	24	theme	Rpt2	1707:1710	arg1	modification					1671:1682	increased O-GlcNAc modification	1652:1682	increased O-GlcNAc modification of proteasomal subunit Rpt2	1652:1710	Mechanistically, ULK1 negatively regulated 26S proteasome functionality, which was at least partly mediated by O-linked-GlcNAc transferase (OGT), probably by increased O-GlcNAc modification of proteasomal subunit Rpt2.
25541949	4	25	theme	26S	479:481	arg1	proteasome					483:492	26S proteasome	479:492	26S proteasome functionality	479:506	We recently identified NO as an endogenous inhibitor of 26S proteasome functionality with a cellular reporter system.
25541949	8	26	theme	embryonic	1011:1019	arg1	MEF					1034:1036	MEF	1034:1036	MEF	1034:1036	NO also stabilized an autophagy-related protein unc-51 like kinase (ULK1), but did not restore SIRT1 protein levels in ULK1-siRNA-treated cells or in mouse embryonic fibroblasts (MEF) from Ulk1-/- mice.
25541949	8	26	theme	embryonic	1011:1019	arg1	fibroblasts					1021:1031	mouse embryonic fibroblasts	1005:1031	mouse embryonic fibroblasts (MEF) from Ulk1-/- mice	1005:1055	NO also stabilized an autophagy-related protein unc-51 like kinase (ULK1), but did not restore SIRT1 protein levels in ULK1-siRNA-treated cells or in mouse embryonic fibroblasts (MEF) from Ulk1-/- mice.
25541949	6	27	theme	SIRT1	758:762	arg1	protein					764:770	SIRT1 protein	758:770	SIRT1 protein	758:770	In cycloheximide (CHX)-treated endothelial cells, NONOate, an NO donor, and A23187, an eNOS activator, significantly stabilized SIRT1 protein.
25541949	10	28	theme	siRNA	1213:1217	arg1	treatment					1219:1227	ULK1 siRNA treatment	1208:1227	ULK1 siRNA treatment	1208:1227	Furthermore, adenoviral overexpression of ULK1 increased SIRT1 protein expression, while ULK1 siRNA treatment decreased it.
25541949	8	29	theme	mouse	1005:1009	arg1	MEF					1034:1036	MEF	1034:1036	MEF	1034:1036	NO also stabilized an autophagy-related protein unc-51 like kinase (ULK1), but did not restore SIRT1 protein levels in ULK1-siRNA-treated cells or in mouse embryonic fibroblasts (MEF) from Ulk1-/- mice.
25541949	8	29	theme	mouse	1005:1009	arg1	fibroblasts					1021:1031	mouse embryonic fibroblasts	1005:1031	mouse embryonic fibroblasts (MEF) from Ulk1-/- mice	1005:1055	NO also stabilized an autophagy-related protein unc-51 like kinase (ULK1), but did not restore SIRT1 protein levels in ULK1-siRNA-treated cells or in mouse embryonic fibroblasts (MEF) from Ulk1-/- mice.
25541949	5	30	theme	novel	576:580	arg1	pathway					582:588	a novel pathway	574:588	a novel pathway that regulates SIRT1 protein breakdown	574:627	Here we extended this finding to a novel pathway that regulates SIRT1 protein breakdown.
25541949	10	31	theme	ULK1	1208:1211	arg1	treatment					1219:1227	ULK1 siRNA treatment	1208:1227	ULK1 siRNA treatment	1208:1227	Furthermore, adenoviral overexpression of ULK1 increased SIRT1 protein expression, while ULK1 siRNA treatment decreased it.
25541949	12	32	with	Treatment	1364:1372	arg1	MG132					1379:1383	MG132	1379:1383	MG132	1379:1383	Treatment with MG132, a proteasome inhibitor, or siRNA of β-TrCP1, an E3 ligase, prevented SIRT1 reduction induced by ULK1-siRNA.
25541949	12	32	with	Treatment	1364:1372	arg1	inhibitor					1399:1407	a proteasome inhibitor	1386:1407	a proteasome inhibitor	1386:1407	Treatment with MG132, a proteasome inhibitor, or siRNA of β-TrCP1, an E3 ligase, prevented SIRT1 reduction induced by ULK1-siRNA.
25541949	12	32	with	Treatment	1364:1372	arg1	siRNA					1413:1417	siRNA	1413:1417	siRNA	1413:1417	Treatment with MG132, a proteasome inhibitor, or siRNA of β-TrCP1, an E3 ligase, prevented SIRT1 reduction induced by ULK1-siRNA.
25541949	0	33	theme	kinase	28:33	arg1	Upregulation					0:11	Upregulation	0:11	Upregulation of Unc-51-like kinase 1 by nitric oxide	0:51	Upregulation of Unc-51-like kinase 1 by nitric oxide stabilizes SIRT1, independent of autophagy.
25541949	8	34	theme	protein	956:962	arg1	levels					964:969	SIRT1 protein levels	950:969	SIRT1 protein levels in ULK1-siRNA-treated cells or in mouse embryonic fibroblasts (MEF) from Ulk1-/- mice	950:1055	NO also stabilized an autophagy-related protein unc-51 like kinase (ULK1), but did not restore SIRT1 protein levels in ULK1-siRNA-treated cells or in mouse embryonic fibroblasts (MEF) from Ulk1-/- mice.
25541949	3	35	theme	oxide	354:358	arg1	eNOS					370:373	eNOS	370:373	eNOS	370:373	However, emerging evidence suggests that endothelial nitric oxide synthase (eNOS) positively regulates SIRT1 protein expression.
25541949	3	35	theme	oxide	354:358	arg1	synthase					360:367	endothelial nitric oxide synthase	335:367	endothelial nitric oxide synthase (eNOS)	335:374	However, emerging evidence suggests that endothelial nitric oxide synthase (eNOS) positively regulates SIRT1 protein expression.
25541949	8	36	theme	SIRT1	950:954	arg1	levels					964:969	SIRT1 protein levels	950:969	SIRT1 protein levels in ULK1-siRNA-treated cells or in mouse embryonic fibroblasts (MEF) from Ulk1-/- mice	950:1055	NO also stabilized an autophagy-related protein unc-51 like kinase (ULK1), but did not restore SIRT1 protein levels in ULK1-siRNA-treated cells or in mouse embryonic fibroblasts (MEF) from Ulk1-/- mice.
25541949	14	37	theme	tissue	1843:1848	arg1	homogenates					1850:1860	tissue homogenates	1843:1860	tissue homogenates	1843:1860	The NO-ULK1-SIRT1 axis was likely operative in the whole animal: both ULK1 and SIRT1 protein levels were significantly reduced in tissue homogenates in eNOS-knockout mice (lung) and in db/db mice where eNOS is downregulated (lung and heart).
25541949	0	38	theme	Unc-51-like	16:26	arg1	kinase					28:33	Unc-51-like kinase 1	16:35	Unc-51-like kinase 1	16:35	Upregulation of Unc-51-like kinase 1 by nitric oxide stabilizes SIRT1, independent of autophagy.
25541949	7	39	theme	SIRT1	796:800	arg1	protein					802:808	SIRT1 protein	796:808	SIRT1 protein	796:808	Similarly, NO enhanced SIRT1 protein, but not mRNA expression, in CHX-free cells.
25541949	15	40	theme	endothelial	2100:2110	arg1	cells					2112:2116	endothelial cells	2100:2116	endothelial cells	2100:2116	Taken together, the results show that NO stabilizes SIRT1 by regulating 26S proteasome functionality through ULK1 and OGT, but not autophagy, in endothelial cells.
25541949	3	41	theme	protein	403:409	arg1	expression					411:420	SIRT1 protein expression	397:420	SIRT1 protein expression	397:420	However, emerging evidence suggests that endothelial nitric oxide synthase (eNOS) positively regulates SIRT1 protein expression.
25541949	8	42	from	levels	964:969	arg1	MEF					1034:1036	MEF	1034:1036	MEF	1034:1036	NO also stabilized an autophagy-related protein unc-51 like kinase (ULK1), but did not restore SIRT1 protein levels in ULK1-siRNA-treated cells or in mouse embryonic fibroblasts (MEF) from Ulk1-/- mice.
25541949	8	42	from	levels	964:969	arg1	fibroblasts					1021:1031	mouse embryonic fibroblasts	1005:1031	mouse embryonic fibroblasts (MEF) from Ulk1-/- mice	1005:1055	NO also stabilized an autophagy-related protein unc-51 like kinase (ULK1), but did not restore SIRT1 protein levels in ULK1-siRNA-treated cells or in mouse embryonic fibroblasts (MEF) from Ulk1-/- mice.
25541949	8	42	from	levels	964:969	arg1	cells					993:997	ULK1-siRNA-treated cells	974:997	ULK1-siRNA-treated cells	974:997	NO also stabilized an autophagy-related protein unc-51 like kinase (ULK1), but did not restore SIRT1 protein levels in ULK1-siRNA-treated cells or in mouse embryonic fibroblasts (MEF) from Ulk1-/- mice.
25541949	8	42	from	levels	964:969	arg1	mice					1052:1055	Ulk1-/- mice	1044:1055	Ulk1-/- mice	1044:1055	NO also stabilized an autophagy-related protein unc-51 like kinase (ULK1), but did not restore SIRT1 protein levels in ULK1-siRNA-treated cells or in mouse embryonic fibroblasts (MEF) from Ulk1-/- mice.
25541949	13	43	theme	O-linked-GlcNAc	1605:1619	arg1	OGT					1634:1636	OGT	1634:1636	OGT	1634:1636	Mechanistically, ULK1 negatively regulated 26S proteasome functionality, which was at least partly mediated by O-linked-GlcNAc transferase (OGT), probably by increased O-GlcNAc modification of proteasomal subunit Rpt2.
25541949	13	43	theme	O-linked-GlcNAc	1605:1619	arg1	transferase					1621:1631	O-linked-GlcNAc transferase	1605:1631	O-linked-GlcNAc transferase (OGT)	1605:1637	Mechanistically, ULK1 negatively regulated 26S proteasome functionality, which was at least partly mediated by O-linked-GlcNAc transferase (OGT), probably by increased O-GlcNAc modification of proteasomal subunit Rpt2.
25541949	12	44	theme	E3	1434:1435	arg1	ligase					1437:1442	an E3 ligase	1431:1442	an E3 ligase	1431:1442	Treatment with MG132, a proteasome inhibitor, or siRNA of β-TrCP1, an E3 ligase, prevented SIRT1 reduction induced by ULK1-siRNA.
25541949	12	44	theme	E3	1434:1435	arg1	β-TrCP1					1422:1428	β-TrCP1	1422:1428	β-TrCP1	1422:1428	Treatment with MG132, a proteasome inhibitor, or siRNA of β-TrCP1, an E3 ligase, prevented SIRT1 reduction induced by ULK1-siRNA.
25541949	15	45	theme	proteasome	2031:2040	arg1	functionality					2042:2054	26S proteasome functionality	2027:2054	26S proteasome functionality	2027:2054	Taken together, the results show that NO stabilizes SIRT1 by regulating 26S proteasome functionality through ULK1 and OGT, but not autophagy, in endothelial cells.
25541949	6	46	theme	endothelial	661:671	arg1	cells					673:677	cycloheximide (CHX)-treated endothelial cells	633:677	cycloheximide (CHX)-treated endothelial cells	633:677	In cycloheximide (CHX)-treated endothelial cells, NONOate, an NO donor, and A23187, an eNOS activator, significantly stabilized SIRT1 protein.
25541949	10	47	theme	protein	1182:1188	arg1	expression					1190:1199	SIRT1 protein expression	1176:1199	SIRT1 protein expression	1176:1199	Furthermore, adenoviral overexpression of ULK1 increased SIRT1 protein expression, while ULK1 siRNA treatment decreased it.
25541949	12	48	theme	SIRT1	1455:1459	arg1	reduction					1461:1469	SIRT1 reduction	1455:1469	SIRT1 reduction induced by ULK1-siRNA	1455:1491	Treatment with MG132, a proteasome inhibitor, or siRNA of β-TrCP1, an E3 ligase, prevented SIRT1 reduction induced by ULK1-siRNA.
25541949	4	49	theme	endogenous	455:464	arg1	inhibitor					466:474	an endogenous inhibitor	452:474	an endogenous inhibitor of 26S proteasome functionality with a cellular reporter system	452:538	We recently identified NO as an endogenous inhibitor of 26S proteasome functionality with a cellular reporter system.
25541949	4	49	theme	endogenous	455:464	arg1	NO					446:447	NO	446:447	NO	446:447	We recently identified NO as an endogenous inhibitor of 26S proteasome functionality with a cellular reporter system.
25541949	14	50	from	animal	1770:1775	arg1	axis					1731:1734	The NO-ULK1-SIRT1 axis	1713:1734	The NO-ULK1-SIRT1 axis	1713:1734	The NO-ULK1-SIRT1 axis was likely operative in the whole animal: both ULK1 and SIRT1 protein levels were significantly reduced in tissue homogenates in eNOS-knockout mice (lung) and in db/db mice where eNOS is downregulated (lung and heart).
25541949	14	50	from	animal	1770:1775	arg1	operative					1747:1755	operative	1747:1755	operative	1747:1755	The NO-ULK1-SIRT1 axis was likely operative in the whole animal: both ULK1 and SIRT1 protein levels were significantly reduced in tissue homogenates in eNOS-knockout mice (lung) and in db/db mice where eNOS is downregulated (lung and heart).
25541949	8	51	theme	autophagy-related	877:893	arg1	unc-51					903:908	an autophagy-related protein unc-51	874:908	an autophagy-related protein unc-51	874:908	NO also stabilized an autophagy-related protein unc-51 like kinase (ULK1), but did not restore SIRT1 protein levels in ULK1-siRNA-treated cells or in mouse embryonic fibroblasts (MEF) from Ulk1-/- mice.
25541949	1	52	theme	several	197:203	arg1	conditions					213:222	several medical conditions	197:222	several medical conditions	197:222	SIRT1 is central to the lifespan and vascular health, but undergoes degradation that contributes to several medical conditions, including diabetes.
25541949	1	52	theme	several	197:203	arg1	diabetes					235:242	diabetes	235:242	diabetes	235:242	SIRT1 is central to the lifespan and vascular health, but undergoes degradation that contributes to several medical conditions, including diabetes.
25541949	13	53	theme	proteasomal	1687:1697	arg1	Rpt2					1707:1710	proteasomal subunit Rpt2	1687:1710	proteasomal subunit Rpt2	1687:1710	Mechanistically, ULK1 negatively regulated 26S proteasome functionality, which was at least partly mediated by O-linked-GlcNAc transferase (OGT), probably by increased O-GlcNAc modification of proteasomal subunit Rpt2.
25541949	4	54	theme	reporter	524:531	arg1	system					533:538	a cellular reporter system	513:538	a cellular reporter system	513:538	We recently identified NO as an endogenous inhibitor of 26S proteasome functionality with a cellular reporter system.
25541949	8	55	theme	Ulk1-/-	1044:1050	arg1	mice					1052:1055	Ulk1-/- mice	1044:1055	Ulk1-/- mice	1044:1055	NO also stabilized an autophagy-related protein unc-51 like kinase (ULK1), but did not restore SIRT1 protein levels in ULK1-siRNA-treated cells or in mouse embryonic fibroblasts (MEF) from Ulk1-/- mice.
25541949	14	56	theme	whole	1764:1768	arg1	animal					1770:1775	the whole animal	1760:1775	the whole animal	1760:1775	The NO-ULK1-SIRT1 axis was likely operative in the whole animal: both ULK1 and SIRT1 protein levels were significantly reduced in tissue homogenates in eNOS-knockout mice (lung) and in db/db mice where eNOS is downregulated (lung and heart).
25541949	14	57	theme	db/db	1898:1902	arg1	mice					1904:1907	db/db mice	1898:1907	db/db mice where eNOS is downregulated (lung and heart)	1898:1952	The NO-ULK1-SIRT1 axis was likely operative in the whole animal: both ULK1 and SIRT1 protein levels were significantly reduced in tissue homogenates in eNOS-knockout mice (lung) and in db/db mice where eNOS is downregulated (lung and heart).
25541949	12	58	theme	proteasome	1388:1397	arg1	MG132					1379:1383	MG132	1379:1383	MG132	1379:1383	Treatment with MG132, a proteasome inhibitor, or siRNA of β-TrCP1, an E3 ligase, prevented SIRT1 reduction induced by ULK1-siRNA.
25541949	12	58	theme	proteasome	1388:1397	arg1	inhibitor					1399:1407	a proteasome inhibitor	1386:1407	a proteasome inhibitor	1386:1407	Treatment with MG132, a proteasome inhibitor, or siRNA of β-TrCP1, an E3 ligase, prevented SIRT1 reduction induced by ULK1-siRNA.
25541949	3	59	theme	SIRT1	397:401	arg1	expression					411:420	SIRT1 protein expression	397:420	SIRT1 protein expression	397:420	However, emerging evidence suggests that endothelial nitric oxide synthase (eNOS) positively regulates SIRT1 protein expression.
25541949	3	60	theme	nitric	347:352	arg1	eNOS					370:373	eNOS	370:373	eNOS	370:373	However, emerging evidence suggests that endothelial nitric oxide synthase (eNOS) positively regulates SIRT1 protein expression.
25541949	3	60	theme	nitric	347:352	arg1	synthase					360:367	endothelial nitric oxide synthase	335:367	endothelial nitric oxide synthase (eNOS)	335:374	However, emerging evidence suggests that endothelial nitric oxide synthase (eNOS) positively regulates SIRT1 protein expression.
25541949	12	61	theme	β-TrCP1	1422:1428	arg1	Treatment					1364:1372	Treatment	1364:1372	Treatment with MG132, a proteasome inhibitor, or siRNA of β-TrCP1, an E3 ligase,	1364:1443	Treatment with MG132, a proteasome inhibitor, or siRNA of β-TrCP1, an E3 ligase, prevented SIRT1 reduction induced by ULK1-siRNA.
25541949	13	62	theme	O-GlcNAc	1662:1669	arg1	modification					1671:1682	increased O-GlcNAc modification	1652:1682	increased O-GlcNAc modification of proteasomal subunit Rpt2	1652:1710	Mechanistically, ULK1 negatively regulated 26S proteasome functionality, which was at least partly mediated by O-linked-GlcNAc transferase (OGT), probably by increased O-GlcNAc modification of proteasomal subunit Rpt2.
25541949	6	63	theme	eNOS	717:720	arg1	A23187					706:711	A23187	706:711	A23187	706:711	In cycloheximide (CHX)-treated endothelial cells, NONOate, an NO donor, and A23187, an eNOS activator, significantly stabilized SIRT1 protein.
25541949	6	63	theme	eNOS	717:720	arg1	activator					722:730	an eNOS activator	714:730	an eNOS activator	714:730	In cycloheximide (CHX)-treated endothelial cells, NONOate, an NO donor, and A23187, an eNOS activator, significantly stabilized SIRT1 protein.
25541949	6	64	theme	-treated	652:659	arg1	cells					673:677	cycloheximide (CHX)-treated endothelial cells	633:677	cycloheximide (CHX)-treated endothelial cells	633:677	In cycloheximide (CHX)-treated endothelial cells, NONOate, an NO donor, and A23187, an eNOS activator, significantly stabilized SIRT1 protein.
25541949	15	65	from	ULK1	2064:2067	arg1	cells					2112:2116	endothelial cells	2100:2116	endothelial cells	2100:2116	Taken together, the results show that NO stabilizes SIRT1 by regulating 26S proteasome functionality through ULK1 and OGT, but not autophagy, in endothelial cells.
25541949	2	66	theme	SIRT1	249:253	arg1	turnover					255:262	SIRT1 turnover	249:262	SIRT1 turnover	249:262	How SIRT1 turnover is regulated remains unclear.
25541949	8	67	theme	protein	895:901	arg1	unc-51					903:908	an autophagy-related protein unc-51	874:908	an autophagy-related protein unc-51	874:908	NO also stabilized an autophagy-related protein unc-51 like kinase (ULK1), but did not restore SIRT1 protein levels in ULK1-siRNA-treated cells or in mouse embryonic fibroblasts (MEF) from Ulk1-/- mice.
25541949	14	68	theme	protein	1798:1804	arg1	levels					1806:1811	SIRT1 protein levels	1792:1811	SIRT1 protein levels	1792:1811	The NO-ULK1-SIRT1 axis was likely operative in the whole animal: both ULK1 and SIRT1 protein levels were significantly reduced in tissue homogenates in eNOS-knockout mice (lung) and in db/db mice where eNOS is downregulated (lung and heart).
25541949	10	69	theme	SIRT1	1176:1180	arg1	expression					1190:1199	SIRT1 protein expression	1176:1199	SIRT1 protein expression	1176:1199	Furthermore, adenoviral overexpression of ULK1 increased SIRT1 protein expression, while ULK1 siRNA treatment decreased it.
25541949	1	70	theme	medical	205:211	arg1	conditions					213:222	several medical conditions	197:222	several medical conditions	197:222	SIRT1 is central to the lifespan and vascular health, but undergoes degradation that contributes to several medical conditions, including diabetes.
25541949	1	70	theme	medical	205:211	arg1	diabetes					235:242	diabetes	235:242	diabetes	235:242	SIRT1 is central to the lifespan and vascular health, but undergoes degradation that contributes to several medical conditions, including diabetes.
25541949	15	71	from	OGT	2073:2075	arg1	cells					2112:2116	endothelial cells	2100:2116	endothelial cells	2100:2116	Taken together, the results show that NO stabilizes SIRT1 by regulating 26S proteasome functionality through ULK1 and OGT, but not autophagy, in endothelial cells.
25541949	13	72	theme	proteasome	1541:1550	arg1	functionality					1552:1564	26S proteasome functionality	1537:1564	26S proteasome functionality	1537:1564	Mechanistically, ULK1 negatively regulated 26S proteasome functionality, which was at least partly mediated by O-linked-GlcNAc transferase (OGT), probably by increased O-GlcNAc modification of proteasomal subunit Rpt2.
25541949	15	73	theme	26S	2027:2029	arg1	functionality					2042:2054	26S proteasome functionality	2027:2054	26S proteasome functionality	2027:2054	Taken together, the results show that NO stabilizes SIRT1 by regulating 26S proteasome functionality through ULK1 and OGT, but not autophagy, in endothelial cells.
25541949	14	74	theme	SIRT1	1792:1796	arg1	levels					1806:1811	SIRT1 protein levels	1792:1811	SIRT1 protein levels	1792:1811	The NO-ULK1-SIRT1 axis was likely operative in the whole animal: both ULK1 and SIRT1 protein levels were significantly reduced in tissue homogenates in eNOS-knockout mice (lung) and in db/db mice where eNOS is downregulated (lung and heart).
25541949	11	75	theme	ULK1	1331:1334	arg1	effects					1320:1326	the effects	1316:1326	the effects of ULK1	1316:1334	Rapamycin-induced autophagy did not mimic these effects, suggesting that the effects of ULK1 were autophagy-independent.
25541949	11	75	theme	ULK1	1331:1334	arg1	autophagy-independent					1341:1361	autophagy-independent	1341:1361	autophagy-independent	1341:1361	Rapamycin-induced autophagy did not mimic these effects, suggesting that the effects of ULK1 were autophagy-independent.
25541949	7	76	theme	CHX-free	839:846	arg1	cells					848:852	CHX-free cells	839:852	CHX-free cells	839:852	Similarly, NO enhanced SIRT1 protein, but not mRNA expression, in CHX-free cells.
25541949	1	77	theme	lifespan	121:128	arg1	health					143:148	the lifespan and vascular health	117:148	the lifespan and vascular health	117:148	SIRT1 is central to the lifespan and vascular health, but undergoes degradation that contributes to several medical conditions, including diabetes.
25541949	10	78	theme	ULK1	1161:1164	arg1	overexpression					1143:1156	adenoviral overexpression	1132:1156	adenoviral overexpression of ULK1	1132:1164	Furthermore, adenoviral overexpression of ULK1 increased SIRT1 protein expression, while ULK1 siRNA treatment decreased it.
25541949	14	79	from	operative	1747:1755	arg1	animal					1770:1775	the whole animal	1760:1775	the whole animal	1760:1775	The NO-ULK1-SIRT1 axis was likely operative in the whole animal: both ULK1 and SIRT1 protein levels were significantly reduced in tissue homogenates in eNOS-knockout mice (lung) and in db/db mice where eNOS is downregulated (lung and heart).
25541949	11	80	theme	Rapamycin-induced	1243:1259	arg1	autophagy					1261:1269	Rapamycin-induced autophagy	1243:1269	Rapamycin-induced autophagy	1243:1269	Rapamycin-induced autophagy did not mimic these effects, suggesting that the effects of ULK1 were autophagy-independent.
25541949	9	81	theme	NO	1095:1096	arg1	regulation					1098:1107	the NO regulation	1091:1107	the NO regulation of SIRT1	1091:1116	This suggests that ULK1 mediated the NO regulation of SIRT1.
25541949	14	82	theme	NO-ULK1-SIRT1	1717:1729	arg1	axis					1731:1734	The NO-ULK1-SIRT1 axis	1713:1734	The NO-ULK1-SIRT1 axis	1713:1734	The NO-ULK1-SIRT1 axis was likely operative in the whole animal: both ULK1 and SIRT1 protein levels were significantly reduced in tissue homogenates in eNOS-knockout mice (lung) and in db/db mice where eNOS is downregulated (lung and heart).
25541949	14	82	theme	NO-ULK1-SIRT1	1717:1729	arg1	operative					1747:1755	operative	1747:1755	operative	1747:1755	The NO-ULK1-SIRT1 axis was likely operative in the whole animal: both ULK1 and SIRT1 protein levels were significantly reduced in tissue homogenates in eNOS-knockout mice (lung) and in db/db mice where eNOS is downregulated (lung and heart).
25541949	6	83	theme	cycloheximide	633:645	arg1	cells					673:677	cycloheximide (CHX)-treated endothelial cells	633:677	cycloheximide (CHX)-treated endothelial cells	633:677	In cycloheximide (CHX)-treated endothelial cells, NONOate, an NO donor, and A23187, an eNOS activator, significantly stabilized SIRT1 protein.
21540332	7	0	used	used	1178:1181	arg2	We					1170:1171	We	1170:1171	We	1170:1171	We also used GlcNAlk, in combination with a biotin affinity tag, to identify 374 proteins, 279 of which were not previously reported, and we subsequently confirmed the enrichment of three previously uncharacterized proteins.
21540332	7	1	theme	374	1247:1249	arg1	proteins					1251:1258	374 proteins	1247:1258	374 proteins	1247:1258	We also used GlcNAlk, in combination with a biotin affinity tag, to identify 374 proteins, 279 of which were not previously reported, and we subsequently confirmed the enrichment of three previously uncharacterized proteins.
21540332	2	2	from	reporter	437:444	arg1	cells					481:485	living cells	474:485	living cells	474:485	Herein we describe the development of an alkynyl-modified GlcNAc analog (GlcNAlk) as a new chemical reporter of O-GlcNAc modification in living cells.
21540332	1	3	theme	nuclear	176:182	arg1	proteins					200:207	nuclear and cytoplasmic proteins	176:207	nuclear and cytoplasmic proteins	176:207	The dynamic modification of nuclear and cytoplasmic proteins by the monosaccharide N-acetyl-glucosamine (GlcNAc) continues to emerge as an important regulator of many biological processes.
21540332	7	4	theme	proteins	1251:1258	arg1	proteins					1251:1258	374 proteins	1247:1258	374 proteins	1247:1258	We also used GlcNAlk, in combination with a biotin affinity tag, to identify 374 proteins, 279 of which were not previously reported, and we subsequently confirmed the enrichment of three previously uncharacterized proteins.
21540332	7	4	theme	proteins	1251:1258	arg1	279					1261:1263	279	1261:1263	279	1261:1263	We also used GlcNAlk, in combination with a biotin affinity tag, to identify 374 proteins, 279 of which were not previously reported, and we subsequently confirmed the enrichment of three previously uncharacterized proteins.
21540332	5	5	theme	reported	946:953	arg1	GlcNAz					969:974	GlcNAz	969:974	GlcNAz	969:974	Using in-gel fluorescence detection, we characterized the metabolic fates of GlcNAlk and the previously reported azido analog, GlcNAz.
21540332	5	5	theme	reported	946:953	arg1	analog					961:966	the previously reported azido analog	931:966	the previously reported azido analog	931:966	Using in-gel fluorescence detection, we characterized the metabolic fates of GlcNAlk and the previously reported azido analog, GlcNAz.
21540332	2	6	theme	alkynyl-modified	378:393	arg1	GlcNAlk					410:416	GlcNAlk	410:416	GlcNAlk	410:416	Herein we describe the development of an alkynyl-modified GlcNAc analog (GlcNAlk) as a new chemical reporter of O-GlcNAc modification in living cells.
21540332	2	6	theme	alkynyl-modified	378:393	arg1	analog					402:407	an alkynyl-modified GlcNAc analog	375:407	an alkynyl-modified GlcNAc analog (GlcNAlk)	375:417	Herein we describe the development of an alkynyl-modified GlcNAc analog (GlcNAlk) as a new chemical reporter of O-GlcNAc modification in living cells.
21540332	8	7	gly	glycosylation	1494:1506	arg1	protein					1516:1522	this protein	1511:1522	this protein	1511:1522	Finally we confirmed the O-GlcNAc modification of the ubiquitin ligase NEDD4-1, the first reported glycosylation of this protein.
21540332	3	8	theme	GlcNAc	573:578	arg1	pathway					593:599	the GlcNAc biosynthetic pathway	569:599	the GlcNAc biosynthetic pathway	569:599	This strategy is based on metabolic incorporation of reactive functionality into the GlcNAc biosynthetic pathway.
21540332	1	9	theme	important	287:295	arg1	regulator					297:305	an important regulator	284:305	an important regulator of many biological processes	284:334	The dynamic modification of nuclear and cytoplasmic proteins by the monosaccharide N-acetyl-glucosamine (GlcNAc) continues to emerge as an important regulator of many biological processes.
21540332	3	10	theme	biosynthetic	580:591	arg1	pathway					593:599	the GlcNAc biosynthetic pathway	569:599	the GlcNAc biosynthetic pathway	569:599	This strategy is based on metabolic incorporation of reactive functionality into the GlcNAc biosynthetic pathway.
21540332	2	11	theme	GlcNAc	395:400	arg1	GlcNAlk					410:416	GlcNAlk	410:416	GlcNAlk	410:416	Herein we describe the development of an alkynyl-modified GlcNAc analog (GlcNAlk) as a new chemical reporter of O-GlcNAc modification in living cells.
21540332	2	11	theme	GlcNAc	395:400	arg1	analog					402:407	an alkynyl-modified GlcNAc analog	375:407	an alkynyl-modified GlcNAc analog (GlcNAlk)	375:417	Herein we describe the development of an alkynyl-modified GlcNAc analog (GlcNAlk) as a new chemical reporter of O-GlcNAc modification in living cells.
21540332	4	12	theme	fluorescent	730:740	arg1	visualization					742:754	the robust in-gel fluorescent visualization	712:754	the robust in-gel fluorescent visualization of O-GlcNAc and affinity enrichment	712:790	When combined with the Cu(I)-catalyzed [3 + 2] azide-alkyne cycloaddition, this chemical reporter allowed for the robust in-gel fluorescent visualization of O-GlcNAc and affinity enrichment and identification of O-GlcNAc-modified proteins.
21540332	0	13	theme	ligase	132:137	arg1	NEDD4-1					139:145	the ubiquitin ligase NEDD4-1	118:145	the ubiquitin ligase NEDD4-1	118:145	Chemical reporters for fluorescent detection and identification of O-GlcNAc-modified proteins reveal glycosylation of the ubiquitin ligase NEDD4-1.
21540332	5	14	theme	in-gel	848:853	arg1	detection					868:876	in-gel fluorescence detection	848:876	in-gel fluorescence detection	848:876	Using in-gel fluorescence detection, we characterized the metabolic fates of GlcNAlk and the previously reported azido analog, GlcNAz.
21540332	5	15	theme	GlcNAlk	919:925	arg1	GlcNAz					969:974	GlcNAz	969:974	GlcNAz	969:974	Using in-gel fluorescence detection, we characterized the metabolic fates of GlcNAlk and the previously reported azido analog, GlcNAz.
21540332	5	15	theme	GlcNAlk	919:925	arg1	analog					961:966	the previously reported azido analog	931:966	the previously reported azido analog	931:966	Using in-gel fluorescence detection, we characterized the metabolic fates of GlcNAlk and the previously reported azido analog, GlcNAz.
21540332	5	15	theme	GlcNAlk	919:925	arg1	fates					910:914	the metabolic fates	896:914	the metabolic fates of GlcNAlk	896:925	Using in-gel fluorescence detection, we characterized the metabolic fates of GlcNAlk and the previously reported azido analog, GlcNAz.
21540332	1	16	theme	cytoplasmic	188:198	arg1	proteins					200:207	nuclear and cytoplasmic proteins	176:207	nuclear and cytoplasmic proteins	176:207	The dynamic modification of nuclear and cytoplasmic proteins by the monosaccharide N-acetyl-glucosamine (GlcNAc) continues to emerge as an important regulator of many biological processes.
21540332	0	17	theme	ubiquitin	122:130	arg1	NEDD4-1					139:145	the ubiquitin ligase NEDD4-1	118:145	the ubiquitin ligase NEDD4-1	118:145	Chemical reporters for fluorescent detection and identification of O-GlcNAc-modified proteins reveal glycosylation of the ubiquitin ligase NEDD4-1.
21540332	0	18	gly	glycosylation	101:113	arg1	NEDD4-1					139:145	the ubiquitin ligase NEDD4-1	118:145	the ubiquitin ligase NEDD4-1	118:145	Chemical reporters for fluorescent detection and identification of O-GlcNAc-modified proteins reveal glycosylation of the ubiquitin ligase NEDD4-1.
21540332	1	19	theme	proteins	200:207	arg1	modification					160:171	The dynamic modification	148:171	The dynamic modification of nuclear and cytoplasmic proteins by the monosaccharide N-acetyl-glucosamine (GlcNAc)	148:259	The dynamic modification of nuclear and cytoplasmic proteins by the monosaccharide N-acetyl-glucosamine (GlcNAc) continues to emerge as an important regulator of many biological processes.
21540332	2	20	theme	living	474:479	arg1	cells					481:485	living cells	474:485	living cells	474:485	Herein we describe the development of an alkynyl-modified GlcNAc analog (GlcNAlk) as a new chemical reporter of O-GlcNAc modification in living cells.
21540332	3	21	theme	functionality	550:562	arg1	incorporation					524:536	metabolic incorporation	514:536	metabolic incorporation of reactive functionality into the GlcNAc biosynthetic pathway	514:599	This strategy is based on metabolic incorporation of reactive functionality into the GlcNAc biosynthetic pathway.
21540332	4	22	theme	O-GlcNAc	759:766	arg1	identification					796:809	identification	796:809	identification of O-GlcNAc-modified proteins	796:839	When combined with the Cu(I)-catalyzed [3 + 2] azide-alkyne cycloaddition, this chemical reporter allowed for the robust in-gel fluorescent visualization of O-GlcNAc and affinity enrichment and identification of O-GlcNAc-modified proteins.
21540332	4	22	theme	O-GlcNAc	759:766	arg1	visualization					742:754	the robust in-gel fluorescent visualization	712:754	the robust in-gel fluorescent visualization of O-GlcNAc and affinity enrichment	712:790	When combined with the Cu(I)-catalyzed [3 + 2] azide-alkyne cycloaddition, this chemical reporter allowed for the robust in-gel fluorescent visualization of O-GlcNAc and affinity enrichment and identification of O-GlcNAc-modified proteins.
21540332	7	23	theme	biotin	1214:1219	arg1	tag					1230:1232	a biotin affinity tag	1212:1232	a biotin affinity tag	1212:1232	We also used GlcNAlk, in combination with a biotin affinity tag, to identify 374 proteins, 279 of which were not previously reported, and we subsequently confirmed the enrichment of three previously uncharacterized proteins.
21540332	4	24	theme	chemical	682:689	arg1	reporter					691:698	this chemical reporter	677:698	this chemical reporter	677:698	When combined with the Cu(I)-catalyzed [3 + 2] azide-alkyne cycloaddition, this chemical reporter allowed for the robust in-gel fluorescent visualization of O-GlcNAc and affinity enrichment and identification of O-GlcNAc-modified proteins.
21540332	0	25	theme	Chemical	0:7	arg1	reporters					9:17	Chemical reporters	0:17	Chemical reporters for fluorescent detection and identification of O-GlcNAc-modified proteins	0:92	Chemical reporters for fluorescent detection and identification of O-GlcNAc-modified proteins reveal glycosylation of the ubiquitin ligase NEDD4-1.
21540332	5	26	theme	fluorescence	855:866	arg1	detection					868:876	in-gel fluorescence detection	848:876	in-gel fluorescence detection	848:876	Using in-gel fluorescence detection, we characterized the metabolic fates of GlcNAlk and the previously reported azido analog, GlcNAz.
21540332	8	27	theme	ligase	1459:1464	arg1	modification					1429:1440	the O-GlcNAc modification	1416:1440	the O-GlcNAc modification of the ubiquitin ligase NEDD4-1, the first reported glycosylation of this protein	1416:1522	Finally we confirmed the O-GlcNAc modification of the ubiquitin ligase NEDD4-1, the first reported glycosylation of this protein.
21540332	8	28	dep	ligase	1459:1464	arg1	NEDD4-1					1466:1472	NEDD4-1	1466:1472	NEDD4-1	1466:1472	Finally we confirmed the O-GlcNAc modification of the ubiquitin ligase NEDD4-1, the first reported glycosylation of this protein.
21540332	0	29	theme	fluorescent	23:33	arg1	detection					35:43	detection	35:43	detection	35:43	Chemical reporters for fluorescent detection and identification of O-GlcNAc-modified proteins reveal glycosylation of the ubiquitin ligase NEDD4-1.
21540332	1	30	theme	many	310:313	arg1	processes					326:334	many biological processes	310:334	many biological processes	310:334	The dynamic modification of nuclear and cytoplasmic proteins by the monosaccharide N-acetyl-glucosamine (GlcNAc) continues to emerge as an important regulator of many biological processes.
21540332	7	31	theme	proteins	1385:1392	arg1	enrichment					1338:1347	the enrichment	1334:1347	the enrichment of three previously uncharacterized proteins	1334:1392	We also used GlcNAlk, in combination with a biotin affinity tag, to identify 374 proteins, 279 of which were not previously reported, and we subsequently confirmed the enrichment of three previously uncharacterized proteins.
21540332	4	32	theme	affinity	772:779	arg1	enrichment					781:790	affinity enrichment	772:790	affinity enrichment	772:790	When combined with the Cu(I)-catalyzed [3 + 2] azide-alkyne cycloaddition, this chemical reporter allowed for the robust in-gel fluorescent visualization of O-GlcNAc and affinity enrichment and identification of O-GlcNAc-modified proteins.
21540332	1	33	theme	monosaccharide	216:229	arg1	N-acetyl-glucosamine					231:250	the monosaccharide N-acetyl-glucosamine	212:250	the monosaccharide N-acetyl-glucosamine (GlcNAc)	212:259	The dynamic modification of nuclear and cytoplasmic proteins by the monosaccharide N-acetyl-glucosamine (GlcNAc) continues to emerge as an important regulator of many biological processes.
21540332	1	33	theme	monosaccharide	216:229	arg1	GlcNAc					253:258	GlcNAc	253:258	GlcNAc	253:258	The dynamic modification of nuclear and cytoplasmic proteins by the monosaccharide N-acetyl-glucosamine (GlcNAc) continues to emerge as an important regulator of many biological processes.
21540332	2	34	theme	O-GlcNAc	449:456	arg1	modification					458:469	O-GlcNAc modification	449:469	O-GlcNAc modification	449:469	Herein we describe the development of an alkynyl-modified GlcNAc analog (GlcNAlk) as a new chemical reporter of O-GlcNAc modification in living cells.
21540332	1	35	theme	biological	315:324	arg1	processes					326:334	many biological processes	310:334	many biological processes	310:334	The dynamic modification of nuclear and cytoplasmic proteins by the monosaccharide N-acetyl-glucosamine (GlcNAc) continues to emerge as an important regulator of many biological processes.
21540332	0	36	theme	NEDD4-1	139:145	arg1	glycosylation					101:113	glycosylation	101:113	glycosylation of the ubiquitin ligase NEDD4-1	101:145	Chemical reporters for fluorescent detection and identification of O-GlcNAc-modified proteins reveal glycosylation of the ubiquitin ligase NEDD4-1.
21540332	8	37	theme	reported	1485:1492	arg1	glycosylation					1494:1506	the first reported glycosylation	1475:1506	the first reported glycosylation of this protein	1475:1522	Finally we confirmed the O-GlcNAc modification of the ubiquitin ligase NEDD4-1, the first reported glycosylation of this protein.
21540332	8	37	theme	reported	1485:1492	arg1	ligase					1459:1464	the ubiquitin ligase NEDD4-1, the first reported glycosylation of this protein	1445:1522	ligase	1459:1464	Finally we confirmed the O-GlcNAc modification of the ubiquitin ligase NEDD4-1, the first reported glycosylation of this protein.
21540332	5	38	theme	azido	955:959	arg1	GlcNAz					969:974	GlcNAz	969:974	GlcNAz	969:974	Using in-gel fluorescence detection, we characterized the metabolic fates of GlcNAlk and the previously reported azido analog, GlcNAz.
21540332	5	38	theme	azido	955:959	arg1	analog					961:966	the previously reported azido analog	931:966	the previously reported azido analog	931:966	Using in-gel fluorescence detection, we characterized the metabolic fates of GlcNAlk and the previously reported azido analog, GlcNAz.
21540332	6	39	theme	modification	1156:1167	arg1	reporter					1135:1142	a more specific metabolic reporter	1109:1142	a more specific metabolic reporter of O-GlcNAc modification	1109:1167	We confirmed previous results that GlcNAz can be metabolically interconverted to GalNAz, whereas GlcNAlk does not, thereby yielding a more specific metabolic reporter of O-GlcNAc modification.
21540332	1	40	theme	processes	326:334	arg1	regulator					297:305	an important regulator	284:305	an important regulator of many biological processes	284:334	The dynamic modification of nuclear and cytoplasmic proteins by the monosaccharide N-acetyl-glucosamine (GlcNAc) continues to emerge as an important regulator of many biological processes.
21540332	4	41	theme	azide-alkyne	649:660	arg1	cycloaddition					662:674	2] azide-alkyne cycloaddition	646:674	2] azide-alkyne cycloaddition	646:674	When combined with the Cu(I)-catalyzed [3 + 2] azide-alkyne cycloaddition, this chemical reporter allowed for the robust in-gel fluorescent visualization of O-GlcNAc and affinity enrichment and identification of O-GlcNAc-modified proteins.
21540332	2	42	theme	chemical	428:435	arg1	reporter					437:444	a new chemical reporter	422:444	a new chemical reporter of O-GlcNAc modification in living cells	422:485	Herein we describe the development of an alkynyl-modified GlcNAc analog (GlcNAlk) as a new chemical reporter of O-GlcNAc modification in living cells.
21540332	6	43	theme	metabolic	1125:1133	arg1	reporter					1135:1142	a more specific metabolic reporter	1109:1142	a more specific metabolic reporter of O-GlcNAc modification	1109:1167	We confirmed previous results that GlcNAz can be metabolically interconverted to GalNAz, whereas GlcNAlk does not, thereby yielding a more specific metabolic reporter of O-GlcNAc modification.
21540332	4	44	theme	enrichment	781:790	arg1	identification					796:809	identification	796:809	identification of O-GlcNAc-modified proteins	796:839	When combined with the Cu(I)-catalyzed [3 + 2] azide-alkyne cycloaddition, this chemical reporter allowed for the robust in-gel fluorescent visualization of O-GlcNAc and affinity enrichment and identification of O-GlcNAc-modified proteins.
21540332	4	44	theme	enrichment	781:790	arg1	visualization					742:754	the robust in-gel fluorescent visualization	712:754	the robust in-gel fluorescent visualization of O-GlcNAc and affinity enrichment	712:790	When combined with the Cu(I)-catalyzed [3 + 2] azide-alkyne cycloaddition, this chemical reporter allowed for the robust in-gel fluorescent visualization of O-GlcNAc and affinity enrichment and identification of O-GlcNAc-modified proteins.
21540332	2	45	theme	modification	458:469	arg1	reporter					437:444	a new chemical reporter	422:444	a new chemical reporter of O-GlcNAc modification in living cells	422:485	Herein we describe the development of an alkynyl-modified GlcNAc analog (GlcNAlk) as a new chemical reporter of O-GlcNAc modification in living cells.
21540332	2	46	theme	new	424:426	arg1	reporter					437:444	a new chemical reporter	422:444	a new chemical reporter of O-GlcNAc modification in living cells	422:485	Herein we describe the development of an alkynyl-modified GlcNAc analog (GlcNAlk) as a new chemical reporter of O-GlcNAc modification in living cells.
21540332	6	47	theme	previous	990:997	arg1	results					999:1005	previous results	990:1005	previous results	990:1005	We confirmed previous results that GlcNAz can be metabolically interconverted to GalNAz, whereas GlcNAlk does not, thereby yielding a more specific metabolic reporter of O-GlcNAc modification.
21540332	8	48	theme	ubiquitin	1449:1457	arg1	glycosylation					1494:1506	the first reported glycosylation	1475:1506	the first reported glycosylation of this protein	1475:1522	Finally we confirmed the O-GlcNAc modification of the ubiquitin ligase NEDD4-1, the first reported glycosylation of this protein.
21540332	8	48	theme	ubiquitin	1449:1457	arg1	ligase					1459:1464	the ubiquitin ligase NEDD4-1, the first reported glycosylation of this protein	1445:1522	ligase	1459:1464	Finally we confirmed the O-GlcNAc modification of the ubiquitin ligase NEDD4-1, the first reported glycosylation of this protein.
21540332	6	49	theme	O-GlcNAc	1147:1154	arg1	modification					1156:1167	O-GlcNAc modification	1147:1167	O-GlcNAc modification	1147:1167	We confirmed previous results that GlcNAz can be metabolically interconverted to GalNAz, whereas GlcNAlk does not, thereby yielding a more specific metabolic reporter of O-GlcNAc modification.
21540332	4	50	theme	in-gel	723:728	arg1	visualization					742:754	the robust in-gel fluorescent visualization	712:754	the robust in-gel fluorescent visualization of O-GlcNAc and affinity enrichment	712:790	When combined with the Cu(I)-catalyzed [3 + 2] azide-alkyne cycloaddition, this chemical reporter allowed for the robust in-gel fluorescent visualization of O-GlcNAc and affinity enrichment and identification of O-GlcNAc-modified proteins.
21540332	8	51	theme	protein	1516:1522	arg1	glycosylation					1494:1506	the first reported glycosylation	1475:1506	the first reported glycosylation of this protein	1475:1522	Finally we confirmed the O-GlcNAc modification of the ubiquitin ligase NEDD4-1, the first reported glycosylation of this protein.
21540332	8	51	theme	protein	1516:1522	arg1	ligase					1459:1464	the ubiquitin ligase NEDD4-1, the first reported glycosylation of this protein	1445:1522	ligase	1459:1464	Finally we confirmed the O-GlcNAc modification of the ubiquitin ligase NEDD4-1, the first reported glycosylation of this protein.
21540332	3	52	theme	metabolic	514:522	arg1	incorporation					524:536	metabolic incorporation	514:536	metabolic incorporation of reactive functionality into the GlcNAc biosynthetic pathway	514:599	This strategy is based on metabolic incorporation of reactive functionality into the GlcNAc biosynthetic pathway.
21540332	4	53	dep	cycloaddition	662:674	arg1	2					646:646	2	646:646	2	646:646	When combined with the Cu(I)-catalyzed [3 + 2] azide-alkyne cycloaddition, this chemical reporter allowed for the robust in-gel fluorescent visualization of O-GlcNAc and affinity enrichment and identification of O-GlcNAc-modified proteins.
21540332	4	54	theme	proteins	832:839	arg1	identification					796:809	identification	796:809	identification of O-GlcNAc-modified proteins	796:839	When combined with the Cu(I)-catalyzed [3 + 2] azide-alkyne cycloaddition, this chemical reporter allowed for the robust in-gel fluorescent visualization of O-GlcNAc and affinity enrichment and identification of O-GlcNAc-modified proteins.
21540332	4	54	theme	proteins	832:839	arg1	visualization					742:754	the robust in-gel fluorescent visualization	712:754	the robust in-gel fluorescent visualization of O-GlcNAc and affinity enrichment	712:790	When combined with the Cu(I)-catalyzed [3 + 2] azide-alkyne cycloaddition, this chemical reporter allowed for the robust in-gel fluorescent visualization of O-GlcNAc and affinity enrichment and identification of O-GlcNAc-modified proteins.
21540332	8	55	theme	O-GlcNAc	1420:1427	arg1	modification					1429:1440	the O-GlcNAc modification	1416:1440	the O-GlcNAc modification of the ubiquitin ligase NEDD4-1, the first reported glycosylation of this protein	1416:1522	Finally we confirmed the O-GlcNAc modification of the ubiquitin ligase NEDD4-1, the first reported glycosylation of this protein.
21540332	7	56	with	combination	1195:1205	arg1	tag					1230:1232	a biotin affinity tag	1212:1232	a biotin affinity tag	1212:1232	We also used GlcNAlk, in combination with a biotin affinity tag, to identify 374 proteins, 279 of which were not previously reported, and we subsequently confirmed the enrichment of three previously uncharacterized proteins.
21540332	4	57	theme	O-GlcNAc-modified	814:830	arg1	proteins					832:839	O-GlcNAc-modified proteins	814:839	O-GlcNAc-modified proteins	814:839	When combined with the Cu(I)-catalyzed [3 + 2] azide-alkyne cycloaddition, this chemical reporter allowed for the robust in-gel fluorescent visualization of O-GlcNAc and affinity enrichment and identification of O-GlcNAc-modified proteins.
21540332	1	58	theme	dynamic	152:158	arg1	modification					160:171	The dynamic modification	148:171	The dynamic modification of nuclear and cytoplasmic proteins by the monosaccharide N-acetyl-glucosamine (GlcNAc)	148:259	The dynamic modification of nuclear and cytoplasmic proteins by the monosaccharide N-acetyl-glucosamine (GlcNAc) continues to emerge as an important regulator of many biological processes.
21540332	0	59	theme	proteins	85:92	arg1	identification					49:62	identification	49:62	identification	49:62	Chemical reporters for fluorescent detection and identification of O-GlcNAc-modified proteins reveal glycosylation of the ubiquitin ligase NEDD4-1.
21540332	0	59	theme	proteins	85:92	arg1	detection					35:43	detection	35:43	detection	35:43	Chemical reporters for fluorescent detection and identification of O-GlcNAc-modified proteins reveal glycosylation of the ubiquitin ligase NEDD4-1.
21540332	5	60	theme	metabolic	900:908	arg1	fates					910:914	the metabolic fates	896:914	the metabolic fates of GlcNAlk	896:925	Using in-gel fluorescence detection, we characterized the metabolic fates of GlcNAlk and the previously reported azido analog, GlcNAz.
21540332	7	61	theme	uncharacterized	1369:1383	arg1	proteins					1385:1392	three previously uncharacterized proteins	1352:1392	three previously uncharacterized proteins	1352:1392	We also used GlcNAlk, in combination with a biotin affinity tag, to identify 374 proteins, 279 of which were not previously reported, and we subsequently confirmed the enrichment of three previously uncharacterized proteins.
21540332	3	62	theme	reactive	541:548	arg1	functionality					550:562	reactive functionality	541:562	reactive functionality	541:562	This strategy is based on metabolic incorporation of reactive functionality into the GlcNAc biosynthetic pathway.
21540332	6	63	theme	specific	1116:1123	arg1	reporter					1135:1142	a more specific metabolic reporter	1109:1142	a more specific metabolic reporter of O-GlcNAc modification	1109:1167	We confirmed previous results that GlcNAz can be metabolically interconverted to GalNAz, whereas GlcNAlk does not, thereby yielding a more specific metabolic reporter of O-GlcNAc modification.
21540332	0	64	theme	O-GlcNAc-modified	67:83	arg1	proteins					85:92	O-GlcNAc-modified proteins	67:92	O-GlcNAc-modified proteins	67:92	Chemical reporters for fluorescent detection and identification of O-GlcNAc-modified proteins reveal glycosylation of the ubiquitin ligase NEDD4-1.
21540332	4	65	theme	-catalyzed	630:639	arg1	[3					641:642	the Cu(I)-catalyzed [3	621:642	the Cu(I)-catalyzed [3	621:642	When combined with the Cu(I)-catalyzed [3 + 2] azide-alkyne cycloaddition, this chemical reporter allowed for the robust in-gel fluorescent visualization of O-GlcNAc and affinity enrichment and identification of O-GlcNAc-modified proteins.
21540332	2	66	theme	analog	402:407	arg1	development					360:370	the development	356:370	the development of an alkynyl-modified GlcNAc analog (GlcNAlk) as a new chemical reporter of O-GlcNAc modification in living cells	356:485	Herein we describe the development of an alkynyl-modified GlcNAc analog (GlcNAlk) as a new chemical reporter of O-GlcNAc modification in living cells.
21540332	7	67	theme	affinity	1221:1228	arg1	tag					1230:1232	a biotin affinity tag	1212:1232	a biotin affinity tag	1212:1232	We also used GlcNAlk, in combination with a biotin affinity tag, to identify 374 proteins, 279 of which were not previously reported, and we subsequently confirmed the enrichment of three previously uncharacterized proteins.
21540332	4	68	theme	robust	716:721	arg1	visualization					742:754	the robust in-gel fluorescent visualization	712:754	the robust in-gel fluorescent visualization of O-GlcNAc and affinity enrichment	712:790	When combined with the Cu(I)-catalyzed [3 + 2] azide-alkyne cycloaddition, this chemical reporter allowed for the robust in-gel fluorescent visualization of O-GlcNAc and affinity enrichment and identification of O-GlcNAc-modified proteins.
22759405	8	0	theme	ATM	1355:1357	arg1	processes					1368:1376	ATM recovery processes	1355:1376	ATM recovery processes	1355:1376	However, decreases in protein O-GlcNAcylation did not affect levels of ATM activation, but these decreases did delay ATM activation and ATM recovery processes based on assessment of de-phosphorylation of phospho-ATM.
22759405	8	1	from	decreases	1228:1236	arg1	O-GlcNAcylation					1249:1263	protein O-GlcNAcylation	1241:1263	protein O-GlcNAcylation	1241:1263	However, decreases in protein O-GlcNAcylation did not affect levels of ATM activation, but these decreases did delay ATM activation and ATM recovery processes based on assessment of de-phosphorylation of phospho-ATM.
22759405	1	2	theme	regulatory	162:171	arg1	responsive					246:255	responsive	246:255	responsive	246:255	BACKGROUND O-Linked β-N-acetylglucosamine (O-GlcNAc) is a reversible, post-translational, and regulatory modification of nuclear, mitochondrial, and cytoplasmic proteins that is responsive to cellular stress.
22759405	1	2	theme	regulatory	162:171	arg1	β-N-acetylglucosamine					88:108	BACKGROUND O-Linked β-N-acetylglucosamine	68:108	BACKGROUND O-Linked β-N-acetylglucosamine (O-GlcNAc)	68:119	BACKGROUND O-Linked β-N-acetylglucosamine (O-GlcNAc) is a reversible, post-translational, and regulatory modification of nuclear, mitochondrial, and cytoplasmic proteins that is responsive to cellular stress.
22759405	1	2	theme	regulatory	162:171	arg1	modification					173:184	a reversible, post-translational, and regulatory modification	124:184	a reversible, post-translational, and regulatory modification of nuclear, mitochondrial, and cytoplasmic proteins that is responsive to cellular stress	124:274	BACKGROUND O-Linked β-N-acetylglucosamine (O-GlcNAc) is a reversible, post-translational, and regulatory modification of nuclear, mitochondrial, and cytoplasmic proteins that is responsive to cellular stress.
22759405	1	3	theme	cellular	260:267	arg1	stress					269:274	cellular stress	260:274	cellular stress	260:274	BACKGROUND O-Linked β-N-acetylglucosamine (O-GlcNAc) is a reversible, post-translational, and regulatory modification of nuclear, mitochondrial, and cytoplasmic proteins that is responsive to cellular stress.
22759405	7	4	theme	protein	1137:1143	arg1	O-GlcNAcylation					1145:1159	protein O-GlcNAcylation	1137:1159	protein O-GlcNAcylation	1137:1159	RESULTS Enhancement of protein O-GlcNAcylation increased levels of X-irradiation-induced ATM activation.
22759405	11	5	theme	steady-state	1578:1589	arg1	responsive					1635:1644	responsive	1635:1644	responsive	1635:1644	The steady-state O-GlcNAc level of ATM was not significantly responsive to X-irradiation or oxidative stress.
22759405	11	5	theme	steady-state	1578:1589	arg1	level					1600:1604	The steady-state O-GlcNAc level	1574:1604	The steady-state O-GlcNAc level of ATM	1574:1611	The steady-state O-GlcNAc level of ATM was not significantly responsive to X-irradiation or oxidative stress.
22759405	2	6	theme	damage	361:366	arg1	response					368:375	the ataxia-telangiectasia mutated (ATM)-mediated DNA damage response	308:375	the ataxia-telangiectasia mutated (ATM)-mediated DNA damage response	308:375	The role of O-GlcNAcylation in the ataxia-telangiectasia mutated (ATM)-mediated DNA damage response is unknown.
22759405	12	7	theme	dynamic	1746:1752	arg1	modification					1763:1774	dynamic O-GlcNAc modification	1746:1774	dynamic O-GlcNAc modification	1746:1774	GENERAL SIGNIFICANCE ATM is an O-GlcNAc modified protein, and dynamic O-GlcNAc modification affects the ATM-mediated DNA damage response.
22759405	6	8	theme	target	1021:1026	arg1	proteins					1028:1035	target proteins	1021:1035	target proteins	1021:1035	Interaction of ATM with O-GlcNAc transferase (OGT), the enzyme that adds O-GlcNAc to target proteins, was examined by immunoprecipitation and immunoblot analyses using anti-ATM.
22759405	7	9	theme	RESULTS	1114:1120	arg1	Enhancement					1122:1132	RESULTS Enhancement	1114:1132	RESULTS Enhancement of protein O-GlcNAcylation	1114:1159	RESULTS Enhancement of protein O-GlcNAcylation increased levels of X-irradiation-induced ATM activation.
22759405	11	10	theme	O-GlcNAc	1591:1598	arg1	responsive					1635:1644	responsive	1635:1644	responsive	1635:1644	The steady-state O-GlcNAc level of ATM was not significantly responsive to X-irradiation or oxidative stress.
22759405	11	10	theme	O-GlcNAc	1591:1598	arg1	level					1600:1604	The steady-state O-GlcNAc level	1574:1604	The steady-state O-GlcNAc level of ATM	1574:1611	The steady-state O-GlcNAc level of ATM was not significantly responsive to X-irradiation or oxidative stress.
22759405	3	11	theme	O-GlcNAc-modified	542:558	arg1	ATM					411:413	ATM	411:413	ATM	411:413	It is unclear whether ATM, which is an early acting and central component of the signal transduction system activated by DNA double strand breaks, is an O-GlcNAc-modified protein.
22759405	3	11	theme	O-GlcNAc-modified	542:558	arg1	protein					560:566	an O-GlcNAc-modified protein	539:566	an O-GlcNAc-modified protein	539:566	It is unclear whether ATM, which is an early acting and central component of the signal transduction system activated by DNA double strand breaks, is an O-GlcNAc-modified protein.
22759405	4	12	from	effect	581:586	arg1	activation					620:629	ATM activation	616:629	ATM activation	616:629	METHODS The effect of O-GlcNAc modification on ATM activation was examined using two inhibitors, PUGNAc and DON that increase and decrease, respectively, levels of protein O-GlcNAcylation.
22759405	2	13	theme	O-GlcNAcylation	289:303	arg1	role					281:284	The role	277:284	The role of O-GlcNAcylation in the ataxia-telangiectasia mutated (ATM)-mediated DNA damage response	277:375	The role of O-GlcNAcylation in the ataxia-telangiectasia mutated (ATM)-mediated DNA damage response is unknown.
22759405	2	13	theme	O-GlcNAcylation	289:303	arg1	unknown					380:386	unknown	380:386	unknown	380:386	The role of O-GlcNAcylation in the ataxia-telangiectasia mutated (ATM)-mediated DNA damage response is unknown.
22759405	1	14	theme	BACKGROUND	68:77	arg1	responsive					246:255	responsive	246:255	responsive	246:255	BACKGROUND O-Linked β-N-acetylglucosamine (O-GlcNAc) is a reversible, post-translational, and regulatory modification of nuclear, mitochondrial, and cytoplasmic proteins that is responsive to cellular stress.
22759405	1	14	theme	BACKGROUND	68:77	arg1	O-GlcNAc					111:118	O-GlcNAc	111:118	O-GlcNAc	111:118	BACKGROUND O-Linked β-N-acetylglucosamine (O-GlcNAc) is a reversible, post-translational, and regulatory modification of nuclear, mitochondrial, and cytoplasmic proteins that is responsive to cellular stress.
22759405	1	14	theme	BACKGROUND	68:77	arg1	β-N-acetylglucosamine					88:108	BACKGROUND O-Linked β-N-acetylglucosamine	68:108	BACKGROUND O-Linked β-N-acetylglucosamine (O-GlcNAc)	68:119	BACKGROUND O-Linked β-N-acetylglucosamine (O-GlcNAc) is a reversible, post-translational, and regulatory modification of nuclear, mitochondrial, and cytoplasmic proteins that is responsive to cellular stress.
22759405	1	14	theme	BACKGROUND	68:77	arg1	modification					173:184	a reversible, post-translational, and regulatory modification	124:184	a reversible, post-translational, and regulatory modification of nuclear, mitochondrial, and cytoplasmic proteins that is responsive to cellular stress	124:274	BACKGROUND O-Linked β-N-acetylglucosamine (O-GlcNAc) is a reversible, post-translational, and regulatory modification of nuclear, mitochondrial, and cytoplasmic proteins that is responsive to cellular stress.
22759405	1	15	theme	post-translational	138:155	arg1	responsive					246:255	responsive	246:255	responsive	246:255	BACKGROUND O-Linked β-N-acetylglucosamine (O-GlcNAc) is a reversible, post-translational, and regulatory modification of nuclear, mitochondrial, and cytoplasmic proteins that is responsive to cellular stress.
22759405	1	15	theme	post-translational	138:155	arg1	β-N-acetylglucosamine					88:108	BACKGROUND O-Linked β-N-acetylglucosamine	68:108	BACKGROUND O-Linked β-N-acetylglucosamine (O-GlcNAc)	68:119	BACKGROUND O-Linked β-N-acetylglucosamine (O-GlcNAc) is a reversible, post-translational, and regulatory modification of nuclear, mitochondrial, and cytoplasmic proteins that is responsive to cellular stress.
22759405	1	15	theme	post-translational	138:155	arg1	modification					173:184	a reversible, post-translational, and regulatory modification	124:184	a reversible, post-translational, and regulatory modification of nuclear, mitochondrial, and cytoplasmic proteins that is responsive to cellular stress	124:274	BACKGROUND O-Linked β-N-acetylglucosamine (O-GlcNAc) is a reversible, post-translational, and regulatory modification of nuclear, mitochondrial, and cytoplasmic proteins that is responsive to cellular stress.
22759405	3	16	theme	transduction	477:488	arg1	system					490:495	the signal transduction system	466:495	the signal transduction system activated by DNA double strand breaks	466:533	It is unclear whether ATM, which is an early acting and central component of the signal transduction system activated by DNA double strand breaks, is an O-GlcNAc-modified protein.
22759405	5	17	theme	anti-ATM	842:849	arg1	antibody					868:875	anti-ATM or anti-O-GlcNAc antibody	842:875	anti-ATM or anti-O-GlcNAc antibody	842:875	To assess O-GlcNAcylation of ATM, immunoprecipitation and immunoblot analyses using anti-ATM or anti-O-GlcNAc antibody were performed in HeLa cells and primary cultured neurons.
22759405	1	18	theme	O-Linked	79:86	arg1	responsive					246:255	responsive	246:255	responsive	246:255	BACKGROUND O-Linked β-N-acetylglucosamine (O-GlcNAc) is a reversible, post-translational, and regulatory modification of nuclear, mitochondrial, and cytoplasmic proteins that is responsive to cellular stress.
22759405	1	18	theme	O-Linked	79:86	arg1	O-GlcNAc					111:118	O-GlcNAc	111:118	O-GlcNAc	111:118	BACKGROUND O-Linked β-N-acetylglucosamine (O-GlcNAc) is a reversible, post-translational, and regulatory modification of nuclear, mitochondrial, and cytoplasmic proteins that is responsive to cellular stress.
22759405	1	18	theme	O-Linked	79:86	arg1	β-N-acetylglucosamine					88:108	BACKGROUND O-Linked β-N-acetylglucosamine	68:108	BACKGROUND O-Linked β-N-acetylglucosamine (O-GlcNAc)	68:119	BACKGROUND O-Linked β-N-acetylglucosamine (O-GlcNAc) is a reversible, post-translational, and regulatory modification of nuclear, mitochondrial, and cytoplasmic proteins that is responsive to cellular stress.
22759405	1	18	theme	O-Linked	79:86	arg1	modification					173:184	a reversible, post-translational, and regulatory modification	124:184	a reversible, post-translational, and regulatory modification of nuclear, mitochondrial, and cytoplasmic proteins that is responsive to cellular stress	124:274	BACKGROUND O-Linked β-N-acetylglucosamine (O-GlcNAc) is a reversible, post-translational, and regulatory modification of nuclear, mitochondrial, and cytoplasmic proteins that is responsive to cellular stress.
22759405	8	19	theme	phospho-ATM	1423:1433	arg1	de-phosphorylation					1401:1418	de-phosphorylation	1401:1418	de-phosphorylation of phospho-ATM	1401:1433	However, decreases in protein O-GlcNAcylation did not affect levels of ATM activation, but these decreases did delay ATM activation and ATM recovery processes based on assessment of de-phosphorylation of phospho-ATM.
22759405	6	20	theme	immunoblot	1078:1087	arg1	analyses					1089:1096	immunoblot analyses	1078:1096	immunoblot analyses using anti-ATM	1078:1111	Interaction of ATM with O-GlcNAc transferase (OGT), the enzyme that adds O-GlcNAc to target proteins, was examined by immunoprecipitation and immunoblot analyses using anti-ATM.
22759405	9	21	theme	ATM	1469:1471	arg1	recovery					1457:1464	recovery	1457:1464	recovery	1457:1464	Thus, activation and recovery of ATM were affected by O-GlcNAcylation.
22759405	9	21	theme	ATM	1469:1471	arg1	activation					1442:1451	activation	1442:1451	activation	1442:1451	Thus, activation and recovery of ATM were affected by O-GlcNAcylation.
22759405	5	22	theme	primary	910:916	arg1	neurons					927:933	primary cultured neurons	910:933	primary cultured neurons	910:933	To assess O-GlcNAcylation of ATM, immunoprecipitation and immunoblot analyses using anti-ATM or anti-O-GlcNAc antibody were performed in HeLa cells and primary cultured neurons.
22759405	11	23	theme	ATM	1609:1611	arg1	responsive					1635:1644	responsive	1635:1644	responsive	1635:1644	The steady-state O-GlcNAc level of ATM was not significantly responsive to X-irradiation or oxidative stress.
22759405	11	23	theme	ATM	1609:1611	arg1	level					1600:1604	The steady-state O-GlcNAc level	1574:1604	The steady-state O-GlcNAc level of ATM	1574:1611	The steady-state O-GlcNAc level of ATM was not significantly responsive to X-irradiation or oxidative stress.
22759405	4	24	theme	O-GlcNAc	591:598	arg1	modification					600:611	O-GlcNAc modification	591:611	O-GlcNAc modification	591:611	METHODS The effect of O-GlcNAc modification on ATM activation was examined using two inhibitors, PUGNAc and DON that increase and decrease, respectively, levels of protein O-GlcNAcylation.
22759405	12	25	theme	modified	1724:1731	arg1	protein					1733:1739	an O-GlcNAc modified protein	1712:1739	an O-GlcNAc modified protein	1712:1739	GENERAL SIGNIFICANCE ATM is an O-GlcNAc modified protein, and dynamic O-GlcNAc modification affects the ATM-mediated DNA damage response.
22759405	12	25	theme	modified	1724:1731	arg1	ATM					1705:1707	GENERAL SIGNIFICANCE ATM	1684:1707	GENERAL SIGNIFICANCE ATM	1684:1707	GENERAL SIGNIFICANCE ATM is an O-GlcNAc modified protein, and dynamic O-GlcNAc modification affects the ATM-mediated DNA damage response.
22759405	1	26	theme	nuclear	189:195	arg1	proteins					229:236	nuclear, mitochondrial, and cytoplasmic proteins	189:236	nuclear, mitochondrial, and cytoplasmic proteins	189:236	BACKGROUND O-Linked β-N-acetylglucosamine (O-GlcNAc) is a reversible, post-translational, and regulatory modification of nuclear, mitochondrial, and cytoplasmic proteins that is responsive to cellular stress.
22759405	5	27	theme	immunoprecipitation	792:810	arg1	analyses					827:834	immunoprecipitation and immunoblot analyses	792:834	immunoprecipitation and immunoblot analyses using anti-ATM or anti-O-GlcNAc antibody	792:875	To assess O-GlcNAcylation of ATM, immunoprecipitation and immunoblot analyses using anti-ATM or anti-O-GlcNAc antibody were performed in HeLa cells and primary cultured neurons.
22759405	12	28	theme	ATM-mediated	1788:1799	arg1	damage					1805:1810	the ATM-mediated DNA damage	1784:1810	the ATM-mediated DNA damage response	1784:1819	GENERAL SIGNIFICANCE ATM is an O-GlcNAc modified protein, and dynamic O-GlcNAc modification affects the ATM-mediated DNA damage response.
22759405	8	29	theme	de-phosphorylation	1401:1418	arg1	assessment					1387:1396	assessment	1387:1396	assessment of de-phosphorylation of phospho-ATM	1387:1433	However, decreases in protein O-GlcNAcylation did not affect levels of ATM activation, but these decreases did delay ATM activation and ATM recovery processes based on assessment of de-phosphorylation of phospho-ATM.
22759405	7	30	theme	activation	1207:1216	arg1	levels					1171:1176	levels	1171:1176	levels of X-irradiation-induced ATM activation	1171:1216	RESULTS Enhancement of protein O-GlcNAcylation increased levels of X-irradiation-induced ATM activation.
22759405	8	31	theme	ATM	1290:1292	arg1	activation					1294:1303	ATM activation	1290:1303	ATM activation	1290:1303	However, decreases in protein O-GlcNAcylation did not affect levels of ATM activation, but these decreases did delay ATM activation and ATM recovery processes based on assessment of de-phosphorylation of phospho-ATM.
22759405	0	32	theme	O-GlcNAc	0:7	arg1	modification					9:20	O-GlcNAc modification	0:20	O-GlcNAc modification	0:20	O-GlcNAc modification affects the ATM-mediated DNA damage response.
22759405	2	33	theme	mutated	334:340	arg1	response					368:375	the ataxia-telangiectasia mutated (ATM)-mediated DNA damage response	308:375	the ataxia-telangiectasia mutated (ATM)-mediated DNA damage response	308:375	The role of O-GlcNAcylation in the ataxia-telangiectasia mutated (ATM)-mediated DNA damage response is unknown.
22759405	8	34	theme	activation	1294:1303	arg1	levels					1280:1285	levels	1280:1285	levels of ATM activation	1280:1303	However, decreases in protein O-GlcNAcylation did not affect levels of ATM activation, but these decreases did delay ATM activation and ATM recovery processes based on assessment of de-phosphorylation of phospho-ATM.
22759405	1	35	theme	mitochondrial	198:210	arg1	proteins					229:236	nuclear, mitochondrial, and cytoplasmic proteins	189:236	nuclear, mitochondrial, and cytoplasmic proteins	189:236	BACKGROUND O-Linked β-N-acetylglucosamine (O-GlcNAc) is a reversible, post-translational, and regulatory modification of nuclear, mitochondrial, and cytoplasmic proteins that is responsive to cellular stress.
22759405	5	36	theme	immunoblot	816:825	arg1	analyses					827:834	immunoprecipitation and immunoblot analyses	792:834	immunoprecipitation and immunoblot analyses using anti-ATM or anti-O-GlcNAc antibody	792:875	To assess O-GlcNAcylation of ATM, immunoprecipitation and immunoblot analyses using anti-ATM or anti-O-GlcNAc antibody were performed in HeLa cells and primary cultured neurons.
22759405	8	37	theme	ATM	1336:1338	arg1	activation					1340:1349	delay ATM activation	1330:1349	delay ATM activation	1330:1349	However, decreases in protein O-GlcNAcylation did not affect levels of ATM activation, but these decreases did delay ATM activation and ATM recovery processes based on assessment of de-phosphorylation of phospho-ATM.
22759405	8	38	theme	delay	1330:1334	arg1	activation					1340:1349	delay ATM activation	1330:1349	delay ATM activation	1330:1349	However, decreases in protein O-GlcNAcylation did not affect levels of ATM activation, but these decreases did delay ATM activation and ATM recovery processes based on assessment of de-phosphorylation of phospho-ATM.
22759405	12	39	theme	damage	1805:1810	arg1	response					1812:1819	the ATM-mediated DNA damage response	1784:1819	the ATM-mediated DNA damage response	1784:1819	GENERAL SIGNIFICANCE ATM is an O-GlcNAc modified protein, and dynamic O-GlcNAc modification affects the ATM-mediated DNA damage response.
22759405	4	40	theme	protein	733:739	arg1	O-GlcNAcylation					741:755	protein O-GlcNAcylation	733:755	protein O-GlcNAcylation	733:755	METHODS The effect of O-GlcNAc modification on ATM activation was examined using two inhibitors, PUGNAc and DON that increase and decrease, respectively, levels of protein O-GlcNAcylation.
22759405	7	41	theme	ATM	1203:1205	arg1	activation					1207:1216	X-irradiation-induced ATM activation	1181:1216	X-irradiation-induced ATM activation	1181:1216	RESULTS Enhancement of protein O-GlcNAcylation increased levels of X-irradiation-induced ATM activation.
22759405	3	42	theme	strand	521:526	arg1	breaks					528:533	DNA double strand breaks	510:533	DNA double strand breaks	510:533	It is unclear whether ATM, which is an early acting and central component of the signal transduction system activated by DNA double strand breaks, is an O-GlcNAc-modified protein.
22759405	3	43	theme	system	490:495	arg1	ATM					411:413	ATM	411:413	ATM	411:413	It is unclear whether ATM, which is an early acting and central component of the signal transduction system activated by DNA double strand breaks, is an O-GlcNAc-modified protein.
22759405	3	43	theme	system	490:495	arg1	component					453:461	an early acting and central component	425:461	an early acting and central component of the signal transduction system activated by DNA double strand breaks	425:533	It is unclear whether ATM, which is an early acting and central component of the signal transduction system activated by DNA double strand breaks, is an O-GlcNAc-modified protein.
22759405	5	44	theme	HeLa	895:898	arg1	cells					900:904	HeLa cells	895:904	HeLa cells	895:904	To assess O-GlcNAcylation of ATM, immunoprecipitation and immunoblot analyses using anti-ATM or anti-O-GlcNAc antibody were performed in HeLa cells and primary cultured neurons.
22759405	0	45	theme	DNA	47:49	arg1	damage					51:56	the ATM-mediated DNA damage	30:56	the ATM-mediated DNA damage response	30:65	O-GlcNAc modification affects the ATM-mediated DNA damage response.
22759405	2	46	theme	-mediated	347:355	arg1	response					368:375	the ataxia-telangiectasia mutated (ATM)-mediated DNA damage response	308:375	the ataxia-telangiectasia mutated (ATM)-mediated DNA damage response	308:375	The role of O-GlcNAcylation in the ataxia-telangiectasia mutated (ATM)-mediated DNA damage response is unknown.
22759405	12	47	theme	SIGNIFICANCE	1692:1703	arg1	protein					1733:1739	an O-GlcNAc modified protein	1712:1739	an O-GlcNAc modified protein	1712:1739	GENERAL SIGNIFICANCE ATM is an O-GlcNAc modified protein, and dynamic O-GlcNAc modification affects the ATM-mediated DNA damage response.
22759405	12	47	theme	SIGNIFICANCE	1692:1703	arg1	ATM					1705:1707	GENERAL SIGNIFICANCE ATM	1684:1707	GENERAL SIGNIFICANCE ATM	1684:1707	GENERAL SIGNIFICANCE ATM is an O-GlcNAc modified protein, and dynamic O-GlcNAc modification affects the ATM-mediated DNA damage response.
22759405	1	48	theme	cytoplasmic	217:227	arg1	proteins					229:236	nuclear, mitochondrial, and cytoplasmic proteins	189:236	nuclear, mitochondrial, and cytoplasmic proteins	189:236	BACKGROUND O-Linked β-N-acetylglucosamine (O-GlcNAc) is a reversible, post-translational, and regulatory modification of nuclear, mitochondrial, and cytoplasmic proteins that is responsive to cellular stress.
22759405	0	49	theme	ATM-mediated	34:45	arg1	damage					51:56	the ATM-mediated DNA damage	30:56	the ATM-mediated DNA damage response	30:65	O-GlcNAc modification affects the ATM-mediated DNA damage response.
22759405	6	50	theme	O-GlcNAc	960:967	arg1	enzyme					992:997	the enzyme	988:997	the enzyme that adds O-GlcNAc to target proteins	988:1035	Interaction of ATM with O-GlcNAc transferase (OGT), the enzyme that adds O-GlcNAc to target proteins, was examined by immunoprecipitation and immunoblot analyses using anti-ATM.
22759405	6	50	theme	O-GlcNAc	960:967	arg1	OGT					982:984	OGT	982:984	OGT	982:984	Interaction of ATM with O-GlcNAc transferase (OGT), the enzyme that adds O-GlcNAc to target proteins, was examined by immunoprecipitation and immunoblot analyses using anti-ATM.
22759405	6	50	theme	O-GlcNAc	960:967	arg1	transferase					969:979	O-GlcNAc transferase	960:979	O-GlcNAc transferase (OGT)	960:985	Interaction of ATM with O-GlcNAc transferase (OGT), the enzyme that adds O-GlcNAc to target proteins, was examined by immunoprecipitation and immunoblot analyses using anti-ATM.
22759405	8	51	theme	protein	1241:1247	arg1	O-GlcNAcylation					1249:1263	protein O-GlcNAcylation	1241:1263	protein O-GlcNAcylation	1241:1263	However, decreases in protein O-GlcNAcylation did not affect levels of ATM activation, but these decreases did delay ATM activation and ATM recovery processes based on assessment of de-phosphorylation of phospho-ATM.
22759405	4	52	theme	O-GlcNAcylation	741:755	arg1	levels					723:728	levels	723:728	levels of protein O-GlcNAcylation	723:755	METHODS The effect of O-GlcNAc modification on ATM activation was examined using two inhibitors, PUGNAc and DON that increase and decrease, respectively, levels of protein O-GlcNAcylation.
22759405	7	53	theme	X-irradiation-induced	1181:1201	arg1	activation					1207:1216	X-irradiation-induced ATM activation	1181:1216	X-irradiation-induced ATM activation	1181:1216	RESULTS Enhancement of protein O-GlcNAcylation increased levels of X-irradiation-induced ATM activation.
22759405	5	54	theme	anti-O-GlcNAc	854:866	arg1	antibody					868:875	anti-ATM or anti-O-GlcNAc antibody	842:875	anti-ATM or anti-O-GlcNAc antibody	842:875	To assess O-GlcNAcylation of ATM, immunoprecipitation and immunoblot analyses using anti-ATM or anti-O-GlcNAc antibody were performed in HeLa cells and primary cultured neurons.
22759405	1	55	theme	proteins	229:236	arg1	responsive					246:255	responsive	246:255	responsive	246:255	BACKGROUND O-Linked β-N-acetylglucosamine (O-GlcNAc) is a reversible, post-translational, and regulatory modification of nuclear, mitochondrial, and cytoplasmic proteins that is responsive to cellular stress.
22759405	1	55	theme	proteins	229:236	arg1	β-N-acetylglucosamine					88:108	BACKGROUND O-Linked β-N-acetylglucosamine	68:108	BACKGROUND O-Linked β-N-acetylglucosamine (O-GlcNAc)	68:119	BACKGROUND O-Linked β-N-acetylglucosamine (O-GlcNAc) is a reversible, post-translational, and regulatory modification of nuclear, mitochondrial, and cytoplasmic proteins that is responsive to cellular stress.
22759405	1	55	theme	proteins	229:236	arg1	modification					173:184	a reversible, post-translational, and regulatory modification	124:184	a reversible, post-translational, and regulatory modification of nuclear, mitochondrial, and cytoplasmic proteins that is responsive to cellular stress	124:274	BACKGROUND O-Linked β-N-acetylglucosamine (O-GlcNAc) is a reversible, post-translational, and regulatory modification of nuclear, mitochondrial, and cytoplasmic proteins that is responsive to cellular stress.
22759405	5	56	theme	ATM	787:789	arg1	O-GlcNAcylation					768:782	O-GlcNAcylation	768:782	O-GlcNAcylation of ATM	768:789	To assess O-GlcNAcylation of ATM, immunoprecipitation and immunoblot analyses using anti-ATM or anti-O-GlcNAc antibody were performed in HeLa cells and primary cultured neurons.
22759405	12	57	theme	GENERAL	1684:1690	arg1	protein					1733:1739	an O-GlcNAc modified protein	1712:1739	an O-GlcNAc modified protein	1712:1739	GENERAL SIGNIFICANCE ATM is an O-GlcNAc modified protein, and dynamic O-GlcNAc modification affects the ATM-mediated DNA damage response.
22759405	12	57	theme	GENERAL	1684:1690	arg1	ATM					1705:1707	GENERAL SIGNIFICANCE ATM	1684:1707	GENERAL SIGNIFICANCE ATM	1684:1707	GENERAL SIGNIFICANCE ATM is an O-GlcNAc modified protein, and dynamic O-GlcNAc modification affects the ATM-mediated DNA damage response.
22759405	4	58	dep	METHODS	569:575	arg1	examined					635:642	examined	635:642	was examined using two inhibitors, PUGNAc and DON that increase and decrease, respectively, levels of protein O-GlcNAcylation	631:755	METHODS The effect of O-GlcNAc modification on ATM activation was examined using two inhibitors, PUGNAc and DON that increase and decrease, respectively, levels of protein O-GlcNAcylation.
22759405	2	59	theme	DNA	357:359	arg1	response					368:375	the ataxia-telangiectasia mutated (ATM)-mediated DNA damage response	308:375	the ataxia-telangiectasia mutated (ATM)-mediated DNA damage response	308:375	The role of O-GlcNAcylation in the ataxia-telangiectasia mutated (ATM)-mediated DNA damage response is unknown.
22759405	0	60	theme	damage	51:56	arg1	response					58:65	the ATM-mediated DNA damage response	30:65	the ATM-mediated DNA damage response	30:65	O-GlcNAc modification affects the ATM-mediated DNA damage response.
22759405	6	61	theme	ATM	951:953	arg1	Interaction					936:946	Interaction	936:946	Interaction of ATM with O-GlcNAc transferase (OGT), the enzyme that adds O-GlcNAc to target proteins,	936:1036	Interaction of ATM with O-GlcNAc transferase (OGT), the enzyme that adds O-GlcNAc to target proteins, was examined by immunoprecipitation and immunoblot analyses using anti-ATM.
22759405	1	62	theme	reversible	126:135	arg1	responsive					246:255	responsive	246:255	responsive	246:255	BACKGROUND O-Linked β-N-acetylglucosamine (O-GlcNAc) is a reversible, post-translational, and regulatory modification of nuclear, mitochondrial, and cytoplasmic proteins that is responsive to cellular stress.
22759405	1	62	theme	reversible	126:135	arg1	β-N-acetylglucosamine					88:108	BACKGROUND O-Linked β-N-acetylglucosamine	68:108	BACKGROUND O-Linked β-N-acetylglucosamine (O-GlcNAc)	68:119	BACKGROUND O-Linked β-N-acetylglucosamine (O-GlcNAc) is a reversible, post-translational, and regulatory modification of nuclear, mitochondrial, and cytoplasmic proteins that is responsive to cellular stress.
22759405	1	62	theme	reversible	126:135	arg1	modification					173:184	a reversible, post-translational, and regulatory modification	124:184	a reversible, post-translational, and regulatory modification of nuclear, mitochondrial, and cytoplasmic proteins that is responsive to cellular stress	124:274	BACKGROUND O-Linked β-N-acetylglucosamine (O-GlcNAc) is a reversible, post-translational, and regulatory modification of nuclear, mitochondrial, and cytoplasmic proteins that is responsive to cellular stress.
22759405	12	63	theme	DNA	1801:1803	arg1	damage					1805:1810	the ATM-mediated DNA damage	1784:1810	the ATM-mediated DNA damage response	1784:1819	GENERAL SIGNIFICANCE ATM is an O-GlcNAc modified protein, and dynamic O-GlcNAc modification affects the ATM-mediated DNA damage response.
22759405	6	64	with	Interaction	936:946	arg1	enzyme					992:997	the enzyme	988:997	the enzyme that adds O-GlcNAc to target proteins	988:1035	Interaction of ATM with O-GlcNAc transferase (OGT), the enzyme that adds O-GlcNAc to target proteins, was examined by immunoprecipitation and immunoblot analyses using anti-ATM.
22759405	6	64	with	Interaction	936:946	arg1	OGT					982:984	OGT	982:984	OGT	982:984	Interaction of ATM with O-GlcNAc transferase (OGT), the enzyme that adds O-GlcNAc to target proteins, was examined by immunoprecipitation and immunoblot analyses using anti-ATM.
22759405	6	64	with	Interaction	936:946	arg1	transferase					969:979	O-GlcNAc transferase	960:979	O-GlcNAc transferase (OGT)	960:985	Interaction of ATM with O-GlcNAc transferase (OGT), the enzyme that adds O-GlcNAc to target proteins, was examined by immunoprecipitation and immunoblot analyses using anti-ATM.
22759405	2	65	from	role	281:284	arg1	response					368:375	the ataxia-telangiectasia mutated (ATM)-mediated DNA damage response	308:375	the ataxia-telangiectasia mutated (ATM)-mediated DNA damage response	308:375	The role of O-GlcNAcylation in the ataxia-telangiectasia mutated (ATM)-mediated DNA damage response is unknown.
22759405	4	66	theme	modification	600:611	arg1	effect					581:586	The effect	577:586	The effect of O-GlcNAc modification on ATM activation	577:629	METHODS The effect of O-GlcNAc modification on ATM activation was examined using two inhibitors, PUGNAc and DON that increase and decrease, respectively, levels of protein O-GlcNAcylation.
22759405	5	67	theme	cultured	918:925	arg1	neurons					927:933	primary cultured neurons	910:933	primary cultured neurons	910:933	To assess O-GlcNAcylation of ATM, immunoprecipitation and immunoblot analyses using anti-ATM or anti-O-GlcNAc antibody were performed in HeLa cells and primary cultured neurons.
22759405	11	68	theme	oxidative	1666:1674	arg1	stress					1676:1681	oxidative stress	1666:1681	oxidative stress	1666:1681	The steady-state O-GlcNAc level of ATM was not significantly responsive to X-irradiation or oxidative stress.
22759405	2	69	dep	mutated	334:340	arg1	ataxia-telangiectasia					312:332	ataxia-telangiectasia	312:332	ataxia-telangiectasia	312:332	The role of O-GlcNAcylation in the ataxia-telangiectasia mutated (ATM)-mediated DNA damage response is unknown.
22759405	2	69	dep	mutated	334:340	arg1	ATM					343:345	ATM	343:345	ATM	343:345	The role of O-GlcNAcylation in the ataxia-telangiectasia mutated (ATM)-mediated DNA damage response is unknown.
22759405	8	70	theme	recovery	1359:1366	arg1	processes					1368:1376	ATM recovery processes	1355:1376	ATM recovery processes	1355:1376	However, decreases in protein O-GlcNAcylation did not affect levels of ATM activation, but these decreases did delay ATM activation and ATM recovery processes based on assessment of de-phosphorylation of phospho-ATM.
22759405	3	71	theme	acting	434:439	arg1	ATM					411:413	ATM	411:413	ATM	411:413	It is unclear whether ATM, which is an early acting and central component of the signal transduction system activated by DNA double strand breaks, is an O-GlcNAc-modified protein.
22759405	3	71	theme	acting	434:439	arg1	component					453:461	an early acting and central component	425:461	an early acting and central component of the signal transduction system activated by DNA double strand breaks	425:533	It is unclear whether ATM, which is an early acting and central component of the signal transduction system activated by DNA double strand breaks, is an O-GlcNAc-modified protein.
22759405	3	72	theme	central	445:451	arg1	ATM					411:413	ATM	411:413	ATM	411:413	It is unclear whether ATM, which is an early acting and central component of the signal transduction system activated by DNA double strand breaks, is an O-GlcNAc-modified protein.
22759405	3	72	theme	central	445:451	arg1	component					453:461	an early acting and central component	425:461	an early acting and central component of the signal transduction system activated by DNA double strand breaks	425:533	It is unclear whether ATM, which is an early acting and central component of the signal transduction system activated by DNA double strand breaks, is an O-GlcNAc-modified protein.
22759405	3	73	theme	DNA	510:512	arg1	breaks					528:533	DNA double strand breaks	510:533	DNA double strand breaks	510:533	It is unclear whether ATM, which is an early acting and central component of the signal transduction system activated by DNA double strand breaks, is an O-GlcNAc-modified protein.
22759405	3	74	theme	signal	470:475	arg1	system					490:495	the signal transduction system	466:495	the signal transduction system activated by DNA double strand breaks	466:533	It is unclear whether ATM, which is an early acting and central component of the signal transduction system activated by DNA double strand breaks, is an O-GlcNAc-modified protein.
22759405	4	75	theme	ATM	616:618	arg1	activation					620:629	ATM activation	616:629	ATM activation	616:629	METHODS The effect of O-GlcNAc modification on ATM activation was examined using two inhibitors, PUGNAc and DON that increase and decrease, respectively, levels of protein O-GlcNAcylation.
22759405	7	76	theme	O-GlcNAcylation	1145:1159	arg1	Enhancement					1122:1132	RESULTS Enhancement	1114:1132	RESULTS Enhancement of protein O-GlcNAcylation	1114:1159	RESULTS Enhancement of protein O-GlcNAcylation increased levels of X-irradiation-induced ATM activation.
22759405	3	77	theme	double	514:519	arg1	breaks					528:533	DNA double strand breaks	510:533	DNA double strand breaks	510:533	It is unclear whether ATM, which is an early acting and central component of the signal transduction system activated by DNA double strand breaks, is an O-GlcNAc-modified protein.
22759405	12	78	theme	O-GlcNAc	1754:1761	arg1	modification					1763:1774	dynamic O-GlcNAc modification	1746:1774	dynamic O-GlcNAc modification	1746:1774	GENERAL SIGNIFICANCE ATM is an O-GlcNAc modified protein, and dynamic O-GlcNAc modification affects the ATM-mediated DNA damage response.
12150998	0	0	theme	protein	81:87	arg1	O-GlcNAcylation					89:103	coupling protein O-GlcNAcylation	72:103	Recruitment of O-GlcNAc transferase to promoters by corepressor mSin3A: coupling protein O-GlcNAcylation to transcriptional repression.	0:134	Recruitment of O-GlcNAc transferase to promoters by corepressor mSin3A: coupling protein O-GlcNAcylation to transcriptional repression.
12150998	2	1	theme	histone	490:496	arg1	complex					510:516	a histone deacetylase complex	488:516	a histone deacetylase complex	488:516	Here, we show that O-GlcNAc transferase (OGT), the enzyme that catalyzes this posttranslational modification, interacts with a histone deacetylase complex by binding to the corepressor mSin3A.
12150998	4	2	theme	transcription	723:735	arg1	factors					737:743	transcription factors	723:743	transcription factors	723:743	We propose that mSin3A targets OGT to promoters to inactivate transcription factors and RNA polymerase II by O-GlcNAc modification, which acts in concert with histone deacetylation to promote gene silencing in an efficient and specific manner.
12150998	0	3	theme	coupling	72:79	arg1	O-GlcNAcylation					89:103	coupling protein O-GlcNAcylation	72:103	Recruitment of O-GlcNAc transferase to promoters by corepressor mSin3A: coupling protein O-GlcNAcylation to transcriptional repression.	0:134	Recruitment of O-GlcNAc transferase to promoters by corepressor mSin3A: coupling protein O-GlcNAcylation to transcriptional repression.
12150998	4	4	theme	specific	888:895	arg1	manner					897:902	an efficient and specific manner	871:902	an efficient and specific manner	871:902	We propose that mSin3A targets OGT to promoters to inactivate transcription factors and RNA polymerase II by O-GlcNAc modification, which acts in concert with histone deacetylation to promote gene silencing in an efficient and specific manner.
12150998	4	5	with	concert	807:813	arg1	deacetylation					828:840	histone deacetylation	820:840	histone deacetylation	820:840	We propose that mSin3A targets OGT to promoters to inactivate transcription factors and RNA polymerase II by O-GlcNAc modification, which acts in concert with histone deacetylation to promote gene silencing in an efficient and specific manner.
12150998	0	6	theme	transcriptional	108:122	arg1	repression					124:133	transcriptional repression	108:133	transcriptional repression	108:133	Recruitment of O-GlcNAc transferase to promoters by corepressor mSin3A: coupling protein O-GlcNAcylation to transcriptional repression.
12150998	1	7	link	O-linked	199:206	arg1	O-GlcNAc					229:236	O-GlcNAc	229:236	O-GlcNAc	229:236	Transcription factors and RNA polymerase II can be modified by O-linked N-acetylglucosamine (O-GlcNAc) monosaccharides at serine or threonine residues, yet the precise functional roles of this modification are largely unknown.
12150998	1	7	link	O-linked	199:206	arg1	N-acetylglucosamine					208:226	O-linked N-acetylglucosamine	199:226	O-linked N-acetylglucosamine (O-GlcNAc) monosaccharides at serine or threonine residues	199:285	Transcription factors and RNA polymerase II can be modified by O-linked N-acetylglucosamine (O-GlcNAc) monosaccharides at serine or threonine residues, yet the precise functional roles of this modification are largely unknown.
12150998	2	8	theme	posttranslational	441:457	arg1	modification					459:470	this posttranslational modification	436:470	this posttranslational modification	436:470	Here, we show that O-GlcNAc transferase (OGT), the enzyme that catalyzes this posttranslational modification, interacts with a histone deacetylase complex by binding to the corepressor mSin3A.
12150998	4	9	theme	efficient	874:882	arg1	manner					897:902	an efficient and specific manner	871:902	an efficient and specific manner	871:902	We propose that mSin3A targets OGT to promoters to inactivate transcription factors and RNA polymerase II by O-GlcNAc modification, which acts in concert with histone deacetylation to promote gene silencing in an efficient and specific manner.
12150998	1	10	theme	O-linked	199:206	arg1	O-GlcNAc					229:236	O-GlcNAc	229:236	O-GlcNAc	229:236	Transcription factors and RNA polymerase II can be modified by O-linked N-acetylglucosamine (O-GlcNAc) monosaccharides at serine or threonine residues, yet the precise functional roles of this modification are largely unknown.
12150998	1	10	theme	O-linked	199:206	arg1	N-acetylglucosamine					208:226	O-linked N-acetylglucosamine	199:226	O-linked N-acetylglucosamine (O-GlcNAc) monosaccharides at serine or threonine residues	199:285	Transcription factors and RNA polymerase II can be modified by O-linked N-acetylglucosamine (O-GlcNAc) monosaccharides at serine or threonine residues, yet the precise functional roles of this modification are largely unknown.
12150998	0	11	theme	transferase	24:34	arg1	Recruitment					0:10	Recruitment	0:10	Recruitment of O-GlcNAc transferase to promoters by corepressor mSin3A: coupling protein O-GlcNAcylation to transcriptional repression.	0:134	Recruitment of O-GlcNAc transferase to promoters by corepressor mSin3A: coupling protein O-GlcNAcylation to transcriptional repression.
12150998	1	12	theme	precise	296:302	arg1	roles					315:319	the precise functional roles	292:319	the precise functional roles of this modification	292:340	Transcription factors and RNA polymerase II can be modified by O-linked N-acetylglucosamine (O-GlcNAc) monosaccharides at serine or threonine residues, yet the precise functional roles of this modification are largely unknown.
12150998	1	12	theme	precise	296:302	arg1	unknown					354:360	unknown	354:360	unknown	354:360	Transcription factors and RNA polymerase II can be modified by O-linked N-acetylglucosamine (O-GlcNAc) monosaccharides at serine or threonine residues, yet the precise functional roles of this modification are largely unknown.
12150998	1	13	theme	N-acetylglucosamine	208:226	arg1	monosaccharides					239:253	O-linked N-acetylglucosamine (O-GlcNAc) monosaccharides	199:253	O-linked N-acetylglucosamine (O-GlcNAc) monosaccharides at serine or threonine residues	199:285	Transcription factors and RNA polymerase II can be modified by O-linked N-acetylglucosamine (O-GlcNAc) monosaccharides at serine or threonine residues, yet the precise functional roles of this modification are largely unknown.
12150998	0	14	theme	O-GlcNAc	15:22	arg1	transferase					24:34	O-GlcNAc transferase	15:34	O-GlcNAc transferase to promoters	15:47	Recruitment of O-GlcNAc transferase to promoters by corepressor mSin3A: coupling protein O-GlcNAcylation to transcriptional repression.
12150998	1	15	theme	functional	304:313	arg1	roles					315:319	the precise functional roles	292:319	the precise functional roles of this modification	292:340	Transcription factors and RNA polymerase II can be modified by O-linked N-acetylglucosamine (O-GlcNAc) monosaccharides at serine or threonine residues, yet the precise functional roles of this modification are largely unknown.
12150998	1	15	theme	functional	304:313	arg1	unknown					354:360	unknown	354:360	unknown	354:360	Transcription factors and RNA polymerase II can be modified by O-linked N-acetylglucosamine (O-GlcNAc) monosaccharides at serine or threonine residues, yet the precise functional roles of this modification are largely unknown.
12150998	1	16	dep	serine	258:263	arg1	residues					278:285	residues	278:285	residues	278:285	Transcription factors and RNA polymerase II can be modified by O-linked N-acetylglucosamine (O-GlcNAc) monosaccharides at serine or threonine residues, yet the precise functional roles of this modification are largely unknown.
12150998	4	17	theme	O-GlcNAc	770:777	arg1	modification					779:790	O-GlcNAc modification	770:790	O-GlcNAc modification	770:790	We propose that mSin3A targets OGT to promoters to inactivate transcription factors and RNA polymerase II by O-GlcNAc modification, which acts in concert with histone deacetylation to promote gene silencing in an efficient and specific manner.
12150998	1	18	from	threonine	268:276	arg1	monosaccharides					239:253	O-linked N-acetylglucosamine (O-GlcNAc) monosaccharides	199:253	O-linked N-acetylglucosamine (O-GlcNAc) monosaccharides at serine or threonine residues	199:285	Transcription factors and RNA polymerase II can be modified by O-linked N-acetylglucosamine (O-GlcNAc) monosaccharides at serine or threonine residues, yet the precise functional roles of this modification are largely unknown.
12150998	2	19	theme	O-GlcNAc	382:389	arg1	OGT					404:406	OGT	404:406	OGT	404:406	Here, we show that O-GlcNAc transferase (OGT), the enzyme that catalyzes this posttranslational modification, interacts with a histone deacetylase complex by binding to the corepressor mSin3A.
12150998	2	19	theme	O-GlcNAc	382:389	arg1	transferase					391:401	O-GlcNAc transferase	382:401	O-GlcNAc transferase (OGT)	382:407	Here, we show that O-GlcNAc transferase (OGT), the enzyme that catalyzes this posttranslational modification, interacts with a histone deacetylase complex by binding to the corepressor mSin3A.
12150998	2	19	theme	O-GlcNAc	382:389	arg1	enzyme					414:419	the enzyme	410:419	the enzyme that catalyzes this posttranslational modification	410:470	Here, we show that O-GlcNAc transferase (OGT), the enzyme that catalyzes this posttranslational modification, interacts with a histone deacetylase complex by binding to the corepressor mSin3A.
12150998	2	20	theme	corepressor	536:546	arg1	mSin3A					548:553	the corepressor mSin3A	532:553	the corepressor mSin3A	532:553	Here, we show that O-GlcNAc transferase (OGT), the enzyme that catalyzes this posttranslational modification, interacts with a histone deacetylase complex by binding to the corepressor mSin3A.
12150998	0	21	theme	corepressor	52:62	arg1	mSin3A					64:69	corepressor mSin3A	52:69	corepressor mSin3A	52:69	Recruitment of O-GlcNAc transferase to promoters by corepressor mSin3A: coupling protein O-GlcNAcylation to transcriptional repression.
12150998	1	22	from	serine	258:263	arg1	monosaccharides					239:253	O-linked N-acetylglucosamine (O-GlcNAc) monosaccharides	199:253	O-linked N-acetylglucosamine (O-GlcNAc) monosaccharides at serine or threonine residues	199:285	Transcription factors and RNA polymerase II can be modified by O-linked N-acetylglucosamine (O-GlcNAc) monosaccharides at serine or threonine residues, yet the precise functional roles of this modification are largely unknown.
12150998	1	23	theme	modification	329:340	arg1	roles					315:319	the precise functional roles	292:319	the precise functional roles of this modification	292:340	Transcription factors and RNA polymerase II can be modified by O-linked N-acetylglucosamine (O-GlcNAc) monosaccharides at serine or threonine residues, yet the precise functional roles of this modification are largely unknown.
12150998	1	23	theme	modification	329:340	arg1	unknown					354:360	unknown	354:360	unknown	354:360	Transcription factors and RNA polymerase II can be modified by O-linked N-acetylglucosamine (O-GlcNAc) monosaccharides at serine or threonine residues, yet the precise functional roles of this modification are largely unknown.
12150998	4	24	theme	gene	853:856	arg1	silencing					858:866	gene silencing	853:866	gene silencing	853:866	We propose that mSin3A targets OGT to promoters to inactivate transcription factors and RNA polymerase II by O-GlcNAc modification, which acts in concert with histone deacetylation to promote gene silencing in an efficient and specific manner.
12150998	1	25	theme	Transcription	136:148	arg1	factors					150:156	Transcription factors	136:156	Transcription factors	136:156	Transcription factors and RNA polymerase II can be modified by O-linked N-acetylglucosamine (O-GlcNAc) monosaccharides at serine or threonine residues, yet the precise functional roles of this modification are largely unknown.
12150998	4	26	theme	histone	820:826	arg1	deacetylation					828:840	histone deacetylation	820:840	histone deacetylation	820:840	We propose that mSin3A targets OGT to promoters to inactivate transcription factors and RNA polymerase II by O-GlcNAc modification, which acts in concert with histone deacetylation to promote gene silencing in an efficient and specific manner.
12150998	3	27	theme	histone	638:644	arg1	deacetylation					646:658	histone deacetylation	638:658	histone deacetylation	638:658	Functionally, OGT and mSin3A cooperatively repress transcription in parallel with histone deacetylation.
12150998	1	28	mod	modified	187:194	arg1	factors					150:156	Transcription factors	136:156	Transcription factors	136:156	Transcription factors and RNA polymerase II can be modified by O-linked N-acetylglucosamine (O-GlcNAc) monosaccharides at serine or threonine residues, yet the precise functional roles of this modification are largely unknown.
12150998	1	28	mod	modified	187:194	arg3	monosaccharides					239:253	O-linked N-acetylglucosamine (O-GlcNAc) monosaccharides	199:253	O-linked N-acetylglucosamine (O-GlcNAc) monosaccharides at serine or threonine residues	199:285	Transcription factors and RNA polymerase II can be modified by O-linked N-acetylglucosamine (O-GlcNAc) monosaccharides at serine or threonine residues, yet the precise functional roles of this modification are largely unknown.
12150998	1	28	mod	modified	187:194	arg1	polymerase					166:175	RNA polymerase II	162:178	RNA polymerase II	162:178	Transcription factors and RNA polymerase II can be modified by O-linked N-acetylglucosamine (O-GlcNAc) monosaccharides at serine or threonine residues, yet the precise functional roles of this modification are largely unknown.
12150998	4	29	theme	RNA	749:751	arg1	polymerase					753:762	RNA polymerase II	749:765	RNA polymerase II	749:765	We propose that mSin3A targets OGT to promoters to inactivate transcription factors and RNA polymerase II by O-GlcNAc modification, which acts in concert with histone deacetylation to promote gene silencing in an efficient and specific manner.
12150998	3	30	with	parallel	624:631	arg1	deacetylation					646:658	histone deacetylation	638:658	histone deacetylation	638:658	Functionally, OGT and mSin3A cooperatively repress transcription in parallel with histone deacetylation.
12150998	1	31	theme	RNA	162:164	arg1	polymerase					166:175	RNA polymerase II	162:178	RNA polymerase II	162:178	Transcription factors and RNA polymerase II can be modified by O-linked N-acetylglucosamine (O-GlcNAc) monosaccharides at serine or threonine residues, yet the precise functional roles of this modification are largely unknown.
12150998	2	32	theme	deacetylase	498:508	arg1	complex					510:516	a histone deacetylase complex	488:516	a histone deacetylase complex	488:516	Here, we show that O-GlcNAc transferase (OGT), the enzyme that catalyzes this posttranslational modification, interacts with a histone deacetylase complex by binding to the corepressor mSin3A.
12150998	0	33	dep	Recruitment	0:10	arg1	O-GlcNAcylation					89:103	coupling protein O-GlcNAcylation	72:103	Recruitment of O-GlcNAc transferase to promoters by corepressor mSin3A: coupling protein O-GlcNAcylation to transcriptional repression.	0:134	Recruitment of O-GlcNAc transferase to promoters by corepressor mSin3A: coupling protein O-GlcNAcylation to transcriptional repression.
33237428	6	0	theme	kinase	949:954	arg1	PKC					959:961	PKC	959:961	PKC	959:961	Ito reduction was prevented by inhibition of protein kinase C (PKC) and NADPH oxidase 2 (NOX2)-derived reactive oxygen species (ROS).
33237428	6	0	theme	kinase	949:954	arg1	C					956:956	protein kinase C	941:956	protein kinase C (PKC)	941:962	Ito reduction was prevented by inhibition of protein kinase C (PKC) and NADPH oxidase 2 (NOX2)-derived reactive oxygen species (ROS).
33237428	5	1	theme	IK1	649:651	arg1	amplitude					653:661	IK1 amplitude	649:661	IK1 amplitude	649:661	Additionally, IK1 amplitude and Ito recovery effects (but not Ito amplitude) were prevented by the Ca2+/calmodulin-dependent kinase II (CaMKII) inhibitor autocamtide-2-related inhibitory peptide, CaMKIIδ-knockout, and O-GlcNAc-resistant CaMKIIδ-S280A knock-in.
33237428	3	2	from	inactivation	452:463	arg1	myocytes					547:554	mouse, rat, and rabbit myocytes	524:554	mouse, rat, and rabbit myocytes	524:554	Here, we show that acute hyperglycemia increases inward rectifier K+ current (IK1), but reduces the amplitude and inactivation recovery time of the transient outward K+ current (Ito) in mouse, rat, and rabbit myocytes.
33237428	1	3	theme	channel	170:176	arg1	remodeling					178:187	K+ channel remodeling	167:187	K+ channel remodeling	167:187	Chronic hyperglycemia and diabetes lead to impaired cardiac repolarization, K+ channel remodeling and increased arrhythmia risk.
33237428	6	4	theme	reactive	999:1006	arg1	species					1015:1021	-derived reactive oxygen species	990:1021	-derived reactive oxygen species (ROS)	990:1027	Ito reduction was prevented by inhibition of protein kinase C (PKC) and NADPH oxidase 2 (NOX2)-derived reactive oxygen species (ROS).
33237428	6	4	theme	reactive	999:1006	arg1	ROS					1024:1026	ROS	1024:1026	ROS	1024:1026	Ito reduction was prevented by inhibition of protein kinase C (PKC) and NADPH oxidase 2 (NOX2)-derived reactive oxygen species (ROS).
33237428	5	5	theme	Ito	697:699	arg1	amplitude					701:709	Ito amplitude	697:709	Ito amplitude	697:709	Additionally, IK1 amplitude and Ito recovery effects (but not Ito amplitude) were prevented by the Ca2+/calmodulin-dependent kinase II (CaMKII) inhibitor autocamtide-2-related inhibitory peptide, CaMKIIδ-knockout, and O-GlcNAc-resistant CaMKIIδ-S280A knock-in.
33237428	5	5	theme	Ito	697:699	arg1	effects					680:686	Ito recovery effects	667:686	Ito recovery effects (but not Ito amplitude)	667:710	Additionally, IK1 amplitude and Ito recovery effects (but not Ito amplitude) were prevented by the Ca2+/calmodulin-dependent kinase II (CaMKII) inhibitor autocamtide-2-related inhibitory peptide, CaMKIIδ-knockout, and O-GlcNAc-resistant CaMKIIδ-S280A knock-in.
33237428	6	6	theme	protein	941:947	arg1	PKC					959:961	PKC	959:961	PKC	959:961	Ito reduction was prevented by inhibition of protein kinase C (PKC) and NADPH oxidase 2 (NOX2)-derived reactive oxygen species (ROS).
33237428	6	6	theme	protein	941:947	arg1	C					956:956	protein kinase C	941:956	protein kinase C (PKC)	941:962	Ito reduction was prevented by inhibition of protein kinase C (PKC) and NADPH oxidase 2 (NOX2)-derived reactive oxygen species (ROS).
33237428	8	7	from	downregulation	1250:1263	arg1	diabetes					1268:1275	diabetes	1268:1275	diabetes	1268:1275	However, IK1 downregulation in diabetes was markedly attenuated in CaMKIIδ-S280A.
33237428	6	8	theme	-derived	990:997	arg1	species					1015:1021	-derived reactive oxygen species	990:1021	-derived reactive oxygen species (ROS)	990:1027	Ito reduction was prevented by inhibition of protein kinase C (PKC) and NADPH oxidase 2 (NOX2)-derived reactive oxygen species (ROS).
33237428	6	8	theme	-derived	990:997	arg1	ROS					1024:1026	ROS	1024:1026	ROS	1024:1026	Ito reduction was prevented by inhibition of protein kinase C (PKC) and NADPH oxidase 2 (NOX2)-derived reactive oxygen species (ROS).
33237428	3	9	theme	inward	387:392	arg1	IK1					416:418	IK1	416:418	IK1	416:418	Here, we show that acute hyperglycemia increases inward rectifier K+ current (IK1), but reduces the amplitude and inactivation recovery time of the transient outward K+ current (Ito) in mouse, rat, and rabbit myocytes.
33237428	3	9	theme	inward	387:392	arg1	current					407:413	inward rectifier K+ current	387:413	inward rectifier K+ current (IK1)	387:419	Here, we show that acute hyperglycemia increases inward rectifier K+ current (IK1), but reduces the amplitude and inactivation recovery time of the transient outward K+ current (Ito) in mouse, rat, and rabbit myocytes.
33237428	3	10	theme	rat	531:533	arg1	myocytes					547:554	mouse, rat, and rabbit myocytes	524:554	mouse, rat, and rabbit myocytes	524:554	Here, we show that acute hyperglycemia increases inward rectifier K+ current (IK1), but reduces the amplitude and inactivation recovery time of the transient outward K+ current (Ito) in mouse, rat, and rabbit myocytes.
33237428	6	11	link	-derived	990:997	arg1	species					1015:1021	-derived reactive oxygen species	990:1021	-derived reactive oxygen species (ROS)	990:1027	Ito reduction was prevented by inhibition of protein kinase C (PKC) and NADPH oxidase 2 (NOX2)-derived reactive oxygen species (ROS).
33237428	6	11	link	-derived	990:997	arg1	ROS					1024:1026	ROS	1024:1026	ROS	1024:1026	Ito reduction was prevented by inhibition of protein kinase C (PKC) and NADPH oxidase 2 (NOX2)-derived reactive oxygen species (ROS).
33237428	6	12	dep	C	956:956	arg1	species					1015:1021	-derived reactive oxygen species	990:1021	-derived reactive oxygen species (ROS)	990:1027	Ito reduction was prevented by inhibition of protein kinase C (PKC) and NADPH oxidase 2 (NOX2)-derived reactive oxygen species (ROS).
33237428	6	12	dep	C	956:956	arg1	ROS					1024:1026	ROS	1024:1026	ROS	1024:1026	Ito reduction was prevented by inhibition of protein kinase C (PKC) and NADPH oxidase 2 (NOX2)-derived reactive oxygen species (ROS).
33237428	3	13	theme	rectifier	394:402	arg1	IK1					416:418	IK1	416:418	IK1	416:418	Here, we show that acute hyperglycemia increases inward rectifier K+ current (IK1), but reduces the amplitude and inactivation recovery time of the transient outward K+ current (Ito) in mouse, rat, and rabbit myocytes.
33237428	3	13	theme	rectifier	394:402	arg1	current					407:413	inward rectifier K+ current	387:413	inward rectifier K+ current (IK1)	387:419	Here, we show that acute hyperglycemia increases inward rectifier K+ current (IK1), but reduces the amplitude and inactivation recovery time of the transient outward K+ current (Ito) in mouse, rat, and rabbit myocytes.
33237428	5	14	theme	Ito	667:669	arg1	amplitude					701:709	Ito amplitude	697:709	Ito amplitude	697:709	Additionally, IK1 amplitude and Ito recovery effects (but not Ito amplitude) were prevented by the Ca2+/calmodulin-dependent kinase II (CaMKII) inhibitor autocamtide-2-related inhibitory peptide, CaMKIIδ-knockout, and O-GlcNAc-resistant CaMKIIδ-S280A knock-in.
33237428	5	14	theme	Ito	667:669	arg1	effects					680:686	Ito recovery effects	667:686	Ito recovery effects (but not Ito amplitude)	667:710	Additionally, IK1 amplitude and Ito recovery effects (but not Ito amplitude) were prevented by the Ca2+/calmodulin-dependent kinase II (CaMKII) inhibitor autocamtide-2-related inhibitory peptide, CaMKIIδ-knockout, and O-GlcNAc-resistant CaMKIIδ-S280A knock-in.
33237428	7	15	dep	diabetes	1057:1064	arg1	diabetes					1057:1064	chronic diabetes	1049:1064	chronic diabetes (streptozotocin, db/db, and high-fat diet)	1049:1107	In mouse models of chronic diabetes (streptozotocin, db/db, and high-fat diet), heart failure, and CaMKIIδ overexpression, both Ito and IK1 were reduced in line with the downregulated K+ channel expression.
33237428	7	15	dep	diabetes	1057:1064	arg1	db/db					1083:1087	db/db	1083:1087	db/db	1083:1087	In mouse models of chronic diabetes (streptozotocin, db/db, and high-fat diet), heart failure, and CaMKIIδ overexpression, both Ito and IK1 were reduced in line with the downregulated K+ channel expression.
33237428	7	15	dep	diabetes	1057:1064	arg1	streptozotocin					1067:1080	streptozotocin	1067:1080	streptozotocin	1067:1080	In mouse models of chronic diabetes (streptozotocin, db/db, and high-fat diet), heart failure, and CaMKIIδ overexpression, both Ito and IK1 were reduced in line with the downregulated K+ channel expression.
33237428	7	15	dep	diabetes	1057:1064	arg1	diet					1103:1106	high-fat diet	1094:1106	high-fat diet	1094:1106	In mouse models of chronic diabetes (streptozotocin, db/db, and high-fat diet), heart failure, and CaMKIIδ overexpression, both Ito and IK1 were reduced in line with the downregulated K+ channel expression.
33237428	7	16	theme	channel	1217:1223	arg1	expression					1225:1234	the downregulated K+ channel expression	1196:1234	the downregulated K+ channel expression	1196:1234	In mouse models of chronic diabetes (streptozotocin, db/db, and high-fat diet), heart failure, and CaMKIIδ overexpression, both Ito and IK1 were reduced in line with the downregulated K+ channel expression.
33237428	10	17	theme	K+	1557:1558	arg1	expression					1568:1577	K+ channel expression	1557:1577	K+ channel expression	1557:1577	Moreover, chronic hyperglycemia during diabetes and CaMKII activation downregulate K+ channel expression and function, which may further increase arrhythmia susceptibility.
33237428	9	18	theme	NOX2-ROS-PKC	1452:1463	arg1	pathway					1465:1471	a NOX2-ROS-PKC pathway	1450:1471	a NOX2-ROS-PKC pathway	1450:1471	We conclude that acute hyperglycemia enhances IK1 and Ito recovery via CaMKIIδ-S280 O-GlcNAcylation, but reduces Ito amplitude via a NOX2-ROS-PKC pathway.
33237428	5	19	dep	inhibitor	779:787	arg1	peptide					822:828	autocamtide-2-related inhibitory peptide	789:828	the Ca2+/calmodulin-dependent kinase II (CaMKII) inhibitor autocamtide-2-related inhibitory peptide	730:828	Additionally, IK1 amplitude and Ito recovery effects (but not Ito amplitude) were prevented by the Ca2+/calmodulin-dependent kinase II (CaMKII) inhibitor autocamtide-2-related inhibitory peptide, CaMKIIδ-knockout, and O-GlcNAc-resistant CaMKIIδ-S280A knock-in.
33237428	2	20	theme	K+	309:310	arg1	channels					312:319	cardiac K+ channels	301:319	cardiac K+ channels	301:319	However, the exact signaling mechanism by which diabetic hyperglycemia regulates cardiac K+ channels remains elusive.
33237428	10	21	theme	CaMKII	1526:1531	arg1	activation					1533:1542	CaMKII activation	1526:1542	CaMKII activation	1526:1542	Moreover, chronic hyperglycemia during diabetes and CaMKII activation downregulate K+ channel expression and function, which may further increase arrhythmia susceptibility.
33237428	5	22	theme	autocamtide-2-related	789:809	arg1	peptide					822:828	autocamtide-2-related inhibitory peptide	789:828	the Ca2+/calmodulin-dependent kinase II (CaMKII) inhibitor autocamtide-2-related inhibitory peptide	730:828	Additionally, IK1 amplitude and Ito recovery effects (but not Ito amplitude) were prevented by the Ca2+/calmodulin-dependent kinase II (CaMKII) inhibitor autocamtide-2-related inhibitory peptide, CaMKIIδ-knockout, and O-GlcNAc-resistant CaMKIIδ-S280A knock-in.
33237428	10	23	theme	arrhythmia	1620:1629	arg1	susceptibility					1631:1644	arrhythmia susceptibility	1620:1644	arrhythmia susceptibility	1620:1644	Moreover, chronic hyperglycemia during diabetes and CaMKII activation downregulate K+ channel expression and function, which may further increase arrhythmia susceptibility.
33237428	7	24	theme	diabetes	1057:1064	arg1	models					1039:1044	mouse models	1033:1044	mouse models of chronic diabetes (streptozotocin, db/db, and high-fat diet), heart failure, and CaMKIIδ overexpression	1033:1150	In mouse models of chronic diabetes (streptozotocin, db/db, and high-fat diet), heart failure, and CaMKIIδ overexpression, both Ito and IK1 were reduced in line with the downregulated K+ channel expression.
33237428	1	25	theme	Chronic	91:97	arg1	hyperglycemia					99:111	Chronic hyperglycemia	91:111	Chronic hyperglycemia	91:111	Chronic hyperglycemia and diabetes lead to impaired cardiac repolarization, K+ channel remodeling and increased arrhythmia risk.
33237428	1	26	theme	increased	193:201	arg1	risk					214:217	increased arrhythmia risk	193:217	increased arrhythmia risk	193:217	Chronic hyperglycemia and diabetes lead to impaired cardiac repolarization, K+ channel remodeling and increased arrhythmia risk.
33237428	5	27	theme	inhibitory	811:820	arg1	peptide					822:828	autocamtide-2-related inhibitory peptide	789:828	the Ca2+/calmodulin-dependent kinase II (CaMKII) inhibitor autocamtide-2-related inhibitory peptide	730:828	Additionally, IK1 amplitude and Ito recovery effects (but not Ito amplitude) were prevented by the Ca2+/calmodulin-dependent kinase II (CaMKII) inhibitor autocamtide-2-related inhibitory peptide, CaMKIIδ-knockout, and O-GlcNAc-resistant CaMKIIδ-S280A knock-in.
33237428	6	28	theme	NADPH	968:972	arg1	oxidase					974:980	NADPH oxidase 2	968:982	NADPH oxidase 2 (NOX2)	968:989	Ito reduction was prevented by inhibition of protein kinase C (PKC) and NADPH oxidase 2 (NOX2)-derived reactive oxygen species (ROS).
33237428	6	28	theme	NADPH	968:972	arg1	NOX2					985:988	NOX2	985:988	NOX2	985:988	Ito reduction was prevented by inhibition of protein kinase C (PKC) and NADPH oxidase 2 (NOX2)-derived reactive oxygen species (ROS).
33237428	10	29	theme	channel	1560:1566	arg1	expression					1568:1577	K+ channel expression	1557:1577	K+ channel expression	1557:1577	Moreover, chronic hyperglycemia during diabetes and CaMKII activation downregulate K+ channel expression and function, which may further increase arrhythmia susceptibility.
33237428	7	30	theme	CaMKIIδ	1129:1135	arg1	overexpression					1137:1150	CaMKIIδ overexpression	1129:1150	CaMKIIδ overexpression	1129:1150	In mouse models of chronic diabetes (streptozotocin, db/db, and high-fat diet), heart failure, and CaMKIIδ overexpression, both Ito and IK1 were reduced in line with the downregulated K+ channel expression.
33237428	1	31	theme	arrhythmia	203:212	arg1	risk					214:217	increased arrhythmia risk	193:217	increased arrhythmia risk	193:217	Chronic hyperglycemia and diabetes lead to impaired cardiac repolarization, K+ channel remodeling and increased arrhythmia risk.
33237428	7	32	theme	overexpression	1137:1150	arg1	models					1039:1044	mouse models	1033:1044	mouse models of chronic diabetes (streptozotocin, db/db, and high-fat diet), heart failure, and CaMKIIδ overexpression	1033:1150	In mouse models of chronic diabetes (streptozotocin, db/db, and high-fat diet), heart failure, and CaMKIIδ overexpression, both Ito and IK1 were reduced in line with the downregulated K+ channel expression.
33237428	6	33	theme	Ito	896:898	arg1	reduction					900:908	Ito reduction	896:908	Ito reduction	896:908	Ito reduction was prevented by inhibition of protein kinase C (PKC) and NADPH oxidase 2 (NOX2)-derived reactive oxygen species (ROS).
33237428	3	34	theme	K+	404:405	arg1	IK1					416:418	IK1	416:418	IK1	416:418	Here, we show that acute hyperglycemia increases inward rectifier K+ current (IK1), but reduces the amplitude and inactivation recovery time of the transient outward K+ current (Ito) in mouse, rat, and rabbit myocytes.
33237428	3	34	theme	K+	404:405	arg1	current					407:413	inward rectifier K+ current	387:413	inward rectifier K+ current (IK1)	387:419	Here, we show that acute hyperglycemia increases inward rectifier K+ current (IK1), but reduces the amplitude and inactivation recovery time of the transient outward K+ current (Ito) in mouse, rat, and rabbit myocytes.
33237428	7	35	theme	chronic	1049:1055	arg1	diet					1103:1106	high-fat diet	1094:1106	high-fat diet	1094:1106	In mouse models of chronic diabetes (streptozotocin, db/db, and high-fat diet), heart failure, and CaMKIIδ overexpression, both Ito and IK1 were reduced in line with the downregulated K+ channel expression.
33237428	7	35	theme	chronic	1049:1055	arg1	db/db					1083:1087	db/db	1083:1087	db/db	1083:1087	In mouse models of chronic diabetes (streptozotocin, db/db, and high-fat diet), heart failure, and CaMKIIδ overexpression, both Ito and IK1 were reduced in line with the downregulated K+ channel expression.
33237428	7	35	theme	chronic	1049:1055	arg1	streptozotocin					1067:1080	streptozotocin	1067:1080	streptozotocin	1067:1080	In mouse models of chronic diabetes (streptozotocin, db/db, and high-fat diet), heart failure, and CaMKIIδ overexpression, both Ito and IK1 were reduced in line with the downregulated K+ channel expression.
33237428	7	35	theme	chronic	1049:1055	arg1	diabetes					1057:1064	chronic diabetes	1049:1064	chronic diabetes (streptozotocin, db/db, and high-fat diet)	1049:1107	In mouse models of chronic diabetes (streptozotocin, db/db, and high-fat diet), heart failure, and CaMKIIδ overexpression, both Ito and IK1 were reduced in line with the downregulated K+ channel expression.
33237428	9	36	theme	Ito	1432:1434	arg1	amplitude					1436:1444	Ito amplitude	1432:1444	Ito amplitude	1432:1444	We conclude that acute hyperglycemia enhances IK1 and Ito recovery via CaMKIIδ-S280 O-GlcNAcylation, but reduces Ito amplitude via a NOX2-ROS-PKC pathway.
33237428	0	37	theme	cardiac	24:30	arg1	channels					35:42	cardiac K+ channels	24:42	cardiac K+ channels	24:42	Hyperglycemia regulates cardiac K+ channels via O-GlcNAc-CaMKII and NOX2-ROS-PKC pathways.
33237428	6	38	theme	oxidase	974:980	arg1	inhibition					927:936	inhibition	927:936	inhibition of protein kinase C (PKC) and NADPH oxidase 2 (NOX2)-derived reactive oxygen species (ROS)	927:1027	Ito reduction was prevented by inhibition of protein kinase C (PKC) and NADPH oxidase 2 (NOX2)-derived reactive oxygen species (ROS).
33237428	3	39	theme	mouse	524:528	arg1	myocytes					547:554	mouse, rat, and rabbit myocytes	524:554	mouse, rat, and rabbit myocytes	524:554	Here, we show that acute hyperglycemia increases inward rectifier K+ current (IK1), but reduces the amplitude and inactivation recovery time of the transient outward K+ current (Ito) in mouse, rat, and rabbit myocytes.
33237428	9	40	dep	IK1	1365:1367	arg1	recovery					1377:1384	recovery	1377:1384	recovery	1377:1384	We conclude that acute hyperglycemia enhances IK1 and Ito recovery via CaMKIIδ-S280 O-GlcNAcylation, but reduces Ito amplitude via a NOX2-ROS-PKC pathway.
33237428	3	41	theme	rabbit	540:545	arg1	myocytes					547:554	mouse, rat, and rabbit myocytes	524:554	mouse, rat, and rabbit myocytes	524:554	Here, we show that acute hyperglycemia increases inward rectifier K+ current (IK1), but reduces the amplitude and inactivation recovery time of the transient outward K+ current (Ito) in mouse, rat, and rabbit myocytes.
33237428	7	42	theme	heart	1110:1114	arg1	failure					1116:1122	heart failure	1110:1122	heart failure	1110:1122	In mouse models of chronic diabetes (streptozotocin, db/db, and high-fat diet), heart failure, and CaMKIIδ overexpression, both Ito and IK1 were reduced in line with the downregulated K+ channel expression.
33237428	3	43	theme	current	507:513	arg1	inactivation					452:463	inactivation	452:463	inactivation	452:463	Here, we show that acute hyperglycemia increases inward rectifier K+ current (IK1), but reduces the amplitude and inactivation recovery time of the transient outward K+ current (Ito) in mouse, rat, and rabbit myocytes.
33237428	3	43	theme	current	507:513	arg1	amplitude					438:446	amplitude	438:446	amplitude	438:446	Here, we show that acute hyperglycemia increases inward rectifier K+ current (IK1), but reduces the amplitude and inactivation recovery time of the transient outward K+ current (Ito) in mouse, rat, and rabbit myocytes.
33237428	5	44	theme	O-GlcNAc-resistant	853:870	arg1	knock-in					886:893	O-GlcNAc-resistant CaMKIIδ-S280A knock-in	853:893	O-GlcNAc-resistant CaMKIIδ-S280A knock-in	853:893	Additionally, IK1 amplitude and Ito recovery effects (but not Ito amplitude) were prevented by the Ca2+/calmodulin-dependent kinase II (CaMKII) inhibitor autocamtide-2-related inhibitory peptide, CaMKIIδ-knockout, and O-GlcNAc-resistant CaMKIIδ-S280A knock-in.
33237428	7	45	with	line	1186:1189	arg1	expression					1225:1234	the downregulated K+ channel expression	1196:1234	the downregulated K+ channel expression	1196:1234	In mouse models of chronic diabetes (streptozotocin, db/db, and high-fat diet), heart failure, and CaMKIIδ overexpression, both Ito and IK1 were reduced in line with the downregulated K+ channel expression.
33237428	3	46	theme	recovery	465:472	arg1	time					474:477	recovery time	465:477	recovery time	465:477	Here, we show that acute hyperglycemia increases inward rectifier K+ current (IK1), but reduces the amplitude and inactivation recovery time of the transient outward K+ current (Ito) in mouse, rat, and rabbit myocytes.
33237428	7	47	theme	failure	1116:1122	arg1	models					1039:1044	mouse models	1033:1044	mouse models of chronic diabetes (streptozotocin, db/db, and high-fat diet), heart failure, and CaMKIIδ overexpression	1033:1150	In mouse models of chronic diabetes (streptozotocin, db/db, and high-fat diet), heart failure, and CaMKIIδ overexpression, both Ito and IK1 were reduced in line with the downregulated K+ channel expression.
33237428	7	48	theme	high-fat	1094:1101	arg1	diabetes					1057:1064	chronic diabetes	1049:1064	chronic diabetes (streptozotocin, db/db, and high-fat diet)	1049:1107	In mouse models of chronic diabetes (streptozotocin, db/db, and high-fat diet), heart failure, and CaMKIIδ overexpression, both Ito and IK1 were reduced in line with the downregulated K+ channel expression.
33237428	7	48	theme	high-fat	1094:1101	arg1	diet					1103:1106	high-fat diet	1094:1106	high-fat diet	1094:1106	In mouse models of chronic diabetes (streptozotocin, db/db, and high-fat diet), heart failure, and CaMKIIδ overexpression, both Ito and IK1 were reduced in line with the downregulated K+ channel expression.
33237428	9	49	theme	acute	1336:1340	arg1	hyperglycemia					1342:1354	acute hyperglycemia	1336:1354	acute hyperglycemia	1336:1354	We conclude that acute hyperglycemia enhances IK1 and Ito recovery via CaMKIIδ-S280 O-GlcNAcylation, but reduces Ito amplitude via a NOX2-ROS-PKC pathway.
33237428	0	50	theme	K+	32:33	arg1	channels					35:42	cardiac K+ channels	24:42	cardiac K+ channels	24:42	Hyperglycemia regulates cardiac K+ channels via O-GlcNAc-CaMKII and NOX2-ROS-PKC pathways.
33237428	8	51	theme	IK1	1246:1248	arg1	downregulation					1250:1263	IK1 downregulation	1246:1263	IK1 downregulation in diabetes	1246:1275	However, IK1 downregulation in diabetes was markedly attenuated in CaMKIIδ-S280A.
33237428	5	52	theme	CaMKIIδ-S280A	872:884	arg1	knock-in					886:893	O-GlcNAc-resistant CaMKIIδ-S280A knock-in	853:893	O-GlcNAc-resistant CaMKIIδ-S280A knock-in	853:893	Additionally, IK1 amplitude and Ito recovery effects (but not Ito amplitude) were prevented by the Ca2+/calmodulin-dependent kinase II (CaMKII) inhibitor autocamtide-2-related inhibitory peptide, CaMKIIδ-knockout, and O-GlcNAc-resistant CaMKIIδ-S280A knock-in.
33237428	5	53	theme	recovery	671:678	arg1	amplitude					701:709	Ito amplitude	697:709	Ito amplitude	697:709	Additionally, IK1 amplitude and Ito recovery effects (but not Ito amplitude) were prevented by the Ca2+/calmodulin-dependent kinase II (CaMKII) inhibitor autocamtide-2-related inhibitory peptide, CaMKIIδ-knockout, and O-GlcNAc-resistant CaMKIIδ-S280A knock-in.
33237428	5	53	theme	recovery	671:678	arg1	effects					680:686	Ito recovery effects	667:686	Ito recovery effects (but not Ito amplitude)	667:710	Additionally, IK1 amplitude and Ito recovery effects (but not Ito amplitude) were prevented by the Ca2+/calmodulin-dependent kinase II (CaMKII) inhibitor autocamtide-2-related inhibitory peptide, CaMKIIδ-knockout, and O-GlcNAc-resistant CaMKIIδ-S280A knock-in.
33237428	3	54	theme	acute	357:361	arg1	hyperglycemia					363:375	acute hyperglycemia	357:375	acute hyperglycemia	357:375	Here, we show that acute hyperglycemia increases inward rectifier K+ current (IK1), but reduces the amplitude and inactivation recovery time of the transient outward K+ current (Ito) in mouse, rat, and rabbit myocytes.
33237428	2	55	theme	signaling	239:247	arg1	mechanism					249:257	the exact signaling mechanism	229:257	the exact signaling mechanism by which diabetic hyperglycemia regulates cardiac K+ channels	229:319	However, the exact signaling mechanism by which diabetic hyperglycemia regulates cardiac K+ channels remains elusive.
33237428	3	56	theme	K+	504:505	arg1	Ito					516:518	Ito	516:518	Ito	516:518	Here, we show that acute hyperglycemia increases inward rectifier K+ current (IK1), but reduces the amplitude and inactivation recovery time of the transient outward K+ current (Ito) in mouse, rat, and rabbit myocytes.
33237428	3	56	theme	K+	504:505	arg1	current					507:513	the transient outward K+ current	482:513	the transient outward K+ current (Ito)	482:519	Here, we show that acute hyperglycemia increases inward rectifier K+ current (IK1), but reduces the amplitude and inactivation recovery time of the transient outward K+ current (Ito) in mouse, rat, and rabbit myocytes.
33237428	0	57	theme	O-GlcNAc-CaMKII	48:62	arg1	pathways					81:88	O-GlcNAc-CaMKII and NOX2-ROS-PKC pathways	48:88	O-GlcNAc-CaMKII and NOX2-ROS-PKC pathways	48:88	Hyperglycemia regulates cardiac K+ channels via O-GlcNAc-CaMKII and NOX2-ROS-PKC pathways.
33237428	7	58	theme	mouse	1033:1037	arg1	models					1039:1044	mouse models	1033:1044	mouse models of chronic diabetes (streptozotocin, db/db, and high-fat diet), heart failure, and CaMKIIδ overexpression	1033:1150	In mouse models of chronic diabetes (streptozotocin, db/db, and high-fat diet), heart failure, and CaMKIIδ overexpression, both Ito and IK1 were reduced in line with the downregulated K+ channel expression.
33237428	2	59	theme	exact	233:237	arg1	mechanism					249:257	the exact signaling mechanism	229:257	the exact signaling mechanism by which diabetic hyperglycemia regulates cardiac K+ channels	229:319	However, the exact signaling mechanism by which diabetic hyperglycemia regulates cardiac K+ channels remains elusive.
33237428	1	60	theme	impaired	134:141	arg1	repolarization					151:164	impaired cardiac repolarization	134:164	impaired cardiac repolarization	134:164	Chronic hyperglycemia and diabetes lead to impaired cardiac repolarization, K+ channel remodeling and increased arrhythmia risk.
33237428	7	61	theme	downregulated	1200:1212	arg1	expression					1225:1234	the downregulated K+ channel expression	1196:1234	the downregulated K+ channel expression	1196:1234	In mouse models of chronic diabetes (streptozotocin, db/db, and high-fat diet), heart failure, and CaMKIIδ overexpression, both Ito and IK1 were reduced in line with the downregulated K+ channel expression.
33237428	10	62	theme	chronic	1484:1490	arg1	hyperglycemia					1492:1504	chronic hyperglycemia	1484:1504	chronic hyperglycemia during diabetes and CaMKII activation	1484:1542	Moreover, chronic hyperglycemia during diabetes and CaMKII activation downregulate K+ channel expression and function, which may further increase arrhythmia susceptibility.
33237428	3	63	dep	amplitude	438:446	arg1	time					474:477	recovery time	465:477	recovery time	465:477	Here, we show that acute hyperglycemia increases inward rectifier K+ current (IK1), but reduces the amplitude and inactivation recovery time of the transient outward K+ current (Ito) in mouse, rat, and rabbit myocytes.
33237428	3	63	dep	amplitude	438:446	arg1	the					434:436	the	434:436	the	434:436	Here, we show that acute hyperglycemia increases inward rectifier K+ current (IK1), but reduces the amplitude and inactivation recovery time of the transient outward K+ current (Ito) in mouse, rat, and rabbit myocytes.
33237428	1	64	theme	cardiac	143:149	arg1	repolarization					151:164	impaired cardiac repolarization	134:164	impaired cardiac repolarization	134:164	Chronic hyperglycemia and diabetes lead to impaired cardiac repolarization, K+ channel remodeling and increased arrhythmia risk.
33237428	2	65	theme	cardiac	301:307	arg1	channels					312:319	cardiac K+ channels	301:319	cardiac K+ channels	301:319	However, the exact signaling mechanism by which diabetic hyperglycemia regulates cardiac K+ channels remains elusive.
33237428	3	66	theme	outward	496:502	arg1	Ito					516:518	Ito	516:518	Ito	516:518	Here, we show that acute hyperglycemia increases inward rectifier K+ current (IK1), but reduces the amplitude and inactivation recovery time of the transient outward K+ current (Ito) in mouse, rat, and rabbit myocytes.
33237428	3	66	theme	outward	496:502	arg1	current					507:513	the transient outward K+ current	482:513	the transient outward K+ current (Ito)	482:519	Here, we show that acute hyperglycemia increases inward rectifier K+ current (IK1), but reduces the amplitude and inactivation recovery time of the transient outward K+ current (Ito) in mouse, rat, and rabbit myocytes.
33237428	3	67	theme	transient	486:494	arg1	Ito					516:518	Ito	516:518	Ito	516:518	Here, we show that acute hyperglycemia increases inward rectifier K+ current (IK1), but reduces the amplitude and inactivation recovery time of the transient outward K+ current (Ito) in mouse, rat, and rabbit myocytes.
33237428	3	67	theme	transient	486:494	arg1	current					507:513	the transient outward K+ current	482:513	the transient outward K+ current (Ito)	482:519	Here, we show that acute hyperglycemia increases inward rectifier K+ current (IK1), but reduces the amplitude and inactivation recovery time of the transient outward K+ current (Ito) in mouse, rat, and rabbit myocytes.
33237428	5	68	theme	Ca2+/calmodulin-dependent	734:758	arg1	kinase					760:765	the Ca2+/calmodulin-dependent kinase II	730:768	the Ca2+/calmodulin-dependent kinase II (CaMKII) inhibitor autocamtide-2-related inhibitory peptide	730:828	Additionally, IK1 amplitude and Ito recovery effects (but not Ito amplitude) were prevented by the Ca2+/calmodulin-dependent kinase II (CaMKII) inhibitor autocamtide-2-related inhibitory peptide, CaMKIIδ-knockout, and O-GlcNAc-resistant CaMKIIδ-S280A knock-in.
33237428	5	68	theme	Ca2+/calmodulin-dependent	734:758	arg1	CaMKII					771:776	CaMKII	771:776	CaMKII	771:776	Additionally, IK1 amplitude and Ito recovery effects (but not Ito amplitude) were prevented by the Ca2+/calmodulin-dependent kinase II (CaMKII) inhibitor autocamtide-2-related inhibitory peptide, CaMKIIδ-knockout, and O-GlcNAc-resistant CaMKIIδ-S280A knock-in.
33237428	2	69	theme	diabetic	268:275	arg1	hyperglycemia					277:289	diabetic hyperglycemia	268:289	diabetic hyperglycemia	268:289	However, the exact signaling mechanism by which diabetic hyperglycemia regulates cardiac K+ channels remains elusive.
33237428	3	70	from	amplitude	438:446	arg1	myocytes					547:554	mouse, rat, and rabbit myocytes	524:554	mouse, rat, and rabbit myocytes	524:554	Here, we show that acute hyperglycemia increases inward rectifier K+ current (IK1), but reduces the amplitude and inactivation recovery time of the transient outward K+ current (Ito) in mouse, rat, and rabbit myocytes.
33237428	5	71	theme	kinase	760:765	arg1	inhibitor					779:787	the Ca2+/calmodulin-dependent kinase II (CaMKII) inhibitor	730:787	the Ca2+/calmodulin-dependent kinase II (CaMKII) inhibitor autocamtide-2-related inhibitory peptide	730:828	Additionally, IK1 amplitude and Ito recovery effects (but not Ito amplitude) were prevented by the Ca2+/calmodulin-dependent kinase II (CaMKII) inhibitor autocamtide-2-related inhibitory peptide, CaMKIIδ-knockout, and O-GlcNAc-resistant CaMKIIδ-S280A knock-in.
33237428	4	72	theme	intracellular	604:616	arg1	O-GlcNAcylation					618:632	intracellular O-GlcNAcylation	604:632	intracellular O-GlcNAcylation	604:632	These changes were all critically dependent on intracellular O-GlcNAcylation.
33237428	0	73	theme	NOX2-ROS-PKC	68:79	arg1	pathways					81:88	O-GlcNAc-CaMKII and NOX2-ROS-PKC pathways	48:88	O-GlcNAc-CaMKII and NOX2-ROS-PKC pathways	48:88	Hyperglycemia regulates cardiac K+ channels via O-GlcNAc-CaMKII and NOX2-ROS-PKC pathways.
33237428	6	74	theme	C	956:956	arg1	inhibition					927:936	inhibition	927:936	inhibition of protein kinase C (PKC) and NADPH oxidase 2 (NOX2)-derived reactive oxygen species (ROS)	927:1027	Ito reduction was prevented by inhibition of protein kinase C (PKC) and NADPH oxidase 2 (NOX2)-derived reactive oxygen species (ROS).
33237428	7	75	theme	K+	1214:1215	arg1	expression					1225:1234	the downregulated K+ channel expression	1196:1234	the downregulated K+ channel expression	1196:1234	In mouse models of chronic diabetes (streptozotocin, db/db, and high-fat diet), heart failure, and CaMKIIδ overexpression, both Ito and IK1 were reduced in line with the downregulated K+ channel expression.
33237428	1	76	theme	K+	167:168	arg1	remodeling					178:187	K+ channel remodeling	167:187	K+ channel remodeling	167:187	Chronic hyperglycemia and diabetes lead to impaired cardiac repolarization, K+ channel remodeling and increased arrhythmia risk.
33237428	6	77	theme	oxygen	1008:1013	arg1	species					1015:1021	-derived reactive oxygen species	990:1021	-derived reactive oxygen species (ROS)	990:1027	Ito reduction was prevented by inhibition of protein kinase C (PKC) and NADPH oxidase 2 (NOX2)-derived reactive oxygen species (ROS).
33237428	6	77	theme	oxygen	1008:1013	arg1	ROS					1024:1026	ROS	1024:1026	ROS	1024:1026	Ito reduction was prevented by inhibition of protein kinase C (PKC) and NADPH oxidase 2 (NOX2)-derived reactive oxygen species (ROS).
35818332	5	0	theme	SNW1	798:801	arg1	SNW1					778:781	SNW1	778:781	SNW1	778:781	O-GlcNAc levels in SNW1 and effects of SNW1 on NF-κB p65 were determined by immunoprecipitation.
35818332	5	0	theme	SNW1	798:801	arg1	effects					787:793	effects	787:793	effects of SNW1 on NF-κB p65	787:814	O-GlcNAc levels in SNW1 and effects of SNW1 on NF-κB p65 were determined by immunoprecipitation.
35818332	8	1	theme	SNW1	1226:1229	arg1	O-GlcNAcylation					1207:1221	O-GlcNAcylation	1207:1221	O-GlcNAcylation of SNW1	1207:1229	Dex reversed the H/R-induced increase of SNW1 protein by upregulating OGT and enhancing O-GlcNAcylation of SNW1.
35818332	2	2	theme	p65	399:401	arg1	coactivator					336:346	a coactivator	334:346	a coactivator of the pro-inflammatory transcription factor NF-κB p65	334:401	SNW domain-containing protein 1 (SNW1) is a coactivator of the pro-inflammatory transcription factor NF-κB p65.
35818332	2	2	theme	p65	399:401	arg1	protein					314:320	SNW domain-containing protein 1	292:322	SNW domain-containing protein 1 (SNW1)	292:329	SNW domain-containing protein 1 (SNW1) is a coactivator of the pro-inflammatory transcription factor NF-κB p65.
35818332	7	3	theme	Luciferase	931:940	arg1	assay					951:955	A Luciferase reporter assay	929:955	A Luciferase reporter assay	929:955	A Luciferase reporter assay demonstrated that increased SNW1 levels led to increased NF-κB p65 activity and increased secretion of neuron-derived inflammatory factors demonstrated by ELISA.
35818332	4	4	theme	PC12	630:633	arg1	cells					635:639	SH-SY5Y and PC12 cells	618:639	cells	635:639	SH-SY5Y and PC12 cells under hypoxia/reoxygenation (H/R) conditions were treated with Dex and with inhibitors of O-GlcNAc transferase (OGT).
35818332	6	5	theme	SNW1	870:873	arg1	levels					883:888	SNW1 protein levels	870:888	SNW1 protein levels	870:888	H/R increased SNW1 protein levels but inhibited O-GlcNAcylation of SNW1.
35818332	7	6	theme	NF-κB	1014:1018	arg1	activity					1024:1031	increased NF-κB p65 activity	1004:1031	increased NF-κB p65 activity	1004:1031	A Luciferase reporter assay demonstrated that increased SNW1 levels led to increased NF-κB p65 activity and increased secretion of neuron-derived inflammatory factors demonstrated by ELISA.
35818332	2	7	theme	NF-κB	393:397	arg1	p65					399:401	the pro-inflammatory transcription factor NF-κB p65	351:401	the pro-inflammatory transcription factor NF-κB p65	351:401	SNW domain-containing protein 1 (SNW1) is a coactivator of the pro-inflammatory transcription factor NF-κB p65.
35818332	5	8	from	p65	812:814	arg1	levels					768:773	O-GlcNAc levels	759:773	O-GlcNAc levels in SNW1 and effects of SNW1 on NF-κB p65	759:814	O-GlcNAc levels in SNW1 and effects of SNW1 on NF-κB p65 were determined by immunoprecipitation.
35818332	7	9	theme	p65	1020:1022	arg1	activity					1024:1031	increased NF-κB p65 activity	1004:1031	increased NF-κB p65 activity	1004:1031	A Luciferase reporter assay demonstrated that increased SNW1 levels led to increased NF-κB p65 activity and increased secretion of neuron-derived inflammatory factors demonstrated by ELISA.
35818332	0	10	theme	SNW1	132:135	arg1	O-GlcNAcylation					113:127	O-GlcNAcylation	113:127	O-GlcNAcylation of SNW1	113:135	Dexmedetomidine Inhibits NF-κB-Transcriptional Activity in Neurons Undergoing Ischemia-Reperfusion by Regulating O-GlcNAcylation of SNW1.
35818332	9	11	theme	complex	1266:1272	arg1	suppression					1236:1246	Dex suppression	1232:1246	Dex suppression of the SNW1/NF-κB complex	1232:1272	Dex suppression of the SNW1/NF-κB complex resulted in neuroprotection in vitro and in a middle cerebral artery occlusion model in vivo.
35818332	10	12	theme	ERK1/2	1376:1381	arg1	inhibitors					1383:1392	PKA and ERK1/2 inhibitors	1368:1392	PKA and ERK1/2 inhibitors	1368:1392	PKA and ERK1/2 inhibitors abolished the effect of Dex on OGT protein.
35818332	10	13	theme	PKA	1368:1370	arg1	inhibitors					1383:1392	PKA and ERK1/2 inhibitors	1368:1392	PKA and ERK1/2 inhibitors	1368:1392	PKA and ERK1/2 inhibitors abolished the effect of Dex on OGT protein.
35818332	4	14	theme	transferase	740:750	arg1	inhibitors					717:726	inhibitors	717:726	inhibitors of O-GlcNAc transferase (OGT)	717:756	SH-SY5Y and PC12 cells under hypoxia/reoxygenation (H/R) conditions were treated with Dex and with inhibitors of O-GlcNAc transferase (OGT).
35818332	1	15	from	ischemia-reperfusion	182:201	arg1	neuroprotective					163:177	neuroprotective	163:177	neuroprotective	163:177	Dexmedetomidine (Dex) is neuroprotective in ischemia-reperfusion (I/R) by suppressing inflammation but the underlying molecular mechanisms are not known.
35818332	10	16	from	effect	1408:1413	arg1	protein					1429:1435	OGT protein	1425:1435	OGT protein	1425:1435	PKA and ERK1/2 inhibitors abolished the effect of Dex on OGT protein.
35818332	3	17	from	activity	531:538	arg1	neurons					543:549	neurons	543:549	neurons undergoing I/R	543:564	Because SNW1 is regulated by O-GlcNAcylation, we aimed to determine whether this modification influences NF-κB transcriptional activity in neurons undergoing I/R and how Dex may affect the O-GlcNAcylation of SNW1.
35818332	9	18	theme	occlusion	1343:1351	arg1	model					1353:1357	a middle cerebral artery occlusion model	1318:1357	a middle cerebral artery occlusion model in vivo	1318:1365	Dex suppression of the SNW1/NF-κB complex resulted in neuroprotection in vitro and in a middle cerebral artery occlusion model in vivo.
35818332	6	19	theme	SNW1	923:926	arg1	O-GlcNAcylation					904:918	O-GlcNAcylation	904:918	O-GlcNAcylation of SNW1	904:926	H/R increased SNW1 protein levels but inhibited O-GlcNAcylation of SNW1.
35818332	8	20	theme	H/R-induced	1136:1146	arg1	increase					1148:1155	the H/R-induced increase	1132:1155	the H/R-induced increase of SNW1 protein	1132:1171	Dex reversed the H/R-induced increase of SNW1 protein by upregulating OGT and enhancing O-GlcNAcylation of SNW1.
35818332	1	21	from	neuroprotective	163:177	arg1	ischemia-reperfusion					182:201	ischemia-reperfusion	182:201	ischemia-reperfusion (I/R)	182:207	Dexmedetomidine (Dex) is neuroprotective in ischemia-reperfusion (I/R) by suppressing inflammation but the underlying molecular mechanisms are not known.
35818332	1	21	from	neuroprotective	163:177	arg1	I/R					204:206	I/R	204:206	I/R	204:206	Dexmedetomidine (Dex) is neuroprotective in ischemia-reperfusion (I/R) by suppressing inflammation but the underlying molecular mechanisms are not known.
35818332	11	22	theme	NF-κB-transcriptional	1492:1512	arg1	activity					1514:1521	NF-κB-transcriptional activity	1492:1521	NF-κB-transcriptional activity in neurons undergoing I/R	1492:1547	Taken together, these data indicate that Dex inhibits NF-κB-transcriptional activity in neurons undergoing I/R by regulating O-GlcNAcylation of SNW1.
35818332	7	23	theme	increased	975:983	arg1	levels					990:995	increased SNW1 levels	975:995	increased SNW1 levels	975:995	A Luciferase reporter assay demonstrated that increased SNW1 levels led to increased NF-κB p65 activity and increased secretion of neuron-derived inflammatory factors demonstrated by ELISA.
35818332	10	24	theme	Dex	1418:1420	arg1	effect					1408:1413	the effect	1404:1413	the effect of Dex on OGT protein	1404:1435	PKA and ERK1/2 inhibitors abolished the effect of Dex on OGT protein.
35818332	11	25	from	activity	1514:1521	arg1	neurons					1526:1532	neurons	1526:1532	neurons undergoing I/R	1526:1547	Taken together, these data indicate that Dex inhibits NF-κB-transcriptional activity in neurons undergoing I/R by regulating O-GlcNAcylation of SNW1.
35818332	7	26	theme	SNW1	985:988	arg1	levels					990:995	increased SNW1 levels	975:995	increased SNW1 levels	975:995	A Luciferase reporter assay demonstrated that increased SNW1 levels led to increased NF-κB p65 activity and increased secretion of neuron-derived inflammatory factors demonstrated by ELISA.
35818332	9	27	theme	SNW1/NF-κB	1255:1264	arg1	complex					1266:1272	the SNW1/NF-κB complex	1251:1272	the SNW1/NF-κB complex	1251:1272	Dex suppression of the SNW1/NF-κB complex resulted in neuroprotection in vitro and in a middle cerebral artery occlusion model in vivo.
35818332	3	28	theme	NF-κB	509:513	arg1	activity					531:538	NF-κB transcriptional activity	509:538	NF-κB transcriptional activity in neurons undergoing I/R	509:564	Because SNW1 is regulated by O-GlcNAcylation, we aimed to determine whether this modification influences NF-κB transcriptional activity in neurons undergoing I/R and how Dex may affect the O-GlcNAcylation of SNW1.
35818332	0	29	theme	NF-κB-Transcriptional	25:45	arg1	Activity					47:54	NF-κB-Transcriptional Activity	25:54	NF-κB-Transcriptional Activity in Neurons Undergoing Ischemia-Reperfusion	25:97	Dexmedetomidine Inhibits NF-κB-Transcriptional Activity in Neurons Undergoing Ischemia-Reperfusion by Regulating O-GlcNAcylation of SNW1.
35818332	4	30	theme	SH-SY5Y	618:624	arg1	cells					635:639	SH-SY5Y and PC12 cells	618:639	cells	635:639	SH-SY5Y and PC12 cells under hypoxia/reoxygenation (H/R) conditions were treated with Dex and with inhibitors of O-GlcNAc transferase (OGT).
35818332	5	31	from	SNW1	778:781	arg1	p65					812:814	NF-κB p65	806:814	NF-κB p65	806:814	O-GlcNAc levels in SNW1 and effects of SNW1 on NF-κB p65 were determined by immunoprecipitation.
35818332	3	32	theme	SNW1	612:615	arg1	O-GlcNAcylation					593:607	the O-GlcNAcylation	589:607	the O-GlcNAcylation of SNW1	589:615	Because SNW1 is regulated by O-GlcNAcylation, we aimed to determine whether this modification influences NF-κB transcriptional activity in neurons undergoing I/R and how Dex may affect the O-GlcNAcylation of SNW1.
35818332	7	33	theme	increased	1004:1012	arg1	activity					1024:1031	increased NF-κB p65 activity	1004:1031	increased NF-κB p65 activity	1004:1031	A Luciferase reporter assay demonstrated that increased SNW1 levels led to increased NF-κB p65 activity and increased secretion of neuron-derived inflammatory factors demonstrated by ELISA.
35818332	3	34	theme	transcriptional	515:529	arg1	activity					531:538	NF-κB transcriptional activity	509:538	NF-κB transcriptional activity in neurons undergoing I/R	509:564	Because SNW1 is regulated by O-GlcNAcylation, we aimed to determine whether this modification influences NF-κB transcriptional activity in neurons undergoing I/R and how Dex may affect the O-GlcNAcylation of SNW1.
35818332	5	35	theme	NF-κB	806:810	arg1	p65					812:814	NF-κB p65	806:814	NF-κB p65	806:814	O-GlcNAc levels in SNW1 and effects of SNW1 on NF-κB p65 were determined by immunoprecipitation.
35818332	8	36	theme	protein	1165:1171	arg1	increase					1148:1155	the H/R-induced increase	1132:1155	the H/R-induced increase of SNW1 protein	1132:1171	Dex reversed the H/R-induced increase of SNW1 protein by upregulating OGT and enhancing O-GlcNAcylation of SNW1.
35818332	1	37	theme	underlying	245:254	arg1	mechanisms					266:275	the underlying molecular mechanisms	241:275	the underlying molecular mechanisms	241:275	Dexmedetomidine (Dex) is neuroprotective in ischemia-reperfusion (I/R) by suppressing inflammation but the underlying molecular mechanisms are not known.
35818332	5	38	theme	O-GlcNAc	759:766	arg1	levels					768:773	O-GlcNAc levels	759:773	O-GlcNAc levels in SNW1 and effects of SNW1 on NF-κB p65	759:814	O-GlcNAc levels in SNW1 and effects of SNW1 on NF-κB p65 were determined by immunoprecipitation.
35818332	5	39	from	levels	768:773	arg1	SNW1					778:781	SNW1	778:781	SNW1	778:781	O-GlcNAc levels in SNW1 and effects of SNW1 on NF-κB p65 were determined by immunoprecipitation.
35818332	5	39	from	levels	768:773	arg1	p65					812:814	NF-κB p65	806:814	NF-κB p65	806:814	O-GlcNAc levels in SNW1 and effects of SNW1 on NF-κB p65 were determined by immunoprecipitation.
35818332	5	39	from	levels	768:773	arg1	effects					787:793	effects	787:793	effects of SNW1 on NF-κB p65	787:814	O-GlcNAc levels in SNW1 and effects of SNW1 on NF-κB p65 were determined by immunoprecipitation.
35818332	7	40	theme	inflammatory	1075:1086	arg1	factors					1088:1094	neuron-derived inflammatory factors	1060:1094	neuron-derived inflammatory factors demonstrated by ELISA	1060:1116	A Luciferase reporter assay demonstrated that increased SNW1 levels led to increased NF-κB p65 activity and increased secretion of neuron-derived inflammatory factors demonstrated by ELISA.
35818332	1	41	theme	molecular	256:264	arg1	mechanisms					266:275	the underlying molecular mechanisms	241:275	the underlying molecular mechanisms	241:275	Dexmedetomidine (Dex) is neuroprotective in ischemia-reperfusion (I/R) by suppressing inflammation but the underlying molecular mechanisms are not known.
35818332	7	42	link	neuron-derived	1060:1073	arg1	factors					1088:1094	neuron-derived inflammatory factors	1060:1094	neuron-derived inflammatory factors demonstrated by ELISA	1060:1116	A Luciferase reporter assay demonstrated that increased SNW1 levels led to increased NF-κB p65 activity and increased secretion of neuron-derived inflammatory factors demonstrated by ELISA.
35818332	9	43	theme	middle	1320:1325	arg1	occlusion					1343:1351	middle cerebral artery occlusion	1320:1351	a middle cerebral artery occlusion model in vivo	1318:1365	Dex suppression of the SNW1/NF-κB complex resulted in neuroprotection in vitro and in a middle cerebral artery occlusion model in vivo.
35818332	7	44	theme	factors	1088:1094	arg1	activity					1024:1031	increased NF-κB p65 activity	1004:1031	increased NF-κB p65 activity	1004:1031	A Luciferase reporter assay demonstrated that increased SNW1 levels led to increased NF-κB p65 activity and increased secretion of neuron-derived inflammatory factors demonstrated by ELISA.
35818332	7	44	theme	factors	1088:1094	arg1	secretion					1047:1055	increased secretion	1037:1055	increased secretion of neuron-derived inflammatory factors demonstrated by ELISA	1037:1116	A Luciferase reporter assay demonstrated that increased SNW1 levels led to increased NF-κB p65 activity and increased secretion of neuron-derived inflammatory factors demonstrated by ELISA.
35818332	2	45	theme	factor	386:391	arg1	p65					399:401	the pro-inflammatory transcription factor NF-κB p65	351:401	the pro-inflammatory transcription factor NF-κB p65	351:401	SNW domain-containing protein 1 (SNW1) is a coactivator of the pro-inflammatory transcription factor NF-κB p65.
35818332	8	46	theme	SNW1	1160:1163	arg1	protein					1165:1171	SNW1 protein	1160:1171	SNW1 protein	1160:1171	Dex reversed the H/R-induced increase of SNW1 protein by upregulating OGT and enhancing O-GlcNAcylation of SNW1.
35818332	9	47	theme	cerebral	1327:1334	arg1	occlusion					1343:1351	middle cerebral artery occlusion	1320:1351	a middle cerebral artery occlusion model in vivo	1318:1365	Dex suppression of the SNW1/NF-κB complex resulted in neuroprotection in vitro and in a middle cerebral artery occlusion model in vivo.
35818332	9	48	theme	artery	1336:1341	arg1	occlusion					1343:1351	middle cerebral artery occlusion	1320:1351	a middle cerebral artery occlusion model in vivo	1318:1365	Dex suppression of the SNW1/NF-κB complex resulted in neuroprotection in vitro and in a middle cerebral artery occlusion model in vivo.
35818332	2	49	theme	transcription	372:384	arg1	factor					386:391	pro-inflammatory transcription factor	355:391	the pro-inflammatory transcription factor NF-κB p65	351:401	SNW domain-containing protein 1 (SNW1) is a coactivator of the pro-inflammatory transcription factor NF-κB p65.
35818332	6	50	theme	protein	875:881	arg1	levels					883:888	SNW1 protein levels	870:888	SNW1 protein levels	870:888	H/R increased SNW1 protein levels but inhibited O-GlcNAcylation of SNW1.
35818332	7	51	theme	neuron-derived	1060:1073	arg1	factors					1088:1094	neuron-derived inflammatory factors	1060:1094	neuron-derived inflammatory factors demonstrated by ELISA	1060:1116	A Luciferase reporter assay demonstrated that increased SNW1 levels led to increased NF-κB p65 activity and increased secretion of neuron-derived inflammatory factors demonstrated by ELISA.
35818332	2	52	theme	pro-inflammatory	355:370	arg1	factor					386:391	pro-inflammatory transcription factor	355:391	the pro-inflammatory transcription factor NF-κB p65	351:401	SNW domain-containing protein 1 (SNW1) is a coactivator of the pro-inflammatory transcription factor NF-κB p65.
35818332	11	53	theme	SNW1	1582:1585	arg1	O-GlcNAcylation					1563:1577	O-GlcNAcylation	1563:1577	O-GlcNAcylation of SNW1	1563:1585	Taken together, these data indicate that Dex inhibits NF-κB-transcriptional activity in neurons undergoing I/R by regulating O-GlcNAcylation of SNW1.
35818332	5	54	from	effects	787:793	arg1	p65					812:814	NF-κB p65	806:814	NF-κB p65	806:814	O-GlcNAc levels in SNW1 and effects of SNW1 on NF-κB p65 were determined by immunoprecipitation.
35818332	2	55	theme	domain-containing	296:312	arg1	SNW1					325:328	SNW1	325:328	SNW1	325:328	SNW domain-containing protein 1 (SNW1) is a coactivator of the pro-inflammatory transcription factor NF-κB p65.
35818332	2	55	theme	domain-containing	296:312	arg1	coactivator					336:346	a coactivator	334:346	a coactivator of the pro-inflammatory transcription factor NF-κB p65	334:401	SNW domain-containing protein 1 (SNW1) is a coactivator of the pro-inflammatory transcription factor NF-κB p65.
35818332	2	55	theme	domain-containing	296:312	arg1	protein					314:320	SNW domain-containing protein 1	292:322	SNW domain-containing protein 1 (SNW1)	292:329	SNW domain-containing protein 1 (SNW1) is a coactivator of the pro-inflammatory transcription factor NF-κB p65.
35818332	7	56	theme	increased	1037:1045	arg1	secretion					1047:1055	increased secretion	1037:1055	increased secretion of neuron-derived inflammatory factors demonstrated by ELISA	1037:1116	A Luciferase reporter assay demonstrated that increased SNW1 levels led to increased NF-κB p65 activity and increased secretion of neuron-derived inflammatory factors demonstrated by ELISA.
35818332	7	57	theme	reporter	942:949	arg1	assay					951:955	A Luciferase reporter assay	929:955	A Luciferase reporter assay	929:955	A Luciferase reporter assay demonstrated that increased SNW1 levels led to increased NF-κB p65 activity and increased secretion of neuron-derived inflammatory factors demonstrated by ELISA.
35818332	4	58	theme	hypoxia/reoxygenation	647:667	arg1	conditions					675:684	hypoxia/reoxygenation (H/R) conditions	647:684	hypoxia/reoxygenation (H/R) conditions	647:684	SH-SY5Y and PC12 cells under hypoxia/reoxygenation (H/R) conditions were treated with Dex and with inhibitors of O-GlcNAc transferase (OGT).
35818332	2	59	theme	SNW	292:294	arg1	SNW1					325:328	SNW1	325:328	SNW1	325:328	SNW domain-containing protein 1 (SNW1) is a coactivator of the pro-inflammatory transcription factor NF-κB p65.
35818332	2	59	theme	SNW	292:294	arg1	coactivator					336:346	a coactivator	334:346	a coactivator of the pro-inflammatory transcription factor NF-κB p65	334:401	SNW domain-containing protein 1 (SNW1) is a coactivator of the pro-inflammatory transcription factor NF-κB p65.
35818332	2	59	theme	SNW	292:294	arg1	protein					314:320	SNW domain-containing protein 1	292:322	SNW domain-containing protein 1 (SNW1)	292:329	SNW domain-containing protein 1 (SNW1) is a coactivator of the pro-inflammatory transcription factor NF-κB p65.
35818332	9	60	theme	Dex	1232:1234	arg1	suppression					1236:1246	Dex suppression	1232:1246	Dex suppression of the SNW1/NF-κB complex	1232:1272	Dex suppression of the SNW1/NF-κB complex resulted in neuroprotection in vitro and in a middle cerebral artery occlusion model in vivo.
35818332	4	61	theme	O-GlcNAc	731:738	arg1	transferase					740:750	O-GlcNAc transferase	731:750	O-GlcNAc transferase (OGT)	731:756	SH-SY5Y and PC12 cells under hypoxia/reoxygenation (H/R) conditions were treated with Dex and with inhibitors of O-GlcNAc transferase (OGT).
35818332	4	61	theme	O-GlcNAc	731:738	arg1	OGT					753:755	OGT	753:755	OGT	753:755	SH-SY5Y and PC12 cells under hypoxia/reoxygenation (H/R) conditions were treated with Dex and with inhibitors of O-GlcNAc transferase (OGT).
35818332	0	62	from	Activity	47:54	arg1	Neurons					59:65	Neurons	59:65	Neurons Undergoing Ischemia-Reperfusion	59:97	Dexmedetomidine Inhibits NF-κB-Transcriptional Activity in Neurons Undergoing Ischemia-Reperfusion by Regulating O-GlcNAcylation of SNW1.
35818332	10	63	theme	OGT	1425:1427	arg1	protein					1429:1435	OGT protein	1425:1435	OGT protein	1425:1435	PKA and ERK1/2 inhibitors abolished the effect of Dex on OGT protein.
33709700	2	0	gly	glycosylates	302:313	arg1	substrates					361:370	more than 1000 unique nuclear and cytoplasmic substrates	315:370	more than 1000 unique nuclear and cytoplasmic substrates	315:370	O-GlcNAc transferase (OGT), the sole enzyme responsible for this modification, glycosylates more than 1000 unique nuclear and cytoplasmic substrates.
33709700	7	1	theme	lumenal	1109:1115	arg1	binding					1117:1123	lumenal binding	1109:1123	lumenal binding	1109:1123	We also found that substrates with glycosylation sites close to the C-terminus bypass lumenal binding.
33709700	4	2	theme	individual	688:697	arg1	substrates					699:708	individual substrates	688:708	individual substrates	688:708	OGT contains a long tetratricopeptide repeat (TPR) domain that has been implicated in substrate selection, but there is almost no information about how changes to this domain affect glycosylation of individual substrates.
33709700	4	3	theme	substrate	575:583	arg1	selection					585:593	substrate selection	575:593	substrate selection	575:593	OGT contains a long tetratricopeptide repeat (TPR) domain that has been implicated in substrate selection, but there is almost no information about how changes to this domain affect glycosylation of individual substrates.
33709700	0	4	theme	Repeat	80:85	arg1	Domain					87:92	O-GlcNAc Transferase's Tetratricopeptide Repeat Domain	39:92	O-GlcNAc Transferase's Tetratricopeptide Repeat Domain	39:92	Protein Substrates Engage the Lumen of O-GlcNAc Transferase's Tetratricopeptide Repeat Domain in Different Ways.
33709700	4	5	theme	repeat	527:532	arg1	domain					540:545	a long tetratricopeptide repeat (TPR) domain	502:545	a long tetratricopeptide repeat (TPR) domain that has been implicated in substrate selection	502:593	OGT contains a long tetratricopeptide repeat (TPR) domain that has been implicated in substrate selection, but there is almost no information about how changes to this domain affect glycosylation of individual substrates.
33709700	8	6	theme	ways	1208:1211	arg1	variety					1187:1193	a variety	1185:1193	a variety of different ways for glycosylation	1185:1229	Our findings demonstrate that substrates can engage OGT in a variety of different ways for glycosylation.
33709700	8	6	theme	ways	1208:1211	arg1	ways					1208:1211	different ways	1198:1211	different ways for glycosylation	1198:1229	Our findings demonstrate that substrates can engage OGT in a variety of different ways for glycosylation.
33709700	7	7	gly	glycosylation	1058:1070	arg2	sites					1072:1076	glycosylation sites	1058:1076	glycosylation sites close to the C-terminus	1058:1100	We also found that substrates with glycosylation sites close to the C-terminus bypass lumenal binding.
33709700	0	8	theme	Different	97:105	arg1	Ways					107:110	Different Ways	97:110	Different Ways	97:110	Protein Substrates Engage the Lumen of O-GlcNAc Transferase's Tetratricopeptide Repeat Domain in Different Ways.
33709700	4	9	theme	tetratricopeptide	509:525	arg1	TPR					535:537	TPR	535:537	TPR	535:537	OGT contains a long tetratricopeptide repeat (TPR) domain that has been implicated in substrate selection, but there is almost no information about how changes to this domain affect glycosylation of individual substrates.
33709700	4	9	theme	tetratricopeptide	509:525	arg1	repeat					527:532	long tetratricopeptide repeat	504:532	a long tetratricopeptide repeat (TPR) domain that has been implicated in substrate selection	502:593	OGT contains a long tetratricopeptide repeat (TPR) domain that has been implicated in substrate selection, but there is almost no information about how changes to this domain affect glycosylation of individual substrates.
33709700	6	10	theme	different	985:993	arg1	regions					995:1001	different regions	985:1001	different regions of OGT's TPR lumen	985:1020	Different substrates are sensitive to changes in different regions of OGT's TPR lumen.
33709700	5	11	theme	substrate	911:919	arg1	glycosylation					921:933	substrate glycosylation	911:933	substrate glycosylation	911:933	By profiling O-GlcNAc in cell extracts and probing glycosylation of purified substrates, we show here that ladders of asparagines and aspartates that extend the full length of OGT's TPR lumen control substrate glycosylation.
33709700	5	12	theme	cell	736:739	arg1	extracts					741:748	cell extracts	736:748	cell extracts	736:748	By profiling O-GlcNAc in cell extracts and probing glycosylation of purified substrates, we show here that ladders of asparagines and aspartates that extend the full length of OGT's TPR lumen control substrate glycosylation.
33709700	5	13	theme	TPR	893:895	arg1	lumen					897:901	OGT's TPR lumen	887:901	OGT's TPR lumen	887:901	By profiling O-GlcNAc in cell extracts and probing glycosylation of purified substrates, we show here that ladders of asparagines and aspartates that extend the full length of OGT's TPR lumen control substrate glycosylation.
33709700	5	14	theme	asparagines	829:839	arg1	ladders					818:824	ladders	818:824	ladders of asparagines and aspartates that extend the full length of OGT's TPR lumen	818:901	By profiling O-GlcNAc in cell extracts and probing glycosylation of purified substrates, we show here that ladders of asparagines and aspartates that extend the full length of OGT's TPR lumen control substrate glycosylation.
33709700	1	15	theme	essential	169:177	arg1	modification					198:209	an essential post-translational modification	166:209	an essential post-translational modification in mammals	166:220	Glycosylation of nuclear and cytoplasmic proteins is an essential post-translational modification in mammals.
33709700	1	15	theme	essential	169:177	arg1	Glycosylation					113:125	Glycosylation	113:125	Glycosylation of nuclear and cytoplasmic proteins	113:161	Glycosylation of nuclear and cytoplasmic proteins is an essential post-translational modification in mammals.
33709700	0	16	theme	O-GlcNAc	39:46	arg1	Transferase					48:58	O-GlcNAc Transferase	39:58	O-GlcNAc Transferase's Tetratricopeptide Repeat Domain	39:92	Protein Substrates Engage the Lumen of O-GlcNAc Transferase's Tetratricopeptide Repeat Domain in Different Ways.
33709700	8	17	theme	different	1198:1206	arg1	ways					1208:1211	different ways	1198:1211	different ways for glycosylation	1198:1229	Our findings demonstrate that substrates can engage OGT in a variety of different ways for glycosylation.
33709700	7	18	theme	glycosylation	1058:1070	arg1	sites					1072:1076	glycosylation sites	1058:1076	glycosylation sites close to the C-terminus	1058:1100	We also found that substrates with glycosylation sites close to the C-terminus bypass lumenal binding.
33709700	5	19	gly	glycosylation	762:774	arg1	substrates					788:797	purified substrates	779:797	purified substrates	779:797	By profiling O-GlcNAc in cell extracts and probing glycosylation of purified substrates, we show here that ladders of asparagines and aspartates that extend the full length of OGT's TPR lumen control substrate glycosylation.
33709700	1	20	theme	post-translational	179:196	arg1	modification					198:209	an essential post-translational modification	166:209	an essential post-translational modification in mammals	166:220	Glycosylation of nuclear and cytoplasmic proteins is an essential post-translational modification in mammals.
33709700	1	20	theme	post-translational	179:196	arg1	Glycosylation					113:125	Glycosylation	113:125	Glycosylation of nuclear and cytoplasmic proteins	113:161	Glycosylation of nuclear and cytoplasmic proteins is an essential post-translational modification in mammals.
33709700	0	21	from	Lumen	30:34	arg1	Ways					107:110	Different Ways	97:110	Different Ways	97:110	Protein Substrates Engage the Lumen of O-GlcNAc Transferase's Tetratricopeptide Repeat Domain in Different Ways.
33709700	0	22	theme	Protein	0:6	arg1	Substrates					8:17	Protein Substrates	0:17	Protein Substrates	0:17	Protein Substrates Engage the Lumen of O-GlcNAc Transferase's Tetratricopeptide Repeat Domain in Different Ways.
33709700	5	23	theme	full	872:875	arg1	length					877:882	the full length	868:882	the full length of OGT's TPR lumen	868:901	By profiling O-GlcNAc in cell extracts and probing glycosylation of purified substrates, we show here that ladders of asparagines and aspartates that extend the full length of OGT's TPR lumen control substrate glycosylation.
33709700	1	24	gly	Glycosylation	113:125	arg1	proteins					154:161	nuclear and cytoplasmic proteins	130:161	nuclear and cytoplasmic proteins	130:161	Glycosylation of nuclear and cytoplasmic proteins is an essential post-translational modification in mammals.
33709700	3	25	theme	unusual	472:478	arg1	biology					480:486	OGT's unusual biology	466:486	OGT's unusual biology	466:486	How OGT selects its substrates is a fundamental question that must be answered to understand OGT's unusual biology.
33709700	5	26	theme	purified	779:786	arg1	substrates					788:797	purified substrates	779:797	purified substrates	779:797	By profiling O-GlcNAc in cell extracts and probing glycosylation of purified substrates, we show here that ladders of asparagines and aspartates that extend the full length of OGT's TPR lumen control substrate glycosylation.
33709700	4	27	theme	substrates	699:708	arg1	glycosylation					671:683	glycosylation	671:683	glycosylation of individual substrates	671:708	OGT contains a long tetratricopeptide repeat (TPR) domain that has been implicated in substrate selection, but there is almost no information about how changes to this domain affect glycosylation of individual substrates.
33709700	6	28	from	changes	974:980	arg1	regions					995:1001	different regions	985:1001	different regions of OGT's TPR lumen	985:1020	Different substrates are sensitive to changes in different regions of OGT's TPR lumen.
33709700	5	29	theme	substrates	788:797	arg1	glycosylation					762:774	glycosylation	762:774	glycosylation of purified substrates	762:797	By profiling O-GlcNAc in cell extracts and probing glycosylation of purified substrates, we show here that ladders of asparagines and aspartates that extend the full length of OGT's TPR lumen control substrate glycosylation.
33709700	5	30	from	O-GlcNAc	724:731	arg1	extracts					741:748	cell extracts	736:748	cell extracts	736:748	By profiling O-GlcNAc in cell extracts and probing glycosylation of purified substrates, we show here that ladders of asparagines and aspartates that extend the full length of OGT's TPR lumen control substrate glycosylation.
33709700	5	31	theme	lumen	897:901	arg1	length					877:882	the full length	868:882	the full length of OGT's TPR lumen	868:901	By profiling O-GlcNAc in cell extracts and probing glycosylation of purified substrates, we show here that ladders of asparagines and aspartates that extend the full length of OGT's TPR lumen control substrate glycosylation.
33709700	5	32	theme	aspartates	845:854	arg1	ladders					818:824	ladders	818:824	ladders of asparagines and aspartates that extend the full length of OGT's TPR lumen	818:901	By profiling O-GlcNAc in cell extracts and probing glycosylation of purified substrates, we show here that ladders of asparagines and aspartates that extend the full length of OGT's TPR lumen control substrate glycosylation.
33709700	6	33	theme	Different	936:944	arg1	substrates					946:955	Different substrates	936:955	Different substrates	936:955	Different substrates are sensitive to changes in different regions of OGT's TPR lumen.
33709700	2	34	theme	cytoplasmic	349:359	arg1	substrates					361:370	more than 1000 unique nuclear and cytoplasmic substrates	315:370	more than 1000 unique nuclear and cytoplasmic substrates	315:370	O-GlcNAc transferase (OGT), the sole enzyme responsible for this modification, glycosylates more than 1000 unique nuclear and cytoplasmic substrates.
33709700	3	35	theme	fundamental	409:419	arg1	question					421:428	a fundamental question	407:428	a fundamental question that must be answered to understand OGT's unusual biology	407:486	How OGT selects its substrates is a fundamental question that must be answered to understand OGT's unusual biology.
33709700	4	36	gly	glycosylation	671:683	arg1	substrates					699:708	individual substrates	688:708	individual substrates	688:708	OGT contains a long tetratricopeptide repeat (TPR) domain that has been implicated in substrate selection, but there is almost no information about how changes to this domain affect glycosylation of individual substrates.
33709700	4	37	contain	contains	493:500	arg1	OGT					489:491	OGT	489:491	OGT	489:491	OGT contains a long tetratricopeptide repeat (TPR) domain that has been implicated in substrate selection, but there is almost no information about how changes to this domain affect glycosylation of individual substrates.
33709700	4	37	contain	contains	493:500	arg2	domain					540:545	a long tetratricopeptide repeat (TPR) domain	502:545	a long tetratricopeptide repeat (TPR) domain that has been implicated in substrate selection	502:593	OGT contains a long tetratricopeptide repeat (TPR) domain that has been implicated in substrate selection, but there is almost no information about how changes to this domain affect glycosylation of individual substrates.
33709700	2	38	theme	O-GlcNAc	223:230	arg1	enzyme					260:265	the sole enzyme	251:265	the sole enzyme responsible for this modification	251:299	O-GlcNAc transferase (OGT), the sole enzyme responsible for this modification, glycosylates more than 1000 unique nuclear and cytoplasmic substrates.
33709700	2	38	theme	O-GlcNAc	223:230	arg1	OGT					245:247	OGT	245:247	OGT	245:247	O-GlcNAc transferase (OGT), the sole enzyme responsible for this modification, glycosylates more than 1000 unique nuclear and cytoplasmic substrates.
33709700	2	38	theme	O-GlcNAc	223:230	arg1	transferase					232:242	O-GlcNAc transferase	223:242	O-GlcNAc transferase (OGT)	223:248	O-GlcNAc transferase (OGT), the sole enzyme responsible for this modification, glycosylates more than 1000 unique nuclear and cytoplasmic substrates.
33709700	2	39	theme	responsible	267:277	arg1	enzyme					260:265	the sole enzyme	251:265	the sole enzyme responsible for this modification	251:299	O-GlcNAc transferase (OGT), the sole enzyme responsible for this modification, glycosylates more than 1000 unique nuclear and cytoplasmic substrates.
33709700	2	39	theme	responsible	267:277	arg1	transferase					232:242	O-GlcNAc transferase	223:242	O-GlcNAc transferase (OGT)	223:248	O-GlcNAc transferase (OGT), the sole enzyme responsible for this modification, glycosylates more than 1000 unique nuclear and cytoplasmic substrates.
33709700	6	40	theme	TPR	1012:1014	arg1	lumen					1016:1020	OGT's TPR lumen	1006:1020	OGT's TPR lumen	1006:1020	Different substrates are sensitive to changes in different regions of OGT's TPR lumen.
33709700	1	41	theme	nuclear	130:136	arg1	proteins					154:161	nuclear and cytoplasmic proteins	130:161	nuclear and cytoplasmic proteins	130:161	Glycosylation of nuclear and cytoplasmic proteins is an essential post-translational modification in mammals.
33709700	6	42	theme	lumen	1016:1020	arg1	regions					995:1001	different regions	985:1001	different regions of OGT's TPR lumen	985:1020	Different substrates are sensitive to changes in different regions of OGT's TPR lumen.
33709700	1	43	from	modification	198:209	arg1	mammals					214:220	mammals	214:220	mammals	214:220	Glycosylation of nuclear and cytoplasmic proteins is an essential post-translational modification in mammals.
33709700	2	44	theme	unique	330:335	arg1	substrates					361:370	more than 1000 unique nuclear and cytoplasmic substrates	315:370	more than 1000 unique nuclear and cytoplasmic substrates	315:370	O-GlcNAc transferase (OGT), the sole enzyme responsible for this modification, glycosylates more than 1000 unique nuclear and cytoplasmic substrates.
33709700	2	45	theme	nuclear	337:343	arg1	substrates					361:370	more than 1000 unique nuclear and cytoplasmic substrates	315:370	more than 1000 unique nuclear and cytoplasmic substrates	315:370	O-GlcNAc transferase (OGT), the sole enzyme responsible for this modification, glycosylates more than 1000 unique nuclear and cytoplasmic substrates.
33709700	0	46	theme	Tetratricopeptide	62:78	arg1	Domain					87:92	O-GlcNAc Transferase's Tetratricopeptide Repeat Domain	39:92	O-GlcNAc Transferase's Tetratricopeptide Repeat Domain	39:92	Protein Substrates Engage the Lumen of O-GlcNAc Transferase's Tetratricopeptide Repeat Domain in Different Ways.
33709700	2	47	theme	sole	255:258	arg1	enzyme					260:265	the sole enzyme	251:265	the sole enzyme responsible for this modification	251:299	O-GlcNAc transferase (OGT), the sole enzyme responsible for this modification, glycosylates more than 1000 unique nuclear and cytoplasmic substrates.
33709700	2	47	theme	sole	255:258	arg1	transferase					232:242	O-GlcNAc transferase	223:242	O-GlcNAc transferase (OGT)	223:248	O-GlcNAc transferase (OGT), the sole enzyme responsible for this modification, glycosylates more than 1000 unique nuclear and cytoplasmic substrates.
33709700	1	48	theme	cytoplasmic	142:152	arg1	proteins					154:161	nuclear and cytoplasmic proteins	130:161	nuclear and cytoplasmic proteins	130:161	Glycosylation of nuclear and cytoplasmic proteins is an essential post-translational modification in mammals.
33709700	7	49	with	substrates	1042:1051	arg1	sites					1072:1076	glycosylation sites	1058:1076	glycosylation sites close to the C-terminus	1058:1100	We also found that substrates with glycosylation sites close to the C-terminus bypass lumenal binding.
33709700	4	50	theme	long	504:507	arg1	TPR					535:537	TPR	535:537	TPR	535:537	OGT contains a long tetratricopeptide repeat (TPR) domain that has been implicated in substrate selection, but there is almost no information about how changes to this domain affect glycosylation of individual substrates.
33709700	4	50	theme	long	504:507	arg1	repeat					527:532	long tetratricopeptide repeat	504:532	a long tetratricopeptide repeat (TPR) domain that has been implicated in substrate selection	502:593	OGT contains a long tetratricopeptide repeat (TPR) domain that has been implicated in substrate selection, but there is almost no information about how changes to this domain affect glycosylation of individual substrates.
33709700	1	51	theme	proteins	154:161	arg1	modification					198:209	an essential post-translational modification	166:209	an essential post-translational modification in mammals	166:220	Glycosylation of nuclear and cytoplasmic proteins is an essential post-translational modification in mammals.
33709700	1	51	theme	proteins	154:161	arg1	Glycosylation					113:125	Glycosylation	113:125	Glycosylation of nuclear and cytoplasmic proteins	113:161	Glycosylation of nuclear and cytoplasmic proteins is an essential post-translational modification in mammals.
18818698	4	0	theme	GT-B	715:718	arg1	fold					720:723	the (metal-independent) GT-B fold	691:723	the (metal-independent) GT-B fold	691:723	Here, we show, by X-ray crystallography and mutagenesis, that OGT adopts the (metal-independent) GT-B fold and binds a UDP-GlcNAc analogue at the bottom of a highly conserved putative peptide-binding groove, covered by a mobile loop.
18818698	2	1	theme	single	382:387	arg1	genes					401:405	single, essential, genes	382:405	single, essential, genes in metazoan genomes	382:425	O-GlcNAcylation is regulated by O-GlcNAc transferase (OGT) and O-GlcNAcase, both encoded by single, essential, genes in metazoan genomes.
18818698	5	2	theme	continuous	949:958	arg1	surface					987:993	a continuous 120 A putative interaction surface	947:993	a continuous 120 A putative interaction surface	947:993	Strikingly, the tetratricopeptide repeats (TPRs) tightly interact with the active site to form a continuous 120 A putative interaction surface, whereas the previously predicted phosphatidylinositide-binding site locates to the opposite end of the catalytic domain.
18818698	5	3	theme	catalytic	1099:1107	arg1	domain					1109:1114	the catalytic domain	1095:1114	the catalytic domain	1095:1114	Strikingly, the tetratricopeptide repeats (TPRs) tightly interact with the active site to form a continuous 120 A putative interaction surface, whereas the previously predicted phosphatidylinositide-binding site locates to the opposite end of the catalytic domain.
18818698	2	4	dep	single	382:387	arg1	essential					390:398	essential	390:398	essential	390:398	O-GlcNAcylation is regulated by O-GlcNAc transferase (OGT) and O-GlcNAcase, both encoded by single, essential, genes in metazoan genomes.
18818698	5	5	theme	domain	1109:1114	arg1	end					1088:1090	the opposite end	1075:1090	the opposite end of the catalytic domain	1075:1114	Strikingly, the tetratricopeptide repeats (TPRs) tightly interact with the active site to form a continuous 120 A putative interaction surface, whereas the previously predicted phosphatidylinositide-binding site locates to the opposite end of the catalytic domain.
18818698	6	6	theme	first	1274:1278	arg1	insights					1280:1287	first insights	1274:1287	first insights into how OGT may recognise its substrates	1274:1329	On the basis of the structure, we identify truncation/point mutants of the TPRs that have differential effects on activity towards proteins/peptides, giving first insights into how OGT may recognise its substrates.
18818698	4	7	from	bottom	764:769	arg1	analogue					748:755	a UDP-GlcNAc analogue	735:755	a UDP-GlcNAc analogue	735:755	Here, we show, by X-ray crystallography and mutagenesis, that OGT adopts the (metal-independent) GT-B fold and binds a UDP-GlcNAc analogue at the bottom of a highly conserved putative peptide-binding groove, covered by a mobile loop.
18818698	1	8	theme	Post-translational	76:93	arg1	modification					95:106	Post-translational modification	76:106	Post-translational modification of protein serines/threonines with N-acetylglucosamine (O-GlcNAc)	76:172	Post-translational modification of protein serines/threonines with N-acetylglucosamine (O-GlcNAc) is dynamic, inducible and abundant, regulating many cellular processes by interfering with protein phosphorylation.
18818698	5	9	theme	tetratricopeptide	868:884	arg1	TPRs					895:898	TPRs	895:898	TPRs	895:898	Strikingly, the tetratricopeptide repeats (TPRs) tightly interact with the active site to form a continuous 120 A putative interaction surface, whereas the previously predicted phosphatidylinositide-binding site locates to the opposite end of the catalytic domain.
18818698	5	9	theme	tetratricopeptide	868:884	arg1	repeats					886:892	the tetratricopeptide repeats	864:892	the tetratricopeptide repeats (TPRs)	864:899	Strikingly, the tetratricopeptide repeats (TPRs) tightly interact with the active site to form a continuous 120 A putative interaction surface, whereas the previously predicted phosphatidylinositide-binding site locates to the opposite end of the catalytic domain.
18818698	4	10	theme	mobile	839:844	arg1	loop					846:849	a mobile loop	837:849	a mobile loop	837:849	Here, we show, by X-ray crystallography and mutagenesis, that OGT adopts the (metal-independent) GT-B fold and binds a UDP-GlcNAc analogue at the bottom of a highly conserved putative peptide-binding groove, covered by a mobile loop.
18818698	5	11	theme	putative	966:973	arg1	surface					987:993	a continuous 120 A putative interaction surface	947:993	a continuous 120 A putative interaction surface	947:993	Strikingly, the tetratricopeptide repeats (TPRs) tightly interact with the active site to form a continuous 120 A putative interaction surface, whereas the previously predicted phosphatidylinositide-binding site locates to the opposite end of the catalytic domain.
18818698	2	12	theme	metazoan	410:417	arg1	genomes					419:425	metazoan genomes	410:425	metazoan genomes	410:425	O-GlcNAcylation is regulated by O-GlcNAc transferase (OGT) and O-GlcNAcase, both encoded by single, essential, genes in metazoan genomes.
18818698	3	13	theme	protein	598:604	arg1	substrates					606:615	specific cellular protein substrates	580:615	specific cellular protein substrates	580:615	It is not understood how OGT recognises its sugar nucleotide donor and performs O-GlcNAc transfer onto proteins/peptides, and how the enzyme recognises specific cellular protein substrates.
18818698	2	14	dep	regulated	309:317	arg1	both					366:369	both	366:369	both	366:369	O-GlcNAcylation is regulated by O-GlcNAc transferase (OGT) and O-GlcNAcase, both encoded by single, essential, genes in metazoan genomes.
18818698	0	15	theme	Structural	0:9	arg1	insights					11:18	Structural insights	0:18	Structural insights into mechanism and specificity of O-GlcNAc transferase	0:73	Structural insights into mechanism and specificity of O-GlcNAc transferase.
18818698	1	16	theme	protein	111:117	arg1	serines/threonines					119:136	protein serines/threonines	111:136	protein serines/threonines	111:136	Post-translational modification of protein serines/threonines with N-acetylglucosamine (O-GlcNAc) is dynamic, inducible and abundant, regulating many cellular processes by interfering with protein phosphorylation.
18818698	3	17	theme	specific	580:587	arg1	substrates					606:615	specific cellular protein substrates	580:615	specific cellular protein substrates	580:615	It is not understood how OGT recognises its sugar nucleotide donor and performs O-GlcNAc transfer onto proteins/peptides, and how the enzyme recognises specific cellular protein substrates.
18818698	1	18	theme	many	221:224	arg1	processes					235:243	many cellular processes	221:243	many cellular processes	221:243	Post-translational modification of protein serines/threonines with N-acetylglucosamine (O-GlcNAc) is dynamic, inducible and abundant, regulating many cellular processes by interfering with protein phosphorylation.
18818698	4	19	theme	UDP-GlcNAc	737:746	arg1	analogue					748:755	a UDP-GlcNAc analogue	735:755	a UDP-GlcNAc analogue	735:755	Here, we show, by X-ray crystallography and mutagenesis, that OGT adopts the (metal-independent) GT-B fold and binds a UDP-GlcNAc analogue at the bottom of a highly conserved putative peptide-binding groove, covered by a mobile loop.
18818698	2	20	theme	O-GlcNAc	322:329	arg1	transferase					331:341	O-GlcNAc transferase	322:341	O-GlcNAc transferase (OGT)	322:347	O-GlcNAcylation is regulated by O-GlcNAc transferase (OGT) and O-GlcNAcase, both encoded by single, essential, genes in metazoan genomes.
18818698	2	20	theme	O-GlcNAc	322:329	arg1	OGT					344:346	OGT	344:346	OGT	344:346	O-GlcNAcylation is regulated by O-GlcNAc transferase (OGT) and O-GlcNAcase, both encoded by single, essential, genes in metazoan genomes.
18818698	5	21	theme	opposite	1079:1086	arg1	end					1088:1090	the opposite end	1075:1090	the opposite end of the catalytic domain	1075:1114	Strikingly, the tetratricopeptide repeats (TPRs) tightly interact with the active site to form a continuous 120 A putative interaction surface, whereas the previously predicted phosphatidylinositide-binding site locates to the opposite end of the catalytic domain.
18818698	3	22	theme	cellular	589:596	arg1	substrates					606:615	specific cellular protein substrates	580:615	specific cellular protein substrates	580:615	It is not understood how OGT recognises its sugar nucleotide donor and performs O-GlcNAc transfer onto proteins/peptides, and how the enzyme recognises specific cellular protein substrates.
18818698	1	23	theme	cellular	226:233	arg1	processes					235:243	many cellular processes	221:243	many cellular processes	221:243	Post-translational modification of protein serines/threonines with N-acetylglucosamine (O-GlcNAc) is dynamic, inducible and abundant, regulating many cellular processes by interfering with protein phosphorylation.
18818698	3	24	dep	understood	438:447	arg1	recognises					569:578	recognises	569:578	recognises specific cellular protein substrates	569:615	It is not understood how OGT recognises its sugar nucleotide donor and performs O-GlcNAc transfer onto proteins/peptides, and how the enzyme recognises specific cellular protein substrates.
18818698	3	24	dep	understood	438:447	arg1	recognises					457:466	recognises	457:466	recognises its sugar nucleotide donor	457:493	It is not understood how OGT recognises its sugar nucleotide donor and performs O-GlcNAc transfer onto proteins/peptides, and how the enzyme recognises specific cellular protein substrates.
18818698	3	24	dep	understood	438:447	arg1	performs					499:506	performs	499:506	performs O-GlcNAc transfer onto proteins/peptides	499:547	It is not understood how OGT recognises its sugar nucleotide donor and performs O-GlcNAc transfer onto proteins/peptides, and how the enzyme recognises specific cellular protein substrates.
18818698	1	25	with	modification	95:106	arg1	O-GlcNAc					164:171	O-GlcNAc	164:171	O-GlcNAc	164:171	Post-translational modification of protein serines/threonines with N-acetylglucosamine (O-GlcNAc) is dynamic, inducible and abundant, regulating many cellular processes by interfering with protein phosphorylation.
18818698	1	25	with	modification	95:106	arg1	N-acetylglucosamine					143:161	N-acetylglucosamine	143:161	N-acetylglucosamine (O-GlcNAc)	143:172	Post-translational modification of protein serines/threonines with N-acetylglucosamine (O-GlcNAc) is dynamic, inducible and abundant, regulating many cellular processes by interfering with protein phosphorylation.
18818698	5	26	dep	interact	909:916	arg1	whereas					996:1002	whereas	996:1002	whereas	996:1002	Strikingly, the tetratricopeptide repeats (TPRs) tightly interact with the active site to form a continuous 120 A putative interaction surface, whereas the previously predicted phosphatidylinositide-binding site locates to the opposite end of the catalytic domain.
18818698	4	27	theme	X-ray	636:640	arg1	crystallography					642:656	X-ray crystallography	636:656	X-ray crystallography	636:656	Here, we show, by X-ray crystallography and mutagenesis, that OGT adopts the (metal-independent) GT-B fold and binds a UDP-GlcNAc analogue at the bottom of a highly conserved putative peptide-binding groove, covered by a mobile loop.
18818698	3	28	theme	sugar	472:476	arg1	donor					489:493	its sugar nucleotide donor	468:493	its sugar nucleotide donor	468:493	It is not understood how OGT recognises its sugar nucleotide donor and performs O-GlcNAc transfer onto proteins/peptides, and how the enzyme recognises specific cellular protein substrates.
18818698	0	29	theme	O-GlcNAc	54:61	arg1	transferase					63:73	O-GlcNAc transferase	54:73	O-GlcNAc transferase	54:73	Structural insights into mechanism and specificity of O-GlcNAc transferase.
18818698	5	30	theme	predicted	1019:1027	arg1	site					1059:1062	the previously predicted phosphatidylinositide-binding site	1004:1062	the previously predicted phosphatidylinositide-binding site	1004:1062	Strikingly, the tetratricopeptide repeats (TPRs) tightly interact with the active site to form a continuous 120 A putative interaction surface, whereas the previously predicted phosphatidylinositide-binding site locates to the opposite end of the catalytic domain.
18818698	2	31	from	genes	401:405	arg1	genomes					419:425	metazoan genomes	410:425	metazoan genomes	410:425	O-GlcNAcylation is regulated by O-GlcNAc transferase (OGT) and O-GlcNAcase, both encoded by single, essential, genes in metazoan genomes.
18818698	3	32	theme	O-GlcNAc	508:515	arg1	transfer					517:524	O-GlcNAc transfer	508:524	O-GlcNAc transfer onto proteins/peptides	508:547	It is not understood how OGT recognises its sugar nucleotide donor and performs O-GlcNAc transfer onto proteins/peptides, and how the enzyme recognises specific cellular protein substrates.
18818698	6	33	contain	have	1202:1205	arg1	TPRs					1192:1195	the TPRs	1188:1195	the TPRs that have differential effects on activity towards proteins/peptides	1188:1264	On the basis of the structure, we identify truncation/point mutants of the TPRs that have differential effects on activity towards proteins/peptides, giving first insights into how OGT may recognise its substrates.
18818698	6	33	contain	have	1202:1205	arg2	effects					1220:1226	differential effects	1207:1226	differential effects	1207:1226	On the basis of the structure, we identify truncation/point mutants of the TPRs that have differential effects on activity towards proteins/peptides, giving first insights into how OGT may recognise its substrates.
18818698	5	34	theme	phosphatidylinositide-binding	1029:1057	arg1	site					1059:1062	the previously predicted phosphatidylinositide-binding site	1004:1062	the previously predicted phosphatidylinositide-binding site	1004:1062	Strikingly, the tetratricopeptide repeats (TPRs) tightly interact with the active site to form a continuous 120 A putative interaction surface, whereas the previously predicted phosphatidylinositide-binding site locates to the opposite end of the catalytic domain.
18818698	6	35	theme	TPRs	1192:1195	arg1	mutants					1177:1183	truncation/point mutants	1160:1183	truncation/point mutants of the TPRs that have differential effects on activity towards proteins/peptides	1160:1264	On the basis of the structure, we identify truncation/point mutants of the TPRs that have differential effects on activity towards proteins/peptides, giving first insights into how OGT may recognise its substrates.
18818698	5	36	theme	interaction	975:985	arg1	surface					987:993	a continuous 120 A putative interaction surface	947:993	a continuous 120 A putative interaction surface	947:993	Strikingly, the tetratricopeptide repeats (TPRs) tightly interact with the active site to form a continuous 120 A putative interaction surface, whereas the previously predicted phosphatidylinositide-binding site locates to the opposite end of the catalytic domain.
18818698	4	37	theme	putative	793:800	arg1	groove					818:823	a highly conserved putative peptide-binding groove	774:823	a highly conserved putative peptide-binding groove	774:823	Here, we show, by X-ray crystallography and mutagenesis, that OGT adopts the (metal-independent) GT-B fold and binds a UDP-GlcNAc analogue at the bottom of a highly conserved putative peptide-binding groove, covered by a mobile loop.
18818698	1	38	theme	serines/threonines	119:136	arg1	modification					95:106	Post-translational modification	76:106	Post-translational modification of protein serines/threonines with N-acetylglucosamine (O-GlcNAc)	76:172	Post-translational modification of protein serines/threonines with N-acetylglucosamine (O-GlcNAc) is dynamic, inducible and abundant, regulating many cellular processes by interfering with protein phosphorylation.
18818698	6	39	theme	truncation/point	1160:1175	arg1	mutants					1177:1183	truncation/point mutants	1160:1183	truncation/point mutants of the TPRs that have differential effects on activity towards proteins/peptides	1160:1264	On the basis of the structure, we identify truncation/point mutants of the TPRs that have differential effects on activity towards proteins/peptides, giving first insights into how OGT may recognise its substrates.
18818698	4	40	theme	conserved	783:791	arg1	groove					818:823	a highly conserved putative peptide-binding groove	774:823	a highly conserved putative peptide-binding groove	774:823	Here, we show, by X-ray crystallography and mutagenesis, that OGT adopts the (metal-independent) GT-B fold and binds a UDP-GlcNAc analogue at the bottom of a highly conserved putative peptide-binding groove, covered by a mobile loop.
18818698	5	41	theme	active	927:932	arg1	site					934:937	the active site	923:937	the active site	923:937	Strikingly, the tetratricopeptide repeats (TPRs) tightly interact with the active site to form a continuous 120 A putative interaction surface, whereas the previously predicted phosphatidylinositide-binding site locates to the opposite end of the catalytic domain.
18818698	5	42	theme	A	964:964	arg1	surface					987:993	a continuous 120 A putative interaction surface	947:993	a continuous 120 A putative interaction surface	947:993	Strikingly, the tetratricopeptide repeats (TPRs) tightly interact with the active site to form a continuous 120 A putative interaction surface, whereas the previously predicted phosphatidylinositide-binding site locates to the opposite end of the catalytic domain.
18818698	4	43	theme	groove	818:823	arg1	bottom					764:769	the bottom	760:769	the bottom of a highly conserved putative peptide-binding groove	760:823	Here, we show, by X-ray crystallography and mutagenesis, that OGT adopts the (metal-independent) GT-B fold and binds a UDP-GlcNAc analogue at the bottom of a highly conserved putative peptide-binding groove, covered by a mobile loop.
18818698	3	44	theme	nucleotide	478:487	arg1	donor					489:493	its sugar nucleotide donor	468:493	its sugar nucleotide donor	468:493	It is not understood how OGT recognises its sugar nucleotide donor and performs O-GlcNAc transfer onto proteins/peptides, and how the enzyme recognises specific cellular protein substrates.
18818698	4	45	theme	metal-independent	696:712	arg1	fold					720:723	the (metal-independent) GT-B fold	691:723	the (metal-independent) GT-B fold	691:723	Here, we show, by X-ray crystallography and mutagenesis, that OGT adopts the (metal-independent) GT-B fold and binds a UDP-GlcNAc analogue at the bottom of a highly conserved putative peptide-binding groove, covered by a mobile loop.
18818698	6	46	dep	structure	1137:1145	arg1	basis					1124:1128	basis	1124:1128	basis	1124:1128	On the basis of the structure, we identify truncation/point mutants of the TPRs that have differential effects on activity towards proteins/peptides, giving first insights into how OGT may recognise its substrates.
18818698	6	46	dep	structure	1137:1145	arg1	the					1120:1122	the	1120:1122	the	1120:1122	On the basis of the structure, we identify truncation/point mutants of the TPRs that have differential effects on activity towards proteins/peptides, giving first insights into how OGT may recognise its substrates.
18818698	1	47	theme	protein	265:271	arg1	phosphorylation					273:287	protein phosphorylation	265:287	protein phosphorylation	265:287	Post-translational modification of protein serines/threonines with N-acetylglucosamine (O-GlcNAc) is dynamic, inducible and abundant, regulating many cellular processes by interfering with protein phosphorylation.
18818698	0	48	theme	transferase	63:73	arg1	specificity					39:49	specificity	39:49	specificity	39:49	Structural insights into mechanism and specificity of O-GlcNAc transferase.
18818698	0	48	theme	transferase	63:73	arg1	mechanism					25:33	mechanism	25:33	mechanism	25:33	Structural insights into mechanism and specificity of O-GlcNAc transferase.
18818698	4	49	theme	peptide-binding	802:816	arg1	groove					818:823	a highly conserved putative peptide-binding groove	774:823	a highly conserved putative peptide-binding groove	774:823	Here, we show, by X-ray crystallography and mutagenesis, that OGT adopts the (metal-independent) GT-B fold and binds a UDP-GlcNAc analogue at the bottom of a highly conserved putative peptide-binding groove, covered by a mobile loop.
18818698	6	50	theme	differential	1207:1218	arg1	effects					1220:1226	differential effects	1207:1226	differential effects	1207:1226	On the basis of the structure, we identify truncation/point mutants of the TPRs that have differential effects on activity towards proteins/peptides, giving first insights into how OGT may recognise its substrates.
30093632	5	0	theme	CRC	769:771	arg1	patients					773:780	The CRC patients	765:780	The CRC patients with higher levels of O-GlcNAcylation	765:818	The CRC patients with higher levels of O-GlcNAcylation exhibited greater lymph node metastasis potential and lower overall survival.
30093632	5	1	theme	node	844:847	arg1	potential					860:868	greater lymph node metastasis potential	830:868	greater lymph node metastasis potential	830:868	The CRC patients with higher levels of O-GlcNAcylation exhibited greater lymph node metastasis potential and lower overall survival.
30093632	1	2	theme	deadliest	160:168	arg1	cancers					170:176	the deadliest cancers	156:176	the deadliest cancers	156:176	Advanced colorectal cancer (CRC) is one of the deadliest cancers, and the 5-year survival rate of patients with metastasis is extremely low.
30093632	7	3	from	modification	1109:1120	arg1	region					1146:1151	the miR-101 promoter region	1125:1151	the miR-101 promoter region	1125:1151	In addition, O-GlcNAcylation and H3K27me3 modification in the miR-101 promoter region further inhibited the transcription of miR-101, resulting in the upregulation of OGT and EZH2 in metastatic CRC, thus forming a vicious cycle.
30093632	7	4	theme	miR-101	1129:1135	arg1	region					1146:1151	the miR-101 promoter region	1125:1151	the miR-101 promoter region	1125:1151	In addition, O-GlcNAcylation and H3K27me3 modification in the miR-101 promoter region further inhibited the transcription of miR-101, resulting in the upregulation of OGT and EZH2 in metastatic CRC, thus forming a vicious cycle.
30093632	7	5	theme	miR-101	1192:1198	arg1	transcription					1175:1187	the transcription	1171:1187	the transcription of miR-101	1171:1198	In addition, O-GlcNAcylation and H3K27me3 modification in the miR-101 promoter region further inhibited the transcription of miR-101, resulting in the upregulation of OGT and EZH2 in metastatic CRC, thus forming a vicious cycle.
30093632	1	6	theme	cancers	170:176	arg1	one					149:151	one	149:151	one	149:151	Advanced colorectal cancer (CRC) is one of the deadliest cancers, and the 5-year survival rate of patients with metastasis is extremely low.
30093632	1	6	theme	cancers	170:176	arg1	cancers					170:176	the deadliest cancers	156:176	the deadliest cancers	156:176	Advanced colorectal cancer (CRC) is one of the deadliest cancers, and the 5-year survival rate of patients with metastasis is extremely low.
30093632	7	7	theme	metastatic	1250:1259	arg1	CRC					1261:1263	metastatic CRC	1250:1263	metastatic CRC	1250:1263	In addition, O-GlcNAcylation and H3K27me3 modification in the miR-101 promoter region further inhibited the transcription of miR-101, resulting in the upregulation of OGT and EZH2 in metastatic CRC, thus forming a vicious cycle.
30093632	5	8	with	patients	773:780	arg1	levels					794:799	higher levels	787:799	higher levels of O-GlcNAcylation	787:818	The CRC patients with higher levels of O-GlcNAcylation exhibited greater lymph node metastasis potential and lower overall survival.
30093632	8	9	theme	CRC	1412:1414	arg1	metastasis					1416:1425	CRC metastasis	1412:1425	CRC metastasis	1412:1425	In this study, we demonstrated that O-GlcNAcylation, which is negatively regulated by microRNA-101, likely promotes CRC metastasis by enhancing EZH2 protein stability and function.
30093632	6	10	theme	luciferase	925:934	arg1	assays					945:950	luciferase reporter assays	925:950	luciferase reporter assays	925:950	Bioinformatic analysis and luciferase reporter assays revealed that both O-GlcNAcylation transferase (OGT) and EZH2 are posttranscriptionally inhibited by microRNA-101.
30093632	2	11	theme	fundamental	350:360	arg1	basis					372:376	the fundamental molecular basis	346:376	the fundamental molecular basis underlying this effect	346:399	The epithelial-mesenchymal transition (EMT) is considered essential for metastatic CRC, but the fundamental molecular basis underlying this effect remains unknown.
30093632	9	12	theme	Reducing	1477:1484	arg1	O-GlcNAcylation					1486:1500	Reducing O-GlcNAcylation	1477:1500	Reducing O-GlcNAcylation	1477:1500	Reducing O-GlcNAcylation may be a potential therapeutic strategy for metastatic CRC.
30093632	9	12	theme	Reducing	1477:1484	arg1	strategy					1533:1540	a potential therapeutic strategy	1509:1540	a potential therapeutic strategy for metastatic CRC	1509:1559	Reducing O-GlcNAcylation may be a potential therapeutic strategy for metastatic CRC.
30093632	7	13	theme	EZH2	1242:1245	arg1	upregulation					1218:1229	the upregulation	1214:1229	the upregulation of OGT and EZH2	1214:1245	In addition, O-GlcNAcylation and H3K27me3 modification in the miR-101 promoter region further inhibited the transcription of miR-101, resulting in the upregulation of OGT and EZH2 in metastatic CRC, thus forming a vicious cycle.
30093632	5	14	theme	metastasis	849:858	arg1	potential					860:868	greater lymph node metastasis potential	830:868	greater lymph node metastasis potential	830:868	The CRC patients with higher levels of O-GlcNAcylation exhibited greater lymph node metastasis potential and lower overall survival.
30093632	4	15	theme	cell	673:676	arg1	lines					678:682	cell lines	673:682	cell lines	673:682	The levels of O-GlcNAcylation were increased in the metastatic CRC tissues and cell lines, which likely promoted the EMT by enhancing EZH2 protein stability and function.
30093632	9	16	theme	potential	1511:1519	arg1	O-GlcNAcylation					1486:1500	Reducing O-GlcNAcylation	1477:1500	Reducing O-GlcNAcylation	1477:1500	Reducing O-GlcNAcylation may be a potential therapeutic strategy for metastatic CRC.
30093632	9	16	theme	potential	1511:1519	arg1	strategy					1533:1540	a potential therapeutic strategy	1509:1540	a potential therapeutic strategy for metastatic CRC	1509:1559	Reducing O-GlcNAcylation may be a potential therapeutic strategy for metastatic CRC.
30093632	4	17	theme	metastatic	646:655	arg1	tissues					661:667	metastatic CRC tissues	646:667	metastatic CRC tissues	646:667	The levels of O-GlcNAcylation were increased in the metastatic CRC tissues and cell lines, which likely promoted the EMT by enhancing EZH2 protein stability and function.
30093632	7	18	from	O-GlcNAcylation	1080:1094	arg1	region					1146:1151	the miR-101 promoter region	1125:1151	the miR-101 promoter region	1125:1151	In addition, O-GlcNAcylation and H3K27me3 modification in the miR-101 promoter region further inhibited the transcription of miR-101, resulting in the upregulation of OGT and EZH2 in metastatic CRC, thus forming a vicious cycle.
30093632	5	19	theme	overall	880:886	arg1	survival					888:895	lower overall survival	874:895	lower overall survival	874:895	The CRC patients with higher levels of O-GlcNAcylation exhibited greater lymph node metastasis potential and lower overall survival.
30093632	5	20	theme	O-GlcNAcylation	804:818	arg1	levels					794:799	higher levels	787:799	higher levels of O-GlcNAcylation	787:818	The CRC patients with higher levels of O-GlcNAcylation exhibited greater lymph node metastasis potential and lower overall survival.
30093632	3	21	theme	metabolic	525:533	arg1	reprogramming					535:547	cancer metabolic reprogramming	518:547	cancer metabolic reprogramming	518:547	Here, we identified that O-GlcNAcylation, a unique posttranslational modification (PTM) involved in cancer metabolic reprogramming, increased the metastatic capability of CRC.
30093632	7	22	theme	promoter	1137:1144	arg1	region					1146:1151	the miR-101 promoter region	1125:1151	the miR-101 promoter region	1125:1151	In addition, O-GlcNAcylation and H3K27me3 modification in the miR-101 promoter region further inhibited the transcription of miR-101, resulting in the upregulation of OGT and EZH2 in metastatic CRC, thus forming a vicious cycle.
30093632	1	23	theme	Advanced	113:120	arg1	CRC					141:143	CRC	141:143	CRC	141:143	Advanced colorectal cancer (CRC) is one of the deadliest cancers, and the 5-year survival rate of patients with metastasis is extremely low.
30093632	1	23	theme	Advanced	113:120	arg1	cancer					133:138	Advanced colorectal cancer	113:138	Advanced colorectal cancer (CRC)	113:144	Advanced colorectal cancer (CRC) is one of the deadliest cancers, and the 5-year survival rate of patients with metastasis is extremely low.
30093632	7	24	theme	OGT	1234:1236	arg1	upregulation					1218:1229	the upregulation	1214:1229	the upregulation of OGT and EZH2	1214:1245	In addition, O-GlcNAcylation and H3K27me3 modification in the miR-101 promoter region further inhibited the transcription of miR-101, resulting in the upregulation of OGT and EZH2 in metastatic CRC, thus forming a vicious cycle.
30093632	3	25	theme	CRC	589:591	arg1	capability					575:584	the metastatic capability	560:584	the metastatic capability of CRC	560:591	Here, we identified that O-GlcNAcylation, a unique posttranslational modification (PTM) involved in cancer metabolic reprogramming, increased the metastatic capability of CRC.
30093632	1	26	theme	5-year	187:192	arg1	rate					203:206	the 5-year survival rate	183:206	the 5-year survival rate of patients with metastasis	183:234	Advanced colorectal cancer (CRC) is one of the deadliest cancers, and the 5-year survival rate of patients with metastasis is extremely low.
30093632	1	26	theme	5-year	187:192	arg1	low					249:251	low	249:251	low	249:251	Advanced colorectal cancer (CRC) is one of the deadliest cancers, and the 5-year survival rate of patients with metastasis is extremely low.
30093632	0	27	theme	cancer	36:41	arg1	metastasis					43:52	colorectal cancer metastasis	25:52	colorectal cancer metastasis	25:52	O-GlcNAcylation promotes colorectal cancer metastasis via the miR-101-O-GlcNAc/EZH2 regulatory feedback circuit.
30093632	4	28	theme	protein	733:739	arg1	stability					741:749	EZH2 protein stability	728:749	EZH2 protein stability	728:749	The levels of O-GlcNAcylation were increased in the metastatic CRC tissues and cell lines, which likely promoted the EMT by enhancing EZH2 protein stability and function.
30093632	3	29	theme	metastatic	564:573	arg1	capability					575:584	the metastatic capability	560:584	the metastatic capability of CRC	560:591	Here, we identified that O-GlcNAcylation, a unique posttranslational modification (PTM) involved in cancer metabolic reprogramming, increased the metastatic capability of CRC.
30093632	8	30	theme	EZH2	1440:1443	arg1	stability					1453:1461	EZH2 protein stability	1440:1461	EZH2 protein stability	1440:1461	In this study, we demonstrated that O-GlcNAcylation, which is negatively regulated by microRNA-101, likely promotes CRC metastasis by enhancing EZH2 protein stability and function.
30093632	3	31	theme	unique	462:467	arg1	PTM					501:503	PTM	501:503	PTM	501:503	Here, we identified that O-GlcNAcylation, a unique posttranslational modification (PTM) involved in cancer metabolic reprogramming, increased the metastatic capability of CRC.
30093632	3	31	theme	unique	462:467	arg1	modification					487:498	a unique posttranslational modification	460:498	a unique posttranslational modification (PTM) involved in cancer metabolic reprogramming	460:547	Here, we identified that O-GlcNAcylation, a unique posttranslational modification (PTM) involved in cancer metabolic reprogramming, increased the metastatic capability of CRC.
30093632	3	31	theme	unique	462:467	arg1	O-GlcNAcylation					443:457	O-GlcNAcylation	443:457	O-GlcNAcylation	443:457	Here, we identified that O-GlcNAcylation, a unique posttranslational modification (PTM) involved in cancer metabolic reprogramming, increased the metastatic capability of CRC.
30093632	1	32	theme	colorectal	122:131	arg1	CRC					141:143	CRC	141:143	CRC	141:143	Advanced colorectal cancer (CRC) is one of the deadliest cancers, and the 5-year survival rate of patients with metastasis is extremely low.
30093632	1	32	theme	colorectal	122:131	arg1	cancer					133:138	Advanced colorectal cancer	113:138	Advanced colorectal cancer (CRC)	113:144	Advanced colorectal cancer (CRC) is one of the deadliest cancers, and the 5-year survival rate of patients with metastasis is extremely low.
30093632	1	33	with	patients	211:218	arg1	metastasis					225:234	metastasis	225:234	metastasis	225:234	Advanced colorectal cancer (CRC) is one of the deadliest cancers, and the 5-year survival rate of patients with metastasis is extremely low.
30093632	3	34	theme	posttranslational	469:485	arg1	PTM					501:503	PTM	501:503	PTM	501:503	Here, we identified that O-GlcNAcylation, a unique posttranslational modification (PTM) involved in cancer metabolic reprogramming, increased the metastatic capability of CRC.
30093632	3	34	theme	posttranslational	469:485	arg1	modification					487:498	a unique posttranslational modification	460:498	a unique posttranslational modification (PTM) involved in cancer metabolic reprogramming	460:547	Here, we identified that O-GlcNAcylation, a unique posttranslational modification (PTM) involved in cancer metabolic reprogramming, increased the metastatic capability of CRC.
30093632	3	34	theme	posttranslational	469:485	arg1	O-GlcNAcylation					443:457	O-GlcNAcylation	443:457	O-GlcNAcylation	443:457	Here, we identified that O-GlcNAcylation, a unique posttranslational modification (PTM) involved in cancer metabolic reprogramming, increased the metastatic capability of CRC.
30093632	4	35	dep	tissues	661:667	arg1	the					642:644	the	642:644	the	642:644	The levels of O-GlcNAcylation were increased in the metastatic CRC tissues and cell lines, which likely promoted the EMT by enhancing EZH2 protein stability and function.
30093632	5	36	theme	lower	874:878	arg1	survival					888:895	lower overall survival	874:895	lower overall survival	874:895	The CRC patients with higher levels of O-GlcNAcylation exhibited greater lymph node metastasis potential and lower overall survival.
30093632	5	37	theme	higher	787:792	arg1	levels					794:799	higher levels	787:799	higher levels of O-GlcNAcylation	787:818	The CRC patients with higher levels of O-GlcNAcylation exhibited greater lymph node metastasis potential and lower overall survival.
30093632	5	38	theme	greater	830:836	arg1	potential					860:868	greater lymph node metastasis potential	830:868	greater lymph node metastasis potential	830:868	The CRC patients with higher levels of O-GlcNAcylation exhibited greater lymph node metastasis potential and lower overall survival.
30093632	1	39	theme	patients	211:218	arg1	rate					203:206	the 5-year survival rate	183:206	the 5-year survival rate of patients with metastasis	183:234	Advanced colorectal cancer (CRC) is one of the deadliest cancers, and the 5-year survival rate of patients with metastasis is extremely low.
30093632	1	39	theme	patients	211:218	arg1	low					249:251	low	249:251	low	249:251	Advanced colorectal cancer (CRC) is one of the deadliest cancers, and the 5-year survival rate of patients with metastasis is extremely low.
30093632	0	40	theme	miR-101-O-GlcNAc/EZH2	62:82	arg1	circuit					104:110	the miR-101-O-GlcNAc/EZH2 regulatory feedback circuit	58:110	the miR-101-O-GlcNAc/EZH2 regulatory feedback circuit	58:110	O-GlcNAcylation promotes colorectal cancer metastasis via the miR-101-O-GlcNAc/EZH2 regulatory feedback circuit.
30093632	9	41	theme	metastatic	1546:1555	arg1	CRC					1557:1559	metastatic CRC	1546:1559	metastatic CRC	1546:1559	Reducing O-GlcNAcylation may be a potential therapeutic strategy for metastatic CRC.
30093632	6	42	theme	reporter	936:943	arg1	assays					945:950	luciferase reporter assays	925:950	luciferase reporter assays	925:950	Bioinformatic analysis and luciferase reporter assays revealed that both O-GlcNAcylation transferase (OGT) and EZH2 are posttranscriptionally inhibited by microRNA-101.
30093632	6	43	theme	O-GlcNAcylation	971:985	arg1	transferase					987:997	O-GlcNAcylation transferase	971:997	O-GlcNAcylation transferase (OGT)	971:1003	Bioinformatic analysis and luciferase reporter assays revealed that both O-GlcNAcylation transferase (OGT) and EZH2 are posttranscriptionally inhibited by microRNA-101.
30093632	6	43	theme	O-GlcNAcylation	971:985	arg1	OGT					1000:1002	OGT	1000:1002	OGT	1000:1002	Bioinformatic analysis and luciferase reporter assays revealed that both O-GlcNAcylation transferase (OGT) and EZH2 are posttranscriptionally inhibited by microRNA-101.
30093632	7	44	theme	H3K27me3	1100:1107	arg1	modification					1109:1120	H3K27me3 modification	1100:1120	H3K27me3 modification	1100:1120	In addition, O-GlcNAcylation and H3K27me3 modification in the miR-101 promoter region further inhibited the transcription of miR-101, resulting in the upregulation of OGT and EZH2 in metastatic CRC, thus forming a vicious cycle.
30093632	8	45	theme	protein	1445:1451	arg1	stability					1453:1461	EZH2 protein stability	1440:1461	EZH2 protein stability	1440:1461	In this study, we demonstrated that O-GlcNAcylation, which is negatively regulated by microRNA-101, likely promotes CRC metastasis by enhancing EZH2 protein stability and function.
30093632	6	46	theme	Bioinformatic	898:910	arg1	analysis					912:919	Bioinformatic analysis	898:919	Bioinformatic analysis	898:919	Bioinformatic analysis and luciferase reporter assays revealed that both O-GlcNAcylation transferase (OGT) and EZH2 are posttranscriptionally inhibited by microRNA-101.
30093632	2	47	theme	epithelial-mesenchymal	258:279	arg1	EMT					293:295	EMT	293:295	EMT	293:295	The epithelial-mesenchymal transition (EMT) is considered essential for metastatic CRC, but the fundamental molecular basis underlying this effect remains unknown.
30093632	2	47	theme	epithelial-mesenchymal	258:279	arg1	transition					281:290	The epithelial-mesenchymal transition	254:290	The epithelial-mesenchymal transition (EMT)	254:296	The epithelial-mesenchymal transition (EMT) is considered essential for metastatic CRC, but the fundamental molecular basis underlying this effect remains unknown.
30093632	4	48	theme	EZH2	728:731	arg1	stability					741:749	EZH2 protein stability	728:749	EZH2 protein stability	728:749	The levels of O-GlcNAcylation were increased in the metastatic CRC tissues and cell lines, which likely promoted the EMT by enhancing EZH2 protein stability and function.
30093632	5	49	theme	lymph	838:842	arg1	node					844:847	lymph node	838:847	greater lymph node metastasis potential	830:868	The CRC patients with higher levels of O-GlcNAcylation exhibited greater lymph node metastasis potential and lower overall survival.
30093632	2	50	theme	metastatic	326:335	arg1	CRC					337:339	metastatic CRC	326:339	metastatic CRC	326:339	The epithelial-mesenchymal transition (EMT) is considered essential for metastatic CRC, but the fundamental molecular basis underlying this effect remains unknown.
30093632	4	51	theme	O-GlcNAcylation	608:622	arg1	levels					598:603	The levels	594:603	The levels of O-GlcNAcylation	594:622	The levels of O-GlcNAcylation were increased in the metastatic CRC tissues and cell lines, which likely promoted the EMT by enhancing EZH2 protein stability and function.
30093632	0	52	theme	feedback	95:102	arg1	circuit					104:110	the miR-101-O-GlcNAc/EZH2 regulatory feedback circuit	58:110	the miR-101-O-GlcNAc/EZH2 regulatory feedback circuit	58:110	O-GlcNAcylation promotes colorectal cancer metastasis via the miR-101-O-GlcNAc/EZH2 regulatory feedback circuit.
30093632	4	53	theme	CRC	657:659	arg1	tissues					661:667	metastatic CRC tissues	646:667	metastatic CRC tissues	646:667	The levels of O-GlcNAcylation were increased in the metastatic CRC tissues and cell lines, which likely promoted the EMT by enhancing EZH2 protein stability and function.
30093632	9	54	dep	potential	1511:1519	arg1	therapeutic					1521:1531	therapeutic	1521:1531	therapeutic	1521:1531	Reducing O-GlcNAcylation may be a potential therapeutic strategy for metastatic CRC.
30093632	1	55	theme	survival	194:201	arg1	rate					203:206	the 5-year survival rate	183:206	the 5-year survival rate of patients with metastasis	183:234	Advanced colorectal cancer (CRC) is one of the deadliest cancers, and the 5-year survival rate of patients with metastasis is extremely low.
30093632	1	55	theme	survival	194:201	arg1	low					249:251	low	249:251	low	249:251	Advanced colorectal cancer (CRC) is one of the deadliest cancers, and the 5-year survival rate of patients with metastasis is extremely low.
30093632	3	56	theme	cancer	518:523	arg1	reprogramming					535:547	cancer metabolic reprogramming	518:547	cancer metabolic reprogramming	518:547	Here, we identified that O-GlcNAcylation, a unique posttranslational modification (PTM) involved in cancer metabolic reprogramming, increased the metastatic capability of CRC.
30093632	0	57	theme	regulatory	84:93	arg1	circuit					104:110	the miR-101-O-GlcNAc/EZH2 regulatory feedback circuit	58:110	the miR-101-O-GlcNAc/EZH2 regulatory feedback circuit	58:110	O-GlcNAcylation promotes colorectal cancer metastasis via the miR-101-O-GlcNAc/EZH2 regulatory feedback circuit.
30093632	0	58	theme	colorectal	25:34	arg1	metastasis					43:52	colorectal cancer metastasis	25:52	colorectal cancer metastasis	25:52	O-GlcNAcylation promotes colorectal cancer metastasis via the miR-101-O-GlcNAc/EZH2 regulatory feedback circuit.
30093632	2	59	theme	molecular	362:370	arg1	basis					372:376	the fundamental molecular basis	346:376	the fundamental molecular basis underlying this effect	346:399	The epithelial-mesenchymal transition (EMT) is considered essential for metastatic CRC, but the fundamental molecular basis underlying this effect remains unknown.
30093632	7	60	theme	vicious	1281:1287	arg1	cycle					1289:1293	a vicious cycle	1279:1293	a vicious cycle	1279:1293	In addition, O-GlcNAcylation and H3K27me3 modification in the miR-101 promoter region further inhibited the transcription of miR-101, resulting in the upregulation of OGT and EZH2 in metastatic CRC, thus forming a vicious cycle.
35470239	0	0	theme	embryonic	108:116	arg1	neurogenesis					118:129	embryonic neurogenesis	108:129	embryonic neurogenesis	108:129	Nutrient sensitive protein O-GlcNAcylation modulates the transcriptome through epigenetic mechanisms during embryonic neurogenesis.
35470239	4	1	theme	increased	840:848	arg1	levels					858:863	increased H3K4me3 levels	840:863	increased H3K4me3 levels	840:863	This transcriptional de-repression is associated with reduced H3K27me3 and increased H3K4me3 levels on the promoters of these genes, perturbing promoter bivalency possibly through increased EZH2-Thr311 phosphorylation.
35470239	2	2	theme	nutrient	431:438	arg1	perturbations					440:452	nutrient perturbations	431:452	nutrient perturbations during development	431:471	However, the role of protein O-GlcNAcylation on epigenome regulation in response to nutrient perturbations during development is not well understood.
35470239	5	3	from	H2BS112O-GlcNAc	1071:1085	arg1	promoters					1105:1113	promoters	1105:1113	promoters	1105:1113	Elevated O-GlcNAc levels also lead to increased Pol II-Ser5 phosphorylation and affect H2BS112O-GlcNAc and H2BK120Ub1 on promoters.
35470239	1	4	from	deposited	208:216	arg1	factors					301:307	transcription factors	287:307	transcription factors	287:307	Protein O-GlcNAcylation is a dynamic, nutrient-sensitive mono-glycosylation deposited on numerous nucleo-cytoplasmic and mitochondrial proteins, including transcription factors, epigenetic regulators, and histones.
35470239	1	4	from	deposited	208:216	arg1	regulators					321:330	epigenetic regulators	310:330	epigenetic regulators	310:330	Protein O-GlcNAcylation is a dynamic, nutrient-sensitive mono-glycosylation deposited on numerous nucleo-cytoplasmic and mitochondrial proteins, including transcription factors, epigenetic regulators, and histones.
35470239	1	4	from	deposited	208:216	arg1	histones					337:344	histones	337:344	histones	337:344	Protein O-GlcNAcylation is a dynamic, nutrient-sensitive mono-glycosylation deposited on numerous nucleo-cytoplasmic and mitochondrial proteins, including transcription factors, epigenetic regulators, and histones.
35470239	1	4	from	deposited	208:216	arg1	proteins					267:274	numerous nucleo-cytoplasmic and mitochondrial proteins	221:274	numerous nucleo-cytoplasmic and mitochondrial proteins	221:274	Protein O-GlcNAcylation is a dynamic, nutrient-sensitive mono-glycosylation deposited on numerous nucleo-cytoplasmic and mitochondrial proteins, including transcription factors, epigenetic regulators, and histones.
35470239	4	5	from	H3K27me3	827:834	arg1	promoters					872:880	the promoters	868:880	the promoters of these genes	868:895	This transcriptional de-repression is associated with reduced H3K27me3 and increased H3K4me3 levels on the promoters of these genes, perturbing promoter bivalency possibly through increased EZH2-Thr311 phosphorylation.
35470239	7	6	theme	nutrient	1480:1487	arg1	status					1489:1494	nutrient status	1480:1494	nutrient status	1480:1494	Together, our results demonstrate O-GlcNAc mediated sensitivity of chromatin to nutrient status, and indicate how metabolic perturbations could affect gene expression during neurodevelopment.
35470239	6	7	from	levels	1206:1211	arg1	brains					1268:1273	the developing embryo brains	1246:1273	the developing embryo brains	1246:1273	Using an in vivo rat model of maternal hyperglycemia, we show similarly elevated O-GlcNAc levels and epigenetic dysregulations in the developing embryo brains because of hyperglycemia, whereas pharmacological inhibition of O-GlcNAc transferase (OGT) restored these molecular changes.
35470239	1	8	dep	dynamic	161:167	arg1	nutrient-sensitive					170:187	nutrient-sensitive	170:187	nutrient-sensitive	170:187	Protein O-GlcNAcylation is a dynamic, nutrient-sensitive mono-glycosylation deposited on numerous nucleo-cytoplasmic and mitochondrial proteins, including transcription factors, epigenetic regulators, and histones.
35470239	6	9	theme	O-GlcNAc	1339:1346	arg1	OGT					1361:1363	OGT	1361:1363	OGT	1361:1363	Using an in vivo rat model of maternal hyperglycemia, we show similarly elevated O-GlcNAc levels and epigenetic dysregulations in the developing embryo brains because of hyperglycemia, whereas pharmacological inhibition of O-GlcNAc transferase (OGT) restored these molecular changes.
35470239	6	9	theme	O-GlcNAc	1339:1346	arg1	transferase					1348:1358	O-GlcNAc transferase	1339:1358	O-GlcNAc transferase (OGT)	1339:1364	Using an in vivo rat model of maternal hyperglycemia, we show similarly elevated O-GlcNAc levels and epigenetic dysregulations in the developing embryo brains because of hyperglycemia, whereas pharmacological inhibition of O-GlcNAc transferase (OGT) restored these molecular changes.
35470239	3	10	theme	stem	659:662	arg1	differentiation					680:694	human embryonic stem cells' neuronal differentiation	643:694	human embryonic stem cells' neuronal differentiation	643:694	Herein we recapitulated early human embryonic neurogenesis in cell culture and found that pharmacological up-regulation of O-GlcNAc levels during human embryonic stem cells' neuronal differentiation leads to up-regulation of key neurogenic transcription factor genes.
35470239	5	11	theme	increased	1022:1030	arg1	phosphorylation					1044:1058	increased Pol II-Ser5 phosphorylation	1022:1058	increased Pol II-Ser5 phosphorylation	1022:1058	Elevated O-GlcNAc levels also lead to increased Pol II-Ser5 phosphorylation and affect H2BS112O-GlcNAc and H2BK120Ub1 on promoters.
35470239	7	12	theme	metabolic	1514:1522	arg1	perturbations					1524:1536	metabolic perturbations	1514:1536	metabolic perturbations	1514:1536	Together, our results demonstrate O-GlcNAc mediated sensitivity of chromatin to nutrient status, and indicate how metabolic perturbations could affect gene expression during neurodevelopment.
35470239	4	13	from	levels	858:863	arg1	promoters					872:880	the promoters	868:880	the promoters of these genes	868:895	This transcriptional de-repression is associated with reduced H3K27me3 and increased H3K4me3 levels on the promoters of these genes, perturbing promoter bivalency possibly through increased EZH2-Thr311 phosphorylation.
35470239	1	14	theme	numerous	221:228	arg1	factors					301:307	transcription factors	287:307	transcription factors	287:307	Protein O-GlcNAcylation is a dynamic, nutrient-sensitive mono-glycosylation deposited on numerous nucleo-cytoplasmic and mitochondrial proteins, including transcription factors, epigenetic regulators, and histones.
35470239	1	14	theme	numerous	221:228	arg1	regulators					321:330	epigenetic regulators	310:330	epigenetic regulators	310:330	Protein O-GlcNAcylation is a dynamic, nutrient-sensitive mono-glycosylation deposited on numerous nucleo-cytoplasmic and mitochondrial proteins, including transcription factors, epigenetic regulators, and histones.
35470239	1	14	theme	numerous	221:228	arg1	histones					337:344	histones	337:344	histones	337:344	Protein O-GlcNAcylation is a dynamic, nutrient-sensitive mono-glycosylation deposited on numerous nucleo-cytoplasmic and mitochondrial proteins, including transcription factors, epigenetic regulators, and histones.
35470239	1	14	theme	numerous	221:228	arg1	proteins					267:274	numerous nucleo-cytoplasmic and mitochondrial proteins	221:274	numerous nucleo-cytoplasmic and mitochondrial proteins	221:274	Protein O-GlcNAcylation is a dynamic, nutrient-sensitive mono-glycosylation deposited on numerous nucleo-cytoplasmic and mitochondrial proteins, including transcription factors, epigenetic regulators, and histones.
35470239	6	15	theme	hyperglycemia	1155:1167	arg1	model					1137:1141	an in vivo rat model	1122:1141	an in vivo rat model of maternal hyperglycemia	1122:1167	Using an in vivo rat model of maternal hyperglycemia, we show similarly elevated O-GlcNAc levels and epigenetic dysregulations in the developing embryo brains because of hyperglycemia, whereas pharmacological inhibition of O-GlcNAc transferase (OGT) restored these molecular changes.
35470239	6	16	theme	pharmacological	1309:1323	arg1	inhibition					1325:1334	pharmacological inhibition	1309:1334	pharmacological inhibition of O-GlcNAc transferase (OGT)	1309:1364	Using an in vivo rat model of maternal hyperglycemia, we show similarly elevated O-GlcNAc levels and epigenetic dysregulations in the developing embryo brains because of hyperglycemia, whereas pharmacological inhibition of O-GlcNAc transferase (OGT) restored these molecular changes.
35470239	3	17	theme	human	643:647	arg1	differentiation					680:694	human embryonic stem cells' neuronal differentiation	643:694	human embryonic stem cells' neuronal differentiation	643:694	Herein we recapitulated early human embryonic neurogenesis in cell culture and found that pharmacological up-regulation of O-GlcNAc levels during human embryonic stem cells' neuronal differentiation leads to up-regulation of key neurogenic transcription factor genes.
35470239	1	18	theme	nucleo-cytoplasmic	230:247	arg1	factors					301:307	transcription factors	287:307	transcription factors	287:307	Protein O-GlcNAcylation is a dynamic, nutrient-sensitive mono-glycosylation deposited on numerous nucleo-cytoplasmic and mitochondrial proteins, including transcription factors, epigenetic regulators, and histones.
35470239	1	18	theme	nucleo-cytoplasmic	230:247	arg1	regulators					321:330	epigenetic regulators	310:330	epigenetic regulators	310:330	Protein O-GlcNAcylation is a dynamic, nutrient-sensitive mono-glycosylation deposited on numerous nucleo-cytoplasmic and mitochondrial proteins, including transcription factors, epigenetic regulators, and histones.
35470239	1	18	theme	nucleo-cytoplasmic	230:247	arg1	histones					337:344	histones	337:344	histones	337:344	Protein O-GlcNAcylation is a dynamic, nutrient-sensitive mono-glycosylation deposited on numerous nucleo-cytoplasmic and mitochondrial proteins, including transcription factors, epigenetic regulators, and histones.
35470239	1	18	theme	nucleo-cytoplasmic	230:247	arg1	proteins					267:274	numerous nucleo-cytoplasmic and mitochondrial proteins	221:274	numerous nucleo-cytoplasmic and mitochondrial proteins	221:274	Protein O-GlcNAcylation is a dynamic, nutrient-sensitive mono-glycosylation deposited on numerous nucleo-cytoplasmic and mitochondrial proteins, including transcription factors, epigenetic regulators, and histones.
35470239	0	19	theme	sensitive	9:17	arg1	O-GlcNAcylation					27:41	Nutrient sensitive protein O-GlcNAcylation	0:41	Nutrient sensitive protein O-GlcNAcylation	0:41	Nutrient sensitive protein O-GlcNAcylation modulates the transcriptome through epigenetic mechanisms during embryonic neurogenesis.
35470239	3	20	theme	levels	629:634	arg1	up-regulation					603:615	pharmacological up-regulation	587:615	pharmacological up-regulation of O-GlcNAc levels during human embryonic stem cells' neuronal differentiation	587:694	Herein we recapitulated early human embryonic neurogenesis in cell culture and found that pharmacological up-regulation of O-GlcNAc levels during human embryonic stem cells' neuronal differentiation leads to up-regulation of key neurogenic transcription factor genes.
35470239	7	21	theme	chromatin	1467:1475	arg1	sensitivity					1452:1462	O-GlcNAc mediated sensitivity	1434:1462	O-GlcNAc mediated sensitivity of chromatin to nutrient status	1434:1494	Together, our results demonstrate O-GlcNAc mediated sensitivity of chromatin to nutrient status, and indicate how metabolic perturbations could affect gene expression during neurodevelopment.
35470239	3	22	theme	neuronal	671:678	arg1	differentiation					680:694	human embryonic stem cells' neuronal differentiation	643:694	human embryonic stem cells' neuronal differentiation	643:694	Herein we recapitulated early human embryonic neurogenesis in cell culture and found that pharmacological up-regulation of O-GlcNAc levels during human embryonic stem cells' neuronal differentiation leads to up-regulation of key neurogenic transcription factor genes.
35470239	6	23	theme	developing	1250:1259	arg1	brains					1268:1273	the developing embryo brains	1246:1273	the developing embryo brains	1246:1273	Using an in vivo rat model of maternal hyperglycemia, we show similarly elevated O-GlcNAc levels and epigenetic dysregulations in the developing embryo brains because of hyperglycemia, whereas pharmacological inhibition of O-GlcNAc transferase (OGT) restored these molecular changes.
35470239	5	24	theme	II-Ser5	1036:1042	arg1	phosphorylation					1044:1058	increased Pol II-Ser5 phosphorylation	1022:1058	increased Pol II-Ser5 phosphorylation	1022:1058	Elevated O-GlcNAc levels also lead to increased Pol II-Ser5 phosphorylation and affect H2BS112O-GlcNAc and H2BK120Ub1 on promoters.
35470239	0	25	theme	Nutrient	0:7	arg1	O-GlcNAcylation					27:41	Nutrient sensitive protein O-GlcNAcylation	0:41	Nutrient sensitive protein O-GlcNAcylation	0:41	Nutrient sensitive protein O-GlcNAcylation modulates the transcriptome through epigenetic mechanisms during embryonic neurogenesis.
35470239	6	26	theme	maternal	1146:1153	arg1	hyperglycemia					1155:1167	maternal hyperglycemia	1146:1167	maternal hyperglycemia	1146:1167	Using an in vivo rat model of maternal hyperglycemia, we show similarly elevated O-GlcNAc levels and epigenetic dysregulations in the developing embryo brains because of hyperglycemia, whereas pharmacological inhibition of O-GlcNAc transferase (OGT) restored these molecular changes.
35470239	5	27	from	H2BK120Ub1	1091:1100	arg1	promoters					1105:1113	promoters	1105:1113	promoters	1105:1113	Elevated O-GlcNAc levels also lead to increased Pol II-Ser5 phosphorylation and affect H2BS112O-GlcNAc and H2BK120Ub1 on promoters.
35470239	2	28	theme	O-GlcNAcylation	376:390	arg1	role					360:363	the role	356:363	the role of protein O-GlcNAcylation on epigenome regulation in response to nutrient perturbations during development	356:471	However, the role of protein O-GlcNAcylation on epigenome regulation in response to nutrient perturbations during development is not well understood.
35470239	1	29	theme	mitochondrial	253:265	arg1	factors					301:307	transcription factors	287:307	transcription factors	287:307	Protein O-GlcNAcylation is a dynamic, nutrient-sensitive mono-glycosylation deposited on numerous nucleo-cytoplasmic and mitochondrial proteins, including transcription factors, epigenetic regulators, and histones.
35470239	1	29	theme	mitochondrial	253:265	arg1	regulators					321:330	epigenetic regulators	310:330	epigenetic regulators	310:330	Protein O-GlcNAcylation is a dynamic, nutrient-sensitive mono-glycosylation deposited on numerous nucleo-cytoplasmic and mitochondrial proteins, including transcription factors, epigenetic regulators, and histones.
35470239	1	29	theme	mitochondrial	253:265	arg1	histones					337:344	histones	337:344	histones	337:344	Protein O-GlcNAcylation is a dynamic, nutrient-sensitive mono-glycosylation deposited on numerous nucleo-cytoplasmic and mitochondrial proteins, including transcription factors, epigenetic regulators, and histones.
35470239	1	29	theme	mitochondrial	253:265	arg1	proteins					267:274	numerous nucleo-cytoplasmic and mitochondrial proteins	221:274	numerous nucleo-cytoplasmic and mitochondrial proteins	221:274	Protein O-GlcNAcylation is a dynamic, nutrient-sensitive mono-glycosylation deposited on numerous nucleo-cytoplasmic and mitochondrial proteins, including transcription factors, epigenetic regulators, and histones.
35470239	5	30	theme	Elevated	984:991	arg1	levels					1002:1007	Elevated O-GlcNAc levels	984:1007	Elevated O-GlcNAc levels	984:1007	Elevated O-GlcNAc levels also lead to increased Pol II-Ser5 phosphorylation and affect H2BS112O-GlcNAc and H2BK120Ub1 on promoters.
35470239	4	31	theme	EZH2-Thr311	955:965	arg1	phosphorylation					967:981	increased EZH2-Thr311 phosphorylation	945:981	increased EZH2-Thr311 phosphorylation	945:981	This transcriptional de-repression is associated with reduced H3K27me3 and increased H3K4me3 levels on the promoters of these genes, perturbing promoter bivalency possibly through increased EZH2-Thr311 phosphorylation.
35470239	6	32	from	dysregulations	1228:1241	arg1	brains					1268:1273	the developing embryo brains	1246:1273	the developing embryo brains	1246:1273	Using an in vivo rat model of maternal hyperglycemia, we show similarly elevated O-GlcNAc levels and epigenetic dysregulations in the developing embryo brains because of hyperglycemia, whereas pharmacological inhibition of O-GlcNAc transferase (OGT) restored these molecular changes.
35470239	2	33	theme	protein	368:374	arg1	O-GlcNAcylation					376:390	protein O-GlcNAcylation	368:390	protein O-GlcNAcylation	368:390	However, the role of protein O-GlcNAcylation on epigenome regulation in response to nutrient perturbations during development is not well understood.
35470239	2	34	from	regulation	405:414	arg1	response					419:426	response	419:426	response to nutrient perturbations during development	419:471	However, the role of protein O-GlcNAcylation on epigenome regulation in response to nutrient perturbations during development is not well understood.
35470239	3	35	theme	cell	559:562	arg1	culture					564:570	cell culture	559:570	cell culture	559:570	Herein we recapitulated early human embryonic neurogenesis in cell culture and found that pharmacological up-regulation of O-GlcNAc levels during human embryonic stem cells' neuronal differentiation leads to up-regulation of key neurogenic transcription factor genes.
35470239	0	36	theme	protein	19:25	arg1	O-GlcNAcylation					27:41	Nutrient sensitive protein O-GlcNAcylation	0:41	Nutrient sensitive protein O-GlcNAcylation	0:41	Nutrient sensitive protein O-GlcNAcylation modulates the transcriptome through epigenetic mechanisms during embryonic neurogenesis.
35470239	6	37	theme	embryo	1261:1266	arg1	brains					1268:1273	the developing embryo brains	1246:1273	the developing embryo brains	1246:1273	Using an in vivo rat model of maternal hyperglycemia, we show similarly elevated O-GlcNAc levels and epigenetic dysregulations in the developing embryo brains because of hyperglycemia, whereas pharmacological inhibition of O-GlcNAc transferase (OGT) restored these molecular changes.
35470239	6	38	theme	molecular	1381:1389	arg1	changes					1391:1397	these molecular changes	1375:1397	these molecular changes	1375:1397	Using an in vivo rat model of maternal hyperglycemia, we show similarly elevated O-GlcNAc levels and epigenetic dysregulations in the developing embryo brains because of hyperglycemia, whereas pharmacological inhibition of O-GlcNAc transferase (OGT) restored these molecular changes.
35470239	4	39	theme	genes	891:895	arg1	promoters					872:880	the promoters	868:880	the promoters of these genes	868:895	This transcriptional de-repression is associated with reduced H3K27me3 and increased H3K4me3 levels on the promoters of these genes, perturbing promoter bivalency possibly through increased EZH2-Thr311 phosphorylation.
35470239	5	40	theme	Pol	1032:1034	arg1	phosphorylation					1044:1058	increased Pol II-Ser5 phosphorylation	1022:1058	increased Pol II-Ser5 phosphorylation	1022:1058	Elevated O-GlcNAc levels also lead to increased Pol II-Ser5 phosphorylation and affect H2BS112O-GlcNAc and H2BK120Ub1 on promoters.
35470239	4	41	theme	H3K4me3	850:856	arg1	levels					858:863	increased H3K4me3 levels	840:863	increased H3K4me3 levels	840:863	This transcriptional de-repression is associated with reduced H3K27me3 and increased H3K4me3 levels on the promoters of these genes, perturbing promoter bivalency possibly through increased EZH2-Thr311 phosphorylation.
35470239	6	42	theme	epigenetic	1217:1226	arg1	dysregulations					1228:1241	epigenetic dysregulations	1217:1241	epigenetic dysregulations	1217:1241	Using an in vivo rat model of maternal hyperglycemia, we show similarly elevated O-GlcNAc levels and epigenetic dysregulations in the developing embryo brains because of hyperglycemia, whereas pharmacological inhibition of O-GlcNAc transferase (OGT) restored these molecular changes.
35470239	6	43	theme	rat	1133:1135	arg1	model					1137:1141	an in vivo rat model	1122:1141	an in vivo rat model of maternal hyperglycemia	1122:1167	Using an in vivo rat model of maternal hyperglycemia, we show similarly elevated O-GlcNAc levels and epigenetic dysregulations in the developing embryo brains because of hyperglycemia, whereas pharmacological inhibition of O-GlcNAc transferase (OGT) restored these molecular changes.
35470239	3	44	theme	early	521:525	arg1	neurogenesis					543:554	early human embryonic neurogenesis	521:554	early human embryonic neurogenesis in cell culture	521:570	Herein we recapitulated early human embryonic neurogenesis in cell culture and found that pharmacological up-regulation of O-GlcNAc levels during human embryonic stem cells' neuronal differentiation leads to up-regulation of key neurogenic transcription factor genes.
35470239	4	45	theme	transcriptional	770:784	arg1	de-repression					786:798	This transcriptional de-repression	765:798	This transcriptional de-repression	765:798	This transcriptional de-repression is associated with reduced H3K27me3 and increased H3K4me3 levels on the promoters of these genes, perturbing promoter bivalency possibly through increased EZH2-Thr311 phosphorylation.
35470239	3	46	theme	human	527:531	arg1	neurogenesis					543:554	early human embryonic neurogenesis	521:554	early human embryonic neurogenesis in cell culture	521:570	Herein we recapitulated early human embryonic neurogenesis in cell culture and found that pharmacological up-regulation of O-GlcNAc levels during human embryonic stem cells' neuronal differentiation leads to up-regulation of key neurogenic transcription factor genes.
35470239	3	47	theme	genes	758:762	arg1	up-regulation					705:717	up-regulation	705:717	up-regulation of key neurogenic transcription factor genes	705:762	Herein we recapitulated early human embryonic neurogenesis in cell culture and found that pharmacological up-regulation of O-GlcNAc levels during human embryonic stem cells' neuronal differentiation leads to up-regulation of key neurogenic transcription factor genes.
35470239	6	48	theme	elevated	1188:1195	arg1	levels					1206:1211	similarly elevated O-GlcNAc levels	1178:1211	similarly elevated O-GlcNAc levels	1178:1211	Using an in vivo rat model of maternal hyperglycemia, we show similarly elevated O-GlcNAc levels and epigenetic dysregulations in the developing embryo brains because of hyperglycemia, whereas pharmacological inhibition of O-GlcNAc transferase (OGT) restored these molecular changes.
35470239	3	49	from	neurogenesis	543:554	arg1	culture					564:570	cell culture	559:570	cell culture	559:570	Herein we recapitulated early human embryonic neurogenesis in cell culture and found that pharmacological up-regulation of O-GlcNAc levels during human embryonic stem cells' neuronal differentiation leads to up-regulation of key neurogenic transcription factor genes.
35470239	1	50	theme	transcription	287:299	arg1	factors					301:307	transcription factors	287:307	transcription factors	287:307	Protein O-GlcNAcylation is a dynamic, nutrient-sensitive mono-glycosylation deposited on numerous nucleo-cytoplasmic and mitochondrial proteins, including transcription factors, epigenetic regulators, and histones.
35470239	6	51	theme	in	1125:1126	arg1	model					1137:1141	an in vivo rat model	1122:1141	an in vivo rat model of maternal hyperglycemia	1122:1167	Using an in vivo rat model of maternal hyperglycemia, we show similarly elevated O-GlcNAc levels and epigenetic dysregulations in the developing embryo brains because of hyperglycemia, whereas pharmacological inhibition of O-GlcNAc transferase (OGT) restored these molecular changes.
35470239	5	52	theme	O-GlcNAc	993:1000	arg1	levels					1002:1007	Elevated O-GlcNAc levels	984:1007	Elevated O-GlcNAc levels	984:1007	Elevated O-GlcNAc levels also lead to increased Pol II-Ser5 phosphorylation and affect H2BS112O-GlcNAc and H2BK120Ub1 on promoters.
35470239	6	53	dep	in	1125:1126	arg1	vivo					1128:1131	vivo	1128:1131	vivo	1128:1131	Using an in vivo rat model of maternal hyperglycemia, we show similarly elevated O-GlcNAc levels and epigenetic dysregulations in the developing embryo brains because of hyperglycemia, whereas pharmacological inhibition of O-GlcNAc transferase (OGT) restored these molecular changes.
35470239	6	54	theme	transferase	1348:1358	arg1	inhibition					1325:1334	pharmacological inhibition	1309:1334	pharmacological inhibition of O-GlcNAc transferase (OGT)	1309:1364	Using an in vivo rat model of maternal hyperglycemia, we show similarly elevated O-GlcNAc levels and epigenetic dysregulations in the developing embryo brains because of hyperglycemia, whereas pharmacological inhibition of O-GlcNAc transferase (OGT) restored these molecular changes.
35470239	7	55	theme	gene	1551:1554	arg1	expression					1556:1565	gene expression	1551:1565	gene expression	1551:1565	Together, our results demonstrate O-GlcNAc mediated sensitivity of chromatin to nutrient status, and indicate how metabolic perturbations could affect gene expression during neurodevelopment.
35470239	3	56	theme	pharmacological	587:601	arg1	up-regulation					603:615	pharmacological up-regulation	587:615	pharmacological up-regulation of O-GlcNAc levels during human embryonic stem cells' neuronal differentiation	587:694	Herein we recapitulated early human embryonic neurogenesis in cell culture and found that pharmacological up-regulation of O-GlcNAc levels during human embryonic stem cells' neuronal differentiation leads to up-regulation of key neurogenic transcription factor genes.
35470239	4	57	theme	increased	945:953	arg1	phosphorylation					967:981	increased EZH2-Thr311 phosphorylation	945:981	increased EZH2-Thr311 phosphorylation	945:981	This transcriptional de-repression is associated with reduced H3K27me3 and increased H3K4me3 levels on the promoters of these genes, perturbing promoter bivalency possibly through increased EZH2-Thr311 phosphorylation.
35470239	3	58	theme	transcription	737:749	arg1	genes					758:762	key neurogenic transcription factor genes	722:762	key neurogenic transcription factor genes	722:762	Herein we recapitulated early human embryonic neurogenesis in cell culture and found that pharmacological up-regulation of O-GlcNAc levels during human embryonic stem cells' neuronal differentiation leads to up-regulation of key neurogenic transcription factor genes.
35470239	4	59	theme	reduced	819:825	arg1	H3K27me3					827:834	reduced H3K27me3	819:834	reduced H3K27me3	819:834	This transcriptional de-repression is associated with reduced H3K27me3 and increased H3K4me3 levels on the promoters of these genes, perturbing promoter bivalency possibly through increased EZH2-Thr311 phosphorylation.
35470239	1	60	theme	dynamic	161:167	arg1	deposited					208:216	a dynamic, nutrient-sensitive mono-glycosylation deposited	159:216	a dynamic, nutrient-sensitive mono-glycosylation deposited on numerous nucleo-cytoplasmic and mitochondrial proteins, including transcription factors, epigenetic regulators, and histones	159:344	Protein O-GlcNAcylation is a dynamic, nutrient-sensitive mono-glycosylation deposited on numerous nucleo-cytoplasmic and mitochondrial proteins, including transcription factors, epigenetic regulators, and histones.
35470239	1	60	theme	dynamic	161:167	arg1	O-GlcNAcylation					140:154	Protein O-GlcNAcylation	132:154	Protein O-GlcNAcylation	132:154	Protein O-GlcNAcylation is a dynamic, nutrient-sensitive mono-glycosylation deposited on numerous nucleo-cytoplasmic and mitochondrial proteins, including transcription factors, epigenetic regulators, and histones.
35470239	1	61	theme	Protein	132:138	arg1	deposited					208:216	a dynamic, nutrient-sensitive mono-glycosylation deposited	159:216	a dynamic, nutrient-sensitive mono-glycosylation deposited on numerous nucleo-cytoplasmic and mitochondrial proteins, including transcription factors, epigenetic regulators, and histones	159:344	Protein O-GlcNAcylation is a dynamic, nutrient-sensitive mono-glycosylation deposited on numerous nucleo-cytoplasmic and mitochondrial proteins, including transcription factors, epigenetic regulators, and histones.
35470239	1	61	theme	Protein	132:138	arg1	O-GlcNAcylation					140:154	Protein O-GlcNAcylation	132:154	Protein O-GlcNAcylation	132:154	Protein O-GlcNAcylation is a dynamic, nutrient-sensitive mono-glycosylation deposited on numerous nucleo-cytoplasmic and mitochondrial proteins, including transcription factors, epigenetic regulators, and histones.
35470239	4	62	theme	promoter	909:916	arg1	bivalency					918:926	promoter bivalency	909:926	promoter bivalency	909:926	This transcriptional de-repression is associated with reduced H3K27me3 and increased H3K4me3 levels on the promoters of these genes, perturbing promoter bivalency possibly through increased EZH2-Thr311 phosphorylation.
35470239	3	63	theme	factor	751:756	arg1	genes					758:762	key neurogenic transcription factor genes	722:762	key neurogenic transcription factor genes	722:762	Herein we recapitulated early human embryonic neurogenesis in cell culture and found that pharmacological up-regulation of O-GlcNAc levels during human embryonic stem cells' neuronal differentiation leads to up-regulation of key neurogenic transcription factor genes.
35470239	2	64	theme	epigenome	395:403	arg1	regulation					405:414	epigenome regulation	395:414	epigenome regulation in response to nutrient perturbations during development	395:471	However, the role of protein O-GlcNAcylation on epigenome regulation in response to nutrient perturbations during development is not well understood.
35470239	2	65	from	role	360:363	arg1	regulation					405:414	epigenome regulation	395:414	epigenome regulation in response to nutrient perturbations during development	395:471	However, the role of protein O-GlcNAcylation on epigenome regulation in response to nutrient perturbations during development is not well understood.
35470239	6	66	theme	O-GlcNAc	1197:1204	arg1	levels					1206:1211	similarly elevated O-GlcNAc levels	1178:1211	similarly elevated O-GlcNAc levels	1178:1211	Using an in vivo rat model of maternal hyperglycemia, we show similarly elevated O-GlcNAc levels and epigenetic dysregulations in the developing embryo brains because of hyperglycemia, whereas pharmacological inhibition of O-GlcNAc transferase (OGT) restored these molecular changes.
35470239	7	67	theme	O-GlcNAc	1434:1441	arg1	sensitivity					1452:1462	O-GlcNAc mediated sensitivity	1434:1462	O-GlcNAc mediated sensitivity of chromatin to nutrient status	1434:1494	Together, our results demonstrate O-GlcNAc mediated sensitivity of chromatin to nutrient status, and indicate how metabolic perturbations could affect gene expression during neurodevelopment.
35470239	3	68	theme	key	722:724	arg1	genes					758:762	key neurogenic transcription factor genes	722:762	key neurogenic transcription factor genes	722:762	Herein we recapitulated early human embryonic neurogenesis in cell culture and found that pharmacological up-regulation of O-GlcNAc levels during human embryonic stem cells' neuronal differentiation leads to up-regulation of key neurogenic transcription factor genes.
35470239	3	69	theme	O-GlcNAc	620:627	arg1	levels					629:634	O-GlcNAc levels	620:634	O-GlcNAc levels	620:634	Herein we recapitulated early human embryonic neurogenesis in cell culture and found that pharmacological up-regulation of O-GlcNAc levels during human embryonic stem cells' neuronal differentiation leads to up-regulation of key neurogenic transcription factor genes.
35470239	3	70	theme	embryonic	533:541	arg1	neurogenesis					543:554	early human embryonic neurogenesis	521:554	early human embryonic neurogenesis in cell culture	521:570	Herein we recapitulated early human embryonic neurogenesis in cell culture and found that pharmacological up-regulation of O-GlcNAc levels during human embryonic stem cells' neuronal differentiation leads to up-regulation of key neurogenic transcription factor genes.
35470239	1	71	theme	epigenetic	310:319	arg1	regulators					321:330	epigenetic regulators	310:330	epigenetic regulators	310:330	Protein O-GlcNAcylation is a dynamic, nutrient-sensitive mono-glycosylation deposited on numerous nucleo-cytoplasmic and mitochondrial proteins, including transcription factors, epigenetic regulators, and histones.
35470239	0	72	theme	epigenetic	79:88	arg1	mechanisms					90:99	epigenetic mechanisms	79:99	epigenetic mechanisms during embryonic neurogenesis	79:129	Nutrient sensitive protein O-GlcNAcylation modulates the transcriptome through epigenetic mechanisms during embryonic neurogenesis.
35470239	3	73	theme	embryonic	649:657	arg1	differentiation					680:694	human embryonic stem cells' neuronal differentiation	643:694	human embryonic stem cells' neuronal differentiation	643:694	Herein we recapitulated early human embryonic neurogenesis in cell culture and found that pharmacological up-regulation of O-GlcNAc levels during human embryonic stem cells' neuronal differentiation leads to up-regulation of key neurogenic transcription factor genes.
35470239	3	74	theme	neurogenic	726:735	arg1	genes					758:762	key neurogenic transcription factor genes	722:762	key neurogenic transcription factor genes	722:762	Herein we recapitulated early human embryonic neurogenesis in cell culture and found that pharmacological up-regulation of O-GlcNAc levels during human embryonic stem cells' neuronal differentiation leads to up-regulation of key neurogenic transcription factor genes.
35470239	1	75	theme	mono-glycosylation	189:206	arg1	deposited					208:216	a dynamic, nutrient-sensitive mono-glycosylation deposited	159:216	a dynamic, nutrient-sensitive mono-glycosylation deposited on numerous nucleo-cytoplasmic and mitochondrial proteins, including transcription factors, epigenetic regulators, and histones	159:344	Protein O-GlcNAcylation is a dynamic, nutrient-sensitive mono-glycosylation deposited on numerous nucleo-cytoplasmic and mitochondrial proteins, including transcription factors, epigenetic regulators, and histones.
35470239	1	75	theme	mono-glycosylation	189:206	arg1	O-GlcNAcylation					140:154	Protein O-GlcNAcylation	132:154	Protein O-GlcNAcylation	132:154	Protein O-GlcNAcylation is a dynamic, nutrient-sensitive mono-glycosylation deposited on numerous nucleo-cytoplasmic and mitochondrial proteins, including transcription factors, epigenetic regulators, and histones.
35470239	7	76	theme	mediated	1443:1450	arg1	sensitivity					1452:1462	O-GlcNAc mediated sensitivity	1434:1462	O-GlcNAc mediated sensitivity of chromatin to nutrient status	1434:1494	Together, our results demonstrate O-GlcNAc mediated sensitivity of chromatin to nutrient status, and indicate how metabolic perturbations could affect gene expression during neurodevelopment.
28739801	8	0	theme	sustained	1508:1516	arg1	elevation					1518:1526	sustained elevation	1508:1526	sustained elevation in O-GlcNAcylation coupled with increased OGA expression	1508:1583	In summary, sustained elevation in O-GlcNAcylation coupled with increased OGA expression reprograms energy metabolism, a finding that has potential implications for the etiology, development, and management of metabolic diseases.
28739801	5	1	contain	had	876:878	arg2	mitochondria					890:901	elongated mitochondria	880:901	elongated mitochondria	880:901	Cells with elevated O-GlcNAc levels had elongated mitochondria and increased mitochondrial membrane potential, and RNA-sequencing analysis indicated transcriptome reprogramming and down-regulation of the NRF2-mediated antioxidant response.
28739801	5	1	contain	had	876:878	arg2	potential					940:948	increased mitochondrial membrane potential	907:948	increased mitochondrial membrane potential	907:948	Cells with elevated O-GlcNAc levels had elongated mitochondria and increased mitochondrial membrane potential, and RNA-sequencing analysis indicated transcriptome reprogramming and down-regulation of the NRF2-mediated antioxidant response.
28739801	5	1	contain	had	876:878	arg1	Cells					840:844	Cells	840:844	Cells with elevated O-GlcNAc levels	840:874	Cells with elevated O-GlcNAc levels had elongated mitochondria and increased mitochondrial membrane potential, and RNA-sequencing analysis indicated transcriptome reprogramming and down-regulation of the NRF2-mediated antioxidant response.
28739801	8	2	theme	potential	1634:1642	arg1	implications					1644:1655	potential implications	1634:1655	potential implications for the etiology, development, and management of metabolic diseases	1634:1723	In summary, sustained elevation in O-GlcNAcylation coupled with increased OGA expression reprograms energy metabolism, a finding that has potential implications for the etiology, development, and management of metabolic diseases.
28739801	1	3	theme	chronic	174:180	arg1	diseases					182:189	chronic diseases	174:189	chronic diseases	174:189	Dysfunctional mitochondria and generation of reactive oxygen species (ROS) promote chronic diseases, which have spurred interest in the molecular mechanisms underlying these conditions.
28739801	3	4	from	alterations	590:600	arg1	O-GlcNAcylation					605:619	O-GlcNAcylation	605:619	O-GlcNAcylation	605:619	Here, we report that sustained alterations in O-GlcNAcylation either by pharmacological or genetic manipulation also alter metabolic function.
28739801	2	5	theme	mitochondrial	535:547	arg1	function					549:556	mitochondrial function	535:556	mitochondrial function	535:556	Previously, we have demonstrated that disruption of post-translational modification of proteins with β-linked N-acetylglucosamine (O-GlcNAcylation) via overexpression of the O-GlcNAc-regulating enzymes O-GlcNAc transferase (OGT) or O-GlcNAcase (OGA) impairs mitochondrial function.
28739801	6	6	theme	Sustained	1080:1088	arg1	O-GlcNAcylation					1090:1104	Sustained O-GlcNAcylation	1080:1104	Sustained O-GlcNAcylation in mouse brain and liver	1080:1129	Sustained O-GlcNAcylation in mouse brain and liver validated the metabolic phenotypes observed in the cells, and OGT knockdown in the liver elevated ROS levels, impaired respiration, and increased the NRF2 antioxidant response.
28739801	5	7	theme	antioxidant	1058:1068	arg1	response					1070:1077	the NRF2-mediated antioxidant response	1040:1077	the NRF2-mediated antioxidant response	1040:1077	Cells with elevated O-GlcNAc levels had elongated mitochondria and increased mitochondrial membrane potential, and RNA-sequencing analysis indicated transcriptome reprogramming and down-regulation of the NRF2-mediated antioxidant response.
28739801	5	8	theme	response	1070:1077	arg1	down-regulation					1021:1035	down-regulation	1021:1035	down-regulation	1021:1035	Cells with elevated O-GlcNAc levels had elongated mitochondria and increased mitochondrial membrane potential, and RNA-sequencing analysis indicated transcriptome reprogramming and down-regulation of the NRF2-mediated antioxidant response.
28739801	5	8	theme	response	1070:1077	arg1	reprogramming					1003:1015	transcriptome reprogramming	989:1015	transcriptome reprogramming	989:1015	Cells with elevated O-GlcNAc levels had elongated mitochondria and increased mitochondrial membrane potential, and RNA-sequencing analysis indicated transcriptome reprogramming and down-regulation of the NRF2-mediated antioxidant response.
28739801	8	9	theme	metabolic	1706:1714	arg1	diseases					1716:1723	metabolic diseases	1706:1723	metabolic diseases	1706:1723	In summary, sustained elevation in O-GlcNAcylation coupled with increased OGA expression reprograms energy metabolism, a finding that has potential implications for the etiology, development, and management of metabolic diseases.
28739801	7	10	theme	O-GlcNAc	1327:1334	arg1	levels					1336:1341	elevated O-GlcNAc levels	1318:1341	elevated O-GlcNAc levels	1318:1341	Moreover, elevated O-GlcNAc levels promoted weight loss and lowered respiration in mice and skewed the mice toward carbohydrate-dependent metabolism as determined by indirect calorimetry.
28739801	2	11	link	β-linked	378:385	arg1	O-GlcNAcylation					408:422	O-GlcNAcylation	408:422	O-GlcNAcylation	408:422	Previously, we have demonstrated that disruption of post-translational modification of proteins with β-linked N-acetylglucosamine (O-GlcNAcylation) via overexpression of the O-GlcNAc-regulating enzymes O-GlcNAc transferase (OGT) or O-GlcNAcase (OGA) impairs mitochondrial function.
28739801	2	11	link	β-linked	378:385	arg1	N-acetylglucosamine					387:405	β-linked N-acetylglucosamine	378:405	β-linked N-acetylglucosamine (O-GlcNAcylation)	378:423	Previously, we have demonstrated that disruption of post-translational modification of proteins with β-linked N-acetylglucosamine (O-GlcNAcylation) via overexpression of the O-GlcNAc-regulating enzymes O-GlcNAc transferase (OGT) or O-GlcNAcase (OGA) impairs mitochondrial function.
28739801	6	12	from	knockdown	1197:1205	arg1	liver					1214:1218	the liver	1210:1218	the liver	1210:1218	Sustained O-GlcNAcylation in mouse brain and liver validated the metabolic phenotypes observed in the cells, and OGT knockdown in the liver elevated ROS levels, impaired respiration, and increased the NRF2 antioxidant response.
28739801	8	13	theme	OGA	1570:1572	arg1	expression					1574:1583	increased OGA expression	1560:1583	increased OGA expression	1560:1583	In summary, sustained elevation in O-GlcNAcylation coupled with increased OGA expression reprograms energy metabolism, a finding that has potential implications for the etiology, development, and management of metabolic diseases.
28739801	6	14	from	O-GlcNAcylation	1090:1104	arg1	liver					1125:1129	liver	1125:1129	liver	1125:1129	Sustained O-GlcNAcylation in mouse brain and liver validated the metabolic phenotypes observed in the cells, and OGT knockdown in the liver elevated ROS levels, impaired respiration, and increased the NRF2 antioxidant response.
28739801	6	14	from	O-GlcNAcylation	1090:1104	arg1	brain					1115:1119	mouse brain	1109:1119	mouse brain	1109:1119	Sustained O-GlcNAcylation in mouse brain and liver validated the metabolic phenotypes observed in the cells, and OGT knockdown in the liver elevated ROS levels, impaired respiration, and increased the NRF2 antioxidant response.
28739801	4	15	theme	cellular	799:806	arg1	respiration					808:818	cellular respiration	799:818	cellular respiration	799:818	Sustained O-GlcNAc elevation in SH-SY5Y neuroblastoma cells increased OGA expression and reduced cellular respiration and ROS generation.
28739801	3	16	dep	O-GlcNAcylation	605:619	arg1	either					621:626	either	621:626	either	621:626	Here, we report that sustained alterations in O-GlcNAcylation either by pharmacological or genetic manipulation also alter metabolic function.
28739801	4	17	theme	SH-SY5Y	734:740	arg1	cells					756:760	SH-SY5Y neuroblastoma cells	734:760	SH-SY5Y neuroblastoma cells	734:760	Sustained O-GlcNAc elevation in SH-SY5Y neuroblastoma cells increased OGA expression and reduced cellular respiration and ROS generation.
28739801	1	18	theme	Dysfunctional	91:103	arg1	mitochondria					105:116	Dysfunctional mitochondria	91:116	Dysfunctional mitochondria	91:116	Dysfunctional mitochondria and generation of reactive oxygen species (ROS) promote chronic diseases, which have spurred interest in the molecular mechanisms underlying these conditions.
28739801	2	19	theme	O-GlcNAc-regulating	451:469	arg1	O-GlcNAcase					509:519	O-GlcNAcase	509:519	O-GlcNAcase (OGA)	509:525	Previously, we have demonstrated that disruption of post-translational modification of proteins with β-linked N-acetylglucosamine (O-GlcNAcylation) via overexpression of the O-GlcNAc-regulating enzymes O-GlcNAc transferase (OGT) or O-GlcNAcase (OGA) impairs mitochondrial function.
28739801	2	19	theme	O-GlcNAc-regulating	451:469	arg1	transferase					488:498	O-GlcNAc transferase	479:498	O-GlcNAc transferase (OGT)	479:504	Previously, we have demonstrated that disruption of post-translational modification of proteins with β-linked N-acetylglucosamine (O-GlcNAcylation) via overexpression of the O-GlcNAc-regulating enzymes O-GlcNAc transferase (OGT) or O-GlcNAcase (OGA) impairs mitochondrial function.
28739801	2	19	theme	O-GlcNAc-regulating	451:469	arg1	enzymes					471:477	the O-GlcNAc-regulating enzymes	447:477	the O-GlcNAc-regulating enzymes O-GlcNAc transferase (OGT) or O-GlcNAcase (OGA)	447:525	Previously, we have demonstrated that disruption of post-translational modification of proteins with β-linked N-acetylglucosamine (O-GlcNAcylation) via overexpression of the O-GlcNAc-regulating enzymes O-GlcNAc transferase (OGT) or O-GlcNAcase (OGA) impairs mitochondrial function.
28739801	5	20	theme	elevated	851:858	arg1	levels					869:874	elevated O-GlcNAc levels	851:874	elevated O-GlcNAc levels	851:874	Cells with elevated O-GlcNAc levels had elongated mitochondria and increased mitochondrial membrane potential, and RNA-sequencing analysis indicated transcriptome reprogramming and down-regulation of the NRF2-mediated antioxidant response.
28739801	8	21	from	elevation	1518:1526	arg1	O-GlcNAcylation					1531:1545	O-GlcNAcylation	1531:1545	O-GlcNAcylation	1531:1545	In summary, sustained elevation in O-GlcNAcylation coupled with increased OGA expression reprograms energy metabolism, a finding that has potential implications for the etiology, development, and management of metabolic diseases.
28739801	7	22	theme	weight	1352:1357	arg1	loss					1359:1362	weight loss	1352:1362	weight loss	1352:1362	Moreover, elevated O-GlcNAc levels promoted weight loss and lowered respiration in mice and skewed the mice toward carbohydrate-dependent metabolism as determined by indirect calorimetry.
28739801	4	23	theme	neuroblastoma	742:754	arg1	cells					756:760	SH-SY5Y neuroblastoma cells	734:760	SH-SY5Y neuroblastoma cells	734:760	Sustained O-GlcNAc elevation in SH-SY5Y neuroblastoma cells increased OGA expression and reduced cellular respiration and ROS generation.
28739801	5	24	theme	membrane	931:938	arg1	potential					940:948	increased mitochondrial membrane potential	907:948	increased mitochondrial membrane potential	907:948	Cells with elevated O-GlcNAc levels had elongated mitochondria and increased mitochondrial membrane potential, and RNA-sequencing analysis indicated transcriptome reprogramming and down-regulation of the NRF2-mediated antioxidant response.
28739801	5	25	theme	elongated	880:888	arg1	mitochondria					890:901	elongated mitochondria	880:901	elongated mitochondria	880:901	Cells with elevated O-GlcNAc levels had elongated mitochondria and increased mitochondrial membrane potential, and RNA-sequencing analysis indicated transcriptome reprogramming and down-regulation of the NRF2-mediated antioxidant response.
28739801	7	26	theme	indirect	1474:1481	arg1	calorimetry					1483:1493	indirect calorimetry	1474:1493	indirect calorimetry	1474:1493	Moreover, elevated O-GlcNAc levels promoted weight loss and lowered respiration in mice and skewed the mice toward carbohydrate-dependent metabolism as determined by indirect calorimetry.
28739801	7	27	theme	carbohydrate-dependent	1423:1444	arg1	metabolism					1446:1455	carbohydrate-dependent metabolism	1423:1455	carbohydrate-dependent metabolism	1423:1455	Moreover, elevated O-GlcNAc levels promoted weight loss and lowered respiration in mice and skewed the mice toward carbohydrate-dependent metabolism as determined by indirect calorimetry.
28739801	3	28	theme	pharmacological	631:645	arg1	manipulation					658:669	pharmacological or genetic manipulation	631:669	pharmacological or genetic manipulation	631:669	Here, we report that sustained alterations in O-GlcNAcylation either by pharmacological or genetic manipulation also alter metabolic function.
28739801	4	29	theme	OGA	772:774	arg1	expression					776:785	OGA expression	772:785	OGA expression	772:785	Sustained O-GlcNAc elevation in SH-SY5Y neuroblastoma cells increased OGA expression and reduced cellular respiration and ROS generation.
28739801	0	30	theme	Sustained	0:8	arg1	O-GlcNAcylation					10:24	Sustained O-GlcNAcylation	0:24	Sustained O-GlcNAcylation	0:24	Sustained O-GlcNAcylation reprograms mitochondrial function to regulate energy metabolism.
28739801	4	31	theme	ROS	824:826	arg1	generation					828:837	ROS generation	824:837	ROS generation	824:837	Sustained O-GlcNAc elevation in SH-SY5Y neuroblastoma cells increased OGA expression and reduced cellular respiration and ROS generation.
28739801	2	32	theme	modification	348:359	arg1	disruption					315:324	disruption	315:324	disruption of post-translational modification of proteins with β-linked N-acetylglucosamine (O-GlcNAcylation) via overexpression of the O-GlcNAc-regulating enzymes O-GlcNAc transferase (OGT) or O-GlcNAcase (OGA)	315:525	Previously, we have demonstrated that disruption of post-translational modification of proteins with β-linked N-acetylglucosamine (O-GlcNAcylation) via overexpression of the O-GlcNAc-regulating enzymes O-GlcNAc transferase (OGT) or O-GlcNAcase (OGA) impairs mitochondrial function.
28739801	6	33	theme	ROS	1229:1231	arg1	levels					1233:1238	ROS levels	1229:1238	ROS levels	1229:1238	Sustained O-GlcNAcylation in mouse brain and liver validated the metabolic phenotypes observed in the cells, and OGT knockdown in the liver elevated ROS levels, impaired respiration, and increased the NRF2 antioxidant response.
28739801	0	34	theme	mitochondrial	37:49	arg1	function					51:58	mitochondrial function	37:58	mitochondrial function	37:58	Sustained O-GlcNAcylation reprograms mitochondrial function to regulate energy metabolism.
28739801	6	35	theme	metabolic	1145:1153	arg1	phenotypes					1155:1164	the metabolic phenotypes	1141:1164	the metabolic phenotypes observed in the cells	1141:1186	Sustained O-GlcNAcylation in mouse brain and liver validated the metabolic phenotypes observed in the cells, and OGT knockdown in the liver elevated ROS levels, impaired respiration, and increased the NRF2 antioxidant response.
28739801	2	36	theme	post-translational	329:346	arg1	modification					348:359	post-translational modification	329:359	post-translational modification of proteins with β-linked N-acetylglucosamine (O-GlcNAcylation)	329:423	Previously, we have demonstrated that disruption of post-translational modification of proteins with β-linked N-acetylglucosamine (O-GlcNAcylation) via overexpression of the O-GlcNAc-regulating enzymes O-GlcNAc transferase (OGT) or O-GlcNAcase (OGA) impairs mitochondrial function.
28739801	5	37	theme	RNA-sequencing	955:968	arg1	analysis					970:977	RNA-sequencing analysis	955:977	RNA-sequencing analysis	955:977	Cells with elevated O-GlcNAc levels had elongated mitochondria and increased mitochondrial membrane potential, and RNA-sequencing analysis indicated transcriptome reprogramming and down-regulation of the NRF2-mediated antioxidant response.
28739801	8	38	theme	increased	1560:1568	arg1	expression					1574:1583	increased OGA expression	1560:1583	increased OGA expression	1560:1583	In summary, sustained elevation in O-GlcNAcylation coupled with increased OGA expression reprograms energy metabolism, a finding that has potential implications for the etiology, development, and management of metabolic diseases.
28739801	3	39	theme	sustained	580:588	arg1	alterations					590:600	sustained alterations	580:600	sustained alterations in O-GlcNAcylation either by pharmacological or genetic manipulation	580:669	Here, we report that sustained alterations in O-GlcNAcylation either by pharmacological or genetic manipulation also alter metabolic function.
28739801	1	40	theme	reactive	136:143	arg1	ROS					161:163	ROS	161:163	ROS	161:163	Dysfunctional mitochondria and generation of reactive oxygen species (ROS) promote chronic diseases, which have spurred interest in the molecular mechanisms underlying these conditions.
28739801	1	40	theme	reactive	136:143	arg1	species					152:158	reactive oxygen species	136:158	reactive oxygen species (ROS)	136:164	Dysfunctional mitochondria and generation of reactive oxygen species (ROS) promote chronic diseases, which have spurred interest in the molecular mechanisms underlying these conditions.
28739801	4	41	from	elevation	721:729	arg1	cells					756:760	SH-SY5Y neuroblastoma cells	734:760	SH-SY5Y neuroblastoma cells	734:760	Sustained O-GlcNAc elevation in SH-SY5Y neuroblastoma cells increased OGA expression and reduced cellular respiration and ROS generation.
28739801	4	42	theme	O-GlcNAc	712:719	arg1	elevation					721:729	Sustained O-GlcNAc elevation	702:729	Sustained O-GlcNAc elevation in SH-SY5Y neuroblastoma cells	702:760	Sustained O-GlcNAc elevation in SH-SY5Y neuroblastoma cells increased OGA expression and reduced cellular respiration and ROS generation.
28739801	2	43	theme	β-linked	378:385	arg1	O-GlcNAcylation					408:422	O-GlcNAcylation	408:422	O-GlcNAcylation	408:422	Previously, we have demonstrated that disruption of post-translational modification of proteins with β-linked N-acetylglucosamine (O-GlcNAcylation) via overexpression of the O-GlcNAc-regulating enzymes O-GlcNAc transferase (OGT) or O-GlcNAcase (OGA) impairs mitochondrial function.
28739801	2	43	theme	β-linked	378:385	arg1	N-acetylglucosamine					387:405	β-linked N-acetylglucosamine	378:405	β-linked N-acetylglucosamine (O-GlcNAcylation)	378:423	Previously, we have demonstrated that disruption of post-translational modification of proteins with β-linked N-acetylglucosamine (O-GlcNAcylation) via overexpression of the O-GlcNAc-regulating enzymes O-GlcNAc transferase (OGT) or O-GlcNAcase (OGA) impairs mitochondrial function.
28739801	2	44	with	proteins	364:371	arg1	O-GlcNAcylation					408:422	O-GlcNAcylation	408:422	O-GlcNAcylation	408:422	Previously, we have demonstrated that disruption of post-translational modification of proteins with β-linked N-acetylglucosamine (O-GlcNAcylation) via overexpression of the O-GlcNAc-regulating enzymes O-GlcNAc transferase (OGT) or O-GlcNAcase (OGA) impairs mitochondrial function.
28739801	2	44	with	proteins	364:371	arg1	N-acetylglucosamine					387:405	β-linked N-acetylglucosamine	378:405	β-linked N-acetylglucosamine (O-GlcNAcylation)	378:423	Previously, we have demonstrated that disruption of post-translational modification of proteins with β-linked N-acetylglucosamine (O-GlcNAcylation) via overexpression of the O-GlcNAc-regulating enzymes O-GlcNAc transferase (OGT) or O-GlcNAcase (OGA) impairs mitochondrial function.
28739801	7	45	from	respiration	1376:1386	arg1	mice					1391:1394	mice	1391:1394	mice	1391:1394	Moreover, elevated O-GlcNAc levels promoted weight loss and lowered respiration in mice and skewed the mice toward carbohydrate-dependent metabolism as determined by indirect calorimetry.
28739801	7	45	from	respiration	1376:1386	arg1	mice					1411:1414	the mice	1407:1414	skewed the mice	1400:1414	Moreover, elevated O-GlcNAc levels promoted weight loss and lowered respiration in mice and skewed the mice toward carbohydrate-dependent metabolism as determined by indirect calorimetry.
28739801	2	46	theme	O-GlcNAc	479:486	arg1	OGT					501:503	OGT	501:503	OGT	501:503	Previously, we have demonstrated that disruption of post-translational modification of proteins with β-linked N-acetylglucosamine (O-GlcNAcylation) via overexpression of the O-GlcNAc-regulating enzymes O-GlcNAc transferase (OGT) or O-GlcNAcase (OGA) impairs mitochondrial function.
28739801	2	46	theme	O-GlcNAc	479:486	arg1	transferase					488:498	O-GlcNAc transferase	479:498	O-GlcNAc transferase (OGT)	479:504	Previously, we have demonstrated that disruption of post-translational modification of proteins with β-linked N-acetylglucosamine (O-GlcNAcylation) via overexpression of the O-GlcNAc-regulating enzymes O-GlcNAc transferase (OGT) or O-GlcNAcase (OGA) impairs mitochondrial function.
28739801	2	46	theme	O-GlcNAc	479:486	arg1	enzymes					471:477	the O-GlcNAc-regulating enzymes	447:477	the O-GlcNAc-regulating enzymes O-GlcNAc transferase (OGT) or O-GlcNAcase (OGA)	447:525	Previously, we have demonstrated that disruption of post-translational modification of proteins with β-linked N-acetylglucosamine (O-GlcNAcylation) via overexpression of the O-GlcNAc-regulating enzymes O-GlcNAc transferase (OGT) or O-GlcNAcase (OGA) impairs mitochondrial function.
28739801	7	47	theme	elevated	1318:1325	arg1	levels					1336:1341	elevated O-GlcNAc levels	1318:1341	elevated O-GlcNAc levels	1318:1341	Moreover, elevated O-GlcNAc levels promoted weight loss and lowered respiration in mice and skewed the mice toward carbohydrate-dependent metabolism as determined by indirect calorimetry.
28739801	8	48	dep	etiology	1665:1672	arg1	the					1661:1663	the	1661:1663	the	1661:1663	In summary, sustained elevation in O-GlcNAcylation coupled with increased OGA expression reprograms energy metabolism, a finding that has potential implications for the etiology, development, and management of metabolic diseases.
28739801	2	49	dep	enzymes	471:477	arg1	OGA					522:524	OGA	522:524	OGA	522:524	Previously, we have demonstrated that disruption of post-translational modification of proteins with β-linked N-acetylglucosamine (O-GlcNAcylation) via overexpression of the O-GlcNAc-regulating enzymes O-GlcNAc transferase (OGT) or O-GlcNAcase (OGA) impairs mitochondrial function.
28739801	2	49	dep	enzymes	471:477	arg1	OGT					501:503	OGT	501:503	OGT	501:503	Previously, we have demonstrated that disruption of post-translational modification of proteins with β-linked N-acetylglucosamine (O-GlcNAcylation) via overexpression of the O-GlcNAc-regulating enzymes O-GlcNAc transferase (OGT) or O-GlcNAcase (OGA) impairs mitochondrial function.
28739801	2	49	dep	enzymes	471:477	arg1	O-GlcNAcase					509:519	O-GlcNAcase	509:519	O-GlcNAcase (OGA)	509:525	Previously, we have demonstrated that disruption of post-translational modification of proteins with β-linked N-acetylglucosamine (O-GlcNAcylation) via overexpression of the O-GlcNAc-regulating enzymes O-GlcNAc transferase (OGT) or O-GlcNAcase (OGA) impairs mitochondrial function.
28739801	2	49	dep	enzymes	471:477	arg1	transferase					488:498	O-GlcNAc transferase	479:498	O-GlcNAc transferase (OGT)	479:504	Previously, we have demonstrated that disruption of post-translational modification of proteins with β-linked N-acetylglucosamine (O-GlcNAcylation) via overexpression of the O-GlcNAc-regulating enzymes O-GlcNAc transferase (OGT) or O-GlcNAcase (OGA) impairs mitochondrial function.
28739801	2	49	dep	enzymes	471:477	arg1	enzymes					471:477	the O-GlcNAc-regulating enzymes	447:477	the O-GlcNAc-regulating enzymes O-GlcNAc transferase (OGT) or O-GlcNAcase (OGA)	447:525	Previously, we have demonstrated that disruption of post-translational modification of proteins with β-linked N-acetylglucosamine (O-GlcNAcylation) via overexpression of the O-GlcNAc-regulating enzymes O-GlcNAc transferase (OGT) or O-GlcNAcase (OGA) impairs mitochondrial function.
28739801	5	50	theme	transcriptome	989:1001	arg1	reprogramming					1003:1015	transcriptome reprogramming	989:1015	transcriptome reprogramming	989:1015	Cells with elevated O-GlcNAc levels had elongated mitochondria and increased mitochondrial membrane potential, and RNA-sequencing analysis indicated transcriptome reprogramming and down-regulation of the NRF2-mediated antioxidant response.
28739801	1	51	theme	molecular	227:235	arg1	mechanisms					237:246	the molecular mechanisms	223:246	the molecular mechanisms underlying these conditions	223:274	Dysfunctional mitochondria and generation of reactive oxygen species (ROS) promote chronic diseases, which have spurred interest in the molecular mechanisms underlying these conditions.
28739801	0	52	theme	energy	72:77	arg1	metabolism					79:88	energy metabolism	72:88	energy metabolism	72:88	Sustained O-GlcNAcylation reprograms mitochondrial function to regulate energy metabolism.
28739801	7	53	theme	skewed	1400:1405	arg1	mice					1411:1414	the mice	1407:1414	skewed the mice	1400:1414	Moreover, elevated O-GlcNAc levels promoted weight loss and lowered respiration in mice and skewed the mice toward carbohydrate-dependent metabolism as determined by indirect calorimetry.
28739801	3	54	theme	genetic	650:656	arg1	manipulation					658:669	pharmacological or genetic manipulation	631:669	pharmacological or genetic manipulation	631:669	Here, we report that sustained alterations in O-GlcNAcylation either by pharmacological or genetic manipulation also alter metabolic function.
28739801	6	55	theme	antioxidant	1286:1296	arg1	response					1298:1305	the NRF2 antioxidant response	1277:1305	the NRF2 antioxidant response	1277:1305	Sustained O-GlcNAcylation in mouse brain and liver validated the metabolic phenotypes observed in the cells, and OGT knockdown in the liver elevated ROS levels, impaired respiration, and increased the NRF2 antioxidant response.
28739801	1	56	theme	oxygen	145:150	arg1	ROS					161:163	ROS	161:163	ROS	161:163	Dysfunctional mitochondria and generation of reactive oxygen species (ROS) promote chronic diseases, which have spurred interest in the molecular mechanisms underlying these conditions.
28739801	1	56	theme	oxygen	145:150	arg1	species					152:158	reactive oxygen species	136:158	reactive oxygen species (ROS)	136:164	Dysfunctional mitochondria and generation of reactive oxygen species (ROS) promote chronic diseases, which have spurred interest in the molecular mechanisms underlying these conditions.
28739801	5	57	theme	mitochondrial	917:929	arg1	potential					940:948	increased mitochondrial membrane potential	907:948	increased mitochondrial membrane potential	907:948	Cells with elevated O-GlcNAc levels had elongated mitochondria and increased mitochondrial membrane potential, and RNA-sequencing analysis indicated transcriptome reprogramming and down-regulation of the NRF2-mediated antioxidant response.
28739801	5	58	with	Cells	840:844	arg1	levels					869:874	elevated O-GlcNAc levels	851:874	elevated O-GlcNAc levels	851:874	Cells with elevated O-GlcNAc levels had elongated mitochondria and increased mitochondrial membrane potential, and RNA-sequencing analysis indicated transcriptome reprogramming and down-regulation of the NRF2-mediated antioxidant response.
28739801	1	59	theme	species	152:158	arg1	generation					122:131	generation	122:131	generation	122:131	Dysfunctional mitochondria and generation of reactive oxygen species (ROS) promote chronic diseases, which have spurred interest in the molecular mechanisms underlying these conditions.
28739801	1	59	theme	species	152:158	arg1	mitochondria					105:116	Dysfunctional mitochondria	91:116	Dysfunctional mitochondria	91:116	Dysfunctional mitochondria and generation of reactive oxygen species (ROS) promote chronic diseases, which have spurred interest in the molecular mechanisms underlying these conditions.
28739801	6	60	theme	mouse	1109:1113	arg1	brain					1115:1119	mouse brain	1109:1119	mouse brain	1109:1119	Sustained O-GlcNAcylation in mouse brain and liver validated the metabolic phenotypes observed in the cells, and OGT knockdown in the liver elevated ROS levels, impaired respiration, and increased the NRF2 antioxidant response.
28739801	8	61	theme	energy	1596:1601	arg1	metabolism					1603:1612	energy metabolism	1596:1612	energy metabolism	1596:1612	In summary, sustained elevation in O-GlcNAcylation coupled with increased OGA expression reprograms energy metabolism, a finding that has potential implications for the etiology, development, and management of metabolic diseases.
28739801	8	61	theme	energy	1596:1601	arg1	finding					1617:1623	a finding	1615:1623	a finding that has potential implications for the etiology, development, and management of metabolic diseases	1615:1723	In summary, sustained elevation in O-GlcNAcylation coupled with increased OGA expression reprograms energy metabolism, a finding that has potential implications for the etiology, development, and management of metabolic diseases.
28739801	6	62	theme	NRF2	1281:1284	arg1	response					1298:1305	the NRF2 antioxidant response	1277:1305	the NRF2 antioxidant response	1277:1305	Sustained O-GlcNAcylation in mouse brain and liver validated the metabolic phenotypes observed in the cells, and OGT knockdown in the liver elevated ROS levels, impaired respiration, and increased the NRF2 antioxidant response.
28739801	6	63	located	observed	1166:1173	arg2	phenotypes					1155:1164	the metabolic phenotypes	1141:1164	the metabolic phenotypes observed in the cells	1141:1186	Sustained O-GlcNAcylation in mouse brain and liver validated the metabolic phenotypes observed in the cells, and OGT knockdown in the liver elevated ROS levels, impaired respiration, and increased the NRF2 antioxidant response.
28739801	6	63	located	observed	1166:1173	arg1	cells					1182:1186	the cells	1178:1186	the cells	1178:1186	Sustained O-GlcNAcylation in mouse brain and liver validated the metabolic phenotypes observed in the cells, and OGT knockdown in the liver elevated ROS levels, impaired respiration, and increased the NRF2 antioxidant response.
28739801	2	64	theme	proteins	364:371	arg1	modification					348:359	post-translational modification	329:359	post-translational modification of proteins with β-linked N-acetylglucosamine (O-GlcNAcylation)	329:423	Previously, we have demonstrated that disruption of post-translational modification of proteins with β-linked N-acetylglucosamine (O-GlcNAcylation) via overexpression of the O-GlcNAc-regulating enzymes O-GlcNAc transferase (OGT) or O-GlcNAcase (OGA) impairs mitochondrial function.
28739801	6	65	theme	OGT	1193:1195	arg1	knockdown					1197:1205	OGT knockdown	1193:1205	OGT knockdown in the liver	1193:1218	Sustained O-GlcNAcylation in mouse brain and liver validated the metabolic phenotypes observed in the cells, and OGT knockdown in the liver elevated ROS levels, impaired respiration, and increased the NRF2 antioxidant response.
28739801	5	66	theme	O-GlcNAc	860:867	arg1	levels					869:874	elevated O-GlcNAc levels	851:874	elevated O-GlcNAc levels	851:874	Cells with elevated O-GlcNAc levels had elongated mitochondria and increased mitochondrial membrane potential, and RNA-sequencing analysis indicated transcriptome reprogramming and down-regulation of the NRF2-mediated antioxidant response.
28739801	2	67	theme	enzymes	471:477	arg1	overexpression					429:442	overexpression	429:442	overexpression of the O-GlcNAc-regulating enzymes O-GlcNAc transferase (OGT) or O-GlcNAcase (OGA)	429:525	Previously, we have demonstrated that disruption of post-translational modification of proteins with β-linked N-acetylglucosamine (O-GlcNAcylation) via overexpression of the O-GlcNAc-regulating enzymes O-GlcNAc transferase (OGT) or O-GlcNAcase (OGA) impairs mitochondrial function.
28739801	3	68	theme	metabolic	682:690	arg1	function					692:699	metabolic function	682:699	metabolic function	682:699	Here, we report that sustained alterations in O-GlcNAcylation either by pharmacological or genetic manipulation also alter metabolic function.
28739801	8	69	contain	has	1630:1632	arg2	implications					1644:1655	potential implications	1634:1655	potential implications for the etiology, development, and management of metabolic diseases	1634:1723	In summary, sustained elevation in O-GlcNAcylation coupled with increased OGA expression reprograms energy metabolism, a finding that has potential implications for the etiology, development, and management of metabolic diseases.
28739801	8	69	contain	has	1630:1632	arg1	metabolism					1603:1612	energy metabolism	1596:1612	energy metabolism	1596:1612	In summary, sustained elevation in O-GlcNAcylation coupled with increased OGA expression reprograms energy metabolism, a finding that has potential implications for the etiology, development, and management of metabolic diseases.
28739801	8	69	contain	has	1630:1632	arg1	finding					1617:1623	a finding	1615:1623	a finding that has potential implications for the etiology, development, and management of metabolic diseases	1615:1723	In summary, sustained elevation in O-GlcNAcylation coupled with increased OGA expression reprograms energy metabolism, a finding that has potential implications for the etiology, development, and management of metabolic diseases.
28739801	4	70	theme	Sustained	702:710	arg1	elevation					721:729	Sustained O-GlcNAc elevation	702:729	Sustained O-GlcNAc elevation in SH-SY5Y neuroblastoma cells	702:760	Sustained O-GlcNAc elevation in SH-SY5Y neuroblastoma cells increased OGA expression and reduced cellular respiration and ROS generation.
28739801	5	71	theme	increased	907:915	arg1	potential					940:948	increased mitochondrial membrane potential	907:948	increased mitochondrial membrane potential	907:948	Cells with elevated O-GlcNAc levels had elongated mitochondria and increased mitochondrial membrane potential, and RNA-sequencing analysis indicated transcriptome reprogramming and down-regulation of the NRF2-mediated antioxidant response.
28739801	5	72	theme	NRF2-mediated	1044:1056	arg1	response					1070:1077	the NRF2-mediated antioxidant response	1040:1077	the NRF2-mediated antioxidant response	1040:1077	Cells with elevated O-GlcNAc levels had elongated mitochondria and increased mitochondrial membrane potential, and RNA-sequencing analysis indicated transcriptome reprogramming and down-regulation of the NRF2-mediated antioxidant response.
28739801	8	73	theme	diseases	1716:1723	arg1	development					1675:1685	development	1675:1685	development	1675:1685	In summary, sustained elevation in O-GlcNAcylation coupled with increased OGA expression reprograms energy metabolism, a finding that has potential implications for the etiology, development, and management of metabolic diseases.
28739801	8	73	theme	diseases	1716:1723	arg1	management					1692:1701	management	1692:1701	management	1692:1701	In summary, sustained elevation in O-GlcNAcylation coupled with increased OGA expression reprograms energy metabolism, a finding that has potential implications for the etiology, development, and management of metabolic diseases.
28739801	8	73	theme	diseases	1716:1723	arg1	etiology					1665:1672	etiology	1665:1672	etiology	1665:1672	In summary, sustained elevation in O-GlcNAcylation coupled with increased OGA expression reprograms energy metabolism, a finding that has potential implications for the etiology, development, and management of metabolic diseases.
17707335	5	0	from	site	876:879	arg1	Runx2					913:917	Runx2	913:917	Runx2	913:917	By conducting activity assays of the osteocalcin promoter and transcription factor, we found that the OSE2 site in the osteocalcin promoter and Runx2 were important for increased osteocalcin promoter activity by PUGNAc.
17707335	5	0	from	site	876:879	arg1	promoter					900:907	the osteocalcin promoter	884:907	the osteocalcin promoter	884:907	By conducting activity assays of the osteocalcin promoter and transcription factor, we found that the OSE2 site in the osteocalcin promoter and Runx2 were important for increased osteocalcin promoter activity by PUGNAc.
17707335	2	1	from	activity	463:470	arg1	differentiation					488:502	osteoblastic differentiation	475:502	osteoblastic differentiation	475:502	Here, we demonstrate that O-GlcNAc modification regulates the expression of osteocalcin, an osteoblast-specific marker, via Runx2 transcriptional activity in osteoblastic differentiation.
17707335	2	2	theme	osteocalcin	393:403	arg1	expression					379:388	the expression	375:388	the expression of osteocalcin, an osteoblast-specific marker,	375:435	Here, we demonstrate that O-GlcNAc modification regulates the expression of osteocalcin, an osteoblast-specific marker, via Runx2 transcriptional activity in osteoblastic differentiation.
17707335	1	3	theme	proteins	275:282	arg1	regulation					214:223	the regulation	210:223	the regulation of protein stability	210:244	O-Linked beta-N-acetylglucosamine (O-GlcNAc) modification, a reversible post-translational modification, has been implicated in the regulation of protein stability, subcellular localization of proteins and protein-protein interaction.
17707335	1	3	theme	proteins	275:282	arg1	interaction					304:314	protein-protein interaction	288:314	protein-protein interaction	288:314	O-Linked beta-N-acetylglucosamine (O-GlcNAc) modification, a reversible post-translational modification, has been implicated in the regulation of protein stability, subcellular localization of proteins and protein-protein interaction.
17707335	1	3	theme	proteins	275:282	arg1	localization					259:270	subcellular localization	247:270	subcellular localization of proteins	247:282	O-Linked beta-N-acetylglucosamine (O-GlcNAc) modification, a reversible post-translational modification, has been implicated in the regulation of protein stability, subcellular localization of proteins and protein-protein interaction.
17707335	5	4	theme	osteocalcin	806:816	arg1	promoter					818:825	the osteocalcin promoter	802:825	the osteocalcin promoter	802:825	By conducting activity assays of the osteocalcin promoter and transcription factor, we found that the OSE2 site in the osteocalcin promoter and Runx2 were important for increased osteocalcin promoter activity by PUGNAc.
17707335	1	5	theme	O-Linked	82:89	arg1	beta-N-acetylglucosamine					91:114	O-Linked beta-N-acetylglucosamine	82:114	O-Linked beta-N-acetylglucosamine (O-GlcNAc) modification	82:138	O-Linked beta-N-acetylglucosamine (O-GlcNAc) modification, a reversible post-translational modification, has been implicated in the regulation of protein stability, subcellular localization of proteins and protein-protein interaction.
17707335	1	5	theme	O-Linked	82:89	arg1	O-GlcNAc					117:124	O-GlcNAc	117:124	O-GlcNAc	117:124	O-Linked beta-N-acetylglucosamine (O-GlcNAc) modification, a reversible post-translational modification, has been implicated in the regulation of protein stability, subcellular localization of proteins and protein-protein interaction.
17707335	7	6	theme	new	1194:1196	arg1	mode					1198:1201	a new mode	1192:1201	a new mode of osteoblastic differentiation regulation	1192:1244	Thus, these data provide evidence that O-GlcNAc modification may be a new mode of osteoblastic differentiation regulation.
17707335	7	6	theme	new	1194:1196	arg1	modification					1172:1183	O-GlcNAc modification	1163:1183	O-GlcNAc modification	1163:1183	Thus, these data provide evidence that O-GlcNAc modification may be a new mode of osteoblastic differentiation regulation.
17707335	1	7	theme	protein-protein	288:302	arg1	interaction					304:314	protein-protein interaction	288:314	protein-protein interaction	288:314	O-Linked beta-N-acetylglucosamine (O-GlcNAc) modification, a reversible post-translational modification, has been implicated in the regulation of protein stability, subcellular localization of proteins and protein-protein interaction.
17707335	5	8	theme	transcription	831:843	arg1	factor					845:850	transcription factor	831:850	transcription factor	831:850	By conducting activity assays of the osteocalcin promoter and transcription factor, we found that the OSE2 site in the osteocalcin promoter and Runx2 were important for increased osteocalcin promoter activity by PUGNAc.
17707335	6	9	theme	gene	1106:1109	arg1	osteocalcin					1111:1121	its target gene osteocalcin	1095:1121	its target gene osteocalcin	1095:1121	Furthermore, PUGNAc led to increased O-GlcNAc modification of Runx2, which regulated the transcription of its target gene osteocalcin.
17707335	3	10	theme	Protein-associated	505:522	arg1	O-GlcNAc					524:531	Protein-associated O-GlcNAc	505:531	Protein-associated O-GlcNAc	505:531	Protein-associated O-GlcNAc was increased during osteoblastic differentiation in MC3T3-E1 preosteoblasts.
17707335	7	11	theme	O-GlcNAc	1163:1170	arg1	mode					1198:1201	a new mode	1192:1201	a new mode of osteoblastic differentiation regulation	1192:1244	Thus, these data provide evidence that O-GlcNAc modification may be a new mode of osteoblastic differentiation regulation.
17707335	7	11	theme	O-GlcNAc	1163:1170	arg1	modification					1172:1183	O-GlcNAc modification	1163:1183	O-GlcNAc modification	1163:1183	Thus, these data provide evidence that O-GlcNAc modification may be a new mode of osteoblastic differentiation regulation.
17707335	3	12	from	differentiation	567:581	arg1	preosteoblasts					595:608	MC3T3-E1 preosteoblasts	586:608	MC3T3-E1 preosteoblasts	586:608	Protein-associated O-GlcNAc was increased during osteoblastic differentiation in MC3T3-E1 preosteoblasts.
17707335	2	13	theme	O-GlcNAc	343:350	arg1	modification					352:363	O-GlcNAc modification	343:363	O-GlcNAc modification	343:363	Here, we demonstrate that O-GlcNAc modification regulates the expression of osteocalcin, an osteoblast-specific marker, via Runx2 transcriptional activity in osteoblastic differentiation.
17707335	5	14	theme	osteocalcin	948:958	arg1	activity					969:976	increased osteocalcin promoter activity	938:976	increased osteocalcin promoter activity by PUGNAc	938:986	By conducting activity assays of the osteocalcin promoter and transcription factor, we found that the OSE2 site in the osteocalcin promoter and Runx2 were important for increased osteocalcin promoter activity by PUGNAc.
17707335	0	15	theme	O-GlcNAc	0:7	arg1	modification					9:20	O-GlcNAc modification	0:20	O-GlcNAc modification	0:20	O-GlcNAc modification modulates the expression of osteocalcin via OSE2 and Runx2.
17707335	1	16	theme	beta-N-acetylglucosamine	91:114	arg1	modification					173:184	a reversible post-translational modification	141:184	a reversible post-translational modification	141:184	O-Linked beta-N-acetylglucosamine (O-GlcNAc) modification, a reversible post-translational modification, has been implicated in the regulation of protein stability, subcellular localization of proteins and protein-protein interaction.
17707335	1	16	theme	beta-N-acetylglucosamine	91:114	arg1	modification					127:138	O-Linked beta-N-acetylglucosamine (O-GlcNAc) modification	82:138	O-Linked beta-N-acetylglucosamine (O-GlcNAc) modification	82:138	O-Linked beta-N-acetylglucosamine (O-GlcNAc) modification, a reversible post-translational modification, has been implicated in the regulation of protein stability, subcellular localization of proteins and protein-protein interaction.
17707335	2	17	theme	osteoblast-specific	409:427	arg1	osteocalcin					393:403	osteocalcin	393:403	osteocalcin	393:403	Here, we demonstrate that O-GlcNAc modification regulates the expression of osteocalcin, an osteoblast-specific marker, via Runx2 transcriptional activity in osteoblastic differentiation.
17707335	2	17	theme	osteoblast-specific	409:427	arg1	marker					429:434	an osteoblast-specific marker	406:434	an osteoblast-specific marker	406:434	Here, we demonstrate that O-GlcNAc modification regulates the expression of osteocalcin, an osteoblast-specific marker, via Runx2 transcriptional activity in osteoblastic differentiation.
17707335	5	18	theme	osteocalcin	888:898	arg1	promoter					900:907	the osteocalcin promoter	884:907	the osteocalcin promoter	884:907	By conducting activity assays of the osteocalcin promoter and transcription factor, we found that the OSE2 site in the osteocalcin promoter and Runx2 were important for increased osteocalcin promoter activity by PUGNAc.
17707335	5	19	theme	activity	783:790	arg1	assays					792:797	activity assays	783:797	activity assays of the osteocalcin promoter and transcription factor	783:850	By conducting activity assays of the osteocalcin promoter and transcription factor, we found that the OSE2 site in the osteocalcin promoter and Runx2 were important for increased osteocalcin promoter activity by PUGNAc.
17707335	2	20	theme	osteoblastic	475:486	arg1	differentiation					488:502	osteoblastic differentiation	475:502	osteoblastic differentiation	475:502	Here, we demonstrate that O-GlcNAc modification regulates the expression of osteocalcin, an osteoblast-specific marker, via Runx2 transcriptional activity in osteoblastic differentiation.
17707335	6	21	theme	Runx2	1051:1055	arg1	modification					1035:1046	increased O-GlcNAc modification	1016:1046	increased O-GlcNAc modification	1016:1046	Furthermore, PUGNAc led to increased O-GlcNAc modification of Runx2, which regulated the transcription of its target gene osteocalcin.
17707335	6	22	theme	target	1099:1104	arg1	osteocalcin					1111:1121	its target gene osteocalcin	1095:1121	its target gene osteocalcin	1095:1121	Furthermore, PUGNAc led to increased O-GlcNAc modification of Runx2, which regulated the transcription of its target gene osteocalcin.
17707335	7	23	theme	regulation	1235:1244	arg1	mode					1198:1201	a new mode	1192:1201	a new mode of osteoblastic differentiation regulation	1192:1244	Thus, these data provide evidence that O-GlcNAc modification may be a new mode of osteoblastic differentiation regulation.
17707335	7	23	theme	regulation	1235:1244	arg1	modification					1172:1183	O-GlcNAc modification	1163:1183	O-GlcNAc modification	1163:1183	Thus, these data provide evidence that O-GlcNAc modification may be a new mode of osteoblastic differentiation regulation.
17707335	4	24	theme	O-GlcNAcase	648:658	arg1	PUGNAc					624:629	PUGNAc	624:629	PUGNAc	624:629	In addition, PUGNAc, an inhibitor of O-GlcNAcase, potentiated the expression of osteocalcin caused by ascorbic acid, parathyroid hormone (PTH) and forskolin.
17707335	4	24	theme	O-GlcNAcase	648:658	arg1	inhibitor					635:643	an inhibitor	632:643	an inhibitor of O-GlcNAcase	632:658	In addition, PUGNAc, an inhibitor of O-GlcNAcase, potentiated the expression of osteocalcin caused by ascorbic acid, parathyroid hormone (PTH) and forskolin.
17707335	4	25	theme	parathyroid	728:738	arg1	PTH					749:751	PTH	749:751	PTH	749:751	In addition, PUGNAc, an inhibitor of O-GlcNAcase, potentiated the expression of osteocalcin caused by ascorbic acid, parathyroid hormone (PTH) and forskolin.
17707335	4	25	theme	parathyroid	728:738	arg1	hormone					740:746	parathyroid hormone	728:746	parathyroid hormone (PTH)	728:752	In addition, PUGNAc, an inhibitor of O-GlcNAcase, potentiated the expression of osteocalcin caused by ascorbic acid, parathyroid hormone (PTH) and forskolin.
17707335	5	26	theme	promoter	960:967	arg1	activity					969:976	increased osteocalcin promoter activity	938:976	increased osteocalcin promoter activity by PUGNAc	938:986	By conducting activity assays of the osteocalcin promoter and transcription factor, we found that the OSE2 site in the osteocalcin promoter and Runx2 were important for increased osteocalcin promoter activity by PUGNAc.
17707335	2	27	theme	transcriptional	447:461	arg1	activity					463:470	Runx2 transcriptional activity	441:470	Runx2 transcriptional activity in osteoblastic differentiation	441:502	Here, we demonstrate that O-GlcNAc modification regulates the expression of osteocalcin, an osteoblast-specific marker, via Runx2 transcriptional activity in osteoblastic differentiation.
17707335	6	28	theme	osteocalcin	1111:1121	arg1	transcription					1078:1090	the transcription	1074:1090	the transcription of its target gene osteocalcin	1074:1121	Furthermore, PUGNAc led to increased O-GlcNAc modification of Runx2, which regulated the transcription of its target gene osteocalcin.
17707335	4	29	theme	ascorbic	713:720	arg1	acid					722:725	ascorbic acid	713:725	ascorbic acid	713:725	In addition, PUGNAc, an inhibitor of O-GlcNAcase, potentiated the expression of osteocalcin caused by ascorbic acid, parathyroid hormone (PTH) and forskolin.
17707335	1	30	theme	protein	228:234	arg1	stability					236:244	protein stability	228:244	protein stability	228:244	O-Linked beta-N-acetylglucosamine (O-GlcNAc) modification, a reversible post-translational modification, has been implicated in the regulation of protein stability, subcellular localization of proteins and protein-protein interaction.
17707335	5	31	theme	OSE2	871:874	arg1	important					924:932	important	924:932	important	924:932	By conducting activity assays of the osteocalcin promoter and transcription factor, we found that the OSE2 site in the osteocalcin promoter and Runx2 were important for increased osteocalcin promoter activity by PUGNAc.
17707335	5	31	theme	OSE2	871:874	arg1	site					876:879	the OSE2 site	867:879	the OSE2 site in the osteocalcin promoter and Runx2	867:917	By conducting activity assays of the osteocalcin promoter and transcription factor, we found that the OSE2 site in the osteocalcin promoter and Runx2 were important for increased osteocalcin promoter activity by PUGNAc.
17707335	6	32	theme	O-GlcNAc	1026:1033	arg1	modification					1035:1046	increased O-GlcNAc modification	1016:1046	increased O-GlcNAc modification	1016:1046	Furthermore, PUGNAc led to increased O-GlcNAc modification of Runx2, which regulated the transcription of its target gene osteocalcin.
17707335	0	33	theme	osteocalcin	50:60	arg1	expression					36:45	the expression	32:45	the expression of osteocalcin	32:60	O-GlcNAc modification modulates the expression of osteocalcin via OSE2 and Runx2.
17707335	6	34	theme	increased	1016:1024	arg1	modification					1035:1046	increased O-GlcNAc modification	1016:1046	increased O-GlcNAc modification	1016:1046	Furthermore, PUGNAc led to increased O-GlcNAc modification of Runx2, which regulated the transcription of its target gene osteocalcin.
17707335	3	35	theme	MC3T3-E1	586:593	arg1	preosteoblasts					595:608	MC3T3-E1 preosteoblasts	586:608	MC3T3-E1 preosteoblasts	586:608	Protein-associated O-GlcNAc was increased during osteoblastic differentiation in MC3T3-E1 preosteoblasts.
17707335	6	36	mod	modification	1035:1046	arg1	Runx2					1051:1055	Runx2	1051:1055	Runx2	1051:1055	Furthermore, PUGNAc led to increased O-GlcNAc modification of Runx2, which regulated the transcription of its target gene osteocalcin.
17707335	6	36	mod	modification	1035:1046	arg3	O-GlcNAc					1026:1033	increased O-GlcNAc modification	1016:1046	increased O-GlcNAc modification	1016:1046	Furthermore, PUGNAc led to increased O-GlcNAc modification of Runx2, which regulated the transcription of its target gene osteocalcin.
17707335	7	37	theme	differentiation	1219:1233	arg1	regulation					1235:1244	osteoblastic differentiation regulation	1206:1244	osteoblastic differentiation regulation	1206:1244	Thus, these data provide evidence that O-GlcNAc modification may be a new mode of osteoblastic differentiation regulation.
17707335	3	38	theme	osteoblastic	554:565	arg1	differentiation					567:581	osteoblastic differentiation	554:581	osteoblastic differentiation in MC3T3-E1 preosteoblasts	554:608	Protein-associated O-GlcNAc was increased during osteoblastic differentiation in MC3T3-E1 preosteoblasts.
17707335	1	39	theme	stability	236:244	arg1	regulation					214:223	the regulation	210:223	the regulation of protein stability	210:244	O-Linked beta-N-acetylglucosamine (O-GlcNAc) modification, a reversible post-translational modification, has been implicated in the regulation of protein stability, subcellular localization of proteins and protein-protein interaction.
17707335	1	39	theme	stability	236:244	arg1	interaction					304:314	protein-protein interaction	288:314	protein-protein interaction	288:314	O-Linked beta-N-acetylglucosamine (O-GlcNAc) modification, a reversible post-translational modification, has been implicated in the regulation of protein stability, subcellular localization of proteins and protein-protein interaction.
17707335	1	39	theme	stability	236:244	arg1	localization					259:270	subcellular localization	247:270	subcellular localization of proteins	247:282	O-Linked beta-N-acetylglucosamine (O-GlcNAc) modification, a reversible post-translational modification, has been implicated in the regulation of protein stability, subcellular localization of proteins and protein-protein interaction.
17707335	4	40	theme	osteocalcin	691:701	arg1	expression					677:686	the expression	673:686	the expression of osteocalcin caused by ascorbic acid, parathyroid hormone (PTH) and forskolin	673:766	In addition, PUGNAc, an inhibitor of O-GlcNAcase, potentiated the expression of osteocalcin caused by ascorbic acid, parathyroid hormone (PTH) and forskolin.
17707335	5	41	theme	factor	845:850	arg1	assays					792:797	activity assays	783:797	activity assays of the osteocalcin promoter and transcription factor	783:850	By conducting activity assays of the osteocalcin promoter and transcription factor, we found that the OSE2 site in the osteocalcin promoter and Runx2 were important for increased osteocalcin promoter activity by PUGNAc.
17707335	2	42	theme	Runx2	441:445	arg1	activity					463:470	Runx2 transcriptional activity	441:470	Runx2 transcriptional activity in osteoblastic differentiation	441:502	Here, we demonstrate that O-GlcNAc modification regulates the expression of osteocalcin, an osteoblast-specific marker, via Runx2 transcriptional activity in osteoblastic differentiation.
17707335	1	43	theme	reversible	143:152	arg1	modification					173:184	a reversible post-translational modification	141:184	a reversible post-translational modification	141:184	O-Linked beta-N-acetylglucosamine (O-GlcNAc) modification, a reversible post-translational modification, has been implicated in the regulation of protein stability, subcellular localization of proteins and protein-protein interaction.
17707335	1	43	theme	reversible	143:152	arg1	modification					127:138	O-Linked beta-N-acetylglucosamine (O-GlcNAc) modification	82:138	O-Linked beta-N-acetylglucosamine (O-GlcNAc) modification	82:138	O-Linked beta-N-acetylglucosamine (O-GlcNAc) modification, a reversible post-translational modification, has been implicated in the regulation of protein stability, subcellular localization of proteins and protein-protein interaction.
17707335	5	44	theme	increased	938:946	arg1	activity					969:976	increased osteocalcin promoter activity	938:976	increased osteocalcin promoter activity by PUGNAc	938:986	By conducting activity assays of the osteocalcin promoter and transcription factor, we found that the OSE2 site in the osteocalcin promoter and Runx2 were important for increased osteocalcin promoter activity by PUGNAc.
17707335	1	45	theme	subcellular	247:257	arg1	localization					259:270	subcellular localization	247:270	subcellular localization of proteins	247:282	O-Linked beta-N-acetylglucosamine (O-GlcNAc) modification, a reversible post-translational modification, has been implicated in the regulation of protein stability, subcellular localization of proteins and protein-protein interaction.
17707335	7	46	theme	osteoblastic	1206:1217	arg1	regulation					1235:1244	osteoblastic differentiation regulation	1206:1244	osteoblastic differentiation regulation	1206:1244	Thus, these data provide evidence that O-GlcNAc modification may be a new mode of osteoblastic differentiation regulation.
17707335	1	47	theme	post-translational	154:171	arg1	modification					173:184	a reversible post-translational modification	141:184	a reversible post-translational modification	141:184	O-Linked beta-N-acetylglucosamine (O-GlcNAc) modification, a reversible post-translational modification, has been implicated in the regulation of protein stability, subcellular localization of proteins and protein-protein interaction.
17707335	1	47	theme	post-translational	154:171	arg1	modification					127:138	O-Linked beta-N-acetylglucosamine (O-GlcNAc) modification	82:138	O-Linked beta-N-acetylglucosamine (O-GlcNAc) modification	82:138	O-Linked beta-N-acetylglucosamine (O-GlcNAc) modification, a reversible post-translational modification, has been implicated in the regulation of protein stability, subcellular localization of proteins and protein-protein interaction.
17707335	5	48	theme	promoter	818:825	arg1	assays					792:797	activity assays	783:797	activity assays of the osteocalcin promoter and transcription factor	783:850	By conducting activity assays of the osteocalcin promoter and transcription factor, we found that the OSE2 site in the osteocalcin promoter and Runx2 were important for increased osteocalcin promoter activity by PUGNAc.
21383013	9	0	theme	hyperglycemic	1416:1428	arg1	medium					1430:1435	hyperglycemic medium	1416:1435	hyperglycemic medium	1416:1435	Incubation of Mz-ChA-1 cells in hyperglycemic medium caused an increase in the InsP(3)-dependent calcium release from the endoplasmic reticulum.
21383013	7	1	theme	InsP	1258:1261	arg1	R-1					1265:1267	InsP(3)R-1	1258:1267	InsP(3)R-1	1258:1267	Interestingly, the functional impact of O-GlcNAcylation on the InsP(3)R-3 channel was opposite the effect measured with InsP(3)R-1.
21383013	1	2	theme	inositol	104:111	arg1	channel					179:185	an intracellular calcium channel	154:185	an intracellular calcium channel	154:185	The inositol 1,4,5-trisphosphate receptor (InsP(3)R), an intracellular calcium channel, has three isoforms with >65% sequence homology, yet the isoforms differ in their function and regulation by post-translational modifications.
21383013	1	2	theme	inositol	104:111	arg1	receptor					133:140	inositol 1,4,5-trisphosphate receptor	104:140	The inositol 1,4,5-trisphosphate receptor (InsP(3)R)	100:151	The inositol 1,4,5-trisphosphate receptor (InsP(3)R), an intracellular calcium channel, has three isoforms with >65% sequence homology, yet the isoforms differ in their function and regulation by post-translational modifications.
21383013	1	2	theme	inositol	104:111	arg1	R					150:150	InsP(3)R	143:150	InsP(3)R	143:150	The inositol 1,4,5-trisphosphate receptor (InsP(3)R), an intracellular calcium channel, has three isoforms with >65% sequence homology, yet the isoforms differ in their function and regulation by post-translational modifications.
21383013	6	3	theme	InsP	1080:1083	arg1	R-3					1087:1089	InsP(3)R-3	1080:1089	InsP(3)R-3	1080:1089	In contrast, InsP(3)R-3 in Mz-ChA-1 cells, a human cholangiocarcinoma cell line expressing predominantly InsP(3)R-3, was functionally modified by O-GlcNAcylation.
21383013	1	4	theme	calcium	171:177	arg1	channel					179:185	an intracellular calcium channel	154:185	an intracellular calcium channel	154:185	The inositol 1,4,5-trisphosphate receptor (InsP(3)R), an intracellular calcium channel, has three isoforms with >65% sequence homology, yet the isoforms differ in their function and regulation by post-translational modifications.
21383013	1	4	theme	calcium	171:177	arg1	receptor					133:140	inositol 1,4,5-trisphosphate receptor	104:140	The inositol 1,4,5-trisphosphate receptor (InsP(3)R)	100:151	The inositol 1,4,5-trisphosphate receptor (InsP(3)R), an intracellular calcium channel, has three isoforms with >65% sequence homology, yet the isoforms differ in their function and regulation by post-translational modifications.
21383013	10	5	theme	intracellular	1695:1707	arg1	transients					1717:1726	intracellular calcium transients	1695:1726	intracellular calcium transients	1695:1726	The dynamic and inducible nature of O-GlcNAcylation and the InsP(3)R isoform specificity suggest that this form of modification of InsP(3)R and subsequent changes in intracellular calcium transients are important in physiological and pathophysiological processes.
21383013	6	6	theme	cell	1045:1048	arg1	cells					1011:1015	Mz-ChA-1 cells	1002:1015	Mz-ChA-1 cells	1002:1015	In contrast, InsP(3)R-3 in Mz-ChA-1 cells, a human cholangiocarcinoma cell line expressing predominantly InsP(3)R-3, was functionally modified by O-GlcNAcylation.
21383013	6	6	theme	cell	1045:1048	arg1	line					1050:1053	a human cholangiocarcinoma cell line	1018:1053	a human cholangiocarcinoma cell line expressing predominantly InsP(3)R-3	1018:1089	In contrast, InsP(3)R-3 in Mz-ChA-1 cells, a human cholangiocarcinoma cell line expressing predominantly InsP(3)R-3, was functionally modified by O-GlcNAcylation.
21383013	10	7	theme	inducible	1545:1553	arg1	nature					1555:1560	The dynamic and inducible nature	1529:1560	The dynamic and inducible nature of O-GlcNAcylation	1529:1579	The dynamic and inducible nature of O-GlcNAcylation and the InsP(3)R isoform specificity suggest that this form of modification of InsP(3)R and subsequent changes in intracellular calcium transients are important in physiological and pathophysiological processes.
21383013	10	8	theme	changes	1684:1690	arg1	modification					1644:1655	modification	1644:1655	modification of InsP(3)R and subsequent changes in intracellular calcium transients	1644:1726	The dynamic and inducible nature of O-GlcNAcylation and the InsP(3)R isoform specificity suggest that this form of modification of InsP(3)R and subsequent changes in intracellular calcium transients are important in physiological and pathophysiological processes.
21383013	10	9	theme	dynamic	1533:1539	arg1	nature					1555:1560	The dynamic and inducible nature	1529:1560	The dynamic and inducible nature of O-GlcNAcylation	1529:1579	The dynamic and inducible nature of O-GlcNAcylation and the InsP(3)R isoform specificity suggest that this form of modification of InsP(3)R and subsequent changes in intracellular calcium transients are important in physiological and pathophysiological processes.
21383013	7	10	theme	O-GlcNAcylation	1178:1192	arg1	impact					1168:1173	the functional impact	1153:1173	the functional impact of O-GlcNAcylation on the InsP(3)R-3 channel	1153:1218	Interestingly, the functional impact of O-GlcNAcylation on the InsP(3)R-3 channel was opposite the effect measured with InsP(3)R-1.
21383013	5	11	theme	pancreatoma	675:685	arg1	line					692:695	a rat pancreatoma cell line	669:695	a rat pancreatoma cell line expressing predominantly InsP(3)R-2	669:731	Analysis of AR4-2J cells, a rat pancreatoma cell line expressing predominantly InsP(3)R-2, showed no detectable O-GlcNAcylation of InsP(3)R-2 and no significant functional changes despite the presence of the enzymes for addition (O-β-N-acetylglucosaminyltransferase) and removal (O-β-N-acetylglucosaminidase) of the monosaccharide.
21383013	5	11	theme	pancreatoma	675:685	arg1	cells					662:666	AR4-2J cells	655:666	AR4-2J cells	655:666	Analysis of AR4-2J cells, a rat pancreatoma cell line expressing predominantly InsP(3)R-2, showed no detectable O-GlcNAcylation of InsP(3)R-2 and no significant functional changes despite the presence of the enzymes for addition (O-β-N-acetylglucosaminyltransferase) and removal (O-β-N-acetylglucosaminidase) of the monosaccharide.
21383013	9	12	theme	calcium	1481:1487	arg1	release					1489:1495	the InsP(3)-dependent calcium release	1459:1495	the InsP(3)-dependent calcium release from the endoplasmic reticulum	1459:1526	Incubation of Mz-ChA-1 cells in hyperglycemic medium caused an increase in the InsP(3)-dependent calcium release from the endoplasmic reticulum.
21383013	2	13	dep	J.	483:484	arg1	Neurosci					541:548	Neurosci	541:548	Neurosci	541:548	We showed previously that InsP(3)R-1 is functionally modified by O-linked β-N-acetylglucosamine glycosylation (O-GlcNAcylation) (Rengifo, J., Gibson, C. J., Winkler, E., Collin, T., and Ehrlich, B. E. (2007) J. Neurosci.
21383013	10	14	dep	nature	1555:1560	arg1	specificity					1606:1616	isoform specificity	1598:1616	isoform specificity	1598:1616	The dynamic and inducible nature of O-GlcNAcylation and the InsP(3)R isoform specificity suggest that this form of modification of InsP(3)R and subsequent changes in intracellular calcium transients are important in physiological and pathophysiological processes.
21383013	10	15	theme	pathophysiological	1763:1780	arg1	processes					1782:1790	physiological and pathophysiological processes	1745:1790	physiological and pathophysiological processes	1745:1790	The dynamic and inducible nature of O-GlcNAcylation and the InsP(3)R isoform specificity suggest that this form of modification of InsP(3)R and subsequent changes in intracellular calcium transients are important in physiological and pathophysiological processes.
21383013	5	16	theme	enzymes	851:857	arg1	presence					835:842	the presence	831:842	the presence of the enzymes for addition (O-β-N-acetylglucosaminyltransferase) and removal (O-β-N-acetylglucosaminidase) of the monosaccharide	831:972	Analysis of AR4-2J cells, a rat pancreatoma cell line expressing predominantly InsP(3)R-2, showed no detectable O-GlcNAcylation of InsP(3)R-2 and no significant functional changes despite the presence of the enzymes for addition (O-β-N-acetylglucosaminyltransferase) and removal (O-β-N-acetylglucosaminidase) of the monosaccharide.
21383013	4	17	dep	InsP	616:619	arg1	R-3					638:640	R-3	638:640	R-3	638:640	We now report the effect of O-GlcNAcylation on InsP(3)R-2 and InsP(3)R-3.
21383013	4	17	dep	InsP	616:619	arg1	R-2					623:625	R-2	623:625	R-2	623:625	We now report the effect of O-GlcNAcylation on InsP(3)R-2 and InsP(3)R-3.
21383013	9	18	theme	endoplasmic	1506:1516	arg1	reticulum					1518:1526	the endoplasmic reticulum	1502:1526	the endoplasmic reticulum	1502:1526	Incubation of Mz-ChA-1 cells in hyperglycemic medium caused an increase in the InsP(3)-dependent calcium release from the endoplasmic reticulum.
21383013	10	19	theme	physiological	1745:1757	arg1	processes					1782:1790	physiological and pathophysiological processes	1745:1790	physiological and pathophysiological processes	1745:1790	The dynamic and inducible nature of O-GlcNAcylation and the InsP(3)R isoform specificity suggest that this form of modification of InsP(3)R and subsequent changes in intracellular calcium transients are important in physiological and pathophysiological processes.
21383013	0	20	theme	O-linked	76:83	arg1	glycosylation					85:97	O-linked glycosylation	76:97	O-linked glycosylation	76:97	Isoform-specific regulation of the inositol 1,4,5-trisphosphate receptor by O-linked glycosylation.
21383013	10	21	theme	InsP	1589:1592	arg1	R					1596:1596	the InsP(3)R	1585:1596	the InsP(3)R	1585:1596	The dynamic and inducible nature of O-GlcNAcylation and the InsP(3)R isoform specificity suggest that this form of modification of InsP(3)R and subsequent changes in intracellular calcium transients are important in physiological and pathophysiological processes.
21383013	6	22	from	R-3	995:997	arg1	cells					1011:1015	Mz-ChA-1 cells	1002:1015	Mz-ChA-1 cells	1002:1015	In contrast, InsP(3)R-3 in Mz-ChA-1 cells, a human cholangiocarcinoma cell line expressing predominantly InsP(3)R-3, was functionally modified by O-GlcNAcylation.
21383013	6	22	from	R-3	995:997	arg1	line					1050:1053	a human cholangiocarcinoma cell line	1018:1053	a human cholangiocarcinoma cell line expressing predominantly InsP(3)R-3	1018:1089	In contrast, InsP(3)R-3 in Mz-ChA-1 cells, a human cholangiocarcinoma cell line expressing predominantly InsP(3)R-3, was functionally modified by O-GlcNAcylation.
21383013	6	23	theme	Mz-ChA-1	1002:1009	arg1	cells					1011:1015	Mz-ChA-1 cells	1002:1015	Mz-ChA-1 cells	1002:1015	In contrast, InsP(3)R-3 in Mz-ChA-1 cells, a human cholangiocarcinoma cell line expressing predominantly InsP(3)R-3, was functionally modified by O-GlcNAcylation.
21383013	6	23	theme	Mz-ChA-1	1002:1009	arg1	line					1050:1053	a human cholangiocarcinoma cell line	1018:1053	a human cholangiocarcinoma cell line expressing predominantly InsP(3)R-3	1018:1089	In contrast, InsP(3)R-3 in Mz-ChA-1 cells, a human cholangiocarcinoma cell line expressing predominantly InsP(3)R-3, was functionally modified by O-GlcNAcylation.
21383013	5	24	theme	R-2	781:783	arg1	O-GlcNAcylation					755:769	no detectable O-GlcNAcylation	741:769	no detectable O-GlcNAcylation of InsP(3)R-2	741:783	Analysis of AR4-2J cells, a rat pancreatoma cell line expressing predominantly InsP(3)R-2, showed no detectable O-GlcNAcylation of InsP(3)R-2 and no significant functional changes despite the presence of the enzymes for addition (O-β-N-acetylglucosaminyltransferase) and removal (O-β-N-acetylglucosaminidase) of the monosaccharide.
21383013	5	24	theme	R-2	781:783	arg1	changes					815:821	no significant functional changes	789:821	no significant functional changes	789:821	Analysis of AR4-2J cells, a rat pancreatoma cell line expressing predominantly InsP(3)R-2, showed no detectable O-GlcNAcylation of InsP(3)R-2 and no significant functional changes despite the presence of the enzymes for addition (O-β-N-acetylglucosaminyltransferase) and removal (O-β-N-acetylglucosaminidase) of the monosaccharide.
21383013	0	25	theme	Isoform-specific	0:15	arg1	regulation					17:26	Isoform-specific regulation	0:26	Isoform-specific regulation of the inositol 1,4,5-trisphosphate receptor by O-linked glycosylation.	0:98	Isoform-specific regulation of the inositol 1,4,5-trisphosphate receptor by O-linked glycosylation.
21383013	1	26	theme	1,4,5-trisphosphate	113:131	arg1	channel					179:185	an intracellular calcium channel	154:185	an intracellular calcium channel	154:185	The inositol 1,4,5-trisphosphate receptor (InsP(3)R), an intracellular calcium channel, has three isoforms with >65% sequence homology, yet the isoforms differ in their function and regulation by post-translational modifications.
21383013	1	26	theme	1,4,5-trisphosphate	113:131	arg1	receptor					133:140	inositol 1,4,5-trisphosphate receptor	104:140	The inositol 1,4,5-trisphosphate receptor (InsP(3)R)	100:151	The inositol 1,4,5-trisphosphate receptor (InsP(3)R), an intracellular calcium channel, has three isoforms with >65% sequence homology, yet the isoforms differ in their function and regulation by post-translational modifications.
21383013	1	26	theme	1,4,5-trisphosphate	113:131	arg1	R					150:150	InsP(3)R	143:150	InsP(3)R	143:150	The inositol 1,4,5-trisphosphate receptor (InsP(3)R), an intracellular calcium channel, has three isoforms with >65% sequence homology, yet the isoforms differ in their function and regulation by post-translational modifications.
21383013	7	27	from	impact	1168:1173	arg1	channel					1212:1218	the InsP(3)R-3 channel	1197:1218	the InsP(3)R-3 channel	1197:1218	Interestingly, the functional impact of O-GlcNAcylation on the InsP(3)R-3 channel was opposite the effect measured with InsP(3)R-1.
21383013	1	28	dep	R	150:150	arg1	3					148:148	3	148:148	3	148:148	The inositol 1,4,5-trisphosphate receptor (InsP(3)R), an intracellular calcium channel, has three isoforms with >65% sequence homology, yet the isoforms differ in their function and regulation by post-translational modifications.
21383013	2	29	theme	O-linked	395:402	arg1	O-GlcNAcylation					441:455	O-GlcNAcylation	441:455	O-GlcNAcylation	441:455	We showed previously that InsP(3)R-1 is functionally modified by O-linked β-N-acetylglucosamine glycosylation (O-GlcNAcylation) (Rengifo, J., Gibson, C. J., Winkler, E., Collin, T., and Ehrlich, B. E. (2007) J. Neurosci.
21383013	2	29	theme	O-linked	395:402	arg1	glycosylation					426:438	O-linked β-N-acetylglucosamine glycosylation	395:438	O-linked β-N-acetylglucosamine glycosylation (O-GlcNAcylation)	395:456	We showed previously that InsP(3)R-1 is functionally modified by O-linked β-N-acetylglucosamine glycosylation (O-GlcNAcylation) (Rengifo, J., Gibson, C. J., Winkler, E., Collin, T., and Ehrlich, B. E. (2007) J. Neurosci.
21383013	5	30	theme	cells	662:666	arg1	Analysis					643:650	Analysis	643:650	Analysis of AR4-2J cells, a rat pancreatoma cell line expressing predominantly InsP(3)R-2,	643:732	Analysis of AR4-2J cells, a rat pancreatoma cell line expressing predominantly InsP(3)R-2, showed no detectable O-GlcNAcylation of InsP(3)R-2 and no significant functional changes despite the presence of the enzymes for addition (O-β-N-acetylglucosaminyltransferase) and removal (O-β-N-acetylglucosaminidase) of the monosaccharide.
21383013	5	31	theme	InsP	774:777	arg1	R-2					781:783	InsP(3)R-2	774:783	InsP(3)R-2	774:783	Analysis of AR4-2J cells, a rat pancreatoma cell line expressing predominantly InsP(3)R-2, showed no detectable O-GlcNAcylation of InsP(3)R-2 and no significant functional changes despite the presence of the enzymes for addition (O-β-N-acetylglucosaminyltransferase) and removal (O-β-N-acetylglucosaminidase) of the monosaccharide.
21383013	10	32	dep	R	1667:1667	arg1	3					1665:1665	3	1665:1665	3	1665:1665	The dynamic and inducible nature of O-GlcNAcylation and the InsP(3)R isoform specificity suggest that this form of modification of InsP(3)R and subsequent changes in intracellular calcium transients are important in physiological and pathophysiological processes.
21383013	2	33	dep	modified	383:390	arg1	B.					525:526	B.	525:526	B.	525:526	We showed previously that InsP(3)R-1 is functionally modified by O-linked β-N-acetylglucosamine glycosylation (O-GlcNAcylation) (Rengifo, J., Gibson, C. J., Winkler, E., Collin, T., and Ehrlich, B. E. (2007) J. Neurosci.
21383013	2	33	dep	modified	383:390	arg1	J.					483:484	J.	483:484	J.	483:484	We showed previously that InsP(3)R-1 is functionally modified by O-linked β-N-acetylglucosamine glycosylation (O-GlcNAcylation) (Rengifo, J., Gibson, C. J., Winkler, E., Collin, T., and Ehrlich, B. E. (2007) J. Neurosci.
21383013	2	33	dep	modified	383:390	arg1	E					528:528	E	528:528	E	528:528	We showed previously that InsP(3)R-1 is functionally modified by O-linked β-N-acetylglucosamine glycosylation (O-GlcNAcylation) (Rengifo, J., Gibson, C. J., Winkler, E., Collin, T., and Ehrlich, B. E. (2007) J. Neurosci.
21383013	2	33	dep	modified	383:390	arg1	T.					508:509	T.	508:509	T.	508:509	We showed previously that InsP(3)R-1 is functionally modified by O-linked β-N-acetylglucosamine glycosylation (O-GlcNAcylation) (Rengifo, J., Gibson, C. J., Winkler, E., Collin, T., and Ehrlich, B. E. (2007) J. Neurosci.
21383013	2	33	dep	modified	383:390	arg1	J.					468:469	J.	468:469	J.	468:469	We showed previously that InsP(3)R-1 is functionally modified by O-linked β-N-acetylglucosamine glycosylation (O-GlcNAcylation) (Rengifo, J., Gibson, C. J., Winkler, E., Collin, T., and Ehrlich, B. E. (2007) J. Neurosci.
21383013	2	33	dep	modified	383:390	arg1	Gibson					472:477	Gibson	472:477	Gibson	472:477	We showed previously that InsP(3)R-1 is functionally modified by O-linked β-N-acetylglucosamine glycosylation (O-GlcNAcylation) (Rengifo, J., Gibson, C. J., Winkler, E., Collin, T., and Ehrlich, B. E. (2007) J. Neurosci.
21383013	2	33	dep	modified	383:390	arg1	2007					532:535	2007	532:535	2007	532:535	We showed previously that InsP(3)R-1 is functionally modified by O-linked β-N-acetylglucosamine glycosylation (O-GlcNAcylation) (Rengifo, J., Gibson, C. J., Winkler, E., Collin, T., and Ehrlich, B. E. (2007) J. Neurosci.
21383013	2	33	dep	modified	383:390	arg1	E.					496:497	E.	496:497	E.	496:497	We showed previously that InsP(3)R-1 is functionally modified by O-linked β-N-acetylglucosamine glycosylation (O-GlcNAcylation) (Rengifo, J., Gibson, C. J., Winkler, E., Collin, T., and Ehrlich, B. E. (2007) J. Neurosci.
21383013	2	33	dep	modified	383:390	arg1	Collin					500:505	Collin	500:505	Collin	500:505	We showed previously that InsP(3)R-1 is functionally modified by O-linked β-N-acetylglucosamine glycosylation (O-GlcNAcylation) (Rengifo, J., Gibson, C. J., Winkler, E., Collin, T., and Ehrlich, B. E. (2007) J. Neurosci.
21383013	2	33	dep	modified	383:390	arg1	C.					480:481	C.	480:481	C.	480:481	We showed previously that InsP(3)R-1 is functionally modified by O-linked β-N-acetylglucosamine glycosylation (O-GlcNAcylation) (Rengifo, J., Gibson, C. J., Winkler, E., Collin, T., and Ehrlich, B. E. (2007) J. Neurosci.
21383013	5	34	theme	cell	687:690	arg1	line					692:695	a rat pancreatoma cell line	669:695	a rat pancreatoma cell line expressing predominantly InsP(3)R-2	669:731	Analysis of AR4-2J cells, a rat pancreatoma cell line expressing predominantly InsP(3)R-2, showed no detectable O-GlcNAcylation of InsP(3)R-2 and no significant functional changes despite the presence of the enzymes for addition (O-β-N-acetylglucosaminyltransferase) and removal (O-β-N-acetylglucosaminidase) of the monosaccharide.
21383013	5	34	theme	cell	687:690	arg1	cells					662:666	AR4-2J cells	655:666	AR4-2J cells	655:666	Analysis of AR4-2J cells, a rat pancreatoma cell line expressing predominantly InsP(3)R-2, showed no detectable O-GlcNAcylation of InsP(3)R-2 and no significant functional changes despite the presence of the enzymes for addition (O-β-N-acetylglucosaminyltransferase) and removal (O-β-N-acetylglucosaminidase) of the monosaccharide.
21383013	0	35	theme	inositol	35:42	arg1	receptor					64:71	the inositol 1,4,5-trisphosphate receptor	31:71	the inositol 1,4,5-trisphosphate receptor	31:71	Isoform-specific regulation of the inositol 1,4,5-trisphosphate receptor by O-linked glycosylation.
21383013	0	36	theme	receptor	64:71	arg1	regulation					17:26	Isoform-specific regulation	0:26	Isoform-specific regulation of the inositol 1,4,5-trisphosphate receptor by O-linked glycosylation.	0:98	Isoform-specific regulation of the inositol 1,4,5-trisphosphate receptor by O-linked glycosylation.
21383013	10	37	from	processes	1782:1790	arg1	important					1732:1740	important	1732:1740	important	1732:1740	The dynamic and inducible nature of O-GlcNAcylation and the InsP(3)R isoform specificity suggest that this form of modification of InsP(3)R and subsequent changes in intracellular calcium transients are important in physiological and pathophysiological processes.
21383013	8	38	theme	single	1351:1356	arg1	probability					1371:1381	InsP(3)R-3 single channel open probability	1340:1381	InsP(3)R-3 single channel open probability	1340:1381	Addition of O-GlcNAc by O-β-N-acetylglucosaminyltransferase increased InsP(3)R-3 single channel open probability.
21383013	1	39	theme	>65	212:214	arg1	%					215:215	%	215:215	%	215:215	The inositol 1,4,5-trisphosphate receptor (InsP(3)R), an intracellular calcium channel, has three isoforms with >65% sequence homology, yet the isoforms differ in their function and regulation by post-translational modifications.
21383013	6	40	theme	InsP	988:991	arg1	R-3					995:997	InsP(3)R-3	988:997	InsP(3)R-3 in Mz-ChA-1 cells, a human cholangiocarcinoma cell line expressing predominantly InsP(3)R-3,	988:1090	In contrast, InsP(3)R-3 in Mz-ChA-1 cells, a human cholangiocarcinoma cell line expressing predominantly InsP(3)R-3, was functionally modified by O-GlcNAcylation.
21383013	9	41	theme	Mz-ChA-1	1398:1405	arg1	cells					1407:1411	Mz-ChA-1 cells	1398:1411	Mz-ChA-1 cells	1398:1411	Incubation of Mz-ChA-1 cells in hyperglycemic medium caused an increase in the InsP(3)-dependent calcium release from the endoplasmic reticulum.
21383013	8	42	theme	open	1366:1369	arg1	probability					1371:1381	InsP(3)R-3 single channel open probability	1340:1381	InsP(3)R-3 single channel open probability	1340:1381	Addition of O-GlcNAc by O-β-N-acetylglucosaminyltransferase increased InsP(3)R-3 single channel open probability.
21383013	1	43	contain	has	188:190	arg1	channel					179:185	an intracellular calcium channel	154:185	an intracellular calcium channel	154:185	The inositol 1,4,5-trisphosphate receptor (InsP(3)R), an intracellular calcium channel, has three isoforms with >65% sequence homology, yet the isoforms differ in their function and regulation by post-translational modifications.
21383013	1	43	contain	has	188:190	arg2	isoforms					198:205	three isoforms	192:205	three isoforms with >65% sequence homology	192:233	The inositol 1,4,5-trisphosphate receptor (InsP(3)R), an intracellular calcium channel, has three isoforms with >65% sequence homology, yet the isoforms differ in their function and regulation by post-translational modifications.
21383013	1	43	contain	has	188:190	arg1	receptor					133:140	inositol 1,4,5-trisphosphate receptor	104:140	The inositol 1,4,5-trisphosphate receptor (InsP(3)R)	100:151	The inositol 1,4,5-trisphosphate receptor (InsP(3)R), an intracellular calcium channel, has three isoforms with >65% sequence homology, yet the isoforms differ in their function and regulation by post-translational modifications.
21383013	1	43	contain	has	188:190	arg1	R					150:150	InsP(3)R	143:150	InsP(3)R	143:150	The inositol 1,4,5-trisphosphate receptor (InsP(3)R), an intracellular calcium channel, has three isoforms with >65% sequence homology, yet the isoforms differ in their function and regulation by post-translational modifications.
21383013	4	44	from	effect	587:592	arg1	InsP					616:619	InsP(3)	616:622	InsP(3)	616:622	We now report the effect of O-GlcNAcylation on InsP(3)R-2 and InsP(3)R-3.
21383013	4	44	from	effect	587:592	arg1	InsP					631:634	InsP(3)	631:637	InsP(3)	631:637	We now report the effect of O-GlcNAcylation on InsP(3)R-2 and InsP(3)R-3.
21383013	1	45	theme	sequence	217:224	arg1	homology					226:233	>65% sequence homology	212:233	>65% sequence homology	212:233	The inositol 1,4,5-trisphosphate receptor (InsP(3)R), an intracellular calcium channel, has three isoforms with >65% sequence homology, yet the isoforms differ in their function and regulation by post-translational modifications.
21383013	6	46	mod	modified	1109:1116	arg1	R-3					995:997	InsP(3)R-3	988:997	InsP(3)R-3 in Mz-ChA-1 cells, a human cholangiocarcinoma cell line expressing predominantly InsP(3)R-3,	988:1090	In contrast, InsP(3)R-3 in Mz-ChA-1 cells, a human cholangiocarcinoma cell line expressing predominantly InsP(3)R-3, was functionally modified by O-GlcNAcylation.
21383013	6	46	mod	modified	1109:1116	arg3	O-GlcNAcylation					1121:1135	O-GlcNAcylation	1121:1135	O-GlcNAcylation	1121:1135	In contrast, InsP(3)R-3 in Mz-ChA-1 cells, a human cholangiocarcinoma cell line expressing predominantly InsP(3)R-3, was functionally modified by O-GlcNAcylation.
21383013	5	47	theme	functional	804:813	arg1	changes					815:821	no significant functional changes	789:821	no significant functional changes	789:821	Analysis of AR4-2J cells, a rat pancreatoma cell line expressing predominantly InsP(3)R-2, showed no detectable O-GlcNAcylation of InsP(3)R-2 and no significant functional changes despite the presence of the enzymes for addition (O-β-N-acetylglucosaminyltransferase) and removal (O-β-N-acetylglucosaminidase) of the monosaccharide.
21383013	10	48	theme	InsP	1660:1663	arg1	R					1667:1667	InsP(3)R	1660:1667	InsP(3)R	1660:1667	The dynamic and inducible nature of O-GlcNAcylation and the InsP(3)R isoform specificity suggest that this form of modification of InsP(3)R and subsequent changes in intracellular calcium transients are important in physiological and pathophysiological processes.
21383013	10	49	dep	R	1596:1596	arg1	3					1594:1594	3	1594:1594	3	1594:1594	The dynamic and inducible nature of O-GlcNAcylation and the InsP(3)R isoform specificity suggest that this form of modification of InsP(3)R and subsequent changes in intracellular calcium transients are important in physiological and pathophysiological processes.
21383013	10	50	theme	modification	1644:1655	arg1	form					1636:1639	this form	1631:1639	this form of modification of InsP(3)R and subsequent changes in intracellular calcium transients	1631:1726	The dynamic and inducible nature of O-GlcNAcylation and the InsP(3)R isoform specificity suggest that this form of modification of InsP(3)R and subsequent changes in intracellular calcium transients are important in physiological and pathophysiological processes.
21383013	10	51	theme	R	1667:1667	arg1	modification					1644:1655	modification	1644:1655	modification of InsP(3)R and subsequent changes in intracellular calcium transients	1644:1726	The dynamic and inducible nature of O-GlcNAcylation and the InsP(3)R isoform specificity suggest that this form of modification of InsP(3)R and subsequent changes in intracellular calcium transients are important in physiological and pathophysiological processes.
21383013	1	52	theme	intracellular	157:169	arg1	channel					179:185	an intracellular calcium channel	154:185	an intracellular calcium channel	154:185	The inositol 1,4,5-trisphosphate receptor (InsP(3)R), an intracellular calcium channel, has three isoforms with >65% sequence homology, yet the isoforms differ in their function and regulation by post-translational modifications.
21383013	1	52	theme	intracellular	157:169	arg1	receptor					133:140	inositol 1,4,5-trisphosphate receptor	104:140	The inositol 1,4,5-trisphosphate receptor (InsP(3)R)	100:151	The inositol 1,4,5-trisphosphate receptor (InsP(3)R), an intracellular calcium channel, has three isoforms with >65% sequence homology, yet the isoforms differ in their function and regulation by post-translational modifications.
21383013	7	53	theme	opposite	1224:1231	arg1	effect					1237:1242	opposite the effect	1224:1242	opposite the effect	1224:1242	Interestingly, the functional impact of O-GlcNAcylation on the InsP(3)R-3 channel was opposite the effect measured with InsP(3)R-1.
21383013	7	54	theme	R-3	1208:1210	arg1	channel					1212:1218	the InsP(3)R-3 channel	1197:1218	the InsP(3)R-3 channel	1197:1218	Interestingly, the functional impact of O-GlcNAcylation on the InsP(3)R-3 channel was opposite the effect measured with InsP(3)R-1.
21383013	10	55	from	modification	1644:1655	arg1	transients					1717:1726	intracellular calcium transients	1695:1726	intracellular calcium transients	1695:1726	The dynamic and inducible nature of O-GlcNAcylation and the InsP(3)R isoform specificity suggest that this form of modification of InsP(3)R and subsequent changes in intracellular calcium transients are important in physiological and pathophysiological processes.
21383013	9	56	theme	InsP	1463:1466	arg1	release					1489:1495	the InsP(3)-dependent calcium release	1459:1495	the InsP(3)-dependent calcium release from the endoplasmic reticulum	1459:1526	Incubation of Mz-ChA-1 cells in hyperglycemic medium caused an increase in the InsP(3)-dependent calcium release from the endoplasmic reticulum.
21383013	2	57	mod	modified	383:390	arg1	R-1					363:365	InsP(3)R-1	356:365	InsP(3)R-1	356:365	We showed previously that InsP(3)R-1 is functionally modified by O-linked β-N-acetylglucosamine glycosylation (O-GlcNAcylation) (Rengifo, J., Gibson, C. J., Winkler, E., Collin, T., and Ehrlich, B. E. (2007) J. Neurosci.
21383013	2	57	mod	modified	383:390	arg3	glycosylation					426:438	O-linked β-N-acetylglucosamine glycosylation	395:438	O-linked β-N-acetylglucosamine glycosylation (O-GlcNAcylation)	395:456	We showed previously that InsP(3)R-1 is functionally modified by O-linked β-N-acetylglucosamine glycosylation (O-GlcNAcylation) (Rengifo, J., Gibson, C. J., Winkler, E., Collin, T., and Ehrlich, B. E. (2007) J. Neurosci.
21383013	2	57	mod	modified	383:390	arg3	O-GlcNAcylation					441:455	O-GlcNAcylation	441:455	O-GlcNAcylation	441:455	We showed previously that InsP(3)R-1 is functionally modified by O-linked β-N-acetylglucosamine glycosylation (O-GlcNAcylation) (Rengifo, J., Gibson, C. J., Winkler, E., Collin, T., and Ehrlich, B. E. (2007) J. Neurosci.
21383013	9	58	from	increase	1447:1454	arg1	release					1489:1495	the InsP(3)-dependent calcium release	1459:1495	the InsP(3)-dependent calcium release from the endoplasmic reticulum	1459:1526	Incubation of Mz-ChA-1 cells in hyperglycemic medium caused an increase in the InsP(3)-dependent calcium release from the endoplasmic reticulum.
21383013	9	58	from	increase	1447:1454	arg1	reticulum					1518:1526	the endoplasmic reticulum	1502:1526	the endoplasmic reticulum	1502:1526	Incubation of Mz-ChA-1 cells in hyperglycemic medium caused an increase in the InsP(3)-dependent calcium release from the endoplasmic reticulum.
21383013	7	59	theme	InsP	1201:1204	arg1	channel					1212:1218	the InsP(3)R-3 channel	1197:1218	the InsP(3)R-3 channel	1197:1218	Interestingly, the functional impact of O-GlcNAcylation on the InsP(3)R-3 channel was opposite the effect measured with InsP(3)R-1.
21383013	10	60	theme	subsequent	1673:1682	arg1	changes					1684:1690	subsequent changes	1673:1690	subsequent changes in intracellular calcium transients	1673:1726	The dynamic and inducible nature of O-GlcNAcylation and the InsP(3)R isoform specificity suggest that this form of modification of InsP(3)R and subsequent changes in intracellular calcium transients are important in physiological and pathophysiological processes.
21383013	5	61	theme	rat	671:673	arg1	line					692:695	a rat pancreatoma cell line	669:695	a rat pancreatoma cell line expressing predominantly InsP(3)R-2	669:731	Analysis of AR4-2J cells, a rat pancreatoma cell line expressing predominantly InsP(3)R-2, showed no detectable O-GlcNAcylation of InsP(3)R-2 and no significant functional changes despite the presence of the enzymes for addition (O-β-N-acetylglucosaminyltransferase) and removal (O-β-N-acetylglucosaminidase) of the monosaccharide.
21383013	5	61	theme	rat	671:673	arg1	cells					662:666	AR4-2J cells	655:666	AR4-2J cells	655:666	Analysis of AR4-2J cells, a rat pancreatoma cell line expressing predominantly InsP(3)R-2, showed no detectable O-GlcNAcylation of InsP(3)R-2 and no significant functional changes despite the presence of the enzymes for addition (O-β-N-acetylglucosaminyltransferase) and removal (O-β-N-acetylglucosaminidase) of the monosaccharide.
21383013	9	62	theme	-dependent	1470:1479	arg1	release					1489:1495	the InsP(3)-dependent calcium release	1459:1495	the InsP(3)-dependent calcium release from the endoplasmic reticulum	1459:1526	Incubation of Mz-ChA-1 cells in hyperglycemic medium caused an increase in the InsP(3)-dependent calcium release from the endoplasmic reticulum.
21383013	6	63	theme	human	1020:1024	arg1	cells					1011:1015	Mz-ChA-1 cells	1002:1015	Mz-ChA-1 cells	1002:1015	In contrast, InsP(3)R-3 in Mz-ChA-1 cells, a human cholangiocarcinoma cell line expressing predominantly InsP(3)R-3, was functionally modified by O-GlcNAcylation.
21383013	6	63	theme	human	1020:1024	arg1	line					1050:1053	a human cholangiocarcinoma cell line	1018:1053	a human cholangiocarcinoma cell line expressing predominantly InsP(3)R-3	1018:1089	In contrast, InsP(3)R-3 in Mz-ChA-1 cells, a human cholangiocarcinoma cell line expressing predominantly InsP(3)R-3, was functionally modified by O-GlcNAcylation.
21383013	1	64	theme	post-translational	296:313	arg1	modifications					315:327	post-translational modifications	296:327	post-translational modifications	296:327	The inositol 1,4,5-trisphosphate receptor (InsP(3)R), an intracellular calcium channel, has three isoforms with >65% sequence homology, yet the isoforms differ in their function and regulation by post-translational modifications.
21383013	10	65	theme	O-GlcNAcylation	1565:1579	arg1	R					1596:1596	the InsP(3)R	1585:1596	the InsP(3)R	1585:1596	The dynamic and inducible nature of O-GlcNAcylation and the InsP(3)R isoform specificity suggest that this form of modification of InsP(3)R and subsequent changes in intracellular calcium transients are important in physiological and pathophysiological processes.
21383013	10	65	theme	O-GlcNAcylation	1565:1579	arg1	nature					1555:1560	The dynamic and inducible nature	1529:1560	The dynamic and inducible nature of O-GlcNAcylation	1529:1579	The dynamic and inducible nature of O-GlcNAcylation and the InsP(3)R isoform specificity suggest that this form of modification of InsP(3)R and subsequent changes in intracellular calcium transients are important in physiological and pathophysiological processes.
21383013	9	66	from	Incubation	1384:1393	arg1	medium					1430:1435	hyperglycemic medium	1416:1435	hyperglycemic medium	1416:1435	Incubation of Mz-ChA-1 cells in hyperglycemic medium caused an increase in the InsP(3)-dependent calcium release from the endoplasmic reticulum.
21383013	1	67	theme	InsP	143:146	arg1	receptor					133:140	inositol 1,4,5-trisphosphate receptor	104:140	The inositol 1,4,5-trisphosphate receptor (InsP(3)R)	100:151	The inositol 1,4,5-trisphosphate receptor (InsP(3)R), an intracellular calcium channel, has three isoforms with >65% sequence homology, yet the isoforms differ in their function and regulation by post-translational modifications.
21383013	1	67	theme	InsP	143:146	arg1	R					150:150	InsP(3)R	143:150	InsP(3)R	143:150	The inositol 1,4,5-trisphosphate receptor (InsP(3)R), an intracellular calcium channel, has three isoforms with >65% sequence homology, yet the isoforms differ in their function and regulation by post-translational modifications.
21383013	10	68	from	R	1667:1667	arg1	transients					1717:1726	intracellular calcium transients	1695:1726	intracellular calcium transients	1695:1726	The dynamic and inducible nature of O-GlcNAcylation and the InsP(3)R isoform specificity suggest that this form of modification of InsP(3)R and subsequent changes in intracellular calcium transients are important in physiological and pathophysiological processes.
21383013	5	69	dep	R-2	781:783	arg1	3					779:779	3	779:779	3	779:779	Analysis of AR4-2J cells, a rat pancreatoma cell line expressing predominantly InsP(3)R-2, showed no detectable O-GlcNAcylation of InsP(3)R-2 and no significant functional changes despite the presence of the enzymes for addition (O-β-N-acetylglucosaminyltransferase) and removal (O-β-N-acetylglucosaminidase) of the monosaccharide.
21383013	10	70	theme	calcium	1709:1715	arg1	transients					1717:1726	intracellular calcium transients	1695:1726	intracellular calcium transients	1695:1726	The dynamic and inducible nature of O-GlcNAcylation and the InsP(3)R isoform specificity suggest that this form of modification of InsP(3)R and subsequent changes in intracellular calcium transients are important in physiological and pathophysiological processes.
21383013	7	71	theme	functional	1157:1166	arg1	impact					1168:1173	the functional impact	1153:1173	the functional impact of O-GlcNAcylation on the InsP(3)R-3 channel	1153:1218	Interestingly, the functional impact of O-GlcNAcylation on the InsP(3)R-3 channel was opposite the effect measured with InsP(3)R-1.
21383013	4	72	theme	O-GlcNAcylation	597:611	arg1	effect					587:592	the effect	583:592	the effect of O-GlcNAcylation on InsP(3)R-2 and InsP(3)R-3	583:640	We now report the effect of O-GlcNAcylation on InsP(3)R-2 and InsP(3)R-3.
21383013	5	73	theme	InsP	722:725	arg1	R-2					729:731	InsP(3)R-2	722:731	InsP(3)R-2	722:731	Analysis of AR4-2J cells, a rat pancreatoma cell line expressing predominantly InsP(3)R-2, showed no detectable O-GlcNAcylation of InsP(3)R-2 and no significant functional changes despite the presence of the enzymes for addition (O-β-N-acetylglucosaminyltransferase) and removal (O-β-N-acetylglucosaminidase) of the monosaccharide.
21383013	10	74	from	changes	1684:1690	arg1	transients					1717:1726	intracellular calcium transients	1695:1726	intracellular calcium transients	1695:1726	The dynamic and inducible nature of O-GlcNAcylation and the InsP(3)R isoform specificity suggest that this form of modification of InsP(3)R and subsequent changes in intracellular calcium transients are important in physiological and pathophysiological processes.
21383013	5	75	theme	monosaccharide	959:972	arg1	O-β-N-acetylglucosaminidase					923:949	O-β-N-acetylglucosaminidase	923:949	O-β-N-acetylglucosaminidase	923:949	Analysis of AR4-2J cells, a rat pancreatoma cell line expressing predominantly InsP(3)R-2, showed no detectable O-GlcNAcylation of InsP(3)R-2 and no significant functional changes despite the presence of the enzymes for addition (O-β-N-acetylglucosaminyltransferase) and removal (O-β-N-acetylglucosaminidase) of the monosaccharide.
21383013	5	75	theme	monosaccharide	959:972	arg1	O-β-N-acetylglucosaminyltransferase					873:907	O-β-N-acetylglucosaminyltransferase	873:907	O-β-N-acetylglucosaminyltransferase	873:907	Analysis of AR4-2J cells, a rat pancreatoma cell line expressing predominantly InsP(3)R-2, showed no detectable O-GlcNAcylation of InsP(3)R-2 and no significant functional changes despite the presence of the enzymes for addition (O-β-N-acetylglucosaminyltransferase) and removal (O-β-N-acetylglucosaminidase) of the monosaccharide.
21383013	5	75	theme	monosaccharide	959:972	arg1	removal					914:920	removal	914:920	removal (O-β-N-acetylglucosaminidase)	914:950	Analysis of AR4-2J cells, a rat pancreatoma cell line expressing predominantly InsP(3)R-2, showed no detectable O-GlcNAcylation of InsP(3)R-2 and no significant functional changes despite the presence of the enzymes for addition (O-β-N-acetylglucosaminyltransferase) and removal (O-β-N-acetylglucosaminidase) of the monosaccharide.
21383013	5	75	theme	monosaccharide	959:972	arg1	addition					863:870	addition	863:870	addition (O-β-N-acetylglucosaminyltransferase)	863:908	Analysis of AR4-2J cells, a rat pancreatoma cell line expressing predominantly InsP(3)R-2, showed no detectable O-GlcNAcylation of InsP(3)R-2 and no significant functional changes despite the presence of the enzymes for addition (O-β-N-acetylglucosaminyltransferase) and removal (O-β-N-acetylglucosaminidase) of the monosaccharide.
21383013	8	76	theme	O-GlcNAc	1282:1289	arg1	Addition					1270:1277	Addition	1270:1277	Addition of O-GlcNAc by O-β-N-acetylglucosaminyltransferase	1270:1328	Addition of O-GlcNAc by O-β-N-acetylglucosaminyltransferase increased InsP(3)R-3 single channel open probability.
21383013	10	77	from	transients	1717:1726	arg1	modification					1644:1655	modification	1644:1655	modification of InsP(3)R and subsequent changes in intracellular calcium transients	1644:1726	The dynamic and inducible nature of O-GlcNAcylation and the InsP(3)R isoform specificity suggest that this form of modification of InsP(3)R and subsequent changes in intracellular calcium transients are important in physiological and pathophysiological processes.
21383013	10	78	from	important	1732:1740	arg1	processes					1782:1790	physiological and pathophysiological processes	1745:1790	physiological and pathophysiological processes	1745:1790	The dynamic and inducible nature of O-GlcNAcylation and the InsP(3)R isoform specificity suggest that this form of modification of InsP(3)R and subsequent changes in intracellular calcium transients are important in physiological and pathophysiological processes.
21383013	5	79	theme	detectable	744:753	arg1	O-GlcNAcylation					755:769	no detectable O-GlcNAcylation	741:769	no detectable O-GlcNAcylation of InsP(3)R-2	741:783	Analysis of AR4-2J cells, a rat pancreatoma cell line expressing predominantly InsP(3)R-2, showed no detectable O-GlcNAcylation of InsP(3)R-2 and no significant functional changes despite the presence of the enzymes for addition (O-β-N-acetylglucosaminyltransferase) and removal (O-β-N-acetylglucosaminidase) of the monosaccharide.
21383013	8	80	theme	InsP	1340:1343	arg1	probability					1371:1381	InsP(3)R-3 single channel open probability	1340:1381	InsP(3)R-3 single channel open probability	1340:1381	Addition of O-GlcNAc by O-β-N-acetylglucosaminyltransferase increased InsP(3)R-3 single channel open probability.
21383013	5	81	theme	AR4-2J	655:660	arg1	line					692:695	a rat pancreatoma cell line	669:695	a rat pancreatoma cell line expressing predominantly InsP(3)R-2	669:731	Analysis of AR4-2J cells, a rat pancreatoma cell line expressing predominantly InsP(3)R-2, showed no detectable O-GlcNAcylation of InsP(3)R-2 and no significant functional changes despite the presence of the enzymes for addition (O-β-N-acetylglucosaminyltransferase) and removal (O-β-N-acetylglucosaminidase) of the monosaccharide.
21383013	5	81	theme	AR4-2J	655:660	arg1	cells					662:666	AR4-2J cells	655:666	AR4-2J cells	655:666	Analysis of AR4-2J cells, a rat pancreatoma cell line expressing predominantly InsP(3)R-2, showed no detectable O-GlcNAcylation of InsP(3)R-2 and no significant functional changes despite the presence of the enzymes for addition (O-β-N-acetylglucosaminyltransferase) and removal (O-β-N-acetylglucosaminidase) of the monosaccharide.
21383013	5	82	theme	significant	792:802	arg1	changes					815:821	no significant functional changes	789:821	no significant functional changes	789:821	Analysis of AR4-2J cells, a rat pancreatoma cell line expressing predominantly InsP(3)R-2, showed no detectable O-GlcNAcylation of InsP(3)R-2 and no significant functional changes despite the presence of the enzymes for addition (O-β-N-acetylglucosaminyltransferase) and removal (O-β-N-acetylglucosaminidase) of the monosaccharide.
21383013	1	83	with	isoforms	198:205	arg1	homology					226:233	>65% sequence homology	212:233	>65% sequence homology	212:233	The inositol 1,4,5-trisphosphate receptor (InsP(3)R), an intracellular calcium channel, has three isoforms with >65% sequence homology, yet the isoforms differ in their function and regulation by post-translational modifications.
21383013	6	84	theme	cholangiocarcinoma	1026:1043	arg1	cells					1011:1015	Mz-ChA-1 cells	1002:1015	Mz-ChA-1 cells	1002:1015	In contrast, InsP(3)R-3 in Mz-ChA-1 cells, a human cholangiocarcinoma cell line expressing predominantly InsP(3)R-3, was functionally modified by O-GlcNAcylation.
21383013	6	84	theme	cholangiocarcinoma	1026:1043	arg1	line					1050:1053	a human cholangiocarcinoma cell line	1018:1053	a human cholangiocarcinoma cell line expressing predominantly InsP(3)R-3	1018:1089	In contrast, InsP(3)R-3 in Mz-ChA-1 cells, a human cholangiocarcinoma cell line expressing predominantly InsP(3)R-3, was functionally modified by O-GlcNAcylation.
21383013	2	85	theme	β-N-acetylglucosamine	404:424	arg1	O-GlcNAcylation					441:455	O-GlcNAcylation	441:455	O-GlcNAcylation	441:455	We showed previously that InsP(3)R-1 is functionally modified by O-linked β-N-acetylglucosamine glycosylation (O-GlcNAcylation) (Rengifo, J., Gibson, C. J., Winkler, E., Collin, T., and Ehrlich, B. E. (2007) J. Neurosci.
21383013	2	85	theme	β-N-acetylglucosamine	404:424	arg1	glycosylation					426:438	O-linked β-N-acetylglucosamine glycosylation	395:438	O-linked β-N-acetylglucosamine glycosylation (O-GlcNAcylation)	395:456	We showed previously that InsP(3)R-1 is functionally modified by O-linked β-N-acetylglucosamine glycosylation (O-GlcNAcylation) (Rengifo, J., Gibson, C. J., Winkler, E., Collin, T., and Ehrlich, B. E. (2007) J. Neurosci.
21383013	0	86	theme	1,4,5-trisphosphate	44:62	arg1	receptor					64:71	the inositol 1,4,5-trisphosphate receptor	31:71	the inositol 1,4,5-trisphosphate receptor	31:71	Isoform-specific regulation of the inositol 1,4,5-trisphosphate receptor by O-linked glycosylation.
21383013	8	87	theme	R-3	1347:1349	arg1	probability					1371:1381	InsP(3)R-3 single channel open probability	1340:1381	InsP(3)R-3 single channel open probability	1340:1381	Addition of O-GlcNAc by O-β-N-acetylglucosaminyltransferase increased InsP(3)R-3 single channel open probability.
21383013	10	88	theme	isoform	1598:1604	arg1	specificity					1606:1616	isoform specificity	1598:1616	isoform specificity	1598:1616	The dynamic and inducible nature of O-GlcNAcylation and the InsP(3)R isoform specificity suggest that this form of modification of InsP(3)R and subsequent changes in intracellular calcium transients are important in physiological and pathophysiological processes.
21383013	8	89	theme	channel	1358:1364	arg1	probability					1371:1381	InsP(3)R-3 single channel open probability	1340:1381	InsP(3)R-3 single channel open probability	1340:1381	Addition of O-GlcNAc by O-β-N-acetylglucosaminyltransferase increased InsP(3)R-3 single channel open probability.
21383013	7	90	dep	measured	1244:1251	arg1	effect					1237:1242	opposite the effect	1224:1242	opposite the effect	1224:1242	Interestingly, the functional impact of O-GlcNAcylation on the InsP(3)R-3 channel was opposite the effect measured with InsP(3)R-1.
21383013	0	91	link	O-linked	76:83	arg1	glycosylation					85:97	O-linked glycosylation	76:97	O-linked glycosylation	76:97	Isoform-specific regulation of the inositol 1,4,5-trisphosphate receptor by O-linked glycosylation.
21383013	2	92	link	O-linked	395:402	arg1	O-GlcNAcylation					441:455	O-GlcNAcylation	441:455	O-GlcNAcylation	441:455	We showed previously that InsP(3)R-1 is functionally modified by O-linked β-N-acetylglucosamine glycosylation (O-GlcNAcylation) (Rengifo, J., Gibson, C. J., Winkler, E., Collin, T., and Ehrlich, B. E. (2007) J. Neurosci.
21383013	2	92	link	O-linked	395:402	arg1	glycosylation					426:438	O-linked β-N-acetylglucosamine glycosylation	395:438	O-linked β-N-acetylglucosamine glycosylation (O-GlcNAcylation)	395:456	We showed previously that InsP(3)R-1 is functionally modified by O-linked β-N-acetylglucosamine glycosylation (O-GlcNAcylation) (Rengifo, J., Gibson, C. J., Winkler, E., Collin, T., and Ehrlich, B. E. (2007) J. Neurosci.
21383013	1	93	theme	%	215:215	arg1	homology					226:233	>65% sequence homology	212:233	>65% sequence homology	212:233	The inositol 1,4,5-trisphosphate receptor (InsP(3)R), an intracellular calcium channel, has three isoforms with >65% sequence homology, yet the isoforms differ in their function and regulation by post-translational modifications.
21383013	9	94	from	reticulum	1518:1526	arg1	release					1489:1495	the InsP(3)-dependent calcium release	1459:1495	the InsP(3)-dependent calcium release from the endoplasmic reticulum	1459:1526	Incubation of Mz-ChA-1 cells in hyperglycemic medium caused an increase in the InsP(3)-dependent calcium release from the endoplasmic reticulum.
21383013	9	94	from	reticulum	1518:1526	arg1	increase					1447:1454	an increase	1444:1454	an increase in the InsP(3)-dependent calcium release from the endoplasmic reticulum	1444:1526	Incubation of Mz-ChA-1 cells in hyperglycemic medium caused an increase in the InsP(3)-dependent calcium release from the endoplasmic reticulum.
21383013	9	95	theme	cells	1407:1411	arg1	Incubation					1384:1393	Incubation	1384:1393	Incubation of Mz-ChA-1 cells in hyperglycemic medium	1384:1435	Incubation of Mz-ChA-1 cells in hyperglycemic medium caused an increase in the InsP(3)-dependent calcium release from the endoplasmic reticulum.
21383013	2	96	theme	InsP	356:359	arg1	R-1					363:365	InsP(3)R-1	356:365	InsP(3)R-1	356:365	We showed previously that InsP(3)R-1 is functionally modified by O-linked β-N-acetylglucosamine glycosylation (O-GlcNAcylation) (Rengifo, J., Gibson, C. J., Winkler, E., Collin, T., and Ehrlich, B. E. (2007) J. Neurosci.
21383013	3	97	dep	27	551:552	arg1	13813-13821					555:565	13813-13821	555:565	13813-13821	555:565	27, 13813-13821).
18077693	7	0	theme	O-GlcNAc	1080:1087	arg1	addition					1068:1075	the addition	1064:1075	the addition of O-GlcNAc	1064:1087	We found that channel activity was decreased by the addition of O-GlcNAc and that this decrease was reversed by removal of the sugar.
18077693	5	1	theme	Ca2+	838:841	arg1	transients					843:852	intracellular Ca2+ transients	824:852	intracellular Ca2+ transients	824:852	We monitored the effects of this modification on InsP3R function at the single-channel level and on intracellular Ca2+ transients.
18077693	3	2	link	O-linked	433:440	arg1	glycosylation					442:454	O-linked glycosylation	433:454	O-linked glycosylation of serine or threonine residues with beta-N-acetylglucosamine (O-GlcNAc)	433:527	We report that the InsP3R-I is modified by O-linked glycosylation of serine or threonine residues with beta-N-acetylglucosamine (O-GlcNAc).
18077693	1	3	theme	many	227:230	arg1	neurons					262:268	central neurons	254:268	central neurons	254:268	The inositol 1,4,5-trisphosphate (InsP3) receptor type I (InsP3R-I) is the principle channel for intracellular calcium (Ca2+) release in many cell types, including central neurons.
18077693	1	3	theme	many	227:230	arg1	types					237:241	many cell types	227:241	many cell types	227:241	The inositol 1,4,5-trisphosphate (InsP3) receptor type I (InsP3R-I) is the principle channel for intracellular calcium (Ca2+) release in many cell types, including central neurons.
18077693	6	4	theme	Single-channel	855:868	arg1	activity					870:877	Single-channel activity	855:877	Single-channel activity	855:877	Single-channel activity was monitored with InsP3R incorporated into bilayers; Ca2+ signaling was monitored using cells loaded with a Ca2+-sensitive fluorophore.
18077693	3	5	theme	threonine	469:477	arg1	glycosylation					442:454	O-linked glycosylation	433:454	O-linked glycosylation of serine or threonine residues with beta-N-acetylglucosamine (O-GlcNAc)	433:527	We report that the InsP3R-I is modified by O-linked glycosylation of serine or threonine residues with beta-N-acetylglucosamine (O-GlcNAc).
18077693	1	6	theme	cell	232:235	arg1	neurons					262:268	central neurons	254:268	central neurons	254:268	The inositol 1,4,5-trisphosphate (InsP3) receptor type I (InsP3R-I) is the principle channel for intracellular calcium (Ca2+) release in many cell types, including central neurons.
18077693	1	6	theme	cell	232:235	arg1	types					237:241	many cell types	227:241	many cell types	227:241	The inositol 1,4,5-trisphosphate (InsP3) receptor type I (InsP3R-I) is the principle channel for intracellular calcium (Ca2+) release in many cell types, including central neurons.
18077693	4	7	theme	loading	693:699	arg1	cells					701:705	loading cells	693:705	loading cells with UDP-GlcNAc	693:721	The level of O-GlcNAcylation can be altered in vitro by the addition of the enzymes which add [OGT (O-GlcNActransferase)] or remove (O-GlcNAcase) this sugar or by loading cells with UDP-GlcNAc.
18077693	3	8	mod	modified	421:428	arg3	glycosylation					442:454	O-linked glycosylation	433:454	O-linked glycosylation of serine or threonine residues with beta-N-acetylglucosamine (O-GlcNAc)	433:527	We report that the InsP3R-I is modified by O-linked glycosylation of serine or threonine residues with beta-N-acetylglucosamine (O-GlcNAc).
18077693	3	8	mod	modified	421:428	arg1	InsP3R-I					409:416	the InsP3R-I	405:416	the InsP3R-I	405:416	We report that the InsP3R-I is modified by O-linked glycosylation of serine or threonine residues with beta-N-acetylglucosamine (O-GlcNAc).
18077693	4	9	theme	enzymes	606:612	arg1	addition					590:597	the addition	586:597	the addition of the enzymes which add [OGT (O-GlcNActransferase)] or remove (O-GlcNAcase) this sugar	586:685	The level of O-GlcNAcylation can be altered in vitro by the addition of the enzymes which add [OGT (O-GlcNActransferase)] or remove (O-GlcNAcase) this sugar or by loading cells with UDP-GlcNAc.
18077693	5	10	theme	InsP3R	773:778	arg1	function					780:787	InsP3R function	773:787	InsP3R function at the single-channel level	773:815	We monitored the effects of this modification on InsP3R function at the single-channel level and on intracellular Ca2+ transients.
18077693	8	11	theme	attenuated	1197:1206	arg1	response					1208:1215	an attenuated response	1194:1215	an attenuated response to uncaging of InsP3	1194:1236	Similarly, cells loaded with UDP-GlcNAc had an attenuated response to uncaging of InsP3.
18077693	7	12	theme	sugar	1143:1147	arg1	removal					1128:1134	removal	1128:1134	removal of the sugar	1128:1147	We found that channel activity was decreased by the addition of O-GlcNAc and that this decrease was reversed by removal of the sugar.
18077693	5	13	from	effects	741:747	arg1	function					780:787	InsP3R function	773:787	InsP3R function at the single-channel level	773:815	We monitored the effects of this modification on InsP3R function at the single-channel level and on intracellular Ca2+ transients.
18077693	5	13	from	effects	741:747	arg1	transients					843:852	intracellular Ca2+ transients	824:852	intracellular Ca2+ transients	824:852	We monitored the effects of this modification on InsP3R function at the single-channel level and on intracellular Ca2+ transients.
18077693	3	14	with	glycosylation	442:454	arg1	O-GlcNAc					519:526	O-GlcNAc	519:526	O-GlcNAc	519:526	We report that the InsP3R-I is modified by O-linked glycosylation of serine or threonine residues with beta-N-acetylglucosamine (O-GlcNAc).
18077693	3	14	with	glycosylation	442:454	arg1	beta-N-acetylglucosamine					493:516	beta-N-acetylglucosamine	493:516	beta-N-acetylglucosamine (O-GlcNAc)	493:527	We report that the InsP3R-I is modified by O-linked glycosylation of serine or threonine residues with beta-N-acetylglucosamine (O-GlcNAc).
18077693	3	15	dep	serine	459:464	arg1	residues					479:486	residues	479:486	residues	479:486	We report that the InsP3R-I is modified by O-linked glycosylation of serine or threonine residues with beta-N-acetylglucosamine (O-GlcNAc).
18077693	5	16	theme	single-channel	796:809	arg1	level					811:815	the single-channel level	792:815	the single-channel level	792:815	We monitored the effects of this modification on InsP3R function at the single-channel level and on intracellular Ca2+ transients.
18077693	1	17	theme	principle	165:173	arg1	channel					175:181	the principle channel	161:181	the principle channel for intracellular calcium (Ca2+) release in many cell types, including central neurons	161:268	The inositol 1,4,5-trisphosphate (InsP3) receptor type I (InsP3R-I) is the principle channel for intracellular calcium (Ca2+) release in many cell types, including central neurons.
18077693	1	17	theme	principle	165:173	arg1	type					140:143	The inositol 1,4,5-trisphosphate (InsP3) receptor type I	90:145	The inositol 1,4,5-trisphosphate (InsP3) receptor type I (InsP3R-I)	90:156	The inositol 1,4,5-trisphosphate (InsP3) receptor type I (InsP3R-I) is the principle channel for intracellular calcium (Ca2+) release in many cell types, including central neurons.
18077693	6	18	theme	Ca2+	933:936	arg1	signaling					938:946	Ca2+ signaling	933:946	Ca2+ signaling	933:946	Single-channel activity was monitored with InsP3R incorporated into bilayers; Ca2+ signaling was monitored using cells loaded with a Ca2+-sensitive fluorophore.
18077693	8	19	contain	had	1190:1192	arg1	cells					1161:1165	cells	1161:1165	cells loaded with UDP-GlcNAc	1161:1188	Similarly, cells loaded with UDP-GlcNAc had an attenuated response to uncaging of InsP3.
18077693	8	19	contain	had	1190:1192	arg2	response					1208:1215	an attenuated response	1194:1215	an attenuated response to uncaging of InsP3	1194:1236	Similarly, cells loaded with UDP-GlcNAc had an attenuated response to uncaging of InsP3.
18077693	1	20	theme	inositol	94:101	arg1	InsP3					124:128	InsP3	124:128	InsP3	124:128	The inositol 1,4,5-trisphosphate (InsP3) receptor type I (InsP3R-I) is the principle channel for intracellular calcium (Ca2+) release in many cell types, including central neurons.
18077693	1	20	theme	inositol	94:101	arg1	1,4,5-trisphosphate					103:121	inositol 1,4,5-trisphosphate	94:121	The inositol 1,4,5-trisphosphate (InsP3) receptor type I (InsP3R-I)	90:156	The inositol 1,4,5-trisphosphate (InsP3) receptor type I (InsP3R-I) is the principle channel for intracellular calcium (Ca2+) release in many cell types, including central neurons.
18077693	2	21	theme	protein	333:339	arg1	partners					341:348	protein partners	333:348	protein partners	333:348	It is regulated by endogenous compounds like Ca2+ and ATP, by protein partners, and by posttranslational modification.
18077693	0	22	theme	inositol	18:25	arg1	type					56:59	the inositol 1,4,5-trisphosphate receptor type I	14:61	the inositol 1,4,5-trisphosphate receptor type I	14:61	Regulation of the inositol 1,4,5-trisphosphate receptor type I by O-GlcNAc glycosylation.
18077693	1	23	theme	central	254:260	arg1	neurons					262:268	central neurons	254:268	central neurons	254:268	The inositol 1,4,5-trisphosphate (InsP3) receptor type I (InsP3R-I) is the principle channel for intracellular calcium (Ca2+) release in many cell types, including central neurons.
18077693	7	24	theme	channel	1030:1036	arg1	activity					1038:1045	channel activity	1030:1045	channel activity	1030:1045	We found that channel activity was decreased by the addition of O-GlcNAc and that this decrease was reversed by removal of the sugar.
18077693	3	25	gly	glycosylation	442:454	arg1	threonine					469:477	threonine	469:477	threonine	469:477	We report that the InsP3R-I is modified by O-linked glycosylation of serine or threonine residues with beta-N-acetylglucosamine (O-GlcNAc).
18077693	3	25	gly	glycosylation	442:454	arg1	serine					459:464	serine	459:464	serine	459:464	We report that the InsP3R-I is modified by O-linked glycosylation of serine or threonine residues with beta-N-acetylglucosamine (O-GlcNAc).
18077693	5	26	theme	modification	757:768	arg1	effects					741:747	the effects	737:747	the effects of this modification on InsP3R function at the single-channel level and on intracellular Ca2+ transients	737:852	We monitored the effects of this modification on InsP3R function at the single-channel level and on intracellular Ca2+ transients.
18077693	4	27	with	cells	701:705	arg1	UDP-GlcNAc					712:721	UDP-GlcNAc	712:721	UDP-GlcNAc	712:721	The level of O-GlcNAcylation can be altered in vitro by the addition of the enzymes which add [OGT (O-GlcNActransferase)] or remove (O-GlcNAcase) this sugar or by loading cells with UDP-GlcNAc.
18077693	1	28	theme	intracellular	187:199	arg1	Ca2+					210:213	Ca2+	210:213	Ca2+	210:213	The inositol 1,4,5-trisphosphate (InsP3) receptor type I (InsP3R-I) is the principle channel for intracellular calcium (Ca2+) release in many cell types, including central neurons.
18077693	1	28	theme	intracellular	187:199	arg1	calcium					201:207	intracellular calcium	187:207	intracellular calcium (Ca2+) release in many cell types, including central neurons	187:268	The inositol 1,4,5-trisphosphate (InsP3) receptor type I (InsP3R-I) is the principle channel for intracellular calcium (Ca2+) release in many cell types, including central neurons.
18077693	0	29	theme	receptor	47:54	arg1	type					56:59	the inositol 1,4,5-trisphosphate receptor type I	14:61	the inositol 1,4,5-trisphosphate receptor type I	14:61	Regulation of the inositol 1,4,5-trisphosphate receptor type I by O-GlcNAc glycosylation.
18077693	8	30	theme	InsP3	1232:1236	arg1	uncaging					1220:1227	uncaging	1220:1227	uncaging of InsP3	1220:1236	Similarly, cells loaded with UDP-GlcNAc had an attenuated response to uncaging of InsP3.
18077693	1	31	theme	calcium	201:207	arg1	release					216:222	intracellular calcium (Ca2+) release	187:222	intracellular calcium (Ca2+) release in many cell types, including central neurons	187:268	The inositol 1,4,5-trisphosphate (InsP3) receptor type I (InsP3R-I) is the principle channel for intracellular calcium (Ca2+) release in many cell types, including central neurons.
18077693	2	32	theme	posttranslational	358:374	arg1	modification					376:387	posttranslational modification	358:387	posttranslational modification	358:387	It is regulated by endogenous compounds like Ca2+ and ATP, by protein partners, and by posttranslational modification.
18077693	0	33	theme	1,4,5-trisphosphate	27:45	arg1	type					56:59	the inositol 1,4,5-trisphosphate receptor type I	14:61	the inositol 1,4,5-trisphosphate receptor type I	14:61	Regulation of the inositol 1,4,5-trisphosphate receptor type I by O-GlcNAc glycosylation.
18077693	4	34	theme	O-GlcNAcylation	543:557	arg1	level					534:538	The level	530:538	The level of O-GlcNAcylation	530:557	The level of O-GlcNAcylation can be altered in vitro by the addition of the enzymes which add [OGT (O-GlcNActransferase)] or remove (O-GlcNAcase) this sugar or by loading cells with UDP-GlcNAc.
18077693	6	35	theme	Ca2+-sensitive	988:1001	arg1	fluorophore					1003:1013	a Ca2+-sensitive fluorophore	986:1013	a Ca2+-sensitive fluorophore	986:1013	Single-channel activity was monitored with InsP3R incorporated into bilayers; Ca2+ signaling was monitored using cells loaded with a Ca2+-sensitive fluorophore.
18077693	9	36	theme	InsP3R-I	1312:1319	arg1	regulator					1295:1303	an important regulator	1282:1303	an important regulator of the InsP3R-I	1282:1319	These results show that O-GlcNAcylation is an important regulator of the InsP3R-I and suggest a mechanism for neuronal dysfunction under conditions in which O-GlcNAc is high, such as diabetes or physiological stress.
18077693	9	36	theme	InsP3R-I	1312:1319	arg1	O-GlcNAcylation					1263:1277	O-GlcNAcylation	1263:1277	O-GlcNAcylation	1263:1277	These results show that O-GlcNAcylation is an important regulator of the InsP3R-I and suggest a mechanism for neuronal dysfunction under conditions in which O-GlcNAc is high, such as diabetes or physiological stress.
18077693	1	37	from	release	216:222	arg1	neurons					262:268	central neurons	254:268	central neurons	254:268	The inositol 1,4,5-trisphosphate (InsP3) receptor type I (InsP3R-I) is the principle channel for intracellular calcium (Ca2+) release in many cell types, including central neurons.
18077693	1	37	from	release	216:222	arg1	types					237:241	many cell types	227:241	many cell types	227:241	The inositol 1,4,5-trisphosphate (InsP3) receptor type I (InsP3R-I) is the principle channel for intracellular calcium (Ca2+) release in many cell types, including central neurons.
18077693	9	38	theme	important	1285:1293	arg1	regulator					1295:1303	an important regulator	1282:1303	an important regulator of the InsP3R-I	1282:1319	These results show that O-GlcNAcylation is an important regulator of the InsP3R-I and suggest a mechanism for neuronal dysfunction under conditions in which O-GlcNAc is high, such as diabetes or physiological stress.
18077693	9	38	theme	important	1285:1293	arg1	O-GlcNAcylation					1263:1277	O-GlcNAcylation	1263:1277	O-GlcNAcylation	1263:1277	These results show that O-GlcNAcylation is an important regulator of the InsP3R-I and suggest a mechanism for neuronal dysfunction under conditions in which O-GlcNAc is high, such as diabetes or physiological stress.
18077693	0	39	theme	type	56:59	arg1	Regulation					0:9	Regulation	0:9	Regulation of the inositol 1,4,5-trisphosphate receptor type I by O-GlcNAc glycosylation.	0:88	Regulation of the inositol 1,4,5-trisphosphate receptor type I by O-GlcNAc glycosylation.
18077693	9	40	from	conditions	1376:1385	arg1	high					1408:1411	high	1408:1411	high	1408:1411	These results show that O-GlcNAcylation is an important regulator of the InsP3R-I and suggest a mechanism for neuronal dysfunction under conditions in which O-GlcNAc is high, such as diabetes or physiological stress.
18077693	3	41	theme	serine	459:464	arg1	glycosylation					442:454	O-linked glycosylation	433:454	O-linked glycosylation of serine or threonine residues with beta-N-acetylglucosamine (O-GlcNAc)	433:527	We report that the InsP3R-I is modified by O-linked glycosylation of serine or threonine residues with beta-N-acetylglucosamine (O-GlcNAc).
18077693	1	42	theme	receptor	131:138	arg1	type					140:143	The inositol 1,4,5-trisphosphate (InsP3) receptor type I	90:145	The inositol 1,4,5-trisphosphate (InsP3) receptor type I (InsP3R-I)	90:156	The inositol 1,4,5-trisphosphate (InsP3) receptor type I (InsP3R-I) is the principle channel for intracellular calcium (Ca2+) release in many cell types, including central neurons.
18077693	1	42	theme	receptor	131:138	arg1	InsP3R-I					148:155	InsP3R-I	148:155	InsP3R-I	148:155	The inositol 1,4,5-trisphosphate (InsP3) receptor type I (InsP3R-I) is the principle channel for intracellular calcium (Ca2+) release in many cell types, including central neurons.
18077693	1	42	theme	receptor	131:138	arg1	channel					175:181	the principle channel	161:181	the principle channel for intracellular calcium (Ca2+) release in many cell types, including central neurons	161:268	The inositol 1,4,5-trisphosphate (InsP3) receptor type I (InsP3R-I) is the principle channel for intracellular calcium (Ca2+) release in many cell types, including central neurons.
18077693	1	43	theme	1,4,5-trisphosphate	103:121	arg1	receptor					131:138	The inositol 1,4,5-trisphosphate (InsP3) receptor	90:138	The inositol 1,4,5-trisphosphate (InsP3) receptor type I (InsP3R-I)	90:156	The inositol 1,4,5-trisphosphate (InsP3) receptor type I (InsP3R-I) is the principle channel for intracellular calcium (Ca2+) release in many cell types, including central neurons.
18077693	4	44	dep	[OGT	624:627	arg1	sugar					681:685	this sugar	676:685	this sugar	676:685	The level of O-GlcNAcylation can be altered in vitro by the addition of the enzymes which add [OGT (O-GlcNActransferase)] or remove (O-GlcNAcase) this sugar or by loading cells with UDP-GlcNAc.
18077693	5	45	from	level	811:815	arg1	function					780:787	InsP3R function	773:787	InsP3R function at the single-channel level	773:815	We monitored the effects of this modification on InsP3R function at the single-channel level and on intracellular Ca2+ transients.
18077693	2	46	theme	endogenous	290:299	arg1	compounds					301:309	endogenous compounds	290:309	endogenous compounds like Ca2+ and ATP	290:327	It is regulated by endogenous compounds like Ca2+ and ATP, by protein partners, and by posttranslational modification.
18077693	3	47	theme	O-linked	433:440	arg1	glycosylation					442:454	O-linked glycosylation	433:454	O-linked glycosylation of serine or threonine residues with beta-N-acetylglucosamine (O-GlcNAc)	433:527	We report that the InsP3R-I is modified by O-linked glycosylation of serine or threonine residues with beta-N-acetylglucosamine (O-GlcNAc).
18077693	0	48	theme	O-GlcNAc	66:73	arg1	glycosylation					75:87	O-GlcNAc glycosylation	66:87	O-GlcNAc glycosylation	66:87	Regulation of the inositol 1,4,5-trisphosphate receptor type I by O-GlcNAc glycosylation.
18077693	9	49	from	high	1408:1411	arg1	stress					1448:1453	physiological stress	1434:1453	physiological stress	1434:1453	These results show that O-GlcNAcylation is an important regulator of the InsP3R-I and suggest a mechanism for neuronal dysfunction under conditions in which O-GlcNAc is high, such as diabetes or physiological stress.
18077693	9	49	from	high	1408:1411	arg1	conditions					1376:1385	conditions	1376:1385	conditions	1376:1385	These results show that O-GlcNAcylation is an important regulator of the InsP3R-I and suggest a mechanism for neuronal dysfunction under conditions in which O-GlcNAc is high, such as diabetes or physiological stress.
18077693	9	49	from	high	1408:1411	arg1	diabetes					1422:1429	diabetes	1422:1429	diabetes	1422:1429	These results show that O-GlcNAcylation is an important regulator of the InsP3R-I and suggest a mechanism for neuronal dysfunction under conditions in which O-GlcNAc is high, such as diabetes or physiological stress.
18077693	9	50	theme	physiological	1434:1446	arg1	stress					1448:1453	physiological stress	1434:1453	physiological stress	1434:1453	These results show that O-GlcNAcylation is an important regulator of the InsP3R-I and suggest a mechanism for neuronal dysfunction under conditions in which O-GlcNAc is high, such as diabetes or physiological stress.
18077693	5	51	theme	intracellular	824:836	arg1	transients					843:852	intracellular Ca2+ transients	824:852	intracellular Ca2+ transients	824:852	We monitored the effects of this modification on InsP3R function at the single-channel level and on intracellular Ca2+ transients.
18077693	9	52	theme	neuronal	1349:1356	arg1	dysfunction					1358:1368	neuronal dysfunction	1349:1368	neuronal dysfunction	1349:1368	These results show that O-GlcNAcylation is an important regulator of the InsP3R-I and suggest a mechanism for neuronal dysfunction under conditions in which O-GlcNAc is high, such as diabetes or physiological stress.
23103942	2	0	theme	transfer	541:548	arg1	mechanism					519:527	a new catalytic mechanism	503:527	a new catalytic mechanism	503:527	Through crystallographic snapshots and mechanism-inspired chemical probes, we define how human OGT recognizes the sugar donor and acceptor peptide and uses a new catalytic mechanism of glycosyl transfer, involving the sugar donor α-phosphate as the catalytic base as well as an essential lysine.
23103942	3	1	theme	bulky	741:745	arg1	substrate					764:772	a bulky protein acceptor substrate	739:772	a bulky protein acceptor substrate	739:772	This mechanism seems to be a unique evolutionary solution to the spatial constraints imposed by a bulky protein acceptor substrate and explains the unexpected specificity of a recently reported metabolic OGT inhibitor.
23103942	2	2	theme	glycosyl	532:539	arg1	transfer					541:548	glycosyl transfer	532:548	glycosyl transfer	532:548	Through crystallographic snapshots and mechanism-inspired chemical probes, we define how human OGT recognizes the sugar donor and acceptor peptide and uses a new catalytic mechanism of glycosyl transfer, involving the sugar donor α-phosphate as the catalytic base as well as an essential lysine.
23103942	1	3	theme	unknown	289:295	arg1	mechanisms					297:306	unknown mechanisms	289:306	unknown mechanisms of transfer and substrate recognition	289:344	Protein O-GlcNAcylation is an essential post-translational modification on hundreds of intracellular proteins in metazoa, catalyzed by O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) using unknown mechanisms of transfer and substrate recognition.
23103942	1	4	from	metazoa	201:207	arg1	hundreds					163:170	hundreds	163:170	hundreds of intracellular proteins in metazoa	163:207	Protein O-GlcNAcylation is an essential post-translational modification on hundreds of intracellular proteins in metazoa, catalyzed by O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) using unknown mechanisms of transfer and substrate recognition.
23103942	2	5	theme	donor	571:575	arg1	base					606:609	the catalytic base	592:609	the catalytic base as well as an essential lysine	592:640	Through crystallographic snapshots and mechanism-inspired chemical probes, we define how human OGT recognizes the sugar donor and acceptor peptide and uses a new catalytic mechanism of glycosyl transfer, involving the sugar donor α-phosphate as the catalytic base as well as an essential lysine.
23103942	2	5	theme	donor	571:575	arg1	lysine					635:640	an essential lysine	622:640	the catalytic base as well as an essential lysine	592:640	Through crystallographic snapshots and mechanism-inspired chemical probes, we define how human OGT recognizes the sugar donor and acceptor peptide and uses a new catalytic mechanism of glycosyl transfer, involving the sugar donor α-phosphate as the catalytic base as well as an essential lysine.
23103942	2	5	theme	donor	571:575	arg1	α-phosphate					577:587	the sugar donor α-phosphate	561:587	the sugar donor α-phosphate	561:587	Through crystallographic snapshots and mechanism-inspired chemical probes, we define how human OGT recognizes the sugar donor and acceptor peptide and uses a new catalytic mechanism of glycosyl transfer, involving the sugar donor α-phosphate as the catalytic base as well as an essential lysine.
23103942	2	6	theme	essential	625:633	arg1	lysine					635:640	an essential lysine	622:640	the catalytic base as well as an essential lysine	592:640	Through crystallographic snapshots and mechanism-inspired chemical probes, we define how human OGT recognizes the sugar donor and acceptor peptide and uses a new catalytic mechanism of glycosyl transfer, involving the sugar donor α-phosphate as the catalytic base as well as an essential lysine.
23103942	2	6	theme	essential	625:633	arg1	α-phosphate					577:587	the sugar donor α-phosphate	561:587	the sugar donor α-phosphate	561:587	Through crystallographic snapshots and mechanism-inspired chemical probes, we define how human OGT recognizes the sugar donor and acceptor peptide and uses a new catalytic mechanism of glycosyl transfer, involving the sugar donor α-phosphate as the catalytic base as well as an essential lysine.
23103942	2	7	theme	sugar	565:569	arg1	base					606:609	the catalytic base	592:609	the catalytic base as well as an essential lysine	592:640	Through crystallographic snapshots and mechanism-inspired chemical probes, we define how human OGT recognizes the sugar donor and acceptor peptide and uses a new catalytic mechanism of glycosyl transfer, involving the sugar donor α-phosphate as the catalytic base as well as an essential lysine.
23103942	2	7	theme	sugar	565:569	arg1	lysine					635:640	an essential lysine	622:640	the catalytic base as well as an essential lysine	592:640	Through crystallographic snapshots and mechanism-inspired chemical probes, we define how human OGT recognizes the sugar donor and acceptor peptide and uses a new catalytic mechanism of glycosyl transfer, involving the sugar donor α-phosphate as the catalytic base as well as an essential lysine.
23103942	2	7	theme	sugar	565:569	arg1	α-phosphate					577:587	the sugar donor α-phosphate	561:587	the sugar donor α-phosphate	561:587	Through crystallographic snapshots and mechanism-inspired chemical probes, we define how human OGT recognizes the sugar donor and acceptor peptide and uses a new catalytic mechanism of glycosyl transfer, involving the sugar donor α-phosphate as the catalytic base as well as an essential lysine.
23103942	0	8	from	participation	60:72	arg1	catalysis					77:85	catalysis	77:85	catalysis	77:85	O-GlcNAc transferase invokes nucleotide sugar pyrophosphate participation in catalysis.
23103942	1	9	from	proteins	189:196	arg1	metazoa					201:207	metazoa	201:207	metazoa	201:207	Protein O-GlcNAcylation is an essential post-translational modification on hundreds of intracellular proteins in metazoa, catalyzed by O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) using unknown mechanisms of transfer and substrate recognition.
23103942	1	10	theme	Protein	88:94	arg1	modification					147:158	an essential post-translational modification	115:158	an essential post-translational modification	115:158	Protein O-GlcNAcylation is an essential post-translational modification on hundreds of intracellular proteins in metazoa, catalyzed by O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) using unknown mechanisms of transfer and substrate recognition.
23103942	1	10	theme	Protein	88:94	arg1	O-GlcNAcylation					96:110	Protein O-GlcNAcylation	88:110	Protein O-GlcNAcylation	88:110	Protein O-GlcNAcylation is an essential post-translational modification on hundreds of intracellular proteins in metazoa, catalyzed by O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) using unknown mechanisms of transfer and substrate recognition.
23103942	3	11	theme	protein	747:753	arg1	substrate					764:772	a bulky protein acceptor substrate	739:772	a bulky protein acceptor substrate	739:772	This mechanism seems to be a unique evolutionary solution to the spatial constraints imposed by a bulky protein acceptor substrate and explains the unexpected specificity of a recently reported metabolic OGT inhibitor.
23103942	1	12	link	O-linked	223:230	arg1	OGT					278:280	OGT	278:280	OGT	278:280	Protein O-GlcNAcylation is an essential post-translational modification on hundreds of intracellular proteins in metazoa, catalyzed by O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) using unknown mechanisms of transfer and substrate recognition.
23103942	1	12	link	O-linked	223:230	arg1	transferase					265:275	O-linked β-N-acetylglucosamine (O-GlcNAc) transferase	223:275	O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) using unknown mechanisms of transfer and substrate recognition	223:344	Protein O-GlcNAcylation is an essential post-translational modification on hundreds of intracellular proteins in metazoa, catalyzed by O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) using unknown mechanisms of transfer and substrate recognition.
23103942	1	13	from	hundreds	163:170	arg1	metazoa					201:207	metazoa	201:207	metazoa	201:207	Protein O-GlcNAcylation is an essential post-translational modification on hundreds of intracellular proteins in metazoa, catalyzed by O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) using unknown mechanisms of transfer and substrate recognition.
23103942	3	14	theme	acceptor	755:762	arg1	substrate					764:772	a bulky protein acceptor substrate	739:772	a bulky protein acceptor substrate	739:772	This mechanism seems to be a unique evolutionary solution to the spatial constraints imposed by a bulky protein acceptor substrate and explains the unexpected specificity of a recently reported metabolic OGT inhibitor.
23103942	3	15	theme	unexpected	791:800	arg1	specificity					802:812	the unexpected specificity	787:812	the unexpected specificity of a recently reported metabolic OGT inhibitor	787:859	This mechanism seems to be a unique evolutionary solution to the spatial constraints imposed by a bulky protein acceptor substrate and explains the unexpected specificity of a recently reported metabolic OGT inhibitor.
23103942	0	16	theme	O-GlcNAc	0:7	arg1	transferase					9:19	O-GlcNAc transferase	0:19	O-GlcNAc transferase	0:19	O-GlcNAc transferase invokes nucleotide sugar pyrophosphate participation in catalysis.
23103942	1	17	theme	transfer	311:318	arg1	mechanisms					297:306	unknown mechanisms	289:306	unknown mechanisms of transfer and substrate recognition	289:344	Protein O-GlcNAcylation is an essential post-translational modification on hundreds of intracellular proteins in metazoa, catalyzed by O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) using unknown mechanisms of transfer and substrate recognition.
23103942	1	18	from	modification	147:158	arg1	hundreds					163:170	hundreds	163:170	hundreds of intracellular proteins in metazoa	163:207	Protein O-GlcNAcylation is an essential post-translational modification on hundreds of intracellular proteins in metazoa, catalyzed by O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) using unknown mechanisms of transfer and substrate recognition.
23103942	2	19	theme	crystallographic	355:370	arg1	snapshots					372:380	crystallographic snapshots	355:380	crystallographic snapshots	355:380	Through crystallographic snapshots and mechanism-inspired chemical probes, we define how human OGT recognizes the sugar donor and acceptor peptide and uses a new catalytic mechanism of glycosyl transfer, involving the sugar donor α-phosphate as the catalytic base as well as an essential lysine.
23103942	1	20	theme	O-linked	223:230	arg1	OGT					278:280	OGT	278:280	OGT	278:280	Protein O-GlcNAcylation is an essential post-translational modification on hundreds of intracellular proteins in metazoa, catalyzed by O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) using unknown mechanisms of transfer and substrate recognition.
23103942	1	20	theme	O-linked	223:230	arg1	transferase					265:275	O-linked β-N-acetylglucosamine (O-GlcNAc) transferase	223:275	O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) using unknown mechanisms of transfer and substrate recognition	223:344	Protein O-GlcNAcylation is an essential post-translational modification on hundreds of intracellular proteins in metazoa, catalyzed by O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) using unknown mechanisms of transfer and substrate recognition.
23103942	0	21	theme	nucleotide	29:38	arg1	participation					60:72	nucleotide sugar pyrophosphate participation	29:72	nucleotide sugar pyrophosphate participation in catalysis	29:85	O-GlcNAc transferase invokes nucleotide sugar pyrophosphate participation in catalysis.
23103942	1	22	theme	essential	118:126	arg1	modification					147:158	an essential post-translational modification	115:158	an essential post-translational modification	115:158	Protein O-GlcNAcylation is an essential post-translational modification on hundreds of intracellular proteins in metazoa, catalyzed by O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) using unknown mechanisms of transfer and substrate recognition.
23103942	1	22	theme	essential	118:126	arg1	O-GlcNAcylation					96:110	Protein O-GlcNAcylation	88:110	Protein O-GlcNAcylation	88:110	Protein O-GlcNAcylation is an essential post-translational modification on hundreds of intracellular proteins in metazoa, catalyzed by O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) using unknown mechanisms of transfer and substrate recognition.
23103942	1	23	theme	β-N-acetylglucosamine	232:252	arg1	OGT					278:280	OGT	278:280	OGT	278:280	Protein O-GlcNAcylation is an essential post-translational modification on hundreds of intracellular proteins in metazoa, catalyzed by O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) using unknown mechanisms of transfer and substrate recognition.
23103942	1	23	theme	β-N-acetylglucosamine	232:252	arg1	transferase					265:275	O-linked β-N-acetylglucosamine (O-GlcNAc) transferase	223:275	O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) using unknown mechanisms of transfer and substrate recognition	223:344	Protein O-GlcNAcylation is an essential post-translational modification on hundreds of intracellular proteins in metazoa, catalyzed by O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) using unknown mechanisms of transfer and substrate recognition.
23103942	1	24	theme	substrate	324:332	arg1	recognition					334:344	substrate recognition	324:344	substrate recognition	324:344	Protein O-GlcNAcylation is an essential post-translational modification on hundreds of intracellular proteins in metazoa, catalyzed by O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) using unknown mechanisms of transfer and substrate recognition.
23103942	2	25	theme	catalytic	596:604	arg1	base					606:609	the catalytic base	592:609	the catalytic base as well as an essential lysine	592:640	Through crystallographic snapshots and mechanism-inspired chemical probes, we define how human OGT recognizes the sugar donor and acceptor peptide and uses a new catalytic mechanism of glycosyl transfer, involving the sugar donor α-phosphate as the catalytic base as well as an essential lysine.
23103942	2	25	theme	catalytic	596:604	arg1	α-phosphate					577:587	the sugar donor α-phosphate	561:587	the sugar donor α-phosphate	561:587	Through crystallographic snapshots and mechanism-inspired chemical probes, we define how human OGT recognizes the sugar donor and acceptor peptide and uses a new catalytic mechanism of glycosyl transfer, involving the sugar donor α-phosphate as the catalytic base as well as an essential lysine.
23103942	3	26	theme	evolutionary	679:690	arg1	solution					692:699	a unique evolutionary solution	670:699	a unique evolutionary solution to the spatial constraints imposed by a bulky protein acceptor substrate	670:772	This mechanism seems to be a unique evolutionary solution to the spatial constraints imposed by a bulky protein acceptor substrate and explains the unexpected specificity of a recently reported metabolic OGT inhibitor.
23103942	3	26	theme	evolutionary	679:690	arg1	mechanism					648:656	This mechanism	643:656	This mechanism	643:656	This mechanism seems to be a unique evolutionary solution to the spatial constraints imposed by a bulky protein acceptor substrate and explains the unexpected specificity of a recently reported metabolic OGT inhibitor.
23103942	1	27	theme	post-translational	128:145	arg1	modification					147:158	an essential post-translational modification	115:158	an essential post-translational modification	115:158	Protein O-GlcNAcylation is an essential post-translational modification on hundreds of intracellular proteins in metazoa, catalyzed by O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) using unknown mechanisms of transfer and substrate recognition.
23103942	1	27	theme	post-translational	128:145	arg1	O-GlcNAcylation					96:110	Protein O-GlcNAcylation	88:110	Protein O-GlcNAcylation	88:110	Protein O-GlcNAcylation is an essential post-translational modification on hundreds of intracellular proteins in metazoa, catalyzed by O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) using unknown mechanisms of transfer and substrate recognition.
23103942	0	28	theme	pyrophosphate	46:58	arg1	participation					60:72	nucleotide sugar pyrophosphate participation	29:72	nucleotide sugar pyrophosphate participation in catalysis	29:85	O-GlcNAc transferase invokes nucleotide sugar pyrophosphate participation in catalysis.
23103942	1	29	theme	recognition	334:344	arg1	mechanisms					297:306	unknown mechanisms	289:306	unknown mechanisms of transfer and substrate recognition	289:344	Protein O-GlcNAcylation is an essential post-translational modification on hundreds of intracellular proteins in metazoa, catalyzed by O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) using unknown mechanisms of transfer and substrate recognition.
23103942	2	30	theme	donor	467:471	arg1	peptide					486:492	the sugar donor and acceptor peptide	457:492	the sugar donor and acceptor peptide	457:492	Through crystallographic snapshots and mechanism-inspired chemical probes, we define how human OGT recognizes the sugar donor and acceptor peptide and uses a new catalytic mechanism of glycosyl transfer, involving the sugar donor α-phosphate as the catalytic base as well as an essential lysine.
23103942	2	31	theme	human	436:440	arg1	OGT					442:444	human OGT	436:444	human OGT	436:444	Through crystallographic snapshots and mechanism-inspired chemical probes, we define how human OGT recognizes the sugar donor and acceptor peptide and uses a new catalytic mechanism of glycosyl transfer, involving the sugar donor α-phosphate as the catalytic base as well as an essential lysine.
23103942	1	32	theme	O-GlcNAc	255:262	arg1	OGT					278:280	OGT	278:280	OGT	278:280	Protein O-GlcNAcylation is an essential post-translational modification on hundreds of intracellular proteins in metazoa, catalyzed by O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) using unknown mechanisms of transfer and substrate recognition.
23103942	1	32	theme	O-GlcNAc	255:262	arg1	transferase					265:275	O-linked β-N-acetylglucosamine (O-GlcNAc) transferase	223:275	O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) using unknown mechanisms of transfer and substrate recognition	223:344	Protein O-GlcNAcylation is an essential post-translational modification on hundreds of intracellular proteins in metazoa, catalyzed by O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) using unknown mechanisms of transfer and substrate recognition.
23103942	0	33	theme	sugar	40:44	arg1	participation					60:72	nucleotide sugar pyrophosphate participation	29:72	nucleotide sugar pyrophosphate participation in catalysis	29:85	O-GlcNAc transferase invokes nucleotide sugar pyrophosphate participation in catalysis.
23103942	2	34	theme	sugar	461:465	arg1	donor					467:471	the sugar donor	457:471	the sugar donor	457:471	Through crystallographic snapshots and mechanism-inspired chemical probes, we define how human OGT recognizes the sugar donor and acceptor peptide and uses a new catalytic mechanism of glycosyl transfer, involving the sugar donor α-phosphate as the catalytic base as well as an essential lysine.
23103942	2	35	theme	catalytic	509:517	arg1	mechanism					519:527	a new catalytic mechanism	503:527	a new catalytic mechanism	503:527	Through crystallographic snapshots and mechanism-inspired chemical probes, we define how human OGT recognizes the sugar donor and acceptor peptide and uses a new catalytic mechanism of glycosyl transfer, involving the sugar donor α-phosphate as the catalytic base as well as an essential lysine.
23103942	3	36	theme	reported	828:835	arg1	inhibitor					851:859	a recently reported metabolic OGT inhibitor	817:859	a recently reported metabolic OGT inhibitor	817:859	This mechanism seems to be a unique evolutionary solution to the spatial constraints imposed by a bulky protein acceptor substrate and explains the unexpected specificity of a recently reported metabolic OGT inhibitor.
23103942	3	37	theme	unique	672:677	arg1	solution					692:699	a unique evolutionary solution	670:699	a unique evolutionary solution to the spatial constraints imposed by a bulky protein acceptor substrate	670:772	This mechanism seems to be a unique evolutionary solution to the spatial constraints imposed by a bulky protein acceptor substrate and explains the unexpected specificity of a recently reported metabolic OGT inhibitor.
23103942	3	37	theme	unique	672:677	arg1	mechanism					648:656	This mechanism	643:656	This mechanism	643:656	This mechanism seems to be a unique evolutionary solution to the spatial constraints imposed by a bulky protein acceptor substrate and explains the unexpected specificity of a recently reported metabolic OGT inhibitor.
23103942	2	38	theme	new	505:507	arg1	mechanism					519:527	a new catalytic mechanism	503:527	a new catalytic mechanism	503:527	Through crystallographic snapshots and mechanism-inspired chemical probes, we define how human OGT recognizes the sugar donor and acceptor peptide and uses a new catalytic mechanism of glycosyl transfer, involving the sugar donor α-phosphate as the catalytic base as well as an essential lysine.
23103942	3	39	theme	spatial	708:714	arg1	constraints					716:726	the spatial constraints	704:726	the spatial constraints imposed by a bulky protein acceptor substrate	704:772	This mechanism seems to be a unique evolutionary solution to the spatial constraints imposed by a bulky protein acceptor substrate and explains the unexpected specificity of a recently reported metabolic OGT inhibitor.
23103942	2	40	theme	chemical	405:412	arg1	probes					414:419	mechanism-inspired chemical probes	386:419	mechanism-inspired chemical probes	386:419	Through crystallographic snapshots and mechanism-inspired chemical probes, we define how human OGT recognizes the sugar donor and acceptor peptide and uses a new catalytic mechanism of glycosyl transfer, involving the sugar donor α-phosphate as the catalytic base as well as an essential lysine.
23103942	2	41	theme	mechanism-inspired	386:403	arg1	probes					414:419	mechanism-inspired chemical probes	386:419	mechanism-inspired chemical probes	386:419	Through crystallographic snapshots and mechanism-inspired chemical probes, we define how human OGT recognizes the sugar donor and acceptor peptide and uses a new catalytic mechanism of glycosyl transfer, involving the sugar donor α-phosphate as the catalytic base as well as an essential lysine.
23103942	3	42	theme	inhibitor	851:859	arg1	specificity					802:812	the unexpected specificity	787:812	the unexpected specificity of a recently reported metabolic OGT inhibitor	787:859	This mechanism seems to be a unique evolutionary solution to the spatial constraints imposed by a bulky protein acceptor substrate and explains the unexpected specificity of a recently reported metabolic OGT inhibitor.
23103942	2	43	theme	acceptor	477:484	arg1	peptide					486:492	the sugar donor and acceptor peptide	457:492	the sugar donor and acceptor peptide	457:492	Through crystallographic snapshots and mechanism-inspired chemical probes, we define how human OGT recognizes the sugar donor and acceptor peptide and uses a new catalytic mechanism of glycosyl transfer, involving the sugar donor α-phosphate as the catalytic base as well as an essential lysine.
23103942	1	44	theme	intracellular	175:187	arg1	proteins					189:196	intracellular proteins	175:196	intracellular proteins in metazoa	175:207	Protein O-GlcNAcylation is an essential post-translational modification on hundreds of intracellular proteins in metazoa, catalyzed by O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) using unknown mechanisms of transfer and substrate recognition.
23103942	3	45	theme	metabolic	837:845	arg1	inhibitor					851:859	a recently reported metabolic OGT inhibitor	817:859	a recently reported metabolic OGT inhibitor	817:859	This mechanism seems to be a unique evolutionary solution to the spatial constraints imposed by a bulky protein acceptor substrate and explains the unexpected specificity of a recently reported metabolic OGT inhibitor.
23103942	1	46	theme	proteins	189:196	arg1	hundreds					163:170	hundreds	163:170	hundreds of intracellular proteins in metazoa	163:207	Protein O-GlcNAcylation is an essential post-translational modification on hundreds of intracellular proteins in metazoa, catalyzed by O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) using unknown mechanisms of transfer and substrate recognition.
23103942	3	47	theme	OGT	847:849	arg1	inhibitor					851:859	a recently reported metabolic OGT inhibitor	817:859	a recently reported metabolic OGT inhibitor	817:859	This mechanism seems to be a unique evolutionary solution to the spatial constraints imposed by a bulky protein acceptor substrate and explains the unexpected specificity of a recently reported metabolic OGT inhibitor.
22311971	0	0	from	substrates	168:177	arg1	analysis					99:106	kinetic analysis	91:106	kinetic analysis of O-GlcNAc transferase and O-GlcNAcase activity on protein substrates	91:177	Insights into O-linked N-acetylglucosamine ([0-9]O-GlcNAc) processing and dynamics through kinetic analysis of O-GlcNAc transferase and O-GlcNAcase activity on protein substrates.
22311971	3	1	theme	proteins	665:672	arg1	processing					636:645	human OGA (hOGA)-catalyzed processing	609:645	human OGA (hOGA)-catalyzed processing of these modified proteins	609:672	We found a remarkably invariant upper limit for k(cat)/K(m) values for human OGA (hOGA)-catalyzed processing of these modified proteins, which suggests that hOGA processing is driven by the GlcNAc moiety and is independent of the protein.
22311971	0	2	link	O-linked	14:21	arg1	N-acetylglucosamine					23:41	O-linked N-acetylglucosamine	14:41	O-linked N-acetylglucosamine ([0-9]O-GlcNAc) processing	14:68	Insights into O-linked N-acetylglucosamine ([0-9]O-GlcNAc) processing and dynamics through kinetic analysis of O-GlcNAc transferase and O-GlcNAcase activity on protein substrates.
22311971	0	2	link	O-linked	14:21	arg1	O-GlcNAc					49:56	[0-9]O-GlcNAc	44:56	[0-9]O-GlcNAc	44:56	Insights into O-linked N-acetylglucosamine ([0-9]O-GlcNAc) processing and dynamics through kinetic analysis of O-GlcNAc transferase and O-GlcNAcase activity on protein substrates.
22311971	5	3	dep	K	967:967	arg1	m					969:969	m	969:969	m	969:969	This was supported by the observation that K(m,app) values for UDP-GlcNAc varied considerably (from 1 μM to over 20 μM), depending on the protein substrate, suggesting that some OGT substrates will be nutrient-responsive, whereas others are constitutively modified.
22311971	5	3	dep	K	967:967	arg1	app					971:973	app	971:973	app	971:973	This was supported by the observation that K(m,app) values for UDP-GlcNAc varied considerably (from 1 μM to over 20 μM), depending on the protein substrate, suggesting that some OGT substrates will be nutrient-responsive, whereas others are constitutively modified.
22311971	7	4	located	observed	1717:1724	arg2	levels					1710:1715	CaMKIV O-GlcNAc levels	1694:1715	CaMKIV O-GlcNAc levels observed in cells	1694:1733	We show that changes in the specific activities of hOGT and hOGA measured in vitro on calcium/calmodulin-dependent kinase IV (CaMKIV) and its pseudophosphorylated form can account for previously reported changes in CaMKIV O-GlcNAc levels observed in cells.
22311971	7	4	located	observed	1717:1724	arg1	cells					1729:1733	cells	1729:1733	cells	1729:1733	We show that changes in the specific activities of hOGT and hOGA measured in vitro on calcium/calmodulin-dependent kinase IV (CaMKIV) and its pseudophosphorylated form can account for previously reported changes in CaMKIV O-GlcNAc levels observed in cells.
22311971	8	5	from	O-GlcNAc	1801:1808	arg1	proteins					1833:1840	proteins	1833:1840	proteins	1833:1840	These studies provide kinetic evidence for the interplay between O-GlcNAc and phosphorylation on proteins and indicate that these effects can be mediated by changes in hOGT and hOGA kinetic activity.
22311971	3	6	theme	upper	570:574	arg1	limit					576:580	a remarkably invariant upper limit	547:580	a remarkably invariant upper limit	547:580	We found a remarkably invariant upper limit for k(cat)/K(m) values for human OGA (hOGA)-catalyzed processing of these modified proteins, which suggests that hOGA processing is driven by the GlcNAc moiety and is independent of the protein.
22311971	1	7	theme	Cellular	180:187	arg1	levels					229:234	Cellular O-linked N-acetylglucosamine (O-GlcNAc) levels	180:234	Cellular O-linked N-acetylglucosamine (O-GlcNAc) levels	180:234	Cellular O-linked N-acetylglucosamine (O-GlcNAc) levels are modulated by two enzymes: uridine diphosphate-N-acetyl-D-glucosamine:polypeptidyltransferase (OGT) and O-GlcNAcase (OGA).
22311971	1	8	theme	N-acetylglucosamine	198:216	arg1	levels					229:234	Cellular O-linked N-acetylglucosamine (O-GlcNAc) levels	180:234	Cellular O-linked N-acetylglucosamine (O-GlcNAc) levels	180:234	Cellular O-linked N-acetylglucosamine (O-GlcNAc) levels are modulated by two enzymes: uridine diphosphate-N-acetyl-D-glucosamine:polypeptidyltransferase (OGT) and O-GlcNAcase (OGA).
22311971	0	9	theme	O-GlcNAc	111:118	arg1	transferase					120:130	O-GlcNAc transferase	111:130	O-GlcNAc transferase	111:130	Insights into O-linked N-acetylglucosamine ([0-9]O-GlcNAc) processing and dynamics through kinetic analysis of O-GlcNAc transferase and O-GlcNAcase activity on protein substrates.
22311971	0	10	theme	activity	148:155	arg1	analysis					99:106	kinetic analysis	91:106	kinetic analysis of O-GlcNAc transferase and O-GlcNAcase activity on protein substrates	91:177	Insights into O-linked N-acetylglucosamine ([0-9]O-GlcNAc) processing and dynamics through kinetic analysis of O-GlcNAc transferase and O-GlcNAcase activity on protein substrates.
22311971	5	11	theme	K	967:967	arg1	values					976:981	K(m,app) values	967:981	K(m,app) values for UDP-GlcNAc	967:996	This was supported by the observation that K(m,app) values for UDP-GlcNAc varied considerably (from 1 μM to over 20 μM), depending on the protein substrate, suggesting that some OGT substrates will be nutrient-responsive, whereas others are constitutively modified.
22311971	0	12	from	analysis	99:106	arg1	substrates					168:177	protein substrates	160:177	protein substrates	160:177	Insights into O-linked N-acetylglucosamine ([0-9]O-GlcNAc) processing and dynamics through kinetic analysis of O-GlcNAc transferase and O-GlcNAcase activity on protein substrates.
22311971	6	13	theme	target	1430:1435	arg1	proteins					1437:1444	target proteins	1430:1444	target proteins	1430:1444	The ratios of k(cat)/K(m) values obtained from hOGT and hOGA kinetic studies enable a prediction of the dynamic equilibrium position of O-GlcNAc levels that can be recapitulated in vitro and suggest the relative O-GlcNAc stoichiometries of target proteins in the absence of other factors.
22311971	7	14	theme	calcium/calmodulin-dependent	1565:1592	arg1	CaMKIV					1605:1610	CaMKIV	1605:1610	CaMKIV	1605:1610	We show that changes in the specific activities of hOGT and hOGA measured in vitro on calcium/calmodulin-dependent kinase IV (CaMKIV) and its pseudophosphorylated form can account for previously reported changes in CaMKIV O-GlcNAc levels observed in cells.
22311971	7	14	theme	calcium/calmodulin-dependent	1565:1592	arg1	kinase					1594:1599	calcium/calmodulin-dependent kinase IV	1565:1602	calcium/calmodulin-dependent kinase IV (CaMKIV)	1565:1611	We show that changes in the specific activities of hOGT and hOGA measured in vitro on calcium/calmodulin-dependent kinase IV (CaMKIV) and its pseudophosphorylated form can account for previously reported changes in CaMKIV O-GlcNAc levels observed in cells.
22311971	1	15	dep	diphosphate-N-acetyl-D-glucosamine	274:307	arg1	OGA					356:358	OGA	356:358	OGA	356:358	Cellular O-linked N-acetylglucosamine (O-GlcNAc) levels are modulated by two enzymes: uridine diphosphate-N-acetyl-D-glucosamine:polypeptidyltransferase (OGT) and O-GlcNAcase (OGA).
22311971	1	15	dep	diphosphate-N-acetyl-D-glucosamine	274:307	arg1	OGT					334:336	OGT	334:336	OGT	334:336	Cellular O-linked N-acetylglucosamine (O-GlcNAc) levels are modulated by two enzymes: uridine diphosphate-N-acetyl-D-glucosamine:polypeptidyltransferase (OGT) and O-GlcNAcase (OGA).
22311971	1	15	dep	diphosphate-N-acetyl-D-glucosamine	274:307	arg1	O-GlcNAcase					343:353	O-GlcNAcase	343:353	O-GlcNAcase (OGA)	343:359	Cellular O-linked N-acetylglucosamine (O-GlcNAc) levels are modulated by two enzymes: uridine diphosphate-N-acetyl-D-glucosamine:polypeptidyltransferase (OGT) and O-GlcNAcase (OGA).
22311971	1	15	dep	diphosphate-N-acetyl-D-glucosamine	274:307	arg1	polypeptidyltransferase					309:331	polypeptidyltransferase	309:331	polypeptidyltransferase (OGT)	309:337	Cellular O-linked N-acetylglucosamine (O-GlcNAc) levels are modulated by two enzymes: uridine diphosphate-N-acetyl-D-glucosamine:polypeptidyltransferase (OGT) and O-GlcNAcase (OGA).
22311971	3	16	theme	protein	768:774	arg1	independent					749:759	independent	749:759	independent	749:759	We found a remarkably invariant upper limit for k(cat)/K(m) values for human OGA (hOGA)-catalyzed processing of these modified proteins, which suggests that hOGA processing is driven by the GlcNAc moiety and is independent of the protein.
22311971	0	17	theme	protein	160:166	arg1	substrates					168:177	protein substrates	160:177	protein substrates	160:177	Insights into O-linked N-acetylglucosamine ([0-9]O-GlcNAc) processing and dynamics through kinetic analysis of O-GlcNAc transferase and O-GlcNAcase activity on protein substrates.
22311971	4	18	theme	protein	899:905	arg1	levels					916:921	fine tuning protein O-GlcNAc levels	887:921	fine tuning protein O-GlcNAc levels	887:921	Human OGT (hOGT) activity ranged more widely, by up to 15-fold, suggesting that hOGT is the senior partner in fine tuning protein O-GlcNAc levels.
22311971	4	19	from	partner	876:882	arg1	levels					916:921	fine tuning protein O-GlcNAc levels	887:921	fine tuning protein O-GlcNAc levels	887:921	Human OGT (hOGT) activity ranged more widely, by up to 15-fold, suggesting that hOGT is the senior partner in fine tuning protein O-GlcNAc levels.
22311971	6	20	theme	relative	1393:1400	arg1	stoichiometries					1411:1425	the relative O-GlcNAc stoichiometries	1389:1425	the relative O-GlcNAc stoichiometries of target proteins in the absence of other factors	1389:1476	The ratios of k(cat)/K(m) values obtained from hOGT and hOGA kinetic studies enable a prediction of the dynamic equilibrium position of O-GlcNAc levels that can be recapitulated in vitro and suggest the relative O-GlcNAc stoichiometries of target proteins in the absence of other factors.
22311971	2	21	theme	O-GlcNAc-modified	512:528	arg1	states					530:535	both unmodified and O-GlcNAc-modified states	492:535	both unmodified and O-GlcNAc-modified states	492:535	To quantitatively address the activity of these enzymes on protein substrates, we generated five structurally diverse proteins in both unmodified and O-GlcNAc-modified states.
22311971	4	22	theme	fine	887:890	arg1	levels					916:921	fine tuning protein O-GlcNAc levels	887:921	fine tuning protein O-GlcNAc levels	887:921	Human OGT (hOGT) activity ranged more widely, by up to 15-fold, suggesting that hOGT is the senior partner in fine tuning protein O-GlcNAc levels.
22311971	1	23	link	O-linked	189:196	arg1	O-GlcNAc					219:226	O-GlcNAc	219:226	O-GlcNAc	219:226	Cellular O-linked N-acetylglucosamine (O-GlcNAc) levels are modulated by two enzymes: uridine diphosphate-N-acetyl-D-glucosamine:polypeptidyltransferase (OGT) and O-GlcNAcase (OGA).
22311971	1	23	link	O-linked	189:196	arg1	N-acetylglucosamine					198:216	O-linked N-acetylglucosamine	189:216	Cellular O-linked N-acetylglucosamine (O-GlcNAc) levels	180:234	Cellular O-linked N-acetylglucosamine (O-GlcNAc) levels are modulated by two enzymes: uridine diphosphate-N-acetyl-D-glucosamine:polypeptidyltransferase (OGT) and O-GlcNAcase (OGA).
22311971	6	24	theme	other	1464:1468	arg1	factors					1470:1476	other factors	1464:1476	other factors	1464:1476	The ratios of k(cat)/K(m) values obtained from hOGT and hOGA kinetic studies enable a prediction of the dynamic equilibrium position of O-GlcNAc levels that can be recapitulated in vitro and suggest the relative O-GlcNAc stoichiometries of target proteins in the absence of other factors.
22311971	7	25	theme	specific	1507:1514	arg1	activities					1516:1525	the specific activities	1503:1525	the specific activities of hOGT and hOGA	1503:1542	We show that changes in the specific activities of hOGT and hOGA measured in vitro on calcium/calmodulin-dependent kinase IV (CaMKIV) and its pseudophosphorylated form can account for previously reported changes in CaMKIV O-GlcNAc levels observed in cells.
22311971	2	26	theme	diverse	472:478	arg1	proteins					480:487	five structurally diverse proteins	454:487	five structurally diverse proteins	454:487	To quantitatively address the activity of these enzymes on protein substrates, we generated five structurally diverse proteins in both unmodified and O-GlcNAc-modified states.
22311971	8	27	theme	kinetic	1918:1924	arg1	activity					1926:1933	hOGA kinetic activity	1913:1933	hOGA kinetic activity	1913:1933	These studies provide kinetic evidence for the interplay between O-GlcNAc and phosphorylation on proteins and indicate that these effects can be mediated by changes in hOGT and hOGA kinetic activity.
22311971	0	28	theme	O-linked	14:21	arg1	N-acetylglucosamine					23:41	O-linked N-acetylglucosamine	14:41	O-linked N-acetylglucosamine ([0-9]O-GlcNAc) processing	14:68	Insights into O-linked N-acetylglucosamine ([0-9]O-GlcNAc) processing and dynamics through kinetic analysis of O-GlcNAc transferase and O-GlcNAcase activity on protein substrates.
22311971	0	28	theme	O-linked	14:21	arg1	O-GlcNAc					49:56	[0-9]O-GlcNAc	44:56	[0-9]O-GlcNAc	44:56	Insights into O-linked N-acetylglucosamine ([0-9]O-GlcNAc) processing and dynamics through kinetic analysis of O-GlcNAc transferase and O-GlcNAcase activity on protein substrates.
22311971	6	29	dep	hOGT	1237:1240	arg1	studies					1259:1265	kinetic studies	1251:1265	kinetic studies	1251:1265	The ratios of k(cat)/K(m) values obtained from hOGT and hOGA kinetic studies enable a prediction of the dynamic equilibrium position of O-GlcNAc levels that can be recapitulated in vitro and suggest the relative O-GlcNAc stoichiometries of target proteins in the absence of other factors.
22311971	7	30	from	changes	1683:1689	arg1	levels					1710:1715	CaMKIV O-GlcNAc levels	1694:1715	CaMKIV O-GlcNAc levels observed in cells	1694:1733	We show that changes in the specific activities of hOGT and hOGA measured in vitro on calcium/calmodulin-dependent kinase IV (CaMKIV) and its pseudophosphorylated form can account for previously reported changes in CaMKIV O-GlcNAc levels observed in cells.
22311971	2	31	theme	unmodified	497:506	arg1	states					530:535	both unmodified and O-GlcNAc-modified states	492:535	both unmodified and O-GlcNAc-modified states	492:535	To quantitatively address the activity of these enzymes on protein substrates, we generated five structurally diverse proteins in both unmodified and O-GlcNAc-modified states.
22311971	3	32	theme	-catalyzed	625:634	arg1	processing					636:645	human OGA (hOGA)-catalyzed processing	609:645	human OGA (hOGA)-catalyzed processing of these modified proteins	609:672	We found a remarkably invariant upper limit for k(cat)/K(m) values for human OGA (hOGA)-catalyzed processing of these modified proteins, which suggests that hOGA processing is driven by the GlcNAc moiety and is independent of the protein.
22311971	4	33	theme	OGT	783:785	arg1	activity					794:801	Human OGT (hOGT) activity	777:801	Human OGT (hOGT) activity	777:801	Human OGT (hOGT) activity ranged more widely, by up to 15-fold, suggesting that hOGT is the senior partner in fine tuning protein O-GlcNAc levels.
22311971	4	34	theme	hOGT	788:791	arg1	activity					794:801	Human OGT (hOGT) activity	777:801	Human OGT (hOGT) activity	777:801	Human OGT (hOGT) activity ranged more widely, by up to 15-fold, suggesting that hOGT is the senior partner in fine tuning protein O-GlcNAc levels.
22311971	7	35	theme	reported	1674:1681	arg1	changes					1683:1689	previously reported changes	1663:1689	previously reported changes in CaMKIV O-GlcNAc levels observed in cells	1663:1733	We show that changes in the specific activities of hOGT and hOGA measured in vitro on calcium/calmodulin-dependent kinase IV (CaMKIV) and its pseudophosphorylated form can account for previously reported changes in CaMKIV O-GlcNAc levels observed in cells.
22311971	3	36	theme	modified	656:663	arg1	proteins					665:672	these modified proteins	650:672	these modified proteins	650:672	We found a remarkably invariant upper limit for k(cat)/K(m) values for human OGA (hOGA)-catalyzed processing of these modified proteins, which suggests that hOGA processing is driven by the GlcNAc moiety and is independent of the protein.
22311971	6	37	theme	O-GlcNAc	1326:1333	arg1	levels					1335:1340	O-GlcNAc levels	1326:1340	O-GlcNAc levels that can be recapitulated in vitro	1326:1375	The ratios of k(cat)/K(m) values obtained from hOGT and hOGA kinetic studies enable a prediction of the dynamic equilibrium position of O-GlcNAc levels that can be recapitulated in vitro and suggest the relative O-GlcNAc stoichiometries of target proteins in the absence of other factors.
22311971	6	38	theme	position	1314:1321	arg1	prediction					1276:1285	a prediction	1274:1285	a prediction of the dynamic equilibrium position of O-GlcNAc levels that can be recapitulated in vitro	1274:1375	The ratios of k(cat)/K(m) values obtained from hOGT and hOGA kinetic studies enable a prediction of the dynamic equilibrium position of O-GlcNAc levels that can be recapitulated in vitro and suggest the relative O-GlcNAc stoichiometries of target proteins in the absence of other factors.
22311971	5	39	theme	OGT	1102:1104	arg1	substrates					1106:1115	some OGT substrates	1097:1115	some OGT substrates	1097:1115	This was supported by the observation that K(m,app) values for UDP-GlcNAc varied considerably (from 1 μM to over 20 μM), depending on the protein substrate, suggesting that some OGT substrates will be nutrient-responsive, whereas others are constitutively modified.
22311971	6	40	theme	values	1216:1221	arg1	ratios					1194:1199	The ratios	1190:1199	The ratios of k(cat)/K(m) values obtained from hOGT and hOGA kinetic studies	1190:1265	The ratios of k(cat)/K(m) values obtained from hOGT and hOGA kinetic studies enable a prediction of the dynamic equilibrium position of O-GlcNAc levels that can be recapitulated in vitro and suggest the relative O-GlcNAc stoichiometries of target proteins in the absence of other factors.
22311971	6	41	theme	dynamic	1294:1300	arg1	position					1314:1321	the dynamic equilibrium position	1290:1321	the dynamic equilibrium position of O-GlcNAc levels that can be recapitulated in vitro	1290:1375	The ratios of k(cat)/K(m) values obtained from hOGT and hOGA kinetic studies enable a prediction of the dynamic equilibrium position of O-GlcNAc levels that can be recapitulated in vitro and suggest the relative O-GlcNAc stoichiometries of target proteins in the absence of other factors.
22311971	5	42	theme	protein	1062:1068	arg1	substrate					1070:1078	the protein substrate	1058:1078	the protein substrate	1058:1078	This was supported by the observation that K(m,app) values for UDP-GlcNAc varied considerably (from 1 μM to over 20 μM), depending on the protein substrate, suggesting that some OGT substrates will be nutrient-responsive, whereas others are constitutively modified.
22311971	7	43	theme	pseudophosphorylated	1621:1640	arg1	form					1642:1645	its pseudophosphorylated form	1617:1645	its pseudophosphorylated form	1617:1645	We show that changes in the specific activities of hOGT and hOGA measured in vitro on calcium/calmodulin-dependent kinase IV (CaMKIV) and its pseudophosphorylated form can account for previously reported changes in CaMKIV O-GlcNAc levels observed in cells.
22311971	1	44	theme	uridine	266:272	arg1	diphosphate-N-acetyl-D-glucosamine					274:307	uridine diphosphate-N-acetyl-D-glucosamine	266:307	two enzymes: uridine diphosphate-N-acetyl-D-glucosamine:polypeptidyltransferase (OGT) and O-GlcNAcase (OGA)	253:359	Cellular O-linked N-acetylglucosamine (O-GlcNAc) levels are modulated by two enzymes: uridine diphosphate-N-acetyl-D-glucosamine:polypeptidyltransferase (OGT) and O-GlcNAcase (OGA).
22311971	0	45	from	activity	148:155	arg1	substrates					168:177	protein substrates	160:177	protein substrates	160:177	Insights into O-linked N-acetylglucosamine ([0-9]O-GlcNAc) processing and dynamics through kinetic analysis of O-GlcNAc transferase and O-GlcNAcase activity on protein substrates.
22311971	3	46	theme	invariant	560:568	arg1	limit					576:580	a remarkably invariant upper limit	547:580	a remarkably invariant upper limit	547:580	We found a remarkably invariant upper limit for k(cat)/K(m) values for human OGA (hOGA)-catalyzed processing of these modified proteins, which suggests that hOGA processing is driven by the GlcNAc moiety and is independent of the protein.
22311971	3	47	theme	hOGA	695:698	arg1	processing					700:709	hOGA processing	695:709	hOGA processing	695:709	We found a remarkably invariant upper limit for k(cat)/K(m) values for human OGA (hOGA)-catalyzed processing of these modified proteins, which suggests that hOGA processing is driven by the GlcNAc moiety and is independent of the protein.
22311971	3	48	theme	cat	588:590	arg1	m					595:595	m	595:595	m	595:595	We found a remarkably invariant upper limit for k(cat)/K(m) values for human OGA (hOGA)-catalyzed processing of these modified proteins, which suggests that hOGA processing is driven by the GlcNAc moiety and is independent of the protein.
22311971	3	48	theme	cat	588:590	arg1	/K					592:593	k(cat)/K	586:593	k(cat)/K(m) values for human OGA (hOGA)-catalyzed processing of these modified proteins	586:672	We found a remarkably invariant upper limit for k(cat)/K(m) values for human OGA (hOGA)-catalyzed processing of these modified proteins, which suggests that hOGA processing is driven by the GlcNAc moiety and is independent of the protein.
22311971	1	49	theme	O-linked	189:196	arg1	O-GlcNAc					219:226	O-GlcNAc	219:226	O-GlcNAc	219:226	Cellular O-linked N-acetylglucosamine (O-GlcNAc) levels are modulated by two enzymes: uridine diphosphate-N-acetyl-D-glucosamine:polypeptidyltransferase (OGT) and O-GlcNAcase (OGA).
22311971	1	49	theme	O-linked	189:196	arg1	N-acetylglucosamine					198:216	O-linked N-acetylglucosamine	189:216	Cellular O-linked N-acetylglucosamine (O-GlcNAc) levels	180:234	Cellular O-linked N-acetylglucosamine (O-GlcNAc) levels are modulated by two enzymes: uridine diphosphate-N-acetyl-D-glucosamine:polypeptidyltransferase (OGT) and O-GlcNAcase (OGA).
22311971	2	50	from	activity	392:399	arg1	substrates					429:438	protein substrates	421:438	protein substrates	421:438	To quantitatively address the activity of these enzymes on protein substrates, we generated five structurally diverse proteins in both unmodified and O-GlcNAc-modified states.
22311971	3	51	theme	GlcNAc	728:733	arg1	moiety					735:740	the GlcNAc moiety	724:740	the GlcNAc moiety	724:740	We found a remarkably invariant upper limit for k(cat)/K(m) values for human OGA (hOGA)-catalyzed processing of these modified proteins, which suggests that hOGA processing is driven by the GlcNAc moiety and is independent of the protein.
22311971	8	52	theme	kinetic	1758:1764	arg1	evidence					1766:1773	kinetic evidence	1758:1773	kinetic evidence for the interplay between O-GlcNAc and phosphorylation on proteins	1758:1840	These studies provide kinetic evidence for the interplay between O-GlcNAc and phosphorylation on proteins and indicate that these effects can be mediated by changes in hOGT and hOGA kinetic activity.
22311971	3	53	theme	k	586:586	arg1	m					595:595	m	595:595	m	595:595	We found a remarkably invariant upper limit for k(cat)/K(m) values for human OGA (hOGA)-catalyzed processing of these modified proteins, which suggests that hOGA processing is driven by the GlcNAc moiety and is independent of the protein.
22311971	3	53	theme	k	586:586	arg1	/K					592:593	k(cat)/K	586:593	k(cat)/K(m) values for human OGA (hOGA)-catalyzed processing of these modified proteins	586:672	We found a remarkably invariant upper limit for k(cat)/K(m) values for human OGA (hOGA)-catalyzed processing of these modified proteins, which suggests that hOGA processing is driven by the GlcNAc moiety and is independent of the protein.
22311971	6	54	theme	k	1204:1204	arg1	m					1213:1213	m	1213:1213	m	1213:1213	The ratios of k(cat)/K(m) values obtained from hOGT and hOGA kinetic studies enable a prediction of the dynamic equilibrium position of O-GlcNAc levels that can be recapitulated in vitro and suggest the relative O-GlcNAc stoichiometries of target proteins in the absence of other factors.
22311971	6	54	theme	k	1204:1204	arg1	/K					1210:1211	k(cat)/K	1204:1211	k(cat)/K(m) values obtained from hOGT and hOGA kinetic studies	1204:1265	The ratios of k(cat)/K(m) values obtained from hOGT and hOGA kinetic studies enable a prediction of the dynamic equilibrium position of O-GlcNAc levels that can be recapitulated in vitro and suggest the relative O-GlcNAc stoichiometries of target proteins in the absence of other factors.
22311971	8	55	from	phosphorylation	1814:1828	arg1	proteins					1833:1840	proteins	1833:1840	proteins	1833:1840	These studies provide kinetic evidence for the interplay between O-GlcNAc and phosphorylation on proteins and indicate that these effects can be mediated by changes in hOGT and hOGA kinetic activity.
22311971	7	56	from	changes	1492:1498	arg1	activities					1516:1525	the specific activities	1503:1525	the specific activities of hOGT and hOGA	1503:1542	We show that changes in the specific activities of hOGT and hOGA measured in vitro on calcium/calmodulin-dependent kinase IV (CaMKIV) and its pseudophosphorylated form can account for previously reported changes in CaMKIV O-GlcNAc levels observed in cells.
22311971	3	57	theme	/K	592:593	arg1	values					598:603	k(cat)/K(m) values	586:603	k(cat)/K(m) values for human OGA (hOGA)-catalyzed processing of these modified proteins	586:672	We found a remarkably invariant upper limit for k(cat)/K(m) values for human OGA (hOGA)-catalyzed processing of these modified proteins, which suggests that hOGA processing is driven by the GlcNAc moiety and is independent of the protein.
22311971	6	58	theme	proteins	1437:1444	arg1	stoichiometries					1411:1425	the relative O-GlcNAc stoichiometries	1389:1425	the relative O-GlcNAc stoichiometries of target proteins in the absence of other factors	1389:1476	The ratios of k(cat)/K(m) values obtained from hOGT and hOGA kinetic studies enable a prediction of the dynamic equilibrium position of O-GlcNAc levels that can be recapitulated in vitro and suggest the relative O-GlcNAc stoichiometries of target proteins in the absence of other factors.
22311971	0	59	theme	transferase	120:130	arg1	analysis					99:106	kinetic analysis	91:106	kinetic analysis of O-GlcNAc transferase and O-GlcNAcase activity on protein substrates	91:177	Insights into O-linked N-acetylglucosamine ([0-9]O-GlcNAc) processing and dynamics through kinetic analysis of O-GlcNAc transferase and O-GlcNAcase activity on protein substrates.
22311971	6	60	theme	cat	1206:1208	arg1	m					1213:1213	m	1213:1213	m	1213:1213	The ratios of k(cat)/K(m) values obtained from hOGT and hOGA kinetic studies enable a prediction of the dynamic equilibrium position of O-GlcNAc levels that can be recapitulated in vitro and suggest the relative O-GlcNAc stoichiometries of target proteins in the absence of other factors.
22311971	6	60	theme	cat	1206:1208	arg1	/K					1210:1211	k(cat)/K	1204:1211	k(cat)/K(m) values obtained from hOGT and hOGA kinetic studies	1204:1265	The ratios of k(cat)/K(m) values obtained from hOGT and hOGA kinetic studies enable a prediction of the dynamic equilibrium position of O-GlcNAc levels that can be recapitulated in vitro and suggest the relative O-GlcNAc stoichiometries of target proteins in the absence of other factors.
22311971	1	61	dep	enzymes	257:263	arg1	diphosphate-N-acetyl-D-glucosamine					274:307	uridine diphosphate-N-acetyl-D-glucosamine	266:307	two enzymes: uridine diphosphate-N-acetyl-D-glucosamine:polypeptidyltransferase (OGT) and O-GlcNAcase (OGA)	253:359	Cellular O-linked N-acetylglucosamine (O-GlcNAc) levels are modulated by two enzymes: uridine diphosphate-N-acetyl-D-glucosamine:polypeptidyltransferase (OGT) and O-GlcNAcase (OGA).
22311971	6	62	theme	O-GlcNAc	1402:1409	arg1	stoichiometries					1411:1425	the relative O-GlcNAc stoichiometries	1389:1425	the relative O-GlcNAc stoichiometries of target proteins in the absence of other factors	1389:1476	The ratios of k(cat)/K(m) values obtained from hOGT and hOGA kinetic studies enable a prediction of the dynamic equilibrium position of O-GlcNAc levels that can be recapitulated in vitro and suggest the relative O-GlcNAc stoichiometries of target proteins in the absence of other factors.
22311971	4	63	theme	tuning	892:897	arg1	levels					916:921	fine tuning protein O-GlcNAc levels	887:921	fine tuning protein O-GlcNAc levels	887:921	Human OGT (hOGT) activity ranged more widely, by up to 15-fold, suggesting that hOGT is the senior partner in fine tuning protein O-GlcNAc levels.
22311971	4	64	dep	15-fold	832:838	arg1	to					829:830	to	829:830	to	829:830	Human OGT (hOGT) activity ranged more widely, by up to 15-fold, suggesting that hOGT is the senior partner in fine tuning protein O-GlcNAc levels.
22311971	6	65	from	stoichiometries	1411:1425	arg1	absence					1453:1459	the absence	1449:1459	the absence of other factors	1449:1476	The ratios of k(cat)/K(m) values obtained from hOGT and hOGA kinetic studies enable a prediction of the dynamic equilibrium position of O-GlcNAc levels that can be recapitulated in vitro and suggest the relative O-GlcNAc stoichiometries of target proteins in the absence of other factors.
22311971	4	66	theme	O-GlcNAc	907:914	arg1	levels					916:921	fine tuning protein O-GlcNAc levels	887:921	fine tuning protein O-GlcNAc levels	887:921	Human OGT (hOGT) activity ranged more widely, by up to 15-fold, suggesting that hOGT is the senior partner in fine tuning protein O-GlcNAc levels.
22311971	0	67	theme	kinetic	91:97	arg1	analysis					99:106	kinetic analysis	91:106	kinetic analysis of O-GlcNAc transferase and O-GlcNAcase activity on protein substrates	91:177	Insights into O-linked N-acetylglucosamine ([0-9]O-GlcNAc) processing and dynamics through kinetic analysis of O-GlcNAc transferase and O-GlcNAcase activity on protein substrates.
22311971	7	68	theme	hOGA	1539:1542	arg1	activities					1516:1525	the specific activities	1503:1525	the specific activities of hOGT and hOGA	1503:1542	We show that changes in the specific activities of hOGT and hOGA measured in vitro on calcium/calmodulin-dependent kinase IV (CaMKIV) and its pseudophosphorylated form can account for previously reported changes in CaMKIV O-GlcNAc levels observed in cells.
22311971	4	69	theme	senior	869:874	arg1	hOGT					857:860	hOGT	857:860	hOGT	857:860	Human OGT (hOGT) activity ranged more widely, by up to 15-fold, suggesting that hOGT is the senior partner in fine tuning protein O-GlcNAc levels.
22311971	4	69	theme	senior	869:874	arg1	partner					876:882	the senior partner	865:882	the senior partner in fine tuning protein O-GlcNAc levels	865:921	Human OGT (hOGT) activity ranged more widely, by up to 15-fold, suggesting that hOGT is the senior partner in fine tuning protein O-GlcNAc levels.
22311971	6	70	theme	/K	1210:1211	arg1	values					1216:1221	k(cat)/K(m) values	1204:1221	k(cat)/K(m) values obtained from hOGT and hOGA kinetic studies	1204:1265	The ratios of k(cat)/K(m) values obtained from hOGT and hOGA kinetic studies enable a prediction of the dynamic equilibrium position of O-GlcNAc levels that can be recapitulated in vitro and suggest the relative O-GlcNAc stoichiometries of target proteins in the absence of other factors.
22311971	6	71	theme	factors	1470:1476	arg1	absence					1453:1459	the absence	1449:1459	the absence of other factors	1449:1476	The ratios of k(cat)/K(m) values obtained from hOGT and hOGA kinetic studies enable a prediction of the dynamic equilibrium position of O-GlcNAc levels that can be recapitulated in vitro and suggest the relative O-GlcNAc stoichiometries of target proteins in the absence of other factors.
22311971	7	72	theme	hOGT	1530:1533	arg1	activities					1516:1525	the specific activities	1503:1525	the specific activities of hOGT and hOGA	1503:1542	We show that changes in the specific activities of hOGT and hOGA measured in vitro on calcium/calmodulin-dependent kinase IV (CaMKIV) and its pseudophosphorylated form can account for previously reported changes in CaMKIV O-GlcNAc levels observed in cells.
22311971	8	73	theme	hOGA	1913:1916	arg1	activity					1926:1933	hOGA kinetic activity	1913:1933	hOGA kinetic activity	1913:1933	These studies provide kinetic evidence for the interplay between O-GlcNAc and phosphorylation on proteins and indicate that these effects can be mediated by changes in hOGT and hOGA kinetic activity.
22311971	8	74	from	changes	1893:1899	arg1	activity					1926:1933	hOGA kinetic activity	1913:1933	hOGA kinetic activity	1913:1933	These studies provide kinetic evidence for the interplay between O-GlcNAc and phosphorylation on proteins and indicate that these effects can be mediated by changes in hOGT and hOGA kinetic activity.
22311971	8	74	from	changes	1893:1899	arg1	hOGT					1904:1907	hOGT	1904:1907	hOGT	1904:1907	These studies provide kinetic evidence for the interplay between O-GlcNAc and phosphorylation on proteins and indicate that these effects can be mediated by changes in hOGT and hOGA kinetic activity.
22311971	2	75	theme	enzymes	410:416	arg1	activity					392:399	the activity	388:399	the activity of these enzymes on protein substrates	388:438	To quantitatively address the activity of these enzymes on protein substrates, we generated five structurally diverse proteins in both unmodified and O-GlcNAc-modified states.
22311971	0	76	theme	O-GlcNAcase	136:146	arg1	activity					148:155	O-GlcNAcase activity	136:155	O-GlcNAcase activity	136:155	Insights into O-linked N-acetylglucosamine ([0-9]O-GlcNAc) processing and dynamics through kinetic analysis of O-GlcNAc transferase and O-GlcNAcase activity on protein substrates.
22311971	0	77	theme	N-acetylglucosamine	23:41	arg1	processing					59:68	O-linked N-acetylglucosamine ([0-9]O-GlcNAc) processing	14:68	O-linked N-acetylglucosamine ([0-9]O-GlcNAc) processing	14:68	Insights into O-linked N-acetylglucosamine ([0-9]O-GlcNAc) processing and dynamics through kinetic analysis of O-GlcNAc transferase and O-GlcNAcase activity on protein substrates.
22311971	6	78	theme	kinetic	1251:1257	arg1	studies					1259:1265	kinetic studies	1251:1265	kinetic studies	1251:1265	The ratios of k(cat)/K(m) values obtained from hOGT and hOGA kinetic studies enable a prediction of the dynamic equilibrium position of O-GlcNAc levels that can be recapitulated in vitro and suggest the relative O-GlcNAc stoichiometries of target proteins in the absence of other factors.
22311971	4	79	theme	Human	777:781	arg1	activity					794:801	Human OGT (hOGT) activity	777:801	Human OGT (hOGT) activity	777:801	Human OGT (hOGT) activity ranged more widely, by up to 15-fold, suggesting that hOGT is the senior partner in fine tuning protein O-GlcNAc levels.
22311971	2	80	theme	protein	421:427	arg1	substrates					429:438	protein substrates	421:438	protein substrates	421:438	To quantitatively address the activity of these enzymes on protein substrates, we generated five structurally diverse proteins in both unmodified and O-GlcNAc-modified states.
22311971	7	81	theme	CaMKIV	1694:1699	arg1	levels					1710:1715	CaMKIV O-GlcNAc levels	1694:1715	CaMKIV O-GlcNAc levels observed in cells	1694:1733	We show that changes in the specific activities of hOGT and hOGA measured in vitro on calcium/calmodulin-dependent kinase IV (CaMKIV) and its pseudophosphorylated form can account for previously reported changes in CaMKIV O-GlcNAc levels observed in cells.
22311971	6	82	theme	levels	1335:1340	arg1	position					1314:1321	the dynamic equilibrium position	1290:1321	the dynamic equilibrium position of O-GlcNAc levels that can be recapitulated in vitro	1290:1375	The ratios of k(cat)/K(m) values obtained from hOGT and hOGA kinetic studies enable a prediction of the dynamic equilibrium position of O-GlcNAc levels that can be recapitulated in vitro and suggest the relative O-GlcNAc stoichiometries of target proteins in the absence of other factors.
22311971	7	83	theme	O-GlcNAc	1701:1708	arg1	levels					1710:1715	CaMKIV O-GlcNAc levels	1694:1715	CaMKIV O-GlcNAc levels observed in cells	1694:1733	We show that changes in the specific activities of hOGT and hOGA measured in vitro on calcium/calmodulin-dependent kinase IV (CaMKIV) and its pseudophosphorylated form can account for previously reported changes in CaMKIV O-GlcNAc levels observed in cells.
22311971	0	84	from	transferase	120:130	arg1	substrates					168:177	protein substrates	160:177	protein substrates	160:177	Insights into O-linked N-acetylglucosamine ([0-9]O-GlcNAc) processing and dynamics through kinetic analysis of O-GlcNAc transferase and O-GlcNAcase activity on protein substrates.
22311971	6	85	theme	equilibrium	1302:1312	arg1	position					1314:1321	the dynamic equilibrium position	1290:1321	the dynamic equilibrium position of O-GlcNAc levels that can be recapitulated in vitro	1290:1375	The ratios of k(cat)/K(m) values obtained from hOGT and hOGA kinetic studies enable a prediction of the dynamic equilibrium position of O-GlcNAc levels that can be recapitulated in vitro and suggest the relative O-GlcNAc stoichiometries of target proteins in the absence of other factors.
29217192	3	0	theme	signaling	248:256	arg1	factor					263:268	another Hippo signaling core factor	234:268	another Hippo signaling core factor which could be O-GlcNAcylated	234:298	Here, we identified that besides YAP, AMOT was another Hippo signaling core factor which could be O-GlcNAcylated.
29217192	3	1	theme	core	258:261	arg1	factor					263:268	another Hippo signaling core factor	234:268	another Hippo signaling core factor which could be O-GlcNAcylated	234:298	Here, we identified that besides YAP, AMOT was another Hippo signaling core factor which could be O-GlcNAcylated.
29217192	0	2	theme	liver	58:62	arg1	malignancy					64:73	high glucose induced liver malignancy	37:73	high glucose induced liver malignancy	37:73	AMOT is required for YAP function in high glucose induced liver malignancy.
29217192	8	3	theme	regulated	869:877	arg1	factors					884:890	the aberrantly regulated core factors	854:890	the aberrantly regulated core factors in Hippo pathway	854:907	Targeting the aberrantly regulated core factors in Hippo pathway might be a more effective therapeutic approach for liver cancer associated with possibly diabetes.
29217192	8	4	theme	Hippo	895:899	arg1	pathway					901:907	Hippo pathway	895:907	Hippo pathway	895:907	Targeting the aberrantly regulated core factors in Hippo pathway might be a more effective therapeutic approach for liver cancer associated with possibly diabetes.
29217192	7	5	theme	glucose	829:835	arg1	level					837:841	high glucose level	824:841	high glucose level	824:841	Collectively, we have uncovered that AMOT acts as a YAP stimulator in high glucose level.
29217192	8	6	theme	effective	925:933	arg1	approach					947:954	a more effective therapeutic approach	918:954	a more effective therapeutic approach for liver cancer associated with possibly diabetes	918:1005	Targeting the aberrantly regulated core factors in Hippo pathway might be a more effective therapeutic approach for liver cancer associated with possibly diabetes.
29217192	5	7	theme	YAP	547:549	arg1	genes					538:542	target genes	531:542	target genes of YAP	531:549	We also found that HG stimulated nuclear accumulation, transcription activity, interaction with transcription factor and transcription of target genes of YAP via AMOT, while AMOT acted as a suppressor of YAP in normal glucose level.
29217192	5	8	from	level	619:623	arg1	AMOT					567:570	AMOT	567:570	AMOT	567:570	We also found that HG stimulated nuclear accumulation, transcription activity, interaction with transcription factor and transcription of target genes of YAP via AMOT, while AMOT acted as a suppressor of YAP in normal glucose level.
29217192	5	8	from	level	619:623	arg1	suppressor					583:592	a suppressor	581:592	a suppressor of YAP in normal glucose level	581:623	We also found that HG stimulated nuclear accumulation, transcription activity, interaction with transcription factor and transcription of target genes of YAP via AMOT, while AMOT acted as a suppressor of YAP in normal glucose level.
29217192	6	9	from	accumulation	676:687	arg1	STZ					722:724	STZ	722:724	STZ	722:724	Finally, we observed the upregulation and nuclear accumulation of AMOT and YAP in Streptozocin (STZ) induced high glucose mice.
29217192	6	9	from	accumulation	676:687	arg1	Streptozocin					708:719	Streptozocin	708:719	Streptozocin (STZ)	708:725	Finally, we observed the upregulation and nuclear accumulation of AMOT and YAP in Streptozocin (STZ) induced high glucose mice.
29217192	8	10	theme	core	879:882	arg1	factors					884:890	the aberrantly regulated core factors	854:890	the aberrantly regulated core factors in Hippo pathway	854:907	Targeting the aberrantly regulated core factors in Hippo pathway might be a more effective therapeutic approach for liver cancer associated with possibly diabetes.
29217192	5	11	theme	nuclear	426:432	arg1	accumulation					434:445	nuclear accumulation	426:445	nuclear accumulation	426:445	We also found that HG stimulated nuclear accumulation, transcription activity, interaction with transcription factor and transcription of target genes of YAP via AMOT, while AMOT acted as a suppressor of YAP in normal glucose level.
29217192	0	12	from	function	25:32	arg1	malignancy					64:73	high glucose induced liver malignancy	37:73	high glucose induced liver malignancy	37:73	AMOT is required for YAP function in high glucose induced liver malignancy.
29217192	8	13	theme	therapeutic	935:945	arg1	approach					947:954	a more effective therapeutic approach	918:954	a more effective therapeutic approach for liver cancer associated with possibly diabetes	918:1005	Targeting the aberrantly regulated core factors in Hippo pathway might be a more effective therapeutic approach for liver cancer associated with possibly diabetes.
29217192	7	14	theme	high	824:827	arg1	level					837:841	high glucose level	824:841	high glucose level	824:841	Collectively, we have uncovered that AMOT acts as a YAP stimulator in high glucose level.
29217192	5	15	with	interaction	472:482	arg1	factor					503:508	transcription factor	489:508	transcription factor	489:508	We also found that HG stimulated nuclear accumulation, transcription activity, interaction with transcription factor and transcription of target genes of YAP via AMOT, while AMOT acted as a suppressor of YAP in normal glucose level.
29217192	8	16	theme	liver	960:964	arg1	cancer					966:971	liver cancer	960:971	liver cancer associated with possibly diabetes	960:1005	Targeting the aberrantly regulated core factors in Hippo pathway might be a more effective therapeutic approach for liver cancer associated with possibly diabetes.
29217192	6	17	theme	YAP	701:703	arg1	accumulation					676:687	nuclear accumulation	668:687	nuclear accumulation of AMOT and YAP in Streptozocin (STZ)	668:725	Finally, we observed the upregulation and nuclear accumulation of AMOT and YAP in Streptozocin (STZ) induced high glucose mice.
29217192	5	18	theme	target	531:536	arg1	genes					538:542	target genes	531:542	target genes of YAP	531:549	We also found that HG stimulated nuclear accumulation, transcription activity, interaction with transcription factor and transcription of target genes of YAP via AMOT, while AMOT acted as a suppressor of YAP in normal glucose level.
29217192	5	19	theme	genes	538:542	arg1	transcription					514:526	transcription	514:526	transcription of target genes of YAP	514:549	We also found that HG stimulated nuclear accumulation, transcription activity, interaction with transcription factor and transcription of target genes of YAP via AMOT, while AMOT acted as a suppressor of YAP in normal glucose level.
29217192	5	19	theme	genes	538:542	arg1	interaction					472:482	interaction	472:482	interaction with transcription factor	472:508	We also found that HG stimulated nuclear accumulation, transcription activity, interaction with transcription factor and transcription of target genes of YAP via AMOT, while AMOT acted as a suppressor of YAP in normal glucose level.
29217192	5	19	theme	genes	538:542	arg1	accumulation					434:445	nuclear accumulation	426:445	nuclear accumulation	426:445	We also found that HG stimulated nuclear accumulation, transcription activity, interaction with transcription factor and transcription of target genes of YAP via AMOT, while AMOT acted as a suppressor of YAP in normal glucose level.
29217192	5	19	theme	genes	538:542	arg1	activity					462:469	transcription activity	448:469	transcription activity	448:469	We also found that HG stimulated nuclear accumulation, transcription activity, interaction with transcription factor and transcription of target genes of YAP via AMOT, while AMOT acted as a suppressor of YAP in normal glucose level.
29217192	5	20	with	transcription	514:526	arg1	factor					503:508	transcription factor	489:508	transcription factor	489:508	We also found that HG stimulated nuclear accumulation, transcription activity, interaction with transcription factor and transcription of target genes of YAP via AMOT, while AMOT acted as a suppressor of YAP in normal glucose level.
29217192	6	21	theme	nuclear	668:674	arg1	accumulation					676:687	nuclear accumulation	668:687	nuclear accumulation of AMOT and YAP in Streptozocin (STZ)	668:725	Finally, we observed the upregulation and nuclear accumulation of AMOT and YAP in Streptozocin (STZ) induced high glucose mice.
29217192	4	22	theme	AMOT	387:390	arg1	O-GlcNAcylation					368:382	O-GlcNAcylation	368:382	O-GlcNAcylation	368:382	Moreover, high glucose (HG) was able to enhance the expression and O-GlcNAcylation of AMOT.
29217192	4	22	theme	AMOT	387:390	arg1	expression					353:362	expression	353:362	expression	353:362	Moreover, high glucose (HG) was able to enhance the expression and O-GlcNAcylation of AMOT.
29217192	0	23	theme	YAP	21:23	arg1	function					25:32	YAP function	21:32	YAP function in high glucose induced liver malignancy	21:73	AMOT is required for YAP function in high glucose induced liver malignancy.
29217192	5	24	from	suppressor	583:592	arg1	level					619:623	normal glucose level	604:623	normal glucose level	604:623	We also found that HG stimulated nuclear accumulation, transcription activity, interaction with transcription factor and transcription of target genes of YAP via AMOT, while AMOT acted as a suppressor of YAP in normal glucose level.
29217192	5	25	from	YAP	597:599	arg1	level					619:623	normal glucose level	604:623	normal glucose level	604:623	We also found that HG stimulated nuclear accumulation, transcription activity, interaction with transcription factor and transcription of target genes of YAP via AMOT, while AMOT acted as a suppressor of YAP in normal glucose level.
29217192	0	26	theme	high	37:40	arg1	malignancy					64:73	high glucose induced liver malignancy	37:73	high glucose induced liver malignancy	37:73	AMOT is required for YAP function in high glucose induced liver malignancy.
29217192	5	27	theme	YAP	597:599	arg1	AMOT					567:570	AMOT	567:570	AMOT	567:570	We also found that HG stimulated nuclear accumulation, transcription activity, interaction with transcription factor and transcription of target genes of YAP via AMOT, while AMOT acted as a suppressor of YAP in normal glucose level.
29217192	5	27	theme	YAP	597:599	arg1	suppressor					583:592	a suppressor	581:592	a suppressor of YAP in normal glucose level	581:623	We also found that HG stimulated nuclear accumulation, transcription activity, interaction with transcription factor and transcription of target genes of YAP via AMOT, while AMOT acted as a suppressor of YAP in normal glucose level.
29217192	5	28	theme	transcription	489:501	arg1	factor					503:508	transcription factor	489:508	transcription factor	489:508	We also found that HG stimulated nuclear accumulation, transcription activity, interaction with transcription factor and transcription of target genes of YAP via AMOT, while AMOT acted as a suppressor of YAP in normal glucose level.
29217192	8	29	from	factors	884:890	arg1	pathway					901:907	Hippo pathway	895:907	Hippo pathway	895:907	Targeting the aberrantly regulated core factors in Hippo pathway might be a more effective therapeutic approach for liver cancer associated with possibly diabetes.
29217192	5	30	with	accumulation	434:445	arg1	factor					503:508	transcription factor	489:508	transcription factor	489:508	We also found that HG stimulated nuclear accumulation, transcription activity, interaction with transcription factor and transcription of target genes of YAP via AMOT, while AMOT acted as a suppressor of YAP in normal glucose level.
29217192	4	31	theme	high	311:314	arg1	HG					325:326	HG	325:326	HG	325:326	Moreover, high glucose (HG) was able to enhance the expression and O-GlcNAcylation of AMOT.
29217192	4	31	theme	high	311:314	arg1	glucose					316:322	high glucose	311:322	high glucose (HG)	311:327	Moreover, high glucose (HG) was able to enhance the expression and O-GlcNAcylation of AMOT.
29217192	6	32	theme	AMOT	692:695	arg1	accumulation					676:687	nuclear accumulation	668:687	nuclear accumulation of AMOT and YAP in Streptozocin (STZ)	668:725	Finally, we observed the upregulation and nuclear accumulation of AMOT and YAP in Streptozocin (STZ) induced high glucose mice.
29217192	5	33	theme	normal	604:609	arg1	level					619:623	normal glucose level	604:623	normal glucose level	604:623	We also found that HG stimulated nuclear accumulation, transcription activity, interaction with transcription factor and transcription of target genes of YAP via AMOT, while AMOT acted as a suppressor of YAP in normal glucose level.
29217192	6	34	theme	glucose	740:746	arg1	mice					748:751	high glucose mice	735:751	high glucose mice	735:751	Finally, we observed the upregulation and nuclear accumulation of AMOT and YAP in Streptozocin (STZ) induced high glucose mice.
29217192	7	35	theme	YAP	806:808	arg1	stimulator					810:819	a YAP stimulator	804:819	a YAP stimulator	804:819	Collectively, we have uncovered that AMOT acts as a YAP stimulator in high glucose level.
29217192	7	35	theme	YAP	806:808	arg1	AMOT					791:794	AMOT	791:794	AMOT	791:794	Collectively, we have uncovered that AMOT acts as a YAP stimulator in high glucose level.
29217192	5	36	theme	glucose	611:617	arg1	level					619:623	normal glucose level	604:623	normal glucose level	604:623	We also found that HG stimulated nuclear accumulation, transcription activity, interaction with transcription factor and transcription of target genes of YAP via AMOT, while AMOT acted as a suppressor of YAP in normal glucose level.
29217192	6	37	theme	high	735:738	arg1	glucose					740:746	high glucose	735:746	high glucose mice	735:751	Finally, we observed the upregulation and nuclear accumulation of AMOT and YAP in Streptozocin (STZ) induced high glucose mice.
29217192	5	38	theme	transcription	448:460	arg1	activity					462:469	transcription activity	448:469	transcription activity	448:469	We also found that HG stimulated nuclear accumulation, transcription activity, interaction with transcription factor and transcription of target genes of YAP via AMOT, while AMOT acted as a suppressor of YAP in normal glucose level.
29217192	1	39	theme	YAP	106:108	arg1	AMOT					76:79	AMOT	76:79	AMOT	76:79	AMOT has been identified as a YAP interactor.
29217192	1	39	theme	YAP	106:108	arg1	interactor					110:119	a YAP interactor	104:119	a YAP interactor	104:119	AMOT has been identified as a YAP interactor.
29217192	3	40	theme	Hippo	242:246	arg1	factor					263:268	another Hippo signaling core factor	234:268	another Hippo signaling core factor which could be O-GlcNAcylated	234:298	Here, we identified that besides YAP, AMOT was another Hippo signaling core factor which could be O-GlcNAcylated.
29217192	0	41	theme	induced	50:56	arg1	malignancy					64:73	high glucose induced liver malignancy	37:73	high glucose induced liver malignancy	37:73	AMOT is required for YAP function in high glucose induced liver malignancy.
29217192	4	42	dep	expression	353:362	arg1	the					349:351	the	349:351	the	349:351	Moreover, high glucose (HG) was able to enhance the expression and O-GlcNAcylation of AMOT.
29217192	5	43	with	activity	462:469	arg1	factor					503:508	transcription factor	489:508	transcription factor	489:508	We also found that HG stimulated nuclear accumulation, transcription activity, interaction with transcription factor and transcription of target genes of YAP via AMOT, while AMOT acted as a suppressor of YAP in normal glucose level.
23899520	1	0	theme	critical	183:190	arg1	roles					192:196	critical roles	183:196	critical roles	183:196	Intricate cross-talks exist among multiple post-translational modifications that play critical roles in various cellular events, such as the control of gene expression and regulation of protein function.
23899520	7	1	mod	modified	1129:1136	arg3	O-GlcNAc					1141:1148	O-GlcNAc	1141:1148	O-GlcNAc	1141:1148	It was also found that endogenous FBXW10 was modified by O-GlcNAc in HEK293T cells, implying O-GlcNAcylation might regulate FBXW10 in multiple levels.
23899520	7	1	mod	modified	1129:1136	arg1	FBXW10					1118:1123	endogenous FBXW10	1107:1123	endogenous FBXW10	1107:1123	It was also found that endogenous FBXW10 was modified by O-GlcNAc in HEK293T cells, implying O-GlcNAcylation might regulate FBXW10 in multiple levels.
23899520	0	2	theme	protein	72:78	arg1	O-GlcNAcylation					80:94	protein O-GlcNAcylation	72:94	protein O-GlcNAcylation	72:94	FBXW10 is negatively regulated in transcription and expression level by protein O-GlcNAcylation.
23899520	1	3	dep	Intricate	97:105	arg1	cross-talks					107:117	cross-talks	107:117	cross-talks	107:117	Intricate cross-talks exist among multiple post-translational modifications that play critical roles in various cellular events, such as the control of gene expression and regulation of protein function.
23899520	7	4	theme	multiple	1218:1225	arg1	levels					1227:1232	multiple levels	1218:1232	multiple levels	1218:1232	It was also found that endogenous FBXW10 was modified by O-GlcNAc in HEK293T cells, implying O-GlcNAcylation might regulate FBXW10 in multiple levels.
23899520	3	5	dep	elevation	502:510	arg1	response					486:493	response	486:493	response	486:493	By PCR array, 84 ubiquitination-related genes were explored in transcription level in response to the elevation of total protein O-GlcNAcylation due to over-expression of OGT, inhibition of OGA or GlcN treatment.
23899520	6	6	theme	time-dependent	1007:1020	arg1	way					1022:1024	a time-dependent way	1005:1024	a time-dependent way	1005:1024	By RT-PCR and Western blot analysis, it was found that FBXW10 could be sharply down-regulated in mRNA and protein level in GlcN-treated cells in a time-dependent way, in line with the enhancement of protein O-GlcNAcylation.
23899520	3	7	theme	inhibition	576:585	arg1	over-expression					552:566	over-expression	552:566	over-expression of OGT, inhibition of OGA or GlcN treatment	552:610	By PCR array, 84 ubiquitination-related genes were explored in transcription level in response to the elevation of total protein O-GlcNAcylation due to over-expression of OGT, inhibition of OGA or GlcN treatment.
23899520	3	8	theme	O-GlcNAcylation	529:543	arg1	elevation					502:510	the elevation	498:510	the elevation of total protein O-GlcNAcylation due to over-expression of OGT, inhibition of OGA or GlcN treatment	498:610	By PCR array, 84 ubiquitination-related genes were explored in transcription level in response to the elevation of total protein O-GlcNAcylation due to over-expression of OGT, inhibition of OGA or GlcN treatment.
23899520	1	9	theme	protein	283:289	arg1	function					291:298	protein function	283:298	protein function	283:298	Intricate cross-talks exist among multiple post-translational modifications that play critical roles in various cellular events, such as the control of gene expression and regulation of protein function.
23899520	8	10	theme	genes	1336:1340	arg1	regulation					1299:1308	the regulation	1295:1308	the regulation of ubiquitination-related genes	1295:1340	These findings indicate that O-GlcNAcylation is involved in the regulation of ubiquitination-related genes, and help us understand the cross-talk between O-GlcNAcylation and ubiquitination.
23899520	7	11	theme	endogenous	1107:1116	arg1	FBXW10					1118:1123	endogenous FBXW10	1107:1123	endogenous FBXW10	1107:1123	It was also found that endogenous FBXW10 was modified by O-GlcNAc in HEK293T cells, implying O-GlcNAcylation might regulate FBXW10 in multiple levels.
23899520	8	12	theme	ubiquitination-related	1313:1334	arg1	genes					1336:1340	ubiquitination-related genes	1313:1340	ubiquitination-related genes	1313:1340	These findings indicate that O-GlcNAcylation is involved in the regulation of ubiquitination-related genes, and help us understand the cross-talk between O-GlcNAcylation and ubiquitination.
23899520	3	13	theme	transcription	463:475	arg1	level					477:481	transcription level	463:481	transcription level	463:481	By PCR array, 84 ubiquitination-related genes were explored in transcription level in response to the elevation of total protein O-GlcNAcylation due to over-expression of OGT, inhibition of OGA or GlcN treatment.
23899520	4	14	theme	Varied	613:618	arg1	genes					620:624	Varied genes	613:624	Varied genes	613:624	Varied genes were transcriptionally regulated by using different method.
23899520	3	15	theme	OGT	571:573	arg1	over-expression					552:566	over-expression	552:566	over-expression of OGT, inhibition of OGA or GlcN treatment	552:610	By PCR array, 84 ubiquitination-related genes were explored in transcription level in response to the elevation of total protein O-GlcNAcylation due to over-expression of OGT, inhibition of OGA or GlcN treatment.
23899520	1	16	theme	various	201:207	arg1	regulation					269:278	regulation	269:278	regulation of protein function	269:298	Intricate cross-talks exist among multiple post-translational modifications that play critical roles in various cellular events, such as the control of gene expression and regulation of protein function.
23899520	1	16	theme	various	201:207	arg1	control					238:244	the control	234:244	the control of gene expression	234:263	Intricate cross-talks exist among multiple post-translational modifications that play critical roles in various cellular events, such as the control of gene expression and regulation of protein function.
23899520	1	16	theme	various	201:207	arg1	events					218:223	various cellular events	201:223	various cellular events	201:223	Intricate cross-talks exist among multiple post-translational modifications that play critical roles in various cellular events, such as the control of gene expression and regulation of protein function.
23899520	5	17	theme	protein	835:841	arg1	O-GlcNAcylation					843:857	protein O-GlcNAcylation	835:857	protein O-GlcNAcylation	835:857	But FBXW10, an F-box protein targeting specific proteins for ubiquitination, could be negatively regulated in all ways, suggesting its regulation by protein O-GlcNAcylation.
23899520	1	18	theme	cellular	209:216	arg1	regulation					269:278	regulation	269:278	regulation of protein function	269:298	Intricate cross-talks exist among multiple post-translational modifications that play critical roles in various cellular events, such as the control of gene expression and regulation of protein function.
23899520	1	18	theme	cellular	209:216	arg1	control					238:244	the control	234:244	the control of gene expression	234:263	Intricate cross-talks exist among multiple post-translational modifications that play critical roles in various cellular events, such as the control of gene expression and regulation of protein function.
23899520	1	18	theme	cellular	209:216	arg1	events					218:223	various cellular events	201:223	various cellular events	201:223	Intricate cross-talks exist among multiple post-translational modifications that play critical roles in various cellular events, such as the control of gene expression and regulation of protein function.
23899520	1	19	theme	function	291:298	arg1	regulation					269:278	regulation	269:278	regulation of protein function	269:298	Intricate cross-talks exist among multiple post-translational modifications that play critical roles in various cellular events, such as the control of gene expression and regulation of protein function.
23899520	1	19	theme	function	291:298	arg1	control					238:244	the control	234:244	the control of gene expression	234:263	Intricate cross-talks exist among multiple post-translational modifications that play critical roles in various cellular events, such as the control of gene expression and regulation of protein function.
23899520	3	20	theme	GlcN	597:600	arg1	treatment					602:610	GlcN treatment	597:610	GlcN treatment	597:610	By PCR array, 84 ubiquitination-related genes were explored in transcription level in response to the elevation of total protein O-GlcNAcylation due to over-expression of OGT, inhibition of OGA or GlcN treatment.
23899520	4	21	theme	different	668:676	arg1	method					678:683	different method	668:683	different method	668:683	Varied genes were transcriptionally regulated by using different method.
23899520	3	22	theme	PCR	403:405	arg1	array					407:411	PCR array	403:411	PCR array	403:411	By PCR array, 84 ubiquitination-related genes were explored in transcription level in response to the elevation of total protein O-GlcNAcylation due to over-expression of OGT, inhibition of OGA or GlcN treatment.
23899520	6	23	theme	GlcN-treated	983:994	arg1	cells					996:1000	GlcN-treated cells	983:1000	GlcN-treated cells	983:1000	By RT-PCR and Western blot analysis, it was found that FBXW10 could be sharply down-regulated in mRNA and protein level in GlcN-treated cells in a time-dependent way, in line with the enhancement of protein O-GlcNAcylation.
23899520	3	24	theme	OGA	590:592	arg1	treatment					602:610	GlcN treatment	597:610	GlcN treatment	597:610	By PCR array, 84 ubiquitination-related genes were explored in transcription level in response to the elevation of total protein O-GlcNAcylation due to over-expression of OGT, inhibition of OGA or GlcN treatment.
23899520	3	24	theme	OGA	590:592	arg1	inhibition					576:585	inhibition	576:585	inhibition of OGA	576:592	By PCR array, 84 ubiquitination-related genes were explored in transcription level in response to the elevation of total protein O-GlcNAcylation due to over-expression of OGT, inhibition of OGA or GlcN treatment.
23899520	3	24	theme	OGA	590:592	arg1	OGT					571:573	OGT	571:573	OGT	571:573	By PCR array, 84 ubiquitination-related genes were explored in transcription level in response to the elevation of total protein O-GlcNAcylation due to over-expression of OGT, inhibition of OGA or GlcN treatment.
23899520	6	25	theme	protein	1059:1065	arg1	O-GlcNAcylation					1067:1081	protein O-GlcNAcylation	1059:1081	protein O-GlcNAcylation	1059:1081	By RT-PCR and Western blot analysis, it was found that FBXW10 could be sharply down-regulated in mRNA and protein level in GlcN-treated cells in a time-dependent way, in line with the enhancement of protein O-GlcNAcylation.
23899520	0	26	theme	transcription	34:46	arg1	level					63:67	transcription and expression level	34:67	transcription and expression level	34:67	FBXW10 is negatively regulated in transcription and expression level by protein O-GlcNAcylation.
23899520	3	27	theme	protein	521:527	arg1	O-GlcNAcylation					529:543	total protein O-GlcNAcylation	515:543	total protein O-GlcNAcylation due to over-expression of OGT, inhibition of OGA or GlcN treatment	515:610	By PCR array, 84 ubiquitination-related genes were explored in transcription level in response to the elevation of total protein O-GlcNAcylation due to over-expression of OGT, inhibition of OGA or GlcN treatment.
23899520	8	28	gly	O-GlcNAcylation	1264:1278	arg1	regulation					1299:1308	the regulation	1295:1308	the regulation of ubiquitination-related genes	1295:1340	These findings indicate that O-GlcNAcylation is involved in the regulation of ubiquitination-related genes, and help us understand the cross-talk between O-GlcNAcylation and ubiquitination.
23899520	6	29	with	line	1030:1033	arg1	enhancement					1044:1054	the enhancement	1040:1054	the enhancement of protein O-GlcNAcylation	1040:1081	By RT-PCR and Western blot analysis, it was found that FBXW10 could be sharply down-regulated in mRNA and protein level in GlcN-treated cells in a time-dependent way, in line with the enhancement of protein O-GlcNAcylation.
23899520	0	30	theme	expression	52:61	arg1	level					63:67	transcription and expression level	34:67	transcription and expression level	34:67	FBXW10 is negatively regulated in transcription and expression level by protein O-GlcNAcylation.
23899520	6	31	theme	protein	966:972	arg1	level					974:978	mRNA and protein level	957:978	mRNA and protein level in GlcN-treated cells	957:1000	By RT-PCR and Western blot analysis, it was found that FBXW10 could be sharply down-regulated in mRNA and protein level in GlcN-treated cells in a time-dependent way, in line with the enhancement of protein O-GlcNAcylation.
23899520	5	32	theme	F-box	701:705	arg1	FBXW10					690:695	FBXW10	690:695	FBXW10	690:695	But FBXW10, an F-box protein targeting specific proteins for ubiquitination, could be negatively regulated in all ways, suggesting its regulation by protein O-GlcNAcylation.
23899520	5	32	theme	F-box	701:705	arg1	protein					707:713	an F-box protein	698:713	an F-box protein targeting specific proteins for ubiquitination	698:760	But FBXW10, an F-box protein targeting specific proteins for ubiquitination, could be negatively regulated in all ways, suggesting its regulation by protein O-GlcNAcylation.
23899520	3	33	theme	treatment	602:610	arg1	over-expression					552:566	over-expression	552:566	over-expression of OGT, inhibition of OGA or GlcN treatment	552:610	By PCR array, 84 ubiquitination-related genes were explored in transcription level in response to the elevation of total protein O-GlcNAcylation due to over-expression of OGT, inhibition of OGA or GlcN treatment.
23899520	3	34	theme	total	515:519	arg1	O-GlcNAcylation					529:543	total protein O-GlcNAcylation	515:543	total protein O-GlcNAcylation due to over-expression of OGT, inhibition of OGA or GlcN treatment	515:610	By PCR array, 84 ubiquitination-related genes were explored in transcription level in response to the elevation of total protein O-GlcNAcylation due to over-expression of OGT, inhibition of OGA or GlcN treatment.
23899520	3	35	theme	ubiquitination-related	417:438	arg1	genes					440:444	84 ubiquitination-related genes	414:444	84 ubiquitination-related genes	414:444	By PCR array, 84 ubiquitination-related genes were explored in transcription level in response to the elevation of total protein O-GlcNAcylation due to over-expression of OGT, inhibition of OGA or GlcN treatment.
23899520	6	36	theme	blot	882:885	arg1	analysis					887:894	Western blot analysis	874:894	Western blot analysis	874:894	By RT-PCR and Western blot analysis, it was found that FBXW10 could be sharply down-regulated in mRNA and protein level in GlcN-treated cells in a time-dependent way, in line with the enhancement of protein O-GlcNAcylation.
23899520	3	37	theme	due	545:547	arg1	O-GlcNAcylation					529:543	total protein O-GlcNAcylation	515:543	total protein O-GlcNAcylation due to over-expression of OGT, inhibition of OGA or GlcN treatment	515:610	By PCR array, 84 ubiquitination-related genes were explored in transcription level in response to the elevation of total protein O-GlcNAcylation due to over-expression of OGT, inhibition of OGA or GlcN treatment.
23899520	1	38	theme	multiple	131:138	arg1	modifications					159:171	multiple post-translational modifications	131:171	multiple post-translational modifications that play critical roles in various cellular events, such as the control of gene expression and regulation of protein function	131:298	Intricate cross-talks exist among multiple post-translational modifications that play critical roles in various cellular events, such as the control of gene expression and regulation of protein function.
23899520	6	39	theme	mRNA	957:960	arg1	level					974:978	mRNA and protein level	957:978	mRNA and protein level in GlcN-treated cells	957:1000	By RT-PCR and Western blot analysis, it was found that FBXW10 could be sharply down-regulated in mRNA and protein level in GlcN-treated cells in a time-dependent way, in line with the enhancement of protein O-GlcNAcylation.
23899520	6	40	from	level	974:978	arg1	cells					996:1000	GlcN-treated cells	983:1000	GlcN-treated cells	983:1000	By RT-PCR and Western blot analysis, it was found that FBXW10 could be sharply down-regulated in mRNA and protein level in GlcN-treated cells in a time-dependent way, in line with the enhancement of protein O-GlcNAcylation.
23899520	6	41	theme	Western	874:880	arg1	analysis					887:894	Western blot analysis	874:894	Western blot analysis	874:894	By RT-PCR and Western blot analysis, it was found that FBXW10 could be sharply down-regulated in mRNA and protein level in GlcN-treated cells in a time-dependent way, in line with the enhancement of protein O-GlcNAcylation.
23899520	7	42	theme	HEK293T	1153:1159	arg1	cells					1161:1165	HEK293T cells	1153:1165	HEK293T cells	1153:1165	It was also found that endogenous FBXW10 was modified by O-GlcNAc in HEK293T cells, implying O-GlcNAcylation might regulate FBXW10 in multiple levels.
23899520	1	43	theme	post-translational	140:157	arg1	modifications					159:171	multiple post-translational modifications	131:171	multiple post-translational modifications that play critical roles in various cellular events, such as the control of gene expression and regulation of protein function	131:298	Intricate cross-talks exist among multiple post-translational modifications that play critical roles in various cellular events, such as the control of gene expression and regulation of protein function.
23899520	5	44	theme	specific	725:732	arg1	proteins					734:741	specific proteins	725:741	specific proteins	725:741	But FBXW10, an F-box protein targeting specific proteins for ubiquitination, could be negatively regulated in all ways, suggesting its regulation by protein O-GlcNAcylation.
23899520	6	45	theme	O-GlcNAcylation	1067:1081	arg1	enhancement					1044:1054	the enhancement	1040:1054	the enhancement of protein O-GlcNAcylation	1040:1081	By RT-PCR and Western blot analysis, it was found that FBXW10 could be sharply down-regulated in mRNA and protein level in GlcN-treated cells in a time-dependent way, in line with the enhancement of protein O-GlcNAcylation.
23899520	2	46	theme	HEK293T	385:391	arg1	cells					393:397	HEK293T cells	385:397	HEK293T cells	385:397	Here, the cross-talk between O-GlcNAcylation and ubiquitination was investigated in HEK293T cells.
23899520	1	47	theme	gene	249:252	arg1	expression					254:263	gene expression	249:263	gene expression	249:263	Intricate cross-talks exist among multiple post-translational modifications that play critical roles in various cellular events, such as the control of gene expression and regulation of protein function.
23899520	1	48	theme	expression	254:263	arg1	regulation					269:278	regulation	269:278	regulation of protein function	269:298	Intricate cross-talks exist among multiple post-translational modifications that play critical roles in various cellular events, such as the control of gene expression and regulation of protein function.
23899520	1	48	theme	expression	254:263	arg1	control					238:244	the control	234:244	the control of gene expression	234:263	Intricate cross-talks exist among multiple post-translational modifications that play critical roles in various cellular events, such as the control of gene expression and regulation of protein function.
37070251	4	0	theme	multivariate	604:615	arg1	analysis					632:639	multivariate Cox regression analysis	604:639	multivariate Cox regression analysis	604:639	The prognostic significance of LARP1 was evaluated by Kaplan-Meier method and multivariate Cox regression analysis.
37070251	10	1	theme	LARP1	1540:1544	arg1	overexpression					1546:1559	LARP1 overexpression	1540:1559	LARP1 overexpression	1540:1559	LARP1 knockdown abolished cell proliferation, triggered cell apoptosis in vitro as well as prohibited tumour growth in vivo, whereas LARP1 overexpression incited HB progression.
37070251	10	2	theme	LARP1	1407:1411	arg1	knockdown					1413:1421	LARP1 knockdown	1407:1421	LARP1 knockdown	1407:1421	LARP1 knockdown abolished cell proliferation, triggered cell apoptosis in vitro as well as prohibited tumour growth in vivo, whereas LARP1 overexpression incited HB progression.
37070251	8	3	theme	diagnostic	1167:1176	arg1	significance					1178:1189	diagnostic significance	1167:1189	diagnostic significance	1167:1189	The expression and diagnostic significance of plasma DKK4 protein in multi-centre cohorts were evaluated by ELISA and ROC curves.
37070251	12	4	theme	mRNA	1820:1823	arg1	stabilisation					1825:1837	DKK4 mRNA stabilisation	1815:1837	DKK4 mRNA stabilisation	1815:1837	LARP1 upregulation subsequently led to DKK4 mRNA stabilisation by competitively interacting with PABPC1 to prevent DKK4 mRNA from B-cell translocation gene 2-dependent deadenylation and degradation, thus facilitating β-catenin protein expression and nuclear import.
37070251	13	5	theme	LARP1	2123:2127	arg1	level					2099:2103	upregulated protein level	2079:2103	upregulated protein level of O-GlcNAcylated LARP1 mediated by circCLNS1A	2079:2150	CONCLUSION This study indicates that upregulated protein level of O-GlcNAcylated LARP1 mediated by circCLNS1A promotes the tumorigenesis and progression of HB through LARP1/DKK4/β-catenin axis.
37070251	4	6	theme	regression	621:630	arg1	analysis					632:639	multivariate Cox regression analysis	604:639	multivariate Cox regression analysis	604:639	The prognostic significance of LARP1 was evaluated by Kaplan-Meier method and multivariate Cox regression analysis.
37070251	13	7	theme	upregulated	2079:2089	arg1	level					2099:2103	upregulated protein level	2079:2103	upregulated protein level of O-GlcNAcylated LARP1 mediated by circCLNS1A	2079:2150	CONCLUSION This study indicates that upregulated protein level of O-GlcNAcylated LARP1 mediated by circCLNS1A promotes the tumorigenesis and progression of HB through LARP1/DKK4/β-catenin axis.
37070251	2	8	theme	biological	309:318	arg1	role					320:323	biological role	309:323	biological role of LARP1 in hepatoblastoma (HB)	309:355	However, the expression pattern and biological role of LARP1 in hepatoblastoma (HB) remain unclear so far.
37070251	5	9	theme	in	655:656	arg1	assays					674:679	In vitro and in vivo functional assays	642:679	In vitro and in vivo functional assays	642:679	In vitro and in vivo functional assays were implemented to clarify the biological effects of LARP1 on HB cells.
37070251	8	10	theme	DKK4	1201:1204	arg1	protein					1206:1212	plasma DKK4 protein	1194:1212	plasma DKK4 protein	1194:1212	The expression and diagnostic significance of plasma DKK4 protein in multi-centre cohorts were evaluated by ELISA and ROC curves.
37070251	6	11	theme	RNA	919:921	arg1	RIP					944:946	RIP	944:946	RIP	944:946	Mechanistically, the regulatory roles of O-GlcNAcylation and circCLNS1A in LARP1 expression were investigated by co-immunoprecipitation (co-IP), immunofluorescence, RNA immunoprecipitation (RIP), RNA pull-down and protein stability assays.
37070251	6	11	theme	RNA	919:921	arg1	immunoprecipitation					923:941	RNA immunoprecipitation	919:941	RNA immunoprecipitation (RIP)	919:947	Mechanistically, the regulatory roles of O-GlcNAcylation and circCLNS1A in LARP1 expression were investigated by co-immunoprecipitation (co-IP), immunofluorescence, RNA immunoprecipitation (RIP), RNA pull-down and protein stability assays.
37070251	8	12	theme	ROC	1266:1268	arg1	curves					1270:1275	ROC curves	1266:1275	ROC curves	1266:1275	The expression and diagnostic significance of plasma DKK4 protein in multi-centre cohorts were evaluated by ELISA and ROC curves.
37070251	5	13	theme	functional	663:672	arg1	assays					674:679	In vitro and in vivo functional assays	642:679	In vitro and in vivo functional assays	642:679	In vitro and in vivo functional assays were implemented to clarify the biological effects of LARP1 on HB cells.
37070251	14	14	theme	diagnostic/prognostic	2297:2317	arg1	biomarker					2326:2334	diagnostic/prognostic plasma biomarker	2297:2334	diagnostic/prognostic plasma biomarker	2297:2334	Hence, LARP1 and DKK4 are promising therapeutical target and diagnostic/prognostic plasma biomarker for HB.
37070251	5	15	theme	LARP1	735:739	arg1	effects					724:730	the biological effects	709:730	the biological effects of LARP1 on HB cells	709:751	In vitro and in vivo functional assays were implemented to clarify the biological effects of LARP1 on HB cells.
37070251	5	16	theme	HB	744:745	arg1	cells					747:751	HB cells	744:751	HB cells	744:751	In vitro and in vivo functional assays were implemented to clarify the biological effects of LARP1 on HB cells.
37070251	7	17	theme	stability	1037:1045	arg1	assays					1071:1076	RNA-sequencing, co-IP, RIP, mRNA stability and poly(A)-tail length assays	1004:1076	RNA-sequencing, co-IP, RIP, mRNA stability and poly(A)-tail length assays	1004:1076	Moreover, RNA-sequencing, co-IP, RIP, mRNA stability and poly(A)-tail length assays were performed to investigate the association between LARP1 and DKK4.
37070251	6	18	theme	stability	976:984	arg1	assays					986:991	protein stability assays	968:991	protein stability assays	968:991	Mechanistically, the regulatory roles of O-GlcNAcylation and circCLNS1A in LARP1 expression were investigated by co-immunoprecipitation (co-IP), immunofluorescence, RNA immunoprecipitation (RIP), RNA pull-down and protein stability assays.
37070251	5	19	theme	biological	713:722	arg1	effects					724:730	the biological effects	709:730	the biological effects of LARP1 on HB cells	709:751	In vitro and in vivo functional assays were implemented to clarify the biological effects of LARP1 on HB cells.
37070251	14	20	theme	promising	2262:2270	arg1	target					2286:2291	promising therapeutical target	2262:2291	promising therapeutical target	2262:2291	Hence, LARP1 and DKK4 are promising therapeutical target and diagnostic/prognostic plasma biomarker for HB.
37070251	14	20	theme	promising	2262:2270	arg1	DKK4					2253:2256	DKK4	2253:2256	DKK4	2253:2256	Hence, LARP1 and DKK4 are promising therapeutical target and diagnostic/prognostic plasma biomarker for HB.
37070251	14	20	theme	promising	2262:2270	arg1	LARP1					2243:2247	LARP1	2243:2247	LARP1	2243:2247	Hence, LARP1 and DKK4 are promising therapeutical target and diagnostic/prognostic plasma biomarker for HB.
37070251	9	21	theme	RESULTS	1278:1284	arg1	mRNA					1292:1295	RESULTS LARP1 mRNA and protein levels	1278:1314	mRNA	1292:1295	RESULTS LARP1 mRNA and protein levels were remarkably elevated in HB tissues and associated with worse prognosis of HB patients.
37070251	1	22	theme	La-related	178:187	arg1	protein					189:195	La-related protein 1	178:197	La-related protein 1 (LARP1)	178:205	BACKGROUND Accumulating studies have shown that La-related protein 1 (LARP1) is involved in the occurrence and development of various tumours.
37070251	1	22	theme	La-related	178:187	arg1	LARP1					200:204	LARP1	200:204	LARP1	200:204	BACKGROUND Accumulating studies have shown that La-related protein 1 (LARP1) is involved in the occurrence and development of various tumours.
37070251	2	23	from	role	320:323	arg1	HB					353:354	HB	353:354	HB	353:354	However, the expression pattern and biological role of LARP1 in hepatoblastoma (HB) remain unclear so far.
37070251	2	23	from	role	320:323	arg1	hepatoblastoma					337:350	hepatoblastoma	337:350	hepatoblastoma (HB)	337:355	However, the expression pattern and biological role of LARP1 in hepatoblastoma (HB) remain unclear so far.
37070251	0	24	theme	DKK4/β-catenin	103:116	arg1	signalling					118:127	DKK4/β-catenin signalling	103:127	DKK4/β-catenin signalling	103:127	O-GlcNAcylated LARP1 positively regulated by circCLNS1A facilitates hepatoblastoma progression through DKK4/β-catenin signalling.
37070251	9	25	theme	protein	1301:1307	arg1	levels					1309:1314	RESULTS LARP1 mRNA and protein levels	1278:1314	levels	1309:1314	RESULTS LARP1 mRNA and protein levels were remarkably elevated in HB tissues and associated with worse prognosis of HB patients.
37070251	12	26	theme	nuclear	2026:2032	arg1	import					2034:2039	nuclear import	2026:2039	nuclear import	2026:2039	LARP1 upregulation subsequently led to DKK4 mRNA stabilisation by competitively interacting with PABPC1 to prevent DKK4 mRNA from B-cell translocation gene 2-dependent deadenylation and degradation, thus facilitating β-catenin protein expression and nuclear import.
37070251	5	27	theme	In	642:643	arg1	assays					674:679	In vitro and in vivo functional assays	642:679	In vitro and in vivo functional assays	642:679	In vitro and in vivo functional assays were implemented to clarify the biological effects of LARP1 on HB cells.
37070251	8	28	dep	expression	1152:1161	arg1	The					1148:1150	The	1148:1150	The	1148:1150	The expression and diagnostic significance of plasma DKK4 protein in multi-centre cohorts were evaluated by ELISA and ROC curves.
37070251	3	29	theme	expression	394:403	arg1	level					405:409	METHODS LARP1 expression level	380:409	METHODS LARP1 expression level in HB and adjacent normal liver tissues	380:449	METHODS LARP1 expression level in HB and adjacent normal liver tissues was analysed by qRT-PCR, Western blotting and immunohistochemistry assays.
37070251	3	30	theme	normal	430:435	arg1	tissues					443:449	adjacent normal liver tissues	421:449	adjacent normal liver tissues	421:449	METHODS LARP1 expression level in HB and adjacent normal liver tissues was analysed by qRT-PCR, Western blotting and immunohistochemistry assays.
37070251	0	31	theme	O-GlcNAcylated	0:13	arg1	LARP1					15:19	O-GlcNAcylated LARP1	0:19	O-GlcNAcylated LARP1 positively regulated by circCLNS1A	0:54	O-GlcNAcylated LARP1 positively regulated by circCLNS1A facilitates hepatoblastoma progression through DKK4/β-catenin signalling.
37070251	9	32	theme	HB	1344:1345	arg1	tissues					1347:1353	HB tissues	1344:1353	HB tissues	1344:1353	RESULTS LARP1 mRNA and protein levels were remarkably elevated in HB tissues and associated with worse prognosis of HB patients.
37070251	12	33	theme	β-catenin	1993:2001	arg1	expression					2011:2020	β-catenin protein expression	1993:2020	β-catenin protein expression	1993:2020	LARP1 upregulation subsequently led to DKK4 mRNA stabilisation by competitively interacting with PABPC1 to prevent DKK4 mRNA from B-cell translocation gene 2-dependent deadenylation and degradation, thus facilitating β-catenin protein expression and nuclear import.
37070251	1	34	theme	BACKGROUND	130:139	arg1	studies					154:160	BACKGROUND Accumulating studies	130:160	BACKGROUND Accumulating studies	130:160	BACKGROUND Accumulating studies have shown that La-related protein 1 (LARP1) is involved in the occurrence and development of various tumours.
37070251	3	35	theme	METHODS	380:386	arg1	level					405:409	METHODS LARP1 expression level	380:409	METHODS LARP1 expression level in HB and adjacent normal liver tissues	380:449	METHODS LARP1 expression level in HB and adjacent normal liver tissues was analysed by qRT-PCR, Western blotting and immunohistochemistry assays.
37070251	13	36	theme	protein	2091:2097	arg1	level					2099:2103	upregulated protein level	2079:2103	upregulated protein level of O-GlcNAcylated LARP1 mediated by circCLNS1A	2079:2150	CONCLUSION This study indicates that upregulated protein level of O-GlcNAcylated LARP1 mediated by circCLNS1A promotes the tumorigenesis and progression of HB through LARP1/DKK4/β-catenin axis.
37070251	8	37	from	expression	1152:1161	arg1	cohorts					1230:1236	multi-centre cohorts	1217:1236	multi-centre cohorts	1217:1236	The expression and diagnostic significance of plasma DKK4 protein in multi-centre cohorts were evaluated by ELISA and ROC curves.
37070251	4	38	theme	Kaplan-Meier	580:591	arg1	method					593:598	Kaplan-Meier method	580:598	Kaplan-Meier method	580:598	The prognostic significance of LARP1 was evaluated by Kaplan-Meier method and multivariate Cox regression analysis.
37070251	12	39	theme	DKK4	1891:1894	arg1	mRNA					1896:1899	DKK4 mRNA	1891:1899	DKK4 mRNA	1891:1899	LARP1 upregulation subsequently led to DKK4 mRNA stabilisation by competitively interacting with PABPC1 to prevent DKK4 mRNA from B-cell translocation gene 2-dependent deadenylation and degradation, thus facilitating β-catenin protein expression and nuclear import.
37070251	11	40	theme	TRIM-25-mediated	1727:1742	arg1	ubiquitination					1744:1757	TRIM-25-mediated ubiquitination	1727:1757	TRIM-25-mediated ubiquitination	1727:1757	Mechanistically, O-GlcNAcylation of LARP1 Ser672 by O-GlcNAc transferase strengthened its binding to circCLNS1A and then protected LARP1 from TRIM-25-mediated ubiquitination and proteolysis.
37070251	11	41	theme	Ser672	1627:1632	arg1	O-GlcNAcylation					1602:1616	O-GlcNAcylation	1602:1616	O-GlcNAcylation of LARP1 Ser672 by O-GlcNAc transferase	1602:1656	Mechanistically, O-GlcNAcylation of LARP1 Ser672 by O-GlcNAc transferase strengthened its binding to circCLNS1A and then protected LARP1 from TRIM-25-mediated ubiquitination and proteolysis.
37070251	12	42	theme	B-cell	1906:1911	arg1	deadenylation					1944:1956	B-cell translocation gene 2-dependent deadenylation	1906:1956	B-cell translocation gene 2-dependent deadenylation	1906:1956	LARP1 upregulation subsequently led to DKK4 mRNA stabilisation by competitively interacting with PABPC1 to prevent DKK4 mRNA from B-cell translocation gene 2-dependent deadenylation and degradation, thus facilitating β-catenin protein expression and nuclear import.
37070251	5	43	dep	In	642:643	arg1	vitro					645:649	vitro	645:649	vitro	645:649	In vitro and in vivo functional assays were implemented to clarify the biological effects of LARP1 on HB cells.
37070251	4	44	theme	LARP1	557:561	arg1	significance					541:552	The prognostic significance	526:552	The prognostic significance of LARP1	526:561	The prognostic significance of LARP1 was evaluated by Kaplan-Meier method and multivariate Cox regression analysis.
37070251	3	45	theme	Western	476:482	arg1	blotting					484:491	Western blotting	476:491	Western blotting	476:491	METHODS LARP1 expression level in HB and adjacent normal liver tissues was analysed by qRT-PCR, Western blotting and immunohistochemistry assays.
37070251	9	46	theme	HB	1394:1395	arg1	patients					1397:1404	HB patients	1394:1404	HB patients	1394:1404	RESULTS LARP1 mRNA and protein levels were remarkably elevated in HB tissues and associated with worse prognosis of HB patients.
37070251	12	47	theme	gene	1927:1930	arg1	deadenylation					1944:1956	B-cell translocation gene 2-dependent deadenylation	1906:1956	B-cell translocation gene 2-dependent deadenylation	1906:1956	LARP1 upregulation subsequently led to DKK4 mRNA stabilisation by competitively interacting with PABPC1 to prevent DKK4 mRNA from B-cell translocation gene 2-dependent deadenylation and degradation, thus facilitating β-catenin protein expression and nuclear import.
37070251	6	48	from	roles	786:790	arg1	expression					835:844	LARP1 expression	829:844	LARP1 expression	829:844	Mechanistically, the regulatory roles of O-GlcNAcylation and circCLNS1A in LARP1 expression were investigated by co-immunoprecipitation (co-IP), immunofluorescence, RNA immunoprecipitation (RIP), RNA pull-down and protein stability assays.
37070251	10	49	theme	HB	1569:1570	arg1	progression					1572:1582	HB progression	1569:1582	HB progression	1569:1582	LARP1 knockdown abolished cell proliferation, triggered cell apoptosis in vitro as well as prohibited tumour growth in vivo, whereas LARP1 overexpression incited HB progression.
37070251	1	50	theme	tumours	264:270	arg1	occurrence					226:235	occurrence	226:235	occurrence	226:235	BACKGROUND Accumulating studies have shown that La-related protein 1 (LARP1) is involved in the occurrence and development of various tumours.
37070251	1	50	theme	tumours	264:270	arg1	development					241:251	development	241:251	development	241:251	BACKGROUND Accumulating studies have shown that La-related protein 1 (LARP1) is involved in the occurrence and development of various tumours.
37070251	11	51	theme	O-GlcNAc	1637:1644	arg1	transferase					1646:1656	O-GlcNAc transferase	1637:1656	O-GlcNAc transferase	1637:1656	Mechanistically, O-GlcNAcylation of LARP1 Ser672 by O-GlcNAc transferase strengthened its binding to circCLNS1A and then protected LARP1 from TRIM-25-mediated ubiquitination and proteolysis.
37070251	6	52	theme	circCLNS1A	815:824	arg1	roles					786:790	the regulatory roles	771:790	the regulatory roles of O-GlcNAcylation and circCLNS1A in LARP1 expression	771:844	Mechanistically, the regulatory roles of O-GlcNAcylation and circCLNS1A in LARP1 expression were investigated by co-immunoprecipitation (co-IP), immunofluorescence, RNA immunoprecipitation (RIP), RNA pull-down and protein stability assays.
37070251	4	53	theme	Cox	617:619	arg1	analysis					632:639	multivariate Cox regression analysis	604:639	multivariate Cox regression analysis	604:639	The prognostic significance of LARP1 was evaluated by Kaplan-Meier method and multivariate Cox regression analysis.
37070251	6	54	theme	LARP1	829:833	arg1	expression					835:844	LARP1 expression	829:844	LARP1 expression	829:844	Mechanistically, the regulatory roles of O-GlcNAcylation and circCLNS1A in LARP1 expression were investigated by co-immunoprecipitation (co-IP), immunofluorescence, RNA immunoprecipitation (RIP), RNA pull-down and protein stability assays.
37070251	5	55	dep	in	655:656	arg1	vivo					658:661	vivo	658:661	vivo	658:661	In vitro and in vivo functional assays were implemented to clarify the biological effects of LARP1 on HB cells.
37070251	10	56	theme	cell	1433:1436	arg1	proliferation					1438:1450	cell proliferation	1433:1450	cell proliferation	1433:1450	LARP1 knockdown abolished cell proliferation, triggered cell apoptosis in vitro as well as prohibited tumour growth in vivo, whereas LARP1 overexpression incited HB progression.
37070251	8	57	theme	plasma	1194:1199	arg1	protein					1206:1212	plasma DKK4 protein	1194:1212	plasma DKK4 protein	1194:1212	The expression and diagnostic significance of plasma DKK4 protein in multi-centre cohorts were evaluated by ELISA and ROC curves.
37070251	12	58	theme	DKK4	1815:1818	arg1	stabilisation					1825:1837	DKK4 mRNA stabilisation	1815:1837	DKK4 mRNA stabilisation	1815:1837	LARP1 upregulation subsequently led to DKK4 mRNA stabilisation by competitively interacting with PABPC1 to prevent DKK4 mRNA from B-cell translocation gene 2-dependent deadenylation and degradation, thus facilitating β-catenin protein expression and nuclear import.
37070251	14	59	theme	plasma	2319:2324	arg1	biomarker					2326:2334	diagnostic/prognostic plasma biomarker	2297:2334	diagnostic/prognostic plasma biomarker	2297:2334	Hence, LARP1 and DKK4 are promising therapeutical target and diagnostic/prognostic plasma biomarker for HB.
37070251	6	60	theme	O-GlcNAcylation	795:809	arg1	roles					786:790	the regulatory roles	771:790	the regulatory roles of O-GlcNAcylation and circCLNS1A in LARP1 expression	771:844	Mechanistically, the regulatory roles of O-GlcNAcylation and circCLNS1A in LARP1 expression were investigated by co-immunoprecipitation (co-IP), immunofluorescence, RNA immunoprecipitation (RIP), RNA pull-down and protein stability assays.
37070251	2	61	theme	LARP1	328:332	arg1	pattern					297:303	the expression pattern	282:303	the expression pattern	282:303	However, the expression pattern and biological role of LARP1 in hepatoblastoma (HB) remain unclear so far.
37070251	2	61	theme	LARP1	328:332	arg1	role					320:323	biological role	309:323	biological role of LARP1 in hepatoblastoma (HB)	309:355	However, the expression pattern and biological role of LARP1 in hepatoblastoma (HB) remain unclear so far.
37070251	8	62	theme	protein	1206:1212	arg1	expression					1152:1161	expression	1152:1161	expression	1152:1161	The expression and diagnostic significance of plasma DKK4 protein in multi-centre cohorts were evaluated by ELISA and ROC curves.
37070251	8	62	theme	protein	1206:1212	arg1	significance					1178:1189	diagnostic significance	1167:1189	diagnostic significance	1167:1189	The expression and diagnostic significance of plasma DKK4 protein in multi-centre cohorts were evaluated by ELISA and ROC curves.
37070251	7	63	theme	-tail	1058:1062	arg1	assays					1071:1076	RNA-sequencing, co-IP, RIP, mRNA stability and poly(A)-tail length assays	1004:1076	RNA-sequencing, co-IP, RIP, mRNA stability and poly(A)-tail length assays	1004:1076	Moreover, RNA-sequencing, co-IP, RIP, mRNA stability and poly(A)-tail length assays were performed to investigate the association between LARP1 and DKK4.
37070251	8	64	theme	multi-centre	1217:1228	arg1	cohorts					1230:1236	multi-centre cohorts	1217:1236	multi-centre cohorts	1217:1236	The expression and diagnostic significance of plasma DKK4 protein in multi-centre cohorts were evaluated by ELISA and ROC curves.
37070251	13	65	dep	tumorigenesis	2165:2177	arg1	the					2161:2163	the	2161:2163	the	2161:2163	CONCLUSION This study indicates that upregulated protein level of O-GlcNAcylated LARP1 mediated by circCLNS1A promotes the tumorigenesis and progression of HB through LARP1/DKK4/β-catenin axis.
37070251	14	66	theme	therapeutical	2272:2284	arg1	target					2286:2291	promising therapeutical target	2262:2291	promising therapeutical target	2262:2291	Hence, LARP1 and DKK4 are promising therapeutical target and diagnostic/prognostic plasma biomarker for HB.
37070251	14	66	theme	therapeutical	2272:2284	arg1	DKK4					2253:2256	DKK4	2253:2256	DKK4	2253:2256	Hence, LARP1 and DKK4 are promising therapeutical target and diagnostic/prognostic plasma biomarker for HB.
37070251	14	66	theme	therapeutical	2272:2284	arg1	LARP1					2243:2247	LARP1	2243:2247	LARP1	2243:2247	Hence, LARP1 and DKK4 are promising therapeutical target and diagnostic/prognostic plasma biomarker for HB.
37070251	6	67	theme	protein	968:974	arg1	assays					986:991	protein stability assays	968:991	protein stability assays	968:991	Mechanistically, the regulatory roles of O-GlcNAcylation and circCLNS1A in LARP1 expression were investigated by co-immunoprecipitation (co-IP), immunofluorescence, RNA immunoprecipitation (RIP), RNA pull-down and protein stability assays.
37070251	7	68	theme	poly	1051:1054	arg1	assays					1071:1076	RNA-sequencing, co-IP, RIP, mRNA stability and poly(A)-tail length assays	1004:1076	RNA-sequencing, co-IP, RIP, mRNA stability and poly(A)-tail length assays	1004:1076	Moreover, RNA-sequencing, co-IP, RIP, mRNA stability and poly(A)-tail length assays were performed to investigate the association between LARP1 and DKK4.
37070251	2	69	theme	expression	286:295	arg1	pattern					297:303	the expression pattern	282:303	the expression pattern	282:303	However, the expression pattern and biological role of LARP1 in hepatoblastoma (HB) remain unclear so far.
37070251	7	70	theme	mRNA	1032:1035	arg1	stability					1037:1045	mRNA stability	1032:1045	mRNA stability	1032:1045	Moreover, RNA-sequencing, co-IP, RIP, mRNA stability and poly(A)-tail length assays were performed to investigate the association between LARP1 and DKK4.
37070251	2	71	from	pattern	297:303	arg1	HB					353:354	HB	353:354	HB	353:354	However, the expression pattern and biological role of LARP1 in hepatoblastoma (HB) remain unclear so far.
37070251	2	71	from	pattern	297:303	arg1	hepatoblastoma					337:350	hepatoblastoma	337:350	hepatoblastoma (HB)	337:355	However, the expression pattern and biological role of LARP1 in hepatoblastoma (HB) remain unclear so far.
37070251	9	72	theme	LARP1	1286:1290	arg1	mRNA					1292:1295	RESULTS LARP1 mRNA and protein levels	1278:1314	mRNA	1292:1295	RESULTS LARP1 mRNA and protein levels were remarkably elevated in HB tissues and associated with worse prognosis of HB patients.
37070251	7	73	theme	RIP	1027:1029	arg1	assays					1071:1076	RNA-sequencing, co-IP, RIP, mRNA stability and poly(A)-tail length assays	1004:1076	RNA-sequencing, co-IP, RIP, mRNA stability and poly(A)-tail length assays	1004:1076	Moreover, RNA-sequencing, co-IP, RIP, mRNA stability and poly(A)-tail length assays were performed to investigate the association between LARP1 and DKK4.
37070251	12	74	theme	LARP1	1776:1780	arg1	upregulation					1782:1793	LARP1 upregulation	1776:1793	LARP1 upregulation	1776:1793	LARP1 upregulation subsequently led to DKK4 mRNA stabilisation by competitively interacting with PABPC1 to prevent DKK4 mRNA from B-cell translocation gene 2-dependent deadenylation and degradation, thus facilitating β-catenin protein expression and nuclear import.
37070251	13	75	theme	HB	2198:2199	arg1	progression					2183:2193	progression	2183:2193	progression	2183:2193	CONCLUSION This study indicates that upregulated protein level of O-GlcNAcylated LARP1 mediated by circCLNS1A promotes the tumorigenesis and progression of HB through LARP1/DKK4/β-catenin axis.
37070251	13	75	theme	HB	2198:2199	arg1	tumorigenesis					2165:2177	tumorigenesis	2165:2177	tumorigenesis	2165:2177	CONCLUSION This study indicates that upregulated protein level of O-GlcNAcylated LARP1 mediated by circCLNS1A promotes the tumorigenesis and progression of HB through LARP1/DKK4/β-catenin axis.
37070251	7	76	theme	co-IP	1020:1024	arg1	assays					1071:1076	RNA-sequencing, co-IP, RIP, mRNA stability and poly(A)-tail length assays	1004:1076	RNA-sequencing, co-IP, RIP, mRNA stability and poly(A)-tail length assays	1004:1076	Moreover, RNA-sequencing, co-IP, RIP, mRNA stability and poly(A)-tail length assays were performed to investigate the association between LARP1 and DKK4.
37070251	4	77	theme	prognostic	530:539	arg1	significance					541:552	The prognostic significance	526:552	The prognostic significance of LARP1	526:561	The prognostic significance of LARP1 was evaluated by Kaplan-Meier method and multivariate Cox regression analysis.
37070251	10	78	theme	cell	1463:1466	arg1	apoptosis					1468:1476	cell apoptosis	1463:1476	cell apoptosis	1463:1476	LARP1 knockdown abolished cell proliferation, triggered cell apoptosis in vitro as well as prohibited tumour growth in vivo, whereas LARP1 overexpression incited HB progression.
37070251	13	79	theme	LARP1/DKK4/β-catenin	2209:2228	arg1	axis					2230:2233	LARP1/DKK4/β-catenin axis	2209:2233	LARP1/DKK4/β-catenin axis	2209:2233	CONCLUSION This study indicates that upregulated protein level of O-GlcNAcylated LARP1 mediated by circCLNS1A promotes the tumorigenesis and progression of HB through LARP1/DKK4/β-catenin axis.
37070251	7	80	theme	RNA-sequencing	1004:1017	arg1	assays					1071:1076	RNA-sequencing, co-IP, RIP, mRNA stability and poly(A)-tail length assays	1004:1076	RNA-sequencing, co-IP, RIP, mRNA stability and poly(A)-tail length assays	1004:1076	Moreover, RNA-sequencing, co-IP, RIP, mRNA stability and poly(A)-tail length assays were performed to investigate the association between LARP1 and DKK4.
37070251	13	81	dep	CONCLUSION	2042:2051	arg1	indicates					2064:2072	indicates	2064:2072	indicates that upregulated protein level of O-GlcNAcylated LARP1 mediated by circCLNS1A promotes the tumorigenesis and progression of HB through LARP1/DKK4/β-catenin axis	2064:2233	CONCLUSION This study indicates that upregulated protein level of O-GlcNAcylated LARP1 mediated by circCLNS1A promotes the tumorigenesis and progression of HB through LARP1/DKK4/β-catenin axis.
37070251	9	82	theme	patients	1397:1404	arg1	prognosis					1381:1389	worse prognosis	1375:1389	worse prognosis of HB patients	1375:1404	RESULTS LARP1 mRNA and protein levels were remarkably elevated in HB tissues and associated with worse prognosis of HB patients.
37070251	3	83	from	level	405:409	arg1	tissues					443:449	adjacent normal liver tissues	421:449	adjacent normal liver tissues	421:449	METHODS LARP1 expression level in HB and adjacent normal liver tissues was analysed by qRT-PCR, Western blotting and immunohistochemistry assays.
37070251	3	83	from	level	405:409	arg1	HB					414:415	HB	414:415	HB	414:415	METHODS LARP1 expression level in HB and adjacent normal liver tissues was analysed by qRT-PCR, Western blotting and immunohistochemistry assays.
37070251	12	84	theme	protein	2003:2009	arg1	expression					2011:2020	β-catenin protein expression	1993:2020	β-catenin protein expression	1993:2020	LARP1 upregulation subsequently led to DKK4 mRNA stabilisation by competitively interacting with PABPC1 to prevent DKK4 mRNA from B-cell translocation gene 2-dependent deadenylation and degradation, thus facilitating β-catenin protein expression and nuclear import.
37070251	3	85	theme	liver	437:441	arg1	tissues					443:449	adjacent normal liver tissues	421:449	adjacent normal liver tissues	421:449	METHODS LARP1 expression level in HB and adjacent normal liver tissues was analysed by qRT-PCR, Western blotting and immunohistochemistry assays.
37070251	1	86	theme	Accumulating	141:152	arg1	studies					154:160	BACKGROUND Accumulating studies	130:160	BACKGROUND Accumulating studies	130:160	BACKGROUND Accumulating studies have shown that La-related protein 1 (LARP1) is involved in the occurrence and development of various tumours.
37070251	3	87	theme	LARP1	388:392	arg1	level					405:409	METHODS LARP1 expression level	380:409	METHODS LARP1 expression level in HB and adjacent normal liver tissues	380:449	METHODS LARP1 expression level in HB and adjacent normal liver tissues was analysed by qRT-PCR, Western blotting and immunohistochemistry assays.
37070251	10	88	theme	tumour	1509:1514	arg1	growth					1516:1521	tumour growth	1509:1521	tumour growth	1509:1521	LARP1 knockdown abolished cell proliferation, triggered cell apoptosis in vitro as well as prohibited tumour growth in vivo, whereas LARP1 overexpression incited HB progression.
37070251	3	89	theme	adjacent	421:428	arg1	tissues					443:449	adjacent normal liver tissues	421:449	adjacent normal liver tissues	421:449	METHODS LARP1 expression level in HB and adjacent normal liver tissues was analysed by qRT-PCR, Western blotting and immunohistochemistry assays.
37070251	11	90	theme	LARP1	1621:1625	arg1	Ser672					1627:1632	LARP1 Ser672	1621:1632	LARP1 Ser672	1621:1632	Mechanistically, O-GlcNAcylation of LARP1 Ser672 by O-GlcNAc transferase strengthened its binding to circCLNS1A and then protected LARP1 from TRIM-25-mediated ubiquitination and proteolysis.
37070251	1	91	theme	various	256:262	arg1	tumours					264:270	various tumours	256:270	various tumours	256:270	BACKGROUND Accumulating studies have shown that La-related protein 1 (LARP1) is involved in the occurrence and development of various tumours.
37070251	0	92	theme	hepatoblastoma	68:81	arg1	progression					83:93	hepatoblastoma progression	68:93	hepatoblastoma progression	68:93	O-GlcNAcylated LARP1 positively regulated by circCLNS1A facilitates hepatoblastoma progression through DKK4/β-catenin signalling.
37070251	9	93	theme	worse	1375:1379	arg1	prognosis					1381:1389	worse prognosis	1375:1389	worse prognosis of HB patients	1375:1404	RESULTS LARP1 mRNA and protein levels were remarkably elevated in HB tissues and associated with worse prognosis of HB patients.
37070251	12	94	theme	translocation	1913:1925	arg1	deadenylation					1944:1956	B-cell translocation gene 2-dependent deadenylation	1906:1956	B-cell translocation gene 2-dependent deadenylation	1906:1956	LARP1 upregulation subsequently led to DKK4 mRNA stabilisation by competitively interacting with PABPC1 to prevent DKK4 mRNA from B-cell translocation gene 2-dependent deadenylation and degradation, thus facilitating β-catenin protein expression and nuclear import.
37070251	7	95	theme	length	1064:1069	arg1	assays					1071:1076	RNA-sequencing, co-IP, RIP, mRNA stability and poly(A)-tail length assays	1004:1076	RNA-sequencing, co-IP, RIP, mRNA stability and poly(A)-tail length assays	1004:1076	Moreover, RNA-sequencing, co-IP, RIP, mRNA stability and poly(A)-tail length assays were performed to investigate the association between LARP1 and DKK4.
37070251	6	96	theme	regulatory	775:784	arg1	roles					786:790	the regulatory roles	771:790	the regulatory roles of O-GlcNAcylation and circCLNS1A in LARP1 expression	771:844	Mechanistically, the regulatory roles of O-GlcNAcylation and circCLNS1A in LARP1 expression were investigated by co-immunoprecipitation (co-IP), immunofluorescence, RNA immunoprecipitation (RIP), RNA pull-down and protein stability assays.
37070251	3	97	theme	immunohistochemistry	497:516	arg1	qRT-PCR					467:473	qRT-PCR	467:473	qRT-PCR	467:473	METHODS LARP1 expression level in HB and adjacent normal liver tissues was analysed by qRT-PCR, Western blotting and immunohistochemistry assays.
37070251	3	97	theme	immunohistochemistry	497:516	arg1	assays					518:523	Western blotting and immunohistochemistry assays	476:523	Western blotting and immunohistochemistry assays	476:523	METHODS LARP1 expression level in HB and adjacent normal liver tissues was analysed by qRT-PCR, Western blotting and immunohistochemistry assays.
37070251	12	98	theme	2-dependent	1932:1942	arg1	deadenylation					1944:1956	B-cell translocation gene 2-dependent deadenylation	1906:1956	B-cell translocation gene 2-dependent deadenylation	1906:1956	LARP1 upregulation subsequently led to DKK4 mRNA stabilisation by competitively interacting with PABPC1 to prevent DKK4 mRNA from B-cell translocation gene 2-dependent deadenylation and degradation, thus facilitating β-catenin protein expression and nuclear import.
37070251	8	99	from	significance	1178:1189	arg1	cohorts					1230:1236	multi-centre cohorts	1217:1236	multi-centre cohorts	1217:1236	The expression and diagnostic significance of plasma DKK4 protein in multi-centre cohorts were evaluated by ELISA and ROC curves.
37070251	3	100	theme	blotting	484:491	arg1	qRT-PCR					467:473	qRT-PCR	467:473	qRT-PCR	467:473	METHODS LARP1 expression level in HB and adjacent normal liver tissues was analysed by qRT-PCR, Western blotting and immunohistochemistry assays.
37070251	3	100	theme	blotting	484:491	arg1	assays					518:523	Western blotting and immunohistochemistry assays	476:523	Western blotting and immunohistochemistry assays	476:523	METHODS LARP1 expression level in HB and adjacent normal liver tissues was analysed by qRT-PCR, Western blotting and immunohistochemistry assays.
37070251	5	101	from	effects	724:730	arg1	cells					747:751	HB cells	744:751	HB cells	744:751	In vitro and in vivo functional assays were implemented to clarify the biological effects of LARP1 on HB cells.
37070251	1	102	dep	occurrence	226:235	arg1	the					222:224	the	222:224	the	222:224	BACKGROUND Accumulating studies have shown that La-related protein 1 (LARP1) is involved in the occurrence and development of various tumours.
37070251	13	103	theme	O-GlcNAcylated	2108:2121	arg1	LARP1					2123:2127	O-GlcNAcylated LARP1	2108:2127	O-GlcNAcylated LARP1 mediated by circCLNS1A	2108:2150	CONCLUSION This study indicates that upregulated protein level of O-GlcNAcylated LARP1 mediated by circCLNS1A promotes the tumorigenesis and progression of HB through LARP1/DKK4/β-catenin axis.
31461653	5	0	theme	viruses	925:931	arg1	range					905:909	a range	903:909	a range of lethal RNA viruses, including human influenza virus	903:964	We further demonstrate that D-glucosamine, a commonly used dietary supplement, effectively protects mice against a range of lethal RNA viruses, including human influenza virus.
31461653	5	0	theme	viruses	925:931	arg1	virus					960:964	human influenza virus	944:964	human influenza virus	944:964	We further demonstrate that D-glucosamine, a commonly used dietary supplement, effectively protects mice against a range of lethal RNA viruses, including human influenza virus.
31461653	6	1	theme	host	1037:1040	arg1	immunity					1052:1059	host antiviral immunity	1037:1059	host antiviral immunity	1037:1059	Our study highlights a critical role of O-GlcNAcylation in regulating host antiviral immunity and validates D-glucosamine as a potential therapeutic for virus infections.
31461653	0	2	theme	RNA	77:79	arg1	Viruses					81:87	Lethal RNA Viruses	70:87	Lethal RNA Viruses	70:87	MAVS O-GlcNAcylation Is Essential for Host Antiviral Immunity against Lethal RNA Viruses.
31461653	3	3	theme	O-GlcNAcylation	489:503	arg1	depletion					505:513	O-GlcNAcylation depletion	489:513	O-GlcNAcylation depletion in myeloid cells	489:530	We show that O-GlcNAcylation depletion in myeloid cells renders the host more susceptible to virus infection both in vitro and in vivo.
31461653	5	4	theme	RNA	921:923	arg1	viruses					925:931	lethal RNA viruses	914:931	lethal RNA viruses	914:931	We further demonstrate that D-glucosamine, a commonly used dietary supplement, effectively protects mice against a range of lethal RNA viruses, including human influenza virus.
31461653	5	4	theme	RNA	921:923	arg1	virus					960:964	human influenza virus	944:964	human influenza virus	944:964	We further demonstrate that D-glucosamine, a commonly used dietary supplement, effectively protects mice against a range of lethal RNA viruses, including human influenza virus.
31461653	3	5	from	depletion	505:513	arg1	cells					526:530	myeloid cells	518:530	myeloid cells	518:530	We show that O-GlcNAcylation depletion in myeloid cells renders the host more susceptible to virus infection both in vitro and in vivo.
31461653	6	6	theme	O-GlcNAcylation	1007:1021	arg1	role					999:1002	a critical role	988:1002	a critical role of O-GlcNAcylation in regulating host antiviral immunity	988:1059	Our study highlights a critical role of O-GlcNAcylation in regulating host antiviral immunity and validates D-glucosamine as a potential therapeutic for virus infections.
31461653	4	7	theme	K63-linked	705:714	arg1	ubiquitination					716:729	virus-induced MAVS K63-linked ubiquitination	686:729	virus-induced MAVS K63-linked ubiquitination	686:729	Mechanistically, we demonstrate that MAVS O-GlcNAcylation is required for virus-induced MAVS K63-linked ubiquitination, thereby facilitating IRF3 activation and IFNβ production.
31461653	3	8	theme	myeloid	518:524	arg1	cells					526:530	myeloid cells	518:530	myeloid cells	518:530	We show that O-GlcNAcylation depletion in myeloid cells renders the host more susceptible to virus infection both in vitro and in vivo.
31461653	5	9	theme	influenza	950:958	arg1	virus					960:964	human influenza virus	944:964	human influenza virus	944:964	We further demonstrate that D-glucosamine, a commonly used dietary supplement, effectively protects mice against a range of lethal RNA viruses, including human influenza virus.
31461653	0	10	theme	Antiviral	43:51	arg1	Immunity					53:60	Host Antiviral Immunity	38:60	Host Antiviral Immunity against Lethal RNA Viruses	38:87	MAVS O-GlcNAcylation Is Essential for Host Antiviral Immunity against Lethal RNA Viruses.
31461653	0	11	theme	Host	38:41	arg1	Immunity					53:60	Host Antiviral Immunity	38:60	Host Antiviral Immunity against Lethal RNA Viruses	38:87	MAVS O-GlcNAcylation Is Essential for Host Antiviral Immunity against Lethal RNA Viruses.
31461653	5	12	theme	used	844:847	arg1	D-glucosamine					818:830	D-glucosamine	818:830	D-glucosamine	818:830	We further demonstrate that D-glucosamine, a commonly used dietary supplement, effectively protects mice against a range of lethal RNA viruses, including human influenza virus.
31461653	5	12	theme	used	844:847	arg1	supplement					857:866	a commonly used dietary supplement	833:866	a commonly used dietary supplement	833:866	We further demonstrate that D-glucosamine, a commonly used dietary supplement, effectively protects mice against a range of lethal RNA viruses, including human influenza virus.
31461653	2	13	theme	signaling	382:390	arg1	protein					337:343	mitochondrial antiviral-signaling protein	303:343	mitochondrial antiviral-signaling protein (MAVS)	303:350	Here, we report that the O-GlcNAcylation of mitochondrial antiviral-signaling protein (MAVS), a key mediator of interferon signaling, is a critical regulation to activate the host innate immunity against RNA viruses.
31461653	2	13	theme	signaling	382:390	arg1	mediator					359:366	a key mediator	353:366	a key mediator of interferon signaling	353:390	Here, we report that the O-GlcNAcylation of mitochondrial antiviral-signaling protein (MAVS), a key mediator of interferon signaling, is a critical regulation to activate the host innate immunity against RNA viruses.
31461653	2	14	theme	host	434:437	arg1	immunity					446:453	the host innate immunity	430:453	the host innate immunity against RNA viruses	430:473	Here, we report that the O-GlcNAcylation of mitochondrial antiviral-signaling protein (MAVS), a key mediator of interferon signaling, is a critical regulation to activate the host innate immunity against RNA viruses.
31461653	2	15	theme	antiviral-signaling	317:335	arg1	MAVS					346:349	MAVS	346:349	MAVS	346:349	Here, we report that the O-GlcNAcylation of mitochondrial antiviral-signaling protein (MAVS), a key mediator of interferon signaling, is a critical regulation to activate the host innate immunity against RNA viruses.
31461653	2	15	theme	antiviral-signaling	317:335	arg1	protein					337:343	mitochondrial antiviral-signaling protein	303:343	mitochondrial antiviral-signaling protein (MAVS)	303:350	Here, we report that the O-GlcNAcylation of mitochondrial antiviral-signaling protein (MAVS), a key mediator of interferon signaling, is a critical regulation to activate the host innate immunity against RNA viruses.
31461653	2	15	theme	antiviral-signaling	317:335	arg1	mediator					359:366	a key mediator	353:366	a key mediator of interferon signaling	353:390	Here, we report that the O-GlcNAcylation of mitochondrial antiviral-signaling protein (MAVS), a key mediator of interferon signaling, is a critical regulation to activate the host innate immunity against RNA viruses.
31461653	2	16	theme	interferon	371:380	arg1	signaling					382:390	interferon signaling	371:390	interferon signaling	371:390	Here, we report that the O-GlcNAcylation of mitochondrial antiviral-signaling protein (MAVS), a key mediator of interferon signaling, is a critical regulation to activate the host innate immunity against RNA viruses.
31461653	0	17	theme	MAVS	0:3	arg1	O-GlcNAcylation					5:19	MAVS O-GlcNAcylation	0:19	MAVS O-GlcNAcylation	0:19	MAVS O-GlcNAcylation Is Essential for Host Antiviral Immunity against Lethal RNA Viruses.
31461653	2	18	theme	mitochondrial	303:315	arg1	MAVS					346:349	MAVS	346:349	MAVS	346:349	Here, we report that the O-GlcNAcylation of mitochondrial antiviral-signaling protein (MAVS), a key mediator of interferon signaling, is a critical regulation to activate the host innate immunity against RNA viruses.
31461653	2	18	theme	mitochondrial	303:315	arg1	protein					337:343	mitochondrial antiviral-signaling protein	303:343	mitochondrial antiviral-signaling protein (MAVS)	303:350	Here, we report that the O-GlcNAcylation of mitochondrial antiviral-signaling protein (MAVS), a key mediator of interferon signaling, is a critical regulation to activate the host innate immunity against RNA viruses.
31461653	2	18	theme	mitochondrial	303:315	arg1	mediator					359:366	a key mediator	353:366	a key mediator of interferon signaling	353:390	Here, we report that the O-GlcNAcylation of mitochondrial antiviral-signaling protein (MAVS), a key mediator of interferon signaling, is a critical regulation to activate the host innate immunity against RNA viruses.
31461653	1	19	theme	metabolism	173:182	arg1	alternation					184:194	the metabolism alternation	169:194	the metabolism alternation	169:194	It is known that lethal viruses profoundly manipulate host metabolism, but how the metabolism alternation affects the immediate host antiviral immunity remains elusive.
31461653	5	20	theme	dietary	849:855	arg1	D-glucosamine					818:830	D-glucosamine	818:830	D-glucosamine	818:830	We further demonstrate that D-glucosamine, a commonly used dietary supplement, effectively protects mice against a range of lethal RNA viruses, including human influenza virus.
31461653	5	20	theme	dietary	849:855	arg1	supplement					857:866	a commonly used dietary supplement	833:866	a commonly used dietary supplement	833:866	We further demonstrate that D-glucosamine, a commonly used dietary supplement, effectively protects mice against a range of lethal RNA viruses, including human influenza virus.
31461653	6	21	theme	virus	1120:1124	arg1	infections					1126:1135	virus infections	1120:1135	virus infections	1120:1135	Our study highlights a critical role of O-GlcNAcylation in regulating host antiviral immunity and validates D-glucosamine as a potential therapeutic for virus infections.
31461653	4	22	link	K63-linked	705:714	arg1	ubiquitination					716:729	virus-induced MAVS K63-linked ubiquitination	686:729	virus-induced MAVS K63-linked ubiquitination	686:729	Mechanistically, we demonstrate that MAVS O-GlcNAcylation is required for virus-induced MAVS K63-linked ubiquitination, thereby facilitating IRF3 activation and IFNβ production.
31461653	6	23	theme	critical	990:997	arg1	role					999:1002	a critical role	988:1002	a critical role of O-GlcNAcylation in regulating host antiviral immunity	988:1059	Our study highlights a critical role of O-GlcNAcylation in regulating host antiviral immunity and validates D-glucosamine as a potential therapeutic for virus infections.
31461653	4	24	theme	IFNβ	773:776	arg1	production					778:787	IFNβ production	773:787	IFNβ production	773:787	Mechanistically, we demonstrate that MAVS O-GlcNAcylation is required for virus-induced MAVS K63-linked ubiquitination, thereby facilitating IRF3 activation and IFNβ production.
31461653	2	25	theme	critical	398:405	arg1	O-GlcNAcylation					284:298	the O-GlcNAcylation	280:298	the O-GlcNAcylation of mitochondrial antiviral-signaling protein (MAVS), a key mediator of interferon signaling,	280:391	Here, we report that the O-GlcNAcylation of mitochondrial antiviral-signaling protein (MAVS), a key mediator of interferon signaling, is a critical regulation to activate the host innate immunity against RNA viruses.
31461653	2	25	theme	critical	398:405	arg1	regulation					407:416	a critical regulation	396:416	a critical regulation to activate the host innate immunity against RNA viruses	396:473	Here, we report that the O-GlcNAcylation of mitochondrial antiviral-signaling protein (MAVS), a key mediator of interferon signaling, is a critical regulation to activate the host innate immunity against RNA viruses.
31461653	2	26	theme	RNA	463:465	arg1	viruses					467:473	RNA viruses	463:473	RNA viruses	463:473	Here, we report that the O-GlcNAcylation of mitochondrial antiviral-signaling protein (MAVS), a key mediator of interferon signaling, is a critical regulation to activate the host innate immunity against RNA viruses.
31461653	5	27	theme	human	944:948	arg1	virus					960:964	human influenza virus	944:964	human influenza virus	944:964	We further demonstrate that D-glucosamine, a commonly used dietary supplement, effectively protects mice against a range of lethal RNA viruses, including human influenza virus.
31461653	4	28	theme	MAVS	649:652	arg1	O-GlcNAcylation					654:668	MAVS O-GlcNAcylation	649:668	MAVS O-GlcNAcylation	649:668	Mechanistically, we demonstrate that MAVS O-GlcNAcylation is required for virus-induced MAVS K63-linked ubiquitination, thereby facilitating IRF3 activation and IFNβ production.
31461653	3	29	theme	in vitro	590:597	arg1	and in vivo					599:609	in vitro and in vivo	590:609	in vitro and in vivo	590:609	We show that O-GlcNAcylation depletion in myeloid cells renders the host more susceptible to virus infection both in vitro and in vivo.
31461653	1	30	theme	immediate	208:216	arg1	immunity					233:240	the immediate host antiviral immunity	204:240	the immediate host antiviral immunity	204:240	It is known that lethal viruses profoundly manipulate host metabolism, but how the metabolism alternation affects the immediate host antiviral immunity remains elusive.
31461653	5	31	theme	lethal	914:919	arg1	viruses					925:931	lethal RNA viruses	914:931	lethal RNA viruses	914:931	We further demonstrate that D-glucosamine, a commonly used dietary supplement, effectively protects mice against a range of lethal RNA viruses, including human influenza virus.
31461653	5	31	theme	lethal	914:919	arg1	virus					960:964	human influenza virus	944:964	human influenza virus	944:964	We further demonstrate that D-glucosamine, a commonly used dietary supplement, effectively protects mice against a range of lethal RNA viruses, including human influenza virus.
31461653	3	32	theme	virus	569:573	arg1	infection					575:583	virus infection	569:583	virus infection	569:583	We show that O-GlcNAcylation depletion in myeloid cells renders the host more susceptible to virus infection both in vitro and in vivo.
31461653	2	33	theme	innate	439:444	arg1	immunity					446:453	the host innate immunity	430:453	the host innate immunity against RNA viruses	430:473	Here, we report that the O-GlcNAcylation of mitochondrial antiviral-signaling protein (MAVS), a key mediator of interferon signaling, is a critical regulation to activate the host innate immunity against RNA viruses.
31461653	1	34	theme	host	144:147	arg1	metabolism					149:158	host metabolism	144:158	host metabolism	144:158	It is known that lethal viruses profoundly manipulate host metabolism, but how the metabolism alternation affects the immediate host antiviral immunity remains elusive.
31461653	1	35	theme	lethal	107:112	arg1	viruses					114:120	lethal viruses	107:120	lethal viruses	107:120	It is known that lethal viruses profoundly manipulate host metabolism, but how the metabolism alternation affects the immediate host antiviral immunity remains elusive.
31461653	4	36	theme	virus-induced	686:698	arg1	ubiquitination					716:729	virus-induced MAVS K63-linked ubiquitination	686:729	virus-induced MAVS K63-linked ubiquitination	686:729	Mechanistically, we demonstrate that MAVS O-GlcNAcylation is required for virus-induced MAVS K63-linked ubiquitination, thereby facilitating IRF3 activation and IFNβ production.
31461653	4	37	theme	IRF3	753:756	arg1	activation					758:767	IRF3 activation	753:767	IRF3 activation	753:767	Mechanistically, we demonstrate that MAVS O-GlcNAcylation is required for virus-induced MAVS K63-linked ubiquitination, thereby facilitating IRF3 activation and IFNβ production.
31461653	1	38	theme	host	218:221	arg1	immunity					233:240	the immediate host antiviral immunity	204:240	the immediate host antiviral immunity	204:240	It is known that lethal viruses profoundly manipulate host metabolism, but how the metabolism alternation affects the immediate host antiviral immunity remains elusive.
31461653	2	39	theme	protein	337:343	arg1	O-GlcNAcylation					284:298	the O-GlcNAcylation	280:298	the O-GlcNAcylation of mitochondrial antiviral-signaling protein (MAVS), a key mediator of interferon signaling,	280:391	Here, we report that the O-GlcNAcylation of mitochondrial antiviral-signaling protein (MAVS), a key mediator of interferon signaling, is a critical regulation to activate the host innate immunity against RNA viruses.
31461653	2	39	theme	protein	337:343	arg1	regulation					407:416	a critical regulation	396:416	a critical regulation to activate the host innate immunity against RNA viruses	396:473	Here, we report that the O-GlcNAcylation of mitochondrial antiviral-signaling protein (MAVS), a key mediator of interferon signaling, is a critical regulation to activate the host innate immunity against RNA viruses.
31461653	1	40	theme	antiviral	223:231	arg1	immunity					233:240	the immediate host antiviral immunity	204:240	the immediate host antiviral immunity	204:240	It is known that lethal viruses profoundly manipulate host metabolism, but how the metabolism alternation affects the immediate host antiviral immunity remains elusive.
31461653	0	41	theme	Lethal	70:75	arg1	Viruses					81:87	Lethal RNA Viruses	70:87	Lethal RNA Viruses	70:87	MAVS O-GlcNAcylation Is Essential for Host Antiviral Immunity against Lethal RNA Viruses.
31461653	4	42	theme	MAVS	700:703	arg1	ubiquitination					716:729	virus-induced MAVS K63-linked ubiquitination	686:729	virus-induced MAVS K63-linked ubiquitination	686:729	Mechanistically, we demonstrate that MAVS O-GlcNAcylation is required for virus-induced MAVS K63-linked ubiquitination, thereby facilitating IRF3 activation and IFNβ production.
31461653	3	43	dep	infection	575:583	arg1	both					585:588	both	585:588	both	585:588	We show that O-GlcNAcylation depletion in myeloid cells renders the host more susceptible to virus infection both in vitro and in vivo.
31461653	2	44	theme	key	355:357	arg1	protein					337:343	mitochondrial antiviral-signaling protein	303:343	mitochondrial antiviral-signaling protein (MAVS)	303:350	Here, we report that the O-GlcNAcylation of mitochondrial antiviral-signaling protein (MAVS), a key mediator of interferon signaling, is a critical regulation to activate the host innate immunity against RNA viruses.
31461653	2	44	theme	key	355:357	arg1	mediator					359:366	a key mediator	353:366	a key mediator of interferon signaling	353:390	Here, we report that the O-GlcNAcylation of mitochondrial antiviral-signaling protein (MAVS), a key mediator of interferon signaling, is a critical regulation to activate the host innate immunity against RNA viruses.
31461653	6	45	theme	antiviral	1042:1050	arg1	immunity					1052:1059	host antiviral immunity	1037:1059	host antiviral immunity	1037:1059	Our study highlights a critical role of O-GlcNAcylation in regulating host antiviral immunity and validates D-glucosamine as a potential therapeutic for virus infections.
30078215	0	0	theme	O-GlcNAcylation-dependent	82:106	arg1	regulation					124:133	O-GlcNAcylation-dependent transcriptional regulation	82:133	O-GlcNAcylation-dependent transcriptional regulation of GJC1	82:141	High glucose stimulates proliferative capacity of liver cancer cells possibly via O-GlcNAcylation-dependent transcriptional regulation of GJC1.
30078215	3	1	theme	cancer	661:666	arg1	cells					668:672	liver cancer cells	655:672	liver cancer cells	655:672	Using data mining, gap junction protein gamma 1 (GJC1) was identified as a critical proto-oncoprotein that is essential for the HG stimulation of proliferative capacity in liver cancer cells.
30078215	7	2	from	cells	1045:1049	arg1	O-GlcNAcylated					1014:1027	O-GlcNAcylated	1014:1027	O-GlcNAcylated	1014:1027	Interestingly, APA1, but not GJC1, can be O-GlcNAcylated in liver cancer cells.
30078215	5	3	located	located	853:859	arg2	motif					831:835	A transcription factor zinc finger protein 410 (APA1)-binding motif	769:835	A transcription factor zinc finger protein 410 (APA1)-binding motif	769:835	A transcription factor zinc finger protein 410 (APA1)-binding motif was found to be located at the -82 to -77 nt region within the GJC1 promoter.
30078215	5	3	located	located	853:859	arg1	region					882:887	the -82 to -77 nt region	864:887	the -82 to -77 nt region within the GJC1 promoter	864:912	A transcription factor zinc finger protein 410 (APA1)-binding motif was found to be located at the -82 to -77 nt region within the GJC1 promoter.
30078215	5	3	located	located	853:859	arg2	located					853:859	located	853:859	located	853:859	A transcription factor zinc finger protein 410 (APA1)-binding motif was found to be located at the -82 to -77 nt region within the GJC1 promoter.
30078215	3	4	theme	capacity	643:650	arg1	stimulation					614:624	the HG stimulation	607:624	the HG stimulation of proliferative capacity in liver cancer cells	607:672	Using data mining, gap junction protein gamma 1 (GJC1) was identified as a critical proto-oncoprotein that is essential for the HG stimulation of proliferative capacity in liver cancer cells.
30078215	7	5	theme	liver	1032:1036	arg1	cells					1045:1049	liver cancer cells	1032:1049	liver cancer cells	1032:1049	Interestingly, APA1, but not GJC1, can be O-GlcNAcylated in liver cancer cells.
30078215	11	6	with	patients	1563:1570	arg1	diabetes					1577:1584	diabetes	1577:1584	diabetes	1577:1584	Therefore, GJC1 could be a potential target for preventing liver cancer in patients with diabetes.
30078215	1	7	theme	underlying	256:265	arg1	mechanism					267:275	the underlying mechanism	252:275	the underlying mechanism	252:275	Although it is generally accepted that diabetes is one of the most important risk factors for liver cancer, the underlying mechanism is still not well understood.
30078215	9	8	theme	GJC1	1200:1203	arg1	O-GlcNAcylation					1157:1171	global O-GlcNAcylation	1150:1171	global O-GlcNAcylation	1150:1171	Notably, global O-GlcNAcylation and expression of APA1 and GJC1 were highly elevated in liver cancer patients with diabetes compared to those in patients without diabetes.
30078215	9	8	theme	GJC1	1200:1203	arg1	expression					1177:1186	expression	1177:1186	expression of APA1 and GJC1	1177:1203	Notably, global O-GlcNAcylation and expression of APA1 and GJC1 were highly elevated in liver cancer patients with diabetes compared to those in patients without diabetes.
30078215	3	9	theme	junction	506:513	arg1	protein					515:521	gap junction protein	502:521	gap junction protein gamma 1 (GJC1)	502:536	Using data mining, gap junction protein gamma 1 (GJC1) was identified as a critical proto-oncoprotein that is essential for the HG stimulation of proliferative capacity in liver cancer cells.
30078215	3	9	theme	junction	506:513	arg1	proto-oncoprotein					567:583	a critical proto-oncoprotein	556:583	a critical proto-oncoprotein that is essential for the HG stimulation of proliferative capacity in liver cancer cells	556:672	Using data mining, gap junction protein gamma 1 (GJC1) was identified as a critical proto-oncoprotein that is essential for the HG stimulation of proliferative capacity in liver cancer cells.
30078215	3	9	theme	junction	506:513	arg1	essential					593:601	essential	593:601	essential	593:601	Using data mining, gap junction protein gamma 1 (GJC1) was identified as a critical proto-oncoprotein that is essential for the HG stimulation of proliferative capacity in liver cancer cells.
30078215	3	9	theme	junction	506:513	arg1	GJC1					532:535	GJC1	532:535	GJC1	532:535	Using data mining, gap junction protein gamma 1 (GJC1) was identified as a critical proto-oncoprotein that is essential for the HG stimulation of proliferative capacity in liver cancer cells.
30078215	3	10	from	stimulation	614:624	arg1	cells					668:672	liver cancer cells	655:672	liver cancer cells	655:672	Using data mining, gap junction protein gamma 1 (GJC1) was identified as a critical proto-oncoprotein that is essential for the HG stimulation of proliferative capacity in liver cancer cells.
30078215	0	11	theme	transcriptional	108:122	arg1	regulation					124:133	O-GlcNAcylation-dependent transcriptional regulation	82:133	O-GlcNAcylation-dependent transcriptional regulation of GJC1	82:141	High glucose stimulates proliferative capacity of liver cancer cells possibly via O-GlcNAcylation-dependent transcriptional regulation of GJC1.
30078215	4	12	theme	GJC1	727:730	arg1	expression					713:722	enhanced transcriptional expression	688:722	enhanced transcriptional expression of GJC1	688:730	Furthermore, enhanced transcriptional expression of GJC1 might occur after stimulation by HG.
30078215	0	13	theme	GJC1	138:141	arg1	regulation					124:133	O-GlcNAcylation-dependent transcriptional regulation	82:133	O-GlcNAcylation-dependent transcriptional regulation of GJC1	82:141	High glucose stimulates proliferative capacity of liver cancer cells possibly via O-GlcNAcylation-dependent transcriptional regulation of GJC1.
30078215	10	14	theme	HG-stimulated	1317:1329	arg1	capacity					1345:1352	The HG-stimulated proliferative capacity	1313:1352	The HG-stimulated proliferative capacity	1313:1352	The HG-stimulated proliferative capacity was abolished upon decreasing O-GlcNAcylation, which could be reversed gradually by the simultaneous overexpression of APA1 and GJC1.
30078215	5	15	theme	GJC1	900:903	arg1	promoter					905:912	the GJC1 promoter	896:912	the GJC1 promoter	896:912	A transcription factor zinc finger protein 410 (APA1)-binding motif was found to be located at the -82 to -77 nt region within the GJC1 promoter.
30078215	8	16	theme	HG-induced	1095:1104	arg1	binding					1111:1117	HG-induced APA1 binding	1095:1117	HG-induced APA1 binding to the GJC1 promoter	1095:1138	Moreover, O-GlcNAcylation is essential for HG-induced APA1 binding to the GJC1 promoter.
30078215	2	17	theme	glucose	393:399	arg1	concentrations					375:388	high concentrations	370:388	high concentrations of glucose (HG), a major symptom of diabetes,	370:434	The purpose of the current study is to further investigate how high concentrations of glucose (HG), a major symptom of diabetes, stimulate the development of liver malignancy.
30078215	0	18	theme	liver	50:54	arg1	cells					63:67	liver cancer cells	50:67	liver cancer cells	50:67	High glucose stimulates proliferative capacity of liver cancer cells possibly via O-GlcNAcylation-dependent transcriptional regulation of GJC1.
30078215	9	19	with	patients	1242:1249	arg1	diabetes					1256:1263	diabetes	1256:1263	diabetes	1256:1263	Notably, global O-GlcNAcylation and expression of APA1 and GJC1 were highly elevated in liver cancer patients with diabetes compared to those in patients without diabetes.
30078215	3	20	theme	gap	502:504	arg1	protein					515:521	gap junction protein	502:521	gap junction protein gamma 1 (GJC1)	502:536	Using data mining, gap junction protein gamma 1 (GJC1) was identified as a critical proto-oncoprotein that is essential for the HG stimulation of proliferative capacity in liver cancer cells.
30078215	3	20	theme	gap	502:504	arg1	proto-oncoprotein					567:583	a critical proto-oncoprotein	556:583	a critical proto-oncoprotein that is essential for the HG stimulation of proliferative capacity in liver cancer cells	556:672	Using data mining, gap junction protein gamma 1 (GJC1) was identified as a critical proto-oncoprotein that is essential for the HG stimulation of proliferative capacity in liver cancer cells.
30078215	3	20	theme	gap	502:504	arg1	essential					593:601	essential	593:601	essential	593:601	Using data mining, gap junction protein gamma 1 (GJC1) was identified as a critical proto-oncoprotein that is essential for the HG stimulation of proliferative capacity in liver cancer cells.
30078215	3	20	theme	gap	502:504	arg1	GJC1					532:535	GJC1	532:535	GJC1	532:535	Using data mining, gap junction protein gamma 1 (GJC1) was identified as a critical proto-oncoprotein that is essential for the HG stimulation of proliferative capacity in liver cancer cells.
30078215	10	21	theme	proliferative	1331:1343	arg1	capacity					1345:1352	The HG-stimulated proliferative capacity	1313:1352	The HG-stimulated proliferative capacity	1313:1352	The HG-stimulated proliferative capacity was abolished upon decreasing O-GlcNAcylation, which could be reversed gradually by the simultaneous overexpression of APA1 and GJC1.
30078215	10	22	theme	GJC1	1482:1485	arg1	overexpression					1455:1468	the simultaneous overexpression	1438:1468	the simultaneous overexpression of APA1 and GJC1	1438:1485	The HG-stimulated proliferative capacity was abolished upon decreasing O-GlcNAcylation, which could be reversed gradually by the simultaneous overexpression of APA1 and GJC1.
30078215	4	23	theme	transcriptional	697:711	arg1	expression					713:722	enhanced transcriptional expression	688:722	enhanced transcriptional expression of GJC1	688:730	Furthermore, enhanced transcriptional expression of GJC1 might occur after stimulation by HG.
30078215	5	24	theme	-binding	822:829	arg1	located					853:859	located	853:859	located	853:859	A transcription factor zinc finger protein 410 (APA1)-binding motif was found to be located at the -82 to -77 nt region within the GJC1 promoter.
30078215	5	24	theme	-binding	822:829	arg1	motif					831:835	A transcription factor zinc finger protein 410 (APA1)-binding motif	769:835	A transcription factor zinc finger protein 410 (APA1)-binding motif	769:835	A transcription factor zinc finger protein 410 (APA1)-binding motif was found to be located at the -82 to -77 nt region within the GJC1 promoter.
30078215	0	25	theme	High	0:3	arg1	glucose					5:11	High glucose	0:11	High glucose	0:11	High glucose stimulates proliferative capacity of liver cancer cells possibly via O-GlcNAcylation-dependent transcriptional regulation of GJC1.
30078215	9	26	theme	liver	1229:1233	arg1	patients					1242:1249	liver cancer patients	1229:1249	liver cancer patients with diabetes	1229:1263	Notably, global O-GlcNAcylation and expression of APA1 and GJC1 were highly elevated in liver cancer patients with diabetes compared to those in patients without diabetes.
30078215	4	27	theme	enhanced	688:695	arg1	expression					713:722	enhanced transcriptional expression	688:722	enhanced transcriptional expression of GJC1	688:730	Furthermore, enhanced transcriptional expression of GJC1 might occur after stimulation by HG.
30078215	2	28	theme	high	370:373	arg1	concentrations					375:388	high concentrations	370:388	high concentrations of glucose (HG), a major symptom of diabetes,	370:434	The purpose of the current study is to further investigate how high concentrations of glucose (HG), a major symptom of diabetes, stimulate the development of liver malignancy.
30078215	0	29	theme	proliferative	24:36	arg1	capacity					38:45	proliferative capacity	24:45	proliferative capacity of liver cancer cells	24:67	High glucose stimulates proliferative capacity of liver cancer cells possibly via O-GlcNAcylation-dependent transcriptional regulation of GJC1.
30078215	5	30	theme	transcription	771:783	arg1	protein					804:810	transcription factor zinc finger protein 410	771:814	transcription factor zinc finger protein 410	771:814	A transcription factor zinc finger protein 410 (APA1)-binding motif was found to be located at the -82 to -77 nt region within the GJC1 promoter.
30078215	8	31	theme	APA1	1106:1109	arg1	binding					1111:1117	HG-induced APA1 binding	1095:1117	HG-induced APA1 binding to the GJC1 promoter	1095:1138	Moreover, O-GlcNAcylation is essential for HG-induced APA1 binding to the GJC1 promoter.
30078215	5	32	theme	nt	879:880	arg1	region					882:887	the -82 to -77 nt region	864:887	the -82 to -77 nt region within the GJC1 promoter	864:912	A transcription factor zinc finger protein 410 (APA1)-binding motif was found to be located at the -82 to -77 nt region within the GJC1 promoter.
30078215	5	33	theme	finger	797:802	arg1	protein					804:810	transcription factor zinc finger protein 410	771:814	transcription factor zinc finger protein 410	771:814	A transcription factor zinc finger protein 410 (APA1)-binding motif was found to be located at the -82 to -77 nt region within the GJC1 promoter.
30078215	5	34	theme	zinc	792:795	arg1	protein					804:810	transcription factor zinc finger protein 410	771:814	transcription factor zinc finger protein 410	771:814	A transcription factor zinc finger protein 410 (APA1)-binding motif was found to be located at the -82 to -77 nt region within the GJC1 promoter.
30078215	5	35	theme	factor	785:790	arg1	protein					804:810	transcription factor zinc finger protein 410	771:814	transcription factor zinc finger protein 410	771:814	A transcription factor zinc finger protein 410 (APA1)-binding motif was found to be located at the -82 to -77 nt region within the GJC1 promoter.
30078215	10	36	theme	APA1	1473:1476	arg1	overexpression					1455:1468	the simultaneous overexpression	1438:1468	the simultaneous overexpression of APA1 and GJC1	1438:1485	The HG-stimulated proliferative capacity was abolished upon decreasing O-GlcNAcylation, which could be reversed gradually by the simultaneous overexpression of APA1 and GJC1.
30078215	1	37	theme	important	211:219	arg1	factors					226:232	the most important risk factors	202:232	the most important risk factors for liver cancer	202:249	Although it is generally accepted that diabetes is one of the most important risk factors for liver cancer, the underlying mechanism is still not well understood.
30078215	11	38	from	cancer	1553:1558	arg1	patients					1563:1570	patients	1563:1570	patients with diabetes	1563:1584	Therefore, GJC1 could be a potential target for preventing liver cancer in patients with diabetes.
30078215	6	39	theme	GJC1	955:958	arg1	expression					960:969	GJC1 expression	955:969	GJC1 expression	955:969	Without APA1, HG was unable to increase GJC1 expression.
30078215	5	40	dep	-binding	822:829	arg1	protein					804:810	transcription factor zinc finger protein 410	771:814	transcription factor zinc finger protein 410	771:814	A transcription factor zinc finger protein 410 (APA1)-binding motif was found to be located at the -82 to -77 nt region within the GJC1 promoter.
30078215	1	41	theme	risk	221:224	arg1	factors					226:232	the most important risk factors	202:232	the most important risk factors for liver cancer	202:249	Although it is generally accepted that diabetes is one of the most important risk factors for liver cancer, the underlying mechanism is still not well understood.
30078215	2	42	theme	major	409:413	arg1	symptom					415:421	a major symptom	407:421	a major symptom of diabetes	407:433	The purpose of the current study is to further investigate how high concentrations of glucose (HG), a major symptom of diabetes, stimulate the development of liver malignancy.
30078215	2	42	theme	major	409:413	arg1	glucose					393:399	glucose	393:399	glucose (HG)	393:404	The purpose of the current study is to further investigate how high concentrations of glucose (HG), a major symptom of diabetes, stimulate the development of liver malignancy.
30078215	1	43	theme	factors	226:232	arg1	one					195:197	one	195:197	one	195:197	Although it is generally accepted that diabetes is one of the most important risk factors for liver cancer, the underlying mechanism is still not well understood.
30078215	1	43	theme	factors	226:232	arg1	factors					226:232	the most important risk factors	202:232	the most important risk factors for liver cancer	202:249	Although it is generally accepted that diabetes is one of the most important risk factors for liver cancer, the underlying mechanism is still not well understood.
30078215	0	44	theme	cancer	56:61	arg1	cells					63:67	liver cancer cells	50:67	liver cancer cells	50:67	High glucose stimulates proliferative capacity of liver cancer cells possibly via O-GlcNAcylation-dependent transcriptional regulation of GJC1.
30078215	0	45	theme	cells	63:67	arg1	capacity					38:45	proliferative capacity	24:45	proliferative capacity of liver cancer cells	24:67	High glucose stimulates proliferative capacity of liver cancer cells possibly via O-GlcNAcylation-dependent transcriptional regulation of GJC1.
30078215	11	46	theme	potential	1515:1523	arg1	target					1525:1530	a potential target	1513:1530	a potential target for preventing liver cancer in patients with diabetes	1513:1584	Therefore, GJC1 could be a potential target for preventing liver cancer in patients with diabetes.
30078215	11	46	theme	potential	1515:1523	arg1	GJC1					1499:1502	GJC1	1499:1502	GJC1	1499:1502	Therefore, GJC1 could be a potential target for preventing liver cancer in patients with diabetes.
30078215	2	47	theme	diabetes	426:433	arg1	symptom					415:421	a major symptom	407:421	a major symptom of diabetes	407:433	The purpose of the current study is to further investigate how high concentrations of glucose (HG), a major symptom of diabetes, stimulate the development of liver malignancy.
30078215	2	47	theme	diabetes	426:433	arg1	glucose					393:399	glucose	393:399	glucose (HG)	393:404	The purpose of the current study is to further investigate how high concentrations of glucose (HG), a major symptom of diabetes, stimulate the development of liver malignancy.
30078215	7	48	from	O-GlcNAcylated	1014:1027	arg1	cells					1045:1049	liver cancer cells	1032:1049	liver cancer cells	1032:1049	Interestingly, APA1, but not GJC1, can be O-GlcNAcylated in liver cancer cells.
30078215	10	49	theme	simultaneous	1442:1453	arg1	overexpression					1455:1468	the simultaneous overexpression	1438:1468	the simultaneous overexpression of APA1 and GJC1	1438:1485	The HG-stimulated proliferative capacity was abolished upon decreasing O-GlcNAcylation, which could be reversed gradually by the simultaneous overexpression of APA1 and GJC1.
30078215	9	50	theme	global	1150:1155	arg1	O-GlcNAcylation					1157:1171	global O-GlcNAcylation	1150:1171	global O-GlcNAcylation	1150:1171	Notably, global O-GlcNAcylation and expression of APA1 and GJC1 were highly elevated in liver cancer patients with diabetes compared to those in patients without diabetes.
30078215	9	51	theme	APA1	1191:1194	arg1	O-GlcNAcylation					1157:1171	global O-GlcNAcylation	1150:1171	global O-GlcNAcylation	1150:1171	Notably, global O-GlcNAcylation and expression of APA1 and GJC1 were highly elevated in liver cancer patients with diabetes compared to those in patients without diabetes.
30078215	9	51	theme	APA1	1191:1194	arg1	expression					1177:1186	expression	1177:1186	expression of APA1 and GJC1	1177:1203	Notably, global O-GlcNAcylation and expression of APA1 and GJC1 were highly elevated in liver cancer patients with diabetes compared to those in patients without diabetes.
30078215	2	52	theme	study	334:338	arg1	purpose					311:317	The purpose	307:317	The purpose of the current study	307:338	The purpose of the current study is to further investigate how high concentrations of glucose (HG), a major symptom of diabetes, stimulate the development of liver malignancy.
30078215	11	53	theme	liver	1547:1551	arg1	cancer					1553:1558	liver cancer	1547:1558	liver cancer in patients with diabetes	1547:1584	Therefore, GJC1 could be a potential target for preventing liver cancer in patients with diabetes.
30078215	3	54	theme	proliferative	629:641	arg1	capacity					643:650	proliferative capacity	629:650	proliferative capacity	629:650	Using data mining, gap junction protein gamma 1 (GJC1) was identified as a critical proto-oncoprotein that is essential for the HG stimulation of proliferative capacity in liver cancer cells.
30078215	7	55	theme	cancer	1038:1043	arg1	cells					1045:1049	liver cancer cells	1032:1049	liver cancer cells	1032:1049	Interestingly, APA1, but not GJC1, can be O-GlcNAcylated in liver cancer cells.
30078215	2	56	theme	current	326:332	arg1	study					334:338	the current study	322:338	the current study	322:338	The purpose of the current study is to further investigate how high concentrations of glucose (HG), a major symptom of diabetes, stimulate the development of liver malignancy.
30078215	5	57	from	region	882:887	arg1	located					853:859	located	853:859	located	853:859	A transcription factor zinc finger protein 410 (APA1)-binding motif was found to be located at the -82 to -77 nt region within the GJC1 promoter.
30078215	5	57	from	region	882:887	arg1	motif					831:835	A transcription factor zinc finger protein 410 (APA1)-binding motif	769:835	A transcription factor zinc finger protein 410 (APA1)-binding motif	769:835	A transcription factor zinc finger protein 410 (APA1)-binding motif was found to be located at the -82 to -77 nt region within the GJC1 promoter.
30078215	3	58	theme	HG	611:612	arg1	stimulation					614:624	the HG stimulation	607:624	the HG stimulation of proliferative capacity in liver cancer cells	607:672	Using data mining, gap junction protein gamma 1 (GJC1) was identified as a critical proto-oncoprotein that is essential for the HG stimulation of proliferative capacity in liver cancer cells.
30078215	9	59	theme	cancer	1235:1240	arg1	patients					1242:1249	liver cancer patients	1229:1249	liver cancer patients with diabetes	1229:1263	Notably, global O-GlcNAcylation and expression of APA1 and GJC1 were highly elevated in liver cancer patients with diabetes compared to those in patients without diabetes.
30078215	3	60	dep	protein	515:521	arg1	gamma					523:527	gamma 1	523:529	gap junction protein gamma 1 (GJC1)	502:536	Using data mining, gap junction protein gamma 1 (GJC1) was identified as a critical proto-oncoprotein that is essential for the HG stimulation of proliferative capacity in liver cancer cells.
30078215	8	61	theme	GJC1	1126:1129	arg1	promoter					1131:1138	the GJC1 promoter	1122:1138	the GJC1 promoter	1122:1138	Moreover, O-GlcNAcylation is essential for HG-induced APA1 binding to the GJC1 promoter.
30078215	1	62	theme	liver	238:242	arg1	cancer					244:249	liver cancer	238:249	liver cancer	238:249	Although it is generally accepted that diabetes is one of the most important risk factors for liver cancer, the underlying mechanism is still not well understood.
30078215	2	63	theme	malignancy	471:480	arg1	development					450:460	the development	446:460	the development of liver malignancy	446:480	The purpose of the current study is to further investigate how high concentrations of glucose (HG), a major symptom of diabetes, stimulate the development of liver malignancy.
30078215	9	64	gly	O-GlcNAcylation	1157:1171	arg1	patients					1242:1249	liver cancer patients	1229:1249	liver cancer patients with diabetes	1229:1263	Notably, global O-GlcNAcylation and expression of APA1 and GJC1 were highly elevated in liver cancer patients with diabetes compared to those in patients without diabetes.
30078215	2	65	theme	liver	465:469	arg1	malignancy					471:480	liver malignancy	465:480	liver malignancy	465:480	The purpose of the current study is to further investigate how high concentrations of glucose (HG), a major symptom of diabetes, stimulate the development of liver malignancy.
30078215	3	66	theme	liver	655:659	arg1	cells					668:672	liver cancer cells	655:672	liver cancer cells	655:672	Using data mining, gap junction protein gamma 1 (GJC1) was identified as a critical proto-oncoprotein that is essential for the HG stimulation of proliferative capacity in liver cancer cells.
30078215	3	67	theme	critical	558:565	arg1	protein					515:521	gap junction protein	502:521	gap junction protein gamma 1 (GJC1)	502:536	Using data mining, gap junction protein gamma 1 (GJC1) was identified as a critical proto-oncoprotein that is essential for the HG stimulation of proliferative capacity in liver cancer cells.
30078215	3	67	theme	critical	558:565	arg1	proto-oncoprotein					567:583	a critical proto-oncoprotein	556:583	a critical proto-oncoprotein that is essential for the HG stimulation of proliferative capacity in liver cancer cells	556:672	Using data mining, gap junction protein gamma 1 (GJC1) was identified as a critical proto-oncoprotein that is essential for the HG stimulation of proliferative capacity in liver cancer cells.
30078215	3	67	theme	critical	558:565	arg1	essential					593:601	essential	593:601	essential	593:601	Using data mining, gap junction protein gamma 1 (GJC1) was identified as a critical proto-oncoprotein that is essential for the HG stimulation of proliferative capacity in liver cancer cells.
30078215	5	68	dep	region	882:887	arg1	to					872:873	to	872:873	to	872:873	A transcription factor zinc finger protein 410 (APA1)-binding motif was found to be located at the -82 to -77 nt region within the GJC1 promoter.
29671171	0	0	theme	post-translational	67:84	arg1	modification					86:97	post-translational modification	67:97	post-translational modification by OGT	67:104	New use for CETSA: monitoring innate immune receptor stability via post-translational modification by OGT.
29671171	1	1	theme	diverse	153:159	arg1	modification					180:191	a dynamic and functionally diverse post-translational modification	126:191	a dynamic and functionally diverse post-translational modification shown to affect thousands of proteins, including the innate immune receptor nucleotide-binding oligomerization domain-containing protein 2 (Nod2)	126:337	O-GlcNAcylation is a dynamic and functionally diverse post-translational modification shown to affect thousands of proteins, including the innate immune receptor nucleotide-binding oligomerization domain-containing protein 2 (Nod2).
29671171	1	1	theme	diverse	153:159	arg1	O-GlcNAcylation					107:121	O-GlcNAcylation	107:121	O-GlcNAcylation	107:121	O-GlcNAcylation is a dynamic and functionally diverse post-translational modification shown to affect thousands of proteins, including the innate immune receptor nucleotide-binding oligomerization domain-containing protein 2 (Nod2).
29671171	1	2	theme	receptor	260:267	arg1	protein					322:328	the innate immune receptor nucleotide-binding oligomerization domain-containing protein 2	242:330	the innate immune receptor nucleotide-binding oligomerization domain-containing protein 2 (Nod2)	242:337	O-GlcNAcylation is a dynamic and functionally diverse post-translational modification shown to affect thousands of proteins, including the innate immune receptor nucleotide-binding oligomerization domain-containing protein 2 (Nod2).
29671171	1	2	theme	receptor	260:267	arg1	Nod2					333:336	Nod2	333:336	Nod2	333:336	O-GlcNAcylation is a dynamic and functionally diverse post-translational modification shown to affect thousands of proteins, including the innate immune receptor nucleotide-binding oligomerization domain-containing protein 2 (Nod2).
29671171	8	3	from	effect	1478:1483	arg1	proteins					1541:1548	O-GlcNAc-transferase (OGT) client proteins	1507:1548	O-GlcNAc-transferase (OGT) client proteins	1507:1548	The results presented here demonstrate that CETSA is a convenient method that can be used to detect the stability effect of O-GlcNAcylation on O-GlcNAc-transferase (OGT) client proteins and will be a powerful tool in studying post-translational modification.
29671171	2	4	contain	have	425:428	arg1	Mutations					340:348	Mutations	340:348	Mutations of Nod2 (R702W, G908R and 1007 fs)	340:383	Mutations of Nod2 (R702W, G908R and 1007 fs) are associated with Crohn's disease and have lower stabilities compared to wild type.
29671171	2	4	contain	have	425:428	arg2	stabilities					436:446	lower stabilities	430:446	lower stabilities compared to wild type	430:468	Mutations of Nod2 (R702W, G908R and 1007 fs) are associated with Crohn's disease and have lower stabilities compared to wild type.
29671171	1	5	theme	post-translational	161:178	arg1	modification					180:191	a dynamic and functionally diverse post-translational modification	126:191	a dynamic and functionally diverse post-translational modification shown to affect thousands of proteins, including the innate immune receptor nucleotide-binding oligomerization domain-containing protein 2 (Nod2)	126:337	O-GlcNAcylation is a dynamic and functionally diverse post-translational modification shown to affect thousands of proteins, including the innate immune receptor nucleotide-binding oligomerization domain-containing protein 2 (Nod2).
29671171	1	5	theme	post-translational	161:178	arg1	O-GlcNAcylation					107:121	O-GlcNAcylation	107:121	O-GlcNAcylation	107:121	O-GlcNAcylation is a dynamic and functionally diverse post-translational modification shown to affect thousands of proteins, including the innate immune receptor nucleotide-binding oligomerization domain-containing protein 2 (Nod2).
29671171	8	6	theme	O-GlcNAcylation	1488:1502	arg1	effect					1478:1483	the stability effect	1464:1483	the stability effect of O-GlcNAcylation on O-GlcNAc-transferase (OGT) client proteins	1464:1548	The results presented here demonstrate that CETSA is a convenient method that can be used to detect the stability effect of O-GlcNAcylation on O-GlcNAc-transferase (OGT) client proteins and will be a powerful tool in studying post-translational modification.
29671171	1	7	theme	nucleotide-binding	269:286	arg1	protein					322:328	the innate immune receptor nucleotide-binding oligomerization domain-containing protein 2	242:330	the innate immune receptor nucleotide-binding oligomerization domain-containing protein 2 (Nod2)	242:337	O-GlcNAcylation is a dynamic and functionally diverse post-translational modification shown to affect thousands of proteins, including the innate immune receptor nucleotide-binding oligomerization domain-containing protein 2 (Nod2).
29671171	1	7	theme	nucleotide-binding	269:286	arg1	Nod2					333:336	Nod2	333:336	Nod2	333:336	O-GlcNAcylation is a dynamic and functionally diverse post-translational modification shown to affect thousands of proteins, including the innate immune receptor nucleotide-binding oligomerization domain-containing protein 2 (Nod2).
29671171	5	8	theme	protein	980:986	arg1	stabilization					988:1000	protein stabilization	980:1000	protein stabilization	980:1000	Here, a recently developed cellular thermal shift assay (CETSA) that is typically used to demonstrate protein-ligand binding was adapted to detect shifts in protein stabilization upon increasing O-GlcNAcylation levels in Nod2.
29671171	6	9	theme	Nod2	1121:1124	arg1	variants					1126:1133	other Crohn's associated Nod2 variants	1096:1133	other Crohn's associated Nod2 variants	1096:1133	This assay was used as a method to predict if other Crohn's associated Nod2 variants were O-GlcNAcylated, and also identified the modification on another NLR, Nod1.
29671171	1	10	theme	oligomerization	288:302	arg1	protein					322:328	the innate immune receptor nucleotide-binding oligomerization domain-containing protein 2	242:330	the innate immune receptor nucleotide-binding oligomerization domain-containing protein 2 (Nod2)	242:337	O-GlcNAcylation is a dynamic and functionally diverse post-translational modification shown to affect thousands of proteins, including the innate immune receptor nucleotide-binding oligomerization domain-containing protein 2 (Nod2).
29671171	1	10	theme	oligomerization	288:302	arg1	Nod2					333:336	Nod2	333:336	Nod2	333:336	O-GlcNAcylation is a dynamic and functionally diverse post-translational modification shown to affect thousands of proteins, including the innate immune receptor nucleotide-binding oligomerization domain-containing protein 2 (Nod2).
29671171	4	11	dep	method	659:664	arg1	assess					669:674	assess	669:674	to assess stability afforded by post-translational modifications	666:729	A more rapid method to assess stability afforded by post-translational modifications is necessary to fully comprehend the correlation between NLR stability and O-GlcNAcylation.
29671171	3	12	theme	-chase	490:495	arg1	assays					507:512	Cycloheximide (CHX)-chase half-life assays	471:512	Cycloheximide (CHX)-chase half-life assays	471:512	Cycloheximide (CHX)-chase half-life assays have been used to show that O-GlcNAcylation increases the stability and response of both wild type and Crohn's variant Nod2, R702W.
29671171	1	13	theme	domain-containing	304:320	arg1	protein					322:328	the innate immune receptor nucleotide-binding oligomerization domain-containing protein 2	242:330	the innate immune receptor nucleotide-binding oligomerization domain-containing protein 2 (Nod2)	242:337	O-GlcNAcylation is a dynamic and functionally diverse post-translational modification shown to affect thousands of proteins, including the innate immune receptor nucleotide-binding oligomerization domain-containing protein 2 (Nod2).
29671171	1	13	theme	domain-containing	304:320	arg1	Nod2					333:336	Nod2	333:336	Nod2	333:336	O-GlcNAcylation is a dynamic and functionally diverse post-translational modification shown to affect thousands of proteins, including the innate immune receptor nucleotide-binding oligomerization domain-containing protein 2 (Nod2).
29671171	8	14	theme	O-GlcNAc-transferase	1507:1526	arg1	proteins					1541:1548	O-GlcNAc-transferase (OGT) client proteins	1507:1548	O-GlcNAc-transferase (OGT) client proteins	1507:1548	The results presented here demonstrate that CETSA is a convenient method that can be used to detect the stability effect of O-GlcNAcylation on O-GlcNAc-transferase (OGT) client proteins and will be a powerful tool in studying post-translational modification.
29671171	3	15	used	used	524:527	arg2	assays					507:512	Cycloheximide (CHX)-chase half-life assays	471:512	Cycloheximide (CHX)-chase half-life assays	471:512	Cycloheximide (CHX)-chase half-life assays have been used to show that O-GlcNAcylation increases the stability and response of both wild type and Crohn's variant Nod2, R702W.
29671171	5	16	theme	thermal	859:865	arg1	CETSA					880:884	CETSA	880:884	CETSA	880:884	Here, a recently developed cellular thermal shift assay (CETSA) that is typically used to demonstrate protein-ligand binding was adapted to detect shifts in protein stabilization upon increasing O-GlcNAcylation levels in Nod2.
29671171	5	16	theme	thermal	859:865	arg1	assay					873:877	a recently developed cellular thermal shift assay	829:877	a recently developed cellular thermal shift assay (CETSA) that is typically used to demonstrate protein-ligand binding	829:946	Here, a recently developed cellular thermal shift assay (CETSA) that is typically used to demonstrate protein-ligand binding was adapted to detect shifts in protein stabilization upon increasing O-GlcNAcylation levels in Nod2.
29671171	1	17	theme	dynamic	128:134	arg1	modification					180:191	a dynamic and functionally diverse post-translational modification	126:191	a dynamic and functionally diverse post-translational modification shown to affect thousands of proteins, including the innate immune receptor nucleotide-binding oligomerization domain-containing protein 2 (Nod2)	126:337	O-GlcNAcylation is a dynamic and functionally diverse post-translational modification shown to affect thousands of proteins, including the innate immune receptor nucleotide-binding oligomerization domain-containing protein 2 (Nod2).
29671171	1	17	theme	dynamic	128:134	arg1	O-GlcNAcylation					107:121	O-GlcNAcylation	107:121	O-GlcNAcylation	107:121	O-GlcNAcylation is a dynamic and functionally diverse post-translational modification shown to affect thousands of proteins, including the innate immune receptor nucleotide-binding oligomerization domain-containing protein 2 (Nod2).
29671171	6	18	used	used	1065:1068	arg2	method					1075:1080	a method	1073:1080	a method	1073:1080	This assay was used as a method to predict if other Crohn's associated Nod2 variants were O-GlcNAcylated, and also identified the modification on another NLR, Nod1.
29671171	6	18	used	used	1065:1068	arg2	assay					1055:1059	This assay	1050:1059	This assay	1050:1059	This assay was used as a method to predict if other Crohn's associated Nod2 variants were O-GlcNAcylated, and also identified the modification on another NLR, Nod1.
29671171	8	19	theme	post-translational	1590:1607	arg1	modification					1609:1620	post-translational modification	1590:1620	post-translational modification	1590:1620	The results presented here demonstrate that CETSA is a convenient method that can be used to detect the stability effect of O-GlcNAcylation on O-GlcNAc-transferase (OGT) client proteins and will be a powerful tool in studying post-translational modification.
29671171	5	20	theme	shift	867:871	arg1	CETSA					880:884	CETSA	880:884	CETSA	880:884	Here, a recently developed cellular thermal shift assay (CETSA) that is typically used to demonstrate protein-ligand binding was adapted to detect shifts in protein stabilization upon increasing O-GlcNAcylation levels in Nod2.
29671171	5	20	theme	shift	867:871	arg1	assay					873:877	a recently developed cellular thermal shift assay	829:877	a recently developed cellular thermal shift assay (CETSA) that is typically used to demonstrate protein-ligand binding	829:946	Here, a recently developed cellular thermal shift assay (CETSA) that is typically used to demonstrate protein-ligand binding was adapted to detect shifts in protein stabilization upon increasing O-GlcNAcylation levels in Nod2.
29671171	0	21	theme	New	0:2	arg1	use					4:6	New use	0:6	New use for CETSA:	0:17	New use for CETSA: monitoring innate immune receptor stability via post-translational modification by OGT.
29671171	5	22	theme	cellular	850:857	arg1	CETSA					880:884	CETSA	880:884	CETSA	880:884	Here, a recently developed cellular thermal shift assay (CETSA) that is typically used to demonstrate protein-ligand binding was adapted to detect shifts in protein stabilization upon increasing O-GlcNAcylation levels in Nod2.
29671171	5	22	theme	cellular	850:857	arg1	assay					873:877	a recently developed cellular thermal shift assay	829:877	a recently developed cellular thermal shift assay (CETSA) that is typically used to demonstrate protein-ligand binding	829:946	Here, a recently developed cellular thermal shift assay (CETSA) that is typically used to demonstrate protein-ligand binding was adapted to detect shifts in protein stabilization upon increasing O-GlcNAcylation levels in Nod2.
29671171	2	23	dep	Nod2	353:356	arg1	R702W					359:363	R702W	359:363	R702W	359:363	Mutations of Nod2 (R702W, G908R and 1007 fs) are associated with Crohn's disease and have lower stabilities compared to wild type.
29671171	2	23	dep	Nod2	353:356	arg1	G908R					366:370	G908R	366:370	G908R	366:370	Mutations of Nod2 (R702W, G908R and 1007 fs) are associated with Crohn's disease and have lower stabilities compared to wild type.
29671171	2	23	dep	Nod2	353:356	arg1	fs					381:382	1007 fs	376:382	1007 fs	376:382	Mutations of Nod2 (R702W, G908R and 1007 fs) are associated with Crohn's disease and have lower stabilities compared to wild type.
29671171	5	24	from	levels	1034:1039	arg1	Nod2					1044:1047	Nod2	1044:1047	Nod2	1044:1047	Here, a recently developed cellular thermal shift assay (CETSA) that is typically used to demonstrate protein-ligand binding was adapted to detect shifts in protein stabilization upon increasing O-GlcNAcylation levels in Nod2.
29671171	2	25	theme	lower	430:434	arg1	stabilities					436:446	lower stabilities	430:446	lower stabilities compared to wild type	430:468	Mutations of Nod2 (R702W, G908R and 1007 fs) are associated with Crohn's disease and have lower stabilities compared to wild type.
29671171	8	26	used	used	1449:1452	arg2	method					1430:1435	a convenient method	1417:1435	a convenient method that can be used to detect the stability effect of O-GlcNAcylation on O-GlcNAc-transferase (OGT) client proteins and will be a powerful tool in studying post-translational modification	1417:1620	The results presented here demonstrate that CETSA is a convenient method that can be used to detect the stability effect of O-GlcNAcylation on O-GlcNAc-transferase (OGT) client proteins and will be a powerful tool in studying post-translational modification.
29671171	8	26	used	used	1449:1452	arg2	CETSA					1408:1412	CETSA	1408:1412	CETSA	1408:1412	The results presented here demonstrate that CETSA is a convenient method that can be used to detect the stability effect of O-GlcNAcylation on O-GlcNAc-transferase (OGT) client proteins and will be a powerful tool in studying post-translational modification.
29671171	8	27	theme	client	1534:1539	arg1	proteins					1541:1548	O-GlcNAc-transferase (OGT) client proteins	1507:1548	O-GlcNAc-transferase (OGT) client proteins	1507:1548	The results presented here demonstrate that CETSA is a convenient method that can be used to detect the stability effect of O-GlcNAcylation on O-GlcNAc-transferase (OGT) client proteins and will be a powerful tool in studying post-translational modification.
29671171	4	28	theme	post-translational	698:715	arg1	modifications					717:729	post-translational modifications	698:729	post-translational modifications	698:729	A more rapid method to assess stability afforded by post-translational modifications is necessary to fully comprehend the correlation between NLR stability and O-GlcNAcylation.
29671171	5	29	theme	protein-ligand	925:938	arg1	binding					940:946	protein-ligand binding	925:946	protein-ligand binding	925:946	Here, a recently developed cellular thermal shift assay (CETSA) that is typically used to demonstrate protein-ligand binding was adapted to detect shifts in protein stabilization upon increasing O-GlcNAcylation levels in Nod2.
29671171	3	30	theme	variant	625:631	arg1	R702W					639:643	R702W	639:643	R702W	639:643	Cycloheximide (CHX)-chase half-life assays have been used to show that O-GlcNAcylation increases the stability and response of both wild type and Crohn's variant Nod2, R702W.
29671171	3	30	theme	variant	625:631	arg1	Nod2					633:636	Crohn's variant Nod2	617:636	Crohn's variant Nod2	617:636	Cycloheximide (CHX)-chase half-life assays have been used to show that O-GlcNAcylation increases the stability and response of both wild type and Crohn's variant Nod2, R702W.
29671171	3	31	theme	half-life	497:505	arg1	assays					507:512	Cycloheximide (CHX)-chase half-life assays	471:512	Cycloheximide (CHX)-chase half-life assays	471:512	Cycloheximide (CHX)-chase half-life assays have been used to show that O-GlcNAcylation increases the stability and response of both wild type and Crohn's variant Nod2, R702W.
29671171	8	32	theme	powerful	1564:1571	arg1	tool					1573:1576	a powerful tool	1562:1576	a powerful tool in studying post-translational modification	1562:1620	The results presented here demonstrate that CETSA is a convenient method that can be used to detect the stability effect of O-GlcNAcylation on O-GlcNAc-transferase (OGT) client proteins and will be a powerful tool in studying post-translational modification.
29671171	3	33	theme	Nod2	633:636	arg1	response					586:593	response	586:593	response	586:593	Cycloheximide (CHX)-chase half-life assays have been used to show that O-GlcNAcylation increases the stability and response of both wild type and Crohn's variant Nod2, R702W.
29671171	3	33	theme	Nod2	633:636	arg1	stability					572:580	stability	572:580	stability	572:580	Cycloheximide (CHX)-chase half-life assays have been used to show that O-GlcNAcylation increases the stability and response of both wild type and Crohn's variant Nod2, R702W.
29671171	1	34	theme	proteins	222:229	arg1	thousands					209:217	thousands	209:217	thousands of proteins, including the innate immune receptor nucleotide-binding oligomerization domain-containing protein 2 (Nod2)	209:337	O-GlcNAcylation is a dynamic and functionally diverse post-translational modification shown to affect thousands of proteins, including the innate immune receptor nucleotide-binding oligomerization domain-containing protein 2 (Nod2).
29671171	3	35	dep	stability	572:580	arg1	the					568:570	the	568:570	the	568:570	Cycloheximide (CHX)-chase half-life assays have been used to show that O-GlcNAcylation increases the stability and response of both wild type and Crohn's variant Nod2, R702W.
29671171	5	36	theme	O-GlcNAcylation	1018:1032	arg1	levels					1034:1039	O-GlcNAcylation levels	1018:1039	O-GlcNAcylation levels in Nod2	1018:1047	Here, a recently developed cellular thermal shift assay (CETSA) that is typically used to demonstrate protein-ligand binding was adapted to detect shifts in protein stabilization upon increasing O-GlcNAcylation levels in Nod2.
29671171	5	37	theme	developed	840:848	arg1	CETSA					880:884	CETSA	880:884	CETSA	880:884	Here, a recently developed cellular thermal shift assay (CETSA) that is typically used to demonstrate protein-ligand binding was adapted to detect shifts in protein stabilization upon increasing O-GlcNAcylation levels in Nod2.
29671171	5	37	theme	developed	840:848	arg1	assay					873:877	a recently developed cellular thermal shift assay	829:877	a recently developed cellular thermal shift assay (CETSA) that is typically used to demonstrate protein-ligand binding	829:946	Here, a recently developed cellular thermal shift assay (CETSA) that is typically used to demonstrate protein-ligand binding was adapted to detect shifts in protein stabilization upon increasing O-GlcNAcylation levels in Nod2.
29671171	0	38	theme	immune	37:42	arg1	stability					53:61	innate immune receptor stability	30:61	innate immune receptor stability	30:61	New use for CETSA: monitoring innate immune receptor stability via post-translational modification by OGT.
29671171	0	39	theme	receptor	44:51	arg1	stability					53:61	innate immune receptor stability	30:61	innate immune receptor stability	30:61	New use for CETSA: monitoring innate immune receptor stability via post-translational modification by OGT.
29671171	7	40	used	used	1284:1287	arg2	assays					1272:1277	NF-κB transcriptional assays	1250:1277	NF-κB transcriptional assays	1250:1277	Classical immunoprecipitations and NF-κB transcriptional assays were used to confirm the presence and effect of this modification on these proteins.
29671171	7	40	used	used	1284:1287	arg2	immunoprecipitations					1225:1244	Classical immunoprecipitations	1215:1244	Classical immunoprecipitations	1215:1244	Classical immunoprecipitations and NF-κB transcriptional assays were used to confirm the presence and effect of this modification on these proteins.
29671171	6	41	theme	associated	1110:1119	arg1	variants					1126:1133	other Crohn's associated Nod2 variants	1096:1133	other Crohn's associated Nod2 variants	1096:1133	This assay was used as a method to predict if other Crohn's associated Nod2 variants were O-GlcNAcylated, and also identified the modification on another NLR, Nod1.
29671171	0	42	theme	innate	30:35	arg1	stability					53:61	innate immune receptor stability	30:61	innate immune receptor stability	30:61	New use for CETSA: monitoring innate immune receptor stability via post-translational modification by OGT.
29671171	8	43	theme	convenient	1419:1428	arg1	CETSA					1408:1412	CETSA	1408:1412	CETSA	1408:1412	The results presented here demonstrate that CETSA is a convenient method that can be used to detect the stability effect of O-GlcNAcylation on O-GlcNAc-transferase (OGT) client proteins and will be a powerful tool in studying post-translational modification.
29671171	8	43	theme	convenient	1419:1428	arg1	method					1430:1435	a convenient method	1417:1435	a convenient method that can be used to detect the stability effect of O-GlcNAcylation on O-GlcNAc-transferase (OGT) client proteins and will be a powerful tool in studying post-translational modification	1417:1620	The results presented here demonstrate that CETSA is a convenient method that can be used to detect the stability effect of O-GlcNAcylation on O-GlcNAc-transferase (OGT) client proteins and will be a powerful tool in studying post-translational modification.
29671171	4	44	theme	NLR	788:790	arg1	stability					792:800	NLR stability	788:800	NLR stability	788:800	A more rapid method to assess stability afforded by post-translational modifications is necessary to fully comprehend the correlation between NLR stability and O-GlcNAcylation.
29671171	3	45	theme	type	608:611	arg1	response					586:593	response	586:593	response	586:593	Cycloheximide (CHX)-chase half-life assays have been used to show that O-GlcNAcylation increases the stability and response of both wild type and Crohn's variant Nod2, R702W.
29671171	3	45	theme	type	608:611	arg1	stability					572:580	stability	572:580	stability	572:580	Cycloheximide (CHX)-chase half-life assays have been used to show that O-GlcNAcylation increases the stability and response of both wild type and Crohn's variant Nod2, R702W.
29671171	7	46	from	presence	1304:1311	arg1	proteins					1354:1361	these proteins	1348:1361	these proteins	1348:1361	Classical immunoprecipitations and NF-κB transcriptional assays were used to confirm the presence and effect of this modification on these proteins.
29671171	3	47	theme	Cycloheximide	471:483	arg1	assays					507:512	Cycloheximide (CHX)-chase half-life assays	471:512	Cycloheximide (CHX)-chase half-life assays	471:512	Cycloheximide (CHX)-chase half-life assays have been used to show that O-GlcNAcylation increases the stability and response of both wild type and Crohn's variant Nod2, R702W.
29671171	6	48	theme	other	1096:1100	arg1	Crohn					1102:1106	other Crohn's	1096:1108	other Crohn's associated Nod2 variants	1096:1133	This assay was used as a method to predict if other Crohn's associated Nod2 variants were O-GlcNAcylated, and also identified the modification on another NLR, Nod1.
29671171	8	49	theme	stability	1468:1476	arg1	effect					1478:1483	the stability effect	1464:1483	the stability effect of O-GlcNAcylation on O-GlcNAc-transferase (OGT) client proteins	1464:1548	The results presented here demonstrate that CETSA is a convenient method that can be used to detect the stability effect of O-GlcNAcylation on O-GlcNAc-transferase (OGT) client proteins and will be a powerful tool in studying post-translational modification.
29671171	5	50	used	used	905:908	arg2	assay					873:877	a recently developed cellular thermal shift assay	829:877	a recently developed cellular thermal shift assay (CETSA) that is typically used to demonstrate protein-ligand binding	829:946	Here, a recently developed cellular thermal shift assay (CETSA) that is typically used to demonstrate protein-ligand binding was adapted to detect shifts in protein stabilization upon increasing O-GlcNAcylation levels in Nod2.
29671171	5	50	used	used	905:908	arg2	CETSA					880:884	CETSA	880:884	CETSA	880:884	Here, a recently developed cellular thermal shift assay (CETSA) that is typically used to demonstrate protein-ligand binding was adapted to detect shifts in protein stabilization upon increasing O-GlcNAcylation levels in Nod2.
29671171	2	51	theme	Nod2	353:356	arg1	Mutations					340:348	Mutations	340:348	Mutations of Nod2 (R702W, G908R and 1007 fs)	340:383	Mutations of Nod2 (R702W, G908R and 1007 fs) are associated with Crohn's disease and have lower stabilities compared to wild type.
29671171	7	52	attach	presence	1304:1311	arg2	modification					1332:1343	this modification	1327:1343	this modification	1327:1343	Classical immunoprecipitations and NF-κB transcriptional assays were used to confirm the presence and effect of this modification on these proteins.
29671171	7	52	attach	presence	1304:1311	arg1	proteins					1354:1361	these proteins	1348:1361	these proteins	1348:1361	Classical immunoprecipitations and NF-κB transcriptional assays were used to confirm the presence and effect of this modification on these proteins.
29671171	7	53	theme	transcriptional	1256:1270	arg1	assays					1272:1277	NF-κB transcriptional assays	1250:1277	NF-κB transcriptional assays	1250:1277	Classical immunoprecipitations and NF-κB transcriptional assays were used to confirm the presence and effect of this modification on these proteins.
29671171	7	54	theme	modification	1332:1343	arg1	effect					1317:1322	effect	1317:1322	effect	1317:1322	Classical immunoprecipitations and NF-κB transcriptional assays were used to confirm the presence and effect of this modification on these proteins.
29671171	7	54	theme	modification	1332:1343	arg1	presence					1304:1311	presence	1304:1311	presence	1304:1311	Classical immunoprecipitations and NF-κB transcriptional assays were used to confirm the presence and effect of this modification on these proteins.
29671171	7	55	from	effect	1317:1322	arg1	proteins					1354:1361	these proteins	1348:1361	these proteins	1348:1361	Classical immunoprecipitations and NF-κB transcriptional assays were used to confirm the presence and effect of this modification on these proteins.
29671171	4	56	theme	rapid	653:657	arg1	method					659:664	A more rapid method	646:664	A more rapid method to assess stability afforded by post-translational modifications	646:729	A more rapid method to assess stability afforded by post-translational modifications is necessary to fully comprehend the correlation between NLR stability and O-GlcNAcylation.
29671171	4	56	theme	rapid	653:657	arg1	necessary					734:742	necessary	734:742	necessary	734:742	A more rapid method to assess stability afforded by post-translational modifications is necessary to fully comprehend the correlation between NLR stability and O-GlcNAcylation.
29671171	1	57	theme	innate	246:251	arg1	protein					322:328	the innate immune receptor nucleotide-binding oligomerization domain-containing protein 2	242:330	the innate immune receptor nucleotide-binding oligomerization domain-containing protein 2 (Nod2)	242:337	O-GlcNAcylation is a dynamic and functionally diverse post-translational modification shown to affect thousands of proteins, including the innate immune receptor nucleotide-binding oligomerization domain-containing protein 2 (Nod2).
29671171	1	57	theme	innate	246:251	arg1	Nod2					333:336	Nod2	333:336	Nod2	333:336	O-GlcNAcylation is a dynamic and functionally diverse post-translational modification shown to affect thousands of proteins, including the innate immune receptor nucleotide-binding oligomerization domain-containing protein 2 (Nod2).
29671171	2	58	theme	wild	460:463	arg1	type					465:468	wild type	460:468	wild type	460:468	Mutations of Nod2 (R702W, G908R and 1007 fs) are associated with Crohn's disease and have lower stabilities compared to wild type.
29671171	7	59	dep	presence	1304:1311	arg1	the					1300:1302	the	1300:1302	the	1300:1302	Classical immunoprecipitations and NF-κB transcriptional assays were used to confirm the presence and effect of this modification on these proteins.
29671171	3	60	theme	wild	603:606	arg1	type					608:611	wild type	603:611	wild type	603:611	Cycloheximide (CHX)-chase half-life assays have been used to show that O-GlcNAcylation increases the stability and response of both wild type and Crohn's variant Nod2, R702W.
29671171	7	61	theme	NF-κB	1250:1254	arg1	assays					1272:1277	NF-κB transcriptional assays	1250:1277	NF-κB transcriptional assays	1250:1277	Classical immunoprecipitations and NF-κB transcriptional assays were used to confirm the presence and effect of this modification on these proteins.
29671171	7	62	theme	Classical	1215:1223	arg1	immunoprecipitations					1225:1244	Classical immunoprecipitations	1215:1244	Classical immunoprecipitations	1215:1244	Classical immunoprecipitations and NF-κB transcriptional assays were used to confirm the presence and effect of this modification on these proteins.
29671171	1	63	theme	immune	253:258	arg1	protein					322:328	the innate immune receptor nucleotide-binding oligomerization domain-containing protein 2	242:330	the innate immune receptor nucleotide-binding oligomerization domain-containing protein 2 (Nod2)	242:337	O-GlcNAcylation is a dynamic and functionally diverse post-translational modification shown to affect thousands of proteins, including the innate immune receptor nucleotide-binding oligomerization domain-containing protein 2 (Nod2).
29671171	1	63	theme	immune	253:258	arg1	Nod2					333:336	Nod2	333:336	Nod2	333:336	O-GlcNAcylation is a dynamic and functionally diverse post-translational modification shown to affect thousands of proteins, including the innate immune receptor nucleotide-binding oligomerization domain-containing protein 2 (Nod2).
26369908	0	0	theme	innate	85:90	arg1	receptor					99:106	the human innate immune receptor	75:106	the human innate immune receptor	75:106	Identification and biological consequences of the O-GlcNAc modification of the human innate immune receptor, Nod2.
26369908	6	1	theme	Crohn's-associated	924:941	arg1	O-GlcNAcylated					955:968	O-GlcNAcylated	955:968	O-GlcNAcylated	955:968	We found that wild-type Nod2 and a Nod2 Crohn's-associated variant are O-GlcNAcylated and this modification affects Nod2's ability to signal via the nuclear factor kappa B pathway.
26369908	6	1	theme	Crohn's-associated	924:941	arg1	variant					943:949	a Nod2 Crohn's-associated variant	917:949	a Nod2 Crohn's-associated variant	917:949	We found that wild-type Nod2 and a Nod2 Crohn's-associated variant are O-GlcNAcylated and this modification affects Nod2's ability to signal via the nuclear factor kappa B pathway.
26369908	3	2	theme	disease	512:518	arg1	development					489:499	the development	485:499	the development of Crohn's disease	485:518	Genetic linkage analysis identified and revealed three major mutations in Nod2 that are associated with the development of Crohn's disease.
26369908	1	3	theme	muramyl	249:255	arg1	component					238:246	the bacterial peptidoglycan component	210:246	the bacterial peptidoglycan component	210:246	Nucleotide-binding oligomerization domain 2 (Nod2) is an intracellular receptor that can sense the bacterial peptidoglycan component, muramyl dipeptide.
26369908	1	3	theme	muramyl	249:255	arg1	dipeptide					257:265	muramyl dipeptide	249:265	muramyl dipeptide	249:265	Nucleotide-binding oligomerization domain 2 (Nod2) is an intracellular receptor that can sense the bacterial peptidoglycan component, muramyl dipeptide.
26369908	0	4	theme	human	79:83	arg1	receptor					99:106	the human innate immune receptor	75:106	the human innate immune receptor	75:106	Identification and biological consequences of the O-GlcNAc modification of the human innate immune receptor, Nod2.
26369908	6	5	theme	B	1054:1054	arg1	pathway					1056:1062	the nuclear factor kappa B pathway	1029:1062	the nuclear factor kappa B pathway	1029:1062	We found that wild-type Nod2 and a Nod2 Crohn's-associated variant are O-GlcNAcylated and this modification affects Nod2's ability to signal via the nuclear factor kappa B pathway.
26369908	0	6	theme	receptor	99:106	arg1	modification					59:70	the O-GlcNAc modification	46:70	the O-GlcNAc modification of the human innate immune receptor	46:106	Identification and biological consequences of the O-GlcNAc modification of the human innate immune receptor, Nod2.
26369908	6	7	theme	kappa	1048:1052	arg1	B					1054:1054	the nuclear factor kappa B	1029:1054	the nuclear factor kappa B pathway	1029:1062	We found that wild-type Nod2 and a Nod2 Crohn's-associated variant are O-GlcNAcylated and this modification affects Nod2's ability to signal via the nuclear factor kappa B pathway.
26369908	4	8	mod	modified	640:647	arg3	O-N-acetylglucosamine					652:672	O-N-acetylglucosamine	652:672	O-N-acetylglucosamine (O-GlcNAc)	652:683	The objective of this study is to further characterize this protein by determining whether Nod2 is posttranslationally modified by O-N-acetylglucosamine (O-GlcNAc).
26369908	4	8	mod	modified	640:647	arg3	O-GlcNAc					675:682	O-GlcNAc	675:682	O-GlcNAc	675:682	The objective of this study is to further characterize this protein by determining whether Nod2 is posttranslationally modified by O-N-acetylglucosamine (O-GlcNAc).
26369908	4	8	mod	modified	640:647	arg1	Nod2					612:615	Nod2	612:615	Nod2	612:615	The objective of this study is to further characterize this protein by determining whether Nod2 is posttranslationally modified by O-N-acetylglucosamine (O-GlcNAc).
26369908	6	9	theme	factor	1041:1046	arg1	B					1054:1054	the nuclear factor kappa B	1029:1054	the nuclear factor kappa B pathway	1029:1062	We found that wild-type Nod2 and a Nod2 Crohn's-associated variant are O-GlcNAcylated and this modification affects Nod2's ability to signal via the nuclear factor kappa B pathway.
26369908	1	10	theme	peptidoglycan	224:236	arg1	component					238:246	the bacterial peptidoglycan component	210:246	the bacterial peptidoglycan component	210:246	Nucleotide-binding oligomerization domain 2 (Nod2) is an intracellular receptor that can sense the bacterial peptidoglycan component, muramyl dipeptide.
26369908	1	10	theme	peptidoglycan	224:236	arg1	dipeptide					257:265	muramyl dipeptide	249:265	muramyl dipeptide	249:265	Nucleotide-binding oligomerization domain 2 (Nod2) is an intracellular receptor that can sense the bacterial peptidoglycan component, muramyl dipeptide.
26369908	5	11	theme	selected	818:825	arg1	residues					848:855	selected serine and threonine residues	818:855	selected serine and threonine residues of intracellular proteins	818:881	O-GlcNAcylation is one type of posttranslational modification in which the O-GlcNAc transferase transfers GlcNAc from UDP-GlcNAc to selected serine and threonine residues of intracellular proteins.
26369908	5	11	theme	selected	818:825	arg1	proteins					874:881	intracellular proteins	860:881	intracellular proteins	860:881	O-GlcNAcylation is one type of posttranslational modification in which the O-GlcNAc transferase transfers GlcNAc from UDP-GlcNAc to selected serine and threonine residues of intracellular proteins.
26369908	2	12	theme	various	316:322	arg1	chemokines					369:378	chemokines	369:378	chemokines	369:378	Upon activation, Nod2 induces the production of various inflammatory molecules such as cytokines and chemokines.
26369908	2	12	theme	various	316:322	arg1	molecules					337:345	various inflammatory molecules	316:345	various inflammatory molecules such as cytokines and chemokines	316:378	Upon activation, Nod2 induces the production of various inflammatory molecules such as cytokines and chemokines.
26369908	2	12	theme	various	316:322	arg1	cytokines					355:363	cytokines	355:363	cytokines	355:363	Upon activation, Nod2 induces the production of various inflammatory molecules such as cytokines and chemokines.
26369908	1	13	theme	intracellular	172:184	arg1	receptor					186:193	an intracellular receptor	169:193	an intracellular receptor that can sense the bacterial peptidoglycan component, muramyl dipeptide	169:265	Nucleotide-binding oligomerization domain 2 (Nod2) is an intracellular receptor that can sense the bacterial peptidoglycan component, muramyl dipeptide.
26369908	1	13	theme	intracellular	172:184	arg1	domain					150:155	Nucleotide-binding oligomerization domain 2	115:157	Nucleotide-binding oligomerization domain 2 (Nod2)	115:164	Nucleotide-binding oligomerization domain 2 (Nod2) is an intracellular receptor that can sense the bacterial peptidoglycan component, muramyl dipeptide.
26369908	5	14	theme	intracellular	860:872	arg1	proteins					874:881	intracellular proteins	860:881	intracellular proteins	860:881	O-GlcNAcylation is one type of posttranslational modification in which the O-GlcNAc transferase transfers GlcNAc from UDP-GlcNAc to selected serine and threonine residues of intracellular proteins.
26369908	6	15	theme	nuclear	1033:1039	arg1	B					1054:1054	the nuclear factor kappa B	1029:1054	the nuclear factor kappa B pathway	1029:1062	We found that wild-type Nod2 and a Nod2 Crohn's-associated variant are O-GlcNAcylated and this modification affects Nod2's ability to signal via the nuclear factor kappa B pathway.
26369908	3	16	theme	Genetic	381:387	arg1	analysis					397:404	Genetic linkage analysis	381:404	Genetic linkage analysis	381:404	Genetic linkage analysis identified and revealed three major mutations in Nod2 that are associated with the development of Crohn's disease.
26369908	5	17	theme	modification	735:746	arg1	type					709:712	one type	705:712	one type of posttranslational modification in which the O-GlcNAc transferase transfers GlcNAc from UDP-GlcNAc to selected serine and threonine residues of intracellular proteins	705:881	O-GlcNAcylation is one type of posttranslational modification in which the O-GlcNAc transferase transfers GlcNAc from UDP-GlcNAc to selected serine and threonine residues of intracellular proteins.
26369908	3	18	theme	linkage	389:395	arg1	analysis					397:404	Genetic linkage analysis	381:404	Genetic linkage analysis	381:404	Genetic linkage analysis identified and revealed three major mutations in Nod2 that are associated with the development of Crohn's disease.
26369908	6	19	theme	Nod2	919:922	arg1	O-GlcNAcylated					955:968	O-GlcNAcylated	955:968	O-GlcNAcylated	955:968	We found that wild-type Nod2 and a Nod2 Crohn's-associated variant are O-GlcNAcylated and this modification affects Nod2's ability to signal via the nuclear factor kappa B pathway.
26369908	6	19	theme	Nod2	919:922	arg1	variant					943:949	a Nod2 Crohn's-associated variant	917:949	a Nod2 Crohn's-associated variant	917:949	We found that wild-type Nod2 and a Nod2 Crohn's-associated variant are O-GlcNAcylated and this modification affects Nod2's ability to signal via the nuclear factor kappa B pathway.
26369908	5	20	theme	serine	827:832	arg1	residues					848:855	selected serine and threonine residues	818:855	selected serine and threonine residues of intracellular proteins	818:881	O-GlcNAcylation is one type of posttranslational modification in which the O-GlcNAc transferase transfers GlcNAc from UDP-GlcNAc to selected serine and threonine residues of intracellular proteins.
26369908	5	20	theme	serine	827:832	arg1	proteins					874:881	intracellular proteins	860:881	intracellular proteins	860:881	O-GlcNAcylation is one type of posttranslational modification in which the O-GlcNAc transferase transfers GlcNAc from UDP-GlcNAc to selected serine and threonine residues of intracellular proteins.
26369908	3	21	theme	major	436:440	arg1	mutations					442:450	three major mutations	430:450	three major mutations in Nod2 that are associated with the development of Crohn's disease	430:518	Genetic linkage analysis identified and revealed three major mutations in Nod2 that are associated with the development of Crohn's disease.
26369908	5	22	theme	proteins	874:881	arg1	residues					848:855	selected serine and threonine residues	818:855	selected serine and threonine residues of intracellular proteins	818:881	O-GlcNAcylation is one type of posttranslational modification in which the O-GlcNAc transferase transfers GlcNAc from UDP-GlcNAc to selected serine and threonine residues of intracellular proteins.
26369908	5	22	theme	proteins	874:881	arg1	proteins					874:881	intracellular proteins	860:881	intracellular proteins	860:881	O-GlcNAcylation is one type of posttranslational modification in which the O-GlcNAc transferase transfers GlcNAc from UDP-GlcNAc to selected serine and threonine residues of intracellular proteins.
26369908	0	23	theme	modification	59:70	arg1	Identification					0:13	Identification	0:13	Identification	0:13	Identification and biological consequences of the O-GlcNAc modification of the human innate immune receptor, Nod2.
26369908	0	23	theme	modification	59:70	arg1	consequences					30:41	biological consequences	19:41	biological consequences	19:41	Identification and biological consequences of the O-GlcNAc modification of the human innate immune receptor, Nod2.
26369908	0	23	theme	modification	59:70	arg1	Nod2					109:112	Nod2	109:112	Nod2	109:112	Identification and biological consequences of the O-GlcNAc modification of the human innate immune receptor, Nod2.
26369908	5	24	theme	O-GlcNAc	761:768	arg1	transferase					770:780	the O-GlcNAc transferase	757:780	the O-GlcNAc transferase	757:780	O-GlcNAcylation is one type of posttranslational modification in which the O-GlcNAc transferase transfers GlcNAc from UDP-GlcNAc to selected serine and threonine residues of intracellular proteins.
26369908	0	25	theme	O-GlcNAc	50:57	arg1	modification					59:70	the O-GlcNAc modification	46:70	the O-GlcNAc modification of the human innate immune receptor	46:106	Identification and biological consequences of the O-GlcNAc modification of the human innate immune receptor, Nod2.
26369908	6	26	theme	wild-type	898:906	arg1	Nod2					908:911	wild-type Nod2	898:911	wild-type Nod2	898:911	We found that wild-type Nod2 and a Nod2 Crohn's-associated variant are O-GlcNAcylated and this modification affects Nod2's ability to signal via the nuclear factor kappa B pathway.
26369908	1	27	theme	Nucleotide-binding	115:132	arg1	domain					150:155	Nucleotide-binding oligomerization domain 2	115:157	Nucleotide-binding oligomerization domain 2 (Nod2)	115:164	Nucleotide-binding oligomerization domain 2 (Nod2) is an intracellular receptor that can sense the bacterial peptidoglycan component, muramyl dipeptide.
26369908	1	27	theme	Nucleotide-binding	115:132	arg1	Nod2					160:163	Nod2	160:163	Nod2	160:163	Nucleotide-binding oligomerization domain 2 (Nod2) is an intracellular receptor that can sense the bacterial peptidoglycan component, muramyl dipeptide.
26369908	1	27	theme	Nucleotide-binding	115:132	arg1	receptor					186:193	an intracellular receptor	169:193	an intracellular receptor that can sense the bacterial peptidoglycan component, muramyl dipeptide	169:265	Nucleotide-binding oligomerization domain 2 (Nod2) is an intracellular receptor that can sense the bacterial peptidoglycan component, muramyl dipeptide.
26369908	4	28	theme	study	543:547	arg1	objective					525:533	The objective	521:533	The objective of this study	521:547	The objective of this study is to further characterize this protein by determining whether Nod2 is posttranslationally modified by O-N-acetylglucosamine (O-GlcNAc).
26369908	1	29	theme	oligomerization	134:148	arg1	domain					150:155	Nucleotide-binding oligomerization domain 2	115:157	Nucleotide-binding oligomerization domain 2 (Nod2)	115:164	Nucleotide-binding oligomerization domain 2 (Nod2) is an intracellular receptor that can sense the bacterial peptidoglycan component, muramyl dipeptide.
26369908	1	29	theme	oligomerization	134:148	arg1	Nod2					160:163	Nod2	160:163	Nod2	160:163	Nucleotide-binding oligomerization domain 2 (Nod2) is an intracellular receptor that can sense the bacterial peptidoglycan component, muramyl dipeptide.
26369908	1	29	theme	oligomerization	134:148	arg1	receptor					186:193	an intracellular receptor	169:193	an intracellular receptor that can sense the bacterial peptidoglycan component, muramyl dipeptide	169:265	Nucleotide-binding oligomerization domain 2 (Nod2) is an intracellular receptor that can sense the bacterial peptidoglycan component, muramyl dipeptide.
26369908	1	30	theme	bacterial	214:222	arg1	component					238:246	the bacterial peptidoglycan component	210:246	the bacterial peptidoglycan component	210:246	Nucleotide-binding oligomerization domain 2 (Nod2) is an intracellular receptor that can sense the bacterial peptidoglycan component, muramyl dipeptide.
26369908	1	30	theme	bacterial	214:222	arg1	dipeptide					257:265	muramyl dipeptide	249:265	muramyl dipeptide	249:265	Nucleotide-binding oligomerization domain 2 (Nod2) is an intracellular receptor that can sense the bacterial peptidoglycan component, muramyl dipeptide.
26369908	5	31	theme	posttranslational	717:733	arg1	modification					735:746	posttranslational modification	717:746	posttranslational modification	717:746	O-GlcNAcylation is one type of posttranslational modification in which the O-GlcNAc transferase transfers GlcNAc from UDP-GlcNAc to selected serine and threonine residues of intracellular proteins.
26369908	3	32	from	mutations	442:450	arg1	Nod2					455:458	Nod2	455:458	Nod2	455:458	Genetic linkage analysis identified and revealed three major mutations in Nod2 that are associated with the development of Crohn's disease.
26369908	2	33	theme	inflammatory	324:335	arg1	chemokines					369:378	chemokines	369:378	chemokines	369:378	Upon activation, Nod2 induces the production of various inflammatory molecules such as cytokines and chemokines.
26369908	2	33	theme	inflammatory	324:335	arg1	molecules					337:345	various inflammatory molecules	316:345	various inflammatory molecules such as cytokines and chemokines	316:378	Upon activation, Nod2 induces the production of various inflammatory molecules such as cytokines and chemokines.
26369908	2	33	theme	inflammatory	324:335	arg1	cytokines					355:363	cytokines	355:363	cytokines	355:363	Upon activation, Nod2 induces the production of various inflammatory molecules such as cytokines and chemokines.
26369908	2	34	theme	molecules	337:345	arg1	production					302:311	the production	298:311	the production of various inflammatory molecules such as cytokines and chemokines	298:378	Upon activation, Nod2 induces the production of various inflammatory molecules such as cytokines and chemokines.
26369908	5	35	from	UDP-GlcNAc	804:813	arg1	GlcNAc					792:797	GlcNAc	792:797	GlcNAc from UDP-GlcNAc	792:813	O-GlcNAcylation is one type of posttranslational modification in which the O-GlcNAc transferase transfers GlcNAc from UDP-GlcNAc to selected serine and threonine residues of intracellular proteins.
26369908	5	36	theme	threonine	838:846	arg1	residues					848:855	selected serine and threonine residues	818:855	selected serine and threonine residues of intracellular proteins	818:881	O-GlcNAcylation is one type of posttranslational modification in which the O-GlcNAc transferase transfers GlcNAc from UDP-GlcNAc to selected serine and threonine residues of intracellular proteins.
26369908	5	36	theme	threonine	838:846	arg1	proteins					874:881	intracellular proteins	860:881	intracellular proteins	860:881	O-GlcNAcylation is one type of posttranslational modification in which the O-GlcNAc transferase transfers GlcNAc from UDP-GlcNAc to selected serine and threonine residues of intracellular proteins.
26369908	0	37	theme	biological	19:28	arg1	consequences					30:41	biological consequences	19:41	biological consequences	19:41	Identification and biological consequences of the O-GlcNAc modification of the human innate immune receptor, Nod2.
26369908	0	38	theme	immune	92:97	arg1	receptor					99:106	the human innate immune receptor	75:106	the human innate immune receptor	75:106	Identification and biological consequences of the O-GlcNAc modification of the human innate immune receptor, Nod2.
32663610	8	0	theme	lipid	966:970	arg1	accumulation					972:983	lipid accumulation	966:983	lipid accumulation	966:983	Similarly, GlcN suppressed lipid accumulation in livers of overfed zebrafish.
32663610	4	1	theme	stress	484:489	arg1	inhibitors					491:500	ER stress inhibitors	481:500	ER stress inhibitors	481:500	ER stress inhibitors did not suppress HG or GlcN-mediated lipid accumulation.
32663610	5	2	theme	element-binding	661:675	arg1	protein					677:683	carbohydrate-responsive element-binding protein	637:683	carbohydrate-responsive element-binding protein (ChREBP)	637:692	HG and GlcN stimulated protein expression, DNA binding and O-GlcNAcylation of carbohydrate-responsive element-binding protein (ChREBP).
32663610	5	2	theme	element-binding	661:675	arg1	ChREBP					686:691	ChREBP	686:691	ChREBP	686:691	HG and GlcN stimulated protein expression, DNA binding and O-GlcNAcylation of carbohydrate-responsive element-binding protein (ChREBP).
32663610	7	3	dep	effect	851:856	arg1	contrast					823:830	contrast	823:830	contrast	823:830	In contrast to its stimulatory effect under NG, GlcN suppressed lipid accumulation in HepG2 cells under HG conditions.
32663610	2	4	theme	fed	325:327	arg1	larvae					339:344	normal fed zebrafish larvae	318:344	normal fed zebrafish larvae	318:344	GlcN also exerted a promotory effect on lipid accumulation in HepG2 cells under normal glucose conditions (NG, 5 mM) and liver of normal fed zebrafish larvae.
32663610	12	5	theme	lipid	1510:1514	arg1	accumulation					1516:1527	GlcN-induced lipid accumulation	1497:1527	GlcN-induced lipid accumulation	1497:1527	GlcN-induced lipid accumulation was inhibited by the AMPK activator, AICAR.
32663610	9	6	from	addition	1020:1027	arg1	stimulatory					1093:1103	stimulatory	1093:1103	stimulatory	1093:1103	In addition, GlcN activity on DNA binding and O-GlcNAcylation of ChREBP was stimulatory under NG and inhibitory under HG conditions.
32663610	5	7	theme	protein	677:683	arg1	O-GlcNAcylation					618:632	O-GlcNAcylation	618:632	O-GlcNAcylation of carbohydrate-responsive element-binding protein (ChREBP)	618:692	HG and GlcN stimulated protein expression, DNA binding and O-GlcNAcylation of carbohydrate-responsive element-binding protein (ChREBP).
32663610	5	7	theme	protein	677:683	arg1	expression					590:599	protein expression	582:599	protein expression	582:599	HG and GlcN stimulated protein expression, DNA binding and O-GlcNAcylation of carbohydrate-responsive element-binding protein (ChREBP).
32663610	5	7	theme	protein	677:683	arg1	binding					606:612	DNA binding	602:612	DNA binding	602:612	HG and GlcN stimulated protein expression, DNA binding and O-GlcNAcylation of carbohydrate-responsive element-binding protein (ChREBP).
32663610	2	8	theme	normal	318:323	arg1	larvae					339:344	normal fed zebrafish larvae	318:344	normal fed zebrafish larvae	318:344	GlcN also exerted a promotory effect on lipid accumulation in HepG2 cells under normal glucose conditions (NG, 5 mM) and liver of normal fed zebrafish larvae.
32663610	12	9	theme	GlcN-induced	1497:1508	arg1	accumulation					1516:1527	GlcN-induced lipid accumulation	1497:1527	GlcN-induced lipid accumulation	1497:1527	GlcN-induced lipid accumulation was inhibited by the AMPK activator, AICAR.
32663610	0	10	theme	normal	96:101	arg1	states					86:91	states	86:91	states of normal and excess	86:112	Glucosamine regulates hepatic lipid accumulation by sensing glucose levels or feeding states of normal and excess.
32663610	9	11	from	stimulatory	1093:1103	arg1	addition					1020:1027	addition	1020:1027	addition	1020:1027	In addition, GlcN activity on DNA binding and O-GlcNAcylation of ChREBP was stimulatory under NG and inhibitory under HG conditions.
32663610	3	12	dep	glucose	352:358	arg1	25 mM					365:369	25 mM	365:369	25 mM	365:369	High glucose (HG, 25 mM)-induced lipid accumulation was suppressed by l-glutamine-d-fructose 6-phosphate amidotransferase inhibitors.
32663610	3	12	dep	glucose	352:358	arg1	HG					361:362	HG	361:362	HG	361:362	High glucose (HG, 25 mM)-induced lipid accumulation was suppressed by l-glutamine-d-fructose 6-phosphate amidotransferase inhibitors.
32663610	8	13	theme	overfed	998:1004	arg1	zebrafish					1006:1014	overfed zebrafish	998:1014	overfed zebrafish	998:1014	Similarly, GlcN suppressed lipid accumulation in livers of overfed zebrafish.
32663610	7	14	theme	lipid	884:888	arg1	accumulation					890:901	lipid accumulation	884:901	lipid accumulation	884:901	In contrast to its stimulatory effect under NG, GlcN suppressed lipid accumulation in HepG2 cells under HG conditions.
32663610	11	15	theme	O-GlcNAcase	1392:1402	arg1	PUGNAc					1415:1420	PUGNAc	1415:1420	PUGNAc	1415:1420	The O-GlcNAc transferase inhibitor, alloxan, reduced lipid accumulation by HG or GlcN while the O-GlcNAcase inhibitor, PUGNAc, enhanced lipid accumulation in HepG2 cells and liver of zebrafish larvae.
32663610	11	15	theme	O-GlcNAcase	1392:1402	arg1	inhibitor					1404:1412	the O-GlcNAcase inhibitor	1388:1412	the O-GlcNAcase inhibitor	1388:1412	The O-GlcNAc transferase inhibitor, alloxan, reduced lipid accumulation by HG or GlcN while the O-GlcNAcase inhibitor, PUGNAc, enhanced lipid accumulation in HepG2 cells and liver of zebrafish larvae.
32663610	2	16	theme	glucose	275:281	arg1	conditions					283:292	normal glucose conditions	268:292	normal glucose conditions (NG, 5 mM)	268:303	GlcN also exerted a promotory effect on lipid accumulation in HepG2 cells under normal glucose conditions (NG, 5 mM) and liver of normal fed zebrafish larvae.
32663610	5	17	theme	DNA	602:604	arg1	binding					606:612	DNA binding	602:612	DNA binding	602:612	HG and GlcN stimulated protein expression, DNA binding and O-GlcNAcylation of carbohydrate-responsive element-binding protein (ChREBP).
32663610	2	18	dep	conditions	283:292	arg1	NG					295:296	NG	295:296	NG	295:296	GlcN also exerted a promotory effect on lipid accumulation in HepG2 cells under normal glucose conditions (NG, 5 mM) and liver of normal fed zebrafish larvae.
32663610	2	18	dep	conditions	283:292	arg1	5 mM					299:302	5 mM	299:302	5 mM	299:302	GlcN also exerted a promotory effect on lipid accumulation in HepG2 cells under normal glucose conditions (NG, 5 mM) and liver of normal fed zebrafish larvae.
32663610	2	19	from	effect	218:223	arg1	accumulation					234:245	lipid accumulation	228:245	lipid accumulation	228:245	GlcN also exerted a promotory effect on lipid accumulation in HepG2 cells under normal glucose conditions (NG, 5 mM) and liver of normal fed zebrafish larvae.
32663610	2	19	from	effect	218:223	arg1	cells					256:260	HepG2 cells	250:260	HepG2 cells	250:260	GlcN also exerted a promotory effect on lipid accumulation in HepG2 cells under normal glucose conditions (NG, 5 mM) and liver of normal fed zebrafish larvae.
32663610	0	20	theme	excess	107:112	arg1	states					86:91	states	86:91	states of normal and excess	86:112	Glucosamine regulates hepatic lipid accumulation by sensing glucose levels or feeding states of normal and excess.
32663610	2	21	theme	normal	268:273	arg1	conditions					283:292	normal glucose conditions	268:292	normal glucose conditions (NG, 5 mM)	268:303	GlcN also exerted a promotory effect on lipid accumulation in HepG2 cells under normal glucose conditions (NG, 5 mM) and liver of normal fed zebrafish larvae.
32663610	9	22	theme	ChREBP	1082:1087	arg1	binding					1051:1057	DNA binding	1047:1057	DNA binding	1047:1057	In addition, GlcN activity on DNA binding and O-GlcNAcylation of ChREBP was stimulatory under NG and inhibitory under HG conditions.
32663610	9	22	theme	ChREBP	1082:1087	arg1	O-GlcNAcylation					1063:1077	O-GlcNAcylation	1063:1077	O-GlcNAcylation	1063:1077	In addition, GlcN activity on DNA binding and O-GlcNAcylation of ChREBP was stimulatory under NG and inhibitory under HG conditions.
32663610	4	23	theme	ER	481:482	arg1	inhibitors					491:500	ER stress inhibitors	481:500	ER stress inhibitors	481:500	ER stress inhibitors did not suppress HG or GlcN-mediated lipid accumulation.
32663610	11	24	theme	larvae	1489:1494	arg1	accumulation					1438:1449	lipid accumulation	1432:1449	lipid accumulation in HepG2 cells and liver of zebrafish larvae	1432:1494	The O-GlcNAc transferase inhibitor, alloxan, reduced lipid accumulation by HG or GlcN while the O-GlcNAcase inhibitor, PUGNAc, enhanced lipid accumulation in HepG2 cells and liver of zebrafish larvae.
32663610	6	25	theme	HepG2	807:811	arg1	cells					813:817	HepG2 cells	807:817	HepG2 cells	807:817	Furthermore, both HG and GlcN increased nuclear sterol regulatory element-binding protein-1 (SREBP-1) levels in HepG2 cells.
32663610	10	26	theme	HG-induced	1256:1265	arg1	upregulation					1267:1278	HG-induced upregulation	1256:1278	HG-induced upregulation in HepG2 cells	1256:1293	Moreover, GlcN enhanced ChREBP, SREBP-1c, ACC, FAS, L-PK and SCD-1 mRNA expression under NG but inhibited HG-induced upregulation in HepG2 cells.
32663610	1	27	theme	HepG2	175:179	arg1	cells					181:185	HepG2 cells	175:185	HepG2 cells	175:185	Dose-dependent lipid accumulation was induced by glucose in HepG2 cells.
32663610	15	28	theme	fuel	1888:1891	arg1	states					1860:1865	the glucose or energy states	1838:1865	states	1860:1865	Our results collectively suggest that GlcN regulates lipogenesis by sensing the glucose or energy states of normal and excess fuel through AMPK modulation.
32663610	15	29	theme	AMPK	1901:1904	arg1	modulation					1906:1915	AMPK modulation	1901:1915	AMPK modulation	1901:1915	Our results collectively suggest that GlcN regulates lipogenesis by sensing the glucose or energy states of normal and excess fuel through AMPK modulation.
32663610	8	30	theme	zebrafish	1006:1014	arg1	livers					988:993	livers	988:993	livers of overfed zebrafish	988:1014	Similarly, GlcN suppressed lipid accumulation in livers of overfed zebrafish.
32663610	9	31	from	activity	1035:1042	arg1	binding					1051:1057	DNA binding	1047:1057	DNA binding	1047:1057	In addition, GlcN activity on DNA binding and O-GlcNAcylation of ChREBP was stimulatory under NG and inhibitory under HG conditions.
32663610	9	31	from	activity	1035:1042	arg1	O-GlcNAcylation					1063:1077	O-GlcNAcylation	1063:1077	O-GlcNAcylation	1063:1077	In addition, GlcN activity on DNA binding and O-GlcNAcylation of ChREBP was stimulatory under NG and inhibitory under HG conditions.
32663610	14	32	theme	GlcN-	1723:1727	arg1	inhibition					1750:1759	GlcN- or HG-induced p-AMPK inhibition	1723:1759	GlcN- or HG-induced p-AMPK inhibition	1723:1759	PUGNAc downregulated p-AMPK while alloxan restored GlcN- or HG-induced p-AMPK inhibition.
32663610	3	33	theme	-induced	371:378	arg1	accumulation					386:397	High glucose (HG, 25 mM)-induced lipid accumulation	347:397	High glucose (HG, 25 mM)-induced lipid accumulation	347:397	High glucose (HG, 25 mM)-induced lipid accumulation was suppressed by l-glutamine-d-fructose 6-phosphate amidotransferase inhibitors.
32663610	5	34	theme	carbohydrate-responsive	637:659	arg1	protein					677:683	carbohydrate-responsive element-binding protein	637:683	carbohydrate-responsive element-binding protein (ChREBP)	637:692	HG and GlcN stimulated protein expression, DNA binding and O-GlcNAcylation of carbohydrate-responsive element-binding protein (ChREBP).
32663610	5	34	theme	carbohydrate-responsive	637:659	arg1	ChREBP					686:691	ChREBP	686:691	ChREBP	686:691	HG and GlcN stimulated protein expression, DNA binding and O-GlcNAcylation of carbohydrate-responsive element-binding protein (ChREBP).
32663610	7	35	theme	stimulatory	839:849	arg1	effect					851:856	its stimulatory effect	835:856	its stimulatory effect under NG	835:865	In contrast to its stimulatory effect under NG, GlcN suppressed lipid accumulation in HepG2 cells under HG conditions.
32663610	3	36	theme	lipid	380:384	arg1	accumulation					386:397	High glucose (HG, 25 mM)-induced lipid accumulation	347:397	High glucose (HG, 25 mM)-induced lipid accumulation	347:397	High glucose (HG, 25 mM)-induced lipid accumulation was suppressed by l-glutamine-d-fructose 6-phosphate amidotransferase inhibitors.
32663610	0	37	theme	lipid	30:34	arg1	accumulation					36:47	hepatic lipid accumulation	22:47	hepatic lipid accumulation	22:47	Glucosamine regulates hepatic lipid accumulation by sensing glucose levels or feeding states of normal and excess.
32663610	4	38	theme	lipid	539:543	arg1	accumulation					545:556	HG or GlcN-mediated lipid accumulation	519:556	HG or GlcN-mediated lipid accumulation	519:556	ER stress inhibitors did not suppress HG or GlcN-mediated lipid accumulation.
32663610	5	39	theme	protein	582:588	arg1	expression					590:599	protein expression	582:599	protein expression	582:599	HG and GlcN stimulated protein expression, DNA binding and O-GlcNAcylation of carbohydrate-responsive element-binding protein (ChREBP).
32663610	3	40	theme	l-glutamine-d-fructose	417:438	arg1	inhibitors					469:478	l-glutamine-d-fructose 6-phosphate amidotransferase inhibitors	417:478	l-glutamine-d-fructose 6-phosphate amidotransferase inhibitors	417:478	High glucose (HG, 25 mM)-induced lipid accumulation was suppressed by l-glutamine-d-fructose 6-phosphate amidotransferase inhibitors.
32663610	0	41	theme	hepatic	22:28	arg1	accumulation					36:47	hepatic lipid accumulation	22:47	hepatic lipid accumulation	22:47	Glucosamine regulates hepatic lipid accumulation by sensing glucose levels or feeding states of normal and excess.
32663610	14	42	theme	HG-induced	1732:1741	arg1	inhibition					1750:1759	GlcN- or HG-induced p-AMPK inhibition	1723:1759	GlcN- or HG-induced p-AMPK inhibition	1723:1759	PUGNAc downregulated p-AMPK while alloxan restored GlcN- or HG-induced p-AMPK inhibition.
32663610	13	43	theme	AMPK	1592:1595	arg1	Phosphorylation					1573:1587	Phosphorylation	1573:1587	Phosphorylation of AMPK (p-AMPK)	1573:1604	Phosphorylation of AMPK (p-AMPK) was suppressed by GlcN under NG while increased by GlcN under HG.
32663610	15	44	theme	glucose	1842:1848	arg1	states					1860:1865	the glucose or energy states	1838:1865	states	1860:1865	Our results collectively suggest that GlcN regulates lipogenesis by sensing the glucose or energy states of normal and excess fuel through AMPK modulation.
32663610	11	45	theme	lipid	1432:1436	arg1	accumulation					1438:1449	lipid accumulation	1432:1449	lipid accumulation in HepG2 cells and liver of zebrafish larvae	1432:1494	The O-GlcNAc transferase inhibitor, alloxan, reduced lipid accumulation by HG or GlcN while the O-GlcNAcase inhibitor, PUGNAc, enhanced lipid accumulation in HepG2 cells and liver of zebrafish larvae.
32663610	3	46	theme	6-phosphate	440:450	arg1	inhibitors					469:478	l-glutamine-d-fructose 6-phosphate amidotransferase inhibitors	417:478	l-glutamine-d-fructose 6-phosphate amidotransferase inhibitors	417:478	High glucose (HG, 25 mM)-induced lipid accumulation was suppressed by l-glutamine-d-fructose 6-phosphate amidotransferase inhibitors.
32663610	6	47	from	levels	797:802	arg1	cells					813:817	HepG2 cells	807:817	HepG2 cells	807:817	Furthermore, both HG and GlcN increased nuclear sterol regulatory element-binding protein-1 (SREBP-1) levels in HepG2 cells.
32663610	2	48	theme	lipid	228:232	arg1	accumulation					234:245	lipid accumulation	228:245	lipid accumulation	228:245	GlcN also exerted a promotory effect on lipid accumulation in HepG2 cells under normal glucose conditions (NG, 5 mM) and liver of normal fed zebrafish larvae.
32663610	10	49	theme	HepG2	1283:1287	arg1	cells					1289:1293	HepG2 cells	1283:1293	HepG2 cells	1283:1293	Moreover, GlcN enhanced ChREBP, SREBP-1c, ACC, FAS, L-PK and SCD-1 mRNA expression under NG but inhibited HG-induced upregulation in HepG2 cells.
32663610	11	50	theme	lipid	1349:1353	arg1	accumulation					1355:1366	lipid accumulation	1349:1366	lipid accumulation	1349:1366	The O-GlcNAc transferase inhibitor, alloxan, reduced lipid accumulation by HG or GlcN while the O-GlcNAcase inhibitor, PUGNAc, enhanced lipid accumulation in HepG2 cells and liver of zebrafish larvae.
32663610	4	51	theme	HG	519:520	arg1	accumulation					545:556	HG or GlcN-mediated lipid accumulation	519:556	HG or GlcN-mediated lipid accumulation	519:556	ER stress inhibitors did not suppress HG or GlcN-mediated lipid accumulation.
32663610	15	52	theme	normal	1870:1875	arg1	fuel					1888:1891	normal and excess fuel	1870:1891	normal and excess fuel	1870:1891	Our results collectively suggest that GlcN regulates lipogenesis by sensing the glucose or energy states of normal and excess fuel through AMPK modulation.
32663610	11	53	theme	HepG2	1454:1458	arg1	cells					1460:1464	HepG2 cells	1454:1464	HepG2 cells	1454:1464	The O-GlcNAc transferase inhibitor, alloxan, reduced lipid accumulation by HG or GlcN while the O-GlcNAcase inhibitor, PUGNAc, enhanced lipid accumulation in HepG2 cells and liver of zebrafish larvae.
32663610	11	54	theme	O-GlcNAc	1300:1307	arg1	inhibitor					1321:1329	The O-GlcNAc transferase inhibitor	1296:1329	The O-GlcNAc transferase inhibitor	1296:1329	The O-GlcNAc transferase inhibitor, alloxan, reduced lipid accumulation by HG or GlcN while the O-GlcNAcase inhibitor, PUGNAc, enhanced lipid accumulation in HepG2 cells and liver of zebrafish larvae.
32663610	11	54	theme	O-GlcNAc	1300:1307	arg1	alloxan					1332:1338	alloxan	1332:1338	alloxan	1332:1338	The O-GlcNAc transferase inhibitor, alloxan, reduced lipid accumulation by HG or GlcN while the O-GlcNAcase inhibitor, PUGNAc, enhanced lipid accumulation in HepG2 cells and liver of zebrafish larvae.
32663610	0	55	theme	glucose	60:66	arg1	levels					68:73	glucose levels	60:73	glucose levels	60:73	Glucosamine regulates hepatic lipid accumulation by sensing glucose levels or feeding states of normal and excess.
32663610	11	56	from	accumulation	1438:1449	arg1	liver					1470:1474	liver	1470:1474	liver	1470:1474	The O-GlcNAc transferase inhibitor, alloxan, reduced lipid accumulation by HG or GlcN while the O-GlcNAcase inhibitor, PUGNAc, enhanced lipid accumulation in HepG2 cells and liver of zebrafish larvae.
32663610	11	56	from	accumulation	1438:1449	arg1	cells					1460:1464	HepG2 cells	1454:1464	HepG2 cells	1454:1464	The O-GlcNAc transferase inhibitor, alloxan, reduced lipid accumulation by HG or GlcN while the O-GlcNAcase inhibitor, PUGNAc, enhanced lipid accumulation in HepG2 cells and liver of zebrafish larvae.
32663610	9	57	theme	HG	1135:1136	arg1	conditions					1138:1147	HG conditions	1135:1147	HG conditions	1135:1147	In addition, GlcN activity on DNA binding and O-GlcNAcylation of ChREBP was stimulatory under NG and inhibitory under HG conditions.
32663610	4	58	theme	GlcN-mediated	525:537	arg1	accumulation					545:556	HG or GlcN-mediated lipid accumulation	519:556	HG or GlcN-mediated lipid accumulation	519:556	ER stress inhibitors did not suppress HG or GlcN-mediated lipid accumulation.
32663610	2	59	theme	promotory	208:216	arg1	effect					218:223	a promotory effect	206:223	a promotory effect on lipid accumulation in HepG2 cells	206:260	GlcN also exerted a promotory effect on lipid accumulation in HepG2 cells under normal glucose conditions (NG, 5 mM) and liver of normal fed zebrafish larvae.
32663610	6	60	theme	protein-1	777:785	arg1	levels					797:802	nuclear sterol regulatory element-binding protein-1 (SREBP-1) levels	735:802	nuclear sterol regulatory element-binding protein-1 (SREBP-1) levels in HepG2 cells	735:817	Furthermore, both HG and GlcN increased nuclear sterol regulatory element-binding protein-1 (SREBP-1) levels in HepG2 cells.
32663610	1	61	theme	Dose-dependent	115:128	arg1	accumulation					136:147	Dose-dependent lipid accumulation	115:147	Dose-dependent lipid accumulation	115:147	Dose-dependent lipid accumulation was induced by glucose in HepG2 cells.
32663610	10	62	theme	mRNA	1217:1220	arg1	expression					1222:1231	mRNA expression	1217:1231	mRNA expression	1217:1231	Moreover, GlcN enhanced ChREBP, SREBP-1c, ACC, FAS, L-PK and SCD-1 mRNA expression under NG but inhibited HG-induced upregulation in HepG2 cells.
32663610	14	63	theme	p-AMPK	1743:1748	arg1	inhibition					1750:1759	GlcN- or HG-induced p-AMPK inhibition	1723:1759	GlcN- or HG-induced p-AMPK inhibition	1723:1759	PUGNAc downregulated p-AMPK while alloxan restored GlcN- or HG-induced p-AMPK inhibition.
32663610	6	64	theme	element-binding	761:775	arg1	protein-1					777:785	sterol regulatory element-binding protein-1	743:785	nuclear sterol regulatory element-binding protein-1 (SREBP-1) levels in HepG2 cells	735:817	Furthermore, both HG and GlcN increased nuclear sterol regulatory element-binding protein-1 (SREBP-1) levels in HepG2 cells.
32663610	6	64	theme	element-binding	761:775	arg1	SREBP-1					788:794	SREBP-1	788:794	SREBP-1	788:794	Furthermore, both HG and GlcN increased nuclear sterol regulatory element-binding protein-1 (SREBP-1) levels in HepG2 cells.
32663610	1	65	theme	lipid	130:134	arg1	accumulation					136:147	Dose-dependent lipid accumulation	115:147	Dose-dependent lipid accumulation	115:147	Dose-dependent lipid accumulation was induced by glucose in HepG2 cells.
32663610	7	66	theme	HG	924:925	arg1	conditions					927:936	HG conditions	924:936	HG conditions	924:936	In contrast to its stimulatory effect under NG, GlcN suppressed lipid accumulation in HepG2 cells under HG conditions.
32663610	11	67	theme	transferase	1309:1319	arg1	inhibitor					1321:1329	The O-GlcNAc transferase inhibitor	1296:1329	The O-GlcNAc transferase inhibitor	1296:1329	The O-GlcNAc transferase inhibitor, alloxan, reduced lipid accumulation by HG or GlcN while the O-GlcNAcase inhibitor, PUGNAc, enhanced lipid accumulation in HepG2 cells and liver of zebrafish larvae.
32663610	11	67	theme	transferase	1309:1319	arg1	alloxan					1332:1338	alloxan	1332:1338	alloxan	1332:1338	The O-GlcNAc transferase inhibitor, alloxan, reduced lipid accumulation by HG or GlcN while the O-GlcNAcase inhibitor, PUGNAc, enhanced lipid accumulation in HepG2 cells and liver of zebrafish larvae.
32663610	2	68	theme	HepG2	250:254	arg1	cells					256:260	HepG2 cells	250:260	HepG2 cells	250:260	GlcN also exerted a promotory effect on lipid accumulation in HepG2 cells under normal glucose conditions (NG, 5 mM) and liver of normal fed zebrafish larvae.
32663610	6	69	theme	regulatory	750:759	arg1	protein-1					777:785	sterol regulatory element-binding protein-1	743:785	nuclear sterol regulatory element-binding protein-1 (SREBP-1) levels in HepG2 cells	735:817	Furthermore, both HG and GlcN increased nuclear sterol regulatory element-binding protein-1 (SREBP-1) levels in HepG2 cells.
32663610	6	69	theme	regulatory	750:759	arg1	SREBP-1					788:794	SREBP-1	788:794	SREBP-1	788:794	Furthermore, both HG and GlcN increased nuclear sterol regulatory element-binding protein-1 (SREBP-1) levels in HepG2 cells.
32663610	7	70	theme	HepG2	906:910	arg1	cells					912:916	HepG2 cells	906:916	HepG2 cells	906:916	In contrast to its stimulatory effect under NG, GlcN suppressed lipid accumulation in HepG2 cells under HG conditions.
32663610	3	71	theme	amidotransferase	452:467	arg1	inhibitors					469:478	l-glutamine-d-fructose 6-phosphate amidotransferase inhibitors	417:478	l-glutamine-d-fructose 6-phosphate amidotransferase inhibitors	417:478	High glucose (HG, 25 mM)-induced lipid accumulation was suppressed by l-glutamine-d-fructose 6-phosphate amidotransferase inhibitors.
32663610	10	72	from	upregulation	1267:1278	arg1	cells					1289:1293	HepG2 cells	1283:1293	HepG2 cells	1283:1293	Moreover, GlcN enhanced ChREBP, SREBP-1c, ACC, FAS, L-PK and SCD-1 mRNA expression under NG but inhibited HG-induced upregulation in HepG2 cells.
32663610	10	73	dep	SREBP-1c	1182:1189	arg1	expression					1222:1231	mRNA expression	1217:1231	mRNA expression	1217:1231	Moreover, GlcN enhanced ChREBP, SREBP-1c, ACC, FAS, L-PK and SCD-1 mRNA expression under NG but inhibited HG-induced upregulation in HepG2 cells.
32663610	11	74	theme	zebrafish	1479:1487	arg1	larvae					1489:1494	zebrafish larvae	1479:1494	zebrafish larvae	1479:1494	The O-GlcNAc transferase inhibitor, alloxan, reduced lipid accumulation by HG or GlcN while the O-GlcNAcase inhibitor, PUGNAc, enhanced lipid accumulation in HepG2 cells and liver of zebrafish larvae.
32663610	6	75	theme	sterol	743:748	arg1	protein-1					777:785	sterol regulatory element-binding protein-1	743:785	nuclear sterol regulatory element-binding protein-1 (SREBP-1) levels in HepG2 cells	735:817	Furthermore, both HG and GlcN increased nuclear sterol regulatory element-binding protein-1 (SREBP-1) levels in HepG2 cells.
32663610	6	75	theme	sterol	743:748	arg1	SREBP-1					788:794	SREBP-1	788:794	SREBP-1	788:794	Furthermore, both HG and GlcN increased nuclear sterol regulatory element-binding protein-1 (SREBP-1) levels in HepG2 cells.
32663610	2	76	theme	larvae	339:344	arg1	liver					309:313	liver	309:313	liver of normal fed zebrafish larvae	309:344	GlcN also exerted a promotory effect on lipid accumulation in HepG2 cells under normal glucose conditions (NG, 5 mM) and liver of normal fed zebrafish larvae.
32663610	2	76	theme	larvae	339:344	arg1	conditions					283:292	normal glucose conditions	268:292	normal glucose conditions (NG, 5 mM)	268:303	GlcN also exerted a promotory effect on lipid accumulation in HepG2 cells under normal glucose conditions (NG, 5 mM) and liver of normal fed zebrafish larvae.
32663610	9	77	theme	GlcN	1030:1033	arg1	activity					1035:1042	GlcN activity	1030:1042	GlcN activity on DNA binding and O-GlcNAcylation of ChREBP	1030:1087	In addition, GlcN activity on DNA binding and O-GlcNAcylation of ChREBP was stimulatory under NG and inhibitory under HG conditions.
32663610	12	78	theme	AMPK	1550:1553	arg1	AICAR					1566:1570	AICAR	1566:1570	AICAR	1566:1570	GlcN-induced lipid accumulation was inhibited by the AMPK activator, AICAR.
32663610	12	78	theme	AMPK	1550:1553	arg1	activator					1555:1563	the AMPK activator	1546:1563	the AMPK activator	1546:1563	GlcN-induced lipid accumulation was inhibited by the AMPK activator, AICAR.
32663610	15	79	theme	energy	1853:1858	arg1	states					1860:1865	the glucose or energy states	1838:1865	states	1860:1865	Our results collectively suggest that GlcN regulates lipogenesis by sensing the glucose or energy states of normal and excess fuel through AMPK modulation.
32663610	3	80	theme	High	347:350	arg1	glucose					352:358	High glucose	347:358	High glucose (HG, 25 mM)	347:370	High glucose (HG, 25 mM)-induced lipid accumulation was suppressed by l-glutamine-d-fructose 6-phosphate amidotransferase inhibitors.
32663610	6	81	theme	nuclear	735:741	arg1	levels					797:802	nuclear sterol regulatory element-binding protein-1 (SREBP-1) levels	735:802	nuclear sterol regulatory element-binding protein-1 (SREBP-1) levels in HepG2 cells	735:817	Furthermore, both HG and GlcN increased nuclear sterol regulatory element-binding protein-1 (SREBP-1) levels in HepG2 cells.
32663610	2	82	theme	zebrafish	329:337	arg1	larvae					339:344	normal fed zebrafish larvae	318:344	normal fed zebrafish larvae	318:344	GlcN also exerted a promotory effect on lipid accumulation in HepG2 cells under normal glucose conditions (NG, 5 mM) and liver of normal fed zebrafish larvae.
32663610	9	83	theme	DNA	1047:1049	arg1	binding					1051:1057	DNA binding	1047:1057	DNA binding	1047:1057	In addition, GlcN activity on DNA binding and O-GlcNAcylation of ChREBP was stimulatory under NG and inhibitory under HG conditions.
32663610	15	84	theme	excess	1881:1886	arg1	fuel					1888:1891	normal and excess fuel	1870:1891	normal and excess fuel	1870:1891	Our results collectively suggest that GlcN regulates lipogenesis by sensing the glucose or energy states of normal and excess fuel through AMPK modulation.
35422493	9	0	theme	post-translational	1304:1321	arg1	modification					1323:1334	an important post-translational modification	1291:1334	an important post-translational modification of SIRT7 in pancreatic cancer cells	1291:1370	Collectively, we demonstrate that O-GlcNAcylation is an important post-translational modification of SIRT7 in pancreatic cancer cells, and elucidating this mechanism of SIRT7 is expected to pave the way for the development of novel therapeutic methods in the future.
35422493	9	0	theme	post-translational	1304:1321	arg1	O-GlcNAcylation					1272:1286	O-GlcNAcylation	1272:1286	O-GlcNAcylation	1272:1286	Collectively, we demonstrate that O-GlcNAcylation is an important post-translational modification of SIRT7 in pancreatic cancer cells, and elucidating this mechanism of SIRT7 is expected to pave the way for the development of novel therapeutic methods in the future.
35422493	9	1	theme	cancer	1359:1364	arg1	cells					1366:1370	pancreatic cancer cells	1348:1370	pancreatic cancer cells	1348:1370	Collectively, we demonstrate that O-GlcNAcylation is an important post-translational modification of SIRT7 in pancreatic cancer cells, and elucidating this mechanism of SIRT7 is expected to pave the way for the development of novel therapeutic methods in the future.
35422493	8	2	theme	in	1135:1136	arg1	experiments					1144:1154	In vivo and in vitro experiments	1123:1154	In vivo and in vitro experiments	1123:1154	In vivo and in vitro experiments showed that blocking SIRT7 O-GlcNAcylation at S136 attenuates tumour progression.
35422493	3	3	from	roles	419:423	arg1	PDAC					428:431	PDAC	428:431	PDAC	428:431	However, its functional roles in PDAC are still unclear.
35422493	2	4	theme	transformed	360:370	arg1	state					372:376	the transformed state	356:376	the transformed state of cancer cells	356:392	SIRT7 is a classic NAD+-dependent deacetylase that stabilizes the transformed state of cancer cells.
35422493	7	5	theme	SIRT7	995:999	arg1	O-GlcNAcylation					1001:1015	SIRT7 O-GlcNAcylation	995:1015	SIRT7 O-GlcNAcylation at the serine 136 residue (S136)	995:1048	In addition, SIRT7 O-GlcNAcylation at the serine 136 residue (S136) is required to maintain its protein stability and deacetylation ability.
35422493	7	6	theme	deacetylation	1100:1112	arg1	ability					1114:1120	deacetylation ability	1100:1120	deacetylation ability	1100:1120	In addition, SIRT7 O-GlcNAcylation at the serine 136 residue (S136) is required to maintain its protein stability and deacetylation ability.
35422493	5	7	theme	SIRT7	590:594	arg1	proteins					578:585	the new interacting proteins	558:585	the new interacting proteins of SIRT7	558:594	Then we screened the new interacting proteins of SIRT7 by mass spectrometry and the results showed that SIRT7 can interact with O-GlcNAc transferase (OGT).
35422493	0	8	theme	SIRT7-REGγ	96:105	arg1	interaction					107:117	the SIRT7-REGγ interaction	92:117	the SIRT7-REGγ interaction	92:117	O-GlcNAcylation and stablization of SIRT7 promote pancreatic cancer progression by blocking the SIRT7-REGγ interaction.
35422493	9	9	theme	SIRT7	1339:1343	arg1	modification					1323:1334	an important post-translational modification	1291:1334	an important post-translational modification of SIRT7 in pancreatic cancer cells	1291:1370	Collectively, we demonstrate that O-GlcNAcylation is an important post-translational modification of SIRT7 in pancreatic cancer cells, and elucidating this mechanism of SIRT7 is expected to pave the way for the development of novel therapeutic methods in the future.
35422493	9	9	theme	SIRT7	1339:1343	arg1	O-GlcNAcylation					1272:1286	O-GlcNAcylation	1272:1286	O-GlcNAcylation	1272:1286	Collectively, we demonstrate that O-GlcNAcylation is an important post-translational modification of SIRT7 in pancreatic cancer cells, and elucidating this mechanism of SIRT7 is expected to pave the way for the development of novel therapeutic methods in the future.
35422493	1	10	theme	potential	262:270	arg1	mechanisms					282:291	the potential oncogenic mechanisms	258:291	the potential oncogenic mechanisms	258:291	Pancreatic ductal adenocarcinoma (PDAC) is one of the most lethal cancers and its dismal prognosis indicates the urgent need to elucidate the potential oncogenic mechanisms.
35422493	9	11	from	modification	1323:1334	arg1	cells					1366:1370	pancreatic cancer cells	1348:1370	pancreatic cancer cells	1348:1370	Collectively, we demonstrate that O-GlcNAcylation is an important post-translational modification of SIRT7 in pancreatic cancer cells, and elucidating this mechanism of SIRT7 is expected to pave the way for the development of novel therapeutic methods in the future.
35422493	5	12	theme	mass	599:602	arg1	spectrometry					604:615	mass spectrometry	599:615	mass spectrometry	599:615	Then we screened the new interacting proteins of SIRT7 by mass spectrometry and the results showed that SIRT7 can interact with O-GlcNAc transferase (OGT).
35422493	9	13	theme	pancreatic	1348:1357	arg1	cells					1366:1370	pancreatic cancer cells	1348:1370	pancreatic cancer cells	1348:1370	Collectively, we demonstrate that O-GlcNAcylation is an important post-translational modification of SIRT7 in pancreatic cancer cells, and elucidating this mechanism of SIRT7 is expected to pave the way for the development of novel therapeutic methods in the future.
35422493	0	14	theme	pancreatic	50:59	arg1	progression					68:78	pancreatic cancer progression	50:78	pancreatic cancer progression	50:78	O-GlcNAcylation and stablization of SIRT7 promote pancreatic cancer progression by blocking the SIRT7-REGγ interaction.
35422493	6	15	theme	H3K18	887:891	arg1	hypoacetylation					868:882	hypoacetylation	868:882	hypoacetylation of H3K18 via SIRT7, which promotes transcriptional repression of several tumour suppressor genes	868:979	O-GlcNAcylation stabilizes the SIRT7 protein by inhibiting its interaction with REGγ to prevent degradation, and hyper-O-GlcNAcylation in pancreatic cancer cells leads to hypoacetylation of H3K18 via SIRT7, which promotes transcriptional repression of several tumour suppressor genes.
35422493	8	16	dep	in	1135:1136	arg1	vitro					1138:1142	vitro	1138:1142	vitro	1138:1142	In vivo and in vitro experiments showed that blocking SIRT7 O-GlcNAcylation at S136 attenuates tumour progression.
35422493	1	17	theme	most	174:177	arg1	cancers					186:192	the most lethal cancers	170:192	the most lethal cancers	170:192	Pancreatic ductal adenocarcinoma (PDAC) is one of the most lethal cancers and its dismal prognosis indicates the urgent need to elucidate the potential oncogenic mechanisms.
35422493	8	18	dep	In	1123:1124	arg1	vivo					1126:1129	vivo	1126:1129	vivo	1126:1129	In vivo and in vitro experiments showed that blocking SIRT7 O-GlcNAcylation at S136 attenuates tumour progression.
35422493	4	19	theme	SIRT7	472:476	arg1	expression					478:487	SIRT7 expression	472:487	SIRT7 expression	472:487	Here, we found that SIRT7 expression is upregulated and predicts poor prognosis in PDAC.
35422493	5	20	theme	new	562:564	arg1	proteins					578:585	the new interacting proteins	558:585	the new interacting proteins of SIRT7	558:594	Then we screened the new interacting proteins of SIRT7 by mass spectrometry and the results showed that SIRT7 can interact with O-GlcNAc transferase (OGT).
35422493	2	21	theme	NAD+-dependent	313:326	arg1	deacetylase					328:338	a classic NAD+-dependent deacetylase	303:338	a classic NAD+-dependent deacetylase that stabilizes the transformed state of cancer cells	303:392	SIRT7 is a classic NAD+-dependent deacetylase that stabilizes the transformed state of cancer cells.
35422493	2	21	theme	NAD+-dependent	313:326	arg1	SIRT7					294:298	SIRT7	294:298	SIRT7	294:298	SIRT7 is a classic NAD+-dependent deacetylase that stabilizes the transformed state of cancer cells.
35422493	7	22	gly	O-GlcNAcylation	1001:1015	arg1	addition					985:992	addition	985:992	addition	985:992	In addition, SIRT7 O-GlcNAcylation at the serine 136 residue (S136) is required to maintain its protein stability and deacetylation ability.
35422493	1	23	theme	lethal	179:184	arg1	cancers					186:192	the most lethal cancers	170:192	the most lethal cancers	170:192	Pancreatic ductal adenocarcinoma (PDAC) is one of the most lethal cancers and its dismal prognosis indicates the urgent need to elucidate the potential oncogenic mechanisms.
35422493	8	24	theme	SIRT7	1177:1181	arg1	O-GlcNAcylation					1183:1197	SIRT7 O-GlcNAcylation	1177:1197	SIRT7 O-GlcNAcylation	1177:1197	In vivo and in vitro experiments showed that blocking SIRT7 O-GlcNAcylation at S136 attenuates tumour progression.
35422493	1	25	theme	oncogenic	272:280	arg1	mechanisms					282:291	the potential oncogenic mechanisms	258:291	the potential oncogenic mechanisms	258:291	Pancreatic ductal adenocarcinoma (PDAC) is one of the most lethal cancers and its dismal prognosis indicates the urgent need to elucidate the potential oncogenic mechanisms.
35422493	7	26	theme	protein	1078:1084	arg1	stability					1086:1094	protein stability	1078:1094	protein stability	1078:1094	In addition, SIRT7 O-GlcNAcylation at the serine 136 residue (S136) is required to maintain its protein stability and deacetylation ability.
35422493	5	27	theme	interacting	566:576	arg1	proteins					578:585	the new interacting proteins	558:585	the new interacting proteins of SIRT7	558:594	Then we screened the new interacting proteins of SIRT7 by mass spectrometry and the results showed that SIRT7 can interact with O-GlcNAc transferase (OGT).
35422493	2	28	theme	classic	305:311	arg1	deacetylase					328:338	a classic NAD+-dependent deacetylase	303:338	a classic NAD+-dependent deacetylase that stabilizes the transformed state of cancer cells	303:392	SIRT7 is a classic NAD+-dependent deacetylase that stabilizes the transformed state of cancer cells.
35422493	2	28	theme	classic	305:311	arg1	SIRT7					294:298	SIRT7	294:298	SIRT7	294:298	SIRT7 is a classic NAD+-dependent deacetylase that stabilizes the transformed state of cancer cells.
35422493	2	29	theme	cells	388:392	arg1	state					372:376	the transformed state	356:376	the transformed state of cancer cells	356:392	SIRT7 is a classic NAD+-dependent deacetylase that stabilizes the transformed state of cancer cells.
35422493	6	30	with	interaction	760:770	arg1	REGγ					777:780	REGγ	777:780	REGγ	777:780	O-GlcNAcylation stabilizes the SIRT7 protein by inhibiting its interaction with REGγ to prevent degradation, and hyper-O-GlcNAcylation in pancreatic cancer cells leads to hypoacetylation of H3K18 via SIRT7, which promotes transcriptional repression of several tumour suppressor genes.
35422493	6	31	theme	genes	975:979	arg1	repression					935:944	transcriptional repression	919:944	transcriptional repression of several tumour suppressor genes	919:979	O-GlcNAcylation stabilizes the SIRT7 protein by inhibiting its interaction with REGγ to prevent degradation, and hyper-O-GlcNAcylation in pancreatic cancer cells leads to hypoacetylation of H3K18 via SIRT7, which promotes transcriptional repression of several tumour suppressor genes.
35422493	1	32	theme	Pancreatic	120:129	arg1	PDAC					154:157	PDAC	154:157	PDAC	154:157	Pancreatic ductal adenocarcinoma (PDAC) is one of the most lethal cancers and its dismal prognosis indicates the urgent need to elucidate the potential oncogenic mechanisms.
35422493	1	32	theme	Pancreatic	120:129	arg1	adenocarcinoma					138:151	Pancreatic ductal adenocarcinoma	120:151	Pancreatic ductal adenocarcinoma (PDAC)	120:158	Pancreatic ductal adenocarcinoma (PDAC) is one of the most lethal cancers and its dismal prognosis indicates the urgent need to elucidate the potential oncogenic mechanisms.
35422493	8	33	theme	tumour	1218:1223	arg1	progression					1225:1235	tumour progression	1218:1235	tumour progression	1218:1235	In vivo and in vitro experiments showed that blocking SIRT7 O-GlcNAcylation at S136 attenuates tumour progression.
35422493	6	34	theme	suppressor	964:973	arg1	genes					975:979	several tumour suppressor genes	949:979	several tumour suppressor genes	949:979	O-GlcNAcylation stabilizes the SIRT7 protein by inhibiting its interaction with REGγ to prevent degradation, and hyper-O-GlcNAcylation in pancreatic cancer cells leads to hypoacetylation of H3K18 via SIRT7, which promotes transcriptional repression of several tumour suppressor genes.
35422493	9	35	dep	novel	1464:1468	arg1	therapeutic					1470:1480	therapeutic	1470:1480	therapeutic	1470:1480	Collectively, we demonstrate that O-GlcNAcylation is an important post-translational modification of SIRT7 in pancreatic cancer cells, and elucidating this mechanism of SIRT7 is expected to pave the way for the development of novel therapeutic methods in the future.
35422493	1	36	theme	cancers	186:192	arg1	cancers					186:192	the most lethal cancers	170:192	the most lethal cancers	170:192	Pancreatic ductal adenocarcinoma (PDAC) is one of the most lethal cancers and its dismal prognosis indicates the urgent need to elucidate the potential oncogenic mechanisms.
35422493	1	36	theme	cancers	186:192	arg1	one					163:165	one	163:165	one	163:165	Pancreatic ductal adenocarcinoma (PDAC) is one of the most lethal cancers and its dismal prognosis indicates the urgent need to elucidate the potential oncogenic mechanisms.
35422493	1	37	theme	dismal	202:207	arg1	prognosis					209:217	its dismal prognosis	198:217	its dismal prognosis	198:217	Pancreatic ductal adenocarcinoma (PDAC) is one of the most lethal cancers and its dismal prognosis indicates the urgent need to elucidate the potential oncogenic mechanisms.
35422493	0	38	theme	SIRT7	36:40	arg1	stablization					20:31	stablization	20:31	stablization	20:31	O-GlcNAcylation and stablization of SIRT7 promote pancreatic cancer progression by blocking the SIRT7-REGγ interaction.
35422493	0	38	theme	SIRT7	36:40	arg1	O-GlcNAcylation					0:14	O-GlcNAcylation	0:14	O-GlcNAcylation	0:14	O-GlcNAcylation and stablization of SIRT7 promote pancreatic cancer progression by blocking the SIRT7-REGγ interaction.
35422493	6	39	theme	tumour	957:962	arg1	genes					975:979	several tumour suppressor genes	949:979	several tumour suppressor genes	949:979	O-GlcNAcylation stabilizes the SIRT7 protein by inhibiting its interaction with REGγ to prevent degradation, and hyper-O-GlcNAcylation in pancreatic cancer cells leads to hypoacetylation of H3K18 via SIRT7, which promotes transcriptional repression of several tumour suppressor genes.
35422493	6	40	from	hyper-O-GlcNAcylation	810:830	arg1	cells					853:857	pancreatic cancer cells	835:857	pancreatic cancer cells	835:857	O-GlcNAcylation stabilizes the SIRT7 protein by inhibiting its interaction with REGγ to prevent degradation, and hyper-O-GlcNAcylation in pancreatic cancer cells leads to hypoacetylation of H3K18 via SIRT7, which promotes transcriptional repression of several tumour suppressor genes.
35422493	7	41	theme	serine	1024:1029	arg1	S136					1044:1047	S136	1044:1047	S136	1044:1047	In addition, SIRT7 O-GlcNAcylation at the serine 136 residue (S136) is required to maintain its protein stability and deacetylation ability.
35422493	7	41	theme	serine	1024:1029	arg1	residue					1035:1041	the serine 136 residue	1020:1041	the serine 136 residue (S136)	1020:1048	In addition, SIRT7 O-GlcNAcylation at the serine 136 residue (S136) is required to maintain its protein stability and deacetylation ability.
35422493	0	42	theme	cancer	61:66	arg1	progression					68:78	pancreatic cancer progression	50:78	pancreatic cancer progression	50:78	O-GlcNAcylation and stablization of SIRT7 promote pancreatic cancer progression by blocking the SIRT7-REGγ interaction.
35422493	4	43	theme	poor	517:520	arg1	prognosis					522:530	poor prognosis	517:530	poor prognosis in PDAC	517:538	Here, we found that SIRT7 expression is upregulated and predicts poor prognosis in PDAC.
35422493	7	44	theme	136	1031:1033	arg1	S136					1044:1047	S136	1044:1047	S136	1044:1047	In addition, SIRT7 O-GlcNAcylation at the serine 136 residue (S136) is required to maintain its protein stability and deacetylation ability.
35422493	7	44	theme	136	1031:1033	arg1	residue					1035:1041	the serine 136 residue	1020:1041	the serine 136 residue (S136)	1020:1048	In addition, SIRT7 O-GlcNAcylation at the serine 136 residue (S136) is required to maintain its protein stability and deacetylation ability.
35422493	1	45	theme	ductal	131:136	arg1	PDAC					154:157	PDAC	154:157	PDAC	154:157	Pancreatic ductal adenocarcinoma (PDAC) is one of the most lethal cancers and its dismal prognosis indicates the urgent need to elucidate the potential oncogenic mechanisms.
35422493	1	45	theme	ductal	131:136	arg1	adenocarcinoma					138:151	Pancreatic ductal adenocarcinoma	120:151	Pancreatic ductal adenocarcinoma (PDAC)	120:158	Pancreatic ductal adenocarcinoma (PDAC) is one of the most lethal cancers and its dismal prognosis indicates the urgent need to elucidate the potential oncogenic mechanisms.
35422493	3	46	theme	functional	408:417	arg1	roles					419:423	its functional roles	404:423	its functional roles in PDAC	404:431	However, its functional roles in PDAC are still unclear.
35422493	9	47	theme	important	1294:1302	arg1	modification					1323:1334	an important post-translational modification	1291:1334	an important post-translational modification of SIRT7 in pancreatic cancer cells	1291:1370	Collectively, we demonstrate that O-GlcNAcylation is an important post-translational modification of SIRT7 in pancreatic cancer cells, and elucidating this mechanism of SIRT7 is expected to pave the way for the development of novel therapeutic methods in the future.
35422493	9	47	theme	important	1294:1302	arg1	O-GlcNAcylation					1272:1286	O-GlcNAcylation	1272:1286	O-GlcNAcylation	1272:1286	Collectively, we demonstrate that O-GlcNAcylation is an important post-translational modification of SIRT7 in pancreatic cancer cells, and elucidating this mechanism of SIRT7 is expected to pave the way for the development of novel therapeutic methods in the future.
35422493	6	48	theme	cancer	846:851	arg1	cells					853:857	pancreatic cancer cells	835:857	pancreatic cancer cells	835:857	O-GlcNAcylation stabilizes the SIRT7 protein by inhibiting its interaction with REGγ to prevent degradation, and hyper-O-GlcNAcylation in pancreatic cancer cells leads to hypoacetylation of H3K18 via SIRT7, which promotes transcriptional repression of several tumour suppressor genes.
35422493	9	49	theme	SIRT7	1407:1411	arg1	mechanism					1394:1402	this mechanism	1389:1402	elucidating this mechanism of SIRT7	1377:1411	Collectively, we demonstrate that O-GlcNAcylation is an important post-translational modification of SIRT7 in pancreatic cancer cells, and elucidating this mechanism of SIRT7 is expected to pave the way for the development of novel therapeutic methods in the future.
35422493	5	50	theme	O-GlcNAc	669:676	arg1	OGT					691:693	OGT	691:693	OGT	691:693	Then we screened the new interacting proteins of SIRT7 by mass spectrometry and the results showed that SIRT7 can interact with O-GlcNAc transferase (OGT).
35422493	5	50	theme	O-GlcNAc	669:676	arg1	transferase					678:688	O-GlcNAc transferase	669:688	O-GlcNAc transferase (OGT)	669:694	Then we screened the new interacting proteins of SIRT7 by mass spectrometry and the results showed that SIRT7 can interact with O-GlcNAc transferase (OGT).
35422493	6	51	theme	pancreatic	835:844	arg1	cells					853:857	pancreatic cancer cells	835:857	pancreatic cancer cells	835:857	O-GlcNAcylation stabilizes the SIRT7 protein by inhibiting its interaction with REGγ to prevent degradation, and hyper-O-GlcNAcylation in pancreatic cancer cells leads to hypoacetylation of H3K18 via SIRT7, which promotes transcriptional repression of several tumour suppressor genes.
35422493	8	52	theme	In	1123:1124	arg1	experiments					1144:1154	In vivo and in vitro experiments	1123:1154	In vivo and in vitro experiments	1123:1154	In vivo and in vitro experiments showed that blocking SIRT7 O-GlcNAcylation at S136 attenuates tumour progression.
35422493	7	53	from	residue	1035:1041	arg1	O-GlcNAcylation					1001:1015	SIRT7 O-GlcNAcylation	995:1015	SIRT7 O-GlcNAcylation at the serine 136 residue (S136)	995:1048	In addition, SIRT7 O-GlcNAcylation at the serine 136 residue (S136) is required to maintain its protein stability and deacetylation ability.
35422493	6	54	theme	SIRT7	728:732	arg1	protein					734:740	the SIRT7 protein	724:740	the SIRT7 protein	724:740	O-GlcNAcylation stabilizes the SIRT7 protein by inhibiting its interaction with REGγ to prevent degradation, and hyper-O-GlcNAcylation in pancreatic cancer cells leads to hypoacetylation of H3K18 via SIRT7, which promotes transcriptional repression of several tumour suppressor genes.
35422493	9	55	theme	novel	1464:1468	arg1	methods					1482:1488	novel therapeutic methods	1464:1488	novel therapeutic methods	1464:1488	Collectively, we demonstrate that O-GlcNAcylation is an important post-translational modification of SIRT7 in pancreatic cancer cells, and elucidating this mechanism of SIRT7 is expected to pave the way for the development of novel therapeutic methods in the future.
35422493	9	56	theme	methods	1482:1488	arg1	development					1449:1459	the development	1445:1459	the development of novel therapeutic methods in the future	1445:1502	Collectively, we demonstrate that O-GlcNAcylation is an important post-translational modification of SIRT7 in pancreatic cancer cells, and elucidating this mechanism of SIRT7 is expected to pave the way for the development of novel therapeutic methods in the future.
35422493	2	57	theme	cancer	381:386	arg1	cells					388:392	cancer cells	381:392	cancer cells	381:392	SIRT7 is a classic NAD+-dependent deacetylase that stabilizes the transformed state of cancer cells.
35422493	9	58	theme	elucidating	1377:1387	arg1	mechanism					1394:1402	this mechanism	1389:1402	elucidating this mechanism of SIRT7	1377:1411	Collectively, we demonstrate that O-GlcNAcylation is an important post-translational modification of SIRT7 in pancreatic cancer cells, and elucidating this mechanism of SIRT7 is expected to pave the way for the development of novel therapeutic methods in the future.
35422493	1	59	theme	urgent	233:238	arg1	need					240:243	the urgent need	229:243	the urgent need to elucidate the potential oncogenic mechanisms	229:291	Pancreatic ductal adenocarcinoma (PDAC) is one of the most lethal cancers and its dismal prognosis indicates the urgent need to elucidate the potential oncogenic mechanisms.
35422493	4	60	from	prognosis	522:530	arg1	PDAC					535:538	PDAC	535:538	PDAC	535:538	Here, we found that SIRT7 expression is upregulated and predicts poor prognosis in PDAC.
35422493	6	61	theme	transcriptional	919:933	arg1	repression					935:944	transcriptional repression	919:944	transcriptional repression of several tumour suppressor genes	919:979	O-GlcNAcylation stabilizes the SIRT7 protein by inhibiting its interaction with REGγ to prevent degradation, and hyper-O-GlcNAcylation in pancreatic cancer cells leads to hypoacetylation of H3K18 via SIRT7, which promotes transcriptional repression of several tumour suppressor genes.
35422493	9	62	from	development	1449:1459	arg1	future					1497:1502	future	1497:1502	future	1497:1502	Collectively, we demonstrate that O-GlcNAcylation is an important post-translational modification of SIRT7 in pancreatic cancer cells, and elucidating this mechanism of SIRT7 is expected to pave the way for the development of novel therapeutic methods in the future.
35422493	6	63	theme	several	949:955	arg1	genes					975:979	several tumour suppressor genes	949:979	several tumour suppressor genes	949:979	O-GlcNAcylation stabilizes the SIRT7 protein by inhibiting its interaction with REGγ to prevent degradation, and hyper-O-GlcNAcylation in pancreatic cancer cells leads to hypoacetylation of H3K18 via SIRT7, which promotes transcriptional repression of several tumour suppressor genes.
35614056	5	0	theme	LARS1	705:709	arg1	interaction					690:700	the interaction	686:700	the interaction of LARS1 with RagD GTPase	686:726	This modification inhibits the interaction of LARS1 with RagD GTPase and reduces the affinity of LARS1 for leucine by promoting phosphorylation of its leucine-binding site by the autophagy-activating kinase ULK1, decreasing mTORC1 activity.
35614056	1	1	theme	living	152:157	arg1	organisms					159:167	All living organisms	148:167	All living organisms	148:167	All living organisms have the ability to sense nutrient levels to coordinate cellular metabolism.
35614056	6	2	theme	LARS1	912:916	arg1	O-GlcNAcylation					918:932	LARS1 O-GlcNAcylation	912:932	LARS1 O-GlcNAcylation	912:932	The lack of LARS1 O-GlcNAcylation constitutively activates mTORC1, supporting its ability to sense leucine, and deregulates protein synthesis and leucine catabolism under glucose starvation.
35614056	5	3	theme	RagD	716:719	arg1	GTPase					721:726	RagD GTPase	716:726	RagD GTPase	716:726	This modification inhibits the interaction of LARS1 with RagD GTPase and reduces the affinity of LARS1 for leucine by promoting phosphorylation of its leucine-binding site by the autophagy-activating kinase ULK1, decreasing mTORC1 activity.
35614056	3	4	theme	effector	499:506	arg1	mTORC1					508:513	the central nutrient effector mTORC1	478:513	the central nutrient effector mTORC1	478:513	Here, we show that glucose availability regulates the central nutrient effector mTORC1 through intracellular leucine sensor leucyl-tRNA synthetase 1 (LARS1).
35614056	6	5	theme	protein	1024:1030	arg1	synthesis					1032:1040	protein synthesis	1024:1040	protein synthesis	1024:1040	The lack of LARS1 O-GlcNAcylation constitutively activates mTORC1, supporting its ability to sense leucine, and deregulates protein synthesis and leucine catabolism under glucose starvation.
35614056	6	6	theme	O-GlcNAcylation	918:932	arg1	lack					904:907	The lack	900:907	The lack of LARS1 O-GlcNAcylation	900:932	The lack of LARS1 O-GlcNAcylation constitutively activates mTORC1, supporting its ability to sense leucine, and deregulates protein synthesis and leucine catabolism under glucose starvation.
35614056	3	7	theme	sensor	545:550	arg1	synthetase					564:573	intracellular leucine sensor leucyl-tRNA synthetase 1	523:575	intracellular leucine sensor leucyl-tRNA synthetase 1 (LARS1)	523:583	Here, we show that glucose availability regulates the central nutrient effector mTORC1 through intracellular leucine sensor leucyl-tRNA synthetase 1 (LARS1).
35614056	3	7	theme	sensor	545:550	arg1	LARS1					578:582	LARS1	578:582	LARS1	578:582	Here, we show that glucose availability regulates the central nutrient effector mTORC1 through intracellular leucine sensor leucyl-tRNA synthetase 1 (LARS1).
35614056	4	8	theme	LARS1	635:639	arg1	O-GlcNAcylation					616:630	O-GlcNAcylation	616:630	O-GlcNAcylation of LARS1 on residue S1042	616:656	Glucose starvation results in O-GlcNAcylation of LARS1 on residue S1042.
35614056	7	9	theme	metabolic	1196:1204	arg1	fate					1206:1209	the metabolic fate	1192:1209	the metabolic fate of leucine	1192:1220	This work demonstrates that LARS1 integrates leucine and glucose availability to regulate mTORC1 and the metabolic fate of leucine.
35614056	3	10	theme	leucyl-tRNA	552:562	arg1	synthetase					564:573	intracellular leucine sensor leucyl-tRNA synthetase 1	523:575	intracellular leucine sensor leucyl-tRNA synthetase 1 (LARS1)	523:583	Here, we show that glucose availability regulates the central nutrient effector mTORC1 through intracellular leucine sensor leucyl-tRNA synthetase 1 (LARS1).
35614056	3	10	theme	leucyl-tRNA	552:562	arg1	LARS1					578:582	LARS1	578:582	LARS1	578:582	Here, we show that glucose availability regulates the central nutrient effector mTORC1 through intracellular leucine sensor leucyl-tRNA synthetase 1 (LARS1).
35614056	4	11	theme	Glucose	586:592	arg1	starvation					594:603	Glucose starvation	586:603	Glucose starvation	586:603	Glucose starvation results in O-GlcNAcylation of LARS1 on residue S1042.
35614056	5	12	theme	kinase	859:864	arg1	ULK1					866:869	the autophagy-activating kinase ULK1	834:869	the autophagy-activating kinase ULK1	834:869	This modification inhibits the interaction of LARS1 with RagD GTPase and reduces the affinity of LARS1 for leucine by promoting phosphorylation of its leucine-binding site by the autophagy-activating kinase ULK1, decreasing mTORC1 activity.
35614056	3	13	theme	glucose	447:453	arg1	availability					455:466	glucose availability	447:466	glucose availability	447:466	Here, we show that glucose availability regulates the central nutrient effector mTORC1 through intracellular leucine sensor leucyl-tRNA synthetase 1 (LARS1).
35614056	2	14	theme	pathways	289:296	arg1	importance					258:267	the importance	254:267	the importance of nutrient-sensing pathways that detect the levels of amino acids and glucose	254:346	Despite the importance of nutrient-sensing pathways that detect the levels of amino acids and glucose, how the availability of these two types of nutrients is integrated is unclear.
35614056	7	15	theme	glucose	1148:1154	arg1	availability					1156:1167	glucose availability	1148:1167	glucose availability	1148:1167	This work demonstrates that LARS1 integrates leucine and glucose availability to regulate mTORC1 and the metabolic fate of leucine.
35614056	2	16	theme	nutrient-sensing	272:287	arg1	pathways					289:296	nutrient-sensing pathways	272:296	nutrient-sensing pathways that detect the levels of amino acids and glucose	272:346	Despite the importance of nutrient-sensing pathways that detect the levels of amino acids and glucose, how the availability of these two types of nutrients is integrated is unclear.
35614056	2	17	theme	types	383:387	arg1	availability					357:368	the availability	353:368	the availability of these two types of nutrients	353:400	Despite the importance of nutrient-sensing pathways that detect the levels of amino acids and glucose, how the availability of these two types of nutrients is integrated is unclear.
35614056	5	18	theme	leucine-binding	810:824	arg1	site					826:829	its leucine-binding site	806:829	its leucine-binding site	806:829	This modification inhibits the interaction of LARS1 with RagD GTPase and reduces the affinity of LARS1 for leucine by promoting phosphorylation of its leucine-binding site by the autophagy-activating kinase ULK1, decreasing mTORC1 activity.
35614056	5	19	theme	LARS1	756:760	arg1	affinity					744:751	the affinity	740:751	the affinity of LARS1 for leucine	740:772	This modification inhibits the interaction of LARS1 with RagD GTPase and reduces the affinity of LARS1 for leucine by promoting phosphorylation of its leucine-binding site by the autophagy-activating kinase ULK1, decreasing mTORC1 activity.
35614056	2	20	theme	amino	324:328	arg1	acids					330:334	amino acids	324:334	amino acids	324:334	Despite the importance of nutrient-sensing pathways that detect the levels of amino acids and glucose, how the availability of these two types of nutrients is integrated is unclear.
35614056	3	21	theme	intracellular	523:535	arg1	synthetase					564:573	intracellular leucine sensor leucyl-tRNA synthetase 1	523:575	intracellular leucine sensor leucyl-tRNA synthetase 1 (LARS1)	523:583	Here, we show that glucose availability regulates the central nutrient effector mTORC1 through intracellular leucine sensor leucyl-tRNA synthetase 1 (LARS1).
35614056	3	21	theme	intracellular	523:535	arg1	LARS1					578:582	LARS1	578:582	LARS1	578:582	Here, we show that glucose availability regulates the central nutrient effector mTORC1 through intracellular leucine sensor leucyl-tRNA synthetase 1 (LARS1).
35614056	0	22	theme	O-GlcNAc	0:7	arg1	modification					9:20	O-GlcNAc modification	0:20	O-GlcNAc modification of leucyl-tRNA synthetase 1	0:48	O-GlcNAc modification of leucyl-tRNA synthetase 1 integrates leucine and glucose availability to regulate mTORC1 and the metabolic fate of leucine.
35614056	5	23	with	interaction	690:700	arg1	GTPase					721:726	RagD GTPase	716:726	RagD GTPase	716:726	This modification inhibits the interaction of LARS1 with RagD GTPase and reduces the affinity of LARS1 for leucine by promoting phosphorylation of its leucine-binding site by the autophagy-activating kinase ULK1, decreasing mTORC1 activity.
35614056	0	24	theme	leucyl-tRNA	25:35	arg1	synthetase					37:46	leucyl-tRNA synthetase 1	25:48	leucyl-tRNA synthetase 1	25:48	O-GlcNAc modification of leucyl-tRNA synthetase 1 integrates leucine and glucose availability to regulate mTORC1 and the metabolic fate of leucine.
35614056	5	25	theme	site	826:829	arg1	phosphorylation					787:801	phosphorylation	787:801	phosphorylation of its leucine-binding site	787:829	This modification inhibits the interaction of LARS1 with RagD GTPase and reduces the affinity of LARS1 for leucine by promoting phosphorylation of its leucine-binding site by the autophagy-activating kinase ULK1, decreasing mTORC1 activity.
35614056	1	26	theme	sense	189:193	arg1	levels					204:209	sense nutrient levels	189:209	sense nutrient levels	189:209	All living organisms have the ability to sense nutrient levels to coordinate cellular metabolism.
35614056	7	27	theme	leucine	1214:1220	arg1	fate					1206:1209	the metabolic fate	1192:1209	the metabolic fate of leucine	1192:1220	This work demonstrates that LARS1 integrates leucine and glucose availability to regulate mTORC1 and the metabolic fate of leucine.
35614056	7	27	theme	leucine	1214:1220	arg1	mTORC1					1181:1186	mTORC1	1181:1186	mTORC1	1181:1186	This work demonstrates that LARS1 integrates leucine and glucose availability to regulate mTORC1 and the metabolic fate of leucine.
35614056	6	28	theme	sense	993:997	arg1	leucine					999:1005	sense leucine	993:1005	sense leucine	993:1005	The lack of LARS1 O-GlcNAcylation constitutively activates mTORC1, supporting its ability to sense leucine, and deregulates protein synthesis and leucine catabolism under glucose starvation.
35614056	0	29	theme	metabolic	121:129	arg1	fate					131:134	the metabolic fate	117:134	the metabolic fate of leucine	117:145	O-GlcNAc modification of leucyl-tRNA synthetase 1 integrates leucine and glucose availability to regulate mTORC1 and the metabolic fate of leucine.
35614056	1	30	theme	nutrient	195:202	arg1	levels					204:209	sense nutrient levels	189:209	sense nutrient levels	189:209	All living organisms have the ability to sense nutrient levels to coordinate cellular metabolism.
35614056	3	31	theme	nutrient	490:497	arg1	mTORC1					508:513	the central nutrient effector mTORC1	478:513	the central nutrient effector mTORC1	478:513	Here, we show that glucose availability regulates the central nutrient effector mTORC1 through intracellular leucine sensor leucyl-tRNA synthetase 1 (LARS1).
35614056	3	32	theme	central	482:488	arg1	mTORC1					508:513	the central nutrient effector mTORC1	478:513	the central nutrient effector mTORC1	478:513	Here, we show that glucose availability regulates the central nutrient effector mTORC1 through intracellular leucine sensor leucyl-tRNA synthetase 1 (LARS1).
35614056	0	33	theme	leucine	139:145	arg1	mTORC1					106:111	mTORC1	106:111	mTORC1	106:111	O-GlcNAc modification of leucyl-tRNA synthetase 1 integrates leucine and glucose availability to regulate mTORC1 and the metabolic fate of leucine.
35614056	0	33	theme	leucine	139:145	arg1	fate					131:134	the metabolic fate	117:134	the metabolic fate of leucine	117:145	O-GlcNAc modification of leucyl-tRNA synthetase 1 integrates leucine and glucose availability to regulate mTORC1 and the metabolic fate of leucine.
35614056	0	34	theme	synthetase	37:46	arg1	modification					9:20	O-GlcNAc modification	0:20	O-GlcNAc modification of leucyl-tRNA synthetase 1	0:48	O-GlcNAc modification of leucyl-tRNA synthetase 1 integrates leucine and glucose availability to regulate mTORC1 and the metabolic fate of leucine.
35614056	2	35	theme	nutrients	392:400	arg1	types					383:387	these two types	373:387	these two types of nutrients	373:400	Despite the importance of nutrient-sensing pathways that detect the levels of amino acids and glucose, how the availability of these two types of nutrients is integrated is unclear.
35614056	1	36	contain	have	169:172	arg2	ability					178:184	the ability	174:184	the ability to sense nutrient levels to coordinate cellular metabolism	174:243	All living organisms have the ability to sense nutrient levels to coordinate cellular metabolism.
35614056	1	36	contain	have	169:172	arg1	organisms					159:167	All living organisms	148:167	All living organisms	148:167	All living organisms have the ability to sense nutrient levels to coordinate cellular metabolism.
35614056	2	37	theme	glucose	340:346	arg1	levels					314:319	the levels	310:319	the levels of amino acids and glucose	310:346	Despite the importance of nutrient-sensing pathways that detect the levels of amino acids and glucose, how the availability of these two types of nutrients is integrated is unclear.
35614056	3	38	theme	leucine	537:543	arg1	synthetase					564:573	intracellular leucine sensor leucyl-tRNA synthetase 1	523:575	intracellular leucine sensor leucyl-tRNA synthetase 1 (LARS1)	523:583	Here, we show that glucose availability regulates the central nutrient effector mTORC1 through intracellular leucine sensor leucyl-tRNA synthetase 1 (LARS1).
35614056	3	38	theme	leucine	537:543	arg1	LARS1					578:582	LARS1	578:582	LARS1	578:582	Here, we show that glucose availability regulates the central nutrient effector mTORC1 through intracellular leucine sensor leucyl-tRNA synthetase 1 (LARS1).
35614056	2	39	theme	acids	330:334	arg1	levels					314:319	the levels	310:319	the levels of amino acids and glucose	310:346	Despite the importance of nutrient-sensing pathways that detect the levels of amino acids and glucose, how the availability of these two types of nutrients is integrated is unclear.
35614056	1	40	theme	cellular	225:232	arg1	metabolism					234:243	cellular metabolism	225:243	cellular metabolism	225:243	All living organisms have the ability to sense nutrient levels to coordinate cellular metabolism.
35614056	0	41	theme	glucose	73:79	arg1	availability					81:92	glucose availability	73:92	glucose availability	73:92	O-GlcNAc modification of leucyl-tRNA synthetase 1 integrates leucine and glucose availability to regulate mTORC1 and the metabolic fate of leucine.
35614056	6	42	theme	glucose	1071:1077	arg1	starvation					1079:1088	glucose starvation	1071:1088	glucose starvation	1071:1088	The lack of LARS1 O-GlcNAcylation constitutively activates mTORC1, supporting its ability to sense leucine, and deregulates protein synthesis and leucine catabolism under glucose starvation.
35614056	5	43	theme	autophagy-activating	838:857	arg1	ULK1					866:869	the autophagy-activating kinase ULK1	834:869	the autophagy-activating kinase ULK1	834:869	This modification inhibits the interaction of LARS1 with RagD GTPase and reduces the affinity of LARS1 for leucine by promoting phosphorylation of its leucine-binding site by the autophagy-activating kinase ULK1, decreasing mTORC1 activity.
35614056	5	44	theme	mTORC1	883:888	arg1	activity					890:897	mTORC1 activity	883:897	mTORC1 activity	883:897	This modification inhibits the interaction of LARS1 with RagD GTPase and reduces the affinity of LARS1 for leucine by promoting phosphorylation of its leucine-binding site by the autophagy-activating kinase ULK1, decreasing mTORC1 activity.
35614056	6	45	theme	leucine	1046:1052	arg1	catabolism					1054:1063	leucine catabolism	1046:1063	leucine catabolism	1046:1063	The lack of LARS1 O-GlcNAcylation constitutively activates mTORC1, supporting its ability to sense leucine, and deregulates protein synthesis and leucine catabolism under glucose starvation.
35614056	4	46	from	O-GlcNAcylation	616:630	arg1	residue					644:650	residue S1042	644:656	residue S1042	644:656	Glucose starvation results in O-GlcNAcylation of LARS1 on residue S1042.
12754519	0	0	theme	isotope	94:100	arg1	labeling					102:109	stable isotope labeling	87:109	stable isotope labeling	87:109	Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry.
12754519	2	1	theme	technical	523:531	arg1	challenge					533:541	an as-yet-unresolved technical challenge	502:541	an as-yet-unresolved technical challenge	502:541	Owing to the enormous complexity of proteomes, their comprehensive analysis is an as-yet-unresolved technical challenge.
12754519	2	1	theme	technical	523:531	arg1	analysis					490:497	their comprehensive analysis	470:497	their comprehensive analysis	470:497	Owing to the enormous complexity of proteomes, their comprehensive analysis is an as-yet-unresolved technical challenge.
12754519	6	2	gly	glycosylated	1095:1106	arg1	peptides					1108:1115	formerly N-linked glycosylated peptides	1077:1115	formerly N-linked glycosylated peptides	1077:1115	It is based on the conjugation of glycoproteins to a solid support using hydrazide chemistry, stable isotope labeling of glycopeptides and the specific release of formerly N-linked glycosylated peptides via peptide- N-glycosidase F (PNGase F).
12754519	1	3	theme	isotope	179:185	arg1	tagging					195:201	stable isotope protein tagging	172:201	stable isotope protein tagging	172:201	Quantitative proteome profiling using stable isotope protein tagging and automated tandem mass spectrometry (MS/MS) is an emerging technology with great potential for the functional analysis of biological systems and for the detection of clinical diagnostic or prognostic marker proteins.
12754519	6	4	theme	solid	967:971	arg1	support					973:979	a solid support	965:979	a solid support using hydrazide chemistry, stable isotope labeling of glycopeptides and the specific release of formerly N-linked glycosylated peptides via peptide- N-glycosidase F (PNGase F)	965:1155	It is based on the conjugation of glycoproteins to a solid support using hydrazide chemistry, stable isotope labeling of glycopeptides and the specific release of formerly N-linked glycosylated peptides via peptide- N-glycosidase F (PNGase F).
12754519	0	5	theme	stable	87:92	arg1	labeling					102:109	stable isotope labeling	87:109	stable isotope labeling	87:109	Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry.
12754519	1	6	theme	protein	187:193	arg1	tagging					195:201	stable isotope protein tagging	172:201	stable isotope protein tagging	172:201	Quantitative proteome profiling using stable isotope protein tagging and automated tandem mass spectrometry (MS/MS) is an emerging technology with great potential for the functional analysis of biological systems and for the detection of clinical diagnostic or prognostic marker proteins.
12754519	1	7	theme	great	281:285	arg1	potential					287:295	great potential	281:295	great potential	281:295	Quantitative proteome profiling using stable isotope protein tagging and automated tandem mass spectrometry (MS/MS) is an emerging technology with great potential for the functional analysis of biological systems and for the detection of clinical diagnostic or prognostic marker proteins.
12754519	1	8	theme	clinical	372:379	arg1	proteins					413:420	clinical diagnostic or prognostic marker proteins	372:420	clinical diagnostic or prognostic marker proteins	372:420	Quantitative proteome profiling using stable isotope protein tagging and automated tandem mass spectrometry (MS/MS) is an emerging technology with great potential for the functional analysis of biological systems and for the detection of clinical diagnostic or prognostic marker proteins.
12754519	6	9	link	N-linked	1086:1093	arg1	peptides					1108:1115	formerly N-linked glycosylated peptides	1077:1115	formerly N-linked glycosylated peptides	1077:1115	It is based on the conjugation of glycoproteins to a solid support using hydrazide chemistry, stable isotope labeling of glycopeptides and the specific release of formerly N-linked glycosylated peptides via peptide- N-glycosidase F (PNGase F).
12754519	6	10	theme	specific	1057:1064	arg1	release					1066:1072	the specific release	1053:1072	the specific release of formerly N-linked glycosylated peptides via peptide- N-glycosidase F (PNGase F)	1053:1155	It is based on the conjugation of glycoproteins to a solid support using hydrazide chemistry, stable isotope labeling of glycopeptides and the specific release of formerly N-linked glycosylated peptides via peptide- N-glycosidase F (PNGase F).
12754519	4	11	theme	post-translational	743:760	arg1	Glycosylation					710:722	Glycosylation	710:722	Glycosylation	710:722	Glycosylation is the most common post-translational modification.
12754519	4	11	theme	post-translational	743:760	arg1	modification					762:773	the most common post-translational modification	727:773	the most common post-translational modification	727:773	Glycosylation is the most common post-translational modification.
12754519	1	12	theme	diagnostic	381:390	arg1	proteins					413:420	clinical diagnostic or prognostic marker proteins	372:420	clinical diagnostic or prognostic marker proteins	372:420	Quantitative proteome profiling using stable isotope protein tagging and automated tandem mass spectrometry (MS/MS) is an emerging technology with great potential for the functional analysis of biological systems and for the detection of clinical diagnostic or prognostic marker proteins.
12754519	8	13	theme	blood	1326:1330	arg1	serum					1332:1336	human blood serum	1320:1336	human blood serum	1320:1336	We applied the approach to the analysis of plasma membrane proteins and proteins contained in human blood serum.
12754519	0	14	theme	mass	115:118	arg1	spectrometry					120:131	mass spectrometry	115:131	mass spectrometry	115:131	Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry.
12754519	2	15	theme	as-yet-unresolved	505:521	arg1	challenge					533:541	an as-yet-unresolved technical challenge	502:541	an as-yet-unresolved technical challenge	502:541	Owing to the enormous complexity of proteomes, their comprehensive analysis is an as-yet-unresolved technical challenge.
12754519	2	15	theme	as-yet-unresolved	505:521	arg1	analysis					490:497	their comprehensive analysis	470:497	their comprehensive analysis	470:497	Owing to the enormous complexity of proteomes, their comprehensive analysis is an as-yet-unresolved technical challenge.
12754519	8	16	theme	proteins	1285:1292	arg1	analysis					1257:1264	the analysis	1253:1264	the analysis of plasma membrane proteins and proteins contained in human blood serum	1253:1336	We applied the approach to the analysis of plasma membrane proteins and proteins contained in human blood serum.
12754519	3	17	theme	important	580:588	arg1	information					590:600	biologically or clinically important information	553:600	biologically or clinically important information	553:600	However, biologically or clinically important information can be obtained if specific, information-rich protein classes, or sub-proteomes, are isolated and analyzed.
12754519	6	18	theme	stable	1008:1013	arg1	labeling					1023:1030	stable isotope labeling	1008:1030	stable isotope labeling of glycopeptides	1008:1047	It is based on the conjugation of glycoproteins to a solid support using hydrazide chemistry, stable isotope labeling of glycopeptides and the specific release of formerly N-linked glycosylated peptides via peptide- N-glycosidase F (PNGase F).
12754519	1	19	theme	prognostic	395:404	arg1	proteins					413:420	clinical diagnostic or prognostic marker proteins	372:420	clinical diagnostic or prognostic marker proteins	372:420	Quantitative proteome profiling using stable isotope protein tagging and automated tandem mass spectrometry (MS/MS) is an emerging technology with great potential for the functional analysis of biological systems and for the detection of clinical diagnostic or prognostic marker proteins.
12754519	8	20	theme	human	1320:1324	arg1	serum					1332:1336	human blood serum	1320:1336	human blood serum	1320:1336	We applied the approach to the analysis of plasma membrane proteins and proteins contained in human blood serum.
12754519	1	21	theme	automated	207:215	arg1	spectrometry					229:240	automated tandem mass spectrometry	207:240	automated tandem mass spectrometry (MS/MS)	207:248	Quantitative proteome profiling using stable isotope protein tagging and automated tandem mass spectrometry (MS/MS) is an emerging technology with great potential for the functional analysis of biological systems and for the detection of clinical diagnostic or prognostic marker proteins.
12754519	1	21	theme	automated	207:215	arg1	MS/MS					243:247	MS/MS	243:247	MS/MS	243:247	Quantitative proteome profiling using stable isotope protein tagging and automated tandem mass spectrometry (MS/MS) is an emerging technology with great potential for the functional analysis of biological systems and for the detection of clinical diagnostic or prognostic marker proteins.
12754519	7	22	theme	recovered	1162:1170	arg1	peptides					1172:1179	The recovered peptides	1158:1179	The recovered peptides	1158:1179	The recovered peptides are then identified and quantified by MS/MS.
12754519	3	23	theme	specific	621:628	arg1	classes					656:662	specific, information-rich protein classes	621:662	specific, information-rich protein classes	621:662	However, biologically or clinically important information can be obtained if specific, information-rich protein classes, or sub-proteomes, are isolated and analyzed.
12754519	1	24	theme	tandem	217:222	arg1	spectrometry					229:240	automated tandem mass spectrometry	207:240	automated tandem mass spectrometry (MS/MS)	207:248	Quantitative proteome profiling using stable isotope protein tagging and automated tandem mass spectrometry (MS/MS) is an emerging technology with great potential for the functional analysis of biological systems and for the detection of clinical diagnostic or prognostic marker proteins.
12754519	1	24	theme	tandem	217:222	arg1	MS/MS					243:247	MS/MS	243:247	MS/MS	243:247	Quantitative proteome profiling using stable isotope protein tagging and automated tandem mass spectrometry (MS/MS) is an emerging technology with great potential for the functional analysis of biological systems and for the detection of clinical diagnostic or prognostic marker proteins.
12754519	2	25	theme	proteomes	459:467	arg1	complexity					445:454	the enormous complexity	432:454	the enormous complexity of proteomes	432:467	Owing to the enormous complexity of proteomes, their comprehensive analysis is an as-yet-unresolved technical challenge.
12754519	6	26	theme	glycopeptides	1035:1047	arg1	labeling					1023:1030	stable isotope labeling	1008:1030	stable isotope labeling of glycopeptides	1008:1047	It is based on the conjugation of glycoproteins to a solid support using hydrazide chemistry, stable isotope labeling of glycopeptides and the specific release of formerly N-linked glycosylated peptides via peptide- N-glycosidase F (PNGase F).
12754519	6	26	theme	glycopeptides	1035:1047	arg1	release					1066:1072	the specific release	1053:1072	the specific release of formerly N-linked glycosylated peptides via peptide- N-glycosidase F (PNGase F)	1053:1155	It is based on the conjugation of glycoproteins to a solid support using hydrazide chemistry, stable isotope labeling of glycopeptides and the specific release of formerly N-linked glycosylated peptides via peptide- N-glycosidase F (PNGase F).
12754519	6	26	theme	glycopeptides	1035:1047	arg1	chemistry					997:1005	hydrazide chemistry	987:1005	hydrazide chemistry	987:1005	It is based on the conjugation of glycoproteins to a solid support using hydrazide chemistry, stable isotope labeling of glycopeptides and the specific release of formerly N-linked glycosylated peptides via peptide- N-glycosidase F (PNGase F).
12754519	0	27	link	N-linked	37:44	arg1	glycoproteins					46:58	N-linked glycoproteins	37:58	N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry	37:131	Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry.
12754519	8	28	theme	plasma	1269:1274	arg1	proteins					1285:1292	plasma membrane proteins	1269:1292	plasma membrane proteins	1269:1292	We applied the approach to the analysis of plasma membrane proteins and proteins contained in human blood serum.
12754519	1	29	theme	mass	224:227	arg1	spectrometry					229:240	automated tandem mass spectrometry	207:240	automated tandem mass spectrometry (MS/MS)	207:248	Quantitative proteome profiling using stable isotope protein tagging and automated tandem mass spectrometry (MS/MS) is an emerging technology with great potential for the functional analysis of biological systems and for the detection of clinical diagnostic or prognostic marker proteins.
12754519	1	29	theme	mass	224:227	arg1	MS/MS					243:247	MS/MS	243:247	MS/MS	243:247	Quantitative proteome profiling using stable isotope protein tagging and automated tandem mass spectrometry (MS/MS) is an emerging technology with great potential for the functional analysis of biological systems and for the detection of clinical diagnostic or prognostic marker proteins.
12754519	1	30	theme	functional	305:314	arg1	analysis					316:323	the functional analysis	301:323	the functional analysis of biological systems	301:345	Quantitative proteome profiling using stable isotope protein tagging and automated tandem mass spectrometry (MS/MS) is an emerging technology with great potential for the functional analysis of biological systems and for the detection of clinical diagnostic or prognostic marker proteins.
12754519	1	31	theme	marker	406:411	arg1	proteins					413:420	clinical diagnostic or prognostic marker proteins	372:420	clinical diagnostic or prognostic marker proteins	372:420	Quantitative proteome profiling using stable isotope protein tagging and automated tandem mass spectrometry (MS/MS) is an emerging technology with great potential for the functional analysis of biological systems and for the detection of clinical diagnostic or prognostic marker proteins.
12754519	3	32	dep	specific	621:628	arg1	information-rich					631:646	information-rich	631:646	information-rich	631:646	However, biologically or clinically important information can be obtained if specific, information-rich protein classes, or sub-proteomes, are isolated and analyzed.
12754519	6	33	theme	hydrazide	987:995	arg1	chemistry					997:1005	hydrazide chemistry	987:1005	hydrazide chemistry	987:1005	It is based on the conjugation of glycoproteins to a solid support using hydrazide chemistry, stable isotope labeling of glycopeptides and the specific release of formerly N-linked glycosylated peptides via peptide- N-glycosidase F (PNGase F).
12754519	2	34	theme	enormous	436:443	arg1	complexity					445:454	the enormous complexity	432:454	the enormous complexity of proteomes	432:467	Owing to the enormous complexity of proteomes, their comprehensive analysis is an as-yet-unresolved technical challenge.
12754519	0	35	theme	glycoproteins	46:58	arg1	quantification					19:32	quantification	19:32	quantification	19:32	Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry.
12754519	0	35	theme	glycoproteins	46:58	arg1	Identification					0:13	Identification	0:13	Identification	0:13	Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry.
12754519	1	36	theme	proteins	413:420	arg1	detection					359:367	the detection	355:367	the detection of clinical diagnostic or prognostic marker proteins	355:420	Quantitative proteome profiling using stable isotope protein tagging and automated tandem mass spectrometry (MS/MS) is an emerging technology with great potential for the functional analysis of biological systems and for the detection of clinical diagnostic or prognostic marker proteins.
12754519	3	37	theme	protein	648:654	arg1	classes					656:662	specific, information-rich protein classes	621:662	specific, information-rich protein classes	621:662	However, biologically or clinically important information can be obtained if specific, information-rich protein classes, or sub-proteomes, are isolated and analyzed.
12754519	6	38	theme	PNGase	1147:1152	arg1	F					1144:1144	peptide- N-glycosidase F	1121:1144	peptide- N-glycosidase F (PNGase F)	1121:1155	It is based on the conjugation of glycoproteins to a solid support using hydrazide chemistry, stable isotope labeling of glycopeptides and the specific release of formerly N-linked glycosylated peptides via peptide- N-glycosidase F (PNGase F).
12754519	6	38	theme	PNGase	1147:1152	arg1	F					1154:1154	PNGase F	1147:1154	PNGase F	1147:1154	It is based on the conjugation of glycoproteins to a solid support using hydrazide chemistry, stable isotope labeling of glycopeptides and the specific release of formerly N-linked glycosylated peptides via peptide- N-glycosidase F (PNGase F).
12754519	6	39	theme	N-glycosidase	1130:1142	arg1	F					1144:1144	peptide- N-glycosidase F	1121:1144	peptide- N-glycosidase F (PNGase F)	1121:1155	It is based on the conjugation of glycoproteins to a solid support using hydrazide chemistry, stable isotope labeling of glycopeptides and the specific release of formerly N-linked glycosylated peptides via peptide- N-glycosidase F (PNGase F).
12754519	6	39	theme	N-glycosidase	1130:1142	arg1	F					1154:1154	PNGase F	1147:1154	PNGase F	1147:1154	It is based on the conjugation of glycoproteins to a solid support using hydrazide chemistry, stable isotope labeling of glycopeptides and the specific release of formerly N-linked glycosylated peptides via peptide- N-glycosidase F (PNGase F).
12754519	0	40	theme	N-linked	37:44	arg1	glycoproteins					46:58	N-linked glycoproteins	37:58	N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry	37:131	Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry.
12754519	8	41	theme	membrane	1276:1283	arg1	proteins					1285:1292	plasma membrane proteins	1269:1292	plasma membrane proteins	1269:1292	We applied the approach to the analysis of plasma membrane proteins and proteins contained in human blood serum.
12754519	5	42	contain	contain	882:888	arg2	carbohydrates					899:911	N-linked carbohydrates	890:911	N-linked carbohydrates	890:911	Here we describe a method for the selective isolation, identification and quantification of peptides that contain N-linked carbohydrates.
12754519	5	42	contain	contain	882:888	arg1	peptides					868:875	peptides	868:875	peptides that contain N-linked carbohydrates	868:911	Here we describe a method for the selective isolation, identification and quantification of peptides that contain N-linked carbohydrates.
12754519	5	43	theme	N-linked	890:897	arg1	carbohydrates					899:911	N-linked carbohydrates	890:911	N-linked carbohydrates	890:911	Here we describe a method for the selective isolation, identification and quantification of peptides that contain N-linked carbohydrates.
12754519	6	44	theme	peptide-	1121:1128	arg1	F					1144:1144	peptide- N-glycosidase F	1121:1144	peptide- N-glycosidase F (PNGase F)	1121:1155	It is based on the conjugation of glycoproteins to a solid support using hydrazide chemistry, stable isotope labeling of glycopeptides and the specific release of formerly N-linked glycosylated peptides via peptide- N-glycosidase F (PNGase F).
12754519	6	44	theme	peptide-	1121:1128	arg1	F					1154:1154	PNGase F	1147:1154	PNGase F	1147:1154	It is based on the conjugation of glycoproteins to a solid support using hydrazide chemistry, stable isotope labeling of glycopeptides and the specific release of formerly N-linked glycosylated peptides via peptide- N-glycosidase F (PNGase F).
12754519	0	45	theme	hydrazide	66:74	arg1	chemistry					76:84	hydrazide chemistry	66:84	hydrazide chemistry	66:84	Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry.
12754519	1	46	theme	biological	328:337	arg1	systems					339:345	biological systems	328:345	biological systems	328:345	Quantitative proteome profiling using stable isotope protein tagging and automated tandem mass spectrometry (MS/MS) is an emerging technology with great potential for the functional analysis of biological systems and for the detection of clinical diagnostic or prognostic marker proteins.
12754519	5	47	theme	peptides	868:875	arg1	isolation					820:828	the selective isolation	806:828	the selective isolation	806:828	Here we describe a method for the selective isolation, identification and quantification of peptides that contain N-linked carbohydrates.
12754519	5	47	theme	peptides	868:875	arg1	quantification					850:863	quantification	850:863	quantification	850:863	Here we describe a method for the selective isolation, identification and quantification of peptides that contain N-linked carbohydrates.
12754519	5	47	theme	peptides	868:875	arg1	identification					831:844	identification	831:844	identification	831:844	Here we describe a method for the selective isolation, identification and quantification of peptides that contain N-linked carbohydrates.
12754519	2	48	theme	comprehensive	476:488	arg1	challenge					533:541	an as-yet-unresolved technical challenge	502:541	an as-yet-unresolved technical challenge	502:541	Owing to the enormous complexity of proteomes, their comprehensive analysis is an as-yet-unresolved technical challenge.
12754519	2	48	theme	comprehensive	476:488	arg1	analysis					490:497	their comprehensive analysis	470:497	their comprehensive analysis	470:497	Owing to the enormous complexity of proteomes, their comprehensive analysis is an as-yet-unresolved technical challenge.
12754519	1	49	theme	systems	339:345	arg1	analysis					316:323	the functional analysis	301:323	the functional analysis of biological systems	301:345	Quantitative proteome profiling using stable isotope protein tagging and automated tandem mass spectrometry (MS/MS) is an emerging technology with great potential for the functional analysis of biological systems and for the detection of clinical diagnostic or prognostic marker proteins.
12754519	1	50	with	technology	265:274	arg1	potential					287:295	great potential	281:295	great potential	281:295	Quantitative proteome profiling using stable isotope protein tagging and automated tandem mass spectrometry (MS/MS) is an emerging technology with great potential for the functional analysis of biological systems and for the detection of clinical diagnostic or prognostic marker proteins.
12754519	1	51	theme	Quantitative	134:145	arg1	profiling					156:164	Quantitative proteome profiling	134:164	Quantitative proteome profiling using stable isotope protein tagging and automated tandem mass spectrometry (MS/MS)	134:248	Quantitative proteome profiling using stable isotope protein tagging and automated tandem mass spectrometry (MS/MS) is an emerging technology with great potential for the functional analysis of biological systems and for the detection of clinical diagnostic or prognostic marker proteins.
12754519	1	51	theme	Quantitative	134:145	arg1	technology					265:274	an emerging technology	253:274	an emerging technology with great potential for the functional analysis of biological systems and for the detection of clinical diagnostic or prognostic marker proteins	253:420	Quantitative proteome profiling using stable isotope protein tagging and automated tandem mass spectrometry (MS/MS) is an emerging technology with great potential for the functional analysis of biological systems and for the detection of clinical diagnostic or prognostic marker proteins.
12754519	6	52	gly	glycopeptides	1035:1047	arg2	glycopeptides					1035:1047	glycopeptides	1035:1047	glycopeptides	1035:1047	It is based on the conjugation of glycoproteins to a solid support using hydrazide chemistry, stable isotope labeling of glycopeptides and the specific release of formerly N-linked glycosylated peptides via peptide- N-glycosidase F (PNGase F).
12754519	6	53	theme	glycoproteins	948:960	arg1	conjugation					933:943	the conjugation	929:943	the conjugation of glycoproteins to a solid support using hydrazide chemistry, stable isotope labeling of glycopeptides and the specific release of formerly N-linked glycosylated peptides via peptide- N-glycosidase F (PNGase F)	929:1155	It is based on the conjugation of glycoproteins to a solid support using hydrazide chemistry, stable isotope labeling of glycopeptides and the specific release of formerly N-linked glycosylated peptides via peptide- N-glycosidase F (PNGase F).
12754519	5	54	link	N-linked	890:897	arg1	carbohydrates					899:911	N-linked carbohydrates	890:911	N-linked carbohydrates	890:911	Here we describe a method for the selective isolation, identification and quantification of peptides that contain N-linked carbohydrates.
12754519	1	55	theme	proteome	147:154	arg1	profiling					156:164	Quantitative proteome profiling	134:164	Quantitative proteome profiling using stable isotope protein tagging and automated tandem mass spectrometry (MS/MS)	134:248	Quantitative proteome profiling using stable isotope protein tagging and automated tandem mass spectrometry (MS/MS) is an emerging technology with great potential for the functional analysis of biological systems and for the detection of clinical diagnostic or prognostic marker proteins.
12754519	1	55	theme	proteome	147:154	arg1	technology					265:274	an emerging technology	253:274	an emerging technology with great potential for the functional analysis of biological systems and for the detection of clinical diagnostic or prognostic marker proteins	253:420	Quantitative proteome profiling using stable isotope protein tagging and automated tandem mass spectrometry (MS/MS) is an emerging technology with great potential for the functional analysis of biological systems and for the detection of clinical diagnostic or prognostic marker proteins.
12754519	0	56	gly	glycoproteins	46:58	arg1	glycoproteins					46:58	N-linked glycoproteins	37:58	N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry	37:131	Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry.
12754519	6	57	gly	glycoproteins	948:960	arg1	glycoproteins					948:960	glycoproteins	948:960	glycoproteins	948:960	It is based on the conjugation of glycoproteins to a solid support using hydrazide chemistry, stable isotope labeling of glycopeptides and the specific release of formerly N-linked glycosylated peptides via peptide- N-glycosidase F (PNGase F).
12754519	6	58	theme	peptides	1108:1115	arg1	labeling					1023:1030	stable isotope labeling	1008:1030	stable isotope labeling of glycopeptides	1008:1047	It is based on the conjugation of glycoproteins to a solid support using hydrazide chemistry, stable isotope labeling of glycopeptides and the specific release of formerly N-linked glycosylated peptides via peptide- N-glycosidase F (PNGase F).
12754519	6	58	theme	peptides	1108:1115	arg1	release					1066:1072	the specific release	1053:1072	the specific release of formerly N-linked glycosylated peptides via peptide- N-glycosidase F (PNGase F)	1053:1155	It is based on the conjugation of glycoproteins to a solid support using hydrazide chemistry, stable isotope labeling of glycopeptides and the specific release of formerly N-linked glycosylated peptides via peptide- N-glycosidase F (PNGase F).
12754519	6	58	theme	peptides	1108:1115	arg1	chemistry					997:1005	hydrazide chemistry	987:1005	hydrazide chemistry	987:1005	It is based on the conjugation of glycoproteins to a solid support using hydrazide chemistry, stable isotope labeling of glycopeptides and the specific release of formerly N-linked glycosylated peptides via peptide- N-glycosidase F (PNGase F).
12754519	5	59	theme	selective	810:818	arg1	isolation					820:828	the selective isolation	806:828	the selective isolation	806:828	Here we describe a method for the selective isolation, identification and quantification of peptides that contain N-linked carbohydrates.
12754519	4	60	theme	common	736:741	arg1	Glycosylation					710:722	Glycosylation	710:722	Glycosylation	710:722	Glycosylation is the most common post-translational modification.
12754519	4	60	theme	common	736:741	arg1	modification					762:773	the most common post-translational modification	727:773	the most common post-translational modification	727:773	Glycosylation is the most common post-translational modification.
12754519	6	61	theme	glycosylated	1095:1106	arg1	peptides					1108:1115	formerly N-linked glycosylated peptides	1077:1115	formerly N-linked glycosylated peptides	1077:1115	It is based on the conjugation of glycoproteins to a solid support using hydrazide chemistry, stable isotope labeling of glycopeptides and the specific release of formerly N-linked glycosylated peptides via peptide- N-glycosidase F (PNGase F).
12754519	8	62	theme	proteins	1298:1305	arg1	analysis					1257:1264	the analysis	1253:1264	the analysis of plasma membrane proteins and proteins contained in human blood serum	1253:1336	We applied the approach to the analysis of plasma membrane proteins and proteins contained in human blood serum.
12754519	6	63	theme	N-linked	1086:1093	arg1	peptides					1108:1115	formerly N-linked glycosylated peptides	1077:1115	formerly N-linked glycosylated peptides	1077:1115	It is based on the conjugation of glycoproteins to a solid support using hydrazide chemistry, stable isotope labeling of glycopeptides and the specific release of formerly N-linked glycosylated peptides via peptide- N-glycosidase F (PNGase F).
12754519	1	64	theme	stable	172:177	arg1	tagging					195:201	stable isotope protein tagging	172:201	stable isotope protein tagging	172:201	Quantitative proteome profiling using stable isotope protein tagging and automated tandem mass spectrometry (MS/MS) is an emerging technology with great potential for the functional analysis of biological systems and for the detection of clinical diagnostic or prognostic marker proteins.
12754519	6	65	theme	isotope	1015:1021	arg1	labeling					1023:1030	stable isotope labeling	1008:1030	stable isotope labeling of glycopeptides	1008:1047	It is based on the conjugation of glycoproteins to a solid support using hydrazide chemistry, stable isotope labeling of glycopeptides and the specific release of formerly N-linked glycosylated peptides via peptide- N-glycosidase F (PNGase F).
12754519	1	66	theme	emerging	256:263	arg1	profiling					156:164	Quantitative proteome profiling	134:164	Quantitative proteome profiling using stable isotope protein tagging and automated tandem mass spectrometry (MS/MS)	134:248	Quantitative proteome profiling using stable isotope protein tagging and automated tandem mass spectrometry (MS/MS) is an emerging technology with great potential for the functional analysis of biological systems and for the detection of clinical diagnostic or prognostic marker proteins.
12754519	1	66	theme	emerging	256:263	arg1	technology					265:274	an emerging technology	253:274	an emerging technology with great potential for the functional analysis of biological systems and for the detection of clinical diagnostic or prognostic marker proteins	253:420	Quantitative proteome profiling using stable isotope protein tagging and automated tandem mass spectrometry (MS/MS) is an emerging technology with great potential for the functional analysis of biological systems and for the detection of clinical diagnostic or prognostic marker proteins.
29061980	0	0	theme	Pompe	77:81	arg1	disease					83:89	Pompe disease	77:89	Pompe disease	77:89	Structure of human lysosomal acid α-glucosidase-a guide for the treatment of Pompe disease.
29061980	1	1	theme	motor	320:324	arg1	handicap					326:333	progressive motor handicap	308:333	progressive motor handicap	308:333	Pompe disease, a rare lysosomal storage disease caused by deficiency of the lysosomal acid α-glucosidase (GAA), is characterized by glycogen accumulation, triggering severe secondary cellular damage and resulting in progressive motor handicap and premature death.
29061980	4	2	theme	mutations	876:884	arg1	effects					849:855	the deleterious effects	833:855	the deleterious effects of disease-causing mutations	833:884	These structures portray the unbound form of rhGAA and complexes thereof with active site-directed inhibitors, providing insight into substrate recognition and the molecular framework for the rationalization of the deleterious effects of disease-causing mutations.
29061980	2	3	theme	pathological	461:472	arg1	variants					474:481	the pathological variants	457:481	the pathological variants	457:481	Numerous disease-causing mutations in the gaa gene have been reported, but the structural effects of the pathological variants were unknown.
29061980	4	4	theme	disease-causing	860:874	arg1	mutations					876:884	disease-causing mutations	860:884	disease-causing mutations	860:884	These structures portray the unbound form of rhGAA and complexes thereof with active site-directed inhibitors, providing insight into substrate recognition and the molecular framework for the rationalization of the deleterious effects of disease-causing mutations.
29061980	2	5	theme	variants	474:481	arg1	effects					446:452	the structural effects	431:452	the structural effects of the pathological variants	431:481	Numerous disease-causing mutations in the gaa gene have been reported, but the structural effects of the pathological variants were unknown.
29061980	2	5	theme	variants	474:481	arg1	unknown					488:494	unknown	488:494	unknown	488:494	Numerous disease-causing mutations in the gaa gene have been reported, but the structural effects of the pathological variants were unknown.
29061980	4	6	theme	rhGAA	667:671	arg1	form					659:662	the unbound form	647:662	the unbound form of rhGAA and complexes thereof with active site-directed inhibitors, providing insight into substrate recognition and the molecular framework for the rationalization of the deleterious effects of disease-causing mutations	647:884	These structures portray the unbound form of rhGAA and complexes thereof with active site-directed inhibitors, providing insight into substrate recognition and the molecular framework for the rationalization of the deleterious effects of disease-causing mutations.
29061980	1	7	theme	glycogen	224:231	arg1	accumulation					233:244	glycogen accumulation	224:244	glycogen accumulation	224:244	Pompe disease, a rare lysosomal storage disease caused by deficiency of the lysosomal acid α-glucosidase (GAA), is characterized by glycogen accumulation, triggering severe secondary cellular damage and resulting in progressive motor handicap and premature death.
29061980	4	8	with	complexes	677:685	arg1	inhibitors					721:730	active site-directed inhibitors	700:730	active site-directed inhibitors	700:730	These structures portray the unbound form of rhGAA and complexes thereof with active site-directed inhibitors, providing insight into substrate recognition and the molecular framework for the rationalization of the deleterious effects of disease-causing mutations.
29061980	3	9	theme	crystal	533:539	arg1	structures					541:550	the high-resolution crystal structures	513:550	the high-resolution crystal structures of recombinant human GAA (rhGAA), the standard care of Pompe disease	513:619	Here we present the high-resolution crystal structures of recombinant human GAA (rhGAA), the standard care of Pompe disease.
29061980	5	10	theme	allosteric	953:962	arg1	N-acetylcysteine					990:1005	the allosteric pharmacological chaperone N-acetylcysteine	949:1005	the allosteric pharmacological chaperone N-acetylcysteine	949:1005	Furthermore, we report the structure of rhGAA in complex with the allosteric pharmacological chaperone N-acetylcysteine, which reveals the stabilizing function of this chaperone at the structural level.
29061980	0	11	theme	disease	83:89	arg1	treatment					64:72	the treatment	60:72	the treatment of Pompe disease	60:89	Structure of human lysosomal acid α-glucosidase-a guide for the treatment of Pompe disease.
29061980	1	12	theme	premature	339:347	arg1	death					349:353	premature death	339:353	premature death	339:353	Pompe disease, a rare lysosomal storage disease caused by deficiency of the lysosomal acid α-glucosidase (GAA), is characterized by glycogen accumulation, triggering severe secondary cellular damage and resulting in progressive motor handicap and premature death.
29061980	5	13	theme	chaperone	980:988	arg1	N-acetylcysteine					990:1005	the allosteric pharmacological chaperone N-acetylcysteine	949:1005	the allosteric pharmacological chaperone N-acetylcysteine	949:1005	Furthermore, we report the structure of rhGAA in complex with the allosteric pharmacological chaperone N-acetylcysteine, which reveals the stabilizing function of this chaperone at the structural level.
29061980	4	14	theme	site-directed	707:719	arg1	inhibitors					721:730	active site-directed inhibitors	700:730	active site-directed inhibitors	700:730	These structures portray the unbound form of rhGAA and complexes thereof with active site-directed inhibitors, providing insight into substrate recognition and the molecular framework for the rationalization of the deleterious effects of disease-causing mutations.
29061980	4	15	theme	deleterious	837:847	arg1	effects					849:855	the deleterious effects	833:855	the deleterious effects of disease-causing mutations	833:884	These structures portray the unbound form of rhGAA and complexes thereof with active site-directed inhibitors, providing insight into substrate recognition and the molecular framework for the rationalization of the deleterious effects of disease-causing mutations.
29061980	5	16	theme	rhGAA	927:931	arg1	structure					914:922	the structure	910:922	the structure of rhGAA in complex with the allosteric pharmacological chaperone N-acetylcysteine, which reveals the stabilizing function of this chaperone at the structural level	910:1087	Furthermore, we report the structure of rhGAA in complex with the allosteric pharmacological chaperone N-acetylcysteine, which reveals the stabilizing function of this chaperone at the structural level.
29061980	5	17	from	rhGAA	927:931	arg1	complex					936:942	complex	936:942	complex with the allosteric pharmacological chaperone N-acetylcysteine, which reveals the stabilizing function of this chaperone at the structural level	936:1087	Furthermore, we report the structure of rhGAA in complex with the allosteric pharmacological chaperone N-acetylcysteine, which reveals the stabilizing function of this chaperone at the structural level.
29061980	3	18	theme	high-resolution	517:531	arg1	structures					541:550	the high-resolution crystal structures	513:550	the high-resolution crystal structures of recombinant human GAA (rhGAA), the standard care of Pompe disease	513:619	Here we present the high-resolution crystal structures of recombinant human GAA (rhGAA), the standard care of Pompe disease.
29061980	3	19	theme	human	567:571	arg1	care					599:602	the standard care	586:602	the standard care of Pompe disease	586:619	Here we present the high-resolution crystal structures of recombinant human GAA (rhGAA), the standard care of Pompe disease.
29061980	3	19	theme	human	567:571	arg1	rhGAA					578:582	rhGAA	578:582	rhGAA	578:582	Here we present the high-resolution crystal structures of recombinant human GAA (rhGAA), the standard care of Pompe disease.
29061980	3	19	theme	human	567:571	arg1	GAA					573:575	recombinant human GAA	555:575	recombinant human GAA (rhGAA)	555:583	Here we present the high-resolution crystal structures of recombinant human GAA (rhGAA), the standard care of Pompe disease.
29061980	4	20	with	rhGAA	667:671	arg1	inhibitors					721:730	active site-directed inhibitors	700:730	active site-directed inhibitors	700:730	These structures portray the unbound form of rhGAA and complexes thereof with active site-directed inhibitors, providing insight into substrate recognition and the molecular framework for the rationalization of the deleterious effects of disease-causing mutations.
29061980	4	21	theme	unbound	651:657	arg1	form					659:662	the unbound form	647:662	the unbound form of rhGAA and complexes thereof with active site-directed inhibitors, providing insight into substrate recognition and the molecular framework for the rationalization of the deleterious effects of disease-causing mutations	647:884	These structures portray the unbound form of rhGAA and complexes thereof with active site-directed inhibitors, providing insight into substrate recognition and the molecular framework for the rationalization of the deleterious effects of disease-causing mutations.
29061980	4	22	theme	effects	849:855	arg1	rationalization					814:828	the rationalization	810:828	the rationalization of the deleterious effects of disease-causing mutations	810:884	These structures portray the unbound form of rhGAA and complexes thereof with active site-directed inhibitors, providing insight into substrate recognition and the molecular framework for the rationalization of the deleterious effects of disease-causing mutations.
29061980	5	23	from	structure	914:922	arg1	complex					936:942	complex	936:942	complex with the allosteric pharmacological chaperone N-acetylcysteine, which reveals the stabilizing function of this chaperone at the structural level	936:1087	Furthermore, we report the structure of rhGAA in complex with the allosteric pharmacological chaperone N-acetylcysteine, which reveals the stabilizing function of this chaperone at the structural level.
29061980	3	24	theme	GAA	573:575	arg1	structures					541:550	the high-resolution crystal structures	513:550	the high-resolution crystal structures of recombinant human GAA (rhGAA), the standard care of Pompe disease	513:619	Here we present the high-resolution crystal structures of recombinant human GAA (rhGAA), the standard care of Pompe disease.
29061980	2	25	theme	disease-causing	365:379	arg1	mutations					381:389	Numerous disease-causing mutations	356:389	Numerous disease-causing mutations in the gaa gene	356:405	Numerous disease-causing mutations in the gaa gene have been reported, but the structural effects of the pathological variants were unknown.
29061980	0	26	theme	lysosomal	19:27	arg1	α-glucosidase-a					34:48	human lysosomal acid α-glucosidase-a	13:48	human lysosomal acid α-glucosidase-a	13:48	Structure of human lysosomal acid α-glucosidase-a guide for the treatment of Pompe disease.
29061980	1	27	theme	severe	258:263	arg1	damage					284:289	severe secondary cellular damage	258:289	severe secondary cellular damage	258:289	Pompe disease, a rare lysosomal storage disease caused by deficiency of the lysosomal acid α-glucosidase (GAA), is characterized by glycogen accumulation, triggering severe secondary cellular damage and resulting in progressive motor handicap and premature death.
29061980	1	28	theme	Pompe	92:96	arg1	disease					132:138	a rare lysosomal storage disease	107:138	a rare lysosomal storage disease caused by deficiency of the lysosomal acid α-glucosidase (GAA)	107:201	Pompe disease, a rare lysosomal storage disease caused by deficiency of the lysosomal acid α-glucosidase (GAA), is characterized by glycogen accumulation, triggering severe secondary cellular damage and resulting in progressive motor handicap and premature death.
29061980	1	28	theme	Pompe	92:96	arg1	disease					98:104	Pompe disease	92:104	Pompe disease	92:104	Pompe disease, a rare lysosomal storage disease caused by deficiency of the lysosomal acid α-glucosidase (GAA), is characterized by glycogen accumulation, triggering severe secondary cellular damage and resulting in progressive motor handicap and premature death.
29061980	1	29	theme	acid	178:181	arg1	α-glucosidase					183:195	the lysosomal acid α-glucosidase	164:195	the lysosomal acid α-glucosidase (GAA)	164:201	Pompe disease, a rare lysosomal storage disease caused by deficiency of the lysosomal acid α-glucosidase (GAA), is characterized by glycogen accumulation, triggering severe secondary cellular damage and resulting in progressive motor handicap and premature death.
29061980	1	29	theme	acid	178:181	arg1	GAA					198:200	GAA	198:200	GAA	198:200	Pompe disease, a rare lysosomal storage disease caused by deficiency of the lysosomal acid α-glucosidase (GAA), is characterized by glycogen accumulation, triggering severe secondary cellular damage and resulting in progressive motor handicap and premature death.
29061980	0	30	theme	human	13:17	arg1	α-glucosidase-a					34:48	human lysosomal acid α-glucosidase-a	13:48	human lysosomal acid α-glucosidase-a	13:48	Structure of human lysosomal acid α-glucosidase-a guide for the treatment of Pompe disease.
29061980	1	31	theme	secondary	265:273	arg1	damage					284:289	severe secondary cellular damage	258:289	severe secondary cellular damage	258:289	Pompe disease, a rare lysosomal storage disease caused by deficiency of the lysosomal acid α-glucosidase (GAA), is characterized by glycogen accumulation, triggering severe secondary cellular damage and resulting in progressive motor handicap and premature death.
29061980	2	32	theme	Numerous	356:363	arg1	mutations					381:389	Numerous disease-causing mutations	356:389	Numerous disease-causing mutations in the gaa gene	356:405	Numerous disease-causing mutations in the gaa gene have been reported, but the structural effects of the pathological variants were unknown.
29061980	3	33	theme	recombinant	555:565	arg1	care					599:602	the standard care	586:602	the standard care of Pompe disease	586:619	Here we present the high-resolution crystal structures of recombinant human GAA (rhGAA), the standard care of Pompe disease.
29061980	3	33	theme	recombinant	555:565	arg1	rhGAA					578:582	rhGAA	578:582	rhGAA	578:582	Here we present the high-resolution crystal structures of recombinant human GAA (rhGAA), the standard care of Pompe disease.
29061980	3	33	theme	recombinant	555:565	arg1	GAA					573:575	recombinant human GAA	555:575	recombinant human GAA (rhGAA)	555:583	Here we present the high-resolution crystal structures of recombinant human GAA (rhGAA), the standard care of Pompe disease.
29061980	1	34	theme	α-glucosidase	183:195	arg1	deficiency					150:159	deficiency	150:159	deficiency of the lysosomal acid α-glucosidase (GAA)	150:201	Pompe disease, a rare lysosomal storage disease caused by deficiency of the lysosomal acid α-glucosidase (GAA), is characterized by glycogen accumulation, triggering severe secondary cellular damage and resulting in progressive motor handicap and premature death.
29061980	0	35	theme	α-glucosidase-a	34:48	arg1	Structure					0:8	Structure	0:8	Structure of human lysosomal acid α-glucosidase-a	0:48	Structure of human lysosomal acid α-glucosidase-a guide for the treatment of Pompe disease.
29061980	1	36	theme	cellular	275:282	arg1	damage					284:289	severe secondary cellular damage	258:289	severe secondary cellular damage	258:289	Pompe disease, a rare lysosomal storage disease caused by deficiency of the lysosomal acid α-glucosidase (GAA), is characterized by glycogen accumulation, triggering severe secondary cellular damage and resulting in progressive motor handicap and premature death.
29061980	5	37	theme	stabilizing	1026:1036	arg1	function					1038:1045	the stabilizing function	1022:1045	the stabilizing function of this chaperone	1022:1063	Furthermore, we report the structure of rhGAA in complex with the allosteric pharmacological chaperone N-acetylcysteine, which reveals the stabilizing function of this chaperone at the structural level.
29061980	1	38	theme	lysosomal	168:176	arg1	α-glucosidase					183:195	the lysosomal acid α-glucosidase	164:195	the lysosomal acid α-glucosidase (GAA)	164:201	Pompe disease, a rare lysosomal storage disease caused by deficiency of the lysosomal acid α-glucosidase (GAA), is characterized by glycogen accumulation, triggering severe secondary cellular damage and resulting in progressive motor handicap and premature death.
29061980	1	38	theme	lysosomal	168:176	arg1	GAA					198:200	GAA	198:200	GAA	198:200	Pompe disease, a rare lysosomal storage disease caused by deficiency of the lysosomal acid α-glucosidase (GAA), is characterized by glycogen accumulation, triggering severe secondary cellular damage and resulting in progressive motor handicap and premature death.
29061980	0	39	theme	acid	29:32	arg1	α-glucosidase-a					34:48	human lysosomal acid α-glucosidase-a	13:48	human lysosomal acid α-glucosidase-a	13:48	Structure of human lysosomal acid α-glucosidase-a guide for the treatment of Pompe disease.
29061980	3	40	theme	Pompe	607:611	arg1	disease					613:619	Pompe disease	607:619	Pompe disease	607:619	Here we present the high-resolution crystal structures of recombinant human GAA (rhGAA), the standard care of Pompe disease.
29061980	5	41	with	complex	936:942	arg1	N-acetylcysteine					990:1005	the allosteric pharmacological chaperone N-acetylcysteine	949:1005	the allosteric pharmacological chaperone N-acetylcysteine	949:1005	Furthermore, we report the structure of rhGAA in complex with the allosteric pharmacological chaperone N-acetylcysteine, which reveals the stabilizing function of this chaperone at the structural level.
29061980	2	42	from	mutations	381:389	arg1	gene					402:405	the gaa gene	394:405	the gaa gene	394:405	Numerous disease-causing mutations in the gaa gene have been reported, but the structural effects of the pathological variants were unknown.
29061980	2	43	theme	gaa	398:400	arg1	gene					402:405	the gaa gene	394:405	the gaa gene	394:405	Numerous disease-causing mutations in the gaa gene have been reported, but the structural effects of the pathological variants were unknown.
29061980	3	44	theme	disease	613:619	arg1	care					599:602	the standard care	586:602	the standard care of Pompe disease	586:619	Here we present the high-resolution crystal structures of recombinant human GAA (rhGAA), the standard care of Pompe disease.
29061980	3	44	theme	disease	613:619	arg1	GAA					573:575	recombinant human GAA	555:575	recombinant human GAA (rhGAA)	555:583	Here we present the high-resolution crystal structures of recombinant human GAA (rhGAA), the standard care of Pompe disease.
29061980	2	45	theme	structural	435:444	arg1	effects					446:452	the structural effects	431:452	the structural effects of the pathological variants	431:481	Numerous disease-causing mutations in the gaa gene have been reported, but the structural effects of the pathological variants were unknown.
29061980	2	45	theme	structural	435:444	arg1	unknown					488:494	unknown	488:494	unknown	488:494	Numerous disease-causing mutations in the gaa gene have been reported, but the structural effects of the pathological variants were unknown.
29061980	5	46	theme	chaperone	1055:1063	arg1	function					1038:1045	the stabilizing function	1022:1045	the stabilizing function of this chaperone	1022:1063	Furthermore, we report the structure of rhGAA in complex with the allosteric pharmacological chaperone N-acetylcysteine, which reveals the stabilizing function of this chaperone at the structural level.
29061980	4	47	theme	complexes	677:685	arg1	form					659:662	the unbound form	647:662	the unbound form of rhGAA and complexes thereof with active site-directed inhibitors, providing insight into substrate recognition and the molecular framework for the rationalization of the deleterious effects of disease-causing mutations	647:884	These structures portray the unbound form of rhGAA and complexes thereof with active site-directed inhibitors, providing insight into substrate recognition and the molecular framework for the rationalization of the deleterious effects of disease-causing mutations.
29061980	4	48	theme	molecular	786:794	arg1	framework					796:804	the molecular framework	782:804	the molecular framework for the rationalization of the deleterious effects of disease-causing mutations	782:884	These structures portray the unbound form of rhGAA and complexes thereof with active site-directed inhibitors, providing insight into substrate recognition and the molecular framework for the rationalization of the deleterious effects of disease-causing mutations.
29061980	1	49	theme	rare	109:112	arg1	disease					132:138	a rare lysosomal storage disease	107:138	a rare lysosomal storage disease caused by deficiency of the lysosomal acid α-glucosidase (GAA)	107:201	Pompe disease, a rare lysosomal storage disease caused by deficiency of the lysosomal acid α-glucosidase (GAA), is characterized by glycogen accumulation, triggering severe secondary cellular damage and resulting in progressive motor handicap and premature death.
29061980	1	49	theme	rare	109:112	arg1	disease					98:104	Pompe disease	92:104	Pompe disease	92:104	Pompe disease, a rare lysosomal storage disease caused by deficiency of the lysosomal acid α-glucosidase (GAA), is characterized by glycogen accumulation, triggering severe secondary cellular damage and resulting in progressive motor handicap and premature death.
29061980	4	50	theme	substrate	756:764	arg1	recognition					766:776	substrate recognition	756:776	substrate recognition	756:776	These structures portray the unbound form of rhGAA and complexes thereof with active site-directed inhibitors, providing insight into substrate recognition and the molecular framework for the rationalization of the deleterious effects of disease-causing mutations.
29061980	5	51	theme	structural	1072:1081	arg1	level					1083:1087	the structural level	1068:1087	the structural level	1068:1087	Furthermore, we report the structure of rhGAA in complex with the allosteric pharmacological chaperone N-acetylcysteine, which reveals the stabilizing function of this chaperone at the structural level.
29061980	5	52	theme	pharmacological	964:978	arg1	N-acetylcysteine					990:1005	the allosteric pharmacological chaperone N-acetylcysteine	949:1005	the allosteric pharmacological chaperone N-acetylcysteine	949:1005	Furthermore, we report the structure of rhGAA in complex with the allosteric pharmacological chaperone N-acetylcysteine, which reveals the stabilizing function of this chaperone at the structural level.
29061980	1	53	theme	lysosomal	114:122	arg1	disease					132:138	a rare lysosomal storage disease	107:138	a rare lysosomal storage disease caused by deficiency of the lysosomal acid α-glucosidase (GAA)	107:201	Pompe disease, a rare lysosomal storage disease caused by deficiency of the lysosomal acid α-glucosidase (GAA), is characterized by glycogen accumulation, triggering severe secondary cellular damage and resulting in progressive motor handicap and premature death.
29061980	1	53	theme	lysosomal	114:122	arg1	disease					98:104	Pompe disease	92:104	Pompe disease	92:104	Pompe disease, a rare lysosomal storage disease caused by deficiency of the lysosomal acid α-glucosidase (GAA), is characterized by glycogen accumulation, triggering severe secondary cellular damage and resulting in progressive motor handicap and premature death.
29061980	5	54	from	complex	936:942	arg1	structure					914:922	the structure	910:922	the structure of rhGAA in complex with the allosteric pharmacological chaperone N-acetylcysteine, which reveals the stabilizing function of this chaperone at the structural level	910:1087	Furthermore, we report the structure of rhGAA in complex with the allosteric pharmacological chaperone N-acetylcysteine, which reveals the stabilizing function of this chaperone at the structural level.
29061980	4	55	theme	active	700:705	arg1	inhibitors					721:730	active site-directed inhibitors	700:730	active site-directed inhibitors	700:730	These structures portray the unbound form of rhGAA and complexes thereof with active site-directed inhibitors, providing insight into substrate recognition and the molecular framework for the rationalization of the deleterious effects of disease-causing mutations.
29061980	4	56	dep	inhibitors	721:730	arg1	providing					733:741	providing	733:741	providing insight into substrate recognition and the molecular framework for the rationalization of the deleterious effects of disease-causing mutations	733:884	These structures portray the unbound form of rhGAA and complexes thereof with active site-directed inhibitors, providing insight into substrate recognition and the molecular framework for the rationalization of the deleterious effects of disease-causing mutations.
29061980	1	57	theme	storage	124:130	arg1	disease					132:138	a rare lysosomal storage disease	107:138	a rare lysosomal storage disease caused by deficiency of the lysosomal acid α-glucosidase (GAA)	107:201	Pompe disease, a rare lysosomal storage disease caused by deficiency of the lysosomal acid α-glucosidase (GAA), is characterized by glycogen accumulation, triggering severe secondary cellular damage and resulting in progressive motor handicap and premature death.
29061980	1	57	theme	storage	124:130	arg1	disease					98:104	Pompe disease	92:104	Pompe disease	92:104	Pompe disease, a rare lysosomal storage disease caused by deficiency of the lysosomal acid α-glucosidase (GAA), is characterized by glycogen accumulation, triggering severe secondary cellular damage and resulting in progressive motor handicap and premature death.
29061980	1	58	theme	progressive	308:318	arg1	handicap					326:333	progressive motor handicap	308:333	progressive motor handicap	308:333	Pompe disease, a rare lysosomal storage disease caused by deficiency of the lysosomal acid α-glucosidase (GAA), is characterized by glycogen accumulation, triggering severe secondary cellular damage and resulting in progressive motor handicap and premature death.
29061980	3	59	theme	standard	590:597	arg1	care					599:602	the standard care	586:602	the standard care of Pompe disease	586:619	Here we present the high-resolution crystal structures of recombinant human GAA (rhGAA), the standard care of Pompe disease.
29061980	3	59	theme	standard	590:597	arg1	GAA					573:575	recombinant human GAA	555:575	recombinant human GAA (rhGAA)	555:583	Here we present the high-resolution crystal structures of recombinant human GAA (rhGAA), the standard care of Pompe disease.
6587378	5	0	theme	beta	708:711	arg1	2-glycoprotein					713:726	beta 2-glycoprotein I	708:728	beta 2-glycoprotein I	708:728	This suggests that beta 2-glycoprotein I may have evolved by repeated duplications of a gene coding for a 60-amino acid segment of protein.
6587378	0	1	gly	2-glycoprotein	50:63	arg1	2-glycoprotein					50:63	human plasma beta 2-glycoprotein I	32:65	human plasma beta 2-glycoprotein I	32:65	Complete amino acid sequence of human plasma beta 2-glycoprotein I.
6587378	1	2	dep	2-glycoprotein	128:141	arg1	congruent					150:158	congruent	150:158	congruent to 50,000	150:168	We have determined the complete amino acid sequence of beta 2-glycoprotein I (Mr, congruent to 50,000), a human plasma protein that is associated with lipids and binds to platelets but whose function is not yet known.
6587378	1	2	dep	2-glycoprotein	128:141	arg1	Mr					146:147	Mr	146:147	Mr	146:147	We have determined the complete amino acid sequence of beta 2-glycoprotein I (Mr, congruent to 50,000), a human plasma protein that is associated with lipids and binds to platelets but whose function is not yet known.
6587378	4	3	theme	Computerized	532:543	arg1	analysis					545:552	Computerized analysis	532:552	Computerized analysis of the sequence	532:568	Computerized analysis of the sequence reveals five consecutive homologous segments in which cysteine, proline, and tryptophan appear to be highly conserved.
6587378	5	4	theme	gene	777:780	arg1	duplications					759:770	repeated duplications	750:770	repeated duplications of a gene coding for a 60-amino acid segment of protein	750:826	This suggests that beta 2-glycoprotein I may have evolved by repeated duplications of a gene coding for a 60-amino acid segment of protein.
6587378	5	5	gly	2-glycoprotein	713:726	arg1	2-glycoprotein					713:726	beta 2-glycoprotein I	708:728	beta 2-glycoprotein I	708:728	This suggests that beta 2-glycoprotein I may have evolved by repeated duplications of a gene coding for a 60-amino acid segment of protein.
6587378	5	6	theme	acid	804:807	arg1	segment					809:815	a 60-amino acid segment	793:815	a 60-amino acid segment of protein	793:826	This suggests that beta 2-glycoprotein I may have evolved by repeated duplications of a gene coding for a 60-amino acid segment of protein.
6587378	5	7	theme	repeated	750:757	arg1	duplications					759:770	repeated duplications	750:770	repeated duplications of a gene coding for a 60-amino acid segment of protein	750:826	This suggests that beta 2-glycoprotein I may have evolved by repeated duplications of a gene coding for a 60-amino acid segment of protein.
6587378	5	8	theme	60-amino	795:802	arg1	segment					809:815	a 60-amino acid segment	793:815	a 60-amino acid segment of protein	793:826	This suggests that beta 2-glycoprotein I may have evolved by repeated duplications of a gene coding for a 60-amino acid segment of protein.
6587378	0	9	theme	amino	9:13	arg1	sequence					20:27	Complete amino acid sequence	0:27	Complete amino acid sequence of human plasma beta 2-glycoprotein I	0:65	Complete amino acid sequence of human plasma beta 2-glycoprotein I.
6587378	3	10	from	proline	425:431	arg1	rich					404:407	rich	404:407	rich	404:407	The protein is rich in cysteine and proline, and the sequence is notable for the frequent occurrence of Cys-Pro linkages at regular intervals.
6587378	3	10	from	proline	425:431	arg1	protein					393:399	The protein	389:399	The protein	389:399	The protein is rich in cysteine and proline, and the sequence is notable for the frequent occurrence of Cys-Pro linkages at regular intervals.
6587378	3	11	theme	linkages	501:508	arg1	occurrence					479:488	the frequent occurrence	466:488	the frequent occurrence of Cys-Pro linkages at regular intervals	466:529	The protein is rich in cysteine and proline, and the sequence is notable for the frequent occurrence of Cys-Pro linkages at regular intervals.
6587378	2	12	theme	amino	314:318	arg1	acids					320:324	326 amino acids	310:324	326 amino acids	310:324	The protein consists of 326 amino acids and has five attached glucosamine-containing oligosaccharides.
6587378	0	13	theme	Complete	0:7	arg1	sequence					20:27	Complete amino acid sequence	0:27	Complete amino acid sequence of human plasma beta 2-glycoprotein I	0:65	Complete amino acid sequence of human plasma beta 2-glycoprotein I.
6587378	3	14	theme	Cys-Pro	493:499	arg1	linkages					501:508	Cys-Pro linkages	493:508	Cys-Pro linkages	493:508	The protein is rich in cysteine and proline, and the sequence is notable for the frequent occurrence of Cys-Pro linkages at regular intervals.
6587378	3	15	from	intervals	521:529	arg1	occurrence					479:488	the frequent occurrence	466:488	the frequent occurrence of Cys-Pro linkages at regular intervals	466:529	The protein is rich in cysteine and proline, and the sequence is notable for the frequent occurrence of Cys-Pro linkages at regular intervals.
6587378	2	16	theme	glucosamine-containing	348:369	arg1	oligosaccharides					371:386	five attached glucosamine-containing oligosaccharides	334:386	five attached glucosamine-containing oligosaccharides	334:386	The protein consists of 326 amino acids and has five attached glucosamine-containing oligosaccharides.
6587378	0	17	theme	acid	15:18	arg1	sequence					20:27	Complete amino acid sequence	0:27	Complete amino acid sequence of human plasma beta 2-glycoprotein I	0:65	Complete amino acid sequence of human plasma beta 2-glycoprotein I.
6587378	1	18	theme	complete	91:98	arg1	sequence					111:118	the complete amino acid sequence	87:118	the complete amino acid sequence of beta 2-glycoprotein I (Mr, congruent to 50,000), a human plasma protein that is associated with lipids and binds to platelets but whose function is not yet known	87:283	We have determined the complete amino acid sequence of beta 2-glycoprotein I (Mr, congruent to 50,000), a human plasma protein that is associated with lipids and binds to platelets but whose function is not yet known.
6587378	2	19	theme	attached	339:346	arg1	oligosaccharides					371:386	five attached glucosamine-containing oligosaccharides	334:386	five attached glucosamine-containing oligosaccharides	334:386	The protein consists of 326 amino acids and has five attached glucosamine-containing oligosaccharides.
6587378	0	20	theme	human	32:36	arg1	2-glycoprotein					50:63	human plasma beta 2-glycoprotein I	32:65	human plasma beta 2-glycoprotein I	32:65	Complete amino acid sequence of human plasma beta 2-glycoprotein I.
6587378	1	21	dep	congruent	150:158	arg1	to					160:161	to	160:161	to	160:161	We have determined the complete amino acid sequence of beta 2-glycoprotein I (Mr, congruent to 50,000), a human plasma protein that is associated with lipids and binds to platelets but whose function is not yet known.
6587378	1	21	dep	congruent	150:158	arg1	50,000					163:168	50,000	163:168	50,000	163:168	We have determined the complete amino acid sequence of beta 2-glycoprotein I (Mr, congruent to 50,000), a human plasma protein that is associated with lipids and binds to platelets but whose function is not yet known.
6587378	4	22	theme	homologous	595:604	arg1	segments					606:613	five consecutive homologous segments	578:613	five consecutive homologous segments in which cysteine, proline, and tryptophan appear to be highly conserved	578:686	Computerized analysis of the sequence reveals five consecutive homologous segments in which cysteine, proline, and tryptophan appear to be highly conserved.
6587378	4	23	theme	consecutive	583:593	arg1	segments					606:613	five consecutive homologous segments	578:613	five consecutive homologous segments in which cysteine, proline, and tryptophan appear to be highly conserved	578:686	Computerized analysis of the sequence reveals five consecutive homologous segments in which cysteine, proline, and tryptophan appear to be highly conserved.
6587378	0	24	theme	beta	45:48	arg1	2-glycoprotein					50:63	human plasma beta 2-glycoprotein I	32:65	human plasma beta 2-glycoprotein I	32:65	Complete amino acid sequence of human plasma beta 2-glycoprotein I.
6587378	1	25	gly	2-glycoprotein	128:141	arg1	protein					187:193	a human plasma protein	172:193	a human plasma protein that is associated with lipids and binds to platelets but whose function is not yet known	172:283	We have determined the complete amino acid sequence of beta 2-glycoprotein I (Mr, congruent to 50,000), a human plasma protein that is associated with lipids and binds to platelets but whose function is not yet known.
6587378	1	25	gly	2-glycoprotein	128:141	arg1	2-glycoprotein					128:141	beta 2-glycoprotein I	123:143	beta 2-glycoprotein I (Mr, congruent to 50,000)	123:169	We have determined the complete amino acid sequence of beta 2-glycoprotein I (Mr, congruent to 50,000), a human plasma protein that is associated with lipids and binds to platelets but whose function is not yet known.
6587378	3	26	theme	regular	513:519	arg1	intervals					521:529	regular intervals	513:529	regular intervals	513:529	The protein is rich in cysteine and proline, and the sequence is notable for the frequent occurrence of Cys-Pro linkages at regular intervals.
6587378	3	27	from	rich	404:407	arg1	proline					425:431	proline	425:431	proline	425:431	The protein is rich in cysteine and proline, and the sequence is notable for the frequent occurrence of Cys-Pro linkages at regular intervals.
6587378	3	27	from	rich	404:407	arg1	cysteine					412:419	cysteine	412:419	cysteine	412:419	The protein is rich in cysteine and proline, and the sequence is notable for the frequent occurrence of Cys-Pro linkages at regular intervals.
6587378	1	28	theme	amino	100:104	arg1	sequence					111:118	the complete amino acid sequence	87:118	the complete amino acid sequence of beta 2-glycoprotein I (Mr, congruent to 50,000), a human plasma protein that is associated with lipids and binds to platelets but whose function is not yet known	87:283	We have determined the complete amino acid sequence of beta 2-glycoprotein I (Mr, congruent to 50,000), a human plasma protein that is associated with lipids and binds to platelets but whose function is not yet known.
6587378	0	29	theme	plasma	38:43	arg1	2-glycoprotein					50:63	human plasma beta 2-glycoprotein I	32:65	human plasma beta 2-glycoprotein I	32:65	Complete amino acid sequence of human plasma beta 2-glycoprotein I.
6587378	2	30	contain	has	330:332	arg1	protein					290:296	The protein	286:296	The protein	286:296	The protein consists of 326 amino acids and has five attached glucosamine-containing oligosaccharides.
6587378	2	30	contain	has	330:332	arg2	oligosaccharides					371:386	five attached glucosamine-containing oligosaccharides	334:386	five attached glucosamine-containing oligosaccharides	334:386	The protein consists of 326 amino acids and has five attached glucosamine-containing oligosaccharides.
6587378	1	31	theme	acid	106:109	arg1	sequence					111:118	the complete amino acid sequence	87:118	the complete amino acid sequence of beta 2-glycoprotein I (Mr, congruent to 50,000), a human plasma protein that is associated with lipids and binds to platelets but whose function is not yet known	87:283	We have determined the complete amino acid sequence of beta 2-glycoprotein I (Mr, congruent to 50,000), a human plasma protein that is associated with lipids and binds to platelets but whose function is not yet known.
6587378	3	32	from	cysteine	412:419	arg1	rich					404:407	rich	404:407	rich	404:407	The protein is rich in cysteine and proline, and the sequence is notable for the frequent occurrence of Cys-Pro linkages at regular intervals.
6587378	3	32	from	cysteine	412:419	arg1	protein					393:399	The protein	389:399	The protein	389:399	The protein is rich in cysteine and proline, and the sequence is notable for the frequent occurrence of Cys-Pro linkages at regular intervals.
6587378	1	33	theme	human	174:178	arg1	protein					187:193	a human plasma protein	172:193	a human plasma protein that is associated with lipids and binds to platelets but whose function is not yet known	172:283	We have determined the complete amino acid sequence of beta 2-glycoprotein I (Mr, congruent to 50,000), a human plasma protein that is associated with lipids and binds to platelets but whose function is not yet known.
6587378	1	33	theme	human	174:178	arg1	2-glycoprotein					128:141	beta 2-glycoprotein I	123:143	beta 2-glycoprotein I (Mr, congruent to 50,000)	123:169	We have determined the complete amino acid sequence of beta 2-glycoprotein I (Mr, congruent to 50,000), a human plasma protein that is associated with lipids and binds to platelets but whose function is not yet known.
6587378	3	34	theme	frequent	470:477	arg1	occurrence					479:488	the frequent occurrence	466:488	the frequent occurrence of Cys-Pro linkages at regular intervals	466:529	The protein is rich in cysteine and proline, and the sequence is notable for the frequent occurrence of Cys-Pro linkages at regular intervals.
6587378	5	35	theme	protein	820:826	arg1	segment					809:815	a 60-amino acid segment	793:815	a 60-amino acid segment of protein	793:826	This suggests that beta 2-glycoprotein I may have evolved by repeated duplications of a gene coding for a 60-amino acid segment of protein.
6587378	1	36	theme	plasma	180:185	arg1	protein					187:193	a human plasma protein	172:193	a human plasma protein that is associated with lipids and binds to platelets but whose function is not yet known	172:283	We have determined the complete amino acid sequence of beta 2-glycoprotein I (Mr, congruent to 50,000), a human plasma protein that is associated with lipids and binds to platelets but whose function is not yet known.
6587378	1	36	theme	plasma	180:185	arg1	2-glycoprotein					128:141	beta 2-glycoprotein I	123:143	beta 2-glycoprotein I (Mr, congruent to 50,000)	123:169	We have determined the complete amino acid sequence of beta 2-glycoprotein I (Mr, congruent to 50,000), a human plasma protein that is associated with lipids and binds to platelets but whose function is not yet known.
6587378	1	37	theme	beta	123:126	arg1	protein					187:193	a human plasma protein	172:193	a human plasma protein that is associated with lipids and binds to platelets but whose function is not yet known	172:283	We have determined the complete amino acid sequence of beta 2-glycoprotein I (Mr, congruent to 50,000), a human plasma protein that is associated with lipids and binds to platelets but whose function is not yet known.
6587378	1	37	theme	beta	123:126	arg1	2-glycoprotein					128:141	beta 2-glycoprotein I	123:143	beta 2-glycoprotein I (Mr, congruent to 50,000)	123:169	We have determined the complete amino acid sequence of beta 2-glycoprotein I (Mr, congruent to 50,000), a human plasma protein that is associated with lipids and binds to platelets but whose function is not yet known.
6587378	4	38	theme	sequence	561:568	arg1	analysis					545:552	Computerized analysis	532:552	Computerized analysis of the sequence	532:568	Computerized analysis of the sequence reveals five consecutive homologous segments in which cysteine, proline, and tryptophan appear to be highly conserved.
6587378	0	39	theme	2-glycoprotein	50:63	arg1	sequence					20:27	Complete amino acid sequence	0:27	Complete amino acid sequence of human plasma beta 2-glycoprotein I	0:65	Complete amino acid sequence of human plasma beta 2-glycoprotein I.
6587378	1	40	theme	2-glycoprotein	128:141	arg1	sequence					111:118	the complete amino acid sequence	87:118	the complete amino acid sequence of beta 2-glycoprotein I (Mr, congruent to 50,000), a human plasma protein that is associated with lipids and binds to platelets but whose function is not yet known	87:283	We have determined the complete amino acid sequence of beta 2-glycoprotein I (Mr, congruent to 50,000), a human plasma protein that is associated with lipids and binds to platelets but whose function is not yet known.
33031746	6	0	theme	mucociliary	622:632	arg1	clearance					634:642	mucociliary clearance	622:642	mucociliary clearance	622:642	Our findings reveal the shared mechanism by which complex macromolecules responsible for blood clotting, mucociliary clearance, and the intestinal mucosal barrier form protective polymers and hydrogels.
33031746	7	1	theme	cryo-electron	734:746	arg1	microscopy					748:757	cryo-electron microscopy	734:757	cryo-electron microscopy	734:757	Specifically, cryo-electron microscopy and crystal structures show how disulfide-rich bridges and pH-tunable interfaces control successive assembly steps in the endoplasmic reticulum and Golgi apparatus.
33031746	9	2	theme	mucin	1019:1023	arg1	mechanism					1034:1042	The mucin assembly mechanism	1015:1042	The mucin assembly mechanism	1015:1042	The mucin assembly mechanism and its adaptation for hemostasis provide the foundation for rational manipulation of barrier function and coagulation.
33031746	6	3	theme	responsible	590:600	arg1	macromolecules					575:588	complex macromolecules	567:588	complex macromolecules responsible for blood clotting, mucociliary clearance, and the intestinal mucosal barrier	567:678	Our findings reveal the shared mechanism by which complex macromolecules responsible for blood clotting, mucociliary clearance, and the intestinal mucosal barrier form protective polymers and hydrogels.
33031746	8	4	theme	mucin	961:965	arg1	domain					967:972	a densely O-glycosylated mucin domain	936:972	a densely O-glycosylated mucin domain	936:972	Remarkably, a densely O-glycosylated mucin domain performs an organizational role in MUC2.
33031746	3	5	gly	glycoproteins	264:276	arg1	glycoproteins					264:276	Mucin glycoproteins	258:276	Mucin glycoproteins	258:276	Mucin glycoproteins and the related von Willebrand factor guard the vulnerable cell layers in these diverse systems.
33031746	9	6	theme	assembly	1025:1032	arg1	mechanism					1034:1042	The mucin assembly mechanism	1015:1042	The mucin assembly mechanism	1015:1042	The mucin assembly mechanism and its adaptation for hemostasis provide the foundation for rational manipulation of barrier function and coagulation.
33031746	7	7	theme	assembly	859:866	arg1	steps					868:872	successive assembly steps	848:872	successive assembly steps in the endoplasmic reticulum and Golgi apparatus	848:921	Specifically, cryo-electron microscopy and crystal structures show how disulfide-rich bridges and pH-tunable interfaces control successive assembly steps in the endoplasmic reticulum and Golgi apparatus.
33031746	9	8	theme	barrier	1130:1136	arg1	function					1138:1145	barrier function	1130:1145	barrier function	1130:1145	The mucin assembly mechanism and its adaptation for hemostasis provide the foundation for rational manipulation of barrier function and coagulation.
33031746	9	9	theme	coagulation	1151:1161	arg1	manipulation					1114:1125	rational manipulation	1105:1125	rational manipulation of barrier function and coagulation	1105:1161	The mucin assembly mechanism and its adaptation for hemostasis provide the foundation for rational manipulation of barrier function and coagulation.
33031746	3	10	theme	cell	337:340	arg1	layers					342:347	the vulnerable cell layers	322:347	the vulnerable cell layers in these diverse systems	322:372	Mucin glycoproteins and the related von Willebrand factor guard the vulnerable cell layers in these diverse systems.
33031746	9	11	theme	rational	1105:1112	arg1	manipulation					1114:1125	rational manipulation	1105:1125	rational manipulation of barrier function and coagulation	1105:1161	The mucin assembly mechanism and its adaptation for hemostasis provide the foundation for rational manipulation of barrier function and coagulation.
33031746	7	12	theme	Golgi	907:911	arg1	apparatus					913:921	Golgi apparatus	907:921	Golgi apparatus	907:921	Specifically, cryo-electron microscopy and crystal structures show how disulfide-rich bridges and pH-tunable interfaces control successive assembly steps in the endoplasmic reticulum and Golgi apparatus.
33031746	6	13	theme	complex	567:573	arg1	macromolecules					575:588	complex macromolecules	567:588	complex macromolecules responsible for blood clotting, mucociliary clearance, and the intestinal mucosal barrier	567:678	Our findings reveal the shared mechanism by which complex macromolecules responsible for blood clotting, mucociliary clearance, and the intestinal mucosal barrier form protective polymers and hydrogels.
33031746	1	14	theme	respiratory	68:78	arg1	tracts					95:100	The respiratory and intestinal tracts	64:100	The respiratory and intestinal tracts	64:100	The respiratory and intestinal tracts are exposed to physical and biological hazards accompanying the intake of air and food.
33031746	7	15	theme	endoplasmic	881:891	arg1	reticulum					893:901	the endoplasmic reticulum	877:901	the endoplasmic reticulum	877:901	Specifically, cryo-electron microscopy and crystal structures show how disulfide-rich bridges and pH-tunable interfaces control successive assembly steps in the endoplasmic reticulum and Golgi apparatus.
33031746	6	16	theme	blood	606:610	arg1	clotting					612:619	blood clotting	606:619	blood clotting	606:619	Our findings reveal the shared mechanism by which complex macromolecules responsible for blood clotting, mucociliary clearance, and the intestinal mucosal barrier form protective polymers and hydrogels.
33031746	8	17	theme	O-glycosylated	946:959	arg1	domain					967:972	a densely O-glycosylated mucin domain	936:972	a densely O-glycosylated mucin domain	936:972	Remarkably, a densely O-glycosylated mucin domain performs an organizational role in MUC2.
33031746	5	18	theme	intestinal	494:503	arg1	MUC2					511:514	the intestinal mucin MUC2	490:514	the intestinal mucin MUC2	490:514	Here, we present an integrated structural analysis of the intestinal mucin MUC2.
33031746	1	19	theme	air	176:178	arg1	intake					166:171	the intake	162:171	the intake of air and food	162:187	The respiratory and intestinal tracts are exposed to physical and biological hazards accompanying the intake of air and food.
33031746	0	20	theme	Assembly	0:7	arg1	Mechanism					9:17	Assembly Mechanism	0:17	Assembly Mechanism of Mucin	0:26	Assembly Mechanism of Mucin and von Willebrand Factor Polymers.
33031746	4	21	theme	Colon	375:379	arg1	mucins					381:386	Colon mucins	375:386	Colon mucins	375:386	Colon mucins additionally house and feed the gut microbiome.
33031746	1	22	theme	intestinal	84:93	arg1	tracts					95:100	The respiratory and intestinal tracts	64:100	The respiratory and intestinal tracts	64:100	The respiratory and intestinal tracts are exposed to physical and biological hazards accompanying the intake of air and food.
33031746	6	23	theme	mucosal	664:670	arg1	barrier					672:678	the intestinal mucosal barrier	649:678	the intestinal mucosal barrier	649:678	Our findings reveal the shared mechanism by which complex macromolecules responsible for blood clotting, mucociliary clearance, and the intestinal mucosal barrier form protective polymers and hydrogels.
33031746	3	24	theme	diverse	358:364	arg1	systems					366:372	these diverse systems	352:372	these diverse systems	352:372	Mucin glycoproteins and the related von Willebrand factor guard the vulnerable cell layers in these diverse systems.
33031746	7	25	theme	successive	848:857	arg1	steps					868:872	successive assembly steps	848:872	successive assembly steps in the endoplasmic reticulum and Golgi apparatus	848:921	Specifically, cryo-electron microscopy and crystal structures show how disulfide-rich bridges and pH-tunable interfaces control successive assembly steps in the endoplasmic reticulum and Golgi apparatus.
33031746	1	26	theme	food	184:187	arg1	intake					166:171	the intake	162:171	the intake of air and food	162:187	The respiratory and intestinal tracts are exposed to physical and biological hazards accompanying the intake of air and food.
33031746	7	27	theme	pH-tunable	818:827	arg1	interfaces					829:838	pH-tunable interfaces	818:838	pH-tunable interfaces	818:838	Specifically, cryo-electron microscopy and crystal structures show how disulfide-rich bridges and pH-tunable interfaces control successive assembly steps in the endoplasmic reticulum and Golgi apparatus.
33031746	0	28	dep	Polymers	54:61	arg1	Mechanism					9:17	Assembly Mechanism	0:17	Assembly Mechanism of Mucin	0:26	Assembly Mechanism of Mucin and von Willebrand Factor Polymers.
33031746	0	28	dep	Polymers	54:61	arg1	Factor					47:52	von Willebrand Factor	32:52	von Willebrand Factor	32:52	Assembly Mechanism of Mucin and von Willebrand Factor Polymers.
33031746	5	29	theme	integrated	456:465	arg1	analysis					478:485	an integrated structural analysis	453:485	an integrated structural analysis of the intestinal mucin MUC2	453:514	Here, we present an integrated structural analysis of the intestinal mucin MUC2.
33031746	6	30	theme	protective	685:694	arg1	polymers					696:703	protective polymers	685:703	protective polymers	685:703	Our findings reveal the shared mechanism by which complex macromolecules responsible for blood clotting, mucociliary clearance, and the intestinal mucosal barrier form protective polymers and hydrogels.
33031746	0	31	theme	von	32:34	arg1	Factor					47:52	von Willebrand Factor	32:52	von Willebrand Factor	32:52	Assembly Mechanism of Mucin and von Willebrand Factor Polymers.
33031746	9	32	theme	function	1138:1145	arg1	manipulation					1114:1125	rational manipulation	1105:1125	rational manipulation of barrier function and coagulation	1105:1161	The mucin assembly mechanism and its adaptation for hemostasis provide the foundation for rational manipulation of barrier function and coagulation.
33031746	3	33	from	layers	342:347	arg1	systems					366:372	these diverse systems	352:372	these diverse systems	352:372	Mucin glycoproteins and the related von Willebrand factor guard the vulnerable cell layers in these diverse systems.
33031746	5	34	theme	structural	467:476	arg1	analysis					478:485	an integrated structural analysis	453:485	an integrated structural analysis of the intestinal mucin MUC2	453:514	Here, we present an integrated structural analysis of the intestinal mucin MUC2.
33031746	3	35	theme	Mucin	258:262	arg1	glycoproteins					264:276	Mucin glycoproteins	258:276	Mucin glycoproteins	258:276	Mucin glycoproteins and the related von Willebrand factor guard the vulnerable cell layers in these diverse systems.
33031746	0	36	theme	Mucin	22:26	arg1	Mechanism					9:17	Assembly Mechanism	0:17	Assembly Mechanism of Mucin	0:26	Assembly Mechanism of Mucin and von Willebrand Factor Polymers.
33031746	0	36	theme	Mucin	22:26	arg1	Factor					47:52	von Willebrand Factor	32:52	von Willebrand Factor	32:52	Assembly Mechanism of Mucin and von Willebrand Factor Polymers.
33031746	8	37	from	role	1001:1004	arg1	MUC2					1009:1012	MUC2	1009:1012	MUC2	1009:1012	Remarkably, a densely O-glycosylated mucin domain performs an organizational role in MUC2.
33031746	3	38	theme	von	294:296	arg1	factor					309:314	the related von Willebrand factor	282:314	the related von Willebrand factor	282:314	Mucin glycoproteins and the related von Willebrand factor guard the vulnerable cell layers in these diverse systems.
33031746	0	39	theme	Willebrand	36:45	arg1	Factor					47:52	von Willebrand Factor	32:52	von Willebrand Factor	32:52	Assembly Mechanism of Mucin and von Willebrand Factor Polymers.
33031746	3	40	theme	Willebrand	298:307	arg1	factor					309:314	the related von Willebrand factor	282:314	the related von Willebrand factor	282:314	Mucin glycoproteins and the related von Willebrand factor guard the vulnerable cell layers in these diverse systems.
33031746	8	41	theme	organizational	986:999	arg1	role					1001:1004	an organizational role	983:1004	an organizational role in MUC2	983:1012	Remarkably, a densely O-glycosylated mucin domain performs an organizational role in MUC2.
33031746	6	42	theme	intestinal	653:662	arg1	barrier					672:678	the intestinal mucosal barrier	649:678	the intestinal mucosal barrier	649:678	Our findings reveal the shared mechanism by which complex macromolecules responsible for blood clotting, mucociliary clearance, and the intestinal mucosal barrier form protective polymers and hydrogels.
33031746	7	43	theme	disulfide-rich	791:804	arg1	bridges					806:812	disulfide-rich bridges	791:812	disulfide-rich bridges	791:812	Specifically, cryo-electron microscopy and crystal structures show how disulfide-rich bridges and pH-tunable interfaces control successive assembly steps in the endoplasmic reticulum and Golgi apparatus.
33031746	8	44	gly	O-glycosylated	946:959	arg1	domain					967:972	a densely O-glycosylated mucin domain	936:972	a densely O-glycosylated mucin domain	936:972	Remarkably, a densely O-glycosylated mucin domain performs an organizational role in MUC2.
33031746	7	45	from	steps	868:872	arg1	reticulum					893:901	the endoplasmic reticulum	877:901	the endoplasmic reticulum	877:901	Specifically, cryo-electron microscopy and crystal structures show how disulfide-rich bridges and pH-tunable interfaces control successive assembly steps in the endoplasmic reticulum and Golgi apparatus.
33031746	7	45	from	steps	868:872	arg1	apparatus					913:921	Golgi apparatus	907:921	Golgi apparatus	907:921	Specifically, cryo-electron microscopy and crystal structures show how disulfide-rich bridges and pH-tunable interfaces control successive assembly steps in the endoplasmic reticulum and Golgi apparatus.
33031746	1	46	theme	physical	117:124	arg1	hazards					141:147	physical and biological hazards	117:147	physical and biological hazards accompanying the intake of air and food	117:187	The respiratory and intestinal tracts are exposed to physical and biological hazards accompanying the intake of air and food.
33031746	3	47	theme	related	286:292	arg1	factor					309:314	the related von Willebrand factor	282:314	the related von Willebrand factor	282:314	Mucin glycoproteins and the related von Willebrand factor guard the vulnerable cell layers in these diverse systems.
33031746	5	48	theme	mucin	505:509	arg1	MUC2					511:514	the intestinal mucin MUC2	490:514	the intestinal mucin MUC2	490:514	Here, we present an integrated structural analysis of the intestinal mucin MUC2.
33031746	6	49	theme	shared	541:546	arg1	mechanism					548:556	the shared mechanism	537:556	the shared mechanism by which complex macromolecules responsible for blood clotting, mucociliary clearance, and the intestinal mucosal barrier form protective polymers and hydrogels	537:717	Our findings reveal the shared mechanism by which complex macromolecules responsible for blood clotting, mucociliary clearance, and the intestinal mucosal barrier form protective polymers and hydrogels.
33031746	4	50	theme	gut	420:422	arg1	microbiome					424:433	the gut microbiome	416:433	the gut microbiome	416:433	Colon mucins additionally house and feed the gut microbiome.
33031746	5	51	theme	MUC2	511:514	arg1	analysis					478:485	an integrated structural analysis	453:485	an integrated structural analysis of the intestinal mucin MUC2	453:514	Here, we present an integrated structural analysis of the intestinal mucin MUC2.
33031746	1	52	theme	biological	130:139	arg1	hazards					141:147	physical and biological hazards	117:147	physical and biological hazards accompanying the intake of air and food	117:187	The respiratory and intestinal tracts are exposed to physical and biological hazards accompanying the intake of air and food.
33031746	3	53	theme	vulnerable	326:335	arg1	layers					342:347	the vulnerable cell layers	322:347	the vulnerable cell layers in these diverse systems	322:372	Mucin glycoproteins and the related von Willebrand factor guard the vulnerable cell layers in these diverse systems.
33031746	7	54	theme	crystal	763:769	arg1	structures					771:780	crystal structures	763:780	crystal structures	763:780	Specifically, cryo-electron microscopy and crystal structures show how disulfide-rich bridges and pH-tunable interfaces control successive assembly steps in the endoplasmic reticulum and Golgi apparatus.
20427285	6	0	dep	residues	830:837	arg1	residues					830:837	ZPI residues Glu-313 and Glu-383	826:857	ZPI residues Glu-313 and Glu-383	826:857	Modeling of the ternary Michaelis complex implicated ZPI residues Glu-313 and Glu-383 in fXa binding.
20427285	6	0	dep	residues	830:837	arg1	Glu-383					851:857	Glu-383	851:857	Glu-383	851:857	Modeling of the ternary Michaelis complex implicated ZPI residues Glu-313 and Glu-383 in fXa binding.
20427285	6	0	dep	residues	830:837	arg1	Glu-313					839:845	Glu-313	839:845	Glu-313	839:845	Modeling of the ternary Michaelis complex implicated ZPI residues Glu-313 and Glu-383 in fXa binding.
20427285	6	1	theme	ZPI	826:828	arg1	residues					830:837	ZPI residues Glu-313 and Glu-383	826:857	ZPI residues Glu-313 and Glu-383	826:857	Modeling of the ternary Michaelis complex implicated ZPI residues Glu-313 and Glu-383 in fXa binding.
20427285	6	1	theme	ZPI	826:828	arg1	Glu-383					851:857	Glu-383	851:857	Glu-383	851:857	Modeling of the ternary Michaelis complex implicated ZPI residues Glu-313 and Glu-383 in fXa binding.
20427285	6	1	theme	ZPI	826:828	arg1	Glu-313					839:845	Glu-313	839:845	Glu-313	839:845	Modeling of the ternary Michaelis complex implicated ZPI residues Glu-313 and Glu-383 in fXa binding.
20427285	9	2	dep	together	1199:1206	arg1	with					1208:1211	with	1208:1211	with	1208:1211	Instead, template bridging from membrane association, together with previously demonstrated interaction of the fXa and ZPI Gla domains, resulted in an additional approximately 1000-fold rate enhancement.
20427285	3	3	theme	PZ	481:482	arg1	structure					453:461	the x-ray structure	443:461	the x-ray structure of Gla-domainless PZ (PZ(DeltaGD)) complexed with protein Z-dependent proteinase inhibitor (ZPI)	443:558	To elucidate the role of PZ, we determined the x-ray structure of Gla-domainless PZ (PZ(DeltaGD)) complexed with protein Z-dependent proteinase inhibitor (ZPI).
20427285	1	4	theme	factor	239:244	arg1	fXa					250:252	fXa	250:252	fXa	250:252	The serpin ZPI is a protein Z (PZ)-dependent specific inhibitor of membrane-associated factor Xa (fXa) despite having an unfavorable P1 Tyr.
20427285	1	4	theme	factor	239:244	arg1	Xa					246:247	membrane-associated factor Xa	219:247	membrane-associated factor Xa (fXa)	219:253	The serpin ZPI is a protein Z (PZ)-dependent specific inhibitor of membrane-associated factor Xa (fXa) despite having an unfavorable P1 Tyr.
20427285	6	5	theme	complex	807:813	arg1	Modeling					773:780	Modeling	773:780	Modeling of the ternary Michaelis complex	773:813	Modeling of the ternary Michaelis complex implicated ZPI residues Glu-313 and Glu-383 in fXa binding.
20427285	4	6	theme	PZ	565:566	arg1	domain					584:589	The PZ pseudocatalytic domain	561:589	The PZ pseudocatalytic domain	561:589	The PZ pseudocatalytic domain bound ZPI at a novel site through ionic and polar interactions.
20427285	10	7	theme	P1	1375:1376	arg1	tyrosine					1378:1385	P1 tyrosine	1375:1385	P1 tyrosine	1375:1385	To understand why ZPI has P1 tyrosine, we examined a P1 Arg variant.
20427285	1	8	theme	serpin	156:161	arg1	ZPI					163:165	The serpin ZPI	152:165	The serpin ZPI	152:165	The serpin ZPI is a protein Z (PZ)-dependent specific inhibitor of membrane-associated factor Xa (fXa) despite having an unfavorable P1 Tyr.
20427285	1	8	theme	serpin	156:161	arg1	inhibitor					206:214	a protein Z (PZ)-dependent specific inhibitor	170:214	a protein Z (PZ)-dependent specific inhibitor of membrane-associated factor Xa (fXa)	170:253	The serpin ZPI is a protein Z (PZ)-dependent specific inhibitor of membrane-associated factor Xa (fXa) despite having an unfavorable P1 Tyr.
20427285	8	9	theme	rate	1127:1130	arg1	enhancement					1132:1142	rate enhancement	1127:1142	rate enhancement	1127:1142	Limited conformational change in ZPI resulted from PZ binding, which contributed only approximately 2-fold to rate enhancement.
20427285	6	10	theme	ternary	789:795	arg1	complex					807:813	the ternary Michaelis complex	785:813	the ternary Michaelis complex	785:813	Modeling of the ternary Michaelis complex implicated ZPI residues Glu-313 and Glu-383 in fXa binding.
20427285	0	11	theme	membrane-associated	121:139	arg1	Xa					148:149	membrane-associated factor Xa	121:149	membrane-associated factor Xa	121:149	Basis for the specificity and activation of the serpin protein Z-dependent proteinase inhibitor (ZPI) as an inhibitor of membrane-associated factor Xa.
20427285	12	12	theme	high	1892:1895	arg1	rate					1897:1900	a high rate	1890:1900	a high rate of reaction as an inhibitor	1890:1928	P1 tyrosine thus ensures that reaction with fXa or most other arginine-specific proteinases is insignificant unless PZ binds and localizes ZPI and fXa on the membrane, where the combined effects of Gla-Gla interaction, template bridging, and interaction of fXa with Glu-313 overcome the unfavorability of P1 Tyr and ensure a high rate of reaction as an inhibitor.
20427285	7	13	theme	inhibition	1005:1014	arg1	acceleration					976:987	rate acceleration	971:987	rate acceleration of fXa and fXIa inhibition	971:1014	Mutagenesis established that only Glu-313 is important, contributing approximately 5-10-fold to rate acceleration of fXa and fXIa inhibition.
20427285	5	14	theme	inhibition	761:770	arg1	acceleration					741:752	membrane-dependent PZ acceleration	719:752	membrane-dependent PZ acceleration of fXa inhibition	719:770	Mutation of four ZPI contact residues eliminated PZ binding and membrane-dependent PZ acceleration of fXa inhibition.
20427285	5	14	theme	inhibition	761:770	arg1	binding					707:713	PZ binding	704:713	PZ binding	704:713	Mutation of four ZPI contact residues eliminated PZ binding and membrane-dependent PZ acceleration of fXa inhibition.
20427285	12	15	theme	Tyr	1875:1877	arg1	unfavorability					1854:1867	the unfavorability	1850:1867	the unfavorability of P1 Tyr	1850:1877	P1 tyrosine thus ensures that reaction with fXa or most other arginine-specific proteinases is insignificant unless PZ binds and localizes ZPI and fXa on the membrane, where the combined effects of Gla-Gla interaction, template bridging, and interaction of fXa with Glu-313 overcome the unfavorability of P1 Tyr and ensure a high rate of reaction as an inhibitor.
20427285	8	16	theme	Limited	1017:1023	arg1	change					1040:1045	Limited conformational change	1017:1045	Limited conformational change in ZPI	1017:1052	Limited conformational change in ZPI resulted from PZ binding, which contributed only approximately 2-fold to rate enhancement.
20427285	12	17	theme	arginine-specific	1629:1645	arg1	proteinases					1647:1657	most other arginine-specific proteinases	1618:1657	most other arginine-specific proteinases	1618:1657	P1 tyrosine thus ensures that reaction with fXa or most other arginine-specific proteinases is insignificant unless PZ binds and localizes ZPI and fXa on the membrane, where the combined effects of Gla-Gla interaction, template bridging, and interaction of fXa with Glu-313 overcome the unfavorability of P1 Tyr and ensure a high rate of reaction as an inhibitor.
20427285	4	18	theme	ionic	625:629	arg1	interactions					641:652	ionic and polar interactions	625:652	ionic and polar interactions	625:652	The PZ pseudocatalytic domain bound ZPI at a novel site through ionic and polar interactions.
20427285	12	19	dep	PZ	1683:1684	arg1	localizes					1696:1704	localizes	1696:1704	localizes ZPI and fXa on the membrane, where the combined effects of Gla-Gla interaction, template bridging, and interaction of fXa with Glu-313 overcome the unfavorability of P1 Tyr and ensure a high rate of reaction as an inhibitor	1696:1928	P1 tyrosine thus ensures that reaction with fXa or most other arginine-specific proteinases is insignificant unless PZ binds and localizes ZPI and fXa on the membrane, where the combined effects of Gla-Gla interaction, template bridging, and interaction of fXa with Glu-313 overcome the unfavorability of P1 Tyr and ensure a high rate of reaction as an inhibitor.
20427285	12	19	dep	PZ	1683:1684	arg1	binds					1686:1690	binds	1686:1690	binds	1686:1690	P1 tyrosine thus ensures that reaction with fXa or most other arginine-specific proteinases is insignificant unless PZ binds and localizes ZPI and fXa on the membrane, where the combined effects of Gla-Gla interaction, template bridging, and interaction of fXa with Glu-313 overcome the unfavorability of P1 Tyr and ensure a high rate of reaction as an inhibitor.
20427285	7	20	theme	rate	971:974	arg1	acceleration					976:987	rate acceleration	971:987	rate acceleration of fXa and fXIa inhibition	971:1014	Mutagenesis established that only Glu-313 is important, contributing approximately 5-10-fold to rate acceleration of fXa and fXIa inhibition.
20427285	10	21	contain	has	1371:1373	arg1	ZPI					1367:1369	ZPI	1367:1369	ZPI	1367:1369	To understand why ZPI has P1 tyrosine, we examined a P1 Arg variant.
20427285	10	21	contain	has	1371:1373	arg2	tyrosine					1378:1385	P1 tyrosine	1375:1385	P1 tyrosine	1375:1385	To understand why ZPI has P1 tyrosine, we examined a P1 Arg variant.
20427285	1	22	theme	P1	285:286	arg1	Tyr					288:290	an unfavorable P1 Tyr	270:290	an unfavorable P1 Tyr	270:290	The serpin ZPI is a protein Z (PZ)-dependent specific inhibitor of membrane-associated factor Xa (fXa) despite having an unfavorable P1 Tyr.
20427285	3	23	theme	Z-dependent	521:531	arg1	ZPI					555:557	ZPI	555:557	ZPI	555:557	To elucidate the role of PZ, we determined the x-ray structure of Gla-domainless PZ (PZ(DeltaGD)) complexed with protein Z-dependent proteinase inhibitor (ZPI).
20427285	3	23	theme	Z-dependent	521:531	arg1	inhibitor					544:552	protein Z-dependent proteinase inhibitor	513:552	protein Z-dependent proteinase inhibitor (ZPI)	513:558	To elucidate the role of PZ, we determined the x-ray structure of Gla-domainless PZ (PZ(DeltaGD)) complexed with protein Z-dependent proteinase inhibitor (ZPI).
20427285	0	24	theme	Xa	148:149	arg1	inhibitor					108:116	an inhibitor	105:116	an inhibitor of membrane-associated factor Xa	105:149	Basis for the specificity and activation of the serpin protein Z-dependent proteinase inhibitor (ZPI) as an inhibitor of membrane-associated factor Xa.
20427285	0	25	theme	Z-dependent	63:73	arg1	ZPI					97:99	ZPI	97:99	ZPI	97:99	Basis for the specificity and activation of the serpin protein Z-dependent proteinase inhibitor (ZPI) as an inhibitor of membrane-associated factor Xa.
20427285	0	25	theme	Z-dependent	63:73	arg1	inhibitor					86:94	the serpin protein Z-dependent proteinase inhibitor	44:94	the serpin protein Z-dependent proteinase inhibitor (ZPI)	44:100	Basis for the specificity and activation of the serpin protein Z-dependent proteinase inhibitor (ZPI) as an inhibitor of membrane-associated factor Xa.
20427285	12	26	theme	most	1618:1621	arg1	proteinases					1647:1657	most other arginine-specific proteinases	1618:1657	most other arginine-specific proteinases	1618:1657	P1 tyrosine thus ensures that reaction with fXa or most other arginine-specific proteinases is insignificant unless PZ binds and localizes ZPI and fXa on the membrane, where the combined effects of Gla-Gla interaction, template bridging, and interaction of fXa with Glu-313 overcome the unfavorability of P1 Tyr and ensure a high rate of reaction as an inhibitor.
20427285	11	27	theme	diffusion-limited	1436:1452	arg1	rate					1454:1457	a diffusion-limited rate	1434:1457	a diffusion-limited rate with fXa	1434:1466	This reacted at a diffusion-limited rate with fXa, even without PZ, and predominantly as substrate, reflecting both rapid acylation and deacylation.
20427285	0	28	theme	inhibitor	86:94	arg1	activation					30:39	activation	30:39	activation	30:39	Basis for the specificity and activation of the serpin protein Z-dependent proteinase inhibitor (ZPI) as an inhibitor of membrane-associated factor Xa.
20427285	0	28	theme	inhibitor	86:94	arg1	specificity					14:24	specificity	14:24	specificity	14:24	Basis for the specificity and activation of the serpin protein Z-dependent proteinase inhibitor (ZPI) as an inhibitor of membrane-associated factor Xa.
20427285	9	29	theme	Gla	1268:1270	arg1	domains					1272:1278	ZPI Gla domains	1264:1278	ZPI Gla domains	1264:1278	Instead, template bridging from membrane association, together with previously demonstrated interaction of the fXa and ZPI Gla domains, resulted in an additional approximately 1000-fold rate enhancement.
20427285	10	30	theme	P1	1402:1403	arg1	variant					1409:1415	a P1 Arg variant	1400:1415	a P1 Arg variant	1400:1415	To understand why ZPI has P1 tyrosine, we examined a P1 Arg variant.
20427285	4	31	theme	polar	635:639	arg1	interactions					641:652	ionic and polar interactions	625:652	ionic and polar interactions	625:652	The PZ pseudocatalytic domain bound ZPI at a novel site through ionic and polar interactions.
20427285	1	32	theme	Xa	246:247	arg1	ZPI					163:165	The serpin ZPI	152:165	The serpin ZPI	152:165	The serpin ZPI is a protein Z (PZ)-dependent specific inhibitor of membrane-associated factor Xa (fXa) despite having an unfavorable P1 Tyr.
20427285	1	32	theme	Xa	246:247	arg1	inhibitor					206:214	a protein Z (PZ)-dependent specific inhibitor	170:214	a protein Z (PZ)-dependent specific inhibitor of membrane-associated factor Xa (fXa)	170:253	The serpin ZPI is a protein Z (PZ)-dependent specific inhibitor of membrane-associated factor Xa (fXa) despite having an unfavorable P1 Tyr.
20427285	9	33	dep	fXa	1256:1258	arg1	the					1252:1254	the	1252:1254	the	1252:1254	Instead, template bridging from membrane association, together with previously demonstrated interaction of the fXa and ZPI Gla domains, resulted in an additional approximately 1000-fold rate enhancement.
20427285	5	34	theme	PZ	738:739	arg1	acceleration					741:752	membrane-dependent PZ acceleration	719:752	membrane-dependent PZ acceleration of fXa inhibition	719:770	Mutation of four ZPI contact residues eliminated PZ binding and membrane-dependent PZ acceleration of fXa inhibition.
20427285	5	35	theme	residues	684:691	arg1	Mutation					655:662	Mutation	655:662	Mutation of four ZPI contact residues	655:691	Mutation of four ZPI contact residues eliminated PZ binding and membrane-dependent PZ acceleration of fXa inhibition.
20427285	9	36	theme	additional	1296:1305	arg1	enhancement					1336:1346	an additional approximately 1000-fold rate enhancement	1293:1346	an additional approximately 1000-fold rate enhancement	1293:1346	Instead, template bridging from membrane association, together with previously demonstrated interaction of the fXa and ZPI Gla domains, resulted in an additional approximately 1000-fold rate enhancement.
20427285	12	37	theme	bridging	1795:1802	arg1	template					1786:1793	template bridging	1786:1802	template bridging	1786:1802	P1 tyrosine thus ensures that reaction with fXa or most other arginine-specific proteinases is insignificant unless PZ binds and localizes ZPI and fXa on the membrane, where the combined effects of Gla-Gla interaction, template bridging, and interaction of fXa with Glu-313 overcome the unfavorability of P1 Tyr and ensure a high rate of reaction as an inhibitor.
20427285	12	38	theme	reaction	1905:1912	arg1	rate					1897:1900	a high rate	1890:1900	a high rate of reaction as an inhibitor	1890:1928	P1 tyrosine thus ensures that reaction with fXa or most other arginine-specific proteinases is insignificant unless PZ binds and localizes ZPI and fXa on the membrane, where the combined effects of Gla-Gla interaction, template bridging, and interaction of fXa with Glu-313 overcome the unfavorability of P1 Tyr and ensure a high rate of reaction as an inhibitor.
20427285	0	39	theme	serpin	48:53	arg1	ZPI					97:99	ZPI	97:99	ZPI	97:99	Basis for the specificity and activation of the serpin protein Z-dependent proteinase inhibitor (ZPI) as an inhibitor of membrane-associated factor Xa.
20427285	0	39	theme	serpin	48:53	arg1	inhibitor					86:94	the serpin protein Z-dependent proteinase inhibitor	44:94	the serpin protein Z-dependent proteinase inhibitor (ZPI)	44:100	Basis for the specificity and activation of the serpin protein Z-dependent proteinase inhibitor (ZPI) as an inhibitor of membrane-associated factor Xa.
20427285	3	40	theme	PZ	425:426	arg1	role					417:420	the role	413:420	the role of PZ	413:426	To elucidate the role of PZ, we determined the x-ray structure of Gla-domainless PZ (PZ(DeltaGD)) complexed with protein Z-dependent proteinase inhibitor (ZPI).
20427285	8	41	theme	conformational	1025:1038	arg1	change					1040:1045	Limited conformational change	1017:1045	Limited conformational change in ZPI	1017:1052	Limited conformational change in ZPI resulted from PZ binding, which contributed only approximately 2-fold to rate enhancement.
20427285	9	42	theme	1000-fold	1321:1329	arg1	enhancement					1336:1346	an additional approximately 1000-fold rate enhancement	1293:1346	an additional approximately 1000-fold rate enhancement	1293:1346	Instead, template bridging from membrane association, together with previously demonstrated interaction of the fXa and ZPI Gla domains, resulted in an additional approximately 1000-fold rate enhancement.
20427285	12	43	theme	combined	1745:1752	arg1	effects					1754:1760	the combined effects	1741:1760	the combined effects of Gla-Gla interaction, template bridging, and interaction of fXa with Glu-313	1741:1839	P1 tyrosine thus ensures that reaction with fXa or most other arginine-specific proteinases is insignificant unless PZ binds and localizes ZPI and fXa on the membrane, where the combined effects of Gla-Gla interaction, template bridging, and interaction of fXa with Glu-313 overcome the unfavorability of P1 Tyr and ensure a high rate of reaction as an inhibitor.
20427285	12	44	theme	Gla-Gla	1765:1771	arg1	interaction					1773:1783	Gla-Gla interaction	1765:1783	Gla-Gla interaction	1765:1783	P1 tyrosine thus ensures that reaction with fXa or most other arginine-specific proteinases is insignificant unless PZ binds and localizes ZPI and fXa on the membrane, where the combined effects of Gla-Gla interaction, template bridging, and interaction of fXa with Glu-313 overcome the unfavorability of P1 Tyr and ensure a high rate of reaction as an inhibitor.
20427285	1	45	theme	-dependent	186:195	arg1	ZPI					163:165	The serpin ZPI	152:165	The serpin ZPI	152:165	The serpin ZPI is a protein Z (PZ)-dependent specific inhibitor of membrane-associated factor Xa (fXa) despite having an unfavorable P1 Tyr.
20427285	1	45	theme	-dependent	186:195	arg1	inhibitor					206:214	a protein Z (PZ)-dependent specific inhibitor	170:214	a protein Z (PZ)-dependent specific inhibitor of membrane-associated factor Xa (fXa)	170:253	The serpin ZPI is a protein Z (PZ)-dependent specific inhibitor of membrane-associated factor Xa (fXa) despite having an unfavorable P1 Tyr.
20427285	8	46	theme	PZ	1068:1069	arg1	binding					1071:1077	PZ binding	1068:1077	PZ binding	1068:1077	Limited conformational change in ZPI resulted from PZ binding, which contributed only approximately 2-fold to rate enhancement.
20427285	11	47	theme	rapid	1534:1538	arg1	acylation					1540:1548	rapid acylation	1534:1548	rapid acylation	1534:1548	This reacted at a diffusion-limited rate with fXa, even without PZ, and predominantly as substrate, reflecting both rapid acylation and deacylation.
20427285	12	48	with	interaction	1773:1783	arg1	Glu-313					1833:1839	Glu-313	1833:1839	Glu-313	1833:1839	P1 tyrosine thus ensures that reaction with fXa or most other arginine-specific proteinases is insignificant unless PZ binds and localizes ZPI and fXa on the membrane, where the combined effects of Gla-Gla interaction, template bridging, and interaction of fXa with Glu-313 overcome the unfavorability of P1 Tyr and ensure a high rate of reaction as an inhibitor.
20427285	1	49	theme	membrane-associated	219:237	arg1	fXa					250:252	fXa	250:252	fXa	250:252	The serpin ZPI is a protein Z (PZ)-dependent specific inhibitor of membrane-associated factor Xa (fXa) despite having an unfavorable P1 Tyr.
20427285	1	49	theme	membrane-associated	219:237	arg1	Xa					246:247	membrane-associated factor Xa	219:247	membrane-associated factor Xa (fXa)	219:253	The serpin ZPI is a protein Z (PZ)-dependent specific inhibitor of membrane-associated factor Xa (fXa) despite having an unfavorable P1 Tyr.
20427285	5	50	theme	PZ	704:705	arg1	binding					707:713	PZ binding	704:713	PZ binding	704:713	Mutation of four ZPI contact residues eliminated PZ binding and membrane-dependent PZ acceleration of fXa inhibition.
20427285	6	51	theme	Michaelis	797:805	arg1	complex					807:813	the ternary Michaelis complex	785:813	the ternary Michaelis complex	785:813	Modeling of the ternary Michaelis complex implicated ZPI residues Glu-313 and Glu-383 in fXa binding.
20427285	12	52	with	interaction	1809:1819	arg1	Glu-313					1833:1839	Glu-313	1833:1839	Glu-313	1833:1839	P1 tyrosine thus ensures that reaction with fXa or most other arginine-specific proteinases is insignificant unless PZ binds and localizes ZPI and fXa on the membrane, where the combined effects of Gla-Gla interaction, template bridging, and interaction of fXa with Glu-313 overcome the unfavorability of P1 Tyr and ensure a high rate of reaction as an inhibitor.
20427285	5	53	theme	ZPI	672:674	arg1	residues					684:691	four ZPI contact residues	667:691	four ZPI contact residues	667:691	Mutation of four ZPI contact residues eliminated PZ binding and membrane-dependent PZ acceleration of fXa inhibition.
20427285	4	54	theme	pseudocatalytic	568:582	arg1	domain					584:589	The PZ pseudocatalytic domain	561:589	The PZ pseudocatalytic domain	561:589	The PZ pseudocatalytic domain bound ZPI at a novel site through ionic and polar interactions.
20427285	7	55	theme	fXIa	1000:1003	arg1	inhibition					1005:1014	fXIa inhibition	1000:1014	fXIa inhibition	1000:1014	Mutagenesis established that only Glu-313 is important, contributing approximately 5-10-fold to rate acceleration of fXa and fXIa inhibition.
20427285	1	56	dep	-dependent	186:195	arg1	PZ					183:184	PZ	183:184	PZ	183:184	The serpin ZPI is a protein Z (PZ)-dependent specific inhibitor of membrane-associated factor Xa (fXa) despite having an unfavorable P1 Tyr.
20427285	7	57	theme	fXa	992:994	arg1	acceleration					976:987	rate acceleration	971:987	rate acceleration of fXa and fXIa inhibition	971:1014	Mutagenesis established that only Glu-313 is important, contributing approximately 5-10-fold to rate acceleration of fXa and fXIa inhibition.
20427285	9	58	theme	membrane	1177:1184	arg1	association					1186:1196	membrane association	1177:1196	membrane association	1177:1196	Instead, template bridging from membrane association, together with previously demonstrated interaction of the fXa and ZPI Gla domains, resulted in an additional approximately 1000-fold rate enhancement.
20427285	5	59	theme	fXa	757:759	arg1	inhibition					761:770	fXa inhibition	757:770	fXa inhibition	757:770	Mutation of four ZPI contact residues eliminated PZ binding and membrane-dependent PZ acceleration of fXa inhibition.
20427285	1	60	theme	unfavorable	273:283	arg1	Tyr					288:290	an unfavorable P1 Tyr	270:290	an unfavorable P1 Tyr	270:290	The serpin ZPI is a protein Z (PZ)-dependent specific inhibitor of membrane-associated factor Xa (fXa) despite having an unfavorable P1 Tyr.
20427285	0	61	theme	factor	141:146	arg1	Xa					148:149	membrane-associated factor Xa	121:149	membrane-associated factor Xa	121:149	Basis for the specificity and activation of the serpin protein Z-dependent proteinase inhibitor (ZPI) as an inhibitor of membrane-associated factor Xa.
20427285	12	62	theme	P1	1872:1873	arg1	Tyr					1875:1877	P1 Tyr	1872:1877	P1 Tyr	1872:1877	P1 tyrosine thus ensures that reaction with fXa or most other arginine-specific proteinases is insignificant unless PZ binds and localizes ZPI and fXa on the membrane, where the combined effects of Gla-Gla interaction, template bridging, and interaction of fXa with Glu-313 overcome the unfavorability of P1 Tyr and ensure a high rate of reaction as an inhibitor.
20427285	4	63	theme	novel	606:610	arg1	site					612:615	a novel site	604:615	a novel site through ionic and polar interactions	604:652	The PZ pseudocatalytic domain bound ZPI at a novel site through ionic and polar interactions.
20427285	3	64	theme	proteinase	533:542	arg1	ZPI					555:557	ZPI	555:557	ZPI	555:557	To elucidate the role of PZ, we determined the x-ray structure of Gla-domainless PZ (PZ(DeltaGD)) complexed with protein Z-dependent proteinase inhibitor (ZPI).
20427285	3	64	theme	proteinase	533:542	arg1	inhibitor					544:552	protein Z-dependent proteinase inhibitor	513:552	protein Z-dependent proteinase inhibitor (ZPI)	513:558	To elucidate the role of PZ, we determined the x-ray structure of Gla-domainless PZ (PZ(DeltaGD)) complexed with protein Z-dependent proteinase inhibitor (ZPI).
20427285	12	65	theme	other	1623:1627	arg1	proteinases					1647:1657	most other arginine-specific proteinases	1618:1657	most other arginine-specific proteinases	1618:1657	P1 tyrosine thus ensures that reaction with fXa or most other arginine-specific proteinases is insignificant unless PZ binds and localizes ZPI and fXa on the membrane, where the combined effects of Gla-Gla interaction, template bridging, and interaction of fXa with Glu-313 overcome the unfavorability of P1 Tyr and ensure a high rate of reaction as an inhibitor.
20427285	8	66	from	change	1040:1045	arg1	ZPI					1050:1052	ZPI	1050:1052	ZPI	1050:1052	Limited conformational change in ZPI resulted from PZ binding, which contributed only approximately 2-fold to rate enhancement.
20427285	0	67	theme	protein	55:61	arg1	ZPI					97:99	ZPI	97:99	ZPI	97:99	Basis for the specificity and activation of the serpin protein Z-dependent proteinase inhibitor (ZPI) as an inhibitor of membrane-associated factor Xa.
20427285	0	67	theme	protein	55:61	arg1	inhibitor					86:94	the serpin protein Z-dependent proteinase inhibitor	44:94	the serpin protein Z-dependent proteinase inhibitor (ZPI)	44:100	Basis for the specificity and activation of the serpin protein Z-dependent proteinase inhibitor (ZPI) as an inhibitor of membrane-associated factor Xa.
20427285	9	68	theme	demonstrated	1224:1235	arg1	interaction					1237:1247	previously demonstrated interaction	1213:1247	previously demonstrated interaction of the fXa and ZPI Gla domains	1213:1278	Instead, template bridging from membrane association, together with previously demonstrated interaction of the fXa and ZPI Gla domains, resulted in an additional approximately 1000-fold rate enhancement.
20427285	3	69	theme	protein	513:519	arg1	ZPI					555:557	ZPI	555:557	ZPI	555:557	To elucidate the role of PZ, we determined the x-ray structure of Gla-domainless PZ (PZ(DeltaGD)) complexed with protein Z-dependent proteinase inhibitor (ZPI).
20427285	3	69	theme	protein	513:519	arg1	inhibitor					544:552	protein Z-dependent proteinase inhibitor	513:552	protein Z-dependent proteinase inhibitor (ZPI)	513:558	To elucidate the role of PZ, we determined the x-ray structure of Gla-domainless PZ (PZ(DeltaGD)) complexed with protein Z-dependent proteinase inhibitor (ZPI).
20427285	0	70	theme	proteinase	75:84	arg1	ZPI					97:99	ZPI	97:99	ZPI	97:99	Basis for the specificity and activation of the serpin protein Z-dependent proteinase inhibitor (ZPI) as an inhibitor of membrane-associated factor Xa.
20427285	0	70	theme	proteinase	75:84	arg1	inhibitor					86:94	the serpin protein Z-dependent proteinase inhibitor	44:94	the serpin protein Z-dependent proteinase inhibitor (ZPI)	44:100	Basis for the specificity and activation of the serpin protein Z-dependent proteinase inhibitor (ZPI) as an inhibitor of membrane-associated factor Xa.
20427285	11	71	with	rate	1454:1457	arg1	fXa					1464:1466	fXa	1464:1466	fXa	1464:1466	This reacted at a diffusion-limited rate with fXa, even without PZ, and predominantly as substrate, reflecting both rapid acylation and deacylation.
20427285	9	72	theme	fXa	1256:1258	arg1	interaction					1237:1247	previously demonstrated interaction	1213:1247	previously demonstrated interaction of the fXa and ZPI Gla domains	1213:1278	Instead, template bridging from membrane association, together with previously demonstrated interaction of the fXa and ZPI Gla domains, resulted in an additional approximately 1000-fold rate enhancement.
20427285	9	73	theme	ZPI	1264:1266	arg1	domains					1272:1278	ZPI Gla domains	1264:1278	ZPI Gla domains	1264:1278	Instead, template bridging from membrane association, together with previously demonstrated interaction of the fXa and ZPI Gla domains, resulted in an additional approximately 1000-fold rate enhancement.
20427285	12	74	theme	interaction	1809:1819	arg1	effects					1754:1760	the combined effects	1741:1760	the combined effects of Gla-Gla interaction, template bridging, and interaction of fXa with Glu-313	1741:1839	P1 tyrosine thus ensures that reaction with fXa or most other arginine-specific proteinases is insignificant unless PZ binds and localizes ZPI and fXa on the membrane, where the combined effects of Gla-Gla interaction, template bridging, and interaction of fXa with Glu-313 overcome the unfavorability of P1 Tyr and ensure a high rate of reaction as an inhibitor.
20427285	10	75	theme	Arg	1405:1407	arg1	variant					1409:1415	a P1 Arg variant	1400:1415	a P1 Arg variant	1400:1415	To understand why ZPI has P1 tyrosine, we examined a P1 Arg variant.
20427285	9	76	theme	domains	1272:1278	arg1	interaction					1237:1247	previously demonstrated interaction	1213:1247	previously demonstrated interaction of the fXa and ZPI Gla domains	1213:1278	Instead, template bridging from membrane association, together with previously demonstrated interaction of the fXa and ZPI Gla domains, resulted in an additional approximately 1000-fold rate enhancement.
20427285	12	77	theme	fXa	1824:1826	arg1	template					1786:1793	template bridging	1786:1802	template bridging	1786:1802	P1 tyrosine thus ensures that reaction with fXa or most other arginine-specific proteinases is insignificant unless PZ binds and localizes ZPI and fXa on the membrane, where the combined effects of Gla-Gla interaction, template bridging, and interaction of fXa with Glu-313 overcome the unfavorability of P1 Tyr and ensure a high rate of reaction as an inhibitor.
20427285	12	77	theme	fXa	1824:1826	arg1	interaction					1773:1783	Gla-Gla interaction	1765:1783	Gla-Gla interaction	1765:1783	P1 tyrosine thus ensures that reaction with fXa or most other arginine-specific proteinases is insignificant unless PZ binds and localizes ZPI and fXa on the membrane, where the combined effects of Gla-Gla interaction, template bridging, and interaction of fXa with Glu-313 overcome the unfavorability of P1 Tyr and ensure a high rate of reaction as an inhibitor.
20427285	12	77	theme	fXa	1824:1826	arg1	interaction					1809:1819	interaction	1809:1819	interaction	1809:1819	P1 tyrosine thus ensures that reaction with fXa or most other arginine-specific proteinases is insignificant unless PZ binds and localizes ZPI and fXa on the membrane, where the combined effects of Gla-Gla interaction, template bridging, and interaction of fXa with Glu-313 overcome the unfavorability of P1 Tyr and ensure a high rate of reaction as an inhibitor.
20427285	5	78	theme	membrane-dependent	719:736	arg1	acceleration					741:752	membrane-dependent PZ acceleration	719:752	membrane-dependent PZ acceleration of fXa inhibition	719:770	Mutation of four ZPI contact residues eliminated PZ binding and membrane-dependent PZ acceleration of fXa inhibition.
20427285	12	79	theme	template	1786:1793	arg1	effects					1754:1760	the combined effects	1741:1760	the combined effects of Gla-Gla interaction, template bridging, and interaction of fXa with Glu-313	1741:1839	P1 tyrosine thus ensures that reaction with fXa or most other arginine-specific proteinases is insignificant unless PZ binds and localizes ZPI and fXa on the membrane, where the combined effects of Gla-Gla interaction, template bridging, and interaction of fXa with Glu-313 overcome the unfavorability of P1 Tyr and ensure a high rate of reaction as an inhibitor.
20427285	5	80	theme	contact	676:682	arg1	residues					684:691	four ZPI contact residues	667:691	four ZPI contact residues	667:691	Mutation of four ZPI contact residues eliminated PZ binding and membrane-dependent PZ acceleration of fXa inhibition.
20427285	12	81	with	reaction	1597:1604	arg1	proteinases					1647:1657	most other arginine-specific proteinases	1618:1657	most other arginine-specific proteinases	1618:1657	P1 tyrosine thus ensures that reaction with fXa or most other arginine-specific proteinases is insignificant unless PZ binds and localizes ZPI and fXa on the membrane, where the combined effects of Gla-Gla interaction, template bridging, and interaction of fXa with Glu-313 overcome the unfavorability of P1 Tyr and ensure a high rate of reaction as an inhibitor.
20427285	12	81	with	reaction	1597:1604	arg1	fXa					1611:1613	fXa	1611:1613	fXa	1611:1613	P1 tyrosine thus ensures that reaction with fXa or most other arginine-specific proteinases is insignificant unless PZ binds and localizes ZPI and fXa on the membrane, where the combined effects of Gla-Gla interaction, template bridging, and interaction of fXa with Glu-313 overcome the unfavorability of P1 Tyr and ensure a high rate of reaction as an inhibitor.
20427285	12	82	theme	P1	1567:1568	arg1	tyrosine					1570:1577	P1 tyrosine	1567:1577	P1 tyrosine	1567:1577	P1 tyrosine thus ensures that reaction with fXa or most other arginine-specific proteinases is insignificant unless PZ binds and localizes ZPI and fXa on the membrane, where the combined effects of Gla-Gla interaction, template bridging, and interaction of fXa with Glu-313 overcome the unfavorability of P1 Tyr and ensure a high rate of reaction as an inhibitor.
20427285	12	83	with	template	1786:1793	arg1	Glu-313					1833:1839	Glu-313	1833:1839	Glu-313	1833:1839	P1 tyrosine thus ensures that reaction with fXa or most other arginine-specific proteinases is insignificant unless PZ binds and localizes ZPI and fXa on the membrane, where the combined effects of Gla-Gla interaction, template bridging, and interaction of fXa with Glu-313 overcome the unfavorability of P1 Tyr and ensure a high rate of reaction as an inhibitor.
20427285	2	84	dep	phospholipid	375:386	arg1	the					359:361	the	359:361	the	359:361	PZ accelerates the inhibition reaction approximately 2000-fold in the presence of phospholipid and Ca(2+).
20427285	2	84	dep	phospholipid	375:386	arg1	presence					363:370	presence	363:370	presence	363:370	PZ accelerates the inhibition reaction approximately 2000-fold in the presence of phospholipid and Ca(2+).
20427285	9	85	theme	rate	1331:1334	arg1	enhancement					1336:1346	an additional approximately 1000-fold rate enhancement	1293:1346	an additional approximately 1000-fold rate enhancement	1293:1346	Instead, template bridging from membrane association, together with previously demonstrated interaction of the fXa and ZPI Gla domains, resulted in an additional approximately 1000-fold rate enhancement.
20427285	12	86	theme	interaction	1773:1783	arg1	effects					1754:1760	the combined effects	1741:1760	the combined effects of Gla-Gla interaction, template bridging, and interaction of fXa with Glu-313	1741:1839	P1 tyrosine thus ensures that reaction with fXa or most other arginine-specific proteinases is insignificant unless PZ binds and localizes ZPI and fXa on the membrane, where the combined effects of Gla-Gla interaction, template bridging, and interaction of fXa with Glu-313 overcome the unfavorability of P1 Tyr and ensure a high rate of reaction as an inhibitor.
20427285	2	87	theme	inhibition	312:321	arg1	reaction					323:330	the inhibition reaction	308:330	the inhibition reaction	308:330	PZ accelerates the inhibition reaction approximately 2000-fold in the presence of phospholipid and Ca(2+).
20427285	3	88	theme	x-ray	447:451	arg1	structure					453:461	the x-ray structure	443:461	the x-ray structure of Gla-domainless PZ (PZ(DeltaGD)) complexed with protein Z-dependent proteinase inhibitor (ZPI)	443:558	To elucidate the role of PZ, we determined the x-ray structure of Gla-domainless PZ (PZ(DeltaGD)) complexed with protein Z-dependent proteinase inhibitor (ZPI).
20427285	1	89	theme	specific	197:204	arg1	ZPI					163:165	The serpin ZPI	152:165	The serpin ZPI	152:165	The serpin ZPI is a protein Z (PZ)-dependent specific inhibitor of membrane-associated factor Xa (fXa) despite having an unfavorable P1 Tyr.
20427285	1	89	theme	specific	197:204	arg1	inhibitor					206:214	a protein Z (PZ)-dependent specific inhibitor	170:214	a protein Z (PZ)-dependent specific inhibitor of membrane-associated factor Xa (fXa)	170:253	The serpin ZPI is a protein Z (PZ)-dependent specific inhibitor of membrane-associated factor Xa (fXa) despite having an unfavorable P1 Tyr.
35637289	4	0	theme	O-GlcNAc	489:496	arg1	sites					511:515	multiple O-GlcNAc modification sites	480:515	multiple O-GlcNAc modification sites for the endogenous SynGAP isolated from rat brain and the recombinantly expressed protein	480:605	We identified multiple O-GlcNAc modification sites for the endogenous SynGAP isolated from rat brain and the recombinantly expressed protein.
35637289	5	1	theme	O-GlcNAcylated	669:682	arg1	forms					684:688	site-specifically O-GlcNAcylated forms	651:688	site-specifically O-GlcNAcylated forms of SynGAP	651:698	Protein semisynthesis was used to generate site-specifically O-GlcNAcylated forms of SynGAP, and in vitro and cell-based LLPS assays demonstrated that T1306 O-GlcNAc of SynGAP blocks the interaction with PSD-95, thus inhibiting LLPS.
35637289	6	2	theme	dominant-negative	906:922	arg1	manner					924:929	a dominant-negative manner	904:929	a dominant-negative manner	904:929	Furthermore, O-GlcNAcylation suppresses SynGAP/PSD-95 LLPS in a dominant-negative manner, enabling sub-stoichiometric O-GlcNAcylation to exert effective regulation.
35637289	5	3	used	used	634:637	arg2	semisynthesis					616:628	Protein semisynthesis	608:628	Protein semisynthesis	608:628	Protein semisynthesis was used to generate site-specifically O-GlcNAcylated forms of SynGAP, and in vitro and cell-based LLPS assays demonstrated that T1306 O-GlcNAc of SynGAP blocks the interaction with PSD-95, thus inhibiting LLPS.
35637289	5	4	dep	in	705:706	arg1	vitro					708:712	vitro	708:712	vitro	708:712	Protein semisynthesis was used to generate site-specifically O-GlcNAcylated forms of SynGAP, and in vitro and cell-based LLPS assays demonstrated that T1306 O-GlcNAc of SynGAP blocks the interaction with PSD-95, thus inhibiting LLPS.
35637289	6	5	theme	sub-stoichiometric	941:958	arg1	O-GlcNAcylation					960:974	sub-stoichiometric O-GlcNAcylation	941:974	sub-stoichiometric O-GlcNAcylation	941:974	Furthermore, O-GlcNAcylation suppresses SynGAP/PSD-95 LLPS in a dominant-negative manner, enabling sub-stoichiometric O-GlcNAcylation to exert effective regulation.
35637289	7	6	theme	O-GlcNAc-dependent	1027:1044	arg1	LLPS					1046:1049	O-GlcNAc-dependent LLPS	1027:1049	O-GlcNAc-dependent LLPS	1027:1049	We also showed that O-GlcNAc-dependent LLPS is reversibly regulated by O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA).
35637289	5	7	theme	Protein	608:614	arg1	semisynthesis					616:628	Protein semisynthesis	608:628	Protein semisynthesis	608:628	Protein semisynthesis was used to generate site-specifically O-GlcNAcylated forms of SynGAP, and in vitro and cell-based LLPS assays demonstrated that T1306 O-GlcNAc of SynGAP blocks the interaction with PSD-95, thus inhibiting LLPS.
35637289	1	8	theme	Liquid-liquid	75:87	arg1	separation					95:104	Liquid-liquid phase separation	75:104	Liquid-liquid phase separation (LLPS) of SynGAP and PSD-95	75:132	Liquid-liquid phase separation (LLPS) of SynGAP and PSD-95, two abundant proteins that interact in the postsynaptic density (PSD) of neurons, has been implicated in modulating SynGAP PSD enrichment in excitatory synapses.
35637289	1	8	theme	Liquid-liquid	75:87	arg1	proteins					148:155	two abundant proteins	135:155	two abundant proteins that interact in the postsynaptic density (PSD) of neurons	135:214	Liquid-liquid phase separation (LLPS) of SynGAP and PSD-95, two abundant proteins that interact in the postsynaptic density (PSD) of neurons, has been implicated in modulating SynGAP PSD enrichment in excitatory synapses.
35637289	1	8	theme	Liquid-liquid	75:87	arg1	LLPS					107:110	LLPS	107:110	LLPS	107:110	Liquid-liquid phase separation (LLPS) of SynGAP and PSD-95, two abundant proteins that interact in the postsynaptic density (PSD) of neurons, has been implicated in modulating SynGAP PSD enrichment in excitatory synapses.
35637289	4	9	attach	isolated	543:550	arg1	brain					561:565	rat brain	557:565	rat brain	557:565	We identified multiple O-GlcNAc modification sites for the endogenous SynGAP isolated from rat brain and the recombinantly expressed protein.
35637289	4	9	attach	isolated	543:550	arg2	SynGAP					536:541	the endogenous SynGAP	521:541	the endogenous SynGAP isolated from rat brain	521:565	We identified multiple O-GlcNAc modification sites for the endogenous SynGAP isolated from rat brain and the recombinantly expressed protein.
35637289	5	10	theme	SynGAP	693:698	arg1	forms					684:688	site-specifically O-GlcNAcylated forms	651:688	site-specifically O-GlcNAcylated forms of SynGAP	651:698	Protein semisynthesis was used to generate site-specifically O-GlcNAcylated forms of SynGAP, and in vitro and cell-based LLPS assays demonstrated that T1306 O-GlcNAc of SynGAP blocks the interaction with PSD-95, thus inhibiting LLPS.
35637289	1	11	theme	phase	89:93	arg1	separation					95:104	Liquid-liquid phase separation	75:104	Liquid-liquid phase separation (LLPS) of SynGAP and PSD-95	75:132	Liquid-liquid phase separation (LLPS) of SynGAP and PSD-95, two abundant proteins that interact in the postsynaptic density (PSD) of neurons, has been implicated in modulating SynGAP PSD enrichment in excitatory synapses.
35637289	1	11	theme	phase	89:93	arg1	proteins					148:155	two abundant proteins	135:155	two abundant proteins that interact in the postsynaptic density (PSD) of neurons	135:214	Liquid-liquid phase separation (LLPS) of SynGAP and PSD-95, two abundant proteins that interact in the postsynaptic density (PSD) of neurons, has been implicated in modulating SynGAP PSD enrichment in excitatory synapses.
35637289	1	11	theme	phase	89:93	arg1	LLPS					107:110	LLPS	107:110	LLPS	107:110	Liquid-liquid phase separation (LLPS) of SynGAP and PSD-95, two abundant proteins that interact in the postsynaptic density (PSD) of neurons, has been implicated in modulating SynGAP PSD enrichment in excitatory synapses.
35637289	1	12	theme	SynGAP	251:256	arg1	enrichment					262:271	SynGAP PSD enrichment	251:271	SynGAP PSD enrichment in excitatory synapses	251:294	Liquid-liquid phase separation (LLPS) of SynGAP and PSD-95, two abundant proteins that interact in the postsynaptic density (PSD) of neurons, has been implicated in modulating SynGAP PSD enrichment in excitatory synapses.
35637289	5	13	theme	T1306	759:763	arg1	O-GlcNAc					765:772	T1306 O-GlcNAc	759:772	T1306 O-GlcNAc of SynGAP	759:782	Protein semisynthesis was used to generate site-specifically O-GlcNAcylated forms of SynGAP, and in vitro and cell-based LLPS assays demonstrated that T1306 O-GlcNAc of SynGAP blocks the interaction with PSD-95, thus inhibiting LLPS.
35637289	5	14	with	interaction	795:805	arg1	PSD-95					812:817	PSD-95	812:817	PSD-95	812:817	Protein semisynthesis was used to generate site-specifically O-GlcNAcylated forms of SynGAP, and in vitro and cell-based LLPS assays demonstrated that T1306 O-GlcNAc of SynGAP blocks the interaction with PSD-95, thus inhibiting LLPS.
35637289	3	15	theme	SynGAP	400:405	arg1	O-GlcNAcylation					381:395	O-GlcNAcylation	381:395	O-GlcNAcylation of SynGAP	381:405	Here we report that O-GlcNAcylation of SynGAP acts as a suppressor of LLPS of the SynGAP/PSD-95 complex.
35637289	3	15	theme	SynGAP	400:405	arg1	suppressor					417:426	a suppressor	415:426	a suppressor of LLPS of the SynGAP/PSD-95 complex	415:463	Here we report that O-GlcNAcylation of SynGAP acts as a suppressor of LLPS of the SynGAP/PSD-95 complex.
35637289	4	16	theme	multiple	480:487	arg1	sites					511:515	multiple O-GlcNAc modification sites	480:515	multiple O-GlcNAc modification sites for the endogenous SynGAP isolated from rat brain and the recombinantly expressed protein	480:605	We identified multiple O-GlcNAc modification sites for the endogenous SynGAP isolated from rat brain and the recombinantly expressed protein.
35637289	3	17	theme	LLPS	431:434	arg1	O-GlcNAcylation					381:395	O-GlcNAcylation	381:395	O-GlcNAcylation of SynGAP	381:405	Here we report that O-GlcNAcylation of SynGAP acts as a suppressor of LLPS of the SynGAP/PSD-95 complex.
35637289	3	17	theme	LLPS	431:434	arg1	suppressor					417:426	a suppressor	415:426	a suppressor of LLPS of the SynGAP/PSD-95 complex	415:463	Here we report that O-GlcNAcylation of SynGAP acts as a suppressor of LLPS of the SynGAP/PSD-95 complex.
35637289	1	18	theme	excitatory	276:285	arg1	synapses					287:294	excitatory synapses	276:294	excitatory synapses	276:294	Liquid-liquid phase separation (LLPS) of SynGAP and PSD-95, two abundant proteins that interact in the postsynaptic density (PSD) of neurons, has been implicated in modulating SynGAP PSD enrichment in excitatory synapses.
35637289	4	19	theme	rat	557:559	arg1	brain					561:565	rat brain	557:565	rat brain	557:565	We identified multiple O-GlcNAc modification sites for the endogenous SynGAP isolated from rat brain and the recombinantly expressed protein.
35637289	1	20	theme	postsynaptic	178:189	arg1	PSD					200:202	PSD	200:202	PSD	200:202	Liquid-liquid phase separation (LLPS) of SynGAP and PSD-95, two abundant proteins that interact in the postsynaptic density (PSD) of neurons, has been implicated in modulating SynGAP PSD enrichment in excitatory synapses.
35637289	1	20	theme	postsynaptic	178:189	arg1	density					191:197	the postsynaptic density	174:197	the postsynaptic density (PSD) of neurons	174:214	Liquid-liquid phase separation (LLPS) of SynGAP and PSD-95, two abundant proteins that interact in the postsynaptic density (PSD) of neurons, has been implicated in modulating SynGAP PSD enrichment in excitatory synapses.
35637289	1	21	theme	PSD	258:260	arg1	enrichment					262:271	SynGAP PSD enrichment	251:271	SynGAP PSD enrichment in excitatory synapses	251:294	Liquid-liquid phase separation (LLPS) of SynGAP and PSD-95, two abundant proteins that interact in the postsynaptic density (PSD) of neurons, has been implicated in modulating SynGAP PSD enrichment in excitatory synapses.
35637289	1	22	from	enrichment	262:271	arg1	synapses					287:294	excitatory synapses	276:294	excitatory synapses	276:294	Liquid-liquid phase separation (LLPS) of SynGAP and PSD-95, two abundant proteins that interact in the postsynaptic density (PSD) of neurons, has been implicated in modulating SynGAP PSD enrichment in excitatory synapses.
35637289	0	23	theme	phase	40:44	arg1	separation					46:55	liquid-liquid phase separation	26:55	liquid-liquid phase separation of SynGAP/PSD-95	26:72	O-GlcNAcylation modulates liquid-liquid phase separation of SynGAP/PSD-95.
35637289	3	24	theme	SynGAP/PSD-95	443:455	arg1	complex					457:463	the SynGAP/PSD-95 complex	439:463	the SynGAP/PSD-95 complex	439:463	Here we report that O-GlcNAcylation of SynGAP acts as a suppressor of LLPS of the SynGAP/PSD-95 complex.
35637289	0	25	theme	liquid-liquid	26:38	arg1	separation					46:55	liquid-liquid phase separation	26:55	liquid-liquid phase separation of SynGAP/PSD-95	26:72	O-GlcNAcylation modulates liquid-liquid phase separation of SynGAP/PSD-95.
35637289	5	26	theme	cell-based	718:727	arg1	assays					734:739	in vitro and cell-based LLPS assays	705:739	in vitro and cell-based LLPS assays	705:739	Protein semisynthesis was used to generate site-specifically O-GlcNAcylated forms of SynGAP, and in vitro and cell-based LLPS assays demonstrated that T1306 O-GlcNAc of SynGAP blocks the interaction with PSD-95, thus inhibiting LLPS.
35637289	1	27	theme	SynGAP	116:121	arg1	separation					95:104	Liquid-liquid phase separation	75:104	Liquid-liquid phase separation (LLPS) of SynGAP and PSD-95	75:132	Liquid-liquid phase separation (LLPS) of SynGAP and PSD-95, two abundant proteins that interact in the postsynaptic density (PSD) of neurons, has been implicated in modulating SynGAP PSD enrichment in excitatory synapses.
35637289	1	27	theme	SynGAP	116:121	arg1	proteins					148:155	two abundant proteins	135:155	two abundant proteins that interact in the postsynaptic density (PSD) of neurons	135:214	Liquid-liquid phase separation (LLPS) of SynGAP and PSD-95, two abundant proteins that interact in the postsynaptic density (PSD) of neurons, has been implicated in modulating SynGAP PSD enrichment in excitatory synapses.
35637289	1	27	theme	SynGAP	116:121	arg1	LLPS					107:110	LLPS	107:110	LLPS	107:110	Liquid-liquid phase separation (LLPS) of SynGAP and PSD-95, two abundant proteins that interact in the postsynaptic density (PSD) of neurons, has been implicated in modulating SynGAP PSD enrichment in excitatory synapses.
35637289	3	28	theme	complex	457:463	arg1	LLPS					431:434	LLPS	431:434	LLPS of the SynGAP/PSD-95 complex	431:463	Here we report that O-GlcNAcylation of SynGAP acts as a suppressor of LLPS of the SynGAP/PSD-95 complex.
35637289	2	29	theme	regulatory	321:330	arg1	mechanisms					332:341	the underlying regulatory mechanisms	306:341	the underlying regulatory mechanisms	306:341	However, the underlying regulatory mechanisms remain enigmatic.
35637289	5	30	theme	LLPS	729:732	arg1	assays					734:739	in vitro and cell-based LLPS assays	705:739	in vitro and cell-based LLPS assays	705:739	Protein semisynthesis was used to generate site-specifically O-GlcNAcylated forms of SynGAP, and in vitro and cell-based LLPS assays demonstrated that T1306 O-GlcNAc of SynGAP blocks the interaction with PSD-95, thus inhibiting LLPS.
35637289	4	31	theme	endogenous	525:534	arg1	SynGAP					536:541	the endogenous SynGAP	521:541	the endogenous SynGAP isolated from rat brain	521:565	We identified multiple O-GlcNAc modification sites for the endogenous SynGAP isolated from rat brain and the recombinantly expressed protein.
35637289	8	32	theme	post-translational	1232:1249	arg1	cycling					1192:1198	OGT- and OGA-catalysed O-GlcNAc cycling	1160:1198	OGT- and OGA-catalysed O-GlcNAc cycling	1160:1198	These findings demonstrate that OGT- and OGA-catalysed O-GlcNAc cycling may serve as an LLPS-regulating post-translational modification.
35637289	8	32	theme	post-translational	1232:1249	arg1	modification					1251:1262	an LLPS-regulating post-translational modification	1213:1262	an LLPS-regulating post-translational modification	1213:1262	These findings demonstrate that OGT- and OGA-catalysed O-GlcNAc cycling may serve as an LLPS-regulating post-translational modification.
35637289	8	33	theme	LLPS-regulating	1216:1230	arg1	cycling					1192:1198	OGT- and OGA-catalysed O-GlcNAc cycling	1160:1198	OGT- and OGA-catalysed O-GlcNAc cycling	1160:1198	These findings demonstrate that OGT- and OGA-catalysed O-GlcNAc cycling may serve as an LLPS-regulating post-translational modification.
35637289	8	33	theme	LLPS-regulating	1216:1230	arg1	modification					1251:1262	an LLPS-regulating post-translational modification	1213:1262	an LLPS-regulating post-translational modification	1213:1262	These findings demonstrate that OGT- and OGA-catalysed O-GlcNAc cycling may serve as an LLPS-regulating post-translational modification.
35637289	6	34	theme	SynGAP/PSD-95	882:894	arg1	LLPS					896:899	SynGAP/PSD-95 LLPS	882:899	SynGAP/PSD-95 LLPS	882:899	Furthermore, O-GlcNAcylation suppresses SynGAP/PSD-95 LLPS in a dominant-negative manner, enabling sub-stoichiometric O-GlcNAcylation to exert effective regulation.
35637289	8	35	theme	O-GlcNAc	1183:1190	arg1	cycling					1192:1198	OGT- and OGA-catalysed O-GlcNAc cycling	1160:1198	OGT- and OGA-catalysed O-GlcNAc cycling	1160:1198	These findings demonstrate that OGT- and OGA-catalysed O-GlcNAc cycling may serve as an LLPS-regulating post-translational modification.
35637289	8	35	theme	O-GlcNAc	1183:1190	arg1	modification					1251:1262	an LLPS-regulating post-translational modification	1213:1262	an LLPS-regulating post-translational modification	1213:1262	These findings demonstrate that OGT- and OGA-catalysed O-GlcNAc cycling may serve as an LLPS-regulating post-translational modification.
35637289	0	36	theme	SynGAP/PSD-95	60:72	arg1	separation					46:55	liquid-liquid phase separation	26:55	liquid-liquid phase separation of SynGAP/PSD-95	26:72	O-GlcNAcylation modulates liquid-liquid phase separation of SynGAP/PSD-95.
35637289	8	37	theme	OGT-	1160:1163	arg1	cycling					1192:1198	OGT- and OGA-catalysed O-GlcNAc cycling	1160:1198	OGT- and OGA-catalysed O-GlcNAc cycling	1160:1198	These findings demonstrate that OGT- and OGA-catalysed O-GlcNAc cycling may serve as an LLPS-regulating post-translational modification.
35637289	8	37	theme	OGT-	1160:1163	arg1	modification					1251:1262	an LLPS-regulating post-translational modification	1213:1262	an LLPS-regulating post-translational modification	1213:1262	These findings demonstrate that OGT- and OGA-catalysed O-GlcNAc cycling may serve as an LLPS-regulating post-translational modification.
35637289	1	38	theme	PSD-95	127:132	arg1	separation					95:104	Liquid-liquid phase separation	75:104	Liquid-liquid phase separation (LLPS) of SynGAP and PSD-95	75:132	Liquid-liquid phase separation (LLPS) of SynGAP and PSD-95, two abundant proteins that interact in the postsynaptic density (PSD) of neurons, has been implicated in modulating SynGAP PSD enrichment in excitatory synapses.
35637289	1	38	theme	PSD-95	127:132	arg1	proteins					148:155	two abundant proteins	135:155	two abundant proteins that interact in the postsynaptic density (PSD) of neurons	135:214	Liquid-liquid phase separation (LLPS) of SynGAP and PSD-95, two abundant proteins that interact in the postsynaptic density (PSD) of neurons, has been implicated in modulating SynGAP PSD enrichment in excitatory synapses.
35637289	1	38	theme	PSD-95	127:132	arg1	LLPS					107:110	LLPS	107:110	LLPS	107:110	Liquid-liquid phase separation (LLPS) of SynGAP and PSD-95, two abundant proteins that interact in the postsynaptic density (PSD) of neurons, has been implicated in modulating SynGAP PSD enrichment in excitatory synapses.
35637289	6	39	theme	effective	985:993	arg1	regulation					995:1004	effective regulation	985:1004	effective regulation	985:1004	Furthermore, O-GlcNAcylation suppresses SynGAP/PSD-95 LLPS in a dominant-negative manner, enabling sub-stoichiometric O-GlcNAcylation to exert effective regulation.
35637289	5	40	theme	in	705:706	arg1	assays					734:739	in vitro and cell-based LLPS assays	705:739	in vitro and cell-based LLPS assays	705:739	Protein semisynthesis was used to generate site-specifically O-GlcNAcylated forms of SynGAP, and in vitro and cell-based LLPS assays demonstrated that T1306 O-GlcNAc of SynGAP blocks the interaction with PSD-95, thus inhibiting LLPS.
35637289	7	41	theme	O-GlcNAc	1078:1085	arg1	OGT					1100:1102	OGT	1100:1102	OGT	1100:1102	We also showed that O-GlcNAc-dependent LLPS is reversibly regulated by O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA).
35637289	7	41	theme	O-GlcNAc	1078:1085	arg1	transferase					1087:1097	O-GlcNAc transferase	1078:1097	O-GlcNAc transferase (OGT)	1078:1103	We also showed that O-GlcNAc-dependent LLPS is reversibly regulated by O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA).
35637289	2	42	theme	underlying	310:319	arg1	mechanisms					332:341	the underlying regulatory mechanisms	306:341	the underlying regulatory mechanisms	306:341	However, the underlying regulatory mechanisms remain enigmatic.
35637289	1	43	theme	neurons	208:214	arg1	PSD					200:202	PSD	200:202	PSD	200:202	Liquid-liquid phase separation (LLPS) of SynGAP and PSD-95, two abundant proteins that interact in the postsynaptic density (PSD) of neurons, has been implicated in modulating SynGAP PSD enrichment in excitatory synapses.
35637289	1	43	theme	neurons	208:214	arg1	density					191:197	the postsynaptic density	174:197	the postsynaptic density (PSD) of neurons	174:214	Liquid-liquid phase separation (LLPS) of SynGAP and PSD-95, two abundant proteins that interact in the postsynaptic density (PSD) of neurons, has been implicated in modulating SynGAP PSD enrichment in excitatory synapses.
35637289	8	44	theme	OGA-catalysed	1169:1181	arg1	cycling					1192:1198	OGT- and OGA-catalysed O-GlcNAc cycling	1160:1198	OGT- and OGA-catalysed O-GlcNAc cycling	1160:1198	These findings demonstrate that OGT- and OGA-catalysed O-GlcNAc cycling may serve as an LLPS-regulating post-translational modification.
35637289	8	44	theme	OGA-catalysed	1169:1181	arg1	modification					1251:1262	an LLPS-regulating post-translational modification	1213:1262	an LLPS-regulating post-translational modification	1213:1262	These findings demonstrate that OGT- and OGA-catalysed O-GlcNAc cycling may serve as an LLPS-regulating post-translational modification.
35637289	1	45	theme	abundant	139:146	arg1	separation					95:104	Liquid-liquid phase separation	75:104	Liquid-liquid phase separation (LLPS) of SynGAP and PSD-95	75:132	Liquid-liquid phase separation (LLPS) of SynGAP and PSD-95, two abundant proteins that interact in the postsynaptic density (PSD) of neurons, has been implicated in modulating SynGAP PSD enrichment in excitatory synapses.
35637289	1	45	theme	abundant	139:146	arg1	proteins					148:155	two abundant proteins	135:155	two abundant proteins that interact in the postsynaptic density (PSD) of neurons	135:214	Liquid-liquid phase separation (LLPS) of SynGAP and PSD-95, two abundant proteins that interact in the postsynaptic density (PSD) of neurons, has been implicated in modulating SynGAP PSD enrichment in excitatory synapses.
35637289	4	46	theme	expressed	589:597	arg1	protein					599:605	the recombinantly expressed protein	571:605	the recombinantly expressed protein	571:605	We identified multiple O-GlcNAc modification sites for the endogenous SynGAP isolated from rat brain and the recombinantly expressed protein.
35637289	5	47	theme	SynGAP	777:782	arg1	O-GlcNAc					765:772	T1306 O-GlcNAc	759:772	T1306 O-GlcNAc of SynGAP	759:782	Protein semisynthesis was used to generate site-specifically O-GlcNAcylated forms of SynGAP, and in vitro and cell-based LLPS assays demonstrated that T1306 O-GlcNAc of SynGAP blocks the interaction with PSD-95, thus inhibiting LLPS.
35637289	4	48	theme	modification	498:509	arg1	sites					511:515	multiple O-GlcNAc modification sites	480:515	multiple O-GlcNAc modification sites for the endogenous SynGAP isolated from rat brain and the recombinantly expressed protein	480:605	We identified multiple O-GlcNAc modification sites for the endogenous SynGAP isolated from rat brain and the recombinantly expressed protein.
31747588	8	0	theme	age-dependent	1170:1182	arg1	stress					1194:1199	age-dependent oxidative stress	1170:1199	age-dependent oxidative stress	1170:1199	These results suggest that NPGPx modulates O-GlcNAcylation by inhibiting OGA to cope with age-dependent oxidative stress and protect motor neurons from degeneration, providing a potential therapeutic axis for ALS.
31747588	7	1	theme	unaffected	1061:1070	arg1	adults					1072:1077	unaffected adults	1061:1077	unaffected adults	1061:1077	Furthermore, expression of NPGPx in ALS patients is significantly lower than in unaffected adults.
31747588	7	2	from	expression	994:1003	arg1	patients					1021:1028	ALS patients	1017:1028	ALS patients	1017:1028	Furthermore, expression of NPGPx in ALS patients is significantly lower than in unaffected adults.
31747588	5	3	theme	stress-activated	771:786	arg1	NPGPx					788:792	stress-activated NPGPx	771:792	stress-activated NPGPx	771:792	Mechanistically, stress-activated NPGPx inhibits O-GlcNAcase (OGA) through disulfide bonding to fine-tune global O-GlcNAcylation.
31747588	6	4	theme	neuron	939:944	arg1	loss					946:949	spinal motor neuron loss	926:949	spinal motor neuron loss in aged NPGPx-deficient mice	926:978	Pharmacological inhibition of OGA rescues spinal motor neuron loss in aged NPGPx-deficient mice.
31747588	3	5	theme	muscle	474:479	arg1	denervation					481:491	muscle denervation	474:491	muscle denervation	474:491	Here, we found that mice deficient in NPGPx (GPx7), an oxidative stress sensor, develop ALS-like phenotypes, including paralysis, muscle denervation, and motor neurons loss.
31747588	4	6	theme	motor	539:543	arg1	neurons					545:551	normal spinal motor neurons	525:551	normal spinal motor neurons that exhibit elevated O-GlcNAcylation against age-dependent oxidative stress	525:628	Unlike normal spinal motor neurons that exhibit elevated O-GlcNAcylation against age-dependent oxidative stress, NPGPx-deficient spinal motor neurons fail to boost O-GlcNAcylation and exacerbate ROS accumulation, leading to cell death.
31747588	6	7	theme	motor	933:937	arg1	loss					946:949	spinal motor neuron loss	926:949	spinal motor neuron loss in aged NPGPx-deficient mice	926:978	Pharmacological inhibition of OGA rescues spinal motor neuron loss in aged NPGPx-deficient mice.
31747588	2	8	theme	age-related	277:287	arg1	stress					300:305	age-related cumulative stress	277:305	age-related cumulative stress	277:305	However, the molecular basis of age-related cumulative stress in ALS pathogenesis remains elusive.
31747588	4	9	theme	cell	742:745	arg1	death					747:751	cell death	742:751	cell death	742:751	Unlike normal spinal motor neurons that exhibit elevated O-GlcNAcylation against age-dependent oxidative stress, NPGPx-deficient spinal motor neurons fail to boost O-GlcNAcylation and exacerbate ROS accumulation, leading to cell death.
31747588	6	10	theme	spinal	926:931	arg1	loss					946:949	spinal motor neuron loss	926:949	spinal motor neuron loss in aged NPGPx-deficient mice	926:978	Pharmacological inhibition of OGA rescues spinal motor neuron loss in aged NPGPx-deficient mice.
31747588	4	11	theme	oxidative	613:621	arg1	stress					623:628	age-dependent oxidative stress	599:628	age-dependent oxidative stress	599:628	Unlike normal spinal motor neurons that exhibit elevated O-GlcNAcylation against age-dependent oxidative stress, NPGPx-deficient spinal motor neurons fail to boost O-GlcNAcylation and exacerbate ROS accumulation, leading to cell death.
31747588	3	12	theme	oxidative	399:407	arg1	NPGPx					382:386	NPGPx	382:386	NPGPx (GPx7)	382:393	Here, we found that mice deficient in NPGPx (GPx7), an oxidative stress sensor, develop ALS-like phenotypes, including paralysis, muscle denervation, and motor neurons loss.
31747588	3	12	theme	oxidative	399:407	arg1	sensor					416:421	an oxidative stress sensor	396:421	an oxidative stress sensor	396:421	Here, we found that mice deficient in NPGPx (GPx7), an oxidative stress sensor, develop ALS-like phenotypes, including paralysis, muscle denervation, and motor neurons loss.
31747588	8	13	theme	motor	1213:1217	arg1	neurons					1219:1225	motor neurons	1213:1225	motor neurons	1213:1225	These results suggest that NPGPx modulates O-GlcNAcylation by inhibiting OGA to cope with age-dependent oxidative stress and protect motor neurons from degeneration, providing a potential therapeutic axis for ALS.
31747588	3	14	from	deficient	369:377	arg1	GPx7					389:392	GPx7	389:392	GPx7	389:392	Here, we found that mice deficient in NPGPx (GPx7), an oxidative stress sensor, develop ALS-like phenotypes, including paralysis, muscle denervation, and motor neurons loss.
31747588	3	14	from	deficient	369:377	arg1	sensor					416:421	an oxidative stress sensor	396:421	an oxidative stress sensor	396:421	Here, we found that mice deficient in NPGPx (GPx7), an oxidative stress sensor, develop ALS-like phenotypes, including paralysis, muscle denervation, and motor neurons loss.
31747588	3	14	from	deficient	369:377	arg1	NPGPx					382:386	NPGPx	382:386	NPGPx (GPx7)	382:393	Here, we found that mice deficient in NPGPx (GPx7), an oxidative stress sensor, develop ALS-like phenotypes, including paralysis, muscle denervation, and motor neurons loss.
31747588	2	15	theme	molecular	258:266	arg1	basis					268:272	the molecular basis	254:272	the molecular basis of age-related cumulative stress in ALS pathogenesis	254:325	However, the molecular basis of age-related cumulative stress in ALS pathogenesis remains elusive.
31747588	3	16	theme	stress	409:414	arg1	NPGPx					382:386	NPGPx	382:386	NPGPx (GPx7)	382:393	Here, we found that mice deficient in NPGPx (GPx7), an oxidative stress sensor, develop ALS-like phenotypes, including paralysis, muscle denervation, and motor neurons loss.
31747588	3	16	theme	stress	409:414	arg1	sensor					416:421	an oxidative stress sensor	396:421	an oxidative stress sensor	396:421	Here, we found that mice deficient in NPGPx (GPx7), an oxidative stress sensor, develop ALS-like phenotypes, including paralysis, muscle denervation, and motor neurons loss.
31747588	3	17	theme	deficient	369:377	arg1	mice					364:367	mice	364:367	mice deficient in NPGPx (GPx7), an oxidative stress sensor,	364:422	Here, we found that mice deficient in NPGPx (GPx7), an oxidative stress sensor, develop ALS-like phenotypes, including paralysis, muscle denervation, and motor neurons loss.
31747588	6	18	from	loss	946:949	arg1	mice					975:978	aged NPGPx-deficient mice	954:978	aged NPGPx-deficient mice	954:978	Pharmacological inhibition of OGA rescues spinal motor neuron loss in aged NPGPx-deficient mice.
31747588	3	19	dep	paralysis	463:471	arg1	loss					512:515	loss	512:515	loss	512:515	Here, we found that mice deficient in NPGPx (GPx7), an oxidative stress sensor, develop ALS-like phenotypes, including paralysis, muscle denervation, and motor neurons loss.
31747588	2	20	theme	ALS	310:312	arg1	pathogenesis					314:325	ALS pathogenesis	310:325	ALS pathogenesis	310:325	However, the molecular basis of age-related cumulative stress in ALS pathogenesis remains elusive.
31747588	1	21	theme	common	178:183	arg1	disease					198:204	the most common motor neuron disease	169:204	the most common motor neuron disease	169:204	Amyotrophic lateral sclerosis (ALS), the most common motor neuron disease, usually occurs in middle-aged people.
31747588	1	21	theme	common	178:183	arg1	sclerosis					152:160	Amyotrophic lateral sclerosis	132:160	Amyotrophic lateral sclerosis (ALS)	132:166	Amyotrophic lateral sclerosis (ALS), the most common motor neuron disease, usually occurs in middle-aged people.
31747588	0	22	theme	NPGPx-Mediated	0:13	arg1	Adaptation					15:24	NPGPx-Mediated Adaptation	0:24	NPGPx-Mediated Adaptation to Oxidative Stress	0:44	NPGPx-Mediated Adaptation to Oxidative Stress Protects Motor Neurons from Degeneration in Aging by Directly Modulating O-GlcNAcase.
31747588	1	23	theme	motor	185:189	arg1	disease					198:204	the most common motor neuron disease	169:204	the most common motor neuron disease	169:204	Amyotrophic lateral sclerosis (ALS), the most common motor neuron disease, usually occurs in middle-aged people.
31747588	1	23	theme	motor	185:189	arg1	sclerosis					152:160	Amyotrophic lateral sclerosis	132:160	Amyotrophic lateral sclerosis (ALS)	132:166	Amyotrophic lateral sclerosis (ALS), the most common motor neuron disease, usually occurs in middle-aged people.
31747588	0	24	theme	Oxidative	29:37	arg1	Stress					39:44	Oxidative Stress	29:44	Oxidative Stress	29:44	NPGPx-Mediated Adaptation to Oxidative Stress Protects Motor Neurons from Degeneration in Aging by Directly Modulating O-GlcNAcase.
31747588	2	25	theme	stress	300:305	arg1	basis					268:272	the molecular basis	254:272	the molecular basis of age-related cumulative stress in ALS pathogenesis	254:325	However, the molecular basis of age-related cumulative stress in ALS pathogenesis remains elusive.
31747588	1	26	theme	neuron	191:196	arg1	disease					198:204	the most common motor neuron disease	169:204	the most common motor neuron disease	169:204	Amyotrophic lateral sclerosis (ALS), the most common motor neuron disease, usually occurs in middle-aged people.
31747588	1	26	theme	neuron	191:196	arg1	sclerosis					152:160	Amyotrophic lateral sclerosis	132:160	Amyotrophic lateral sclerosis (ALS)	132:166	Amyotrophic lateral sclerosis (ALS), the most common motor neuron disease, usually occurs in middle-aged people.
31747588	5	27	theme	disulfide	829:837	arg1	bonding					839:845	disulfide bonding	829:845	disulfide bonding to fine-tune global O-GlcNAcylation	829:881	Mechanistically, stress-activated NPGPx inhibits O-GlcNAcase (OGA) through disulfide bonding to fine-tune global O-GlcNAcylation.
31747588	4	28	theme	spinal	532:537	arg1	neurons					545:551	normal spinal motor neurons	525:551	normal spinal motor neurons that exhibit elevated O-GlcNAcylation against age-dependent oxidative stress	525:628	Unlike normal spinal motor neurons that exhibit elevated O-GlcNAcylation against age-dependent oxidative stress, NPGPx-deficient spinal motor neurons fail to boost O-GlcNAcylation and exacerbate ROS accumulation, leading to cell death.
31747588	2	29	theme	cumulative	289:298	arg1	stress					300:305	age-related cumulative stress	277:305	age-related cumulative stress	277:305	However, the molecular basis of age-related cumulative stress in ALS pathogenesis remains elusive.
31747588	8	30	theme	oxidative	1184:1192	arg1	stress					1194:1199	age-dependent oxidative stress	1170:1199	age-dependent oxidative stress	1170:1199	These results suggest that NPGPx modulates O-GlcNAcylation by inhibiting OGA to cope with age-dependent oxidative stress and protect motor neurons from degeneration, providing a potential therapeutic axis for ALS.
31747588	3	31	theme	ALS-like	432:439	arg1	neurons					504:510	motor neurons	498:510	motor neurons	498:510	Here, we found that mice deficient in NPGPx (GPx7), an oxidative stress sensor, develop ALS-like phenotypes, including paralysis, muscle denervation, and motor neurons loss.
31747588	3	31	theme	ALS-like	432:439	arg1	phenotypes					441:450	ALS-like phenotypes	432:450	ALS-like phenotypes	432:450	Here, we found that mice deficient in NPGPx (GPx7), an oxidative stress sensor, develop ALS-like phenotypes, including paralysis, muscle denervation, and motor neurons loss.
31747588	3	31	theme	ALS-like	432:439	arg1	paralysis					463:471	paralysis	463:471	paralysis	463:471	Here, we found that mice deficient in NPGPx (GPx7), an oxidative stress sensor, develop ALS-like phenotypes, including paralysis, muscle denervation, and motor neurons loss.
31747588	3	31	theme	ALS-like	432:439	arg1	denervation					481:491	muscle denervation	474:491	muscle denervation	474:491	Here, we found that mice deficient in NPGPx (GPx7), an oxidative stress sensor, develop ALS-like phenotypes, including paralysis, muscle denervation, and motor neurons loss.
31747588	8	32	theme	potential	1258:1266	arg1	axis					1280:1283	a potential therapeutic axis	1256:1283	a potential therapeutic axis for ALS	1256:1291	These results suggest that NPGPx modulates O-GlcNAcylation by inhibiting OGA to cope with age-dependent oxidative stress and protect motor neurons from degeneration, providing a potential therapeutic axis for ALS.
31747588	4	33	theme	normal	525:530	arg1	neurons					545:551	normal spinal motor neurons	525:551	normal spinal motor neurons that exhibit elevated O-GlcNAcylation against age-dependent oxidative stress	525:628	Unlike normal spinal motor neurons that exhibit elevated O-GlcNAcylation against age-dependent oxidative stress, NPGPx-deficient spinal motor neurons fail to boost O-GlcNAcylation and exacerbate ROS accumulation, leading to cell death.
31747588	8	34	dep	potential	1258:1266	arg1	therapeutic					1268:1278	therapeutic	1268:1278	therapeutic	1268:1278	These results suggest that NPGPx modulates O-GlcNAcylation by inhibiting OGA to cope with age-dependent oxidative stress and protect motor neurons from degeneration, providing a potential therapeutic axis for ALS.
31747588	5	35	theme	fine-tune	850:858	arg1	O-GlcNAcylation					867:881	fine-tune global O-GlcNAcylation	850:881	fine-tune global O-GlcNAcylation	850:881	Mechanistically, stress-activated NPGPx inhibits O-GlcNAcase (OGA) through disulfide bonding to fine-tune global O-GlcNAcylation.
31747588	4	36	theme	NPGPx-deficient	631:645	arg1	neurons					660:666	NPGPx-deficient spinal motor neurons	631:666	NPGPx-deficient spinal motor neurons	631:666	Unlike normal spinal motor neurons that exhibit elevated O-GlcNAcylation against age-dependent oxidative stress, NPGPx-deficient spinal motor neurons fail to boost O-GlcNAcylation and exacerbate ROS accumulation, leading to cell death.
31747588	4	37	theme	motor	654:658	arg1	neurons					660:666	NPGPx-deficient spinal motor neurons	631:666	NPGPx-deficient spinal motor neurons	631:666	Unlike normal spinal motor neurons that exhibit elevated O-GlcNAcylation against age-dependent oxidative stress, NPGPx-deficient spinal motor neurons fail to boost O-GlcNAcylation and exacerbate ROS accumulation, leading to cell death.
31747588	0	38	from	Degeneration	74:85	arg1	Aging					90:94	Aging	90:94	Aging	90:94	NPGPx-Mediated Adaptation to Oxidative Stress Protects Motor Neurons from Degeneration in Aging by Directly Modulating O-GlcNAcase.
31747588	4	39	theme	age-dependent	599:611	arg1	stress					623:628	age-dependent oxidative stress	599:628	age-dependent oxidative stress	599:628	Unlike normal spinal motor neurons that exhibit elevated O-GlcNAcylation against age-dependent oxidative stress, NPGPx-deficient spinal motor neurons fail to boost O-GlcNAcylation and exacerbate ROS accumulation, leading to cell death.
31747588	5	40	theme	global	860:865	arg1	O-GlcNAcylation					867:881	fine-tune global O-GlcNAcylation	850:881	fine-tune global O-GlcNAcylation	850:881	Mechanistically, stress-activated NPGPx inhibits O-GlcNAcase (OGA) through disulfide bonding to fine-tune global O-GlcNAcylation.
31747588	6	41	theme	OGA	914:916	arg1	inhibition					900:909	Pharmacological inhibition	884:909	Pharmacological inhibition of OGA	884:916	Pharmacological inhibition of OGA rescues spinal motor neuron loss in aged NPGPx-deficient mice.
31747588	4	42	theme	ROS	713:715	arg1	accumulation					717:728	ROS accumulation	713:728	ROS accumulation	713:728	Unlike normal spinal motor neurons that exhibit elevated O-GlcNAcylation against age-dependent oxidative stress, NPGPx-deficient spinal motor neurons fail to boost O-GlcNAcylation and exacerbate ROS accumulation, leading to cell death.
31747588	0	43	theme	Motor	55:59	arg1	Neurons					61:67	Motor Neurons	55:67	Motor Neurons	55:67	NPGPx-Mediated Adaptation to Oxidative Stress Protects Motor Neurons from Degeneration in Aging by Directly Modulating O-GlcNAcase.
31747588	6	44	theme	NPGPx-deficient	959:973	arg1	mice					975:978	aged NPGPx-deficient mice	954:978	aged NPGPx-deficient mice	954:978	Pharmacological inhibition of OGA rescues spinal motor neuron loss in aged NPGPx-deficient mice.
31747588	1	45	theme	Amyotrophic	132:142	arg1	ALS					163:165	ALS	163:165	ALS	163:165	Amyotrophic lateral sclerosis (ALS), the most common motor neuron disease, usually occurs in middle-aged people.
31747588	1	45	theme	Amyotrophic	132:142	arg1	sclerosis					152:160	Amyotrophic lateral sclerosis	132:160	Amyotrophic lateral sclerosis (ALS)	132:166	Amyotrophic lateral sclerosis (ALS), the most common motor neuron disease, usually occurs in middle-aged people.
31747588	1	45	theme	Amyotrophic	132:142	arg1	disease					198:204	the most common motor neuron disease	169:204	the most common motor neuron disease	169:204	Amyotrophic lateral sclerosis (ALS), the most common motor neuron disease, usually occurs in middle-aged people.
31747588	2	46	from	basis	268:272	arg1	pathogenesis					314:325	ALS pathogenesis	310:325	ALS pathogenesis	310:325	However, the molecular basis of age-related cumulative stress in ALS pathogenesis remains elusive.
31747588	6	47	theme	aged	954:957	arg1	mice					975:978	aged NPGPx-deficient mice	954:978	aged NPGPx-deficient mice	954:978	Pharmacological inhibition of OGA rescues spinal motor neuron loss in aged NPGPx-deficient mice.
31747588	1	48	theme	lateral	144:150	arg1	ALS					163:165	ALS	163:165	ALS	163:165	Amyotrophic lateral sclerosis (ALS), the most common motor neuron disease, usually occurs in middle-aged people.
31747588	1	48	theme	lateral	144:150	arg1	sclerosis					152:160	Amyotrophic lateral sclerosis	132:160	Amyotrophic lateral sclerosis (ALS)	132:166	Amyotrophic lateral sclerosis (ALS), the most common motor neuron disease, usually occurs in middle-aged people.
31747588	1	48	theme	lateral	144:150	arg1	disease					198:204	the most common motor neuron disease	169:204	the most common motor neuron disease	169:204	Amyotrophic lateral sclerosis (ALS), the most common motor neuron disease, usually occurs in middle-aged people.
31747588	3	49	theme	motor	498:502	arg1	neurons					504:510	motor neurons	498:510	motor neurons	498:510	Here, we found that mice deficient in NPGPx (GPx7), an oxidative stress sensor, develop ALS-like phenotypes, including paralysis, muscle denervation, and motor neurons loss.
31747588	7	50	theme	ALS	1017:1019	arg1	patients					1021:1028	ALS patients	1017:1028	ALS patients	1017:1028	Furthermore, expression of NPGPx in ALS patients is significantly lower than in unaffected adults.
31747588	4	51	theme	elevated	566:573	arg1	O-GlcNAcylation					575:589	elevated O-GlcNAcylation	566:589	elevated O-GlcNAcylation	566:589	Unlike normal spinal motor neurons that exhibit elevated O-GlcNAcylation against age-dependent oxidative stress, NPGPx-deficient spinal motor neurons fail to boost O-GlcNAcylation and exacerbate ROS accumulation, leading to cell death.
31747588	6	52	theme	Pharmacological	884:898	arg1	inhibition					900:909	Pharmacological inhibition	884:909	Pharmacological inhibition of OGA	884:916	Pharmacological inhibition of OGA rescues spinal motor neuron loss in aged NPGPx-deficient mice.
31747588	4	53	theme	spinal	647:652	arg1	neurons					660:666	NPGPx-deficient spinal motor neurons	631:666	NPGPx-deficient spinal motor neurons	631:666	Unlike normal spinal motor neurons that exhibit elevated O-GlcNAcylation against age-dependent oxidative stress, NPGPx-deficient spinal motor neurons fail to boost O-GlcNAcylation and exacerbate ROS accumulation, leading to cell death.
31747588	1	54	theme	middle-aged	225:235	arg1	people					237:242	middle-aged people	225:242	middle-aged people	225:242	Amyotrophic lateral sclerosis (ALS), the most common motor neuron disease, usually occurs in middle-aged people.
31747588	3	55	from	NPGPx	382:386	arg1	deficient					369:377	deficient	369:377	deficient	369:377	Here, we found that mice deficient in NPGPx (GPx7), an oxidative stress sensor, develop ALS-like phenotypes, including paralysis, muscle denervation, and motor neurons loss.
31747588	7	56	theme	NPGPx	1008:1012	arg1	expression					994:1003	expression	994:1003	expression of NPGPx in ALS patients	994:1028	Furthermore, expression of NPGPx in ALS patients is significantly lower than in unaffected adults.
35739577	4	0	theme	cord	904:907	arg1	cells					959:963	(i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells	884:963	(i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells (HSPCs)	884:971	METHODS Cellular O-GlcNAcylation was manipulated using small molecule inhibition or CRISPR/Cas9 manipulation of catalyzing enzyme O-GlcNAc transferase (OGT) and removing enzyme O-GlcNAcase (OGA) in two cell models of erythroid differentiation, starting from: (i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells (HSPCs) to investigate the erythroid lineage specification and differentiation; and (ii) human-derived erythroblastic leukemia K562 cells to investigate the terminal differentiation.
35739577	4	0	theme	cord	904:907	arg1	HSPCs					966:970	HSPCs	966:970	HSPCs	966:970	METHODS Cellular O-GlcNAcylation was manipulated using small molecule inhibition or CRISPR/Cas9 manipulation of catalyzing enzyme O-GlcNAc transferase (OGT) and removing enzyme O-GlcNAcase (OGA) in two cell models of erythroid differentiation, starting from: (i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells (HSPCs) to investigate the erythroid lineage specification and differentiation; and (ii) human-derived erythroblastic leukemia K562 cells to investigate the terminal differentiation.
35739577	3	1	theme	erythroid	537:545	arg1	lineage					547:553	the erythroid lineage	533:553	the erythroid lineage	533:553	However, how O-GlcNAcylation, a posttranslational modification of proteins that is an ideal metabolic sensor, contributes to the commitment of HSCs to the erythroid lineage and to the terminal erythroid differentiation has not been addressed.
35739577	9	2	dep	Fourier	2069:2075	arg1	spectroscopy					2103:2114	infrared (FTIR) spectroscopy	2087:2114	synchrotron-based Fourier transform infrared (FTIR) spectroscopy	2051:2114	Additionally, analysis of biochemical contents using synchrotron-based Fourier transform infrared (FTIR) spectroscopy showed unique metabolic fingerprints upon OGA inhibition during erythroid differentiation, supporting that metabolic reprogramming plays a part in this process.
35739577	9	2	dep	Fourier	2069:2075	arg1	transform					2077:2085	transform	2077:2085	transform	2077:2085	Additionally, analysis of biochemical contents using synchrotron-based Fourier transform infrared (FTIR) spectroscopy showed unique metabolic fingerprints upon OGA inhibition during erythroid differentiation, supporting that metabolic reprogramming plays a part in this process.
35739577	4	3	theme	CD34+	923:927	arg1	cells					959:963	(i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells	884:963	(i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells (HSPCs)	884:971	METHODS Cellular O-GlcNAcylation was manipulated using small molecule inhibition or CRISPR/Cas9 manipulation of catalyzing enzyme O-GlcNAc transferase (OGT) and removing enzyme O-GlcNAcase (OGA) in two cell models of erythroid differentiation, starting from: (i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells (HSPCs) to investigate the erythroid lineage specification and differentiation; and (ii) human-derived erythroblastic leukemia K562 cells to investigate the terminal differentiation.
35739577	4	3	theme	CD34+	923:927	arg1	HSPCs					966:970	HSPCs	966:970	HSPCs	966:970	METHODS Cellular O-GlcNAcylation was manipulated using small molecule inhibition or CRISPR/Cas9 manipulation of catalyzing enzyme O-GlcNAc transferase (OGT) and removing enzyme O-GlcNAcase (OGA) in two cell models of erythroid differentiation, starting from: (i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells (HSPCs) to investigate the erythroid lineage specification and differentiation; and (ii) human-derived erythroblastic leukemia K562 cells to investigate the terminal differentiation.
35739577	10	4	dep	CONCLUSIONS	2277:2287	arg1	evidence					2293:2300	The evidence	2289:2300	CONCLUSIONS The evidence presented here	2277:2315	CONCLUSIONS The evidence presented here demonstrated the novel regulatory role of O-GlcNAc/BCL11A axis in erythroid differentiation, maturation, and globin production that could be important in understanding erythropoiesis and hematologic disorders whose etiology is related to impaired erythroid differentiation and hemoglobinopathies.
35739577	4	5	theme	Cellular	633:640	arg1	O-GlcNAcylation					642:656	Cellular O-GlcNAcylation	633:656	Cellular O-GlcNAcylation	633:656	METHODS Cellular O-GlcNAcylation was manipulated using small molecule inhibition or CRISPR/Cas9 manipulation of catalyzing enzyme O-GlcNAc transferase (OGT) and removing enzyme O-GlcNAcase (OGA) in two cell models of erythroid differentiation, starting from: (i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells (HSPCs) to investigate the erythroid lineage specification and differentiation; and (ii) human-derived erythroblastic leukemia K562 cells to investigate the terminal differentiation.
35739577	11	6	theme	ex	2693:2694	arg1	production					2701:2710	an ex vivo production	2690:2710	an ex vivo production of functional human reticulocytes for transfusion from renewable cell sources, i.e., HSPCs and pluripotent stem cells	2690:2828	Our findings may lay the groundwork for future clinical applications toward an ex vivo production of functional human reticulocytes for transfusion from renewable cell sources, i.e., HSPCs and pluripotent stem cells.
35739577	3	7	theme	erythroid	575:583	arg1	differentiation					585:599	the terminal erythroid differentiation	562:599	the terminal erythroid differentiation	562:599	However, how O-GlcNAcylation, a posttranslational modification of proteins that is an ideal metabolic sensor, contributes to the commitment of HSCs to the erythroid lineage and to the terminal erythroid differentiation has not been addressed.
35739577	4	8	theme	i	885:885	arg1	cells					959:963	(i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells	884:963	(i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells (HSPCs)	884:971	METHODS Cellular O-GlcNAcylation was manipulated using small molecule inhibition or CRISPR/Cas9 manipulation of catalyzing enzyme O-GlcNAc transferase (OGT) and removing enzyme O-GlcNAcase (OGA) in two cell models of erythroid differentiation, starting from: (i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells (HSPCs) to investigate the erythroid lineage specification and differentiation; and (ii) human-derived erythroblastic leukemia K562 cells to investigate the terminal differentiation.
35739577	4	8	theme	i	885:885	arg1	HSPCs					966:970	HSPCs	966:970	HSPCs	966:970	METHODS Cellular O-GlcNAcylation was manipulated using small molecule inhibition or CRISPR/Cas9 manipulation of catalyzing enzyme O-GlcNAc transferase (OGT) and removing enzyme O-GlcNAcase (OGA) in two cell models of erythroid differentiation, starting from: (i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells (HSPCs) to investigate the erythroid lineage specification and differentiation; and (ii) human-derived erythroblastic leukemia K562 cells to investigate the terminal differentiation.
35739577	9	9	theme	infrared	2087:2094	arg1	spectroscopy					2103:2114	infrared (FTIR) spectroscopy	2087:2114	synchrotron-based Fourier transform infrared (FTIR) spectroscopy	2051:2114	Additionally, analysis of biochemical contents using synchrotron-based Fourier transform infrared (FTIR) spectroscopy showed unique metabolic fingerprints upon OGA inhibition during erythroid differentiation, supporting that metabolic reprogramming plays a part in this process.
35739577	2	10	theme	important	299:307	arg1	metabolism					282:291	Cellular metabolism	273:291	Cellular metabolism	273:291	Cellular metabolism is an important regulator of cell fate determination during the differentiation of HSCs.
35739577	2	10	theme	important	299:307	arg1	regulator					309:317	an important regulator	296:317	an important regulator of cell fate determination during the differentiation of HSCs	296:379	Cellular metabolism is an important regulator of cell fate determination during the differentiation of HSCs.
35739577	6	11	theme	erythroid-associated	1617:1636	arg1	genes					1638:1642	erythroid-associated genes	1617:1642	erythroid-associated genes	1617:1642	RESULTS First, we observed that two-step inhibition of OGT and OGA, which were established from the observed dynamics of O-GlcNAc level along the course of differentiation, promotes HSPCs toward erythroid differentiation and enucleation, in agreement with an upregulation of a multitude of erythroid-associated genes.
35739577	4	12	theme	human	888:892	arg1	cells					959:963	(i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells	884:963	(i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells (HSPCs)	884:971	METHODS Cellular O-GlcNAcylation was manipulated using small molecule inhibition or CRISPR/Cas9 manipulation of catalyzing enzyme O-GlcNAc transferase (OGT) and removing enzyme O-GlcNAcase (OGA) in two cell models of erythroid differentiation, starting from: (i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells (HSPCs) to investigate the erythroid lineage specification and differentiation; and (ii) human-derived erythroblastic leukemia K562 cells to investigate the terminal differentiation.
35739577	4	12	theme	human	888:892	arg1	HSPCs					966:970	HSPCs	966:970	HSPCs	966:970	METHODS Cellular O-GlcNAcylation was manipulated using small molecule inhibition or CRISPR/Cas9 manipulation of catalyzing enzyme O-GlcNAc transferase (OGT) and removing enzyme O-GlcNAcase (OGA) in two cell models of erythroid differentiation, starting from: (i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells (HSPCs) to investigate the erythroid lineage specification and differentiation; and (ii) human-derived erythroblastic leukemia K562 cells to investigate the terminal differentiation.
35739577	4	13	link	blood-derived	909:921	arg1	cells					959:963	(i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells	884:963	(i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells (HSPCs)	884:971	METHODS Cellular O-GlcNAcylation was manipulated using small molecule inhibition or CRISPR/Cas9 manipulation of catalyzing enzyme O-GlcNAc transferase (OGT) and removing enzyme O-GlcNAcase (OGA) in two cell models of erythroid differentiation, starting from: (i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells (HSPCs) to investigate the erythroid lineage specification and differentiation; and (ii) human-derived erythroblastic leukemia K562 cells to investigate the terminal differentiation.
35739577	4	13	link	blood-derived	909:921	arg1	HSPCs					966:970	HSPCs	966:970	HSPCs	966:970	METHODS Cellular O-GlcNAcylation was manipulated using small molecule inhibition or CRISPR/Cas9 manipulation of catalyzing enzyme O-GlcNAc transferase (OGT) and removing enzyme O-GlcNAcase (OGA) in two cell models of erythroid differentiation, starting from: (i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells (HSPCs) to investigate the erythroid lineage specification and differentiation; and (ii) human-derived erythroblastic leukemia K562 cells to investigate the terminal differentiation.
35739577	6	14	theme	multitude	1604:1612	arg1	upregulation					1586:1597	an upregulation	1583:1597	an upregulation of a multitude of erythroid-associated genes	1583:1642	RESULTS First, we observed that two-step inhibition of OGT and OGA, which were established from the observed dynamics of O-GlcNAc level along the course of differentiation, promotes HSPCs toward erythroid differentiation and enucleation, in agreement with an upregulation of a multitude of erythroid-associated genes.
35739577	1	15	theme	stem	227:230	arg1	HSCs					239:242	HSCs	239:242	HSCs	239:242	BACKGROUND Human erythropoiesis is a tightly regulated, multistep process encompassing the differentiation of hematopoietic stem cells (HSCs) toward mature erythrocytes.
35739577	1	15	theme	stem	227:230	arg1	cells					232:236	hematopoietic stem cells	213:236	hematopoietic stem cells (HSCs)	213:243	BACKGROUND Human erythropoiesis is a tightly regulated, multistep process encompassing the differentiation of hematopoietic stem cells (HSCs) toward mature erythrocytes.
35739577	7	16	theme	subsequent	1752:1761	arg1	hyper-O-GlcNAcylation					1763:1783	subsequent hyper-O-GlcNAcylation	1752:1783	subsequent hyper-O-GlcNAcylation	1752:1783	Further studies in the efficient K562 model of erythroid differentiation confirmed that OGA inhibition and subsequent hyper-O-GlcNAcylation enhance terminal erythroid differentiation and affect globin production.
35739577	4	17	theme	molecule	686:693	arg1	inhibition					695:704	small molecule inhibition	680:704	small molecule inhibition	680:704	METHODS Cellular O-GlcNAcylation was manipulated using small molecule inhibition or CRISPR/Cas9 manipulation of catalyzing enzyme O-GlcNAc transferase (OGT) and removing enzyme O-GlcNAcase (OGA) in two cell models of erythroid differentiation, starting from: (i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells (HSPCs) to investigate the erythroid lineage specification and differentiation; and (ii) human-derived erythroblastic leukemia K562 cells to investigate the terminal differentiation.
35739577	2	18	theme	fate	327:330	arg1	determination					332:344	cell fate determination	322:344	cell fate determination	322:344	Cellular metabolism is an important regulator of cell fate determination during the differentiation of HSCs.
35739577	10	19	theme	impaired	2555:2562	arg1	differentiation					2574:2588	impaired erythroid differentiation	2555:2588	impaired erythroid differentiation	2555:2588	CONCLUSIONS The evidence presented here demonstrated the novel regulatory role of O-GlcNAc/BCL11A axis in erythroid differentiation, maturation, and globin production that could be important in understanding erythropoiesis and hematologic disorders whose etiology is related to impaired erythroid differentiation and hemoglobinopathies.
35739577	9	20	theme	synchrotron-based	2051:2067	arg1	Fourier					2069:2075	synchrotron-based Fourier transform infrared (FTIR) spectroscopy	2051:2114	synchrotron-based Fourier transform infrared (FTIR) spectroscopy	2051:2114	Additionally, analysis of biochemical contents using synchrotron-based Fourier transform infrared (FTIR) spectroscopy showed unique metabolic fingerprints upon OGA inhibition during erythroid differentiation, supporting that metabolic reprogramming plays a part in this process.
35739577	9	21	theme	unique	2123:2128	arg1	fingerprints					2140:2151	unique metabolic fingerprints	2123:2151	unique metabolic fingerprints	2123:2151	Additionally, analysis of biochemical contents using synchrotron-based Fourier transform infrared (FTIR) spectroscopy showed unique metabolic fingerprints upon OGA inhibition during erythroid differentiation, supporting that metabolic reprogramming plays a part in this process.
35739577	10	22	theme	hematologic	2504:2514	arg1	disorders					2516:2524	hematologic disorders	2504:2524	hematologic disorders whose etiology is related to impaired erythroid differentiation and hemoglobinopathies	2504:2611	CONCLUSIONS The evidence presented here demonstrated the novel regulatory role of O-GlcNAc/BCL11A axis in erythroid differentiation, maturation, and globin production that could be important in understanding erythropoiesis and hematologic disorders whose etiology is related to impaired erythroid differentiation and hemoglobinopathies.
35739577	4	23	theme	stem/progenitor	943:957	arg1	cells					959:963	(i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells	884:963	(i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells (HSPCs)	884:971	METHODS Cellular O-GlcNAcylation was manipulated using small molecule inhibition or CRISPR/Cas9 manipulation of catalyzing enzyme O-GlcNAc transferase (OGT) and removing enzyme O-GlcNAcase (OGA) in two cell models of erythroid differentiation, starting from: (i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells (HSPCs) to investigate the erythroid lineage specification and differentiation; and (ii) human-derived erythroblastic leukemia K562 cells to investigate the terminal differentiation.
35739577	4	23	theme	stem/progenitor	943:957	arg1	HSPCs					966:970	HSPCs	966:970	HSPCs	966:970	METHODS Cellular O-GlcNAcylation was manipulated using small molecule inhibition or CRISPR/Cas9 manipulation of catalyzing enzyme O-GlcNAc transferase (OGT) and removing enzyme O-GlcNAcase (OGA) in two cell models of erythroid differentiation, starting from: (i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells (HSPCs) to investigate the erythroid lineage specification and differentiation; and (ii) human-derived erythroblastic leukemia K562 cells to investigate the terminal differentiation.
35739577	10	24	theme	erythroid	2383:2391	arg1	differentiation					2393:2407	erythroid differentiation	2383:2407	erythroid differentiation	2383:2407	CONCLUSIONS The evidence presented here demonstrated the novel regulatory role of O-GlcNAc/BCL11A axis in erythroid differentiation, maturation, and globin production that could be important in understanding erythropoiesis and hematologic disorders whose etiology is related to impaired erythroid differentiation and hemoglobinopathies.
35739577	6	25	theme	OGA	1390:1392	arg1	inhibition					1368:1377	two-step inhibition	1359:1377	two-step inhibition of OGT and OGA, which were established from the observed dynamics of O-GlcNAc level along the course of differentiation,	1359:1498	RESULTS First, we observed that two-step inhibition of OGT and OGA, which were established from the observed dynamics of O-GlcNAc level along the course of differentiation, promotes HSPCs toward erythroid differentiation and enucleation, in agreement with an upregulation of a multitude of erythroid-associated genes.
35739577	7	26	theme	differentiation	1702:1716	arg1	model					1683:1687	the efficient K562 model	1664:1687	the efficient K562 model of erythroid differentiation	1664:1716	Further studies in the efficient K562 model of erythroid differentiation confirmed that OGA inhibition and subsequent hyper-O-GlcNAcylation enhance terminal erythroid differentiation and affect globin production.
35739577	9	27	theme	OGA	2158:2160	arg1	inhibition					2162:2171	OGA inhibition	2158:2171	OGA inhibition during erythroid differentiation	2158:2204	Additionally, analysis of biochemical contents using synchrotron-based Fourier transform infrared (FTIR) spectroscopy showed unique metabolic fingerprints upon OGA inhibition during erythroid differentiation, supporting that metabolic reprogramming plays a part in this process.
35739577	4	28	theme	removing	786:793	arg1	OGA					815:817	OGA	815:817	OGA	815:817	METHODS Cellular O-GlcNAcylation was manipulated using small molecule inhibition or CRISPR/Cas9 manipulation of catalyzing enzyme O-GlcNAc transferase (OGT) and removing enzyme O-GlcNAcase (OGA) in two cell models of erythroid differentiation, starting from: (i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells (HSPCs) to investigate the erythroid lineage specification and differentiation; and (ii) human-derived erythroblastic leukemia K562 cells to investigate the terminal differentiation.
35739577	4	28	theme	removing	786:793	arg1	O-GlcNAcase					802:812	removing enzyme O-GlcNAcase	786:812	removing enzyme O-GlcNAcase (OGA)	786:818	METHODS Cellular O-GlcNAcylation was manipulated using small molecule inhibition or CRISPR/Cas9 manipulation of catalyzing enzyme O-GlcNAc transferase (OGT) and removing enzyme O-GlcNAcase (OGA) in two cell models of erythroid differentiation, starting from: (i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells (HSPCs) to investigate the erythroid lineage specification and differentiation; and (ii) human-derived erythroblastic leukemia K562 cells to investigate the terminal differentiation.
35739577	6	29	theme	OGT	1382:1384	arg1	inhibition					1368:1377	two-step inhibition	1359:1377	two-step inhibition of OGT and OGA, which were established from the observed dynamics of O-GlcNAc level along the course of differentiation,	1359:1498	RESULTS First, we observed that two-step inhibition of OGT and OGA, which were established from the observed dynamics of O-GlcNAc level along the course of differentiation, promotes HSPCs toward erythroid differentiation and enucleation, in agreement with an upregulation of a multitude of erythroid-associated genes.
35739577	3	30	theme	terminal	566:573	arg1	differentiation					585:599	the terminal erythroid differentiation	562:599	the terminal erythroid differentiation	562:599	However, how O-GlcNAcylation, a posttranslational modification of proteins that is an ideal metabolic sensor, contributes to the commitment of HSCs to the erythroid lineage and to the terminal erythroid differentiation has not been addressed.
35739577	8	31	theme	O-GlcNAc-driven	1917:1931	arg1	differentiation					1943:1957	O-GlcNAc-driven erythroid differentiation	1917:1957	O-GlcNAc-driven erythroid differentiation	1917:1957	Mechanistically, we found that BCL11A is a key mediator of O-GlcNAc-driven erythroid differentiation and β- and α-globin production herein.
35739577	11	32	theme	pluripotent	2807:2817	arg1	cells					2824:2828	pluripotent stem cells	2807:2828	pluripotent stem cells	2807:2828	Our findings may lay the groundwork for future clinical applications toward an ex vivo production of functional human reticulocytes for transfusion from renewable cell sources, i.e., HSPCs and pluripotent stem cells.
35739577	11	33	theme	functional	2715:2724	arg1	reticulocytes					2732:2744	functional human reticulocytes	2715:2744	functional human reticulocytes for transfusion from renewable cell sources, i.e., HSPCs and pluripotent stem cells	2715:2828	Our findings may lay the groundwork for future clinical applications toward an ex vivo production of functional human reticulocytes for transfusion from renewable cell sources, i.e., HSPCs and pluripotent stem cells.
35739577	4	34	theme	O-GlcNAc	755:762	arg1	transferase					764:774	enzyme O-GlcNAc transferase	748:774	enzyme O-GlcNAc transferase (OGT)	748:780	METHODS Cellular O-GlcNAcylation was manipulated using small molecule inhibition or CRISPR/Cas9 manipulation of catalyzing enzyme O-GlcNAc transferase (OGT) and removing enzyme O-GlcNAcase (OGA) in two cell models of erythroid differentiation, starting from: (i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells (HSPCs) to investigate the erythroid lineage specification and differentiation; and (ii) human-derived erythroblastic leukemia K562 cells to investigate the terminal differentiation.
35739577	4	34	theme	O-GlcNAc	755:762	arg1	OGT					777:779	OGT	777:779	OGT	777:779	METHODS Cellular O-GlcNAcylation was manipulated using small molecule inhibition or CRISPR/Cas9 manipulation of catalyzing enzyme O-GlcNAc transferase (OGT) and removing enzyme O-GlcNAcase (OGA) in two cell models of erythroid differentiation, starting from: (i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells (HSPCs) to investigate the erythroid lineage specification and differentiation; and (ii) human-derived erythroblastic leukemia K562 cells to investigate the terminal differentiation.
35739577	5	35	theme	O-GlcNAcylation	1187:1201	arg1	roles					1178:1182	The functional and regulatory roles	1148:1182	The functional and regulatory roles of O-GlcNAcylation in erythroid differentiation, maturation, and globin production	1148:1265	The functional and regulatory roles of O-GlcNAcylation in erythroid differentiation, maturation, and globin production were investigated, and downstream signaling was delineated.
35739577	2	36	theme	Cellular	273:280	arg1	metabolism					282:291	Cellular metabolism	273:291	Cellular metabolism	273:291	Cellular metabolism is an important regulator of cell fate determination during the differentiation of HSCs.
35739577	2	36	theme	Cellular	273:280	arg1	regulator					309:317	an important regulator	296:317	an important regulator of cell fate determination during the differentiation of HSCs	296:379	Cellular metabolism is an important regulator of cell fate determination during the differentiation of HSCs.
35739577	8	37	theme	differentiation	1943:1957	arg1	mediator					1905:1912	a key mediator	1899:1912	a key mediator of O-GlcNAc-driven erythroid differentiation and β- and α-globin production	1899:1988	Mechanistically, we found that BCL11A is a key mediator of O-GlcNAc-driven erythroid differentiation and β- and α-globin production herein.
35739577	8	37	theme	differentiation	1943:1957	arg1	BCL11A					1889:1894	BCL11A	1889:1894	BCL11A	1889:1894	Mechanistically, we found that BCL11A is a key mediator of O-GlcNAc-driven erythroid differentiation and β- and α-globin production herein.
35739577	7	38	theme	K562	1678:1681	arg1	model					1683:1687	the efficient K562 model	1664:1687	the efficient K562 model of erythroid differentiation	1664:1716	Further studies in the efficient K562 model of erythroid differentiation confirmed that OGA inhibition and subsequent hyper-O-GlcNAcylation enhance terminal erythroid differentiation and affect globin production.
35739577	6	39	theme	O-GlcNAc	1448:1455	arg1	level					1457:1461	O-GlcNAc level	1448:1461	O-GlcNAc level	1448:1461	RESULTS First, we observed that two-step inhibition of OGT and OGA, which were established from the observed dynamics of O-GlcNAc level along the course of differentiation, promotes HSPCs toward erythroid differentiation and enucleation, in agreement with an upregulation of a multitude of erythroid-associated genes.
35739577	5	40	theme	erythroid	1206:1214	arg1	differentiation					1216:1230	erythroid differentiation	1206:1230	erythroid differentiation	1206:1230	The functional and regulatory roles of O-GlcNAcylation in erythroid differentiation, maturation, and globin production were investigated, and downstream signaling was delineated.
35739577	8	41	theme	β-	1963:1964	arg1	production					1979:1988	β- and α-globin production	1963:1988	β- and α-globin production	1963:1988	Mechanistically, we found that BCL11A is a key mediator of O-GlcNAc-driven erythroid differentiation and β- and α-globin production herein.
35739577	4	42	theme	erythroid	992:1000	arg1	specification					1010:1022	the erythroid lineage specification	988:1022	the erythroid lineage specification	988:1022	METHODS Cellular O-GlcNAcylation was manipulated using small molecule inhibition or CRISPR/Cas9 manipulation of catalyzing enzyme O-GlcNAc transferase (OGT) and removing enzyme O-GlcNAcase (OGA) in two cell models of erythroid differentiation, starting from: (i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells (HSPCs) to investigate the erythroid lineage specification and differentiation; and (ii) human-derived erythroblastic leukemia K562 cells to investigate the terminal differentiation.
35739577	11	43	theme	reticulocytes	2732:2744	arg1	production					2701:2710	an ex vivo production	2690:2710	an ex vivo production of functional human reticulocytes for transfusion from renewable cell sources, i.e., HSPCs and pluripotent stem cells	2690:2828	Our findings may lay the groundwork for future clinical applications toward an ex vivo production of functional human reticulocytes for transfusion from renewable cell sources, i.e., HSPCs and pluripotent stem cells.
35739577	1	44	dep	regulated	148:156	arg1	multistep					159:167	multistep	159:167	multistep	159:167	BACKGROUND Human erythropoiesis is a tightly regulated, multistep process encompassing the differentiation of hematopoietic stem cells (HSCs) toward mature erythrocytes.
35739577	8	45	theme	α-globin	1970:1977	arg1	production					1979:1988	β- and α-globin production	1963:1988	β- and α-globin production	1963:1988	Mechanistically, we found that BCL11A is a key mediator of O-GlcNAc-driven erythroid differentiation and β- and α-globin production herein.
35739577	4	46	link	human-derived	1054:1066	arg1	cells					1097:1101	(ii) human-derived erythroblastic leukemia K562 cells	1049:1101	(ii) human-derived erythroblastic leukemia K562 cells	1049:1101	METHODS Cellular O-GlcNAcylation was manipulated using small molecule inhibition or CRISPR/Cas9 manipulation of catalyzing enzyme O-GlcNAc transferase (OGT) and removing enzyme O-GlcNAcase (OGA) in two cell models of erythroid differentiation, starting from: (i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells (HSPCs) to investigate the erythroid lineage specification and differentiation; and (ii) human-derived erythroblastic leukemia K562 cells to investigate the terminal differentiation.
35739577	9	47	theme	metabolic	2223:2231	arg1	reprogramming					2233:2245	metabolic reprogramming	2223:2245	metabolic reprogramming	2223:2245	Additionally, analysis of biochemical contents using synchrotron-based Fourier transform infrared (FTIR) spectroscopy showed unique metabolic fingerprints upon OGA inhibition during erythroid differentiation, supporting that metabolic reprogramming plays a part in this process.
35739577	4	48	theme	cell	827:830	arg1	models					832:837	two cell models	823:837	two cell models of erythroid differentiation	823:866	METHODS Cellular O-GlcNAcylation was manipulated using small molecule inhibition or CRISPR/Cas9 manipulation of catalyzing enzyme O-GlcNAc transferase (OGT) and removing enzyme O-GlcNAcase (OGA) in two cell models of erythroid differentiation, starting from: (i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells (HSPCs) to investigate the erythroid lineage specification and differentiation; and (ii) human-derived erythroblastic leukemia K562 cells to investigate the terminal differentiation.
35739577	3	49	theme	metabolic	474:482	arg1	sensor					484:489	an ideal metabolic sensor	465:489	an ideal metabolic sensor	465:489	However, how O-GlcNAcylation, a posttranslational modification of proteins that is an ideal metabolic sensor, contributes to the commitment of HSCs to the erythroid lineage and to the terminal erythroid differentiation has not been addressed.
35739577	3	49	theme	metabolic	474:482	arg1	modification					432:443	a posttranslational modification	412:443	a posttranslational modification of proteins that is an ideal metabolic sensor	412:489	However, how O-GlcNAcylation, a posttranslational modification of proteins that is an ideal metabolic sensor, contributes to the commitment of HSCs to the erythroid lineage and to the terminal erythroid differentiation has not been addressed.
35739577	3	49	theme	metabolic	474:482	arg1	O-GlcNAcylation					395:409	O-GlcNAcylation	395:409	O-GlcNAcylation	395:409	However, how O-GlcNAcylation, a posttranslational modification of proteins that is an ideal metabolic sensor, contributes to the commitment of HSCs to the erythroid lineage and to the terminal erythroid differentiation has not been addressed.
35739577	9	50	dep	infrared	2087:2094	arg1	FTIR					2097:2100	FTIR	2097:2100	FTIR	2097:2100	Additionally, analysis of biochemical contents using synchrotron-based Fourier transform infrared (FTIR) spectroscopy showed unique metabolic fingerprints upon OGA inhibition during erythroid differentiation, supporting that metabolic reprogramming plays a part in this process.
35739577	4	51	theme	leukemia	1083:1090	arg1	cells					1097:1101	(ii) human-derived erythroblastic leukemia K562 cells	1049:1101	(ii) human-derived erythroblastic leukemia K562 cells	1049:1101	METHODS Cellular O-GlcNAcylation was manipulated using small molecule inhibition or CRISPR/Cas9 manipulation of catalyzing enzyme O-GlcNAc transferase (OGT) and removing enzyme O-GlcNAcase (OGA) in two cell models of erythroid differentiation, starting from: (i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells (HSPCs) to investigate the erythroid lineage specification and differentiation; and (ii) human-derived erythroblastic leukemia K562 cells to investigate the terminal differentiation.
35739577	11	52	theme	renewable	2767:2775	arg1	sources					2782:2788	renewable cell sources	2767:2788	renewable cell sources	2767:2788	Our findings may lay the groundwork for future clinical applications toward an ex vivo production of functional human reticulocytes for transfusion from renewable cell sources, i.e., HSPCs and pluripotent stem cells.
35739577	11	53	theme	clinical	2661:2668	arg1	applications					2670:2681	future clinical applications	2654:2681	future clinical applications toward an ex vivo production of functional human reticulocytes for transfusion from renewable cell sources, i.e., HSPCs and pluripotent stem cells	2654:2828	Our findings may lay the groundwork for future clinical applications toward an ex vivo production of functional human reticulocytes for transfusion from renewable cell sources, i.e., HSPCs and pluripotent stem cells.
35739577	11	54	dep	ex	2693:2694	arg1	vivo					2696:2699	vivo	2696:2699	vivo	2696:2699	Our findings may lay the groundwork for future clinical applications toward an ex vivo production of functional human reticulocytes for transfusion from renewable cell sources, i.e., HSPCs and pluripotent stem cells.
35739577	0	55	theme	Metabolic	0:8	arg1	O-GlcNAcylation					17:31	Metabolic sensor O-GlcNAcylation	0:31	Metabolic sensor O-GlcNAcylation	0:31	Metabolic sensor O-GlcNAcylation regulates erythroid differentiation and globin production via BCL11A.
35739577	5	56	theme	globin	1249:1254	arg1	production					1256:1265	globin production	1249:1265	globin production	1249:1265	The functional and regulatory roles of O-GlcNAcylation in erythroid differentiation, maturation, and globin production were investigated, and downstream signaling was delineated.
35739577	1	57	theme	Human	114:118	arg1	process					169:175	a tightly regulated, multistep process	138:175	a tightly regulated, multistep process encompassing the differentiation of hematopoietic stem cells (HSCs) toward mature erythrocytes	138:270	BACKGROUND Human erythropoiesis is a tightly regulated, multistep process encompassing the differentiation of hematopoietic stem cells (HSCs) toward mature erythrocytes.
35739577	1	57	theme	Human	114:118	arg1	erythropoiesis					120:133	BACKGROUND Human erythropoiesis	103:133	BACKGROUND Human erythropoiesis	103:133	BACKGROUND Human erythropoiesis is a tightly regulated, multistep process encompassing the differentiation of hematopoietic stem cells (HSCs) toward mature erythrocytes.
35739577	7	58	theme	terminal	1793:1800	arg1	differentiation					1812:1826	terminal erythroid differentiation	1793:1826	terminal erythroid differentiation	1793:1826	Further studies in the efficient K562 model of erythroid differentiation confirmed that OGA inhibition and subsequent hyper-O-GlcNAcylation enhance terminal erythroid differentiation and affect globin production.
35739577	7	59	from	studies	1653:1659	arg1	model					1683:1687	the efficient K562 model	1664:1687	the efficient K562 model of erythroid differentiation	1664:1716	Further studies in the efficient K562 model of erythroid differentiation confirmed that OGA inhibition and subsequent hyper-O-GlcNAcylation enhance terminal erythroid differentiation and affect globin production.
35739577	0	60	theme	erythroid	43:51	arg1	differentiation					53:67	erythroid differentiation	43:67	erythroid differentiation	43:67	Metabolic sensor O-GlcNAcylation regulates erythroid differentiation and globin production via BCL11A.
35739577	6	61	theme	differentiation	1483:1497	arg1	course					1473:1478	the course	1469:1478	the course of differentiation	1469:1497	RESULTS First, we observed that two-step inhibition of OGT and OGA, which were established from the observed dynamics of O-GlcNAc level along the course of differentiation, promotes HSPCs toward erythroid differentiation and enucleation, in agreement with an upregulation of a multitude of erythroid-associated genes.
35739577	4	62	theme	human-derived	1054:1066	arg1	cells					1097:1101	(ii) human-derived erythroblastic leukemia K562 cells	1049:1101	(ii) human-derived erythroblastic leukemia K562 cells	1049:1101	METHODS Cellular O-GlcNAcylation was manipulated using small molecule inhibition or CRISPR/Cas9 manipulation of catalyzing enzyme O-GlcNAc transferase (OGT) and removing enzyme O-GlcNAcase (OGA) in two cell models of erythroid differentiation, starting from: (i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells (HSPCs) to investigate the erythroid lineage specification and differentiation; and (ii) human-derived erythroblastic leukemia K562 cells to investigate the terminal differentiation.
35739577	3	63	theme	HSCs	525:528	arg1	commitment					511:520	the commitment	507:520	the commitment of HSCs to the erythroid lineage	507:553	However, how O-GlcNAcylation, a posttranslational modification of proteins that is an ideal metabolic sensor, contributes to the commitment of HSCs to the erythroid lineage and to the terminal erythroid differentiation has not been addressed.
35739577	10	64	from	role	2351:2354	arg1	maturation					2410:2419	maturation	2410:2419	maturation	2410:2419	CONCLUSIONS The evidence presented here demonstrated the novel regulatory role of O-GlcNAc/BCL11A axis in erythroid differentiation, maturation, and globin production that could be important in understanding erythropoiesis and hematologic disorders whose etiology is related to impaired erythroid differentiation and hemoglobinopathies.
35739577	10	64	from	role	2351:2354	arg1	differentiation					2393:2407	erythroid differentiation	2383:2407	erythroid differentiation	2383:2407	CONCLUSIONS The evidence presented here demonstrated the novel regulatory role of O-GlcNAc/BCL11A axis in erythroid differentiation, maturation, and globin production that could be important in understanding erythropoiesis and hematologic disorders whose etiology is related to impaired erythroid differentiation and hemoglobinopathies.
35739577	10	64	from	role	2351:2354	arg1	production					2433:2442	globin production	2426:2442	globin production	2426:2442	CONCLUSIONS The evidence presented here demonstrated the novel regulatory role of O-GlcNAc/BCL11A axis in erythroid differentiation, maturation, and globin production that could be important in understanding erythropoiesis and hematologic disorders whose etiology is related to impaired erythroid differentiation and hemoglobinopathies.
35739577	4	65	theme	differentiation	852:866	arg1	models					832:837	two cell models	823:837	two cell models of erythroid differentiation	823:866	METHODS Cellular O-GlcNAcylation was manipulated using small molecule inhibition or CRISPR/Cas9 manipulation of catalyzing enzyme O-GlcNAc transferase (OGT) and removing enzyme O-GlcNAcase (OGA) in two cell models of erythroid differentiation, starting from: (i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells (HSPCs) to investigate the erythroid lineage specification and differentiation; and (ii) human-derived erythroblastic leukemia K562 cells to investigate the terminal differentiation.
35739577	11	66	dep	HSPCs	2797:2801	arg1	i.e.					2791:2794	i.e.	2791:2794	i.e.	2791:2794	Our findings may lay the groundwork for future clinical applications toward an ex vivo production of functional human reticulocytes for transfusion from renewable cell sources, i.e., HSPCs and pluripotent stem cells.
35739577	9	67	theme	contents	2036:2043	arg1	analysis					2012:2019	analysis	2012:2019	analysis of biochemical contents using synchrotron-based Fourier transform infrared (FTIR) spectroscopy	2012:2114	Additionally, analysis of biochemical contents using synchrotron-based Fourier transform infrared (FTIR) spectroscopy showed unique metabolic fingerprints upon OGA inhibition during erythroid differentiation, supporting that metabolic reprogramming plays a part in this process.
35739577	6	68	with	agreement	1568:1576	arg1	upregulation					1586:1597	an upregulation	1583:1597	an upregulation of a multitude of erythroid-associated genes	1583:1642	RESULTS First, we observed that two-step inhibition of OGT and OGA, which were established from the observed dynamics of O-GlcNAc level along the course of differentiation, promotes HSPCs toward erythroid differentiation and enucleation, in agreement with an upregulation of a multitude of erythroid-associated genes.
35739577	4	69	theme	umbilical	894:902	arg1	cells					959:963	(i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells	884:963	(i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells (HSPCs)	884:971	METHODS Cellular O-GlcNAcylation was manipulated using small molecule inhibition or CRISPR/Cas9 manipulation of catalyzing enzyme O-GlcNAc transferase (OGT) and removing enzyme O-GlcNAcase (OGA) in two cell models of erythroid differentiation, starting from: (i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells (HSPCs) to investigate the erythroid lineage specification and differentiation; and (ii) human-derived erythroblastic leukemia K562 cells to investigate the terminal differentiation.
35739577	4	69	theme	umbilical	894:902	arg1	HSPCs					966:970	HSPCs	966:970	HSPCs	966:970	METHODS Cellular O-GlcNAcylation was manipulated using small molecule inhibition or CRISPR/Cas9 manipulation of catalyzing enzyme O-GlcNAc transferase (OGT) and removing enzyme O-GlcNAcase (OGA) in two cell models of erythroid differentiation, starting from: (i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells (HSPCs) to investigate the erythroid lineage specification and differentiation; and (ii) human-derived erythroblastic leukemia K562 cells to investigate the terminal differentiation.
35739577	4	70	theme	terminal	1122:1129	arg1	differentiation					1131:1145	the terminal differentiation	1118:1145	the terminal differentiation	1118:1145	METHODS Cellular O-GlcNAcylation was manipulated using small molecule inhibition or CRISPR/Cas9 manipulation of catalyzing enzyme O-GlcNAc transferase (OGT) and removing enzyme O-GlcNAcase (OGA) in two cell models of erythroid differentiation, starting from: (i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells (HSPCs) to investigate the erythroid lineage specification and differentiation; and (ii) human-derived erythroblastic leukemia K562 cells to investigate the terminal differentiation.
35739577	6	71	theme	two-step	1359:1366	arg1	inhibition					1368:1377	two-step inhibition	1359:1377	two-step inhibition of OGT and OGA, which were established from the observed dynamics of O-GlcNAc level along the course of differentiation,	1359:1498	RESULTS First, we observed that two-step inhibition of OGT and OGA, which were established from the observed dynamics of O-GlcNAc level along the course of differentiation, promotes HSPCs toward erythroid differentiation and enucleation, in agreement with an upregulation of a multitude of erythroid-associated genes.
35739577	2	72	theme	cell	322:325	arg1	determination					332:344	cell fate determination	322:344	cell fate determination	322:344	Cellular metabolism is an important regulator of cell fate determination during the differentiation of HSCs.
35739577	5	73	theme	downstream	1290:1299	arg1	signaling					1301:1309	downstream signaling	1290:1309	downstream signaling	1290:1309	The functional and regulatory roles of O-GlcNAcylation in erythroid differentiation, maturation, and globin production were investigated, and downstream signaling was delineated.
35739577	4	74	theme	blood-derived	909:921	arg1	cells					959:963	(i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells	884:963	(i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells (HSPCs)	884:971	METHODS Cellular O-GlcNAcylation was manipulated using small molecule inhibition or CRISPR/Cas9 manipulation of catalyzing enzyme O-GlcNAc transferase (OGT) and removing enzyme O-GlcNAcase (OGA) in two cell models of erythroid differentiation, starting from: (i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells (HSPCs) to investigate the erythroid lineage specification and differentiation; and (ii) human-derived erythroblastic leukemia K562 cells to investigate the terminal differentiation.
35739577	4	74	theme	blood-derived	909:921	arg1	HSPCs					966:970	HSPCs	966:970	HSPCs	966:970	METHODS Cellular O-GlcNAcylation was manipulated using small molecule inhibition or CRISPR/Cas9 manipulation of catalyzing enzyme O-GlcNAc transferase (OGT) and removing enzyme O-GlcNAcase (OGA) in two cell models of erythroid differentiation, starting from: (i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells (HSPCs) to investigate the erythroid lineage specification and differentiation; and (ii) human-derived erythroblastic leukemia K562 cells to investigate the terminal differentiation.
35739577	10	75	theme	novel	2334:2338	arg1	role					2351:2354	the novel regulatory role	2330:2354	the novel regulatory role of O-GlcNAc/BCL11A axis in erythroid differentiation, maturation, and globin production that could be important in understanding erythropoiesis and hematologic disorders whose etiology is related to impaired erythroid differentiation and hemoglobinopathies	2330:2611	CONCLUSIONS The evidence presented here demonstrated the novel regulatory role of O-GlcNAc/BCL11A axis in erythroid differentiation, maturation, and globin production that could be important in understanding erythropoiesis and hematologic disorders whose etiology is related to impaired erythroid differentiation and hemoglobinopathies.
35739577	10	75	theme	novel	2334:2338	arg1	important					2458:2466	important	2458:2466	important	2458:2466	CONCLUSIONS The evidence presented here demonstrated the novel regulatory role of O-GlcNAc/BCL11A axis in erythroid differentiation, maturation, and globin production that could be important in understanding erythropoiesis and hematologic disorders whose etiology is related to impaired erythroid differentiation and hemoglobinopathies.
35739577	6	76	theme	genes	1638:1642	arg1	multitude					1604:1612	a multitude	1602:1612	a multitude of erythroid-associated genes	1602:1642	RESULTS First, we observed that two-step inhibition of OGT and OGA, which were established from the observed dynamics of O-GlcNAc level along the course of differentiation, promotes HSPCs toward erythroid differentiation and enucleation, in agreement with an upregulation of a multitude of erythroid-associated genes.
35739577	4	77	theme	CRISPR/Cas9	709:719	arg1	manipulation					721:732	CRISPR/Cas9 manipulation	709:732	CRISPR/Cas9 manipulation	709:732	METHODS Cellular O-GlcNAcylation was manipulated using small molecule inhibition or CRISPR/Cas9 manipulation of catalyzing enzyme O-GlcNAc transferase (OGT) and removing enzyme O-GlcNAcase (OGA) in two cell models of erythroid differentiation, starting from: (i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells (HSPCs) to investigate the erythroid lineage specification and differentiation; and (ii) human-derived erythroblastic leukemia K562 cells to investigate the terminal differentiation.
35739577	1	78	theme	hematopoietic	213:225	arg1	HSCs					239:242	HSCs	239:242	HSCs	239:242	BACKGROUND Human erythropoiesis is a tightly regulated, multistep process encompassing the differentiation of hematopoietic stem cells (HSCs) toward mature erythrocytes.
35739577	1	78	theme	hematopoietic	213:225	arg1	cells					232:236	hematopoietic stem cells	213:236	hematopoietic stem cells (HSCs)	213:243	BACKGROUND Human erythropoiesis is a tightly regulated, multistep process encompassing the differentiation of hematopoietic stem cells (HSCs) toward mature erythrocytes.
35739577	10	79	theme	O-GlcNAc/BCL11A	2359:2373	arg1	axis					2375:2378	O-GlcNAc/BCL11A axis	2359:2378	O-GlcNAc/BCL11A axis	2359:2378	CONCLUSIONS The evidence presented here demonstrated the novel regulatory role of O-GlcNAc/BCL11A axis in erythroid differentiation, maturation, and globin production that could be important in understanding erythropoiesis and hematologic disorders whose etiology is related to impaired erythroid differentiation and hemoglobinopathies.
35739577	2	80	theme	determination	332:344	arg1	metabolism					282:291	Cellular metabolism	273:291	Cellular metabolism	273:291	Cellular metabolism is an important regulator of cell fate determination during the differentiation of HSCs.
35739577	2	80	theme	determination	332:344	arg1	regulator					309:317	an important regulator	296:317	an important regulator of cell fate determination during the differentiation of HSCs	296:379	Cellular metabolism is an important regulator of cell fate determination during the differentiation of HSCs.
35739577	1	81	theme	cells	232:236	arg1	differentiation					194:208	the differentiation	190:208	the differentiation of hematopoietic stem cells (HSCs) toward mature erythrocytes	190:270	BACKGROUND Human erythropoiesis is a tightly regulated, multistep process encompassing the differentiation of hematopoietic stem cells (HSCs) toward mature erythrocytes.
35739577	11	82	from	sources	2782:2788	arg1	transfusion					2750:2760	transfusion	2750:2760	transfusion from renewable cell sources, i.e., HSPCs and pluripotent stem cells	2750:2828	Our findings may lay the groundwork for future clinical applications toward an ex vivo production of functional human reticulocytes for transfusion from renewable cell sources, i.e., HSPCs and pluripotent stem cells.
35739577	7	83	theme	OGA	1733:1735	arg1	inhibition					1737:1746	OGA inhibition	1733:1746	OGA inhibition	1733:1746	Further studies in the efficient K562 model of erythroid differentiation confirmed that OGA inhibition and subsequent hyper-O-GlcNAcylation enhance terminal erythroid differentiation and affect globin production.
35739577	10	84	theme	erythroid	2564:2572	arg1	differentiation					2574:2588	impaired erythroid differentiation	2555:2588	impaired erythroid differentiation	2555:2588	CONCLUSIONS The evidence presented here demonstrated the novel regulatory role of O-GlcNAc/BCL11A axis in erythroid differentiation, maturation, and globin production that could be important in understanding erythropoiesis and hematologic disorders whose etiology is related to impaired erythroid differentiation and hemoglobinopathies.
35739577	4	85	theme	small	680:684	arg1	inhibition					695:704	small molecule inhibition	680:704	small molecule inhibition	680:704	METHODS Cellular O-GlcNAcylation was manipulated using small molecule inhibition or CRISPR/Cas9 manipulation of catalyzing enzyme O-GlcNAc transferase (OGT) and removing enzyme O-GlcNAcase (OGA) in two cell models of erythroid differentiation, starting from: (i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells (HSPCs) to investigate the erythroid lineage specification and differentiation; and (ii) human-derived erythroblastic leukemia K562 cells to investigate the terminal differentiation.
35739577	4	86	dep	METHODS	625:631	arg1	manipulated					662:672	manipulated	662:672	was manipulated using small molecule inhibition or CRISPR/Cas9 manipulation of catalyzing enzyme O-GlcNAc transferase (OGT) and removing enzyme O-GlcNAcase (OGA) in two cell models of erythroid differentiation, starting from: (i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells (HSPCs) to investigate the erythroid lineage specification and differentiation; and (ii) human-derived erythroblastic leukemia K562 cells to investigate the terminal differentiation	658:1145	METHODS Cellular O-GlcNAcylation was manipulated using small molecule inhibition or CRISPR/Cas9 manipulation of catalyzing enzyme O-GlcNAc transferase (OGT) and removing enzyme O-GlcNAcase (OGA) in two cell models of erythroid differentiation, starting from: (i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells (HSPCs) to investigate the erythroid lineage specification and differentiation; and (ii) human-derived erythroblastic leukemia K562 cells to investigate the terminal differentiation.
35739577	6	87	theme	erythroid	1522:1530	arg1	differentiation					1532:1546	erythroid differentiation	1522:1546	erythroid differentiation	1522:1546	RESULTS First, we observed that two-step inhibition of OGT and OGA, which were established from the observed dynamics of O-GlcNAc level along the course of differentiation, promotes HSPCs toward erythroid differentiation and enucleation, in agreement with an upregulation of a multitude of erythroid-associated genes.
35739577	9	88	theme	metabolic	2130:2138	arg1	fingerprints					2140:2151	unique metabolic fingerprints	2123:2151	unique metabolic fingerprints	2123:2151	Additionally, analysis of biochemical contents using synchrotron-based Fourier transform infrared (FTIR) spectroscopy showed unique metabolic fingerprints upon OGA inhibition during erythroid differentiation, supporting that metabolic reprogramming plays a part in this process.
35739577	5	89	theme	functional	1152:1161	arg1	roles					1178:1182	The functional and regulatory roles	1148:1182	The functional and regulatory roles of O-GlcNAcylation in erythroid differentiation, maturation, and globin production	1148:1265	The functional and regulatory roles of O-GlcNAcylation in erythroid differentiation, maturation, and globin production were investigated, and downstream signaling was delineated.
35739577	7	90	theme	erythroid	1692:1700	arg1	differentiation					1702:1716	erythroid differentiation	1692:1716	erythroid differentiation	1692:1716	Further studies in the efficient K562 model of erythroid differentiation confirmed that OGA inhibition and subsequent hyper-O-GlcNAcylation enhance terminal erythroid differentiation and affect globin production.
35739577	4	91	theme	hematopoietic	929:941	arg1	cells					959:963	(i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells	884:963	(i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells (HSPCs)	884:971	METHODS Cellular O-GlcNAcylation was manipulated using small molecule inhibition or CRISPR/Cas9 manipulation of catalyzing enzyme O-GlcNAc transferase (OGT) and removing enzyme O-GlcNAcase (OGA) in two cell models of erythroid differentiation, starting from: (i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells (HSPCs) to investigate the erythroid lineage specification and differentiation; and (ii) human-derived erythroblastic leukemia K562 cells to investigate the terminal differentiation.
35739577	4	91	theme	hematopoietic	929:941	arg1	HSPCs					966:970	HSPCs	966:970	HSPCs	966:970	METHODS Cellular O-GlcNAcylation was manipulated using small molecule inhibition or CRISPR/Cas9 manipulation of catalyzing enzyme O-GlcNAc transferase (OGT) and removing enzyme O-GlcNAcase (OGA) in two cell models of erythroid differentiation, starting from: (i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells (HSPCs) to investigate the erythroid lineage specification and differentiation; and (ii) human-derived erythroblastic leukemia K562 cells to investigate the terminal differentiation.
35739577	11	92	theme	stem	2819:2822	arg1	cells					2824:2828	pluripotent stem cells	2807:2828	pluripotent stem cells	2807:2828	Our findings may lay the groundwork for future clinical applications toward an ex vivo production of functional human reticulocytes for transfusion from renewable cell sources, i.e., HSPCs and pluripotent stem cells.
35739577	8	93	theme	key	1901:1903	arg1	mediator					1905:1912	a key mediator	1899:1912	a key mediator of O-GlcNAc-driven erythroid differentiation and β- and α-globin production	1899:1988	Mechanistically, we found that BCL11A is a key mediator of O-GlcNAc-driven erythroid differentiation and β- and α-globin production herein.
35739577	8	93	theme	key	1901:1903	arg1	BCL11A					1889:1894	BCL11A	1889:1894	BCL11A	1889:1894	Mechanistically, we found that BCL11A is a key mediator of O-GlcNAc-driven erythroid differentiation and β- and α-globin production herein.
35739577	1	94	theme	regulated	148:156	arg1	process					169:175	a tightly regulated, multistep process	138:175	a tightly regulated, multistep process encompassing the differentiation of hematopoietic stem cells (HSCs) toward mature erythrocytes	138:270	BACKGROUND Human erythropoiesis is a tightly regulated, multistep process encompassing the differentiation of hematopoietic stem cells (HSCs) toward mature erythrocytes.
35739577	1	94	theme	regulated	148:156	arg1	erythropoiesis					120:133	BACKGROUND Human erythropoiesis	103:133	BACKGROUND Human erythropoiesis	103:133	BACKGROUND Human erythropoiesis is a tightly regulated, multistep process encompassing the differentiation of hematopoietic stem cells (HSCs) toward mature erythrocytes.
35739577	10	95	theme	axis	2375:2378	arg1	role					2351:2354	the novel regulatory role	2330:2354	the novel regulatory role of O-GlcNAc/BCL11A axis in erythroid differentiation, maturation, and globin production that could be important in understanding erythropoiesis and hematologic disorders whose etiology is related to impaired erythroid differentiation and hemoglobinopathies	2330:2611	CONCLUSIONS The evidence presented here demonstrated the novel regulatory role of O-GlcNAc/BCL11A axis in erythroid differentiation, maturation, and globin production that could be important in understanding erythropoiesis and hematologic disorders whose etiology is related to impaired erythroid differentiation and hemoglobinopathies.
35739577	10	95	theme	axis	2375:2378	arg1	important					2458:2466	important	2458:2466	important	2458:2466	CONCLUSIONS The evidence presented here demonstrated the novel regulatory role of O-GlcNAc/BCL11A axis in erythroid differentiation, maturation, and globin production that could be important in understanding erythropoiesis and hematologic disorders whose etiology is related to impaired erythroid differentiation and hemoglobinopathies.
35739577	3	96	theme	posttranslational	414:430	arg1	sensor					484:489	an ideal metabolic sensor	465:489	an ideal metabolic sensor	465:489	However, how O-GlcNAcylation, a posttranslational modification of proteins that is an ideal metabolic sensor, contributes to the commitment of HSCs to the erythroid lineage and to the terminal erythroid differentiation has not been addressed.
35739577	3	96	theme	posttranslational	414:430	arg1	modification					432:443	a posttranslational modification	412:443	a posttranslational modification of proteins that is an ideal metabolic sensor	412:489	However, how O-GlcNAcylation, a posttranslational modification of proteins that is an ideal metabolic sensor, contributes to the commitment of HSCs to the erythroid lineage and to the terminal erythroid differentiation has not been addressed.
35739577	3	96	theme	posttranslational	414:430	arg1	O-GlcNAcylation					395:409	O-GlcNAcylation	395:409	O-GlcNAcylation	395:409	However, how O-GlcNAcylation, a posttranslational modification of proteins that is an ideal metabolic sensor, contributes to the commitment of HSCs to the erythroid lineage and to the terminal erythroid differentiation has not been addressed.
35739577	7	97	theme	efficient	1668:1676	arg1	model					1683:1687	the efficient K562 model	1664:1687	the efficient K562 model of erythroid differentiation	1664:1716	Further studies in the efficient K562 model of erythroid differentiation confirmed that OGA inhibition and subsequent hyper-O-GlcNAcylation enhance terminal erythroid differentiation and affect globin production.
35739577	9	98	theme	erythroid	2180:2188	arg1	differentiation					2190:2204	erythroid differentiation	2180:2204	erythroid differentiation	2180:2204	Additionally, analysis of biochemical contents using synchrotron-based Fourier transform infrared (FTIR) spectroscopy showed unique metabolic fingerprints upon OGA inhibition during erythroid differentiation, supporting that metabolic reprogramming plays a part in this process.
35739577	4	99	theme	enzyme	748:753	arg1	transferase					764:774	enzyme O-GlcNAc transferase	748:774	enzyme O-GlcNAc transferase (OGT)	748:780	METHODS Cellular O-GlcNAcylation was manipulated using small molecule inhibition or CRISPR/Cas9 manipulation of catalyzing enzyme O-GlcNAc transferase (OGT) and removing enzyme O-GlcNAcase (OGA) in two cell models of erythroid differentiation, starting from: (i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells (HSPCs) to investigate the erythroid lineage specification and differentiation; and (ii) human-derived erythroblastic leukemia K562 cells to investigate the terminal differentiation.
35739577	4	99	theme	enzyme	748:753	arg1	OGT					777:779	OGT	777:779	OGT	777:779	METHODS Cellular O-GlcNAcylation was manipulated using small molecule inhibition or CRISPR/Cas9 manipulation of catalyzing enzyme O-GlcNAc transferase (OGT) and removing enzyme O-GlcNAcase (OGA) in two cell models of erythroid differentiation, starting from: (i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells (HSPCs) to investigate the erythroid lineage specification and differentiation; and (ii) human-derived erythroblastic leukemia K562 cells to investigate the terminal differentiation.
35739577	6	100	theme	level	1457:1461	arg1	dynamics					1436:1443	the observed dynamics	1423:1443	the observed dynamics of O-GlcNAc level	1423:1461	RESULTS First, we observed that two-step inhibition of OGT and OGA, which were established from the observed dynamics of O-GlcNAc level along the course of differentiation, promotes HSPCs toward erythroid differentiation and enucleation, in agreement with an upregulation of a multitude of erythroid-associated genes.
35739577	8	101	theme	erythroid	1933:1941	arg1	differentiation					1943:1957	O-GlcNAc-driven erythroid differentiation	1917:1957	O-GlcNAc-driven erythroid differentiation	1917:1957	Mechanistically, we found that BCL11A is a key mediator of O-GlcNAc-driven erythroid differentiation and β- and α-globin production herein.
35739577	11	102	theme	human	2726:2730	arg1	reticulocytes					2732:2744	functional human reticulocytes	2715:2744	functional human reticulocytes for transfusion from renewable cell sources, i.e., HSPCs and pluripotent stem cells	2715:2828	Our findings may lay the groundwork for future clinical applications toward an ex vivo production of functional human reticulocytes for transfusion from renewable cell sources, i.e., HSPCs and pluripotent stem cells.
35739577	7	103	theme	Further	1645:1651	arg1	studies					1653:1659	Further studies	1645:1659	Further studies in the efficient K562 model of erythroid differentiation	1645:1716	Further studies in the efficient K562 model of erythroid differentiation confirmed that OGA inhibition and subsequent hyper-O-GlcNAcylation enhance terminal erythroid differentiation and affect globin production.
35739577	11	104	theme	cell	2777:2780	arg1	sources					2782:2788	renewable cell sources	2767:2788	renewable cell sources	2767:2788	Our findings may lay the groundwork for future clinical applications toward an ex vivo production of functional human reticulocytes for transfusion from renewable cell sources, i.e., HSPCs and pluripotent stem cells.
35739577	6	105	theme	observed	1427:1434	arg1	dynamics					1436:1443	the observed dynamics	1423:1443	the observed dynamics of O-GlcNAc level	1423:1461	RESULTS First, we observed that two-step inhibition of OGT and OGA, which were established from the observed dynamics of O-GlcNAc level along the course of differentiation, promotes HSPCs toward erythroid differentiation and enucleation, in agreement with an upregulation of a multitude of erythroid-associated genes.
35739577	5	106	theme	regulatory	1167:1176	arg1	roles					1178:1182	The functional and regulatory roles	1148:1182	The functional and regulatory roles of O-GlcNAcylation in erythroid differentiation, maturation, and globin production	1148:1265	The functional and regulatory roles of O-GlcNAcylation in erythroid differentiation, maturation, and globin production were investigated, and downstream signaling was delineated.
35739577	7	107	theme	globin	1839:1844	arg1	production					1846:1855	globin production	1839:1855	globin production	1839:1855	Further studies in the efficient K562 model of erythroid differentiation confirmed that OGA inhibition and subsequent hyper-O-GlcNAcylation enhance terminal erythroid differentiation and affect globin production.
35739577	4	108	theme	lineage	1002:1008	arg1	specification					1010:1022	the erythroid lineage specification	988:1022	the erythroid lineage specification	988:1022	METHODS Cellular O-GlcNAcylation was manipulated using small molecule inhibition or CRISPR/Cas9 manipulation of catalyzing enzyme O-GlcNAc transferase (OGT) and removing enzyme O-GlcNAcase (OGA) in two cell models of erythroid differentiation, starting from: (i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells (HSPCs) to investigate the erythroid lineage specification and differentiation; and (ii) human-derived erythroblastic leukemia K562 cells to investigate the terminal differentiation.
35739577	11	109	theme	future	2654:2659	arg1	applications					2670:2681	future clinical applications	2654:2681	future clinical applications toward an ex vivo production of functional human reticulocytes for transfusion from renewable cell sources, i.e., HSPCs and pluripotent stem cells	2654:2828	Our findings may lay the groundwork for future clinical applications toward an ex vivo production of functional human reticulocytes for transfusion from renewable cell sources, i.e., HSPCs and pluripotent stem cells.
35739577	0	110	theme	sensor	10:15	arg1	O-GlcNAcylation					17:31	Metabolic sensor O-GlcNAcylation	0:31	Metabolic sensor O-GlcNAcylation	0:31	Metabolic sensor O-GlcNAcylation regulates erythroid differentiation and globin production via BCL11A.
35739577	8	111	theme	production	1979:1988	arg1	mediator					1905:1912	a key mediator	1899:1912	a key mediator of O-GlcNAc-driven erythroid differentiation and β- and α-globin production	1899:1988	Mechanistically, we found that BCL11A is a key mediator of O-GlcNAc-driven erythroid differentiation and β- and α-globin production herein.
35739577	8	111	theme	production	1979:1988	arg1	BCL11A					1889:1894	BCL11A	1889:1894	BCL11A	1889:1894	Mechanistically, we found that BCL11A is a key mediator of O-GlcNAc-driven erythroid differentiation and β- and α-globin production herein.
35739577	1	112	theme	BACKGROUND	103:112	arg1	process					169:175	a tightly regulated, multistep process	138:175	a tightly regulated, multistep process encompassing the differentiation of hematopoietic stem cells (HSCs) toward mature erythrocytes	138:270	BACKGROUND Human erythropoiesis is a tightly regulated, multistep process encompassing the differentiation of hematopoietic stem cells (HSCs) toward mature erythrocytes.
35739577	1	112	theme	BACKGROUND	103:112	arg1	erythropoiesis					120:133	BACKGROUND Human erythropoiesis	103:133	BACKGROUND Human erythropoiesis	103:133	BACKGROUND Human erythropoiesis is a tightly regulated, multistep process encompassing the differentiation of hematopoietic stem cells (HSCs) toward mature erythrocytes.
35739577	4	113	theme	erythroblastic	1068:1081	arg1	cells					1097:1101	(ii) human-derived erythroblastic leukemia K562 cells	1049:1101	(ii) human-derived erythroblastic leukemia K562 cells	1049:1101	METHODS Cellular O-GlcNAcylation was manipulated using small molecule inhibition or CRISPR/Cas9 manipulation of catalyzing enzyme O-GlcNAc transferase (OGT) and removing enzyme O-GlcNAcase (OGA) in two cell models of erythroid differentiation, starting from: (i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells (HSPCs) to investigate the erythroid lineage specification and differentiation; and (ii) human-derived erythroblastic leukemia K562 cells to investigate the terminal differentiation.
35739577	4	114	theme	enzyme	795:800	arg1	OGA					815:817	OGA	815:817	OGA	815:817	METHODS Cellular O-GlcNAcylation was manipulated using small molecule inhibition or CRISPR/Cas9 manipulation of catalyzing enzyme O-GlcNAc transferase (OGT) and removing enzyme O-GlcNAcase (OGA) in two cell models of erythroid differentiation, starting from: (i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells (HSPCs) to investigate the erythroid lineage specification and differentiation; and (ii) human-derived erythroblastic leukemia K562 cells to investigate the terminal differentiation.
35739577	4	114	theme	enzyme	795:800	arg1	O-GlcNAcase					802:812	removing enzyme O-GlcNAcase	786:812	removing enzyme O-GlcNAcase (OGA)	786:818	METHODS Cellular O-GlcNAcylation was manipulated using small molecule inhibition or CRISPR/Cas9 manipulation of catalyzing enzyme O-GlcNAc transferase (OGT) and removing enzyme O-GlcNAcase (OGA) in two cell models of erythroid differentiation, starting from: (i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells (HSPCs) to investigate the erythroid lineage specification and differentiation; and (ii) human-derived erythroblastic leukemia K562 cells to investigate the terminal differentiation.
35739577	3	115	theme	ideal	468:472	arg1	sensor					484:489	an ideal metabolic sensor	465:489	an ideal metabolic sensor	465:489	However, how O-GlcNAcylation, a posttranslational modification of proteins that is an ideal metabolic sensor, contributes to the commitment of HSCs to the erythroid lineage and to the terminal erythroid differentiation has not been addressed.
35739577	3	115	theme	ideal	468:472	arg1	modification					432:443	a posttranslational modification	412:443	a posttranslational modification of proteins that is an ideal metabolic sensor	412:489	However, how O-GlcNAcylation, a posttranslational modification of proteins that is an ideal metabolic sensor, contributes to the commitment of HSCs to the erythroid lineage and to the terminal erythroid differentiation has not been addressed.
35739577	3	115	theme	ideal	468:472	arg1	O-GlcNAcylation					395:409	O-GlcNAcylation	395:409	O-GlcNAcylation	395:409	However, how O-GlcNAcylation, a posttranslational modification of proteins that is an ideal metabolic sensor, contributes to the commitment of HSCs to the erythroid lineage and to the terminal erythroid differentiation has not been addressed.
35739577	10	116	theme	globin	2426:2431	arg1	production					2433:2442	globin production	2426:2442	globin production	2426:2442	CONCLUSIONS The evidence presented here demonstrated the novel regulatory role of O-GlcNAc/BCL11A axis in erythroid differentiation, maturation, and globin production that could be important in understanding erythropoiesis and hematologic disorders whose etiology is related to impaired erythroid differentiation and hemoglobinopathies.
35739577	7	117	theme	erythroid	1802:1810	arg1	differentiation					1812:1826	terminal erythroid differentiation	1793:1826	terminal erythroid differentiation	1793:1826	Further studies in the efficient K562 model of erythroid differentiation confirmed that OGA inhibition and subsequent hyper-O-GlcNAcylation enhance terminal erythroid differentiation and affect globin production.
35739577	4	118	theme	K562	1092:1095	arg1	cells					1097:1101	(ii) human-derived erythroblastic leukemia K562 cells	1049:1101	(ii) human-derived erythroblastic leukemia K562 cells	1049:1101	METHODS Cellular O-GlcNAcylation was manipulated using small molecule inhibition or CRISPR/Cas9 manipulation of catalyzing enzyme O-GlcNAc transferase (OGT) and removing enzyme O-GlcNAcase (OGA) in two cell models of erythroid differentiation, starting from: (i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells (HSPCs) to investigate the erythroid lineage specification and differentiation; and (ii) human-derived erythroblastic leukemia K562 cells to investigate the terminal differentiation.
35739577	10	119	theme	regulatory	2340:2349	arg1	role					2351:2354	the novel regulatory role	2330:2354	the novel regulatory role of O-GlcNAc/BCL11A axis in erythroid differentiation, maturation, and globin production that could be important in understanding erythropoiesis and hematologic disorders whose etiology is related to impaired erythroid differentiation and hemoglobinopathies	2330:2611	CONCLUSIONS The evidence presented here demonstrated the novel regulatory role of O-GlcNAc/BCL11A axis in erythroid differentiation, maturation, and globin production that could be important in understanding erythropoiesis and hematologic disorders whose etiology is related to impaired erythroid differentiation and hemoglobinopathies.
35739577	10	119	theme	regulatory	2340:2349	arg1	important					2458:2466	important	2458:2466	important	2458:2466	CONCLUSIONS The evidence presented here demonstrated the novel regulatory role of O-GlcNAc/BCL11A axis in erythroid differentiation, maturation, and globin production that could be important in understanding erythropoiesis and hematologic disorders whose etiology is related to impaired erythroid differentiation and hemoglobinopathies.
35739577	0	120	theme	globin	73:78	arg1	production					80:89	globin production	73:89	globin production	73:89	Metabolic sensor O-GlcNAcylation regulates erythroid differentiation and globin production via BCL11A.
35739577	3	121	theme	proteins	448:455	arg1	sensor					484:489	an ideal metabolic sensor	465:489	an ideal metabolic sensor	465:489	However, how O-GlcNAcylation, a posttranslational modification of proteins that is an ideal metabolic sensor, contributes to the commitment of HSCs to the erythroid lineage and to the terminal erythroid differentiation has not been addressed.
35739577	3	121	theme	proteins	448:455	arg1	modification					432:443	a posttranslational modification	412:443	a posttranslational modification of proteins that is an ideal metabolic sensor	412:489	However, how O-GlcNAcylation, a posttranslational modification of proteins that is an ideal metabolic sensor, contributes to the commitment of HSCs to the erythroid lineage and to the terminal erythroid differentiation has not been addressed.
35739577	3	121	theme	proteins	448:455	arg1	O-GlcNAcylation					395:409	O-GlcNAcylation	395:409	O-GlcNAcylation	395:409	However, how O-GlcNAcylation, a posttranslational modification of proteins that is an ideal metabolic sensor, contributes to the commitment of HSCs to the erythroid lineage and to the terminal erythroid differentiation has not been addressed.
35739577	2	122	theme	HSCs	376:379	arg1	differentiation					357:371	the differentiation	353:371	the differentiation of HSCs	353:379	Cellular metabolism is an important regulator of cell fate determination during the differentiation of HSCs.
35739577	1	123	theme	mature	252:257	arg1	erythrocytes					259:270	mature erythrocytes	252:270	mature erythrocytes	252:270	BACKGROUND Human erythropoiesis is a tightly regulated, multistep process encompassing the differentiation of hematopoietic stem cells (HSCs) toward mature erythrocytes.
35739577	9	124	theme	biochemical	2024:2034	arg1	contents					2036:2043	biochemical contents	2024:2043	biochemical contents	2024:2043	Additionally, analysis of biochemical contents using synchrotron-based Fourier transform infrared (FTIR) spectroscopy showed unique metabolic fingerprints upon OGA inhibition during erythroid differentiation, supporting that metabolic reprogramming plays a part in this process.
35739577	4	125	theme	erythroid	842:850	arg1	differentiation					852:866	erythroid differentiation	842:866	erythroid differentiation	842:866	METHODS Cellular O-GlcNAcylation was manipulated using small molecule inhibition or CRISPR/Cas9 manipulation of catalyzing enzyme O-GlcNAc transferase (OGT) and removing enzyme O-GlcNAcase (OGA) in two cell models of erythroid differentiation, starting from: (i) human umbilical cord blood-derived CD34+ hematopoietic stem/progenitor cells (HSPCs) to investigate the erythroid lineage specification and differentiation; and (ii) human-derived erythroblastic leukemia K562 cells to investigate the terminal differentiation.
35739577	5	126	from	roles	1178:1182	arg1	production					1256:1265	globin production	1249:1265	globin production	1249:1265	The functional and regulatory roles of O-GlcNAcylation in erythroid differentiation, maturation, and globin production were investigated, and downstream signaling was delineated.
35739577	5	126	from	roles	1178:1182	arg1	maturation					1233:1242	maturation	1233:1242	maturation	1233:1242	The functional and regulatory roles of O-GlcNAcylation in erythroid differentiation, maturation, and globin production were investigated, and downstream signaling was delineated.
35739577	5	126	from	roles	1178:1182	arg1	differentiation					1216:1230	erythroid differentiation	1206:1230	erythroid differentiation	1206:1230	The functional and regulatory roles of O-GlcNAcylation in erythroid differentiation, maturation, and globin production were investigated, and downstream signaling was delineated.
29689198	6	0	theme	autophagic	673:682	arg1	flux					684:687	autophagic flux	673:687	autophagic flux	673:687	GRASP55 depletion reduces autophagic flux and results in autophagosome accumulation, while expression of an O-GlcNAcylation-deficient mutant of GRASP55 accelerates autophagic flux.
29689198	7	1	dep	autophagosomes	880:893	arg1	the					876:878	the	876:878	the	876:878	Biochemically, GRASP55 interacts with LC3-II on the autophagosomes and LAMP2 on late endosomes/lysosomes and functions as a bridge between LC3-II and LAMP2 for autophagosome and lysosome fusion; this function is negatively regulated by GRASP55 O-GlcNAcylation.
29689198	8	2	theme	glucose	1115:1121	arg1	levels					1123:1128	glucose levels	1115:1128	glucose levels	1115:1128	Therefore, GRASP55 senses glucose levels through O-GlcNAcylation and acts as a tether to facilitate autophagosome maturation.
29689198	5	3	theme	late	621:624	arg1	endosomes/lysosomes					626:644	late endosomes/lysosomes	621:644	late endosomes/lysosomes	621:644	De-O-GlcNAcylated GRASP55 forms puncta outside of the Golgi area, which co-localize with autophagosomes and late endosomes/lysosomes.
29689198	8	4	theme	O-GlcNAcylation	1138:1152	arg1	and acts					1154:1161	O-GlcNAcylation and acts	1138:1161	O-GlcNAcylation and acts	1138:1161	Therefore, GRASP55 senses glucose levels through O-GlcNAcylation and acts as a tether to facilitate autophagosome maturation.
29689198	7	5	from	LC3-II	866:871	arg1	LAMP2					899:903	LAMP2	899:903	LAMP2	899:903	Biochemically, GRASP55 interacts with LC3-II on the autophagosomes and LAMP2 on late endosomes/lysosomes and functions as a bridge between LC3-II and LAMP2 for autophagosome and lysosome fusion; this function is negatively regulated by GRASP55 O-GlcNAcylation.
29689198	7	5	from	LC3-II	866:871	arg1	autophagosomes					880:893	autophagosomes	880:893	autophagosomes	880:893	Biochemically, GRASP55 interacts with LC3-II on the autophagosomes and LAMP2 on late endosomes/lysosomes and functions as a bridge between LC3-II and LAMP2 for autophagosome and lysosome fusion; this function is negatively regulated by GRASP55 O-GlcNAcylation.
29689198	1	6	dep	protein	144:150	arg1	trafficking					152:162	trafficking	152:162	trafficking	152:162	The Golgi apparatus is the central hub for protein trafficking and glycosylation in the secretory pathway.
29689198	6	7	theme	mutant	781:786	arg1	expression					738:747	expression	738:747	expression of an O-GlcNAcylation-deficient mutant of GRASP55	738:797	GRASP55 depletion reduces autophagic flux and results in autophagosome accumulation, while expression of an O-GlcNAcylation-deficient mutant of GRASP55 accelerates autophagic flux.
29689198	6	8	theme	O-GlcNAcylation-deficient	755:779	arg1	mutant					781:786	an O-GlcNAcylation-deficient mutant	752:786	an O-GlcNAcylation-deficient mutant of GRASP55	752:797	GRASP55 depletion reduces autophagic flux and results in autophagosome accumulation, while expression of an O-GlcNAcylation-deficient mutant of GRASP55 accelerates autophagic flux.
29689198	5	9	theme	De-O-GlcNAcylated	513:529	arg1	GRASP55					531:537	De-O-GlcNAcylated GRASP55	513:537	De-O-GlcNAcylated GRASP55	513:537	De-O-GlcNAcylated GRASP55 forms puncta outside of the Golgi area, which co-localize with autophagosomes and late endosomes/lysosomes.
29689198	3	10	theme	located	339:345	arg1	protein					331:337	the Golgi stacking protein	312:337	the Golgi stacking protein located in medial- and trans-Golgi cisternae	312:382	Here, we report that GRASP55, the Golgi stacking protein located in medial- and trans-Golgi cisternae, is O-GlcNAcylated by the O-GlcNAc transferase OGT under growth conditions.
29689198	3	10	theme	located	339:345	arg1	GRASP55					303:309	GRASP55	303:309	GRASP55	303:309	Here, we report that GRASP55, the Golgi stacking protein located in medial- and trans-Golgi cisternae, is O-GlcNAcylated by the O-GlcNAc transferase OGT under growth conditions.
29689198	3	11	from	cisternae	374:382	arg1	located					339:345	located	339:345	located	339:345	Here, we report that GRASP55, the Golgi stacking protein located in medial- and trans-Golgi cisternae, is O-GlcNAcylated by the O-GlcNAc transferase OGT under growth conditions.
29689198	1	12	theme	secretory	189:197	arg1	pathway					199:205	the secretory pathway	185:205	the secretory pathway	185:205	The Golgi apparatus is the central hub for protein trafficking and glycosylation in the secretory pathway.
29689198	6	13	theme	GRASP55	647:653	arg1	depletion					655:663	GRASP55 depletion	647:663	GRASP55 depletion	647:663	GRASP55 depletion reduces autophagic flux and results in autophagosome accumulation, while expression of an O-GlcNAcylation-deficient mutant of GRASP55 accelerates autophagic flux.
29689198	4	14	theme	GRASP55	488:494	arg1	O-GlcNAcylation					496:510	GRASP55 O-GlcNAcylation	488:510	GRASP55 O-GlcNAcylation	488:510	Glucose deprivation reduces GRASP55 O-GlcNAcylation.
29689198	7	15	from	autophagosomes	880:893	arg1	endosomes/lysosomes					913:931	late endosomes/lysosomes	908:931	late endosomes/lysosomes	908:931	Biochemically, GRASP55 interacts with LC3-II on the autophagosomes and LAMP2 on late endosomes/lysosomes and functions as a bridge between LC3-II and LAMP2 for autophagosome and lysosome fusion; this function is negatively regulated by GRASP55 O-GlcNAcylation.
29689198	1	16	theme	Golgi	105:109	arg1	apparatus					111:119	The Golgi apparatus	101:119	The Golgi apparatus	101:119	The Golgi apparatus is the central hub for protein trafficking and glycosylation in the secretory pathway.
29689198	1	16	theme	Golgi	105:109	arg1	hub					136:138	the central hub	124:138	the central hub for protein trafficking and glycosylation in the secretory pathway	124:205	The Golgi apparatus is the central hub for protein trafficking and glycosylation in the secretory pathway.
29689198	3	17	theme	O-GlcNAc	410:417	arg1	OGT					431:433	the O-GlcNAc transferase OGT	406:433	the O-GlcNAc transferase OGT	406:433	Here, we report that GRASP55, the Golgi stacking protein located in medial- and trans-Golgi cisternae, is O-GlcNAcylated by the O-GlcNAc transferase OGT under growth conditions.
29689198	7	18	theme	lysosome	1006:1013	arg1	fusion					1015:1020	lysosome fusion	1006:1020	lysosome fusion	1006:1020	Biochemically, GRASP55 interacts with LC3-II on the autophagosomes and LAMP2 on late endosomes/lysosomes and functions as a bridge between LC3-II and LAMP2 for autophagosome and lysosome fusion; this function is negatively regulated by GRASP55 O-GlcNAcylation.
29689198	7	19	theme	late	908:911	arg1	endosomes/lysosomes					913:931	late endosomes/lysosomes	908:931	late endosomes/lysosomes	908:931	Biochemically, GRASP55 interacts with LC3-II on the autophagosomes and LAMP2 on late endosomes/lysosomes and functions as a bridge between LC3-II and LAMP2 for autophagosome and lysosome fusion; this function is negatively regulated by GRASP55 O-GlcNAcylation.
29689198	3	20	theme	transferase	419:429	arg1	OGT					431:433	the O-GlcNAc transferase OGT	406:433	the O-GlcNAc transferase OGT	406:433	Here, we report that GRASP55, the Golgi stacking protein located in medial- and trans-Golgi cisternae, is O-GlcNAcylated by the O-GlcNAc transferase OGT under growth conditions.
29689198	1	21	from	hub	136:138	arg1	pathway					199:205	the secretory pathway	185:205	the secretory pathway	185:205	The Golgi apparatus is the central hub for protein trafficking and glycosylation in the secretory pathway.
29689198	7	22	from	LAMP2	899:903	arg1	endosomes/lysosomes					913:931	late endosomes/lysosomes	908:931	late endosomes/lysosomes	908:931	Biochemically, GRASP55 interacts with LC3-II on the autophagosomes and LAMP2 on late endosomes/lysosomes and functions as a bridge between LC3-II and LAMP2 for autophagosome and lysosome fusion; this function is negatively regulated by GRASP55 O-GlcNAcylation.
29689198	3	23	theme	trans-Golgi	362:372	arg1	cisternae					374:382	trans-Golgi cisternae	362:382	trans-Golgi cisternae	362:382	Here, we report that GRASP55, the Golgi stacking protein located in medial- and trans-Golgi cisternae, is O-GlcNAcylated by the O-GlcNAc transferase OGT under growth conditions.
29689198	0	24	theme	Autophagosome-Lysosome	70:91	arg1	Fusion					93:98	Autophagosome-Lysosome Fusion	70:98	Autophagosome-Lysosome Fusion	70:98	GRASP55 Senses Glucose Deprivation through O-GlcNAcylation to Promote Autophagosome-Lysosome Fusion.
29689198	3	25	from	located	339:345	arg1	cisternae					374:382	trans-Golgi cisternae	362:382	trans-Golgi cisternae	362:382	Here, we report that GRASP55, the Golgi stacking protein located in medial- and trans-Golgi cisternae, is O-GlcNAcylated by the O-GlcNAc transferase OGT under growth conditions.
29689198	3	25	from	located	339:345	arg1	medial-					350:356	medial-	350:356	medial-	350:356	Here, we report that GRASP55, the Golgi stacking protein located in medial- and trans-Golgi cisternae, is O-GlcNAcylated by the O-GlcNAc transferase OGT under growth conditions.
29689198	2	26	theme	glucose	243:249	arg1	deprivation					251:261	glucose deprivation	243:261	glucose deprivation	243:261	However, how the Golgi responds to glucose deprivation is so far unknown.
29689198	3	27	theme	growth	441:446	arg1	conditions					448:457	growth conditions	441:457	growth conditions	441:457	Here, we report that GRASP55, the Golgi stacking protein located in medial- and trans-Golgi cisternae, is O-GlcNAcylated by the O-GlcNAc transferase OGT under growth conditions.
29689198	8	28	theme	autophagosome	1189:1201	arg1	maturation					1203:1212	autophagosome maturation	1189:1212	autophagosome maturation	1189:1212	Therefore, GRASP55 senses glucose levels through O-GlcNAcylation and acts as a tether to facilitate autophagosome maturation.
29689198	4	29	theme	Glucose	460:466	arg1	deprivation					468:478	Glucose deprivation	460:478	Glucose deprivation	460:478	Glucose deprivation reduces GRASP55 O-GlcNAcylation.
29689198	5	30	theme	Golgi	567:571	arg1	area					573:576	the Golgi area	563:576	the Golgi area	563:576	De-O-GlcNAcylated GRASP55 forms puncta outside of the Golgi area, which co-localize with autophagosomes and late endosomes/lysosomes.
29689198	3	31	from	medial-	350:356	arg1	located					339:345	located	339:345	located	339:345	Here, we report that GRASP55, the Golgi stacking protein located in medial- and trans-Golgi cisternae, is O-GlcNAcylated by the O-GlcNAc transferase OGT under growth conditions.
29689198	1	32	theme	central	128:134	arg1	apparatus					111:119	The Golgi apparatus	101:119	The Golgi apparatus	101:119	The Golgi apparatus is the central hub for protein trafficking and glycosylation in the secretory pathway.
29689198	1	32	theme	central	128:134	arg1	hub					136:138	the central hub	124:138	the central hub for protein trafficking and glycosylation in the secretory pathway	124:205	The Golgi apparatus is the central hub for protein trafficking and glycosylation in the secretory pathway.
29689198	6	33	theme	autophagosome	704:716	arg1	accumulation					718:729	autophagosome accumulation	704:729	autophagosome accumulation	704:729	GRASP55 depletion reduces autophagic flux and results in autophagosome accumulation, while expression of an O-GlcNAcylation-deficient mutant of GRASP55 accelerates autophagic flux.
29689198	6	34	theme	autophagic	811:820	arg1	flux					822:825	autophagic flux	811:825	autophagic flux	811:825	GRASP55 depletion reduces autophagic flux and results in autophagosome accumulation, while expression of an O-GlcNAcylation-deficient mutant of GRASP55 accelerates autophagic flux.
29689198	3	35	theme	Golgi	316:320	arg1	protein					331:337	the Golgi stacking protein	312:337	the Golgi stacking protein located in medial- and trans-Golgi cisternae	312:382	Here, we report that GRASP55, the Golgi stacking protein located in medial- and trans-Golgi cisternae, is O-GlcNAcylated by the O-GlcNAc transferase OGT under growth conditions.
29689198	3	35	theme	Golgi	316:320	arg1	GRASP55					303:309	GRASP55	303:309	GRASP55	303:309	Here, we report that GRASP55, the Golgi stacking protein located in medial- and trans-Golgi cisternae, is O-GlcNAcylated by the O-GlcNAc transferase OGT under growth conditions.
29689198	3	36	theme	stacking	322:329	arg1	protein					331:337	the Golgi stacking protein	312:337	the Golgi stacking protein located in medial- and trans-Golgi cisternae	312:382	Here, we report that GRASP55, the Golgi stacking protein located in medial- and trans-Golgi cisternae, is O-GlcNAcylated by the O-GlcNAc transferase OGT under growth conditions.
29689198	3	36	theme	stacking	322:329	arg1	GRASP55					303:309	GRASP55	303:309	GRASP55	303:309	Here, we report that GRASP55, the Golgi stacking protein located in medial- and trans-Golgi cisternae, is O-GlcNAcylated by the O-GlcNAc transferase OGT under growth conditions.
29689198	0	37	theme	Glucose	15:21	arg1	Deprivation					23:33	Glucose Deprivation	15:33	Glucose Deprivation	15:33	GRASP55 Senses Glucose Deprivation through O-GlcNAcylation to Promote Autophagosome-Lysosome Fusion.
29689198	6	38	theme	GRASP55	791:797	arg1	mutant					781:786	an O-GlcNAcylation-deficient mutant	752:786	an O-GlcNAcylation-deficient mutant of GRASP55	752:797	GRASP55 depletion reduces autophagic flux and results in autophagosome accumulation, while expression of an O-GlcNAcylation-deficient mutant of GRASP55 accelerates autophagic flux.
26315267	9	0	theme	TXNIP	1311:1315	arg1	expression					1317:1326	2DG induced TXNIP expression	1299:1326	2DG induced TXNIP expression	1299:1326	We have shown that 2DG induced TXNIP expression is independent of carbohydrate response element mediated transcription.
26315267	6	1	theme	thioredoxin	861:871	arg1	protein					885:891	thioredoxin interacting protein	861:891	thioredoxin interacting protein (TXNIP)	861:899	In addition, 2DG is also known to induce the expression of thioredoxin interacting protein (TXNIP), a tumor suppressor protein and an important negative regulator of cellular glucose uptake.
26315267	6	1	theme	thioredoxin	861:871	arg1	protein					921:927	a tumor suppressor protein	902:927	a tumor suppressor protein	902:927	In addition, 2DG is also known to induce the expression of thioredoxin interacting protein (TXNIP), a tumor suppressor protein and an important negative regulator of cellular glucose uptake.
26315267	6	1	theme	thioredoxin	861:871	arg1	TXNIP					894:898	TXNIP	894:898	TXNIP	894:898	In addition, 2DG is also known to induce the expression of thioredoxin interacting protein (TXNIP), a tumor suppressor protein and an important negative regulator of cellular glucose uptake.
26315267	8	2	theme	TXNIP	1262:1266	arg1	regulation					1268:1277	the 2DG dependent TXNIP regulation	1244:1277	the 2DG dependent TXNIP regulation	1244:1277	Therefore, in this study we sought to test various hypotheses for the mechanistic basis of the 2DG dependent TXNIP regulation.
26315267	7	3	theme	mechanism	1024:1032	arg1	characterization					1000:1015	characterization	1000:1015	characterization of the mechanism through which 2DG regulates TXNIP expression	1000:1077	Hence, characterization of the mechanism through which 2DG regulates TXNIP expression may reveal novel approaches to target the Warburg effect in cancer cells.
26315267	6	4	theme	uptake	985:990	arg1	expression					847:856	the expression	843:856	the expression of thioredoxin interacting protein (TXNIP), a tumor suppressor protein	843:927	In addition, 2DG is also known to induce the expression of thioredoxin interacting protein (TXNIP), a tumor suppressor protein and an important negative regulator of cellular glucose uptake.
26315267	6	4	theme	uptake	985:990	arg1	regulator					955:963	an important negative regulator	933:963	an important negative regulator of cellular glucose uptake	933:990	In addition, 2DG is also known to induce the expression of thioredoxin interacting protein (TXNIP), a tumor suppressor protein and an important negative regulator of cellular glucose uptake.
26315267	10	5	theme	2DG	1475:1477	arg1	ability					1464:1470	the ability	1460:1470	the ability of 2DG to deplete cellular ATP nor to cause endoplasmic reticulum stress	1460:1543	Furthermore, the induction of TXNIP is neither dependent on the ability of 2DG to deplete cellular ATP nor to cause endoplasmic reticulum stress.
26315267	10	6	theme	TXNIP	1430:1434	arg1	dependent					1447:1455	dependent	1447:1455	dependent	1447:1455	Furthermore, the induction of TXNIP is neither dependent on the ability of 2DG to deplete cellular ATP nor to cause endoplasmic reticulum stress.
26315267	10	6	theme	TXNIP	1430:1434	arg1	induction					1417:1425	the induction	1413:1425	the induction of TXNIP	1413:1434	Furthermore, the induction of TXNIP is neither dependent on the ability of 2DG to deplete cellular ATP nor to cause endoplasmic reticulum stress.
26315267	2	7	from	mechanism	327:335	arg1	cells					374:378	cancer cells	367:378	cancer cells	367:378	The major mechanism of metabolic reprogramming in cancer cells is the Warburg effect, defined as the preferential utilization of glucose via glycolysis even in the presence of oxygen.
26315267	2	8	theme	reprogramming	350:362	arg1	effect					395:400	the Warburg effect	383:400	the Warburg effect	383:400	The major mechanism of metabolic reprogramming in cancer cells is the Warburg effect, defined as the preferential utilization of glucose via glycolysis even in the presence of oxygen.
26315267	2	8	theme	reprogramming	350:362	arg1	mechanism					327:335	The major mechanism	317:335	The major mechanism of metabolic reprogramming in cancer cells	317:378	The major mechanism of metabolic reprogramming in cancer cells is the Warburg effect, defined as the preferential utilization of glucose via glycolysis even in the presence of oxygen.
26315267	1	9	theme	tumor	252:256	arg1	tissue					258:263	the tumor tissue	248:263	the tumor tissue	248:263	The high proliferation rate of cancer cells and the microenvironment in the tumor tissue require the reprogramming of tumor cell metabolism.
26315267	9	10	dep	induced	1303:1309	arg1	2DG					1299:1301	2DG	1299:1301	2DG	1299:1301	We have shown that 2DG induced TXNIP expression is independent of carbohydrate response element mediated transcription.
26315267	9	11	theme	carbohydrate	1346:1357	arg1	element					1368:1374	carbohydrate response element	1346:1374	carbohydrate response element	1346:1374	We have shown that 2DG induced TXNIP expression is independent of carbohydrate response element mediated transcription.
26315267	6	12	theme	cellular	968:975	arg1	uptake					985:990	cellular glucose uptake	968:990	cellular glucose uptake	968:990	In addition, 2DG is also known to induce the expression of thioredoxin interacting protein (TXNIP), a tumor suppressor protein and an important negative regulator of cellular glucose uptake.
26315267	10	13	dep	ability	1464:1470	arg1	cause					1510:1514	cause	1510:1514	to cause endoplasmic reticulum stress	1507:1543	Furthermore, the induction of TXNIP is neither dependent on the ability of 2DG to deplete cellular ATP nor to cause endoplasmic reticulum stress.
26315267	10	13	dep	ability	1464:1470	arg1	deplete					1482:1488	deplete	1482:1488	to deplete cellular ATP	1479:1501	Furthermore, the induction of TXNIP is neither dependent on the ability of 2DG to deplete cellular ATP nor to cause endoplasmic reticulum stress.
26315267	11	14	theme	induced	1568:1574	arg1	expression					1582:1591	the 2DG induced TXNIP expression	1560:1591	the 2DG induced TXNIP expression	1560:1591	We found that the 2DG induced TXNIP expression is at least in part dependent on the inhibition of the O-GlcNAcase enzyme and the accumulation of O-GlcNAc modified proteins.
26315267	11	14	theme	induced	1568:1574	arg1	dependent					1613:1621	dependent	1613:1621	dependent	1613:1621	We found that the 2DG induced TXNIP expression is at least in part dependent on the inhibition of the O-GlcNAcase enzyme and the accumulation of O-GlcNAc modified proteins.
26315267	12	15	theme	TXNIP	1809:1813	arg1	expression					1815:1824	TXNIP expression	1809:1824	TXNIP expression in cancer	1809:1834	These results have implications for the identification of therapeutic targets to increase TXNIP expression in cancer.
26315267	0	16	from	effect	152:157	arg1	cells					169:173	cancer cells	162:173	cancer cells	162:173	2-Deoxyglucose induces the expression of thioredoxin interacting protein (TXNIP) by increasing O-GlcNAcylation - Implications for targeting the Warburg effect in cancer cells.
26315267	6	17	theme	protein	885:891	arg1	expression					847:856	the expression	843:856	the expression of thioredoxin interacting protein (TXNIP), a tumor suppressor protein	843:927	In addition, 2DG is also known to induce the expression of thioredoxin interacting protein (TXNIP), a tumor suppressor protein and an important negative regulator of cellular glucose uptake.
26315267	6	17	theme	protein	885:891	arg1	regulator					955:963	an important negative regulator	933:963	an important negative regulator of cellular glucose uptake	933:990	In addition, 2DG is also known to induce the expression of thioredoxin interacting protein (TXNIP), a tumor suppressor protein and an important negative regulator of cellular glucose uptake.
26315267	10	18	theme	endoplasmic	1516:1526	arg1	reticulum					1528:1536	endoplasmic reticulum	1516:1536	endoplasmic reticulum stress	1516:1543	Furthermore, the induction of TXNIP is neither dependent on the ability of 2DG to deplete cellular ATP nor to cause endoplasmic reticulum stress.
26315267	8	19	theme	mechanistic	1223:1233	arg1	basis					1235:1239	the mechanistic basis	1219:1239	the mechanistic basis of the 2DG dependent TXNIP regulation	1219:1277	Therefore, in this study we sought to test various hypotheses for the mechanistic basis of the 2DG dependent TXNIP regulation.
26315267	12	20	theme	targets	1789:1795	arg1	identification					1759:1772	the identification	1755:1772	the identification of therapeutic targets to increase TXNIP expression in cancer	1755:1834	These results have implications for the identification of therapeutic targets to increase TXNIP expression in cancer.
26315267	7	21	theme	Warburg	1121:1127	arg1	effect					1129:1134	the Warburg effect	1117:1134	the Warburg effect	1117:1134	Hence, characterization of the mechanism through which 2DG regulates TXNIP expression may reveal novel approaches to target the Warburg effect in cancer cells.
26315267	6	22	theme	interacting	873:883	arg1	protein					885:891	thioredoxin interacting protein	861:891	thioredoxin interacting protein (TXNIP)	861:899	In addition, 2DG is also known to induce the expression of thioredoxin interacting protein (TXNIP), a tumor suppressor protein and an important negative regulator of cellular glucose uptake.
26315267	6	22	theme	interacting	873:883	arg1	protein					921:927	a tumor suppressor protein	902:927	a tumor suppressor protein	902:927	In addition, 2DG is also known to induce the expression of thioredoxin interacting protein (TXNIP), a tumor suppressor protein and an important negative regulator of cellular glucose uptake.
26315267	6	22	theme	interacting	873:883	arg1	TXNIP					894:898	TXNIP	894:898	TXNIP	894:898	In addition, 2DG is also known to induce the expression of thioredoxin interacting protein (TXNIP), a tumor suppressor protein and an important negative regulator of cellular glucose uptake.
26315267	5	23	theme	hexokinase	764:773	arg1	level					755:759	the level	751:759	the level of hexokinase and phosphoglucoisomerase	751:799	2DG exerts its effect by directly inhibiting glycolysis at the level of hexokinase and phosphoglucoisomerase.
26315267	11	24	from	part	1608:1611	arg1	expression					1582:1591	the 2DG induced TXNIP expression	1560:1591	the 2DG induced TXNIP expression	1560:1591	We found that the 2DG induced TXNIP expression is at least in part dependent on the inhibition of the O-GlcNAcase enzyme and the accumulation of O-GlcNAc modified proteins.
26315267	11	24	from	part	1608:1611	arg1	dependent					1613:1621	dependent	1613:1621	dependent	1613:1621	We found that the 2DG induced TXNIP expression is at least in part dependent on the inhibition of the O-GlcNAcase enzyme and the accumulation of O-GlcNAc modified proteins.
26315267	2	25	theme	Warburg	387:393	arg1	effect					395:400	the Warburg effect	383:400	the Warburg effect	383:400	The major mechanism of metabolic reprogramming in cancer cells is the Warburg effect, defined as the preferential utilization of glucose via glycolysis even in the presence of oxygen.
26315267	2	25	theme	Warburg	387:393	arg1	mechanism					327:335	The major mechanism	317:335	The major mechanism of metabolic reprogramming in cancer cells	317:378	The major mechanism of metabolic reprogramming in cancer cells is the Warburg effect, defined as the preferential utilization of glucose via glycolysis even in the presence of oxygen.
26315267	2	26	theme	glucose	446:452	arg1	utilization					431:441	the preferential utilization	414:441	the preferential utilization of glucose	414:452	The major mechanism of metabolic reprogramming in cancer cells is the Warburg effect, defined as the preferential utilization of glucose via glycolysis even in the presence of oxygen.
26315267	3	27	theme	Warburg	515:521	arg1	effect					523:528	the Warburg effect	511:528	the Warburg effect	511:528	Targeting the Warburg effect is considered as a promising therapeutic strategy in cancer therapy.
26315267	10	28	theme	reticulum	1528:1536	arg1	stress					1538:1543	endoplasmic reticulum stress	1516:1543	endoplasmic reticulum stress	1516:1543	Furthermore, the induction of TXNIP is neither dependent on the ability of 2DG to deplete cellular ATP nor to cause endoplasmic reticulum stress.
26315267	3	29	theme	therapeutic	559:569	arg1	strategy					571:578	a promising therapeutic strategy	547:578	a promising therapeutic strategy in cancer therapy	547:596	Targeting the Warburg effect is considered as a promising therapeutic strategy in cancer therapy.
26315267	11	30	dep	induced	1568:1574	arg1	2DG					1564:1566	2DG	1564:1566	2DG	1564:1566	We found that the 2DG induced TXNIP expression is at least in part dependent on the inhibition of the O-GlcNAcase enzyme and the accumulation of O-GlcNAc modified proteins.
26315267	1	31	theme	high	180:183	arg1	rate					199:202	The high proliferation rate	176:202	The high proliferation rate of cancer cells	176:218	The high proliferation rate of cancer cells and the microenvironment in the tumor tissue require the reprogramming of tumor cell metabolism.
26315267	1	32	theme	proliferation	185:197	arg1	rate					199:202	The high proliferation rate	176:202	The high proliferation rate of cancer cells	176:218	The high proliferation rate of cancer cells and the microenvironment in the tumor tissue require the reprogramming of tumor cell metabolism.
26315267	6	33	theme	negative	946:953	arg1	regulator					955:963	an important negative regulator	933:963	an important negative regulator of cellular glucose uptake	933:990	In addition, 2DG is also known to induce the expression of thioredoxin interacting protein (TXNIP), a tumor suppressor protein and an important negative regulator of cellular glucose uptake.
26315267	8	34	theme	regulation	1268:1277	arg1	basis					1235:1239	the mechanistic basis	1219:1239	the mechanistic basis of the 2DG dependent TXNIP regulation	1219:1277	Therefore, in this study we sought to test various hypotheses for the mechanistic basis of the 2DG dependent TXNIP regulation.
26315267	7	35	theme	novel	1090:1094	arg1	approaches					1096:1105	novel approaches	1090:1105	novel approaches	1090:1105	Hence, characterization of the mechanism through which 2DG regulates TXNIP expression may reveal novel approaches to target the Warburg effect in cancer cells.
26315267	4	36	theme	glycolytic	619:628	arg1	2DG					656:658	2DG	656:658	2DG	656:658	In this regard, the glycolytic inhibitor 2-deoxyglucose (2DG) has been evaluated clinically.
26315267	4	36	theme	glycolytic	619:628	arg1	2-deoxyglucose					640:653	the glycolytic inhibitor 2-deoxyglucose	615:653	the glycolytic inhibitor 2-deoxyglucose (2DG)	615:659	In this regard, the glycolytic inhibitor 2-deoxyglucose (2DG) has been evaluated clinically.
26315267	2	37	theme	preferential	418:429	arg1	utilization					431:441	the preferential utilization	414:441	the preferential utilization of glucose	414:452	The major mechanism of metabolic reprogramming in cancer cells is the Warburg effect, defined as the preferential utilization of glucose via glycolysis even in the presence of oxygen.
26315267	6	38	theme	important	936:944	arg1	regulator					955:963	an important negative regulator	933:963	an important negative regulator of cellular glucose uptake	933:990	In addition, 2DG is also known to induce the expression of thioredoxin interacting protein (TXNIP), a tumor suppressor protein and an important negative regulator of cellular glucose uptake.
26315267	7	39	theme	TXNIP	1062:1066	arg1	expression					1068:1077	TXNIP expression	1062:1077	TXNIP expression	1062:1077	Hence, characterization of the mechanism through which 2DG regulates TXNIP expression may reveal novel approaches to target the Warburg effect in cancer cells.
26315267	11	40	theme	enzyme	1660:1665	arg1	accumulation					1675:1686	the accumulation	1671:1686	the accumulation of O-GlcNAc modified proteins	1671:1716	We found that the 2DG induced TXNIP expression is at least in part dependent on the inhibition of the O-GlcNAcase enzyme and the accumulation of O-GlcNAc modified proteins.
26315267	11	40	theme	enzyme	1660:1665	arg1	inhibition					1630:1639	the inhibition	1626:1639	the inhibition of the O-GlcNAcase enzyme	1626:1665	We found that the 2DG induced TXNIP expression is at least in part dependent on the inhibition of the O-GlcNAcase enzyme and the accumulation of O-GlcNAc modified proteins.
26315267	3	41	theme	promising	549:557	arg1	strategy					571:578	a promising therapeutic strategy	547:578	a promising therapeutic strategy in cancer therapy	547:596	Targeting the Warburg effect is considered as a promising therapeutic strategy in cancer therapy.
26315267	0	42	theme	thioredoxin	41:51	arg1	TXNIP					74:78	TXNIP	74:78	TXNIP	74:78	2-Deoxyglucose induces the expression of thioredoxin interacting protein (TXNIP) by increasing O-GlcNAcylation - Implications for targeting the Warburg effect in cancer cells.
26315267	0	42	theme	thioredoxin	41:51	arg1	protein					65:71	thioredoxin interacting protein	41:71	thioredoxin interacting protein (TXNIP)	41:79	2-Deoxyglucose induces the expression of thioredoxin interacting protein (TXNIP) by increasing O-GlcNAcylation - Implications for targeting the Warburg effect in cancer cells.
26315267	1	43	theme	tumor	294:298	arg1	metabolism					305:314	tumor cell metabolism	294:314	tumor cell metabolism	294:314	The high proliferation rate of cancer cells and the microenvironment in the tumor tissue require the reprogramming of tumor cell metabolism.
26315267	0	44	theme	Warburg	144:150	arg1	effect					152:157	the Warburg effect	140:157	the Warburg effect in cancer cells	140:173	2-Deoxyglucose induces the expression of thioredoxin interacting protein (TXNIP) by increasing O-GlcNAcylation - Implications for targeting the Warburg effect in cancer cells.
26315267	1	45	theme	cancer	207:212	arg1	cells					214:218	cancer cells	207:218	cancer cells	207:218	The high proliferation rate of cancer cells and the microenvironment in the tumor tissue require the reprogramming of tumor cell metabolism.
26315267	7	46	theme	cancer	1139:1144	arg1	cells					1146:1150	cancer cells	1139:1150	cancer cells	1139:1150	Hence, characterization of the mechanism through which 2DG regulates TXNIP expression may reveal novel approaches to target the Warburg effect in cancer cells.
26315267	1	47	theme	cell	300:303	arg1	metabolism					305:314	tumor cell metabolism	294:314	tumor cell metabolism	294:314	The high proliferation rate of cancer cells and the microenvironment in the tumor tissue require the reprogramming of tumor cell metabolism.
26315267	6	48	theme	glucose	977:983	arg1	uptake					985:990	cellular glucose uptake	968:990	cellular glucose uptake	968:990	In addition, 2DG is also known to induce the expression of thioredoxin interacting protein (TXNIP), a tumor suppressor protein and an important negative regulator of cellular glucose uptake.
26315267	11	49	theme	modified	1700:1707	arg1	proteins					1709:1716	O-GlcNAc modified proteins	1691:1716	O-GlcNAc modified proteins	1691:1716	We found that the 2DG induced TXNIP expression is at least in part dependent on the inhibition of the O-GlcNAcase enzyme and the accumulation of O-GlcNAc modified proteins.
26315267	11	50	from	dependent	1613:1621	arg1	part					1608:1611	part	1608:1611	part	1608:1611	We found that the 2DG induced TXNIP expression is at least in part dependent on the inhibition of the O-GlcNAcase enzyme and the accumulation of O-GlcNAc modified proteins.
26315267	1	51	theme	cells	214:218	arg1	microenvironment					228:243	the microenvironment	224:243	the microenvironment in the tumor tissue	224:263	The high proliferation rate of cancer cells and the microenvironment in the tumor tissue require the reprogramming of tumor cell metabolism.
26315267	1	51	theme	cells	214:218	arg1	rate					199:202	The high proliferation rate	176:202	The high proliferation rate of cancer cells	176:218	The high proliferation rate of cancer cells and the microenvironment in the tumor tissue require the reprogramming of tumor cell metabolism.
26315267	0	52	theme	protein	65:71	arg1	expression					27:36	the expression	23:36	the expression of thioredoxin interacting protein (TXNIP)	23:79	2-Deoxyglucose induces the expression of thioredoxin interacting protein (TXNIP) by increasing O-GlcNAcylation - Implications for targeting the Warburg effect in cancer cells.
26315267	1	53	theme	metabolism	305:314	arg1	reprogramming					277:289	the reprogramming	273:289	the reprogramming of tumor cell metabolism	273:314	The high proliferation rate of cancer cells and the microenvironment in the tumor tissue require the reprogramming of tumor cell metabolism.
26315267	1	54	from	microenvironment	228:243	arg1	tissue					258:263	the tumor tissue	248:263	the tumor tissue	248:263	The high proliferation rate of cancer cells and the microenvironment in the tumor tissue require the reprogramming of tumor cell metabolism.
26315267	9	55	theme	induced	1303:1309	arg1	expression					1317:1326	2DG induced TXNIP expression	1299:1326	2DG induced TXNIP expression	1299:1326	We have shown that 2DG induced TXNIP expression is independent of carbohydrate response element mediated transcription.
26315267	10	56	theme	cellular	1490:1497	arg1	ATP					1499:1501	cellular ATP	1490:1501	cellular ATP	1490:1501	Furthermore, the induction of TXNIP is neither dependent on the ability of 2DG to deplete cellular ATP nor to cause endoplasmic reticulum stress.
26315267	2	57	theme	metabolic	340:348	arg1	reprogramming					350:362	metabolic reprogramming	340:362	metabolic reprogramming	340:362	The major mechanism of metabolic reprogramming in cancer cells is the Warburg effect, defined as the preferential utilization of glucose via glycolysis even in the presence of oxygen.
26315267	0	58	theme	interacting	53:63	arg1	TXNIP					74:78	TXNIP	74:78	TXNIP	74:78	2-Deoxyglucose induces the expression of thioredoxin interacting protein (TXNIP) by increasing O-GlcNAcylation - Implications for targeting the Warburg effect in cancer cells.
26315267	0	58	theme	interacting	53:63	arg1	protein					65:71	thioredoxin interacting protein	41:71	thioredoxin interacting protein (TXNIP)	41:79	2-Deoxyglucose induces the expression of thioredoxin interacting protein (TXNIP) by increasing O-GlcNAcylation - Implications for targeting the Warburg effect in cancer cells.
26315267	6	59	theme	suppressor	910:919	arg1	protein					921:927	a tumor suppressor protein	902:927	a tumor suppressor protein	902:927	In addition, 2DG is also known to induce the expression of thioredoxin interacting protein (TXNIP), a tumor suppressor protein and an important negative regulator of cellular glucose uptake.
26315267	6	59	theme	suppressor	910:919	arg1	protein					885:891	thioredoxin interacting protein	861:891	thioredoxin interacting protein (TXNIP)	861:899	In addition, 2DG is also known to induce the expression of thioredoxin interacting protein (TXNIP), a tumor suppressor protein and an important negative regulator of cellular glucose uptake.
26315267	3	60	theme	cancer	583:588	arg1	therapy					590:596	cancer therapy	583:596	cancer therapy	583:596	Targeting the Warburg effect is considered as a promising therapeutic strategy in cancer therapy.
26315267	1	61	from	rate	199:202	arg1	tissue					258:263	the tumor tissue	248:263	the tumor tissue	248:263	The high proliferation rate of cancer cells and the microenvironment in the tumor tissue require the reprogramming of tumor cell metabolism.
26315267	8	62	theme	dependent	1252:1260	arg1	regulation					1268:1277	the 2DG dependent TXNIP regulation	1244:1277	the 2DG dependent TXNIP regulation	1244:1277	Therefore, in this study we sought to test various hypotheses for the mechanistic basis of the 2DG dependent TXNIP regulation.
26315267	6	63	theme	tumor	904:908	arg1	protein					921:927	a tumor suppressor protein	902:927	a tumor suppressor protein	902:927	In addition, 2DG is also known to induce the expression of thioredoxin interacting protein (TXNIP), a tumor suppressor protein and an important negative regulator of cellular glucose uptake.
26315267	6	63	theme	tumor	904:908	arg1	protein					885:891	thioredoxin interacting protein	861:891	thioredoxin interacting protein (TXNIP)	861:899	In addition, 2DG is also known to induce the expression of thioredoxin interacting protein (TXNIP), a tumor suppressor protein and an important negative regulator of cellular glucose uptake.
26315267	2	64	dep	oxygen	493:498	arg1	the					477:479	the	477:479	the	477:479	The major mechanism of metabolic reprogramming in cancer cells is the Warburg effect, defined as the preferential utilization of glucose via glycolysis even in the presence of oxygen.
26315267	2	64	dep	oxygen	493:498	arg1	presence					481:488	presence	481:488	presence	481:488	The major mechanism of metabolic reprogramming in cancer cells is the Warburg effect, defined as the preferential utilization of glucose via glycolysis even in the presence of oxygen.
26315267	12	65	theme	therapeutic	1777:1787	arg1	targets					1789:1795	therapeutic targets	1777:1795	therapeutic targets	1777:1795	These results have implications for the identification of therapeutic targets to increase TXNIP expression in cancer.
26315267	9	66	theme	response	1359:1366	arg1	element					1368:1374	carbohydrate response element	1346:1374	carbohydrate response element	1346:1374	We have shown that 2DG induced TXNIP expression is independent of carbohydrate response element mediated transcription.
26315267	0	67	theme	cancer	162:167	arg1	cells					169:173	cancer cells	162:173	cancer cells	162:173	2-Deoxyglucose induces the expression of thioredoxin interacting protein (TXNIP) by increasing O-GlcNAcylation - Implications for targeting the Warburg effect in cancer cells.
26315267	2	68	theme	major	321:325	arg1	effect					395:400	the Warburg effect	383:400	the Warburg effect	383:400	The major mechanism of metabolic reprogramming in cancer cells is the Warburg effect, defined as the preferential utilization of glucose via glycolysis even in the presence of oxygen.
26315267	2	68	theme	major	321:325	arg1	mechanism					327:335	The major mechanism	317:335	The major mechanism of metabolic reprogramming in cancer cells	317:378	The major mechanism of metabolic reprogramming in cancer cells is the Warburg effect, defined as the preferential utilization of glucose via glycolysis even in the presence of oxygen.
26315267	8	69	theme	various	1196:1202	arg1	hypotheses					1204:1213	various hypotheses	1196:1213	various hypotheses for the mechanistic basis of the 2DG dependent TXNIP regulation	1196:1277	Therefore, in this study we sought to test various hypotheses for the mechanistic basis of the 2DG dependent TXNIP regulation.
26315267	12	70	contain	have	1733:1736	arg2	implications					1738:1749	implications	1738:1749	implications for the identification of therapeutic targets to increase TXNIP expression in cancer	1738:1834	These results have implications for the identification of therapeutic targets to increase TXNIP expression in cancer.
26315267	12	70	contain	have	1733:1736	arg1	results					1725:1731	These results	1719:1731	These results	1719:1731	These results have implications for the identification of therapeutic targets to increase TXNIP expression in cancer.
26315267	2	71	theme	oxygen	493:498	arg1	effect					395:400	the Warburg effect	383:400	the Warburg effect	383:400	The major mechanism of metabolic reprogramming in cancer cells is the Warburg effect, defined as the preferential utilization of glucose via glycolysis even in the presence of oxygen.
26315267	2	71	theme	oxygen	493:498	arg1	mechanism					327:335	The major mechanism	317:335	The major mechanism of metabolic reprogramming in cancer cells	317:378	The major mechanism of metabolic reprogramming in cancer cells is the Warburg effect, defined as the preferential utilization of glucose via glycolysis even in the presence of oxygen.
26315267	4	72	theme	inhibitor	630:638	arg1	2DG					656:658	2DG	656:658	2DG	656:658	In this regard, the glycolytic inhibitor 2-deoxyglucose (2DG) has been evaluated clinically.
26315267	4	72	theme	inhibitor	630:638	arg1	2-deoxyglucose					640:653	the glycolytic inhibitor 2-deoxyglucose	615:653	the glycolytic inhibitor 2-deoxyglucose (2DG)	615:659	In this regard, the glycolytic inhibitor 2-deoxyglucose (2DG) has been evaluated clinically.
26315267	3	73	from	strategy	571:578	arg1	therapy					590:596	cancer therapy	583:596	cancer therapy	583:596	Targeting the Warburg effect is considered as a promising therapeutic strategy in cancer therapy.
26315267	9	74	theme	mediated	1376:1383	arg1	transcription					1385:1397	carbohydrate response element mediated transcription	1346:1397	carbohydrate response element mediated transcription	1346:1397	We have shown that 2DG induced TXNIP expression is independent of carbohydrate response element mediated transcription.
26315267	5	75	theme	phosphoglucoisomerase	779:799	arg1	level					755:759	the level	751:759	the level of hexokinase and phosphoglucoisomerase	751:799	2DG exerts its effect by directly inhibiting glycolysis at the level of hexokinase and phosphoglucoisomerase.
26315267	12	76	from	expression	1815:1824	arg1	cancer					1829:1834	cancer	1829:1834	cancer	1829:1834	These results have implications for the identification of therapeutic targets to increase TXNIP expression in cancer.
26315267	11	77	theme	proteins	1709:1716	arg1	accumulation					1675:1686	the accumulation	1671:1686	the accumulation of O-GlcNAc modified proteins	1671:1716	We found that the 2DG induced TXNIP expression is at least in part dependent on the inhibition of the O-GlcNAcase enzyme and the accumulation of O-GlcNAc modified proteins.
26315267	11	77	theme	proteins	1709:1716	arg1	inhibition					1630:1639	the inhibition	1626:1639	the inhibition of the O-GlcNAcase enzyme	1626:1665	We found that the 2DG induced TXNIP expression is at least in part dependent on the inhibition of the O-GlcNAcase enzyme and the accumulation of O-GlcNAc modified proteins.
26315267	11	78	theme	TXNIP	1576:1580	arg1	expression					1582:1591	the 2DG induced TXNIP expression	1560:1591	the 2DG induced TXNIP expression	1560:1591	We found that the 2DG induced TXNIP expression is at least in part dependent on the inhibition of the O-GlcNAcase enzyme and the accumulation of O-GlcNAc modified proteins.
26315267	11	78	theme	TXNIP	1576:1580	arg1	dependent					1613:1621	dependent	1613:1621	dependent	1613:1621	We found that the 2DG induced TXNIP expression is at least in part dependent on the inhibition of the O-GlcNAcase enzyme and the accumulation of O-GlcNAc modified proteins.
26315267	2	79	theme	cancer	367:372	arg1	cells					374:378	cancer cells	367:378	cancer cells	367:378	The major mechanism of metabolic reprogramming in cancer cells is the Warburg effect, defined as the preferential utilization of glucose via glycolysis even in the presence of oxygen.
26315267	11	80	theme	O-GlcNAcase	1648:1658	arg1	enzyme					1660:1665	the O-GlcNAcase enzyme	1644:1665	the O-GlcNAcase enzyme	1644:1665	We found that the 2DG induced TXNIP expression is at least in part dependent on the inhibition of the O-GlcNAcase enzyme and the accumulation of O-GlcNAc modified proteins.
26315267	9	81	theme	transcription	1385:1397	arg1	independent					1331:1341	independent	1331:1341	independent	1331:1341	We have shown that 2DG induced TXNIP expression is independent of carbohydrate response element mediated transcription.
34731008	3	0	theme	membrane	647:654	arg1	surface					632:638	the cytoplasmic surface	616:638	the cytoplasmic surface of the membrane	616:654	The structure reveals a unique protein fold consisting of an unusual cysteine-rich domain that folds as an arch bridge stabilized by 11 pairs of disulfide bonds, a previously uncharacterized domain named β sheet–rich domain, a previously unidentified seven-transmembrane fold wherein TM4 to TM6 are broken near the cytoplasmic surface of the membrane, and a coiled-coil domain placed below the transmembrane domain.
34731008	5	1	theme	function	847:854	arg1	mechanisms					868:877	the function and disease mechanisms	843:877	the function and disease mechanisms of Meckelin	843:889	Our structure establishes a framework for dissecting the function and disease mechanisms of Meckelin.
34731008	4	2	with	homodimer	745:753	arg1	interface					779:787	an extensive dimer interface	760:787	an extensive dimer interface	760:787	Meckelin forms a stable homodimer with an extensive dimer interface.
34731008	1	3	from	Mutations	55:63	arg1	gene					81:84	the Meckelin gene	68:84	the Meckelin gene	68:84	Mutations in the Meckelin gene account for most cases of the Meckel-Gruber syndrome, the most severe ciliopathy with a 100% mortality rate.
34731008	3	4	theme	wherein	581:587	arg1	TM4					589:591	a previously unidentified seven-transmembrane fold wherein TM4	530:591	a previously unidentified seven-transmembrane fold wherein TM4 to TM6	530:598	The structure reveals a unique protein fold consisting of an unusual cysteine-rich domain that folds as an arch bridge stabilized by 11 pairs of disulfide bonds, a previously uncharacterized domain named β sheet–rich domain, a previously unidentified seven-transmembrane fold wherein TM4 to TM6 are broken near the cytoplasmic surface of the membrane, and a coiled-coil domain placed below the transmembrane domain.
34731008	3	4	theme	wherein	581:587	arg1	domain					522:527	β sheet–rich domain	509:527	β sheet–rich domain	509:527	The structure reveals a unique protein fold consisting of an unusual cysteine-rich domain that folds as an arch bridge stabilized by 11 pairs of disulfide bonds, a previously uncharacterized domain named β sheet–rich domain, a previously unidentified seven-transmembrane fold wherein TM4 to TM6 are broken near the cytoplasmic surface of the membrane, and a coiled-coil domain placed below the transmembrane domain.
34731008	3	5	theme	disulfide	450:458	arg1	bonds					460:464	disulfide bonds	450:464	disulfide bonds	450:464	The structure reveals a unique protein fold consisting of an unusual cysteine-rich domain that folds as an arch bridge stabilized by 11 pairs of disulfide bonds, a previously uncharacterized domain named β sheet–rich domain, a previously unidentified seven-transmembrane fold wherein TM4 to TM6 are broken near the cytoplasmic surface of the membrane, and a coiled-coil domain placed below the transmembrane domain.
34731008	2	6	theme	human	257:261	arg1	Meckelin					263:270	human Meckelin	257:270	human Meckelin (also known as TMEM67 and MKS3)	257:302	Here, we report a 3.3-Å cryo–electron microscopy structure of human Meckelin (also known as TMEM67 and MKS3).
34731008	2	7	theme	Meckelin	263:270	arg1	structure					244:252	a 3.3-Å cryo–electron microscopy structure	211:252	a 3.3-Å cryo–electron microscopy structure of human Meckelin (also known as TMEM67 and MKS3)	211:302	Here, we report a 3.3-Å cryo–electron microscopy structure of human Meckelin (also known as TMEM67 and MKS3).
34731008	3	8	theme	uncharacterized	480:494	arg1	domain					496:501	a previously uncharacterized domain	467:501	a previously uncharacterized domain named β sheet–rich domain, a previously unidentified seven-transmembrane fold wherein TM4 to TM6 are broken near the cytoplasmic surface of the membrane	467:654	The structure reveals a unique protein fold consisting of an unusual cysteine-rich domain that folds as an arch bridge stabilized by 11 pairs of disulfide bonds, a previously uncharacterized domain named β sheet–rich domain, a previously unidentified seven-transmembrane fold wherein TM4 to TM6 are broken near the cytoplasmic surface of the membrane, and a coiled-coil domain placed below the transmembrane domain.
34731008	5	9	theme	Meckelin	882:889	arg1	mechanisms					868:877	the function and disease mechanisms	843:877	the function and disease mechanisms of Meckelin	843:889	Our structure establishes a framework for dissecting the function and disease mechanisms of Meckelin.
34731008	3	10	theme	coiled-coil	663:673	arg1	domain					675:680	a coiled-coil domain	661:680	a coiled-coil domain placed below the transmembrane domain	661:718	The structure reveals a unique protein fold consisting of an unusual cysteine-rich domain that folds as an arch bridge stabilized by 11 pairs of disulfide bonds, a previously uncharacterized domain named β sheet–rich domain, a previously unidentified seven-transmembrane fold wherein TM4 to TM6 are broken near the cytoplasmic surface of the membrane, and a coiled-coil domain placed below the transmembrane domain.
34731008	3	11	theme	arch	412:415	arg1	bridge					417:422	an arch bridge	409:422	an arch bridge stabilized by 11 pairs of disulfide bonds	409:464	The structure reveals a unique protein fold consisting of an unusual cysteine-rich domain that folds as an arch bridge stabilized by 11 pairs of disulfide bonds, a previously uncharacterized domain named β sheet–rich domain, a previously unidentified seven-transmembrane fold wherein TM4 to TM6 are broken near the cytoplasmic surface of the membrane, and a coiled-coil domain placed below the transmembrane domain.
34731008	1	12	theme	severe	149:154	arg1	ciliopathy					156:165	the most severe ciliopathy	140:165	the most severe ciliopathy with a 100% mortality rate	140:192	Mutations in the Meckelin gene account for most cases of the Meckel-Gruber syndrome, the most severe ciliopathy with a 100% mortality rate.
34731008	1	12	theme	severe	149:154	arg1	syndrome					130:137	the Meckel-Gruber syndrome	112:137	the Meckel-Gruber syndrome	112:137	Mutations in the Meckelin gene account for most cases of the Meckel-Gruber syndrome, the most severe ciliopathy with a 100% mortality rate.
34731008	1	13	theme	Meckelin	72:79	arg1	gene					81:84	the Meckelin gene	68:84	the Meckelin gene	68:84	Mutations in the Meckelin gene account for most cases of the Meckel-Gruber syndrome, the most severe ciliopathy with a 100% mortality rate.
34731008	3	14	theme	unique	329:334	arg1	fold					344:347	a unique protein fold	327:347	a unique protein fold consisting of an unusual cysteine-rich domain that folds as an arch bridge stabilized by 11 pairs of disulfide bonds, a previously uncharacterized domain named β sheet–rich domain, a previously unidentified seven-transmembrane fold wherein TM4 to TM6 are broken near the cytoplasmic surface of the membrane, and a coiled-coil domain placed below the transmembrane domain	327:718	The structure reveals a unique protein fold consisting of an unusual cysteine-rich domain that folds as an arch bridge stabilized by 11 pairs of disulfide bonds, a previously uncharacterized domain named β sheet–rich domain, a previously unidentified seven-transmembrane fold wherein TM4 to TM6 are broken near the cytoplasmic surface of the membrane, and a coiled-coil domain placed below the transmembrane domain.
34731008	3	15	theme	β	509:509	arg1	domain					522:527	β sheet–rich domain	509:527	β sheet–rich domain	509:527	The structure reveals a unique protein fold consisting of an unusual cysteine-rich domain that folds as an arch bridge stabilized by 11 pairs of disulfide bonds, a previously uncharacterized domain named β sheet–rich domain, a previously unidentified seven-transmembrane fold wherein TM4 to TM6 are broken near the cytoplasmic surface of the membrane, and a coiled-coil domain placed below the transmembrane domain.
34731008	3	15	theme	β	509:509	arg1	TM4					589:591	a previously unidentified seven-transmembrane fold wherein TM4	530:591	a previously unidentified seven-transmembrane fold wherein TM4 to TM6	530:598	The structure reveals a unique protein fold consisting of an unusual cysteine-rich domain that folds as an arch bridge stabilized by 11 pairs of disulfide bonds, a previously uncharacterized domain named β sheet–rich domain, a previously unidentified seven-transmembrane fold wherein TM4 to TM6 are broken near the cytoplasmic surface of the membrane, and a coiled-coil domain placed below the transmembrane domain.
34731008	3	16	theme	unusual	366:372	arg1	domain					388:393	an unusual cysteine-rich domain	363:393	an unusual cysteine-rich domain that folds as an arch bridge stabilized by 11 pairs of disulfide bonds	363:464	The structure reveals a unique protein fold consisting of an unusual cysteine-rich domain that folds as an arch bridge stabilized by 11 pairs of disulfide bonds, a previously uncharacterized domain named β sheet–rich domain, a previously unidentified seven-transmembrane fold wherein TM4 to TM6 are broken near the cytoplasmic surface of the membrane, and a coiled-coil domain placed below the transmembrane domain.
34731008	3	17	theme	protein	336:342	arg1	fold					344:347	a unique protein fold	327:347	a unique protein fold consisting of an unusual cysteine-rich domain that folds as an arch bridge stabilized by 11 pairs of disulfide bonds, a previously uncharacterized domain named β sheet–rich domain, a previously unidentified seven-transmembrane fold wherein TM4 to TM6 are broken near the cytoplasmic surface of the membrane, and a coiled-coil domain placed below the transmembrane domain	327:718	The structure reveals a unique protein fold consisting of an unusual cysteine-rich domain that folds as an arch bridge stabilized by 11 pairs of disulfide bonds, a previously uncharacterized domain named β sheet–rich domain, a previously unidentified seven-transmembrane fold wherein TM4 to TM6 are broken near the cytoplasmic surface of the membrane, and a coiled-coil domain placed below the transmembrane domain.
34731008	3	18	theme	sheet–rich	511:520	arg1	domain					522:527	β sheet–rich domain	509:527	β sheet–rich domain	509:527	The structure reveals a unique protein fold consisting of an unusual cysteine-rich domain that folds as an arch bridge stabilized by 11 pairs of disulfide bonds, a previously uncharacterized domain named β sheet–rich domain, a previously unidentified seven-transmembrane fold wherein TM4 to TM6 are broken near the cytoplasmic surface of the membrane, and a coiled-coil domain placed below the transmembrane domain.
34731008	3	18	theme	sheet–rich	511:520	arg1	TM4					589:591	a previously unidentified seven-transmembrane fold wherein TM4	530:591	a previously unidentified seven-transmembrane fold wherein TM4 to TM6	530:598	The structure reveals a unique protein fold consisting of an unusual cysteine-rich domain that folds as an arch bridge stabilized by 11 pairs of disulfide bonds, a previously uncharacterized domain named β sheet–rich domain, a previously unidentified seven-transmembrane fold wherein TM4 to TM6 are broken near the cytoplasmic surface of the membrane, and a coiled-coil domain placed below the transmembrane domain.
34731008	3	19	theme	cysteine-rich	374:386	arg1	domain					388:393	an unusual cysteine-rich domain	363:393	an unusual cysteine-rich domain that folds as an arch bridge stabilized by 11 pairs of disulfide bonds	363:464	The structure reveals a unique protein fold consisting of an unusual cysteine-rich domain that folds as an arch bridge stabilized by 11 pairs of disulfide bonds, a previously uncharacterized domain named β sheet–rich domain, a previously unidentified seven-transmembrane fold wherein TM4 to TM6 are broken near the cytoplasmic surface of the membrane, and a coiled-coil domain placed below the transmembrane domain.
34731008	0	20	theme	human	17:21	arg1	protein					37:43	the human Meckel-Gruber protein	13:43	the human Meckel-Gruber protein	13:43	Structure of the human Meckel-Gruber protein Meckelin.
34731008	4	21	theme	extensive	763:771	arg1	interface					779:787	an extensive dimer interface	760:787	an extensive dimer interface	760:787	Meckelin forms a stable homodimer with an extensive dimer interface.
34731008	1	22	theme	100	174:176	arg1	%					177:177	%	177:177	%	177:177	Mutations in the Meckelin gene account for most cases of the Meckel-Gruber syndrome, the most severe ciliopathy with a 100% mortality rate.
34731008	1	23	theme	most	98:101	arg1	cases					103:107	most cases	98:107	most cases of the Meckel-Gruber syndrome, the most severe ciliopathy with a 100% mortality rate	98:192	Mutations in the Meckelin gene account for most cases of the Meckel-Gruber syndrome, the most severe ciliopathy with a 100% mortality rate.
34731008	1	24	theme	%	177:177	arg1	rate					189:192	a 100% mortality rate	172:192	a 100% mortality rate	172:192	Mutations in the Meckelin gene account for most cases of the Meckel-Gruber syndrome, the most severe ciliopathy with a 100% mortality rate.
34731008	0	25	theme	protein	37:43	arg1	Structure					0:8	Structure	0:8	Structure of the human Meckel-Gruber protein	0:43	Structure of the human Meckel-Gruber protein Meckelin.
34731008	1	26	theme	mortality	179:187	arg1	rate					189:192	a 100% mortality rate	172:192	a 100% mortality rate	172:192	Mutations in the Meckelin gene account for most cases of the Meckel-Gruber syndrome, the most severe ciliopathy with a 100% mortality rate.
34731008	0	27	theme	Meckel-Gruber	23:35	arg1	protein					37:43	the human Meckel-Gruber protein	13:43	the human Meckel-Gruber protein	13:43	Structure of the human Meckel-Gruber protein Meckelin.
34731008	0	28	dep	Meckelin	45:52	arg1	Structure					0:8	Structure	0:8	Structure of the human Meckel-Gruber protein	0:43	Structure of the human Meckel-Gruber protein Meckelin.
34731008	4	29	theme	dimer	773:777	arg1	interface					779:787	an extensive dimer interface	760:787	an extensive dimer interface	760:787	Meckelin forms a stable homodimer with an extensive dimer interface.
34731008	5	30	theme	disease	860:866	arg1	mechanisms					868:877	the function and disease mechanisms	843:877	the function and disease mechanisms of Meckelin	843:889	Our structure establishes a framework for dissecting the function and disease mechanisms of Meckelin.
34731008	3	31	theme	transmembrane	699:711	arg1	domain					713:718	the transmembrane domain	695:718	the transmembrane domain	695:718	The structure reveals a unique protein fold consisting of an unusual cysteine-rich domain that folds as an arch bridge stabilized by 11 pairs of disulfide bonds, a previously uncharacterized domain named β sheet–rich domain, a previously unidentified seven-transmembrane fold wherein TM4 to TM6 are broken near the cytoplasmic surface of the membrane, and a coiled-coil domain placed below the transmembrane domain.
34731008	3	32	theme	cytoplasmic	620:630	arg1	surface					632:638	the cytoplasmic surface	616:638	the cytoplasmic surface of the membrane	616:654	The structure reveals a unique protein fold consisting of an unusual cysteine-rich domain that folds as an arch bridge stabilized by 11 pairs of disulfide bonds, a previously uncharacterized domain named β sheet–rich domain, a previously unidentified seven-transmembrane fold wherein TM4 to TM6 are broken near the cytoplasmic surface of the membrane, and a coiled-coil domain placed below the transmembrane domain.
34731008	2	33	dep	Meckelin	263:270	arg1	known					278:282	known	278:282	known as TMEM67 and MKS3	278:301	Here, we report a 3.3-Å cryo–electron microscopy structure of human Meckelin (also known as TMEM67 and MKS3).
34731008	4	34	theme	stable	738:743	arg1	homodimer					745:753	a stable homodimer	736:753	a stable homodimer with an extensive dimer interface	736:787	Meckelin forms a stable homodimer with an extensive dimer interface.
34731008	3	35	theme	fold	576:579	arg1	TM4					589:591	a previously unidentified seven-transmembrane fold wherein TM4	530:591	a previously unidentified seven-transmembrane fold wherein TM4 to TM6	530:598	The structure reveals a unique protein fold consisting of an unusual cysteine-rich domain that folds as an arch bridge stabilized by 11 pairs of disulfide bonds, a previously uncharacterized domain named β sheet–rich domain, a previously unidentified seven-transmembrane fold wherein TM4 to TM6 are broken near the cytoplasmic surface of the membrane, and a coiled-coil domain placed below the transmembrane domain.
34731008	3	35	theme	fold	576:579	arg1	domain					522:527	β sheet–rich domain	509:527	β sheet–rich domain	509:527	The structure reveals a unique protein fold consisting of an unusual cysteine-rich domain that folds as an arch bridge stabilized by 11 pairs of disulfide bonds, a previously uncharacterized domain named β sheet–rich domain, a previously unidentified seven-transmembrane fold wherein TM4 to TM6 are broken near the cytoplasmic surface of the membrane, and a coiled-coil domain placed below the transmembrane domain.
34731008	2	36	theme	cryo–electron	219:231	arg1	structure					244:252	a 3.3-Å cryo–electron microscopy structure	211:252	a 3.3-Å cryo–electron microscopy structure of human Meckelin (also known as TMEM67 and MKS3)	211:302	Here, we report a 3.3-Å cryo–electron microscopy structure of human Meckelin (also known as TMEM67 and MKS3).
34731008	2	37	dep	known	278:282	arg1	also					273:276	also	273:276	also	273:276	Here, we report a 3.3-Å cryo–electron microscopy structure of human Meckelin (also known as TMEM67 and MKS3).
34731008	1	38	with	ciliopathy	156:165	arg1	rate					189:192	a 100% mortality rate	172:192	a 100% mortality rate	172:192	Mutations in the Meckelin gene account for most cases of the Meckel-Gruber syndrome, the most severe ciliopathy with a 100% mortality rate.
34731008	2	39	theme	3.3-Å	213:217	arg1	structure					244:252	a 3.3-Å cryo–electron microscopy structure	211:252	a 3.3-Å cryo–electron microscopy structure of human Meckelin (also known as TMEM67 and MKS3)	211:302	Here, we report a 3.3-Å cryo–electron microscopy structure of human Meckelin (also known as TMEM67 and MKS3).
34731008	1	40	theme	Meckel-Gruber	116:128	arg1	ciliopathy					156:165	the most severe ciliopathy	140:165	the most severe ciliopathy with a 100% mortality rate	140:192	Mutations in the Meckelin gene account for most cases of the Meckel-Gruber syndrome, the most severe ciliopathy with a 100% mortality rate.
34731008	1	40	theme	Meckel-Gruber	116:128	arg1	syndrome					130:137	the Meckel-Gruber syndrome	112:137	the Meckel-Gruber syndrome	112:137	Mutations in the Meckelin gene account for most cases of the Meckel-Gruber syndrome, the most severe ciliopathy with a 100% mortality rate.
34731008	3	41	theme	unidentified	543:554	arg1	TM4					589:591	a previously unidentified seven-transmembrane fold wherein TM4	530:591	a previously unidentified seven-transmembrane fold wherein TM4 to TM6	530:598	The structure reveals a unique protein fold consisting of an unusual cysteine-rich domain that folds as an arch bridge stabilized by 11 pairs of disulfide bonds, a previously uncharacterized domain named β sheet–rich domain, a previously unidentified seven-transmembrane fold wherein TM4 to TM6 are broken near the cytoplasmic surface of the membrane, and a coiled-coil domain placed below the transmembrane domain.
34731008	3	41	theme	unidentified	543:554	arg1	domain					522:527	β sheet–rich domain	509:527	β sheet–rich domain	509:527	The structure reveals a unique protein fold consisting of an unusual cysteine-rich domain that folds as an arch bridge stabilized by 11 pairs of disulfide bonds, a previously uncharacterized domain named β sheet–rich domain, a previously unidentified seven-transmembrane fold wherein TM4 to TM6 are broken near the cytoplasmic surface of the membrane, and a coiled-coil domain placed below the transmembrane domain.
34731008	1	42	theme	syndrome	130:137	arg1	cases					103:107	most cases	98:107	most cases of the Meckel-Gruber syndrome, the most severe ciliopathy with a 100% mortality rate	98:192	Mutations in the Meckelin gene account for most cases of the Meckel-Gruber syndrome, the most severe ciliopathy with a 100% mortality rate.
34731008	2	43	theme	microscopy	233:242	arg1	structure					244:252	a 3.3-Å cryo–electron microscopy structure	211:252	a 3.3-Å cryo–electron microscopy structure of human Meckelin (also known as TMEM67 and MKS3)	211:302	Here, we report a 3.3-Å cryo–electron microscopy structure of human Meckelin (also known as TMEM67 and MKS3).
34731008	3	44	theme	seven-transmembrane	556:574	arg1	TM4					589:591	a previously unidentified seven-transmembrane fold wherein TM4	530:591	a previously unidentified seven-transmembrane fold wherein TM4 to TM6	530:598	The structure reveals a unique protein fold consisting of an unusual cysteine-rich domain that folds as an arch bridge stabilized by 11 pairs of disulfide bonds, a previously uncharacterized domain named β sheet–rich domain, a previously unidentified seven-transmembrane fold wherein TM4 to TM6 are broken near the cytoplasmic surface of the membrane, and a coiled-coil domain placed below the transmembrane domain.
34731008	3	44	theme	seven-transmembrane	556:574	arg1	domain					522:527	β sheet–rich domain	509:527	β sheet–rich domain	509:527	The structure reveals a unique protein fold consisting of an unusual cysteine-rich domain that folds as an arch bridge stabilized by 11 pairs of disulfide bonds, a previously uncharacterized domain named β sheet–rich domain, a previously unidentified seven-transmembrane fold wherein TM4 to TM6 are broken near the cytoplasmic surface of the membrane, and a coiled-coil domain placed below the transmembrane domain.
34731008	3	45	theme	bonds	460:464	arg1	pairs					441:445	11 pairs	438:445	11 pairs of disulfide bonds	438:464	The structure reveals a unique protein fold consisting of an unusual cysteine-rich domain that folds as an arch bridge stabilized by 11 pairs of disulfide bonds, a previously uncharacterized domain named β sheet–rich domain, a previously unidentified seven-transmembrane fold wherein TM4 to TM6 are broken near the cytoplasmic surface of the membrane, and a coiled-coil domain placed below the transmembrane domain.
25500532	5	0	theme	recognition	576:586	arg1	mode					588:591	the receptors' recognition mode	561:591	the receptors' recognition mode for IL-18	561:601	Generally, the receptors' recognition mode for IL-18 is similar to IL-1β; however, certain notable differences were observed.
25500532	1	1	theme	IL-1	141:144	arg1	family					146:151	the IL-1 family	137:151	the IL-1 family	137:151	Interleukin (IL)-18 is a proinflammatory cytokine that belongs to the IL-1 family and plays an important role in inflammation.
25500532	3	2	theme	IL-18	338:342	arg1	Rα					356:357	Rα	356:357	Rα	356:357	IL-18 forms a signalling complex with the IL-18 receptor α (Rα) and β (Rβ) chains at the plasma membrane, which induces multiple inflammatory cytokines.
25500532	3	2	theme	IL-18	338:342	arg1	receptor					344:351	IL-18 receptor α	338:353	IL-18 receptor α (Rα)	338:358	IL-18 forms a signalling complex with the IL-18 receptor α (Rα) and β (Rβ) chains at the plasma membrane, which induces multiple inflammatory cytokines.
25500532	2	3	theme	chronic	266:272	arg1	disease					287:293	severe chronic inflammatory disease	259:293	severe chronic inflammatory disease	259:293	The uncontrolled release of this cytokine is associated with severe chronic inflammatory disease.
25500532	4	4	theme	receptor	518:525	arg1	domains					541:547	the two receptor extracellular domains	510:547	the two receptor extracellular domains	510:547	Here, we present a crystal structure of human IL-18 bound to the two receptor extracellular domains.
25500532	3	5	theme	receptor	344:351	arg1	chains					371:376	the IL-18 receptor α (Rα) and β (Rβ) chains	334:376	the IL-18 receptor α (Rα) and β (Rβ) chains at the plasma membrane	334:399	IL-18 forms a signalling complex with the IL-18 receptor α (Rα) and β (Rβ) chains at the plasma membrane, which induces multiple inflammatory cytokines.
25500532	2	6	theme	severe	259:264	arg1	disease					287:293	severe chronic inflammatory disease	259:293	severe chronic inflammatory disease	259:293	The uncontrolled release of this cytokine is associated with severe chronic inflammatory disease.
25500532	7	7	theme	IL-18	1010:1014	arg1	activity					1016:1023	IL-18 activity	1010:1023	IL-18 activity	1010:1023	The structures and associated biochemical and cellular data should aid in developing novel drugs to neutralize IL-18 activity.
25500532	6	8	theme	domain	722:727	arg1	architecture					680:691	The architecture	676:691	The architecture of the IL-18 receptor second domain (D2)	676:732	The architecture of the IL-18 receptor second domain (D2) is unique among the other IL-1R family members, which presumably distinguishes them from the IL-1 receptors that exhibit a more promiscuous ligand recognition mode.
25500532	6	8	theme	domain	722:727	arg1	unique					737:742	unique	737:742	unique	737:742	The architecture of the IL-18 receptor second domain (D2) is unique among the other IL-1R family members, which presumably distinguishes them from the IL-1 receptors that exhibit a more promiscuous ligand recognition mode.
25500532	1	9	theme	Interleukin	71:81	arg1	cytokine					112:119	a proinflammatory cytokine	94:119	a proinflammatory cytokine that belongs to the IL-1 family and plays an important role in inflammation	94:195	Interleukin (IL)-18 is a proinflammatory cytokine that belongs to the IL-1 family and plays an important role in inflammation.
25500532	1	9	theme	Interleukin	71:81	arg1	IL					84:85	Interleukin (IL)-18	71:89	Interleukin (IL)-18	71:89	Interleukin (IL)-18 is a proinflammatory cytokine that belongs to the IL-1 family and plays an important role in inflammation.
25500532	6	10	theme	second	715:720	arg1	D2					730:731	D2	730:731	D2	730:731	The architecture of the IL-18 receptor second domain (D2) is unique among the other IL-1R family members, which presumably distinguishes them from the IL-1 receptors that exhibit a more promiscuous ligand recognition mode.
25500532	6	10	theme	second	715:720	arg1	domain					722:727	the IL-18 receptor second domain	696:727	the IL-18 receptor second domain (D2)	696:732	The architecture of the IL-18 receptor second domain (D2) is unique among the other IL-1R family members, which presumably distinguishes them from the IL-1 receptors that exhibit a more promiscuous ligand recognition mode.
25500532	0	11	theme	structural	4:13	arg1	basis					15:19	The structural basis	0:19	The structural basis for receptor recognition of human interleukin-18	0:68	The structural basis for receptor recognition of human interleukin-18.
25500532	6	12	theme	receptor	706:713	arg1	D2					730:731	D2	730:731	D2	730:731	The architecture of the IL-18 receptor second domain (D2) is unique among the other IL-1R family members, which presumably distinguishes them from the IL-1 receptors that exhibit a more promiscuous ligand recognition mode.
25500532	6	12	theme	receptor	706:713	arg1	domain					722:727	the IL-18 receptor second domain	696:727	the IL-18 receptor second domain (D2)	696:732	The architecture of the IL-18 receptor second domain (D2) is unique among the other IL-1R family members, which presumably distinguishes them from the IL-1 receptors that exhibit a more promiscuous ligand recognition mode.
25500532	4	13	theme	human	489:493	arg1	IL-18					495:499	human IL-18	489:499	human IL-18 bound to the two receptor extracellular domains	489:547	Here, we present a crystal structure of human IL-18 bound to the two receptor extracellular domains.
25500532	6	14	theme	IL-18	700:704	arg1	D2					730:731	D2	730:731	D2	730:731	The architecture of the IL-18 receptor second domain (D2) is unique among the other IL-1R family members, which presumably distinguishes them from the IL-1 receptors that exhibit a more promiscuous ligand recognition mode.
25500532	6	14	theme	IL-18	700:704	arg1	domain					722:727	the IL-18 receptor second domain	696:727	the IL-18 receptor second domain (D2)	696:732	The architecture of the IL-18 receptor second domain (D2) is unique among the other IL-1R family members, which presumably distinguishes them from the IL-1 receptors that exhibit a more promiscuous ligand recognition mode.
25500532	6	15	theme	ligand	874:879	arg1	mode					893:896	a more promiscuous ligand recognition mode	855:896	a more promiscuous ligand recognition mode	855:896	The architecture of the IL-18 receptor second domain (D2) is unique among the other IL-1R family members, which presumably distinguishes them from the IL-1 receptors that exhibit a more promiscuous ligand recognition mode.
25500532	7	16	theme	novel	984:988	arg1	drugs					990:994	novel drugs	984:994	novel drugs	984:994	The structures and associated biochemical and cellular data should aid in developing novel drugs to neutralize IL-18 activity.
25500532	1	17	theme	important	166:174	arg1	role					176:179	an important role	163:179	an important role	163:179	Interleukin (IL)-18 is a proinflammatory cytokine that belongs to the IL-1 family and plays an important role in inflammation.
25500532	6	18	theme	promiscuous	862:872	arg1	mode					893:896	a more promiscuous ligand recognition mode	855:896	a more promiscuous ligand recognition mode	855:896	The architecture of the IL-18 receptor second domain (D2) is unique among the other IL-1R family members, which presumably distinguishes them from the IL-1 receptors that exhibit a more promiscuous ligand recognition mode.
25500532	2	19	theme	inflammatory	274:285	arg1	disease					287:293	severe chronic inflammatory disease	259:293	severe chronic inflammatory disease	259:293	The uncontrolled release of this cytokine is associated with severe chronic inflammatory disease.
25500532	4	20	theme	IL-18	495:499	arg1	structure					476:484	a crystal structure	466:484	a crystal structure of human IL-18 bound to the two receptor extracellular domains	466:547	Here, we present a crystal structure of human IL-18 bound to the two receptor extracellular domains.
25500532	6	21	theme	family	766:771	arg1	members					773:779	the other IL-1R family members	750:779	the other IL-1R family members	750:779	The architecture of the IL-18 receptor second domain (D2) is unique among the other IL-1R family members, which presumably distinguishes them from the IL-1 receptors that exhibit a more promiscuous ligand recognition mode.
25500532	3	22	theme	plasma	385:390	arg1	membrane					392:399	the plasma membrane	381:399	the plasma membrane	381:399	IL-18 forms a signalling complex with the IL-18 receptor α (Rα) and β (Rβ) chains at the plasma membrane, which induces multiple inflammatory cytokines.
25500532	0	23	theme	receptor	25:32	arg1	recognition					34:44	receptor recognition	25:44	receptor recognition of human interleukin-18	25:68	The structural basis for receptor recognition of human interleukin-18.
25500532	5	24	theme	certain	633:639	arg1	differences					649:659	certain notable differences	633:659	certain notable differences	633:659	Generally, the receptors' recognition mode for IL-18 is similar to IL-1β; however, certain notable differences were observed.
25500532	6	25	theme	IL-1R	760:764	arg1	members					773:779	the other IL-1R family members	750:779	the other IL-1R family members	750:779	The architecture of the IL-18 receptor second domain (D2) is unique among the other IL-1R family members, which presumably distinguishes them from the IL-1 receptors that exhibit a more promiscuous ligand recognition mode.
25500532	2	26	theme	uncontrolled	202:213	arg1	release					215:221	The uncontrolled release	198:221	The uncontrolled release of this cytokine	198:238	The uncontrolled release of this cytokine is associated with severe chronic inflammatory disease.
25500532	7	27	theme	biochemical	929:939	arg1	data					954:957	associated biochemical and cellular data	918:957	associated biochemical and cellular data	918:957	The structures and associated biochemical and cellular data should aid in developing novel drugs to neutralize IL-18 activity.
25500532	0	28	theme	human	49:53	arg1	interleukin-18					55:68	human interleukin-18	49:68	human interleukin-18	49:68	The structural basis for receptor recognition of human interleukin-18.
25500532	5	29	theme	notable	641:647	arg1	differences					649:659	certain notable differences	633:659	certain notable differences	633:659	Generally, the receptors' recognition mode for IL-18 is similar to IL-1β; however, certain notable differences were observed.
25500532	6	30	theme	other	754:758	arg1	members					773:779	the other IL-1R family members	750:779	the other IL-1R family members	750:779	The architecture of the IL-18 receptor second domain (D2) is unique among the other IL-1R family members, which presumably distinguishes them from the IL-1 receptors that exhibit a more promiscuous ligand recognition mode.
25500532	3	31	from	membrane	392:399	arg1	chains					371:376	the IL-18 receptor α (Rα) and β (Rβ) chains	334:376	the IL-18 receptor α (Rα) and β (Rβ) chains at the plasma membrane	334:399	IL-18 forms a signalling complex with the IL-18 receptor α (Rα) and β (Rβ) chains at the plasma membrane, which induces multiple inflammatory cytokines.
25500532	3	32	theme	inflammatory	425:436	arg1	cytokines					438:446	multiple inflammatory cytokines	416:446	multiple inflammatory cytokines	416:446	IL-18 forms a signalling complex with the IL-18 receptor α (Rα) and β (Rβ) chains at the plasma membrane, which induces multiple inflammatory cytokines.
25500532	3	33	theme	β	364:364	arg1	chains					371:376	the IL-18 receptor α (Rα) and β (Rβ) chains	334:376	the IL-18 receptor α (Rα) and β (Rβ) chains at the plasma membrane	334:399	IL-18 forms a signalling complex with the IL-18 receptor α (Rα) and β (Rβ) chains at the plasma membrane, which induces multiple inflammatory cytokines.
25500532	1	34	theme	proinflammatory	96:110	arg1	cytokine					112:119	a proinflammatory cytokine	94:119	a proinflammatory cytokine that belongs to the IL-1 family and plays an important role in inflammation	94:195	Interleukin (IL)-18 is a proinflammatory cytokine that belongs to the IL-1 family and plays an important role in inflammation.
25500532	1	34	theme	proinflammatory	96:110	arg1	IL					84:85	Interleukin (IL)-18	71:89	Interleukin (IL)-18	71:89	Interleukin (IL)-18 is a proinflammatory cytokine that belongs to the IL-1 family and plays an important role in inflammation.
25500532	4	35	theme	crystal	468:474	arg1	structure					476:484	a crystal structure	466:484	a crystal structure of human IL-18 bound to the two receptor extracellular domains	466:547	Here, we present a crystal structure of human IL-18 bound to the two receptor extracellular domains.
25500532	7	36	theme	cellular	945:952	arg1	data					954:957	associated biochemical and cellular data	918:957	associated biochemical and cellular data	918:957	The structures and associated biochemical and cellular data should aid in developing novel drugs to neutralize IL-18 activity.
25500532	7	37	theme	associated	918:927	arg1	data					954:957	associated biochemical and cellular data	918:957	associated biochemical and cellular data	918:957	The structures and associated biochemical and cellular data should aid in developing novel drugs to neutralize IL-18 activity.
25500532	2	38	theme	cytokine	231:238	arg1	release					215:221	The uncontrolled release	198:221	The uncontrolled release of this cytokine	198:238	The uncontrolled release of this cytokine is associated with severe chronic inflammatory disease.
25500532	3	39	theme	multiple	416:423	arg1	cytokines					438:446	multiple inflammatory cytokines	416:446	multiple inflammatory cytokines	416:446	IL-18 forms a signalling complex with the IL-18 receptor α (Rα) and β (Rβ) chains at the plasma membrane, which induces multiple inflammatory cytokines.
25500532	4	40	theme	extracellular	527:539	arg1	domains					541:547	the two receptor extracellular domains	510:547	the two receptor extracellular domains	510:547	Here, we present a crystal structure of human IL-18 bound to the two receptor extracellular domains.
25500532	3	41	theme	signalling	310:319	arg1	complex					321:327	a signalling complex	308:327	a signalling complex	308:327	IL-18 forms a signalling complex with the IL-18 receptor α (Rα) and β (Rβ) chains at the plasma membrane, which induces multiple inflammatory cytokines.
25500532	0	42	theme	interleukin-18	55:68	arg1	recognition					34:44	receptor recognition	25:44	receptor recognition of human interleukin-18	25:68	The structural basis for receptor recognition of human interleukin-18.
25500532	6	43	theme	IL-1	827:830	arg1	receptors					832:840	the IL-1 receptors	823:840	the IL-1 receptors that exhibit a more promiscuous ligand recognition mode	823:896	The architecture of the IL-18 receptor second domain (D2) is unique among the other IL-1R family members, which presumably distinguishes them from the IL-1 receptors that exhibit a more promiscuous ligand recognition mode.
25500532	3	44	with	complex	321:327	arg1	chains					371:376	the IL-18 receptor α (Rα) and β (Rβ) chains	334:376	the IL-18 receptor α (Rα) and β (Rβ) chains at the plasma membrane	334:399	IL-18 forms a signalling complex with the IL-18 receptor α (Rα) and β (Rβ) chains at the plasma membrane, which induces multiple inflammatory cytokines.
25500532	6	45	theme	recognition	881:891	arg1	mode					893:896	a more promiscuous ligand recognition mode	855:896	a more promiscuous ligand recognition mode	855:896	The architecture of the IL-18 receptor second domain (D2) is unique among the other IL-1R family members, which presumably distinguishes them from the IL-1 receptors that exhibit a more promiscuous ligand recognition mode.
25261253	1	0	theme	immune	193:198	arg1	responses					200:208	innate and acquired immune responses	173:208	innate and acquired immune responses	173:208	Interleukin 18 (IL-18), a member of the IL-1 family of cytokines, is an important regulator of innate and acquired immune responses.
25261253	0	1	theme	alpha	62:66	arg1	receptor					68:75	its alpha receptor	58:75	its alpha receptor	58:75	Structural basis for the specific recognition of IL-18 by its alpha receptor.
25261253	4	2	theme	surface	468:474	arg1	complementarity					483:497	surface charge complementarity	468:497	surface charge complementarity	468:497	It confirms that surface charge complementarity determines the ligand-binding specificity of primary receptors in the IL-1 receptor family.
25261253	1	3	theme	IL-1	118:121	arg1	family					123:128	the IL-1 family	114:128	the IL-1 family of cytokines	114:141	Interleukin 18 (IL-18), a member of the IL-1 family of cytokines, is an important regulator of innate and acquired immune responses.
25261253	1	4	theme	responses	200:208	arg1	Interleukin					78:88	Interleukin 18	78:91	Interleukin 18 (IL-18)	78:99	Interleukin 18 (IL-18), a member of the IL-1 family of cytokines, is an important regulator of innate and acquired immune responses.
25261253	1	4	theme	responses	200:208	arg1	regulator					160:168	an important regulator	147:168	an important regulator of innate and acquired immune responses	147:208	Interleukin 18 (IL-18), a member of the IL-1 family of cytokines, is an important regulator of innate and acquired immune responses.
25261253	5	5	theme	general	705:711	arg1	assembly					729:736	a general ligand-receptor assembly and activation model	703:757	assembly	729:736	We suggest that IL-18 signaling complex adopts an architecture similar to other agonistic cytokines and propose a general ligand-receptor assembly and activation model for the IL-1 family.
25261253	2	6	theme	ligand-binding	234:247	arg1	IL-18Rα					266:272	its ligand-binding primary receptor IL-18Rα	230:272	its ligand-binding primary receptor IL-18Rα	230:272	It signals through its ligand-binding primary receptor IL-18Rα and accessory receptor IL-18Rβ.
25261253	4	7	theme	IL-1	569:572	arg1	family					583:588	the IL-1 receptor family	565:588	the IL-1 receptor family	565:588	It confirms that surface charge complementarity determines the ligand-binding specificity of primary receptors in the IL-1 receptor family.
25261253	5	8	theme	ligand-receptor	713:727	arg1	assembly					729:736	a general ligand-receptor assembly and activation model	703:757	assembly	729:736	We suggest that IL-18 signaling complex adopts an architecture similar to other agonistic cytokines and propose a general ligand-receptor assembly and activation model for the IL-1 family.
25261253	2	9	theme	accessory	278:286	arg1	IL-18Rβ					297:303	accessory receptor IL-18Rβ	278:303	accessory receptor IL-18Rβ	278:303	It signals through its ligand-binding primary receptor IL-18Rα and accessory receptor IL-18Rβ.
25261253	1	10	theme	cytokines	133:141	arg1	family					123:128	the IL-1 family	114:128	the IL-1 family of cytokines	114:141	Interleukin 18 (IL-18), a member of the IL-1 family of cytokines, is an important regulator of innate and acquired immune responses.
25261253	1	11	theme	family	123:128	arg1	Interleukin					78:88	Interleukin 18	78:91	Interleukin 18 (IL-18)	78:99	Interleukin 18 (IL-18), a member of the IL-1 family of cytokines, is an important regulator of innate and acquired immune responses.
25261253	1	11	theme	family	123:128	arg1	member					104:109	a member	102:109	a member of the IL-1 family of cytokines	102:141	Interleukin 18 (IL-18), a member of the IL-1 family of cytokines, is an important regulator of innate and acquired immune responses.
25261253	3	12	theme	IL-18	346:350	arg1	structure					333:341	the crystal structure	321:341	the crystal structure of IL-18 with the ectodomain of IL-18Rα, which reveals the structural basis for their specific recognition	321:448	Here we report the crystal structure of IL-18 with the ectodomain of IL-18Rα, which reveals the structural basis for their specific recognition.
25261253	5	13	theme	IL-18	607:611	arg1	complex					623:629	IL-18 signaling complex	607:629	IL-18 signaling complex	607:629	We suggest that IL-18 signaling complex adopts an architecture similar to other agonistic cytokines and propose a general ligand-receptor assembly and activation model for the IL-1 family.
25261253	3	14	theme	IL-18Rα	375:381	arg1	IL-18Rα					375:381	IL-18Rα	375:381	IL-18Rα	375:381	Here we report the crystal structure of IL-18 with the ectodomain of IL-18Rα, which reveals the structural basis for their specific recognition.
25261253	3	14	theme	IL-18Rα	375:381	arg1	ectodomain					361:370	the ectodomain	357:370	the ectodomain	357:370	Here we report the crystal structure of IL-18 with the ectodomain of IL-18Rα, which reveals the structural basis for their specific recognition.
25261253	0	15	theme	Structural	0:9	arg1	basis					11:15	Structural basis	0:15	Structural basis for the specific recognition of IL-18 by its alpha receptor	0:75	Structural basis for the specific recognition of IL-18 by its alpha receptor.
25261253	5	16	theme	signaling	613:621	arg1	complex					623:629	IL-18 signaling complex	607:629	IL-18 signaling complex	607:629	We suggest that IL-18 signaling complex adopts an architecture similar to other agonistic cytokines and propose a general ligand-receptor assembly and activation model for the IL-1 family.
25261253	3	17	with	structure	333:341	arg1	IL-18Rα					375:381	IL-18Rα	375:381	IL-18Rα	375:381	Here we report the crystal structure of IL-18 with the ectodomain of IL-18Rα, which reveals the structural basis for their specific recognition.
25261253	3	17	with	structure	333:341	arg1	ectodomain					361:370	the ectodomain	357:370	the ectodomain	357:370	Here we report the crystal structure of IL-18 with the ectodomain of IL-18Rα, which reveals the structural basis for their specific recognition.
25261253	3	18	theme	crystal	325:331	arg1	structure					333:341	the crystal structure	321:341	the crystal structure of IL-18 with the ectodomain of IL-18Rα, which reveals the structural basis for their specific recognition	321:448	Here we report the crystal structure of IL-18 with the ectodomain of IL-18Rα, which reveals the structural basis for their specific recognition.
25261253	4	19	theme	ligand-binding	514:527	arg1	specificity					529:539	the ligand-binding specificity	510:539	the ligand-binding specificity of primary receptors in the IL-1 receptor family	510:588	It confirms that surface charge complementarity determines the ligand-binding specificity of primary receptors in the IL-1 receptor family.
25261253	2	20	theme	receptor	257:264	arg1	IL-18Rα					266:272	its ligand-binding primary receptor IL-18Rα	230:272	its ligand-binding primary receptor IL-18Rα	230:272	It signals through its ligand-binding primary receptor IL-18Rα and accessory receptor IL-18Rβ.
25261253	4	21	theme	primary	544:550	arg1	receptors					552:560	primary receptors	544:560	primary receptors	544:560	It confirms that surface charge complementarity determines the ligand-binding specificity of primary receptors in the IL-1 receptor family.
25261253	2	22	theme	primary	249:255	arg1	IL-18Rα					266:272	its ligand-binding primary receptor IL-18Rα	230:272	its ligand-binding primary receptor IL-18Rα	230:272	It signals through its ligand-binding primary receptor IL-18Rα and accessory receptor IL-18Rβ.
25261253	5	23	theme	IL-1	767:770	arg1	family					772:777	the IL-1 family	763:777	the IL-1 family	763:777	We suggest that IL-18 signaling complex adopts an architecture similar to other agonistic cytokines and propose a general ligand-receptor assembly and activation model for the IL-1 family.
25261253	1	24	theme	important	150:158	arg1	Interleukin					78:88	Interleukin 18	78:91	Interleukin 18 (IL-18)	78:99	Interleukin 18 (IL-18), a member of the IL-1 family of cytokines, is an important regulator of innate and acquired immune responses.
25261253	1	24	theme	important	150:158	arg1	regulator					160:168	an important regulator	147:168	an important regulator of innate and acquired immune responses	147:208	Interleukin 18 (IL-18), a member of the IL-1 family of cytokines, is an important regulator of innate and acquired immune responses.
25261253	0	25	theme	specific	25:32	arg1	recognition					34:44	the specific recognition	21:44	the specific recognition of IL-18 by its alpha receptor	21:75	Structural basis for the specific recognition of IL-18 by its alpha receptor.
25261253	4	26	theme	receptors	552:560	arg1	specificity					529:539	the ligand-binding specificity	510:539	the ligand-binding specificity of primary receptors in the IL-1 receptor family	510:588	It confirms that surface charge complementarity determines the ligand-binding specificity of primary receptors in the IL-1 receptor family.
25261253	4	27	from	specificity	529:539	arg1	family					583:588	the IL-1 receptor family	565:588	the IL-1 receptor family	565:588	It confirms that surface charge complementarity determines the ligand-binding specificity of primary receptors in the IL-1 receptor family.
25261253	3	28	theme	structural	402:411	arg1	basis					413:417	the structural basis	398:417	the structural basis for their specific recognition	398:448	Here we report the crystal structure of IL-18 with the ectodomain of IL-18Rα, which reveals the structural basis for their specific recognition.
25261253	0	29	theme	IL-18	49:53	arg1	recognition					34:44	the specific recognition	21:44	the specific recognition of IL-18 by its alpha receptor	21:75	Structural basis for the specific recognition of IL-18 by its alpha receptor.
25261253	4	30	theme	charge	476:481	arg1	complementarity					483:497	surface charge complementarity	468:497	surface charge complementarity	468:497	It confirms that surface charge complementarity determines the ligand-binding specificity of primary receptors in the IL-1 receptor family.
25261253	5	31	theme	similar	654:660	arg1	architecture					641:652	an architecture	638:652	an architecture similar to other agonistic cytokines	638:689	We suggest that IL-18 signaling complex adopts an architecture similar to other agonistic cytokines and propose a general ligand-receptor assembly and activation model for the IL-1 family.
25261253	4	32	theme	receptor	574:581	arg1	family					583:588	the IL-1 receptor family	565:588	the IL-1 receptor family	565:588	It confirms that surface charge complementarity determines the ligand-binding specificity of primary receptors in the IL-1 receptor family.
25261253	5	33	theme	other	665:669	arg1	cytokines					681:689	other agonistic cytokines	665:689	other agonistic cytokines	665:689	We suggest that IL-18 signaling complex adopts an architecture similar to other agonistic cytokines and propose a general ligand-receptor assembly and activation model for the IL-1 family.
25261253	2	34	theme	receptor	288:295	arg1	IL-18Rβ					297:303	accessory receptor IL-18Rβ	278:303	accessory receptor IL-18Rβ	278:303	It signals through its ligand-binding primary receptor IL-18Rα and accessory receptor IL-18Rβ.
25261253	5	35	theme	agonistic	671:679	arg1	cytokines					681:689	other agonistic cytokines	665:689	other agonistic cytokines	665:689	We suggest that IL-18 signaling complex adopts an architecture similar to other agonistic cytokines and propose a general ligand-receptor assembly and activation model for the IL-1 family.
25261253	3	36	theme	specific	429:436	arg1	recognition					438:448	their specific recognition	423:448	their specific recognition	423:448	Here we report the crystal structure of IL-18 with the ectodomain of IL-18Rα, which reveals the structural basis for their specific recognition.
25261253	1	37	theme	innate	173:178	arg1	responses					200:208	innate and acquired immune responses	173:208	innate and acquired immune responses	173:208	Interleukin 18 (IL-18), a member of the IL-1 family of cytokines, is an important regulator of innate and acquired immune responses.
25261253	5	38	theme	activation	742:751	arg1	model					753:757	a general ligand-receptor assembly and activation model	703:757	model	753:757	We suggest that IL-18 signaling complex adopts an architecture similar to other agonistic cytokines and propose a general ligand-receptor assembly and activation model for the IL-1 family.
25261253	1	39	theme	acquired	184:191	arg1	responses					200:208	innate and acquired immune responses	173:208	innate and acquired immune responses	173:208	Interleukin 18 (IL-18), a member of the IL-1 family of cytokines, is an important regulator of innate and acquired immune responses.
20540760	8	0	theme	dipeptidyl	1175:1184	arg1	proteolysis					1186:1196	dipeptidyl proteolysis	1175:1196	dipeptidyl proteolysis of N-terminal substrates	1175:1221	In contrast, the substrate binding groove of DPP7 is occluded by a short amino-acid insertion unique to DPP7 that creates a truncated active site selective for dipeptidyl proteolysis of N-terminal substrates.
20540760	8	1	theme	selective	1161:1169	arg1	site					1156:1159	a truncated active site	1137:1159	a truncated active site selective for dipeptidyl proteolysis of N-terminal substrates	1137:1221	In contrast, the substrate binding groove of DPP7 is occluded by a short amino-acid insertion unique to DPP7 that creates a truncated active site selective for dipeptidyl proteolysis of N-terminal substrates.
20540760	7	2	contain	has	906:908	arg1	PRCP					901:904	PRCP	901:904	PRCP	901:904	PRCP has an extended active-site cleft that can accommodate proline substrates with multiple N-terminal residues.
20540760	7	2	contain	has	906:908	arg2	cleft					934:938	an extended active-site cleft	910:938	an extended active-site cleft that can accommodate proline substrates with multiple N-terminal residues	910:1012	PRCP has an extended active-site cleft that can accommodate proline substrates with multiple N-terminal residues.
20540760	6	3	with	alignment	761:769	arg1	structure					803:811	the previously undescribed structure	776:811	the previously undescribed structure of DPP7	776:819	A structure-based alignment with the previously undescribed structure of DPP7 illuminates the mechanism of orthogonal substrate specificity of PRCP and DPP7.
20540760	5	4	with	comparisons	651:661	arg1	DPP4					692:695	DPP4	692:695	DPP4	692:695	Structural comparisons with prolylendopeptidase and DPP4 identify the S1 proline binding site of PRCP.
20540760	5	4	with	comparisons	651:661	arg1	prolylendopeptidase					668:686	prolylendopeptidase	668:686	prolylendopeptidase	668:686	Structural comparisons with prolylendopeptidase and DPP4 identify the S1 proline binding site of PRCP.
20540760	7	5	theme	extended	913:920	arg1	cleft					934:938	an extended active-site cleft	910:938	an extended active-site cleft that can accommodate proline substrates with multiple N-terminal residues	910:1012	PRCP has an extended active-site cleft that can accommodate proline substrates with multiple N-terminal residues.
20540760	4	6	theme	novel	581:585	arg1	domain					606:611	a novel helical structural domain	579:611	a novel helical structural domain that caps the active site	579:637	PRCP contains an alpha/beta hydrolase domain harboring the catalytic Asp-His-Ser triad and a novel helical structural domain that caps the active site.
20540760	5	7	theme	binding	721:727	arg1	PRCP					737:740	PRCP	737:740	PRCP	737:740	Structural comparisons with prolylendopeptidase and DPP4 identify the S1 proline binding site of PRCP.
20540760	5	7	theme	binding	721:727	arg1	site					729:732	the S1 proline binding site	706:732	the S1 proline binding site of PRCP	706:740	Structural comparisons with prolylendopeptidase and DPP4 identify the S1 proline binding site of PRCP.
20540760	4	8	theme	alpha/beta	505:514	arg1	domain					526:531	an alpha/beta hydrolase domain	502:531	an alpha/beta hydrolase domain harboring the catalytic Asp-His-Ser triad	502:573	PRCP contains an alpha/beta hydrolase domain harboring the catalytic Asp-His-Ser triad and a novel helical structural domain that caps the active site.
20540760	8	9	theme	DPP7	1060:1063	arg1	groove					1050:1055	the substrate binding groove	1028:1055	the substrate binding groove of DPP7	1028:1063	In contrast, the substrate binding groove of DPP7 is occluded by a short amino-acid insertion unique to DPP7 that creates a truncated active site selective for dipeptidyl proteolysis of N-terminal substrates.
20540760	4	10	contain	contains	493:500	arg2	domain					526:531	an alpha/beta hydrolase domain	502:531	an alpha/beta hydrolase domain harboring the catalytic Asp-His-Ser triad	502:573	PRCP contains an alpha/beta hydrolase domain harboring the catalytic Asp-His-Ser triad and a novel helical structural domain that caps the active site.
20540760	4	10	contain	contains	493:500	arg2	domain					606:611	a novel helical structural domain	579:611	a novel helical structural domain that caps the active site	579:637	PRCP contains an alpha/beta hydrolase domain harboring the catalytic Asp-His-Ser triad and a novel helical structural domain that caps the active site.
20540760	4	10	contain	contains	493:500	arg1	PRCP					488:491	PRCP	488:491	PRCP	488:491	PRCP contains an alpha/beta hydrolase domain harboring the catalytic Asp-His-Ser triad and a novel helical structural domain that caps the active site.
20540760	8	11	theme	binding	1042:1048	arg1	groove					1050:1055	the substrate binding groove	1028:1055	the substrate binding groove of DPP7	1028:1063	In contrast, the substrate binding groove of DPP7 is occluded by a short amino-acid insertion unique to DPP7 that creates a truncated active site selective for dipeptidyl proteolysis of N-terminal substrates.
20540760	5	12	theme	PRCP	737:740	arg1	PRCP					737:740	PRCP	737:740	PRCP	737:740	Structural comparisons with prolylendopeptidase and DPP4 identify the S1 proline binding site of PRCP.
20540760	5	12	theme	PRCP	737:740	arg1	site					729:732	the S1 proline binding site	706:732	the S1 proline binding site of PRCP	706:740	Structural comparisons with prolylendopeptidase and DPP4 identify the S1 proline binding site of PRCP.
20540760	9	13	theme	PRCP	1332:1335	arg1	basis					1323:1327	the structural basis	1308:1327	the structural basis of PRCP and DPP7 substrate specificity	1308:1366	CONCLUSION The results define the structure of the S28 family of proteases, provide the structural basis of PRCP and DPP7 substrate specificity and enable the rational design of selective PRCP modulators.
20540760	2	14	theme	specificities	296:308	arg1	basis					263:267	The structural basis	248:267	The structural basis of the different substrate specificities of the two enzymes	248:327	The structural basis of the different substrate specificities of the two enzymes is not understood nor has the structure of the S28 fold been described.
20540760	4	15	theme	structural	595:604	arg1	domain					606:611	a novel helical structural domain	579:611	a novel helical structural domain that caps the active site	579:637	PRCP contains an alpha/beta hydrolase domain harboring the catalytic Asp-His-Ser triad and a novel helical structural domain that caps the active site.
20540760	0	16	theme	crystal	80:86	arg1	structure					88:96	the crystal structure	76:96	Structural definition and substrate specificity of the S28 protease family: the crystal structure of human prolylcarboxypeptidase.	0:129	Structural definition and substrate specificity of the S28 protease family: the crystal structure of human prolylcarboxypeptidase.
20540760	7	17	theme	multiple	985:992	arg1	residues					1005:1012	multiple N-terminal residues	985:1012	multiple N-terminal residues	985:1012	PRCP has an extended active-site cleft that can accommodate proline substrates with multiple N-terminal residues.
20540760	2	18	theme	substrate	286:294	arg1	specificities					296:308	the different substrate specificities	272:308	the different substrate specificities of the two enzymes	272:327	The structural basis of the different substrate specificities of the two enzymes is not understood nor has the structure of the S28 fold been described.
20540760	4	19	theme	helical	587:593	arg1	domain					606:611	a novel helical structural domain	579:611	a novel helical structural domain that caps the active site	579:637	PRCP contains an alpha/beta hydrolase domain harboring the catalytic Asp-His-Ser triad and a novel helical structural domain that caps the active site.
20540760	0	20	theme	human	101:105	arg1	prolylcarboxypeptidase					107:128	human prolylcarboxypeptidase	101:128	human prolylcarboxypeptidase	101:128	Structural definition and substrate specificity of the S28 protease family: the crystal structure of human prolylcarboxypeptidase.
20540760	9	21	theme	DPP7	1341:1344	arg1	specificity					1356:1366	DPP7 substrate specificity	1341:1366	DPP7 substrate specificity	1341:1366	CONCLUSION The results define the structure of the S28 family of proteases, provide the structural basis of PRCP and DPP7 substrate specificity and enable the rational design of selective PRCP modulators.
20540760	8	22	theme	substrates	1212:1221	arg1	proteolysis					1186:1196	dipeptidyl proteolysis	1175:1196	dipeptidyl proteolysis of N-terminal substrates	1175:1221	In contrast, the substrate binding groove of DPP7 is occluded by a short amino-acid insertion unique to DPP7 that creates a truncated active site selective for dipeptidyl proteolysis of N-terminal substrates.
20540760	4	23	theme	active	627:632	arg1	site					634:637	the active site	623:637	the active site	623:637	PRCP contains an alpha/beta hydrolase domain harboring the catalytic Asp-His-Ser triad and a novel helical structural domain that caps the active site.
20540760	2	24	theme	different	276:284	arg1	specificities					296:308	the different substrate specificities	272:308	the different substrate specificities of the two enzymes	272:327	The structural basis of the different substrate specificities of the two enzymes is not understood nor has the structure of the S28 fold been described.
20540760	1	25	theme	proteases	167:175	arg1	family					157:162	The unique S28 family	142:162	The unique S28 family of proteases	142:175	BACKGROUND The unique S28 family of proteases is comprised of the carboxypeptidase PRCP and the aminopeptidase DPP7.
20540760	8	26	theme	N-terminal	1201:1210	arg1	substrates					1212:1221	N-terminal substrates	1201:1221	N-terminal substrates	1201:1221	In contrast, the substrate binding groove of DPP7 is occluded by a short amino-acid insertion unique to DPP7 that creates a truncated active site selective for dipeptidyl proteolysis of N-terminal substrates.
20540760	9	27	theme	substrate	1346:1354	arg1	specificity					1356:1366	DPP7 substrate specificity	1341:1366	DPP7 substrate specificity	1341:1366	CONCLUSION The results define the structure of the S28 family of proteases, provide the structural basis of PRCP and DPP7 substrate specificity and enable the rational design of selective PRCP modulators.
20540760	6	28	theme	PRCP	886:889	arg1	specificity					871:881	orthogonal substrate specificity	850:881	orthogonal substrate specificity of PRCP and DPP7	850:898	A structure-based alignment with the previously undescribed structure of DPP7 illuminates the mechanism of orthogonal substrate specificity of PRCP and DPP7.
20540760	3	29	theme	A	439:439	arg1	structure					449:457	RESULTS The experimentally phased 2.8 A crystal structure	401:457	RESULTS The experimentally phased 2.8 A crystal structure	401:457	RESULTS The experimentally phased 2.8 A crystal structure is presented for human PRCP.
20540760	9	30	theme	specificity	1356:1366	arg1	basis					1323:1327	the structural basis	1308:1327	the structural basis of PRCP and DPP7 substrate specificity	1308:1366	CONCLUSION The results define the structure of the S28 family of proteases, provide the structural basis of PRCP and DPP7 substrate specificity and enable the rational design of selective PRCP modulators.
20540760	8	31	theme	substrate	1032:1040	arg1	groove					1050:1055	the substrate binding groove	1028:1055	the substrate binding groove of DPP7	1028:1063	In contrast, the substrate binding groove of DPP7 is occluded by a short amino-acid insertion unique to DPP7 that creates a truncated active site selective for dipeptidyl proteolysis of N-terminal substrates.
20540760	2	32	theme	enzymes	321:327	arg1	specificities					296:308	the different substrate specificities	272:308	the different substrate specificities of the two enzymes	272:327	The structural basis of the different substrate specificities of the two enzymes is not understood nor has the structure of the S28 fold been described.
20540760	2	33	theme	S28	376:378	arg1	structure					359:367	the structure	355:367	the structure of the S28	355:378	The structural basis of the different substrate specificities of the two enzymes is not understood nor has the structure of the S28 fold been described.
20540760	0	34	theme	Structural	0:9	arg1	definition					11:20	Structural definition	0:20	Structural definition	0:20	Structural definition and substrate specificity of the S28 protease family: the crystal structure of human prolylcarboxypeptidase.
20540760	4	35	theme	Asp-His-Ser	557:567	arg1	triad					569:573	the catalytic Asp-His-Ser triad	543:573	the catalytic Asp-His-Ser triad	543:573	PRCP contains an alpha/beta hydrolase domain harboring the catalytic Asp-His-Ser triad and a novel helical structural domain that caps the active site.
20540760	5	36	theme	Structural	640:649	arg1	comparisons					651:661	Structural comparisons	640:661	Structural comparisons with prolylendopeptidase and DPP4	640:695	Structural comparisons with prolylendopeptidase and DPP4 identify the S1 proline binding site of PRCP.
20540760	8	37	theme	short	1082:1086	arg1	insertion					1099:1107	a short amino-acid insertion	1080:1107	a short amino-acid insertion unique to DPP7 that creates a truncated active site selective for dipeptidyl proteolysis of N-terminal substrates	1080:1221	In contrast, the substrate binding groove of DPP7 is occluded by a short amino-acid insertion unique to DPP7 that creates a truncated active site selective for dipeptidyl proteolysis of N-terminal substrates.
20540760	3	38	theme	phased	428:433	arg1	structure					449:457	RESULTS The experimentally phased 2.8 A crystal structure	401:457	RESULTS The experimentally phased 2.8 A crystal structure	401:457	RESULTS The experimentally phased 2.8 A crystal structure is presented for human PRCP.
20540760	0	39	theme	substrate	26:34	arg1	specificity					36:46	substrate specificity	26:46	substrate specificity	26:46	Structural definition and substrate specificity of the S28 protease family: the crystal structure of human prolylcarboxypeptidase.
20540760	0	40	dep	definition	11:20	arg1	structure					88:96	the crystal structure	76:96	Structural definition and substrate specificity of the S28 protease family: the crystal structure of human prolylcarboxypeptidase.	0:129	Structural definition and substrate specificity of the S28 protease family: the crystal structure of human prolylcarboxypeptidase.
20540760	5	41	theme	proline	713:719	arg1	PRCP					737:740	PRCP	737:740	PRCP	737:740	Structural comparisons with prolylendopeptidase and DPP4 identify the S1 proline binding site of PRCP.
20540760	5	41	theme	proline	713:719	arg1	site					729:732	the S1 proline binding site	706:732	the S1 proline binding site of PRCP	706:740	Structural comparisons with prolylendopeptidase and DPP4 identify the S1 proline binding site of PRCP.
20540760	6	42	theme	undescribed	791:801	arg1	structure					803:811	the previously undescribed structure	776:811	the previously undescribed structure of DPP7	776:819	A structure-based alignment with the previously undescribed structure of DPP7 illuminates the mechanism of orthogonal substrate specificity of PRCP and DPP7.
20540760	9	43	theme	S28	1275:1277	arg1	family					1279:1284	the S28 family	1271:1284	the S28 family of proteases	1271:1297	CONCLUSION The results define the structure of the S28 family of proteases, provide the structural basis of PRCP and DPP7 substrate specificity and enable the rational design of selective PRCP modulators.
20540760	0	44	theme	prolylcarboxypeptidase	107:128	arg1	structure					88:96	the crystal structure	76:96	Structural definition and substrate specificity of the S28 protease family: the crystal structure of human prolylcarboxypeptidase.	0:129	Structural definition and substrate specificity of the S28 protease family: the crystal structure of human prolylcarboxypeptidase.
20540760	7	45	theme	N-terminal	994:1003	arg1	residues					1005:1012	multiple N-terminal residues	985:1012	multiple N-terminal residues	985:1012	PRCP has an extended active-site cleft that can accommodate proline substrates with multiple N-terminal residues.
20540760	1	46	theme	carboxypeptidase	197:212	arg1	PRCP					214:217	the carboxypeptidase PRCP	193:217	the carboxypeptidase PRCP	193:217	BACKGROUND The unique S28 family of proteases is comprised of the carboxypeptidase PRCP and the aminopeptidase DPP7.
20540760	3	47	theme	RESULTS	401:407	arg1	structure					449:457	RESULTS The experimentally phased 2.8 A crystal structure	401:457	RESULTS The experimentally phased 2.8 A crystal structure	401:457	RESULTS The experimentally phased 2.8 A crystal structure is presented for human PRCP.
20540760	9	48	theme	rational	1383:1390	arg1	design					1392:1397	the rational design	1379:1397	the rational design of selective PRCP modulators	1379:1426	CONCLUSION The results define the structure of the S28 family of proteases, provide the structural basis of PRCP and DPP7 substrate specificity and enable the rational design of selective PRCP modulators.
20540760	6	49	theme	DPP7	895:898	arg1	specificity					871:881	orthogonal substrate specificity	850:881	orthogonal substrate specificity of PRCP and DPP7	850:898	A structure-based alignment with the previously undescribed structure of DPP7 illuminates the mechanism of orthogonal substrate specificity of PRCP and DPP7.
20540760	8	50	theme	unique	1109:1114	arg1	insertion					1099:1107	a short amino-acid insertion	1080:1107	a short amino-acid insertion unique to DPP7 that creates a truncated active site selective for dipeptidyl proteolysis of N-terminal substrates	1080:1221	In contrast, the substrate binding groove of DPP7 is occluded by a short amino-acid insertion unique to DPP7 that creates a truncated active site selective for dipeptidyl proteolysis of N-terminal substrates.
20540760	3	51	theme	crystal	441:447	arg1	structure					449:457	RESULTS The experimentally phased 2.8 A crystal structure	401:457	RESULTS The experimentally phased 2.8 A crystal structure	401:457	RESULTS The experimentally phased 2.8 A crystal structure is presented for human PRCP.
20540760	3	52	theme	2.8	435:437	arg1	structure					449:457	RESULTS The experimentally phased 2.8 A crystal structure	401:457	RESULTS The experimentally phased 2.8 A crystal structure	401:457	RESULTS The experimentally phased 2.8 A crystal structure is presented for human PRCP.
20540760	9	53	theme	family	1279:1284	arg1	structure					1258:1266	the structure	1254:1266	the structure of the S28 family of proteases	1254:1297	CONCLUSION The results define the structure of the S28 family of proteases, provide the structural basis of PRCP and DPP7 substrate specificity and enable the rational design of selective PRCP modulators.
20540760	9	54	theme	PRCP	1412:1415	arg1	modulators					1417:1426	selective PRCP modulators	1402:1426	selective PRCP modulators	1402:1426	CONCLUSION The results define the structure of the S28 family of proteases, provide the structural basis of PRCP and DPP7 substrate specificity and enable the rational design of selective PRCP modulators.
20540760	0	55	theme	S28	55:57	arg1	family					68:73	the S28 protease family	51:73	the S28 protease family	51:73	Structural definition and substrate specificity of the S28 protease family: the crystal structure of human prolylcarboxypeptidase.
20540760	4	56	theme	hydrolase	516:524	arg1	domain					526:531	an alpha/beta hydrolase domain	502:531	an alpha/beta hydrolase domain harboring the catalytic Asp-His-Ser triad	502:573	PRCP contains an alpha/beta hydrolase domain harboring the catalytic Asp-His-Ser triad and a novel helical structural domain that caps the active site.
20540760	4	57	theme	catalytic	547:555	arg1	triad					569:573	the catalytic Asp-His-Ser triad	543:573	the catalytic Asp-His-Ser triad	543:573	PRCP contains an alpha/beta hydrolase domain harboring the catalytic Asp-His-Ser triad and a novel helical structural domain that caps the active site.
20540760	9	58	theme	selective	1402:1410	arg1	modulators					1417:1426	selective PRCP modulators	1402:1426	selective PRCP modulators	1402:1426	CONCLUSION The results define the structure of the S28 family of proteases, provide the structural basis of PRCP and DPP7 substrate specificity and enable the rational design of selective PRCP modulators.
20540760	9	59	theme	proteases	1289:1297	arg1	family					1279:1284	the S28 family	1271:1284	the S28 family of proteases	1271:1297	CONCLUSION The results define the structure of the S28 family of proteases, provide the structural basis of PRCP and DPP7 substrate specificity and enable the rational design of selective PRCP modulators.
20540760	8	60	theme	amino-acid	1088:1097	arg1	insertion					1099:1107	a short amino-acid insertion	1080:1107	a short amino-acid insertion unique to DPP7 that creates a truncated active site selective for dipeptidyl proteolysis of N-terminal substrates	1080:1221	In contrast, the substrate binding groove of DPP7 is occluded by a short amino-acid insertion unique to DPP7 that creates a truncated active site selective for dipeptidyl proteolysis of N-terminal substrates.
20540760	7	61	theme	proline	961:967	arg1	substrates					969:978	proline substrates	961:978	proline substrates	961:978	PRCP has an extended active-site cleft that can accommodate proline substrates with multiple N-terminal residues.
20540760	8	62	theme	active	1149:1154	arg1	site					1156:1159	a truncated active site	1137:1159	a truncated active site selective for dipeptidyl proteolysis of N-terminal substrates	1137:1221	In contrast, the substrate binding groove of DPP7 is occluded by a short amino-acid insertion unique to DPP7 that creates a truncated active site selective for dipeptidyl proteolysis of N-terminal substrates.
20540760	6	63	theme	specificity	871:881	arg1	mechanism					837:845	the mechanism	833:845	the mechanism of orthogonal substrate specificity of PRCP and DPP7	833:898	A structure-based alignment with the previously undescribed structure of DPP7 illuminates the mechanism of orthogonal substrate specificity of PRCP and DPP7.
20540760	8	64	theme	truncated	1139:1147	arg1	site					1156:1159	a truncated active site	1137:1159	a truncated active site selective for dipeptidyl proteolysis of N-terminal substrates	1137:1221	In contrast, the substrate binding groove of DPP7 is occluded by a short amino-acid insertion unique to DPP7 that creates a truncated active site selective for dipeptidyl proteolysis of N-terminal substrates.
20540760	6	65	theme	DPP7	816:819	arg1	structure					803:811	the previously undescribed structure	776:811	the previously undescribed structure of DPP7	776:819	A structure-based alignment with the previously undescribed structure of DPP7 illuminates the mechanism of orthogonal substrate specificity of PRCP and DPP7.
20540760	9	66	theme	modulators	1417:1426	arg1	design					1392:1397	the rational design	1379:1397	the rational design of selective PRCP modulators	1379:1426	CONCLUSION The results define the structure of the S28 family of proteases, provide the structural basis of PRCP and DPP7 substrate specificity and enable the rational design of selective PRCP modulators.
20540760	5	67	theme	S1	710:711	arg1	PRCP					737:740	PRCP	737:740	PRCP	737:740	Structural comparisons with prolylendopeptidase and DPP4 identify the S1 proline binding site of PRCP.
20540760	5	67	theme	S1	710:711	arg1	site					729:732	the S1 proline binding site	706:732	the S1 proline binding site of PRCP	706:740	Structural comparisons with prolylendopeptidase and DPP4 identify the S1 proline binding site of PRCP.
20540760	6	68	theme	substrate	861:869	arg1	specificity					871:881	orthogonal substrate specificity	850:881	orthogonal substrate specificity of PRCP and DPP7	850:898	A structure-based alignment with the previously undescribed structure of DPP7 illuminates the mechanism of orthogonal substrate specificity of PRCP and DPP7.
20540760	1	69	dep	BACKGROUND	131:140	arg1	comprised					180:188	comprised	180:188	is comprised of the carboxypeptidase PRCP and the aminopeptidase DPP7	177:245	BACKGROUND The unique S28 family of proteases is comprised of the carboxypeptidase PRCP and the aminopeptidase DPP7.
20540760	6	70	theme	structure-based	745:759	arg1	alignment					761:769	A structure-based alignment	743:769	A structure-based alignment with the previously undescribed structure of DPP7	743:819	A structure-based alignment with the previously undescribed structure of DPP7 illuminates the mechanism of orthogonal substrate specificity of PRCP and DPP7.
20540760	3	71	theme	human	476:480	arg1	PRCP					482:485	human PRCP	476:485	human PRCP	476:485	RESULTS The experimentally phased 2.8 A crystal structure is presented for human PRCP.
20540760	7	72	theme	active-site	922:932	arg1	cleft					934:938	an extended active-site cleft	910:938	an extended active-site cleft that can accommodate proline substrates with multiple N-terminal residues	910:1012	PRCP has an extended active-site cleft that can accommodate proline substrates with multiple N-terminal residues.
20540760	1	73	theme	aminopeptidase	227:240	arg1	DPP7					242:245	the aminopeptidase DPP7	223:245	the aminopeptidase DPP7	223:245	BACKGROUND The unique S28 family of proteases is comprised of the carboxypeptidase PRCP and the aminopeptidase DPP7.
20540760	0	74	theme	family	68:73	arg1	definition					11:20	Structural definition	0:20	Structural definition	0:20	Structural definition and substrate specificity of the S28 protease family: the crystal structure of human prolylcarboxypeptidase.
20540760	0	74	theme	family	68:73	arg1	specificity					36:46	substrate specificity	26:46	substrate specificity	26:46	Structural definition and substrate specificity of the S28 protease family: the crystal structure of human prolylcarboxypeptidase.
20540760	6	75	theme	orthogonal	850:859	arg1	specificity					871:881	orthogonal substrate specificity	850:881	orthogonal substrate specificity of PRCP and DPP7	850:898	A structure-based alignment with the previously undescribed structure of DPP7 illuminates the mechanism of orthogonal substrate specificity of PRCP and DPP7.
20540760	2	76	theme	structural	252:261	arg1	basis					263:267	The structural basis	248:267	The structural basis of the different substrate specificities of the two enzymes	248:327	The structural basis of the different substrate specificities of the two enzymes is not understood nor has the structure of the S28 fold been described.
20540760	1	77	theme	unique	146:151	arg1	family					157:162	The unique S28 family	142:162	The unique S28 family of proteases	142:175	BACKGROUND The unique S28 family of proteases is comprised of the carboxypeptidase PRCP and the aminopeptidase DPP7.
20540760	9	78	dep	CONCLUSION	1224:1233	arg1	provide					1300:1306	provide	1300:1306	provide the structural basis of PRCP and DPP7 substrate specificity	1300:1366	CONCLUSION The results define the structure of the S28 family of proteases, provide the structural basis of PRCP and DPP7 substrate specificity and enable the rational design of selective PRCP modulators.
20540760	9	78	dep	CONCLUSION	1224:1233	arg1	enable					1372:1377	enable	1372:1377	enable the rational design of selective PRCP modulators	1372:1426	CONCLUSION The results define the structure of the S28 family of proteases, provide the structural basis of PRCP and DPP7 substrate specificity and enable the rational design of selective PRCP modulators.
20540760	9	78	dep	CONCLUSION	1224:1233	arg1	define					1247:1252	define	1247:1252	define the structure of the S28 family of proteases	1247:1297	CONCLUSION The results define the structure of the S28 family of proteases, provide the structural basis of PRCP and DPP7 substrate specificity and enable the rational design of selective PRCP modulators.
20540760	0	79	theme	protease	59:66	arg1	family					68:73	the S28 protease family	51:73	the S28 protease family	51:73	Structural definition and substrate specificity of the S28 protease family: the crystal structure of human prolylcarboxypeptidase.
20540760	9	80	theme	structural	1312:1321	arg1	basis					1323:1327	the structural basis	1308:1327	the structural basis of PRCP and DPP7 substrate specificity	1308:1366	CONCLUSION The results define the structure of the S28 family of proteases, provide the structural basis of PRCP and DPP7 substrate specificity and enable the rational design of selective PRCP modulators.
20540760	1	81	theme	S28	153:155	arg1	family					157:162	The unique S28 family	142:162	The unique S28 family of proteases	142:175	BACKGROUND The unique S28 family of proteases is comprised of the carboxypeptidase PRCP and the aminopeptidase DPP7.
28784760	8	0	theme	disease-causing	1361:1375	arg1	mutations					1377:1385	the disease-causing mutations	1357:1385	the disease-causing mutations	1357:1385	Additionally, this structure allows us to more precisely map all of the disease-causing mutations, allowing future molecular insights into the pathogenesis of NPC disease.
28784760	2	1	theme	lysosomal	328:336	arg1	disease					317:323	Niemann-Pick type C disease	297:323	Niemann-Pick type C disease	297:323	Mutations in these proteins result in Niemann-Pick type C disease, a lysosomal storage disease.
28784760	2	1	theme	lysosomal	328:336	arg1	disease					346:352	a lysosomal storage disease	326:352	a lysosomal storage disease	326:352	Mutations in these proteins result in Niemann-Pick type C disease, a lysosomal storage disease.
28784760	1	2	theme	cholesterol	226:236	arg1	export					204:209	the export	200:209	the export of LDL-derived cholesterol from late endosomes	200:256	Niemann-Pick C1 (NPC1) and NPC2 proteins are indispensable for the export of LDL-derived cholesterol from late endosomes.
28784760	1	3	from	endosomes	248:256	arg1	export					204:209	the export	200:209	the export of LDL-derived cholesterol from late endosomes	200:256	Niemann-Pick C1 (NPC1) and NPC2 proteins are indispensable for the export of LDL-derived cholesterol from late endosomes.
28784760	1	3	from	endosomes	248:256	arg1	cholesterol					226:236	LDL-derived cholesterol	214:236	LDL-derived cholesterol from late endosomes	214:256	Niemann-Pick C1 (NPC1) and NPC2 proteins are indispensable for the export of LDL-derived cholesterol from late endosomes.
28784760	7	4	theme	physiological	1137:1149	arg1	relevance					1151:1159	the physiological relevance	1133:1159	the physiological relevance of the CTD-NTD interaction, which might function to keep the NTD in the proper orientation for receiving cholesterol from NPC2	1133:1286	Our mutagenesis experiments highlight the physiological relevance of the CTD-NTD interaction, which might function to keep the NTD in the proper orientation for receiving cholesterol from NPC2.
28784760	5	5	theme	bonds	827:831	arg1	bonds					827:831	four disulfide bonds	812:831	four disulfide bonds	812:831	Notably, all eight cysteines of the CTD form four disulfide bonds, one of which (C909-C914) enforces a specific loop that in turn mediates an interaction with a loop of the N-terminal domain (NTD).
28784760	5	5	theme	bonds	827:831	arg1	one					834:836	one	834:836	one	834:836	Notably, all eight cysteines of the CTD form four disulfide bonds, one of which (C909-C914) enforces a specific loop that in turn mediates an interaction with a loop of the N-terminal domain (NTD).
28784760	4	6	from	resolution	628:637	arg1	structure					609:617	a crystal structure	599:617	a crystal structure at 3.3 Å resolution of NPC1* (residues 314-1,278)	599:667	Here, we report a crystal structure at 3.3 Å resolution of NPC1* (residues 314-1,278), which-in contrast to previous lower resolution structures-features the entire CTD well resolved.
28784760	7	7	theme	proper	1233:1238	arg1	orientation					1240:1250	the proper orientation	1229:1250	the proper orientation	1229:1250	Our mutagenesis experiments highlight the physiological relevance of the CTD-NTD interaction, which might function to keep the NTD in the proper orientation for receiving cholesterol from NPC2.
28784760	4	8	theme	previous	691:698	arg1	resolution					706:715	previous lower resolution	691:715	previous lower resolution	691:715	Here, we report a crystal structure at 3.3 Å resolution of NPC1* (residues 314-1,278), which-in contrast to previous lower resolution structures-features the entire CTD well resolved.
28784760	1	9	theme	late	243:246	arg1	endosomes					248:256	late endosomes	243:256	late endosomes	243:256	Niemann-Pick C1 (NPC1) and NPC2 proteins are indispensable for the export of LDL-derived cholesterol from late endosomes.
28784760	8	10	theme	molecular	1404:1412	arg1	insights					1414:1421	future molecular insights	1397:1421	future molecular insights into the pathogenesis of NPC disease	1397:1458	Additionally, this structure allows us to more precisely map all of the disease-causing mutations, allowing future molecular insights into the pathogenesis of NPC disease.
28784760	6	11	theme	previous	1046:1053	arg1	structures					1055:1064	any previous structures	1042:1064	any previous structures due to the lower resolution	1042:1092	Importantly, this loop and its interaction with the NTD were not observed in any previous structures due to the lower resolution.
28784760	4	12	theme	NPC1	642:645	arg1	residues					649:656	residues 314-1,278	649:666	residues 314-1,278	649:666	Here, we report a crystal structure at 3.3 Å resolution of NPC1* (residues 314-1,278), which-in contrast to previous lower resolution structures-features the entire CTD well resolved.
28784760	4	12	theme	NPC1	642:645	arg1	*					646:646	NPC1*	642:646	NPC1* (residues 314-1,278)	642:667	Here, we report a crystal structure at 3.3 Å resolution of NPC1* (residues 314-1,278), which-in contrast to previous lower resolution structures-features the entire CTD well resolved.
28784760	7	13	from	NTD	1222:1224	arg1	orientation					1240:1250	the proper orientation	1229:1250	the proper orientation	1229:1250	Our mutagenesis experiments highlight the physiological relevance of the CTD-NTD interaction, which might function to keep the NTD in the proper orientation for receiving cholesterol from NPC2.
28784760	3	14	theme	C-terminal	456:465	arg1	CTD					483:485	CTD	483:485	CTD	483:485	Despite recent reports of the NPC1 structure depicting its overall architecture, the function of its C-terminal luminal domain (CTD) remains poorly understood even though 45% of NPC disease-causing mutations are in this domain.
28784760	3	14	theme	C-terminal	456:465	arg1	domain					475:480	its C-terminal luminal domain	452:480	its C-terminal luminal domain (CTD)	452:486	Despite recent reports of the NPC1 structure depicting its overall architecture, the function of its C-terminal luminal domain (CTD) remains poorly understood even though 45% of NPC disease-causing mutations are in this domain.
28784760	0	15	theme	luminal	96:102	arg1	domain					104:109	the C-terminal luminal domain	81:109	the C-terminal luminal domain	81:109	3.3 Å structure of Niemann-Pick C1 protein reveals insights into the function of the C-terminal luminal domain in cholesterol transport.
28784760	8	16	theme	future	1397:1402	arg1	insights					1414:1421	future molecular insights	1397:1421	future molecular insights into the pathogenesis of NPC disease	1397:1458	Additionally, this structure allows us to more precisely map all of the disease-causing mutations, allowing future molecular insights into the pathogenesis of NPC disease.
28784760	3	17	theme	overall	414:420	arg1	architecture					422:433	its overall architecture	410:433	its overall architecture	410:433	Despite recent reports of the NPC1 structure depicting its overall architecture, the function of its C-terminal luminal domain (CTD) remains poorly understood even though 45% of NPC disease-causing mutations are in this domain.
28784760	0	18	theme	C-terminal	85:94	arg1	domain					104:109	the C-terminal luminal domain	81:109	the C-terminal luminal domain	81:109	3.3 Å structure of Niemann-Pick C1 protein reveals insights into the function of the C-terminal luminal domain in cholesterol transport.
28784760	3	19	theme	NPC1	385:388	arg1	structure					390:398	the NPC1 structure	381:398	the NPC1 structure depicting its overall architecture	381:433	Despite recent reports of the NPC1 structure depicting its overall architecture, the function of its C-terminal luminal domain (CTD) remains poorly understood even though 45% of NPC disease-causing mutations are in this domain.
28784760	4	20	theme	crystal	601:607	arg1	structure					609:617	a crystal structure	599:617	a crystal structure at 3.3 Å resolution of NPC1* (residues 314-1,278)	599:667	Here, we report a crystal structure at 3.3 Å resolution of NPC1* (residues 314-1,278), which-in contrast to previous lower resolution structures-features the entire CTD well resolved.
28784760	0	21	theme	Å	4:4	arg1	structure					6:14	3.3 Å structure	0:14	3.3 Å structure of Niemann-Pick C1 protein	0:41	3.3 Å structure of Niemann-Pick C1 protein reveals insights into the function of the C-terminal luminal domain in cholesterol transport.
28784760	6	22	with	loop	983:986	arg1	NTD					1017:1019	the NTD	1013:1019	the NTD	1013:1019	Importantly, this loop and its interaction with the NTD were not observed in any previous structures due to the lower resolution.
28784760	1	23	link	LDL-derived	214:224	arg1	cholesterol					226:236	LDL-derived cholesterol	214:236	LDL-derived cholesterol from late endosomes	214:256	Niemann-Pick C1 (NPC1) and NPC2 proteins are indispensable for the export of LDL-derived cholesterol from late endosomes.
28784760	2	24	theme	Niemann-Pick	297:308	arg1	disease					317:323	Niemann-Pick type C disease	297:323	Niemann-Pick type C disease	297:323	Mutations in these proteins result in Niemann-Pick type C disease, a lysosomal storage disease.
28784760	2	24	theme	Niemann-Pick	297:308	arg1	disease					346:352	a lysosomal storage disease	326:352	a lysosomal storage disease	326:352	Mutations in these proteins result in Niemann-Pick type C disease, a lysosomal storage disease.
28784760	5	25	theme	CTD	803:805	arg1	cysteines					786:794	all eight cysteines	776:794	all eight cysteines of the CTD	776:805	Notably, all eight cysteines of the CTD form four disulfide bonds, one of which (C909-C914) enforces a specific loop that in turn mediates an interaction with a loop of the N-terminal domain (NTD).
28784760	7	26	theme	CTD-NTD	1168:1174	arg1	interaction					1176:1186	the CTD-NTD interaction	1164:1186	the CTD-NTD interaction	1164:1186	Our mutagenesis experiments highlight the physiological relevance of the CTD-NTD interaction, which might function to keep the NTD in the proper orientation for receiving cholesterol from NPC2.
28784760	3	27	theme	NPC	533:535	arg1	mutations					553:561	NPC disease-causing mutations	533:561	NPC disease-causing mutations	533:561	Despite recent reports of the NPC1 structure depicting its overall architecture, the function of its C-terminal luminal domain (CTD) remains poorly understood even though 45% of NPC disease-causing mutations are in this domain.
28784760	1	28	theme	NPC2	164:167	arg1	proteins					169:176	NPC2 proteins	164:176	NPC2 proteins	164:176	Niemann-Pick C1 (NPC1) and NPC2 proteins are indispensable for the export of LDL-derived cholesterol from late endosomes.
28784760	3	29	theme	mutations	553:561	arg1	%					528:528	45%	526:528	45% of NPC disease-causing mutations	526:561	Despite recent reports of the NPC1 structure depicting its overall architecture, the function of its C-terminal luminal domain (CTD) remains poorly understood even though 45% of NPC disease-causing mutations are in this domain.
28784760	3	29	theme	mutations	553:561	arg1	mutations					553:561	NPC disease-causing mutations	533:561	NPC disease-causing mutations	533:561	Despite recent reports of the NPC1 structure depicting its overall architecture, the function of its C-terminal luminal domain (CTD) remains poorly understood even though 45% of NPC disease-causing mutations are in this domain.
28784760	4	30	dep	residues	649:656	arg1	314-1,278					658:666	314-1,278	658:666	314-1,278	658:666	Here, we report a crystal structure at 3.3 Å resolution of NPC1* (residues 314-1,278), which-in contrast to previous lower resolution structures-features the entire CTD well resolved.
28784760	8	31	theme	NPC	1448:1450	arg1	disease					1452:1458	NPC disease	1448:1458	NPC disease	1448:1458	Additionally, this structure allows us to more precisely map all of the disease-causing mutations, allowing future molecular insights into the pathogenesis of NPC disease.
28784760	0	32	theme	domain	104:109	arg1	function					69:76	the function	65:76	the function of the C-terminal luminal domain in cholesterol transport	65:134	3.3 Å structure of Niemann-Pick C1 protein reveals insights into the function of the C-terminal luminal domain in cholesterol transport.
28784760	0	33	from	function	69:76	arg1	transport					126:134	cholesterol transport	114:134	cholesterol transport	114:134	3.3 Å structure of Niemann-Pick C1 protein reveals insights into the function of the C-terminal luminal domain in cholesterol transport.
28784760	4	34	theme	which-in	670:677	arg1	contrast					679:686	which-in contrast	670:686	which-in contrast to previous lower resolution	670:715	Here, we report a crystal structure at 3.3 Å resolution of NPC1* (residues 314-1,278), which-in contrast to previous lower resolution structures-features the entire CTD well resolved.
28784760	5	35	dep	enforces	859:866	arg1	C909-C914					848:856	C909-C914	848:856	C909-C914	848:856	Notably, all eight cysteines of the CTD form four disulfide bonds, one of which (C909-C914) enforces a specific loop that in turn mediates an interaction with a loop of the N-terminal domain (NTD).
28784760	0	36	theme	C1	32:33	arg1	protein					35:41	Niemann-Pick C1 protein	19:41	Niemann-Pick C1 protein	19:41	3.3 Å structure of Niemann-Pick C1 protein reveals insights into the function of the C-terminal luminal domain in cholesterol transport.
28784760	4	37	theme	*	646:646	arg1	structure					609:617	a crystal structure	599:617	a crystal structure at 3.3 Å resolution of NPC1* (residues 314-1,278)	599:667	Here, we report a crystal structure at 3.3 Å resolution of NPC1* (residues 314-1,278), which-in contrast to previous lower resolution structures-features the entire CTD well resolved.
28784760	4	38	dep	previous	691:698	arg1	lower					700:704	lower	700:704	lower	700:704	Here, we report a crystal structure at 3.3 Å resolution of NPC1* (residues 314-1,278), which-in contrast to previous lower resolution structures-features the entire CTD well resolved.
28784760	4	39	dep	structures-features	717:735	arg1	resolved					757:764	resolved	757:764	structures-features the entire CTD well resolved	717:764	Here, we report a crystal structure at 3.3 Å resolution of NPC1* (residues 314-1,278), which-in contrast to previous lower resolution structures-features the entire CTD well resolved.
28784760	7	40	theme	interaction	1176:1186	arg1	relevance					1151:1159	the physiological relevance	1133:1159	the physiological relevance of the CTD-NTD interaction, which might function to keep the NTD in the proper orientation for receiving cholesterol from NPC2	1133:1286	Our mutagenesis experiments highlight the physiological relevance of the CTD-NTD interaction, which might function to keep the NTD in the proper orientation for receiving cholesterol from NPC2.
28784760	0	41	theme	Niemann-Pick	19:30	arg1	protein					35:41	Niemann-Pick C1 protein	19:41	Niemann-Pick C1 protein	19:41	3.3 Å structure of Niemann-Pick C1 protein reveals insights into the function of the C-terminal luminal domain in cholesterol transport.
28784760	0	42	theme	cholesterol	114:124	arg1	transport					126:134	cholesterol transport	114:134	cholesterol transport	114:134	3.3 Å structure of Niemann-Pick C1 protein reveals insights into the function of the C-terminal luminal domain in cholesterol transport.
28784760	4	43	dep	report	592:597	arg1	structures-features					717:735	structures-features	717:735	structures-features the entire CTD well resolved	717:764	Here, we report a crystal structure at 3.3 Å resolution of NPC1* (residues 314-1,278), which-in contrast to previous lower resolution structures-features the entire CTD well resolved.
28784760	8	44	theme	disease	1452:1458	arg1	pathogenesis					1432:1443	the pathogenesis	1428:1443	the pathogenesis of NPC disease	1428:1458	Additionally, this structure allows us to more precisely map all of the disease-causing mutations, allowing future molecular insights into the pathogenesis of NPC disease.
28784760	7	45	theme	mutagenesis	1099:1109	arg1	experiments					1111:1121	Our mutagenesis experiments	1095:1121	Our mutagenesis experiments	1095:1121	Our mutagenesis experiments highlight the physiological relevance of the CTD-NTD interaction, which might function to keep the NTD in the proper orientation for receiving cholesterol from NPC2.
28784760	3	46	theme	disease-causing	537:551	arg1	mutations					553:561	NPC disease-causing mutations	533:561	NPC disease-causing mutations	533:561	Despite recent reports of the NPC1 structure depicting its overall architecture, the function of its C-terminal luminal domain (CTD) remains poorly understood even though 45% of NPC disease-causing mutations are in this domain.
28784760	3	47	theme	luminal	467:473	arg1	CTD					483:485	CTD	483:485	CTD	483:485	Despite recent reports of the NPC1 structure depicting its overall architecture, the function of its C-terminal luminal domain (CTD) remains poorly understood even though 45% of NPC disease-causing mutations are in this domain.
28784760	3	47	theme	luminal	467:473	arg1	domain					475:480	its C-terminal luminal domain	452:480	its C-terminal luminal domain (CTD)	452:486	Despite recent reports of the NPC1 structure depicting its overall architecture, the function of its C-terminal luminal domain (CTD) remains poorly understood even though 45% of NPC disease-causing mutations are in this domain.
28784760	0	48	theme	protein	35:41	arg1	structure					6:14	3.3 Å structure	0:14	3.3 Å structure of Niemann-Pick C1 protein	0:41	3.3 Å structure of Niemann-Pick C1 protein reveals insights into the function of the C-terminal luminal domain in cholesterol transport.
28784760	6	49	with	interaction	996:1006	arg1	NTD					1017:1019	the NTD	1013:1019	the NTD	1013:1019	Importantly, this loop and its interaction with the NTD were not observed in any previous structures due to the lower resolution.
28784760	1	50	theme	Niemann-Pick	137:148	arg1	NPC1					154:157	NPC1	154:157	NPC1	154:157	Niemann-Pick C1 (NPC1) and NPC2 proteins are indispensable for the export of LDL-derived cholesterol from late endosomes.
28784760	1	50	theme	Niemann-Pick	137:148	arg1	C1					150:151	Niemann-Pick C1	137:151	Niemann-Pick C1 (NPC1)	137:158	Niemann-Pick C1 (NPC1) and NPC2 proteins are indispensable for the export of LDL-derived cholesterol from late endosomes.
28784760	3	51	theme	domain	475:480	arg1	function					440:447	the function	436:447	the function of its C-terminal luminal domain (CTD)	436:486	Despite recent reports of the NPC1 structure depicting its overall architecture, the function of its C-terminal luminal domain (CTD) remains poorly understood even though 45% of NPC disease-causing mutations are in this domain.
28784760	2	52	from	Mutations	259:267	arg1	proteins					278:285	these proteins	272:285	these proteins	272:285	Mutations in these proteins result in Niemann-Pick type C disease, a lysosomal storage disease.
28784760	6	53	theme	due	1066:1068	arg1	structures					1055:1064	any previous structures	1042:1064	any previous structures due to the lower resolution	1042:1092	Importantly, this loop and its interaction with the NTD were not observed in any previous structures due to the lower resolution.
28784760	5	54	theme	N-terminal	940:949	arg1	domain					951:956	the N-terminal domain	936:956	the N-terminal domain (NTD)	936:962	Notably, all eight cysteines of the CTD form four disulfide bonds, one of which (C909-C914) enforces a specific loop that in turn mediates an interaction with a loop of the N-terminal domain (NTD).
28784760	5	54	theme	N-terminal	940:949	arg1	NTD					959:961	NTD	959:961	NTD	959:961	Notably, all eight cysteines of the CTD form four disulfide bonds, one of which (C909-C914) enforces a specific loop that in turn mediates an interaction with a loop of the N-terminal domain (NTD).
28784760	6	55	theme	lower	1077:1081	arg1	resolution					1083:1092	the lower resolution	1073:1092	the lower resolution	1073:1092	Importantly, this loop and its interaction with the NTD were not observed in any previous structures due to the lower resolution.
28784760	4	56	theme	Å	626:626	arg1	resolution					628:637	3.3 Å resolution	622:637	3.3 Å resolution	622:637	Here, we report a crystal structure at 3.3 Å resolution of NPC1* (residues 314-1,278), which-in contrast to previous lower resolution structures-features the entire CTD well resolved.
28784760	2	57	theme	C	315:315	arg1	disease					317:323	Niemann-Pick type C disease	297:323	Niemann-Pick type C disease	297:323	Mutations in these proteins result in Niemann-Pick type C disease, a lysosomal storage disease.
28784760	2	57	theme	C	315:315	arg1	disease					346:352	a lysosomal storage disease	326:352	a lysosomal storage disease	326:352	Mutations in these proteins result in Niemann-Pick type C disease, a lysosomal storage disease.
28784760	7	58	from	NPC2	1283:1286	arg1	cholesterol					1266:1276	cholesterol	1266:1276	cholesterol from NPC2	1266:1286	Our mutagenesis experiments highlight the physiological relevance of the CTD-NTD interaction, which might function to keep the NTD in the proper orientation for receiving cholesterol from NPC2.
28784760	1	59	from	export	204:209	arg1	endosomes					248:256	late endosomes	243:256	late endosomes	243:256	Niemann-Pick C1 (NPC1) and NPC2 proteins are indispensable for the export of LDL-derived cholesterol from late endosomes.
28784760	5	60	theme	domain	951:956	arg1	loop					928:931	a loop	926:931	a loop of the N-terminal domain (NTD)	926:962	Notably, all eight cysteines of the CTD form four disulfide bonds, one of which (C909-C914) enforces a specific loop that in turn mediates an interaction with a loop of the N-terminal domain (NTD).
28784760	5	61	theme	specific	870:877	arg1	loop					879:882	a specific loop	868:882	a specific loop that in turn mediates an interaction with a loop of the N-terminal domain (NTD)	868:962	Notably, all eight cysteines of the CTD form four disulfide bonds, one of which (C909-C914) enforces a specific loop that in turn mediates an interaction with a loop of the N-terminal domain (NTD).
28784760	2	62	theme	type	310:313	arg1	disease					317:323	Niemann-Pick type C disease	297:323	Niemann-Pick type C disease	297:323	Mutations in these proteins result in Niemann-Pick type C disease, a lysosomal storage disease.
28784760	2	62	theme	type	310:313	arg1	disease					346:352	a lysosomal storage disease	326:352	a lysosomal storage disease	326:352	Mutations in these proteins result in Niemann-Pick type C disease, a lysosomal storage disease.
28784760	6	63	located	observed	1030:1037	arg2	interaction					996:1006	its interaction	992:1006	its interaction with the NTD	992:1019	Importantly, this loop and its interaction with the NTD were not observed in any previous structures due to the lower resolution.
28784760	6	63	located	observed	1030:1037	arg2	loop					983:986	this loop	978:986	this loop	978:986	Importantly, this loop and its interaction with the NTD were not observed in any previous structures due to the lower resolution.
28784760	6	63	located	observed	1030:1037	arg1	structures					1055:1064	any previous structures	1042:1064	any previous structures due to the lower resolution	1042:1092	Importantly, this loop and its interaction with the NTD were not observed in any previous structures due to the lower resolution.
28784760	5	64	theme	disulfide	817:825	arg1	bonds					827:831	four disulfide bonds	812:831	four disulfide bonds	812:831	Notably, all eight cysteines of the CTD form four disulfide bonds, one of which (C909-C914) enforces a specific loop that in turn mediates an interaction with a loop of the N-terminal domain (NTD).
28784760	3	65	theme	recent	363:368	arg1	reports					370:376	recent reports	363:376	recent reports of the NPC1 structure depicting its overall architecture	363:433	Despite recent reports of the NPC1 structure depicting its overall architecture, the function of its C-terminal luminal domain (CTD) remains poorly understood even though 45% of NPC disease-causing mutations are in this domain.
28784760	5	66	with	interaction	909:919	arg1	loop					928:931	a loop	926:931	a loop of the N-terminal domain (NTD)	926:962	Notably, all eight cysteines of the CTD form four disulfide bonds, one of which (C909-C914) enforces a specific loop that in turn mediates an interaction with a loop of the N-terminal domain (NTD).
28784760	3	67	theme	structure	390:398	arg1	reports					370:376	recent reports	363:376	recent reports of the NPC1 structure depicting its overall architecture	363:433	Despite recent reports of the NPC1 structure depicting its overall architecture, the function of its C-terminal luminal domain (CTD) remains poorly understood even though 45% of NPC disease-causing mutations are in this domain.
28784760	4	68	theme	entire	741:746	arg1	CTD					748:750	the entire CTD	737:750	the entire CTD	737:750	Here, we report a crystal structure at 3.3 Å resolution of NPC1* (residues 314-1,278), which-in contrast to previous lower resolution structures-features the entire CTD well resolved.
28784760	2	69	theme	storage	338:344	arg1	disease					317:323	Niemann-Pick type C disease	297:323	Niemann-Pick type C disease	297:323	Mutations in these proteins result in Niemann-Pick type C disease, a lysosomal storage disease.
28784760	2	69	theme	storage	338:344	arg1	disease					346:352	a lysosomal storage disease	326:352	a lysosomal storage disease	326:352	Mutations in these proteins result in Niemann-Pick type C disease, a lysosomal storage disease.
28784760	1	70	theme	LDL-derived	214:224	arg1	cholesterol					226:236	LDL-derived cholesterol	214:236	LDL-derived cholesterol from late endosomes	214:256	Niemann-Pick C1 (NPC1) and NPC2 proteins are indispensable for the export of LDL-derived cholesterol from late endosomes.
34298689	0	0	theme	Carcinoma	111:119	arg1	Phenotypes					131:140	Hepatocellular Carcinoma Malignant Phenotypes	96:140	Hepatocellular Carcinoma Malignant Phenotypes	96:140	RANBP2 Activates O-GlcNAcylation through Inducing CEBPα-Dependent OGA Downregulation to Promote Hepatocellular Carcinoma Malignant Phenotypes.
34298689	7	1	theme	genes	1529:1533	arg1	hyper-O-GlcNAcylation					1504:1524	the hyper-O-GlcNAcylation	1500:1524	the hyper-O-GlcNAcylation of genes, such as PGC1α	1500:1548	Altogether, our results show a novel molecular mechanism whereby RANBP2 regulates its function through CEBPα-dependent OGA downregulation to induce a global change in the hyper-O-GlcNAcylation of genes, such as PGC1α, encouraging the further study of promising implications for HCC therapy.
34298689	2	2	theme	underlying	388:397	arg1	mechanisms					399:408	the underlying mechanisms	384:408	the underlying mechanisms of the OGT/OGA imbalance responsible for HCC tumorigenesis	384:467	Aberrant hyper-O-GlcNAcylation is reported to yield hepatocellular carcinoma (HCC) malignancy, but the underlying mechanisms of the OGT/OGA imbalance responsible for HCC tumorigenesis remain largely unknown.
34298689	0	3	theme	Hepatocellular	96:109	arg1	Carcinoma					111:119	Hepatocellular Carcinoma	96:119	Hepatocellular Carcinoma Malignant Phenotypes	96:140	RANBP2 Activates O-GlcNAcylation through Inducing CEBPα-Dependent OGA Downregulation to Promote Hepatocellular Carcinoma Malignant Phenotypes.
34298689	5	4	theme	O-GlcNAc	926:933	arg1	level					935:939	the O-GlcNAc level	922:939	the O-GlcNAc level	922:939	As a transcriptional factor, CEBPα was verified to augment OGA transcription, and further experiments demonstrated that RANBP2 enhanced the O-GlcNAc level by downregulating OGA transcription while not affecting OGT expression.
34298689	6	5	theme	gamma	1270:1274	arg1	alpha					1290:1294	peroxisome proliferative-activated receptor gamma coactivator 1 alpha	1226:1294	peroxisome proliferative-activated receptor gamma coactivator 1 alpha (PGC1α)	1226:1302	Importantly, we provided in vitro and in vivo evidence of HCC malignant phenotypes that RANBP2 triggered through an imbalance of OGT/OGA and subsequent higher O-GlcNAcylation events for oncogenic proteins such as peroxisome proliferative-activated receptor gamma coactivator 1 alpha (PGC1α) in a CEBPα-dependent manner.
34298689	6	5	theme	gamma	1270:1274	arg1	PGC1α					1297:1301	PGC1α	1297:1301	PGC1α	1297:1301	Importantly, we provided in vitro and in vivo evidence of HCC malignant phenotypes that RANBP2 triggered through an imbalance of OGT/OGA and subsequent higher O-GlcNAcylation events for oncogenic proteins such as peroxisome proliferative-activated receptor gamma coactivator 1 alpha (PGC1α) in a CEBPα-dependent manner.
34298689	3	6	theme	small	557:561	arg1	SUMO					588:591	SUMO	588:591	SUMO	588:591	Here, we report that RAN-binding protein 2 (RANBP2), one of the small ubiquitin-like modifier (SUMO) E3 ligases, contributed to malignant phenotypes in HCC.
34298689	3	6	theme	small	557:561	arg1	modifier					578:585	small ubiquitin-like modifier	557:585	the small ubiquitin-like modifier (SUMO) E3 ligases	553:603	Here, we report that RAN-binding protein 2 (RANBP2), one of the small ubiquitin-like modifier (SUMO) E3 ligases, contributed to malignant phenotypes in HCC.
34298689	6	7	theme	O-GlcNAcylation	1172:1186	arg1	events					1188:1193	subsequent higher O-GlcNAcylation events	1154:1193	subsequent higher O-GlcNAcylation events for oncogenic proteins such as peroxisome proliferative-activated receptor gamma coactivator 1 alpha (PGC1α)	1154:1302	Importantly, we provided in vitro and in vivo evidence of HCC malignant phenotypes that RANBP2 triggered through an imbalance of OGT/OGA and subsequent higher O-GlcNAcylation events for oncogenic proteins such as peroxisome proliferative-activated receptor gamma coactivator 1 alpha (PGC1α) in a CEBPα-dependent manner.
34298689	0	8	theme	Malignant	121:129	arg1	Phenotypes					131:140	Hepatocellular Carcinoma Malignant Phenotypes	96:140	Hepatocellular Carcinoma Malignant Phenotypes	96:140	RANBP2 Activates O-GlcNAcylation through Inducing CEBPα-Dependent OGA Downregulation to Promote Hepatocellular Carcinoma Malignant Phenotypes.
34298689	6	9	dep	evidence	1059:1066	arg1	triggered					1108:1116	triggered	1108:1116	triggered through an imbalance of OGT/OGA and subsequent higher O-GlcNAcylation events for oncogenic proteins such as peroxisome proliferative-activated receptor gamma coactivator 1 alpha (PGC1α) in a CEBPα-dependent manner	1108:1330	Importantly, we provided in vitro and in vivo evidence of HCC malignant phenotypes that RANBP2 triggered through an imbalance of OGT/OGA and subsequent higher O-GlcNAcylation events for oncogenic proteins such as peroxisome proliferative-activated receptor gamma coactivator 1 alpha (PGC1α) in a CEBPα-dependent manner.
34298689	3	10	theme	ubiquitin-like	563:576	arg1	SUMO					588:591	SUMO	588:591	SUMO	588:591	Here, we report that RAN-binding protein 2 (RANBP2), one of the small ubiquitin-like modifier (SUMO) E3 ligases, contributed to malignant phenotypes in HCC.
34298689	3	10	theme	ubiquitin-like	563:576	arg1	modifier					578:585	small ubiquitin-like modifier	557:585	the small ubiquitin-like modifier (SUMO) E3 ligases	553:603	Here, we report that RAN-binding protein 2 (RANBP2), one of the small ubiquitin-like modifier (SUMO) E3 ligases, contributed to malignant phenotypes in HCC.
34298689	5	11	theme	OGA	959:961	arg1	transcription					963:975	OGA transcription	959:975	OGA transcription	959:975	As a transcriptional factor, CEBPα was verified to augment OGA transcription, and further experiments demonstrated that RANBP2 enhanced the O-GlcNAc level by downregulating OGA transcription while not affecting OGT expression.
34298689	6	12	theme	CEBPα-dependent	1309:1323	arg1	manner					1325:1330	a CEBPα-dependent manner	1307:1330	a CEBPα-dependent manner	1307:1330	Importantly, we provided in vitro and in vivo evidence of HCC malignant phenotypes that RANBP2 triggered through an imbalance of OGT/OGA and subsequent higher O-GlcNAcylation events for oncogenic proteins such as peroxisome proliferative-activated receptor gamma coactivator 1 alpha (PGC1α) in a CEBPα-dependent manner.
34298689	4	13	theme	CCAAT/enhancer-binding	681:702	arg1	CEBPα					719:723	CEBPα	719:723	CEBPα	719:723	RANBP2 was found to facilitate CCAAT/enhancer-binding protein alpha (CEBPα) SUMOylation and degradation by direct interplay with CEBPα.
34298689	4	13	theme	CCAAT/enhancer-binding	681:702	arg1	alpha					712:716	CCAAT/enhancer-binding protein alpha	681:716	CCAAT/enhancer-binding protein alpha (CEBPα) SUMOylation	681:736	RANBP2 was found to facilitate CCAAT/enhancer-binding protein alpha (CEBPα) SUMOylation and degradation by direct interplay with CEBPα.
34298689	2	14	theme	responsible	435:445	arg1	imbalance					425:433	the OGT/OGA imbalance	413:433	the OGT/OGA imbalance responsible for HCC tumorigenesis	413:467	Aberrant hyper-O-GlcNAcylation is reported to yield hepatocellular carcinoma (HCC) malignancy, but the underlying mechanisms of the OGT/OGA imbalance responsible for HCC tumorigenesis remain largely unknown.
34298689	5	15	theme	transcriptional	791:805	arg1	CEBPα					815:819	CEBPα	815:819	CEBPα	815:819	As a transcriptional factor, CEBPα was verified to augment OGA transcription, and further experiments demonstrated that RANBP2 enhanced the O-GlcNAc level by downregulating OGA transcription while not affecting OGT expression.
34298689	5	15	theme	transcriptional	791:805	arg1	factor					807:812	a transcriptional factor	789:812	a transcriptional factor	789:812	As a transcriptional factor, CEBPα was verified to augment OGA transcription, and further experiments demonstrated that RANBP2 enhanced the O-GlcNAc level by downregulating OGA transcription while not affecting OGT expression.
34298689	6	16	theme	events	1188:1193	arg1	imbalance					1129:1137	an imbalance	1126:1137	an imbalance of OGT/OGA and subsequent higher O-GlcNAcylation events for oncogenic proteins such as peroxisome proliferative-activated receptor gamma coactivator 1 alpha (PGC1α)	1126:1302	Importantly, we provided in vitro and in vivo evidence of HCC malignant phenotypes that RANBP2 triggered through an imbalance of OGT/OGA and subsequent higher O-GlcNAcylation events for oncogenic proteins such as peroxisome proliferative-activated receptor gamma coactivator 1 alpha (PGC1α) in a CEBPα-dependent manner.
34298689	3	17	from	phenotypes	631:640	arg1	HCC					645:647	HCC	645:647	HCC	645:647	Here, we report that RAN-binding protein 2 (RANBP2), one of the small ubiquitin-like modifier (SUMO) E3 ligases, contributed to malignant phenotypes in HCC.
34298689	2	18	theme	imbalance	425:433	arg1	mechanisms					399:408	the underlying mechanisms	384:408	the underlying mechanisms of the OGT/OGA imbalance responsible for HCC tumorigenesis	384:467	Aberrant hyper-O-GlcNAcylation is reported to yield hepatocellular carcinoma (HCC) malignancy, but the underlying mechanisms of the OGT/OGA imbalance responsible for HCC tumorigenesis remain largely unknown.
34298689	6	19	theme	oncogenic	1199:1207	arg1	alpha					1290:1294	peroxisome proliferative-activated receptor gamma coactivator 1 alpha	1226:1294	peroxisome proliferative-activated receptor gamma coactivator 1 alpha (PGC1α)	1226:1302	Importantly, we provided in vitro and in vivo evidence of HCC malignant phenotypes that RANBP2 triggered through an imbalance of OGT/OGA and subsequent higher O-GlcNAcylation events for oncogenic proteins such as peroxisome proliferative-activated receptor gamma coactivator 1 alpha (PGC1α) in a CEBPα-dependent manner.
34298689	6	19	theme	oncogenic	1199:1207	arg1	proteins					1209:1216	oncogenic proteins	1199:1216	oncogenic proteins such as peroxisome proliferative-activated receptor gamma coactivator 1 alpha (PGC1α)	1199:1302	Importantly, we provided in vitro and in vivo evidence of HCC malignant phenotypes that RANBP2 triggered through an imbalance of OGT/OGA and subsequent higher O-GlcNAcylation events for oncogenic proteins such as peroxisome proliferative-activated receptor gamma coactivator 1 alpha (PGC1α) in a CEBPα-dependent manner.
34298689	4	20	theme	direct	757:762	arg1	interplay					764:772	direct interplay	757:772	direct interplay with CEBPα	757:783	RANBP2 was found to facilitate CCAAT/enhancer-binding protein alpha (CEBPα) SUMOylation and degradation by direct interplay with CEBPα.
34298689	6	21	dep	subsequent	1154:1163	arg1	higher					1165:1170	higher	1165:1170	higher	1165:1170	Importantly, we provided in vitro and in vivo evidence of HCC malignant phenotypes that RANBP2 triggered through an imbalance of OGT/OGA and subsequent higher O-GlcNAcylation events for oncogenic proteins such as peroxisome proliferative-activated receptor gamma coactivator 1 alpha (PGC1α) in a CEBPα-dependent manner.
34298689	2	22	theme	OGT/OGA	417:423	arg1	imbalance					425:433	the OGT/OGA imbalance	413:433	the OGT/OGA imbalance responsible for HCC tumorigenesis	413:467	Aberrant hyper-O-GlcNAcylation is reported to yield hepatocellular carcinoma (HCC) malignancy, but the underlying mechanisms of the OGT/OGA imbalance responsible for HCC tumorigenesis remain largely unknown.
34298689	7	23	theme	global	1483:1488	arg1	change					1490:1495	a global change	1481:1495	a global change	1481:1495	Altogether, our results show a novel molecular mechanism whereby RANBP2 regulates its function through CEBPα-dependent OGA downregulation to induce a global change in the hyper-O-GlcNAcylation of genes, such as PGC1α, encouraging the further study of promising implications for HCC therapy.
34298689	1	24	theme	O-GlcNAc	235:242	arg1	OGT					257:259	OGT	257:259	OGT	257:259	O-GlcNAcylation is an important post-translational modification (PTM) jointly controlled by O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA).
34298689	1	24	theme	O-GlcNAc	235:242	arg1	transferase					244:254	O-GlcNAc transferase	235:254	O-GlcNAc transferase (OGT)	235:260	O-GlcNAcylation is an important post-translational modification (PTM) jointly controlled by O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA).
34298689	7	25	theme	CEBPα-dependent	1436:1450	arg1	downregulation					1456:1469	CEBPα-dependent OGA downregulation	1436:1469	CEBPα-dependent OGA downregulation	1436:1469	Altogether, our results show a novel molecular mechanism whereby RANBP2 regulates its function through CEBPα-dependent OGA downregulation to induce a global change in the hyper-O-GlcNAcylation of genes, such as PGC1α, encouraging the further study of promising implications for HCC therapy.
34298689	2	26	theme	carcinoma	352:360	arg1	malignancy					368:377	hepatocellular carcinoma (HCC) malignancy	337:377	hepatocellular carcinoma (HCC) malignancy	337:377	Aberrant hyper-O-GlcNAcylation is reported to yield hepatocellular carcinoma (HCC) malignancy, but the underlying mechanisms of the OGT/OGA imbalance responsible for HCC tumorigenesis remain largely unknown.
34298689	5	27	theme	OGA	845:847	arg1	transcription					849:861	OGA transcription	845:861	OGA transcription	845:861	As a transcriptional factor, CEBPα was verified to augment OGA transcription, and further experiments demonstrated that RANBP2 enhanced the O-GlcNAc level by downregulating OGA transcription while not affecting OGT expression.
34298689	6	28	theme	OGT/OGA	1142:1148	arg1	imbalance					1129:1137	an imbalance	1126:1137	an imbalance of OGT/OGA and subsequent higher O-GlcNAcylation events for oncogenic proteins such as peroxisome proliferative-activated receptor gamma coactivator 1 alpha (PGC1α)	1126:1302	Importantly, we provided in vitro and in vivo evidence of HCC malignant phenotypes that RANBP2 triggered through an imbalance of OGT/OGA and subsequent higher O-GlcNAcylation events for oncogenic proteins such as peroxisome proliferative-activated receptor gamma coactivator 1 alpha (PGC1α) in a CEBPα-dependent manner.
34298689	6	29	theme	peroxisome	1226:1235	arg1	gamma					1270:1274	peroxisome proliferative-activated receptor gamma	1226:1274	peroxisome proliferative-activated receptor gamma coactivator 1 alpha (PGC1α)	1226:1302	Importantly, we provided in vitro and in vivo evidence of HCC malignant phenotypes that RANBP2 triggered through an imbalance of OGT/OGA and subsequent higher O-GlcNAcylation events for oncogenic proteins such as peroxisome proliferative-activated receptor gamma coactivator 1 alpha (PGC1α) in a CEBPα-dependent manner.
34298689	2	30	theme	hepatocellular	337:350	arg1	carcinoma					352:360	hepatocellular carcinoma	337:360	hepatocellular carcinoma (HCC) malignancy	337:377	Aberrant hyper-O-GlcNAcylation is reported to yield hepatocellular carcinoma (HCC) malignancy, but the underlying mechanisms of the OGT/OGA imbalance responsible for HCC tumorigenesis remain largely unknown.
34298689	2	30	theme	hepatocellular	337:350	arg1	HCC					363:365	HCC	363:365	HCC	363:365	Aberrant hyper-O-GlcNAcylation is reported to yield hepatocellular carcinoma (HCC) malignancy, but the underlying mechanisms of the OGT/OGA imbalance responsible for HCC tumorigenesis remain largely unknown.
34298689	6	31	theme	HCC	1071:1073	arg1	phenotypes					1085:1094	HCC malignant phenotypes	1071:1094	HCC malignant phenotypes	1071:1094	Importantly, we provided in vitro and in vivo evidence of HCC malignant phenotypes that RANBP2 triggered through an imbalance of OGT/OGA and subsequent higher O-GlcNAcylation events for oncogenic proteins such as peroxisome proliferative-activated receptor gamma coactivator 1 alpha (PGC1α) in a CEBPα-dependent manner.
34298689	0	32	theme	CEBPα-Dependent	50:64	arg1	Downregulation					70:83	CEBPα-Dependent OGA Downregulation	50:83	CEBPα-Dependent OGA Downregulation	50:83	RANBP2 Activates O-GlcNAcylation through Inducing CEBPα-Dependent OGA Downregulation to Promote Hepatocellular Carcinoma Malignant Phenotypes.
34298689	5	33	theme	OGT	997:999	arg1	expression					1001:1010	OGT expression	997:1010	OGT expression	997:1010	As a transcriptional factor, CEBPα was verified to augment OGA transcription, and further experiments demonstrated that RANBP2 enhanced the O-GlcNAc level by downregulating OGA transcription while not affecting OGT expression.
34298689	7	34	theme	HCC	1611:1613	arg1	therapy					1615:1621	HCC therapy	1611:1621	HCC therapy	1611:1621	Altogether, our results show a novel molecular mechanism whereby RANBP2 regulates its function through CEBPα-dependent OGA downregulation to induce a global change in the hyper-O-GlcNAcylation of genes, such as PGC1α, encouraging the further study of promising implications for HCC therapy.
34298689	7	35	theme	OGA	1452:1454	arg1	downregulation					1456:1469	CEBPα-dependent OGA downregulation	1436:1469	CEBPα-dependent OGA downregulation	1436:1469	Altogether, our results show a novel molecular mechanism whereby RANBP2 regulates its function through CEBPα-dependent OGA downregulation to induce a global change in the hyper-O-GlcNAcylation of genes, such as PGC1α, encouraging the further study of promising implications for HCC therapy.
34298689	6	36	theme	phenotypes	1085:1094	arg1	evidence					1059:1066	evidence	1059:1066	evidence of HCC malignant phenotypes that RANBP2 triggered through an imbalance of OGT/OGA and subsequent higher O-GlcNAcylation events for oncogenic proteins such as peroxisome proliferative-activated receptor gamma coactivator 1 alpha (PGC1α) in a CEBPα-dependent manner	1059:1330	Importantly, we provided in vitro and in vivo evidence of HCC malignant phenotypes that RANBP2 triggered through an imbalance of OGT/OGA and subsequent higher O-GlcNAcylation events for oncogenic proteins such as peroxisome proliferative-activated receptor gamma coactivator 1 alpha (PGC1α) in a CEBPα-dependent manner.
34298689	2	37	theme	HCC	451:453	arg1	tumorigenesis					455:467	HCC tumorigenesis	451:467	HCC tumorigenesis	451:467	Aberrant hyper-O-GlcNAcylation is reported to yield hepatocellular carcinoma (HCC) malignancy, but the underlying mechanisms of the OGT/OGA imbalance responsible for HCC tumorigenesis remain largely unknown.
34298689	5	38	theme	further	868:874	arg1	experiments					876:886	further experiments	868:886	further experiments	868:886	As a transcriptional factor, CEBPα was verified to augment OGA transcription, and further experiments demonstrated that RANBP2 enhanced the O-GlcNAc level by downregulating OGA transcription while not affecting OGT expression.
34298689	7	39	theme	promising	1584:1592	arg1	implications					1594:1605	promising implications	1584:1605	promising implications for HCC therapy	1584:1621	Altogether, our results show a novel molecular mechanism whereby RANBP2 regulates its function through CEBPα-dependent OGA downregulation to induce a global change in the hyper-O-GlcNAcylation of genes, such as PGC1α, encouraging the further study of promising implications for HCC therapy.
34298689	4	40	with	interplay	764:772	arg1	CEBPα					779:783	CEBPα	779:783	CEBPα	779:783	RANBP2 was found to facilitate CCAAT/enhancer-binding protein alpha (CEBPα) SUMOylation and degradation by direct interplay with CEBPα.
34298689	7	41	theme	implications	1594:1605	arg1	study					1575:1579	the further study	1563:1579	the further study of promising implications for HCC therapy	1563:1621	Altogether, our results show a novel molecular mechanism whereby RANBP2 regulates its function through CEBPα-dependent OGA downregulation to induce a global change in the hyper-O-GlcNAcylation of genes, such as PGC1α, encouraging the further study of promising implications for HCC therapy.
34298689	3	42	theme	E3	594:595	arg1	ligases					597:603	the small ubiquitin-like modifier (SUMO) E3 ligases	553:603	the small ubiquitin-like modifier (SUMO) E3 ligases	553:603	Here, we report that RAN-binding protein 2 (RANBP2), one of the small ubiquitin-like modifier (SUMO) E3 ligases, contributed to malignant phenotypes in HCC.
34298689	0	43	theme	OGA	66:68	arg1	Downregulation					70:83	CEBPα-Dependent OGA Downregulation	50:83	CEBPα-Dependent OGA Downregulation	50:83	RANBP2 Activates O-GlcNAcylation through Inducing CEBPα-Dependent OGA Downregulation to Promote Hepatocellular Carcinoma Malignant Phenotypes.
34298689	7	44	theme	molecular	1370:1378	arg1	mechanism					1380:1388	a novel molecular mechanism	1362:1388	a novel molecular mechanism whereby RANBP2 regulates its function through CEBPα-dependent OGA downregulation to induce a global change in the hyper-O-GlcNAcylation of genes, such as PGC1α, encouraging the further study of promising implications for HCC therapy	1362:1621	Altogether, our results show a novel molecular mechanism whereby RANBP2 regulates its function through CEBPα-dependent OGA downregulation to induce a global change in the hyper-O-GlcNAcylation of genes, such as PGC1α, encouraging the further study of promising implications for HCC therapy.
34298689	3	45	theme	ligases	597:603	arg1	protein					526:532	RAN-binding protein 2	514:534	RAN-binding protein 2 (RANBP2)	514:543	Here, we report that RAN-binding protein 2 (RANBP2), one of the small ubiquitin-like modifier (SUMO) E3 ligases, contributed to malignant phenotypes in HCC.
34298689	3	45	theme	ligases	597:603	arg1	ligases					597:603	the small ubiquitin-like modifier (SUMO) E3 ligases	553:603	the small ubiquitin-like modifier (SUMO) E3 ligases	553:603	Here, we report that RAN-binding protein 2 (RANBP2), one of the small ubiquitin-like modifier (SUMO) E3 ligases, contributed to malignant phenotypes in HCC.
34298689	3	45	theme	ligases	597:603	arg1	one					546:548	one	546:548	one	546:548	Here, we report that RAN-binding protein 2 (RANBP2), one of the small ubiquitin-like modifier (SUMO) E3 ligases, contributed to malignant phenotypes in HCC.
34298689	6	46	theme	subsequent	1154:1163	arg1	events					1188:1193	subsequent higher O-GlcNAcylation events	1154:1193	subsequent higher O-GlcNAcylation events for oncogenic proteins such as peroxisome proliferative-activated receptor gamma coactivator 1 alpha (PGC1α)	1154:1302	Importantly, we provided in vitro and in vivo evidence of HCC malignant phenotypes that RANBP2 triggered through an imbalance of OGT/OGA and subsequent higher O-GlcNAcylation events for oncogenic proteins such as peroxisome proliferative-activated receptor gamma coactivator 1 alpha (PGC1α) in a CEBPα-dependent manner.
34298689	6	47	theme	proliferative-activated	1237:1259	arg1	gamma					1270:1274	peroxisome proliferative-activated receptor gamma	1226:1274	peroxisome proliferative-activated receptor gamma coactivator 1 alpha (PGC1α)	1226:1302	Importantly, we provided in vitro and in vivo evidence of HCC malignant phenotypes that RANBP2 triggered through an imbalance of OGT/OGA and subsequent higher O-GlcNAcylation events for oncogenic proteins such as peroxisome proliferative-activated receptor gamma coactivator 1 alpha (PGC1α) in a CEBPα-dependent manner.
34298689	6	48	theme	coactivator	1276:1286	arg1	alpha					1290:1294	peroxisome proliferative-activated receptor gamma coactivator 1 alpha	1226:1294	peroxisome proliferative-activated receptor gamma coactivator 1 alpha (PGC1α)	1226:1302	Importantly, we provided in vitro and in vivo evidence of HCC malignant phenotypes that RANBP2 triggered through an imbalance of OGT/OGA and subsequent higher O-GlcNAcylation events for oncogenic proteins such as peroxisome proliferative-activated receptor gamma coactivator 1 alpha (PGC1α) in a CEBPα-dependent manner.
34298689	6	48	theme	coactivator	1276:1286	arg1	PGC1α					1297:1301	PGC1α	1297:1301	PGC1α	1297:1301	Importantly, we provided in vitro and in vivo evidence of HCC malignant phenotypes that RANBP2 triggered through an imbalance of OGT/OGA and subsequent higher O-GlcNAcylation events for oncogenic proteins such as peroxisome proliferative-activated receptor gamma coactivator 1 alpha (PGC1α) in a CEBPα-dependent manner.
34298689	1	49	theme	important	165:173	arg1	PTM					208:210	PTM	208:210	PTM	208:210	O-GlcNAcylation is an important post-translational modification (PTM) jointly controlled by O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA).
34298689	1	49	theme	important	165:173	arg1	modification					194:205	an important post-translational modification	162:205	an important post-translational modification (PTM) jointly controlled by O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA)	162:282	O-GlcNAcylation is an important post-translational modification (PTM) jointly controlled by O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA).
34298689	1	49	theme	important	165:173	arg1	O-GlcNAcylation					143:157	O-GlcNAcylation	143:157	O-GlcNAcylation	143:157	O-GlcNAcylation is an important post-translational modification (PTM) jointly controlled by O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA).
34298689	3	50	theme	modifier	578:585	arg1	ligases					597:603	the small ubiquitin-like modifier (SUMO) E3 ligases	553:603	the small ubiquitin-like modifier (SUMO) E3 ligases	553:603	Here, we report that RAN-binding protein 2 (RANBP2), one of the small ubiquitin-like modifier (SUMO) E3 ligases, contributed to malignant phenotypes in HCC.
34298689	2	51	theme	Aberrant	285:292	arg1	hyper-O-GlcNAcylation					294:314	Aberrant hyper-O-GlcNAcylation	285:314	Aberrant hyper-O-GlcNAcylation	285:314	Aberrant hyper-O-GlcNAcylation is reported to yield hepatocellular carcinoma (HCC) malignancy, but the underlying mechanisms of the OGT/OGA imbalance responsible for HCC tumorigenesis remain largely unknown.
34298689	1	52	theme	post-translational	175:192	arg1	PTM					208:210	PTM	208:210	PTM	208:210	O-GlcNAcylation is an important post-translational modification (PTM) jointly controlled by O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA).
34298689	1	52	theme	post-translational	175:192	arg1	modification					194:205	an important post-translational modification	162:205	an important post-translational modification (PTM) jointly controlled by O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA)	162:282	O-GlcNAcylation is an important post-translational modification (PTM) jointly controlled by O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA).
34298689	1	52	theme	post-translational	175:192	arg1	O-GlcNAcylation					143:157	O-GlcNAcylation	143:157	O-GlcNAcylation	143:157	O-GlcNAcylation is an important post-translational modification (PTM) jointly controlled by O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA).
34298689	7	53	theme	novel	1364:1368	arg1	mechanism					1380:1388	a novel molecular mechanism	1362:1388	a novel molecular mechanism whereby RANBP2 regulates its function through CEBPα-dependent OGA downregulation to induce a global change in the hyper-O-GlcNAcylation of genes, such as PGC1α, encouraging the further study of promising implications for HCC therapy	1362:1621	Altogether, our results show a novel molecular mechanism whereby RANBP2 regulates its function through CEBPα-dependent OGA downregulation to induce a global change in the hyper-O-GlcNAcylation of genes, such as PGC1α, encouraging the further study of promising implications for HCC therapy.
34298689	3	54	theme	RAN-binding	514:524	arg1	ligases					597:603	the small ubiquitin-like modifier (SUMO) E3 ligases	553:603	the small ubiquitin-like modifier (SUMO) E3 ligases	553:603	Here, we report that RAN-binding protein 2 (RANBP2), one of the small ubiquitin-like modifier (SUMO) E3 ligases, contributed to malignant phenotypes in HCC.
34298689	3	54	theme	RAN-binding	514:524	arg1	protein					526:532	RAN-binding protein 2	514:534	RAN-binding protein 2 (RANBP2)	514:543	Here, we report that RAN-binding protein 2 (RANBP2), one of the small ubiquitin-like modifier (SUMO) E3 ligases, contributed to malignant phenotypes in HCC.
34298689	3	54	theme	RAN-binding	514:524	arg1	RANBP2					537:542	RANBP2	537:542	RANBP2	537:542	Here, we report that RAN-binding protein 2 (RANBP2), one of the small ubiquitin-like modifier (SUMO) E3 ligases, contributed to malignant phenotypes in HCC.
34298689	3	54	theme	RAN-binding	514:524	arg1	one					546:548	one	546:548	one	546:548	Here, we report that RAN-binding protein 2 (RANBP2), one of the small ubiquitin-like modifier (SUMO) E3 ligases, contributed to malignant phenotypes in HCC.
34298689	7	55	theme	further	1567:1573	arg1	study					1575:1579	the further study	1563:1579	the further study of promising implications for HCC therapy	1563:1621	Altogether, our results show a novel molecular mechanism whereby RANBP2 regulates its function through CEBPα-dependent OGA downregulation to induce a global change in the hyper-O-GlcNAcylation of genes, such as PGC1α, encouraging the further study of promising implications for HCC therapy.
34298689	6	56	theme	receptor	1261:1268	arg1	gamma					1270:1274	peroxisome proliferative-activated receptor gamma	1226:1274	peroxisome proliferative-activated receptor gamma coactivator 1 alpha (PGC1α)	1226:1302	Importantly, we provided in vitro and in vivo evidence of HCC malignant phenotypes that RANBP2 triggered through an imbalance of OGT/OGA and subsequent higher O-GlcNAcylation events for oncogenic proteins such as peroxisome proliferative-activated receptor gamma coactivator 1 alpha (PGC1α) in a CEBPα-dependent manner.
34298689	6	57	theme	malignant	1075:1083	arg1	phenotypes					1085:1094	HCC malignant phenotypes	1071:1094	HCC malignant phenotypes	1071:1094	Importantly, we provided in vitro and in vivo evidence of HCC malignant phenotypes that RANBP2 triggered through an imbalance of OGT/OGA and subsequent higher O-GlcNAcylation events for oncogenic proteins such as peroxisome proliferative-activated receptor gamma coactivator 1 alpha (PGC1α) in a CEBPα-dependent manner.
34298689	4	58	theme	alpha	712:716	arg1	SUMOylation					726:736	CCAAT/enhancer-binding protein alpha (CEBPα) SUMOylation	681:736	CCAAT/enhancer-binding protein alpha (CEBPα) SUMOylation	681:736	RANBP2 was found to facilitate CCAAT/enhancer-binding protein alpha (CEBPα) SUMOylation and degradation by direct interplay with CEBPα.
34298689	3	59	theme	malignant	621:629	arg1	phenotypes					631:640	malignant phenotypes	621:640	malignant phenotypes in HCC	621:647	Here, we report that RAN-binding protein 2 (RANBP2), one of the small ubiquitin-like modifier (SUMO) E3 ligases, contributed to malignant phenotypes in HCC.
34298689	4	60	theme	protein	704:710	arg1	CEBPα					719:723	CEBPα	719:723	CEBPα	719:723	RANBP2 was found to facilitate CCAAT/enhancer-binding protein alpha (CEBPα) SUMOylation and degradation by direct interplay with CEBPα.
34298689	4	60	theme	protein	704:710	arg1	alpha					712:716	CCAAT/enhancer-binding protein alpha	681:716	CCAAT/enhancer-binding protein alpha (CEBPα) SUMOylation	681:736	RANBP2 was found to facilitate CCAAT/enhancer-binding protein alpha (CEBPα) SUMOylation and degradation by direct interplay with CEBPα.
31679690	8	0	theme	FOXM1	1137:1141	arg1	expression					1143:1152	FOXM1 expression	1137:1152	FOXM1 expression	1137:1152	Moreover, FOXM1 expression and cell proliferation were reduced in FBXL2-induced NUGC-3 cells, and the reductions were attenuated by TMG, indicating that FOXM1 was stabilized by O-GlcNAcylation-mediated degradation of FBXL2 to induce cancer progression.
31679690	6	1	theme	ubiquitinated	925:937	arg1	FOXM1					939:943	FBXL2 ubiquitinated FOXM1	919:943	FBXL2 ubiquitinated FOXM1	919:943	We found that FBXL2 ubiquitinated FOXM1, and the interaction with FBXL2 and ubiquitination of FOXM1 were reduced by TMG in NUGC-3 cells.
31679690	9	2	theme	elevated	1404:1411	arg1	O-GlcNAcylation					1413:1427	elevated O-GlcNAcylation	1404:1427	elevated O-GlcNAcylation	1404:1427	These data suggest that elevated O-GlcNAcylation contributes to cancer progression by suppressing FBXL2-mediated degradation of FOXM1.
31679690	8	3	theme	FBXL2	1344:1348	arg1	degradation					1329:1339	O-GlcNAcylation-mediated degradation	1304:1339	O-GlcNAcylation-mediated degradation of FBXL2 to induce cancer progression	1304:1377	Moreover, FOXM1 expression and cell proliferation were reduced in FBXL2-induced NUGC-3 cells, and the reductions were attenuated by TMG, indicating that FOXM1 was stabilized by O-GlcNAcylation-mediated degradation of FBXL2 to induce cancer progression.
31679690	8	4	theme	FBXL2-induced	1193:1205	arg1	NUGC-3 cells					1207:1218	FBXL2-induced NUGC-3 cells	1193:1218	FBXL2-induced NUGC-3 cells	1193:1218	Moreover, FOXM1 expression and cell proliferation were reduced in FBXL2-induced NUGC-3 cells, and the reductions were attenuated by TMG, indicating that FOXM1 was stabilized by O-GlcNAcylation-mediated degradation of FBXL2 to induce cancer progression.
31679690	9	5	theme	cancer	1444:1449	arg1	progression					1451:1461	cancer progression	1444:1461	cancer progression	1444:1461	These data suggest that elevated O-GlcNAcylation contributes to cancer progression by suppressing FBXL2-mediated degradation of FOXM1.
31679690	3	6	theme	critical	388:395	arg1	FOXM1					379:383	FOXM1	379:383	FOXM1	379:383	We previously showed that the expression of FOXM1, a critical oncogenic transcription factor widely overexpressed in solid tumors, was elevated in MKN45 cells, a human gastric cancer cell line, by the O-GlcNAcase inhibitor Thiamet G (TMG), which induces augmented O-GlcNAcylation.
31679690	3	6	theme	critical	388:395	arg1	factor					421:426	a critical oncogenic transcription factor	386:426	a critical oncogenic transcription factor widely overexpressed in solid tumors	386:463	We previously showed that the expression of FOXM1, a critical oncogenic transcription factor widely overexpressed in solid tumors, was elevated in MKN45 cells, a human gastric cancer cell line, by the O-GlcNAcase inhibitor Thiamet G (TMG), which induces augmented O-GlcNAcylation.
31679690	3	7	theme	O-GlcNAcase	536:546	arg1	TMG					569:571	TMG	569:571	TMG	569:571	We previously showed that the expression of FOXM1, a critical oncogenic transcription factor widely overexpressed in solid tumors, was elevated in MKN45 cells, a human gastric cancer cell line, by the O-GlcNAcase inhibitor Thiamet G (TMG), which induces augmented O-GlcNAcylation.
31679690	3	7	theme	O-GlcNAcase	536:546	arg1	G					566:566	the O-GlcNAcase inhibitor Thiamet G	532:566	the O-GlcNAcase inhibitor Thiamet G (TMG)	532:572	We previously showed that the expression of FOXM1, a critical oncogenic transcription factor widely overexpressed in solid tumors, was elevated in MKN45 cells, a human gastric cancer cell line, by the O-GlcNAcase inhibitor Thiamet G (TMG), which induces augmented O-GlcNAcylation.
31679690	6	8	theme	FOXM1	999:1003	arg1	FBXL2					971:975	FBXL2	971:975	FBXL2	971:975	We found that FBXL2 ubiquitinated FOXM1, and the interaction with FBXL2 and ubiquitination of FOXM1 were reduced by TMG in NUGC-3 cells.
31679690	6	8	theme	FOXM1	999:1003	arg1	ubiquitination					981:994	ubiquitination	981:994	ubiquitination	981:994	We found that FBXL2 ubiquitinated FOXM1, and the interaction with FBXL2 and ubiquitination of FOXM1 were reduced by TMG in NUGC-3 cells.
31679690	3	9	theme	oncogenic	397:405	arg1	FOXM1					379:383	FOXM1	379:383	FOXM1	379:383	We previously showed that the expression of FOXM1, a critical oncogenic transcription factor widely overexpressed in solid tumors, was elevated in MKN45 cells, a human gastric cancer cell line, by the O-GlcNAcase inhibitor Thiamet G (TMG), which induces augmented O-GlcNAcylation.
31679690	3	9	theme	oncogenic	397:405	arg1	factor					421:426	a critical oncogenic transcription factor	386:426	a critical oncogenic transcription factor widely overexpressed in solid tumors	386:463	We previously showed that the expression of FOXM1, a critical oncogenic transcription factor widely overexpressed in solid tumors, was elevated in MKN45 cells, a human gastric cancer cell line, by the O-GlcNAcase inhibitor Thiamet G (TMG), which induces augmented O-GlcNAcylation.
31679690	5	10	from	TMG	837:839	arg1	lines					874:878	the other gastric cancer cell lines	844:878	the other gastric cancer cell lines	844:878	Consistent with the results in MKN45 cells, FOXM1 expression was increased, accompanied by its decreased ubiquitination and degradation by TMG in the other gastric cancer cell lines, including NUGC-3 cells.
31679690	5	10	from	TMG	837:839	arg1	NUGC-3 cells					891:902	NUGC-3 cells	891:902	NUGC-3 cells	891:902	Consistent with the results in MKN45 cells, FOXM1 expression was increased, accompanied by its decreased ubiquitination and degradation by TMG in the other gastric cancer cell lines, including NUGC-3 cells.
31679690	9	11	theme	FOXM1	1508:1512	arg1	degradation					1493:1503	FBXL2-mediated degradation	1478:1503	FBXL2-mediated degradation of FOXM1	1478:1512	These data suggest that elevated O-GlcNAcylation contributes to cancer progression by suppressing FBXL2-mediated degradation of FOXM1.
31679690	5	12	theme	cell	869:872	arg1	lines					874:878	the other gastric cancer cell lines	844:878	the other gastric cancer cell lines	844:878	Consistent with the results in MKN45 cells, FOXM1 expression was increased, accompanied by its decreased ubiquitination and degradation by TMG in the other gastric cancer cell lines, including NUGC-3 cells.
31679690	5	12	theme	cell	869:872	arg1	NUGC-3 cells					891:902	NUGC-3 cells	891:902	NUGC-3 cells	891:902	Consistent with the results in MKN45 cells, FOXM1 expression was increased, accompanied by its decreased ubiquitination and degradation by TMG in the other gastric cancer cell lines, including NUGC-3 cells.
31679690	5	13	theme	other	848:852	arg1	lines					874:878	the other gastric cancer cell lines	844:878	the other gastric cancer cell lines	844:878	Consistent with the results in MKN45 cells, FOXM1 expression was increased, accompanied by its decreased ubiquitination and degradation by TMG in the other gastric cancer cell lines, including NUGC-3 cells.
31679690	5	13	theme	other	848:852	arg1	NUGC-3 cells					891:902	NUGC-3 cells	891:902	NUGC-3 cells	891:902	Consistent with the results in MKN45 cells, FOXM1 expression was increased, accompanied by its decreased ubiquitination and degradation by TMG in the other gastric cancer cell lines, including NUGC-3 cells.
31679690	4	14	theme	E3	642:643	arg1	ligase					655:660	FBXL2 E3 ubiquitin ligase	636:660	FBXL2 E3 ubiquitin ligase	636:660	Here, we identified FBXL2 E3 ubiquitin ligase as a new target of O-GlcNAcylation.
31679690	4	14	theme	E3	642:643	arg1	target					671:676	a new target	665:676	a new target of O-GlcNAcylation	665:695	Here, we identified FBXL2 E3 ubiquitin ligase as a new target of O-GlcNAcylation.
31679690	2	15	theme	cancer	315:320	arg1	progression					322:332	cancer progression	315:332	cancer progression	315:332	Elevated O-GlcNAcylation is a general property of cancer and plays a critical role in cancer progression.
31679690	1	16	theme	cellular	209:216	arg1	signaling					218:226	cellular signaling	209:226	cellular signaling	209:226	O-GlcNAcylation is a dynamic and reversible post-translational modification of cytonuclear molecules that regulates cellular signaling.
31679690	5	17	from	results	718:724	arg1	MKN45 cells					729:739	MKN45 cells	729:739	MKN45 cells	729:739	Consistent with the results in MKN45 cells, FOXM1 expression was increased, accompanied by its decreased ubiquitination and degradation by TMG in the other gastric cancer cell lines, including NUGC-3 cells.
31679690	8	18	theme	cancer	1360:1365	arg1	progression					1367:1377	cancer progression	1360:1377	cancer progression	1360:1377	Moreover, FOXM1 expression and cell proliferation were reduced in FBXL2-induced NUGC-3 cells, and the reductions were attenuated by TMG, indicating that FOXM1 was stabilized by O-GlcNAcylation-mediated degradation of FBXL2 to induce cancer progression.
31679690	9	19	theme	FBXL2-mediated	1478:1491	arg1	degradation					1493:1503	FBXL2-mediated degradation	1478:1503	FBXL2-mediated degradation of FOXM1	1478:1512	These data suggest that elevated O-GlcNAcylation contributes to cancer progression by suppressing FBXL2-mediated degradation of FOXM1.
31679690	3	20	theme	inhibitor	548:556	arg1	TMG					569:571	TMG	569:571	TMG	569:571	We previously showed that the expression of FOXM1, a critical oncogenic transcription factor widely overexpressed in solid tumors, was elevated in MKN45 cells, a human gastric cancer cell line, by the O-GlcNAcase inhibitor Thiamet G (TMG), which induces augmented O-GlcNAcylation.
31679690	3	20	theme	inhibitor	548:556	arg1	G					566:566	the O-GlcNAcase inhibitor Thiamet G	532:566	the O-GlcNAcase inhibitor Thiamet G (TMG)	532:572	We previously showed that the expression of FOXM1, a critical oncogenic transcription factor widely overexpressed in solid tumors, was elevated in MKN45 cells, a human gastric cancer cell line, by the O-GlcNAcase inhibitor Thiamet G (TMG), which induces augmented O-GlcNAcylation.
31679690	0	21	theme	O-GlcNAcylation-mediated	0:23	arg1	degradation					25:35	O-GlcNAcylation-mediated degradation	0:35	O-GlcNAcylation-mediated degradation of FBXL2	0:44	O-GlcNAcylation-mediated degradation of FBXL2 stabilizes FOXM1 to induce cancer progression.
31679690	0	22	theme	FBXL2	40:44	arg1	degradation					25:35	O-GlcNAcylation-mediated degradation	0:35	O-GlcNAcylation-mediated degradation of FBXL2	0:44	O-GlcNAcylation-mediated degradation of FBXL2 stabilizes FOXM1 to induce cancer progression.
31679690	3	23	theme	transcription	407:419	arg1	FOXM1					379:383	FOXM1	379:383	FOXM1	379:383	We previously showed that the expression of FOXM1, a critical oncogenic transcription factor widely overexpressed in solid tumors, was elevated in MKN45 cells, a human gastric cancer cell line, by the O-GlcNAcase inhibitor Thiamet G (TMG), which induces augmented O-GlcNAcylation.
31679690	3	23	theme	transcription	407:419	arg1	factor					421:426	a critical oncogenic transcription factor	386:426	a critical oncogenic transcription factor widely overexpressed in solid tumors	386:463	We previously showed that the expression of FOXM1, a critical oncogenic transcription factor widely overexpressed in solid tumors, was elevated in MKN45 cells, a human gastric cancer cell line, by the O-GlcNAcase inhibitor Thiamet G (TMG), which induces augmented O-GlcNAcylation.
31679690	8	24	theme	cell	1158:1161	arg1	proliferation					1163:1175	cell proliferation	1158:1175	cell proliferation	1158:1175	Moreover, FOXM1 expression and cell proliferation were reduced in FBXL2-induced NUGC-3 cells, and the reductions were attenuated by TMG, indicating that FOXM1 was stabilized by O-GlcNAcylation-mediated degradation of FBXL2 to induce cancer progression.
31679690	1	25	theme	dynamic	114:120	arg1	modification					156:167	a dynamic and reversible post-translational modification	112:167	a dynamic and reversible post-translational modification of cytonuclear molecules that regulates cellular signaling	112:226	O-GlcNAcylation is a dynamic and reversible post-translational modification of cytonuclear molecules that regulates cellular signaling.
31679690	1	25	theme	dynamic	114:120	arg1	O-GlcNAcylation					93:107	O-GlcNAcylation	93:107	O-GlcNAcylation	93:107	O-GlcNAcylation is a dynamic and reversible post-translational modification of cytonuclear molecules that regulates cellular signaling.
31679690	3	26	theme	human	497:501	arg1	line					523:526	a human gastric cancer cell line	495:526	a human gastric cancer cell line	495:526	We previously showed that the expression of FOXM1, a critical oncogenic transcription factor widely overexpressed in solid tumors, was elevated in MKN45 cells, a human gastric cancer cell line, by the O-GlcNAcase inhibitor Thiamet G (TMG), which induces augmented O-GlcNAcylation.
31679690	3	26	theme	human	497:501	arg1	MKN45 cells					482:492	MKN45 cells	482:492	MKN45 cells	482:492	We previously showed that the expression of FOXM1, a critical oncogenic transcription factor widely overexpressed in solid tumors, was elevated in MKN45 cells, a human gastric cancer cell line, by the O-GlcNAcase inhibitor Thiamet G (TMG), which induces augmented O-GlcNAcylation.
31679690	3	27	theme	Thiamet	558:564	arg1	TMG					569:571	TMG	569:571	TMG	569:571	We previously showed that the expression of FOXM1, a critical oncogenic transcription factor widely overexpressed in solid tumors, was elevated in MKN45 cells, a human gastric cancer cell line, by the O-GlcNAcase inhibitor Thiamet G (TMG), which induces augmented O-GlcNAcylation.
31679690	3	27	theme	Thiamet	558:564	arg1	G					566:566	the O-GlcNAcase inhibitor Thiamet G	532:566	the O-GlcNAcase inhibitor Thiamet G (TMG)	532:572	We previously showed that the expression of FOXM1, a critical oncogenic transcription factor widely overexpressed in solid tumors, was elevated in MKN45 cells, a human gastric cancer cell line, by the O-GlcNAcase inhibitor Thiamet G (TMG), which induces augmented O-GlcNAcylation.
31679690	2	28	theme	Elevated	229:236	arg1	property					267:274	a general property	257:274	a general property of cancer	257:284	Elevated O-GlcNAcylation is a general property of cancer and plays a critical role in cancer progression.
31679690	2	28	theme	Elevated	229:236	arg1	O-GlcNAcylation					238:252	Elevated O-GlcNAcylation	229:252	Elevated O-GlcNAcylation	229:252	Elevated O-GlcNAcylation is a general property of cancer and plays a critical role in cancer progression.
31679690	3	29	theme	gastric	503:509	arg1	line					523:526	a human gastric cancer cell line	495:526	a human gastric cancer cell line	495:526	We previously showed that the expression of FOXM1, a critical oncogenic transcription factor widely overexpressed in solid tumors, was elevated in MKN45 cells, a human gastric cancer cell line, by the O-GlcNAcase inhibitor Thiamet G (TMG), which induces augmented O-GlcNAcylation.
31679690	3	29	theme	gastric	503:509	arg1	MKN45 cells					482:492	MKN45 cells	482:492	MKN45 cells	482:492	We previously showed that the expression of FOXM1, a critical oncogenic transcription factor widely overexpressed in solid tumors, was elevated in MKN45 cells, a human gastric cancer cell line, by the O-GlcNAcase inhibitor Thiamet G (TMG), which induces augmented O-GlcNAcylation.
31679690	6	30	dep	ubiquitinated	925:937	arg1	FBXL2					919:923	FBXL2	919:923	FBXL2	919:923	We found that FBXL2 ubiquitinated FOXM1, and the interaction with FBXL2 and ubiquitination of FOXM1 were reduced by TMG in NUGC-3 cells.
31679690	5	31	dep	increased	763:771	arg1	accompanied					774:784	accompanied	774:784	accompanied by its decreased ubiquitination and degradation by TMG in the other gastric cancer cell lines, including NUGC-3 cells	774:902	Consistent with the results in MKN45 cells, FOXM1 expression was increased, accompanied by its decreased ubiquitination and degradation by TMG in the other gastric cancer cell lines, including NUGC-3 cells.
31679690	5	32	theme	gastric	854:860	arg1	lines					874:878	the other gastric cancer cell lines	844:878	the other gastric cancer cell lines	844:878	Consistent with the results in MKN45 cells, FOXM1 expression was increased, accompanied by its decreased ubiquitination and degradation by TMG in the other gastric cancer cell lines, including NUGC-3 cells.
31679690	5	32	theme	gastric	854:860	arg1	NUGC-3 cells					891:902	NUGC-3 cells	891:902	NUGC-3 cells	891:902	Consistent with the results in MKN45 cells, FOXM1 expression was increased, accompanied by its decreased ubiquitination and degradation by TMG in the other gastric cancer cell lines, including NUGC-3 cells.
31679690	4	33	theme	new	667:669	arg1	ligase					655:660	FBXL2 E3 ubiquitin ligase	636:660	FBXL2 E3 ubiquitin ligase	636:660	Here, we identified FBXL2 E3 ubiquitin ligase as a new target of O-GlcNAcylation.
31679690	4	33	theme	new	667:669	arg1	target					671:676	a new target	665:676	a new target of O-GlcNAcylation	665:695	Here, we identified FBXL2 E3 ubiquitin ligase as a new target of O-GlcNAcylation.
31679690	5	34	theme	decreased	793:801	arg1	ubiquitination					803:816	decreased ubiquitination	793:816	decreased ubiquitination	793:816	Consistent with the results in MKN45 cells, FOXM1 expression was increased, accompanied by its decreased ubiquitination and degradation by TMG in the other gastric cancer cell lines, including NUGC-3 cells.
31679690	8	35	theme	O-GlcNAcylation-mediated	1304:1327	arg1	degradation					1329:1339	O-GlcNAcylation-mediated degradation	1304:1339	O-GlcNAcylation-mediated degradation of FBXL2 to induce cancer progression	1304:1377	Moreover, FOXM1 expression and cell proliferation were reduced in FBXL2-induced NUGC-3 cells, and the reductions were attenuated by TMG, indicating that FOXM1 was stabilized by O-GlcNAcylation-mediated degradation of FBXL2 to induce cancer progression.
31679690	2	36	theme	cancer	279:284	arg1	property					267:274	a general property	257:274	a general property of cancer	257:284	Elevated O-GlcNAcylation is a general property of cancer and plays a critical role in cancer progression.
31679690	2	36	theme	cancer	279:284	arg1	O-GlcNAcylation					238:252	Elevated O-GlcNAcylation	229:252	Elevated O-GlcNAcylation	229:252	Elevated O-GlcNAcylation is a general property of cancer and plays a critical role in cancer progression.
31679690	5	37	theme	cancer	862:867	arg1	lines					874:878	the other gastric cancer cell lines	844:878	the other gastric cancer cell lines	844:878	Consistent with the results in MKN45 cells, FOXM1 expression was increased, accompanied by its decreased ubiquitination and degradation by TMG in the other gastric cancer cell lines, including NUGC-3 cells.
31679690	5	37	theme	cancer	862:867	arg1	NUGC-3 cells					891:902	NUGC-3 cells	891:902	NUGC-3 cells	891:902	Consistent with the results in MKN45 cells, FOXM1 expression was increased, accompanied by its decreased ubiquitination and degradation by TMG in the other gastric cancer cell lines, including NUGC-3 cells.
31679690	0	38	theme	cancer	73:78	arg1	progression					80:90	cancer progression	73:90	cancer progression	73:90	O-GlcNAcylation-mediated degradation of FBXL2 stabilizes FOXM1 to induce cancer progression.
31679690	3	39	theme	augmented	589:597	arg1	O-GlcNAcylation					599:613	augmented O-GlcNAcylation	589:613	augmented O-GlcNAcylation	589:613	We previously showed that the expression of FOXM1, a critical oncogenic transcription factor widely overexpressed in solid tumors, was elevated in MKN45 cells, a human gastric cancer cell line, by the O-GlcNAcase inhibitor Thiamet G (TMG), which induces augmented O-GlcNAcylation.
31679690	1	40	theme	reversible	126:135	arg1	modification					156:167	a dynamic and reversible post-translational modification	112:167	a dynamic and reversible post-translational modification of cytonuclear molecules that regulates cellular signaling	112:226	O-GlcNAcylation is a dynamic and reversible post-translational modification of cytonuclear molecules that regulates cellular signaling.
31679690	1	40	theme	reversible	126:135	arg1	O-GlcNAcylation					93:107	O-GlcNAcylation	93:107	O-GlcNAcylation	93:107	O-GlcNAcylation is a dynamic and reversible post-translational modification of cytonuclear molecules that regulates cellular signaling.
31679690	3	41	theme	solid	452:456	arg1	tumors					458:463	solid tumors	452:463	solid tumors	452:463	We previously showed that the expression of FOXM1, a critical oncogenic transcription factor widely overexpressed in solid tumors, was elevated in MKN45 cells, a human gastric cancer cell line, by the O-GlcNAcase inhibitor Thiamet G (TMG), which induces augmented O-GlcNAcylation.
31679690	2	42	theme	general	259:265	arg1	property					267:274	a general property	257:274	a general property of cancer	257:284	Elevated O-GlcNAcylation is a general property of cancer and plays a critical role in cancer progression.
31679690	2	42	theme	general	259:265	arg1	O-GlcNAcylation					238:252	Elevated O-GlcNAcylation	229:252	Elevated O-GlcNAcylation	229:252	Elevated O-GlcNAcylation is a general property of cancer and plays a critical role in cancer progression.
31679690	5	43	with	Consistent	698:707	arg1	results					718:724	the results	714:724	the results in MKN45 cells	714:739	Consistent with the results in MKN45 cells, FOXM1 expression was increased, accompanied by its decreased ubiquitination and degradation by TMG in the other gastric cancer cell lines, including NUGC-3 cells.
31679690	1	44	theme	post-translational	137:154	arg1	modification					156:167	a dynamic and reversible post-translational modification	112:167	a dynamic and reversible post-translational modification of cytonuclear molecules that regulates cellular signaling	112:226	O-GlcNAcylation is a dynamic and reversible post-translational modification of cytonuclear molecules that regulates cellular signaling.
31679690	1	44	theme	post-translational	137:154	arg1	O-GlcNAcylation					93:107	O-GlcNAcylation	93:107	O-GlcNAcylation	93:107	O-GlcNAcylation is a dynamic and reversible post-translational modification of cytonuclear molecules that regulates cellular signaling.
31679690	4	45	theme	O-GlcNAcylation	681:695	arg1	ligase					655:660	FBXL2 E3 ubiquitin ligase	636:660	FBXL2 E3 ubiquitin ligase	636:660	Here, we identified FBXL2 E3 ubiquitin ligase as a new target of O-GlcNAcylation.
31679690	4	45	theme	O-GlcNAcylation	681:695	arg1	target					671:676	a new target	665:676	a new target of O-GlcNAcylation	665:695	Here, we identified FBXL2 E3 ubiquitin ligase as a new target of O-GlcNAcylation.
31679690	3	46	theme	cancer	511:516	arg1	line					523:526	a human gastric cancer cell line	495:526	a human gastric cancer cell line	495:526	We previously showed that the expression of FOXM1, a critical oncogenic transcription factor widely overexpressed in solid tumors, was elevated in MKN45 cells, a human gastric cancer cell line, by the O-GlcNAcase inhibitor Thiamet G (TMG), which induces augmented O-GlcNAcylation.
31679690	3	46	theme	cancer	511:516	arg1	MKN45 cells					482:492	MKN45 cells	482:492	MKN45 cells	482:492	We previously showed that the expression of FOXM1, a critical oncogenic transcription factor widely overexpressed in solid tumors, was elevated in MKN45 cells, a human gastric cancer cell line, by the O-GlcNAcase inhibitor Thiamet G (TMG), which induces augmented O-GlcNAcylation.
31679690	6	47	with	interaction	954:964	arg1	FBXL2					971:975	FBXL2	971:975	FBXL2	971:975	We found that FBXL2 ubiquitinated FOXM1, and the interaction with FBXL2 and ubiquitination of FOXM1 were reduced by TMG in NUGC-3 cells.
31679690	6	47	with	interaction	954:964	arg1	ubiquitination					981:994	ubiquitination	981:994	ubiquitination	981:994	We found that FBXL2 ubiquitinated FOXM1, and the interaction with FBXL2 and ubiquitination of FOXM1 were reduced by TMG in NUGC-3 cells.
31679690	2	48	theme	critical	298:305	arg1	role					307:310	a critical role	296:310	a critical role	296:310	Elevated O-GlcNAcylation is a general property of cancer and plays a critical role in cancer progression.
31679690	3	49	theme	cell	518:521	arg1	line					523:526	a human gastric cancer cell line	495:526	a human gastric cancer cell line	495:526	We previously showed that the expression of FOXM1, a critical oncogenic transcription factor widely overexpressed in solid tumors, was elevated in MKN45 cells, a human gastric cancer cell line, by the O-GlcNAcase inhibitor Thiamet G (TMG), which induces augmented O-GlcNAcylation.
31679690	3	49	theme	cell	518:521	arg1	MKN45 cells					482:492	MKN45 cells	482:492	MKN45 cells	482:492	We previously showed that the expression of FOXM1, a critical oncogenic transcription factor widely overexpressed in solid tumors, was elevated in MKN45 cells, a human gastric cancer cell line, by the O-GlcNAcase inhibitor Thiamet G (TMG), which induces augmented O-GlcNAcylation.
31679690	6	50	with	FOXM1	939:943	arg1	FBXL2					971:975	FBXL2	971:975	FBXL2	971:975	We found that FBXL2 ubiquitinated FOXM1, and the interaction with FBXL2 and ubiquitination of FOXM1 were reduced by TMG in NUGC-3 cells.
31679690	6	50	with	FOXM1	939:943	arg1	ubiquitination					981:994	ubiquitination	981:994	ubiquitination	981:994	We found that FBXL2 ubiquitinated FOXM1, and the interaction with FBXL2 and ubiquitination of FOXM1 were reduced by TMG in NUGC-3 cells.
31679690	4	51	theme	ubiquitin	645:653	arg1	ligase					655:660	FBXL2 E3 ubiquitin ligase	636:660	FBXL2 E3 ubiquitin ligase	636:660	Here, we identified FBXL2 E3 ubiquitin ligase as a new target of O-GlcNAcylation.
31679690	4	51	theme	ubiquitin	645:653	arg1	target					671:676	a new target	665:676	a new target of O-GlcNAcylation	665:695	Here, we identified FBXL2 E3 ubiquitin ligase as a new target of O-GlcNAcylation.
31679690	1	52	theme	cytonuclear	172:182	arg1	molecules					184:192	cytonuclear molecules	172:192	cytonuclear molecules	172:192	O-GlcNAcylation is a dynamic and reversible post-translational modification of cytonuclear molecules that regulates cellular signaling.
31679690	4	53	theme	FBXL2	636:640	arg1	ligase					655:660	FBXL2 E3 ubiquitin ligase	636:660	FBXL2 E3 ubiquitin ligase	636:660	Here, we identified FBXL2 E3 ubiquitin ligase as a new target of O-GlcNAcylation.
31679690	4	53	theme	FBXL2	636:640	arg1	target					671:676	a new target	665:676	a new target of O-GlcNAcylation	665:695	Here, we identified FBXL2 E3 ubiquitin ligase as a new target of O-GlcNAcylation.
31679690	3	54	theme	FOXM1	379:383	arg1	expression					365:374	the expression	361:374	the expression of FOXM1, a critical oncogenic transcription factor widely overexpressed in solid tumors,	361:464	We previously showed that the expression of FOXM1, a critical oncogenic transcription factor widely overexpressed in solid tumors, was elevated in MKN45 cells, a human gastric cancer cell line, by the O-GlcNAcase inhibitor Thiamet G (TMG), which induces augmented O-GlcNAcylation.
31679690	1	55	theme	molecules	184:192	arg1	modification					156:167	a dynamic and reversible post-translational modification	112:167	a dynamic and reversible post-translational modification of cytonuclear molecules that regulates cellular signaling	112:226	O-GlcNAcylation is a dynamic and reversible post-translational modification of cytonuclear molecules that regulates cellular signaling.
31679690	1	55	theme	molecules	184:192	arg1	O-GlcNAcylation					93:107	O-GlcNAcylation	93:107	O-GlcNAcylation	93:107	O-GlcNAcylation is a dynamic and reversible post-translational modification of cytonuclear molecules that regulates cellular signaling.
31679690	5	56	theme	FOXM1	742:746	arg1	expression					748:757	FOXM1 expression	742:757	FOXM1 expression	742:757	Consistent with the results in MKN45 cells, FOXM1 expression was increased, accompanied by its decreased ubiquitination and degradation by TMG in the other gastric cancer cell lines, including NUGC-3 cells.
36067866	9	0	from	changes	1349:1355	arg1	O-glycosylation					1360:1374	O-glycosylation	1360:1374	O-glycosylation of NOTCH3	1360:1384	The resultant changes in O-glycosylation of NOTCH3 were evaluated by label-free glycopeptide quantification.
36067866	7	1	theme	repeats	1195:1201	arg1	secretion					1171:1179	the secretion	1167:1179	the secretion of NOTCH1 EGF repeats	1167:1201	Our results in HEK293T cells revealed that, unlike the effect on endogenous NOTCH receptors, overexpressed EGF domain-specific O-GlcNAc transferase (EOGT) markedly enhanced the secretion of NOTCH1 EGF repeats in an enzyme activity-dependent manner.
36067866	7	2	theme	domain-specific	1105:1119	arg1	EOGT					1143:1146	EOGT	1143:1146	EOGT	1143:1146	Our results in HEK293T cells revealed that, unlike the effect on endogenous NOTCH receptors, overexpressed EGF domain-specific O-GlcNAc transferase (EOGT) markedly enhanced the secretion of NOTCH1 EGF repeats in an enzyme activity-dependent manner.
36067866	7	2	theme	domain-specific	1105:1119	arg1	transferase					1130:1140	domain-specific O-GlcNAc transferase	1105:1140	overexpressed EGF domain-specific O-GlcNAc transferase (EOGT)	1087:1147	Our results in HEK293T cells revealed that, unlike the effect on endogenous NOTCH receptors, overexpressed EGF domain-specific O-GlcNAc transferase (EOGT) markedly enhanced the secretion of NOTCH1 EGF repeats in an enzyme activity-dependent manner.
36067866	9	3	theme	label-free	1404:1413	arg1	quantification					1428:1441	label-free glycopeptide quantification	1404:1441	label-free glycopeptide quantification	1404:1441	The resultant changes in O-glycosylation of NOTCH3 were evaluated by label-free glycopeptide quantification.
36067866	6	4	theme	repeats	985:991	arg1	secretion					962:970	the secretion	958:970	the secretion of NOTCH EGF repeats	958:991	This study evaluated the effect of EGF domain-modifying glycosyltransferases on the secretion of NOTCH EGF repeats.
36067866	1	5	theme	essential	198:206	arg1	signaling					188:196	evolutionarily conserved intercellular signaling	149:196	evolutionarily conserved intercellular signaling essential for cell-to-cell communication during development	149:256	The Notch pathway represents evolutionarily conserved intercellular signaling essential for cell-to-cell communication during development.
36067866	10	6	gly	O-glycosylation	1601:1615	arg1	domains					1624:1630	EGF domains	1620:1630	EGF domains	1620:1630	This study provides an experimental strategy to efficiently generate NOTCH EGF repeats by manipulating the expression of glycosyltransferases that alter the O-glycosylation of EGF domains.
36067866	8	7	theme	EOGT	1329:1332	arg1	effect					1319:1324	the effect	1315:1324	the effect of EOGT	1315:1332	The co-expression of protein O-glucosyltransferase 1 further manifested the effect of EOGT.
36067866	5	8	theme	potent	792:797	arg1	activity					816:823	potent Notch inhibitory activity	792:823	potent Notch inhibitory activity	792:823	Although full-length NOTCH EGF repeats exhibited potent Notch inhibitory activity, they were poorly produced in the transfected cells.
36067866	3	9	from	ligands	477:483	arg1	cells					500:504	neighboring cells	488:504	neighboring cells	488:504	Notch signaling is initiated by the interaction of NOTCH receptors with their ligands on neighboring cells.
36067866	7	10	theme	NOTCH1	1184:1189	arg1	repeats					1195:1201	NOTCH1 EGF repeats	1184:1201	NOTCH1 EGF repeats	1184:1201	Our results in HEK293T cells revealed that, unlike the effect on endogenous NOTCH receptors, overexpressed EGF domain-specific O-GlcNAc transferase (EOGT) markedly enhanced the secretion of NOTCH1 EGF repeats in an enzyme activity-dependent manner.
36067866	10	11	theme	EGF	1519:1521	arg1	repeats					1523:1529	NOTCH EGF repeats	1513:1529	NOTCH EGF repeats	1513:1529	This study provides an experimental strategy to efficiently generate NOTCH EGF repeats by manipulating the expression of glycosyltransferases that alter the O-glycosylation of EGF domains.
36067866	10	12	theme	experimental	1467:1478	arg1	strategy					1480:1487	an experimental strategy	1464:1487	an experimental strategy to efficiently generate NOTCH EGF repeats by manipulating the expression of glycosyltransferases that alter the O-glycosylation of EGF domains	1464:1630	This study provides an experimental strategy to efficiently generate NOTCH EGF repeats by manipulating the expression of glycosyltransferases that alter the O-glycosylation of EGF domains.
36067866	3	13	theme	receptors	456:464	arg1	interaction					435:445	the interaction	431:445	the interaction of NOTCH receptors with their ligands on neighboring cells	431:504	Notch signaling is initiated by the interaction of NOTCH receptors with their ligands on neighboring cells.
36067866	0	14	theme	increased	93:101	arg1	O-glycosylation					103:117	increased O-glycosylation	93:117	increased O-glycosylation	93:117	Secretory expression of mammalian NOTCH tandem epidermal growth factor-like repeats based on increased O-glycosylation.
36067866	6	15	theme	NOTCH	975:979	arg1	repeats					985:991	NOTCH EGF repeats	975:991	NOTCH EGF repeats	975:991	This study evaluated the effect of EGF domain-modifying glycosyltransferases on the secretion of NOTCH EGF repeats.
36067866	7	16	theme	EGF	1191:1193	arg1	repeats					1195:1201	NOTCH1 EGF repeats	1184:1201	NOTCH1 EGF repeats	1184:1201	Our results in HEK293T cells revealed that, unlike the effect on endogenous NOTCH receptors, overexpressed EGF domain-specific O-GlcNAc transferase (EOGT) markedly enhanced the secretion of NOTCH1 EGF repeats in an enzyme activity-dependent manner.
36067866	10	17	theme	NOTCH	1513:1517	arg1	repeats					1523:1529	NOTCH EGF repeats	1513:1529	NOTCH EGF repeats	1513:1529	This study provides an experimental strategy to efficiently generate NOTCH EGF repeats by manipulating the expression of glycosyltransferases that alter the O-glycosylation of EGF domains.
36067866	5	18	theme	inhibitory	805:814	arg1	activity					816:823	potent Notch inhibitory activity	792:823	potent Notch inhibitory activity	792:823	Although full-length NOTCH EGF repeats exhibited potent Notch inhibitory activity, they were poorly produced in the transfected cells.
36067866	4	19	theme	NOTCH	532:536	arg1	molecule					649:656	a decoy molecule	641:656	a decoy molecule that competes for ligand binding and thus inhibits ligand-dependent Notch signaling	641:740	Therefore, the truncated NOTCH ectodomain, composed mainly of tandem repeats of epidermal growth factor-like (EGF) domains, serves as a decoy molecule that competes for ligand binding and thus inhibits ligand-dependent Notch signaling.
36067866	4	19	theme	NOTCH	532:536	arg1	ectodomain					538:547	the truncated NOTCH ectodomain	518:547	the truncated NOTCH ectodomain	518:547	Therefore, the truncated NOTCH ectodomain, composed mainly of tandem repeats of epidermal growth factor-like (EGF) domains, serves as a decoy molecule that competes for ligand binding and thus inhibits ligand-dependent Notch signaling.
36067866	10	20	theme	EGF	1620:1622	arg1	domains					1624:1630	EGF domains	1620:1630	EGF domains	1620:1630	This study provides an experimental strategy to efficiently generate NOTCH EGF repeats by manipulating the expression of glycosyltransferases that alter the O-glycosylation of EGF domains.
36067866	7	21	dep	EGF	1101:1103	arg1	EOGT					1143:1146	EOGT	1143:1146	EOGT	1143:1146	Our results in HEK293T cells revealed that, unlike the effect on endogenous NOTCH receptors, overexpressed EGF domain-specific O-GlcNAc transferase (EOGT) markedly enhanced the secretion of NOTCH1 EGF repeats in an enzyme activity-dependent manner.
36067866	7	21	dep	EGF	1101:1103	arg1	transferase					1130:1140	domain-specific O-GlcNAc transferase	1105:1140	overexpressed EGF domain-specific O-GlcNAc transferase (EOGT)	1087:1147	Our results in HEK293T cells revealed that, unlike the effect on endogenous NOTCH receptors, overexpressed EGF domain-specific O-GlcNAc transferase (EOGT) markedly enhanced the secretion of NOTCH1 EGF repeats in an enzyme activity-dependent manner.
36067866	5	22	theme	transfected	859:869	arg1	cells					871:875	the transfected cells	855:875	the transfected cells	855:875	Although full-length NOTCH EGF repeats exhibited potent Notch inhibitory activity, they were poorly produced in the transfected cells.
36067866	7	23	theme	activity-dependent	1216:1233	arg1	manner					1235:1240	an enzyme activity-dependent manner	1206:1240	an enzyme activity-dependent manner	1206:1240	Our results in HEK293T cells revealed that, unlike the effect on endogenous NOTCH receptors, overexpressed EGF domain-specific O-GlcNAc transferase (EOGT) markedly enhanced the secretion of NOTCH1 EGF repeats in an enzyme activity-dependent manner.
36067866	6	24	theme	EGF	913:915	arg1	glycosyltransferases					934:953	EGF domain-modifying glycosyltransferases	913:953	EGF domain-modifying glycosyltransferases	913:953	This study evaluated the effect of EGF domain-modifying glycosyltransferases on the secretion of NOTCH EGF repeats.
36067866	0	25	theme	Secretory	0:8	arg1	expression					10:19	Secretory expression	0:19	Secretory expression of mammalian NOTCH tandem epidermal growth factor-like repeats	0:82	Secretory expression of mammalian NOTCH tandem epidermal growth factor-like repeats based on increased O-glycosylation.
36067866	1	26	theme	cell-to-cell	212:223	arg1	communication					225:237	cell-to-cell communication	212:237	cell-to-cell communication during development	212:256	The Notch pathway represents evolutionarily conserved intercellular signaling essential for cell-to-cell communication during development.
36067866	8	27	theme	O-glucosyltransferase	1272:1292	arg1	co-expression					1247:1259	The co-expression	1243:1259	The co-expression of protein O-glucosyltransferase 1	1243:1294	The co-expression of protein O-glucosyltransferase 1 further manifested the effect of EOGT.
36067866	8	28	theme	protein	1264:1270	arg1	O-glucosyltransferase					1272:1292	protein O-glucosyltransferase 1	1264:1294	protein O-glucosyltransferase 1	1264:1294	The co-expression of protein O-glucosyltransferase 1 further manifested the effect of EOGT.
36067866	2	29	theme	cancer	372:377	arg1	strategy					389:396	a potential cancer treatment strategy	360:396	a potential cancer treatment strategy	360:396	Dysregulation of Notch signaling has been implicated in various diseases, and its control represents a potential cancer treatment strategy.
36067866	9	30	theme	glycopeptide	1415:1426	arg1	quantification					1428:1441	label-free glycopeptide quantification	1404:1441	label-free glycopeptide quantification	1404:1441	The resultant changes in O-glycosylation of NOTCH3 were evaluated by label-free glycopeptide quantification.
36067866	4	31	theme	Notch	726:730	arg1	signaling					732:740	ligand-dependent Notch signaling	709:740	ligand-dependent Notch signaling	709:740	Therefore, the truncated NOTCH ectodomain, composed mainly of tandem repeats of epidermal growth factor-like (EGF) domains, serves as a decoy molecule that competes for ligand binding and thus inhibits ligand-dependent Notch signaling.
36067866	3	32	theme	NOTCH	450:454	arg1	receptors					456:464	NOTCH receptors	450:464	NOTCH receptors	450:464	Notch signaling is initiated by the interaction of NOTCH receptors with their ligands on neighboring cells.
36067866	4	33	theme	EGF	617:619	arg1	domains					622:628	epidermal growth factor-like (EGF) domains	587:628	epidermal growth factor-like (EGF) domains	587:628	Therefore, the truncated NOTCH ectodomain, composed mainly of tandem repeats of epidermal growth factor-like (EGF) domains, serves as a decoy molecule that competes for ligand binding and thus inhibits ligand-dependent Notch signaling.
36067866	2	34	theme	potential	362:370	arg1	strategy					389:396	a potential cancer treatment strategy	360:396	a potential cancer treatment strategy	360:396	Dysregulation of Notch signaling has been implicated in various diseases, and its control represents a potential cancer treatment strategy.
36067866	3	35	theme	neighboring	488:498	arg1	cells					500:504	neighboring cells	488:504	neighboring cells	488:504	Notch signaling is initiated by the interaction of NOTCH receptors with their ligands on neighboring cells.
36067866	0	36	theme	mammalian	24:32	arg1	repeats					76:82	mammalian NOTCH tandem epidermal growth factor-like repeats	24:82	mammalian NOTCH tandem epidermal growth factor-like repeats	24:82	Secretory expression of mammalian NOTCH tandem epidermal growth factor-like repeats based on increased O-glycosylation.
36067866	5	37	theme	NOTCH	764:768	arg1	repeats					774:780	full-length NOTCH EGF repeats	752:780	full-length NOTCH EGF repeats	752:780	Although full-length NOTCH EGF repeats exhibited potent Notch inhibitory activity, they were poorly produced in the transfected cells.
36067866	4	38	theme	ligand	676:681	arg1	binding					683:689	ligand binding	676:689	ligand binding	676:689	Therefore, the truncated NOTCH ectodomain, composed mainly of tandem repeats of epidermal growth factor-like (EGF) domains, serves as a decoy molecule that competes for ligand binding and thus inhibits ligand-dependent Notch signaling.
36067866	3	39	with	interaction	435:445	arg1	ligands					477:483	their ligands	471:483	their ligands on neighboring cells	471:504	Notch signaling is initiated by the interaction of NOTCH receptors with their ligands on neighboring cells.
36067866	4	40	theme	domains	622:628	arg1	repeats					576:582	tandem repeats	569:582	tandem repeats of epidermal growth factor-like (EGF) domains	569:628	Therefore, the truncated NOTCH ectodomain, composed mainly of tandem repeats of epidermal growth factor-like (EGF) domains, serves as a decoy molecule that competes for ligand binding and thus inhibits ligand-dependent Notch signaling.
36067866	5	41	theme	EGF	770:772	arg1	repeats					774:780	full-length NOTCH EGF repeats	752:780	full-length NOTCH EGF repeats	752:780	Although full-length NOTCH EGF repeats exhibited potent Notch inhibitory activity, they were poorly produced in the transfected cells.
36067866	9	42	theme	resultant	1339:1347	arg1	changes					1349:1355	The resultant changes	1335:1355	The resultant changes in O-glycosylation of NOTCH3	1335:1384	The resultant changes in O-glycosylation of NOTCH3 were evaluated by label-free glycopeptide quantification.
36067866	9	43	gly	glycopeptide	1415:1426	arg2	glycopeptide					1415:1426	label-free glycopeptide quantification	1404:1441	label-free glycopeptide quantification	1404:1441	The resultant changes in O-glycosylation of NOTCH3 were evaluated by label-free glycopeptide quantification.
36067866	0	44	theme	tandem	40:45	arg1	repeats					76:82	mammalian NOTCH tandem epidermal growth factor-like repeats	24:82	mammalian NOTCH tandem epidermal growth factor-like repeats	24:82	Secretory expression of mammalian NOTCH tandem epidermal growth factor-like repeats based on increased O-glycosylation.
36067866	6	45	theme	glycosyltransferases	934:953	arg1	effect					903:908	the effect	899:908	the effect of EGF domain-modifying glycosyltransferases on the secretion of NOTCH EGF repeats	899:991	This study evaluated the effect of EGF domain-modifying glycosyltransferases on the secretion of NOTCH EGF repeats.
36067866	4	46	theme	ligand-dependent	709:724	arg1	signaling					732:740	ligand-dependent Notch signaling	709:740	ligand-dependent Notch signaling	709:740	Therefore, the truncated NOTCH ectodomain, composed mainly of tandem repeats of epidermal growth factor-like (EGF) domains, serves as a decoy molecule that competes for ligand binding and thus inhibits ligand-dependent Notch signaling.
36067866	0	47	theme	NOTCH	34:38	arg1	repeats					76:82	mammalian NOTCH tandem epidermal growth factor-like repeats	24:82	mammalian NOTCH tandem epidermal growth factor-like repeats	24:82	Secretory expression of mammalian NOTCH tandem epidermal growth factor-like repeats based on increased O-glycosylation.
36067866	4	48	theme	epidermal	587:595	arg1	domains					622:628	epidermal growth factor-like (EGF) domains	587:628	epidermal growth factor-like (EGF) domains	587:628	Therefore, the truncated NOTCH ectodomain, composed mainly of tandem repeats of epidermal growth factor-like (EGF) domains, serves as a decoy molecule that competes for ligand binding and thus inhibits ligand-dependent Notch signaling.
36067866	10	49	theme	domains	1624:1630	arg1	O-glycosylation					1601:1615	the O-glycosylation	1597:1615	the O-glycosylation of EGF domains	1597:1630	This study provides an experimental strategy to efficiently generate NOTCH EGF repeats by manipulating the expression of glycosyltransferases that alter the O-glycosylation of EGF domains.
36067866	4	50	theme	truncated	522:530	arg1	molecule					649:656	a decoy molecule	641:656	a decoy molecule that competes for ligand binding and thus inhibits ligand-dependent Notch signaling	641:740	Therefore, the truncated NOTCH ectodomain, composed mainly of tandem repeats of epidermal growth factor-like (EGF) domains, serves as a decoy molecule that competes for ligand binding and thus inhibits ligand-dependent Notch signaling.
36067866	4	50	theme	truncated	522:530	arg1	ectodomain					538:547	the truncated NOTCH ectodomain	518:547	the truncated NOTCH ectodomain	518:547	Therefore, the truncated NOTCH ectodomain, composed mainly of tandem repeats of epidermal growth factor-like (EGF) domains, serves as a decoy molecule that competes for ligand binding and thus inhibits ligand-dependent Notch signaling.
36067866	6	51	from	effect	903:908	arg1	secretion					962:970	the secretion	958:970	the secretion of NOTCH EGF repeats	958:991	This study evaluated the effect of EGF domain-modifying glycosyltransferases on the secretion of NOTCH EGF repeats.
36067866	9	52	gly	O-glycosylation	1360:1374	arg1	NOTCH3					1379:1384	NOTCH3	1379:1384	NOTCH3	1379:1384	The resultant changes in O-glycosylation of NOTCH3 were evaluated by label-free glycopeptide quantification.
36067866	0	53	theme	growth	57:62	arg1	repeats					76:82	mammalian NOTCH tandem epidermal growth factor-like repeats	24:82	mammalian NOTCH tandem epidermal growth factor-like repeats	24:82	Secretory expression of mammalian NOTCH tandem epidermal growth factor-like repeats based on increased O-glycosylation.
36067866	7	54	from	results	998:1004	arg1	cells					1017:1021	HEK293T cells	1009:1021	HEK293T cells	1009:1021	Our results in HEK293T cells revealed that, unlike the effect on endogenous NOTCH receptors, overexpressed EGF domain-specific O-GlcNAc transferase (EOGT) markedly enhanced the secretion of NOTCH1 EGF repeats in an enzyme activity-dependent manner.
36067866	7	55	theme	O-GlcNAc	1121:1128	arg1	EOGT					1143:1146	EOGT	1143:1146	EOGT	1143:1146	Our results in HEK293T cells revealed that, unlike the effect on endogenous NOTCH receptors, overexpressed EGF domain-specific O-GlcNAc transferase (EOGT) markedly enhanced the secretion of NOTCH1 EGF repeats in an enzyme activity-dependent manner.
36067866	7	55	theme	O-GlcNAc	1121:1128	arg1	transferase					1130:1140	domain-specific O-GlcNAc transferase	1105:1140	overexpressed EGF domain-specific O-GlcNAc transferase (EOGT)	1087:1147	Our results in HEK293T cells revealed that, unlike the effect on endogenous NOTCH receptors, overexpressed EGF domain-specific O-GlcNAc transferase (EOGT) markedly enhanced the secretion of NOTCH1 EGF repeats in an enzyme activity-dependent manner.
36067866	0	56	theme	factor-like	64:74	arg1	repeats					76:82	mammalian NOTCH tandem epidermal growth factor-like repeats	24:82	mammalian NOTCH tandem epidermal growth factor-like repeats	24:82	Secretory expression of mammalian NOTCH tandem epidermal growth factor-like repeats based on increased O-glycosylation.
36067866	2	57	theme	signaling	282:290	arg1	Dysregulation					259:271	Dysregulation	259:271	Dysregulation of Notch signaling	259:290	Dysregulation of Notch signaling has been implicated in various diseases, and its control represents a potential cancer treatment strategy.
36067866	7	58	theme	overexpressed	1087:1099	arg1	EGF					1101:1103	overexpressed EGF domain-specific O-GlcNAc transferase (EOGT)	1087:1147	overexpressed EGF domain-specific O-GlcNAc transferase (EOGT)	1087:1147	Our results in HEK293T cells revealed that, unlike the effect on endogenous NOTCH receptors, overexpressed EGF domain-specific O-GlcNAc transferase (EOGT) markedly enhanced the secretion of NOTCH1 EGF repeats in an enzyme activity-dependent manner.
36067866	1	59	theme	Notch	124:128	arg1	pathway					130:136	The Notch pathway	120:136	The Notch pathway	120:136	The Notch pathway represents evolutionarily conserved intercellular signaling essential for cell-to-cell communication during development.
36067866	0	60	theme	epidermal	47:55	arg1	repeats					76:82	mammalian NOTCH tandem epidermal growth factor-like repeats	24:82	mammalian NOTCH tandem epidermal growth factor-like repeats	24:82	Secretory expression of mammalian NOTCH tandem epidermal growth factor-like repeats based on increased O-glycosylation.
36067866	4	61	theme	factor-like	604:614	arg1	domains					622:628	epidermal growth factor-like (EGF) domains	587:628	epidermal growth factor-like (EGF) domains	587:628	Therefore, the truncated NOTCH ectodomain, composed mainly of tandem repeats of epidermal growth factor-like (EGF) domains, serves as a decoy molecule that competes for ligand binding and thus inhibits ligand-dependent Notch signaling.
36067866	2	62	theme	Notch	276:280	arg1	signaling					282:290	Notch signaling	276:290	Notch signaling	276:290	Dysregulation of Notch signaling has been implicated in various diseases, and its control represents a potential cancer treatment strategy.
36067866	7	63	theme	NOTCH	1070:1074	arg1	receptors					1076:1084	endogenous NOTCH receptors	1059:1084	endogenous NOTCH receptors	1059:1084	Our results in HEK293T cells revealed that, unlike the effect on endogenous NOTCH receptors, overexpressed EGF domain-specific O-GlcNAc transferase (EOGT) markedly enhanced the secretion of NOTCH1 EGF repeats in an enzyme activity-dependent manner.
36067866	6	64	theme	domain-modifying	917:932	arg1	glycosyltransferases					934:953	EGF domain-modifying glycosyltransferases	913:953	EGF domain-modifying glycosyltransferases	913:953	This study evaluated the effect of EGF domain-modifying glycosyltransferases on the secretion of NOTCH EGF repeats.
36067866	4	65	theme	growth	597:602	arg1	domains					622:628	epidermal growth factor-like (EGF) domains	587:628	epidermal growth factor-like (EGF) domains	587:628	Therefore, the truncated NOTCH ectodomain, composed mainly of tandem repeats of epidermal growth factor-like (EGF) domains, serves as a decoy molecule that competes for ligand binding and thus inhibits ligand-dependent Notch signaling.
36067866	7	66	theme	HEK293T	1009:1015	arg1	cells					1017:1021	HEK293T cells	1009:1021	HEK293T cells	1009:1021	Our results in HEK293T cells revealed that, unlike the effect on endogenous NOTCH receptors, overexpressed EGF domain-specific O-GlcNAc transferase (EOGT) markedly enhanced the secretion of NOTCH1 EGF repeats in an enzyme activity-dependent manner.
36067866	7	67	theme	enzyme	1209:1214	arg1	manner					1235:1240	an enzyme activity-dependent manner	1206:1240	an enzyme activity-dependent manner	1206:1240	Our results in HEK293T cells revealed that, unlike the effect on endogenous NOTCH receptors, overexpressed EGF domain-specific O-GlcNAc transferase (EOGT) markedly enhanced the secretion of NOTCH1 EGF repeats in an enzyme activity-dependent manner.
36067866	5	68	theme	full-length	752:762	arg1	repeats					774:780	full-length NOTCH EGF repeats	752:780	full-length NOTCH EGF repeats	752:780	Although full-length NOTCH EGF repeats exhibited potent Notch inhibitory activity, they were poorly produced in the transfected cells.
36067866	4	69	theme	tandem	569:574	arg1	repeats					576:582	tandem repeats	569:582	tandem repeats of epidermal growth factor-like (EGF) domains	569:628	Therefore, the truncated NOTCH ectodomain, composed mainly of tandem repeats of epidermal growth factor-like (EGF) domains, serves as a decoy molecule that competes for ligand binding and thus inhibits ligand-dependent Notch signaling.
36067866	2	70	theme	various	315:321	arg1	diseases					323:330	various diseases	315:330	various diseases	315:330	Dysregulation of Notch signaling has been implicated in various diseases, and its control represents a potential cancer treatment strategy.
36067866	2	71	theme	treatment	379:387	arg1	strategy					389:396	a potential cancer treatment strategy	360:396	a potential cancer treatment strategy	360:396	Dysregulation of Notch signaling has been implicated in various diseases, and its control represents a potential cancer treatment strategy.
36067866	4	72	theme	decoy	643:647	arg1	molecule					649:656	a decoy molecule	641:656	a decoy molecule that competes for ligand binding and thus inhibits ligand-dependent Notch signaling	641:740	Therefore, the truncated NOTCH ectodomain, composed mainly of tandem repeats of epidermal growth factor-like (EGF) domains, serves as a decoy molecule that competes for ligand binding and thus inhibits ligand-dependent Notch signaling.
36067866	4	72	theme	decoy	643:647	arg1	ectodomain					538:547	the truncated NOTCH ectodomain	518:547	the truncated NOTCH ectodomain	518:547	Therefore, the truncated NOTCH ectodomain, composed mainly of tandem repeats of epidermal growth factor-like (EGF) domains, serves as a decoy molecule that competes for ligand binding and thus inhibits ligand-dependent Notch signaling.
36067866	0	73	theme	repeats	76:82	arg1	expression					10:19	Secretory expression	0:19	Secretory expression of mammalian NOTCH tandem epidermal growth factor-like repeats	0:82	Secretory expression of mammalian NOTCH tandem epidermal growth factor-like repeats based on increased O-glycosylation.
36067866	7	74	theme	endogenous	1059:1068	arg1	receptors					1076:1084	endogenous NOTCH receptors	1059:1084	endogenous NOTCH receptors	1059:1084	Our results in HEK293T cells revealed that, unlike the effect on endogenous NOTCH receptors, overexpressed EGF domain-specific O-GlcNAc transferase (EOGT) markedly enhanced the secretion of NOTCH1 EGF repeats in an enzyme activity-dependent manner.
36067866	1	75	theme	conserved	164:172	arg1	signaling					188:196	evolutionarily conserved intercellular signaling	149:196	evolutionarily conserved intercellular signaling essential for cell-to-cell communication during development	149:256	The Notch pathway represents evolutionarily conserved intercellular signaling essential for cell-to-cell communication during development.
36067866	7	76	from	effect	1049:1054	arg1	receptors					1076:1084	endogenous NOTCH receptors	1059:1084	endogenous NOTCH receptors	1059:1084	Our results in HEK293T cells revealed that, unlike the effect on endogenous NOTCH receptors, overexpressed EGF domain-specific O-GlcNAc transferase (EOGT) markedly enhanced the secretion of NOTCH1 EGF repeats in an enzyme activity-dependent manner.
36067866	6	77	theme	EGF	981:983	arg1	repeats					985:991	NOTCH EGF repeats	975:991	NOTCH EGF repeats	975:991	This study evaluated the effect of EGF domain-modifying glycosyltransferases on the secretion of NOTCH EGF repeats.
36067866	3	78	theme	Notch	399:403	arg1	signaling					405:413	Notch signaling	399:413	Notch signaling	399:413	Notch signaling is initiated by the interaction of NOTCH receptors with their ligands on neighboring cells.
36067866	9	79	theme	NOTCH3	1379:1384	arg1	O-glycosylation					1360:1374	O-glycosylation	1360:1374	O-glycosylation of NOTCH3	1360:1384	The resultant changes in O-glycosylation of NOTCH3 were evaluated by label-free glycopeptide quantification.
36067866	1	80	theme	intercellular	174:186	arg1	signaling					188:196	evolutionarily conserved intercellular signaling	149:196	evolutionarily conserved intercellular signaling essential for cell-to-cell communication during development	149:256	The Notch pathway represents evolutionarily conserved intercellular signaling essential for cell-to-cell communication during development.
36067866	10	81	theme	glycosyltransferases	1565:1584	arg1	expression					1551:1560	the expression	1547:1560	the expression of glycosyltransferases that alter the O-glycosylation of EGF domains	1547:1630	This study provides an experimental strategy to efficiently generate NOTCH EGF repeats by manipulating the expression of glycosyltransferases that alter the O-glycosylation of EGF domains.
36067866	5	82	theme	Notch	799:803	arg1	activity					816:823	potent Notch inhibitory activity	792:823	potent Notch inhibitory activity	792:823	Although full-length NOTCH EGF repeats exhibited potent Notch inhibitory activity, they were poorly produced in the transfected cells.
24995978	5	0	dep	substrate	736:744	arg1	arrest					757:762	arrest	757:762	to arrest mitochondrial motility by mapping	754:796	We establish the mitochondrial motor-adaptor protein Milton as a required substrate for OGT to arrest mitochondrial motility by mapping and mutating the key O-GlcNAcylated serine residues.
24995978	5	0	dep	substrate	736:744	arg1	mutating					802:809	mutating	802:809	mutating the key O-GlcNAcylated serine residues	802:848	We establish the mitochondrial motor-adaptor protein Milton as a required substrate for OGT to arrest mitochondrial motility by mapping and mutating the key O-GlcNAcylated serine residues.
24995978	3	1	from	availability	423:434	arg1	form					443:446	the form	439:446	the form of extracellular glucose	439:471	Here, we report a molecular mechanism by which nutrient availability in the form of extracellular glucose and the enzyme O-GlcNAc Transferase (OGT), whose activity depends on glucose availability, regulates mitochondrial motility in neurons.
24995978	5	2	theme	mitochondrial	679:691	arg1	substrate					736:744	a required substrate	725:744	a required substrate for OGT to arrest mitochondrial motility by mapping and mutating the key O-GlcNAcylated serine residues	725:848	We establish the mitochondrial motor-adaptor protein Milton as a required substrate for OGT to arrest mitochondrial motility by mapping and mutating the key O-GlcNAcylated serine residues.
24995978	5	2	theme	mitochondrial	679:691	arg1	Milton					715:720	the mitochondrial motor-adaptor protein Milton	675:720	the mitochondrial motor-adaptor protein Milton	675:720	We establish the mitochondrial motor-adaptor protein Milton as a required substrate for OGT to arrest mitochondrial motility by mapping and mutating the key O-GlcNAcylated serine residues.
24995978	1	3	used	used	177:180	arg2	resources					117:125	substantial resources	105:125	substantial resources toward monitoring levels of nutrients that can be used for ATP generation by mitochondria	105:215	Cells allocate substantial resources toward monitoring levels of nutrients that can be used for ATP generation by mitochondria.
24995978	5	4	theme	motor-adaptor	693:705	arg1	substrate					736:744	a required substrate	725:744	a required substrate for OGT to arrest mitochondrial motility by mapping and mutating the key O-GlcNAcylated serine residues	725:848	We establish the mitochondrial motor-adaptor protein Milton as a required substrate for OGT to arrest mitochondrial motility by mapping and mutating the key O-GlcNAcylated serine residues.
24995978	5	4	theme	motor-adaptor	693:705	arg1	Milton					715:720	the mitochondrial motor-adaptor protein Milton	675:720	the mitochondrial motor-adaptor protein Milton	675:720	We establish the mitochondrial motor-adaptor protein Milton as a required substrate for OGT to arrest mitochondrial motility by mapping and mutating the key O-GlcNAcylated serine residues.
24995978	3	5	theme	glucose	542:548	arg1	availability					550:561	glucose availability	542:561	glucose availability	542:561	Here, we report a molecular mechanism by which nutrient availability in the form of extracellular glucose and the enzyme O-GlcNAc Transferase (OGT), whose activity depends on glucose availability, regulates mitochondrial motility in neurons.
24995978	3	6	theme	O-GlcNAc	488:495	arg1	Transferase					497:507	the enzyme O-GlcNAc Transferase	477:507	the enzyme O-GlcNAc Transferase (OGT)	477:513	Here, we report a molecular mechanism by which nutrient availability in the form of extracellular glucose and the enzyme O-GlcNAc Transferase (OGT), whose activity depends on glucose availability, regulates mitochondrial motility in neurons.
24995978	3	6	theme	O-GlcNAc	488:495	arg1	OGT					510:512	OGT	510:512	OGT	510:512	Here, we report a molecular mechanism by which nutrient availability in the form of extracellular glucose and the enzyme O-GlcNAc Transferase (OGT), whose activity depends on glucose availability, regulates mitochondrial motility in neurons.
24995978	5	7	theme	mitochondrial	764:776	arg1	motility					778:785	mitochondrial motility	764:785	mitochondrial motility by mapping	764:796	We establish the mitochondrial motor-adaptor protein Milton as a required substrate for OGT to arrest mitochondrial motility by mapping and mutating the key O-GlcNAcylated serine residues.
24995978	6	8	theme	extracellular	912:924	arg1	glucose					926:932	extracellular glucose	912:932	extracellular glucose	912:932	We find that the GlcNAcylation state of Milton is altered by extracellular glucose and that OGT alters mitochondrial motility in vivo.
24995978	0	9	theme	Milton	45:50	arg1	modification					52:63	Milton modification	45:63	Milton modification by O-GlcNAc transferase	45:87	Glucose regulates mitochondrial motility via Milton modification by O-GlcNAc transferase.
24995978	1	10	theme	ATP	186:188	arg1	generation					190:199	ATP generation	186:199	ATP generation by mitochondria	186:215	Cells allocate substantial resources toward monitoring levels of nutrients that can be used for ATP generation by mitochondria.
24995978	3	11	theme	molecular	385:393	arg1	mechanism					395:403	a molecular mechanism	383:403	a molecular mechanism by which nutrient availability in the form of extracellular glucose and the enzyme O-GlcNAc Transferase (OGT), whose activity depends on glucose availability, regulates mitochondrial motility in neurons	383:606	Here, we report a molecular mechanism by which nutrient availability in the form of extracellular glucose and the enzyme O-GlcNAc Transferase (OGT), whose activity depends on glucose availability, regulates mitochondrial motility in neurons.
24995978	1	12	theme	substantial	105:115	arg1	resources					117:125	substantial resources	105:125	substantial resources toward monitoring levels of nutrients that can be used for ATP generation by mitochondria	105:215	Cells allocate substantial resources toward monitoring levels of nutrients that can be used for ATP generation by mitochondria.
24995978	3	13	from	Transferase	497:507	arg1	form					443:446	the form	439:446	the form of extracellular glucose	439:471	Here, we report a molecular mechanism by which nutrient availability in the form of extracellular glucose and the enzyme O-GlcNAc Transferase (OGT), whose activity depends on glucose availability, regulates mitochondrial motility in neurons.
24995978	2	14	theme	complex	321:327	arg1	morphology					329:338	their complex morphology	315:338	their complex morphology	315:338	Among the many specialized cell types, neurons are particularly dependent on mitochondria due to their complex morphology and regional energy needs.
24995978	3	15	from	motility	588:595	arg1	neurons					600:606	neurons	600:606	neurons	600:606	Here, we report a molecular mechanism by which nutrient availability in the form of extracellular glucose and the enzyme O-GlcNAc Transferase (OGT), whose activity depends on glucose availability, regulates mitochondrial motility in neurons.
24995978	5	16	theme	required	727:734	arg1	substrate					736:744	a required substrate	725:744	a required substrate for OGT to arrest mitochondrial motility by mapping and mutating the key O-GlcNAcylated serine residues	725:848	We establish the mitochondrial motor-adaptor protein Milton as a required substrate for OGT to arrest mitochondrial motility by mapping and mutating the key O-GlcNAcylated serine residues.
24995978	5	16	theme	required	727:734	arg1	Milton					715:720	the mitochondrial motor-adaptor protein Milton	675:720	the mitochondrial motor-adaptor protein Milton	675:720	We establish the mitochondrial motor-adaptor protein Milton as a required substrate for OGT to arrest mitochondrial motility by mapping and mutating the key O-GlcNAcylated serine residues.
24995978	3	17	theme	mitochondrial	574:586	arg1	motility					588:595	mitochondrial motility	574:595	mitochondrial motility in neurons	574:606	Here, we report a molecular mechanism by which nutrient availability in the form of extracellular glucose and the enzyme O-GlcNAc Transferase (OGT), whose activity depends on glucose availability, regulates mitochondrial motility in neurons.
24995978	7	18	theme	nutrient	1116:1123	arg1	availability					1125:1136	nutrient availability	1116:1136	nutrient availability	1116:1136	Our findings suggest that, by dynamically regulating Milton GlcNAcylation, OGT tailors mitochondrial dynamics in neurons based on nutrient availability.
24995978	2	19	dep	energy	353:358	arg1	needs					360:364	needs	360:364	needs	360:364	Among the many specialized cell types, neurons are particularly dependent on mitochondria due to their complex morphology and regional energy needs.
24995978	4	20	theme	mitochondrial	638:650	arg1	motility					652:659	mitochondrial motility	638:659	mitochondrial motility	638:659	Activation of OGT diminishes mitochondrial motility.
24995978	3	21	theme	nutrient	414:421	arg1	availability					423:434	nutrient availability	414:434	nutrient availability in the form of extracellular glucose	414:471	Here, we report a molecular mechanism by which nutrient availability in the form of extracellular glucose and the enzyme O-GlcNAc Transferase (OGT), whose activity depends on glucose availability, regulates mitochondrial motility in neurons.
24995978	3	22	theme	extracellular	451:463	arg1	glucose					465:471	extracellular glucose	451:471	extracellular glucose	451:471	Here, we report a molecular mechanism by which nutrient availability in the form of extracellular glucose and the enzyme O-GlcNAc Transferase (OGT), whose activity depends on glucose availability, regulates mitochondrial motility in neurons.
24995978	5	23	theme	key	815:817	arg1	residues					841:848	the key O-GlcNAcylated serine residues	811:848	the key O-GlcNAcylated serine residues	811:848	We establish the mitochondrial motor-adaptor protein Milton as a required substrate for OGT to arrest mitochondrial motility by mapping and mutating the key O-GlcNAcylated serine residues.
24995978	6	24	theme	Milton	891:896	arg1	state					882:886	the GlcNAcylation state	864:886	the GlcNAcylation state of Milton	864:896	We find that the GlcNAcylation state of Milton is altered by extracellular glucose and that OGT alters mitochondrial motility in vivo.
24995978	2	25	theme	cell	245:248	arg1	types					250:254	the many specialized cell types	224:254	the many specialized cell types	224:254	Among the many specialized cell types, neurons are particularly dependent on mitochondria due to their complex morphology and regional energy needs.
24995978	3	26	theme	glucose	465:471	arg1	form					443:446	the form	439:446	the form of extracellular glucose	439:471	Here, we report a molecular mechanism by which nutrient availability in the form of extracellular glucose and the enzyme O-GlcNAc Transferase (OGT), whose activity depends on glucose availability, regulates mitochondrial motility in neurons.
24995978	5	27	theme	O-GlcNAcylated	819:832	arg1	residues					841:848	the key O-GlcNAcylated serine residues	811:848	the key O-GlcNAcylated serine residues	811:848	We establish the mitochondrial motor-adaptor protein Milton as a required substrate for OGT to arrest mitochondrial motility by mapping and mutating the key O-GlcNAcylated serine residues.
24995978	5	28	theme	protein	707:713	arg1	substrate					736:744	a required substrate	725:744	a required substrate for OGT to arrest mitochondrial motility by mapping and mutating the key O-GlcNAcylated serine residues	725:848	We establish the mitochondrial motor-adaptor protein Milton as a required substrate for OGT to arrest mitochondrial motility by mapping and mutating the key O-GlcNAcylated serine residues.
24995978	5	28	theme	protein	707:713	arg1	Milton					715:720	the mitochondrial motor-adaptor protein Milton	675:720	the mitochondrial motor-adaptor protein Milton	675:720	We establish the mitochondrial motor-adaptor protein Milton as a required substrate for OGT to arrest mitochondrial motility by mapping and mutating the key O-GlcNAcylated serine residues.
24995978	2	29	theme	specialized	233:243	arg1	types					250:254	the many specialized cell types	224:254	the many specialized cell types	224:254	Among the many specialized cell types, neurons are particularly dependent on mitochondria due to their complex morphology and regional energy needs.
24995978	1	30	theme	monitoring	134:143	arg1	levels					145:150	monitoring levels	134:150	monitoring levels of nutrients	134:163	Cells allocate substantial resources toward monitoring levels of nutrients that can be used for ATP generation by mitochondria.
24995978	5	31	theme	serine	834:839	arg1	residues					841:848	the key O-GlcNAcylated serine residues	811:848	the key O-GlcNAcylated serine residues	811:848	We establish the mitochondrial motor-adaptor protein Milton as a required substrate for OGT to arrest mitochondrial motility by mapping and mutating the key O-GlcNAcylated serine residues.
24995978	2	32	theme	many	228:231	arg1	types					250:254	the many specialized cell types	224:254	the many specialized cell types	224:254	Among the many specialized cell types, neurons are particularly dependent on mitochondria due to their complex morphology and regional energy needs.
24995978	7	33	theme	Milton	1039:1044	arg1	GlcNAcylation					1046:1058	dynamically regulating Milton GlcNAcylation	1016:1058	dynamically regulating Milton GlcNAcylation	1016:1058	Our findings suggest that, by dynamically regulating Milton GlcNAcylation, OGT tailors mitochondrial dynamics in neurons based on nutrient availability.
24995978	6	34	theme	GlcNAcylation	868:880	arg1	state					882:886	the GlcNAcylation state	864:886	the GlcNAcylation state of Milton	864:896	We find that the GlcNAcylation state of Milton is altered by extracellular glucose and that OGT alters mitochondrial motility in vivo.
24995978	2	35	theme	regional	344:351	arg1	energy					353:358	regional energy needs	344:364	regional energy needs	344:364	Among the many specialized cell types, neurons are particularly dependent on mitochondria due to their complex morphology and regional energy needs.
24995978	7	36	theme	mitochondrial	1073:1085	arg1	dynamics					1087:1094	mitochondrial dynamics	1073:1094	mitochondrial dynamics in neurons based on nutrient availability	1073:1136	Our findings suggest that, by dynamically regulating Milton GlcNAcylation, OGT tailors mitochondrial dynamics in neurons based on nutrient availability.
24995978	1	37	theme	nutrients	155:163	arg1	levels					145:150	monitoring levels	134:150	monitoring levels of nutrients	134:163	Cells allocate substantial resources toward monitoring levels of nutrients that can be used for ATP generation by mitochondria.
24995978	3	38	theme	enzyme	481:486	arg1	Transferase					497:507	the enzyme O-GlcNAc Transferase	477:507	the enzyme O-GlcNAc Transferase (OGT)	477:513	Here, we report a molecular mechanism by which nutrient availability in the form of extracellular glucose and the enzyme O-GlcNAc Transferase (OGT), whose activity depends on glucose availability, regulates mitochondrial motility in neurons.
24995978	3	38	theme	enzyme	481:486	arg1	OGT					510:512	OGT	510:512	OGT	510:512	Here, we report a molecular mechanism by which nutrient availability in the form of extracellular glucose and the enzyme O-GlcNAc Transferase (OGT), whose activity depends on glucose availability, regulates mitochondrial motility in neurons.
24995978	7	39	theme	regulating	1028:1037	arg1	GlcNAcylation					1046:1058	dynamically regulating Milton GlcNAcylation	1016:1058	dynamically regulating Milton GlcNAcylation	1016:1058	Our findings suggest that, by dynamically regulating Milton GlcNAcylation, OGT tailors mitochondrial dynamics in neurons based on nutrient availability.
24995978	7	40	from	dynamics	1087:1094	arg1	neurons					1099:1105	neurons	1099:1105	neurons based on nutrient availability	1099:1136	Our findings suggest that, by dynamically regulating Milton GlcNAcylation, OGT tailors mitochondrial dynamics in neurons based on nutrient availability.
24995978	0	41	theme	O-GlcNAc	68:75	arg1	transferase					77:87	O-GlcNAc transferase	68:87	O-GlcNAc transferase	68:87	Glucose regulates mitochondrial motility via Milton modification by O-GlcNAc transferase.
24995978	6	42	theme	mitochondrial	954:966	arg1	motility					968:975	mitochondrial motility	954:975	mitochondrial motility	954:975	We find that the GlcNAcylation state of Milton is altered by extracellular glucose and that OGT alters mitochondrial motility in vivo.
24995978	0	43	theme	mitochondrial	18:30	arg1	motility					32:39	mitochondrial motility	18:39	mitochondrial motility	18:39	Glucose regulates mitochondrial motility via Milton modification by O-GlcNAc transferase.
24995978	4	44	theme	OGT	623:625	arg1	Activation					609:618	Activation	609:618	Activation of OGT	609:625	Activation of OGT diminishes mitochondrial motility.
33843053	0	0	theme	FOXA2	96:100	arg1	stability					102:110	FOXA2 stability	96:110	FOXA2 stability	96:110	O-GlcNAcylation promotes the migratory ability of hepatocellular carcinoma cells via regulating FOXA2 stability and transcriptional activity.
33843053	1	1	theme	cell	367:370	arg1	motility					372:379	cell motility	367:379	cell motility	367:379	O-GlcNAcylation is a posttranslational modification that regulates numerous nuclear and cytoplasmic proteins and is emerging as a key regulator of various biological processes, such as transcription, signal transduction, and cell motility.
33843053	4	2	theme	HCC	885:887	arg1	tissues					889:895	HCC tissues	885:895	HCC tissues	885:895	Opposite FOXA2 and OGT expression tendency were observed in HCC tissues, and lower FOXA2 levels predicted a poor prognosis in HCC patients.
33843053	8	3	theme	gene	1499:1502	arg1	E-cadherin					1504:1513	FOXA2 downstream target gene E-cadherin	1475:1513	FOXA2 downstream target gene E-cadherin	1475:1513	O-GlcNAcylation decreased the transcription of FOXA2 downstream target gene E-cadherin and it ultimately promoted O-GlcNAcylation-mediated HCC cell migration and invasion.
33843053	8	4	theme	cell	1571:1574	arg1	migration					1576:1584	O-GlcNAcylation-mediated HCC cell migration	1542:1584	O-GlcNAcylation-mediated HCC cell migration	1542:1584	O-GlcNAcylation decreased the transcription of FOXA2 downstream target gene E-cadherin and it ultimately promoted O-GlcNAcylation-mediated HCC cell migration and invasion.
33843053	5	5	theme	migratory	1081:1089	arg1	ability					1091:1097	cell migratory ability	1076:1097	cell migratory ability	1076:1097	The reduction of FOXA2 in HCC cells was found to be inversely correlated with the cellular O-GlcNAcylation and cell migratory ability.
33843053	1	6	theme	various	289:295	arg1	motility					372:379	cell motility	367:379	cell motility	367:379	O-GlcNAcylation is a posttranslational modification that regulates numerous nuclear and cytoplasmic proteins and is emerging as a key regulator of various biological processes, such as transcription, signal transduction, and cell motility.
33843053	1	6	theme	various	289:295	arg1	transcription					327:339	transcription	327:339	transcription	327:339	O-GlcNAcylation is a posttranslational modification that regulates numerous nuclear and cytoplasmic proteins and is emerging as a key regulator of various biological processes, such as transcription, signal transduction, and cell motility.
33843053	1	6	theme	various	289:295	arg1	transduction					349:360	signal transduction	342:360	signal transduction	342:360	O-GlcNAcylation is a posttranslational modification that regulates numerous nuclear and cytoplasmic proteins and is emerging as a key regulator of various biological processes, such as transcription, signal transduction, and cell motility.
33843053	1	6	theme	various	289:295	arg1	processes					308:316	various biological processes	289:316	various biological processes	289:316	O-GlcNAcylation is a posttranslational modification that regulates numerous nuclear and cytoplasmic proteins and is emerging as a key regulator of various biological processes, such as transcription, signal transduction, and cell motility.
33843053	4	7	theme	HCC	951:953	arg1	patients					955:962	HCC patients	951:962	HCC patients	951:962	Opposite FOXA2 and OGT expression tendency were observed in HCC tissues, and lower FOXA2 levels predicted a poor prognosis in HCC patients.
33843053	3	8	theme	HCC	712:714	arg1	developing					716:725	HCC developing	712:725	HCC developing	712:725	In this study, we demonstrated that forkhead box protein A2 (FOXA2), an essential transcription factor for liver homeostasis and HCC developing, was O-GlcNAcylated by O-GlcNAc transferase (OGT) and regulates HCC cells migration and invasion.
33843053	9	9	theme	HCC	1733:1735	arg1	metastasis					1737:1746	HCC metastasis	1733:1746	HCC metastasis	1733:1746	The results provide insights into the role of O-GlcNAcylation in regulating FOXA2 activity and suggest its important implications in HCC metastasis.
33843053	4	10	located	observed	873:880	arg2	FOXA2					834:838	Opposite FOXA2 and OGT expression tendency	825:866	FOXA2	834:838	Opposite FOXA2 and OGT expression tendency were observed in HCC tissues, and lower FOXA2 levels predicted a poor prognosis in HCC patients.
33843053	4	10	located	observed	873:880	arg1	tissues					889:895	HCC tissues	885:895	HCC tissues	885:895	Opposite FOXA2 and OGT expression tendency were observed in HCC tissues, and lower FOXA2 levels predicted a poor prognosis in HCC patients.
33843053	4	10	located	observed	873:880	arg2	tendency					859:866	Opposite FOXA2 and OGT expression tendency	825:866	tendency	859:866	Opposite FOXA2 and OGT expression tendency were observed in HCC tissues, and lower FOXA2 levels predicted a poor prognosis in HCC patients.
33843053	1	11	theme	biological	297:306	arg1	motility					372:379	cell motility	367:379	cell motility	367:379	O-GlcNAcylation is a posttranslational modification that regulates numerous nuclear and cytoplasmic proteins and is emerging as a key regulator of various biological processes, such as transcription, signal transduction, and cell motility.
33843053	1	11	theme	biological	297:306	arg1	transcription					327:339	transcription	327:339	transcription	327:339	O-GlcNAcylation is a posttranslational modification that regulates numerous nuclear and cytoplasmic proteins and is emerging as a key regulator of various biological processes, such as transcription, signal transduction, and cell motility.
33843053	1	11	theme	biological	297:306	arg1	transduction					349:360	signal transduction	342:360	signal transduction	342:360	O-GlcNAcylation is a posttranslational modification that regulates numerous nuclear and cytoplasmic proteins and is emerging as a key regulator of various biological processes, such as transcription, signal transduction, and cell motility.
33843053	1	11	theme	biological	297:306	arg1	processes					308:316	various biological processes	289:316	various biological processes	289:316	O-GlcNAcylation is a posttranslational modification that regulates numerous nuclear and cytoplasmic proteins and is emerging as a key regulator of various biological processes, such as transcription, signal transduction, and cell motility.
33843053	9	12	from	implications	1717:1728	arg1	metastasis					1737:1746	HCC metastasis	1733:1746	HCC metastasis	1733:1746	The results provide insights into the role of O-GlcNAcylation in regulating FOXA2 activity and suggest its important implications in HCC metastasis.
33843053	1	13	theme	processes	308:316	arg1	regulator					276:284	a key regulator	270:284	a key regulator of various biological processes, such as transcription, signal transduction, and cell motility	270:379	O-GlcNAcylation is a posttranslational modification that regulates numerous nuclear and cytoplasmic proteins and is emerging as a key regulator of various biological processes, such as transcription, signal transduction, and cell motility.
33843053	3	14	theme	O-GlcNAc	750:757	arg1	OGT					772:774	OGT	772:774	OGT	772:774	In this study, we demonstrated that forkhead box protein A2 (FOXA2), an essential transcription factor for liver homeostasis and HCC developing, was O-GlcNAcylated by O-GlcNAc transferase (OGT) and regulates HCC cells migration and invasion.
33843053	3	14	theme	O-GlcNAc	750:757	arg1	transferase					759:769	O-GlcNAc transferase	750:769	O-GlcNAc transferase (OGT)	750:775	In this study, we demonstrated that forkhead box protein A2 (FOXA2), an essential transcription factor for liver homeostasis and HCC developing, was O-GlcNAcylated by O-GlcNAc transferase (OGT) and regulates HCC cells migration and invasion.
33843053	1	15	theme	numerous	209:216	arg1	proteins					242:249	numerous nuclear and cytoplasmic proteins	209:249	numerous nuclear and cytoplasmic proteins	209:249	O-GlcNAcylation is a posttranslational modification that regulates numerous nuclear and cytoplasmic proteins and is emerging as a key regulator of various biological processes, such as transcription, signal transduction, and cell motility.
33843053	0	16	theme	transcriptional	116:130	arg1	activity					132:139	transcriptional activity	116:139	transcriptional activity	116:139	O-GlcNAcylation promotes the migratory ability of hepatocellular carcinoma cells via regulating FOXA2 stability and transcriptional activity.
33843053	4	17	theme	expression	848:857	arg1	tendency					859:866	Opposite FOXA2 and OGT expression tendency	825:866	tendency	859:866	Opposite FOXA2 and OGT expression tendency were observed in HCC tissues, and lower FOXA2 levels predicted a poor prognosis in HCC patients.
33843053	9	18	theme	important	1707:1715	arg1	implications					1717:1728	its important implications	1703:1728	its important implications in HCC metastasis	1703:1746	The results provide insights into the role of O-GlcNAcylation in regulating FOXA2 activity and suggest its important implications in HCC metastasis.
33843053	5	19	theme	FOXA2	982:986	arg1	reduction					969:977	The reduction	965:977	The reduction of FOXA2 in HCC cells	965:999	The reduction of FOXA2 in HCC cells was found to be inversely correlated with the cellular O-GlcNAcylation and cell migratory ability.
33843053	1	20	theme	nuclear	218:224	arg1	proteins					242:249	numerous nuclear and cytoplasmic proteins	209:249	numerous nuclear and cytoplasmic proteins	209:249	O-GlcNAcylation is a posttranslational modification that regulates numerous nuclear and cytoplasmic proteins and is emerging as a key regulator of various biological processes, such as transcription, signal transduction, and cell motility.
33843053	3	21	theme	transcription	665:677	arg1	A2					640:641	forkhead box protein A2	619:641	forkhead box protein A2 (FOXA2)	619:649	In this study, we demonstrated that forkhead box protein A2 (FOXA2), an essential transcription factor for liver homeostasis and HCC developing, was O-GlcNAcylated by O-GlcNAc transferase (OGT) and regulates HCC cells migration and invasion.
33843053	3	21	theme	transcription	665:677	arg1	factor					679:684	an essential transcription factor	652:684	an essential transcription factor for liver homeostasis and HCC developing	652:725	In this study, we demonstrated that forkhead box protein A2 (FOXA2), an essential transcription factor for liver homeostasis and HCC developing, was O-GlcNAcylated by O-GlcNAc transferase (OGT) and regulates HCC cells migration and invasion.
33843053	3	22	dep	cells	795:799	arg1	invasion					815:822	invasion	815:822	invasion	815:822	In this study, we demonstrated that forkhead box protein A2 (FOXA2), an essential transcription factor for liver homeostasis and HCC developing, was O-GlcNAcylated by O-GlcNAc transferase (OGT) and regulates HCC cells migration and invasion.
33843053	3	22	dep	cells	795:799	arg1	migration					801:809	migration	801:809	migration	801:809	In this study, we demonstrated that forkhead box protein A2 (FOXA2), an essential transcription factor for liver homeostasis and HCC developing, was O-GlcNAcylated by O-GlcNAc transferase (OGT) and regulates HCC cells migration and invasion.
33843053	3	22	dep	cells	795:799	arg1	cells					795:799	HCC cells migration and invasion	791:822	HCC cells migration and invasion	791:822	In this study, we demonstrated that forkhead box protein A2 (FOXA2), an essential transcription factor for liver homeostasis and HCC developing, was O-GlcNAcylated by O-GlcNAc transferase (OGT) and regulates HCC cells migration and invasion.
33843053	2	23	theme	elevated	426:433	arg1	levels					435:440	elevated levels	426:440	elevated levels of global O-GlcNAcylation	426:466	Although increasing evidence has shown that elevated levels of global O-GlcNAcylation are linked to the metastasis in hepatocellular carcinoma (HCC) cells, the underlying mechanism is still ambiguous.
33843053	5	24	theme	cellular	1047:1054	arg1	O-GlcNAcylation					1056:1070	the cellular O-GlcNAcylation	1043:1070	the cellular O-GlcNAcylation	1043:1070	The reduction of FOXA2 in HCC cells was found to be inversely correlated with the cellular O-GlcNAcylation and cell migratory ability.
33843053	3	25	theme	liver	690:694	arg1	homeostasis					696:706	liver homeostasis	690:706	liver homeostasis	690:706	In this study, we demonstrated that forkhead box protein A2 (FOXA2), an essential transcription factor for liver homeostasis and HCC developing, was O-GlcNAcylated by O-GlcNAc transferase (OGT) and regulates HCC cells migration and invasion.
33843053	1	26	theme	cytoplasmic	230:240	arg1	proteins					242:249	numerous nuclear and cytoplasmic proteins	209:249	numerous nuclear and cytoplasmic proteins	209:249	O-GlcNAcylation is a posttranslational modification that regulates numerous nuclear and cytoplasmic proteins and is emerging as a key regulator of various biological processes, such as transcription, signal transduction, and cell motility.
33843053	0	27	theme	migratory	29:37	arg1	ability					39:45	the migratory ability	25:45	the migratory ability of hepatocellular carcinoma cells	25:79	O-GlcNAcylation promotes the migratory ability of hepatocellular carcinoma cells via regulating FOXA2 stability and transcriptional activity.
33843053	8	28	theme	target	1492:1497	arg1	E-cadherin					1504:1513	FOXA2 downstream target gene E-cadherin	1475:1513	FOXA2 downstream target gene E-cadherin	1475:1513	O-GlcNAcylation decreased the transcription of FOXA2 downstream target gene E-cadherin and it ultimately promoted O-GlcNAcylation-mediated HCC cell migration and invasion.
33843053	6	29	theme	FOXA2	1230:1234	arg1	degradation					1215:1225	the ubiquitination degradation	1196:1225	the ubiquitination degradation of FOXA2	1196:1234	Notably, we found that FOXA2 was modified by O-GlcNAcylation and that O-GlcNAcylation activated the ubiquitination degradation of FOXA2 in highly metastatic HCC cells.
33843053	6	30	theme	metastatic	1246:1255	arg1	cells					1261:1265	highly metastatic HCC cells	1239:1265	highly metastatic HCC cells	1239:1265	Notably, we found that FOXA2 was modified by O-GlcNAcylation and that O-GlcNAcylation activated the ubiquitination degradation of FOXA2 in highly metastatic HCC cells.
33843053	7	31	theme	nuclear	1316:1322	arg1	capability					1337:1346	FOXA2 nuclear localization capability	1310:1346	FOXA2 nuclear localization capability	1310:1346	Although this modification did not affect FOXA2 nuclear localization capability, O-GlcNAcylation on FOXA2 was key for attenuating FOXA2-mediated transcription.
33843053	9	32	theme	O-GlcNAcylation	1646:1660	arg1	role					1638:1641	the role	1634:1641	the role of O-GlcNAcylation in regulating FOXA2 activity	1634:1689	The results provide insights into the role of O-GlcNAcylation in regulating FOXA2 activity and suggest its important implications in HCC metastasis.
33843053	4	33	from	prognosis	938:946	arg1	patients					955:962	HCC patients	951:962	HCC patients	951:962	Opposite FOXA2 and OGT expression tendency were observed in HCC tissues, and lower FOXA2 levels predicted a poor prognosis in HCC patients.
33843053	3	34	theme	essential	655:663	arg1	A2					640:641	forkhead box protein A2	619:641	forkhead box protein A2 (FOXA2)	619:649	In this study, we demonstrated that forkhead box protein A2 (FOXA2), an essential transcription factor for liver homeostasis and HCC developing, was O-GlcNAcylated by O-GlcNAc transferase (OGT) and regulates HCC cells migration and invasion.
33843053	3	34	theme	essential	655:663	arg1	factor					679:684	an essential transcription factor	652:684	an essential transcription factor for liver homeostasis and HCC developing	652:725	In this study, we demonstrated that forkhead box protein A2 (FOXA2), an essential transcription factor for liver homeostasis and HCC developing, was O-GlcNAcylated by O-GlcNAc transferase (OGT) and regulates HCC cells migration and invasion.
33843053	7	35	theme	localization	1324:1335	arg1	capability					1337:1346	FOXA2 nuclear localization capability	1310:1346	FOXA2 nuclear localization capability	1310:1346	Although this modification did not affect FOXA2 nuclear localization capability, O-GlcNAcylation on FOXA2 was key for attenuating FOXA2-mediated transcription.
33843053	7	36	theme	FOXA2	1310:1314	arg1	capability					1337:1346	FOXA2 nuclear localization capability	1310:1346	FOXA2 nuclear localization capability	1310:1346	Although this modification did not affect FOXA2 nuclear localization capability, O-GlcNAcylation on FOXA2 was key for attenuating FOXA2-mediated transcription.
33843053	5	37	from	reduction	969:977	arg1	cells					995:999	HCC cells	991:999	HCC cells	991:999	The reduction of FOXA2 in HCC cells was found to be inversely correlated with the cellular O-GlcNAcylation and cell migratory ability.
33843053	2	38	attach	linked	472:477	arg1	metastasis					486:495	the metastasis	482:495	the metastasis	482:495	Although increasing evidence has shown that elevated levels of global O-GlcNAcylation are linked to the metastasis in hepatocellular carcinoma (HCC) cells, the underlying mechanism is still ambiguous.
33843053	2	38	attach	linked	472:477	arg3	cells					531:535	hepatocellular carcinoma (HCC) cells	500:535	hepatocellular carcinoma (HCC) cells	500:535	Although increasing evidence has shown that elevated levels of global O-GlcNAcylation are linked to the metastasis in hepatocellular carcinoma (HCC) cells, the underlying mechanism is still ambiguous.
33843053	2	38	attach	linked	472:477	arg2	levels					435:440	elevated levels	426:440	elevated levels of global O-GlcNAcylation	426:466	Although increasing evidence has shown that elevated levels of global O-GlcNAcylation are linked to the metastasis in hepatocellular carcinoma (HCC) cells, the underlying mechanism is still ambiguous.
33843053	3	39	theme	box	628:630	arg1	FOXA2					644:648	FOXA2	644:648	FOXA2	644:648	In this study, we demonstrated that forkhead box protein A2 (FOXA2), an essential transcription factor for liver homeostasis and HCC developing, was O-GlcNAcylated by O-GlcNAc transferase (OGT) and regulates HCC cells migration and invasion.
33843053	3	39	theme	box	628:630	arg1	factor					679:684	an essential transcription factor	652:684	an essential transcription factor for liver homeostasis and HCC developing	652:725	In this study, we demonstrated that forkhead box protein A2 (FOXA2), an essential transcription factor for liver homeostasis and HCC developing, was O-GlcNAcylated by O-GlcNAc transferase (OGT) and regulates HCC cells migration and invasion.
33843053	3	39	theme	box	628:630	arg1	A2					640:641	forkhead box protein A2	619:641	forkhead box protein A2 (FOXA2)	619:649	In this study, we demonstrated that forkhead box protein A2 (FOXA2), an essential transcription factor for liver homeostasis and HCC developing, was O-GlcNAcylated by O-GlcNAc transferase (OGT) and regulates HCC cells migration and invasion.
33843053	2	40	theme	O-GlcNAcylation	452:466	arg1	levels					435:440	elevated levels	426:440	elevated levels of global O-GlcNAcylation	426:466	Although increasing evidence has shown that elevated levels of global O-GlcNAcylation are linked to the metastasis in hepatocellular carcinoma (HCC) cells, the underlying mechanism is still ambiguous.
33843053	3	41	theme	HCC	791:793	arg1	invasion					815:822	invasion	815:822	invasion	815:822	In this study, we demonstrated that forkhead box protein A2 (FOXA2), an essential transcription factor for liver homeostasis and HCC developing, was O-GlcNAcylated by O-GlcNAc transferase (OGT) and regulates HCC cells migration and invasion.
33843053	3	41	theme	HCC	791:793	arg1	migration					801:809	migration	801:809	migration	801:809	In this study, we demonstrated that forkhead box protein A2 (FOXA2), an essential transcription factor for liver homeostasis and HCC developing, was O-GlcNAcylated by O-GlcNAc transferase (OGT) and regulates HCC cells migration and invasion.
33843053	3	41	theme	HCC	791:793	arg1	cells					795:799	HCC cells migration and invasion	791:822	HCC cells migration and invasion	791:822	In this study, we demonstrated that forkhead box protein A2 (FOXA2), an essential transcription factor for liver homeostasis and HCC developing, was O-GlcNAcylated by O-GlcNAc transferase (OGT) and regulates HCC cells migration and invasion.
33843053	4	42	theme	poor	933:936	arg1	prognosis					938:946	a poor prognosis	931:946	a poor prognosis in HCC patients	931:962	Opposite FOXA2 and OGT expression tendency were observed in HCC tissues, and lower FOXA2 levels predicted a poor prognosis in HCC patients.
33843053	5	43	theme	cell	1076:1079	arg1	ability					1091:1097	cell migratory ability	1076:1097	cell migratory ability	1076:1097	The reduction of FOXA2 in HCC cells was found to be inversely correlated with the cellular O-GlcNAcylation and cell migratory ability.
33843053	3	44	theme	protein	632:638	arg1	FOXA2					644:648	FOXA2	644:648	FOXA2	644:648	In this study, we demonstrated that forkhead box protein A2 (FOXA2), an essential transcription factor for liver homeostasis and HCC developing, was O-GlcNAcylated by O-GlcNAc transferase (OGT) and regulates HCC cells migration and invasion.
33843053	3	44	theme	protein	632:638	arg1	factor					679:684	an essential transcription factor	652:684	an essential transcription factor for liver homeostasis and HCC developing	652:725	In this study, we demonstrated that forkhead box protein A2 (FOXA2), an essential transcription factor for liver homeostasis and HCC developing, was O-GlcNAcylated by O-GlcNAc transferase (OGT) and regulates HCC cells migration and invasion.
33843053	3	44	theme	protein	632:638	arg1	A2					640:641	forkhead box protein A2	619:641	forkhead box protein A2 (FOXA2)	619:649	In this study, we demonstrated that forkhead box protein A2 (FOXA2), an essential transcription factor for liver homeostasis and HCC developing, was O-GlcNAcylated by O-GlcNAc transferase (OGT) and regulates HCC cells migration and invasion.
33843053	7	45	theme	FOXA2-mediated	1398:1411	arg1	transcription					1413:1425	FOXA2-mediated transcription	1398:1425	FOXA2-mediated transcription	1398:1425	Although this modification did not affect FOXA2 nuclear localization capability, O-GlcNAcylation on FOXA2 was key for attenuating FOXA2-mediated transcription.
33843053	2	46	theme	underlying	542:551	arg1	mechanism					553:561	the underlying mechanism	538:561	the underlying mechanism	538:561	Although increasing evidence has shown that elevated levels of global O-GlcNAcylation are linked to the metastasis in hepatocellular carcinoma (HCC) cells, the underlying mechanism is still ambiguous.
33843053	2	46	theme	underlying	542:551	arg1	ambiguous					572:580	ambiguous	572:580	ambiguous	572:580	Although increasing evidence has shown that elevated levels of global O-GlcNAcylation are linked to the metastasis in hepatocellular carcinoma (HCC) cells, the underlying mechanism is still ambiguous.
33843053	2	47	theme	carcinoma	515:523	arg1	cells					531:535	hepatocellular carcinoma (HCC) cells	500:535	hepatocellular carcinoma (HCC) cells	500:535	Although increasing evidence has shown that elevated levels of global O-GlcNAcylation are linked to the metastasis in hepatocellular carcinoma (HCC) cells, the underlying mechanism is still ambiguous.
33843053	1	48	theme	signal	342:347	arg1	transduction					349:360	signal transduction	342:360	signal transduction	342:360	O-GlcNAcylation is a posttranslational modification that regulates numerous nuclear and cytoplasmic proteins and is emerging as a key regulator of various biological processes, such as transcription, signal transduction, and cell motility.
33843053	4	49	theme	lower	902:906	arg1	levels					914:919	lower FOXA2 levels	902:919	lower FOXA2 levels	902:919	Opposite FOXA2 and OGT expression tendency were observed in HCC tissues, and lower FOXA2 levels predicted a poor prognosis in HCC patients.
33843053	0	50	theme	cells	75:79	arg1	ability					39:45	the migratory ability	25:45	the migratory ability of hepatocellular carcinoma cells	25:79	O-GlcNAcylation promotes the migratory ability of hepatocellular carcinoma cells via regulating FOXA2 stability and transcriptional activity.
33843053	4	51	theme	OGT	844:846	arg1	tendency					859:866	Opposite FOXA2 and OGT expression tendency	825:866	tendency	859:866	Opposite FOXA2 and OGT expression tendency were observed in HCC tissues, and lower FOXA2 levels predicted a poor prognosis in HCC patients.
33843053	0	52	theme	hepatocellular	50:63	arg1	cells					75:79	hepatocellular carcinoma cells	50:79	hepatocellular carcinoma cells	50:79	O-GlcNAcylation promotes the migratory ability of hepatocellular carcinoma cells via regulating FOXA2 stability and transcriptional activity.
33843053	2	53	theme	hepatocellular	500:513	arg1	carcinoma					515:523	hepatocellular carcinoma	500:523	hepatocellular carcinoma (HCC) cells	500:535	Although increasing evidence has shown that elevated levels of global O-GlcNAcylation are linked to the metastasis in hepatocellular carcinoma (HCC) cells, the underlying mechanism is still ambiguous.
33843053	2	53	theme	hepatocellular	500:513	arg1	HCC					526:528	HCC	526:528	HCC	526:528	Although increasing evidence has shown that elevated levels of global O-GlcNAcylation are linked to the metastasis in hepatocellular carcinoma (HCC) cells, the underlying mechanism is still ambiguous.
33843053	3	54	theme	forkhead	619:626	arg1	FOXA2					644:648	FOXA2	644:648	FOXA2	644:648	In this study, we demonstrated that forkhead box protein A2 (FOXA2), an essential transcription factor for liver homeostasis and HCC developing, was O-GlcNAcylated by O-GlcNAc transferase (OGT) and regulates HCC cells migration and invasion.
33843053	3	54	theme	forkhead	619:626	arg1	factor					679:684	an essential transcription factor	652:684	an essential transcription factor for liver homeostasis and HCC developing	652:725	In this study, we demonstrated that forkhead box protein A2 (FOXA2), an essential transcription factor for liver homeostasis and HCC developing, was O-GlcNAcylated by O-GlcNAc transferase (OGT) and regulates HCC cells migration and invasion.
33843053	3	54	theme	forkhead	619:626	arg1	A2					640:641	forkhead box protein A2	619:641	forkhead box protein A2 (FOXA2)	619:649	In this study, we demonstrated that forkhead box protein A2 (FOXA2), an essential transcription factor for liver homeostasis and HCC developing, was O-GlcNAcylated by O-GlcNAc transferase (OGT) and regulates HCC cells migration and invasion.
33843053	8	55	theme	downstream	1481:1490	arg1	E-cadherin					1504:1513	FOXA2 downstream target gene E-cadherin	1475:1513	FOXA2 downstream target gene E-cadherin	1475:1513	O-GlcNAcylation decreased the transcription of FOXA2 downstream target gene E-cadherin and it ultimately promoted O-GlcNAcylation-mediated HCC cell migration and invasion.
33843053	8	56	theme	FOXA2	1475:1479	arg1	E-cadherin					1504:1513	FOXA2 downstream target gene E-cadherin	1475:1513	FOXA2 downstream target gene E-cadherin	1475:1513	O-GlcNAcylation decreased the transcription of FOXA2 downstream target gene E-cadherin and it ultimately promoted O-GlcNAcylation-mediated HCC cell migration and invasion.
33843053	4	57	theme	Opposite	825:832	arg1	FOXA2					834:838	Opposite FOXA2 and OGT expression tendency	825:866	FOXA2	834:838	Opposite FOXA2 and OGT expression tendency were observed in HCC tissues, and lower FOXA2 levels predicted a poor prognosis in HCC patients.
33843053	8	58	theme	E-cadherin	1504:1513	arg1	transcription					1458:1470	the transcription	1454:1470	the transcription of FOXA2 downstream target gene E-cadherin	1454:1513	O-GlcNAcylation decreased the transcription of FOXA2 downstream target gene E-cadherin and it ultimately promoted O-GlcNAcylation-mediated HCC cell migration and invasion.
33843053	4	59	theme	FOXA2	908:912	arg1	levels					914:919	lower FOXA2 levels	902:919	lower FOXA2 levels	902:919	Opposite FOXA2 and OGT expression tendency were observed in HCC tissues, and lower FOXA2 levels predicted a poor prognosis in HCC patients.
33843053	8	60	theme	HCC	1567:1569	arg1	migration					1576:1584	O-GlcNAcylation-mediated HCC cell migration	1542:1584	O-GlcNAcylation-mediated HCC cell migration	1542:1584	O-GlcNAcylation decreased the transcription of FOXA2 downstream target gene E-cadherin and it ultimately promoted O-GlcNAcylation-mediated HCC cell migration and invasion.
33843053	5	61	theme	HCC	991:993	arg1	cells					995:999	HCC cells	991:999	HCC cells	991:999	The reduction of FOXA2 in HCC cells was found to be inversely correlated with the cellular O-GlcNAcylation and cell migratory ability.
33843053	9	62	theme	FOXA2	1676:1680	arg1	activity					1682:1689	FOXA2 activity	1676:1689	FOXA2 activity	1676:1689	The results provide insights into the role of O-GlcNAcylation in regulating FOXA2 activity and suggest its important implications in HCC metastasis.
33843053	8	63	theme	O-GlcNAcylation-mediated	1542:1565	arg1	migration					1576:1584	O-GlcNAcylation-mediated HCC cell migration	1542:1584	O-GlcNAcylation-mediated HCC cell migration	1542:1584	O-GlcNAcylation decreased the transcription of FOXA2 downstream target gene E-cadherin and it ultimately promoted O-GlcNAcylation-mediated HCC cell migration and invasion.
33843053	2	64	theme	global	445:450	arg1	O-GlcNAcylation					452:466	global O-GlcNAcylation	445:466	global O-GlcNAcylation	445:466	Although increasing evidence has shown that elevated levels of global O-GlcNAcylation are linked to the metastasis in hepatocellular carcinoma (HCC) cells, the underlying mechanism is still ambiguous.
33843053	6	65	theme	ubiquitination	1200:1213	arg1	degradation					1215:1225	the ubiquitination degradation	1196:1225	the ubiquitination degradation of FOXA2	1196:1234	Notably, we found that FOXA2 was modified by O-GlcNAcylation and that O-GlcNAcylation activated the ubiquitination degradation of FOXA2 in highly metastatic HCC cells.
33843053	6	66	mod	modified	1133:1140	arg3	O-GlcNAcylation					1145:1159	O-GlcNAcylation	1145:1159	O-GlcNAcylation	1145:1159	Notably, we found that FOXA2 was modified by O-GlcNAcylation and that O-GlcNAcylation activated the ubiquitination degradation of FOXA2 in highly metastatic HCC cells.
33843053	6	66	mod	modified	1133:1140	arg1	FOXA2					1123:1127	FOXA2	1123:1127	FOXA2	1123:1127	Notably, we found that FOXA2 was modified by O-GlcNAcylation and that O-GlcNAcylation activated the ubiquitination degradation of FOXA2 in highly metastatic HCC cells.
33843053	1	67	theme	posttranslational	163:179	arg1	modification					181:192	a posttranslational modification	161:192	a posttranslational modification that regulates numerous nuclear and cytoplasmic proteins and is emerging as a key regulator of various biological processes, such as transcription, signal transduction, and cell motility	161:379	O-GlcNAcylation is a posttranslational modification that regulates numerous nuclear and cytoplasmic proteins and is emerging as a key regulator of various biological processes, such as transcription, signal transduction, and cell motility.
33843053	1	67	theme	posttranslational	163:179	arg1	O-GlcNAcylation					142:156	O-GlcNAcylation	142:156	O-GlcNAcylation	142:156	O-GlcNAcylation is a posttranslational modification that regulates numerous nuclear and cytoplasmic proteins and is emerging as a key regulator of various biological processes, such as transcription, signal transduction, and cell motility.
33843053	1	68	theme	key	272:274	arg1	regulator					276:284	a key regulator	270:284	a key regulator of various biological processes, such as transcription, signal transduction, and cell motility	270:379	O-GlcNAcylation is a posttranslational modification that regulates numerous nuclear and cytoplasmic proteins and is emerging as a key regulator of various biological processes, such as transcription, signal transduction, and cell motility.
33843053	0	69	theme	carcinoma	65:73	arg1	cells					75:79	hepatocellular carcinoma cells	50:79	hepatocellular carcinoma cells	50:79	O-GlcNAcylation promotes the migratory ability of hepatocellular carcinoma cells via regulating FOXA2 stability and transcriptional activity.
33843053	6	70	theme	HCC	1257:1259	arg1	cells					1261:1265	highly metastatic HCC cells	1239:1265	highly metastatic HCC cells	1239:1265	Notably, we found that FOXA2 was modified by O-GlcNAcylation and that O-GlcNAcylation activated the ubiquitination degradation of FOXA2 in highly metastatic HCC cells.
33843053	7	71	from	O-GlcNAcylation	1349:1363	arg1	FOXA2					1368:1372	FOXA2	1368:1372	FOXA2	1368:1372	Although this modification did not affect FOXA2 nuclear localization capability, O-GlcNAcylation on FOXA2 was key for attenuating FOXA2-mediated transcription.
20805223	9	0	theme	OGT	1247:1249	arg1	overexpression					1251:1264	OGT overexpression	1247:1264	OGT overexpression	1247:1264	Moreover, OGT overexpression results in an increase in abnormal chromosomal bridge formation.
20805223	9	1	theme	abnormal	1292:1299	arg1	formation					1320:1328	abnormal chromosomal bridge formation	1292:1328	abnormal chromosomal bridge formation	1292:1328	Moreover, OGT overexpression results in an increase in abnormal chromosomal bridge formation.
20805223	5	2	from	threonine	795:803	arg1	proteins					772:779	nuclear and cytoplasmic proteins	748:779	nuclear and cytoplasmic proteins at serine and threonine residues	748:812	Here, we report that N-acetylglucosamine (O-GlcNAc) transferase (OGT), the enzyme catalyzing the addition of O-GlcNAc moieties to nuclear and cytoplasmic proteins at serine and threonine residues, regulates some aspects of mitotic chromatin dynamics.
20805223	6	3	theme	OGT	869:871	arg1	amounts					881:887	OGT protein amounts	869:887	OGT protein amounts	869:887	OGT protein amounts decrease during M phase.
20805223	8	4	theme	mitotic	1087:1093	arg1	phosphorylation					1095:1109	mitotic phosphorylation	1087:1109	mitotic phosphorylation of coactivator-associated arginine methyltransferase 1 (CARM1)	1087:1172	Overexpression of OGT also prevents mitotic phosphorylation of coactivator-associated arginine methyltransferase 1 (CARM1) and prevents its correct cellular localization during mitosis.
20805223	9	5	theme	bridge	1313:1318	arg1	formation					1320:1328	abnormal chromosomal bridge formation	1292:1328	abnormal chromosomal bridge formation	1292:1328	Moreover, OGT overexpression results in an increase in abnormal chromosomal bridge formation.
20805223	3	6	theme	octameric	363:371	arg1	complex					373:379	an octameric complex	360:379	an octameric complex of basic proteins important in regulating DNA organization and accessibility	360:456	Histones form an octameric complex of basic proteins important in regulating DNA organization and accessibility.
20805223	10	7	theme	correct	1434:1440	arg1	segregation					1454:1464	correct chromosomal segregation	1434:1464	correct chromosomal segregation during mitosis	1434:1479	Together, these results show that regulating the amount of OGT during mitosis is important in ensuring correct chromosomal segregation during mitosis.
20805223	2	8	theme	DNA	160:162	arg1	condensation					164:175	DNA condensation	160:175	DNA condensation	160:175	DNA condensation is crucial in ensuring that chromosomes are correctly attached to the mitotic spindle for segregation, preventing DNA breaks or constrictions from the contractile ring.
20805223	2	9	theme	DNA	291:293	arg1	breaks					295:300	DNA breaks	291:300	DNA breaks	291:300	DNA condensation is crucial in ensuring that chromosomes are correctly attached to the mitotic spindle for segregation, preventing DNA breaks or constrictions from the contractile ring.
20805223	0	10	theme	O-GlcNAc	0:7	arg1	transferase					9:19	O-GlcNAc transferase	0:19	O-GlcNAc transferase	0:19	O-GlcNAc transferase regulates mitotic chromatin dynamics.
20805223	1	11	theme	same	137:140	arg1	material					150:157	the same genetic material	133:157	the same genetic material	133:157	Mitosis must faithfully divide the genome such that each progeny inherits the same genetic material.
20805223	8	12	theme	coactivator-associated	1114:1135	arg1	CARM1					1167:1171	CARM1	1167:1171	CARM1	1167:1171	Overexpression of OGT also prevents mitotic phosphorylation of coactivator-associated arginine methyltransferase 1 (CARM1) and prevents its correct cellular localization during mitosis.
20805223	8	12	theme	coactivator-associated	1114:1135	arg1	methyltransferase					1146:1162	coactivator-associated arginine methyltransferase 1	1114:1164	coactivator-associated arginine methyltransferase 1 (CARM1)	1114:1172	Overexpression of OGT also prevents mitotic phosphorylation of coactivator-associated arginine methyltransferase 1 (CARM1) and prevents its correct cellular localization during mitosis.
20805223	7	13	theme	Modest	914:919	arg1	overexpression					921:934	Modest overexpression	914:934	Modest overexpression of OGT	914:941	Modest overexpression of OGT alters mitotic histone post-translational modifications at Lys-9, Ser-10, Arg-17, and Lys-27 of histone H3.
20805223	2	14	attach	attached	231:238	arg1	spindle					255:261	the mitotic spindle	243:261	the mitotic spindle for segregation	243:277	DNA condensation is crucial in ensuring that chromosomes are correctly attached to the mitotic spindle for segregation, preventing DNA breaks or constrictions from the contractile ring.
20805223	2	14	attach	attached	231:238	arg2	chromosomes					205:215	chromosomes	205:215	chromosomes	205:215	DNA condensation is crucial in ensuring that chromosomes are correctly attached to the mitotic spindle for segregation, preventing DNA breaks or constrictions from the contractile ring.
20805223	1	15	dep	inherits	124:131	arg1	such					101:104	such	101:104	such	101:104	Mitosis must faithfully divide the genome such that each progeny inherits the same genetic material.
20805223	3	16	theme	proteins	390:397	arg1	complex					373:379	an octameric complex	360:379	an octameric complex of basic proteins important in regulating DNA organization and accessibility	360:456	Histones form an octameric complex of basic proteins important in regulating DNA organization and accessibility.
20805223	8	17	theme	methyltransferase	1146:1162	arg1	phosphorylation					1095:1109	mitotic phosphorylation	1087:1109	mitotic phosphorylation of coactivator-associated arginine methyltransferase 1 (CARM1)	1087:1172	Overexpression of OGT also prevents mitotic phosphorylation of coactivator-associated arginine methyltransferase 1 (CARM1) and prevents its correct cellular localization during mitosis.
20805223	3	18	theme	important	399:407	arg1	proteins					390:397	basic proteins	384:397	basic proteins important in regulating DNA organization and accessibility	384:456	Histones form an octameric complex of basic proteins important in regulating DNA organization and accessibility.
20805223	8	19	theme	arginine	1137:1144	arg1	CARM1					1167:1171	CARM1	1167:1171	CARM1	1167:1171	Overexpression of OGT also prevents mitotic phosphorylation of coactivator-associated arginine methyltransferase 1 (CARM1) and prevents its correct cellular localization during mitosis.
20805223	8	19	theme	arginine	1137:1144	arg1	methyltransferase					1146:1162	coactivator-associated arginine methyltransferase 1	1114:1164	coactivator-associated arginine methyltransferase 1 (CARM1)	1114:1172	Overexpression of OGT also prevents mitotic phosphorylation of coactivator-associated arginine methyltransferase 1 (CARM1) and prevents its correct cellular localization during mitosis.
20805223	8	20	theme	OGT	1069:1071	arg1	Overexpression					1051:1064	Overexpression	1051:1064	Overexpression of OGT	1051:1071	Overexpression of OGT also prevents mitotic phosphorylation of coactivator-associated arginine methyltransferase 1 (CARM1) and prevents its correct cellular localization during mitosis.
20805223	0	21	theme	mitotic	31:37	arg1	dynamics					49:56	mitotic chromatin dynamics	31:56	mitotic chromatin dynamics	31:56	O-GlcNAc transferase regulates mitotic chromatin dynamics.
20805223	5	22	theme	dynamics	859:866	arg1	aspects					830:836	some aspects	825:836	some aspects of mitotic chromatin dynamics	825:866	Here, we report that N-acetylglucosamine (O-GlcNAc) transferase (OGT), the enzyme catalyzing the addition of O-GlcNAc moieties to nuclear and cytoplasmic proteins at serine and threonine residues, regulates some aspects of mitotic chromatin dynamics.
20805223	5	23	theme	N-acetylglucosamine	639:657	arg1	enzyme					693:698	the enzyme	689:698	the enzyme catalyzing the addition of O-GlcNAc moieties to nuclear and cytoplasmic proteins at serine and threonine residues	689:812	Here, we report that N-acetylglucosamine (O-GlcNAc) transferase (OGT), the enzyme catalyzing the addition of O-GlcNAc moieties to nuclear and cytoplasmic proteins at serine and threonine residues, regulates some aspects of mitotic chromatin dynamics.
20805223	5	23	theme	N-acetylglucosamine	639:657	arg1	OGT					683:685	OGT	683:685	OGT	683:685	Here, we report that N-acetylglucosamine (O-GlcNAc) transferase (OGT), the enzyme catalyzing the addition of O-GlcNAc moieties to nuclear and cytoplasmic proteins at serine and threonine residues, regulates some aspects of mitotic chromatin dynamics.
20805223	5	23	theme	N-acetylglucosamine	639:657	arg1	transferase					670:680	N-acetylglucosamine (O-GlcNAc) transferase	639:680	N-acetylglucosamine (O-GlcNAc) transferase (OGT)	639:686	Here, we report that N-acetylglucosamine (O-GlcNAc) transferase (OGT), the enzyme catalyzing the addition of O-GlcNAc moieties to nuclear and cytoplasmic proteins at serine and threonine residues, regulates some aspects of mitotic chromatin dynamics.
20805223	3	24	theme	basic	384:388	arg1	proteins					390:397	basic proteins	384:397	basic proteins important in regulating DNA organization and accessibility	384:456	Histones form an octameric complex of basic proteins important in regulating DNA organization and accessibility.
20805223	5	25	theme	nuclear	748:754	arg1	proteins					772:779	nuclear and cytoplasmic proteins	748:779	nuclear and cytoplasmic proteins at serine and threonine residues	748:812	Here, we report that N-acetylglucosamine (O-GlcNAc) transferase (OGT), the enzyme catalyzing the addition of O-GlcNAc moieties to nuclear and cytoplasmic proteins at serine and threonine residues, regulates some aspects of mitotic chromatin dynamics.
20805223	5	26	from	serine	784:789	arg1	proteins					772:779	nuclear and cytoplasmic proteins	748:779	nuclear and cytoplasmic proteins at serine and threonine residues	748:812	Here, we report that N-acetylglucosamine (O-GlcNAc) transferase (OGT), the enzyme catalyzing the addition of O-GlcNAc moieties to nuclear and cytoplasmic proteins at serine and threonine residues, regulates some aspects of mitotic chromatin dynamics.
20805223	10	27	theme	OGT	1390:1392	arg1	OGT					1390:1392	OGT	1390:1392	OGT	1390:1392	Together, these results show that regulating the amount of OGT during mitosis is important in ensuring correct chromosomal segregation during mitosis.
20805223	10	27	theme	OGT	1390:1392	arg1	amount					1380:1385	the amount	1376:1385	the amount of OGT	1376:1392	Together, these results show that regulating the amount of OGT during mitosis is important in ensuring correct chromosomal segregation during mitosis.
20805223	3	28	theme	DNA	423:425	arg1	organization					427:438	DNA organization	423:438	DNA organization	423:438	Histones form an octameric complex of basic proteins important in regulating DNA organization and accessibility.
20805223	4	29	theme	post-translational	467:484	arg1	modifications					486:498	Histone post-translational modifications	459:498	Histone post-translational modifications	459:498	Histone post-translational modifications are altered during mitosis, although the roles of these post-translational modifications remain poorly characterized.
20805223	0	30	theme	chromatin	39:47	arg1	dynamics					49:56	mitotic chromatin dynamics	31:56	mitotic chromatin dynamics	31:56	O-GlcNAc transferase regulates mitotic chromatin dynamics.
20805223	4	31	theme	modifications	575:587	arg1	roles					541:545	the roles	537:545	the roles of these post-translational modifications	537:587	Histone post-translational modifications are altered during mitosis, although the roles of these post-translational modifications remain poorly characterized.
20805223	5	32	theme	cytoplasmic	760:770	arg1	proteins					772:779	nuclear and cytoplasmic proteins	748:779	nuclear and cytoplasmic proteins at serine and threonine residues	748:812	Here, we report that N-acetylglucosamine (O-GlcNAc) transferase (OGT), the enzyme catalyzing the addition of O-GlcNAc moieties to nuclear and cytoplasmic proteins at serine and threonine residues, regulates some aspects of mitotic chromatin dynamics.
20805223	4	33	theme	post-translational	556:573	arg1	modifications					575:587	these post-translational modifications	550:587	these post-translational modifications	550:587	Histone post-translational modifications are altered during mitosis, although the roles of these post-translational modifications remain poorly characterized.
20805223	5	34	dep	serine	784:789	arg1	residues					805:812	residues	805:812	residues	805:812	Here, we report that N-acetylglucosamine (O-GlcNAc) transferase (OGT), the enzyme catalyzing the addition of O-GlcNAc moieties to nuclear and cytoplasmic proteins at serine and threonine residues, regulates some aspects of mitotic chromatin dynamics.
20805223	6	35	theme	M	905:905	arg1	phase					907:911	M phase	905:911	M phase	905:911	OGT protein amounts decrease during M phase.
20805223	8	36	theme	correct	1191:1197	arg1	localization					1208:1219	its correct cellular localization	1187:1219	its correct cellular localization	1187:1219	Overexpression of OGT also prevents mitotic phosphorylation of coactivator-associated arginine methyltransferase 1 (CARM1) and prevents its correct cellular localization during mitosis.
20805223	5	37	theme	mitotic	841:847	arg1	dynamics					859:866	mitotic chromatin dynamics	841:866	mitotic chromatin dynamics	841:866	Here, we report that N-acetylglucosamine (O-GlcNAc) transferase (OGT), the enzyme catalyzing the addition of O-GlcNAc moieties to nuclear and cytoplasmic proteins at serine and threonine residues, regulates some aspects of mitotic chromatin dynamics.
20805223	7	38	theme	post-translational	966:983	arg1	modifications					985:997	mitotic histone post-translational modifications	950:997	mitotic histone post-translational modifications	950:997	Modest overexpression of OGT alters mitotic histone post-translational modifications at Lys-9, Ser-10, Arg-17, and Lys-27 of histone H3.
20805223	9	39	theme	chromosomal	1301:1311	arg1	formation					1320:1328	abnormal chromosomal bridge formation	1292:1328	abnormal chromosomal bridge formation	1292:1328	Moreover, OGT overexpression results in an increase in abnormal chromosomal bridge formation.
20805223	5	40	theme	O-GlcNAc	727:734	arg1	moieties					736:743	O-GlcNAc moieties	727:743	O-GlcNAc moieties	727:743	Here, we report that N-acetylglucosamine (O-GlcNAc) transferase (OGT), the enzyme catalyzing the addition of O-GlcNAc moieties to nuclear and cytoplasmic proteins at serine and threonine residues, regulates some aspects of mitotic chromatin dynamics.
20805223	9	41	from	increase	1280:1287	arg1	formation					1320:1328	abnormal chromosomal bridge formation	1292:1328	abnormal chromosomal bridge formation	1292:1328	Moreover, OGT overexpression results in an increase in abnormal chromosomal bridge formation.
20805223	5	42	theme	moieties	736:743	arg1	addition					715:722	the addition	711:722	the addition of O-GlcNAc moieties to nuclear and cytoplasmic proteins at serine and threonine residues	711:812	Here, we report that N-acetylglucosamine (O-GlcNAc) transferase (OGT), the enzyme catalyzing the addition of O-GlcNAc moieties to nuclear and cytoplasmic proteins at serine and threonine residues, regulates some aspects of mitotic chromatin dynamics.
20805223	4	43	theme	Histone	459:465	arg1	modifications					486:498	Histone post-translational modifications	459:498	Histone post-translational modifications	459:498	Histone post-translational modifications are altered during mitosis, although the roles of these post-translational modifications remain poorly characterized.
20805223	7	44	theme	histone	1039:1045	arg1	H3					1047:1048	histone H3	1039:1048	histone H3	1039:1048	Modest overexpression of OGT alters mitotic histone post-translational modifications at Lys-9, Ser-10, Arg-17, and Lys-27 of histone H3.
20805223	2	45	theme	contractile	328:338	arg1	ring					340:343	the contractile ring	324:343	the contractile ring	324:343	DNA condensation is crucial in ensuring that chromosomes are correctly attached to the mitotic spindle for segregation, preventing DNA breaks or constrictions from the contractile ring.
20805223	7	46	theme	mitotic	950:956	arg1	modifications					985:997	mitotic histone post-translational modifications	950:997	mitotic histone post-translational modifications	950:997	Modest overexpression of OGT alters mitotic histone post-translational modifications at Lys-9, Ser-10, Arg-17, and Lys-27 of histone H3.
20805223	6	47	theme	protein	873:879	arg1	amounts					881:887	OGT protein amounts	869:887	OGT protein amounts	869:887	OGT protein amounts decrease during M phase.
20805223	7	48	theme	H3	1047:1048	arg1	Arg-17					1017:1022	Arg-17	1017:1022	Arg-17	1017:1022	Modest overexpression of OGT alters mitotic histone post-translational modifications at Lys-9, Ser-10, Arg-17, and Lys-27 of histone H3.
20805223	7	48	theme	H3	1047:1048	arg1	Lys-27					1029:1034	Lys-27	1029:1034	Lys-27	1029:1034	Modest overexpression of OGT alters mitotic histone post-translational modifications at Lys-9, Ser-10, Arg-17, and Lys-27 of histone H3.
20805223	7	48	theme	H3	1047:1048	arg1	Ser-10					1009:1014	Ser-10	1009:1014	Ser-10	1009:1014	Modest overexpression of OGT alters mitotic histone post-translational modifications at Lys-9, Ser-10, Arg-17, and Lys-27 of histone H3.
20805223	7	48	theme	H3	1047:1048	arg1	Lys-9					1002:1006	Lys-9	1002:1006	Lys-9	1002:1006	Modest overexpression of OGT alters mitotic histone post-translational modifications at Lys-9, Ser-10, Arg-17, and Lys-27 of histone H3.
20805223	1	49	theme	genetic	142:148	arg1	material					150:157	the same genetic material	133:157	the same genetic material	133:157	Mitosis must faithfully divide the genome such that each progeny inherits the same genetic material.
20805223	7	50	theme	histone	958:964	arg1	modifications					985:997	mitotic histone post-translational modifications	950:997	mitotic histone post-translational modifications	950:997	Modest overexpression of OGT alters mitotic histone post-translational modifications at Lys-9, Ser-10, Arg-17, and Lys-27 of histone H3.
20805223	8	51	theme	cellular	1199:1206	arg1	localization					1208:1219	its correct cellular localization	1187:1219	its correct cellular localization	1187:1219	Overexpression of OGT also prevents mitotic phosphorylation of coactivator-associated arginine methyltransferase 1 (CARM1) and prevents its correct cellular localization during mitosis.
20805223	2	52	theme	mitotic	247:253	arg1	spindle					255:261	the mitotic spindle	243:261	the mitotic spindle for segregation	243:277	DNA condensation is crucial in ensuring that chromosomes are correctly attached to the mitotic spindle for segregation, preventing DNA breaks or constrictions from the contractile ring.
20805223	10	53	theme	chromosomal	1442:1452	arg1	segregation					1454:1464	correct chromosomal segregation	1434:1464	correct chromosomal segregation during mitosis	1434:1479	Together, these results show that regulating the amount of OGT during mitosis is important in ensuring correct chromosomal segregation during mitosis.
20805223	5	54	theme	chromatin	849:857	arg1	dynamics					859:866	mitotic chromatin dynamics	841:866	mitotic chromatin dynamics	841:866	Here, we report that N-acetylglucosamine (O-GlcNAc) transferase (OGT), the enzyme catalyzing the addition of O-GlcNAc moieties to nuclear and cytoplasmic proteins at serine and threonine residues, regulates some aspects of mitotic chromatin dynamics.
20805223	7	55	theme	OGT	939:941	arg1	overexpression					921:934	Modest overexpression	914:934	Modest overexpression of OGT	914:941	Modest overexpression of OGT alters mitotic histone post-translational modifications at Lys-9, Ser-10, Arg-17, and Lys-27 of histone H3.
27259240	0	0	theme	colon	106:110	arg1	cells					119:123	5-fluorouracil-resistant colon cancer cells	81:123	5-fluorouracil-resistant colon cancer cells	81:123	Interaction of DNA demethylase and histone methyltransferase upregulates Nrf2 in 5-fluorouracil-resistant colon cancer cells.
27259240	4	1	theme	histone	717:723	arg1	lysine					728:733	histone H3 lysine 4	717:735	histone H3 lysine 4	717:735	Mixed-lineage leukemia (MLL), a histone methyltransferase, was upregulated, leading to increased trimethylation of histone H3 lysine 4, while G9a was downregulated, leading to decreased dimethylation of histone H3 lysine 9.
27259240	4	2	theme	Mixed-lineage	602:614	arg1	leukemia					616:623	Mixed-lineage leukemia	602:623	Mixed-lineage leukemia (MLL)	602:629	Mixed-lineage leukemia (MLL), a histone methyltransferase, was upregulated, leading to increased trimethylation of histone H3 lysine 4, while G9a was downregulated, leading to decreased dimethylation of histone H3 lysine 9.
27259240	4	2	theme	Mixed-lineage	602:614	arg1	methyltransferase					642:658	a histone methyltransferase	632:658	a histone methyltransferase	632:658	Mixed-lineage leukemia (MLL), a histone methyltransferase, was upregulated, leading to increased trimethylation of histone H3 lysine 4, while G9a was downregulated, leading to decreased dimethylation of histone H3 lysine 9.
27259240	4	2	theme	Mixed-lineage	602:614	arg1	MLL					626:628	MLL	626:628	MLL	626:628	Mixed-lineage leukemia (MLL), a histone methyltransferase, was upregulated, leading to increased trimethylation of histone H3 lysine 4, while G9a was downregulated, leading to decreased dimethylation of histone H3 lysine 9.
27259240	0	3	theme	5-fluorouracil-resistant	81:104	arg1	cells					119:123	5-fluorouracil-resistant colon cancer cells	81:123	5-fluorouracil-resistant colon cancer cells	81:123	Interaction of DNA demethylase and histone methyltransferase upregulates Nrf2 in 5-fluorouracil-resistant colon cancer cells.
27259240	8	4	theme	Nrf2	1253:1256	arg1	region					1267:1272	the Nrf2 promoter region	1249:1272	the Nrf2 promoter region	1249:1272	In SNUC5/5-FUR cells, a larger fraction of OGT was bound to TET1, which recruits OGT to the Nrf2 promoter region, than in SNUC5 cells.
27259240	3	5	theme	histone	464:470	arg1	HAT					491:493	HAT	491:493	HAT	491:493	Histone deacetylase (HDAC) and histone acetyltransferase (HAT) were respectively decreased and increased in SNUC5/5-FUR cells as compared to non-resistant parent cells.
27259240	3	5	theme	histone	464:470	arg1	acetyltransferase					472:488	histone acetyltransferase	464:488	histone acetyltransferase (HAT)	464:494	Histone deacetylase (HDAC) and histone acetyltransferase (HAT) were respectively decreased and increased in SNUC5/5-FUR cells as compared to non-resistant parent cells.
27259240	1	6	theme	5-fluorouracil-resistant	268:291	arg1	SNUC5/5-FUR					313:323	SNUC5/5-FUR	313:323	SNUC5/5-FUR	313:323	We recently reported that DNA demethylase ten-eleven translocation 1 (TET1) upregulates nuclear factor erythroid 2-related factor 2 (Nrf2) in 5-fluorouracil-resistant colon cancer cells (SNUC5/5-FUR).
27259240	1	6	theme	5-fluorouracil-resistant	268:291	arg1	cells					306:310	5-fluorouracil-resistant colon cancer cells	268:310	5-fluorouracil-resistant colon cancer cells (SNUC5/5-FUR)	268:324	We recently reported that DNA demethylase ten-eleven translocation 1 (TET1) upregulates nuclear factor erythroid 2-related factor 2 (Nrf2) in 5-fluorouracil-resistant colon cancer cells (SNUC5/5-FUR).
27259240	0	7	theme	cancer	112:117	arg1	cells					119:123	5-fluorouracil-resistant colon cancer cells	81:123	5-fluorouracil-resistant colon cancer cells	81:123	Interaction of DNA demethylase and histone methyltransferase upregulates Nrf2 in 5-fluorouracil-resistant colon cancer cells.
27259240	7	8	theme	HCF1	1108:1111	arg1	transferase					1073:1083	O-GlcNAc transferase	1064:1083	O-GlcNAc transferase (OGT)	1064:1089	Upregulation of O-GlcNAc transferase (OGT), an activator of HCF1, was also associated with HCF1-MLL interaction.
27259240	7	8	theme	HCF1	1108:1111	arg1	activator					1095:1103	an activator	1092:1103	an activator of HCF1	1092:1111	Upregulation of O-GlcNAc transferase (OGT), an activator of HCF1, was also associated with HCF1-MLL interaction.
27259240	5	9	theme	greater	894:900	arg1	extent					902:907	a greater extent	892:907	a greater extent than did silencing HAT1	892:931	siRNA-mediated MLL knockdown decreased levels of Nrf2 and HO-1 to a greater extent than did silencing HAT1.
27259240	1	10	theme	colon	293:297	arg1	SNUC5/5-FUR					313:323	SNUC5/5-FUR	313:323	SNUC5/5-FUR	313:323	We recently reported that DNA demethylase ten-eleven translocation 1 (TET1) upregulates nuclear factor erythroid 2-related factor 2 (Nrf2) in 5-fluorouracil-resistant colon cancer cells (SNUC5/5-FUR).
27259240	1	10	theme	colon	293:297	arg1	cells					306:310	5-fluorouracil-resistant colon cancer cells	268:310	5-fluorouracil-resistant colon cancer cells (SNUC5/5-FUR)	268:324	We recently reported that DNA demethylase ten-eleven translocation 1 (TET1) upregulates nuclear factor erythroid 2-related factor 2 (Nrf2) in 5-fluorouracil-resistant colon cancer cells (SNUC5/5-FUR).
27259240	7	11	theme	HCF1-MLL	1139:1146	arg1	interaction					1148:1158	HCF1-MLL interaction	1139:1158	HCF1-MLL interaction	1139:1158	Upregulation of O-GlcNAc transferase (OGT), an activator of HCF1, was also associated with HCF1-MLL interaction.
27259240	9	12	theme	proteins	1427:1434	arg1	demethylase					1451:1461	DNA demethylase	1447:1461	expression of histone methylation-related proteins as well as DNA demethylase	1385:1461	These findings indicate that SNUC5/5-FUR cells are under oxidative stress, which induces expression of histone methylation-related proteins as well as DNA demethylase, leading to upregulation of Nrf2 and 5-FU resistance.
27259240	9	12	theme	proteins	1427:1434	arg1	expression					1385:1394	expression	1385:1394	expression of histone methylation-related proteins as well as DNA demethylase	1385:1461	These findings indicate that SNUC5/5-FUR cells are under oxidative stress, which induces expression of histone methylation-related proteins as well as DNA demethylase, leading to upregulation of Nrf2 and 5-FU resistance.
27259240	7	13	theme	transferase	1073:1083	arg1	Upregulation					1048:1059	Upregulation	1048:1059	Upregulation of O-GlcNAc transferase (OGT), an activator of HCF1,	1048:1112	Upregulation of O-GlcNAc transferase (OGT), an activator of HCF1, was also associated with HCF1-MLL interaction.
27259240	4	14	theme	histone	634:640	arg1	leukemia					616:623	Mixed-lineage leukemia	602:623	Mixed-lineage leukemia (MLL)	602:629	Mixed-lineage leukemia (MLL), a histone methyltransferase, was upregulated, leading to increased trimethylation of histone H3 lysine 4, while G9a was downregulated, leading to decreased dimethylation of histone H3 lysine 9.
27259240	4	14	theme	histone	634:640	arg1	methyltransferase					642:658	a histone methyltransferase	632:658	a histone methyltransferase	632:658	Mixed-lineage leukemia (MLL), a histone methyltransferase, was upregulated, leading to increased trimethylation of histone H3 lysine 4, while G9a was downregulated, leading to decreased dimethylation of histone H3 lysine 9.
27259240	3	15	theme	SNUC5/5-FUR	541:551	arg1	cells					553:557	SNUC5/5-FUR cells	541:557	SNUC5/5-FUR cells	541:557	Histone deacetylase (HDAC) and histone acetyltransferase (HAT) were respectively decreased and increased in SNUC5/5-FUR cells as compared to non-resistant parent cells.
27259240	8	16	theme	OGT	1204:1206	arg1	fraction					1192:1199	a larger fraction	1183:1199	a larger fraction of OGT	1183:1206	In SNUC5/5-FUR cells, a larger fraction of OGT was bound to TET1, which recruits OGT to the Nrf2 promoter region, than in SNUC5 cells.
27259240	2	17	theme	Nrf2	400:403	arg1	activation					421:430	Nrf2 transcriptional activation	400:430	Nrf2 transcriptional activation	400:430	In the present study, we examined the effect of histone modifications on Nrf2 transcriptional activation.
27259240	9	18	theme	oxidative	1353:1361	arg1	stress					1363:1368	oxidative stress	1353:1368	oxidative stress	1353:1368	These findings indicate that SNUC5/5-FUR cells are under oxidative stress, which induces expression of histone methylation-related proteins as well as DNA demethylase, leading to upregulation of Nrf2 and 5-FU resistance.
27259240	6	19	theme	SNUC5/5-FUR	979:989	arg1	cells					991:995	SNUC5/5-FUR cells	979:995	SNUC5/5-FUR cells	979:995	Host cell factor 1 (HCF1) was upregulated in SNUC5/5-FUR cells, and we observed interaction between HCF1 and MLL.
27259240	9	20	theme	DNA	1447:1449	arg1	demethylase					1451:1461	DNA demethylase	1447:1461	expression of histone methylation-related proteins as well as DNA demethylase	1385:1461	These findings indicate that SNUC5/5-FUR cells are under oxidative stress, which induces expression of histone methylation-related proteins as well as DNA demethylase, leading to upregulation of Nrf2 and 5-FU resistance.
27259240	2	21	theme	present	334:340	arg1	study					342:346	the present study	330:346	the present study	330:346	In the present study, we examined the effect of histone modifications on Nrf2 transcriptional activation.
27259240	5	22	theme	Nrf2	875:878	arg1	levels					865:870	levels	865:870	levels of Nrf2 and HO-1	865:887	siRNA-mediated MLL knockdown decreased levels of Nrf2 and HO-1 to a greater extent than did silencing HAT1.
27259240	9	23	theme	Nrf2	1491:1494	arg1	upregulation					1475:1486	upregulation	1475:1486	upregulation of Nrf2 and 5-FU resistance	1475:1514	These findings indicate that SNUC5/5-FUR cells are under oxidative stress, which induces expression of histone methylation-related proteins as well as DNA demethylase, leading to upregulation of Nrf2 and 5-FU resistance.
27259240	3	24	theme	parent	588:593	arg1	cells					595:599	non-resistant parent cells	574:599	non-resistant parent cells	574:599	Histone deacetylase (HDAC) and histone acetyltransferase (HAT) were respectively decreased and increased in SNUC5/5-FUR cells as compared to non-resistant parent cells.
27259240	2	25	theme	modifications	383:395	arg1	effect					365:370	the effect	361:370	the effect of histone modifications on Nrf2 transcriptional activation	361:430	In the present study, we examined the effect of histone modifications on Nrf2 transcriptional activation.
27259240	1	26	theme	cancer	299:304	arg1	SNUC5/5-FUR					313:323	SNUC5/5-FUR	313:323	SNUC5/5-FUR	313:323	We recently reported that DNA demethylase ten-eleven translocation 1 (TET1) upregulates nuclear factor erythroid 2-related factor 2 (Nrf2) in 5-fluorouracil-resistant colon cancer cells (SNUC5/5-FUR).
27259240	1	26	theme	cancer	299:304	arg1	cells					306:310	5-fluorouracil-resistant colon cancer cells	268:310	5-fluorouracil-resistant colon cancer cells (SNUC5/5-FUR)	268:324	We recently reported that DNA demethylase ten-eleven translocation 1 (TET1) upregulates nuclear factor erythroid 2-related factor 2 (Nrf2) in 5-fluorouracil-resistant colon cancer cells (SNUC5/5-FUR).
27259240	7	27	theme	O-GlcNAc	1064:1071	arg1	transferase					1073:1083	O-GlcNAc transferase	1064:1083	O-GlcNAc transferase (OGT)	1064:1089	Upregulation of O-GlcNAc transferase (OGT), an activator of HCF1, was also associated with HCF1-MLL interaction.
27259240	7	27	theme	O-GlcNAc	1064:1071	arg1	activator					1095:1103	an activator	1092:1103	an activator of HCF1	1092:1111	Upregulation of O-GlcNAc transferase (OGT), an activator of HCF1, was also associated with HCF1-MLL interaction.
27259240	7	27	theme	O-GlcNAc	1064:1071	arg1	OGT					1086:1088	OGT	1086:1088	OGT	1086:1088	Upregulation of O-GlcNAc transferase (OGT), an activator of HCF1, was also associated with HCF1-MLL interaction.
27259240	5	28	dep	extent	902:907	arg1	did					914:916	did	914:916	did	914:916	siRNA-mediated MLL knockdown decreased levels of Nrf2 and HO-1 to a greater extent than did silencing HAT1.
27259240	9	29	theme	5-FU	1500:1503	arg1	resistance					1505:1514	5-FU resistance	1500:1514	5-FU resistance	1500:1514	These findings indicate that SNUC5/5-FUR cells are under oxidative stress, which induces expression of histone methylation-related proteins as well as DNA demethylase, leading to upregulation of Nrf2 and 5-FU resistance.
27259240	2	30	theme	histone	375:381	arg1	modifications					383:395	histone modifications	375:395	histone modifications	375:395	In the present study, we examined the effect of histone modifications on Nrf2 transcriptional activation.
27259240	0	31	theme	demethylase	19:29	arg1	Interaction					0:10	Interaction	0:10	Interaction of DNA demethylase and histone methyltransferase	0:59	Interaction of DNA demethylase and histone methyltransferase upregulates Nrf2 in 5-fluorouracil-resistant colon cancer cells.
27259240	2	32	from	effect	365:370	arg1	activation					421:430	Nrf2 transcriptional activation	400:430	Nrf2 transcriptional activation	400:430	In the present study, we examined the effect of histone modifications on Nrf2 transcriptional activation.
27259240	9	33	theme	resistance	1505:1514	arg1	upregulation					1475:1486	upregulation	1475:1486	upregulation of Nrf2 and 5-FU resistance	1475:1514	These findings indicate that SNUC5/5-FUR cells are under oxidative stress, which induces expression of histone methylation-related proteins as well as DNA demethylase, leading to upregulation of Nrf2 and 5-FU resistance.
27259240	1	34	theme	nuclear	214:220	arg1	factor					249:254	nuclear factor erythroid 2-related factor 2	214:256	nuclear factor erythroid 2-related factor 2 (Nrf2) in 5-fluorouracil-resistant colon cancer cells (SNUC5/5-FUR)	214:324	We recently reported that DNA demethylase ten-eleven translocation 1 (TET1) upregulates nuclear factor erythroid 2-related factor 2 (Nrf2) in 5-fluorouracil-resistant colon cancer cells (SNUC5/5-FUR).
27259240	1	34	theme	nuclear	214:220	arg1	Nrf2					259:262	Nrf2	259:262	Nrf2	259:262	We recently reported that DNA demethylase ten-eleven translocation 1 (TET1) upregulates nuclear factor erythroid 2-related factor 2 (Nrf2) in 5-fluorouracil-resistant colon cancer cells (SNUC5/5-FUR).
27259240	0	35	theme	DNA	15:17	arg1	demethylase					19:29	DNA demethylase	15:29	DNA demethylase	15:29	Interaction of DNA demethylase and histone methyltransferase upregulates Nrf2 in 5-fluorouracil-resistant colon cancer cells.
27259240	4	36	theme	decreased	778:786	arg1	dimethylation					788:800	decreased dimethylation	778:800	decreased dimethylation of histone H3 lysine 9	778:823	Mixed-lineage leukemia (MLL), a histone methyltransferase, was upregulated, leading to increased trimethylation of histone H3 lysine 4, while G9a was downregulated, leading to decreased dimethylation of histone H3 lysine 9.
27259240	3	37	theme	non-resistant	574:586	arg1	cells					595:599	non-resistant parent cells	574:599	non-resistant parent cells	574:599	Histone deacetylase (HDAC) and histone acetyltransferase (HAT) were respectively decreased and increased in SNUC5/5-FUR cells as compared to non-resistant parent cells.
27259240	1	38	theme	factor	222:227	arg1	factor					249:254	nuclear factor erythroid 2-related factor 2	214:256	nuclear factor erythroid 2-related factor 2 (Nrf2) in 5-fluorouracil-resistant colon cancer cells (SNUC5/5-FUR)	214:324	We recently reported that DNA demethylase ten-eleven translocation 1 (TET1) upregulates nuclear factor erythroid 2-related factor 2 (Nrf2) in 5-fluorouracil-resistant colon cancer cells (SNUC5/5-FUR).
27259240	1	38	theme	factor	222:227	arg1	Nrf2					259:262	Nrf2	259:262	Nrf2	259:262	We recently reported that DNA demethylase ten-eleven translocation 1 (TET1) upregulates nuclear factor erythroid 2-related factor 2 (Nrf2) in 5-fluorouracil-resistant colon cancer cells (SNUC5/5-FUR).
27259240	0	39	theme	histone	35:41	arg1	methyltransferase					43:59	histone methyltransferase	35:59	histone methyltransferase	35:59	Interaction of DNA demethylase and histone methyltransferase upregulates Nrf2 in 5-fluorouracil-resistant colon cancer cells.
27259240	9	40	theme	histone	1399:1405	arg1	proteins					1427:1434	histone methylation-related proteins	1399:1434	histone methylation-related proteins	1399:1434	These findings indicate that SNUC5/5-FUR cells are under oxidative stress, which induces expression of histone methylation-related proteins as well as DNA demethylase, leading to upregulation of Nrf2 and 5-FU resistance.
27259240	5	41	theme	HO-1	884:887	arg1	levels					865:870	levels	865:870	levels of Nrf2 and HO-1	865:887	siRNA-mediated MLL knockdown decreased levels of Nrf2 and HO-1 to a greater extent than did silencing HAT1.
27259240	1	42	theme	erythroid	229:237	arg1	factor					249:254	nuclear factor erythroid 2-related factor 2	214:256	nuclear factor erythroid 2-related factor 2 (Nrf2) in 5-fluorouracil-resistant colon cancer cells (SNUC5/5-FUR)	214:324	We recently reported that DNA demethylase ten-eleven translocation 1 (TET1) upregulates nuclear factor erythroid 2-related factor 2 (Nrf2) in 5-fluorouracil-resistant colon cancer cells (SNUC5/5-FUR).
27259240	1	42	theme	erythroid	229:237	arg1	Nrf2					259:262	Nrf2	259:262	Nrf2	259:262	We recently reported that DNA demethylase ten-eleven translocation 1 (TET1) upregulates nuclear factor erythroid 2-related factor 2 (Nrf2) in 5-fluorouracil-resistant colon cancer cells (SNUC5/5-FUR).
27259240	3	43	theme	Histone	433:439	arg1	HDAC					454:457	HDAC	454:457	HDAC	454:457	Histone deacetylase (HDAC) and histone acetyltransferase (HAT) were respectively decreased and increased in SNUC5/5-FUR cells as compared to non-resistant parent cells.
27259240	3	43	theme	Histone	433:439	arg1	deacetylase					441:451	Histone deacetylase	433:451	Histone deacetylase (HDAC)	433:458	Histone deacetylase (HDAC) and histone acetyltransferase (HAT) were respectively decreased and increased in SNUC5/5-FUR cells as compared to non-resistant parent cells.
27259240	8	44	theme	SNUC5/5-FUR	1164:1174	arg1	cells					1176:1180	SNUC5/5-FUR cells	1164:1180	SNUC5/5-FUR cells	1164:1180	In SNUC5/5-FUR cells, a larger fraction of OGT was bound to TET1, which recruits OGT to the Nrf2 promoter region, than in SNUC5 cells.
27259240	4	45	theme	lysine	816:821	arg1	dimethylation					788:800	decreased dimethylation	778:800	decreased dimethylation of histone H3 lysine 9	778:823	Mixed-lineage leukemia (MLL), a histone methyltransferase, was upregulated, leading to increased trimethylation of histone H3 lysine 4, while G9a was downregulated, leading to decreased dimethylation of histone H3 lysine 9.
27259240	2	46	theme	transcriptional	405:419	arg1	activation					421:430	Nrf2 transcriptional activation	400:430	Nrf2 transcriptional activation	400:430	In the present study, we examined the effect of histone modifications on Nrf2 transcriptional activation.
27259240	6	47	theme	cell	939:942	arg1	factor					944:949	Host cell factor 1	934:951	Host cell factor 1 (HCF1)	934:958	Host cell factor 1 (HCF1) was upregulated in SNUC5/5-FUR cells, and we observed interaction between HCF1 and MLL.
27259240	6	47	theme	cell	939:942	arg1	HCF1					954:957	HCF1	954:957	HCF1	954:957	Host cell factor 1 (HCF1) was upregulated in SNUC5/5-FUR cells, and we observed interaction between HCF1 and MLL.
27259240	8	48	theme	SNUC5	1283:1287	arg1	cells					1289:1293	SNUC5 cells	1283:1293	SNUC5 cells	1283:1293	In SNUC5/5-FUR cells, a larger fraction of OGT was bound to TET1, which recruits OGT to the Nrf2 promoter region, than in SNUC5 cells.
27259240	4	49	theme	lysine	728:733	arg1	trimethylation					699:712	increased trimethylation	689:712	increased trimethylation of histone H3 lysine 4	689:735	Mixed-lineage leukemia (MLL), a histone methyltransferase, was upregulated, leading to increased trimethylation of histone H3 lysine 4, while G9a was downregulated, leading to decreased dimethylation of histone H3 lysine 9.
27259240	0	50	theme	methyltransferase	43:59	arg1	Interaction					0:10	Interaction	0:10	Interaction of DNA demethylase and histone methyltransferase	0:59	Interaction of DNA demethylase and histone methyltransferase upregulates Nrf2 in 5-fluorouracil-resistant colon cancer cells.
27259240	6	51	theme	Host	934:937	arg1	factor					944:949	Host cell factor 1	934:951	Host cell factor 1 (HCF1)	934:958	Host cell factor 1 (HCF1) was upregulated in SNUC5/5-FUR cells, and we observed interaction between HCF1 and MLL.
27259240	6	51	theme	Host	934:937	arg1	HCF1					954:957	HCF1	954:957	HCF1	954:957	Host cell factor 1 (HCF1) was upregulated in SNUC5/5-FUR cells, and we observed interaction between HCF1 and MLL.
27259240	4	52	theme	H3	725:726	arg1	lysine					728:733	histone H3 lysine 4	717:735	histone H3 lysine 4	717:735	Mixed-lineage leukemia (MLL), a histone methyltransferase, was upregulated, leading to increased trimethylation of histone H3 lysine 4, while G9a was downregulated, leading to decreased dimethylation of histone H3 lysine 9.
27259240	1	53	from	factor	249:254	arg1	SNUC5/5-FUR					313:323	SNUC5/5-FUR	313:323	SNUC5/5-FUR	313:323	We recently reported that DNA demethylase ten-eleven translocation 1 (TET1) upregulates nuclear factor erythroid 2-related factor 2 (Nrf2) in 5-fluorouracil-resistant colon cancer cells (SNUC5/5-FUR).
27259240	1	53	from	factor	249:254	arg1	cells					306:310	5-fluorouracil-resistant colon cancer cells	268:310	5-fluorouracil-resistant colon cancer cells (SNUC5/5-FUR)	268:324	We recently reported that DNA demethylase ten-eleven translocation 1 (TET1) upregulates nuclear factor erythroid 2-related factor 2 (Nrf2) in 5-fluorouracil-resistant colon cancer cells (SNUC5/5-FUR).
27259240	4	54	theme	increased	689:697	arg1	trimethylation					699:712	increased trimethylation	689:712	increased trimethylation of histone H3 lysine 4	689:735	Mixed-lineage leukemia (MLL), a histone methyltransferase, was upregulated, leading to increased trimethylation of histone H3 lysine 4, while G9a was downregulated, leading to decreased dimethylation of histone H3 lysine 9.
27259240	5	55	theme	silencing	918:926	arg1	HAT1					928:931	silencing HAT1	918:931	silencing HAT1	918:931	siRNA-mediated MLL knockdown decreased levels of Nrf2 and HO-1 to a greater extent than did silencing HAT1.
27259240	5	56	dep	did	914:916	arg1	than					909:912	than	909:912	than	909:912	siRNA-mediated MLL knockdown decreased levels of Nrf2 and HO-1 to a greater extent than did silencing HAT1.
27259240	5	57	theme	siRNA-mediated	826:839	arg1	knockdown					845:853	siRNA-mediated MLL knockdown	826:853	siRNA-mediated MLL knockdown	826:853	siRNA-mediated MLL knockdown decreased levels of Nrf2 and HO-1 to a greater extent than did silencing HAT1.
27259240	1	58	theme	DNA	152:154	arg1	translocation					179:191	DNA demethylase ten-eleven translocation 1	152:193	DNA demethylase ten-eleven translocation 1 (TET1)	152:200	We recently reported that DNA demethylase ten-eleven translocation 1 (TET1) upregulates nuclear factor erythroid 2-related factor 2 (Nrf2) in 5-fluorouracil-resistant colon cancer cells (SNUC5/5-FUR).
27259240	1	58	theme	DNA	152:154	arg1	TET1					196:199	TET1	196:199	TET1	196:199	We recently reported that DNA demethylase ten-eleven translocation 1 (TET1) upregulates nuclear factor erythroid 2-related factor 2 (Nrf2) in 5-fluorouracil-resistant colon cancer cells (SNUC5/5-FUR).
27259240	8	59	theme	promoter	1258:1265	arg1	region					1267:1272	the Nrf2 promoter region	1249:1272	the Nrf2 promoter region	1249:1272	In SNUC5/5-FUR cells, a larger fraction of OGT was bound to TET1, which recruits OGT to the Nrf2 promoter region, than in SNUC5 cells.
27259240	9	60	theme	methylation-related	1407:1425	arg1	proteins					1427:1434	histone methylation-related proteins	1399:1434	histone methylation-related proteins	1399:1434	These findings indicate that SNUC5/5-FUR cells are under oxidative stress, which induces expression of histone methylation-related proteins as well as DNA demethylase, leading to upregulation of Nrf2 and 5-FU resistance.
27259240	1	61	theme	2-related	239:247	arg1	factor					249:254	nuclear factor erythroid 2-related factor 2	214:256	nuclear factor erythroid 2-related factor 2 (Nrf2) in 5-fluorouracil-resistant colon cancer cells (SNUC5/5-FUR)	214:324	We recently reported that DNA demethylase ten-eleven translocation 1 (TET1) upregulates nuclear factor erythroid 2-related factor 2 (Nrf2) in 5-fluorouracil-resistant colon cancer cells (SNUC5/5-FUR).
27259240	1	61	theme	2-related	239:247	arg1	Nrf2					259:262	Nrf2	259:262	Nrf2	259:262	We recently reported that DNA demethylase ten-eleven translocation 1 (TET1) upregulates nuclear factor erythroid 2-related factor 2 (Nrf2) in 5-fluorouracil-resistant colon cancer cells (SNUC5/5-FUR).
27259240	4	62	theme	H3	813:814	arg1	lysine					816:821	histone H3 lysine 9	805:823	histone H3 lysine 9	805:823	Mixed-lineage leukemia (MLL), a histone methyltransferase, was upregulated, leading to increased trimethylation of histone H3 lysine 4, while G9a was downregulated, leading to decreased dimethylation of histone H3 lysine 9.
27259240	5	63	theme	MLL	841:843	arg1	knockdown					845:853	siRNA-mediated MLL knockdown	826:853	siRNA-mediated MLL knockdown	826:853	siRNA-mediated MLL knockdown decreased levels of Nrf2 and HO-1 to a greater extent than did silencing HAT1.
27259240	1	64	theme	demethylase	156:166	arg1	translocation					179:191	DNA demethylase ten-eleven translocation 1	152:193	DNA demethylase ten-eleven translocation 1 (TET1)	152:200	We recently reported that DNA demethylase ten-eleven translocation 1 (TET1) upregulates nuclear factor erythroid 2-related factor 2 (Nrf2) in 5-fluorouracil-resistant colon cancer cells (SNUC5/5-FUR).
27259240	1	64	theme	demethylase	156:166	arg1	TET1					196:199	TET1	196:199	TET1	196:199	We recently reported that DNA demethylase ten-eleven translocation 1 (TET1) upregulates nuclear factor erythroid 2-related factor 2 (Nrf2) in 5-fluorouracil-resistant colon cancer cells (SNUC5/5-FUR).
27259240	8	65	theme	larger	1185:1190	arg1	fraction					1192:1199	a larger fraction	1183:1199	a larger fraction of OGT	1183:1206	In SNUC5/5-FUR cells, a larger fraction of OGT was bound to TET1, which recruits OGT to the Nrf2 promoter region, than in SNUC5 cells.
27259240	4	66	theme	histone	805:811	arg1	lysine					816:821	histone H3 lysine 9	805:823	histone H3 lysine 9	805:823	Mixed-lineage leukemia (MLL), a histone methyltransferase, was upregulated, leading to increased trimethylation of histone H3 lysine 4, while G9a was downregulated, leading to decreased dimethylation of histone H3 lysine 9.
27259240	1	67	theme	ten-eleven	168:177	arg1	translocation					179:191	DNA demethylase ten-eleven translocation 1	152:193	DNA demethylase ten-eleven translocation 1 (TET1)	152:200	We recently reported that DNA demethylase ten-eleven translocation 1 (TET1) upregulates nuclear factor erythroid 2-related factor 2 (Nrf2) in 5-fluorouracil-resistant colon cancer cells (SNUC5/5-FUR).
27259240	1	67	theme	ten-eleven	168:177	arg1	TET1					196:199	TET1	196:199	TET1	196:199	We recently reported that DNA demethylase ten-eleven translocation 1 (TET1) upregulates nuclear factor erythroid 2-related factor 2 (Nrf2) in 5-fluorouracil-resistant colon cancer cells (SNUC5/5-FUR).
27259240	9	68	theme	SNUC5/5-FUR	1325:1335	arg1	cells					1337:1341	SNUC5/5-FUR cells	1325:1341	SNUC5/5-FUR cells	1325:1341	These findings indicate that SNUC5/5-FUR cells are under oxidative stress, which induces expression of histone methylation-related proteins as well as DNA demethylase, leading to upregulation of Nrf2 and 5-FU resistance.
27515988	11	0	theme	promising	1562:1570	arg1	feedback					1489:1496	a positive auto-regulatory feedback	1462:1496	a positive auto-regulatory feedback	1462:1496	Collectively, we have uncovered a positive auto-regulatory feedback between O-GlcNAcylation and TRIB2, which might be regarded as a promising therapeutic target for liver cancer.
27515988	11	0	theme	promising	1562:1570	arg1	target					1584:1589	a promising therapeutic target	1560:1589	a promising therapeutic target for liver cancer	1560:1606	Collectively, we have uncovered a positive auto-regulatory feedback between O-GlcNAcylation and TRIB2, which might be regarded as a promising therapeutic target for liver cancer.
27515988	10	1	theme	TRIB2	1368:1372	arg1	O-GlcNAcylation					1349:1363	O-GlcNAcylation	1349:1363	O-GlcNAcylation of TRIB2	1349:1372	Mouse experiments demonstrate that O-GlcNAcylation of TRIB2 is much higher in the livers of diabetic mice compared to control mice, suggesting that O-GlcNAcylation of TRIB2 might be critical for diabetes-associated liver cancer.
27515988	9	2	theme	phenotypes	1148:1157	arg1	regulation					1107:1116	TRIB2-dependent regulation	1091:1116	TRIB2-dependent regulation of metabolism, transformative phenotypes, and O-GlcNAcylation	1091:1178	Importantly, TRIB2-dependent regulation of metabolism, transformative phenotypes, and O-GlcNAcylation all rely on GUCY1A3.
27515988	7	3	theme	HBP	833:835	arg1	metabolism					819:828	the metabolism	815:828	the metabolism of HBP	815:835	Interestingly, TRIB2 stimulated the metabolism of HBP, demonstrating that TRIB2 has positive feedback on O-GlcNAcylation.
27515988	4	4	theme	O-GlcNAcylation	519:533	arg1	stimulation					504:514	stimulation	504:514	stimulation of O-GlcNAcylation	504:533	We found that stimulation of O-GlcNAcylation elevates TRIB2 by enhancing its protein stability.
27515988	8	5	theme	HBP	1017:1019	arg1	component					1004:1012	a key component	998:1012	a key component of HBP	998:1019	Notably, TRIB2 was found to maintain the stability of guanylate cyclase 1 alpha 3 (GUCY1A3), a key component of HBP, by interacting GUCY1A3 and reducing its ubiquitination.
27515988	8	5	theme	HBP	1017:1019	arg1	cyclase					969:975	guanylate cyclase 1 alpha 3 (GUCY1A3)	959:995	guanylate cyclase 1 alpha 3 (GUCY1A3)	959:995	Notably, TRIB2 was found to maintain the stability of guanylate cyclase 1 alpha 3 (GUCY1A3), a key component of HBP, by interacting GUCY1A3 and reducing its ubiquitination.
27515988	10	6	theme	diabetic	1293:1300	arg1	mice					1302:1305	diabetic mice	1293:1305	diabetic mice	1293:1305	Mouse experiments demonstrate that O-GlcNAcylation of TRIB2 is much higher in the livers of diabetic mice compared to control mice, suggesting that O-GlcNAcylation of TRIB2 might be critical for diabetes-associated liver cancer.
27515988	1	7	theme	transformative	257:270	arg1	phenotypes					272:281	transformative phenotypes	257:281	transformative phenotypes in liver cancer cells	257:303	TRIB2 has been identified as an onco-protein, and O-GlcNAcylation of target proteins has been reported to stimulate transformative phenotypes in liver cancer cells.
27515988	10	8	theme	liver	1416:1420	arg1	cancer					1422:1427	diabetes-associated liver cancer	1396:1427	diabetes-associated liver cancer	1396:1427	Mouse experiments demonstrate that O-GlcNAcylation of TRIB2 is much higher in the livers of diabetic mice compared to control mice, suggesting that O-GlcNAcylation of TRIB2 might be critical for diabetes-associated liver cancer.
27515988	0	9	theme	transformative	92:105	arg1	phenotypes					107:116	transformative phenotypes	92:116	transformative phenotypes	92:116	Reciprocal regulation between O-GlcNAcylation and tribbles pseudokinase 2 (TRIB2) maintains transformative phenotypes in liver cancer cells.
27515988	5	10	theme	hexosamine	621:630	arg1	HBP					654:656	HBP	654:656	HBP	654:656	TRIB2 can be O-GlcNAcylated by the hexosamine biosynthesis pathway (HBP).
27515988	5	10	theme	hexosamine	621:630	arg1	pathway					645:651	the hexosamine biosynthesis pathway	617:651	the hexosamine biosynthesis pathway (HBP)	617:657	TRIB2 can be O-GlcNAcylated by the hexosamine biosynthesis pathway (HBP).
27515988	11	11	theme	auto-regulatory	1473:1487	arg1	feedback					1489:1496	a positive auto-regulatory feedback	1462:1496	a positive auto-regulatory feedback	1462:1496	Collectively, we have uncovered a positive auto-regulatory feedback between O-GlcNAcylation and TRIB2, which might be regarded as a promising therapeutic target for liver cancer.
27515988	11	11	theme	auto-regulatory	1473:1487	arg1	target					1584:1589	a promising therapeutic target	1560:1589	a promising therapeutic target for liver cancer	1560:1606	Collectively, we have uncovered a positive auto-regulatory feedback between O-GlcNAcylation and TRIB2, which might be regarded as a promising therapeutic target for liver cancer.
27515988	6	12	theme	cells	736:740	arg1	phenotypes					709:718	transformative phenotypes	694:718	transformative phenotypes of liver cancer cells	694:740	Also, O-GlcNAcylation boosting of transformative phenotypes of liver cancer cells might occur in a TRIB2-dependent manner.
27515988	0	13	theme	liver	121:125	arg1	cells					134:138	liver cancer cells	121:138	liver cancer cells	121:138	Reciprocal regulation between O-GlcNAcylation and tribbles pseudokinase 2 (TRIB2) maintains transformative phenotypes in liver cancer cells.
27515988	5	14	theme	biosynthesis	632:643	arg1	HBP					654:656	HBP	654:656	HBP	654:656	TRIB2 can be O-GlcNAcylated by the hexosamine biosynthesis pathway (HBP).
27515988	5	14	theme	biosynthesis	632:643	arg1	pathway					645:651	the hexosamine biosynthesis pathway	617:651	the hexosamine biosynthesis pathway (HBP)	617:657	TRIB2 can be O-GlcNAcylated by the hexosamine biosynthesis pathway (HBP).
27515988	6	15	theme	cancer	729:734	arg1	cells					736:740	liver cancer cells	723:740	liver cancer cells	723:740	Also, O-GlcNAcylation boosting of transformative phenotypes of liver cancer cells might occur in a TRIB2-dependent manner.
27515988	8	16	theme	key	1000:1002	arg1	component					1004:1012	a key component	998:1012	a key component of HBP	998:1019	Notably, TRIB2 was found to maintain the stability of guanylate cyclase 1 alpha 3 (GUCY1A3), a key component of HBP, by interacting GUCY1A3 and reducing its ubiquitination.
27515988	8	16	theme	key	1000:1002	arg1	cyclase					969:975	guanylate cyclase 1 alpha 3 (GUCY1A3)	959:995	guanylate cyclase 1 alpha 3 (GUCY1A3)	959:995	Notably, TRIB2 was found to maintain the stability of guanylate cyclase 1 alpha 3 (GUCY1A3), a key component of HBP, by interacting GUCY1A3 and reducing its ubiquitination.
27515988	6	17	theme	liver	723:727	arg1	cells					736:740	liver cancer cells	723:740	liver cancer cells	723:740	Also, O-GlcNAcylation boosting of transformative phenotypes of liver cancer cells might occur in a TRIB2-dependent manner.
27515988	11	18	theme	positive	1464:1471	arg1	feedback					1489:1496	a positive auto-regulatory feedback	1462:1496	a positive auto-regulatory feedback	1462:1496	Collectively, we have uncovered a positive auto-regulatory feedback between O-GlcNAcylation and TRIB2, which might be regarded as a promising therapeutic target for liver cancer.
27515988	11	18	theme	positive	1464:1471	arg1	target					1584:1589	a promising therapeutic target	1560:1589	a promising therapeutic target for liver cancer	1560:1606	Collectively, we have uncovered a positive auto-regulatory feedback between O-GlcNAcylation and TRIB2, which might be regarded as a promising therapeutic target for liver cancer.
27515988	1	19	theme	liver	286:290	arg1	cells					299:303	liver cancer cells	286:303	liver cancer cells	286:303	TRIB2 has been identified as an onco-protein, and O-GlcNAcylation of target proteins has been reported to stimulate transformative phenotypes in liver cancer cells.
27515988	0	20	theme	Reciprocal	0:9	arg1	regulation					11:20	Reciprocal regulation	0:20	Reciprocal regulation between O-GlcNAcylation and tribbles pseudokinase 2 (TRIB2)	0:80	Reciprocal regulation between O-GlcNAcylation and tribbles pseudokinase 2 (TRIB2) maintains transformative phenotypes in liver cancer cells.
27515988	4	21	theme	protein	567:573	arg1	stability					575:583	its protein stability	563:583	its protein stability	563:583	We found that stimulation of O-GlcNAcylation elevates TRIB2 by enhancing its protein stability.
27515988	3	22	dep	investigate	415:425	arg1	whether					427:433	whether	427:433	whether	427:433	The aim of this study was to investigate whether and how O-GlcNAcylation and TRIB2 regulate each other.
27515988	6	23	theme	phenotypes	709:718	arg1	boosting					682:689	O-GlcNAcylation boosting	666:689	O-GlcNAcylation boosting of transformative phenotypes of liver cancer cells	666:740	Also, O-GlcNAcylation boosting of transformative phenotypes of liver cancer cells might occur in a TRIB2-dependent manner.
27515988	1	24	theme	cancer	292:297	arg1	cells					299:303	liver cancer cells	286:303	liver cancer cells	286:303	TRIB2 has been identified as an onco-protein, and O-GlcNAcylation of target proteins has been reported to stimulate transformative phenotypes in liver cancer cells.
27515988	1	25	from	phenotypes	272:281	arg1	cells					299:303	liver cancer cells	286:303	liver cancer cells	286:303	TRIB2 has been identified as an onco-protein, and O-GlcNAcylation of target proteins has been reported to stimulate transformative phenotypes in liver cancer cells.
27515988	11	26	theme	liver	1595:1599	arg1	cancer					1601:1606	liver cancer	1595:1606	liver cancer	1595:1606	Collectively, we have uncovered a positive auto-regulatory feedback between O-GlcNAcylation and TRIB2, which might be regarded as a promising therapeutic target for liver cancer.
27515988	6	27	theme	transformative	694:707	arg1	phenotypes					709:718	transformative phenotypes	694:718	transformative phenotypes of liver cancer cells	694:740	Also, O-GlcNAcylation boosting of transformative phenotypes of liver cancer cells might occur in a TRIB2-dependent manner.
27515988	9	28	theme	O-GlcNAcylation	1164:1178	arg1	regulation					1107:1116	TRIB2-dependent regulation	1091:1116	TRIB2-dependent regulation of metabolism, transformative phenotypes, and O-GlcNAcylation	1091:1178	Importantly, TRIB2-dependent regulation of metabolism, transformative phenotypes, and O-GlcNAcylation all rely on GUCY1A3.
27515988	0	29	theme	cancer	127:132	arg1	cells					134:138	liver cancer cells	121:138	liver cancer cells	121:138	Reciprocal regulation between O-GlcNAcylation and tribbles pseudokinase 2 (TRIB2) maintains transformative phenotypes in liver cancer cells.
27515988	10	30	theme	control	1319:1325	arg1	mice					1327:1330	control mice	1319:1330	control mice	1319:1330	Mouse experiments demonstrate that O-GlcNAcylation of TRIB2 is much higher in the livers of diabetic mice compared to control mice, suggesting that O-GlcNAcylation of TRIB2 might be critical for diabetes-associated liver cancer.
27515988	9	31	theme	TRIB2-dependent	1091:1105	arg1	regulation					1107:1116	TRIB2-dependent regulation	1091:1116	TRIB2-dependent regulation of metabolism, transformative phenotypes, and O-GlcNAcylation	1091:1178	Importantly, TRIB2-dependent regulation of metabolism, transformative phenotypes, and O-GlcNAcylation all rely on GUCY1A3.
27515988	0	32	theme	tribbles	50:57	arg1	pseudokinase					59:70	tribbles pseudokinase 2	50:72	tribbles pseudokinase 2 (TRIB2)	50:80	Reciprocal regulation between O-GlcNAcylation and tribbles pseudokinase 2 (TRIB2) maintains transformative phenotypes in liver cancer cells.
27515988	0	32	theme	tribbles	50:57	arg1	TRIB2					75:79	TRIB2	75:79	TRIB2	75:79	Reciprocal regulation between O-GlcNAcylation and tribbles pseudokinase 2 (TRIB2) maintains transformative phenotypes in liver cancer cells.
27515988	10	33	theme	mice	1302:1305	arg1	livers					1283:1288	the livers	1279:1288	the livers of diabetic mice	1279:1305	Mouse experiments demonstrate that O-GlcNAcylation of TRIB2 is much higher in the livers of diabetic mice compared to control mice, suggesting that O-GlcNAcylation of TRIB2 might be critical for diabetes-associated liver cancer.
27515988	7	34	contain	has	863:865	arg1	TRIB2					857:861	TRIB2	857:861	TRIB2	857:861	Interestingly, TRIB2 stimulated the metabolism of HBP, demonstrating that TRIB2 has positive feedback on O-GlcNAcylation.
27515988	7	34	contain	has	863:865	arg2	feedback					876:883	positive feedback	867:883	positive feedback	867:883	Interestingly, TRIB2 stimulated the metabolism of HBP, demonstrating that TRIB2 has positive feedback on O-GlcNAcylation.
27515988	3	35	dep	whether	427:433	arg1	regulate					469:476	regulate	469:476	regulate each other	469:487	The aim of this study was to investigate whether and how O-GlcNAcylation and TRIB2 regulate each other.
27515988	9	36	theme	metabolism	1121:1130	arg1	regulation					1107:1116	TRIB2-dependent regulation	1091:1116	TRIB2-dependent regulation of metabolism, transformative phenotypes, and O-GlcNAcylation	1091:1178	Importantly, TRIB2-dependent regulation of metabolism, transformative phenotypes, and O-GlcNAcylation all rely on GUCY1A3.
27515988	1	37	theme	target	210:215	arg1	proteins					217:224	target proteins	210:224	target proteins	210:224	TRIB2 has been identified as an onco-protein, and O-GlcNAcylation of target proteins has been reported to stimulate transformative phenotypes in liver cancer cells.
27515988	11	38	theme	therapeutic	1572:1582	arg1	feedback					1489:1496	a positive auto-regulatory feedback	1462:1496	a positive auto-regulatory feedback	1462:1496	Collectively, we have uncovered a positive auto-regulatory feedback between O-GlcNAcylation and TRIB2, which might be regarded as a promising therapeutic target for liver cancer.
27515988	11	38	theme	therapeutic	1572:1582	arg1	target					1584:1589	a promising therapeutic target	1560:1589	a promising therapeutic target for liver cancer	1560:1606	Collectively, we have uncovered a positive auto-regulatory feedback between O-GlcNAcylation and TRIB2, which might be regarded as a promising therapeutic target for liver cancer.
27515988	1	39	theme	proteins	217:224	arg1	O-GlcNAcylation					191:205	O-GlcNAcylation	191:205	O-GlcNAcylation of target proteins	191:224	TRIB2 has been identified as an onco-protein, and O-GlcNAcylation of target proteins has been reported to stimulate transformative phenotypes in liver cancer cells.
27515988	3	40	theme	study	402:406	arg1	aim					390:392	The aim	386:392	The aim of this study	386:406	The aim of this study was to investigate whether and how O-GlcNAcylation and TRIB2 regulate each other.
27515988	9	41	theme	transformative	1133:1146	arg1	phenotypes					1148:1157	transformative phenotypes	1133:1157	transformative phenotypes	1133:1157	Importantly, TRIB2-dependent regulation of metabolism, transformative phenotypes, and O-GlcNAcylation all rely on GUCY1A3.
27515988	8	42	theme	guanylate	959:967	arg1	component					1004:1012	a key component	998:1012	a key component of HBP	998:1019	Notably, TRIB2 was found to maintain the stability of guanylate cyclase 1 alpha 3 (GUCY1A3), a key component of HBP, by interacting GUCY1A3 and reducing its ubiquitination.
27515988	8	42	theme	guanylate	959:967	arg1	cyclase					969:975	guanylate cyclase 1 alpha 3 (GUCY1A3)	959:995	guanylate cyclase 1 alpha 3 (GUCY1A3)	959:995	Notably, TRIB2 was found to maintain the stability of guanylate cyclase 1 alpha 3 (GUCY1A3), a key component of HBP, by interacting GUCY1A3 and reducing its ubiquitination.
27515988	6	43	theme	O-GlcNAcylation	666:680	arg1	boosting					682:689	O-GlcNAcylation boosting	666:689	O-GlcNAcylation boosting of transformative phenotypes of liver cancer cells	666:740	Also, O-GlcNAcylation boosting of transformative phenotypes of liver cancer cells might occur in a TRIB2-dependent manner.
27515988	6	44	theme	TRIB2-dependent	759:773	arg1	manner					775:780	a TRIB2-dependent manner	757:780	a TRIB2-dependent manner	757:780	Also, O-GlcNAcylation boosting of transformative phenotypes of liver cancer cells might occur in a TRIB2-dependent manner.
27515988	10	45	theme	Mouse	1201:1205	arg1	experiments					1207:1217	Mouse experiments	1201:1217	Mouse experiments	1201:1217	Mouse experiments demonstrate that O-GlcNAcylation of TRIB2 is much higher in the livers of diabetic mice compared to control mice, suggesting that O-GlcNAcylation of TRIB2 might be critical for diabetes-associated liver cancer.
27515988	10	46	theme	TRIB2	1255:1259	arg1	O-GlcNAcylation					1236:1250	O-GlcNAcylation	1236:1250	O-GlcNAcylation of TRIB2	1236:1259	Mouse experiments demonstrate that O-GlcNAcylation of TRIB2 is much higher in the livers of diabetic mice compared to control mice, suggesting that O-GlcNAcylation of TRIB2 might be critical for diabetes-associated liver cancer.
27515988	7	47	theme	positive	867:874	arg1	feedback					876:883	positive feedback	867:883	positive feedback	867:883	Interestingly, TRIB2 stimulated the metabolism of HBP, demonstrating that TRIB2 has positive feedback on O-GlcNAcylation.
27515988	8	48	theme	cyclase	969:975	arg1	stability					946:954	the stability	942:954	the stability of guanylate cyclase 1 alpha 3 (GUCY1A3), a key component of HBP,	942:1020	Notably, TRIB2 was found to maintain the stability of guanylate cyclase 1 alpha 3 (GUCY1A3), a key component of HBP, by interacting GUCY1A3 and reducing its ubiquitination.
27515988	10	49	theme	diabetes-associated	1396:1414	arg1	cancer					1422:1427	diabetes-associated liver cancer	1396:1427	diabetes-associated liver cancer	1396:1427	Mouse experiments demonstrate that O-GlcNAcylation of TRIB2 is much higher in the livers of diabetic mice compared to control mice, suggesting that O-GlcNAcylation of TRIB2 might be critical for diabetes-associated liver cancer.
27515988	8	50	dep	cyclase	969:975	arg1	alpha					979:983	1 alpha 3	977:985	guanylate cyclase 1 alpha 3 (GUCY1A3)	959:995	Notably, TRIB2 was found to maintain the stability of guanylate cyclase 1 alpha 3 (GUCY1A3), a key component of HBP, by interacting GUCY1A3 and reducing its ubiquitination.
27515988	8	50	dep	cyclase	969:975	arg1	GUCY1A3					988:994	GUCY1A3	988:994	GUCY1A3	988:994	Notably, TRIB2 was found to maintain the stability of guanylate cyclase 1 alpha 3 (GUCY1A3), a key component of HBP, by interacting GUCY1A3 and reducing its ubiquitination.
32152092	0	0	theme	metabolic	83:91	arg1	switching					93:101	liver metabolic switching	77:101	liver metabolic switching	77:101	Spatiotemporal gating of SIRT1 functions by O-GlcNAcylation is essential for liver metabolic switching and prevents hyperglycemia.
32152092	3	1	theme	upstream	355:362	arg1	mechanisms					364:373	upstream mechanisms	355:373	upstream mechanisms that control temporal engagement of transcription factors, which are essential to mediate physiological fed-fast-refed transitions	355:504	Specifically, upstream mechanisms that control temporal engagement of transcription factors, which are essential to mediate physiological fed-fast-refed transitions are less understood.
32152092	4	2	theme	therapeutic	638:648	arg1	target					650:655	a key therapeutic target	632:655	a key therapeutic target	632:655	SIRT1, a NAD+-dependent deacetylase, is pivotal in regulating hepatic gene expression and has emerged as a key therapeutic target.
32152092	0	3	theme	liver	77:81	arg1	switching					93:101	liver metabolic switching	77:101	liver metabolic switching	77:101	Spatiotemporal gating of SIRT1 functions by O-GlcNAcylation is essential for liver metabolic switching and prevents hyperglycemia.
32152092	7	4	theme	various	1052:1058	arg1	factors					1074:1080	various transcription factors	1052:1080	various transcription factors	1052:1080	Our findings demonstrate that during a fasted-to-refed transition, glycosylation of SIRT1 modulates its interactions with various transcription factors and a nodal cytosolic kinase involved in insulin signaling.
32152092	8	5	gly	glycosylation	1162:1174	arg1	state					1187:1191	the fed state	1179:1191	the fed state	1179:1191	Moreover, sustained glycosylation in the fed state causes nuclear exclusion and cytosolic ubiquitin-mediated degradation of SIRT1.
32152092	4	6	theme	key	634:636	arg1	target					650:655	a key therapeutic target	632:655	a key therapeutic target	632:655	SIRT1, a NAD+-dependent deacetylase, is pivotal in regulating hepatic gene expression and has emerged as a key therapeutic target.
32152092	7	7	theme	transcription	1060:1072	arg1	factors					1074:1080	various transcription factors	1052:1080	various transcription factors	1052:1080	Our findings demonstrate that during a fasted-to-refed transition, glycosylation of SIRT1 modulates its interactions with various transcription factors and a nodal cytosolic kinase involved in insulin signaling.
32152092	3	8	theme	transcription	411:423	arg1	factors					425:431	transcription factors	411:431	transcription factors	411:431	Specifically, upstream mechanisms that control temporal engagement of transcription factors, which are essential to mediate physiological fed-fast-refed transitions are less understood.
32152092	4	9	theme	NAD+-dependent	536:549	arg1	deacetylase					551:561	a NAD+-dependent deacetylase	534:561	a NAD+-dependent deacetylase	534:561	SIRT1, a NAD+-dependent deacetylase, is pivotal in regulating hepatic gene expression and has emerged as a key therapeutic target.
32152092	4	9	theme	NAD+-dependent	536:549	arg1	SIRT1					527:531	SIRT1	527:531	SIRT1	527:531	SIRT1, a NAD+-dependent deacetylase, is pivotal in regulating hepatic gene expression and has emerged as a key therapeutic target.
32152092	10	10	theme	gene	1483:1486	arg1	expression					1488:1497	aberrant gene expression	1474:1497	aberrant gene expression	1474:1497	Of note, loss of SIRT1 glycosylation discomposed these interactions resulting in aberrant gene expression, mitochondrial dysfunctions, and enhanced hepatic gluconeogenesis.
32152092	10	11	theme	enhanced	1532:1539	arg1	gluconeogenesis					1549:1563	enhanced hepatic gluconeogenesis	1532:1563	enhanced hepatic gluconeogenesis	1532:1563	Of note, loss of SIRT1 glycosylation discomposed these interactions resulting in aberrant gene expression, mitochondrial dysfunctions, and enhanced hepatic gluconeogenesis.
32152092	10	12	theme	glycosylation	1416:1428	arg1	loss					1402:1405	loss	1402:1405	loss of SIRT1 glycosylation	1402:1428	Of note, loss of SIRT1 glycosylation discomposed these interactions resulting in aberrant gene expression, mitochondrial dysfunctions, and enhanced hepatic gluconeogenesis.
32152092	8	13	theme	ubiquitin-mediated	1232:1249	arg1	degradation					1251:1261	cytosolic ubiquitin-mediated degradation	1222:1261	cytosolic ubiquitin-mediated degradation of SIRT1	1222:1270	Moreover, sustained glycosylation in the fed state causes nuclear exclusion and cytosolic ubiquitin-mediated degradation of SIRT1.
32152092	3	14	theme	temporal	388:395	arg1	engagement					397:406	temporal engagement	388:406	temporal engagement	388:406	Specifically, upstream mechanisms that control temporal engagement of transcription factors, which are essential to mediate physiological fed-fast-refed transitions are less understood.
32152092	5	15	theme	nutrient	679:686	arg1	inputs					688:693	if/how nutrient inputs	672:693	if/how nutrient inputs	672:693	Despite this, if/how nutrient inputs regulate SIRT1 interactions, stability, and therefore downstream functions are still unknown.
32152092	5	16	theme	if/how	672:677	arg1	inputs					688:693	if/how nutrient inputs	672:693	if/how nutrient inputs	672:693	Despite this, if/how nutrient inputs regulate SIRT1 interactions, stability, and therefore downstream functions are still unknown.
32152092	10	17	theme	SIRT1	1410:1414	arg1	glycosylation					1416:1428	SIRT1 glycosylation	1410:1428	SIRT1 glycosylation	1410:1428	Of note, loss of SIRT1 glycosylation discomposed these interactions resulting in aberrant gene expression, mitochondrial dysfunctions, and enhanced hepatic gluconeogenesis.
32152092	1	18	theme	metabolic	188:196	arg1	disorders					198:206	metabolic disorders	188:206	metabolic disorders	188:206	Inefficient physiological transitions are known to cause metabolic disorders.
32152092	6	19	theme	N-terminal	864:873	arg1	domain					875:880	its N-terminal domain	860:880	its N-terminal domain	860:880	Here, we establish nutrient-dependent O-GlcNAcylation of SIRT1, within its N-terminal domain, as a crucial determinant of hepatic functions.
32152092	9	20	theme	molecular	1376:1384	arg1	relay					1386:1390	a previously unknown molecular relay	1355:1390	a previously unknown molecular relay	1355:1390	This mechanism exerts spatiotemporal control over SIRT1 functions by constituting a previously unknown molecular relay.
32152092	13	21	theme	nutrient-dependent	1953:1970	arg1	glycosylation					1972:1984	nutrient-dependent glycosylation	1953:1984	nutrient-dependent glycosylation of SIRT1	1953:1993	Thus, we establish that nutrient-dependent glycosylation of SIRT1 is essential to gate its functions and maintain physiological fitness.
32152092	12	22	theme	SIRT1	1868:1872	arg1	hyperglycosylation					1846:1863	hyperglycosylation	1846:1863	hyperglycosylation of SIRT1	1846:1872	Conversely, our study also reveals that hyperglycosylation of SIRT1 is associated with aging and high-fat-induced obesity.
32152092	3	23	theme	fed-fast-refed	479:492	arg1	transitions					494:504	physiological fed-fast-refed transitions	465:504	physiological fed-fast-refed transitions	465:504	Specifically, upstream mechanisms that control temporal engagement of transcription factors, which are essential to mediate physiological fed-fast-refed transitions are less understood.
32152092	0	24	theme	Spatiotemporal	0:13	arg1	gating					15:20	Spatiotemporal gating	0:20	Spatiotemporal gating of SIRT1 functions by O-GlcNAcylation	0:58	Spatiotemporal gating of SIRT1 functions by O-GlcNAcylation is essential for liver metabolic switching and prevents hyperglycemia.
32152092	5	25	theme	SIRT1	704:708	arg1	stability					724:732	stability	724:732	stability	724:732	Despite this, if/how nutrient inputs regulate SIRT1 interactions, stability, and therefore downstream functions are still unknown.
32152092	5	25	theme	SIRT1	704:708	arg1	interactions					710:721	SIRT1 interactions	704:721	SIRT1 interactions	704:721	Despite this, if/how nutrient inputs regulate SIRT1 interactions, stability, and therefore downstream functions are still unknown.
32152092	7	26	gly	glycosylation	997:1009	arg1	SIRT1					1014:1018	SIRT1	1014:1018	SIRT1	1014:1018	Our findings demonstrate that during a fasted-to-refed transition, glycosylation of SIRT1 modulates its interactions with various transcription factors and a nodal cytosolic kinase involved in insulin signaling.
32152092	8	27	theme	SIRT1	1266:1270	arg1	exclusion					1208:1216	nuclear exclusion	1200:1216	nuclear exclusion	1200:1216	Moreover, sustained glycosylation in the fed state causes nuclear exclusion and cytosolic ubiquitin-mediated degradation of SIRT1.
32152092	8	27	theme	SIRT1	1266:1270	arg1	degradation					1251:1261	cytosolic ubiquitin-mediated degradation	1222:1261	cytosolic ubiquitin-mediated degradation of SIRT1	1222:1270	Moreover, sustained glycosylation in the fed state causes nuclear exclusion and cytosolic ubiquitin-mediated degradation of SIRT1.
32152092	11	28	from	Expression	1566:1575	arg1	liver					1611:1615	the liver	1607:1615	the liver	1607:1615	Expression of nonglycosylatable SIRT1 in the liver abrogated metabolic flexibility, resulting in systemic insulin resistance, hyperglycemia, and hepatic inflammation, highlighting the physiological costs associated with its overactivation.
32152092	3	29	theme	factors	425:431	arg1	engagement					397:406	temporal engagement	388:406	temporal engagement	388:406	Specifically, upstream mechanisms that control temporal engagement of transcription factors, which are essential to mediate physiological fed-fast-refed transitions are less understood.
32152092	8	30	theme	fed	1183:1185	arg1	state					1187:1191	the fed state	1179:1191	the fed state	1179:1191	Moreover, sustained glycosylation in the fed state causes nuclear exclusion and cytosolic ubiquitin-mediated degradation of SIRT1.
32152092	7	31	theme	SIRT1	1014:1018	arg1	glycosylation					997:1009	glycosylation	997:1009	glycosylation of SIRT1	997:1018	Our findings demonstrate that during a fasted-to-refed transition, glycosylation of SIRT1 modulates its interactions with various transcription factors and a nodal cytosolic kinase involved in insulin signaling.
32152092	9	32	theme	spatiotemporal	1295:1308	arg1	control					1310:1316	spatiotemporal control	1295:1316	spatiotemporal control over SIRT1 functions	1295:1337	This mechanism exerts spatiotemporal control over SIRT1 functions by constituting a previously unknown molecular relay.
32152092	12	33	gly	hyperglycosylation	1846:1863	arg1	SIRT1					1868:1872	SIRT1	1868:1872	SIRT1	1868:1872	Conversely, our study also reveals that hyperglycosylation of SIRT1 is associated with aging and high-fat-induced obesity.
32152092	13	34	theme	SIRT1	1989:1993	arg1	glycosylation					1972:1984	nutrient-dependent glycosylation	1953:1984	nutrient-dependent glycosylation of SIRT1	1953:1993	Thus, we establish that nutrient-dependent glycosylation of SIRT1 is essential to gate its functions and maintain physiological fitness.
32152092	10	35	theme	aberrant	1474:1481	arg1	expression					1488:1497	aberrant gene expression	1474:1497	aberrant gene expression	1474:1497	Of note, loss of SIRT1 glycosylation discomposed these interactions resulting in aberrant gene expression, mitochondrial dysfunctions, and enhanced hepatic gluconeogenesis.
32152092	11	36	theme	nonglycosylatable	1580:1596	arg1	SIRT1					1598:1602	nonglycosylatable SIRT1	1580:1602	nonglycosylatable SIRT1	1580:1602	Expression of nonglycosylatable SIRT1 in the liver abrogated metabolic flexibility, resulting in systemic insulin resistance, hyperglycemia, and hepatic inflammation, highlighting the physiological costs associated with its overactivation.
32152092	13	37	theme	physiological	2043:2055	arg1	fitness					2057:2063	physiological fitness	2043:2063	physiological fitness	2043:2063	Thus, we establish that nutrient-dependent glycosylation of SIRT1 is essential to gate its functions and maintain physiological fitness.
32152092	8	38	theme	sustained	1152:1160	arg1	glycosylation					1162:1174	sustained glycosylation	1152:1174	sustained glycosylation in the fed state	1152:1191	Moreover, sustained glycosylation in the fed state causes nuclear exclusion and cytosolic ubiquitin-mediated degradation of SIRT1.
32152092	9	39	theme	unknown	1368:1374	arg1	relay					1386:1390	a previously unknown molecular relay	1355:1390	a previously unknown molecular relay	1355:1390	This mechanism exerts spatiotemporal control over SIRT1 functions by constituting a previously unknown molecular relay.
32152092	11	40	theme	metabolic	1627:1635	arg1	flexibility					1637:1647	metabolic flexibility	1627:1647	metabolic flexibility	1627:1647	Expression of nonglycosylatable SIRT1 in the liver abrogated metabolic flexibility, resulting in systemic insulin resistance, hyperglycemia, and hepatic inflammation, highlighting the physiological costs associated with its overactivation.
32152092	0	41	theme	functions	31:39	arg1	gating					15:20	Spatiotemporal gating	0:20	Spatiotemporal gating of SIRT1 functions by O-GlcNAcylation	0:58	Spatiotemporal gating of SIRT1 functions by O-GlcNAcylation is essential for liver metabolic switching and prevents hyperglycemia.
32152092	4	42	theme	gene	597:600	arg1	expression					602:611	hepatic gene expression	589:611	hepatic gene expression	589:611	SIRT1, a NAD+-dependent deacetylase, is pivotal in regulating hepatic gene expression and has emerged as a key therapeutic target.
32152092	3	43	theme	physiological	465:477	arg1	transitions					494:504	physiological fed-fast-refed transitions	465:504	physiological fed-fast-refed transitions	465:504	Specifically, upstream mechanisms that control temporal engagement of transcription factors, which are essential to mediate physiological fed-fast-refed transitions are less understood.
32152092	7	44	with	kinase	1104:1109	arg1	factors					1074:1080	various transcription factors	1052:1080	various transcription factors	1052:1080	Our findings demonstrate that during a fasted-to-refed transition, glycosylation of SIRT1 modulates its interactions with various transcription factors and a nodal cytosolic kinase involved in insulin signaling.
32152092	0	45	theme	SIRT1	25:29	arg1	functions					31:39	SIRT1 functions	25:39	SIRT1 functions	25:39	Spatiotemporal gating of SIRT1 functions by O-GlcNAcylation is essential for liver metabolic switching and prevents hyperglycemia.
32152092	6	46	theme	SIRT1	846:850	arg1	O-GlcNAcylation					827:841	nutrient-dependent O-GlcNAcylation	808:841	nutrient-dependent O-GlcNAcylation of SIRT1	808:850	Here, we establish nutrient-dependent O-GlcNAcylation of SIRT1, within its N-terminal domain, as a crucial determinant of hepatic functions.
32152092	6	46	theme	SIRT1	846:850	arg1	determinant					896:906	a crucial determinant	886:906	a crucial determinant of hepatic functions	886:927	Here, we establish nutrient-dependent O-GlcNAcylation of SIRT1, within its N-terminal domain, as a crucial determinant of hepatic functions.
32152092	9	47	theme	SIRT1	1323:1327	arg1	functions					1329:1337	SIRT1 functions	1323:1337	SIRT1 functions	1323:1337	This mechanism exerts spatiotemporal control over SIRT1 functions by constituting a previously unknown molecular relay.
32152092	4	48	theme	hepatic	589:595	arg1	expression					602:611	hepatic gene expression	589:611	hepatic gene expression	589:611	SIRT1, a NAD+-dependent deacetylase, is pivotal in regulating hepatic gene expression and has emerged as a key therapeutic target.
32152092	6	49	theme	functions	919:927	arg1	O-GlcNAcylation					827:841	nutrient-dependent O-GlcNAcylation	808:841	nutrient-dependent O-GlcNAcylation of SIRT1	808:850	Here, we establish nutrient-dependent O-GlcNAcylation of SIRT1, within its N-terminal domain, as a crucial determinant of hepatic functions.
32152092	6	49	theme	functions	919:927	arg1	determinant					896:906	a crucial determinant	886:906	a crucial determinant of hepatic functions	886:927	Here, we establish nutrient-dependent O-GlcNAcylation of SIRT1, within its N-terminal domain, as a crucial determinant of hepatic functions.
32152092	2	50	theme	molecular	261:269	arg1	switches					271:278	molecular switches	261:278	molecular switches	261:278	Therefore, investigating mechanisms that constitute molecular switches in a central metabolic organ like the liver becomes crucial.
32152092	7	51	theme	insulin	1123:1129	arg1	signaling					1131:1139	insulin signaling	1123:1139	insulin signaling	1123:1139	Our findings demonstrate that during a fasted-to-refed transition, glycosylation of SIRT1 modulates its interactions with various transcription factors and a nodal cytosolic kinase involved in insulin signaling.
32152092	10	52	theme	hepatic	1541:1547	arg1	gluconeogenesis					1549:1563	enhanced hepatic gluconeogenesis	1532:1563	enhanced hepatic gluconeogenesis	1532:1563	Of note, loss of SIRT1 glycosylation discomposed these interactions resulting in aberrant gene expression, mitochondrial dysfunctions, and enhanced hepatic gluconeogenesis.
32152092	8	53	theme	nuclear	1200:1206	arg1	exclusion					1208:1216	nuclear exclusion	1200:1216	nuclear exclusion	1200:1216	Moreover, sustained glycosylation in the fed state causes nuclear exclusion and cytosolic ubiquitin-mediated degradation of SIRT1.
32152092	6	54	theme	hepatic	911:917	arg1	functions					919:927	hepatic functions	911:927	hepatic functions	911:927	Here, we establish nutrient-dependent O-GlcNAcylation of SIRT1, within its N-terminal domain, as a crucial determinant of hepatic functions.
32152092	7	55	theme	cytosolic	1094:1102	arg1	kinase					1104:1109	a nodal cytosolic kinase	1086:1109	a nodal cytosolic kinase involved in insulin signaling	1086:1139	Our findings demonstrate that during a fasted-to-refed transition, glycosylation of SIRT1 modulates its interactions with various transcription factors and a nodal cytosolic kinase involved in insulin signaling.
32152092	1	56	theme	Inefficient	131:141	arg1	transitions					157:167	Inefficient physiological transitions	131:167	Inefficient physiological transitions	131:167	Inefficient physiological transitions are known to cause metabolic disorders.
32152092	11	57	theme	systemic	1663:1670	arg1	resistance					1680:1689	systemic insulin resistance	1663:1689	systemic insulin resistance	1663:1689	Expression of nonglycosylatable SIRT1 in the liver abrogated metabolic flexibility, resulting in systemic insulin resistance, hyperglycemia, and hepatic inflammation, highlighting the physiological costs associated with its overactivation.
32152092	5	58	theme	downstream	749:758	arg1	functions					760:768	therefore downstream functions	739:768	therefore downstream functions	739:768	Despite this, if/how nutrient inputs regulate SIRT1 interactions, stability, and therefore downstream functions are still unknown.
32152092	11	59	theme	physiological	1750:1762	arg1	costs					1764:1768	the physiological costs	1746:1768	the physiological costs associated with its overactivation	1746:1803	Expression of nonglycosylatable SIRT1 in the liver abrogated metabolic flexibility, resulting in systemic insulin resistance, hyperglycemia, and hepatic inflammation, highlighting the physiological costs associated with its overactivation.
32152092	6	60	theme	nutrient-dependent	808:825	arg1	O-GlcNAcylation					827:841	nutrient-dependent O-GlcNAcylation	808:841	nutrient-dependent O-GlcNAcylation of SIRT1	808:850	Here, we establish nutrient-dependent O-GlcNAcylation of SIRT1, within its N-terminal domain, as a crucial determinant of hepatic functions.
32152092	6	60	theme	nutrient-dependent	808:825	arg1	determinant					896:906	a crucial determinant	886:906	a crucial determinant of hepatic functions	886:927	Here, we establish nutrient-dependent O-GlcNAcylation of SIRT1, within its N-terminal domain, as a crucial determinant of hepatic functions.
32152092	1	61	theme	physiological	143:155	arg1	transitions					157:167	Inefficient physiological transitions	131:167	Inefficient physiological transitions	131:167	Inefficient physiological transitions are known to cause metabolic disorders.
32152092	11	62	theme	insulin	1672:1678	arg1	resistance					1680:1689	systemic insulin resistance	1663:1689	systemic insulin resistance	1663:1689	Expression of nonglycosylatable SIRT1 in the liver abrogated metabolic flexibility, resulting in systemic insulin resistance, hyperglycemia, and hepatic inflammation, highlighting the physiological costs associated with its overactivation.
32152092	13	63	gly	glycosylation	1972:1984	arg1	SIRT1					1989:1993	SIRT1	1989:1993	SIRT1	1989:1993	Thus, we establish that nutrient-dependent glycosylation of SIRT1 is essential to gate its functions and maintain physiological fitness.
32152092	2	64	theme	metabolic	293:301	arg1	organ					303:307	a central metabolic organ	283:307	a central metabolic organ like the liver	283:322	Therefore, investigating mechanisms that constitute molecular switches in a central metabolic organ like the liver becomes crucial.
32152092	8	65	theme	cytosolic	1222:1230	arg1	degradation					1251:1261	cytosolic ubiquitin-mediated degradation	1222:1261	cytosolic ubiquitin-mediated degradation of SIRT1	1222:1270	Moreover, sustained glycosylation in the fed state causes nuclear exclusion and cytosolic ubiquitin-mediated degradation of SIRT1.
32152092	7	66	theme	fasted-to-refed	969:983	arg1	transition					985:994	a fasted-to-refed transition	967:994	a fasted-to-refed transition	967:994	Our findings demonstrate that during a fasted-to-refed transition, glycosylation of SIRT1 modulates its interactions with various transcription factors and a nodal cytosolic kinase involved in insulin signaling.
32152092	11	67	theme	SIRT1	1598:1602	arg1	Expression					1566:1575	Expression	1566:1575	Expression of nonglycosylatable SIRT1 in the liver	1566:1615	Expression of nonglycosylatable SIRT1 in the liver abrogated metabolic flexibility, resulting in systemic insulin resistance, hyperglycemia, and hepatic inflammation, highlighting the physiological costs associated with its overactivation.
32152092	11	68	theme	hepatic	1711:1717	arg1	inflammation					1719:1730	hepatic inflammation	1711:1730	hepatic inflammation	1711:1730	Expression of nonglycosylatable SIRT1 in the liver abrogated metabolic flexibility, resulting in systemic insulin resistance, hyperglycemia, and hepatic inflammation, highlighting the physiological costs associated with its overactivation.
32152092	6	69	theme	crucial	888:894	arg1	O-GlcNAcylation					827:841	nutrient-dependent O-GlcNAcylation	808:841	nutrient-dependent O-GlcNAcylation of SIRT1	808:850	Here, we establish nutrient-dependent O-GlcNAcylation of SIRT1, within its N-terminal domain, as a crucial determinant of hepatic functions.
32152092	6	69	theme	crucial	888:894	arg1	determinant					896:906	a crucial determinant	886:906	a crucial determinant of hepatic functions	886:927	Here, we establish nutrient-dependent O-GlcNAcylation of SIRT1, within its N-terminal domain, as a crucial determinant of hepatic functions.
32152092	2	70	theme	central	285:291	arg1	organ					303:307	a central metabolic organ	283:307	a central metabolic organ like the liver	283:322	Therefore, investigating mechanisms that constitute molecular switches in a central metabolic organ like the liver becomes crucial.
32152092	7	71	theme	nodal	1088:1092	arg1	kinase					1104:1109	a nodal cytosolic kinase	1086:1109	a nodal cytosolic kinase involved in insulin signaling	1086:1139	Our findings demonstrate that during a fasted-to-refed transition, glycosylation of SIRT1 modulates its interactions with various transcription factors and a nodal cytosolic kinase involved in insulin signaling.
32152092	12	72	theme	high-fat-induced	1903:1918	arg1	obesity					1920:1926	high-fat-induced obesity	1903:1926	high-fat-induced obesity	1903:1926	Conversely, our study also reveals that hyperglycosylation of SIRT1 is associated with aging and high-fat-induced obesity.
32152092	7	73	with	interactions	1034:1045	arg1	factors					1074:1080	various transcription factors	1052:1080	various transcription factors	1052:1080	Our findings demonstrate that during a fasted-to-refed transition, glycosylation of SIRT1 modulates its interactions with various transcription factors and a nodal cytosolic kinase involved in insulin signaling.
32152092	10	74	theme	mitochondrial	1500:1512	arg1	dysfunctions					1514:1525	mitochondrial dysfunctions	1500:1525	mitochondrial dysfunctions	1500:1525	Of note, loss of SIRT1 glycosylation discomposed these interactions resulting in aberrant gene expression, mitochondrial dysfunctions, and enhanced hepatic gluconeogenesis.
32152092	8	75	from	glycosylation	1162:1174	arg1	state					1187:1191	the fed state	1179:1191	the fed state	1179:1191	Moreover, sustained glycosylation in the fed state causes nuclear exclusion and cytosolic ubiquitin-mediated degradation of SIRT1.
22826440	8	0	from	cells	1620:1624	arg1	data					1565:1568	re-analyzing mass spectrometric data	1533:1568	re-analyzing mass spectrometric data from human embryonic and induced pluripotent stem cells	1533:1624	By re-analyzing mass spectrometric data from human embryonic and induced pluripotent stem cells, our study also identified Zinc finger protein 462 (ZNF462) as the first human O-GlcNAc-6-phosphate modified protein.
22826440	3	1	theme	phosphorylated	461:474	arg1	O-GlcNAc					476:483	phosphorylated O-GlcNAc	461:483	phosphorylated O-GlcNAc	461:483	Upon collision induced dissociation, the modification generates a highly mass deficient fragment ion (m/z 284.0530) that can be used as a reporter for the identification of phosphorylated O-GlcNAc.
22826440	4	2	theme	accuracy	640:647	arg1	spectra					661:667	high resolution/high accuracy tandem mass spectra	619:667	high resolution/high accuracy tandem mass spectra	619:667	Using a publically available mouse brain phosphoproteome data set, we employed our recently developed Oscore software to re-evaluate high resolution/high accuracy tandem mass spectra and discovered the modification on 23 peptides corresponding to 11 mouse proteins.
22826440	5	3	theme	standard	850:857	arg1	analysis					767:774	The systematic analysis	752:774	The systematic analysis of 220 candidate phosphoGlcNAc tandem mass spectra as well as a synthetic standard	752:857	The systematic analysis of 220 candidate phosphoGlcNAc tandem mass spectra as well as a synthetic standard enabled the dissection of the major phosphoGlcNAc fragmentation pathways, suggesting that the modification is O-GlcNAc-6-phosphate.
22826440	7	4	theme	regulatory	1488:1497	arg1	role					1499:1502	a potential regulatory role	1476:1502	a potential regulatory role for O-GlcNAc-6-phosphate	1476:1527	Many of the identified proteins are involved in synaptic transmission and for Ca(2+)/calmodulin kinase IV, the O-GlcNAc-6-phosphate modification was found in the vicinity of two autophosphorylation sites required for full activation of the kinase suggesting a potential regulatory role for O-GlcNAc-6-phosphate.
22826440	4	5	theme	brain	521:525	arg1	set					548:550	a publically available mouse brain phosphoproteome data set	492:550	a publically available mouse brain phosphoproteome data set	492:550	Using a publically available mouse brain phosphoproteome data set, we employed our recently developed Oscore software to re-evaluate high resolution/high accuracy tandem mass spectra and discovered the modification on 23 peptides corresponding to 11 mouse proteins.
22826440	4	6	theme	mass	656:659	arg1	spectra					661:667	high resolution/high accuracy tandem mass spectra	619:667	high resolution/high accuracy tandem mass spectra	619:667	Using a publically available mouse brain phosphoproteome data set, we employed our recently developed Oscore software to re-evaluate high resolution/high accuracy tandem mass spectra and discovered the modification on 23 peptides corresponding to 11 mouse proteins.
22826440	1	7	theme	protein	206:212	arg1	AP180					214:218	the neuronal protein AP180	193:218	the neuronal protein AP180 from the rat	193:231	Phosphorylated O-GlcNAc is a novel post-translational modification that has so far only been found on the neuronal protein AP180 from the rat (Graham et al., J. Proteome Res.
22826440	7	8	theme	sites	1416:1420	arg1	vicinity					1380:1387	the vicinity	1376:1387	the vicinity of two autophosphorylation sites required for full activation of the kinase	1376:1463	Many of the identified proteins are involved in synaptic transmission and for Ca(2+)/calmodulin kinase IV, the O-GlcNAc-6-phosphate modification was found in the vicinity of two autophosphorylation sites required for full activation of the kinase suggesting a potential regulatory role for O-GlcNAc-6-phosphate.
22826440	4	9	theme	high	619:622	arg1	spectra					661:667	high resolution/high accuracy tandem mass spectra	619:667	high resolution/high accuracy tandem mass spectra	619:667	Using a publically available mouse brain phosphoproteome data set, we employed our recently developed Oscore software to re-evaluate high resolution/high accuracy tandem mass spectra and discovered the modification on 23 peptides corresponding to 11 mouse proteins.
22826440	5	10	theme	mass	814:817	arg1	spectra					819:825	220 candidate phosphoGlcNAc tandem mass spectra	779:825	220 candidate phosphoGlcNAc tandem mass spectra as well as a synthetic standard	779:857	The systematic analysis of 220 candidate phosphoGlcNAc tandem mass spectra as well as a synthetic standard enabled the dissection of the major phosphoGlcNAc fragmentation pathways, suggesting that the modification is O-GlcNAc-6-phosphate.
22826440	8	11	theme	pluripotent	1603:1613	arg1	cells					1620:1624	human embryonic and induced pluripotent stem cells	1575:1624	human embryonic and induced pluripotent stem cells	1575:1624	By re-analyzing mass spectrometric data from human embryonic and induced pluripotent stem cells, our study also identified Zinc finger protein 462 (ZNF462) as the first human O-GlcNAc-6-phosphate modified protein.
22826440	7	12	located	found	1367:1371	arg1	vicinity					1380:1387	the vicinity	1376:1387	the vicinity of two autophosphorylation sites required for full activation of the kinase	1376:1463	Many of the identified proteins are involved in synaptic transmission and for Ca(2+)/calmodulin kinase IV, the O-GlcNAc-6-phosphate modification was found in the vicinity of two autophosphorylation sites required for full activation of the kinase suggesting a potential regulatory role for O-GlcNAc-6-phosphate.
22826440	7	12	located	found	1367:1371	arg2	modification					1350:1361	the O-GlcNAc-6-phosphate modification	1325:1361	the O-GlcNAc-6-phosphate modification	1325:1361	Many of the identified proteins are involved in synaptic transmission and for Ca(2+)/calmodulin kinase IV, the O-GlcNAc-6-phosphate modification was found in the vicinity of two autophosphorylation sites required for full activation of the kinase suggesting a potential regulatory role for O-GlcNAc-6-phosphate.
22826440	5	13	theme	fragmentation	909:921	arg1	pathways					923:930	the major phosphoGlcNAc fragmentation pathways	885:930	the major phosphoGlcNAc fragmentation pathways	885:930	The systematic analysis of 220 candidate phosphoGlcNAc tandem mass spectra as well as a synthetic standard enabled the dissection of the major phosphoGlcNAc fragmentation pathways, suggesting that the modification is O-GlcNAc-6-phosphate.
22826440	9	14	theme	general	1807:1813	arg1	modification					1832:1843	a general post-translation modification	1805:1843	a general post-translation modification of mammalian proteins with a variety of possible cellular functions	1805:1911	Collectively, the data suggests that O-GlcNAc-6-phosphate is a general post-translation modification of mammalian proteins with a variety of possible cellular functions.
22826440	9	14	theme	general	1807:1813	arg1	O-GlcNAc-6-phosphate					1781:1800	O-GlcNAc-6-phosphate	1781:1800	O-GlcNAc-6-phosphate	1781:1800	Collectively, the data suggests that O-GlcNAc-6-phosphate is a general post-translation modification of mammalian proteins with a variety of possible cellular functions.
22826440	7	15	theme	synaptic	1266:1273	arg1	transmission					1275:1286	synaptic transmission	1266:1286	synaptic transmission	1266:1286	Many of the identified proteins are involved in synaptic transmission and for Ca(2+)/calmodulin kinase IV, the O-GlcNAc-6-phosphate modification was found in the vicinity of two autophosphorylation sites required for full activation of the kinase suggesting a potential regulatory role for O-GlcNAc-6-phosphate.
22826440	5	16	theme	spectra	819:825	arg1	analysis					767:774	The systematic analysis	752:774	The systematic analysis of 220 candidate phosphoGlcNAc tandem mass spectra as well as a synthetic standard	752:857	The systematic analysis of 220 candidate phosphoGlcNAc tandem mass spectra as well as a synthetic standard enabled the dissection of the major phosphoGlcNAc fragmentation pathways, suggesting that the modification is O-GlcNAc-6-phosphate.
22826440	6	17	theme	O-GlcNAc	1018:1025	arg1	modification					1027:1038	the classical O-GlcNAc modification	1004:1038	the classical O-GlcNAc modification	1004:1038	We find that the classical O-GlcNAc modification often exists on the same peptides indicating that O-GlcNAc-6-phosphate may biosynthetically arise in two steps involving the O-GlcNAc transferase and a currently unknown kinase.
22826440	8	18	theme	mass	1546:1549	arg1	data					1565:1568	re-analyzing mass spectrometric data	1533:1568	re-analyzing mass spectrometric data from human embryonic and induced pluripotent stem cells	1533:1624	By re-analyzing mass spectrometric data from human embryonic and induced pluripotent stem cells, our study also identified Zinc finger protein 462 (ZNF462) as the first human O-GlcNAc-6-phosphate modified protein.
22826440	2	19	dep	10	272:273	arg1	2725-2733					276:284	2725-2733	276:284	2725-2733	276:284	2011, 10, 2725-2733).
22826440	2	19	dep	10	272:273	arg1	2011					266:269	2011	266:269	2011	266:269	2011, 10, 2725-2733).
22826440	5	20	theme	systematic	756:765	arg1	analysis					767:774	The systematic analysis	752:774	The systematic analysis of 220 candidate phosphoGlcNAc tandem mass spectra as well as a synthetic standard	752:857	The systematic analysis of 220 candidate phosphoGlcNAc tandem mass spectra as well as a synthetic standard enabled the dissection of the major phosphoGlcNAc fragmentation pathways, suggesting that the modification is O-GlcNAc-6-phosphate.
22826440	1	21	dep	Graham	234:239	arg1	al.					244:246	Graham et al.	234:246	Graham et al.	234:246	Phosphorylated O-GlcNAc is a novel post-translational modification that has so far only been found on the neuronal protein AP180 from the rat (Graham et al., J. Proteome Res.
22826440	5	22	theme	major	889:893	arg1	pathways					923:930	the major phosphoGlcNAc fragmentation pathways	885:930	the major phosphoGlcNAc fragmentation pathways	885:930	The systematic analysis of 220 candidate phosphoGlcNAc tandem mass spectra as well as a synthetic standard enabled the dissection of the major phosphoGlcNAc fragmentation pathways, suggesting that the modification is O-GlcNAc-6-phosphate.
22826440	9	23	theme	mammalian	1848:1856	arg1	proteins					1858:1865	mammalian proteins	1848:1865	mammalian proteins	1848:1865	Collectively, the data suggests that O-GlcNAc-6-phosphate is a general post-translation modification of mammalian proteins with a variety of possible cellular functions.
22826440	0	24	from	Discovery	0:8	arg1	phosphoproteomics					67:83	large-scale phosphoproteomics	55:83	large-scale phosphoproteomics	55:83	Discovery of O-GlcNAc-6-phosphate modified proteins in large-scale phosphoproteomics data.
22826440	7	25	theme	proteins	1241:1248	arg1	proteins					1241:1248	the identified proteins	1226:1248	the identified proteins	1226:1248	Many of the identified proteins are involved in synaptic transmission and for Ca(2+)/calmodulin kinase IV, the O-GlcNAc-6-phosphate modification was found in the vicinity of two autophosphorylation sites required for full activation of the kinase suggesting a potential regulatory role for O-GlcNAc-6-phosphate.
22826440	7	25	theme	proteins	1241:1248	arg1	Many					1218:1221	Many	1218:1221	Many	1218:1221	Many of the identified proteins are involved in synaptic transmission and for Ca(2+)/calmodulin kinase IV, the O-GlcNAc-6-phosphate modification was found in the vicinity of two autophosphorylation sites required for full activation of the kinase suggesting a potential regulatory role for O-GlcNAc-6-phosphate.
22826440	8	26	theme	human	1575:1579	arg1	cells					1620:1624	human embryonic and induced pluripotent stem cells	1575:1624	human embryonic and induced pluripotent stem cells	1575:1624	By re-analyzing mass spectrometric data from human embryonic and induced pluripotent stem cells, our study also identified Zinc finger protein 462 (ZNF462) as the first human O-GlcNAc-6-phosphate modified protein.
22826440	1	27	located	found	184:188	arg2	modification					145:156	a novel post-translational modification	118:156	a novel post-translational modification that has so far only been found on the neuronal protein AP180 from the rat (Graham et al., J. Proteome Res	118:263	Phosphorylated O-GlcNAc is a novel post-translational modification that has so far only been found on the neuronal protein AP180 from the rat (Graham et al., J. Proteome Res.
22826440	1	27	located	found	184:188	arg2	O-GlcNAc					106:113	Phosphorylated O-GlcNAc	91:113	Phosphorylated O-GlcNAc	91:113	Phosphorylated O-GlcNAc is a novel post-translational modification that has so far only been found on the neuronal protein AP180 from the rat (Graham et al., J. Proteome Res.
22826440	1	27	located	found	184:188	arg1	AP180					214:218	the neuronal protein AP180	193:218	the neuronal protein AP180 from the rat	193:231	Phosphorylated O-GlcNAc is a novel post-translational modification that has so far only been found on the neuronal protein AP180 from the rat (Graham et al., J. Proteome Res.
22826440	7	28	dep	/calmodulin	1302:1312	arg1	kinase					1314:1319	kinase IV	1314:1322	Ca(2+)/calmodulin kinase IV	1296:1322	Many of the identified proteins are involved in synaptic transmission and for Ca(2+)/calmodulin kinase IV, the O-GlcNAc-6-phosphate modification was found in the vicinity of two autophosphorylation sites required for full activation of the kinase suggesting a potential regulatory role for O-GlcNAc-6-phosphate.
22826440	3	29	theme	induced	303:309	arg1	dissociation					311:322	collision induced dissociation	293:322	collision induced dissociation	293:322	Upon collision induced dissociation, the modification generates a highly mass deficient fragment ion (m/z 284.0530) that can be used as a reporter for the identification of phosphorylated O-GlcNAc.
22826440	3	30	used	used	416:419	arg2	m/z					390:392	m/z 284.0530	390:401	m/z 284.0530	390:401	Upon collision induced dissociation, the modification generates a highly mass deficient fragment ion (m/z 284.0530) that can be used as a reporter for the identification of phosphorylated O-GlcNAc.
22826440	3	30	used	used	416:419	arg2	reporter					426:433	a reporter	424:433	a reporter for the identification of phosphorylated O-GlcNAc	424:483	Upon collision induced dissociation, the modification generates a highly mass deficient fragment ion (m/z 284.0530) that can be used as a reporter for the identification of phosphorylated O-GlcNAc.
22826440	3	30	used	used	416:419	arg2	ion					385:387	a highly mass deficient fragment ion	352:387	a highly mass deficient fragment ion (m/z 284.0530) that can be used as a reporter for the identification of phosphorylated O-GlcNAc	352:483	Upon collision induced dissociation, the modification generates a highly mass deficient fragment ion (m/z 284.0530) that can be used as a reporter for the identification of phosphorylated O-GlcNAc.
22826440	5	31	theme	tandem	807:812	arg1	spectra					819:825	220 candidate phosphoGlcNAc tandem mass spectra	779:825	220 candidate phosphoGlcNAc tandem mass spectra as well as a synthetic standard	779:857	The systematic analysis of 220 candidate phosphoGlcNAc tandem mass spectra as well as a synthetic standard enabled the dissection of the major phosphoGlcNAc fragmentation pathways, suggesting that the modification is O-GlcNAc-6-phosphate.
22826440	9	32	theme	possible	1885:1892	arg1	functions					1903:1911	possible cellular functions	1885:1911	possible cellular functions	1885:1911	Collectively, the data suggests that O-GlcNAc-6-phosphate is a general post-translation modification of mammalian proteins with a variety of possible cellular functions.
22826440	4	33	theme	mouse	515:519	arg1	set					548:550	a publically available mouse brain phosphoproteome data set	492:550	a publically available mouse brain phosphoproteome data set	492:550	Using a publically available mouse brain phosphoproteome data set, we employed our recently developed Oscore software to re-evaluate high resolution/high accuracy tandem mass spectra and discovered the modification on 23 peptides corresponding to 11 mouse proteins.
22826440	4	34	theme	mouse	736:740	arg1	proteins					742:749	11 mouse proteins	733:749	11 mouse proteins	733:749	Using a publically available mouse brain phosphoproteome data set, we employed our recently developed Oscore software to re-evaluate high resolution/high accuracy tandem mass spectra and discovered the modification on 23 peptides corresponding to 11 mouse proteins.
22826440	0	35	theme	O-GlcNAc-6-phosphate	13:32	arg1	proteins					43:50	O-GlcNAc-6-phosphate modified proteins	13:50	O-GlcNAc-6-phosphate modified proteins	13:50	Discovery of O-GlcNAc-6-phosphate modified proteins in large-scale phosphoproteomics data.
22826440	1	36	theme	post-translational	126:143	arg1	modification					145:156	a novel post-translational modification	118:156	a novel post-translational modification that has so far only been found on the neuronal protein AP180 from the rat (Graham et al., J. Proteome Res	118:263	Phosphorylated O-GlcNAc is a novel post-translational modification that has so far only been found on the neuronal protein AP180 from the rat (Graham et al., J. Proteome Res.
22826440	1	36	theme	post-translational	126:143	arg1	O-GlcNAc					106:113	Phosphorylated O-GlcNAc	91:113	Phosphorylated O-GlcNAc	91:113	Phosphorylated O-GlcNAc is a novel post-translational modification that has so far only been found on the neuronal protein AP180 from the rat (Graham et al., J. Proteome Res.
22826440	6	37	theme	same	1060:1063	arg1	peptides					1065:1072	the same peptides	1056:1072	the same peptides indicating that O-GlcNAc-6-phosphate may biosynthetically arise in two steps involving the O-GlcNAc transferase and a currently unknown kinase	1056:1215	We find that the classical O-GlcNAc modification often exists on the same peptides indicating that O-GlcNAc-6-phosphate may biosynthetically arise in two steps involving the O-GlcNAc transferase and a currently unknown kinase.
22826440	9	38	theme	functions	1903:1911	arg1	variety					1874:1880	a variety	1872:1880	a variety of possible cellular functions	1872:1911	Collectively, the data suggests that O-GlcNAc-6-phosphate is a general post-translation modification of mammalian proteins with a variety of possible cellular functions.
22826440	9	38	theme	functions	1903:1911	arg1	functions					1903:1911	possible cellular functions	1885:1911	possible cellular functions	1885:1911	Collectively, the data suggests that O-GlcNAc-6-phosphate is a general post-translation modification of mammalian proteins with a variety of possible cellular functions.
22826440	4	39	theme	phosphoproteome	527:541	arg1	set					548:550	a publically available mouse brain phosphoproteome data set	492:550	a publically available mouse brain phosphoproteome data set	492:550	Using a publically available mouse brain phosphoproteome data set, we employed our recently developed Oscore software to re-evaluate high resolution/high accuracy tandem mass spectra and discovered the modification on 23 peptides corresponding to 11 mouse proteins.
22826440	0	40	theme	proteins	43:50	arg1	Discovery					0:8	Discovery	0:8	Discovery of O-GlcNAc-6-phosphate modified proteins in large-scale phosphoproteomics	0:83	Discovery of O-GlcNAc-6-phosphate modified proteins in large-scale phosphoproteomics data.
22826440	3	41	theme	fragment	376:383	arg1	ion					385:387	a highly mass deficient fragment ion	352:387	a highly mass deficient fragment ion (m/z 284.0530) that can be used as a reporter for the identification of phosphorylated O-GlcNAc	352:483	Upon collision induced dissociation, the modification generates a highly mass deficient fragment ion (m/z 284.0530) that can be used as a reporter for the identification of phosphorylated O-GlcNAc.
22826440	3	41	theme	fragment	376:383	arg1	reporter					426:433	a reporter	424:433	a reporter for the identification of phosphorylated O-GlcNAc	424:483	Upon collision induced dissociation, the modification generates a highly mass deficient fragment ion (m/z 284.0530) that can be used as a reporter for the identification of phosphorylated O-GlcNAc.
22826440	3	41	theme	fragment	376:383	arg1	m/z					390:392	m/z 284.0530	390:401	m/z 284.0530	390:401	Upon collision induced dissociation, the modification generates a highly mass deficient fragment ion (m/z 284.0530) that can be used as a reporter for the identification of phosphorylated O-GlcNAc.
22826440	5	42	theme	candidate	783:791	arg1	spectra					819:825	220 candidate phosphoGlcNAc tandem mass spectra	779:825	220 candidate phosphoGlcNAc tandem mass spectra as well as a synthetic standard	779:857	The systematic analysis of 220 candidate phosphoGlcNAc tandem mass spectra as well as a synthetic standard enabled the dissection of the major phosphoGlcNAc fragmentation pathways, suggesting that the modification is O-GlcNAc-6-phosphate.
22826440	6	43	theme	unknown	1202:1208	arg1	kinase					1210:1215	a currently unknown kinase	1190:1215	a currently unknown kinase	1190:1215	We find that the classical O-GlcNAc modification often exists on the same peptides indicating that O-GlcNAc-6-phosphate may biosynthetically arise in two steps involving the O-GlcNAc transferase and a currently unknown kinase.
22826440	7	44	theme	2+	1299:1300	arg1	/calmodulin					1302:1312	Ca(2+)/calmodulin	1296:1312	Ca(2+)/calmodulin kinase IV	1296:1322	Many of the identified proteins are involved in synaptic transmission and for Ca(2+)/calmodulin kinase IV, the O-GlcNAc-6-phosphate modification was found in the vicinity of two autophosphorylation sites required for full activation of the kinase suggesting a potential regulatory role for O-GlcNAc-6-phosphate.
22826440	8	45	theme	Zinc	1653:1656	arg1	protein					1665:1671	Zinc finger protein 462	1653:1675	Zinc finger protein 462 (ZNF462)	1653:1684	By re-analyzing mass spectrometric data from human embryonic and induced pluripotent stem cells, our study also identified Zinc finger protein 462 (ZNF462) as the first human O-GlcNAc-6-phosphate modified protein.
22826440	8	45	theme	Zinc	1653:1656	arg1	protein					1735:1741	the first human O-GlcNAc-6-phosphate modified protein	1689:1741	the first human O-GlcNAc-6-phosphate modified protein	1689:1741	By re-analyzing mass spectrometric data from human embryonic and induced pluripotent stem cells, our study also identified Zinc finger protein 462 (ZNF462) as the first human O-GlcNAc-6-phosphate modified protein.
22826440	8	45	theme	Zinc	1653:1656	arg1	ZNF462					1678:1683	ZNF462	1678:1683	ZNF462	1678:1683	By re-analyzing mass spectrometric data from human embryonic and induced pluripotent stem cells, our study also identified Zinc finger protein 462 (ZNF462) as the first human O-GlcNAc-6-phosphate modified protein.
22826440	3	46	theme	O-GlcNAc	476:483	arg1	identification					443:456	the identification	439:456	the identification of phosphorylated O-GlcNAc	439:483	Upon collision induced dissociation, the modification generates a highly mass deficient fragment ion (m/z 284.0530) that can be used as a reporter for the identification of phosphorylated O-GlcNAc.
22826440	8	47	theme	human	1699:1703	arg1	protein					1665:1671	Zinc finger protein 462	1653:1675	Zinc finger protein 462 (ZNF462)	1653:1684	By re-analyzing mass spectrometric data from human embryonic and induced pluripotent stem cells, our study also identified Zinc finger protein 462 (ZNF462) as the first human O-GlcNAc-6-phosphate modified protein.
22826440	8	47	theme	human	1699:1703	arg1	protein					1735:1741	the first human O-GlcNAc-6-phosphate modified protein	1689:1741	the first human O-GlcNAc-6-phosphate modified protein	1689:1741	By re-analyzing mass spectrometric data from human embryonic and induced pluripotent stem cells, our study also identified Zinc finger protein 462 (ZNF462) as the first human O-GlcNAc-6-phosphate modified protein.
22826440	7	48	theme	Ca	1296:1297	arg1	/calmodulin					1302:1312	Ca(2+)/calmodulin	1296:1312	Ca(2+)/calmodulin kinase IV	1296:1322	Many of the identified proteins are involved in synaptic transmission and for Ca(2+)/calmodulin kinase IV, the O-GlcNAc-6-phosphate modification was found in the vicinity of two autophosphorylation sites required for full activation of the kinase suggesting a potential regulatory role for O-GlcNAc-6-phosphate.
22826440	4	49	theme	developed	578:586	arg1	software					595:602	our recently developed Oscore software	565:602	our recently developed Oscore software	565:602	Using a publically available mouse brain phosphoproteome data set, we employed our recently developed Oscore software to re-evaluate high resolution/high accuracy tandem mass spectra and discovered the modification on 23 peptides corresponding to 11 mouse proteins.
22826440	8	50	theme	modified	1726:1733	arg1	protein					1665:1671	Zinc finger protein 462	1653:1675	Zinc finger protein 462 (ZNF462)	1653:1684	By re-analyzing mass spectrometric data from human embryonic and induced pluripotent stem cells, our study also identified Zinc finger protein 462 (ZNF462) as the first human O-GlcNAc-6-phosphate modified protein.
22826440	8	50	theme	modified	1726:1733	arg1	protein					1735:1741	the first human O-GlcNAc-6-phosphate modified protein	1689:1741	the first human O-GlcNAc-6-phosphate modified protein	1689:1741	By re-analyzing mass spectrometric data from human embryonic and induced pluripotent stem cells, our study also identified Zinc finger protein 462 (ZNF462) as the first human O-GlcNAc-6-phosphate modified protein.
22826440	0	51	theme	large-scale	55:65	arg1	phosphoproteomics					67:83	large-scale phosphoproteomics	55:83	large-scale phosphoproteomics	55:83	Discovery of O-GlcNAc-6-phosphate modified proteins in large-scale phosphoproteomics data.
22826440	7	52	theme	potential	1478:1486	arg1	role					1499:1502	a potential regulatory role	1476:1502	a potential regulatory role for O-GlcNAc-6-phosphate	1476:1527	Many of the identified proteins are involved in synaptic transmission and for Ca(2+)/calmodulin kinase IV, the O-GlcNAc-6-phosphate modification was found in the vicinity of two autophosphorylation sites required for full activation of the kinase suggesting a potential regulatory role for O-GlcNAc-6-phosphate.
22826440	7	53	theme	kinase	1458:1463	arg1	activation					1440:1449	full activation	1435:1449	full activation of the kinase	1435:1463	Many of the identified proteins are involved in synaptic transmission and for Ca(2+)/calmodulin kinase IV, the O-GlcNAc-6-phosphate modification was found in the vicinity of two autophosphorylation sites required for full activation of the kinase suggesting a potential regulatory role for O-GlcNAc-6-phosphate.
22826440	4	54	theme	resolution/high	624:638	arg1	spectra					661:667	high resolution/high accuracy tandem mass spectra	619:667	high resolution/high accuracy tandem mass spectra	619:667	Using a publically available mouse brain phosphoproteome data set, we employed our recently developed Oscore software to re-evaluate high resolution/high accuracy tandem mass spectra and discovered the modification on 23 peptides corresponding to 11 mouse proteins.
22826440	1	55	theme	neuronal	197:204	arg1	AP180					214:218	the neuronal protein AP180	193:218	the neuronal protein AP180 from the rat	193:231	Phosphorylated O-GlcNAc is a novel post-translational modification that has so far only been found on the neuronal protein AP180 from the rat (Graham et al., J. Proteome Res.
22826440	4	56	theme	tandem	649:654	arg1	spectra					661:667	high resolution/high accuracy tandem mass spectra	619:667	high resolution/high accuracy tandem mass spectra	619:667	Using a publically available mouse brain phosphoproteome data set, we employed our recently developed Oscore software to re-evaluate high resolution/high accuracy tandem mass spectra and discovered the modification on 23 peptides corresponding to 11 mouse proteins.
22826440	7	57	theme	full	1435:1438	arg1	activation					1440:1449	full activation	1435:1449	full activation of the kinase	1435:1463	Many of the identified proteins are involved in synaptic transmission and for Ca(2+)/calmodulin kinase IV, the O-GlcNAc-6-phosphate modification was found in the vicinity of two autophosphorylation sites required for full activation of the kinase suggesting a potential regulatory role for O-GlcNAc-6-phosphate.
22826440	1	58	from	rat	229:231	arg1	AP180					214:218	the neuronal protein AP180	193:218	the neuronal protein AP180 from the rat	193:231	Phosphorylated O-GlcNAc is a novel post-translational modification that has so far only been found on the neuronal protein AP180 from the rat (Graham et al., J. Proteome Res.
22826440	5	59	theme	phosphoGlcNAc	895:907	arg1	pathways					923:930	the major phosphoGlcNAc fragmentation pathways	885:930	the major phosphoGlcNAc fragmentation pathways	885:930	The systematic analysis of 220 candidate phosphoGlcNAc tandem mass spectra as well as a synthetic standard enabled the dissection of the major phosphoGlcNAc fragmentation pathways, suggesting that the modification is O-GlcNAc-6-phosphate.
22826440	7	60	theme	autophosphorylation	1396:1414	arg1	sites					1416:1420	two autophosphorylation sites	1392:1420	two autophosphorylation sites required for full activation of the kinase	1392:1463	Many of the identified proteins are involved in synaptic transmission and for Ca(2+)/calmodulin kinase IV, the O-GlcNAc-6-phosphate modification was found in the vicinity of two autophosphorylation sites required for full activation of the kinase suggesting a potential regulatory role for O-GlcNAc-6-phosphate.
22826440	9	61	with	modification	1832:1843	arg1	variety					1874:1880	a variety	1872:1880	a variety of possible cellular functions	1872:1911	Collectively, the data suggests that O-GlcNAc-6-phosphate is a general post-translation modification of mammalian proteins with a variety of possible cellular functions.
22826440	9	61	with	modification	1832:1843	arg1	functions					1903:1911	possible cellular functions	1885:1911	possible cellular functions	1885:1911	Collectively, the data suggests that O-GlcNAc-6-phosphate is a general post-translation modification of mammalian proteins with a variety of possible cellular functions.
22826440	5	62	theme	pathways	923:930	arg1	dissection					871:880	the dissection	867:880	the dissection of the major phosphoGlcNAc fragmentation pathways	867:930	The systematic analysis of 220 candidate phosphoGlcNAc tandem mass spectra as well as a synthetic standard enabled the dissection of the major phosphoGlcNAc fragmentation pathways, suggesting that the modification is O-GlcNAc-6-phosphate.
22826440	8	63	theme	re-analyzing	1533:1544	arg1	data					1565:1568	re-analyzing mass spectrometric data	1533:1568	re-analyzing mass spectrometric data from human embryonic and induced pluripotent stem cells	1533:1624	By re-analyzing mass spectrometric data from human embryonic and induced pluripotent stem cells, our study also identified Zinc finger protein 462 (ZNF462) as the first human O-GlcNAc-6-phosphate modified protein.
22826440	9	64	theme	post-translation	1815:1830	arg1	modification					1832:1843	a general post-translation modification	1805:1843	a general post-translation modification of mammalian proteins with a variety of possible cellular functions	1805:1911	Collectively, the data suggests that O-GlcNAc-6-phosphate is a general post-translation modification of mammalian proteins with a variety of possible cellular functions.
22826440	9	64	theme	post-translation	1815:1830	arg1	O-GlcNAc-6-phosphate					1781:1800	O-GlcNAc-6-phosphate	1781:1800	O-GlcNAc-6-phosphate	1781:1800	Collectively, the data suggests that O-GlcNAc-6-phosphate is a general post-translation modification of mammalian proteins with a variety of possible cellular functions.
22826440	8	65	theme	spectrometric	1551:1563	arg1	data					1565:1568	re-analyzing mass spectrometric data	1533:1568	re-analyzing mass spectrometric data from human embryonic and induced pluripotent stem cells	1533:1624	By re-analyzing mass spectrometric data from human embryonic and induced pluripotent stem cells, our study also identified Zinc finger protein 462 (ZNF462) as the first human O-GlcNAc-6-phosphate modified protein.
22826440	6	66	theme	classical	1008:1016	arg1	modification					1027:1038	the classical O-GlcNAc modification	1004:1038	the classical O-GlcNAc modification	1004:1038	We find that the classical O-GlcNAc modification often exists on the same peptides indicating that O-GlcNAc-6-phosphate may biosynthetically arise in two steps involving the O-GlcNAc transferase and a currently unknown kinase.
22826440	3	67	theme	collision	293:301	arg1	dissociation					311:322	collision induced dissociation	293:322	collision induced dissociation	293:322	Upon collision induced dissociation, the modification generates a highly mass deficient fragment ion (m/z 284.0530) that can be used as a reporter for the identification of phosphorylated O-GlcNAc.
22826440	7	68	theme	identified	1230:1239	arg1	proteins					1241:1248	the identified proteins	1226:1248	the identified proteins	1226:1248	Many of the identified proteins are involved in synaptic transmission and for Ca(2+)/calmodulin kinase IV, the O-GlcNAc-6-phosphate modification was found in the vicinity of two autophosphorylation sites required for full activation of the kinase suggesting a potential regulatory role for O-GlcNAc-6-phosphate.
22826440	9	69	theme	proteins	1858:1865	arg1	modification					1832:1843	a general post-translation modification	1805:1843	a general post-translation modification of mammalian proteins with a variety of possible cellular functions	1805:1911	Collectively, the data suggests that O-GlcNAc-6-phosphate is a general post-translation modification of mammalian proteins with a variety of possible cellular functions.
22826440	9	69	theme	proteins	1858:1865	arg1	O-GlcNAc-6-phosphate					1781:1800	O-GlcNAc-6-phosphate	1781:1800	O-GlcNAc-6-phosphate	1781:1800	Collectively, the data suggests that O-GlcNAc-6-phosphate is a general post-translation modification of mammalian proteins with a variety of possible cellular functions.
22826440	8	70	theme	embryonic	1581:1589	arg1	cells					1620:1624	human embryonic and induced pluripotent stem cells	1575:1624	human embryonic and induced pluripotent stem cells	1575:1624	By re-analyzing mass spectrometric data from human embryonic and induced pluripotent stem cells, our study also identified Zinc finger protein 462 (ZNF462) as the first human O-GlcNAc-6-phosphate modified protein.
22826440	1	71	theme	Phosphorylated	91:104	arg1	modification					145:156	a novel post-translational modification	118:156	a novel post-translational modification that has so far only been found on the neuronal protein AP180 from the rat (Graham et al., J. Proteome Res	118:263	Phosphorylated O-GlcNAc is a novel post-translational modification that has so far only been found on the neuronal protein AP180 from the rat (Graham et al., J. Proteome Res.
22826440	1	71	theme	Phosphorylated	91:104	arg1	O-GlcNAc					106:113	Phosphorylated O-GlcNAc	91:113	Phosphorylated O-GlcNAc	91:113	Phosphorylated O-GlcNAc is a novel post-translational modification that has so far only been found on the neuronal protein AP180 from the rat (Graham et al., J. Proteome Res.
22826440	8	72	theme	induced	1595:1601	arg1	cells					1620:1624	human embryonic and induced pluripotent stem cells	1575:1624	human embryonic and induced pluripotent stem cells	1575:1624	By re-analyzing mass spectrometric data from human embryonic and induced pluripotent stem cells, our study also identified Zinc finger protein 462 (ZNF462) as the first human O-GlcNAc-6-phosphate modified protein.
22826440	5	73	theme	phosphoGlcNAc	793:805	arg1	spectra					819:825	220 candidate phosphoGlcNAc tandem mass spectra	779:825	220 candidate phosphoGlcNAc tandem mass spectra as well as a synthetic standard	779:857	The systematic analysis of 220 candidate phosphoGlcNAc tandem mass spectra as well as a synthetic standard enabled the dissection of the major phosphoGlcNAc fragmentation pathways, suggesting that the modification is O-GlcNAc-6-phosphate.
22826440	7	74	theme	O-GlcNAc-6-phosphate	1329:1348	arg1	modification					1350:1361	the O-GlcNAc-6-phosphate modification	1325:1361	the O-GlcNAc-6-phosphate modification	1325:1361	Many of the identified proteins are involved in synaptic transmission and for Ca(2+)/calmodulin kinase IV, the O-GlcNAc-6-phosphate modification was found in the vicinity of two autophosphorylation sites required for full activation of the kinase suggesting a potential regulatory role for O-GlcNAc-6-phosphate.
22826440	3	75	theme	deficient	366:374	arg1	ion					385:387	a highly mass deficient fragment ion	352:387	a highly mass deficient fragment ion (m/z 284.0530) that can be used as a reporter for the identification of phosphorylated O-GlcNAc	352:483	Upon collision induced dissociation, the modification generates a highly mass deficient fragment ion (m/z 284.0530) that can be used as a reporter for the identification of phosphorylated O-GlcNAc.
22826440	3	75	theme	deficient	366:374	arg1	reporter					426:433	a reporter	424:433	a reporter for the identification of phosphorylated O-GlcNAc	424:483	Upon collision induced dissociation, the modification generates a highly mass deficient fragment ion (m/z 284.0530) that can be used as a reporter for the identification of phosphorylated O-GlcNAc.
22826440	3	75	theme	deficient	366:374	arg1	m/z					390:392	m/z 284.0530	390:401	m/z 284.0530	390:401	Upon collision induced dissociation, the modification generates a highly mass deficient fragment ion (m/z 284.0530) that can be used as a reporter for the identification of phosphorylated O-GlcNAc.
22826440	8	76	theme	stem	1615:1618	arg1	cells					1620:1624	human embryonic and induced pluripotent stem cells	1575:1624	human embryonic and induced pluripotent stem cells	1575:1624	By re-analyzing mass spectrometric data from human embryonic and induced pluripotent stem cells, our study also identified Zinc finger protein 462 (ZNF462) as the first human O-GlcNAc-6-phosphate modified protein.
22826440	1	77	dep	found	184:188	arg1	Graham					234:239	Graham	234:239	Graham	234:239	Phosphorylated O-GlcNAc is a novel post-translational modification that has so far only been found on the neuronal protein AP180 from the rat (Graham et al., J. Proteome Res.
22826440	1	77	dep	found	184:188	arg1	Res					261:263	Res	261:263	Res	261:263	Phosphorylated O-GlcNAc is a novel post-translational modification that has so far only been found on the neuronal protein AP180 from the rat (Graham et al., J. Proteome Res.
22826440	0	78	theme	modified	34:41	arg1	proteins					43:50	O-GlcNAc-6-phosphate modified proteins	13:50	O-GlcNAc-6-phosphate modified proteins	13:50	Discovery of O-GlcNAc-6-phosphate modified proteins in large-scale phosphoproteomics data.
22826440	1	79	theme	novel	120:124	arg1	modification					145:156	a novel post-translational modification	118:156	a novel post-translational modification that has so far only been found on the neuronal protein AP180 from the rat (Graham et al., J. Proteome Res	118:263	Phosphorylated O-GlcNAc is a novel post-translational modification that has so far only been found on the neuronal protein AP180 from the rat (Graham et al., J. Proteome Res.
22826440	1	79	theme	novel	120:124	arg1	O-GlcNAc					106:113	Phosphorylated O-GlcNAc	91:113	Phosphorylated O-GlcNAc	91:113	Phosphorylated O-GlcNAc is a novel post-translational modification that has so far only been found on the neuronal protein AP180 from the rat (Graham et al., J. Proteome Res.
22826440	9	80	theme	cellular	1894:1901	arg1	functions					1903:1911	possible cellular functions	1885:1911	possible cellular functions	1885:1911	Collectively, the data suggests that O-GlcNAc-6-phosphate is a general post-translation modification of mammalian proteins with a variety of possible cellular functions.
22826440	4	81	theme	data	543:546	arg1	set					548:550	a publically available mouse brain phosphoproteome data set	492:550	a publically available mouse brain phosphoproteome data set	492:550	Using a publically available mouse brain phosphoproteome data set, we employed our recently developed Oscore software to re-evaluate high resolution/high accuracy tandem mass spectra and discovered the modification on 23 peptides corresponding to 11 mouse proteins.
22826440	6	82	theme	O-GlcNAc	1165:1172	arg1	transferase					1174:1184	the O-GlcNAc transferase	1161:1184	the O-GlcNAc transferase	1161:1184	We find that the classical O-GlcNAc modification often exists on the same peptides indicating that O-GlcNAc-6-phosphate may biosynthetically arise in two steps involving the O-GlcNAc transferase and a currently unknown kinase.
22826440	4	83	theme	available	505:513	arg1	set					548:550	a publically available mouse brain phosphoproteome data set	492:550	a publically available mouse brain phosphoproteome data set	492:550	Using a publically available mouse brain phosphoproteome data set, we employed our recently developed Oscore software to re-evaluate high resolution/high accuracy tandem mass spectra and discovered the modification on 23 peptides corresponding to 11 mouse proteins.
22826440	8	84	theme	first	1693:1697	arg1	protein					1665:1671	Zinc finger protein 462	1653:1675	Zinc finger protein 462 (ZNF462)	1653:1684	By re-analyzing mass spectrometric data from human embryonic and induced pluripotent stem cells, our study also identified Zinc finger protein 462 (ZNF462) as the first human O-GlcNAc-6-phosphate modified protein.
22826440	8	84	theme	first	1693:1697	arg1	protein					1735:1741	the first human O-GlcNAc-6-phosphate modified protein	1689:1741	the first human O-GlcNAc-6-phosphate modified protein	1689:1741	By re-analyzing mass spectrometric data from human embryonic and induced pluripotent stem cells, our study also identified Zinc finger protein 462 (ZNF462) as the first human O-GlcNAc-6-phosphate modified protein.
22826440	8	85	theme	finger	1658:1663	arg1	protein					1665:1671	Zinc finger protein 462	1653:1675	Zinc finger protein 462 (ZNF462)	1653:1684	By re-analyzing mass spectrometric data from human embryonic and induced pluripotent stem cells, our study also identified Zinc finger protein 462 (ZNF462) as the first human O-GlcNAc-6-phosphate modified protein.
22826440	8	85	theme	finger	1658:1663	arg1	protein					1735:1741	the first human O-GlcNAc-6-phosphate modified protein	1689:1741	the first human O-GlcNAc-6-phosphate modified protein	1689:1741	By re-analyzing mass spectrometric data from human embryonic and induced pluripotent stem cells, our study also identified Zinc finger protein 462 (ZNF462) as the first human O-GlcNAc-6-phosphate modified protein.
22826440	8	85	theme	finger	1658:1663	arg1	ZNF462					1678:1683	ZNF462	1678:1683	ZNF462	1678:1683	By re-analyzing mass spectrometric data from human embryonic and induced pluripotent stem cells, our study also identified Zinc finger protein 462 (ZNF462) as the first human O-GlcNAc-6-phosphate modified protein.
22826440	8	86	theme	O-GlcNAc-6-phosphate	1705:1724	arg1	protein					1665:1671	Zinc finger protein 462	1653:1675	Zinc finger protein 462 (ZNF462)	1653:1684	By re-analyzing mass spectrometric data from human embryonic and induced pluripotent stem cells, our study also identified Zinc finger protein 462 (ZNF462) as the first human O-GlcNAc-6-phosphate modified protein.
22826440	8	86	theme	O-GlcNAc-6-phosphate	1705:1724	arg1	protein					1735:1741	the first human O-GlcNAc-6-phosphate modified protein	1689:1741	the first human O-GlcNAc-6-phosphate modified protein	1689:1741	By re-analyzing mass spectrometric data from human embryonic and induced pluripotent stem cells, our study also identified Zinc finger protein 462 (ZNF462) as the first human O-GlcNAc-6-phosphate modified protein.
22826440	4	87	theme	Oscore	588:593	arg1	software					595:602	our recently developed Oscore software	565:602	our recently developed Oscore software	565:602	Using a publically available mouse brain phosphoproteome data set, we employed our recently developed Oscore software to re-evaluate high resolution/high accuracy tandem mass spectra and discovered the modification on 23 peptides corresponding to 11 mouse proteins.
34207636	0	0	theme	Alzheimer	80:88	arg1	Disease					90:96	Alzheimer Disease	80:96	Alzheimer Disease	80:96	What Can N-glycomics and N-glycoproteomics of Cerebrospinal Fluid Tell Us about Alzheimer Disease?
34207636	6	1	contain	have	1133:1136	arg2	glycosylation					1154:1166	altered protein glycosylation	1138:1166	altered protein glycosylation	1138:1166	Several proteins related to Alzheimer disease pathogenesis have altered protein glycosylation, and recent glycomics studies have shown differences in cerebrospinal fluid as well as in brain tissue in Alzheimer disease as compared to controls.
34207636	6	1	contain	have	1133:1136	arg1	proteins					1082:1089	Several proteins	1074:1089	Several proteins related to Alzheimer disease pathogenesis	1074:1131	Several proteins related to Alzheimer disease pathogenesis have altered protein glycosylation, and recent glycomics studies have shown differences in cerebrospinal fluid as well as in brain tissue in Alzheimer disease as compared to controls.
34207636	5	2	theme	glycan	926:931	arg1	derivatization					933:946	glycan derivatization	926:946	glycan derivatization	926:946	Herein, we briefly touch upon important steps such as sample preparation and preconcentration, glycan release, glycan derivatization and quantification and advances in mass spectrometry that today are the work-horse for glycomics and glycoproteomics studies.
34207636	5	3	from	advances	971:978	arg1	spectrometry					988:999	mass spectrometry	983:999	mass spectrometry	983:999	Herein, we briefly touch upon important steps such as sample preparation and preconcentration, glycan release, glycan derivatization and quantification and advances in mass spectrometry that today are the work-horse for glycomics and glycoproteomics studies.
34207636	2	4	theme	pathological	304:315	arg1	processes					317:325	biological and pathological processes	289:325	biological and pathological processes	289:325	To fully understand biological and pathological processes it is crucial to also include post-translational modifications in the "omics".
34207636	7	5	theme	glycan	1436:1441	arg1	biomarkers					1443:1452	glycan biomarkers	1436:1452	glycan biomarkers in cerebrospinal fluid	1436:1475	In this review, we discuss these techniques and how they have been used to shed light on Alzheimer disease and to find glycan biomarkers in cerebrospinal fluid.
34207636	6	6	theme	cerebrospinal	1224:1236	arg1	fluid					1238:1242	cerebrospinal fluid	1224:1242	cerebrospinal fluid	1224:1242	Several proteins related to Alzheimer disease pathogenesis have altered protein glycosylation, and recent glycomics studies have shown differences in cerebrospinal fluid as well as in brain tissue in Alzheimer disease as compared to controls.
34207636	4	7	theme	preparation	745:755	arg1	array					729:733	an array	726:733	an array of sample preparation and analysis steps that needs to be carefully considered	726:812	The study of protein glycosylation requires a workflow that involves an array of sample preparation and analysis steps that needs to be carefully considered.
34207636	2	8	theme	biological	289:298	arg1	processes					317:325	biological and pathological processes	289:325	biological and pathological processes	289:325	To fully understand biological and pathological processes it is crucial to also include post-translational modifications in the "omics".
34207636	1	9	theme	enormous	177:184	arg1	interest					186:193	an enormous interest	174:193	an enormous interest for studies aimed at revealing proteins and pathways involved in disease	174:266	Proteomics-large-scale studies of proteins-has over the last decade gained an enormous interest for studies aimed at revealing proteins and pathways involved in disease.
34207636	6	10	theme	Several	1074:1080	arg1	proteins					1082:1089	Several proteins	1074:1089	Several proteins related to Alzheimer disease pathogenesis	1074:1131	Several proteins related to Alzheimer disease pathogenesis have altered protein glycosylation, and recent glycomics studies have shown differences in cerebrospinal fluid as well as in brain tissue in Alzheimer disease as compared to controls.
34207636	6	11	theme	altered	1138:1144	arg1	glycosylation					1154:1166	altered protein glycosylation	1138:1166	altered protein glycosylation	1138:1166	Several proteins related to Alzheimer disease pathogenesis have altered protein glycosylation, and recent glycomics studies have shown differences in cerebrospinal fluid as well as in brain tissue in Alzheimer disease as compared to controls.
34207636	3	12	with	peptides/proteins	585:601	arg1	glycans					612:618	the glycans	608:618	the glycans still attached	608:633	To this end, glycomics (identification and quantification of glycans enzymatically or chemically released from proteins) and glycoproteomics (identification and quantification of peptides/proteins with the glycans still attached) is gaining interest.
34207636	2	13	from	modifications	376:388	arg1	"					403:403	the "omics"	393:403	the "omics"	393:403	To fully understand biological and pathological processes it is crucial to also include post-translational modifications in the "omics".
34207636	5	14	from	steps	855:859	arg1	spectrometry					988:999	mass spectrometry	983:999	mass spectrometry	983:999	Herein, we briefly touch upon important steps such as sample preparation and preconcentration, glycan release, glycan derivatization and quantification and advances in mass spectrometry that today are the work-horse for glycomics and glycoproteomics studies.
34207636	3	15	dep	glycomics	419:427	arg1	quantification					449:462	quantification	449:462	quantification	449:462	To this end, glycomics (identification and quantification of glycans enzymatically or chemically released from proteins) and glycoproteomics (identification and quantification of peptides/proteins with the glycans still attached) is gaining interest.
34207636	3	15	dep	glycomics	419:427	arg1	identification					430:443	identification	430:443	identification	430:443	To this end, glycomics (identification and quantification of glycans enzymatically or chemically released from proteins) and glycoproteomics (identification and quantification of peptides/proteins with the glycans still attached) is gaining interest.
34207636	3	15	dep	glycomics	419:427	arg1	glycomics					419:427	glycomics	419:427	glycomics (identification and quantification of glycans enzymatically or chemically released from proteins)	419:525	To this end, glycomics (identification and quantification of glycans enzymatically or chemically released from proteins) and glycoproteomics (identification and quantification of peptides/proteins with the glycans still attached) is gaining interest.
34207636	4	16	theme	steps	770:774	arg1	array					729:733	an array	726:733	an array of sample preparation and analysis steps that needs to be carefully considered	726:812	The study of protein glycosylation requires a workflow that involves an array of sample preparation and analysis steps that needs to be carefully considered.
34207636	2	17	theme	omics	398:402	arg1	"					403:403	the "omics"	393:403	the "omics"	393:403	To fully understand biological and pathological processes it is crucial to also include post-translational modifications in the "omics".
34207636	5	18	theme	important	845:853	arg1	quantification					952:965	quantification	952:965	quantification	952:965	Herein, we briefly touch upon important steps such as sample preparation and preconcentration, glycan release, glycan derivatization and quantification and advances in mass spectrometry that today are the work-horse for glycomics and glycoproteomics studies.
34207636	5	18	theme	important	845:853	arg1	advances					971:978	advances	971:978	advances in mass spectrometry	971:999	Herein, we briefly touch upon important steps such as sample preparation and preconcentration, glycan release, glycan derivatization and quantification and advances in mass spectrometry that today are the work-horse for glycomics and glycoproteomics studies.
34207636	5	18	theme	important	845:853	arg1	release					917:923	glycan release	910:923	glycan release	910:923	Herein, we briefly touch upon important steps such as sample preparation and preconcentration, glycan release, glycan derivatization and quantification and advances in mass spectrometry that today are the work-horse for glycomics and glycoproteomics studies.
34207636	5	18	theme	important	845:853	arg1	preparation					876:886	sample preparation	869:886	sample preparation	869:886	Herein, we briefly touch upon important steps such as sample preparation and preconcentration, glycan release, glycan derivatization and quantification and advances in mass spectrometry that today are the work-horse for glycomics and glycoproteomics studies.
34207636	5	18	theme	important	845:853	arg1	work-horse					1020:1029	the work-horse	1016:1029	the work-horse for glycomics and glycoproteomics studies	1016:1071	Herein, we briefly touch upon important steps such as sample preparation and preconcentration, glycan release, glycan derivatization and quantification and advances in mass spectrometry that today are the work-horse for glycomics and glycoproteomics studies.
34207636	5	18	theme	important	845:853	arg1	derivatization					933:946	glycan derivatization	926:946	glycan derivatization	926:946	Herein, we briefly touch upon important steps such as sample preparation and preconcentration, glycan release, glycan derivatization and quantification and advances in mass spectrometry that today are the work-horse for glycomics and glycoproteomics studies.
34207636	5	18	theme	important	845:853	arg1	steps					855:859	important steps	845:859	important steps such as sample preparation and preconcentration, glycan release, glycan derivatization and quantification	845:965	Herein, we briefly touch upon important steps such as sample preparation and preconcentration, glycan release, glycan derivatization and quantification and advances in mass spectrometry that today are the work-horse for glycomics and glycoproteomics studies.
34207636	5	18	theme	important	845:853	arg1	preconcentration					892:907	preconcentration	892:907	preconcentration	892:907	Herein, we briefly touch upon important steps such as sample preparation and preconcentration, glycan release, glycan derivatization and quantification and advances in mass spectrometry that today are the work-horse for glycomics and glycoproteomics studies.
34207636	3	19	dep	glycoproteomics	531:545	arg1	quantification					567:580	quantification	567:580	quantification	567:580	To this end, glycomics (identification and quantification of glycans enzymatically or chemically released from proteins) and glycoproteomics (identification and quantification of peptides/proteins with the glycans still attached) is gaining interest.
34207636	3	19	dep	glycoproteomics	531:545	arg1	identification					548:561	identification	548:561	identification	548:561	To this end, glycomics (identification and quantification of glycans enzymatically or chemically released from proteins) and glycoproteomics (identification and quantification of peptides/proteins with the glycans still attached) is gaining interest.
34207636	3	19	dep	glycoproteomics	531:545	arg1	glycoproteomics					531:545	glycoproteomics	531:545	glycoproteomics (identification and quantification of peptides/proteins with the glycans still attached)	531:634	To this end, glycomics (identification and quantification of glycans enzymatically or chemically released from proteins) and glycoproteomics (identification and quantification of peptides/proteins with the glycans still attached) is gaining interest.
34207636	6	20	from	differences	1209:1219	arg1	fluid					1238:1242	cerebrospinal fluid	1224:1242	cerebrospinal fluid	1224:1242	Several proteins related to Alzheimer disease pathogenesis have altered protein glycosylation, and recent glycomics studies have shown differences in cerebrospinal fluid as well as in brain tissue in Alzheimer disease as compared to controls.
34207636	6	20	from	differences	1209:1219	arg1	tissue					1264:1269	brain tissue	1258:1269	brain tissue in Alzheimer disease	1258:1290	Several proteins related to Alzheimer disease pathogenesis have altered protein glycosylation, and recent glycomics studies have shown differences in cerebrospinal fluid as well as in brain tissue in Alzheimer disease as compared to controls.
34207636	6	21	theme	disease	1112:1118	arg1	pathogenesis					1120:1131	Alzheimer disease pathogenesis	1102:1131	Alzheimer disease pathogenesis	1102:1131	Several proteins related to Alzheimer disease pathogenesis have altered protein glycosylation, and recent glycomics studies have shown differences in cerebrospinal fluid as well as in brain tissue in Alzheimer disease as compared to controls.
34207636	5	22	theme	mass	983:986	arg1	spectrometry					988:999	mass spectrometry	983:999	mass spectrometry	983:999	Herein, we briefly touch upon important steps such as sample preparation and preconcentration, glycan release, glycan derivatization and quantification and advances in mass spectrometry that today are the work-horse for glycomics and glycoproteomics studies.
34207636	7	23	used	used	1384:1387	arg2	they					1369:1372	they	1369:1372	they	1369:1372	In this review, we discuss these techniques and how they have been used to shed light on Alzheimer disease and to find glycan biomarkers in cerebrospinal fluid.
34207636	0	24	dep	Tell	66:69	arg1	What					0:3	What	0:3	What	0:3	What Can N-glycomics and N-glycoproteomics of Cerebrospinal Fluid Tell Us about Alzheimer Disease?
34207636	6	25	theme	Alzheimer	1102:1110	arg1	pathogenesis					1120:1131	Alzheimer disease pathogenesis	1102:1131	Alzheimer disease pathogenesis	1102:1131	Several proteins related to Alzheimer disease pathogenesis have altered protein glycosylation, and recent glycomics studies have shown differences in cerebrospinal fluid as well as in brain tissue in Alzheimer disease as compared to controls.
34207636	4	26	theme	sample	738:743	arg1	preparation					745:755	sample preparation	738:755	sample preparation	738:755	The study of protein glycosylation requires a workflow that involves an array of sample preparation and analysis steps that needs to be carefully considered.
34207636	5	27	theme	sample	869:874	arg1	preparation					876:886	sample preparation	869:886	sample preparation	869:886	Herein, we briefly touch upon important steps such as sample preparation and preconcentration, glycan release, glycan derivatization and quantification and advances in mass spectrometry that today are the work-horse for glycomics and glycoproteomics studies.
34207636	1	28	theme	Proteomics-large-scale	99:120	arg1	studies					122:128	Proteomics-large-scale studies	99:128	Proteomics-large-scale studies of proteins-has over the last decade	99:165	Proteomics-large-scale studies of proteins-has over the last decade gained an enormous interest for studies aimed at revealing proteins and pathways involved in disease.
34207636	4	29	theme	glycosylation	678:690	arg1	study					661:665	The study	657:665	The study of protein glycosylation	657:690	The study of protein glycosylation requires a workflow that involves an array of sample preparation and analysis steps that needs to be carefully considered.
34207636	6	30	theme	protein	1146:1152	arg1	glycosylation					1154:1166	altered protein glycosylation	1138:1166	altered protein glycosylation	1138:1166	Several proteins related to Alzheimer disease pathogenesis have altered protein glycosylation, and recent glycomics studies have shown differences in cerebrospinal fluid as well as in brain tissue in Alzheimer disease as compared to controls.
34207636	4	31	theme	protein	670:676	arg1	glycosylation					678:690	protein glycosylation	670:690	protein glycosylation	670:690	The study of protein glycosylation requires a workflow that involves an array of sample preparation and analysis steps that needs to be carefully considered.
34207636	0	32	theme	Fluid	60:64	arg1	N-glycomics					9:19	N-glycomics	9:19	N-glycomics	9:19	What Can N-glycomics and N-glycoproteomics of Cerebrospinal Fluid Tell Us about Alzheimer Disease?
34207636	0	32	theme	Fluid	60:64	arg1	N-glycoproteomics					25:41	N-glycoproteomics	25:41	N-glycoproteomics	25:41	What Can N-glycomics and N-glycoproteomics of Cerebrospinal Fluid Tell Us about Alzheimer Disease?
34207636	6	33	theme	related	1091:1097	arg1	proteins					1082:1089	Several proteins	1074:1089	Several proteins related to Alzheimer disease pathogenesis	1074:1131	Several proteins related to Alzheimer disease pathogenesis have altered protein glycosylation, and recent glycomics studies have shown differences in cerebrospinal fluid as well as in brain tissue in Alzheimer disease as compared to controls.
34207636	7	34	theme	Alzheimer	1406:1414	arg1	disease					1416:1422	Alzheimer disease	1406:1422	Alzheimer disease	1406:1422	In this review, we discuss these techniques and how they have been used to shed light on Alzheimer disease and to find glycan biomarkers in cerebrospinal fluid.
34207636	6	35	theme	recent	1173:1178	arg1	studies					1190:1196	recent glycomics studies	1173:1196	recent glycomics studies	1173:1196	Several proteins related to Alzheimer disease pathogenesis have altered protein glycosylation, and recent glycomics studies have shown differences in cerebrospinal fluid as well as in brain tissue in Alzheimer disease as compared to controls.
34207636	2	36	theme	post-translational	357:374	arg1	modifications					376:388	post-translational modifications	357:388	post-translational modifications in the "omics"	357:403	To fully understand biological and pathological processes it is crucial to also include post-translational modifications in the "omics".
34207636	0	37	theme	Cerebrospinal	46:58	arg1	Fluid					60:64	Cerebrospinal Fluid	46:64	Cerebrospinal Fluid	46:64	What Can N-glycomics and N-glycoproteomics of Cerebrospinal Fluid Tell Us about Alzheimer Disease?
34207636	3	38	theme	attached	626:633	arg1	glycans					612:618	the glycans	608:618	the glycans still attached	608:633	To this end, glycomics (identification and quantification of glycans enzymatically or chemically released from proteins) and glycoproteomics (identification and quantification of peptides/proteins with the glycans still attached) is gaining interest.
34207636	1	39	theme	proteins-has	133:144	arg1	studies					122:128	Proteomics-large-scale studies	99:128	Proteomics-large-scale studies of proteins-has over the last decade	99:165	Proteomics-large-scale studies of proteins-has over the last decade gained an enormous interest for studies aimed at revealing proteins and pathways involved in disease.
34207636	6	40	theme	brain	1258:1262	arg1	tissue					1264:1269	brain tissue	1258:1269	brain tissue in Alzheimer disease	1258:1290	Several proteins related to Alzheimer disease pathogenesis have altered protein glycosylation, and recent glycomics studies have shown differences in cerebrospinal fluid as well as in brain tissue in Alzheimer disease as compared to controls.
34207636	5	41	theme	glycan	910:915	arg1	release					917:923	glycan release	910:923	glycan release	910:923	Herein, we briefly touch upon important steps such as sample preparation and preconcentration, glycan release, glycan derivatization and quantification and advances in mass spectrometry that today are the work-horse for glycomics and glycoproteomics studies.
34207636	6	42	theme	Alzheimer	1274:1282	arg1	disease					1284:1290	Alzheimer disease	1274:1290	Alzheimer disease	1274:1290	Several proteins related to Alzheimer disease pathogenesis have altered protein glycosylation, and recent glycomics studies have shown differences in cerebrospinal fluid as well as in brain tissue in Alzheimer disease as compared to controls.
34207636	7	43	theme	cerebrospinal	1457:1469	arg1	fluid					1471:1475	cerebrospinal fluid	1457:1475	cerebrospinal fluid	1457:1475	In this review, we discuss these techniques and how they have been used to shed light on Alzheimer disease and to find glycan biomarkers in cerebrospinal fluid.
34207636	2	44	dep	crucial	333:339	arg1	understand					278:287	understand	278:287	To fully understand biological and pathological processes	269:325	To fully understand biological and pathological processes it is crucial to also include post-translational modifications in the "omics".
34207636	3	45	theme	peptides/proteins	585:601	arg1	quantification					567:580	quantification	567:580	quantification	567:580	To this end, glycomics (identification and quantification of glycans enzymatically or chemically released from proteins) and glycoproteomics (identification and quantification of peptides/proteins with the glycans still attached) is gaining interest.
34207636	3	45	theme	peptides/proteins	585:601	arg1	identification					548:561	identification	548:561	identification	548:561	To this end, glycomics (identification and quantification of glycans enzymatically or chemically released from proteins) and glycoproteomics (identification and quantification of peptides/proteins with the glycans still attached) is gaining interest.
34207636	3	45	theme	peptides/proteins	585:601	arg1	glycoproteomics					531:545	glycoproteomics	531:545	glycoproteomics (identification and quantification of peptides/proteins with the glycans still attached)	531:634	To this end, glycomics (identification and quantification of glycans enzymatically or chemically released from proteins) and glycoproteomics (identification and quantification of peptides/proteins with the glycans still attached) is gaining interest.
34207636	7	46	dep	discuss	1336:1342	arg1	used					1384:1387	used	1384:1387	have been used to shed light on Alzheimer disease and to find glycan biomarkers in cerebrospinal fluid	1374:1475	In this review, we discuss these techniques and how they have been used to shed light on Alzheimer disease and to find glycan biomarkers in cerebrospinal fluid.
34207636	6	47	theme	glycomics	1180:1188	arg1	studies					1190:1196	recent glycomics studies	1173:1196	recent glycomics studies	1173:1196	Several proteins related to Alzheimer disease pathogenesis have altered protein glycosylation, and recent glycomics studies have shown differences in cerebrospinal fluid as well as in brain tissue in Alzheimer disease as compared to controls.
34207636	7	48	from	biomarkers	1443:1452	arg1	fluid					1471:1475	cerebrospinal fluid	1457:1475	cerebrospinal fluid	1457:1475	In this review, we discuss these techniques and how they have been used to shed light on Alzheimer disease and to find glycan biomarkers in cerebrospinal fluid.
34207636	4	49	theme	analysis	761:768	arg1	steps					770:774	analysis steps	761:774	analysis steps	761:774	The study of protein glycosylation requires a workflow that involves an array of sample preparation and analysis steps that needs to be carefully considered.
34207636	3	50	theme	glycans	467:473	arg1	quantification					449:462	quantification	449:462	quantification	449:462	To this end, glycomics (identification and quantification of glycans enzymatically or chemically released from proteins) and glycoproteomics (identification and quantification of peptides/proteins with the glycans still attached) is gaining interest.
34207636	3	50	theme	glycans	467:473	arg1	identification					430:443	identification	430:443	identification	430:443	To this end, glycomics (identification and quantification of glycans enzymatically or chemically released from proteins) and glycoproteomics (identification and quantification of peptides/proteins with the glycans still attached) is gaining interest.
34207636	3	50	theme	glycans	467:473	arg1	glycomics					419:427	glycomics	419:427	glycomics (identification and quantification of glycans enzymatically or chemically released from proteins)	419:525	To this end, glycomics (identification and quantification of glycans enzymatically or chemically released from proteins) and glycoproteomics (identification and quantification of peptides/proteins with the glycans still attached) is gaining interest.
34207636	1	51	theme	last	155:158	arg1	decade					160:165	the last decade	151:165	the last decade	151:165	Proteomics-large-scale studies of proteins-has over the last decade gained an enormous interest for studies aimed at revealing proteins and pathways involved in disease.
34207636	6	52	dep	differences	1209:1219	arg1	compared					1295:1302	compared	1295:1302	compared to controls	1295:1314	Several proteins related to Alzheimer disease pathogenesis have altered protein glycosylation, and recent glycomics studies have shown differences in cerebrospinal fluid as well as in brain tissue in Alzheimer disease as compared to controls.
34207636	5	53	theme	glycoproteomics	1049:1063	arg1	studies					1065:1071	glycoproteomics studies	1049:1071	glycoproteomics studies	1049:1071	Herein, we briefly touch upon important steps such as sample preparation and preconcentration, glycan release, glycan derivatization and quantification and advances in mass spectrometry that today are the work-horse for glycomics and glycoproteomics studies.
34207636	3	54	attach	released	503:510	arg2	glycans					467:473	glycans	467:473	glycans enzymatically or chemically released from proteins	467:524	To this end, glycomics (identification and quantification of glycans enzymatically or chemically released from proteins) and glycoproteomics (identification and quantification of peptides/proteins with the glycans still attached) is gaining interest.
34207636	3	54	attach	released	503:510	arg1	proteins					517:524	proteins	517:524	proteins	517:524	To this end, glycomics (identification and quantification of glycans enzymatically or chemically released from proteins) and glycoproteomics (identification and quantification of peptides/proteins with the glycans still attached) is gaining interest.
34207636	6	55	from	tissue	1264:1269	arg1	disease					1284:1290	Alzheimer disease	1274:1290	Alzheimer disease	1274:1290	Several proteins related to Alzheimer disease pathogenesis have altered protein glycosylation, and recent glycomics studies have shown differences in cerebrospinal fluid as well as in brain tissue in Alzheimer disease as compared to controls.
11447134	0	0	theme	beta-hexosaminidase	75:93	arg1	B					95:95	human beta-hexosaminidase B	69:95	human beta-hexosaminidase B	69:95	Complete analysis of the glycosylation and disulfide bond pattern of human beta-hexosaminidase B by MALDI-MS.
11447134	8	1	theme	enzymatic	1091:1099	arg1	deglycosylation					1101:1115	enzymatic deglycosylation	1091:1115	enzymatic deglycosylation	1091:1115	The analysis of the N-glycosylation was performed by tryptic digestion of the protein, isolation of glycopeptides by lectin chromatography and mass measurement before and after enzymatic deglycosylation.
11447134	8	2	theme	tryptic	967:973	arg1	digestion					975:983	tryptic digestion	967:983	tryptic digestion of the protein	967:998	The analysis of the N-glycosylation was performed by tryptic digestion of the protein, isolation of glycopeptides by lectin chromatography and mass measurement before and after enzymatic deglycosylation.
11447134	8	2	theme	tryptic	967:973	arg1	isolation					1001:1009	isolation	1001:1009	isolation of glycopeptides by lectin chromatography and mass measurement	1001:1072	The analysis of the N-glycosylation was performed by tryptic digestion of the protein, isolation of glycopeptides by lectin chromatography and mass measurement before and after enzymatic deglycosylation.
11447134	4	3	theme	bond	462:465	arg1	pattern					467:473	the disulfide bond pattern	448:473	the disulfide bond pattern of the protein	448:488	Here, the complete analysis of the disulfide bond pattern of the protein is described for the first time.
11447134	9	4	dep	glycosylated	1191:1202	arg1	peptide					1223:1229	peptide	1223:1229	peptide	1223:1229	Carbohydrate structures were calculated from the mass difference between glycosylated and deglycosylated peptide.
11447134	0	5	theme	human	69:73	arg1	B					95:95	human beta-hexosaminidase B	69:95	human beta-hexosaminidase B	69:95	Complete analysis of the glycosylation and disulfide bond pattern of human beta-hexosaminidase B by MALDI-MS.
11447134	5	6	theme	N-glycans	559:567	arg1	structures					541:550	the structures	537:550	the structures of the N-glycans	537:567	Additionally, the structures of the N-glycans are analyzed for the native human protein and for recombinant protein expressed in SF21 cells.
11447134	7	7	theme	disulfide	837:845	arg1	bonds					847:851	three disulfide bonds	831:851	three disulfide bonds (C91-C137; C309-C360; C534-C551)	831:884	The analysis revealed three disulfide bonds (C91-C137; C309-C360; C534-C551) and a free cysteine (C487).
11447134	4	8	theme	protein	482:488	arg1	pattern					467:473	the disulfide bond pattern	448:473	the disulfide bond pattern of the protein	448:488	Here, the complete analysis of the disulfide bond pattern of the protein is described for the first time.
11447134	5	9	theme	recombinant	619:629	arg1	protein					631:637	recombinant protein	619:637	recombinant protein expressed in SF21 cells	619:661	Additionally, the structures of the N-glycans are analyzed for the native human protein and for recombinant protein expressed in SF21 cells.
11447134	10	10	theme	recombinant	1336:1346	arg1	protein					1348:1354	the recombinant protein	1332:1354	the recombinant protein expressed in SF21 cells	1332:1378	For beta-hexosaminidase B from human placenta, four N-glycans were identified and analyzed, whereas the recombinant protein expressed in SF21 cells carried only three glycans.
11447134	0	11	theme	B	95:95	arg1	pattern					58:64	the glycosylation and disulfide bond pattern	21:64	pattern	58:64	Complete analysis of the glycosylation and disulfide bond pattern of human beta-hexosaminidase B by MALDI-MS.
11447134	0	11	theme	B	95:95	arg1	glycosylation					25:37	the glycosylation and disulfide bond pattern	21:64	glycosylation	25:37	Complete analysis of the glycosylation and disulfide bond pattern of human beta-hexosaminidase B by MALDI-MS.
11447134	4	12	theme	disulfide	452:460	arg1	pattern					467:473	the disulfide bond pattern	448:473	the disulfide bond pattern of the protein	448:488	Here, the complete analysis of the disulfide bond pattern of the protein is described for the first time.
11447134	6	13	theme	resulting	763:771	arg1	peptides					773:780	the resulting peptides	759:780	the resulting peptides	759:780	For the analysis of the disulfide bond structure, the protein was proteolytically digested and the resulting peptides were analyzed by MALDI-MS.
11447134	2	14	theme	Sandhoff	259:266	arg1	disorder					298:305	a glycolipid storage disorder	277:305	a glycolipid storage disorder characterized by severe neurodegeneration	277:347	Mutation in the HEXB gene lead to Sandhoff disease, a glycolipid storage disorder characterized by severe neurodegeneration.
11447134	2	14	theme	Sandhoff	259:266	arg1	disease					268:274	Sandhoff disease	259:274	Sandhoff disease	259:274	Mutation in the HEXB gene lead to Sandhoff disease, a glycolipid storage disorder characterized by severe neurodegeneration.
11447134	2	15	theme	severe	324:329	arg1	neurodegeneration					331:347	severe neurodegeneration	324:347	severe neurodegeneration	324:347	Mutation in the HEXB gene lead to Sandhoff disease, a glycolipid storage disorder characterized by severe neurodegeneration.
11447134	8	16	theme	protein	992:998	arg1	digestion					975:983	tryptic digestion	967:983	tryptic digestion of the protein	967:998	The analysis of the N-glycosylation was performed by tryptic digestion of the protein, isolation of glycopeptides by lectin chromatography and mass measurement before and after enzymatic deglycosylation.
11447134	8	16	theme	protein	992:998	arg1	isolation					1001:1009	isolation	1001:1009	isolation of glycopeptides by lectin chromatography and mass measurement	1001:1072	The analysis of the N-glycosylation was performed by tryptic digestion of the protein, isolation of glycopeptides by lectin chromatography and mass measurement before and after enzymatic deglycosylation.
11447134	10	17	theme	SF21	1369:1372	arg1	cells					1374:1378	SF21 cells	1369:1378	SF21 cells	1369:1378	For beta-hexosaminidase B from human placenta, four N-glycans were identified and analyzed, whereas the recombinant protein expressed in SF21 cells carried only three glycans.
11447134	8	18	gly	glycopeptides	1014:1026	arg2	glycopeptides					1014:1026	glycopeptides	1014:1026	glycopeptides	1014:1026	The analysis of the N-glycosylation was performed by tryptic digestion of the protein, isolation of glycopeptides by lectin chromatography and mass measurement before and after enzymatic deglycosylation.
11447134	11	19	gly	fucosylated	1528:1538	arg1	structures					1513:1522	some carbohydrate structures	1495:1522	some carbohydrate structures	1495:1522	In both cases the glycosylation belongs to the mannose-core- or high-mannose-type, and some carbohydrate structures are fucosylated.
11447134	4	20	theme	pattern	467:473	arg1	analysis					436:443	the complete analysis	423:443	the complete analysis of the disulfide bond pattern of the protein	423:488	Here, the complete analysis of the disulfide bond pattern of the protein is described for the first time.
11447134	5	21	theme	native	590:595	arg1	protein					603:609	the native human protein	586:609	the native human protein	586:609	Additionally, the structures of the N-glycans are analyzed for the native human protein and for recombinant protein expressed in SF21 cells.
11447134	8	22	theme	N-glycosylation	934:948	arg1	analysis					918:925	The analysis	914:925	The analysis of the N-glycosylation	914:948	The analysis of the N-glycosylation was performed by tryptic digestion of the protein, isolation of glycopeptides by lectin chromatography and mass measurement before and after enzymatic deglycosylation.
11447134	2	23	from	Mutation	225:232	arg1	gene					246:249	the HEXB gene	237:249	the HEXB gene	237:249	Mutation in the HEXB gene lead to Sandhoff disease, a glycolipid storage disorder characterized by severe neurodegeneration.
11447134	3	24	theme	structural	365:374	arg1	information					376:386	little structural information	358:386	little structural information on the protein	358:401	So far, little structural information on the protein is available.
11447134	3	25	from	information	376:386	arg1	protein					395:401	the protein	391:401	the protein	391:401	So far, little structural information on the protein is available.
11447134	5	26	theme	human	597:601	arg1	protein					603:609	the native human protein	586:609	the native human protein	586:609	Additionally, the structures of the N-glycans are analyzed for the native human protein and for recombinant protein expressed in SF21 cells.
11447134	7	27	theme	free	892:895	arg1	C487					907:910	C487	907:910	C487	907:910	The analysis revealed three disulfide bonds (C91-C137; C309-C360; C534-C551) and a free cysteine (C487).
11447134	7	27	theme	free	892:895	arg1	cysteine					897:904	a free cysteine	890:904	a free cysteine (C487)	890:911	The analysis revealed three disulfide bonds (C91-C137; C309-C360; C534-C551) and a free cysteine (C487).
11447134	2	28	theme	storage	290:296	arg1	disorder					298:305	a glycolipid storage disorder	277:305	a glycolipid storage disorder characterized by severe neurodegeneration	277:347	Mutation in the HEXB gene lead to Sandhoff disease, a glycolipid storage disorder characterized by severe neurodegeneration.
11447134	2	28	theme	storage	290:296	arg1	disease					268:274	Sandhoff disease	259:274	Sandhoff disease	259:274	Mutation in the HEXB gene lead to Sandhoff disease, a glycolipid storage disorder characterized by severe neurodegeneration.
11447134	10	29	theme	human	1263:1267	arg1	placenta					1269:1276	human placenta	1263:1276	human placenta	1263:1276	For beta-hexosaminidase B from human placenta, four N-glycans were identified and analyzed, whereas the recombinant protein expressed in SF21 cells carried only three glycans.
11447134	0	30	theme	Complete	0:7	arg1	analysis					9:16	Complete analysis	0:16	Complete analysis of the glycosylation and disulfide bond pattern of human beta-hexosaminidase B by MALDI-MS.	0:108	Complete analysis of the glycosylation and disulfide bond pattern of human beta-hexosaminidase B by MALDI-MS.
11447134	2	31	theme	glycolipid	279:288	arg1	disorder					298:305	a glycolipid storage disorder	277:305	a glycolipid storage disorder characterized by severe neurodegeneration	277:347	Mutation in the HEXB gene lead to Sandhoff disease, a glycolipid storage disorder characterized by severe neurodegeneration.
11447134	2	31	theme	glycolipid	279:288	arg1	disease					268:274	Sandhoff disease	259:274	Sandhoff disease	259:274	Mutation in the HEXB gene lead to Sandhoff disease, a glycolipid storage disorder characterized by severe neurodegeneration.
11447134	6	32	theme	bond	698:701	arg1	structure					703:711	the disulfide bond structure	684:711	the disulfide bond structure	684:711	For the analysis of the disulfide bond structure, the protein was proteolytically digested and the resulting peptides were analyzed by MALDI-MS.
11447134	8	33	theme	glycopeptides	1014:1026	arg1	digestion					975:983	tryptic digestion	967:983	tryptic digestion of the protein	967:998	The analysis of the N-glycosylation was performed by tryptic digestion of the protein, isolation of glycopeptides by lectin chromatography and mass measurement before and after enzymatic deglycosylation.
11447134	8	33	theme	glycopeptides	1014:1026	arg1	isolation					1001:1009	isolation	1001:1009	isolation of glycopeptides by lectin chromatography and mass measurement	1001:1072	The analysis of the N-glycosylation was performed by tryptic digestion of the protein, isolation of glycopeptides by lectin chromatography and mass measurement before and after enzymatic deglycosylation.
11447134	7	34	dep	C91-C137	854:861	arg1	C309-C360					864:872	C309-C360	864:872	C309-C360	864:872	The analysis revealed three disulfide bonds (C91-C137; C309-C360; C534-C551) and a free cysteine (C487).
11447134	7	34	dep	C91-C137	854:861	arg1	C534-C551					875:883	C534-C551	875:883	C534-C551	875:883	The analysis revealed three disulfide bonds (C91-C137; C309-C360; C534-C551) and a free cysteine (C487).
11447134	1	35	theme	glycolipids	184:194	arg1	degradation					169:179	the degradation	165:179	the degradation of glycolipids and glycans in the lysosome	165:222	beta-hexosaminidase B is an enzyme that is involved in the degradation of glycolipids and glycans in the lysosome.
11447134	3	36	theme	little	358:363	arg1	information					376:386	little structural information	358:386	little structural information on the protein	358:401	So far, little structural information on the protein is available.
11447134	4	37	theme	complete	427:434	arg1	analysis					436:443	the complete analysis	423:443	the complete analysis of the disulfide bond pattern of the protein	423:488	Here, the complete analysis of the disulfide bond pattern of the protein is described for the first time.
11447134	8	38	theme	lectin	1031:1036	arg1	chromatography					1038:1051	lectin chromatography	1031:1051	lectin chromatography	1031:1051	The analysis of the N-glycosylation was performed by tryptic digestion of the protein, isolation of glycopeptides by lectin chromatography and mass measurement before and after enzymatic deglycosylation.
11447134	10	39	theme	beta-hexosaminidase	1236:1254	arg1	B					1256:1256	beta-hexosaminidase B	1236:1256	beta-hexosaminidase B from human placenta	1236:1276	For beta-hexosaminidase B from human placenta, four N-glycans were identified and analyzed, whereas the recombinant protein expressed in SF21 cells carried only three glycans.
11447134	10	40	from	placenta	1269:1276	arg1	B					1256:1256	beta-hexosaminidase B	1236:1256	beta-hexosaminidase B from human placenta	1236:1276	For beta-hexosaminidase B from human placenta, four N-glycans were identified and analyzed, whereas the recombinant protein expressed in SF21 cells carried only three glycans.
11447134	1	41	theme	glycans	200:206	arg1	degradation					169:179	the degradation	165:179	the degradation of glycolipids and glycans in the lysosome	165:222	beta-hexosaminidase B is an enzyme that is involved in the degradation of glycolipids and glycans in the lysosome.
11447134	0	42	theme	glycosylation	25:37	arg1	analysis					9:16	Complete analysis	0:16	Complete analysis of the glycosylation and disulfide bond pattern of human beta-hexosaminidase B by MALDI-MS.	0:108	Complete analysis of the glycosylation and disulfide bond pattern of human beta-hexosaminidase B by MALDI-MS.
11447134	10	43	dep	identified	1299:1308	arg1	whereas					1324:1330	whereas	1324:1330	whereas	1324:1330	For beta-hexosaminidase B from human placenta, four N-glycans were identified and analyzed, whereas the recombinant protein expressed in SF21 cells carried only three glycans.
11447134	0	44	theme	bond	53:56	arg1	pattern					58:64	the glycosylation and disulfide bond pattern	21:64	pattern	58:64	Complete analysis of the glycosylation and disulfide bond pattern of human beta-hexosaminidase B by MALDI-MS.
11447134	7	45	dep	bonds	847:851	arg1	C91-C137					854:861	C91-C137	854:861	C91-C137; C309-C360; C534-C551	854:883	The analysis revealed three disulfide bonds (C91-C137; C309-C360; C534-C551) and a free cysteine (C487).
11447134	1	46	theme	beta-hexosaminidase	110:128	arg1	B					130:130	beta-hexosaminidase B	110:130	beta-hexosaminidase B	110:130	beta-hexosaminidase B is an enzyme that is involved in the degradation of glycolipids and glycans in the lysosome.
11447134	1	46	theme	beta-hexosaminidase	110:128	arg1	enzyme					138:143	an enzyme	135:143	an enzyme that is involved in the degradation of glycolipids and glycans in the lysosome	135:222	beta-hexosaminidase B is an enzyme that is involved in the degradation of glycolipids and glycans in the lysosome.
11447134	0	47	theme	disulfide	43:51	arg1	pattern					58:64	the glycosylation and disulfide bond pattern	21:64	pattern	58:64	Complete analysis of the glycosylation and disulfide bond pattern of human beta-hexosaminidase B by MALDI-MS.
11447134	4	48	theme	first	511:515	arg1	time					517:520	the first time	507:520	the first time	507:520	Here, the complete analysis of the disulfide bond pattern of the protein is described for the first time.
11447134	5	49	theme	SF21	652:655	arg1	cells					657:661	SF21 cells	652:661	SF21 cells	652:661	Additionally, the structures of the N-glycans are analyzed for the native human protein and for recombinant protein expressed in SF21 cells.
11447134	9	50	theme	mass	1167:1170	arg1	difference					1172:1181	the mass difference	1163:1181	the mass difference between glycosylated and deglycosylated peptide	1163:1229	Carbohydrate structures were calculated from the mass difference between glycosylated and deglycosylated peptide.
11447134	0	51	gly	glycosylation	25:37	arg1	B					95:95	human beta-hexosaminidase B	69:95	human beta-hexosaminidase B	69:95	Complete analysis of the glycosylation and disulfide bond pattern of human beta-hexosaminidase B by MALDI-MS.
11447134	6	52	theme	structure	703:711	arg1	analysis					672:679	the analysis	668:679	the analysis of the disulfide bond structure	668:711	For the analysis of the disulfide bond structure, the protein was proteolytically digested and the resulting peptides were analyzed by MALDI-MS.
11447134	8	53	theme	mass	1057:1060	arg1	measurement					1062:1072	mass measurement	1057:1072	mass measurement	1057:1072	The analysis of the N-glycosylation was performed by tryptic digestion of the protein, isolation of glycopeptides by lectin chromatography and mass measurement before and after enzymatic deglycosylation.
11447134	2	54	theme	HEXB	241:244	arg1	gene					246:249	the HEXB gene	237:249	the HEXB gene	237:249	Mutation in the HEXB gene lead to Sandhoff disease, a glycolipid storage disorder characterized by severe neurodegeneration.
11447134	1	55	from	degradation	169:179	arg1	lysosome					215:222	the lysosome	211:222	the lysosome	211:222	beta-hexosaminidase B is an enzyme that is involved in the degradation of glycolipids and glycans in the lysosome.
11447134	11	56	theme	carbohydrate	1500:1511	arg1	structures					1513:1522	some carbohydrate structures	1495:1522	some carbohydrate structures	1495:1522	In both cases the glycosylation belongs to the mannose-core- or high-mannose-type, and some carbohydrate structures are fucosylated.
11447134	6	57	theme	disulfide	688:696	arg1	structure					703:711	the disulfide bond structure	684:711	the disulfide bond structure	684:711	For the analysis of the disulfide bond structure, the protein was proteolytically digested and the resulting peptides were analyzed by MALDI-MS.
11447134	10	58	contain	carried	1380:1386	arg1	protein					1348:1354	the recombinant protein	1332:1354	the recombinant protein expressed in SF21 cells	1332:1378	For beta-hexosaminidase B from human placenta, four N-glycans were identified and analyzed, whereas the recombinant protein expressed in SF21 cells carried only three glycans.
11447134	10	58	contain	carried	1380:1386	arg2	glycans					1399:1405	only three glycans	1388:1405	only three glycans	1388:1405	For beta-hexosaminidase B from human placenta, four N-glycans were identified and analyzed, whereas the recombinant protein expressed in SF21 cells carried only three glycans.
11447134	0	59	theme	pattern	58:64	arg1	analysis					9:16	Complete analysis	0:16	Complete analysis of the glycosylation and disulfide bond pattern of human beta-hexosaminidase B by MALDI-MS.	0:108	Complete analysis of the glycosylation and disulfide bond pattern of human beta-hexosaminidase B by MALDI-MS.
11447134	9	60	theme	Carbohydrate	1118:1129	arg1	structures					1131:1140	Carbohydrate structures	1118:1140	Carbohydrate structures	1118:1140	Carbohydrate structures were calculated from the mass difference between glycosylated and deglycosylated peptide.
4077844	4	0	theme	Smith	696:700	arg1	degradation					702:712	Smith degradation	696:712	Smith degradation	696:712	The structures of purified PA-sugar chains were analyzed by a combination of stepwise exoglycosidase digestions, size determination by paper electrophoresis, methylation analysis, Smith degradation, and partial acetolysis.
4077844	2	1	attach	liberated	207:215	arg2	chains					195:200	The sugar chains	185:200	The sugar chains	185:200	The sugar chains were liberated from the polypeptide chains by hydrazinolysis, and the free amino groups were N-acetylated.
4077844	2	1	attach	liberated	207:215	arg1	chains					238:243	the polypeptide chains	222:243	the polypeptide chains	222:243	The sugar chains were liberated from the polypeptide chains by hydrazinolysis, and the free amino groups were N-acetylated.
4077844	0	2	theme	complement	59:68	arg1	component					40:48	the third component	30:48	the third component of human complement	30:68	Structures of sugar chains of the third component of human complement.
4077844	6	3	theme	C3	912:913	arg1	beta-chains					897:907	beta-chains	897:907	beta-chains	897:907	Analyses of the sugar chains of alpha- and beta-chains of C3 indicated that the alpha-chain contained mainly Man8GlcNAc2 and Man9GlcNAc2, while the beta-chain contained mainly Man5GlcNAc2 and Man6GlcNAc2.
4077844	6	3	theme	C3	912:913	arg1	alpha-					886:891	alpha-	886:891	alpha-	886:891	Analyses of the sugar chains of alpha- and beta-chains of C3 indicated that the alpha-chain contained mainly Man8GlcNAc2 and Man9GlcNAc2, while the beta-chain contained mainly Man5GlcNAc2 and Man6GlcNAc2.
4077844	5	4	theme	type	795:798	arg1	chains					806:811	two high-mannose type sugar chains	778:811	two high-mannose type sugar chains ranging from Man5GlcNAc2 to Man9GlcNAc2	778:851	These results showed that C3 contained two high-mannose type sugar chains ranging from Man5GlcNAc2 to Man9GlcNAc2.
4077844	6	5	contain	contained	1013:1021	arg1	beta-chain					1002:1011	the beta-chain	998:1011	the beta-chain	998:1011	Analyses of the sugar chains of alpha- and beta-chains of C3 indicated that the alpha-chain contained mainly Man8GlcNAc2 and Man9GlcNAc2, while the beta-chain contained mainly Man5GlcNAc2 and Man6GlcNAc2.
4077844	6	5	contain	contained	1013:1021	arg2	Man6GlcNAc2					1046:1056	Man6GlcNAc2	1046:1056	Man6GlcNAc2	1046:1056	Analyses of the sugar chains of alpha- and beta-chains of C3 indicated that the alpha-chain contained mainly Man8GlcNAc2 and Man9GlcNAc2, while the beta-chain contained mainly Man5GlcNAc2 and Man6GlcNAc2.
4077844	6	5	contain	contained	1013:1021	arg2	Man5GlcNAc2					1030:1040	Man5GlcNAc2	1030:1040	Man5GlcNAc2	1030:1040	Analyses of the sugar chains of alpha- and beta-chains of C3 indicated that the alpha-chain contained mainly Man8GlcNAc2 and Man9GlcNAc2, while the beta-chain contained mainly Man5GlcNAc2 and Man6GlcNAc2.
4077844	6	6	theme	beta-chains	897:907	arg1	chains					876:881	the sugar chains	866:881	the sugar chains of alpha- and beta-chains of C3	866:913	Analyses of the sugar chains of alpha- and beta-chains of C3 indicated that the alpha-chain contained mainly Man8GlcNAc2 and Man9GlcNAc2, while the beta-chain contained mainly Man5GlcNAc2 and Man6GlcNAc2.
4077844	1	7	theme	human	104:108	arg1	complement					110:119	human complement	104:119	human complement	104:119	Human C3, the third component of human complement, contained mannose and N-acetylglucosamine as sugar components.
4077844	3	8	theme	end	322:324	arg1	residues					326:333	The reducing end residues	309:333	The reducing end residues of the sugar chains thus obtained	309:367	The reducing end residues of the sugar chains thus obtained were tagged with 2-aminopyridine, and the pyridylamino (PA-) derivatives of sugar chains were separated by high-performance liquid chromatography.
4077844	3	8	theme	end	322:324	arg1	chains					348:353	the sugar chains	338:353	the sugar chains thus obtained	338:367	The reducing end residues of the sugar chains thus obtained were tagged with 2-aminopyridine, and the pyridylamino (PA-) derivatives of sugar chains were separated by high-performance liquid chromatography.
4077844	1	9	theme	third	85:89	arg1	C3					77:78	Human C3	71:78	Human C3	71:78	Human C3, the third component of human complement, contained mannose and N-acetylglucosamine as sugar components.
4077844	1	9	theme	third	85:89	arg1	component					91:99	the third component	81:99	the third component of human complement	81:119	Human C3, the third component of human complement, contained mannose and N-acetylglucosamine as sugar components.
4077844	4	10	theme	digestions	617:626	arg1	acetolysis					727:736	partial acetolysis	719:736	partial acetolysis	719:736	The structures of purified PA-sugar chains were analyzed by a combination of stepwise exoglycosidase digestions, size determination by paper electrophoresis, methylation analysis, Smith degradation, and partial acetolysis.
4077844	4	10	theme	digestions	617:626	arg1	determination					634:646	size determination	629:646	size determination by paper electrophoresis	629:671	The structures of purified PA-sugar chains were analyzed by a combination of stepwise exoglycosidase digestions, size determination by paper electrophoresis, methylation analysis, Smith degradation, and partial acetolysis.
4077844	4	10	theme	digestions	617:626	arg1	degradation					702:712	Smith degradation	696:712	Smith degradation	696:712	The structures of purified PA-sugar chains were analyzed by a combination of stepwise exoglycosidase digestions, size determination by paper electrophoresis, methylation analysis, Smith degradation, and partial acetolysis.
4077844	4	10	theme	digestions	617:626	arg1	combination					578:588	a combination	576:588	a combination of stepwise exoglycosidase digestions	576:626	The structures of purified PA-sugar chains were analyzed by a combination of stepwise exoglycosidase digestions, size determination by paper electrophoresis, methylation analysis, Smith degradation, and partial acetolysis.
4077844	4	10	theme	digestions	617:626	arg1	analysis					686:693	methylation analysis	674:693	methylation analysis	674:693	The structures of purified PA-sugar chains were analyzed by a combination of stepwise exoglycosidase digestions, size determination by paper electrophoresis, methylation analysis, Smith degradation, and partial acetolysis.
4077844	4	11	theme	paper	651:655	arg1	electrophoresis					657:671	paper electrophoresis	651:671	paper electrophoresis	651:671	The structures of purified PA-sugar chains were analyzed by a combination of stepwise exoglycosidase digestions, size determination by paper electrophoresis, methylation analysis, Smith degradation, and partial acetolysis.
4077844	5	12	theme	sugar	800:804	arg1	chains					806:811	two high-mannose type sugar chains	778:811	two high-mannose type sugar chains ranging from Man5GlcNAc2 to Man9GlcNAc2	778:851	These results showed that C3 contained two high-mannose type sugar chains ranging from Man5GlcNAc2 to Man9GlcNAc2.
4077844	6	13	theme	alpha-	886:891	arg1	chains					876:881	the sugar chains	866:881	the sugar chains of alpha- and beta-chains of C3	866:913	Analyses of the sugar chains of alpha- and beta-chains of C3 indicated that the alpha-chain contained mainly Man8GlcNAc2 and Man9GlcNAc2, while the beta-chain contained mainly Man5GlcNAc2 and Man6GlcNAc2.
4077844	3	14	theme	pyridylamino	411:422	arg1	derivatives					430:440	the pyridylamino (PA-) derivatives	407:440	the pyridylamino (PA-) derivatives of sugar chains	407:456	The reducing end residues of the sugar chains thus obtained were tagged with 2-aminopyridine, and the pyridylamino (PA-) derivatives of sugar chains were separated by high-performance liquid chromatography.
4077844	1	15	theme	Human	71:75	arg1	C3					77:78	Human C3	71:78	Human C3	71:78	Human C3, the third component of human complement, contained mannose and N-acetylglucosamine as sugar components.
4077844	1	15	theme	Human	71:75	arg1	component					91:99	the third component	81:99	the third component of human complement	81:119	Human C3, the third component of human complement, contained mannose and N-acetylglucosamine as sugar components.
4077844	1	16	contain	contained	122:130	arg2	mannose					132:138	mannose	132:138	mannose	132:138	Human C3, the third component of human complement, contained mannose and N-acetylglucosamine as sugar components.
4077844	1	16	contain	contained	122:130	arg1	C3					77:78	Human C3	71:78	Human C3	71:78	Human C3, the third component of human complement, contained mannose and N-acetylglucosamine as sugar components.
4077844	1	16	contain	contained	122:130	arg1	component					91:99	the third component	81:99	the third component of human complement	81:119	Human C3, the third component of human complement, contained mannose and N-acetylglucosamine as sugar components.
4077844	1	16	contain	contained	122:130	arg2	N-acetylglucosamine					144:162	N-acetylglucosamine	144:162	N-acetylglucosamine	144:162	Human C3, the third component of human complement, contained mannose and N-acetylglucosamine as sugar components.
4077844	1	16	contain	contained	122:130	arg2	components					173:182	sugar components	167:182	sugar components	167:182	Human C3, the third component of human complement, contained mannose and N-acetylglucosamine as sugar components.
4077844	4	17	theme	purified	534:541	arg1	chains					552:557	purified PA-sugar chains	534:557	purified PA-sugar chains	534:557	The structures of purified PA-sugar chains were analyzed by a combination of stepwise exoglycosidase digestions, size determination by paper electrophoresis, methylation analysis, Smith degradation, and partial acetolysis.
4077844	1	18	theme	sugar	167:171	arg1	N-acetylglucosamine					144:162	N-acetylglucosamine	144:162	N-acetylglucosamine	144:162	Human C3, the third component of human complement, contained mannose and N-acetylglucosamine as sugar components.
4077844	1	18	theme	sugar	167:171	arg1	components					173:182	sugar components	167:182	sugar components	167:182	Human C3, the third component of human complement, contained mannose and N-acetylglucosamine as sugar components.
4077844	1	18	theme	sugar	167:171	arg1	mannose					132:138	mannose	132:138	mannose	132:138	Human C3, the third component of human complement, contained mannose and N-acetylglucosamine as sugar components.
4077844	3	19	theme	sugar	342:346	arg1	chains					348:353	the sugar chains	338:353	the sugar chains thus obtained	338:367	The reducing end residues of the sugar chains thus obtained were tagged with 2-aminopyridine, and the pyridylamino (PA-) derivatives of sugar chains were separated by high-performance liquid chromatography.
4077844	6	20	contain	contained	946:954	arg2	Man9GlcNAc2					979:989	Man9GlcNAc2	979:989	Man9GlcNAc2	979:989	Analyses of the sugar chains of alpha- and beta-chains of C3 indicated that the alpha-chain contained mainly Man8GlcNAc2 and Man9GlcNAc2, while the beta-chain contained mainly Man5GlcNAc2 and Man6GlcNAc2.
4077844	6	20	contain	contained	946:954	arg1	alpha-chain					934:944	the alpha-chain	930:944	the alpha-chain	930:944	Analyses of the sugar chains of alpha- and beta-chains of C3 indicated that the alpha-chain contained mainly Man8GlcNAc2 and Man9GlcNAc2, while the beta-chain contained mainly Man5GlcNAc2 and Man6GlcNAc2.
4077844	6	20	contain	contained	946:954	arg2	Man8GlcNAc2					963:973	Man8GlcNAc2	963:973	Man8GlcNAc2	963:973	Analyses of the sugar chains of alpha- and beta-chains of C3 indicated that the alpha-chain contained mainly Man8GlcNAc2 and Man9GlcNAc2, while the beta-chain contained mainly Man5GlcNAc2 and Man6GlcNAc2.
4077844	2	21	theme	amino	277:281	arg1	N-acetylated					295:306	N-acetylated	295:306	N-acetylated	295:306	The sugar chains were liberated from the polypeptide chains by hydrazinolysis, and the free amino groups were N-acetylated.
4077844	2	21	theme	amino	277:281	arg1	groups					283:288	the free amino groups	268:288	the free amino groups	268:288	The sugar chains were liberated from the polypeptide chains by hydrazinolysis, and the free amino groups were N-acetylated.
4077844	0	22	theme	sugar	14:18	arg1	chains					20:25	sugar chains	14:25	sugar chains of the third component of human complement	14:68	Structures of sugar chains of the third component of human complement.
4077844	4	23	theme	chains	552:557	arg1	structures					520:529	The structures	516:529	The structures of purified PA-sugar chains	516:557	The structures of purified PA-sugar chains were analyzed by a combination of stepwise exoglycosidase digestions, size determination by paper electrophoresis, methylation analysis, Smith degradation, and partial acetolysis.
4077844	6	24	theme	chains	876:881	arg1	Analyses					854:861	Analyses	854:861	Analyses of the sugar chains of alpha- and beta-chains of C3	854:913	Analyses of the sugar chains of alpha- and beta-chains of C3 indicated that the alpha-chain contained mainly Man8GlcNAc2 and Man9GlcNAc2, while the beta-chain contained mainly Man5GlcNAc2 and Man6GlcNAc2.
4077844	2	25	theme	free	272:275	arg1	N-acetylated					295:306	N-acetylated	295:306	N-acetylated	295:306	The sugar chains were liberated from the polypeptide chains by hydrazinolysis, and the free amino groups were N-acetylated.
4077844	2	25	theme	free	272:275	arg1	groups					283:288	the free amino groups	268:288	the free amino groups	268:288	The sugar chains were liberated from the polypeptide chains by hydrazinolysis, and the free amino groups were N-acetylated.
4077844	3	26	theme	high-performance	476:491	arg1	chromatography					500:513	high-performance liquid chromatography	476:513	high-performance liquid chromatography	476:513	The reducing end residues of the sugar chains thus obtained were tagged with 2-aminopyridine, and the pyridylamino (PA-) derivatives of sugar chains were separated by high-performance liquid chromatography.
4077844	4	27	theme	PA-sugar	543:550	arg1	chains					552:557	purified PA-sugar chains	534:557	purified PA-sugar chains	534:557	The structures of purified PA-sugar chains were analyzed by a combination of stepwise exoglycosidase digestions, size determination by paper electrophoresis, methylation analysis, Smith degradation, and partial acetolysis.
4077844	6	28	theme	sugar	870:874	arg1	chains					876:881	the sugar chains	866:881	the sugar chains of alpha- and beta-chains of C3	866:913	Analyses of the sugar chains of alpha- and beta-chains of C3 indicated that the alpha-chain contained mainly Man8GlcNAc2 and Man9GlcNAc2, while the beta-chain contained mainly Man5GlcNAc2 and Man6GlcNAc2.
4077844	5	29	theme	high-mannose	782:793	arg1	chains					806:811	two high-mannose type sugar chains	778:811	two high-mannose type sugar chains ranging from Man5GlcNAc2 to Man9GlcNAc2	778:851	These results showed that C3 contained two high-mannose type sugar chains ranging from Man5GlcNAc2 to Man9GlcNAc2.
4077844	0	30	theme	chains	20:25	arg1	Structures					0:9	Structures	0:9	Structures of sugar chains of the third component of human complement	0:68	Structures of sugar chains of the third component of human complement.
4077844	4	31	theme	size	629:632	arg1	determination					634:646	size determination	629:646	size determination by paper electrophoresis	629:671	The structures of purified PA-sugar chains were analyzed by a combination of stepwise exoglycosidase digestions, size determination by paper electrophoresis, methylation analysis, Smith degradation, and partial acetolysis.
4077844	0	32	theme	component	40:48	arg1	chains					20:25	sugar chains	14:25	sugar chains of the third component of human complement	14:68	Structures of sugar chains of the third component of human complement.
4077844	3	33	theme	chains	451:456	arg1	derivatives					430:440	the pyridylamino (PA-) derivatives	407:440	the pyridylamino (PA-) derivatives of sugar chains	407:456	The reducing end residues of the sugar chains thus obtained were tagged with 2-aminopyridine, and the pyridylamino (PA-) derivatives of sugar chains were separated by high-performance liquid chromatography.
4077844	0	34	theme	third	34:38	arg1	component					40:48	the third component	30:48	the third component of human complement	30:68	Structures of sugar chains of the third component of human complement.
4077844	2	35	theme	sugar	189:193	arg1	chains					195:200	The sugar chains	185:200	The sugar chains	185:200	The sugar chains were liberated from the polypeptide chains by hydrazinolysis, and the free amino groups were N-acetylated.
4077844	4	36	theme	methylation	674:684	arg1	analysis					686:693	methylation analysis	674:693	methylation analysis	674:693	The structures of purified PA-sugar chains were analyzed by a combination of stepwise exoglycosidase digestions, size determination by paper electrophoresis, methylation analysis, Smith degradation, and partial acetolysis.
4077844	4	37	theme	partial	719:725	arg1	acetolysis					727:736	partial acetolysis	719:736	partial acetolysis	719:736	The structures of purified PA-sugar chains were analyzed by a combination of stepwise exoglycosidase digestions, size determination by paper electrophoresis, methylation analysis, Smith degradation, and partial acetolysis.
4077844	3	38	theme	sugar	445:449	arg1	chains					451:456	sugar chains	445:456	sugar chains	445:456	The reducing end residues of the sugar chains thus obtained were tagged with 2-aminopyridine, and the pyridylamino (PA-) derivatives of sugar chains were separated by high-performance liquid chromatography.
4077844	0	39	theme	human	53:57	arg1	complement					59:68	human complement	53:68	human complement	53:68	Structures of sugar chains of the third component of human complement.
4077844	2	40	theme	polypeptide	226:236	arg1	chains					238:243	the polypeptide chains	222:243	the polypeptide chains	222:243	The sugar chains were liberated from the polypeptide chains by hydrazinolysis, and the free amino groups were N-acetylated.
4077844	1	41	theme	complement	110:119	arg1	C3					77:78	Human C3	71:78	Human C3	71:78	Human C3, the third component of human complement, contained mannose and N-acetylglucosamine as sugar components.
4077844	1	41	theme	complement	110:119	arg1	component					91:99	the third component	81:99	the third component of human complement	81:119	Human C3, the third component of human complement, contained mannose and N-acetylglucosamine as sugar components.
4077844	4	42	theme	exoglycosidase	602:615	arg1	digestions					617:626	stepwise exoglycosidase digestions	593:626	stepwise exoglycosidase digestions	593:626	The structures of purified PA-sugar chains were analyzed by a combination of stepwise exoglycosidase digestions, size determination by paper electrophoresis, methylation analysis, Smith degradation, and partial acetolysis.
4077844	3	43	theme	reducing	313:320	arg1	residues					326:333	The reducing end residues	309:333	The reducing end residues of the sugar chains thus obtained	309:367	The reducing end residues of the sugar chains thus obtained were tagged with 2-aminopyridine, and the pyridylamino (PA-) derivatives of sugar chains were separated by high-performance liquid chromatography.
4077844	3	43	theme	reducing	313:320	arg1	chains					348:353	the sugar chains	338:353	the sugar chains thus obtained	338:367	The reducing end residues of the sugar chains thus obtained were tagged with 2-aminopyridine, and the pyridylamino (PA-) derivatives of sugar chains were separated by high-performance liquid chromatography.
4077844	5	44	contain	contained	768:776	arg1	C3					765:766	C3	765:766	C3	765:766	These results showed that C3 contained two high-mannose type sugar chains ranging from Man5GlcNAc2 to Man9GlcNAc2.
4077844	5	44	contain	contained	768:776	arg2	chains					806:811	two high-mannose type sugar chains	778:811	two high-mannose type sugar chains ranging from Man5GlcNAc2 to Man9GlcNAc2	778:851	These results showed that C3 contained two high-mannose type sugar chains ranging from Man5GlcNAc2 to Man9GlcNAc2.
4077844	3	45	theme	chains	348:353	arg1	residues					326:333	The reducing end residues	309:333	The reducing end residues of the sugar chains thus obtained	309:367	The reducing end residues of the sugar chains thus obtained were tagged with 2-aminopyridine, and the pyridylamino (PA-) derivatives of sugar chains were separated by high-performance liquid chromatography.
4077844	3	45	theme	chains	348:353	arg1	chains					348:353	the sugar chains	338:353	the sugar chains thus obtained	338:367	The reducing end residues of the sugar chains thus obtained were tagged with 2-aminopyridine, and the pyridylamino (PA-) derivatives of sugar chains were separated by high-performance liquid chromatography.
4077844	3	46	theme	liquid	493:498	arg1	chromatography					500:513	high-performance liquid chromatography	476:513	high-performance liquid chromatography	476:513	The reducing end residues of the sugar chains thus obtained were tagged with 2-aminopyridine, and the pyridylamino (PA-) derivatives of sugar chains were separated by high-performance liquid chromatography.
4077844	4	47	theme	stepwise	593:600	arg1	digestions					617:626	stepwise exoglycosidase digestions	593:626	stepwise exoglycosidase digestions	593:626	The structures of purified PA-sugar chains were analyzed by a combination of stepwise exoglycosidase digestions, size determination by paper electrophoresis, methylation analysis, Smith degradation, and partial acetolysis.
12794138	1	0	theme	class	304:308	arg1	members					319:325	other nonclassical class I family members	285:325	other nonclassical class I family members	285:325	MHC-related protein (MR)1 is an MHC class I-related molecule encoded on chromosome 1 that is highly conserved among mammals and is more closely related to classical class I molecules than are other nonclassical class I family members.
12794138	1	1	theme	class	129:133	arg1	molecule					145:152	an MHC class I-related molecule	122:152	an MHC class I-related molecule encoded on chromosome 1 that is highly conserved among mammals and is more closely related to classical class I molecules than are other nonclassical class I family members	122:325	MHC-related protein (MR)1 is an MHC class I-related molecule encoded on chromosome 1 that is highly conserved among mammals and is more closely related to classical class I molecules than are other nonclassical class I family members.
12794138	1	1	theme	class	129:133	arg1	MR					114:115	MHC-related protein (MR)1	93:117	MHC-related protein (MR)1	93:117	MHC-related protein (MR)1 is an MHC class I-related molecule encoded on chromosome 1 that is highly conserved among mammals and is more closely related to classical class I molecules than are other nonclassical class I family members.
12794138	1	1	theme	class	129:133	arg1	related					237:243	related	237:243	related	237:243	MHC-related protein (MR)1 is an MHC class I-related molecule encoded on chromosome 1 that is highly conserved among mammals and is more closely related to classical class I molecules than are other nonclassical class I family members.
12794138	3	2	theme	I	799:799	arg1	molecules					801:809	class I molecules	793:809	class I molecules	793:809	We also report the production of recombinant human MR1 molecules in insect cells using highly supplemented media and provide evidence that the MR1 H chain can assume a folded conformation and is stoichiometrically associated with beta(2)-microglobulin, similar to class I molecules.
12794138	3	3	theme	beta	759:762	arg1	-microglobulin					766:779	beta(2)-microglobulin	759:779	beta(2)-microglobulin	759:779	We also report the production of recombinant human MR1 molecules in insect cells using highly supplemented media and provide evidence that the MR1 H chain can assume a folded conformation and is stoichiometrically associated with beta(2)-microglobulin, similar to class I molecules.
12794138	0	4	theme	immunological	69:81	arg1	function					83:90	an immunological function	66:90	an immunological function	66:90	Biochemical features of the MHC-related protein 1 consistent with an immunological function.
12794138	1	5	theme	I	310:310	arg1	members					319:325	other nonclassical class I family members	285:325	other nonclassical class I family members	285:325	MHC-related protein (MR)1 is an MHC class I-related molecule encoded on chromosome 1 that is highly conserved among mammals and is more closely related to classical class I molecules than are other nonclassical class I family members.
12794138	1	6	theme	I-related	135:143	arg1	molecule					145:152	an MHC class I-related molecule	122:152	an MHC class I-related molecule encoded on chromosome 1 that is highly conserved among mammals and is more closely related to classical class I molecules than are other nonclassical class I family members	122:325	MHC-related protein (MR)1 is an MHC class I-related molecule encoded on chromosome 1 that is highly conserved among mammals and is more closely related to classical class I molecules than are other nonclassical class I family members.
12794138	1	6	theme	I-related	135:143	arg1	MR					114:115	MHC-related protein (MR)1	93:117	MHC-related protein (MR)1	93:117	MHC-related protein (MR)1 is an MHC class I-related molecule encoded on chromosome 1 that is highly conserved among mammals and is more closely related to classical class I molecules than are other nonclassical class I family members.
12794138	1	6	theme	I-related	135:143	arg1	related					237:243	related	237:243	related	237:243	MHC-related protein (MR)1 is an MHC class I-related molecule encoded on chromosome 1 that is highly conserved among mammals and is more closely related to classical class I molecules than are other nonclassical class I family members.
12794138	3	7	theme	similar	782:788	arg1	-microglobulin					766:779	beta(2)-microglobulin	759:779	beta(2)-microglobulin	759:779	We also report the production of recombinant human MR1 molecules in insect cells using highly supplemented media and provide evidence that the MR1 H chain can assume a folded conformation and is stoichiometrically associated with beta(2)-microglobulin, similar to class I molecules.
12794138	1	8	theme	family	312:317	arg1	members					319:325	other nonclassical class I family members	285:325	other nonclassical class I family members	285:325	MHC-related protein (MR)1 is an MHC class I-related molecule encoded on chromosome 1 that is highly conserved among mammals and is more closely related to classical class I molecules than are other nonclassical class I family members.
12794138	2	9	theme	cells	522:526	arg1	surface					499:505	the surface	495:505	the surface of transfected cells	495:526	In this report, we show for the first time that both mouse and human MR1 molecules can associate with the peptide-loading complex and can be detected at low levels at the surface of transfected cells.
12794138	4	10	theme	surface	858:864	arg1	expression					866:875	surface expression	858:875	surface expression of MR1	858:882	Cumulatively, these findings demonstrate that surface expression of MR1 is possible but may be limited by a specific ligand or associated molecule.
12794138	2	11	theme	transfected	510:520	arg1	cells					522:526	transfected cells	510:526	transfected cells	510:526	In this report, we show for the first time that both mouse and human MR1 molecules can associate with the peptide-loading complex and can be detected at low levels at the surface of transfected cells.
12794138	2	12	dep	molecules	401:409	arg1	both					376:379	both	376:379	both	376:379	In this report, we show for the first time that both mouse and human MR1 molecules can associate with the peptide-loading complex and can be detected at low levels at the surface of transfected cells.
12794138	2	12	dep	molecules	401:409	arg1	human					391:395	human	391:395	human	391:395	In this report, we show for the first time that both mouse and human MR1 molecules can associate with the peptide-loading complex and can be detected at low levels at the surface of transfected cells.
12794138	2	13	dep	both	376:379	arg1	mouse					381:385	mouse	381:385	mouse	381:385	In this report, we show for the first time that both mouse and human MR1 molecules can associate with the peptide-loading complex and can be detected at low levels at the surface of transfected cells.
12794138	1	14	dep	molecules	266:274	arg1	members					319:325	other nonclassical class I family members	285:325	other nonclassical class I family members	285:325	MHC-related protein (MR)1 is an MHC class I-related molecule encoded on chromosome 1 that is highly conserved among mammals and is more closely related to classical class I molecules than are other nonclassical class I family members.
12794138	4	15	theme	specific	920:927	arg1	ligand					929:934	a specific ligand	918:934	a specific ligand	918:934	Cumulatively, these findings demonstrate that surface expression of MR1 is possible but may be limited by a specific ligand or associated molecule.
12794138	4	16	theme	MR1	880:882	arg1	expression					866:875	surface expression	858:875	surface expression of MR1	858:882	Cumulatively, these findings demonstrate that surface expression of MR1 is possible but may be limited by a specific ligand or associated molecule.
12794138	3	17	theme	MR1	672:674	arg1	chain					678:682	the MR1 H chain	668:682	the MR1 H chain	668:682	We also report the production of recombinant human MR1 molecules in insect cells using highly supplemented media and provide evidence that the MR1 H chain can assume a folded conformation and is stoichiometrically associated with beta(2)-microglobulin, similar to class I molecules.
12794138	3	18	from	production	548:557	arg1	cells					604:608	insect cells	597:608	insect cells using highly supplemented media	597:640	We also report the production of recombinant human MR1 molecules in insect cells using highly supplemented media and provide evidence that the MR1 H chain can assume a folded conformation and is stoichiometrically associated with beta(2)-microglobulin, similar to class I molecules.
12794138	0	19	theme	Biochemical	0:10	arg1	features					12:19	Biochemical features	0:19	Biochemical features of the MHC-related protein 1 consistent with an immunological function	0:90	Biochemical features of the MHC-related protein 1 consistent with an immunological function.
12794138	3	20	theme	H	676:676	arg1	chain					678:682	the MR1 H chain	668:682	the MR1 H chain	668:682	We also report the production of recombinant human MR1 molecules in insect cells using highly supplemented media and provide evidence that the MR1 H chain can assume a folded conformation and is stoichiometrically associated with beta(2)-microglobulin, similar to class I molecules.
12794138	1	21	theme	MHC-related	93:103	arg1	MR					114:115	MHC-related protein (MR)1	93:117	MHC-related protein (MR)1	93:117	MHC-related protein (MR)1 is an MHC class I-related molecule encoded on chromosome 1 that is highly conserved among mammals and is more closely related to classical class I molecules than are other nonclassical class I family members.
12794138	1	21	theme	MHC-related	93:103	arg1	molecule					145:152	an MHC class I-related molecule	122:152	an MHC class I-related molecule encoded on chromosome 1 that is highly conserved among mammals and is more closely related to classical class I molecules than are other nonclassical class I family members	122:325	MHC-related protein (MR)1 is an MHC class I-related molecule encoded on chromosome 1 that is highly conserved among mammals and is more closely related to classical class I molecules than are other nonclassical class I family members.
12794138	1	21	theme	MHC-related	93:103	arg1	related					237:243	related	237:243	related	237:243	MHC-related protein (MR)1 is an MHC class I-related molecule encoded on chromosome 1 that is highly conserved among mammals and is more closely related to classical class I molecules than are other nonclassical class I family members.
12794138	4	22	theme	associated	939:948	arg1	molecule					950:957	associated molecule	939:957	associated molecule	939:957	Cumulatively, these findings demonstrate that surface expression of MR1 is possible but may be limited by a specific ligand or associated molecule.
12794138	1	23	theme	classical	248:256	arg1	molecules					266:274	classical class I molecules	248:274	classical class I molecules than are other nonclassical class I family members	248:325	MHC-related protein (MR)1 is an MHC class I-related molecule encoded on chromosome 1 that is highly conserved among mammals and is more closely related to classical class I molecules than are other nonclassical class I family members.
12794138	1	24	theme	protein	105:111	arg1	MR					114:115	MHC-related protein (MR)1	93:117	MHC-related protein (MR)1	93:117	MHC-related protein (MR)1 is an MHC class I-related molecule encoded on chromosome 1 that is highly conserved among mammals and is more closely related to classical class I molecules than are other nonclassical class I family members.
12794138	1	24	theme	protein	105:111	arg1	molecule					145:152	an MHC class I-related molecule	122:152	an MHC class I-related molecule encoded on chromosome 1 that is highly conserved among mammals and is more closely related to classical class I molecules than are other nonclassical class I family members	122:325	MHC-related protein (MR)1 is an MHC class I-related molecule encoded on chromosome 1 that is highly conserved among mammals and is more closely related to classical class I molecules than are other nonclassical class I family members.
12794138	1	24	theme	protein	105:111	arg1	related					237:243	related	237:243	related	237:243	MHC-related protein (MR)1 is an MHC class I-related molecule encoded on chromosome 1 that is highly conserved among mammals and is more closely related to classical class I molecules than are other nonclassical class I family members.
12794138	1	25	theme	class	258:262	arg1	molecules					266:274	classical class I molecules	248:274	classical class I molecules than are other nonclassical class I family members	248:325	MHC-related protein (MR)1 is an MHC class I-related molecule encoded on chromosome 1 that is highly conserved among mammals and is more closely related to classical class I molecules than are other nonclassical class I family members.
12794138	2	26	theme	low	481:483	arg1	levels					485:490	low levels	481:490	low levels	481:490	In this report, we show for the first time that both mouse and human MR1 molecules can associate with the peptide-loading complex and can be detected at low levels at the surface of transfected cells.
12794138	3	27	theme	human	574:578	arg1	molecules					584:592	recombinant human MR1 molecules	562:592	recombinant human MR1 molecules	562:592	We also report the production of recombinant human MR1 molecules in insect cells using highly supplemented media and provide evidence that the MR1 H chain can assume a folded conformation and is stoichiometrically associated with beta(2)-microglobulin, similar to class I molecules.
12794138	2	28	located	detected	469:476	arg1	levels					485:490	low levels	481:490	low levels	481:490	In this report, we show for the first time that both mouse and human MR1 molecules can associate with the peptide-loading complex and can be detected at low levels at the surface of transfected cells.
12794138	2	28	located	detected	469:476	arg2	molecules					401:409	both mouse and human MR1 molecules	376:409	both mouse and human MR1 molecules	376:409	In this report, we show for the first time that both mouse and human MR1 molecules can associate with the peptide-loading complex and can be detected at low levels at the surface of transfected cells.
12794138	2	28	located	detected	469:476	arg1	surface					499:505	the surface	495:505	the surface of transfected cells	495:526	In this report, we show for the first time that both mouse and human MR1 molecules can associate with the peptide-loading complex and can be detected at low levels at the surface of transfected cells.
12794138	2	29	theme	first	360:364	arg1	time					366:369	the first time	356:369	the first time	356:369	In this report, we show for the first time that both mouse and human MR1 molecules can associate with the peptide-loading complex and can be detected at low levels at the surface of transfected cells.
12794138	0	30	theme	protein	40:46	arg1	features					12:19	Biochemical features	0:19	Biochemical features of the MHC-related protein 1 consistent with an immunological function	0:90	Biochemical features of the MHC-related protein 1 consistent with an immunological function.
12794138	1	31	theme	I	264:264	arg1	molecules					266:274	classical class I molecules	248:274	classical class I molecules than are other nonclassical class I family members	248:325	MHC-related protein (MR)1 is an MHC class I-related molecule encoded on chromosome 1 that is highly conserved among mammals and is more closely related to classical class I molecules than are other nonclassical class I family members.
12794138	3	32	theme	MR1	580:582	arg1	molecules					584:592	recombinant human MR1 molecules	562:592	recombinant human MR1 molecules	562:592	We also report the production of recombinant human MR1 molecules in insect cells using highly supplemented media and provide evidence that the MR1 H chain can assume a folded conformation and is stoichiometrically associated with beta(2)-microglobulin, similar to class I molecules.
12794138	0	33	theme	MHC-related	28:38	arg1	protein					40:46	the MHC-related protein 1	24:48	the MHC-related protein 1 consistent with an immunological function	24:90	Biochemical features of the MHC-related protein 1 consistent with an immunological function.
12794138	0	34	theme	consistent	50:59	arg1	protein					40:46	the MHC-related protein 1	24:48	the MHC-related protein 1 consistent with an immunological function	24:90	Biochemical features of the MHC-related protein 1 consistent with an immunological function.
12794138	3	35	theme	folded	697:702	arg1	conformation					704:715	a folded conformation	695:715	a folded conformation	695:715	We also report the production of recombinant human MR1 molecules in insect cells using highly supplemented media and provide evidence that the MR1 H chain can assume a folded conformation and is stoichiometrically associated with beta(2)-microglobulin, similar to class I molecules.
12794138	3	36	theme	recombinant	562:572	arg1	molecules					584:592	recombinant human MR1 molecules	562:592	recombinant human MR1 molecules	562:592	We also report the production of recombinant human MR1 molecules in insect cells using highly supplemented media and provide evidence that the MR1 H chain can assume a folded conformation and is stoichiometrically associated with beta(2)-microglobulin, similar to class I molecules.
12794138	1	37	dep	members	319:325	arg1	than					276:279	than	276:279	than	276:279	MHC-related protein (MR)1 is an MHC class I-related molecule encoded on chromosome 1 that is highly conserved among mammals and is more closely related to classical class I molecules than are other nonclassical class I family members.
12794138	1	37	dep	members	319:325	arg1	are					281:283	are	281:283	are	281:283	MHC-related protein (MR)1 is an MHC class I-related molecule encoded on chromosome 1 that is highly conserved among mammals and is more closely related to classical class I molecules than are other nonclassical class I family members.
12794138	3	38	theme	supplemented	623:634	arg1	media					636:640	highly supplemented media	616:640	highly supplemented media	616:640	We also report the production of recombinant human MR1 molecules in insect cells using highly supplemented media and provide evidence that the MR1 H chain can assume a folded conformation and is stoichiometrically associated with beta(2)-microglobulin, similar to class I molecules.
12794138	3	39	theme	insect	597:602	arg1	cells					604:608	insect cells	597:608	insect cells using highly supplemented media	597:640	We also report the production of recombinant human MR1 molecules in insect cells using highly supplemented media and provide evidence that the MR1 H chain can assume a folded conformation and is stoichiometrically associated with beta(2)-microglobulin, similar to class I molecules.
12794138	1	40	theme	other	285:289	arg1	members					319:325	other nonclassical class I family members	285:325	other nonclassical class I family members	285:325	MHC-related protein (MR)1 is an MHC class I-related molecule encoded on chromosome 1 that is highly conserved among mammals and is more closely related to classical class I molecules than are other nonclassical class I family members.
12794138	3	41	theme	molecules	584:592	arg1	production					548:557	the production	544:557	the production of recombinant human MR1 molecules in insect cells using highly supplemented media	544:640	We also report the production of recombinant human MR1 molecules in insect cells using highly supplemented media and provide evidence that the MR1 H chain can assume a folded conformation and is stoichiometrically associated with beta(2)-microglobulin, similar to class I molecules.
12794138	0	42	with	consistent	50:59	arg1	function					83:90	an immunological function	66:90	an immunological function	66:90	Biochemical features of the MHC-related protein 1 consistent with an immunological function.
12794138	2	43	theme	peptide-loading	434:448	arg1	complex					450:456	the peptide-loading complex	430:456	the peptide-loading complex	430:456	In this report, we show for the first time that both mouse and human MR1 molecules can associate with the peptide-loading complex and can be detected at low levels at the surface of transfected cells.
12794138	2	44	theme	MR1	397:399	arg1	molecules					401:409	both mouse and human MR1 molecules	376:409	both mouse and human MR1 molecules	376:409	In this report, we show for the first time that both mouse and human MR1 molecules can associate with the peptide-loading complex and can be detected at low levels at the surface of transfected cells.
12794138	1	45	theme	nonclassical	291:302	arg1	members					319:325	other nonclassical class I family members	285:325	other nonclassical class I family members	285:325	MHC-related protein (MR)1 is an MHC class I-related molecule encoded on chromosome 1 that is highly conserved among mammals and is more closely related to classical class I molecules than are other nonclassical class I family members.
12794138	1	46	theme	MHC	125:127	arg1	molecule					145:152	an MHC class I-related molecule	122:152	an MHC class I-related molecule encoded on chromosome 1 that is highly conserved among mammals and is more closely related to classical class I molecules than are other nonclassical class I family members	122:325	MHC-related protein (MR)1 is an MHC class I-related molecule encoded on chromosome 1 that is highly conserved among mammals and is more closely related to classical class I molecules than are other nonclassical class I family members.
12794138	1	46	theme	MHC	125:127	arg1	MR					114:115	MHC-related protein (MR)1	93:117	MHC-related protein (MR)1	93:117	MHC-related protein (MR)1 is an MHC class I-related molecule encoded on chromosome 1 that is highly conserved among mammals and is more closely related to classical class I molecules than are other nonclassical class I family members.
12794138	1	46	theme	MHC	125:127	arg1	related					237:243	related	237:243	related	237:243	MHC-related protein (MR)1 is an MHC class I-related molecule encoded on chromosome 1 that is highly conserved among mammals and is more closely related to classical class I molecules than are other nonclassical class I family members.
12794138	3	47	theme	class	793:797	arg1	molecules					801:809	class I molecules	793:809	class I molecules	793:809	We also report the production of recombinant human MR1 molecules in insect cells using highly supplemented media and provide evidence that the MR1 H chain can assume a folded conformation and is stoichiometrically associated with beta(2)-microglobulin, similar to class I molecules.
19159218	9	0	theme	corresponding	1578:1590	arg1	small					1634:1638	small	1634:1638	small	1634:1638	Among the 317 additional N-glycosites, 98 (30.9%) could not be identified by trypsin in theory because the corresponding in silico tryptic peptides are either too small or too big to detect in mass spectrometer.
19159218	9	0	theme	corresponding	1578:1590	arg1	either					1623:1628	either	1623:1628	either	1623:1628	Among the 317 additional N-glycosites, 98 (30.9%) could not be identified by trypsin in theory because the corresponding in silico tryptic peptides are either too small or too big to detect in mass spectrometer.
19159218	9	0	theme	corresponding	1578:1590	arg1	peptides					1610:1617	the corresponding in silico tryptic peptides	1574:1617	the corresponding in silico tryptic peptides	1574:1617	Among the 317 additional N-glycosites, 98 (30.9%) could not be identified by trypsin in theory because the corresponding in silico tryptic peptides are either too small or too big to detect in mass spectrometer.
19159218	2	1	theme	N-glycopeptides	363:377	arg1	extraction					341:350	Solid phase extraction	329:350	Solid phase extraction of tryptic N-glycopeptides by hydrazide chemistry	329:400	Solid phase extraction of tryptic N-glycopeptides by hydrazide chemistry is becoming a popular protocol for the analysis of N-glycoproteome.
19159218	1	2	theme	dynamic	249:255	arg1	complexity					232:241	the enormous complexity	219:241	the enormous complexity	219:241	The study of protein glycosylation has lagged far behind the progress of current proteomics because of the enormous complexity, wide dynamic range distribution and low stoichiometric modification of glycoprotein.
19159218	1	2	theme	dynamic	249:255	arg1	range					257:261	wide dynamic range	244:261	wide dynamic range	244:261	The study of protein glycosylation has lagged far behind the progress of current proteomics because of the enormous complexity, wide dynamic range distribution and low stoichiometric modification of glycoprotein.
19159218	11	3	theme	human	2039:2043	arg1	liver					2045:2049	human liver	2039:2049	human liver	2039:2049	A total number of 939 N-glycosites were identified confidently, covering 523 noredundant glycoproteins from human liver tissue, which leads to the establishment of the largest data set of glycoproteome from human liver up to now.
19159218	8	4	theme	trypsin	1315:1321	arg1	Use					1308:1310	Use	1308:1310	Use of trypsin	1308:1321	Use of trypsin alone resulted in identification of 622 N-glycosites, while using pepsin and thermolysin resulted in identification of 317 additional N-glycosites.
19159218	3	5	theme	significant	566:576	arg1	percentage					578:587	a significant percentage	564:587	a significant percentage of tryptic N-glycopeptides	564:614	However, in silico digestion of proteins in human proteome database by trypsin indicates that a significant percentage of tryptic N-glycopeptides is not in the preferred detection mass range of shotgun proteomics approach, that is, from 800 to 3500 Da.
19159218	6	6	theme	enzyme	1138:1143	arg1	digestion					1145:1153	multiple enzyme digestion	1129:1153	multiple enzyme digestion	1129:1153	Herein, we describe a comprehensive way to analyze the N-glycoproteome of human liver tissue by combination of hydrazide chemistry method and multiple enzyme digestion.
19159218	8	7	gly	N-glycosites	1363:1374	arg2	N-glycosites					1363:1374	622 N-glycosites	1359:1374	622 N-glycosites	1359:1374	Use of trypsin alone resulted in identification of 622 N-glycosites, while using pepsin and thermolysin resulted in identification of 317 additional N-glycosites.
19159218	3	8	theme	N-glycopeptides	600:614	arg1	percentage					578:587	a significant percentage	564:587	a significant percentage of tryptic N-glycopeptides	564:614	However, in silico digestion of proteins in human proteome database by trypsin indicates that a significant percentage of tryptic N-glycopeptides is not in the preferred detection mass range of shotgun proteomics approach, that is, from 800 to 3500 Da.
19159218	11	9	theme	largest	2000:2006	arg1	glycoproteome					2020:2032	glycoproteome	2020:2032	glycoproteome from human liver	2020:2049	A total number of 939 N-glycosites were identified confidently, covering 523 noredundant glycoproteins from human liver tissue, which leads to the establishment of the largest data set of glycoproteome from human liver up to now.
19159218	11	9	theme	largest	2000:2006	arg1	set					2013:2015	the largest data set	1996:2015	the largest data set of glycoproteome from human liver	1996:2049	A total number of 939 N-glycosites were identified confidently, covering 523 noredundant glycoproteins from human liver tissue, which leads to the establishment of the largest data set of glycoproteome from human liver up to now.
19159218	6	10	theme	chemistry	1108:1116	arg1	method					1118:1123	hydrazide chemistry method	1098:1123	hydrazide chemistry method	1098:1123	Herein, we describe a comprehensive way to analyze the N-glycoproteome of human liver tissue by combination of hydrazide chemistry method and multiple enzyme digestion.
19159218	4	11	gly	N-glycosites	814:825	arg2	N-glycosites					814:825	N-glycosites	814:825	N-glycosites	814:825	And the quite big size of glycan groups may block trypsin to access the K, R residues near N-glycosites for digestion, which will result in generation of big glycopeptides.
19159218	10	12	theme	N-glycosites	1736:1747	arg1	coverage					1724:1731	the coverage	1720:1731	the coverage of N-glycosites	1720:1747	This study clearly demonstrated that the coverage of N-glycosites could be significantly increased due to the adoption of multiple enzyme digestion.
19159218	11	13	theme	glycoproteome	2020:2032	arg1	glycoproteome					2020:2032	glycoproteome	2020:2032	glycoproteome from human liver	2020:2049	A total number of 939 N-glycosites were identified confidently, covering 523 noredundant glycoproteins from human liver tissue, which leads to the establishment of the largest data set of glycoproteome from human liver up to now.
19159218	11	13	theme	glycoproteome	2020:2032	arg1	set					2013:2015	the largest data set	1996:2015	the largest data set of glycoproteome from human liver	1996:2049	A total number of 939 N-glycosites were identified confidently, covering 523 noredundant glycoproteins from human liver tissue, which leads to the establishment of the largest data set of glycoproteome from human liver up to now.
19159218	11	14	theme	set	2013:2015	arg1	establishment					1979:1991	the establishment	1975:1991	the establishment of the largest data set of glycoproteome from human liver up to now	1975:2059	A total number of 939 N-glycosites were identified confidently, covering 523 noredundant glycoproteins from human liver tissue, which leads to the establishment of the largest data set of glycoproteome from human liver up to now.
19159218	3	15	gly	N-glycopeptides	600:614	arg2	N-glycopeptides					600:614	tryptic N-glycopeptides	592:614	tryptic N-glycopeptides	592:614	However, in silico digestion of proteins in human proteome database by trypsin indicates that a significant percentage of tryptic N-glycopeptides is not in the preferred detection mass range of shotgun proteomics approach, that is, from 800 to 3500 Da.
19159218	8	16	gly	N-glycosites	1457:1468	arg2	N-glycosites					1457:1468	317 additional N-glycosites	1442:1468	317 additional N-glycosites	1442:1468	Use of trypsin alone resulted in identification of 622 N-glycosites, while using pepsin and thermolysin resulted in identification of 317 additional N-glycosites.
19159218	4	17	theme	big	877:879	arg1	glycopeptides					881:893	big glycopeptides	877:893	big glycopeptides	877:893	And the quite big size of glycan groups may block trypsin to access the K, R residues near N-glycosites for digestion, which will result in generation of big glycopeptides.
19159218	11	18	from	set	2013:2015	arg1	liver					2045:2049	human liver	2039:2049	human liver	2039:2049	A total number of 939 N-glycosites were identified confidently, covering 523 noredundant glycoproteins from human liver tissue, which leads to the establishment of the largest data set of glycoproteome from human liver up to now.
19159218	11	19	theme	human	1940:1944	arg1	tissue					1952:1957	human liver tissue	1940:1957	human liver tissue	1940:1957	A total number of 939 N-glycosites were identified confidently, covering 523 noredundant glycoproteins from human liver tissue, which leads to the establishment of the largest data set of glycoproteome from human liver up to now.
19159218	1	20	gly	glycoprotein	315:326	arg1	glycoprotein					315:326	glycoprotein	315:326	glycoprotein	315:326	The study of protein glycosylation has lagged far behind the progress of current proteomics because of the enormous complexity, wide dynamic range distribution and low stoichiometric modification of glycoprotein.
19159218	5	21	theme	many	901:904	arg1	N-glycosites					906:917	many N-glycosites	901:917	many N-glycosites	901:917	Thus many N-glycosites could not be localized if only trypsin was used to digest proteins.
19159218	10	22	gly	N-glycosites	1736:1747	arg2	N-glycosites					1736:1747	N-glycosites	1736:1747	N-glycosites	1736:1747	This study clearly demonstrated that the coverage of N-glycosites could be significantly increased due to the adoption of multiple enzyme digestion.
19159218	3	23	theme	detection	640:648	arg1	range					655:659	the preferred detection mass range	626:659	the preferred detection mass range of shotgun proteomics approach, that is, from 800 to 3500 Da	626:720	However, in silico digestion of proteins in human proteome database by trypsin indicates that a significant percentage of tryptic N-glycopeptides is not in the preferred detection mass range of shotgun proteomics approach, that is, from 800 to 3500 Da.
19159218	8	24	theme	additional	1446:1455	arg1	N-glycosites					1457:1468	317 additional N-glycosites	1442:1468	317 additional N-glycosites	1442:1468	Use of trypsin alone resulted in identification of 622 N-glycosites, while using pepsin and thermolysin resulted in identification of 317 additional N-glycosites.
19159218	0	25	theme	enzyme	74:79	arg1	digestion					81:89	multiple enzyme digestion	65:89	multiple enzyme digestion	65:89	Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.
19159218	4	26	theme	groups	756:761	arg1	size					741:744	And the quite big size	723:744	size	741:744	And the quite big size of glycan groups may block trypsin to access the K, R residues near N-glycosites for digestion, which will result in generation of big glycopeptides.
19159218	7	27	theme	human	1170:1174	arg1	tissue					1182:1187	human liver tissue	1170:1187	human liver tissue	1170:1187	The lysate of human liver tissue was digested with three proteases, that is, trypsin, pepsin and thermolysin, with different specificities, separately.
19159218	1	28	theme	protein	129:135	arg1	glycosylation					137:149	protein glycosylation	129:149	protein glycosylation	129:149	The study of protein glycosylation has lagged far behind the progress of current proteomics because of the enormous complexity, wide dynamic range distribution and low stoichiometric modification of glycoprotein.
19159218	4	29	theme	big	737:739	arg1	size					741:744	And the quite big size	723:744	size	741:744	And the quite big size of glycan groups may block trypsin to access the K, R residues near N-glycosites for digestion, which will result in generation of big glycopeptides.
19159218	2	30	theme	popular	416:422	arg1	protocol					424:431	a popular protocol	414:431	a popular protocol for the analysis of N-glycoproteome	414:467	Solid phase extraction of tryptic N-glycopeptides by hydrazide chemistry is becoming a popular protocol for the analysis of N-glycoproteome.
19159218	0	31	theme	chemistry	105:113	arg1	combination					50:60	combination	50:60	combination of multiple enzyme digestion and hydrazide chemistry	50:113	Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.
19159218	9	32	dep	either	1623:1628	arg1	small					1634:1638	small	1634:1638	small	1634:1638	Among the 317 additional N-glycosites, 98 (30.9%) could not be identified by trypsin in theory because the corresponding in silico tryptic peptides are either too small or too big to detect in mass spectrometer.
19159218	9	32	dep	either	1623:1628	arg1	either					1623:1628	either	1623:1628	either	1623:1628	Among the 317 additional N-glycosites, 98 (30.9%) could not be identified by trypsin in theory because the corresponding in silico tryptic peptides are either too small or too big to detect in mass spectrometer.
19159218	9	32	dep	either	1623:1628	arg1	peptides					1610:1617	the corresponding in silico tryptic peptides	1574:1617	the corresponding in silico tryptic peptides	1574:1617	Among the 317 additional N-glycosites, 98 (30.9%) could not be identified by trypsin in theory because the corresponding in silico tryptic peptides are either too small or too big to detect in mass spectrometer.
19159218	1	33	dep	lagged	155:160	arg1	behind					166:171	behind	166:171	has lagged far behind the progress of current proteomics because of the enormous complexity, wide dynamic range distribution and low stoichiometric modification of glycoprotein	151:326	The study of protein glycosylation has lagged far behind the progress of current proteomics because of the enormous complexity, wide dynamic range distribution and low stoichiometric modification of glycoprotein.
19159218	0	34	theme	Glycoproteomics	0:14	arg1	analysis					16:23	Glycoproteomics analysis	0:23	Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.	0:114	Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.
19159218	2	35	theme	N-glycoproteome	453:467	arg1	analysis					441:448	the analysis	437:448	the analysis of N-glycoproteome	437:467	Solid phase extraction of tryptic N-glycopeptides by hydrazide chemistry is becoming a popular protocol for the analysis of N-glycoproteome.
19159218	11	36	theme	noredundant	1909:1919	arg1	glycoproteins					1921:1933	523 noredundant glycoproteins	1905:1933	523 noredundant glycoproteins	1905:1933	A total number of 939 N-glycosites were identified confidently, covering 523 noredundant glycoproteins from human liver tissue, which leads to the establishment of the largest data set of glycoproteome from human liver up to now.
19159218	9	37	dep	in	1592:1593	arg1	silico					1595:1600	silico	1595:1600	silico	1595:1600	Among the 317 additional N-glycosites, 98 (30.9%) could not be identified by trypsin in theory because the corresponding in silico tryptic peptides are either too small or too big to detect in mass spectrometer.
19159218	1	38	theme	stoichiometric	284:297	arg1	modification					299:310	low stoichiometric modification	280:310	low stoichiometric modification of glycoprotein	280:326	The study of protein glycosylation has lagged far behind the progress of current proteomics because of the enormous complexity, wide dynamic range distribution and low stoichiometric modification of glycoprotein.
19159218	2	39	gly	N-glycopeptides	363:377	arg2	N-glycopeptides					363:377	tryptic N-glycopeptides	355:377	tryptic N-glycopeptides	355:377	Solid phase extraction of tryptic N-glycopeptides by hydrazide chemistry is becoming a popular protocol for the analysis of N-glycoproteome.
19159218	0	40	theme	liver	34:38	arg1	tissue					40:45	human liver tissue	28:45	human liver tissue	28:45	Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.
19159218	3	41	theme	shotgun	664:670	arg1	proteomics					672:681	shotgun proteomics	664:681	shotgun proteomics approach, that is, from 800 to 3500 Da	664:720	However, in silico digestion of proteins in human proteome database by trypsin indicates that a significant percentage of tryptic N-glycopeptides is not in the preferred detection mass range of shotgun proteomics approach, that is, from 800 to 3500 Da.
19159218	8	42	theme	622	1359:1361	arg1	N-glycosites					1363:1374	622 N-glycosites	1359:1374	622 N-glycosites	1359:1374	Use of trypsin alone resulted in identification of 622 N-glycosites, while using pepsin and thermolysin resulted in identification of 317 additional N-glycosites.
19159218	2	43	theme	tryptic	355:361	arg1	N-glycopeptides					363:377	tryptic N-glycopeptides	355:377	tryptic N-glycopeptides	355:377	Solid phase extraction of tryptic N-glycopeptides by hydrazide chemistry is becoming a popular protocol for the analysis of N-glycoproteome.
19159218	10	44	theme	digestion	1821:1829	arg1	adoption					1793:1800	the adoption	1789:1800	the adoption of multiple enzyme digestion	1789:1829	This study clearly demonstrated that the coverage of N-glycosites could be significantly increased due to the adoption of multiple enzyme digestion.
19159218	3	45	from	digestion	489:497	arg1	database					529:536	human proteome database	514:536	human proteome database	514:536	However, in silico digestion of proteins in human proteome database by trypsin indicates that a significant percentage of tryptic N-glycopeptides is not in the preferred detection mass range of shotgun proteomics approach, that is, from 800 to 3500 Da.
19159218	5	46	used	used	962:965	arg2	trypsin					950:956	only trypsin	945:956	only trypsin	945:956	Thus many N-glycosites could not be localized if only trypsin was used to digest proteins.
19159218	3	47	dep	in	479:480	arg1	silico					482:487	silico	482:487	silico	482:487	However, in silico digestion of proteins in human proteome database by trypsin indicates that a significant percentage of tryptic N-glycopeptides is not in the preferred detection mass range of shotgun proteomics approach, that is, from 800 to 3500 Da.
19159218	6	48	theme	tissue	1073:1078	arg1	N-glycoproteome					1042:1056	the N-glycoproteome	1038:1056	the N-glycoproteome of human liver tissue by combination of hydrazide chemistry method and multiple enzyme digestion	1038:1153	Herein, we describe a comprehensive way to analyze the N-glycoproteome of human liver tissue by combination of hydrazide chemistry method and multiple enzyme digestion.
19159218	10	49	theme	multiple	1805:1812	arg1	digestion					1821:1829	multiple enzyme digestion	1805:1829	multiple enzyme digestion	1805:1829	This study clearly demonstrated that the coverage of N-glycosites could be significantly increased due to the adoption of multiple enzyme digestion.
19159218	11	50	theme	N-glycosites	1854:1865	arg1	number					1840:1845	A total number	1832:1845	A total number of 939 N-glycosites	1832:1865	A total number of 939 N-glycosites were identified confidently, covering 523 noredundant glycoproteins from human liver tissue, which leads to the establishment of the largest data set of glycoproteome from human liver up to now.
19159218	3	51	dep	proteomics	672:681	arg1	approach					683:690	approach	683:690	approach	683:690	However, in silico digestion of proteins in human proteome database by trypsin indicates that a significant percentage of tryptic N-glycopeptides is not in the preferred detection mass range of shotgun proteomics approach, that is, from 800 to 3500 Da.
19159218	6	52	theme	human	1061:1065	arg1	tissue					1073:1078	human liver tissue	1061:1078	human liver tissue	1061:1078	Herein, we describe a comprehensive way to analyze the N-glycoproteome of human liver tissue by combination of hydrazide chemistry method and multiple enzyme digestion.
19159218	7	53	theme	liver	1176:1180	arg1	tissue					1182:1187	human liver tissue	1170:1187	human liver tissue	1170:1187	The lysate of human liver tissue was digested with three proteases, that is, trypsin, pepsin and thermolysin, with different specificities, separately.
19159218	3	54	theme	proteome	520:527	arg1	database					529:536	human proteome database	514:536	human proteome database	514:536	However, in silico digestion of proteins in human proteome database by trypsin indicates that a significant percentage of tryptic N-glycopeptides is not in the preferred detection mass range of shotgun proteomics approach, that is, from 800 to 3500 Da.
19159218	1	55	theme	wide	244:247	arg1	complexity					232:241	the enormous complexity	219:241	the enormous complexity	219:241	The study of protein glycosylation has lagged far behind the progress of current proteomics because of the enormous complexity, wide dynamic range distribution and low stoichiometric modification of glycoprotein.
19159218	1	55	theme	wide	244:247	arg1	range					257:261	wide dynamic range	244:261	wide dynamic range	244:261	The study of protein glycosylation has lagged far behind the progress of current proteomics because of the enormous complexity, wide dynamic range distribution and low stoichiometric modification of glycoprotein.
19159218	9	56	theme	in	1592:1593	arg1	small					1634:1638	small	1634:1638	small	1634:1638	Among the 317 additional N-glycosites, 98 (30.9%) could not be identified by trypsin in theory because the corresponding in silico tryptic peptides are either too small or too big to detect in mass spectrometer.
19159218	9	56	theme	in	1592:1593	arg1	either					1623:1628	either	1623:1628	either	1623:1628	Among the 317 additional N-glycosites, 98 (30.9%) could not be identified by trypsin in theory because the corresponding in silico tryptic peptides are either too small or too big to detect in mass spectrometer.
19159218	9	56	theme	in	1592:1593	arg1	peptides					1610:1617	the corresponding in silico tryptic peptides	1574:1617	the corresponding in silico tryptic peptides	1574:1617	Among the 317 additional N-glycosites, 98 (30.9%) could not be identified by trypsin in theory because the corresponding in silico tryptic peptides are either too small or too big to detect in mass spectrometer.
19159218	3	57	from	database	529:536	arg1	digestion					489:497	in silico digestion	479:497	in silico digestion of proteins in human proteome database by trypsin	479:547	However, in silico digestion of proteins in human proteome database by trypsin indicates that a significant percentage of tryptic N-glycopeptides is not in the preferred detection mass range of shotgun proteomics approach, that is, from 800 to 3500 Da.
19159218	3	58	theme	tryptic	592:598	arg1	N-glycopeptides					600:614	tryptic N-glycopeptides	592:614	tryptic N-glycopeptides	592:614	However, in silico digestion of proteins in human proteome database by trypsin indicates that a significant percentage of tryptic N-glycopeptides is not in the preferred detection mass range of shotgun proteomics approach, that is, from 800 to 3500 Da.
19159218	9	59	theme	tryptic	1602:1608	arg1	small					1634:1638	small	1634:1638	small	1634:1638	Among the 317 additional N-glycosites, 98 (30.9%) could not be identified by trypsin in theory because the corresponding in silico tryptic peptides are either too small or too big to detect in mass spectrometer.
19159218	9	59	theme	tryptic	1602:1608	arg1	either					1623:1628	either	1623:1628	either	1623:1628	Among the 317 additional N-glycosites, 98 (30.9%) could not be identified by trypsin in theory because the corresponding in silico tryptic peptides are either too small or too big to detect in mass spectrometer.
19159218	9	59	theme	tryptic	1602:1608	arg1	peptides					1610:1617	the corresponding in silico tryptic peptides	1574:1617	the corresponding in silico tryptic peptides	1574:1617	Among the 317 additional N-glycosites, 98 (30.9%) could not be identified by trypsin in theory because the corresponding in silico tryptic peptides are either too small or too big to detect in mass spectrometer.
19159218	11	60	theme	liver	1946:1950	arg1	tissue					1952:1957	human liver tissue	1940:1957	human liver tissue	1940:1957	A total number of 939 N-glycosites were identified confidently, covering 523 noredundant glycoproteins from human liver tissue, which leads to the establishment of the largest data set of glycoproteome from human liver up to now.
19159218	6	61	theme	multiple	1129:1136	arg1	digestion					1145:1153	multiple enzyme digestion	1129:1153	multiple enzyme digestion	1129:1153	Herein, we describe a comprehensive way to analyze the N-glycoproteome of human liver tissue by combination of hydrazide chemistry method and multiple enzyme digestion.
19159218	7	62	theme	tissue	1182:1187	arg1	lysate					1160:1165	The lysate	1156:1165	The lysate of human liver tissue	1156:1187	The lysate of human liver tissue was digested with three proteases, that is, trypsin, pepsin and thermolysin, with different specificities, separately.
19159218	3	63	from	proteins	502:509	arg1	database					529:536	human proteome database	514:536	human proteome database	514:536	However, in silico digestion of proteins in human proteome database by trypsin indicates that a significant percentage of tryptic N-glycopeptides is not in the preferred detection mass range of shotgun proteomics approach, that is, from 800 to 3500 Da.
19159218	2	64	theme	Solid	329:333	arg1	extraction					341:350	Solid phase extraction	329:350	Solid phase extraction of tryptic N-glycopeptides by hydrazide chemistry	329:400	Solid phase extraction of tryptic N-glycopeptides by hydrazide chemistry is becoming a popular protocol for the analysis of N-glycoproteome.
19159218	6	65	theme	method	1118:1123	arg1	digestion					1145:1153	multiple enzyme digestion	1129:1153	multiple enzyme digestion	1129:1153	Herein, we describe a comprehensive way to analyze the N-glycoproteome of human liver tissue by combination of hydrazide chemistry method and multiple enzyme digestion.
19159218	6	65	theme	method	1118:1123	arg1	combination					1083:1093	combination	1083:1093	combination of hydrazide chemistry method	1083:1123	Herein, we describe a comprehensive way to analyze the N-glycoproteome of human liver tissue by combination of hydrazide chemistry method and multiple enzyme digestion.
19159218	1	66	theme	current	189:195	arg1	proteomics					197:206	current proteomics	189:206	current proteomics	189:206	The study of protein glycosylation has lagged far behind the progress of current proteomics because of the enormous complexity, wide dynamic range distribution and low stoichiometric modification of glycoprotein.
19159218	4	67	theme	glycopeptides	881:893	arg1	generation					863:872	generation	863:872	generation of big glycopeptides	863:893	And the quite big size of glycan groups may block trypsin to access the K, R residues near N-glycosites for digestion, which will result in generation of big glycopeptides.
19159218	1	68	dep	complexity	232:241	arg1	distribution					263:274	distribution	263:274	distribution	263:274	The study of protein glycosylation has lagged far behind the progress of current proteomics because of the enormous complexity, wide dynamic range distribution and low stoichiometric modification of glycoprotein.
19159218	6	69	theme	hydrazide	1098:1106	arg1	method					1118:1123	hydrazide chemistry method	1098:1123	hydrazide chemistry method	1098:1123	Herein, we describe a comprehensive way to analyze the N-glycoproteome of human liver tissue by combination of hydrazide chemistry method and multiple enzyme digestion.
19159218	11	70	dep	now	2057:2059	arg1	up					2051:2052	up	2051:2052	up	2051:2052	A total number of 939 N-glycosites were identified confidently, covering 523 noredundant glycoproteins from human liver tissue, which leads to the establishment of the largest data set of glycoproteome from human liver up to now.
19159218	11	71	from	liver	2045:2049	arg1	glycoproteome					2020:2032	glycoproteome	2020:2032	glycoproteome from human liver	2020:2049	A total number of 939 N-glycosites were identified confidently, covering 523 noredundant glycoproteins from human liver tissue, which leads to the establishment of the largest data set of glycoproteome from human liver up to now.
19159218	11	71	from	liver	2045:2049	arg1	set					2013:2015	the largest data set	1996:2015	the largest data set of glycoproteome from human liver	1996:2049	A total number of 939 N-glycosites were identified confidently, covering 523 noredundant glycoproteins from human liver tissue, which leads to the establishment of the largest data set of glycoproteome from human liver up to now.
19159218	4	72	gly	glycopeptides	881:893	arg2	glycopeptides					881:893	big glycopeptides	877:893	big glycopeptides	877:893	And the quite big size of glycan groups may block trypsin to access the K, R residues near N-glycosites for digestion, which will result in generation of big glycopeptides.
19159218	3	73	theme	mass	650:653	arg1	range					655:659	the preferred detection mass range	626:659	the preferred detection mass range of shotgun proteomics approach, that is, from 800 to 3500 Da	626:720	However, in silico digestion of proteins in human proteome database by trypsin indicates that a significant percentage of tryptic N-glycopeptides is not in the preferred detection mass range of shotgun proteomics approach, that is, from 800 to 3500 Da.
19159218	9	74	theme	mass	1664:1667	arg1	spectrometer					1669:1680	mass spectrometer	1664:1680	mass spectrometer	1664:1680	Among the 317 additional N-glycosites, 98 (30.9%) could not be identified by trypsin in theory because the corresponding in silico tryptic peptides are either too small or too big to detect in mass spectrometer.
19159218	0	75	theme	multiple	65:72	arg1	digestion					81:89	multiple enzyme digestion	65:89	multiple enzyme digestion	65:89	Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.
19159218	3	76	theme	preferred	630:638	arg1	range					655:659	the preferred detection mass range	626:659	the preferred detection mass range of shotgun proteomics approach, that is, from 800 to 3500 Da	626:720	However, in silico digestion of proteins in human proteome database by trypsin indicates that a significant percentage of tryptic N-glycopeptides is not in the preferred detection mass range of shotgun proteomics approach, that is, from 800 to 3500 Da.
19159218	1	77	theme	glycosylation	137:149	arg1	study					120:124	The study	116:124	The study of protein glycosylation	116:149	The study of protein glycosylation has lagged far behind the progress of current proteomics because of the enormous complexity, wide dynamic range distribution and low stoichiometric modification of glycoprotein.
19159218	8	78	theme	N-glycosites	1457:1468	arg1	identification					1424:1437	identification	1424:1437	identification of 317 additional N-glycosites	1424:1468	Use of trypsin alone resulted in identification of 622 N-glycosites, while using pepsin and thermolysin resulted in identification of 317 additional N-glycosites.
19159218	0	79	theme	digestion	81:89	arg1	combination					50:60	combination	50:60	combination of multiple enzyme digestion and hydrazide chemistry	50:113	Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.
19159218	9	80	theme	additional	1485:1494	arg1	N-glycosites					1496:1507	the 317 additional N-glycosites	1477:1507	the 317 additional N-glycosites	1477:1507	Among the 317 additional N-glycosites, 98 (30.9%) could not be identified by trypsin in theory because the corresponding in silico tryptic peptides are either too small or too big to detect in mass spectrometer.
19159218	11	81	theme	data	2008:2011	arg1	glycoproteome					2020:2032	glycoproteome	2020:2032	glycoproteome from human liver	2020:2049	A total number of 939 N-glycosites were identified confidently, covering 523 noredundant glycoproteins from human liver tissue, which leads to the establishment of the largest data set of glycoproteome from human liver up to now.
19159218	11	81	theme	data	2008:2011	arg1	set					2013:2015	the largest data set	1996:2015	the largest data set of glycoproteome from human liver	1996:2049	A total number of 939 N-glycosites were identified confidently, covering 523 noredundant glycoproteins from human liver tissue, which leads to the establishment of the largest data set of glycoproteome from human liver up to now.
19159218	11	82	gly	N-glycosites	1854:1865	arg2	N-glycosites					1854:1865	939 N-glycosites	1850:1865	939 N-glycosites	1850:1865	A total number of 939 N-glycosites were identified confidently, covering 523 noredundant glycoproteins from human liver tissue, which leads to the establishment of the largest data set of glycoproteome from human liver up to now.
19159218	0	83	theme	hydrazide	95:103	arg1	chemistry					105:113	hydrazide chemistry	95:113	hydrazide chemistry	95:113	Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.
19159218	5	84	gly	N-glycosites	906:917	arg2	N-glycosites					906:917	many N-glycosites	901:917	many N-glycosites	901:917	Thus many N-glycosites could not be localized if only trypsin was used to digest proteins.
19159218	4	85	theme	glycan	749:754	arg1	groups					756:761	glycan groups	749:761	glycan groups	749:761	And the quite big size of glycan groups may block trypsin to access the K, R residues near N-glycosites for digestion, which will result in generation of big glycopeptides.
19159218	3	86	theme	proteins	502:509	arg1	digestion					489:497	in silico digestion	479:497	in silico digestion of proteins in human proteome database by trypsin	479:547	However, in silico digestion of proteins in human proteome database by trypsin indicates that a significant percentage of tryptic N-glycopeptides is not in the preferred detection mass range of shotgun proteomics approach, that is, from 800 to 3500 Da.
19159218	1	87	theme	proteomics	197:206	arg1	progress					177:184	the progress	173:184	the progress of current proteomics	173:206	The study of protein glycosylation has lagged far behind the progress of current proteomics because of the enormous complexity, wide dynamic range distribution and low stoichiometric modification of glycoprotein.
19159218	5	88	theme	only	945:948	arg1	trypsin					950:956	only trypsin	945:956	only trypsin	945:956	Thus many N-glycosites could not be localized if only trypsin was used to digest proteins.
19159218	7	89	theme	different	1271:1279	arg1	specificities					1281:1293	different specificities	1271:1293	different specificities	1271:1293	The lysate of human liver tissue was digested with three proteases, that is, trypsin, pepsin and thermolysin, with different specificities, separately.
19159218	9	90	gly	N-glycosites	1496:1507	arg2	N-glycosites					1496:1507	the 317 additional N-glycosites	1477:1507	the 317 additional N-glycosites	1477:1507	Among the 317 additional N-glycosites, 98 (30.9%) could not be identified by trypsin in theory because the corresponding in silico tryptic peptides are either too small or too big to detect in mass spectrometer.
19159218	11	91	theme	total	1834:1838	arg1	number					1840:1845	A total number	1832:1845	A total number of 939 N-glycosites	1832:1865	A total number of 939 N-glycosites were identified confidently, covering 523 noredundant glycoproteins from human liver tissue, which leads to the establishment of the largest data set of glycoproteome from human liver up to now.
19159218	0	92	theme	human	28:32	arg1	tissue					40:45	human liver tissue	28:45	human liver tissue	28:45	Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.
19159218	1	93	theme	low	280:282	arg1	modification					299:310	low stoichiometric modification	280:310	low stoichiometric modification of glycoprotein	280:326	The study of protein glycosylation has lagged far behind the progress of current proteomics because of the enormous complexity, wide dynamic range distribution and low stoichiometric modification of glycoprotein.
19159218	6	94	theme	comprehensive	1009:1021	arg1	way					1023:1025	a comprehensive way	1007:1025	a comprehensive way to analyze the N-glycoproteome of human liver tissue by combination of hydrazide chemistry method and multiple enzyme digestion	1007:1153	Herein, we describe a comprehensive way to analyze the N-glycoproteome of human liver tissue by combination of hydrazide chemistry method and multiple enzyme digestion.
19159218	11	95	gly	glycoproteins	1921:1933	arg1	glycoproteins					1921:1933	523 noredundant glycoproteins	1905:1933	523 noredundant glycoproteins	1905:1933	A total number of 939 N-glycosites were identified confidently, covering 523 noredundant glycoproteins from human liver tissue, which leads to the establishment of the largest data set of glycoproteome from human liver up to now.
19159218	3	96	theme	proteomics	672:681	arg1	range					655:659	the preferred detection mass range	626:659	the preferred detection mass range of shotgun proteomics approach, that is, from 800 to 3500 Da	626:720	However, in silico digestion of proteins in human proteome database by trypsin indicates that a significant percentage of tryptic N-glycopeptides is not in the preferred detection mass range of shotgun proteomics approach, that is, from 800 to 3500 Da.
19159218	0	97	theme	tissue	40:45	arg1	analysis					16:23	Glycoproteomics analysis	0:23	Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.	0:114	Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.
19159218	3	98	dep	3500	714:717	arg1	to					711:712	to	711:712	to	711:712	However, in silico digestion of proteins in human proteome database by trypsin indicates that a significant percentage of tryptic N-glycopeptides is not in the preferred detection mass range of shotgun proteomics approach, that is, from 800 to 3500 Da.
19159218	4	99	theme	K	795:795	arg1	residues					800:807	the K, R residues	791:807	the K, R residues near N-glycosites	791:825	And the quite big size of glycan groups may block trypsin to access the K, R residues near N-glycosites for digestion, which will result in generation of big glycopeptides.
19159218	3	100	theme	in	479:480	arg1	digestion					489:497	in silico digestion	479:497	in silico digestion of proteins in human proteome database by trypsin	479:547	However, in silico digestion of proteins in human proteome database by trypsin indicates that a significant percentage of tryptic N-glycopeptides is not in the preferred detection mass range of shotgun proteomics approach, that is, from 800 to 3500 Da.
19159218	1	101	theme	glycoprotein	315:326	arg1	complexity					232:241	the enormous complexity	219:241	the enormous complexity	219:241	The study of protein glycosylation has lagged far behind the progress of current proteomics because of the enormous complexity, wide dynamic range distribution and low stoichiometric modification of glycoprotein.
19159218	1	101	theme	glycoprotein	315:326	arg1	modification					299:310	low stoichiometric modification	280:310	low stoichiometric modification of glycoprotein	280:326	The study of protein glycosylation has lagged far behind the progress of current proteomics because of the enormous complexity, wide dynamic range distribution and low stoichiometric modification of glycoprotein.
19159218	1	101	theme	glycoprotein	315:326	arg1	range					257:261	wide dynamic range	244:261	wide dynamic range	244:261	The study of protein glycosylation has lagged far behind the progress of current proteomics because of the enormous complexity, wide dynamic range distribution and low stoichiometric modification of glycoprotein.
19159218	3	102	theme	human	514:518	arg1	database					529:536	human proteome database	514:536	human proteome database	514:536	However, in silico digestion of proteins in human proteome database by trypsin indicates that a significant percentage of tryptic N-glycopeptides is not in the preferred detection mass range of shotgun proteomics approach, that is, from 800 to 3500 Da.
19159218	11	103	theme	523	1905:1907	arg1	glycoproteins					1921:1933	523 noredundant glycoproteins	1905:1933	523 noredundant glycoproteins	1905:1933	A total number of 939 N-glycosites were identified confidently, covering 523 noredundant glycoproteins from human liver tissue, which leads to the establishment of the largest data set of glycoproteome from human liver up to now.
19159218	10	104	theme	enzyme	1814:1819	arg1	digestion					1821:1829	multiple enzyme digestion	1805:1829	multiple enzyme digestion	1805:1829	This study clearly demonstrated that the coverage of N-glycosites could be significantly increased due to the adoption of multiple enzyme digestion.
19159218	8	105	theme	N-glycosites	1363:1374	arg1	identification					1341:1354	identification	1341:1354	identification of 622 N-glycosites	1341:1374	Use of trypsin alone resulted in identification of 622 N-glycosites, while using pepsin and thermolysin resulted in identification of 317 additional N-glycosites.
19159218	2	106	theme	phase	335:339	arg1	extraction					341:350	Solid phase extraction	329:350	Solid phase extraction of tryptic N-glycopeptides by hydrazide chemistry	329:400	Solid phase extraction of tryptic N-glycopeptides by hydrazide chemistry is becoming a popular protocol for the analysis of N-glycoproteome.
19159218	1	107	theme	enormous	223:230	arg1	complexity					232:241	the enormous complexity	219:241	the enormous complexity	219:241	The study of protein glycosylation has lagged far behind the progress of current proteomics because of the enormous complexity, wide dynamic range distribution and low stoichiometric modification of glycoprotein.
19159218	1	107	theme	enormous	223:230	arg1	range					257:261	wide dynamic range	244:261	wide dynamic range	244:261	The study of protein glycosylation has lagged far behind the progress of current proteomics because of the enormous complexity, wide dynamic range distribution and low stoichiometric modification of glycoprotein.
19159218	6	108	theme	liver	1067:1071	arg1	tissue					1073:1078	human liver tissue	1061:1078	human liver tissue	1061:1078	Herein, we describe a comprehensive way to analyze the N-glycoproteome of human liver tissue by combination of hydrazide chemistry method and multiple enzyme digestion.
19159218	2	109	theme	hydrazide	382:390	arg1	chemistry					392:400	hydrazide chemistry	382:400	hydrazide chemistry	382:400	Solid phase extraction of tryptic N-glycopeptides by hydrazide chemistry is becoming a popular protocol for the analysis of N-glycoproteome.
35348747	0	0	theme	p53	72:74	arg1	Activation					76:85	p53 Activation	72:85	p53 Activation in Prostate Cancer	72:104	VPRBP Functions Downstream of the Androgen Receptor and OGT to Restrict p53 Activation in Prostate Cancer.
35348747	5	1	theme	cancer	758:763	arg1	cells					765:769	prostate cancer cells	749:769	prostate cancer cells	749:769	VPRBP knockdown in prostate cancer cells led to a significant decrease in cell proliferation, p53 stabilization, nucleolar fragmentation, and increased p53 recruitment to the chromatin.
35348747	2	2	theme	Gleason	443:449	arg1	score					451:455	high Gleason score	438:455	high Gleason score	438:455	O-GlcNAc transferase (OGT), the enzyme that catalyzes the covalent addition of UDP-N-acetylglucosamine (UDP-GlcNAc) to serine and threonine residues of proteins, is often highly expressed in prostate cancer with its expression correlated with high Gleason score.
35348747	3	3	theme	Associated	590:599	arg1	Factor					601:606	CUL4 Associated Factor 1	585:608	CUL4 Associated Factor 1 (DCAF1)	585:616	In this study, we have identified an AR and OGT coregulated factor, Vpr (HIV-1) binding protein (VPRBP) also known as DDB1 and CUL4 Associated Factor 1 (DCAF1).
35348747	3	3	theme	Associated	590:599	arg1	DCAF1					611:615	DCAF1	611:615	DCAF1	611:615	In this study, we have identified an AR and OGT coregulated factor, Vpr (HIV-1) binding protein (VPRBP) also known as DDB1 and CUL4 Associated Factor 1 (DCAF1).
35348747	6	4	theme	protein	955:961	arg1	overexpression					963:976	VPRBP protein overexpression	949:976	VPRBP protein overexpression	949:976	In human prostate tumor samples, VPRBP protein overexpression correlated with AR amplification, OGT overexpression, a shorter time to postoperative biochemical progression and poor clinical outcome.
35348747	7	5	theme	clinical	1118:1125	arg1	data					1142:1145	clinical transcriptomic data	1118:1145	clinical transcriptomic data	1118:1145	In clinical transcriptomic data, VPRBP expression was positively correlated with the AR and also with AR activity gene signatures.
35348747	6	6	theme	VPRBP	949:953	arg1	overexpression					963:976	VPRBP protein overexpression	949:976	VPRBP protein overexpression	949:976	In human prostate tumor samples, VPRBP protein overexpression correlated with AR amplification, OGT overexpression, a shorter time to postoperative biochemical progression and poor clinical outcome.
35348747	6	7	theme	clinical	1097:1104	arg1	outcome					1106:1112	poor clinical outcome	1092:1112	poor clinical outcome	1092:1112	In human prostate tumor samples, VPRBP protein overexpression correlated with AR amplification, OGT overexpression, a shorter time to postoperative biochemical progression and poor clinical outcome.
35348747	3	8	theme	OGT	502:504	arg1	protein					546:552	an AR and OGT coregulated factor, Vpr (HIV-1) binding protein	492:552	protein	546:552	In this study, we have identified an AR and OGT coregulated factor, Vpr (HIV-1) binding protein (VPRBP) also known as DDB1 and CUL4 Associated Factor 1 (DCAF1).
35348747	3	9	theme	coregulated	506:516	arg1	protein					546:552	an AR and OGT coregulated factor, Vpr (HIV-1) binding protein	492:552	protein	546:552	In this study, we have identified an AR and OGT coregulated factor, Vpr (HIV-1) binding protein (VPRBP) also known as DDB1 and CUL4 Associated Factor 1 (DCAF1).
35348747	5	10	theme	p53	824:826	arg1	stabilization					828:840	p53 stabilization	824:840	p53 stabilization	824:840	VPRBP knockdown in prostate cancer cells led to a significant decrease in cell proliferation, p53 stabilization, nucleolar fragmentation, and increased p53 recruitment to the chromatin.
35348747	2	11	dep	serine	314:319	arg1	residues					335:342	residues	335:342	residues	335:342	O-GlcNAc transferase (OGT), the enzyme that catalyzes the covalent addition of UDP-N-acetylglucosamine (UDP-GlcNAc) to serine and threonine residues of proteins, is often highly expressed in prostate cancer with its expression correlated with high Gleason score.
35348747	7	12	theme	VPRBP	1148:1152	arg1	expression					1154:1163	VPRBP expression	1148:1163	VPRBP expression	1148:1163	In clinical transcriptomic data, VPRBP expression was positively correlated with the AR and also with AR activity gene signatures.
35348747	8	13	theme	AR	1406:1407	arg1	influence					1389:1397	the influence	1385:1397	the influence of the AR and OGT	1385:1415	IMPLICATIONS In conclusion, we have shown that VPRBP/DCAF1 promotes prostate cancer cell proliferation by restraining p53 activation under the influence of the AR and OGT.
35348747	8	14	dep	AR	1406:1407	arg1	the					1402:1404	the	1402:1404	the	1402:1404	IMPLICATIONS In conclusion, we have shown that VPRBP/DCAF1 promotes prostate cancer cell proliferation by restraining p53 activation under the influence of the AR and OGT.
35348747	6	15	theme	shorter	1034:1040	arg1	time					1042:1045	a shorter time	1032:1045	a shorter time to postoperative biochemical progression	1032:1086	In human prostate tumor samples, VPRBP protein overexpression correlated with AR amplification, OGT overexpression, a shorter time to postoperative biochemical progression and poor clinical outcome.
35348747	5	16	theme	VPRBP	730:734	arg1	knockdown					736:744	VPRBP knockdown	730:744	VPRBP knockdown in prostate cancer cells	730:769	VPRBP knockdown in prostate cancer cells led to a significant decrease in cell proliferation, p53 stabilization, nucleolar fragmentation, and increased p53 recruitment to the chromatin.
35348747	1	17	theme	major	135:139	arg1	receptor					116:123	Androgen receptor	107:123	Androgen receptor (AR)	107:128	Androgen receptor (AR) is a major driver of prostate cancer initiation and progression.
35348747	1	17	theme	major	135:139	arg1	driver					141:146	a major driver	133:146	a major driver of prostate cancer initiation and progression	133:192	Androgen receptor (AR) is a major driver of prostate cancer initiation and progression.
35348747	0	18	theme	Prostate	90:97	arg1	Cancer					99:104	Prostate Cancer	90:104	Prostate Cancer	90:104	VPRBP Functions Downstream of the Androgen Receptor and OGT to Restrict p53 Activation in Prostate Cancer.
35348747	0	19	theme	Androgen	34:41	arg1	Receptor					43:50	the Androgen Receptor	30:50	the Androgen Receptor	30:50	VPRBP Functions Downstream of the Androgen Receptor and OGT to Restrict p53 Activation in Prostate Cancer.
35348747	6	20	theme	tumor	934:938	arg1	samples					940:946	human prostate tumor samples	919:946	human prostate tumor samples	919:946	In human prostate tumor samples, VPRBP protein overexpression correlated with AR amplification, OGT overexpression, a shorter time to postoperative biochemical progression and poor clinical outcome.
35348747	8	21	theme	OGT	1413:1415	arg1	influence					1389:1397	the influence	1385:1397	the influence of the AR and OGT	1385:1415	IMPLICATIONS In conclusion, we have shown that VPRBP/DCAF1 promotes prostate cancer cell proliferation by restraining p53 activation under the influence of the AR and OGT.
35348747	4	22	theme	protein	715:721	arg1	level					723:727	the protein level	711:727	the protein level	711:727	We show that VPRBP is regulated by the AR at the transcript level, and stabilized by OGT at the protein level.
35348747	2	23	theme	UDP-N-acetylglucosamine	274:296	arg1	addition					262:269	the covalent addition	249:269	the covalent addition of UDP-N-acetylglucosamine (UDP-GlcNAc) to serine and threonine residues of proteins	249:354	O-GlcNAc transferase (OGT), the enzyme that catalyzes the covalent addition of UDP-N-acetylglucosamine (UDP-GlcNAc) to serine and threonine residues of proteins, is often highly expressed in prostate cancer with its expression correlated with high Gleason score.
35348747	2	24	theme	proteins	347:354	arg1	addition					262:269	the covalent addition	249:269	the covalent addition of UDP-N-acetylglucosamine (UDP-GlcNAc) to serine and threonine residues of proteins	249:354	O-GlcNAc transferase (OGT), the enzyme that catalyzes the covalent addition of UDP-N-acetylglucosamine (UDP-GlcNAc) to serine and threonine residues of proteins, is often highly expressed in prostate cancer with its expression correlated with high Gleason score.
35348747	3	25	theme	factor	518:523	arg1	protein					546:552	an AR and OGT coregulated factor, Vpr (HIV-1) binding protein	492:552	protein	546:552	In this study, we have identified an AR and OGT coregulated factor, Vpr (HIV-1) binding protein (VPRBP) also known as DDB1 and CUL4 Associated Factor 1 (DCAF1).
35348747	1	26	theme	prostate	151:158	arg1	cancer					160:165	prostate cancer initiation and progression	151:192	cancer	160:165	Androgen receptor (AR) is a major driver of prostate cancer initiation and progression.
35348747	6	27	theme	biochemical	1064:1074	arg1	progression					1076:1086	postoperative biochemical progression	1050:1086	postoperative biochemical progression	1050:1086	In human prostate tumor samples, VPRBP protein overexpression correlated with AR amplification, OGT overexpression, a shorter time to postoperative biochemical progression and poor clinical outcome.
35348747	7	28	theme	activity	1220:1227	arg1	signatures					1234:1243	AR activity gene signatures	1217:1243	AR activity gene signatures	1217:1243	In clinical transcriptomic data, VPRBP expression was positively correlated with the AR and also with AR activity gene signatures.
35348747	5	29	theme	cell	804:807	arg1	proliferation					809:821	cell proliferation	804:821	cell proliferation	804:821	VPRBP knockdown in prostate cancer cells led to a significant decrease in cell proliferation, p53 stabilization, nucleolar fragmentation, and increased p53 recruitment to the chromatin.
35348747	1	30	theme	cancer	160:165	arg1	receptor					116:123	Androgen receptor	107:123	Androgen receptor (AR)	107:128	Androgen receptor (AR) is a major driver of prostate cancer initiation and progression.
35348747	1	30	theme	cancer	160:165	arg1	driver					141:146	a major driver	133:146	a major driver of prostate cancer initiation and progression	133:192	Androgen receptor (AR) is a major driver of prostate cancer initiation and progression.
35348747	2	31	theme	prostate	386:393	arg1	cancer					395:400	prostate cancer	386:400	prostate cancer	386:400	O-GlcNAc transferase (OGT), the enzyme that catalyzes the covalent addition of UDP-N-acetylglucosamine (UDP-GlcNAc) to serine and threonine residues of proteins, is often highly expressed in prostate cancer with its expression correlated with high Gleason score.
35348747	8	32	theme	cell	1330:1333	arg1	proliferation					1335:1347	prostate cancer cell proliferation	1314:1347	prostate cancer cell proliferation	1314:1347	IMPLICATIONS In conclusion, we have shown that VPRBP/DCAF1 promotes prostate cancer cell proliferation by restraining p53 activation under the influence of the AR and OGT.
35348747	2	33	theme	covalent	253:260	arg1	addition					262:269	the covalent addition	249:269	the covalent addition of UDP-N-acetylglucosamine (UDP-GlcNAc) to serine and threonine residues of proteins	249:354	O-GlcNAc transferase (OGT), the enzyme that catalyzes the covalent addition of UDP-N-acetylglucosamine (UDP-GlcNAc) to serine and threonine residues of proteins, is often highly expressed in prostate cancer with its expression correlated with high Gleason score.
35348747	8	34	theme	prostate	1314:1321	arg1	proliferation					1335:1347	prostate cancer cell proliferation	1314:1347	prostate cancer cell proliferation	1314:1347	IMPLICATIONS In conclusion, we have shown that VPRBP/DCAF1 promotes prostate cancer cell proliferation by restraining p53 activation under the influence of the AR and OGT.
35348747	2	35	theme	high	438:441	arg1	score					451:455	high Gleason score	438:455	high Gleason score	438:455	O-GlcNAc transferase (OGT), the enzyme that catalyzes the covalent addition of UDP-N-acetylglucosamine (UDP-GlcNAc) to serine and threonine residues of proteins, is often highly expressed in prostate cancer with its expression correlated with high Gleason score.
35348747	6	36	theme	AR	994:995	arg1	amplification					997:1009	AR amplification	994:1009	AR amplification	994:1009	In human prostate tumor samples, VPRBP protein overexpression correlated with AR amplification, OGT overexpression, a shorter time to postoperative biochemical progression and poor clinical outcome.
35348747	8	37	theme	cancer	1323:1328	arg1	proliferation					1335:1347	prostate cancer cell proliferation	1314:1347	prostate cancer cell proliferation	1314:1347	IMPLICATIONS In conclusion, we have shown that VPRBP/DCAF1 promotes prostate cancer cell proliferation by restraining p53 activation under the influence of the AR and OGT.
35348747	5	38	theme	increased	872:880	arg1	recruitment					886:896	increased p53 recruitment	872:896	increased p53 recruitment to the chromatin	872:913	VPRBP knockdown in prostate cancer cells led to a significant decrease in cell proliferation, p53 stabilization, nucleolar fragmentation, and increased p53 recruitment to the chromatin.
35348747	6	39	theme	postoperative	1050:1062	arg1	progression					1076:1086	postoperative biochemical progression	1050:1086	postoperative biochemical progression	1050:1086	In human prostate tumor samples, VPRBP protein overexpression correlated with AR amplification, OGT overexpression, a shorter time to postoperative biochemical progression and poor clinical outcome.
35348747	3	40	dep	protein	546:552	arg1	Vpr					526:528	an AR and OGT coregulated factor, Vpr (HIV-1) binding protein	492:552	Vpr	526:528	In this study, we have identified an AR and OGT coregulated factor, Vpr (HIV-1) binding protein (VPRBP) also known as DDB1 and CUL4 Associated Factor 1 (DCAF1).
35348747	6	41	theme	prostate	925:932	arg1	samples					940:946	human prostate tumor samples	919:946	human prostate tumor samples	919:946	In human prostate tumor samples, VPRBP protein overexpression correlated with AR amplification, OGT overexpression, a shorter time to postoperative biochemical progression and poor clinical outcome.
35348747	3	42	theme	HIV-1	531:535	arg1	protein					546:552	an AR and OGT coregulated factor, Vpr (HIV-1) binding protein	492:552	protein	546:552	In this study, we have identified an AR and OGT coregulated factor, Vpr (HIV-1) binding protein (VPRBP) also known as DDB1 and CUL4 Associated Factor 1 (DCAF1).
35348747	1	43	theme	progression	182:192	arg1	receptor					116:123	Androgen receptor	107:123	Androgen receptor (AR)	107:128	Androgen receptor (AR) is a major driver of prostate cancer initiation and progression.
35348747	1	43	theme	progression	182:192	arg1	driver					141:146	a major driver	133:146	a major driver of prostate cancer initiation and progression	133:192	Androgen receptor (AR) is a major driver of prostate cancer initiation and progression.
35348747	7	44	theme	AR	1217:1218	arg1	signatures					1234:1243	AR activity gene signatures	1217:1243	AR activity gene signatures	1217:1243	In clinical transcriptomic data, VPRBP expression was positively correlated with the AR and also with AR activity gene signatures.
35348747	2	45	theme	O-GlcNAc	195:202	arg1	transferase					204:214	O-GlcNAc transferase	195:214	O-GlcNAc transferase (OGT)	195:220	O-GlcNAc transferase (OGT), the enzyme that catalyzes the covalent addition of UDP-N-acetylglucosamine (UDP-GlcNAc) to serine and threonine residues of proteins, is often highly expressed in prostate cancer with its expression correlated with high Gleason score.
35348747	2	45	theme	O-GlcNAc	195:202	arg1	enzyme					227:232	the enzyme	223:232	the enzyme that catalyzes the covalent addition of UDP-N-acetylglucosamine (UDP-GlcNAc) to serine and threonine residues of proteins	223:354	O-GlcNAc transferase (OGT), the enzyme that catalyzes the covalent addition of UDP-N-acetylglucosamine (UDP-GlcNAc) to serine and threonine residues of proteins, is often highly expressed in prostate cancer with its expression correlated with high Gleason score.
35348747	2	45	theme	O-GlcNAc	195:202	arg1	OGT					217:219	OGT	217:219	OGT	217:219	O-GlcNAc transferase (OGT), the enzyme that catalyzes the covalent addition of UDP-N-acetylglucosamine (UDP-GlcNAc) to serine and threonine residues of proteins, is often highly expressed in prostate cancer with its expression correlated with high Gleason score.
35348747	0	46	theme	Receptor	43:50	arg1	Downstream					16:25	Downstream	16:25	Downstream	16:25	VPRBP Functions Downstream of the Androgen Receptor and OGT to Restrict p53 Activation in Prostate Cancer.
35348747	8	47	theme	p53	1364:1366	arg1	activation					1368:1377	p53 activation	1364:1377	p53 activation	1364:1377	IMPLICATIONS In conclusion, we have shown that VPRBP/DCAF1 promotes prostate cancer cell proliferation by restraining p53 activation under the influence of the AR and OGT.
35348747	6	48	theme	poor	1092:1095	arg1	outcome					1106:1112	poor clinical outcome	1092:1112	poor clinical outcome	1092:1112	In human prostate tumor samples, VPRBP protein overexpression correlated with AR amplification, OGT overexpression, a shorter time to postoperative biochemical progression and poor clinical outcome.
35348747	1	49	theme	Androgen	107:114	arg1	receptor					116:123	Androgen receptor	107:123	Androgen receptor (AR)	107:128	Androgen receptor (AR) is a major driver of prostate cancer initiation and progression.
35348747	1	49	theme	Androgen	107:114	arg1	driver					141:146	a major driver	133:146	a major driver of prostate cancer initiation and progression	133:192	Androgen receptor (AR) is a major driver of prostate cancer initiation and progression.
35348747	1	49	theme	Androgen	107:114	arg1	AR					126:127	AR	126:127	AR	126:127	Androgen receptor (AR) is a major driver of prostate cancer initiation and progression.
35348747	4	50	theme	transcript	668:677	arg1	level					679:683	the transcript level	664:683	the transcript level	664:683	We show that VPRBP is regulated by the AR at the transcript level, and stabilized by OGT at the protein level.
35348747	3	51	theme	CUL4	585:588	arg1	Factor					601:606	CUL4 Associated Factor 1	585:608	CUL4 Associated Factor 1 (DCAF1)	585:616	In this study, we have identified an AR and OGT coregulated factor, Vpr (HIV-1) binding protein (VPRBP) also known as DDB1 and CUL4 Associated Factor 1 (DCAF1).
35348747	3	51	theme	CUL4	585:588	arg1	DCAF1					611:615	DCAF1	611:615	DCAF1	611:615	In this study, we have identified an AR and OGT coregulated factor, Vpr (HIV-1) binding protein (VPRBP) also known as DDB1 and CUL4 Associated Factor 1 (DCAF1).
35348747	5	52	theme	nucleolar	843:851	arg1	fragmentation					853:865	nucleolar fragmentation	843:865	nucleolar fragmentation	843:865	VPRBP knockdown in prostate cancer cells led to a significant decrease in cell proliferation, p53 stabilization, nucleolar fragmentation, and increased p53 recruitment to the chromatin.
35348747	5	53	theme	p53	882:884	arg1	recruitment					886:896	increased p53 recruitment	872:896	increased p53 recruitment to the chromatin	872:913	VPRBP knockdown in prostate cancer cells led to a significant decrease in cell proliferation, p53 stabilization, nucleolar fragmentation, and increased p53 recruitment to the chromatin.
35348747	6	54	theme	OGT	1012:1014	arg1	overexpression					1016:1029	OGT overexpression	1012:1029	OGT overexpression	1012:1029	In human prostate tumor samples, VPRBP protein overexpression correlated with AR amplification, OGT overexpression, a shorter time to postoperative biochemical progression and poor clinical outcome.
35348747	6	55	theme	human	919:923	arg1	samples					940:946	human prostate tumor samples	919:946	human prostate tumor samples	919:946	In human prostate tumor samples, VPRBP protein overexpression correlated with AR amplification, OGT overexpression, a shorter time to postoperative biochemical progression and poor clinical outcome.
35348747	5	56	theme	significant	780:790	arg1	decrease					792:799	a significant decrease	778:799	a significant decrease in cell proliferation, p53 stabilization, nucleolar fragmentation, and increased p53 recruitment to the chromatin	778:913	VPRBP knockdown in prostate cancer cells led to a significant decrease in cell proliferation, p53 stabilization, nucleolar fragmentation, and increased p53 recruitment to the chromatin.
35348747	5	57	from	decrease	792:799	arg1	recruitment					886:896	increased p53 recruitment	872:896	increased p53 recruitment to the chromatin	872:913	VPRBP knockdown in prostate cancer cells led to a significant decrease in cell proliferation, p53 stabilization, nucleolar fragmentation, and increased p53 recruitment to the chromatin.
35348747	5	57	from	decrease	792:799	arg1	proliferation					809:821	cell proliferation	804:821	cell proliferation	804:821	VPRBP knockdown in prostate cancer cells led to a significant decrease in cell proliferation, p53 stabilization, nucleolar fragmentation, and increased p53 recruitment to the chromatin.
35348747	5	57	from	decrease	792:799	arg1	stabilization					828:840	p53 stabilization	824:840	p53 stabilization	824:840	VPRBP knockdown in prostate cancer cells led to a significant decrease in cell proliferation, p53 stabilization, nucleolar fragmentation, and increased p53 recruitment to the chromatin.
35348747	5	57	from	decrease	792:799	arg1	fragmentation					853:865	nucleolar fragmentation	843:865	nucleolar fragmentation	843:865	VPRBP knockdown in prostate cancer cells led to a significant decrease in cell proliferation, p53 stabilization, nucleolar fragmentation, and increased p53 recruitment to the chromatin.
35348747	0	58	from	Activation	76:85	arg1	Cancer					99:104	Prostate Cancer	90:104	Prostate Cancer	90:104	VPRBP Functions Downstream of the Androgen Receptor and OGT to Restrict p53 Activation in Prostate Cancer.
35348747	1	59	dep	cancer	160:165	arg1	initiation					167:176	initiation	167:176	initiation	167:176	Androgen receptor (AR) is a major driver of prostate cancer initiation and progression.
35348747	5	60	from	knockdown	736:744	arg1	cells					765:769	prostate cancer cells	749:769	prostate cancer cells	749:769	VPRBP knockdown in prostate cancer cells led to a significant decrease in cell proliferation, p53 stabilization, nucleolar fragmentation, and increased p53 recruitment to the chromatin.
35348747	7	61	theme	transcriptomic	1127:1140	arg1	data					1142:1145	clinical transcriptomic data	1118:1145	clinical transcriptomic data	1118:1145	In clinical transcriptomic data, VPRBP expression was positively correlated with the AR and also with AR activity gene signatures.
35348747	0	62	theme	OGT	56:58	arg1	Downstream					16:25	Downstream	16:25	Downstream	16:25	VPRBP Functions Downstream of the Androgen Receptor and OGT to Restrict p53 Activation in Prostate Cancer.
35348747	7	63	theme	gene	1229:1232	arg1	signatures					1234:1243	AR activity gene signatures	1217:1243	AR activity gene signatures	1217:1243	In clinical transcriptomic data, VPRBP expression was positively correlated with the AR and also with AR activity gene signatures.
35348747	3	64	theme	binding	538:544	arg1	protein					546:552	an AR and OGT coregulated factor, Vpr (HIV-1) binding protein	492:552	protein	546:552	In this study, we have identified an AR and OGT coregulated factor, Vpr (HIV-1) binding protein (VPRBP) also known as DDB1 and CUL4 Associated Factor 1 (DCAF1).
35348747	5	65	theme	prostate	749:756	arg1	cells					765:769	prostate cancer cells	749:769	prostate cancer cells	749:769	VPRBP knockdown in prostate cancer cells led to a significant decrease in cell proliferation, p53 stabilization, nucleolar fragmentation, and increased p53 recruitment to the chromatin.
35348747	8	66	dep	IMPLICATIONS	1246:1257	arg1	shown					1282:1286	shown	1282:1286	have shown that VPRBP/DCAF1 promotes prostate cancer cell proliferation by restraining p53 activation under the influence of the AR and OGT	1277:1415	IMPLICATIONS In conclusion, we have shown that VPRBP/DCAF1 promotes prostate cancer cell proliferation by restraining p53 activation under the influence of the AR and OGT.
36765030	5	0	theme	transferase	603:613	arg1	O-GlcNAcylation					630:644	O-GlcNAc transferase (OGT)-mediated O-GlcNAcylation	594:644	O-GlcNAc transferase (OGT)-mediated O-GlcNAcylation of YTHDF2 on serine 263	594:668	O-GlcNAc transferase (OGT)-mediated O-GlcNAcylation of YTHDF2 on serine 263 enhanced its protein stability and oncogenic activity by inhibiting its ubiquitination.
36765030	8	1	theme	new	1110:1112	arg1	mechanism					1125:1133	a new regulatory mechanism	1108:1133	a new regulatory mechanism for YTHDF2	1108:1144	Taken together, our findings reveal a new regulatory mechanism for YTHDF2 and highlight an essential role of YTHDF2 O-GlcNAcylation in RNA m6A methylation and HCC progression.
36765030	1	2	theme	major	166:170	arg1	factor					177:182	a major risk factor	164:182	a major risk factor for hepatocellular carcinoma (HCC)	164:217	Hepatitis B virus (HBV) infection is a major risk factor for hepatocellular carcinoma (HCC), but its pathogenic mechanism remains to be explored.
36765030	1	2	theme	major	166:170	arg1	infection					151:159	Hepatitis B virus (HBV) infection	127:159	Hepatitis B virus (HBV) infection	127:159	Hepatitis B virus (HBV) infection is a major risk factor for hepatocellular carcinoma (HCC), but its pathogenic mechanism remains to be explored.
36765030	0	3	theme	N6-methyladenosine-dependent	90:117	arg1	manner					119:124	an N6-methyladenosine-dependent manner	87:124	an N6-methyladenosine-dependent manner	87:124	O-GlcNAcylation of YTHDF2 promotes HBV-related hepatocellular carcinoma progression in an N6-methyladenosine-dependent manner.
36765030	6	4	theme	minichromosome	793:806	arg1	protein					820:826	minichromosome maintenance protein 2	793:828	minichromosome maintenance protein 2 (MCM2)	793:835	Mechanistically, YTHDF2 stabilized minichromosome maintenance protein 2 (MCM2) and MCM5 transcripts in an m6A-dependent manner, thus promoting cell cycle progression and HBV-related HCC tumorigenesis.
36765030	6	4	theme	minichromosome	793:806	arg1	MCM2					831:834	MCM2	831:834	MCM2	831:834	Mechanistically, YTHDF2 stabilized minichromosome maintenance protein 2 (MCM2) and MCM5 transcripts in an m6A-dependent manner, thus promoting cell cycle progression and HBV-related HCC tumorigenesis.
36765030	3	5	theme	YTHDF2	453:458	arg1	function					415:422	function	415:422	function	415:422	However, the function and regulatory mechanisms of YTHDF2 in HBV-related HCC remain largely elusive.
36765030	3	5	theme	YTHDF2	453:458	arg1	mechanisms					439:448	regulatory mechanisms	428:448	regulatory mechanisms	428:448	However, the function and regulatory mechanisms of YTHDF2 in HBV-related HCC remain largely elusive.
36765030	2	6	theme	homology	327:334	arg1	domain					337:342	YTH (YT521-B homology) domain 2	314:344	YTH (YT521-B homology) domain 2 (YTHDF2)	314:353	The RNA N6-methyladenosine (m6A) reader, YTH (YT521-B homology) domain 2 (YTHDF2), plays a critical role in the HCC progression.
36765030	2	6	theme	homology	327:334	arg1	YTHDF2					347:352	YTHDF2	347:352	YTHDF2	347:352	The RNA N6-methyladenosine (m6A) reader, YTH (YT521-B homology) domain 2 (YTHDF2), plays a critical role in the HCC progression.
36765030	2	6	theme	homology	327:334	arg1	reader					306:311	The RNA N6-methyladenosine (m6A) reader	273:311	The RNA N6-methyladenosine (m6A) reader	273:311	The RNA N6-methyladenosine (m6A) reader, YTH (YT521-B homology) domain 2 (YTHDF2), plays a critical role in the HCC progression.
36765030	2	7	theme	N6-methyladenosine	281:298	arg1	domain					337:342	YTH (YT521-B homology) domain 2	314:344	YTH (YT521-B homology) domain 2 (YTHDF2)	314:353	The RNA N6-methyladenosine (m6A) reader, YTH (YT521-B homology) domain 2 (YTHDF2), plays a critical role in the HCC progression.
36765030	2	7	theme	N6-methyladenosine	281:298	arg1	reader					306:311	The RNA N6-methyladenosine (m6A) reader	273:311	The RNA N6-methyladenosine (m6A) reader	273:311	The RNA N6-methyladenosine (m6A) reader, YTH (YT521-B homology) domain 2 (YTHDF2), plays a critical role in the HCC progression.
36765030	1	8	theme	risk	172:175	arg1	factor					177:182	a major risk factor	164:182	a major risk factor for hepatocellular carcinoma (HCC)	164:217	Hepatitis B virus (HBV) infection is a major risk factor for hepatocellular carcinoma (HCC), but its pathogenic mechanism remains to be explored.
36765030	1	8	theme	risk	172:175	arg1	infection					151:159	Hepatitis B virus (HBV) infection	127:159	Hepatitis B virus (HBV) infection	127:159	Hepatitis B virus (HBV) infection is a major risk factor for hepatocellular carcinoma (HCC), but its pathogenic mechanism remains to be explored.
36765030	5	9	theme	protein	683:689	arg1	stability					691:699	its protein stability	679:699	its protein stability	679:699	O-GlcNAc transferase (OGT)-mediated O-GlcNAcylation of YTHDF2 on serine 263 enhanced its protein stability and oncogenic activity by inhibiting its ubiquitination.
36765030	6	10	theme	m6A-dependent	864:876	arg1	manner					878:883	an m6A-dependent manner	861:883	an m6A-dependent manner	861:883	Mechanistically, YTHDF2 stabilized minichromosome maintenance protein 2 (MCM2) and MCM5 transcripts in an m6A-dependent manner, thus promoting cell cycle progression and HBV-related HCC tumorigenesis.
36765030	2	11	theme	RNA	277:279	arg1	domain					337:342	YTH (YT521-B homology) domain 2	314:344	YTH (YT521-B homology) domain 2 (YTHDF2)	314:353	The RNA N6-methyladenosine (m6A) reader, YTH (YT521-B homology) domain 2 (YTHDF2), plays a critical role in the HCC progression.
36765030	2	11	theme	RNA	277:279	arg1	reader					306:311	The RNA N6-methyladenosine (m6A) reader	273:311	The RNA N6-methyladenosine (m6A) reader	273:311	The RNA N6-methyladenosine (m6A) reader, YTH (YT521-B homology) domain 2 (YTHDF2), plays a critical role in the HCC progression.
36765030	4	12	theme	YTHDF2	528:533	arg1	O-GlcNAcylation					535:549	YTHDF2 O-GlcNAcylation	528:549	YTHDF2 O-GlcNAcylation	528:549	Here, we discovered that YTHDF2 O-GlcNAcylation was markedly increased upon HBV infection.
36765030	3	13	theme	regulatory	428:437	arg1	mechanisms					439:448	regulatory mechanisms	428:448	regulatory mechanisms	428:448	However, the function and regulatory mechanisms of YTHDF2 in HBV-related HCC remain largely elusive.
36765030	4	14	theme	HBV	579:581	arg1	infection					583:591	HBV infection	579:591	HBV infection	579:591	Here, we discovered that YTHDF2 O-GlcNAcylation was markedly increased upon HBV infection.
36765030	8	15	theme	essential	1163:1171	arg1	role					1173:1176	an essential role	1160:1176	an essential role of YTHDF2 O-GlcNAcylation in RNA m6A methylation and HCC progression	1160:1245	Taken together, our findings reveal a new regulatory mechanism for YTHDF2 and highlight an essential role of YTHDF2 O-GlcNAcylation in RNA m6A methylation and HCC progression.
36765030	9	16	theme	therapeutic	1320:1330	arg1	targets					1332:1338	therapeutic targets	1320:1338	therapeutic targets for suppression of HCC progression due to HBV infection	1320:1394	Further description of the molecular pathway has the potential to yield therapeutic targets for suppression of HCC progression due to HBV infection.
36765030	8	17	theme	m6A	1211:1213	arg1	methylation					1215:1225	RNA m6A methylation	1207:1225	RNA m6A methylation	1207:1225	Taken together, our findings reveal a new regulatory mechanism for YTHDF2 and highlight an essential role of YTHDF2 O-GlcNAcylation in RNA m6A methylation and HCC progression.
36765030	3	18	from	function	415:422	arg1	HCC					475:477	HBV-related HCC	463:477	HBV-related HCC	463:477	However, the function and regulatory mechanisms of YTHDF2 in HBV-related HCC remain largely elusive.
36765030	9	19	contain	has	1293:1295	arg2	potential					1301:1309	the potential to yield therapeutic targets for suppression of HCC progression due to HBV infection	1297:1394	the potential to yield therapeutic targets for suppression of HCC progression due to HBV infection	1297:1394	Further description of the molecular pathway has the potential to yield therapeutic targets for suppression of HCC progression due to HBV infection.
36765030	9	19	contain	has	1293:1295	arg1	description					1256:1266	Further description	1248:1266	Further description of the molecular pathway	1248:1291	Further description of the molecular pathway has the potential to yield therapeutic targets for suppression of HCC progression due to HBV infection.
36765030	8	20	theme	HCC	1231:1233	arg1	progression					1235:1245	HCC progression	1231:1245	HCC progression	1231:1245	Taken together, our findings reveal a new regulatory mechanism for YTHDF2 and highlight an essential role of YTHDF2 O-GlcNAcylation in RNA m6A methylation and HCC progression.
36765030	8	21	theme	YTHDF2	1181:1186	arg1	O-GlcNAcylation					1188:1202	YTHDF2 O-GlcNAcylation	1181:1202	YTHDF2 O-GlcNAcylation	1181:1202	Taken together, our findings reveal a new regulatory mechanism for YTHDF2 and highlight an essential role of YTHDF2 O-GlcNAcylation in RNA m6A methylation and HCC progression.
36765030	9	22	theme	HCC	1359:1361	arg1	progression					1363:1373	HCC progression	1359:1373	HCC progression	1359:1373	Further description of the molecular pathway has the potential to yield therapeutic targets for suppression of HCC progression due to HBV infection.
36765030	1	23	theme	hepatocellular	188:201	arg1	HCC					214:216	HCC	214:216	HCC	214:216	Hepatitis B virus (HBV) infection is a major risk factor for hepatocellular carcinoma (HCC), but its pathogenic mechanism remains to be explored.
36765030	1	23	theme	hepatocellular	188:201	arg1	carcinoma					203:211	hepatocellular carcinoma	188:211	hepatocellular carcinoma (HCC)	188:217	Hepatitis B virus (HBV) infection is a major risk factor for hepatocellular carcinoma (HCC), but its pathogenic mechanism remains to be explored.
36765030	2	24	theme	HCC	385:387	arg1	progression					389:399	the HCC progression	381:399	the HCC progression	381:399	The RNA N6-methyladenosine (m6A) reader, YTH (YT521-B homology) domain 2 (YTHDF2), plays a critical role in the HCC progression.
36765030	5	25	theme	O-GlcNAc	594:601	arg1	OGT					616:618	OGT	616:618	OGT	616:618	O-GlcNAc transferase (OGT)-mediated O-GlcNAcylation of YTHDF2 on serine 263 enhanced its protein stability and oncogenic activity by inhibiting its ubiquitination.
36765030	5	25	theme	O-GlcNAc	594:601	arg1	transferase					603:613	O-GlcNAc transferase	594:613	O-GlcNAc transferase (OGT)-mediated O-GlcNAcylation of YTHDF2 on serine 263	594:668	O-GlcNAc transferase (OGT)-mediated O-GlcNAcylation of YTHDF2 on serine 263 enhanced its protein stability and oncogenic activity by inhibiting its ubiquitination.
36765030	1	26	theme	Hepatitis	127:135	arg1	HBV					146:148	HBV	146:148	HBV	146:148	Hepatitis B virus (HBV) infection is a major risk factor for hepatocellular carcinoma (HCC), but its pathogenic mechanism remains to be explored.
36765030	1	26	theme	Hepatitis	127:135	arg1	virus					139:143	Hepatitis B virus	127:143	Hepatitis B virus (HBV) infection	127:159	Hepatitis B virus (HBV) infection is a major risk factor for hepatocellular carcinoma (HCC), but its pathogenic mechanism remains to be explored.
36765030	3	27	from	mechanisms	439:448	arg1	HCC					475:477	HBV-related HCC	463:477	HBV-related HCC	463:477	However, the function and regulatory mechanisms of YTHDF2 in HBV-related HCC remain largely elusive.
36765030	2	28	theme	m6A	301:303	arg1	domain					337:342	YTH (YT521-B homology) domain 2	314:344	YTH (YT521-B homology) domain 2 (YTHDF2)	314:353	The RNA N6-methyladenosine (m6A) reader, YTH (YT521-B homology) domain 2 (YTHDF2), plays a critical role in the HCC progression.
36765030	2	28	theme	m6A	301:303	arg1	reader					306:311	The RNA N6-methyladenosine (m6A) reader	273:311	The RNA N6-methyladenosine (m6A) reader	273:311	The RNA N6-methyladenosine (m6A) reader, YTH (YT521-B homology) domain 2 (YTHDF2), plays a critical role in the HCC progression.
36765030	0	29	theme	YTHDF2	19:24	arg1	O-GlcNAcylation					0:14	O-GlcNAcylation	0:14	O-GlcNAcylation of YTHDF2	0:24	O-GlcNAcylation of YTHDF2 promotes HBV-related hepatocellular carcinoma progression in an N6-methyladenosine-dependent manner.
36765030	6	30	theme	HCC	940:942	arg1	tumorigenesis					944:956	HBV-related HCC tumorigenesis	928:956	HBV-related HCC tumorigenesis	928:956	Mechanistically, YTHDF2 stabilized minichromosome maintenance protein 2 (MCM2) and MCM5 transcripts in an m6A-dependent manner, thus promoting cell cycle progression and HBV-related HCC tumorigenesis.
36765030	6	31	theme	MCM5	841:844	arg1	transcripts					846:856	MCM5 transcripts	841:856	MCM5 transcripts	841:856	Mechanistically, YTHDF2 stabilized minichromosome maintenance protein 2 (MCM2) and MCM5 transcripts in an m6A-dependent manner, thus promoting cell cycle progression and HBV-related HCC tumorigenesis.
36765030	1	32	theme	virus	139:143	arg1	factor					177:182	a major risk factor	164:182	a major risk factor for hepatocellular carcinoma (HCC)	164:217	Hepatitis B virus (HBV) infection is a major risk factor for hepatocellular carcinoma (HCC), but its pathogenic mechanism remains to be explored.
36765030	1	32	theme	virus	139:143	arg1	infection					151:159	Hepatitis B virus (HBV) infection	127:159	Hepatitis B virus (HBV) infection	127:159	Hepatitis B virus (HBV) infection is a major risk factor for hepatocellular carcinoma (HCC), but its pathogenic mechanism remains to be explored.
36765030	2	33	theme	critical	364:371	arg1	role					373:376	a critical role	362:376	a critical role	362:376	The RNA N6-methyladenosine (m6A) reader, YTH (YT521-B homology) domain 2 (YTHDF2), plays a critical role in the HCC progression.
36765030	0	34	theme	hepatocellular	47:60	arg1	progression					72:82	HBV-related hepatocellular carcinoma progression	35:82	HBV-related hepatocellular carcinoma progression	35:82	O-GlcNAcylation of YTHDF2 promotes HBV-related hepatocellular carcinoma progression in an N6-methyladenosine-dependent manner.
36765030	6	35	theme	HBV-related	928:938	arg1	tumorigenesis					944:956	HBV-related HCC tumorigenesis	928:956	HBV-related HCC tumorigenesis	928:956	Mechanistically, YTHDF2 stabilized minichromosome maintenance protein 2 (MCM2) and MCM5 transcripts in an m6A-dependent manner, thus promoting cell cycle progression and HBV-related HCC tumorigenesis.
36765030	7	36	theme	HCC	1055:1057	arg1	progression					1059:1069	HCC progression	1055:1069	HCC progression	1055:1069	Moreover, targeting YTHDF2 O-GlcNAcylation by the OGT inhibitor OSMI-1 significantly suppressed HCC progression.
36765030	0	37	theme	HBV-related	35:45	arg1	progression					72:82	HBV-related hepatocellular carcinoma progression	35:82	HBV-related hepatocellular carcinoma progression	35:82	O-GlcNAcylation of YTHDF2 promotes HBV-related hepatocellular carcinoma progression in an N6-methyladenosine-dependent manner.
36765030	9	38	theme	progression	1363:1373	arg1	suppression					1344:1354	suppression	1344:1354	suppression of HCC progression due to HBV infection	1344:1394	Further description of the molecular pathway has the potential to yield therapeutic targets for suppression of HCC progression due to HBV infection.
36765030	8	39	theme	RNA	1207:1209	arg1	methylation					1215:1225	RNA m6A methylation	1207:1225	RNA m6A methylation	1207:1225	Taken together, our findings reveal a new regulatory mechanism for YTHDF2 and highlight an essential role of YTHDF2 O-GlcNAcylation in RNA m6A methylation and HCC progression.
36765030	9	40	theme	HBV	1382:1384	arg1	infection					1386:1394	HBV infection	1382:1394	HBV infection	1382:1394	Further description of the molecular pathway has the potential to yield therapeutic targets for suppression of HCC progression due to HBV infection.
36765030	9	41	theme	molecular	1275:1283	arg1	pathway					1285:1291	the molecular pathway	1271:1291	the molecular pathway	1271:1291	Further description of the molecular pathway has the potential to yield therapeutic targets for suppression of HCC progression due to HBV infection.
36765030	5	42	theme	-mediated	620:628	arg1	O-GlcNAcylation					630:644	O-GlcNAc transferase (OGT)-mediated O-GlcNAcylation	594:644	O-GlcNAc transferase (OGT)-mediated O-GlcNAcylation of YTHDF2 on serine 263	594:668	O-GlcNAc transferase (OGT)-mediated O-GlcNAcylation of YTHDF2 on serine 263 enhanced its protein stability and oncogenic activity by inhibiting its ubiquitination.
36765030	9	43	theme	Further	1248:1254	arg1	description					1256:1266	Further description	1248:1266	Further description of the molecular pathway	1248:1291	Further description of the molecular pathway has the potential to yield therapeutic targets for suppression of HCC progression due to HBV infection.
36765030	7	44	theme	OGT	1009:1011	arg1	OSMI-1					1023:1028	the OGT inhibitor OSMI-1	1005:1028	the OGT inhibitor OSMI-1	1005:1028	Moreover, targeting YTHDF2 O-GlcNAcylation by the OGT inhibitor OSMI-1 significantly suppressed HCC progression.
36765030	2	45	theme	YT521-B	319:325	arg1	domain					337:342	YTH (YT521-B homology) domain 2	314:344	YTH (YT521-B homology) domain 2 (YTHDF2)	314:353	The RNA N6-methyladenosine (m6A) reader, YTH (YT521-B homology) domain 2 (YTHDF2), plays a critical role in the HCC progression.
36765030	2	45	theme	YT521-B	319:325	arg1	YTHDF2					347:352	YTHDF2	347:352	YTHDF2	347:352	The RNA N6-methyladenosine (m6A) reader, YTH (YT521-B homology) domain 2 (YTHDF2), plays a critical role in the HCC progression.
36765030	2	45	theme	YT521-B	319:325	arg1	reader					306:311	The RNA N6-methyladenosine (m6A) reader	273:311	The RNA N6-methyladenosine (m6A) reader	273:311	The RNA N6-methyladenosine (m6A) reader, YTH (YT521-B homology) domain 2 (YTHDF2), plays a critical role in the HCC progression.
36765030	0	46	theme	carcinoma	62:70	arg1	progression					72:82	HBV-related hepatocellular carcinoma progression	35:82	HBV-related hepatocellular carcinoma progression	35:82	O-GlcNAcylation of YTHDF2 promotes HBV-related hepatocellular carcinoma progression in an N6-methyladenosine-dependent manner.
36765030	6	47	theme	cycle	906:910	arg1	progression					912:922	cell cycle progression	901:922	cell cycle progression	901:922	Mechanistically, YTHDF2 stabilized minichromosome maintenance protein 2 (MCM2) and MCM5 transcripts in an m6A-dependent manner, thus promoting cell cycle progression and HBV-related HCC tumorigenesis.
36765030	8	48	from	role	1173:1176	arg1	methylation					1215:1225	RNA m6A methylation	1207:1225	RNA m6A methylation	1207:1225	Taken together, our findings reveal a new regulatory mechanism for YTHDF2 and highlight an essential role of YTHDF2 O-GlcNAcylation in RNA m6A methylation and HCC progression.
36765030	8	48	from	role	1173:1176	arg1	progression					1235:1245	HCC progression	1231:1245	HCC progression	1231:1245	Taken together, our findings reveal a new regulatory mechanism for YTHDF2 and highlight an essential role of YTHDF2 O-GlcNAcylation in RNA m6A methylation and HCC progression.
36765030	6	49	theme	cell	901:904	arg1	progression					912:922	cell cycle progression	901:922	cell cycle progression	901:922	Mechanistically, YTHDF2 stabilized minichromosome maintenance protein 2 (MCM2) and MCM5 transcripts in an m6A-dependent manner, thus promoting cell cycle progression and HBV-related HCC tumorigenesis.
36765030	7	50	theme	inhibitor	1013:1021	arg1	OSMI-1					1023:1028	the OGT inhibitor OSMI-1	1005:1028	the OGT inhibitor OSMI-1	1005:1028	Moreover, targeting YTHDF2 O-GlcNAcylation by the OGT inhibitor OSMI-1 significantly suppressed HCC progression.
36765030	8	51	theme	regulatory	1114:1123	arg1	mechanism					1125:1133	a new regulatory mechanism	1108:1133	a new regulatory mechanism for YTHDF2	1108:1144	Taken together, our findings reveal a new regulatory mechanism for YTHDF2 and highlight an essential role of YTHDF2 O-GlcNAcylation in RNA m6A methylation and HCC progression.
36765030	2	52	theme	YTH	314:316	arg1	domain					337:342	YTH (YT521-B homology) domain 2	314:344	YTH (YT521-B homology) domain 2 (YTHDF2)	314:353	The RNA N6-methyladenosine (m6A) reader, YTH (YT521-B homology) domain 2 (YTHDF2), plays a critical role in the HCC progression.
36765030	2	52	theme	YTH	314:316	arg1	YTHDF2					347:352	YTHDF2	347:352	YTHDF2	347:352	The RNA N6-methyladenosine (m6A) reader, YTH (YT521-B homology) domain 2 (YTHDF2), plays a critical role in the HCC progression.
36765030	2	52	theme	YTH	314:316	arg1	reader					306:311	The RNA N6-methyladenosine (m6A) reader	273:311	The RNA N6-methyladenosine (m6A) reader	273:311	The RNA N6-methyladenosine (m6A) reader, YTH (YT521-B homology) domain 2 (YTHDF2), plays a critical role in the HCC progression.
36765030	1	53	theme	B	137:137	arg1	HBV					146:148	HBV	146:148	HBV	146:148	Hepatitis B virus (HBV) infection is a major risk factor for hepatocellular carcinoma (HCC), but its pathogenic mechanism remains to be explored.
36765030	1	53	theme	B	137:137	arg1	virus					139:143	Hepatitis B virus	127:143	Hepatitis B virus (HBV) infection	127:159	Hepatitis B virus (HBV) infection is a major risk factor for hepatocellular carcinoma (HCC), but its pathogenic mechanism remains to be explored.
36765030	5	54	theme	YTHDF2	649:654	arg1	O-GlcNAcylation					630:644	O-GlcNAc transferase (OGT)-mediated O-GlcNAcylation	594:644	O-GlcNAc transferase (OGT)-mediated O-GlcNAcylation of YTHDF2 on serine 263	594:668	O-GlcNAc transferase (OGT)-mediated O-GlcNAcylation of YTHDF2 on serine 263 enhanced its protein stability and oncogenic activity by inhibiting its ubiquitination.
36765030	3	55	dep	function	415:422	arg1	the					411:413	the	411:413	the	411:413	However, the function and regulatory mechanisms of YTHDF2 in HBV-related HCC remain largely elusive.
36765030	7	56	theme	targeting	969:977	arg1	O-GlcNAcylation					986:1000	targeting YTHDF2 O-GlcNAcylation	969:1000	targeting YTHDF2 O-GlcNAcylation by the OGT inhibitor OSMI-1	969:1028	Moreover, targeting YTHDF2 O-GlcNAcylation by the OGT inhibitor OSMI-1 significantly suppressed HCC progression.
36765030	5	57	theme	oncogenic	705:713	arg1	activity					715:722	oncogenic activity	705:722	oncogenic activity	705:722	O-GlcNAc transferase (OGT)-mediated O-GlcNAcylation of YTHDF2 on serine 263 enhanced its protein stability and oncogenic activity by inhibiting its ubiquitination.
36765030	6	58	theme	maintenance	808:818	arg1	protein					820:826	minichromosome maintenance protein 2	793:828	minichromosome maintenance protein 2 (MCM2)	793:835	Mechanistically, YTHDF2 stabilized minichromosome maintenance protein 2 (MCM2) and MCM5 transcripts in an m6A-dependent manner, thus promoting cell cycle progression and HBV-related HCC tumorigenesis.
36765030	6	58	theme	maintenance	808:818	arg1	MCM2					831:834	MCM2	831:834	MCM2	831:834	Mechanistically, YTHDF2 stabilized minichromosome maintenance protein 2 (MCM2) and MCM5 transcripts in an m6A-dependent manner, thus promoting cell cycle progression and HBV-related HCC tumorigenesis.
36765030	7	59	theme	YTHDF2	979:984	arg1	O-GlcNAcylation					986:1000	targeting YTHDF2 O-GlcNAcylation	969:1000	targeting YTHDF2 O-GlcNAcylation by the OGT inhibitor OSMI-1	969:1028	Moreover, targeting YTHDF2 O-GlcNAcylation by the OGT inhibitor OSMI-1 significantly suppressed HCC progression.
36765030	1	60	theme	pathogenic	228:237	arg1	mechanism					239:247	its pathogenic mechanism	224:247	its pathogenic mechanism	224:247	Hepatitis B virus (HBV) infection is a major risk factor for hepatocellular carcinoma (HCC), but its pathogenic mechanism remains to be explored.
36765030	9	61	theme	pathway	1285:1291	arg1	description					1256:1266	Further description	1248:1266	Further description of the molecular pathway	1248:1291	Further description of the molecular pathway has the potential to yield therapeutic targets for suppression of HCC progression due to HBV infection.
36765030	8	62	theme	O-GlcNAcylation	1188:1202	arg1	role					1173:1176	an essential role	1160:1176	an essential role of YTHDF2 O-GlcNAcylation in RNA m6A methylation and HCC progression	1160:1245	Taken together, our findings reveal a new regulatory mechanism for YTHDF2 and highlight an essential role of YTHDF2 O-GlcNAcylation in RNA m6A methylation and HCC progression.
36765030	3	63	theme	HBV-related	463:473	arg1	HCC					475:477	HBV-related HCC	463:477	HBV-related HCC	463:477	However, the function and regulatory mechanisms of YTHDF2 in HBV-related HCC remain largely elusive.
36765030	5	64	from	O-GlcNAcylation	630:644	arg1	serine					659:664	serine 263	659:668	serine 263	659:668	O-GlcNAc transferase (OGT)-mediated O-GlcNAcylation of YTHDF2 on serine 263 enhanced its protein stability and oncogenic activity by inhibiting its ubiquitination.
11425311	0	0	theme	RNA	80:82	arg1	polymerase					84:93	RNA polymerase II	80:96	RNA polymerase II	80:96	Reciprocity between O-GlcNAc and O-phosphate on the carboxyl terminal domain of RNA polymerase II.
11425311	5	1	theme	CTD	741:743	arg1	kinase					745:750	CTD kinase	741:750	CTD kinase	741:750	In addition, we show that O-GlcNAc transferase and CTD kinase have different CTD repeat requirements for enzymatic activity.
11425311	3	2	link	beta-O-linked	452:464	arg1	GlcNAc					466:471	beta-O-linked GlcNAc	452:471	beta-O-linked GlcNAc on a subset of RNA Pol II molecules	452:507	The CTD is also modified by beta-O-linked GlcNAc on a subset of RNA Pol II molecules.
11425311	2	3	theme	spatial	359:365	arg1	coordination					380:391	the spatial and temporal coordination	355:391	the spatial and temporal coordination of these different activities	355:421	Specific phosphorylation events are associated with the spatial and temporal coordination of these different activities.
11425311	6	4	theme	similar	876:882	arg1	range					884:888	a similar range	874:888	a similar range	874:888	The Km values of the two enzymes for CTD substrates are in a similar range, indicating that neither enzyme has a distinct kinetic advantage.
11425311	3	5	mod	modified	440:447	arg3	GlcNAc					466:471	beta-O-linked GlcNAc	452:471	beta-O-linked GlcNAc on a subset of RNA Pol II molecules	452:507	The CTD is also modified by beta-O-linked GlcNAc on a subset of RNA Pol II molecules.
11425311	3	5	mod	modified	440:447	arg1	CTD					428:430	The CTD	424:430	The CTD	424:430	The CTD is also modified by beta-O-linked GlcNAc on a subset of RNA Pol II molecules.
11425311	8	6	theme	direct	1174:1179	arg1	competition					1181:1191	direct competition	1174:1191	direct competition between OGT and CTD kinase in vivo	1174:1226	Furthermore, direct competition between OGT and CTD kinase in vivo could generate multiple functionally distinct isoforms of RNA Pol II.
11425311	4	7	theme	O-GlcNAc	560:567	arg1	modification					583:594	O-GlcNAc and phosphate modification	560:594	modification	583:594	Using synthetic CTD substrates, we show here that O-GlcNAc and phosphate modification of the CTD are mutually exclusive at the level of the enzymes responsible for their addition.
11425311	7	8	theme	transcription	1140:1152	arg1	cycle					1154:1158	the transcription cycle	1136:1158	the transcription cycle	1136:1158	Thus, the in vivo regulation of O-GlcNAc and phosphate modification of the CTD may involve the differential association of these two enzymes with the CTD at specific stages during the transcription cycle.
11425311	0	9	from	Reciprocity	0:10	arg1	domain					70:75	the carboxyl terminal domain	48:75	the carboxyl terminal domain of RNA polymerase II	48:96	Reciprocity between O-GlcNAc and O-phosphate on the carboxyl terminal domain of RNA polymerase II.
11425311	0	9	from	Reciprocity	0:10	arg1	polymerase					84:93	RNA polymerase II	80:96	RNA polymerase II	80:96	Reciprocity between O-GlcNAc and O-phosphate on the carboxyl terminal domain of RNA polymerase II.
11425311	7	10	theme	differential	1051:1062	arg1	association					1064:1074	the differential association	1047:1074	the differential association of these two enzymes with the CTD	1047:1108	Thus, the in vivo regulation of O-GlcNAc and phosphate modification of the CTD may involve the differential association of these two enzymes with the CTD at specific stages during the transcription cycle.
11425311	0	11	theme	polymerase	84:93	arg1	domain					70:75	the carboxyl terminal domain	48:75	the carboxyl terminal domain of RNA polymerase II	48:96	Reciprocity between O-GlcNAc and O-phosphate on the carboxyl terminal domain of RNA polymerase II.
11425311	0	11	theme	polymerase	84:93	arg1	polymerase					84:93	RNA polymerase II	80:96	RNA polymerase II	80:96	Reciprocity between O-GlcNAc and O-phosphate on the carboxyl terminal domain of RNA polymerase II.
11425311	1	12	contain	has	149:151	arg1	domain					121:126	The carboxyl terminal domain	99:126	The carboxyl terminal domain of RNA polymerase II	99:147	The carboxyl terminal domain of RNA polymerase II has multiple essential roles in transcription initiation, promoter clearance, transcript elongation, and the recruitment of the RNA processing machinery.
11425311	1	12	contain	has	149:151	arg1	polymerase					135:144	RNA polymerase II	131:147	RNA polymerase II	131:147	The carboxyl terminal domain of RNA polymerase II has multiple essential roles in transcription initiation, promoter clearance, transcript elongation, and the recruitment of the RNA processing machinery.
11425311	1	12	contain	has	149:151	arg2	roles					172:176	multiple essential roles	153:176	multiple essential roles	153:176	The carboxyl terminal domain of RNA polymerase II has multiple essential roles in transcription initiation, promoter clearance, transcript elongation, and the recruitment of the RNA processing machinery.
11425311	6	13	theme	kinetic	937:943	arg1	advantage					945:953	a distinct kinetic advantage	926:953	a distinct kinetic advantage	926:953	The Km values of the two enzymes for CTD substrates are in a similar range, indicating that neither enzyme has a distinct kinetic advantage.
11425311	8	14	theme	RNA	1286:1288	arg1	Pol					1290:1292	RNA Pol II	1286:1295	RNA Pol II	1286:1295	Furthermore, direct competition between OGT and CTD kinase in vivo could generate multiple functionally distinct isoforms of RNA Pol II.
11425311	4	15	theme	phosphate	573:581	arg1	modification					583:594	O-GlcNAc and phosphate modification	560:594	modification	583:594	Using synthetic CTD substrates, we show here that O-GlcNAc and phosphate modification of the CTD are mutually exclusive at the level of the enzymes responsible for their addition.
11425311	3	16	theme	RNA	488:490	arg1	molecules					499:507	RNA Pol II molecules	488:507	RNA Pol II molecules	488:507	The CTD is also modified by beta-O-linked GlcNAc on a subset of RNA Pol II molecules.
11425311	7	17	mod	modification	1011:1022	arg1	CTD					1031:1033	the CTD	1027:1033	the CTD	1027:1033	Thus, the in vivo regulation of O-GlcNAc and phosphate modification of the CTD may involve the differential association of these two enzymes with the CTD at specific stages during the transcription cycle.
11425311	7	17	mod	modification	1011:1022	arg3	phosphate					1001:1009	O-GlcNAc and phosphate modification	988:1022	phosphate	1001:1009	Thus, the in vivo regulation of O-GlcNAc and phosphate modification of the CTD may involve the differential association of these two enzymes with the CTD at specific stages during the transcription cycle.
11425311	7	17	mod	modification	1011:1022	arg3	O-GlcNAc					988:995	O-GlcNAc and phosphate modification	988:1022	O-GlcNAc	988:995	Thus, the in vivo regulation of O-GlcNAc and phosphate modification of the CTD may involve the differential association of these two enzymes with the CTD at specific stages during the transcription cycle.
11425311	8	18	theme	CTD	1209:1211	arg1	kinase					1213:1218	CTD kinase	1209:1218	CTD kinase	1209:1218	Furthermore, direct competition between OGT and CTD kinase in vivo could generate multiple functionally distinct isoforms of RNA Pol II.
11425311	9	19	theme	additional	1367:1376	arg1	states					1389:1394	additional functional states	1367:1394	additional functional states of RNA Pol II	1367:1408	Taken together, these results suggest that O-GlcNAc may give rise to additional functional states of RNA Pol II and may coordinate with phosphorylation to regulate class II gene transcription.
11425311	1	20	theme	multiple	153:160	arg1	roles					172:176	multiple essential roles	153:176	multiple essential roles	153:176	The carboxyl terminal domain of RNA polymerase II has multiple essential roles in transcription initiation, promoter clearance, transcript elongation, and the recruitment of the RNA processing machinery.
11425311	5	21	theme	O-GlcNAc	716:723	arg1	transferase					725:735	O-GlcNAc transferase	716:735	O-GlcNAc transferase	716:735	In addition, we show that O-GlcNAc transferase and CTD kinase have different CTD repeat requirements for enzymatic activity.
11425311	6	22	theme	CTD	852:854	arg1	substrates					856:865	CTD substrates	852:865	CTD substrates	852:865	The Km values of the two enzymes for CTD substrates are in a similar range, indicating that neither enzyme has a distinct kinetic advantage.
11425311	7	23	dep	in	966:967	arg1	vivo					969:972	vivo	969:972	vivo	969:972	Thus, the in vivo regulation of O-GlcNAc and phosphate modification of the CTD may involve the differential association of these two enzymes with the CTD at specific stages during the transcription cycle.
11425311	1	24	theme	essential	162:170	arg1	roles					172:176	multiple essential roles	153:176	multiple essential roles	153:176	The carboxyl terminal domain of RNA polymerase II has multiple essential roles in transcription initiation, promoter clearance, transcript elongation, and the recruitment of the RNA processing machinery.
11425311	7	25	theme	specific	1113:1120	arg1	stages					1122:1127	specific stages	1113:1127	specific stages during the transcription cycle	1113:1158	Thus, the in vivo regulation of O-GlcNAc and phosphate modification of the CTD may involve the differential association of these two enzymes with the CTD at specific stages during the transcription cycle.
11425311	7	26	theme	CTD	1031:1033	arg1	modification					1011:1022	O-GlcNAc and phosphate modification	988:1022	modification	1011:1022	Thus, the in vivo regulation of O-GlcNAc and phosphate modification of the CTD may involve the differential association of these two enzymes with the CTD at specific stages during the transcription cycle.
11425311	2	27	theme	phosphorylation	312:326	arg1	events					328:333	Specific phosphorylation events	303:333	Specific phosphorylation events	303:333	Specific phosphorylation events are associated with the spatial and temporal coordination of these different activities.
11425311	4	28	from	level	637:641	arg1	exclusive					620:628	exclusive	620:628	exclusive	620:628	Using synthetic CTD substrates, we show here that O-GlcNAc and phosphate modification of the CTD are mutually exclusive at the level of the enzymes responsible for their addition.
11425311	4	29	theme	enzymes	650:656	arg1	level					637:641	the level	633:641	the level of the enzymes responsible for their addition	633:687	Using synthetic CTD substrates, we show here that O-GlcNAc and phosphate modification of the CTD are mutually exclusive at the level of the enzymes responsible for their addition.
11425311	6	30	theme	distinct	928:935	arg1	advantage					945:953	a distinct kinetic advantage	926:953	a distinct kinetic advantage	926:953	The Km values of the two enzymes for CTD substrates are in a similar range, indicating that neither enzyme has a distinct kinetic advantage.
11425311	5	31	contain	have	752:755	arg2	requirements					778:789	different CTD repeat requirements	757:789	different CTD repeat requirements for enzymatic activity	757:812	In addition, we show that O-GlcNAc transferase and CTD kinase have different CTD repeat requirements for enzymatic activity.
11425311	5	31	contain	have	752:755	arg1	transferase					725:735	O-GlcNAc transferase	716:735	O-GlcNAc transferase	716:735	In addition, we show that O-GlcNAc transferase and CTD kinase have different CTD repeat requirements for enzymatic activity.
11425311	5	31	contain	have	752:755	arg1	kinase					745:750	CTD kinase	741:750	CTD kinase	741:750	In addition, we show that O-GlcNAc transferase and CTD kinase have different CTD repeat requirements for enzymatic activity.
11425311	7	32	theme	modification	1011:1022	arg1	regulation					974:983	the in vivo regulation	962:983	the in vivo regulation of O-GlcNAc and phosphate modification of the CTD	962:1033	Thus, the in vivo regulation of O-GlcNAc and phosphate modification of the CTD may involve the differential association of these two enzymes with the CTD at specific stages during the transcription cycle.
11425311	2	33	theme	Specific	303:310	arg1	events					328:333	Specific phosphorylation events	303:333	Specific phosphorylation events	303:333	Specific phosphorylation events are associated with the spatial and temporal coordination of these different activities.
11425311	9	34	theme	RNA	1399:1401	arg1	Pol					1403:1405	RNA Pol II	1399:1408	RNA Pol II	1399:1408	Taken together, these results suggest that O-GlcNAc may give rise to additional functional states of RNA Pol II and may coordinate with phosphorylation to regulate class II gene transcription.
11425311	5	35	theme	enzymatic	795:803	arg1	activity					805:812	enzymatic activity	795:812	enzymatic activity	795:812	In addition, we show that O-GlcNAc transferase and CTD kinase have different CTD repeat requirements for enzymatic activity.
11425311	8	36	theme	multiple	1243:1250	arg1	isoforms					1274:1281	multiple functionally distinct isoforms	1243:1281	multiple functionally distinct isoforms of RNA Pol II	1243:1295	Furthermore, direct competition between OGT and CTD kinase in vivo could generate multiple functionally distinct isoforms of RNA Pol II.
11425311	9	37	theme	functional	1378:1387	arg1	states					1389:1394	additional functional states	1367:1394	additional functional states of RNA Pol II	1367:1408	Taken together, these results suggest that O-GlcNAc may give rise to additional functional states of RNA Pol II and may coordinate with phosphorylation to regulate class II gene transcription.
11425311	5	38	theme	CTD	767:769	arg1	requirements					778:789	different CTD repeat requirements	757:789	different CTD repeat requirements for enzymatic activity	757:812	In addition, we show that O-GlcNAc transferase and CTD kinase have different CTD repeat requirements for enzymatic activity.
11425311	1	39	theme	transcription	181:193	arg1	initiation					195:204	transcription initiation	181:204	transcription initiation	181:204	The carboxyl terminal domain of RNA polymerase II has multiple essential roles in transcription initiation, promoter clearance, transcript elongation, and the recruitment of the RNA processing machinery.
11425311	1	40	theme	RNA	277:279	arg1	machinery					292:300	the RNA processing machinery	273:300	the RNA processing machinery	273:300	The carboxyl terminal domain of RNA polymerase II has multiple essential roles in transcription initiation, promoter clearance, transcript elongation, and the recruitment of the RNA processing machinery.
11425311	6	41	theme	enzymes	840:846	arg1	values					822:827	The Km values	815:827	The Km values of the two enzymes for CTD substrates	815:865	The Km values of the two enzymes for CTD substrates are in a similar range, indicating that neither enzyme has a distinct kinetic advantage.
11425311	3	42	theme	Pol	492:494	arg1	molecules					499:507	RNA Pol II molecules	488:507	RNA Pol II molecules	488:507	The CTD is also modified by beta-O-linked GlcNAc on a subset of RNA Pol II molecules.
11425311	9	43	theme	gene	1471:1474	arg1	transcription					1476:1488	class II gene transcription	1462:1488	class II gene transcription	1462:1488	Taken together, these results suggest that O-GlcNAc may give rise to additional functional states of RNA Pol II and may coordinate with phosphorylation to regulate class II gene transcription.
11425311	2	44	theme	temporal	371:378	arg1	coordination					380:391	the spatial and temporal coordination	355:391	the spatial and temporal coordination of these different activities	355:421	Specific phosphorylation events are associated with the spatial and temporal coordination of these different activities.
11425311	1	45	theme	processing	281:290	arg1	machinery					292:300	the RNA processing machinery	273:300	the RNA processing machinery	273:300	The carboxyl terminal domain of RNA polymerase II has multiple essential roles in transcription initiation, promoter clearance, transcript elongation, and the recruitment of the RNA processing machinery.
11425311	7	46	theme	phosphate	1001:1009	arg1	modification					1011:1022	O-GlcNAc and phosphate modification	988:1022	modification	1011:1022	Thus, the in vivo regulation of O-GlcNAc and phosphate modification of the CTD may involve the differential association of these two enzymes with the CTD at specific stages during the transcription cycle.
11425311	3	47	theme	beta-O-linked	452:464	arg1	GlcNAc					466:471	beta-O-linked GlcNAc	452:471	beta-O-linked GlcNAc on a subset of RNA Pol II molecules	452:507	The CTD is also modified by beta-O-linked GlcNAc on a subset of RNA Pol II molecules.
11425311	2	48	theme	different	402:410	arg1	activities					412:421	these different activities	396:421	these different activities	396:421	Specific phosphorylation events are associated with the spatial and temporal coordination of these different activities.
11425311	1	49	theme	machinery	292:300	arg1	initiation					195:204	transcription initiation	181:204	transcription initiation	181:204	The carboxyl terminal domain of RNA polymerase II has multiple essential roles in transcription initiation, promoter clearance, transcript elongation, and the recruitment of the RNA processing machinery.
11425311	1	49	theme	machinery	292:300	arg1	clearance					216:224	promoter clearance	207:224	promoter clearance	207:224	The carboxyl terminal domain of RNA polymerase II has multiple essential roles in transcription initiation, promoter clearance, transcript elongation, and the recruitment of the RNA processing machinery.
11425311	1	49	theme	machinery	292:300	arg1	elongation					238:247	transcript elongation	227:247	transcript elongation	227:247	The carboxyl terminal domain of RNA polymerase II has multiple essential roles in transcription initiation, promoter clearance, transcript elongation, and the recruitment of the RNA processing machinery.
11425311	1	49	theme	machinery	292:300	arg1	recruitment					258:268	the recruitment	254:268	the recruitment of the RNA processing machinery	254:300	The carboxyl terminal domain of RNA polymerase II has multiple essential roles in transcription initiation, promoter clearance, transcript elongation, and the recruitment of the RNA processing machinery.
11425311	5	50	theme	different	757:765	arg1	requirements					778:789	different CTD repeat requirements	757:789	different CTD repeat requirements for enzymatic activity	757:812	In addition, we show that O-GlcNAc transferase and CTD kinase have different CTD repeat requirements for enzymatic activity.
11425311	8	51	theme	distinct	1265:1272	arg1	isoforms					1274:1281	multiple functionally distinct isoforms	1243:1281	multiple functionally distinct isoforms of RNA Pol II	1243:1295	Furthermore, direct competition between OGT and CTD kinase in vivo could generate multiple functionally distinct isoforms of RNA Pol II.
11425311	6	52	contain	has	922:924	arg2	advantage					945:953	a distinct kinetic advantage	926:953	a distinct kinetic advantage	926:953	The Km values of the two enzymes for CTD substrates are in a similar range, indicating that neither enzyme has a distinct kinetic advantage.
11425311	6	52	contain	has	922:924	arg1	enzyme					915:920	neither enzyme	907:920	neither enzyme	907:920	The Km values of the two enzymes for CTD substrates are in a similar range, indicating that neither enzyme has a distinct kinetic advantage.
11425311	7	53	theme	in	966:967	arg1	regulation					974:983	the in vivo regulation	962:983	the in vivo regulation of O-GlcNAc and phosphate modification of the CTD	962:1033	Thus, the in vivo regulation of O-GlcNAc and phosphate modification of the CTD may involve the differential association of these two enzymes with the CTD at specific stages during the transcription cycle.
11425311	2	54	theme	activities	412:421	arg1	coordination					380:391	the spatial and temporal coordination	355:391	the spatial and temporal coordination of these different activities	355:421	Specific phosphorylation events are associated with the spatial and temporal coordination of these different activities.
11425311	0	55	theme	carboxyl	52:59	arg1	domain					70:75	the carboxyl terminal domain	48:75	the carboxyl terminal domain of RNA polymerase II	48:96	Reciprocity between O-GlcNAc and O-phosphate on the carboxyl terminal domain of RNA polymerase II.
11425311	0	55	theme	carboxyl	52:59	arg1	polymerase					84:93	RNA polymerase II	80:96	RNA polymerase II	80:96	Reciprocity between O-GlcNAc and O-phosphate on the carboxyl terminal domain of RNA polymerase II.
11425311	4	56	theme	CTD	526:528	arg1	substrates					530:539	synthetic CTD substrates	516:539	synthetic CTD substrates	516:539	Using synthetic CTD substrates, we show here that O-GlcNAc and phosphate modification of the CTD are mutually exclusive at the level of the enzymes responsible for their addition.
11425311	7	57	theme	O-GlcNAc	988:995	arg1	modification					1011:1022	O-GlcNAc and phosphate modification	988:1022	modification	1011:1022	Thus, the in vivo regulation of O-GlcNAc and phosphate modification of the CTD may involve the differential association of these two enzymes with the CTD at specific stages during the transcription cycle.
11425311	4	58	mod	modification	583:594	arg3	O-GlcNAc					560:567	O-GlcNAc and phosphate modification	560:594	O-GlcNAc	560:567	Using synthetic CTD substrates, we show here that O-GlcNAc and phosphate modification of the CTD are mutually exclusive at the level of the enzymes responsible for their addition.
11425311	4	58	mod	modification	583:594	arg3	phosphate					573:581	O-GlcNAc and phosphate modification	560:594	phosphate	573:581	Using synthetic CTD substrates, we show here that O-GlcNAc and phosphate modification of the CTD are mutually exclusive at the level of the enzymes responsible for their addition.
11425311	4	58	mod	modification	583:594	arg1	CTD					603:605	the CTD	599:605	the CTD	599:605	Using synthetic CTD substrates, we show here that O-GlcNAc and phosphate modification of the CTD are mutually exclusive at the level of the enzymes responsible for their addition.
11425311	3	59	from	GlcNAc	466:471	arg1	subset					478:483	a subset	476:483	a subset of RNA Pol II molecules	476:507	The CTD is also modified by beta-O-linked GlcNAc on a subset of RNA Pol II molecules.
11425311	1	60	theme	carboxyl	103:110	arg1	domain					121:126	The carboxyl terminal domain	99:126	The carboxyl terminal domain of RNA polymerase II	99:147	The carboxyl terminal domain of RNA polymerase II has multiple essential roles in transcription initiation, promoter clearance, transcript elongation, and the recruitment of the RNA processing machinery.
11425311	1	60	theme	carboxyl	103:110	arg1	polymerase					135:144	RNA polymerase II	131:147	RNA polymerase II	131:147	The carboxyl terminal domain of RNA polymerase II has multiple essential roles in transcription initiation, promoter clearance, transcript elongation, and the recruitment of the RNA processing machinery.
11425311	5	61	theme	repeat	771:776	arg1	requirements					778:789	different CTD repeat requirements	757:789	different CTD repeat requirements for enzymatic activity	757:812	In addition, we show that O-GlcNAc transferase and CTD kinase have different CTD repeat requirements for enzymatic activity.
11425311	3	62	theme	molecules	499:507	arg1	subset					478:483	a subset	476:483	a subset of RNA Pol II molecules	476:507	The CTD is also modified by beta-O-linked GlcNAc on a subset of RNA Pol II molecules.
11425311	1	63	theme	terminal	112:119	arg1	domain					121:126	The carboxyl terminal domain	99:126	The carboxyl terminal domain of RNA polymerase II	99:147	The carboxyl terminal domain of RNA polymerase II has multiple essential roles in transcription initiation, promoter clearance, transcript elongation, and the recruitment of the RNA processing machinery.
11425311	1	63	theme	terminal	112:119	arg1	polymerase					135:144	RNA polymerase II	131:147	RNA polymerase II	131:147	The carboxyl terminal domain of RNA polymerase II has multiple essential roles in transcription initiation, promoter clearance, transcript elongation, and the recruitment of the RNA processing machinery.
11425311	6	64	theme	Km	819:820	arg1	values					822:827	The Km values	815:827	The Km values of the two enzymes for CTD substrates	815:865	The Km values of the two enzymes for CTD substrates are in a similar range, indicating that neither enzyme has a distinct kinetic advantage.
11425311	7	65	theme	enzymes	1089:1095	arg1	association					1064:1074	the differential association	1047:1074	the differential association of these two enzymes with the CTD	1047:1108	Thus, the in vivo regulation of O-GlcNAc and phosphate modification of the CTD may involve the differential association of these two enzymes with the CTD at specific stages during the transcription cycle.
11425311	9	66	theme	class	1462:1466	arg1	transcription					1476:1488	class II gene transcription	1462:1488	class II gene transcription	1462:1488	Taken together, these results suggest that O-GlcNAc may give rise to additional functional states of RNA Pol II and may coordinate with phosphorylation to regulate class II gene transcription.
11425311	4	67	theme	responsible	658:668	arg1	enzymes					650:656	the enzymes	646:656	the enzymes responsible for their addition	646:687	Using synthetic CTD substrates, we show here that O-GlcNAc and phosphate modification of the CTD are mutually exclusive at the level of the enzymes responsible for their addition.
11425311	8	68	theme	Pol	1290:1292	arg1	isoforms					1274:1281	multiple functionally distinct isoforms	1243:1281	multiple functionally distinct isoforms of RNA Pol II	1243:1295	Furthermore, direct competition between OGT and CTD kinase in vivo could generate multiple functionally distinct isoforms of RNA Pol II.
11425311	4	69	theme	synthetic	516:524	arg1	substrates					530:539	synthetic CTD substrates	516:539	synthetic CTD substrates	516:539	Using synthetic CTD substrates, we show here that O-GlcNAc and phosphate modification of the CTD are mutually exclusive at the level of the enzymes responsible for their addition.
11425311	1	70	theme	promoter	207:214	arg1	clearance					216:224	promoter clearance	207:224	promoter clearance	207:224	The carboxyl terminal domain of RNA polymerase II has multiple essential roles in transcription initiation, promoter clearance, transcript elongation, and the recruitment of the RNA processing machinery.
11425311	9	71	theme	Pol	1403:1405	arg1	states					1389:1394	additional functional states	1367:1394	additional functional states of RNA Pol II	1367:1408	Taken together, these results suggest that O-GlcNAc may give rise to additional functional states of RNA Pol II and may coordinate with phosphorylation to regulate class II gene transcription.
11425311	1	72	theme	RNA	131:133	arg1	polymerase					135:144	RNA polymerase II	131:147	RNA polymerase II	131:147	The carboxyl terminal domain of RNA polymerase II has multiple essential roles in transcription initiation, promoter clearance, transcript elongation, and the recruitment of the RNA processing machinery.
11425311	1	73	theme	transcript	227:236	arg1	elongation					238:247	transcript elongation	227:247	transcript elongation	227:247	The carboxyl terminal domain of RNA polymerase II has multiple essential roles in transcription initiation, promoter clearance, transcript elongation, and the recruitment of the RNA processing machinery.
11425311	0	74	theme	terminal	61:68	arg1	domain					70:75	the carboxyl terminal domain	48:75	the carboxyl terminal domain of RNA polymerase II	48:96	Reciprocity between O-GlcNAc and O-phosphate on the carboxyl terminal domain of RNA polymerase II.
11425311	0	74	theme	terminal	61:68	arg1	polymerase					84:93	RNA polymerase II	80:96	RNA polymerase II	80:96	Reciprocity between O-GlcNAc and O-phosphate on the carboxyl terminal domain of RNA polymerase II.
11425311	1	75	theme	polymerase	135:144	arg1	domain					121:126	The carboxyl terminal domain	99:126	The carboxyl terminal domain of RNA polymerase II	99:147	The carboxyl terminal domain of RNA polymerase II has multiple essential roles in transcription initiation, promoter clearance, transcript elongation, and the recruitment of the RNA processing machinery.
11425311	1	75	theme	polymerase	135:144	arg1	polymerase					135:144	RNA polymerase II	131:147	RNA polymerase II	131:147	The carboxyl terminal domain of RNA polymerase II has multiple essential roles in transcription initiation, promoter clearance, transcript elongation, and the recruitment of the RNA processing machinery.
11425311	7	76	with	association	1064:1074	arg1	CTD					1106:1108	the CTD	1102:1108	the CTD	1102:1108	Thus, the in vivo regulation of O-GlcNAc and phosphate modification of the CTD may involve the differential association of these two enzymes with the CTD at specific stages during the transcription cycle.
11425311	4	77	theme	CTD	603:605	arg1	modification					583:594	O-GlcNAc and phosphate modification	560:594	modification	583:594	Using synthetic CTD substrates, we show here that O-GlcNAc and phosphate modification of the CTD are mutually exclusive at the level of the enzymes responsible for their addition.
34974534	6	0	theme	growth	1037:1042	arg1	genes					1013:1017	TGF-β1 target genes connective tissue growth factor (CTGF) and snail family transcriptional repressor 1 (SNAIL)	999:1109	TGF-β1 target genes connective tissue growth factor (CTGF) and snail family transcriptional repressor 1 (SNAIL)	999:1109	O-GlcNAcylated MORC2 is required for transcriptional activation of TGF-β1 target genes connective tissue growth factor (CTGF) and snail family transcriptional repressor 1 (SNAIL).
34974534	6	0	theme	growth	1037:1042	arg1	CTGF					1052:1055	CTGF	1052:1055	CTGF	1052:1055	O-GlcNAcylated MORC2 is required for transcriptional activation of TGF-β1 target genes connective tissue growth factor (CTGF) and snail family transcriptional repressor 1 (SNAIL).
34974534	6	0	theme	growth	1037:1042	arg1	factor					1044:1049	connective tissue growth factor	1019:1049	connective tissue growth factor (CTGF)	1019:1056	O-GlcNAcylated MORC2 is required for transcriptional activation of TGF-β1 target genes connective tissue growth factor (CTGF) and snail family transcriptional repressor 1 (SNAIL).
34974534	5	1	theme	aminotransferase	843:858	arg1	stability					799:807	the stability	795:807	the stability of glutamine-fructose-6-phosphate aminotransferase (GFAT), the rate-limiting enzyme for producing the sugar donor for OGT	795:929	Moreover, transforming growth factor-β1 (TGF-β1) induces MORC2 O-GlcNAcylation through enhancing the stability of glutamine-fructose-6-phosphate aminotransferase (GFAT), the rate-limiting enzyme for producing the sugar donor for OGT.
34974534	7	2	theme	cell	1252:1255	arg1	migration					1257:1265	TGF-β1-induced, MORC2 O-GlcNAcylation-mediated breast cancer cell migration	1191:1265	TGF-β1-induced, MORC2 O-GlcNAcylation-mediated breast cancer cell migration	1191:1265	In support of these observations, knockdown of GFAT, SNAIL or CTGF compromises TGF-β1-induced, MORC2 O-GlcNAcylation-mediated breast cancer cell migration and invasion.
34974534	4	3	theme	site	551:554	arg1	Mutation					534:541	Mutation	534:541	Mutation of this site	534:554	Mutation of this site or pharmacological inhibition of OGT impairs MORC2-mediated breast cancer cell migration and invasion in vitro and lung colonization in vivo.
34974534	4	3	theme	site	551:554	arg1	inhibition					575:584	pharmacological inhibition	559:584	pharmacological inhibition of OGT	559:591	Mutation of this site or pharmacological inhibition of OGT impairs MORC2-mediated breast cancer cell migration and invasion in vitro and lung colonization in vivo.
34974534	6	4	theme	snail	1062:1066	arg1	genes					1013:1017	TGF-β1 target genes connective tissue growth factor (CTGF) and snail family transcriptional repressor 1 (SNAIL)	999:1109	TGF-β1 target genes connective tissue growth factor (CTGF) and snail family transcriptional repressor 1 (SNAIL)	999:1109	O-GlcNAcylated MORC2 is required for transcriptional activation of TGF-β1 target genes connective tissue growth factor (CTGF) and snail family transcriptional repressor 1 (SNAIL).
34974534	6	4	theme	snail	1062:1066	arg1	SNAIL					1104:1108	snail family transcriptional repressor 1 (SNAIL)	1062:1109	snail family transcriptional repressor 1 (SNAIL)	1062:1109	O-GlcNAcylated MORC2 is required for transcriptional activation of TGF-β1 target genes connective tissue growth factor (CTGF) and snail family transcriptional repressor 1 (SNAIL).
34974534	1	5	theme	neurodevelopmental	323:340	arg1	disorder					342:349	neurodevelopmental disorder	323:349	neurodevelopmental disorder	323:349	MORC family CW-type zinc finger 2 (MORC2) is a newly identified chromatin-remodeling enzyme involved in DNA damage response and gene transcription, and its dysregulation has been linked with Charcot-Marie-Tooth disease, neurodevelopmental disorder, and cancer.
34974534	3	6	theme	O-GlcNAc	489:496	arg1	OGT					511:513	OGT	511:513	OGT	511:513	Here, we report that MORC2 is O-GlcNAcylated by O-GlcNAc transferase (OGT) at threonine 556.
34974534	3	6	theme	O-GlcNAc	489:496	arg1	transferase					498:508	O-GlcNAc transferase	489:508	O-GlcNAc transferase (OGT) at threonine 556	489:531	Here, we report that MORC2 is O-GlcNAcylated by O-GlcNAc transferase (OGT) at threonine 556.
34974534	1	7	theme	gene	231:234	arg1	transcription					236:248	gene transcription	231:248	gene transcription	231:248	MORC family CW-type zinc finger 2 (MORC2) is a newly identified chromatin-remodeling enzyme involved in DNA damage response and gene transcription, and its dysregulation has been linked with Charcot-Marie-Tooth disease, neurodevelopmental disorder, and cancer.
34974534	0	8	theme	cancer	83:88	arg1	progression					90:100	breast cancer progression	76:100	breast cancer progression	76:100	O-GlcNAcylation of MORC2 at threonine 556 by OGT couples TGF-β signaling to breast cancer progression.
34974534	6	9	dep	genes	1013:1017	arg1	genes					1013:1017	TGF-β1 target genes connective tissue growth factor (CTGF) and snail family transcriptional repressor 1 (SNAIL)	999:1109	TGF-β1 target genes connective tissue growth factor (CTGF) and snail family transcriptional repressor 1 (SNAIL)	999:1109	O-GlcNAcylated MORC2 is required for transcriptional activation of TGF-β1 target genes connective tissue growth factor (CTGF) and snail family transcriptional repressor 1 (SNAIL).
34974534	6	9	dep	genes	1013:1017	arg1	CTGF					1052:1055	CTGF	1052:1055	CTGF	1052:1055	O-GlcNAcylated MORC2 is required for transcriptional activation of TGF-β1 target genes connective tissue growth factor (CTGF) and snail family transcriptional repressor 1 (SNAIL).
34974534	6	9	dep	genes	1013:1017	arg1	factor					1044:1049	connective tissue growth factor	1019:1049	connective tissue growth factor (CTGF)	1019:1056	O-GlcNAcylated MORC2 is required for transcriptional activation of TGF-β1 target genes connective tissue growth factor (CTGF) and snail family transcriptional repressor 1 (SNAIL).
34974534	6	9	dep	genes	1013:1017	arg1	SNAIL					1104:1108	snail family transcriptional repressor 1 (SNAIL)	1062:1109	snail family transcriptional repressor 1 (SNAIL)	1062:1109	O-GlcNAcylated MORC2 is required for transcriptional activation of TGF-β1 target genes connective tissue growth factor (CTGF) and snail family transcriptional repressor 1 (SNAIL).
34974534	8	10	theme	CTGF	1335:1338	arg1	expression					1298:1307	high expression	1293:1307	high expression of OGT, MORC2, SNAIL, and CTGF in breast tumors	1293:1355	Clinically, high expression of OGT, MORC2, SNAIL, and CTGF in breast tumors is associated with poor patient prognosis.
34974534	3	11	from	threonine	519:527	arg1	OGT					511:513	OGT	511:513	OGT	511:513	Here, we report that MORC2 is O-GlcNAcylated by O-GlcNAc transferase (OGT) at threonine 556.
34974534	3	11	from	threonine	519:527	arg1	transferase					498:508	O-GlcNAc transferase	489:508	O-GlcNAc transferase (OGT) at threonine 556	489:531	Here, we report that MORC2 is O-GlcNAcylated by O-GlcNAc transferase (OGT) at threonine 556.
34974534	4	12	theme	pharmacological	559:573	arg1	inhibition					575:584	pharmacological inhibition	559:584	pharmacological inhibition of OGT	559:591	Mutation of this site or pharmacological inhibition of OGT impairs MORC2-mediated breast cancer cell migration and invasion in vitro and lung colonization in vivo.
34974534	0	13	theme	breast	76:81	arg1	progression					90:100	breast cancer progression	76:100	breast cancer progression	76:100	O-GlcNAcylation of MORC2 at threonine 556 by OGT couples TGF-β signaling to breast cancer progression.
34974534	6	14	theme	TGF-β1	999:1004	arg1	genes					1013:1017	TGF-β1 target genes connective tissue growth factor (CTGF) and snail family transcriptional repressor 1 (SNAIL)	999:1109	TGF-β1 target genes connective tissue growth factor (CTGF) and snail family transcriptional repressor 1 (SNAIL)	999:1109	O-GlcNAcylated MORC2 is required for transcriptional activation of TGF-β1 target genes connective tissue growth factor (CTGF) and snail family transcriptional repressor 1 (SNAIL).
34974534	6	14	theme	TGF-β1	999:1004	arg1	factor					1044:1049	connective tissue growth factor	1019:1049	connective tissue growth factor (CTGF)	1019:1056	O-GlcNAcylated MORC2 is required for transcriptional activation of TGF-β1 target genes connective tissue growth factor (CTGF) and snail family transcriptional repressor 1 (SNAIL).
34974534	6	14	theme	TGF-β1	999:1004	arg1	SNAIL					1104:1108	snail family transcriptional repressor 1 (SNAIL)	1062:1109	snail family transcriptional repressor 1 (SNAIL)	1062:1109	O-GlcNAcylated MORC2 is required for transcriptional activation of TGF-β1 target genes connective tissue growth factor (CTGF) and snail family transcriptional repressor 1 (SNAIL).
34974534	5	15	theme	growth	721:726	arg1	TGF-β1					739:744	TGF-β1	739:744	TGF-β1	739:744	Moreover, transforming growth factor-β1 (TGF-β1) induces MORC2 O-GlcNAcylation through enhancing the stability of glutamine-fructose-6-phosphate aminotransferase (GFAT), the rate-limiting enzyme for producing the sugar donor for OGT.
34974534	5	15	theme	growth	721:726	arg1	factor-β1					728:736	transforming growth factor-β1	708:736	transforming growth factor-β1 (TGF-β1)	708:745	Moreover, transforming growth factor-β1 (TGF-β1) induces MORC2 O-GlcNAcylation through enhancing the stability of glutamine-fructose-6-phosphate aminotransferase (GFAT), the rate-limiting enzyme for producing the sugar donor for OGT.
34974534	4	16	theme	MORC2-mediated	601:614	arg1	cancer					623:628	MORC2-mediated breast cancer	601:628	MORC2-mediated breast cancer cell migration	601:643	Mutation of this site or pharmacological inhibition of OGT impairs MORC2-mediated breast cancer cell migration and invasion in vitro and lung colonization in vivo.
34974534	8	17	theme	breast	1343:1348	arg1	tumors					1350:1355	breast tumors	1343:1355	breast tumors	1343:1355	Clinically, high expression of OGT, MORC2, SNAIL, and CTGF in breast tumors is associated with poor patient prognosis.
34974534	6	18	theme	transcriptional	1075:1089	arg1	genes					1013:1017	TGF-β1 target genes connective tissue growth factor (CTGF) and snail family transcriptional repressor 1 (SNAIL)	999:1109	TGF-β1 target genes connective tissue growth factor (CTGF) and snail family transcriptional repressor 1 (SNAIL)	999:1109	O-GlcNAcylated MORC2 is required for transcriptional activation of TGF-β1 target genes connective tissue growth factor (CTGF) and snail family transcriptional repressor 1 (SNAIL).
34974534	6	18	theme	transcriptional	1075:1089	arg1	SNAIL					1104:1108	snail family transcriptional repressor 1 (SNAIL)	1062:1109	snail family transcriptional repressor 1 (SNAIL)	1062:1109	O-GlcNAcylated MORC2 is required for transcriptional activation of TGF-β1 target genes connective tissue growth factor (CTGF) and snail family transcriptional repressor 1 (SNAIL).
34974534	9	19	theme	mechanistic	1463:1473	arg1	role					1475:1478	a previously unrecognized mechanistic role	1437:1478	a previously unrecognized mechanistic role for MORC2 O-GlcNAcylation in breast cancer progression	1437:1533	Collectively, these findings uncover a previously unrecognized mechanistic role for MORC2 O-GlcNAcylation in breast cancer progression and provide evidence for targeting MORC2-dependent breast cancer through blocking its O-GlcNAcylation.
34974534	5	20	theme	sugar	911:915	arg1	donor					917:921	the sugar donor	907:921	the sugar donor for OGT	907:929	Moreover, transforming growth factor-β1 (TGF-β1) induces MORC2 O-GlcNAcylation through enhancing the stability of glutamine-fructose-6-phosphate aminotransferase (GFAT), the rate-limiting enzyme for producing the sugar donor for OGT.
34974534	6	21	theme	connective	1019:1028	arg1	genes					1013:1017	TGF-β1 target genes connective tissue growth factor (CTGF) and snail family transcriptional repressor 1 (SNAIL)	999:1109	TGF-β1 target genes connective tissue growth factor (CTGF) and snail family transcriptional repressor 1 (SNAIL)	999:1109	O-GlcNAcylated MORC2 is required for transcriptional activation of TGF-β1 target genes connective tissue growth factor (CTGF) and snail family transcriptional repressor 1 (SNAIL).
34974534	6	21	theme	connective	1019:1028	arg1	CTGF					1052:1055	CTGF	1052:1055	CTGF	1052:1055	O-GlcNAcylated MORC2 is required for transcriptional activation of TGF-β1 target genes connective tissue growth factor (CTGF) and snail family transcriptional repressor 1 (SNAIL).
34974534	6	21	theme	connective	1019:1028	arg1	factor					1044:1049	connective tissue growth factor	1019:1049	connective tissue growth factor (CTGF)	1019:1056	O-GlcNAcylated MORC2 is required for transcriptional activation of TGF-β1 target genes connective tissue growth factor (CTGF) and snail family transcriptional repressor 1 (SNAIL).
34974534	9	22	theme	breast	1586:1591	arg1	cancer					1593:1598	MORC2-dependent breast cancer	1570:1598	MORC2-dependent breast cancer	1570:1598	Collectively, these findings uncover a previously unrecognized mechanistic role for MORC2 O-GlcNAcylation in breast cancer progression and provide evidence for targeting MORC2-dependent breast cancer through blocking its O-GlcNAcylation.
34974534	2	23	theme	functional	376:385	arg1	importance					387:396	its functional importance	372:396	its functional importance	372:396	Despite its functional importance, how MORC2 is regulated remains enigmatic.
34974534	7	24	theme	SNAIL	1165:1169	arg1	knockdown					1146:1154	knockdown	1146:1154	knockdown of GFAT, SNAIL or CTGF	1146:1177	In support of these observations, knockdown of GFAT, SNAIL or CTGF compromises TGF-β1-induced, MORC2 O-GlcNAcylation-mediated breast cancer cell migration and invasion.
34974534	0	25	from	threonine	28:36	arg1	O-GlcNAcylation					0:14	O-GlcNAcylation	0:14	O-GlcNAcylation of MORC2 at threonine 556 by OGT	0:47	O-GlcNAcylation of MORC2 at threonine 556 by OGT couples TGF-β signaling to breast cancer progression.
34974534	7	26	theme	breast	1238:1243	arg1	cancer					1245:1250	TGF-β1-induced, MORC2 O-GlcNAcylation-mediated breast cancer	1191:1250	TGF-β1-induced, MORC2 O-GlcNAcylation-mediated breast cancer cell migration	1191:1265	In support of these observations, knockdown of GFAT, SNAIL or CTGF compromises TGF-β1-induced, MORC2 O-GlcNAcylation-mediated breast cancer cell migration and invasion.
34974534	5	27	theme	rate-limiting	872:884	arg1	aminotransferase					843:858	glutamine-fructose-6-phosphate aminotransferase	812:858	glutamine-fructose-6-phosphate aminotransferase (GFAT)	812:865	Moreover, transforming growth factor-β1 (TGF-β1) induces MORC2 O-GlcNAcylation through enhancing the stability of glutamine-fructose-6-phosphate aminotransferase (GFAT), the rate-limiting enzyme for producing the sugar donor for OGT.
34974534	5	27	theme	rate-limiting	872:884	arg1	enzyme					886:891	the rate-limiting enzyme	868:891	the rate-limiting enzyme for producing the sugar donor for OGT	868:929	Moreover, transforming growth factor-β1 (TGF-β1) induces MORC2 O-GlcNAcylation through enhancing the stability of glutamine-fructose-6-phosphate aminotransferase (GFAT), the rate-limiting enzyme for producing the sugar donor for OGT.
34974534	6	28	theme	O-GlcNAcylated	932:945	arg1	MORC2					947:951	O-GlcNAcylated MORC2	932:951	O-GlcNAcylated MORC2	932:951	O-GlcNAcylated MORC2 is required for transcriptional activation of TGF-β1 target genes connective tissue growth factor (CTGF) and snail family transcriptional repressor 1 (SNAIL).
34974534	6	29	theme	family	1068:1073	arg1	genes					1013:1017	TGF-β1 target genes connective tissue growth factor (CTGF) and snail family transcriptional repressor 1 (SNAIL)	999:1109	TGF-β1 target genes connective tissue growth factor (CTGF) and snail family transcriptional repressor 1 (SNAIL)	999:1109	O-GlcNAcylated MORC2 is required for transcriptional activation of TGF-β1 target genes connective tissue growth factor (CTGF) and snail family transcriptional repressor 1 (SNAIL).
34974534	6	29	theme	family	1068:1073	arg1	SNAIL					1104:1108	snail family transcriptional repressor 1 (SNAIL)	1062:1109	snail family transcriptional repressor 1 (SNAIL)	1062:1109	O-GlcNAcylated MORC2 is required for transcriptional activation of TGF-β1 target genes connective tissue growth factor (CTGF) and snail family transcriptional repressor 1 (SNAIL).
34974534	7	30	theme	GFAT	1159:1162	arg1	knockdown					1146:1154	knockdown	1146:1154	knockdown of GFAT, SNAIL or CTGF	1146:1177	In support of these observations, knockdown of GFAT, SNAIL or CTGF compromises TGF-β1-induced, MORC2 O-GlcNAcylation-mediated breast cancer cell migration and invasion.
34974534	8	31	theme	OGT	1312:1314	arg1	expression					1298:1307	high expression	1293:1307	high expression of OGT, MORC2, SNAIL, and CTGF in breast tumors	1293:1355	Clinically, high expression of OGT, MORC2, SNAIL, and CTGF in breast tumors is associated with poor patient prognosis.
34974534	8	32	from	expression	1298:1307	arg1	tumors					1350:1355	breast tumors	1343:1355	breast tumors	1343:1355	Clinically, high expression of OGT, MORC2, SNAIL, and CTGF in breast tumors is associated with poor patient prognosis.
34974534	8	33	theme	SNAIL	1324:1328	arg1	expression					1298:1307	high expression	1293:1307	high expression of OGT, MORC2, SNAIL, and CTGF in breast tumors	1293:1355	Clinically, high expression of OGT, MORC2, SNAIL, and CTGF in breast tumors is associated with poor patient prognosis.
34974534	4	34	theme	breast	616:621	arg1	cancer					623:628	MORC2-mediated breast cancer	601:628	MORC2-mediated breast cancer cell migration	601:643	Mutation of this site or pharmacological inhibition of OGT impairs MORC2-mediated breast cancer cell migration and invasion in vitro and lung colonization in vivo.
34974534	0	35	theme	MORC2	19:23	arg1	O-GlcNAcylation					0:14	O-GlcNAcylation	0:14	O-GlcNAcylation of MORC2 at threonine 556 by OGT	0:47	O-GlcNAcylation of MORC2 at threonine 556 by OGT couples TGF-β signaling to breast cancer progression.
34974534	6	36	theme	transcriptional	969:983	arg1	activation					985:994	transcriptional activation	969:994	transcriptional activation of TGF-β1 target genes connective tissue growth factor (CTGF) and snail family transcriptional repressor 1 (SNAIL)	969:1109	O-GlcNAcylated MORC2 is required for transcriptional activation of TGF-β1 target genes connective tissue growth factor (CTGF) and snail family transcriptional repressor 1 (SNAIL).
34974534	9	37	theme	breast	1509:1514	arg1	progression					1523:1533	breast cancer progression	1509:1533	breast cancer progression	1509:1533	Collectively, these findings uncover a previously unrecognized mechanistic role for MORC2 O-GlcNAcylation in breast cancer progression and provide evidence for targeting MORC2-dependent breast cancer through blocking its O-GlcNAcylation.
34974534	4	38	theme	lung	671:674	arg1	colonization					676:687	lung colonization	671:687	lung colonization	671:687	Mutation of this site or pharmacological inhibition of OGT impairs MORC2-mediated breast cancer cell migration and invasion in vitro and lung colonization in vivo.
34974534	1	39	theme	chromatin-remodeling	167:186	arg1	enzyme					188:193	a newly identified chromatin-remodeling enzyme	148:193	a newly identified chromatin-remodeling enzyme involved in DNA damage response and gene transcription	148:248	MORC family CW-type zinc finger 2 (MORC2) is a newly identified chromatin-remodeling enzyme involved in DNA damage response and gene transcription, and its dysregulation has been linked with Charcot-Marie-Tooth disease, neurodevelopmental disorder, and cancer.
34974534	1	39	theme	chromatin-remodeling	167:186	arg1	finger					128:133	MORC family CW-type zinc finger 2	103:135	MORC family CW-type zinc finger 2 (MORC2)	103:143	MORC family CW-type zinc finger 2 (MORC2) is a newly identified chromatin-remodeling enzyme involved in DNA damage response and gene transcription, and its dysregulation has been linked with Charcot-Marie-Tooth disease, neurodevelopmental disorder, and cancer.
34974534	5	40	theme	MORC2	755:759	arg1	O-GlcNAcylation					761:775	MORC2 O-GlcNAcylation	755:775	MORC2 O-GlcNAcylation	755:775	Moreover, transforming growth factor-β1 (TGF-β1) induces MORC2 O-GlcNAcylation through enhancing the stability of glutamine-fructose-6-phosphate aminotransferase (GFAT), the rate-limiting enzyme for producing the sugar donor for OGT.
34974534	8	41	theme	high	1293:1296	arg1	expression					1298:1307	high expression	1293:1307	high expression of OGT, MORC2, SNAIL, and CTGF in breast tumors	1293:1355	Clinically, high expression of OGT, MORC2, SNAIL, and CTGF in breast tumors is associated with poor patient prognosis.
34974534	8	42	theme	patient	1381:1387	arg1	prognosis					1389:1397	poor patient prognosis	1376:1397	poor patient prognosis	1376:1397	Clinically, high expression of OGT, MORC2, SNAIL, and CTGF in breast tumors is associated with poor patient prognosis.
34974534	9	43	theme	unrecognized	1450:1461	arg1	role					1475:1478	a previously unrecognized mechanistic role	1437:1478	a previously unrecognized mechanistic role for MORC2 O-GlcNAcylation in breast cancer progression	1437:1533	Collectively, these findings uncover a previously unrecognized mechanistic role for MORC2 O-GlcNAcylation in breast cancer progression and provide evidence for targeting MORC2-dependent breast cancer through blocking its O-GlcNAcylation.
34974534	4	44	theme	cell	630:633	arg1	migration					635:643	MORC2-mediated breast cancer cell migration	601:643	MORC2-mediated breast cancer cell migration	601:643	Mutation of this site or pharmacological inhibition of OGT impairs MORC2-mediated breast cancer cell migration and invasion in vitro and lung colonization in vivo.
34974534	6	45	theme	genes	1013:1017	arg1	activation					985:994	transcriptional activation	969:994	transcriptional activation of TGF-β1 target genes connective tissue growth factor (CTGF) and snail family transcriptional repressor 1 (SNAIL)	969:1109	O-GlcNAcylated MORC2 is required for transcriptional activation of TGF-β1 target genes connective tissue growth factor (CTGF) and snail family transcriptional repressor 1 (SNAIL).
34974534	5	46	theme	transforming	708:719	arg1	TGF-β1					739:744	TGF-β1	739:744	TGF-β1	739:744	Moreover, transforming growth factor-β1 (TGF-β1) induces MORC2 O-GlcNAcylation through enhancing the stability of glutamine-fructose-6-phosphate aminotransferase (GFAT), the rate-limiting enzyme for producing the sugar donor for OGT.
34974534	5	46	theme	transforming	708:719	arg1	factor-β1					728:736	transforming growth factor-β1	708:736	transforming growth factor-β1 (TGF-β1)	708:745	Moreover, transforming growth factor-β1 (TGF-β1) induces MORC2 O-GlcNAcylation through enhancing the stability of glutamine-fructose-6-phosphate aminotransferase (GFAT), the rate-limiting enzyme for producing the sugar donor for OGT.
34974534	6	47	theme	tissue	1030:1035	arg1	genes					1013:1017	TGF-β1 target genes connective tissue growth factor (CTGF) and snail family transcriptional repressor 1 (SNAIL)	999:1109	TGF-β1 target genes connective tissue growth factor (CTGF) and snail family transcriptional repressor 1 (SNAIL)	999:1109	O-GlcNAcylated MORC2 is required for transcriptional activation of TGF-β1 target genes connective tissue growth factor (CTGF) and snail family transcriptional repressor 1 (SNAIL).
34974534	6	47	theme	tissue	1030:1035	arg1	CTGF					1052:1055	CTGF	1052:1055	CTGF	1052:1055	O-GlcNAcylated MORC2 is required for transcriptional activation of TGF-β1 target genes connective tissue growth factor (CTGF) and snail family transcriptional repressor 1 (SNAIL).
34974534	6	47	theme	tissue	1030:1035	arg1	factor					1044:1049	connective tissue growth factor	1019:1049	connective tissue growth factor (CTGF)	1019:1056	O-GlcNAcylated MORC2 is required for transcriptional activation of TGF-β1 target genes connective tissue growth factor (CTGF) and snail family transcriptional repressor 1 (SNAIL).
34974534	4	48	theme	cancer	623:628	arg1	migration					635:643	MORC2-mediated breast cancer cell migration	601:643	MORC2-mediated breast cancer cell migration	601:643	Mutation of this site or pharmacological inhibition of OGT impairs MORC2-mediated breast cancer cell migration and invasion in vitro and lung colonization in vivo.
34974534	7	49	theme	observations	1132:1143	arg1	support					1115:1121	support	1115:1121	support of these observations	1115:1143	In support of these observations, knockdown of GFAT, SNAIL or CTGF compromises TGF-β1-induced, MORC2 O-GlcNAcylation-mediated breast cancer cell migration and invasion.
34974534	7	50	theme	TGF-β1-induced	1191:1204	arg1	cancer					1245:1250	TGF-β1-induced, MORC2 O-GlcNAcylation-mediated breast cancer	1191:1250	TGF-β1-induced, MORC2 O-GlcNAcylation-mediated breast cancer cell migration	1191:1265	In support of these observations, knockdown of GFAT, SNAIL or CTGF compromises TGF-β1-induced, MORC2 O-GlcNAcylation-mediated breast cancer cell migration and invasion.
34974534	7	51	theme	cancer	1245:1250	arg1	migration					1257:1265	TGF-β1-induced, MORC2 O-GlcNAcylation-mediated breast cancer cell migration	1191:1265	TGF-β1-induced, MORC2 O-GlcNAcylation-mediated breast cancer cell migration	1191:1265	In support of these observations, knockdown of GFAT, SNAIL or CTGF compromises TGF-β1-induced, MORC2 O-GlcNAcylation-mediated breast cancer cell migration and invasion.
34974534	1	52	theme	MORC	103:106	arg1	enzyme					188:193	a newly identified chromatin-remodeling enzyme	148:193	a newly identified chromatin-remodeling enzyme involved in DNA damage response and gene transcription	148:248	MORC family CW-type zinc finger 2 (MORC2) is a newly identified chromatin-remodeling enzyme involved in DNA damage response and gene transcription, and its dysregulation has been linked with Charcot-Marie-Tooth disease, neurodevelopmental disorder, and cancer.
34974534	1	52	theme	MORC	103:106	arg1	finger					128:133	MORC family CW-type zinc finger 2	103:135	MORC family CW-type zinc finger 2 (MORC2)	103:143	MORC family CW-type zinc finger 2 (MORC2) is a newly identified chromatin-remodeling enzyme involved in DNA damage response and gene transcription, and its dysregulation has been linked with Charcot-Marie-Tooth disease, neurodevelopmental disorder, and cancer.
34974534	1	52	theme	MORC	103:106	arg1	MORC2					138:142	MORC2	138:142	MORC2	138:142	MORC family CW-type zinc finger 2 (MORC2) is a newly identified chromatin-remodeling enzyme involved in DNA damage response and gene transcription, and its dysregulation has been linked with Charcot-Marie-Tooth disease, neurodevelopmental disorder, and cancer.
34974534	9	53	theme	cancer	1516:1521	arg1	progression					1523:1533	breast cancer progression	1509:1533	breast cancer progression	1509:1533	Collectively, these findings uncover a previously unrecognized mechanistic role for MORC2 O-GlcNAcylation in breast cancer progression and provide evidence for targeting MORC2-dependent breast cancer through blocking its O-GlcNAcylation.
34974534	1	54	theme	family	108:113	arg1	enzyme					188:193	a newly identified chromatin-remodeling enzyme	148:193	a newly identified chromatin-remodeling enzyme involved in DNA damage response and gene transcription	148:248	MORC family CW-type zinc finger 2 (MORC2) is a newly identified chromatin-remodeling enzyme involved in DNA damage response and gene transcription, and its dysregulation has been linked with Charcot-Marie-Tooth disease, neurodevelopmental disorder, and cancer.
34974534	1	54	theme	family	108:113	arg1	finger					128:133	MORC family CW-type zinc finger 2	103:135	MORC family CW-type zinc finger 2 (MORC2)	103:143	MORC family CW-type zinc finger 2 (MORC2) is a newly identified chromatin-remodeling enzyme involved in DNA damage response and gene transcription, and its dysregulation has been linked with Charcot-Marie-Tooth disease, neurodevelopmental disorder, and cancer.
34974534	1	54	theme	family	108:113	arg1	MORC2					138:142	MORC2	138:142	MORC2	138:142	MORC family CW-type zinc finger 2 (MORC2) is a newly identified chromatin-remodeling enzyme involved in DNA damage response and gene transcription, and its dysregulation has been linked with Charcot-Marie-Tooth disease, neurodevelopmental disorder, and cancer.
34974534	1	55	theme	Charcot-Marie-Tooth	294:312	arg1	disease					314:320	Charcot-Marie-Tooth disease	294:320	Charcot-Marie-Tooth disease	294:320	MORC family CW-type zinc finger 2 (MORC2) is a newly identified chromatin-remodeling enzyme involved in DNA damage response and gene transcription, and its dysregulation has been linked with Charcot-Marie-Tooth disease, neurodevelopmental disorder, and cancer.
34974534	7	56	dep	TGF-β1-induced	1191:1204	arg1	O-GlcNAcylation-mediated					1213:1236	O-GlcNAcylation-mediated	1213:1236	O-GlcNAcylation-mediated	1213:1236	In support of these observations, knockdown of GFAT, SNAIL or CTGF compromises TGF-β1-induced, MORC2 O-GlcNAcylation-mediated breast cancer cell migration and invasion.
34974534	8	57	theme	poor	1376:1379	arg1	prognosis					1389:1397	poor patient prognosis	1376:1397	poor patient prognosis	1376:1397	Clinically, high expression of OGT, MORC2, SNAIL, and CTGF in breast tumors is associated with poor patient prognosis.
34974534	1	58	theme	CW-type	115:121	arg1	enzyme					188:193	a newly identified chromatin-remodeling enzyme	148:193	a newly identified chromatin-remodeling enzyme involved in DNA damage response and gene transcription	148:248	MORC family CW-type zinc finger 2 (MORC2) is a newly identified chromatin-remodeling enzyme involved in DNA damage response and gene transcription, and its dysregulation has been linked with Charcot-Marie-Tooth disease, neurodevelopmental disorder, and cancer.
34974534	1	58	theme	CW-type	115:121	arg1	finger					128:133	MORC family CW-type zinc finger 2	103:135	MORC family CW-type zinc finger 2 (MORC2)	103:143	MORC family CW-type zinc finger 2 (MORC2) is a newly identified chromatin-remodeling enzyme involved in DNA damage response and gene transcription, and its dysregulation has been linked with Charcot-Marie-Tooth disease, neurodevelopmental disorder, and cancer.
34974534	1	58	theme	CW-type	115:121	arg1	MORC2					138:142	MORC2	138:142	MORC2	138:142	MORC family CW-type zinc finger 2 (MORC2) is a newly identified chromatin-remodeling enzyme involved in DNA damage response and gene transcription, and its dysregulation has been linked with Charcot-Marie-Tooth disease, neurodevelopmental disorder, and cancer.
34974534	9	59	from	role	1475:1478	arg1	progression					1523:1533	breast cancer progression	1509:1533	breast cancer progression	1509:1533	Collectively, these findings uncover a previously unrecognized mechanistic role for MORC2 O-GlcNAcylation in breast cancer progression and provide evidence for targeting MORC2-dependent breast cancer through blocking its O-GlcNAcylation.
34974534	1	60	theme	zinc	123:126	arg1	enzyme					188:193	a newly identified chromatin-remodeling enzyme	148:193	a newly identified chromatin-remodeling enzyme involved in DNA damage response and gene transcription	148:248	MORC family CW-type zinc finger 2 (MORC2) is a newly identified chromatin-remodeling enzyme involved in DNA damage response and gene transcription, and its dysregulation has been linked with Charcot-Marie-Tooth disease, neurodevelopmental disorder, and cancer.
34974534	1	60	theme	zinc	123:126	arg1	finger					128:133	MORC family CW-type zinc finger 2	103:135	MORC family CW-type zinc finger 2 (MORC2)	103:143	MORC family CW-type zinc finger 2 (MORC2) is a newly identified chromatin-remodeling enzyme involved in DNA damage response and gene transcription, and its dysregulation has been linked with Charcot-Marie-Tooth disease, neurodevelopmental disorder, and cancer.
34974534	1	60	theme	zinc	123:126	arg1	MORC2					138:142	MORC2	138:142	MORC2	138:142	MORC family CW-type zinc finger 2 (MORC2) is a newly identified chromatin-remodeling enzyme involved in DNA damage response and gene transcription, and its dysregulation has been linked with Charcot-Marie-Tooth disease, neurodevelopmental disorder, and cancer.
34974534	1	61	theme	DNA	207:209	arg1	damage					211:216	DNA damage	207:216	DNA damage response	207:225	MORC family CW-type zinc finger 2 (MORC2) is a newly identified chromatin-remodeling enzyme involved in DNA damage response and gene transcription, and its dysregulation has been linked with Charcot-Marie-Tooth disease, neurodevelopmental disorder, and cancer.
34974534	0	62	theme	TGF-β	57:61	arg1	signaling					63:71	TGF-β signaling	57:71	TGF-β signaling	57:71	O-GlcNAcylation of MORC2 at threonine 556 by OGT couples TGF-β signaling to breast cancer progression.
34974534	9	63	theme	MORC2	1484:1488	arg1	O-GlcNAcylation					1490:1504	MORC2 O-GlcNAcylation	1484:1504	MORC2 O-GlcNAcylation	1484:1504	Collectively, these findings uncover a previously unrecognized mechanistic role for MORC2 O-GlcNAcylation in breast cancer progression and provide evidence for targeting MORC2-dependent breast cancer through blocking its O-GlcNAcylation.
34974534	1	64	theme	identified	156:165	arg1	enzyme					188:193	a newly identified chromatin-remodeling enzyme	148:193	a newly identified chromatin-remodeling enzyme involved in DNA damage response and gene transcription	148:248	MORC family CW-type zinc finger 2 (MORC2) is a newly identified chromatin-remodeling enzyme involved in DNA damage response and gene transcription, and its dysregulation has been linked with Charcot-Marie-Tooth disease, neurodevelopmental disorder, and cancer.
34974534	1	64	theme	identified	156:165	arg1	finger					128:133	MORC family CW-type zinc finger 2	103:135	MORC family CW-type zinc finger 2 (MORC2)	103:143	MORC family CW-type zinc finger 2 (MORC2) is a newly identified chromatin-remodeling enzyme involved in DNA damage response and gene transcription, and its dysregulation has been linked with Charcot-Marie-Tooth disease, neurodevelopmental disorder, and cancer.
34974534	6	65	theme	repressor	1091:1099	arg1	genes					1013:1017	TGF-β1 target genes connective tissue growth factor (CTGF) and snail family transcriptional repressor 1 (SNAIL)	999:1109	TGF-β1 target genes connective tissue growth factor (CTGF) and snail family transcriptional repressor 1 (SNAIL)	999:1109	O-GlcNAcylated MORC2 is required for transcriptional activation of TGF-β1 target genes connective tissue growth factor (CTGF) and snail family transcriptional repressor 1 (SNAIL).
34974534	6	65	theme	repressor	1091:1099	arg1	SNAIL					1104:1108	snail family transcriptional repressor 1 (SNAIL)	1062:1109	snail family transcriptional repressor 1 (SNAIL)	1062:1109	O-GlcNAcylated MORC2 is required for transcriptional activation of TGF-β1 target genes connective tissue growth factor (CTGF) and snail family transcriptional repressor 1 (SNAIL).
34974534	1	66	theme	damage	211:216	arg1	response					218:225	DNA damage response	207:225	DNA damage response	207:225	MORC family CW-type zinc finger 2 (MORC2) is a newly identified chromatin-remodeling enzyme involved in DNA damage response and gene transcription, and its dysregulation has been linked with Charcot-Marie-Tooth disease, neurodevelopmental disorder, and cancer.
34974534	6	67	theme	target	1006:1011	arg1	genes					1013:1017	TGF-β1 target genes connective tissue growth factor (CTGF) and snail family transcriptional repressor 1 (SNAIL)	999:1109	TGF-β1 target genes connective tissue growth factor (CTGF) and snail family transcriptional repressor 1 (SNAIL)	999:1109	O-GlcNAcylated MORC2 is required for transcriptional activation of TGF-β1 target genes connective tissue growth factor (CTGF) and snail family transcriptional repressor 1 (SNAIL).
34974534	6	67	theme	target	1006:1011	arg1	factor					1044:1049	connective tissue growth factor	1019:1049	connective tissue growth factor (CTGF)	1019:1056	O-GlcNAcylated MORC2 is required for transcriptional activation of TGF-β1 target genes connective tissue growth factor (CTGF) and snail family transcriptional repressor 1 (SNAIL).
34974534	6	67	theme	target	1006:1011	arg1	SNAIL					1104:1108	snail family transcriptional repressor 1 (SNAIL)	1062:1109	snail family transcriptional repressor 1 (SNAIL)	1062:1109	O-GlcNAcylated MORC2 is required for transcriptional activation of TGF-β1 target genes connective tissue growth factor (CTGF) and snail family transcriptional repressor 1 (SNAIL).
34974534	7	68	theme	CTGF	1174:1177	arg1	knockdown					1146:1154	knockdown	1146:1154	knockdown of GFAT, SNAIL or CTGF	1146:1177	In support of these observations, knockdown of GFAT, SNAIL or CTGF compromises TGF-β1-induced, MORC2 O-GlcNAcylation-mediated breast cancer cell migration and invasion.
34974534	5	69	theme	glutamine-fructose-6-phosphate	812:841	arg1	GFAT					861:864	GFAT	861:864	GFAT	861:864	Moreover, transforming growth factor-β1 (TGF-β1) induces MORC2 O-GlcNAcylation through enhancing the stability of glutamine-fructose-6-phosphate aminotransferase (GFAT), the rate-limiting enzyme for producing the sugar donor for OGT.
34974534	5	69	theme	glutamine-fructose-6-phosphate	812:841	arg1	aminotransferase					843:858	glutamine-fructose-6-phosphate aminotransferase	812:858	glutamine-fructose-6-phosphate aminotransferase (GFAT)	812:865	Moreover, transforming growth factor-β1 (TGF-β1) induces MORC2 O-GlcNAcylation through enhancing the stability of glutamine-fructose-6-phosphate aminotransferase (GFAT), the rate-limiting enzyme for producing the sugar donor for OGT.
34974534	5	69	theme	glutamine-fructose-6-phosphate	812:841	arg1	enzyme					886:891	the rate-limiting enzyme	868:891	the rate-limiting enzyme for producing the sugar donor for OGT	868:929	Moreover, transforming growth factor-β1 (TGF-β1) induces MORC2 O-GlcNAcylation through enhancing the stability of glutamine-fructose-6-phosphate aminotransferase (GFAT), the rate-limiting enzyme for producing the sugar donor for OGT.
34974534	9	70	theme	MORC2-dependent	1570:1584	arg1	cancer					1593:1598	MORC2-dependent breast cancer	1570:1598	MORC2-dependent breast cancer	1570:1598	Collectively, these findings uncover a previously unrecognized mechanistic role for MORC2 O-GlcNAcylation in breast cancer progression and provide evidence for targeting MORC2-dependent breast cancer through blocking its O-GlcNAcylation.
34974534	8	71	theme	MORC2	1317:1321	arg1	expression					1298:1307	high expression	1293:1307	high expression of OGT, MORC2, SNAIL, and CTGF in breast tumors	1293:1355	Clinically, high expression of OGT, MORC2, SNAIL, and CTGF in breast tumors is associated with poor patient prognosis.
34974534	4	72	theme	OGT	589:591	arg1	Mutation					534:541	Mutation	534:541	Mutation of this site	534:554	Mutation of this site or pharmacological inhibition of OGT impairs MORC2-mediated breast cancer cell migration and invasion in vitro and lung colonization in vivo.
34974534	4	72	theme	OGT	589:591	arg1	inhibition					575:584	pharmacological inhibition	559:584	pharmacological inhibition of OGT	559:591	Mutation of this site or pharmacological inhibition of OGT impairs MORC2-mediated breast cancer cell migration and invasion in vitro and lung colonization in vivo.
25813380	10	0	with	set	1603:1605	arg1	potential					1651:1659	biomarker potential	1641:1659	biomarker potential in gastric cancer	1641:1677	The study provides a discovery strategy for aberrantly glycosylated O-glycoproteins and a set of O-glycoprotein candidates with biomarker potential in gastric cancer.
25813380	7	1	theme	healthy	1199:1205	arg1	individuals					1207:1217	healthy individuals	1199:1217	healthy individuals	1199:1217	We identified 37 O-glycoproteins in the pool of cancer sera, and only nine of these were also found in sera from healthy individuals.
25813380	7	2	from	individuals	1207:1217	arg1	sera					1189:1192	sera	1189:1192	sera from healthy individuals	1189:1217	We identified 37 O-glycoproteins in the pool of cancer sera, and only nine of these were also found in sera from healthy individuals.
25813380	4	3	theme	MKN45	615:619	arg1	AGS					610:612	AGS	610:612	AGS	610:612	Here, we used the COSMC KO "SimpleCell" (SC) strategy to characterize the O-glycoproteome of two gastric cancer SimpleCell lines (AGS, MKN45) as well as a gastric cell line (KATO III) which naturally expresses at least partially truncated O-glycans.
25813380	10	4	theme	discovery	1534:1542	arg1	strategy					1544:1551	a discovery strategy	1532:1551	a discovery strategy for aberrantly glycosylated O-glycoproteins and a set of O-glycoprotein candidates with biomarker potential in gastric cancer	1532:1677	The study provides a discovery strategy for aberrantly glycosylated O-glycoproteins and a set of O-glycoprotein candidates with biomarker potential in gastric cancer.
25813380	2	5	theme	biomarkers	329:338	arg1	glycoforms					288:297	cancer-associated aberrant glycoforms	261:297	cancer-associated aberrant glycoforms of circulating O-glycoprotein biomarkers	261:338	We have recently shown that selective detection of cancer-associated aberrant glycoforms of circulating O-glycoprotein biomarkers can increase specificity of cancer biomarker assays.
25813380	9	6	theme	ligation	1407:1414	arg1	assay					1416:1420	A proximity ligation assay	1395:1420	A proximity ligation assay	1395:1420	A proximity ligation assay was used to show that CD44 was expressed with the STn glycoform in gastric cancer tissues.
25813380	2	7	gly	O-glycoprotein	314:327	arg1	O-glycoprotein					314:327	circulating O-glycoprotein biomarkers	302:338	circulating O-glycoprotein biomarkers	302:338	We have recently shown that selective detection of cancer-associated aberrant glycoforms of circulating O-glycoprotein biomarkers can increase specificity of cancer biomarker assays.
25813380	2	8	theme	circulating	302:312	arg1	biomarkers					329:338	circulating O-glycoprotein biomarkers	302:338	circulating O-glycoprotein biomarkers	302:338	We have recently shown that selective detection of cancer-associated aberrant glycoforms of circulating O-glycoprotein biomarkers can increase specificity of cancer biomarker assays.
25813380	1	9	theme	prognostic	189:198	arg1	purposes					200:207	diagnostic and prognostic purposes	174:207	diagnostic and prognostic purposes	174:207	Circulating O-glycoproteins shed from cancer cells represent important serum biomarkers for diagnostic and prognostic purposes.
25813380	5	10	gly	O-glycoproteins	841:855	arg1	O-glycoproteins					841:855	a total 47 O-glycoproteins and 73 O-glycosites	830:875	O-glycoproteins	841:855	Overall, we identified 499 O-glycoproteins and 1236 O-glycosites in gastric cancer SimpleCells, and a total 47 O-glycoproteins and 73 O-glycosites in the KATO III cell line.
25813380	10	11	theme	glycosylated	1568:1579	arg1	O-glycoproteins					1581:1595	aberrantly glycosylated O-glycoproteins	1557:1595	aberrantly glycosylated O-glycoproteins	1557:1595	The study provides a discovery strategy for aberrantly glycosylated O-glycoproteins and a set of O-glycoprotein candidates with biomarker potential in gastric cancer.
25813380	4	12	theme	gastric	635:641	arg1	KATO					654:657	KATO	654:657	KATO	654:657	Here, we used the COSMC KO "SimpleCell" (SC) strategy to characterize the O-glycoproteome of two gastric cancer SimpleCell lines (AGS, MKN45) as well as a gastric cell line (KATO III) which naturally expresses at least partially truncated O-glycans.
25813380	4	12	theme	gastric	635:641	arg1	line					648:651	a gastric cell line	633:651	two gastric cancer SimpleCell lines (AGS, MKN45) as well as a gastric cell line (KATO III) which naturally expresses at least partially truncated O-glycans	573:727	Here, we used the COSMC KO "SimpleCell" (SC) strategy to characterize the O-glycoproteome of two gastric cancer SimpleCell lines (AGS, MKN45) as well as a gastric cell line (KATO III) which naturally expresses at least partially truncated O-glycans.
25813380	5	13	theme	total	832:836	arg1	O-glycoproteins					841:855	a total 47 O-glycoproteins and 73 O-glycosites	830:875	O-glycoproteins	841:855	Overall, we identified 499 O-glycoproteins and 1236 O-glycosites in gastric cancer SimpleCells, and a total 47 O-glycoproteins and 73 O-glycosites in the KATO III cell line.
25813380	4	14	theme	line	648:651	arg1	O-glycoproteome					554:568	the O-glycoproteome	550:568	the O-glycoproteome of two gastric cancer SimpleCell lines (AGS, MKN45) as well as a gastric cell line (KATO III) which naturally expresses at least partially truncated O-glycans	550:727	Here, we used the COSMC KO "SimpleCell" (SC) strategy to characterize the O-glycoproteome of two gastric cancer SimpleCell lines (AGS, MKN45) as well as a gastric cell line (KATO III) which naturally expresses at least partially truncated O-glycans.
25813380	6	15	theme	glycoproteomic	925:938	arg1	strategy					940:947	the glycoproteomic strategy	921:947	the glycoproteomic strategy to apply it to pools of sera from gastric cancer and healthy individuals to identify circulating O-glycoproteins with the STn glycoform	921:1083	We next modified the glycoproteomic strategy to apply it to pools of sera from gastric cancer and healthy individuals to identify circulating O-glycoproteins with the STn glycoform.
25813380	4	16	theme	KO	504:505	arg1	SC					521:522	SC	521:522	SC	521:522	Here, we used the COSMC KO "SimpleCell" (SC) strategy to characterize the O-glycoproteome of two gastric cancer SimpleCell lines (AGS, MKN45) as well as a gastric cell line (KATO III) which naturally expresses at least partially truncated O-glycans.
25813380	4	16	theme	KO	504:505	arg1	"					518:518	COSMC KO "SimpleCell"	498:518	the COSMC KO "SimpleCell" (SC) strategy	494:532	Here, we used the COSMC KO "SimpleCell" (SC) strategy to characterize the O-glycoproteome of two gastric cancer SimpleCell lines (AGS, MKN45) as well as a gastric cell line (KATO III) which naturally expresses at least partially truncated O-glycans.
25813380	5	17	from	O-glycoproteins	757:771	arg1	SimpleCells					813:823	gastric cancer SimpleCells	798:823	gastric cancer SimpleCells	798:823	Overall, we identified 499 O-glycoproteins and 1236 O-glycosites in gastric cancer SimpleCells, and a total 47 O-glycoproteins and 73 O-glycosites in the KATO III cell line.
25813380	5	17	from	O-glycoproteins	757:771	arg1	line					898:901	the KATO III cell line	880:901	the KATO III cell line	880:901	Overall, we identified 499 O-glycoproteins and 1236 O-glycosites in gastric cancer SimpleCells, and a total 47 O-glycoproteins and 73 O-glycosites in the KATO III cell line.
25813380	8	18	gly	O-glycoprotein	1245:1258	arg1	O-glycoprotein					1245:1258	identified candidate O-glycoprotein biomarkers	1224:1269	Two identified candidate O-glycoprotein biomarkers (CD44 and GalNAc-T5) circulating with the STn glycoform	1220:1325	Two identified candidate O-glycoprotein biomarkers (CD44 and GalNAc-T5) circulating with the STn glycoform were further validated as being expressed in gastric cancer tissue.
25813380	2	19	theme	glycoforms	288:297	arg1	detection					248:256	selective detection	238:256	selective detection of cancer-associated aberrant glycoforms of circulating O-glycoprotein biomarkers	238:338	We have recently shown that selective detection of cancer-associated aberrant glycoforms of circulating O-glycoprotein biomarkers can increase specificity of cancer biomarker assays.
25813380	5	20	from	O-glycosites	864:875	arg1	SimpleCells					813:823	gastric cancer SimpleCells	798:823	gastric cancer SimpleCells	798:823	Overall, we identified 499 O-glycoproteins and 1236 O-glycosites in gastric cancer SimpleCells, and a total 47 O-glycoproteins and 73 O-glycosites in the KATO III cell line.
25813380	5	20	from	O-glycosites	864:875	arg1	line					898:901	the KATO III cell line	880:901	the KATO III cell line	880:901	Overall, we identified 499 O-glycoproteins and 1236 O-glycosites in gastric cancer SimpleCells, and a total 47 O-glycoproteins and 73 O-glycosites in the KATO III cell line.
25813380	1	21	theme	important	143:151	arg1	biomarkers					159:168	important serum biomarkers	143:168	important serum biomarkers for diagnostic and prognostic purposes	143:207	Circulating O-glycoproteins shed from cancer cells represent important serum biomarkers for diagnostic and prognostic purposes.
25813380	2	22	theme	cancer-associated	261:277	arg1	glycoforms					288:297	cancer-associated aberrant glycoforms	261:297	cancer-associated aberrant glycoforms of circulating O-glycoprotein biomarkers	261:338	We have recently shown that selective detection of cancer-associated aberrant glycoforms of circulating O-glycoprotein biomarkers can increase specificity of cancer biomarker assays.
25813380	5	23	theme	KATO	884:887	arg1	line					898:901	the KATO III cell line	880:901	the KATO III cell line	880:901	Overall, we identified 499 O-glycoproteins and 1236 O-glycosites in gastric cancer SimpleCells, and a total 47 O-glycoproteins and 73 O-glycosites in the KATO III cell line.
25813380	6	24	theme	gastric	983:989	arg1	cancer					991:996	gastric cancer	983:996	gastric cancer	983:996	We next modified the glycoproteomic strategy to apply it to pools of sera from gastric cancer and healthy individuals to identify circulating O-glycoproteins with the STn glycoform.
25813380	6	25	from	cancer	991:996	arg1	sera					973:976	sera	973:976	sera from gastric cancer	973:996	We next modified the glycoproteomic strategy to apply it to pools of sera from gastric cancer and healthy individuals to identify circulating O-glycoproteins with the STn glycoform.
25813380	6	25	from	cancer	991:996	arg1	pools					964:968	pools	964:968	pools of sera from gastric cancer	964:996	We next modified the glycoproteomic strategy to apply it to pools of sera from gastric cancer and healthy individuals to identify circulating O-glycoproteins with the STn glycoform.
25813380	10	26	gly	O-glycoprotein	1610:1623	arg1	O-glycoprotein					1610:1623	O-glycoprotein candidates	1610:1634	O-glycoprotein candidates	1610:1634	The study provides a discovery strategy for aberrantly glycosylated O-glycoproteins and a set of O-glycoprotein candidates with biomarker potential in gastric cancer.
25813380	1	27	theme	diagnostic	174:183	arg1	purposes					200:207	diagnostic and prognostic purposes	174:207	diagnostic and prognostic purposes	174:207	Circulating O-glycoproteins shed from cancer cells represent important serum biomarkers for diagnostic and prognostic purposes.
25813380	6	28	theme	sera	973:976	arg1	pools					964:968	pools	964:968	pools of sera from gastric cancer	964:996	We next modified the glycoproteomic strategy to apply it to pools of sera from gastric cancer and healthy individuals to identify circulating O-glycoproteins with the STn glycoform.
25813380	3	29	theme	current	406:412	arg1	knowledge					414:422	the current knowledge	402:422	the current knowledge of secreted and circulating O-glycoproteins	402:466	However, the current knowledge of secreted and circulating O-glycoproteins is limited.
25813380	6	30	gly	glycoform	1075:1083	arg1	STn					1071:1073	the STn glycoform	1067:1083	the STn glycoform	1067:1083	We next modified the glycoproteomic strategy to apply it to pools of sera from gastric cancer and healthy individuals to identify circulating O-glycoproteins with the STn glycoform.
25813380	4	31	used	used	489:492	arg2	we					486:487	we	486:487	we	486:487	Here, we used the COSMC KO "SimpleCell" (SC) strategy to characterize the O-glycoproteome of two gastric cancer SimpleCell lines (AGS, MKN45) as well as a gastric cell line (KATO III) which naturally expresses at least partially truncated O-glycans.
25813380	4	32	dep	lines	603:607	arg1	AGS					610:612	AGS	610:612	AGS	610:612	Here, we used the COSMC KO "SimpleCell" (SC) strategy to characterize the O-glycoproteome of two gastric cancer SimpleCell lines (AGS, MKN45) as well as a gastric cell line (KATO III) which naturally expresses at least partially truncated O-glycans.
25813380	3	33	gly	O-glycoproteins	452:466	arg1	O-glycoproteins					452:466	secreted and circulating O-glycoproteins	427:466	secreted and circulating O-glycoproteins	427:466	However, the current knowledge of secreted and circulating O-glycoproteins is limited.
25813380	9	34	theme	STn	1472:1474	arg1	glycoform					1476:1484	the STn glycoform	1468:1484	the STn glycoform in gastric cancer tissues	1468:1510	A proximity ligation assay was used to show that CD44 was expressed with the STn glycoform in gastric cancer tissues.
25813380	4	35	theme	SimpleCell	508:517	arg1	SC					521:522	SC	521:522	SC	521:522	Here, we used the COSMC KO "SimpleCell" (SC) strategy to characterize the O-glycoproteome of two gastric cancer SimpleCell lines (AGS, MKN45) as well as a gastric cell line (KATO III) which naturally expresses at least partially truncated O-glycans.
25813380	4	35	theme	SimpleCell	508:517	arg1	"					518:518	COSMC KO "SimpleCell"	498:518	the COSMC KO "SimpleCell" (SC) strategy	494:532	Here, we used the COSMC KO "SimpleCell" (SC) strategy to characterize the O-glycoproteome of two gastric cancer SimpleCell lines (AGS, MKN45) as well as a gastric cell line (KATO III) which naturally expresses at least partially truncated O-glycans.
25813380	10	36	theme	biomarker	1641:1649	arg1	potential					1651:1659	biomarker potential	1641:1659	biomarker potential in gastric cancer	1641:1677	The study provides a discovery strategy for aberrantly glycosylated O-glycoproteins and a set of O-glycoprotein candidates with biomarker potential in gastric cancer.
25813380	7	37	theme	these	1164:1168	arg1	these					1164:1168	these	1164:1168	these	1164:1168	We identified 37 O-glycoproteins in the pool of cancer sera, and only nine of these were also found in sera from healthy individuals.
25813380	7	37	theme	these	1164:1168	arg1	nine					1156:1159	nine	1156:1159	nine	1156:1159	We identified 37 O-glycoproteins in the pool of cancer sera, and only nine of these were also found in sera from healthy individuals.
25813380	0	38	theme	cancer	39:44	arg1	lines					51:55	gastric cancer cell lines	31:55	gastric cancer cell lines	31:55	Probing the O-glycoproteome of gastric cancer cell lines for biomarker discovery.
25813380	10	39	gly	O-glycoproteins	1581:1595	arg1	O-glycoproteins					1581:1595	aberrantly glycosylated O-glycoproteins	1557:1595	aberrantly glycosylated O-glycoproteins	1557:1595	The study provides a discovery strategy for aberrantly glycosylated O-glycoproteins and a set of O-glycoprotein candidates with biomarker potential in gastric cancer.
25813380	10	40	theme	candidates	1625:1634	arg1	O-glycoproteins					1581:1595	aberrantly glycosylated O-glycoproteins	1557:1595	aberrantly glycosylated O-glycoproteins	1557:1595	The study provides a discovery strategy for aberrantly glycosylated O-glycoproteins and a set of O-glycoprotein candidates with biomarker potential in gastric cancer.
25813380	10	40	theme	candidates	1625:1634	arg1	set					1603:1605	a set	1601:1605	a set of O-glycoprotein candidates with biomarker potential in gastric cancer	1601:1677	The study provides a discovery strategy for aberrantly glycosylated O-glycoproteins and a set of O-glycoprotein candidates with biomarker potential in gastric cancer.
25813380	10	40	theme	candidates	1625:1634	arg1	candidates					1625:1634	O-glycoprotein candidates	1610:1634	O-glycoprotein candidates	1610:1634	The study provides a discovery strategy for aberrantly glycosylated O-glycoproteins and a set of O-glycoprotein candidates with biomarker potential in gastric cancer.
25813380	4	41	theme	gastric	577:583	arg1	lines					603:607	two gastric cancer SimpleCell lines	573:607	two gastric cancer SimpleCell lines (AGS, MKN45) as well as a gastric cell line (KATO III) which naturally expresses at least partially truncated O-glycans	573:727	Here, we used the COSMC KO "SimpleCell" (SC) strategy to characterize the O-glycoproteome of two gastric cancer SimpleCell lines (AGS, MKN45) as well as a gastric cell line (KATO III) which naturally expresses at least partially truncated O-glycans.
25813380	4	42	theme	SimpleCell	592:601	arg1	lines					603:607	two gastric cancer SimpleCell lines	573:607	two gastric cancer SimpleCell lines (AGS, MKN45) as well as a gastric cell line (KATO III) which naturally expresses at least partially truncated O-glycans	573:727	Here, we used the COSMC KO "SimpleCell" (SC) strategy to characterize the O-glycoproteome of two gastric cancer SimpleCell lines (AGS, MKN45) as well as a gastric cell line (KATO III) which naturally expresses at least partially truncated O-glycans.
25813380	8	43	theme	gastric	1372:1378	arg1	tissue					1387:1392	gastric cancer tissue	1372:1392	gastric cancer tissue	1372:1392	Two identified candidate O-glycoprotein biomarkers (CD44 and GalNAc-T5) circulating with the STn glycoform were further validated as being expressed in gastric cancer tissue.
25813380	0	44	theme	gastric	31:37	arg1	lines					51:55	gastric cancer cell lines	31:55	gastric cancer cell lines	31:55	Probing the O-glycoproteome of gastric cancer cell lines for biomarker discovery.
25813380	7	45	theme	sera	1141:1144	arg1	pool					1126:1129	the pool	1122:1129	the pool of cancer sera	1122:1144	We identified 37 O-glycoproteins in the pool of cancer sera, and only nine of these were also found in sera from healthy individuals.
25813380	3	46	theme	O-glycoproteins	452:466	arg1	knowledge					414:422	the current knowledge	402:422	the current knowledge of secreted and circulating O-glycoproteins	402:466	However, the current knowledge of secreted and circulating O-glycoproteins is limited.
25813380	5	47	theme	gastric	798:804	arg1	SimpleCells					813:823	gastric cancer SimpleCells	798:823	gastric cancer SimpleCells	798:823	Overall, we identified 499 O-glycoproteins and 1236 O-glycosites in gastric cancer SimpleCells, and a total 47 O-glycoproteins and 73 O-glycosites in the KATO III cell line.
25813380	10	48	with	O-glycoproteins	1581:1595	arg1	potential					1651:1659	biomarker potential	1641:1659	biomarker potential in gastric cancer	1641:1677	The study provides a discovery strategy for aberrantly glycosylated O-glycoproteins and a set of O-glycoprotein candidates with biomarker potential in gastric cancer.
25813380	6	49	gly	O-glycoproteins	1046:1060	arg1	O-glycoproteins					1046:1060	circulating O-glycoproteins	1034:1060	circulating O-glycoproteins with the STn glycoform	1034:1083	We next modified the glycoproteomic strategy to apply it to pools of sera from gastric cancer and healthy individuals to identify circulating O-glycoproteins with the STn glycoform.
25813380	5	50	gly	O-glycosites	782:793	arg2	O-glycosites					782:793	1236 O-glycosites	777:793	1236 O-glycosites	777:793	Overall, we identified 499 O-glycoproteins and 1236 O-glycosites in gastric cancer SimpleCells, and a total 47 O-glycoproteins and 73 O-glycosites in the KATO III cell line.
25813380	2	51	theme	assays	385:390	arg1	specificity					353:363	specificity	353:363	specificity of cancer biomarker assays	353:390	We have recently shown that selective detection of cancer-associated aberrant glycoforms of circulating O-glycoprotein biomarkers can increase specificity of cancer biomarker assays.
25813380	7	52	located	found	1180:1184	arg2	nine					1156:1159	nine	1156:1159	nine	1156:1159	We identified 37 O-glycoproteins in the pool of cancer sera, and only nine of these were also found in sera from healthy individuals.
25813380	7	52	located	found	1180:1184	arg1	sera					1189:1192	sera	1189:1192	sera from healthy individuals	1189:1217	We identified 37 O-glycoproteins in the pool of cancer sera, and only nine of these were also found in sera from healthy individuals.
25813380	7	52	located	found	1180:1184	arg2	these					1164:1168	these	1164:1168	these	1164:1168	We identified 37 O-glycoproteins in the pool of cancer sera, and only nine of these were also found in sera from healthy individuals.
25813380	9	53	theme	proximity	1397:1405	arg1	assay					1416:1420	A proximity ligation assay	1395:1420	A proximity ligation assay	1395:1420	A proximity ligation assay was used to show that CD44 was expressed with the STn glycoform in gastric cancer tissues.
25813380	5	54	gly	O-glycosites	864:875	arg2	O-glycosites					864:875	a total 47 O-glycoproteins and 73 O-glycosites	830:875	O-glycosites	864:875	Overall, we identified 499 O-glycoproteins and 1236 O-glycosites in gastric cancer SimpleCells, and a total 47 O-glycoproteins and 73 O-glycosites in the KATO III cell line.
25813380	9	55	from	glycoform	1476:1484	arg1	tissues					1504:1510	gastric cancer tissues	1489:1510	gastric cancer tissues	1489:1510	A proximity ligation assay was used to show that CD44 was expressed with the STn glycoform in gastric cancer tissues.
25813380	2	56	theme	O-glycoprotein	314:327	arg1	biomarkers					329:338	circulating O-glycoprotein biomarkers	302:338	circulating O-glycoprotein biomarkers	302:338	We have recently shown that selective detection of cancer-associated aberrant glycoforms of circulating O-glycoprotein biomarkers can increase specificity of cancer biomarker assays.
25813380	0	57	theme	cell	46:49	arg1	lines					51:55	gastric cancer cell lines	31:55	gastric cancer cell lines	31:55	Probing the O-glycoproteome of gastric cancer cell lines for biomarker discovery.
25813380	2	58	gly	glycoforms	288:297	arg1	biomarkers					329:338	circulating O-glycoprotein biomarkers	302:338	circulating O-glycoprotein biomarkers	302:338	We have recently shown that selective detection of cancer-associated aberrant glycoforms of circulating O-glycoprotein biomarkers can increase specificity of cancer biomarker assays.
25813380	2	59	theme	cancer	368:373	arg1	assays					385:390	cancer biomarker assays	368:390	cancer biomarker assays	368:390	We have recently shown that selective detection of cancer-associated aberrant glycoforms of circulating O-glycoprotein biomarkers can increase specificity of cancer biomarker assays.
25813380	4	60	theme	COSMC	498:502	arg1	SC					521:522	SC	521:522	SC	521:522	Here, we used the COSMC KO "SimpleCell" (SC) strategy to characterize the O-glycoproteome of two gastric cancer SimpleCell lines (AGS, MKN45) as well as a gastric cell line (KATO III) which naturally expresses at least partially truncated O-glycans.
25813380	4	60	theme	COSMC	498:502	arg1	"					518:518	COSMC KO "SimpleCell"	498:518	the COSMC KO "SimpleCell" (SC) strategy	494:532	Here, we used the COSMC KO "SimpleCell" (SC) strategy to characterize the O-glycoproteome of two gastric cancer SimpleCell lines (AGS, MKN45) as well as a gastric cell line (KATO III) which naturally expresses at least partially truncated O-glycans.
25813380	5	61	theme	cell	893:896	arg1	line					898:901	the KATO III cell line	880:901	the KATO III cell line	880:901	Overall, we identified 499 O-glycoproteins and 1236 O-glycosites in gastric cancer SimpleCells, and a total 47 O-glycoproteins and 73 O-glycosites in the KATO III cell line.
25813380	9	62	theme	cancer	1497:1502	arg1	tissues					1504:1510	gastric cancer tissues	1489:1510	gastric cancer tissues	1489:1510	A proximity ligation assay was used to show that CD44 was expressed with the STn glycoform in gastric cancer tissues.
25813380	8	63	theme	identified	1224:1233	arg1	GalNAc-T5					1281:1289	GalNAc-T5	1281:1289	GalNAc-T5	1281:1289	Two identified candidate O-glycoprotein biomarkers (CD44 and GalNAc-T5) circulating with the STn glycoform were further validated as being expressed in gastric cancer tissue.
25813380	8	63	theme	identified	1224:1233	arg1	CD44					1272:1275	CD44	1272:1275	CD44	1272:1275	Two identified candidate O-glycoprotein biomarkers (CD44 and GalNAc-T5) circulating with the STn glycoform were further validated as being expressed in gastric cancer tissue.
25813380	8	63	theme	identified	1224:1233	arg1	biomarkers					1260:1269	identified candidate O-glycoprotein biomarkers	1224:1269	Two identified candidate O-glycoprotein biomarkers (CD44 and GalNAc-T5) circulating with the STn glycoform	1220:1325	Two identified candidate O-glycoprotein biomarkers (CD44 and GalNAc-T5) circulating with the STn glycoform were further validated as being expressed in gastric cancer tissue.
25813380	6	64	dep	strategy	940:947	arg1	identify					1025:1032	identify	1025:1032	to identify circulating O-glycoproteins with the STn glycoform	1022:1083	We next modified the glycoproteomic strategy to apply it to pools of sera from gastric cancer and healthy individuals to identify circulating O-glycoproteins with the STn glycoform.
25813380	6	64	dep	strategy	940:947	arg1	apply					952:956	apply	952:956	to apply it to pools of sera from gastric cancer	949:996	We next modified the glycoproteomic strategy to apply it to pools of sera from gastric cancer and healthy individuals to identify circulating O-glycoproteins with the STn glycoform.
25813380	4	65	theme	cell	643:646	arg1	KATO					654:657	KATO	654:657	KATO	654:657	Here, we used the COSMC KO "SimpleCell" (SC) strategy to characterize the O-glycoproteome of two gastric cancer SimpleCell lines (AGS, MKN45) as well as a gastric cell line (KATO III) which naturally expresses at least partially truncated O-glycans.
25813380	4	65	theme	cell	643:646	arg1	line					648:651	a gastric cell line	633:651	two gastric cancer SimpleCell lines (AGS, MKN45) as well as a gastric cell line (KATO III) which naturally expresses at least partially truncated O-glycans	573:727	Here, we used the COSMC KO "SimpleCell" (SC) strategy to characterize the O-glycoproteome of two gastric cancer SimpleCell lines (AGS, MKN45) as well as a gastric cell line (KATO III) which naturally expresses at least partially truncated O-glycans.
25813380	2	66	theme	selective	238:246	arg1	detection					248:256	selective detection	238:256	selective detection of cancer-associated aberrant glycoforms of circulating O-glycoprotein biomarkers	238:338	We have recently shown that selective detection of cancer-associated aberrant glycoforms of circulating O-glycoprotein biomarkers can increase specificity of cancer biomarker assays.
25813380	5	67	from	O-glycoproteins	841:855	arg1	SimpleCells					813:823	gastric cancer SimpleCells	798:823	gastric cancer SimpleCells	798:823	Overall, we identified 499 O-glycoproteins and 1236 O-glycosites in gastric cancer SimpleCells, and a total 47 O-glycoproteins and 73 O-glycosites in the KATO III cell line.
25813380	5	67	from	O-glycoproteins	841:855	arg1	line					898:901	the KATO III cell line	880:901	the KATO III cell line	880:901	Overall, we identified 499 O-glycoproteins and 1236 O-glycosites in gastric cancer SimpleCells, and a total 47 O-glycoproteins and 73 O-glycosites in the KATO III cell line.
25813380	1	68	theme	cancer	120:125	arg1	cells					127:131	cancer cells	120:131	cancer cells	120:131	Circulating O-glycoproteins shed from cancer cells represent important serum biomarkers for diagnostic and prognostic purposes.
25813380	6	69	theme	healthy	1002:1008	arg1	individuals					1010:1020	healthy individuals	1002:1020	healthy individuals	1002:1020	We next modified the glycoproteomic strategy to apply it to pools of sera from gastric cancer and healthy individuals to identify circulating O-glycoproteins with the STn glycoform.
25813380	4	70	theme	truncated	709:717	arg1	O-glycans					719:727	at least partially truncated O-glycans	690:727	at least partially truncated O-glycans	690:727	Here, we used the COSMC KO "SimpleCell" (SC) strategy to characterize the O-glycoproteome of two gastric cancer SimpleCell lines (AGS, MKN45) as well as a gastric cell line (KATO III) which naturally expresses at least partially truncated O-glycans.
25813380	7	71	gly	O-glycoproteins	1103:1117	arg1	O-glycoproteins					1103:1117	37 O-glycoproteins	1100:1117	37 O-glycoproteins	1100:1117	We identified 37 O-glycoproteins in the pool of cancer sera, and only nine of these were also found in sera from healthy individuals.
25813380	0	72	theme	biomarker	61:69	arg1	discovery					71:79	biomarker discovery	61:79	biomarker discovery	61:79	Probing the O-glycoproteome of gastric cancer cell lines for biomarker discovery.
25813380	2	73	theme	aberrant	279:286	arg1	glycoforms					288:297	cancer-associated aberrant glycoforms	261:297	cancer-associated aberrant glycoforms of circulating O-glycoprotein biomarkers	261:338	We have recently shown that selective detection of cancer-associated aberrant glycoforms of circulating O-glycoprotein biomarkers can increase specificity of cancer biomarker assays.
25813380	8	74	theme	candidate	1235:1243	arg1	GalNAc-T5					1281:1289	GalNAc-T5	1281:1289	GalNAc-T5	1281:1289	Two identified candidate O-glycoprotein biomarkers (CD44 and GalNAc-T5) circulating with the STn glycoform were further validated as being expressed in gastric cancer tissue.
25813380	8	74	theme	candidate	1235:1243	arg1	CD44					1272:1275	CD44	1272:1275	CD44	1272:1275	Two identified candidate O-glycoprotein biomarkers (CD44 and GalNAc-T5) circulating with the STn glycoform were further validated as being expressed in gastric cancer tissue.
25813380	8	74	theme	candidate	1235:1243	arg1	biomarkers					1260:1269	identified candidate O-glycoprotein biomarkers	1224:1269	Two identified candidate O-glycoprotein biomarkers (CD44 and GalNAc-T5) circulating with the STn glycoform	1220:1325	Two identified candidate O-glycoprotein biomarkers (CD44 and GalNAc-T5) circulating with the STn glycoform were further validated as being expressed in gastric cancer tissue.
25813380	1	75	theme	serum	153:157	arg1	biomarkers					159:168	important serum biomarkers	143:168	important serum biomarkers for diagnostic and prognostic purposes	143:207	Circulating O-glycoproteins shed from cancer cells represent important serum biomarkers for diagnostic and prognostic purposes.
25813380	9	76	theme	gastric	1489:1495	arg1	tissues					1504:1510	gastric cancer tissues	1489:1510	gastric cancer tissues	1489:1510	A proximity ligation assay was used to show that CD44 was expressed with the STn glycoform in gastric cancer tissues.
25813380	1	77	gly	O-glycoproteins	94:108	arg1	O-glycoproteins					94:108	Circulating O-glycoproteins	82:108	Circulating O-glycoproteins shed from cancer cells	82:131	Circulating O-glycoproteins shed from cancer cells represent important serum biomarkers for diagnostic and prognostic purposes.
25813380	5	78	from	O-glycosites	782:793	arg1	SimpleCells					813:823	gastric cancer SimpleCells	798:823	gastric cancer SimpleCells	798:823	Overall, we identified 499 O-glycoproteins and 1236 O-glycosites in gastric cancer SimpleCells, and a total 47 O-glycoproteins and 73 O-glycosites in the KATO III cell line.
25813380	5	78	from	O-glycosites	782:793	arg1	line					898:901	the KATO III cell line	880:901	the KATO III cell line	880:901	Overall, we identified 499 O-glycoproteins and 1236 O-glycosites in gastric cancer SimpleCells, and a total 47 O-glycoproteins and 73 O-glycosites in the KATO III cell line.
25813380	8	79	dep	biomarkers	1260:1269	arg1	GalNAc-T5					1281:1289	GalNAc-T5	1281:1289	GalNAc-T5	1281:1289	Two identified candidate O-glycoprotein biomarkers (CD44 and GalNAc-T5) circulating with the STn glycoform were further validated as being expressed in gastric cancer tissue.
25813380	8	79	dep	biomarkers	1260:1269	arg1	CD44					1272:1275	CD44	1272:1275	CD44	1272:1275	Two identified candidate O-glycoprotein biomarkers (CD44 and GalNAc-T5) circulating with the STn glycoform were further validated as being expressed in gastric cancer tissue.
25813380	8	79	dep	biomarkers	1260:1269	arg1	biomarkers					1260:1269	identified candidate O-glycoprotein biomarkers	1224:1269	Two identified candidate O-glycoprotein biomarkers (CD44 and GalNAc-T5) circulating with the STn glycoform	1220:1325	Two identified candidate O-glycoprotein biomarkers (CD44 and GalNAc-T5) circulating with the STn glycoform were further validated as being expressed in gastric cancer tissue.
25813380	4	80	theme	"	518:518	arg1	strategy					525:532	the COSMC KO "SimpleCell" (SC) strategy	494:532	the COSMC KO "SimpleCell" (SC) strategy	494:532	Here, we used the COSMC KO "SimpleCell" (SC) strategy to characterize the O-glycoproteome of two gastric cancer SimpleCell lines (AGS, MKN45) as well as a gastric cell line (KATO III) which naturally expresses at least partially truncated O-glycans.
25813380	8	81	theme	STn	1313:1315	arg1	glycoform					1317:1325	the STn glycoform	1309:1325	the STn glycoform	1309:1325	Two identified candidate O-glycoprotein biomarkers (CD44 and GalNAc-T5) circulating with the STn glycoform were further validated as being expressed in gastric cancer tissue.
25813380	6	82	theme	STn	1071:1073	arg1	glycoform					1075:1083	the STn glycoform	1067:1083	the STn glycoform	1067:1083	We next modified the glycoproteomic strategy to apply it to pools of sera from gastric cancer and healthy individuals to identify circulating O-glycoproteins with the STn glycoform.
25813380	6	83	from	pools	964:968	arg1	cancer					991:996	gastric cancer	983:996	gastric cancer	983:996	We next modified the glycoproteomic strategy to apply it to pools of sera from gastric cancer and healthy individuals to identify circulating O-glycoproteins with the STn glycoform.
25813380	10	84	gly	glycosylated	1568:1579	arg1	O-glycoproteins					1581:1595	aberrantly glycosylated O-glycoproteins	1557:1595	aberrantly glycosylated O-glycoproteins	1557:1595	The study provides a discovery strategy for aberrantly glycosylated O-glycoproteins and a set of O-glycoprotein candidates with biomarker potential in gastric cancer.
25813380	5	85	gly	O-glycoproteins	757:771	arg1	O-glycoproteins					757:771	499 O-glycoproteins	753:771	499 O-glycoproteins	753:771	Overall, we identified 499 O-glycoproteins and 1236 O-glycosites in gastric cancer SimpleCells, and a total 47 O-glycoproteins and 73 O-glycosites in the KATO III cell line.
25813380	5	86	theme	cancer	806:811	arg1	SimpleCells					813:823	gastric cancer SimpleCells	798:823	gastric cancer SimpleCells	798:823	Overall, we identified 499 O-glycoproteins and 1236 O-glycosites in gastric cancer SimpleCells, and a total 47 O-glycoproteins and 73 O-glycosites in the KATO III cell line.
25813380	1	87	theme	Circulating	82:92	arg1	O-glycoproteins					94:108	Circulating O-glycoproteins	82:108	Circulating O-glycoproteins shed from cancer cells	82:131	Circulating O-glycoproteins shed from cancer cells represent important serum biomarkers for diagnostic and prognostic purposes.
25813380	9	88	gly	glycoform	1476:1484	arg2	tissues					1504:1510	gastric cancer tissues	1489:1510	gastric cancer tissues	1489:1510	A proximity ligation assay was used to show that CD44 was expressed with the STn glycoform in gastric cancer tissues.
25813380	9	88	gly	glycoform	1476:1484	arg1	STn					1472:1474	the STn glycoform	1468:1484	the STn glycoform in gastric cancer tissues	1468:1510	A proximity ligation assay was used to show that CD44 was expressed with the STn glycoform in gastric cancer tissues.
25813380	3	89	theme	circulating	440:450	arg1	O-glycoproteins					452:466	secreted and circulating O-glycoproteins	427:466	secreted and circulating O-glycoproteins	427:466	However, the current knowledge of secreted and circulating O-glycoproteins is limited.
25813380	4	90	theme	cancer	585:590	arg1	lines					603:607	two gastric cancer SimpleCell lines	573:607	two gastric cancer SimpleCell lines (AGS, MKN45) as well as a gastric cell line (KATO III) which naturally expresses at least partially truncated O-glycans	573:727	Here, we used the COSMC KO "SimpleCell" (SC) strategy to characterize the O-glycoproteome of two gastric cancer SimpleCell lines (AGS, MKN45) as well as a gastric cell line (KATO III) which naturally expresses at least partially truncated O-glycans.
25813380	10	91	theme	O-glycoprotein	1610:1623	arg1	candidates					1625:1634	O-glycoprotein candidates	1610:1634	O-glycoprotein candidates	1610:1634	The study provides a discovery strategy for aberrantly glycosylated O-glycoproteins and a set of O-glycoprotein candidates with biomarker potential in gastric cancer.
25813380	8	92	gly	glycoform	1317:1325	arg1	STn					1313:1315	the STn glycoform	1309:1325	the STn glycoform	1309:1325	Two identified candidate O-glycoprotein biomarkers (CD44 and GalNAc-T5) circulating with the STn glycoform were further validated as being expressed in gastric cancer tissue.
25813380	9	93	used	used	1426:1429	arg2	assay					1416:1420	A proximity ligation assay	1395:1420	A proximity ligation assay	1395:1420	A proximity ligation assay was used to show that CD44 was expressed with the STn glycoform in gastric cancer tissues.
25813380	6	94	theme	circulating	1034:1044	arg1	O-glycoproteins					1046:1060	circulating O-glycoproteins	1034:1060	circulating O-glycoproteins with the STn glycoform	1034:1083	We next modified the glycoproteomic strategy to apply it to pools of sera from gastric cancer and healthy individuals to identify circulating O-glycoproteins with the STn glycoform.
25813380	3	95	theme	secreted	427:434	arg1	O-glycoproteins					452:466	secreted and circulating O-glycoproteins	427:466	secreted and circulating O-glycoproteins	427:466	However, the current knowledge of secreted and circulating O-glycoproteins is limited.
25813380	4	96	theme	lines	603:607	arg1	O-glycoproteome					554:568	the O-glycoproteome	550:568	the O-glycoproteome of two gastric cancer SimpleCell lines (AGS, MKN45) as well as a gastric cell line (KATO III) which naturally expresses at least partially truncated O-glycans	550:727	Here, we used the COSMC KO "SimpleCell" (SC) strategy to characterize the O-glycoproteome of two gastric cancer SimpleCell lines (AGS, MKN45) as well as a gastric cell line (KATO III) which naturally expresses at least partially truncated O-glycans.
25813380	10	97	theme	gastric	1664:1670	arg1	cancer					1672:1677	gastric cancer	1664:1677	gastric cancer	1664:1677	The study provides a discovery strategy for aberrantly glycosylated O-glycoproteins and a set of O-glycoprotein candidates with biomarker potential in gastric cancer.
25813380	7	98	theme	cancer	1134:1139	arg1	sera					1141:1144	cancer sera	1134:1144	cancer sera	1134:1144	We identified 37 O-glycoproteins in the pool of cancer sera, and only nine of these were also found in sera from healthy individuals.
25813380	6	99	with	O-glycoproteins	1046:1060	arg1	glycoform					1075:1083	the STn glycoform	1067:1083	the STn glycoform	1067:1083	We next modified the glycoproteomic strategy to apply it to pools of sera from gastric cancer and healthy individuals to identify circulating O-glycoproteins with the STn glycoform.
25813380	0	100	theme	lines	51:55	arg1	O-glycoproteome					12:26	the O-glycoproteome	8:26	the O-glycoproteome of gastric cancer cell lines for biomarker discovery	8:79	Probing the O-glycoproteome of gastric cancer cell lines for biomarker discovery.
25813380	8	101	theme	cancer	1380:1385	arg1	tissue					1387:1392	gastric cancer tissue	1372:1392	gastric cancer tissue	1372:1392	Two identified candidate O-glycoprotein biomarkers (CD44 and GalNAc-T5) circulating with the STn glycoform were further validated as being expressed in gastric cancer tissue.
25813380	2	102	theme	biomarker	375:383	arg1	assays					385:390	cancer biomarker assays	368:390	cancer biomarker assays	368:390	We have recently shown that selective detection of cancer-associated aberrant glycoforms of circulating O-glycoprotein biomarkers can increase specificity of cancer biomarker assays.
25813380	8	103	theme	O-glycoprotein	1245:1258	arg1	GalNAc-T5					1281:1289	GalNAc-T5	1281:1289	GalNAc-T5	1281:1289	Two identified candidate O-glycoprotein biomarkers (CD44 and GalNAc-T5) circulating with the STn glycoform were further validated as being expressed in gastric cancer tissue.
25813380	8	103	theme	O-glycoprotein	1245:1258	arg1	CD44					1272:1275	CD44	1272:1275	CD44	1272:1275	Two identified candidate O-glycoprotein biomarkers (CD44 and GalNAc-T5) circulating with the STn glycoform were further validated as being expressed in gastric cancer tissue.
25813380	8	103	theme	O-glycoprotein	1245:1258	arg1	biomarkers					1260:1269	identified candidate O-glycoprotein biomarkers	1224:1269	Two identified candidate O-glycoprotein biomarkers (CD44 and GalNAc-T5) circulating with the STn glycoform	1220:1325	Two identified candidate O-glycoprotein biomarkers (CD44 and GalNAc-T5) circulating with the STn glycoform were further validated as being expressed in gastric cancer tissue.
25813380	10	104	from	potential	1651:1659	arg1	cancer					1672:1677	gastric cancer	1664:1677	gastric cancer	1664:1677	The study provides a discovery strategy for aberrantly glycosylated O-glycoproteins and a set of O-glycoprotein candidates with biomarker potential in gastric cancer.
27434672	5	0	theme	active	631:636	arg1	structure					638:646	the active structure	627:646	the active structure	627:646	In the active structure, L-Trp occupies the orthosteric agonist-binding site at the interdomain cleft and is primarily responsible for inducing extracellular domain closure to initiate receptor activation.
27434672	8	1	theme	inactive	1041:1048	arg1	conformation					1050:1061	the inactive conformation	1037:1061	the inactive conformation	1037:1061	While Ca(2+) ions stabilize the active state, PO4(3-) ions reinforce the inactive conformation.
27434672	2	2	theme	Flytrap	348:354	arg1	module					356:361	the Venus Flytrap module	338:361	the Venus Flytrap module	338:361	It functions as a disulfide-tethered homodimer composed of three main domains, the Venus Flytrap module, cysteine-rich domain, and seven-helix transmembrane region.
27434672	2	2	theme	Flytrap	348:354	arg1	domains					329:335	three main domains	318:335	three main domains	318:335	It functions as a disulfide-tethered homodimer composed of three main domains, the Venus Flytrap module, cysteine-rich domain, and seven-helix transmembrane region.
27434672	9	3	theme	activation	1068:1077	arg1	mechanism					1079:1087	The activation mechanism	1064:1087	The activation mechanism of CaSR	1064:1095	The activation mechanism of CaSR involves the formation of a novel dimer interface between subunits.
27434672	1	4	theme	hormone	240:246	arg1	secretion					248:256	parathyroid hormone secretion	228:256	parathyroid hormone secretion	228:256	Human calcium-sensing receptor (CaSR) is a G-protein-coupled receptor (GPCR) that maintains extracellular Ca(2+) homeostasis through the regulation of parathyroid hormone secretion.
27434672	5	5	theme	extracellular	768:780	arg1	closure					789:795	extracellular domain closure	768:795	extracellular domain closure	768:795	In the active structure, L-Trp occupies the orthosteric agonist-binding site at the interdomain cleft and is primarily responsible for inducing extracellular domain closure to initiate receptor activation.
27434672	0	6	from	mechanism	11:19	arg1	receptor					67:74	human calcium-sensing receptor	45:74	human calcium-sensing receptor	45:74	Structural mechanism of ligand activation in human calcium-sensing receptor.
27434672	7	7	theme	structural	930:939	arg1	integrity					941:949	structural integrity	930:949	structural integrity of the receptor	930:965	Both ions are crucial for structural integrity of the receptor.
27434672	2	8	theme	Venus	342:346	arg1	module					356:361	the Venus Flytrap module	338:361	the Venus Flytrap module	338:361	It functions as a disulfide-tethered homodimer composed of three main domains, the Venus Flytrap module, cysteine-rich domain, and seven-helix transmembrane region.
27434672	2	8	theme	Venus	342:346	arg1	domains					329:335	three main domains	318:335	three main domains	318:335	It functions as a disulfide-tethered homodimer composed of three main domains, the Venus Flytrap module, cysteine-rich domain, and seven-helix transmembrane region.
27434672	1	9	theme	secretion	248:256	arg1	regulation					214:223	the regulation	210:223	the regulation of parathyroid hormone secretion	210:256	Human calcium-sensing receptor (CaSR) is a G-protein-coupled receptor (GPCR) that maintains extracellular Ca(2+) homeostasis through the regulation of parathyroid hormone secretion.
27434672	2	10	theme	disulfide-tethered	277:294	arg1	homodimer					296:304	a disulfide-tethered homodimer	275:304	a disulfide-tethered homodimer composed of three main domains, the Venus Flytrap module, cysteine-rich domain, and seven-helix transmembrane region	275:421	It functions as a disulfide-tethered homodimer composed of three main domains, the Venus Flytrap module, cysteine-rich domain, and seven-helix transmembrane region.
27434672	2	10	theme	disulfide-tethered	277:294	arg1	It					259:260	It	259:260	It	259:260	It functions as a disulfide-tethered homodimer composed of three main domains, the Venus Flytrap module, cysteine-rich domain, and seven-helix transmembrane region.
27434672	3	11	theme	entire	471:476	arg1	CaSR					502:505	CaSR	502:505	CaSR	502:505	Here, we present the crystal structures of the entire extracellular domain of CaSR in the resting and active conformations.
27434672	3	11	theme	entire	471:476	arg1	domain					492:497	the entire extracellular domain	467:497	the entire extracellular domain of CaSR	467:505	Here, we present the crystal structures of the entire extracellular domain of CaSR in the resting and active conformations.
27434672	9	12	theme	novel	1125:1129	arg1	interface					1137:1145	a novel dimer interface	1123:1145	a novel dimer interface between subunits	1123:1162	The activation mechanism of CaSR involves the formation of a novel dimer interface between subunits.
27434672	1	13	theme	Human	77:81	arg1	receptor					138:145	a G-protein-coupled receptor	118:145	a G-protein-coupled receptor (GPCR) that maintains extracellular Ca(2+) homeostasis through the regulation of parathyroid hormone secretion	118:256	Human calcium-sensing receptor (CaSR) is a G-protein-coupled receptor (GPCR) that maintains extracellular Ca(2+) homeostasis through the regulation of parathyroid hormone secretion.
27434672	1	13	theme	Human	77:81	arg1	CaSR					109:112	CaSR	109:112	CaSR	109:112	Human calcium-sensing receptor (CaSR) is a G-protein-coupled receptor (GPCR) that maintains extracellular Ca(2+) homeostasis through the regulation of parathyroid hormone secretion.
27434672	1	13	theme	Human	77:81	arg1	receptor					99:106	Human calcium-sensing receptor	77:106	Human calcium-sensing receptor (CaSR)	77:113	Human calcium-sensing receptor (CaSR) is a G-protein-coupled receptor (GPCR) that maintains extracellular Ca(2+) homeostasis through the regulation of parathyroid hormone secretion.
27434672	4	14	theme	L-amino	580:586	arg1	agonists					598:605	agonists	598:605	agonists of the receptor	598:621	We provide direct evidence that L-amino acids are agonists of the receptor.
27434672	4	14	theme	L-amino	580:586	arg1	acids					588:592	L-amino acids	580:592	L-amino acids	580:592	We provide direct evidence that L-amino acids are agonists of the receptor.
27434672	8	15	theme	active	1000:1005	arg1	state					1007:1011	the active state	996:1011	the active state	996:1011	While Ca(2+) ions stabilize the active state, PO4(3-) ions reinforce the inactive conformation.
27434672	8	16	theme	Ca	974:975	arg1	ions					981:984	Ca(2+) ions	974:984	Ca(2+) ions	974:984	While Ca(2+) ions stabilize the active state, PO4(3-) ions reinforce the inactive conformation.
27434672	1	17	theme	calcium-sensing	83:97	arg1	receptor					138:145	a G-protein-coupled receptor	118:145	a G-protein-coupled receptor (GPCR) that maintains extracellular Ca(2+) homeostasis through the regulation of parathyroid hormone secretion	118:256	Human calcium-sensing receptor (CaSR) is a G-protein-coupled receptor (GPCR) that maintains extracellular Ca(2+) homeostasis through the regulation of parathyroid hormone secretion.
27434672	1	17	theme	calcium-sensing	83:97	arg1	CaSR					109:112	CaSR	109:112	CaSR	109:112	Human calcium-sensing receptor (CaSR) is a G-protein-coupled receptor (GPCR) that maintains extracellular Ca(2+) homeostasis through the regulation of parathyroid hormone secretion.
27434672	1	17	theme	calcium-sensing	83:97	arg1	receptor					99:106	Human calcium-sensing receptor	77:106	Human calcium-sensing receptor (CaSR)	77:113	Human calcium-sensing receptor (CaSR) is a G-protein-coupled receptor (GPCR) that maintains extracellular Ca(2+) homeostasis through the regulation of parathyroid hormone secretion.
27434672	1	18	theme	extracellular	169:181	arg1	Ca					183:184	extracellular Ca	169:184	extracellular Ca(2+) homeostasis	169:200	Human calcium-sensing receptor (CaSR) is a G-protein-coupled receptor (GPCR) that maintains extracellular Ca(2+) homeostasis through the regulation of parathyroid hormone secretion.
27434672	1	18	theme	extracellular	169:181	arg1	2+					186:187	2+	186:187	2+	186:187	Human calcium-sensing receptor (CaSR) is a G-protein-coupled receptor (GPCR) that maintains extracellular Ca(2+) homeostasis through the regulation of parathyroid hormone secretion.
27434672	5	19	theme	receptor	809:816	arg1	activation					818:827	receptor activation	809:827	receptor activation	809:827	In the active structure, L-Trp occupies the orthosteric agonist-binding site at the interdomain cleft and is primarily responsible for inducing extracellular domain closure to initiate receptor activation.
27434672	0	20	from	activation	31:40	arg1	receptor					67:74	human calcium-sensing receptor	45:74	human calcium-sensing receptor	45:74	Structural mechanism of ligand activation in human calcium-sensing receptor.
27434672	9	21	theme	interface	1137:1145	arg1	formation					1110:1118	the formation	1106:1118	the formation of a novel dimer interface between subunits	1106:1162	The activation mechanism of CaSR involves the formation of a novel dimer interface between subunits.
27434672	1	22	theme	Ca	183:184	arg1	homeostasis					190:200	extracellular Ca(2+) homeostasis	169:200	extracellular Ca(2+) homeostasis	169:200	Human calcium-sensing receptor (CaSR) is a G-protein-coupled receptor (GPCR) that maintains extracellular Ca(2+) homeostasis through the regulation of parathyroid hormone secretion.
27434672	0	23	theme	Structural	0:9	arg1	mechanism					11:19	Structural mechanism	0:19	Structural mechanism of ligand activation in human calcium-sensing receptor	0:74	Structural mechanism of ligand activation in human calcium-sensing receptor.
27434672	2	24	theme	cysteine-rich	364:376	arg1	domain					378:383	cysteine-rich domain	364:383	cysteine-rich domain	364:383	It functions as a disulfide-tethered homodimer composed of three main domains, the Venus Flytrap module, cysteine-rich domain, and seven-helix transmembrane region.
27434672	2	24	theme	cysteine-rich	364:376	arg1	domains					329:335	three main domains	318:335	three main domains	318:335	It functions as a disulfide-tethered homodimer composed of three main domains, the Venus Flytrap module, cysteine-rich domain, and seven-helix transmembrane region.
27434672	0	25	theme	ligand	24:29	arg1	activation					31:40	ligand activation	24:40	ligand activation in human calcium-sensing receptor	24:74	Structural mechanism of ligand activation in human calcium-sensing receptor.
27434672	4	26	theme	direct	559:564	arg1	evidence					566:573	direct evidence that L-amino acids are agonists of the receptor	559:621	direct evidence that L-amino acids are agonists of the receptor	559:621	We provide direct evidence that L-amino acids are agonists of the receptor.
27434672	3	27	theme	resting	514:520	arg1	conformations					533:545	the resting and active conformations	510:545	the resting and active conformations	510:545	Here, we present the crystal structures of the entire extracellular domain of CaSR in the resting and active conformations.
27434672	3	28	theme	CaSR	502:505	arg1	CaSR					502:505	CaSR	502:505	CaSR	502:505	Here, we present the crystal structures of the entire extracellular domain of CaSR in the resting and active conformations.
27434672	3	28	theme	CaSR	502:505	arg1	domain					492:497	the entire extracellular domain	467:497	the entire extracellular domain of CaSR	467:505	Here, we present the crystal structures of the entire extracellular domain of CaSR in the resting and active conformations.
27434672	4	29	theme	receptor	614:621	arg1	agonists					598:605	agonists	598:605	agonists of the receptor	598:621	We provide direct evidence that L-amino acids are agonists of the receptor.
27434672	4	29	theme	receptor	614:621	arg1	acids					588:592	L-amino acids	580:592	L-amino acids	580:592	We provide direct evidence that L-amino acids are agonists of the receptor.
27434672	5	30	theme	domain	782:787	arg1	closure					789:795	extracellular domain closure	768:795	extracellular domain closure	768:795	In the active structure, L-Trp occupies the orthosteric agonist-binding site at the interdomain cleft and is primarily responsible for inducing extracellular domain closure to initiate receptor activation.
27434672	2	31	theme	transmembrane	402:414	arg1	region					416:421	seven-helix transmembrane region	390:421	seven-helix transmembrane region	390:421	It functions as a disulfide-tethered homodimer composed of three main domains, the Venus Flytrap module, cysteine-rich domain, and seven-helix transmembrane region.
27434672	2	31	theme	transmembrane	402:414	arg1	domains					329:335	three main domains	318:335	three main domains	318:335	It functions as a disulfide-tethered homodimer composed of three main domains, the Venus Flytrap module, cysteine-rich domain, and seven-helix transmembrane region.
27434672	0	32	theme	activation	31:40	arg1	mechanism					11:19	Structural mechanism	0:19	Structural mechanism of ligand activation in human calcium-sensing receptor	0:74	Structural mechanism of ligand activation in human calcium-sensing receptor.
27434672	5	33	theme	interdomain	708:718	arg1	cleft					720:724	the interdomain cleft	704:724	the interdomain cleft	704:724	In the active structure, L-Trp occupies the orthosteric agonist-binding site at the interdomain cleft and is primarily responsible for inducing extracellular domain closure to initiate receptor activation.
27434672	5	34	from	cleft	720:724	arg1	site					696:699	the orthosteric agonist-binding site	664:699	the orthosteric agonist-binding site at the interdomain cleft	664:724	In the active structure, L-Trp occupies the orthosteric agonist-binding site at the interdomain cleft and is primarily responsible for inducing extracellular domain closure to initiate receptor activation.
27434672	2	35	theme	seven-helix	390:400	arg1	region					416:421	seven-helix transmembrane region	390:421	seven-helix transmembrane region	390:421	It functions as a disulfide-tethered homodimer composed of three main domains, the Venus Flytrap module, cysteine-rich domain, and seven-helix transmembrane region.
27434672	2	35	theme	seven-helix	390:400	arg1	domains					329:335	three main domains	318:335	three main domains	318:335	It functions as a disulfide-tethered homodimer composed of three main domains, the Venus Flytrap module, cysteine-rich domain, and seven-helix transmembrane region.
27434672	0	36	theme	calcium-sensing	51:65	arg1	receptor					67:74	human calcium-sensing receptor	45:74	human calcium-sensing receptor	45:74	Structural mechanism of ligand activation in human calcium-sensing receptor.
27434672	0	37	from	receptor	67:74	arg1	mechanism					11:19	Structural mechanism	0:19	Structural mechanism of ligand activation in human calcium-sensing receptor	0:74	Structural mechanism of ligand activation in human calcium-sensing receptor.
27434672	3	38	theme	extracellular	478:490	arg1	CaSR					502:505	CaSR	502:505	CaSR	502:505	Here, we present the crystal structures of the entire extracellular domain of CaSR in the resting and active conformations.
27434672	3	38	theme	extracellular	478:490	arg1	domain					492:497	the entire extracellular domain	467:497	the entire extracellular domain of CaSR	467:505	Here, we present the crystal structures of the entire extracellular domain of CaSR in the resting and active conformations.
27434672	0	39	theme	human	45:49	arg1	receptor					67:74	human calcium-sensing receptor	45:74	human calcium-sensing receptor	45:74	Structural mechanism of ligand activation in human calcium-sensing receptor.
27434672	9	40	theme	dimer	1131:1135	arg1	interface					1137:1145	a novel dimer interface	1123:1145	a novel dimer interface between subunits	1123:1162	The activation mechanism of CaSR involves the formation of a novel dimer interface between subunits.
27434672	6	41	theme	binding	861:867	arg1	sites					869:873	multiple binding sites	852:873	multiple binding sites for Ca(2+) and PO4(3-) ions	852:901	Our structures reveal multiple binding sites for Ca(2+) and PO4(3-) ions.
27434672	3	42	from	structures	453:462	arg1	conformations					533:545	the resting and active conformations	510:545	the resting and active conformations	510:545	Here, we present the crystal structures of the entire extracellular domain of CaSR in the resting and active conformations.
27434672	3	43	theme	domain	492:497	arg1	structures					453:462	the crystal structures	441:462	the crystal structures of the entire extracellular domain of CaSR in the resting and active conformations	441:545	Here, we present the crystal structures of the entire extracellular domain of CaSR in the resting and active conformations.
27434672	6	44	dep	Ca	879:880	arg1	ions					898:901	ions	898:901	ions	898:901	Our structures reveal multiple binding sites for Ca(2+) and PO4(3-) ions.
27434672	5	45	theme	orthosteric	668:678	arg1	site					696:699	the orthosteric agonist-binding site	664:699	the orthosteric agonist-binding site at the interdomain cleft	664:724	In the active structure, L-Trp occupies the orthosteric agonist-binding site at the interdomain cleft and is primarily responsible for inducing extracellular domain closure to initiate receptor activation.
27434672	6	46	theme	multiple	852:859	arg1	sites					869:873	multiple binding sites	852:873	multiple binding sites for Ca(2+) and PO4(3-) ions	852:901	Our structures reveal multiple binding sites for Ca(2+) and PO4(3-) ions.
27434672	1	47	theme	G-protein-coupled	120:136	arg1	GPCR					148:151	GPCR	148:151	GPCR	148:151	Human calcium-sensing receptor (CaSR) is a G-protein-coupled receptor (GPCR) that maintains extracellular Ca(2+) homeostasis through the regulation of parathyroid hormone secretion.
27434672	1	47	theme	G-protein-coupled	120:136	arg1	receptor					138:145	a G-protein-coupled receptor	118:145	a G-protein-coupled receptor (GPCR) that maintains extracellular Ca(2+) homeostasis through the regulation of parathyroid hormone secretion	118:256	Human calcium-sensing receptor (CaSR) is a G-protein-coupled receptor (GPCR) that maintains extracellular Ca(2+) homeostasis through the regulation of parathyroid hormone secretion.
27434672	1	47	theme	G-protein-coupled	120:136	arg1	receptor					99:106	Human calcium-sensing receptor	77:106	Human calcium-sensing receptor (CaSR)	77:113	Human calcium-sensing receptor (CaSR) is a G-protein-coupled receptor (GPCR) that maintains extracellular Ca(2+) homeostasis through the regulation of parathyroid hormone secretion.
27434672	5	48	theme	agonist-binding	680:694	arg1	site					696:699	the orthosteric agonist-binding site	664:699	the orthosteric agonist-binding site at the interdomain cleft	664:724	In the active structure, L-Trp occupies the orthosteric agonist-binding site at the interdomain cleft and is primarily responsible for inducing extracellular domain closure to initiate receptor activation.
27434672	3	49	theme	active	526:531	arg1	conformations					533:545	the resting and active conformations	510:545	the resting and active conformations	510:545	Here, we present the crystal structures of the entire extracellular domain of CaSR in the resting and active conformations.
27434672	7	50	theme	receptor	958:965	arg1	integrity					941:949	structural integrity	930:949	structural integrity of the receptor	930:965	Both ions are crucial for structural integrity of the receptor.
27434672	2	51	theme	main	324:327	arg1	region					416:421	seven-helix transmembrane region	390:421	seven-helix transmembrane region	390:421	It functions as a disulfide-tethered homodimer composed of three main domains, the Venus Flytrap module, cysteine-rich domain, and seven-helix transmembrane region.
27434672	2	51	theme	main	324:327	arg1	module					356:361	the Venus Flytrap module	338:361	the Venus Flytrap module	338:361	It functions as a disulfide-tethered homodimer composed of three main domains, the Venus Flytrap module, cysteine-rich domain, and seven-helix transmembrane region.
27434672	2	51	theme	main	324:327	arg1	domains					329:335	three main domains	318:335	three main domains	318:335	It functions as a disulfide-tethered homodimer composed of three main domains, the Venus Flytrap module, cysteine-rich domain, and seven-helix transmembrane region.
27434672	2	51	theme	main	324:327	arg1	domain					378:383	cysteine-rich domain	364:383	cysteine-rich domain	364:383	It functions as a disulfide-tethered homodimer composed of three main domains, the Venus Flytrap module, cysteine-rich domain, and seven-helix transmembrane region.
27434672	3	52	theme	crystal	445:451	arg1	structures					453:462	the crystal structures	441:462	the crystal structures of the entire extracellular domain of CaSR in the resting and active conformations	441:545	Here, we present the crystal structures of the entire extracellular domain of CaSR in the resting and active conformations.
27434672	9	53	theme	CaSR	1092:1095	arg1	mechanism					1079:1087	The activation mechanism	1064:1087	The activation mechanism of CaSR	1064:1095	The activation mechanism of CaSR involves the formation of a novel dimer interface between subunits.
27434672	1	54	theme	parathyroid	228:238	arg1	secretion					248:256	parathyroid hormone secretion	228:256	parathyroid hormone secretion	228:256	Human calcium-sensing receptor (CaSR) is a G-protein-coupled receptor (GPCR) that maintains extracellular Ca(2+) homeostasis through the regulation of parathyroid hormone secretion.
20489211	8	0	theme	favorable	1393:1401	arg1	complex					1384:1390	the transmembrane complex	1366:1390	the transmembrane complex	1366:1390	Importantly, this geometry positions the C termini of the membrane-proximal fibronectin type III domains of the tall cytokine receptors in close proximity within the transmembrane complex, favorable for receptor-associated Janus kinases to trans-phosphorylate and activate each other.
20489211	1	1	theme	6-like	237:242	arg1	cytokines					244:252	interleukin 6-like cytokines	225:252	interleukin 6-like cytokines	225:252	gp130 is the shared signal-transducing receptor subunit for the large and important family of interleukin 6-like cytokines.
20489211	8	2	theme	Janus	1427:1431	arg1	kinases					1433:1439	receptor-associated Janus kinases	1407:1439	receptor-associated Janus kinases	1407:1439	Importantly, this geometry positions the C termini of the membrane-proximal fibronectin type III domains of the tall cytokine receptors in close proximity within the transmembrane complex, favorable for receptor-associated Janus kinases to trans-phosphorylate and activate each other.
20489211	7	3	theme	Key	1036:1038	arg1	residues					1040:1047	Key residues	1036:1047	Key residues at this interface	1036:1065	Key residues at this interface are highly conserved across the entire tall receptor family, suggesting that this acute bend may be a common feature of these receptors.
20489211	3	4	theme	crystal	429:435	arg1	structure					437:445	the crystal structure	425:445	the crystal structure of the entire extracellular portion of human gp130 (domains 1-6, D1-D6) at 3.6 A resolution	425:537	Here we report the crystal structure of the entire extracellular portion of human gp130 (domains 1-6, D1-D6) at 3.6 A resolution, in an unliganded form, as well as a higher resolution structure of the membrane-proximal fibronectin type III domains (D4-D6) at 1.9 A.
20489211	8	5	theme	membrane-proximal	1262:1278	arg1	domains					1301:1307	the membrane-proximal fibronectin type III domains	1258:1307	the membrane-proximal fibronectin type III domains of the tall cytokine receptors	1258:1338	Importantly, this geometry positions the C termini of the membrane-proximal fibronectin type III domains of the tall cytokine receptors in close proximity within the transmembrane complex, favorable for receptor-associated Janus kinases to trans-phosphorylate and activate each other.
20489211	8	5	theme	membrane-proximal	1262:1278	arg1	receptors					1330:1338	the tall cytokine receptors	1312:1338	the tall cytokine receptors	1312:1338	Importantly, this geometry positions the C termini of the membrane-proximal fibronectin type III domains of the tall cytokine receptors in close proximity within the transmembrane complex, favorable for receptor-associated Janus kinases to trans-phosphorylate and activate each other.
20489211	1	6	theme	cytokines	244:252	arg1	family					215:220	the large and important family	191:220	the large and important family of interleukin 6-like cytokines	191:252	gp130 is the shared signal-transducing receptor subunit for the large and important family of interleukin 6-like cytokines.
20489211	7	7	theme	tall	1106:1109	arg1	family					1120:1125	the entire tall receptor family	1095:1125	the entire tall receptor family	1095:1125	Key residues at this interface are highly conserved across the entire tall receptor family, suggesting that this acute bend may be a common feature of these receptors.
20489211	3	8	theme	resolution	583:592	arg1	structure					594:602	a higher resolution structure	574:602	a higher resolution structure of the membrane-proximal fibronectin type III domains (D4-D6)	574:664	Here we report the crystal structure of the entire extracellular portion of human gp130 (domains 1-6, D1-D6) at 3.6 A resolution, in an unliganded form, as well as a higher resolution structure of the membrane-proximal fibronectin type III domains (D4-D6) at 1.9 A.
20489211	8	9	theme	tall	1316:1319	arg1	receptors					1330:1338	the tall cytokine receptors	1312:1338	the tall cytokine receptors	1312:1338	Importantly, this geometry positions the C termini of the membrane-proximal fibronectin type III domains of the tall cytokine receptors in close proximity within the transmembrane complex, favorable for receptor-associated Janus kinases to trans-phosphorylate and activate each other.
20489211	2	10	theme	ligand-receptor	284:298	arg1	complexes					300:308	ligand-receptor complexes	284:308	ligand-receptor complexes of this family	284:323	Previous x-ray structures of ligand-receptor complexes of this family lack the three membrane-proximal domains that are essential for signal transduction.
20489211	3	11	from	resolution	528:537	arg1	domains					499:505	domains 1-6	499:509	domains 1-6	499:509	Here we report the crystal structure of the entire extracellular portion of human gp130 (domains 1-6, D1-D6) at 3.6 A resolution, in an unliganded form, as well as a higher resolution structure of the membrane-proximal fibronectin type III domains (D4-D6) at 1.9 A.
20489211	3	11	from	resolution	528:537	arg1	portion					475:481	the entire extracellular portion	450:481	the entire extracellular portion of human gp130 (domains 1-6, D1-D6) at 3.6 A resolution	450:537	Here we report the crystal structure of the entire extracellular portion of human gp130 (domains 1-6, D1-D6) at 3.6 A resolution, in an unliganded form, as well as a higher resolution structure of the membrane-proximal fibronectin type III domains (D4-D6) at 1.9 A.
20489211	3	11	from	resolution	528:537	arg1	gp130					492:496	human gp130	486:496	human gp130 (domains 1-6, D1-D6) at 3.6 A resolution	486:537	Here we report the crystal structure of the entire extracellular portion of human gp130 (domains 1-6, D1-D6) at 3.6 A resolution, in an unliganded form, as well as a higher resolution structure of the membrane-proximal fibronectin type III domains (D4-D6) at 1.9 A.
20489211	0	12	theme	molecular	71:79	arg1	assembly					81:88	the molecular assembly	67:88	the molecular assembly of the tall cytokine receptor complexes	67:128	Crystal structure of the entire ectodomain of gp130: insights into the molecular assembly of the tall cytokine receptor complexes.
20489211	8	13	theme	C	1245:1245	arg1	termini					1247:1253	the C termini	1241:1253	the C termini of the membrane-proximal fibronectin type III domains of the tall cytokine receptors	1241:1338	Importantly, this geometry positions the C termini of the membrane-proximal fibronectin type III domains of the tall cytokine receptors in close proximity within the transmembrane complex, favorable for receptor-associated Janus kinases to trans-phosphorylate and activate each other.
20489211	4	14	theme	complete	737:744	arg1	receptor					780:787	any "tall" cytokine receptor	760:787	any "tall" cytokine receptor	760:787	This represents the first atomic resolution structure of the complete ectodomain of any "tall" cytokine receptor.
20489211	4	14	theme	complete	737:744	arg1	ectodomain					746:755	the complete ectodomain	733:755	the complete ectodomain of any "tall" cytokine receptor	733:787	This represents the first atomic resolution structure of the complete ectodomain of any "tall" cytokine receptor.
20489211	4	15	theme	resolution	709:718	arg1	structure					720:728	the first atomic resolution structure	692:728	the first atomic resolution structure of the complete ectodomain of any "tall" cytokine receptor	692:787	This represents the first atomic resolution structure of the complete ectodomain of any "tall" cytokine receptor.
20489211	6	16	theme	gp130	1019:1023	arg1	structure					1025:1033	the gp130 structure	1015:1033	the gp130 structure	1015:1033	They also reveal that the interface between the D4 and D5 domains forms an acute bend in the gp130 structure.
20489211	5	17	theme	D1	851:852	arg1	domain					854:859	the D1 domain	847:859	the D1 domain	847:859	These structures show that other than a reorientation of the D1 domain, there is little structural change in gp130 upon ligand binding.
20489211	8	18	theme	transmembrane	1370:1382	arg1	complex					1384:1390	the transmembrane complex	1366:1390	the transmembrane complex	1366:1390	Importantly, this geometry positions the C termini of the membrane-proximal fibronectin type III domains of the tall cytokine receptors in close proximity within the transmembrane complex, favorable for receptor-associated Janus kinases to trans-phosphorylate and activate each other.
20489211	2	19	theme	signal	389:394	arg1	transduction					396:407	signal transduction	389:407	signal transduction	389:407	Previous x-ray structures of ligand-receptor complexes of this family lack the three membrane-proximal domains that are essential for signal transduction.
20489211	1	20	theme	shared	144:149	arg1	gp130					131:135	gp130	131:135	gp130	131:135	gp130 is the shared signal-transducing receptor subunit for the large and important family of interleukin 6-like cytokines.
20489211	1	20	theme	shared	144:149	arg1	subunit					179:185	the shared signal-transducing receptor subunit	140:185	the shared signal-transducing receptor subunit for the large and important family of interleukin 6-like cytokines	140:252	gp130 is the shared signal-transducing receptor subunit for the large and important family of interleukin 6-like cytokines.
20489211	7	21	theme	entire	1099:1104	arg1	family					1120:1125	the entire tall receptor family	1095:1125	the entire tall receptor family	1095:1125	Key residues at this interface are highly conserved across the entire tall receptor family, suggesting that this acute bend may be a common feature of these receptors.
20489211	4	22	theme	receptor	780:787	arg1	receptor					780:787	any "tall" cytokine receptor	760:787	any "tall" cytokine receptor	760:787	This represents the first atomic resolution structure of the complete ectodomain of any "tall" cytokine receptor.
20489211	4	22	theme	receptor	780:787	arg1	ectodomain					746:755	the complete ectodomain	733:755	the complete ectodomain of any "tall" cytokine receptor	733:787	This represents the first atomic resolution structure of the complete ectodomain of any "tall" cytokine receptor.
20489211	2	23	theme	x-ray	264:268	arg1	structures					270:279	Previous x-ray structures	255:279	Previous x-ray structures of ligand-receptor complexes of this family	255:323	Previous x-ray structures of ligand-receptor complexes of this family lack the three membrane-proximal domains that are essential for signal transduction.
20489211	6	24	theme	acute	1001:1005	arg1	bend					1007:1010	an acute bend	998:1010	an acute bend in the gp130 structure	998:1033	They also reveal that the interface between the D4 and D5 domains forms an acute bend in the gp130 structure.
20489211	1	25	theme	signal-transducing	151:168	arg1	gp130					131:135	gp130	131:135	gp130	131:135	gp130 is the shared signal-transducing receptor subunit for the large and important family of interleukin 6-like cytokines.
20489211	1	25	theme	signal-transducing	151:168	arg1	subunit					179:185	the shared signal-transducing receptor subunit	140:185	the shared signal-transducing receptor subunit for the large and important family of interleukin 6-like cytokines	140:252	gp130 is the shared signal-transducing receptor subunit for the large and important family of interleukin 6-like cytokines.
20489211	2	26	theme	family	318:323	arg1	complexes					300:308	ligand-receptor complexes	284:308	ligand-receptor complexes of this family	284:323	Previous x-ray structures of ligand-receptor complexes of this family lack the three membrane-proximal domains that are essential for signal transduction.
20489211	1	27	theme	receptor	170:177	arg1	gp130					131:135	gp130	131:135	gp130	131:135	gp130 is the shared signal-transducing receptor subunit for the large and important family of interleukin 6-like cytokines.
20489211	1	27	theme	receptor	170:177	arg1	subunit					179:185	the shared signal-transducing receptor subunit	140:185	the shared signal-transducing receptor subunit for the large and important family of interleukin 6-like cytokines	140:252	gp130 is the shared signal-transducing receptor subunit for the large and important family of interleukin 6-like cytokines.
20489211	0	28	theme	Crystal	0:6	arg1	structure					8:16	Crystal structure	0:16	Crystal structure of the entire ectodomain of gp130: insights into the molecular assembly of the tall cytokine receptor complexes.	0:129	Crystal structure of the entire ectodomain of gp130: insights into the molecular assembly of the tall cytokine receptor complexes.
20489211	8	29	theme	receptor-associated	1407:1425	arg1	kinases					1433:1439	receptor-associated Janus kinases	1407:1439	receptor-associated Janus kinases	1407:1439	Importantly, this geometry positions the C termini of the membrane-proximal fibronectin type III domains of the tall cytokine receptors in close proximity within the transmembrane complex, favorable for receptor-associated Janus kinases to trans-phosphorylate and activate each other.
20489211	3	30	theme	unliganded	546:555	arg1	form					557:560	an unliganded form	543:560	an unliganded form	543:560	Here we report the crystal structure of the entire extracellular portion of human gp130 (domains 1-6, D1-D6) at 3.6 A resolution, in an unliganded form, as well as a higher resolution structure of the membrane-proximal fibronectin type III domains (D4-D6) at 1.9 A.
20489211	3	31	theme	membrane-proximal	611:627	arg1	D4-D6					659:663	D4-D6	659:663	D4-D6	659:663	Here we report the crystal structure of the entire extracellular portion of human gp130 (domains 1-6, D1-D6) at 3.6 A resolution, in an unliganded form, as well as a higher resolution structure of the membrane-proximal fibronectin type III domains (D4-D6) at 1.9 A.
20489211	3	31	theme	membrane-proximal	611:627	arg1	domains					650:656	the membrane-proximal fibronectin type III domains	607:656	the membrane-proximal fibronectin type III domains (D4-D6)	607:664	Here we report the crystal structure of the entire extracellular portion of human gp130 (domains 1-6, D1-D6) at 3.6 A resolution, in an unliganded form, as well as a higher resolution structure of the membrane-proximal fibronectin type III domains (D4-D6) at 1.9 A.
20489211	7	32	theme	receptor	1111:1118	arg1	family					1120:1125	the entire tall receptor family	1095:1125	the entire tall receptor family	1095:1125	Key residues at this interface are highly conserved across the entire tall receptor family, suggesting that this acute bend may be a common feature of these receptors.
20489211	8	33	theme	receptors	1330:1338	arg1	domains					1301:1307	the membrane-proximal fibronectin type III domains	1258:1307	the membrane-proximal fibronectin type III domains of the tall cytokine receptors	1258:1338	Importantly, this geometry positions the C termini of the membrane-proximal fibronectin type III domains of the tall cytokine receptors in close proximity within the transmembrane complex, favorable for receptor-associated Janus kinases to trans-phosphorylate and activate each other.
20489211	8	33	theme	receptors	1330:1338	arg1	receptors					1330:1338	the tall cytokine receptors	1312:1338	the tall cytokine receptors	1312:1338	Importantly, this geometry positions the C termini of the membrane-proximal fibronectin type III domains of the tall cytokine receptors in close proximity within the transmembrane complex, favorable for receptor-associated Janus kinases to trans-phosphorylate and activate each other.
20489211	0	34	theme	cytokine	102:109	arg1	complexes					120:128	the tall cytokine receptor complexes	93:128	the tall cytokine receptor complexes	93:128	Crystal structure of the entire ectodomain of gp130: insights into the molecular assembly of the tall cytokine receptor complexes.
20489211	8	35	theme	domains	1301:1307	arg1	termini					1247:1253	the C termini	1241:1253	the C termini of the membrane-proximal fibronectin type III domains of the tall cytokine receptors	1241:1338	Importantly, this geometry positions the C termini of the membrane-proximal fibronectin type III domains of the tall cytokine receptors in close proximity within the transmembrane complex, favorable for receptor-associated Janus kinases to trans-phosphorylate and activate each other.
20489211	4	36	theme	atomic	702:707	arg1	structure					720:728	the first atomic resolution structure	692:728	the first atomic resolution structure of the complete ectodomain of any "tall" cytokine receptor	692:787	This represents the first atomic resolution structure of the complete ectodomain of any "tall" cytokine receptor.
20489211	3	37	theme	portion	475:481	arg1	structure					437:445	the crystal structure	425:445	the crystal structure of the entire extracellular portion of human gp130 (domains 1-6, D1-D6) at 3.6 A resolution	425:537	Here we report the crystal structure of the entire extracellular portion of human gp130 (domains 1-6, D1-D6) at 3.6 A resolution, in an unliganded form, as well as a higher resolution structure of the membrane-proximal fibronectin type III domains (D4-D6) at 1.9 A.
20489211	5	38	theme	little	871:876	arg1	change					889:894	little structural change	871:894	little structural change in gp130 upon ligand binding	871:923	These structures show that other than a reorientation of the D1 domain, there is little structural change in gp130 upon ligand binding.
20489211	0	39	theme	tall	97:100	arg1	complexes					120:128	the tall cytokine receptor complexes	93:128	the tall cytokine receptor complexes	93:128	Crystal structure of the entire ectodomain of gp130: insights into the molecular assembly of the tall cytokine receptor complexes.
20489211	8	40	theme	close	1343:1347	arg1	proximity					1349:1357	close proximity	1343:1357	close proximity within the transmembrane complex, favorable for receptor-associated Janus kinases to trans-phosphorylate	1343:1462	Importantly, this geometry positions the C termini of the membrane-proximal fibronectin type III domains of the tall cytokine receptors in close proximity within the transmembrane complex, favorable for receptor-associated Janus kinases to trans-phosphorylate and activate each other.
20489211	2	41	theme	complexes	300:308	arg1	structures					270:279	Previous x-ray structures	255:279	Previous x-ray structures of ligand-receptor complexes of this family	255:323	Previous x-ray structures of ligand-receptor complexes of this family lack the three membrane-proximal domains that are essential for signal transduction.
20489211	6	42	theme	D4	974:975	arg1	domains					984:990	the D4 and D5 domains	970:990	the D4 and D5 domains	970:990	They also reveal that the interface between the D4 and D5 domains forms an acute bend in the gp130 structure.
20489211	0	43	theme	ectodomain	32:41	arg1	structure					8:16	Crystal structure	0:16	Crystal structure of the entire ectodomain of gp130: insights into the molecular assembly of the tall cytokine receptor complexes.	0:129	Crystal structure of the entire ectodomain of gp130: insights into the molecular assembly of the tall cytokine receptor complexes.
20489211	3	44	theme	higher	576:581	arg1	structure					594:602	a higher resolution structure	574:602	a higher resolution structure of the membrane-proximal fibronectin type III domains (D4-D6)	574:664	Here we report the crystal structure of the entire extracellular portion of human gp130 (domains 1-6, D1-D6) at 3.6 A resolution, in an unliganded form, as well as a higher resolution structure of the membrane-proximal fibronectin type III domains (D4-D6) at 1.9 A.
20489211	0	45	theme	complexes	120:128	arg1	assembly					81:88	the molecular assembly	67:88	the molecular assembly of the tall cytokine receptor complexes	67:128	Crystal structure of the entire ectodomain of gp130: insights into the molecular assembly of the tall cytokine receptor complexes.
20489211	3	46	theme	entire	454:459	arg1	portion					475:481	the entire extracellular portion	450:481	the entire extracellular portion of human gp130 (domains 1-6, D1-D6) at 3.6 A resolution	450:537	Here we report the crystal structure of the entire extracellular portion of human gp130 (domains 1-6, D1-D6) at 3.6 A resolution, in an unliganded form, as well as a higher resolution structure of the membrane-proximal fibronectin type III domains (D4-D6) at 1.9 A.
20489211	4	47	theme	tall	765:768	arg1	receptor					780:787	any "tall" cytokine receptor	760:787	any "tall" cytokine receptor	760:787	This represents the first atomic resolution structure of the complete ectodomain of any "tall" cytokine receptor.
20489211	6	48	theme	D5	981:982	arg1	domains					984:990	the D4 and D5 domains	970:990	the D4 and D5 domains	970:990	They also reveal that the interface between the D4 and D5 domains forms an acute bend in the gp130 structure.
20489211	1	49	theme	large	195:199	arg1	family					215:220	the large and important family	191:220	the large and important family of interleukin 6-like cytokines	191:252	gp130 is the shared signal-transducing receptor subunit for the large and important family of interleukin 6-like cytokines.
20489211	0	50	theme	entire	25:30	arg1	ectodomain					32:41	the entire ectodomain	21:41	the entire ectodomain of gp130	21:50	Crystal structure of the entire ectodomain of gp130: insights into the molecular assembly of the tall cytokine receptor complexes.
20489211	0	50	theme	entire	25:30	arg1	gp130					46:50	gp130	46:50	gp130	46:50	Crystal structure of the entire ectodomain of gp130: insights into the molecular assembly of the tall cytokine receptor complexes.
20489211	0	51	theme	receptor	111:118	arg1	complexes					120:128	the tall cytokine receptor complexes	93:128	the tall cytokine receptor complexes	93:128	Crystal structure of the entire ectodomain of gp130: insights into the molecular assembly of the tall cytokine receptor complexes.
20489211	8	52	theme	fibronectin	1280:1290	arg1	domains					1301:1307	the membrane-proximal fibronectin type III domains	1258:1307	the membrane-proximal fibronectin type III domains of the tall cytokine receptors	1258:1338	Importantly, this geometry positions the C termini of the membrane-proximal fibronectin type III domains of the tall cytokine receptors in close proximity within the transmembrane complex, favorable for receptor-associated Janus kinases to trans-phosphorylate and activate each other.
20489211	8	52	theme	fibronectin	1280:1290	arg1	receptors					1330:1338	the tall cytokine receptors	1312:1338	the tall cytokine receptors	1312:1338	Importantly, this geometry positions the C termini of the membrane-proximal fibronectin type III domains of the tall cytokine receptors in close proximity within the transmembrane complex, favorable for receptor-associated Janus kinases to trans-phosphorylate and activate each other.
20489211	8	53	theme	type	1292:1295	arg1	domains					1301:1307	the membrane-proximal fibronectin type III domains	1258:1307	the membrane-proximal fibronectin type III domains of the tall cytokine receptors	1258:1338	Importantly, this geometry positions the C termini of the membrane-proximal fibronectin type III domains of the tall cytokine receptors in close proximity within the transmembrane complex, favorable for receptor-associated Janus kinases to trans-phosphorylate and activate each other.
20489211	8	53	theme	type	1292:1295	arg1	receptors					1330:1338	the tall cytokine receptors	1312:1338	the tall cytokine receptors	1312:1338	Importantly, this geometry positions the C termini of the membrane-proximal fibronectin type III domains of the tall cytokine receptors in close proximity within the transmembrane complex, favorable for receptor-associated Janus kinases to trans-phosphorylate and activate each other.
20489211	3	54	theme	extracellular	461:473	arg1	portion					475:481	the entire extracellular portion	450:481	the entire extracellular portion of human gp130 (domains 1-6, D1-D6) at 3.6 A resolution	450:537	Here we report the crystal structure of the entire extracellular portion of human gp130 (domains 1-6, D1-D6) at 3.6 A resolution, in an unliganded form, as well as a higher resolution structure of the membrane-proximal fibronectin type III domains (D4-D6) at 1.9 A.
20489211	0	55	theme	gp130	46:50	arg1	ectodomain					32:41	the entire ectodomain	21:41	the entire ectodomain of gp130	21:50	Crystal structure of the entire ectodomain of gp130: insights into the molecular assembly of the tall cytokine receptor complexes.
20489211	0	55	theme	gp130	46:50	arg1	gp130					46:50	gp130	46:50	gp130	46:50	Crystal structure of the entire ectodomain of gp130: insights into the molecular assembly of the tall cytokine receptor complexes.
20489211	7	56	theme	common	1169:1174	arg1	bend					1155:1158	this acute bend	1144:1158	this acute bend	1144:1158	Key residues at this interface are highly conserved across the entire tall receptor family, suggesting that this acute bend may be a common feature of these receptors.
20489211	7	56	theme	common	1169:1174	arg1	feature					1176:1182	a common feature	1167:1182	a common feature of these receptors	1167:1201	Key residues at this interface are highly conserved across the entire tall receptor family, suggesting that this acute bend may be a common feature of these receptors.
20489211	4	57	theme	cytokine	771:778	arg1	receptor					780:787	any "tall" cytokine receptor	760:787	any "tall" cytokine receptor	760:787	This represents the first atomic resolution structure of the complete ectodomain of any "tall" cytokine receptor.
20489211	2	58	theme	membrane-proximal	340:356	arg1	domains					358:364	the three membrane-proximal domains	330:364	the three membrane-proximal domains that are essential for signal transduction	330:407	Previous x-ray structures of ligand-receptor complexes of this family lack the three membrane-proximal domains that are essential for signal transduction.
20489211	2	58	theme	membrane-proximal	340:356	arg1	essential					375:383	essential	375:383	essential	375:383	Previous x-ray structures of ligand-receptor complexes of this family lack the three membrane-proximal domains that are essential for signal transduction.
20489211	7	59	from	interface	1057:1065	arg1	residues					1040:1047	Key residues	1036:1047	Key residues at this interface	1036:1065	Key residues at this interface are highly conserved across the entire tall receptor family, suggesting that this acute bend may be a common feature of these receptors.
20489211	7	60	theme	acute	1149:1153	arg1	bend					1155:1158	this acute bend	1144:1158	this acute bend	1144:1158	Key residues at this interface are highly conserved across the entire tall receptor family, suggesting that this acute bend may be a common feature of these receptors.
20489211	7	60	theme	acute	1149:1153	arg1	feature					1176:1182	a common feature	1167:1182	a common feature of these receptors	1167:1201	Key residues at this interface are highly conserved across the entire tall receptor family, suggesting that this acute bend may be a common feature of these receptors.
20489211	4	61	theme	"	769:769	arg1	receptor					780:787	any "tall" cytokine receptor	760:787	any "tall" cytokine receptor	760:787	This represents the first atomic resolution structure of the complete ectodomain of any "tall" cytokine receptor.
20489211	3	62	from	portion	475:481	arg1	resolution					528:537	3.6 A resolution	522:537	3.6 A resolution	522:537	Here we report the crystal structure of the entire extracellular portion of human gp130 (domains 1-6, D1-D6) at 3.6 A resolution, in an unliganded form, as well as a higher resolution structure of the membrane-proximal fibronectin type III domains (D4-D6) at 1.9 A.
20489211	5	63	theme	domain	854:859	arg1	reorientation					830:842	a reorientation	828:842	a reorientation of the D1 domain	828:859	These structures show that other than a reorientation of the D1 domain, there is little structural change in gp130 upon ligand binding.
20489211	3	64	theme	domains	650:656	arg1	structure					594:602	a higher resolution structure	574:602	a higher resolution structure of the membrane-proximal fibronectin type III domains (D4-D6)	574:664	Here we report the crystal structure of the entire extracellular portion of human gp130 (domains 1-6, D1-D6) at 3.6 A resolution, in an unliganded form, as well as a higher resolution structure of the membrane-proximal fibronectin type III domains (D4-D6) at 1.9 A.
20489211	2	65	theme	Previous	255:262	arg1	structures					270:279	Previous x-ray structures	255:279	Previous x-ray structures of ligand-receptor complexes of this family	255:323	Previous x-ray structures of ligand-receptor complexes of this family lack the three membrane-proximal domains that are essential for signal transduction.
20489211	3	66	theme	human	486:490	arg1	domains					499:505	domains 1-6	499:509	domains 1-6	499:509	Here we report the crystal structure of the entire extracellular portion of human gp130 (domains 1-6, D1-D6) at 3.6 A resolution, in an unliganded form, as well as a higher resolution structure of the membrane-proximal fibronectin type III domains (D4-D6) at 1.9 A.
20489211	3	66	theme	human	486:490	arg1	gp130					492:496	human gp130	486:496	human gp130 (domains 1-6, D1-D6) at 3.6 A resolution	486:537	Here we report the crystal structure of the entire extracellular portion of human gp130 (domains 1-6, D1-D6) at 3.6 A resolution, in an unliganded form, as well as a higher resolution structure of the membrane-proximal fibronectin type III domains (D4-D6) at 1.9 A.
20489211	5	67	theme	structural	878:887	arg1	change					889:894	little structural change	871:894	little structural change in gp130 upon ligand binding	871:923	These structures show that other than a reorientation of the D1 domain, there is little structural change in gp130 upon ligand binding.
20489211	1	68	theme	important	205:213	arg1	family					215:220	the large and important family	191:220	the large and important family of interleukin 6-like cytokines	191:252	gp130 is the shared signal-transducing receptor subunit for the large and important family of interleukin 6-like cytokines.
20489211	3	69	dep	domains	499:505	arg1	D1-D6					512:516	D1-D6	512:516	D1-D6	512:516	Here we report the crystal structure of the entire extracellular portion of human gp130 (domains 1-6, D1-D6) at 3.6 A resolution, in an unliganded form, as well as a higher resolution structure of the membrane-proximal fibronectin type III domains (D4-D6) at 1.9 A.
20489211	3	69	dep	domains	499:505	arg1	1-6					507:509	1-6	507:509	1-6	507:509	Here we report the crystal structure of the entire extracellular portion of human gp130 (domains 1-6, D1-D6) at 3.6 A resolution, in an unliganded form, as well as a higher resolution structure of the membrane-proximal fibronectin type III domains (D4-D6) at 1.9 A.
20489211	3	70	theme	fibronectin	629:639	arg1	D4-D6					659:663	D4-D6	659:663	D4-D6	659:663	Here we report the crystal structure of the entire extracellular portion of human gp130 (domains 1-6, D1-D6) at 3.6 A resolution, in an unliganded form, as well as a higher resolution structure of the membrane-proximal fibronectin type III domains (D4-D6) at 1.9 A.
20489211	3	70	theme	fibronectin	629:639	arg1	domains					650:656	the membrane-proximal fibronectin type III domains	607:656	the membrane-proximal fibronectin type III domains (D4-D6)	607:664	Here we report the crystal structure of the entire extracellular portion of human gp130 (domains 1-6, D1-D6) at 3.6 A resolution, in an unliganded form, as well as a higher resolution structure of the membrane-proximal fibronectin type III domains (D4-D6) at 1.9 A.
20489211	3	71	theme	A	526:526	arg1	resolution					528:537	3.6 A resolution	522:537	3.6 A resolution	522:537	Here we report the crystal structure of the entire extracellular portion of human gp130 (domains 1-6, D1-D6) at 3.6 A resolution, in an unliganded form, as well as a higher resolution structure of the membrane-proximal fibronectin type III domains (D4-D6) at 1.9 A.
20489211	4	72	theme	first	696:700	arg1	structure					720:728	the first atomic resolution structure	692:728	the first atomic resolution structure of the complete ectodomain of any "tall" cytokine receptor	692:787	This represents the first atomic resolution structure of the complete ectodomain of any "tall" cytokine receptor.
20489211	3	73	theme	gp130	492:496	arg1	portion					475:481	the entire extracellular portion	450:481	the entire extracellular portion of human gp130 (domains 1-6, D1-D6) at 3.6 A resolution	450:537	Here we report the crystal structure of the entire extracellular portion of human gp130 (domains 1-6, D1-D6) at 3.6 A resolution, in an unliganded form, as well as a higher resolution structure of the membrane-proximal fibronectin type III domains (D4-D6) at 1.9 A.
20489211	4	74	theme	ectodomain	746:755	arg1	structure					720:728	the first atomic resolution structure	692:728	the first atomic resolution structure of the complete ectodomain of any "tall" cytokine receptor	692:787	This represents the first atomic resolution structure of the complete ectodomain of any "tall" cytokine receptor.
20489211	3	75	theme	type	641:644	arg1	D4-D6					659:663	D4-D6	659:663	D4-D6	659:663	Here we report the crystal structure of the entire extracellular portion of human gp130 (domains 1-6, D1-D6) at 3.6 A resolution, in an unliganded form, as well as a higher resolution structure of the membrane-proximal fibronectin type III domains (D4-D6) at 1.9 A.
20489211	3	75	theme	type	641:644	arg1	domains					650:656	the membrane-proximal fibronectin type III domains	607:656	the membrane-proximal fibronectin type III domains (D4-D6)	607:664	Here we report the crystal structure of the entire extracellular portion of human gp130 (domains 1-6, D1-D6) at 3.6 A resolution, in an unliganded form, as well as a higher resolution structure of the membrane-proximal fibronectin type III domains (D4-D6) at 1.9 A.
20489211	0	76	dep	structure	8:16	arg1	insights					53:60	insights	53:60	Crystal structure of the entire ectodomain of gp130: insights into the molecular assembly of the tall cytokine receptor complexes.	0:129	Crystal structure of the entire ectodomain of gp130: insights into the molecular assembly of the tall cytokine receptor complexes.
20489211	7	77	theme	receptors	1193:1201	arg1	bend					1155:1158	this acute bend	1144:1158	this acute bend	1144:1158	Key residues at this interface are highly conserved across the entire tall receptor family, suggesting that this acute bend may be a common feature of these receptors.
20489211	7	77	theme	receptors	1193:1201	arg1	feature					1176:1182	a common feature	1167:1182	a common feature of these receptors	1167:1201	Key residues at this interface are highly conserved across the entire tall receptor family, suggesting that this acute bend may be a common feature of these receptors.
20489211	5	78	from	change	889:894	arg1	gp130					899:903	gp130	899:903	gp130	899:903	These structures show that other than a reorientation of the D1 domain, there is little structural change in gp130 upon ligand binding.
20489211	6	79	from	bend	1007:1010	arg1	structure					1025:1033	the gp130 structure	1015:1033	the gp130 structure	1015:1033	They also reveal that the interface between the D4 and D5 domains forms an acute bend in the gp130 structure.
20489211	8	80	theme	cytokine	1321:1328	arg1	receptors					1330:1338	the tall cytokine receptors	1312:1338	the tall cytokine receptors	1312:1338	Importantly, this geometry positions the C termini of the membrane-proximal fibronectin type III domains of the tall cytokine receptors in close proximity within the transmembrane complex, favorable for receptor-associated Janus kinases to trans-phosphorylate and activate each other.
20489211	5	81	theme	ligand	910:915	arg1	binding					917:923	ligand binding	910:923	ligand binding	910:923	These structures show that other than a reorientation of the D1 domain, there is little structural change in gp130 upon ligand binding.
20489211	1	82	theme	interleukin	225:235	arg1	cytokines					244:252	interleukin 6-like cytokines	225:252	interleukin 6-like cytokines	225:252	gp130 is the shared signal-transducing receptor subunit for the large and important family of interleukin 6-like cytokines.
20237569	0	0	theme	factor	69:74	arg1	complexes					76:84	vitamin-B(12)-intrinsic factor complexes	45:84	vitamin-B(12)-intrinsic factor complexes	45:84	Structural basis for receptor recognition of vitamin-B(12)-intrinsic factor complexes.
20237569	2	1	theme	intrinsic	270:278	arg1	factor					280:285	the gastric intrinsic factor	258:285	the gastric intrinsic factor (IF)	258:290	This occurs by the combined action of the gastric intrinsic factor (IF) and the ileal endocytic cubam receptor formed by the 460-kilodalton (kDa) protein cubilin and the 45-kDa transmembrane protein amnionless.
20237569	7	2	theme	interactions	1354:1365	arg1	theme					1312:1316	a common theme	1303:1316	a common theme of Ca(2+)-dependent ligand-receptor interactions	1303:1365	Finally, the comparison of Ca(2+)-binding CUB domains and the low-density lipoprotein (LDL) receptor-type A modules suggests that the electrostatic pairing of a basic ligand arginine/lysine residue with Ca(2+)-coordinating acidic aspartates/glutamates is a common theme of Ca(2+)-dependent ligand-receptor interactions.
20237569	7	2	theme	interactions	1354:1365	arg1	pairing					1196:1202	the electrostatic pairing	1178:1202	the electrostatic pairing of a basic ligand arginine/lysine residue with Ca(2+)-coordinating acidic aspartates/glutamates	1178:1298	Finally, the comparison of Ca(2+)-binding CUB domains and the low-density lipoprotein (LDL) receptor-type A modules suggests that the electrostatic pairing of a basic ligand arginine/lysine residue with Ca(2+)-coordinating acidic aspartates/glutamates is a common theme of Ca(2+)-dependent ligand-receptor interactions.
20237569	0	3	theme	-intrinsic	58:67	arg1	complexes					76:84	vitamin-B(12)-intrinsic factor complexes	45:84	vitamin-B(12)-intrinsic factor complexes	45:84	Structural basis for receptor recognition of vitamin-B(12)-intrinsic factor complexes.
20237569	7	4	theme	-coordinating	1257:1269	arg1	aspartates/glutamates					1278:1298	Ca(2+)-coordinating acidic aspartates/glutamates	1251:1298	Ca(2+)-coordinating acidic aspartates/glutamates	1251:1298	Finally, the comparison of Ca(2+)-binding CUB domains and the low-density lipoprotein (LDL) receptor-type A modules suggests that the electrostatic pairing of a basic ligand arginine/lysine residue with Ca(2+)-coordinating acidic aspartates/glutamates is a common theme of Ca(2+)-dependent ligand-receptor interactions.
20237569	2	5	theme	gastric	262:268	arg1	factor					280:285	the gastric intrinsic factor	258:285	the gastric intrinsic factor (IF)	258:290	This occurs by the combined action of the gastric intrinsic factor (IF) and the ileal endocytic cubam receptor formed by the 460-kilodalton (kDa) protein cubilin and the 45-kDa transmembrane protein amnionless.
20237569	5	6	theme	distant	833:839	arg1	domains					845:851	two distant CUB domains	829:851	two distant CUB domains	829:851	The structure provides insight into how several CUB (for 'complement C1r/C1s, Uegf, Bmp1') domains collectively function as modular ligand-binding regions, and how two distant CUB domains embrace the Cbl molecule by binding the two IF domains in a Ca(2+)-dependent manner.
20237569	3	7	theme	function	439:446	arg1	Loss					431:434	Loss	431:434	Loss of function of any of these proteins	431:471	Loss of function of any of these proteins ultimately leads to Cbl deficiency in man.
20237569	6	8	theme	dual-point	943:952	arg1	model					954:958	This dual-point model	938:958	This dual-point model	938:958	This dual-point model provides a probable explanation of how Cbl indirectly induces ligand-receptor coupling.
20237569	7	9	theme	-dependent	1327:1336	arg1	interactions					1354:1365	Ca(2+)-dependent ligand-receptor interactions	1321:1365	Ca(2+)-dependent ligand-receptor interactions	1321:1365	Finally, the comparison of Ca(2+)-binding CUB domains and the low-density lipoprotein (LDL) receptor-type A modules suggests that the electrostatic pairing of a basic ligand arginine/lysine residue with Ca(2+)-coordinating acidic aspartates/glutamates is a common theme of Ca(2+)-dependent ligand-receptor interactions.
20237569	0	10	theme	complexes	76:84	arg1	recognition					30:40	receptor recognition	21:40	receptor recognition of vitamin-B(12)-intrinsic factor complexes	21:84	Structural basis for receptor recognition of vitamin-B(12)-intrinsic factor complexes.
20237569	3	11	from	deficiency	497:506	arg1	man					511:513	man	511:513	man	511:513	Loss of function of any of these proteins ultimately leads to Cbl deficiency in man.
20237569	7	12	theme	ligand-receptor	1338:1352	arg1	interactions					1354:1365	Ca(2+)-dependent ligand-receptor interactions	1321:1365	Ca(2+)-dependent ligand-receptor interactions	1321:1365	Finally, the comparison of Ca(2+)-binding CUB domains and the low-density lipoprotein (LDL) receptor-type A modules suggests that the electrostatic pairing of a basic ligand arginine/lysine residue with Ca(2+)-coordinating acidic aspartates/glutamates is a common theme of Ca(2+)-dependent ligand-receptor interactions.
20237569	2	13	theme	protein	411:417	arg1	amnionless					419:428	the 460-kilodalton (kDa) protein cubilin and the 45-kDa transmembrane protein amnionless	341:428	the 460-kilodalton (kDa) protein cubilin and the 45-kDa transmembrane protein amnionless	341:428	This occurs by the combined action of the gastric intrinsic factor (IF) and the ileal endocytic cubam receptor formed by the 460-kilodalton (kDa) protein cubilin and the 45-kDa transmembrane protein amnionless.
20237569	7	14	theme	electrostatic	1182:1194	arg1	theme					1312:1316	a common theme	1303:1316	a common theme of Ca(2+)-dependent ligand-receptor interactions	1303:1365	Finally, the comparison of Ca(2+)-binding CUB domains and the low-density lipoprotein (LDL) receptor-type A modules suggests that the electrostatic pairing of a basic ligand arginine/lysine residue with Ca(2+)-coordinating acidic aspartates/glutamates is a common theme of Ca(2+)-dependent ligand-receptor interactions.
20237569	7	14	theme	electrostatic	1182:1194	arg1	pairing					1196:1202	the electrostatic pairing	1178:1202	the electrostatic pairing of a basic ligand arginine/lysine residue with Ca(2+)-coordinating acidic aspartates/glutamates	1178:1298	Finally, the comparison of Ca(2+)-binding CUB domains and the low-density lipoprotein (LDL) receptor-type A modules suggests that the electrostatic pairing of a basic ligand arginine/lysine residue with Ca(2+)-coordinating acidic aspartates/glutamates is a common theme of Ca(2+)-dependent ligand-receptor interactions.
20237569	5	15	theme	several	705:711	arg1	domains					756:762	several CUB (for 'complement C1r/C1s, Uegf, Bmp1') domains	705:762	several CUB (for 'complement C1r/C1s, Uegf, Bmp1') domains	705:762	The structure provides insight into how several CUB (for 'complement C1r/C1s, Uegf, Bmp1') domains collectively function as modular ligand-binding regions, and how two distant CUB domains embrace the Cbl molecule by binding the two IF domains in a Ca(2+)-dependent manner.
20237569	5	15	theme	several	705:711	arg1	regions					812:818	modular ligand-binding regions	789:818	modular ligand-binding regions	789:818	The structure provides insight into how several CUB (for 'complement C1r/C1s, Uegf, Bmp1') domains collectively function as modular ligand-binding regions, and how two distant CUB domains embrace the Cbl molecule by binding the two IF domains in a Ca(2+)-dependent manner.
20237569	5	15	theme	several	705:711	arg1	molecule					869:876	the Cbl molecule	861:876	the Cbl molecule	861:876	The structure provides insight into how several CUB (for 'complement C1r/C1s, Uegf, Bmp1') domains collectively function as modular ligand-binding regions, and how two distant CUB domains embrace the Cbl molecule by binding the two IF domains in a Ca(2+)-dependent manner.
20237569	7	16	theme	ligand	1215:1220	arg1	residue					1238:1244	a basic ligand arginine/lysine residue	1207:1244	a basic ligand arginine/lysine residue	1207:1244	Finally, the comparison of Ca(2+)-binding CUB domains and the low-density lipoprotein (LDL) receptor-type A modules suggests that the electrostatic pairing of a basic ligand arginine/lysine residue with Ca(2+)-coordinating acidic aspartates/glutamates is a common theme of Ca(2+)-dependent ligand-receptor interactions.
20237569	5	17	theme	complement	723:732	arg1	Bmp1					749:752	complement C1r/C1s, Uegf, Bmp1	723:752	Bmp1	749:752	The structure provides insight into how several CUB (for 'complement C1r/C1s, Uegf, Bmp1') domains collectively function as modular ligand-binding regions, and how two distant CUB domains embrace the Cbl molecule by binding the two IF domains in a Ca(2+)-dependent manner.
20237569	2	18	theme	transmembrane	397:409	arg1	protein					411:417	the 45-kDa transmembrane protein	386:417	the 45-kDa transmembrane protein	386:417	This occurs by the combined action of the gastric intrinsic factor (IF) and the ileal endocytic cubam receptor formed by the 460-kilodalton (kDa) protein cubilin and the 45-kDa transmembrane protein amnionless.
20237569	5	19	from	domains	900:906	arg1	manner					930:935	a Ca(2+)-dependent manner	911:935	a Ca(2+)-dependent manner	911:935	The structure provides insight into how several CUB (for 'complement C1r/C1s, Uegf, Bmp1') domains collectively function as modular ligand-binding regions, and how two distant CUB domains embrace the Cbl molecule by binding the two IF domains in a Ca(2+)-dependent manner.
20237569	6	20	theme	probable	971:978	arg1	explanation					980:990	a probable explanation	969:990	a probable explanation of how Cbl indirectly induces ligand-receptor coupling	969:1045	This dual-point model provides a probable explanation of how Cbl indirectly induces ligand-receptor coupling.
20237569	4	21	theme	crystal	536:542	arg1	structure					544:552	the crystal structure	532:552	the crystal structure of the complex between IF-Cbl and the cubilin IF-Cbl-binding-region (CUB(5-8)) determined at 3.3 A resolution	532:662	Here we present the crystal structure of the complex between IF-Cbl and the cubilin IF-Cbl-binding-region (CUB(5-8)) determined at 3.3 A resolution.
20237569	2	22	theme	460-kilodalton	345:358	arg1	cubilin					374:380	460-kilodalton (kDa) protein cubilin	345:380	460-kilodalton (kDa) protein cubilin	345:380	This occurs by the combined action of the gastric intrinsic factor (IF) and the ileal endocytic cubam receptor formed by the 460-kilodalton (kDa) protein cubilin and the 45-kDa transmembrane protein amnionless.
20237569	2	23	theme	cubilin	374:380	arg1	amnionless					419:428	the 460-kilodalton (kDa) protein cubilin and the 45-kDa transmembrane protein amnionless	341:428	the 460-kilodalton (kDa) protein cubilin and the 45-kDa transmembrane protein amnionless	341:428	This occurs by the combined action of the gastric intrinsic factor (IF) and the ileal endocytic cubam receptor formed by the 460-kilodalton (kDa) protein cubilin and the 45-kDa transmembrane protein amnionless.
20237569	7	24	theme	CUB	1090:1092	arg1	domains					1094:1100	Ca(2+)-binding CUB domains	1075:1100	Ca(2+)-binding CUB domains	1075:1100	Finally, the comparison of Ca(2+)-binding CUB domains and the low-density lipoprotein (LDL) receptor-type A modules suggests that the electrostatic pairing of a basic ligand arginine/lysine residue with Ca(2+)-coordinating acidic aspartates/glutamates is a common theme of Ca(2+)-dependent ligand-receptor interactions.
20237569	1	25	theme	bacterial	123:131	arg1	Cobalamin					87:95	Cobalamin	87:95	Cobalamin (Cbl, vitamin B(12))	87:116	Cobalamin (Cbl, vitamin B(12)) is a bacterial organic compound and an essential coenzyme in mammals, which take it up from the diet.
20237569	1	25	theme	bacterial	123:131	arg1	compound					141:148	a bacterial organic compound	121:148	a bacterial organic compound	121:148	Cobalamin (Cbl, vitamin B(12)) is a bacterial organic compound and an essential coenzyme in mammals, which take it up from the diet.
20237569	0	26	theme	Structural	0:9	arg1	basis					11:15	Structural basis	0:15	Structural basis for receptor recognition of vitamin-B(12)-intrinsic factor complexes.	0:85	Structural basis for receptor recognition of vitamin-B(12)-intrinsic factor complexes.
20237569	7	27	theme	residue	1238:1244	arg1	theme					1312:1316	a common theme	1303:1316	a common theme of Ca(2+)-dependent ligand-receptor interactions	1303:1365	Finally, the comparison of Ca(2+)-binding CUB domains and the low-density lipoprotein (LDL) receptor-type A modules suggests that the electrostatic pairing of a basic ligand arginine/lysine residue with Ca(2+)-coordinating acidic aspartates/glutamates is a common theme of Ca(2+)-dependent ligand-receptor interactions.
20237569	7	27	theme	residue	1238:1244	arg1	pairing					1196:1202	the electrostatic pairing	1178:1202	the electrostatic pairing of a basic ligand arginine/lysine residue with Ca(2+)-coordinating acidic aspartates/glutamates	1178:1298	Finally, the comparison of Ca(2+)-binding CUB domains and the low-density lipoprotein (LDL) receptor-type A modules suggests that the electrostatic pairing of a basic ligand arginine/lysine residue with Ca(2+)-coordinating acidic aspartates/glutamates is a common theme of Ca(2+)-dependent ligand-receptor interactions.
20237569	7	28	theme	common	1305:1310	arg1	theme					1312:1316	a common theme	1303:1316	a common theme of Ca(2+)-dependent ligand-receptor interactions	1303:1365	Finally, the comparison of Ca(2+)-binding CUB domains and the low-density lipoprotein (LDL) receptor-type A modules suggests that the electrostatic pairing of a basic ligand arginine/lysine residue with Ca(2+)-coordinating acidic aspartates/glutamates is a common theme of Ca(2+)-dependent ligand-receptor interactions.
20237569	7	28	theme	common	1305:1310	arg1	pairing					1196:1202	the electrostatic pairing	1178:1202	the electrostatic pairing of a basic ligand arginine/lysine residue with Ca(2+)-coordinating acidic aspartates/glutamates	1178:1298	Finally, the comparison of Ca(2+)-binding CUB domains and the low-density lipoprotein (LDL) receptor-type A modules suggests that the electrostatic pairing of a basic ligand arginine/lysine residue with Ca(2+)-coordinating acidic aspartates/glutamates is a common theme of Ca(2+)-dependent ligand-receptor interactions.
20237569	5	29	dep	Bmp1	749:752	arg1	Uegf					743:746	complement C1r/C1s, Uegf, Bmp1	723:752	Uegf	743:746	The structure provides insight into how several CUB (for 'complement C1r/C1s, Uegf, Bmp1') domains collectively function as modular ligand-binding regions, and how two distant CUB domains embrace the Cbl molecule by binding the two IF domains in a Ca(2+)-dependent manner.
20237569	7	30	theme	modules	1156:1162	arg1	comparison					1061:1070	the comparison	1057:1070	the comparison of Ca(2+)-binding CUB domains and the low-density lipoprotein (LDL) receptor-type A modules	1057:1162	Finally, the comparison of Ca(2+)-binding CUB domains and the low-density lipoprotein (LDL) receptor-type A modules suggests that the electrostatic pairing of a basic ligand arginine/lysine residue with Ca(2+)-coordinating acidic aspartates/glutamates is a common theme of Ca(2+)-dependent ligand-receptor interactions.
20237569	1	31	theme	organic	133:139	arg1	Cobalamin					87:95	Cobalamin	87:95	Cobalamin (Cbl, vitamin B(12))	87:116	Cobalamin (Cbl, vitamin B(12)) is a bacterial organic compound and an essential coenzyme in mammals, which take it up from the diet.
20237569	1	31	theme	organic	133:139	arg1	compound					141:148	a bacterial organic compound	121:148	a bacterial organic compound	121:148	Cobalamin (Cbl, vitamin B(12)) is a bacterial organic compound and an essential coenzyme in mammals, which take it up from the diet.
20237569	0	32	theme	receptor	21:28	arg1	recognition					30:40	receptor recognition	21:40	receptor recognition of vitamin-B(12)-intrinsic factor complexes	21:84	Structural basis for receptor recognition of vitamin-B(12)-intrinsic factor complexes.
20237569	3	33	theme	any	451:453	arg1	Loss					431:434	Loss	431:434	Loss of function of any of these proteins	431:471	Loss of function of any of these proteins ultimately leads to Cbl deficiency in man.
20237569	2	34	theme	receptor	322:329	arg1	action					248:253	the combined action	235:253	the combined action of the gastric intrinsic factor (IF) and the ileal endocytic cubam receptor formed by the 460-kilodalton (kDa) protein cubilin and the 45-kDa transmembrane protein amnionless	235:428	This occurs by the combined action of the gastric intrinsic factor (IF) and the ileal endocytic cubam receptor formed by the 460-kilodalton (kDa) protein cubilin and the 45-kDa transmembrane protein amnionless.
20237569	7	35	theme	basic	1209:1213	arg1	residue					1238:1244	a basic ligand arginine/lysine residue	1207:1244	a basic ligand arginine/lysine residue	1207:1244	Finally, the comparison of Ca(2+)-binding CUB domains and the low-density lipoprotein (LDL) receptor-type A modules suggests that the electrostatic pairing of a basic ligand arginine/lysine residue with Ca(2+)-coordinating acidic aspartates/glutamates is a common theme of Ca(2+)-dependent ligand-receptor interactions.
20237569	5	36	theme	ligand-binding	797:810	arg1	domains					756:762	several CUB (for 'complement C1r/C1s, Uegf, Bmp1') domains	705:762	several CUB (for 'complement C1r/C1s, Uegf, Bmp1') domains	705:762	The structure provides insight into how several CUB (for 'complement C1r/C1s, Uegf, Bmp1') domains collectively function as modular ligand-binding regions, and how two distant CUB domains embrace the Cbl molecule by binding the two IF domains in a Ca(2+)-dependent manner.
20237569	5	36	theme	ligand-binding	797:810	arg1	regions					812:818	modular ligand-binding regions	789:818	modular ligand-binding regions	789:818	The structure provides insight into how several CUB (for 'complement C1r/C1s, Uegf, Bmp1') domains collectively function as modular ligand-binding regions, and how two distant CUB domains embrace the Cbl molecule by binding the two IF domains in a Ca(2+)-dependent manner.
20237569	5	36	theme	ligand-binding	797:810	arg1	molecule					869:876	the Cbl molecule	861:876	the Cbl molecule	861:876	The structure provides insight into how several CUB (for 'complement C1r/C1s, Uegf, Bmp1') domains collectively function as modular ligand-binding regions, and how two distant CUB domains embrace the Cbl molecule by binding the two IF domains in a Ca(2+)-dependent manner.
20237569	2	37	theme	cubam	316:320	arg1	receptor					322:329	the ileal endocytic cubam receptor	296:329	the ileal endocytic cubam receptor formed by the 460-kilodalton (kDa) protein cubilin and the 45-kDa transmembrane protein amnionless	296:428	This occurs by the combined action of the gastric intrinsic factor (IF) and the ileal endocytic cubam receptor formed by the 460-kilodalton (kDa) protein cubilin and the 45-kDa transmembrane protein amnionless.
20237569	2	38	theme	protein	366:372	arg1	cubilin					374:380	460-kilodalton (kDa) protein cubilin	345:380	460-kilodalton (kDa) protein cubilin	345:380	This occurs by the combined action of the gastric intrinsic factor (IF) and the ileal endocytic cubam receptor formed by the 460-kilodalton (kDa) protein cubilin and the 45-kDa transmembrane protein amnionless.
20237569	7	39	theme	domains	1094:1100	arg1	comparison					1061:1070	the comparison	1057:1070	the comparison of Ca(2+)-binding CUB domains and the low-density lipoprotein (LDL) receptor-type A modules	1057:1162	Finally, the comparison of Ca(2+)-binding CUB domains and the low-density lipoprotein (LDL) receptor-type A modules suggests that the electrostatic pairing of a basic ligand arginine/lysine residue with Ca(2+)-coordinating acidic aspartates/glutamates is a common theme of Ca(2+)-dependent ligand-receptor interactions.
20237569	5	40	theme	CUB	713:715	arg1	domains					756:762	several CUB (for 'complement C1r/C1s, Uegf, Bmp1') domains	705:762	several CUB (for 'complement C1r/C1s, Uegf, Bmp1') domains	705:762	The structure provides insight into how several CUB (for 'complement C1r/C1s, Uegf, Bmp1') domains collectively function as modular ligand-binding regions, and how two distant CUB domains embrace the Cbl molecule by binding the two IF domains in a Ca(2+)-dependent manner.
20237569	5	40	theme	CUB	713:715	arg1	regions					812:818	modular ligand-binding regions	789:818	modular ligand-binding regions	789:818	The structure provides insight into how several CUB (for 'complement C1r/C1s, Uegf, Bmp1') domains collectively function as modular ligand-binding regions, and how two distant CUB domains embrace the Cbl molecule by binding the two IF domains in a Ca(2+)-dependent manner.
20237569	5	40	theme	CUB	713:715	arg1	molecule					869:876	the Cbl molecule	861:876	the Cbl molecule	861:876	The structure provides insight into how several CUB (for 'complement C1r/C1s, Uegf, Bmp1') domains collectively function as modular ligand-binding regions, and how two distant CUB domains embrace the Cbl molecule by binding the two IF domains in a Ca(2+)-dependent manner.
20237569	5	41	theme	C1r/C1s	734:740	arg1	Bmp1					749:752	complement C1r/C1s, Uegf, Bmp1	723:752	Bmp1	749:752	The structure provides insight into how several CUB (for 'complement C1r/C1s, Uegf, Bmp1') domains collectively function as modular ligand-binding regions, and how two distant CUB domains embrace the Cbl molecule by binding the two IF domains in a Ca(2+)-dependent manner.
20237569	2	42	theme	endocytic	306:314	arg1	receptor					322:329	the ileal endocytic cubam receptor	296:329	the ileal endocytic cubam receptor formed by the 460-kilodalton (kDa) protein cubilin and the 45-kDa transmembrane protein amnionless	296:428	This occurs by the combined action of the gastric intrinsic factor (IF) and the ileal endocytic cubam receptor formed by the 460-kilodalton (kDa) protein cubilin and the 45-kDa transmembrane protein amnionless.
20237569	3	43	theme	Cbl	493:495	arg1	deficiency					497:506	Cbl deficiency	493:506	Cbl deficiency in man	493:513	Loss of function of any of these proteins ultimately leads to Cbl deficiency in man.
20237569	1	44	theme	essential	157:165	arg1	coenzyme					167:174	an essential coenzyme	154:174	an essential coenzyme in mammals	154:185	Cobalamin (Cbl, vitamin B(12)) is a bacterial organic compound and an essential coenzyme in mammals, which take it up from the diet.
20237569	2	45	theme	kDa	361:363	arg1	cubilin					374:380	460-kilodalton (kDa) protein cubilin	345:380	460-kilodalton (kDa) protein cubilin	345:380	This occurs by the combined action of the gastric intrinsic factor (IF) and the ileal endocytic cubam receptor formed by the 460-kilodalton (kDa) protein cubilin and the 45-kDa transmembrane protein amnionless.
20237569	5	46	theme	Cbl	865:867	arg1	domains					756:762	several CUB (for 'complement C1r/C1s, Uegf, Bmp1') domains	705:762	several CUB (for 'complement C1r/C1s, Uegf, Bmp1') domains	705:762	The structure provides insight into how several CUB (for 'complement C1r/C1s, Uegf, Bmp1') domains collectively function as modular ligand-binding regions, and how two distant CUB domains embrace the Cbl molecule by binding the two IF domains in a Ca(2+)-dependent manner.
20237569	5	46	theme	Cbl	865:867	arg1	regions					812:818	modular ligand-binding regions	789:818	modular ligand-binding regions	789:818	The structure provides insight into how several CUB (for 'complement C1r/C1s, Uegf, Bmp1') domains collectively function as modular ligand-binding regions, and how two distant CUB domains embrace the Cbl molecule by binding the two IF domains in a Ca(2+)-dependent manner.
20237569	5	46	theme	Cbl	865:867	arg1	molecule					869:876	the Cbl molecule	861:876	the Cbl molecule	861:876	The structure provides insight into how several CUB (for 'complement C1r/C1s, Uegf, Bmp1') domains collectively function as modular ligand-binding regions, and how two distant CUB domains embrace the Cbl molecule by binding the two IF domains in a Ca(2+)-dependent manner.
20237569	4	47	theme	cubilin	592:598	arg1	CUB					623:625	CUB(5-8)	623:630	CUB(5-8)	623:630	Here we present the crystal structure of the complex between IF-Cbl and the cubilin IF-Cbl-binding-region (CUB(5-8)) determined at 3.3 A resolution.
20237569	4	47	theme	cubilin	592:598	arg1	IF-Cbl-binding-region					600:620	the cubilin IF-Cbl-binding-region	588:620	the cubilin IF-Cbl-binding-region (CUB(5-8)) determined at 3.3 A resolution	588:662	Here we present the crystal structure of the complex between IF-Cbl and the cubilin IF-Cbl-binding-region (CUB(5-8)) determined at 3.3 A resolution.
20237569	0	48	theme	vitamin-B	45:53	arg1	complexes					76:84	vitamin-B(12)-intrinsic factor complexes	45:84	vitamin-B(12)-intrinsic factor complexes	45:84	Structural basis for receptor recognition of vitamin-B(12)-intrinsic factor complexes.
20237569	5	49	theme	-dependent	919:928	arg1	manner					930:935	a Ca(2+)-dependent manner	911:935	a Ca(2+)-dependent manner	911:935	The structure provides insight into how several CUB (for 'complement C1r/C1s, Uegf, Bmp1') domains collectively function as modular ligand-binding regions, and how two distant CUB domains embrace the Cbl molecule by binding the two IF domains in a Ca(2+)-dependent manner.
20237569	1	50	from	compound	141:148	arg1	mammals					179:185	mammals	179:185	mammals	179:185	Cobalamin (Cbl, vitamin B(12)) is a bacterial organic compound and an essential coenzyme in mammals, which take it up from the diet.
20237569	7	51	theme	-binding	1081:1088	arg1	domains					1094:1100	Ca(2+)-binding CUB domains	1075:1100	Ca(2+)-binding CUB domains	1075:1100	Finally, the comparison of Ca(2+)-binding CUB domains and the low-density lipoprotein (LDL) receptor-type A modules suggests that the electrostatic pairing of a basic ligand arginine/lysine residue with Ca(2+)-coordinating acidic aspartates/glutamates is a common theme of Ca(2+)-dependent ligand-receptor interactions.
20237569	7	52	theme	acidic	1271:1276	arg1	aspartates/glutamates					1278:1298	Ca(2+)-coordinating acidic aspartates/glutamates	1251:1298	Ca(2+)-coordinating acidic aspartates/glutamates	1251:1298	Finally, the comparison of Ca(2+)-binding CUB domains and the low-density lipoprotein (LDL) receptor-type A modules suggests that the electrostatic pairing of a basic ligand arginine/lysine residue with Ca(2+)-coordinating acidic aspartates/glutamates is a common theme of Ca(2+)-dependent ligand-receptor interactions.
20237569	1	53	from	coenzyme	167:174	arg1	mammals					179:185	mammals	179:185	mammals	179:185	Cobalamin (Cbl, vitamin B(12)) is a bacterial organic compound and an essential coenzyme in mammals, which take it up from the diet.
20237569	7	54	theme	A	1154:1154	arg1	modules					1156:1162	the low-density lipoprotein (LDL) receptor-type A modules	1106:1162	the low-density lipoprotein (LDL) receptor-type A modules	1106:1162	Finally, the comparison of Ca(2+)-binding CUB domains and the low-density lipoprotein (LDL) receptor-type A modules suggests that the electrostatic pairing of a basic ligand arginine/lysine residue with Ca(2+)-coordinating acidic aspartates/glutamates is a common theme of Ca(2+)-dependent ligand-receptor interactions.
20237569	6	55	theme	ligand-receptor	1022:1036	arg1	coupling					1038:1045	ligand-receptor coupling	1022:1045	ligand-receptor coupling	1022:1045	This dual-point model provides a probable explanation of how Cbl indirectly induces ligand-receptor coupling.
20237569	4	56	theme	complex	561:567	arg1	structure					544:552	the crystal structure	532:552	the crystal structure of the complex between IF-Cbl and the cubilin IF-Cbl-binding-region (CUB(5-8)) determined at 3.3 A resolution	532:662	Here we present the crystal structure of the complex between IF-Cbl and the cubilin IF-Cbl-binding-region (CUB(5-8)) determined at 3.3 A resolution.
20237569	1	57	theme	vitamin	103:109	arg1	12					113:114	12	113:114	12	113:114	Cobalamin (Cbl, vitamin B(12)) is a bacterial organic compound and an essential coenzyme in mammals, which take it up from the diet.
20237569	1	57	theme	vitamin	103:109	arg1	Cbl					98:100	Cbl	98:100	Cbl	98:100	Cobalamin (Cbl, vitamin B(12)) is a bacterial organic compound and an essential coenzyme in mammals, which take it up from the diet.
20237569	1	57	theme	vitamin	103:109	arg1	B					111:111	vitamin B	103:111	vitamin B(12)	103:115	Cobalamin (Cbl, vitamin B(12)) is a bacterial organic compound and an essential coenzyme in mammals, which take it up from the diet.
20237569	5	58	theme	modular	789:795	arg1	domains					756:762	several CUB (for 'complement C1r/C1s, Uegf, Bmp1') domains	705:762	several CUB (for 'complement C1r/C1s, Uegf, Bmp1') domains	705:762	The structure provides insight into how several CUB (for 'complement C1r/C1s, Uegf, Bmp1') domains collectively function as modular ligand-binding regions, and how two distant CUB domains embrace the Cbl molecule by binding the two IF domains in a Ca(2+)-dependent manner.
20237569	5	58	theme	modular	789:795	arg1	regions					812:818	modular ligand-binding regions	789:818	modular ligand-binding regions	789:818	The structure provides insight into how several CUB (for 'complement C1r/C1s, Uegf, Bmp1') domains collectively function as modular ligand-binding regions, and how two distant CUB domains embrace the Cbl molecule by binding the two IF domains in a Ca(2+)-dependent manner.
20237569	5	58	theme	modular	789:795	arg1	molecule					869:876	the Cbl molecule	861:876	the Cbl molecule	861:876	The structure provides insight into how several CUB (for 'complement C1r/C1s, Uegf, Bmp1') domains collectively function as modular ligand-binding regions, and how two distant CUB domains embrace the Cbl molecule by binding the two IF domains in a Ca(2+)-dependent manner.
20237569	7	59	theme	arginine/lysine	1222:1236	arg1	residue					1238:1244	a basic ligand arginine/lysine residue	1207:1244	a basic ligand arginine/lysine residue	1207:1244	Finally, the comparison of Ca(2+)-binding CUB domains and the low-density lipoprotein (LDL) receptor-type A modules suggests that the electrostatic pairing of a basic ligand arginine/lysine residue with Ca(2+)-coordinating acidic aspartates/glutamates is a common theme of Ca(2+)-dependent ligand-receptor interactions.
20237569	4	60	theme	A	651:651	arg1	resolution					653:662	3.3 A resolution	647:662	3.3 A resolution	647:662	Here we present the crystal structure of the complex between IF-Cbl and the cubilin IF-Cbl-binding-region (CUB(5-8)) determined at 3.3 A resolution.
20237569	2	61	theme	combined	239:246	arg1	action					248:253	the combined action	235:253	the combined action of the gastric intrinsic factor (IF) and the ileal endocytic cubam receptor formed by the 460-kilodalton (kDa) protein cubilin and the 45-kDa transmembrane protein amnionless	235:428	This occurs by the combined action of the gastric intrinsic factor (IF) and the ileal endocytic cubam receptor formed by the 460-kilodalton (kDa) protein cubilin and the 45-kDa transmembrane protein amnionless.
20237569	7	62	theme	low-density	1110:1120	arg1	lipoprotein					1122:1132	the low-density lipoprotein	1106:1132	the low-density lipoprotein (LDL)	1106:1138	Finally, the comparison of Ca(2+)-binding CUB domains and the low-density lipoprotein (LDL) receptor-type A modules suggests that the electrostatic pairing of a basic ligand arginine/lysine residue with Ca(2+)-coordinating acidic aspartates/glutamates is a common theme of Ca(2+)-dependent ligand-receptor interactions.
20237569	7	62	theme	low-density	1110:1120	arg1	LDL					1135:1137	LDL	1135:1137	LDL	1135:1137	Finally, the comparison of Ca(2+)-binding CUB domains and the low-density lipoprotein (LDL) receptor-type A modules suggests that the electrostatic pairing of a basic ligand arginine/lysine residue with Ca(2+)-coordinating acidic aspartates/glutamates is a common theme of Ca(2+)-dependent ligand-receptor interactions.
20237569	2	63	theme	45-kDa	390:395	arg1	protein					411:417	the 45-kDa transmembrane protein	386:417	the 45-kDa transmembrane protein	386:417	This occurs by the combined action of the gastric intrinsic factor (IF) and the ileal endocytic cubam receptor formed by the 460-kilodalton (kDa) protein cubilin and the 45-kDa transmembrane protein amnionless.
20237569	2	64	theme	ileal	300:304	arg1	receptor					322:329	the ileal endocytic cubam receptor	296:329	the ileal endocytic cubam receptor formed by the 460-kilodalton (kDa) protein cubilin and the 45-kDa transmembrane protein amnionless	296:428	This occurs by the combined action of the gastric intrinsic factor (IF) and the ileal endocytic cubam receptor formed by the 460-kilodalton (kDa) protein cubilin and the 45-kDa transmembrane protein amnionless.
20237569	5	65	theme	CUB	841:843	arg1	domains					845:851	two distant CUB domains	829:851	two distant CUB domains	829:851	The structure provides insight into how several CUB (for 'complement C1r/C1s, Uegf, Bmp1') domains collectively function as modular ligand-binding regions, and how two distant CUB domains embrace the Cbl molecule by binding the two IF domains in a Ca(2+)-dependent manner.
20237569	1	66	dep	Cobalamin	87:95	arg1	Cbl					98:100	Cbl	98:100	Cbl	98:100	Cobalamin (Cbl, vitamin B(12)) is a bacterial organic compound and an essential coenzyme in mammals, which take it up from the diet.
20237569	1	66	dep	Cobalamin	87:95	arg1	B					111:111	vitamin B	103:111	vitamin B(12)	103:115	Cobalamin (Cbl, vitamin B(12)) is a bacterial organic compound and an essential coenzyme in mammals, which take it up from the diet.
20237569	1	67	dep	diet	214:217	arg1	up					202:203	up	202:203	up	202:203	Cobalamin (Cbl, vitamin B(12)) is a bacterial organic compound and an essential coenzyme in mammals, which take it up from the diet.
20237569	7	68	theme	receptor-type	1140:1152	arg1	modules					1156:1162	the low-density lipoprotein (LDL) receptor-type A modules	1106:1162	the low-density lipoprotein (LDL) receptor-type A modules	1106:1162	Finally, the comparison of Ca(2+)-binding CUB domains and the low-density lipoprotein (LDL) receptor-type A modules suggests that the electrostatic pairing of a basic ligand arginine/lysine residue with Ca(2+)-coordinating acidic aspartates/glutamates is a common theme of Ca(2+)-dependent ligand-receptor interactions.
20237569	2	69	theme	factor	280:285	arg1	action					248:253	the combined action	235:253	the combined action of the gastric intrinsic factor (IF) and the ileal endocytic cubam receptor formed by the 460-kilodalton (kDa) protein cubilin and the 45-kDa transmembrane protein amnionless	235:428	This occurs by the combined action of the gastric intrinsic factor (IF) and the ileal endocytic cubam receptor formed by the 460-kilodalton (kDa) protein cubilin and the 45-kDa transmembrane protein amnionless.
20237569	7	70	with	pairing	1196:1202	arg1	aspartates/glutamates					1278:1298	Ca(2+)-coordinating acidic aspartates/glutamates	1251:1298	Ca(2+)-coordinating acidic aspartates/glutamates	1251:1298	Finally, the comparison of Ca(2+)-binding CUB domains and the low-density lipoprotein (LDL) receptor-type A modules suggests that the electrostatic pairing of a basic ligand arginine/lysine residue with Ca(2+)-coordinating acidic aspartates/glutamates is a common theme of Ca(2+)-dependent ligand-receptor interactions.
31932717	2	0	theme	molecular	526:534	arg1	dynamics					536:543	molecular dynamics	526:543	molecular dynamics	526:543	We explored the molecular mechanism for GalNAc-T3 glycosylation of FGF23 using engineered cell models and biophysical studies including kinetics, molecular dynamics and X-ray crystallography of GalNAc-T3 complexed to glycopeptide substrates.
31932717	1	1	theme	familial	351:358	arg1	calcinosis					368:377	familial tumoral calcinosis	351:377	familial tumoral calcinosis	351:377	Polypeptide GalNAc-transferase T3 (GalNAc-T3) regulates fibroblast growth factor 23 (FGF23) by O-glycosylating Thr178 in a furin proprotein processing motif RHT178R↓S. FGF23 regulates phosphate homeostasis and deficiency in GALNT3 or FGF23 results in hyperphosphatemia and familial tumoral calcinosis.
31932717	7	2	theme	isoenzyme-specific	1215:1232	arg1	functions					1247:1255	isoenzyme-specific nonredundant functions	1215:1255	isoenzyme-specific nonredundant functions	1215:1255	Our findings provide an insight into how GalNAc-T isoenzymes achieve isoenzyme-specific nonredundant functions.
31932717	4	3	theme	substrate	764:772	arg1	site					774:777	a poor substrate site	757:777	a poor substrate site with limiting glycosylation due to substrate clashes leading to destabilization of the catalytic domain flexible loop	757:895	Notably, Thr178 is a poor substrate site with limiting glycosylation due to substrate clashes leading to destabilization of the catalytic domain flexible loop.
31932717	4	3	theme	substrate	764:772	arg1	Thr178					747:752	Thr178	747:752	Thr178	747:752	Notably, Thr178 is a poor substrate site with limiting glycosylation due to substrate clashes leading to destabilization of the catalytic domain flexible loop.
31932717	1	4	theme	tumoral	360:366	arg1	calcinosis					368:377	familial tumoral calcinosis	351:377	familial tumoral calcinosis	351:377	Polypeptide GalNAc-transferase T3 (GalNAc-T3) regulates fibroblast growth factor 23 (FGF23) by O-glycosylating Thr178 in a furin proprotein processing motif RHT178R↓S. FGF23 regulates phosphate homeostasis and deficiency in GALNT3 or FGF23 results in hyperphosphatemia and familial tumoral calcinosis.
31932717	5	5	dep	suggest	901:907	arg1	achieved					1006:1013	achieved	1006:1013	suggest GalNAc-T3 specificity for FGF23 and its ability to control circulating levels of intact FGF23 is achieved by FGF23 being a poor substrate	901:1045	We suggest GalNAc-T3 specificity for FGF23 and its ability to control circulating levels of intact FGF23 is achieved by FGF23 being a poor substrate.
31932717	4	6	theme	poor	759:762	arg1	site					774:777	a poor substrate site	757:777	a poor substrate site with limiting glycosylation due to substrate clashes leading to destabilization of the catalytic domain flexible loop	757:895	Notably, Thr178 is a poor substrate site with limiting glycosylation due to substrate clashes leading to destabilization of the catalytic domain flexible loop.
31932717	4	6	theme	poor	759:762	arg1	Thr178					747:752	Thr178	747:752	Thr178	747:752	Notably, Thr178 is a poor substrate site with limiting glycosylation due to substrate clashes leading to destabilization of the catalytic domain flexible loop.
31932717	1	7	theme	phosphate	262:270	arg1	homeostasis					272:282	phosphate homeostasis	262:282	phosphate homeostasis	262:282	Polypeptide GalNAc-transferase T3 (GalNAc-T3) regulates fibroblast growth factor 23 (FGF23) by O-glycosylating Thr178 in a furin proprotein processing motif RHT178R↓S. FGF23 regulates phosphate homeostasis and deficiency in GALNT3 or FGF23 results in hyperphosphatemia and familial tumoral calcinosis.
31932717	2	8	theme	GalNAc-T3	574:582	arg1	dynamics					536:543	molecular dynamics	526:543	molecular dynamics	526:543	We explored the molecular mechanism for GalNAc-T3 glycosylation of FGF23 using engineered cell models and biophysical studies including kinetics, molecular dynamics and X-ray crystallography of GalNAc-T3 complexed to glycopeptide substrates.
31932717	2	8	theme	GalNAc-T3	574:582	arg1	crystallography					555:569	X-ray crystallography	549:569	X-ray crystallography	549:569	We explored the molecular mechanism for GalNAc-T3 glycosylation of FGF23 using engineered cell models and biophysical studies including kinetics, molecular dynamics and X-ray crystallography of GalNAc-T3 complexed to glycopeptide substrates.
31932717	2	8	theme	GalNAc-T3	574:582	arg1	kinetics					516:523	kinetics	516:523	kinetics	516:523	We explored the molecular mechanism for GalNAc-T3 glycosylation of FGF23 using engineered cell models and biophysical studies including kinetics, molecular dynamics and X-ray crystallography of GalNAc-T3 complexed to glycopeptide substrates.
31932717	6	9	theme	molecular	1090:1098	arg1	bases					1100:1104	the molecular bases	1086:1104	the molecular bases for reported disease-causing mutations	1086:1143	GalNAc-T3's structure further reveals the molecular bases for reported disease-causing mutations.
31932717	2	10	gly	glycosylation	430:442	arg1	FGF23					447:451	FGF23	447:451	FGF23	447:451	We explored the molecular mechanism for GalNAc-T3 glycosylation of FGF23 using engineered cell models and biophysical studies including kinetics, molecular dynamics and X-ray crystallography of GalNAc-T3 complexed to glycopeptide substrates.
31932717	5	11	theme	poor	1032:1035	arg1	substrate					1037:1045	a poor substrate	1030:1045	a poor substrate	1030:1045	We suggest GalNAc-T3 specificity for FGF23 and its ability to control circulating levels of intact FGF23 is achieved by FGF23 being a poor substrate.
31932717	5	11	theme	poor	1032:1035	arg1	FGF23					1018:1022	FGF23	1018:1022	FGF23	1018:1022	We suggest GalNAc-T3 specificity for FGF23 and its ability to control circulating levels of intact FGF23 is achieved by FGF23 being a poor substrate.
31932717	3	12	gly	glycosylation	713:725	arg1	Thr171					730:735	Thr171	730:735	Thr171	730:735	GalNAc-T3 uses a lectin domain mediated mechanism to glycosylate Thr178 requiring previous glycosylation at Thr171.
31932717	1	13	gly	O-glycosylating	173:187	arg0	Thr178					189:194	O-glycosylating Thr178	173:194	O-glycosylating Thr178 in a furin proprotein processing motif	173:233	Polypeptide GalNAc-transferase T3 (GalNAc-T3) regulates fibroblast growth factor 23 (FGF23) by O-glycosylating Thr178 in a furin proprotein processing motif RHT178R↓S. FGF23 regulates phosphate homeostasis and deficiency in GALNT3 or FGF23 results in hyperphosphatemia and familial tumoral calcinosis.
31932717	3	14	gly	glycosylate	675:685	arg1	Thr178					687:692	Thr178	687:692	Thr178 requiring previous glycosylation at Thr171	687:735	GalNAc-T3 uses a lectin domain mediated mechanism to glycosylate Thr178 requiring previous glycosylation at Thr171.
31932717	2	15	theme	GalNAc-T3	420:428	arg1	glycosylation					430:442	GalNAc-T3 glycosylation	420:442	GalNAc-T3 glycosylation of FGF23	420:451	We explored the molecular mechanism for GalNAc-T3 glycosylation of FGF23 using engineered cell models and biophysical studies including kinetics, molecular dynamics and X-ray crystallography of GalNAc-T3 complexed to glycopeptide substrates.
31932717	2	16	theme	X-ray	549:553	arg1	crystallography					555:569	X-ray crystallography	549:569	X-ray crystallography	549:569	We explored the molecular mechanism for GalNAc-T3 glycosylation of FGF23 using engineered cell models and biophysical studies including kinetics, molecular dynamics and X-ray crystallography of GalNAc-T3 complexed to glycopeptide substrates.
31932717	7	17	theme	GalNAc-T	1187:1194	arg1	isoenzymes					1196:1205	GalNAc-T isoenzymes	1187:1205	GalNAc-T isoenzymes	1187:1205	Our findings provide an insight into how GalNAc-T isoenzymes achieve isoenzyme-specific nonredundant functions.
31932717	1	18	theme	Polypeptide	78:88	arg1	GalNAc-transferase					90:107	Polypeptide GalNAc-transferase	78:107	Polypeptide GalNAc-transferase T3 (GalNAc-T3)	78:122	Polypeptide GalNAc-transferase T3 (GalNAc-T3) regulates fibroblast growth factor 23 (FGF23) by O-glycosylating Thr178 in a furin proprotein processing motif RHT178R↓S. FGF23 regulates phosphate homeostasis and deficiency in GALNT3 or FGF23 results in hyperphosphatemia and familial tumoral calcinosis.
31932717	1	19	from	deficiency	288:297	arg1	GALNT3					302:307	GALNT3	302:307	GALNT3	302:307	Polypeptide GalNAc-transferase T3 (GalNAc-T3) regulates fibroblast growth factor 23 (FGF23) by O-glycosylating Thr178 in a furin proprotein processing motif RHT178R↓S. FGF23 regulates phosphate homeostasis and deficiency in GALNT3 or FGF23 results in hyperphosphatemia and familial tumoral calcinosis.
31932717	1	19	from	deficiency	288:297	arg1	results					318:324	FGF23 results	312:324	FGF23 results	312:324	Polypeptide GalNAc-transferase T3 (GalNAc-T3) regulates fibroblast growth factor 23 (FGF23) by O-glycosylating Thr178 in a furin proprotein processing motif RHT178R↓S. FGF23 regulates phosphate homeostasis and deficiency in GALNT3 or FGF23 results in hyperphosphatemia and familial tumoral calcinosis.
31932717	1	20	theme	GalNAc-transferase	90:107	arg1	T3					109:110	Polypeptide GalNAc-transferase T3	78:110	Polypeptide GalNAc-transferase T3 (GalNAc-T3)	78:122	Polypeptide GalNAc-transferase T3 (GalNAc-T3) regulates fibroblast growth factor 23 (FGF23) by O-glycosylating Thr178 in a furin proprotein processing motif RHT178R↓S. FGF23 regulates phosphate homeostasis and deficiency in GALNT3 or FGF23 results in hyperphosphatemia and familial tumoral calcinosis.
31932717	1	20	theme	GalNAc-transferase	90:107	arg1	GalNAc-T3					113:121	GalNAc-T3	113:121	GalNAc-T3	113:121	Polypeptide GalNAc-transferase T3 (GalNAc-T3) regulates fibroblast growth factor 23 (FGF23) by O-glycosylating Thr178 in a furin proprotein processing motif RHT178R↓S. FGF23 regulates phosphate homeostasis and deficiency in GALNT3 or FGF23 results in hyperphosphatemia and familial tumoral calcinosis.
31932717	1	21	theme	O-glycosylating	173:187	arg1	Thr178					189:194	O-glycosylating Thr178	173:194	O-glycosylating Thr178 in a furin proprotein processing motif	173:233	Polypeptide GalNAc-transferase T3 (GalNAc-T3) regulates fibroblast growth factor 23 (FGF23) by O-glycosylating Thr178 in a furin proprotein processing motif RHT178R↓S. FGF23 regulates phosphate homeostasis and deficiency in GALNT3 or FGF23 results in hyperphosphatemia and familial tumoral calcinosis.
31932717	0	22	theme	Molecular	0:8	arg1	basis					10:14	Molecular basis	0:14	Molecular basis for fibroblast growth factor 23 O-glycosylation by GalNAc-T3.	0:76	Molecular basis for fibroblast growth factor 23 O-glycosylation by GalNAc-T3.
31932717	2	23	theme	molecular	396:404	arg1	mechanism					406:414	the molecular mechanism	392:414	the molecular mechanism for GalNAc-T3 glycosylation of FGF23	392:451	We explored the molecular mechanism for GalNAc-T3 glycosylation of FGF23 using engineered cell models and biophysical studies including kinetics, molecular dynamics and X-ray crystallography of GalNAc-T3 complexed to glycopeptide substrates.
31932717	0	24	theme	fibroblast	20:29	arg1	factor					38:43	fibroblast growth factor 23	20:46	fibroblast growth factor 23 O-glycosylation	20:62	Molecular basis for fibroblast growth factor 23 O-glycosylation by GalNAc-T3.
31932717	1	25	from	homeostasis	272:282	arg1	GALNT3					302:307	GALNT3	302:307	GALNT3	302:307	Polypeptide GalNAc-transferase T3 (GalNAc-T3) regulates fibroblast growth factor 23 (FGF23) by O-glycosylating Thr178 in a furin proprotein processing motif RHT178R↓S. FGF23 regulates phosphate homeostasis and deficiency in GALNT3 or FGF23 results in hyperphosphatemia and familial tumoral calcinosis.
31932717	1	25	from	homeostasis	272:282	arg1	results					318:324	FGF23 results	312:324	FGF23 results	312:324	Polypeptide GalNAc-transferase T3 (GalNAc-T3) regulates fibroblast growth factor 23 (FGF23) by O-glycosylating Thr178 in a furin proprotein processing motif RHT178R↓S. FGF23 regulates phosphate homeostasis and deficiency in GALNT3 or FGF23 results in hyperphosphatemia and familial tumoral calcinosis.
31932717	5	26	theme	GalNAc-T3	909:917	arg1	specificity					919:929	GalNAc-T3 specificity	909:929	GalNAc-T3 specificity for FGF23	909:939	We suggest GalNAc-T3 specificity for FGF23 and its ability to control circulating levels of intact FGF23 is achieved by FGF23 being a poor substrate.
31932717	2	27	theme	engineered	459:468	arg1	models					475:480	engineered cell models	459:480	engineered cell models	459:480	We explored the molecular mechanism for GalNAc-T3 glycosylation of FGF23 using engineered cell models and biophysical studies including kinetics, molecular dynamics and X-ray crystallography of GalNAc-T3 complexed to glycopeptide substrates.
31932717	2	28	theme	glycopeptide	597:608	arg1	substrates					610:619	glycopeptide substrates	597:619	glycopeptide substrates	597:619	We explored the molecular mechanism for GalNAc-T3 glycosylation of FGF23 using engineered cell models and biophysical studies including kinetics, molecular dynamics and X-ray crystallography of GalNAc-T3 complexed to glycopeptide substrates.
31932717	4	29	theme	substrate	814:822	arg1	clashes					824:830	substrate clashes	814:830	substrate clashes leading to destabilization of the catalytic domain flexible loop	814:895	Notably, Thr178 is a poor substrate site with limiting glycosylation due to substrate clashes leading to destabilization of the catalytic domain flexible loop.
31932717	2	30	theme	FGF23	447:451	arg1	glycosylation					430:442	GalNAc-T3 glycosylation	420:442	GalNAc-T3 glycosylation of FGF23	420:451	We explored the molecular mechanism for GalNAc-T3 glycosylation of FGF23 using engineered cell models and biophysical studies including kinetics, molecular dynamics and X-ray crystallography of GalNAc-T3 complexed to glycopeptide substrates.
31932717	0	31	theme	factor	38:43	arg1	O-glycosylation					48:62	fibroblast growth factor 23 O-glycosylation	20:62	fibroblast growth factor 23 O-glycosylation	20:62	Molecular basis for fibroblast growth factor 23 O-glycosylation by GalNAc-T3.
31932717	6	32	theme	disease-causing	1119:1133	arg1	mutations					1135:1143	reported disease-causing mutations	1110:1143	reported disease-causing mutations	1110:1143	GalNAc-T3's structure further reveals the molecular bases for reported disease-causing mutations.
31932717	3	33	theme	mediated	653:660	arg1	mechanism					662:670	a lectin domain mediated mechanism	637:670	a lectin domain mediated mechanism to glycosylate Thr178 requiring previous glycosylation at Thr171	637:735	GalNAc-T3 uses a lectin domain mediated mechanism to glycosylate Thr178 requiring previous glycosylation at Thr171.
31932717	1	34	theme	furin	201:205	arg1	motif					229:233	a furin proprotein processing motif	199:233	a furin proprotein processing motif	199:233	Polypeptide GalNAc-transferase T3 (GalNAc-T3) regulates fibroblast growth factor 23 (FGF23) by O-glycosylating Thr178 in a furin proprotein processing motif RHT178R↓S. FGF23 regulates phosphate homeostasis and deficiency in GALNT3 or FGF23 results in hyperphosphatemia and familial tumoral calcinosis.
31932717	0	35	theme	growth	31:36	arg1	factor					38:43	fibroblast growth factor 23	20:46	fibroblast growth factor 23 O-glycosylation	20:62	Molecular basis for fibroblast growth factor 23 O-glycosylation by GalNAc-T3.
31932717	1	36	theme	FGF23	312:316	arg1	results					318:324	FGF23 results	312:324	FGF23 results	312:324	Polypeptide GalNAc-transferase T3 (GalNAc-T3) regulates fibroblast growth factor 23 (FGF23) by O-glycosylating Thr178 in a furin proprotein processing motif RHT178R↓S. FGF23 regulates phosphate homeostasis and deficiency in GALNT3 or FGF23 results in hyperphosphatemia and familial tumoral calcinosis.
31932717	3	37	theme	previous	704:711	arg1	glycosylation					713:725	previous glycosylation	704:725	previous glycosylation	704:725	GalNAc-T3 uses a lectin domain mediated mechanism to glycosylate Thr178 requiring previous glycosylation at Thr171.
31932717	2	38	theme	cell	470:473	arg1	models					475:480	engineered cell models	459:480	engineered cell models	459:480	We explored the molecular mechanism for GalNAc-T3 glycosylation of FGF23 using engineered cell models and biophysical studies including kinetics, molecular dynamics and X-ray crystallography of GalNAc-T3 complexed to glycopeptide substrates.
31932717	1	39	theme	proprotein	207:216	arg1	motif					229:233	a furin proprotein processing motif	199:233	a furin proprotein processing motif	199:233	Polypeptide GalNAc-transferase T3 (GalNAc-T3) regulates fibroblast growth factor 23 (FGF23) by O-glycosylating Thr178 in a furin proprotein processing motif RHT178R↓S. FGF23 regulates phosphate homeostasis and deficiency in GALNT3 or FGF23 results in hyperphosphatemia and familial tumoral calcinosis.
31932717	7	40	theme	nonredundant	1234:1245	arg1	functions					1247:1255	isoenzyme-specific nonredundant functions	1215:1255	isoenzyme-specific nonredundant functions	1215:1255	Our findings provide an insight into how GalNAc-T isoenzymes achieve isoenzyme-specific nonredundant functions.
31932717	3	41	theme	lectin	639:644	arg1	domain					646:651	lectin domain	639:651	lectin domain	639:651	GalNAc-T3 uses a lectin domain mediated mechanism to glycosylate Thr178 requiring previous glycosylation at Thr171.
31932717	5	42	theme	intact	990:995	arg1	FGF23					997:1001	intact FGF23	990:1001	intact FGF23	990:1001	We suggest GalNAc-T3 specificity for FGF23 and its ability to control circulating levels of intact FGF23 is achieved by FGF23 being a poor substrate.
31932717	2	43	theme	biophysical	486:496	arg1	studies					498:504	biophysical studies	486:504	biophysical studies including kinetics, molecular dynamics and X-ray crystallography of GalNAc-T3 complexed to glycopeptide substrates	486:619	We explored the molecular mechanism for GalNAc-T3 glycosylation of FGF23 using engineered cell models and biophysical studies including kinetics, molecular dynamics and X-ray crystallography of GalNAc-T3 complexed to glycopeptide substrates.
31932717	5	44	theme	FGF23	997:1001	arg1	levels					980:985	circulating levels	968:985	circulating levels of intact FGF23	968:1001	We suggest GalNAc-T3 specificity for FGF23 and its ability to control circulating levels of intact FGF23 is achieved by FGF23 being a poor substrate.
31932717	4	45	theme	catalytic	866:874	arg1	loop					892:895	the catalytic domain flexible loop	862:895	the catalytic domain flexible loop	862:895	Notably, Thr178 is a poor substrate site with limiting glycosylation due to substrate clashes leading to destabilization of the catalytic domain flexible loop.
31932717	4	46	theme	loop	892:895	arg1	destabilization					843:857	destabilization	843:857	destabilization of the catalytic domain flexible loop	843:895	Notably, Thr178 is a poor substrate site with limiting glycosylation due to substrate clashes leading to destabilization of the catalytic domain flexible loop.
31932717	1	47	theme	fibroblast	134:143	arg1	factor					152:157	fibroblast growth factor 23	134:160	fibroblast growth factor 23 (FGF23)	134:168	Polypeptide GalNAc-transferase T3 (GalNAc-T3) regulates fibroblast growth factor 23 (FGF23) by O-glycosylating Thr178 in a furin proprotein processing motif RHT178R↓S. FGF23 regulates phosphate homeostasis and deficiency in GALNT3 or FGF23 results in hyperphosphatemia and familial tumoral calcinosis.
31932717	1	47	theme	fibroblast	134:143	arg1	FGF23					163:167	FGF23	163:167	FGF23	163:167	Polypeptide GalNAc-transferase T3 (GalNAc-T3) regulates fibroblast growth factor 23 (FGF23) by O-glycosylating Thr178 in a furin proprotein processing motif RHT178R↓S. FGF23 regulates phosphate homeostasis and deficiency in GALNT3 or FGF23 results in hyperphosphatemia and familial tumoral calcinosis.
31932717	1	48	theme	processing	218:227	arg1	motif					229:233	a furin proprotein processing motif	199:233	a furin proprotein processing motif	199:233	Polypeptide GalNAc-transferase T3 (GalNAc-T3) regulates fibroblast growth factor 23 (FGF23) by O-glycosylating Thr178 in a furin proprotein processing motif RHT178R↓S. FGF23 regulates phosphate homeostasis and deficiency in GALNT3 or FGF23 results in hyperphosphatemia and familial tumoral calcinosis.
31932717	1	49	theme	growth	145:150	arg1	factor					152:157	fibroblast growth factor 23	134:160	fibroblast growth factor 23 (FGF23)	134:168	Polypeptide GalNAc-transferase T3 (GalNAc-T3) regulates fibroblast growth factor 23 (FGF23) by O-glycosylating Thr178 in a furin proprotein processing motif RHT178R↓S. FGF23 regulates phosphate homeostasis and deficiency in GALNT3 or FGF23 results in hyperphosphatemia and familial tumoral calcinosis.
31932717	1	49	theme	growth	145:150	arg1	FGF23					163:167	FGF23	163:167	FGF23	163:167	Polypeptide GalNAc-transferase T3 (GalNAc-T3) regulates fibroblast growth factor 23 (FGF23) by O-glycosylating Thr178 in a furin proprotein processing motif RHT178R↓S. FGF23 regulates phosphate homeostasis and deficiency in GALNT3 or FGF23 results in hyperphosphatemia and familial tumoral calcinosis.
31932717	6	50	theme	reported	1110:1117	arg1	mutations					1135:1143	reported disease-causing mutations	1110:1143	reported disease-causing mutations	1110:1143	GalNAc-T3's structure further reveals the molecular bases for reported disease-causing mutations.
31932717	4	51	theme	flexible	883:890	arg1	loop					892:895	the catalytic domain flexible loop	862:895	the catalytic domain flexible loop	862:895	Notably, Thr178 is a poor substrate site with limiting glycosylation due to substrate clashes leading to destabilization of the catalytic domain flexible loop.
31932717	1	52	from	Thr178	189:194	arg1	motif					229:233	a furin proprotein processing motif	199:233	a furin proprotein processing motif	199:233	Polypeptide GalNAc-transferase T3 (GalNAc-T3) regulates fibroblast growth factor 23 (FGF23) by O-glycosylating Thr178 in a furin proprotein processing motif RHT178R↓S. FGF23 regulates phosphate homeostasis and deficiency in GALNT3 or FGF23 results in hyperphosphatemia and familial tumoral calcinosis.
31932717	2	53	gly	glycopeptide	597:608	arg2	glycopeptide					597:608	glycopeptide	597:608	glycopeptide	597:608	We explored the molecular mechanism for GalNAc-T3 glycosylation of FGF23 using engineered cell models and biophysical studies including kinetics, molecular dynamics and X-ray crystallography of GalNAc-T3 complexed to glycopeptide substrates.
31932717	1	54	theme	RHT178R↓S.	235:244	arg1	FGF23					246:250	RHT178R↓S. FGF23	235:250	RHT178R↓S. FGF23	235:250	Polypeptide GalNAc-transferase T3 (GalNAc-T3) regulates fibroblast growth factor 23 (FGF23) by O-glycosylating Thr178 in a furin proprotein processing motif RHT178R↓S. FGF23 regulates phosphate homeostasis and deficiency in GALNT3 or FGF23 results in hyperphosphatemia and familial tumoral calcinosis.
31932717	4	55	theme	domain	876:881	arg1	loop					892:895	the catalytic domain flexible loop	862:895	the catalytic domain flexible loop	862:895	Notably, Thr178 is a poor substrate site with limiting glycosylation due to substrate clashes leading to destabilization of the catalytic domain flexible loop.
31932717	5	56	theme	circulating	968:978	arg1	levels					980:985	circulating levels	968:985	circulating levels of intact FGF23	968:1001	We suggest GalNAc-T3 specificity for FGF23 and its ability to control circulating levels of intact FGF23 is achieved by FGF23 being a poor substrate.
3134887	3	0	theme	primary	332:338	arg1	sequence					340:347	The primary sequence	328:347	The primary sequence of this 224 amino acid recombinant protein which lacks most of the carboxy-terminal transmembrane and cytoplasmic portions of the intact protein	328:492	The primary sequence of this 224 amino acid recombinant protein which lacks most of the carboxy-terminal transmembrane and cytoplasmic portions of the intact protein was established by sequence analyses.
3134887	5	1	theme	interleukin-2	671:683	arg1	receptor					685:692	natural interleukin-2 receptor	663:692	natural interleukin-2 receptor	663:692	As in the case of natural interleukin-2 receptor they occur between cysteines 3-147, 46-104, 131-163, and 28/30-59/61.
3134887	5	2	theme	receptor	685:692	arg1	case					655:658	the case	651:658	the case of natural interleukin-2 receptor	651:692	As in the case of natural interleukin-2 receptor they occur between cysteines 3-147, 46-104, 131-163, and 28/30-59/61.
3134887	4	3	theme	reduced	604:610	arg1	digests					636:642	the reduced and non-reduced peptide digests	600:642	the reduced and non-reduced peptide digests	600:642	The disulfide bonds were assigned by comparative peptide mapping of the reduced and non-reduced peptide digests.
3134887	3	4	theme	acid	367:370	arg1	protein					384:390	this 224 amino acid recombinant protein	352:390	this 224 amino acid recombinant protein which lacks most of the carboxy-terminal transmembrane and cytoplasmic portions of the intact protein	352:492	The primary sequence of this 224 amino acid recombinant protein which lacks most of the carboxy-terminal transmembrane and cytoplasmic portions of the intact protein was established by sequence analyses.
3134887	4	5	theme	disulfide	536:544	arg1	bonds					546:550	The disulfide bonds	532:550	The disulfide bonds	532:550	The disulfide bonds were assigned by comparative peptide mapping of the reduced and non-reduced peptide digests.
3134887	2	6	dep	form	189:192	arg1	engineered					239:248	engineered	239:248	engineered	239:248	A purified soluble and functional form of recombinant human interleukin-2 receptor, engineered and expressed in Chinese hamster ovary cells, was structurally characterized.
3134887	2	6	dep	form	189:192	arg1	expressed					254:262	expressed	254:262	expressed in Chinese hamster ovary cells	254:293	A purified soluble and functional form of recombinant human interleukin-2 receptor, engineered and expressed in Chinese hamster ovary cells, was structurally characterized.
3134887	3	7	theme	recombinant	372:382	arg1	protein					384:390	this 224 amino acid recombinant protein	352:390	this 224 amino acid recombinant protein which lacks most of the carboxy-terminal transmembrane and cytoplasmic portions of the intact protein	352:492	The primary sequence of this 224 amino acid recombinant protein which lacks most of the carboxy-terminal transmembrane and cytoplasmic portions of the intact protein was established by sequence analyses.
3134887	2	8	theme	purified	157:164	arg1	form					189:192	A purified soluble and functional form	155:192	A purified soluble and functional form	155:192	A purified soluble and functional form of recombinant human interleukin-2 receptor, engineered and expressed in Chinese hamster ovary cells, was structurally characterized.
3134887	1	9	theme	Primary	73:79	arg1	structure					81:89	Primary structure	73:89	Primary structure	73:89	Primary structure, assignment of disulfide bonds and core IL-2 binding structure.
3134887	4	10	theme	non-reduced	616:626	arg1	digests					636:642	the reduced and non-reduced peptide digests	600:642	the reduced and non-reduced peptide digests	600:642	The disulfide bonds were assigned by comparative peptide mapping of the reduced and non-reduced peptide digests.
3134887	6	11	theme	structural	810:819	arg1	model					821:825	a structural model	808:825	a structural model of the interleukin-2 receptor for interleukin-2 binding	808:881	Based on assignment of the disulfide bonds, a structural model of the interleukin-2 receptor for interleukin-2 binding is proposed.
3134887	3	12	theme	amino	361:365	arg1	protein					384:390	this 224 amino acid recombinant protein	352:390	this 224 amino acid recombinant protein which lacks most of the carboxy-terminal transmembrane and cytoplasmic portions of the intact protein	352:492	The primary sequence of this 224 amino acid recombinant protein which lacks most of the carboxy-terminal transmembrane and cytoplasmic portions of the intact protein was established by sequence analyses.
3134887	3	13	theme	carboxy-terminal	416:431	arg1	portions					463:470	the carboxy-terminal transmembrane and cytoplasmic portions	412:470	the carboxy-terminal transmembrane and cytoplasmic portions of the intact protein	412:492	The primary sequence of this 224 amino acid recombinant protein which lacks most of the carboxy-terminal transmembrane and cytoplasmic portions of the intact protein was established by sequence analyses.
3134887	2	14	theme	ovary	283:287	arg1	cells					289:293	Chinese hamster ovary cells	267:293	Chinese hamster ovary cells	267:293	A purified soluble and functional form of recombinant human interleukin-2 receptor, engineered and expressed in Chinese hamster ovary cells, was structurally characterized.
3134887	0	15	theme	Structural	0:9	arg1	analysis					11:18	Structural analysis	0:18	Structural analysis of recombinant soluble human interleukin-2 receptor	0:70	Structural analysis of recombinant soluble human interleukin-2 receptor.
3134887	5	16	theme	natural	663:669	arg1	receptor					685:692	natural interleukin-2 receptor	663:692	natural interleukin-2 receptor	663:692	As in the case of natural interleukin-2 receptor they occur between cysteines 3-147, 46-104, 131-163, and 28/30-59/61.
3134887	6	17	theme	bonds	801:805	arg1	assignment					773:782	assignment	773:782	assignment of the disulfide bonds	773:805	Based on assignment of the disulfide bonds, a structural model of the interleukin-2 receptor for interleukin-2 binding is proposed.
3134887	6	18	theme	interleukin-2	861:873	arg1	binding					875:881	interleukin-2 binding	861:881	interleukin-2 binding	861:881	Based on assignment of the disulfide bonds, a structural model of the interleukin-2 receptor for interleukin-2 binding is proposed.
3134887	3	19	theme	cytoplasmic	451:461	arg1	portions					463:470	the carboxy-terminal transmembrane and cytoplasmic portions	412:470	the carboxy-terminal transmembrane and cytoplasmic portions of the intact protein	412:492	The primary sequence of this 224 amino acid recombinant protein which lacks most of the carboxy-terminal transmembrane and cytoplasmic portions of the intact protein was established by sequence analyses.
3134887	0	20	theme	recombinant	23:33	arg1	receptor					63:70	recombinant soluble human interleukin-2 receptor	23:70	recombinant soluble human interleukin-2 receptor	23:70	Structural analysis of recombinant soluble human interleukin-2 receptor.
3134887	4	21	theme	peptide	581:587	arg1	mapping					589:595	comparative peptide mapping	569:595	comparative peptide mapping of the reduced and non-reduced peptide digests	569:642	The disulfide bonds were assigned by comparative peptide mapping of the reduced and non-reduced peptide digests.
3134887	6	22	theme	disulfide	791:799	arg1	bonds					801:805	the disulfide bonds	787:805	the disulfide bonds	787:805	Based on assignment of the disulfide bonds, a structural model of the interleukin-2 receptor for interleukin-2 binding is proposed.
3134887	1	23	theme	disulfide	106:114	arg1	bonds					116:120	disulfide bonds	106:120	disulfide bonds	106:120	Primary structure, assignment of disulfide bonds and core IL-2 binding structure.
3134887	3	24	theme	protein	486:492	arg1	portions					463:470	the carboxy-terminal transmembrane and cytoplasmic portions	412:470	the carboxy-terminal transmembrane and cytoplasmic portions of the intact protein	412:492	The primary sequence of this 224 amino acid recombinant protein which lacks most of the carboxy-terminal transmembrane and cytoplasmic portions of the intact protein was established by sequence analyses.
3134887	1	25	theme	bonds	116:120	arg1	structure					81:89	Primary structure	73:89	Primary structure	73:89	Primary structure, assignment of disulfide bonds and core IL-2 binding structure.
3134887	1	25	theme	bonds	116:120	arg1	assignment					92:101	assignment	92:101	assignment of disulfide bonds	92:120	Primary structure, assignment of disulfide bonds and core IL-2 binding structure.
3134887	1	25	theme	bonds	116:120	arg1	structure					144:152	core IL-2 binding structure	126:152	core IL-2 binding structure	126:152	Primary structure, assignment of disulfide bonds and core IL-2 binding structure.
3134887	0	26	theme	human	43:47	arg1	receptor					63:70	recombinant soluble human interleukin-2 receptor	23:70	recombinant soluble human interleukin-2 receptor	23:70	Structural analysis of recombinant soluble human interleukin-2 receptor.
3134887	2	27	theme	functional	178:187	arg1	form					189:192	A purified soluble and functional form	155:192	A purified soluble and functional form	155:192	A purified soluble and functional form of recombinant human interleukin-2 receptor, engineered and expressed in Chinese hamster ovary cells, was structurally characterized.
3134887	0	28	theme	soluble	35:41	arg1	receptor					63:70	recombinant soluble human interleukin-2 receptor	23:70	recombinant soluble human interleukin-2 receptor	23:70	Structural analysis of recombinant soluble human interleukin-2 receptor.
3134887	3	29	theme	transmembrane	433:445	arg1	portions					463:470	the carboxy-terminal transmembrane and cytoplasmic portions	412:470	the carboxy-terminal transmembrane and cytoplasmic portions of the intact protein	412:492	The primary sequence of this 224 amino acid recombinant protein which lacks most of the carboxy-terminal transmembrane and cytoplasmic portions of the intact protein was established by sequence analyses.
3134887	3	30	theme	protein	384:390	arg1	sequence					340:347	The primary sequence	328:347	The primary sequence of this 224 amino acid recombinant protein which lacks most of the carboxy-terminal transmembrane and cytoplasmic portions of the intact protein	328:492	The primary sequence of this 224 amino acid recombinant protein which lacks most of the carboxy-terminal transmembrane and cytoplasmic portions of the intact protein was established by sequence analyses.
3134887	3	31	theme	intact	479:484	arg1	protein					486:492	the intact protein	475:492	the intact protein	475:492	The primary sequence of this 224 amino acid recombinant protein which lacks most of the carboxy-terminal transmembrane and cytoplasmic portions of the intact protein was established by sequence analyses.
3134887	0	32	theme	receptor	63:70	arg1	analysis					11:18	Structural analysis	0:18	Structural analysis of recombinant soluble human interleukin-2 receptor	0:70	Structural analysis of recombinant soluble human interleukin-2 receptor.
3134887	2	33	theme	soluble	166:172	arg1	form					189:192	A purified soluble and functional form	155:192	A purified soluble and functional form	155:192	A purified soluble and functional form of recombinant human interleukin-2 receptor, engineered and expressed in Chinese hamster ovary cells, was structurally characterized.
3134887	3	34	theme	sequence	513:520	arg1	analyses					522:529	sequence analyses	513:529	sequence analyses	513:529	The primary sequence of this 224 amino acid recombinant protein which lacks most of the carboxy-terminal transmembrane and cytoplasmic portions of the intact protein was established by sequence analyses.
3134887	0	35	theme	interleukin-2	49:61	arg1	receptor					63:70	recombinant soluble human interleukin-2 receptor	23:70	recombinant soluble human interleukin-2 receptor	23:70	Structural analysis of recombinant soluble human interleukin-2 receptor.
3134887	4	36	theme	comparative	569:579	arg1	mapping					589:595	comparative peptide mapping	569:595	comparative peptide mapping of the reduced and non-reduced peptide digests	569:642	The disulfide bonds were assigned by comparative peptide mapping of the reduced and non-reduced peptide digests.
3134887	2	37	theme	interleukin-2	215:227	arg1	receptor					229:236	recombinant human interleukin-2 receptor	197:236	recombinant human interleukin-2 receptor	197:236	A purified soluble and functional form of recombinant human interleukin-2 receptor, engineered and expressed in Chinese hamster ovary cells, was structurally characterized.
3134887	2	38	theme	receptor	229:236	arg1	form					189:192	A purified soluble and functional form	155:192	A purified soluble and functional form	155:192	A purified soluble and functional form of recombinant human interleukin-2 receptor, engineered and expressed in Chinese hamster ovary cells, was structurally characterized.
3134887	1	39	theme	core	126:129	arg1	structure					144:152	core IL-2 binding structure	126:152	core IL-2 binding structure	126:152	Primary structure, assignment of disulfide bonds and core IL-2 binding structure.
3134887	2	40	theme	human	209:213	arg1	receptor					229:236	recombinant human interleukin-2 receptor	197:236	recombinant human interleukin-2 receptor	197:236	A purified soluble and functional form of recombinant human interleukin-2 receptor, engineered and expressed in Chinese hamster ovary cells, was structurally characterized.
3134887	2	41	theme	hamster	275:281	arg1	cells					289:293	Chinese hamster ovary cells	267:293	Chinese hamster ovary cells	267:293	A purified soluble and functional form of recombinant human interleukin-2 receptor, engineered and expressed in Chinese hamster ovary cells, was structurally characterized.
3134887	1	42	theme	IL-2	131:134	arg1	structure					144:152	core IL-2 binding structure	126:152	core IL-2 binding structure	126:152	Primary structure, assignment of disulfide bonds and core IL-2 binding structure.
3134887	2	43	theme	recombinant	197:207	arg1	receptor					229:236	recombinant human interleukin-2 receptor	197:236	recombinant human interleukin-2 receptor	197:236	A purified soluble and functional form of recombinant human interleukin-2 receptor, engineered and expressed in Chinese hamster ovary cells, was structurally characterized.
3134887	2	44	theme	Chinese	267:273	arg1	cells					289:293	Chinese hamster ovary cells	267:293	Chinese hamster ovary cells	267:293	A purified soluble and functional form of recombinant human interleukin-2 receptor, engineered and expressed in Chinese hamster ovary cells, was structurally characterized.
3134887	1	45	theme	binding	136:142	arg1	structure					144:152	core IL-2 binding structure	126:152	core IL-2 binding structure	126:152	Primary structure, assignment of disulfide bonds and core IL-2 binding structure.
3134887	4	46	theme	digests	636:642	arg1	mapping					589:595	comparative peptide mapping	569:595	comparative peptide mapping of the reduced and non-reduced peptide digests	569:642	The disulfide bonds were assigned by comparative peptide mapping of the reduced and non-reduced peptide digests.
3134887	6	47	theme	interleukin-2	834:846	arg1	receptor					848:855	the interleukin-2 receptor	830:855	the interleukin-2 receptor	830:855	Based on assignment of the disulfide bonds, a structural model of the interleukin-2 receptor for interleukin-2 binding is proposed.
3134887	6	48	theme	receptor	848:855	arg1	model					821:825	a structural model	808:825	a structural model of the interleukin-2 receptor for interleukin-2 binding	808:881	Based on assignment of the disulfide bonds, a structural model of the interleukin-2 receptor for interleukin-2 binding is proposed.
3134887	4	49	theme	peptide	628:634	arg1	digests					636:642	the reduced and non-reduced peptide digests	600:642	the reduced and non-reduced peptide digests	600:642	The disulfide bonds were assigned by comparative peptide mapping of the reduced and non-reduced peptide digests.
20473317	3	0	theme	structural	432:441	arg1	elements					443:450	CLD1 structural elements	427:450	CLD1 structural elements	427:450	CLD1 structural elements and disulfide composition are unique to mammals, indicating an unexpected structural diversity within higher and lower vertebrate RET CLD regions.
20473317	2	1	theme	classical	406:414	arg1	cadherins					416:424	classical cadherins	406:424	classical cadherins	406:424	Here we show that two N-terminal cadherin-like domains, CLD1 and CLD2 (CLD(1-2)), from human RET adopt a clam-shell arrangement distinct from that of classical cadherins.
20473317	4	2	theme	severity	828:835	arg1	correlate					802:810	a biochemical correlate	788:810	a biochemical correlate of HSCR disease severity	788:835	We identify two unpaired cysteines that predispose human RET to maturation impediments in the endoplasmic reticulum and establish a quantitative cell-based RET maturation assay that offers a biochemical correlate of HSCR disease severity.
20473317	5	3	theme	key	861:863	arg1	framework					876:884	a key conceptual framework	859:884	a key conceptual framework	859:884	Our findings provide a key conceptual framework and means of testing and predicting genotype-phenotype correlations in HSCR.
20473317	3	4	theme	CLD	586:588	arg1	regions					590:596	higher and lower vertebrate RET CLD regions	554:596	higher and lower vertebrate RET CLD regions	554:596	CLD1 structural elements and disulfide composition are unique to mammals, indicating an unexpected structural diversity within higher and lower vertebrate RET CLD regions.
20473317	4	5	theme	cell-based	744:753	arg1	assay					770:774	a quantitative cell-based RET maturation assay	729:774	a quantitative cell-based RET maturation assay that offers a biochemical correlate of HSCR disease severity	729:835	We identify two unpaired cysteines that predispose human RET to maturation impediments in the endoplasmic reticulum and establish a quantitative cell-based RET maturation assay that offers a biochemical correlate of HSCR disease severity.
20473317	4	6	theme	biochemical	790:800	arg1	correlate					802:810	a biochemical correlate	788:810	a biochemical correlate of HSCR disease severity	788:835	We identify two unpaired cysteines that predispose human RET to maturation impediments in the endoplasmic reticulum and establish a quantitative cell-based RET maturation assay that offers a biochemical correlate of HSCR disease severity.
20473317	4	7	theme	endoplasmic	693:703	arg1	reticulum					705:713	the endoplasmic reticulum	689:713	the endoplasmic reticulum	689:713	We identify two unpaired cysteines that predispose human RET to maturation impediments in the endoplasmic reticulum and establish a quantitative cell-based RET maturation assay that offers a biochemical correlate of HSCR disease severity.
20473317	1	8	theme	complex	228:234	arg1	disease					247:253	a complex multigenic disease	226:253	a complex multigenic disease	226:253	The maturation of human RET is adversely affected by a range of missense mutations found in patients with Hirschsprung's disease (HSCR), a complex multigenic disease.
20473317	1	8	theme	complex	228:234	arg1	disease					210:216	Hirschsprung's disease	195:216	Hirschsprung's disease (HSCR)	195:223	The maturation of human RET is adversely affected by a range of missense mutations found in patients with Hirschsprung's disease (HSCR), a complex multigenic disease.
20473317	4	9	theme	human	650:654	arg1	RET					656:658	human RET	650:658	human RET	650:658	We identify two unpaired cysteines that predispose human RET to maturation impediments in the endoplasmic reticulum and establish a quantitative cell-based RET maturation assay that offers a biochemical correlate of HSCR disease severity.
20473317	1	10	theme	multigenic	236:245	arg1	disease					247:253	a complex multigenic disease	226:253	a complex multigenic disease	226:253	The maturation of human RET is adversely affected by a range of missense mutations found in patients with Hirschsprung's disease (HSCR), a complex multigenic disease.
20473317	1	10	theme	multigenic	236:245	arg1	disease					210:216	Hirschsprung's disease	195:216	Hirschsprung's disease (HSCR)	195:223	The maturation of human RET is adversely affected by a range of missense mutations found in patients with Hirschsprung's disease (HSCR), a complex multigenic disease.
20473317	4	11	theme	quantitative	731:742	arg1	assay					770:774	a quantitative cell-based RET maturation assay	729:774	a quantitative cell-based RET maturation assay that offers a biochemical correlate of HSCR disease severity	729:835	We identify two unpaired cysteines that predispose human RET to maturation impediments in the endoplasmic reticulum and establish a quantitative cell-based RET maturation assay that offers a biochemical correlate of HSCR disease severity.
20473317	1	12	theme	missense	153:160	arg1	mutations					162:170	missense mutations	153:170	missense mutations found in patients with Hirschsprung's disease (HSCR), a complex multigenic disease	153:253	The maturation of human RET is adversely affected by a range of missense mutations found in patients with Hirschsprung's disease (HSCR), a complex multigenic disease.
20473317	2	13	theme	distinct	384:391	arg1	arrangement					372:382	a clam-shell arrangement	359:382	a clam-shell arrangement distinct from that of classical cadherins	359:424	Here we show that two N-terminal cadherin-like domains, CLD1 and CLD2 (CLD(1-2)), from human RET adopt a clam-shell arrangement distinct from that of classical cadherins.
20473317	5	14	theme	conceptual	865:874	arg1	framework					876:884	a key conceptual framework	859:884	a key conceptual framework	859:884	Our findings provide a key conceptual framework and means of testing and predicting genotype-phenotype correlations in HSCR.
20473317	0	15	theme	Mammal-restricted	0:16	arg1	elements					18:25	Mammal-restricted elements	0:25	Mammal-restricted elements	0:25	Mammal-restricted elements predispose human RET to folding impairment by HSCR mutations.
20473317	1	16	theme	mutations	162:170	arg1	range					144:148	a range	142:148	a range of missense mutations found in patients with Hirschsprung's disease (HSCR), a complex multigenic disease	142:253	The maturation of human RET is adversely affected by a range of missense mutations found in patients with Hirschsprung's disease (HSCR), a complex multigenic disease.
20473317	2	17	from	that	398:401	arg1	distinct					384:391	distinct	384:391	distinct	384:391	Here we show that two N-terminal cadherin-like domains, CLD1 and CLD2 (CLD(1-2)), from human RET adopt a clam-shell arrangement distinct from that of classical cadherins.
20473317	4	18	theme	disease	820:826	arg1	severity					828:835	HSCR disease severity	815:835	HSCR disease severity	815:835	We identify two unpaired cysteines that predispose human RET to maturation impediments in the endoplasmic reticulum and establish a quantitative cell-based RET maturation assay that offers a biochemical correlate of HSCR disease severity.
20473317	2	19	theme	N-terminal	278:287	arg1	CLD2					321:324	CLD2	321:324	CLD2	321:324	Here we show that two N-terminal cadherin-like domains, CLD1 and CLD2 (CLD(1-2)), from human RET adopt a clam-shell arrangement distinct from that of classical cadherins.
20473317	2	19	theme	N-terminal	278:287	arg1	CLD1					312:315	CLD1	312:315	CLD1	312:315	Here we show that two N-terminal cadherin-like domains, CLD1 and CLD2 (CLD(1-2)), from human RET adopt a clam-shell arrangement distinct from that of classical cadherins.
20473317	2	19	theme	N-terminal	278:287	arg1	domains					303:309	two N-terminal cadherin-like domains	274:309	two N-terminal cadherin-like domains	274:309	Here we show that two N-terminal cadherin-like domains, CLD1 and CLD2 (CLD(1-2)), from human RET adopt a clam-shell arrangement distinct from that of classical cadherins.
20473317	4	20	theme	unpaired	615:622	arg1	cysteines					624:632	two unpaired cysteines	611:632	two unpaired cysteines that predispose human RET to maturation impediments in the endoplasmic reticulum	611:713	We identify two unpaired cysteines that predispose human RET to maturation impediments in the endoplasmic reticulum and establish a quantitative cell-based RET maturation assay that offers a biochemical correlate of HSCR disease severity.
20473317	2	21	theme	clam-shell	361:370	arg1	arrangement					372:382	a clam-shell arrangement	359:382	a clam-shell arrangement distinct from that of classical cadherins	359:424	Here we show that two N-terminal cadherin-like domains, CLD1 and CLD2 (CLD(1-2)), from human RET adopt a clam-shell arrangement distinct from that of classical cadherins.
20473317	4	22	theme	maturation	663:672	arg1	impediments					674:684	maturation impediments	663:684	maturation impediments in the endoplasmic reticulum	663:713	We identify two unpaired cysteines that predispose human RET to maturation impediments in the endoplasmic reticulum and establish a quantitative cell-based RET maturation assay that offers a biochemical correlate of HSCR disease severity.
20473317	0	23	theme	human	38:42	arg1	RET					44:46	human RET	38:46	human RET	38:46	Mammal-restricted elements predispose human RET to folding impairment by HSCR mutations.
20473317	1	24	theme	human	107:111	arg1	RET					113:115	human RET	107:115	human RET	107:115	The maturation of human RET is adversely affected by a range of missense mutations found in patients with Hirschsprung's disease (HSCR), a complex multigenic disease.
20473317	2	25	theme	human	343:347	arg1	RET					349:351	human RET	343:351	human RET	343:351	Here we show that two N-terminal cadherin-like domains, CLD1 and CLD2 (CLD(1-2)), from human RET adopt a clam-shell arrangement distinct from that of classical cadherins.
20473317	1	26	with	patients	181:188	arg1	HSCR					219:222	HSCR	219:222	HSCR	219:222	The maturation of human RET is adversely affected by a range of missense mutations found in patients with Hirschsprung's disease (HSCR), a complex multigenic disease.
20473317	1	26	with	patients	181:188	arg1	disease					210:216	Hirschsprung's disease	195:216	Hirschsprung's disease (HSCR)	195:223	The maturation of human RET is adversely affected by a range of missense mutations found in patients with Hirschsprung's disease (HSCR), a complex multigenic disease.
20473317	1	26	with	patients	181:188	arg1	disease					247:253	a complex multigenic disease	226:253	a complex multigenic disease	226:253	The maturation of human RET is adversely affected by a range of missense mutations found in patients with Hirschsprung's disease (HSCR), a complex multigenic disease.
20473317	3	27	theme	RET	582:584	arg1	regions					590:596	higher and lower vertebrate RET CLD regions	554:596	higher and lower vertebrate RET CLD regions	554:596	CLD1 structural elements and disulfide composition are unique to mammals, indicating an unexpected structural diversity within higher and lower vertebrate RET CLD regions.
20473317	1	28	located	found	172:176	arg2	mutations					162:170	missense mutations	153:170	missense mutations found in patients with Hirschsprung's disease (HSCR), a complex multigenic disease	153:253	The maturation of human RET is adversely affected by a range of missense mutations found in patients with Hirschsprung's disease (HSCR), a complex multigenic disease.
20473317	1	28	located	found	172:176	arg1	patients					181:188	patients	181:188	patients with Hirschsprung's disease (HSCR), a complex multigenic disease	181:253	The maturation of human RET is adversely affected by a range of missense mutations found in patients with Hirschsprung's disease (HSCR), a complex multigenic disease.
20473317	3	29	theme	unexpected	515:524	arg1	diversity					537:545	an unexpected structural diversity	512:545	an unexpected structural diversity within higher and lower vertebrate RET CLD regions	512:596	CLD1 structural elements and disulfide composition are unique to mammals, indicating an unexpected structural diversity within higher and lower vertebrate RET CLD regions.
20473317	4	30	theme	HSCR	815:818	arg1	severity					828:835	HSCR disease severity	815:835	HSCR disease severity	815:835	We identify two unpaired cysteines that predispose human RET to maturation impediments in the endoplasmic reticulum and establish a quantitative cell-based RET maturation assay that offers a biochemical correlate of HSCR disease severity.
20473317	1	31	theme	RET	113:115	arg1	maturation					93:102	The maturation	89:102	The maturation of human RET	89:115	The maturation of human RET is adversely affected by a range of missense mutations found in patients with Hirschsprung's disease (HSCR), a complex multigenic disease.
20473317	0	32	theme	folding	51:57	arg1	impairment					59:68	folding impairment	51:68	folding impairment by HSCR mutations	51:86	Mammal-restricted elements predispose human RET to folding impairment by HSCR mutations.
20473317	3	33	theme	structural	526:535	arg1	diversity					537:545	an unexpected structural diversity	512:545	an unexpected structural diversity within higher and lower vertebrate RET CLD regions	512:596	CLD1 structural elements and disulfide composition are unique to mammals, indicating an unexpected structural diversity within higher and lower vertebrate RET CLD regions.
20473317	3	34	theme	CLD1	427:430	arg1	elements					443:450	CLD1 structural elements	427:450	CLD1 structural elements	427:450	CLD1 structural elements and disulfide composition are unique to mammals, indicating an unexpected structural diversity within higher and lower vertebrate RET CLD regions.
20473317	4	35	from	impediments	674:684	arg1	reticulum					705:713	the endoplasmic reticulum	689:713	the endoplasmic reticulum	689:713	We identify two unpaired cysteines that predispose human RET to maturation impediments in the endoplasmic reticulum and establish a quantitative cell-based RET maturation assay that offers a biochemical correlate of HSCR disease severity.
20473317	4	36	theme	RET	755:757	arg1	assay					770:774	a quantitative cell-based RET maturation assay	729:774	a quantitative cell-based RET maturation assay that offers a biochemical correlate of HSCR disease severity	729:835	We identify two unpaired cysteines that predispose human RET to maturation impediments in the endoplasmic reticulum and establish a quantitative cell-based RET maturation assay that offers a biochemical correlate of HSCR disease severity.
20473317	3	37	theme	lower	565:569	arg1	regions					590:596	higher and lower vertebrate RET CLD regions	554:596	higher and lower vertebrate RET CLD regions	554:596	CLD1 structural elements and disulfide composition are unique to mammals, indicating an unexpected structural diversity within higher and lower vertebrate RET CLD regions.
20473317	3	38	theme	vertebrate	571:580	arg1	regions					590:596	higher and lower vertebrate RET CLD regions	554:596	higher and lower vertebrate RET CLD regions	554:596	CLD1 structural elements and disulfide composition are unique to mammals, indicating an unexpected structural diversity within higher and lower vertebrate RET CLD regions.
20473317	2	39	theme	cadherin-like	289:301	arg1	CLD2					321:324	CLD2	321:324	CLD2	321:324	Here we show that two N-terminal cadherin-like domains, CLD1 and CLD2 (CLD(1-2)), from human RET adopt a clam-shell arrangement distinct from that of classical cadherins.
20473317	2	39	theme	cadherin-like	289:301	arg1	CLD1					312:315	CLD1	312:315	CLD1	312:315	Here we show that two N-terminal cadherin-like domains, CLD1 and CLD2 (CLD(1-2)), from human RET adopt a clam-shell arrangement distinct from that of classical cadherins.
20473317	2	39	theme	cadherin-like	289:301	arg1	domains					303:309	two N-terminal cadherin-like domains	274:309	two N-terminal cadherin-like domains	274:309	Here we show that two N-terminal cadherin-like domains, CLD1 and CLD2 (CLD(1-2)), from human RET adopt a clam-shell arrangement distinct from that of classical cadherins.
20473317	0	40	theme	HSCR	73:76	arg1	mutations					78:86	HSCR mutations	73:86	HSCR mutations	73:86	Mammal-restricted elements predispose human RET to folding impairment by HSCR mutations.
20473317	3	41	theme	higher	554:559	arg1	regions					590:596	higher and lower vertebrate RET CLD regions	554:596	higher and lower vertebrate RET CLD regions	554:596	CLD1 structural elements and disulfide composition are unique to mammals, indicating an unexpected structural diversity within higher and lower vertebrate RET CLD regions.
20473317	5	42	theme	genotype-phenotype	922:939	arg1	correlations					941:952	genotype-phenotype correlations	922:952	genotype-phenotype correlations	922:952	Our findings provide a key conceptual framework and means of testing and predicting genotype-phenotype correlations in HSCR.
20473317	4	43	theme	maturation	759:768	arg1	assay					770:774	a quantitative cell-based RET maturation assay	729:774	a quantitative cell-based RET maturation assay that offers a biochemical correlate of HSCR disease severity	729:835	We identify two unpaired cysteines that predispose human RET to maturation impediments in the endoplasmic reticulum and establish a quantitative cell-based RET maturation assay that offers a biochemical correlate of HSCR disease severity.
20473317	2	44	from	RET	349:351	arg1	CLD2					321:324	CLD2	321:324	CLD2	321:324	Here we show that two N-terminal cadherin-like domains, CLD1 and CLD2 (CLD(1-2)), from human RET adopt a clam-shell arrangement distinct from that of classical cadherins.
20473317	2	44	from	RET	349:351	arg1	CLD1					312:315	CLD1	312:315	CLD1	312:315	Here we show that two N-terminal cadherin-like domains, CLD1 and CLD2 (CLD(1-2)), from human RET adopt a clam-shell arrangement distinct from that of classical cadherins.
20473317	2	44	from	RET	349:351	arg1	domains					303:309	two N-terminal cadherin-like domains	274:309	two N-terminal cadherin-like domains	274:309	Here we show that two N-terminal cadherin-like domains, CLD1 and CLD2 (CLD(1-2)), from human RET adopt a clam-shell arrangement distinct from that of classical cadherins.
20473317	3	45	theme	disulfide	456:464	arg1	composition					466:476	disulfide composition	456:476	disulfide composition	456:476	CLD1 structural elements and disulfide composition are unique to mammals, indicating an unexpected structural diversity within higher and lower vertebrate RET CLD regions.
12768205	0	0	theme	FcalphaRI	81:89	arg1	structures					61:70	the crystal structures	49:70	the crystal structures of human FcalphaRI	49:89	Insights into IgA-mediated immune responses from the crystal structures of human FcalphaRI and its complex with IgA1-Fc.
12768205	1	1	theme	-bound	147:152	arg1	antigens					154:161	Immunoglobulin-alpha (IgA)-bound antigens	121:161	Immunoglobulin-alpha (IgA)-bound antigens	121:161	Immunoglobulin-alpha (IgA)-bound antigens induce immune effector responses by activating the IgA-specific receptor FcalphaRI (CD89) on immune cells.
12768205	6	2	theme	reported	864:871	arg1	pIgR					908:911	pIgR	908:911	pIgR	908:911	The FcalphaRI-binding site on IgA1 overlaps the reported polymeric immunoglobulin receptor (pIgR)-binding site, which might explain why secretory IgA cannot initiate phagocytosis or bind to FcalphaRI-expressing cells in the absence of an integrin co-receptor.
12768205	6	2	theme	reported	864:871	arg1	receptor					898:905	reported polymeric immunoglobulin receptor	864:905	reported polymeric immunoglobulin receptor (pIgR)	864:912	The FcalphaRI-binding site on IgA1 overlaps the reported polymeric immunoglobulin receptor (pIgR)-binding site, which might explain why secretory IgA cannot initiate phagocytosis or bind to FcalphaRI-expressing cells in the absence of an integrin co-receptor.
12768205	0	3	theme	human	75:79	arg1	FcalphaRI					81:89	human FcalphaRI	75:89	human FcalphaRI	75:89	Insights into IgA-mediated immune responses from the crystal structures of human FcalphaRI and its complex with IgA1-Fc.
12768205	6	4	theme	immunoglobulin	883:896	arg1	pIgR					908:911	pIgR	908:911	pIgR	908:911	The FcalphaRI-binding site on IgA1 overlaps the reported polymeric immunoglobulin receptor (pIgR)-binding site, which might explain why secretory IgA cannot initiate phagocytosis or bind to FcalphaRI-expressing cells in the absence of an integrin co-receptor.
12768205	6	4	theme	immunoglobulin	883:896	arg1	receptor					898:905	reported polymeric immunoglobulin receptor	864:905	reported polymeric immunoglobulin receptor (pIgR)	864:912	The FcalphaRI-binding site on IgA1 overlaps the reported polymeric immunoglobulin receptor (pIgR)-binding site, which might explain why secretory IgA cannot initiate phagocytosis or bind to FcalphaRI-expressing cells in the absence of an integrin co-receptor.
12768205	6	5	theme	integrin	1054:1061	arg1	co-receptor					1063:1073	an integrin co-receptor	1051:1073	an integrin co-receptor	1051:1073	The FcalphaRI-binding site on IgA1 overlaps the reported polymeric immunoglobulin receptor (pIgR)-binding site, which might explain why secretory IgA cannot initiate phagocytosis or bind to FcalphaRI-expressing cells in the absence of an integrin co-receptor.
12768205	6	6	theme	IgA	962:964	arg1	cannot					966:971	secretory IgA cannot	952:971	secretory IgA cannot	952:971	The FcalphaRI-binding site on IgA1 overlaps the reported polymeric immunoglobulin receptor (pIgR)-binding site, which might explain why secretory IgA cannot initiate phagocytosis or bind to FcalphaRI-expressing cells in the absence of an integrin co-receptor.
12768205	5	7	theme	epsilon	703:709	arg1	RI					711:712	Fc epsilon RI	700:712	Fc epsilon RI	700:712	Unlike 1:1 FcgammaRIII:IgG and Fc epsilon RI:IgE complexes, two FcalphaRI molecules bind each Fcalpha dimer, one at each Calpha2-Calpha3 junction.
12768205	6	8	theme	polymeric	873:881	arg1	pIgR					908:911	pIgR	908:911	pIgR	908:911	The FcalphaRI-binding site on IgA1 overlaps the reported polymeric immunoglobulin receptor (pIgR)-binding site, which might explain why secretory IgA cannot initiate phagocytosis or bind to FcalphaRI-expressing cells in the absence of an integrin co-receptor.
12768205	6	8	theme	polymeric	873:881	arg1	receptor					898:905	reported polymeric immunoglobulin receptor	864:905	reported polymeric immunoglobulin receptor (pIgR)	864:912	The FcalphaRI-binding site on IgA1 overlaps the reported polymeric immunoglobulin receptor (pIgR)-binding site, which might explain why secretory IgA cannot initiate phagocytosis or bind to FcalphaRI-expressing cells in the absence of an integrin co-receptor.
12768205	1	9	theme	immune	256:261	arg1	cells					263:267	immune cells	256:267	immune cells	256:267	Immunoglobulin-alpha (IgA)-bound antigens induce immune effector responses by activating the IgA-specific receptor FcalphaRI (CD89) on immune cells.
12768205	5	10	dep	FcgammaRIII	680:690	arg1	IgG					692:694	IgG	692:694	IgG	692:694	Unlike 1:1 FcgammaRIII:IgG and Fc epsilon RI:IgE complexes, two FcalphaRI molecules bind each Fcalpha dimer, one at each Calpha2-Calpha3 junction.
12768205	5	10	dep	FcgammaRIII	680:690	arg1	RI					711:712	Fc epsilon RI	700:712	Fc epsilon RI	700:712	Unlike 1:1 FcgammaRIII:IgG and Fc epsilon RI:IgE complexes, two FcalphaRI molecules bind each Fcalpha dimer, one at each Calpha2-Calpha3 junction.
12768205	5	10	dep	FcgammaRIII	680:690	arg1	complexes					718:726	IgE complexes	714:726	FcgammaRIII:IgG and Fc epsilon RI:IgE complexes	680:726	Unlike 1:1 FcgammaRIII:IgG and Fc epsilon RI:IgE complexes, two FcalphaRI molecules bind each Fcalpha dimer, one at each Calpha2-Calpha3 junction.
12768205	4	11	contain	has	556:558	arg2	carbohydrates					654:666	interdomain N-linked carbohydrates	633:666	interdomain N-linked carbohydrates	633:666	Fcalpha resembles the Fcs of immunoglobulins IgG and IgE, but has differently located interchain disulphide bonds and external rather than interdomain N-linked carbohydrates.
12768205	4	11	contain	has	556:558	arg2	bonds					602:606	differently located interchain disulphide bonds	560:606	differently located interchain disulphide bonds	560:606	Fcalpha resembles the Fcs of immunoglobulins IgG and IgE, but has differently located interchain disulphide bonds and external rather than interdomain N-linked carbohydrates.
12768205	4	11	contain	has	556:558	arg1	Fcalpha					494:500	Fcalpha	494:500	Fcalpha	494:500	Fcalpha resembles the Fcs of immunoglobulins IgG and IgE, but has differently located interchain disulphide bonds and external rather than interdomain N-linked carbohydrates.
12768205	4	11	contain	has	556:558	arg2	external					612:619	external	612:619	external	612:619	Fcalpha resembles the Fcs of immunoglobulins IgG and IgE, but has differently located interchain disulphide bonds and external rather than interdomain N-linked carbohydrates.
12768205	6	12	theme	co-receptor	1063:1073	arg1	absence					1040:1046	the absence	1036:1046	the absence of an integrin co-receptor	1036:1073	The FcalphaRI-binding site on IgA1 overlaps the reported polymeric immunoglobulin receptor (pIgR)-binding site, which might explain why secretory IgA cannot initiate phagocytosis or bind to FcalphaRI-expressing cells in the absence of an integrin co-receptor.
12768205	2	13	theme	IgA1	369:372	arg1	region					359:364	the Fc region	352:364	the Fc region of IgA1 (Fcalpha)	352:382	Here we present crystal structures of human FcalphaRI alone and in a complex with the Fc region of IgA1 (Fcalpha).
12768205	5	14	theme	IgE	714:716	arg1	complexes					718:726	IgE complexes	714:726	FcgammaRIII:IgG and Fc epsilon RI:IgE complexes	680:726	Unlike 1:1 FcgammaRIII:IgG and Fc epsilon RI:IgE complexes, two FcalphaRI molecules bind each Fcalpha dimer, one at each Calpha2-Calpha3 junction.
12768205	4	15	dep	immunoglobulins	523:537	arg1	immunoglobulins					523:537	immunoglobulins IgG and IgE	523:549	immunoglobulins IgG and IgE	523:549	Fcalpha resembles the Fcs of immunoglobulins IgG and IgE, but has differently located interchain disulphide bonds and external rather than interdomain N-linked carbohydrates.
12768205	4	15	dep	immunoglobulins	523:537	arg1	IgE					547:549	IgE	547:549	IgE	547:549	Fcalpha resembles the Fcs of immunoglobulins IgG and IgE, but has differently located interchain disulphide bonds and external rather than interdomain N-linked carbohydrates.
12768205	4	15	dep	immunoglobulins	523:537	arg1	IgG					539:541	IgG	539:541	IgG	539:541	Fcalpha resembles the Fcs of immunoglobulins IgG and IgE, but has differently located interchain disulphide bonds and external rather than interdomain N-linked carbohydrates.
12768205	1	16	theme	immune	170:175	arg1	responses					186:194	immune effector responses	170:194	immune effector responses	170:194	Immunoglobulin-alpha (IgA)-bound antigens induce immune effector responses by activating the IgA-specific receptor FcalphaRI (CD89) on immune cells.
12768205	5	17	theme	FcalphaRI	733:741	arg1	molecules					743:751	two FcalphaRI molecules	729:751	two FcalphaRI molecules	729:751	Unlike 1:1 FcgammaRIII:IgG and Fc epsilon RI:IgE complexes, two FcalphaRI molecules bind each Fcalpha dimer, one at each Calpha2-Calpha3 junction.
12768205	0	18	with	complex	99:105	arg1	IgA1-Fc					112:118	IgA1-Fc	112:118	IgA1-Fc	112:118	Insights into IgA-mediated immune responses from the crystal structures of human FcalphaRI and its complex with IgA1-Fc.
12768205	2	19	theme	human	308:312	arg1	FcalphaRI					314:322	human FcalphaRI	308:322	human FcalphaRI alone and in a complex with the Fc region of IgA1 (Fcalpha)	308:382	Here we present crystal structures of human FcalphaRI alone and in a complex with the Fc region of IgA1 (Fcalpha).
12768205	1	20	theme	effector	177:184	arg1	responses					186:194	immune effector responses	170:194	immune effector responses	170:194	Immunoglobulin-alpha (IgA)-bound antigens induce immune effector responses by activating the IgA-specific receptor FcalphaRI (CD89) on immune cells.
12768205	4	21	theme	immunoglobulins	523:537	arg1	Fcs					516:518	the Fcs	512:518	the Fcs of immunoglobulins IgG and IgE	512:549	Fcalpha resembles the Fcs of immunoglobulins IgG and IgE, but has differently located interchain disulphide bonds and external rather than interdomain N-linked carbohydrates.
12768205	2	22	with	complex	339:345	arg1	region					359:364	the Fc region	352:364	the Fc region of IgA1 (Fcalpha)	352:382	Here we present crystal structures of human FcalphaRI alone and in a complex with the Fc region of IgA1 (Fcalpha).
12768205	2	23	theme	Fc	356:357	arg1	region					359:364	the Fc region	352:364	the Fc region of IgA1 (Fcalpha)	352:382	Here we present crystal structures of human FcalphaRI alone and in a complex with the Fc region of IgA1 (Fcalpha).
12768205	0	24	theme	immune	27:32	arg1	responses					34:42	IgA-mediated immune responses	14:42	IgA-mediated immune responses from the crystal structures of human FcalphaRI	14:89	Insights into IgA-mediated immune responses from the crystal structures of human FcalphaRI and its complex with IgA1-Fc.
12768205	0	25	theme	IgA-mediated	14:25	arg1	responses					34:42	IgA-mediated immune responses	14:42	IgA-mediated immune responses from the crystal structures of human FcalphaRI	14:89	Insights into IgA-mediated immune responses from the crystal structures of human FcalphaRI and its complex with IgA1-Fc.
12768205	2	26	theme	crystal	286:292	arg1	structures					294:303	crystal structures	286:303	crystal structures of human FcalphaRI alone and in a complex with the Fc region of IgA1 (Fcalpha)	286:382	Here we present crystal structures of human FcalphaRI alone and in a complex with the Fc region of IgA1 (Fcalpha).
12768205	5	27	theme	Calpha2-Calpha3	790:804	arg1	junction					806:813	each Calpha2-Calpha3 junction	785:813	each Calpha2-Calpha3 junction	785:813	Unlike 1:1 FcgammaRIII:IgG and Fc epsilon RI:IgE complexes, two FcalphaRI molecules bind each Fcalpha dimer, one at each Calpha2-Calpha3 junction.
12768205	4	28	theme	N-linked	645:652	arg1	carbohydrates					654:666	interdomain N-linked carbohydrates	633:666	interdomain N-linked carbohydrates	633:666	Fcalpha resembles the Fcs of immunoglobulins IgG and IgE, but has differently located interchain disulphide bonds and external rather than interdomain N-linked carbohydrates.
12768205	6	29	theme	FcalphaRI-expressing	1006:1025	arg1	cells					1027:1031	FcalphaRI-expressing cells	1006:1031	FcalphaRI-expressing cells	1006:1031	The FcalphaRI-binding site on IgA1 overlaps the reported polymeric immunoglobulin receptor (pIgR)-binding site, which might explain why secretory IgA cannot initiate phagocytosis or bind to FcalphaRI-expressing cells in the absence of an integrin co-receptor.
12768205	4	30	theme	interdomain	633:643	arg1	carbohydrates					654:666	interdomain N-linked carbohydrates	633:666	interdomain N-linked carbohydrates	633:666	Fcalpha resembles the Fcs of immunoglobulins IgG and IgE, but has differently located interchain disulphide bonds and external rather than interdomain N-linked carbohydrates.
12768205	5	31	theme	Fc	700:701	arg1	RI					711:712	Fc epsilon RI	700:712	Fc epsilon RI	700:712	Unlike 1:1 FcgammaRIII:IgG and Fc epsilon RI:IgE complexes, two FcalphaRI molecules bind each Fcalpha dimer, one at each Calpha2-Calpha3 junction.
12768205	6	32	theme	FcalphaRI-binding	820:836	arg1	site					838:841	The FcalphaRI-binding site	816:841	The FcalphaRI-binding site on IgA1	816:849	The FcalphaRI-binding site on IgA1 overlaps the reported polymeric immunoglobulin receptor (pIgR)-binding site, which might explain why secretory IgA cannot initiate phagocytosis or bind to FcalphaRI-expressing cells in the absence of an integrin co-receptor.
12768205	4	33	link	N-linked	645:652	arg1	carbohydrates					654:666	interdomain N-linked carbohydrates	633:666	interdomain N-linked carbohydrates	633:666	Fcalpha resembles the Fcs of immunoglobulins IgG and IgE, but has differently located interchain disulphide bonds and external rather than interdomain N-linked carbohydrates.
12768205	5	34	from	junction	806:813	arg1	one					778:780	one	778:780	one	778:780	Unlike 1:1 FcgammaRIII:IgG and Fc epsilon RI:IgE complexes, two FcalphaRI molecules bind each Fcalpha dimer, one at each Calpha2-Calpha3 junction.
12768205	5	34	from	junction	806:813	arg1	dimer					771:775	each Fcalpha dimer	758:775	each Fcalpha dimer	758:775	Unlike 1:1 FcgammaRIII:IgG and Fc epsilon RI:IgE complexes, two FcalphaRI molecules bind each Fcalpha dimer, one at each Calpha2-Calpha3 junction.
12768205	1	35	theme	IgA-specific	214:225	arg1	CD89					247:250	CD89	247:250	CD89	247:250	Immunoglobulin-alpha (IgA)-bound antigens induce immune effector responses by activating the IgA-specific receptor FcalphaRI (CD89) on immune cells.
12768205	1	35	theme	IgA-specific	214:225	arg1	FcalphaRI					236:244	the IgA-specific receptor FcalphaRI	210:244	the IgA-specific receptor FcalphaRI (CD89) on immune cells	210:267	Immunoglobulin-alpha (IgA)-bound antigens induce immune effector responses by activating the IgA-specific receptor FcalphaRI (CD89) on immune cells.
12768205	0	36	theme	crystal	53:59	arg1	structures					61:70	the crystal structures	49:70	the crystal structures of human FcalphaRI	49:89	Insights into IgA-mediated immune responses from the crystal structures of human FcalphaRI and its complex with IgA1-Fc.
12768205	6	37	theme	-binding	913:920	arg1	site					922:925	the reported polymeric immunoglobulin receptor (pIgR)-binding site	860:925	the reported polymeric immunoglobulin receptor (pIgR)-binding site	860:925	The FcalphaRI-binding site on IgA1 overlaps the reported polymeric immunoglobulin receptor (pIgR)-binding site, which might explain why secretory IgA cannot initiate phagocytosis or bind to FcalphaRI-expressing cells in the absence of an integrin co-receptor.
12768205	0	38	from	structures	61:70	arg1	responses					34:42	IgA-mediated immune responses	14:42	IgA-mediated immune responses from the crystal structures of human FcalphaRI	14:89	Insights into IgA-mediated immune responses from the crystal structures of human FcalphaRI and its complex with IgA1-Fc.
12768205	3	39	theme	right	466:470	arg1	angles					472:477	approximately right angles	452:477	approximately right angles to each other	452:491	FcalphaRI has two immunoglobulin-like domains that are oriented at approximately right angles to each other.
12768205	5	40	theme	Fcalpha	763:769	arg1	one					778:780	one	778:780	one	778:780	Unlike 1:1 FcgammaRIII:IgG and Fc epsilon RI:IgE complexes, two FcalphaRI molecules bind each Fcalpha dimer, one at each Calpha2-Calpha3 junction.
12768205	5	40	theme	Fcalpha	763:769	arg1	dimer					771:775	each Fcalpha dimer	758:775	each Fcalpha dimer	758:775	Unlike 1:1 FcgammaRIII:IgG and Fc epsilon RI:IgE complexes, two FcalphaRI molecules bind each Fcalpha dimer, one at each Calpha2-Calpha3 junction.
12768205	3	41	contain	has	395:397	arg1	FcalphaRI					385:393	FcalphaRI	385:393	FcalphaRI	385:393	FcalphaRI has two immunoglobulin-like domains that are oriented at approximately right angles to each other.
12768205	3	41	contain	has	395:397	arg2	domains					423:429	two immunoglobulin-like domains	399:429	two immunoglobulin-like domains that are oriented at approximately right angles to each other	399:491	FcalphaRI has two immunoglobulin-like domains that are oriented at approximately right angles to each other.
12768205	0	42	with	Insights	0:7	arg1	IgA1-Fc					112:118	IgA1-Fc	112:118	IgA1-Fc	112:118	Insights into IgA-mediated immune responses from the crystal structures of human FcalphaRI and its complex with IgA1-Fc.
12768205	1	43	theme	receptor	227:234	arg1	CD89					247:250	CD89	247:250	CD89	247:250	Immunoglobulin-alpha (IgA)-bound antigens induce immune effector responses by activating the IgA-specific receptor FcalphaRI (CD89) on immune cells.
12768205	1	43	theme	receptor	227:234	arg1	FcalphaRI					236:244	the IgA-specific receptor FcalphaRI	210:244	the IgA-specific receptor FcalphaRI (CD89) on immune cells	210:267	Immunoglobulin-alpha (IgA)-bound antigens induce immune effector responses by activating the IgA-specific receptor FcalphaRI (CD89) on immune cells.
12768205	1	44	from	FcalphaRI	236:244	arg1	cells					263:267	immune cells	256:267	immune cells	256:267	Immunoglobulin-alpha (IgA)-bound antigens induce immune effector responses by activating the IgA-specific receptor FcalphaRI (CD89) on immune cells.
12768205	2	45	theme	FcalphaRI	314:322	arg1	structures					294:303	crystal structures	286:303	crystal structures of human FcalphaRI alone and in a complex with the Fc region of IgA1 (Fcalpha)	286:382	Here we present crystal structures of human FcalphaRI alone and in a complex with the Fc region of IgA1 (Fcalpha).
12768205	3	46	theme	immunoglobulin-like	403:421	arg1	domains					423:429	two immunoglobulin-like domains	399:429	two immunoglobulin-like domains that are oriented at approximately right angles to each other	399:491	FcalphaRI has two immunoglobulin-like domains that are oriented at approximately right angles to each other.
12768205	4	47	theme	disulphide	591:600	arg1	bonds					602:606	differently located interchain disulphide bonds	560:606	differently located interchain disulphide bonds	560:606	Fcalpha resembles the Fcs of immunoglobulins IgG and IgE, but has differently located interchain disulphide bonds and external rather than interdomain N-linked carbohydrates.
12768205	6	48	theme	secretory	952:960	arg1	cannot					966:971	secretory IgA cannot	952:971	secretory IgA cannot	952:971	The FcalphaRI-binding site on IgA1 overlaps the reported polymeric immunoglobulin receptor (pIgR)-binding site, which might explain why secretory IgA cannot initiate phagocytosis or bind to FcalphaRI-expressing cells in the absence of an integrin co-receptor.
12768205	6	49	from	site	838:841	arg1	IgA1					846:849	IgA1	846:849	IgA1	846:849	The FcalphaRI-binding site on IgA1 overlaps the reported polymeric immunoglobulin receptor (pIgR)-binding site, which might explain why secretory IgA cannot initiate phagocytosis or bind to FcalphaRI-expressing cells in the absence of an integrin co-receptor.
12768205	4	50	theme	located	572:578	arg1	bonds					602:606	differently located interchain disulphide bonds	560:606	differently located interchain disulphide bonds	560:606	Fcalpha resembles the Fcs of immunoglobulins IgG and IgE, but has differently located interchain disulphide bonds and external rather than interdomain N-linked carbohydrates.
12768205	4	51	theme	interchain	580:589	arg1	bonds					602:606	differently located interchain disulphide bonds	560:606	differently located interchain disulphide bonds	560:606	Fcalpha resembles the Fcs of immunoglobulins IgG and IgE, but has differently located interchain disulphide bonds and external rather than interdomain N-linked carbohydrates.
19349973	1	0	theme	single	359:364	arg1	measurement					366:376	a single measurement	357:376	a single measurement	357:376	Although the classification of cell types often relies on the identification of cell surface proteins as differentiation markers, flow cytometry requires suitable antibodies and currently permits detection of only up to a dozen differentiation markers in a single measurement.
19349973	2	1	from	antibodies	560:569	arg1	fashion					586:592	an unbiased fashion	574:592	an unbiased fashion	574:592	We use multiplexed mass-spectrometric identification of several hundred N-linked glycosylation sites specifically from cell surface-exposed glycoproteins to phenotype cells without antibodies in an unbiased fashion and without a priori knowledge.
19349973	3	2	theme	relative	770:777	arg1	comparison					792:801	relative quantitative comparison	770:801	relative quantitative comparison	770:801	We apply our cell surface-capturing (CSC) technology, which covalently labels extracellular glycan moieties on live cells, to the detection and relative quantitative comparison of the cell surface N-glycoproteomes of T and B cells, as well as to monitor changes in the abundance of cell surface N-glycoprotein markers during T-cell activation and the controlled differentiation of embryonic stem cells into the neural lineage.
19349973	1	3	theme	cell	182:185	arg1	proteins					195:202	cell surface proteins	182:202	cell surface proteins as differentiation markers	182:229	Although the classification of cell types often relies on the identification of cell surface proteins as differentiation markers, flow cytometry requires suitable antibodies and currently permits detection of only up to a dozen differentiation markers in a single measurement.
19349973	3	4	theme	surface	913:919	arg1	markers					936:942	cell surface N-glycoprotein markers	908:942	cell surface N-glycoprotein markers	908:942	We apply our cell surface-capturing (CSC) technology, which covalently labels extracellular glycan moieties on live cells, to the detection and relative quantitative comparison of the cell surface N-glycoproteomes of T and B cells, as well as to monitor changes in the abundance of cell surface N-glycoprotein markers during T-cell activation and the controlled differentiation of embryonic stem cells into the neural lineage.
19349973	3	5	theme	N-glycoprotein	921:934	arg1	markers					936:942	cell surface N-glycoprotein markers	908:942	cell surface N-glycoprotein markers	908:942	We apply our cell surface-capturing (CSC) technology, which covalently labels extracellular glycan moieties on live cells, to the detection and relative quantitative comparison of the cell surface N-glycoproteomes of T and B cells, as well as to monitor changes in the abundance of cell surface N-glycoprotein markers during T-cell activation and the controlled differentiation of embryonic stem cells into the neural lineage.
19349973	3	6	from	moieties	725:732	arg1	cells					742:746	live cells	737:746	live cells	737:746	We apply our cell surface-capturing (CSC) technology, which covalently labels extracellular glycan moieties on live cells, to the detection and relative quantitative comparison of the cell surface N-glycoproteomes of T and B cells, as well as to monitor changes in the abundance of cell surface N-glycoprotein markers during T-cell activation and the controlled differentiation of embryonic stem cells into the neural lineage.
19349973	2	7	gly	glycosylation	460:472	arg2	sites					474:478	several hundred N-linked glycosylation sites	435:478	several hundred N-linked glycosylation sites	435:478	We use multiplexed mass-spectrometric identification of several hundred N-linked glycosylation sites specifically from cell surface-exposed glycoproteins to phenotype cells without antibodies in an unbiased fashion and without a priori knowledge.
19349973	2	7	gly	glycosylation	460:472	arg2	hundred					443:449	hundred	443:449	hundred	443:449	We use multiplexed mass-spectrometric identification of several hundred N-linked glycosylation sites specifically from cell surface-exposed glycoproteins to phenotype cells without antibodies in an unbiased fashion and without a priori knowledge.
19349973	3	8	gly	N-glycoprotein	921:934	arg1	N-glycoprotein					921:934	cell surface N-glycoprotein markers	908:942	cell surface N-glycoprotein markers	908:942	We apply our cell surface-capturing (CSC) technology, which covalently labels extracellular glycan moieties on live cells, to the detection and relative quantitative comparison of the cell surface N-glycoproteomes of T and B cells, as well as to monitor changes in the abundance of cell surface N-glycoprotein markers during T-cell activation and the controlled differentiation of embryonic stem cells into the neural lineage.
19349973	0	9	gly	glycoproteins	87:99	arg1	glycoproteins					87:99	N-linked cell surface glycoproteins	65:99	N-linked cell surface glycoproteins	65:99	Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.
19349973	3	10	theme	B	849:849	arg1	cells					851:855	T and B cells	843:855	cells	851:855	We apply our cell surface-capturing (CSC) technology, which covalently labels extracellular glycan moieties on live cells, to the detection and relative quantitative comparison of the cell surface N-glycoproteomes of T and B cells, as well as to monitor changes in the abundance of cell surface N-glycoprotein markers during T-cell activation and the controlled differentiation of embryonic stem cells into the neural lineage.
19349973	1	11	theme	surface	187:193	arg1	proteins					195:202	cell surface proteins	182:202	cell surface proteins as differentiation markers	182:229	Although the classification of cell types often relies on the identification of cell surface proteins as differentiation markers, flow cytometry requires suitable antibodies and currently permits detection of only up to a dozen differentiation markers in a single measurement.
19349973	4	12	theme	cell	1076:1079	arg1	N-glycoproteins					1089:1103	the cell surface N-glycoproteins	1072:1103	the cell surface N-glycoproteins	1072:1103	A snapshot view of the cell surface N-glycoproteins will enable detection of panels of N-glycoproteins as potential differentiation markers that are currently not accessible by other means.
19349973	3	13	theme	quantitative	779:790	arg1	comparison					792:801	relative quantitative comparison	770:801	relative quantitative comparison	770:801	We apply our cell surface-capturing (CSC) technology, which covalently labels extracellular glycan moieties on live cells, to the detection and relative quantitative comparison of the cell surface N-glycoproteomes of T and B cells, as well as to monitor changes in the abundance of cell surface N-glycoprotein markers during T-cell activation and the controlled differentiation of embryonic stem cells into the neural lineage.
19349973	2	14	theme	surface-exposed	503:517	arg1	glycoproteins					519:531	cell surface-exposed glycoproteins	498:531	cell surface-exposed glycoproteins	498:531	We use multiplexed mass-spectrometric identification of several hundred N-linked glycosylation sites specifically from cell surface-exposed glycoproteins to phenotype cells without antibodies in an unbiased fashion and without a priori knowledge.
19349973	2	15	theme	unbiased	577:584	arg1	fashion					586:592	an unbiased fashion	574:592	an unbiased fashion	574:592	We use multiplexed mass-spectrometric identification of several hundred N-linked glycosylation sites specifically from cell surface-exposed glycoproteins to phenotype cells without antibodies in an unbiased fashion and without a priori knowledge.
19349973	1	16	theme	proteins	195:202	arg1	identification					164:177	the identification	160:177	the identification of cell surface proteins as differentiation markers	160:229	Although the classification of cell types often relies on the identification of cell surface proteins as differentiation markers, flow cytometry requires suitable antibodies and currently permits detection of only up to a dozen differentiation markers in a single measurement.
19349973	4	17	theme	surface	1081:1087	arg1	N-glycoproteins					1089:1103	the cell surface N-glycoproteins	1072:1103	the cell surface N-glycoproteins	1072:1103	A snapshot view of the cell surface N-glycoproteins will enable detection of panels of N-glycoproteins as potential differentiation markers that are currently not accessible by other means.
19349973	3	18	theme	controlled	977:986	arg1	differentiation					988:1002	the controlled differentiation	973:1002	the controlled differentiation of embryonic stem cells into the neural lineage	973:1050	We apply our cell surface-capturing (CSC) technology, which covalently labels extracellular glycan moieties on live cells, to the detection and relative quantitative comparison of the cell surface N-glycoproteomes of T and B cells, as well as to monitor changes in the abundance of cell surface N-glycoprotein markers during T-cell activation and the controlled differentiation of embryonic stem cells into the neural lineage.
19349973	0	19	link	N-linked	65:72	arg1	glycoproteins					87:99	N-linked cell surface glycoproteins	65:99	N-linked cell surface glycoproteins	65:99	Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.
19349973	3	20	theme	cell	639:642	arg1	technology					668:677	our cell surface-capturing (CSC) technology	635:677	our cell surface-capturing (CSC) technology	635:677	We apply our cell surface-capturing (CSC) technology, which covalently labels extracellular glycan moieties on live cells, to the detection and relative quantitative comparison of the cell surface N-glycoproteomes of T and B cells, as well as to monitor changes in the abundance of cell surface N-glycoprotein markers during T-cell activation and the controlled differentiation of embryonic stem cells into the neural lineage.
19349973	0	21	theme	Mass-spectrometric	0:17	arg1	identification					19:32	Mass-spectrometric identification	0:32	Mass-spectrometric identification	0:32	Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.
19349973	1	22	theme	only	311:314	arg1	up					316:317	only up	311:317	only up to a dozen differentiation markers	311:352	Although the classification of cell types often relies on the identification of cell surface proteins as differentiation markers, flow cytometry requires suitable antibodies and currently permits detection of only up to a dozen differentiation markers in a single measurement.
19349973	3	23	theme	N-glycoproteomes	823:838	arg1	comparison					792:801	relative quantitative comparison	770:801	relative quantitative comparison	770:801	We apply our cell surface-capturing (CSC) technology, which covalently labels extracellular glycan moieties on live cells, to the detection and relative quantitative comparison of the cell surface N-glycoproteomes of T and B cells, as well as to monitor changes in the abundance of cell surface N-glycoprotein markers during T-cell activation and the controlled differentiation of embryonic stem cells into the neural lineage.
19349973	3	23	theme	N-glycoproteomes	823:838	arg1	detection					756:764	the detection	752:764	the detection	752:764	We apply our cell surface-capturing (CSC) technology, which covalently labels extracellular glycan moieties on live cells, to the detection and relative quantitative comparison of the cell surface N-glycoproteomes of T and B cells, as well as to monitor changes in the abundance of cell surface N-glycoprotein markers during T-cell activation and the controlled differentiation of embryonic stem cells into the neural lineage.
19349973	3	24	theme	surface-capturing	644:660	arg1	technology					668:677	our cell surface-capturing (CSC) technology	635:677	our cell surface-capturing (CSC) technology	635:677	We apply our cell surface-capturing (CSC) technology, which covalently labels extracellular glycan moieties on live cells, to the detection and relative quantitative comparison of the cell surface N-glycoproteomes of T and B cells, as well as to monitor changes in the abundance of cell surface N-glycoprotein markers during T-cell activation and the controlled differentiation of embryonic stem cells into the neural lineage.
19349973	1	25	theme	differentiation	207:221	arg1	markers					223:229	differentiation markers	207:229	differentiation markers	207:229	Although the classification of cell types often relies on the identification of cell surface proteins as differentiation markers, flow cytometry requires suitable antibodies and currently permits detection of only up to a dozen differentiation markers in a single measurement.
19349973	0	26	theme	relative	38:45	arg1	quantification					47:60	relative quantification	38:60	relative quantification	38:60	Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.
19349973	1	27	theme	up	316:317	arg1	detection					298:306	detection	298:306	detection of only up to a dozen differentiation markers	298:352	Although the classification of cell types often relies on the identification of cell surface proteins as differentiation markers, flow cytometry requires suitable antibodies and currently permits detection of only up to a dozen differentiation markers in a single measurement.
19349973	3	28	theme	embryonic	1007:1015	arg1	cells					1022:1026	embryonic stem cells	1007:1026	embryonic stem cells	1007:1026	We apply our cell surface-capturing (CSC) technology, which covalently labels extracellular glycan moieties on live cells, to the detection and relative quantitative comparison of the cell surface N-glycoproteomes of T and B cells, as well as to monitor changes in the abundance of cell surface N-glycoprotein markers during T-cell activation and the controlled differentiation of embryonic stem cells into the neural lineage.
19349973	4	29	theme	N-glycoproteins	1089:1103	arg1	view					1064:1067	A snapshot view	1053:1067	A snapshot view of the cell surface N-glycoproteins	1053:1103	A snapshot view of the cell surface N-glycoproteins will enable detection of panels of N-glycoproteins as potential differentiation markers that are currently not accessible by other means.
19349973	3	30	theme	cell	810:813	arg1	N-glycoproteomes					823:838	the cell surface N-glycoproteomes	806:838	the cell surface N-glycoproteomes of T and B cells	806:855	We apply our cell surface-capturing (CSC) technology, which covalently labels extracellular glycan moieties on live cells, to the detection and relative quantitative comparison of the cell surface N-glycoproteomes of T and B cells, as well as to monitor changes in the abundance of cell surface N-glycoprotein markers during T-cell activation and the controlled differentiation of embryonic stem cells into the neural lineage.
19349973	1	31	theme	cell	133:136	arg1	types					138:142	cell types	133:142	cell types	133:142	Although the classification of cell types often relies on the identification of cell surface proteins as differentiation markers, flow cytometry requires suitable antibodies and currently permits detection of only up to a dozen differentiation markers in a single measurement.
19349973	2	32	theme	phenotype	536:544	arg1	cells					546:550	phenotype cells	536:550	phenotype cells without antibodies in an unbiased fashion and without a priori knowledge	536:623	We use multiplexed mass-spectrometric identification of several hundred N-linked glycosylation sites specifically from cell surface-exposed glycoproteins to phenotype cells without antibodies in an unbiased fashion and without a priori knowledge.
19349973	2	33	theme	sites	474:478	arg1	identification					417:430	multiplexed mass-spectrometric identification	386:430	multiplexed mass-spectrometric identification of several hundred N-linked glycosylation sites	386:478	We use multiplexed mass-spectrometric identification of several hundred N-linked glycosylation sites specifically from cell surface-exposed glycoproteins to phenotype cells without antibodies in an unbiased fashion and without a priori knowledge.
19349973	3	34	theme	surface	815:821	arg1	N-glycoproteomes					823:838	the cell surface N-glycoproteomes	806:838	the cell surface N-glycoproteomes of T and B cells	806:855	We apply our cell surface-capturing (CSC) technology, which covalently labels extracellular glycan moieties on live cells, to the detection and relative quantitative comparison of the cell surface N-glycoproteomes of T and B cells, as well as to monitor changes in the abundance of cell surface N-glycoprotein markers during T-cell activation and the controlled differentiation of embryonic stem cells into the neural lineage.
19349973	3	35	from	changes	880:886	arg1	abundance					895:903	the abundance	891:903	the abundance of cell surface N-glycoprotein markers	891:942	We apply our cell surface-capturing (CSC) technology, which covalently labels extracellular glycan moieties on live cells, to the detection and relative quantitative comparison of the cell surface N-glycoproteomes of T and B cells, as well as to monitor changes in the abundance of cell surface N-glycoprotein markers during T-cell activation and the controlled differentiation of embryonic stem cells into the neural lineage.
19349973	2	36	theme	glycosylation	460:472	arg1	sites					474:478	several hundred N-linked glycosylation sites	435:478	several hundred N-linked glycosylation sites	435:478	We use multiplexed mass-spectrometric identification of several hundred N-linked glycosylation sites specifically from cell surface-exposed glycoproteins to phenotype cells without antibodies in an unbiased fashion and without a priori knowledge.
19349973	1	37	theme	flow	232:235	arg1	cytometry					237:245	flow cytometry	232:245	flow cytometry	232:245	Although the classification of cell types often relies on the identification of cell surface proteins as differentiation markers, flow cytometry requires suitable antibodies and currently permits detection of only up to a dozen differentiation markers in a single measurement.
19349973	4	38	theme	snapshot	1055:1062	arg1	view					1064:1067	A snapshot view	1053:1067	A snapshot view of the cell surface N-glycoproteins	1053:1103	A snapshot view of the cell surface N-glycoproteins will enable detection of panels of N-glycoproteins as potential differentiation markers that are currently not accessible by other means.
19349973	1	39	theme	dozen	324:328	arg1	markers					346:352	a dozen differentiation markers	322:352	a dozen differentiation markers	322:352	Although the classification of cell types often relies on the identification of cell surface proteins as differentiation markers, flow cytometry requires suitable antibodies and currently permits detection of only up to a dozen differentiation markers in a single measurement.
19349973	2	40	theme	priori	608:613	arg1	knowledge					615:623	a priori knowledge	606:623	a priori knowledge	606:623	We use multiplexed mass-spectrometric identification of several hundred N-linked glycosylation sites specifically from cell surface-exposed glycoproteins to phenotype cells without antibodies in an unbiased fashion and without a priori knowledge.
19349973	3	41	theme	extracellular	704:716	arg1	moieties					725:732	extracellular glycan moieties	704:732	extracellular glycan moieties on live cells	704:746	We apply our cell surface-capturing (CSC) technology, which covalently labels extracellular glycan moieties on live cells, to the detection and relative quantitative comparison of the cell surface N-glycoproteomes of T and B cells, as well as to monitor changes in the abundance of cell surface N-glycoprotein markers during T-cell activation and the controlled differentiation of embryonic stem cells into the neural lineage.
19349973	2	42	theme	cell	498:501	arg1	glycoproteins					519:531	cell surface-exposed glycoproteins	498:531	cell surface-exposed glycoproteins	498:531	We use multiplexed mass-spectrometric identification of several hundred N-linked glycosylation sites specifically from cell surface-exposed glycoproteins to phenotype cells without antibodies in an unbiased fashion and without a priori knowledge.
19349973	2	43	theme	N-linked	451:458	arg1	sites					474:478	several hundred N-linked glycosylation sites	435:478	several hundred N-linked glycosylation sites	435:478	We use multiplexed mass-spectrometric identification of several hundred N-linked glycosylation sites specifically from cell surface-exposed glycoproteins to phenotype cells without antibodies in an unbiased fashion and without a priori knowledge.
19349973	0	44	theme	cell	74:77	arg1	glycoproteins					87:99	N-linked cell surface glycoproteins	65:99	N-linked cell surface glycoproteins	65:99	Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.
19349973	1	45	theme	differentiation	330:344	arg1	markers					346:352	a dozen differentiation markers	322:352	a dozen differentiation markers	322:352	Although the classification of cell types often relies on the identification of cell surface proteins as differentiation markers, flow cytometry requires suitable antibodies and currently permits detection of only up to a dozen differentiation markers in a single measurement.
19349973	3	46	theme	glycan	718:723	arg1	moieties					725:732	extracellular glycan moieties	704:732	extracellular glycan moieties on live cells	704:746	We apply our cell surface-capturing (CSC) technology, which covalently labels extracellular glycan moieties on live cells, to the detection and relative quantitative comparison of the cell surface N-glycoproteomes of T and B cells, as well as to monitor changes in the abundance of cell surface N-glycoprotein markers during T-cell activation and the controlled differentiation of embryonic stem cells into the neural lineage.
19349973	4	47	gly	N-glycoproteins	1089:1103	arg1	N-glycoproteins					1089:1103	the cell surface N-glycoproteins	1072:1103	the cell surface N-glycoproteins	1072:1103	A snapshot view of the cell surface N-glycoproteins will enable detection of panels of N-glycoproteins as potential differentiation markers that are currently not accessible by other means.
19349973	1	48	theme	types	138:142	arg1	classification					115:128	the classification	111:128	the classification of cell types	111:142	Although the classification of cell types often relies on the identification of cell surface proteins as differentiation markers, flow cytometry requires suitable antibodies and currently permits detection of only up to a dozen differentiation markers in a single measurement.
19349973	0	49	theme	N-linked	65:72	arg1	glycoproteins					87:99	N-linked cell surface glycoproteins	65:99	N-linked cell surface glycoproteins	65:99	Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.
19349973	3	50	theme	T	843:843	arg1	cells					851:855	T and B cells	843:855	cells	851:855	We apply our cell surface-capturing (CSC) technology, which covalently labels extracellular glycan moieties on live cells, to the detection and relative quantitative comparison of the cell surface N-glycoproteomes of T and B cells, as well as to monitor changes in the abundance of cell surface N-glycoprotein markers during T-cell activation and the controlled differentiation of embryonic stem cells into the neural lineage.
19349973	4	51	gly	N-glycoproteins	1140:1154	arg1	N-glycoproteins					1140:1154	N-glycoproteins	1140:1154	N-glycoproteins	1140:1154	A snapshot view of the cell surface N-glycoproteins will enable detection of panels of N-glycoproteins as potential differentiation markers that are currently not accessible by other means.
19349973	3	52	theme	CSC	663:665	arg1	technology					668:677	our cell surface-capturing (CSC) technology	635:677	our cell surface-capturing (CSC) technology	635:677	We apply our cell surface-capturing (CSC) technology, which covalently labels extracellular glycan moieties on live cells, to the detection and relative quantitative comparison of the cell surface N-glycoproteomes of T and B cells, as well as to monitor changes in the abundance of cell surface N-glycoprotein markers during T-cell activation and the controlled differentiation of embryonic stem cells into the neural lineage.
19349973	3	53	theme	stem	1017:1020	arg1	cells					1022:1026	embryonic stem cells	1007:1026	embryonic stem cells	1007:1026	We apply our cell surface-capturing (CSC) technology, which covalently labels extracellular glycan moieties on live cells, to the detection and relative quantitative comparison of the cell surface N-glycoproteomes of T and B cells, as well as to monitor changes in the abundance of cell surface N-glycoprotein markers during T-cell activation and the controlled differentiation of embryonic stem cells into the neural lineage.
19349973	4	54	theme	N-glycoproteins	1140:1154	arg1	panels					1130:1135	panels	1130:1135	panels of N-glycoproteins	1130:1154	A snapshot view of the cell surface N-glycoproteins will enable detection of panels of N-glycoproteins as potential differentiation markers that are currently not accessible by other means.
19349973	2	55	link	N-linked	451:458	arg1	sites					474:478	several hundred N-linked glycosylation sites	435:478	several hundred N-linked glycosylation sites	435:478	We use multiplexed mass-spectrometric identification of several hundred N-linked glycosylation sites specifically from cell surface-exposed glycoproteins to phenotype cells without antibodies in an unbiased fashion and without a priori knowledge.
19349973	3	56	theme	cells	1022:1026	arg1	differentiation					988:1002	the controlled differentiation	973:1002	the controlled differentiation of embryonic stem cells into the neural lineage	973:1050	We apply our cell surface-capturing (CSC) technology, which covalently labels extracellular glycan moieties on live cells, to the detection and relative quantitative comparison of the cell surface N-glycoproteomes of T and B cells, as well as to monitor changes in the abundance of cell surface N-glycoprotein markers during T-cell activation and the controlled differentiation of embryonic stem cells into the neural lineage.
19349973	3	56	theme	cells	1022:1026	arg1	activation					958:967	T-cell activation	951:967	T-cell activation	951:967	We apply our cell surface-capturing (CSC) technology, which covalently labels extracellular glycan moieties on live cells, to the detection and relative quantitative comparison of the cell surface N-glycoproteomes of T and B cells, as well as to monitor changes in the abundance of cell surface N-glycoprotein markers during T-cell activation and the controlled differentiation of embryonic stem cells into the neural lineage.
19349973	3	57	theme	cell	908:911	arg1	markers					936:942	cell surface N-glycoprotein markers	908:942	cell surface N-glycoprotein markers	908:942	We apply our cell surface-capturing (CSC) technology, which covalently labels extracellular glycan moieties on live cells, to the detection and relative quantitative comparison of the cell surface N-glycoproteomes of T and B cells, as well as to monitor changes in the abundance of cell surface N-glycoprotein markers during T-cell activation and the controlled differentiation of embryonic stem cells into the neural lineage.
19349973	3	58	theme	T-cell	951:956	arg1	activation					958:967	T-cell activation	951:967	T-cell activation	951:967	We apply our cell surface-capturing (CSC) technology, which covalently labels extracellular glycan moieties on live cells, to the detection and relative quantitative comparison of the cell surface N-glycoproteomes of T and B cells, as well as to monitor changes in the abundance of cell surface N-glycoprotein markers during T-cell activation and the controlled differentiation of embryonic stem cells into the neural lineage.
19349973	3	59	theme	live	737:740	arg1	cells					742:746	live cells	737:746	live cells	737:746	We apply our cell surface-capturing (CSC) technology, which covalently labels extracellular glycan moieties on live cells, to the detection and relative quantitative comparison of the cell surface N-glycoproteomes of T and B cells, as well as to monitor changes in the abundance of cell surface N-glycoprotein markers during T-cell activation and the controlled differentiation of embryonic stem cells into the neural lineage.
19349973	2	60	gly	glycoproteins	519:531	arg1	glycoproteins					519:531	cell surface-exposed glycoproteins	498:531	cell surface-exposed glycoproteins	498:531	We use multiplexed mass-spectrometric identification of several hundred N-linked glycosylation sites specifically from cell surface-exposed glycoproteins to phenotype cells without antibodies in an unbiased fashion and without a priori knowledge.
19349973	4	61	theme	differentiation	1169:1183	arg1	markers					1185:1191	potential differentiation markers	1159:1191	potential differentiation markers that are currently not accessible by other means	1159:1240	A snapshot view of the cell surface N-glycoproteins will enable detection of panels of N-glycoproteins as potential differentiation markers that are currently not accessible by other means.
19349973	4	61	theme	differentiation	1169:1183	arg1	detection					1117:1125	detection	1117:1125	detection of panels of N-glycoproteins	1117:1154	A snapshot view of the cell surface N-glycoproteins will enable detection of panels of N-glycoproteins as potential differentiation markers that are currently not accessible by other means.
19349973	4	62	theme	potential	1159:1167	arg1	markers					1185:1191	potential differentiation markers	1159:1191	potential differentiation markers that are currently not accessible by other means	1159:1240	A snapshot view of the cell surface N-glycoproteins will enable detection of panels of N-glycoproteins as potential differentiation markers that are currently not accessible by other means.
19349973	4	62	theme	potential	1159:1167	arg1	detection					1117:1125	detection	1117:1125	detection of panels of N-glycoproteins	1117:1154	A snapshot view of the cell surface N-glycoproteins will enable detection of panels of N-glycoproteins as potential differentiation markers that are currently not accessible by other means.
19349973	1	63	theme	suitable	256:263	arg1	antibodies					265:274	suitable antibodies	256:274	suitable antibodies	256:274	Although the classification of cell types often relies on the identification of cell surface proteins as differentiation markers, flow cytometry requires suitable antibodies and currently permits detection of only up to a dozen differentiation markers in a single measurement.
19349973	0	64	theme	glycoproteins	87:99	arg1	identification					19:32	Mass-spectrometric identification	0:32	Mass-spectrometric identification	0:32	Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.
19349973	0	64	theme	glycoproteins	87:99	arg1	quantification					47:60	relative quantification	38:60	relative quantification	38:60	Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.
19349973	4	65	theme	panels	1130:1135	arg1	detection					1117:1125	detection	1117:1125	detection of panels of N-glycoproteins	1117:1154	A snapshot view of the cell surface N-glycoproteins will enable detection of panels of N-glycoproteins as potential differentiation markers that are currently not accessible by other means.
19349973	4	65	theme	panels	1130:1135	arg1	markers					1185:1191	potential differentiation markers	1159:1191	potential differentiation markers that are currently not accessible by other means	1159:1240	A snapshot view of the cell surface N-glycoproteins will enable detection of panels of N-glycoproteins as potential differentiation markers that are currently not accessible by other means.
19349973	4	66	theme	other	1230:1234	arg1	means					1236:1240	other means	1230:1240	other means	1230:1240	A snapshot view of the cell surface N-glycoproteins will enable detection of panels of N-glycoproteins as potential differentiation markers that are currently not accessible by other means.
19349973	2	67	theme	mass-spectrometric	398:415	arg1	identification					417:430	multiplexed mass-spectrometric identification	386:430	multiplexed mass-spectrometric identification of several hundred N-linked glycosylation sites	386:478	We use multiplexed mass-spectrometric identification of several hundred N-linked glycosylation sites specifically from cell surface-exposed glycoproteins to phenotype cells without antibodies in an unbiased fashion and without a priori knowledge.
19349973	2	68	theme	several	435:441	arg1	sites					474:478	several hundred N-linked glycosylation sites	435:478	several hundred N-linked glycosylation sites	435:478	We use multiplexed mass-spectrometric identification of several hundred N-linked glycosylation sites specifically from cell surface-exposed glycoproteins to phenotype cells without antibodies in an unbiased fashion and without a priori knowledge.
19349973	0	69	theme	surface	79:85	arg1	glycoproteins					87:99	N-linked cell surface glycoproteins	65:99	N-linked cell surface glycoproteins	65:99	Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.
19349973	3	70	theme	neural	1037:1042	arg1	lineage					1044:1050	the neural lineage	1033:1050	the neural lineage	1033:1050	We apply our cell surface-capturing (CSC) technology, which covalently labels extracellular glycan moieties on live cells, to the detection and relative quantitative comparison of the cell surface N-glycoproteomes of T and B cells, as well as to monitor changes in the abundance of cell surface N-glycoprotein markers during T-cell activation and the controlled differentiation of embryonic stem cells into the neural lineage.
19349973	2	71	theme	multiplexed	386:396	arg1	identification					417:430	multiplexed mass-spectrometric identification	386:430	multiplexed mass-spectrometric identification of several hundred N-linked glycosylation sites	386:478	We use multiplexed mass-spectrometric identification of several hundred N-linked glycosylation sites specifically from cell surface-exposed glycoproteins to phenotype cells without antibodies in an unbiased fashion and without a priori knowledge.
19349973	3	72	theme	markers	936:942	arg1	abundance					895:903	the abundance	891:903	the abundance of cell surface N-glycoprotein markers	891:942	We apply our cell surface-capturing (CSC) technology, which covalently labels extracellular glycan moieties on live cells, to the detection and relative quantitative comparison of the cell surface N-glycoproteomes of T and B cells, as well as to monitor changes in the abundance of cell surface N-glycoprotein markers during T-cell activation and the controlled differentiation of embryonic stem cells into the neural lineage.
19349973	3	73	theme	cells	851:855	arg1	N-glycoproteomes					823:838	the cell surface N-glycoproteomes	806:838	the cell surface N-glycoproteomes of T and B cells	806:855	We apply our cell surface-capturing (CSC) technology, which covalently labels extracellular glycan moieties on live cells, to the detection and relative quantitative comparison of the cell surface N-glycoproteomes of T and B cells, as well as to monitor changes in the abundance of cell surface N-glycoprotein markers during T-cell activation and the controlled differentiation of embryonic stem cells into the neural lineage.
8051056	4	0	theme	85-kDa	696:701	arg1	molecule					686:693	the conventional M-CSF molecule	663:693	the conventional M-CSF molecule (85-kDa M-CSF)	663:708	The 150-200-kDa subunit carries a chondroitin sulfate chain, and its amino-terminal amino acid sequence was identical to that of the 43-kDa subunit, which is known to form the conventional M-CSF molecule (85-kDa M-CSF).
8051056	4	0	theme	85-kDa	696:701	arg1	M-CSF					703:707	85-kDa M-CSF	696:707	85-kDa M-CSF	696:707	The 150-200-kDa subunit carries a chondroitin sulfate chain, and its amino-terminal amino acid sequence was identical to that of the 43-kDa subunit, which is known to form the conventional M-CSF molecule (85-kDa M-CSF).
8051056	3	1	contain	contained	349:357	arg2	form					437:440	a heterodimeric form	421:440	a heterodimeric form of a 43-kDa subunit and the 150-200-kDa subunit	421:488	PG-M-CSF contained two types of molecules, a homodimeric 150-200-kDa subunit and a heterodimeric form of a 43-kDa subunit and the 150-200-kDa subunit.
8051056	3	1	contain	contained	349:357	arg2	subunit					409:415	a homodimeric 150-200-kDa subunit	383:415	a homodimeric 150-200-kDa subunit	383:415	PG-M-CSF contained two types of molecules, a homodimeric 150-200-kDa subunit and a heterodimeric form of a 43-kDa subunit and the 150-200-kDa subunit.
8051056	3	1	contain	contained	349:357	arg1	PG-M-CSF					340:347	PG-M-CSF	340:347	PG-M-CSF	340:347	PG-M-CSF contained two types of molecules, a homodimeric 150-200-kDa subunit and a heterodimeric form of a 43-kDa subunit and the 150-200-kDa subunit.
8051056	3	1	contain	contained	349:357	arg2	types					363:367	two types	359:367	two types of molecules	359:380	PG-M-CSF contained two types of molecules, a homodimeric 150-200-kDa subunit and a heterodimeric form of a 43-kDa subunit and the 150-200-kDa subunit.
8051056	4	2	contain	carries	515:521	arg2	chain					545:549	a chondroitin sulfate chain	523:549	a chondroitin sulfate chain	523:549	The 150-200-kDa subunit carries a chondroitin sulfate chain, and its amino-terminal amino acid sequence was identical to that of the 43-kDa subunit, which is known to form the conventional M-CSF molecule (85-kDa M-CSF).
8051056	4	2	contain	carries	515:521	arg1	subunit					507:513	The 150-200-kDa subunit	491:513	The 150-200-kDa subunit	491:513	The 150-200-kDa subunit carries a chondroitin sulfate chain, and its amino-terminal amino acid sequence was identical to that of the 43-kDa subunit, which is known to form the conventional M-CSF molecule (85-kDa M-CSF).
8051056	7	3	theme	mutation	1230:1237	arg1	analysis					1239:1246	Truncated mutation analysis	1220:1246	Truncated mutation analysis	1220:1246	Truncated mutation analysis showed that the carboxyl terminus of the 150-200-kDa subunit lay downstream of Arg412.
8051056	4	4	theme	sulfate	537:543	arg1	chain					545:549	a chondroitin sulfate chain	523:549	a chondroitin sulfate chain	523:549	The 150-200-kDa subunit carries a chondroitin sulfate chain, and its amino-terminal amino acid sequence was identical to that of the 43-kDa subunit, which is known to form the conventional M-CSF molecule (85-kDa M-CSF).
8051056	6	5	theme	43-kDa	1079:1084	arg1	subunit					1086:1092	the 43-kDa subunit	1075:1092	the 43-kDa subunit	1075:1092	The expression of mutagenized cDNA, in which Arg220 was replaced by an alanine residue, resulted in the disappearance of the 43-kDa subunit but not that of the 150-200-kDa subunit, indicating that Arg220-Pro-Pro-Arg is essential to process PG-M-CSF to 85-kDa M-CSF.
8051056	3	6	theme	molecules	372:380	arg1	subunit					409:415	a homodimeric 150-200-kDa subunit	383:415	a homodimeric 150-200-kDa subunit	383:415	PG-M-CSF contained two types of molecules, a homodimeric 150-200-kDa subunit and a heterodimeric form of a 43-kDa subunit and the 150-200-kDa subunit.
8051056	3	6	theme	molecules	372:380	arg1	types					363:367	two types	359:367	two types of molecules	359:380	PG-M-CSF contained two types of molecules, a homodimeric 150-200-kDa subunit and a heterodimeric form of a 43-kDa subunit and the 150-200-kDa subunit.
8051056	3	6	theme	molecules	372:380	arg1	form					437:440	a heterodimeric form	421:440	a heterodimeric form of a 43-kDa subunit and the 150-200-kDa subunit	421:488	PG-M-CSF contained two types of molecules, a homodimeric 150-200-kDa subunit and a heterodimeric form of a 43-kDa subunit and the 150-200-kDa subunit.
8051056	4	7	theme	chondroitin	525:535	arg1	chain					545:549	a chondroitin sulfate chain	523:549	a chondroitin sulfate chain	523:549	The 150-200-kDa subunit carries a chondroitin sulfate chain, and its amino-terminal amino acid sequence was identical to that of the 43-kDa subunit, which is known to form the conventional M-CSF molecule (85-kDa M-CSF).
8051056	1	8	theme	Proteoglycan	74:85	arg1	PG-M-CSF					125:132	PG-M-CSF	125:132	PG-M-CSF	125:132	Proteoglycan macrophage colony-stimulating factor (PG-M-CSF) was recently reported as a high molecular type of macrophage colony-stimulating factor (M-CSF).
8051056	1	8	theme	Proteoglycan	74:85	arg1	factor					117:122	Proteoglycan macrophage colony-stimulating factor	74:122	Proteoglycan macrophage colony-stimulating factor (PG-M-CSF)	74:133	Proteoglycan macrophage colony-stimulating factor (PG-M-CSF) was recently reported as a high molecular type of macrophage colony-stimulating factor (M-CSF).
8051056	1	8	theme	Proteoglycan	74:85	arg1	type					177:180	a high molecular type	160:180	a high molecular type of macrophage colony-stimulating factor (M-CSF)	160:228	Proteoglycan macrophage colony-stimulating factor (PG-M-CSF) was recently reported as a high molecular type of macrophage colony-stimulating factor (M-CSF).
8051056	8	9	theme	binding	1379:1385	arg1	Ser277					1423:1428	Ser277	1423:1428	Ser277	1423:1428	We also showed that the chondroitin sulfate binding site in the 150-200-kDa subunit was Ser277, since conversion of Ser277 to the alanine residue resulted in complete loss of the chondroitin sulfate substitution.
8051056	8	9	theme	binding	1379:1385	arg1	site					1387:1390	the chondroitin sulfate binding site	1355:1390	the chondroitin sulfate binding site in the 150-200-kDa subunit	1355:1417	We also showed that the chondroitin sulfate binding site in the 150-200-kDa subunit was Ser277, since conversion of Ser277 to the alanine residue resulted in complete loss of the chondroitin sulfate substitution.
8051056	6	10	theme	cDNA	984:987	arg1	expression					958:967	The expression	954:967	The expression	954:967	The expression of mutagenized cDNA, in which Arg220 was replaced by an alanine residue, resulted in the disappearance of the 43-kDa subunit but not that of the 150-200-kDa subunit, indicating that Arg220-Pro-Pro-Arg is essential to process PG-M-CSF to 85-kDa M-CSF.
8051056	8	11	theme	chondroitin	1514:1524	arg1	sulfate					1526:1532	the chondroitin sulfate substitution	1510:1545	the chondroitin sulfate substitution	1510:1545	We also showed that the chondroitin sulfate binding site in the 150-200-kDa subunit was Ser277, since conversion of Ser277 to the alanine residue resulted in complete loss of the chondroitin sulfate substitution.
8051056	1	12	theme	macrophage	87:96	arg1	PG-M-CSF					125:132	PG-M-CSF	125:132	PG-M-CSF	125:132	Proteoglycan macrophage colony-stimulating factor (PG-M-CSF) was recently reported as a high molecular type of macrophage colony-stimulating factor (M-CSF).
8051056	1	12	theme	macrophage	87:96	arg1	factor					117:122	Proteoglycan macrophage colony-stimulating factor	74:122	Proteoglycan macrophage colony-stimulating factor (PG-M-CSF)	74:133	Proteoglycan macrophage colony-stimulating factor (PG-M-CSF) was recently reported as a high molecular type of macrophage colony-stimulating factor (M-CSF).
8051056	1	12	theme	macrophage	87:96	arg1	type					177:180	a high molecular type	160:180	a high molecular type of macrophage colony-stimulating factor (M-CSF)	160:228	Proteoglycan macrophage colony-stimulating factor (PG-M-CSF) was recently reported as a high molecular type of macrophage colony-stimulating factor (M-CSF).
8051056	2	13	theme	cDNA	303:306	arg1	expression					276:285	the expression	272:285	the expression of mutant M-CSF cDNA in Chinese hamster ovary cells	272:337	We analyzed its structure by determining the expression of mutant M-CSF cDNA in Chinese hamster ovary cells.
8051056	5	14	theme	sequence	863:870	arg1	part					841:844	a large part	833:844	a large part of the precursor sequence	833:870	The results obtained with the carboxyl-terminal deleted mutants showed that the PG-M-CSF-specific 150-200-kDa subunit had a large part of the precursor sequence at its carboxyl terminus removed in the 43-kDa subunit by proteolytic processing.
8051056	6	15	theme	150-200-kDa	1114:1124	arg1	subunit					1126:1132	the 150-200-kDa subunit	1110:1132	the 150-200-kDa subunit	1110:1132	The expression of mutagenized cDNA, in which Arg220 was replaced by an alanine residue, resulted in the disappearance of the 43-kDa subunit but not that of the 150-200-kDa subunit, indicating that Arg220-Pro-Pro-Arg is essential to process PG-M-CSF to 85-kDa M-CSF.
8051056	6	16	theme	subunit	1086:1092	arg1	disappearance					1058:1070	the disappearance	1054:1070	the disappearance of the 43-kDa subunit but not that of the 150-200-kDa subunit	1054:1132	The expression of mutagenized cDNA, in which Arg220 was replaced by an alanine residue, resulted in the disappearance of the 43-kDa subunit but not that of the 150-200-kDa subunit, indicating that Arg220-Pro-Pro-Arg is essential to process PG-M-CSF to 85-kDa M-CSF.
8051056	1	17	theme	colony-stimulating	98:115	arg1	PG-M-CSF					125:132	PG-M-CSF	125:132	PG-M-CSF	125:132	Proteoglycan macrophage colony-stimulating factor (PG-M-CSF) was recently reported as a high molecular type of macrophage colony-stimulating factor (M-CSF).
8051056	1	17	theme	colony-stimulating	98:115	arg1	factor					117:122	Proteoglycan macrophage colony-stimulating factor	74:122	Proteoglycan macrophage colony-stimulating factor (PG-M-CSF)	74:133	Proteoglycan macrophage colony-stimulating factor (PG-M-CSF) was recently reported as a high molecular type of macrophage colony-stimulating factor (M-CSF).
8051056	1	17	theme	colony-stimulating	98:115	arg1	type					177:180	a high molecular type	160:180	a high molecular type of macrophage colony-stimulating factor (M-CSF)	160:228	Proteoglycan macrophage colony-stimulating factor (PG-M-CSF) was recently reported as a high molecular type of macrophage colony-stimulating factor (M-CSF).
8051056	4	18	theme	conventional	667:678	arg1	molecule					686:693	the conventional M-CSF molecule	663:693	the conventional M-CSF molecule (85-kDa M-CSF)	663:708	The 150-200-kDa subunit carries a chondroitin sulfate chain, and its amino-terminal amino acid sequence was identical to that of the 43-kDa subunit, which is known to form the conventional M-CSF molecule (85-kDa M-CSF).
8051056	4	18	theme	conventional	667:678	arg1	M-CSF					703:707	85-kDa M-CSF	696:707	85-kDa M-CSF	696:707	The 150-200-kDa subunit carries a chondroitin sulfate chain, and its amino-terminal amino acid sequence was identical to that of the 43-kDa subunit, which is known to form the conventional M-CSF molecule (85-kDa M-CSF).
8051056	1	19	theme	macrophage	185:194	arg1	factor					215:220	macrophage colony-stimulating factor	185:220	macrophage colony-stimulating factor (M-CSF)	185:228	Proteoglycan macrophage colony-stimulating factor (PG-M-CSF) was recently reported as a high molecular type of macrophage colony-stimulating factor (M-CSF).
8051056	1	19	theme	macrophage	185:194	arg1	M-CSF					223:227	M-CSF	223:227	M-CSF	223:227	Proteoglycan macrophage colony-stimulating factor (PG-M-CSF) was recently reported as a high molecular type of macrophage colony-stimulating factor (M-CSF).
8051056	5	20	theme	150-200-kDa	809:819	arg1	subunit					821:827	the PG-M-CSF-specific 150-200-kDa subunit	787:827	the PG-M-CSF-specific 150-200-kDa subunit	787:827	The results obtained with the carboxyl-terminal deleted mutants showed that the PG-M-CSF-specific 150-200-kDa subunit had a large part of the precursor sequence at its carboxyl terminus removed in the 43-kDa subunit by proteolytic processing.
8051056	3	21	theme	heterodimeric	423:435	arg1	types					363:367	two types	359:367	two types of molecules	359:380	PG-M-CSF contained two types of molecules, a homodimeric 150-200-kDa subunit and a heterodimeric form of a 43-kDa subunit and the 150-200-kDa subunit.
8051056	3	21	theme	heterodimeric	423:435	arg1	form					437:440	a heterodimeric form	421:440	a heterodimeric form of a 43-kDa subunit and the 150-200-kDa subunit	421:488	PG-M-CSF contained two types of molecules, a homodimeric 150-200-kDa subunit and a heterodimeric form of a 43-kDa subunit and the 150-200-kDa subunit.
8051056	2	22	theme	mutant	290:295	arg1	cDNA					303:306	mutant M-CSF cDNA	290:306	mutant M-CSF cDNA	290:306	We analyzed its structure by determining the expression of mutant M-CSF cDNA in Chinese hamster ovary cells.
8051056	1	23	theme	colony-stimulating	196:213	arg1	factor					215:220	macrophage colony-stimulating factor	185:220	macrophage colony-stimulating factor (M-CSF)	185:228	Proteoglycan macrophage colony-stimulating factor (PG-M-CSF) was recently reported as a high molecular type of macrophage colony-stimulating factor (M-CSF).
8051056	1	23	theme	colony-stimulating	196:213	arg1	M-CSF					223:227	M-CSF	223:227	M-CSF	223:227	Proteoglycan macrophage colony-stimulating factor (PG-M-CSF) was recently reported as a high molecular type of macrophage colony-stimulating factor (M-CSF).
8051056	3	24	theme	150-200-kDa	397:407	arg1	subunit					409:415	a homodimeric 150-200-kDa subunit	383:415	a homodimeric 150-200-kDa subunit	383:415	PG-M-CSF contained two types of molecules, a homodimeric 150-200-kDa subunit and a heterodimeric form of a 43-kDa subunit and the 150-200-kDa subunit.
8051056	3	24	theme	150-200-kDa	397:407	arg1	types					363:367	two types	359:367	two types of molecules	359:380	PG-M-CSF contained two types of molecules, a homodimeric 150-200-kDa subunit and a heterodimeric form of a 43-kDa subunit and the 150-200-kDa subunit.
8051056	4	25	theme	150-200-kDa	495:505	arg1	subunit					507:513	The 150-200-kDa subunit	491:513	The 150-200-kDa subunit	491:513	The 150-200-kDa subunit carries a chondroitin sulfate chain, and its amino-terminal amino acid sequence was identical to that of the 43-kDa subunit, which is known to form the conventional M-CSF molecule (85-kDa M-CSF).
8051056	7	26	theme	Truncated	1220:1228	arg1	analysis					1239:1246	Truncated mutation analysis	1220:1246	Truncated mutation analysis	1220:1246	Truncated mutation analysis showed that the carboxyl terminus of the 150-200-kDa subunit lay downstream of Arg412.
8051056	8	27	theme	sulfate	1371:1377	arg1	Ser277					1423:1428	Ser277	1423:1428	Ser277	1423:1428	We also showed that the chondroitin sulfate binding site in the 150-200-kDa subunit was Ser277, since conversion of Ser277 to the alanine residue resulted in complete loss of the chondroitin sulfate substitution.
8051056	8	27	theme	sulfate	1371:1377	arg1	site					1387:1390	the chondroitin sulfate binding site	1355:1390	the chondroitin sulfate binding site in the 150-200-kDa subunit	1355:1417	We also showed that the chondroitin sulfate binding site in the 150-200-kDa subunit was Ser277, since conversion of Ser277 to the alanine residue resulted in complete loss of the chondroitin sulfate substitution.
8051056	1	28	theme	factor	215:220	arg1	factor					117:122	Proteoglycan macrophage colony-stimulating factor	74:122	Proteoglycan macrophage colony-stimulating factor (PG-M-CSF)	74:133	Proteoglycan macrophage colony-stimulating factor (PG-M-CSF) was recently reported as a high molecular type of macrophage colony-stimulating factor (M-CSF).
8051056	1	28	theme	factor	215:220	arg1	type					177:180	a high molecular type	160:180	a high molecular type of macrophage colony-stimulating factor (M-CSF)	160:228	Proteoglycan macrophage colony-stimulating factor (PG-M-CSF) was recently reported as a high molecular type of macrophage colony-stimulating factor (M-CSF).
8051056	0	29	theme	Structural	0:9	arg1	analysis					11:18	Structural analysis	0:18	Structural analysis of proteoglycan macrophage colony-stimulating factor	0:71	Structural analysis of proteoglycan macrophage colony-stimulating factor.
8051056	4	30	theme	amino	575:579	arg1	sequence					586:593	its amino-terminal amino acid sequence	556:593	its amino-terminal amino acid sequence	556:593	The 150-200-kDa subunit carries a chondroitin sulfate chain, and its amino-terminal amino acid sequence was identical to that of the 43-kDa subunit, which is known to form the conventional M-CSF molecule (85-kDa M-CSF).
8051056	2	31	theme	ovary	327:331	arg1	cells					333:337	Chinese hamster ovary cells	311:337	Chinese hamster ovary cells	311:337	We analyzed its structure by determining the expression of mutant M-CSF cDNA in Chinese hamster ovary cells.
8051056	5	32	theme	carboxyl	879:886	arg1	terminus					888:895	its carboxyl terminus	875:895	its carboxyl terminus removed in the 43-kDa subunit by proteolytic processing	875:951	The results obtained with the carboxyl-terminal deleted mutants showed that the PG-M-CSF-specific 150-200-kDa subunit had a large part of the precursor sequence at its carboxyl terminus removed in the 43-kDa subunit by proteolytic processing.
8051056	0	33	theme	proteoglycan	23:34	arg1	factor					66:71	proteoglycan macrophage colony-stimulating factor	23:71	proteoglycan macrophage colony-stimulating factor	23:71	Structural analysis of proteoglycan macrophage colony-stimulating factor.
8051056	4	34	theme	amino-terminal	560:573	arg1	sequence					586:593	its amino-terminal amino acid sequence	556:593	its amino-terminal amino acid sequence	556:593	The 150-200-kDa subunit carries a chondroitin sulfate chain, and its amino-terminal amino acid sequence was identical to that of the 43-kDa subunit, which is known to form the conventional M-CSF molecule (85-kDa M-CSF).
8051056	8	35	theme	Ser277	1451:1456	arg1	conversion					1437:1446	conversion	1437:1446	conversion of Ser277 to the alanine residue	1437:1479	We also showed that the chondroitin sulfate binding site in the 150-200-kDa subunit was Ser277, since conversion of Ser277 to the alanine residue resulted in complete loss of the chondroitin sulfate substitution.
8051056	5	36	theme	proteolytic	930:940	arg1	processing					942:951	proteolytic processing	930:951	proteolytic processing	930:951	The results obtained with the carboxyl-terminal deleted mutants showed that the PG-M-CSF-specific 150-200-kDa subunit had a large part of the precursor sequence at its carboxyl terminus removed in the 43-kDa subunit by proteolytic processing.
8051056	2	37	theme	hamster	319:325	arg1	cells					333:337	Chinese hamster ovary cells	311:337	Chinese hamster ovary cells	311:337	We analyzed its structure by determining the expression of mutant M-CSF cDNA in Chinese hamster ovary cells.
8051056	3	38	theme	150-200-kDa	470:480	arg1	subunit					482:488	the 150-200-kDa subunit	466:488	the 150-200-kDa subunit	466:488	PG-M-CSF contained two types of molecules, a homodimeric 150-200-kDa subunit and a heterodimeric form of a 43-kDa subunit and the 150-200-kDa subunit.
8051056	3	39	theme	homodimeric	385:395	arg1	subunit					409:415	a homodimeric 150-200-kDa subunit	383:415	a homodimeric 150-200-kDa subunit	383:415	PG-M-CSF contained two types of molecules, a homodimeric 150-200-kDa subunit and a heterodimeric form of a 43-kDa subunit and the 150-200-kDa subunit.
8051056	3	39	theme	homodimeric	385:395	arg1	types					363:367	two types	359:367	two types of molecules	359:380	PG-M-CSF contained two types of molecules, a homodimeric 150-200-kDa subunit and a heterodimeric form of a 43-kDa subunit and the 150-200-kDa subunit.
8051056	6	40	theme	mutagenized	972:982	arg1	cDNA					984:987	mutagenized cDNA	972:987	mutagenized cDNA	972:987	The expression of mutagenized cDNA, in which Arg220 was replaced by an alanine residue, resulted in the disappearance of the 43-kDa subunit but not that of the 150-200-kDa subunit, indicating that Arg220-Pro-Pro-Arg is essential to process PG-M-CSF to 85-kDa M-CSF.
8051056	2	41	theme	M-CSF	297:301	arg1	cDNA					303:306	mutant M-CSF cDNA	290:306	mutant M-CSF cDNA	290:306	We analyzed its structure by determining the expression of mutant M-CSF cDNA in Chinese hamster ovary cells.
8051056	2	42	theme	Chinese	311:317	arg1	cells					333:337	Chinese hamster ovary cells	311:337	Chinese hamster ovary cells	311:337	We analyzed its structure by determining the expression of mutant M-CSF cDNA in Chinese hamster ovary cells.
8051056	3	43	theme	subunit	482:488	arg1	subunit					409:415	a homodimeric 150-200-kDa subunit	383:415	a homodimeric 150-200-kDa subunit	383:415	PG-M-CSF contained two types of molecules, a homodimeric 150-200-kDa subunit and a heterodimeric form of a 43-kDa subunit and the 150-200-kDa subunit.
8051056	3	43	theme	subunit	482:488	arg1	types					363:367	two types	359:367	two types of molecules	359:380	PG-M-CSF contained two types of molecules, a homodimeric 150-200-kDa subunit and a heterodimeric form of a 43-kDa subunit and the 150-200-kDa subunit.
8051056	3	43	theme	subunit	482:488	arg1	form					437:440	a heterodimeric form	421:440	a heterodimeric form of a 43-kDa subunit and the 150-200-kDa subunit	421:488	PG-M-CSF contained two types of molecules, a homodimeric 150-200-kDa subunit and a heterodimeric form of a 43-kDa subunit and the 150-200-kDa subunit.
8051056	0	44	theme	colony-stimulating	47:64	arg1	factor					66:71	proteoglycan macrophage colony-stimulating factor	23:71	proteoglycan macrophage colony-stimulating factor	23:71	Structural analysis of proteoglycan macrophage colony-stimulating factor.
8051056	4	45	theme	acid	581:584	arg1	sequence					586:593	its amino-terminal amino acid sequence	556:593	its amino-terminal amino acid sequence	556:593	The 150-200-kDa subunit carries a chondroitin sulfate chain, and its amino-terminal amino acid sequence was identical to that of the 43-kDa subunit, which is known to form the conventional M-CSF molecule (85-kDa M-CSF).
8051056	2	46	from	expression	276:285	arg1	cells					333:337	Chinese hamster ovary cells	311:337	Chinese hamster ovary cells	311:337	We analyzed its structure by determining the expression of mutant M-CSF cDNA in Chinese hamster ovary cells.
8051056	7	47	theme	150-200-kDa	1289:1299	arg1	subunit					1301:1307	the 150-200-kDa subunit	1285:1307	the 150-200-kDa subunit	1285:1307	Truncated mutation analysis showed that the carboxyl terminus of the 150-200-kDa subunit lay downstream of Arg412.
8051056	0	48	theme	macrophage	36:45	arg1	factor					66:71	proteoglycan macrophage colony-stimulating factor	23:71	proteoglycan macrophage colony-stimulating factor	23:71	Structural analysis of proteoglycan macrophage colony-stimulating factor.
8051056	5	49	contain	had	829:831	arg2	part					841:844	a large part	833:844	a large part of the precursor sequence	833:870	The results obtained with the carboxyl-terminal deleted mutants showed that the PG-M-CSF-specific 150-200-kDa subunit had a large part of the precursor sequence at its carboxyl terminus removed in the 43-kDa subunit by proteolytic processing.
8051056	5	49	contain	had	829:831	arg1	subunit					821:827	the PG-M-CSF-specific 150-200-kDa subunit	787:827	the PG-M-CSF-specific 150-200-kDa subunit	787:827	The results obtained with the carboxyl-terminal deleted mutants showed that the PG-M-CSF-specific 150-200-kDa subunit had a large part of the precursor sequence at its carboxyl terminus removed in the 43-kDa subunit by proteolytic processing.
8051056	5	50	theme	precursor	853:861	arg1	sequence					863:870	the precursor sequence	849:870	the precursor sequence	849:870	The results obtained with the carboxyl-terminal deleted mutants showed that the PG-M-CSF-specific 150-200-kDa subunit had a large part of the precursor sequence at its carboxyl terminus removed in the 43-kDa subunit by proteolytic processing.
8051056	5	51	theme	PG-M-CSF-specific	791:807	arg1	subunit					821:827	the PG-M-CSF-specific 150-200-kDa subunit	787:827	the PG-M-CSF-specific 150-200-kDa subunit	787:827	The results obtained with the carboxyl-terminal deleted mutants showed that the PG-M-CSF-specific 150-200-kDa subunit had a large part of the precursor sequence at its carboxyl terminus removed in the 43-kDa subunit by proteolytic processing.
8051056	3	52	theme	43-kDa	447:452	arg1	subunit					454:460	a 43-kDa subunit	445:460	a 43-kDa subunit	445:460	PG-M-CSF contained two types of molecules, a homodimeric 150-200-kDa subunit and a heterodimeric form of a 43-kDa subunit and the 150-200-kDa subunit.
8051056	8	53	theme	chondroitin	1359:1369	arg1	sulfate					1371:1377	chondroitin sulfate	1359:1377	the chondroitin sulfate binding site in the 150-200-kDa subunit	1355:1417	We also showed that the chondroitin sulfate binding site in the 150-200-kDa subunit was Ser277, since conversion of Ser277 to the alanine residue resulted in complete loss of the chondroitin sulfate substitution.
8051056	5	54	theme	43-kDa	912:917	arg1	subunit					919:925	the 43-kDa subunit	908:925	the 43-kDa subunit	908:925	The results obtained with the carboxyl-terminal deleted mutants showed that the PG-M-CSF-specific 150-200-kDa subunit had a large part of the precursor sequence at its carboxyl terminus removed in the 43-kDa subunit by proteolytic processing.
8051056	0	55	theme	factor	66:71	arg1	analysis					11:18	Structural analysis	0:18	Structural analysis of proteoglycan macrophage colony-stimulating factor	0:71	Structural analysis of proteoglycan macrophage colony-stimulating factor.
8051056	7	56	theme	Arg412	1327:1332	arg1	downstream					1313:1322	downstream	1313:1322	downstream	1313:1322	Truncated mutation analysis showed that the carboxyl terminus of the 150-200-kDa subunit lay downstream of Arg412.
8051056	8	57	theme	alanine	1465:1471	arg1	residue					1473:1479	the alanine residue	1461:1479	the alanine residue	1461:1479	We also showed that the chondroitin sulfate binding site in the 150-200-kDa subunit was Ser277, since conversion of Ser277 to the alanine residue resulted in complete loss of the chondroitin sulfate substitution.
8051056	8	58	theme	150-200-kDa	1399:1409	arg1	subunit					1411:1417	the 150-200-kDa subunit	1395:1417	the 150-200-kDa subunit	1395:1417	We also showed that the chondroitin sulfate binding site in the 150-200-kDa subunit was Ser277, since conversion of Ser277 to the alanine residue resulted in complete loss of the chondroitin sulfate substitution.
8051056	6	59	theme	85-kDa	1206:1211	arg1	M-CSF					1213:1217	85-kDa M-CSF	1206:1217	85-kDa M-CSF	1206:1217	The expression of mutagenized cDNA, in which Arg220 was replaced by an alanine residue, resulted in the disappearance of the 43-kDa subunit but not that of the 150-200-kDa subunit, indicating that Arg220-Pro-Pro-Arg is essential to process PG-M-CSF to 85-kDa M-CSF.
8051056	7	60	theme	carboxyl	1264:1271	arg1	terminus					1273:1280	the carboxyl terminus	1260:1280	the carboxyl terminus of the 150-200-kDa subunit	1260:1307	Truncated mutation analysis showed that the carboxyl terminus of the 150-200-kDa subunit lay downstream of Arg412.
8051056	6	61	theme	alanine	1025:1031	arg1	residue					1033:1039	an alanine residue	1022:1039	an alanine residue	1022:1039	The expression of mutagenized cDNA, in which Arg220 was replaced by an alanine residue, resulted in the disappearance of the 43-kDa subunit but not that of the 150-200-kDa subunit, indicating that Arg220-Pro-Pro-Arg is essential to process PG-M-CSF to 85-kDa M-CSF.
8051056	4	62	theme	M-CSF	680:684	arg1	molecule					686:693	the conventional M-CSF molecule	663:693	the conventional M-CSF molecule (85-kDa M-CSF)	663:708	The 150-200-kDa subunit carries a chondroitin sulfate chain, and its amino-terminal amino acid sequence was identical to that of the 43-kDa subunit, which is known to form the conventional M-CSF molecule (85-kDa M-CSF).
8051056	4	62	theme	M-CSF	680:684	arg1	M-CSF					703:707	85-kDa M-CSF	696:707	85-kDa M-CSF	696:707	The 150-200-kDa subunit carries a chondroitin sulfate chain, and its amino-terminal amino acid sequence was identical to that of the 43-kDa subunit, which is known to form the conventional M-CSF molecule (85-kDa M-CSF).
8051056	8	63	dep	sulfate	1526:1532	arg1	substitution					1534:1545	substitution	1534:1545	the chondroitin sulfate substitution	1510:1545	We also showed that the chondroitin sulfate binding site in the 150-200-kDa subunit was Ser277, since conversion of Ser277 to the alanine residue resulted in complete loss of the chondroitin sulfate substitution.
8051056	5	64	theme	carboxyl-terminal	741:757	arg1	mutants					767:773	the carboxyl-terminal deleted mutants	737:773	the carboxyl-terminal deleted mutants	737:773	The results obtained with the carboxyl-terminal deleted mutants showed that the PG-M-CSF-specific 150-200-kDa subunit had a large part of the precursor sequence at its carboxyl terminus removed in the 43-kDa subunit by proteolytic processing.
8051056	7	65	theme	subunit	1301:1307	arg1	terminus					1273:1280	the carboxyl terminus	1260:1280	the carboxyl terminus of the 150-200-kDa subunit	1260:1307	Truncated mutation analysis showed that the carboxyl terminus of the 150-200-kDa subunit lay downstream of Arg412.
8051056	8	66	theme	sulfate	1526:1532	arg1	loss					1502:1505	complete loss	1493:1505	complete loss of the chondroitin sulfate substitution	1493:1545	We also showed that the chondroitin sulfate binding site in the 150-200-kDa subunit was Ser277, since conversion of Ser277 to the alanine residue resulted in complete loss of the chondroitin sulfate substitution.
8051056	1	67	theme	high	162:165	arg1	factor					117:122	Proteoglycan macrophage colony-stimulating factor	74:122	Proteoglycan macrophage colony-stimulating factor (PG-M-CSF)	74:133	Proteoglycan macrophage colony-stimulating factor (PG-M-CSF) was recently reported as a high molecular type of macrophage colony-stimulating factor (M-CSF).
8051056	1	67	theme	high	162:165	arg1	type					177:180	a high molecular type	160:180	a high molecular type of macrophage colony-stimulating factor (M-CSF)	160:228	Proteoglycan macrophage colony-stimulating factor (PG-M-CSF) was recently reported as a high molecular type of macrophage colony-stimulating factor (M-CSF).
8051056	3	68	theme	subunit	454:460	arg1	subunit					409:415	a homodimeric 150-200-kDa subunit	383:415	a homodimeric 150-200-kDa subunit	383:415	PG-M-CSF contained two types of molecules, a homodimeric 150-200-kDa subunit and a heterodimeric form of a 43-kDa subunit and the 150-200-kDa subunit.
8051056	3	68	theme	subunit	454:460	arg1	types					363:367	two types	359:367	two types of molecules	359:380	PG-M-CSF contained two types of molecules, a homodimeric 150-200-kDa subunit and a heterodimeric form of a 43-kDa subunit and the 150-200-kDa subunit.
8051056	3	68	theme	subunit	454:460	arg1	form					437:440	a heterodimeric form	421:440	a heterodimeric form of a 43-kDa subunit and the 150-200-kDa subunit	421:488	PG-M-CSF contained two types of molecules, a homodimeric 150-200-kDa subunit and a heterodimeric form of a 43-kDa subunit and the 150-200-kDa subunit.
8051056	5	69	theme	deleted	759:765	arg1	mutants					767:773	the carboxyl-terminal deleted mutants	737:773	the carboxyl-terminal deleted mutants	737:773	The results obtained with the carboxyl-terminal deleted mutants showed that the PG-M-CSF-specific 150-200-kDa subunit had a large part of the precursor sequence at its carboxyl terminus removed in the 43-kDa subunit by proteolytic processing.
8051056	8	70	theme	complete	1493:1500	arg1	loss					1502:1505	complete loss	1493:1505	complete loss of the chondroitin sulfate substitution	1493:1545	We also showed that the chondroitin sulfate binding site in the 150-200-kDa subunit was Ser277, since conversion of Ser277 to the alanine residue resulted in complete loss of the chondroitin sulfate substitution.
8051056	5	71	theme	large	835:839	arg1	part					841:844	a large part	833:844	a large part of the precursor sequence	833:870	The results obtained with the carboxyl-terminal deleted mutants showed that the PG-M-CSF-specific 150-200-kDa subunit had a large part of the precursor sequence at its carboxyl terminus removed in the 43-kDa subunit by proteolytic processing.
8051056	1	72	theme	molecular	167:175	arg1	factor					117:122	Proteoglycan macrophage colony-stimulating factor	74:122	Proteoglycan macrophage colony-stimulating factor (PG-M-CSF)	74:133	Proteoglycan macrophage colony-stimulating factor (PG-M-CSF) was recently reported as a high molecular type of macrophage colony-stimulating factor (M-CSF).
8051056	1	72	theme	molecular	167:175	arg1	type					177:180	a high molecular type	160:180	a high molecular type of macrophage colony-stimulating factor (M-CSF)	160:228	Proteoglycan macrophage colony-stimulating factor (PG-M-CSF) was recently reported as a high molecular type of macrophage colony-stimulating factor (M-CSF).
8051056	8	73	from	site	1387:1390	arg1	subunit					1411:1417	the 150-200-kDa subunit	1395:1417	the 150-200-kDa subunit	1395:1417	We also showed that the chondroitin sulfate binding site in the 150-200-kDa subunit was Ser277, since conversion of Ser277 to the alanine residue resulted in complete loss of the chondroitin sulfate substitution.
8051056	4	74	theme	43-kDa	624:629	arg1	subunit					631:637	the 43-kDa subunit	620:637	the 43-kDa subunit	620:637	The 150-200-kDa subunit carries a chondroitin sulfate chain, and its amino-terminal amino acid sequence was identical to that of the 43-kDa subunit, which is known to form the conventional M-CSF molecule (85-kDa M-CSF).
23888046	6	0	theme	inhibitors	1257:1266	arg1	development					1205:1215	development	1205:1215	development	1205:1215	These results explain the calcium-modulated substrate specificity of APA in central hypertension regulation and can guide the design and development of brain-targeting antihypertensive APA inhibitors.
23888046	6	0	theme	inhibitors	1257:1266	arg1	design					1194:1199	design	1194:1199	design	1194:1199	These results explain the calcium-modulated substrate specificity of APA in central hypertension regulation and can guide the design and development of brain-targeting antihypertensive APA inhibitors.
23888046	5	1	contain	has	949:951	arg1	amastatin					939:947	amastatin	939:947	amastatin	939:947	Of the peptidomimetic inhibitors of APA, amastatin has higher potency than bestatin by fitting better in the S1 pocket and interacting additionally with the S3' subsite.
23888046	5	1	contain	has	949:951	arg2	potency					960:966	higher potency	953:966	higher potency than bestatin	953:980	Of the peptidomimetic inhibitors of APA, amastatin has higher potency than bestatin by fitting better in the S1 pocket and interacting additionally with the S3' subsite.
23888046	3	2	theme	salt	671:674	arg1	bridges					676:682	salt bridges	671:682	salt bridges	671:682	Without calcium, the S1 pocket can bind both acidic and basic residues through formation of salt bridges with the charged side chains.
23888046	6	3	theme	APA	1253:1255	arg1	inhibitors					1257:1266	brain-targeting antihypertensive APA inhibitors	1220:1266	brain-targeting antihypertensive APA inhibitors	1220:1266	These results explain the calcium-modulated substrate specificity of APA in central hypertension regulation and can guide the design and development of brain-targeting antihypertensive APA inhibitors.
23888046	3	4	theme	acidic	624:629	arg1	residues					641:648	both acidic and basic residues	619:648	both acidic and basic residues	619:648	Without calcium, the S1 pocket can bind both acidic and basic residues through formation of salt bridges with the charged side chains.
23888046	2	5	theme	calcium-binding	533:547	arg1	site					549:552	a calcium-binding site	531:552	a calcium-binding site in the S1 pocket of APA	531:576	Here, we determined the crystal structures of human APA and its complexes with different ligands and identified a calcium-binding site in the S1 pocket of APA.
23888046	3	6	theme	bridges	676:682	arg1	formation					658:666	formation	658:666	formation of salt bridges with the charged side chains	658:711	Without calcium, the S1 pocket can bind both acidic and basic residues through formation of salt bridges with the charged side chains.
23888046	4	7	theme	basic	835:839	arg1	residues					841:848	basic residues	835:848	basic residues	835:848	In the presence of calcium, the binding of acidic residues is enhanced as they ligate the cation, whereas the binding of basic residues is no longer favorable due to charge repulsion.
23888046	2	8	with	complexes	483:491	arg1	ligands					508:514	different ligands	498:514	different ligands	498:514	Here, we determined the crystal structures of human APA and its complexes with different ligands and identified a calcium-binding site in the S1 pocket of APA.
23888046	5	9	theme	peptidomimetic	905:918	arg1	inhibitors					920:929	the peptidomimetic inhibitors	901:929	the peptidomimetic inhibitors of APA	901:936	Of the peptidomimetic inhibitors of APA, amastatin has higher potency than bestatin by fitting better in the S1 pocket and interacting additionally with the S3' subsite.
23888046	6	10	theme	brain-targeting	1220:1234	arg1	inhibitors					1257:1266	brain-targeting antihypertensive APA inhibitors	1220:1266	brain-targeting antihypertensive APA inhibitors	1220:1266	These results explain the calcium-modulated substrate specificity of APA in central hypertension regulation and can guide the design and development of brain-targeting antihypertensive APA inhibitors.
23888046	4	11	theme	calcium	733:739	arg1	presence					721:728	the presence	717:728	the presence of calcium	717:739	In the presence of calcium, the binding of acidic residues is enhanced as they ligate the cation, whereas the binding of basic residues is no longer favorable due to charge repulsion.
23888046	6	12	from	specificity	1122:1132	arg1	regulation					1165:1174	central hypertension regulation	1144:1174	central hypertension regulation	1144:1174	These results explain the calcium-modulated substrate specificity of APA in central hypertension regulation and can guide the design and development of brain-targeting antihypertensive APA inhibitors.
23888046	0	13	theme	human	60:64	arg1	Hypertension					84:95	human aminopeptidase A. Hypertension	60:95	human aminopeptidase A. Hypertension	60:95	Structural insights into central hypertension regulation by human aminopeptidase A. Hypertension is regulated through both the central and systemic renin-angiotensin systems.
23888046	1	14	theme	central	182:188	arg1	system					208:213	the central renin-angiotensin system	178:213	the central renin-angiotensin system	178:213	In the central renin-angiotensin system, zinc-dependent aminopeptidase A (APA) up-regulates blood pressure by specifically cleaving the N-terminal aspartate, but not the adjacent arginine, from angiotensin II, a process facilitated by calcium.
23888046	3	15	theme	charged	693:699	arg1	chains					706:711	the charged side chains	689:711	the charged side chains	689:711	Without calcium, the S1 pocket can bind both acidic and basic residues through formation of salt bridges with the charged side chains.
23888046	5	16	theme	APA	934:936	arg1	inhibitors					920:929	the peptidomimetic inhibitors	901:929	the peptidomimetic inhibitors of APA	901:936	Of the peptidomimetic inhibitors of APA, amastatin has higher potency than bestatin by fitting better in the S1 pocket and interacting additionally with the S3' subsite.
23888046	3	17	with	formation	658:666	arg1	chains					706:711	the charged side chains	689:711	the charged side chains	689:711	Without calcium, the S1 pocket can bind both acidic and basic residues through formation of salt bridges with the charged side chains.
23888046	1	18	theme	renin-angiotensin	190:206	arg1	system					208:213	the central renin-angiotensin system	178:213	the central renin-angiotensin system	178:213	In the central renin-angiotensin system, zinc-dependent aminopeptidase A (APA) up-regulates blood pressure by specifically cleaving the N-terminal aspartate, but not the adjacent arginine, from angiotensin II, a process facilitated by calcium.
23888046	3	19	theme	side	701:704	arg1	chains					706:711	the charged side chains	689:711	the charged side chains	689:711	Without calcium, the S1 pocket can bind both acidic and basic residues through formation of salt bridges with the charged side chains.
23888046	6	20	theme	calcium-modulated	1094:1110	arg1	specificity					1122:1132	the calcium-modulated substrate specificity	1090:1132	the calcium-modulated substrate specificity of APA in central hypertension regulation	1090:1174	These results explain the calcium-modulated substrate specificity of APA in central hypertension regulation and can guide the design and development of brain-targeting antihypertensive APA inhibitors.
23888046	4	21	theme	residues	841:848	arg1	binding					824:830	the binding	820:830	the binding of basic residues	820:848	In the presence of calcium, the binding of acidic residues is enhanced as they ligate the cation, whereas the binding of basic residues is no longer favorable due to charge repulsion.
23888046	4	21	theme	residues	841:848	arg1	favorable					863:871	favorable	863:871	favorable	863:871	In the presence of calcium, the binding of acidic residues is enhanced as they ligate the cation, whereas the binding of basic residues is no longer favorable due to charge repulsion.
23888046	0	22	theme	Structural	0:9	arg1	insights					11:18	Structural insights	0:18	Structural insights into central hypertension regulation by human aminopeptidase A. Hypertension	0:95	Structural insights into central hypertension regulation by human aminopeptidase A. Hypertension is regulated through both the central and systemic renin-angiotensin systems.
23888046	4	23	theme	charge	880:885	arg1	repulsion					887:895	charge repulsion	880:895	charge repulsion	880:895	In the presence of calcium, the binding of acidic residues is enhanced as they ligate the cation, whereas the binding of basic residues is no longer favorable due to charge repulsion.
23888046	0	24	theme	central	25:31	arg1	regulation					46:55	central hypertension regulation	25:55	central hypertension regulation by human aminopeptidase A. Hypertension	25:95	Structural insights into central hypertension regulation by human aminopeptidase A. Hypertension is regulated through both the central and systemic renin-angiotensin systems.
23888046	1	25	theme	N-terminal	311:320	arg1	aspartate					322:330	the N-terminal aspartate	307:330	the N-terminal aspartate	307:330	In the central renin-angiotensin system, zinc-dependent aminopeptidase A (APA) up-regulates blood pressure by specifically cleaving the N-terminal aspartate, but not the adjacent arginine, from angiotensin II, a process facilitated by calcium.
23888046	2	26	theme	S1	561:562	arg1	pocket					564:569	the S1 pocket	557:569	the S1 pocket of APA	557:576	Here, we determined the crystal structures of human APA and its complexes with different ligands and identified a calcium-binding site in the S1 pocket of APA.
23888046	1	27	theme	zinc-dependent	216:229	arg1	APA					249:251	APA	249:251	APA	249:251	In the central renin-angiotensin system, zinc-dependent aminopeptidase A (APA) up-regulates blood pressure by specifically cleaving the N-terminal aspartate, but not the adjacent arginine, from angiotensin II, a process facilitated by calcium.
23888046	1	27	theme	zinc-dependent	216:229	arg1	A					246:246	zinc-dependent aminopeptidase A	216:246	zinc-dependent aminopeptidase A (APA)	216:252	In the central renin-angiotensin system, zinc-dependent aminopeptidase A (APA) up-regulates blood pressure by specifically cleaving the N-terminal aspartate, but not the adjacent arginine, from angiotensin II, a process facilitated by calcium.
23888046	6	28	theme	APA	1137:1139	arg1	specificity					1122:1132	the calcium-modulated substrate specificity	1090:1132	the calcium-modulated substrate specificity of APA in central hypertension regulation	1090:1174	These results explain the calcium-modulated substrate specificity of APA in central hypertension regulation and can guide the design and development of brain-targeting antihypertensive APA inhibitors.
23888046	5	29	theme	S1	1007:1008	arg1	pocket					1010:1015	the S1 pocket	1003:1015	the S1 pocket	1003:1015	Of the peptidomimetic inhibitors of APA, amastatin has higher potency than bestatin by fitting better in the S1 pocket and interacting additionally with the S3' subsite.
23888046	6	30	theme	central	1144:1150	arg1	regulation					1165:1174	central hypertension regulation	1144:1174	central hypertension regulation	1144:1174	These results explain the calcium-modulated substrate specificity of APA in central hypertension regulation and can guide the design and development of brain-targeting antihypertensive APA inhibitors.
23888046	1	31	theme	aminopeptidase	231:244	arg1	APA					249:251	APA	249:251	APA	249:251	In the central renin-angiotensin system, zinc-dependent aminopeptidase A (APA) up-regulates blood pressure by specifically cleaving the N-terminal aspartate, but not the adjacent arginine, from angiotensin II, a process facilitated by calcium.
23888046	1	31	theme	aminopeptidase	231:244	arg1	A					246:246	zinc-dependent aminopeptidase A	216:246	zinc-dependent aminopeptidase A (APA)	216:252	In the central renin-angiotensin system, zinc-dependent aminopeptidase A (APA) up-regulates blood pressure by specifically cleaving the N-terminal aspartate, but not the adjacent arginine, from angiotensin II, a process facilitated by calcium.
23888046	5	32	theme	higher	953:958	arg1	potency					960:966	higher potency	953:966	higher potency than bestatin	953:980	Of the peptidomimetic inhibitors of APA, amastatin has higher potency than bestatin by fitting better in the S1 pocket and interacting additionally with the S3' subsite.
23888046	0	33	theme	renin-angiotensin	148:164	arg1	systems					166:172	systemic renin-angiotensin systems	139:172	systemic renin-angiotensin systems	139:172	Structural insights into central hypertension regulation by human aminopeptidase A. Hypertension is regulated through both the central and systemic renin-angiotensin systems.
23888046	3	34	theme	basic	635:639	arg1	residues					641:648	both acidic and basic residues	619:648	both acidic and basic residues	619:648	Without calcium, the S1 pocket can bind both acidic and basic residues through formation of salt bridges with the charged side chains.
23888046	0	35	theme	hypertension	33:44	arg1	regulation					46:55	central hypertension regulation	25:55	central hypertension regulation by human aminopeptidase A. Hypertension	25:95	Structural insights into central hypertension regulation by human aminopeptidase A. Hypertension is regulated through both the central and systemic renin-angiotensin systems.
23888046	0	36	theme	systemic	139:146	arg1	systems					166:172	systemic renin-angiotensin systems	139:172	systemic renin-angiotensin systems	139:172	Structural insights into central hypertension regulation by human aminopeptidase A. Hypertension is regulated through both the central and systemic renin-angiotensin systems.
23888046	2	37	theme	crystal	443:449	arg1	structures					451:460	the crystal structures	439:460	the crystal structures of human APA	439:473	Here, we determined the crystal structures of human APA and its complexes with different ligands and identified a calcium-binding site in the S1 pocket of APA.
23888046	4	38	dep	enhanced	776:783	arg1	whereas					812:818	whereas	812:818	whereas	812:818	In the presence of calcium, the binding of acidic residues is enhanced as they ligate the cation, whereas the binding of basic residues is no longer favorable due to charge repulsion.
23888046	2	39	theme	APA	471:473	arg1	structures					451:460	the crystal structures	439:460	the crystal structures of human APA	439:473	Here, we determined the crystal structures of human APA and its complexes with different ligands and identified a calcium-binding site in the S1 pocket of APA.
23888046	2	39	theme	APA	471:473	arg1	complexes					483:491	its complexes	479:491	its complexes with different ligands	479:514	Here, we determined the crystal structures of human APA and its complexes with different ligands and identified a calcium-binding site in the S1 pocket of APA.
23888046	0	40	theme	aminopeptidase	66:79	arg1	Hypertension					84:95	human aminopeptidase A. Hypertension	60:95	human aminopeptidase A. Hypertension	60:95	Structural insights into central hypertension regulation by human aminopeptidase A. Hypertension is regulated through both the central and systemic renin-angiotensin systems.
23888046	2	41	theme	human	465:469	arg1	APA					471:473	human APA	465:473	human APA	465:473	Here, we determined the crystal structures of human APA and its complexes with different ligands and identified a calcium-binding site in the S1 pocket of APA.
23888046	2	42	theme	APA	574:576	arg1	pocket					564:569	the S1 pocket	557:569	the S1 pocket of APA	557:576	Here, we determined the crystal structures of human APA and its complexes with different ligands and identified a calcium-binding site in the S1 pocket of APA.
23888046	6	43	theme	antihypertensive	1236:1251	arg1	inhibitors					1257:1266	brain-targeting antihypertensive APA inhibitors	1220:1266	brain-targeting antihypertensive APA inhibitors	1220:1266	These results explain the calcium-modulated substrate specificity of APA in central hypertension regulation and can guide the design and development of brain-targeting antihypertensive APA inhibitors.
23888046	1	44	theme	adjacent	345:352	arg1	arginine					354:361	the adjacent arginine	341:361	the adjacent arginine	341:361	In the central renin-angiotensin system, zinc-dependent aminopeptidase A (APA) up-regulates blood pressure by specifically cleaving the N-terminal aspartate, but not the adjacent arginine, from angiotensin II, a process facilitated by calcium.
23888046	4	45	theme	acidic	757:762	arg1	residues					764:771	acidic residues	757:771	acidic residues	757:771	In the presence of calcium, the binding of acidic residues is enhanced as they ligate the cation, whereas the binding of basic residues is no longer favorable due to charge repulsion.
23888046	2	46	with	structures	451:460	arg1	ligands					508:514	different ligands	498:514	different ligands	498:514	Here, we determined the crystal structures of human APA and its complexes with different ligands and identified a calcium-binding site in the S1 pocket of APA.
23888046	6	47	theme	substrate	1112:1120	arg1	specificity					1122:1132	the calcium-modulated substrate specificity	1090:1132	the calcium-modulated substrate specificity of APA in central hypertension regulation	1090:1174	These results explain the calcium-modulated substrate specificity of APA in central hypertension regulation and can guide the design and development of brain-targeting antihypertensive APA inhibitors.
23888046	6	48	theme	hypertension	1152:1163	arg1	regulation					1165:1174	central hypertension regulation	1144:1174	central hypertension regulation	1144:1174	These results explain the calcium-modulated substrate specificity of APA in central hypertension regulation and can guide the design and development of brain-targeting antihypertensive APA inhibitors.
23888046	2	49	from	site	549:552	arg1	pocket					564:569	the S1 pocket	557:569	the S1 pocket of APA	557:576	Here, we determined the crystal structures of human APA and its complexes with different ligands and identified a calcium-binding site in the S1 pocket of APA.
23888046	0	50	theme	A.	81:82	arg1	Hypertension					84:95	human aminopeptidase A. Hypertension	60:95	human aminopeptidase A. Hypertension	60:95	Structural insights into central hypertension regulation by human aminopeptidase A. Hypertension is regulated through both the central and systemic renin-angiotensin systems.
23888046	3	51	theme	S1	600:601	arg1	pocket					603:608	the S1 pocket	596:608	the S1 pocket	596:608	Without calcium, the S1 pocket can bind both acidic and basic residues through formation of salt bridges with the charged side chains.
23888046	2	52	theme	different	498:506	arg1	ligands					508:514	different ligands	498:514	different ligands	498:514	Here, we determined the crystal structures of human APA and its complexes with different ligands and identified a calcium-binding site in the S1 pocket of APA.
23888046	4	53	theme	residues	764:771	arg1	binding					746:752	the binding	742:752	the binding of acidic residues	742:771	In the presence of calcium, the binding of acidic residues is enhanced as they ligate the cation, whereas the binding of basic residues is no longer favorable due to charge repulsion.
23888046	6	54	dep	design	1194:1199	arg1	the					1190:1192	the	1190:1192	the	1190:1192	These results explain the calcium-modulated substrate specificity of APA in central hypertension regulation and can guide the design and development of brain-targeting antihypertensive APA inhibitors.
23888046	1	55	theme	blood	267:271	arg1	pressure					273:280	blood pressure	267:280	blood pressure	267:280	In the central renin-angiotensin system, zinc-dependent aminopeptidase A (APA) up-regulates blood pressure by specifically cleaving the N-terminal aspartate, but not the adjacent arginine, from angiotensin II, a process facilitated by calcium.
22624035	0	0	theme	RHBDD1-induced	88:101	arg1	proteolysis					103:113	rhomboid protease RHBDD1-induced proteolysis	70:113	rhomboid protease RHBDD1-induced proteolysis	70:113	Exosome-related multi-pass transmembrane protein TSAP6 is a target of rhomboid protease RHBDD1-induced proteolysis.
22624035	8	1	theme	exosomal	1100:1107	arg1	components					1109:1118	certain exosomal components	1092:1118	certain exosomal components	1092:1118	The increased exosome secretion was verfied through the detection of certain exosomal components, including Tsg101, Tf-R, FasL and Trail.
22624035	8	1	theme	exosomal	1100:1107	arg1	Tsg101					1131:1136	Tsg101	1131:1136	Tsg101	1131:1136	The increased exosome secretion was verfied through the detection of certain exosomal components, including Tsg101, Tf-R, FasL and Trail.
22624035	8	1	theme	exosomal	1100:1107	arg1	Trail					1154:1158	Trail	1154:1158	Trail	1154:1158	The increased exosome secretion was verfied through the detection of certain exosomal components, including Tsg101, Tf-R, FasL and Trail.
22624035	8	1	theme	exosomal	1100:1107	arg1	FasL					1145:1148	FasL	1145:1148	FasL	1145:1148	The increased exosome secretion was verfied through the detection of certain exosomal components, including Tsg101, Tf-R, FasL and Trail.
22624035	8	1	theme	exosomal	1100:1107	arg1	Tf-R					1139:1142	Tf-R	1139:1142	Tf-R	1139:1142	The increased exosome secretion was verfied through the detection of certain exosomal components, including Tsg101, Tf-R, FasL and Trail.
22624035	0	2	theme	protease	79:86	arg1	proteolysis					103:113	rhomboid protease RHBDD1-induced proteolysis	70:113	rhomboid protease RHBDD1-induced proteolysis	70:113	Exosome-related multi-pass transmembrane protein TSAP6 is a target of rhomboid protease RHBDD1-induced proteolysis.
22624035	6	3	theme	endogenous	870:879	arg1	RHBDD1					881:886	the endogenous RHBDD1	866:886	the endogenous RHBDD1 in HCT116 and RKO colon cancer cells	866:923	A somatic cell knock-in approach was used to genetically inactivate the endogenous RHBDD1 in HCT116 and RKO colon cancer cells.
22624035	3	4	theme	TSAP6	476:480	arg1	proteolysis					461:471	the proteolysis	457:471	the proteolysis of TSAP6	457:480	RHBDD1 was found to induce the proteolysis of TSAP6 in a dose- and activity-dependent manner.
22624035	4	5	theme	TSAP6	540:544	arg1	restricted					554:563	restricted	554:563	restricted	554:563	The cleavage of TSAP6 was not restricted to its glycosylated form and occurred in three different regions.
22624035	4	5	theme	TSAP6	540:544	arg1	cleavage					528:535	The cleavage	524:535	The cleavage of TSAP6	524:544	The cleavage of TSAP6 was not restricted to its glycosylated form and occurred in three different regions.
22624035	11	6	theme	exosomal	1576:1583	arg1	pathway					1595:1601	a nonclassical exosomal secretion pathway	1561:1601	a nonclassical exosomal secretion pathway through the restriction of TSAP6	1561:1634	Taken together, our findings suggest that RHBDD1 is involved in the regulation of a nonclassical exosomal secretion pathway through the restriction of TSAP6.
22624035	7	7	theme	Exosome	926:932	arg1	secretion					934:942	Exosome secretion	926:942	Exosome secretion	926:942	Exosome secretion was significantly elevated when RHBDD1 was inactivated in the two cells lines.
22624035	3	8	theme	activity-dependent	497:514	arg1	manner					516:521	activity-dependent manner	497:521	activity-dependent manner	497:521	RHBDD1 was found to induce the proteolysis of TSAP6 in a dose- and activity-dependent manner.
22624035	0	9	theme	proteolysis	103:113	arg1	TSAP6					49:53	Exosome-related multi-pass transmembrane protein TSAP6	0:53	Exosome-related multi-pass transmembrane protein TSAP6	0:53	Exosome-related multi-pass transmembrane protein TSAP6 is a target of rhomboid protease RHBDD1-induced proteolysis.
22624035	0	9	theme	proteolysis	103:113	arg1	target					60:65	a target	58:65	a target of rhomboid protease RHBDD1-induced proteolysis	58:113	Exosome-related multi-pass transmembrane protein TSAP6 is a target of rhomboid protease RHBDD1-induced proteolysis.
22624035	4	10	gly	glycosylated	572:583	arg1	form					585:588	its glycosylated form	568:588	its glycosylated form	568:588	The cleavage of TSAP6 was not restricted to its glycosylated form and occurred in three different regions.
22624035	9	11	theme	RHBDD1	1301:1306	arg1	role					1293:1296	the role	1289:1296	the role of RHBDD1 in regulating exosomal trafficking	1289:1341	In addition, the elevation of exosome secretion by RHBDD1 inactivation was reduced when TSAP6 was knocked down, indicating that the role of RHBDD1 in regulating exosomal trafficking is very likely to be TSAP6-dependent.
22624035	9	11	theme	RHBDD1	1301:1306	arg1	likely					1351:1356	likely	1351:1356	likely	1351:1356	In addition, the elevation of exosome secretion by RHBDD1 inactivation was reduced when TSAP6 was knocked down, indicating that the role of RHBDD1 in regulating exosomal trafficking is very likely to be TSAP6-dependent.
22624035	9	11	theme	RHBDD1	1301:1306	arg1	TSAP6-dependent					1364:1378	TSAP6-dependent	1364:1378	TSAP6-dependent	1364:1378	In addition, the elevation of exosome secretion by RHBDD1 inactivation was reduced when TSAP6 was knocked down, indicating that the role of RHBDD1 in regulating exosomal trafficking is very likely to be TSAP6-dependent.
22624035	11	12	theme	pathway	1595:1601	arg1	regulation					1547:1556	the regulation	1543:1556	the regulation of a nonclassical exosomal secretion pathway through the restriction of TSAP6	1543:1634	Taken together, our findings suggest that RHBDD1 is involved in the regulation of a nonclassical exosomal secretion pathway through the restriction of TSAP6.
22624035	5	13	theme	third	761:765	arg1	TSAP6					791:795	TSAP6	791:795	TSAP6	791:795	In addition, mass spectrometry and mutagenesis analyses both indicated that the major cleavage site laid in the C-terminal of the third transmembrane domain of TSAP6.
22624035	5	13	theme	third	761:765	arg1	domain					781:786	the third transmembrane domain	757:786	the third transmembrane domain of TSAP6	757:795	In addition, mass spectrometry and mutagenesis analyses both indicated that the major cleavage site laid in the C-terminal of the third transmembrane domain of TSAP6.
22624035	5	14	theme	major	711:715	arg1	site					726:729	the major cleavage site	707:729	the major cleavage site	707:729	In addition, mass spectrometry and mutagenesis analyses both indicated that the major cleavage site laid in the C-terminal of the third transmembrane domain of TSAP6.
22624035	5	15	theme	transmembrane	767:779	arg1	TSAP6					791:795	TSAP6	791:795	TSAP6	791:795	In addition, mass spectrometry and mutagenesis analyses both indicated that the major cleavage site laid in the C-terminal of the third transmembrane domain of TSAP6.
22624035	5	15	theme	transmembrane	767:779	arg1	domain					781:786	the third transmembrane domain	757:786	the third transmembrane domain of TSAP6	757:795	In addition, mass spectrometry and mutagenesis analyses both indicated that the major cleavage site laid in the C-terminal of the third transmembrane domain of TSAP6.
22624035	4	16	theme	different	612:620	arg1	regions					622:628	three different regions	606:628	three different regions	606:628	The cleavage of TSAP6 was not restricted to its glycosylated form and occurred in three different regions.
22624035	2	17	theme	RHBDD1	422:427	arg1	protein					340:346	a multi-pass transmembrane protein	313:346	a multi-pass transmembrane protein	313:346	In this study, we identified a multi-pass transmembrane protein, tumor suppressor activated pathway-6 (TSAP6) as a potential substrate of RHBDD1.
22624035	2	17	theme	RHBDD1	422:427	arg1	substrate					409:417	a potential substrate	397:417	a potential substrate of RHBDD1	397:427	In this study, we identified a multi-pass transmembrane protein, tumor suppressor activated pathway-6 (TSAP6) as a potential substrate of RHBDD1.
22624035	6	18	from	RHBDD1	881:886	arg1	cells					919:923	RKO colon cancer cells	902:923	RKO colon cancer cells	902:923	A somatic cell knock-in approach was used to genetically inactivate the endogenous RHBDD1 in HCT116 and RKO colon cancer cells.
22624035	6	18	from	RHBDD1	881:886	arg1	HCT116					891:896	HCT116	891:896	HCT116	891:896	A somatic cell knock-in approach was used to genetically inactivate the endogenous RHBDD1 in HCT116 and RKO colon cancer cells.
22624035	8	19	theme	increased	1027:1035	arg1	secretion					1045:1053	The increased exosome secretion	1023:1053	The increased exosome secretion	1023:1053	The increased exosome secretion was verfied through the detection of certain exosomal components, including Tsg101, Tf-R, FasL and Trail.
22624035	5	20	theme	cleavage	717:724	arg1	site					726:729	the major cleavage site	707:729	the major cleavage site	707:729	In addition, mass spectrometry and mutagenesis analyses both indicated that the major cleavage site laid in the C-terminal of the third transmembrane domain of TSAP6.
22624035	10	21	theme	Jurkat	1465:1470	arg1	cells					1472:1476	Jurkat cells	1465:1476	Jurkat cells	1465:1476	We found that the increase in FasL and Trail increased exosome-induced apoptosis in Jurkat cells.
22624035	2	22	theme	activated	366:374	arg1	pathway-6					376:384	tumor suppressor activated pathway-6	349:384	tumor suppressor activated pathway-6 (TSAP6)	349:392	In this study, we identified a multi-pass transmembrane protein, tumor suppressor activated pathway-6 (TSAP6) as a potential substrate of RHBDD1.
22624035	2	22	theme	activated	366:374	arg1	protein					340:346	a multi-pass transmembrane protein	313:346	a multi-pass transmembrane protein	313:346	In this study, we identified a multi-pass transmembrane protein, tumor suppressor activated pathway-6 (TSAP6) as a potential substrate of RHBDD1.
22624035	2	22	theme	activated	366:374	arg1	TSAP6					387:391	TSAP6	387:391	TSAP6	387:391	In this study, we identified a multi-pass transmembrane protein, tumor suppressor activated pathway-6 (TSAP6) as a potential substrate of RHBDD1.
22624035	0	23	theme	Exosome-related	0:14	arg1	TSAP6					49:53	Exosome-related multi-pass transmembrane protein TSAP6	0:53	Exosome-related multi-pass transmembrane protein TSAP6	0:53	Exosome-related multi-pass transmembrane protein TSAP6 is a target of rhomboid protease RHBDD1-induced proteolysis.
22624035	0	23	theme	Exosome-related	0:14	arg1	target					60:65	a target	58:65	a target of rhomboid protease RHBDD1-induced proteolysis	58:113	Exosome-related multi-pass transmembrane protein TSAP6 is a target of rhomboid protease RHBDD1-induced proteolysis.
22624035	1	24	theme	Bcl-2	265:269	arg1	Bik					279:281	the Bcl-2 protein Bik	261:281	the Bcl-2 protein Bik	261:281	We have previously reported that rhomboid domain containing 1 (RHBDD1), a mammalian rhomboid protease highly expressed in the testis, can cleave the Bcl-2 protein Bik.
22624035	9	25	theme	secretion	1199:1207	arg1	elevation					1178:1186	the elevation	1174:1186	the elevation of exosome secretion by RHBDD1 inactivation	1174:1230	In addition, the elevation of exosome secretion by RHBDD1 inactivation was reduced when TSAP6 was knocked down, indicating that the role of RHBDD1 in regulating exosomal trafficking is very likely to be TSAP6-dependent.
22624035	11	26	theme	nonclassical	1563:1574	arg1	pathway					1595:1601	a nonclassical exosomal secretion pathway	1561:1601	a nonclassical exosomal secretion pathway through the restriction of TSAP6	1561:1634	Taken together, our findings suggest that RHBDD1 is involved in the regulation of a nonclassical exosomal secretion pathway through the restriction of TSAP6.
22624035	2	27	theme	suppressor	355:364	arg1	pathway-6					376:384	tumor suppressor activated pathway-6	349:384	tumor suppressor activated pathway-6 (TSAP6)	349:392	In this study, we identified a multi-pass transmembrane protein, tumor suppressor activated pathway-6 (TSAP6) as a potential substrate of RHBDD1.
22624035	2	27	theme	suppressor	355:364	arg1	protein					340:346	a multi-pass transmembrane protein	313:346	a multi-pass transmembrane protein	313:346	In this study, we identified a multi-pass transmembrane protein, tumor suppressor activated pathway-6 (TSAP6) as a potential substrate of RHBDD1.
22624035	2	27	theme	suppressor	355:364	arg1	TSAP6					387:391	TSAP6	387:391	TSAP6	387:391	In this study, we identified a multi-pass transmembrane protein, tumor suppressor activated pathway-6 (TSAP6) as a potential substrate of RHBDD1.
22624035	0	28	theme	protein	41:47	arg1	TSAP6					49:53	Exosome-related multi-pass transmembrane protein TSAP6	0:53	Exosome-related multi-pass transmembrane protein TSAP6	0:53	Exosome-related multi-pass transmembrane protein TSAP6 is a target of rhomboid protease RHBDD1-induced proteolysis.
22624035	0	28	theme	protein	41:47	arg1	target					60:65	a target	58:65	a target of rhomboid protease RHBDD1-induced proteolysis	58:113	Exosome-related multi-pass transmembrane protein TSAP6 is a target of rhomboid protease RHBDD1-induced proteolysis.
22624035	1	29	theme	protein	271:277	arg1	Bik					279:281	the Bcl-2 protein Bik	261:281	the Bcl-2 protein Bik	261:281	We have previously reported that rhomboid domain containing 1 (RHBDD1), a mammalian rhomboid protease highly expressed in the testis, can cleave the Bcl-2 protein Bik.
22624035	10	30	theme	exosome-induced	1436:1450	arg1	apoptosis					1452:1460	exosome-induced apoptosis	1436:1460	exosome-induced apoptosis in Jurkat cells	1436:1476	We found that the increase in FasL and Trail increased exosome-induced apoptosis in Jurkat cells.
22624035	6	31	used	used	835:838	arg2	approach					822:829	A somatic cell knock-in approach	798:829	A somatic cell knock-in approach	798:829	A somatic cell knock-in approach was used to genetically inactivate the endogenous RHBDD1 in HCT116 and RKO colon cancer cells.
22624035	1	32	theme	mammalian	190:198	arg1	protease					209:216	a mammalian rhomboid protease	188:216	a mammalian rhomboid protease highly expressed in the testis	188:247	We have previously reported that rhomboid domain containing 1 (RHBDD1), a mammalian rhomboid protease highly expressed in the testis, can cleave the Bcl-2 protein Bik.
22624035	1	32	theme	mammalian	190:198	arg1	domain					158:163	rhomboid domain containing 1	149:176	rhomboid domain containing 1 (RHBDD1)	149:185	We have previously reported that rhomboid domain containing 1 (RHBDD1), a mammalian rhomboid protease highly expressed in the testis, can cleave the Bcl-2 protein Bik.
22624035	2	33	theme	potential	399:407	arg1	protein					340:346	a multi-pass transmembrane protein	313:346	a multi-pass transmembrane protein	313:346	In this study, we identified a multi-pass transmembrane protein, tumor suppressor activated pathway-6 (TSAP6) as a potential substrate of RHBDD1.
22624035	2	33	theme	potential	399:407	arg1	substrate					409:417	a potential substrate	397:417	a potential substrate of RHBDD1	397:427	In this study, we identified a multi-pass transmembrane protein, tumor suppressor activated pathway-6 (TSAP6) as a potential substrate of RHBDD1.
22624035	5	34	theme	mutagenesis	666:676	arg1	analyses					678:685	mass spectrometry and mutagenesis analyses	644:685	analyses	678:685	In addition, mass spectrometry and mutagenesis analyses both indicated that the major cleavage site laid in the C-terminal of the third transmembrane domain of TSAP6.
22624035	9	35	theme	exosome	1191:1197	arg1	secretion					1199:1207	exosome secretion	1191:1207	exosome secretion	1191:1207	In addition, the elevation of exosome secretion by RHBDD1 inactivation was reduced when TSAP6 was knocked down, indicating that the role of RHBDD1 in regulating exosomal trafficking is very likely to be TSAP6-dependent.
22624035	2	36	theme	transmembrane	326:338	arg1	pathway-6					376:384	tumor suppressor activated pathway-6	349:384	tumor suppressor activated pathway-6 (TSAP6)	349:392	In this study, we identified a multi-pass transmembrane protein, tumor suppressor activated pathway-6 (TSAP6) as a potential substrate of RHBDD1.
22624035	2	36	theme	transmembrane	326:338	arg1	protein					340:346	a multi-pass transmembrane protein	313:346	a multi-pass transmembrane protein	313:346	In this study, we identified a multi-pass transmembrane protein, tumor suppressor activated pathway-6 (TSAP6) as a potential substrate of RHBDD1.
22624035	2	36	theme	transmembrane	326:338	arg1	substrate					409:417	a potential substrate	397:417	a potential substrate of RHBDD1	397:427	In this study, we identified a multi-pass transmembrane protein, tumor suppressor activated pathway-6 (TSAP6) as a potential substrate of RHBDD1.
22624035	8	37	theme	components	1109:1118	arg1	detection					1079:1087	the detection	1075:1087	the detection of certain exosomal components, including Tsg101, Tf-R, FasL and Trail	1075:1158	The increased exosome secretion was verfied through the detection of certain exosomal components, including Tsg101, Tf-R, FasL and Trail.
22624035	1	38	theme	rhomboid	200:207	arg1	protease					209:216	a mammalian rhomboid protease	188:216	a mammalian rhomboid protease highly expressed in the testis	188:247	We have previously reported that rhomboid domain containing 1 (RHBDD1), a mammalian rhomboid protease highly expressed in the testis, can cleave the Bcl-2 protein Bik.
22624035	1	38	theme	rhomboid	200:207	arg1	domain					158:163	rhomboid domain containing 1	149:176	rhomboid domain containing 1 (RHBDD1)	149:185	We have previously reported that rhomboid domain containing 1 (RHBDD1), a mammalian rhomboid protease highly expressed in the testis, can cleave the Bcl-2 protein Bik.
22624035	6	39	theme	cancer	912:917	arg1	cells					919:923	RKO colon cancer cells	902:923	RKO colon cancer cells	902:923	A somatic cell knock-in approach was used to genetically inactivate the endogenous RHBDD1 in HCT116 and RKO colon cancer cells.
22624035	8	40	theme	exosome	1037:1043	arg1	secretion					1045:1053	The increased exosome secretion	1023:1053	The increased exosome secretion	1023:1053	The increased exosome secretion was verfied through the detection of certain exosomal components, including Tsg101, Tf-R, FasL and Trail.
22624035	6	41	theme	colon	906:910	arg1	cells					919:923	RKO colon cancer cells	902:923	RKO colon cancer cells	902:923	A somatic cell knock-in approach was used to genetically inactivate the endogenous RHBDD1 in HCT116 and RKO colon cancer cells.
22624035	10	42	from	apoptosis	1452:1460	arg1	cells					1472:1476	Jurkat cells	1465:1476	Jurkat cells	1465:1476	We found that the increase in FasL and Trail increased exosome-induced apoptosis in Jurkat cells.
22624035	6	43	theme	knock-in	813:820	arg1	approach					822:829	A somatic cell knock-in approach	798:829	A somatic cell knock-in approach	798:829	A somatic cell knock-in approach was used to genetically inactivate the endogenous RHBDD1 in HCT116 and RKO colon cancer cells.
22624035	5	44	theme	domain	781:786	arg1	C-terminal					743:752	C-terminal	743:752	C-terminal	743:752	In addition, mass spectrometry and mutagenesis analyses both indicated that the major cleavage site laid in the C-terminal of the third transmembrane domain of TSAP6.
22624035	6	45	theme	RKO	902:904	arg1	cells					919:923	RKO colon cancer cells	902:923	RKO colon cancer cells	902:923	A somatic cell knock-in approach was used to genetically inactivate the endogenous RHBDD1 in HCT116 and RKO colon cancer cells.
22624035	6	46	theme	cell	808:811	arg1	approach					822:829	A somatic cell knock-in approach	798:829	A somatic cell knock-in approach	798:829	A somatic cell knock-in approach was used to genetically inactivate the endogenous RHBDD1 in HCT116 and RKO colon cancer cells.
22624035	2	47	theme	multi-pass	315:324	arg1	pathway-6					376:384	tumor suppressor activated pathway-6	349:384	tumor suppressor activated pathway-6 (TSAP6)	349:392	In this study, we identified a multi-pass transmembrane protein, tumor suppressor activated pathway-6 (TSAP6) as a potential substrate of RHBDD1.
22624035	2	47	theme	multi-pass	315:324	arg1	protein					340:346	a multi-pass transmembrane protein	313:346	a multi-pass transmembrane protein	313:346	In this study, we identified a multi-pass transmembrane protein, tumor suppressor activated pathway-6 (TSAP6) as a potential substrate of RHBDD1.
22624035	2	47	theme	multi-pass	315:324	arg1	substrate					409:417	a potential substrate	397:417	a potential substrate of RHBDD1	397:427	In this study, we identified a multi-pass transmembrane protein, tumor suppressor activated pathway-6 (TSAP6) as a potential substrate of RHBDD1.
22624035	7	48	theme	cells	1010:1014	arg1	lines					1016:1020	the two cells lines	1002:1020	the two cells lines	1002:1020	Exosome secretion was significantly elevated when RHBDD1 was inactivated in the two cells lines.
22624035	6	49	theme	somatic	800:806	arg1	approach					822:829	A somatic cell knock-in approach	798:829	A somatic cell knock-in approach	798:829	A somatic cell knock-in approach was used to genetically inactivate the endogenous RHBDD1 in HCT116 and RKO colon cancer cells.
22624035	1	50	theme	containing	165:174	arg1	RHBDD1					179:184	RHBDD1	179:184	RHBDD1	179:184	We have previously reported that rhomboid domain containing 1 (RHBDD1), a mammalian rhomboid protease highly expressed in the testis, can cleave the Bcl-2 protein Bik.
22624035	1	50	theme	containing	165:174	arg1	protease					209:216	a mammalian rhomboid protease	188:216	a mammalian rhomboid protease highly expressed in the testis	188:247	We have previously reported that rhomboid domain containing 1 (RHBDD1), a mammalian rhomboid protease highly expressed in the testis, can cleave the Bcl-2 protein Bik.
22624035	1	50	theme	containing	165:174	arg1	domain					158:163	rhomboid domain containing 1	149:176	rhomboid domain containing 1 (RHBDD1)	149:185	We have previously reported that rhomboid domain containing 1 (RHBDD1), a mammalian rhomboid protease highly expressed in the testis, can cleave the Bcl-2 protein Bik.
22624035	11	51	theme	TSAP6	1630:1634	arg1	restriction					1615:1625	the restriction	1611:1625	the restriction of TSAP6	1611:1634	Taken together, our findings suggest that RHBDD1 is involved in the regulation of a nonclassical exosomal secretion pathway through the restriction of TSAP6.
22624035	5	52	theme	mass	644:647	arg1	spectrometry					649:660	mass spectrometry and mutagenesis analyses	644:685	spectrometry	649:660	In addition, mass spectrometry and mutagenesis analyses both indicated that the major cleavage site laid in the C-terminal of the third transmembrane domain of TSAP6.
22624035	9	53	theme	exosomal	1322:1329	arg1	trafficking					1331:1341	exosomal trafficking	1322:1341	exosomal trafficking	1322:1341	In addition, the elevation of exosome secretion by RHBDD1 inactivation was reduced when TSAP6 was knocked down, indicating that the role of RHBDD1 in regulating exosomal trafficking is very likely to be TSAP6-dependent.
22624035	9	54	theme	RHBDD1	1212:1217	arg1	inactivation					1219:1230	RHBDD1 inactivation	1212:1230	RHBDD1 inactivation	1212:1230	In addition, the elevation of exosome secretion by RHBDD1 inactivation was reduced when TSAP6 was knocked down, indicating that the role of RHBDD1 in regulating exosomal trafficking is very likely to be TSAP6-dependent.
22624035	1	55	theme	rhomboid	149:156	arg1	RHBDD1					179:184	RHBDD1	179:184	RHBDD1	179:184	We have previously reported that rhomboid domain containing 1 (RHBDD1), a mammalian rhomboid protease highly expressed in the testis, can cleave the Bcl-2 protein Bik.
22624035	1	55	theme	rhomboid	149:156	arg1	protease					209:216	a mammalian rhomboid protease	188:216	a mammalian rhomboid protease highly expressed in the testis	188:247	We have previously reported that rhomboid domain containing 1 (RHBDD1), a mammalian rhomboid protease highly expressed in the testis, can cleave the Bcl-2 protein Bik.
22624035	1	55	theme	rhomboid	149:156	arg1	domain					158:163	rhomboid domain containing 1	149:176	rhomboid domain containing 1 (RHBDD1)	149:185	We have previously reported that rhomboid domain containing 1 (RHBDD1), a mammalian rhomboid protease highly expressed in the testis, can cleave the Bcl-2 protein Bik.
22624035	0	56	theme	rhomboid	70:77	arg1	proteolysis					103:113	rhomboid protease RHBDD1-induced proteolysis	70:113	rhomboid protease RHBDD1-induced proteolysis	70:113	Exosome-related multi-pass transmembrane protein TSAP6 is a target of rhomboid protease RHBDD1-induced proteolysis.
22624035	10	57	from	increase	1399:1406	arg1	Trail					1420:1424	Trail	1420:1424	Trail	1420:1424	We found that the increase in FasL and Trail increased exosome-induced apoptosis in Jurkat cells.
22624035	10	57	from	increase	1399:1406	arg1	FasL					1411:1414	FasL	1411:1414	FasL	1411:1414	We found that the increase in FasL and Trail increased exosome-induced apoptosis in Jurkat cells.
22624035	5	58	theme	TSAP6	791:795	arg1	TSAP6					791:795	TSAP6	791:795	TSAP6	791:795	In addition, mass spectrometry and mutagenesis analyses both indicated that the major cleavage site laid in the C-terminal of the third transmembrane domain of TSAP6.
22624035	5	58	theme	TSAP6	791:795	arg1	domain					781:786	the third transmembrane domain	757:786	the third transmembrane domain of TSAP6	757:795	In addition, mass spectrometry and mutagenesis analyses both indicated that the major cleavage site laid in the C-terminal of the third transmembrane domain of TSAP6.
22624035	2	59	theme	tumor	349:353	arg1	pathway-6					376:384	tumor suppressor activated pathway-6	349:384	tumor suppressor activated pathway-6 (TSAP6)	349:392	In this study, we identified a multi-pass transmembrane protein, tumor suppressor activated pathway-6 (TSAP6) as a potential substrate of RHBDD1.
22624035	2	59	theme	tumor	349:353	arg1	protein					340:346	a multi-pass transmembrane protein	313:346	a multi-pass transmembrane protein	313:346	In this study, we identified a multi-pass transmembrane protein, tumor suppressor activated pathway-6 (TSAP6) as a potential substrate of RHBDD1.
22624035	2	59	theme	tumor	349:353	arg1	TSAP6					387:391	TSAP6	387:391	TSAP6	387:391	In this study, we identified a multi-pass transmembrane protein, tumor suppressor activated pathway-6 (TSAP6) as a potential substrate of RHBDD1.
22624035	8	60	theme	certain	1092:1098	arg1	components					1109:1118	certain exosomal components	1092:1118	certain exosomal components	1092:1118	The increased exosome secretion was verfied through the detection of certain exosomal components, including Tsg101, Tf-R, FasL and Trail.
22624035	8	60	theme	certain	1092:1098	arg1	Tsg101					1131:1136	Tsg101	1131:1136	Tsg101	1131:1136	The increased exosome secretion was verfied through the detection of certain exosomal components, including Tsg101, Tf-R, FasL and Trail.
22624035	8	60	theme	certain	1092:1098	arg1	Trail					1154:1158	Trail	1154:1158	Trail	1154:1158	The increased exosome secretion was verfied through the detection of certain exosomal components, including Tsg101, Tf-R, FasL and Trail.
22624035	8	60	theme	certain	1092:1098	arg1	FasL					1145:1148	FasL	1145:1148	FasL	1145:1148	The increased exosome secretion was verfied through the detection of certain exosomal components, including Tsg101, Tf-R, FasL and Trail.
22624035	8	60	theme	certain	1092:1098	arg1	Tf-R					1139:1142	Tf-R	1139:1142	Tf-R	1139:1142	The increased exosome secretion was verfied through the detection of certain exosomal components, including Tsg101, Tf-R, FasL and Trail.
22624035	11	61	theme	secretion	1585:1593	arg1	pathway					1595:1601	a nonclassical exosomal secretion pathway	1561:1601	a nonclassical exosomal secretion pathway through the restriction of TSAP6	1561:1634	Taken together, our findings suggest that RHBDD1 is involved in the regulation of a nonclassical exosomal secretion pathway through the restriction of TSAP6.
22624035	0	62	theme	transmembrane	27:39	arg1	TSAP6					49:53	Exosome-related multi-pass transmembrane protein TSAP6	0:53	Exosome-related multi-pass transmembrane protein TSAP6	0:53	Exosome-related multi-pass transmembrane protein TSAP6 is a target of rhomboid protease RHBDD1-induced proteolysis.
22624035	0	62	theme	transmembrane	27:39	arg1	target					60:65	a target	58:65	a target of rhomboid protease RHBDD1-induced proteolysis	58:113	Exosome-related multi-pass transmembrane protein TSAP6 is a target of rhomboid protease RHBDD1-induced proteolysis.
22624035	0	63	theme	multi-pass	16:25	arg1	TSAP6					49:53	Exosome-related multi-pass transmembrane protein TSAP6	0:53	Exosome-related multi-pass transmembrane protein TSAP6	0:53	Exosome-related multi-pass transmembrane protein TSAP6 is a target of rhomboid protease RHBDD1-induced proteolysis.
22624035	0	63	theme	multi-pass	16:25	arg1	target					60:65	a target	58:65	a target of rhomboid protease RHBDD1-induced proteolysis	58:113	Exosome-related multi-pass transmembrane protein TSAP6 is a target of rhomboid protease RHBDD1-induced proteolysis.
22624035	4	64	theme	glycosylated	572:583	arg1	form					585:588	its glycosylated form	568:588	its glycosylated form	568:588	The cleavage of TSAP6 was not restricted to its glycosylated form and occurred in three different regions.
12839991	0	0	theme	related	75:81	arg1	proteins					83:90	related proteins	75:90	related proteins	75:90	Structure and axon outgrowth inhibitor binding of the Nogo-66 receptor and related proteins.
12839991	7	1	theme	NgR	1131:1133	arg1	residues					1143:1150	NgR surface residues	1131:1150	NgR surface residues not conserved in NgR2 and NgR3	1131:1181	The NgR structure analysis, as well as a comparison of NgR surface residues not conserved in NgR2 and NgR3, identifies potential protein interaction sites important in the assembly of a functional signaling complex.
12839991	3	2	theme	cell-surface	495:506	arg1	NgR					508:510	cell-surface NgR	495:510	cell-surface NgR	495:510	By deletion analysis, we show that the binding of soluble fragments of Nogo, MAG and NgR to cell-surface NgR requires the entire leucine-rich repeat (LRR) region of NgR, but not other portions of the protein.
12839991	7	3	theme	surface	1135:1141	arg1	residues					1143:1150	NgR surface residues	1131:1150	NgR surface residues not conserved in NgR2 and NgR3	1131:1181	The NgR structure analysis, as well as a comparison of NgR surface residues not conserved in NgR2 and NgR3, identifies potential protein interaction sites important in the assembly of a functional signaling complex.
12839991	1	4	theme	axonal	146:151	arg1	regeneration					153:164	axonal regeneration	146:164	axonal regeneration after injury of the spinal cord and brain	146:206	The myelin-derived proteins Nogo, MAG and OMgp limit axonal regeneration after injury of the spinal cord and brain.
12839991	5	5	theme	NgR	924:926	arg1	ectodomain					910:919	the biologically active ligand-binding soluble ectodomain	863:919	the biologically active ligand-binding soluble ectodomain of NgR	863:926	To investigate NgR specificity and multi-ligand binding, we determined the crystal structure of the biologically active ligand-binding soluble ectodomain of NgR.
12839991	5	5	theme	NgR	924:926	arg1	NgR					924:926	NgR	924:926	NgR	924:926	To investigate NgR specificity and multi-ligand binding, we determined the crystal structure of the biologically active ligand-binding soluble ectodomain of NgR.
12839991	6	6	theme	N-terminal	1027:1036	arg1	cap					1038:1040	an N-terminal cap	1024:1040	an N-terminal cap	1024:1040	The molecule is banana shaped with elongation and curvature arising from eight LRRs flanked by an N-terminal cap and a small C-terminal subdomain.
12839991	7	7	theme	complex	1283:1289	arg1	assembly					1248:1255	the assembly	1244:1255	the assembly of a functional signaling complex	1244:1289	The NgR structure analysis, as well as a comparison of NgR surface residues not conserved in NgR2 and NgR3, identifies potential protein interaction sites important in the assembly of a functional signaling complex.
12839991	3	8	theme	repeat	545:550	arg1	region					558:563	the entire leucine-rich repeat (LRR) region	521:563	the entire leucine-rich repeat (LRR) region of NgR	521:570	By deletion analysis, we show that the binding of soluble fragments of Nogo, MAG and NgR to cell-surface NgR requires the entire leucine-rich repeat (LRR) region of NgR, but not other portions of the protein.
12839991	5	9	theme	ligand-binding	887:900	arg1	ectodomain					910:919	the biologically active ligand-binding soluble ectodomain	863:919	the biologically active ligand-binding soluble ectodomain of NgR	863:926	To investigate NgR specificity and multi-ligand binding, we determined the crystal structure of the biologically active ligand-binding soluble ectodomain of NgR.
12839991	5	9	theme	ligand-binding	887:900	arg1	NgR					924:926	NgR	924:926	NgR	924:926	To investigate NgR specificity and multi-ligand binding, we determined the crystal structure of the biologically active ligand-binding soluble ectodomain of NgR.
12839991	0	10	theme	proteins	83:90	arg1	Structure					0:8	Structure	0:8	Structure	0:8	Structure and axon outgrowth inhibitor binding of the Nogo-66 receptor and related proteins.
12839991	0	10	theme	proteins	83:90	arg1	outgrowth					19:27	axon outgrowth	14:27	axon outgrowth	14:27	Structure and axon outgrowth inhibitor binding of the Nogo-66 receptor and related proteins.
12839991	5	11	theme	ectodomain	910:919	arg1	structure					850:858	the crystal structure	838:858	the crystal structure of the biologically active ligand-binding soluble ectodomain of NgR	838:926	To investigate NgR specificity and multi-ligand binding, we determined the crystal structure of the biologically active ligand-binding soluble ectodomain of NgR.
12839991	4	12	theme	related	672:678	arg1	NgR3					699:702	NgR3	699:702	NgR3	699:702	Despite sharing extensive sequence similarity with NgR, two related proteins, NgR2 and NgR3, which we have identified, do not bind Nogo, MAG, OMgp or NgR.
12839991	4	12	theme	related	672:678	arg1	NgR2					690:693	NgR2	690:693	NgR2	690:693	Despite sharing extensive sequence similarity with NgR, two related proteins, NgR2 and NgR3, which we have identified, do not bind Nogo, MAG, OMgp or NgR.
12839991	4	12	theme	related	672:678	arg1	proteins					680:687	two related proteins	668:687	two related proteins	668:687	Despite sharing extensive sequence similarity with NgR, two related proteins, NgR2 and NgR3, which we have identified, do not bind Nogo, MAG, OMgp or NgR.
12839991	5	13	theme	NgR	782:784	arg1	specificity					786:796	NgR specificity	782:796	NgR specificity	782:796	To investigate NgR specificity and multi-ligand binding, we determined the crystal structure of the biologically active ligand-binding soluble ectodomain of NgR.
12839991	3	14	theme	NgR	488:490	arg1	fragments					461:469	soluble fragments	453:469	soluble fragments of Nogo, MAG and NgR	453:490	By deletion analysis, we show that the binding of soluble fragments of Nogo, MAG and NgR to cell-surface NgR requires the entire leucine-rich repeat (LRR) region of NgR, but not other portions of the protein.
12839991	7	15	theme	important	1231:1239	arg1	sites					1225:1229	potential protein interaction sites	1195:1229	potential protein interaction sites important in the assembly of a functional signaling complex	1195:1289	The NgR structure analysis, as well as a comparison of NgR surface residues not conserved in NgR2 and NgR3, identifies potential protein interaction sites important in the assembly of a functional signaling complex.
12839991	1	16	dep	proteins	112:119	arg1	OMgp					135:138	OMgp	135:138	OMgp	135:138	The myelin-derived proteins Nogo, MAG and OMgp limit axonal regeneration after injury of the spinal cord and brain.
12839991	1	16	dep	proteins	112:119	arg1	proteins					112:119	The myelin-derived proteins	93:119	The myelin-derived proteins Nogo, MAG and OMgp	93:138	The myelin-derived proteins Nogo, MAG and OMgp limit axonal regeneration after injury of the spinal cord and brain.
12839991	1	16	dep	proteins	112:119	arg1	MAG					127:129	MAG	127:129	MAG	127:129	The myelin-derived proteins Nogo, MAG and OMgp limit axonal regeneration after injury of the spinal cord and brain.
12839991	1	16	dep	proteins	112:119	arg1	Nogo					121:124	Nogo	121:124	Nogo	121:124	The myelin-derived proteins Nogo, MAG and OMgp limit axonal regeneration after injury of the spinal cord and brain.
12839991	4	17	theme	sequence	638:645	arg1	similarity					647:656	extensive sequence similarity	628:656	extensive sequence similarity with NgR	628:665	Despite sharing extensive sequence similarity with NgR, two related proteins, NgR2 and NgR3, which we have identified, do not bind Nogo, MAG, OMgp or NgR.
12839991	2	18	theme	neuronal	266:273	arg1	receptors					275:283	multi-subunit neuronal receptors	252:283	multi-subunit neuronal receptors that contain a common ligand-binding glycosylphosphatidylinositol-anchored subunit termed the Nogo-66 receptor (NgR)	252:400	These cell-surface proteins signal through multi-subunit neuronal receptors that contain a common ligand-binding glycosylphosphatidylinositol-anchored subunit termed the Nogo-66 receptor (NgR).
12839991	3	19	theme	soluble	453:459	arg1	fragments					461:469	soluble fragments	453:469	soluble fragments of Nogo, MAG and NgR	453:490	By deletion analysis, we show that the binding of soluble fragments of Nogo, MAG and NgR to cell-surface NgR requires the entire leucine-rich repeat (LRR) region of NgR, but not other portions of the protein.
12839991	3	20	theme	deletion	406:413	arg1	analysis					415:422	deletion analysis	406:422	deletion analysis	406:422	By deletion analysis, we show that the binding of soluble fragments of Nogo, MAG and NgR to cell-surface NgR requires the entire leucine-rich repeat (LRR) region of NgR, but not other portions of the protein.
12839991	7	21	theme	protein	1205:1211	arg1	sites					1225:1229	potential protein interaction sites	1195:1229	potential protein interaction sites important in the assembly of a functional signaling complex	1195:1289	The NgR structure analysis, as well as a comparison of NgR surface residues not conserved in NgR2 and NgR3, identifies potential protein interaction sites important in the assembly of a functional signaling complex.
12839991	7	22	theme	residues	1143:1150	arg1	comparison					1117:1126	a comparison	1115:1126	a comparison of NgR surface residues not conserved in NgR2 and NgR3	1115:1181	The NgR structure analysis, as well as a comparison of NgR surface residues not conserved in NgR2 and NgR3, identifies potential protein interaction sites important in the assembly of a functional signaling complex.
12839991	7	22	theme	residues	1143:1150	arg1	analysis					1094:1101	The NgR structure analysis	1076:1101	The NgR structure analysis	1076:1101	The NgR structure analysis, as well as a comparison of NgR surface residues not conserved in NgR2 and NgR3, identifies potential protein interaction sites important in the assembly of a functional signaling complex.
12839991	2	23	theme	glycosylphosphatidylinositol-anchored	322:358	arg1	subunit					360:366	a common ligand-binding glycosylphosphatidylinositol-anchored subunit	298:366	a common ligand-binding glycosylphosphatidylinositol-anchored subunit termed the Nogo-66 receptor (NgR)	298:400	These cell-surface proteins signal through multi-subunit neuronal receptors that contain a common ligand-binding glycosylphosphatidylinositol-anchored subunit termed the Nogo-66 receptor (NgR).
12839991	6	24	theme	C-terminal	1054:1063	arg1	subdomain					1065:1073	a small C-terminal subdomain	1046:1073	a small C-terminal subdomain	1046:1073	The molecule is banana shaped with elongation and curvature arising from eight LRRs flanked by an N-terminal cap and a small C-terminal subdomain.
12839991	2	25	theme	ligand-binding	307:320	arg1	subunit					360:366	a common ligand-binding glycosylphosphatidylinositol-anchored subunit	298:366	a common ligand-binding glycosylphosphatidylinositol-anchored subunit termed the Nogo-66 receptor (NgR)	298:400	These cell-surface proteins signal through multi-subunit neuronal receptors that contain a common ligand-binding glycosylphosphatidylinositol-anchored subunit termed the Nogo-66 receptor (NgR).
12839991	4	26	with	similarity	647:656	arg1	NgR					663:665	NgR	663:665	NgR	663:665	Despite sharing extensive sequence similarity with NgR, two related proteins, NgR2 and NgR3, which we have identified, do not bind Nogo, MAG, OMgp or NgR.
12839991	2	27	theme	common	300:305	arg1	subunit					360:366	a common ligand-binding glycosylphosphatidylinositol-anchored subunit	298:366	a common ligand-binding glycosylphosphatidylinositol-anchored subunit termed the Nogo-66 receptor (NgR)	298:400	These cell-surface proteins signal through multi-subunit neuronal receptors that contain a common ligand-binding glycosylphosphatidylinositol-anchored subunit termed the Nogo-66 receptor (NgR).
12839991	6	28	with	shaped	952:957	arg1	curvature					979:987	curvature	979:987	curvature	979:987	The molecule is banana shaped with elongation and curvature arising from eight LRRs flanked by an N-terminal cap and a small C-terminal subdomain.
12839991	6	28	with	shaped	952:957	arg1	elongation					964:973	elongation	964:973	elongation	964:973	The molecule is banana shaped with elongation and curvature arising from eight LRRs flanked by an N-terminal cap and a small C-terminal subdomain.
12839991	3	29	theme	Nogo	474:477	arg1	fragments					461:469	soluble fragments	453:469	soluble fragments of Nogo, MAG and NgR	453:490	By deletion analysis, we show that the binding of soluble fragments of Nogo, MAG and NgR to cell-surface NgR requires the entire leucine-rich repeat (LRR) region of NgR, but not other portions of the protein.
12839991	0	30	theme	axon	14:17	arg1	outgrowth					19:27	axon outgrowth	14:27	axon outgrowth	14:27	Structure and axon outgrowth inhibitor binding of the Nogo-66 receptor and related proteins.
12839991	3	31	theme	entire	525:530	arg1	region					558:563	the entire leucine-rich repeat (LRR) region	521:563	the entire leucine-rich repeat (LRR) region of NgR	521:570	By deletion analysis, we show that the binding of soluble fragments of Nogo, MAG and NgR to cell-surface NgR requires the entire leucine-rich repeat (LRR) region of NgR, but not other portions of the protein.
12839991	1	32	theme	myelin-derived	97:110	arg1	OMgp					135:138	OMgp	135:138	OMgp	135:138	The myelin-derived proteins Nogo, MAG and OMgp limit axonal regeneration after injury of the spinal cord and brain.
12839991	1	32	theme	myelin-derived	97:110	arg1	proteins					112:119	The myelin-derived proteins	93:119	The myelin-derived proteins Nogo, MAG and OMgp	93:138	The myelin-derived proteins Nogo, MAG and OMgp limit axonal regeneration after injury of the spinal cord and brain.
12839991	1	32	theme	myelin-derived	97:110	arg1	MAG					127:129	MAG	127:129	MAG	127:129	The myelin-derived proteins Nogo, MAG and OMgp limit axonal regeneration after injury of the spinal cord and brain.
12839991	1	32	theme	myelin-derived	97:110	arg1	Nogo					121:124	Nogo	121:124	Nogo	121:124	The myelin-derived proteins Nogo, MAG and OMgp limit axonal regeneration after injury of the spinal cord and brain.
12839991	1	33	theme	spinal	186:191	arg1	cord					193:196	the spinal cord	182:196	the spinal cord	182:196	The myelin-derived proteins Nogo, MAG and OMgp limit axonal regeneration after injury of the spinal cord and brain.
12839991	7	34	theme	NgR	1080:1082	arg1	analysis					1094:1101	The NgR structure analysis	1076:1101	The NgR structure analysis	1076:1101	The NgR structure analysis, as well as a comparison of NgR surface residues not conserved in NgR2 and NgR3, identifies potential protein interaction sites important in the assembly of a functional signaling complex.
12839991	2	35	contain	contain	290:296	arg2	subunit					360:366	a common ligand-binding glycosylphosphatidylinositol-anchored subunit	298:366	a common ligand-binding glycosylphosphatidylinositol-anchored subunit termed the Nogo-66 receptor (NgR)	298:400	These cell-surface proteins signal through multi-subunit neuronal receptors that contain a common ligand-binding glycosylphosphatidylinositol-anchored subunit termed the Nogo-66 receptor (NgR).
12839991	2	35	contain	contain	290:296	arg1	receptors					275:283	multi-subunit neuronal receptors	252:283	multi-subunit neuronal receptors that contain a common ligand-binding glycosylphosphatidylinositol-anchored subunit termed the Nogo-66 receptor (NgR)	252:400	These cell-surface proteins signal through multi-subunit neuronal receptors that contain a common ligand-binding glycosylphosphatidylinositol-anchored subunit termed the Nogo-66 receptor (NgR).
12839991	3	36	theme	fragments	461:469	arg1	binding					442:448	the binding	438:448	the binding of soluble fragments of Nogo, MAG and NgR to cell-surface NgR	438:510	By deletion analysis, we show that the binding of soluble fragments of Nogo, MAG and NgR to cell-surface NgR requires the entire leucine-rich repeat (LRR) region of NgR, but not other portions of the protein.
12839991	2	37	theme	cell-surface	215:226	arg1	proteins					228:235	These cell-surface proteins	209:235	These cell-surface proteins	209:235	These cell-surface proteins signal through multi-subunit neuronal receptors that contain a common ligand-binding glycosylphosphatidylinositol-anchored subunit termed the Nogo-66 receptor (NgR).
12839991	5	38	theme	multi-ligand	802:813	arg1	binding					815:821	multi-ligand binding	802:821	multi-ligand binding	802:821	To investigate NgR specificity and multi-ligand binding, we determined the crystal structure of the biologically active ligand-binding soluble ectodomain of NgR.
12839991	1	39	theme	cord	193:196	arg1	regeneration					153:164	axonal regeneration	146:164	axonal regeneration after injury of the spinal cord and brain	146:206	The myelin-derived proteins Nogo, MAG and OMgp limit axonal regeneration after injury of the spinal cord and brain.
12839991	0	40	theme	inhibitor	29:37	arg1	binding					39:45	inhibitor binding	29:45	inhibitor binding	29:45	Structure and axon outgrowth inhibitor binding of the Nogo-66 receptor and related proteins.
12839991	7	41	theme	structure	1084:1092	arg1	analysis					1094:1101	The NgR structure analysis	1076:1101	The NgR structure analysis	1076:1101	The NgR structure analysis, as well as a comparison of NgR surface residues not conserved in NgR2 and NgR3, identifies potential protein interaction sites important in the assembly of a functional signaling complex.
12839991	3	42	theme	protein	603:609	arg1	portions					587:594	other portions	581:594	other portions of the protein	581:609	By deletion analysis, we show that the binding of soluble fragments of Nogo, MAG and NgR to cell-surface NgR requires the entire leucine-rich repeat (LRR) region of NgR, but not other portions of the protein.
12839991	7	43	theme	interaction	1213:1223	arg1	sites					1225:1229	potential protein interaction sites	1195:1229	potential protein interaction sites important in the assembly of a functional signaling complex	1195:1289	The NgR structure analysis, as well as a comparison of NgR surface residues not conserved in NgR2 and NgR3, identifies potential protein interaction sites important in the assembly of a functional signaling complex.
12839991	0	44	theme	Nogo-66	54:60	arg1	receptor					62:69	Nogo-66 receptor	54:69	Nogo-66 receptor	54:69	Structure and axon outgrowth inhibitor binding of the Nogo-66 receptor and related proteins.
12839991	3	45	theme	NgR	568:570	arg1	region					558:563	the entire leucine-rich repeat (LRR) region	521:563	the entire leucine-rich repeat (LRR) region of NgR	521:570	By deletion analysis, we show that the binding of soluble fragments of Nogo, MAG and NgR to cell-surface NgR requires the entire leucine-rich repeat (LRR) region of NgR, but not other portions of the protein.
12839991	2	46	theme	Nogo-66	379:385	arg1	NgR					397:399	NgR	397:399	NgR	397:399	These cell-surface proteins signal through multi-subunit neuronal receptors that contain a common ligand-binding glycosylphosphatidylinositol-anchored subunit termed the Nogo-66 receptor (NgR).
12839991	2	46	theme	Nogo-66	379:385	arg1	receptor					387:394	Nogo-66 receptor	379:394	the Nogo-66 receptor (NgR)	375:400	These cell-surface proteins signal through multi-subunit neuronal receptors that contain a common ligand-binding glycosylphosphatidylinositol-anchored subunit termed the Nogo-66 receptor (NgR).
12839991	5	47	theme	active	880:885	arg1	ectodomain					910:919	the biologically active ligand-binding soluble ectodomain	863:919	the biologically active ligand-binding soluble ectodomain of NgR	863:926	To investigate NgR specificity and multi-ligand binding, we determined the crystal structure of the biologically active ligand-binding soluble ectodomain of NgR.
12839991	5	47	theme	active	880:885	arg1	NgR					924:926	NgR	924:926	NgR	924:926	To investigate NgR specificity and multi-ligand binding, we determined the crystal structure of the biologically active ligand-binding soluble ectodomain of NgR.
12839991	5	48	theme	crystal	842:848	arg1	structure					850:858	the crystal structure	838:858	the crystal structure of the biologically active ligand-binding soluble ectodomain of NgR	838:926	To investigate NgR specificity and multi-ligand binding, we determined the crystal structure of the biologically active ligand-binding soluble ectodomain of NgR.
12839991	7	49	theme	functional	1262:1271	arg1	complex					1283:1289	a functional signaling complex	1260:1289	a functional signaling complex	1260:1289	The NgR structure analysis, as well as a comparison of NgR surface residues not conserved in NgR2 and NgR3, identifies potential protein interaction sites important in the assembly of a functional signaling complex.
12839991	7	50	theme	signaling	1273:1281	arg1	complex					1283:1289	a functional signaling complex	1260:1289	a functional signaling complex	1260:1289	The NgR structure analysis, as well as a comparison of NgR surface residues not conserved in NgR2 and NgR3, identifies potential protein interaction sites important in the assembly of a functional signaling complex.
12839991	2	51	theme	multi-subunit	252:264	arg1	receptors					275:283	multi-subunit neuronal receptors	252:283	multi-subunit neuronal receptors that contain a common ligand-binding glycosylphosphatidylinositol-anchored subunit termed the Nogo-66 receptor (NgR)	252:400	These cell-surface proteins signal through multi-subunit neuronal receptors that contain a common ligand-binding glycosylphosphatidylinositol-anchored subunit termed the Nogo-66 receptor (NgR).
12839991	7	52	from	important	1231:1239	arg1	assembly					1248:1255	the assembly	1244:1255	the assembly of a functional signaling complex	1244:1289	The NgR structure analysis, as well as a comparison of NgR surface residues not conserved in NgR2 and NgR3, identifies potential protein interaction sites important in the assembly of a functional signaling complex.
12839991	3	53	theme	MAG	480:482	arg1	fragments					461:469	soluble fragments	453:469	soluble fragments of Nogo, MAG and NgR	453:490	By deletion analysis, we show that the binding of soluble fragments of Nogo, MAG and NgR to cell-surface NgR requires the entire leucine-rich repeat (LRR) region of NgR, but not other portions of the protein.
12839991	0	54	dep	receptor	62:69	arg1	the					50:52	the	50:52	the	50:52	Structure and axon outgrowth inhibitor binding of the Nogo-66 receptor and related proteins.
12839991	1	55	theme	brain	202:206	arg1	regeneration					153:164	axonal regeneration	146:164	axonal regeneration after injury of the spinal cord and brain	146:206	The myelin-derived proteins Nogo, MAG and OMgp limit axonal regeneration after injury of the spinal cord and brain.
12839991	3	56	theme	leucine-rich	532:543	arg1	repeat					545:550	leucine-rich repeat	532:550	the entire leucine-rich repeat (LRR) region of NgR	521:570	By deletion analysis, we show that the binding of soluble fragments of Nogo, MAG and NgR to cell-surface NgR requires the entire leucine-rich repeat (LRR) region of NgR, but not other portions of the protein.
12839991	3	56	theme	leucine-rich	532:543	arg1	LRR					553:555	LRR	553:555	LRR	553:555	By deletion analysis, we show that the binding of soluble fragments of Nogo, MAG and NgR to cell-surface NgR requires the entire leucine-rich repeat (LRR) region of NgR, but not other portions of the protein.
12839991	7	57	theme	potential	1195:1203	arg1	sites					1225:1229	potential protein interaction sites	1195:1229	potential protein interaction sites important in the assembly of a functional signaling complex	1195:1289	The NgR structure analysis, as well as a comparison of NgR surface residues not conserved in NgR2 and NgR3, identifies potential protein interaction sites important in the assembly of a functional signaling complex.
12839991	5	58	theme	soluble	902:908	arg1	ectodomain					910:919	the biologically active ligand-binding soluble ectodomain	863:919	the biologically active ligand-binding soluble ectodomain of NgR	863:926	To investigate NgR specificity and multi-ligand binding, we determined the crystal structure of the biologically active ligand-binding soluble ectodomain of NgR.
12839991	5	58	theme	soluble	902:908	arg1	NgR					924:926	NgR	924:926	NgR	924:926	To investigate NgR specificity and multi-ligand binding, we determined the crystal structure of the biologically active ligand-binding soluble ectodomain of NgR.
12839991	6	59	theme	small	1048:1052	arg1	subdomain					1065:1073	a small C-terminal subdomain	1046:1073	a small C-terminal subdomain	1046:1073	The molecule is banana shaped with elongation and curvature arising from eight LRRs flanked by an N-terminal cap and a small C-terminal subdomain.
12839991	0	60	theme	receptor	62:69	arg1	Structure					0:8	Structure	0:8	Structure	0:8	Structure and axon outgrowth inhibitor binding of the Nogo-66 receptor and related proteins.
12839991	0	60	theme	receptor	62:69	arg1	outgrowth					19:27	axon outgrowth	14:27	axon outgrowth	14:27	Structure and axon outgrowth inhibitor binding of the Nogo-66 receptor and related proteins.
12839991	3	61	theme	other	581:585	arg1	portions					587:594	other portions	581:594	other portions of the protein	581:609	By deletion analysis, we show that the binding of soluble fragments of Nogo, MAG and NgR to cell-surface NgR requires the entire leucine-rich repeat (LRR) region of NgR, but not other portions of the protein.
12839991	4	62	theme	extensive	628:636	arg1	similarity					647:656	extensive sequence similarity	628:656	extensive sequence similarity with NgR	628:665	Despite sharing extensive sequence similarity with NgR, two related proteins, NgR2 and NgR3, which we have identified, do not bind Nogo, MAG, OMgp or NgR.
12839991	1	63	link	myelin-derived	97:110	arg1	OMgp					135:138	OMgp	135:138	OMgp	135:138	The myelin-derived proteins Nogo, MAG and OMgp limit axonal regeneration after injury of the spinal cord and brain.
12839991	1	63	link	myelin-derived	97:110	arg1	proteins					112:119	The myelin-derived proteins	93:119	The myelin-derived proteins Nogo, MAG and OMgp	93:138	The myelin-derived proteins Nogo, MAG and OMgp limit axonal regeneration after injury of the spinal cord and brain.
12839991	1	63	link	myelin-derived	97:110	arg1	MAG					127:129	MAG	127:129	MAG	127:129	The myelin-derived proteins Nogo, MAG and OMgp limit axonal regeneration after injury of the spinal cord and brain.
12839991	1	63	link	myelin-derived	97:110	arg1	Nogo					121:124	Nogo	121:124	Nogo	121:124	The myelin-derived proteins Nogo, MAG and OMgp limit axonal regeneration after injury of the spinal cord and brain.
12839991	0	64	dep	Structure	0:8	arg1	binding					39:45	inhibitor binding	29:45	inhibitor binding	29:45	Structure and axon outgrowth inhibitor binding of the Nogo-66 receptor and related proteins.
12839991	7	65	from	assembly	1248:1255	arg1	important					1231:1239	important	1231:1239	important	1231:1239	The NgR structure analysis, as well as a comparison of NgR surface residues not conserved in NgR2 and NgR3, identifies potential protein interaction sites important in the assembly of a functional signaling complex.
12718853	1	0	theme	mammalian	139:147	arg1	CNS					173:175	CNS	173:175	CNS	173:175	Failure of axon regeneration in the adult mammalian central nervous system (CNS) is at least partly due to inhibitory molecules associated with myelin.
12718853	1	0	theme	mammalian	139:147	arg1	system					165:170	the adult mammalian central nervous system	129:170	the adult mammalian central nervous system (CNS)	129:176	Failure of axon regeneration in the adult mammalian central nervous system (CNS) is at least partly due to inhibitory molecules associated with myelin.
12718853	2	1	theme	inhibitory	433:442	arg1	ligands					444:450	myelin-associated inhibitory ligands	415:450	myelin-associated inhibitory ligands	415:450	Recent studies suggest that an axon surface protein, the Nogo receptor (NgR), may play a role in this process through an unprecedented degree of crossreactivity with myelin-associated inhibitory ligands.
12718853	5	2	from	base	847:850	arg1	cleft					823:827	A deep cleft	816:827	A deep cleft at the C-terminal base of the LRR	816:861	A deep cleft at the C-terminal base of the LRR may play a role in NgR association with the p75 coreceptor.
12718853	1	3	theme	central	149:155	arg1	CNS					173:175	CNS	173:175	CNS	173:175	Failure of axon regeneration in the adult mammalian central nervous system (CNS) is at least partly due to inhibitory molecules associated with myelin.
12718853	1	3	theme	central	149:155	arg1	system					165:170	the adult mammalian central nervous system	129:170	the adult mammalian central nervous system (CNS)	129:176	Failure of axon regeneration in the adult mammalian central nervous system (CNS) is at least partly due to inhibitory molecules associated with myelin.
12718853	5	4	theme	p75	907:909	arg1	coreceptor					911:920	the p75 coreceptor	903:920	the p75 coreceptor	903:920	A deep cleft at the C-terminal base of the LRR may play a role in NgR association with the p75 coreceptor.
12718853	3	5	theme	crystal	479:485	arg1	structure					487:495	1.5 A crystal structure	473:495	1.5 A crystal structure	473:495	Here, we report the 1.5 A crystal structure and functional characterization of a soluble extracellular domain of the human Nogo receptor.
12718853	4	6	theme	broad	689:693	arg1	region					695:700	a broad region	687:700	a broad region of evolutionarily conserved patches of aromatic residues, possibly suggestive of degenerate ligand binding sites	687:813	Nogo receptor adopts a leucine-rich repeat (LRR) module whose concave exterior surface contains a broad region of evolutionarily conserved patches of aromatic residues, possibly suggestive of degenerate ligand binding sites.
12718853	0	7	theme	myelin	78:83	arg1	inhibition					85:94	myelin inhibition	78:94	myelin inhibition	78:94	Structure of the Nogo receptor ectodomain: a recognition module implicated in myelin inhibition.
12718853	6	8	theme	physiological	1032:1044	arg1	relevance					1046:1054	the physiological relevance	1028:1054	the physiological relevance of NgR-mediated protein-protein interactions to axon regeneration inhibition	1028:1131	These results now provide a detailed framework for focused structure-function studies aimed at assessing the physiological relevance of NgR-mediated protein-protein interactions to axon regeneration inhibition.
12718853	4	9	theme	exterior	661:668	arg1	surface					670:676	concave exterior surface	653:676	concave exterior surface	653:676	Nogo receptor adopts a leucine-rich repeat (LRR) module whose concave exterior surface contains a broad region of evolutionarily conserved patches of aromatic residues, possibly suggestive of degenerate ligand binding sites.
12718853	4	10	theme	concave	653:659	arg1	surface					670:676	concave exterior surface	653:676	concave exterior surface	653:676	Nogo receptor adopts a leucine-rich repeat (LRR) module whose concave exterior surface contains a broad region of evolutionarily conserved patches of aromatic residues, possibly suggestive of degenerate ligand binding sites.
12718853	4	11	theme	binding	801:807	arg1	sites					809:813	degenerate ligand binding sites	783:813	degenerate ligand binding sites	783:813	Nogo receptor adopts a leucine-rich repeat (LRR) module whose concave exterior surface contains a broad region of evolutionarily conserved patches of aromatic residues, possibly suggestive of degenerate ligand binding sites.
12718853	2	12	theme	Recent	249:254	arg1	studies					256:262	Recent studies	249:262	Recent studies	249:262	Recent studies suggest that an axon surface protein, the Nogo receptor (NgR), may play a role in this process through an unprecedented degree of crossreactivity with myelin-associated inhibitory ligands.
12718853	1	13	theme	nervous	157:163	arg1	CNS					173:175	CNS	173:175	CNS	173:175	Failure of axon regeneration in the adult mammalian central nervous system (CNS) is at least partly due to inhibitory molecules associated with myelin.
12718853	1	13	theme	nervous	157:163	arg1	system					165:170	the adult mammalian central nervous system	129:170	the adult mammalian central nervous system (CNS)	129:176	Failure of axon regeneration in the adult mammalian central nervous system (CNS) is at least partly due to inhibitory molecules associated with myelin.
12718853	0	14	theme	ectodomain	31:40	arg1	Structure					0:8	Structure	0:8	Structure of the Nogo receptor ectodomain: a recognition module implicated in myelin inhibition.	0:95	Structure of the Nogo receptor ectodomain: a recognition module implicated in myelin inhibition.
12718853	3	15	theme	A	477:477	arg1	structure					487:495	1.5 A crystal structure	473:495	1.5 A crystal structure	473:495	Here, we report the 1.5 A crystal structure and functional characterization of a soluble extracellular domain of the human Nogo receptor.
12718853	5	16	theme	deep	818:821	arg1	cleft					823:827	A deep cleft	816:827	A deep cleft at the C-terminal base of the LRR	816:861	A deep cleft at the C-terminal base of the LRR may play a role in NgR association with the p75 coreceptor.
12718853	2	17	theme	surface	285:291	arg1	protein					293:299	an axon surface protein	277:299	an axon surface protein	277:299	Recent studies suggest that an axon surface protein, the Nogo receptor (NgR), may play a role in this process through an unprecedented degree of crossreactivity with myelin-associated inhibitory ligands.
12718853	2	17	theme	surface	285:291	arg1	receptor					311:318	Nogo receptor	306:318	the Nogo receptor (NgR)	302:324	Recent studies suggest that an axon surface protein, the Nogo receptor (NgR), may play a role in this process through an unprecedented degree of crossreactivity with myelin-associated inhibitory ligands.
12718853	4	18	theme	repeat	627:632	arg1	module					640:645	a leucine-rich repeat (LRR) module	612:645	a leucine-rich repeat (LRR) module whose concave exterior surface contains a broad region of evolutionarily conserved patches of aromatic residues, possibly suggestive of degenerate ligand binding sites	612:813	Nogo receptor adopts a leucine-rich repeat (LRR) module whose concave exterior surface contains a broad region of evolutionarily conserved patches of aromatic residues, possibly suggestive of degenerate ligand binding sites.
12718853	2	19	theme	unprecedented	370:382	arg1	degree					384:389	an unprecedented degree	367:389	an unprecedented degree of crossreactivity with myelin-associated inhibitory ligands	367:450	Recent studies suggest that an axon surface protein, the Nogo receptor (NgR), may play a role in this process through an unprecedented degree of crossreactivity with myelin-associated inhibitory ligands.
12718853	4	20	theme	sites	809:813	arg1	suggestive					769:778	suggestive	769:778	suggestive	769:778	Nogo receptor adopts a leucine-rich repeat (LRR) module whose concave exterior surface contains a broad region of evolutionarily conserved patches of aromatic residues, possibly suggestive of degenerate ligand binding sites.
12718853	2	21	theme	axon	280:283	arg1	protein					293:299	an axon surface protein	277:299	an axon surface protein	277:299	Recent studies suggest that an axon surface protein, the Nogo receptor (NgR), may play a role in this process through an unprecedented degree of crossreactivity with myelin-associated inhibitory ligands.
12718853	2	21	theme	axon	280:283	arg1	receptor					311:318	Nogo receptor	306:318	the Nogo receptor (NgR)	302:324	Recent studies suggest that an axon surface protein, the Nogo receptor (NgR), may play a role in this process through an unprecedented degree of crossreactivity with myelin-associated inhibitory ligands.
12718853	4	22	theme	leucine-rich	614:625	arg1	LRR					635:637	LRR	635:637	LRR	635:637	Nogo receptor adopts a leucine-rich repeat (LRR) module whose concave exterior surface contains a broad region of evolutionarily conserved patches of aromatic residues, possibly suggestive of degenerate ligand binding sites.
12718853	4	22	theme	leucine-rich	614:625	arg1	repeat					627:632	a leucine-rich repeat	612:632	a leucine-rich repeat (LRR) module whose concave exterior surface contains a broad region of evolutionarily conserved patches of aromatic residues, possibly suggestive of degenerate ligand binding sites	612:813	Nogo receptor adopts a leucine-rich repeat (LRR) module whose concave exterior surface contains a broad region of evolutionarily conserved patches of aromatic residues, possibly suggestive of degenerate ligand binding sites.
12718853	0	23	theme	Nogo	17:20	arg1	ectodomain					31:40	the Nogo receptor ectodomain	13:40	the Nogo receptor ectodomain	13:40	Structure of the Nogo receptor ectodomain: a recognition module implicated in myelin inhibition.
12718853	6	24	theme	regeneration	1109:1120	arg1	inhibition					1122:1131	axon regeneration inhibition	1104:1131	axon regeneration inhibition	1104:1131	These results now provide a detailed framework for focused structure-function studies aimed at assessing the physiological relevance of NgR-mediated protein-protein interactions to axon regeneration inhibition.
12718853	4	25	theme	suggestive	769:778	arg1	patches					730:736	evolutionarily conserved patches	705:736	evolutionarily conserved patches	705:736	Nogo receptor adopts a leucine-rich repeat (LRR) module whose concave exterior surface contains a broad region of evolutionarily conserved patches of aromatic residues, possibly suggestive of degenerate ligand binding sites.
12718853	6	26	theme	structure-function	982:999	arg1	studies					1001:1007	focused structure-function studies	974:1007	focused structure-function studies aimed at assessing the physiological relevance of NgR-mediated protein-protein interactions to axon regeneration inhibition	974:1131	These results now provide a detailed framework for focused structure-function studies aimed at assessing the physiological relevance of NgR-mediated protein-protein interactions to axon regeneration inhibition.
12718853	6	27	theme	NgR-mediated	1059:1070	arg1	interactions					1088:1099	NgR-mediated protein-protein interactions	1059:1099	NgR-mediated protein-protein interactions	1059:1099	These results now provide a detailed framework for focused structure-function studies aimed at assessing the physiological relevance of NgR-mediated protein-protein interactions to axon regeneration inhibition.
12718853	4	28	contain	contains	678:685	arg2	region					695:700	a broad region	687:700	a broad region of evolutionarily conserved patches of aromatic residues, possibly suggestive of degenerate ligand binding sites	687:813	Nogo receptor adopts a leucine-rich repeat (LRR) module whose concave exterior surface contains a broad region of evolutionarily conserved patches of aromatic residues, possibly suggestive of degenerate ligand binding sites.
12718853	4	28	contain	contains	678:685	arg1	surface					670:676	concave exterior surface	653:676	concave exterior surface	653:676	Nogo receptor adopts a leucine-rich repeat (LRR) module whose concave exterior surface contains a broad region of evolutionarily conserved patches of aromatic residues, possibly suggestive of degenerate ligand binding sites.
12718853	4	29	theme	patches	730:736	arg1	region					695:700	a broad region	687:700	a broad region of evolutionarily conserved patches of aromatic residues, possibly suggestive of degenerate ligand binding sites	687:813	Nogo receptor adopts a leucine-rich repeat (LRR) module whose concave exterior surface contains a broad region of evolutionarily conserved patches of aromatic residues, possibly suggestive of degenerate ligand binding sites.
12718853	3	30	theme	functional	501:510	arg1	characterization					512:527	functional characterization	501:527	functional characterization	501:527	Here, we report the 1.5 A crystal structure and functional characterization of a soluble extracellular domain of the human Nogo receptor.
12718853	6	31	theme	focused	974:980	arg1	studies					1001:1007	focused structure-function studies	974:1007	focused structure-function studies aimed at assessing the physiological relevance of NgR-mediated protein-protein interactions to axon regeneration inhibition	974:1131	These results now provide a detailed framework for focused structure-function studies aimed at assessing the physiological relevance of NgR-mediated protein-protein interactions to axon regeneration inhibition.
12718853	2	32	theme	myelin-associated	415:431	arg1	ligands					444:450	myelin-associated inhibitory ligands	415:450	myelin-associated inhibitory ligands	415:450	Recent studies suggest that an axon surface protein, the Nogo receptor (NgR), may play a role in this process through an unprecedented degree of crossreactivity with myelin-associated inhibitory ligands.
12718853	5	33	theme	LRR	859:861	arg1	base					847:850	the C-terminal base	832:850	the C-terminal base of the LRR	832:861	A deep cleft at the C-terminal base of the LRR may play a role in NgR association with the p75 coreceptor.
12718853	6	34	theme	interactions	1088:1099	arg1	relevance					1046:1054	the physiological relevance	1028:1054	the physiological relevance of NgR-mediated protein-protein interactions to axon regeneration inhibition	1028:1131	These results now provide a detailed framework for focused structure-function studies aimed at assessing the physiological relevance of NgR-mediated protein-protein interactions to axon regeneration inhibition.
12718853	3	35	theme	extracellular	542:554	arg1	receptor					581:588	the human Nogo receptor	566:588	the human Nogo receptor	566:588	Here, we report the 1.5 A crystal structure and functional characterization of a soluble extracellular domain of the human Nogo receptor.
12718853	3	35	theme	extracellular	542:554	arg1	domain					556:561	a soluble extracellular domain	532:561	a soluble extracellular domain of the human Nogo receptor	532:588	Here, we report the 1.5 A crystal structure and functional characterization of a soluble extracellular domain of the human Nogo receptor.
12718853	0	36	theme	receptor	22:29	arg1	ectodomain					31:40	the Nogo receptor ectodomain	13:40	the Nogo receptor ectodomain	13:40	Structure of the Nogo receptor ectodomain: a recognition module implicated in myelin inhibition.
12718853	3	37	theme	receptor	581:588	arg1	receptor					581:588	the human Nogo receptor	566:588	the human Nogo receptor	566:588	Here, we report the 1.5 A crystal structure and functional characterization of a soluble extracellular domain of the human Nogo receptor.
12718853	3	37	theme	receptor	581:588	arg1	domain					556:561	a soluble extracellular domain	532:561	a soluble extracellular domain of the human Nogo receptor	532:588	Here, we report the 1.5 A crystal structure and functional characterization of a soluble extracellular domain of the human Nogo receptor.
12718853	3	38	theme	domain	556:561	arg1	structure					487:495	1.5 A crystal structure	473:495	1.5 A crystal structure	473:495	Here, we report the 1.5 A crystal structure and functional characterization of a soluble extracellular domain of the human Nogo receptor.
12718853	3	38	theme	domain	556:561	arg1	characterization					512:527	functional characterization	501:527	functional characterization	501:527	Here, we report the 1.5 A crystal structure and functional characterization of a soluble extracellular domain of the human Nogo receptor.
12718853	4	39	theme	Nogo	591:594	arg1	receptor					596:603	Nogo receptor	591:603	Nogo receptor	591:603	Nogo receptor adopts a leucine-rich repeat (LRR) module whose concave exterior surface contains a broad region of evolutionarily conserved patches of aromatic residues, possibly suggestive of degenerate ligand binding sites.
12718853	2	40	theme	crossreactivity	394:408	arg1	degree					384:389	an unprecedented degree	367:389	an unprecedented degree of crossreactivity with myelin-associated inhibitory ligands	367:450	Recent studies suggest that an axon surface protein, the Nogo receptor (NgR), may play a role in this process through an unprecedented degree of crossreactivity with myelin-associated inhibitory ligands.
12718853	4	41	theme	degenerate	783:792	arg1	sites					809:813	degenerate ligand binding sites	783:813	degenerate ligand binding sites	783:813	Nogo receptor adopts a leucine-rich repeat (LRR) module whose concave exterior surface contains a broad region of evolutionarily conserved patches of aromatic residues, possibly suggestive of degenerate ligand binding sites.
12718853	2	42	theme	Nogo	306:309	arg1	protein					293:299	an axon surface protein	277:299	an axon surface protein	277:299	Recent studies suggest that an axon surface protein, the Nogo receptor (NgR), may play a role in this process through an unprecedented degree of crossreactivity with myelin-associated inhibitory ligands.
12718853	2	42	theme	Nogo	306:309	arg1	NgR					321:323	NgR	321:323	NgR	321:323	Recent studies suggest that an axon surface protein, the Nogo receptor (NgR), may play a role in this process through an unprecedented degree of crossreactivity with myelin-associated inhibitory ligands.
12718853	2	42	theme	Nogo	306:309	arg1	receptor					311:318	Nogo receptor	306:318	the Nogo receptor (NgR)	302:324	Recent studies suggest that an axon surface protein, the Nogo receptor (NgR), may play a role in this process through an unprecedented degree of crossreactivity with myelin-associated inhibitory ligands.
12718853	5	43	with	association	886:896	arg1	coreceptor					911:920	the p75 coreceptor	903:920	the p75 coreceptor	903:920	A deep cleft at the C-terminal base of the LRR may play a role in NgR association with the p75 coreceptor.
12718853	4	44	theme	ligand	794:799	arg1	sites					809:813	degenerate ligand binding sites	783:813	degenerate ligand binding sites	783:813	Nogo receptor adopts a leucine-rich repeat (LRR) module whose concave exterior surface contains a broad region of evolutionarily conserved patches of aromatic residues, possibly suggestive of degenerate ligand binding sites.
12718853	3	45	theme	soluble	534:540	arg1	receptor					581:588	the human Nogo receptor	566:588	the human Nogo receptor	566:588	Here, we report the 1.5 A crystal structure and functional characterization of a soluble extracellular domain of the human Nogo receptor.
12718853	3	45	theme	soluble	534:540	arg1	domain					556:561	a soluble extracellular domain	532:561	a soluble extracellular domain of the human Nogo receptor	532:588	Here, we report the 1.5 A crystal structure and functional characterization of a soluble extracellular domain of the human Nogo receptor.
12718853	1	46	theme	axon	108:111	arg1	regeneration					113:124	axon regeneration	108:124	axon regeneration	108:124	Failure of axon regeneration in the adult mammalian central nervous system (CNS) is at least partly due to inhibitory molecules associated with myelin.
12718853	4	47	theme	residues	750:757	arg1	patches					730:736	evolutionarily conserved patches	705:736	evolutionarily conserved patches	705:736	Nogo receptor adopts a leucine-rich repeat (LRR) module whose concave exterior surface contains a broad region of evolutionarily conserved patches of aromatic residues, possibly suggestive of degenerate ligand binding sites.
12718853	4	48	theme	aromatic	741:748	arg1	residues					750:757	aromatic residues	741:757	aromatic residues	741:757	Nogo receptor adopts a leucine-rich repeat (LRR) module whose concave exterior surface contains a broad region of evolutionarily conserved patches of aromatic residues, possibly suggestive of degenerate ligand binding sites.
12718853	3	49	theme	human	570:574	arg1	receptor					581:588	the human Nogo receptor	566:588	the human Nogo receptor	566:588	Here, we report the 1.5 A crystal structure and functional characterization of a soluble extracellular domain of the human Nogo receptor.
12718853	1	50	theme	regeneration	113:124	arg1	Failure					97:103	Failure	97:103	Failure of axon regeneration in the adult mammalian central nervous system (CNS)	97:176	Failure of axon regeneration in the adult mammalian central nervous system (CNS) is at least partly due to inhibitory molecules associated with myelin.
12718853	1	51	from	Failure	97:103	arg1	CNS					173:175	CNS	173:175	CNS	173:175	Failure of axon regeneration in the adult mammalian central nervous system (CNS) is at least partly due to inhibitory molecules associated with myelin.
12718853	1	51	from	Failure	97:103	arg1	system					165:170	the adult mammalian central nervous system	129:170	the adult mammalian central nervous system (CNS)	129:176	Failure of axon regeneration in the adult mammalian central nervous system (CNS) is at least partly due to inhibitory molecules associated with myelin.
12718853	6	52	theme	detailed	951:958	arg1	framework					960:968	a detailed framework	949:968	a detailed framework for focused structure-function studies aimed at assessing the physiological relevance of NgR-mediated protein-protein interactions to axon regeneration inhibition	949:1131	These results now provide a detailed framework for focused structure-function studies aimed at assessing the physiological relevance of NgR-mediated protein-protein interactions to axon regeneration inhibition.
12718853	4	53	theme	conserved	720:728	arg1	patches					730:736	evolutionarily conserved patches	705:736	evolutionarily conserved patches	705:736	Nogo receptor adopts a leucine-rich repeat (LRR) module whose concave exterior surface contains a broad region of evolutionarily conserved patches of aromatic residues, possibly suggestive of degenerate ligand binding sites.
12718853	3	54	theme	Nogo	576:579	arg1	receptor					581:588	the human Nogo receptor	566:588	the human Nogo receptor	566:588	Here, we report the 1.5 A crystal structure and functional characterization of a soluble extracellular domain of the human Nogo receptor.
12718853	2	55	with	crossreactivity	394:408	arg1	ligands					444:450	myelin-associated inhibitory ligands	415:450	myelin-associated inhibitory ligands	415:450	Recent studies suggest that an axon surface protein, the Nogo receptor (NgR), may play a role in this process through an unprecedented degree of crossreactivity with myelin-associated inhibitory ligands.
12718853	3	56	dep	structure	487:495	arg1	the					469:471	the	469:471	the	469:471	Here, we report the 1.5 A crystal structure and functional characterization of a soluble extracellular domain of the human Nogo receptor.
12718853	6	57	theme	protein-protein	1072:1086	arg1	interactions					1088:1099	NgR-mediated protein-protein interactions	1059:1099	NgR-mediated protein-protein interactions	1059:1099	These results now provide a detailed framework for focused structure-function studies aimed at assessing the physiological relevance of NgR-mediated protein-protein interactions to axon regeneration inhibition.
12718853	5	58	theme	C-terminal	836:845	arg1	base					847:850	the C-terminal base	832:850	the C-terminal base of the LRR	832:861	A deep cleft at the C-terminal base of the LRR may play a role in NgR association with the p75 coreceptor.
12718853	5	59	theme	NgR	882:884	arg1	association					886:896	NgR association	882:896	NgR association with the p75 coreceptor	882:920	A deep cleft at the C-terminal base of the LRR may play a role in NgR association with the p75 coreceptor.
12718853	0	60	theme	recognition	45:55	arg1	module					57:62	a recognition module	43:62	Structure of the Nogo receptor ectodomain: a recognition module implicated in myelin inhibition.	0:95	Structure of the Nogo receptor ectodomain: a recognition module implicated in myelin inhibition.
12718853	6	61	theme	axon	1104:1107	arg1	inhibition					1122:1131	axon regeneration inhibition	1104:1131	axon regeneration inhibition	1104:1131	These results now provide a detailed framework for focused structure-function studies aimed at assessing the physiological relevance of NgR-mediated protein-protein interactions to axon regeneration inhibition.
12718853	0	62	dep	Structure	0:8	arg1	module					57:62	a recognition module	43:62	Structure of the Nogo receptor ectodomain: a recognition module implicated in myelin inhibition.	0:95	Structure of the Nogo receptor ectodomain: a recognition module implicated in myelin inhibition.
12718853	1	63	theme	adult	133:137	arg1	CNS					173:175	CNS	173:175	CNS	173:175	Failure of axon regeneration in the adult mammalian central nervous system (CNS) is at least partly due to inhibitory molecules associated with myelin.
12718853	1	63	theme	adult	133:137	arg1	system					165:170	the adult mammalian central nervous system	129:170	the adult mammalian central nervous system (CNS)	129:176	Failure of axon regeneration in the adult mammalian central nervous system (CNS) is at least partly due to inhibitory molecules associated with myelin.
12718853	1	64	theme	inhibitory	204:213	arg1	molecules					215:223	inhibitory molecules	204:223	inhibitory molecules associated with myelin	204:246	Failure of axon regeneration in the adult mammalian central nervous system (CNS) is at least partly due to inhibitory molecules associated with myelin.
22902367	3	0	theme	nectins	379:385	arg1	nectin-like					411:421	the related protein nectin-like 5	391:423	the related protein nectin-like 5 (Necl-5)	391:432	We determined the homophilic binding affinities and heterophilic specificities of all four nectins and the related protein nectin-like 5 (Necl-5) from human and mouse, revealing a range of homophilic interaction strengths and a defined heterophilic specificity pattern.
22902367	3	0	theme	nectins	379:385	arg1	Necl-5					426:431	Necl-5	426:431	Necl-5	426:431	We determined the homophilic binding affinities and heterophilic specificities of all four nectins and the related protein nectin-like 5 (Necl-5) from human and mouse, revealing a range of homophilic interaction strengths and a defined heterophilic specificity pattern.
22902367	3	0	theme	nectins	379:385	arg1	affinities					325:334	the homophilic binding affinities	302:334	the homophilic binding affinities	302:334	We determined the homophilic binding affinities and heterophilic specificities of all four nectins and the related protein nectin-like 5 (Necl-5) from human and mouse, revealing a range of homophilic interaction strengths and a defined heterophilic specificity pattern.
22902367	3	0	theme	nectins	379:385	arg1	specificities					353:365	heterophilic specificities	340:365	heterophilic specificities	340:365	We determined the homophilic binding affinities and heterophilic specificities of all four nectins and the related protein nectin-like 5 (Necl-5) from human and mouse, revealing a range of homophilic interaction strengths and a defined heterophilic specificity pattern.
22902367	6	1	theme	cross-linking	976:988	arg1	experiments					990:1000	targeted cross-linking experiments	967:1000	targeted cross-linking experiments	967:1000	However, conservation of this interface and the results of targeted cross-linking experiments showed that this dimer probably represents the adhesive trans interaction.
22902367	5	2	theme	stereotyped	831:841	arg1	interface					843:851	a stereotyped interface	829:851	a stereotyped interface that was previously proposed to represent a cis dimer	829:905	All of the crystal structures revealed dimeric nectins bound through a stereotyped interface that was previously proposed to represent a cis dimer.
22902367	6	3	theme	targeted	967:974	arg1	experiments					990:1000	targeted cross-linking experiments	967:1000	targeted cross-linking experiments	967:1000	However, conservation of this interface and the results of targeted cross-linking experiments showed that this dimer probably represents the adhesive trans interaction.
22902367	4	4	theme	Necl-5	752:757	arg1	Necl-5					752:757	Necl-5	752:757	Necl-5	752:757	To understand the molecular basis of their adhesion and specificity, we determined the crystal structures of natively glycosylated full ectodomains or adhesive fragments of all four nectins and Necl-5.
22902367	4	4	theme	Necl-5	752:757	arg1	nectins					740:746	all four nectins	731:746	all four nectins	731:746	To understand the molecular basis of their adhesion and specificity, we determined the crystal structures of natively glycosylated full ectodomains or adhesive fragments of all four nectins and Necl-5.
22902367	4	4	theme	Necl-5	752:757	arg1	ectodomains					694:704	natively glycosylated full ectodomains	667:704	natively glycosylated full ectodomains	667:704	To understand the molecular basis of their adhesion and specificity, we determined the crystal structures of natively glycosylated full ectodomains or adhesive fragments of all four nectins and Necl-5.
22902367	4	4	theme	Necl-5	752:757	arg1	fragments					718:726	adhesive fragments	709:726	adhesive fragments of all four nectins and Necl-5	709:757	To understand the molecular basis of their adhesion and specificity, we determined the crystal structures of natively glycosylated full ectodomains or adhesive fragments of all four nectins and Necl-5.
22902367	1	5	gly	glycoproteins	107:119	arg1	glycoproteins					107:119	immunoglobulin superfamily glycoproteins	80:119	immunoglobulin superfamily glycoproteins that mediate intercellular adhesion in many vertebrate tissues	80:182	Nectins are immunoglobulin superfamily glycoproteins that mediate intercellular adhesion in many vertebrate tissues.
22902367	1	5	gly	glycoproteins	107:119	arg1	Nectins					68:74	Nectins	68:74	Nectins	68:74	Nectins are immunoglobulin superfamily glycoproteins that mediate intercellular adhesion in many vertebrate tissues.
22902367	4	6	theme	crystal	645:651	arg1	structures					653:662	the crystal structures	641:662	the crystal structures of natively glycosylated full ectodomains or adhesive fragments of all four nectins and Necl-5	641:757	To understand the molecular basis of their adhesion and specificity, we determined the crystal structures of natively glycosylated full ectodomains or adhesive fragments of all four nectins and Necl-5.
22902367	2	7	theme	Homophilic	185:194	arg1	interactions					213:224	Homophilic and heterophilic interactions	185:224	Homophilic and heterophilic interactions between nectin family members	185:254	Homophilic and heterophilic interactions between nectin family members help mediate tissue patterning.
22902367	3	8	theme	heterophilic	524:535	arg1	pattern					549:555	a defined heterophilic specificity pattern	514:555	a defined heterophilic specificity pattern	514:555	We determined the homophilic binding affinities and heterophilic specificities of all four nectins and the related protein nectin-like 5 (Necl-5) from human and mouse, revealing a range of homophilic interaction strengths and a defined heterophilic specificity pattern.
22902367	3	9	theme	protein	403:409	arg1	nectin-like					411:421	the related protein nectin-like 5	391:423	the related protein nectin-like 5 (Necl-5)	391:432	We determined the homophilic binding affinities and heterophilic specificities of all four nectins and the related protein nectin-like 5 (Necl-5) from human and mouse, revealing a range of homophilic interaction strengths and a defined heterophilic specificity pattern.
22902367	3	9	theme	protein	403:409	arg1	Necl-5					426:431	Necl-5	426:431	Necl-5	426:431	We determined the homophilic binding affinities and heterophilic specificities of all four nectins and the related protein nectin-like 5 (Necl-5) from human and mouse, revealing a range of homophilic interaction strengths and a defined heterophilic specificity pattern.
22902367	3	10	theme	specificity	537:547	arg1	pattern					549:555	a defined heterophilic specificity pattern	514:555	a defined heterophilic specificity pattern	514:555	We determined the homophilic binding affinities and heterophilic specificities of all four nectins and the related protein nectin-like 5 (Necl-5) from human and mouse, revealing a range of homophilic interaction strengths and a defined heterophilic specificity pattern.
22902367	4	11	gly	glycosylated	676:687	arg1	Necl-5					752:757	Necl-5	752:757	Necl-5	752:757	To understand the molecular basis of their adhesion and specificity, we determined the crystal structures of natively glycosylated full ectodomains or adhesive fragments of all four nectins and Necl-5.
22902367	4	11	gly	glycosylated	676:687	arg1	nectins					740:746	all four nectins	731:746	all four nectins	731:746	To understand the molecular basis of their adhesion and specificity, we determined the crystal structures of natively glycosylated full ectodomains or adhesive fragments of all four nectins and Necl-5.
22902367	4	11	gly	glycosylated	676:687	arg1	ectodomains					694:704	natively glycosylated full ectodomains	667:704	natively glycosylated full ectodomains	667:704	To understand the molecular basis of their adhesion and specificity, we determined the crystal structures of natively glycosylated full ectodomains or adhesive fragments of all four nectins and Necl-5.
22902367	6	12	theme	trans	1058:1062	arg1	interaction					1064:1074	the adhesive trans interaction	1045:1074	the adhesive trans interaction	1045:1074	However, conservation of this interface and the results of targeted cross-linking experiments showed that this dimer probably represents the adhesive trans interaction.
22902367	3	13	theme	homophilic	306:315	arg1	affinities					325:334	the homophilic binding affinities	302:334	the homophilic binding affinities	302:334	We determined the homophilic binding affinities and heterophilic specificities of all four nectins and the related protein nectin-like 5 (Necl-5) from human and mouse, revealing a range of homophilic interaction strengths and a defined heterophilic specificity pattern.
22902367	7	14	theme	adhesive	1152:1159	arg1	specificity					1169:1179	the adhesive binding specificity	1148:1179	the adhesive binding specificity of nectins	1148:1190	The structure of the dimer provides a simple molecular explanation for the adhesive binding specificity of nectins.
22902367	1	15	theme	immunoglobulin	80:93	arg1	glycoproteins					107:119	immunoglobulin superfamily glycoproteins	80:119	immunoglobulin superfamily glycoproteins that mediate intercellular adhesion in many vertebrate tissues	80:182	Nectins are immunoglobulin superfamily glycoproteins that mediate intercellular adhesion in many vertebrate tissues.
22902367	1	15	theme	immunoglobulin	80:93	arg1	Nectins					68:74	Nectins	68:74	Nectins	68:74	Nectins are immunoglobulin superfamily glycoproteins that mediate intercellular adhesion in many vertebrate tissues.
22902367	3	16	theme	homophilic	477:486	arg1	interaction					488:498	homophilic interaction strengths and a defined heterophilic specificity pattern	477:555	interaction	488:498	We determined the homophilic binding affinities and heterophilic specificities of all four nectins and the related protein nectin-like 5 (Necl-5) from human and mouse, revealing a range of homophilic interaction strengths and a defined heterophilic specificity pattern.
22902367	0	17	theme	ectodomain	7:16	arg1	structures					18:27	Nectin ectodomain structures	0:27	Nectin ectodomain structures	0:27	Nectin ectodomain structures reveal a canonical adhesive interface.
22902367	6	18	theme	interface	938:946	arg1	conservation					917:928	conservation	917:928	conservation of this interface	917:946	However, conservation of this interface and the results of targeted cross-linking experiments showed that this dimer probably represents the adhesive trans interaction.
22902367	6	18	theme	interface	938:946	arg1	results					956:962	the results	952:962	the results of targeted cross-linking experiments	952:1000	However, conservation of this interface and the results of targeted cross-linking experiments showed that this dimer probably represents the adhesive trans interaction.
22902367	7	19	theme	binding	1161:1167	arg1	specificity					1169:1179	the adhesive binding specificity	1148:1179	the adhesive binding specificity of nectins	1148:1190	The structure of the dimer provides a simple molecular explanation for the adhesive binding specificity of nectins.
22902367	1	20	theme	superfamily	95:105	arg1	glycoproteins					107:119	immunoglobulin superfamily glycoproteins	80:119	immunoglobulin superfamily glycoproteins that mediate intercellular adhesion in many vertebrate tissues	80:182	Nectins are immunoglobulin superfamily glycoproteins that mediate intercellular adhesion in many vertebrate tissues.
22902367	1	20	theme	superfamily	95:105	arg1	Nectins					68:74	Nectins	68:74	Nectins	68:74	Nectins are immunoglobulin superfamily glycoproteins that mediate intercellular adhesion in many vertebrate tissues.
22902367	0	21	theme	Nectin	0:5	arg1	structures					18:27	Nectin ectodomain structures	0:27	Nectin ectodomain structures	0:27	Nectin ectodomain structures reveal a canonical adhesive interface.
22902367	6	22	theme	adhesive	1049:1056	arg1	interaction					1064:1074	the adhesive trans interaction	1045:1074	the adhesive trans interaction	1045:1074	However, conservation of this interface and the results of targeted cross-linking experiments showed that this dimer probably represents the adhesive trans interaction.
22902367	4	23	theme	adhesion	601:608	arg1	basis					586:590	the molecular basis	572:590	the molecular basis of their adhesion and specificity	572:624	To understand the molecular basis of their adhesion and specificity, we determined the crystal structures of natively glycosylated full ectodomains or adhesive fragments of all four nectins and Necl-5.
22902367	1	24	from	adhesion	148:155	arg1	tissues					176:182	many vertebrate tissues	160:182	many vertebrate tissues	160:182	Nectins are immunoglobulin superfamily glycoproteins that mediate intercellular adhesion in many vertebrate tissues.
22902367	4	25	theme	ectodomains	694:704	arg1	structures					653:662	the crystal structures	641:662	the crystal structures of natively glycosylated full ectodomains or adhesive fragments of all four nectins and Necl-5	641:757	To understand the molecular basis of their adhesion and specificity, we determined the crystal structures of natively glycosylated full ectodomains or adhesive fragments of all four nectins and Necl-5.
22902367	3	26	theme	heterophilic	340:351	arg1	specificities					353:365	heterophilic specificities	340:365	heterophilic specificities	340:365	We determined the homophilic binding affinities and heterophilic specificities of all four nectins and the related protein nectin-like 5 (Necl-5) from human and mouse, revealing a range of homophilic interaction strengths and a defined heterophilic specificity pattern.
22902367	4	27	theme	full	689:692	arg1	Necl-5					752:757	Necl-5	752:757	Necl-5	752:757	To understand the molecular basis of their adhesion and specificity, we determined the crystal structures of natively glycosylated full ectodomains or adhesive fragments of all four nectins and Necl-5.
22902367	4	27	theme	full	689:692	arg1	nectins					740:746	all four nectins	731:746	all four nectins	731:746	To understand the molecular basis of their adhesion and specificity, we determined the crystal structures of natively glycosylated full ectodomains or adhesive fragments of all four nectins and Necl-5.
22902367	4	27	theme	full	689:692	arg1	ectodomains					694:704	natively glycosylated full ectodomains	667:704	natively glycosylated full ectodomains	667:704	To understand the molecular basis of their adhesion and specificity, we determined the crystal structures of natively glycosylated full ectodomains or adhesive fragments of all four nectins and Necl-5.
22902367	0	28	theme	canonical	38:46	arg1	interface					57:65	a canonical adhesive interface	36:65	a canonical adhesive interface	36:65	Nectin ectodomain structures reveal a canonical adhesive interface.
22902367	4	29	theme	specificity	614:624	arg1	basis					586:590	the molecular basis	572:590	the molecular basis of their adhesion and specificity	572:624	To understand the molecular basis of their adhesion and specificity, we determined the crystal structures of natively glycosylated full ectodomains or adhesive fragments of all four nectins and Necl-5.
22902367	3	30	theme	binding	317:323	arg1	affinities					325:334	the homophilic binding affinities	302:334	the homophilic binding affinities	302:334	We determined the homophilic binding affinities and heterophilic specificities of all four nectins and the related protein nectin-like 5 (Necl-5) from human and mouse, revealing a range of homophilic interaction strengths and a defined heterophilic specificity pattern.
22902367	4	31	theme	adhesive	709:716	arg1	fragments					718:726	adhesive fragments	709:726	adhesive fragments of all four nectins and Necl-5	709:757	To understand the molecular basis of their adhesion and specificity, we determined the crystal structures of natively glycosylated full ectodomains or adhesive fragments of all four nectins and Necl-5.
22902367	3	32	theme	interaction	488:498	arg1	range					468:472	a range	466:472	a range of homophilic interaction strengths and a defined heterophilic specificity pattern	466:555	We determined the homophilic binding affinities and heterophilic specificities of all four nectins and the related protein nectin-like 5 (Necl-5) from human and mouse, revealing a range of homophilic interaction strengths and a defined heterophilic specificity pattern.
22902367	5	33	theme	crystal	771:777	arg1	structures					779:788	the crystal structures	767:788	the crystal structures	767:788	All of the crystal structures revealed dimeric nectins bound through a stereotyped interface that was previously proposed to represent a cis dimer.
22902367	2	34	theme	heterophilic	200:211	arg1	interactions					213:224	Homophilic and heterophilic interactions	185:224	Homophilic and heterophilic interactions between nectin family members	185:254	Homophilic and heterophilic interactions between nectin family members help mediate tissue patterning.
22902367	4	35	theme	molecular	576:584	arg1	basis					586:590	the molecular basis	572:590	the molecular basis of their adhesion and specificity	572:624	To understand the molecular basis of their adhesion and specificity, we determined the crystal structures of natively glycosylated full ectodomains or adhesive fragments of all four nectins and Necl-5.
22902367	7	36	theme	simple	1115:1120	arg1	explanation					1132:1142	a simple molecular explanation	1113:1142	a simple molecular explanation for the adhesive binding specificity of nectins	1113:1190	The structure of the dimer provides a simple molecular explanation for the adhesive binding specificity of nectins.
22902367	2	37	theme	tissue	269:274	arg1	patterning					276:285	tissue patterning	269:285	tissue patterning	269:285	Homophilic and heterophilic interactions between nectin family members help mediate tissue patterning.
22902367	7	38	theme	dimer	1098:1102	arg1	structure					1081:1089	The structure	1077:1089	The structure of the dimer	1077:1102	The structure of the dimer provides a simple molecular explanation for the adhesive binding specificity of nectins.
22902367	1	39	theme	intercellular	134:146	arg1	adhesion					148:155	intercellular adhesion	134:155	intercellular adhesion in many vertebrate tissues	134:182	Nectins are immunoglobulin superfamily glycoproteins that mediate intercellular adhesion in many vertebrate tissues.
22902367	0	40	theme	adhesive	48:55	arg1	interface					57:65	a canonical adhesive interface	36:65	a canonical adhesive interface	36:65	Nectin ectodomain structures reveal a canonical adhesive interface.
22902367	7	41	theme	molecular	1122:1130	arg1	explanation					1132:1142	a simple molecular explanation	1113:1142	a simple molecular explanation for the adhesive binding specificity of nectins	1113:1190	The structure of the dimer provides a simple molecular explanation for the adhesive binding specificity of nectins.
22902367	7	42	theme	nectins	1184:1190	arg1	specificity					1169:1179	the adhesive binding specificity	1148:1179	the adhesive binding specificity of nectins	1148:1190	The structure of the dimer provides a simple molecular explanation for the adhesive binding specificity of nectins.
22902367	3	43	theme	pattern	549:555	arg1	range					468:472	a range	466:472	a range of homophilic interaction strengths and a defined heterophilic specificity pattern	466:555	We determined the homophilic binding affinities and heterophilic specificities of all four nectins and the related protein nectin-like 5 (Necl-5) from human and mouse, revealing a range of homophilic interaction strengths and a defined heterophilic specificity pattern.
22902367	3	44	dep	interaction	488:498	arg1	strengths					500:508	strengths	500:508	strengths	500:508	We determined the homophilic binding affinities and heterophilic specificities of all four nectins and the related protein nectin-like 5 (Necl-5) from human and mouse, revealing a range of homophilic interaction strengths and a defined heterophilic specificity pattern.
22902367	3	45	theme	defined	516:522	arg1	pattern					549:555	a defined heterophilic specificity pattern	514:555	a defined heterophilic specificity pattern	514:555	We determined the homophilic binding affinities and heterophilic specificities of all four nectins and the related protein nectin-like 5 (Necl-5) from human and mouse, revealing a range of homophilic interaction strengths and a defined heterophilic specificity pattern.
22902367	5	46	theme	dimeric	799:805	arg1	nectins					807:813	dimeric nectins	799:813	dimeric nectins bound through a stereotyped interface that was previously proposed to represent a cis dimer	799:905	All of the crystal structures revealed dimeric nectins bound through a stereotyped interface that was previously proposed to represent a cis dimer.
22902367	2	47	theme	family	241:246	arg1	members					248:254	nectin family members	234:254	nectin family members	234:254	Homophilic and heterophilic interactions between nectin family members help mediate tissue patterning.
22902367	1	48	theme	many	160:163	arg1	tissues					176:182	many vertebrate tissues	160:182	many vertebrate tissues	160:182	Nectins are immunoglobulin superfamily glycoproteins that mediate intercellular adhesion in many vertebrate tissues.
22902367	2	49	theme	nectin	234:239	arg1	members					248:254	nectin family members	234:254	nectin family members	234:254	Homophilic and heterophilic interactions between nectin family members help mediate tissue patterning.
22902367	5	50	theme	cis	897:899	arg1	dimer					901:905	a cis dimer	895:905	a cis dimer	895:905	All of the crystal structures revealed dimeric nectins bound through a stereotyped interface that was previously proposed to represent a cis dimer.
22902367	1	51	theme	vertebrate	165:174	arg1	tissues					176:182	many vertebrate tissues	160:182	many vertebrate tissues	160:182	Nectins are immunoglobulin superfamily glycoproteins that mediate intercellular adhesion in many vertebrate tissues.
22902367	4	52	theme	fragments	718:726	arg1	structures					653:662	the crystal structures	641:662	the crystal structures of natively glycosylated full ectodomains or adhesive fragments of all four nectins and Necl-5	641:757	To understand the molecular basis of their adhesion and specificity, we determined the crystal structures of natively glycosylated full ectodomains or adhesive fragments of all four nectins and Necl-5.
22902367	4	53	theme	glycosylated	676:687	arg1	Necl-5					752:757	Necl-5	752:757	Necl-5	752:757	To understand the molecular basis of their adhesion and specificity, we determined the crystal structures of natively glycosylated full ectodomains or adhesive fragments of all four nectins and Necl-5.
22902367	4	53	theme	glycosylated	676:687	arg1	nectins					740:746	all four nectins	731:746	all four nectins	731:746	To understand the molecular basis of their adhesion and specificity, we determined the crystal structures of natively glycosylated full ectodomains or adhesive fragments of all four nectins and Necl-5.
22902367	4	53	theme	glycosylated	676:687	arg1	ectodomains					694:704	natively glycosylated full ectodomains	667:704	natively glycosylated full ectodomains	667:704	To understand the molecular basis of their adhesion and specificity, we determined the crystal structures of natively glycosylated full ectodomains or adhesive fragments of all four nectins and Necl-5.
22902367	3	54	theme	related	395:401	arg1	nectin-like					411:421	the related protein nectin-like 5	391:423	the related protein nectin-like 5 (Necl-5)	391:432	We determined the homophilic binding affinities and heterophilic specificities of all four nectins and the related protein nectin-like 5 (Necl-5) from human and mouse, revealing a range of homophilic interaction strengths and a defined heterophilic specificity pattern.
22902367	3	54	theme	related	395:401	arg1	Necl-5					426:431	Necl-5	426:431	Necl-5	426:431	We determined the homophilic binding affinities and heterophilic specificities of all four nectins and the related protein nectin-like 5 (Necl-5) from human and mouse, revealing a range of homophilic interaction strengths and a defined heterophilic specificity pattern.
22902367	6	55	theme	experiments	990:1000	arg1	conservation					917:928	conservation	917:928	conservation of this interface	917:946	However, conservation of this interface and the results of targeted cross-linking experiments showed that this dimer probably represents the adhesive trans interaction.
22902367	6	55	theme	experiments	990:1000	arg1	results					956:962	the results	952:962	the results of targeted cross-linking experiments	952:1000	However, conservation of this interface and the results of targeted cross-linking experiments showed that this dimer probably represents the adhesive trans interaction.
22902367	4	56	theme	nectins	740:746	arg1	Necl-5					752:757	Necl-5	752:757	Necl-5	752:757	To understand the molecular basis of their adhesion and specificity, we determined the crystal structures of natively glycosylated full ectodomains or adhesive fragments of all four nectins and Necl-5.
22902367	4	56	theme	nectins	740:746	arg1	nectins					740:746	all four nectins	731:746	all four nectins	731:746	To understand the molecular basis of their adhesion and specificity, we determined the crystal structures of natively glycosylated full ectodomains or adhesive fragments of all four nectins and Necl-5.
22902367	4	56	theme	nectins	740:746	arg1	ectodomains					694:704	natively glycosylated full ectodomains	667:704	natively glycosylated full ectodomains	667:704	To understand the molecular basis of their adhesion and specificity, we determined the crystal structures of natively glycosylated full ectodomains or adhesive fragments of all four nectins and Necl-5.
22902367	4	56	theme	nectins	740:746	arg1	fragments					718:726	adhesive fragments	709:726	adhesive fragments of all four nectins and Necl-5	709:757	To understand the molecular basis of their adhesion and specificity, we determined the crystal structures of natively glycosylated full ectodomains or adhesive fragments of all four nectins and Necl-5.
23520111	1	0	theme	single-stranded	137:151	arg1	RNA					153:155	single-stranded RNA	137:155	single-stranded RNA	137:155	Toll-like receptor 7 (TLR7) and TLR8 recognize single-stranded RNA and initiate innate immune responses.
23520111	0	1	theme	agonistic	71:79	arg1	ligands					81:87	agonistic ligands	71:87	agonistic ligands	71:87	Structural reorganization of the Toll-like receptor 8 dimer induced by agonistic ligands.
23520111	5	2	theme	ligand	594:599	arg1	stimulation					601:611	ligand stimulation	594:611	ligand stimulation	594:611	Upon ligand stimulation, the TLR8 dimer was reorganized such that the two C termini were brought into proximity.
23520111	4	3	theme	Ligand	504:509	arg1	recognition					511:521	Ligand recognition	504:521	Ligand recognition	504:521	Ligand recognition was mediated by a dimerization interface formed by two protomers.
23520111	7	4	theme	dimer	943:947	arg1	reorganization					916:929	reorganization	916:929	reorganization of the TLR8 dimer, which enables downstream signaling processes	916:993	Thus, ligand binding induces reorganization of the TLR8 dimer, which enables downstream signaling processes.
23520111	2	5	theme	molecular	285:293	arg1	unknown					379:385	unknown	379:385	unknown	379:385	Several synthetic agonists of TLR7-TLR8 display novel therapeutic potential; however, the molecular basis for ligand recognition and activation of signaling by TLR7 or TLR8 is largely unknown.
23520111	2	5	theme	molecular	285:293	arg1	basis					295:299	the molecular basis	281:299	the molecular basis for ligand recognition and activation of signaling by TLR7 or TLR8	281:366	Several synthetic agonists of TLR7-TLR8 display novel therapeutic potential; however, the molecular basis for ligand recognition and activation of signaling by TLR7 or TLR8 is largely unknown.
23520111	5	6	dep	brought	678:684	arg1	such					645:648	such	645:648	such	645:648	Upon ligand stimulation, the TLR8 dimer was reorganized such that the two C termini were brought into proximity.
23520111	3	7	theme	dimers	480:485	arg1	structures					415:424	the crystal structures	403:424	the crystal structures of unliganded and ligand-induced activated human TLR8 dimers	403:485	In this study, the crystal structures of unliganded and ligand-induced activated human TLR8 dimers were elucidated.
23520111	5	8	theme	TLR8	618:621	arg1	dimer					623:627	the TLR8 dimer	614:627	the TLR8 dimer	614:627	Upon ligand stimulation, the TLR8 dimer was reorganized such that the two C termini were brought into proximity.
23520111	6	9	theme	ligand	850:855	arg1	recognition					857:867	ligand recognition	850:867	ligand recognition	850:867	The loop between leucine-rich repeat 14 (LRR14) and LRR15 was cleaved; however, the N- and C-terminal halves remained associated and contributed to ligand recognition and dimerization.
23520111	7	10	theme	downstream	964:973	arg1	processes					985:993	downstream signaling processes	964:993	downstream signaling processes	964:993	Thus, ligand binding induces reorganization of the TLR8 dimer, which enables downstream signaling processes.
23520111	1	11	theme	innate	170:175	arg1	responses					184:192	innate immune responses	170:192	innate immune responses	170:192	Toll-like receptor 7 (TLR7) and TLR8 recognize single-stranded RNA and initiate innate immune responses.
23520111	0	12	theme	Structural	0:9	arg1	reorganization					11:24	Structural reorganization	0:24	Structural reorganization of the Toll-like receptor 8 dimer	0:58	Structural reorganization of the Toll-like receptor 8 dimer induced by agonistic ligands.
23520111	7	13	theme	ligand	893:898	arg1	binding					900:906	ligand binding	893:906	ligand binding	893:906	Thus, ligand binding induces reorganization of the TLR8 dimer, which enables downstream signaling processes.
23520111	1	14	theme	Toll-like	90:98	arg1	receptor					100:107	Toll-like receptor 7	90:109	Toll-like receptor 7 (TLR7)	90:116	Toll-like receptor 7 (TLR7) and TLR8 recognize single-stranded RNA and initiate innate immune responses.
23520111	1	14	theme	Toll-like	90:98	arg1	TLR7					112:115	TLR7	112:115	TLR7	112:115	Toll-like receptor 7 (TLR7) and TLR8 recognize single-stranded RNA and initiate innate immune responses.
23520111	3	15	theme	crystal	407:413	arg1	structures					415:424	the crystal structures	403:424	the crystal structures of unliganded and ligand-induced activated human TLR8 dimers	403:485	In this study, the crystal structures of unliganded and ligand-induced activated human TLR8 dimers were elucidated.
23520111	4	16	theme	dimerization	541:552	arg1	interface					554:562	a dimerization interface	539:562	a dimerization interface formed by two protomers	539:586	Ligand recognition was mediated by a dimerization interface formed by two protomers.
23520111	7	17	theme	TLR8	938:941	arg1	dimer					943:947	the TLR8 dimer	934:947	the TLR8 dimer	934:947	Thus, ligand binding induces reorganization of the TLR8 dimer, which enables downstream signaling processes.
23520111	3	18	theme	ligand-induced	444:457	arg1	dimers					480:485	unliganded and ligand-induced activated human TLR8 dimers	429:485	unliganded and ligand-induced activated human TLR8 dimers	429:485	In this study, the crystal structures of unliganded and ligand-induced activated human TLR8 dimers were elucidated.
23520111	2	19	theme	ligand	305:310	arg1	recognition					312:322	ligand recognition	305:322	ligand recognition	305:322	Several synthetic agonists of TLR7-TLR8 display novel therapeutic potential; however, the molecular basis for ligand recognition and activation of signaling by TLR7 or TLR8 is largely unknown.
23520111	3	20	theme	activated	459:467	arg1	dimers					480:485	unliganded and ligand-induced activated human TLR8 dimers	429:485	unliganded and ligand-induced activated human TLR8 dimers	429:485	In this study, the crystal structures of unliganded and ligand-induced activated human TLR8 dimers were elucidated.
23520111	0	21	theme	receptor	43:50	arg1	dimer					54:58	the Toll-like receptor 8 dimer	29:58	the Toll-like receptor 8 dimer	29:58	Structural reorganization of the Toll-like receptor 8 dimer induced by agonistic ligands.
23520111	1	22	theme	immune	177:182	arg1	responses					184:192	innate immune responses	170:192	innate immune responses	170:192	Toll-like receptor 7 (TLR7) and TLR8 recognize single-stranded RNA and initiate innate immune responses.
23520111	3	23	theme	unliganded	429:438	arg1	dimers					480:485	unliganded and ligand-induced activated human TLR8 dimers	429:485	unliganded and ligand-induced activated human TLR8 dimers	429:485	In this study, the crystal structures of unliganded and ligand-induced activated human TLR8 dimers were elucidated.
23520111	0	24	theme	Toll-like	33:41	arg1	dimer					54:58	the Toll-like receptor 8 dimer	29:58	the Toll-like receptor 8 dimer	29:58	Structural reorganization of the Toll-like receptor 8 dimer induced by agonistic ligands.
23520111	2	25	theme	TLR7-TLR8	225:233	arg1	agonists					213:220	Several synthetic agonists	195:220	Several synthetic agonists of TLR7-TLR8	195:233	Several synthetic agonists of TLR7-TLR8 display novel therapeutic potential; however, the molecular basis for ligand recognition and activation of signaling by TLR7 or TLR8 is largely unknown.
23520111	0	26	theme	dimer	54:58	arg1	reorganization					11:24	Structural reorganization	0:24	Structural reorganization of the Toll-like receptor 8 dimer	0:58	Structural reorganization of the Toll-like receptor 8 dimer induced by agonistic ligands.
23520111	5	27	theme	C	663:663	arg1	termini					665:671	the two C termini	655:671	the two C termini	655:671	Upon ligand stimulation, the TLR8 dimer was reorganized such that the two C termini were brought into proximity.
23520111	2	28	theme	signaling	342:350	arg1	activation					328:337	activation	328:337	activation	328:337	Several synthetic agonists of TLR7-TLR8 display novel therapeutic potential; however, the molecular basis for ligand recognition and activation of signaling by TLR7 or TLR8 is largely unknown.
23520111	2	28	theme	signaling	342:350	arg1	recognition					312:322	ligand recognition	305:322	ligand recognition	305:322	Several synthetic agonists of TLR7-TLR8 display novel therapeutic potential; however, the molecular basis for ligand recognition and activation of signaling by TLR7 or TLR8 is largely unknown.
23520111	2	29	theme	synthetic	203:211	arg1	agonists					213:220	Several synthetic agonists	195:220	Several synthetic agonists of TLR7-TLR8	195:233	Several synthetic agonists of TLR7-TLR8 display novel therapeutic potential; however, the molecular basis for ligand recognition and activation of signaling by TLR7 or TLR8 is largely unknown.
23520111	6	30	theme	C-terminal	793:802	arg1	halves					804:809	C-terminal halves	793:809	C-terminal halves	793:809	The loop between leucine-rich repeat 14 (LRR14) and LRR15 was cleaved; however, the N- and C-terminal halves remained associated and contributed to ligand recognition and dimerization.
23520111	7	31	theme	signaling	975:983	arg1	processes					985:993	downstream signaling processes	964:993	downstream signaling processes	964:993	Thus, ligand binding induces reorganization of the TLR8 dimer, which enables downstream signaling processes.
23520111	2	32	theme	Several	195:201	arg1	agonists					213:220	Several synthetic agonists	195:220	Several synthetic agonists of TLR7-TLR8	195:233	Several synthetic agonists of TLR7-TLR8 display novel therapeutic potential; however, the molecular basis for ligand recognition and activation of signaling by TLR7 or TLR8 is largely unknown.
23520111	3	33	theme	human	469:473	arg1	dimers					480:485	unliganded and ligand-induced activated human TLR8 dimers	429:485	unliganded and ligand-induced activated human TLR8 dimers	429:485	In this study, the crystal structures of unliganded and ligand-induced activated human TLR8 dimers were elucidated.
23520111	3	34	theme	TLR8	475:478	arg1	dimers					480:485	unliganded and ligand-induced activated human TLR8 dimers	429:485	unliganded and ligand-induced activated human TLR8 dimers	429:485	In this study, the crystal structures of unliganded and ligand-induced activated human TLR8 dimers were elucidated.
23520111	2	35	theme	therapeutic	249:259	arg1	potential					261:269	novel therapeutic potential	243:269	novel therapeutic potential	243:269	Several synthetic agonists of TLR7-TLR8 display novel therapeutic potential; however, the molecular basis for ligand recognition and activation of signaling by TLR7 or TLR8 is largely unknown.
23520111	6	36	theme	leucine-rich	719:730	arg1	repeat					732:737	leucine-rich repeat 14	719:740	leucine-rich repeat 14 (LRR14)	719:748	The loop between leucine-rich repeat 14 (LRR14) and LRR15 was cleaved; however, the N- and C-terminal halves remained associated and contributed to ligand recognition and dimerization.
23520111	6	36	theme	leucine-rich	719:730	arg1	LRR14					743:747	LRR14	743:747	LRR14	743:747	The loop between leucine-rich repeat 14 (LRR14) and LRR15 was cleaved; however, the N- and C-terminal halves remained associated and contributed to ligand recognition and dimerization.
23520111	2	37	theme	novel	243:247	arg1	potential					261:269	novel therapeutic potential	243:269	novel therapeutic potential	243:269	Several synthetic agonists of TLR7-TLR8 display novel therapeutic potential; however, the molecular basis for ligand recognition and activation of signaling by TLR7 or TLR8 is largely unknown.
24548619	0	0	theme	endoplasmic	82:92	arg1	reticulum					94:102	the endoplasmic reticulum	78:102	the endoplasmic reticulum	78:102	A unique C-terminal domain allows retention of matrix metalloproteinase-27 in the endoplasmic reticulum.
24548619	4	1	theme	fractionation	523:535	arg1	retention					571:579	endoglycosidase H. Subcellular fractionation and confocal microscopy evidenced retention	492:579	endoglycosidase H. Subcellular fractionation and confocal microscopy evidenced retention of endogenous MMP-27 or recombinant rMMP-27 in the endoplasmic reticulum (ER)	492:657	Intracellular MMP-27 was sensitive to endoglycosidase H. Subcellular fractionation and confocal microscopy evidenced retention of endogenous MMP-27 or recombinant rMMP-27 in the endoplasmic reticulum (ER) with locked exit across the intermediate compartment (ERGIC).
24548619	6	2	theme	ER	905:906	arg1	retention					908:916	ER retention	905:916	ER retention	905:916	CTE addition to rMMP-10 (a secreted MMP) caused ER retention and blocked secretion.
24548619	8	3	theme	integral	1383:1390	arg1	MMP-27					1366:1371	MMP-27	1366:1371	MMP-27	1366:1371	Moreover, MMP-27 was protected from digestion by proteinase K. Finally, MT1-MMP/MMP-14 but neither endogenous nor recombinant MMP-27 partitioned in the detergent phase after Triton X-114 extraction, indicating that MMP-27 is not an integral membrane protein.
24548619	8	3	theme	integral	1383:1390	arg1	protein					1401:1407	an integral membrane protein	1380:1407	an integral membrane protein	1380:1407	Moreover, MMP-27 was protected from digestion by proteinase K. Finally, MT1-MMP/MMP-14 but neither endogenous nor recombinant MMP-27 partitioned in the detergent phase after Triton X-114 extraction, indicating that MMP-27 is not an integral membrane protein.
24548619	2	4	theme	Sequence	167:174	arg1	comparison					176:185	Sequence comparison	167:185	Sequence comparison	167:185	Sequence comparison suggests that a C-terminal extension (CTE) includes a potential transmembrane domain as in some membrane-type (MT)-MMPs.
24548619	10	5	theme	novel	1566:1570	arg1	system					1585:1590	a novel ER retention system	1564:1590	a novel ER retention system	1564:1590	This could represent a novel ER retention system.
24548619	4	6	theme	microscopy	550:559	arg1	retention					571:579	endoglycosidase H. Subcellular fractionation and confocal microscopy evidenced retention	492:579	endoglycosidase H. Subcellular fractionation and confocal microscopy evidenced retention of endogenous MMP-27 or recombinant rMMP-27 in the endoplasmic reticulum (ER)	492:657	Intracellular MMP-27 was sensitive to endoglycosidase H. Subcellular fractionation and confocal microscopy evidenced retention of endogenous MMP-27 or recombinant rMMP-27 in the endoplasmic reticulum (ER) with locked exit across the intermediate compartment (ERGIC).
24548619	7	7	theme	cytosolic	982:990	arg1	C-terminus					992:1001	the cytosolic C-terminus	978:1001	the cytosolic C-terminus of transmembrane MT1-MMP/MMP-14	978:1033	Addition of a PKA target sequence to the cytosolic C-terminus of transmembrane MT1-MMP/MMP-14 led to effective phosphorylation upon forskolin stimulation, but not for MMP-27, excluding transmembrane anchorage.
24548619	4	8	theme	confocal	541:548	arg1	microscopy					550:559	confocal microscopy	541:559	confocal microscopy	541:559	Intracellular MMP-27 was sensitive to endoglycosidase H. Subcellular fractionation and confocal microscopy evidenced retention of endogenous MMP-27 or recombinant rMMP-27 in the endoplasmic reticulum (ER) with locked exit across the intermediate compartment (ERGIC).
24548619	8	9	dep	K.	1211:1212	arg1	partitioned					1284:1294	partitioned	1284:1294	partitioned	1284:1294	Moreover, MMP-27 was protected from digestion by proteinase K. Finally, MT1-MMP/MMP-14 but neither endogenous nor recombinant MMP-27 partitioned in the detergent phase after Triton X-114 extraction, indicating that MMP-27 is not an integral membrane protein.
24548619	6	10	theme	CTE	857:859	arg1	addition					861:868	CTE addition	857:868	CTE addition to rMMP-10 (a secreted MMP)	857:896	CTE addition to rMMP-10 (a secreted MMP) caused ER retention and blocked secretion.
24548619	2	11	theme	MT	298:299	arg1	-MMPs					301:305	some membrane-type (MT)-MMPs	278:305	some membrane-type (MT)-MMPs	278:305	Sequence comparison suggests that a C-terminal extension (CTE) includes a potential transmembrane domain as in some membrane-type (MT)-MMPs.
24548619	7	12	theme	transmembrane	1006:1018	arg1	MT1-MMP/MMP-14					1020:1033	transmembrane MT1-MMP/MMP-14	1006:1033	transmembrane MT1-MMP/MMP-14	1006:1033	Addition of a PKA target sequence to the cytosolic C-terminus of transmembrane MT1-MMP/MMP-14 led to effective phosphorylation upon forskolin stimulation, but not for MMP-27, excluding transmembrane anchorage.
24548619	5	13	theme	downstream	772:781	arg1	ERGIC					807:811	ERGIC	807:811	ERGIC	807:811	Conversely, truncated rMMP-27 without CTE accessed downstream secretory compartments (ERGIC and Golgi) and was constitutively secreted.
24548619	5	13	theme	downstream	772:781	arg1	compartments					793:804	downstream secretory compartments	772:804	downstream secretory compartments (ERGIC and Golgi)	772:822	Conversely, truncated rMMP-27 without CTE accessed downstream secretory compartments (ERGIC and Golgi) and was constitutively secreted.
24548619	5	13	theme	downstream	772:781	arg1	Golgi					817:821	Golgi	817:821	Golgi	817:821	Conversely, truncated rMMP-27 without CTE accessed downstream secretory compartments (ERGIC and Golgi) and was constitutively secreted.
24548619	4	14	theme	endoglycosidase	492:506	arg1	retention					571:579	endoglycosidase H. Subcellular fractionation and confocal microscopy evidenced retention	492:579	endoglycosidase H. Subcellular fractionation and confocal microscopy evidenced retention of endogenous MMP-27 or recombinant rMMP-27 in the endoplasmic reticulum (ER)	492:657	Intracellular MMP-27 was sensitive to endoglycosidase H. Subcellular fractionation and confocal microscopy evidenced retention of endogenous MMP-27 or recombinant rMMP-27 in the endoplasmic reticulum (ER) with locked exit across the intermediate compartment (ERGIC).
24548619	8	15	dep	proteinase	1200:1209	arg1	K.					1211:1212	K.	1211:1212	K.	1211:1212	Moreover, MMP-27 was protected from digestion by proteinase K. Finally, MT1-MMP/MMP-14 but neither endogenous nor recombinant MMP-27 partitioned in the detergent phase after Triton X-114 extraction, indicating that MMP-27 is not an integral membrane protein.
24548619	8	16	theme	membrane	1392:1399	arg1	MMP-27					1366:1371	MMP-27	1366:1371	MMP-27	1366:1371	Moreover, MMP-27 was protected from digestion by proteinase K. Finally, MT1-MMP/MMP-14 but neither endogenous nor recombinant MMP-27 partitioned in the detergent phase after Triton X-114 extraction, indicating that MMP-27 is not an integral membrane protein.
24548619	8	16	theme	membrane	1392:1399	arg1	protein					1401:1407	an integral membrane protein	1380:1407	an integral membrane protein	1380:1407	Moreover, MMP-27 was protected from digestion by proteinase K. Finally, MT1-MMP/MMP-14 but neither endogenous nor recombinant MMP-27 partitioned in the detergent phase after Triton X-114 extraction, indicating that MMP-27 is not an integral membrane protein.
24548619	4	17	theme	endoplasmic	632:642	arg1	ER					655:656	ER	655:656	ER	655:656	Intracellular MMP-27 was sensitive to endoglycosidase H. Subcellular fractionation and confocal microscopy evidenced retention of endogenous MMP-27 or recombinant rMMP-27 in the endoplasmic reticulum (ER) with locked exit across the intermediate compartment (ERGIC).
24548619	4	17	theme	endoplasmic	632:642	arg1	reticulum					644:652	the endoplasmic reticulum	628:652	the endoplasmic reticulum (ER)	628:657	Intracellular MMP-27 was sensitive to endoglycosidase H. Subcellular fractionation and confocal microscopy evidenced retention of endogenous MMP-27 or recombinant rMMP-27 in the endoplasmic reticulum (ER) with locked exit across the intermediate compartment (ERGIC).
24548619	5	18	theme	secretory	783:791	arg1	ERGIC					807:811	ERGIC	807:811	ERGIC	807:811	Conversely, truncated rMMP-27 without CTE accessed downstream secretory compartments (ERGIC and Golgi) and was constitutively secreted.
24548619	5	18	theme	secretory	783:791	arg1	compartments					793:804	downstream secretory compartments	772:804	downstream secretory compartments (ERGIC and Golgi)	772:822	Conversely, truncated rMMP-27 without CTE accessed downstream secretory compartments (ERGIC and Golgi) and was constitutively secreted.
24548619	5	18	theme	secretory	783:791	arg1	Golgi					817:821	Golgi	817:821	Golgi	817:821	Conversely, truncated rMMP-27 without CTE accessed downstream secretory compartments (ERGIC and Golgi) and was constitutively secreted.
24548619	2	19	theme	membrane-type	283:295	arg1	-MMPs					301:305	some membrane-type (MT)-MMPs	278:305	some membrane-type (MT)-MMPs	278:305	Sequence comparison suggests that a C-terminal extension (CTE) includes a potential transmembrane domain as in some membrane-type (MT)-MMPs.
24548619	4	20	with	sensitive	479:487	arg1	exit					671:674	locked exit	664:674	locked exit	664:674	Intracellular MMP-27 was sensitive to endoglycosidase H. Subcellular fractionation and confocal microscopy evidenced retention of endogenous MMP-27 or recombinant rMMP-27 in the endoplasmic reticulum (ER) with locked exit across the intermediate compartment (ERGIC).
24548619	4	21	theme	Subcellular	511:521	arg1	fractionation					523:535	Subcellular fractionation	511:535	Subcellular fractionation	511:535	Intracellular MMP-27 was sensitive to endoglycosidase H. Subcellular fractionation and confocal microscopy evidenced retention of endogenous MMP-27 or recombinant rMMP-27 in the endoplasmic reticulum (ER) with locked exit across the intermediate compartment (ERGIC).
24548619	8	22	theme	recombinant	1265:1275	arg1	MMP-27					1277:1282	endogenous nor recombinant MMP-27	1250:1282	MT1-MMP/MMP-14 but neither endogenous nor recombinant MMP-27	1223:1282	Moreover, MMP-27 was protected from digestion by proteinase K. Finally, MT1-MMP/MMP-14 but neither endogenous nor recombinant MMP-27 partitioned in the detergent phase after Triton X-114 extraction, indicating that MMP-27 is not an integral membrane protein.
24548619	7	23	theme	target	959:964	arg1	sequence					966:973	a PKA target sequence	953:973	a PKA target sequence	953:973	Addition of a PKA target sequence to the cytosolic C-terminus of transmembrane MT1-MMP/MMP-14 led to effective phosphorylation upon forskolin stimulation, but not for MMP-27, excluding transmembrane anchorage.
24548619	4	24	theme	intermediate	687:698	arg1	compartment					700:710	the intermediate compartment	683:710	the intermediate compartment (ERGIC)	683:718	Intracellular MMP-27 was sensitive to endoglycosidase H. Subcellular fractionation and confocal microscopy evidenced retention of endogenous MMP-27 or recombinant rMMP-27 in the endoplasmic reticulum (ER) with locked exit across the intermediate compartment (ERGIC).
24548619	4	24	theme	intermediate	687:698	arg1	ERGIC					713:717	ERGIC	713:717	ERGIC	713:717	Intracellular MMP-27 was sensitive to endoglycosidase H. Subcellular fractionation and confocal microscopy evidenced retention of endogenous MMP-27 or recombinant rMMP-27 in the endoplasmic reticulum (ER) with locked exit across the intermediate compartment (ERGIC).
24548619	3	25	theme	subcellular	376:386	arg1	localization					388:399	its subcellular localization	372:399	its subcellular localization	372:399	Having noticed that MMP-27 was barely secreted, we investigated its subcellular localization and addressed CTE contribution for MMP-27 retention.
24548619	4	26	theme	H.	508:509	arg1	retention					571:579	endoglycosidase H. Subcellular fractionation and confocal microscopy evidenced retention	492:579	endoglycosidase H. Subcellular fractionation and confocal microscopy evidenced retention of endogenous MMP-27 or recombinant rMMP-27 in the endoplasmic reticulum (ER)	492:657	Intracellular MMP-27 was sensitive to endoglycosidase H. Subcellular fractionation and confocal microscopy evidenced retention of endogenous MMP-27 or recombinant rMMP-27 in the endoplasmic reticulum (ER) with locked exit across the intermediate compartment (ERGIC).
24548619	7	27	theme	sequence	966:973	arg1	Addition					941:948	Addition	941:948	Addition of a PKA target sequence to the cytosolic C-terminus of transmembrane MT1-MMP/MMP-14	941:1033	Addition of a PKA target sequence to the cytosolic C-terminus of transmembrane MT1-MMP/MMP-14 led to effective phosphorylation upon forskolin stimulation, but not for MMP-27, excluding transmembrane anchorage.
24548619	7	28	theme	transmembrane	1126:1138	arg1	anchorage					1140:1148	transmembrane anchorage	1126:1148	transmembrane anchorage	1126:1148	Addition of a PKA target sequence to the cytosolic C-terminus of transmembrane MT1-MMP/MMP-14 led to effective phosphorylation upon forskolin stimulation, but not for MMP-27, excluding transmembrane anchorage.
24548619	2	29	from	domain	265:270	arg1	-MMPs					301:305	some membrane-type (MT)-MMPs	278:305	some membrane-type (MT)-MMPs	278:305	Sequence comparison suggests that a C-terminal extension (CTE) includes a potential transmembrane domain as in some membrane-type (MT)-MMPs.
24548619	3	30	theme	MMP-27	436:441	arg1	retention					443:451	MMP-27 retention	436:451	MMP-27 retention	436:451	Having noticed that MMP-27 was barely secreted, we investigated its subcellular localization and addressed CTE contribution for MMP-27 retention.
24548619	8	31	theme	endogenous	1250:1259	arg1	MMP-27					1277:1282	endogenous nor recombinant MMP-27	1250:1282	MT1-MMP/MMP-14 but neither endogenous nor recombinant MMP-27	1223:1282	Moreover, MMP-27 was protected from digestion by proteinase K. Finally, MT1-MMP/MMP-14 but neither endogenous nor recombinant MMP-27 partitioned in the detergent phase after Triton X-114 extraction, indicating that MMP-27 is not an integral membrane protein.
24548619	4	32	theme	MMP-27	595:600	arg1	retention					571:579	endoglycosidase H. Subcellular fractionation and confocal microscopy evidenced retention	492:579	endoglycosidase H. Subcellular fractionation and confocal microscopy evidenced retention of endogenous MMP-27 or recombinant rMMP-27 in the endoplasmic reticulum (ER)	492:657	Intracellular MMP-27 was sensitive to endoglycosidase H. Subcellular fractionation and confocal microscopy evidenced retention of endogenous MMP-27 or recombinant rMMP-27 in the endoplasmic reticulum (ER) with locked exit across the intermediate compartment (ERGIC).
24548619	5	33	theme	truncated	733:741	arg1	rMMP-27					743:749	truncated rMMP-27	733:749	truncated rMMP-27 without CTE	733:761	Conversely, truncated rMMP-27 without CTE accessed downstream secretory compartments (ERGIC and Golgi) and was constitutively secreted.
24548619	7	34	theme	PKA	955:957	arg1	sequence					966:973	a PKA target sequence	953:973	a PKA target sequence	953:973	Addition of a PKA target sequence to the cytosolic C-terminus of transmembrane MT1-MMP/MMP-14 led to effective phosphorylation upon forskolin stimulation, but not for MMP-27, excluding transmembrane anchorage.
24548619	1	35	theme	Matrix	105:110	arg1	MMP-27					134:139	MMP-27	134:139	MMP-27	134:139	Matrix metalloproteinase-27 (MMP-27) is poorly characterized.
24548619	1	35	theme	Matrix	105:110	arg1	metalloproteinase-27					112:131	Matrix metalloproteinase-27	105:131	Matrix metalloproteinase-27 (MMP-27)	105:140	Matrix metalloproteinase-27 (MMP-27) is poorly characterized.
24548619	8	36	theme	Triton	1325:1330	arg1	extraction					1338:1347	Triton X-114 extraction	1325:1347	Triton X-114 extraction	1325:1347	Moreover, MMP-27 was protected from digestion by proteinase K. Finally, MT1-MMP/MMP-14 but neither endogenous nor recombinant MMP-27 partitioned in the detergent phase after Triton X-114 extraction, indicating that MMP-27 is not an integral membrane protein.
24548619	0	37	theme	C-terminal	9:18	arg1	domain					20:25	A unique C-terminal domain	0:25	A unique C-terminal domain	0:25	A unique C-terminal domain allows retention of matrix metalloproteinase-27 in the endoplasmic reticulum.
24548619	4	38	theme	rMMP-27	617:623	arg1	retention					571:579	endoglycosidase H. Subcellular fractionation and confocal microscopy evidenced retention	492:579	endoglycosidase H. Subcellular fractionation and confocal microscopy evidenced retention of endogenous MMP-27 or recombinant rMMP-27 in the endoplasmic reticulum (ER)	492:657	Intracellular MMP-27 was sensitive to endoglycosidase H. Subcellular fractionation and confocal microscopy evidenced retention of endogenous MMP-27 or recombinant rMMP-27 in the endoplasmic reticulum (ER) with locked exit across the intermediate compartment (ERGIC).
24548619	4	39	from	retention	571:579	arg1	ER					655:656	ER	655:656	ER	655:656	Intracellular MMP-27 was sensitive to endoglycosidase H. Subcellular fractionation and confocal microscopy evidenced retention of endogenous MMP-27 or recombinant rMMP-27 in the endoplasmic reticulum (ER) with locked exit across the intermediate compartment (ERGIC).
24548619	4	39	from	retention	571:579	arg1	reticulum					644:652	the endoplasmic reticulum	628:652	the endoplasmic reticulum (ER)	628:657	Intracellular MMP-27 was sensitive to endoglycosidase H. Subcellular fractionation and confocal microscopy evidenced retention of endogenous MMP-27 or recombinant rMMP-27 in the endoplasmic reticulum (ER) with locked exit across the intermediate compartment (ERGIC).
24548619	4	40	theme	locked	664:669	arg1	exit					671:674	locked exit	664:674	locked exit	664:674	Intracellular MMP-27 was sensitive to endoglycosidase H. Subcellular fractionation and confocal microscopy evidenced retention of endogenous MMP-27 or recombinant rMMP-27 in the endoplasmic reticulum (ER) with locked exit across the intermediate compartment (ERGIC).
24548619	3	41	theme	CTE	415:417	arg1	contribution					419:430	CTE contribution	415:430	CTE contribution for MMP-27 retention	415:451	Having noticed that MMP-27 was barely secreted, we investigated its subcellular localization and addressed CTE contribution for MMP-27 retention.
24548619	4	42	theme	recombinant	605:615	arg1	rMMP-27					617:623	recombinant rMMP-27	605:623	recombinant rMMP-27	605:623	Intracellular MMP-27 was sensitive to endoglycosidase H. Subcellular fractionation and confocal microscopy evidenced retention of endogenous MMP-27 or recombinant rMMP-27 in the endoplasmic reticulum (ER) with locked exit across the intermediate compartment (ERGIC).
24548619	4	43	theme	Intracellular	454:466	arg1	MMP-27					468:473	Intracellular MMP-27	454:473	Intracellular MMP-27	454:473	Intracellular MMP-27 was sensitive to endoglycosidase H. Subcellular fractionation and confocal microscopy evidenced retention of endogenous MMP-27 or recombinant rMMP-27 in the endoplasmic reticulum (ER) with locked exit across the intermediate compartment (ERGIC).
24548619	2	44	theme	potential	241:249	arg1	domain					265:270	a potential transmembrane domain	239:270	a potential transmembrane domain as in some membrane-type (MT)-MMPs	239:305	Sequence comparison suggests that a C-terminal extension (CTE) includes a potential transmembrane domain as in some membrane-type (MT)-MMPs.
24548619	8	45	theme	detergent	1303:1311	arg1	phase					1313:1317	the detergent phase	1299:1317	the detergent phase after Triton X-114 extraction	1299:1347	Moreover, MMP-27 was protected from digestion by proteinase K. Finally, MT1-MMP/MMP-14 but neither endogenous nor recombinant MMP-27 partitioned in the detergent phase after Triton X-114 extraction, indicating that MMP-27 is not an integral membrane protein.
24548619	9	46	theme	unique	1481:1486	arg1	CTE					1488:1490	its unique CTE	1477:1490	its unique CTE	1477:1490	In conclusion, MMP-27 is efficiently retained within the ER due to its unique CTE, which does not lead to stable membrane insertion.
24548619	8	47	theme	X-114	1332:1336	arg1	extraction					1338:1347	Triton X-114 extraction	1325:1347	Triton X-114 extraction	1325:1347	Moreover, MMP-27 was protected from digestion by proteinase K. Finally, MT1-MMP/MMP-14 but neither endogenous nor recombinant MMP-27 partitioned in the detergent phase after Triton X-114 extraction, indicating that MMP-27 is not an integral membrane protein.
24548619	0	48	theme	matrix	47:52	arg1	metalloproteinase-27					54:73	matrix metalloproteinase-27	47:73	matrix metalloproteinase-27	47:73	A unique C-terminal domain allows retention of matrix metalloproteinase-27 in the endoplasmic reticulum.
24548619	4	49	theme	evidenced	561:569	arg1	retention					571:579	endoglycosidase H. Subcellular fractionation and confocal microscopy evidenced retention	492:579	endoglycosidase H. Subcellular fractionation and confocal microscopy evidenced retention of endogenous MMP-27 or recombinant rMMP-27 in the endoplasmic reticulum (ER)	492:657	Intracellular MMP-27 was sensitive to endoglycosidase H. Subcellular fractionation and confocal microscopy evidenced retention of endogenous MMP-27 or recombinant rMMP-27 in the endoplasmic reticulum (ER) with locked exit across the intermediate compartment (ERGIC).
24548619	6	50	theme	secreted	884:891	arg1	MMP					893:895	a secreted MMP	882:895	a secreted MMP	882:895	CTE addition to rMMP-10 (a secreted MMP) caused ER retention and blocked secretion.
24548619	6	50	theme	secreted	884:891	arg1	rMMP-10					873:879	rMMP-10	873:879	rMMP-10 (a secreted MMP)	873:896	CTE addition to rMMP-10 (a secreted MMP) caused ER retention and blocked secretion.
24548619	9	51	theme	stable	1516:1521	arg1	insertion					1532:1540	stable membrane insertion	1516:1540	stable membrane insertion	1516:1540	In conclusion, MMP-27 is efficiently retained within the ER due to its unique CTE, which does not lead to stable membrane insertion.
24548619	4	52	theme	endogenous	584:593	arg1	MMP-27					595:600	endogenous MMP-27	584:600	endogenous MMP-27	584:600	Intracellular MMP-27 was sensitive to endoglycosidase H. Subcellular fractionation and confocal microscopy evidenced retention of endogenous MMP-27 or recombinant rMMP-27 in the endoplasmic reticulum (ER) with locked exit across the intermediate compartment (ERGIC).
24548619	5	53	dep	compartments	793:804	arg1	ERGIC					807:811	ERGIC	807:811	ERGIC	807:811	Conversely, truncated rMMP-27 without CTE accessed downstream secretory compartments (ERGIC and Golgi) and was constitutively secreted.
24548619	5	53	dep	compartments	793:804	arg1	compartments					793:804	downstream secretory compartments	772:804	downstream secretory compartments (ERGIC and Golgi)	772:822	Conversely, truncated rMMP-27 without CTE accessed downstream secretory compartments (ERGIC and Golgi) and was constitutively secreted.
24548619	5	53	dep	compartments	793:804	arg1	Golgi					817:821	Golgi	817:821	Golgi	817:821	Conversely, truncated rMMP-27 without CTE accessed downstream secretory compartments (ERGIC and Golgi) and was constitutively secreted.
24548619	10	54	theme	ER	1572:1573	arg1	system					1585:1590	a novel ER retention system	1564:1590	a novel ER retention system	1564:1590	This could represent a novel ER retention system.
24548619	9	55	theme	membrane	1523:1530	arg1	insertion					1532:1540	stable membrane insertion	1516:1540	stable membrane insertion	1516:1540	In conclusion, MMP-27 is efficiently retained within the ER due to its unique CTE, which does not lead to stable membrane insertion.
24548619	7	56	theme	forskolin	1073:1081	arg1	stimulation					1083:1093	forskolin stimulation	1073:1093	forskolin stimulation	1073:1093	Addition of a PKA target sequence to the cytosolic C-terminus of transmembrane MT1-MMP/MMP-14 led to effective phosphorylation upon forskolin stimulation, but not for MMP-27, excluding transmembrane anchorage.
24548619	7	57	theme	effective	1042:1050	arg1	phosphorylation					1052:1066	effective phosphorylation	1042:1066	effective phosphorylation	1042:1066	Addition of a PKA target sequence to the cytosolic C-terminus of transmembrane MT1-MMP/MMP-14 led to effective phosphorylation upon forskolin stimulation, but not for MMP-27, excluding transmembrane anchorage.
24548619	7	58	theme	MT1-MMP/MMP-14	1020:1033	arg1	C-terminus					992:1001	the cytosolic C-terminus	978:1001	the cytosolic C-terminus of transmembrane MT1-MMP/MMP-14	978:1033	Addition of a PKA target sequence to the cytosolic C-terminus of transmembrane MT1-MMP/MMP-14 led to effective phosphorylation upon forskolin stimulation, but not for MMP-27, excluding transmembrane anchorage.
24548619	2	59	theme	C-terminal	203:212	arg1	extension					214:222	a C-terminal extension	201:222	a C-terminal extension (CTE)	201:228	Sequence comparison suggests that a C-terminal extension (CTE) includes a potential transmembrane domain as in some membrane-type (MT)-MMPs.
24548619	2	59	theme	C-terminal	203:212	arg1	CTE					225:227	CTE	225:227	CTE	225:227	Sequence comparison suggests that a C-terminal extension (CTE) includes a potential transmembrane domain as in some membrane-type (MT)-MMPs.
24548619	0	60	theme	metalloproteinase-27	54:73	arg1	retention					34:42	retention	34:42	retention of matrix metalloproteinase-27	34:73	A unique C-terminal domain allows retention of matrix metalloproteinase-27 in the endoplasmic reticulum.
24548619	2	61	theme	transmembrane	251:263	arg1	domain					265:270	a potential transmembrane domain	239:270	a potential transmembrane domain as in some membrane-type (MT)-MMPs	239:305	Sequence comparison suggests that a C-terminal extension (CTE) includes a potential transmembrane domain as in some membrane-type (MT)-MMPs.
24548619	0	62	theme	unique	2:7	arg1	domain					20:25	A unique C-terminal domain	0:25	A unique C-terminal domain	0:25	A unique C-terminal domain allows retention of matrix metalloproteinase-27 in the endoplasmic reticulum.
24548619	10	63	theme	retention	1575:1583	arg1	system					1585:1590	a novel ER retention system	1564:1590	a novel ER retention system	1564:1590	This could represent a novel ER retention system.
12407114	4	0	located	present	751:757	arg1	levels					787:792	very low or undetectable levels	762:792	very low or undetectable levels in other tissues	762:809	Real time PCR analysis revealed pp-GalNAc-T13 to be highly and restrictively expressed in the brain and present at very low or undetectable levels in other tissues, in contrast to the ubiquitous expression of pp-GalNAc-T1.
12407114	4	0	located	present	751:757	arg2	pp-GalNAc-T13					679:691	pp-GalNAc-T13	679:691	pp-GalNAc-T13 to be highly and restrictively expressed in the brain and present at very low or undetectable levels in other tissues	679:809	Real time PCR analysis revealed pp-GalNAc-T13 to be highly and restrictively expressed in the brain and present at very low or undetectable levels in other tissues, in contrast to the ubiquitous expression of pp-GalNAc-T1.
12407114	3	1	theme	amino	547:551	arg1	sequences					558:566	amino acid sequences	547:566	amino acid sequences	547:566	In amino acid sequences, pp-GalNAc-T13 was highly homologous, showing 84.3% identity, to pp-GalNAc-T1.
12407114	1	2	theme	polypeptide	311:321	arg1	N-acetylgalactosaminyltransferase					323:355	polypeptide N-acetylgalactosaminyltransferase	311:355	the UDP-N-acetyl-alpha-d-galactosamine:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) family	272:376	To date, 10 members of the UDP-N-acetyl-alpha-d-galactosamine:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) family have been cloned and analyzed in human.
12407114	1	2	theme	polypeptide	311:321	arg1	pp-GalNAc-T					358:368	pp-GalNAc-T	358:368	pp-GalNAc-T	358:368	To date, 10 members of the UDP-N-acetyl-alpha-d-galactosamine:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) family have been cloned and analyzed in human.
12407114	0	3	theme	N-acetylgalactosaminyltransferase	91:123	arg1	characterization					12:27	characterization	12:27	characterization	12:27	Cloning and characterization of a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, designated pp-GalNAc-T13, that is specifically expressed in neurons and synthesizes GalNAc alpha-serine/threonine antigen.
12407114	0	3	theme	N-acetylgalactosaminyltransferase	91:123	arg1	Cloning					0:6	Cloning	0:6	Cloning	0:6	Cloning and characterization of a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, designated pp-GalNAc-T13, that is specifically expressed in neurons and synthesizes GalNAc alpha-serine/threonine antigen.
12407114	2	4	from	library	504:510	arg1	pp-GalNAc-T					470:480	a novel human pp-GalNAc-T	456:480	a novel human pp-GalNAc-T from an NT2 cell cDNA library	456:510	In this study, we cloned and analyzed a novel human pp-GalNAc-T from an NT2 cell cDNA library, and we named it pp-GalNAc-T13.
12407114	0	5	theme	alpha-serine/threonine	217:238	arg1	antigen					240:246	GalNAc alpha-serine/threonine antigen	210:246	GalNAc alpha-serine/threonine antigen	210:246	Cloning and characterization of a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, designated pp-GalNAc-T13, that is specifically expressed in neurons and synthesizes GalNAc alpha-serine/threonine antigen.
12407114	3	6	theme	acid	553:556	arg1	sequences					558:566	amino acid sequences	547:566	amino acid sequences	547:566	In amino acid sequences, pp-GalNAc-T13 was highly homologous, showing 84.3% identity, to pp-GalNAc-T1.
12407114	1	7	theme	N-acetylgalactosaminyltransferase	323:355	arg1	family					371:376	the UDP-N-acetyl-alpha-d-galactosamine:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) family	272:376	the UDP-N-acetyl-alpha-d-galactosamine:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) family	272:376	To date, 10 members of the UDP-N-acetyl-alpha-d-galactosamine:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) family have been cloned and analyzed in human.
12407114	11	8	theme	antigen	1728:1734	arg1	epitope					1736:1742	specifically the Tn antigen epitope	1708:1742	specifically the Tn antigen epitope	1708:1742	pp-GalNAc-T13 would be a major enzyme responsible for the synthesis of O-glycan and specifically the Tn antigen epitope in neurons.
12407114	6	9	dep	did	1152:1154	arg1	than					1147:1150	than	1147:1150	than	1147:1150	pp-GalNAc-T13 exhibited much stronger activity to transfer GalNAc to mucin peptides, such as Muc5Ac and MUC7, than did pp-GalNAc-T1.
12407114	4	10	theme	other	797:801	arg1	tissues					803:809	other tissues	797:809	other tissues	797:809	Real time PCR analysis revealed pp-GalNAc-T13 to be highly and restrictively expressed in the brain and present at very low or undetectable levels in other tissues, in contrast to the ubiquitous expression of pp-GalNAc-T1.
12407114	3	11	from	homologous	594:603	arg1	sequences					558:566	amino acid sequences	547:566	amino acid sequences	547:566	In amino acid sequences, pp-GalNAc-T13 was highly homologous, showing 84.3% identity, to pp-GalNAc-T1.
12407114	3	12	from	sequences	558:566	arg1	homologous					594:603	homologous	594:603	homologous	594:603	In amino acid sequences, pp-GalNAc-T13 was highly homologous, showing 84.3% identity, to pp-GalNAc-T1.
12407114	5	13	theme	cultured	1016:1023	arg1	astrocytes					1025:1034	primary cultured astrocytes	1008:1034	primary cultured astrocytes	1008:1034	pp-GalNAc-T13 was abundantly expressed in all neuroblastoma cells examined and primary cultured neurons but not in glioblastoma cells and primary cultured astrocytes.
12407114	4	14	theme	low	767:769	arg1	levels					787:792	very low or undetectable levels	762:792	very low or undetectable levels in other tissues	762:809	Real time PCR analysis revealed pp-GalNAc-T13 to be highly and restrictively expressed in the brain and present at very low or undetectable levels in other tissues, in contrast to the ubiquitous expression of pp-GalNAc-T1.
12407114	10	15	theme	remarkable	1524:1533	arg1	decrease					1535:1542	a remarkable decrease	1522:1542	a remarkable decrease in Tn antigen expression in the cerebellum of the pp-GalNAc-T13 knockout mouse	1522:1621	Immunohistochemical study showed a remarkable decrease in Tn antigen expression in the cerebellum of the pp-GalNAc-T13 knockout mouse.
12407114	2	16	theme	novel	458:462	arg1	pp-GalNAc-T					470:480	a novel human pp-GalNAc-T	456:480	a novel human pp-GalNAc-T from an NT2 cell cDNA library	456:510	In this study, we cloned and analyzed a novel human pp-GalNAc-T from an NT2 cell cDNA library, and we named it pp-GalNAc-T13.
12407114	5	17	theme	primary	949:955	arg1	neurons					966:972	primary cultured neurons	949:972	primary cultured neurons	949:972	pp-GalNAc-T13 was abundantly expressed in all neuroblastoma cells examined and primary cultured neurons but not in glioblastoma cells and primary cultured astrocytes.
12407114	6	18	theme	stronger	1066:1073	arg1	activity					1075:1082	much stronger activity	1061:1082	much stronger activity	1061:1082	pp-GalNAc-T13 exhibited much stronger activity to transfer GalNAc to mucin peptides, such as Muc5Ac and MUC7, than did pp-GalNAc-T1.
12407114	4	19	from	levels	787:792	arg1	present					751:757	present	751:757	present	751:757	Real time PCR analysis revealed pp-GalNAc-T13 to be highly and restrictively expressed in the brain and present at very low or undetectable levels in other tissues, in contrast to the ubiquitous expression of pp-GalNAc-T1.
12407114	4	19	from	levels	787:792	arg1	tissues					803:809	other tissues	797:809	other tissues	797:809	Real time PCR analysis revealed pp-GalNAc-T13 to be highly and restrictively expressed in the brain and present at very low or undetectable levels in other tissues, in contrast to the ubiquitous expression of pp-GalNAc-T1.
12407114	8	20	theme	Tn	1289:1290	arg1	structures					1334:1343	three consecutive GalNAc-Ser/Thr structures	1301:1343	three consecutive GalNAc-Ser/Thr structures	1301:1343	pp-GalNAc-T13 was able to form a triplet Tn epitope, three consecutive GalNAc-Ser/Thr structures, on peptides encoded in syndecan-3, a proteoglycan expressed in neurons.
12407114	8	20	theme	Tn	1289:1290	arg1	epitope					1292:1298	a triplet Tn epitope	1279:1298	a triplet Tn epitope	1279:1298	pp-GalNAc-T13 was able to form a triplet Tn epitope, three consecutive GalNAc-Ser/Thr structures, on peptides encoded in syndecan-3, a proteoglycan expressed in neurons.
12407114	10	21	theme	Tn	1547:1548	arg1	expression					1558:1567	Tn antigen expression	1547:1567	Tn antigen expression in the cerebellum of the pp-GalNAc-T13 knockout mouse	1547:1621	Immunohistochemical study showed a remarkable decrease in Tn antigen expression in the cerebellum of the pp-GalNAc-T13 knockout mouse.
12407114	10	22	theme	Immunohistochemical	1489:1507	arg1	study					1509:1513	Immunohistochemical study	1489:1513	Immunohistochemical study	1489:1513	Immunohistochemical study showed a remarkable decrease in Tn antigen expression in the cerebellum of the pp-GalNAc-T13 knockout mouse.
12407114	3	23	theme	84.3	614:617	arg1	%					618:618	%	618:618	%	618:618	In amino acid sequences, pp-GalNAc-T13 was highly homologous, showing 84.3% identity, to pp-GalNAc-T1.
12407114	2	24	theme	cDNA	499:502	arg1	library					504:510	an NT2 cell cDNA library	487:510	an NT2 cell cDNA library	487:510	In this study, we cloned and analyzed a novel human pp-GalNAc-T from an NT2 cell cDNA library, and we named it pp-GalNAc-T13.
12407114	3	25	theme	%	618:618	arg1	identity					620:627	84.3% identity	614:627	84.3% identity	614:627	In amino acid sequences, pp-GalNAc-T13 was highly homologous, showing 84.3% identity, to pp-GalNAc-T1.
12407114	11	26	theme	Tn	1725:1726	arg1	epitope					1736:1742	specifically the Tn antigen epitope	1708:1742	specifically the Tn antigen epitope	1708:1742	pp-GalNAc-T13 would be a major enzyme responsible for the synthesis of O-glycan and specifically the Tn antigen epitope in neurons.
12407114	5	27	theme	neuroblastoma	916:928	arg1	cells					930:934	all neuroblastoma cells	912:934	all neuroblastoma cells examined	912:943	pp-GalNAc-T13 was abundantly expressed in all neuroblastoma cells examined and primary cultured neurons but not in glioblastoma cells and primary cultured astrocytes.
12407114	2	28	theme	cell	494:497	arg1	library					504:510	an NT2 cell cDNA library	487:510	an NT2 cell cDNA library	487:510	In this study, we cloned and analyzed a novel human pp-GalNAc-T from an NT2 cell cDNA library, and we named it pp-GalNAc-T13.
12407114	1	29	theme	family	371:376	arg1	members					261:267	10 members	258:267	10 members of the UDP-N-acetyl-alpha-d-galactosamine:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) family	258:376	To date, 10 members of the UDP-N-acetyl-alpha-d-galactosamine:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) family have been cloned and analyzed in human.
12407114	11	30	theme	major	1649:1653	arg1	enzyme					1655:1660	a major enzyme	1647:1660	a major enzyme responsible for the synthesis of O-glycan and specifically the Tn antigen epitope in neurons	1647:1753	pp-GalNAc-T13 would be a major enzyme responsible for the synthesis of O-glycan and specifically the Tn antigen epitope in neurons.
12407114	11	30	theme	major	1649:1653	arg1	pp-GalNAc-T13					1624:1636	pp-GalNAc-T13	1624:1636	pp-GalNAc-T13	1624:1636	pp-GalNAc-T13 would be a major enzyme responsible for the synthesis of O-glycan and specifically the Tn antigen epitope in neurons.
12407114	8	31	theme	GalNAc-Ser/Thr	1319:1332	arg1	structures					1334:1343	three consecutive GalNAc-Ser/Thr structures	1301:1343	three consecutive GalNAc-Ser/Thr structures	1301:1343	pp-GalNAc-T13 was able to form a triplet Tn epitope, three consecutive GalNAc-Ser/Thr structures, on peptides encoded in syndecan-3, a proteoglycan expressed in neurons.
12407114	8	31	theme	GalNAc-Ser/Thr	1319:1332	arg1	epitope					1292:1298	a triplet Tn epitope	1279:1298	a triplet Tn epitope	1279:1298	pp-GalNAc-T13 was able to form a triplet Tn epitope, three consecutive GalNAc-Ser/Thr structures, on peptides encoded in syndecan-3, a proteoglycan expressed in neurons.
12407114	2	32	theme	NT2	490:492	arg1	library					504:510	an NT2 cell cDNA library	487:510	an NT2 cell cDNA library	487:510	In this study, we cloned and analyzed a novel human pp-GalNAc-T from an NT2 cell cDNA library, and we named it pp-GalNAc-T13.
12407114	10	33	from	decrease	1535:1542	arg1	expression					1558:1567	Tn antigen expression	1547:1567	Tn antigen expression in the cerebellum of the pp-GalNAc-T13 knockout mouse	1547:1621	Immunohistochemical study showed a remarkable decrease in Tn antigen expression in the cerebellum of the pp-GalNAc-T13 knockout mouse.
12407114	5	34	theme	glioblastoma	985:996	arg1	cells					998:1002	glioblastoma cells	985:1002	glioblastoma cells	985:1002	pp-GalNAc-T13 was abundantly expressed in all neuroblastoma cells examined and primary cultured neurons but not in glioblastoma cells and primary cultured astrocytes.
12407114	4	35	theme	undetectable	774:785	arg1	levels					787:792	very low or undetectable levels	762:792	very low or undetectable levels in other tissues	762:809	Real time PCR analysis revealed pp-GalNAc-T13 to be highly and restrictively expressed in the brain and present at very low or undetectable levels in other tissues, in contrast to the ubiquitous expression of pp-GalNAc-T1.
12407114	8	36	theme	consecutive	1307:1317	arg1	structures					1334:1343	three consecutive GalNAc-Ser/Thr structures	1301:1343	three consecutive GalNAc-Ser/Thr structures	1301:1343	pp-GalNAc-T13 was able to form a triplet Tn epitope, three consecutive GalNAc-Ser/Thr structures, on peptides encoded in syndecan-3, a proteoglycan expressed in neurons.
12407114	8	36	theme	consecutive	1307:1317	arg1	epitope					1292:1298	a triplet Tn epitope	1279:1298	a triplet Tn epitope	1279:1298	pp-GalNAc-T13 was able to form a triplet Tn epitope, three consecutive GalNAc-Ser/Thr structures, on peptides encoded in syndecan-3, a proteoglycan expressed in neurons.
12407114	0	37	theme	new	34:36	arg1	N-acetylgalactosaminyltransferase					91:123	a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase	32:123	a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase	32:123	Cloning and characterization of a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, designated pp-GalNAc-T13, that is specifically expressed in neurons and synthesizes GalNAc alpha-serine/threonine antigen.
12407114	6	38	theme	mucin	1106:1110	arg1	peptides					1112:1119	mucin peptides	1106:1119	mucin peptides	1106:1119	pp-GalNAc-T13 exhibited much stronger activity to transfer GalNAc to mucin peptides, such as Muc5Ac and MUC7, than did pp-GalNAc-T1.
12407114	6	38	theme	mucin	1106:1110	arg1	MUC7					1141:1144	MUC7	1141:1144	MUC7	1141:1144	pp-GalNAc-T13 exhibited much stronger activity to transfer GalNAc to mucin peptides, such as Muc5Ac and MUC7, than did pp-GalNAc-T1.
12407114	6	38	theme	mucin	1106:1110	arg1	Muc5Ac					1130:1135	Muc5Ac	1130:1135	Muc5Ac	1130:1135	pp-GalNAc-T13 exhibited much stronger activity to transfer GalNAc to mucin peptides, such as Muc5Ac and MUC7, than did pp-GalNAc-T1.
12407114	4	39	dep	expression	842:851	arg1	contrast					815:822	contrast	815:822	contrast	815:822	Real time PCR analysis revealed pp-GalNAc-T13 to be highly and restrictively expressed in the brain and present at very low or undetectable levels in other tissues, in contrast to the ubiquitous expression of pp-GalNAc-T1.
12407114	9	40	theme	pp-GalNAc-T13-deficient	1418:1440	arg1	mice					1442:1445	pp-GalNAc-T13-deficient mice	1418:1445	pp-GalNAc-T13-deficient mice	1418:1445	pp-GalNAc-T13-deficient mice have been established in a previous work.
12407114	4	41	theme	PCR	657:659	arg1	analysis					661:668	Real time PCR analysis	647:668	Real time PCR analysis	647:668	Real time PCR analysis revealed pp-GalNAc-T13 to be highly and restrictively expressed in the brain and present at very low or undetectable levels in other tissues, in contrast to the ubiquitous expression of pp-GalNAc-T1.
12407114	2	42	theme	human	464:468	arg1	pp-GalNAc-T					470:480	a novel human pp-GalNAc-T	456:480	a novel human pp-GalNAc-T from an NT2 cell cDNA library	456:510	In this study, we cloned and analyzed a novel human pp-GalNAc-T from an NT2 cell cDNA library, and we named it pp-GalNAc-T13.
12407114	0	43	theme	UDP-N-acetyl-alpha-D-galactosamine	44:77	arg1	N-acetylgalactosaminyltransferase					91:123	a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase	32:123	a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase	32:123	Cloning and characterization of a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, designated pp-GalNAc-T13, that is specifically expressed in neurons and synthesizes GalNAc alpha-serine/threonine antigen.
12407114	10	44	theme	mouse	1617:1621	arg1	cerebellum					1576:1585	the cerebellum	1572:1585	the cerebellum of the pp-GalNAc-T13 knockout mouse	1572:1621	Immunohistochemical study showed a remarkable decrease in Tn antigen expression in the cerebellum of the pp-GalNAc-T13 knockout mouse.
12407114	4	45	theme	pp-GalNAc-T1	856:867	arg1	expression					842:851	the ubiquitous expression	827:851	the ubiquitous expression of pp-GalNAc-T1	827:867	Real time PCR analysis revealed pp-GalNAc-T13 to be highly and restrictively expressed in the brain and present at very low or undetectable levels in other tissues, in contrast to the ubiquitous expression of pp-GalNAc-T1.
12407114	10	46	theme	pp-GalNAc-T13	1594:1606	arg1	mouse					1617:1621	the pp-GalNAc-T13 knockout mouse	1590:1621	the pp-GalNAc-T13 knockout mouse	1590:1621	Immunohistochemical study showed a remarkable decrease in Tn antigen expression in the cerebellum of the pp-GalNAc-T13 knockout mouse.
12407114	5	47	theme	cultured	957:964	arg1	neurons					966:972	primary cultured neurons	949:972	primary cultured neurons	949:972	pp-GalNAc-T13 was abundantly expressed in all neuroblastoma cells examined and primary cultured neurons but not in glioblastoma cells and primary cultured astrocytes.
12407114	0	48	theme	human	38:42	arg1	N-acetylgalactosaminyltransferase					91:123	a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase	32:123	a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase	32:123	Cloning and characterization of a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, designated pp-GalNAc-T13, that is specifically expressed in neurons and synthesizes GalNAc alpha-serine/threonine antigen.
12407114	10	49	from	expression	1558:1567	arg1	cerebellum					1576:1585	the cerebellum	1572:1585	the cerebellum of the pp-GalNAc-T13 knockout mouse	1572:1621	Immunohistochemical study showed a remarkable decrease in Tn antigen expression in the cerebellum of the pp-GalNAc-T13 knockout mouse.
12407114	10	50	theme	knockout	1608:1615	arg1	mouse					1617:1621	the pp-GalNAc-T13 knockout mouse	1590:1621	the pp-GalNAc-T13 knockout mouse	1590:1621	Immunohistochemical study showed a remarkable decrease in Tn antigen expression in the cerebellum of the pp-GalNAc-T13 knockout mouse.
12407114	10	51	theme	antigen	1550:1556	arg1	expression					1558:1567	Tn antigen expression	1547:1567	Tn antigen expression in the cerebellum of the pp-GalNAc-T13 knockout mouse	1547:1621	Immunohistochemical study showed a remarkable decrease in Tn antigen expression in the cerebellum of the pp-GalNAc-T13 knockout mouse.
12407114	8	52	from	epitope	1292:1298	arg1	peptides					1349:1356	peptides	1349:1356	peptides encoded in syndecan-3, a proteoglycan expressed in neurons	1349:1415	pp-GalNAc-T13 was able to form a triplet Tn epitope, three consecutive GalNAc-Ser/Thr structures, on peptides encoded in syndecan-3, a proteoglycan expressed in neurons.
12407114	11	53	theme	responsible	1662:1672	arg1	enzyme					1655:1660	a major enzyme	1647:1660	a major enzyme responsible for the synthesis of O-glycan and specifically the Tn antigen epitope in neurons	1647:1753	pp-GalNAc-T13 would be a major enzyme responsible for the synthesis of O-glycan and specifically the Tn antigen epitope in neurons.
12407114	11	53	theme	responsible	1662:1672	arg1	pp-GalNAc-T13					1624:1636	pp-GalNAc-T13	1624:1636	pp-GalNAc-T13	1624:1636	pp-GalNAc-T13 would be a major enzyme responsible for the synthesis of O-glycan and specifically the Tn antigen epitope in neurons.
12407114	7	54	theme	substrate	1209:1217	arg1	specificity					1219:1229	substrate specificity	1209:1229	substrate specificity to pp-GalNAc-T1	1209:1245	In addition, pp-GalNAc-T13 differed in substrate specificity to pp-GalNAc-T1.
12407114	0	55	theme	GalNAc	210:215	arg1	antigen					240:246	GalNAc alpha-serine/threonine antigen	210:246	GalNAc alpha-serine/threonine antigen	210:246	Cloning and characterization of a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, designated pp-GalNAc-T13, that is specifically expressed in neurons and synthesizes GalNAc alpha-serine/threonine antigen.
12407114	4	56	theme	ubiquitous	831:840	arg1	expression					842:851	the ubiquitous expression	827:851	the ubiquitous expression of pp-GalNAc-T1	827:867	Real time PCR analysis revealed pp-GalNAc-T13 to be highly and restrictively expressed in the brain and present at very low or undetectable levels in other tissues, in contrast to the ubiquitous expression of pp-GalNAc-T1.
12407114	4	57	theme	Real	647:650	arg1	analysis					661:668	Real time PCR analysis	647:668	Real time PCR analysis	647:668	Real time PCR analysis revealed pp-GalNAc-T13 to be highly and restrictively expressed in the brain and present at very low or undetectable levels in other tissues, in contrast to the ubiquitous expression of pp-GalNAc-T1.
12407114	5	58	theme	primary	1008:1014	arg1	astrocytes					1025:1034	primary cultured astrocytes	1008:1034	primary cultured astrocytes	1008:1034	pp-GalNAc-T13 was abundantly expressed in all neuroblastoma cells examined and primary cultured neurons but not in glioblastoma cells and primary cultured astrocytes.
12407114	11	59	from	synthesis	1682:1690	arg1	neurons					1747:1753	neurons	1747:1753	neurons	1747:1753	pp-GalNAc-T13 would be a major enzyme responsible for the synthesis of O-glycan and specifically the Tn antigen epitope in neurons.
12407114	0	60	theme	polypeptide	79:89	arg1	N-acetylgalactosaminyltransferase					91:123	a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase	32:123	a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase	32:123	Cloning and characterization of a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, designated pp-GalNAc-T13, that is specifically expressed in neurons and synthesizes GalNAc alpha-serine/threonine antigen.
12407114	1	61	theme	UDP-N-acetyl-alpha-d-galactosamine	276:309	arg1	family					371:376	the UDP-N-acetyl-alpha-d-galactosamine:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) family	272:376	the UDP-N-acetyl-alpha-d-galactosamine:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) family	272:376	To date, 10 members of the UDP-N-acetyl-alpha-d-galactosamine:polypeptide N-acetylgalactosaminyltransferase (pp-GalNAc-T) family have been cloned and analyzed in human.
12407114	8	62	theme	triplet	1281:1287	arg1	structures					1334:1343	three consecutive GalNAc-Ser/Thr structures	1301:1343	three consecutive GalNAc-Ser/Thr structures	1301:1343	pp-GalNAc-T13 was able to form a triplet Tn epitope, three consecutive GalNAc-Ser/Thr structures, on peptides encoded in syndecan-3, a proteoglycan expressed in neurons.
12407114	8	62	theme	triplet	1281:1287	arg1	epitope					1292:1298	a triplet Tn epitope	1279:1298	a triplet Tn epitope	1279:1298	pp-GalNAc-T13 was able to form a triplet Tn epitope, three consecutive GalNAc-Ser/Thr structures, on peptides encoded in syndecan-3, a proteoglycan expressed in neurons.
12407114	11	63	theme	epitope	1736:1742	arg1	synthesis					1682:1690	the synthesis	1678:1690	the synthesis of O-glycan and specifically the Tn antigen epitope in neurons	1678:1753	pp-GalNAc-T13 would be a major enzyme responsible for the synthesis of O-glycan and specifically the Tn antigen epitope in neurons.
12407114	9	64	theme	previous	1474:1481	arg1	work					1483:1486	a previous work	1472:1486	a previous work	1472:1486	pp-GalNAc-T13-deficient mice have been established in a previous work.
12407114	11	65	theme	O-glycan	1695:1702	arg1	synthesis					1682:1690	the synthesis	1678:1690	the synthesis of O-glycan and specifically the Tn antigen epitope in neurons	1678:1753	pp-GalNAc-T13 would be a major enzyme responsible for the synthesis of O-glycan and specifically the Tn antigen epitope in neurons.
12407114	4	66	theme	time	652:655	arg1	analysis					661:668	Real time PCR analysis	647:668	Real time PCR analysis	647:668	Real time PCR analysis revealed pp-GalNAc-T13 to be highly and restrictively expressed in the brain and present at very low or undetectable levels in other tissues, in contrast to the ubiquitous expression of pp-GalNAc-T1.
17881000	12	0	theme	His96-99-57	2057:2067	arg1	triad					2069:2073	The His96-99-57 triad	2053:2073	The His96-99-57 triad	2053:2073	The His96-99-57 triad is thus suggested to be responsible for the Zn2+-mediated inhibition of hK5 catalysis.
17881000	12	0	theme	His96-99-57	2057:2067	arg1	responsible					2099:2109	responsible	2099:2109	responsible	2099:2109	The His96-99-57 triad is thus suggested to be responsible for the Zn2+-mediated inhibition of hK5 catalysis.
17881000	8	1	theme	triad	1435:1439	arg1	position					1441:1448	its triad position to provide the third co-ordination site of the bound Zn2+, rendering Zn2+-bound hK5 inactive	1431:1541	its triad position to provide the third co-ordination site of the bound Zn2+, rendering Zn2+-bound hK5 inactive	1431:1541	Modeling studies show that in the absence of bound leupeptin, Zn2+ is likely further coordinated by the imidazolyl side-chain of the catalytic His57 which can, similar to equivalent His57 imidazole groups in the related rat kallikrein proteinase tonin and in an engineered metal-binding rat trypsin, rotate out of its triad position to provide the third co-ordination site of the bound Zn2+, rendering Zn2+-bound hK5 inactive.
17881000	8	2	theme	bound	1497:1501	arg1	Zn2+					1503:1506	the bound Zn2+	1493:1506	the bound Zn2+	1493:1506	Modeling studies show that in the absence of bound leupeptin, Zn2+ is likely further coordinated by the imidazolyl side-chain of the catalytic His57 which can, similar to equivalent His57 imidazole groups in the related rat kallikrein proteinase tonin and in an engineered metal-binding rat trypsin, rotate out of its triad position to provide the third co-ordination site of the bound Zn2+, rendering Zn2+-bound hK5 inactive.
17881000	9	3	theme	inhibition	1673:1682	arg1	analyses					1656:1663	kinetic analyses	1648:1663	kinetic analyses of Zn2+ inhibition	1648:1682	In solution, this mode of binding likely occurs in the presence of free and substrate saturated hK5, as kinetic analyses of Zn2+ inhibition indicate a non-competitive mechanism.
17881000	10	4	theme	His57	1737:1741	arg1	re-orientation					1743:1756	the His57 re-orientation	1733:1756	the His57 re-orientation	1733:1756	Supporting the His57 re-orientation, Zn2+ does not fully inhibit hK5 hydrolysis of tripeptidyl substrates containing a P2-His residue.
17881000	7	5	theme	large	1013:1017	arg1	shift					1019:1023	a large shift	1011:1023	a large shift in the backbone conformation of the 99-loop and by large movements of both His side-chains	1011:1114	This zinc binding is accompanied by a large shift in the backbone conformation of the 99-loop and by large movements of both His side-chains.
17881000	8	6	theme	Zn2+-bound	1519:1528	arg1	hK5					1530:1532	Zn2+-bound hK5 inactive	1519:1541	Zn2+-bound hK5 inactive	1519:1541	Modeling studies show that in the absence of bound leupeptin, Zn2+ is likely further coordinated by the imidazolyl side-chain of the catalytic His57 which can, similar to equivalent His57 imidazole groups in the related rat kallikrein proteinase tonin and in an engineered metal-binding rat trypsin, rotate out of its triad position to provide the third co-ordination site of the bound Zn2+, rendering Zn2+-bound hK5 inactive.
17881000	1	7	theme	family	132:137	arg1	kallikrein					76:85	Human kallikrein 5	70:87	Human kallikrein 5 (hK5)	70:93	Human kallikrein 5 (hK5) is a member of the tissue kallikrein family of serine peptidases.
17881000	1	7	theme	family	132:137	arg1	member					100:105	a member	98:105	a member of the tissue kallikrein family of serine peptidases	98:158	Human kallikrein 5 (hK5) is a member of the tissue kallikrein family of serine peptidases.
17881000	11	8	from	other	1914:1918	arg1	complex					1944:1950	the enzyme-substrate complex	1923:1950	the enzyme-substrate complex	1923:1950	The P2 and His57 imidazole groups would lie next to each other in the enzyme-substrate complex, indicating that incomplete inhibition is due to competition between both imidazole groups for Zn2+.
17881000	8	9	theme	inactive	1534:1541	arg1	hK5					1530:1532	Zn2+-bound hK5 inactive	1519:1541	Zn2+-bound hK5 inactive	1519:1541	Modeling studies show that in the absence of bound leupeptin, Zn2+ is likely further coordinated by the imidazolyl side-chain of the catalytic His57 which can, similar to equivalent His57 imidazole groups in the related rat kallikrein proteinase tonin and in an engineered metal-binding rat trypsin, rotate out of its triad position to provide the third co-ordination site of the bound Zn2+, rendering Zn2+-bound hK5 inactive.
17881000	1	10	theme	serine	142:147	arg1	peptidases					149:158	serine peptidases	142:158	serine peptidases	142:158	Human kallikrein 5 (hK5) is a member of the tissue kallikrein family of serine peptidases.
17881000	11	11	theme	P2	1861:1862	arg1	groups					1884:1889	The P2 and His57 imidazole groups	1857:1889	The P2 and His57 imidazole groups	1857:1889	The P2 and His57 imidazole groups would lie next to each other in the enzyme-substrate complex, indicating that incomplete inhibition is due to competition between both imidazole groups for Zn2+.
17881000	3	12	theme	aldehyde	485:492	arg1	leupeptin					504:512	the tripeptidyl aldehyde inhibitor leupeptin	469:512	the tripeptidyl aldehyde inhibitor leupeptin	469:512	To further understand the interaction of hK5 with substrates and metal ions, active recombinant hK5 was crystallized in complex with the tripeptidyl aldehyde inhibitor leupeptin, and structures at 2.3 A resolution were obtained with and without Zn2+.
17881000	8	13	theme	His57	1260:1264	arg1	side-chain					1232:1241	the imidazolyl side-chain	1217:1241	the imidazolyl side-chain of the catalytic His57 which can, similar to equivalent His57 imidazole groups in the related rat kallikrein proteinase tonin and in an engineered metal-binding rat trypsin, rotate out of its triad position to provide the third co-ordination site of the bound Zn2+, rendering Zn2+-bound hK5 inactive	1217:1541	Modeling studies show that in the absence of bound leupeptin, Zn2+ is likely further coordinated by the imidazolyl side-chain of the catalytic His57 which can, similar to equivalent His57 imidazole groups in the related rat kallikrein proteinase tonin and in an engineered metal-binding rat trypsin, rotate out of its triad position to provide the third co-ordination site of the bound Zn2+, rendering Zn2+-bound hK5 inactive.
17881000	10	14	theme	hK5	1787:1789	arg1	hydrolysis					1791:1800	hK5 hydrolysis	1787:1800	hK5 hydrolysis of tripeptidyl substrates containing a P2-His residue	1787:1854	Supporting the His57 re-orientation, Zn2+ does not fully inhibit hK5 hydrolysis of tripeptidyl substrates containing a P2-His residue.
17881000	2	15	contain	has	164:166	arg1	It					161:162	It	161:162	It	161:162	It has trypsin-like substrate specificity, is inhibited by metal ions, and is abundantly expressed in human skin, where it is believed to play a central role in desquamation.
17881000	2	15	contain	has	164:166	arg2	specificity					191:201	trypsin-like substrate specificity	168:201	trypsin-like substrate specificity	168:201	It has trypsin-like substrate specificity, is inhibited by metal ions, and is abundantly expressed in human skin, where it is believed to play a central role in desquamation.
17881000	8	16	theme	Modeling	1117:1124	arg1	studies					1126:1132	Modeling studies	1117:1132	Modeling studies	1117:1132	Modeling studies show that in the absence of bound leupeptin, Zn2+ is likely further coordinated by the imidazolyl side-chain of the catalytic His57 which can, similar to equivalent His57 imidazole groups in the related rat kallikrein proteinase tonin and in an engineered metal-binding rat trypsin, rotate out of its triad position to provide the third co-ordination site of the bound Zn2+, rendering Zn2+-bound hK5 inactive.
17881000	2	17	theme	trypsin-like	168:179	arg1	specificity					191:201	trypsin-like substrate specificity	168:201	trypsin-like substrate specificity	168:201	It has trypsin-like substrate specificity, is inhibited by metal ions, and is abundantly expressed in human skin, where it is believed to play a central role in desquamation.
17881000	11	18	theme	His57	1868:1872	arg1	groups					1884:1889	The P2 and His57 imidazole groups	1857:1889	The P2 and His57 imidazole groups	1857:1889	The P2 and His57 imidazole groups would lie next to each other in the enzyme-substrate complex, indicating that incomplete inhibition is due to competition between both imidazole groups for Zn2+.
17881000	4	19	theme	pocket	641:646	arg1	similar					675:681	similar	675:681	similar	675:681	While the overall structure and the specificity of S1 pocket for basic side-chains were similar to that of hK4, a closely related family member, both differed in their interaction with Zn2+.
17881000	4	19	theme	pocket	641:646	arg1	structure					605:613	the overall structure	593:613	the overall structure	593:613	While the overall structure and the specificity of S1 pocket for basic side-chains were similar to that of hK4, a closely related family member, both differed in their interaction with Zn2+.
17881000	4	19	theme	pocket	641:646	arg1	specificity					623:633	the specificity	619:633	the specificity of S1 pocket for basic side-chains	619:668	While the overall structure and the specificity of S1 pocket for basic side-chains were similar to that of hK4, a closely related family member, both differed in their interaction with Zn2+.
17881000	10	20	theme	substrates	1817:1826	arg1	hydrolysis					1791:1800	hK5 hydrolysis	1787:1800	hK5 hydrolysis of tripeptidyl substrates containing a P2-His residue	1787:1854	Supporting the His57 re-orientation, Zn2+ does not fully inhibit hK5 hydrolysis of tripeptidyl substrates containing a P2-His residue.
17881000	6	21	theme	active	879:884	arg1	site					886:889	the active site	875:889	the active site	875:889	Instead, Zn2+ binds adjacent to the active site, becoming coordinated by the imidazole rings of His99 and His96 not present in hK4.
17881000	8	22	theme	equivalent	1288:1297	arg1	groups					1315:1320	equivalent His57 imidazole groups	1288:1320	equivalent His57 imidazole groups in the related rat kallikrein proteinase tonin and in an engineered metal-binding rat trypsin	1288:1414	Modeling studies show that in the absence of bound leupeptin, Zn2+ is likely further coordinated by the imidazolyl side-chain of the catalytic His57 which can, similar to equivalent His57 imidazole groups in the related rat kallikrein proteinase tonin and in an engineered metal-binding rat trypsin, rotate out of its triad position to provide the third co-ordination site of the bound Zn2+, rendering Zn2+-bound hK5 inactive.
17881000	7	23	theme	99-loop	1061:1067	arg1	conformation					1041:1052	the backbone conformation	1028:1052	the backbone conformation of the 99-loop	1028:1067	This zinc binding is accompanied by a large shift in the backbone conformation of the 99-loop and by large movements of both His side-chains.
17881000	3	24	theme	A	537:537	arg1	resolution					539:548	2.3 A resolution	533:548	2.3 A resolution	533:548	To further understand the interaction of hK5 with substrates and metal ions, active recombinant hK5 was crystallized in complex with the tripeptidyl aldehyde inhibitor leupeptin, and structures at 2.3 A resolution were obtained with and without Zn2+.
17881000	8	25	theme	imidazole	1305:1313	arg1	groups					1315:1320	equivalent His57 imidazole groups	1288:1320	equivalent His57 imidazole groups in the related rat kallikrein proteinase tonin and in an engineered metal-binding rat trypsin	1288:1414	Modeling studies show that in the absence of bound leupeptin, Zn2+ is likely further coordinated by the imidazolyl side-chain of the catalytic His57 which can, similar to equivalent His57 imidazole groups in the related rat kallikrein proteinase tonin and in an engineered metal-binding rat trypsin, rotate out of its triad position to provide the third co-ordination site of the bound Zn2+, rendering Zn2+-bound hK5 inactive.
17881000	11	26	from	complex	1944:1950	arg1	other					1914:1918	other	1914:1918	other	1914:1918	The P2 and His57 imidazole groups would lie next to each other in the enzyme-substrate complex, indicating that incomplete inhibition is due to competition between both imidazole groups for Zn2+.
17881000	1	27	theme	tissue	114:119	arg1	family					132:137	the tissue kallikrein family	110:137	the tissue kallikrein family of serine peptidases	110:158	Human kallikrein 5 (hK5) is a member of the tissue kallikrein family of serine peptidases.
17881000	8	28	theme	bound	1162:1166	arg1	leupeptin					1168:1176	bound leupeptin	1162:1176	bound leupeptin	1162:1176	Modeling studies show that in the absence of bound leupeptin, Zn2+ is likely further coordinated by the imidazolyl side-chain of the catalytic His57 which can, similar to equivalent His57 imidazole groups in the related rat kallikrein proteinase tonin and in an engineered metal-binding rat trypsin, rotate out of its triad position to provide the third co-ordination site of the bound Zn2+, rendering Zn2+-bound hK5 inactive.
17881000	7	29	theme	backbone	1032:1039	arg1	conformation					1041:1052	the backbone conformation	1028:1052	the backbone conformation of the 99-loop	1028:1067	This zinc binding is accompanied by a large shift in the backbone conformation of the 99-loop and by large movements of both His side-chains.
17881000	11	30	theme	imidazole	2026:2034	arg1	groups					2036:2041	both imidazole groups	2021:2041	both imidazole groups	2021:2041	The P2 and His57 imidazole groups would lie next to each other in the enzyme-substrate complex, indicating that incomplete inhibition is due to competition between both imidazole groups for Zn2+.
17881000	8	31	theme	related	1329:1335	arg1	tonin					1363:1367	the related rat kallikrein proteinase tonin	1325:1367	the related rat kallikrein proteinase tonin	1325:1367	Modeling studies show that in the absence of bound leupeptin, Zn2+ is likely further coordinated by the imidazolyl side-chain of the catalytic His57 which can, similar to equivalent His57 imidazole groups in the related rat kallikrein proteinase tonin and in an engineered metal-binding rat trypsin, rotate out of its triad position to provide the third co-ordination site of the bound Zn2+, rendering Zn2+-bound hK5 inactive.
17881000	8	32	theme	kallikrein	1341:1350	arg1	tonin					1363:1367	the related rat kallikrein proteinase tonin	1325:1367	the related rat kallikrein proteinase tonin	1325:1367	Modeling studies show that in the absence of bound leupeptin, Zn2+ is likely further coordinated by the imidazolyl side-chain of the catalytic His57 which can, similar to equivalent His57 imidazole groups in the related rat kallikrein proteinase tonin and in an engineered metal-binding rat trypsin, rotate out of its triad position to provide the third co-ordination site of the bound Zn2+, rendering Zn2+-bound hK5 inactive.
17881000	4	33	theme	basic	652:656	arg1	side-chains					658:668	basic side-chains	652:668	basic side-chains	652:668	While the overall structure and the specificity of S1 pocket for basic side-chains were similar to that of hK4, a closely related family member, both differed in their interaction with Zn2+.
17881000	2	34	theme	central	306:312	arg1	role					314:317	a central role	304:317	a central role	304:317	It has trypsin-like substrate specificity, is inhibited by metal ions, and is abundantly expressed in human skin, where it is believed to play a central role in desquamation.
17881000	0	35	theme	Structural	0:9	arg1	basis					11:15	Structural basis	0:15	Structural basis of the zinc inhibition of human tissue kallikrein 5	0:67	Structural basis of the zinc inhibition of human tissue kallikrein 5.
17881000	9	36	theme	free	1611:1614	arg1	hK5					1640:1642	free and substrate saturated hK5	1611:1642	hK5	1640:1642	In solution, this mode of binding likely occurs in the presence of free and substrate saturated hK5, as kinetic analyses of Zn2+ inhibition indicate a non-competitive mechanism.
17881000	4	37	theme	family	717:722	arg1	hK4					694:696	hK4	694:696	hK4	694:696	While the overall structure and the specificity of S1 pocket for basic side-chains were similar to that of hK4, a closely related family member, both differed in their interaction with Zn2+.
17881000	4	37	theme	family	717:722	arg1	member					724:729	a closely related family member	699:729	a closely related family member	699:729	While the overall structure and the specificity of S1 pocket for basic side-chains were similar to that of hK4, a closely related family member, both differed in their interaction with Zn2+.
17881000	3	38	theme	hK5	377:379	arg1	interaction					362:372	the interaction	358:372	the interaction of hK5 with substrates and metal ions	358:410	To further understand the interaction of hK5 with substrates and metal ions, active recombinant hK5 was crystallized in complex with the tripeptidyl aldehyde inhibitor leupeptin, and structures at 2.3 A resolution were obtained with and without Zn2+.
17881000	0	39	theme	zinc	24:27	arg1	inhibition					29:38	the zinc inhibition	20:38	the zinc inhibition of human tissue kallikrein 5	20:67	Structural basis of the zinc inhibition of human tissue kallikrein 5.
17881000	3	40	with	complex	456:462	arg1	leupeptin					504:512	the tripeptidyl aldehyde inhibitor leupeptin	469:512	the tripeptidyl aldehyde inhibitor leupeptin	469:512	To further understand the interaction of hK5 with substrates and metal ions, active recombinant hK5 was crystallized in complex with the tripeptidyl aldehyde inhibitor leupeptin, and structures at 2.3 A resolution were obtained with and without Zn2+.
17881000	9	41	theme	substrate	1620:1628	arg1	hK5					1640:1642	free and substrate saturated hK5	1611:1642	hK5	1640:1642	In solution, this mode of binding likely occurs in the presence of free and substrate saturated hK5, as kinetic analyses of Zn2+ inhibition indicate a non-competitive mechanism.
17881000	8	42	theme	engineered	1379:1388	arg1	trypsin					1408:1414	an engineered metal-binding rat trypsin	1376:1414	an engineered metal-binding rat trypsin	1376:1414	Modeling studies show that in the absence of bound leupeptin, Zn2+ is likely further coordinated by the imidazolyl side-chain of the catalytic His57 which can, similar to equivalent His57 imidazole groups in the related rat kallikrein proteinase tonin and in an engineered metal-binding rat trypsin, rotate out of its triad position to provide the third co-ordination site of the bound Zn2+, rendering Zn2+-bound hK5 inactive.
17881000	0	43	theme	tissue	49:54	arg1	kallikrein					56:65	human tissue kallikrein 5	43:67	human tissue kallikrein 5	43:67	Structural basis of the zinc inhibition of human tissue kallikrein 5.
17881000	8	44	theme	imidazolyl	1221:1230	arg1	side-chain					1232:1241	the imidazolyl side-chain	1217:1241	the imidazolyl side-chain of the catalytic His57 which can, similar to equivalent His57 imidazole groups in the related rat kallikrein proteinase tonin and in an engineered metal-binding rat trypsin, rotate out of its triad position to provide the third co-ordination site of the bound Zn2+, rendering Zn2+-bound hK5 inactive	1217:1541	Modeling studies show that in the absence of bound leupeptin, Zn2+ is likely further coordinated by the imidazolyl side-chain of the catalytic His57 which can, similar to equivalent His57 imidazole groups in the related rat kallikrein proteinase tonin and in an engineered metal-binding rat trypsin, rotate out of its triad position to provide the third co-ordination site of the bound Zn2+, rendering Zn2+-bound hK5 inactive.
17881000	6	45	from	present	959:965	arg1	hK4					970:972	hK4	970:972	hK4	970:972	Instead, Zn2+ binds adjacent to the active site, becoming coordinated by the imidazole rings of His99 and His96 not present in hK4.
17881000	7	46	theme	zinc	980:983	arg1	binding					985:991	This zinc binding	975:991	This zinc binding	975:991	This zinc binding is accompanied by a large shift in the backbone conformation of the 99-loop and by large movements of both His side-chains.
17881000	7	47	theme	side-chains	1104:1114	arg1	movements					1082:1090	large movements	1076:1090	large movements of both His side-chains	1076:1114	This zinc binding is accompanied by a large shift in the backbone conformation of the 99-loop and by large movements of both His side-chains.
17881000	9	48	theme	hK5	1640:1642	arg1	presence					1599:1606	the presence	1595:1606	the presence of free and substrate saturated hK5	1595:1642	In solution, this mode of binding likely occurs in the presence of free and substrate saturated hK5, as kinetic analyses of Zn2+ inhibition indicate a non-competitive mechanism.
17881000	8	49	theme	rat	1404:1406	arg1	trypsin					1408:1414	an engineered metal-binding rat trypsin	1376:1414	an engineered metal-binding rat trypsin	1376:1414	Modeling studies show that in the absence of bound leupeptin, Zn2+ is likely further coordinated by the imidazolyl side-chain of the catalytic His57 which can, similar to equivalent His57 imidazole groups in the related rat kallikrein proteinase tonin and in an engineered metal-binding rat trypsin, rotate out of its triad position to provide the third co-ordination site of the bound Zn2+, rendering Zn2+-bound hK5 inactive.
17881000	6	50	from	hK4	970:972	arg1	present					959:965	present	959:965	present	959:965	Instead, Zn2+ binds adjacent to the active site, becoming coordinated by the imidazole rings of His99 and His96 not present in hK4.
17881000	3	51	theme	metal	401:405	arg1	ions					407:410	metal ions	401:410	metal ions	401:410	To further understand the interaction of hK5 with substrates and metal ions, active recombinant hK5 was crystallized in complex with the tripeptidyl aldehyde inhibitor leupeptin, and structures at 2.3 A resolution were obtained with and without Zn2+.
17881000	6	52	theme	present	959:965	arg1	rings					930:934	the imidazole rings	916:934	the imidazole rings of His99 and His96 not present in hK4	916:972	Instead, Zn2+ binds adjacent to the active site, becoming coordinated by the imidazole rings of His99 and His96 not present in hK4.
17881000	8	53	theme	catalytic	1250:1258	arg1	His57					1260:1264	the catalytic His57	1246:1264	the catalytic His57 which can, similar to equivalent His57 imidazole groups in the related rat kallikrein proteinase tonin and in an engineered metal-binding rat trypsin, rotate out of its triad position to provide the third co-ordination site of the bound Zn2+, rendering Zn2+-bound hK5 inactive	1246:1541	Modeling studies show that in the absence of bound leupeptin, Zn2+ is likely further coordinated by the imidazolyl side-chain of the catalytic His57 which can, similar to equivalent His57 imidazole groups in the related rat kallikrein proteinase tonin and in an engineered metal-binding rat trypsin, rotate out of its triad position to provide the third co-ordination site of the bound Zn2+, rendering Zn2+-bound hK5 inactive.
17881000	8	54	theme	third	1465:1469	arg1	Zn2+					1503:1506	the bound Zn2+	1493:1506	the bound Zn2+	1493:1506	Modeling studies show that in the absence of bound leupeptin, Zn2+ is likely further coordinated by the imidazolyl side-chain of the catalytic His57 which can, similar to equivalent His57 imidazole groups in the related rat kallikrein proteinase tonin and in an engineered metal-binding rat trypsin, rotate out of its triad position to provide the third co-ordination site of the bound Zn2+, rendering Zn2+-bound hK5 inactive.
17881000	8	54	theme	third	1465:1469	arg1	site					1485:1488	the third co-ordination site	1461:1488	the third co-ordination site of the bound Zn2+	1461:1506	Modeling studies show that in the absence of bound leupeptin, Zn2+ is likely further coordinated by the imidazolyl side-chain of the catalytic His57 which can, similar to equivalent His57 imidazole groups in the related rat kallikrein proteinase tonin and in an engineered metal-binding rat trypsin, rotate out of its triad position to provide the third co-ordination site of the bound Zn2+, rendering Zn2+-bound hK5 inactive.
17881000	11	55	theme	incomplete	1969:1978	arg1	inhibition					1980:1989	incomplete inhibition	1969:1989	incomplete inhibition	1969:1989	The P2 and His57 imidazole groups would lie next to each other in the enzyme-substrate complex, indicating that incomplete inhibition is due to competition between both imidazole groups for Zn2+.
17881000	6	56	theme	His96	949:953	arg1	rings					930:934	the imidazole rings	916:934	the imidazole rings of His99 and His96 not present in hK4	916:972	Instead, Zn2+ binds adjacent to the active site, becoming coordinated by the imidazole rings of His99 and His96 not present in hK4.
17881000	3	57	theme	recombinant	420:430	arg1	hK5					432:434	active recombinant hK5	413:434	active recombinant hK5	413:434	To further understand the interaction of hK5 with substrates and metal ions, active recombinant hK5 was crystallized in complex with the tripeptidyl aldehyde inhibitor leupeptin, and structures at 2.3 A resolution were obtained with and without Zn2+.
17881000	6	58	theme	His99	939:943	arg1	rings					930:934	the imidazole rings	916:934	the imidazole rings of His99 and His96 not present in hK4	916:972	Instead, Zn2+ binds adjacent to the active site, becoming coordinated by the imidazole rings of His99 and His96 not present in hK4.
17881000	9	59	theme	Zn2+	1668:1671	arg1	inhibition					1673:1682	Zn2+ inhibition	1668:1682	Zn2+ inhibition	1668:1682	In solution, this mode of binding likely occurs in the presence of free and substrate saturated hK5, as kinetic analyses of Zn2+ inhibition indicate a non-competitive mechanism.
17881000	12	60	theme	catalysis	2151:2159	arg1	inhibition					2133:2142	the Zn2+-mediated inhibition	2115:2142	the Zn2+-mediated inhibition of hK5 catalysis	2115:2159	The His96-99-57 triad is thus suggested to be responsible for the Zn2+-mediated inhibition of hK5 catalysis.
17881000	3	61	theme	inhibitor	494:502	arg1	leupeptin					504:512	the tripeptidyl aldehyde inhibitor leupeptin	469:512	the tripeptidyl aldehyde inhibitor leupeptin	469:512	To further understand the interaction of hK5 with substrates and metal ions, active recombinant hK5 was crystallized in complex with the tripeptidyl aldehyde inhibitor leupeptin, and structures at 2.3 A resolution were obtained with and without Zn2+.
17881000	8	62	theme	Zn2+	1503:1506	arg1	Zn2+					1503:1506	the bound Zn2+	1493:1506	the bound Zn2+	1493:1506	Modeling studies show that in the absence of bound leupeptin, Zn2+ is likely further coordinated by the imidazolyl side-chain of the catalytic His57 which can, similar to equivalent His57 imidazole groups in the related rat kallikrein proteinase tonin and in an engineered metal-binding rat trypsin, rotate out of its triad position to provide the third co-ordination site of the bound Zn2+, rendering Zn2+-bound hK5 inactive.
17881000	8	62	theme	Zn2+	1503:1506	arg1	site					1485:1488	the third co-ordination site	1461:1488	the third co-ordination site of the bound Zn2+	1461:1506	Modeling studies show that in the absence of bound leupeptin, Zn2+ is likely further coordinated by the imidazolyl side-chain of the catalytic His57 which can, similar to equivalent His57 imidazole groups in the related rat kallikrein proteinase tonin and in an engineered metal-binding rat trypsin, rotate out of its triad position to provide the third co-ordination site of the bound Zn2+, rendering Zn2+-bound hK5 inactive.
17881000	1	63	theme	kallikrein	121:130	arg1	family					132:137	the tissue kallikrein family	110:137	the tissue kallikrein family of serine peptidases	110:158	Human kallikrein 5 (hK5) is a member of the tissue kallikrein family of serine peptidases.
17881000	11	64	theme	enzyme-substrate	1927:1942	arg1	complex					1944:1950	the enzyme-substrate complex	1923:1950	the enzyme-substrate complex	1923:1950	The P2 and His57 imidazole groups would lie next to each other in the enzyme-substrate complex, indicating that incomplete inhibition is due to competition between both imidazole groups for Zn2+.
17881000	9	65	theme	non-competitive	1695:1709	arg1	mechanism					1711:1719	a non-competitive mechanism	1693:1719	a non-competitive mechanism	1693:1719	In solution, this mode of binding likely occurs in the presence of free and substrate saturated hK5, as kinetic analyses of Zn2+ inhibition indicate a non-competitive mechanism.
17881000	2	66	theme	human	263:267	arg1	skin					269:272	human skin	263:272	human skin	263:272	It has trypsin-like substrate specificity, is inhibited by metal ions, and is abundantly expressed in human skin, where it is believed to play a central role in desquamation.
17881000	3	67	theme	tripeptidyl	473:483	arg1	leupeptin					504:512	the tripeptidyl aldehyde inhibitor leupeptin	469:512	the tripeptidyl aldehyde inhibitor leupeptin	469:512	To further understand the interaction of hK5 with substrates and metal ions, active recombinant hK5 was crystallized in complex with the tripeptidyl aldehyde inhibitor leupeptin, and structures at 2.3 A resolution were obtained with and without Zn2+.
17881000	1	68	theme	peptidases	149:158	arg1	family					132:137	the tissue kallikrein family	110:137	the tissue kallikrein family of serine peptidases	110:158	Human kallikrein 5 (hK5) is a member of the tissue kallikrein family of serine peptidases.
17881000	7	69	from	shift	1019:1023	arg1	conformation					1041:1052	the backbone conformation	1028:1052	the backbone conformation of the 99-loop	1028:1067	This zinc binding is accompanied by a large shift in the backbone conformation of the 99-loop and by large movements of both His side-chains.
17881000	12	70	theme	hK5	2147:2149	arg1	catalysis					2151:2159	hK5 catalysis	2147:2159	hK5 catalysis	2147:2159	The His96-99-57 triad is thus suggested to be responsible for the Zn2+-mediated inhibition of hK5 catalysis.
17881000	2	71	theme	substrate	181:189	arg1	specificity					191:201	trypsin-like substrate specificity	168:201	trypsin-like substrate specificity	168:201	It has trypsin-like substrate specificity, is inhibited by metal ions, and is abundantly expressed in human skin, where it is believed to play a central role in desquamation.
17881000	3	72	with	interaction	362:372	arg1	substrates					386:395	substrates	386:395	substrates	386:395	To further understand the interaction of hK5 with substrates and metal ions, active recombinant hK5 was crystallized in complex with the tripeptidyl aldehyde inhibitor leupeptin, and structures at 2.3 A resolution were obtained with and without Zn2+.
17881000	3	72	with	interaction	362:372	arg1	ions					407:410	metal ions	401:410	metal ions	401:410	To further understand the interaction of hK5 with substrates and metal ions, active recombinant hK5 was crystallized in complex with the tripeptidyl aldehyde inhibitor leupeptin, and structures at 2.3 A resolution were obtained with and without Zn2+.
17881000	2	73	theme	metal	220:224	arg1	ions					226:229	metal ions	220:229	metal ions	220:229	It has trypsin-like substrate specificity, is inhibited by metal ions, and is abundantly expressed in human skin, where it is believed to play a central role in desquamation.
17881000	5	74	theme	hK5	805:807	arg1	75-loop					794:800	the 75-loop	790:800	the 75-loop of hK5	790:807	Unlike hK4, the 75-loop of hK5 is not structured to bind a Zn2+.
17881000	11	75	theme	imidazole	1874:1882	arg1	groups					1884:1889	The P2 and His57 imidazole groups	1857:1889	The P2 and His57 imidazole groups	1857:1889	The P2 and His57 imidazole groups would lie next to each other in the enzyme-substrate complex, indicating that incomplete inhibition is due to competition between both imidazole groups for Zn2+.
17881000	8	76	theme	His57	1299:1303	arg1	groups					1315:1320	equivalent His57 imidazole groups	1288:1320	equivalent His57 imidazole groups in the related rat kallikrein proteinase tonin and in an engineered metal-binding rat trypsin	1288:1414	Modeling studies show that in the absence of bound leupeptin, Zn2+ is likely further coordinated by the imidazolyl side-chain of the catalytic His57 which can, similar to equivalent His57 imidazole groups in the related rat kallikrein proteinase tonin and in an engineered metal-binding rat trypsin, rotate out of its triad position to provide the third co-ordination site of the bound Zn2+, rendering Zn2+-bound hK5 inactive.
17881000	4	77	theme	S1	638:639	arg1	pocket					641:646	S1 pocket	638:646	S1 pocket	638:646	While the overall structure and the specificity of S1 pocket for basic side-chains were similar to that of hK4, a closely related family member, both differed in their interaction with Zn2+.
17881000	10	78	theme	tripeptidyl	1805:1815	arg1	substrates					1817:1826	tripeptidyl substrates	1805:1826	tripeptidyl substrates containing a P2-His residue	1805:1854	Supporting the His57 re-orientation, Zn2+ does not fully inhibit hK5 hydrolysis of tripeptidyl substrates containing a P2-His residue.
17881000	0	79	theme	kallikrein	56:65	arg1	inhibition					29:38	the zinc inhibition	20:38	the zinc inhibition of human tissue kallikrein 5	20:67	Structural basis of the zinc inhibition of human tissue kallikrein 5.
17881000	4	80	with	interaction	755:765	arg1	Zn2+					772:775	Zn2+	772:775	Zn2+	772:775	While the overall structure and the specificity of S1 pocket for basic side-chains were similar to that of hK4, a closely related family member, both differed in their interaction with Zn2+.
17881000	4	81	theme	overall	597:603	arg1	structure					605:613	the overall structure	593:613	the overall structure	593:613	While the overall structure and the specificity of S1 pocket for basic side-chains were similar to that of hK4, a closely related family member, both differed in their interaction with Zn2+.
17881000	4	81	theme	overall	597:603	arg1	similar					675:681	similar	675:681	similar	675:681	While the overall structure and the specificity of S1 pocket for basic side-chains were similar to that of hK4, a closely related family member, both differed in their interaction with Zn2+.
17881000	8	82	dep	position	1441:1448	arg1	out					1424:1426	out	1424:1426	out	1424:1426	Modeling studies show that in the absence of bound leupeptin, Zn2+ is likely further coordinated by the imidazolyl side-chain of the catalytic His57 which can, similar to equivalent His57 imidazole groups in the related rat kallikrein proteinase tonin and in an engineered metal-binding rat trypsin, rotate out of its triad position to provide the third co-ordination site of the bound Zn2+, rendering Zn2+-bound hK5 inactive.
17881000	10	83	theme	P2-His	1841:1846	arg1	residue					1848:1854	a P2-His residue	1839:1854	a P2-His residue	1839:1854	Supporting the His57 re-orientation, Zn2+ does not fully inhibit hK5 hydrolysis of tripeptidyl substrates containing a P2-His residue.
17881000	9	84	theme	binding	1570:1576	arg1	mode					1562:1565	this mode	1557:1565	this mode of binding	1557:1576	In solution, this mode of binding likely occurs in the presence of free and substrate saturated hK5, as kinetic analyses of Zn2+ inhibition indicate a non-competitive mechanism.
17881000	8	85	theme	rat	1337:1339	arg1	tonin					1363:1367	the related rat kallikrein proteinase tonin	1325:1367	the related rat kallikrein proteinase tonin	1325:1367	Modeling studies show that in the absence of bound leupeptin, Zn2+ is likely further coordinated by the imidazolyl side-chain of the catalytic His57 which can, similar to equivalent His57 imidazole groups in the related rat kallikrein proteinase tonin and in an engineered metal-binding rat trypsin, rotate out of its triad position to provide the third co-ordination site of the bound Zn2+, rendering Zn2+-bound hK5 inactive.
17881000	8	86	theme	proteinase	1352:1361	arg1	tonin					1363:1367	the related rat kallikrein proteinase tonin	1325:1367	the related rat kallikrein proteinase tonin	1325:1367	Modeling studies show that in the absence of bound leupeptin, Zn2+ is likely further coordinated by the imidazolyl side-chain of the catalytic His57 which can, similar to equivalent His57 imidazole groups in the related rat kallikrein proteinase tonin and in an engineered metal-binding rat trypsin, rotate out of its triad position to provide the third co-ordination site of the bound Zn2+, rendering Zn2+-bound hK5 inactive.
17881000	10	87	contain	containing	1828:1837	arg2	residue					1848:1854	a P2-His residue	1839:1854	a P2-His residue	1839:1854	Supporting the His57 re-orientation, Zn2+ does not fully inhibit hK5 hydrolysis of tripeptidyl substrates containing a P2-His residue.
17881000	10	87	contain	containing	1828:1837	arg1	substrates					1817:1826	tripeptidyl substrates	1805:1826	tripeptidyl substrates containing a P2-His residue	1805:1854	Supporting the His57 re-orientation, Zn2+ does not fully inhibit hK5 hydrolysis of tripeptidyl substrates containing a P2-His residue.
17881000	8	88	theme	leupeptin	1168:1176	arg1	absence					1151:1157	the absence	1147:1157	the absence of bound leupeptin	1147:1176	Modeling studies show that in the absence of bound leupeptin, Zn2+ is likely further coordinated by the imidazolyl side-chain of the catalytic His57 which can, similar to equivalent His57 imidazole groups in the related rat kallikrein proteinase tonin and in an engineered metal-binding rat trypsin, rotate out of its triad position to provide the third co-ordination site of the bound Zn2+, rendering Zn2+-bound hK5 inactive.
17881000	3	89	from	resolution	539:548	arg1	structures					519:528	structures	519:528	structures at 2.3 A resolution	519:548	To further understand the interaction of hK5 with substrates and metal ions, active recombinant hK5 was crystallized in complex with the tripeptidyl aldehyde inhibitor leupeptin, and structures at 2.3 A resolution were obtained with and without Zn2+.
17881000	1	90	theme	Human	70:74	arg1	kallikrein					76:85	Human kallikrein 5	70:87	Human kallikrein 5 (hK5)	70:93	Human kallikrein 5 (hK5) is a member of the tissue kallikrein family of serine peptidases.
17881000	1	90	theme	Human	70:74	arg1	hK5					90:92	hK5	90:92	hK5	90:92	Human kallikrein 5 (hK5) is a member of the tissue kallikrein family of serine peptidases.
17881000	1	90	theme	Human	70:74	arg1	member					100:105	a member	98:105	a member of the tissue kallikrein family of serine peptidases	98:158	Human kallikrein 5 (hK5) is a member of the tissue kallikrein family of serine peptidases.
17881000	6	91	theme	imidazole	920:928	arg1	rings					930:934	the imidazole rings	916:934	the imidazole rings of His99 and His96 not present in hK4	916:972	Instead, Zn2+ binds adjacent to the active site, becoming coordinated by the imidazole rings of His99 and His96 not present in hK4.
17881000	12	92	theme	Zn2+-mediated	2119:2131	arg1	inhibition					2133:2142	the Zn2+-mediated inhibition	2115:2142	the Zn2+-mediated inhibition of hK5 catalysis	2115:2159	The His96-99-57 triad is thus suggested to be responsible for the Zn2+-mediated inhibition of hK5 catalysis.
17881000	8	93	from	groups	1315:1320	arg1	tonin					1363:1367	the related rat kallikrein proteinase tonin	1325:1367	the related rat kallikrein proteinase tonin	1325:1367	Modeling studies show that in the absence of bound leupeptin, Zn2+ is likely further coordinated by the imidazolyl side-chain of the catalytic His57 which can, similar to equivalent His57 imidazole groups in the related rat kallikrein proteinase tonin and in an engineered metal-binding rat trypsin, rotate out of its triad position to provide the third co-ordination site of the bound Zn2+, rendering Zn2+-bound hK5 inactive.
17881000	8	93	from	groups	1315:1320	arg1	trypsin					1408:1414	an engineered metal-binding rat trypsin	1376:1414	an engineered metal-binding rat trypsin	1376:1414	Modeling studies show that in the absence of bound leupeptin, Zn2+ is likely further coordinated by the imidazolyl side-chain of the catalytic His57 which can, similar to equivalent His57 imidazole groups in the related rat kallikrein proteinase tonin and in an engineered metal-binding rat trypsin, rotate out of its triad position to provide the third co-ordination site of the bound Zn2+, rendering Zn2+-bound hK5 inactive.
17881000	0	94	theme	inhibition	29:38	arg1	basis					11:15	Structural basis	0:15	Structural basis of the zinc inhibition of human tissue kallikrein 5	0:67	Structural basis of the zinc inhibition of human tissue kallikrein 5.
17881000	8	95	theme	metal-binding	1390:1402	arg1	trypsin					1408:1414	an engineered metal-binding rat trypsin	1376:1414	an engineered metal-binding rat trypsin	1376:1414	Modeling studies show that in the absence of bound leupeptin, Zn2+ is likely further coordinated by the imidazolyl side-chain of the catalytic His57 which can, similar to equivalent His57 imidazole groups in the related rat kallikrein proteinase tonin and in an engineered metal-binding rat trypsin, rotate out of its triad position to provide the third co-ordination site of the bound Zn2+, rendering Zn2+-bound hK5 inactive.
17881000	4	96	theme	related	709:715	arg1	hK4					694:696	hK4	694:696	hK4	694:696	While the overall structure and the specificity of S1 pocket for basic side-chains were similar to that of hK4, a closely related family member, both differed in their interaction with Zn2+.
17881000	4	96	theme	related	709:715	arg1	member					724:729	a closely related family member	699:729	a closely related family member	699:729	While the overall structure and the specificity of S1 pocket for basic side-chains were similar to that of hK4, a closely related family member, both differed in their interaction with Zn2+.
17881000	0	97	theme	human	43:47	arg1	kallikrein					56:65	human tissue kallikrein 5	43:67	human tissue kallikrein 5	43:67	Structural basis of the zinc inhibition of human tissue kallikrein 5.
17881000	7	98	theme	His	1100:1102	arg1	side-chains					1104:1114	both His side-chains	1095:1114	both His side-chains	1095:1114	This zinc binding is accompanied by a large shift in the backbone conformation of the 99-loop and by large movements of both His side-chains.
17881000	9	99	theme	saturated	1630:1638	arg1	hK5					1640:1642	free and substrate saturated hK5	1611:1642	hK5	1640:1642	In solution, this mode of binding likely occurs in the presence of free and substrate saturated hK5, as kinetic analyses of Zn2+ inhibition indicate a non-competitive mechanism.
17881000	3	100	theme	active	413:418	arg1	hK5					432:434	active recombinant hK5	413:434	active recombinant hK5	413:434	To further understand the interaction of hK5 with substrates and metal ions, active recombinant hK5 was crystallized in complex with the tripeptidyl aldehyde inhibitor leupeptin, and structures at 2.3 A resolution were obtained with and without Zn2+.
17881000	6	101	attach	present	959:965	arg2	rings					930:934	the imidazole rings	916:934	the imidazole rings of His99 and His96 not present in hK4	916:972	Instead, Zn2+ binds adjacent to the active site, becoming coordinated by the imidazole rings of His99 and His96 not present in hK4.
17881000	6	101	attach	present	959:965	arg1	hK4					970:972	hK4	970:972	hK4	970:972	Instead, Zn2+ binds adjacent to the active site, becoming coordinated by the imidazole rings of His99 and His96 not present in hK4.
17881000	8	102	theme	co-ordination	1471:1483	arg1	Zn2+					1503:1506	the bound Zn2+	1493:1506	the bound Zn2+	1493:1506	Modeling studies show that in the absence of bound leupeptin, Zn2+ is likely further coordinated by the imidazolyl side-chain of the catalytic His57 which can, similar to equivalent His57 imidazole groups in the related rat kallikrein proteinase tonin and in an engineered metal-binding rat trypsin, rotate out of its triad position to provide the third co-ordination site of the bound Zn2+, rendering Zn2+-bound hK5 inactive.
17881000	8	102	theme	co-ordination	1471:1483	arg1	site					1485:1488	the third co-ordination site	1461:1488	the third co-ordination site of the bound Zn2+	1461:1506	Modeling studies show that in the absence of bound leupeptin, Zn2+ is likely further coordinated by the imidazolyl side-chain of the catalytic His57 which can, similar to equivalent His57 imidazole groups in the related rat kallikrein proteinase tonin and in an engineered metal-binding rat trypsin, rotate out of its triad position to provide the third co-ordination site of the bound Zn2+, rendering Zn2+-bound hK5 inactive.
17881000	7	103	theme	large	1076:1080	arg1	movements					1082:1090	large movements	1076:1090	large movements of both His side-chains	1076:1114	This zinc binding is accompanied by a large shift in the backbone conformation of the 99-loop and by large movements of both His side-chains.
17881000	9	104	theme	kinetic	1648:1654	arg1	analyses					1656:1663	kinetic analyses	1648:1663	kinetic analyses of Zn2+ inhibition	1648:1682	In solution, this mode of binding likely occurs in the presence of free and substrate saturated hK5, as kinetic analyses of Zn2+ inhibition indicate a non-competitive mechanism.
15983417	4	0	from	regions	518:524	arg1	monomers					506:513	the six IL-22(Dm) monomers	488:513	the six IL-22(Dm) monomers at regions corresponding to the IL-22R1 and IL-10R2 binding sites	488:579	However, 1-4 A main-chain differences are observed between the six IL-22(Dm) monomers at regions corresponding to the IL-22R1 and IL-10R2 binding sites.
15983417	4	1	theme	main-chain	444:453	arg1	differences					455:465	1-4 A main-chain differences	438:465	1-4 A main-chain differences	438:465	However, 1-4 A main-chain differences are observed between the six IL-22(Dm) monomers at regions corresponding to the IL-22R1 and IL-10R2 binding sites.
15983417	4	2	theme	Dm	502:503	arg1	monomers					506:513	the six IL-22(Dm) monomers	488:513	the six IL-22(Dm) monomers at regions corresponding to the IL-22R1 and IL-10R2 binding sites	488:579	However, 1-4 A main-chain differences are observed between the six IL-22(Dm) monomers at regions corresponding to the IL-22R1 and IL-10R2 binding sites.
15983417	5	3	theme	IL22	652:655	arg1	variation					639:647	the conformational variation	620:647	the conformational variation of IL22(Dm)	620:659	The structure of the carbohydrate and the conformational variation of IL22(Dm) provide new insights into IL-22 receptor recognition.
15983417	5	3	theme	IL22	652:655	arg1	structure					586:594	The structure	582:594	The structure of the carbohydrate	582:614	The structure of the carbohydrate and the conformational variation of IL22(Dm) provide new insights into IL-22 receptor recognition.
15983417	4	4	theme	A	442:442	arg1	differences					455:465	1-4 A main-chain differences	438:465	1-4 A main-chain differences	438:465	However, 1-4 A main-chain differences are observed between the six IL-22(Dm) monomers at regions corresponding to the IL-22R1 and IL-10R2 binding sites.
15983417	0	5	link	insect-cell-derived	13:31	arg1	IL-22					33:37	insect-cell-derived IL-22	13:37	insect-cell-derived IL-22	13:37	Structure of insect-cell-derived IL-22.
15983417	3	6	dep	IL-22	258:262	arg1	interleukin-22					283:296	interleukin-22	283:296	interleukin-22	283:296	Comparison of IL-22(Dm) and IL-22(Ec) (interleukin-22 produced in Escherichia coli) structures reveals that N-linked glycosylation causes only minor structural changes to the cytokine.
15983417	1	7	theme	interleukin-22	65:78	arg1	structure					52:60	The crystal structure	40:60	The crystal structure of interleukin-22 expressed in Drosophila melanogaster S2 cells (IL-22(Dm))	40:136	The crystal structure of interleukin-22 expressed in Drosophila melanogaster S2 cells (IL-22(Dm)) has been determined at 2.6 A resolution.
15983417	3	8	link	N-linked	352:359	arg1	glycosylation					361:373	N-linked glycosylation	352:373	N-linked glycosylation	352:373	Comparison of IL-22(Dm) and IL-22(Ec) (interleukin-22 produced in Escherichia coli) structures reveals that N-linked glycosylation causes only minor structural changes to the cytokine.
15983417	2	9	theme	asymmetric	227:236	arg1	unit					238:241	the asymmetric unit	223:241	the asymmetric unit	223:241	IL-22(Dm) crystals contain six molecules in the asymmetric unit.
15983417	3	10	theme	N-linked	352:359	arg1	glycosylation					361:373	N-linked glycosylation	352:373	N-linked glycosylation	352:373	Comparison of IL-22(Dm) and IL-22(Ec) (interleukin-22 produced in Escherichia coli) structures reveals that N-linked glycosylation causes only minor structural changes to the cytokine.
15983417	1	11	theme	melanogaster	104:115	arg1	IL-22					127:131	IL-22	127:131	IL-22(Dm)	127:135	The crystal structure of interleukin-22 expressed in Drosophila melanogaster S2 cells (IL-22(Dm)) has been determined at 2.6 A resolution.
15983417	1	11	theme	melanogaster	104:115	arg1	cells					120:124	Drosophila melanogaster S2 cells	93:124	Drosophila melanogaster S2 cells (IL-22(Dm))	93:136	The crystal structure of interleukin-22 expressed in Drosophila melanogaster S2 cells (IL-22(Dm)) has been determined at 2.6 A resolution.
15983417	2	12	from	molecules	210:218	arg1	unit					238:241	the asymmetric unit	223:241	the asymmetric unit	223:241	IL-22(Dm) crystals contain six molecules in the asymmetric unit.
15983417	0	13	theme	IL-22	33:37	arg1	Structure					0:8	Structure	0:8	Structure of insect-cell-derived IL-22.	0:38	Structure of insect-cell-derived IL-22.
15983417	1	14	theme	S2	117:118	arg1	IL-22					127:131	IL-22	127:131	IL-22(Dm)	127:135	The crystal structure of interleukin-22 expressed in Drosophila melanogaster S2 cells (IL-22(Dm)) has been determined at 2.6 A resolution.
15983417	1	14	theme	S2	117:118	arg1	cells					120:124	Drosophila melanogaster S2 cells	93:124	Drosophila melanogaster S2 cells (IL-22(Dm))	93:136	The crystal structure of interleukin-22 expressed in Drosophila melanogaster S2 cells (IL-22(Dm)) has been determined at 2.6 A resolution.
15983417	0	15	theme	insect-cell-derived	13:31	arg1	IL-22					33:37	insect-cell-derived IL-22	13:37	insect-cell-derived IL-22	13:37	Structure of insect-cell-derived IL-22.
15983417	5	16	theme	conformational	624:637	arg1	variation					639:647	the conformational variation	620:647	the conformational variation of IL22(Dm)	620:659	The structure of the carbohydrate and the conformational variation of IL22(Dm) provide new insights into IL-22 receptor recognition.
15983417	4	17	theme	IL-22R1	547:553	arg1	sites					575:579	the IL-22R1 and IL-10R2 binding sites	543:579	the IL-22R1 and IL-10R2 binding sites	543:579	However, 1-4 A main-chain differences are observed between the six IL-22(Dm) monomers at regions corresponding to the IL-22R1 and IL-10R2 binding sites.
15983417	5	18	theme	IL-22	687:691	arg1	recognition					702:712	IL-22 receptor recognition	687:712	IL-22 receptor recognition	687:712	The structure of the carbohydrate and the conformational variation of IL22(Dm) provide new insights into IL-22 receptor recognition.
15983417	4	19	theme	IL-22	496:500	arg1	monomers					506:513	the six IL-22(Dm) monomers	488:513	the six IL-22(Dm) monomers at regions corresponding to the IL-22R1 and IL-10R2 binding sites	488:579	However, 1-4 A main-chain differences are observed between the six IL-22(Dm) monomers at regions corresponding to the IL-22R1 and IL-10R2 binding sites.
15983417	4	20	theme	binding	567:573	arg1	sites					575:579	the IL-22R1 and IL-10R2 binding sites	543:579	the IL-22R1 and IL-10R2 binding sites	543:579	However, 1-4 A main-chain differences are observed between the six IL-22(Dm) monomers at regions corresponding to the IL-22R1 and IL-10R2 binding sites.
15983417	3	21	theme	minor	387:391	arg1	changes					404:410	only minor structural changes	382:410	only minor structural changes	382:410	Comparison of IL-22(Dm) and IL-22(Ec) (interleukin-22 produced in Escherichia coli) structures reveals that N-linked glycosylation causes only minor structural changes to the cytokine.
15983417	5	22	theme	receptor	693:700	arg1	recognition					702:712	IL-22 receptor recognition	687:712	IL-22 receptor recognition	687:712	The structure of the carbohydrate and the conformational variation of IL22(Dm) provide new insights into IL-22 receptor recognition.
15983417	3	23	theme	structural	393:402	arg1	changes					404:410	only minor structural changes	382:410	only minor structural changes	382:410	Comparison of IL-22(Dm) and IL-22(Ec) (interleukin-22 produced in Escherichia coli) structures reveals that N-linked glycosylation causes only minor structural changes to the cytokine.
15983417	3	24	theme	structures	328:337	arg1	Comparison					244:253	Comparison	244:253	Comparison of IL-22(Dm) and IL-22(Ec) (interleukin-22 produced in Escherichia coli) structures	244:337	Comparison of IL-22(Dm) and IL-22(Ec) (interleukin-22 produced in Escherichia coli) structures reveals that N-linked glycosylation causes only minor structural changes to the cytokine.
15983417	5	25	theme	carbohydrate	603:614	arg1	variation					639:647	the conformational variation	620:647	the conformational variation of IL22(Dm)	620:659	The structure of the carbohydrate and the conformational variation of IL22(Dm) provide new insights into IL-22 receptor recognition.
15983417	5	25	theme	carbohydrate	603:614	arg1	structure					586:594	The structure	582:594	The structure of the carbohydrate	582:614	The structure of the carbohydrate and the conformational variation of IL22(Dm) provide new insights into IL-22 receptor recognition.
15983417	2	26	theme	IL-22	179:183	arg1	crystals					189:196	IL-22(Dm) crystals	179:196	IL-22(Dm) crystals	179:196	IL-22(Dm) crystals contain six molecules in the asymmetric unit.
15983417	3	27	theme	IL-22	258:262	arg1	structures					328:337	IL-22(Dm) and IL-22(Ec) (interleukin-22 produced in Escherichia coli) structures	258:337	IL-22(Dm) and IL-22(Ec) (interleukin-22 produced in Escherichia coli) structures	258:337	Comparison of IL-22(Dm) and IL-22(Ec) (interleukin-22 produced in Escherichia coli) structures reveals that N-linked glycosylation causes only minor structural changes to the cytokine.
15983417	3	28	theme	IL-22	272:276	arg1	structures					328:337	IL-22(Dm) and IL-22(Ec) (interleukin-22 produced in Escherichia coli) structures	258:337	IL-22(Dm) and IL-22(Ec) (interleukin-22 produced in Escherichia coli) structures	258:337	Comparison of IL-22(Dm) and IL-22(Ec) (interleukin-22 produced in Escherichia coli) structures reveals that N-linked glycosylation causes only minor structural changes to the cytokine.
15983417	4	29	theme	IL-10R2	559:565	arg1	sites					575:579	the IL-22R1 and IL-10R2 binding sites	543:579	the IL-22R1 and IL-10R2 binding sites	543:579	However, 1-4 A main-chain differences are observed between the six IL-22(Dm) monomers at regions corresponding to the IL-22R1 and IL-10R2 binding sites.
15983417	1	30	theme	crystal	44:50	arg1	structure					52:60	The crystal structure	40:60	The crystal structure of interleukin-22 expressed in Drosophila melanogaster S2 cells (IL-22(Dm))	40:136	The crystal structure of interleukin-22 expressed in Drosophila melanogaster S2 cells (IL-22(Dm)) has been determined at 2.6 A resolution.
15983417	5	31	theme	new	669:671	arg1	insights					673:680	new insights	669:680	new insights into IL-22 receptor recognition	669:712	The structure of the carbohydrate and the conformational variation of IL22(Dm) provide new insights into IL-22 receptor recognition.
15983417	2	32	contain	contain	198:204	arg1	crystals					189:196	IL-22(Dm) crystals	179:196	IL-22(Dm) crystals	179:196	IL-22(Dm) crystals contain six molecules in the asymmetric unit.
15983417	2	32	contain	contain	198:204	arg2	molecules					210:218	six molecules	206:218	six molecules in the asymmetric unit	206:241	IL-22(Dm) crystals contain six molecules in the asymmetric unit.
2983222	2	0	theme	cleavage	349:356	arg1	site					358:361	a precursor processing enzyme cleavage site	319:361	a precursor processing enzyme cleavage site	319:361	The precursor starts with a 27-amino-acid signal sequence, followed by the receptor alpha-subunit, a precursor processing enzyme cleavage site, then the beta-subunit containing a single 23-amino-acid transmembrane sequence.
2983222	2	0	theme	cleavage	349:356	arg1	alpha-subunit					304:316	the receptor alpha-subunit	291:316	the receptor alpha-subunit	291:316	The precursor starts with a 27-amino-acid signal sequence, followed by the receptor alpha-subunit, a precursor processing enzyme cleavage site, then the beta-subunit containing a single 23-amino-acid transmembrane sequence.
2983222	2	1	theme	enzyme	342:347	arg1	site					358:361	a precursor processing enzyme cleavage site	319:361	a precursor processing enzyme cleavage site	319:361	The precursor starts with a 27-amino-acid signal sequence, followed by the receptor alpha-subunit, a precursor processing enzyme cleavage site, then the beta-subunit containing a single 23-amino-acid transmembrane sequence.
2983222	2	1	theme	enzyme	342:347	arg1	alpha-subunit					304:316	the receptor alpha-subunit	291:316	the receptor alpha-subunit	291:316	The precursor starts with a 27-amino-acid signal sequence, followed by the receptor alpha-subunit, a precursor processing enzyme cleavage site, then the beta-subunit containing a single 23-amino-acid transmembrane sequence.
2983222	3	2	theme	family	543:548	arg1	homologies					463:472	sequence homologies	454:472	sequence homologies to human epidermal growth factor receptor	454:514	There are sequence homologies to human epidermal growth factor receptor and the members of the src family of oncogene products.
2983222	3	2	theme	family	543:548	arg1	members					524:530	the members	520:530	the members of the src family of oncogene products	520:569	There are sequence homologies to human epidermal growth factor receptor and the members of the src family of oncogene products.
2983222	3	3	theme	products	562:569	arg1	family					543:548	the src family	535:548	the src family of oncogene products	535:569	There are sequence homologies to human epidermal growth factor receptor and the members of the src family of oncogene products.
2983222	0	4	theme	oncogenes	77:85	arg1	family					67:72	the tyrosine kinase family	47:72	the tyrosine kinase family of oncogenes	47:85	Human insulin receptor and its relationship to the tyrosine kinase family of oncogenes.
2983222	3	5	theme	growth	493:498	arg1	receptor					507:514	human epidermal growth factor receptor	477:514	human epidermal growth factor receptor	477:514	There are sequence homologies to human epidermal growth factor receptor and the members of the src family of oncogene products.
2983222	3	6	theme	factor	500:505	arg1	receptor					507:514	human epidermal growth factor receptor	477:514	human epidermal growth factor receptor	477:514	There are sequence homologies to human epidermal growth factor receptor and the members of the src family of oncogene products.
2983222	2	7	theme	23-amino-acid	406:418	arg1	sequence					434:441	a single 23-amino-acid transmembrane sequence	397:441	a single 23-amino-acid transmembrane sequence	397:441	The precursor starts with a 27-amino-acid signal sequence, followed by the receptor alpha-subunit, a precursor processing enzyme cleavage site, then the beta-subunit containing a single 23-amino-acid transmembrane sequence.
2983222	1	8	theme	insulin	154:160	arg1	precursor					171:179	the human insulin receptor precursor	144:179	the human insulin receptor precursor	144:179	We have deduced the entire 1,370-amino-acid sequence of the human insulin receptor precursor from a single complementary DNA clone.
2983222	2	9	theme	signal	262:267	arg1	sequence					269:276	a 27-amino-acid signal sequence	246:276	a 27-amino-acid signal sequence	246:276	The precursor starts with a 27-amino-acid signal sequence, followed by the receptor alpha-subunit, a precursor processing enzyme cleavage site, then the beta-subunit containing a single 23-amino-acid transmembrane sequence.
2983222	1	10	theme	receptor	162:169	arg1	precursor					171:179	the human insulin receptor precursor	144:179	the human insulin receptor precursor	144:179	We have deduced the entire 1,370-amino-acid sequence of the human insulin receptor precursor from a single complementary DNA clone.
2983222	0	11	theme	insulin	6:12	arg1	receptor					14:21	Human insulin receptor	0:21	Human insulin receptor	0:21	Human insulin receptor and its relationship to the tyrosine kinase family of oncogenes.
2983222	1	12	theme	precursor	171:179	arg1	sequence					132:139	the entire 1,370-amino-acid sequence	104:139	the entire 1,370-amino-acid sequence of the human insulin receptor precursor	104:179	We have deduced the entire 1,370-amino-acid sequence of the human insulin receptor precursor from a single complementary DNA clone.
2983222	0	13	theme	Human	0:4	arg1	receptor					14:21	Human insulin receptor	0:21	Human insulin receptor	0:21	Human insulin receptor and its relationship to the tyrosine kinase family of oncogenes.
2983222	2	14	theme	receptor	295:302	arg1	beta-subunit					373:384	then the beta-subunit	364:384	then the beta-subunit containing a single 23-amino-acid transmembrane sequence	364:441	The precursor starts with a 27-amino-acid signal sequence, followed by the receptor alpha-subunit, a precursor processing enzyme cleavage site, then the beta-subunit containing a single 23-amino-acid transmembrane sequence.
2983222	2	14	theme	receptor	295:302	arg1	site					358:361	a precursor processing enzyme cleavage site	319:361	a precursor processing enzyme cleavage site	319:361	The precursor starts with a 27-amino-acid signal sequence, followed by the receptor alpha-subunit, a precursor processing enzyme cleavage site, then the beta-subunit containing a single 23-amino-acid transmembrane sequence.
2983222	2	14	theme	receptor	295:302	arg1	alpha-subunit					304:316	the receptor alpha-subunit	291:316	the receptor alpha-subunit	291:316	The precursor starts with a 27-amino-acid signal sequence, followed by the receptor alpha-subunit, a precursor processing enzyme cleavage site, then the beta-subunit containing a single 23-amino-acid transmembrane sequence.
2983222	3	15	theme	human	477:481	arg1	receptor					507:514	human epidermal growth factor receptor	477:514	human epidermal growth factor receptor	477:514	There are sequence homologies to human epidermal growth factor receptor and the members of the src family of oncogene products.
2983222	3	16	theme	oncogene	553:560	arg1	products					562:569	oncogene products	553:569	oncogene products	553:569	There are sequence homologies to human epidermal growth factor receptor and the members of the src family of oncogene products.
2983222	2	17	theme	transmembrane	420:432	arg1	sequence					434:441	a single 23-amino-acid transmembrane sequence	397:441	a single 23-amino-acid transmembrane sequence	397:441	The precursor starts with a 27-amino-acid signal sequence, followed by the receptor alpha-subunit, a precursor processing enzyme cleavage site, then the beta-subunit containing a single 23-amino-acid transmembrane sequence.
2983222	1	18	theme	human	148:152	arg1	precursor					171:179	the human insulin receptor precursor	144:179	the human insulin receptor precursor	144:179	We have deduced the entire 1,370-amino-acid sequence of the human insulin receptor precursor from a single complementary DNA clone.
2983222	1	19	theme	single	188:193	arg1	clone					213:217	a single complementary DNA clone	186:217	a single complementary DNA clone	186:217	We have deduced the entire 1,370-amino-acid sequence of the human insulin receptor precursor from a single complementary DNA clone.
2983222	2	20	theme	single	399:404	arg1	sequence					434:441	a single 23-amino-acid transmembrane sequence	397:441	a single 23-amino-acid transmembrane sequence	397:441	The precursor starts with a 27-amino-acid signal sequence, followed by the receptor alpha-subunit, a precursor processing enzyme cleavage site, then the beta-subunit containing a single 23-amino-acid transmembrane sequence.
2983222	1	21	theme	complementary	195:207	arg1	clone					213:217	a single complementary DNA clone	186:217	a single complementary DNA clone	186:217	We have deduced the entire 1,370-amino-acid sequence of the human insulin receptor precursor from a single complementary DNA clone.
2983222	1	22	theme	DNA	209:211	arg1	clone					213:217	a single complementary DNA clone	186:217	a single complementary DNA clone	186:217	We have deduced the entire 1,370-amino-acid sequence of the human insulin receptor precursor from a single complementary DNA clone.
2983222	2	23	contain	containing	386:395	arg1	beta-subunit					373:384	then the beta-subunit	364:384	then the beta-subunit containing a single 23-amino-acid transmembrane sequence	364:441	The precursor starts with a 27-amino-acid signal sequence, followed by the receptor alpha-subunit, a precursor processing enzyme cleavage site, then the beta-subunit containing a single 23-amino-acid transmembrane sequence.
2983222	2	23	contain	containing	386:395	arg2	sequence					434:441	a single 23-amino-acid transmembrane sequence	397:441	a single 23-amino-acid transmembrane sequence	397:441	The precursor starts with a 27-amino-acid signal sequence, followed by the receptor alpha-subunit, a precursor processing enzyme cleavage site, then the beta-subunit containing a single 23-amino-acid transmembrane sequence.
2983222	2	23	contain	containing	386:395	arg1	alpha-subunit					304:316	the receptor alpha-subunit	291:316	the receptor alpha-subunit	291:316	The precursor starts with a 27-amino-acid signal sequence, followed by the receptor alpha-subunit, a precursor processing enzyme cleavage site, then the beta-subunit containing a single 23-amino-acid transmembrane sequence.
2983222	2	24	theme	processing	331:340	arg1	site					358:361	a precursor processing enzyme cleavage site	319:361	a precursor processing enzyme cleavage site	319:361	The precursor starts with a 27-amino-acid signal sequence, followed by the receptor alpha-subunit, a precursor processing enzyme cleavage site, then the beta-subunit containing a single 23-amino-acid transmembrane sequence.
2983222	2	24	theme	processing	331:340	arg1	alpha-subunit					304:316	the receptor alpha-subunit	291:316	the receptor alpha-subunit	291:316	The precursor starts with a 27-amino-acid signal sequence, followed by the receptor alpha-subunit, a precursor processing enzyme cleavage site, then the beta-subunit containing a single 23-amino-acid transmembrane sequence.
2983222	2	25	theme	precursor	321:329	arg1	site					358:361	a precursor processing enzyme cleavage site	319:361	a precursor processing enzyme cleavage site	319:361	The precursor starts with a 27-amino-acid signal sequence, followed by the receptor alpha-subunit, a precursor processing enzyme cleavage site, then the beta-subunit containing a single 23-amino-acid transmembrane sequence.
2983222	2	25	theme	precursor	321:329	arg1	alpha-subunit					304:316	the receptor alpha-subunit	291:316	the receptor alpha-subunit	291:316	The precursor starts with a 27-amino-acid signal sequence, followed by the receptor alpha-subunit, a precursor processing enzyme cleavage site, then the beta-subunit containing a single 23-amino-acid transmembrane sequence.
2983222	2	26	theme	27-amino-acid	248:260	arg1	sequence					269:276	a 27-amino-acid signal sequence	246:276	a 27-amino-acid signal sequence	246:276	The precursor starts with a 27-amino-acid signal sequence, followed by the receptor alpha-subunit, a precursor processing enzyme cleavage site, then the beta-subunit containing a single 23-amino-acid transmembrane sequence.
2983222	1	27	theme	entire	108:113	arg1	sequence					132:139	the entire 1,370-amino-acid sequence	104:139	the entire 1,370-amino-acid sequence of the human insulin receptor precursor	104:179	We have deduced the entire 1,370-amino-acid sequence of the human insulin receptor precursor from a single complementary DNA clone.
2983222	3	28	theme	src	539:541	arg1	family					543:548	the src family	535:548	the src family of oncogene products	535:569	There are sequence homologies to human epidermal growth factor receptor and the members of the src family of oncogene products.
2983222	1	29	theme	1,370-amino-acid	115:130	arg1	sequence					132:139	the entire 1,370-amino-acid sequence	104:139	the entire 1,370-amino-acid sequence of the human insulin receptor precursor	104:179	We have deduced the entire 1,370-amino-acid sequence of the human insulin receptor precursor from a single complementary DNA clone.
2983222	3	30	theme	epidermal	483:491	arg1	receptor					507:514	human epidermal growth factor receptor	477:514	human epidermal growth factor receptor	477:514	There are sequence homologies to human epidermal growth factor receptor and the members of the src family of oncogene products.
2983222	0	31	theme	kinase	60:65	arg1	family					67:72	the tyrosine kinase family	47:72	the tyrosine kinase family of oncogenes	47:85	Human insulin receptor and its relationship to the tyrosine kinase family of oncogenes.
2983222	3	32	theme	sequence	454:461	arg1	homologies					463:472	sequence homologies	454:472	sequence homologies to human epidermal growth factor receptor	454:514	There are sequence homologies to human epidermal growth factor receptor and the members of the src family of oncogene products.
2983222	0	33	theme	tyrosine	51:58	arg1	family					67:72	the tyrosine kinase family	47:72	the tyrosine kinase family of oncogenes	47:85	Human insulin receptor and its relationship to the tyrosine kinase family of oncogenes.
11279502	10	0	theme	stable	1340:1345	arg1	complexes					1358:1366	unusually stable signalling complexes	1330:1366	unusually stable signalling complexes	1330:1366	This zipper-like oligomerization provides the structural basis for forming unusually stable signalling complexes at the T-cell surface, underscoring the importance of potent inhibitory signalling in human immune responses.
11279502	10	1	theme	T-cell	1375:1380	arg1	surface					1382:1388	the T-cell surface	1371:1388	the T-cell surface	1371:1388	This zipper-like oligomerization provides the structural basis for forming unusually stable signalling complexes at the T-cell surface, underscoring the importance of potent inhibitory signalling in human immune responses.
11279502	2	2	from	ligands	181:187	arg1	cells					225:229	antigen-presenting cells	206:229	antigen-presenting cells	206:229	The shared ligands B7-1 and B7-2 on antigen-presenting cells deliver the co-stimulatory signal through CD28 and CTLA-4 on T cells.
11279502	5	3	theme	extracellular	698:710	arg1	interactions					712:723	these extracellular interactions	692:723	these extracellular interactions	692:723	With the consequences of these signals well established, and details of the downstream signalling events emerging, understanding the molecular nature of these extracellular interactions becomes crucial.
11279502	5	4	theme	events	637:642	arg1	details					600:606	details	600:606	details of the downstream signalling events emerging	600:651	With the consequences of these signals well established, and details of the downstream signalling events emerging, understanding the molecular nature of these extracellular interactions becomes crucial.
11279502	5	4	theme	events	637:642	arg1	consequences					548:559	the consequences	544:559	the consequences of these signals well established	544:593	With the consequences of these signals well established, and details of the downstream signalling events emerging, understanding the molecular nature of these extracellular interactions becomes crucial.
11279502	3	5	theme	CTLA-4	363:368	arg1	signalling					370:379	CTLA-4 signalling	363:379	CTLA-4 signalling	363:379	Signalling through CD28 augments the T-cell response, whereas CTLA-4 signalling attenuates it.
11279502	8	6	theme	conserved	1084:1092	arg1	residues					1094:1101	highly conserved residues	1077:1101	highly conserved residues	1077:1101	CTLA-4 forms homodimers through a newly defined interface of highly conserved residues.
11279502	5	7	theme	interactions	712:723	arg1	nature					682:687	the molecular nature	668:687	the molecular nature of these extracellular interactions	668:723	With the consequences of these signals well established, and details of the downstream signalling events emerging, understanding the molecular nature of these extracellular interactions becomes crucial.
11279502	4	8	theme	animal	405:410	arg1	studies					412:418	Numerous animal studies	396:418	Numerous animal studies	396:418	Numerous animal studies and recent clinical trials indicate that manipulating these interactions holds considerable promise for immunotherapy.
11279502	7	9	theme	complementarity	999:1013	arg1	degree					983:988	an unusually high degree	965:988	an unusually high degree of shape complementarity	965:1013	In contrast to other interacting cell-surface molecules, the relatively small CTLA-4/B7-1 binding interface exhibits an unusually high degree of shape complementarity.
11279502	9	10	theme	B7-1	1238:1241	arg1	homodimers					1243:1252	bivalent B7-1 homodimers	1229:1252	bivalent B7-1 homodimers	1229:1252	In the crystal lattice, CTLA-4 and B7-1 pack in a strikingly periodic arrangement in which bivalent CTLA-4 homodimers bridge bivalent B7-1 homodimers.
11279502	9	11	from	pack	1144:1147	arg1	lattice					1119:1125	the crystal lattice	1107:1125	the crystal lattice	1107:1125	In the crystal lattice, CTLA-4 and B7-1 pack in a strikingly periodic arrangement in which bivalent CTLA-4 homodimers bridge bivalent B7-1 homodimers.
11279502	9	11	from	pack	1144:1147	arg1	arrangement					1174:1184	a strikingly periodic arrangement	1152:1184	a strikingly periodic arrangement in which bivalent CTLA-4 homodimers bridge bivalent B7-1 homodimers	1152:1252	In the crystal lattice, CTLA-4 and B7-1 pack in a strikingly periodic arrangement in which bivalent CTLA-4 homodimers bridge bivalent B7-1 homodimers.
11279502	4	12	theme	recent	424:429	arg1	trials					440:445	recent clinical trials	424:445	recent clinical trials	424:445	Numerous animal studies and recent clinical trials indicate that manipulating these interactions holds considerable promise for immunotherapy.
11279502	2	13	theme	T	292:292	arg1	cells					294:298	T cells	292:298	T cells	292:298	The shared ligands B7-1 and B7-2 on antigen-presenting cells deliver the co-stimulatory signal through CD28 and CTLA-4 on T cells.
11279502	7	14	theme	CTLA-4/B7-1	926:936	arg1	interface					946:954	the relatively small CTLA-4/B7-1 binding interface	905:954	the relatively small CTLA-4/B7-1 binding interface	905:954	In contrast to other interacting cell-surface molecules, the relatively small CTLA-4/B7-1 binding interface exhibits an unusually high degree of shape complementarity.
11279502	2	15	dep	ligands	181:187	arg1	ligands					181:187	The shared ligands	170:187	The shared ligands B7-1 and B7-2 on antigen-presenting cells	170:229	The shared ligands B7-1 and B7-2 on antigen-presenting cells deliver the co-stimulatory signal through CD28 and CTLA-4 on T cells.
11279502	2	15	dep	ligands	181:187	arg1	B7-2					198:201	B7-2	198:201	B7-2	198:201	The shared ligands B7-1 and B7-2 on antigen-presenting cells deliver the co-stimulatory signal through CD28 and CTLA-4 on T cells.
11279502	2	15	dep	ligands	181:187	arg1	B7-1					189:192	B7-1	189:192	B7-1	189:192	The shared ligands B7-1 and B7-2 on antigen-presenting cells deliver the co-stimulatory signal through CD28 and CTLA-4 on T cells.
11279502	4	16	theme	considerable	499:510	arg1	promise					512:518	considerable promise	499:518	considerable promise for immunotherapy	499:536	Numerous animal studies and recent clinical trials indicate that manipulating these interactions holds considerable promise for immunotherapy.
11279502	6	17	theme	crystal	761:767	arg1	structure					769:777	the crystal structure	757:777	the crystal structure of the human CTLA-4/B7-1 co-stimulatory complex at 3.0 A resolution	757:845	Here we report the crystal structure of the human CTLA-4/B7-1 co-stimulatory complex at 3.0 A resolution.
11279502	10	18	theme	structural	1301:1310	arg1	basis					1312:1316	the structural basis	1297:1316	the structural basis for forming unusually stable signalling complexes at the T-cell surface	1297:1388	This zipper-like oligomerization provides the structural basis for forming unusually stable signalling complexes at the T-cell surface, underscoring the importance of potent inhibitory signalling in human immune responses.
11279502	5	19	theme	molecular	672:680	arg1	nature					682:687	the molecular nature	668:687	the molecular nature of these extracellular interactions	668:723	With the consequences of these signals well established, and details of the downstream signalling events emerging, understanding the molecular nature of these extracellular interactions becomes crucial.
11279502	8	20	theme	residues	1094:1101	arg1	interface					1064:1072	a newly defined interface	1048:1072	a newly defined interface of highly conserved residues	1048:1101	CTLA-4 forms homodimers through a newly defined interface of highly conserved residues.
11279502	0	21	theme	immune	65:70	arg1	responses					72:80	human immune responses	59:80	human immune responses	59:80	Crystal structure of the B7-1/CTLA-4 complex that inhibits human immune responses.
11279502	1	22	theme	Optimal	83:89	arg1	responses					98:106	Optimal immune responses	83:106	Optimal immune responses	83:106	Optimal immune responses require both an antigen-specific and a co-stimulatory signal.
11279502	7	23	theme	small	920:924	arg1	interface					946:954	the relatively small CTLA-4/B7-1 binding interface	905:954	the relatively small CTLA-4/B7-1 binding interface	905:954	In contrast to other interacting cell-surface molecules, the relatively small CTLA-4/B7-1 binding interface exhibits an unusually high degree of shape complementarity.
11279502	0	24	theme	Crystal	0:6	arg1	structure					8:16	Crystal structure	0:16	Crystal structure of the B7-1/CTLA-4 complex that inhibits human immune responses.	0:81	Crystal structure of the B7-1/CTLA-4 complex that inhibits human immune responses.
11279502	7	25	theme	other	863:867	arg1	molecules					894:902	other interacting cell-surface molecules	863:902	other interacting cell-surface molecules	863:902	In contrast to other interacting cell-surface molecules, the relatively small CTLA-4/B7-1 binding interface exhibits an unusually high degree of shape complementarity.
11279502	4	26	theme	Numerous	396:403	arg1	studies					412:418	Numerous animal studies	396:418	Numerous animal studies	396:418	Numerous animal studies and recent clinical trials indicate that manipulating these interactions holds considerable promise for immunotherapy.
11279502	1	27	theme	immune	91:96	arg1	responses					98:106	Optimal immune responses	83:106	Optimal immune responses	83:106	Optimal immune responses require both an antigen-specific and a co-stimulatory signal.
11279502	10	28	theme	signalling	1440:1449	arg1	importance					1408:1417	the importance	1404:1417	the importance of potent inhibitory signalling in human immune responses	1404:1475	This zipper-like oligomerization provides the structural basis for forming unusually stable signalling complexes at the T-cell surface, underscoring the importance of potent inhibitory signalling in human immune responses.
11279502	10	29	theme	signalling	1347:1356	arg1	complexes					1358:1366	unusually stable signalling complexes	1330:1366	unusually stable signalling complexes	1330:1366	This zipper-like oligomerization provides the structural basis for forming unusually stable signalling complexes at the T-cell surface, underscoring the importance of potent inhibitory signalling in human immune responses.
11279502	5	30	theme	downstream	615:624	arg1	events					637:642	the downstream signalling events	611:642	the downstream signalling events emerging	611:651	With the consequences of these signals well established, and details of the downstream signalling events emerging, understanding the molecular nature of these extracellular interactions becomes crucial.
11279502	3	31	dep	augments	325:332	arg1	whereas					355:361	whereas	355:361	whereas	355:361	Signalling through CD28 augments the T-cell response, whereas CTLA-4 signalling attenuates it.
11279502	5	32	theme	signalling	626:635	arg1	events					637:642	the downstream signalling events	611:642	the downstream signalling events emerging	611:651	With the consequences of these signals well established, and details of the downstream signalling events emerging, understanding the molecular nature of these extracellular interactions becomes crucial.
11279502	10	33	theme	potent	1422:1427	arg1	signalling					1440:1449	potent inhibitory signalling	1422:1449	potent inhibitory signalling	1422:1449	This zipper-like oligomerization provides the structural basis for forming unusually stable signalling complexes at the T-cell surface, underscoring the importance of potent inhibitory signalling in human immune responses.
11279502	2	34	from	signal	258:263	arg1	cells					294:298	T cells	292:298	T cells	292:298	The shared ligands B7-1 and B7-2 on antigen-presenting cells deliver the co-stimulatory signal through CD28 and CTLA-4 on T cells.
11279502	6	35	from	resolution	836:845	arg1	structure					769:777	the crystal structure	757:777	the crystal structure of the human CTLA-4/B7-1 co-stimulatory complex at 3.0 A resolution	757:845	Here we report the crystal structure of the human CTLA-4/B7-1 co-stimulatory complex at 3.0 A resolution.
11279502	9	36	theme	periodic	1165:1172	arg1	arrangement					1174:1184	a strikingly periodic arrangement	1152:1184	a strikingly periodic arrangement in which bivalent CTLA-4 homodimers bridge bivalent B7-1 homodimers	1152:1252	In the crystal lattice, CTLA-4 and B7-1 pack in a strikingly periodic arrangement in which bivalent CTLA-4 homodimers bridge bivalent B7-1 homodimers.
11279502	10	37	theme	human	1454:1458	arg1	responses					1467:1475	human immune responses	1454:1475	human immune responses	1454:1475	This zipper-like oligomerization provides the structural basis for forming unusually stable signalling complexes at the T-cell surface, underscoring the importance of potent inhibitory signalling in human immune responses.
11279502	7	38	theme	cell-surface	881:892	arg1	molecules					894:902	other interacting cell-surface molecules	863:902	other interacting cell-surface molecules	863:902	In contrast to other interacting cell-surface molecules, the relatively small CTLA-4/B7-1 binding interface exhibits an unusually high degree of shape complementarity.
11279502	0	39	theme	complex	37:43	arg1	structure					8:16	Crystal structure	0:16	Crystal structure of the B7-1/CTLA-4 complex that inhibits human immune responses.	0:81	Crystal structure of the B7-1/CTLA-4 complex that inhibits human immune responses.
11279502	7	40	theme	binding	938:944	arg1	interface					946:954	the relatively small CTLA-4/B7-1 binding interface	905:954	the relatively small CTLA-4/B7-1 binding interface	905:954	In contrast to other interacting cell-surface molecules, the relatively small CTLA-4/B7-1 binding interface exhibits an unusually high degree of shape complementarity.
11279502	2	41	theme	co-stimulatory	243:256	arg1	signal					258:263	the co-stimulatory signal	239:263	the co-stimulatory signal through CD28 and CTLA-4 on T cells	239:298	The shared ligands B7-1 and B7-2 on antigen-presenting cells deliver the co-stimulatory signal through CD28 and CTLA-4 on T cells.
11279502	9	42	theme	bivalent	1195:1202	arg1	homodimers					1211:1220	bivalent CTLA-4 homodimers	1195:1220	bivalent CTLA-4 homodimers	1195:1220	In the crystal lattice, CTLA-4 and B7-1 pack in a strikingly periodic arrangement in which bivalent CTLA-4 homodimers bridge bivalent B7-1 homodimers.
11279502	0	43	theme	B7-1/CTLA-4	25:35	arg1	complex					37:43	the B7-1/CTLA-4 complex	21:43	the B7-1/CTLA-4 complex that inhibits human immune responses	21:80	Crystal structure of the B7-1/CTLA-4 complex that inhibits human immune responses.
11279502	2	44	theme	shared	174:179	arg1	ligands					181:187	The shared ligands	170:187	The shared ligands B7-1 and B7-2 on antigen-presenting cells	170:229	The shared ligands B7-1 and B7-2 on antigen-presenting cells deliver the co-stimulatory signal through CD28 and CTLA-4 on T cells.
11279502	2	44	theme	shared	174:179	arg1	B7-2					198:201	B7-2	198:201	B7-2	198:201	The shared ligands B7-1 and B7-2 on antigen-presenting cells deliver the co-stimulatory signal through CD28 and CTLA-4 on T cells.
11279502	2	44	theme	shared	174:179	arg1	B7-1					189:192	B7-1	189:192	B7-1	189:192	The shared ligands B7-1 and B7-2 on antigen-presenting cells deliver the co-stimulatory signal through CD28 and CTLA-4 on T cells.
11279502	9	45	theme	CTLA-4	1204:1209	arg1	homodimers					1211:1220	bivalent CTLA-4 homodimers	1195:1220	bivalent CTLA-4 homodimers	1195:1220	In the crystal lattice, CTLA-4 and B7-1 pack in a strikingly periodic arrangement in which bivalent CTLA-4 homodimers bridge bivalent B7-1 homodimers.
11279502	8	46	theme	defined	1056:1062	arg1	interface					1064:1072	a newly defined interface	1048:1072	a newly defined interface of highly conserved residues	1048:1101	CTLA-4 forms homodimers through a newly defined interface of highly conserved residues.
11279502	7	47	theme	interacting	869:879	arg1	molecules					894:902	other interacting cell-surface molecules	863:902	other interacting cell-surface molecules	863:902	In contrast to other interacting cell-surface molecules, the relatively small CTLA-4/B7-1 binding interface exhibits an unusually high degree of shape complementarity.
11279502	10	48	from	importance	1408:1417	arg1	responses					1467:1475	human immune responses	1454:1475	human immune responses	1454:1475	This zipper-like oligomerization provides the structural basis for forming unusually stable signalling complexes at the T-cell surface, underscoring the importance of potent inhibitory signalling in human immune responses.
11279502	10	49	theme	immune	1460:1465	arg1	responses					1467:1475	human immune responses	1454:1475	human immune responses	1454:1475	This zipper-like oligomerization provides the structural basis for forming unusually stable signalling complexes at the T-cell surface, underscoring the importance of potent inhibitory signalling in human immune responses.
11279502	2	50	theme	antigen-presenting	206:223	arg1	cells					225:229	antigen-presenting cells	206:229	antigen-presenting cells	206:229	The shared ligands B7-1 and B7-2 on antigen-presenting cells deliver the co-stimulatory signal through CD28 and CTLA-4 on T cells.
11279502	6	51	theme	complex	819:825	arg1	structure					769:777	the crystal structure	757:777	the crystal structure of the human CTLA-4/B7-1 co-stimulatory complex at 3.0 A resolution	757:845	Here we report the crystal structure of the human CTLA-4/B7-1 co-stimulatory complex at 3.0 A resolution.
11279502	6	52	theme	A	834:834	arg1	resolution					836:845	3.0 A resolution	830:845	3.0 A resolution	830:845	Here we report the crystal structure of the human CTLA-4/B7-1 co-stimulatory complex at 3.0 A resolution.
11279502	4	53	theme	clinical	431:438	arg1	trials					440:445	recent clinical trials	424:445	recent clinical trials	424:445	Numerous animal studies and recent clinical trials indicate that manipulating these interactions holds considerable promise for immunotherapy.
11279502	6	54	theme	co-stimulatory	804:817	arg1	complex					819:825	the human CTLA-4/B7-1 co-stimulatory complex	782:825	the human CTLA-4/B7-1 co-stimulatory complex	782:825	Here we report the crystal structure of the human CTLA-4/B7-1 co-stimulatory complex at 3.0 A resolution.
11279502	7	55	theme	shape	993:997	arg1	complementarity					999:1013	shape complementarity	993:1013	shape complementarity	993:1013	In contrast to other interacting cell-surface molecules, the relatively small CTLA-4/B7-1 binding interface exhibits an unusually high degree of shape complementarity.
11279502	9	56	theme	bivalent	1229:1236	arg1	homodimers					1243:1252	bivalent B7-1 homodimers	1229:1252	bivalent B7-1 homodimers	1229:1252	In the crystal lattice, CTLA-4 and B7-1 pack in a strikingly periodic arrangement in which bivalent CTLA-4 homodimers bridge bivalent B7-1 homodimers.
11279502	6	57	theme	CTLA-4/B7-1	792:802	arg1	complex					819:825	the human CTLA-4/B7-1 co-stimulatory complex	782:825	the human CTLA-4/B7-1 co-stimulatory complex	782:825	Here we report the crystal structure of the human CTLA-4/B7-1 co-stimulatory complex at 3.0 A resolution.
11279502	10	58	theme	inhibitory	1429:1438	arg1	signalling					1440:1449	potent inhibitory signalling	1422:1449	potent inhibitory signalling	1422:1449	This zipper-like oligomerization provides the structural basis for forming unusually stable signalling complexes at the T-cell surface, underscoring the importance of potent inhibitory signalling in human immune responses.
11279502	7	59	theme	high	978:981	arg1	degree					983:988	an unusually high degree	965:988	an unusually high degree of shape complementarity	965:1013	In contrast to other interacting cell-surface molecules, the relatively small CTLA-4/B7-1 binding interface exhibits an unusually high degree of shape complementarity.
11279502	3	60	theme	T-cell	338:343	arg1	response					345:352	the T-cell response	334:352	the T-cell response	334:352	Signalling through CD28 augments the T-cell response, whereas CTLA-4 signalling attenuates it.
11279502	6	61	theme	human	786:790	arg1	complex					819:825	the human CTLA-4/B7-1 co-stimulatory complex	782:825	the human CTLA-4/B7-1 co-stimulatory complex	782:825	Here we report the crystal structure of the human CTLA-4/B7-1 co-stimulatory complex at 3.0 A resolution.
11279502	9	62	theme	crystal	1111:1117	arg1	lattice					1119:1125	the crystal lattice	1107:1125	the crystal lattice	1107:1125	In the crystal lattice, CTLA-4 and B7-1 pack in a strikingly periodic arrangement in which bivalent CTLA-4 homodimers bridge bivalent B7-1 homodimers.
11279502	0	63	theme	human	59:63	arg1	responses					72:80	human immune responses	59:80	human immune responses	59:80	Crystal structure of the B7-1/CTLA-4 complex that inhibits human immune responses.
11279502	9	64	from	bridge	1222:1227	arg1	arrangement					1174:1184	a strikingly periodic arrangement	1152:1184	a strikingly periodic arrangement in which bivalent CTLA-4 homodimers bridge bivalent B7-1 homodimers	1152:1252	In the crystal lattice, CTLA-4 and B7-1 pack in a strikingly periodic arrangement in which bivalent CTLA-4 homodimers bridge bivalent B7-1 homodimers.
11279502	5	65	theme	signals	570:576	arg1	details					600:606	details	600:606	details of the downstream signalling events emerging	600:651	With the consequences of these signals well established, and details of the downstream signalling events emerging, understanding the molecular nature of these extracellular interactions becomes crucial.
11279502	5	65	theme	signals	570:576	arg1	consequences					548:559	the consequences	544:559	the consequences of these signals well established	544:593	With the consequences of these signals well established, and details of the downstream signalling events emerging, understanding the molecular nature of these extracellular interactions becomes crucial.
11279502	1	66	theme	co-stimulatory	147:160	arg1	signal					162:167	a co-stimulatory signal	145:167	a co-stimulatory signal	145:167	Optimal immune responses require both an antigen-specific and a co-stimulatory signal.
11279502	10	67	theme	zipper-like	1260:1270	arg1	oligomerization					1272:1286	This zipper-like oligomerization	1255:1286	This zipper-like oligomerization	1255:1286	This zipper-like oligomerization provides the structural basis for forming unusually stable signalling complexes at the T-cell surface, underscoring the importance of potent inhibitory signalling in human immune responses.
29717535	5	0	theme	ligands	737:743	arg1	groups					723:728	the alpha and beta phosphate groups	694:728	the alpha and beta phosphate groups of its ligands	694:743	The enzyme exhibits little preference for nucleobase type, and forms specific contacts with the alpha and beta phosphate groups of its ligands.
29717535	5	0	theme	ligands	737:743	arg1	ligands					737:743	its ligands	733:743	its ligands	733:743	The enzyme exhibits little preference for nucleobase type, and forms specific contacts with the alpha and beta phosphate groups of its ligands.
29717535	2	1	theme	cells	369:373	arg1	surface					352:358	the surface	348:358	the surface of these cells	348:373	CD203c (NPP3, ENPP3) regulates the inflammatory response of basophils via ATP hydrolysis and is a marker for allergen sensitivity on the surface of these cells.
29717535	2	2	from	marker	313:318	arg1	surface					352:358	the surface	348:358	the surface of these cells	348:373	CD203c (NPP3, ENPP3) regulates the inflammatory response of basophils via ATP hydrolysis and is a marker for allergen sensitivity on the surface of these cells.
29717535	8	3	theme	human	1000:1004	arg1	6C01					994:997	6C01	994:997	6C01	994:997	DATABASE Structural data are available in the Protein Data Bank under the accession numbers 6C01 (human NPP3) and 6C02 (human NPP3 T205A N594S with AMPCPP).
29717535	8	3	theme	human	1000:1004	arg1	NPP3					1006:1009	human NPP3	1000:1009	human NPP3	1000:1009	DATABASE Structural data are available in the Protein Data Bank under the accession numbers 6C01 (human NPP3) and 6C02 (human NPP3 T205A N594S with AMPCPP).
29717535	1	4	theme	extracellular	188:200	arg1	nucleotides					202:212	extracellular nucleotides	188:212	extracellular nucleotides	188:212	The ecto-nucleotide pyrophosphatase/phosphodiesterase (NPP) enzyme family modulates purinergic signaling by degrading extracellular nucleotides.
29717535	5	5	theme	nucleobase	644:653	arg1	type					655:658	nucleobase type	644:658	nucleobase type	644:658	The enzyme exhibits little preference for nucleobase type, and forms specific contacts with the alpha and beta phosphate groups of its ligands.
29717535	8	6	theme	Data	956:959	arg1	Bank					961:964	the Protein Data Bank	944:964	the Protein Data Bank	944:964	DATABASE Structural data are available in the Protein Data Bank under the accession numbers 6C01 (human NPP3) and 6C02 (human NPP3 T205A N594S with AMPCPP).
29717535	7	7	theme	substrate	857:865	arg1	recognition					867:877	substrate recognition	857:877	substrate recognition within the NPP family	857:899	These findings expand our understanding of substrate recognition within the NPP family.
29717535	3	8	theme	Multiple	376:383	arg1	roles					391:395	Multiple other roles	376:395	Multiple other roles	376:395	Multiple other roles and substrates have also been proposed for this protein.
29717535	2	9	dep	CD203c	215:220	arg1	ENPP3					229:233	ENPP3	229:233	ENPP3	229:233	CD203c (NPP3, ENPP3) regulates the inflammatory response of basophils via ATP hydrolysis and is a marker for allergen sensitivity on the surface of these cells.
29717535	2	9	dep	CD203c	215:220	arg1	NPP3					223:226	NPP3	223:226	NPP3	223:226	CD203c (NPP3, ENPP3) regulates the inflammatory response of basophils via ATP hydrolysis and is a marker for allergen sensitivity on the surface of these cells.
29717535	5	10	theme	phosphate	713:721	arg1	groups					723:728	the alpha and beta phosphate groups	694:728	the alpha and beta phosphate groups of its ligands	694:743	The enzyme exhibits little preference for nucleobase type, and forms specific contacts with the alpha and beta phosphate groups of its ligands.
29717535	5	10	theme	phosphate	713:721	arg1	ligands					737:743	its ligands	733:743	its ligands	733:743	The enzyme exhibits little preference for nucleobase type, and forms specific contacts with the alpha and beta phosphate groups of its ligands.
29717535	4	11	theme	molecular	488:496	arg1	functions					498:506	its molecular functions	484:506	its molecular functions	484:506	In order to gain insight into its molecular functions, we determined the crystal structure of human NPP3 as well as its complex with an ATP analog.
29717535	6	12	theme	protein	766:772	arg1	Dimerization					746:757	Dimerization	746:757	Dimerization of the protein	746:772	Dimerization of the protein does not affect its catalytic activity.
29717535	1	13	theme	ecto-nucleotide	74:88	arg1	family					137:142	The ecto-nucleotide pyrophosphatase/phosphodiesterase (NPP) enzyme family	70:142	The ecto-nucleotide pyrophosphatase/phosphodiesterase (NPP) enzyme family	70:142	The ecto-nucleotide pyrophosphatase/phosphodiesterase (NPP) enzyme family modulates purinergic signaling by degrading extracellular nucleotides.
29717535	8	14	dep	numbers	986:992	arg1	numbers					986:992	the accession numbers 6C01 (human NPP3) and 6C02	972:1019	the accession numbers 6C01 (human NPP3) and 6C02	972:1019	DATABASE Structural data are available in the Protein Data Bank under the accession numbers 6C01 (human NPP3) and 6C02 (human NPP3 T205A N594S with AMPCPP).
29717535	8	14	dep	numbers	986:992	arg1	6C01					994:997	6C01	994:997	6C01	994:997	DATABASE Structural data are available in the Protein Data Bank under the accession numbers 6C01 (human NPP3) and 6C02 (human NPP3 T205A N594S with AMPCPP).
29717535	8	14	dep	numbers	986:992	arg1	NPP3					1006:1009	human NPP3	1000:1009	human NPP3	1000:1009	DATABASE Structural data are available in the Protein Data Bank under the accession numbers 6C01 (human NPP3) and 6C02 (human NPP3 T205A N594S with AMPCPP).
29717535	8	14	dep	numbers	986:992	arg1	6C02					1016:1019	6C02	1016:1019	6C02	1016:1019	DATABASE Structural data are available in the Protein Data Bank under the accession numbers 6C01 (human NPP3) and 6C02 (human NPP3 T205A N594S with AMPCPP).
29717535	8	15	theme	accession	976:984	arg1	numbers					986:992	the accession numbers 6C01 (human NPP3) and 6C02	972:1019	the accession numbers 6C01 (human NPP3) and 6C02	972:1019	DATABASE Structural data are available in the Protein Data Bank under the accession numbers 6C01 (human NPP3) and 6C02 (human NPP3 T205A N594S with AMPCPP).
29717535	8	15	theme	accession	976:984	arg1	6C01					994:997	6C01	994:997	6C01	994:997	DATABASE Structural data are available in the Protein Data Bank under the accession numbers 6C01 (human NPP3) and 6C02 (human NPP3 T205A N594S with AMPCPP).
29717535	8	15	theme	accession	976:984	arg1	6C02					1016:1019	6C02	1016:1019	6C02	1016:1019	DATABASE Structural data are available in the Protein Data Bank under the accession numbers 6C01 (human NPP3) and 6C02 (human NPP3 T205A N594S with AMPCPP).
29717535	1	16	theme	pyrophosphatase/phosphodiesterase	90:122	arg1	family					137:142	The ecto-nucleotide pyrophosphatase/phosphodiesterase (NPP) enzyme family	70:142	The ecto-nucleotide pyrophosphatase/phosphodiesterase (NPP) enzyme family	70:142	The ecto-nucleotide pyrophosphatase/phosphodiesterase (NPP) enzyme family modulates purinergic signaling by degrading extracellular nucleotides.
29717535	0	17	theme	Structural	0:9	arg1	basis					11:15	Structural basis	0:15	Structural basis for nucleotide recognition by the ectoenzyme CD203c	0:67	Structural basis for nucleotide recognition by the ectoenzyme CD203c.
29717535	4	18	theme	NPP3	554:557	arg1	structure					535:543	the crystal structure	523:543	the crystal structure of human NPP3 as well as its complex with an ATP analog	523:599	In order to gain insight into its molecular functions, we determined the crystal structure of human NPP3 as well as its complex with an ATP analog.
29717535	4	18	theme	NPP3	554:557	arg1	complex					574:580	its complex	570:580	the crystal structure of human NPP3 as well as its complex with an ATP analog	523:599	In order to gain insight into its molecular functions, we determined the crystal structure of human NPP3 as well as its complex with an ATP analog.
29717535	0	19	theme	nucleotide	21:30	arg1	recognition					32:42	nucleotide recognition	21:42	nucleotide recognition by the ectoenzyme CD203c	21:67	Structural basis for nucleotide recognition by the ectoenzyme CD203c.
29717535	2	20	theme	allergen	324:331	arg1	sensitivity					333:343	allergen sensitivity	324:343	allergen sensitivity	324:343	CD203c (NPP3, ENPP3) regulates the inflammatory response of basophils via ATP hydrolysis and is a marker for allergen sensitivity on the surface of these cells.
29717535	3	21	theme	other	385:389	arg1	roles					391:395	Multiple other roles	376:395	Multiple other roles	376:395	Multiple other roles and substrates have also been proposed for this protein.
29717535	4	22	theme	human	548:552	arg1	NPP3					554:557	human NPP3	548:557	human NPP3	548:557	In order to gain insight into its molecular functions, we determined the crystal structure of human NPP3 as well as its complex with an ATP analog.
29717535	1	23	theme	NPP	125:127	arg1	family					137:142	The ecto-nucleotide pyrophosphatase/phosphodiesterase (NPP) enzyme family	70:142	The ecto-nucleotide pyrophosphatase/phosphodiesterase (NPP) enzyme family	70:142	The ecto-nucleotide pyrophosphatase/phosphodiesterase (NPP) enzyme family modulates purinergic signaling by degrading extracellular nucleotides.
29717535	4	24	with	structure	535:543	arg1	analog					594:599	an ATP analog	587:599	an ATP analog	587:599	In order to gain insight into its molecular functions, we determined the crystal structure of human NPP3 as well as its complex with an ATP analog.
29717535	8	25	dep	available	931:939	arg1	N594S					1039:1043	N594S	1039:1043	N594S	1039:1043	DATABASE Structural data are available in the Protein Data Bank under the accession numbers 6C01 (human NPP3) and 6C02 (human NPP3 T205A N594S with AMPCPP).
29717535	5	26	with	contacts	680:687	arg1	groups					723:728	the alpha and beta phosphate groups	694:728	the alpha and beta phosphate groups of its ligands	694:743	The enzyme exhibits little preference for nucleobase type, and forms specific contacts with the alpha and beta phosphate groups of its ligands.
29717535	5	26	with	contacts	680:687	arg1	ligands					737:743	its ligands	733:743	its ligands	733:743	The enzyme exhibits little preference for nucleobase type, and forms specific contacts with the alpha and beta phosphate groups of its ligands.
29717535	4	27	theme	crystal	527:533	arg1	structure					535:543	the crystal structure	523:543	the crystal structure of human NPP3 as well as its complex with an ATP analog	523:599	In order to gain insight into its molecular functions, we determined the crystal structure of human NPP3 as well as its complex with an ATP analog.
29717535	5	28	theme	alpha	698:702	arg1	groups					723:728	the alpha and beta phosphate groups	694:728	the alpha and beta phosphate groups of its ligands	694:743	The enzyme exhibits little preference for nucleobase type, and forms specific contacts with the alpha and beta phosphate groups of its ligands.
29717535	5	28	theme	alpha	698:702	arg1	ligands					737:743	its ligands	733:743	its ligands	733:743	The enzyme exhibits little preference for nucleobase type, and forms specific contacts with the alpha and beta phosphate groups of its ligands.
29717535	2	29	theme	inflammatory	250:261	arg1	response					263:270	the inflammatory response	246:270	the inflammatory response of basophils	246:283	CD203c (NPP3, ENPP3) regulates the inflammatory response of basophils via ATP hydrolysis and is a marker for allergen sensitivity on the surface of these cells.
29717535	8	30	theme	Structural	911:920	arg1	data					922:925	DATABASE Structural data	902:925	DATABASE Structural data	902:925	DATABASE Structural data are available in the Protein Data Bank under the accession numbers 6C01 (human NPP3) and 6C02 (human NPP3 T205A N594S with AMPCPP).
29717535	8	31	from	available	931:939	arg1	Bank					961:964	the Protein Data Bank	944:964	the Protein Data Bank	944:964	DATABASE Structural data are available in the Protein Data Bank under the accession numbers 6C01 (human NPP3) and 6C02 (human NPP3 T205A N594S with AMPCPP).
29717535	0	32	theme	ectoenzyme	51:60	arg1	CD203c					62:67	the ectoenzyme CD203c	47:67	the ectoenzyme CD203c	47:67	Structural basis for nucleotide recognition by the ectoenzyme CD203c.
29717535	8	33	theme	DATABASE	902:909	arg1	data					922:925	DATABASE Structural data	902:925	DATABASE Structural data	902:925	DATABASE Structural data are available in the Protein Data Bank under the accession numbers 6C01 (human NPP3) and 6C02 (human NPP3 T205A N594S with AMPCPP).
29717535	1	34	theme	enzyme	130:135	arg1	family					137:142	The ecto-nucleotide pyrophosphatase/phosphodiesterase (NPP) enzyme family	70:142	The ecto-nucleotide pyrophosphatase/phosphodiesterase (NPP) enzyme family	70:142	The ecto-nucleotide pyrophosphatase/phosphodiesterase (NPP) enzyme family modulates purinergic signaling by degrading extracellular nucleotides.
29717535	5	35	theme	little	622:627	arg1	preference					629:638	little preference	622:638	little preference for nucleobase type	622:658	The enzyme exhibits little preference for nucleobase type, and forms specific contacts with the alpha and beta phosphate groups of its ligands.
29717535	2	36	theme	ATP	289:291	arg1	hydrolysis					293:302	ATP hydrolysis	289:302	ATP hydrolysis	289:302	CD203c (NPP3, ENPP3) regulates the inflammatory response of basophils via ATP hydrolysis and is a marker for allergen sensitivity on the surface of these cells.
29717535	8	37	from	Bank	961:964	arg1	available					931:939	available	931:939	available	931:939	DATABASE Structural data are available in the Protein Data Bank under the accession numbers 6C01 (human NPP3) and 6C02 (human NPP3 T205A N594S with AMPCPP).
29717535	4	38	theme	ATP	590:592	arg1	analog					594:599	an ATP analog	587:599	an ATP analog	587:599	In order to gain insight into its molecular functions, we determined the crystal structure of human NPP3 as well as its complex with an ATP analog.
29717535	5	39	theme	specific	671:678	arg1	contacts					680:687	specific contacts	671:687	specific contacts with the alpha and beta phosphate groups of its ligands	671:743	The enzyme exhibits little preference for nucleobase type, and forms specific contacts with the alpha and beta phosphate groups of its ligands.
29717535	4	40	with	complex	574:580	arg1	analog					594:599	an ATP analog	587:599	an ATP analog	587:599	In order to gain insight into its molecular functions, we determined the crystal structure of human NPP3 as well as its complex with an ATP analog.
29717535	1	41	theme	purinergic	154:163	arg1	signaling					165:173	purinergic signaling	154:173	purinergic signaling	154:173	The ecto-nucleotide pyrophosphatase/phosphodiesterase (NPP) enzyme family modulates purinergic signaling by degrading extracellular nucleotides.
29717535	6	42	theme	catalytic	794:802	arg1	activity					804:811	its catalytic activity	790:811	its catalytic activity	790:811	Dimerization of the protein does not affect its catalytic activity.
29717535	2	43	theme	basophils	275:283	arg1	response					263:270	the inflammatory response	246:270	the inflammatory response of basophils	246:283	CD203c (NPP3, ENPP3) regulates the inflammatory response of basophils via ATP hydrolysis and is a marker for allergen sensitivity on the surface of these cells.
29717535	7	44	theme	NPP	890:892	arg1	family					894:899	the NPP family	886:899	the NPP family	886:899	These findings expand our understanding of substrate recognition within the NPP family.
29717535	8	45	theme	Protein	948:954	arg1	Bank					961:964	the Protein Data Bank	944:964	the Protein Data Bank	944:964	DATABASE Structural data are available in the Protein Data Bank under the accession numbers 6C01 (human NPP3) and 6C02 (human NPP3 T205A N594S with AMPCPP).
29717535	7	46	theme	recognition	867:877	arg1	understanding					840:852	our understanding	836:852	our understanding of substrate recognition within the NPP family	836:899	These findings expand our understanding of substrate recognition within the NPP family.
29717535	5	47	theme	beta	708:711	arg1	groups					723:728	the alpha and beta phosphate groups	694:728	the alpha and beta phosphate groups of its ligands	694:743	The enzyme exhibits little preference for nucleobase type, and forms specific contacts with the alpha and beta phosphate groups of its ligands.
29717535	5	47	theme	beta	708:711	arg1	ligands					737:743	its ligands	733:743	its ligands	733:743	The enzyme exhibits little preference for nucleobase type, and forms specific contacts with the alpha and beta phosphate groups of its ligands.
18775332	5	0	theme	class	1207:1211	arg1	assembly					1184:1191	assembly	1184:1191	assembly of the "tall" class of gp130 family cytokine receptor complexes including LIF, IL-27, IL-12, and others	1184:1295	These studies also enumerate the organizing principles for assembly of the "tall" class of gp130 family cytokine receptor complexes including LIF, IL-27, IL-12, and others.
18775332	4	1	theme	receptor	933:940	arg1	segments					974:981	the receptor extracellular and transmembrane segments	929:981	the receptor extracellular and transmembrane segments	929:981	Single particle electron microscopic analysis of the full-length gp130/LIF-R/CNTF-Ralpha/CNTF quaternary complex elucidates an asymmetric structural arrangement, in which the receptor extracellular and transmembrane segments join as a continuous, rigid unit, poised to sensitively transduce ligand engagement to the membrane-proximal intracellular signaling regions.
18775332	5	2	theme	tall	1201:1204	arg1	class					1207:1211	the "tall" class	1196:1211	the "tall" class of gp130 family cytokine receptor complexes including LIF, IL-27, IL-12, and others	1196:1295	These studies also enumerate the organizing principles for assembly of the "tall" class of gp130 family cytokine receptor complexes including LIF, IL-27, IL-12, and others.
18775332	4	3	theme	ligand	1049:1054	arg1	engagement					1056:1065	ligand engagement	1049:1065	ligand engagement	1049:1065	Single particle electron microscopic analysis of the full-length gp130/LIF-R/CNTF-Ralpha/CNTF quaternary complex elucidates an asymmetric structural arrangement, in which the receptor extracellular and transmembrane segments join as a continuous, rigid unit, poised to sensitively transduce ligand engagement to the membrane-proximal intracellular signaling regions.
18775332	3	4	theme	noncooperative	693:706	arg1	energetics					708:717	noncooperative energetics	693:717	noncooperative energetics	693:717	Thermodynamic analysis indicates that, unlike the cooperative assembly of the symmetric gp130/Interleukin-6/IL-6Ralpha hexameric complex, CNTF/CNTF-Ralpha heterodimerizes gp130 and LIF-R via noncooperative energetics to form an asymmetric 1:1:1:1 complex.
18775332	4	5	theme	full-length	811:821	arg1	complex					863:869	the full-length gp130/LIF-R/CNTF-Ralpha/CNTF quaternary complex	807:869	the full-length gp130/LIF-R/CNTF-Ralpha/CNTF quaternary complex	807:869	Single particle electron microscopic analysis of the full-length gp130/LIF-R/CNTF-Ralpha/CNTF quaternary complex elucidates an asymmetric structural arrangement, in which the receptor extracellular and transmembrane segments join as a continuous, rigid unit, poised to sensitively transduce ligand engagement to the membrane-proximal intracellular signaling regions.
18775332	5	6	theme	cytokine	1229:1236	arg1	LIF					1267:1269	LIF	1267:1269	LIF	1267:1269	These studies also enumerate the organizing principles for assembly of the "tall" class of gp130 family cytokine receptor complexes including LIF, IL-27, IL-12, and others.
18775332	5	6	theme	cytokine	1229:1236	arg1	complexes					1247:1255	gp130 family cytokine receptor complexes	1216:1255	gp130 family cytokine receptor complexes including LIF, IL-27, IL-12, and others	1216:1295	These studies also enumerate the organizing principles for assembly of the "tall" class of gp130 family cytokine receptor complexes including LIF, IL-27, IL-12, and others.
18775332	5	6	theme	cytokine	1229:1236	arg1	IL-12					1279:1283	IL-12	1279:1283	IL-12	1279:1283	These studies also enumerate the organizing principles for assembly of the "tall" class of gp130 family cytokine receptor complexes including LIF, IL-27, IL-12, and others.
18775332	5	6	theme	cytokine	1229:1236	arg1	others					1290:1295	others	1290:1295	others	1290:1295	These studies also enumerate the organizing principles for assembly of the "tall" class of gp130 family cytokine receptor complexes including LIF, IL-27, IL-12, and others.
18775332	5	6	theme	cytokine	1229:1236	arg1	IL-27					1272:1276	IL-27	1272:1276	IL-27	1272:1276	These studies also enumerate the organizing principles for assembly of the "tall" class of gp130 family cytokine receptor complexes including LIF, IL-27, IL-12, and others.
18775332	3	7	theme	Thermodynamic	502:514	arg1	analysis					516:523	Thermodynamic analysis	502:523	Thermodynamic analysis	502:523	Thermodynamic analysis indicates that, unlike the cooperative assembly of the symmetric gp130/Interleukin-6/IL-6Ralpha hexameric complex, CNTF/CNTF-Ralpha heterodimerizes gp130 and LIF-R via noncooperative energetics to form an asymmetric 1:1:1:1 complex.
18775332	4	8	theme	Single	758:763	arg1	analysis					795:802	Single particle electron microscopic analysis	758:802	Single particle electron microscopic analysis of the full-length gp130/LIF-R/CNTF-Ralpha/CNTF quaternary complex	758:869	Single particle electron microscopic analysis of the full-length gp130/LIF-R/CNTF-Ralpha/CNTF quaternary complex elucidates an asymmetric structural arrangement, in which the receptor extracellular and transmembrane segments join as a continuous, rigid unit, poised to sensitively transduce ligand engagement to the membrane-proximal intracellular signaling regions.
18775332	3	9	theme	1:1:1:1	741:747	arg1	complex					749:755	an asymmetric 1:1:1:1 complex	727:755	an asymmetric 1:1:1:1 complex	727:755	Thermodynamic analysis indicates that, unlike the cooperative assembly of the symmetric gp130/Interleukin-6/IL-6Ralpha hexameric complex, CNTF/CNTF-Ralpha heterodimerizes gp130 and LIF-R via noncooperative energetics to form an asymmetric 1:1:1:1 complex.
18775332	4	10	theme	extracellular	942:954	arg1	segments					974:981	the receptor extracellular and transmembrane segments	929:981	the receptor extracellular and transmembrane segments	929:981	Single particle electron microscopic analysis of the full-length gp130/LIF-R/CNTF-Ralpha/CNTF quaternary complex elucidates an asymmetric structural arrangement, in which the receptor extracellular and transmembrane segments join as a continuous, rigid unit, poised to sensitively transduce ligand engagement to the membrane-proximal intracellular signaling regions.
18775332	4	11	theme	microscopic	783:793	arg1	analysis					795:802	Single particle electron microscopic analysis	758:802	Single particle electron microscopic analysis of the full-length gp130/LIF-R/CNTF-Ralpha/CNTF quaternary complex	758:869	Single particle electron microscopic analysis of the full-length gp130/LIF-R/CNTF-Ralpha/CNTF quaternary complex elucidates an asymmetric structural arrangement, in which the receptor extracellular and transmembrane segments join as a continuous, rigid unit, poised to sensitively transduce ligand engagement to the membrane-proximal intracellular signaling regions.
18775332	4	12	dep	continuous	993:1002	arg1	rigid					1005:1009	rigid	1005:1009	rigid	1005:1009	Single particle electron microscopic analysis of the full-length gp130/LIF-R/CNTF-Ralpha/CNTF quaternary complex elucidates an asymmetric structural arrangement, in which the receptor extracellular and transmembrane segments join as a continuous, rigid unit, poised to sensitively transduce ligand engagement to the membrane-proximal intracellular signaling regions.
18775332	2	13	theme	alpha	472:476	arg1	receptor					478:485	its alpha receptor	468:485	its alpha receptor (CNTF-Ralpha)	468:499	Here, we biophysically and structurally characterize the full-length, transmembrane form of a quaternary cytokine receptor complex consisting of gp130, LIF-R, the cytokine Ciliary Neurotrophic Factor (CNTF), and its alpha receptor (CNTF-Ralpha).
18775332	2	13	theme	alpha	472:476	arg1	CNTF-Ralpha					488:498	CNTF-Ralpha	488:498	CNTF-Ralpha	488:498	Here, we biophysically and structurally characterize the full-length, transmembrane form of a quaternary cytokine receptor complex consisting of gp130, LIF-R, the cytokine Ciliary Neurotrophic Factor (CNTF), and its alpha receptor (CNTF-Ralpha).
18775332	0	14	theme	Structural	0:9	arg1	organization					11:22	Structural organization	0:22	Structural organization of a full-length gp130/LIF-R cytokine receptor transmembrane complex	0:91	Structural organization of a full-length gp130/LIF-R cytokine receptor transmembrane complex.
18775332	2	15	theme	complex	379:385	arg1	form					340:343	the full-length, transmembrane form	309:343	the full-length, transmembrane form of a quaternary cytokine receptor complex consisting of gp130, LIF-R, the cytokine Ciliary Neurotrophic Factor (CNTF), and its alpha receptor (CNTF-Ralpha)	309:499	Here, we biophysically and structurally characterize the full-length, transmembrane form of a quaternary cytokine receptor complex consisting of gp130, LIF-R, the cytokine Ciliary Neurotrophic Factor (CNTF), and its alpha receptor (CNTF-Ralpha).
18775332	2	16	theme	Ciliary	428:434	arg1	Factor					449:454	the cytokine Ciliary Neurotrophic Factor	415:454	the cytokine Ciliary Neurotrophic Factor (CNTF)	415:461	Here, we biophysically and structurally characterize the full-length, transmembrane form of a quaternary cytokine receptor complex consisting of gp130, LIF-R, the cytokine Ciliary Neurotrophic Factor (CNTF), and its alpha receptor (CNTF-Ralpha).
18775332	2	16	theme	Ciliary	428:434	arg1	CNTF					457:460	CNTF	457:460	CNTF	457:460	Here, we biophysically and structurally characterize the full-length, transmembrane form of a quaternary cytokine receptor complex consisting of gp130, LIF-R, the cytokine Ciliary Neurotrophic Factor (CNTF), and its alpha receptor (CNTF-Ralpha).
18775332	3	17	theme	asymmetric	730:739	arg1	complex					749:755	an asymmetric 1:1:1:1 complex	727:755	an asymmetric 1:1:1:1 complex	727:755	Thermodynamic analysis indicates that, unlike the cooperative assembly of the symmetric gp130/Interleukin-6/IL-6Ralpha hexameric complex, CNTF/CNTF-Ralpha heterodimerizes gp130 and LIF-R via noncooperative energetics to form an asymmetric 1:1:1:1 complex.
18775332	2	18	dep	full-length	313:323	arg1	transmembrane					326:338	transmembrane	326:338	transmembrane	326:338	Here, we biophysically and structurally characterize the full-length, transmembrane form of a quaternary cytokine receptor complex consisting of gp130, LIF-R, the cytokine Ciliary Neurotrophic Factor (CNTF), and its alpha receptor (CNTF-Ralpha).
18775332	2	19	theme	receptor	370:377	arg1	complex					379:385	a quaternary cytokine receptor complex	348:385	a quaternary cytokine receptor complex consisting of gp130, LIF-R, the cytokine Ciliary Neurotrophic Factor (CNTF), and its alpha receptor (CNTF-Ralpha)	348:499	Here, we biophysically and structurally characterize the full-length, transmembrane form of a quaternary cytokine receptor complex consisting of gp130, LIF-R, the cytokine Ciliary Neurotrophic Factor (CNTF), and its alpha receptor (CNTF-Ralpha).
18775332	2	20	theme	cytokine	419:426	arg1	Factor					449:454	the cytokine Ciliary Neurotrophic Factor	415:454	the cytokine Ciliary Neurotrophic Factor (CNTF)	415:461	Here, we biophysically and structurally characterize the full-length, transmembrane form of a quaternary cytokine receptor complex consisting of gp130, LIF-R, the cytokine Ciliary Neurotrophic Factor (CNTF), and its alpha receptor (CNTF-Ralpha).
18775332	2	20	theme	cytokine	419:426	arg1	CNTF					457:460	CNTF	457:460	CNTF	457:460	Here, we biophysically and structurally characterize the full-length, transmembrane form of a quaternary cytokine receptor complex consisting of gp130, LIF-R, the cytokine Ciliary Neurotrophic Factor (CNTF), and its alpha receptor (CNTF-Ralpha).
18775332	5	21	theme	gp130	1216:1220	arg1	LIF					1267:1269	LIF	1267:1269	LIF	1267:1269	These studies also enumerate the organizing principles for assembly of the "tall" class of gp130 family cytokine receptor complexes including LIF, IL-27, IL-12, and others.
18775332	5	21	theme	gp130	1216:1220	arg1	complexes					1247:1255	gp130 family cytokine receptor complexes	1216:1255	gp130 family cytokine receptor complexes including LIF, IL-27, IL-12, and others	1216:1295	These studies also enumerate the organizing principles for assembly of the "tall" class of gp130 family cytokine receptor complexes including LIF, IL-27, IL-12, and others.
18775332	5	21	theme	gp130	1216:1220	arg1	IL-12					1279:1283	IL-12	1279:1283	IL-12	1279:1283	These studies also enumerate the organizing principles for assembly of the "tall" class of gp130 family cytokine receptor complexes including LIF, IL-27, IL-12, and others.
18775332	5	21	theme	gp130	1216:1220	arg1	others					1290:1295	others	1290:1295	others	1290:1295	These studies also enumerate the organizing principles for assembly of the "tall" class of gp130 family cytokine receptor complexes including LIF, IL-27, IL-12, and others.
18775332	5	21	theme	gp130	1216:1220	arg1	IL-27					1272:1276	IL-27	1272:1276	IL-27	1272:1276	These studies also enumerate the organizing principles for assembly of the "tall" class of gp130 family cytokine receptor complexes including LIF, IL-27, IL-12, and others.
18775332	4	22	theme	intracellular	1092:1104	arg1	regions					1116:1122	the membrane-proximal intracellular signaling regions	1070:1122	the membrane-proximal intracellular signaling regions	1070:1122	Single particle electron microscopic analysis of the full-length gp130/LIF-R/CNTF-Ralpha/CNTF quaternary complex elucidates an asymmetric structural arrangement, in which the receptor extracellular and transmembrane segments join as a continuous, rigid unit, poised to sensitively transduce ligand engagement to the membrane-proximal intracellular signaling regions.
18775332	4	23	theme	signaling	1106:1114	arg1	regions					1116:1122	the membrane-proximal intracellular signaling regions	1070:1122	the membrane-proximal intracellular signaling regions	1070:1122	Single particle electron microscopic analysis of the full-length gp130/LIF-R/CNTF-Ralpha/CNTF quaternary complex elucidates an asymmetric structural arrangement, in which the receptor extracellular and transmembrane segments join as a continuous, rigid unit, poised to sensitively transduce ligand engagement to the membrane-proximal intracellular signaling regions.
18775332	0	24	theme	cytokine	53:60	arg1	complex					85:91	a full-length gp130/LIF-R cytokine receptor transmembrane complex	27:91	a full-length gp130/LIF-R cytokine receptor transmembrane complex	27:91	Structural organization of a full-length gp130/LIF-R cytokine receptor transmembrane complex.
18775332	2	25	theme	cytokine	361:368	arg1	complex					379:385	a quaternary cytokine receptor complex	348:385	a quaternary cytokine receptor complex consisting of gp130, LIF-R, the cytokine Ciliary Neurotrophic Factor (CNTF), and its alpha receptor (CNTF-Ralpha)	348:499	Here, we biophysically and structurally characterize the full-length, transmembrane form of a quaternary cytokine receptor complex consisting of gp130, LIF-R, the cytokine Ciliary Neurotrophic Factor (CNTF), and its alpha receptor (CNTF-Ralpha).
18775332	4	26	theme	continuous	993:1002	arg1	unit					1011:1014	a continuous, rigid unit	991:1014	a continuous, rigid unit	991:1014	Single particle electron microscopic analysis of the full-length gp130/LIF-R/CNTF-Ralpha/CNTF quaternary complex elucidates an asymmetric structural arrangement, in which the receptor extracellular and transmembrane segments join as a continuous, rigid unit, poised to sensitively transduce ligand engagement to the membrane-proximal intracellular signaling regions.
18775332	4	27	theme	asymmetric	885:894	arg1	arrangement					907:917	an asymmetric structural arrangement	882:917	an asymmetric structural arrangement	882:917	Single particle electron microscopic analysis of the full-length gp130/LIF-R/CNTF-Ralpha/CNTF quaternary complex elucidates an asymmetric structural arrangement, in which the receptor extracellular and transmembrane segments join as a continuous, rigid unit, poised to sensitively transduce ligand engagement to the membrane-proximal intracellular signaling regions.
18775332	1	28	theme	shared	105:110	arg1	gp130					94:98	gp130	94:98	gp130	94:98	gp130 is a shared receptor for at least nine cytokines and can signal either as a homodimer or as a heterodimer with Leukemia Inhibitory Factor Receptor (LIF-R).
18775332	1	28	theme	shared	105:110	arg1	receptor					112:119	a shared receptor	103:119	a shared receptor for at least nine cytokines	103:147	gp130 is a shared receptor for at least nine cytokines and can signal either as a homodimer or as a heterodimer with Leukemia Inhibitory Factor Receptor (LIF-R).
18775332	1	29	with	heterodimer	194:204	arg1	LIF-R					248:252	LIF-R	248:252	LIF-R	248:252	gp130 is a shared receptor for at least nine cytokines and can signal either as a homodimer or as a heterodimer with Leukemia Inhibitory Factor Receptor (LIF-R).
18775332	1	29	with	heterodimer	194:204	arg1	Receptor					238:245	Leukemia Inhibitory Factor Receptor	211:245	Leukemia Inhibitory Factor Receptor (LIF-R)	211:253	gp130 is a shared receptor for at least nine cytokines and can signal either as a homodimer or as a heterodimer with Leukemia Inhibitory Factor Receptor (LIF-R).
18775332	5	30	theme	organizing	1158:1167	arg1	principles					1169:1178	the organizing principles	1154:1178	the organizing principles for assembly of the "tall" class of gp130 family cytokine receptor complexes including LIF, IL-27, IL-12, and others	1154:1295	These studies also enumerate the organizing principles for assembly of the "tall" class of gp130 family cytokine receptor complexes including LIF, IL-27, IL-12, and others.
18775332	4	31	theme	particle	765:772	arg1	analysis					795:802	Single particle electron microscopic analysis	758:802	Single particle electron microscopic analysis of the full-length gp130/LIF-R/CNTF-Ralpha/CNTF quaternary complex	758:869	Single particle electron microscopic analysis of the full-length gp130/LIF-R/CNTF-Ralpha/CNTF quaternary complex elucidates an asymmetric structural arrangement, in which the receptor extracellular and transmembrane segments join as a continuous, rigid unit, poised to sensitively transduce ligand engagement to the membrane-proximal intracellular signaling regions.
18775332	0	32	theme	gp130/LIF-R	41:51	arg1	complex					85:91	a full-length gp130/LIF-R cytokine receptor transmembrane complex	27:91	a full-length gp130/LIF-R cytokine receptor transmembrane complex	27:91	Structural organization of a full-length gp130/LIF-R cytokine receptor transmembrane complex.
18775332	0	33	theme	full-length	29:39	arg1	complex					85:91	a full-length gp130/LIF-R cytokine receptor transmembrane complex	27:91	a full-length gp130/LIF-R cytokine receptor transmembrane complex	27:91	Structural organization of a full-length gp130/LIF-R cytokine receptor transmembrane complex.
18775332	4	34	theme	membrane-proximal	1074:1090	arg1	regions					1116:1122	the membrane-proximal intracellular signaling regions	1070:1122	the membrane-proximal intracellular signaling regions	1070:1122	Single particle electron microscopic analysis of the full-length gp130/LIF-R/CNTF-Ralpha/CNTF quaternary complex elucidates an asymmetric structural arrangement, in which the receptor extracellular and transmembrane segments join as a continuous, rigid unit, poised to sensitively transduce ligand engagement to the membrane-proximal intracellular signaling regions.
18775332	3	35	theme	complex	631:637	arg1	assembly					564:571	the cooperative assembly	548:571	the cooperative assembly of the symmetric gp130/Interleukin-6/IL-6Ralpha hexameric complex	548:637	Thermodynamic analysis indicates that, unlike the cooperative assembly of the symmetric gp130/Interleukin-6/IL-6Ralpha hexameric complex, CNTF/CNTF-Ralpha heterodimerizes gp130 and LIF-R via noncooperative energetics to form an asymmetric 1:1:1:1 complex.
18775332	5	36	theme	complexes	1247:1255	arg1	class					1207:1211	the "tall" class	1196:1211	the "tall" class of gp130 family cytokine receptor complexes including LIF, IL-27, IL-12, and others	1196:1295	These studies also enumerate the organizing principles for assembly of the "tall" class of gp130 family cytokine receptor complexes including LIF, IL-27, IL-12, and others.
18775332	0	37	theme	receptor	62:69	arg1	complex					85:91	a full-length gp130/LIF-R cytokine receptor transmembrane complex	27:91	a full-length gp130/LIF-R cytokine receptor transmembrane complex	27:91	Structural organization of a full-length gp130/LIF-R cytokine receptor transmembrane complex.
18775332	5	38	theme	family	1222:1227	arg1	LIF					1267:1269	LIF	1267:1269	LIF	1267:1269	These studies also enumerate the organizing principles for assembly of the "tall" class of gp130 family cytokine receptor complexes including LIF, IL-27, IL-12, and others.
18775332	5	38	theme	family	1222:1227	arg1	complexes					1247:1255	gp130 family cytokine receptor complexes	1216:1255	gp130 family cytokine receptor complexes including LIF, IL-27, IL-12, and others	1216:1295	These studies also enumerate the organizing principles for assembly of the "tall" class of gp130 family cytokine receptor complexes including LIF, IL-27, IL-12, and others.
18775332	5	38	theme	family	1222:1227	arg1	IL-12					1279:1283	IL-12	1279:1283	IL-12	1279:1283	These studies also enumerate the organizing principles for assembly of the "tall" class of gp130 family cytokine receptor complexes including LIF, IL-27, IL-12, and others.
18775332	5	38	theme	family	1222:1227	arg1	others					1290:1295	others	1290:1295	others	1290:1295	These studies also enumerate the organizing principles for assembly of the "tall" class of gp130 family cytokine receptor complexes including LIF, IL-27, IL-12, and others.
18775332	5	38	theme	family	1222:1227	arg1	IL-27					1272:1276	IL-27	1272:1276	IL-27	1272:1276	These studies also enumerate the organizing principles for assembly of the "tall" class of gp130 family cytokine receptor complexes including LIF, IL-27, IL-12, and others.
18775332	4	39	theme	structural	896:905	arg1	arrangement					907:917	an asymmetric structural arrangement	882:917	an asymmetric structural arrangement	882:917	Single particle electron microscopic analysis of the full-length gp130/LIF-R/CNTF-Ralpha/CNTF quaternary complex elucidates an asymmetric structural arrangement, in which the receptor extracellular and transmembrane segments join as a continuous, rigid unit, poised to sensitively transduce ligand engagement to the membrane-proximal intracellular signaling regions.
18775332	2	40	theme	Neurotrophic	436:447	arg1	Factor					449:454	the cytokine Ciliary Neurotrophic Factor	415:454	the cytokine Ciliary Neurotrophic Factor (CNTF)	415:461	Here, we biophysically and structurally characterize the full-length, transmembrane form of a quaternary cytokine receptor complex consisting of gp130, LIF-R, the cytokine Ciliary Neurotrophic Factor (CNTF), and its alpha receptor (CNTF-Ralpha).
18775332	2	40	theme	Neurotrophic	436:447	arg1	CNTF					457:460	CNTF	457:460	CNTF	457:460	Here, we biophysically and structurally characterize the full-length, transmembrane form of a quaternary cytokine receptor complex consisting of gp130, LIF-R, the cytokine Ciliary Neurotrophic Factor (CNTF), and its alpha receptor (CNTF-Ralpha).
18775332	5	41	theme	receptor	1238:1245	arg1	LIF					1267:1269	LIF	1267:1269	LIF	1267:1269	These studies also enumerate the organizing principles for assembly of the "tall" class of gp130 family cytokine receptor complexes including LIF, IL-27, IL-12, and others.
18775332	5	41	theme	receptor	1238:1245	arg1	complexes					1247:1255	gp130 family cytokine receptor complexes	1216:1255	gp130 family cytokine receptor complexes including LIF, IL-27, IL-12, and others	1216:1295	These studies also enumerate the organizing principles for assembly of the "tall" class of gp130 family cytokine receptor complexes including LIF, IL-27, IL-12, and others.
18775332	5	41	theme	receptor	1238:1245	arg1	IL-12					1279:1283	IL-12	1279:1283	IL-12	1279:1283	These studies also enumerate the organizing principles for assembly of the "tall" class of gp130 family cytokine receptor complexes including LIF, IL-27, IL-12, and others.
18775332	5	41	theme	receptor	1238:1245	arg1	others					1290:1295	others	1290:1295	others	1290:1295	These studies also enumerate the organizing principles for assembly of the "tall" class of gp130 family cytokine receptor complexes including LIF, IL-27, IL-12, and others.
18775332	5	41	theme	receptor	1238:1245	arg1	IL-27					1272:1276	IL-27	1272:1276	IL-27	1272:1276	These studies also enumerate the organizing principles for assembly of the "tall" class of gp130 family cytokine receptor complexes including LIF, IL-27, IL-12, and others.
18775332	4	42	theme	transmembrane	960:972	arg1	segments					974:981	the receptor extracellular and transmembrane segments	929:981	the receptor extracellular and transmembrane segments	929:981	Single particle electron microscopic analysis of the full-length gp130/LIF-R/CNTF-Ralpha/CNTF quaternary complex elucidates an asymmetric structural arrangement, in which the receptor extracellular and transmembrane segments join as a continuous, rigid unit, poised to sensitively transduce ligand engagement to the membrane-proximal intracellular signaling regions.
18775332	3	43	theme	cooperative	552:562	arg1	assembly					564:571	the cooperative assembly	548:571	the cooperative assembly of the symmetric gp130/Interleukin-6/IL-6Ralpha hexameric complex	548:637	Thermodynamic analysis indicates that, unlike the cooperative assembly of the symmetric gp130/Interleukin-6/IL-6Ralpha hexameric complex, CNTF/CNTF-Ralpha heterodimerizes gp130 and LIF-R via noncooperative energetics to form an asymmetric 1:1:1:1 complex.
18775332	4	44	theme	quaternary	852:861	arg1	complex					863:869	the full-length gp130/LIF-R/CNTF-Ralpha/CNTF quaternary complex	807:869	the full-length gp130/LIF-R/CNTF-Ralpha/CNTF quaternary complex	807:869	Single particle electron microscopic analysis of the full-length gp130/LIF-R/CNTF-Ralpha/CNTF quaternary complex elucidates an asymmetric structural arrangement, in which the receptor extracellular and transmembrane segments join as a continuous, rigid unit, poised to sensitively transduce ligand engagement to the membrane-proximal intracellular signaling regions.
18775332	4	45	theme	gp130/LIF-R/CNTF-Ralpha/CNTF	823:850	arg1	complex					863:869	the full-length gp130/LIF-R/CNTF-Ralpha/CNTF quaternary complex	807:869	the full-length gp130/LIF-R/CNTF-Ralpha/CNTF quaternary complex	807:869	Single particle electron microscopic analysis of the full-length gp130/LIF-R/CNTF-Ralpha/CNTF quaternary complex elucidates an asymmetric structural arrangement, in which the receptor extracellular and transmembrane segments join as a continuous, rigid unit, poised to sensitively transduce ligand engagement to the membrane-proximal intracellular signaling regions.
18775332	3	46	theme	gp130/Interleukin-6/IL-6Ralpha	590:619	arg1	complex					631:637	the symmetric gp130/Interleukin-6/IL-6Ralpha hexameric complex	576:637	the symmetric gp130/Interleukin-6/IL-6Ralpha hexameric complex	576:637	Thermodynamic analysis indicates that, unlike the cooperative assembly of the symmetric gp130/Interleukin-6/IL-6Ralpha hexameric complex, CNTF/CNTF-Ralpha heterodimerizes gp130 and LIF-R via noncooperative energetics to form an asymmetric 1:1:1:1 complex.
18775332	2	47	theme	full-length	313:323	arg1	form					340:343	the full-length, transmembrane form	309:343	the full-length, transmembrane form of a quaternary cytokine receptor complex consisting of gp130, LIF-R, the cytokine Ciliary Neurotrophic Factor (CNTF), and its alpha receptor (CNTF-Ralpha)	309:499	Here, we biophysically and structurally characterize the full-length, transmembrane form of a quaternary cytokine receptor complex consisting of gp130, LIF-R, the cytokine Ciliary Neurotrophic Factor (CNTF), and its alpha receptor (CNTF-Ralpha).
18775332	4	48	theme	electron	774:781	arg1	analysis					795:802	Single particle electron microscopic analysis	758:802	Single particle electron microscopic analysis of the full-length gp130/LIF-R/CNTF-Ralpha/CNTF quaternary complex	758:869	Single particle electron microscopic analysis of the full-length gp130/LIF-R/CNTF-Ralpha/CNTF quaternary complex elucidates an asymmetric structural arrangement, in which the receptor extracellular and transmembrane segments join as a continuous, rigid unit, poised to sensitively transduce ligand engagement to the membrane-proximal intracellular signaling regions.
18775332	3	49	theme	hexameric	621:629	arg1	complex					631:637	the symmetric gp130/Interleukin-6/IL-6Ralpha hexameric complex	576:637	the symmetric gp130/Interleukin-6/IL-6Ralpha hexameric complex	576:637	Thermodynamic analysis indicates that, unlike the cooperative assembly of the symmetric gp130/Interleukin-6/IL-6Ralpha hexameric complex, CNTF/CNTF-Ralpha heterodimerizes gp130 and LIF-R via noncooperative energetics to form an asymmetric 1:1:1:1 complex.
18775332	1	50	theme	Leukemia	211:218	arg1	LIF-R					248:252	LIF-R	248:252	LIF-R	248:252	gp130 is a shared receptor for at least nine cytokines and can signal either as a homodimer or as a heterodimer with Leukemia Inhibitory Factor Receptor (LIF-R).
18775332	1	50	theme	Leukemia	211:218	arg1	Receptor					238:245	Leukemia Inhibitory Factor Receptor	211:245	Leukemia Inhibitory Factor Receptor (LIF-R)	211:253	gp130 is a shared receptor for at least nine cytokines and can signal either as a homodimer or as a heterodimer with Leukemia Inhibitory Factor Receptor (LIF-R).
18775332	0	51	theme	complex	85:91	arg1	organization					11:22	Structural organization	0:22	Structural organization of a full-length gp130/LIF-R cytokine receptor transmembrane complex	0:91	Structural organization of a full-length gp130/LIF-R cytokine receptor transmembrane complex.
18775332	4	52	theme	complex	863:869	arg1	analysis					795:802	Single particle electron microscopic analysis	758:802	Single particle electron microscopic analysis of the full-length gp130/LIF-R/CNTF-Ralpha/CNTF quaternary complex	758:869	Single particle electron microscopic analysis of the full-length gp130/LIF-R/CNTF-Ralpha/CNTF quaternary complex elucidates an asymmetric structural arrangement, in which the receptor extracellular and transmembrane segments join as a continuous, rigid unit, poised to sensitively transduce ligand engagement to the membrane-proximal intracellular signaling regions.
18775332	2	53	theme	quaternary	350:359	arg1	complex					379:385	a quaternary cytokine receptor complex	348:385	a quaternary cytokine receptor complex consisting of gp130, LIF-R, the cytokine Ciliary Neurotrophic Factor (CNTF), and its alpha receptor (CNTF-Ralpha)	348:499	Here, we biophysically and structurally characterize the full-length, transmembrane form of a quaternary cytokine receptor complex consisting of gp130, LIF-R, the cytokine Ciliary Neurotrophic Factor (CNTF), and its alpha receptor (CNTF-Ralpha).
18775332	1	54	theme	Inhibitory	220:229	arg1	LIF-R					248:252	LIF-R	248:252	LIF-R	248:252	gp130 is a shared receptor for at least nine cytokines and can signal either as a homodimer or as a heterodimer with Leukemia Inhibitory Factor Receptor (LIF-R).
18775332	1	54	theme	Inhibitory	220:229	arg1	Receptor					238:245	Leukemia Inhibitory Factor Receptor	211:245	Leukemia Inhibitory Factor Receptor (LIF-R)	211:253	gp130 is a shared receptor for at least nine cytokines and can signal either as a homodimer or as a heterodimer with Leukemia Inhibitory Factor Receptor (LIF-R).
18775332	0	55	theme	transmembrane	71:83	arg1	complex					85:91	a full-length gp130/LIF-R cytokine receptor transmembrane complex	27:91	a full-length gp130/LIF-R cytokine receptor transmembrane complex	27:91	Structural organization of a full-length gp130/LIF-R cytokine receptor transmembrane complex.
18775332	5	56	theme	"	1205:1205	arg1	class					1207:1211	the "tall" class	1196:1211	the "tall" class of gp130 family cytokine receptor complexes including LIF, IL-27, IL-12, and others	1196:1295	These studies also enumerate the organizing principles for assembly of the "tall" class of gp130 family cytokine receptor complexes including LIF, IL-27, IL-12, and others.
18775332	3	57	theme	symmetric	580:588	arg1	complex					631:637	the symmetric gp130/Interleukin-6/IL-6Ralpha hexameric complex	576:637	the symmetric gp130/Interleukin-6/IL-6Ralpha hexameric complex	576:637	Thermodynamic analysis indicates that, unlike the cooperative assembly of the symmetric gp130/Interleukin-6/IL-6Ralpha hexameric complex, CNTF/CNTF-Ralpha heterodimerizes gp130 and LIF-R via noncooperative energetics to form an asymmetric 1:1:1:1 complex.
18775332	1	58	theme	Factor	231:236	arg1	LIF-R					248:252	LIF-R	248:252	LIF-R	248:252	gp130 is a shared receptor for at least nine cytokines and can signal either as a homodimer or as a heterodimer with Leukemia Inhibitory Factor Receptor (LIF-R).
18775332	1	58	theme	Factor	231:236	arg1	Receptor					238:245	Leukemia Inhibitory Factor Receptor	211:245	Leukemia Inhibitory Factor Receptor (LIF-R)	211:253	gp130 is a shared receptor for at least nine cytokines and can signal either as a homodimer or as a heterodimer with Leukemia Inhibitory Factor Receptor (LIF-R).
21854986	4	0	theme	ligand-specific	724:738	arg1	interactions					740:751	ligand-specific interactions	724:751	ligand-specific interactions that "tune" the relative IFN-binding affinities, in an apparent extracellular "ligand proofreading" mechanism that modulates biological activity	724:896	Receptor-ligand cross-reactivity is enabled by conserved receptor-ligand "anchor points" interspersed among ligand-specific interactions that "tune" the relative IFN-binding affinities, in an apparent extracellular "ligand proofreading" mechanism that modulates biological activity.
21854986	3	1	theme	heterotrimeric	486:499	arg1	architectures					501:513	heterotrimeric architectures	486:513	heterotrimeric architectures	486:513	The crystal structures of two human type I IFN ternary signaling complexes containing IFNα2 and IFNω reveal recognition modes and heterotrimeric architectures that are unique among the cytokine receptor superfamily but conserved between different type I IFNs.
21854986	5	2	theme	phosphorylation	1173:1187	arg1	profiles					1189:1196	differential STAT phosphorylation profiles	1155:1196	differential STAT phosphorylation profiles	1155:1196	Functional differences between IFNs are linked to their respective receptor recognition chemistries, in concert with a ligand-induced conformational change in IFNAR1, that collectively control signal initiation and complex stability, ultimately regulating differential STAT phosphorylation profiles, receptor internalization rates, and downstream gene expression patterns.
21854986	0	3	theme	I	81:81	arg1	interferons					83:93	type I interferons	76:93	type I interferons	76:93	Structural linkage between ligand discrimination and receptor activation by type I interferons.
21854986	5	4	from	patterns	1262:1269	arg1	concert					1003:1009	concert	1003:1009	concert with a ligand-induced conformational change in IFNAR1	1003:1063	Functional differences between IFNs are linked to their respective receptor recognition chemistries, in concert with a ligand-induced conformational change in IFNAR1, that collectively control signal initiation and complex stability, ultimately regulating differential STAT phosphorylation profiles, receptor internalization rates, and downstream gene expression patterns.
21854986	2	5	theme	different	323:331	arg1	effects					347:353	markedly different physiological effects	314:353	markedly different physiological effects	314:353	Sixteen human type I IFN variants signal through the same cell-surface receptors, IFNAR1 and IFNAR2, yet they can evoke markedly different physiological effects.
21854986	4	6	theme	relative	769:776	arg1	affinities					790:799	the relative IFN-binding affinities	765:799	the relative IFN-binding affinities	765:799	Receptor-ligand cross-reactivity is enabled by conserved receptor-ligand "anchor points" interspersed among ligand-specific interactions that "tune" the relative IFN-binding affinities, in an apparent extracellular "ligand proofreading" mechanism that modulates biological activity.
21854986	5	7	attach	linked	939:944	arg1	rates					1224:1228	receptor internalization rates	1199:1228	receptor internalization rates	1199:1228	Functional differences between IFNs are linked to their respective receptor recognition chemistries, in concert with a ligand-induced conformational change in IFNAR1, that collectively control signal initiation and complex stability, ultimately regulating differential STAT phosphorylation profiles, receptor internalization rates, and downstream gene expression patterns.
21854986	5	7	attach	linked	939:944	arg2	differences					910:920	Functional differences	899:920	Functional differences between IFNs	899:933	Functional differences between IFNs are linked to their respective receptor recognition chemistries, in concert with a ligand-induced conformational change in IFNAR1, that collectively control signal initiation and complex stability, ultimately regulating differential STAT phosphorylation profiles, receptor internalization rates, and downstream gene expression patterns.
21854986	5	7	attach	linked	939:944	arg1	patterns					1262:1269	downstream gene expression patterns	1235:1269	downstream gene expression patterns	1235:1269	Functional differences between IFNs are linked to their respective receptor recognition chemistries, in concert with a ligand-induced conformational change in IFNAR1, that collectively control signal initiation and complex stability, ultimately regulating differential STAT phosphorylation profiles, receptor internalization rates, and downstream gene expression patterns.
21854986	5	7	attach	linked	939:944	arg1	chemistries					987:997	their respective receptor recognition chemistries	949:997	their respective receptor recognition chemistries	949:997	Functional differences between IFNs are linked to their respective receptor recognition chemistries, in concert with a ligand-induced conformational change in IFNAR1, that collectively control signal initiation and complex stability, ultimately regulating differential STAT phosphorylation profiles, receptor internalization rates, and downstream gene expression patterns.
21854986	3	8	theme	cytokine	541:548	arg1	superfamily					559:569	the cytokine receptor superfamily	537:569	the cytokine receptor superfamily	537:569	The crystal structures of two human type I IFN ternary signaling complexes containing IFNα2 and IFNω reveal recognition modes and heterotrimeric architectures that are unique among the cytokine receptor superfamily but conserved between different type I IFNs.
21854986	2	9	dep	different	323:331	arg1	physiological					333:345	physiological	333:345	physiological	333:345	Sixteen human type I IFN variants signal through the same cell-surface receptors, IFNAR1 and IFNAR2, yet they can evoke markedly different physiological effects.
21854986	5	10	theme	Functional	899:908	arg1	differences					910:920	Functional differences	899:920	Functional differences between IFNs	899:933	Functional differences between IFNs are linked to their respective receptor recognition chemistries, in concert with a ligand-induced conformational change in IFNAR1, that collectively control signal initiation and complex stability, ultimately regulating differential STAT phosphorylation profiles, receptor internalization rates, and downstream gene expression patterns.
21854986	4	11	theme	biological	878:887	arg1	activity					889:896	biological activity	878:896	biological activity	878:896	Receptor-ligand cross-reactivity is enabled by conserved receptor-ligand "anchor points" interspersed among ligand-specific interactions that "tune" the relative IFN-binding affinities, in an apparent extracellular "ligand proofreading" mechanism that modulates biological activity.
21854986	5	12	from	change	1048:1053	arg1	IFNAR1					1058:1063	IFNAR1	1058:1063	IFNAR1	1058:1063	Functional differences between IFNs are linked to their respective receptor recognition chemistries, in concert with a ligand-induced conformational change in IFNAR1, that collectively control signal initiation and complex stability, ultimately regulating differential STAT phosphorylation profiles, receptor internalization rates, and downstream gene expression patterns.
21854986	5	13	theme	conformational	1033:1046	arg1	change					1048:1053	a ligand-induced conformational change	1016:1053	a ligand-induced conformational change in IFNAR1	1016:1063	Functional differences between IFNs are linked to their respective receptor recognition chemistries, in concert with a ligand-induced conformational change in IFNAR1, that collectively control signal initiation and complex stability, ultimately regulating differential STAT phosphorylation profiles, receptor internalization rates, and downstream gene expression patterns.
21854986	4	14	theme	points	697:702	arg1	"					703:703	anchor points"	690:703	conserved receptor-ligand "anchor points" interspersed among ligand-specific interactions that "tune" the relative IFN-binding affinities, in an apparent extracellular "ligand proofreading" mechanism that modulates biological activity	663:896	Receptor-ligand cross-reactivity is enabled by conserved receptor-ligand "anchor points" interspersed among ligand-specific interactions that "tune" the relative IFN-binding affinities, in an apparent extracellular "ligand proofreading" mechanism that modulates biological activity.
21854986	3	15	theme	signaling	411:419	arg1	complexes					421:429	two human type I IFN ternary signaling complexes	382:429	two human type I IFN ternary signaling complexes containing IFNα2 and IFNω	382:455	The crystal structures of two human type I IFN ternary signaling complexes containing IFNα2 and IFNω reveal recognition modes and heterotrimeric architectures that are unique among the cytokine receptor superfamily but conserved between different type I IFNs.
21854986	3	16	theme	human	386:390	arg1	complexes					421:429	two human type I IFN ternary signaling complexes	382:429	two human type I IFN ternary signaling complexes containing IFNα2 and IFNω	382:455	The crystal structures of two human type I IFN ternary signaling complexes containing IFNα2 and IFNω reveal recognition modes and heterotrimeric architectures that are unique among the cytokine receptor superfamily but conserved between different type I IFNs.
21854986	2	17	theme	cell-surface	252:263	arg1	IFNAR2					287:292	IFNAR2	287:292	IFNAR2	287:292	Sixteen human type I IFN variants signal through the same cell-surface receptors, IFNAR1 and IFNAR2, yet they can evoke markedly different physiological effects.
21854986	2	17	theme	cell-surface	252:263	arg1	IFNAR1					276:281	IFNAR1	276:281	IFNAR1	276:281	Sixteen human type I IFN variants signal through the same cell-surface receptors, IFNAR1 and IFNAR2, yet they can evoke markedly different physiological effects.
21854986	2	17	theme	cell-surface	252:263	arg1	receptors					265:273	the same cell-surface receptors	243:273	the same cell-surface receptors	243:273	Sixteen human type I IFN variants signal through the same cell-surface receptors, IFNAR1 and IFNAR2, yet they can evoke markedly different physiological effects.
21854986	3	18	theme	complexes	421:429	arg1	structures					368:377	The crystal structures	356:377	The crystal structures of two human type I IFN ternary signaling complexes containing IFNα2 and IFNω	356:455	The crystal structures of two human type I IFN ternary signaling complexes containing IFNα2 and IFNω reveal recognition modes and heterotrimeric architectures that are unique among the cytokine receptor superfamily but conserved between different type I IFNs.
21854986	5	19	with	concert	1003:1009	arg1	change					1048:1053	a ligand-induced conformational change	1016:1053	a ligand-induced conformational change in IFNAR1	1016:1063	Functional differences between IFNs are linked to their respective receptor recognition chemistries, in concert with a ligand-induced conformational change in IFNAR1, that collectively control signal initiation and complex stability, ultimately regulating differential STAT phosphorylation profiles, receptor internalization rates, and downstream gene expression patterns.
21854986	5	20	theme	receptor	1199:1206	arg1	rates					1224:1228	receptor internalization rates	1199:1228	receptor internalization rates	1199:1228	Functional differences between IFNs are linked to their respective receptor recognition chemistries, in concert with a ligand-induced conformational change in IFNAR1, that collectively control signal initiation and complex stability, ultimately regulating differential STAT phosphorylation profiles, receptor internalization rates, and downstream gene expression patterns.
21854986	5	21	from	chemistries	987:997	arg1	concert					1003:1009	concert	1003:1009	concert with a ligand-induced conformational change in IFNAR1	1003:1063	Functional differences between IFNs are linked to their respective receptor recognition chemistries, in concert with a ligand-induced conformational change in IFNAR1, that collectively control signal initiation and complex stability, ultimately regulating differential STAT phosphorylation profiles, receptor internalization rates, and downstream gene expression patterns.
21854986	3	22	theme	IFN	399:401	arg1	complexes					421:429	two human type I IFN ternary signaling complexes	382:429	two human type I IFN ternary signaling complexes containing IFNα2 and IFNω	382:455	The crystal structures of two human type I IFN ternary signaling complexes containing IFNα2 and IFNω reveal recognition modes and heterotrimeric architectures that are unique among the cytokine receptor superfamily but conserved between different type I IFNs.
21854986	0	23	theme	Structural	0:9	arg1	linkage					11:17	Structural linkage	0:17	Structural linkage between ligand discrimination and receptor activation by type I interferons.	0:94	Structural linkage between ligand discrimination and receptor activation by type I interferons.
21854986	1	24	theme	Type	96:99	arg1	cytokines					136:144	important cytokines	126:144	important cytokines for innate immunity against viruses and cancer	126:191	Type I Interferons (IFNs) are important cytokines for innate immunity against viruses and cancer.
21854986	1	24	theme	Type	96:99	arg1	IFNs					116:119	IFNs	116:119	IFNs	116:119	Type I Interferons (IFNs) are important cytokines for innate immunity against viruses and cancer.
21854986	1	24	theme	Type	96:99	arg1	Interferons					103:113	Type I Interferons	96:113	Type I Interferons (IFNs)	96:120	Type I Interferons (IFNs) are important cytokines for innate immunity against viruses and cancer.
21854986	3	25	theme	ternary	403:409	arg1	complexes					421:429	two human type I IFN ternary signaling complexes	382:429	two human type I IFN ternary signaling complexes containing IFNα2 and IFNω	382:455	The crystal structures of two human type I IFN ternary signaling complexes containing IFNα2 and IFNω reveal recognition modes and heterotrimeric architectures that are unique among the cytokine receptor superfamily but conserved between different type I IFNs.
21854986	0	26	theme	ligand	27:32	arg1	discrimination					34:47	ligand discrimination	27:47	ligand discrimination	27:47	Structural linkage between ligand discrimination and receptor activation by type I interferons.
21854986	5	27	theme	STAT	1168:1171	arg1	profiles					1189:1196	differential STAT phosphorylation profiles	1155:1196	differential STAT phosphorylation profiles	1155:1196	Functional differences between IFNs are linked to their respective receptor recognition chemistries, in concert with a ligand-induced conformational change in IFNAR1, that collectively control signal initiation and complex stability, ultimately regulating differential STAT phosphorylation profiles, receptor internalization rates, and downstream gene expression patterns.
21854986	3	28	theme	different	593:601	arg1	IFNs					610:613	different type I IFNs	593:613	different type I IFNs	593:613	The crystal structures of two human type I IFN ternary signaling complexes containing IFNα2 and IFNω reveal recognition modes and heterotrimeric architectures that are unique among the cytokine receptor superfamily but conserved between different type I IFNs.
21854986	1	29	theme	I	101:101	arg1	cytokines					136:144	important cytokines	126:144	important cytokines for innate immunity against viruses and cancer	126:191	Type I Interferons (IFNs) are important cytokines for innate immunity against viruses and cancer.
21854986	1	29	theme	I	101:101	arg1	IFNs					116:119	IFNs	116:119	IFNs	116:119	Type I Interferons (IFNs) are important cytokines for innate immunity against viruses and cancer.
21854986	1	29	theme	I	101:101	arg1	Interferons					103:113	Type I Interferons	96:113	Type I Interferons (IFNs)	96:120	Type I Interferons (IFNs) are important cytokines for innate immunity against viruses and cancer.
21854986	4	30	theme	"	851:851	arg1	mechanism					853:861	an apparent extracellular "ligand proofreading" mechanism	805:861	an apparent extracellular "ligand proofreading" mechanism that modulates biological activity	805:896	Receptor-ligand cross-reactivity is enabled by conserved receptor-ligand "anchor points" interspersed among ligand-specific interactions that "tune" the relative IFN-binding affinities, in an apparent extracellular "ligand proofreading" mechanism that modulates biological activity.
21854986	3	31	theme	crystal	360:366	arg1	structures					368:377	The crystal structures	356:377	The crystal structures of two human type I IFN ternary signaling complexes containing IFNα2 and IFNω	356:455	The crystal structures of two human type I IFN ternary signaling complexes containing IFNα2 and IFNω reveal recognition modes and heterotrimeric architectures that are unique among the cytokine receptor superfamily but conserved between different type I IFNs.
21854986	1	32	theme	innate	150:155	arg1	immunity					157:164	innate immunity	150:164	innate immunity against viruses and cancer	150:191	Type I Interferons (IFNs) are important cytokines for innate immunity against viruses and cancer.
21854986	5	33	theme	ligand-induced	1018:1031	arg1	change					1048:1053	a ligand-induced conformational change	1016:1053	a ligand-induced conformational change in IFNAR1	1016:1063	Functional differences between IFNs are linked to their respective receptor recognition chemistries, in concert with a ligand-induced conformational change in IFNAR1, that collectively control signal initiation and complex stability, ultimately regulating differential STAT phosphorylation profiles, receptor internalization rates, and downstream gene expression patterns.
21854986	3	34	theme	type	392:395	arg1	IFN					399:401	type I IFN	392:401	two human type I IFN ternary signaling complexes containing IFNα2 and IFNω	382:455	The crystal structures of two human type I IFN ternary signaling complexes containing IFNα2 and IFNω reveal recognition modes and heterotrimeric architectures that are unique among the cytokine receptor superfamily but conserved between different type I IFNs.
21854986	3	35	contain	containing	431:440	arg2	IFNω					452:455	IFNω	452:455	IFNω	452:455	The crystal structures of two human type I IFN ternary signaling complexes containing IFNα2 and IFNω reveal recognition modes and heterotrimeric architectures that are unique among the cytokine receptor superfamily but conserved between different type I IFNs.
21854986	3	35	contain	containing	431:440	arg2	IFNα2					442:446	IFNα2	442:446	IFNα2	442:446	The crystal structures of two human type I IFN ternary signaling complexes containing IFNα2 and IFNω reveal recognition modes and heterotrimeric architectures that are unique among the cytokine receptor superfamily but conserved between different type I IFNs.
21854986	3	35	contain	containing	431:440	arg1	complexes					421:429	two human type I IFN ternary signaling complexes	382:429	two human type I IFN ternary signaling complexes containing IFNα2 and IFNω	382:455	The crystal structures of two human type I IFN ternary signaling complexes containing IFNα2 and IFNω reveal recognition modes and heterotrimeric architectures that are unique among the cytokine receptor superfamily but conserved between different type I IFNs.
21854986	3	36	theme	type	603:606	arg1	IFNs					610:613	different type I IFNs	593:613	different type I IFNs	593:613	The crystal structures of two human type I IFN ternary signaling complexes containing IFNα2 and IFNω reveal recognition modes and heterotrimeric architectures that are unique among the cytokine receptor superfamily but conserved between different type I IFNs.
21854986	4	37	theme	anchor	690:695	arg1	"					703:703	anchor points"	690:703	conserved receptor-ligand "anchor points" interspersed among ligand-specific interactions that "tune" the relative IFN-binding affinities, in an apparent extracellular "ligand proofreading" mechanism that modulates biological activity	663:896	Receptor-ligand cross-reactivity is enabled by conserved receptor-ligand "anchor points" interspersed among ligand-specific interactions that "tune" the relative IFN-binding affinities, in an apparent extracellular "ligand proofreading" mechanism that modulates biological activity.
21854986	4	38	theme	conserved	663:671	arg1	"					703:703	anchor points"	690:703	conserved receptor-ligand "anchor points" interspersed among ligand-specific interactions that "tune" the relative IFN-binding affinities, in an apparent extracellular "ligand proofreading" mechanism that modulates biological activity	663:896	Receptor-ligand cross-reactivity is enabled by conserved receptor-ligand "anchor points" interspersed among ligand-specific interactions that "tune" the relative IFN-binding affinities, in an apparent extracellular "ligand proofreading" mechanism that modulates biological activity.
21854986	3	39	theme	I	397:397	arg1	IFN					399:401	type I IFN	392:401	two human type I IFN ternary signaling complexes containing IFNα2 and IFNω	382:455	The crystal structures of two human type I IFN ternary signaling complexes containing IFNα2 and IFNω reveal recognition modes and heterotrimeric architectures that are unique among the cytokine receptor superfamily but conserved between different type I IFNs.
21854986	5	40	theme	downstream	1235:1244	arg1	patterns					1262:1269	downstream gene expression patterns	1235:1269	downstream gene expression patterns	1235:1269	Functional differences between IFNs are linked to their respective receptor recognition chemistries, in concert with a ligand-induced conformational change in IFNAR1, that collectively control signal initiation and complex stability, ultimately regulating differential STAT phosphorylation profiles, receptor internalization rates, and downstream gene expression patterns.
21854986	5	41	theme	differential	1155:1166	arg1	profiles					1189:1196	differential STAT phosphorylation profiles	1155:1196	differential STAT phosphorylation profiles	1155:1196	Functional differences between IFNs are linked to their respective receptor recognition chemistries, in concert with a ligand-induced conformational change in IFNAR1, that collectively control signal initiation and complex stability, ultimately regulating differential STAT phosphorylation profiles, receptor internalization rates, and downstream gene expression patterns.
21854986	2	42	theme	IFN	215:217	arg1	variants					219:226	Sixteen human type I IFN variants	194:226	Sixteen human type I IFN variants	194:226	Sixteen human type I IFN variants signal through the same cell-surface receptors, IFNAR1 and IFNAR2, yet they can evoke markedly different physiological effects.
21854986	4	43	theme	IFN-binding	778:788	arg1	affinities					790:799	the relative IFN-binding affinities	765:799	the relative IFN-binding affinities	765:799	Receptor-ligand cross-reactivity is enabled by conserved receptor-ligand "anchor points" interspersed among ligand-specific interactions that "tune" the relative IFN-binding affinities, in an apparent extracellular "ligand proofreading" mechanism that modulates biological activity.
21854986	5	44	theme	gene	1246:1249	arg1	patterns					1262:1269	downstream gene expression patterns	1235:1269	downstream gene expression patterns	1235:1269	Functional differences between IFNs are linked to their respective receptor recognition chemistries, in concert with a ligand-induced conformational change in IFNAR1, that collectively control signal initiation and complex stability, ultimately regulating differential STAT phosphorylation profiles, receptor internalization rates, and downstream gene expression patterns.
21854986	5	45	theme	complex	1114:1120	arg1	stability					1122:1130	complex stability	1114:1130	complex stability	1114:1130	Functional differences between IFNs are linked to their respective receptor recognition chemistries, in concert with a ligand-induced conformational change in IFNAR1, that collectively control signal initiation and complex stability, ultimately regulating differential STAT phosphorylation profiles, receptor internalization rates, and downstream gene expression patterns.
21854986	5	46	theme	signal	1092:1097	arg1	initiation					1099:1108	signal initiation	1092:1108	signal initiation	1092:1108	Functional differences between IFNs are linked to their respective receptor recognition chemistries, in concert with a ligand-induced conformational change in IFNAR1, that collectively control signal initiation and complex stability, ultimately regulating differential STAT phosphorylation profiles, receptor internalization rates, and downstream gene expression patterns.
21854986	5	47	from	rates	1224:1228	arg1	concert					1003:1009	concert	1003:1009	concert with a ligand-induced conformational change in IFNAR1	1003:1063	Functional differences between IFNs are linked to their respective receptor recognition chemistries, in concert with a ligand-induced conformational change in IFNAR1, that collectively control signal initiation and complex stability, ultimately regulating differential STAT phosphorylation profiles, receptor internalization rates, and downstream gene expression patterns.
21854986	5	48	theme	respective	955:964	arg1	chemistries					987:997	their respective receptor recognition chemistries	949:997	their respective receptor recognition chemistries	949:997	Functional differences between IFNs are linked to their respective receptor recognition chemistries, in concert with a ligand-induced conformational change in IFNAR1, that collectively control signal initiation and complex stability, ultimately regulating differential STAT phosphorylation profiles, receptor internalization rates, and downstream gene expression patterns.
21854986	0	49	theme	receptor	53:60	arg1	activation					62:71	receptor activation	53:71	receptor activation	53:71	Structural linkage between ligand discrimination and receptor activation by type I interferons.
21854986	5	50	theme	expression	1251:1260	arg1	patterns					1262:1269	downstream gene expression patterns	1235:1269	downstream gene expression patterns	1235:1269	Functional differences between IFNs are linked to their respective receptor recognition chemistries, in concert with a ligand-induced conformational change in IFNAR1, that collectively control signal initiation and complex stability, ultimately regulating differential STAT phosphorylation profiles, receptor internalization rates, and downstream gene expression patterns.
21854986	2	51	theme	human	202:206	arg1	variants					219:226	Sixteen human type I IFN variants	194:226	Sixteen human type I IFN variants	194:226	Sixteen human type I IFN variants signal through the same cell-surface receptors, IFNAR1 and IFNAR2, yet they can evoke markedly different physiological effects.
21854986	2	52	theme	type	208:211	arg1	IFN					215:217	type I IFN	208:217	Sixteen human type I IFN variants	194:226	Sixteen human type I IFN variants signal through the same cell-surface receptors, IFNAR1 and IFNAR2, yet they can evoke markedly different physiological effects.
21854986	5	53	theme	receptor	966:973	arg1	chemistries					987:997	their respective receptor recognition chemistries	949:997	their respective receptor recognition chemistries	949:997	Functional differences between IFNs are linked to their respective receptor recognition chemistries, in concert with a ligand-induced conformational change in IFNAR1, that collectively control signal initiation and complex stability, ultimately regulating differential STAT phosphorylation profiles, receptor internalization rates, and downstream gene expression patterns.
21854986	4	54	theme	extracellular	817:829	arg1	mechanism					853:861	an apparent extracellular "ligand proofreading" mechanism	805:861	an apparent extracellular "ligand proofreading" mechanism that modulates biological activity	805:896	Receptor-ligand cross-reactivity is enabled by conserved receptor-ligand "anchor points" interspersed among ligand-specific interactions that "tune" the relative IFN-binding affinities, in an apparent extracellular "ligand proofreading" mechanism that modulates biological activity.
21854986	2	55	theme	same	247:250	arg1	IFNAR2					287:292	IFNAR2	287:292	IFNAR2	287:292	Sixteen human type I IFN variants signal through the same cell-surface receptors, IFNAR1 and IFNAR2, yet they can evoke markedly different physiological effects.
21854986	2	55	theme	same	247:250	arg1	IFNAR1					276:281	IFNAR1	276:281	IFNAR1	276:281	Sixteen human type I IFN variants signal through the same cell-surface receptors, IFNAR1 and IFNAR2, yet they can evoke markedly different physiological effects.
21854986	2	55	theme	same	247:250	arg1	receptors					265:273	the same cell-surface receptors	243:273	the same cell-surface receptors	243:273	Sixteen human type I IFN variants signal through the same cell-surface receptors, IFNAR1 and IFNAR2, yet they can evoke markedly different physiological effects.
21854986	4	56	theme	proofreading	839:850	arg1	mechanism					853:861	an apparent extracellular "ligand proofreading" mechanism	805:861	an apparent extracellular "ligand proofreading" mechanism that modulates biological activity	805:896	Receptor-ligand cross-reactivity is enabled by conserved receptor-ligand "anchor points" interspersed among ligand-specific interactions that "tune" the relative IFN-binding affinities, in an apparent extracellular "ligand proofreading" mechanism that modulates biological activity.
21854986	5	57	theme	recognition	975:985	arg1	chemistries					987:997	their respective receptor recognition chemistries	949:997	their respective receptor recognition chemistries	949:997	Functional differences between IFNs are linked to their respective receptor recognition chemistries, in concert with a ligand-induced conformational change in IFNAR1, that collectively control signal initiation and complex stability, ultimately regulating differential STAT phosphorylation profiles, receptor internalization rates, and downstream gene expression patterns.
21854986	3	58	theme	receptor	550:557	arg1	superfamily					559:569	the cytokine receptor superfamily	537:569	the cytokine receptor superfamily	537:569	The crystal structures of two human type I IFN ternary signaling complexes containing IFNα2 and IFNω reveal recognition modes and heterotrimeric architectures that are unique among the cytokine receptor superfamily but conserved between different type I IFNs.
21854986	4	59	theme	apparent	808:815	arg1	mechanism					853:861	an apparent extracellular "ligand proofreading" mechanism	805:861	an apparent extracellular "ligand proofreading" mechanism that modulates biological activity	805:896	Receptor-ligand cross-reactivity is enabled by conserved receptor-ligand "anchor points" interspersed among ligand-specific interactions that "tune" the relative IFN-binding affinities, in an apparent extracellular "ligand proofreading" mechanism that modulates biological activity.
21854986	3	60	theme	recognition	464:474	arg1	modes					476:480	recognition modes	464:480	recognition modes	464:480	The crystal structures of two human type I IFN ternary signaling complexes containing IFNα2 and IFNω reveal recognition modes and heterotrimeric architectures that are unique among the cytokine receptor superfamily but conserved between different type I IFNs.
21854986	0	61	theme	type	76:79	arg1	interferons					83:93	type I interferons	76:93	type I interferons	76:93	Structural linkage between ligand discrimination and receptor activation by type I interferons.
21854986	4	62	theme	ligand	832:837	arg1	mechanism					853:861	an apparent extracellular "ligand proofreading" mechanism	805:861	an apparent extracellular "ligand proofreading" mechanism that modulates biological activity	805:896	Receptor-ligand cross-reactivity is enabled by conserved receptor-ligand "anchor points" interspersed among ligand-specific interactions that "tune" the relative IFN-binding affinities, in an apparent extracellular "ligand proofreading" mechanism that modulates biological activity.
21854986	1	63	theme	important	126:134	arg1	cytokines					136:144	important cytokines	126:144	important cytokines for innate immunity against viruses and cancer	126:191	Type I Interferons (IFNs) are important cytokines for innate immunity against viruses and cancer.
21854986	1	63	theme	important	126:134	arg1	Interferons					103:113	Type I Interferons	96:113	Type I Interferons (IFNs)	96:120	Type I Interferons (IFNs) are important cytokines for innate immunity against viruses and cancer.
21854986	4	64	theme	receptor-ligand	673:687	arg1	"					703:703	anchor points"	690:703	conserved receptor-ligand "anchor points" interspersed among ligand-specific interactions that "tune" the relative IFN-binding affinities, in an apparent extracellular "ligand proofreading" mechanism that modulates biological activity	663:896	Receptor-ligand cross-reactivity is enabled by conserved receptor-ligand "anchor points" interspersed among ligand-specific interactions that "tune" the relative IFN-binding affinities, in an apparent extracellular "ligand proofreading" mechanism that modulates biological activity.
21854986	5	65	theme	internalization	1208:1222	arg1	rates					1224:1228	receptor internalization rates	1199:1228	receptor internalization rates	1199:1228	Functional differences between IFNs are linked to their respective receptor recognition chemistries, in concert with a ligand-induced conformational change in IFNAR1, that collectively control signal initiation and complex stability, ultimately regulating differential STAT phosphorylation profiles, receptor internalization rates, and downstream gene expression patterns.
21854986	4	66	theme	Receptor-ligand	616:630	arg1	cross-reactivity					632:647	Receptor-ligand cross-reactivity	616:647	Receptor-ligand cross-reactivity	616:647	Receptor-ligand cross-reactivity is enabled by conserved receptor-ligand "anchor points" interspersed among ligand-specific interactions that "tune" the relative IFN-binding affinities, in an apparent extracellular "ligand proofreading" mechanism that modulates biological activity.
30337524	4	0	from	presence	574:581	arg1	structures					532:541	cryo-electron microscopy structures	507:541	cryo-electron microscopy structures of human STEAP4 in absence and presence of Fe3+-NTA	507:593	Here, we report cryo-electron microscopy structures of human STEAP4 in absence and presence of Fe3+-NTA.
30337524	5	1	theme	single	731:736	arg1	heme					745:748	a single b-type heme	729:748	a single b-type heme that cross the transmembrane-domain to enable electron transfer	729:812	Domain-swapped, trimeric STEAP4 orients NADPH bound to a cytosolic domain onto axially aligned flavin-adenine dinucleotide (FAD) and a single b-type heme that cross the transmembrane-domain to enable electron transfer.
30337524	7	2	theme	iron	965:968	arg1	reduction					970:978	iron reduction	965:978	iron reduction	965:978	These molecular principles of iron reduction provide a basis for exploring STEAPs as therapeutic targets.
30337524	1	3	theme	prostate	135:142	arg1	family					152:157	the prostate (STEAP) family	131:157	the prostate (STEAP) family	131:157	Enzymes of the six-transmembrane epithelial antigen of the prostate (STEAP) family reduce Fe3+ and Cu2+ ions to facilitate metal-ion uptake by mammalian cells.
30337524	4	4	theme	STEAP4	552:557	arg1	structures					532:541	cryo-electron microscopy structures	507:541	cryo-electron microscopy structures of human STEAP4 in absence and presence of Fe3+-NTA	507:593	Here, we report cryo-electron microscopy structures of human STEAP4 in absence and presence of Fe3+-NTA.
30337524	5	5	theme	b-type	738:743	arg1	heme					745:748	a single b-type heme	729:748	a single b-type heme that cross the transmembrane-domain to enable electron transfer	729:812	Domain-swapped, trimeric STEAP4 orients NADPH bound to a cytosolic domain onto axially aligned flavin-adenine dinucleotide (FAD) and a single b-type heme that cross the transmembrane-domain to enable electron transfer.
30337524	3	6	from	side	469:472	arg1	basis					361:365	the structural basis	346:365	the structural basis for STEAP-catalyzed electron transfer through an array of cofactors to metals at the membrane luminal side	346:472	However, the structural basis for STEAP-catalyzed electron transfer through an array of cofactors to metals at the membrane luminal side remains elusive.
30337524	2	7	theme	potential	306:314	arg1	targets					328:334	potential therapeutic targets	306:334	potential therapeutic targets	306:334	STEAPs are highly upregulated in several types of cancer, making them potential therapeutic targets.
30337524	1	8	theme	mammalian	219:227	arg1	cells					229:233	mammalian cells	219:233	mammalian cells	219:233	Enzymes of the six-transmembrane epithelial antigen of the prostate (STEAP) family reduce Fe3+ and Cu2+ ions to facilitate metal-ion uptake by mammalian cells.
30337524	4	9	from	absence	562:568	arg1	structures					532:541	cryo-electron microscopy structures	507:541	cryo-electron microscopy structures of human STEAP4 in absence and presence of Fe3+-NTA	507:593	Here, we report cryo-electron microscopy structures of human STEAP4 in absence and presence of Fe3+-NTA.
30337524	3	10	theme	structural	350:359	arg1	basis					361:365	the structural basis	346:365	the structural basis for STEAP-catalyzed electron transfer through an array of cofactors to metals at the membrane luminal side	346:472	However, the structural basis for STEAP-catalyzed electron transfer through an array of cofactors to metals at the membrane luminal side remains elusive.
30337524	0	11	theme	reduction	65:73	arg1	mechanism					42:50	mechanism	42:50	mechanism of iron(III) reduction	42:73	Cryo-EM structures of human STEAP4 reveal mechanism of iron(III) reduction.
30337524	2	12	theme	therapeutic	316:326	arg1	targets					328:334	potential therapeutic targets	306:334	potential therapeutic targets	306:334	STEAPs are highly upregulated in several types of cancer, making them potential therapeutic targets.
30337524	2	13	theme	cancer	286:291	arg1	types					277:281	several types	269:281	several types of cancer	269:291	STEAPs are highly upregulated in several types of cancer, making them potential therapeutic targets.
30337524	4	14	from	STEAP4	552:557	arg1	presence					574:581	presence	574:581	presence	574:581	Here, we report cryo-electron microscopy structures of human STEAP4 in absence and presence of Fe3+-NTA.
30337524	4	14	from	STEAP4	552:557	arg1	absence					562:568	absence	562:568	absence	562:568	Here, we report cryo-electron microscopy structures of human STEAP4 in absence and presence of Fe3+-NTA.
30337524	1	15	theme	STEAP	145:149	arg1	family					152:157	the prostate (STEAP) family	131:157	the prostate (STEAP) family	131:157	Enzymes of the six-transmembrane epithelial antigen of the prostate (STEAP) family reduce Fe3+ and Cu2+ ions to facilitate metal-ion uptake by mammalian cells.
30337524	5	16	dep	Domain-swapped	596:609	arg1	trimeric					612:619	trimeric	612:619	trimeric	612:619	Domain-swapped, trimeric STEAP4 orients NADPH bound to a cytosolic domain onto axially aligned flavin-adenine dinucleotide (FAD) and a single b-type heme that cross the transmembrane-domain to enable electron transfer.
30337524	5	17	theme	Domain-swapped	596:609	arg1	STEAP4					621:626	Domain-swapped, trimeric STEAP4	596:626	Domain-swapped, trimeric STEAP4	596:626	Domain-swapped, trimeric STEAP4 orients NADPH bound to a cytosolic domain onto axially aligned flavin-adenine dinucleotide (FAD) and a single b-type heme that cross the transmembrane-domain to enable electron transfer.
30337524	0	18	dep	reduction	65:73	arg1	III					60:62	III	60:62	III	60:62	Cryo-EM structures of human STEAP4 reveal mechanism of iron(III) reduction.
30337524	1	19	theme	family	152:157	arg1	antigen					120:126	the six-transmembrane epithelial antigen	87:126	the six-transmembrane epithelial antigen of the prostate (STEAP) family	87:157	Enzymes of the six-transmembrane epithelial antigen of the prostate (STEAP) family reduce Fe3+ and Cu2+ ions to facilitate metal-ion uptake by mammalian cells.
30337524	0	20	theme	Cryo-EM	0:6	arg1	structures					8:17	Cryo-EM structures	0:17	Cryo-EM structures of human STEAP4	0:33	Cryo-EM structures of human STEAP4 reveal mechanism of iron(III) reduction.
30337524	4	21	theme	microscopy	521:530	arg1	structures					532:541	cryo-electron microscopy structures	507:541	cryo-electron microscopy structures of human STEAP4 in absence and presence of Fe3+-NTA	507:593	Here, we report cryo-electron microscopy structures of human STEAP4 in absence and presence of Fe3+-NTA.
30337524	6	22	with	complex	908:914	arg1	chelator					925:932	its chelator	921:932	its chelator	921:932	Substrate binding within a positively charged ring indicates that iron gets reduced while in complex with its chelator.
30337524	0	23	theme	human	22:26	arg1	STEAP4					28:33	human STEAP4	22:33	human STEAP4	22:33	Cryo-EM structures of human STEAP4 reveal mechanism of iron(III) reduction.
30337524	4	24	theme	cryo-electron	507:519	arg1	microscopy					521:530	cryo-electron microscopy	507:530	cryo-electron microscopy structures of human STEAP4 in absence and presence of Fe3+-NTA	507:593	Here, we report cryo-electron microscopy structures of human STEAP4 in absence and presence of Fe3+-NTA.
30337524	2	25	theme	several	269:275	arg1	types					277:281	several types	269:281	several types of cancer	269:291	STEAPs are highly upregulated in several types of cancer, making them potential therapeutic targets.
30337524	7	26	theme	molecular	941:949	arg1	principles					951:960	These molecular principles	935:960	These molecular principles of iron reduction	935:978	These molecular principles of iron reduction provide a basis for exploring STEAPs as therapeutic targets.
30337524	5	27	theme	electron	796:803	arg1	transfer					805:812	electron transfer	796:812	electron transfer	796:812	Domain-swapped, trimeric STEAP4 orients NADPH bound to a cytosolic domain onto axially aligned flavin-adenine dinucleotide (FAD) and a single b-type heme that cross the transmembrane-domain to enable electron transfer.
30337524	6	28	theme	charged	853:859	arg1	ring					861:864	a positively charged ring	840:864	a positively charged ring	840:864	Substrate binding within a positively charged ring indicates that iron gets reduced while in complex with its chelator.
30337524	4	29	theme	human	546:550	arg1	STEAP4					552:557	human STEAP4	546:557	human STEAP4 in absence and presence of Fe3+-NTA	546:593	Here, we report cryo-electron microscopy structures of human STEAP4 in absence and presence of Fe3+-NTA.
30337524	3	30	theme	STEAP-catalyzed	371:385	arg1	transfer					396:403	STEAP-catalyzed electron transfer	371:403	STEAP-catalyzed electron transfer through an array of cofactors to metals	371:443	However, the structural basis for STEAP-catalyzed electron transfer through an array of cofactors to metals at the membrane luminal side remains elusive.
30337524	3	31	theme	luminal	461:467	arg1	side					469:472	the membrane luminal side	448:472	the membrane luminal side	448:472	However, the structural basis for STEAP-catalyzed electron transfer through an array of cofactors to metals at the membrane luminal side remains elusive.
30337524	5	32	theme	aligned	683:689	arg1	FAD					720:722	FAD	720:722	FAD	720:722	Domain-swapped, trimeric STEAP4 orients NADPH bound to a cytosolic domain onto axially aligned flavin-adenine dinucleotide (FAD) and a single b-type heme that cross the transmembrane-domain to enable electron transfer.
30337524	5	32	theme	aligned	683:689	arg1	dinucleotide					706:717	axially aligned flavin-adenine dinucleotide	675:717	axially aligned flavin-adenine dinucleotide (FAD)	675:723	Domain-swapped, trimeric STEAP4 orients NADPH bound to a cytosolic domain onto axially aligned flavin-adenine dinucleotide (FAD) and a single b-type heme that cross the transmembrane-domain to enable electron transfer.
30337524	1	33	theme	Cu2+	175:178	arg1	ions					180:183	Cu2+ ions	175:183	Cu2+ ions	175:183	Enzymes of the six-transmembrane epithelial antigen of the prostate (STEAP) family reduce Fe3+ and Cu2+ ions to facilitate metal-ion uptake by mammalian cells.
30337524	0	34	theme	STEAP4	28:33	arg1	structures					8:17	Cryo-EM structures	0:17	Cryo-EM structures of human STEAP4	0:33	Cryo-EM structures of human STEAP4 reveal mechanism of iron(III) reduction.
30337524	3	35	theme	electron	387:394	arg1	transfer					396:403	STEAP-catalyzed electron transfer	371:403	STEAP-catalyzed electron transfer through an array of cofactors to metals	371:443	However, the structural basis for STEAP-catalyzed electron transfer through an array of cofactors to metals at the membrane luminal side remains elusive.
30337524	4	36	theme	Fe3+-NTA	586:593	arg1	presence					574:581	presence	574:581	presence	574:581	Here, we report cryo-electron microscopy structures of human STEAP4 in absence and presence of Fe3+-NTA.
30337524	4	36	theme	Fe3+-NTA	586:593	arg1	absence					562:568	absence	562:568	absence	562:568	Here, we report cryo-electron microscopy structures of human STEAP4 in absence and presence of Fe3+-NTA.
30337524	3	37	theme	cofactors	425:433	arg1	array					416:420	an array	413:420	an array of cofactors	413:433	However, the structural basis for STEAP-catalyzed electron transfer through an array of cofactors to metals at the membrane luminal side remains elusive.
30337524	7	38	theme	therapeutic	1020:1030	arg1	STEAPs					1010:1015	STEAPs	1010:1015	STEAPs	1010:1015	These molecular principles of iron reduction provide a basis for exploring STEAPs as therapeutic targets.
30337524	7	38	theme	therapeutic	1020:1030	arg1	targets					1032:1038	therapeutic targets	1020:1038	therapeutic targets	1020:1038	These molecular principles of iron reduction provide a basis for exploring STEAPs as therapeutic targets.
30337524	3	39	theme	membrane	452:459	arg1	side					469:472	the membrane luminal side	448:472	the membrane luminal side	448:472	However, the structural basis for STEAP-catalyzed electron transfer through an array of cofactors to metals at the membrane luminal side remains elusive.
30337524	5	40	theme	flavin-adenine	691:704	arg1	FAD					720:722	FAD	720:722	FAD	720:722	Domain-swapped, trimeric STEAP4 orients NADPH bound to a cytosolic domain onto axially aligned flavin-adenine dinucleotide (FAD) and a single b-type heme that cross the transmembrane-domain to enable electron transfer.
30337524	5	40	theme	flavin-adenine	691:704	arg1	dinucleotide					706:717	axially aligned flavin-adenine dinucleotide	675:717	axially aligned flavin-adenine dinucleotide (FAD)	675:723	Domain-swapped, trimeric STEAP4 orients NADPH bound to a cytosolic domain onto axially aligned flavin-adenine dinucleotide (FAD) and a single b-type heme that cross the transmembrane-domain to enable electron transfer.
30337524	1	41	theme	six-transmembrane	91:107	arg1	antigen					120:126	the six-transmembrane epithelial antigen	87:126	the six-transmembrane epithelial antigen of the prostate (STEAP) family	87:157	Enzymes of the six-transmembrane epithelial antigen of the prostate (STEAP) family reduce Fe3+ and Cu2+ ions to facilitate metal-ion uptake by mammalian cells.
30337524	5	42	theme	cytosolic	653:661	arg1	domain					663:668	a cytosolic domain	651:668	a cytosolic domain onto axially aligned flavin-adenine dinucleotide (FAD) and a single b-type heme that cross the transmembrane-domain to enable electron transfer	651:812	Domain-swapped, trimeric STEAP4 orients NADPH bound to a cytosolic domain onto axially aligned flavin-adenine dinucleotide (FAD) and a single b-type heme that cross the transmembrane-domain to enable electron transfer.
30337524	6	43	theme	Substrate	815:823	arg1	binding					825:831	Substrate binding	815:831	Substrate binding within a positively charged ring	815:864	Substrate binding within a positively charged ring indicates that iron gets reduced while in complex with its chelator.
30337524	1	44	theme	epithelial	109:118	arg1	antigen					120:126	the six-transmembrane epithelial antigen	87:126	the six-transmembrane epithelial antigen of the prostate (STEAP) family	87:157	Enzymes of the six-transmembrane epithelial antigen of the prostate (STEAP) family reduce Fe3+ and Cu2+ ions to facilitate metal-ion uptake by mammalian cells.
30337524	4	45	from	structures	532:541	arg1	presence					574:581	presence	574:581	presence	574:581	Here, we report cryo-electron microscopy structures of human STEAP4 in absence and presence of Fe3+-NTA.
30337524	4	45	from	structures	532:541	arg1	absence					562:568	absence	562:568	absence	562:568	Here, we report cryo-electron microscopy structures of human STEAP4 in absence and presence of Fe3+-NTA.
30337524	7	46	theme	reduction	970:978	arg1	principles					951:960	These molecular principles	935:960	These molecular principles of iron reduction	935:978	These molecular principles of iron reduction provide a basis for exploring STEAPs as therapeutic targets.
30337524	1	47	theme	antigen	120:126	arg1	Enzymes					76:82	Enzymes	76:82	Enzymes of the six-transmembrane epithelial antigen of the prostate (STEAP) family	76:157	Enzymes of the six-transmembrane epithelial antigen of the prostate (STEAP) family reduce Fe3+ and Cu2+ ions to facilitate metal-ion uptake by mammalian cells.
30337524	1	48	theme	metal-ion	199:207	arg1	uptake					209:214	metal-ion uptake	199:214	metal-ion uptake	199:214	Enzymes of the six-transmembrane epithelial antigen of the prostate (STEAP) family reduce Fe3+ and Cu2+ ions to facilitate metal-ion uptake by mammalian cells.
30337524	0	49	theme	iron	55:58	arg1	reduction					65:73	iron(III) reduction	55:73	iron(III) reduction	55:73	Cryo-EM structures of human STEAP4 reveal mechanism of iron(III) reduction.
16477002	4	0	theme	rapid	805:809	arg1	rate					823:826	the rapid association rate	801:826	the rapid association rate	801:826	The IL-2R alpha subunit forms the largest of the three IL-2/IL-2R interfaces, which, together with the high abundance of charge-charge interactions, correlates well with the rapid association rate and high-affinity interaction of IL-2R alpha with IL-2 at the cell surface.
16477002	9	1	theme	smallest	1695:1702	arg1	surface					1711:1717	the smallest buried surface	1691:1717	the smallest buried surface	1691:1717	The IL-2/gamma(c) interface itself exhibits the smallest buried surface and the fewest hydrogen bonds in the complex, which is consistent with its promiscuous use in other cytokine receptor complexes.
16477002	1	2	theme	ligand-induced	227:240	arg1	hetero-trimerization					242:261	ligand-induced hetero-trimerization	227:261	ligand-induced hetero-trimerization of the receptor subunits IL-2R alpha, IL-2R beta, and gamma(c)	227:324	IL-2 is a cytokine that functions as a growth factor and central regulator in the immune system and mediates its effects through ligand-induced hetero-trimerization of the receptor subunits IL-2R alpha, IL-2R beta, and gamma(c).
16477002	7	3	theme	signaling	1378:1386	arg1	complex					1388:1394	the fully assembled IL-2 signaling complex	1353:1394	the fully assembled IL-2 signaling complex	1353:1394	Cooperativity in assembly of the final quaternary complex is easily explained by the extraordinarily extensive set of interfaces found within the fully assembled IL-2 signaling complex, which nearly span the entire length of the IL-2R beta and gamma(c) subunits.
16477002	7	4	theme	complex	1261:1267	arg1	assembly					1228:1235	assembly	1228:1235	assembly of the final quaternary complex	1228:1267	Cooperativity in assembly of the final quaternary complex is easily explained by the extraordinarily extensive set of interfaces found within the fully assembled IL-2 signaling complex, which nearly span the entire length of the IL-2R beta and gamma(c) subunits.
16477002	7	5	theme	interfaces	1329:1338	arg1	interfaces					1329:1338	interfaces	1329:1338	interfaces found within the fully assembled IL-2 signaling complex, which nearly span the entire length of the IL-2R beta and gamma(c) subunits	1329:1471	Cooperativity in assembly of the final quaternary complex is easily explained by the extraordinarily extensive set of interfaces found within the fully assembled IL-2 signaling complex, which nearly span the entire length of the IL-2R beta and gamma(c) subunits.
16477002	7	5	theme	interfaces	1329:1338	arg1	set					1322:1324	the extraordinarily extensive set	1292:1324	the extraordinarily extensive set of interfaces found within the fully assembled IL-2 signaling complex, which nearly span the entire length of the IL-2R beta and gamma(c) subunits	1292:1471	Cooperativity in assembly of the final quaternary complex is easily explained by the extraordinarily extensive set of interfaces found within the fully assembled IL-2 signaling complex, which nearly span the entire length of the IL-2R beta and gamma(c) subunits.
16477002	7	6	theme	assembled	1363:1371	arg1	complex					1388:1394	the fully assembled IL-2 signaling complex	1353:1394	the fully assembled IL-2 signaling complex	1353:1394	Cooperativity in assembly of the final quaternary complex is easily explained by the extraordinarily extensive set of interfaces found within the fully assembled IL-2 signaling complex, which nearly span the entire length of the IL-2R beta and gamma(c) subunits.
16477002	0	7	theme	Crystal	0:6	arg1	structure					8:16	Crystal structure	0:16	Crystal structure of the IL-2 signaling complex: paradigm for a heterotrimeric cytokine receptor.	0:96	Crystal structure of the IL-2 signaling complex: paradigm for a heterotrimeric cytokine receptor.
16477002	9	8	theme	hydrogen	1734:1741	arg1	bonds					1743:1747	the fewest hydrogen bonds	1723:1747	the fewest hydrogen bonds in the complex, which is consistent with its promiscuous use in other cytokine receptor complexes	1723:1845	The IL-2/gamma(c) interface itself exhibits the smallest buried surface and the fewest hydrogen bonds in the complex, which is consistent with its promiscuous use in other cytokine receptor complexes.
16477002	4	9	theme	alpha	867:871	arg1	interaction					846:856	high-affinity interaction	832:856	high-affinity interaction of IL-2R alpha with IL-2 at the cell surface	832:901	The IL-2R alpha subunit forms the largest of the three IL-2/IL-2R interfaces, which, together with the high abundance of charge-charge interactions, correlates well with the rapid association rate and high-affinity interaction of IL-2R alpha with IL-2 at the cell surface.
16477002	4	9	theme	alpha	867:871	arg1	rate					823:826	the rapid association rate	801:826	the rapid association rate	801:826	The IL-2R alpha subunit forms the largest of the three IL-2/IL-2R interfaces, which, together with the high abundance of charge-charge interactions, correlates well with the rapid association rate and high-affinity interaction of IL-2R alpha with IL-2 at the cell surface.
16477002	3	10	theme	IL-2/IL-2R	542:551	arg1	alpha					553:557	IL-2/IL-2R alpha	542:557	IL-2/IL-2R alpha	542:557	The quaternary structure is consistent with a stepwise assembly from IL-2/IL-2R alpha to IL-2/IL-2R alpha/IL-2R beta to IL-2/IL-2R alpha/IL-2R beta/gamma(c).
16477002	8	11	theme	binding	1598:1604	arg1	site					1606:1609	a composite binding site	1586:1609	a composite binding site for the final gamma(c) recruitment	1586:1644	Helix A of IL-2 wedges tightly between IL-2R beta and gamma(c) to form a three-way junction that coalesces into a composite binding site for the final gamma(c) recruitment.
16477002	4	12	theme	high-affinity	832:844	arg1	interaction					846:856	high-affinity interaction	832:856	high-affinity interaction of IL-2R alpha with IL-2 at the cell surface	832:901	The IL-2R alpha subunit forms the largest of the three IL-2/IL-2R interfaces, which, together with the high abundance of charge-charge interactions, correlates well with the rapid association rate and high-affinity interaction of IL-2R alpha with IL-2 at the cell surface.
16477002	6	13	theme	alpha	1119:1123	arg1	role					1105:1108	the principal role	1091:1108	the principal role of IL-2R alpha to deliver IL-2 to the signaling complex and act as regulator of signal transduction	1091:1208	These findings support the principal role of IL-2R alpha to deliver IL-2 to the signaling complex and act as regulator of signal transduction.
16477002	6	14	theme	signal	1190:1195	arg1	transduction					1197:1208	signal transduction	1190:1208	signal transduction	1190:1208	These findings support the principal role of IL-2R alpha to deliver IL-2 to the signaling complex and act as regulator of signal transduction.
16477002	4	15	with	rate	823:826	arg1	IL-2					878:881	IL-2	878:881	IL-2 at the cell surface	878:901	The IL-2R alpha subunit forms the largest of the three IL-2/IL-2R interfaces, which, together with the high abundance of charge-charge interactions, correlates well with the rapid association rate and high-affinity interaction of IL-2R alpha with IL-2 at the cell surface.
16477002	7	16	theme	final	1244:1248	arg1	complex					1261:1267	the final quaternary complex	1240:1267	the final quaternary complex	1240:1267	Cooperativity in assembly of the final quaternary complex is easily explained by the extraordinarily extensive set of interfaces found within the fully assembled IL-2 signaling complex, which nearly span the entire length of the IL-2R beta and gamma(c) subunits.
16477002	3	17	theme	alpha/IL-2R	573:583	arg1	beta					585:588	IL-2/IL-2R alpha/IL-2R beta	562:588	IL-2/IL-2R alpha/IL-2R beta to IL-2/IL-2R alpha/IL-2R beta/gamma(c)	562:628	The quaternary structure is consistent with a stepwise assembly from IL-2/IL-2R alpha to IL-2/IL-2R alpha/IL-2R beta to IL-2/IL-2R alpha/IL-2R beta/gamma(c).
16477002	8	18	theme	final	1619:1623	arg1	recruitment					1634:1644	the final gamma(c) recruitment	1615:1644	the final gamma(c) recruitment	1615:1644	Helix A of IL-2 wedges tightly between IL-2R beta and gamma(c) to form a three-way junction that coalesces into a composite binding site for the final gamma(c) recruitment.
16477002	7	19	theme	subunits	1464:1471	arg1	length					1426:1431	the entire length	1415:1431	the entire length of the IL-2R beta and gamma(c) subunits	1415:1471	Cooperativity in assembly of the final quaternary complex is easily explained by the extraordinarily extensive set of interfaces found within the fully assembled IL-2 signaling complex, which nearly span the entire length of the IL-2R beta and gamma(c) subunits.
16477002	6	20	theme	principal	1095:1103	arg1	role					1105:1108	the principal role	1091:1108	the principal role of IL-2R alpha to deliver IL-2 to the signaling complex and act as regulator of signal transduction	1091:1208	These findings support the principal role of IL-2R alpha to deliver IL-2 to the signaling complex and act as regulator of signal transduction.
16477002	4	21	theme	alpha	641:645	arg1	subunit					647:653	The IL-2R alpha subunit	631:653	The IL-2R alpha subunit	631:653	The IL-2R alpha subunit forms the largest of the three IL-2/IL-2R interfaces, which, together with the high abundance of charge-charge interactions, correlates well with the rapid association rate and high-affinity interaction of IL-2R alpha with IL-2 at the cell surface.
16477002	2	22	with	complex	434:440	arg1	IL-2					447:450	IL-2	447:450	IL-2	447:450	Here, we describe the crystal structure of the trimeric assembly of the human IL-2 receptor ectodomains in complex with IL-2 at 3.0 A resolution.
16477002	1	23	theme	growth	137:142	arg1	cytokine					108:115	a cytokine	106:115	a cytokine that functions as a growth factor and central regulator in the immune system and mediates its effects through ligand-induced hetero-trimerization of the receptor subunits IL-2R alpha, IL-2R beta, and gamma(c)	106:324	IL-2 is a cytokine that functions as a growth factor and central regulator in the immune system and mediates its effects through ligand-induced hetero-trimerization of the receptor subunits IL-2R alpha, IL-2R beta, and gamma(c).
16477002	1	23	theme	growth	137:142	arg1	factor					144:149	a growth factor	135:149	a growth factor	135:149	IL-2 is a cytokine that functions as a growth factor and central regulator in the immune system and mediates its effects through ligand-induced hetero-trimerization of the receptor subunits IL-2R alpha, IL-2R beta, and gamma(c).
16477002	1	23	theme	growth	137:142	arg1	effects					211:217	its effects	207:217	its effects	207:217	IL-2 is a cytokine that functions as a growth factor and central regulator in the immune system and mediates its effects through ligand-induced hetero-trimerization of the receptor subunits IL-2R alpha, IL-2R beta, and gamma(c).
16477002	7	24	theme	gamma	1455:1459	arg1	subunits					1464:1471	the IL-2R beta and gamma(c) subunits	1436:1471	the IL-2R beta and gamma(c) subunits	1436:1471	Cooperativity in assembly of the final quaternary complex is easily explained by the extraordinarily extensive set of interfaces found within the fully assembled IL-2 signaling complex, which nearly span the entire length of the IL-2R beta and gamma(c) subunits.
16477002	9	25	theme	other	1813:1817	arg1	complexes					1837:1845	other cytokine receptor complexes	1813:1845	other cytokine receptor complexes	1813:1845	The IL-2/gamma(c) interface itself exhibits the smallest buried surface and the fewest hydrogen bonds in the complex, which is consistent with its promiscuous use in other cytokine receptor complexes.
16477002	0	26	theme	cytokine	79:86	arg1	receptor					88:95	a heterotrimeric cytokine receptor	62:95	a heterotrimeric cytokine receptor	62:95	Crystal structure of the IL-2 signaling complex: paradigm for a heterotrimeric cytokine receptor.
16477002	7	27	theme	beta	1446:1449	arg1	subunits					1464:1471	the IL-2R beta and gamma(c) subunits	1436:1471	the IL-2R beta and gamma(c) subunits	1436:1471	Cooperativity in assembly of the final quaternary complex is easily explained by the extraordinarily extensive set of interfaces found within the fully assembled IL-2 signaling complex, which nearly span the entire length of the IL-2R beta and gamma(c) subunits.
16477002	9	28	theme	receptor	1828:1835	arg1	complexes					1837:1845	other cytokine receptor complexes	1813:1845	other cytokine receptor complexes	1813:1845	The IL-2/gamma(c) interface itself exhibits the smallest buried surface and the fewest hydrogen bonds in the complex, which is consistent with its promiscuous use in other cytokine receptor complexes.
16477002	5	29	from	structure	1025:1033	arg1	response					1038:1045	response	1038:1045	response to receptor binding	1038:1065	Surprisingly, IL-2R alpha makes no contacts with IL-2R beta or gamma(c), and only minor changes are observed in the IL-2 structure in response to receptor binding.
16477002	5	30	theme	IL-2R	918:922	arg1	alpha					924:928	IL-2R alpha	918:928	IL-2R alpha	918:928	Surprisingly, IL-2R alpha makes no contacts with IL-2R beta or gamma(c), and only minor changes are observed in the IL-2 structure in response to receptor binding.
16477002	9	31	from	use	1806:1808	arg1	complexes					1837:1845	other cytokine receptor complexes	1813:1845	other cytokine receptor complexes	1813:1845	The IL-2/gamma(c) interface itself exhibits the smallest buried surface and the fewest hydrogen bonds in the complex, which is consistent with its promiscuous use in other cytokine receptor complexes.
16477002	3	32	with	consistent	501:510	arg1	assembly					528:535	a stepwise assembly	517:535	a stepwise assembly from IL-2/IL-2R alpha to IL-2/IL-2R alpha/IL-2R beta to IL-2/IL-2R alpha/IL-2R beta/gamma(c)	517:628	The quaternary structure is consistent with a stepwise assembly from IL-2/IL-2R alpha to IL-2/IL-2R alpha/IL-2R beta to IL-2/IL-2R alpha/IL-2R beta/gamma(c).
16477002	2	33	theme	assembly	383:390	arg1	structure					357:365	the crystal structure	345:365	the crystal structure of the trimeric assembly of the human IL-2 receptor ectodomains in complex with IL-2 at 3.0 A resolution	345:470	Here, we describe the crystal structure of the trimeric assembly of the human IL-2 receptor ectodomains in complex with IL-2 at 3.0 A resolution.
16477002	4	34	theme	IL-2/IL-2R	686:695	arg1	interfaces					697:706	the three IL-2/IL-2R interfaces	676:706	the three IL-2/IL-2R interfaces	676:706	The IL-2R alpha subunit forms the largest of the three IL-2/IL-2R interfaces, which, together with the high abundance of charge-charge interactions, correlates well with the rapid association rate and high-affinity interaction of IL-2R alpha with IL-2 at the cell surface.
16477002	1	35	theme	subunits	279:286	arg1	hetero-trimerization					242:261	ligand-induced hetero-trimerization	227:261	ligand-induced hetero-trimerization of the receptor subunits IL-2R alpha, IL-2R beta, and gamma(c)	227:324	IL-2 is a cytokine that functions as a growth factor and central regulator in the immune system and mediates its effects through ligand-induced hetero-trimerization of the receptor subunits IL-2R alpha, IL-2R beta, and gamma(c).
16477002	2	36	theme	ectodomains	419:429	arg1	assembly					383:390	the trimeric assembly	370:390	the trimeric assembly of the human IL-2 receptor ectodomains in complex with IL-2 at 3.0 A resolution	370:470	Here, we describe the crystal structure of the trimeric assembly of the human IL-2 receptor ectodomains in complex with IL-2 at 3.0 A resolution.
16477002	3	37	theme	alpha/IL-2R	604:614	arg1	c					627:627	c	627:627	c	627:627	The quaternary structure is consistent with a stepwise assembly from IL-2/IL-2R alpha to IL-2/IL-2R alpha/IL-2R beta to IL-2/IL-2R alpha/IL-2R beta/gamma(c).
16477002	3	37	theme	alpha/IL-2R	604:614	arg1	beta/gamma					616:625	IL-2/IL-2R alpha/IL-2R beta/gamma	593:625	IL-2/IL-2R alpha/IL-2R beta/gamma(c)	593:628	The quaternary structure is consistent with a stepwise assembly from IL-2/IL-2R alpha to IL-2/IL-2R alpha/IL-2R beta to IL-2/IL-2R alpha/IL-2R beta/gamma(c).
16477002	0	38	theme	IL-2	25:28	arg1	complex					40:46	the IL-2 signaling complex	21:46	the IL-2 signaling complex	21:46	Crystal structure of the IL-2 signaling complex: paradigm for a heterotrimeric cytokine receptor.
16477002	7	39	located	found	1340:1344	arg2	interfaces					1329:1338	interfaces	1329:1338	interfaces found within the fully assembled IL-2 signaling complex, which nearly span the entire length of the IL-2R beta and gamma(c) subunits	1329:1471	Cooperativity in assembly of the final quaternary complex is easily explained by the extraordinarily extensive set of interfaces found within the fully assembled IL-2 signaling complex, which nearly span the entire length of the IL-2R beta and gamma(c) subunits.
16477002	7	39	located	found	1340:1344	arg1	complex					1388:1394	the fully assembled IL-2 signaling complex	1353:1394	the fully assembled IL-2 signaling complex	1353:1394	Cooperativity in assembly of the final quaternary complex is easily explained by the extraordinarily extensive set of interfaces found within the fully assembled IL-2 signaling complex, which nearly span the entire length of the IL-2R beta and gamma(c) subunits.
16477002	9	40	theme	IL-2/gamma	1651:1660	arg1	interface					1665:1673	The IL-2/gamma(c) interface itself	1647:1680	The IL-2/gamma(c) interface itself	1647:1680	The IL-2/gamma(c) interface itself exhibits the smallest buried surface and the fewest hydrogen bonds in the complex, which is consistent with its promiscuous use in other cytokine receptor complexes.
16477002	7	41	theme	entire	1419:1424	arg1	length					1426:1431	the entire length	1415:1431	the entire length of the IL-2R beta and gamma(c) subunits	1415:1471	Cooperativity in assembly of the final quaternary complex is easily explained by the extraordinarily extensive set of interfaces found within the fully assembled IL-2 signaling complex, which nearly span the entire length of the IL-2R beta and gamma(c) subunits.
16477002	5	42	theme	IL-2R	953:957	arg1	beta					959:962	IL-2R beta	953:962	IL-2R beta	953:962	Surprisingly, IL-2R alpha makes no contacts with IL-2R beta or gamma(c), and only minor changes are observed in the IL-2 structure in response to receptor binding.
16477002	2	43	theme	IL-2	405:408	arg1	ectodomains					419:429	the human IL-2 receptor ectodomains	395:429	the human IL-2 receptor ectodomains in complex with IL-2 at 3.0 A resolution	395:470	Here, we describe the crystal structure of the trimeric assembly of the human IL-2 receptor ectodomains in complex with IL-2 at 3.0 A resolution.
16477002	4	44	theme	interactions	766:777	arg1	abundance					739:747	the high abundance	730:747	the high abundance of charge-charge interactions	730:777	The IL-2R alpha subunit forms the largest of the three IL-2/IL-2R interfaces, which, together with the high abundance of charge-charge interactions, correlates well with the rapid association rate and high-affinity interaction of IL-2R alpha with IL-2 at the cell surface.
16477002	0	45	theme	complex	40:46	arg1	structure					8:16	Crystal structure	0:16	Crystal structure of the IL-2 signaling complex: paradigm for a heterotrimeric cytokine receptor.	0:96	Crystal structure of the IL-2 signaling complex: paradigm for a heterotrimeric cytokine receptor.
16477002	5	46	theme	receptor	1050:1057	arg1	binding					1059:1065	receptor binding	1050:1065	receptor binding	1050:1065	Surprisingly, IL-2R alpha makes no contacts with IL-2R beta or gamma(c), and only minor changes are observed in the IL-2 structure in response to receptor binding.
16477002	1	47	dep	subunits	279:286	arg1	gamma					317:321	gamma	317:321	gamma(c)	317:324	IL-2 is a cytokine that functions as a growth factor and central regulator in the immune system and mediates its effects through ligand-induced hetero-trimerization of the receptor subunits IL-2R alpha, IL-2R beta, and gamma(c).
16477002	1	47	dep	subunits	279:286	arg1	subunits					279:286	the receptor subunits IL-2R alpha, IL-2R beta, and gamma(c)	266:324	the receptor subunits IL-2R alpha, IL-2R beta, and gamma(c)	266:324	IL-2 is a cytokine that functions as a growth factor and central regulator in the immune system and mediates its effects through ligand-induced hetero-trimerization of the receptor subunits IL-2R alpha, IL-2R beta, and gamma(c).
16477002	1	47	dep	subunits	279:286	arg1	c					323:323	c	323:323	c	323:323	IL-2 is a cytokine that functions as a growth factor and central regulator in the immune system and mediates its effects through ligand-induced hetero-trimerization of the receptor subunits IL-2R alpha, IL-2R beta, and gamma(c).
16477002	1	47	dep	subunits	279:286	arg1	alpha					294:298	IL-2R alpha	288:298	IL-2R alpha	288:298	IL-2 is a cytokine that functions as a growth factor and central regulator in the immune system and mediates its effects through ligand-induced hetero-trimerization of the receptor subunits IL-2R alpha, IL-2R beta, and gamma(c).
16477002	1	47	dep	subunits	279:286	arg1	beta					307:310	IL-2R beta	301:310	IL-2R beta	301:310	IL-2 is a cytokine that functions as a growth factor and central regulator in the immune system and mediates its effects through ligand-induced hetero-trimerization of the receptor subunits IL-2R alpha, IL-2R beta, and gamma(c).
16477002	8	48	theme	IL-2R	1513:1517	arg1	beta					1519:1522	IL-2R beta	1513:1522	IL-2R beta	1513:1522	Helix A of IL-2 wedges tightly between IL-2R beta and gamma(c) to form a three-way junction that coalesces into a composite binding site for the final gamma(c) recruitment.
16477002	4	49	theme	high	734:737	arg1	abundance					739:747	the high abundance	730:747	the high abundance of charge-charge interactions	730:777	The IL-2R alpha subunit forms the largest of the three IL-2/IL-2R interfaces, which, together with the high abundance of charge-charge interactions, correlates well with the rapid association rate and high-affinity interaction of IL-2R alpha with IL-2 at the cell surface.
16477002	4	50	from	surface	895:901	arg1	IL-2					878:881	IL-2	878:881	IL-2 at the cell surface	878:901	The IL-2R alpha subunit forms the largest of the three IL-2/IL-2R interfaces, which, together with the high abundance of charge-charge interactions, correlates well with the rapid association rate and high-affinity interaction of IL-2R alpha with IL-2 at the cell surface.
16477002	7	51	theme	IL-2	1373:1376	arg1	complex					1388:1394	the fully assembled IL-2 signaling complex	1353:1394	the fully assembled IL-2 signaling complex	1353:1394	Cooperativity in assembly of the final quaternary complex is easily explained by the extraordinarily extensive set of interfaces found within the fully assembled IL-2 signaling complex, which nearly span the entire length of the IL-2R beta and gamma(c) subunits.
16477002	9	52	theme	buried	1704:1709	arg1	surface					1711:1717	the smallest buried surface	1691:1717	the smallest buried surface	1691:1717	The IL-2/gamma(c) interface itself exhibits the smallest buried surface and the fewest hydrogen bonds in the complex, which is consistent with its promiscuous use in other cytokine receptor complexes.
16477002	8	53	theme	IL-2	1485:1488	arg1	A					1480:1480	Helix A	1474:1480	Helix A of IL-2	1474:1488	Helix A of IL-2 wedges tightly between IL-2R beta and gamma(c) to form a three-way junction that coalesces into a composite binding site for the final gamma(c) recruitment.
16477002	3	54	theme	quaternary	477:486	arg1	consistent					501:510	consistent	501:510	consistent	501:510	The quaternary structure is consistent with a stepwise assembly from IL-2/IL-2R alpha to IL-2/IL-2R alpha/IL-2R beta to IL-2/IL-2R alpha/IL-2R beta/gamma(c).
16477002	3	54	theme	quaternary	477:486	arg1	structure					488:496	The quaternary structure	473:496	The quaternary structure	473:496	The quaternary structure is consistent with a stepwise assembly from IL-2/IL-2R alpha to IL-2/IL-2R alpha/IL-2R beta to IL-2/IL-2R alpha/IL-2R beta/gamma(c).
16477002	4	55	theme	association	811:821	arg1	rate					823:826	the rapid association rate	801:826	the rapid association rate	801:826	The IL-2R alpha subunit forms the largest of the three IL-2/IL-2R interfaces, which, together with the high abundance of charge-charge interactions, correlates well with the rapid association rate and high-affinity interaction of IL-2R alpha with IL-2 at the cell surface.
16477002	9	56	from	surface	1711:1717	arg1	consistent					1774:1783	consistent	1774:1783	consistent	1774:1783	The IL-2/gamma(c) interface itself exhibits the smallest buried surface and the fewest hydrogen bonds in the complex, which is consistent with its promiscuous use in other cytokine receptor complexes.
16477002	9	56	from	surface	1711:1717	arg1	complex					1756:1762	the complex	1752:1762	the complex	1752:1762	The IL-2/gamma(c) interface itself exhibits the smallest buried surface and the fewest hydrogen bonds in the complex, which is consistent with its promiscuous use in other cytokine receptor complexes.
16477002	6	57	theme	signaling	1148:1156	arg1	complex					1158:1164	the signaling complex	1144:1164	the signaling complex	1144:1164	These findings support the principal role of IL-2R alpha to deliver IL-2 to the signaling complex and act as regulator of signal transduction.
16477002	9	58	theme	c	1662:1662	arg1	interface					1665:1673	The IL-2/gamma(c) interface itself	1647:1680	The IL-2/gamma(c) interface itself	1647:1680	The IL-2/gamma(c) interface itself exhibits the smallest buried surface and the fewest hydrogen bonds in the complex, which is consistent with its promiscuous use in other cytokine receptor complexes.
16477002	9	59	theme	fewest	1727:1732	arg1	bonds					1743:1747	the fewest hydrogen bonds	1723:1747	the fewest hydrogen bonds in the complex, which is consistent with its promiscuous use in other cytokine receptor complexes	1723:1845	The IL-2/gamma(c) interface itself exhibits the smallest buried surface and the fewest hydrogen bonds in the complex, which is consistent with its promiscuous use in other cytokine receptor complexes.
16477002	1	60	theme	IL-2R	301:305	arg1	subunits					279:286	the receptor subunits IL-2R alpha, IL-2R beta, and gamma(c)	266:324	the receptor subunits IL-2R alpha, IL-2R beta, and gamma(c)	266:324	IL-2 is a cytokine that functions as a growth factor and central regulator in the immune system and mediates its effects through ligand-induced hetero-trimerization of the receptor subunits IL-2R alpha, IL-2R beta, and gamma(c).
16477002	1	60	theme	IL-2R	301:305	arg1	beta					307:310	IL-2R beta	301:310	IL-2R beta	301:310	IL-2 is a cytokine that functions as a growth factor and central regulator in the immune system and mediates its effects through ligand-induced hetero-trimerization of the receptor subunits IL-2R alpha, IL-2R beta, and gamma(c).
16477002	8	61	theme	three-way	1547:1555	arg1	junction					1557:1564	a three-way junction	1545:1564	a three-way junction that coalesces into a composite binding site for the final gamma(c) recruitment	1545:1644	Helix A of IL-2 wedges tightly between IL-2R beta and gamma(c) to form a three-way junction that coalesces into a composite binding site for the final gamma(c) recruitment.
16477002	1	62	theme	central	155:161	arg1	regulator					163:171	central regulator	155:171	central regulator	155:171	IL-2 is a cytokine that functions as a growth factor and central regulator in the immune system and mediates its effects through ligand-induced hetero-trimerization of the receptor subunits IL-2R alpha, IL-2R beta, and gamma(c).
16477002	7	63	theme	extensive	1312:1320	arg1	interfaces					1329:1338	interfaces	1329:1338	interfaces found within the fully assembled IL-2 signaling complex, which nearly span the entire length of the IL-2R beta and gamma(c) subunits	1329:1471	Cooperativity in assembly of the final quaternary complex is easily explained by the extraordinarily extensive set of interfaces found within the fully assembled IL-2 signaling complex, which nearly span the entire length of the IL-2R beta and gamma(c) subunits.
16477002	7	63	theme	extensive	1312:1320	arg1	set					1322:1324	the extraordinarily extensive set	1292:1324	the extraordinarily extensive set of interfaces found within the fully assembled IL-2 signaling complex, which nearly span the entire length of the IL-2R beta and gamma(c) subunits	1292:1471	Cooperativity in assembly of the final quaternary complex is easily explained by the extraordinarily extensive set of interfaces found within the fully assembled IL-2 signaling complex, which nearly span the entire length of the IL-2R beta and gamma(c) subunits.
16477002	4	64	theme	IL-2R	861:865	arg1	alpha					867:871	IL-2R alpha	861:871	IL-2R alpha	861:871	The IL-2R alpha subunit forms the largest of the three IL-2/IL-2R interfaces, which, together with the high abundance of charge-charge interactions, correlates well with the rapid association rate and high-affinity interaction of IL-2R alpha with IL-2 at the cell surface.
16477002	2	65	from	complex	434:440	arg1	assembly					383:390	the trimeric assembly	370:390	the trimeric assembly of the human IL-2 receptor ectodomains in complex with IL-2 at 3.0 A resolution	370:470	Here, we describe the crystal structure of the trimeric assembly of the human IL-2 receptor ectodomains in complex with IL-2 at 3.0 A resolution.
16477002	5	66	located	observed	1004:1011	arg2	changes					992:998	only minor changes	981:998	only minor changes	981:998	Surprisingly, IL-2R alpha makes no contacts with IL-2R beta or gamma(c), and only minor changes are observed in the IL-2 structure in response to receptor binding.
16477002	5	66	located	observed	1004:1011	arg1	structure					1025:1033	the IL-2 structure	1016:1033	the IL-2 structure in response to receptor binding	1016:1065	Surprisingly, IL-2R alpha makes no contacts with IL-2R beta or gamma(c), and only minor changes are observed in the IL-2 structure in response to receptor binding.
16477002	1	67	theme	immune	180:185	arg1	system					187:192	the immune system	176:192	the immune system	176:192	IL-2 is a cytokine that functions as a growth factor and central regulator in the immune system and mediates its effects through ligand-induced hetero-trimerization of the receptor subunits IL-2R alpha, IL-2R beta, and gamma(c).
16477002	9	68	from	bonds	1743:1747	arg1	consistent					1774:1783	consistent	1774:1783	consistent	1774:1783	The IL-2/gamma(c) interface itself exhibits the smallest buried surface and the fewest hydrogen bonds in the complex, which is consistent with its promiscuous use in other cytokine receptor complexes.
16477002	9	68	from	bonds	1743:1747	arg1	complex					1756:1762	the complex	1752:1762	the complex	1752:1762	The IL-2/gamma(c) interface itself exhibits the smallest buried surface and the fewest hydrogen bonds in the complex, which is consistent with its promiscuous use in other cytokine receptor complexes.
16477002	6	69	theme	transduction	1197:1208	arg1	regulator					1177:1185	regulator	1177:1185	regulator of signal transduction	1177:1208	These findings support the principal role of IL-2R alpha to deliver IL-2 to the signaling complex and act as regulator of signal transduction.
16477002	5	70	theme	minor	986:990	arg1	changes					992:998	only minor changes	981:998	only minor changes	981:998	Surprisingly, IL-2R alpha makes no contacts with IL-2R beta or gamma(c), and only minor changes are observed in the IL-2 structure in response to receptor binding.
16477002	3	71	theme	stepwise	519:526	arg1	assembly					528:535	a stepwise assembly	517:535	a stepwise assembly from IL-2/IL-2R alpha to IL-2/IL-2R alpha/IL-2R beta to IL-2/IL-2R alpha/IL-2R beta/gamma(c)	517:628	The quaternary structure is consistent with a stepwise assembly from IL-2/IL-2R alpha to IL-2/IL-2R alpha/IL-2R beta to IL-2/IL-2R alpha/IL-2R beta/gamma(c).
16477002	8	72	theme	composite	1588:1596	arg1	site					1606:1609	a composite binding site	1586:1609	a composite binding site for the final gamma(c) recruitment	1586:1644	Helix A of IL-2 wedges tightly between IL-2R beta and gamma(c) to form a three-way junction that coalesces into a composite binding site for the final gamma(c) recruitment.
16477002	6	73	theme	IL-2R	1113:1117	arg1	alpha					1119:1123	IL-2R alpha	1113:1123	IL-2R alpha	1113:1123	These findings support the principal role of IL-2R alpha to deliver IL-2 to the signaling complex and act as regulator of signal transduction.
16477002	3	74	theme	IL-2/IL-2R	562:571	arg1	beta					585:588	IL-2/IL-2R alpha/IL-2R beta	562:588	IL-2/IL-2R alpha/IL-2R beta to IL-2/IL-2R alpha/IL-2R beta/gamma(c)	562:628	The quaternary structure is consistent with a stepwise assembly from IL-2/IL-2R alpha to IL-2/IL-2R alpha/IL-2R beta to IL-2/IL-2R alpha/IL-2R beta/gamma(c).
16477002	2	75	from	resolution	461:470	arg1	complex					434:440	complex	434:440	complex with IL-2 at 3.0 A resolution	434:470	Here, we describe the crystal structure of the trimeric assembly of the human IL-2 receptor ectodomains in complex with IL-2 at 3.0 A resolution.
16477002	2	75	from	resolution	461:470	arg1	ectodomains					419:429	the human IL-2 receptor ectodomains	395:429	the human IL-2 receptor ectodomains in complex with IL-2 at 3.0 A resolution	395:470	Here, we describe the crystal structure of the trimeric assembly of the human IL-2 receptor ectodomains in complex with IL-2 at 3.0 A resolution.
16477002	7	76	theme	quaternary	1250:1259	arg1	complex					1261:1267	the final quaternary complex	1240:1267	the final quaternary complex	1240:1267	Cooperativity in assembly of the final quaternary complex is easily explained by the extraordinarily extensive set of interfaces found within the fully assembled IL-2 signaling complex, which nearly span the entire length of the IL-2R beta and gamma(c) subunits.
16477002	2	77	from	assembly	383:390	arg1	complex					434:440	complex	434:440	complex with IL-2 at 3.0 A resolution	434:470	Here, we describe the crystal structure of the trimeric assembly of the human IL-2 receptor ectodomains in complex with IL-2 at 3.0 A resolution.
16477002	9	78	theme	promiscuous	1794:1804	arg1	use					1806:1808	its promiscuous use	1790:1808	its promiscuous use in other cytokine receptor complexes	1790:1845	The IL-2/gamma(c) interface itself exhibits the smallest buried surface and the fewest hydrogen bonds in the complex, which is consistent with its promiscuous use in other cytokine receptor complexes.
16477002	0	79	theme	heterotrimeric	64:77	arg1	receptor					88:95	a heterotrimeric cytokine receptor	62:95	a heterotrimeric cytokine receptor	62:95	Crystal structure of the IL-2 signaling complex: paradigm for a heterotrimeric cytokine receptor.
16477002	5	80	theme	IL-2	1020:1023	arg1	structure					1025:1033	the IL-2 structure	1016:1033	the IL-2 structure in response to receptor binding	1016:1065	Surprisingly, IL-2R alpha makes no contacts with IL-2R beta or gamma(c), and only minor changes are observed in the IL-2 structure in response to receptor binding.
16477002	8	81	theme	gamma	1625:1629	arg1	recruitment					1634:1644	the final gamma(c) recruitment	1615:1644	the final gamma(c) recruitment	1615:1644	Helix A of IL-2 wedges tightly between IL-2R beta and gamma(c) to form a three-way junction that coalesces into a composite binding site for the final gamma(c) recruitment.
16477002	4	82	theme	IL-2R	635:639	arg1	subunit					647:653	The IL-2R alpha subunit	631:653	The IL-2R alpha subunit	631:653	The IL-2R alpha subunit forms the largest of the three IL-2/IL-2R interfaces, which, together with the high abundance of charge-charge interactions, correlates well with the rapid association rate and high-affinity interaction of IL-2R alpha with IL-2 at the cell surface.
16477002	9	83	with	consistent	1774:1783	arg1	use					1806:1808	its promiscuous use	1790:1808	its promiscuous use in other cytokine receptor complexes	1790:1845	The IL-2/gamma(c) interface itself exhibits the smallest buried surface and the fewest hydrogen bonds in the complex, which is consistent with its promiscuous use in other cytokine receptor complexes.
16477002	8	84	theme	c	1631:1631	arg1	recruitment					1634:1644	the final gamma(c) recruitment	1615:1644	the final gamma(c) recruitment	1615:1644	Helix A of IL-2 wedges tightly between IL-2R beta and gamma(c) to form a three-way junction that coalesces into a composite binding site for the final gamma(c) recruitment.
16477002	7	85	theme	IL-2R	1440:1444	arg1	beta					1446:1449	IL-2R beta	1440:1449	IL-2R beta	1440:1449	Cooperativity in assembly of the final quaternary complex is easily explained by the extraordinarily extensive set of interfaces found within the fully assembled IL-2 signaling complex, which nearly span the entire length of the IL-2R beta and gamma(c) subunits.
16477002	2	86	theme	A	459:459	arg1	resolution					461:470	3.0 A resolution	455:470	3.0 A resolution	455:470	Here, we describe the crystal structure of the trimeric assembly of the human IL-2 receptor ectodomains in complex with IL-2 at 3.0 A resolution.
16477002	9	87	theme	cytokine	1819:1826	arg1	complexes					1837:1845	other cytokine receptor complexes	1813:1845	other cytokine receptor complexes	1813:1845	The IL-2/gamma(c) interface itself exhibits the smallest buried surface and the fewest hydrogen bonds in the complex, which is consistent with its promiscuous use in other cytokine receptor complexes.
16477002	3	88	from	alpha	553:557	arg1	assembly					528:535	a stepwise assembly	517:535	a stepwise assembly from IL-2/IL-2R alpha to IL-2/IL-2R alpha/IL-2R beta to IL-2/IL-2R alpha/IL-2R beta/gamma(c)	517:628	The quaternary structure is consistent with a stepwise assembly from IL-2/IL-2R alpha to IL-2/IL-2R alpha/IL-2R beta to IL-2/IL-2R alpha/IL-2R beta/gamma(c).
16477002	4	89	theme	cell	890:893	arg1	surface					895:901	the cell surface	886:901	the cell surface	886:901	The IL-2R alpha subunit forms the largest of the three IL-2/IL-2R interfaces, which, together with the high abundance of charge-charge interactions, correlates well with the rapid association rate and high-affinity interaction of IL-2R alpha with IL-2 at the cell surface.
16477002	2	90	from	ectodomains	419:429	arg1	complex					434:440	complex	434:440	complex with IL-2 at 3.0 A resolution	434:470	Here, we describe the crystal structure of the trimeric assembly of the human IL-2 receptor ectodomains in complex with IL-2 at 3.0 A resolution.
16477002	2	90	from	ectodomains	419:429	arg1	resolution					461:470	3.0 A resolution	455:470	3.0 A resolution	455:470	Here, we describe the crystal structure of the trimeric assembly of the human IL-2 receptor ectodomains in complex with IL-2 at 3.0 A resolution.
16477002	1	91	theme	receptor	270:277	arg1	subunits					279:286	the receptor subunits IL-2R alpha, IL-2R beta, and gamma(c)	266:324	the receptor subunits IL-2R alpha, IL-2R beta, and gamma(c)	266:324	IL-2 is a cytokine that functions as a growth factor and central regulator in the immune system and mediates its effects through ligand-induced hetero-trimerization of the receptor subunits IL-2R alpha, IL-2R beta, and gamma(c).
16477002	1	91	theme	receptor	270:277	arg1	gamma					317:321	gamma	317:321	gamma(c)	317:324	IL-2 is a cytokine that functions as a growth factor and central regulator in the immune system and mediates its effects through ligand-induced hetero-trimerization of the receptor subunits IL-2R alpha, IL-2R beta, and gamma(c).
16477002	1	91	theme	receptor	270:277	arg1	alpha					294:298	IL-2R alpha	288:298	IL-2R alpha	288:298	IL-2 is a cytokine that functions as a growth factor and central regulator in the immune system and mediates its effects through ligand-induced hetero-trimerization of the receptor subunits IL-2R alpha, IL-2R beta, and gamma(c).
16477002	1	91	theme	receptor	270:277	arg1	beta					307:310	IL-2R beta	301:310	IL-2R beta	301:310	IL-2 is a cytokine that functions as a growth factor and central regulator in the immune system and mediates its effects through ligand-induced hetero-trimerization of the receptor subunits IL-2R alpha, IL-2R beta, and gamma(c).
16477002	4	92	with	interaction	846:856	arg1	IL-2					878:881	IL-2	878:881	IL-2 at the cell surface	878:901	The IL-2R alpha subunit forms the largest of the three IL-2/IL-2R interfaces, which, together with the high abundance of charge-charge interactions, correlates well with the rapid association rate and high-affinity interaction of IL-2R alpha with IL-2 at the cell surface.
16477002	2	93	theme	trimeric	374:381	arg1	assembly					383:390	the trimeric assembly	370:390	the trimeric assembly of the human IL-2 receptor ectodomains in complex with IL-2 at 3.0 A resolution	370:470	Here, we describe the crystal structure of the trimeric assembly of the human IL-2 receptor ectodomains in complex with IL-2 at 3.0 A resolution.
16477002	3	94	theme	IL-2/IL-2R	593:602	arg1	c					627:627	c	627:627	c	627:627	The quaternary structure is consistent with a stepwise assembly from IL-2/IL-2R alpha to IL-2/IL-2R alpha/IL-2R beta to IL-2/IL-2R alpha/IL-2R beta/gamma(c).
16477002	3	94	theme	IL-2/IL-2R	593:602	arg1	beta/gamma					616:625	IL-2/IL-2R alpha/IL-2R beta/gamma	593:625	IL-2/IL-2R alpha/IL-2R beta/gamma(c)	593:628	The quaternary structure is consistent with a stepwise assembly from IL-2/IL-2R alpha to IL-2/IL-2R alpha/IL-2R beta to IL-2/IL-2R alpha/IL-2R beta/gamma(c).
16477002	0	95	theme	signaling	30:38	arg1	complex					40:46	the IL-2 signaling complex	21:46	the IL-2 signaling complex	21:46	Crystal structure of the IL-2 signaling complex: paradigm for a heterotrimeric cytokine receptor.
16477002	1	96	theme	IL-2R	288:292	arg1	subunits					279:286	the receptor subunits IL-2R alpha, IL-2R beta, and gamma(c)	266:324	the receptor subunits IL-2R alpha, IL-2R beta, and gamma(c)	266:324	IL-2 is a cytokine that functions as a growth factor and central regulator in the immune system and mediates its effects through ligand-induced hetero-trimerization of the receptor subunits IL-2R alpha, IL-2R beta, and gamma(c).
16477002	1	96	theme	IL-2R	288:292	arg1	alpha					294:298	IL-2R alpha	288:298	IL-2R alpha	288:298	IL-2 is a cytokine that functions as a growth factor and central regulator in the immune system and mediates its effects through ligand-induced hetero-trimerization of the receptor subunits IL-2R alpha, IL-2R beta, and gamma(c).
16477002	2	97	theme	receptor	410:417	arg1	ectodomains					419:429	the human IL-2 receptor ectodomains	395:429	the human IL-2 receptor ectodomains in complex with IL-2 at 3.0 A resolution	395:470	Here, we describe the crystal structure of the trimeric assembly of the human IL-2 receptor ectodomains in complex with IL-2 at 3.0 A resolution.
16477002	2	98	theme	crystal	349:355	arg1	structure					357:365	the crystal structure	345:365	the crystal structure of the trimeric assembly of the human IL-2 receptor ectodomains in complex with IL-2 at 3.0 A resolution	345:470	Here, we describe the crystal structure of the trimeric assembly of the human IL-2 receptor ectodomains in complex with IL-2 at 3.0 A resolution.
16477002	2	99	theme	human	399:403	arg1	ectodomains					419:429	the human IL-2 receptor ectodomains	395:429	the human IL-2 receptor ectodomains in complex with IL-2 at 3.0 A resolution	395:470	Here, we describe the crystal structure of the trimeric assembly of the human IL-2 receptor ectodomains in complex with IL-2 at 3.0 A resolution.
16477002	4	100	theme	charge-charge	752:764	arg1	interactions					766:777	charge-charge interactions	752:777	charge-charge interactions	752:777	The IL-2R alpha subunit forms the largest of the three IL-2/IL-2R interfaces, which, together with the high abundance of charge-charge interactions, correlates well with the rapid association rate and high-affinity interaction of IL-2R alpha with IL-2 at the cell surface.
16477002	8	101	theme	Helix	1474:1478	arg1	A					1480:1480	Helix A	1474:1480	Helix A of IL-2	1474:1488	Helix A of IL-2 wedges tightly between IL-2R beta and gamma(c) to form a three-way junction that coalesces into a composite binding site for the final gamma(c) recruitment.
16477002	0	102	dep	structure	8:16	arg1	paradigm					49:56	paradigm	49:56	Crystal structure of the IL-2 signaling complex: paradigm for a heterotrimeric cytokine receptor.	0:96	Crystal structure of the IL-2 signaling complex: paradigm for a heterotrimeric cytokine receptor.
16477002	7	103	from	Cooperativity	1211:1223	arg1	assembly					1228:1235	assembly	1228:1235	assembly of the final quaternary complex	1228:1267	Cooperativity in assembly of the final quaternary complex is easily explained by the extraordinarily extensive set of interfaces found within the fully assembled IL-2 signaling complex, which nearly span the entire length of the IL-2R beta and gamma(c) subunits.
16477002	5	104	with	contacts	939:946	arg1	c					973:973	c	973:973	c	973:973	Surprisingly, IL-2R alpha makes no contacts with IL-2R beta or gamma(c), and only minor changes are observed in the IL-2 structure in response to receptor binding.
16477002	5	104	with	contacts	939:946	arg1	gamma					967:971	gamma	967:971	gamma(c)	967:974	Surprisingly, IL-2R alpha makes no contacts with IL-2R beta or gamma(c), and only minor changes are observed in the IL-2 structure in response to receptor binding.
16477002	5	104	with	contacts	939:946	arg1	beta					959:962	IL-2R beta	953:962	IL-2R beta	953:962	Surprisingly, IL-2R alpha makes no contacts with IL-2R beta or gamma(c), and only minor changes are observed in the IL-2 structure in response to receptor binding.
20684603	1	0	theme	imidazolopyrimidine	345:363	arg1	series					365:370	an imidazolopyrimidine series	342:370	an imidazolopyrimidine series in particular	342:384	Continued structure-activity relationship (SAR) exploration within our previously disclosed azolopyrimidine containing dipeptidyl peptidase-4 (DPP4) inhibitors led us to focus on an imidazolopyrimidine series in particular.
20684603	2	1	theme	related	635:641	arg1	hERG					649:652	hERG	649:652	hERG	649:652	Further study revealed that by replacing the aryl substitution on the imidazole ring with a more polar carboxylic ester or amide, these compounds displayed not only increased DPP4 binding activity but also significantly reduced human ether-a-go-go related gene (hERG) and sodium channel inhibitory activities.
20684603	2	1	theme	related	635:641	arg1	gene					643:646	human ether-a-go-go related gene	615:646	human ether-a-go-go related gene (hERG)	615:653	Further study revealed that by replacing the aryl substitution on the imidazole ring with a more polar carboxylic ester or amide, these compounds displayed not only increased DPP4 binding activity but also significantly reduced human ether-a-go-go related gene (hERG) and sodium channel inhibitory activities.
20684603	2	2	from	substitution	437:448	arg1	ring					467:470	the imidazole ring	453:470	the imidazole ring	453:470	Further study revealed that by replacing the aryl substitution on the imidazole ring with a more polar carboxylic ester or amide, these compounds displayed not only increased DPP4 binding activity but also significantly reduced human ether-a-go-go related gene (hERG) and sodium channel inhibitory activities.
20684603	5	3	theme	PK	1215:1216	arg1	profiles					1218:1225	excellent PK profiles	1205:1225	excellent PK profiles	1205:1225	A subsequent lead molecule from this series, (+)-6-(aminomethyl)-5-(2,4-dichlorophenyl)-N-(1-ethyl-1H-pyrazol-5-yl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamide (24s), emerged as a potent, selective DPP4 inhibitor that displayed excellent PK profiles and in vivo efficacy in ob/ob mice.
20684603	0	4	theme	-7-methylimidazo[1,2-a	51:72	arg1	Discovery					0:8	Discovery	0:8	Discovery of 6-(aminomethyl)-5-(2,4-dichlorophenyl)-7-methylimidazo[1,2-a]	0:73	Discovery of 6-(aminomethyl)-5-(2,4-dichlorophenyl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamides as potent, selective dipeptidyl peptidase-4 (DPP4) inhibitors.
20684603	2	5	theme	ether-a-go-go	621:633	arg1	hERG					649:652	hERG	649:652	hERG	649:652	Further study revealed that by replacing the aryl substitution on the imidazole ring with a more polar carboxylic ester or amide, these compounds displayed not only increased DPP4 binding activity but also significantly reduced human ether-a-go-go related gene (hERG) and sodium channel inhibitory activities.
20684603	2	5	theme	ether-a-go-go	621:633	arg1	gene					643:646	human ether-a-go-go related gene	615:646	human ether-a-go-go related gene (hERG)	615:653	Further study revealed that by replacing the aryl substitution on the imidazole ring with a more polar carboxylic ester or amide, these compounds displayed not only increased DPP4 binding activity but also significantly reduced human ether-a-go-go related gene (hERG) and sodium channel inhibitory activities.
20684603	2	6	theme	inhibitory	674:683	arg1	activities					685:694	sodium channel inhibitory activities	659:694	sodium channel inhibitory activities	659:694	Further study revealed that by replacing the aryl substitution on the imidazole ring with a more polar carboxylic ester or amide, these compounds displayed not only increased DPP4 binding activity but also significantly reduced human ether-a-go-go related gene (hERG) and sodium channel inhibitory activities.
20684603	1	7	theme	dipeptidyl	282:291	arg1	inhibitors					312:321	dipeptidyl peptidase-4 (DPP4) inhibitors	282:321	dipeptidyl peptidase-4 (DPP4) inhibitors	282:321	Continued structure-activity relationship (SAR) exploration within our previously disclosed azolopyrimidine containing dipeptidyl peptidase-4 (DPP4) inhibitors led us to focus on an imidazolopyrimidine series in particular.
20684603	4	8	theme	amide	963:967	arg1	24c					969:971	amide 24c	963:971	amide 24c	963:971	The active site binding mode of these compounds was determined by X-ray crystallography as exemplified by amide 24c.
20684603	2	9	theme	human	615:619	arg1	hERG					649:652	hERG	649:652	hERG	649:652	Further study revealed that by replacing the aryl substitution on the imidazole ring with a more polar carboxylic ester or amide, these compounds displayed not only increased DPP4 binding activity but also significantly reduced human ether-a-go-go related gene (hERG) and sodium channel inhibitory activities.
20684603	2	9	theme	human	615:619	arg1	gene					643:646	human ether-a-go-go related gene	615:646	human ether-a-go-go related gene (hERG)	615:653	Further study revealed that by replacing the aryl substitution on the imidazole ring with a more polar carboxylic ester or amide, these compounds displayed not only increased DPP4 binding activity but also significantly reduced human ether-a-go-go related gene (hERG) and sodium channel inhibitory activities.
20684603	2	10	theme	channel	666:672	arg1	activities					685:694	sodium channel inhibitory activities	659:694	sodium channel inhibitory activities	659:694	Further study revealed that by replacing the aryl substitution on the imidazole ring with a more polar carboxylic ester or amide, these compounds displayed not only increased DPP4 binding activity but also significantly reduced human ether-a-go-go related gene (hERG) and sodium channel inhibitory activities.
20684603	5	11	from	series	1011:1016	arg1	molecule					992:999	A subsequent lead molecule	974:999	A subsequent lead molecule from this series	974:1016	A subsequent lead molecule from this series, (+)-6-(aminomethyl)-5-(2,4-dichlorophenyl)-N-(1-ethyl-1H-pyrazol-5-yl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamide (24s), emerged as a potent, selective DPP4 inhibitor that displayed excellent PK profiles and in vivo efficacy in ob/ob mice.
20684603	5	11	from	series	1011:1016	arg1	pyrimidine-2-carboxamide					1112:1135	(+)-6-(aminomethyl)-5-(2,4-dichlorophenyl)-N-(1-ethyl-1H-pyrazol-5-yl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamide	1019:1135	pyrimidine-2-carboxamide	1112:1135	A subsequent lead molecule from this series, (+)-6-(aminomethyl)-5-(2,4-dichlorophenyl)-N-(1-ethyl-1H-pyrazol-5-yl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamide (24s), emerged as a potent, selective DPP4 inhibitor that displayed excellent PK profiles and in vivo efficacy in ob/ob mice.
20684603	1	12	theme	peptidase-4	293:303	arg1	inhibitors					312:321	dipeptidyl peptidase-4 (DPP4) inhibitors	282:321	dipeptidyl peptidase-4 (DPP4) inhibitors	282:321	Continued structure-activity relationship (SAR) exploration within our previously disclosed azolopyrimidine containing dipeptidyl peptidase-4 (DPP4) inhibitors led us to focus on an imidazolopyrimidine series in particular.
20684603	5	13	theme	ob/ob	1251:1255	arg1	mice					1257:1260	ob/ob mice	1251:1260	ob/ob mice	1251:1260	A subsequent lead molecule from this series, (+)-6-(aminomethyl)-5-(2,4-dichlorophenyl)-N-(1-ethyl-1H-pyrazol-5-yl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamide (24s), emerged as a potent, selective DPP4 inhibitor that displayed excellent PK profiles and in vivo efficacy in ob/ob mice.
20684603	2	14	theme	sodium	659:664	arg1	activities					685:694	sodium channel inhibitory activities	659:694	sodium channel inhibitory activities	659:694	Further study revealed that by replacing the aryl substitution on the imidazole ring with a more polar carboxylic ester or amide, these compounds displayed not only increased DPP4 binding activity but also significantly reduced human ether-a-go-go related gene (hERG) and sodium channel inhibitory activities.
20684603	0	15	dep	potent	103:108	arg1	selective					111:119	selective	111:119	selective	111:119	Discovery of 6-(aminomethyl)-5-(2,4-dichlorophenyl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamides as potent, selective dipeptidyl peptidase-4 (DPP4) inhibitors.
20684603	5	16	theme	in	1231:1232	arg1	efficacy					1239:1246	in vivo efficacy	1231:1246	in vivo efficacy	1231:1246	A subsequent lead molecule from this series, (+)-6-(aminomethyl)-5-(2,4-dichlorophenyl)-N-(1-ethyl-1H-pyrazol-5-yl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamide (24s), emerged as a potent, selective DPP4 inhibitor that displayed excellent PK profiles and in vivo efficacy in ob/ob mice.
20684603	1	17	theme	Continued	163:171	arg1	exploration					211:221	Continued structure-activity relationship (SAR) exploration	163:221	Continued structure-activity relationship (SAR) exploration within our previously disclosed azolopyrimidine containing dipeptidyl peptidase-4 (DPP4) inhibitors	163:321	Continued structure-activity relationship (SAR) exploration within our previously disclosed azolopyrimidine containing dipeptidyl peptidase-4 (DPP4) inhibitors led us to focus on an imidazolopyrimidine series in particular.
20684603	0	18	theme	potent	103:108	arg1	inhibitors					151:160	potent, selective dipeptidyl peptidase-4 (DPP4) inhibitors	103:160	potent, selective dipeptidyl peptidase-4 (DPP4) inhibitors	103:160	Discovery of 6-(aminomethyl)-5-(2,4-dichlorophenyl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamides as potent, selective dipeptidyl peptidase-4 (DPP4) inhibitors.
20684603	2	19	theme	carboxylic	490:499	arg1	ester					501:505	a more polar carboxylic ester	477:505	a more polar carboxylic ester	477:505	Further study revealed that by replacing the aryl substitution on the imidazole ring with a more polar carboxylic ester or amide, these compounds displayed not only increased DPP4 binding activity but also significantly reduced human ether-a-go-go related gene (hERG) and sodium channel inhibitory activities.
20684603	1	20	theme	structure-activity	173:190	arg1	relationship					192:203	structure-activity relationship	173:203	Continued structure-activity relationship (SAR) exploration within our previously disclosed azolopyrimidine containing dipeptidyl peptidase-4 (DPP4) inhibitors	163:321	Continued structure-activity relationship (SAR) exploration within our previously disclosed azolopyrimidine containing dipeptidyl peptidase-4 (DPP4) inhibitors led us to focus on an imidazolopyrimidine series in particular.
20684603	2	21	theme	polar	484:488	arg1	ester					501:505	a more polar carboxylic ester	477:505	a more polar carboxylic ester	477:505	Further study revealed that by replacing the aryl substitution on the imidazole ring with a more polar carboxylic ester or amide, these compounds displayed not only increased DPP4 binding activity but also significantly reduced human ether-a-go-go related gene (hERG) and sodium channel inhibitory activities.
20684603	3	22	theme	permeable	750:758	arg1	molecules					760:768	permeable molecules	750:768	permeable molecules which exhibited favorable pharmacokinetic (PK) profiles in preclinical animal species	750:854	Additional incremental adjustment of polarity led to permeable molecules which exhibited favorable pharmacokinetic (PK) profiles in preclinical animal species.
20684603	4	23	theme	compounds	895:903	arg1	mode					881:884	The active site binding mode	857:884	The active site binding mode of these compounds	857:903	The active site binding mode of these compounds was determined by X-ray crystallography as exemplified by amide 24c.
20684603	3	24	theme	pharmacokinetic	796:810	arg1	profiles					817:824	favorable pharmacokinetic (PK) profiles	786:824	favorable pharmacokinetic (PK) profiles	786:824	Additional incremental adjustment of polarity led to permeable molecules which exhibited favorable pharmacokinetic (PK) profiles in preclinical animal species.
20684603	3	24	theme	pharmacokinetic	796:810	arg1	PK					813:814	PK	813:814	PK	813:814	Additional incremental adjustment of polarity led to permeable molecules which exhibited favorable pharmacokinetic (PK) profiles in preclinical animal species.
20684603	5	25	theme	subsequent	976:985	arg1	molecule					992:999	A subsequent lead molecule	974:999	A subsequent lead molecule from this series	974:1016	A subsequent lead molecule from this series, (+)-6-(aminomethyl)-5-(2,4-dichlorophenyl)-N-(1-ethyl-1H-pyrazol-5-yl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamide (24s), emerged as a potent, selective DPP4 inhibitor that displayed excellent PK profiles and in vivo efficacy in ob/ob mice.
20684603	5	25	theme	subsequent	976:985	arg1	pyrimidine-2-carboxamide					1112:1135	(+)-6-(aminomethyl)-5-(2,4-dichlorophenyl)-N-(1-ethyl-1H-pyrazol-5-yl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamide	1019:1135	pyrimidine-2-carboxamide	1112:1135	A subsequent lead molecule from this series, (+)-6-(aminomethyl)-5-(2,4-dichlorophenyl)-N-(1-ethyl-1H-pyrazol-5-yl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamide (24s), emerged as a potent, selective DPP4 inhibitor that displayed excellent PK profiles and in vivo efficacy in ob/ob mice.
20684603	1	26	theme	relationship	192:203	arg1	exploration					211:221	Continued structure-activity relationship (SAR) exploration	163:221	Continued structure-activity relationship (SAR) exploration within our previously disclosed azolopyrimidine containing dipeptidyl peptidase-4 (DPP4) inhibitors	163:321	Continued structure-activity relationship (SAR) exploration within our previously disclosed azolopyrimidine containing dipeptidyl peptidase-4 (DPP4) inhibitors led us to focus on an imidazolopyrimidine series in particular.
20684603	1	27	theme	DPP4	306:309	arg1	inhibitors					312:321	dipeptidyl peptidase-4 (DPP4) inhibitors	282:321	dipeptidyl peptidase-4 (DPP4) inhibitors	282:321	Continued structure-activity relationship (SAR) exploration within our previously disclosed azolopyrimidine containing dipeptidyl peptidase-4 (DPP4) inhibitors led us to focus on an imidazolopyrimidine series in particular.
20684603	5	28	theme	lead	987:990	arg1	molecule					992:999	A subsequent lead molecule	974:999	A subsequent lead molecule from this series	974:1016	A subsequent lead molecule from this series, (+)-6-(aminomethyl)-5-(2,4-dichlorophenyl)-N-(1-ethyl-1H-pyrazol-5-yl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamide (24s), emerged as a potent, selective DPP4 inhibitor that displayed excellent PK profiles and in vivo efficacy in ob/ob mice.
20684603	5	28	theme	lead	987:990	arg1	pyrimidine-2-carboxamide					1112:1135	(+)-6-(aminomethyl)-5-(2,4-dichlorophenyl)-N-(1-ethyl-1H-pyrazol-5-yl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamide	1019:1135	pyrimidine-2-carboxamide	1112:1135	A subsequent lead molecule from this series, (+)-6-(aminomethyl)-5-(2,4-dichlorophenyl)-N-(1-ethyl-1H-pyrazol-5-yl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamide (24s), emerged as a potent, selective DPP4 inhibitor that displayed excellent PK profiles and in vivo efficacy in ob/ob mice.
20684603	2	29	theme	imidazole	457:465	arg1	ring					467:470	the imidazole ring	453:470	the imidazole ring	453:470	Further study revealed that by replacing the aryl substitution on the imidazole ring with a more polar carboxylic ester or amide, these compounds displayed not only increased DPP4 binding activity but also significantly reduced human ether-a-go-go related gene (hERG) and sodium channel inhibitory activities.
20684603	0	30	theme	dipeptidyl	121:130	arg1	peptidase-4					132:142	dipeptidyl peptidase-4	121:142	potent, selective dipeptidyl peptidase-4 (DPP4) inhibitors	103:160	Discovery of 6-(aminomethyl)-5-(2,4-dichlorophenyl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamides as potent, selective dipeptidyl peptidase-4 (DPP4) inhibitors.
20684603	0	30	theme	dipeptidyl	121:130	arg1	DPP4					145:148	DPP4	145:148	DPP4	145:148	Discovery of 6-(aminomethyl)-5-(2,4-dichlorophenyl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamides as potent, selective dipeptidyl peptidase-4 (DPP4) inhibitors.
20684603	5	31	theme	2,4-dichlorophenyl	1042:1059	arg1	24s					1138:1140	24s	1138:1140	24s	1138:1140	A subsequent lead molecule from this series, (+)-6-(aminomethyl)-5-(2,4-dichlorophenyl)-N-(1-ethyl-1H-pyrazol-5-yl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamide (24s), emerged as a potent, selective DPP4 inhibitor that displayed excellent PK profiles and in vivo efficacy in ob/ob mice.
20684603	5	31	theme	2,4-dichlorophenyl	1042:1059	arg1	molecule					992:999	A subsequent lead molecule	974:999	A subsequent lead molecule from this series	974:1016	A subsequent lead molecule from this series, (+)-6-(aminomethyl)-5-(2,4-dichlorophenyl)-N-(1-ethyl-1H-pyrazol-5-yl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamide (24s), emerged as a potent, selective DPP4 inhibitor that displayed excellent PK profiles and in vivo efficacy in ob/ob mice.
20684603	5	31	theme	2,4-dichlorophenyl	1042:1059	arg1	pyrimidine-2-carboxamide					1112:1135	(+)-6-(aminomethyl)-5-(2,4-dichlorophenyl)-N-(1-ethyl-1H-pyrazol-5-yl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamide	1019:1135	pyrimidine-2-carboxamide	1112:1135	A subsequent lead molecule from this series, (+)-6-(aminomethyl)-5-(2,4-dichlorophenyl)-N-(1-ethyl-1H-pyrazol-5-yl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamide (24s), emerged as a potent, selective DPP4 inhibitor that displayed excellent PK profiles and in vivo efficacy in ob/ob mice.
20684603	4	32	theme	active	861:866	arg1	mode					881:884	The active site binding mode	857:884	The active site binding mode of these compounds	857:903	The active site binding mode of these compounds was determined by X-ray crystallography as exemplified by amide 24c.
20684603	2	33	theme	DPP4	562:565	arg1	activity					575:582	DPP4 binding activity	562:582	DPP4 binding activity	562:582	Further study revealed that by replacing the aryl substitution on the imidazole ring with a more polar carboxylic ester or amide, these compounds displayed not only increased DPP4 binding activity but also significantly reduced human ether-a-go-go related gene (hERG) and sodium channel inhibitory activities.
20684603	5	34	theme	1-ethyl-1H-pyrazol-5-yl	1065:1087	arg1	24s					1138:1140	24s	1138:1140	24s	1138:1140	A subsequent lead molecule from this series, (+)-6-(aminomethyl)-5-(2,4-dichlorophenyl)-N-(1-ethyl-1H-pyrazol-5-yl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamide (24s), emerged as a potent, selective DPP4 inhibitor that displayed excellent PK profiles and in vivo efficacy in ob/ob mice.
20684603	5	34	theme	1-ethyl-1H-pyrazol-5-yl	1065:1087	arg1	molecule					992:999	A subsequent lead molecule	974:999	A subsequent lead molecule from this series	974:1016	A subsequent lead molecule from this series, (+)-6-(aminomethyl)-5-(2,4-dichlorophenyl)-N-(1-ethyl-1H-pyrazol-5-yl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamide (24s), emerged as a potent, selective DPP4 inhibitor that displayed excellent PK profiles and in vivo efficacy in ob/ob mice.
20684603	5	34	theme	1-ethyl-1H-pyrazol-5-yl	1065:1087	arg1	pyrimidine-2-carboxamide					1112:1135	(+)-6-(aminomethyl)-5-(2,4-dichlorophenyl)-N-(1-ethyl-1H-pyrazol-5-yl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamide	1019:1135	pyrimidine-2-carboxamide	1112:1135	A subsequent lead molecule from this series, (+)-6-(aminomethyl)-5-(2,4-dichlorophenyl)-N-(1-ethyl-1H-pyrazol-5-yl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamide (24s), emerged as a potent, selective DPP4 inhibitor that displayed excellent PK profiles and in vivo efficacy in ob/ob mice.
20684603	5	35	theme	-5-	1038:1040	arg1	24s					1138:1140	24s	1138:1140	24s	1138:1140	A subsequent lead molecule from this series, (+)-6-(aminomethyl)-5-(2,4-dichlorophenyl)-N-(1-ethyl-1H-pyrazol-5-yl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamide (24s), emerged as a potent, selective DPP4 inhibitor that displayed excellent PK profiles and in vivo efficacy in ob/ob mice.
20684603	5	35	theme	-5-	1038:1040	arg1	molecule					992:999	A subsequent lead molecule	974:999	A subsequent lead molecule from this series	974:1016	A subsequent lead molecule from this series, (+)-6-(aminomethyl)-5-(2,4-dichlorophenyl)-N-(1-ethyl-1H-pyrazol-5-yl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamide (24s), emerged as a potent, selective DPP4 inhibitor that displayed excellent PK profiles and in vivo efficacy in ob/ob mice.
20684603	5	35	theme	-5-	1038:1040	arg1	pyrimidine-2-carboxamide					1112:1135	(+)-6-(aminomethyl)-5-(2,4-dichlorophenyl)-N-(1-ethyl-1H-pyrazol-5-yl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamide	1019:1135	pyrimidine-2-carboxamide	1112:1135	A subsequent lead molecule from this series, (+)-6-(aminomethyl)-5-(2,4-dichlorophenyl)-N-(1-ethyl-1H-pyrazol-5-yl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamide (24s), emerged as a potent, selective DPP4 inhibitor that displayed excellent PK profiles and in vivo efficacy in ob/ob mice.
20684603	1	36	from	series	365:370	arg1	particular					375:384	particular	375:384	particular	375:384	Continued structure-activity relationship (SAR) exploration within our previously disclosed azolopyrimidine containing dipeptidyl peptidase-4 (DPP4) inhibitors led us to focus on an imidazolopyrimidine series in particular.
20684603	3	37	theme	favorable	786:794	arg1	profiles					817:824	favorable pharmacokinetic (PK) profiles	786:824	favorable pharmacokinetic (PK) profiles	786:824	Additional incremental adjustment of polarity led to permeable molecules which exhibited favorable pharmacokinetic (PK) profiles in preclinical animal species.
20684603	3	37	theme	favorable	786:794	arg1	PK					813:814	PK	813:814	PK	813:814	Additional incremental adjustment of polarity led to permeable molecules which exhibited favorable pharmacokinetic (PK) profiles in preclinical animal species.
20684603	1	38	dep	relationship	192:203	arg1	SAR					206:208	SAR	206:208	SAR	206:208	Continued structure-activity relationship (SAR) exploration within our previously disclosed azolopyrimidine containing dipeptidyl peptidase-4 (DPP4) inhibitors led us to focus on an imidazolopyrimidine series in particular.
20684603	2	39	theme	aryl	432:435	arg1	substitution					437:448	the aryl substitution	428:448	the aryl substitution on the imidazole ring	428:470	Further study revealed that by replacing the aryl substitution on the imidazole ring with a more polar carboxylic ester or amide, these compounds displayed not only increased DPP4 binding activity but also significantly reduced human ether-a-go-go related gene (hERG) and sodium channel inhibitory activities.
20684603	0	40	theme	aminomethyl	16:26	arg1	-7-methylimidazo[1,2-a					51:72	6-(aminomethyl)-5-(2,4-dichlorophenyl)-7-methylimidazo[1,2-a]	13:73	6-(aminomethyl)-5-(2,4-dichlorophenyl)-7-methylimidazo[1,2-a]	13:73	Discovery of 6-(aminomethyl)-5-(2,4-dichlorophenyl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamides as potent, selective dipeptidyl peptidase-4 (DPP4) inhibitors.
20684603	5	41	theme	potent	1157:1162	arg1	inhibitor					1180:1188	a potent, selective DPP4 inhibitor	1155:1188	inhibitor	1180:1188	A subsequent lead molecule from this series, (+)-6-(aminomethyl)-5-(2,4-dichlorophenyl)-N-(1-ethyl-1H-pyrazol-5-yl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamide (24s), emerged as a potent, selective DPP4 inhibitor that displayed excellent PK profiles and in vivo efficacy in ob/ob mice.
20684603	0	42	theme	peptidase-4	132:142	arg1	inhibitors					151:160	potent, selective dipeptidyl peptidase-4 (DPP4) inhibitors	103:160	potent, selective dipeptidyl peptidase-4 (DPP4) inhibitors	103:160	Discovery of 6-(aminomethyl)-5-(2,4-dichlorophenyl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamides as potent, selective dipeptidyl peptidase-4 (DPP4) inhibitors.
20684603	5	43	theme	-7-methylimidazo[1,2-a	1089:1110	arg1	24s					1138:1140	24s	1138:1140	24s	1138:1140	A subsequent lead molecule from this series, (+)-6-(aminomethyl)-5-(2,4-dichlorophenyl)-N-(1-ethyl-1H-pyrazol-5-yl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamide (24s), emerged as a potent, selective DPP4 inhibitor that displayed excellent PK profiles and in vivo efficacy in ob/ob mice.
20684603	5	43	theme	-7-methylimidazo[1,2-a	1089:1110	arg1	molecule					992:999	A subsequent lead molecule	974:999	A subsequent lead molecule from this series	974:1016	A subsequent lead molecule from this series, (+)-6-(aminomethyl)-5-(2,4-dichlorophenyl)-N-(1-ethyl-1H-pyrazol-5-yl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamide (24s), emerged as a potent, selective DPP4 inhibitor that displayed excellent PK profiles and in vivo efficacy in ob/ob mice.
20684603	5	43	theme	-7-methylimidazo[1,2-a	1089:1110	arg1	pyrimidine-2-carboxamide					1112:1135	(+)-6-(aminomethyl)-5-(2,4-dichlorophenyl)-N-(1-ethyl-1H-pyrazol-5-yl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamide	1019:1135	pyrimidine-2-carboxamide	1112:1135	A subsequent lead molecule from this series, (+)-6-(aminomethyl)-5-(2,4-dichlorophenyl)-N-(1-ethyl-1H-pyrazol-5-yl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamide (24s), emerged as a potent, selective DPP4 inhibitor that displayed excellent PK profiles and in vivo efficacy in ob/ob mice.
20684603	3	44	theme	preclinical	829:839	arg1	species					848:854	preclinical animal species	829:854	preclinical animal species	829:854	Additional incremental adjustment of polarity led to permeable molecules which exhibited favorable pharmacokinetic (PK) profiles in preclinical animal species.
20684603	5	45	theme	excellent	1205:1213	arg1	profiles					1218:1225	excellent PK profiles	1205:1225	excellent PK profiles	1205:1225	A subsequent lead molecule from this series, (+)-6-(aminomethyl)-5-(2,4-dichlorophenyl)-N-(1-ethyl-1H-pyrazol-5-yl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamide (24s), emerged as a potent, selective DPP4 inhibitor that displayed excellent PK profiles and in vivo efficacy in ob/ob mice.
20684603	5	46	theme	aminomethyl	1026:1036	arg1	24s					1138:1140	24s	1138:1140	24s	1138:1140	A subsequent lead molecule from this series, (+)-6-(aminomethyl)-5-(2,4-dichlorophenyl)-N-(1-ethyl-1H-pyrazol-5-yl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamide (24s), emerged as a potent, selective DPP4 inhibitor that displayed excellent PK profiles and in vivo efficacy in ob/ob mice.
20684603	5	46	theme	aminomethyl	1026:1036	arg1	molecule					992:999	A subsequent lead molecule	974:999	A subsequent lead molecule from this series	974:1016	A subsequent lead molecule from this series, (+)-6-(aminomethyl)-5-(2,4-dichlorophenyl)-N-(1-ethyl-1H-pyrazol-5-yl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamide (24s), emerged as a potent, selective DPP4 inhibitor that displayed excellent PK profiles and in vivo efficacy in ob/ob mice.
20684603	5	46	theme	aminomethyl	1026:1036	arg1	pyrimidine-2-carboxamide					1112:1135	(+)-6-(aminomethyl)-5-(2,4-dichlorophenyl)-N-(1-ethyl-1H-pyrazol-5-yl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamide	1019:1135	pyrimidine-2-carboxamide	1112:1135	A subsequent lead molecule from this series, (+)-6-(aminomethyl)-5-(2,4-dichlorophenyl)-N-(1-ethyl-1H-pyrazol-5-yl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamide (24s), emerged as a potent, selective DPP4 inhibitor that displayed excellent PK profiles and in vivo efficacy in ob/ob mice.
20684603	4	47	theme	binding	873:879	arg1	mode					881:884	The active site binding mode	857:884	The active site binding mode of these compounds	857:903	The active site binding mode of these compounds was determined by X-ray crystallography as exemplified by amide 24c.
20684603	0	48	theme	-5-	28:30	arg1	-7-methylimidazo[1,2-a					51:72	6-(aminomethyl)-5-(2,4-dichlorophenyl)-7-methylimidazo[1,2-a]	13:73	6-(aminomethyl)-5-(2,4-dichlorophenyl)-7-methylimidazo[1,2-a]	13:73	Discovery of 6-(aminomethyl)-5-(2,4-dichlorophenyl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamides as potent, selective dipeptidyl peptidase-4 (DPP4) inhibitors.
20684603	5	49	theme	selective	1165:1173	arg1	inhibitor					1180:1188	a potent, selective DPP4 inhibitor	1155:1188	inhibitor	1180:1188	A subsequent lead molecule from this series, (+)-6-(aminomethyl)-5-(2,4-dichlorophenyl)-N-(1-ethyl-1H-pyrazol-5-yl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamide (24s), emerged as a potent, selective DPP4 inhibitor that displayed excellent PK profiles and in vivo efficacy in ob/ob mice.
20684603	2	50	theme	binding	567:573	arg1	activity					575:582	DPP4 binding activity	562:582	DPP4 binding activity	562:582	Further study revealed that by replacing the aryl substitution on the imidazole ring with a more polar carboxylic ester or amide, these compounds displayed not only increased DPP4 binding activity but also significantly reduced human ether-a-go-go related gene (hERG) and sodium channel inhibitory activities.
20684603	3	51	theme	Additional	697:706	arg1	adjustment					720:729	Additional incremental adjustment	697:729	Additional incremental adjustment of polarity	697:741	Additional incremental adjustment of polarity led to permeable molecules which exhibited favorable pharmacokinetic (PK) profiles in preclinical animal species.
20684603	4	52	theme	site	868:871	arg1	mode					881:884	The active site binding mode	857:884	The active site binding mode of these compounds	857:903	The active site binding mode of these compounds was determined by X-ray crystallography as exemplified by amide 24c.
20684603	4	53	theme	X-ray	923:927	arg1	crystallography					929:943	X-ray crystallography	923:943	X-ray crystallography	923:943	The active site binding mode of these compounds was determined by X-ray crystallography as exemplified by amide 24c.
20684603	5	54	theme	DPP4	1175:1178	arg1	inhibitor					1180:1188	a potent, selective DPP4 inhibitor	1155:1188	inhibitor	1180:1188	A subsequent lead molecule from this series, (+)-6-(aminomethyl)-5-(2,4-dichlorophenyl)-N-(1-ethyl-1H-pyrazol-5-yl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamide (24s), emerged as a potent, selective DPP4 inhibitor that displayed excellent PK profiles and in vivo efficacy in ob/ob mice.
20684603	3	55	theme	incremental	708:718	arg1	adjustment					720:729	Additional incremental adjustment	697:729	Additional incremental adjustment of polarity	697:741	Additional incremental adjustment of polarity led to permeable molecules which exhibited favorable pharmacokinetic (PK) profiles in preclinical animal species.
20684603	5	56	theme	+	1020:1020	arg1	24s					1138:1140	24s	1138:1140	24s	1138:1140	A subsequent lead molecule from this series, (+)-6-(aminomethyl)-5-(2,4-dichlorophenyl)-N-(1-ethyl-1H-pyrazol-5-yl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamide (24s), emerged as a potent, selective DPP4 inhibitor that displayed excellent PK profiles and in vivo efficacy in ob/ob mice.
20684603	5	56	theme	+	1020:1020	arg1	molecule					992:999	A subsequent lead molecule	974:999	A subsequent lead molecule from this series	974:1016	A subsequent lead molecule from this series, (+)-6-(aminomethyl)-5-(2,4-dichlorophenyl)-N-(1-ethyl-1H-pyrazol-5-yl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamide (24s), emerged as a potent, selective DPP4 inhibitor that displayed excellent PK profiles and in vivo efficacy in ob/ob mice.
20684603	5	56	theme	+	1020:1020	arg1	pyrimidine-2-carboxamide					1112:1135	(+)-6-(aminomethyl)-5-(2,4-dichlorophenyl)-N-(1-ethyl-1H-pyrazol-5-yl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamide	1019:1135	pyrimidine-2-carboxamide	1112:1135	A subsequent lead molecule from this series, (+)-6-(aminomethyl)-5-(2,4-dichlorophenyl)-N-(1-ethyl-1H-pyrazol-5-yl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamide (24s), emerged as a potent, selective DPP4 inhibitor that displayed excellent PK profiles and in vivo efficacy in ob/ob mice.
20684603	5	57	theme	-N-	1061:1063	arg1	24s					1138:1140	24s	1138:1140	24s	1138:1140	A subsequent lead molecule from this series, (+)-6-(aminomethyl)-5-(2,4-dichlorophenyl)-N-(1-ethyl-1H-pyrazol-5-yl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamide (24s), emerged as a potent, selective DPP4 inhibitor that displayed excellent PK profiles and in vivo efficacy in ob/ob mice.
20684603	5	57	theme	-N-	1061:1063	arg1	molecule					992:999	A subsequent lead molecule	974:999	A subsequent lead molecule from this series	974:1016	A subsequent lead molecule from this series, (+)-6-(aminomethyl)-5-(2,4-dichlorophenyl)-N-(1-ethyl-1H-pyrazol-5-yl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamide (24s), emerged as a potent, selective DPP4 inhibitor that displayed excellent PK profiles and in vivo efficacy in ob/ob mice.
20684603	5	57	theme	-N-	1061:1063	arg1	pyrimidine-2-carboxamide					1112:1135	(+)-6-(aminomethyl)-5-(2,4-dichlorophenyl)-N-(1-ethyl-1H-pyrazol-5-yl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamide	1019:1135	pyrimidine-2-carboxamide	1112:1135	A subsequent lead molecule from this series, (+)-6-(aminomethyl)-5-(2,4-dichlorophenyl)-N-(1-ethyl-1H-pyrazol-5-yl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamide (24s), emerged as a potent, selective DPP4 inhibitor that displayed excellent PK profiles and in vivo efficacy in ob/ob mice.
20684603	2	58	dep	displayed	533:541	arg1	increased					552:560	increased	552:560	displayed not only increased DPP4 binding activity but also significantly reduced human ether-a-go-go related gene (hERG) and sodium channel inhibitory activities	533:694	Further study revealed that by replacing the aryl substitution on the imidazole ring with a more polar carboxylic ester or amide, these compounds displayed not only increased DPP4 binding activity but also significantly reduced human ether-a-go-go related gene (hERG) and sodium channel inhibitory activities.
20684603	5	59	dep	in	1231:1232	arg1	vivo					1234:1237	vivo	1234:1237	vivo	1234:1237	A subsequent lead molecule from this series, (+)-6-(aminomethyl)-5-(2,4-dichlorophenyl)-N-(1-ethyl-1H-pyrazol-5-yl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamide (24s), emerged as a potent, selective DPP4 inhibitor that displayed excellent PK profiles and in vivo efficacy in ob/ob mice.
20684603	5	60	theme	-6-	1022:1024	arg1	24s					1138:1140	24s	1138:1140	24s	1138:1140	A subsequent lead molecule from this series, (+)-6-(aminomethyl)-5-(2,4-dichlorophenyl)-N-(1-ethyl-1H-pyrazol-5-yl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamide (24s), emerged as a potent, selective DPP4 inhibitor that displayed excellent PK profiles and in vivo efficacy in ob/ob mice.
20684603	5	60	theme	-6-	1022:1024	arg1	molecule					992:999	A subsequent lead molecule	974:999	A subsequent lead molecule from this series	974:1016	A subsequent lead molecule from this series, (+)-6-(aminomethyl)-5-(2,4-dichlorophenyl)-N-(1-ethyl-1H-pyrazol-5-yl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamide (24s), emerged as a potent, selective DPP4 inhibitor that displayed excellent PK profiles and in vivo efficacy in ob/ob mice.
20684603	5	60	theme	-6-	1022:1024	arg1	pyrimidine-2-carboxamide					1112:1135	(+)-6-(aminomethyl)-5-(2,4-dichlorophenyl)-N-(1-ethyl-1H-pyrazol-5-yl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamide	1019:1135	pyrimidine-2-carboxamide	1112:1135	A subsequent lead molecule from this series, (+)-6-(aminomethyl)-5-(2,4-dichlorophenyl)-N-(1-ethyl-1H-pyrazol-5-yl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamide (24s), emerged as a potent, selective DPP4 inhibitor that displayed excellent PK profiles and in vivo efficacy in ob/ob mice.
20684603	1	61	theme	disclosed	245:253	arg1	azolopyrimidine					255:269	our previously disclosed azolopyrimidine	230:269	our previously disclosed azolopyrimidine containing dipeptidyl peptidase-4 (DPP4) inhibitors	230:321	Continued structure-activity relationship (SAR) exploration within our previously disclosed azolopyrimidine containing dipeptidyl peptidase-4 (DPP4) inhibitors led us to focus on an imidazolopyrimidine series in particular.
20684603	0	62	theme	2,4-dichlorophenyl	32:49	arg1	-7-methylimidazo[1,2-a					51:72	6-(aminomethyl)-5-(2,4-dichlorophenyl)-7-methylimidazo[1,2-a]	13:73	6-(aminomethyl)-5-(2,4-dichlorophenyl)-7-methylimidazo[1,2-a]	13:73	Discovery of 6-(aminomethyl)-5-(2,4-dichlorophenyl)-7-methylimidazo[1,2-a]pyrimidine-2-carboxamides as potent, selective dipeptidyl peptidase-4 (DPP4) inhibitors.
20684603	3	63	theme	polarity	734:741	arg1	adjustment					720:729	Additional incremental adjustment	697:729	Additional incremental adjustment of polarity	697:741	Additional incremental adjustment of polarity led to permeable molecules which exhibited favorable pharmacokinetic (PK) profiles in preclinical animal species.
20684603	1	64	contain	containing	271:280	arg1	azolopyrimidine					255:269	our previously disclosed azolopyrimidine	230:269	our previously disclosed azolopyrimidine containing dipeptidyl peptidase-4 (DPP4) inhibitors	230:321	Continued structure-activity relationship (SAR) exploration within our previously disclosed azolopyrimidine containing dipeptidyl peptidase-4 (DPP4) inhibitors led us to focus on an imidazolopyrimidine series in particular.
20684603	1	64	contain	containing	271:280	arg2	inhibitors					312:321	dipeptidyl peptidase-4 (DPP4) inhibitors	282:321	dipeptidyl peptidase-4 (DPP4) inhibitors	282:321	Continued structure-activity relationship (SAR) exploration within our previously disclosed azolopyrimidine containing dipeptidyl peptidase-4 (DPP4) inhibitors led us to focus on an imidazolopyrimidine series in particular.
20684603	2	65	theme	Further	387:393	arg1	study					395:399	Further study	387:399	Further study	387:399	Further study revealed that by replacing the aryl substitution on the imidazole ring with a more polar carboxylic ester or amide, these compounds displayed not only increased DPP4 binding activity but also significantly reduced human ether-a-go-go related gene (hERG) and sodium channel inhibitory activities.
20684603	3	66	theme	animal	841:846	arg1	species					848:854	preclinical animal species	829:854	preclinical animal species	829:854	Additional incremental adjustment of polarity led to permeable molecules which exhibited favorable pharmacokinetic (PK) profiles in preclinical animal species.
12483204	0	0	theme	substrate	74:82	arg1	analog					84:89	a substrate analog	72:89	a substrate analog	72:89	Crystal structure of human dipeptidyl peptidase IV/CD26 in complex with a substrate analog.
12483204	6	1	theme	new	752:754	arg1	opening					771:777	a new and unexpected opening	750:777	a new and unexpected opening to the active site	750:796	The structure indicates how substrate specificity is achieved and reveals a new and unexpected opening to the active site.
12483204	1	2	theme	multifunctional	135:149	arg1	peptidase					180:188	a multifunctional type II transmembrane serine peptidase	133:188	a multifunctional type II transmembrane serine peptidase	133:188	Dipeptidyl peptidase IV (DPP-IV/CD26) is a multifunctional type II transmembrane serine peptidase.
12483204	1	2	theme	multifunctional	135:149	arg1	peptidase					103:111	Dipeptidyl peptidase IV	92:114	Dipeptidyl peptidase IV (DPP-IV/CD26)	92:128	Dipeptidyl peptidase IV (DPP-IV/CD26) is a multifunctional type II transmembrane serine peptidase.
12483204	4	3	from	located	513:519	arg1	cavity					532:537	a large cavity	524:537	a large cavity formed between the alpha/beta-hydrolase domain and an eight-bladed beta-propeller domain	524:626	The catalytic site is located in a large cavity formed between the alpha/beta-hydrolase domain and an eight-bladed beta-propeller domain.
12483204	1	4	theme	type	151:154	arg1	peptidase					180:188	a multifunctional type II transmembrane serine peptidase	133:188	a multifunctional type II transmembrane serine peptidase	133:188	Dipeptidyl peptidase IV (DPP-IV/CD26) is a multifunctional type II transmembrane serine peptidase.
12483204	1	4	theme	type	151:154	arg1	peptidase					103:111	Dipeptidyl peptidase IV	92:114	Dipeptidyl peptidase IV (DPP-IV/CD26)	92:128	Dipeptidyl peptidase IV (DPP-IV/CD26) is a multifunctional type II transmembrane serine peptidase.
12483204	4	5	theme	beta-propeller	606:619	arg1	domain					621:626	an eight-bladed beta-propeller domain	590:626	an eight-bladed beta-propeller domain	590:626	The catalytic site is located in a large cavity formed between the alpha/beta-hydrolase domain and an eight-bladed beta-propeller domain.
12483204	2	6	theme	sugar	285:289	arg1	homeostasis					291:301	blood sugar homeostasis	279:301	blood sugar homeostasis	279:301	This enzyme contributes to the regulation of various physiological processes, including blood sugar homeostasis, by cleaving peptide hormones, chemokines and neuropeptides.
12483204	4	7	theme	eight-bladed	593:604	arg1	domain					621:626	an eight-bladed beta-propeller domain	590:626	an eight-bladed beta-propeller domain	590:626	The catalytic site is located in a large cavity formed between the alpha/beta-hydrolase domain and an eight-bladed beta-propeller domain.
12483204	0	8	with	complex	59:65	arg1	analog					84:89	a substrate analog	72:89	a substrate analog	72:89	Crystal structure of human dipeptidyl peptidase IV/CD26 in complex with a substrate analog.
12483204	2	9	theme	blood	279:283	arg1	homeostasis					291:301	blood sugar homeostasis	279:301	blood sugar homeostasis	279:301	This enzyme contributes to the regulation of various physiological processes, including blood sugar homeostasis, by cleaving peptide hormones, chemokines and neuropeptides.
12483204	1	10	theme	serine	173:178	arg1	peptidase					180:188	a multifunctional type II transmembrane serine peptidase	133:188	a multifunctional type II transmembrane serine peptidase	133:188	Dipeptidyl peptidase IV (DPP-IV/CD26) is a multifunctional type II transmembrane serine peptidase.
12483204	1	10	theme	serine	173:178	arg1	peptidase					103:111	Dipeptidyl peptidase IV	92:114	Dipeptidyl peptidase IV (DPP-IV/CD26)	92:128	Dipeptidyl peptidase IV (DPP-IV/CD26) is a multifunctional type II transmembrane serine peptidase.
12483204	3	11	theme	DPP-IV	434:439	arg1	region					424:429	the extracellular region	406:429	the extracellular region of DPP-IV	406:439	We have determined the 2.5 A structure of the extracellular region of DPP-IV in complex with the inhibitor valine-pyrrolidide.
12483204	4	12	theme	catalytic	495:503	arg1	located					513:519	located	513:519	located	513:519	The catalytic site is located in a large cavity formed between the alpha/beta-hydrolase domain and an eight-bladed beta-propeller domain.
12483204	4	12	theme	catalytic	495:503	arg1	site					505:508	The catalytic site	491:508	The catalytic site	491:508	The catalytic site is located in a large cavity formed between the alpha/beta-hydrolase domain and an eight-bladed beta-propeller domain.
12483204	1	13	theme	transmembrane	159:171	arg1	peptidase					180:188	a multifunctional type II transmembrane serine peptidase	133:188	a multifunctional type II transmembrane serine peptidase	133:188	Dipeptidyl peptidase IV (DPP-IV/CD26) is a multifunctional type II transmembrane serine peptidase.
12483204	1	13	theme	transmembrane	159:171	arg1	peptidase					103:111	Dipeptidyl peptidase IV	92:114	Dipeptidyl peptidase IV (DPP-IV/CD26)	92:128	Dipeptidyl peptidase IV (DPP-IV/CD26) is a multifunctional type II transmembrane serine peptidase.
12483204	5	14	theme	inhibitor	657:665	arg1	binding					667:673	inhibitor binding	657:673	inhibitor binding	657:673	Both domains participate in inhibitor binding.
12483204	2	15	theme	peptide	316:322	arg1	hormones					324:331	peptide hormones	316:331	peptide hormones	316:331	This enzyme contributes to the regulation of various physiological processes, including blood sugar homeostasis, by cleaving peptide hormones, chemokines and neuropeptides.
12483204	3	16	theme	region	424:429	arg1	structure					393:401	A structure	391:401	the 2.5 A structure of the extracellular region of DPP-IV in complex with the inhibitor valine-pyrrolidide	383:488	We have determined the 2.5 A structure of the extracellular region of DPP-IV in complex with the inhibitor valine-pyrrolidide.
12483204	0	17	theme	Crystal	0:6	arg1	structure					8:16	Crystal structure	0:16	Crystal structure of human dipeptidyl peptidase	0:46	Crystal structure of human dipeptidyl peptidase IV/CD26 in complex with a substrate analog.
12483204	4	18	from	cavity	532:537	arg1	located					513:519	located	513:519	located	513:519	The catalytic site is located in a large cavity formed between the alpha/beta-hydrolase domain and an eight-bladed beta-propeller domain.
12483204	4	18	from	cavity	532:537	arg1	site					505:508	The catalytic site	491:508	The catalytic site	491:508	The catalytic site is located in a large cavity formed between the alpha/beta-hydrolase domain and an eight-bladed beta-propeller domain.
12483204	0	19	theme	human	21:25	arg1	peptidase					38:46	human dipeptidyl peptidase	21:46	human dipeptidyl peptidase	21:46	Crystal structure of human dipeptidyl peptidase IV/CD26 in complex with a substrate analog.
12483204	3	20	with	complex	444:450	arg1	valine-pyrrolidide					471:488	the inhibitor valine-pyrrolidide	457:488	the inhibitor valine-pyrrolidide	457:488	We have determined the 2.5 A structure of the extracellular region of DPP-IV in complex with the inhibitor valine-pyrrolidide.
12483204	1	21	theme	Dipeptidyl	92:101	arg1	DPP-IV/CD26					117:127	DPP-IV/CD26	117:127	DPP-IV/CD26	117:127	Dipeptidyl peptidase IV (DPP-IV/CD26) is a multifunctional type II transmembrane serine peptidase.
12483204	1	21	theme	Dipeptidyl	92:101	arg1	peptidase					180:188	a multifunctional type II transmembrane serine peptidase	133:188	a multifunctional type II transmembrane serine peptidase	133:188	Dipeptidyl peptidase IV (DPP-IV/CD26) is a multifunctional type II transmembrane serine peptidase.
12483204	1	21	theme	Dipeptidyl	92:101	arg1	peptidase					103:111	Dipeptidyl peptidase IV	92:114	Dipeptidyl peptidase IV (DPP-IV/CD26)	92:128	Dipeptidyl peptidase IV (DPP-IV/CD26) is a multifunctional type II transmembrane serine peptidase.
12483204	6	22	theme	substrate	704:712	arg1	specificity					714:724	substrate specificity	704:724	substrate specificity	704:724	The structure indicates how substrate specificity is achieved and reveals a new and unexpected opening to the active site.
12483204	3	23	theme	inhibitor	461:469	arg1	valine-pyrrolidide					471:488	the inhibitor valine-pyrrolidide	457:488	the inhibitor valine-pyrrolidide	457:488	We have determined the 2.5 A structure of the extracellular region of DPP-IV in complex with the inhibitor valine-pyrrolidide.
12483204	0	24	theme	peptidase	38:46	arg1	structure					8:16	Crystal structure	0:16	Crystal structure of human dipeptidyl peptidase	0:46	Crystal structure of human dipeptidyl peptidase IV/CD26 in complex with a substrate analog.
12483204	4	25	theme	alpha/beta-hydrolase	558:577	arg1	domain					579:584	the alpha/beta-hydrolase domain	554:584	the alpha/beta-hydrolase domain	554:584	The catalytic site is located in a large cavity formed between the alpha/beta-hydrolase domain and an eight-bladed beta-propeller domain.
12483204	0	26	theme	dipeptidyl	27:36	arg1	peptidase					38:46	human dipeptidyl peptidase	21:46	human dipeptidyl peptidase	21:46	Crystal structure of human dipeptidyl peptidase IV/CD26 in complex with a substrate analog.
12483204	4	27	theme	large	526:530	arg1	cavity					532:537	a large cavity	524:537	a large cavity formed between the alpha/beta-hydrolase domain and an eight-bladed beta-propeller domain	524:626	The catalytic site is located in a large cavity formed between the alpha/beta-hydrolase domain and an eight-bladed beta-propeller domain.
12483204	3	28	theme	extracellular	410:422	arg1	region					424:429	the extracellular region	406:429	the extracellular region of DPP-IV	406:439	We have determined the 2.5 A structure of the extracellular region of DPP-IV in complex with the inhibitor valine-pyrrolidide.
12483204	6	29	theme	active	786:791	arg1	site					793:796	the active site	782:796	the active site	782:796	The structure indicates how substrate specificity is achieved and reveals a new and unexpected opening to the active site.
12483204	4	30	located	located	513:519	arg1	cavity					532:537	a large cavity	524:537	a large cavity formed between the alpha/beta-hydrolase domain and an eight-bladed beta-propeller domain	524:626	The catalytic site is located in a large cavity formed between the alpha/beta-hydrolase domain and an eight-bladed beta-propeller domain.
12483204	4	30	located	located	513:519	arg2	located					513:519	located	513:519	located	513:519	The catalytic site is located in a large cavity formed between the alpha/beta-hydrolase domain and an eight-bladed beta-propeller domain.
12483204	4	30	located	located	513:519	arg2	site					505:508	The catalytic site	491:508	The catalytic site	491:508	The catalytic site is located in a large cavity formed between the alpha/beta-hydrolase domain and an eight-bladed beta-propeller domain.
12483204	2	31	theme	processes	258:266	arg1	regulation					222:231	the regulation	218:231	the regulation of various physiological processes, including blood sugar homeostasis,	218:302	This enzyme contributes to the regulation of various physiological processes, including blood sugar homeostasis, by cleaving peptide hormones, chemokines and neuropeptides.
12483204	2	32	theme	physiological	244:256	arg1	homeostasis					291:301	blood sugar homeostasis	279:301	blood sugar homeostasis	279:301	This enzyme contributes to the regulation of various physiological processes, including blood sugar homeostasis, by cleaving peptide hormones, chemokines and neuropeptides.
12483204	2	32	theme	physiological	244:256	arg1	processes					258:266	various physiological processes	236:266	various physiological processes	236:266	This enzyme contributes to the regulation of various physiological processes, including blood sugar homeostasis, by cleaving peptide hormones, chemokines and neuropeptides.
12483204	6	33	theme	unexpected	760:769	arg1	opening					771:777	a new and unexpected opening	750:777	a new and unexpected opening to the active site	750:796	The structure indicates how substrate specificity is achieved and reveals a new and unexpected opening to the active site.
12483204	3	34	from	structure	393:401	arg1	complex					444:450	complex	444:450	complex with the inhibitor valine-pyrrolidide	444:488	We have determined the 2.5 A structure of the extracellular region of DPP-IV in complex with the inhibitor valine-pyrrolidide.
12483204	2	35	theme	various	236:242	arg1	homeostasis					291:301	blood sugar homeostasis	279:301	blood sugar homeostasis	279:301	This enzyme contributes to the regulation of various physiological processes, including blood sugar homeostasis, by cleaving peptide hormones, chemokines and neuropeptides.
12483204	2	35	theme	various	236:242	arg1	processes					258:266	various physiological processes	236:266	various physiological processes	236:266	This enzyme contributes to the regulation of various physiological processes, including blood sugar homeostasis, by cleaving peptide hormones, chemokines and neuropeptides.
23835475	6	0	from	subdomain	870:878	arg1	divergent					836:844	divergent	836:844	divergent	836:844	MERS-CoV RBD and related SARS-CoV RBD share a high degree of structural similarity in their core subdomains, but are notably divergent in the receptor-binding subdomain.
23835475	5	1	theme	receptor-binding	612:627	arg1	subdomain					629:637	The receptor-binding subdomain	608:637	The receptor-binding subdomain	608:637	The receptor-binding subdomain interacts with DPP4 β-propeller but not its intrinsic hydrolase domain.
23835475	1	2	theme	East	145:148	arg1	MERS-CoV					184:191	MERS-CoV	184:191	MERS-CoV	184:191	The spike glycoprotein (S) of recently identified Middle East respiratory syndrome coronavirus (MERS-CoV) targets the cellular receptor, dipeptidyl peptidase 4 (DPP4).
23835475	1	2	theme	East	145:148	arg1	coronavirus					171:181	East respiratory syndrome coronavirus	145:181	The spike glycoprotein (S) of recently identified Middle East respiratory syndrome coronavirus (MERS-CoV)	88:192	The spike glycoprotein (S) of recently identified Middle East respiratory syndrome coronavirus (MERS-CoV) targets the cellular receptor, dipeptidyl peptidase 4 (DPP4).
23835475	8	3	theme	MERS-CoV	1092:1099	arg1	RBD					1101:1103	MERS-CoV RBD	1092:1103	MERS-CoV RBD	1092:1103	The atomic details at the interface between MERS-CoV RBD and DPP4 provide structural understanding of the virus and receptor interaction, which can guide development of therapeutics and vaccines against MERS-CoV infection.
23835475	8	4	theme	structural	1122:1131	arg1	understanding					1133:1145	structural understanding	1122:1145	structural understanding	1122:1145	The atomic details at the interface between MERS-CoV RBD and DPP4 provide structural understanding of the virus and receptor interaction, which can guide development of therapeutics and vaccines against MERS-CoV infection.
23835475	8	5	theme	virus	1154:1158	arg1	interaction					1173:1183	the virus and receptor interaction	1150:1183	interaction	1173:1183	The atomic details at the interface between MERS-CoV RBD and DPP4 provide structural understanding of the virus and receptor interaction, which can guide development of therapeutics and vaccines against MERS-CoV infection.
23835475	1	6	theme	respiratory	150:160	arg1	MERS-CoV					184:191	MERS-CoV	184:191	MERS-CoV	184:191	The spike glycoprotein (S) of recently identified Middle East respiratory syndrome coronavirus (MERS-CoV) targets the cellular receptor, dipeptidyl peptidase 4 (DPP4).
23835475	1	6	theme	respiratory	150:160	arg1	coronavirus					171:181	East respiratory syndrome coronavirus	145:181	The spike glycoprotein (S) of recently identified Middle East respiratory syndrome coronavirus (MERS-CoV)	88:192	The spike glycoprotein (S) of recently identified Middle East respiratory syndrome coronavirus (MERS-CoV) targets the cellular receptor, dipeptidyl peptidase 4 (DPP4).
23835475	4	7	theme	MERS-CoV	542:549	arg1	RBD					551:553	MERS-CoV RBD	542:553	MERS-CoV RBD	542:553	Our results show that MERS-CoV RBD consists of a core and a receptor-binding subdomain.
23835475	3	8	theme	extracellular	484:496	arg1	DPP4					514:517	human DPP4	508:517	human DPP4	508:517	We report the 3.0 Å-resolution crystal structure of MERS-CoV RBD bound to the extracellular domain of human DPP4.
23835475	3	8	theme	extracellular	484:496	arg1	domain					498:503	the extracellular domain	480:503	the extracellular domain of human DPP4	480:517	We report the 3.0 Å-resolution crystal structure of MERS-CoV RBD bound to the extracellular domain of human DPP4.
23835475	3	9	theme	DPP4	514:517	arg1	DPP4					514:517	human DPP4	508:517	human DPP4	508:517	We report the 3.0 Å-resolution crystal structure of MERS-CoV RBD bound to the extracellular domain of human DPP4.
23835475	3	9	theme	DPP4	514:517	arg1	domain					498:503	the extracellular domain	480:503	the extracellular domain of human DPP4	480:517	We report the 3.0 Å-resolution crystal structure of MERS-CoV RBD bound to the extracellular domain of human DPP4.
23835475	6	10	from	degree	762:767	arg1	subdomains					808:817	their core subdomains	797:817	their core subdomains	797:817	MERS-CoV RBD and related SARS-CoV RBD share a high degree of structural similarity in their core subdomains, but are notably divergent in the receptor-binding subdomain.
23835475	2	11	from	domain	340:345	arg1	spike					366:370	the viral spike	356:370	the viral spike	356:370	Sequence comparison and modeling analysis have revealed a putative receptor-binding domain (RBD) on the viral spike, which mediates this interaction.
23835475	4	12	theme	receptor-binding	580:595	arg1	subdomain					597:605	a receptor-binding subdomain	578:605	a receptor-binding subdomain	578:605	Our results show that MERS-CoV RBD consists of a core and a receptor-binding subdomain.
23835475	2	13	theme	Sequence	256:263	arg1	comparison					265:274	Sequence comparison	256:274	Sequence comparison	256:274	Sequence comparison and modeling analysis have revealed a putative receptor-binding domain (RBD) on the viral spike, which mediates this interaction.
23835475	1	14	theme	syndrome	162:169	arg1	MERS-CoV					184:191	MERS-CoV	184:191	MERS-CoV	184:191	The spike glycoprotein (S) of recently identified Middle East respiratory syndrome coronavirus (MERS-CoV) targets the cellular receptor, dipeptidyl peptidase 4 (DPP4).
23835475	1	14	theme	syndrome	162:169	arg1	coronavirus					171:181	East respiratory syndrome coronavirus	145:181	The spike glycoprotein (S) of recently identified Middle East respiratory syndrome coronavirus (MERS-CoV)	88:192	The spike glycoprotein (S) of recently identified Middle East respiratory syndrome coronavirus (MERS-CoV) targets the cellular receptor, dipeptidyl peptidase 4 (DPP4).
23835475	1	15	gly	glycoprotein	98:109	arg1	S					112:112	S	112:112	S	112:112	The spike glycoprotein (S) of recently identified Middle East respiratory syndrome coronavirus (MERS-CoV) targets the cellular receptor, dipeptidyl peptidase 4 (DPP4).
23835475	1	15	gly	glycoprotein	98:109	arg1	glycoprotein					98:109	The spike glycoprotein	88:109	The spike glycoprotein (S) of recently identified Middle East respiratory syndrome coronavirus (MERS-CoV)	88:192	The spike glycoprotein (S) of recently identified Middle East respiratory syndrome coronavirus (MERS-CoV) targets the cellular receptor, dipeptidyl peptidase 4 (DPP4).
23835475	6	16	theme	receptor-binding	853:868	arg1	subdomain					870:878	the receptor-binding subdomain	849:878	the receptor-binding subdomain	849:878	MERS-CoV RBD and related SARS-CoV RBD share a high degree of structural similarity in their core subdomains, but are notably divergent in the receptor-binding subdomain.
23835475	3	17	theme	human	508:512	arg1	DPP4					514:517	human DPP4	508:517	human DPP4	508:517	We report the 3.0 Å-resolution crystal structure of MERS-CoV RBD bound to the extracellular domain of human DPP4.
23835475	8	18	theme	therapeutics	1217:1228	arg1	development					1202:1212	development	1202:1212	development of therapeutics and vaccines against MERS-CoV infection	1202:1268	The atomic details at the interface between MERS-CoV RBD and DPP4 provide structural understanding of the virus and receptor interaction, which can guide development of therapeutics and vaccines against MERS-CoV infection.
23835475	8	19	theme	interaction	1173:1183	arg1	understanding					1133:1145	structural understanding	1122:1145	structural understanding	1122:1145	The atomic details at the interface between MERS-CoV RBD and DPP4 provide structural understanding of the virus and receptor interaction, which can guide development of therapeutics and vaccines against MERS-CoV infection.
23835475	8	20	theme	atomic	1052:1057	arg1	details					1059:1065	The atomic details	1048:1065	The atomic details at the interface between MERS-CoV RBD and DPP4	1048:1112	The atomic details at the interface between MERS-CoV RBD and DPP4 provide structural understanding of the virus and receptor interaction, which can guide development of therapeutics and vaccines against MERS-CoV infection.
23835475	2	21	theme	viral	360:364	arg1	spike					366:370	the viral spike	356:370	the viral spike	356:370	Sequence comparison and modeling analysis have revealed a putative receptor-binding domain (RBD) on the viral spike, which mediates this interaction.
23835475	8	22	theme	receptor	1164:1171	arg1	interaction					1173:1183	the virus and receptor interaction	1150:1183	interaction	1173:1183	The atomic details at the interface between MERS-CoV RBD and DPP4 provide structural understanding of the virus and receptor interaction, which can guide development of therapeutics and vaccines against MERS-CoV infection.
23835475	6	23	theme	core	803:806	arg1	subdomains					808:817	their core subdomains	797:817	their core subdomains	797:817	MERS-CoV RBD and related SARS-CoV RBD share a high degree of structural similarity in their core subdomains, but are notably divergent in the receptor-binding subdomain.
23835475	6	24	theme	high	757:760	arg1	degree					762:767	a high degree	755:767	a high degree of structural similarity in their core subdomains	755:817	MERS-CoV RBD and related SARS-CoV RBD share a high degree of structural similarity in their core subdomains, but are notably divergent in the receptor-binding subdomain.
23835475	1	25	theme	spike	92:96	arg1	S					112:112	S	112:112	S	112:112	The spike glycoprotein (S) of recently identified Middle East respiratory syndrome coronavirus (MERS-CoV) targets the cellular receptor, dipeptidyl peptidase 4 (DPP4).
23835475	1	25	theme	spike	92:96	arg1	glycoprotein					98:109	The spike glycoprotein	88:109	The spike glycoprotein (S) of recently identified Middle East respiratory syndrome coronavirus (MERS-CoV)	88:192	The spike glycoprotein (S) of recently identified Middle East respiratory syndrome coronavirus (MERS-CoV) targets the cellular receptor, dipeptidyl peptidase 4 (DPP4).
23835475	8	26	theme	MERS-CoV	1251:1258	arg1	infection					1260:1268	MERS-CoV infection	1251:1268	MERS-CoV infection	1251:1268	The atomic details at the interface between MERS-CoV RBD and DPP4 provide structural understanding of the virus and receptor interaction, which can guide development of therapeutics and vaccines against MERS-CoV infection.
23835475	8	27	theme	vaccines	1234:1241	arg1	development					1202:1212	development	1202:1212	development of therapeutics and vaccines against MERS-CoV infection	1202:1268	The atomic details at the interface between MERS-CoV RBD and DPP4 provide structural understanding of the virus and receptor interaction, which can guide development of therapeutics and vaccines against MERS-CoV infection.
23835475	7	28	theme	several	917:923	arg1	residues					929:936	several key residues	917:936	several key residues in the receptor-binding subdomain that are critical for viral binding to DPP4 and entry into the target cell	917:1045	Mutagenesis studies have identified several key residues in the receptor-binding subdomain that are critical for viral binding to DPP4 and entry into the target cell.
23835475	6	29	theme	structural	772:781	arg1	similarity					783:792	structural similarity	772:792	structural similarity in their core subdomains	772:817	MERS-CoV RBD and related SARS-CoV RBD share a high degree of structural similarity in their core subdomains, but are notably divergent in the receptor-binding subdomain.
23835475	3	30	theme	crystal	437:443	arg1	structure					445:453	the 3.0 Å-resolution crystal structure	416:453	the 3.0 Å-resolution crystal structure of MERS-CoV RBD bound to the extracellular domain of human DPP4	416:517	We report the 3.0 Å-resolution crystal structure of MERS-CoV RBD bound to the extracellular domain of human DPP4.
23835475	0	31	theme	MERS-CoV	13:20	arg1	Structure					0:8	Structure	0:8	Structure of MERS-CoV	0:20	Structure of MERS-CoV spike receptor-binding domain complexed with human receptor DPP4.
23835475	5	32	theme	intrinsic	683:691	arg1	domain					703:708	its intrinsic hydrolase domain	679:708	DPP4 β-propeller but not its intrinsic hydrolase domain	654:708	The receptor-binding subdomain interacts with DPP4 β-propeller but not its intrinsic hydrolase domain.
23835475	2	33	theme	modeling	280:287	arg1	analysis					289:296	modeling analysis	280:296	modeling analysis	280:296	Sequence comparison and modeling analysis have revealed a putative receptor-binding domain (RBD) on the viral spike, which mediates this interaction.
23835475	6	34	theme	similarity	783:792	arg1	degree					762:767	a high degree	755:767	a high degree of structural similarity in their core subdomains	755:817	MERS-CoV RBD and related SARS-CoV RBD share a high degree of structural similarity in their core subdomains, but are notably divergent in the receptor-binding subdomain.
23835475	1	35	theme	identified	127:136	arg1	Middle					138:143	recently identified Middle	118:143	recently identified Middle	118:143	The spike glycoprotein (S) of recently identified Middle East respiratory syndrome coronavirus (MERS-CoV) targets the cellular receptor, dipeptidyl peptidase 4 (DPP4).
23835475	6	36	from	subdomains	808:817	arg1	degree					762:767	a high degree	755:767	a high degree of structural similarity in their core subdomains	755:817	MERS-CoV RBD and related SARS-CoV RBD share a high degree of structural similarity in their core subdomains, but are notably divergent in the receptor-binding subdomain.
23835475	5	37	theme	hydrolase	693:701	arg1	domain					703:708	its intrinsic hydrolase domain	679:708	DPP4 β-propeller but not its intrinsic hydrolase domain	654:708	The receptor-binding subdomain interacts with DPP4 β-propeller but not its intrinsic hydrolase domain.
23835475	7	38	theme	receptor-binding	945:960	arg1	subdomain					962:970	the receptor-binding subdomain	941:970	the receptor-binding subdomain	941:970	Mutagenesis studies have identified several key residues in the receptor-binding subdomain that are critical for viral binding to DPP4 and entry into the target cell.
23835475	0	39	theme	receptor-binding	28:43	arg1	domain					45:50	receptor-binding domain	28:50	receptor-binding domain complexed with human receptor DPP4	28:85	Structure of MERS-CoV spike receptor-binding domain complexed with human receptor DPP4.
23835475	3	40	theme	Å-resolution	424:435	arg1	structure					445:453	the 3.0 Å-resolution crystal structure	416:453	the 3.0 Å-resolution crystal structure of MERS-CoV RBD bound to the extracellular domain of human DPP4	416:517	We report the 3.0 Å-resolution crystal structure of MERS-CoV RBD bound to the extracellular domain of human DPP4.
23835475	5	41	theme	DPP4	654:657	arg1	β-propeller					659:669	DPP4 β-propeller	654:669	DPP4 β-propeller but not its intrinsic hydrolase domain	654:708	The receptor-binding subdomain interacts with DPP4 β-propeller but not its intrinsic hydrolase domain.
23835475	3	42	theme	RBD	467:469	arg1	structure					445:453	the 3.0 Å-resolution crystal structure	416:453	the 3.0 Å-resolution crystal structure of MERS-CoV RBD bound to the extracellular domain of human DPP4	416:517	We report the 3.0 Å-resolution crystal structure of MERS-CoV RBD bound to the extracellular domain of human DPP4.
23835475	7	43	theme	target	1035:1040	arg1	cell					1042:1045	the target cell	1031:1045	the target cell	1031:1045	Mutagenesis studies have identified several key residues in the receptor-binding subdomain that are critical for viral binding to DPP4 and entry into the target cell.
23835475	6	44	from	similarity	783:792	arg1	subdomains					808:817	their core subdomains	797:817	their core subdomains	797:817	MERS-CoV RBD and related SARS-CoV RBD share a high degree of structural similarity in their core subdomains, but are notably divergent in the receptor-binding subdomain.
23835475	6	45	theme	SARS-CoV	736:743	arg1	RBD					745:747	related SARS-CoV RBD	728:747	related SARS-CoV RBD	728:747	MERS-CoV RBD and related SARS-CoV RBD share a high degree of structural similarity in their core subdomains, but are notably divergent in the receptor-binding subdomain.
23835475	2	46	theme	receptor-binding	323:338	arg1	RBD					348:350	RBD	348:350	RBD	348:350	Sequence comparison and modeling analysis have revealed a putative receptor-binding domain (RBD) on the viral spike, which mediates this interaction.
23835475	2	46	theme	receptor-binding	323:338	arg1	domain					340:345	a putative receptor-binding domain	312:345	a putative receptor-binding domain (RBD)	312:351	Sequence comparison and modeling analysis have revealed a putative receptor-binding domain (RBD) on the viral spike, which mediates this interaction.
23835475	7	47	theme	key	925:927	arg1	residues					929:936	several key residues	917:936	several key residues in the receptor-binding subdomain that are critical for viral binding to DPP4 and entry into the target cell	917:1045	Mutagenesis studies have identified several key residues in the receptor-binding subdomain that are critical for viral binding to DPP4 and entry into the target cell.
23835475	6	48	theme	related	728:734	arg1	RBD					745:747	related SARS-CoV RBD	728:747	related SARS-CoV RBD	728:747	MERS-CoV RBD and related SARS-CoV RBD share a high degree of structural similarity in their core subdomains, but are notably divergent in the receptor-binding subdomain.
23835475	2	49	theme	putative	314:321	arg1	RBD					348:350	RBD	348:350	RBD	348:350	Sequence comparison and modeling analysis have revealed a putative receptor-binding domain (RBD) on the viral spike, which mediates this interaction.
23835475	2	49	theme	putative	314:321	arg1	domain					340:345	a putative receptor-binding domain	312:345	a putative receptor-binding domain (RBD)	312:351	Sequence comparison and modeling analysis have revealed a putative receptor-binding domain (RBD) on the viral spike, which mediates this interaction.
23835475	8	50	from	interface	1074:1082	arg1	details					1059:1065	The atomic details	1048:1065	The atomic details at the interface between MERS-CoV RBD and DPP4	1048:1112	The atomic details at the interface between MERS-CoV RBD and DPP4 provide structural understanding of the virus and receptor interaction, which can guide development of therapeutics and vaccines against MERS-CoV infection.
23835475	3	51	theme	MERS-CoV	458:465	arg1	RBD					467:469	MERS-CoV RBD	458:469	MERS-CoV RBD bound to the extracellular domain of human DPP4	458:517	We report the 3.0 Å-resolution crystal structure of MERS-CoV RBD bound to the extracellular domain of human DPP4.
23835475	7	52	theme	Mutagenesis	881:891	arg1	studies					893:899	Mutagenesis studies	881:899	Mutagenesis studies	881:899	Mutagenesis studies have identified several key residues in the receptor-binding subdomain that are critical for viral binding to DPP4 and entry into the target cell.
23835475	7	53	from	residues	929:936	arg1	subdomain					962:970	the receptor-binding subdomain	941:970	the receptor-binding subdomain	941:970	Mutagenesis studies have identified several key residues in the receptor-binding subdomain that are critical for viral binding to DPP4 and entry into the target cell.
23835475	0	54	theme	receptor	73:80	arg1	DPP4					82:85	human receptor DPP4	67:85	human receptor DPP4	67:85	Structure of MERS-CoV spike receptor-binding domain complexed with human receptor DPP4.
23835475	1	55	theme	cellular	206:213	arg1	receptor					215:222	the cellular receptor	202:222	the cellular receptor	202:222	The spike glycoprotein (S) of recently identified Middle East respiratory syndrome coronavirus (MERS-CoV) targets the cellular receptor, dipeptidyl peptidase 4 (DPP4).
23835475	1	55	theme	cellular	206:213	arg1	peptidase					236:244	dipeptidyl peptidase 4	225:246	dipeptidyl peptidase 4 (DPP4)	225:253	The spike glycoprotein (S) of recently identified Middle East respiratory syndrome coronavirus (MERS-CoV) targets the cellular receptor, dipeptidyl peptidase 4 (DPP4).
23835475	7	56	theme	viral	994:998	arg1	binding					1000:1006	viral binding	994:1006	viral binding to DPP4	994:1014	Mutagenesis studies have identified several key residues in the receptor-binding subdomain that are critical for viral binding to DPP4 and entry into the target cell.
23835475	1	57	dep	glycoprotein	98:109	arg1	MERS-CoV					184:191	MERS-CoV	184:191	MERS-CoV	184:191	The spike glycoprotein (S) of recently identified Middle East respiratory syndrome coronavirus (MERS-CoV) targets the cellular receptor, dipeptidyl peptidase 4 (DPP4).
23835475	1	57	dep	glycoprotein	98:109	arg1	coronavirus					171:181	East respiratory syndrome coronavirus	145:181	The spike glycoprotein (S) of recently identified Middle East respiratory syndrome coronavirus (MERS-CoV)	88:192	The spike glycoprotein (S) of recently identified Middle East respiratory syndrome coronavirus (MERS-CoV) targets the cellular receptor, dipeptidyl peptidase 4 (DPP4).
23835475	1	58	theme	dipeptidyl	225:234	arg1	receptor					215:222	the cellular receptor	202:222	the cellular receptor	202:222	The spike glycoprotein (S) of recently identified Middle East respiratory syndrome coronavirus (MERS-CoV) targets the cellular receptor, dipeptidyl peptidase 4 (DPP4).
23835475	1	58	theme	dipeptidyl	225:234	arg1	peptidase					236:244	dipeptidyl peptidase 4	225:246	dipeptidyl peptidase 4 (DPP4)	225:253	The spike glycoprotein (S) of recently identified Middle East respiratory syndrome coronavirus (MERS-CoV) targets the cellular receptor, dipeptidyl peptidase 4 (DPP4).
23835475	1	58	theme	dipeptidyl	225:234	arg1	DPP4					249:252	DPP4	249:252	DPP4	249:252	The spike glycoprotein (S) of recently identified Middle East respiratory syndrome coronavirus (MERS-CoV) targets the cellular receptor, dipeptidyl peptidase 4 (DPP4).
23835475	0	59	theme	human	67:71	arg1	DPP4					82:85	human receptor DPP4	67:85	human receptor DPP4	67:85	Structure of MERS-CoV spike receptor-binding domain complexed with human receptor DPP4.
23835475	6	60	from	divergent	836:844	arg1	subdomain					870:878	the receptor-binding subdomain	849:878	the receptor-binding subdomain	849:878	MERS-CoV RBD and related SARS-CoV RBD share a high degree of structural similarity in their core subdomains, but are notably divergent in the receptor-binding subdomain.
23835475	6	61	theme	MERS-CoV	711:718	arg1	RBD					720:722	MERS-CoV RBD	711:722	MERS-CoV RBD	711:722	MERS-CoV RBD and related SARS-CoV RBD share a high degree of structural similarity in their core subdomains, but are notably divergent in the receptor-binding subdomain.
23835475	1	62	theme	Middle	138:143	arg1	S					112:112	S	112:112	S	112:112	The spike glycoprotein (S) of recently identified Middle East respiratory syndrome coronavirus (MERS-CoV) targets the cellular receptor, dipeptidyl peptidase 4 (DPP4).
23835475	1	62	theme	Middle	138:143	arg1	glycoprotein					98:109	The spike glycoprotein	88:109	The spike glycoprotein (S) of recently identified Middle East respiratory syndrome coronavirus (MERS-CoV)	88:192	The spike glycoprotein (S) of recently identified Middle East respiratory syndrome coronavirus (MERS-CoV) targets the cellular receptor, dipeptidyl peptidase 4 (DPP4).
30765606	0	0	theme	animal	74:79	arg1	toxins					81:86	animal toxins	74:86	animal toxins	74:86	Structures of human Nav1.7 channel in complex with auxiliary subunits and animal toxins.
30765606	5	1	theme	mechanistic	847:857	arg1	understanding					859:871	mechanistic understanding	847:871	mechanistic understanding of the function and disease of Nav1.7	847:909	The structures illuminate the path toward mechanistic understanding of the function and disease of Nav1.7 and establish the foundation for structure-aided development of analgesics.
30765606	1	2	theme	pain	159:162	arg1	relief					164:169	pain relief	159:169	pain relief	159:169	Voltage-gated sodium channel Nav1.7 represents a promising target for pain relief.
30765606	0	3	from	Structures	0:9	arg1	complex					38:44	complex	38:44	complex with auxiliary subunits and animal toxins	38:86	Structures of human Nav1.7 channel in complex with auxiliary subunits and animal toxins.
30765606	2	4	theme	pore	290:293	arg1	blockers					295:302	pore blockers	290:302	pore blockers	290:302	Here we report the cryo-electron microscopy structures of the human Nav1.7-β1-β2 complex bound to two combinations of pore blockers and gating modifier toxins (GMTs), tetrodotoxin with protoxin-II and saxitoxin with huwentoxin-IV, both determined at overall resolutions of 3.2 angstroms.
30765606	2	5	theme	blockers	295:302	arg1	combinations					274:285	two combinations	270:285	two combinations of pore blockers and gating modifier toxins (GMTs)	270:336	Here we report the cryo-electron microscopy structures of the human Nav1.7-β1-β2 complex bound to two combinations of pore blockers and gating modifier toxins (GMTs), tetrodotoxin with protoxin-II and saxitoxin with huwentoxin-IV, both determined at overall resolutions of 3.2 angstroms.
30765606	5	6	theme	disease	893:899	arg1	understanding					859:871	mechanistic understanding	847:871	mechanistic understanding of the function and disease of Nav1.7	847:909	The structures illuminate the path toward mechanistic understanding of the function and disease of Nav1.7 and establish the foundation for structure-aided development of analgesics.
30765606	4	7	theme	gate	792:795	arg1	closed					797:802	the intracellular gate closed	774:802	the intracellular gate closed	774:802	One additional protoxin-II sits on top of the S3-S4 linker in VSDIV The structures may represent an inactivated state with all four VSDs "up" and the intracellular gate closed.
30765606	4	8	theme	additional	632:641	arg1	protoxin-II					643:653	One additional protoxin-II	628:653	One additional protoxin-II	628:653	One additional protoxin-II sits on top of the S3-S4 linker in VSDIV The structures may represent an inactivated state with all four VSDs "up" and the intracellular gate closed.
30765606	4	9	theme	intracellular	778:790	arg1	closed					797:802	the intracellular gate closed	774:802	the intracellular gate closed	774:802	One additional protoxin-II sits on top of the S3-S4 linker in VSDIV The structures may represent an inactivated state with all four VSDs "up" and the intracellular gate closed.
30765606	3	10	theme	voltage-sensing	527:541	arg1	domain					543:548	voltage-sensing domain II	527:551	voltage-sensing domain II (VSDII)	527:559	The two structures are nearly identical except for minor shifts of voltage-sensing domain II (VSDII), whose S3-S4 linker accommodates the two GMTs in a similar manner.
30765606	3	10	theme	voltage-sensing	527:541	arg1	VSDII					554:558	VSDII	554:558	VSDII	554:558	The two structures are nearly identical except for minor shifts of voltage-sensing domain II (VSDII), whose S3-S4 linker accommodates the two GMTs in a similar manner.
30765606	4	11	dep	VSDs	760:763	arg1	closed					797:802	the intracellular gate closed	774:802	the intracellular gate closed	774:802	One additional protoxin-II sits on top of the S3-S4 linker in VSDIV The structures may represent an inactivated state with all four VSDs "up" and the intracellular gate closed.
30765606	4	11	dep	VSDs	760:763	arg1	"					768:768	"up"	765:768	"up"	765:768	One additional protoxin-II sits on top of the S3-S4 linker in VSDIV The structures may represent an inactivated state with all four VSDs "up" and the intracellular gate closed.
30765606	2	12	theme	overall	422:428	arg1	resolutions					430:440	overall resolutions	422:440	overall resolutions of 3.2 angstroms	422:457	Here we report the cryo-electron microscopy structures of the human Nav1.7-β1-β2 complex bound to two combinations of pore blockers and gating modifier toxins (GMTs), tetrodotoxin with protoxin-II and saxitoxin with huwentoxin-IV, both determined at overall resolutions of 3.2 angstroms.
30765606	2	13	theme	modifier	315:322	arg1	GMTs					332:335	GMTs	332:335	GMTs	332:335	Here we report the cryo-electron microscopy structures of the human Nav1.7-β1-β2 complex bound to two combinations of pore blockers and gating modifier toxins (GMTs), tetrodotoxin with protoxin-II and saxitoxin with huwentoxin-IV, both determined at overall resolutions of 3.2 angstroms.
30765606	2	13	theme	modifier	315:322	arg1	toxins					324:329	gating modifier toxins	308:329	gating modifier toxins (GMTs)	308:336	Here we report the cryo-electron microscopy structures of the human Nav1.7-β1-β2 complex bound to two combinations of pore blockers and gating modifier toxins (GMTs), tetrodotoxin with protoxin-II and saxitoxin with huwentoxin-IV, both determined at overall resolutions of 3.2 angstroms.
30765606	2	14	theme	gating	308:313	arg1	GMTs					332:335	GMTs	332:335	GMTs	332:335	Here we report the cryo-electron microscopy structures of the human Nav1.7-β1-β2 complex bound to two combinations of pore blockers and gating modifier toxins (GMTs), tetrodotoxin with protoxin-II and saxitoxin with huwentoxin-IV, both determined at overall resolutions of 3.2 angstroms.
30765606	2	14	theme	gating	308:313	arg1	toxins					324:329	gating modifier toxins	308:329	gating modifier toxins (GMTs)	308:336	Here we report the cryo-electron microscopy structures of the human Nav1.7-β1-β2 complex bound to two combinations of pore blockers and gating modifier toxins (GMTs), tetrodotoxin with protoxin-II and saxitoxin with huwentoxin-IV, both determined at overall resolutions of 3.2 angstroms.
30765606	4	15	theme	inactivated	728:738	arg1	state					740:744	an inactivated state	725:744	an inactivated state with all four VSDs "up" and the intracellular gate closed	725:802	One additional protoxin-II sits on top of the S3-S4 linker in VSDIV The structures may represent an inactivated state with all four VSDs "up" and the intracellular gate closed.
30765606	0	16	theme	Nav1.7	20:25	arg1	channel					27:33	human Nav1.7 channel	14:33	human Nav1.7 channel	14:33	Structures of human Nav1.7 channel in complex with auxiliary subunits and animal toxins.
30765606	4	17	with	state	740:744	arg1	VSDs					760:763	all four VSDs	751:763	all four VSDs "up" and the intracellular gate closed	751:802	One additional protoxin-II sits on top of the S3-S4 linker in VSDIV The structures may represent an inactivated state with all four VSDs "up" and the intracellular gate closed.
30765606	1	18	theme	Voltage-gated	89:101	arg1	channel					110:116	Voltage-gated sodium channel Nav1.7	89:123	Voltage-gated sodium channel Nav1.7	89:123	Voltage-gated sodium channel Nav1.7 represents a promising target for pain relief.
30765606	0	19	theme	human	14:18	arg1	channel					27:33	human Nav1.7 channel	14:33	human Nav1.7 channel	14:33	Structures of human Nav1.7 channel in complex with auxiliary subunits and animal toxins.
30765606	1	20	theme	sodium	103:108	arg1	channel					110:116	Voltage-gated sodium channel Nav1.7	89:123	Voltage-gated sodium channel Nav1.7	89:123	Voltage-gated sodium channel Nav1.7 represents a promising target for pain relief.
30765606	3	21	theme	minor	511:515	arg1	shifts					517:522	minor shifts	511:522	minor shifts	511:522	The two structures are nearly identical except for minor shifts of voltage-sensing domain II (VSDII), whose S3-S4 linker accommodates the two GMTs in a similar manner.
30765606	2	22	theme	human	234:238	arg1	complex					253:259	the human Nav1.7-β1-β2 complex	230:259	the human Nav1.7-β1-β2 complex bound to two combinations of pore blockers and gating modifier toxins (GMTs)	230:336	Here we report the cryo-electron microscopy structures of the human Nav1.7-β1-β2 complex bound to two combinations of pore blockers and gating modifier toxins (GMTs), tetrodotoxin with protoxin-II and saxitoxin with huwentoxin-IV, both determined at overall resolutions of 3.2 angstroms.
30765606	0	23	theme	channel	27:33	arg1	Structures					0:9	Structures	0:9	Structures of human Nav1.7 channel in complex with auxiliary subunits and animal toxins.	0:87	Structures of human Nav1.7 channel in complex with auxiliary subunits and animal toxins.
30765606	4	24	theme	up	766:767	arg1	"					768:768	"up"	765:768	"up"	765:768	One additional protoxin-II sits on top of the S3-S4 linker in VSDIV The structures may represent an inactivated state with all four VSDs "up" and the intracellular gate closed.
30765606	5	25	dep	function	880:887	arg1	the					876:878	the	876:878	the	876:878	The structures illuminate the path toward mechanistic understanding of the function and disease of Nav1.7 and establish the foundation for structure-aided development of analgesics.
30765606	3	26	theme	similar	612:618	arg1	manner					620:625	a similar manner	610:625	a similar manner	610:625	The two structures are nearly identical except for minor shifts of voltage-sensing domain II (VSDII), whose S3-S4 linker accommodates the two GMTs in a similar manner.
30765606	2	27	theme	angstroms	449:457	arg1	resolutions					430:440	overall resolutions	422:440	overall resolutions of 3.2 angstroms	422:457	Here we report the cryo-electron microscopy structures of the human Nav1.7-β1-β2 complex bound to two combinations of pore blockers and gating modifier toxins (GMTs), tetrodotoxin with protoxin-II and saxitoxin with huwentoxin-IV, both determined at overall resolutions of 3.2 angstroms.
30765606	2	28	theme	microscopy	205:214	arg1	structures					216:225	the cryo-electron microscopy structures	187:225	the cryo-electron microscopy structures of the human Nav1.7-β1-β2 complex bound to two combinations of pore blockers and gating modifier toxins (GMTs)	187:336	Here we report the cryo-electron microscopy structures of the human Nav1.7-β1-β2 complex bound to two combinations of pore blockers and gating modifier toxins (GMTs), tetrodotoxin with protoxin-II and saxitoxin with huwentoxin-IV, both determined at overall resolutions of 3.2 angstroms.
30765606	3	29	theme	S3-S4	568:572	arg1	linker					574:579	linker	574:579	linker	574:579	The two structures are nearly identical except for minor shifts of voltage-sensing domain II (VSDII), whose S3-S4 linker accommodates the two GMTs in a similar manner.
30765606	4	30	theme	S3-S4	674:678	arg1	linker					680:685	the S3-S4 linker	670:685	the S3-S4 linker	670:685	One additional protoxin-II sits on top of the S3-S4 linker in VSDIV The structures may represent an inactivated state with all four VSDs "up" and the intracellular gate closed.
30765606	5	31	theme	analgesics	975:984	arg1	development					960:970	structure-aided development	944:970	structure-aided development of analgesics	944:984	The structures illuminate the path toward mechanistic understanding of the function and disease of Nav1.7 and establish the foundation for structure-aided development of analgesics.
30765606	2	32	theme	cryo-electron	191:203	arg1	microscopy					205:214	cryo-electron microscopy	191:214	the cryo-electron microscopy structures of the human Nav1.7-β1-β2 complex bound to two combinations of pore blockers and gating modifier toxins (GMTs)	187:336	Here we report the cryo-electron microscopy structures of the human Nav1.7-β1-β2 complex bound to two combinations of pore blockers and gating modifier toxins (GMTs), tetrodotoxin with protoxin-II and saxitoxin with huwentoxin-IV, both determined at overall resolutions of 3.2 angstroms.
30765606	5	33	theme	structure-aided	944:958	arg1	development					960:970	structure-aided development	944:970	structure-aided development of analgesics	944:984	The structures illuminate the path toward mechanistic understanding of the function and disease of Nav1.7 and establish the foundation for structure-aided development of analgesics.
30765606	5	34	theme	function	880:887	arg1	understanding					859:871	mechanistic understanding	847:871	mechanistic understanding of the function and disease of Nav1.7	847:909	The structures illuminate the path toward mechanistic understanding of the function and disease of Nav1.7 and establish the foundation for structure-aided development of analgesics.
30765606	5	35	theme	Nav1.7	904:909	arg1	disease					893:899	disease	893:899	disease	893:899	The structures illuminate the path toward mechanistic understanding of the function and disease of Nav1.7 and establish the foundation for structure-aided development of analgesics.
30765606	5	35	theme	Nav1.7	904:909	arg1	function					880:887	function	880:887	function	880:887	The structures illuminate the path toward mechanistic understanding of the function and disease of Nav1.7 and establish the foundation for structure-aided development of analgesics.
30765606	3	36	theme	domain	543:548	arg1	shifts					517:522	minor shifts	511:522	minor shifts	511:522	The two structures are nearly identical except for minor shifts of voltage-sensing domain II (VSDII), whose S3-S4 linker accommodates the two GMTs in a similar manner.
30765606	2	37	theme	toxins	324:329	arg1	combinations					274:285	two combinations	270:285	two combinations of pore blockers and gating modifier toxins (GMTs)	270:336	Here we report the cryo-electron microscopy structures of the human Nav1.7-β1-β2 complex bound to two combinations of pore blockers and gating modifier toxins (GMTs), tetrodotoxin with protoxin-II and saxitoxin with huwentoxin-IV, both determined at overall resolutions of 3.2 angstroms.
30765606	4	38	from	linker	680:685	arg1	VSDIV					690:694	VSDIV	690:694	VSDIV	690:694	One additional protoxin-II sits on top of the S3-S4 linker in VSDIV The structures may represent an inactivated state with all four VSDs "up" and the intracellular gate closed.
30765606	2	39	dep	report	180:185	arg1	both					403:406	both	403:406	both	403:406	Here we report the cryo-electron microscopy structures of the human Nav1.7-β1-β2 complex bound to two combinations of pore blockers and gating modifier toxins (GMTs), tetrodotoxin with protoxin-II and saxitoxin with huwentoxin-IV, both determined at overall resolutions of 3.2 angstroms.
30765606	2	40	theme	complex	253:259	arg1	structures					216:225	the cryo-electron microscopy structures	187:225	the cryo-electron microscopy structures of the human Nav1.7-β1-β2 complex bound to two combinations of pore blockers and gating modifier toxins (GMTs)	187:336	Here we report the cryo-electron microscopy structures of the human Nav1.7-β1-β2 complex bound to two combinations of pore blockers and gating modifier toxins (GMTs), tetrodotoxin with protoxin-II and saxitoxin with huwentoxin-IV, both determined at overall resolutions of 3.2 angstroms.
30765606	0	41	with	complex	38:44	arg1	subunits					61:68	auxiliary subunits	51:68	auxiliary subunits	51:68	Structures of human Nav1.7 channel in complex with auxiliary subunits and animal toxins.
30765606	0	41	with	complex	38:44	arg1	toxins					81:86	animal toxins	74:86	animal toxins	74:86	Structures of human Nav1.7 channel in complex with auxiliary subunits and animal toxins.
30765606	1	42	theme	promising	138:146	arg1	target					148:153	a promising target	136:153	a promising target for pain relief	136:169	Voltage-gated sodium channel Nav1.7 represents a promising target for pain relief.
30765606	0	43	theme	auxiliary	51:59	arg1	subunits					61:68	auxiliary subunits	51:68	auxiliary subunits	51:68	Structures of human Nav1.7 channel in complex with auxiliary subunits and animal toxins.
30765606	2	44	theme	Nav1.7-β1-β2	240:251	arg1	complex					253:259	the human Nav1.7-β1-β2 complex	230:259	the human Nav1.7-β1-β2 complex bound to two combinations of pore blockers and gating modifier toxins (GMTs)	230:336	Here we report the cryo-electron microscopy structures of the human Nav1.7-β1-β2 complex bound to two combinations of pore blockers and gating modifier toxins (GMTs), tetrodotoxin with protoxin-II and saxitoxin with huwentoxin-IV, both determined at overall resolutions of 3.2 angstroms.
31507604	0	0	theme	Complement	87:96	arg1	System					98:103	the Human Complement System	77:103	the Human Complement System	77:103	Structural Basis for Properdin Oligomerization and Convertase Stimulation in the Human Complement System.
31507604	9	1	theme	thrombospondin	1225:1238	arg1	repeats					1240:1246	thrombospondin repeats	1225:1246	thrombospondin repeats	1225:1246	Flexibility at four hinges between thrombospondin repeats is suggested to enable the oligomeric, polydisperse, and extended architecture of FP.
31507604	9	2	theme	oligomeric	1275:1284	arg1	architecture					1314:1325	the oligomeric, polydisperse, and extended architecture	1271:1325	the oligomeric, polydisperse, and extended architecture of FP	1271:1331	Flexibility at four hinges between thrombospondin repeats is suggested to enable the oligomeric, polydisperse, and extended architecture of FP.
31507604	4	3	theme	FP	643:644	arg1	TSR5					646:649	FP TSR5	643:649	FP TSR5	643:649	Stabilization of the interaction between the C3b C-terminus and the MIDAS bound Mg2+ in the Bb protease by FP TSR5 is proposed to underlie FP convertase stabilization.
31507604	9	4	theme	extended	1305:1312	arg1	architecture					1314:1325	the oligomeric, polydisperse, and extended architecture	1271:1325	the oligomeric, polydisperse, and extended architecture of FP	1271:1331	Flexibility at four hinges between thrombospondin repeats is suggested to enable the oligomeric, polydisperse, and extended architecture of FP.
31507604	0	5	theme	Human	81:85	arg1	System					98:103	the Human Complement System	77:103	the Human Complement System	77:103	Structural Basis for Properdin Oligomerization and Convertase Stimulation in the Human Complement System.
31507604	0	6	from	Basis	11:15	arg1	System					98:103	the Human Complement System	77:103	the Human Complement System	77:103	Structural Basis for Properdin Oligomerization and Convertase Stimulation in the Human Complement System.
31507604	8	7	theme	largest	1113:1119	arg1	interface					1121:1129	The second and largest interface	1098:1129	interface	1121:1129	The second and largest interface is formed by TSR1 and TSR6 from the same two FP molecules.
31507604	2	8	theme	FP	336:337	arg1	structures					322:331	two crystal structures	310:331	two crystal structures of FP	310:337	Here we present two crystal structures of FP and two structures of convertase bound FP.
31507604	2	8	theme	FP	336:337	arg1	structures					347:356	two structures	343:356	two structures of convertase bound FP	343:379	Here we present two crystal structures of FP and two structures of convertase bound FP.
31507604	4	9	from	protease	631:638	arg1	Stabilization					536:548	Stabilization	536:548	Stabilization of the interaction between the C3b C-terminus and the MIDAS bound Mg2+ in the Bb protease by FP TSR5	536:649	Stabilization of the interaction between the C3b C-terminus and the MIDAS bound Mg2+ in the Bb protease by FP TSR5 is proposed to underlie FP convertase stabilization.
31507604	7	10	theme	FP	1063:1064	arg1	molecule					1066:1073	one FP molecule	1059:1073	one FP molecule	1059:1073	FP oligomers are held together by two sets of intermolecular contacts, where the first is formed by the TB domain from one FP molecule and TSR4 from another.
31507604	6	11	theme	C3b	856:858	arg1	degradation					860:870	C3b degradation	856:870	C3b degradation	856:870	FP is shown to inhibit C3b degradation by FI due to a direct competition for a common binding site on C3b.
31507604	10	12	theme	FP	1469:1470	arg1	function					1472:1479	FP function	1469:1479	FP function in convertases	1469:1494	Our structures rationalize the effects of mutations associated with FP deficiencies and provide a structural basis for the analysis of FP function in convertases and its possible role in pattern recognition.
31507604	4	13	theme	Mg2+	616:619	arg1	Stabilization					536:548	Stabilization	536:548	Stabilization of the interaction between the C3b C-terminus and the MIDAS bound Mg2+ in the Bb protease by FP TSR5	536:649	Stabilization of the interaction between the C3b C-terminus and the MIDAS bound Mg2+ in the Bb protease by FP TSR5 is proposed to underlie FP convertase stabilization.
31507604	1	14	theme	alternative	248:258	arg1	pathway					260:266	the alternative pathway	244:266	the alternative pathway of the complement system	244:291	Properdin (FP) is a positive regulator of the immune system stimulating the activity of the proteolytically active C3 convertase C3bBb in the alternative pathway of the complement system.
31507604	10	15	from	convertases	1484:1494	arg1	analysis					1457:1464	the analysis	1453:1464	the analysis of FP function in convertases and its possible role in pattern recognition	1453:1539	Our structures rationalize the effects of mutations associated with FP deficiencies and provide a structural basis for the analysis of FP function in convertases and its possible role in pattern recognition.
31507604	6	16	theme	binding	919:925	arg1	site					927:930	a common binding site	910:930	a common binding site on C3b	910:937	FP is shown to inhibit C3b degradation by FI due to a direct competition for a common binding site on C3b.
31507604	10	17	theme	possible	1504:1511	arg1	role					1513:1516	its possible role	1500:1516	its possible role in pattern recognition	1500:1539	Our structures rationalize the effects of mutations associated with FP deficiencies and provide a structural basis for the analysis of FP function in convertases and its possible role in pattern recognition.
31507604	5	18	theme	binding	812:818	arg1	experiments					820:830	binding experiments	812:830	binding experiments	812:830	Intermolecular contacts between FP and the convertase subunits suggested by the structure were confirmed by binding experiments.
31507604	4	19	from	Stabilization	536:548	arg1	protease					631:638	the Bb protease	624:638	the Bb protease	624:638	Stabilization of the interaction between the C3b C-terminus and the MIDAS bound Mg2+ in the Bb protease by FP TSR5 is proposed to underlie FP convertase stabilization.
31507604	7	20	from	molecule	1066:1073	arg1	domain					1047:1052	the TB domain	1040:1052	the TB domain from one FP molecule	1040:1073	FP oligomers are held together by two sets of intermolecular contacts, where the first is formed by the TB domain from one FP molecule and TSR4 from another.
31507604	7	20	from	molecule	1066:1073	arg1	TSR4					1079:1082	TSR4	1079:1082	TSR4 from another	1079:1095	FP oligomers are held together by two sets of intermolecular contacts, where the first is formed by the TB domain from one FP molecule and TSR4 from another.
31507604	6	21	from	site	927:930	arg1	C3b					935:937	C3b	935:937	C3b	935:937	FP is shown to inhibit C3b degradation by FI due to a direct competition for a common binding site on C3b.
31507604	10	22	from	role	1513:1516	arg1	convertases					1484:1494	convertases	1484:1494	convertases	1484:1494	Our structures rationalize the effects of mutations associated with FP deficiencies and provide a structural basis for the analysis of FP function in convertases and its possible role in pattern recognition.
31507604	10	22	from	role	1513:1516	arg1	recognition					1529:1539	pattern recognition	1521:1539	pattern recognition	1521:1539	Our structures rationalize the effects of mutations associated with FP deficiencies and provide a structural basis for the analysis of FP function in convertases and its possible role in pattern recognition.
31507604	1	23	theme	immune	152:157	arg1	system					159:164	the immune system	148:164	the immune system stimulating the activity of the proteolytically active C3 convertase C3bBb in the alternative pathway of the complement system	148:291	Properdin (FP) is a positive regulator of the immune system stimulating the activity of the proteolytically active C3 convertase C3bBb in the alternative pathway of the complement system.
31507604	5	24	theme	convertase	747:756	arg1	subunits					758:765	the convertase subunits	743:765	the convertase subunits suggested by the structure	743:792	Intermolecular contacts between FP and the convertase subunits suggested by the structure were confirmed by binding experiments.
31507604	4	25	theme	interaction	557:567	arg1	Stabilization					536:548	Stabilization	536:548	Stabilization of the interaction between the C3b C-terminus and the MIDAS bound Mg2+ in the Bb protease by FP TSR5	536:649	Stabilization of the interaction between the C3b C-terminus and the MIDAS bound Mg2+ in the Bb protease by FP TSR5 is proposed to underlie FP convertase stabilization.
31507604	4	26	from	Mg2+	616:619	arg1	protease					631:638	the Bb protease	624:638	the Bb protease	624:638	Stabilization of the interaction between the C3b C-terminus and the MIDAS bound Mg2+ in the Bb protease by FP TSR5 is proposed to underlie FP convertase stabilization.
31507604	1	27	theme	system	159:164	arg1	regulator					135:143	a positive regulator	124:143	a positive regulator of the immune system stimulating the activity of the proteolytically active C3 convertase C3bBb in the alternative pathway of the complement system	124:291	Properdin (FP) is a positive regulator of the immune system stimulating the activity of the proteolytically active C3 convertase C3bBb in the alternative pathway of the complement system.
31507604	1	27	theme	system	159:164	arg1	Properdin					106:114	Properdin	106:114	Properdin (FP)	106:119	Properdin (FP) is a positive regulator of the immune system stimulating the activity of the proteolytically active C3 convertase C3bBb in the alternative pathway of the complement system.
31507604	4	28	from	interaction	557:567	arg1	protease					631:638	the Bb protease	624:638	the Bb protease	624:638	Stabilization of the interaction between the C3b C-terminus and the MIDAS bound Mg2+ in the Bb protease by FP TSR5 is proposed to underlie FP convertase stabilization.
31507604	9	29	from	hinges	1210:1215	arg1	Flexibility					1190:1200	Flexibility	1190:1200	Flexibility at four hinges between thrombospondin repeats	1190:1246	Flexibility at four hinges between thrombospondin repeats is suggested to enable the oligomeric, polydisperse, and extended architecture of FP.
31507604	4	30	theme	bound	610:614	arg1	Mg2+					616:619	the MIDAS bound Mg2+	600:619	the MIDAS bound Mg2+ in the Bb protease	600:638	Stabilization of the interaction between the C3b C-terminus and the MIDAS bound Mg2+ in the Bb protease by FP TSR5 is proposed to underlie FP convertase stabilization.
31507604	4	31	theme	FP	675:676	arg1	stabilization					689:701	FP convertase stabilization	675:701	FP convertase stabilization	675:701	Stabilization of the interaction between the C3b C-terminus and the MIDAS bound Mg2+ in the Bb protease by FP TSR5 is proposed to underlie FP convertase stabilization.
31507604	2	32	theme	convertase	361:370	arg1	FP					378:379	convertase bound FP	361:379	convertase bound FP	361:379	Here we present two crystal structures of FP and two structures of convertase bound FP.
31507604	0	33	theme	Structural	0:9	arg1	Basis					11:15	Structural Basis	0:15	Structural Basis for Properdin Oligomerization and Convertase Stimulation in the Human Complement System.	0:104	Structural Basis for Properdin Oligomerization and Convertase Stimulation in the Human Complement System.
31507604	6	34	theme	common	912:917	arg1	site					927:930	a common binding site	910:930	a common binding site on C3b	910:937	FP is shown to inhibit C3b degradation by FI due to a direct competition for a common binding site on C3b.
31507604	10	35	from	analysis	1457:1464	arg1	convertases					1484:1494	convertases	1484:1494	convertases	1484:1494	Our structures rationalize the effects of mutations associated with FP deficiencies and provide a structural basis for the analysis of FP function in convertases and its possible role in pattern recognition.
31507604	10	35	from	analysis	1457:1464	arg1	recognition					1529:1539	pattern recognition	1521:1539	pattern recognition	1521:1539	Our structures rationalize the effects of mutations associated with FP deficiencies and provide a structural basis for the analysis of FP function in convertases and its possible role in pattern recognition.
31507604	10	36	theme	pattern	1521:1527	arg1	recognition					1529:1539	pattern recognition	1521:1539	pattern recognition	1521:1539	Our structures rationalize the effects of mutations associated with FP deficiencies and provide a structural basis for the analysis of FP function in convertases and its possible role in pattern recognition.
31507604	0	37	theme	Properdin	21:29	arg1	Oligomerization					31:45	Properdin Oligomerization	21:45	Properdin Oligomerization	21:45	Structural Basis for Properdin Oligomerization and Convertase Stimulation in the Human Complement System.
31507604	7	38	theme	intermolecular	986:999	arg1	contacts					1001:1008	intermolecular contacts	986:1008	intermolecular contacts	986:1008	FP oligomers are held together by two sets of intermolecular contacts, where the first is formed by the TB domain from one FP molecule and TSR4 from another.
31507604	10	39	theme	function	1472:1479	arg1	analysis					1457:1464	the analysis	1453:1464	the analysis of FP function in convertases and its possible role in pattern recognition	1453:1539	Our structures rationalize the effects of mutations associated with FP deficiencies and provide a structural basis for the analysis of FP function in convertases and its possible role in pattern recognition.
31507604	1	40	theme	complement	275:284	arg1	system					286:291	the complement system	271:291	the complement system	271:291	Properdin (FP) is a positive regulator of the immune system stimulating the activity of the proteolytically active C3 convertase C3bBb in the alternative pathway of the complement system.
31507604	7	41	theme	contacts	1001:1008	arg1	sets					978:981	two sets	974:981	two sets of intermolecular contacts, where the first is formed by the TB domain from one FP molecule and TSR4 from another	974:1095	FP oligomers are held together by two sets of intermolecular contacts, where the first is formed by the TB domain from one FP molecule and TSR4 from another.
31507604	7	41	theme	contacts	1001:1008	arg1	contacts					1001:1008	intermolecular contacts	986:1008	intermolecular contacts	986:1008	FP oligomers are held together by two sets of intermolecular contacts, where the first is formed by the TB domain from one FP molecule and TSR4 from another.
31507604	4	42	theme	convertase	678:687	arg1	stabilization					689:701	FP convertase stabilization	675:701	FP convertase stabilization	675:701	Stabilization of the interaction between the C3b C-terminus and the MIDAS bound Mg2+ in the Bb protease by FP TSR5 is proposed to underlie FP convertase stabilization.
31507604	3	43	theme	convertase	474:483	arg1	site					493:496	the convertase binding site	470:496	the convertase binding site in FP that mainly interacts with C3b	470:533	A structural core formed by three thrombospondin repeats (TSRs) and a TB domain harbors the convertase binding site in FP that mainly interacts with C3b.
31507604	3	44	theme	structural	384:393	arg1	core					395:398	A structural core	382:398	A structural core formed by three thrombospondin repeats (TSRs) and a TB domain	382:460	A structural core formed by three thrombospondin repeats (TSRs) and a TB domain harbors the convertase binding site in FP that mainly interacts with C3b.
31507604	1	45	theme	system	286:291	arg1	pathway					260:266	the alternative pathway	244:266	the alternative pathway of the complement system	244:291	Properdin (FP) is a positive regulator of the immune system stimulating the activity of the proteolytically active C3 convertase C3bBb in the alternative pathway of the complement system.
31507604	10	46	theme	mutations	1376:1384	arg1	effects					1365:1371	the effects	1361:1371	the effects of mutations associated with FP deficiencies	1361:1416	Our structures rationalize the effects of mutations associated with FP deficiencies and provide a structural basis for the analysis of FP function in convertases and its possible role in pattern recognition.
31507604	7	47	from	another	1089:1095	arg1	domain					1047:1052	the TB domain	1040:1052	the TB domain from one FP molecule	1040:1073	FP oligomers are held together by two sets of intermolecular contacts, where the first is formed by the TB domain from one FP molecule and TSR4 from another.
31507604	7	47	from	another	1089:1095	arg1	TSR4					1079:1082	TSR4	1079:1082	TSR4 from another	1079:1095	FP oligomers are held together by two sets of intermolecular contacts, where the first is formed by the TB domain from one FP molecule and TSR4 from another.
31507604	4	48	theme	MIDAS	604:608	arg1	Mg2+					616:619	the MIDAS bound Mg2+	600:619	the MIDAS bound Mg2+ in the Bb protease	600:638	Stabilization of the interaction between the C3b C-terminus and the MIDAS bound Mg2+ in the Bb protease by FP TSR5 is proposed to underlie FP convertase stabilization.
31507604	2	49	theme	FP	378:379	arg1	structures					322:331	two crystal structures	310:331	two crystal structures of FP	310:337	Here we present two crystal structures of FP and two structures of convertase bound FP.
31507604	2	49	theme	FP	378:379	arg1	structures					347:356	two structures	343:356	two structures of convertase bound FP	343:379	Here we present two crystal structures of FP and two structures of convertase bound FP.
31507604	6	50	theme	direct	887:892	arg1	competition					894:904	a direct competition	885:904	a direct competition for a common binding site on C3b	885:937	FP is shown to inhibit C3b degradation by FI due to a direct competition for a common binding site on C3b.
31507604	8	51	theme	second	1102:1107	arg1	interface					1121:1129	The second and largest interface	1098:1129	interface	1121:1129	The second and largest interface is formed by TSR1 and TSR6 from the same two FP molecules.
31507604	4	52	theme	C3b	581:583	arg1	C-terminus					585:594	the C3b C-terminus	577:594	the C3b C-terminus	577:594	Stabilization of the interaction between the C3b C-terminus and the MIDAS bound Mg2+ in the Bb protease by FP TSR5 is proposed to underlie FP convertase stabilization.
31507604	10	53	from	recognition	1529:1539	arg1	analysis					1457:1464	the analysis	1453:1464	the analysis of FP function in convertases and its possible role in pattern recognition	1453:1539	Our structures rationalize the effects of mutations associated with FP deficiencies and provide a structural basis for the analysis of FP function in convertases and its possible role in pattern recognition.
31507604	8	54	theme	FP	1176:1177	arg1	molecules					1179:1187	the same two FP molecules	1163:1187	the same two FP molecules	1163:1187	The second and largest interface is formed by TSR1 and TSR6 from the same two FP molecules.
31507604	7	55	theme	TB	1044:1045	arg1	domain					1047:1052	the TB domain	1040:1052	the TB domain from one FP molecule	1040:1073	FP oligomers are held together by two sets of intermolecular contacts, where the first is formed by the TB domain from one FP molecule and TSR4 from another.
31507604	9	56	theme	FP	1330:1331	arg1	architecture					1314:1325	the oligomeric, polydisperse, and extended architecture	1271:1325	the oligomeric, polydisperse, and extended architecture of FP	1271:1331	Flexibility at four hinges between thrombospondin repeats is suggested to enable the oligomeric, polydisperse, and extended architecture of FP.
31507604	3	57	theme	TB	452:453	arg1	domain					455:460	a TB domain	450:460	a TB domain	450:460	A structural core formed by three thrombospondin repeats (TSRs) and a TB domain harbors the convertase binding site in FP that mainly interacts with C3b.
31507604	0	58	theme	Convertase	51:60	arg1	Stimulation					62:72	Convertase Stimulation	51:72	Convertase Stimulation	51:72	Structural Basis for Properdin Oligomerization and Convertase Stimulation in the Human Complement System.
31507604	10	59	theme	structural	1432:1441	arg1	basis					1443:1447	a structural basis	1430:1447	a structural basis for the analysis of FP function in convertases and its possible role in pattern recognition	1430:1539	Our structures rationalize the effects of mutations associated with FP deficiencies and provide a structural basis for the analysis of FP function in convertases and its possible role in pattern recognition.
31507604	1	60	from	activity	182:189	arg1	pathway					260:266	the alternative pathway	244:266	the alternative pathway of the complement system	244:291	Properdin (FP) is a positive regulator of the immune system stimulating the activity of the proteolytically active C3 convertase C3bBb in the alternative pathway of the complement system.
31507604	8	61	theme	same	1167:1170	arg1	molecules					1179:1187	the same two FP molecules	1163:1187	the same two FP molecules	1163:1187	The second and largest interface is formed by TSR1 and TSR6 from the same two FP molecules.
31507604	10	62	from	function	1472:1479	arg1	convertases					1484:1494	convertases	1484:1494	convertases	1484:1494	Our structures rationalize the effects of mutations associated with FP deficiencies and provide a structural basis for the analysis of FP function in convertases and its possible role in pattern recognition.
31507604	10	62	from	function	1472:1479	arg1	recognition					1529:1539	pattern recognition	1521:1539	pattern recognition	1521:1539	Our structures rationalize the effects of mutations associated with FP deficiencies and provide a structural basis for the analysis of FP function in convertases and its possible role in pattern recognition.
31507604	6	63	theme	due	878:880	arg1	FI					875:876	FI	875:876	FI due to a direct competition for a common binding site on C3b	875:937	FP is shown to inhibit C3b degradation by FI due to a direct competition for a common binding site on C3b.
31507604	7	64	theme	FP	940:941	arg1	oligomers					943:951	FP oligomers	940:951	FP oligomers	940:951	FP oligomers are held together by two sets of intermolecular contacts, where the first is formed by the TB domain from one FP molecule and TSR4 from another.
31507604	2	65	theme	crystal	314:320	arg1	structures					322:331	two crystal structures	310:331	two crystal structures of FP	310:337	Here we present two crystal structures of FP and two structures of convertase bound FP.
31507604	1	66	theme	active	214:219	arg1	C3bBb					235:239	the proteolytically active C3 convertase C3bBb	194:239	the proteolytically active C3 convertase C3bBb	194:239	Properdin (FP) is a positive regulator of the immune system stimulating the activity of the proteolytically active C3 convertase C3bBb in the alternative pathway of the complement system.
31507604	10	67	theme	FP	1402:1403	arg1	deficiencies					1405:1416	FP deficiencies	1402:1416	FP deficiencies	1402:1416	Our structures rationalize the effects of mutations associated with FP deficiencies and provide a structural basis for the analysis of FP function in convertases and its possible role in pattern recognition.
31507604	10	68	theme	role	1513:1516	arg1	analysis					1457:1464	the analysis	1453:1464	the analysis of FP function in convertases and its possible role in pattern recognition	1453:1539	Our structures rationalize the effects of mutations associated with FP deficiencies and provide a structural basis for the analysis of FP function in convertases and its possible role in pattern recognition.
31507604	4	69	theme	Bb	628:629	arg1	protease					631:638	the Bb protease	624:638	the Bb protease	624:638	Stabilization of the interaction between the C3b C-terminus and the MIDAS bound Mg2+ in the Bb protease by FP TSR5 is proposed to underlie FP convertase stabilization.
31507604	1	70	theme	C3	221:222	arg1	C3bBb					235:239	the proteolytically active C3 convertase C3bBb	194:239	the proteolytically active C3 convertase C3bBb	194:239	Properdin (FP) is a positive regulator of the immune system stimulating the activity of the proteolytically active C3 convertase C3bBb in the alternative pathway of the complement system.
31507604	3	71	theme	thrombospondin	416:429	arg1	TSRs					440:443	TSRs	440:443	TSRs	440:443	A structural core formed by three thrombospondin repeats (TSRs) and a TB domain harbors the convertase binding site in FP that mainly interacts with C3b.
31507604	3	71	theme	thrombospondin	416:429	arg1	repeats					431:437	three thrombospondin repeats	410:437	three thrombospondin repeats (TSRs)	410:444	A structural core formed by three thrombospondin repeats (TSRs) and a TB domain harbors the convertase binding site in FP that mainly interacts with C3b.
31507604	1	72	theme	positive	126:133	arg1	regulator					135:143	a positive regulator	124:143	a positive regulator of the immune system stimulating the activity of the proteolytically active C3 convertase C3bBb in the alternative pathway of the complement system	124:291	Properdin (FP) is a positive regulator of the immune system stimulating the activity of the proteolytically active C3 convertase C3bBb in the alternative pathway of the complement system.
31507604	1	72	theme	positive	126:133	arg1	Properdin					106:114	Properdin	106:114	Properdin (FP)	106:119	Properdin (FP) is a positive regulator of the immune system stimulating the activity of the proteolytically active C3 convertase C3bBb in the alternative pathway of the complement system.
31507604	2	73	theme	bound	372:376	arg1	FP					378:379	convertase bound FP	361:379	convertase bound FP	361:379	Here we present two crystal structures of FP and two structures of convertase bound FP.
31507604	1	74	theme	convertase	224:233	arg1	C3bBb					235:239	the proteolytically active C3 convertase C3bBb	194:239	the proteolytically active C3 convertase C3bBb	194:239	Properdin (FP) is a positive regulator of the immune system stimulating the activity of the proteolytically active C3 convertase C3bBb in the alternative pathway of the complement system.
31507604	5	75	theme	Intermolecular	704:717	arg1	contacts					719:726	Intermolecular contacts	704:726	Intermolecular contacts between FP and the convertase subunits suggested by the structure	704:792	Intermolecular contacts between FP and the convertase subunits suggested by the structure were confirmed by binding experiments.
31507604	9	76	theme	polydisperse	1287:1298	arg1	architecture					1314:1325	the oligomeric, polydisperse, and extended architecture	1271:1325	the oligomeric, polydisperse, and extended architecture of FP	1271:1331	Flexibility at four hinges between thrombospondin repeats is suggested to enable the oligomeric, polydisperse, and extended architecture of FP.
31507604	3	77	theme	binding	485:491	arg1	site					493:496	the convertase binding site	470:496	the convertase binding site in FP that mainly interacts with C3b	470:533	A structural core formed by three thrombospondin repeats (TSRs) and a TB domain harbors the convertase binding site in FP that mainly interacts with C3b.
31507604	3	78	from	site	493:496	arg1	FP					501:502	FP	501:502	FP	501:502	A structural core formed by three thrombospondin repeats (TSRs) and a TB domain harbors the convertase binding site in FP that mainly interacts with C3b.
31507604	1	79	theme	C3bBb	235:239	arg1	activity					182:189	the activity	178:189	the activity of the proteolytically active C3 convertase C3bBb in the alternative pathway of the complement system	178:291	Properdin (FP) is a positive regulator of the immune system stimulating the activity of the proteolytically active C3 convertase C3bBb in the alternative pathway of the complement system.
10878002	1	0	theme	complement	141:150	arg1	activation					152:161	complement activation	141:161	complement activation	141:161	Properdin is the positive regulator of the alternative pathway of complement activation.
10878002	9	1	theme	protein	998:1004	arg1	example					985:991	the first example	975:991	the first example of a protein in which the majority of tryptophan residues occurs in the C-mannosylated form	975:1083	This is the first example of a protein in which the majority of tryptophan residues occurs in the C-mannosylated form.
10878002	9	1	theme	protein	998:1004	arg1	This					967:970	This	967:970	This	967:970	This is the first example of a protein in which the majority of tryptophan residues occurs in the C-mannosylated form.
10878002	10	2	theme	complement	1167:1176	arg1	cascade					1189:1195	the complement activation cascade	1163:1195	the complement activation cascade	1163:1195	These results show that C-mannosylated proteins occur at several steps along the complement activation cascade.
10878002	1	3	theme	activation	152:161	arg1	pathway					130:136	the alternative pathway	114:136	the alternative pathway of complement activation	114:161	Properdin is the positive regulator of the alternative pathway of complement activation.
10878002	5	4	theme	terminal	628:635	arg1	proteins					648:655	The terminal complement proteins	624:655	The terminal complement proteins C6-C9	624:661	The terminal complement proteins C6-C9 also carry this modification as part of their thrombospondin type 1 repeats.
10878002	2	5	theme	thrombospondin	214:227	arg1	type					229:232	thrombospondin type 1	214:234	six thrombospondin type 1 repeats	210:242	The 53-kDa protein is essentially composed of six thrombospondin type 1 repeats, all of which contain the WXXW motif, the recognition sequence for C-mannosylation.
10878002	2	6	theme	WXXW	270:273	arg1	sequence					298:305	the recognition sequence	282:305	the recognition sequence for C-mannosylation	282:325	The 53-kDa protein is essentially composed of six thrombospondin type 1 repeats, all of which contain the WXXW motif, the recognition sequence for C-mannosylation.
10878002	2	6	theme	WXXW	270:273	arg1	motif					275:279	the WXXW motif	266:279	the WXXW motif	266:279	The 53-kDa protein is essentially composed of six thrombospondin type 1 repeats, all of which contain the WXXW motif, the recognition sequence for C-mannosylation.
10878002	3	7	theme	indole	526:531	arg1	moiety					533:538	the indole moiety	522:538	the indole moiety of tryptophan	522:552	C-Mannosylation is a post-translational modification of tryptophan residues in which, in contrast to the well known N- and O-glycosylation, the carbohydrate is attached via a C-C bond to C-2 of the indole moiety of tryptophan.
10878002	3	8	theme	moiety	533:538	arg1	C-2					515:517	C-2	515:517	C-2 of the indole moiety of tryptophan	515:552	C-Mannosylation is a post-translational modification of tryptophan residues in which, in contrast to the well known N- and O-glycosylation, the carbohydrate is attached via a C-C bond to C-2 of the indole moiety of tryptophan.
10878002	5	9	theme	complement	637:646	arg1	proteins					648:655	The terminal complement proteins	624:655	The terminal complement proteins C6-C9	624:661	The terminal complement proteins C6-C9 also carry this modification as part of their thrombospondin type 1 repeats.
10878002	6	10	theme	human	782:786	arg1	properdin					788:796	human properdin	782:796	human properdin	782:796	We studied the C-mannosylation pattern of human properdin by mass spectrometry and Edman degradation.
10878002	10	11	gly	C-mannosylated	1110:1123	arg1	proteins					1125:1132	C-mannosylated proteins	1110:1132	C-mannosylated proteins	1110:1132	These results show that C-mannosylated proteins occur at several steps along the complement activation cascade.
10878002	5	12	theme	thrombospondin	709:722	arg1	repeats					731:737	their thrombospondin type 1 repeats	703:737	their thrombospondin type 1 repeats	703:737	The terminal complement proteins C6-C9 also carry this modification as part of their thrombospondin type 1 repeats.
10878002	0	13	gly	C-mannosylated	59:72	arg1	Properdin					0:8	Properdin	0:8	Properdin	0:8	Properdin, the positive regulator of complement, is highly C-mannosylated.
10878002	0	13	gly	C-mannosylated	59:72	arg1	regulator					24:32	the positive regulator	11:32	the positive regulator of complement	11:46	Properdin, the positive regulator of complement, is highly C-mannosylated.
10878002	5	14	theme	type	724:727	arg1	repeats					731:737	their thrombospondin type 1 repeats	703:737	their thrombospondin type 1 repeats	703:737	The terminal complement proteins C6-C9 also carry this modification as part of their thrombospondin type 1 repeats.
10878002	11	15	theme	C-mannosylation	1267:1281	arg1	function					1255:1262	the function	1251:1262	the function of C-mannosylation	1251:1281	Therefore, this system would be ideal to investigate the function of C-mannosylation.
10878002	7	16	theme	motif	907:911	arg1	part					892:895	part	892:895	part of a WXXW motif	892:911	Properdin contains 20 tryptophans of which 17 are part of a WXXW motif.
10878002	7	16	theme	motif	907:911	arg1	17					885:886	17	885:886	17	885:886	Properdin contains 20 tryptophans of which 17 are part of a WXXW motif.
10878002	5	17	dep	proteins	648:655	arg1	C6-C9					657:661	C6-C9	657:661	The terminal complement proteins C6-C9	624:661	The terminal complement proteins C6-C9 also carry this modification as part of their thrombospondin type 1 repeats.
10878002	3	18	theme	tryptophan	384:393	arg1	residues					395:402	tryptophan residues	384:402	tryptophan residues	384:402	C-Mannosylation is a post-translational modification of tryptophan residues in which, in contrast to the well known N- and O-glycosylation, the carbohydrate is attached via a C-C bond to C-2 of the indole moiety of tryptophan.
10878002	6	19	theme	C-mannosylation	755:769	arg1	pattern					771:777	the C-mannosylation pattern	751:777	the C-mannosylation pattern of human properdin	751:796	We studied the C-mannosylation pattern of human properdin by mass spectrometry and Edman degradation.
10878002	2	20	theme	recognition	286:296	arg1	sequence					298:305	the recognition sequence	282:305	the recognition sequence for C-mannosylation	282:325	The 53-kDa protein is essentially composed of six thrombospondin type 1 repeats, all of which contain the WXXW motif, the recognition sequence for C-mannosylation.
10878002	2	20	theme	recognition	286:296	arg1	motif					275:279	the WXXW motif	266:279	the WXXW motif	266:279	The 53-kDa protein is essentially composed of six thrombospondin type 1 repeats, all of which contain the WXXW motif, the recognition sequence for C-mannosylation.
10878002	9	21	theme	tryptophan	1031:1040	arg1	residues					1042:1049	tryptophan residues	1031:1049	tryptophan residues	1031:1049	This is the first example of a protein in which the majority of tryptophan residues occurs in the C-mannosylated form.
10878002	3	22	theme	residues	395:402	arg1	modification					368:379	a post-translational modification	347:379	a post-translational modification of tryptophan residues in which, in contrast to the well known N- and O-glycosylation, the carbohydrate is attached via a C-C bond to C-2 of the indole moiety of tryptophan	347:552	C-Mannosylation is a post-translational modification of tryptophan residues in which, in contrast to the well known N- and O-glycosylation, the carbohydrate is attached via a C-C bond to C-2 of the indole moiety of tryptophan.
10878002	3	22	theme	residues	395:402	arg1	C-Mannosylation					328:342	C-Mannosylation	328:342	C-Mannosylation	328:342	C-Mannosylation is a post-translational modification of tryptophan residues in which, in contrast to the well known N- and O-glycosylation, the carbohydrate is attached via a C-C bond to C-2 of the indole moiety of tryptophan.
10878002	6	23	gly	C-mannosylation	755:769	arg1	properdin					788:796	human properdin	782:796	human properdin	782:796	We studied the C-mannosylation pattern of human properdin by mass spectrometry and Edman degradation.
10878002	4	24	gly	C-Mannosylation	555:569	arg1	RNase					596:600	human RNase 2	590:602	human RNase 2	590:602	C-Mannosylation was first found in human RNase 2 and interleukin-12.
10878002	4	24	gly	C-Mannosylation	555:569	arg1	interleukin-12					608:621	interleukin-12	608:621	interleukin-12	608:621	C-Mannosylation was first found in human RNase 2 and interleukin-12.
10878002	9	25	theme	residues	1042:1049	arg1	majority					1019:1026	the majority	1015:1026	the majority of tryptophan residues	1015:1049	This is the first example of a protein in which the majority of tryptophan residues occurs in the C-mannosylated form.
10878002	0	26	theme	positive	15:22	arg1	Properdin					0:8	Properdin	0:8	Properdin	0:8	Properdin, the positive regulator of complement, is highly C-mannosylated.
10878002	0	26	theme	positive	15:22	arg1	regulator					24:32	the positive regulator	11:32	the positive regulator of complement	11:46	Properdin, the positive regulator of complement, is highly C-mannosylated.
10878002	2	27	contain	contain	258:264	arg2	sequence					298:305	the recognition sequence	282:305	the recognition sequence for C-mannosylation	282:325	The 53-kDa protein is essentially composed of six thrombospondin type 1 repeats, all of which contain the WXXW motif, the recognition sequence for C-mannosylation.
10878002	2	27	contain	contain	258:264	arg1	all					245:247	all	245:247	all	245:247	The 53-kDa protein is essentially composed of six thrombospondin type 1 repeats, all of which contain the WXXW motif, the recognition sequence for C-mannosylation.
10878002	2	27	contain	contain	258:264	arg2	motif					275:279	the WXXW motif	266:279	the WXXW motif	266:279	The 53-kDa protein is essentially composed of six thrombospondin type 1 repeats, all of which contain the WXXW motif, the recognition sequence for C-mannosylation.
10878002	2	27	contain	contain	258:264	arg1	repeats					236:242	six thrombospondin type 1 repeats	210:242	six thrombospondin type 1 repeats	210:242	The 53-kDa protein is essentially composed of six thrombospondin type 1 repeats, all of which contain the WXXW motif, the recognition sequence for C-mannosylation.
10878002	7	28	theme	WXXW	902:905	arg1	motif					907:911	a WXXW motif	900:911	a WXXW motif	900:911	Properdin contains 20 tryptophans of which 17 are part of a WXXW motif.
10878002	6	29	theme	properdin	788:796	arg1	pattern					771:777	the C-mannosylation pattern	751:777	the C-mannosylation pattern of human properdin	751:796	We studied the C-mannosylation pattern of human properdin by mass spectrometry and Edman degradation.
10878002	1	30	theme	positive	92:99	arg1	regulator					101:109	the positive regulator	88:109	the positive regulator of the alternative pathway of complement activation	88:161	Properdin is the positive regulator of the alternative pathway of complement activation.
10878002	1	30	theme	positive	92:99	arg1	Properdin					75:83	Properdin	75:83	Properdin	75:83	Properdin is the positive regulator of the alternative pathway of complement activation.
10878002	2	31	theme	53-kDa	168:173	arg1	protein					175:181	The 53-kDa protein	164:181	The 53-kDa protein	164:181	The 53-kDa protein is essentially composed of six thrombospondin type 1 repeats, all of which contain the WXXW motif, the recognition sequence for C-mannosylation.
10878002	3	32	theme	known	438:442	arg1	N-					444:445	the well known N-	429:445	the well known N-	429:445	C-Mannosylation is a post-translational modification of tryptophan residues in which, in contrast to the well known N- and O-glycosylation, the carbohydrate is attached via a C-C bond to C-2 of the indole moiety of tryptophan.
10878002	5	33	contain	carry	668:672	arg1	proteins					648:655	The terminal complement proteins	624:655	The terminal complement proteins C6-C9	624:661	The terminal complement proteins C6-C9 also carry this modification as part of their thrombospondin type 1 repeats.
10878002	5	33	contain	carry	668:672	arg2	modification					679:690	this modification	674:690	this modification	674:690	The terminal complement proteins C6-C9 also carry this modification as part of their thrombospondin type 1 repeats.
10878002	9	34	theme	C-mannosylated	1065:1078	arg1	form					1080:1083	the C-mannosylated form	1061:1083	the C-mannosylated form	1061:1083	This is the first example of a protein in which the majority of tryptophan residues occurs in the C-mannosylated form.
10878002	2	35	theme	type	229:232	arg1	repeats					236:242	six thrombospondin type 1 repeats	210:242	six thrombospondin type 1 repeats	210:242	The 53-kDa protein is essentially composed of six thrombospondin type 1 repeats, all of which contain the WXXW motif, the recognition sequence for C-mannosylation.
10878002	4	36	located	found	581:585	arg1	RNase					596:600	human RNase 2	590:602	human RNase 2	590:602	C-Mannosylation was first found in human RNase 2 and interleukin-12.
10878002	4	36	located	found	581:585	arg1	interleukin-12					608:621	interleukin-12	608:621	interleukin-12	608:621	C-Mannosylation was first found in human RNase 2 and interleukin-12.
10878002	4	36	located	found	581:585	arg2	C-Mannosylation					555:569	C-Mannosylation	555:569	C-Mannosylation	555:569	C-Mannosylation was first found in human RNase 2 and interleukin-12.
10878002	10	37	theme	C-mannosylated	1110:1123	arg1	proteins					1125:1132	C-mannosylated proteins	1110:1132	C-mannosylated proteins	1110:1132	These results show that C-mannosylated proteins occur at several steps along the complement activation cascade.
10878002	9	38	gly	C-mannosylated	1065:1078	arg1	form					1080:1083	the C-mannosylated form	1061:1083	the C-mannosylated form	1061:1083	This is the first example of a protein in which the majority of tryptophan residues occurs in the C-mannosylated form.
10878002	3	39	theme	tryptophan	543:552	arg1	moiety					533:538	the indole moiety	522:538	the indole moiety of tryptophan	522:552	C-Mannosylation is a post-translational modification of tryptophan residues in which, in contrast to the well known N- and O-glycosylation, the carbohydrate is attached via a C-C bond to C-2 of the indole moiety of tryptophan.
10878002	0	40	theme	complement	37:46	arg1	Properdin					0:8	Properdin	0:8	Properdin	0:8	Properdin, the positive regulator of complement, is highly C-mannosylated.
10878002	0	40	theme	complement	37:46	arg1	regulator					24:32	the positive regulator	11:32	the positive regulator of complement	11:46	Properdin, the positive regulator of complement, is highly C-mannosylated.
10878002	6	41	theme	Edman	823:827	arg1	degradation					829:839	Edman degradation	823:839	Edman degradation	823:839	We studied the C-mannosylation pattern of human properdin by mass spectrometry and Edman degradation.
10878002	7	42	contain	contains	852:859	arg1	Properdin					842:850	Properdin	842:850	Properdin	842:850	Properdin contains 20 tryptophans of which 17 are part of a WXXW motif.
10878002	7	42	contain	contains	852:859	arg2	tryptophans					864:874	20 tryptophans	861:874	20 tryptophans of which 17 are part of a WXXW motif	861:911	Properdin contains 20 tryptophans of which 17 are part of a WXXW motif.
10878002	3	43	attach	attached	488:495	arg3	modification					368:379	a post-translational modification	347:379	a post-translational modification of tryptophan residues in which, in contrast to the well known N- and O-glycosylation, the carbohydrate is attached via a C-C bond to C-2 of the indole moiety of tryptophan	347:552	C-Mannosylation is a post-translational modification of tryptophan residues in which, in contrast to the well known N- and O-glycosylation, the carbohydrate is attached via a C-C bond to C-2 of the indole moiety of tryptophan.
10878002	3	43	attach	attached	488:495	arg1	N-					444:445	the well known N-	429:445	the well known N-	429:445	C-Mannosylation is a post-translational modification of tryptophan residues in which, in contrast to the well known N- and O-glycosylation, the carbohydrate is attached via a C-C bond to C-2 of the indole moiety of tryptophan.
10878002	3	43	attach	attached	488:495	arg1	O-glycosylation					451:465	O-glycosylation	451:465	O-glycosylation	451:465	C-Mannosylation is a post-translational modification of tryptophan residues in which, in contrast to the well known N- and O-glycosylation, the carbohydrate is attached via a C-C bond to C-2 of the indole moiety of tryptophan.
10878002	3	43	attach	attached	488:495	arg3	C-Mannosylation					328:342	C-Mannosylation	328:342	C-Mannosylation	328:342	C-Mannosylation is a post-translational modification of tryptophan residues in which, in contrast to the well known N- and O-glycosylation, the carbohydrate is attached via a C-C bond to C-2 of the indole moiety of tryptophan.
10878002	3	43	attach	attached	488:495	arg2	carbohydrate					472:483	the carbohydrate	468:483	the carbohydrate	468:483	C-Mannosylation is a post-translational modification of tryptophan residues in which, in contrast to the well known N- and O-glycosylation, the carbohydrate is attached via a C-C bond to C-2 of the indole moiety of tryptophan.
10878002	9	44	theme	first	979:983	arg1	example					985:991	the first example	975:991	the first example of a protein in which the majority of tryptophan residues occurs in the C-mannosylated form	975:1083	This is the first example of a protein in which the majority of tryptophan residues occurs in the C-mannosylated form.
10878002	9	44	theme	first	979:983	arg1	This					967:970	This	967:970	This	967:970	This is the first example of a protein in which the majority of tryptophan residues occurs in the C-mannosylated form.
10878002	10	45	theme	several	1143:1149	arg1	steps					1151:1155	several steps	1143:1155	several steps along the complement activation cascade	1143:1195	These results show that C-mannosylated proteins occur at several steps along the complement activation cascade.
10878002	3	46	dep	N-	444:445	arg1	contrast					417:424	contrast	417:424	contrast	417:424	C-Mannosylation is a post-translational modification of tryptophan residues in which, in contrast to the well known N- and O-glycosylation, the carbohydrate is attached via a C-C bond to C-2 of the indole moiety of tryptophan.
10878002	1	47	theme	alternative	118:128	arg1	pathway					130:136	the alternative pathway	114:136	the alternative pathway of complement activation	114:161	Properdin is the positive regulator of the alternative pathway of complement activation.
10878002	7	48	theme	tryptophans	864:874	arg1	part					892:895	part	892:895	part of a WXXW motif	892:911	Properdin contains 20 tryptophans of which 17 are part of a WXXW motif.
10878002	7	48	theme	tryptophans	864:874	arg1	17					885:886	17	885:886	17	885:886	Properdin contains 20 tryptophans of which 17 are part of a WXXW motif.
10878002	6	49	theme	mass	801:804	arg1	spectrometry					806:817	mass spectrometry	801:817	mass spectrometry	801:817	We studied the C-mannosylation pattern of human properdin by mass spectrometry and Edman degradation.
10878002	1	50	theme	pathway	130:136	arg1	regulator					101:109	the positive regulator	88:109	the positive regulator of the alternative pathway of complement activation	88:161	Properdin is the positive regulator of the alternative pathway of complement activation.
10878002	1	50	theme	pathway	130:136	arg1	Properdin					75:83	Properdin	75:83	Properdin	75:83	Properdin is the positive regulator of the alternative pathway of complement activation.
10878002	10	51	theme	activation	1178:1187	arg1	cascade					1189:1195	the complement activation cascade	1163:1195	the complement activation cascade	1163:1195	These results show that C-mannosylated proteins occur at several steps along the complement activation cascade.
10878002	4	52	theme	human	590:594	arg1	RNase					596:600	human RNase 2	590:602	human RNase 2	590:602	C-Mannosylation was first found in human RNase 2 and interleukin-12.
10878002	5	53	theme	repeats	731:737	arg1	part					695:698	part	695:698	part of their thrombospondin type 1 repeats	695:737	The terminal complement proteins C6-C9 also carry this modification as part of their thrombospondin type 1 repeats.
10878002	3	54	theme	C-C	503:505	arg1	bond					507:510	a C-C bond	501:510	a C-C bond to C-2 of the indole moiety of tryptophan	501:552	C-Mannosylation is a post-translational modification of tryptophan residues in which, in contrast to the well known N- and O-glycosylation, the carbohydrate is attached via a C-C bond to C-2 of the indole moiety of tryptophan.
10878002	3	55	theme	post-translational	349:366	arg1	modification					368:379	a post-translational modification	347:379	a post-translational modification of tryptophan residues in which, in contrast to the well known N- and O-glycosylation, the carbohydrate is attached via a C-C bond to C-2 of the indole moiety of tryptophan	347:552	C-Mannosylation is a post-translational modification of tryptophan residues in which, in contrast to the well known N- and O-glycosylation, the carbohydrate is attached via a C-C bond to C-2 of the indole moiety of tryptophan.
10878002	3	55	theme	post-translational	349:366	arg1	C-Mannosylation					328:342	C-Mannosylation	328:342	C-Mannosylation	328:342	C-Mannosylation is a post-translational modification of tryptophan residues in which, in contrast to the well known N- and O-glycosylation, the carbohydrate is attached via a C-C bond to C-2 of the indole moiety of tryptophan.
23980170	7	0	theme	domain-level	1221:1232	arg1	change					1249:1254	domain-level conformational change	1221:1254	domain-level conformational change of IL-1 primary receptors upon ligand binding	1221:1300	The molecular flexibility of ST2 provides structural insights into domain-level conformational change of IL-1 primary receptors upon ligand binding, and the rigidity of IL-1RAcP explains its inability to bind ligands directly.
23980170	0	1	with	interaction	29:39	arg1	receptors					59:67	its receptors	55:67	its receptors	55:67	Structural insights into the interaction of IL-33 with its receptors.
23980170	1	2	theme	IL-1	120:123	arg1	family					125:130	the IL-1 family	116:130	the IL-1 family	116:130	Interleukin (IL)-33 is an important member of the IL-1 family that has pleiotropic activities in innate and adaptive immune responses in host defense and disease.
23980170	5	3	from	complexes	768:776	arg1	family					790:795	the IL-1 family	781:795	the IL-1 family	781:795	Structural comparison with other ligand-receptor complexes in the IL-1 family indicates that surface-charge complementarity is critical in determining ligand-binding specificity of IL-1 primary receptors.
23980170	9	4	theme	structure-function	1595:1612	arg1	relationships					1614:1626	IL-33 structure-function relationships	1589:1626	IL-33 structure-function relationships	1589:1626	The collective results confer IL-33 structure-function relationships, supporting and extending a general model for ligand-receptor assembly and activation in the IL-1 family.
23980170	7	5	theme	conformational	1234:1247	arg1	change					1249:1254	domain-level conformational change	1221:1254	domain-level conformational change of IL-1 primary receptors upon ligand binding	1221:1300	The molecular flexibility of ST2 provides structural insights into domain-level conformational change of IL-1 primary receptors upon ligand binding, and the rigidity of IL-1RAcP explains its inability to bind ligands directly.
23980170	6	6	theme	rigid	1101:1105	arg1	conformation					1107:1118	a rigid conformation	1099:1118	a rigid conformation	1099:1118	Combined crystallography and small-angle X-ray-scattering studies reveal that ST2 possesses hinge flexibility between the D3 domain and D1D2 module, whereas IL-1RAcP exhibits a rigid conformation in the unbound state in solution.
23980170	1	7	theme	family	125:130	arg1	IL					83:84	Interleukin (IL)-33	70:88	Interleukin (IL)-33	70:88	Interleukin (IL)-33 is an important member of the IL-1 family that has pleiotropic activities in innate and adaptive immune responses in host defense and disease.
23980170	1	7	theme	family	125:130	arg1	member					106:111	an important member	93:111	an important member of the IL-1 family that has pleiotropic activities in innate and adaptive immune responses in host defense and disease	93:230	Interleukin (IL)-33 is an important member of the IL-1 family that has pleiotropic activities in innate and adaptive immune responses in host defense and disease.
23980170	3	8	from	structure	477:485	arg1	complex					499:505	complex	499:505	complex with the ectodomain of ST2	499:532	To clarify the interaction of IL-33 with its receptors, we determined the crystal structure of IL-33 in complex with the ectodomain of ST2 at a resolution of 3.27 Å.
23980170	7	9	theme	molecular	1158:1166	arg1	flexibility					1168:1178	The molecular flexibility	1154:1178	The molecular flexibility of ST2	1154:1185	The molecular flexibility of ST2 provides structural insights into domain-level conformational change of IL-1 primary receptors upon ligand binding, and the rigidity of IL-1RAcP explains its inability to bind ligands directly.
23980170	9	10	theme	IL-1	1721:1724	arg1	family					1726:1731	the IL-1 family	1717:1731	the IL-1 family	1717:1731	The collective results confer IL-33 structure-function relationships, supporting and extending a general model for ligand-receptor assembly and activation in the IL-1 family.
23980170	5	11	with	comparison	730:739	arg1	complexes					768:776	other ligand-receptor complexes	746:776	other ligand-receptor complexes in the IL-1 family	746:795	Structural comparison with other ligand-receptor complexes in the IL-1 family indicates that surface-charge complementarity is critical in determining ligand-binding specificity of IL-1 primary receptors.
23980170	6	12	contain	possesses	1006:1014	arg1	ST2					1002:1004	ST2	1002:1004	ST2	1002:1004	Combined crystallography and small-angle X-ray-scattering studies reveal that ST2 possesses hinge flexibility between the D3 domain and D1D2 module, whereas IL-1RAcP exhibits a rigid conformation in the unbound state in solution.
23980170	6	12	contain	possesses	1006:1014	arg2	flexibility					1022:1032	hinge flexibility	1016:1032	hinge flexibility between the D3 domain and D1D2 module	1016:1070	Combined crystallography and small-angle X-ray-scattering studies reveal that ST2 possesses hinge flexibility between the D3 domain and D1D2 module, whereas IL-1RAcP exhibits a rigid conformation in the unbound state in solution.
23980170	8	13	from	architecture	1394:1405	arg1	analysis					1471:1478	small-angle X-ray-scattering analysis	1442:1478	small-angle X-ray-scattering analysis	1442:1478	The solution architecture of IL-33-ST2-IL-1RAcP complex from small-angle X-ray-scattering analysis resembles IL-1β-IL-1RII-IL-1RAcP and IL-1β-IL-1RI-IL-1RAcP crystal structures.
23980170	6	14	theme	X-ray-scattering	965:980	arg1	studies					982:988	Combined crystallography and small-angle X-ray-scattering studies	924:988	studies	982:988	Combined crystallography and small-angle X-ray-scattering studies reveal that ST2 possesses hinge flexibility between the D3 domain and D1D2 module, whereas IL-1RAcP exhibits a rigid conformation in the unbound state in solution.
23980170	5	15	theme	ligand-receptor	752:766	arg1	complexes					768:776	other ligand-receptor complexes	746:776	other ligand-receptor complexes in the IL-1 family	746:795	Structural comparison with other ligand-receptor complexes in the IL-1 family indicates that surface-charge complementarity is critical in determining ligand-binding specificity of IL-1 primary receptors.
23980170	9	16	theme	general	1656:1662	arg1	model					1664:1668	a general model	1654:1668	a general model for ligand-receptor assembly and activation in the IL-1 family	1654:1731	The collective results confer IL-33 structure-function relationships, supporting and extending a general model for ligand-receptor assembly and activation in the IL-1 family.
23980170	7	17	theme	primary	1264:1270	arg1	receptors					1272:1280	IL-1 primary receptors	1259:1280	IL-1 primary receptors	1259:1280	The molecular flexibility of ST2 provides structural insights into domain-level conformational change of IL-1 primary receptors upon ligand binding, and the rigidity of IL-1RAcP explains its inability to bind ligands directly.
23980170	7	18	theme	IL-1	1259:1262	arg1	receptors					1272:1280	IL-1 primary receptors	1259:1280	IL-1 primary receptors	1259:1280	The molecular flexibility of ST2 provides structural insights into domain-level conformational change of IL-1 primary receptors upon ligand binding, and the rigidity of IL-1RAcP explains its inability to bind ligands directly.
23980170	9	19	from	activation	1703:1712	arg1	family					1726:1731	the IL-1 family	1717:1731	the IL-1 family	1717:1731	The collective results confer IL-33 structure-function relationships, supporting and extending a general model for ligand-receptor assembly and activation in the IL-1 family.
23980170	5	20	theme	primary	905:911	arg1	receptors					913:921	IL-1 primary receptors	900:921	IL-1 primary receptors	900:921	Structural comparison with other ligand-receptor complexes in the IL-1 family indicates that surface-charge complementarity is critical in determining ligand-binding specificity of IL-1 primary receptors.
23980170	8	21	dep	IL-1β-IL-1RII-IL-1RAcP	1490:1511	arg1	structures					1547:1556	crystal structures	1539:1556	crystal structures	1539:1556	The solution architecture of IL-33-ST2-IL-1RAcP complex from small-angle X-ray-scattering analysis resembles IL-1β-IL-1RII-IL-1RAcP and IL-1β-IL-1RI-IL-1RAcP crystal structures.
23980170	5	22	theme	IL-1	785:788	arg1	family					790:795	the IL-1 family	781:795	the IL-1 family	781:795	Structural comparison with other ligand-receptor complexes in the IL-1 family indicates that surface-charge complementarity is critical in determining ligand-binding specificity of IL-1 primary receptors.
23980170	9	23	dep	confer	1582:1587	arg1	supporting					1629:1638	supporting	1629:1638	supporting	1629:1638	The collective results confer IL-33 structure-function relationships, supporting and extending a general model for ligand-receptor assembly and activation in the IL-1 family.
23980170	9	23	dep	confer	1582:1587	arg1	extending					1644:1652	extending	1644:1652	extending a general model for ligand-receptor assembly and activation in the IL-1 family	1644:1731	The collective results confer IL-33 structure-function relationships, supporting and extending a general model for ligand-receptor assembly and activation in the IL-1 family.
23980170	5	24	theme	IL-1	900:903	arg1	receptors					913:921	IL-1 primary receptors	900:921	IL-1 primary receptors	900:921	Structural comparison with other ligand-receptor complexes in the IL-1 family indicates that surface-charge complementarity is critical in determining ligand-binding specificity of IL-1 primary receptors.
23980170	4	25	theme	structure-based	574:588	arg1	mutagenesis					590:600	structure-based mutagenesis	574:600	structure-based mutagenesis	574:600	Coupled with structure-based mutagenesis and binding assay, the structural results define the molecular mechanism by which ST2 specifically recognizes IL-33.
23980170	7	26	theme	structural	1196:1205	arg1	insights					1207:1214	structural insights	1196:1214	structural insights into domain-level conformational change of IL-1 primary receptors upon ligand binding	1196:1300	The molecular flexibility of ST2 provides structural insights into domain-level conformational change of IL-1 primary receptors upon ligand binding, and the rigidity of IL-1RAcP explains its inability to bind ligands directly.
23980170	5	27	theme	ligand-binding	870:883	arg1	specificity					885:895	ligand-binding specificity	870:895	ligand-binding specificity of IL-1 primary receptors	870:921	Structural comparison with other ligand-receptor complexes in the IL-1 family indicates that surface-charge complementarity is critical in determining ligand-binding specificity of IL-1 primary receptors.
23980170	7	28	theme	IL-1RAcP	1323:1330	arg1	rigidity					1311:1318	the rigidity	1307:1318	the rigidity of IL-1RAcP	1307:1330	The molecular flexibility of ST2 provides structural insights into domain-level conformational change of IL-1 primary receptors upon ligand binding, and the rigidity of IL-1RAcP explains its inability to bind ligands directly.
23980170	1	29	theme	Interleukin	70:80	arg1	IL					83:84	Interleukin (IL)-33	70:88	Interleukin (IL)-33	70:88	Interleukin (IL)-33 is an important member of the IL-1 family that has pleiotropic activities in innate and adaptive immune responses in host defense and disease.
23980170	1	29	theme	Interleukin	70:80	arg1	member					106:111	an important member	93:111	an important member of the IL-1 family that has pleiotropic activities in innate and adaptive immune responses in host defense and disease	93:230	Interleukin (IL)-33 is an important member of the IL-1 family that has pleiotropic activities in innate and adaptive immune responses in host defense and disease.
23980170	5	30	theme	surface-charge	812:825	arg1	complementarity					827:841	surface-charge complementarity	812:841	surface-charge complementarity	812:841	Structural comparison with other ligand-receptor complexes in the IL-1 family indicates that surface-charge complementarity is critical in determining ligand-binding specificity of IL-1 primary receptors.
23980170	5	31	theme	other	746:750	arg1	complexes					768:776	other ligand-receptor complexes	746:776	other ligand-receptor complexes in the IL-1 family	746:795	Structural comparison with other ligand-receptor complexes in the IL-1 family indicates that surface-charge complementarity is critical in determining ligand-binding specificity of IL-1 primary receptors.
23980170	5	32	theme	receptors	913:921	arg1	specificity					885:895	ligand-binding specificity	870:895	ligand-binding specificity of IL-1 primary receptors	870:921	Structural comparison with other ligand-receptor complexes in the IL-1 family indicates that surface-charge complementarity is critical in determining ligand-binding specificity of IL-1 primary receptors.
23980170	1	33	theme	pleiotropic	141:151	arg1	activities					153:162	pleiotropic activities	141:162	pleiotropic activities in innate and adaptive immune responses in host defense and disease	141:230	Interleukin (IL)-33 is an important member of the IL-1 family that has pleiotropic activities in innate and adaptive immune responses in host defense and disease.
23980170	0	34	theme	Structural	0:9	arg1	insights					11:18	Structural insights	0:18	Structural insights into the interaction of IL-33 with its receptors	0:67	Structural insights into the interaction of IL-33 with its receptors.
23980170	9	35	theme	ligand-receptor	1674:1688	arg1	assembly					1690:1697	ligand-receptor assembly	1674:1697	ligand-receptor assembly	1674:1697	The collective results confer IL-33 structure-function relationships, supporting and extending a general model for ligand-receptor assembly and activation in the IL-1 family.
23980170	2	36	theme	receptor	279:286	arg1	ST2					288:290	its ligand-binding primary receptor ST2	252:290	its ligand-binding primary receptor ST2	252:290	It signals through its ligand-binding primary receptor ST2 and IL-1 receptor accessory protein (IL-1RAcP), both of which are members of the IL-1 receptor family.
23980170	2	37	theme	receptor	378:385	arg1	family					387:392	the IL-1 receptor family	369:392	the IL-1 receptor family	369:392	It signals through its ligand-binding primary receptor ST2 and IL-1 receptor accessory protein (IL-1RAcP), both of which are members of the IL-1 receptor family.
23980170	4	38	theme	molecular	655:663	arg1	mechanism					665:673	the molecular mechanism	651:673	the molecular mechanism by which ST2 specifically recognizes IL-33	651:716	Coupled with structure-based mutagenesis and binding assay, the structural results define the molecular mechanism by which ST2 specifically recognizes IL-33.
23980170	8	39	theme	crystal	1539:1545	arg1	structures					1547:1556	crystal structures	1539:1556	crystal structures	1539:1556	The solution architecture of IL-33-ST2-IL-1RAcP complex from small-angle X-ray-scattering analysis resembles IL-1β-IL-1RII-IL-1RAcP and IL-1β-IL-1RI-IL-1RAcP crystal structures.
23980170	2	40	theme	primary	271:277	arg1	ST2					288:290	its ligand-binding primary receptor ST2	252:290	its ligand-binding primary receptor ST2	252:290	It signals through its ligand-binding primary receptor ST2 and IL-1 receptor accessory protein (IL-1RAcP), both of which are members of the IL-1 receptor family.
23980170	6	41	theme	D1D2	1060:1063	arg1	module					1065:1070	D1D2 module	1060:1070	D1D2 module	1060:1070	Combined crystallography and small-angle X-ray-scattering studies reveal that ST2 possesses hinge flexibility between the D3 domain and D1D2 module, whereas IL-1RAcP exhibits a rigid conformation in the unbound state in solution.
23980170	2	42	theme	IL-1	373:376	arg1	family					387:392	the IL-1 receptor family	369:392	the IL-1 receptor family	369:392	It signals through its ligand-binding primary receptor ST2 and IL-1 receptor accessory protein (IL-1RAcP), both of which are members of the IL-1 receptor family.
23980170	6	43	theme	small-angle	953:963	arg1	studies					982:988	Combined crystallography and small-angle X-ray-scattering studies	924:988	studies	982:988	Combined crystallography and small-angle X-ray-scattering studies reveal that ST2 possesses hinge flexibility between the D3 domain and D1D2 module, whereas IL-1RAcP exhibits a rigid conformation in the unbound state in solution.
23980170	2	44	theme	family	387:392	arg1	members					358:364	members	358:364	members of the IL-1 receptor family	358:392	It signals through its ligand-binding primary receptor ST2 and IL-1 receptor accessory protein (IL-1RAcP), both of which are members of the IL-1 receptor family.
23980170	2	44	theme	family	387:392	arg1	both					340:343	both	340:343	both	340:343	It signals through its ligand-binding primary receptor ST2 and IL-1 receptor accessory protein (IL-1RAcP), both of which are members of the IL-1 receptor family.
23980170	2	44	theme	family	387:392	arg1	protein					320:326	IL-1 receptor accessory protein	296:326	IL-1 receptor accessory protein (IL-1RAcP)	296:337	It signals through its ligand-binding primary receptor ST2 and IL-1 receptor accessory protein (IL-1RAcP), both of which are members of the IL-1 receptor family.
23980170	2	44	theme	family	387:392	arg1	ST2					288:290	its ligand-binding primary receptor ST2	252:290	its ligand-binding primary receptor ST2	252:290	It signals through its ligand-binding primary receptor ST2 and IL-1 receptor accessory protein (IL-1RAcP), both of which are members of the IL-1 receptor family.
23980170	2	45	theme	ligand-binding	256:269	arg1	ST2					288:290	its ligand-binding primary receptor ST2	252:290	its ligand-binding primary receptor ST2	252:290	It signals through its ligand-binding primary receptor ST2 and IL-1 receptor accessory protein (IL-1RAcP), both of which are members of the IL-1 receptor family.
23980170	8	46	from	analysis	1471:1478	arg1	architecture					1394:1405	The solution architecture	1381:1405	The solution architecture of IL-33-ST2-IL-1RAcP complex from small-angle X-ray-scattering analysis	1381:1478	The solution architecture of IL-33-ST2-IL-1RAcP complex from small-angle X-ray-scattering analysis resembles IL-1β-IL-1RII-IL-1RAcP and IL-1β-IL-1RI-IL-1RAcP crystal structures.
23980170	8	46	from	analysis	1471:1478	arg1	complex					1429:1435	IL-33-ST2-IL-1RAcP complex	1410:1435	IL-33-ST2-IL-1RAcP complex from small-angle X-ray-scattering analysis	1410:1478	The solution architecture of IL-33-ST2-IL-1RAcP complex from small-angle X-ray-scattering analysis resembles IL-1β-IL-1RII-IL-1RAcP and IL-1β-IL-1RI-IL-1RAcP crystal structures.
23980170	1	47	theme	innate	167:172	arg1	responses					194:202	innate and adaptive immune responses	167:202	innate and adaptive immune responses in host defense and disease	167:230	Interleukin (IL)-33 is an important member of the IL-1 family that has pleiotropic activities in innate and adaptive immune responses in host defense and disease.
23980170	4	48	theme	structural	625:634	arg1	results					636:642	the structural results	621:642	the structural results	621:642	Coupled with structure-based mutagenesis and binding assay, the structural results define the molecular mechanism by which ST2 specifically recognizes IL-33.
23980170	3	49	theme	crystal	469:475	arg1	structure					477:485	the crystal structure	465:485	the crystal structure of IL-33 in complex with the ectodomain of ST2	465:532	To clarify the interaction of IL-33 with its receptors, we determined the crystal structure of IL-33 in complex with the ectodomain of ST2 at a resolution of 3.27 Å.
23980170	8	50	theme	complex	1429:1435	arg1	architecture					1394:1405	The solution architecture	1381:1405	The solution architecture of IL-33-ST2-IL-1RAcP complex from small-angle X-ray-scattering analysis	1381:1478	The solution architecture of IL-33-ST2-IL-1RAcP complex from small-angle X-ray-scattering analysis resembles IL-1β-IL-1RII-IL-1RAcP and IL-1β-IL-1RI-IL-1RAcP crystal structures.
23980170	9	51	theme	collective	1563:1572	arg1	results					1574:1580	The collective results	1559:1580	The collective results	1559:1580	The collective results confer IL-33 structure-function relationships, supporting and extending a general model for ligand-receptor assembly and activation in the IL-1 family.
23980170	5	52	theme	Structural	719:728	arg1	comparison					730:739	Structural comparison	719:739	Structural comparison with other ligand-receptor complexes in the IL-1 family	719:795	Structural comparison with other ligand-receptor complexes in the IL-1 family indicates that surface-charge complementarity is critical in determining ligand-binding specificity of IL-1 primary receptors.
23980170	3	53	with	interaction	410:420	arg1	receptors					440:448	its receptors	436:448	its receptors	436:448	To clarify the interaction of IL-33 with its receptors, we determined the crystal structure of IL-33 in complex with the ectodomain of ST2 at a resolution of 3.27 Å.
23980170	1	54	contain	has	137:139	arg1	IL					83:84	Interleukin (IL)-33	70:88	Interleukin (IL)-33	70:88	Interleukin (IL)-33 is an important member of the IL-1 family that has pleiotropic activities in innate and adaptive immune responses in host defense and disease.
23980170	1	54	contain	has	137:139	arg1	member					106:111	an important member	93:111	an important member of the IL-1 family that has pleiotropic activities in innate and adaptive immune responses in host defense and disease	93:230	Interleukin (IL)-33 is an important member of the IL-1 family that has pleiotropic activities in innate and adaptive immune responses in host defense and disease.
23980170	1	54	contain	has	137:139	arg2	activities					153:162	pleiotropic activities	141:162	pleiotropic activities in innate and adaptive immune responses in host defense and disease	141:230	Interleukin (IL)-33 is an important member of the IL-1 family that has pleiotropic activities in innate and adaptive immune responses in host defense and disease.
23980170	3	55	theme	ST2	530:532	arg1	ST2					530:532	ST2	530:532	ST2	530:532	To clarify the interaction of IL-33 with its receptors, we determined the crystal structure of IL-33 in complex with the ectodomain of ST2 at a resolution of 3.27 Å.
23980170	3	55	theme	ST2	530:532	arg1	ectodomain					516:525	the ectodomain	512:525	the ectodomain of ST2	512:532	To clarify the interaction of IL-33 with its receptors, we determined the crystal structure of IL-33 in complex with the ectodomain of ST2 at a resolution of 3.27 Å.
23980170	1	56	theme	adaptive	178:185	arg1	responses					194:202	innate and adaptive immune responses	167:202	innate and adaptive immune responses in host defense and disease	167:230	Interleukin (IL)-33 is an important member of the IL-1 family that has pleiotropic activities in innate and adaptive immune responses in host defense and disease.
23980170	6	57	theme	Combined	924:931	arg1	crystallography					933:947	Combined crystallography and small-angle X-ray-scattering studies	924:988	crystallography	933:947	Combined crystallography and small-angle X-ray-scattering studies reveal that ST2 possesses hinge flexibility between the D3 domain and D1D2 module, whereas IL-1RAcP exhibits a rigid conformation in the unbound state in solution.
23980170	8	58	theme	solution	1385:1392	arg1	architecture					1394:1405	The solution architecture	1381:1405	The solution architecture of IL-33-ST2-IL-1RAcP complex from small-angle X-ray-scattering analysis	1381:1478	The solution architecture of IL-33-ST2-IL-1RAcP complex from small-angle X-ray-scattering analysis resembles IL-1β-IL-1RII-IL-1RAcP and IL-1β-IL-1RI-IL-1RAcP crystal structures.
23980170	3	59	theme	Å	558:558	arg1	resolution					539:548	a resolution	537:548	a resolution of 3.27 Å	537:558	To clarify the interaction of IL-33 with its receptors, we determined the crystal structure of IL-33 in complex with the ectodomain of ST2 at a resolution of 3.27 Å.
23980170	8	60	theme	small-angle	1442:1452	arg1	analysis					1471:1478	small-angle X-ray-scattering analysis	1442:1478	small-angle X-ray-scattering analysis	1442:1478	The solution architecture of IL-33-ST2-IL-1RAcP complex from small-angle X-ray-scattering analysis resembles IL-1β-IL-1RII-IL-1RAcP and IL-1β-IL-1RI-IL-1RAcP crystal structures.
23980170	6	61	theme	unbound	1127:1133	arg1	state					1135:1139	the unbound state	1123:1139	the unbound state in solution	1123:1151	Combined crystallography and small-angle X-ray-scattering studies reveal that ST2 possesses hinge flexibility between the D3 domain and D1D2 module, whereas IL-1RAcP exhibits a rigid conformation in the unbound state in solution.
23980170	2	62	theme	accessory	310:318	arg1	IL-1RAcP					329:336	IL-1RAcP	329:336	IL-1RAcP	329:336	It signals through its ligand-binding primary receptor ST2 and IL-1 receptor accessory protein (IL-1RAcP), both of which are members of the IL-1 receptor family.
23980170	2	62	theme	accessory	310:318	arg1	protein					320:326	IL-1 receptor accessory protein	296:326	IL-1 receptor accessory protein (IL-1RAcP)	296:337	It signals through its ligand-binding primary receptor ST2 and IL-1 receptor accessory protein (IL-1RAcP), both of which are members of the IL-1 receptor family.
23980170	0	63	theme	IL-33	44:48	arg1	interaction					29:39	the interaction	25:39	the interaction of IL-33 with its receptors	25:67	Structural insights into the interaction of IL-33 with its receptors.
23980170	6	64	from	state	1135:1139	arg1	solution					1144:1151	solution	1144:1151	solution	1144:1151	Combined crystallography and small-angle X-ray-scattering studies reveal that ST2 possesses hinge flexibility between the D3 domain and D1D2 module, whereas IL-1RAcP exhibits a rigid conformation in the unbound state in solution.
23980170	2	65	theme	receptor	301:308	arg1	IL-1RAcP					329:336	IL-1RAcP	329:336	IL-1RAcP	329:336	It signals through its ligand-binding primary receptor ST2 and IL-1 receptor accessory protein (IL-1RAcP), both of which are members of the IL-1 receptor family.
23980170	2	65	theme	receptor	301:308	arg1	protein					320:326	IL-1 receptor accessory protein	296:326	IL-1 receptor accessory protein (IL-1RAcP)	296:337	It signals through its ligand-binding primary receptor ST2 and IL-1 receptor accessory protein (IL-1RAcP), both of which are members of the IL-1 receptor family.
23980170	3	66	with	complex	499:505	arg1	ST2					530:532	ST2	530:532	ST2	530:532	To clarify the interaction of IL-33 with its receptors, we determined the crystal structure of IL-33 in complex with the ectodomain of ST2 at a resolution of 3.27 Å.
23980170	3	66	with	complex	499:505	arg1	ectodomain					516:525	the ectodomain	512:525	the ectodomain of ST2	512:532	To clarify the interaction of IL-33 with its receptors, we determined the crystal structure of IL-33 in complex with the ectodomain of ST2 at a resolution of 3.27 Å.
23980170	8	67	theme	IL-33-ST2-IL-1RAcP	1410:1427	arg1	complex					1429:1435	IL-33-ST2-IL-1RAcP complex	1410:1435	IL-33-ST2-IL-1RAcP complex from small-angle X-ray-scattering analysis	1410:1478	The solution architecture of IL-33-ST2-IL-1RAcP complex from small-angle X-ray-scattering analysis resembles IL-1β-IL-1RII-IL-1RAcP and IL-1β-IL-1RI-IL-1RAcP crystal structures.
23980170	1	68	theme	important	96:104	arg1	IL					83:84	Interleukin (IL)-33	70:88	Interleukin (IL)-33	70:88	Interleukin (IL)-33 is an important member of the IL-1 family that has pleiotropic activities in innate and adaptive immune responses in host defense and disease.
23980170	1	68	theme	important	96:104	arg1	member					106:111	an important member	93:111	an important member of the IL-1 family that has pleiotropic activities in innate and adaptive immune responses in host defense and disease	93:230	Interleukin (IL)-33 is an important member of the IL-1 family that has pleiotropic activities in innate and adaptive immune responses in host defense and disease.
23980170	3	69	theme	IL-33	490:494	arg1	structure					477:485	the crystal structure	465:485	the crystal structure of IL-33 in complex with the ectodomain of ST2	465:532	To clarify the interaction of IL-33 with its receptors, we determined the crystal structure of IL-33 in complex with the ectodomain of ST2 at a resolution of 3.27 Å.
23980170	1	70	theme	immune	187:192	arg1	responses					194:202	innate and adaptive immune responses	167:202	innate and adaptive immune responses in host defense and disease	167:230	Interleukin (IL)-33 is an important member of the IL-1 family that has pleiotropic activities in innate and adaptive immune responses in host defense and disease.
23980170	1	71	from	responses	194:202	arg1	disease					224:230	disease	224:230	disease	224:230	Interleukin (IL)-33 is an important member of the IL-1 family that has pleiotropic activities in innate and adaptive immune responses in host defense and disease.
23980170	1	71	from	responses	194:202	arg1	defense					212:218	host defense	207:218	host defense	207:218	Interleukin (IL)-33 is an important member of the IL-1 family that has pleiotropic activities in innate and adaptive immune responses in host defense and disease.
23980170	8	72	theme	X-ray-scattering	1454:1469	arg1	analysis					1471:1478	small-angle X-ray-scattering analysis	1442:1478	small-angle X-ray-scattering analysis	1442:1478	The solution architecture of IL-33-ST2-IL-1RAcP complex from small-angle X-ray-scattering analysis resembles IL-1β-IL-1RII-IL-1RAcP and IL-1β-IL-1RI-IL-1RAcP crystal structures.
23980170	3	73	theme	IL-33	425:429	arg1	interaction					410:420	the interaction	406:420	the interaction of IL-33 with its receptors	406:448	To clarify the interaction of IL-33 with its receptors, we determined the crystal structure of IL-33 in complex with the ectodomain of ST2 at a resolution of 3.27 Å.
23980170	2	74	theme	IL-1	296:299	arg1	IL-1RAcP					329:336	IL-1RAcP	329:336	IL-1RAcP	329:336	It signals through its ligand-binding primary receptor ST2 and IL-1 receptor accessory protein (IL-1RAcP), both of which are members of the IL-1 receptor family.
23980170	2	74	theme	IL-1	296:299	arg1	protein					320:326	IL-1 receptor accessory protein	296:326	IL-1 receptor accessory protein (IL-1RAcP)	296:337	It signals through its ligand-binding primary receptor ST2 and IL-1 receptor accessory protein (IL-1RAcP), both of which are members of the IL-1 receptor family.
23980170	6	75	theme	D3	1046:1047	arg1	domain					1049:1054	the D3 domain	1042:1054	the D3 domain	1042:1054	Combined crystallography and small-angle X-ray-scattering studies reveal that ST2 possesses hinge flexibility between the D3 domain and D1D2 module, whereas IL-1RAcP exhibits a rigid conformation in the unbound state in solution.
23980170	1	76	from	activities	153:162	arg1	responses					194:202	innate and adaptive immune responses	167:202	innate and adaptive immune responses in host defense and disease	167:230	Interleukin (IL)-33 is an important member of the IL-1 family that has pleiotropic activities in innate and adaptive immune responses in host defense and disease.
23980170	7	77	theme	receptors	1272:1280	arg1	change					1249:1254	domain-level conformational change	1221:1254	domain-level conformational change of IL-1 primary receptors upon ligand binding	1221:1300	The molecular flexibility of ST2 provides structural insights into domain-level conformational change of IL-1 primary receptors upon ligand binding, and the rigidity of IL-1RAcP explains its inability to bind ligands directly.
23980170	9	78	from	assembly	1690:1697	arg1	family					1726:1731	the IL-1 family	1717:1731	the IL-1 family	1717:1731	The collective results confer IL-33 structure-function relationships, supporting and extending a general model for ligand-receptor assembly and activation in the IL-1 family.
23980170	6	79	theme	hinge	1016:1020	arg1	flexibility					1022:1032	hinge flexibility	1016:1032	hinge flexibility between the D3 domain and D1D2 module	1016:1070	Combined crystallography and small-angle X-ray-scattering studies reveal that ST2 possesses hinge flexibility between the D3 domain and D1D2 module, whereas IL-1RAcP exhibits a rigid conformation in the unbound state in solution.
23980170	7	80	theme	ligand	1287:1292	arg1	binding					1294:1300	ligand binding	1287:1300	ligand binding	1287:1300	The molecular flexibility of ST2 provides structural insights into domain-level conformational change of IL-1 primary receptors upon ligand binding, and the rigidity of IL-1RAcP explains its inability to bind ligands directly.
23980170	4	81	theme	binding	606:612	arg1	assay					614:618	binding assay	606:618	binding assay	606:618	Coupled with structure-based mutagenesis and binding assay, the structural results define the molecular mechanism by which ST2 specifically recognizes IL-33.
23980170	7	82	theme	ST2	1183:1185	arg1	flexibility					1168:1178	The molecular flexibility	1154:1178	The molecular flexibility of ST2	1154:1185	The molecular flexibility of ST2 provides structural insights into domain-level conformational change of IL-1 primary receptors upon ligand binding, and the rigidity of IL-1RAcP explains its inability to bind ligands directly.
23980170	1	83	theme	host	207:210	arg1	defense					212:218	host defense	207:218	host defense	207:218	Interleukin (IL)-33 is an important member of the IL-1 family that has pleiotropic activities in innate and adaptive immune responses in host defense and disease.
2493268	0	0	theme	protein	82:88	arg1	forms					50:54	the glycosylated forms	33:54	the glycosylated forms of human pancreatic stone protein	33:88	N-terminal sequence extension in the glycosylated forms of human pancreatic stone protein.
2493268	0	1	from	extension	20:28	arg1	forms					50:54	the glycosylated forms	33:54	the glycosylated forms of human pancreatic stone protein	33:88	N-terminal sequence extension in the glycosylated forms of human pancreatic stone protein.
2493268	1	2	theme	amino	154:158	arg1	residue					165:171	the 5th amino acid residue	146:171	the 5th amino acid residue	146:171	The 5-oxoproline N-terminal chain is O-glycosylated on the 5th amino acid residue.
2493268	4	3	from	differences	658:668	arg1	Mr					677:678	the Mr	673:678	the Mr of PSP S2-5	673:690	Variations in the glycan chain composition account for the differences in the Mr of PSP S2-5.
2493268	0	4	theme	stone	76:80	arg1	protein					82:88	human pancreatic stone protein	59:88	human pancreatic stone protein	59:88	N-terminal sequence extension in the glycosylated forms of human pancreatic stone protein.
2493268	5	5	from	soluble	721:727	arg1	solutions					740:748	aqueous solutions	732:748	aqueous solutions between the pH values 5.0-9.0	732:778	The PSP S2-5 forms are very soluble in aqueous solutions between the pH values 5.0-9.0, whereas the proteolysated form is scarcely soluble.
2493268	1	6	theme	acid	160:163	arg1	residue					165:171	the 5th amino acid residue	146:171	the 5th amino acid residue	146:171	The 5-oxoproline N-terminal chain is O-glycosylated on the 5th amino acid residue.
2493268	3	7	theme	molecules	588:596	arg1	chain					567:571	the single carbohydrate chain	543:571	the single carbohydrate chain of the protein molecules	543:596	Among the eleven amino acids of the PSP S2-5 N-terminal extension Z-E-A-Q-T-E-L-P-Q-A-R, the first residue is an oxoproline and the fifth, a threonine, bears the single carbohydrate chain of the protein molecules.
2493268	4	8	theme	chain	624:628	arg1	composition					630:640	the glycan chain composition	613:640	the glycan chain composition	613:640	Variations in the glycan chain composition account for the differences in the Mr of PSP S2-5.
2493268	4	9	theme	PSP	683:685	arg1	S2-5					687:690	PSP S2-5	683:690	PSP S2-5	683:690	Variations in the glycan chain composition account for the differences in the Mr of PSP S2-5.
2493268	5	10	theme	proteolysated	793:805	arg1	form					807:810	the proteolysated form	789:810	the proteolysated form	789:810	The PSP S2-5 forms are very soluble in aqueous solutions between the pH values 5.0-9.0, whereas the proteolysated form is scarcely soluble.
2493268	5	10	theme	proteolysated	793:805	arg1	soluble					824:830	soluble	824:830	soluble	824:830	The PSP S2-5 forms are very soluble in aqueous solutions between the pH values 5.0-9.0, whereas the proteolysated form is scarcely soluble.
2493268	2	11	theme	protein	269:275	arg1	forms					277:281	the immunoreactive protein forms	250:281	the immunoreactive protein forms detected in human pancreatic juice (PSP S2-5)	250:327	The pancreatic stone protein isolated from human calculi (PSP) derives from the immunoreactive protein forms detected in human pancreatic juice (PSP S2-5) through the tryptic cleavage of the Arg-11-Ile-12 bond.
2493268	2	12	attach	isolated	203:210	arg2	protein					195:201	The pancreatic stone protein	174:201	The pancreatic stone protein isolated from human calculi (PSP)	174:235	The pancreatic stone protein isolated from human calculi (PSP) derives from the immunoreactive protein forms detected in human pancreatic juice (PSP S2-5) through the tryptic cleavage of the Arg-11-Ile-12 bond.
2493268	2	12	attach	isolated	203:210	arg1	PSP					232:234	PSP	232:234	PSP	232:234	The pancreatic stone protein isolated from human calculi (PSP) derives from the immunoreactive protein forms detected in human pancreatic juice (PSP S2-5) through the tryptic cleavage of the Arg-11-Ile-12 bond.
2493268	2	12	attach	isolated	203:210	arg1	calculi					223:229	human calculi	217:229	human calculi (PSP)	217:235	The pancreatic stone protein isolated from human calculi (PSP) derives from the immunoreactive protein forms detected in human pancreatic juice (PSP S2-5) through the tryptic cleavage of the Arg-11-Ile-12 bond.
2493268	5	13	theme	PSP	697:699	arg1	whereas					781:787	whereas	781:787	whereas	781:787	The PSP S2-5 forms are very soluble in aqueous solutions between the pH values 5.0-9.0, whereas the proteolysated form is scarcely soluble.
2493268	5	13	theme	PSP	697:699	arg1	forms					706:710	The PSP S2-5 forms	693:710	The PSP S2-5 forms	693:710	The PSP S2-5 forms are very soluble in aqueous solutions between the pH values 5.0-9.0, whereas the proteolysated form is scarcely soluble.
2493268	5	13	theme	PSP	697:699	arg1	soluble					721:727	soluble	721:727	soluble	721:727	The PSP S2-5 forms are very soluble in aqueous solutions between the pH values 5.0-9.0, whereas the proteolysated form is scarcely soluble.
2493268	2	14	theme	immunoreactive	254:267	arg1	forms					277:281	the immunoreactive protein forms	250:281	the immunoreactive protein forms detected in human pancreatic juice (PSP S2-5)	250:327	The pancreatic stone protein isolated from human calculi (PSP) derives from the immunoreactive protein forms detected in human pancreatic juice (PSP S2-5) through the tryptic cleavage of the Arg-11-Ile-12 bond.
2493268	2	15	theme	Arg-11-Ile-12	365:377	arg1	bond					379:382	the Arg-11-Ile-12 bond	361:382	the Arg-11-Ile-12 bond	361:382	The pancreatic stone protein isolated from human calculi (PSP) derives from the immunoreactive protein forms detected in human pancreatic juice (PSP S2-5) through the tryptic cleavage of the Arg-11-Ile-12 bond.
2493268	0	16	theme	sequence	11:18	arg1	extension					20:28	N-terminal sequence extension	0:28	N-terminal sequence extension in the glycosylated forms of human pancreatic stone protein	0:88	N-terminal sequence extension in the glycosylated forms of human pancreatic stone protein.
2493268	5	17	dep	soluble	721:727	arg1	whereas					781:787	whereas	781:787	whereas	781:787	The PSP S2-5 forms are very soluble in aqueous solutions between the pH values 5.0-9.0, whereas the proteolysated form is scarcely soluble.
2493268	5	17	dep	soluble	721:727	arg1	forms					706:710	The PSP S2-5 forms	693:710	The PSP S2-5 forms	693:710	The PSP S2-5 forms are very soluble in aqueous solutions between the pH values 5.0-9.0, whereas the proteolysated form is scarcely soluble.
2493268	5	17	dep	soluble	721:727	arg1	soluble					721:727	soluble	721:727	soluble	721:727	The PSP S2-5 forms are very soluble in aqueous solutions between the pH values 5.0-9.0, whereas the proteolysated form is scarcely soluble.
2493268	5	18	theme	S2-5	701:704	arg1	whereas					781:787	whereas	781:787	whereas	781:787	The PSP S2-5 forms are very soluble in aqueous solutions between the pH values 5.0-9.0, whereas the proteolysated form is scarcely soluble.
2493268	5	18	theme	S2-5	701:704	arg1	forms					706:710	The PSP S2-5 forms	693:710	The PSP S2-5 forms	693:710	The PSP S2-5 forms are very soluble in aqueous solutions between the pH values 5.0-9.0, whereas the proteolysated form is scarcely soluble.
2493268	5	18	theme	S2-5	701:704	arg1	soluble					721:727	soluble	721:727	soluble	721:727	The PSP S2-5 forms are very soluble in aqueous solutions between the pH values 5.0-9.0, whereas the proteolysated form is scarcely soluble.
2493268	3	19	theme	amino	402:406	arg1	acids					408:412	the eleven amino acids	391:412	the eleven amino acids of the PSP S2-5 N-terminal extension Z-E-A-Q-T-E-L-P-Q-A-R	391:471	Among the eleven amino acids of the PSP S2-5 N-terminal extension Z-E-A-Q-T-E-L-P-Q-A-R, the first residue is an oxoproline and the fifth, a threonine, bears the single carbohydrate chain of the protein molecules.
2493268	0	20	theme	N-terminal	0:9	arg1	extension					20:28	N-terminal sequence extension	0:28	N-terminal sequence extension in the glycosylated forms of human pancreatic stone protein	0:88	N-terminal sequence extension in the glycosylated forms of human pancreatic stone protein.
2493268	2	21	theme	pancreatic	301:310	arg1	S2-5					323:326	PSP S2-5	319:326	PSP S2-5	319:326	The pancreatic stone protein isolated from human calculi (PSP) derives from the immunoreactive protein forms detected in human pancreatic juice (PSP S2-5) through the tryptic cleavage of the Arg-11-Ile-12 bond.
2493268	2	21	theme	pancreatic	301:310	arg1	juice					312:316	human pancreatic juice	295:316	human pancreatic juice (PSP S2-5)	295:327	The pancreatic stone protein isolated from human calculi (PSP) derives from the immunoreactive protein forms detected in human pancreatic juice (PSP S2-5) through the tryptic cleavage of the Arg-11-Ile-12 bond.
2493268	5	22	theme	pH	762:763	arg1	values					765:770	the pH values 5.0-9.0	758:778	the pH values 5.0-9.0	758:778	The PSP S2-5 forms are very soluble in aqueous solutions between the pH values 5.0-9.0, whereas the proteolysated form is scarcely soluble.
2493268	3	23	theme	single	547:552	arg1	chain					567:571	the single carbohydrate chain	543:571	the single carbohydrate chain of the protein molecules	543:596	Among the eleven amino acids of the PSP S2-5 N-terminal extension Z-E-A-Q-T-E-L-P-Q-A-R, the first residue is an oxoproline and the fifth, a threonine, bears the single carbohydrate chain of the protein molecules.
2493268	1	24	theme	5-oxoproline	95:106	arg1	O-glycosylated					128:141	O-glycosylated	128:141	O-glycosylated	128:141	The 5-oxoproline N-terminal chain is O-glycosylated on the 5th amino acid residue.
2493268	1	24	theme	5-oxoproline	95:106	arg1	chain					119:123	The 5-oxoproline N-terminal chain	91:123	The 5-oxoproline N-terminal chain	91:123	The 5-oxoproline N-terminal chain is O-glycosylated on the 5th amino acid residue.
2493268	3	25	theme	N-terminal	430:439	arg1	Z-E-A-Q-T-E-L-P-Q-A-R					451:471	the PSP S2-5 N-terminal extension Z-E-A-Q-T-E-L-P-Q-A-R	417:471	the PSP S2-5 N-terminal extension Z-E-A-Q-T-E-L-P-Q-A-R	417:471	Among the eleven amino acids of the PSP S2-5 N-terminal extension Z-E-A-Q-T-E-L-P-Q-A-R, the first residue is an oxoproline and the fifth, a threonine, bears the single carbohydrate chain of the protein molecules.
2493268	4	26	theme	S2-5	687:690	arg1	Mr					677:678	the Mr	673:678	the Mr of PSP S2-5	673:690	Variations in the glycan chain composition account for the differences in the Mr of PSP S2-5.
2493268	3	27	contain	bears	537:541	arg1	fifth					517:521	fifth	517:521	fifth	517:521	Among the eleven amino acids of the PSP S2-5 N-terminal extension Z-E-A-Q-T-E-L-P-Q-A-R, the first residue is an oxoproline and the fifth, a threonine, bears the single carbohydrate chain of the protein molecules.
2493268	3	27	contain	bears	537:541	arg1	threonine					526:534	a threonine	524:534	a threonine	524:534	Among the eleven amino acids of the PSP S2-5 N-terminal extension Z-E-A-Q-T-E-L-P-Q-A-R, the first residue is an oxoproline and the fifth, a threonine, bears the single carbohydrate chain of the protein molecules.
2493268	3	27	contain	bears	537:541	arg2	chain					567:571	the single carbohydrate chain	543:571	the single carbohydrate chain of the protein molecules	543:596	Among the eleven amino acids of the PSP S2-5 N-terminal extension Z-E-A-Q-T-E-L-P-Q-A-R, the first residue is an oxoproline and the fifth, a threonine, bears the single carbohydrate chain of the protein molecules.
2493268	2	28	theme	pancreatic	178:187	arg1	protein					195:201	The pancreatic stone protein	174:201	The pancreatic stone protein isolated from human calculi (PSP)	174:235	The pancreatic stone protein isolated from human calculi (PSP) derives from the immunoreactive protein forms detected in human pancreatic juice (PSP S2-5) through the tryptic cleavage of the Arg-11-Ile-12 bond.
2493268	1	29	theme	N-terminal	108:117	arg1	O-glycosylated					128:141	O-glycosylated	128:141	O-glycosylated	128:141	The 5-oxoproline N-terminal chain is O-glycosylated on the 5th amino acid residue.
2493268	1	29	theme	N-terminal	108:117	arg1	chain					119:123	The 5-oxoproline N-terminal chain	91:123	The 5-oxoproline N-terminal chain	91:123	The 5-oxoproline N-terminal chain is O-glycosylated on the 5th amino acid residue.
2493268	4	30	from	Variations	599:608	arg1	composition					630:640	the glycan chain composition	613:640	the glycan chain composition	613:640	Variations in the glycan chain composition account for the differences in the Mr of PSP S2-5.
2493268	3	31	theme	extension	441:449	arg1	Z-E-A-Q-T-E-L-P-Q-A-R					451:471	the PSP S2-5 N-terminal extension Z-E-A-Q-T-E-L-P-Q-A-R	417:471	the PSP S2-5 N-terminal extension Z-E-A-Q-T-E-L-P-Q-A-R	417:471	Among the eleven amino acids of the PSP S2-5 N-terminal extension Z-E-A-Q-T-E-L-P-Q-A-R, the first residue is an oxoproline and the fifth, a threonine, bears the single carbohydrate chain of the protein molecules.
2493268	0	32	theme	glycosylated	37:48	arg1	forms					50:54	the glycosylated forms	33:54	the glycosylated forms of human pancreatic stone protein	33:88	N-terminal sequence extension in the glycosylated forms of human pancreatic stone protein.
2493268	3	33	theme	carbohydrate	554:565	arg1	chain					567:571	the single carbohydrate chain	543:571	the single carbohydrate chain of the protein molecules	543:596	Among the eleven amino acids of the PSP S2-5 N-terminal extension Z-E-A-Q-T-E-L-P-Q-A-R, the first residue is an oxoproline and the fifth, a threonine, bears the single carbohydrate chain of the protein molecules.
2493268	3	34	theme	PSP	421:423	arg1	Z-E-A-Q-T-E-L-P-Q-A-R					451:471	the PSP S2-5 N-terminal extension Z-E-A-Q-T-E-L-P-Q-A-R	417:471	the PSP S2-5 N-terminal extension Z-E-A-Q-T-E-L-P-Q-A-R	417:471	Among the eleven amino acids of the PSP S2-5 N-terminal extension Z-E-A-Q-T-E-L-P-Q-A-R, the first residue is an oxoproline and the fifth, a threonine, bears the single carbohydrate chain of the protein molecules.
2493268	2	35	theme	bond	379:382	arg1	cleavage					349:356	the tryptic cleavage	337:356	the tryptic cleavage of the Arg-11-Ile-12 bond	337:382	The pancreatic stone protein isolated from human calculi (PSP) derives from the immunoreactive protein forms detected in human pancreatic juice (PSP S2-5) through the tryptic cleavage of the Arg-11-Ile-12 bond.
2493268	1	36	gly	O-glycosylated	128:141	arg2	chain					119:123	The 5-oxoproline N-terminal chain	91:123	The 5-oxoproline N-terminal chain	91:123	The 5-oxoproline N-terminal chain is O-glycosylated on the 5th amino acid residue.
2493268	1	36	gly	O-glycosylated	128:141	arg2	O-glycosylated					128:141	O-glycosylated	128:141	O-glycosylated	128:141	The 5-oxoproline N-terminal chain is O-glycosylated on the 5th amino acid residue.
2493268	1	36	gly	O-glycosylated	128:141	arg2	residue					165:171	the 5th amino acid residue	146:171	the 5th amino acid residue	146:171	The 5-oxoproline N-terminal chain is O-glycosylated on the 5th amino acid residue.
2493268	1	36	gly	O-glycosylated	128:141	arg1	chain					119:123	The 5-oxoproline N-terminal chain	91:123	The 5-oxoproline N-terminal chain	91:123	The 5-oxoproline N-terminal chain is O-glycosylated on the 5th amino acid residue.
2493268	1	36	gly	O-glycosylated	128:141	arg1	O-glycosylated					128:141	O-glycosylated	128:141	O-glycosylated	128:141	The 5-oxoproline N-terminal chain is O-glycosylated on the 5th amino acid residue.
2493268	1	36	gly	O-glycosylated	128:141	arg1	residue					165:171	the 5th amino acid residue	146:171	the 5th amino acid residue	146:171	The 5-oxoproline N-terminal chain is O-glycosylated on the 5th amino acid residue.
2493268	3	37	theme	S2-5	425:428	arg1	Z-E-A-Q-T-E-L-P-Q-A-R					451:471	the PSP S2-5 N-terminal extension Z-E-A-Q-T-E-L-P-Q-A-R	417:471	the PSP S2-5 N-terminal extension Z-E-A-Q-T-E-L-P-Q-A-R	417:471	Among the eleven amino acids of the PSP S2-5 N-terminal extension Z-E-A-Q-T-E-L-P-Q-A-R, the first residue is an oxoproline and the fifth, a threonine, bears the single carbohydrate chain of the protein molecules.
2493268	5	38	theme	aqueous	732:738	arg1	solutions					740:748	aqueous solutions	732:748	aqueous solutions between the pH values 5.0-9.0	732:778	The PSP S2-5 forms are very soluble in aqueous solutions between the pH values 5.0-9.0, whereas the proteolysated form is scarcely soluble.
2493268	2	39	located	detected	283:290	arg1	S2-5					323:326	PSP S2-5	319:326	PSP S2-5	319:326	The pancreatic stone protein isolated from human calculi (PSP) derives from the immunoreactive protein forms detected in human pancreatic juice (PSP S2-5) through the tryptic cleavage of the Arg-11-Ile-12 bond.
2493268	2	39	located	detected	283:290	arg2	forms					277:281	the immunoreactive protein forms	250:281	the immunoreactive protein forms detected in human pancreatic juice (PSP S2-5)	250:327	The pancreatic stone protein isolated from human calculi (PSP) derives from the immunoreactive protein forms detected in human pancreatic juice (PSP S2-5) through the tryptic cleavage of the Arg-11-Ile-12 bond.
2493268	2	39	located	detected	283:290	arg1	juice					312:316	human pancreatic juice	295:316	human pancreatic juice (PSP S2-5)	295:327	The pancreatic stone protein isolated from human calculi (PSP) derives from the immunoreactive protein forms detected in human pancreatic juice (PSP S2-5) through the tryptic cleavage of the Arg-11-Ile-12 bond.
2493268	2	40	theme	human	217:221	arg1	PSP					232:234	PSP	232:234	PSP	232:234	The pancreatic stone protein isolated from human calculi (PSP) derives from the immunoreactive protein forms detected in human pancreatic juice (PSP S2-5) through the tryptic cleavage of the Arg-11-Ile-12 bond.
2493268	2	40	theme	human	217:221	arg1	calculi					223:229	human calculi	217:229	human calculi (PSP)	217:235	The pancreatic stone protein isolated from human calculi (PSP) derives from the immunoreactive protein forms detected in human pancreatic juice (PSP S2-5) through the tryptic cleavage of the Arg-11-Ile-12 bond.
2493268	5	41	from	solutions	740:748	arg1	whereas					781:787	whereas	781:787	whereas	781:787	The PSP S2-5 forms are very soluble in aqueous solutions between the pH values 5.0-9.0, whereas the proteolysated form is scarcely soluble.
2493268	5	41	from	solutions	740:748	arg1	forms					706:710	The PSP S2-5 forms	693:710	The PSP S2-5 forms	693:710	The PSP S2-5 forms are very soluble in aqueous solutions between the pH values 5.0-9.0, whereas the proteolysated form is scarcely soluble.
2493268	5	41	from	solutions	740:748	arg1	soluble					721:727	soluble	721:727	soluble	721:727	The PSP S2-5 forms are very soluble in aqueous solutions between the pH values 5.0-9.0, whereas the proteolysated form is scarcely soluble.
2493268	3	42	theme	first	478:482	arg1	residue					484:490	the first residue	474:490	the first residue	474:490	Among the eleven amino acids of the PSP S2-5 N-terminal extension Z-E-A-Q-T-E-L-P-Q-A-R, the first residue is an oxoproline and the fifth, a threonine, bears the single carbohydrate chain of the protein molecules.
2493268	3	42	theme	first	478:482	arg1	oxoproline					498:507	an oxoproline	495:507	an oxoproline	495:507	Among the eleven amino acids of the PSP S2-5 N-terminal extension Z-E-A-Q-T-E-L-P-Q-A-R, the first residue is an oxoproline and the fifth, a threonine, bears the single carbohydrate chain of the protein molecules.
2493268	3	43	theme	protein	580:586	arg1	molecules					588:596	the protein molecules	576:596	the protein molecules	576:596	Among the eleven amino acids of the PSP S2-5 N-terminal extension Z-E-A-Q-T-E-L-P-Q-A-R, the first residue is an oxoproline and the fifth, a threonine, bears the single carbohydrate chain of the protein molecules.
2493268	2	44	theme	PSP	319:321	arg1	S2-5					323:326	PSP S2-5	319:326	PSP S2-5	319:326	The pancreatic stone protein isolated from human calculi (PSP) derives from the immunoreactive protein forms detected in human pancreatic juice (PSP S2-5) through the tryptic cleavage of the Arg-11-Ile-12 bond.
2493268	2	44	theme	PSP	319:321	arg1	juice					312:316	human pancreatic juice	295:316	human pancreatic juice (PSP S2-5)	295:327	The pancreatic stone protein isolated from human calculi (PSP) derives from the immunoreactive protein forms detected in human pancreatic juice (PSP S2-5) through the tryptic cleavage of the Arg-11-Ile-12 bond.
2493268	2	45	theme	human	295:299	arg1	S2-5					323:326	PSP S2-5	319:326	PSP S2-5	319:326	The pancreatic stone protein isolated from human calculi (PSP) derives from the immunoreactive protein forms detected in human pancreatic juice (PSP S2-5) through the tryptic cleavage of the Arg-11-Ile-12 bond.
2493268	2	45	theme	human	295:299	arg1	juice					312:316	human pancreatic juice	295:316	human pancreatic juice (PSP S2-5)	295:327	The pancreatic stone protein isolated from human calculi (PSP) derives from the immunoreactive protein forms detected in human pancreatic juice (PSP S2-5) through the tryptic cleavage of the Arg-11-Ile-12 bond.
2493268	0	46	gly	glycosylated	37:48	arg1	protein					82:88	human pancreatic stone protein	59:88	human pancreatic stone protein	59:88	N-terminal sequence extension in the glycosylated forms of human pancreatic stone protein.
2493268	0	46	gly	glycosylated	37:48	arg1	forms					50:54	the glycosylated forms	33:54	the glycosylated forms of human pancreatic stone protein	33:88	N-terminal sequence extension in the glycosylated forms of human pancreatic stone protein.
2493268	2	47	theme	tryptic	341:347	arg1	cleavage					349:356	the tryptic cleavage	337:356	the tryptic cleavage of the Arg-11-Ile-12 bond	337:382	The pancreatic stone protein isolated from human calculi (PSP) derives from the immunoreactive protein forms detected in human pancreatic juice (PSP S2-5) through the tryptic cleavage of the Arg-11-Ile-12 bond.
2493268	3	48	theme	Z-E-A-Q-T-E-L-P-Q-A-R	451:471	arg1	acids					408:412	the eleven amino acids	391:412	the eleven amino acids of the PSP S2-5 N-terminal extension Z-E-A-Q-T-E-L-P-Q-A-R	391:471	Among the eleven amino acids of the PSP S2-5 N-terminal extension Z-E-A-Q-T-E-L-P-Q-A-R, the first residue is an oxoproline and the fifth, a threonine, bears the single carbohydrate chain of the protein molecules.
2493268	0	49	theme	pancreatic	65:74	arg1	protein					82:88	human pancreatic stone protein	59:88	human pancreatic stone protein	59:88	N-terminal sequence extension in the glycosylated forms of human pancreatic stone protein.
2493268	2	50	theme	stone	189:193	arg1	protein					195:201	The pancreatic stone protein	174:201	The pancreatic stone protein isolated from human calculi (PSP)	174:235	The pancreatic stone protein isolated from human calculi (PSP) derives from the immunoreactive protein forms detected in human pancreatic juice (PSP S2-5) through the tryptic cleavage of the Arg-11-Ile-12 bond.
2493268	4	51	theme	glycan	617:622	arg1	composition					630:640	the glycan chain composition	613:640	the glycan chain composition	613:640	Variations in the glycan chain composition account for the differences in the Mr of PSP S2-5.
2493268	0	52	theme	human	59:63	arg1	protein					82:88	human pancreatic stone protein	59:88	human pancreatic stone protein	59:88	N-terminal sequence extension in the glycosylated forms of human pancreatic stone protein.
2493268	1	53	theme	5th	150:152	arg1	residue					165:171	the 5th amino acid residue	146:171	the 5th amino acid residue	146:171	The 5-oxoproline N-terminal chain is O-glycosylated on the 5th amino acid residue.
28252640	0	0	theme	luminal	77:83	arg1	SV2C					117:120	its neuronal receptor SV2C	95:120	its neuronal receptor SV2C	95:120	Crystal structure of the BoNT/A2 receptor-binding domain in complex with the luminal domain of its neuronal receptor SV2C.
28252640	0	0	theme	luminal	77:83	arg1	domain					85:90	the luminal domain	73:90	the luminal domain of its neuronal receptor SV2C	73:120	Crystal structure of the BoNT/A2 receptor-binding domain in complex with the luminal domain of its neuronal receptor SV2C.
28252640	2	1	theme	neuronal	474:481	arg1	SV2C					492:495	its neuronal receptor SV2C	470:495	its neuronal receptor SV2C	470:495	The X-ray crystal structure of the receptor-binding domain (HC) of BoNT/A1 in complex with the luminal domain (LD) of its neuronal receptor SV2C revealed only few specific side-chain - side-chain interactions that are important for binding.
28252640	4	2	theme	biological	840:849	arg1	activity					851:858	biological activity	840:858	biological activity	840:858	Because it has been suggested that differential receptor binding of subtypes might explain their differences in biological activity, we determined the crystal structure of BoNT/A2-HC in complex with SV2C-LD.
28252640	4	3	with	complex	914:920	arg1	SV2C-LD					927:933	SV2C-LD	927:933	SV2C-LD	927:933	Because it has been suggested that differential receptor binding of subtypes might explain their differences in biological activity, we determined the crystal structure of BoNT/A2-HC in complex with SV2C-LD.
28252640	2	4	theme	side-chain	537:546	arg1	interactions					548:559	only few specific side-chain - side-chain interactions	506:559	interactions	548:559	The X-ray crystal structure of the receptor-binding domain (HC) of BoNT/A1 in complex with the luminal domain (LD) of its neuronal receptor SV2C revealed only few specific side-chain - side-chain interactions that are important for binding.
28252640	0	5	from	structure	8:16	arg1	complex					60:66	complex	60:66	complex with the luminal domain of its neuronal receptor SV2C	60:120	Crystal structure of the BoNT/A2 receptor-binding domain in complex with the luminal domain of its neuronal receptor SV2C.
28252640	2	6	theme	receptor-binding	387:402	arg1	HC					412:413	HC	412:413	HC	412:413	The X-ray crystal structure of the receptor-binding domain (HC) of BoNT/A1 in complex with the luminal domain (LD) of its neuronal receptor SV2C revealed only few specific side-chain - side-chain interactions that are important for binding.
28252640	2	6	theme	receptor-binding	387:402	arg1	BoNT/A1					419:425	BoNT/A1	419:425	BoNT/A1 in complex with the luminal domain (LD) of its neuronal receptor SV2C	419:495	The X-ray crystal structure of the receptor-binding domain (HC) of BoNT/A1 in complex with the luminal domain (LD) of its neuronal receptor SV2C revealed only few specific side-chain - side-chain interactions that are important for binding.
28252640	2	6	theme	receptor-binding	387:402	arg1	domain					404:409	the receptor-binding domain	383:409	the receptor-binding domain (HC) of BoNT/A1 in complex with the luminal domain (LD) of its neuronal receptor SV2C	383:495	The X-ray crystal structure of the receptor-binding domain (HC) of BoNT/A1 in complex with the luminal domain (LD) of its neuronal receptor SV2C revealed only few specific side-chain - side-chain interactions that are important for binding.
28252640	2	7	theme	specific	515:522	arg1	side-chain					524:533	only few specific side-chain - side-chain interactions	506:559	side-chain	524:533	The X-ray crystal structure of the receptor-binding domain (HC) of BoNT/A1 in complex with the luminal domain (LD) of its neuronal receptor SV2C revealed only few specific side-chain - side-chain interactions that are important for binding.
28252640	6	8	theme	stacking	1231:1238	arg1	interaction					1240:1250	an anion-π stacking interaction	1220:1250	an anion-π stacking interaction	1220:1250	In the BoNT/A2-HC - SV2C complex structure, a missing cation-π stacking is compensated for by an additional salt bridge and an anion-π stacking interaction, which explains why the binding of BoNT/A subtypes to SV2C tolerates variable side chains.
28252640	5	9	theme	BoNT/A	1008:1013	arg1	subtypes					1015:1022	the two BoNT/A subtypes	1000:1022	the two BoNT/A subtypes	1000:1022	Although only few side-chain interactions are conserved between the two BoNT/A subtypes, the overall binding mode of subtypes A1 and A2 is virtually identical.
28252640	6	10	theme	missing	1142:1148	arg1	stacking					1159:1166	a missing cation-π stacking	1140:1166	a missing cation-π stacking	1140:1166	In the BoNT/A2-HC - SV2C complex structure, a missing cation-π stacking is compensated for by an additional salt bridge and an anion-π stacking interaction, which explains why the binding of BoNT/A subtypes to SV2C tolerates variable side chains.
28252640	3	11	with	interaction	672:682	arg1	SV2					689:691	SV2	689:691	SV2	689:691	Notably, two BoNT/A1 residues, Arg 1156 and Arg 1294, that are crucial for the interaction with SV2, are not conserved among subtypes.
28252640	2	12	theme	few	511:513	arg1	side-chain					524:533	only few specific side-chain - side-chain interactions	506:559	side-chain	524:533	The X-ray crystal structure of the receptor-binding domain (HC) of BoNT/A1 in complex with the luminal domain (LD) of its neuronal receptor SV2C revealed only few specific side-chain - side-chain interactions that are important for binding.
28252640	4	13	from	differences	825:835	arg1	activity					851:858	biological activity	840:858	biological activity	840:858	Because it has been suggested that differential receptor binding of subtypes might explain their differences in biological activity, we determined the crystal structure of BoNT/A2-HC in complex with SV2C-LD.
28252640	6	14	theme	anion-π	1223:1229	arg1	interaction					1240:1250	an anion-π stacking interaction	1220:1250	an anion-π stacking interaction	1220:1250	In the BoNT/A2-HC - SV2C complex structure, a missing cation-π stacking is compensated for by an additional salt bridge and an anion-π stacking interaction, which explains why the binding of BoNT/A subtypes to SV2C tolerates variable side chains.
28252640	7	15	theme	shallow	1394:1400	arg1	cleft					1410:1414	a shallow binding cleft	1392:1414	a shallow binding cleft in BoNT/A-HC	1392:1427	These findings suggest that motif extensions and a shallow binding cleft in BoNT/A-HC contribute to binding specificity.
28252640	0	16	theme	neuronal	99:106	arg1	SV2C					117:120	its neuronal receptor SV2C	95:120	its neuronal receptor SV2C	95:120	Crystal structure of the BoNT/A2 receptor-binding domain in complex with the luminal domain of its neuronal receptor SV2C.
28252640	0	17	with	complex	60:66	arg1	SV2C					117:120	its neuronal receptor SV2C	95:120	its neuronal receptor SV2C	95:120	Crystal structure of the BoNT/A2 receptor-binding domain in complex with the luminal domain of its neuronal receptor SV2C.
28252640	0	17	with	complex	60:66	arg1	domain					85:90	the luminal domain	73:90	the luminal domain of its neuronal receptor SV2C	73:120	Crystal structure of the BoNT/A2 receptor-binding domain in complex with the luminal domain of its neuronal receptor SV2C.
28252640	5	18	theme	few	950:952	arg1	interactions					965:976	only few side-chain interactions	945:976	only few side-chain interactions	945:976	Although only few side-chain interactions are conserved between the two BoNT/A subtypes, the overall binding mode of subtypes A1 and A2 is virtually identical.
28252640	1	19	theme	botulinum	161:169	arg1	BoNT					183:186	BoNT	183:186	BoNT	183:186	A detailed molecular understanding of botulinum neurotoxin (BoNT)/host-cell-receptor interactions is fundamental both for developing strategies against botulism and for generating improved BoNT variants for medical applications.
28252640	1	19	theme	botulinum	161:169	arg1	neurotoxin					171:180	botulinum neurotoxin	161:180	botulinum neurotoxin (BoNT)/host-cell-receptor interactions	161:219	A detailed molecular understanding of botulinum neurotoxin (BoNT)/host-cell-receptor interactions is fundamental both for developing strategies against botulism and for generating improved BoNT variants for medical applications.
28252640	7	20	from	cleft	1410:1414	arg1	BoNT/A-HC					1419:1427	BoNT/A-HC	1419:1427	BoNT/A-HC	1419:1427	These findings suggest that motif extensions and a shallow binding cleft in BoNT/A-HC contribute to binding specificity.
28252640	2	21	with	complex	430:436	arg1	LD					463:464	LD	463:464	LD	463:464	The X-ray crystal structure of the receptor-binding domain (HC) of BoNT/A1 in complex with the luminal domain (LD) of its neuronal receptor SV2C revealed only few specific side-chain - side-chain interactions that are important for binding.
28252640	2	21	with	complex	430:436	arg1	domain					455:460	the luminal domain	443:460	the luminal domain (LD) of its neuronal receptor SV2C	443:495	The X-ray crystal structure of the receptor-binding domain (HC) of BoNT/A1 in complex with the luminal domain (LD) of its neuronal receptor SV2C revealed only few specific side-chain - side-chain interactions that are important for binding.
28252640	2	21	with	complex	430:436	arg1	SV2C					492:495	its neuronal receptor SV2C	470:495	its neuronal receptor SV2C	470:495	The X-ray crystal structure of the receptor-binding domain (HC) of BoNT/A1 in complex with the luminal domain (LD) of its neuronal receptor SV2C revealed only few specific side-chain - side-chain interactions that are important for binding.
28252640	2	22	theme	luminal	447:453	arg1	LD					463:464	LD	463:464	LD	463:464	The X-ray crystal structure of the receptor-binding domain (HC) of BoNT/A1 in complex with the luminal domain (LD) of its neuronal receptor SV2C revealed only few specific side-chain - side-chain interactions that are important for binding.
28252640	2	22	theme	luminal	447:453	arg1	domain					455:460	the luminal domain	443:460	the luminal domain (LD) of its neuronal receptor SV2C	443:495	The X-ray crystal structure of the receptor-binding domain (HC) of BoNT/A1 in complex with the luminal domain (LD) of its neuronal receptor SV2C revealed only few specific side-chain - side-chain interactions that are important for binding.
28252640	2	22	theme	luminal	447:453	arg1	SV2C					492:495	its neuronal receptor SV2C	470:495	its neuronal receptor SV2C	470:495	The X-ray crystal structure of the receptor-binding domain (HC) of BoNT/A1 in complex with the luminal domain (LD) of its neuronal receptor SV2C revealed only few specific side-chain - side-chain interactions that are important for binding.
28252640	1	23	theme	neurotoxin	171:180	arg1	interactions					208:219	botulinum neurotoxin (BoNT)/host-cell-receptor interactions	161:219	botulinum neurotoxin (BoNT)/host-cell-receptor interactions	161:219	A detailed molecular understanding of botulinum neurotoxin (BoNT)/host-cell-receptor interactions is fundamental both for developing strategies against botulism and for generating improved BoNT variants for medical applications.
28252640	5	24	theme	subtypes	1053:1060	arg1	identical					1085:1093	identical	1085:1093	identical	1085:1093	Although only few side-chain interactions are conserved between the two BoNT/A subtypes, the overall binding mode of subtypes A1 and A2 is virtually identical.
28252640	5	24	theme	subtypes	1053:1060	arg1	mode					1045:1048	the overall binding mode	1025:1048	the overall binding mode of subtypes A1 and A2	1025:1070	Although only few side-chain interactions are conserved between the two BoNT/A subtypes, the overall binding mode of subtypes A1 and A2 is virtually identical.
28252640	6	25	theme	side	1330:1333	arg1	chains					1335:1340	variable side chains	1321:1340	variable side chains	1321:1340	In the BoNT/A2-HC - SV2C complex structure, a missing cation-π stacking is compensated for by an additional salt bridge and an anion-π stacking interaction, which explains why the binding of BoNT/A subtypes to SV2C tolerates variable side chains.
28252640	6	26	theme	complex	1121:1127	arg1	structure					1129:1137	the BoNT/A2-HC - SV2C complex structure	1099:1137	the BoNT/A2-HC - SV2C complex structure	1099:1137	In the BoNT/A2-HC - SV2C complex structure, a missing cation-π stacking is compensated for by an additional salt bridge and an anion-π stacking interaction, which explains why the binding of BoNT/A subtypes to SV2C tolerates variable side chains.
28252640	0	27	theme	Crystal	0:6	arg1	structure					8:16	Crystal structure	0:16	Crystal structure of the BoNT/A2 receptor-binding domain in complex with the luminal domain of its neuronal receptor SV2C.	0:121	Crystal structure of the BoNT/A2 receptor-binding domain in complex with the luminal domain of its neuronal receptor SV2C.
28252640	6	28	theme	salt	1204:1207	arg1	bridge					1209:1214	an additional salt bridge	1190:1214	an additional salt bridge	1190:1214	In the BoNT/A2-HC - SV2C complex structure, a missing cation-π stacking is compensated for by an additional salt bridge and an anion-π stacking interaction, which explains why the binding of BoNT/A subtypes to SV2C tolerates variable side chains.
28252640	6	29	theme	SV2C	1116:1119	arg1	structure					1129:1137	the BoNT/A2-HC - SV2C complex structure	1099:1137	the BoNT/A2-HC - SV2C complex structure	1099:1137	In the BoNT/A2-HC - SV2C complex structure, a missing cation-π stacking is compensated for by an additional salt bridge and an anion-π stacking interaction, which explains why the binding of BoNT/A subtypes to SV2C tolerates variable side chains.
28252640	6	30	theme	BoNT/A	1287:1292	arg1	subtypes					1294:1301	BoNT/A subtypes	1287:1301	BoNT/A subtypes	1287:1301	In the BoNT/A2-HC - SV2C complex structure, a missing cation-π stacking is compensated for by an additional salt bridge and an anion-π stacking interaction, which explains why the binding of BoNT/A subtypes to SV2C tolerates variable side chains.
28252640	2	31	theme	domain	404:409	arg1	structure					370:378	The X-ray crystal structure	352:378	The X-ray crystal structure of the receptor-binding domain (HC) of BoNT/A1 in complex with the luminal domain (LD) of its neuronal receptor SV2C	352:495	The X-ray crystal structure of the receptor-binding domain (HC) of BoNT/A1 in complex with the luminal domain (LD) of its neuronal receptor SV2C revealed only few specific side-chain - side-chain interactions that are important for binding.
28252640	0	32	theme	SV2C	117:120	arg1	SV2C					117:120	its neuronal receptor SV2C	95:120	its neuronal receptor SV2C	95:120	Crystal structure of the BoNT/A2 receptor-binding domain in complex with the luminal domain of its neuronal receptor SV2C.
28252640	0	32	theme	SV2C	117:120	arg1	domain					85:90	the luminal domain	73:90	the luminal domain of its neuronal receptor SV2C	73:120	Crystal structure of the BoNT/A2 receptor-binding domain in complex with the luminal domain of its neuronal receptor SV2C.
28252640	7	33	theme	motif	1371:1375	arg1	extensions					1377:1386	motif extensions	1371:1386	motif extensions	1371:1386	These findings suggest that motif extensions and a shallow binding cleft in BoNT/A-HC contribute to binding specificity.
28252640	1	34	theme	improved	303:310	arg1	variants					317:324	improved BoNT variants	303:324	improved BoNT variants	303:324	A detailed molecular understanding of botulinum neurotoxin (BoNT)/host-cell-receptor interactions is fundamental both for developing strategies against botulism and for generating improved BoNT variants for medical applications.
28252640	0	35	theme	receptor	108:115	arg1	SV2C					117:120	its neuronal receptor SV2C	95:120	its neuronal receptor SV2C	95:120	Crystal structure of the BoNT/A2 receptor-binding domain in complex with the luminal domain of its neuronal receptor SV2C.
28252640	6	36	theme	BoNT/A2-HC	1103:1112	arg1	structure					1129:1137	the BoNT/A2-HC - SV2C complex structure	1099:1137	the BoNT/A2-HC - SV2C complex structure	1099:1137	In the BoNT/A2-HC - SV2C complex structure, a missing cation-π stacking is compensated for by an additional salt bridge and an anion-π stacking interaction, which explains why the binding of BoNT/A subtypes to SV2C tolerates variable side chains.
28252640	1	37	theme	/host-cell-receptor	188:206	arg1	interactions					208:219	botulinum neurotoxin (BoNT)/host-cell-receptor interactions	161:219	botulinum neurotoxin (BoNT)/host-cell-receptor interactions	161:219	A detailed molecular understanding of botulinum neurotoxin (BoNT)/host-cell-receptor interactions is fundamental both for developing strategies against botulism and for generating improved BoNT variants for medical applications.
28252640	0	38	theme	receptor-binding	33:48	arg1	domain					50:55	the BoNT/A2 receptor-binding domain	21:55	the BoNT/A2 receptor-binding domain	21:55	Crystal structure of the BoNT/A2 receptor-binding domain in complex with the luminal domain of its neuronal receptor SV2C.
28252640	1	39	theme	BoNT	312:315	arg1	variants					317:324	improved BoNT variants	303:324	improved BoNT variants	303:324	A detailed molecular understanding of botulinum neurotoxin (BoNT)/host-cell-receptor interactions is fundamental both for developing strategies against botulism and for generating improved BoNT variants for medical applications.
28252640	7	40	theme	binding	1402:1408	arg1	cleft					1410:1414	a shallow binding cleft	1392:1414	a shallow binding cleft in BoNT/A-HC	1392:1427	These findings suggest that motif extensions and a shallow binding cleft in BoNT/A-HC contribute to binding specificity.
28252640	2	41	theme	BoNT/A1	419:425	arg1	HC					412:413	HC	412:413	HC	412:413	The X-ray crystal structure of the receptor-binding domain (HC) of BoNT/A1 in complex with the luminal domain (LD) of its neuronal receptor SV2C revealed only few specific side-chain - side-chain interactions that are important for binding.
28252640	2	41	theme	BoNT/A1	419:425	arg1	BoNT/A1					419:425	BoNT/A1	419:425	BoNT/A1 in complex with the luminal domain (LD) of its neuronal receptor SV2C	419:495	The X-ray crystal structure of the receptor-binding domain (HC) of BoNT/A1 in complex with the luminal domain (LD) of its neuronal receptor SV2C revealed only few specific side-chain - side-chain interactions that are important for binding.
28252640	2	41	theme	BoNT/A1	419:425	arg1	domain					404:409	the receptor-binding domain	383:409	the receptor-binding domain (HC) of BoNT/A1 in complex with the luminal domain (LD) of its neuronal receptor SV2C	383:495	The X-ray crystal structure of the receptor-binding domain (HC) of BoNT/A1 in complex with the luminal domain (LD) of its neuronal receptor SV2C revealed only few specific side-chain - side-chain interactions that are important for binding.
28252640	6	42	theme	additional	1193:1202	arg1	bridge					1209:1214	an additional salt bridge	1190:1214	an additional salt bridge	1190:1214	In the BoNT/A2-HC - SV2C complex structure, a missing cation-π stacking is compensated for by an additional salt bridge and an anion-π stacking interaction, which explains why the binding of BoNT/A subtypes to SV2C tolerates variable side chains.
28252640	1	43	theme	interactions	208:219	arg1	fundamental					224:234	fundamental	224:234	fundamental	224:234	A detailed molecular understanding of botulinum neurotoxin (BoNT)/host-cell-receptor interactions is fundamental both for developing strategies against botulism and for generating improved BoNT variants for medical applications.
28252640	1	43	theme	interactions	208:219	arg1	developing					245:254	developing	245:254	developing strategies against botulism	245:282	A detailed molecular understanding of botulinum neurotoxin (BoNT)/host-cell-receptor interactions is fundamental both for developing strategies against botulism and for generating improved BoNT variants for medical applications.
28252640	1	43	theme	interactions	208:219	arg1	understanding					144:156	A detailed molecular understanding	123:156	A detailed molecular understanding of botulinum neurotoxin (BoNT)/host-cell-receptor interactions	123:219	A detailed molecular understanding of botulinum neurotoxin (BoNT)/host-cell-receptor interactions is fundamental both for developing strategies against botulism and for generating improved BoNT variants for medical applications.
28252640	1	43	theme	interactions	208:219	arg1	generating					292:301	generating	292:301	generating improved BoNT variants for medical applications	292:349	A detailed molecular understanding of botulinum neurotoxin (BoNT)/host-cell-receptor interactions is fundamental both for developing strategies against botulism and for generating improved BoNT variants for medical applications.
28252640	0	44	theme	BoNT/A2	25:31	arg1	domain					50:55	the BoNT/A2 receptor-binding domain	21:55	the BoNT/A2 receptor-binding domain	21:55	Crystal structure of the BoNT/A2 receptor-binding domain in complex with the luminal domain of its neuronal receptor SV2C.
28252640	4	45	theme	BoNT/A2-HC	900:909	arg1	structure					887:895	the crystal structure	875:895	the crystal structure of BoNT/A2-HC	875:909	Because it has been suggested that differential receptor binding of subtypes might explain their differences in biological activity, we determined the crystal structure of BoNT/A2-HC in complex with SV2C-LD.
28252640	1	46	dep	fundamental	224:234	arg1	fundamental					224:234	fundamental	224:234	fundamental	224:234	A detailed molecular understanding of botulinum neurotoxin (BoNT)/host-cell-receptor interactions is fundamental both for developing strategies against botulism and for generating improved BoNT variants for medical applications.
28252640	1	46	dep	fundamental	224:234	arg1	developing					245:254	developing	245:254	developing strategies against botulism	245:282	A detailed molecular understanding of botulinum neurotoxin (BoNT)/host-cell-receptor interactions is fundamental both for developing strategies against botulism and for generating improved BoNT variants for medical applications.
28252640	1	46	dep	fundamental	224:234	arg1	understanding					144:156	A detailed molecular understanding	123:156	A detailed molecular understanding of botulinum neurotoxin (BoNT)/host-cell-receptor interactions	123:219	A detailed molecular understanding of botulinum neurotoxin (BoNT)/host-cell-receptor interactions is fundamental both for developing strategies against botulism and for generating improved BoNT variants for medical applications.
28252640	1	46	dep	fundamental	224:234	arg1	generating					292:301	generating	292:301	generating improved BoNT variants for medical applications	292:349	A detailed molecular understanding of botulinum neurotoxin (BoNT)/host-cell-receptor interactions is fundamental both for developing strategies against botulism and for generating improved BoNT variants for medical applications.
28252640	4	47	theme	receptor	776:783	arg1	binding					785:791	differential receptor binding	763:791	differential receptor binding of subtypes	763:803	Because it has been suggested that differential receptor binding of subtypes might explain their differences in biological activity, we determined the crystal structure of BoNT/A2-HC in complex with SV2C-LD.
28252640	6	48	theme	variable	1321:1328	arg1	chains					1335:1340	variable side chains	1321:1340	variable side chains	1321:1340	In the BoNT/A2-HC - SV2C complex structure, a missing cation-π stacking is compensated for by an additional salt bridge and an anion-π stacking interaction, which explains why the binding of BoNT/A subtypes to SV2C tolerates variable side chains.
28252640	4	49	theme	subtypes	796:803	arg1	binding					785:791	differential receptor binding	763:791	differential receptor binding of subtypes	763:803	Because it has been suggested that differential receptor binding of subtypes might explain their differences in biological activity, we determined the crystal structure of BoNT/A2-HC in complex with SV2C-LD.
28252640	2	50	from	domain	404:409	arg1	complex					430:436	complex	430:436	complex with the luminal domain (LD) of its neuronal receptor SV2C	430:495	The X-ray crystal structure of the receptor-binding domain (HC) of BoNT/A1 in complex with the luminal domain (LD) of its neuronal receptor SV2C revealed only few specific side-chain - side-chain interactions that are important for binding.
28252640	2	51	theme	crystal	362:368	arg1	structure					370:378	The X-ray crystal structure	352:378	The X-ray crystal structure of the receptor-binding domain (HC) of BoNT/A1 in complex with the luminal domain (LD) of its neuronal receptor SV2C	352:495	The X-ray crystal structure of the receptor-binding domain (HC) of BoNT/A1 in complex with the luminal domain (LD) of its neuronal receptor SV2C revealed only few specific side-chain - side-chain interactions that are important for binding.
28252640	0	52	theme	domain	50:55	arg1	structure					8:16	Crystal structure	0:16	Crystal structure of the BoNT/A2 receptor-binding domain in complex with the luminal domain of its neuronal receptor SV2C.	0:121	Crystal structure of the BoNT/A2 receptor-binding domain in complex with the luminal domain of its neuronal receptor SV2C.
28252640	1	53	theme	medical	330:336	arg1	applications					338:349	medical applications	330:349	medical applications	330:349	A detailed molecular understanding of botulinum neurotoxin (BoNT)/host-cell-receptor interactions is fundamental both for developing strategies against botulism and for generating improved BoNT variants for medical applications.
28252640	6	54	theme	subtypes	1294:1301	arg1	binding					1276:1282	the binding	1272:1282	the binding of BoNT/A subtypes to SV2C	1272:1309	In the BoNT/A2-HC - SV2C complex structure, a missing cation-π stacking is compensated for by an additional salt bridge and an anion-π stacking interaction, which explains why the binding of BoNT/A subtypes to SV2C tolerates variable side chains.
28252640	2	55	theme	X-ray	356:360	arg1	structure					370:378	The X-ray crystal structure	352:378	The X-ray crystal structure of the receptor-binding domain (HC) of BoNT/A1 in complex with the luminal domain (LD) of its neuronal receptor SV2C	352:495	The X-ray crystal structure of the receptor-binding domain (HC) of BoNT/A1 in complex with the luminal domain (LD) of its neuronal receptor SV2C revealed only few specific side-chain - side-chain interactions that are important for binding.
28252640	6	56	theme	cation-π	1150:1157	arg1	stacking					1159:1166	a missing cation-π stacking	1140:1166	a missing cation-π stacking	1140:1166	In the BoNT/A2-HC - SV2C complex structure, a missing cation-π stacking is compensated for by an additional salt bridge and an anion-π stacking interaction, which explains why the binding of BoNT/A subtypes to SV2C tolerates variable side chains.
28252640	4	57	theme	crystal	879:885	arg1	structure					887:895	the crystal structure	875:895	the crystal structure of BoNT/A2-HC	875:909	Because it has been suggested that differential receptor binding of subtypes might explain their differences in biological activity, we determined the crystal structure of BoNT/A2-HC in complex with SV2C-LD.
28252640	5	58	dep	subtypes	1053:1060	arg1	subtypes					1053:1060	subtypes A1 and A2	1053:1070	subtypes A1 and A2	1053:1070	Although only few side-chain interactions are conserved between the two BoNT/A subtypes, the overall binding mode of subtypes A1 and A2 is virtually identical.
28252640	5	58	dep	subtypes	1053:1060	arg1	A2					1069:1070	A2	1069:1070	A2	1069:1070	Although only few side-chain interactions are conserved between the two BoNT/A subtypes, the overall binding mode of subtypes A1 and A2 is virtually identical.
28252640	5	58	dep	subtypes	1053:1060	arg1	A1					1062:1063	A1	1062:1063	A1	1062:1063	Although only few side-chain interactions are conserved between the two BoNT/A subtypes, the overall binding mode of subtypes A1 and A2 is virtually identical.
28252640	5	59	theme	side-chain	954:963	arg1	interactions					965:976	only few side-chain interactions	945:976	only few side-chain interactions	945:976	Although only few side-chain interactions are conserved between the two BoNT/A subtypes, the overall binding mode of subtypes A1 and A2 is virtually identical.
28252640	5	60	theme	overall	1029:1035	arg1	identical					1085:1093	identical	1085:1093	identical	1085:1093	Although only few side-chain interactions are conserved between the two BoNT/A subtypes, the overall binding mode of subtypes A1 and A2 is virtually identical.
28252640	5	60	theme	overall	1029:1035	arg1	mode					1045:1048	the overall binding mode	1025:1048	the overall binding mode of subtypes A1 and A2	1025:1070	Although only few side-chain interactions are conserved between the two BoNT/A subtypes, the overall binding mode of subtypes A1 and A2 is virtually identical.
28252640	2	61	from	BoNT/A1	419:425	arg1	complex					430:436	complex	430:436	complex with the luminal domain (LD) of its neuronal receptor SV2C	430:495	The X-ray crystal structure of the receptor-binding domain (HC) of BoNT/A1 in complex with the luminal domain (LD) of its neuronal receptor SV2C revealed only few specific side-chain - side-chain interactions that are important for binding.
28252640	2	62	theme	SV2C	492:495	arg1	LD					463:464	LD	463:464	LD	463:464	The X-ray crystal structure of the receptor-binding domain (HC) of BoNT/A1 in complex with the luminal domain (LD) of its neuronal receptor SV2C revealed only few specific side-chain - side-chain interactions that are important for binding.
28252640	2	62	theme	SV2C	492:495	arg1	domain					455:460	the luminal domain	443:460	the luminal domain (LD) of its neuronal receptor SV2C	443:495	The X-ray crystal structure of the receptor-binding domain (HC) of BoNT/A1 in complex with the luminal domain (LD) of its neuronal receptor SV2C revealed only few specific side-chain - side-chain interactions that are important for binding.
28252640	2	62	theme	SV2C	492:495	arg1	SV2C					492:495	its neuronal receptor SV2C	470:495	its neuronal receptor SV2C	470:495	The X-ray crystal structure of the receptor-binding domain (HC) of BoNT/A1 in complex with the luminal domain (LD) of its neuronal receptor SV2C revealed only few specific side-chain - side-chain interactions that are important for binding.
28252640	5	63	theme	binding	1037:1043	arg1	identical					1085:1093	identical	1085:1093	identical	1085:1093	Although only few side-chain interactions are conserved between the two BoNT/A subtypes, the overall binding mode of subtypes A1 and A2 is virtually identical.
28252640	5	63	theme	binding	1037:1043	arg1	mode					1045:1048	the overall binding mode	1025:1048	the overall binding mode of subtypes A1 and A2	1025:1070	Although only few side-chain interactions are conserved between the two BoNT/A subtypes, the overall binding mode of subtypes A1 and A2 is virtually identical.
28252640	4	64	theme	differential	763:774	arg1	binding					785:791	differential receptor binding	763:791	differential receptor binding of subtypes	763:803	Because it has been suggested that differential receptor binding of subtypes might explain their differences in biological activity, we determined the crystal structure of BoNT/A2-HC in complex with SV2C-LD.
28252640	1	65	theme	detailed	125:132	arg1	fundamental					224:234	fundamental	224:234	fundamental	224:234	A detailed molecular understanding of botulinum neurotoxin (BoNT)/host-cell-receptor interactions is fundamental both for developing strategies against botulism and for generating improved BoNT variants for medical applications.
28252640	1	65	theme	detailed	125:132	arg1	developing					245:254	developing	245:254	developing strategies against botulism	245:282	A detailed molecular understanding of botulinum neurotoxin (BoNT)/host-cell-receptor interactions is fundamental both for developing strategies against botulism and for generating improved BoNT variants for medical applications.
28252640	1	65	theme	detailed	125:132	arg1	understanding					144:156	A detailed molecular understanding	123:156	A detailed molecular understanding of botulinum neurotoxin (BoNT)/host-cell-receptor interactions	123:219	A detailed molecular understanding of botulinum neurotoxin (BoNT)/host-cell-receptor interactions is fundamental both for developing strategies against botulism and for generating improved BoNT variants for medical applications.
28252640	1	65	theme	detailed	125:132	arg1	generating					292:301	generating	292:301	generating improved BoNT variants for medical applications	292:349	A detailed molecular understanding of botulinum neurotoxin (BoNT)/host-cell-receptor interactions is fundamental both for developing strategies against botulism and for generating improved BoNT variants for medical applications.
28252640	2	66	theme	receptor	483:490	arg1	SV2C					492:495	its neuronal receptor SV2C	470:495	its neuronal receptor SV2C	470:495	The X-ray crystal structure of the receptor-binding domain (HC) of BoNT/A1 in complex with the luminal domain (LD) of its neuronal receptor SV2C revealed only few specific side-chain - side-chain interactions that are important for binding.
28252640	7	67	theme	binding	1443:1449	arg1	specificity					1451:1461	binding specificity	1443:1461	binding specificity	1443:1461	These findings suggest that motif extensions and a shallow binding cleft in BoNT/A-HC contribute to binding specificity.
28252640	3	68	theme	BoNT/A1	606:612	arg1	Arg					624:626	Arg 1156	624:631	Arg 1156	624:631	Notably, two BoNT/A1 residues, Arg 1156 and Arg 1294, that are crucial for the interaction with SV2, are not conserved among subtypes.
28252640	3	68	theme	BoNT/A1	606:612	arg1	Arg					637:639	Arg 1294	637:644	Arg 1294	637:644	Notably, two BoNT/A1 residues, Arg 1156 and Arg 1294, that are crucial for the interaction with SV2, are not conserved among subtypes.
28252640	3	68	theme	BoNT/A1	606:612	arg1	residues					614:621	two BoNT/A1 residues	602:621	two BoNT/A1 residues	602:621	Notably, two BoNT/A1 residues, Arg 1156 and Arg 1294, that are crucial for the interaction with SV2, are not conserved among subtypes.
28252640	2	69	from	complex	430:436	arg1	HC					412:413	HC	412:413	HC	412:413	The X-ray crystal structure of the receptor-binding domain (HC) of BoNT/A1 in complex with the luminal domain (LD) of its neuronal receptor SV2C revealed only few specific side-chain - side-chain interactions that are important for binding.
28252640	2	69	from	complex	430:436	arg1	BoNT/A1					419:425	BoNT/A1	419:425	BoNT/A1 in complex with the luminal domain (LD) of its neuronal receptor SV2C	419:495	The X-ray crystal structure of the receptor-binding domain (HC) of BoNT/A1 in complex with the luminal domain (LD) of its neuronal receptor SV2C revealed only few specific side-chain - side-chain interactions that are important for binding.
28252640	2	69	from	complex	430:436	arg1	domain					404:409	the receptor-binding domain	383:409	the receptor-binding domain (HC) of BoNT/A1 in complex with the luminal domain (LD) of its neuronal receptor SV2C	383:495	The X-ray crystal structure of the receptor-binding domain (HC) of BoNT/A1 in complex with the luminal domain (LD) of its neuronal receptor SV2C revealed only few specific side-chain - side-chain interactions that are important for binding.
28252640	1	70	theme	molecular	134:142	arg1	fundamental					224:234	fundamental	224:234	fundamental	224:234	A detailed molecular understanding of botulinum neurotoxin (BoNT)/host-cell-receptor interactions is fundamental both for developing strategies against botulism and for generating improved BoNT variants for medical applications.
28252640	1	70	theme	molecular	134:142	arg1	developing					245:254	developing	245:254	developing strategies against botulism	245:282	A detailed molecular understanding of botulinum neurotoxin (BoNT)/host-cell-receptor interactions is fundamental both for developing strategies against botulism and for generating improved BoNT variants for medical applications.
28252640	1	70	theme	molecular	134:142	arg1	understanding					144:156	A detailed molecular understanding	123:156	A detailed molecular understanding of botulinum neurotoxin (BoNT)/host-cell-receptor interactions	123:219	A detailed molecular understanding of botulinum neurotoxin (BoNT)/host-cell-receptor interactions is fundamental both for developing strategies against botulism and for generating improved BoNT variants for medical applications.
28252640	1	70	theme	molecular	134:142	arg1	generating					292:301	generating	292:301	generating improved BoNT variants for medical applications	292:349	A detailed molecular understanding of botulinum neurotoxin (BoNT)/host-cell-receptor interactions is fundamental both for developing strategies against botulism and for generating improved BoNT variants for medical applications.
28252640	7	71	from	extensions	1377:1386	arg1	BoNT/A-HC					1419:1427	BoNT/A-HC	1419:1427	BoNT/A-HC	1419:1427	These findings suggest that motif extensions and a shallow binding cleft in BoNT/A-HC contribute to binding specificity.
23302862	7	0	theme	switch	1419:1424	arg1	mechanism					1375:1383	the mechanism	1371:1383	the mechanism of a long-proposed conformational switch in insulin upon receptor engagement	1371:1460	The αCT segment displaces the B-chain C-terminal β-strand away from the hormone core, revealing the mechanism of a long-proposed conformational switch in insulin upon receptor engagement.
23302862	3	1	theme	receptor	669:676	arg1	protein					678:684	the receptor protein	665:684	the receptor protein	665:684	Despite more than three decades of investigation, the three-dimensional structure of the insulin-insulin receptor complex has proved elusive, confounded by the complexity of producing the receptor protein.
23302862	2	2	theme	disease	327:333	arg1	pathogenesis					257:268	the pathogenesis	253:268	the pathogenesis of type 2 diabetes mellitus	253:296	Insulin resistance contributes to the pathogenesis of type 2 diabetes mellitus and the onset of Alzheimer's disease; aberrant signalling occurs in diverse cancers, exacerbated by cross-talk with the homologous type 1 insulin-like growth factor receptor (IGF1R).
23302862	2	2	theme	disease	327:333	arg1	onset					306:310	the onset	302:310	the onset of Alzheimer's disease	302:333	Insulin resistance contributes to the pathogenesis of type 2 diabetes mellitus and the onset of Alzheimer's disease; aberrant signalling occurs in diverse cancers, exacerbated by cross-talk with the homologous type 1 insulin-like growth factor receptor (IGF1R).
23302862	7	3	theme	long-proposed	1390:1402	arg1	switch					1419:1424	a long-proposed conformational switch	1388:1424	a long-proposed conformational switch in insulin upon receptor engagement	1388:1460	The αCT segment displaces the B-chain C-terminal β-strand away from the hormone core, revealing the mechanism of a long-proposed conformational switch in insulin upon receptor engagement.
23302862	10	4	theme	IGF1R	1905:1909	arg1	systems					1911:1917	IGF1R systems	1905:1917	IGF1R systems	1905:1917	Together, our findings provide an explanation for a wealth of biochemical data from the insulin receptor and IGF1R systems relevant to the design of therapeutic insulin analogues.
23302862	3	5	theme	investigation	516:528	arg1	decades					505:511	more than three decades	489:511	more than three decades of investigation	489:528	Despite more than three decades of investigation, the three-dimensional structure of the insulin-insulin receptor complex has proved elusive, confounded by the complexity of producing the receptor protein.
23302862	2	6	theme	homologous	418:427	arg1	IGF1R					473:477	IGF1R	473:477	IGF1R	473:477	Insulin resistance contributes to the pathogenesis of type 2 diabetes mellitus and the onset of Alzheimer's disease; aberrant signalling occurs in diverse cancers, exacerbated by cross-talk with the homologous type 1 insulin-like growth factor receptor (IGF1R).
23302862	2	6	theme	homologous	418:427	arg1	receptor					463:470	the homologous type 1 insulin-like growth factor receptor	414:470	the homologous type 1 insulin-like growth factor receptor (IGF1R)	414:478	Insulin resistance contributes to the pathogenesis of type 2 diabetes mellitus and the onset of Alzheimer's disease; aberrant signalling occurs in diverse cancers, exacerbated by cross-talk with the homologous type 1 insulin-like growth factor receptor (IGF1R).
23302862	10	7	theme	data	1870:1873	arg1	wealth					1848:1853	a wealth	1846:1853	a wealth of biochemical data from the insulin receptor and IGF1R systems relevant to the design of therapeutic insulin analogues	1846:1973	Together, our findings provide an explanation for a wealth of biochemical data from the insulin receptor and IGF1R systems relevant to the design of therapeutic insulin analogues.
23302862	7	8	from	mechanism	1375:1383	arg1	insulin					1429:1435	insulin	1429:1435	insulin	1429:1435	The αCT segment displaces the B-chain C-terminal β-strand away from the hormone core, revealing the mechanism of a long-proposed conformational switch in insulin upon receptor engagement.
23302862	4	9	theme	insulin	865:871	arg1	structures					851:860	four crystal structures	838:860	four crystal structures of insulin bound to truncated insulin receptor constructs	838:918	Here we present the first view, to our knowledge, of the interaction of insulin with its primary binding site on the insulin receptor, on the basis of four crystal structures of insulin bound to truncated insulin receptor constructs.
23302862	10	10	theme	relevant	1919:1926	arg1	data					1870:1873	biochemical data	1858:1873	biochemical data from the insulin receptor and IGF1R systems relevant to the design of therapeutic insulin analogues	1858:1973	Together, our findings provide an explanation for a wealth of biochemical data from the insulin receptor and IGF1R systems relevant to the design of therapeutic insulin analogues.
23302862	6	11	theme	insulin	1249:1255	arg1	residues					1265:1272	insulin B-chain residues	1249:1272	insulin B-chain residues	1249:1272	Contact between insulin and L1 is restricted to insulin B-chain residues.
23302862	5	12	theme	receptor	1013:1020	arg1	L1					998:999	L1	998:999	L1	998:999	The direct interaction of insulin with the first leucine-rich-repeat domain (L1) of insulin receptor is seen to be sparse, the hormone instead engaging the insulin receptor carboxy-terminal α-chain (αCT) segment, which is itself remodelled on the face of L1 upon insulin binding.
23302862	5	12	theme	receptor	1013:1020	arg1	domain					990:995	the first leucine-rich-repeat domain	960:995	the first leucine-rich-repeat domain (L1) of insulin receptor	960:1020	The direct interaction of insulin with the first leucine-rich-repeat domain (L1) of insulin receptor is seen to be sparse, the hormone instead engaging the insulin receptor carboxy-terminal α-chain (αCT) segment, which is itself remodelled on the face of L1 upon insulin binding.
23302862	5	12	theme	receptor	1013:1020	arg1	receptor					1013:1020	insulin receptor	1005:1020	insulin receptor	1005:1020	The direct interaction of insulin with the first leucine-rich-repeat domain (L1) of insulin receptor is seen to be sparse, the hormone instead engaging the insulin receptor carboxy-terminal α-chain (αCT) segment, which is itself remodelled on the face of L1 upon insulin binding.
23302862	2	13	theme	diabetes	280:287	arg1	mellitus					289:296	type 2 diabetes mellitus	273:296	type 2 diabetes mellitus	273:296	Insulin resistance contributes to the pathogenesis of type 2 diabetes mellitus and the onset of Alzheimer's disease; aberrant signalling occurs in diverse cancers, exacerbated by cross-talk with the homologous type 1 insulin-like growth factor receptor (IGF1R).
23302862	10	14	from	receptor	1892:1899	arg1	wealth					1848:1853	a wealth	1846:1853	a wealth of biochemical data from the insulin receptor and IGF1R systems relevant to the design of therapeutic insulin analogues	1846:1973	Together, our findings provide an explanation for a wealth of biochemical data from the insulin receptor and IGF1R systems relevant to the design of therapeutic insulin analogues.
23302862	10	14	from	receptor	1892:1899	arg1	data					1870:1873	biochemical data	1858:1873	biochemical data from the insulin receptor and IGF1R systems relevant to the design of therapeutic insulin analogues	1858:1973	Together, our findings provide an explanation for a wealth of biochemical data from the insulin receptor and IGF1R systems relevant to the design of therapeutic insulin analogues.
23302862	5	15	with	interaction	932:942	arg1	L1					998:999	L1	998:999	L1	998:999	The direct interaction of insulin with the first leucine-rich-repeat domain (L1) of insulin receptor is seen to be sparse, the hormone instead engaging the insulin receptor carboxy-terminal α-chain (αCT) segment, which is itself remodelled on the face of L1 upon insulin binding.
23302862	5	15	with	interaction	932:942	arg1	domain					990:995	the first leucine-rich-repeat domain	960:995	the first leucine-rich-repeat domain (L1) of insulin receptor	960:1020	The direct interaction of insulin with the first leucine-rich-repeat domain (L1) of insulin receptor is seen to be sparse, the hormone instead engaging the insulin receptor carboxy-terminal α-chain (αCT) segment, which is itself remodelled on the face of L1 upon insulin binding.
23302862	5	15	with	interaction	932:942	arg1	receptor					1013:1020	insulin receptor	1005:1020	insulin receptor	1005:1020	The direct interaction of insulin with the first leucine-rich-repeat domain (L1) of insulin receptor is seen to be sparse, the hormone instead engaging the insulin receptor carboxy-terminal α-chain (αCT) segment, which is itself remodelled on the face of L1 upon insulin binding.
23302862	10	16	theme	insulin	1957:1963	arg1	analogues					1965:1973	therapeutic insulin analogues	1945:1973	therapeutic insulin analogues	1945:1973	Together, our findings provide an explanation for a wealth of biochemical data from the insulin receptor and IGF1R systems relevant to the design of therapeutic insulin analogues.
23302862	3	17	theme	receptor	586:593	arg1	complex					595:601	the insulin-insulin receptor complex	566:601	the insulin-insulin receptor complex	566:601	Despite more than three decades of investigation, the three-dimensional structure of the insulin-insulin receptor complex has proved elusive, confounded by the complexity of producing the receptor protein.
23302862	4	18	from	site	792:795	arg1	receptor					812:819	the insulin receptor	800:819	the insulin receptor	800:819	Here we present the first view, to our knowledge, of the interaction of insulin with its primary binding site on the insulin receptor, on the basis of four crystal structures of insulin bound to truncated insulin receptor constructs.
23302862	1	19	theme	central	104:110	arg1	role					112:115	a central role	102:115	a central role	102:115	Insulin receptor signalling has a central role in mammalian biology, regulating cellular metabolism, growth, division, differentiation and survival.
23302862	4	20	theme	structures	851:860	arg1	basis					829:833	the basis	825:833	the basis of four crystal structures of insulin bound to truncated insulin receptor constructs	825:918	Here we present the first view, to our knowledge, of the interaction of insulin with its primary binding site on the insulin receptor, on the basis of four crystal structures of insulin bound to truncated insulin receptor constructs.
23302862	4	21	theme	first	707:711	arg1	view					713:716	the first view	703:716	the first view	703:716	Here we present the first view, to our knowledge, of the interaction of insulin with its primary binding site on the insulin receptor, on the basis of four crystal structures of insulin bound to truncated insulin receptor constructs.
23302862	9	22	theme	isothermal	1705:1714	arg1	calorimetry					1726:1736	isothermal titration calorimetry	1705:1736	isothermal titration calorimetry data that dissect the hormone-insulin receptor interface	1705:1793	We support these findings by photo-crosslinking data that place the suggested interactions into the context of the holoreceptor and by isothermal titration calorimetry data that dissect the hormone-insulin receptor interface.
23302862	4	23	theme	crystal	843:849	arg1	structures					851:860	four crystal structures	838:860	four crystal structures of insulin bound to truncated insulin receptor constructs	838:918	Here we present the first view, to our knowledge, of the interaction of insulin with its primary binding site on the insulin receptor, on the basis of four crystal structures of insulin bound to truncated insulin receptor constructs.
23302862	5	24	theme	L1	1176:1177	arg1	face					1168:1171	the face	1164:1171	the face of L1	1164:1177	The direct interaction of insulin with the first leucine-rich-repeat domain (L1) of insulin receptor is seen to be sparse, the hormone instead engaging the insulin receptor carboxy-terminal α-chain (αCT) segment, which is itself remodelled on the face of L1 upon insulin binding.
23302862	10	25	from	systems	1911:1917	arg1	wealth					1848:1853	a wealth	1846:1853	a wealth of biochemical data from the insulin receptor and IGF1R systems relevant to the design of therapeutic insulin analogues	1846:1973	Together, our findings provide an explanation for a wealth of biochemical data from the insulin receptor and IGF1R systems relevant to the design of therapeutic insulin analogues.
23302862	10	25	from	systems	1911:1917	arg1	data					1870:1873	biochemical data	1858:1873	biochemical data from the insulin receptor and IGF1R systems relevant to the design of therapeutic insulin analogues	1858:1973	Together, our findings provide an explanation for a wealth of biochemical data from the insulin receptor and IGF1R systems relevant to the design of therapeutic insulin analogues.
23302862	4	26	theme	insulin	892:898	arg1	constructs					909:918	truncated insulin receptor constructs	882:918	truncated insulin receptor constructs	882:918	Here we present the first view, to our knowledge, of the interaction of insulin with its primary binding site on the insulin receptor, on the basis of four crystal structures of insulin bound to truncated insulin receptor constructs.
23302862	5	27	theme	insulin	1184:1190	arg1	binding					1192:1198	insulin binding	1184:1198	insulin binding	1184:1198	The direct interaction of insulin with the first leucine-rich-repeat domain (L1) of insulin receptor is seen to be sparse, the hormone instead engaging the insulin receptor carboxy-terminal α-chain (αCT) segment, which is itself remodelled on the face of L1 upon insulin binding.
23302862	2	28	theme	type	273:276	arg1	mellitus					289:296	type 2 diabetes mellitus	273:296	type 2 diabetes mellitus	273:296	Insulin resistance contributes to the pathogenesis of type 2 diabetes mellitus and the onset of Alzheimer's disease; aberrant signalling occurs in diverse cancers, exacerbated by cross-talk with the homologous type 1 insulin-like growth factor receptor (IGF1R).
23302862	0	29	from	site	40:43	arg1	receptor					60:67	the insulin receptor	48:67	the insulin receptor	48:67	How insulin engages its primary binding site on the insulin receptor.
23302862	2	30	theme	type	429:432	arg1	IGF1R					473:477	IGF1R	473:477	IGF1R	473:477	Insulin resistance contributes to the pathogenesis of type 2 diabetes mellitus and the onset of Alzheimer's disease; aberrant signalling occurs in diverse cancers, exacerbated by cross-talk with the homologous type 1 insulin-like growth factor receptor (IGF1R).
23302862	2	30	theme	type	429:432	arg1	receptor					463:470	the homologous type 1 insulin-like growth factor receptor	414:470	the homologous type 1 insulin-like growth factor receptor (IGF1R)	414:478	Insulin resistance contributes to the pathogenesis of type 2 diabetes mellitus and the onset of Alzheimer's disease; aberrant signalling occurs in diverse cancers, exacerbated by cross-talk with the homologous type 1 insulin-like growth factor receptor (IGF1R).
23302862	1	31	theme	receptor	78:85	arg1	signalling					87:96	Insulin receptor signalling	70:96	Insulin receptor signalling	70:96	Insulin receptor signalling has a central role in mammalian biology, regulating cellular metabolism, growth, division, differentiation and survival.
23302862	9	32	theme	receptor	1776:1783	arg1	interface					1785:1793	the hormone-insulin receptor interface	1756:1793	the hormone-insulin receptor interface	1756:1793	We support these findings by photo-crosslinking data that place the suggested interactions into the context of the holoreceptor and by isothermal titration calorimetry data that dissect the hormone-insulin receptor interface.
23302862	2	33	theme	factor	456:461	arg1	IGF1R					473:477	IGF1R	473:477	IGF1R	473:477	Insulin resistance contributes to the pathogenesis of type 2 diabetes mellitus and the onset of Alzheimer's disease; aberrant signalling occurs in diverse cancers, exacerbated by cross-talk with the homologous type 1 insulin-like growth factor receptor (IGF1R).
23302862	2	33	theme	factor	456:461	arg1	receptor					463:470	the homologous type 1 insulin-like growth factor receptor	414:470	the homologous type 1 insulin-like growth factor receptor (IGF1R)	414:478	Insulin resistance contributes to the pathogenesis of type 2 diabetes mellitus and the onset of Alzheimer's disease; aberrant signalling occurs in diverse cancers, exacerbated by cross-talk with the homologous type 1 insulin-like growth factor receptor (IGF1R).
23302862	8	34	theme	recognition	1493:1503	arg1	mode					1468:1471	This mode	1463:1471	This mode of hormone-receptor recognition	1463:1503	This mode of hormone-receptor recognition is novel within the broader family of receptor tyrosine kinases.
23302862	4	35	theme	primary	776:782	arg1	site					792:795	its primary binding site	772:795	its primary binding site on the insulin receptor	772:819	Here we present the first view, to our knowledge, of the interaction of insulin with its primary binding site on the insulin receptor, on the basis of four crystal structures of insulin bound to truncated insulin receptor constructs.
23302862	0	36	theme	primary	24:30	arg1	site					40:43	its primary binding site	20:43	its primary binding site on the insulin receptor	20:67	How insulin engages its primary binding site on the insulin receptor.
23302862	5	37	theme	insulin	1077:1083	arg1	itself					1143:1148	itself	1143:1148	itself	1143:1148	The direct interaction of insulin with the first leucine-rich-repeat domain (L1) of insulin receptor is seen to be sparse, the hormone instead engaging the insulin receptor carboxy-terminal α-chain (αCT) segment, which is itself remodelled on the face of L1 upon insulin binding.
23302862	5	37	theme	insulin	1077:1083	arg1	segment					1125:1131	the insulin receptor carboxy-terminal α-chain (αCT) segment	1073:1131	the insulin receptor carboxy-terminal α-chain (αCT) segment	1073:1131	The direct interaction of insulin with the first leucine-rich-repeat domain (L1) of insulin receptor is seen to be sparse, the hormone instead engaging the insulin receptor carboxy-terminal α-chain (αCT) segment, which is itself remodelled on the face of L1 upon insulin binding.
23302862	5	38	theme	leucine-rich-repeat	970:988	arg1	L1					998:999	L1	998:999	L1	998:999	The direct interaction of insulin with the first leucine-rich-repeat domain (L1) of insulin receptor is seen to be sparse, the hormone instead engaging the insulin receptor carboxy-terminal α-chain (αCT) segment, which is itself remodelled on the face of L1 upon insulin binding.
23302862	5	38	theme	leucine-rich-repeat	970:988	arg1	domain					990:995	the first leucine-rich-repeat domain	960:995	the first leucine-rich-repeat domain (L1) of insulin receptor	960:1020	The direct interaction of insulin with the first leucine-rich-repeat domain (L1) of insulin receptor is seen to be sparse, the hormone instead engaging the insulin receptor carboxy-terminal α-chain (αCT) segment, which is itself remodelled on the face of L1 upon insulin binding.
23302862	5	38	theme	leucine-rich-repeat	970:988	arg1	receptor					1013:1020	insulin receptor	1005:1020	insulin receptor	1005:1020	The direct interaction of insulin with the first leucine-rich-repeat domain (L1) of insulin receptor is seen to be sparse, the hormone instead engaging the insulin receptor carboxy-terminal α-chain (αCT) segment, which is itself remodelled on the face of L1 upon insulin binding.
23302862	2	39	theme	insulin-like	436:447	arg1	IGF1R					473:477	IGF1R	473:477	IGF1R	473:477	Insulin resistance contributes to the pathogenesis of type 2 diabetes mellitus and the onset of Alzheimer's disease; aberrant signalling occurs in diverse cancers, exacerbated by cross-talk with the homologous type 1 insulin-like growth factor receptor (IGF1R).
23302862	2	39	theme	insulin-like	436:447	arg1	receptor					463:470	the homologous type 1 insulin-like growth factor receptor	414:470	the homologous type 1 insulin-like growth factor receptor (IGF1R)	414:478	Insulin resistance contributes to the pathogenesis of type 2 diabetes mellitus and the onset of Alzheimer's disease; aberrant signalling occurs in diverse cancers, exacerbated by cross-talk with the homologous type 1 insulin-like growth factor receptor (IGF1R).
23302862	5	40	theme	carboxy-terminal	1094:1109	arg1	itself					1143:1148	itself	1143:1148	itself	1143:1148	The direct interaction of insulin with the first leucine-rich-repeat domain (L1) of insulin receptor is seen to be sparse, the hormone instead engaging the insulin receptor carboxy-terminal α-chain (αCT) segment, which is itself remodelled on the face of L1 upon insulin binding.
23302862	5	40	theme	carboxy-terminal	1094:1109	arg1	segment					1125:1131	the insulin receptor carboxy-terminal α-chain (αCT) segment	1073:1131	the insulin receptor carboxy-terminal α-chain (αCT) segment	1073:1131	The direct interaction of insulin with the first leucine-rich-repeat domain (L1) of insulin receptor is seen to be sparse, the hormone instead engaging the insulin receptor carboxy-terminal α-chain (αCT) segment, which is itself remodelled on the face of L1 upon insulin binding.
23302862	5	41	theme	insulin	947:953	arg1	sparse					1036:1041	sparse	1036:1041	sparse	1036:1041	The direct interaction of insulin with the first leucine-rich-repeat domain (L1) of insulin receptor is seen to be sparse, the hormone instead engaging the insulin receptor carboxy-terminal α-chain (αCT) segment, which is itself remodelled on the face of L1 upon insulin binding.
23302862	5	41	theme	insulin	947:953	arg1	interaction					932:942	The direct interaction	921:942	The direct interaction of insulin with the first leucine-rich-repeat domain (L1) of insulin receptor	921:1020	The direct interaction of insulin with the first leucine-rich-repeat domain (L1) of insulin receptor is seen to be sparse, the hormone instead engaging the insulin receptor carboxy-terminal α-chain (αCT) segment, which is itself remodelled on the face of L1 upon insulin binding.
23302862	5	42	theme	receptor	1085:1092	arg1	itself					1143:1148	itself	1143:1148	itself	1143:1148	The direct interaction of insulin with the first leucine-rich-repeat domain (L1) of insulin receptor is seen to be sparse, the hormone instead engaging the insulin receptor carboxy-terminal α-chain (αCT) segment, which is itself remodelled on the face of L1 upon insulin binding.
23302862	5	42	theme	receptor	1085:1092	arg1	segment					1125:1131	the insulin receptor carboxy-terminal α-chain (αCT) segment	1073:1131	the insulin receptor carboxy-terminal α-chain (αCT) segment	1073:1131	The direct interaction of insulin with the first leucine-rich-repeat domain (L1) of insulin receptor is seen to be sparse, the hormone instead engaging the insulin receptor carboxy-terminal α-chain (αCT) segment, which is itself remodelled on the face of L1 upon insulin binding.
23302862	7	43	from	insulin	1429:1435	arg1	mechanism					1375:1383	the mechanism	1371:1383	the mechanism of a long-proposed conformational switch in insulin upon receptor engagement	1371:1460	The αCT segment displaces the B-chain C-terminal β-strand away from the hormone core, revealing the mechanism of a long-proposed conformational switch in insulin upon receptor engagement.
23302862	7	44	theme	conformational	1404:1417	arg1	switch					1419:1424	a long-proposed conformational switch	1388:1424	a long-proposed conformational switch in insulin upon receptor engagement	1388:1460	The αCT segment displaces the B-chain C-terminal β-strand away from the hormone core, revealing the mechanism of a long-proposed conformational switch in insulin upon receptor engagement.
23302862	8	45	theme	receptor	1543:1550	arg1	kinases					1561:1567	receptor tyrosine kinases	1543:1567	receptor tyrosine kinases	1543:1567	This mode of hormone-receptor recognition is novel within the broader family of receptor tyrosine kinases.
23302862	4	46	attach	present	695:701	arg2	we					692:693	we	692:693	we	692:693	Here we present the first view, to our knowledge, of the interaction of insulin with its primary binding site on the insulin receptor, on the basis of four crystal structures of insulin bound to truncated insulin receptor constructs.
23302862	4	46	attach	present	695:701	arg1	basis					829:833	the basis	825:833	the basis of four crystal structures of insulin bound to truncated insulin receptor constructs	825:918	Here we present the first view, to our knowledge, of the interaction of insulin with its primary binding site on the insulin receptor, on the basis of four crystal structures of insulin bound to truncated insulin receptor constructs.
23302862	8	47	theme	kinases	1561:1567	arg1	family					1533:1538	the broader family	1521:1538	the broader family of receptor tyrosine kinases	1521:1567	This mode of hormone-receptor recognition is novel within the broader family of receptor tyrosine kinases.
23302862	10	48	theme	biochemical	1858:1868	arg1	data					1870:1873	biochemical data	1858:1873	biochemical data from the insulin receptor and IGF1R systems relevant to the design of therapeutic insulin analogues	1858:1973	Together, our findings provide an explanation for a wealth of biochemical data from the insulin receptor and IGF1R systems relevant to the design of therapeutic insulin analogues.
23302862	9	49	theme	photo-crosslinking	1599:1616	arg1	data					1618:1621	photo-crosslinking data	1599:1621	photo-crosslinking data that place the suggested interactions into the context of the holoreceptor	1599:1696	We support these findings by photo-crosslinking data that place the suggested interactions into the context of the holoreceptor and by isothermal titration calorimetry data that dissect the hormone-insulin receptor interface.
23302862	1	50	theme	cellular	150:157	arg1	metabolism					159:168	cellular metabolism	150:168	cellular metabolism	150:168	Insulin receptor signalling has a central role in mammalian biology, regulating cellular metabolism, growth, division, differentiation and survival.
23302862	10	51	from	wealth	1848:1853	arg1	receptor					1892:1899	the insulin receptor	1880:1899	the insulin receptor	1880:1899	Together, our findings provide an explanation for a wealth of biochemical data from the insulin receptor and IGF1R systems relevant to the design of therapeutic insulin analogues.
23302862	10	51	from	wealth	1848:1853	arg1	systems					1911:1917	IGF1R systems	1905:1917	IGF1R systems	1905:1917	Together, our findings provide an explanation for a wealth of biochemical data from the insulin receptor and IGF1R systems relevant to the design of therapeutic insulin analogues.
23302862	2	52	with	cross-talk	398:407	arg1	IGF1R					473:477	IGF1R	473:477	IGF1R	473:477	Insulin resistance contributes to the pathogenesis of type 2 diabetes mellitus and the onset of Alzheimer's disease; aberrant signalling occurs in diverse cancers, exacerbated by cross-talk with the homologous type 1 insulin-like growth factor receptor (IGF1R).
23302862	2	52	with	cross-talk	398:407	arg1	receptor					463:470	the homologous type 1 insulin-like growth factor receptor	414:470	the homologous type 1 insulin-like growth factor receptor (IGF1R)	414:478	Insulin resistance contributes to the pathogenesis of type 2 diabetes mellitus and the onset of Alzheimer's disease; aberrant signalling occurs in diverse cancers, exacerbated by cross-talk with the homologous type 1 insulin-like growth factor receptor (IGF1R).
23302862	7	53	theme	hormone	1347:1353	arg1	core					1355:1358	the hormone core	1343:1358	the hormone core	1343:1358	The αCT segment displaces the B-chain C-terminal β-strand away from the hormone core, revealing the mechanism of a long-proposed conformational switch in insulin upon receptor engagement.
23302862	10	54	theme	insulin	1884:1890	arg1	receptor					1892:1899	the insulin receptor	1880:1899	the insulin receptor	1880:1899	Together, our findings provide an explanation for a wealth of biochemical data from the insulin receptor and IGF1R systems relevant to the design of therapeutic insulin analogues.
23302862	3	55	theme	three-dimensional	535:551	arg1	structure					553:561	the three-dimensional structure	531:561	the three-dimensional structure of the insulin-insulin receptor complex	531:601	Despite more than three decades of investigation, the three-dimensional structure of the insulin-insulin receptor complex has proved elusive, confounded by the complexity of producing the receptor protein.
23302862	4	56	theme	insulin	804:810	arg1	receptor					812:819	the insulin receptor	800:819	the insulin receptor	800:819	Here we present the first view, to our knowledge, of the interaction of insulin with its primary binding site on the insulin receptor, on the basis of four crystal structures of insulin bound to truncated insulin receptor constructs.
23302862	6	57	theme	B-chain	1257:1263	arg1	residues					1265:1272	insulin B-chain residues	1249:1272	insulin B-chain residues	1249:1272	Contact between insulin and L1 is restricted to insulin B-chain residues.
23302862	2	58	theme	mellitus	289:296	arg1	pathogenesis					257:268	the pathogenesis	253:268	the pathogenesis of type 2 diabetes mellitus	253:296	Insulin resistance contributes to the pathogenesis of type 2 diabetes mellitus and the onset of Alzheimer's disease; aberrant signalling occurs in diverse cancers, exacerbated by cross-talk with the homologous type 1 insulin-like growth factor receptor (IGF1R).
23302862	2	58	theme	mellitus	289:296	arg1	onset					306:310	the onset	302:310	the onset of Alzheimer's disease	302:333	Insulin resistance contributes to the pathogenesis of type 2 diabetes mellitus and the onset of Alzheimer's disease; aberrant signalling occurs in diverse cancers, exacerbated by cross-talk with the homologous type 1 insulin-like growth factor receptor (IGF1R).
23302862	3	59	theme	insulin-insulin	570:584	arg1	complex					595:601	the insulin-insulin receptor complex	566:601	the insulin-insulin receptor complex	566:601	Despite more than three decades of investigation, the three-dimensional structure of the insulin-insulin receptor complex has proved elusive, confounded by the complexity of producing the receptor protein.
23302862	3	60	dep	proved	607:612	arg1	confounded					623:632	confounded	623:632	confounded by the complexity of producing the receptor protein	623:684	Despite more than three decades of investigation, the three-dimensional structure of the insulin-insulin receptor complex has proved elusive, confounded by the complexity of producing the receptor protein.
23302862	9	61	theme	calorimetry	1726:1736	arg1	data					1738:1741	isothermal titration calorimetry data	1705:1741	isothermal titration calorimetry data that dissect the hormone-insulin receptor interface	1705:1793	We support these findings by photo-crosslinking data that place the suggested interactions into the context of the holoreceptor and by isothermal titration calorimetry data that dissect the hormone-insulin receptor interface.
23302862	7	62	from	switch	1419:1424	arg1	insulin					1429:1435	insulin	1429:1435	insulin	1429:1435	The αCT segment displaces the B-chain C-terminal β-strand away from the hormone core, revealing the mechanism of a long-proposed conformational switch in insulin upon receptor engagement.
23302862	9	63	theme	suggested	1638:1646	arg1	interactions					1648:1659	the suggested interactions	1634:1659	the suggested interactions	1634:1659	We support these findings by photo-crosslinking data that place the suggested interactions into the context of the holoreceptor and by isothermal titration calorimetry data that dissect the hormone-insulin receptor interface.
23302862	9	64	theme	holoreceptor	1685:1696	arg1	context					1670:1676	the context	1666:1676	the context of the holoreceptor	1666:1696	We support these findings by photo-crosslinking data that place the suggested interactions into the context of the holoreceptor and by isothermal titration calorimetry data that dissect the hormone-insulin receptor interface.
23302862	7	65	theme	αCT	1279:1281	arg1	segment					1283:1289	The αCT segment	1275:1289	The αCT segment	1275:1289	The αCT segment displaces the B-chain C-terminal β-strand away from the hormone core, revealing the mechanism of a long-proposed conformational switch in insulin upon receptor engagement.
23302862	0	66	theme	insulin	52:58	arg1	receptor					60:67	the insulin receptor	48:67	the insulin receptor	48:67	How insulin engages its primary binding site on the insulin receptor.
23302862	5	67	theme	insulin	1005:1011	arg1	receptor					1013:1020	insulin receptor	1005:1020	insulin receptor	1005:1020	The direct interaction of insulin with the first leucine-rich-repeat domain (L1) of insulin receptor is seen to be sparse, the hormone instead engaging the insulin receptor carboxy-terminal α-chain (αCT) segment, which is itself remodelled on the face of L1 upon insulin binding.
23302862	3	68	theme	complex	595:601	arg1	structure					553:561	the three-dimensional structure	531:561	the three-dimensional structure of the insulin-insulin receptor complex	531:601	Despite more than three decades of investigation, the three-dimensional structure of the insulin-insulin receptor complex has proved elusive, confounded by the complexity of producing the receptor protein.
23302862	1	69	theme	mammalian	120:128	arg1	biology					130:136	mammalian biology	120:136	mammalian biology	120:136	Insulin receptor signalling has a central role in mammalian biology, regulating cellular metabolism, growth, division, differentiation and survival.
23302862	10	70	theme	analogues	1965:1973	arg1	design					1935:1940	the design	1931:1940	the design of therapeutic insulin analogues	1931:1973	Together, our findings provide an explanation for a wealth of biochemical data from the insulin receptor and IGF1R systems relevant to the design of therapeutic insulin analogues.
23302862	9	71	theme	titration	1716:1724	arg1	calorimetry					1726:1736	isothermal titration calorimetry	1705:1736	isothermal titration calorimetry data that dissect the hormone-insulin receptor interface	1705:1793	We support these findings by photo-crosslinking data that place the suggested interactions into the context of the holoreceptor and by isothermal titration calorimetry data that dissect the hormone-insulin receptor interface.
23302862	4	72	theme	truncated	882:890	arg1	constructs					909:918	truncated insulin receptor constructs	882:918	truncated insulin receptor constructs	882:918	Here we present the first view, to our knowledge, of the interaction of insulin with its primary binding site on the insulin receptor, on the basis of four crystal structures of insulin bound to truncated insulin receptor constructs.
23302862	4	73	with	interaction	744:754	arg1	site					792:795	its primary binding site	772:795	its primary binding site on the insulin receptor	772:819	Here we present the first view, to our knowledge, of the interaction of insulin with its primary binding site on the insulin receptor, on the basis of four crystal structures of insulin bound to truncated insulin receptor constructs.
23302862	5	74	theme	direct	925:930	arg1	sparse					1036:1041	sparse	1036:1041	sparse	1036:1041	The direct interaction of insulin with the first leucine-rich-repeat domain (L1) of insulin receptor is seen to be sparse, the hormone instead engaging the insulin receptor carboxy-terminal α-chain (αCT) segment, which is itself remodelled on the face of L1 upon insulin binding.
23302862	5	74	theme	direct	925:930	arg1	interaction					932:942	The direct interaction	921:942	The direct interaction of insulin with the first leucine-rich-repeat domain (L1) of insulin receptor	921:1020	The direct interaction of insulin with the first leucine-rich-repeat domain (L1) of insulin receptor is seen to be sparse, the hormone instead engaging the insulin receptor carboxy-terminal α-chain (αCT) segment, which is itself remodelled on the face of L1 upon insulin binding.
23302862	4	75	theme	receptor	900:907	arg1	constructs					909:918	truncated insulin receptor constructs	882:918	truncated insulin receptor constructs	882:918	Here we present the first view, to our knowledge, of the interaction of insulin with its primary binding site on the insulin receptor, on the basis of four crystal structures of insulin bound to truncated insulin receptor constructs.
23302862	2	76	theme	diverse	366:372	arg1	cancers					374:380	diverse cancers	366:380	diverse cancers	366:380	Insulin resistance contributes to the pathogenesis of type 2 diabetes mellitus and the onset of Alzheimer's disease; aberrant signalling occurs in diverse cancers, exacerbated by cross-talk with the homologous type 1 insulin-like growth factor receptor (IGF1R).
23302862	1	77	theme	Insulin	70:76	arg1	signalling					87:96	Insulin receptor signalling	70:96	Insulin receptor signalling	70:96	Insulin receptor signalling has a central role in mammalian biology, regulating cellular metabolism, growth, division, differentiation and survival.
23302862	9	78	theme	hormone-insulin	1760:1774	arg1	interface					1785:1793	the hormone-insulin receptor interface	1756:1793	the hormone-insulin receptor interface	1756:1793	We support these findings by photo-crosslinking data that place the suggested interactions into the context of the holoreceptor and by isothermal titration calorimetry data that dissect the hormone-insulin receptor interface.
23302862	8	79	theme	hormone-receptor	1476:1491	arg1	recognition					1493:1503	hormone-receptor recognition	1476:1503	hormone-receptor recognition	1476:1503	This mode of hormone-receptor recognition is novel within the broader family of receptor tyrosine kinases.
23302862	5	80	theme	αCT	1120:1122	arg1	itself					1143:1148	itself	1143:1148	itself	1143:1148	The direct interaction of insulin with the first leucine-rich-repeat domain (L1) of insulin receptor is seen to be sparse, the hormone instead engaging the insulin receptor carboxy-terminal α-chain (αCT) segment, which is itself remodelled on the face of L1 upon insulin binding.
23302862	5	80	theme	αCT	1120:1122	arg1	segment					1125:1131	the insulin receptor carboxy-terminal α-chain (αCT) segment	1073:1131	the insulin receptor carboxy-terminal α-chain (αCT) segment	1073:1131	The direct interaction of insulin with the first leucine-rich-repeat domain (L1) of insulin receptor is seen to be sparse, the hormone instead engaging the insulin receptor carboxy-terminal α-chain (αCT) segment, which is itself remodelled on the face of L1 upon insulin binding.
23302862	2	81	theme	Insulin	219:225	arg1	resistance					227:236	Insulin resistance	219:236	Insulin resistance	219:236	Insulin resistance contributes to the pathogenesis of type 2 diabetes mellitus and the onset of Alzheimer's disease; aberrant signalling occurs in diverse cancers, exacerbated by cross-talk with the homologous type 1 insulin-like growth factor receptor (IGF1R).
23302862	0	82	theme	binding	32:38	arg1	site					40:43	its primary binding site	20:43	its primary binding site on the insulin receptor	20:67	How insulin engages its primary binding site on the insulin receptor.
23302862	5	83	theme	first	964:968	arg1	L1					998:999	L1	998:999	L1	998:999	The direct interaction of insulin with the first leucine-rich-repeat domain (L1) of insulin receptor is seen to be sparse, the hormone instead engaging the insulin receptor carboxy-terminal α-chain (αCT) segment, which is itself remodelled on the face of L1 upon insulin binding.
23302862	5	83	theme	first	964:968	arg1	domain					990:995	the first leucine-rich-repeat domain	960:995	the first leucine-rich-repeat domain (L1) of insulin receptor	960:1020	The direct interaction of insulin with the first leucine-rich-repeat domain (L1) of insulin receptor is seen to be sparse, the hormone instead engaging the insulin receptor carboxy-terminal α-chain (αCT) segment, which is itself remodelled on the face of L1 upon insulin binding.
23302862	5	83	theme	first	964:968	arg1	receptor					1013:1020	insulin receptor	1005:1020	insulin receptor	1005:1020	The direct interaction of insulin with the first leucine-rich-repeat domain (L1) of insulin receptor is seen to be sparse, the hormone instead engaging the insulin receptor carboxy-terminal α-chain (αCT) segment, which is itself remodelled on the face of L1 upon insulin binding.
23302862	2	84	theme	growth	449:454	arg1	IGF1R					473:477	IGF1R	473:477	IGF1R	473:477	Insulin resistance contributes to the pathogenesis of type 2 diabetes mellitus and the onset of Alzheimer's disease; aberrant signalling occurs in diverse cancers, exacerbated by cross-talk with the homologous type 1 insulin-like growth factor receptor (IGF1R).
23302862	2	84	theme	growth	449:454	arg1	receptor					463:470	the homologous type 1 insulin-like growth factor receptor	414:470	the homologous type 1 insulin-like growth factor receptor (IGF1R)	414:478	Insulin resistance contributes to the pathogenesis of type 2 diabetes mellitus and the onset of Alzheimer's disease; aberrant signalling occurs in diverse cancers, exacerbated by cross-talk with the homologous type 1 insulin-like growth factor receptor (IGF1R).
23302862	1	85	contain	has	98:100	arg1	signalling					87:96	Insulin receptor signalling	70:96	Insulin receptor signalling	70:96	Insulin receptor signalling has a central role in mammalian biology, regulating cellular metabolism, growth, division, differentiation and survival.
23302862	1	85	contain	has	98:100	arg2	role					112:115	a central role	102:115	a central role	102:115	Insulin receptor signalling has a central role in mammalian biology, regulating cellular metabolism, growth, division, differentiation and survival.
23302862	8	86	theme	broader	1525:1531	arg1	family					1533:1538	the broader family	1521:1538	the broader family of receptor tyrosine kinases	1521:1567	This mode of hormone-receptor recognition is novel within the broader family of receptor tyrosine kinases.
23302862	4	87	theme	binding	784:790	arg1	site					792:795	its primary binding site	772:795	its primary binding site on the insulin receptor	772:819	Here we present the first view, to our knowledge, of the interaction of insulin with its primary binding site on the insulin receptor, on the basis of four crystal structures of insulin bound to truncated insulin receptor constructs.
23302862	5	88	theme	α-chain	1111:1117	arg1	itself					1143:1148	itself	1143:1148	itself	1143:1148	The direct interaction of insulin with the first leucine-rich-repeat domain (L1) of insulin receptor is seen to be sparse, the hormone instead engaging the insulin receptor carboxy-terminal α-chain (αCT) segment, which is itself remodelled on the face of L1 upon insulin binding.
23302862	5	88	theme	α-chain	1111:1117	arg1	segment					1125:1131	the insulin receptor carboxy-terminal α-chain (αCT) segment	1073:1131	the insulin receptor carboxy-terminal α-chain (αCT) segment	1073:1131	The direct interaction of insulin with the first leucine-rich-repeat domain (L1) of insulin receptor is seen to be sparse, the hormone instead engaging the insulin receptor carboxy-terminal α-chain (αCT) segment, which is itself remodelled on the face of L1 upon insulin binding.
23302862	7	89	theme	receptor	1442:1449	arg1	engagement					1451:1460	receptor engagement	1442:1460	receptor engagement	1442:1460	The αCT segment displaces the B-chain C-terminal β-strand away from the hormone core, revealing the mechanism of a long-proposed conformational switch in insulin upon receptor engagement.
23302862	4	90	theme	interaction	744:754	arg1	view					713:716	the first view	703:716	the first view	703:716	Here we present the first view, to our knowledge, of the interaction of insulin with its primary binding site on the insulin receptor, on the basis of four crystal structures of insulin bound to truncated insulin receptor constructs.
23302862	8	91	theme	tyrosine	1552:1559	arg1	kinases					1561:1567	receptor tyrosine kinases	1543:1567	receptor tyrosine kinases	1543:1567	This mode of hormone-receptor recognition is novel within the broader family of receptor tyrosine kinases.
23302862	4	92	theme	insulin	759:765	arg1	interaction					744:754	the interaction	740:754	the interaction of insulin with its primary binding site on the insulin receptor	740:819	Here we present the first view, to our knowledge, of the interaction of insulin with its primary binding site on the insulin receptor, on the basis of four crystal structures of insulin bound to truncated insulin receptor constructs.
23302862	2	93	theme	aberrant	336:343	arg1	signalling					345:354	aberrant signalling	336:354	aberrant signalling	336:354	Insulin resistance contributes to the pathogenesis of type 2 diabetes mellitus and the onset of Alzheimer's disease; aberrant signalling occurs in diverse cancers, exacerbated by cross-talk with the homologous type 1 insulin-like growth factor receptor (IGF1R).
23302862	10	94	theme	therapeutic	1945:1955	arg1	analogues					1965:1973	therapeutic insulin analogues	1945:1973	therapeutic insulin analogues	1945:1973	Together, our findings provide an explanation for a wealth of biochemical data from the insulin receptor and IGF1R systems relevant to the design of therapeutic insulin analogues.
16894147	6	0	theme	second	964:969	arg1	difference					977:986	The second major difference	960:986	The second major difference	960:986	The second major difference is in the sixth module of the CR domain, where IR contains a larger loop that protrudes further into the ligand-binding pocket.
16894147	0	1	theme	ligand	140:145	arg1	specificity					147:157	ligand specificity	140:157	ligand specificity	140:157	The first three domains of the insulin receptor differ structurally from the insulin-like growth factor 1 receptor in the regions governing ligand specificity.
16894147	2	2	theme	A	429:429	arg1	resolution					431:440	2.3 A resolution	425:440	2.3 A resolution	425:440	Here we report the crystal structure of the first three domains (L1-CR-L2) of human IR at 2.3 A resolution and compare it with the previously determined structure of the corresponding fragment of IGF1R.
16894147	3	3	theme	ligand	633:638	arg1	specificity					640:650	ligand specificity	633:650	ligand specificity	633:650	The most important differences seen between the two receptors are in the two regions governing ligand specificity.
16894147	0	4	theme	growth	90:95	arg1	receptor					106:113	the insulin-like growth factor 1 receptor	73:113	the insulin-like growth factor 1 receptor in the regions governing ligand specificity	73:157	The first three domains of the insulin receptor differ structurally from the insulin-like growth factor 1 receptor in the regions governing ligand specificity.
16894147	6	5	theme	larger	1049:1054	arg1	loop					1056:1059	a larger loop	1047:1059	a larger loop that protrudes further into the ligand-binding pocket	1047:1113	The second major difference is in the sixth module of the CR domain, where IR contains a larger loop that protrudes further into the ligand-binding pocket.
16894147	4	6	theme	binding	787:793	arg1	surface					795:801	the ligand binding surface	776:801	the ligand binding surface involving the second (central) beta-sheet	776:843	The first is at the corner of the ligand-binding surface of the L1 domain, where the side chain of F39 in IR forms part of the ligand binding surface involving the second (central) beta-sheet.
16894147	0	7	theme	insulin-like	77:88	arg1	receptor					106:113	the insulin-like growth factor 1 receptor	73:113	the insulin-like growth factor 1 receptor in the regions governing ligand specificity	73:157	The first three domains of the insulin receptor differ structurally from the insulin-like growth factor 1 receptor in the regions governing ligand specificity.
16894147	4	8	theme	ligand	780:785	arg1	surface					795:801	the ligand binding surface	776:801	the ligand binding surface involving the second (central) beta-sheet	776:843	The first is at the corner of the ligand-binding surface of the L1 domain, where the side chain of F39 in IR forms part of the ligand binding surface involving the second (central) beta-sheet.
16894147	4	9	theme	surface	702:708	arg1	corner					673:678	the corner	669:678	the corner of the ligand-binding surface of the L1 domain, where the side chain of F39 in IR forms part of the ligand binding surface involving the second (central) beta-sheet	669:843	The first is at the corner of the ligand-binding surface of the L1 domain, where the side chain of F39 in IR forms part of the ligand binding surface involving the second (central) beta-sheet.
16894147	5	10	from	counterpart	892:902	arg1	S35					914:916	S35	914:916	S35	914:916	This is very different to the location of its counterpart in IGF1R, S35, which is not involved in ligand binding.
16894147	5	10	from	counterpart	892:902	arg1	IGF1R					907:911	IGF1R	907:911	IGF1R	907:911	This is very different to the location of its counterpart in IGF1R, S35, which is not involved in ligand binding.
16894147	7	11	theme	disulfide	1251:1259	arg1	bond					1261:1264	an additional disulfide bond	1237:1264	an additional disulfide bond	1237:1264	This module, which governs IGF1-binding specificity, shows negligible sequence identity, significantly more alpha-helix, an additional disulfide bond, and opposite electrostatic potential compared to that of the IGF1R.
16894147	5	12	from	location	876:883	arg1	S35					914:916	S35	914:916	S35	914:916	This is very different to the location of its counterpart in IGF1R, S35, which is not involved in ligand binding.
16894147	5	12	from	location	876:883	arg1	IGF1R					907:911	IGF1R	907:911	IGF1R	907:911	This is very different to the location of its counterpart in IGF1R, S35, which is not involved in ligand binding.
16894147	4	13	theme	L1	717:718	arg1	domain					720:725	the L1 domain	713:725	the L1 domain	713:725	The first is at the corner of the ligand-binding surface of the L1 domain, where the side chain of F39 in IR forms part of the ligand binding surface involving the second (central) beta-sheet.
16894147	7	14	theme	sequence	1186:1193	arg1	identity					1195:1202	negligible sequence identity	1175:1202	negligible sequence identity	1175:1202	This module, which governs IGF1-binding specificity, shows negligible sequence identity, significantly more alpha-helix, an additional disulfide bond, and opposite electrostatic potential compared to that of the IGF1R.
16894147	0	15	theme	factor	97:102	arg1	receptor					106:113	the insulin-like growth factor 1 receptor	73:113	the insulin-like growth factor 1 receptor in the regions governing ligand specificity	73:157	The first three domains of the insulin receptor differ structurally from the insulin-like growth factor 1 receptor in the regions governing ligand specificity.
16894147	6	16	theme	domain	1021:1026	arg1	module					1004:1009	the sixth module	994:1009	the sixth module of the CR domain	994:1026	The second major difference is in the sixth module of the CR domain, where IR contains a larger loop that protrudes further into the ligand-binding pocket.
16894147	1	17	theme	insulin	164:170	arg1	receptor					172:179	The insulin receptor	160:179	The insulin receptor (IR)	160:184	The insulin receptor (IR) and the type-1 insulin-like growth factor receptor (IGF1R) are homologous multidomain proteins that bind insulin and IGF with differing specificity.
16894147	1	17	theme	insulin	164:170	arg1	proteins					272:279	homologous multidomain proteins	249:279	homologous multidomain proteins that bind insulin and IGF with differing specificity	249:332	The insulin receptor (IR) and the type-1 insulin-like growth factor receptor (IGF1R) are homologous multidomain proteins that bind insulin and IGF with differing specificity.
16894147	1	17	theme	insulin	164:170	arg1	receptor					228:235	the type-1 insulin-like growth factor receptor	190:235	the type-1 insulin-like growth factor receptor (IGF1R)	190:243	The insulin receptor (IR) and the type-1 insulin-like growth factor receptor (IGF1R) are homologous multidomain proteins that bind insulin and IGF with differing specificity.
16894147	1	17	theme	insulin	164:170	arg1	IR					182:183	IR	182:183	IR	182:183	The insulin receptor (IR) and the type-1 insulin-like growth factor receptor (IGF1R) are homologous multidomain proteins that bind insulin and IGF with differing specificity.
16894147	0	18	theme	first	4:8	arg1	domains					16:22	The first three domains	0:22	The first three domains of the insulin receptor	0:46	The first three domains of the insulin receptor differ structurally from the insulin-like growth factor 1 receptor in the regions governing ligand specificity.
16894147	0	18	theme	first	4:8	arg1	receptor					39:46	the insulin receptor	27:46	the insulin receptor	27:46	The first three domains of the insulin receptor differ structurally from the insulin-like growth factor 1 receptor in the regions governing ligand specificity.
16894147	6	19	theme	ligand-binding	1093:1106	arg1	pocket					1108:1113	the ligand-binding pocket	1089:1113	the ligand-binding pocket	1089:1113	The second major difference is in the sixth module of the CR domain, where IR contains a larger loop that protrudes further into the ligand-binding pocket.
16894147	6	20	theme	CR	1018:1019	arg1	domain					1021:1026	the CR domain	1014:1026	the CR domain	1014:1026	The second major difference is in the sixth module of the CR domain, where IR contains a larger loop that protrudes further into the ligand-binding pocket.
16894147	2	21	theme	crystal	354:360	arg1	structure					362:370	the crystal structure	350:370	the crystal structure of the first three domains (L1-CR-L2) of human IR at 2.3 A resolution	350:440	Here we report the crystal structure of the first three domains (L1-CR-L2) of human IR at 2.3 A resolution and compare it with the previously determined structure of the corresponding fragment of IGF1R.
16894147	7	22	theme	opposite	1271:1278	arg1	potential					1294:1302	opposite electrostatic potential	1271:1302	opposite electrostatic potential	1271:1302	This module, which governs IGF1-binding specificity, shows negligible sequence identity, significantly more alpha-helix, an additional disulfide bond, and opposite electrostatic potential compared to that of the IGF1R.
16894147	7	23	theme	negligible	1175:1184	arg1	identity					1195:1202	negligible sequence identity	1175:1202	negligible sequence identity	1175:1202	This module, which governs IGF1-binding specificity, shows negligible sequence identity, significantly more alpha-helix, an additional disulfide bond, and opposite electrostatic potential compared to that of the IGF1R.
16894147	1	24	theme	homologous	249:258	arg1	receptor					172:179	The insulin receptor	160:179	The insulin receptor (IR)	160:184	The insulin receptor (IR) and the type-1 insulin-like growth factor receptor (IGF1R) are homologous multidomain proteins that bind insulin and IGF with differing specificity.
16894147	1	24	theme	homologous	249:258	arg1	proteins					272:279	homologous multidomain proteins	249:279	homologous multidomain proteins that bind insulin and IGF with differing specificity	249:332	The insulin receptor (IR) and the type-1 insulin-like growth factor receptor (IGF1R) are homologous multidomain proteins that bind insulin and IGF with differing specificity.
16894147	1	24	theme	homologous	249:258	arg1	receptor					228:235	the type-1 insulin-like growth factor receptor	190:235	the type-1 insulin-like growth factor receptor (IGF1R)	190:243	The insulin receptor (IR) and the type-1 insulin-like growth factor receptor (IGF1R) are homologous multidomain proteins that bind insulin and IGF with differing specificity.
16894147	4	25	theme	ligand-binding	687:700	arg1	surface					702:708	the ligand-binding surface	683:708	the ligand-binding surface of the L1 domain, where the side chain of F39 in IR forms part of the ligand binding surface involving the second (central) beta-sheet	683:843	The first is at the corner of the ligand-binding surface of the L1 domain, where the side chain of F39 in IR forms part of the ligand binding surface involving the second (central) beta-sheet.
16894147	2	26	theme	domains	391:397	arg1	structure					362:370	the crystal structure	350:370	the crystal structure of the first three domains (L1-CR-L2) of human IR at 2.3 A resolution	350:440	Here we report the crystal structure of the first three domains (L1-CR-L2) of human IR at 2.3 A resolution and compare it with the previously determined structure of the corresponding fragment of IGF1R.
16894147	1	27	theme	multidomain	260:270	arg1	receptor					172:179	The insulin receptor	160:179	The insulin receptor (IR)	160:184	The insulin receptor (IR) and the type-1 insulin-like growth factor receptor (IGF1R) are homologous multidomain proteins that bind insulin and IGF with differing specificity.
16894147	1	27	theme	multidomain	260:270	arg1	proteins					272:279	homologous multidomain proteins	249:279	homologous multidomain proteins that bind insulin and IGF with differing specificity	249:332	The insulin receptor (IR) and the type-1 insulin-like growth factor receptor (IGF1R) are homologous multidomain proteins that bind insulin and IGF with differing specificity.
16894147	1	27	theme	multidomain	260:270	arg1	receptor					228:235	the type-1 insulin-like growth factor receptor	190:235	the type-1 insulin-like growth factor receptor (IGF1R)	190:243	The insulin receptor (IR) and the type-1 insulin-like growth factor receptor (IGF1R) are homologous multidomain proteins that bind insulin and IGF with differing specificity.
16894147	7	28	theme	electrostatic	1280:1292	arg1	potential					1294:1302	opposite electrostatic potential	1271:1302	opposite electrostatic potential	1271:1302	This module, which governs IGF1-binding specificity, shows negligible sequence identity, significantly more alpha-helix, an additional disulfide bond, and opposite electrostatic potential compared to that of the IGF1R.
16894147	2	29	from	resolution	431:440	arg1	structure					362:370	the crystal structure	350:370	the crystal structure of the first three domains (L1-CR-L2) of human IR at 2.3 A resolution	350:440	Here we report the crystal structure of the first three domains (L1-CR-L2) of human IR at 2.3 A resolution and compare it with the previously determined structure of the corresponding fragment of IGF1R.
16894147	5	30	from	IGF1R	907:911	arg1	location					876:883	the location	872:883	the location	872:883	This is very different to the location of its counterpart in IGF1R, S35, which is not involved in ligand binding.
16894147	5	31	theme	ligand	944:949	arg1	binding					951:957	ligand binding	944:957	ligand binding	944:957	This is very different to the location of its counterpart in IGF1R, S35, which is not involved in ligand binding.
16894147	7	32	theme	additional	1240:1249	arg1	bond					1261:1264	an additional disulfide bond	1237:1264	an additional disulfide bond	1237:1264	This module, which governs IGF1-binding specificity, shows negligible sequence identity, significantly more alpha-helix, an additional disulfide bond, and opposite electrostatic potential compared to that of the IGF1R.
16894147	2	33	theme	first	379:383	arg1	IR					419:420	human IR	413:420	human IR	413:420	Here we report the crystal structure of the first three domains (L1-CR-L2) of human IR at 2.3 A resolution and compare it with the previously determined structure of the corresponding fragment of IGF1R.
16894147	2	33	theme	first	379:383	arg1	L1-CR-L2					400:407	L1-CR-L2	400:407	L1-CR-L2	400:407	Here we report the crystal structure of the first three domains (L1-CR-L2) of human IR at 2.3 A resolution and compare it with the previously determined structure of the corresponding fragment of IGF1R.
16894147	2	33	theme	first	379:383	arg1	domains					391:397	the first three domains	375:397	the first three domains (L1-CR-L2) of human IR	375:420	Here we report the crystal structure of the first three domains (L1-CR-L2) of human IR at 2.3 A resolution and compare it with the previously determined structure of the corresponding fragment of IGF1R.
16894147	6	34	contain	contains	1038:1045	arg2	loop					1056:1059	a larger loop	1047:1059	a larger loop that protrudes further into the ligand-binding pocket	1047:1113	The second major difference is in the sixth module of the CR domain, where IR contains a larger loop that protrudes further into the ligand-binding pocket.
16894147	6	34	contain	contains	1038:1045	arg1	IR					1035:1036	IR	1035:1036	IR	1035:1036	The second major difference is in the sixth module of the CR domain, where IR contains a larger loop that protrudes further into the ligand-binding pocket.
16894147	2	35	theme	determined	477:486	arg1	structure					488:496	the previously determined structure	462:496	the previously determined structure of the corresponding fragment of IGF1R	462:535	Here we report the crystal structure of the first three domains (L1-CR-L2) of human IR at 2.3 A resolution and compare it with the previously determined structure of the corresponding fragment of IGF1R.
16894147	3	36	theme	important	547:555	arg1	differences					557:567	The most important differences	538:567	The most important differences seen between the two receptors	538:598	The most important differences seen between the two receptors are in the two regions governing ligand specificity.
16894147	7	37	theme	IGF1-binding	1143:1154	arg1	specificity					1156:1166	IGF1-binding specificity	1143:1166	IGF1-binding specificity	1143:1166	This module, which governs IGF1-binding specificity, shows negligible sequence identity, significantly more alpha-helix, an additional disulfide bond, and opposite electrostatic potential compared to that of the IGF1R.
16894147	2	38	theme	IR	419:420	arg1	IR					419:420	human IR	413:420	human IR	413:420	Here we report the crystal structure of the first three domains (L1-CR-L2) of human IR at 2.3 A resolution and compare it with the previously determined structure of the corresponding fragment of IGF1R.
16894147	2	38	theme	IR	419:420	arg1	L1-CR-L2					400:407	L1-CR-L2	400:407	L1-CR-L2	400:407	Here we report the crystal structure of the first three domains (L1-CR-L2) of human IR at 2.3 A resolution and compare it with the previously determined structure of the corresponding fragment of IGF1R.
16894147	2	38	theme	IR	419:420	arg1	domains					391:397	the first three domains	375:397	the first three domains (L1-CR-L2) of human IR	375:420	Here we report the crystal structure of the first three domains (L1-CR-L2) of human IR at 2.3 A resolution and compare it with the previously determined structure of the corresponding fragment of IGF1R.
16894147	2	39	theme	IGF1R	531:535	arg1	fragment					519:526	the corresponding fragment	501:526	the corresponding fragment of IGF1R	501:535	Here we report the crystal structure of the first three domains (L1-CR-L2) of human IR at 2.3 A resolution and compare it with the previously determined structure of the corresponding fragment of IGF1R.
16894147	4	40	theme	F39	752:754	arg1	chain					743:747	the side chain	734:747	the side chain of F39 in IR	734:760	The first is at the corner of the ligand-binding surface of the L1 domain, where the side chain of F39 in IR forms part of the ligand binding surface involving the second (central) beta-sheet.
16894147	6	41	theme	sixth	998:1002	arg1	module					1004:1009	the sixth module	994:1009	the sixth module of the CR domain	994:1026	The second major difference is in the sixth module of the CR domain, where IR contains a larger loop that protrudes further into the ligand-binding pocket.
16894147	0	42	theme	insulin	31:37	arg1	receptor					39:46	the insulin receptor	27:46	the insulin receptor	27:46	The first three domains of the insulin receptor differ structurally from the insulin-like growth factor 1 receptor in the regions governing ligand specificity.
16894147	4	43	theme	surface	795:801	arg1	part					768:771	part	768:771	part of the ligand binding surface involving the second (central) beta-sheet	768:843	The first is at the corner of the ligand-binding surface of the L1 domain, where the side chain of F39 in IR forms part of the ligand binding surface involving the second (central) beta-sheet.
16894147	2	44	theme	human	413:417	arg1	IR					419:420	human IR	413:420	human IR	413:420	Here we report the crystal structure of the first three domains (L1-CR-L2) of human IR at 2.3 A resolution and compare it with the previously determined structure of the corresponding fragment of IGF1R.
16894147	4	45	from	chain	743:747	arg1	IR					759:760	IR	759:760	IR	759:760	The first is at the corner of the ligand-binding surface of the L1 domain, where the side chain of F39 in IR forms part of the ligand binding surface involving the second (central) beta-sheet.
16894147	2	46	theme	fragment	519:526	arg1	structure					488:496	the previously determined structure	462:496	the previously determined structure of the corresponding fragment of IGF1R	462:535	Here we report the crystal structure of the first three domains (L1-CR-L2) of human IR at 2.3 A resolution and compare it with the previously determined structure of the corresponding fragment of IGF1R.
16894147	4	47	theme	side	738:741	arg1	chain					743:747	the side chain	734:747	the side chain of F39 in IR	734:760	The first is at the corner of the ligand-binding surface of the L1 domain, where the side chain of F39 in IR forms part of the ligand binding surface involving the second (central) beta-sheet.
16894147	1	48	theme	type-1	194:199	arg1	receptor					172:179	The insulin receptor	160:179	The insulin receptor (IR)	160:184	The insulin receptor (IR) and the type-1 insulin-like growth factor receptor (IGF1R) are homologous multidomain proteins that bind insulin and IGF with differing specificity.
16894147	1	48	theme	type-1	194:199	arg1	proteins					272:279	homologous multidomain proteins	249:279	homologous multidomain proteins that bind insulin and IGF with differing specificity	249:332	The insulin receptor (IR) and the type-1 insulin-like growth factor receptor (IGF1R) are homologous multidomain proteins that bind insulin and IGF with differing specificity.
16894147	1	48	theme	type-1	194:199	arg1	IGF1R					238:242	IGF1R	238:242	IGF1R	238:242	The insulin receptor (IR) and the type-1 insulin-like growth factor receptor (IGF1R) are homologous multidomain proteins that bind insulin and IGF with differing specificity.
16894147	1	48	theme	type-1	194:199	arg1	receptor					228:235	the type-1 insulin-like growth factor receptor	190:235	the type-1 insulin-like growth factor receptor (IGF1R)	190:243	The insulin receptor (IR) and the type-1 insulin-like growth factor receptor (IGF1R) are homologous multidomain proteins that bind insulin and IGF with differing specificity.
16894147	2	49	theme	corresponding	505:517	arg1	fragment					519:526	the corresponding fragment	501:526	the corresponding fragment of IGF1R	501:535	Here we report the crystal structure of the first three domains (L1-CR-L2) of human IR at 2.3 A resolution and compare it with the previously determined structure of the corresponding fragment of IGF1R.
16894147	4	50	theme	domain	720:725	arg1	surface					702:708	the ligand-binding surface	683:708	the ligand-binding surface of the L1 domain, where the side chain of F39 in IR forms part of the ligand binding surface involving the second (central) beta-sheet	683:843	The first is at the corner of the ligand-binding surface of the L1 domain, where the side chain of F39 in IR forms part of the ligand binding surface involving the second (central) beta-sheet.
16894147	1	51	theme	insulin-like	201:212	arg1	receptor					172:179	The insulin receptor	160:179	The insulin receptor (IR)	160:184	The insulin receptor (IR) and the type-1 insulin-like growth factor receptor (IGF1R) are homologous multidomain proteins that bind insulin and IGF with differing specificity.
16894147	1	51	theme	insulin-like	201:212	arg1	proteins					272:279	homologous multidomain proteins	249:279	homologous multidomain proteins that bind insulin and IGF with differing specificity	249:332	The insulin receptor (IR) and the type-1 insulin-like growth factor receptor (IGF1R) are homologous multidomain proteins that bind insulin and IGF with differing specificity.
16894147	1	51	theme	insulin-like	201:212	arg1	IGF1R					238:242	IGF1R	238:242	IGF1R	238:242	The insulin receptor (IR) and the type-1 insulin-like growth factor receptor (IGF1R) are homologous multidomain proteins that bind insulin and IGF with differing specificity.
16894147	1	51	theme	insulin-like	201:212	arg1	receptor					228:235	the type-1 insulin-like growth factor receptor	190:235	the type-1 insulin-like growth factor receptor (IGF1R)	190:243	The insulin receptor (IR) and the type-1 insulin-like growth factor receptor (IGF1R) are homologous multidomain proteins that bind insulin and IGF with differing specificity.
16894147	4	52	dep	second	817:822	arg1	central					825:831	central	825:831	central	825:831	The first is at the corner of the ligand-binding surface of the L1 domain, where the side chain of F39 in IR forms part of the ligand binding surface involving the second (central) beta-sheet.
16894147	5	53	theme	counterpart	892:902	arg1	location					876:883	the location	872:883	the location	872:883	This is very different to the location of its counterpart in IGF1R, S35, which is not involved in ligand binding.
16894147	1	54	theme	growth	214:219	arg1	receptor					172:179	The insulin receptor	160:179	The insulin receptor (IR)	160:184	The insulin receptor (IR) and the type-1 insulin-like growth factor receptor (IGF1R) are homologous multidomain proteins that bind insulin and IGF with differing specificity.
16894147	1	54	theme	growth	214:219	arg1	proteins					272:279	homologous multidomain proteins	249:279	homologous multidomain proteins that bind insulin and IGF with differing specificity	249:332	The insulin receptor (IR) and the type-1 insulin-like growth factor receptor (IGF1R) are homologous multidomain proteins that bind insulin and IGF with differing specificity.
16894147	1	54	theme	growth	214:219	arg1	IGF1R					238:242	IGF1R	238:242	IGF1R	238:242	The insulin receptor (IR) and the type-1 insulin-like growth factor receptor (IGF1R) are homologous multidomain proteins that bind insulin and IGF with differing specificity.
16894147	1	54	theme	growth	214:219	arg1	receptor					228:235	the type-1 insulin-like growth factor receptor	190:235	the type-1 insulin-like growth factor receptor (IGF1R)	190:243	The insulin receptor (IR) and the type-1 insulin-like growth factor receptor (IGF1R) are homologous multidomain proteins that bind insulin and IGF with differing specificity.
16894147	0	55	theme	receptor	39:46	arg1	domains					16:22	The first three domains	0:22	The first three domains of the insulin receptor	0:46	The first three domains of the insulin receptor differ structurally from the insulin-like growth factor 1 receptor in the regions governing ligand specificity.
16894147	0	55	theme	receptor	39:46	arg1	receptor					39:46	the insulin receptor	27:46	the insulin receptor	27:46	The first three domains of the insulin receptor differ structurally from the insulin-like growth factor 1 receptor in the regions governing ligand specificity.
16894147	0	56	from	receptor	106:113	arg1	regions					122:128	the regions	118:128	the regions governing ligand specificity	118:157	The first three domains of the insulin receptor differ structurally from the insulin-like growth factor 1 receptor in the regions governing ligand specificity.
16894147	6	57	theme	major	971:975	arg1	difference					977:986	The second major difference	960:986	The second major difference	960:986	The second major difference is in the sixth module of the CR domain, where IR contains a larger loop that protrudes further into the ligand-binding pocket.
16894147	1	58	theme	factor	221:226	arg1	receptor					172:179	The insulin receptor	160:179	The insulin receptor (IR)	160:184	The insulin receptor (IR) and the type-1 insulin-like growth factor receptor (IGF1R) are homologous multidomain proteins that bind insulin and IGF with differing specificity.
16894147	1	58	theme	factor	221:226	arg1	proteins					272:279	homologous multidomain proteins	249:279	homologous multidomain proteins that bind insulin and IGF with differing specificity	249:332	The insulin receptor (IR) and the type-1 insulin-like growth factor receptor (IGF1R) are homologous multidomain proteins that bind insulin and IGF with differing specificity.
16894147	1	58	theme	factor	221:226	arg1	IGF1R					238:242	IGF1R	238:242	IGF1R	238:242	The insulin receptor (IR) and the type-1 insulin-like growth factor receptor (IGF1R) are homologous multidomain proteins that bind insulin and IGF with differing specificity.
16894147	1	58	theme	factor	221:226	arg1	receptor					228:235	the type-1 insulin-like growth factor receptor	190:235	the type-1 insulin-like growth factor receptor (IGF1R)	190:243	The insulin receptor (IR) and the type-1 insulin-like growth factor receptor (IGF1R) are homologous multidomain proteins that bind insulin and IGF with differing specificity.
10531064	2	0	theme	ectodomain	340:349	arg1	structure					315:323	The crystal structure	303:323	The crystal structure	303:323	The crystal structure of the dimeric ectodomain of the human TfR, determined here to 3.2 angstroms resolution, reveals a three-domain subunit.
10531064	3	1	theme	glutamate	530:538	arg1	carboxypeptidase					540:555	membrane glutamate carboxypeptidase	521:555	membrane glutamate carboxypeptidase	521:555	One domain closely resembles carboxy- and aminopeptidases, and features of membrane glutamate carboxypeptidase can be deduced from the TfR structure.
10531064	3	2	theme	carboxypeptidase	540:555	arg1	features					509:516	features	509:516	features of membrane glutamate carboxypeptidase	509:555	One domain closely resembles carboxy- and aminopeptidases, and features of membrane glutamate carboxypeptidase can be deduced from the TfR structure.
10531064	1	3	dep	undergoes	98:106	arg1	importing					194:202	importing	194:202	importing iron-loaded transferrin (Tf)	194:231	The transferrin receptor (TfR) undergoes multiple rounds of clathrin-mediated endocytosis and reemergence at the cell surface, importing iron-loaded transferrin (Tf) and recycling apotransferrin after discharge of iron in the endosome.
10531064	1	3	dep	undergoes	98:106	arg1	recycling					237:245	recycling	237:245	recycling apotransferrin after discharge of iron in the endosome	237:300	The transferrin receptor (TfR) undergoes multiple rounds of clathrin-mediated endocytosis and reemergence at the cell surface, importing iron-loaded transferrin (Tf) and recycling apotransferrin after discharge of iron in the endosome.
10531064	1	4	theme	transferrin	71:81	arg1	TfR					93:95	TfR	93:95	TfR	93:95	The transferrin receptor (TfR) undergoes multiple rounds of clathrin-mediated endocytosis and reemergence at the cell surface, importing iron-loaded transferrin (Tf) and recycling apotransferrin after discharge of iron in the endosome.
10531064	1	4	theme	transferrin	71:81	arg1	receptor					83:90	The transferrin receptor	67:90	The transferrin receptor (TfR)	67:96	The transferrin receptor (TfR) undergoes multiple rounds of clathrin-mediated endocytosis and reemergence at the cell surface, importing iron-loaded transferrin (Tf) and recycling apotransferrin after discharge of iron in the endosome.
10531064	2	5	theme	three-domain	424:435	arg1	subunit					437:443	a three-domain subunit	422:443	a three-domain subunit	422:443	The crystal structure of the dimeric ectodomain of the human TfR, determined here to 3.2 angstroms resolution, reveals a three-domain subunit.
10531064	2	6	theme	crystal	307:313	arg1	structure					315:323	The crystal structure	303:323	The crystal structure	303:323	The crystal structure of the dimeric ectodomain of the human TfR, determined here to 3.2 angstroms resolution, reveals a three-domain subunit.
10531064	1	7	theme	cell	180:183	arg1	surface					185:191	the cell surface	176:191	the cell surface	176:191	The transferrin receptor (TfR) undergoes multiple rounds of clathrin-mediated endocytosis and reemergence at the cell surface, importing iron-loaded transferrin (Tf) and recycling apotransferrin after discharge of iron in the endosome.
10531064	0	8	theme	Crystal	0:6	arg1	structure					8:16	Crystal structure	0:16	Crystal structure of the ectodomain of human transferrin receptor	0:64	Crystal structure of the ectodomain of human transferrin receptor.
10531064	2	9	theme	TfR	364:366	arg1	TfR					364:366	the human TfR	354:366	the human TfR	354:366	The crystal structure of the dimeric ectodomain of the human TfR, determined here to 3.2 angstroms resolution, reveals a three-domain subunit.
10531064	2	9	theme	TfR	364:366	arg1	ectodomain					340:349	the dimeric ectodomain	328:349	the dimeric ectodomain of the human TfR	328:366	The crystal structure of the dimeric ectodomain of the human TfR, determined here to 3.2 angstroms resolution, reveals a three-domain subunit.
10531064	1	10	theme	iron	281:284	arg1	discharge					268:276	discharge	268:276	discharge of iron in the endosome	268:300	The transferrin receptor (TfR) undergoes multiple rounds of clathrin-mediated endocytosis and reemergence at the cell surface, importing iron-loaded transferrin (Tf) and recycling apotransferrin after discharge of iron in the endosome.
10531064	4	11	theme	Tf	620:621	arg1	binding					623:629	Tf binding	620:629	Tf binding to the receptor	620:645	A model is proposed for Tf binding to the receptor.
10531064	1	12	from	discharge	268:276	arg1	endosome					293:300	the endosome	289:300	the endosome	289:300	The transferrin receptor (TfR) undergoes multiple rounds of clathrin-mediated endocytosis and reemergence at the cell surface, importing iron-loaded transferrin (Tf) and recycling apotransferrin after discharge of iron in the endosome.
10531064	1	13	theme	reemergence	161:171	arg1	rounds					117:122	multiple rounds	108:122	multiple rounds of clathrin-mediated endocytosis and reemergence	108:171	The transferrin receptor (TfR) undergoes multiple rounds of clathrin-mediated endocytosis and reemergence at the cell surface, importing iron-loaded transferrin (Tf) and recycling apotransferrin after discharge of iron in the endosome.
10531064	2	14	theme	angstroms	392:400	arg1	resolution					402:411	3.2 angstroms resolution	388:411	3.2 angstroms resolution	388:411	The crystal structure of the dimeric ectodomain of the human TfR, determined here to 3.2 angstroms resolution, reveals a three-domain subunit.
10531064	1	15	theme	iron-loaded	204:214	arg1	Tf					229:230	Tf	229:230	Tf	229:230	The transferrin receptor (TfR) undergoes multiple rounds of clathrin-mediated endocytosis and reemergence at the cell surface, importing iron-loaded transferrin (Tf) and recycling apotransferrin after discharge of iron in the endosome.
10531064	1	15	theme	iron-loaded	204:214	arg1	transferrin					216:226	iron-loaded transferrin	204:226	iron-loaded transferrin (Tf)	204:231	The transferrin receptor (TfR) undergoes multiple rounds of clathrin-mediated endocytosis and reemergence at the cell surface, importing iron-loaded transferrin (Tf) and recycling apotransferrin after discharge of iron in the endosome.
10531064	0	16	theme	ectodomain	25:34	arg1	structure					8:16	Crystal structure	0:16	Crystal structure of the ectodomain of human transferrin receptor	0:64	Crystal structure of the ectodomain of human transferrin receptor.
10531064	0	17	theme	transferrin	45:55	arg1	receptor					57:64	human transferrin receptor	39:64	human transferrin receptor	39:64	Crystal structure of the ectodomain of human transferrin receptor.
10531064	2	18	theme	dimeric	332:338	arg1	TfR					364:366	the human TfR	354:366	the human TfR	354:366	The crystal structure of the dimeric ectodomain of the human TfR, determined here to 3.2 angstroms resolution, reveals a three-domain subunit.
10531064	2	18	theme	dimeric	332:338	arg1	ectodomain					340:349	the dimeric ectodomain	328:349	the dimeric ectodomain of the human TfR	328:366	The crystal structure of the dimeric ectodomain of the human TfR, determined here to 3.2 angstroms resolution, reveals a three-domain subunit.
10531064	0	19	theme	human	39:43	arg1	receptor					57:64	human transferrin receptor	39:64	human transferrin receptor	39:64	Crystal structure of the ectodomain of human transferrin receptor.
10531064	3	20	theme	TfR	581:583	arg1	structure					585:593	the TfR structure	577:593	the TfR structure	577:593	One domain closely resembles carboxy- and aminopeptidases, and features of membrane glutamate carboxypeptidase can be deduced from the TfR structure.
10531064	1	21	theme	multiple	108:115	arg1	rounds					117:122	multiple rounds	108:122	multiple rounds of clathrin-mediated endocytosis and reemergence	108:171	The transferrin receptor (TfR) undergoes multiple rounds of clathrin-mediated endocytosis and reemergence at the cell surface, importing iron-loaded transferrin (Tf) and recycling apotransferrin after discharge of iron in the endosome.
10531064	1	22	theme	clathrin-mediated	127:143	arg1	endocytosis					145:155	clathrin-mediated endocytosis	127:155	clathrin-mediated endocytosis	127:155	The transferrin receptor (TfR) undergoes multiple rounds of clathrin-mediated endocytosis and reemergence at the cell surface, importing iron-loaded transferrin (Tf) and recycling apotransferrin after discharge of iron in the endosome.
10531064	3	23	theme	membrane	521:528	arg1	carboxypeptidase					540:555	membrane glutamate carboxypeptidase	521:555	membrane glutamate carboxypeptidase	521:555	One domain closely resembles carboxy- and aminopeptidases, and features of membrane glutamate carboxypeptidase can be deduced from the TfR structure.
10531064	2	24	theme	human	358:362	arg1	TfR					364:366	the human TfR	354:366	the human TfR	354:366	The crystal structure of the dimeric ectodomain of the human TfR, determined here to 3.2 angstroms resolution, reveals a three-domain subunit.
10531064	0	25	theme	receptor	57:64	arg1	receptor					57:64	human transferrin receptor	39:64	human transferrin receptor	39:64	Crystal structure of the ectodomain of human transferrin receptor.
10531064	0	25	theme	receptor	57:64	arg1	ectodomain					25:34	the ectodomain	21:34	the ectodomain of human transferrin receptor	21:64	Crystal structure of the ectodomain of human transferrin receptor.
10531064	1	26	theme	endocytosis	145:155	arg1	rounds					117:122	multiple rounds	108:122	multiple rounds of clathrin-mediated endocytosis and reemergence	108:171	The transferrin receptor (TfR) undergoes multiple rounds of clathrin-mediated endocytosis and reemergence at the cell surface, importing iron-loaded transferrin (Tf) and recycling apotransferrin after discharge of iron in the endosome.
18036614	4	0	theme	side-chain	809:818	arg1	interactions					820:831	side-chain interactions	809:831	side-chain interactions with its acarvosine unit	809:856	Structural analysis of the NtMGAM-acarbose complex reveals that acarbose is bound to the NtMGAM active site primarily through side-chain interactions with its acarvosine unit, and almost no interactions are made with its glycone rings.
18036614	2	1	theme	homologous	372:381	arg1	subunits					422:429	two homologous glycosyl hydrolase family 31 catalytic subunits	368:429	two homologous glycosyl hydrolase family 31 catalytic subunits: an N-terminal subunit (NtMGAM) found near the membrane-bound end and a C-terminal luminal subunit (CtMGAM)	368:537	MGAM is anchored to the small-intestinal brush-border epithelial cells and contains two homologous glycosyl hydrolase family 31 catalytic subunits: an N-terminal subunit (NtMGAM) found near the membrane-bound end and a C-terminal luminal subunit (CtMGAM).
18036614	2	1	theme	homologous	372:381	arg1	subunit					522:528	a C-terminal luminal subunit	501:528	a C-terminal luminal subunit (CtMGAM)	501:537	MGAM is anchored to the small-intestinal brush-border epithelial cells and contains two homologous glycosyl hydrolase family 31 catalytic subunits: an N-terminal subunit (NtMGAM) found near the membrane-bound end and a C-terminal luminal subunit (CtMGAM).
18036614	2	1	theme	homologous	372:381	arg1	subunit					446:452	an N-terminal subunit	432:452	an N-terminal subunit (NtMGAM) found near the membrane-bound end	432:495	MGAM is anchored to the small-intestinal brush-border epithelial cells and contains two homologous glycosyl hydrolase family 31 catalytic subunits: an N-terminal subunit (NtMGAM) found near the membrane-bound end and a C-terminal luminal subunit (CtMGAM).
18036614	7	2	from	roles	1394:1398	arg1	bioprocessing					1454:1466	the bioprocessing	1450:1466	the bioprocessing of complex starch structures into glucose	1450:1508	The results provide a structural basis for the complementary roles of these glycosyl hydrolase family 31 subunits in the bioprocessing of complex starch structures into glucose.
18036614	3	3	dep	A	639:639	arg1	to					632:633	to	632:633	to	632:633	In this study, we report the crystal structure of the human NtMGAM subunit in its apo form (to 2.0 A) and in complex with acarbose (to 1.9 A).
18036614	0	4	theme	subunit	85:91	arg1	structure					47:55	crystal structure	39:55	crystal structure of the N-terminal catalytic subunit	39:91	Human intestinal maltase-glucoamylase: crystal structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity.
18036614	0	4	theme	subunit	85:91	arg1	basis					97:101	basis	97:101	basis of inhibition and substrate specificity	97:141	Human intestinal maltase-glucoamylase: crystal structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity.
18036614	7	5	theme	subunits	1438:1445	arg1	roles					1394:1398	the complementary roles	1376:1398	the complementary roles of these glycosyl hydrolase family 31 subunits in the bioprocessing of complex starch structures into glucose	1376:1508	The results provide a structural basis for the complementary roles of these glycosyl hydrolase family 31 subunits in the bioprocessing of complex starch structures into glucose.
18036614	3	6	theme	apo	622:624	arg1	form					626:629	its apo form	618:629	its apo form (to 2.0 A)	618:640	In this study, we report the crystal structure of the human NtMGAM subunit in its apo form (to 2.0 A) and in complex with acarbose (to 1.9 A).
18036614	3	6	theme	apo	622:624	arg1	A					639:639	to 2.0 A	632:639	to 2.0 A	632:639	In this study, we report the crystal structure of the human NtMGAM subunit in its apo form (to 2.0 A) and in complex with acarbose (to 1.9 A).
18036614	3	7	with	complex	649:655	arg1	A					679:679	to 1.9 A	672:679	to 1.9 A	672:679	In this study, we report the crystal structure of the human NtMGAM subunit in its apo form (to 2.0 A) and in complex with acarbose (to 1.9 A).
18036614	3	7	with	complex	649:655	arg1	acarbose					662:669	acarbose	662:669	acarbose (to 1.9 A)	662:680	In this study, we report the crystal structure of the human NtMGAM subunit in its apo form (to 2.0 A) and in complex with acarbose (to 1.9 A).
18036614	2	8	contain	contains	359:366	arg2	subunit					446:452	an N-terminal subunit	432:452	an N-terminal subunit (NtMGAM) found near the membrane-bound end	432:495	MGAM is anchored to the small-intestinal brush-border epithelial cells and contains two homologous glycosyl hydrolase family 31 catalytic subunits: an N-terminal subunit (NtMGAM) found near the membrane-bound end and a C-terminal luminal subunit (CtMGAM).
18036614	2	8	contain	contains	359:366	arg2	subunits					422:429	two homologous glycosyl hydrolase family 31 catalytic subunits	368:429	two homologous glycosyl hydrolase family 31 catalytic subunits: an N-terminal subunit (NtMGAM) found near the membrane-bound end and a C-terminal luminal subunit (CtMGAM)	368:537	MGAM is anchored to the small-intestinal brush-border epithelial cells and contains two homologous glycosyl hydrolase family 31 catalytic subunits: an N-terminal subunit (NtMGAM) found near the membrane-bound end and a C-terminal luminal subunit (CtMGAM).
18036614	2	8	contain	contains	359:366	arg1	MGAM					284:287	MGAM	284:287	MGAM	284:287	MGAM is anchored to the small-intestinal brush-border epithelial cells and contains two homologous glycosyl hydrolase family 31 catalytic subunits: an N-terminal subunit (NtMGAM) found near the membrane-bound end and a C-terminal luminal subunit (CtMGAM).
18036614	2	8	contain	contains	359:366	arg2	subunit					522:528	a C-terminal luminal subunit	501:528	a C-terminal luminal subunit (CtMGAM)	501:537	MGAM is anchored to the small-intestinal brush-border epithelial cells and contains two homologous glycosyl hydrolase family 31 catalytic subunits: an N-terminal subunit (NtMGAM) found near the membrane-bound end and a C-terminal luminal subunit (CtMGAM).
18036614	5	9	theme	kinetic	963:969	arg1	studies					971:977	kinetic studies	963:977	kinetic studies	963:977	These observations, along with results from kinetic studies, suggest that the NtMGAM active site contains two primary sugar subsites and that NtMGAM and CtMGAM differ in their substrate specificities despite their structural relationship.
18036614	6	10	theme	Additional	1158:1167	arg1	analysis					1178:1185	Additional sequence analysis	1158:1185	Additional sequence analysis of the CtMGAM subunit	1158:1207	Additional sequence analysis of the CtMGAM subunit suggests several features that could explain the higher affinity of the CtMGAM subunit for longer maltose oligosaccharides.
18036614	1	11	theme	starch	266:271	arg1	digestion					273:281	starch digestion	266:281	starch digestion	266:281	Human maltase-glucoamylase (MGAM) is one of the two enzymes responsible for catalyzing the last glucose-releasing step in starch digestion.
18036614	7	12	theme	family	1428:1433	arg1	subunits					1438:1445	these glycosyl hydrolase family 31 subunits	1403:1445	these glycosyl hydrolase family 31 subunits	1403:1445	The results provide a structural basis for the complementary roles of these glycosyl hydrolase family 31 subunits in the bioprocessing of complex starch structures into glucose.
18036614	2	13	theme	epithelial	338:347	arg1	cells					349:353	the small-intestinal brush-border epithelial cells	304:353	the small-intestinal brush-border epithelial cells	304:353	MGAM is anchored to the small-intestinal brush-border epithelial cells and contains two homologous glycosyl hydrolase family 31 catalytic subunits: an N-terminal subunit (NtMGAM) found near the membrane-bound end and a C-terminal luminal subunit (CtMGAM).
18036614	6	14	theme	maltose	1307:1313	arg1	oligosaccharides					1315:1330	longer maltose oligosaccharides	1300:1330	longer maltose oligosaccharides	1300:1330	Additional sequence analysis of the CtMGAM subunit suggests several features that could explain the higher affinity of the CtMGAM subunit for longer maltose oligosaccharides.
18036614	5	15	theme	primary	1029:1035	arg1	subsites					1043:1050	two primary sugar subsites	1025:1050	two primary sugar subsites	1025:1050	These observations, along with results from kinetic studies, suggest that the NtMGAM active site contains two primary sugar subsites and that NtMGAM and CtMGAM differ in their substrate specificities despite their structural relationship.
18036614	4	16	theme	active	779:784	arg1	site					786:789	the NtMGAM active site	768:789	the NtMGAM active site	768:789	Structural analysis of the NtMGAM-acarbose complex reveals that acarbose is bound to the NtMGAM active site primarily through side-chain interactions with its acarvosine unit, and almost no interactions are made with its glycone rings.
18036614	2	17	theme	N-terminal	435:444	arg1	subunits					422:429	two homologous glycosyl hydrolase family 31 catalytic subunits	368:429	two homologous glycosyl hydrolase family 31 catalytic subunits: an N-terminal subunit (NtMGAM) found near the membrane-bound end and a C-terminal luminal subunit (CtMGAM)	368:537	MGAM is anchored to the small-intestinal brush-border epithelial cells and contains two homologous glycosyl hydrolase family 31 catalytic subunits: an N-terminal subunit (NtMGAM) found near the membrane-bound end and a C-terminal luminal subunit (CtMGAM).
18036614	2	17	theme	N-terminal	435:444	arg1	NtMGAM					455:460	NtMGAM	455:460	NtMGAM	455:460	MGAM is anchored to the small-intestinal brush-border epithelial cells and contains two homologous glycosyl hydrolase family 31 catalytic subunits: an N-terminal subunit (NtMGAM) found near the membrane-bound end and a C-terminal luminal subunit (CtMGAM).
18036614	2	17	theme	N-terminal	435:444	arg1	subunit					446:452	an N-terminal subunit	432:452	an N-terminal subunit (NtMGAM) found near the membrane-bound end	432:495	MGAM is anchored to the small-intestinal brush-border epithelial cells and contains two homologous glycosyl hydrolase family 31 catalytic subunits: an N-terminal subunit (NtMGAM) found near the membrane-bound end and a C-terminal luminal subunit (CtMGAM).
18036614	4	18	theme	NtMGAM-acarbose	710:724	arg1	complex					726:732	the NtMGAM-acarbose complex	706:732	the NtMGAM-acarbose complex	706:732	Structural analysis of the NtMGAM-acarbose complex reveals that acarbose is bound to the NtMGAM active site primarily through side-chain interactions with its acarvosine unit, and almost no interactions are made with its glycone rings.
18036614	4	19	theme	complex	726:732	arg1	analysis					694:701	Structural analysis	683:701	Structural analysis of the NtMGAM-acarbose complex	683:732	Structural analysis of the NtMGAM-acarbose complex reveals that acarbose is bound to the NtMGAM active site primarily through side-chain interactions with its acarvosine unit, and almost no interactions are made with its glycone rings.
18036614	0	20	theme	inhibition	106:115	arg1	structure					47:55	crystal structure	39:55	crystal structure of the N-terminal catalytic subunit	39:91	Human intestinal maltase-glucoamylase: crystal structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity.
18036614	0	20	theme	inhibition	106:115	arg1	basis					97:101	basis	97:101	basis of inhibition and substrate specificity	97:141	Human intestinal maltase-glucoamylase: crystal structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity.
18036614	5	21	theme	sugar	1037:1041	arg1	subsites					1043:1050	two primary sugar subsites	1025:1050	two primary sugar subsites	1025:1050	These observations, along with results from kinetic studies, suggest that the NtMGAM active site contains two primary sugar subsites and that NtMGAM and CtMGAM differ in their substrate specificities despite their structural relationship.
18036614	4	22	theme	NtMGAM	772:777	arg1	site					786:789	the NtMGAM active site	768:789	the NtMGAM active site	768:789	Structural analysis of the NtMGAM-acarbose complex reveals that acarbose is bound to the NtMGAM active site primarily through side-chain interactions with its acarvosine unit, and almost no interactions are made with its glycone rings.
18036614	5	23	contain	contains	1016:1023	arg2	subsites					1043:1050	two primary sugar subsites	1025:1050	two primary sugar subsites	1025:1050	These observations, along with results from kinetic studies, suggest that the NtMGAM active site contains two primary sugar subsites and that NtMGAM and CtMGAM differ in their substrate specificities despite their structural relationship.
18036614	5	23	contain	contains	1016:1023	arg1	site					1011:1014	the NtMGAM active site	993:1014	the NtMGAM active site	993:1014	These observations, along with results from kinetic studies, suggest that the NtMGAM active site contains two primary sugar subsites and that NtMGAM and CtMGAM differ in their substrate specificities despite their structural relationship.
18036614	2	24	theme	catalytic	412:420	arg1	subunits					422:429	two homologous glycosyl hydrolase family 31 catalytic subunits	368:429	two homologous glycosyl hydrolase family 31 catalytic subunits: an N-terminal subunit (NtMGAM) found near the membrane-bound end and a C-terminal luminal subunit (CtMGAM)	368:537	MGAM is anchored to the small-intestinal brush-border epithelial cells and contains two homologous glycosyl hydrolase family 31 catalytic subunits: an N-terminal subunit (NtMGAM) found near the membrane-bound end and a C-terminal luminal subunit (CtMGAM).
18036614	2	24	theme	catalytic	412:420	arg1	subunit					522:528	a C-terminal luminal subunit	501:528	a C-terminal luminal subunit (CtMGAM)	501:537	MGAM is anchored to the small-intestinal brush-border epithelial cells and contains two homologous glycosyl hydrolase family 31 catalytic subunits: an N-terminal subunit (NtMGAM) found near the membrane-bound end and a C-terminal luminal subunit (CtMGAM).
18036614	2	24	theme	catalytic	412:420	arg1	subunit					446:452	an N-terminal subunit	432:452	an N-terminal subunit (NtMGAM) found near the membrane-bound end	432:495	MGAM is anchored to the small-intestinal brush-border epithelial cells and contains two homologous glycosyl hydrolase family 31 catalytic subunits: an N-terminal subunit (NtMGAM) found near the membrane-bound end and a C-terminal luminal subunit (CtMGAM).
18036614	0	25	theme	intestinal	6:15	arg1	maltase-glucoamylase					17:36	Human intestinal maltase-glucoamylase	0:36	Human intestinal maltase-glucoamylase: crystal structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity.	0:142	Human intestinal maltase-glucoamylase: crystal structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity.
18036614	7	26	theme	hydrolase	1418:1426	arg1	family					1428:1433	glycosyl hydrolase family 31	1409:1436	these glycosyl hydrolase family 31 subunits	1403:1445	The results provide a structural basis for the complementary roles of these glycosyl hydrolase family 31 subunits in the bioprocessing of complex starch structures into glucose.
18036614	6	27	theme	subunit	1201:1207	arg1	analysis					1178:1185	Additional sequence analysis	1158:1185	Additional sequence analysis of the CtMGAM subunit	1158:1207	Additional sequence analysis of the CtMGAM subunit suggests several features that could explain the higher affinity of the CtMGAM subunit for longer maltose oligosaccharides.
18036614	2	28	theme	luminal	514:520	arg1	subunits					422:429	two homologous glycosyl hydrolase family 31 catalytic subunits	368:429	two homologous glycosyl hydrolase family 31 catalytic subunits: an N-terminal subunit (NtMGAM) found near the membrane-bound end and a C-terminal luminal subunit (CtMGAM)	368:537	MGAM is anchored to the small-intestinal brush-border epithelial cells and contains two homologous glycosyl hydrolase family 31 catalytic subunits: an N-terminal subunit (NtMGAM) found near the membrane-bound end and a C-terminal luminal subunit (CtMGAM).
18036614	2	28	theme	luminal	514:520	arg1	CtMGAM					531:536	CtMGAM	531:536	CtMGAM	531:536	MGAM is anchored to the small-intestinal brush-border epithelial cells and contains two homologous glycosyl hydrolase family 31 catalytic subunits: an N-terminal subunit (NtMGAM) found near the membrane-bound end and a C-terminal luminal subunit (CtMGAM).
18036614	2	28	theme	luminal	514:520	arg1	subunit					522:528	a C-terminal luminal subunit	501:528	a C-terminal luminal subunit (CtMGAM)	501:537	MGAM is anchored to the small-intestinal brush-border epithelial cells and contains two homologous glycosyl hydrolase family 31 catalytic subunits: an N-terminal subunit (NtMGAM) found near the membrane-bound end and a C-terminal luminal subunit (CtMGAM).
18036614	2	29	theme	brush-border	325:336	arg1	cells					349:353	the small-intestinal brush-border epithelial cells	304:353	the small-intestinal brush-border epithelial cells	304:353	MGAM is anchored to the small-intestinal brush-border epithelial cells and contains two homologous glycosyl hydrolase family 31 catalytic subunits: an N-terminal subunit (NtMGAM) found near the membrane-bound end and a C-terminal luminal subunit (CtMGAM).
18036614	0	30	theme	Human	0:4	arg1	maltase-glucoamylase					17:36	Human intestinal maltase-glucoamylase	0:36	Human intestinal maltase-glucoamylase: crystal structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity.	0:142	Human intestinal maltase-glucoamylase: crystal structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity.
18036614	5	31	theme	substrate	1095:1103	arg1	specificities					1105:1117	their substrate specificities	1089:1117	their substrate specificities	1089:1117	These observations, along with results from kinetic studies, suggest that the NtMGAM active site contains two primary sugar subsites and that NtMGAM and CtMGAM differ in their substrate specificities despite their structural relationship.
18036614	6	32	theme	CtMGAM	1194:1199	arg1	subunit					1201:1207	the CtMGAM subunit	1190:1207	the CtMGAM subunit	1190:1207	Additional sequence analysis of the CtMGAM subunit suggests several features that could explain the higher affinity of the CtMGAM subunit for longer maltose oligosaccharides.
18036614	2	33	theme	small-intestinal	308:323	arg1	cells					349:353	the small-intestinal brush-border epithelial cells	304:353	the small-intestinal brush-border epithelial cells	304:353	MGAM is anchored to the small-intestinal brush-border epithelial cells and contains two homologous glycosyl hydrolase family 31 catalytic subunits: an N-terminal subunit (NtMGAM) found near the membrane-bound end and a C-terminal luminal subunit (CtMGAM).
18036614	6	34	theme	subunit	1288:1294	arg1	affinity					1265:1272	the higher affinity	1254:1272	the higher affinity of the CtMGAM subunit for longer maltose oligosaccharides	1254:1330	Additional sequence analysis of the CtMGAM subunit suggests several features that could explain the higher affinity of the CtMGAM subunit for longer maltose oligosaccharides.
18036614	2	35	theme	family	402:407	arg1	subunits					422:429	two homologous glycosyl hydrolase family 31 catalytic subunits	368:429	two homologous glycosyl hydrolase family 31 catalytic subunits: an N-terminal subunit (NtMGAM) found near the membrane-bound end and a C-terminal luminal subunit (CtMGAM)	368:537	MGAM is anchored to the small-intestinal brush-border epithelial cells and contains two homologous glycosyl hydrolase family 31 catalytic subunits: an N-terminal subunit (NtMGAM) found near the membrane-bound end and a C-terminal luminal subunit (CtMGAM).
18036614	2	35	theme	family	402:407	arg1	subunit					522:528	a C-terminal luminal subunit	501:528	a C-terminal luminal subunit (CtMGAM)	501:537	MGAM is anchored to the small-intestinal brush-border epithelial cells and contains two homologous glycosyl hydrolase family 31 catalytic subunits: an N-terminal subunit (NtMGAM) found near the membrane-bound end and a C-terminal luminal subunit (CtMGAM).
18036614	2	35	theme	family	402:407	arg1	subunit					446:452	an N-terminal subunit	432:452	an N-terminal subunit (NtMGAM) found near the membrane-bound end	432:495	MGAM is anchored to the small-intestinal brush-border epithelial cells and contains two homologous glycosyl hydrolase family 31 catalytic subunits: an N-terminal subunit (NtMGAM) found near the membrane-bound end and a C-terminal luminal subunit (CtMGAM).
18036614	3	36	theme	human	594:598	arg1	subunit					607:613	the human NtMGAM subunit	590:613	the human NtMGAM subunit	590:613	In this study, we report the crystal structure of the human NtMGAM subunit in its apo form (to 2.0 A) and in complex with acarbose (to 1.9 A).
18036614	0	37	theme	specificity	131:141	arg1	structure					47:55	crystal structure	39:55	crystal structure of the N-terminal catalytic subunit	39:91	Human intestinal maltase-glucoamylase: crystal structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity.
18036614	0	37	theme	specificity	131:141	arg1	basis					97:101	basis	97:101	basis of inhibition and substrate specificity	97:141	Human intestinal maltase-glucoamylase: crystal structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity.
18036614	6	38	theme	sequence	1169:1176	arg1	analysis					1178:1185	Additional sequence analysis	1158:1185	Additional sequence analysis of the CtMGAM subunit	1158:1207	Additional sequence analysis of the CtMGAM subunit suggests several features that could explain the higher affinity of the CtMGAM subunit for longer maltose oligosaccharides.
18036614	4	39	theme	Structural	683:692	arg1	analysis					694:701	Structural analysis	683:701	Structural analysis of the NtMGAM-acarbose complex	683:732	Structural analysis of the NtMGAM-acarbose complex reveals that acarbose is bound to the NtMGAM active site primarily through side-chain interactions with its acarvosine unit, and almost no interactions are made with its glycone rings.
18036614	3	40	from	structure	577:585	arg1	form					626:629	its apo form	618:629	its apo form (to 2.0 A)	618:640	In this study, we report the crystal structure of the human NtMGAM subunit in its apo form (to 2.0 A) and in complex with acarbose (to 1.9 A).
18036614	3	40	from	structure	577:585	arg1	complex					649:655	complex	649:655	complex with acarbose (to 1.9 A)	649:680	In this study, we report the crystal structure of the human NtMGAM subunit in its apo form (to 2.0 A) and in complex with acarbose (to 1.9 A).
18036614	3	40	from	structure	577:585	arg1	A					639:639	to 2.0 A	632:639	to 2.0 A	632:639	In this study, we report the crystal structure of the human NtMGAM subunit in its apo form (to 2.0 A) and in complex with acarbose (to 1.9 A).
18036614	0	41	theme	substrate	121:129	arg1	specificity					131:141	substrate specificity	121:141	substrate specificity	121:141	Human intestinal maltase-glucoamylase: crystal structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity.
18036614	5	42	theme	NtMGAM	997:1002	arg1	site					1011:1014	the NtMGAM active site	993:1014	the NtMGAM active site	993:1014	These observations, along with results from kinetic studies, suggest that the NtMGAM active site contains two primary sugar subsites and that NtMGAM and CtMGAM differ in their substrate specificities despite their structural relationship.
18036614	1	43	theme	enzymes	196:202	arg1	enzymes					196:202	the two enzymes	188:202	the two enzymes responsible for catalyzing the last glucose-releasing step in starch digestion	188:281	Human maltase-glucoamylase (MGAM) is one of the two enzymes responsible for catalyzing the last glucose-releasing step in starch digestion.
18036614	1	43	theme	enzymes	196:202	arg1	one					181:183	one	181:183	one	181:183	Human maltase-glucoamylase (MGAM) is one of the two enzymes responsible for catalyzing the last glucose-releasing step in starch digestion.
18036614	1	44	from	step	258:261	arg1	digestion					273:281	starch digestion	266:281	starch digestion	266:281	Human maltase-glucoamylase (MGAM) is one of the two enzymes responsible for catalyzing the last glucose-releasing step in starch digestion.
18036614	5	45	theme	active	1004:1009	arg1	site					1011:1014	the NtMGAM active site	993:1014	the NtMGAM active site	993:1014	These observations, along with results from kinetic studies, suggest that the NtMGAM active site contains two primary sugar subsites and that NtMGAM and CtMGAM differ in their substrate specificities despite their structural relationship.
18036614	7	46	theme	structural	1355:1364	arg1	basis					1366:1370	a structural basis	1353:1370	a structural basis for the complementary roles of these glycosyl hydrolase family 31 subunits in the bioprocessing of complex starch structures into glucose	1353:1508	The results provide a structural basis for the complementary roles of these glycosyl hydrolase family 31 subunits in the bioprocessing of complex starch structures into glucose.
18036614	7	47	theme	structures	1486:1495	arg1	bioprocessing					1454:1466	the bioprocessing	1450:1466	the bioprocessing of complex starch structures into glucose	1450:1508	The results provide a structural basis for the complementary roles of these glycosyl hydrolase family 31 subunits in the bioprocessing of complex starch structures into glucose.
18036614	1	48	theme	responsible	204:214	arg1	enzymes					196:202	the two enzymes	188:202	the two enzymes responsible for catalyzing the last glucose-releasing step in starch digestion	188:281	Human maltase-glucoamylase (MGAM) is one of the two enzymes responsible for catalyzing the last glucose-releasing step in starch digestion.
18036614	0	49	theme	crystal	39:45	arg1	structure					47:55	crystal structure	39:55	crystal structure of the N-terminal catalytic subunit	39:91	Human intestinal maltase-glucoamylase: crystal structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity.
18036614	2	50	theme	membrane-bound	478:491	arg1	end					493:495	the membrane-bound end	474:495	the membrane-bound end	474:495	MGAM is anchored to the small-intestinal brush-border epithelial cells and contains two homologous glycosyl hydrolase family 31 catalytic subunits: an N-terminal subunit (NtMGAM) found near the membrane-bound end and a C-terminal luminal subunit (CtMGAM).
18036614	6	51	theme	CtMGAM	1281:1286	arg1	subunit					1288:1294	the CtMGAM subunit	1277:1294	the CtMGAM subunit	1277:1294	Additional sequence analysis of the CtMGAM subunit suggests several features that could explain the higher affinity of the CtMGAM subunit for longer maltose oligosaccharides.
18036614	6	52	theme	longer	1300:1305	arg1	oligosaccharides					1315:1330	longer maltose oligosaccharides	1300:1330	longer maltose oligosaccharides	1300:1330	Additional sequence analysis of the CtMGAM subunit suggests several features that could explain the higher affinity of the CtMGAM subunit for longer maltose oligosaccharides.
18036614	4	53	theme	acarvosine	842:851	arg1	unit					853:856	its acarvosine unit	838:856	its acarvosine unit	838:856	Structural analysis of the NtMGAM-acarbose complex reveals that acarbose is bound to the NtMGAM active site primarily through side-chain interactions with its acarvosine unit, and almost no interactions are made with its glycone rings.
18036614	2	54	theme	C-terminal	503:512	arg1	subunits					422:429	two homologous glycosyl hydrolase family 31 catalytic subunits	368:429	two homologous glycosyl hydrolase family 31 catalytic subunits: an N-terminal subunit (NtMGAM) found near the membrane-bound end and a C-terminal luminal subunit (CtMGAM)	368:537	MGAM is anchored to the small-intestinal brush-border epithelial cells and contains two homologous glycosyl hydrolase family 31 catalytic subunits: an N-terminal subunit (NtMGAM) found near the membrane-bound end and a C-terminal luminal subunit (CtMGAM).
18036614	2	54	theme	C-terminal	503:512	arg1	CtMGAM					531:536	CtMGAM	531:536	CtMGAM	531:536	MGAM is anchored to the small-intestinal brush-border epithelial cells and contains two homologous glycosyl hydrolase family 31 catalytic subunits: an N-terminal subunit (NtMGAM) found near the membrane-bound end and a C-terminal luminal subunit (CtMGAM).
18036614	2	54	theme	C-terminal	503:512	arg1	subunit					522:528	a C-terminal luminal subunit	501:528	a C-terminal luminal subunit (CtMGAM)	501:537	MGAM is anchored to the small-intestinal brush-border epithelial cells and contains two homologous glycosyl hydrolase family 31 catalytic subunits: an N-terminal subunit (NtMGAM) found near the membrane-bound end and a C-terminal luminal subunit (CtMGAM).
18036614	3	55	theme	crystal	569:575	arg1	structure					577:585	the crystal structure	565:585	the crystal structure of the human NtMGAM subunit in its apo form (to 2.0 A) and in complex with acarbose (to 1.9 A)	565:680	In this study, we report the crystal structure of the human NtMGAM subunit in its apo form (to 2.0 A) and in complex with acarbose (to 1.9 A).
18036614	7	56	theme	glycosyl	1409:1416	arg1	family					1428:1433	glycosyl hydrolase family 31	1409:1436	these glycosyl hydrolase family 31 subunits	1403:1445	The results provide a structural basis for the complementary roles of these glycosyl hydrolase family 31 subunits in the bioprocessing of complex starch structures into glucose.
18036614	4	57	theme	no	870:871	arg1	interactions					873:884	almost no interactions	863:884	almost no interactions	863:884	Structural analysis of the NtMGAM-acarbose complex reveals that acarbose is bound to the NtMGAM active site primarily through side-chain interactions with its acarvosine unit, and almost no interactions are made with its glycone rings.
18036614	7	58	theme	starch	1479:1484	arg1	structures					1486:1495	complex starch structures	1471:1495	complex starch structures	1471:1495	The results provide a structural basis for the complementary roles of these glycosyl hydrolase family 31 subunits in the bioprocessing of complex starch structures into glucose.
18036614	4	59	theme	glycone	904:910	arg1	rings					912:916	its glycone rings	900:916	its glycone rings	900:916	Structural analysis of the NtMGAM-acarbose complex reveals that acarbose is bound to the NtMGAM active site primarily through side-chain interactions with its acarvosine unit, and almost no interactions are made with its glycone rings.
18036614	6	60	theme	higher	1258:1263	arg1	affinity					1265:1272	the higher affinity	1254:1272	the higher affinity of the CtMGAM subunit for longer maltose oligosaccharides	1254:1330	Additional sequence analysis of the CtMGAM subunit suggests several features that could explain the higher affinity of the CtMGAM subunit for longer maltose oligosaccharides.
18036614	5	61	from	studies	971:977	arg1	results					950:956	results	950:956	results from kinetic studies	950:977	These observations, along with results from kinetic studies, suggest that the NtMGAM active site contains two primary sugar subsites and that NtMGAM and CtMGAM differ in their substrate specificities despite their structural relationship.
18036614	3	62	theme	subunit	607:613	arg1	structure					577:585	the crystal structure	565:585	the crystal structure of the human NtMGAM subunit in its apo form (to 2.0 A) and in complex with acarbose (to 1.9 A)	565:680	In this study, we report the crystal structure of the human NtMGAM subunit in its apo form (to 2.0 A) and in complex with acarbose (to 1.9 A).
18036614	7	63	theme	complementary	1380:1392	arg1	roles					1394:1398	the complementary roles	1376:1398	the complementary roles of these glycosyl hydrolase family 31 subunits in the bioprocessing of complex starch structures into glucose	1376:1508	The results provide a structural basis for the complementary roles of these glycosyl hydrolase family 31 subunits in the bioprocessing of complex starch structures into glucose.
18036614	4	64	with	interactions	820:831	arg1	unit					853:856	its acarvosine unit	838:856	its acarvosine unit	838:856	Structural analysis of the NtMGAM-acarbose complex reveals that acarbose is bound to the NtMGAM active site primarily through side-chain interactions with its acarvosine unit, and almost no interactions are made with its glycone rings.
18036614	6	65	theme	several	1218:1224	arg1	features					1226:1233	several features	1218:1233	several features that could explain the higher affinity of the CtMGAM subunit for longer maltose oligosaccharides	1218:1330	Additional sequence analysis of the CtMGAM subunit suggests several features that could explain the higher affinity of the CtMGAM subunit for longer maltose oligosaccharides.
18036614	0	66	dep	maltase-glucoamylase	17:36	arg1	structure					47:55	crystal structure	39:55	crystal structure of the N-terminal catalytic subunit	39:91	Human intestinal maltase-glucoamylase: crystal structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity.
18036614	0	66	dep	maltase-glucoamylase	17:36	arg1	basis					97:101	basis	97:101	basis of inhibition and substrate specificity	97:141	Human intestinal maltase-glucoamylase: crystal structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity.
18036614	5	67	theme	structural	1133:1142	arg1	relationship					1144:1155	their structural relationship	1127:1155	their structural relationship	1127:1155	These observations, along with results from kinetic studies, suggest that the NtMGAM active site contains two primary sugar subsites and that NtMGAM and CtMGAM differ in their substrate specificities despite their structural relationship.
18036614	1	68	theme	Human	144:148	arg1	MGAM					172:175	MGAM	172:175	MGAM	172:175	Human maltase-glucoamylase (MGAM) is one of the two enzymes responsible for catalyzing the last glucose-releasing step in starch digestion.
18036614	1	68	theme	Human	144:148	arg1	maltase-glucoamylase					150:169	Human maltase-glucoamylase	144:169	Human maltase-glucoamylase (MGAM)	144:176	Human maltase-glucoamylase (MGAM) is one of the two enzymes responsible for catalyzing the last glucose-releasing step in starch digestion.
18036614	0	69	theme	catalytic	75:83	arg1	subunit					85:91	the N-terminal catalytic subunit	60:91	the N-terminal catalytic subunit	60:91	Human intestinal maltase-glucoamylase: crystal structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity.
18036614	7	70	theme	complex	1471:1477	arg1	structures					1486:1495	complex starch structures	1471:1495	complex starch structures	1471:1495	The results provide a structural basis for the complementary roles of these glycosyl hydrolase family 31 subunits in the bioprocessing of complex starch structures into glucose.
18036614	2	71	dep	subunits	422:429	arg1	subunits					422:429	two homologous glycosyl hydrolase family 31 catalytic subunits	368:429	two homologous glycosyl hydrolase family 31 catalytic subunits: an N-terminal subunit (NtMGAM) found near the membrane-bound end and a C-terminal luminal subunit (CtMGAM)	368:537	MGAM is anchored to the small-intestinal brush-border epithelial cells and contains two homologous glycosyl hydrolase family 31 catalytic subunits: an N-terminal subunit (NtMGAM) found near the membrane-bound end and a C-terminal luminal subunit (CtMGAM).
18036614	2	71	dep	subunits	422:429	arg1	CtMGAM					531:536	CtMGAM	531:536	CtMGAM	531:536	MGAM is anchored to the small-intestinal brush-border epithelial cells and contains two homologous glycosyl hydrolase family 31 catalytic subunits: an N-terminal subunit (NtMGAM) found near the membrane-bound end and a C-terminal luminal subunit (CtMGAM).
18036614	2	71	dep	subunits	422:429	arg1	NtMGAM					455:460	NtMGAM	455:460	NtMGAM	455:460	MGAM is anchored to the small-intestinal brush-border epithelial cells and contains two homologous glycosyl hydrolase family 31 catalytic subunits: an N-terminal subunit (NtMGAM) found near the membrane-bound end and a C-terminal luminal subunit (CtMGAM).
18036614	2	71	dep	subunits	422:429	arg1	subunit					522:528	a C-terminal luminal subunit	501:528	a C-terminal luminal subunit (CtMGAM)	501:537	MGAM is anchored to the small-intestinal brush-border epithelial cells and contains two homologous glycosyl hydrolase family 31 catalytic subunits: an N-terminal subunit (NtMGAM) found near the membrane-bound end and a C-terminal luminal subunit (CtMGAM).
18036614	2	71	dep	subunits	422:429	arg1	subunit					446:452	an N-terminal subunit	432:452	an N-terminal subunit (NtMGAM) found near the membrane-bound end	432:495	MGAM is anchored to the small-intestinal brush-border epithelial cells and contains two homologous glycosyl hydrolase family 31 catalytic subunits: an N-terminal subunit (NtMGAM) found near the membrane-bound end and a C-terminal luminal subunit (CtMGAM).
18036614	2	72	theme	hydrolase	392:400	arg1	family					402:407	glycosyl hydrolase family 31	383:410	two homologous glycosyl hydrolase family 31 catalytic subunits: an N-terminal subunit (NtMGAM) found near the membrane-bound end and a C-terminal luminal subunit (CtMGAM)	368:537	MGAM is anchored to the small-intestinal brush-border epithelial cells and contains two homologous glycosyl hydrolase family 31 catalytic subunits: an N-terminal subunit (NtMGAM) found near the membrane-bound end and a C-terminal luminal subunit (CtMGAM).
18036614	1	73	theme	last	235:238	arg1	step					258:261	the last glucose-releasing step	231:261	the last glucose-releasing step in starch digestion	231:281	Human maltase-glucoamylase (MGAM) is one of the two enzymes responsible for catalyzing the last glucose-releasing step in starch digestion.
18036614	0	74	theme	N-terminal	64:73	arg1	subunit					85:91	the N-terminal catalytic subunit	60:91	the N-terminal catalytic subunit	60:91	Human intestinal maltase-glucoamylase: crystal structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity.
18036614	3	75	dep	A	679:679	arg1	to					672:673	to	672:673	to	672:673	In this study, we report the crystal structure of the human NtMGAM subunit in its apo form (to 2.0 A) and in complex with acarbose (to 1.9 A).
18036614	3	76	theme	NtMGAM	600:605	arg1	subunit					607:613	the human NtMGAM subunit	590:613	the human NtMGAM subunit	590:613	In this study, we report the crystal structure of the human NtMGAM subunit in its apo form (to 2.0 A) and in complex with acarbose (to 1.9 A).
18036614	2	77	theme	glycosyl	383:390	arg1	family					402:407	glycosyl hydrolase family 31	383:410	two homologous glycosyl hydrolase family 31 catalytic subunits: an N-terminal subunit (NtMGAM) found near the membrane-bound end and a C-terminal luminal subunit (CtMGAM)	368:537	MGAM is anchored to the small-intestinal brush-border epithelial cells and contains two homologous glycosyl hydrolase family 31 catalytic subunits: an N-terminal subunit (NtMGAM) found near the membrane-bound end and a C-terminal luminal subunit (CtMGAM).
18036614	1	78	theme	glucose-releasing	240:256	arg1	step					258:261	the last glucose-releasing step	231:261	the last glucose-releasing step in starch digestion	231:281	Human maltase-glucoamylase (MGAM) is one of the two enzymes responsible for catalyzing the last glucose-releasing step in starch digestion.
20798394	12	0	theme	domain	2036:2041	arg1	specificity					1994:2004	the specificity	1990:2004	the specificity of the tensin1 Src homology 2 domain for binding to different proteins	1990:2075	These data demonstrate that tensin1 is extensively phosphorylated on Ser/Thr residues in cells and phosphorylation by p38 MAPK regulates the specificity of the tensin1 Src homology 2 domain for binding to different proteins.
20798394	11	1	theme	p38	1604:1606	arg1	MAPK					1608:1611	p38 MAPK	1604:1611	p38 MAPK in cells	1604:1620	Activation of p38 MAPK in cells by sorbitol-induced hyperosmotic stress increased phosphorylation of S-tag-tensin1, which reduced binding to deleted in liver cancer-1 and increased binding to endogenous pTyr proteins, including p130Cas and focal adhesion kinase.
20798394	10	2	theme	decreased	1540:1548	arg1	binding					1550:1556	decreased binding	1540:1556	decreased binding with deleted in liver cancer-1	1540:1587	Recombinant p38α MAPK also phosphorylated S-tag-tensin1, resulting in decreased binding with deleted in liver cancer-1.
20798394	11	3	theme	hyperosmotic	1642:1653	arg1	stress					1655:1660	sorbitol-induced hyperosmotic stress	1625:1660	sorbitol-induced hyperosmotic stress	1625:1660	Activation of p38 MAPK in cells by sorbitol-induced hyperosmotic stress increased phosphorylation of S-tag-tensin1, which reduced binding to deleted in liver cancer-1 and increased binding to endogenous pTyr proteins, including p130Cas and focal adhesion kinase.
20798394	13	4	theme	tyrosine	2161:2168	arg1	kinases					2170:2176	tyrosine kinases	2161:2176	tyrosine kinases	2161:2176	Tensin1 provides a hub for connecting signaling pathways involving p38 MAP kinase, tyrosine kinases and RhoGTPases.
20798394	8	5	theme	Tensin1	1152:1158	arg1	F302A					1160:1164	Tensin1 F302A	1152:1164	Tensin1 F302A	1152:1164	Tensin1 F302A, which does not bind protein phosphatase-1, showed > twofold enhanced phosphorylation of seven sites.
20798394	6	6	theme	peroxyvanadate	872:885	arg1	Addition					860:867	Addition	860:867	Addition of peroxyvanadate to cells to inhibit protein tyrosine phosphatases	860:935	Addition of peroxyvanadate to cells to inhibit protein tyrosine phosphatases exposed 10 pTyr sites and addition of calyculin A to cells to inhibit protein phosphatases type 1 and 2A gave a total of 62 pSer/pThr sites.
20798394	4	7	theme	human	627:631	arg1	S-tag-tensin1					633:645	human S-tag-tensin1	627:645	human S-tag-tensin1 expressed in HEK293 cells by mass spectrometry	627:692	In this study we analyzed the phosphorylation of human S-tag-tensin1 expressed in HEK293 cells by mass spectrometry.
20798394	13	8	theme	MAP	2149:2151	arg1	kinase					2153:2158	p38 MAP kinase	2145:2158	p38 MAP kinase	2145:2158	Tensin1 provides a hub for connecting signaling pathways involving p38 MAP kinase, tyrosine kinases and RhoGTPases.
20798394	2	9	theme	homology	253:260	arg1	domain					264:269	a Src homology 2 domain	247:269	a Src homology 2 domain that binds focal adhesion kinase, p130Cas, and the RhoGAP called deleted in liver cancer-1	247:360	Tensin1 has a phosphotyrosine binding domain that binds the cytoplasmic tail of β-integrin, a Src homology 2 domain that binds focal adhesion kinase, p130Cas, and the RhoGAP called deleted in liver cancer-1, a phosphatase and tensin homology domain that binds protein phosphatase-1α and other regions that bind F-actin.
20798394	2	10	contain	has	163:165	arg1	Tensin1					155:161	Tensin1	155:161	Tensin1	155:161	Tensin1 has a phosphotyrosine binding domain that binds the cytoplasmic tail of β-integrin, a Src homology 2 domain that binds focal adhesion kinase, p130Cas, and the RhoGAP called deleted in liver cancer-1, a phosphatase and tensin homology domain that binds protein phosphatase-1α and other regions that bind F-actin.
20798394	2	10	contain	has	163:165	arg2	domain					193:198	a phosphotyrosine binding domain	167:198	a phosphotyrosine binding domain that binds the cytoplasmic tail of β-integrin	167:244	Tensin1 has a phosphotyrosine binding domain that binds the cytoplasmic tail of β-integrin, a Src homology 2 domain that binds focal adhesion kinase, p130Cas, and the RhoGAP called deleted in liver cancer-1, a phosphatase and tensin homology domain that binds protein phosphatase-1α and other regions that bind F-actin.
20798394	11	11	theme	pTyr	1793:1796	arg1	kinase					1845:1850	focal adhesion kinase	1830:1850	focal adhesion kinase	1830:1850	Activation of p38 MAPK in cells by sorbitol-induced hyperosmotic stress increased phosphorylation of S-tag-tensin1, which reduced binding to deleted in liver cancer-1 and increased binding to endogenous pTyr proteins, including p130Cas and focal adhesion kinase.
20798394	11	11	theme	pTyr	1793:1796	arg1	proteins					1798:1805	endogenous pTyr proteins	1782:1805	endogenous pTyr proteins	1782:1805	Activation of p38 MAPK in cells by sorbitol-induced hyperosmotic stress increased phosphorylation of S-tag-tensin1, which reduced binding to deleted in liver cancer-1 and increased binding to endogenous pTyr proteins, including p130Cas and focal adhesion kinase.
20798394	11	11	theme	pTyr	1793:1796	arg1	p130Cas					1818:1824	p130Cas	1818:1824	p130Cas	1818:1824	Activation of p38 MAPK in cells by sorbitol-induced hyperosmotic stress increased phosphorylation of S-tag-tensin1, which reduced binding to deleted in liver cancer-1 and increased binding to endogenous pTyr proteins, including p130Cas and focal adhesion kinase.
20798394	2	12	theme	adhesion	288:295	arg1	kinase					297:302	focal adhesion kinase	282:302	focal adhesion kinase	282:302	Tensin1 has a phosphotyrosine binding domain that binds the cytoplasmic tail of β-integrin, a Src homology 2 domain that binds focal adhesion kinase, p130Cas, and the RhoGAP called deleted in liver cancer-1, a phosphatase and tensin homology domain that binds protein phosphatase-1α and other regions that bind F-actin.
20798394	13	13	theme	signaling	2116:2124	arg1	pathways					2126:2133	signaling pathways	2116:2133	signaling pathways involving p38 MAP kinase, tyrosine kinases and RhoGTPases	2116:2191	Tensin1 provides a hub for connecting signaling pathways involving p38 MAP kinase, tyrosine kinases and RhoGTPases.
20798394	3	14	theme	cell	534:537	arg1	polarization					539:550	cell polarization	534:550	cell polarization	534:550	The association between tensin1 and these partners affects cell polarization, migration, and invasion.
20798394	5	15	theme	phosphorylated	822:835	arg1	tyrosine					837:844	no phosphorylated tyrosine	819:844	no phosphorylated tyrosine (pTyr)	819:851	Peptides covering >90% of the sequence initially revealed 50 phosphorylated serine/phosphorylated threonine (pSer/pThr) but no phosphorylated tyrosine (pTyr) sites.
20798394	5	15	theme	phosphorylated	822:835	arg1	pTyr					847:850	pTyr	847:850	pTyr	847:850	Peptides covering >90% of the sequence initially revealed 50 phosphorylated serine/phosphorylated threonine (pSer/pThr) but no phosphorylated tyrosine (pTyr) sites.
20798394	6	16	theme	pTyr	948:951	arg1	A					985:985	calyculin A	975:985	calyculin A	975:985	Addition of peroxyvanadate to cells to inhibit protein tyrosine phosphatases exposed 10 pTyr sites and addition of calyculin A to cells to inhibit protein phosphatases type 1 and 2A gave a total of 62 pSer/pThr sites.
20798394	6	16	theme	pTyr	948:951	arg1	sites					953:957	10 pTyr sites	945:957	10 pTyr sites	945:957	Addition of peroxyvanadate to cells to inhibit protein tyrosine phosphatases exposed 10 pTyr sites and addition of calyculin A to cells to inhibit protein phosphatases type 1 and 2A gave a total of 62 pSer/pThr sites.
20798394	7	17	theme	O-linked	1122:1129	arg1	N-acetylglucosamine					1131:1149	O-linked N-acetylglucosamine	1122:1149	O-linked N-acetylglucosamine	1122:1149	We also characterized two sites modified by O-linked N-acetylglucosamine.
20798394	6	18	theme	tyrosine	915:922	arg1	phosphatases					924:935	protein tyrosine phosphatases	907:935	protein tyrosine phosphatases	907:935	Addition of peroxyvanadate to cells to inhibit protein tyrosine phosphatases exposed 10 pTyr sites and addition of calyculin A to cells to inhibit protein phosphatases type 1 and 2A gave a total of 62 pSer/pThr sites.
20798394	2	19	theme	Src	249:251	arg1	domain					264:269	a Src homology 2 domain	247:269	a Src homology 2 domain that binds focal adhesion kinase, p130Cas, and the RhoGAP called deleted in liver cancer-1	247:360	Tensin1 has a phosphotyrosine binding domain that binds the cytoplasmic tail of β-integrin, a Src homology 2 domain that binds focal adhesion kinase, p130Cas, and the RhoGAP called deleted in liver cancer-1, a phosphatase and tensin homology domain that binds protein phosphatase-1α and other regions that bind F-actin.
20798394	1	20	theme	family	120:125	arg1	Tensin1					90:96	Tensin1	90:96	Tensin1	90:96	Tensin1 is the archetype of a family of focal adhesion proteins.
20798394	1	20	theme	family	120:125	arg1	archetype					105:113	the archetype	101:113	the archetype of a family of focal adhesion proteins	101:152	Tensin1 is the archetype of a family of focal adhesion proteins.
20798394	4	21	theme	HEK293	660:665	arg1	cells					667:671	HEK293 cells	660:671	HEK293 cells	660:671	In this study we analyzed the phosphorylation of human S-tag-tensin1 expressed in HEK293 cells by mass spectrometry.
20798394	5	22	theme	sequence	725:732	arg1	%					716:716	>90%	713:716	>90% of the sequence	713:732	Peptides covering >90% of the sequence initially revealed 50 phosphorylated serine/phosphorylated threonine (pSer/pThr) but no phosphorylated tyrosine (pTyr) sites.
20798394	5	22	theme	sequence	725:732	arg1	sequence					725:732	the sequence	721:732	the sequence	721:732	Peptides covering >90% of the sequence initially revealed 50 phosphorylated serine/phosphorylated threonine (pSer/pThr) but no phosphorylated tyrosine (pTyr) sites.
20798394	2	23	theme	β-integrin	235:244	arg1	tail					227:230	the cytoplasmic tail	211:230	the cytoplasmic tail of β-integrin	211:244	Tensin1 has a phosphotyrosine binding domain that binds the cytoplasmic tail of β-integrin, a Src homology 2 domain that binds focal adhesion kinase, p130Cas, and the RhoGAP called deleted in liver cancer-1, a phosphatase and tensin homology domain that binds protein phosphatase-1α and other regions that bind F-actin.
20798394	1	24	theme	adhesion	136:143	arg1	proteins					145:152	focal adhesion proteins	130:152	focal adhesion proteins	130:152	Tensin1 is the archetype of a family of focal adhesion proteins.
20798394	12	25	theme	different	2058:2066	arg1	proteins					2068:2075	different proteins	2058:2075	different proteins	2058:2075	These data demonstrate that tensin1 is extensively phosphorylated on Ser/Thr residues in cells and phosphorylation by p38 MAPK regulates the specificity of the tensin1 Src homology 2 domain for binding to different proteins.
20798394	6	26	theme	A	985:985	arg1	A					985:985	calyculin A	975:985	calyculin A	975:985	Addition of peroxyvanadate to cells to inhibit protein tyrosine phosphatases exposed 10 pTyr sites and addition of calyculin A to cells to inhibit protein phosphatases type 1 and 2A gave a total of 62 pSer/pThr sites.
20798394	6	26	theme	A	985:985	arg1	sites					953:957	10 pTyr sites	945:957	10 pTyr sites	945:957	Addition of peroxyvanadate to cells to inhibit protein tyrosine phosphatases exposed 10 pTyr sites and addition of calyculin A to cells to inhibit protein phosphatases type 1 and 2A gave a total of 62 pSer/pThr sites.
20798394	6	26	theme	A	985:985	arg1	addition					963:970	addition	963:970	addition of calyculin A to cells	963:994	Addition of peroxyvanadate to cells to inhibit protein tyrosine phosphatases exposed 10 pTyr sites and addition of calyculin A to cells to inhibit protein phosphatases type 1 and 2A gave a total of 62 pSer/pThr sites.
20798394	0	27	from	Tensin1	51:57	arg1	analysis					14:21	Comprehensive analysis	0:21	Comprehensive analysis of phosphorylation sites in Tensin1	0:57	Comprehensive analysis of phosphorylation sites in Tensin1 reveals regulation by p38MAPK.
20798394	9	28	dep	in	1447:1448	arg1	vitro					1450:1454	vitro	1450:1454	vitro	1450:1454	The majority of pSer/pThr have adjacent proline (Pro) residues and we show endogenous p38 mitogen activated protein kinase (MAPK) associated with and phosphorylated tensin1 in an in vitro kinase assay.
20798394	6	29	theme	protein	907:913	arg1	phosphatases					924:935	protein tyrosine phosphatases	907:935	protein tyrosine phosphatases	907:935	Addition of peroxyvanadate to cells to inhibit protein tyrosine phosphatases exposed 10 pTyr sites and addition of calyculin A to cells to inhibit protein phosphatases type 1 and 2A gave a total of 62 pSer/pThr sites.
20798394	0	30	from	sites	42:46	arg1	Tensin1					51:57	Tensin1	51:57	Tensin1	51:57	Comprehensive analysis of phosphorylation sites in Tensin1 reveals regulation by p38MAPK.
20798394	10	31	from	cancer-1	1580:1587	arg1	deleted					1563:1569	deleted	1563:1569	deleted	1563:1569	Recombinant p38α MAPK also phosphorylated S-tag-tensin1, resulting in decreased binding with deleted in liver cancer-1.
20798394	2	32	theme	liver	347:351	arg1	cancer-1					353:360	liver cancer-1	347:360	liver cancer-1	347:360	Tensin1 has a phosphotyrosine binding domain that binds the cytoplasmic tail of β-integrin, a Src homology 2 domain that binds focal adhesion kinase, p130Cas, and the RhoGAP called deleted in liver cancer-1, a phosphatase and tensin homology domain that binds protein phosphatase-1α and other regions that bind F-actin.
20798394	0	33	theme	Comprehensive	0:12	arg1	analysis					14:21	Comprehensive analysis	0:21	Comprehensive analysis of phosphorylation sites in Tensin1	0:57	Comprehensive analysis of phosphorylation sites in Tensin1 reveals regulation by p38MAPK.
20798394	9	34	theme	proline	1308:1314	arg1	residues					1322:1329	adjacent proline (Pro) residues	1299:1329	adjacent proline (Pro) residues	1299:1329	The majority of pSer/pThr have adjacent proline (Pro) residues and we show endogenous p38 mitogen activated protein kinase (MAPK) associated with and phosphorylated tensin1 in an in vitro kinase assay.
20798394	9	35	contain	have	1294:1297	arg1	majority					1272:1279	The majority	1268:1279	The majority of pSer/pThr	1268:1292	The majority of pSer/pThr have adjacent proline (Pro) residues and we show endogenous p38 mitogen activated protein kinase (MAPK) associated with and phosphorylated tensin1 in an in vitro kinase assay.
20798394	9	35	contain	have	1294:1297	arg2	residues					1322:1329	adjacent proline (Pro) residues	1299:1329	adjacent proline (Pro) residues	1299:1329	The majority of pSer/pThr have adjacent proline (Pro) residues and we show endogenous p38 mitogen activated protein kinase (MAPK) associated with and phosphorylated tensin1 in an in vitro kinase assay.
20798394	2	36	theme	tensin	381:386	arg1	domain					397:402	a phosphatase and tensin homology domain	363:402	domain	397:402	Tensin1 has a phosphotyrosine binding domain that binds the cytoplasmic tail of β-integrin, a Src homology 2 domain that binds focal adhesion kinase, p130Cas, and the RhoGAP called deleted in liver cancer-1, a phosphatase and tensin homology domain that binds protein phosphatase-1α and other regions that bind F-actin.
20798394	9	37	theme	Pro	1317:1319	arg1	residues					1322:1329	adjacent proline (Pro) residues	1299:1329	adjacent proline (Pro) residues	1299:1329	The majority of pSer/pThr have adjacent proline (Pro) residues and we show endogenous p38 mitogen activated protein kinase (MAPK) associated with and phosphorylated tensin1 in an in vitro kinase assay.
20798394	2	38	theme	other	442:446	arg1	regions					448:454	other regions	442:454	other regions that bind F-actin	442:472	Tensin1 has a phosphotyrosine binding domain that binds the cytoplasmic tail of β-integrin, a Src homology 2 domain that binds focal adhesion kinase, p130Cas, and the RhoGAP called deleted in liver cancer-1, a phosphatase and tensin homology domain that binds protein phosphatase-1α and other regions that bind F-actin.
20798394	11	39	theme	S-tag-tensin1	1691:1703	arg1	phosphorylation					1672:1686	phosphorylation	1672:1686	phosphorylation	1672:1686	Activation of p38 MAPK in cells by sorbitol-induced hyperosmotic stress increased phosphorylation of S-tag-tensin1, which reduced binding to deleted in liver cancer-1 and increased binding to endogenous pTyr proteins, including p130Cas and focal adhesion kinase.
20798394	0	40	theme	sites	42:46	arg1	analysis					14:21	Comprehensive analysis	0:21	Comprehensive analysis of phosphorylation sites in Tensin1	0:57	Comprehensive analysis of phosphorylation sites in Tensin1 reveals regulation by p38MAPK.
20798394	5	41	theme	phosphorylated	756:769	arg1	sites					853:857	50 phosphorylated serine/phosphorylated threonine (pSer/pThr) but no phosphorylated tyrosine (pTyr) sites	753:857	50 phosphorylated serine/phosphorylated threonine (pSer/pThr) but no phosphorylated tyrosine (pTyr) sites	753:857	Peptides covering >90% of the sequence initially revealed 50 phosphorylated serine/phosphorylated threonine (pSer/pThr) but no phosphorylated tyrosine (pTyr) sites.
20798394	5	42	theme	threonine	793:801	arg1	sites					853:857	50 phosphorylated serine/phosphorylated threonine (pSer/pThr) but no phosphorylated tyrosine (pTyr) sites	753:857	50 phosphorylated serine/phosphorylated threonine (pSer/pThr) but no phosphorylated tyrosine (pTyr) sites	753:857	Peptides covering >90% of the sequence initially revealed 50 phosphorylated serine/phosphorylated threonine (pSer/pThr) but no phosphorylated tyrosine (pTyr) sites.
20798394	10	43	theme	Recombinant	1470:1480	arg1	MAPK					1487:1490	Recombinant p38α MAPK	1470:1490	Recombinant p38α MAPK	1470:1490	Recombinant p38α MAPK also phosphorylated S-tag-tensin1, resulting in decreased binding with deleted in liver cancer-1.
20798394	11	44	theme	focal	1830:1834	arg1	kinase					1845:1850	focal adhesion kinase	1830:1850	focal adhesion kinase	1830:1850	Activation of p38 MAPK in cells by sorbitol-induced hyperosmotic stress increased phosphorylation of S-tag-tensin1, which reduced binding to deleted in liver cancer-1 and increased binding to endogenous pTyr proteins, including p130Cas and focal adhesion kinase.
20798394	9	45	theme	endogenous	1343:1352	arg1	kinase					1384:1389	endogenous p38 mitogen activated protein kinase	1343:1389	endogenous p38 mitogen activated protein kinase (MAPK) associated with	1343:1412	The majority of pSer/pThr have adjacent proline (Pro) residues and we show endogenous p38 mitogen activated protein kinase (MAPK) associated with and phosphorylated tensin1 in an in vitro kinase assay.
20798394	9	45	theme	endogenous	1343:1352	arg1	MAPK					1392:1395	MAPK	1392:1395	MAPK	1392:1395	The majority of pSer/pThr have adjacent proline (Pro) residues and we show endogenous p38 mitogen activated protein kinase (MAPK) associated with and phosphorylated tensin1 in an in vitro kinase assay.
20798394	2	46	theme	binding	185:191	arg1	domain					193:198	a phosphotyrosine binding domain	167:198	a phosphotyrosine binding domain that binds the cytoplasmic tail of β-integrin	167:244	Tensin1 has a phosphotyrosine binding domain that binds the cytoplasmic tail of β-integrin, a Src homology 2 domain that binds focal adhesion kinase, p130Cas, and the RhoGAP called deleted in liver cancer-1, a phosphatase and tensin homology domain that binds protein phosphatase-1α and other regions that bind F-actin.
20798394	9	47	theme	mitogen	1358:1364	arg1	kinase					1384:1389	endogenous p38 mitogen activated protein kinase	1343:1389	endogenous p38 mitogen activated protein kinase (MAPK) associated with	1343:1412	The majority of pSer/pThr have adjacent proline (Pro) residues and we show endogenous p38 mitogen activated protein kinase (MAPK) associated with and phosphorylated tensin1 in an in vitro kinase assay.
20798394	9	47	theme	mitogen	1358:1364	arg1	MAPK					1392:1395	MAPK	1392:1395	MAPK	1392:1395	The majority of pSer/pThr have adjacent proline (Pro) residues and we show endogenous p38 mitogen activated protein kinase (MAPK) associated with and phosphorylated tensin1 in an in vitro kinase assay.
20798394	12	48	theme	Src	2021:2023	arg1	domain					2036:2041	the tensin1 Src homology 2 domain	2009:2041	the tensin1 Src homology 2 domain	2009:2041	These data demonstrate that tensin1 is extensively phosphorylated on Ser/Thr residues in cells and phosphorylation by p38 MAPK regulates the specificity of the tensin1 Src homology 2 domain for binding to different proteins.
20798394	10	49	from	deleted	1563:1569	arg1	cancer-1					1580:1587	liver cancer-1	1574:1587	liver cancer-1	1574:1587	Recombinant p38α MAPK also phosphorylated S-tag-tensin1, resulting in decreased binding with deleted in liver cancer-1.
20798394	6	50	theme	pSer/pThr	1061:1069	arg1	sites					1071:1075	62 pSer/pThr sites	1058:1075	62 pSer/pThr sites	1058:1075	Addition of peroxyvanadate to cells to inhibit protein tyrosine phosphatases exposed 10 pTyr sites and addition of calyculin A to cells to inhibit protein phosphatases type 1 and 2A gave a total of 62 pSer/pThr sites.
20798394	9	51	theme	protein	1376:1382	arg1	kinase					1384:1389	endogenous p38 mitogen activated protein kinase	1343:1389	endogenous p38 mitogen activated protein kinase (MAPK) associated with	1343:1412	The majority of pSer/pThr have adjacent proline (Pro) residues and we show endogenous p38 mitogen activated protein kinase (MAPK) associated with and phosphorylated tensin1 in an in vitro kinase assay.
20798394	9	51	theme	protein	1376:1382	arg1	MAPK					1392:1395	MAPK	1392:1395	MAPK	1392:1395	The majority of pSer/pThr have adjacent proline (Pro) residues and we show endogenous p38 mitogen activated protein kinase (MAPK) associated with and phosphorylated tensin1 in an in vitro kinase assay.
20798394	6	52	dep	cells	890:894	arg1	inhibit					899:905	inhibit	899:905	to inhibit protein tyrosine phosphatases	896:935	Addition of peroxyvanadate to cells to inhibit protein tyrosine phosphatases exposed 10 pTyr sites and addition of calyculin A to cells to inhibit protein phosphatases type 1 and 2A gave a total of 62 pSer/pThr sites.
20798394	11	53	theme	MAPK	1608:1611	arg1	Activation					1590:1599	Activation	1590:1599	Activation of p38 MAPK in cells by sorbitol-induced hyperosmotic stress	1590:1660	Activation of p38 MAPK in cells by sorbitol-induced hyperosmotic stress increased phosphorylation of S-tag-tensin1, which reduced binding to deleted in liver cancer-1 and increased binding to endogenous pTyr proteins, including p130Cas and focal adhesion kinase.
20798394	8	54	theme	sites	1261:1265	arg1	phosphorylation					1236:1250	phosphorylation	1236:1250	phosphorylation of seven sites	1236:1265	Tensin1 F302A, which does not bind protein phosphatase-1, showed > twofold enhanced phosphorylation of seven sites.
20798394	2	55	theme	protein	415:421	arg1	phosphatase-1α					423:436	protein phosphatase-1α	415:436	protein phosphatase-1α	415:436	Tensin1 has a phosphotyrosine binding domain that binds the cytoplasmic tail of β-integrin, a Src homology 2 domain that binds focal adhesion kinase, p130Cas, and the RhoGAP called deleted in liver cancer-1, a phosphatase and tensin homology domain that binds protein phosphatase-1α and other regions that bind F-actin.
20798394	10	56	theme	liver	1574:1578	arg1	cancer-1					1580:1587	liver cancer-1	1574:1587	liver cancer-1	1574:1587	Recombinant p38α MAPK also phosphorylated S-tag-tensin1, resulting in decreased binding with deleted in liver cancer-1.
20798394	11	57	theme	sorbitol-induced	1625:1640	arg1	stress					1655:1660	sorbitol-induced hyperosmotic stress	1625:1660	sorbitol-induced hyperosmotic stress	1625:1660	Activation of p38 MAPK in cells by sorbitol-induced hyperosmotic stress increased phosphorylation of S-tag-tensin1, which reduced binding to deleted in liver cancer-1 and increased binding to endogenous pTyr proteins, including p130Cas and focal adhesion kinase.
20798394	11	58	from	Activation	1590:1599	arg1	cells					1616:1620	cells	1616:1620	cells	1616:1620	Activation of p38 MAPK in cells by sorbitol-induced hyperosmotic stress increased phosphorylation of S-tag-tensin1, which reduced binding to deleted in liver cancer-1 and increased binding to endogenous pTyr proteins, including p130Cas and focal adhesion kinase.
20798394	12	59	theme	p38	1971:1973	arg1	MAPK					1975:1978	p38 MAPK	1971:1978	p38 MAPK	1971:1978	These data demonstrate that tensin1 is extensively phosphorylated on Ser/Thr residues in cells and phosphorylation by p38 MAPK regulates the specificity of the tensin1 Src homology 2 domain for binding to different proteins.
20798394	10	60	with	binding	1550:1556	arg1	deleted					1563:1569	deleted	1563:1569	deleted	1563:1569	Recombinant p38α MAPK also phosphorylated S-tag-tensin1, resulting in decreased binding with deleted in liver cancer-1.
20798394	4	61	theme	S-tag-tensin1	633:645	arg1	phosphorylation					608:622	the phosphorylation	604:622	the phosphorylation of human S-tag-tensin1 expressed in HEK293 cells by mass spectrometry	604:692	In this study we analyzed the phosphorylation of human S-tag-tensin1 expressed in HEK293 cells by mass spectrometry.
20798394	2	62	theme	focal	282:286	arg1	kinase					297:302	focal adhesion kinase	282:302	focal adhesion kinase	282:302	Tensin1 has a phosphotyrosine binding domain that binds the cytoplasmic tail of β-integrin, a Src homology 2 domain that binds focal adhesion kinase, p130Cas, and the RhoGAP called deleted in liver cancer-1, a phosphatase and tensin homology domain that binds protein phosphatase-1α and other regions that bind F-actin.
20798394	9	63	theme	phosphorylated	1418:1431	arg1	tensin1					1433:1439	phosphorylated tensin1	1418:1439	phosphorylated tensin1	1418:1439	The majority of pSer/pThr have adjacent proline (Pro) residues and we show endogenous p38 mitogen activated protein kinase (MAPK) associated with and phosphorylated tensin1 in an in vitro kinase assay.
20798394	11	64	theme	endogenous	1782:1791	arg1	kinase					1845:1850	focal adhesion kinase	1830:1850	focal adhesion kinase	1830:1850	Activation of p38 MAPK in cells by sorbitol-induced hyperosmotic stress increased phosphorylation of S-tag-tensin1, which reduced binding to deleted in liver cancer-1 and increased binding to endogenous pTyr proteins, including p130Cas and focal adhesion kinase.
20798394	11	64	theme	endogenous	1782:1791	arg1	proteins					1798:1805	endogenous pTyr proteins	1782:1805	endogenous pTyr proteins	1782:1805	Activation of p38 MAPK in cells by sorbitol-induced hyperosmotic stress increased phosphorylation of S-tag-tensin1, which reduced binding to deleted in liver cancer-1 and increased binding to endogenous pTyr proteins, including p130Cas and focal adhesion kinase.
20798394	11	64	theme	endogenous	1782:1791	arg1	p130Cas					1818:1824	p130Cas	1818:1824	p130Cas	1818:1824	Activation of p38 MAPK in cells by sorbitol-induced hyperosmotic stress increased phosphorylation of S-tag-tensin1, which reduced binding to deleted in liver cancer-1 and increased binding to endogenous pTyr proteins, including p130Cas and focal adhesion kinase.
20798394	5	65	theme	tyrosine	837:844	arg1	sites					853:857	50 phosphorylated serine/phosphorylated threonine (pSer/pThr) but no phosphorylated tyrosine (pTyr) sites	753:857	50 phosphorylated serine/phosphorylated threonine (pSer/pThr) but no phosphorylated tyrosine (pTyr) sites	753:857	Peptides covering >90% of the sequence initially revealed 50 phosphorylated serine/phosphorylated threonine (pSer/pThr) but no phosphorylated tyrosine (pTyr) sites.
20798394	13	66	theme	p38	2145:2147	arg1	kinase					2153:2158	p38 MAP kinase	2145:2158	p38 MAP kinase	2145:2158	Tensin1 provides a hub for connecting signaling pathways involving p38 MAP kinase, tyrosine kinases and RhoGTPases.
20798394	2	67	theme	cytoplasmic	215:225	arg1	tail					227:230	the cytoplasmic tail	211:230	the cytoplasmic tail of β-integrin	211:244	Tensin1 has a phosphotyrosine binding domain that binds the cytoplasmic tail of β-integrin, a Src homology 2 domain that binds focal adhesion kinase, p130Cas, and the RhoGAP called deleted in liver cancer-1, a phosphatase and tensin homology domain that binds protein phosphatase-1α and other regions that bind F-actin.
20798394	9	68	theme	in	1447:1448	arg1	assay					1463:1467	an in vitro kinase assay	1444:1467	an in vitro kinase assay	1444:1467	The majority of pSer/pThr have adjacent proline (Pro) residues and we show endogenous p38 mitogen activated protein kinase (MAPK) associated with and phosphorylated tensin1 in an in vitro kinase assay.
20798394	8	69	theme	protein	1187:1193	arg1	phosphatase-1					1195:1207	protein phosphatase-1	1187:1207	protein phosphatase-1	1187:1207	Tensin1 F302A, which does not bind protein phosphatase-1, showed > twofold enhanced phosphorylation of seven sites.
20798394	12	70	theme	tensin1	2013:2019	arg1	domain					2036:2041	the tensin1 Src homology 2 domain	2009:2041	the tensin1 Src homology 2 domain	2009:2041	These data demonstrate that tensin1 is extensively phosphorylated on Ser/Thr residues in cells and phosphorylation by p38 MAPK regulates the specificity of the tensin1 Src homology 2 domain for binding to different proteins.
20798394	4	71	theme	mass	676:679	arg1	spectrometry					681:692	mass spectrometry	676:692	mass spectrometry	676:692	In this study we analyzed the phosphorylation of human S-tag-tensin1 expressed in HEK293 cells by mass spectrometry.
20798394	7	72	link	O-linked	1122:1129	arg1	N-acetylglucosamine					1131:1149	O-linked N-acetylglucosamine	1122:1149	O-linked N-acetylglucosamine	1122:1149	We also characterized two sites modified by O-linked N-acetylglucosamine.
20798394	9	73	theme	kinase	1456:1461	arg1	assay					1463:1467	an in vitro kinase assay	1444:1467	an in vitro kinase assay	1444:1467	The majority of pSer/pThr have adjacent proline (Pro) residues and we show endogenous p38 mitogen activated protein kinase (MAPK) associated with and phosphorylated tensin1 in an in vitro kinase assay.
20798394	6	74	theme	protein	1007:1013	arg1	phosphatases					1015:1026	protein phosphatases type 1 and 2A	1007:1040	protein phosphatases type 1 and 2A gave a total of 62 pSer/pThr sites	1007:1075	Addition of peroxyvanadate to cells to inhibit protein tyrosine phosphatases exposed 10 pTyr sites and addition of calyculin A to cells to inhibit protein phosphatases type 1 and 2A gave a total of 62 pSer/pThr sites.
20798394	6	74	theme	protein	1007:1013	arg1	type					1028:1031	type 1	1028:1033	type 1	1028:1033	Addition of peroxyvanadate to cells to inhibit protein tyrosine phosphatases exposed 10 pTyr sites and addition of calyculin A to cells to inhibit protein phosphatases type 1 and 2A gave a total of 62 pSer/pThr sites.
20798394	6	74	theme	protein	1007:1013	arg1	2A					1039:1040	2A	1039:1040	2A	1039:1040	Addition of peroxyvanadate to cells to inhibit protein tyrosine phosphatases exposed 10 pTyr sites and addition of calyculin A to cells to inhibit protein phosphatases type 1 and 2A gave a total of 62 pSer/pThr sites.
20798394	11	75	theme	liver	1742:1746	arg1	cancer-1					1748:1755	liver cancer-1	1742:1755	liver cancer-1	1742:1755	Activation of p38 MAPK in cells by sorbitol-induced hyperosmotic stress increased phosphorylation of S-tag-tensin1, which reduced binding to deleted in liver cancer-1 and increased binding to endogenous pTyr proteins, including p130Cas and focal adhesion kinase.
20798394	1	76	theme	focal	130:134	arg1	proteins					145:152	focal adhesion proteins	130:152	focal adhesion proteins	130:152	Tensin1 is the archetype of a family of focal adhesion proteins.
20798394	12	77	theme	Ser/Thr	1922:1928	arg1	residues					1930:1937	Ser/Thr residues	1922:1937	Ser/Thr residues	1922:1937	These data demonstrate that tensin1 is extensively phosphorylated on Ser/Thr residues in cells and phosphorylation by p38 MAPK regulates the specificity of the tensin1 Src homology 2 domain for binding to different proteins.
20798394	1	78	theme	proteins	145:152	arg1	family					120:125	a family	118:125	a family of focal adhesion proteins	118:152	Tensin1 is the archetype of a family of focal adhesion proteins.
20798394	0	79	from	analysis	14:21	arg1	Tensin1					51:57	Tensin1	51:57	Tensin1	51:57	Comprehensive analysis of phosphorylation sites in Tensin1 reveals regulation by p38MAPK.
20798394	6	80	theme	calyculin	975:983	arg1	A					985:985	calyculin A	975:985	calyculin A	975:985	Addition of peroxyvanadate to cells to inhibit protein tyrosine phosphatases exposed 10 pTyr sites and addition of calyculin A to cells to inhibit protein phosphatases type 1 and 2A gave a total of 62 pSer/pThr sites.
20798394	6	81	dep	phosphatases	1015:1026	arg1	phosphatases					1015:1026	protein phosphatases type 1 and 2A	1007:1040	protein phosphatases type 1 and 2A gave a total of 62 pSer/pThr sites	1007:1075	Addition of peroxyvanadate to cells to inhibit protein tyrosine phosphatases exposed 10 pTyr sites and addition of calyculin A to cells to inhibit protein phosphatases type 1 and 2A gave a total of 62 pSer/pThr sites.
20798394	6	81	dep	phosphatases	1015:1026	arg1	type					1028:1031	type 1	1028:1033	type 1	1028:1033	Addition of peroxyvanadate to cells to inhibit protein tyrosine phosphatases exposed 10 pTyr sites and addition of calyculin A to cells to inhibit protein phosphatases type 1 and 2A gave a total of 62 pSer/pThr sites.
20798394	6	81	dep	phosphatases	1015:1026	arg1	2A					1039:1040	2A	1039:1040	2A	1039:1040	Addition of peroxyvanadate to cells to inhibit protein tyrosine phosphatases exposed 10 pTyr sites and addition of calyculin A to cells to inhibit protein phosphatases type 1 and 2A gave a total of 62 pSer/pThr sites.
20798394	9	82	theme	pSer/pThr	1284:1292	arg1	majority					1272:1279	The majority	1268:1279	The majority of pSer/pThr	1268:1292	The majority of pSer/pThr have adjacent proline (Pro) residues and we show endogenous p38 mitogen activated protein kinase (MAPK) associated with and phosphorylated tensin1 in an in vitro kinase assay.
20798394	2	83	dep	called	329:334	arg1	RhoGAP					322:327	the RhoGAP	318:327	the RhoGAP called deleted in liver cancer-1	318:360	Tensin1 has a phosphotyrosine binding domain that binds the cytoplasmic tail of β-integrin, a Src homology 2 domain that binds focal adhesion kinase, p130Cas, and the RhoGAP called deleted in liver cancer-1, a phosphatase and tensin homology domain that binds protein phosphatase-1α and other regions that bind F-actin.
20798394	2	83	dep	called	329:334	arg1	deleted					336:342	deleted	336:342	deleted in liver cancer-1	336:360	Tensin1 has a phosphotyrosine binding domain that binds the cytoplasmic tail of β-integrin, a Src homology 2 domain that binds focal adhesion kinase, p130Cas, and the RhoGAP called deleted in liver cancer-1, a phosphatase and tensin homology domain that binds protein phosphatase-1α and other regions that bind F-actin.
20798394	9	84	theme	adjacent	1299:1306	arg1	residues					1322:1329	adjacent proline (Pro) residues	1299:1329	adjacent proline (Pro) residues	1299:1329	The majority of pSer/pThr have adjacent proline (Pro) residues and we show endogenous p38 mitogen activated protein kinase (MAPK) associated with and phosphorylated tensin1 in an in vitro kinase assay.
20798394	0	85	theme	phosphorylation	26:40	arg1	sites					42:46	phosphorylation sites	26:46	phosphorylation sites in Tensin1	26:57	Comprehensive analysis of phosphorylation sites in Tensin1 reveals regulation by p38MAPK.
20798394	8	86	dep	showed	1210:1215	arg1	enhanced					1227:1234	enhanced	1227:1234	showed > twofold enhanced phosphorylation of seven sites	1210:1265	Tensin1 F302A, which does not bind protein phosphatase-1, showed > twofold enhanced phosphorylation of seven sites.
20798394	2	87	theme	homology	388:395	arg1	domain					397:402	a phosphatase and tensin homology domain	363:402	domain	397:402	Tensin1 has a phosphotyrosine binding domain that binds the cytoplasmic tail of β-integrin, a Src homology 2 domain that binds focal adhesion kinase, p130Cas, and the RhoGAP called deleted in liver cancer-1, a phosphatase and tensin homology domain that binds protein phosphatase-1α and other regions that bind F-actin.
20798394	2	88	theme	phosphotyrosine	169:183	arg1	domain					193:198	a phosphotyrosine binding domain	167:198	a phosphotyrosine binding domain that binds the cytoplasmic tail of β-integrin	167:244	Tensin1 has a phosphotyrosine binding domain that binds the cytoplasmic tail of β-integrin, a Src homology 2 domain that binds focal adhesion kinase, p130Cas, and the RhoGAP called deleted in liver cancer-1, a phosphatase and tensin homology domain that binds protein phosphatase-1α and other regions that bind F-actin.
20798394	11	89	from	MAPK	1608:1611	arg1	cells					1616:1620	cells	1616:1620	cells	1616:1620	Activation of p38 MAPK in cells by sorbitol-induced hyperosmotic stress increased phosphorylation of S-tag-tensin1, which reduced binding to deleted in liver cancer-1 and increased binding to endogenous pTyr proteins, including p130Cas and focal adhesion kinase.
20798394	5	90	theme	serine/phosphorylated	771:791	arg1	pSer/pThr					804:812	pSer/pThr	804:812	pSer/pThr	804:812	Peptides covering >90% of the sequence initially revealed 50 phosphorylated serine/phosphorylated threonine (pSer/pThr) but no phosphorylated tyrosine (pTyr) sites.
20798394	5	90	theme	serine/phosphorylated	771:791	arg1	threonine					793:801	serine/phosphorylated threonine	771:801	serine/phosphorylated threonine (pSer/pThr)	771:813	Peptides covering >90% of the sequence initially revealed 50 phosphorylated serine/phosphorylated threonine (pSer/pThr) but no phosphorylated tyrosine (pTyr) sites.
20798394	11	91	from	cells	1616:1620	arg1	Activation					1590:1599	Activation	1590:1599	Activation of p38 MAPK in cells by sorbitol-induced hyperosmotic stress	1590:1660	Activation of p38 MAPK in cells by sorbitol-induced hyperosmotic stress increased phosphorylation of S-tag-tensin1, which reduced binding to deleted in liver cancer-1 and increased binding to endogenous pTyr proteins, including p130Cas and focal adhesion kinase.
20798394	10	92	theme	p38α	1482:1485	arg1	MAPK					1487:1490	Recombinant p38α MAPK	1470:1490	Recombinant p38α MAPK	1470:1490	Recombinant p38α MAPK also phosphorylated S-tag-tensin1, resulting in decreased binding with deleted in liver cancer-1.
20798394	11	93	theme	adhesion	1836:1843	arg1	kinase					1845:1850	focal adhesion kinase	1830:1850	focal adhesion kinase	1830:1850	Activation of p38 MAPK in cells by sorbitol-induced hyperosmotic stress increased phosphorylation of S-tag-tensin1, which reduced binding to deleted in liver cancer-1 and increased binding to endogenous pTyr proteins, including p130Cas and focal adhesion kinase.
20798394	9	94	theme	p38	1354:1356	arg1	kinase					1384:1389	endogenous p38 mitogen activated protein kinase	1343:1389	endogenous p38 mitogen activated protein kinase (MAPK) associated with	1343:1412	The majority of pSer/pThr have adjacent proline (Pro) residues and we show endogenous p38 mitogen activated protein kinase (MAPK) associated with and phosphorylated tensin1 in an in vitro kinase assay.
20798394	9	94	theme	p38	1354:1356	arg1	MAPK					1392:1395	MAPK	1392:1395	MAPK	1392:1395	The majority of pSer/pThr have adjacent proline (Pro) residues and we show endogenous p38 mitogen activated protein kinase (MAPK) associated with and phosphorylated tensin1 in an in vitro kinase assay.
20798394	12	95	theme	homology	2025:2032	arg1	domain					2036:2041	the tensin1 Src homology 2 domain	2009:2041	the tensin1 Src homology 2 domain	2009:2041	These data demonstrate that tensin1 is extensively phosphorylated on Ser/Thr residues in cells and phosphorylation by p38 MAPK regulates the specificity of the tensin1 Src homology 2 domain for binding to different proteins.
20798394	6	96	theme	sites	1071:1075	arg1	total					1049:1053	a total	1047:1053	a total of 62 pSer/pThr sites	1047:1075	Addition of peroxyvanadate to cells to inhibit protein tyrosine phosphatases exposed 10 pTyr sites and addition of calyculin A to cells to inhibit protein phosphatases type 1 and 2A gave a total of 62 pSer/pThr sites.
20798394	9	97	theme	activated	1366:1374	arg1	kinase					1384:1389	endogenous p38 mitogen activated protein kinase	1343:1389	endogenous p38 mitogen activated protein kinase (MAPK) associated with	1343:1412	The majority of pSer/pThr have adjacent proline (Pro) residues and we show endogenous p38 mitogen activated protein kinase (MAPK) associated with and phosphorylated tensin1 in an in vitro kinase assay.
20798394	9	97	theme	activated	1366:1374	arg1	MAPK					1392:1395	MAPK	1392:1395	MAPK	1392:1395	The majority of pSer/pThr have adjacent proline (Pro) residues and we show endogenous p38 mitogen activated protein kinase (MAPK) associated with and phosphorylated tensin1 in an in vitro kinase assay.
1059087	4	0	theme	residues	687:694	arg1	basis					614:618	the basis	610:618	the basis of the locations of glycosylated amino acids	610:663	Glycophorin appears to be organized into three distinct "domains" on the basis of the locations of glycosylated amino acids and the clustering of residues of similar type.
1059087	4	0	theme	residues	687:694	arg1	clustering					673:682	the clustering	669:682	the clustering of residues of similar type	669:710	Glycophorin appears to be organized into three distinct "domains" on the basis of the locations of glycosylated amino acids and the clustering of residues of similar type.
1059087	3	1	theme	Edman	511:515	arg1	techniques					529:538	Edman degradation techniques	511:538	Edman degradation techniques	511:538	The location of each of these oligosaccharides and the complete amino-acid sequence of this molecular have been determined by Edman degradation techniques.
1059087	5	2	from	iii	888:890	arg1	residues					783:790	approximately 64 residues	766:790	approximately 64 residues from the NH2-terminus, (ii) a "hydrophobic" segment of approximately 32 nonpolar residues, and (iii) a COOH-terminal segment	766:915	These include (i) a glycosylated segment composed of approximately 64 residues from the NH2-terminus, (ii) a "hydrophobic" segment of approximately 32 nonpolar residues, and (iii) a COOH-terminal segment, composed of approximately 35 residues, which has an unusual concentration of hydrophilic amino acids.
1059087	5	3	theme	nonpolar	864:871	arg1	residues					873:880	approximately 32 nonpolar residues	847:880	approximately 32 nonpolar residues	847:880	These include (i) a glycosylated segment composed of approximately 64 residues from the NH2-terminus, (ii) a "hydrophobic" segment of approximately 32 nonpolar residues, and (iii) a COOH-terminal segment, composed of approximately 35 residues, which has an unusual concentration of hydrophilic amino acids.
1059087	3	4	theme	degradation	517:527	arg1	techniques					529:538	Edman degradation techniques	511:538	Edman degradation techniques	511:538	The location of each of these oligosaccharides and the complete amino-acid sequence of this molecular have been determined by Edman degradation techniques.
1059087	2	5	attach	attached	361:368	arg2	unit					353:356	one more complex unit	336:356	one more complex unit	336:356	Fifteen oligosaccharides are linked to threonine/serine residues via O-glycosidic bonds, and one more complex unit is attached to asparagine.
1059087	2	5	attach	attached	361:368	arg1	asparagine					373:382	asparagine	373:382	asparagine	373:382	Fifteen oligosaccharides are linked to threonine/serine residues via O-glycosidic bonds, and one more complex unit is attached to asparagine.
1059087	6	6	theme	transmembrane	1164:1176	arg1	orientation					1178:1188	a transmembrane orientation	1162:1188	a transmembrane orientation	1162:1188	This unique structure is consistent with the earlier suggestions that glycophorin is one of the major "intrinsic" membrane proteins which has a transmembrane orientation.
1059087	6	7	theme	"	1132:1132	arg1	proteins					1143:1150	the major "intrinsic" membrane proteins	1112:1150	the major "intrinsic" membrane proteins which has a transmembrane orientation	1112:1188	This unique structure is consistent with the earlier suggestions that glycophorin is one of the major "intrinsic" membrane proteins which has a transmembrane orientation.
1059087	6	8	with	consistent	1045:1054	arg1	suggestions					1073:1083	the earlier suggestions	1061:1083	the earlier suggestions that glycophorin is one of the major "intrinsic" membrane proteins which has a transmembrane orientation	1061:1188	This unique structure is consistent with the earlier suggestions that glycophorin is one of the major "intrinsic" membrane proteins which has a transmembrane orientation.
1059087	5	9	gly	glycosylated	733:744	arg1	segment					746:752	a glycosylated segment	731:752	a glycosylated segment composed of approximately 64 residues from the NH2-terminus, (ii) a "hydrophobic" segment of approximately 32 nonpolar residues, and (iii) a COOH-terminal segment	731:915	These include (i) a glycosylated segment composed of approximately 64 residues from the NH2-terminus, (ii) a "hydrophobic" segment of approximately 32 nonpolar residues, and (iii) a COOH-terminal segment, composed of approximately 35 residues, which has an unusual concentration of hydrophilic amino acids.
1059087	4	10	theme	similar	699:705	arg1	type					707:710	similar type	699:710	similar type	699:710	Glycophorin appears to be organized into three distinct "domains" on the basis of the locations of glycosylated amino acids and the clustering of residues of similar type.
1059087	5	11	theme	hydrophobic	823:833	arg1	segment					836:842	a "hydrophobic" segment	820:842	(ii) a "hydrophobic" segment of approximately 32 nonpolar residues	815:880	These include (i) a glycosylated segment composed of approximately 64 residues from the NH2-terminus, (ii) a "hydrophobic" segment of approximately 32 nonpolar residues, and (iii) a COOH-terminal segment, composed of approximately 35 residues, which has an unusual concentration of hydrophilic amino acids.
1059087	1	12	gly	sialoglycoprotein	114:130	arg1	Glycophorin					91:101	Glycophorin	91:101	Glycophorin	91:101	Glycophorin, the major sialoglycoprotein of the human erythrocyte membrane, is composed of 131 amino acids and an average of 16 oligosaccharide chains.
1059087	1	12	gly	sialoglycoprotein	114:130	arg1	sialoglycoprotein					114:130	the major sialoglycoprotein	104:130	the major sialoglycoprotein of the human erythrocyte membrane	104:164	Glycophorin, the major sialoglycoprotein of the human erythrocyte membrane, is composed of 131 amino acids and an average of 16 oligosaccharide chains.
1059087	4	13	theme	locations	627:635	arg1	basis					614:618	the basis	610:618	the basis of the locations of glycosylated amino acids	610:663	Glycophorin appears to be organized into three distinct "domains" on the basis of the locations of glycosylated amino acids and the clustering of residues of similar type.
1059087	4	13	theme	locations	627:635	arg1	clustering					673:682	the clustering	669:682	the clustering of residues of similar type	669:710	Glycophorin appears to be organized into three distinct "domains" on the basis of the locations of glycosylated amino acids and the clustering of residues of similar type.
1059087	2	14	theme	threonine/serine	282:297	arg1	residues					299:306	threonine/serine residues	282:306	threonine/serine residues	282:306	Fifteen oligosaccharides are linked to threonine/serine residues via O-glycosidic bonds, and one more complex unit is attached to asparagine.
1059087	3	15	theme	complete	440:447	arg1	sequence					460:467	the complete amino-acid sequence	436:467	the complete amino-acid sequence of this molecular	436:485	The location of each of these oligosaccharides and the complete amino-acid sequence of this molecular have been determined by Edman degradation techniques.
1059087	5	16	theme	residues	873:880	arg1	segment					836:842	a "hydrophobic" segment	820:842	(ii) a "hydrophobic" segment of approximately 32 nonpolar residues	815:880	These include (i) a glycosylated segment composed of approximately 64 residues from the NH2-terminus, (ii) a "hydrophobic" segment of approximately 32 nonpolar residues, and (iii) a COOH-terminal segment, composed of approximately 35 residues, which has an unusual concentration of hydrophilic amino acids.
1059087	2	17	attach	linked	272:277	arg1	residues					299:306	threonine/serine residues	282:306	threonine/serine residues	282:306	Fifteen oligosaccharides are linked to threonine/serine residues via O-glycosidic bonds, and one more complex unit is attached to asparagine.
1059087	2	17	attach	linked	272:277	arg2	oligosaccharides					251:266	Fifteen oligosaccharides	243:266	Fifteen oligosaccharides	243:266	Fifteen oligosaccharides are linked to threonine/serine residues via O-glycosidic bonds, and one more complex unit is attached to asparagine.
1059087	2	17	attach	linked	272:277	arg3	bonds					325:329	O-glycosidic bonds	312:329	O-glycosidic bonds	312:329	Fifteen oligosaccharides are linked to threonine/serine residues via O-glycosidic bonds, and one more complex unit is attached to asparagine.
1059087	3	18	theme	amino-acid	449:458	arg1	sequence					460:467	the complete amino-acid sequence	436:467	the complete amino-acid sequence of this molecular	436:485	The location of each of these oligosaccharides and the complete amino-acid sequence of this molecular have been determined by Edman degradation techniques.
1059087	4	19	gly	glycosylated	640:651	arg1	acids					659:663	glycosylated amino acids	640:663	glycosylated amino acids	640:663	Glycophorin appears to be organized into three distinct "domains" on the basis of the locations of glycosylated amino acids and the clustering of residues of similar type.
1059087	5	20	theme	glycosylated	733:744	arg1	segment					746:752	a glycosylated segment	731:752	a glycosylated segment composed of approximately 64 residues from the NH2-terminus, (ii) a "hydrophobic" segment of approximately 32 nonpolar residues, and (iii) a COOH-terminal segment	731:915	These include (i) a glycosylated segment composed of approximately 64 residues from the NH2-terminus, (ii) a "hydrophobic" segment of approximately 32 nonpolar residues, and (iii) a COOH-terminal segment, composed of approximately 35 residues, which has an unusual concentration of hydrophilic amino acids.
1059087	1	21	theme	amino	186:190	arg1	acids					192:196	131 amino acids	182:196	131 amino acids	182:196	Glycophorin, the major sialoglycoprotein of the human erythrocyte membrane, is composed of 131 amino acids and an average of 16 oligosaccharide chains.
1059087	0	22	theme	Amino-acid	0:9	arg1	sequence					11:18	Amino-acid sequence	0:18	Amino-acid sequence	0:18	Amino-acid sequence and oligosaccharide attachment sites of human erythrocyte glycophorin.
1059087	5	23	theme	"	834:834	arg1	segment					836:842	a "hydrophobic" segment	820:842	(ii) a "hydrophobic" segment of approximately 32 nonpolar residues	815:880	These include (i) a glycosylated segment composed of approximately 64 residues from the NH2-terminus, (ii) a "hydrophobic" segment of approximately 32 nonpolar residues, and (iii) a COOH-terminal segment, composed of approximately 35 residues, which has an unusual concentration of hydrophilic amino acids.
1059087	0	24	theme	oligosaccharide	24:38	arg1	sites					51:55	oligosaccharide attachment sites	24:55	oligosaccharide attachment sites	24:55	Amino-acid sequence and oligosaccharide attachment sites of human erythrocyte glycophorin.
1059087	0	24	theme	oligosaccharide	24:38	arg1	glycophorin					78:88	human erythrocyte glycophorin	60:88	human erythrocyte glycophorin	60:88	Amino-acid sequence and oligosaccharide attachment sites of human erythrocyte glycophorin.
1059087	5	25	theme	NH2-terminus	801:812	arg1	segment					836:842	a "hydrophobic" segment	820:842	(ii) a "hydrophobic" segment of approximately 32 nonpolar residues	815:880	These include (i) a glycosylated segment composed of approximately 64 residues from the NH2-terminus, (ii) a "hydrophobic" segment of approximately 32 nonpolar residues, and (iii) a COOH-terminal segment, composed of approximately 35 residues, which has an unusual concentration of hydrophilic amino acids.
1059087	1	26	theme	major	108:112	arg1	Glycophorin					91:101	Glycophorin	91:101	Glycophorin	91:101	Glycophorin, the major sialoglycoprotein of the human erythrocyte membrane, is composed of 131 amino acids and an average of 16 oligosaccharide chains.
1059087	1	26	theme	major	108:112	arg1	sialoglycoprotein					114:130	the major sialoglycoprotein	104:130	the major sialoglycoprotein of the human erythrocyte membrane	104:164	Glycophorin, the major sialoglycoprotein of the human erythrocyte membrane, is composed of 131 amino acids and an average of 16 oligosaccharide chains.
1059087	6	27	theme	unique	1025:1030	arg1	structure					1032:1040	This unique structure	1020:1040	This unique structure	1020:1040	This unique structure is consistent with the earlier suggestions that glycophorin is one of the major "intrinsic" membrane proteins which has a transmembrane orientation.
1059087	6	28	theme	earlier	1065:1071	arg1	suggestions					1073:1083	the earlier suggestions	1061:1083	the earlier suggestions that glycophorin is one of the major "intrinsic" membrane proteins which has a transmembrane orientation	1061:1188	This unique structure is consistent with the earlier suggestions that glycophorin is one of the major "intrinsic" membrane proteins which has a transmembrane orientation.
1059087	4	29	theme	distinct	588:595	arg1	domains					598:604	three distinct "domains	582:604	three distinct "domains" on the basis of the locations of glycosylated amino acids and the clustering of residues of similar type	582:710	Glycophorin appears to be organized into three distinct "domains" on the basis of the locations of glycosylated amino acids and the clustering of residues of similar type.
1059087	2	30	theme	O-glycosidic	312:323	arg1	bonds					325:329	O-glycosidic bonds	312:329	O-glycosidic bonds	312:329	Fifteen oligosaccharides are linked to threonine/serine residues via O-glycosidic bonds, and one more complex unit is attached to asparagine.
1059087	3	31	theme	molecular	477:485	arg1	location					389:396	The location	385:396	The location of each of these oligosaccharides	385:430	The location of each of these oligosaccharides and the complete amino-acid sequence of this molecular have been determined by Edman degradation techniques.
1059087	3	31	theme	molecular	477:485	arg1	sequence					460:467	the complete amino-acid sequence	436:467	the complete amino-acid sequence of this molecular	436:485	The location of each of these oligosaccharides and the complete amino-acid sequence of this molecular have been determined by Edman degradation techniques.
1059087	4	32	theme	type	707:710	arg1	residues					687:694	residues	687:694	residues of similar type	687:710	Glycophorin appears to be organized into three distinct "domains" on the basis of the locations of glycosylated amino acids and the clustering of residues of similar type.
1059087	4	32	theme	type	707:710	arg1	type					707:710	similar type	699:710	similar type	699:710	Glycophorin appears to be organized into three distinct "domains" on the basis of the locations of glycosylated amino acids and the clustering of residues of similar type.
1059087	5	33	dep	segment	836:842	arg1	ii					816:817	ii	816:817	ii	816:817	These include (i) a glycosylated segment composed of approximately 64 residues from the NH2-terminus, (ii) a "hydrophobic" segment of approximately 32 nonpolar residues, and (iii) a COOH-terminal segment, composed of approximately 35 residues, which has an unusual concentration of hydrophilic amino acids.
1059087	5	33	dep	segment	836:842	arg1	segment					909:915	a COOH-terminal segment	893:915	a COOH-terminal segment	893:915	These include (i) a glycosylated segment composed of approximately 64 residues from the NH2-terminus, (ii) a "hydrophobic" segment of approximately 32 nonpolar residues, and (iii) a COOH-terminal segment, composed of approximately 35 residues, which has an unusual concentration of hydrophilic amino acids.
1059087	5	33	dep	segment	836:842	arg1	the					797:799	the	797:799	the	797:799	These include (i) a glycosylated segment composed of approximately 64 residues from the NH2-terminus, (ii) a "hydrophobic" segment of approximately 32 nonpolar residues, and (iii) a COOH-terminal segment, composed of approximately 35 residues, which has an unusual concentration of hydrophilic amino acids.
1059087	5	34	contain	has	963:965	arg2	concentration					978:990	an unusual concentration	967:990	an unusual concentration	967:990	These include (i) a glycosylated segment composed of approximately 64 residues from the NH2-terminus, (ii) a "hydrophobic" segment of approximately 32 nonpolar residues, and (iii) a COOH-terminal segment, composed of approximately 35 residues, which has an unusual concentration of hydrophilic amino acids.
1059087	5	34	contain	has	963:965	arg1	segment					746:752	a glycosylated segment	731:752	a glycosylated segment composed of approximately 64 residues from the NH2-terminus, (ii) a "hydrophobic" segment of approximately 32 nonpolar residues, and (iii) a COOH-terminal segment	731:915	These include (i) a glycosylated segment composed of approximately 64 residues from the NH2-terminus, (ii) a "hydrophobic" segment of approximately 32 nonpolar residues, and (iii) a COOH-terminal segment, composed of approximately 35 residues, which has an unusual concentration of hydrophilic amino acids.
1059087	4	35	theme	amino	653:657	arg1	acids					659:663	glycosylated amino acids	640:663	glycosylated amino acids	640:663	Glycophorin appears to be organized into three distinct "domains" on the basis of the locations of glycosylated amino acids and the clustering of residues of similar type.
1059087	0	36	theme	attachment	40:49	arg1	sites					51:55	oligosaccharide attachment sites	24:55	oligosaccharide attachment sites	24:55	Amino-acid sequence and oligosaccharide attachment sites of human erythrocyte glycophorin.
1059087	0	36	theme	attachment	40:49	arg1	glycophorin					78:88	human erythrocyte glycophorin	60:88	human erythrocyte glycophorin	60:88	Amino-acid sequence and oligosaccharide attachment sites of human erythrocyte glycophorin.
1059087	5	37	dep	segment	746:752	arg1	i					728:728	i	728:728	i	728:728	These include (i) a glycosylated segment composed of approximately 64 residues from the NH2-terminus, (ii) a "hydrophobic" segment of approximately 32 nonpolar residues, and (iii) a COOH-terminal segment, composed of approximately 35 residues, which has an unusual concentration of hydrophilic amino acids.
1059087	4	38	theme	glycosylated	640:651	arg1	acids					659:663	glycosylated amino acids	640:663	glycosylated amino acids	640:663	Glycophorin appears to be organized into three distinct "domains" on the basis of the locations of glycosylated amino acids and the clustering of residues of similar type.
1059087	3	39	theme	each	401:404	arg1	location					389:396	The location	385:396	The location of each of these oligosaccharides	385:430	The location of each of these oligosaccharides and the complete amino-acid sequence of this molecular have been determined by Edman degradation techniques.
1059087	3	39	theme	each	401:404	arg1	sequence					460:467	the complete amino-acid sequence	436:467	the complete amino-acid sequence of this molecular	436:485	The location of each of these oligosaccharides and the complete amino-acid sequence of this molecular have been determined by Edman degradation techniques.
1059087	0	40	theme	erythrocyte	66:76	arg1	glycophorin					78:88	human erythrocyte glycophorin	60:88	human erythrocyte glycophorin	60:88	Amino-acid sequence and oligosaccharide attachment sites of human erythrocyte glycophorin.
1059087	5	41	theme	unusual	970:976	arg1	concentration					978:990	an unusual concentration	967:990	an unusual concentration	967:990	These include (i) a glycosylated segment composed of approximately 64 residues from the NH2-terminus, (ii) a "hydrophobic" segment of approximately 32 nonpolar residues, and (iii) a COOH-terminal segment, composed of approximately 35 residues, which has an unusual concentration of hydrophilic amino acids.
1059087	6	42	theme	intrinsic	1123:1131	arg1	proteins					1143:1150	the major "intrinsic" membrane proteins	1112:1150	the major "intrinsic" membrane proteins which has a transmembrane orientation	1112:1188	This unique structure is consistent with the earlier suggestions that glycophorin is one of the major "intrinsic" membrane proteins which has a transmembrane orientation.
1059087	2	43	theme	complex	345:351	arg1	unit					353:356	one more complex unit	336:356	one more complex unit	336:356	Fifteen oligosaccharides are linked to threonine/serine residues via O-glycosidic bonds, and one more complex unit is attached to asparagine.
1059087	6	44	contain	has	1158:1160	arg2	orientation					1178:1188	a transmembrane orientation	1162:1188	a transmembrane orientation	1162:1188	This unique structure is consistent with the earlier suggestions that glycophorin is one of the major "intrinsic" membrane proteins which has a transmembrane orientation.
1059087	6	44	contain	has	1158:1160	arg1	proteins					1143:1150	the major "intrinsic" membrane proteins	1112:1150	the major "intrinsic" membrane proteins which has a transmembrane orientation	1112:1188	This unique structure is consistent with the earlier suggestions that glycophorin is one of the major "intrinsic" membrane proteins which has a transmembrane orientation.
1059087	5	45	theme	hydrophilic	995:1005	arg1	acids					1013:1017	hydrophilic amino acids	995:1017	hydrophilic amino acids	995:1017	These include (i) a glycosylated segment composed of approximately 64 residues from the NH2-terminus, (ii) a "hydrophobic" segment of approximately 32 nonpolar residues, and (iii) a COOH-terminal segment, composed of approximately 35 residues, which has an unusual concentration of hydrophilic amino acids.
1059087	6	46	dep	suggestions	1073:1083	arg1	one					1105:1107	one	1105:1107	one	1105:1107	This unique structure is consistent with the earlier suggestions that glycophorin is one of the major "intrinsic" membrane proteins which has a transmembrane orientation.
1059087	6	46	dep	suggestions	1073:1083	arg1	proteins					1143:1150	the major "intrinsic" membrane proteins	1112:1150	the major "intrinsic" membrane proteins which has a transmembrane orientation	1112:1188	This unique structure is consistent with the earlier suggestions that glycophorin is one of the major "intrinsic" membrane proteins which has a transmembrane orientation.
1059087	1	47	theme	human	139:143	arg1	membrane					157:164	the human erythrocyte membrane	135:164	the human erythrocyte membrane	135:164	Glycophorin, the major sialoglycoprotein of the human erythrocyte membrane, is composed of 131 amino acids and an average of 16 oligosaccharide chains.
1059087	5	48	theme	COOH-terminal	895:907	arg1	segment					909:915	a COOH-terminal segment	893:915	a COOH-terminal segment	893:915	These include (i) a glycosylated segment composed of approximately 64 residues from the NH2-terminus, (ii) a "hydrophobic" segment of approximately 32 nonpolar residues, and (iii) a COOH-terminal segment, composed of approximately 35 residues, which has an unusual concentration of hydrophilic amino acids.
1059087	6	49	theme	major	1116:1120	arg1	proteins					1143:1150	the major "intrinsic" membrane proteins	1112:1150	the major "intrinsic" membrane proteins which has a transmembrane orientation	1112:1188	This unique structure is consistent with the earlier suggestions that glycophorin is one of the major "intrinsic" membrane proteins which has a transmembrane orientation.
1059087	5	50	theme	amino	1007:1011	arg1	acids					1013:1017	hydrophilic amino acids	995:1017	hydrophilic amino acids	995:1017	These include (i) a glycosylated segment composed of approximately 64 residues from the NH2-terminus, (ii) a "hydrophobic" segment of approximately 32 nonpolar residues, and (iii) a COOH-terminal segment, composed of approximately 35 residues, which has an unusual concentration of hydrophilic amino acids.
1059087	5	51	from	segment	836:842	arg1	residues					783:790	approximately 64 residues	766:790	approximately 64 residues from the NH2-terminus, (ii) a "hydrophobic" segment of approximately 32 nonpolar residues, and (iii) a COOH-terminal segment	766:915	These include (i) a glycosylated segment composed of approximately 64 residues from the NH2-terminus, (ii) a "hydrophobic" segment of approximately 32 nonpolar residues, and (iii) a COOH-terminal segment, composed of approximately 35 residues, which has an unusual concentration of hydrophilic amino acids.
1059087	1	52	theme	erythrocyte	145:155	arg1	membrane					157:164	the human erythrocyte membrane	135:164	the human erythrocyte membrane	135:164	Glycophorin, the major sialoglycoprotein of the human erythrocyte membrane, is composed of 131 amino acids and an average of 16 oligosaccharide chains.
1059087	1	53	theme	oligosaccharide	219:233	arg1	chains					235:240	16 oligosaccharide chains	216:240	16 oligosaccharide chains	216:240	Glycophorin, the major sialoglycoprotein of the human erythrocyte membrane, is composed of 131 amino acids and an average of 16 oligosaccharide chains.
1059087	0	54	theme	glycophorin	78:88	arg1	sites					51:55	oligosaccharide attachment sites	24:55	oligosaccharide attachment sites	24:55	Amino-acid sequence and oligosaccharide attachment sites of human erythrocyte glycophorin.
1059087	0	54	theme	glycophorin	78:88	arg1	sequence					11:18	Amino-acid sequence	0:18	Amino-acid sequence	0:18	Amino-acid sequence and oligosaccharide attachment sites of human erythrocyte glycophorin.
1059087	0	54	theme	glycophorin	78:88	arg1	glycophorin					78:88	human erythrocyte glycophorin	60:88	human erythrocyte glycophorin	60:88	Amino-acid sequence and oligosaccharide attachment sites of human erythrocyte glycophorin.
1059087	6	55	theme	proteins	1143:1150	arg1	one					1105:1107	one	1105:1107	one	1105:1107	This unique structure is consistent with the earlier suggestions that glycophorin is one of the major "intrinsic" membrane proteins which has a transmembrane orientation.
1059087	6	55	theme	proteins	1143:1150	arg1	proteins					1143:1150	the major "intrinsic" membrane proteins	1112:1150	the major "intrinsic" membrane proteins which has a transmembrane orientation	1112:1188	This unique structure is consistent with the earlier suggestions that glycophorin is one of the major "intrinsic" membrane proteins which has a transmembrane orientation.
1059087	1	56	theme	membrane	157:164	arg1	Glycophorin					91:101	Glycophorin	91:101	Glycophorin	91:101	Glycophorin, the major sialoglycoprotein of the human erythrocyte membrane, is composed of 131 amino acids and an average of 16 oligosaccharide chains.
1059087	1	56	theme	membrane	157:164	arg1	sialoglycoprotein					114:130	the major sialoglycoprotein	104:130	the major sialoglycoprotein of the human erythrocyte membrane	104:164	Glycophorin, the major sialoglycoprotein of the human erythrocyte membrane, is composed of 131 amino acids and an average of 16 oligosaccharide chains.
1059087	4	57	theme	acids	659:663	arg1	locations					627:635	the locations	623:635	the locations of glycosylated amino acids	623:663	Glycophorin appears to be organized into three distinct "domains" on the basis of the locations of glycosylated amino acids and the clustering of residues of similar type.
1059087	1	58	theme	chains	235:240	arg1	acids					192:196	131 amino acids	182:196	131 amino acids	182:196	Glycophorin, the major sialoglycoprotein of the human erythrocyte membrane, is composed of 131 amino acids and an average of 16 oligosaccharide chains.
1059087	1	58	theme	chains	235:240	arg1	average					205:211	an average	202:211	an average of 16 oligosaccharide chains	202:240	Glycophorin, the major sialoglycoprotein of the human erythrocyte membrane, is composed of 131 amino acids and an average of 16 oligosaccharide chains.
1059087	0	59	theme	human	60:64	arg1	glycophorin					78:88	human erythrocyte glycophorin	60:88	human erythrocyte glycophorin	60:88	Amino-acid sequence and oligosaccharide attachment sites of human erythrocyte glycophorin.
1059087	6	60	theme	membrane	1134:1141	arg1	proteins					1143:1150	the major "intrinsic" membrane proteins	1112:1150	the major "intrinsic" membrane proteins which has a transmembrane orientation	1112:1188	This unique structure is consistent with the earlier suggestions that glycophorin is one of the major "intrinsic" membrane proteins which has a transmembrane orientation.
1737041	2	0	theme	Human	382:386	arg1	GM-CSF					388:393	Human GM-CSF	382:393	Human GM-CSF	382:393	Human GM-CSF contains two N-linked carbohydrate side chains of the complex acidic type and several sites of O-linked carbohydrate clustered on serine and threonine residues near the N-terminus of the molecule.
1737041	7	1	theme	roles	1457:1461	arg1	range					1448:1452	the range	1444:1452	the range of roles played by carbohydrate modification in the biosynthesis, assembly, and secretion of glycoprotein hormones	1444:1567	These studies help to point out the range of roles played by carbohydrate modification in the biosynthesis, assembly, and secretion of glycoprotein hormones.
1737041	5	2	from	those	1156:1160	arg1	indistinguishable					1133:1149	indistinguishable	1133:1149	indistinguishable	1133:1149	Unlike a number of other secreted glycoproteins, the transient time and secretory efficiency of several carbohydrate-deficient mutants of GM-CSF are indistinguishable from those of the native growth factor in BHK, 293, COS, and ldlD cells.
1737041	4	3	theme	modification	914:925	arg1	role					893:896	the role	889:896	the role of carbohydrate modification in the biosynthesis and secretion of GM-CSF	889:969	Using permanent cell lines and transient expression systems which produce moderate to high levels of native or carbohydrate-deficient forms of the growth factor, the role of carbohydrate modification in the biosynthesis and secretion of GM-CSF was studied.
1737041	5	4	dep	time	1047:1050	arg1	the					1033:1035	the	1033:1035	the	1033:1035	Unlike a number of other secreted glycoproteins, the transient time and secretory efficiency of several carbohydrate-deficient mutants of GM-CSF are indistinguishable from those of the native growth factor in BHK, 293, COS, and ldlD cells.
1737041	3	5	theme	significant	633:643	arg1	role					656:659	a significant functional role	631:659	a significant functional role for the carbohydrate modification characteristic of human GM-CSF	631:724	Previous studies have failed to detect a significant functional role for the carbohydrate modification characteristic of human GM-CSF.
1737041	0	6	from	secretion	56:64	arg1	cells					173:177	normal mesenchymal cells	154:177	normal mesenchymal cells	154:177	Role of carbohydrate modification in the production and secretion of human granulocyte macrophage colony-stimulating factor in genetically engineered and normal mesenchymal cells.
1737041	0	6	from	secretion	56:64	arg1	engineered					139:148	engineered	139:148	engineered	139:148	Role of carbohydrate modification in the production and secretion of human granulocyte macrophage colony-stimulating factor in genetically engineered and normal mesenchymal cells.
1737041	4	7	theme	expression	768:777	arg1	systems					779:785	transient expression systems	758:785	transient expression systems	758:785	Using permanent cell lines and transient expression systems which produce moderate to high levels of native or carbohydrate-deficient forms of the growth factor, the role of carbohydrate modification in the biosynthesis and secretion of GM-CSF was studied.
1737041	0	8	theme	mesenchymal	161:171	arg1	cells					173:177	normal mesenchymal cells	154:177	normal mesenchymal cells	154:177	Role of carbohydrate modification in the production and secretion of human granulocyte macrophage colony-stimulating factor in genetically engineered and normal mesenchymal cells.
1737041	1	9	dep	proliferation	270:282	arg1	the					266:268	the	266:268	the	266:268	Colony-stimulating factors (CSFs) are a group of acidic glycoproteins which stimulate the proliferation and differentiation of hematopoietic progenitor cells in vitro and stimulate hemopoiesis in vivo.
1737041	6	10	theme	human	1244:1248	arg1	cells					1262:1266	normal human endothelial cells	1237:1266	normal human endothelial cells	1237:1266	Furthermore, normal human endothelial cells and fibroblasts, which normally produce the growth factor, can synthesize and secrete GM-CSF that lacks all forms of carbohydrate modification.
1737041	4	11	theme	cell	743:746	arg1	lines					748:752	permanent cell lines	733:752	permanent cell lines	733:752	Using permanent cell lines and transient expression systems which produce moderate to high levels of native or carbohydrate-deficient forms of the growth factor, the role of carbohydrate modification in the biosynthesis and secretion of GM-CSF was studied.
1737041	5	12	theme	BHK	1193:1195	arg1	COS					1203:1205	BHK, 293, COS, and ldlD cells	1193:1221	COS	1203:1205	Unlike a number of other secreted glycoproteins, the transient time and secretory efficiency of several carbohydrate-deficient mutants of GM-CSF are indistinguishable from those of the native growth factor in BHK, 293, COS, and ldlD cells.
1737041	0	13	theme	human	69:73	arg1	factor					117:122	human granulocyte macrophage colony-stimulating factor	69:122	human granulocyte macrophage colony-stimulating factor	69:122	Role of carbohydrate modification in the production and secretion of human granulocyte macrophage colony-stimulating factor in genetically engineered and normal mesenchymal cells.
1737041	1	14	gly	glycoproteins	236:248	arg1	glycoproteins					236:248	acidic glycoproteins	229:248	acidic glycoproteins which stimulate the proliferation and differentiation of hematopoietic progenitor cells in vitro and stimulate hemopoiesis in vivo	229:379	Colony-stimulating factors (CSFs) are a group of acidic glycoproteins which stimulate the proliferation and differentiation of hematopoietic progenitor cells in vitro and stimulate hemopoiesis in vivo.
1737041	1	15	theme	Colony-stimulating	180:197	arg1	CSFs					208:211	CSFs	208:211	CSFs	208:211	Colony-stimulating factors (CSFs) are a group of acidic glycoproteins which stimulate the proliferation and differentiation of hematopoietic progenitor cells in vitro and stimulate hemopoiesis in vivo.
1737041	1	15	theme	Colony-stimulating	180:197	arg1	factors					199:205	Colony-stimulating factors	180:205	Colony-stimulating factors (CSFs)	180:212	Colony-stimulating factors (CSFs) are a group of acidic glycoproteins which stimulate the proliferation and differentiation of hematopoietic progenitor cells in vitro and stimulate hemopoiesis in vivo.
1737041	1	15	theme	Colony-stimulating	180:197	arg1	group					220:224	a group	218:224	a group of acidic glycoproteins which stimulate the proliferation and differentiation of hematopoietic progenitor cells in vitro and stimulate hemopoiesis in vivo	218:379	Colony-stimulating factors (CSFs) are a group of acidic glycoproteins which stimulate the proliferation and differentiation of hematopoietic progenitor cells in vitro and stimulate hemopoiesis in vivo.
1737041	1	15	theme	Colony-stimulating	180:197	arg1	glycoproteins					236:248	acidic glycoproteins	229:248	acidic glycoproteins which stimulate the proliferation and differentiation of hematopoietic progenitor cells in vitro and stimulate hemopoiesis in vivo	229:379	Colony-stimulating factors (CSFs) are a group of acidic glycoproteins which stimulate the proliferation and differentiation of hematopoietic progenitor cells in vitro and stimulate hemopoiesis in vivo.
1737041	0	16	from	Role	0:3	arg1	secretion					56:64	secretion	56:64	secretion	56:64	Role of carbohydrate modification in the production and secretion of human granulocyte macrophage colony-stimulating factor in genetically engineered and normal mesenchymal cells.
1737041	0	16	from	Role	0:3	arg1	production					41:50	production	41:50	production	41:50	Role of carbohydrate modification in the production and secretion of human granulocyte macrophage colony-stimulating factor in genetically engineered and normal mesenchymal cells.
1737041	0	17	theme	macrophage	87:96	arg1	factor					117:122	human granulocyte macrophage colony-stimulating factor	69:122	human granulocyte macrophage colony-stimulating factor	69:122	Role of carbohydrate modification in the production and secretion of human granulocyte macrophage colony-stimulating factor in genetically engineered and normal mesenchymal cells.
1737041	5	18	theme	native	1169:1174	arg1	factor					1183:1188	the native growth factor	1165:1188	the native growth factor in BHK, 293, COS, and ldlD cells	1165:1221	Unlike a number of other secreted glycoproteins, the transient time and secretory efficiency of several carbohydrate-deficient mutants of GM-CSF are indistinguishable from those of the native growth factor in BHK, 293, COS, and ldlD cells.
1737041	0	19	from	production	41:50	arg1	cells					173:177	normal mesenchymal cells	154:177	normal mesenchymal cells	154:177	Role of carbohydrate modification in the production and secretion of human granulocyte macrophage colony-stimulating factor in genetically engineered and normal mesenchymal cells.
1737041	0	19	from	production	41:50	arg1	engineered					139:148	engineered	139:148	engineered	139:148	Role of carbohydrate modification in the production and secretion of human granulocyte macrophage colony-stimulating factor in genetically engineered and normal mesenchymal cells.
1737041	0	20	theme	factor	117:122	arg1	secretion					56:64	secretion	56:64	secretion	56:64	Role of carbohydrate modification in the production and secretion of human granulocyte macrophage colony-stimulating factor in genetically engineered and normal mesenchymal cells.
1737041	0	20	theme	factor	117:122	arg1	production					41:50	production	41:50	production	41:50	Role of carbohydrate modification in the production and secretion of human granulocyte macrophage colony-stimulating factor in genetically engineered and normal mesenchymal cells.
1737041	2	21	contain	contains	395:402	arg1	GM-CSF					388:393	Human GM-CSF	382:393	Human GM-CSF	382:393	Human GM-CSF contains two N-linked carbohydrate side chains of the complex acidic type and several sites of O-linked carbohydrate clustered on serine and threonine residues near the N-terminus of the molecule.
1737041	2	21	contain	contains	395:402	arg2	chains					435:440	two N-linked carbohydrate side chains	404:440	two N-linked carbohydrate side chains of the complex acidic type and several sites of O-linked carbohydrate clustered on serine and threonine residues near the N-terminus of the molecule	404:589	Human GM-CSF contains two N-linked carbohydrate side chains of the complex acidic type and several sites of O-linked carbohydrate clustered on serine and threonine residues near the N-terminus of the molecule.
1737041	2	22	dep	type	464:467	arg1	the					445:447	the	445:447	the	445:447	Human GM-CSF contains two N-linked carbohydrate side chains of the complex acidic type and several sites of O-linked carbohydrate clustered on serine and threonine residues near the N-terminus of the molecule.
1737041	5	23	theme	transient	1037:1045	arg1	time					1047:1050	transient time	1037:1050	transient time	1037:1050	Unlike a number of other secreted glycoproteins, the transient time and secretory efficiency of several carbohydrate-deficient mutants of GM-CSF are indistinguishable from those of the native growth factor in BHK, 293, COS, and ldlD cells.
1737041	2	24	theme	sites	481:485	arg1	chains					435:440	two N-linked carbohydrate side chains	404:440	two N-linked carbohydrate side chains of the complex acidic type and several sites of O-linked carbohydrate clustered on serine and threonine residues near the N-terminus of the molecule	404:589	Human GM-CSF contains two N-linked carbohydrate side chains of the complex acidic type and several sites of O-linked carbohydrate clustered on serine and threonine residues near the N-terminus of the molecule.
1737041	4	25	theme	moderate	801:808	arg1	levels					818:823	moderate to high levels	801:823	moderate to high levels of native or carbohydrate-deficient forms of the growth factor	801:886	Using permanent cell lines and transient expression systems which produce moderate to high levels of native or carbohydrate-deficient forms of the growth factor, the role of carbohydrate modification in the biosynthesis and secretion of GM-CSF was studied.
1737041	2	26	theme	carbohydrate	417:428	arg1	chains					435:440	two N-linked carbohydrate side chains	404:440	two N-linked carbohydrate side chains of the complex acidic type and several sites of O-linked carbohydrate clustered on serine and threonine residues near the N-terminus of the molecule	404:589	Human GM-CSF contains two N-linked carbohydrate side chains of the complex acidic type and several sites of O-linked carbohydrate clustered on serine and threonine residues near the N-terminus of the molecule.
1737041	4	27	theme	high	813:816	arg1	levels					818:823	moderate to high levels	801:823	moderate to high levels of native or carbohydrate-deficient forms of the growth factor	801:886	Using permanent cell lines and transient expression systems which produce moderate to high levels of native or carbohydrate-deficient forms of the growth factor, the role of carbohydrate modification in the biosynthesis and secretion of GM-CSF was studied.
1737041	2	28	theme	acidic	457:462	arg1	type					464:467	complex acidic type	449:467	complex acidic type	449:467	Human GM-CSF contains two N-linked carbohydrate side chains of the complex acidic type and several sites of O-linked carbohydrate clustered on serine and threonine residues near the N-terminus of the molecule.
1737041	0	29	theme	carbohydrate	8:19	arg1	modification					21:32	carbohydrate modification	8:32	carbohydrate modification	8:32	Role of carbohydrate modification in the production and secretion of human granulocyte macrophage colony-stimulating factor in genetically engineered and normal mesenchymal cells.
1737041	1	30	theme	progenitor	321:330	arg1	cells					332:336	hematopoietic progenitor cells	307:336	hematopoietic progenitor cells	307:336	Colony-stimulating factors (CSFs) are a group of acidic glycoproteins which stimulate the proliferation and differentiation of hematopoietic progenitor cells in vitro and stimulate hemopoiesis in vivo.
1737041	5	31	theme	secreted	1009:1016	arg1	glycoproteins					1018:1030	other secreted glycoproteins	1003:1030	other secreted glycoproteins	1003:1030	Unlike a number of other secreted glycoproteins, the transient time and secretory efficiency of several carbohydrate-deficient mutants of GM-CSF are indistinguishable from those of the native growth factor in BHK, 293, COS, and ldlD cells.
1737041	2	32	link	N-linked	408:415	arg1	chains					435:440	two N-linked carbohydrate side chains	404:440	two N-linked carbohydrate side chains of the complex acidic type and several sites of O-linked carbohydrate clustered on serine and threonine residues near the N-terminus of the molecule	404:589	Human GM-CSF contains two N-linked carbohydrate side chains of the complex acidic type and several sites of O-linked carbohydrate clustered on serine and threonine residues near the N-terminus of the molecule.
1737041	4	33	theme	factor	881:886	arg1	forms					861:865	native or carbohydrate-deficient forms	828:865	native or carbohydrate-deficient forms of the growth factor	828:886	Using permanent cell lines and transient expression systems which produce moderate to high levels of native or carbohydrate-deficient forms of the growth factor, the role of carbohydrate modification in the biosynthesis and secretion of GM-CSF was studied.
1737041	4	34	dep	biosynthesis	934:945	arg1	the					930:932	the	930:932	the	930:932	Using permanent cell lines and transient expression systems which produce moderate to high levels of native or carbohydrate-deficient forms of the growth factor, the role of carbohydrate modification in the biosynthesis and secretion of GM-CSF was studied.
1737041	5	35	theme	several	1080:1086	arg1	mutants					1111:1117	several carbohydrate-deficient mutants	1080:1117	several carbohydrate-deficient mutants of GM-CSF	1080:1127	Unlike a number of other secreted glycoproteins, the transient time and secretory efficiency of several carbohydrate-deficient mutants of GM-CSF are indistinguishable from those of the native growth factor in BHK, 293, COS, and ldlD cells.
1737041	2	36	theme	O-linked	490:497	arg1	carbohydrate					499:510	O-linked carbohydrate	490:510	O-linked carbohydrate clustered on serine and threonine residues near the N-terminus of the molecule	490:589	Human GM-CSF contains two N-linked carbohydrate side chains of the complex acidic type and several sites of O-linked carbohydrate clustered on serine and threonine residues near the N-terminus of the molecule.
1737041	3	37	theme	modification	682:693	arg1	characteristic					695:708	the carbohydrate modification characteristic	665:708	the carbohydrate modification characteristic of human GM-CSF	665:724	Previous studies have failed to detect a significant functional role for the carbohydrate modification characteristic of human GM-CSF.
1737041	7	38	theme	glycoprotein	1547:1558	arg1	hormones					1560:1567	glycoprotein hormones	1547:1567	glycoprotein hormones	1547:1567	These studies help to point out the range of roles played by carbohydrate modification in the biosynthesis, assembly, and secretion of glycoprotein hormones.
1737041	5	39	theme	mutants	1111:1117	arg1	time					1047:1050	transient time	1037:1050	transient time	1037:1050	Unlike a number of other secreted glycoproteins, the transient time and secretory efficiency of several carbohydrate-deficient mutants of GM-CSF are indistinguishable from those of the native growth factor in BHK, 293, COS, and ldlD cells.
1737041	5	39	theme	mutants	1111:1117	arg1	efficiency					1066:1075	secretory efficiency	1056:1075	secretory efficiency	1056:1075	Unlike a number of other secreted glycoproteins, the transient time and secretory efficiency of several carbohydrate-deficient mutants of GM-CSF are indistinguishable from those of the native growth factor in BHK, 293, COS, and ldlD cells.
1737041	4	40	theme	forms	861:865	arg1	levels					818:823	moderate to high levels	801:823	moderate to high levels of native or carbohydrate-deficient forms of the growth factor	801:886	Using permanent cell lines and transient expression systems which produce moderate to high levels of native or carbohydrate-deficient forms of the growth factor, the role of carbohydrate modification in the biosynthesis and secretion of GM-CSF was studied.
1737041	0	41	dep	production	41:50	arg1	the					37:39	the	37:39	the	37:39	Role of carbohydrate modification in the production and secretion of human granulocyte macrophage colony-stimulating factor in genetically engineered and normal mesenchymal cells.
1737041	1	42	theme	acidic	229:234	arg1	glycoproteins					236:248	acidic glycoproteins	229:248	acidic glycoproteins which stimulate the proliferation and differentiation of hematopoietic progenitor cells in vitro and stimulate hemopoiesis in vivo	229:379	Colony-stimulating factors (CSFs) are a group of acidic glycoproteins which stimulate the proliferation and differentiation of hematopoietic progenitor cells in vitro and stimulate hemopoiesis in vivo.
1737041	3	43	theme	GM-CSF	719:724	arg1	characteristic					695:708	the carbohydrate modification characteristic	665:708	the carbohydrate modification characteristic of human GM-CSF	665:724	Previous studies have failed to detect a significant functional role for the carbohydrate modification characteristic of human GM-CSF.
1737041	7	44	theme	carbohydrate	1473:1484	arg1	modification					1486:1497	carbohydrate modification	1473:1497	carbohydrate modification	1473:1497	These studies help to point out the range of roles played by carbohydrate modification in the biosynthesis, assembly, and secretion of glycoprotein hormones.
1737041	6	45	theme	growth	1312:1317	arg1	factor					1319:1324	the growth factor	1308:1324	the growth factor	1308:1324	Furthermore, normal human endothelial cells and fibroblasts, which normally produce the growth factor, can synthesize and secrete GM-CSF that lacks all forms of carbohydrate modification.
1737041	4	46	theme	carbohydrate	901:912	arg1	modification					914:925	carbohydrate modification	901:925	carbohydrate modification	901:925	Using permanent cell lines and transient expression systems which produce moderate to high levels of native or carbohydrate-deficient forms of the growth factor, the role of carbohydrate modification in the biosynthesis and secretion of GM-CSF was studied.
1737041	3	47	theme	Previous	592:599	arg1	studies					601:607	Previous studies	592:607	Previous studies	592:607	Previous studies have failed to detect a significant functional role for the carbohydrate modification characteristic of human GM-CSF.
1737041	2	48	theme	molecule	582:589	arg1	N-terminus					564:573	the N-terminus	560:573	the N-terminus of the molecule	560:589	Human GM-CSF contains two N-linked carbohydrate side chains of the complex acidic type and several sites of O-linked carbohydrate clustered on serine and threonine residues near the N-terminus of the molecule.
1737041	4	49	dep	levels	818:823	arg1	to					810:811	to	810:811	to	810:811	Using permanent cell lines and transient expression systems which produce moderate to high levels of native or carbohydrate-deficient forms of the growth factor, the role of carbohydrate modification in the biosynthesis and secretion of GM-CSF was studied.
1737041	0	50	theme	normal	154:159	arg1	cells					173:177	normal mesenchymal cells	154:177	normal mesenchymal cells	154:177	Role of carbohydrate modification in the production and secretion of human granulocyte macrophage colony-stimulating factor in genetically engineered and normal mesenchymal cells.
1737041	7	51	dep	biosynthesis	1506:1517	arg1	the					1502:1504	the	1502:1504	the	1502:1504	These studies help to point out the range of roles played by carbohydrate modification in the biosynthesis, assembly, and secretion of glycoprotein hormones.
1737041	4	52	theme	transient	758:766	arg1	systems					779:785	transient expression systems	758:785	transient expression systems	758:785	Using permanent cell lines and transient expression systems which produce moderate to high levels of native or carbohydrate-deficient forms of the growth factor, the role of carbohydrate modification in the biosynthesis and secretion of GM-CSF was studied.
1737041	5	53	theme	GM-CSF	1122:1127	arg1	mutants					1111:1117	several carbohydrate-deficient mutants	1080:1117	several carbohydrate-deficient mutants of GM-CSF	1080:1127	Unlike a number of other secreted glycoproteins, the transient time and secretory efficiency of several carbohydrate-deficient mutants of GM-CSF are indistinguishable from those of the native growth factor in BHK, 293, COS, and ldlD cells.
1737041	7	54	gly	glycoprotein	1547:1558	arg1	glycoprotein					1547:1558	glycoprotein hormones	1547:1567	glycoprotein hormones	1547:1567	These studies help to point out the range of roles played by carbohydrate modification in the biosynthesis, assembly, and secretion of glycoprotein hormones.
1737041	4	55	theme	GM-CSF	964:969	arg1	secretion					951:959	secretion	951:959	secretion	951:959	Using permanent cell lines and transient expression systems which produce moderate to high levels of native or carbohydrate-deficient forms of the growth factor, the role of carbohydrate modification in the biosynthesis and secretion of GM-CSF was studied.
1737041	4	55	theme	GM-CSF	964:969	arg1	biosynthesis					934:945	biosynthesis	934:945	biosynthesis	934:945	Using permanent cell lines and transient expression systems which produce moderate to high levels of native or carbohydrate-deficient forms of the growth factor, the role of carbohydrate modification in the biosynthesis and secretion of GM-CSF was studied.
1737041	6	56	theme	endothelial	1250:1260	arg1	cells					1262:1266	normal human endothelial cells	1237:1266	normal human endothelial cells	1237:1266	Furthermore, normal human endothelial cells and fibroblasts, which normally produce the growth factor, can synthesize and secrete GM-CSF that lacks all forms of carbohydrate modification.
1737041	3	57	theme	functional	645:654	arg1	role					656:659	a significant functional role	631:659	a significant functional role for the carbohydrate modification characteristic of human GM-CSF	631:724	Previous studies have failed to detect a significant functional role for the carbohydrate modification characteristic of human GM-CSF.
1737041	5	58	gly	glycoproteins	1018:1030	arg1	glycoproteins					1018:1030	other secreted glycoproteins	1003:1030	other secreted glycoproteins	1003:1030	Unlike a number of other secreted glycoproteins, the transient time and secretory efficiency of several carbohydrate-deficient mutants of GM-CSF are indistinguishable from those of the native growth factor in BHK, 293, COS, and ldlD cells.
1737041	6	59	theme	normal	1237:1242	arg1	cells					1262:1266	normal human endothelial cells	1237:1266	normal human endothelial cells	1237:1266	Furthermore, normal human endothelial cells and fibroblasts, which normally produce the growth factor, can synthesize and secrete GM-CSF that lacks all forms of carbohydrate modification.
1737041	4	60	theme	permanent	733:741	arg1	lines					748:752	permanent cell lines	733:752	permanent cell lines	733:752	Using permanent cell lines and transient expression systems which produce moderate to high levels of native or carbohydrate-deficient forms of the growth factor, the role of carbohydrate modification in the biosynthesis and secretion of GM-CSF was studied.
1737041	0	61	theme	granulocyte	75:85	arg1	factor					117:122	human granulocyte macrophage colony-stimulating factor	69:122	human granulocyte macrophage colony-stimulating factor	69:122	Role of carbohydrate modification in the production and secretion of human granulocyte macrophage colony-stimulating factor in genetically engineered and normal mesenchymal cells.
1737041	0	62	theme	colony-stimulating	98:115	arg1	factor					117:122	human granulocyte macrophage colony-stimulating factor	69:122	human granulocyte macrophage colony-stimulating factor	69:122	Role of carbohydrate modification in the production and secretion of human granulocyte macrophage colony-stimulating factor in genetically engineered and normal mesenchymal cells.
1737041	5	63	theme	glycoproteins	1018:1030	arg1	number					993:998	a number	991:998	a number of other secreted glycoproteins	991:1030	Unlike a number of other secreted glycoproteins, the transient time and secretory efficiency of several carbohydrate-deficient mutants of GM-CSF are indistinguishable from those of the native growth factor in BHK, 293, COS, and ldlD cells.
1737041	6	64	theme	modification	1398:1409	arg1	forms					1376:1380	all forms	1372:1380	all forms of carbohydrate modification	1372:1409	Furthermore, normal human endothelial cells and fibroblasts, which normally produce the growth factor, can synthesize and secrete GM-CSF that lacks all forms of carbohydrate modification.
1737041	5	65	theme	growth	1176:1181	arg1	factor					1183:1188	the native growth factor	1165:1188	the native growth factor in BHK, 293, COS, and ldlD cells	1165:1221	Unlike a number of other secreted glycoproteins, the transient time and secretory efficiency of several carbohydrate-deficient mutants of GM-CSF are indistinguishable from those of the native growth factor in BHK, 293, COS, and ldlD cells.
1737041	2	66	link	O-linked	490:497	arg1	carbohydrate					499:510	O-linked carbohydrate	490:510	O-linked carbohydrate clustered on serine and threonine residues near the N-terminus of the molecule	490:589	Human GM-CSF contains two N-linked carbohydrate side chains of the complex acidic type and several sites of O-linked carbohydrate clustered on serine and threonine residues near the N-terminus of the molecule.
1737041	4	67	theme	native	828:833	arg1	forms					861:865	native or carbohydrate-deficient forms	828:865	native or carbohydrate-deficient forms of the growth factor	828:886	Using permanent cell lines and transient expression systems which produce moderate to high levels of native or carbohydrate-deficient forms of the growth factor, the role of carbohydrate modification in the biosynthesis and secretion of GM-CSF was studied.
1737041	2	68	theme	side	430:433	arg1	chains					435:440	two N-linked carbohydrate side chains	404:440	two N-linked carbohydrate side chains of the complex acidic type and several sites of O-linked carbohydrate clustered on serine and threonine residues near the N-terminus of the molecule	404:589	Human GM-CSF contains two N-linked carbohydrate side chains of the complex acidic type and several sites of O-linked carbohydrate clustered on serine and threonine residues near the N-terminus of the molecule.
1737041	5	69	from	factor	1183:1188	arg1	COS					1203:1205	BHK, 293, COS, and ldlD cells	1193:1221	COS	1203:1205	Unlike a number of other secreted glycoproteins, the transient time and secretory efficiency of several carbohydrate-deficient mutants of GM-CSF are indistinguishable from those of the native growth factor in BHK, 293, COS, and ldlD cells.
1737041	5	69	from	factor	1183:1188	arg1	cells					1217:1221	BHK, 293, COS, and ldlD cells	1193:1221	cells	1217:1221	Unlike a number of other secreted glycoproteins, the transient time and secretory efficiency of several carbohydrate-deficient mutants of GM-CSF are indistinguishable from those of the native growth factor in BHK, 293, COS, and ldlD cells.
1737041	4	70	from	role	893:896	arg1	secretion					951:959	secretion	951:959	secretion	951:959	Using permanent cell lines and transient expression systems which produce moderate to high levels of native or carbohydrate-deficient forms of the growth factor, the role of carbohydrate modification in the biosynthesis and secretion of GM-CSF was studied.
1737041	4	70	from	role	893:896	arg1	biosynthesis					934:945	biosynthesis	934:945	biosynthesis	934:945	Using permanent cell lines and transient expression systems which produce moderate to high levels of native or carbohydrate-deficient forms of the growth factor, the role of carbohydrate modification in the biosynthesis and secretion of GM-CSF was studied.
1737041	2	71	theme	several	473:479	arg1	sites					481:485	several sites	473:485	several sites	473:485	Human GM-CSF contains two N-linked carbohydrate side chains of the complex acidic type and several sites of O-linked carbohydrate clustered on serine and threonine residues near the N-terminus of the molecule.
1737041	2	71	theme	several	473:479	arg1	carbohydrate					499:510	O-linked carbohydrate	490:510	O-linked carbohydrate clustered on serine and threonine residues near the N-terminus of the molecule	490:589	Human GM-CSF contains two N-linked carbohydrate side chains of the complex acidic type and several sites of O-linked carbohydrate clustered on serine and threonine residues near the N-terminus of the molecule.
1737041	2	72	theme	N-linked	408:415	arg1	chains					435:440	two N-linked carbohydrate side chains	404:440	two N-linked carbohydrate side chains of the complex acidic type and several sites of O-linked carbohydrate clustered on serine and threonine residues near the N-terminus of the molecule	404:589	Human GM-CSF contains two N-linked carbohydrate side chains of the complex acidic type and several sites of O-linked carbohydrate clustered on serine and threonine residues near the N-terminus of the molecule.
1737041	0	73	theme	modification	21:32	arg1	Role					0:3	Role	0:3	Role of carbohydrate modification in the production and secretion of human granulocyte macrophage colony-stimulating factor in genetically engineered and normal mesenchymal cells.	0:178	Role of carbohydrate modification in the production and secretion of human granulocyte macrophage colony-stimulating factor in genetically engineered and normal mesenchymal cells.
1737041	1	74	theme	hematopoietic	307:319	arg1	cells					332:336	hematopoietic progenitor cells	307:336	hematopoietic progenitor cells	307:336	Colony-stimulating factors (CSFs) are a group of acidic glycoproteins which stimulate the proliferation and differentiation of hematopoietic progenitor cells in vitro and stimulate hemopoiesis in vivo.
1737041	5	75	theme	other	1003:1007	arg1	glycoproteins					1018:1030	other secreted glycoproteins	1003:1030	other secreted glycoproteins	1003:1030	Unlike a number of other secreted glycoproteins, the transient time and secretory efficiency of several carbohydrate-deficient mutants of GM-CSF are indistinguishable from those of the native growth factor in BHK, 293, COS, and ldlD cells.
1737041	2	76	theme	type	464:467	arg1	chains					435:440	two N-linked carbohydrate side chains	404:440	two N-linked carbohydrate side chains of the complex acidic type and several sites of O-linked carbohydrate clustered on serine and threonine residues near the N-terminus of the molecule	404:589	Human GM-CSF contains two N-linked carbohydrate side chains of the complex acidic type and several sites of O-linked carbohydrate clustered on serine and threonine residues near the N-terminus of the molecule.
1737041	2	77	theme	complex	449:455	arg1	type					464:467	complex acidic type	449:467	complex acidic type	449:467	Human GM-CSF contains two N-linked carbohydrate side chains of the complex acidic type and several sites of O-linked carbohydrate clustered on serine and threonine residues near the N-terminus of the molecule.
1737041	1	78	theme	cells	332:336	arg1	proliferation					270:282	proliferation	270:282	proliferation	270:282	Colony-stimulating factors (CSFs) are a group of acidic glycoproteins which stimulate the proliferation and differentiation of hematopoietic progenitor cells in vitro and stimulate hemopoiesis in vivo.
1737041	1	78	theme	cells	332:336	arg1	differentiation					288:302	differentiation	288:302	differentiation	288:302	Colony-stimulating factors (CSFs) are a group of acidic glycoproteins which stimulate the proliferation and differentiation of hematopoietic progenitor cells in vitro and stimulate hemopoiesis in vivo.
1737041	2	79	theme	carbohydrate	499:510	arg1	type					464:467	complex acidic type	449:467	complex acidic type	449:467	Human GM-CSF contains two N-linked carbohydrate side chains of the complex acidic type and several sites of O-linked carbohydrate clustered on serine and threonine residues near the N-terminus of the molecule.
1737041	2	79	theme	carbohydrate	499:510	arg1	sites					481:485	several sites	473:485	several sites	473:485	Human GM-CSF contains two N-linked carbohydrate side chains of the complex acidic type and several sites of O-linked carbohydrate clustered on serine and threonine residues near the N-terminus of the molecule.
1737041	2	79	theme	carbohydrate	499:510	arg1	carbohydrate					499:510	O-linked carbohydrate	490:510	O-linked carbohydrate clustered on serine and threonine residues near the N-terminus of the molecule	490:589	Human GM-CSF contains two N-linked carbohydrate side chains of the complex acidic type and several sites of O-linked carbohydrate clustered on serine and threonine residues near the N-terminus of the molecule.
1737041	3	80	theme	carbohydrate	669:680	arg1	characteristic					695:708	the carbohydrate modification characteristic	665:708	the carbohydrate modification characteristic of human GM-CSF	665:724	Previous studies have failed to detect a significant functional role for the carbohydrate modification characteristic of human GM-CSF.
1737041	4	81	theme	growth	874:879	arg1	factor					881:886	the growth factor	870:886	the growth factor	870:886	Using permanent cell lines and transient expression systems which produce moderate to high levels of native or carbohydrate-deficient forms of the growth factor, the role of carbohydrate modification in the biosynthesis and secretion of GM-CSF was studied.
1737041	6	82	theme	carbohydrate	1385:1396	arg1	modification					1398:1409	carbohydrate modification	1385:1409	carbohydrate modification	1385:1409	Furthermore, normal human endothelial cells and fibroblasts, which normally produce the growth factor, can synthesize and secrete GM-CSF that lacks all forms of carbohydrate modification.
1737041	2	83	dep	serine	525:530	arg1	residues					546:553	residues	546:553	residues	546:553	Human GM-CSF contains two N-linked carbohydrate side chains of the complex acidic type and several sites of O-linked carbohydrate clustered on serine and threonine residues near the N-terminus of the molecule.
1737041	5	84	theme	carbohydrate-deficient	1088:1109	arg1	mutants					1111:1117	several carbohydrate-deficient mutants	1080:1117	several carbohydrate-deficient mutants of GM-CSF	1080:1127	Unlike a number of other secreted glycoproteins, the transient time and secretory efficiency of several carbohydrate-deficient mutants of GM-CSF are indistinguishable from those of the native growth factor in BHK, 293, COS, and ldlD cells.
1737041	5	85	theme	ldlD	1212:1215	arg1	cells					1217:1221	BHK, 293, COS, and ldlD cells	1193:1221	cells	1217:1221	Unlike a number of other secreted glycoproteins, the transient time and secretory efficiency of several carbohydrate-deficient mutants of GM-CSF are indistinguishable from those of the native growth factor in BHK, 293, COS, and ldlD cells.
1737041	7	86	theme	hormones	1560:1567	arg1	assembly					1520:1527	assembly	1520:1527	assembly	1520:1527	These studies help to point out the range of roles played by carbohydrate modification in the biosynthesis, assembly, and secretion of glycoprotein hormones.
1737041	7	86	theme	hormones	1560:1567	arg1	secretion					1534:1542	secretion	1534:1542	secretion	1534:1542	These studies help to point out the range of roles played by carbohydrate modification in the biosynthesis, assembly, and secretion of glycoprotein hormones.
1737041	7	86	theme	hormones	1560:1567	arg1	biosynthesis					1506:1517	biosynthesis	1506:1517	biosynthesis	1506:1517	These studies help to point out the range of roles played by carbohydrate modification in the biosynthesis, assembly, and secretion of glycoprotein hormones.
1737041	3	87	theme	human	713:717	arg1	GM-CSF					719:724	human GM-CSF	713:724	human GM-CSF	713:724	Previous studies have failed to detect a significant functional role for the carbohydrate modification characteristic of human GM-CSF.
1737041	4	88	theme	carbohydrate-deficient	838:859	arg1	forms					861:865	native or carbohydrate-deficient forms	828:865	native or carbohydrate-deficient forms of the growth factor	828:886	Using permanent cell lines and transient expression systems which produce moderate to high levels of native or carbohydrate-deficient forms of the growth factor, the role of carbohydrate modification in the biosynthesis and secretion of GM-CSF was studied.
1737041	1	89	theme	glycoproteins	236:248	arg1	factors					199:205	Colony-stimulating factors	180:205	Colony-stimulating factors (CSFs)	180:212	Colony-stimulating factors (CSFs) are a group of acidic glycoproteins which stimulate the proliferation and differentiation of hematopoietic progenitor cells in vitro and stimulate hemopoiesis in vivo.
1737041	1	89	theme	glycoproteins	236:248	arg1	group					220:224	a group	218:224	a group of acidic glycoproteins which stimulate the proliferation and differentiation of hematopoietic progenitor cells in vitro and stimulate hemopoiesis in vivo	218:379	Colony-stimulating factors (CSFs) are a group of acidic glycoproteins which stimulate the proliferation and differentiation of hematopoietic progenitor cells in vitro and stimulate hemopoiesis in vivo.
1737041	1	89	theme	glycoproteins	236:248	arg1	glycoproteins					236:248	acidic glycoproteins	229:248	acidic glycoproteins which stimulate the proliferation and differentiation of hematopoietic progenitor cells in vitro and stimulate hemopoiesis in vivo	229:379	Colony-stimulating factors (CSFs) are a group of acidic glycoproteins which stimulate the proliferation and differentiation of hematopoietic progenitor cells in vitro and stimulate hemopoiesis in vivo.
1737041	5	90	theme	secretory	1056:1064	arg1	efficiency					1066:1075	secretory efficiency	1056:1075	secretory efficiency	1056:1075	Unlike a number of other secreted glycoproteins, the transient time and secretory efficiency of several carbohydrate-deficient mutants of GM-CSF are indistinguishable from those of the native growth factor in BHK, 293, COS, and ldlD cells.
26190575	1	0	theme	lipid	163:167	arg1	ceramide					169:176	the apoptosis-associated lipid ceramide	138:176	the apoptosis-associated lipid ceramide	138:176	Neutral ceramidase (nCDase) catalyzes conversion of the apoptosis-associated lipid ceramide to sphingosine, the precursor for the proliferative factor sphingosine-1-phosphate.
26190575	3	1	theme	deep	511:514	arg1	pocket					541:546	a striking, 20-Å deep, hydrophobic active site pocket	494:546	pocket	541:546	Here, we present the 2.6-Å crystal structure of human nCDase in complex with phosphate that reveals a striking, 20-Å deep, hydrophobic active site pocket stabilized by a eukaryotic-specific subdomain not present in bacterial ceramidases.
26190575	3	2	attach	present	598:604	arg2	subdomain					584:592	a eukaryotic-specific subdomain	562:592	a eukaryotic-specific subdomain not present in bacterial ceramidases	562:629	Here, we present the 2.6-Å crystal structure of human nCDase in complex with phosphate that reveals a striking, 20-Å deep, hydrophobic active site pocket stabilized by a eukaryotic-specific subdomain not present in bacterial ceramidases.
26190575	3	2	attach	present	598:604	arg1	ceramidases					619:629	bacterial ceramidases	609:629	bacterial ceramidases	609:629	Here, we present the 2.6-Å crystal structure of human nCDase in complex with phosphate that reveals a striking, 20-Å deep, hydrophobic active site pocket stabilized by a eukaryotic-specific subdomain not present in bacterial ceramidases.
26190575	3	3	from	structure	429:437	arg1	complex					458:464	complex	458:464	complex with phosphate	458:479	Here, we present the 2.6-Å crystal structure of human nCDase in complex with phosphate that reveals a striking, 20-Å deep, hydrophobic active site pocket stabilized by a eukaryotic-specific subdomain not present in bacterial ceramidases.
26190575	4	4	theme	transition	778:787	arg1	analog					795:800	the crystallographically observed transition state analog	744:800	the crystallographically observed transition state analog phosphate	744:810	Utilizing flexible ligand docking, we predict a likely binding mode for ceramide that superimposes closely with the crystallographically observed transition state analog phosphate.
26190575	1	5	theme	ceramide	169:176	arg1	conversion					124:133	conversion	124:133	conversion of the apoptosis-associated lipid ceramide to sphingosine	124:191	Neutral ceramidase (nCDase) catalyzes conversion of the apoptosis-associated lipid ceramide to sphingosine, the precursor for the proliferative factor sphingosine-1-phosphate.
26190575	1	5	theme	ceramide	169:176	arg1	precursor					198:206	the precursor	194:206	the precursor for the proliferative factor sphingosine-1-phosphate	194:259	Neutral ceramidase (nCDase) catalyzes conversion of the apoptosis-associated lipid ceramide to sphingosine, the precursor for the proliferative factor sphingosine-1-phosphate.
26190575	3	6	theme	eukaryotic-specific	564:582	arg1	subdomain					584:592	a eukaryotic-specific subdomain	562:592	a eukaryotic-specific subdomain not present in bacterial ceramidases	562:629	Here, we present the 2.6-Å crystal structure of human nCDase in complex with phosphate that reveals a striking, 20-Å deep, hydrophobic active site pocket stabilized by a eukaryotic-specific subdomain not present in bacterial ceramidases.
26190575	2	7	theme	ceramide	301:308	arg1	balance					290:296	the balance	286:296	the balance of ceramide and sphingosine-1-phosphate	286:336	As an enzyme regulating the balance of ceramide and sphingosine-1-phosphate, nCDase is emerging as a therapeutic target for cancer.
26190575	3	8	theme	20-Å	506:509	arg1	pocket					541:546	a striking, 20-Å deep, hydrophobic active site pocket	494:546	pocket	541:546	Here, we present the 2.6-Å crystal structure of human nCDase in complex with phosphate that reveals a striking, 20-Å deep, hydrophobic active site pocket stabilized by a eukaryotic-specific subdomain not present in bacterial ceramidases.
26190575	3	9	from	ceramidases	619:629	arg1	present					598:604	present	598:604	present	598:604	Here, we present the 2.6-Å crystal structure of human nCDase in complex with phosphate that reveals a striking, 20-Å deep, hydrophobic active site pocket stabilized by a eukaryotic-specific subdomain not present in bacterial ceramidases.
26190575	6	10	theme	common	1153:1158	arg1	themes					1160:1165	common themes	1153:1165	common themes	1153:1165	Together, these data provide a foundation to aid drug development and establish common themes for how proteins recognize the bioactive lipid ceramide.
26190575	2	11	theme	therapeutic	363:373	arg1	target					375:380	a therapeutic target	361:380	a therapeutic target for cancer	361:391	As an enzyme regulating the balance of ceramide and sphingosine-1-phosphate, nCDase is emerging as a therapeutic target for cancer.
26190575	4	12	theme	observed	769:776	arg1	analog					795:800	the crystallographically observed transition state analog	744:800	the crystallographically observed transition state analog phosphate	744:810	Utilizing flexible ligand docking, we predict a likely binding mode for ceramide that superimposes closely with the crystallographically observed transition state analog phosphate.
26190575	3	13	theme	active	529:534	arg1	pocket					541:546	a striking, 20-Å deep, hydrophobic active site pocket	494:546	pocket	541:546	Here, we present the 2.6-Å crystal structure of human nCDase in complex with phosphate that reveals a striking, 20-Å deep, hydrophobic active site pocket stabilized by a eukaryotic-specific subdomain not present in bacterial ceramidases.
26190575	5	14	theme	-dependent	885:894	arg1	amidases					896:903	Zn(2+)-dependent amidases	879:903	Zn(2+)-dependent amidases	879:903	Our results suggest that nCDase uses a new catalytic strategy for Zn(2+)-dependent amidases, and generates ceramide specificity by sterically excluding sphingolipids with bulky headgroups and specifically recognizing the small hydroxyl head group of ceramide.
26190575	3	15	theme	nCDase	448:453	arg1	structure					429:437	the 2.6-Å crystal structure	411:437	the 2.6-Å crystal structure of human nCDase in complex with phosphate that reveals a striking, 20-Å deep, hydrophobic active site pocket stabilized by a eukaryotic-specific subdomain not present in bacterial ceramidases	411:629	Here, we present the 2.6-Å crystal structure of human nCDase in complex with phosphate that reveals a striking, 20-Å deep, hydrophobic active site pocket stabilized by a eukaryotic-specific subdomain not present in bacterial ceramidases.
26190575	5	16	theme	ceramide	920:927	arg1	specificity					929:939	ceramide specificity	920:939	ceramide specificity	920:939	Our results suggest that nCDase uses a new catalytic strategy for Zn(2+)-dependent amidases, and generates ceramide specificity by sterically excluding sphingolipids with bulky headgroups and specifically recognizing the small hydroxyl head group of ceramide.
26190575	3	17	theme	site	536:539	arg1	pocket					541:546	a striking, 20-Å deep, hydrophobic active site pocket	494:546	pocket	541:546	Here, we present the 2.6-Å crystal structure of human nCDase in complex with phosphate that reveals a striking, 20-Å deep, hydrophobic active site pocket stabilized by a eukaryotic-specific subdomain not present in bacterial ceramidases.
26190575	6	18	theme	drug	1122:1125	arg1	development					1127:1137	drug development	1122:1137	drug development	1122:1137	Together, these data provide a foundation to aid drug development and establish common themes for how proteins recognize the bioactive lipid ceramide.
26190575	6	19	theme	bioactive	1198:1206	arg1	ceramide					1214:1221	the bioactive lipid ceramide	1194:1221	the bioactive lipid ceramide	1194:1221	Together, these data provide a foundation to aid drug development and establish common themes for how proteins recognize the bioactive lipid ceramide.
26190575	1	20	theme	Neutral	86:92	arg1	ceramidase					94:103	Neutral ceramidase	86:103	Neutral ceramidase (nCDase)	86:112	Neutral ceramidase (nCDase) catalyzes conversion of the apoptosis-associated lipid ceramide to sphingosine, the precursor for the proliferative factor sphingosine-1-phosphate.
26190575	1	20	theme	Neutral	86:92	arg1	nCDase					106:111	nCDase	106:111	nCDase	106:111	Neutral ceramidase (nCDase) catalyzes conversion of the apoptosis-associated lipid ceramide to sphingosine, the precursor for the proliferative factor sphingosine-1-phosphate.
26190575	4	21	theme	binding	687:693	arg1	mode					695:698	a likely binding mode	678:698	a likely binding mode for ceramide that superimposes closely with the crystallographically observed transition state analog phosphate	678:810	Utilizing flexible ligand docking, we predict a likely binding mode for ceramide that superimposes closely with the crystallographically observed transition state analog phosphate.
26190575	0	22	theme	Structural	0:9	arg1	Basis					11:15	Structural Basis	0:15	Structural Basis for Ceramide Recognition and Hydrolysis by Human Neutral Ceramidase.	0:84	Structural Basis for Ceramide Recognition and Hydrolysis by Human Neutral Ceramidase.
26190575	3	23	theme	human	442:446	arg1	nCDase					448:453	human nCDase	442:453	human nCDase in complex with phosphate	442:479	Here, we present the 2.6-Å crystal structure of human nCDase in complex with phosphate that reveals a striking, 20-Å deep, hydrophobic active site pocket stabilized by a eukaryotic-specific subdomain not present in bacterial ceramidases.
26190575	0	24	theme	Ceramide	21:28	arg1	Recognition					30:40	Ceramide Recognition	21:40	Ceramide Recognition	21:40	Structural Basis for Ceramide Recognition and Hydrolysis by Human Neutral Ceramidase.
26190575	3	25	with	complex	458:464	arg1	phosphate					471:479	phosphate	471:479	phosphate	471:479	Here, we present the 2.6-Å crystal structure of human nCDase in complex with phosphate that reveals a striking, 20-Å deep, hydrophobic active site pocket stabilized by a eukaryotic-specific subdomain not present in bacterial ceramidases.
26190575	4	26	theme	state	789:793	arg1	analog					795:800	the crystallographically observed transition state analog	744:800	the crystallographically observed transition state analog phosphate	744:810	Utilizing flexible ligand docking, we predict a likely binding mode for ceramide that superimposes closely with the crystallographically observed transition state analog phosphate.
26190575	3	27	from	present	598:604	arg1	ceramidases					619:629	bacterial ceramidases	609:629	bacterial ceramidases	609:629	Here, we present the 2.6-Å crystal structure of human nCDase in complex with phosphate that reveals a striking, 20-Å deep, hydrophobic active site pocket stabilized by a eukaryotic-specific subdomain not present in bacterial ceramidases.
26190575	5	28	theme	catalytic	856:864	arg1	strategy					866:873	a new catalytic strategy	850:873	a new catalytic strategy for Zn(2+)-dependent amidases	850:903	Our results suggest that nCDase uses a new catalytic strategy for Zn(2+)-dependent amidases, and generates ceramide specificity by sterically excluding sphingolipids with bulky headgroups and specifically recognizing the small hydroxyl head group of ceramide.
26190575	2	29	theme	sphingosine-1-phosphate	314:336	arg1	balance					290:296	the balance	286:296	the balance of ceramide and sphingosine-1-phosphate	286:336	As an enzyme regulating the balance of ceramide and sphingosine-1-phosphate, nCDase is emerging as a therapeutic target for cancer.
26190575	4	30	theme	ligand	651:656	arg1	docking					658:664	flexible ligand docking	642:664	flexible ligand docking	642:664	Utilizing flexible ligand docking, we predict a likely binding mode for ceramide that superimposes closely with the crystallographically observed transition state analog phosphate.
26190575	3	31	theme	crystal	421:427	arg1	structure					429:437	the 2.6-Å crystal structure	411:437	the 2.6-Å crystal structure of human nCDase in complex with phosphate that reveals a striking, 20-Å deep, hydrophobic active site pocket stabilized by a eukaryotic-specific subdomain not present in bacterial ceramidases	411:629	Here, we present the 2.6-Å crystal structure of human nCDase in complex with phosphate that reveals a striking, 20-Å deep, hydrophobic active site pocket stabilized by a eukaryotic-specific subdomain not present in bacterial ceramidases.
26190575	4	32	theme	likely	680:685	arg1	mode					695:698	a likely binding mode	678:698	a likely binding mode for ceramide that superimposes closely with the crystallographically observed transition state analog phosphate	678:810	Utilizing flexible ligand docking, we predict a likely binding mode for ceramide that superimposes closely with the crystallographically observed transition state analog phosphate.
26190575	5	33	with	sphingolipids	965:977	arg1	headgroups					990:999	bulky headgroups	984:999	bulky headgroups	984:999	Our results suggest that nCDase uses a new catalytic strategy for Zn(2+)-dependent amidases, and generates ceramide specificity by sterically excluding sphingolipids with bulky headgroups and specifically recognizing the small hydroxyl head group of ceramide.
26190575	4	34	theme	analog	795:800	arg1	phosphate					802:810	the crystallographically observed transition state analog phosphate	744:810	the crystallographically observed transition state analog phosphate	744:810	Utilizing flexible ligand docking, we predict a likely binding mode for ceramide that superimposes closely with the crystallographically observed transition state analog phosphate.
26190575	3	35	theme	bacterial	609:617	arg1	ceramidases					619:629	bacterial ceramidases	609:629	bacterial ceramidases	609:629	Here, we present the 2.6-Å crystal structure of human nCDase in complex with phosphate that reveals a striking, 20-Å deep, hydrophobic active site pocket stabilized by a eukaryotic-specific subdomain not present in bacterial ceramidases.
26190575	3	36	from	complex	458:464	arg1	structure					429:437	the 2.6-Å crystal structure	411:437	the 2.6-Å crystal structure of human nCDase in complex with phosphate that reveals a striking, 20-Å deep, hydrophobic active site pocket stabilized by a eukaryotic-specific subdomain not present in bacterial ceramidases	411:629	Here, we present the 2.6-Å crystal structure of human nCDase in complex with phosphate that reveals a striking, 20-Å deep, hydrophobic active site pocket stabilized by a eukaryotic-specific subdomain not present in bacterial ceramidases.
26190575	1	37	theme	proliferative	216:228	arg1	sphingosine-1-phosphate					237:259	the proliferative factor sphingosine-1-phosphate	212:259	the proliferative factor sphingosine-1-phosphate	212:259	Neutral ceramidase (nCDase) catalyzes conversion of the apoptosis-associated lipid ceramide to sphingosine, the precursor for the proliferative factor sphingosine-1-phosphate.
26190575	5	38	theme	new	852:854	arg1	strategy					866:873	a new catalytic strategy	850:873	a new catalytic strategy for Zn(2+)-dependent amidases	850:903	Our results suggest that nCDase uses a new catalytic strategy for Zn(2+)-dependent amidases, and generates ceramide specificity by sterically excluding sphingolipids with bulky headgroups and specifically recognizing the small hydroxyl head group of ceramide.
26190575	3	39	theme	striking	496:503	arg1	pocket					541:546	a striking, 20-Å deep, hydrophobic active site pocket	494:546	pocket	541:546	Here, we present the 2.6-Å crystal structure of human nCDase in complex with phosphate that reveals a striking, 20-Å deep, hydrophobic active site pocket stabilized by a eukaryotic-specific subdomain not present in bacterial ceramidases.
26190575	3	40	theme	2.6-Å	415:419	arg1	structure					429:437	the 2.6-Å crystal structure	411:437	the 2.6-Å crystal structure of human nCDase in complex with phosphate that reveals a striking, 20-Å deep, hydrophobic active site pocket stabilized by a eukaryotic-specific subdomain not present in bacterial ceramidases	411:629	Here, we present the 2.6-Å crystal structure of human nCDase in complex with phosphate that reveals a striking, 20-Å deep, hydrophobic active site pocket stabilized by a eukaryotic-specific subdomain not present in bacterial ceramidases.
26190575	3	41	theme	present	598:604	arg1	subdomain					584:592	a eukaryotic-specific subdomain	562:592	a eukaryotic-specific subdomain not present in bacterial ceramidases	562:629	Here, we present the 2.6-Å crystal structure of human nCDase in complex with phosphate that reveals a striking, 20-Å deep, hydrophobic active site pocket stabilized by a eukaryotic-specific subdomain not present in bacterial ceramidases.
26190575	5	42	theme	small	1034:1038	arg1	ceramide					1063:1070	ceramide	1063:1070	ceramide	1063:1070	Our results suggest that nCDase uses a new catalytic strategy for Zn(2+)-dependent amidases, and generates ceramide specificity by sterically excluding sphingolipids with bulky headgroups and specifically recognizing the small hydroxyl head group of ceramide.
26190575	5	42	theme	small	1034:1038	arg1	group					1054:1058	the small hydroxyl head group	1030:1058	the small hydroxyl head group of ceramide	1030:1070	Our results suggest that nCDase uses a new catalytic strategy for Zn(2+)-dependent amidases, and generates ceramide specificity by sterically excluding sphingolipids with bulky headgroups and specifically recognizing the small hydroxyl head group of ceramide.
26190575	5	43	theme	ceramide	1063:1070	arg1	ceramide					1063:1070	ceramide	1063:1070	ceramide	1063:1070	Our results suggest that nCDase uses a new catalytic strategy for Zn(2+)-dependent amidases, and generates ceramide specificity by sterically excluding sphingolipids with bulky headgroups and specifically recognizing the small hydroxyl head group of ceramide.
26190575	5	43	theme	ceramide	1063:1070	arg1	group					1054:1058	the small hydroxyl head group	1030:1058	the small hydroxyl head group of ceramide	1030:1070	Our results suggest that nCDase uses a new catalytic strategy for Zn(2+)-dependent amidases, and generates ceramide specificity by sterically excluding sphingolipids with bulky headgroups and specifically recognizing the small hydroxyl head group of ceramide.
26190575	5	44	theme	bulky	984:988	arg1	headgroups					990:999	bulky headgroups	984:999	bulky headgroups	984:999	Our results suggest that nCDase uses a new catalytic strategy for Zn(2+)-dependent amidases, and generates ceramide specificity by sterically excluding sphingolipids with bulky headgroups and specifically recognizing the small hydroxyl head group of ceramide.
26190575	1	45	theme	factor	230:235	arg1	sphingosine-1-phosphate					237:259	the proliferative factor sphingosine-1-phosphate	212:259	the proliferative factor sphingosine-1-phosphate	212:259	Neutral ceramidase (nCDase) catalyzes conversion of the apoptosis-associated lipid ceramide to sphingosine, the precursor for the proliferative factor sphingosine-1-phosphate.
26190575	6	46	theme	lipid	1208:1212	arg1	ceramide					1214:1221	the bioactive lipid ceramide	1194:1221	the bioactive lipid ceramide	1194:1221	Together, these data provide a foundation to aid drug development and establish common themes for how proteins recognize the bioactive lipid ceramide.
26190575	5	47	theme	hydroxyl	1040:1047	arg1	ceramide					1063:1070	ceramide	1063:1070	ceramide	1063:1070	Our results suggest that nCDase uses a new catalytic strategy for Zn(2+)-dependent amidases, and generates ceramide specificity by sterically excluding sphingolipids with bulky headgroups and specifically recognizing the small hydroxyl head group of ceramide.
26190575	5	47	theme	hydroxyl	1040:1047	arg1	group					1054:1058	the small hydroxyl head group	1030:1058	the small hydroxyl head group of ceramide	1030:1070	Our results suggest that nCDase uses a new catalytic strategy for Zn(2+)-dependent amidases, and generates ceramide specificity by sterically excluding sphingolipids with bulky headgroups and specifically recognizing the small hydroxyl head group of ceramide.
26190575	3	48	theme	hydrophobic	517:527	arg1	pocket					541:546	a striking, 20-Å deep, hydrophobic active site pocket	494:546	pocket	541:546	Here, we present the 2.6-Å crystal structure of human nCDase in complex with phosphate that reveals a striking, 20-Å deep, hydrophobic active site pocket stabilized by a eukaryotic-specific subdomain not present in bacterial ceramidases.
26190575	0	49	theme	Neutral	66:72	arg1	Ceramidase					74:83	Human Neutral Ceramidase	60:83	Human Neutral Ceramidase	60:83	Structural Basis for Ceramide Recognition and Hydrolysis by Human Neutral Ceramidase.
26190575	5	50	theme	head	1049:1052	arg1	ceramide					1063:1070	ceramide	1063:1070	ceramide	1063:1070	Our results suggest that nCDase uses a new catalytic strategy for Zn(2+)-dependent amidases, and generates ceramide specificity by sterically excluding sphingolipids with bulky headgroups and specifically recognizing the small hydroxyl head group of ceramide.
26190575	5	50	theme	head	1049:1052	arg1	group					1054:1058	the small hydroxyl head group	1030:1058	the small hydroxyl head group of ceramide	1030:1070	Our results suggest that nCDase uses a new catalytic strategy for Zn(2+)-dependent amidases, and generates ceramide specificity by sterically excluding sphingolipids with bulky headgroups and specifically recognizing the small hydroxyl head group of ceramide.
26190575	4	51	theme	flexible	642:649	arg1	docking					658:664	flexible ligand docking	642:664	flexible ligand docking	642:664	Utilizing flexible ligand docking, we predict a likely binding mode for ceramide that superimposes closely with the crystallographically observed transition state analog phosphate.
26190575	0	52	theme	Human	60:64	arg1	Ceramidase					74:83	Human Neutral Ceramidase	60:83	Human Neutral Ceramidase	60:83	Structural Basis for Ceramide Recognition and Hydrolysis by Human Neutral Ceramidase.
26190575	3	53	from	nCDase	448:453	arg1	complex					458:464	complex	458:464	complex with phosphate	458:479	Here, we present the 2.6-Å crystal structure of human nCDase in complex with phosphate that reveals a striking, 20-Å deep, hydrophobic active site pocket stabilized by a eukaryotic-specific subdomain not present in bacterial ceramidases.
26190575	1	54	theme	apoptosis-associated	142:161	arg1	ceramide					169:176	the apoptosis-associated lipid ceramide	138:176	the apoptosis-associated lipid ceramide	138:176	Neutral ceramidase (nCDase) catalyzes conversion of the apoptosis-associated lipid ceramide to sphingosine, the precursor for the proliferative factor sphingosine-1-phosphate.
1381905	9	0	theme	acids	1675:1679	arg1	form					1657:1660	the initially synthesized membrane-bound form	1616:1660	the initially synthesized membrane-bound form of 248 amino acids	1616:1679	The data obtained indicate that the recombinant human stem cell factor, as isolated, represents proteolytically processed forms containing amino acids 1-165, derived from the initially synthesized membrane-bound form of 248 amino acids.
1381905	1	1	theme	CHO	263:265	arg1	cells					268:272	Chinese hamster ovary (CHO) cells	240:272	Chinese hamster ovary (CHO) cells transfected with stem cell factor (SCF) cDNA	240:317	This report describes the structure of soluble human stem cell factor isolated from the conditioned medium of Chinese hamster ovary (CHO) cells transfected with stem cell factor (SCF) cDNA, which encodes a leader sequence plus 248 additional amino acids.
1381905	3	2	theme	SDS	616:618	arg1	electrophoresis					640:654	sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis	592:654	sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis	592:654	The isolated material is glycosylated and three bands (apparent M(r) 28,000, M(r) 35,000, and M(r) 40,000) are evident by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis.
1381905	3	3	theme	apparent	525:532	arg1	r					536:536	r	536:536	r	536:536	The isolated material is glycosylated and three bands (apparent M(r) 28,000, M(r) 35,000, and M(r) 40,000) are evident by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis.
1381905	3	3	theme	apparent	525:532	arg1	bands					518:522	three bands	512:522	three bands (apparent M(r) 28,000, M(r) 35,000, and M(r) 40,000)	512:575	The isolated material is glycosylated and three bands (apparent M(r) 28,000, M(r) 35,000, and M(r) 40,000) are evident by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis.
1381905	3	3	theme	apparent	525:532	arg1	M					534:534	apparent M	525:534	apparent M	525:534	The isolated material is glycosylated and three bands (apparent M(r) 28,000, M(r) 35,000, and M(r) 40,000) are evident by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis.
1381905	1	4	theme	cells	268:272	arg1	acids					378:382	248 additional amino acids	357:382	248 additional amino acids	357:382	This report describes the structure of soluble human stem cell factor isolated from the conditioned medium of Chinese hamster ovary (CHO) cells transfected with stem cell factor (SCF) cDNA, which encodes a leader sequence plus 248 additional amino acids.
1381905	1	4	theme	cells	268:272	arg1	sequence					343:350	a leader sequence	334:350	a leader sequence	334:350	This report describes the structure of soluble human stem cell factor isolated from the conditioned medium of Chinese hamster ovary (CHO) cells transfected with stem cell factor (SCF) cDNA, which encodes a leader sequence plus 248 additional amino acids.
1381905	1	4	theme	cells	268:272	arg1	medium					230:235	the conditioned medium	214:235	the conditioned medium	214:235	This report describes the structure of soluble human stem cell factor isolated from the conditioned medium of Chinese hamster ovary (CHO) cells transfected with stem cell factor (SCF) cDNA, which encodes a leader sequence plus 248 additional amino acids.
1381905	3	5	theme	sulfate	607:613	arg1	electrophoresis					640:654	sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis	592:654	sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis	592:654	The isolated material is glycosylated and three bands (apparent M(r) 28,000, M(r) 35,000, and M(r) 40,000) are evident by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis.
1381905	1	6	theme	cell	188:191	arg1	factor					193:198	soluble human stem cell factor	169:198	soluble human stem cell factor isolated from the conditioned medium of Chinese hamster ovary (CHO) cells transfected with stem cell factor (SCF) cDNA, which encodes a leader sequence plus 248 additional amino acids	169:382	This report describes the structure of soluble human stem cell factor isolated from the conditioned medium of Chinese hamster ovary (CHO) cells transfected with stem cell factor (SCF) cDNA, which encodes a leader sequence plus 248 additional amino acids.
1381905	7	7	theme	35,000	1239:1244	arg1	SCF					1214:1216	labeled SCF	1206:1216	labeled SCF of M(r) 28,000, M(r) 35,000, and M(r) 40,000	1206:1261	During a chase with unlabeled Met and Cys, labeled SCF of M(r) 28,000, M(r) 35,000, and M(r) 40,000 appeared in the medium; it was converted to M(r) 18,000-19,000 by glycosidase treatment.
1381905	9	8	contain	containing	1573:1582	arg1	forms					1567:1571	proteolytically processed forms	1541:1571	proteolytically processed forms containing amino acids 1-165, derived from the initially synthesized membrane-bound form of 248 amino acids	1541:1679	The data obtained indicate that the recombinant human stem cell factor, as isolated, represents proteolytically processed forms containing amino acids 1-165, derived from the initially synthesized membrane-bound form of 248 amino acids.
1381905	9	8	contain	containing	1573:1582	arg2	acids					1590:1594	amino acids 1-165	1584:1600	amino acids 1-165	1584:1600	The data obtained indicate that the recombinant human stem cell factor, as isolated, represents proteolytically processed forms containing amino acids 1-165, derived from the initially synthesized membrane-bound form of 248 amino acids.
1381905	5	9	theme	SCF	804:806	arg1	analyses					781:788	Structural analyses	770:788	Structural analyses of the intact SCF, the deglycosylated SCF, and a deglycosylated C-terminal peptide	770:871	Structural analyses of the intact SCF, the deglycosylated SCF, and a deglycosylated C-terminal peptide were performed by laser desorption, fast atom bombardment, or electrospray mass spectrometry.
1381905	10	10	gly	glycosylated	1746:1757	arg2	Asn65					1859:1863	Asn65	1859:1863	Asn65	1859:1863	Further characterization indicated that the M(r) 28,000 form is glycosylated at Asn120, the M(r) 35,000 form at Asn120 and Asn65, and the M(r) 40,000 form at Asn120, Asn93, and Asn65.
1381905	10	10	gly	glycosylated	1746:1757	arg2	form					1832:1835	the M(r) 40,000 form	1816:1835	the M(r) 40,000 form	1816:1835	Further characterization indicated that the M(r) 28,000 form is glycosylated at Asn120, the M(r) 35,000 form at Asn120 and Asn65, and the M(r) 40,000 form at Asn120, Asn93, and Asn65.
1381905	10	10	gly	glycosylated	1746:1757	arg2	Asn120					1840:1845	Asn120	1840:1845	Asn120	1840:1845	Further characterization indicated that the M(r) 28,000 form is glycosylated at Asn120, the M(r) 35,000 form at Asn120 and Asn65, and the M(r) 40,000 form at Asn120, Asn93, and Asn65.
1381905	10	10	gly	glycosylated	1746:1757	arg2	Asn120					1762:1767	Asn120	1762:1767	Asn120	1762:1767	Further characterization indicated that the M(r) 28,000 form is glycosylated at Asn120, the M(r) 35,000 form at Asn120 and Asn65, and the M(r) 40,000 form at Asn120, Asn93, and Asn65.
1381905	10	10	gly	glycosylated	1746:1757	arg2	Asn93					1848:1852	Asn93	1848:1852	Asn93	1848:1852	Further characterization indicated that the M(r) 28,000 form is glycosylated at Asn120, the M(r) 35,000 form at Asn120 and Asn65, and the M(r) 40,000 form at Asn120, Asn93, and Asn65.
1381905	10	10	gly	glycosylated	1746:1757	arg1	form					1738:1741	the M(r) 28,000 form	1722:1741	the M(r) 28,000 form	1722:1741	Further characterization indicated that the M(r) 28,000 form is glycosylated at Asn120, the M(r) 35,000 form at Asn120 and Asn65, and the M(r) 40,000 form at Asn120, Asn93, and Asn65.
1381905	10	10	gly	glycosylated	1746:1757	arg2	form					1786:1789	the M(r) 35,000 form	1770:1789	the M(r) 35,000 form at Asn120 and Asn65	1770:1809	Further characterization indicated that the M(r) 28,000 form is glycosylated at Asn120, the M(r) 35,000 form at Asn120 and Asn65, and the M(r) 40,000 form at Asn120, Asn93, and Asn65.
1381905	3	11	theme	-polyacrylamide	620:634	arg1	electrophoresis					640:654	sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis	592:654	sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis	592:654	The isolated material is glycosylated and three bands (apparent M(r) 28,000, M(r) 35,000, and M(r) 40,000) are evident by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis.
1381905	1	12	theme	248	357:359	arg1	acids					378:382	248 additional amino acids	357:382	248 additional amino acids	357:382	This report describes the structure of soluble human stem cell factor isolated from the conditioned medium of Chinese hamster ovary (CHO) cells transfected with stem cell factor (SCF) cDNA, which encodes a leader sequence plus 248 additional amino acids.
1381905	1	12	theme	248	357:359	arg1	medium					230:235	the conditioned medium	214:235	the conditioned medium	214:235	This report describes the structure of soluble human stem cell factor isolated from the conditioned medium of Chinese hamster ovary (CHO) cells transfected with stem cell factor (SCF) cDNA, which encodes a leader sequence plus 248 additional amino acids.
1381905	5	13	gly	deglycosylated	839:852	arg1	peptide					865:871	a deglycosylated C-terminal peptide	837:871	a deglycosylated C-terminal peptide	837:871	Structural analyses of the intact SCF, the deglycosylated SCF, and a deglycosylated C-terminal peptide were performed by laser desorption, fast atom bombardment, or electrospray mass spectrometry.
1381905	7	14	theme	M	1234:1234	arg1	35,000					1239:1244	M(r) 35,000	1234:1244	M(r) 35,000	1234:1244	During a chase with unlabeled Met and Cys, labeled SCF of M(r) 28,000, M(r) 35,000, and M(r) 40,000 appeared in the medium; it was converted to M(r) 18,000-19,000 by glycosidase treatment.
1381905	1	15	theme	amino	372:376	arg1	acids					378:382	248 additional amino acids	357:382	248 additional amino acids	357:382	This report describes the structure of soluble human stem cell factor isolated from the conditioned medium of Chinese hamster ovary (CHO) cells transfected with stem cell factor (SCF) cDNA, which encodes a leader sequence plus 248 additional amino acids.
1381905	1	15	theme	amino	372:376	arg1	medium					230:235	the conditioned medium	214:235	the conditioned medium	214:235	This report describes the structure of soluble human stem cell factor isolated from the conditioned medium of Chinese hamster ovary (CHO) cells transfected with stem cell factor (SCF) cDNA, which encodes a leader sequence plus 248 additional amino acids.
1381905	9	16	theme	cell	1504:1507	arg1	factor					1509:1514	the recombinant human stem cell factor	1477:1514	the recombinant human stem cell factor	1477:1514	The data obtained indicate that the recombinant human stem cell factor, as isolated, represents proteolytically processed forms containing amino acids 1-165, derived from the initially synthesized membrane-bound form of 248 amino acids.
1381905	11	17	link	O-linked	1890:1897	arg1	carbohydrate					1899:1910	O-linked carbohydrate	1890:1910	O-linked carbohydrate	1890:1910	Each form also contains O-linked carbohydrate.
1381905	3	18	dep	bands	518:522	arg1	M					564:564	M(r) 40,000	564:574	M(r) 40,000	564:574	The isolated material is glycosylated and three bands (apparent M(r) 28,000, M(r) 35,000, and M(r) 40,000) are evident by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis.
1381905	3	18	dep	bands	518:522	arg1	M					534:534	apparent M	525:534	apparent M	525:534	The isolated material is glycosylated and three bands (apparent M(r) 28,000, M(r) 35,000, and M(r) 40,000) are evident by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis.
1381905	3	18	dep	bands	518:522	arg1	r					566:566	r	566:566	r	566:566	The isolated material is glycosylated and three bands (apparent M(r) 28,000, M(r) 35,000, and M(r) 40,000) are evident by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis.
1381905	3	18	dep	bands	518:522	arg1	r					536:536	r	536:536	r	536:536	The isolated material is glycosylated and three bands (apparent M(r) 28,000, M(r) 35,000, and M(r) 40,000) are evident by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis.
1381905	3	18	dep	bands	518:522	arg1	35,000					552:557	M(r) 35,000	547:557	M(r) 35,000	547:557	The isolated material is glycosylated and three bands (apparent M(r) 28,000, M(r) 35,000, and M(r) 40,000) are evident by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis.
1381905	3	18	dep	bands	518:522	arg1	bands					518:522	three bands	512:522	three bands (apparent M(r) 28,000, M(r) 35,000, and M(r) 40,000)	512:575	The isolated material is glycosylated and three bands (apparent M(r) 28,000, M(r) 35,000, and M(r) 40,000) are evident by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis.
1381905	3	18	dep	bands	518:522	arg1	28,000					539:544	28,000	539:544	28,000	539:544	The isolated material is glycosylated and three bands (apparent M(r) 28,000, M(r) 35,000, and M(r) 40,000) are evident by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis.
1381905	12	19	theme	in	2000:2001	arg1	activity					2020:2027	in vitro biological activity	2000:2027	in vitro biological activity	2000:2027	The N-linked glycosylation, particularly that at Asn93 and at Asn65, adversely affects in vitro biological activity and receptor binding.
1381905	5	20	theme	deglycosylated	839:852	arg1	peptide					865:871	a deglycosylated C-terminal peptide	837:871	a deglycosylated C-terminal peptide	837:871	Structural analyses of the intact SCF, the deglycosylated SCF, and a deglycosylated C-terminal peptide were performed by laser desorption, fast atom bombardment, or electrospray mass spectrometry.
1381905	12	21	theme	biological	2009:2018	arg1	activity					2020:2027	in vitro biological activity	2000:2027	in vitro biological activity	2000:2027	The N-linked glycosylation, particularly that at Asn93 and at Asn65, adversely affects in vitro biological activity and receptor binding.
1381905	7	22	theme	M	1221:1221	arg1	SCF					1214:1216	labeled SCF	1206:1216	labeled SCF of M(r) 28,000, M(r) 35,000, and M(r) 40,000	1206:1261	During a chase with unlabeled Met and Cys, labeled SCF of M(r) 28,000, M(r) 35,000, and M(r) 40,000 appeared in the medium; it was converted to M(r) 18,000-19,000 by glycosidase treatment.
1381905	0	23	theme	factor	81:86	arg1	processing					19:28	Post-translational processing	0:28	Post-translational processing of membrane-associated recombinant human stem cell factor	0:86	Post-translational processing of membrane-associated recombinant human stem cell factor expressed in Chinese hamster ovary cells.
1381905	5	24	theme	SCF	828:830	arg1	analyses					781:788	Structural analyses	770:788	Structural analyses of the intact SCF, the deglycosylated SCF, and a deglycosylated C-terminal peptide	770:871	Structural analyses of the intact SCF, the deglycosylated SCF, and a deglycosylated C-terminal peptide were performed by laser desorption, fast atom bombardment, or electrospray mass spectrometry.
1381905	9	25	theme	processed	1557:1565	arg1	forms					1567:1571	proteolytically processed forms	1541:1571	proteolytically processed forms containing amino acids 1-165, derived from the initially synthesized membrane-bound form of 248 amino acids	1541:1679	The data obtained indicate that the recombinant human stem cell factor, as isolated, represents proteolytically processed forms containing amino acids 1-165, derived from the initially synthesized membrane-bound form of 248 amino acids.
1381905	4	26	theme	complete	663:670	arg1	deglycosylation					672:686	complete deglycosylation	663:686	complete deglycosylation	663:686	After complete deglycosylation, the molecular weight by SDS-polyacrylamide gel electrophoresis is 18,000-19,000.
1381905	0	27	theme	hamster	109:115	arg1	cells					123:127	Chinese hamster ovary cells	101:127	Chinese hamster ovary cells	101:127	Post-translational processing of membrane-associated recombinant human stem cell factor expressed in Chinese hamster ovary cells.
1381905	5	28	theme	laser	891:895	arg1	desorption					897:906	laser desorption	891:906	laser desorption	891:906	Structural analyses of the intact SCF, the deglycosylated SCF, and a deglycosylated C-terminal peptide were performed by laser desorption, fast atom bombardment, or electrospray mass spectrometry.
1381905	7	29	theme	glycosidase	1329:1339	arg1	treatment					1341:1349	glycosidase treatment	1329:1349	glycosidase treatment	1329:1349	During a chase with unlabeled Met and Cys, labeled SCF of M(r) 28,000, M(r) 35,000, and M(r) 40,000 appeared in the medium; it was converted to M(r) 18,000-19,000 by glycosidase treatment.
1381905	9	30	dep	factor	1509:1514	arg1	isolated					1520:1527	isolated	1520:1527	isolated	1520:1527	The data obtained indicate that the recombinant human stem cell factor, as isolated, represents proteolytically processed forms containing amino acids 1-165, derived from the initially synthesized membrane-bound form of 248 amino acids.
1381905	2	31	theme	hydrophobic	415:425	arg1	region					441:446	a hydrophobic transmembrane region	413:446	a hydrophobic transmembrane region at positions 190-212	413:467	The 248 amino acids include a hydrophobic transmembrane region at positions 190-212.
1381905	6	32	gly	glycosylated	1048:1059	arg1	SCF					1061:1063	cell-associated glycosylated SCF	1032:1063	cell-associated glycosylated SCF of M(r) 33,000-45,000 which was converted to M(r) 33,000 by in vitro treatment with glycosidases	1032:1160	Pulse-labeling of cells with 35S-labeled Met and Cys resulted in cell-associated glycosylated SCF of M(r) 33,000-45,000 which was converted to M(r) 33,000 by in vitro treatment with glycosidases.
1381905	0	33	theme	Post-translational	0:17	arg1	processing					19:28	Post-translational processing	0:28	Post-translational processing of membrane-associated recombinant human stem cell factor	0:86	Post-translational processing of membrane-associated recombinant human stem cell factor expressed in Chinese hamster ovary cells.
1381905	12	34	gly	glycosylation	1926:1938	arg1	receptor					2033:2040	receptor binding	2033:2048	receptor binding	2033:2048	The N-linked glycosylation, particularly that at Asn93 and at Asn65, adversely affects in vitro biological activity and receptor binding.
1381905	5	35	theme	peptide	865:871	arg1	analyses					781:788	Structural analyses	770:788	Structural analyses of the intact SCF, the deglycosylated SCF, and a deglycosylated C-terminal peptide	770:871	Structural analyses of the intact SCF, the deglycosylated SCF, and a deglycosylated C-terminal peptide were performed by laser desorption, fast atom bombardment, or electrospray mass spectrometry.
1381905	7	36	theme	labeled	1206:1212	arg1	SCF					1214:1216	labeled SCF	1206:1216	labeled SCF of M(r) 28,000, M(r) 35,000, and M(r) 40,000	1206:1261	During a chase with unlabeled Met and Cys, labeled SCF of M(r) 28,000, M(r) 35,000, and M(r) 40,000 appeared in the medium; it was converted to M(r) 18,000-19,000 by glycosidase treatment.
1381905	12	37	theme	N-linked	1917:1924	arg1	glycosylation					1926:1938	The N-linked glycosylation	1913:1938	The N-linked glycosylation	1913:1938	The N-linked glycosylation, particularly that at Asn93 and at Asn65, adversely affects in vitro biological activity and receptor binding.
1381905	12	37	theme	N-linked	1917:1924	arg1	that					1954:1957	that	1954:1957	that	1954:1957	The N-linked glycosylation, particularly that at Asn93 and at Asn65, adversely affects in vitro biological activity and receptor binding.
1381905	2	38	theme	amino	393:397	arg1	acids					399:403	The 248 amino acids	385:403	The 248 amino acids	385:403	The 248 amino acids include a hydrophobic transmembrane region at positions 190-212.
1381905	1	39	theme	stem	291:294	arg1	SCF					309:311	SCF	309:311	SCF	309:311	This report describes the structure of soluble human stem cell factor isolated from the conditioned medium of Chinese hamster ovary (CHO) cells transfected with stem cell factor (SCF) cDNA, which encodes a leader sequence plus 248 additional amino acids.
1381905	1	39	theme	stem	291:294	arg1	factor					301:306	stem cell factor	291:306	stem cell factor (SCF) cDNA	291:317	This report describes the structure of soluble human stem cell factor isolated from the conditioned medium of Chinese hamster ovary (CHO) cells transfected with stem cell factor (SCF) cDNA, which encodes a leader sequence plus 248 additional amino acids.
1381905	4	40	theme	gel	732:734	arg1	electrophoresis					736:750	SDS-polyacrylamide gel electrophoresis	713:750	SDS-polyacrylamide gel electrophoresis	713:750	After complete deglycosylation, the molecular weight by SDS-polyacrylamide gel electrophoresis is 18,000-19,000.
1381905	0	41	theme	recombinant	53:63	arg1	factor					81:86	membrane-associated recombinant human stem cell factor	33:86	membrane-associated recombinant human stem cell factor	33:86	Post-translational processing of membrane-associated recombinant human stem cell factor expressed in Chinese hamster ovary cells.
1381905	1	42	theme	factor	301:306	arg1	cDNA					314:317	stem cell factor (SCF) cDNA	291:317	stem cell factor (SCF) cDNA	291:317	This report describes the structure of soluble human stem cell factor isolated from the conditioned medium of Chinese hamster ovary (CHO) cells transfected with stem cell factor (SCF) cDNA, which encodes a leader sequence plus 248 additional amino acids.
1381905	5	43	theme	electrospray	935:946	arg1	spectrometry					953:964	electrospray mass spectrometry	935:964	electrospray mass spectrometry	935:964	Structural analyses of the intact SCF, the deglycosylated SCF, and a deglycosylated C-terminal peptide were performed by laser desorption, fast atom bombardment, or electrospray mass spectrometry.
1381905	0	44	theme	stem	71:74	arg1	factor					81:86	membrane-associated recombinant human stem cell factor	33:86	membrane-associated recombinant human stem cell factor	33:86	Post-translational processing of membrane-associated recombinant human stem cell factor expressed in Chinese hamster ovary cells.
1381905	9	45	theme	membrane-bound	1642:1655	arg1	form					1657:1660	the initially synthesized membrane-bound form	1616:1660	the initially synthesized membrane-bound form of 248 amino acids	1616:1679	The data obtained indicate that the recombinant human stem cell factor, as isolated, represents proteolytically processed forms containing amino acids 1-165, derived from the initially synthesized membrane-bound form of 248 amino acids.
1381905	4	46	theme	molecular	693:701	arg1	weight					703:708	the molecular weight	689:708	the molecular weight by SDS-polyacrylamide gel electrophoresis	689:750	After complete deglycosylation, the molecular weight by SDS-polyacrylamide gel electrophoresis is 18,000-19,000.
1381905	4	46	theme	molecular	693:701	arg1	18,000-19,000					755:767	18,000-19,000	755:767	18,000-19,000	755:767	After complete deglycosylation, the molecular weight by SDS-polyacrylamide gel electrophoresis is 18,000-19,000.
1381905	6	47	with	cells	985:989	arg1	Cys					1016:1018	Cys	1016:1018	Cys	1016:1018	Pulse-labeling of cells with 35S-labeled Met and Cys resulted in cell-associated glycosylated SCF of M(r) 33,000-45,000 which was converted to M(r) 33,000 by in vitro treatment with glycosidases.
1381905	6	47	with	cells	985:989	arg1	Met					1008:1010	35S-labeled Met	996:1010	35S-labeled Met	996:1010	Pulse-labeling of cells with 35S-labeled Met and Cys resulted in cell-associated glycosylated SCF of M(r) 33,000-45,000 which was converted to M(r) 33,000 by in vitro treatment with glycosidases.
1381905	5	48	theme	atom	914:917	arg1	bombardment					919:929	fast atom bombardment	909:929	fast atom bombardment	909:929	Structural analyses of the intact SCF, the deglycosylated SCF, and a deglycosylated C-terminal peptide were performed by laser desorption, fast atom bombardment, or electrospray mass spectrometry.
1381905	6	49	theme	glycosylated	1048:1059	arg1	SCF					1061:1063	cell-associated glycosylated SCF	1032:1063	cell-associated glycosylated SCF of M(r) 33,000-45,000 which was converted to M(r) 33,000 by in vitro treatment with glycosidases	1032:1160	Pulse-labeling of cells with 35S-labeled Met and Cys resulted in cell-associated glycosylated SCF of M(r) 33,000-45,000 which was converted to M(r) 33,000 by in vitro treatment with glycosidases.
1381905	1	50	theme	hamster	248:254	arg1	cells					268:272	Chinese hamster ovary (CHO) cells	240:272	Chinese hamster ovary (CHO) cells transfected with stem cell factor (SCF) cDNA	240:317	This report describes the structure of soluble human stem cell factor isolated from the conditioned medium of Chinese hamster ovary (CHO) cells transfected with stem cell factor (SCF) cDNA, which encodes a leader sequence plus 248 additional amino acids.
1381905	9	51	theme	amino	1669:1673	arg1	acids					1675:1679	248 amino acids	1665:1679	248 amino acids	1665:1679	The data obtained indicate that the recombinant human stem cell factor, as isolated, represents proteolytically processed forms containing amino acids 1-165, derived from the initially synthesized membrane-bound form of 248 amino acids.
1381905	8	52	theme	transfected	1378:1388	arg1	cells					1394:1398	the transfected CHO cells	1374:1398	the transfected CHO cells	1374:1398	SCF at the surface of the transfected CHO cells could be demonstrated by immunofluorescence.
1381905	3	53	theme	dodecyl	599:605	arg1	electrophoresis					640:654	sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis	592:654	sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis	592:654	The isolated material is glycosylated and three bands (apparent M(r) 28,000, M(r) 35,000, and M(r) 40,000) are evident by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis.
1381905	6	54	with	treatment	1134:1142	arg1	glycosidases					1149:1160	glycosidases	1149:1160	glycosidases	1149:1160	Pulse-labeling of cells with 35S-labeled Met and Cys resulted in cell-associated glycosylated SCF of M(r) 33,000-45,000 which was converted to M(r) 33,000 by in vitro treatment with glycosidases.
1381905	10	55	theme	M	1820:1820	arg1	form					1832:1835	the M(r) 40,000 form	1816:1835	the M(r) 40,000 form	1816:1835	Further characterization indicated that the M(r) 28,000 form is glycosylated at Asn120, the M(r) 35,000 form at Asn120 and Asn65, and the M(r) 40,000 form at Asn120, Asn93, and Asn65.
1381905	10	55	theme	M	1820:1820	arg1	Asn120					1762:1767	Asn120	1762:1767	Asn120	1762:1767	Further characterization indicated that the M(r) 28,000 form is glycosylated at Asn120, the M(r) 35,000 form at Asn120 and Asn65, and the M(r) 40,000 form at Asn120, Asn93, and Asn65.
1381905	8	56	theme	cells	1394:1398	arg1	surface					1363:1369	the surface	1359:1369	the surface of the transfected CHO cells	1359:1398	SCF at the surface of the transfected CHO cells could be demonstrated by immunofluorescence.
1381905	5	57	theme	deglycosylated	813:826	arg1	SCF					828:830	the deglycosylated SCF	809:830	the deglycosylated SCF	809:830	Structural analyses of the intact SCF, the deglycosylated SCF, and a deglycosylated C-terminal peptide were performed by laser desorption, fast atom bombardment, or electrospray mass spectrometry.
1381905	8	58	from	surface	1363:1369	arg1	SCF					1352:1354	SCF	1352:1354	SCF at the surface of the transfected CHO cells	1352:1398	SCF at the surface of the transfected CHO cells could be demonstrated by immunofluorescence.
1381905	1	59	theme	factor	193:198	arg1	structure					156:164	the structure	152:164	the structure of soluble human stem cell factor isolated from the conditioned medium of Chinese hamster ovary (CHO) cells transfected with stem cell factor (SCF) cDNA, which encodes a leader sequence plus 248 additional amino acids	152:382	This report describes the structure of soluble human stem cell factor isolated from the conditioned medium of Chinese hamster ovary (CHO) cells transfected with stem cell factor (SCF) cDNA, which encodes a leader sequence plus 248 additional amino acids.
1381905	1	60	theme	stem	183:186	arg1	factor					193:198	soluble human stem cell factor	169:198	soluble human stem cell factor isolated from the conditioned medium of Chinese hamster ovary (CHO) cells transfected with stem cell factor (SCF) cDNA, which encodes a leader sequence plus 248 additional amino acids	169:382	This report describes the structure of soluble human stem cell factor isolated from the conditioned medium of Chinese hamster ovary (CHO) cells transfected with stem cell factor (SCF) cDNA, which encodes a leader sequence plus 248 additional amino acids.
1381905	9	61	theme	synthesized	1630:1640	arg1	form					1657:1660	the initially synthesized membrane-bound form	1616:1660	the initially synthesized membrane-bound form of 248 amino acids	1616:1679	The data obtained indicate that the recombinant human stem cell factor, as isolated, represents proteolytically processed forms containing amino acids 1-165, derived from the initially synthesized membrane-bound form of 248 amino acids.
1381905	7	62	theme	M	1251:1251	arg1	SCF					1214:1216	labeled SCF	1206:1216	labeled SCF of M(r) 28,000, M(r) 35,000, and M(r) 40,000	1206:1261	During a chase with unlabeled Met and Cys, labeled SCF of M(r) 28,000, M(r) 35,000, and M(r) 40,000 appeared in the medium; it was converted to M(r) 18,000-19,000 by glycosidase treatment.
1381905	10	63	theme	40,000	1825:1830	arg1	form					1832:1835	the M(r) 40,000 form	1816:1835	the M(r) 40,000 form	1816:1835	Further characterization indicated that the M(r) 28,000 form is glycosylated at Asn120, the M(r) 35,000 form at Asn120 and Asn65, and the M(r) 40,000 form at Asn120, Asn93, and Asn65.
1381905	10	63	theme	40,000	1825:1830	arg1	Asn120					1762:1767	Asn120	1762:1767	Asn120	1762:1767	Further characterization indicated that the M(r) 28,000 form is glycosylated at Asn120, the M(r) 35,000 form at Asn120 and Asn65, and the M(r) 40,000 form at Asn120, Asn93, and Asn65.
1381905	10	64	theme	M	1726:1726	arg1	form					1738:1741	the M(r) 28,000 form	1722:1741	the M(r) 28,000 form	1722:1741	Further characterization indicated that the M(r) 28,000 form is glycosylated at Asn120, the M(r) 35,000 form at Asn120 and Asn65, and the M(r) 40,000 form at Asn120, Asn93, and Asn65.
1381905	7	65	with	chase	1172:1176	arg1	Cys					1201:1203	Cys	1201:1203	Cys	1201:1203	During a chase with unlabeled Met and Cys, labeled SCF of M(r) 28,000, M(r) 35,000, and M(r) 40,000 appeared in the medium; it was converted to M(r) 18,000-19,000 by glycosidase treatment.
1381905	7	65	with	chase	1172:1176	arg1	Met					1193:1195	unlabeled Met	1183:1195	unlabeled Met	1183:1195	During a chase with unlabeled Met and Cys, labeled SCF of M(r) 28,000, M(r) 35,000, and M(r) 40,000 appeared in the medium; it was converted to M(r) 18,000-19,000 by glycosidase treatment.
1381905	5	66	theme	intact	797:802	arg1	SCF					804:806	the intact SCF	793:806	the intact SCF	793:806	Structural analyses of the intact SCF, the deglycosylated SCF, and a deglycosylated C-terminal peptide were performed by laser desorption, fast atom bombardment, or electrospray mass spectrometry.
1381905	9	67	theme	recombinant	1481:1491	arg1	factor					1509:1514	the recombinant human stem cell factor	1477:1514	the recombinant human stem cell factor	1477:1514	The data obtained indicate that the recombinant human stem cell factor, as isolated, represents proteolytically processed forms containing amino acids 1-165, derived from the initially synthesized membrane-bound form of 248 amino acids.
1381905	12	68	theme	receptor	2033:2040	arg1	binding					2042:2048	receptor binding	2033:2048	receptor binding	2033:2048	The N-linked glycosylation, particularly that at Asn93 and at Asn65, adversely affects in vitro biological activity and receptor binding.
1381905	1	69	theme	human	177:181	arg1	factor					193:198	soluble human stem cell factor	169:198	soluble human stem cell factor isolated from the conditioned medium of Chinese hamster ovary (CHO) cells transfected with stem cell factor (SCF) cDNA, which encodes a leader sequence plus 248 additional amino acids	169:382	This report describes the structure of soluble human stem cell factor isolated from the conditioned medium of Chinese hamster ovary (CHO) cells transfected with stem cell factor (SCF) cDNA, which encodes a leader sequence plus 248 additional amino acids.
1381905	3	70	theme	gel	636:638	arg1	electrophoresis					640:654	sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis	592:654	sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis	592:654	The isolated material is glycosylated and three bands (apparent M(r) 28,000, M(r) 35,000, and M(r) 40,000) are evident by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis.
1381905	1	71	theme	additional	361:370	arg1	acids					378:382	248 additional amino acids	357:382	248 additional amino acids	357:382	This report describes the structure of soluble human stem cell factor isolated from the conditioned medium of Chinese hamster ovary (CHO) cells transfected with stem cell factor (SCF) cDNA, which encodes a leader sequence plus 248 additional amino acids.
1381905	1	71	theme	additional	361:370	arg1	medium					230:235	the conditioned medium	214:235	the conditioned medium	214:235	This report describes the structure of soluble human stem cell factor isolated from the conditioned medium of Chinese hamster ovary (CHO) cells transfected with stem cell factor (SCF) cDNA, which encodes a leader sequence plus 248 additional amino acids.
1381905	3	72	theme	M	547:547	arg1	35,000					552:557	M(r) 35,000	547:557	M(r) 35,000	547:557	The isolated material is glycosylated and three bands (apparent M(r) 28,000, M(r) 35,000, and M(r) 40,000) are evident by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis.
1381905	5	73	theme	Structural	770:779	arg1	analyses					781:788	Structural analyses	770:788	Structural analyses of the intact SCF, the deglycosylated SCF, and a deglycosylated C-terminal peptide	770:871	Structural analyses of the intact SCF, the deglycosylated SCF, and a deglycosylated C-terminal peptide were performed by laser desorption, fast atom bombardment, or electrospray mass spectrometry.
1381905	9	74	theme	stem	1499:1502	arg1	factor					1509:1514	the recombinant human stem cell factor	1477:1514	the recombinant human stem cell factor	1477:1514	The data obtained indicate that the recombinant human stem cell factor, as isolated, represents proteolytically processed forms containing amino acids 1-165, derived from the initially synthesized membrane-bound form of 248 amino acids.
1381905	6	75	theme	in	1125:1126	arg1	treatment					1134:1142	in vitro treatment	1125:1142	in vitro treatment with glycosidases	1125:1160	Pulse-labeling of cells with 35S-labeled Met and Cys resulted in cell-associated glycosylated SCF of M(r) 33,000-45,000 which was converted to M(r) 33,000 by in vitro treatment with glycosidases.
1381905	9	76	attach	derived	1603:1609	arg2	acids					1590:1594	amino acids 1-165	1584:1600	amino acids 1-165	1584:1600	The data obtained indicate that the recombinant human stem cell factor, as isolated, represents proteolytically processed forms containing amino acids 1-165, derived from the initially synthesized membrane-bound form of 248 amino acids.
1381905	9	76	attach	derived	1603:1609	arg1	form					1657:1660	the initially synthesized membrane-bound form	1616:1660	the initially synthesized membrane-bound form of 248 amino acids	1616:1679	The data obtained indicate that the recombinant human stem cell factor, as isolated, represents proteolytically processed forms containing amino acids 1-165, derived from the initially synthesized membrane-bound form of 248 amino acids.
1381905	5	77	gly	deglycosylated	813:826	arg1	SCF					828:830	the deglycosylated SCF	809:830	the deglycosylated SCF	809:830	Structural analyses of the intact SCF, the deglycosylated SCF, and a deglycosylated C-terminal peptide were performed by laser desorption, fast atom bombardment, or electrospray mass spectrometry.
1381905	10	78	from	Asn65	1805:1809	arg1	form					1832:1835	the M(r) 40,000 form	1816:1835	the M(r) 40,000 form	1816:1835	Further characterization indicated that the M(r) 28,000 form is glycosylated at Asn120, the M(r) 35,000 form at Asn120 and Asn65, and the M(r) 40,000 form at Asn120, Asn93, and Asn65.
1381905	10	78	from	Asn65	1805:1809	arg1	form					1786:1789	the M(r) 35,000 form	1770:1789	the M(r) 35,000 form at Asn120 and Asn65	1770:1809	Further characterization indicated that the M(r) 28,000 form is glycosylated at Asn120, the M(r) 35,000 form at Asn120 and Asn65, and the M(r) 40,000 form at Asn120, Asn93, and Asn65.
1381905	10	78	from	Asn65	1805:1809	arg1	Asn120					1762:1767	Asn120	1762:1767	Asn120	1762:1767	Further characterization indicated that the M(r) 28,000 form is glycosylated at Asn120, the M(r) 35,000 form at Asn120 and Asn65, and the M(r) 40,000 form at Asn120, Asn93, and Asn65.
1381905	6	79	theme	M	1110:1110	arg1	r					1112:1112	M(r) 33,000	1110:1120	M(r) 33,000	1110:1120	Pulse-labeling of cells with 35S-labeled Met and Cys resulted in cell-associated glycosylated SCF of M(r) 33,000-45,000 which was converted to M(r) 33,000 by in vitro treatment with glycosidases.
1381905	10	80	theme	M	1774:1774	arg1	form					1786:1789	the M(r) 35,000 form	1770:1789	the M(r) 35,000 form at Asn120 and Asn65	1770:1809	Further characterization indicated that the M(r) 28,000 form is glycosylated at Asn120, the M(r) 35,000 form at Asn120 and Asn65, and the M(r) 40,000 form at Asn120, Asn93, and Asn65.
1381905	10	80	theme	M	1774:1774	arg1	Asn120					1762:1767	Asn120	1762:1767	Asn120	1762:1767	Further characterization indicated that the M(r) 28,000 form is glycosylated at Asn120, the M(r) 35,000 form at Asn120 and Asn65, and the M(r) 40,000 form at Asn120, Asn93, and Asn65.
1381905	0	81	theme	Chinese	101:107	arg1	cells					123:127	Chinese hamster ovary cells	101:127	Chinese hamster ovary cells	101:127	Post-translational processing of membrane-associated recombinant human stem cell factor expressed in Chinese hamster ovary cells.
1381905	1	82	theme	soluble	169:175	arg1	factor					193:198	soluble human stem cell factor	169:198	soluble human stem cell factor isolated from the conditioned medium of Chinese hamster ovary (CHO) cells transfected with stem cell factor (SCF) cDNA, which encodes a leader sequence plus 248 additional amino acids	169:382	This report describes the structure of soluble human stem cell factor isolated from the conditioned medium of Chinese hamster ovary (CHO) cells transfected with stem cell factor (SCF) cDNA, which encodes a leader sequence plus 248 additional amino acids.
1381905	12	83	link	N-linked	1917:1924	arg1	glycosylation					1926:1938	The N-linked glycosylation	1913:1938	The N-linked glycosylation	1913:1938	The N-linked glycosylation, particularly that at Asn93 and at Asn65, adversely affects in vitro biological activity and receptor binding.
1381905	12	83	link	N-linked	1917:1924	arg1	that					1954:1957	that	1954:1957	that	1954:1957	The N-linked glycosylation, particularly that at Asn93 and at Asn65, adversely affects in vitro biological activity and receptor binding.
1381905	6	84	dep	in	1125:1126	arg1	vitro					1128:1132	vitro	1128:1132	vitro	1128:1132	Pulse-labeling of cells with 35S-labeled Met and Cys resulted in cell-associated glycosylated SCF of M(r) 33,000-45,000 which was converted to M(r) 33,000 by in vitro treatment with glycosidases.
1381905	0	85	theme	ovary	117:121	arg1	cells					123:127	Chinese hamster ovary cells	101:127	Chinese hamster ovary cells	101:127	Post-translational processing of membrane-associated recombinant human stem cell factor expressed in Chinese hamster ovary cells.
1381905	2	86	dep	positions	451:459	arg1	190-212					461:467	190-212	461:467	190-212	461:467	The 248 amino acids include a hydrophobic transmembrane region at positions 190-212.
1381905	3	87	gly	glycosylated	495:506	arg1	material					483:490	The isolated material	470:490	The isolated material	470:490	The isolated material is glycosylated and three bands (apparent M(r) 28,000, M(r) 35,000, and M(r) 40,000) are evident by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis.
1381905	10	88	theme	35,000	1779:1784	arg1	form					1786:1789	the M(r) 35,000 form	1770:1789	the M(r) 35,000 form at Asn120 and Asn65	1770:1809	Further characterization indicated that the M(r) 28,000 form is glycosylated at Asn120, the M(r) 35,000 form at Asn120 and Asn65, and the M(r) 40,000 form at Asn120, Asn93, and Asn65.
1381905	10	88	theme	35,000	1779:1784	arg1	Asn120					1762:1767	Asn120	1762:1767	Asn120	1762:1767	Further characterization indicated that the M(r) 28,000 form is glycosylated at Asn120, the M(r) 35,000 form at Asn120 and Asn65, and the M(r) 40,000 form at Asn120, Asn93, and Asn65.
1381905	1	89	theme	leader	336:341	arg1	sequence					343:350	a leader sequence	334:350	a leader sequence	334:350	This report describes the structure of soluble human stem cell factor isolated from the conditioned medium of Chinese hamster ovary (CHO) cells transfected with stem cell factor (SCF) cDNA, which encodes a leader sequence plus 248 additional amino acids.
1381905	1	89	theme	leader	336:341	arg1	medium					230:235	the conditioned medium	214:235	the conditioned medium	214:235	This report describes the structure of soluble human stem cell factor isolated from the conditioned medium of Chinese hamster ovary (CHO) cells transfected with stem cell factor (SCF) cDNA, which encodes a leader sequence plus 248 additional amino acids.
1381905	9	90	theme	amino	1584:1588	arg1	acids					1590:1594	amino acids 1-165	1584:1600	amino acids 1-165	1584:1600	The data obtained indicate that the recombinant human stem cell factor, as isolated, represents proteolytically processed forms containing amino acids 1-165, derived from the initially synthesized membrane-bound form of 248 amino acids.
1381905	2	91	from	positions	451:459	arg1	region					441:446	a hydrophobic transmembrane region	413:446	a hydrophobic transmembrane region at positions 190-212	413:467	The 248 amino acids include a hydrophobic transmembrane region at positions 190-212.
1381905	5	92	theme	C-terminal	854:863	arg1	peptide					865:871	a deglycosylated C-terminal peptide	837:871	a deglycosylated C-terminal peptide	837:871	Structural analyses of the intact SCF, the deglycosylated SCF, and a deglycosylated C-terminal peptide were performed by laser desorption, fast atom bombardment, or electrospray mass spectrometry.
1381905	6	93	theme	35S-labeled	996:1006	arg1	Met					1008:1010	35S-labeled Met	996:1010	35S-labeled Met	996:1010	Pulse-labeling of cells with 35S-labeled Met and Cys resulted in cell-associated glycosylated SCF of M(r) 33,000-45,000 which was converted to M(r) 33,000 by in vitro treatment with glycosidases.
1381905	9	94	theme	human	1493:1497	arg1	factor					1509:1514	the recombinant human stem cell factor	1477:1514	the recombinant human stem cell factor	1477:1514	The data obtained indicate that the recombinant human stem cell factor, as isolated, represents proteolytically processed forms containing amino acids 1-165, derived from the initially synthesized membrane-bound form of 248 amino acids.
1381905	0	95	theme	membrane-associated	33:51	arg1	factor					81:86	membrane-associated recombinant human stem cell factor	33:86	membrane-associated recombinant human stem cell factor	33:86	Post-translational processing of membrane-associated recombinant human stem cell factor expressed in Chinese hamster ovary cells.
1381905	6	96	theme	cells	985:989	arg1	Pulse-labeling					967:980	Pulse-labeling	967:980	Pulse-labeling of cells with 35S-labeled Met and Cys	967:1018	Pulse-labeling of cells with 35S-labeled Met and Cys resulted in cell-associated glycosylated SCF of M(r) 33,000-45,000 which was converted to M(r) 33,000 by in vitro treatment with glycosidases.
1381905	0	97	theme	human	65:69	arg1	factor					81:86	membrane-associated recombinant human stem cell factor	33:86	membrane-associated recombinant human stem cell factor	33:86	Post-translational processing of membrane-associated recombinant human stem cell factor expressed in Chinese hamster ovary cells.
1381905	1	98	theme	cell	296:299	arg1	SCF					309:311	SCF	309:311	SCF	309:311	This report describes the structure of soluble human stem cell factor isolated from the conditioned medium of Chinese hamster ovary (CHO) cells transfected with stem cell factor (SCF) cDNA, which encodes a leader sequence plus 248 additional amino acids.
1381905	1	98	theme	cell	296:299	arg1	factor					301:306	stem cell factor	291:306	stem cell factor (SCF) cDNA	291:317	This report describes the structure of soluble human stem cell factor isolated from the conditioned medium of Chinese hamster ovary (CHO) cells transfected with stem cell factor (SCF) cDNA, which encodes a leader sequence plus 248 additional amino acids.
1381905	1	99	theme	conditioned	218:228	arg1	acids					378:382	248 additional amino acids	357:382	248 additional amino acids	357:382	This report describes the structure of soluble human stem cell factor isolated from the conditioned medium of Chinese hamster ovary (CHO) cells transfected with stem cell factor (SCF) cDNA, which encodes a leader sequence plus 248 additional amino acids.
1381905	1	99	theme	conditioned	218:228	arg1	sequence					343:350	a leader sequence	334:350	a leader sequence	334:350	This report describes the structure of soluble human stem cell factor isolated from the conditioned medium of Chinese hamster ovary (CHO) cells transfected with stem cell factor (SCF) cDNA, which encodes a leader sequence plus 248 additional amino acids.
1381905	1	99	theme	conditioned	218:228	arg1	medium					230:235	the conditioned medium	214:235	the conditioned medium	214:235	This report describes the structure of soluble human stem cell factor isolated from the conditioned medium of Chinese hamster ovary (CHO) cells transfected with stem cell factor (SCF) cDNA, which encodes a leader sequence plus 248 additional amino acids.
1381905	7	100	theme	unlabeled	1183:1191	arg1	Met					1193:1195	unlabeled Met	1183:1195	unlabeled Met	1183:1195	During a chase with unlabeled Met and Cys, labeled SCF of M(r) 28,000, M(r) 35,000, and M(r) 40,000 appeared in the medium; it was converted to M(r) 18,000-19,000 by glycosidase treatment.
1381905	11	101	theme	O-linked	1890:1897	arg1	carbohydrate					1899:1910	O-linked carbohydrate	1890:1910	O-linked carbohydrate	1890:1910	Each form also contains O-linked carbohydrate.
1381905	1	102	attach	isolated	200:207	arg1	acids					378:382	248 additional amino acids	357:382	248 additional amino acids	357:382	This report describes the structure of soluble human stem cell factor isolated from the conditioned medium of Chinese hamster ovary (CHO) cells transfected with stem cell factor (SCF) cDNA, which encodes a leader sequence plus 248 additional amino acids.
1381905	1	102	attach	isolated	200:207	arg1	medium					230:235	the conditioned medium	214:235	the conditioned medium	214:235	This report describes the structure of soluble human stem cell factor isolated from the conditioned medium of Chinese hamster ovary (CHO) cells transfected with stem cell factor (SCF) cDNA, which encodes a leader sequence plus 248 additional amino acids.
1381905	1	102	attach	isolated	200:207	arg1	sequence					343:350	a leader sequence	334:350	a leader sequence	334:350	This report describes the structure of soluble human stem cell factor isolated from the conditioned medium of Chinese hamster ovary (CHO) cells transfected with stem cell factor (SCF) cDNA, which encodes a leader sequence plus 248 additional amino acids.
1381905	1	102	attach	isolated	200:207	arg2	factor					193:198	soluble human stem cell factor	169:198	soluble human stem cell factor isolated from the conditioned medium of Chinese hamster ovary (CHO) cells transfected with stem cell factor (SCF) cDNA, which encodes a leader sequence plus 248 additional amino acids	169:382	This report describes the structure of soluble human stem cell factor isolated from the conditioned medium of Chinese hamster ovary (CHO) cells transfected with stem cell factor (SCF) cDNA, which encodes a leader sequence plus 248 additional amino acids.
1381905	4	103	theme	SDS-polyacrylamide	713:730	arg1	electrophoresis					736:750	SDS-polyacrylamide gel electrophoresis	713:750	SDS-polyacrylamide gel electrophoresis	713:750	After complete deglycosylation, the molecular weight by SDS-polyacrylamide gel electrophoresis is 18,000-19,000.
1381905	0	104	theme	cell	76:79	arg1	factor					81:86	membrane-associated recombinant human stem cell factor	33:86	membrane-associated recombinant human stem cell factor	33:86	Post-translational processing of membrane-associated recombinant human stem cell factor expressed in Chinese hamster ovary cells.
1381905	5	105	theme	mass	948:951	arg1	spectrometry					953:964	electrospray mass spectrometry	935:964	electrospray mass spectrometry	935:964	Structural analyses of the intact SCF, the deglycosylated SCF, and a deglycosylated C-terminal peptide were performed by laser desorption, fast atom bombardment, or electrospray mass spectrometry.
1381905	6	106	theme	M	1068:1068	arg1	SCF					1061:1063	cell-associated glycosylated SCF	1032:1063	cell-associated glycosylated SCF of M(r) 33,000-45,000 which was converted to M(r) 33,000 by in vitro treatment with glycosidases	1032:1160	Pulse-labeling of cells with 35S-labeled Met and Cys resulted in cell-associated glycosylated SCF of M(r) 33,000-45,000 which was converted to M(r) 33,000 by in vitro treatment with glycosidases.
1381905	2	107	theme	transmembrane	427:439	arg1	region					441:446	a hydrophobic transmembrane region	413:446	a hydrophobic transmembrane region at positions 190-212	413:467	The 248 amino acids include a hydrophobic transmembrane region at positions 190-212.
1381905	10	108	theme	Further	1682:1688	arg1	characterization					1690:1705	Further characterization	1682:1705	Further characterization	1682:1705	Further characterization indicated that the M(r) 28,000 form is glycosylated at Asn120, the M(r) 35,000 form at Asn120 and Asn65, and the M(r) 40,000 form at Asn120, Asn93, and Asn65.
1381905	11	109	contain	contains	1881:1888	arg2	carbohydrate					1899:1910	O-linked carbohydrate	1890:1910	O-linked carbohydrate	1890:1910	Each form also contains O-linked carbohydrate.
1381905	11	109	contain	contains	1881:1888	arg1	form					1871:1874	Each form	1866:1874	Each form	1866:1874	Each form also contains O-linked carbohydrate.
1381905	3	110	theme	isolated	474:481	arg1	material					483:490	The isolated material	470:490	The isolated material	470:490	The isolated material is glycosylated and three bands (apparent M(r) 28,000, M(r) 35,000, and M(r) 40,000) are evident by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis.
1381905	10	111	from	Asn120	1794:1799	arg1	form					1832:1835	the M(r) 40,000 form	1816:1835	the M(r) 40,000 form	1816:1835	Further characterization indicated that the M(r) 28,000 form is glycosylated at Asn120, the M(r) 35,000 form at Asn120 and Asn65, and the M(r) 40,000 form at Asn120, Asn93, and Asn65.
1381905	10	111	from	Asn120	1794:1799	arg1	form					1786:1789	the M(r) 35,000 form	1770:1789	the M(r) 35,000 form at Asn120 and Asn65	1770:1809	Further characterization indicated that the M(r) 28,000 form is glycosylated at Asn120, the M(r) 35,000 form at Asn120 and Asn65, and the M(r) 40,000 form at Asn120, Asn93, and Asn65.
1381905	10	111	from	Asn120	1794:1799	arg1	Asn120					1762:1767	Asn120	1762:1767	Asn120	1762:1767	Further characterization indicated that the M(r) 28,000 form is glycosylated at Asn120, the M(r) 35,000 form at Asn120 and Asn65, and the M(r) 40,000 form at Asn120, Asn93, and Asn65.
1381905	5	112	theme	fast	909:912	arg1	bombardment					919:929	fast atom bombardment	909:929	fast atom bombardment	909:929	Structural analyses of the intact SCF, the deglycosylated SCF, and a deglycosylated C-terminal peptide were performed by laser desorption, fast atom bombardment, or electrospray mass spectrometry.
1381905	1	113	theme	Chinese	240:246	arg1	cells					268:272	Chinese hamster ovary (CHO) cells	240:272	Chinese hamster ovary (CHO) cells transfected with stem cell factor (SCF) cDNA	240:317	This report describes the structure of soluble human stem cell factor isolated from the conditioned medium of Chinese hamster ovary (CHO) cells transfected with stem cell factor (SCF) cDNA, which encodes a leader sequence plus 248 additional amino acids.
1381905	6	114	theme	cell-associated	1032:1046	arg1	SCF					1061:1063	cell-associated glycosylated SCF	1032:1063	cell-associated glycosylated SCF of M(r) 33,000-45,000 which was converted to M(r) 33,000 by in vitro treatment with glycosidases	1032:1160	Pulse-labeling of cells with 35S-labeled Met and Cys resulted in cell-associated glycosylated SCF of M(r) 33,000-45,000 which was converted to M(r) 33,000 by in vitro treatment with glycosidases.
1381905	8	115	theme	CHO	1390:1392	arg1	cells					1394:1398	the transfected CHO cells	1374:1398	the transfected CHO cells	1374:1398	SCF at the surface of the transfected CHO cells could be demonstrated by immunofluorescence.
1381905	3	116	theme	sodium	592:597	arg1	electrophoresis					640:654	sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis	592:654	sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis	592:654	The isolated material is glycosylated and three bands (apparent M(r) 28,000, M(r) 35,000, and M(r) 40,000) are evident by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis.
1381905	12	117	dep	in	2000:2001	arg1	vitro					2003:2007	vitro	2003:2007	vitro	2003:2007	The N-linked glycosylation, particularly that at Asn93 and at Asn65, adversely affects in vitro biological activity and receptor binding.
1381905	1	118	theme	ovary	256:260	arg1	cells					268:272	Chinese hamster ovary (CHO) cells	240:272	Chinese hamster ovary (CHO) cells transfected with stem cell factor (SCF) cDNA	240:317	This report describes the structure of soluble human stem cell factor isolated from the conditioned medium of Chinese hamster ovary (CHO) cells transfected with stem cell factor (SCF) cDNA, which encodes a leader sequence plus 248 additional amino acids.
10917520	0	0	theme	high-affinity	55:67	arg1	receptor					69:76	its high-affinity receptor	51:76	its high-affinity receptor Fc epsilonRI alpha	51:95	Structure of the Fc fragment of human IgE bound to its high-affinity receptor Fc epsilonRI alpha.
10917520	3	1	with	interaction	402:412	arg1	epsilonRI					474:482	Fc epsilonRI	471:482	Fc epsilonRI	471:482	The interaction of the crystallizable fragment (Fc) of IgE (IgE-Fc) with Fc epsilonRI is a key recognition event of this process and involves the extracellular domains of the Fc epsilonRI alpha-chain.
10917520	4	2	theme	alpha	726:730	arg1	complex					732:738	the human IgE-Fc-Fc epsilonRI alpha complex	696:738	the human IgE-Fc-Fc epsilonRI alpha complex	696:738	To understand the structural basis for this interaction, we have solved the crystal structure of the human IgE-Fc-Fc epsilonRI alpha complex to 3.5-A resolution.
10917520	2	3	theme	allergic	379:386	arg1	response					388:395	the allergic response	375:395	the allergic response	375:395	Crosslinking of Fc epsilonRI initiates an intracellular signal transduction cascade that triggers the release of mediators of the allergic response.
10917520	3	4	theme	Fc	471:472	arg1	epsilonRI					474:482	Fc epsilonRI	471:482	Fc epsilonRI	471:482	The interaction of the crystallizable fragment (Fc) of IgE (IgE-Fc) with Fc epsilonRI is a key recognition event of this process and involves the extracellular domains of the Fc epsilonRI alpha-chain.
10917520	5	5	theme	IgE-Fc	937:942	arg1	domain					923:928	one C epsilon3 domain	908:928	one C epsilon3 domain of the IgE-Fc	908:942	The crystal structure reveals that one receptor binds one dimeric IgE-Fc molecule asymmetrically through interactions at two sites, each involving one C epsilon3 domain of the IgE-Fc.
10917520	5	5	theme	IgE-Fc	937:942	arg1	IgE-Fc					937:942	the IgE-Fc	933:942	the IgE-Fc	933:942	The crystal structure reveals that one receptor binds one dimeric IgE-Fc molecule asymmetrically through interactions at two sites, each involving one C epsilon3 domain of the IgE-Fc.
10917520	0	6	theme	Fc	78:79	arg1	alpha					91:95	Fc epsilonRI alpha	78:95	its high-affinity receptor Fc epsilonRI alpha	51:95	Structure of the Fc fragment of human IgE bound to its high-affinity receptor Fc epsilonRI alpha.
10917520	3	7	theme	epsilonRI	576:584	arg1	domains					558:564	the extracellular domains	540:564	the extracellular domains of the Fc epsilonRI alpha-chain	540:596	The interaction of the crystallizable fragment (Fc) of IgE (IgE-Fc) with Fc epsilonRI is a key recognition event of this process and involves the extracellular domains of the Fc epsilonRI alpha-chain.
10917520	3	7	theme	epsilonRI	576:584	arg1	epsilonRI					576:584	the Fc epsilonRI alpha-chain	569:596	the Fc epsilonRI alpha-chain	569:596	The interaction of the crystallizable fragment (Fc) of IgE (IgE-Fc) with Fc epsilonRI is a key recognition event of this process and involves the extracellular domains of the Fc epsilonRI alpha-chain.
10917520	2	8	theme	Fc	265:266	arg1	epsilonRI					268:276	Fc epsilonRI	265:276	Fc epsilonRI	265:276	Crosslinking of Fc epsilonRI initiates an intracellular signal transduction cascade that triggers the release of mediators of the allergic response.
10917520	4	9	theme	structural	617:626	arg1	basis					628:632	the structural basis	613:632	the structural basis for this interaction	613:653	To understand the structural basis for this interaction, we have solved the crystal structure of the human IgE-Fc-Fc epsilonRI alpha complex to 3.5-A resolution.
10917520	1	10	theme	Fc	235:236	arg1	receptor					225:232	its high-affinity receptor	207:232	its high-affinity receptor	207:232	The initiation of immunoglobulin-E (IgE)-mediated allergic responses requires the binding of IgE antibody to its high-affinity receptor, Fc epsilonRI.
10917520	1	10	theme	Fc	235:236	arg1	epsilonRI					238:246	Fc epsilonRI	235:246	Fc epsilonRI	235:246	The initiation of immunoglobulin-E (IgE)-mediated allergic responses requires the binding of IgE antibody to its high-affinity receptor, Fc epsilonRI.
10917520	3	11	theme	process	519:525	arg1	event					505:509	a key recognition event	487:509	a key recognition event of this process	487:525	The interaction of the crystallizable fragment (Fc) of IgE (IgE-Fc) with Fc epsilonRI is a key recognition event of this process and involves the extracellular domains of the Fc epsilonRI alpha-chain.
10917520	3	11	theme	process	519:525	arg1	interaction					402:412	The interaction	398:412	The interaction of the crystallizable fragment (Fc) of IgE (IgE-Fc) with Fc epsilonRI	398:482	The interaction of the crystallizable fragment (Fc) of IgE (IgE-Fc) with Fc epsilonRI is a key recognition event of this process and involves the extracellular domains of the Fc epsilonRI alpha-chain.
10917520	4	12	theme	IgE-Fc-Fc	706:714	arg1	complex					732:738	the human IgE-Fc-Fc epsilonRI alpha complex	696:738	the human IgE-Fc-Fc epsilonRI alpha complex	696:738	To understand the structural basis for this interaction, we have solved the crystal structure of the human IgE-Fc-Fc epsilonRI alpha complex to 3.5-A resolution.
10917520	4	13	theme	crystal	675:681	arg1	structure					683:691	the crystal structure	671:691	the crystal structure of the human IgE-Fc-Fc epsilonRI alpha complex to 3.5-A resolution	671:758	To understand the structural basis for this interaction, we have solved the crystal structure of the human IgE-Fc-Fc epsilonRI alpha complex to 3.5-A resolution.
10917520	7	14	theme	Fc	1199:1200	arg1	epsilonRI					1202:1210	Fc epsilonRI	1199:1210	Fc epsilonRI for the treatment of allergy and asthma	1199:1250	The structure suggests new approaches to inhibiting the binding of IgE to Fc epsilonRI for the treatment of allergy and asthma.
10917520	6	15	theme	receptor	1024:1031	arg1	binding					1004:1010	the binding	1000:1010	the binding of a second receptor	1000:1031	The interaction of one receptor with the IgE-Fc blocks the binding of a second receptor, and features of this interaction are conserved in other members of the Fc receptor family.
10917520	4	16	theme	complex	732:738	arg1	structure					683:691	the crystal structure	671:691	the crystal structure of the human IgE-Fc-Fc epsilonRI alpha complex to 3.5-A resolution	671:758	To understand the structural basis for this interaction, we have solved the crystal structure of the human IgE-Fc-Fc epsilonRI alpha complex to 3.5-A resolution.
10917520	5	17	theme	IgE-Fc	827:832	arg1	molecule					834:841	one dimeric IgE-Fc molecule	815:841	one dimeric IgE-Fc molecule	815:841	The crystal structure reveals that one receptor binds one dimeric IgE-Fc molecule asymmetrically through interactions at two sites, each involving one C epsilon3 domain of the IgE-Fc.
10917520	1	18	theme	-mediated	138:146	arg1	responses					157:165	immunoglobulin-E (IgE)-mediated allergic responses	116:165	immunoglobulin-E (IgE)-mediated allergic responses	116:165	The initiation of immunoglobulin-E (IgE)-mediated allergic responses requires the binding of IgE antibody to its high-affinity receptor, Fc epsilonRI.
10917520	0	19	theme	epsilonRI	81:89	arg1	alpha					91:95	Fc epsilonRI alpha	78:95	its high-affinity receptor Fc epsilonRI alpha	51:95	Structure of the Fc fragment of human IgE bound to its high-affinity receptor Fc epsilonRI alpha.
10917520	6	20	theme	interaction	1055:1065	arg1	features					1038:1045	features	1038:1045	features of this interaction	1038:1065	The interaction of one receptor with the IgE-Fc blocks the binding of a second receptor, and features of this interaction are conserved in other members of the Fc receptor family.
10917520	0	21	dep	receptor	69:76	arg1	alpha					91:95	Fc epsilonRI alpha	78:95	its high-affinity receptor Fc epsilonRI alpha	51:95	Structure of the Fc fragment of human IgE bound to its high-affinity receptor Fc epsilonRI alpha.
10917520	1	22	theme	allergic	148:155	arg1	responses					157:165	immunoglobulin-E (IgE)-mediated allergic responses	116:165	immunoglobulin-E (IgE)-mediated allergic responses	116:165	The initiation of immunoglobulin-E (IgE)-mediated allergic responses requires the binding of IgE antibody to its high-affinity receptor, Fc epsilonRI.
10917520	2	23	theme	intracellular	291:303	arg1	cascade					325:331	an intracellular signal transduction cascade	288:331	an intracellular signal transduction cascade that triggers the release of mediators of the allergic response	288:395	Crosslinking of Fc epsilonRI initiates an intracellular signal transduction cascade that triggers the release of mediators of the allergic response.
10917520	1	24	theme	responses	157:165	arg1	initiation					102:111	The initiation	98:111	The initiation of immunoglobulin-E (IgE)-mediated allergic responses	98:165	The initiation of immunoglobulin-E (IgE)-mediated allergic responses requires the binding of IgE antibody to its high-affinity receptor, Fc epsilonRI.
10917520	5	25	theme	crystal	765:771	arg1	structure					773:781	The crystal structure	761:781	The crystal structure	761:781	The crystal structure reveals that one receptor binds one dimeric IgE-Fc molecule asymmetrically through interactions at two sites, each involving one C epsilon3 domain of the IgE-Fc.
10917520	5	26	theme	dimeric	819:825	arg1	molecule					834:841	one dimeric IgE-Fc molecule	815:841	one dimeric IgE-Fc molecule	815:841	The crystal structure reveals that one receptor binds one dimeric IgE-Fc molecule asymmetrically through interactions at two sites, each involving one C epsilon3 domain of the IgE-Fc.
10917520	4	27	theme	epsilonRI	716:724	arg1	complex					732:738	the human IgE-Fc-Fc epsilonRI alpha complex	696:738	the human IgE-Fc-Fc epsilonRI alpha complex	696:738	To understand the structural basis for this interaction, we have solved the crystal structure of the human IgE-Fc-Fc epsilonRI alpha complex to 3.5-A resolution.
10917520	2	28	theme	mediators	362:370	arg1	release					351:357	the release	347:357	the release of mediators of the allergic response	347:395	Crosslinking of Fc epsilonRI initiates an intracellular signal transduction cascade that triggers the release of mediators of the allergic response.
10917520	0	29	theme	Fc	17:18	arg1	fragment					20:27	the Fc fragment	13:27	the Fc fragment of human IgE	13:40	Structure of the Fc fragment of human IgE bound to its high-affinity receptor Fc epsilonRI alpha.
10917520	6	30	theme	second	1017:1022	arg1	receptor					1024:1031	a second receptor	1015:1031	a second receptor	1015:1031	The interaction of one receptor with the IgE-Fc blocks the binding of a second receptor, and features of this interaction are conserved in other members of the Fc receptor family.
10917520	5	31	from	sites	886:890	arg1	interactions					866:877	interactions	866:877	interactions at two sites, each involving one C epsilon3 domain of the IgE-Fc	866:942	The crystal structure reveals that one receptor binds one dimeric IgE-Fc molecule asymmetrically through interactions at two sites, each involving one C epsilon3 domain of the IgE-Fc.
10917520	4	32	theme	human	700:704	arg1	complex					732:738	the human IgE-Fc-Fc epsilonRI alpha complex	696:738	the human IgE-Fc-Fc epsilonRI alpha complex	696:738	To understand the structural basis for this interaction, we have solved the crystal structure of the human IgE-Fc-Fc epsilonRI alpha complex to 3.5-A resolution.
10917520	6	33	theme	Fc	1105:1106	arg1	family					1117:1122	the Fc receptor family	1101:1122	the Fc receptor family	1101:1122	The interaction of one receptor with the IgE-Fc blocks the binding of a second receptor, and features of this interaction are conserved in other members of the Fc receptor family.
10917520	6	34	theme	family	1117:1122	arg1	members					1090:1096	other members	1084:1096	other members of the Fc receptor family	1084:1122	The interaction of one receptor with the IgE-Fc blocks the binding of a second receptor, and features of this interaction are conserved in other members of the Fc receptor family.
10917520	2	35	theme	epsilonRI	268:276	arg1	Crosslinking					249:260	Crosslinking	249:260	Crosslinking of Fc epsilonRI	249:276	Crosslinking of Fc epsilonRI initiates an intracellular signal transduction cascade that triggers the release of mediators of the allergic response.
10917520	7	36	theme	allergy	1233:1239	arg1	treatment					1220:1228	the treatment	1216:1228	the treatment of allergy and asthma	1216:1250	The structure suggests new approaches to inhibiting the binding of IgE to Fc epsilonRI for the treatment of allergy and asthma.
10917520	3	37	theme	extracellular	544:556	arg1	domains					558:564	the extracellular domains	540:564	the extracellular domains of the Fc epsilonRI alpha-chain	540:596	The interaction of the crystallizable fragment (Fc) of IgE (IgE-Fc) with Fc epsilonRI is a key recognition event of this process and involves the extracellular domains of the Fc epsilonRI alpha-chain.
10917520	3	37	theme	extracellular	544:556	arg1	epsilonRI					576:584	the Fc epsilonRI alpha-chain	569:596	the Fc epsilonRI alpha-chain	569:596	The interaction of the crystallizable fragment (Fc) of IgE (IgE-Fc) with Fc epsilonRI is a key recognition event of this process and involves the extracellular domains of the Fc epsilonRI alpha-chain.
10917520	7	38	theme	asthma	1245:1250	arg1	treatment					1220:1228	the treatment	1216:1228	the treatment of allergy and asthma	1216:1250	The structure suggests new approaches to inhibiting the binding of IgE to Fc epsilonRI for the treatment of allergy and asthma.
10917520	0	39	theme	fragment	20:27	arg1	Structure					0:8	Structure	0:8	Structure of the Fc fragment of human IgE	0:40	Structure of the Fc fragment of human IgE bound to its high-affinity receptor Fc epsilonRI alpha.
10917520	1	40	theme	IgE	191:193	arg1	antibody					195:202	IgE antibody	191:202	IgE antibody	191:202	The initiation of immunoglobulin-E (IgE)-mediated allergic responses requires the binding of IgE antibody to its high-affinity receptor, Fc epsilonRI.
10917520	0	41	theme	IgE	38:40	arg1	fragment					20:27	the Fc fragment	13:27	the Fc fragment of human IgE	13:40	Structure of the Fc fragment of human IgE bound to its high-affinity receptor Fc epsilonRI alpha.
10917520	3	42	theme	crystallizable	421:434	arg1	Fc					446:447	Fc	446:447	Fc	446:447	The interaction of the crystallizable fragment (Fc) of IgE (IgE-Fc) with Fc epsilonRI is a key recognition event of this process and involves the extracellular domains of the Fc epsilonRI alpha-chain.
10917520	3	42	theme	crystallizable	421:434	arg1	fragment					436:443	the crystallizable fragment	417:443	the crystallizable fragment (Fc) of IgE (IgE-Fc)	417:464	The interaction of the crystallizable fragment (Fc) of IgE (IgE-Fc) with Fc epsilonRI is a key recognition event of this process and involves the extracellular domains of the Fc epsilonRI alpha-chain.
10917520	0	43	theme	human	32:36	arg1	IgE					38:40	human IgE	32:40	human IgE	32:40	Structure of the Fc fragment of human IgE bound to its high-affinity receptor Fc epsilonRI alpha.
10917520	6	44	theme	receptor	1108:1115	arg1	family					1117:1122	the Fc receptor family	1101:1122	the Fc receptor family	1101:1122	The interaction of one receptor with the IgE-Fc blocks the binding of a second receptor, and features of this interaction are conserved in other members of the Fc receptor family.
10917520	6	45	theme	other	1084:1088	arg1	members					1090:1096	other members	1084:1096	other members of the Fc receptor family	1084:1122	The interaction of one receptor with the IgE-Fc blocks the binding of a second receptor, and features of this interaction are conserved in other members of the Fc receptor family.
10917520	4	46	theme	3.5-A	743:747	arg1	resolution					749:758	3.5-A resolution	743:758	3.5-A resolution	743:758	To understand the structural basis for this interaction, we have solved the crystal structure of the human IgE-Fc-Fc epsilonRI alpha complex to 3.5-A resolution.
10917520	3	47	theme	Fc	573:574	arg1	epsilonRI					576:584	the Fc epsilonRI alpha-chain	569:596	the Fc epsilonRI alpha-chain	569:596	The interaction of the crystallizable fragment (Fc) of IgE (IgE-Fc) with Fc epsilonRI is a key recognition event of this process and involves the extracellular domains of the Fc epsilonRI alpha-chain.
10917520	2	48	theme	transduction	312:323	arg1	cascade					325:331	an intracellular signal transduction cascade	288:331	an intracellular signal transduction cascade that triggers the release of mediators of the allergic response	288:395	Crosslinking of Fc epsilonRI initiates an intracellular signal transduction cascade that triggers the release of mediators of the allergic response.
10917520	5	49	theme	C	912:912	arg1	domain					923:928	one C epsilon3 domain	908:928	one C epsilon3 domain of the IgE-Fc	908:942	The crystal structure reveals that one receptor binds one dimeric IgE-Fc molecule asymmetrically through interactions at two sites, each involving one C epsilon3 domain of the IgE-Fc.
10917520	5	49	theme	C	912:912	arg1	IgE-Fc					937:942	the IgE-Fc	933:942	the IgE-Fc	933:942	The crystal structure reveals that one receptor binds one dimeric IgE-Fc molecule asymmetrically through interactions at two sites, each involving one C epsilon3 domain of the IgE-Fc.
10917520	1	50	theme	antibody	195:202	arg1	binding					180:186	the binding	176:186	the binding of IgE antibody to its high-affinity receptor, Fc epsilonRI	176:246	The initiation of immunoglobulin-E (IgE)-mediated allergic responses requires the binding of IgE antibody to its high-affinity receptor, Fc epsilonRI.
10917520	3	51	theme	key	489:491	arg1	event					505:509	a key recognition event	487:509	a key recognition event of this process	487:525	The interaction of the crystallizable fragment (Fc) of IgE (IgE-Fc) with Fc epsilonRI is a key recognition event of this process and involves the extracellular domains of the Fc epsilonRI alpha-chain.
10917520	3	51	theme	key	489:491	arg1	interaction					402:412	The interaction	398:412	The interaction of the crystallizable fragment (Fc) of IgE (IgE-Fc) with Fc epsilonRI	398:482	The interaction of the crystallizable fragment (Fc) of IgE (IgE-Fc) with Fc epsilonRI is a key recognition event of this process and involves the extracellular domains of the Fc epsilonRI alpha-chain.
10917520	3	52	theme	recognition	493:503	arg1	event					505:509	a key recognition event	487:509	a key recognition event of this process	487:525	The interaction of the crystallizable fragment (Fc) of IgE (IgE-Fc) with Fc epsilonRI is a key recognition event of this process and involves the extracellular domains of the Fc epsilonRI alpha-chain.
10917520	3	52	theme	recognition	493:503	arg1	interaction					402:412	The interaction	398:412	The interaction of the crystallizable fragment (Fc) of IgE (IgE-Fc) with Fc epsilonRI	398:482	The interaction of the crystallizable fragment (Fc) of IgE (IgE-Fc) with Fc epsilonRI is a key recognition event of this process and involves the extracellular domains of the Fc epsilonRI alpha-chain.
10917520	7	53	theme	new	1148:1150	arg1	approaches					1152:1161	new approaches	1148:1161	new approaches to inhibiting the binding of IgE to Fc epsilonRI for the treatment of allergy and asthma	1148:1250	The structure suggests new approaches to inhibiting the binding of IgE to Fc epsilonRI for the treatment of allergy and asthma.
10917520	2	54	theme	signal	305:310	arg1	cascade					325:331	an intracellular signal transduction cascade	288:331	an intracellular signal transduction cascade that triggers the release of mediators of the allergic response	288:395	Crosslinking of Fc epsilonRI initiates an intracellular signal transduction cascade that triggers the release of mediators of the allergic response.
10917520	3	55	theme	IgE	453:455	arg1	Fc					446:447	Fc	446:447	Fc	446:447	The interaction of the crystallizable fragment (Fc) of IgE (IgE-Fc) with Fc epsilonRI is a key recognition event of this process and involves the extracellular domains of the Fc epsilonRI alpha-chain.
10917520	3	55	theme	IgE	453:455	arg1	fragment					436:443	the crystallizable fragment	417:443	the crystallizable fragment (Fc) of IgE (IgE-Fc)	417:464	The interaction of the crystallizable fragment (Fc) of IgE (IgE-Fc) with Fc epsilonRI is a key recognition event of this process and involves the extracellular domains of the Fc epsilonRI alpha-chain.
10917520	3	56	dep	epsilonRI	576:584	arg1	alpha-chain					586:596	alpha-chain	586:596	the Fc epsilonRI alpha-chain	569:596	The interaction of the crystallizable fragment (Fc) of IgE (IgE-Fc) with Fc epsilonRI is a key recognition event of this process and involves the extracellular domains of the Fc epsilonRI alpha-chain.
10917520	2	57	theme	response	388:395	arg1	mediators					362:370	mediators	362:370	mediators of the allergic response	362:395	Crosslinking of Fc epsilonRI initiates an intracellular signal transduction cascade that triggers the release of mediators of the allergic response.
10917520	5	58	theme	epsilon3	914:921	arg1	domain					923:928	one C epsilon3 domain	908:928	one C epsilon3 domain of the IgE-Fc	908:942	The crystal structure reveals that one receptor binds one dimeric IgE-Fc molecule asymmetrically through interactions at two sites, each involving one C epsilon3 domain of the IgE-Fc.
10917520	5	58	theme	epsilon3	914:921	arg1	IgE-Fc					937:942	the IgE-Fc	933:942	the IgE-Fc	933:942	The crystal structure reveals that one receptor binds one dimeric IgE-Fc molecule asymmetrically through interactions at two sites, each involving one C epsilon3 domain of the IgE-Fc.
10917520	3	59	theme	fragment	436:443	arg1	event					505:509	a key recognition event	487:509	a key recognition event of this process	487:525	The interaction of the crystallizable fragment (Fc) of IgE (IgE-Fc) with Fc epsilonRI is a key recognition event of this process and involves the extracellular domains of the Fc epsilonRI alpha-chain.
10917520	3	59	theme	fragment	436:443	arg1	interaction					402:412	The interaction	398:412	The interaction of the crystallizable fragment (Fc) of IgE (IgE-Fc) with Fc epsilonRI	398:482	The interaction of the crystallizable fragment (Fc) of IgE (IgE-Fc) with Fc epsilonRI is a key recognition event of this process and involves the extracellular domains of the Fc epsilonRI alpha-chain.
10917520	6	60	theme	receptor	968:975	arg1	interaction					949:959	The interaction	945:959	The interaction of one receptor with the IgE-Fc	945:991	The interaction of one receptor with the IgE-Fc blocks the binding of a second receptor, and features of this interaction are conserved in other members of the Fc receptor family.
10917520	6	61	with	interaction	949:959	arg1	IgE-Fc					986:991	the IgE-Fc	982:991	the IgE-Fc	982:991	The interaction of one receptor with the IgE-Fc blocks the binding of a second receptor, and features of this interaction are conserved in other members of the Fc receptor family.
10917520	7	62	theme	IgE	1192:1194	arg1	binding					1181:1187	the binding	1177:1187	the binding of IgE to Fc epsilonRI for the treatment of allergy and asthma	1177:1250	The structure suggests new approaches to inhibiting the binding of IgE to Fc epsilonRI for the treatment of allergy and asthma.
10917520	1	63	theme	high-affinity	211:223	arg1	receptor					225:232	its high-affinity receptor	207:232	its high-affinity receptor	207:232	The initiation of immunoglobulin-E (IgE)-mediated allergic responses requires the binding of IgE antibody to its high-affinity receptor, Fc epsilonRI.
10917520	1	63	theme	high-affinity	211:223	arg1	epsilonRI					238:246	Fc epsilonRI	235:246	Fc epsilonRI	235:246	The initiation of immunoglobulin-E (IgE)-mediated allergic responses requires the binding of IgE antibody to its high-affinity receptor, Fc epsilonRI.
19725875	3	0	theme	fluorogenic	365:375	arg1	substrate					445:453	the substrate	441:453	the substrate	441:453	CHIT1 activity can be conveniently measured using fluorogenic 4-methylumbelliferyl (4MU)-chitotrioside or 4MU-chitobioside as the substrate, however, nonsaturating concentrations have to be used because of apparent substrate inhibition.
19725875	3	0	theme	fluorogenic	365:375	arg1	-chitotrioside					403:416	fluorogenic 4-methylumbelliferyl (4MU)-chitotrioside	365:416	fluorogenic 4-methylumbelliferyl (4MU)-chitotrioside	365:416	CHIT1 activity can be conveniently measured using fluorogenic 4-methylumbelliferyl (4MU)-chitotrioside or 4MU-chitobioside as the substrate, however, nonsaturating concentrations have to be used because of apparent substrate inhibition.
19725875	3	0	theme	fluorogenic	365:375	arg1	4MU-chitobioside					421:436	4MU-chitobioside	421:436	4MU-chitobioside	421:436	CHIT1 activity can be conveniently measured using fluorogenic 4-methylumbelliferyl (4MU)-chitotrioside or 4MU-chitobioside as the substrate, however, nonsaturating concentrations have to be used because of apparent substrate inhibition.
19725875	0	1	from	polymorphism	13:24	arg1	chitotriosidase					29:43	chitotriosidase	29:43	chitotriosidase	29:43	Common G102S polymorphism in chitotriosidase differentially affects activity towards 4-methylumbelliferyl substrates.
19725875	6	2	from	common	792:797	arg1	type					802:805	type I Gaucher disease patients in the Netherlands ( approximately 24% of alleles)	802:883	type I Gaucher disease patients in the Netherlands ( approximately 24% of alleles)	802:883	The G102S allele was found to be common in type I Gaucher disease patients in the Netherlands ( approximately 24% of alleles).
19725875	7	3	theme	CHIT1	933:937	arg1	%					959:959	approximately 70%	943:959	approximately 70% that of wild-type Gly102 CHIT1	943:990	The catalytic efficiency of recombinant Ser102 CHIT1 was approximately 70% that of wild-type Gly102 CHIT1 when measured with 4MU-chitotrioside at a nonsaturating concentration.
19725875	7	3	theme	CHIT1	933:937	arg1	CHIT1					986:990	wild-type Gly102 CHIT1	969:990	wild-type Gly102 CHIT1	969:990	The catalytic efficiency of recombinant Ser102 CHIT1 was approximately 70% that of wild-type Gly102 CHIT1 when measured with 4MU-chitotrioside at a nonsaturating concentration.
19725875	7	3	theme	CHIT1	933:937	arg1	efficiency					900:909	The catalytic efficiency	886:909	The catalytic efficiency of recombinant Ser102 CHIT1	886:937	The catalytic efficiency of recombinant Ser102 CHIT1 was approximately 70% that of wild-type Gly102 CHIT1 when measured with 4MU-chitotrioside at a nonsaturating concentration.
19725875	3	4	theme	4-methylumbelliferyl	377:396	arg1	substrate					445:453	the substrate	441:453	the substrate	441:453	CHIT1 activity can be conveniently measured using fluorogenic 4-methylumbelliferyl (4MU)-chitotrioside or 4MU-chitobioside as the substrate, however, nonsaturating concentrations have to be used because of apparent substrate inhibition.
19725875	3	4	theme	4-methylumbelliferyl	377:396	arg1	-chitotrioside					403:416	fluorogenic 4-methylumbelliferyl (4MU)-chitotrioside	365:416	fluorogenic 4-methylumbelliferyl (4MU)-chitotrioside	365:416	CHIT1 activity can be conveniently measured using fluorogenic 4-methylumbelliferyl (4MU)-chitotrioside or 4MU-chitobioside as the substrate, however, nonsaturating concentrations have to be used because of apparent substrate inhibition.
19725875	3	4	theme	4-methylumbelliferyl	377:396	arg1	4MU-chitobioside					421:436	4MU-chitobioside	421:436	4MU-chitobioside	421:436	CHIT1 activity can be conveniently measured using fluorogenic 4-methylumbelliferyl (4MU)-chitotrioside or 4MU-chitobioside as the substrate, however, nonsaturating concentrations have to be used because of apparent substrate inhibition.
19725875	9	5	theme	Ser102	1391:1396	arg1	CHIT1					1398:1402	Ser102 CHIT1	1391:1402	Ser102 CHIT1	1391:1402	In conclusion, interpretation of CHIT1 activity measurements with 4MU-chitotrioside with respect to CHIT1 protein concentrations depends on the presence of Ser102 CHIT1 in an individual, complicating estimation of the body burden of storage macrophages.
19725875	1	6	theme	activated	177:185	arg1	macrophages					187:197	activated macrophages	177:197	activated macrophages	177:197	Chitotriosidase (CHIT1) is a chitinase that is secreted by activated macrophages.
19725875	8	7	with	consistent	1170:1179	arg1	predictions					1186:1196	predictions	1186:1196	predictions from molecular dynamics simulations	1186:1232	However, the activity was normal with 4MU-deoxychitobioside as the substrate at saturating concentrations, consistent with predictions from molecular dynamics simulations.
19725875	8	8	from	simulations	1222:1232	arg1	predictions					1186:1196	predictions	1186:1196	predictions from molecular dynamics simulations	1186:1232	However, the activity was normal with 4MU-deoxychitobioside as the substrate at saturating concentrations, consistent with predictions from molecular dynamics simulations.
19725875	8	9	theme	molecular	1203:1211	arg1	simulations					1222:1232	molecular dynamics simulations	1203:1232	molecular dynamics simulations	1203:1232	However, the activity was normal with 4MU-deoxychitobioside as the substrate at saturating concentrations, consistent with predictions from molecular dynamics simulations.
19725875	9	10	theme	CHIT1	1398:1402	arg1	presence					1379:1386	the presence	1375:1386	the presence of Ser102 CHIT1 in an individual	1375:1419	In conclusion, interpretation of CHIT1 activity measurements with 4MU-chitotrioside with respect to CHIT1 protein concentrations depends on the presence of Ser102 CHIT1 in an individual, complicating estimation of the body burden of storage macrophages.
19725875	10	11	theme	such	1548:1551	arg1	complications					1553:1565	such complications	1548:1565	such complications	1548:1565	Use of the superior 4MU-deoxychitobioside substrate avoids such complications because activity towards this substrate under saturating conditions is not affected by the G102S substitution.
19725875	9	12	theme	CHIT1	1268:1272	arg1	measurements					1283:1294	CHIT1 activity measurements	1268:1294	CHIT1 activity measurements	1268:1294	In conclusion, interpretation of CHIT1 activity measurements with 4MU-chitotrioside with respect to CHIT1 protein concentrations depends on the presence of Ser102 CHIT1 in an individual, complicating estimation of the body burden of storage macrophages.
19725875	7	13	theme	recombinant	914:924	arg1	CHIT1					933:937	recombinant Ser102 CHIT1	914:937	recombinant Ser102 CHIT1	914:937	The catalytic efficiency of recombinant Ser102 CHIT1 was approximately 70% that of wild-type Gly102 CHIT1 when measured with 4MU-chitotrioside at a nonsaturating concentration.
19725875	5	14	theme	catalytic	728:736	arg1	properties					738:747	the catalytic properties	724:747	the catalytic properties of CHIT1	724:756	We studied the impact of a known polymorphism, G102S, on the catalytic properties of CHIT1.
19725875	7	15	theme	CHIT1	986:990	arg1	efficiency					900:909	The catalytic efficiency	886:909	The catalytic efficiency of recombinant Ser102 CHIT1	886:937	The catalytic efficiency of recombinant Ser102 CHIT1 was approximately 70% that of wild-type Gly102 CHIT1 when measured with 4MU-chitotrioside at a nonsaturating concentration.
19725875	7	15	theme	CHIT1	986:990	arg1	CHIT1					986:990	wild-type Gly102 CHIT1	969:990	wild-type Gly102 CHIT1	969:990	The catalytic efficiency of recombinant Ser102 CHIT1 was approximately 70% that of wild-type Gly102 CHIT1 when measured with 4MU-chitotrioside at a nonsaturating concentration.
19725875	7	15	theme	CHIT1	986:990	arg1	%					959:959	approximately 70%	943:959	approximately 70% that of wild-type Gly102 CHIT1	943:990	The catalytic efficiency of recombinant Ser102 CHIT1 was approximately 70% that of wild-type Gly102 CHIT1 when measured with 4MU-chitotrioside at a nonsaturating concentration.
19725875	6	16	dep	patients	825:832	arg1	alleles					876:882	alleles	876:882	alleles	876:882	The G102S allele was found to be common in type I Gaucher disease patients in the Netherlands ( approximately 24% of alleles).
19725875	6	16	dep	patients	825:832	arg1	%					871:871	approximately 24%	855:871	approximately 24% of alleles	855:882	The G102S allele was found to be common in type I Gaucher disease patients in the Netherlands ( approximately 24% of alleles).
19725875	2	17	from	presence	245:252	arg1	patients					284:291	patients	284:291	patients with Gaucher disease	284:312	Plasma chitotriosidase activity reflects the presence of lipid-laden macrophages in patients with Gaucher disease.
19725875	7	18	theme	catalytic	890:898	arg1	%					959:959	approximately 70%	943:959	approximately 70% that of wild-type Gly102 CHIT1	943:990	The catalytic efficiency of recombinant Ser102 CHIT1 was approximately 70% that of wild-type Gly102 CHIT1 when measured with 4MU-chitotrioside at a nonsaturating concentration.
19725875	7	18	theme	catalytic	890:898	arg1	CHIT1					986:990	wild-type Gly102 CHIT1	969:990	wild-type Gly102 CHIT1	969:990	The catalytic efficiency of recombinant Ser102 CHIT1 was approximately 70% that of wild-type Gly102 CHIT1 when measured with 4MU-chitotrioside at a nonsaturating concentration.
19725875	7	18	theme	catalytic	890:898	arg1	efficiency					900:909	The catalytic efficiency	886:909	The catalytic efficiency of recombinant Ser102 CHIT1	886:937	The catalytic efficiency of recombinant Ser102 CHIT1 was approximately 70% that of wild-type Gly102 CHIT1 when measured with 4MU-chitotrioside at a nonsaturating concentration.
19725875	4	19	used	used	605:608	arg2	concentrations					573:586	Saturating substrate concentrations	552:586	Saturating substrate concentrations	552:586	Saturating substrate concentrations can, however, be used with the newly designed substrate 4MU-deoxychitobioside.
19725875	7	20	dep	%	959:959	arg1	that					961:964	that	961:964	that	961:964	The catalytic efficiency of recombinant Ser102 CHIT1 was approximately 70% that of wild-type Gly102 CHIT1 when measured with 4MU-chitotrioside at a nonsaturating concentration.
19725875	3	21	used	used	505:508	arg2	concentrations					479:492	nonsaturating concentrations	465:492	nonsaturating concentrations	465:492	CHIT1 activity can be conveniently measured using fluorogenic 4-methylumbelliferyl (4MU)-chitotrioside or 4MU-chitobioside as the substrate, however, nonsaturating concentrations have to be used because of apparent substrate inhibition.
19725875	9	22	attach	presence	1379:1386	arg1	individual					1410:1419	an individual	1407:1419	an individual	1407:1419	In conclusion, interpretation of CHIT1 activity measurements with 4MU-chitotrioside with respect to CHIT1 protein concentrations depends on the presence of Ser102 CHIT1 in an individual, complicating estimation of the body burden of storage macrophages.
19725875	9	22	attach	presence	1379:1386	arg2	CHIT1					1398:1402	Ser102 CHIT1	1391:1402	Ser102 CHIT1	1391:1402	In conclusion, interpretation of CHIT1 activity measurements with 4MU-chitotrioside with respect to CHIT1 protein concentrations depends on the presence of Ser102 CHIT1 in an individual, complicating estimation of the body burden of storage macrophages.
19725875	4	23	theme	substrate	563:571	arg1	concentrations					573:586	Saturating substrate concentrations	552:586	Saturating substrate concentrations	552:586	Saturating substrate concentrations can, however, be used with the newly designed substrate 4MU-deoxychitobioside.
19725875	5	24	theme	polymorphism	700:711	arg1	impact					682:687	the impact	678:687	the impact of a known polymorphism, G102S, on the catalytic properties of CHIT1	678:756	We studied the impact of a known polymorphism, G102S, on the catalytic properties of CHIT1.
19725875	7	25	theme	wild-type	969:977	arg1	CHIT1					986:990	wild-type Gly102 CHIT1	969:990	wild-type Gly102 CHIT1	969:990	The catalytic efficiency of recombinant Ser102 CHIT1 was approximately 70% that of wild-type Gly102 CHIT1 when measured with 4MU-chitotrioside at a nonsaturating concentration.
19725875	10	26	theme	substrate	1531:1539	arg1	Use					1489:1491	Use	1489:1491	Use of the superior 4MU-deoxychitobioside substrate	1489:1539	Use of the superior 4MU-deoxychitobioside substrate avoids such complications because activity towards this substrate under saturating conditions is not affected by the G102S substitution.
19725875	6	27	theme	G102S	763:767	arg1	common					792:797	common	792:797	common	792:797	The G102S allele was found to be common in type I Gaucher disease patients in the Netherlands ( approximately 24% of alleles).
19725875	6	27	theme	G102S	763:767	arg1	allele					769:774	The G102S allele	759:774	The G102S allele	759:774	The G102S allele was found to be common in type I Gaucher disease patients in the Netherlands ( approximately 24% of alleles).
19725875	2	28	attach	presence	245:252	arg1	patients					284:291	patients	284:291	patients with Gaucher disease	284:312	Plasma chitotriosidase activity reflects the presence of lipid-laden macrophages in patients with Gaucher disease.
19725875	2	28	attach	presence	245:252	arg2	macrophages					269:279	lipid-laden macrophages	257:279	lipid-laden macrophages	257:279	Plasma chitotriosidase activity reflects the presence of lipid-laden macrophages in patients with Gaucher disease.
19725875	0	29	theme	G102S	7:11	arg1	polymorphism					13:24	Common G102S polymorphism	0:24	Common G102S polymorphism in chitotriosidase	0:43	Common G102S polymorphism in chitotriosidase differentially affects activity towards 4-methylumbelliferyl substrates.
19725875	4	30	theme	Saturating	552:561	arg1	concentrations					573:586	Saturating substrate concentrations	552:586	Saturating substrate concentrations	552:586	Saturating substrate concentrations can, however, be used with the newly designed substrate 4MU-deoxychitobioside.
19725875	7	31	theme	Gly102	979:984	arg1	CHIT1					986:990	wild-type Gly102 CHIT1	969:990	wild-type Gly102 CHIT1	969:990	The catalytic efficiency of recombinant Ser102 CHIT1 was approximately 70% that of wild-type Gly102 CHIT1 when measured with 4MU-chitotrioside at a nonsaturating concentration.
19725875	0	32	theme	Common	0:5	arg1	polymorphism					13:24	Common G102S polymorphism	0:24	Common G102S polymorphism in chitotriosidase	0:43	Common G102S polymorphism in chitotriosidase differentially affects activity towards 4-methylumbelliferyl substrates.
19725875	10	33	theme	superior	1500:1507	arg1	substrate					1531:1539	the superior 4MU-deoxychitobioside substrate	1496:1539	the superior 4MU-deoxychitobioside substrate	1496:1539	Use of the superior 4MU-deoxychitobioside substrate avoids such complications because activity towards this substrate under saturating conditions is not affected by the G102S substitution.
19725875	5	34	theme	known	694:698	arg1	G102S					714:718	G102S	714:718	G102S	714:718	We studied the impact of a known polymorphism, G102S, on the catalytic properties of CHIT1.
19725875	5	34	theme	known	694:698	arg1	polymorphism					700:711	a known polymorphism	692:711	a known polymorphism	692:711	We studied the impact of a known polymorphism, G102S, on the catalytic properties of CHIT1.
19725875	6	35	theme	disease	817:823	arg1	patients					825:832	Gaucher disease patients	809:832	type I Gaucher disease patients in the Netherlands ( approximately 24% of alleles)	802:883	The G102S allele was found to be common in type I Gaucher disease patients in the Netherlands ( approximately 24% of alleles).
19725875	3	36	theme	apparent	521:528	arg1	inhibition					540:549	apparent substrate inhibition	521:549	apparent substrate inhibition	521:549	CHIT1 activity can be conveniently measured using fluorogenic 4-methylumbelliferyl (4MU)-chitotrioside or 4MU-chitobioside as the substrate, however, nonsaturating concentrations have to be used because of apparent substrate inhibition.
19725875	7	37	theme	nonsaturating	1034:1046	arg1	concentration					1048:1060	a nonsaturating concentration	1032:1060	a nonsaturating concentration	1032:1060	The catalytic efficiency of recombinant Ser102 CHIT1 was approximately 70% that of wild-type Gly102 CHIT1 when measured with 4MU-chitotrioside at a nonsaturating concentration.
19725875	4	38	theme	substrate	634:642	arg1	4MU-deoxychitobioside					644:664	the newly designed substrate 4MU-deoxychitobioside	615:664	the newly designed substrate 4MU-deoxychitobioside	615:664	Saturating substrate concentrations can, however, be used with the newly designed substrate 4MU-deoxychitobioside.
19725875	2	39	theme	chitotriosidase	207:221	arg1	activity					223:230	Plasma chitotriosidase activity	200:230	Plasma chitotriosidase activity	200:230	Plasma chitotriosidase activity reflects the presence of lipid-laden macrophages in patients with Gaucher disease.
19725875	5	40	from	impact	682:687	arg1	properties					738:747	the catalytic properties	724:747	the catalytic properties of CHIT1	724:756	We studied the impact of a known polymorphism, G102S, on the catalytic properties of CHIT1.
19725875	3	41	theme	substrate	530:538	arg1	inhibition					540:549	apparent substrate inhibition	521:549	apparent substrate inhibition	521:549	CHIT1 activity can be conveniently measured using fluorogenic 4-methylumbelliferyl (4MU)-chitotrioside or 4MU-chitobioside as the substrate, however, nonsaturating concentrations have to be used because of apparent substrate inhibition.
19725875	3	42	theme	nonsaturating	465:477	arg1	concentrations					479:492	nonsaturating concentrations	465:492	nonsaturating concentrations	465:492	CHIT1 activity can be conveniently measured using fluorogenic 4-methylumbelliferyl (4MU)-chitotrioside or 4MU-chitobioside as the substrate, however, nonsaturating concentrations have to be used because of apparent substrate inhibition.
19725875	4	43	theme	designed	625:632	arg1	4MU-deoxychitobioside					644:664	the newly designed substrate 4MU-deoxychitobioside	615:664	the newly designed substrate 4MU-deoxychitobioside	615:664	Saturating substrate concentrations can, however, be used with the newly designed substrate 4MU-deoxychitobioside.
19725875	10	44	theme	saturating	1613:1622	arg1	conditions					1624:1633	saturating conditions	1613:1633	saturating conditions	1613:1633	Use of the superior 4MU-deoxychitobioside substrate avoids such complications because activity towards this substrate under saturating conditions is not affected by the G102S substitution.
19725875	2	45	theme	Plasma	200:205	arg1	activity					223:230	Plasma chitotriosidase activity	200:230	Plasma chitotriosidase activity	200:230	Plasma chitotriosidase activity reflects the presence of lipid-laden macrophages in patients with Gaucher disease.
19725875	8	46	with	normal	1089:1094	arg1	4MU-deoxychitobioside					1101:1121	4MU-deoxychitobioside	1101:1121	4MU-deoxychitobioside	1101:1121	However, the activity was normal with 4MU-deoxychitobioside as the substrate at saturating concentrations, consistent with predictions from molecular dynamics simulations.
19725875	9	47	theme	body	1453:1456	arg1	burden					1458:1463	the body burden	1449:1463	the body burden of storage macrophages	1449:1486	In conclusion, interpretation of CHIT1 activity measurements with 4MU-chitotrioside with respect to CHIT1 protein concentrations depends on the presence of Ser102 CHIT1 in an individual, complicating estimation of the body burden of storage macrophages.
19725875	3	48	theme	CHIT1	315:319	arg1	activity					321:328	CHIT1 activity	315:328	CHIT1 activity	315:328	CHIT1 activity can be conveniently measured using fluorogenic 4-methylumbelliferyl (4MU)-chitotrioside or 4MU-chitobioside as the substrate, however, nonsaturating concentrations have to be used because of apparent substrate inhibition.
19725875	8	49	theme	dynamics	1213:1220	arg1	simulations					1222:1232	molecular dynamics simulations	1203:1232	molecular dynamics simulations	1203:1232	However, the activity was normal with 4MU-deoxychitobioside as the substrate at saturating concentrations, consistent with predictions from molecular dynamics simulations.
19725875	2	50	theme	macrophages	269:279	arg1	presence					245:252	the presence	241:252	the presence of lipid-laden macrophages in patients with Gaucher disease	241:312	Plasma chitotriosidase activity reflects the presence of lipid-laden macrophages in patients with Gaucher disease.
19725875	6	51	theme	Gaucher	809:815	arg1	patients					825:832	Gaucher disease patients	809:832	type I Gaucher disease patients in the Netherlands ( approximately 24% of alleles)	802:883	The G102S allele was found to be common in type I Gaucher disease patients in the Netherlands ( approximately 24% of alleles).
19725875	9	52	from	presence	1379:1386	arg1	individual					1410:1419	an individual	1407:1419	an individual	1407:1419	In conclusion, interpretation of CHIT1 activity measurements with 4MU-chitotrioside with respect to CHIT1 protein concentrations depends on the presence of Ser102 CHIT1 in an individual, complicating estimation of the body burden of storage macrophages.
19725875	2	53	with	patients	284:291	arg1	disease					306:312	Gaucher disease	298:312	Gaucher disease	298:312	Plasma chitotriosidase activity reflects the presence of lipid-laden macrophages in patients with Gaucher disease.
19725875	9	54	theme	protein	1341:1347	arg1	concentrations					1349:1362	CHIT1 protein concentrations	1335:1362	CHIT1 protein concentrations	1335:1362	In conclusion, interpretation of CHIT1 activity measurements with 4MU-chitotrioside with respect to CHIT1 protein concentrations depends on the presence of Ser102 CHIT1 in an individual, complicating estimation of the body burden of storage macrophages.
19725875	2	55	theme	lipid-laden	257:267	arg1	macrophages					269:279	lipid-laden macrophages	257:279	lipid-laden macrophages	257:279	Plasma chitotriosidase activity reflects the presence of lipid-laden macrophages in patients with Gaucher disease.
19725875	6	56	from	type	802:805	arg1	common					792:797	common	792:797	common	792:797	The G102S allele was found to be common in type I Gaucher disease patients in the Netherlands ( approximately 24% of alleles).
19725875	6	56	from	type	802:805	arg1	allele					769:774	The G102S allele	759:774	The G102S allele	759:774	The G102S allele was found to be common in type I Gaucher disease patients in the Netherlands ( approximately 24% of alleles).
19725875	8	57	theme	saturating	1143:1152	arg1	concentrations					1154:1167	saturating concentrations	1143:1167	saturating concentrations	1143:1167	However, the activity was normal with 4MU-deoxychitobioside as the substrate at saturating concentrations, consistent with predictions from molecular dynamics simulations.
19725875	9	58	with	interpretation	1250:1263	arg1	4MU-chitotrioside					1301:1317	4MU-chitotrioside	1301:1317	4MU-chitotrioside with respect to CHIT1 protein concentrations	1301:1362	In conclusion, interpretation of CHIT1 activity measurements with 4MU-chitotrioside with respect to CHIT1 protein concentrations depends on the presence of Ser102 CHIT1 in an individual, complicating estimation of the body burden of storage macrophages.
19725875	9	59	theme	CHIT1	1335:1339	arg1	concentrations					1349:1362	CHIT1 protein concentrations	1335:1362	CHIT1 protein concentrations	1335:1362	In conclusion, interpretation of CHIT1 activity measurements with 4MU-chitotrioside with respect to CHIT1 protein concentrations depends on the presence of Ser102 CHIT1 in an individual, complicating estimation of the body burden of storage macrophages.
19725875	9	60	theme	storage	1468:1474	arg1	macrophages					1476:1486	storage macrophages	1468:1486	storage macrophages	1468:1486	In conclusion, interpretation of CHIT1 activity measurements with 4MU-chitotrioside with respect to CHIT1 protein concentrations depends on the presence of Ser102 CHIT1 in an individual, complicating estimation of the body burden of storage macrophages.
19725875	5	61	theme	CHIT1	752:756	arg1	properties					738:747	the catalytic properties	724:747	the catalytic properties of CHIT1	724:756	We studied the impact of a known polymorphism, G102S, on the catalytic properties of CHIT1.
19725875	6	62	theme	alleles	876:882	arg1	alleles					876:882	alleles	876:882	alleles	876:882	The G102S allele was found to be common in type I Gaucher disease patients in the Netherlands ( approximately 24% of alleles).
19725875	6	62	theme	alleles	876:882	arg1	%					871:871	approximately 24%	855:871	approximately 24% of alleles	855:882	The G102S allele was found to be common in type I Gaucher disease patients in the Netherlands ( approximately 24% of alleles).
19725875	9	63	theme	measurements	1283:1294	arg1	interpretation					1250:1263	interpretation	1250:1263	interpretation of CHIT1 activity measurements with 4MU-chitotrioside with respect to CHIT1 protein concentrations	1250:1362	In conclusion, interpretation of CHIT1 activity measurements with 4MU-chitotrioside with respect to CHIT1 protein concentrations depends on the presence of Ser102 CHIT1 in an individual, complicating estimation of the body burden of storage macrophages.
19725875	7	64	theme	Ser102	926:931	arg1	CHIT1					933:937	recombinant Ser102 CHIT1	914:937	recombinant Ser102 CHIT1	914:937	The catalytic efficiency of recombinant Ser102 CHIT1 was approximately 70% that of wild-type Gly102 CHIT1 when measured with 4MU-chitotrioside at a nonsaturating concentration.
19725875	8	65	from	concentrations	1154:1167	arg1	normal					1089:1094	normal	1089:1094	normal	1089:1094	However, the activity was normal with 4MU-deoxychitobioside as the substrate at saturating concentrations, consistent with predictions from molecular dynamics simulations.
19725875	8	65	from	concentrations	1154:1167	arg1	activity					1076:1083	the activity	1072:1083	the activity	1072:1083	However, the activity was normal with 4MU-deoxychitobioside as the substrate at saturating concentrations, consistent with predictions from molecular dynamics simulations.
19725875	2	66	theme	Gaucher	298:304	arg1	disease					306:312	Gaucher disease	298:312	Gaucher disease	298:312	Plasma chitotriosidase activity reflects the presence of lipid-laden macrophages in patients with Gaucher disease.
19725875	9	67	theme	activity	1274:1281	arg1	measurements					1283:1294	CHIT1 activity measurements	1268:1294	CHIT1 activity measurements	1268:1294	In conclusion, interpretation of CHIT1 activity measurements with 4MU-chitotrioside with respect to CHIT1 protein concentrations depends on the presence of Ser102 CHIT1 in an individual, complicating estimation of the body burden of storage macrophages.
19725875	0	68	theme	4-methylumbelliferyl	85:104	arg1	substrates					106:115	4-methylumbelliferyl substrates	85:115	4-methylumbelliferyl substrates	85:115	Common G102S polymorphism in chitotriosidase differentially affects activity towards 4-methylumbelliferyl substrates.
19725875	6	69	from	patients	825:832	arg1	Netherlands					841:851	the Netherlands	837:851	the Netherlands	837:851	The G102S allele was found to be common in type I Gaucher disease patients in the Netherlands ( approximately 24% of alleles).
19725875	10	70	theme	G102S	1658:1662	arg1	substitution					1664:1675	the G102S substitution	1654:1675	the G102S substitution	1654:1675	Use of the superior 4MU-deoxychitobioside substrate avoids such complications because activity towards this substrate under saturating conditions is not affected by the G102S substitution.
19725875	3	71	theme	4MU	399:401	arg1	substrate					445:453	the substrate	441:453	the substrate	441:453	CHIT1 activity can be conveniently measured using fluorogenic 4-methylumbelliferyl (4MU)-chitotrioside or 4MU-chitobioside as the substrate, however, nonsaturating concentrations have to be used because of apparent substrate inhibition.
19725875	3	71	theme	4MU	399:401	arg1	-chitotrioside					403:416	fluorogenic 4-methylumbelliferyl (4MU)-chitotrioside	365:416	fluorogenic 4-methylumbelliferyl (4MU)-chitotrioside	365:416	CHIT1 activity can be conveniently measured using fluorogenic 4-methylumbelliferyl (4MU)-chitotrioside or 4MU-chitobioside as the substrate, however, nonsaturating concentrations have to be used because of apparent substrate inhibition.
19725875	3	71	theme	4MU	399:401	arg1	4MU-chitobioside					421:436	4MU-chitobioside	421:436	4MU-chitobioside	421:436	CHIT1 activity can be conveniently measured using fluorogenic 4-methylumbelliferyl (4MU)-chitotrioside or 4MU-chitobioside as the substrate, however, nonsaturating concentrations have to be used because of apparent substrate inhibition.
19725875	10	72	theme	4MU-deoxychitobioside	1509:1529	arg1	substrate					1531:1539	the superior 4MU-deoxychitobioside substrate	1496:1539	the superior 4MU-deoxychitobioside substrate	1496:1539	Use of the superior 4MU-deoxychitobioside substrate avoids such complications because activity towards this substrate under saturating conditions is not affected by the G102S substitution.
19725875	9	73	theme	macrophages	1476:1486	arg1	burden					1458:1463	the body burden	1449:1463	the body burden of storage macrophages	1449:1486	In conclusion, interpretation of CHIT1 activity measurements with 4MU-chitotrioside with respect to CHIT1 protein concentrations depends on the presence of Ser102 CHIT1 in an individual, complicating estimation of the body burden of storage macrophages.
19725875	6	74	dep	type	802:805	arg1	patients					825:832	Gaucher disease patients	809:832	type I Gaucher disease patients in the Netherlands ( approximately 24% of alleles)	802:883	The G102S allele was found to be common in type I Gaucher disease patients in the Netherlands ( approximately 24% of alleles).
19725875	9	75	theme	burden	1458:1463	arg1	estimation					1435:1444	estimation	1435:1444	estimation of the body burden of storage macrophages	1435:1486	In conclusion, interpretation of CHIT1 activity measurements with 4MU-chitotrioside with respect to CHIT1 protein concentrations depends on the presence of Ser102 CHIT1 in an individual, complicating estimation of the body burden of storage macrophages.
9597769	0	0	theme	mass	73:76	arg1	spectrometry					78:89	QTOF ESI mass spectrometry	64:89	QTOF ESI mass spectrometry	64:89	Localization of O-glycosylation sites of MUC1 tandem repeats by QTOF ESI mass spectrometry.
9597769	2	1	theme	overlapping	468:478	arg1	sequence					480:487	an overlapping sequence	465:487	an overlapping sequence of MUC1 tandem repeats which had been glycosylated in vitro by two GalNAc residues in the positions T9 and T21	465:598	The location of O-glycosylation sites was possible in the positive ion (+) mode by detection of prominent y- and b-fragment ions from the underivatized TAP25-2 [T1APPAHGVT9S10APDT14RPAPGS20T21APPA], an overlapping sequence of MUC1 tandem repeats which had been glycosylated in vitro by two GalNAc residues in the positions T9 and T21.
9597769	2	1	theme	overlapping	468:478	arg1	detection					349:357	detection	349:357	detection of prominent y- and b-fragment ions from the underivatized TAP25-2 [T1APPAHGVT9S10APDT14RPAPGS20T21APPA]	349:462	The location of O-glycosylation sites was possible in the positive ion (+) mode by detection of prominent y- and b-fragment ions from the underivatized TAP25-2 [T1APPAHGVT9S10APDT14RPAPGS20T21APPA], an overlapping sequence of MUC1 tandem repeats which had been glycosylated in vitro by two GalNAc residues in the positions T9 and T21.
9597769	4	2	theme	mass	815:818	arg1	approach					834:841	an alternative mass spectrometric approach	800:841	an alternative mass spectrometric approach	800:841	The reduced complexity of the fragment spectra and the higher signal-to-noise ratio render QTOF-(+)ESMS an alternative mass spectrometric approach to the identification of O-glycosylation sites when compared with sequencing by post-source decay matrix-assisted laser desorption/ionization MS. Diagnostic ions from the N-terminus in the b-series offered direct evidence, which was supported by indirect evidence from the C-terminus ions of the y-series.
9597769	3	3	theme	reliable	663:670	arg1	assignments					683:693	reliable structural assignments	663:693	reliable structural assignments	663:693	The high mass resolution and accuracy of QTOF-(+)ESMS allowed reliable structural assignments.
9597769	3	4	theme	structural	672:681	arg1	assignments					683:693	reliable structural assignments	663:693	reliable structural assignments	663:693	The high mass resolution and accuracy of QTOF-(+)ESMS allowed reliable structural assignments.
9597769	0	5	theme	ESI	69:71	arg1	spectrometry					78:89	QTOF ESI mass spectrometry	64:89	QTOF ESI mass spectrometry	64:89	Localization of O-glycosylation sites of MUC1 tandem repeats by QTOF ESI mass spectrometry.
9597769	4	6	theme	alternative	803:813	arg1	approach					834:841	an alternative mass spectrometric approach	800:841	an alternative mass spectrometric approach	800:841	The reduced complexity of the fragment spectra and the higher signal-to-noise ratio render QTOF-(+)ESMS an alternative mass spectrometric approach to the identification of O-glycosylation sites when compared with sequencing by post-source decay matrix-assisted laser desorption/ionization MS. Diagnostic ions from the N-terminus in the b-series offered direct evidence, which was supported by indirect evidence from the C-terminus ions of the y-series.
9597769	2	7	theme	MUC1	492:495	arg1	repeats					504:510	MUC1 tandem repeats	492:510	MUC1 tandem repeats	492:510	The location of O-glycosylation sites was possible in the positive ion (+) mode by detection of prominent y- and b-fragment ions from the underivatized TAP25-2 [T1APPAHGVT9S10APDT14RPAPGS20T21APPA], an overlapping sequence of MUC1 tandem repeats which had been glycosylated in vitro by two GalNAc residues in the positions T9 and T21.
9597769	5	8	dep	glycosylated	1160:1171	arg1	higher					1153:1158	higher	1153:1158	higher	1153:1158	The higher glycosylated GalNAc2-substituted fragments were mainly observed as multiply ionized species.
9597769	1	9	gly	glycopeptides	169:181	arg2	glycopeptides					169:181	glycopeptides	169:181	glycopeptides	169:181	The potential of electrospray mass spectrometry (ESMS) for the sequencing of glycopeptides was evaluated using quadrupole time-of-flight (QTOF) technology in the MS/MS mode.
9597769	2	10	from	possible	308:315	arg1	mode					341:344	the positive ion (+) mode	320:344	mode	341:344	The location of O-glycosylation sites was possible in the positive ion (+) mode by detection of prominent y- and b-fragment ions from the underivatized TAP25-2 [T1APPAHGVT9S10APDT14RPAPGS20T21APPA], an overlapping sequence of MUC1 tandem repeats which had been glycosylated in vitro by two GalNAc residues in the positions T9 and T21.
9597769	2	10	from	possible	308:315	arg1	ion					333:335	the positive ion (+) mode	320:344	ion	333:335	The location of O-glycosylation sites was possible in the positive ion (+) mode by detection of prominent y- and b-fragment ions from the underivatized TAP25-2 [T1APPAHGVT9S10APDT14RPAPGS20T21APPA], an overlapping sequence of MUC1 tandem repeats which had been glycosylated in vitro by two GalNAc residues in the positions T9 and T21.
9597769	4	11	theme	direct	1049:1054	arg1	evidence					1056:1063	the b-series offered direct evidence	1028:1063	the b-series offered direct evidence	1028:1063	The reduced complexity of the fragment spectra and the higher signal-to-noise ratio render QTOF-(+)ESMS an alternative mass spectrometric approach to the identification of O-glycosylation sites when compared with sequencing by post-source decay matrix-assisted laser desorption/ionization MS. Diagnostic ions from the N-terminus in the b-series offered direct evidence, which was supported by indirect evidence from the C-terminus ions of the y-series.
9597769	4	12	theme	laser	957:961	arg1	desorption/ionization					963:983	matrix-assisted laser desorption/ionization	941:983	sequencing by post-source decay matrix-assisted laser desorption/ionization MS. Diagnostic ions from the N-terminus in the b-series offered direct evidence, which was supported by indirect evidence from the C-terminus ions of the y-series	909:1146	The reduced complexity of the fragment spectra and the higher signal-to-noise ratio render QTOF-(+)ESMS an alternative mass spectrometric approach to the identification of O-glycosylation sites when compared with sequencing by post-source decay matrix-assisted laser desorption/ionization MS. Diagnostic ions from the N-terminus in the b-series offered direct evidence, which was supported by indirect evidence from the C-terminus ions of the y-series.
9597769	2	13	theme	repeats	504:510	arg1	sequence					480:487	an overlapping sequence	465:487	an overlapping sequence of MUC1 tandem repeats which had been glycosylated in vitro by two GalNAc residues in the positions T9 and T21	465:598	The location of O-glycosylation sites was possible in the positive ion (+) mode by detection of prominent y- and b-fragment ions from the underivatized TAP25-2 [T1APPAHGVT9S10APDT14RPAPGS20T21APPA], an overlapping sequence of MUC1 tandem repeats which had been glycosylated in vitro by two GalNAc residues in the positions T9 and T21.
9597769	2	13	theme	repeats	504:510	arg1	detection					349:357	detection	349:357	detection of prominent y- and b-fragment ions from the underivatized TAP25-2 [T1APPAHGVT9S10APDT14RPAPGS20T21APPA]	349:462	The location of O-glycosylation sites was possible in the positive ion (+) mode by detection of prominent y- and b-fragment ions from the underivatized TAP25-2 [T1APPAHGVT9S10APDT14RPAPGS20T21APPA], an overlapping sequence of MUC1 tandem repeats which had been glycosylated in vitro by two GalNAc residues in the positions T9 and T21.
9597769	2	14	from	[T1APPAHGVT9S10APDT14RPAPGS20T21APPA	426:461	arg1	detection					349:357	detection	349:357	detection of prominent y- and b-fragment ions from the underivatized TAP25-2 [T1APPAHGVT9S10APDT14RPAPGS20T21APPA]	349:462	The location of O-glycosylation sites was possible in the positive ion (+) mode by detection of prominent y- and b-fragment ions from the underivatized TAP25-2 [T1APPAHGVT9S10APDT14RPAPGS20T21APPA], an overlapping sequence of MUC1 tandem repeats which had been glycosylated in vitro by two GalNAc residues in the positions T9 and T21.
9597769	2	14	from	[T1APPAHGVT9S10APDT14RPAPGS20T21APPA	426:461	arg1	sequence					480:487	an overlapping sequence	465:487	an overlapping sequence of MUC1 tandem repeats which had been glycosylated in vitro by two GalNAc residues in the positions T9 and T21	465:598	The location of O-glycosylation sites was possible in the positive ion (+) mode by detection of prominent y- and b-fragment ions from the underivatized TAP25-2 [T1APPAHGVT9S10APDT14RPAPGS20T21APPA], an overlapping sequence of MUC1 tandem repeats which had been glycosylated in vitro by two GalNAc residues in the positions T9 and T21.
9597769	2	14	from	[T1APPAHGVT9S10APDT14RPAPGS20T21APPA	426:461	arg1	ions					390:393	prominent y- and b-fragment ions	362:393	prominent y- and b-fragment ions from the underivatized TAP25-2 [T1APPAHGVT9S10APDT14RPAPGS20T21APPA	362:461	The location of O-glycosylation sites was possible in the positive ion (+) mode by detection of prominent y- and b-fragment ions from the underivatized TAP25-2 [T1APPAHGVT9S10APDT14RPAPGS20T21APPA], an overlapping sequence of MUC1 tandem repeats which had been glycosylated in vitro by two GalNAc residues in the positions T9 and T21.
9597769	4	15	theme	spectrometric	820:832	arg1	approach					834:841	an alternative mass spectrometric approach	800:841	an alternative mass spectrometric approach	800:841	The reduced complexity of the fragment spectra and the higher signal-to-noise ratio render QTOF-(+)ESMS an alternative mass spectrometric approach to the identification of O-glycosylation sites when compared with sequencing by post-source decay matrix-assisted laser desorption/ionization MS. Diagnostic ions from the N-terminus in the b-series offered direct evidence, which was supported by indirect evidence from the C-terminus ions of the y-series.
9597769	4	16	theme	C-terminus	1116:1125	arg1	ions					1127:1130	the C-terminus ions	1112:1130	the C-terminus ions of the y-series	1112:1146	The reduced complexity of the fragment spectra and the higher signal-to-noise ratio render QTOF-(+)ESMS an alternative mass spectrometric approach to the identification of O-glycosylation sites when compared with sequencing by post-source decay matrix-assisted laser desorption/ionization MS. Diagnostic ions from the N-terminus in the b-series offered direct evidence, which was supported by indirect evidence from the C-terminus ions of the y-series.
9597769	1	17	theme	MS/MS	254:258	arg1	mode					260:263	the MS/MS mode	250:263	the MS/MS mode	250:263	The potential of electrospray mass spectrometry (ESMS) for the sequencing of glycopeptides was evaluated using quadrupole time-of-flight (QTOF) technology in the MS/MS mode.
9597769	2	18	theme	tandem	497:502	arg1	repeats					504:510	MUC1 tandem repeats	492:510	MUC1 tandem repeats	492:510	The location of O-glycosylation sites was possible in the positive ion (+) mode by detection of prominent y- and b-fragment ions from the underivatized TAP25-2 [T1APPAHGVT9S10APDT14RPAPGS20T21APPA], an overlapping sequence of MUC1 tandem repeats which had been glycosylated in vitro by two GalNAc residues in the positions T9 and T21.
9597769	4	19	gly	O-glycosylation	868:882	arg2	sites					884:888	O-glycosylation sites	868:888	O-glycosylation sites	868:888	The reduced complexity of the fragment spectra and the higher signal-to-noise ratio render QTOF-(+)ESMS an alternative mass spectrometric approach to the identification of O-glycosylation sites when compared with sequencing by post-source decay matrix-assisted laser desorption/ionization MS. Diagnostic ions from the N-terminus in the b-series offered direct evidence, which was supported by indirect evidence from the C-terminus ions of the y-series.
9597769	4	20	theme	b-series	1032:1039	arg1	evidence					1056:1063	the b-series offered direct evidence	1028:1063	the b-series offered direct evidence	1028:1063	The reduced complexity of the fragment spectra and the higher signal-to-noise ratio render QTOF-(+)ESMS an alternative mass spectrometric approach to the identification of O-glycosylation sites when compared with sequencing by post-source decay matrix-assisted laser desorption/ionization MS. Diagnostic ions from the N-terminus in the b-series offered direct evidence, which was supported by indirect evidence from the C-terminus ions of the y-series.
9597769	4	21	theme	spectra	735:741	arg1	complexity					708:717	The reduced complexity	696:717	The reduced complexity of the fragment spectra	696:741	The reduced complexity of the fragment spectra and the higher signal-to-noise ratio render QTOF-(+)ESMS an alternative mass spectrometric approach to the identification of O-glycosylation sites when compared with sequencing by post-source decay matrix-assisted laser desorption/ionization MS. Diagnostic ions from the N-terminus in the b-series offered direct evidence, which was supported by indirect evidence from the C-terminus ions of the y-series.
9597769	4	21	theme	spectra	735:741	arg1	ratio					774:778	the higher signal-to-noise ratio	747:778	the higher signal-to-noise ratio	747:778	The reduced complexity of the fragment spectra and the higher signal-to-noise ratio render QTOF-(+)ESMS an alternative mass spectrometric approach to the identification of O-glycosylation sites when compared with sequencing by post-source decay matrix-assisted laser desorption/ionization MS. Diagnostic ions from the N-terminus in the b-series offered direct evidence, which was supported by indirect evidence from the C-terminus ions of the y-series.
9597769	2	22	theme	TAP25-2	418:424	arg1	[T1APPAHGVT9S10APDT14RPAPGS20T21APPA					426:461	the underivatized TAP25-2 [T1APPAHGVT9S10APDT14RPAPGS20T21APPA	400:461	the underivatized TAP25-2 [T1APPAHGVT9S10APDT14RPAPGS20T21APPA	400:461	The location of O-glycosylation sites was possible in the positive ion (+) mode by detection of prominent y- and b-fragment ions from the underivatized TAP25-2 [T1APPAHGVT9S10APDT14RPAPGS20T21APPA], an overlapping sequence of MUC1 tandem repeats which had been glycosylated in vitro by two GalNAc residues in the positions T9 and T21.
9597769	4	23	theme	Diagnostic	989:998	arg1	ions					1000:1003	Diagnostic ions	989:1003	Diagnostic ions	989:1003	The reduced complexity of the fragment spectra and the higher signal-to-noise ratio render QTOF-(+)ESMS an alternative mass spectrometric approach to the identification of O-glycosylation sites when compared with sequencing by post-source decay matrix-assisted laser desorption/ionization MS. Diagnostic ions from the N-terminus in the b-series offered direct evidence, which was supported by indirect evidence from the C-terminus ions of the y-series.
9597769	5	24	theme	GalNAc2-substituted	1173:1191	arg1	species					1244:1250	multiply ionized species	1227:1250	multiply ionized species	1227:1250	The higher glycosylated GalNAc2-substituted fragments were mainly observed as multiply ionized species.
9597769	5	24	theme	GalNAc2-substituted	1173:1191	arg1	fragments					1193:1201	The higher glycosylated GalNAc2-substituted fragments	1149:1201	The higher glycosylated GalNAc2-substituted fragments	1149:1201	The higher glycosylated GalNAc2-substituted fragments were mainly observed as multiply ionized species.
9597769	4	25	theme	fragment	726:733	arg1	spectra					735:741	the fragment spectra	722:741	the fragment spectra	722:741	The reduced complexity of the fragment spectra and the higher signal-to-noise ratio render QTOF-(+)ESMS an alternative mass spectrometric approach to the identification of O-glycosylation sites when compared with sequencing by post-source decay matrix-assisted laser desorption/ionization MS. Diagnostic ions from the N-terminus in the b-series offered direct evidence, which was supported by indirect evidence from the C-terminus ions of the y-series.
9597769	4	26	theme	post-source	923:933	arg1	decay					935:939	post-source decay	923:939	post-source decay	923:939	The reduced complexity of the fragment spectra and the higher signal-to-noise ratio render QTOF-(+)ESMS an alternative mass spectrometric approach to the identification of O-glycosylation sites when compared with sequencing by post-source decay matrix-assisted laser desorption/ionization MS. Diagnostic ions from the N-terminus in the b-series offered direct evidence, which was supported by indirect evidence from the C-terminus ions of the y-series.
9597769	2	27	theme	underivatized	404:416	arg1	[T1APPAHGVT9S10APDT14RPAPGS20T21APPA					426:461	the underivatized TAP25-2 [T1APPAHGVT9S10APDT14RPAPGS20T21APPA	400:461	the underivatized TAP25-2 [T1APPAHGVT9S10APDT14RPAPGS20T21APPA	400:461	The location of O-glycosylation sites was possible in the positive ion (+) mode by detection of prominent y- and b-fragment ions from the underivatized TAP25-2 [T1APPAHGVT9S10APDT14RPAPGS20T21APPA], an overlapping sequence of MUC1 tandem repeats which had been glycosylated in vitro by two GalNAc residues in the positions T9 and T21.
9597769	2	28	gly	O-glycosylation	282:296	arg2	sites					298:302	O-glycosylation sites	282:302	O-glycosylation sites	282:302	The location of O-glycosylation sites was possible in the positive ion (+) mode by detection of prominent y- and b-fragment ions from the underivatized TAP25-2 [T1APPAHGVT9S10APDT14RPAPGS20T21APPA], an overlapping sequence of MUC1 tandem repeats which had been glycosylated in vitro by two GalNAc residues in the positions T9 and T21.
9597769	5	29	theme	glycosylated	1160:1171	arg1	species					1244:1250	multiply ionized species	1227:1250	multiply ionized species	1227:1250	The higher glycosylated GalNAc2-substituted fragments were mainly observed as multiply ionized species.
9597769	5	29	theme	glycosylated	1160:1171	arg1	fragments					1193:1201	The higher glycosylated GalNAc2-substituted fragments	1149:1201	The higher glycosylated GalNAc2-substituted fragments	1149:1201	The higher glycosylated GalNAc2-substituted fragments were mainly observed as multiply ionized species.
9597769	2	30	from	ion	333:335	arg1	possible					308:315	possible	308:315	possible	308:315	The location of O-glycosylation sites was possible in the positive ion (+) mode by detection of prominent y- and b-fragment ions from the underivatized TAP25-2 [T1APPAHGVT9S10APDT14RPAPGS20T21APPA], an overlapping sequence of MUC1 tandem repeats which had been glycosylated in vitro by two GalNAc residues in the positions T9 and T21.
9597769	2	30	from	ion	333:335	arg1	location					270:277	The location	266:277	The location of O-glycosylation sites	266:302	The location of O-glycosylation sites was possible in the positive ion (+) mode by detection of prominent y- and b-fragment ions from the underivatized TAP25-2 [T1APPAHGVT9S10APDT14RPAPGS20T21APPA], an overlapping sequence of MUC1 tandem repeats which had been glycosylated in vitro by two GalNAc residues in the positions T9 and T21.
9597769	2	31	theme	sites	298:302	arg1	possible					308:315	possible	308:315	possible	308:315	The location of O-glycosylation sites was possible in the positive ion (+) mode by detection of prominent y- and b-fragment ions from the underivatized TAP25-2 [T1APPAHGVT9S10APDT14RPAPGS20T21APPA], an overlapping sequence of MUC1 tandem repeats which had been glycosylated in vitro by two GalNAc residues in the positions T9 and T21.
9597769	2	31	theme	sites	298:302	arg1	location					270:277	The location	266:277	The location of O-glycosylation sites	266:302	The location of O-glycosylation sites was possible in the positive ion (+) mode by detection of prominent y- and b-fragment ions from the underivatized TAP25-2 [T1APPAHGVT9S10APDT14RPAPGS20T21APPA], an overlapping sequence of MUC1 tandem repeats which had been glycosylated in vitro by two GalNAc residues in the positions T9 and T21.
9597769	4	32	theme	indirect	1089:1096	arg1	evidence					1098:1105	indirect evidence	1089:1105	indirect evidence from the C-terminus ions of the y-series	1089:1146	The reduced complexity of the fragment spectra and the higher signal-to-noise ratio render QTOF-(+)ESMS an alternative mass spectrometric approach to the identification of O-glycosylation sites when compared with sequencing by post-source decay matrix-assisted laser desorption/ionization MS. Diagnostic ions from the N-terminus in the b-series offered direct evidence, which was supported by indirect evidence from the C-terminus ions of the y-series.
9597769	1	33	theme	glycopeptides	169:181	arg1	sequencing					155:164	the sequencing	151:164	the sequencing of glycopeptides	151:181	The potential of electrospray mass spectrometry (ESMS) for the sequencing of glycopeptides was evaluated using quadrupole time-of-flight (QTOF) technology in the MS/MS mode.
9597769	0	34	theme	sites	32:36	arg1	Localization					0:11	Localization	0:11	Localization of O-glycosylation sites of MUC1 tandem repeats by QTOF ESI mass spectrometry.	0:90	Localization of O-glycosylation sites of MUC1 tandem repeats by QTOF ESI mass spectrometry.
9597769	2	35	from	residues	563:570	arg1	positions					579:587	the positions T9 and T21	575:598	the positions T9 and T21	575:598	The location of O-glycosylation sites was possible in the positive ion (+) mode by detection of prominent y- and b-fragment ions from the underivatized TAP25-2 [T1APPAHGVT9S10APDT14RPAPGS20T21APPA], an overlapping sequence of MUC1 tandem repeats which had been glycosylated in vitro by two GalNAc residues in the positions T9 and T21.
9597769	2	35	from	residues	563:570	arg1	T21					596:598	T21	596:598	T21	596:598	The location of O-glycosylation sites was possible in the positive ion (+) mode by detection of prominent y- and b-fragment ions from the underivatized TAP25-2 [T1APPAHGVT9S10APDT14RPAPGS20T21APPA], an overlapping sequence of MUC1 tandem repeats which had been glycosylated in vitro by two GalNAc residues in the positions T9 and T21.
9597769	2	35	from	residues	563:570	arg1	T9					589:590	T9	589:590	T9	589:590	The location of O-glycosylation sites was possible in the positive ion (+) mode by detection of prominent y- and b-fragment ions from the underivatized TAP25-2 [T1APPAHGVT9S10APDT14RPAPGS20T21APPA], an overlapping sequence of MUC1 tandem repeats which had been glycosylated in vitro by two GalNAc residues in the positions T9 and T21.
9597769	4	36	theme	sites	884:888	arg1	identification					850:863	the identification	846:863	the identification of O-glycosylation sites	846:888	The reduced complexity of the fragment spectra and the higher signal-to-noise ratio render QTOF-(+)ESMS an alternative mass spectrometric approach to the identification of O-glycosylation sites when compared with sequencing by post-source decay matrix-assisted laser desorption/ionization MS. Diagnostic ions from the N-terminus in the b-series offered direct evidence, which was supported by indirect evidence from the C-terminus ions of the y-series.
9597769	2	37	theme	O-glycosylation	282:296	arg1	sites					298:302	O-glycosylation sites	282:302	O-glycosylation sites	282:302	The location of O-glycosylation sites was possible in the positive ion (+) mode by detection of prominent y- and b-fragment ions from the underivatized TAP25-2 [T1APPAHGVT9S10APDT14RPAPGS20T21APPA], an overlapping sequence of MUC1 tandem repeats which had been glycosylated in vitro by two GalNAc residues in the positions T9 and T21.
9597769	2	38	theme	b-fragment	379:388	arg1	ions					390:393	prominent y- and b-fragment ions	362:393	prominent y- and b-fragment ions from the underivatized TAP25-2 [T1APPAHGVT9S10APDT14RPAPGS20T21APPA	362:461	The location of O-glycosylation sites was possible in the positive ion (+) mode by detection of prominent y- and b-fragment ions from the underivatized TAP25-2 [T1APPAHGVT9S10APDT14RPAPGS20T21APPA], an overlapping sequence of MUC1 tandem repeats which had been glycosylated in vitro by two GalNAc residues in the positions T9 and T21.
9597769	0	39	theme	O-glycosylation	16:30	arg1	sites					32:36	O-glycosylation sites	16:36	O-glycosylation sites of MUC1 tandem repeats	16:59	Localization of O-glycosylation sites of MUC1 tandem repeats by QTOF ESI mass spectrometry.
9597769	0	39	theme	O-glycosylation	16:30	arg1	repeats					53:59	MUC1 tandem repeats	41:59	MUC1 tandem repeats	41:59	Localization of O-glycosylation sites of MUC1 tandem repeats by QTOF ESI mass spectrometry.
9597769	4	40	from	N-terminus	1014:1023	arg1	evidence					1056:1063	the b-series offered direct evidence	1028:1063	the b-series offered direct evidence	1028:1063	The reduced complexity of the fragment spectra and the higher signal-to-noise ratio render QTOF-(+)ESMS an alternative mass spectrometric approach to the identification of O-glycosylation sites when compared with sequencing by post-source decay matrix-assisted laser desorption/ionization MS. Diagnostic ions from the N-terminus in the b-series offered direct evidence, which was supported by indirect evidence from the C-terminus ions of the y-series.
9597769	4	41	theme	O-glycosylation	868:882	arg1	sites					884:888	O-glycosylation sites	868:888	O-glycosylation sites	868:888	The reduced complexity of the fragment spectra and the higher signal-to-noise ratio render QTOF-(+)ESMS an alternative mass spectrometric approach to the identification of O-glycosylation sites when compared with sequencing by post-source decay matrix-assisted laser desorption/ionization MS. Diagnostic ions from the N-terminus in the b-series offered direct evidence, which was supported by indirect evidence from the C-terminus ions of the y-series.
9597769	3	42	theme	mass	610:613	arg1	resolution					615:624	high mass resolution	605:624	high mass resolution	605:624	The high mass resolution and accuracy of QTOF-(+)ESMS allowed reliable structural assignments.
9597769	4	43	theme	reduced	700:706	arg1	complexity					708:717	The reduced complexity	696:717	The reduced complexity of the fragment spectra	696:741	The reduced complexity of the fragment spectra and the higher signal-to-noise ratio render QTOF-(+)ESMS an alternative mass spectrometric approach to the identification of O-glycosylation sites when compared with sequencing by post-source decay matrix-assisted laser desorption/ionization MS. Diagnostic ions from the N-terminus in the b-series offered direct evidence, which was supported by indirect evidence from the C-terminus ions of the y-series.
9597769	4	44	theme	matrix-assisted	941:955	arg1	desorption/ionization					963:983	matrix-assisted laser desorption/ionization	941:983	sequencing by post-source decay matrix-assisted laser desorption/ionization MS. Diagnostic ions from the N-terminus in the b-series offered direct evidence, which was supported by indirect evidence from the C-terminus ions of the y-series	909:1146	The reduced complexity of the fragment spectra and the higher signal-to-noise ratio render QTOF-(+)ESMS an alternative mass spectrometric approach to the identification of O-glycosylation sites when compared with sequencing by post-source decay matrix-assisted laser desorption/ionization MS. Diagnostic ions from the N-terminus in the b-series offered direct evidence, which was supported by indirect evidence from the C-terminus ions of the y-series.
9597769	0	45	theme	MUC1	41:44	arg1	repeats					53:59	MUC1 tandem repeats	41:59	MUC1 tandem repeats	41:59	Localization of O-glycosylation sites of MUC1 tandem repeats by QTOF ESI mass spectrometry.
9597769	4	46	dep	sequencing	909:918	arg1	desorption/ionization					963:983	matrix-assisted laser desorption/ionization	941:983	sequencing by post-source decay matrix-assisted laser desorption/ionization MS. Diagnostic ions from the N-terminus in the b-series offered direct evidence, which was supported by indirect evidence from the C-terminus ions of the y-series	909:1146	The reduced complexity of the fragment spectra and the higher signal-to-noise ratio render QTOF-(+)ESMS an alternative mass spectrometric approach to the identification of O-glycosylation sites when compared with sequencing by post-source decay matrix-assisted laser desorption/ionization MS. Diagnostic ions from the N-terminus in the b-series offered direct evidence, which was supported by indirect evidence from the C-terminus ions of the y-series.
9597769	2	47	theme	y-	372:373	arg1	ions					390:393	prominent y- and b-fragment ions	362:393	prominent y- and b-fragment ions from the underivatized TAP25-2 [T1APPAHGVT9S10APDT14RPAPGS20T21APPA	362:461	The location of O-glycosylation sites was possible in the positive ion (+) mode by detection of prominent y- and b-fragment ions from the underivatized TAP25-2 [T1APPAHGVT9S10APDT14RPAPGS20T21APPA], an overlapping sequence of MUC1 tandem repeats which had been glycosylated in vitro by two GalNAc residues in the positions T9 and T21.
9597769	5	48	gly	glycosylated	1160:1171	arg1	species					1244:1250	multiply ionized species	1227:1250	multiply ionized species	1227:1250	The higher glycosylated GalNAc2-substituted fragments were mainly observed as multiply ionized species.
9597769	5	48	gly	glycosylated	1160:1171	arg1	fragments					1193:1201	The higher glycosylated GalNAc2-substituted fragments	1149:1201	The higher glycosylated GalNAc2-substituted fragments	1149:1201	The higher glycosylated GalNAc2-substituted fragments were mainly observed as multiply ionized species.
9597769	1	49	theme	quadrupole	203:212	arg1	technology					236:245	quadrupole time-of-flight (QTOF) technology	203:245	quadrupole time-of-flight (QTOF) technology	203:245	The potential of electrospray mass spectrometry (ESMS) for the sequencing of glycopeptides was evaluated using quadrupole time-of-flight (QTOF) technology in the MS/MS mode.
9597769	0	50	theme	repeats	53:59	arg1	sites					32:36	O-glycosylation sites	16:36	O-glycosylation sites of MUC1 tandem repeats	16:59	Localization of O-glycosylation sites of MUC1 tandem repeats by QTOF ESI mass spectrometry.
9597769	0	50	theme	repeats	53:59	arg1	repeats					53:59	MUC1 tandem repeats	41:59	MUC1 tandem repeats	41:59	Localization of O-glycosylation sites of MUC1 tandem repeats by QTOF ESI mass spectrometry.
9597769	2	51	theme	GalNAc	556:561	arg1	residues					563:570	two GalNAc residues	552:570	two GalNAc residues in the positions T9 and T21	552:598	The location of O-glycosylation sites was possible in the positive ion (+) mode by detection of prominent y- and b-fragment ions from the underivatized TAP25-2 [T1APPAHGVT9S10APDT14RPAPGS20T21APPA], an overlapping sequence of MUC1 tandem repeats which had been glycosylated in vitro by two GalNAc residues in the positions T9 and T21.
9597769	3	52	theme	high	605:608	arg1	resolution					615:624	high mass resolution	605:624	high mass resolution	605:624	The high mass resolution and accuracy of QTOF-(+)ESMS allowed reliable structural assignments.
9597769	0	53	gly	O-glycosylation	16:30	arg2	repeats					53:59	MUC1 tandem repeats	41:59	MUC1 tandem repeats	41:59	Localization of O-glycosylation sites of MUC1 tandem repeats by QTOF ESI mass spectrometry.
9597769	0	53	gly	O-glycosylation	16:30	arg2	sites					32:36	O-glycosylation sites	16:36	O-glycosylation sites of MUC1 tandem repeats	16:59	Localization of O-glycosylation sites of MUC1 tandem repeats by QTOF ESI mass spectrometry.
9597769	0	53	gly	O-glycosylation	16:30	arg1	repeats					53:59	MUC1 tandem repeats	41:59	MUC1 tandem repeats	41:59	Localization of O-glycosylation sites of MUC1 tandem repeats by QTOF ESI mass spectrometry.
9597769	2	54	from	mode	341:344	arg1	possible					308:315	possible	308:315	possible	308:315	The location of O-glycosylation sites was possible in the positive ion (+) mode by detection of prominent y- and b-fragment ions from the underivatized TAP25-2 [T1APPAHGVT9S10APDT14RPAPGS20T21APPA], an overlapping sequence of MUC1 tandem repeats which had been glycosylated in vitro by two GalNAc residues in the positions T9 and T21.
9597769	2	54	from	mode	341:344	arg1	location					270:277	The location	266:277	The location of O-glycosylation sites	266:302	The location of O-glycosylation sites was possible in the positive ion (+) mode by detection of prominent y- and b-fragment ions from the underivatized TAP25-2 [T1APPAHGVT9S10APDT14RPAPGS20T21APPA], an overlapping sequence of MUC1 tandem repeats which had been glycosylated in vitro by two GalNAc residues in the positions T9 and T21.
9597769	2	55	theme	positive	324:331	arg1	ion					333:335	the positive ion (+) mode	320:344	ion	333:335	The location of O-glycosylation sites was possible in the positive ion (+) mode by detection of prominent y- and b-fragment ions from the underivatized TAP25-2 [T1APPAHGVT9S10APDT14RPAPGS20T21APPA], an overlapping sequence of MUC1 tandem repeats which had been glycosylated in vitro by two GalNAc residues in the positions T9 and T21.
9597769	0	56	theme	tandem	46:51	arg1	repeats					53:59	MUC1 tandem repeats	41:59	MUC1 tandem repeats	41:59	Localization of O-glycosylation sites of MUC1 tandem repeats by QTOF ESI mass spectrometry.
9597769	4	57	dep	QTOF-	787:791	arg1	approach					834:841	an alternative mass spectrometric approach	800:841	an alternative mass spectrometric approach	800:841	The reduced complexity of the fragment spectra and the higher signal-to-noise ratio render QTOF-(+)ESMS an alternative mass spectrometric approach to the identification of O-glycosylation sites when compared with sequencing by post-source decay matrix-assisted laser desorption/ionization MS. Diagnostic ions from the N-terminus in the b-series offered direct evidence, which was supported by indirect evidence from the C-terminus ions of the y-series.
9597769	1	58	theme	electrospray	109:120	arg1	ESMS					141:144	ESMS	141:144	ESMS	141:144	The potential of electrospray mass spectrometry (ESMS) for the sequencing of glycopeptides was evaluated using quadrupole time-of-flight (QTOF) technology in the MS/MS mode.
9597769	1	58	theme	electrospray	109:120	arg1	spectrometry					127:138	electrospray mass spectrometry	109:138	electrospray mass spectrometry (ESMS)	109:145	The potential of electrospray mass spectrometry (ESMS) for the sequencing of glycopeptides was evaluated using quadrupole time-of-flight (QTOF) technology in the MS/MS mode.
9597769	4	59	theme	higher	751:756	arg1	ratio					774:778	the higher signal-to-noise ratio	747:778	the higher signal-to-noise ratio	747:778	The reduced complexity of the fragment spectra and the higher signal-to-noise ratio render QTOF-(+)ESMS an alternative mass spectrometric approach to the identification of O-glycosylation sites when compared with sequencing by post-source decay matrix-assisted laser desorption/ionization MS. Diagnostic ions from the N-terminus in the b-series offered direct evidence, which was supported by indirect evidence from the C-terminus ions of the y-series.
9597769	3	60	theme	QTOF-	642:646	arg1	accuracy					630:637	accuracy	630:637	accuracy	630:637	The high mass resolution and accuracy of QTOF-(+)ESMS allowed reliable structural assignments.
9597769	3	60	theme	QTOF-	642:646	arg1	resolution					615:624	high mass resolution	605:624	high mass resolution	605:624	The high mass resolution and accuracy of QTOF-(+)ESMS allowed reliable structural assignments.
9597769	2	61	from	detection	349:357	arg1	[T1APPAHGVT9S10APDT14RPAPGS20T21APPA					426:461	the underivatized TAP25-2 [T1APPAHGVT9S10APDT14RPAPGS20T21APPA	400:461	the underivatized TAP25-2 [T1APPAHGVT9S10APDT14RPAPGS20T21APPA	400:461	The location of O-glycosylation sites was possible in the positive ion (+) mode by detection of prominent y- and b-fragment ions from the underivatized TAP25-2 [T1APPAHGVT9S10APDT14RPAPGS20T21APPA], an overlapping sequence of MUC1 tandem repeats which had been glycosylated in vitro by two GalNAc residues in the positions T9 and T21.
9597769	1	62	theme	mass	122:125	arg1	ESMS					141:144	ESMS	141:144	ESMS	141:144	The potential of electrospray mass spectrometry (ESMS) for the sequencing of glycopeptides was evaluated using quadrupole time-of-flight (QTOF) technology in the MS/MS mode.
9597769	1	62	theme	mass	122:125	arg1	spectrometry					127:138	electrospray mass spectrometry	109:138	electrospray mass spectrometry (ESMS)	109:145	The potential of electrospray mass spectrometry (ESMS) for the sequencing of glycopeptides was evaluated using quadrupole time-of-flight (QTOF) technology in the MS/MS mode.
9597769	1	63	theme	time-of-flight	214:227	arg1	technology					236:245	quadrupole time-of-flight (QTOF) technology	203:245	quadrupole time-of-flight (QTOF) technology	203:245	The potential of electrospray mass spectrometry (ESMS) for the sequencing of glycopeptides was evaluated using quadrupole time-of-flight (QTOF) technology in the MS/MS mode.
9597769	4	64	theme	y-series	1139:1146	arg1	ions					1127:1130	the C-terminus ions	1112:1130	the C-terminus ions of the y-series	1112:1146	The reduced complexity of the fragment spectra and the higher signal-to-noise ratio render QTOF-(+)ESMS an alternative mass spectrometric approach to the identification of O-glycosylation sites when compared with sequencing by post-source decay matrix-assisted laser desorption/ionization MS. Diagnostic ions from the N-terminus in the b-series offered direct evidence, which was supported by indirect evidence from the C-terminus ions of the y-series.
9597769	1	65	theme	spectrometry	127:138	arg1	potential					96:104	The potential	92:104	The potential of electrospray mass spectrometry (ESMS) for the sequencing of glycopeptides	92:181	The potential of electrospray mass spectrometry (ESMS) for the sequencing of glycopeptides was evaluated using quadrupole time-of-flight (QTOF) technology in the MS/MS mode.
9597769	5	66	theme	ionized	1236:1242	arg1	species					1244:1250	multiply ionized species	1227:1250	multiply ionized species	1227:1250	The higher glycosylated GalNAc2-substituted fragments were mainly observed as multiply ionized species.
9597769	5	66	theme	ionized	1236:1242	arg1	fragments					1193:1201	The higher glycosylated GalNAc2-substituted fragments	1149:1201	The higher glycosylated GalNAc2-substituted fragments	1149:1201	The higher glycosylated GalNAc2-substituted fragments were mainly observed as multiply ionized species.
9597769	0	67	theme	QTOF	64:67	arg1	spectrometry					78:89	QTOF ESI mass spectrometry	64:89	QTOF ESI mass spectrometry	64:89	Localization of O-glycosylation sites of MUC1 tandem repeats by QTOF ESI mass spectrometry.
9597769	2	68	theme	prominent	362:370	arg1	ions					390:393	prominent y- and b-fragment ions	362:393	prominent y- and b-fragment ions from the underivatized TAP25-2 [T1APPAHGVT9S10APDT14RPAPGS20T21APPA	362:461	The location of O-glycosylation sites was possible in the positive ion (+) mode by detection of prominent y- and b-fragment ions from the underivatized TAP25-2 [T1APPAHGVT9S10APDT14RPAPGS20T21APPA], an overlapping sequence of MUC1 tandem repeats which had been glycosylated in vitro by two GalNAc residues in the positions T9 and T21.
9597769	4	69	theme	signal-to-noise	758:772	arg1	ratio					774:778	the higher signal-to-noise ratio	747:778	the higher signal-to-noise ratio	747:778	The reduced complexity of the fragment spectra and the higher signal-to-noise ratio render QTOF-(+)ESMS an alternative mass spectrometric approach to the identification of O-glycosylation sites when compared with sequencing by post-source decay matrix-assisted laser desorption/ionization MS. Diagnostic ions from the N-terminus in the b-series offered direct evidence, which was supported by indirect evidence from the C-terminus ions of the y-series.
9597769	2	70	gly	glycosylated	527:538	arg1	sequence					480:487	an overlapping sequence	465:487	an overlapping sequence of MUC1 tandem repeats which had been glycosylated in vitro by two GalNAc residues in the positions T9 and T21	465:598	The location of O-glycosylation sites was possible in the positive ion (+) mode by detection of prominent y- and b-fragment ions from the underivatized TAP25-2 [T1APPAHGVT9S10APDT14RPAPGS20T21APPA], an overlapping sequence of MUC1 tandem repeats which had been glycosylated in vitro by two GalNAc residues in the positions T9 and T21.
9597769	2	70	gly	glycosylated	527:538	arg1	detection					349:357	detection	349:357	detection of prominent y- and b-fragment ions from the underivatized TAP25-2 [T1APPAHGVT9S10APDT14RPAPGS20T21APPA]	349:462	The location of O-glycosylation sites was possible in the positive ion (+) mode by detection of prominent y- and b-fragment ions from the underivatized TAP25-2 [T1APPAHGVT9S10APDT14RPAPGS20T21APPA], an overlapping sequence of MUC1 tandem repeats which had been glycosylated in vitro by two GalNAc residues in the positions T9 and T21.
9597769	4	71	from	ions	1127:1130	arg1	evidence					1098:1105	indirect evidence	1089:1105	indirect evidence from the C-terminus ions of the y-series	1089:1146	The reduced complexity of the fragment spectra and the higher signal-to-noise ratio render QTOF-(+)ESMS an alternative mass spectrometric approach to the identification of O-glycosylation sites when compared with sequencing by post-source decay matrix-assisted laser desorption/ionization MS. Diagnostic ions from the N-terminus in the b-series offered direct evidence, which was supported by indirect evidence from the C-terminus ions of the y-series.
9597769	1	72	theme	QTOF	230:233	arg1	technology					236:245	quadrupole time-of-flight (QTOF) technology	203:245	quadrupole time-of-flight (QTOF) technology	203:245	The potential of electrospray mass spectrometry (ESMS) for the sequencing of glycopeptides was evaluated using quadrupole time-of-flight (QTOF) technology in the MS/MS mode.
9597769	2	73	dep	positions	579:587	arg1	positions					579:587	the positions T9 and T21	575:598	the positions T9 and T21	575:598	The location of O-glycosylation sites was possible in the positive ion (+) mode by detection of prominent y- and b-fragment ions from the underivatized TAP25-2 [T1APPAHGVT9S10APDT14RPAPGS20T21APPA], an overlapping sequence of MUC1 tandem repeats which had been glycosylated in vitro by two GalNAc residues in the positions T9 and T21.
9597769	2	73	dep	positions	579:587	arg1	T21					596:598	T21	596:598	T21	596:598	The location of O-glycosylation sites was possible in the positive ion (+) mode by detection of prominent y- and b-fragment ions from the underivatized TAP25-2 [T1APPAHGVT9S10APDT14RPAPGS20T21APPA], an overlapping sequence of MUC1 tandem repeats which had been glycosylated in vitro by two GalNAc residues in the positions T9 and T21.
9597769	2	73	dep	positions	579:587	arg1	T9					589:590	T9	589:590	T9	589:590	The location of O-glycosylation sites was possible in the positive ion (+) mode by detection of prominent y- and b-fragment ions from the underivatized TAP25-2 [T1APPAHGVT9S10APDT14RPAPGS20T21APPA], an overlapping sequence of MUC1 tandem repeats which had been glycosylated in vitro by two GalNAc residues in the positions T9 and T21.
9597769	2	74	theme	ions	390:393	arg1	detection					349:357	detection	349:357	detection of prominent y- and b-fragment ions from the underivatized TAP25-2 [T1APPAHGVT9S10APDT14RPAPGS20T21APPA]	349:462	The location of O-glycosylation sites was possible in the positive ion (+) mode by detection of prominent y- and b-fragment ions from the underivatized TAP25-2 [T1APPAHGVT9S10APDT14RPAPGS20T21APPA], an overlapping sequence of MUC1 tandem repeats which had been glycosylated in vitro by two GalNAc residues in the positions T9 and T21.
9597769	2	74	theme	ions	390:393	arg1	sequence					480:487	an overlapping sequence	465:487	an overlapping sequence of MUC1 tandem repeats which had been glycosylated in vitro by two GalNAc residues in the positions T9 and T21	465:598	The location of O-glycosylation sites was possible in the positive ion (+) mode by detection of prominent y- and b-fragment ions from the underivatized TAP25-2 [T1APPAHGVT9S10APDT14RPAPGS20T21APPA], an overlapping sequence of MUC1 tandem repeats which had been glycosylated in vitro by two GalNAc residues in the positions T9 and T21.
9597769	3	75	theme	ESMS	650:653	arg1	accuracy					630:637	accuracy	630:637	accuracy	630:637	The high mass resolution and accuracy of QTOF-(+)ESMS allowed reliable structural assignments.
9597769	3	75	theme	ESMS	650:653	arg1	resolution					615:624	high mass resolution	605:624	high mass resolution	605:624	The high mass resolution and accuracy of QTOF-(+)ESMS allowed reliable structural assignments.
9597769	4	76	theme	offered	1041:1047	arg1	evidence					1056:1063	the b-series offered direct evidence	1028:1063	the b-series offered direct evidence	1028:1063	The reduced complexity of the fragment spectra and the higher signal-to-noise ratio render QTOF-(+)ESMS an alternative mass spectrometric approach to the identification of O-glycosylation sites when compared with sequencing by post-source decay matrix-assisted laser desorption/ionization MS. Diagnostic ions from the N-terminus in the b-series offered direct evidence, which was supported by indirect evidence from the C-terminus ions of the y-series.
9597769	3	77	dep	resolution	615:624	arg1	The					601:603	The	601:603	The	601:603	The high mass resolution and accuracy of QTOF-(+)ESMS allowed reliable structural assignments.
33962943	5	0	theme	proximal	624:631	arg1	site					619:622	a newly identified binding site	592:622	a newly identified binding site proximal to adjacent to metal ion-dependent adhesion site	592:680	The α5β1-fibronectin complex revealed simultaneous interactions at the arginine-glycine-aspartate loop, the synergy site, and a newly identified binding site proximal to adjacent to metal ion-dependent adhesion site, inducing the translocation of helix α1 to secure integrin opening.
33962943	4	1	theme	cryo-electron	311:323	arg1	microscopy					325:334	cryo-electron microscopy	311:334	cryo-electron microscopy structures of native human α5β1 with fibronectin to 3.1-angstrom resolution, and in its resting state to 4.6-angstrom resolution	311:463	Here, we report cryo-electron microscopy structures of native human α5β1 with fibronectin to 3.1-angstrom resolution, and in its resting state to 4.6-angstrom resolution.
33962943	6	2	theme	bending	845:851	arg1	binding					871:877	integrin sharp bending inhibiting ligand binding	830:877	integrin sharp bending inhibiting ligand binding	830:877	Resting α5β1 adopts an incompletely bent conformation, challenging the model of integrin sharp bending inhibiting ligand binding.
33962943	6	3	theme	inhibiting	853:862	arg1	binding					871:877	integrin sharp bending inhibiting ligand binding	830:877	integrin sharp bending inhibiting ligand binding	830:877	Resting α5β1 adopts an incompletely bent conformation, challenging the model of integrin sharp bending inhibiting ligand binding.
33962943	4	4	theme	3.1-angstrom	388:399	arg1	resolution					401:410	3.1-angstrom resolution	388:410	3.1-angstrom resolution	388:410	Here, we report cryo-electron microscopy structures of native human α5β1 with fibronectin to 3.1-angstrom resolution, and in its resting state to 4.6-angstrom resolution.
33962943	2	5	theme	complex	150:156	arg1	formation					158:166	complex formation	150:166	complex formation	150:166	Upon complex formation, fibronectin and α5β1 undergo conformational changes.
33962943	6	6	theme	integrin	830:837	arg1	binding					871:877	integrin sharp bending inhibiting ligand binding	830:877	integrin sharp bending inhibiting ligand binding	830:877	Resting α5β1 adopts an incompletely bent conformation, challenging the model of integrin sharp bending inhibiting ligand binding.
33962943	5	7	theme	simultaneous	504:515	arg1	interactions					517:528	simultaneous interactions	504:528	simultaneous interactions at the arginine-glycine-aspartate loop	504:567	The α5β1-fibronectin complex revealed simultaneous interactions at the arginine-glycine-aspartate loop, the synergy site, and a newly identified binding site proximal to adjacent to metal ion-dependent adhesion site, inducing the translocation of helix α1 to secure integrin opening.
33962943	3	8	theme	cell-tissue	244:254	arg1	connections					256:266	cell-tissue connections	244:266	cell-tissue connections	244:266	While this is key for cell-tissue connections, its mechanism is unknown.
33962943	5	9	theme	adjacent	636:643	arg1	site					677:680	adjacent to metal ion-dependent adhesion site	636:680	adjacent to metal ion-dependent adhesion site	636:680	The α5β1-fibronectin complex revealed simultaneous interactions at the arginine-glycine-aspartate loop, the synergy site, and a newly identified binding site proximal to adjacent to metal ion-dependent adhesion site, inducing the translocation of helix α1 to secure integrin opening.
33962943	1	10	theme	Integrin	70:77	arg1	receptor					107:114	a major fibronectin receptor	87:114	a major fibronectin receptor critical for cell migration	87:142	Integrin α5β1 is a major fibronectin receptor critical for cell migration.
33962943	1	10	theme	Integrin	70:77	arg1	α5β1					79:82	Integrin α5β1	70:82	Integrin α5β1	70:82	Integrin α5β1 is a major fibronectin receptor critical for cell migration.
33962943	7	11	theme	structural	900:909	arg1	analyses					911:918	Our biochemical and structural analyses	880:918	Our biochemical and structural analyses	880:918	Our biochemical and structural analyses showed that affinity of α5β1 for fibronectin is increased with manganese ions (Mn2+) while adopting the half-bent conformation, indicating that ligand-binding affinity does not depend on conformation, and α5β1 opening is induced by ligand-binding.
33962943	5	12	theme	metal	648:652	arg1	site					677:680	adjacent to metal ion-dependent adhesion site	636:680	adjacent to metal ion-dependent adhesion site	636:680	The α5β1-fibronectin complex revealed simultaneous interactions at the arginine-glycine-aspartate loop, the synergy site, and a newly identified binding site proximal to adjacent to metal ion-dependent adhesion site, inducing the translocation of helix α1 to secure integrin opening.
33962943	7	13	theme	ligand-binding	1064:1077	arg1	affinity					1079:1086	ligand-binding affinity	1064:1086	ligand-binding affinity	1064:1086	Our biochemical and structural analyses showed that affinity of α5β1 for fibronectin is increased with manganese ions (Mn2+) while adopting the half-bent conformation, indicating that ligand-binding affinity does not depend on conformation, and α5β1 opening is induced by ligand-binding.
33962943	5	14	theme	ion-dependent	654:666	arg1	site					677:680	adjacent to metal ion-dependent adhesion site	636:680	adjacent to metal ion-dependent adhesion site	636:680	The α5β1-fibronectin complex revealed simultaneous interactions at the arginine-glycine-aspartate loop, the synergy site, and a newly identified binding site proximal to adjacent to metal ion-dependent adhesion site, inducing the translocation of helix α1 to secure integrin opening.
33962943	4	15	theme	α5β1	363:366	arg1	structures					336:345	cryo-electron microscopy structures	311:345	cryo-electron microscopy structures of native human α5β1 with fibronectin to 3.1-angstrom resolution, and in its resting state to 4.6-angstrom resolution	311:463	Here, we report cryo-electron microscopy structures of native human α5β1 with fibronectin to 3.1-angstrom resolution, and in its resting state to 4.6-angstrom resolution.
33962943	7	16	theme	biochemical	884:894	arg1	analyses					911:918	Our biochemical and structural analyses	880:918	Our biochemical and structural analyses	880:918	Our biochemical and structural analyses showed that affinity of α5β1 for fibronectin is increased with manganese ions (Mn2+) while adopting the half-bent conformation, indicating that ligand-binding affinity does not depend on conformation, and α5β1 opening is induced by ligand-binding.
33962943	0	17	theme	Structural	0:9	arg1	insights					11:18	Structural insights	0:18	Structural insights into integrin	0:32	Structural insights into integrin α5β1 opening by fibronectin ligand.
33962943	6	18	theme	sharp	839:843	arg1	binding					871:877	integrin sharp bending inhibiting ligand binding	830:877	integrin sharp bending inhibiting ligand binding	830:877	Resting α5β1 adopts an incompletely bent conformation, challenging the model of integrin sharp bending inhibiting ligand binding.
33962943	5	19	theme	adhesion	668:675	arg1	site					677:680	adjacent to metal ion-dependent adhesion site	636:680	adjacent to metal ion-dependent adhesion site	636:680	The α5β1-fibronectin complex revealed simultaneous interactions at the arginine-glycine-aspartate loop, the synergy site, and a newly identified binding site proximal to adjacent to metal ion-dependent adhesion site, inducing the translocation of helix α1 to secure integrin opening.
33962943	5	20	theme	identified	600:609	arg1	site					619:622	a newly identified binding site	592:622	a newly identified binding site proximal to adjacent to metal ion-dependent adhesion site	592:680	The α5β1-fibronectin complex revealed simultaneous interactions at the arginine-glycine-aspartate loop, the synergy site, and a newly identified binding site proximal to adjacent to metal ion-dependent adhesion site, inducing the translocation of helix α1 to secure integrin opening.
33962943	5	21	from	loop	564:567	arg1	interactions					517:528	simultaneous interactions	504:528	simultaneous interactions at the arginine-glycine-aspartate loop	504:567	The α5β1-fibronectin complex revealed simultaneous interactions at the arginine-glycine-aspartate loop, the synergy site, and a newly identified binding site proximal to adjacent to metal ion-dependent adhesion site, inducing the translocation of helix α1 to secure integrin opening.
33962943	5	21	from	loop	564:567	arg1	site					619:622	a newly identified binding site	592:622	a newly identified binding site proximal to adjacent to metal ion-dependent adhesion site	592:680	The α5β1-fibronectin complex revealed simultaneous interactions at the arginine-glycine-aspartate loop, the synergy site, and a newly identified binding site proximal to adjacent to metal ion-dependent adhesion site, inducing the translocation of helix α1 to secure integrin opening.
33962943	5	21	from	loop	564:567	arg1	site					582:585	the synergy site	570:585	the synergy site	570:585	The α5β1-fibronectin complex revealed simultaneous interactions at the arginine-glycine-aspartate loop, the synergy site, and a newly identified binding site proximal to adjacent to metal ion-dependent adhesion site, inducing the translocation of helix α1 to secure integrin opening.
33962943	5	22	dep	site	677:680	arg1	to					645:646	to	645:646	to	645:646	The α5β1-fibronectin complex revealed simultaneous interactions at the arginine-glycine-aspartate loop, the synergy site, and a newly identified binding site proximal to adjacent to metal ion-dependent adhesion site, inducing the translocation of helix α1 to secure integrin opening.
33962943	5	23	theme	binding	611:617	arg1	site					619:622	a newly identified binding site	592:622	a newly identified binding site proximal to adjacent to metal ion-dependent adhesion site	592:680	The α5β1-fibronectin complex revealed simultaneous interactions at the arginine-glycine-aspartate loop, the synergy site, and a newly identified binding site proximal to adjacent to metal ion-dependent adhesion site, inducing the translocation of helix α1 to secure integrin opening.
33962943	1	24	theme	major	89:93	arg1	receptor					107:114	a major fibronectin receptor	87:114	a major fibronectin receptor critical for cell migration	87:142	Integrin α5β1 is a major fibronectin receptor critical for cell migration.
33962943	1	24	theme	major	89:93	arg1	α5β1					79:82	Integrin α5β1	70:82	Integrin α5β1	70:82	Integrin α5β1 is a major fibronectin receptor critical for cell migration.
33962943	5	25	theme	α5β1-fibronectin	470:485	arg1	complex					487:493	The α5β1-fibronectin complex	466:493	The α5β1-fibronectin complex	466:493	The α5β1-fibronectin complex revealed simultaneous interactions at the arginine-glycine-aspartate loop, the synergy site, and a newly identified binding site proximal to adjacent to metal ion-dependent adhesion site, inducing the translocation of helix α1 to secure integrin opening.
33962943	5	26	theme	secure	725:730	arg1	opening					741:747	secure integrin opening	725:747	secure integrin opening	725:747	The α5β1-fibronectin complex revealed simultaneous interactions at the arginine-glycine-aspartate loop, the synergy site, and a newly identified binding site proximal to adjacent to metal ion-dependent adhesion site, inducing the translocation of helix α1 to secure integrin opening.
33962943	4	27	theme	4.6-angstrom	441:452	arg1	resolution					454:463	4.6-angstrom resolution	441:463	4.6-angstrom resolution	441:463	Here, we report cryo-electron microscopy structures of native human α5β1 with fibronectin to 3.1-angstrom resolution, and in its resting state to 4.6-angstrom resolution.
33962943	1	28	theme	fibronectin	95:105	arg1	receptor					107:114	a major fibronectin receptor	87:114	a major fibronectin receptor critical for cell migration	87:142	Integrin α5β1 is a major fibronectin receptor critical for cell migration.
33962943	1	28	theme	fibronectin	95:105	arg1	α5β1					79:82	Integrin α5β1	70:82	Integrin α5β1	70:82	Integrin α5β1 is a major fibronectin receptor critical for cell migration.
33962943	5	29	theme	integrin	732:739	arg1	opening					741:747	secure integrin opening	725:747	secure integrin opening	725:747	The α5β1-fibronectin complex revealed simultaneous interactions at the arginine-glycine-aspartate loop, the synergy site, and a newly identified binding site proximal to adjacent to metal ion-dependent adhesion site, inducing the translocation of helix α1 to secure integrin opening.
33962943	5	30	theme	synergy	574:580	arg1	site					582:585	the synergy site	570:585	the synergy site	570:585	The α5β1-fibronectin complex revealed simultaneous interactions at the arginine-glycine-aspartate loop, the synergy site, and a newly identified binding site proximal to adjacent to metal ion-dependent adhesion site, inducing the translocation of helix α1 to secure integrin opening.
33962943	0	31	theme	fibronectin	50:60	arg1	ligand					62:67	fibronectin ligand	50:67	fibronectin ligand	50:67	Structural insights into integrin α5β1 opening by fibronectin ligand.
33962943	6	32	theme	binding	871:877	arg1	model					821:825	the model	817:825	the model of integrin sharp bending inhibiting ligand binding	817:877	Resting α5β1 adopts an incompletely bent conformation, challenging the model of integrin sharp bending inhibiting ligand binding.
33962943	6	33	theme	bent	786:789	arg1	conformation					791:802	an incompletely bent conformation	770:802	an incompletely bent conformation	770:802	Resting α5β1 adopts an incompletely bent conformation, challenging the model of integrin sharp bending inhibiting ligand binding.
33962943	4	34	with	α5β1	363:366	arg1	fibronectin					373:383	fibronectin	373:383	fibronectin	373:383	Here, we report cryo-electron microscopy structures of native human α5β1 with fibronectin to 3.1-angstrom resolution, and in its resting state to 4.6-angstrom resolution.
33962943	4	35	from	structures	336:345	arg1	state					432:436	its resting state	420:436	its resting state	420:436	Here, we report cryo-electron microscopy structures of native human α5β1 with fibronectin to 3.1-angstrom resolution, and in its resting state to 4.6-angstrom resolution.
33962943	4	36	theme	human	357:361	arg1	α5β1					363:366	native human α5β1	350:366	native human α5β1 with fibronectin to 3.1-angstrom resolution	350:410	Here, we report cryo-electron microscopy structures of native human α5β1 with fibronectin to 3.1-angstrom resolution, and in its resting state to 4.6-angstrom resolution.
33962943	1	37	theme	critical	116:123	arg1	receptor					107:114	a major fibronectin receptor	87:114	a major fibronectin receptor critical for cell migration	87:142	Integrin α5β1 is a major fibronectin receptor critical for cell migration.
33962943	1	37	theme	critical	116:123	arg1	α5β1					79:82	Integrin α5β1	70:82	Integrin α5β1	70:82	Integrin α5β1 is a major fibronectin receptor critical for cell migration.
33962943	5	38	theme	helix	713:717	arg1	translocation					696:708	the translocation	692:708	the translocation of helix α1 to secure integrin opening	692:747	The α5β1-fibronectin complex revealed simultaneous interactions at the arginine-glycine-aspartate loop, the synergy site, and a newly identified binding site proximal to adjacent to metal ion-dependent adhesion site, inducing the translocation of helix α1 to secure integrin opening.
33962943	2	39	theme	conformational	198:211	arg1	changes					213:219	conformational changes	198:219	conformational changes	198:219	Upon complex formation, fibronectin and α5β1 undergo conformational changes.
33962943	4	40	theme	native	350:355	arg1	α5β1					363:366	native human α5β1	350:366	native human α5β1 with fibronectin to 3.1-angstrom resolution	350:410	Here, we report cryo-electron microscopy structures of native human α5β1 with fibronectin to 3.1-angstrom resolution, and in its resting state to 4.6-angstrom resolution.
33962943	6	41	theme	Resting	750:756	arg1	α5β1					758:761	Resting α5β1	750:761	Resting α5β1	750:761	Resting α5β1 adopts an incompletely bent conformation, challenging the model of integrin sharp bending inhibiting ligand binding.
33962943	6	42	theme	ligand	864:869	arg1	binding					871:877	integrin sharp bending inhibiting ligand binding	830:877	integrin sharp bending inhibiting ligand binding	830:877	Resting α5β1 adopts an incompletely bent conformation, challenging the model of integrin sharp bending inhibiting ligand binding.
33962943	5	43	theme	arginine-glycine-aspartate	537:562	arg1	loop					564:567	the arginine-glycine-aspartate loop	533:567	the arginine-glycine-aspartate loop	533:567	The α5β1-fibronectin complex revealed simultaneous interactions at the arginine-glycine-aspartate loop, the synergy site, and a newly identified binding site proximal to adjacent to metal ion-dependent adhesion site, inducing the translocation of helix α1 to secure integrin opening.
33962943	1	44	theme	cell	129:132	arg1	migration					134:142	cell migration	129:142	cell migration	129:142	Integrin α5β1 is a major fibronectin receptor critical for cell migration.
33962943	7	45	theme	α5β1	1125:1128	arg1	opening					1130:1136	α5β1 opening	1125:1136	α5β1 opening	1125:1136	Our biochemical and structural analyses showed that affinity of α5β1 for fibronectin is increased with manganese ions (Mn2+) while adopting the half-bent conformation, indicating that ligand-binding affinity does not depend on conformation, and α5β1 opening is induced by ligand-binding.
33962943	4	46	theme	resting	424:430	arg1	state					432:436	its resting state	420:436	its resting state	420:436	Here, we report cryo-electron microscopy structures of native human α5β1 with fibronectin to 3.1-angstrom resolution, and in its resting state to 4.6-angstrom resolution.
33962943	7	47	theme	half-bent	1024:1032	arg1	conformation					1034:1045	the half-bent conformation	1020:1045	the half-bent conformation	1020:1045	Our biochemical and structural analyses showed that affinity of α5β1 for fibronectin is increased with manganese ions (Mn2+) while adopting the half-bent conformation, indicating that ligand-binding affinity does not depend on conformation, and α5β1 opening is induced by ligand-binding.
33962943	7	48	theme	α5β1	944:947	arg1	affinity					932:939	affinity	932:939	affinity of α5β1 for fibronectin	932:963	Our biochemical and structural analyses showed that affinity of α5β1 for fibronectin is increased with manganese ions (Mn2+) while adopting the half-bent conformation, indicating that ligand-binding affinity does not depend on conformation, and α5β1 opening is induced by ligand-binding.
33962943	7	49	theme	manganese	983:991	arg1	Mn2+					999:1002	Mn2+	999:1002	Mn2+	999:1002	Our biochemical and structural analyses showed that affinity of α5β1 for fibronectin is increased with manganese ions (Mn2+) while adopting the half-bent conformation, indicating that ligand-binding affinity does not depend on conformation, and α5β1 opening is induced by ligand-binding.
33962943	7	49	theme	manganese	983:991	arg1	ions					993:996	manganese ions	983:996	manganese ions (Mn2+)	983:1003	Our biochemical and structural analyses showed that affinity of α5β1 for fibronectin is increased with manganese ions (Mn2+) while adopting the half-bent conformation, indicating that ligand-binding affinity does not depend on conformation, and α5β1 opening is induced by ligand-binding.
33962943	4	50	theme	microscopy	325:334	arg1	structures					336:345	cryo-electron microscopy structures	311:345	cryo-electron microscopy structures of native human α5β1 with fibronectin to 3.1-angstrom resolution, and in its resting state to 4.6-angstrom resolution	311:463	Here, we report cryo-electron microscopy structures of native human α5β1 with fibronectin to 3.1-angstrom resolution, and in its resting state to 4.6-angstrom resolution.
21965667	0	0	theme	affinity	64:71	arg1	binding					90:96	high affinity γ-immunoglobulin binding	59:96	high affinity γ-immunoglobulin binding	59:96	Crystal structure of Fcγ receptor I and its implication in high affinity γ-immunoglobulin binding.
21965667	6	1	theme	affinity	1055:1062	arg1	enhancement					1064:1074	the affinity enhancement	1051:1074	the affinity enhancement	1051:1074	Third, the replacement of FcγRIII FG-loop ((171)LVGSKNV(177)) with that of FcγRI ((171)MGKHRY(176)) resulted in a 15-fold increase in IgG(1) binding affinity, whereas a valine insertion in the FcγRI FG-loop ((171)MVGKHRY(177)) abolished the affinity enhancement.
21965667	3	2	theme	extracellular	430:442	arg1	domains					452:458	all three extracellular Ig-like domains	420:458	all three extracellular Ig-like domains (designated as D1, D2, and D3)	420:489	Here we report the first crystal structure of an FcγRI with all three extracellular Ig-like domains (designated as D1, D2, and D3).
21965667	1	3	theme	immunoglobulin	225:238	arg1	G					240:240	immunoglobulin G	225:240	immunoglobulin G (IgG)	225:246	Fcγ receptors (FcγRs) play critical roles in humoral and cellular immune responses through interactions with the Fc region of immunoglobulin G (IgG).
21965667	1	3	theme	immunoglobulin	225:238	arg1	IgG					243:245	IgG	243:245	IgG	243:245	Fcγ receptors (FcγRs) play critical roles in humoral and cellular immune responses through interactions with the Fc region of immunoglobulin G (IgG).
21965667	0	4	theme	high	59:62	arg1	binding					90:96	high affinity γ-immunoglobulin binding	59:96	high affinity γ-immunoglobulin binding	59:96	Crystal structure of Fcγ receptor I and its implication in high affinity γ-immunoglobulin binding.
21965667	0	5	from	structure	8:16	arg1	binding					90:96	high affinity γ-immunoglobulin binding	59:96	high affinity γ-immunoglobulin binding	59:96	Crystal structure of Fcγ receptor I and its implication in high affinity γ-immunoglobulin binding.
21965667	3	6	theme	Ig-like	444:450	arg1	domains					452:458	all three extracellular Ig-like domains	420:458	all three extracellular Ig-like domains (designated as D1, D2, and D3)	420:489	Here we report the first crystal structure of an FcγRI with all three extracellular Ig-like domains (designated as D1, D2, and D3).
21965667	1	7	theme	G	240:240	arg1	region					215:220	the Fc region	208:220	the Fc region of immunoglobulin G (IgG)	208:246	Fcγ receptors (FcγRs) play critical roles in humoral and cellular immune responses through interactions with the Fc region of immunoglobulin G (IgG).
21965667	4	8	theme	low	631:633	arg1	receptors					648:656	the low affinity Fcγ receptors	627:656	the low affinity Fcγ receptors	627:656	The structure shows that, first, FcγRI has an acute D1-D2 hinge angle similar to that of FcεRI but much smaller than those observed in the low affinity Fcγ receptors.
21965667	4	9	theme	D1-D2	544:548	arg1	angle					556:560	an acute D1-D2 hinge angle	535:560	an acute D1-D2 hinge angle similar to that of FcεRI but much smaller than those observed in the low affinity Fcγ receptors	535:656	The structure shows that, first, FcγRI has an acute D1-D2 hinge angle similar to that of FcεRI but much smaller than those observed in the low affinity Fcγ receptors.
21965667	0	10	theme	γ-immunoglobulin	73:88	arg1	binding					90:96	high affinity γ-immunoglobulin binding	59:96	high affinity γ-immunoglobulin binding	59:96	Crystal structure of Fcγ receptor I and its implication in high affinity γ-immunoglobulin binding.
21965667	6	11	theme	valine	983:988	arg1	insertion					990:998	a valine insertion	981:998	a valine insertion in the FcγRI FG-loop ((171)MVGKHRY(177))	981:1039	Third, the replacement of FcγRIII FG-loop ((171)LVGSKNV(177)) with that of FcγRI ((171)MGKHRY(176)) resulted in a 15-fold increase in IgG(1) binding affinity, whereas a valine insertion in the FcγRI FG-loop ((171)MVGKHRY(177)) abolished the affinity enhancement.
21965667	9	12	theme	molecular	1328:1336	arg1	mechanism					1338:1346	a molecular mechanism	1326:1346	a molecular mechanism for the high affinity IgG recognition by FcγRI	1326:1393	Taken together, our study suggests a molecular mechanism for the high affinity IgG recognition by FcγRI and provides a structural basis for understanding its physiological function and its therapeutic implication in treating autoimmune diseases.
21965667	4	13	theme	smaller	596:602	arg1	angle					556:560	an acute D1-D2 hinge angle	535:560	an acute D1-D2 hinge angle similar to that of FcεRI but much smaller than those observed in the low affinity Fcγ receptors	535:656	The structure shows that, first, FcγRI has an acute D1-D2 hinge angle similar to that of FcεRI but much smaller than those observed in the low affinity Fcγ receptors.
21965667	9	14	theme	physiological	1449:1461	arg1	function					1463:1470	its physiological function	1445:1470	its physiological function	1445:1470	Taken together, our study suggests a molecular mechanism for the high affinity IgG recognition by FcγRI and provides a structural basis for understanding its physiological function and its therapeutic implication in treating autoimmune diseases.
21965667	8	15	theme	structural	1191:1200	arg1	results					1202:1208	The structural results	1187:1208	The structural results	1187:1208	The structural results support FcγRI binding to IgG in a similar mode as its low affinity counterparts.
21965667	3	16	with	FcγRI	409:413	arg1	domains					452:458	all three extracellular Ig-like domains	420:458	all three extracellular Ig-like domains (designated as D1, D2, and D3)	420:489	Here we report the first crystal structure of an FcγRI with all three extracellular Ig-like domains (designated as D1, D2, and D3).
21965667	5	17	from	site	739:742	arg1	receptor					751:758	the receptor	747:758	the receptor	747:758	Second, the D3 domain of FcγRI is positioned away from the putative IgG binding site on the receptor and is thus unlikely to make direct contacts with Fc.
21965667	4	18	theme	Fcγ	644:646	arg1	receptors					648:656	the low affinity Fcγ receptors	627:656	the low affinity Fcγ receptors	627:656	The structure shows that, first, FcγRI has an acute D1-D2 hinge angle similar to that of FcεRI but much smaller than those observed in the low affinity Fcγ receptors.
21965667	5	19	theme	putative	718:725	arg1	site					739:742	the putative IgG binding site	714:742	the putative IgG binding site on the receptor	714:758	Second, the D3 domain of FcγRI is positioned away from the putative IgG binding site on the receptor and is thus unlikely to make direct contacts with Fc.
21965667	1	20	theme	humoral	144:150	arg1	responses					172:180	humoral and cellular immune responses	144:180	humoral and cellular immune responses	144:180	Fcγ receptors (FcγRs) play critical roles in humoral and cellular immune responses through interactions with the Fc region of immunoglobulin G (IgG).
21965667	7	21	theme	one-residue	1120:1130	arg1	deletion					1132:1139	its conserved one-residue deletion	1106:1139	its conserved one-residue deletion	1106:1139	Thus, the FcγRI FG-loop with its conserved one-residue deletion is critical to the high affinity IgG binding.
21965667	4	22	theme	affinity	635:642	arg1	receptors					648:656	the low affinity Fcγ receptors	627:656	the low affinity Fcγ receptors	627:656	The structure shows that, first, FcγRI has an acute D1-D2 hinge angle similar to that of FcεRI but much smaller than those observed in the low affinity Fcγ receptors.
21965667	2	23	theme	potential	324:332	arg1	target					334:339	a potential target	322:339	a potential target for immunotherapy	322:357	Among them, FcγRI is the only high affinity receptor for IgG and thus is a potential target for immunotherapy.
21965667	4	24	theme	acute	538:542	arg1	angle					556:560	an acute D1-D2 hinge angle	535:560	an acute D1-D2 hinge angle similar to that of FcεRI but much smaller than those observed in the low affinity Fcγ receptors	535:656	The structure shows that, first, FcγRI has an acute D1-D2 hinge angle similar to that of FcεRI but much smaller than those observed in the low affinity Fcγ receptors.
21965667	8	25	theme	low	1264:1266	arg1	binding					1224:1230	FcγRI binding	1218:1230	FcγRI binding to IgG	1218:1237	The structural results support FcγRI binding to IgG in a similar mode as its low affinity counterparts.
21965667	8	25	theme	low	1264:1266	arg1	counterparts					1277:1288	its low affinity counterparts	1260:1288	its low affinity counterparts	1260:1288	The structural results support FcγRI binding to IgG in a similar mode as its low affinity counterparts.
21965667	1	26	theme	cellular	156:163	arg1	responses					172:180	humoral and cellular immune responses	144:180	humoral and cellular immune responses	144:180	Fcγ receptors (FcγRs) play critical roles in humoral and cellular immune responses through interactions with the Fc region of immunoglobulin G (IgG).
21965667	0	27	theme	Crystal	0:6	arg1	structure					8:16	Crystal structure	0:16	Crystal structure of Fcγ receptor I	0:34	Crystal structure of Fcγ receptor I and its implication in high affinity γ-immunoglobulin binding.
21965667	7	28	theme	affinity	1165:1172	arg1	binding					1178:1184	the high affinity IgG binding	1156:1184	the high affinity IgG binding	1156:1184	Thus, the FcγRI FG-loop with its conserved one-residue deletion is critical to the high affinity IgG binding.
21965667	7	29	theme	FcγRI	1087:1091	arg1	critical					1144:1151	critical	1144:1151	critical	1144:1151	Thus, the FcγRI FG-loop with its conserved one-residue deletion is critical to the high affinity IgG binding.
21965667	7	29	theme	FcγRI	1087:1091	arg1	FG-loop					1093:1099	the FcγRI FG-loop	1083:1099	the FcγRI FG-loop with its conserved one-residue deletion	1083:1139	Thus, the FcγRI FG-loop with its conserved one-residue deletion is critical to the high affinity IgG binding.
21965667	1	30	theme	immune	165:170	arg1	responses					172:180	humoral and cellular immune responses	144:180	humoral and cellular immune responses	144:180	Fcγ receptors (FcγRs) play critical roles in humoral and cellular immune responses through interactions with the Fc region of immunoglobulin G (IgG).
21965667	0	31	theme	Fcγ	21:23	arg1	receptor					25:32	Fcγ receptor I	21:34	Fcγ receptor I	21:34	Crystal structure of Fcγ receptor I and its implication in high affinity γ-immunoglobulin binding.
21965667	5	32	theme	D3	671:672	arg1	positioned					693:702	positioned	693:702	positioned	693:702	Second, the D3 domain of FcγRI is positioned away from the putative IgG binding site on the receptor and is thus unlikely to make direct contacts with Fc.
21965667	5	32	theme	D3	671:672	arg1	unlikely					772:779	unlikely	772:779	unlikely	772:779	Second, the D3 domain of FcγRI is positioned away from the putative IgG binding site on the receptor and is thus unlikely to make direct contacts with Fc.
21965667	5	32	theme	D3	671:672	arg1	domain					674:679	the D3 domain	667:679	the D3 domain of FcγRI	667:688	Second, the D3 domain of FcγRI is positioned away from the putative IgG binding site on the receptor and is thus unlikely to make direct contacts with Fc.
21965667	5	32	theme	D3	671:672	arg1	FcγRI					684:688	FcγRI	684:688	FcγRI	684:688	Second, the D3 domain of FcγRI is positioned away from the putative IgG binding site on the receptor and is thus unlikely to make direct contacts with Fc.
21965667	1	33	with	interactions	190:201	arg1	region					215:220	the Fc region	208:220	the Fc region of immunoglobulin G (IgG)	208:246	Fcγ receptors (FcγRs) play critical roles in humoral and cellular immune responses through interactions with the Fc region of immunoglobulin G (IgG).
21965667	3	34	dep	domains	452:458	arg1	designated					461:470	designated	461:470	designated as D1, D2, and D3	461:488	Here we report the first crystal structure of an FcγRI with all three extracellular Ig-like domains (designated as D1, D2, and D3).
21965667	5	35	theme	direct	789:794	arg1	contacts					796:803	direct contacts	789:803	direct contacts with Fc	789:811	Second, the D3 domain of FcγRI is positioned away from the putative IgG binding site on the receptor and is thus unlikely to make direct contacts with Fc.
21965667	5	36	theme	FcγRI	684:688	arg1	positioned					693:702	positioned	693:702	positioned	693:702	Second, the D3 domain of FcγRI is positioned away from the putative IgG binding site on the receptor and is thus unlikely to make direct contacts with Fc.
21965667	5	36	theme	FcγRI	684:688	arg1	unlikely					772:779	unlikely	772:779	unlikely	772:779	Second, the D3 domain of FcγRI is positioned away from the putative IgG binding site on the receptor and is thus unlikely to make direct contacts with Fc.
21965667	5	36	theme	FcγRI	684:688	arg1	domain					674:679	the D3 domain	667:679	the D3 domain of FcγRI	667:688	Second, the D3 domain of FcγRI is positioned away from the putative IgG binding site on the receptor and is thus unlikely to make direct contacts with Fc.
21965667	5	36	theme	FcγRI	684:688	arg1	FcγRI					684:688	FcγRI	684:688	FcγRI	684:688	Second, the D3 domain of FcγRI is positioned away from the putative IgG binding site on the receptor and is thus unlikely to make direct contacts with Fc.
21965667	9	37	theme	affinity	1361:1368	arg1	recognition					1374:1384	the high affinity IgG recognition	1352:1384	the high affinity IgG recognition by FcγRI	1352:1393	Taken together, our study suggests a molecular mechanism for the high affinity IgG recognition by FcγRI and provides a structural basis for understanding its physiological function and its therapeutic implication in treating autoimmune diseases.
21965667	4	38	contain	has	531:533	arg2	angle					556:560	an acute D1-D2 hinge angle	535:560	an acute D1-D2 hinge angle similar to that of FcεRI but much smaller than those observed in the low affinity Fcγ receptors	535:656	The structure shows that, first, FcγRI has an acute D1-D2 hinge angle similar to that of FcεRI but much smaller than those observed in the low affinity Fcγ receptors.
21965667	4	38	contain	has	531:533	arg1	FcγRI					525:529	FcγRI	525:529	FcγRI	525:529	The structure shows that, first, FcγRI has an acute D1-D2 hinge angle similar to that of FcεRI but much smaller than those observed in the low affinity Fcγ receptors.
21965667	1	39	theme	Fcγ	99:101	arg1	FcγRs					114:118	FcγRs	114:118	FcγRs	114:118	Fcγ receptors (FcγRs) play critical roles in humoral and cellular immune responses through interactions with the Fc region of immunoglobulin G (IgG).
21965667	1	39	theme	Fcγ	99:101	arg1	receptors					103:111	Fcγ receptors	99:111	Fcγ receptors (FcγRs)	99:119	Fcγ receptors (FcγRs) play critical roles in humoral and cellular immune responses through interactions with the Fc region of immunoglobulin G (IgG).
21965667	7	40	with	FG-loop	1093:1099	arg1	deletion					1132:1139	its conserved one-residue deletion	1106:1139	its conserved one-residue deletion	1106:1139	Thus, the FcγRI FG-loop with its conserved one-residue deletion is critical to the high affinity IgG binding.
21965667	9	41	theme	IgG	1370:1372	arg1	recognition					1374:1384	the high affinity IgG recognition	1352:1384	the high affinity IgG recognition by FcγRI	1352:1393	Taken together, our study suggests a molecular mechanism for the high affinity IgG recognition by FcγRI and provides a structural basis for understanding its physiological function and its therapeutic implication in treating autoimmune diseases.
21965667	6	42	theme	binding	955:961	arg1	affinity					963:970	IgG(1) binding affinity	948:970	IgG(1) binding affinity	948:970	Third, the replacement of FcγRIII FG-loop ((171)LVGSKNV(177)) with that of FcγRI ((171)MGKHRY(176)) resulted in a 15-fold increase in IgG(1) binding affinity, whereas a valine insertion in the FcγRI FG-loop ((171)MVGKHRY(177)) abolished the affinity enhancement.
21965667	4	43	theme	hinge	550:554	arg1	angle					556:560	an acute D1-D2 hinge angle	535:560	an acute D1-D2 hinge angle similar to that of FcεRI but much smaller than those observed in the low affinity Fcγ receptors	535:656	The structure shows that, first, FcγRI has an acute D1-D2 hinge angle similar to that of FcεRI but much smaller than those observed in the low affinity Fcγ receptors.
21965667	3	44	theme	crystal	385:391	arg1	structure					393:401	the first crystal structure	375:401	the first crystal structure of an FcγRI with all three extracellular Ig-like domains (designated as D1, D2, and D3)	375:489	Here we report the first crystal structure of an FcγRI with all three extracellular Ig-like domains (designated as D1, D2, and D3).
21965667	0	45	theme	receptor	25:32	arg1	implication					44:54	its implication	40:54	its implication in high affinity γ-immunoglobulin binding	40:96	Crystal structure of Fcγ receptor I and its implication in high affinity γ-immunoglobulin binding.
21965667	0	45	theme	receptor	25:32	arg1	structure					8:16	Crystal structure	0:16	Crystal structure of Fcγ receptor I	0:34	Crystal structure of Fcγ receptor I and its implication in high affinity γ-immunoglobulin binding.
21965667	8	46	theme	similar	1244:1250	arg1	mode					1252:1255	a similar mode	1242:1255	a similar mode	1242:1255	The structural results support FcγRI binding to IgG in a similar mode as its low affinity counterparts.
21965667	9	47	theme	structural	1410:1419	arg1	basis					1421:1425	a structural basis	1408:1425	a structural basis for understanding its physiological function and its therapeutic implication in treating autoimmune diseases	1408:1534	Taken together, our study suggests a molecular mechanism for the high affinity IgG recognition by FcγRI and provides a structural basis for understanding its physiological function and its therapeutic implication in treating autoimmune diseases.
21965667	9	48	theme	therapeutic	1480:1490	arg1	implication					1492:1502	its therapeutic implication	1476:1502	its therapeutic implication	1476:1502	Taken together, our study suggests a molecular mechanism for the high affinity IgG recognition by FcγRI and provides a structural basis for understanding its physiological function and its therapeutic implication in treating autoimmune diseases.
21965667	5	49	with	contacts	796:803	arg1	Fc					810:811	Fc	810:811	Fc	810:811	Second, the D3 domain of FcγRI is positioned away from the putative IgG binding site on the receptor and is thus unlikely to make direct contacts with Fc.
21965667	9	50	theme	autoimmune	1516:1525	arg1	diseases					1527:1534	autoimmune diseases	1516:1534	autoimmune diseases	1516:1534	Taken together, our study suggests a molecular mechanism for the high affinity IgG recognition by FcγRI and provides a structural basis for understanding its physiological function and its therapeutic implication in treating autoimmune diseases.
21965667	0	51	from	implication	44:54	arg1	binding					90:96	high affinity γ-immunoglobulin binding	59:96	high affinity γ-immunoglobulin binding	59:96	Crystal structure of Fcγ receptor I and its implication in high affinity γ-immunoglobulin binding.
21965667	9	52	theme	high	1356:1359	arg1	recognition					1374:1384	the high affinity IgG recognition	1352:1384	the high affinity IgG recognition by FcγRI	1352:1393	Taken together, our study suggests a molecular mechanism for the high affinity IgG recognition by FcγRI and provides a structural basis for understanding its physiological function and its therapeutic implication in treating autoimmune diseases.
21965667	8	53	theme	FcγRI	1218:1222	arg1	binding					1224:1230	FcγRI binding	1218:1230	FcγRI binding to IgG	1218:1237	The structural results support FcγRI binding to IgG in a similar mode as its low affinity counterparts.
21965667	8	53	theme	FcγRI	1218:1222	arg1	counterparts					1277:1288	its low affinity counterparts	1260:1288	its low affinity counterparts	1260:1288	The structural results support FcγRI binding to IgG in a similar mode as its low affinity counterparts.
21965667	4	54	located	observed	615:622	arg1	receptors					648:656	the low affinity Fcγ receptors	627:656	the low affinity Fcγ receptors	627:656	The structure shows that, first, FcγRI has an acute D1-D2 hinge angle similar to that of FcεRI but much smaller than those observed in the low affinity Fcγ receptors.
21965667	4	54	located	observed	615:622	arg2	those					609:613	those	609:613	those	609:613	The structure shows that, first, FcγRI has an acute D1-D2 hinge angle similar to that of FcεRI but much smaller than those observed in the low affinity Fcγ receptors.
21965667	3	55	theme	FcγRI	409:413	arg1	structure					393:401	the first crystal structure	375:401	the first crystal structure of an FcγRI with all three extracellular Ig-like domains (designated as D1, D2, and D3)	375:489	Here we report the first crystal structure of an FcγRI with all three extracellular Ig-like domains (designated as D1, D2, and D3).
21965667	2	56	theme	affinity	284:291	arg1	FcγRI					261:265	FcγRI	261:265	FcγRI	261:265	Among them, FcγRI is the only high affinity receptor for IgG and thus is a potential target for immunotherapy.
21965667	2	56	theme	affinity	284:291	arg1	receptor					293:300	the only high affinity receptor	270:300	the only high affinity receptor for IgG	270:308	Among them, FcγRI is the only high affinity receptor for IgG and thus is a potential target for immunotherapy.
21965667	6	57	theme	FG-loop	848:854	arg1	replacement					825:835	the replacement	821:835	the replacement of FcγRIII FG-loop ((171)LVGSKNV(177)) with that of FcγRI ((171)MGKHRY(176))	821:912	Third, the replacement of FcγRIII FG-loop ((171)LVGSKNV(177)) with that of FcγRI ((171)MGKHRY(176)) resulted in a 15-fold increase in IgG(1) binding affinity, whereas a valine insertion in the FcγRI FG-loop ((171)MVGKHRY(177)) abolished the affinity enhancement.
21965667	6	58	theme	IgG	948:950	arg1	affinity					963:970	IgG(1) binding affinity	948:970	IgG(1) binding affinity	948:970	Third, the replacement of FcγRIII FG-loop ((171)LVGSKNV(177)) with that of FcγRI ((171)MGKHRY(176)) resulted in a 15-fold increase in IgG(1) binding affinity, whereas a valine insertion in the FcγRI FG-loop ((171)MVGKHRY(177)) abolished the affinity enhancement.
21965667	4	59	theme	similar	562:568	arg1	angle					556:560	an acute D1-D2 hinge angle	535:560	an acute D1-D2 hinge angle similar to that of FcεRI but much smaller than those observed in the low affinity Fcγ receptors	535:656	The structure shows that, first, FcγRI has an acute D1-D2 hinge angle similar to that of FcεRI but much smaller than those observed in the low affinity Fcγ receptors.
21965667	2	60	theme	high	279:282	arg1	FcγRI					261:265	FcγRI	261:265	FcγRI	261:265	Among them, FcγRI is the only high affinity receptor for IgG and thus is a potential target for immunotherapy.
21965667	2	60	theme	high	279:282	arg1	receptor					293:300	the only high affinity receptor	270:300	the only high affinity receptor for IgG	270:308	Among them, FcγRI is the only high affinity receptor for IgG and thus is a potential target for immunotherapy.
21965667	5	61	theme	IgG	727:729	arg1	site					739:742	the putative IgG binding site	714:742	the putative IgG binding site on the receptor	714:758	Second, the D3 domain of FcγRI is positioned away from the putative IgG binding site on the receptor and is thus unlikely to make direct contacts with Fc.
21965667	6	62	from	insertion	990:998	arg1	MVGKHRY					1027:1033	(171)MVGKHRY(177)	1022:1038	(171)MVGKHRY(177)	1022:1038	Third, the replacement of FcγRIII FG-loop ((171)LVGSKNV(177)) with that of FcγRI ((171)MGKHRY(176)) resulted in a 15-fold increase in IgG(1) binding affinity, whereas a valine insertion in the FcγRI FG-loop ((171)MVGKHRY(177)) abolished the affinity enhancement.
21965667	6	62	from	insertion	990:998	arg1	FG-loop					1013:1019	the FcγRI FG-loop	1003:1019	the FcγRI FG-loop ((171)MVGKHRY(177))	1003:1039	Third, the replacement of FcγRIII FG-loop ((171)LVGSKNV(177)) with that of FcγRI ((171)MGKHRY(176)) resulted in a 15-fold increase in IgG(1) binding affinity, whereas a valine insertion in the FcγRI FG-loop ((171)MVGKHRY(177)) abolished the affinity enhancement.
21965667	6	63	theme	FcγRI	1007:1011	arg1	MVGKHRY					1027:1033	(171)MVGKHRY(177)	1022:1038	(171)MVGKHRY(177)	1022:1038	Third, the replacement of FcγRIII FG-loop ((171)LVGSKNV(177)) with that of FcγRI ((171)MGKHRY(176)) resulted in a 15-fold increase in IgG(1) binding affinity, whereas a valine insertion in the FcγRI FG-loop ((171)MVGKHRY(177)) abolished the affinity enhancement.
21965667	6	63	theme	FcγRI	1007:1011	arg1	FG-loop					1013:1019	the FcγRI FG-loop	1003:1019	the FcγRI FG-loop ((171)MVGKHRY(177))	1003:1039	Third, the replacement of FcγRIII FG-loop ((171)LVGSKNV(177)) with that of FcγRI ((171)MGKHRY(176)) resulted in a 15-fold increase in IgG(1) binding affinity, whereas a valine insertion in the FcγRI FG-loop ((171)MVGKHRY(177)) abolished the affinity enhancement.
21965667	7	64	theme	IgG	1174:1176	arg1	binding					1178:1184	the high affinity IgG binding	1156:1184	the high affinity IgG binding	1156:1184	Thus, the FcγRI FG-loop with its conserved one-residue deletion is critical to the high affinity IgG binding.
21965667	2	65	theme	only	274:277	arg1	FcγRI					261:265	FcγRI	261:265	FcγRI	261:265	Among them, FcγRI is the only high affinity receptor for IgG and thus is a potential target for immunotherapy.
21965667	2	65	theme	only	274:277	arg1	receptor					293:300	the only high affinity receptor	270:300	the only high affinity receptor for IgG	270:308	Among them, FcγRI is the only high affinity receptor for IgG and thus is a potential target for immunotherapy.
21965667	1	66	theme	Fc	212:213	arg1	region					215:220	the Fc region	208:220	the Fc region of immunoglobulin G (IgG)	208:246	Fcγ receptors (FcγRs) play critical roles in humoral and cellular immune responses through interactions with the Fc region of immunoglobulin G (IgG).
21965667	7	67	theme	conserved	1110:1118	arg1	deletion					1132:1139	its conserved one-residue deletion	1106:1139	its conserved one-residue deletion	1106:1139	Thus, the FcγRI FG-loop with its conserved one-residue deletion is critical to the high affinity IgG binding.
21965667	6	68	with	replacement	825:835	arg1	that					881:884	that	881:884	that	881:884	Third, the replacement of FcγRIII FG-loop ((171)LVGSKNV(177)) with that of FcγRI ((171)MGKHRY(176)) resulted in a 15-fold increase in IgG(1) binding affinity, whereas a valine insertion in the FcγRI FG-loop ((171)MVGKHRY(177)) abolished the affinity enhancement.
21965667	5	69	theme	binding	731:737	arg1	site					739:742	the putative IgG binding site	714:742	the putative IgG binding site on the receptor	714:758	Second, the D3 domain of FcγRI is positioned away from the putative IgG binding site on the receptor and is thus unlikely to make direct contacts with Fc.
21965667	3	70	theme	first	379:383	arg1	structure					393:401	the first crystal structure	375:401	the first crystal structure of an FcγRI with all three extracellular Ig-like domains (designated as D1, D2, and D3)	375:489	Here we report the first crystal structure of an FcγRI with all three extracellular Ig-like domains (designated as D1, D2, and D3).
21965667	6	71	theme	FcγRIII	840:846	arg1	LVGSKNV					862:868	(171)LVGSKNV(177)	857:873	(171)LVGSKNV(177)	857:873	Third, the replacement of FcγRIII FG-loop ((171)LVGSKNV(177)) with that of FcγRI ((171)MGKHRY(176)) resulted in a 15-fold increase in IgG(1) binding affinity, whereas a valine insertion in the FcγRI FG-loop ((171)MVGKHRY(177)) abolished the affinity enhancement.
21965667	6	71	theme	FcγRIII	840:846	arg1	FG-loop					848:854	FcγRIII FG-loop	840:854	FcγRIII FG-loop ((171)LVGSKNV(177))	840:874	Third, the replacement of FcγRIII FG-loop ((171)LVGSKNV(177)) with that of FcγRI ((171)MGKHRY(176)) resulted in a 15-fold increase in IgG(1) binding affinity, whereas a valine insertion in the FcγRI FG-loop ((171)MVGKHRY(177)) abolished the affinity enhancement.
21965667	6	72	dep	affinity	963:970	arg1	1					952:952	1	952:952	1	952:952	Third, the replacement of FcγRIII FG-loop ((171)LVGSKNV(177)) with that of FcγRI ((171)MGKHRY(176)) resulted in a 15-fold increase in IgG(1) binding affinity, whereas a valine insertion in the FcγRI FG-loop ((171)MVGKHRY(177)) abolished the affinity enhancement.
21965667	7	73	theme	high	1160:1163	arg1	binding					1178:1184	the high affinity IgG binding	1156:1184	the high affinity IgG binding	1156:1184	Thus, the FcγRI FG-loop with its conserved one-residue deletion is critical to the high affinity IgG binding.
21965667	6	74	theme	15-fold	928:934	arg1	increase					936:943	a 15-fold increase	926:943	a 15-fold increase in IgG(1) binding affinity	926:970	Third, the replacement of FcγRIII FG-loop ((171)LVGSKNV(177)) with that of FcγRI ((171)MGKHRY(176)) resulted in a 15-fold increase in IgG(1) binding affinity, whereas a valine insertion in the FcγRI FG-loop ((171)MVGKHRY(177)) abolished the affinity enhancement.
21965667	1	75	theme	critical	126:133	arg1	roles					135:139	critical roles	126:139	critical roles	126:139	Fcγ receptors (FcγRs) play critical roles in humoral and cellular immune responses through interactions with the Fc region of immunoglobulin G (IgG).
21965667	6	76	from	increase	936:943	arg1	affinity					963:970	IgG(1) binding affinity	948:970	IgG(1) binding affinity	948:970	Third, the replacement of FcγRIII FG-loop ((171)LVGSKNV(177)) with that of FcγRI ((171)MGKHRY(176)) resulted in a 15-fold increase in IgG(1) binding affinity, whereas a valine insertion in the FcγRI FG-loop ((171)MVGKHRY(177)) abolished the affinity enhancement.
21965667	8	77	theme	affinity	1268:1275	arg1	binding					1224:1230	FcγRI binding	1218:1230	FcγRI binding to IgG	1218:1237	The structural results support FcγRI binding to IgG in a similar mode as its low affinity counterparts.
21965667	8	77	theme	affinity	1268:1275	arg1	counterparts					1277:1288	its low affinity counterparts	1260:1288	its low affinity counterparts	1260:1288	The structural results support FcγRI binding to IgG in a similar mode as its low affinity counterparts.
1551440	0	0	theme	pathway	62:68	arg1	control					36:42	the control	32:42	the control of the complement pathway	32:68	SP-40,40, a protein involved in the control of the complement pathway, possesses a unique array of disulphide bridges.
1551440	4	1	theme	free	504:507	arg1	residues					518:525	no free cysteine residues	501:525	no free cysteine residues	501:525	There are no free cysteine residues.
1551440	0	2	theme	complement	51:60	arg1	pathway					62:68	the complement pathway	47:68	the complement pathway	47:68	SP-40,40, a protein involved in the control of the complement pathway, possesses a unique array of disulphide bridges.
1551440	5	3	theme	disulphide	532:541	arg1	unique					596:601	unique	596:601	unique	596:601	The disulphide bond motif established in this study for SP-40,40 is unique and bears no obvious homology to those complement components whose disulphide bonds have been assigned, nor is there any homology apparent between SP-40,40 and other multi-chain proteins containing disulphide bonds.
1551440	5	3	theme	disulphide	532:541	arg1	motif					548:552	The disulphide bond motif	528:552	The disulphide bond motif established in this study for SP-40,40	528:591	The disulphide bond motif established in this study for SP-40,40 is unique and bears no obvious homology to those complement components whose disulphide bonds have been assigned, nor is there any homology apparent between SP-40,40 and other multi-chain proteins containing disulphide bonds.
1551440	3	4	theme	interchain	449:458	arg1	bonds					484:488	interchain (alpha-beta) disulphide bonds	449:488	interchain (alpha-beta) disulphide bonds	449:488	Evidence is presented that all the cysteine residues are involved in interchain (alpha-beta) disulphide bonds.
1551440	1	5	theme	assembly	206:213	arg1	inhibitor					189:197	a potent inhibitor	180:197	a potent inhibitor of the assembly of the membrane attack complex of human complement	180:264	SP-40,40 is a two-chain serum protein which acts in vitro as a potent inhibitor of the assembly of the membrane attack complex of human complement.
1551440	1	5	theme	assembly	206:213	arg1	protein					149:155	a two-chain serum protein	131:155	a two-chain serum protein which acts in vitro as a potent inhibitor of the assembly of the membrane attack complex of human complement	131:264	SP-40,40 is a two-chain serum protein which acts in vitro as a potent inhibitor of the assembly of the membrane attack complex of human complement.
1551440	5	6	theme	bond	543:546	arg1	unique					596:601	unique	596:601	unique	596:601	The disulphide bond motif established in this study for SP-40,40 is unique and bears no obvious homology to those complement components whose disulphide bonds have been assigned, nor is there any homology apparent between SP-40,40 and other multi-chain proteins containing disulphide bonds.
1551440	5	6	theme	bond	543:546	arg1	motif					548:552	The disulphide bond motif	528:552	The disulphide bond motif established in this study for SP-40,40	528:591	The disulphide bond motif established in this study for SP-40,40 is unique and bears no obvious homology to those complement components whose disulphide bonds have been assigned, nor is there any homology apparent between SP-40,40 and other multi-chain proteins containing disulphide bonds.
1551440	5	7	theme	disulphide	670:679	arg1	bonds					681:685	disulphide bonds	670:685	disulphide bonds	670:685	The disulphide bond motif established in this study for SP-40,40 is unique and bears no obvious homology to those complement components whose disulphide bonds have been assigned, nor is there any homology apparent between SP-40,40 and other multi-chain proteins containing disulphide bonds.
1551440	0	8	theme	unique	83:88	arg1	array					90:94	a unique array	81:94	a unique array of disulphide bridges	81:116	SP-40,40, a protein involved in the control of the complement pathway, possesses a unique array of disulphide bridges.
1551440	5	9	theme	multi-chain	769:779	arg1	proteins					781:788	other multi-chain proteins	763:788	other multi-chain proteins containing disulphide bonds	763:816	The disulphide bond motif established in this study for SP-40,40 is unique and bears no obvious homology to those complement components whose disulphide bonds have been assigned, nor is there any homology apparent between SP-40,40 and other multi-chain proteins containing disulphide bonds.
1551440	1	10	theme	two-chain	133:141	arg1	protein					149:155	a two-chain serum protein	131:155	a two-chain serum protein which acts in vitro as a potent inhibitor of the assembly of the membrane attack complex of human complement	131:264	SP-40,40 is a two-chain serum protein which acts in vitro as a potent inhibitor of the assembly of the membrane attack complex of human complement.
1551440	1	10	theme	two-chain	133:141	arg1	inhibitor					189:197	a potent inhibitor	180:197	a potent inhibitor of the assembly of the membrane attack complex of human complement	180:264	SP-40,40 is a two-chain serum protein which acts in vitro as a potent inhibitor of the assembly of the membrane attack complex of human complement.
1551440	1	10	theme	two-chain	133:141	arg1	SP-40,40					119:126	SP-40,40	119:126	SP-40,40	119:126	SP-40,40 is a two-chain serum protein which acts in vitro as a potent inhibitor of the assembly of the membrane attack complex of human complement.
1551440	5	11	contain	containing	790:799	arg1	proteins					781:788	other multi-chain proteins	763:788	other multi-chain proteins containing disulphide bonds	763:816	The disulphide bond motif established in this study for SP-40,40 is unique and bears no obvious homology to those complement components whose disulphide bonds have been assigned, nor is there any homology apparent between SP-40,40 and other multi-chain proteins containing disulphide bonds.
1551440	5	11	contain	containing	790:799	arg2	bonds					812:816	disulphide bonds	801:816	disulphide bonds	801:816	The disulphide bond motif established in this study for SP-40,40 is unique and bears no obvious homology to those complement components whose disulphide bonds have been assigned, nor is there any homology apparent between SP-40,40 and other multi-chain proteins containing disulphide bonds.
1551440	3	12	theme	disulphide	473:482	arg1	bonds					484:488	interchain (alpha-beta) disulphide bonds	449:488	interchain (alpha-beta) disulphide bonds	449:488	Evidence is presented that all the cysteine residues are involved in interchain (alpha-beta) disulphide bonds.
1551440	1	13	theme	serum	143:147	arg1	protein					149:155	a two-chain serum protein	131:155	a two-chain serum protein which acts in vitro as a potent inhibitor of the assembly of the membrane attack complex of human complement	131:264	SP-40,40 is a two-chain serum protein which acts in vitro as a potent inhibitor of the assembly of the membrane attack complex of human complement.
1551440	1	13	theme	serum	143:147	arg1	inhibitor					189:197	a potent inhibitor	180:197	a potent inhibitor of the assembly of the membrane attack complex of human complement	180:264	SP-40,40 is a two-chain serum protein which acts in vitro as a potent inhibitor of the assembly of the membrane attack complex of human complement.
1551440	1	13	theme	serum	143:147	arg1	SP-40,40					119:126	SP-40,40	119:126	SP-40,40	119:126	SP-40,40 is a two-chain serum protein which acts in vitro as a potent inhibitor of the assembly of the membrane attack complex of human complement.
1551440	5	14	theme	apparent	733:740	arg1	homology					724:731	any homology apparent	720:740	any homology apparent between SP-40,40 and other multi-chain proteins containing disulphide bonds	720:816	The disulphide bond motif established in this study for SP-40,40 is unique and bears no obvious homology to those complement components whose disulphide bonds have been assigned, nor is there any homology apparent between SP-40,40 and other multi-chain proteins containing disulphide bonds.
1551440	5	15	theme	complement	642:651	arg1	components					653:662	those complement components	636:662	those complement components whose disulphide bonds have been assigned	636:704	The disulphide bond motif established in this study for SP-40,40 is unique and bears no obvious homology to those complement components whose disulphide bonds have been assigned, nor is there any homology apparent between SP-40,40 and other multi-chain proteins containing disulphide bonds.
1551440	1	16	theme	membrane	222:229	arg1	complex					238:244	the membrane attack complex	218:244	the membrane attack complex of human complement	218:264	SP-40,40 is a two-chain serum protein which acts in vitro as a potent inhibitor of the assembly of the membrane attack complex of human complement.
1551440	1	17	theme	attack	231:236	arg1	complex					238:244	the membrane attack complex	218:244	the membrane attack complex of human complement	218:264	SP-40,40 is a two-chain serum protein which acts in vitro as a potent inhibitor of the assembly of the membrane attack complex of human complement.
1551440	2	18	theme	mammalian	361:369	arg1	species					371:377	several mammalian species	353:377	several mammalian species	353:377	It contains 10 cysteine residues, the numbers and locations of which are conserved in several mammalian species.
1551440	1	19	theme	complex	238:244	arg1	assembly					206:213	the assembly	202:213	the assembly of the membrane attack complex of human complement	202:264	SP-40,40 is a two-chain serum protein which acts in vitro as a potent inhibitor of the assembly of the membrane attack complex of human complement.
1551440	4	20	theme	cysteine	509:516	arg1	residues					518:525	no free cysteine residues	501:525	no free cysteine residues	501:525	There are no free cysteine residues.
1551440	2	21	theme	several	353:359	arg1	species					371:377	several mammalian species	353:377	several mammalian species	353:377	It contains 10 cysteine residues, the numbers and locations of which are conserved in several mammalian species.
1551440	0	22	theme	bridges	110:116	arg1	array					90:94	a unique array	81:94	a unique array of disulphide bridges	81:116	SP-40,40, a protein involved in the control of the complement pathway, possesses a unique array of disulphide bridges.
1551440	5	23	theme	disulphide	801:810	arg1	bonds					812:816	disulphide bonds	801:816	disulphide bonds	801:816	The disulphide bond motif established in this study for SP-40,40 is unique and bears no obvious homology to those complement components whose disulphide bonds have been assigned, nor is there any homology apparent between SP-40,40 and other multi-chain proteins containing disulphide bonds.
1551440	1	24	theme	human	249:253	arg1	complement					255:264	human complement	249:264	human complement	249:264	SP-40,40 is a two-chain serum protein which acts in vitro as a potent inhibitor of the assembly of the membrane attack complex of human complement.
1551440	0	25	theme	disulphide	99:108	arg1	bridges					110:116	disulphide bridges	99:116	disulphide bridges	99:116	SP-40,40, a protein involved in the control of the complement pathway, possesses a unique array of disulphide bridges.
1551440	1	26	theme	complement	255:264	arg1	complex					238:244	the membrane attack complex	218:244	the membrane attack complex of human complement	218:264	SP-40,40 is a two-chain serum protein which acts in vitro as a potent inhibitor of the assembly of the membrane attack complex of human complement.
1551440	2	27	theme	residues	291:298	arg1	locations					317:325	locations	317:325	locations	317:325	It contains 10 cysteine residues, the numbers and locations of which are conserved in several mammalian species.
1551440	2	27	theme	residues	291:298	arg1	numbers					305:311	numbers	305:311	numbers	305:311	It contains 10 cysteine residues, the numbers and locations of which are conserved in several mammalian species.
1551440	2	28	theme	cysteine	282:289	arg1	residues					291:298	10 cysteine residues	279:298	10 cysteine residues	279:298	It contains 10 cysteine residues, the numbers and locations of which are conserved in several mammalian species.
1551440	5	29	contain	bears	607:611	arg2	homology					624:631	no obvious homology	613:631	no obvious homology to those complement components whose disulphide bonds have been assigned	613:704	The disulphide bond motif established in this study for SP-40,40 is unique and bears no obvious homology to those complement components whose disulphide bonds have been assigned, nor is there any homology apparent between SP-40,40 and other multi-chain proteins containing disulphide bonds.
1551440	5	29	contain	bears	607:611	arg1	unique					596:601	unique	596:601	unique	596:601	The disulphide bond motif established in this study for SP-40,40 is unique and bears no obvious homology to those complement components whose disulphide bonds have been assigned, nor is there any homology apparent between SP-40,40 and other multi-chain proteins containing disulphide bonds.
1551440	5	29	contain	bears	607:611	arg1	motif					548:552	The disulphide bond motif	528:552	The disulphide bond motif established in this study for SP-40,40	528:591	The disulphide bond motif established in this study for SP-40,40 is unique and bears no obvious homology to those complement components whose disulphide bonds have been assigned, nor is there any homology apparent between SP-40,40 and other multi-chain proteins containing disulphide bonds.
1551440	5	30	theme	obvious	616:622	arg1	homology					624:631	no obvious homology	613:631	no obvious homology to those complement components whose disulphide bonds have been assigned	613:704	The disulphide bond motif established in this study for SP-40,40 is unique and bears no obvious homology to those complement components whose disulphide bonds have been assigned, nor is there any homology apparent between SP-40,40 and other multi-chain proteins containing disulphide bonds.
1551440	0	31	contain	possesses	71:79	arg2	array					90:94	a unique array	81:94	a unique array of disulphide bridges	81:116	SP-40,40, a protein involved in the control of the complement pathway, possesses a unique array of disulphide bridges.
1551440	0	31	contain	possesses	71:79	arg1	SP-40,40					0:7	SP-40,40	0:7	SP-40,40	0:7	SP-40,40, a protein involved in the control of the complement pathway, possesses a unique array of disulphide bridges.
1551440	0	31	contain	possesses	71:79	arg1	protein					12:18	a protein	10:18	a protein involved in the control of the complement pathway	10:68	SP-40,40, a protein involved in the control of the complement pathway, possesses a unique array of disulphide bridges.
1551440	3	32	theme	cysteine	415:422	arg1	residues					424:431	all the cysteine residues	407:431	all the cysteine residues	407:431	Evidence is presented that all the cysteine residues are involved in interchain (alpha-beta) disulphide bonds.
1551440	1	33	theme	potent	182:187	arg1	inhibitor					189:197	a potent inhibitor	180:197	a potent inhibitor of the assembly of the membrane attack complex of human complement	180:264	SP-40,40 is a two-chain serum protein which acts in vitro as a potent inhibitor of the assembly of the membrane attack complex of human complement.
1551440	1	33	theme	potent	182:187	arg1	protein					149:155	a two-chain serum protein	131:155	a two-chain serum protein which acts in vitro as a potent inhibitor of the assembly of the membrane attack complex of human complement	131:264	SP-40,40 is a two-chain serum protein which acts in vitro as a potent inhibitor of the assembly of the membrane attack complex of human complement.
1551440	5	34	theme	other	763:767	arg1	proteins					781:788	other multi-chain proteins	763:788	other multi-chain proteins containing disulphide bonds	763:816	The disulphide bond motif established in this study for SP-40,40 is unique and bears no obvious homology to those complement components whose disulphide bonds have been assigned, nor is there any homology apparent between SP-40,40 and other multi-chain proteins containing disulphide bonds.
1551440	2	35	contain	contains	270:277	arg2	residues					291:298	10 cysteine residues	279:298	10 cysteine residues	279:298	It contains 10 cysteine residues, the numbers and locations of which are conserved in several mammalian species.
1551440	2	35	contain	contains	270:277	arg1	It					267:268	It	267:268	It	267:268	It contains 10 cysteine residues, the numbers and locations of which are conserved in several mammalian species.
1551440	3	36	theme	alpha-beta	461:470	arg1	bonds					484:488	interchain (alpha-beta) disulphide bonds	449:488	interchain (alpha-beta) disulphide bonds	449:488	Evidence is presented that all the cysteine residues are involved in interchain (alpha-beta) disulphide bonds.
6526384	5	0	theme	cysteine	626:633	arg1	residues					635:642	The 20 cysteine residues	619:642	The 20 cysteine residues	619:642	The 20 cysteine residues form 10 disulfide bonds, 9 of which confirm the internal homology by their characteristic arrangement.
6526384	5	1	theme	internal	692:699	arg1	homology					701:708	the internal homology	688:708	the internal homology	688:708	The 20 cysteine residues form 10 disulfide bonds, 9 of which confirm the internal homology by their characteristic arrangement.
6526384	6	2	theme	free	751:754	arg1	component					766:774	The free secretory component	747:774	The free secretory component	747:774	The free secretory component also shows homology to immunoglobulins in some sections.
6526384	0	3	theme	bonds	90:94	arg1	structure					13:21	[The primary structure	0:21	[The primary structure of human free secretory component	0:55	[The primary structure of human free secretory component and the arrangement of disulfide bonds].
6526384	0	3	theme	bonds	90:94	arg1	arrangement					65:75	the arrangement	61:75	the arrangement of disulfide bonds	61:94	[The primary structure of human free secretory component and the arrangement of disulfide bonds].
6526384	7	4	theme	free	893:896	arg1	component					908:916	the free secretory component	889:916	the free secretory component	889:916	A computer-supported tertiary structure is proposed for the free secretory component.
6526384	2	5	theme	free	271:274	arg1	component					286:294	The free secretory component	267:294	The free secretory component	267:294	The free secretory component is a monomeric glycoprotein (Mr approximately 86000), consisting of 558 amino acids with 7 carbohydrate chains bound to asparagine.
6526384	2	5	theme	free	271:274	arg1	glycoprotein					311:322	a monomeric glycoprotein	299:322	a monomeric glycoprotein (Mr approximately 86000)	299:347	The free secretory component is a monomeric glycoprotein (Mr approximately 86000), consisting of 558 amino acids with 7 carbohydrate chains bound to asparagine.
6526384	0	6	theme	disulfide	80:88	arg1	bonds					90:94	disulfide bonds	80:94	disulfide bonds	80:94	[The primary structure of human free secretory component and the arrangement of disulfide bonds].
6526384	7	7	theme	secretory	898:906	arg1	component					908:916	the free secretory component	889:916	the free secretory component	889:916	A computer-supported tertiary structure is proposed for the free secretory component.
6526384	1	8	theme	protein	248:254	arg1	chemistry					256:264	protein chemistry	248:264	protein chemistry	248:264	The amino-acid sequence and the arrangement of the disulfide bonds of the human free secretory component were completely elucidated by the methods of protein chemistry.
6526384	2	9	with	acids	374:378	arg1	chains					400:405	7 carbohydrate chains	385:405	7 carbohydrate chains bound to asparagine	385:425	The free secretory component is a monomeric glycoprotein (Mr approximately 86000), consisting of 558 amino acids with 7 carbohydrate chains bound to asparagine.
6526384	1	10	theme	disulfide	149:157	arg1	bonds					159:163	the disulfide bonds	145:163	the disulfide bonds of the human free secretory component	145:201	The amino-acid sequence and the arrangement of the disulfide bonds of the human free secretory component were completely elucidated by the methods of protein chemistry.
6526384	5	11	theme	characteristic	719:732	arg1	arrangement					734:744	their characteristic arrangement	713:744	their characteristic arrangement	713:744	The 20 cysteine residues form 10 disulfide bonds, 9 of which confirm the internal homology by their characteristic arrangement.
6526384	4	12	from	acids	602:606	arg1	length					611:616	length	611:616	length	611:616	The polypeptide chain is divided into five regions of internal homology, 104 to 114 amino acids in length.
6526384	1	13	theme	bonds	159:163	arg1	sequence					113:120	The amino-acid sequence	98:120	The amino-acid sequence	98:120	The amino-acid sequence and the arrangement of the disulfide bonds of the human free secretory component were completely elucidated by the methods of protein chemistry.
6526384	1	13	theme	bonds	159:163	arg1	arrangement					130:140	the arrangement	126:140	the arrangement of the disulfide bonds of the human free secretory component	126:201	The amino-acid sequence and the arrangement of the disulfide bonds of the human free secretory component were completely elucidated by the methods of protein chemistry.
6526384	0	14	theme	primary	5:11	arg1	structure					13:21	[The primary structure	0:21	[The primary structure of human free secretory component	0:55	[The primary structure of human free secretory component and the arrangement of disulfide bonds].
6526384	4	15	theme	amino	596:600	arg1	acids					602:606	104 to 114 amino acids	585:606	104 to 114 amino acids in length	585:616	The polypeptide chain is divided into five regions of internal homology, 104 to 114 amino acids in length.
6526384	4	15	theme	amino	596:600	arg1	regions					555:561	five regions	550:561	five regions of internal homology	550:582	The polypeptide chain is divided into five regions of internal homology, 104 to 114 amino acids in length.
6526384	0	16	theme	[The	0:3	arg1	structure					13:21	[The primary structure	0:21	[The primary structure of human free secretory component	0:55	[The primary structure of human free secretory component and the arrangement of disulfide bonds].
6526384	1	17	theme	chemistry	256:264	arg1	methods					237:243	the methods	233:243	the methods of protein chemistry	233:264	The amino-acid sequence and the arrangement of the disulfide bonds of the human free secretory component were completely elucidated by the methods of protein chemistry.
6526384	2	18	theme	carbohydrate	387:398	arg1	chains					400:405	7 carbohydrate chains	385:405	7 carbohydrate chains bound to asparagine	385:425	The free secretory component is a monomeric glycoprotein (Mr approximately 86000), consisting of 558 amino acids with 7 carbohydrate chains bound to asparagine.
6526384	2	19	theme	secretory	276:284	arg1	component					286:294	The free secretory component	267:294	The free secretory component	267:294	The free secretory component is a monomeric glycoprotein (Mr approximately 86000), consisting of 558 amino acids with 7 carbohydrate chains bound to asparagine.
6526384	2	19	theme	secretory	276:284	arg1	glycoprotein					311:322	a monomeric glycoprotein	299:322	a monomeric glycoprotein (Mr approximately 86000)	299:347	The free secretory component is a monomeric glycoprotein (Mr approximately 86000), consisting of 558 amino acids with 7 carbohydrate chains bound to asparagine.
6526384	1	20	theme	free	178:181	arg1	component					193:201	the human free secretory component	168:201	the human free secretory component	168:201	The amino-acid sequence and the arrangement of the disulfide bonds of the human free secretory component were completely elucidated by the methods of protein chemistry.
6526384	0	21	theme	free	32:35	arg1	component					47:55	human free secretory component	26:55	human free secretory component	26:55	[The primary structure of human free secretory component and the arrangement of disulfide bonds].
6526384	4	22	theme	polypeptide	516:526	arg1	chain					528:532	The polypeptide chain	512:532	The polypeptide chain	512:532	The polypeptide chain is divided into five regions of internal homology, 104 to 114 amino acids in length.
6526384	5	23	theme	disulfide	652:660	arg1	bonds					662:666	10 disulfide bonds	649:666	10 disulfide bonds	649:666	The 20 cysteine residues form 10 disulfide bonds, 9 of which confirm the internal homology by their characteristic arrangement.
6526384	7	24	theme	tertiary	854:861	arg1	structure					863:871	A computer-supported tertiary structure	833:871	A computer-supported tertiary structure	833:871	A computer-supported tertiary structure is proposed for the free secretory component.
6526384	1	25	theme	secretory	183:191	arg1	component					193:201	the human free secretory component	168:201	the human free secretory component	168:201	The amino-acid sequence and the arrangement of the disulfide bonds of the human free secretory component were completely elucidated by the methods of protein chemistry.
6526384	2	26	theme	amino	368:372	arg1	acids					374:378	558 amino acids	364:378	558 amino acids with 7 carbohydrate chains bound to asparagine	364:425	The free secretory component is a monomeric glycoprotein (Mr approximately 86000), consisting of 558 amino acids with 7 carbohydrate chains bound to asparagine.
6526384	0	27	theme	human	26:30	arg1	component					47:55	human free secretory component	26:55	human free secretory component	26:55	[The primary structure of human free secretory component and the arrangement of disulfide bonds].
6526384	3	28	contain	contains	440:447	arg1	protein					432:438	The protein	428:438	The protein	428:438	The protein contains 20 cysteine residues but, as a special feature, no methionine.
6526384	3	28	contain	contains	440:447	arg2	residues					461:468	20 cysteine residues	449:468	20 cysteine residues	449:468	The protein contains 20 cysteine residues but, as a special feature, no methionine.
6526384	1	29	theme	component	193:201	arg1	bonds					159:163	the disulfide bonds	145:163	the disulfide bonds of the human free secretory component	145:201	The amino-acid sequence and the arrangement of the disulfide bonds of the human free secretory component were completely elucidated by the methods of protein chemistry.
6526384	0	30	theme	component	47:55	arg1	structure					13:21	[The primary structure	0:21	[The primary structure of human free secretory component	0:55	[The primary structure of human free secretory component and the arrangement of disulfide bonds].
6526384	0	30	theme	component	47:55	arg1	arrangement					65:75	the arrangement	61:75	the arrangement of disulfide bonds	61:94	[The primary structure of human free secretory component and the arrangement of disulfide bonds].
6526384	5	31	theme	bonds	662:666	arg1	9					669:669	9	669:669	9	669:669	The 20 cysteine residues form 10 disulfide bonds, 9 of which confirm the internal homology by their characteristic arrangement.
6526384	5	31	theme	bonds	662:666	arg1	bonds					662:666	10 disulfide bonds	649:666	10 disulfide bonds	649:666	The 20 cysteine residues form 10 disulfide bonds, 9 of which confirm the internal homology by their characteristic arrangement.
6526384	0	32	theme	secretory	37:45	arg1	component					47:55	human free secretory component	26:55	human free secretory component	26:55	[The primary structure of human free secretory component and the arrangement of disulfide bonds].
6526384	1	33	theme	amino-acid	102:111	arg1	sequence					113:120	The amino-acid sequence	98:120	The amino-acid sequence	98:120	The amino-acid sequence and the arrangement of the disulfide bonds of the human free secretory component were completely elucidated by the methods of protein chemistry.
6526384	2	34	gly	glycoprotein	311:322	arg1	component					286:294	The free secretory component	267:294	The free secretory component	267:294	The free secretory component is a monomeric glycoprotein (Mr approximately 86000), consisting of 558 amino acids with 7 carbohydrate chains bound to asparagine.
6526384	2	34	gly	glycoprotein	311:322	arg1	Mr					325:326	Mr approximately 86000	325:346	Mr approximately 86000	325:346	The free secretory component is a monomeric glycoprotein (Mr approximately 86000), consisting of 558 amino acids with 7 carbohydrate chains bound to asparagine.
6526384	2	34	gly	glycoprotein	311:322	arg1	glycoprotein					311:322	a monomeric glycoprotein	299:322	a monomeric glycoprotein (Mr approximately 86000)	299:347	The free secretory component is a monomeric glycoprotein (Mr approximately 86000), consisting of 558 amino acids with 7 carbohydrate chains bound to asparagine.
6526384	2	35	theme	monomeric	301:309	arg1	component					286:294	The free secretory component	267:294	The free secretory component	267:294	The free secretory component is a monomeric glycoprotein (Mr approximately 86000), consisting of 558 amino acids with 7 carbohydrate chains bound to asparagine.
6526384	2	35	theme	monomeric	301:309	arg1	Mr					325:326	Mr approximately 86000	325:346	Mr approximately 86000	325:346	The free secretory component is a monomeric glycoprotein (Mr approximately 86000), consisting of 558 amino acids with 7 carbohydrate chains bound to asparagine.
6526384	2	35	theme	monomeric	301:309	arg1	glycoprotein					311:322	a monomeric glycoprotein	299:322	a monomeric glycoprotein (Mr approximately 86000)	299:347	The free secretory component is a monomeric glycoprotein (Mr approximately 86000), consisting of 558 amino acids with 7 carbohydrate chains bound to asparagine.
6526384	7	36	theme	computer-supported	835:852	arg1	structure					863:871	A computer-supported tertiary structure	833:871	A computer-supported tertiary structure	833:871	A computer-supported tertiary structure is proposed for the free secretory component.
6526384	6	37	theme	secretory	756:764	arg1	component					766:774	The free secretory component	747:774	The free secretory component	747:774	The free secretory component also shows homology to immunoglobulins in some sections.
6526384	4	38	dep	acids	602:606	arg1	to					589:590	to	589:590	to	589:590	The polypeptide chain is divided into five regions of internal homology, 104 to 114 amino acids in length.
6526384	1	39	theme	human	172:176	arg1	component					193:201	the human free secretory component	168:201	the human free secretory component	168:201	The amino-acid sequence and the arrangement of the disulfide bonds of the human free secretory component were completely elucidated by the methods of protein chemistry.
6526384	3	40	theme	cysteine	452:459	arg1	residues					461:468	20 cysteine residues	449:468	20 cysteine residues	449:468	The protein contains 20 cysteine residues but, as a special feature, no methionine.
6526384	4	41	theme	homology	575:582	arg1	acids					602:606	104 to 114 amino acids	585:606	104 to 114 amino acids in length	585:616	The polypeptide chain is divided into five regions of internal homology, 104 to 114 amino acids in length.
6526384	4	41	theme	homology	575:582	arg1	regions					555:561	five regions	550:561	five regions of internal homology	550:582	The polypeptide chain is divided into five regions of internal homology, 104 to 114 amino acids in length.
6526384	3	42	theme	special	480:486	arg1	feature					488:494	a special feature	478:494	a special feature	478:494	The protein contains 20 cysteine residues but, as a special feature, no methionine.
6526384	4	43	theme	internal	566:573	arg1	homology					575:582	internal homology	566:582	internal homology	566:582	The polypeptide chain is divided into five regions of internal homology, 104 to 114 amino acids in length.
17761881	3	0	theme	antiparallel	517:528	arg1	dimer					531:535	a homophilic trans (antiparallel) dimer	497:535	a homophilic trans (antiparallel) dimer with an extended and rigid architecture, matching the dimensions of adherens junctions	497:622	Here we describe a 3.1 angstrom crystal structure of the RPTPmu ectodomain that forms a homophilic trans (antiparallel) dimer with an extended and rigid architecture, matching the dimensions of adherens junctions.
17761881	5	1	theme	distance	802:809	arg1	gauge					811:815	a distance gauge	800:815	a distance gauge	800:815	These data suggest that the RPTPmu ectodomain acts as a distance gauge and plays a key regulatory function, locking the phosphatase to its appropriate functional location.
17761881	5	1	theme	distance	802:809	arg1	ectodomain					781:790	the RPTPmu ectodomain	770:790	the RPTPmu ectodomain	770:790	These data suggest that the RPTPmu ectodomain acts as a distance gauge and plays a key regulatory function, locking the phosphatase to its appropriate functional location.
17761881	5	1	theme	distance	802:809	arg1	function					844:851	a key regulatory function	827:851	a key regulatory function	827:851	These data suggest that the RPTPmu ectodomain acts as a distance gauge and plays a key regulatory function, locking the phosphatase to its appropriate functional location.
17761881	1	2	theme	exquisite	172:180	arg1	levels					182:187	exquisite levels	172:187	exquisite levels of control	172:198	Cell-cell contacts are fundamental to multicellular organisms and are subject to exquisite levels of control.
17761881	3	3	with	dimer	531:535	arg1	architecture					564:575	an extended and rigid architecture	542:575	an extended and rigid architecture	542:575	Here we describe a 3.1 angstrom crystal structure of the RPTPmu ectodomain that forms a homophilic trans (antiparallel) dimer with an extended and rigid architecture, matching the dimensions of adherens junctions.
17761881	3	4	theme	rigid	558:562	arg1	architecture					564:575	an extended and rigid architecture	542:575	an extended and rigid architecture	542:575	Here we describe a 3.1 angstrom crystal structure of the RPTPmu ectodomain that forms a homophilic trans (antiparallel) dimer with an extended and rigid architecture, matching the dimensions of adherens junctions.
17761881	2	5	theme	adhesive	285:292	arg1	contact					294:300	an adhesive contact	282:300	an adhesive contact itself	282:307	Human RPTPmu is a type IIB receptor protein tyrosine phosphatase that both forms an adhesive contact itself and is involved in regulating adhesion by dephosphorylating components of cadherin-catenin complexes.
17761881	5	6	theme	RPTPmu	774:779	arg1	gauge					811:815	a distance gauge	800:815	a distance gauge	800:815	These data suggest that the RPTPmu ectodomain acts as a distance gauge and plays a key regulatory function, locking the phosphatase to its appropriate functional location.
17761881	5	6	theme	RPTPmu	774:779	arg1	ectodomain					781:790	the RPTPmu ectodomain	770:790	the RPTPmu ectodomain	770:790	These data suggest that the RPTPmu ectodomain acts as a distance gauge and plays a key regulatory function, locking the phosphatase to its appropriate functional location.
17761881	5	6	theme	RPTPmu	774:779	arg1	function					844:851	a key regulatory function	827:851	a key regulatory function	827:851	These data suggest that the RPTPmu ectodomain acts as a distance gauge and plays a key regulatory function, locking the phosphatase to its appropriate functional location.
17761881	1	7	theme	control	192:198	arg1	levels					182:187	exquisite levels	172:187	exquisite levels of control	172:198	Cell-cell contacts are fundamental to multicellular organisms and are subject to exquisite levels of control.
17761881	3	8	theme	extended	545:552	arg1	architecture					564:575	an extended and rigid architecture	542:575	an extended and rigid architecture	542:575	Here we describe a 3.1 angstrom crystal structure of the RPTPmu ectodomain that forms a homophilic trans (antiparallel) dimer with an extended and rigid architecture, matching the dimensions of adherens junctions.
17761881	4	9	theme	intercellular	680:692	arg1	spacings					694:701	intercellular spacings	680:701	intercellular spacings that correlate with the ectodomain length	680:743	Cell surface expression of deletion constructs induces intercellular spacings that correlate with the ectodomain length.
17761881	5	10	theme	key	829:831	arg1	gauge					811:815	a distance gauge	800:815	a distance gauge	800:815	These data suggest that the RPTPmu ectodomain acts as a distance gauge and plays a key regulatory function, locking the phosphatase to its appropriate functional location.
17761881	5	10	theme	key	829:831	arg1	ectodomain					781:790	the RPTPmu ectodomain	770:790	the RPTPmu ectodomain	770:790	These data suggest that the RPTPmu ectodomain acts as a distance gauge and plays a key regulatory function, locking the phosphatase to its appropriate functional location.
17761881	5	10	theme	key	829:831	arg1	function					844:851	a key regulatory function	827:851	a key regulatory function	827:851	These data suggest that the RPTPmu ectodomain acts as a distance gauge and plays a key regulatory function, locking the phosphatase to its appropriate functional location.
17761881	4	11	theme	constructs	661:670	arg1	expression					638:647	Cell surface expression	625:647	Cell surface expression of deletion constructs	625:670	Cell surface expression of deletion constructs induces intercellular spacings that correlate with the ectodomain length.
17761881	1	12	theme	Cell-cell	91:99	arg1	contacts					101:108	Cell-cell contacts	91:108	Cell-cell contacts	91:108	Cell-cell contacts are fundamental to multicellular organisms and are subject to exquisite levels of control.
17761881	3	13	theme	crystal	443:449	arg1	structure					451:459	a 3.1 angstrom crystal structure	428:459	a 3.1 angstrom crystal structure of the RPTPmu ectodomain that forms a homophilic trans (antiparallel) dimer with an extended and rigid architecture, matching the dimensions of adherens junctions	428:622	Here we describe a 3.1 angstrom crystal structure of the RPTPmu ectodomain that forms a homophilic trans (antiparallel) dimer with an extended and rigid architecture, matching the dimensions of adherens junctions.
17761881	5	14	theme	regulatory	833:842	arg1	gauge					811:815	a distance gauge	800:815	a distance gauge	800:815	These data suggest that the RPTPmu ectodomain acts as a distance gauge and plays a key regulatory function, locking the phosphatase to its appropriate functional location.
17761881	5	14	theme	regulatory	833:842	arg1	ectodomain					781:790	the RPTPmu ectodomain	770:790	the RPTPmu ectodomain	770:790	These data suggest that the RPTPmu ectodomain acts as a distance gauge and plays a key regulatory function, locking the phosphatase to its appropriate functional location.
17761881	5	14	theme	regulatory	833:842	arg1	function					844:851	a key regulatory function	827:851	a key regulatory function	827:851	These data suggest that the RPTPmu ectodomain acts as a distance gauge and plays a key regulatory function, locking the phosphatase to its appropriate functional location.
17761881	2	15	theme	complexes	400:408	arg1	components					369:378	components	369:378	components of cadherin-catenin complexes	369:408	Human RPTPmu is a type IIB receptor protein tyrosine phosphatase that both forms an adhesive contact itself and is involved in regulating adhesion by dephosphorylating components of cadherin-catenin complexes.
17761881	0	16	theme	tyrosine	15:22	arg1	phosphatase					24:34	tyrosine phosphatase	15:34	a tyrosine phosphatase adhesive interaction	13:55	Structure of a tyrosine phosphatase adhesive interaction reveals a spacer-clamp mechanism.
17761881	3	17	theme	adherens	605:612	arg1	junctions					614:622	adherens junctions	605:622	adherens junctions	605:622	Here we describe a 3.1 angstrom crystal structure of the RPTPmu ectodomain that forms a homophilic trans (antiparallel) dimer with an extended and rigid architecture, matching the dimensions of adherens junctions.
17761881	4	18	theme	deletion	652:659	arg1	constructs					661:670	deletion constructs	652:670	deletion constructs	652:670	Cell surface expression of deletion constructs induces intercellular spacings that correlate with the ectodomain length.
17761881	4	19	theme	ectodomain	727:736	arg1	length					738:743	the ectodomain length	723:743	the ectodomain length	723:743	Cell surface expression of deletion constructs induces intercellular spacings that correlate with the ectodomain length.
17761881	0	20	theme	adhesive	36:43	arg1	interaction					45:55	a tyrosine phosphatase adhesive interaction	13:55	a tyrosine phosphatase adhesive interaction	13:55	Structure of a tyrosine phosphatase adhesive interaction reveals a spacer-clamp mechanism.
17761881	2	21	theme	protein	237:243	arg1	phosphatase					254:264	a type IIB receptor protein tyrosine phosphatase	217:264	a type IIB receptor protein tyrosine phosphatase that both forms an adhesive contact itself and is involved in regulating adhesion by dephosphorylating components of cadherin-catenin complexes	217:408	Human RPTPmu is a type IIB receptor protein tyrosine phosphatase that both forms an adhesive contact itself and is involved in regulating adhesion by dephosphorylating components of cadherin-catenin complexes.
17761881	2	21	theme	protein	237:243	arg1	RPTPmu					207:212	Human RPTPmu	201:212	Human RPTPmu	201:212	Human RPTPmu is a type IIB receptor protein tyrosine phosphatase that both forms an adhesive contact itself and is involved in regulating adhesion by dephosphorylating components of cadherin-catenin complexes.
17761881	3	22	theme	RPTPmu	468:473	arg1	ectodomain					475:484	the RPTPmu ectodomain	464:484	the RPTPmu ectodomain	464:484	Here we describe a 3.1 angstrom crystal structure of the RPTPmu ectodomain that forms a homophilic trans (antiparallel) dimer with an extended and rigid architecture, matching the dimensions of adherens junctions.
17761881	0	23	theme	phosphatase	24:34	arg1	interaction					45:55	a tyrosine phosphatase adhesive interaction	13:55	a tyrosine phosphatase adhesive interaction	13:55	Structure of a tyrosine phosphatase adhesive interaction reveals a spacer-clamp mechanism.
17761881	3	24	theme	angstrom	434:441	arg1	structure					451:459	a 3.1 angstrom crystal structure	428:459	a 3.1 angstrom crystal structure of the RPTPmu ectodomain that forms a homophilic trans (antiparallel) dimer with an extended and rigid architecture, matching the dimensions of adherens junctions	428:622	Here we describe a 3.1 angstrom crystal structure of the RPTPmu ectodomain that forms a homophilic trans (antiparallel) dimer with an extended and rigid architecture, matching the dimensions of adherens junctions.
17761881	2	25	theme	receptor	228:235	arg1	phosphatase					254:264	a type IIB receptor protein tyrosine phosphatase	217:264	a type IIB receptor protein tyrosine phosphatase that both forms an adhesive contact itself and is involved in regulating adhesion by dephosphorylating components of cadherin-catenin complexes	217:408	Human RPTPmu is a type IIB receptor protein tyrosine phosphatase that both forms an adhesive contact itself and is involved in regulating adhesion by dephosphorylating components of cadherin-catenin complexes.
17761881	2	25	theme	receptor	228:235	arg1	RPTPmu					207:212	Human RPTPmu	201:212	Human RPTPmu	201:212	Human RPTPmu is a type IIB receptor protein tyrosine phosphatase that both forms an adhesive contact itself and is involved in regulating adhesion by dephosphorylating components of cadherin-catenin complexes.
17761881	3	26	theme	ectodomain	475:484	arg1	structure					451:459	a 3.1 angstrom crystal structure	428:459	a 3.1 angstrom crystal structure of the RPTPmu ectodomain that forms a homophilic trans (antiparallel) dimer with an extended and rigid architecture, matching the dimensions of adherens junctions	428:622	Here we describe a 3.1 angstrom crystal structure of the RPTPmu ectodomain that forms a homophilic trans (antiparallel) dimer with an extended and rigid architecture, matching the dimensions of adherens junctions.
17761881	5	27	theme	functional	897:906	arg1	location					908:915	its appropriate functional location	881:915	its appropriate functional location	881:915	These data suggest that the RPTPmu ectodomain acts as a distance gauge and plays a key regulatory function, locking the phosphatase to its appropriate functional location.
17761881	2	28	theme	IIB	224:226	arg1	phosphatase					254:264	a type IIB receptor protein tyrosine phosphatase	217:264	a type IIB receptor protein tyrosine phosphatase that both forms an adhesive contact itself and is involved in regulating adhesion by dephosphorylating components of cadherin-catenin complexes	217:408	Human RPTPmu is a type IIB receptor protein tyrosine phosphatase that both forms an adhesive contact itself and is involved in regulating adhesion by dephosphorylating components of cadherin-catenin complexes.
17761881	2	28	theme	IIB	224:226	arg1	RPTPmu					207:212	Human RPTPmu	201:212	Human RPTPmu	201:212	Human RPTPmu is a type IIB receptor protein tyrosine phosphatase that both forms an adhesive contact itself and is involved in regulating adhesion by dephosphorylating components of cadherin-catenin complexes.
17761881	3	29	theme	trans	510:514	arg1	dimer					531:535	a homophilic trans (antiparallel) dimer	497:535	a homophilic trans (antiparallel) dimer with an extended and rigid architecture, matching the dimensions of adherens junctions	497:622	Here we describe a 3.1 angstrom crystal structure of the RPTPmu ectodomain that forms a homophilic trans (antiparallel) dimer with an extended and rigid architecture, matching the dimensions of adherens junctions.
17761881	0	30	theme	interaction	45:55	arg1	Structure					0:8	Structure	0:8	Structure of a tyrosine phosphatase adhesive interaction	0:55	Structure of a tyrosine phosphatase adhesive interaction reveals a spacer-clamp mechanism.
17761881	2	31	theme	type	219:222	arg1	phosphatase					254:264	a type IIB receptor protein tyrosine phosphatase	217:264	a type IIB receptor protein tyrosine phosphatase that both forms an adhesive contact itself and is involved in regulating adhesion by dephosphorylating components of cadherin-catenin complexes	217:408	Human RPTPmu is a type IIB receptor protein tyrosine phosphatase that both forms an adhesive contact itself and is involved in regulating adhesion by dephosphorylating components of cadherin-catenin complexes.
17761881	2	31	theme	type	219:222	arg1	RPTPmu					207:212	Human RPTPmu	201:212	Human RPTPmu	201:212	Human RPTPmu is a type IIB receptor protein tyrosine phosphatase that both forms an adhesive contact itself and is involved in regulating adhesion by dephosphorylating components of cadherin-catenin complexes.
17761881	1	32	theme	multicellular	129:141	arg1	organisms					143:151	multicellular organisms	129:151	multicellular organisms	129:151	Cell-cell contacts are fundamental to multicellular organisms and are subject to exquisite levels of control.
17761881	3	33	theme	junctions	614:622	arg1	dimensions					591:600	the dimensions	587:600	the dimensions of adherens junctions	587:622	Here we describe a 3.1 angstrom crystal structure of the RPTPmu ectodomain that forms a homophilic trans (antiparallel) dimer with an extended and rigid architecture, matching the dimensions of adherens junctions.
17761881	4	34	theme	Cell	625:628	arg1	expression					638:647	Cell surface expression	625:647	Cell surface expression of deletion constructs	625:670	Cell surface expression of deletion constructs induces intercellular spacings that correlate with the ectodomain length.
17761881	3	35	theme	homophilic	499:508	arg1	dimer					531:535	a homophilic trans (antiparallel) dimer	497:535	a homophilic trans (antiparallel) dimer with an extended and rigid architecture, matching the dimensions of adherens junctions	497:622	Here we describe a 3.1 angstrom crystal structure of the RPTPmu ectodomain that forms a homophilic trans (antiparallel) dimer with an extended and rigid architecture, matching the dimensions of adherens junctions.
17761881	0	36	theme	spacer-clamp	67:78	arg1	mechanism					80:88	a spacer-clamp mechanism	65:88	a spacer-clamp mechanism	65:88	Structure of a tyrosine phosphatase adhesive interaction reveals a spacer-clamp mechanism.
17761881	2	37	theme	Human	201:205	arg1	RPTPmu					207:212	Human RPTPmu	201:212	Human RPTPmu	201:212	Human RPTPmu is a type IIB receptor protein tyrosine phosphatase that both forms an adhesive contact itself and is involved in regulating adhesion by dephosphorylating components of cadherin-catenin complexes.
17761881	2	37	theme	Human	201:205	arg1	phosphatase					254:264	a type IIB receptor protein tyrosine phosphatase	217:264	a type IIB receptor protein tyrosine phosphatase that both forms an adhesive contact itself and is involved in regulating adhesion by dephosphorylating components of cadherin-catenin complexes	217:408	Human RPTPmu is a type IIB receptor protein tyrosine phosphatase that both forms an adhesive contact itself and is involved in regulating adhesion by dephosphorylating components of cadherin-catenin complexes.
17761881	2	38	theme	cadherin-catenin	383:398	arg1	complexes					400:408	cadherin-catenin complexes	383:408	cadherin-catenin complexes	383:408	Human RPTPmu is a type IIB receptor protein tyrosine phosphatase that both forms an adhesive contact itself and is involved in regulating adhesion by dephosphorylating components of cadherin-catenin complexes.
17761881	5	39	theme	appropriate	885:895	arg1	location					908:915	its appropriate functional location	881:915	its appropriate functional location	881:915	These data suggest that the RPTPmu ectodomain acts as a distance gauge and plays a key regulatory function, locking the phosphatase to its appropriate functional location.
17761881	2	40	theme	tyrosine	245:252	arg1	phosphatase					254:264	a type IIB receptor protein tyrosine phosphatase	217:264	a type IIB receptor protein tyrosine phosphatase that both forms an adhesive contact itself and is involved in regulating adhesion by dephosphorylating components of cadherin-catenin complexes	217:408	Human RPTPmu is a type IIB receptor protein tyrosine phosphatase that both forms an adhesive contact itself and is involved in regulating adhesion by dephosphorylating components of cadherin-catenin complexes.
17761881	2	40	theme	tyrosine	245:252	arg1	RPTPmu					207:212	Human RPTPmu	201:212	Human RPTPmu	201:212	Human RPTPmu is a type IIB receptor protein tyrosine phosphatase that both forms an adhesive contact itself and is involved in regulating adhesion by dephosphorylating components of cadherin-catenin complexes.
17761881	2	41	dep	forms	276:280	arg1	both					271:274	both	271:274	both	271:274	Human RPTPmu is a type IIB receptor protein tyrosine phosphatase that both forms an adhesive contact itself and is involved in regulating adhesion by dephosphorylating components of cadherin-catenin complexes.
17761881	4	42	theme	surface	630:636	arg1	expression					638:647	Cell surface expression	625:647	Cell surface expression of deletion constructs	625:670	Cell surface expression of deletion constructs induces intercellular spacings that correlate with the ectodomain length.
3521732	7	0	with	precursor	904:912	arg1	peptide					928:934	a signal peptide	919:934	a signal peptide of 19 amino acids	919:952	Analysis of the cDNA indicated that human plasma prekallikrein is synthesized as a precursor with a signal peptide of 19 amino acids.
3521732	13	1	theme	proteases	1716:1724	arg1	family					1699:1704	the trypsin family	1687:1704	the trypsin family of serine proteases	1687:1724	The light chain of plasma kallikrein contains the catalytic portion of the enzyme and is homologous to the trypsin family of serine proteases.
3521732	8	2	theme	protein	978:984	arg1	form					966:969	The mature form	955:969	The mature form of the protein that circulates in blood	955:1009	The mature form of the protein that circulates in blood is a single-chain polypeptide of 619 amino acids.
3521732	8	2	theme	protein	978:984	arg1	polypeptide					1029:1039	a single-chain polypeptide	1014:1039	a single-chain polypeptide of 619 amino acids	1014:1058	The mature form of the protein that circulates in blood is a single-chain polypeptide of 619 amino acids.
3521732	9	3	theme	bond	1170:1173	arg1	cleavage					1138:1145	the cleavage	1134:1145	the cleavage of an internal Arg-Ile bond	1134:1173	Plasma prekallikrein is converted to plasma kallikrein by factor XIIa by the cleavage of an internal Arg-Ile bond.
3521732	10	4	theme	disulfide	1320:1328	arg1	bond					1330:1333	a disulfide bond	1318:1333	a disulfide bond	1318:1333	Plasma kallikrein is composed of a heavy chain (371 amino acids) and a light chain (248 amino acids), and these 2 chains are held together by a disulfide bond.
3521732	11	5	theme	kallikrein	1362:1371	arg1	chain					1346:1350	The heavy chain	1336:1350	The heavy chain of plasma kallikrein	1336:1371	The heavy chain of plasma kallikrein originates from the amino-terminal end of the zymogen and is composed of 4 tandem repeats that are 90 or 91 amino acid residues in length.
3521732	11	6	theme	heavy	1340:1344	arg1	chain					1346:1350	The heavy chain	1336:1350	The heavy chain of plasma kallikrein	1336:1371	The heavy chain of plasma kallikrein originates from the amino-terminal end of the zymogen and is composed of 4 tandem repeats that are 90 or 91 amino acid residues in length.
3521732	10	7	theme	heavy	1211:1215	arg1	chain					1217:1221	a heavy chain	1209:1221	a heavy chain (371 amino acids)	1209:1239	Plasma kallikrein is composed of a heavy chain (371 amino acids) and a light chain (248 amino acids), and these 2 chains are held together by a disulfide bond.
3521732	10	7	theme	heavy	1211:1215	arg1	acids					1234:1238	371 amino acids	1224:1238	371 amino acids	1224:1238	Plasma kallikrein is composed of a heavy chain (371 amino acids) and a light chain (248 amino acids), and these 2 chains are held together by a disulfide bond.
3521732	11	8	theme	amino	1481:1485	arg1	residues					1492:1499	90 or 91 amino acid residues	1472:1499	90 or 91 amino acid residues in length	1472:1509	The heavy chain of plasma kallikrein originates from the amino-terminal end of the zymogen and is composed of 4 tandem repeats that are 90 or 91 amino acid residues in length.
3521732	11	8	theme	amino	1481:1485	arg1	repeats					1455:1461	4 tandem repeats	1446:1461	4 tandem repeats that are 90 or 91 amino acid residues in length	1446:1509	The heavy chain of plasma kallikrein originates from the amino-terminal end of the zymogen and is composed of 4 tandem repeats that are 90 or 91 amino acid residues in length.
3521732	13	9	theme	enzyme	1659:1664	arg1	portion					1644:1650	the catalytic portion	1630:1650	the catalytic portion of the enzyme	1630:1664	The light chain of plasma kallikrein contains the catalytic portion of the enzyme and is homologous to the trypsin family of serine proteases.
3521732	7	10	theme	human	857:861	arg1	precursor					904:912	a precursor	902:912	a precursor with a signal peptide of 19 amino acids	902:952	Analysis of the cDNA indicated that human plasma prekallikrein is synthesized as a precursor with a signal peptide of 19 amino acids.
3521732	7	10	theme	human	857:861	arg1	prekallikrein					870:882	human plasma prekallikrein	857:882	human plasma prekallikrein	857:882	Analysis of the cDNA indicated that human plasma prekallikrein is synthesized as a precursor with a signal peptide of 19 amino acids.
3521732	4	11	link	asparagine-linked	526:542	arg1	sites					568:572	Five asparagine-linked carbohydrate attachment sites	521:572	Five asparagine-linked carbohydrate attachment sites	521:572	Five asparagine-linked carbohydrate attachment sites were identified.
3521732	5	12	attach	isolated	698:705	arg1	library					737:743	a lambda gt11 expression library	712:743	a lambda gt11 expression library	712:743	The sequence determined by Edman degradation was aligned with the amino acid sequence predicted from cDNAs isolated from a lambda gt11 expression library.
3521732	5	12	attach	isolated	698:705	arg2	cDNAs					692:696	cDNAs	692:696	cDNAs isolated from a lambda gt11 expression library	692:743	The sequence determined by Edman degradation was aligned with the amino acid sequence predicted from cDNAs isolated from a lambda gt11 expression library.
3521732	9	13	theme	plasma	1098:1103	arg1	kallikrein					1105:1114	plasma kallikrein	1098:1114	plasma kallikrein	1098:1114	Plasma prekallikrein is converted to plasma kallikrein by factor XIIa by the cleavage of an internal Arg-Ile bond.
3521732	1	14	theme	Edman	193:197	arg1	degradation					199:209	automated Edman degradation	183:209	automated Edman degradation	183:209	The amino acid sequence of human plasma prekallikrein was determined by a combination of automated Edman degradation and cDNA sequencing techniques.
3521732	3	15	contain	containing	468:477	arg2	carbohydrate					479:490	carbohydrate	479:490	carbohydrate	479:490	Cyanogen bromide peptides containing carbohydrate were further digested with trypsin, and the peptides containing carbohydrate were isolated and sequenced.
3521732	3	15	contain	containing	468:477	arg1	peptides					459:466	the peptides	455:466	the peptides containing carbohydrate	455:490	Cyanogen bromide peptides containing carbohydrate were further digested with trypsin, and the peptides containing carbohydrate were isolated and sequenced.
3521732	13	16	contain	contains	1621:1628	arg1	homologous					1673:1682	homologous	1673:1682	homologous	1673:1682	The light chain of plasma kallikrein contains the catalytic portion of the enzyme and is homologous to the trypsin family of serine proteases.
3521732	13	16	contain	contains	1621:1628	arg1	chain					1594:1598	The light chain	1584:1598	The light chain of plasma kallikrein	1584:1619	The light chain of plasma kallikrein contains the catalytic portion of the enzyme and is homologous to the trypsin family of serine proteases.
3521732	13	16	contain	contains	1621:1628	arg2	portion					1644:1650	the catalytic portion	1630:1650	the catalytic portion of the enzyme	1630:1664	The light chain of plasma kallikrein contains the catalytic portion of the enzyme and is homologous to the trypsin family of serine proteases.
3521732	5	17	theme	gt11	721:724	arg1	library					737:743	a lambda gt11 expression library	712:743	a lambda gt11 expression library	712:743	The sequence determined by Edman degradation was aligned with the amino acid sequence predicted from cDNAs isolated from a lambda gt11 expression library.
3521732	1	18	theme	amino	98:102	arg1	sequence					109:116	The amino acid sequence	94:116	The amino acid sequence of human plasma prekallikrein	94:146	The amino acid sequence of human plasma prekallikrein was determined by a combination of automated Edman degradation and cDNA sequencing techniques.
3521732	2	19	theme	Human	243:247	arg1	prekallikrein					256:268	Human plasma prekallikrein	243:268	Human plasma prekallikrein	243:268	Human plasma prekallikrein was fragmented with cyanogen bromide, and 13 homogeneous peptides were isolated and sequenced.
3521732	11	20	theme	zymogen	1419:1425	arg1	end					1408:1410	the amino-terminal end	1389:1410	the amino-terminal end of the zymogen	1389:1425	The heavy chain of plasma kallikrein originates from the amino-terminal end of the zymogen and is composed of 4 tandem repeats that are 90 or 91 amino acid residues in length.
3521732	0	21	theme	serine	43:48	arg1	protease					50:57	a serine protease	41:57	a serine protease that contains four tandem repeats	41:91	Human plasma prekallikrein, a zymogen to a serine protease that contains four tandem repeats.
3521732	1	22	theme	human	121:125	arg1	prekallikrein					134:146	human plasma prekallikrein	121:146	human plasma prekallikrein	121:146	The amino acid sequence of human plasma prekallikrein was determined by a combination of automated Edman degradation and cDNA sequencing techniques.
3521732	2	23	with	fragmented	274:283	arg1	bromide					299:305	cyanogen bromide	290:305	cyanogen bromide	290:305	Human plasma prekallikrein was fragmented with cyanogen bromide, and 13 homogeneous peptides were isolated and sequenced.
3521732	11	24	theme	tandem	1448:1453	arg1	repeats					1455:1461	4 tandem repeats	1446:1461	4 tandem repeats that are 90 or 91 amino acid residues in length	1446:1509	The heavy chain of plasma kallikrein originates from the amino-terminal end of the zymogen and is composed of 4 tandem repeats that are 90 or 91 amino acid residues in length.
3521732	11	24	theme	tandem	1448:1453	arg1	residues					1492:1499	90 or 91 amino acid residues	1472:1499	90 or 91 amino acid residues in length	1472:1509	The heavy chain of plasma kallikrein originates from the amino-terminal end of the zymogen and is composed of 4 tandem repeats that are 90 or 91 amino acid residues in length.
3521732	1	25	theme	prekallikrein	134:146	arg1	sequence					109:116	The amino acid sequence	94:116	The amino acid sequence of human plasma prekallikrein	94:146	The amino acid sequence of human plasma prekallikrein was determined by a combination of automated Edman degradation and cDNA sequencing techniques.
3521732	4	26	theme	asparagine-linked	526:542	arg1	sites					568:572	Five asparagine-linked carbohydrate attachment sites	521:572	Five asparagine-linked carbohydrate attachment sites	521:572	Five asparagine-linked carbohydrate attachment sites were identified.
3521732	13	27	theme	kallikrein	1610:1619	arg1	homologous					1673:1682	homologous	1673:1682	homologous	1673:1682	The light chain of plasma kallikrein contains the catalytic portion of the enzyme and is homologous to the trypsin family of serine proteases.
3521732	13	27	theme	kallikrein	1610:1619	arg1	chain					1594:1598	The light chain	1584:1598	The light chain of plasma kallikrein	1584:1619	The light chain of plasma kallikrein contains the catalytic portion of the enzyme and is homologous to the trypsin family of serine proteases.
3521732	12	28	theme	human	1567:1571	arg1	XI					1580:1581	human factor XI	1567:1581	human factor XI	1567:1581	These repeat sequences are also homologous to those in human factor XI.
3521732	8	29	theme	acids	1054:1058	arg1	form					966:969	The mature form	955:969	The mature form of the protein that circulates in blood	955:1009	The mature form of the protein that circulates in blood is a single-chain polypeptide of 619 amino acids.
3521732	8	29	theme	acids	1054:1058	arg1	polypeptide					1029:1039	a single-chain polypeptide	1014:1039	a single-chain polypeptide of 619 amino acids	1014:1058	The mature form of the protein that circulates in blood is a single-chain polypeptide of 619 amino acids.
3521732	13	30	theme	light	1588:1592	arg1	homologous					1673:1682	homologous	1673:1682	homologous	1673:1682	The light chain of plasma kallikrein contains the catalytic portion of the enzyme and is homologous to the trypsin family of serine proteases.
3521732	13	30	theme	light	1588:1592	arg1	chain					1594:1598	The light chain	1584:1598	The light chain of plasma kallikrein	1584:1619	The light chain of plasma kallikrein contains the catalytic portion of the enzyme and is homologous to the trypsin family of serine proteases.
3521732	10	31	theme	light	1247:1251	arg1	acids					1270:1274	248 amino acids	1260:1274	248 amino acids	1260:1274	Plasma kallikrein is composed of a heavy chain (371 amino acids) and a light chain (248 amino acids), and these 2 chains are held together by a disulfide bond.
3521732	10	31	theme	light	1247:1251	arg1	chain					1253:1257	a light chain	1245:1257	a light chain (248 amino acids)	1245:1275	Plasma kallikrein is composed of a heavy chain (371 amino acids) and a light chain (248 amino acids), and these 2 chains are held together by a disulfide bond.
3521732	0	32	theme	Human	0:4	arg1	prekallikrein					13:25	Human plasma prekallikrein	0:25	Human plasma prekallikrein	0:25	Human plasma prekallikrein, a zymogen to a serine protease that contains four tandem repeats.
3521732	0	32	theme	Human	0:4	arg1	zymogen					30:36	a zymogen	28:36	a zymogen to a serine protease that contains four tandem repeats	28:91	Human plasma prekallikrein, a zymogen to a serine protease that contains four tandem repeats.
3521732	7	33	theme	amino	942:946	arg1	acids					948:952	19 amino acids	939:952	19 amino acids	939:952	Analysis of the cDNA indicated that human plasma prekallikrein is synthesized as a precursor with a signal peptide of 19 amino acids.
3521732	3	34	theme	Cyanogen	365:372	arg1	peptides					382:389	Cyanogen bromide peptides	365:389	Cyanogen bromide peptides containing carbohydrate	365:413	Cyanogen bromide peptides containing carbohydrate were further digested with trypsin, and the peptides containing carbohydrate were isolated and sequenced.
3521732	11	35	theme	amino-terminal	1393:1406	arg1	end					1408:1410	the amino-terminal end	1389:1410	the amino-terminal end of the zymogen	1389:1425	The heavy chain of plasma kallikrein originates from the amino-terminal end of the zymogen and is composed of 4 tandem repeats that are 90 or 91 amino acid residues in length.
3521732	10	36	theme	amino	1264:1268	arg1	acids					1270:1274	248 amino acids	1260:1274	248 amino acids	1260:1274	Plasma kallikrein is composed of a heavy chain (371 amino acids) and a light chain (248 amino acids), and these 2 chains are held together by a disulfide bond.
3521732	10	36	theme	amino	1264:1268	arg1	chain					1253:1257	a light chain	1245:1257	a light chain (248 amino acids)	1245:1275	Plasma kallikrein is composed of a heavy chain (371 amino acids) and a light chain (248 amino acids), and these 2 chains are held together by a disulfide bond.
3521732	13	37	theme	trypsin	1691:1697	arg1	family					1699:1704	the trypsin family	1687:1704	the trypsin family of serine proteases	1687:1724	The light chain of plasma kallikrein contains the catalytic portion of the enzyme and is homologous to the trypsin family of serine proteases.
3521732	4	38	theme	attachment	557:566	arg1	sites					568:572	Five asparagine-linked carbohydrate attachment sites	521:572	Five asparagine-linked carbohydrate attachment sites	521:572	Five asparagine-linked carbohydrate attachment sites were identified.
3521732	6	39	theme	poly	808:811	arg1	RNA					816:818	human liver poly(A) RNA	796:818	human liver poly(A) RNA	796:818	This library contained cDNA inserts prepared from human liver poly(A) RNA.
3521732	6	40	theme	human	796:800	arg1	A					813:813	A	813:813	A	813:813	This library contained cDNA inserts prepared from human liver poly(A) RNA.
3521732	6	40	theme	human	796:800	arg1	poly					808:811	human liver poly	796:811	human liver poly(A) RNA	796:818	This library contained cDNA inserts prepared from human liver poly(A) RNA.
3521732	2	41	theme	homogeneous	315:325	arg1	peptides					327:334	13 homogeneous peptides	312:334	13 homogeneous peptides	312:334	Human plasma prekallikrein was fragmented with cyanogen bromide, and 13 homogeneous peptides were isolated and sequenced.
3521732	1	42	theme	degradation	199:209	arg1	combination					168:178	a combination	166:178	a combination of automated Edman degradation and cDNA sequencing techniques	166:240	The amino acid sequence of human plasma prekallikrein was determined by a combination of automated Edman degradation and cDNA sequencing techniques.
3521732	9	43	theme	internal	1153:1160	arg1	bond					1170:1173	an internal Arg-Ile bond	1150:1173	an internal Arg-Ile bond	1150:1173	Plasma prekallikrein is converted to plasma kallikrein by factor XIIa by the cleavage of an internal Arg-Ile bond.
3521732	10	44	theme	Plasma	1176:1181	arg1	kallikrein					1183:1192	Plasma kallikrein	1176:1192	Plasma kallikrein	1176:1192	Plasma kallikrein is composed of a heavy chain (371 amino acids) and a light chain (248 amino acids), and these 2 chains are held together by a disulfide bond.
3521732	13	45	theme	serine	1709:1714	arg1	proteases					1716:1724	serine proteases	1709:1724	serine proteases	1709:1724	The light chain of plasma kallikrein contains the catalytic portion of the enzyme and is homologous to the trypsin family of serine proteases.
3521732	6	46	theme	cDNA	769:772	arg1	inserts					774:780	cDNA inserts	769:780	cDNA inserts prepared from human liver poly(A) RNA	769:818	This library contained cDNA inserts prepared from human liver poly(A) RNA.
3521732	1	47	theme	techniques	231:240	arg1	combination					168:178	a combination	166:178	a combination of automated Edman degradation and cDNA sequencing techniques	166:240	The amino acid sequence of human plasma prekallikrein was determined by a combination of automated Edman degradation and cDNA sequencing techniques.
3521732	6	48	contain	contained	759:767	arg1	library					751:757	This library	746:757	This library	746:757	This library contained cDNA inserts prepared from human liver poly(A) RNA.
3521732	6	48	contain	contained	759:767	arg2	inserts					774:780	cDNA inserts	769:780	cDNA inserts prepared from human liver poly(A) RNA	769:818	This library contained cDNA inserts prepared from human liver poly(A) RNA.
3521732	5	49	theme	acid	663:666	arg1	sequence					668:675	the amino acid sequence	653:675	the amino acid sequence predicted from cDNAs isolated from a lambda gt11 expression library	653:743	The sequence determined by Edman degradation was aligned with the amino acid sequence predicted from cDNAs isolated from a lambda gt11 expression library.
3521732	11	50	theme	acid	1487:1490	arg1	residues					1492:1499	90 or 91 amino acid residues	1472:1499	90 or 91 amino acid residues in length	1472:1509	The heavy chain of plasma kallikrein originates from the amino-terminal end of the zymogen and is composed of 4 tandem repeats that are 90 or 91 amino acid residues in length.
3521732	11	50	theme	acid	1487:1490	arg1	repeats					1455:1461	4 tandem repeats	1446:1461	4 tandem repeats that are 90 or 91 amino acid residues in length	1446:1509	The heavy chain of plasma kallikrein originates from the amino-terminal end of the zymogen and is composed of 4 tandem repeats that are 90 or 91 amino acid residues in length.
3521732	12	51	theme	repeat	1518:1523	arg1	sequences					1525:1533	These repeat sequences	1512:1533	These repeat sequences	1512:1533	These repeat sequences are also homologous to those in human factor XI.
3521732	3	52	contain	containing	391:400	arg1	peptides					382:389	Cyanogen bromide peptides	365:389	Cyanogen bromide peptides containing carbohydrate	365:413	Cyanogen bromide peptides containing carbohydrate were further digested with trypsin, and the peptides containing carbohydrate were isolated and sequenced.
3521732	3	52	contain	containing	391:400	arg2	carbohydrate					402:413	carbohydrate	402:413	carbohydrate	402:413	Cyanogen bromide peptides containing carbohydrate were further digested with trypsin, and the peptides containing carbohydrate were isolated and sequenced.
3521732	8	53	theme	single-chain	1016:1027	arg1	form					966:969	The mature form	955:969	The mature form of the protein that circulates in blood	955:1009	The mature form of the protein that circulates in blood is a single-chain polypeptide of 619 amino acids.
3521732	8	53	theme	single-chain	1016:1027	arg1	polypeptide					1029:1039	a single-chain polypeptide	1014:1039	a single-chain polypeptide of 619 amino acids	1014:1058	The mature form of the protein that circulates in blood is a single-chain polypeptide of 619 amino acids.
3521732	7	54	theme	plasma	863:868	arg1	precursor					904:912	a precursor	902:912	a precursor with a signal peptide of 19 amino acids	902:952	Analysis of the cDNA indicated that human plasma prekallikrein is synthesized as a precursor with a signal peptide of 19 amino acids.
3521732	7	54	theme	plasma	863:868	arg1	prekallikrein					870:882	human plasma prekallikrein	857:882	human plasma prekallikrein	857:882	Analysis of the cDNA indicated that human plasma prekallikrein is synthesized as a precursor with a signal peptide of 19 amino acids.
3521732	11	55	from	residues	1492:1499	arg1	length					1504:1509	length	1504:1509	length	1504:1509	The heavy chain of plasma kallikrein originates from the amino-terminal end of the zymogen and is composed of 4 tandem repeats that are 90 or 91 amino acid residues in length.
3521732	1	56	theme	automated	183:191	arg1	degradation					199:209	automated Edman degradation	183:209	automated Edman degradation	183:209	The amino acid sequence of human plasma prekallikrein was determined by a combination of automated Edman degradation and cDNA sequencing techniques.
3521732	5	57	theme	lambda	714:719	arg1	library					737:743	a lambda gt11 expression library	712:743	a lambda gt11 expression library	712:743	The sequence determined by Edman degradation was aligned with the amino acid sequence predicted from cDNAs isolated from a lambda gt11 expression library.
3521732	0	58	contain	contains	64:71	arg2	repeats					85:91	four tandem repeats	73:91	four tandem repeats	73:91	Human plasma prekallikrein, a zymogen to a serine protease that contains four tandem repeats.
3521732	0	58	contain	contains	64:71	arg1	protease					50:57	a serine protease	41:57	a serine protease that contains four tandem repeats	41:91	Human plasma prekallikrein, a zymogen to a serine protease that contains four tandem repeats.
3521732	10	59	theme	amino	1228:1232	arg1	chain					1217:1221	a heavy chain	1209:1221	a heavy chain (371 amino acids)	1209:1239	Plasma kallikrein is composed of a heavy chain (371 amino acids) and a light chain (248 amino acids), and these 2 chains are held together by a disulfide bond.
3521732	10	59	theme	amino	1228:1232	arg1	acids					1234:1238	371 amino acids	1224:1238	371 amino acids	1224:1238	Plasma kallikrein is composed of a heavy chain (371 amino acids) and a light chain (248 amino acids), and these 2 chains are held together by a disulfide bond.
3521732	5	60	theme	expression	726:735	arg1	library					737:743	a lambda gt11 expression library	712:743	a lambda gt11 expression library	712:743	The sequence determined by Edman degradation was aligned with the amino acid sequence predicted from cDNAs isolated from a lambda gt11 expression library.
3521732	2	61	theme	plasma	249:254	arg1	prekallikrein					256:268	Human plasma prekallikrein	243:268	Human plasma prekallikrein	243:268	Human plasma prekallikrein was fragmented with cyanogen bromide, and 13 homogeneous peptides were isolated and sequenced.
3521732	1	62	theme	acid	104:107	arg1	sequence					109:116	The amino acid sequence	94:116	The amino acid sequence of human plasma prekallikrein	94:146	The amino acid sequence of human plasma prekallikrein was determined by a combination of automated Edman degradation and cDNA sequencing techniques.
3521732	1	63	theme	plasma	127:132	arg1	prekallikrein					134:146	human plasma prekallikrein	121:146	human plasma prekallikrein	121:146	The amino acid sequence of human plasma prekallikrein was determined by a combination of automated Edman degradation and cDNA sequencing techniques.
3521732	4	64	theme	carbohydrate	544:555	arg1	sites					568:572	Five asparagine-linked carbohydrate attachment sites	521:572	Five asparagine-linked carbohydrate attachment sites	521:572	Five asparagine-linked carbohydrate attachment sites were identified.
3521732	13	65	theme	plasma	1603:1608	arg1	kallikrein					1610:1619	plasma kallikrein	1603:1619	plasma kallikrein	1603:1619	The light chain of plasma kallikrein contains the catalytic portion of the enzyme and is homologous to the trypsin family of serine proteases.
3521732	9	66	theme	Plasma	1061:1066	arg1	prekallikrein					1068:1080	Plasma prekallikrein	1061:1080	Plasma prekallikrein	1061:1080	Plasma prekallikrein is converted to plasma kallikrein by factor XIIa by the cleavage of an internal Arg-Ile bond.
3521732	0	67	theme	tandem	78:83	arg1	repeats					85:91	four tandem repeats	73:91	four tandem repeats	73:91	Human plasma prekallikrein, a zymogen to a serine protease that contains four tandem repeats.
3521732	8	68	theme	amino	1048:1052	arg1	acids					1054:1058	619 amino acids	1044:1058	619 amino acids	1044:1058	The mature form of the protein that circulates in blood is a single-chain polypeptide of 619 amino acids.
3521732	10	69	theme	248	1260:1262	arg1	acids					1270:1274	248 amino acids	1260:1274	248 amino acids	1260:1274	Plasma kallikrein is composed of a heavy chain (371 amino acids) and a light chain (248 amino acids), and these 2 chains are held together by a disulfide bond.
3521732	10	69	theme	248	1260:1262	arg1	chain					1253:1257	a light chain	1245:1257	a light chain (248 amino acids)	1245:1275	Plasma kallikrein is composed of a heavy chain (371 amino acids) and a light chain (248 amino acids), and these 2 chains are held together by a disulfide bond.
3521732	5	70	theme	amino	657:661	arg1	sequence					668:675	the amino acid sequence	653:675	the amino acid sequence predicted from cDNAs isolated from a lambda gt11 expression library	653:743	The sequence determined by Edman degradation was aligned with the amino acid sequence predicted from cDNAs isolated from a lambda gt11 expression library.
3521732	11	71	theme	plasma	1355:1360	arg1	kallikrein					1362:1371	plasma kallikrein	1355:1371	plasma kallikrein	1355:1371	The heavy chain of plasma kallikrein originates from the amino-terminal end of the zymogen and is composed of 4 tandem repeats that are 90 or 91 amino acid residues in length.
3521732	0	72	theme	plasma	6:11	arg1	prekallikrein					13:25	Human plasma prekallikrein	0:25	Human plasma prekallikrein	0:25	Human plasma prekallikrein, a zymogen to a serine protease that contains four tandem repeats.
3521732	0	72	theme	plasma	6:11	arg1	zymogen					30:36	a zymogen	28:36	a zymogen to a serine protease that contains four tandem repeats	28:91	Human plasma prekallikrein, a zymogen to a serine protease that contains four tandem repeats.
3521732	5	73	theme	Edman	618:622	arg1	degradation					624:634	Edman degradation	618:634	Edman degradation	618:634	The sequence determined by Edman degradation was aligned with the amino acid sequence predicted from cDNAs isolated from a lambda gt11 expression library.
3521732	12	74	theme	factor	1573:1578	arg1	XI					1580:1581	human factor XI	1567:1581	human factor XI	1567:1581	These repeat sequences are also homologous to those in human factor XI.
3521732	7	75	theme	cDNA	837:840	arg1	Analysis					821:828	Analysis	821:828	Analysis of the cDNA	821:840	Analysis of the cDNA indicated that human plasma prekallikrein is synthesized as a precursor with a signal peptide of 19 amino acids.
3521732	7	76	theme	acids	948:952	arg1	peptide					928:934	a signal peptide	919:934	a signal peptide of 19 amino acids	919:952	Analysis of the cDNA indicated that human plasma prekallikrein is synthesized as a precursor with a signal peptide of 19 amino acids.
3521732	3	77	theme	bromide	374:380	arg1	peptides					382:389	Cyanogen bromide peptides	365:389	Cyanogen bromide peptides containing carbohydrate	365:413	Cyanogen bromide peptides containing carbohydrate were further digested with trypsin, and the peptides containing carbohydrate were isolated and sequenced.
3521732	9	78	theme	factor	1119:1124	arg1	XIIa					1126:1129	factor XIIa	1119:1129	factor XIIa	1119:1129	Plasma prekallikrein is converted to plasma kallikrein by factor XIIa by the cleavage of an internal Arg-Ile bond.
3521732	13	79	theme	catalytic	1634:1642	arg1	portion					1644:1650	the catalytic portion	1630:1650	the catalytic portion of the enzyme	1630:1664	The light chain of plasma kallikrein contains the catalytic portion of the enzyme and is homologous to the trypsin family of serine proteases.
3521732	1	80	theme	cDNA	215:218	arg1	techniques					231:240	cDNA sequencing techniques	215:240	cDNA sequencing techniques	215:240	The amino acid sequence of human plasma prekallikrein was determined by a combination of automated Edman degradation and cDNA sequencing techniques.
3521732	6	81	theme	liver	802:806	arg1	A					813:813	A	813:813	A	813:813	This library contained cDNA inserts prepared from human liver poly(A) RNA.
3521732	6	81	theme	liver	802:806	arg1	poly					808:811	human liver poly	796:811	human liver poly(A) RNA	796:818	This library contained cDNA inserts prepared from human liver poly(A) RNA.
3521732	7	82	theme	signal	921:926	arg1	peptide					928:934	a signal peptide	919:934	a signal peptide of 19 amino acids	919:952	Analysis of the cDNA indicated that human plasma prekallikrein is synthesized as a precursor with a signal peptide of 19 amino acids.
3521732	8	83	theme	mature	959:964	arg1	form					966:969	The mature form	955:969	The mature form of the protein that circulates in blood	955:1009	The mature form of the protein that circulates in blood is a single-chain polypeptide of 619 amino acids.
3521732	8	83	theme	mature	959:964	arg1	polypeptide					1029:1039	a single-chain polypeptide	1014:1039	a single-chain polypeptide of 619 amino acids	1014:1058	The mature form of the protein that circulates in blood is a single-chain polypeptide of 619 amino acids.
3521732	9	84	theme	Arg-Ile	1162:1168	arg1	bond					1170:1173	an internal Arg-Ile bond	1150:1173	an internal Arg-Ile bond	1150:1173	Plasma prekallikrein is converted to plasma kallikrein by factor XIIa by the cleavage of an internal Arg-Ile bond.
3521732	1	85	theme	sequencing	220:229	arg1	techniques					231:240	cDNA sequencing techniques	215:240	cDNA sequencing techniques	215:240	The amino acid sequence of human plasma prekallikrein was determined by a combination of automated Edman degradation and cDNA sequencing techniques.
7460900	1	0	from	case	293:296	arg1	chain					260:264	the peptide chain	248:264	the peptide chain instead of only one in the case of cow and sheep kappa-caseinoglycopeptides	248:340	The study of glycopeptides obtained after enzymic digestions of human caseinoglycopeptide demonstrated the presence of several (up to 10) prosthetic sugar groups distributed throughout the peptide chain instead of only one in the case of cow and sheep kappa-caseinoglycopeptides.
7460900	3	1	theme	secondary	498:506	arg1	structure					508:516	The predicted secondary structure	484:516	The predicted secondary structure	484:516	The predicted secondary structure was in accordance with the high number of sugar groups situated all but one in beta-turns.
7460900	1	2	theme	sheep	309:313	arg1	kappa-caseinoglycopeptides					315:340	cow and sheep kappa-caseinoglycopeptides	301:340	cow and sheep kappa-caseinoglycopeptides	301:340	The study of glycopeptides obtained after enzymic digestions of human caseinoglycopeptide demonstrated the presence of several (up to 10) prosthetic sugar groups distributed throughout the peptide chain instead of only one in the case of cow and sheep kappa-caseinoglycopeptides.
7460900	4	3	theme	human	679:683	arg1	caseinoglycopeptide					685:703	human caseinoglycopeptide	679:703	human caseinoglycopeptide	679:703	A significant microheterogeneity seems to occur at the sugar level of human caseinoglycopeptide, which might thus present differences from one milk to another.
7460900	1	4	theme	kappa-caseinoglycopeptides	315:340	arg1	case					293:296	the case	289:296	the case of cow and sheep kappa-caseinoglycopeptides	289:340	The study of glycopeptides obtained after enzymic digestions of human caseinoglycopeptide demonstrated the presence of several (up to 10) prosthetic sugar groups distributed throughout the peptide chain instead of only one in the case of cow and sheep kappa-caseinoglycopeptides.
7460900	1	5	theme	peptide	252:258	arg1	chain					260:264	the peptide chain	248:264	the peptide chain instead of only one in the case of cow and sheep kappa-caseinoglycopeptides	248:340	The study of glycopeptides obtained after enzymic digestions of human caseinoglycopeptide demonstrated the presence of several (up to 10) prosthetic sugar groups distributed throughout the peptide chain instead of only one in the case of cow and sheep kappa-caseinoglycopeptides.
7460900	3	6	theme	high	545:548	arg1	number					550:555	the high number	541:555	the high number of sugar groups situated all but one in beta-turns	541:606	The predicted secondary structure was in accordance with the high number of sugar groups situated all but one in beta-turns.
7460900	4	7	theme	significant	611:621	arg1	microheterogeneity					623:640	A significant microheterogeneity	609:640	A significant microheterogeneity	609:640	A significant microheterogeneity seems to occur at the sugar level of human caseinoglycopeptide, which might thus present differences from one milk to another.
7460900	3	8	from	beta-turns	597:606	arg1	situated					573:580	situated	573:580	situated	573:580	The predicted secondary structure was in accordance with the high number of sugar groups situated all but one in beta-turns.
7460900	3	9	dep	situated	573:580	arg1	one					590:592	one	590:592	one	590:592	The predicted secondary structure was in accordance with the high number of sugar groups situated all but one in beta-turns.
7460900	3	9	dep	situated	573:580	arg1	all					582:584	all	582:584	all	582:584	The predicted secondary structure was in accordance with the high number of sugar groups situated all but one in beta-turns.
7460900	1	10	gly	glycopeptides	76:88	arg2	glycopeptides					76:88	glycopeptides	76:88	glycopeptides obtained after enzymic digestions of human caseinoglycopeptide	76:151	The study of glycopeptides obtained after enzymic digestions of human caseinoglycopeptide demonstrated the presence of several (up to 10) prosthetic sugar groups distributed throughout the peptide chain instead of only one in the case of cow and sheep kappa-caseinoglycopeptides.
7460900	1	11	from	one	282:284	arg1	case					293:296	the case	289:296	the case of cow and sheep kappa-caseinoglycopeptides	289:340	The study of glycopeptides obtained after enzymic digestions of human caseinoglycopeptide demonstrated the presence of several (up to 10) prosthetic sugar groups distributed throughout the peptide chain instead of only one in the case of cow and sheep kappa-caseinoglycopeptides.
7460900	4	12	theme	caseinoglycopeptide	685:703	arg1	level					670:674	the sugar level	660:674	the sugar level of human caseinoglycopeptide	660:703	A significant microheterogeneity seems to occur at the sugar level of human caseinoglycopeptide, which might thus present differences from one milk to another.
7460900	1	13	gly	kappa-caseinoglycopeptides	315:340	arg2	kappa-caseinoglycopeptides					315:340	cow and sheep kappa-caseinoglycopeptides	301:340	cow and sheep kappa-caseinoglycopeptides	301:340	The study of glycopeptides obtained after enzymic digestions of human caseinoglycopeptide demonstrated the presence of several (up to 10) prosthetic sugar groups distributed throughout the peptide chain instead of only one in the case of cow and sheep kappa-caseinoglycopeptides.
7460900	2	14	gly	glycopeptides	354:366	arg2	glycopeptides					354:366	the glycopeptides	350:366	the glycopeptides	350:366	One of the glycopeptides allowed us to complete the C-terminal sequence of human caseinoglycopeptide previously published in part by others.
7460900	3	15	theme	sugar	560:564	arg1	groups					566:571	sugar groups	560:571	sugar groups situated all but one in beta-turns	560:606	The predicted secondary structure was in accordance with the high number of sugar groups situated all but one in beta-turns.
7460900	1	16	theme	several	182:188	arg1	groups					218:223	several (up to 10) prosthetic sugar groups	182:223	several (up to 10) prosthetic sugar groups distributed throughout the peptide chain instead of only one in the case of cow and sheep kappa-caseinoglycopeptides	182:340	The study of glycopeptides obtained after enzymic digestions of human caseinoglycopeptide demonstrated the presence of several (up to 10) prosthetic sugar groups distributed throughout the peptide chain instead of only one in the case of cow and sheep kappa-caseinoglycopeptides.
7460900	2	17	theme	caseinoglycopeptide	424:442	arg1	sequence					406:413	the C-terminal sequence	391:413	the C-terminal sequence of human caseinoglycopeptide previously published in part by others	391:481	One of the glycopeptides allowed us to complete the C-terminal sequence of human caseinoglycopeptide previously published in part by others.
7460900	3	18	theme	groups	566:571	arg1	number					550:555	the high number	541:555	the high number of sugar groups situated all but one in beta-turns	541:606	The predicted secondary structure was in accordance with the high number of sugar groups situated all but one in beta-turns.
7460900	3	19	from	situated	573:580	arg1	beta-turns					597:606	beta-turns	597:606	beta-turns	597:606	The predicted secondary structure was in accordance with the high number of sugar groups situated all but one in beta-turns.
7460900	2	20	theme	glycopeptides	354:366	arg1	One					343:345	One	343:345	One	343:345	One of the glycopeptides allowed us to complete the C-terminal sequence of human caseinoglycopeptide previously published in part by others.
7460900	2	20	theme	glycopeptides	354:366	arg1	glycopeptides					354:366	the glycopeptides	350:366	the glycopeptides	350:366	One of the glycopeptides allowed us to complete the C-terminal sequence of human caseinoglycopeptide previously published in part by others.
7460900	2	21	theme	human	418:422	arg1	caseinoglycopeptide					424:442	human caseinoglycopeptide	418:442	human caseinoglycopeptide previously published in part by others	418:481	One of the glycopeptides allowed us to complete the C-terminal sequence of human caseinoglycopeptide previously published in part by others.
7460900	4	22	from	milk	752:755	arg1	differences					731:741	differences	731:741	differences from one milk	731:755	A significant microheterogeneity seems to occur at the sugar level of human caseinoglycopeptide, which might thus present differences from one milk to another.
7460900	1	23	theme	glycopeptides	76:88	arg1	study					67:71	The study	63:71	The study of glycopeptides obtained after enzymic digestions of human caseinoglycopeptide	63:151	The study of glycopeptides obtained after enzymic digestions of human caseinoglycopeptide demonstrated the presence of several (up to 10) prosthetic sugar groups distributed throughout the peptide chain instead of only one in the case of cow and sheep kappa-caseinoglycopeptides.
7460900	1	24	from	chain	260:264	arg1	case					293:296	the case	289:296	the case of cow and sheep kappa-caseinoglycopeptides	289:340	The study of glycopeptides obtained after enzymic digestions of human caseinoglycopeptide demonstrated the presence of several (up to 10) prosthetic sugar groups distributed throughout the peptide chain instead of only one in the case of cow and sheep kappa-caseinoglycopeptides.
7460900	1	25	dep	groups	218:223	arg1	10					197:198	10	197:198	10	197:198	The study of glycopeptides obtained after enzymic digestions of human caseinoglycopeptide demonstrated the presence of several (up to 10) prosthetic sugar groups distributed throughout the peptide chain instead of only one in the case of cow and sheep kappa-caseinoglycopeptides.
7460900	3	26	theme	predicted	488:496	arg1	structure					508:516	The predicted secondary structure	484:516	The predicted secondary structure	484:516	The predicted secondary structure was in accordance with the high number of sugar groups situated all but one in beta-turns.
7460900	2	27	theme	C-terminal	395:404	arg1	sequence					406:413	the C-terminal sequence	391:413	the C-terminal sequence of human caseinoglycopeptide previously published in part by others	391:481	One of the glycopeptides allowed us to complete the C-terminal sequence of human caseinoglycopeptide previously published in part by others.
7460900	0	28	theme	sugar	35:39	arg1	part					41:44	the sugar part	31:44	the sugar part of human casein	31:60	Localisation and importance of the sugar part of human casein.
7460900	1	29	theme	one	282:284	arg1	chain					260:264	the peptide chain	248:264	the peptide chain instead of only one in the case of cow and sheep kappa-caseinoglycopeptides	248:340	The study of glycopeptides obtained after enzymic digestions of human caseinoglycopeptide demonstrated the presence of several (up to 10) prosthetic sugar groups distributed throughout the peptide chain instead of only one in the case of cow and sheep kappa-caseinoglycopeptides.
7460900	4	30	theme	sugar	664:668	arg1	level					670:674	the sugar level	660:674	the sugar level of human caseinoglycopeptide	660:703	A significant microheterogeneity seems to occur at the sugar level of human caseinoglycopeptide, which might thus present differences from one milk to another.
7460900	1	31	gly	caseinoglycopeptide	133:151	arg2	caseinoglycopeptide					133:151	human caseinoglycopeptide	127:151	human caseinoglycopeptide	127:151	The study of glycopeptides obtained after enzymic digestions of human caseinoglycopeptide demonstrated the presence of several (up to 10) prosthetic sugar groups distributed throughout the peptide chain instead of only one in the case of cow and sheep kappa-caseinoglycopeptides.
7460900	3	32	theme	situated	573:580	arg1	groups					566:571	sugar groups	560:571	sugar groups situated all but one in beta-turns	560:606	The predicted secondary structure was in accordance with the high number of sugar groups situated all but one in beta-turns.
7460900	0	33	theme	part	41:44	arg1	importance					17:26	importance	17:26	importance	17:26	Localisation and importance of the sugar part of human casein.
7460900	0	33	theme	part	41:44	arg1	Localisation					0:11	Localisation	0:11	Localisation	0:11	Localisation and importance of the sugar part of human casein.
7460900	1	34	theme	enzymic	105:111	arg1	digestions					113:122	enzymic digestions	105:122	enzymic digestions of human caseinoglycopeptide	105:151	The study of glycopeptides obtained after enzymic digestions of human caseinoglycopeptide demonstrated the presence of several (up to 10) prosthetic sugar groups distributed throughout the peptide chain instead of only one in the case of cow and sheep kappa-caseinoglycopeptides.
7460900	2	35	gly	caseinoglycopeptide	424:442	arg2	caseinoglycopeptide					424:442	human caseinoglycopeptide	418:442	human caseinoglycopeptide previously published in part by others	418:481	One of the glycopeptides allowed us to complete the C-terminal sequence of human caseinoglycopeptide previously published in part by others.
7460900	1	36	dep	10	197:198	arg1	to					194:195	to	194:195	to	194:195	The study of glycopeptides obtained after enzymic digestions of human caseinoglycopeptide demonstrated the presence of several (up to 10) prosthetic sugar groups distributed throughout the peptide chain instead of only one in the case of cow and sheep kappa-caseinoglycopeptides.
7460900	1	37	theme	prosthetic	201:210	arg1	groups					218:223	several (up to 10) prosthetic sugar groups	182:223	several (up to 10) prosthetic sugar groups distributed throughout the peptide chain instead of only one in the case of cow and sheep kappa-caseinoglycopeptides	182:340	The study of glycopeptides obtained after enzymic digestions of human caseinoglycopeptide demonstrated the presence of several (up to 10) prosthetic sugar groups distributed throughout the peptide chain instead of only one in the case of cow and sheep kappa-caseinoglycopeptides.
7460900	4	38	gly	caseinoglycopeptide	685:703	arg2	caseinoglycopeptide					685:703	human caseinoglycopeptide	679:703	human caseinoglycopeptide	679:703	A significant microheterogeneity seems to occur at the sugar level of human caseinoglycopeptide, which might thus present differences from one milk to another.
7460900	1	39	theme	sugar	212:216	arg1	groups					218:223	several (up to 10) prosthetic sugar groups	182:223	several (up to 10) prosthetic sugar groups distributed throughout the peptide chain instead of only one in the case of cow and sheep kappa-caseinoglycopeptides	182:340	The study of glycopeptides obtained after enzymic digestions of human caseinoglycopeptide demonstrated the presence of several (up to 10) prosthetic sugar groups distributed throughout the peptide chain instead of only one in the case of cow and sheep kappa-caseinoglycopeptides.
7460900	0	40	theme	casein	55:60	arg1	part					41:44	the sugar part	31:44	the sugar part of human casein	31:60	Localisation and importance of the sugar part of human casein.
7460900	1	41	theme	human	127:131	arg1	caseinoglycopeptide					133:151	human caseinoglycopeptide	127:151	human caseinoglycopeptide	127:151	The study of glycopeptides obtained after enzymic digestions of human caseinoglycopeptide demonstrated the presence of several (up to 10) prosthetic sugar groups distributed throughout the peptide chain instead of only one in the case of cow and sheep kappa-caseinoglycopeptides.
7460900	1	42	theme	groups	218:223	arg1	presence					170:177	the presence	166:177	the presence of several (up to 10) prosthetic sugar groups distributed throughout the peptide chain instead of only one in the case of cow and sheep kappa-caseinoglycopeptides	166:340	The study of glycopeptides obtained after enzymic digestions of human caseinoglycopeptide demonstrated the presence of several (up to 10) prosthetic sugar groups distributed throughout the peptide chain instead of only one in the case of cow and sheep kappa-caseinoglycopeptides.
7460900	0	43	theme	human	49:53	arg1	casein					55:60	human casein	49:60	human casein	49:60	Localisation and importance of the sugar part of human casein.
7460900	1	44	theme	cow	301:303	arg1	kappa-caseinoglycopeptides					315:340	cow and sheep kappa-caseinoglycopeptides	301:340	cow and sheep kappa-caseinoglycopeptides	301:340	The study of glycopeptides obtained after enzymic digestions of human caseinoglycopeptide demonstrated the presence of several (up to 10) prosthetic sugar groups distributed throughout the peptide chain instead of only one in the case of cow and sheep kappa-caseinoglycopeptides.
7460900	1	45	theme	caseinoglycopeptide	133:151	arg1	digestions					113:122	enzymic digestions	105:122	enzymic digestions of human caseinoglycopeptide	105:151	The study of glycopeptides obtained after enzymic digestions of human caseinoglycopeptide demonstrated the presence of several (up to 10) prosthetic sugar groups distributed throughout the peptide chain instead of only one in the case of cow and sheep kappa-caseinoglycopeptides.
10669592	6	0	theme	determinants	1085:1096	arg1	understanding					1033:1045	a detailed understanding	1022:1045	a detailed understanding of the ligand-binding and specificity determinants	1022:1096	The inhibitor is bound to one side of this cavity and its binding mode provides a detailed understanding of the ligand-binding and specificity determinants.
10669592	4	1	theme	NEP	721:723	arg1	NEP					721:723	human NEP	715:723	human NEP	715:723	Here we describe the crystal structure of the extracellular domain (residues 52-749) of human NEP complexed with the generic metalloproteinase inhibitor phosphoramidon at 2.1 A resolution.
10669592	4	1	theme	NEP	721:723	arg1	residues					695:702	residues 52-749	695:709	residues 52-749	695:709	Here we describe the crystal structure of the extracellular domain (residues 52-749) of human NEP complexed with the generic metalloproteinase inhibitor phosphoramidon at 2.1 A resolution.
10669592	4	1	theme	NEP	721:723	arg1	domain					687:692	the extracellular domain	669:692	the extracellular domain (residues 52-749) of human NEP complexed with the generic metalloproteinase inhibitor phosphoramidon at 2.1 A resolution	669:813	Here we describe the crystal structure of the extracellular domain (residues 52-749) of human NEP complexed with the generic metalloproteinase inhibitor phosphoramidon at 2.1 A resolution.
10669592	6	2	theme	detailed	1024:1031	arg1	understanding					1033:1045	a detailed understanding	1022:1045	a detailed understanding of the ligand-binding and specificity determinants	1022:1096	The inhibitor is bound to one side of this cavity and its binding mode provides a detailed understanding of the ligand-binding and specificity determinants.
10669592	3	3	theme	considerable	526:537	arg1	interest					539:546	considerable interest	526:546	considerable interest in inhibitors of this enzyme	526:575	Due to the physiological importance of neutral endopeptidase in the modulation of nociceptive and pressor responses there is considerable interest in inhibitors of this enzyme as novel analgesics and anti-hypertensive agents.
10669592	3	4	from	importance	426:435	arg1	modulation					469:478	the modulation	465:478	the modulation of nociceptive and pressor responses	465:515	Due to the physiological importance of neutral endopeptidase in the modulation of nociceptive and pressor responses there is considerable interest in inhibitors of this enzyme as novel analgesics and anti-hypertensive agents.
10669592	5	5	contain	containing	914:923	arg1	cavity					907:912	a large central cavity	891:912	a large central cavity containing the active site	891:939	The structure reveals two multiply connected folding domains which embrace a large central cavity containing the active site.
10669592	5	5	contain	containing	914:923	arg2	site					936:939	the active site	925:939	the active site	925:939	The structure reveals two multiply connected folding domains which embrace a large central cavity containing the active site.
10669592	4	6	theme	A	802:802	arg1	resolution					804:813	2.1 A resolution	798:813	2.1 A resolution	798:813	Here we describe the crystal structure of the extracellular domain (residues 52-749) of human NEP complexed with the generic metalloproteinase inhibitor phosphoramidon at 2.1 A resolution.
10669592	4	7	theme	inhibitor	770:778	arg1	phosphoramidon					780:793	the generic metalloproteinase inhibitor phosphoramidon	740:793	the generic metalloproteinase inhibitor phosphoramidon	740:793	Here we describe the crystal structure of the extracellular domain (residues 52-749) of human NEP complexed with the generic metalloproteinase inhibitor phosphoramidon at 2.1 A resolution.
10669592	3	8	from	interest	539:546	arg1	inhibitors					551:560	inhibitors	551:560	inhibitors of this enzyme	551:575	Due to the physiological importance of neutral endopeptidase in the modulation of nociceptive and pressor responses there is considerable interest in inhibitors of this enzyme as novel analgesics and anti-hypertensive agents.
10669592	3	9	theme	enzyme	570:575	arg1	inhibitors					551:560	inhibitors	551:560	inhibitors of this enzyme	551:575	Due to the physiological importance of neutral endopeptidase in the modulation of nociceptive and pressor responses there is considerable interest in inhibitors of this enzyme as novel analgesics and anti-hypertensive agents.
10669592	2	10	theme	substance	334:342	arg1	enkephalins					321:331	the enkephalins	317:331	the enkephalins	317:331	The range of substrates cleaved by neutral endopeptidase in vitro includes the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor.
10669592	2	10	theme	substance	334:342	arg1	P					344:344	substance P	334:344	substance P	334:344	The range of substrates cleaved by neutral endopeptidase in vitro includes the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor.
10669592	4	11	theme	human	715:719	arg1	NEP					721:723	human NEP	715:723	human NEP	715:723	Here we describe the crystal structure of the extracellular domain (residues 52-749) of human NEP complexed with the generic metalloproteinase inhibitor phosphoramidon at 2.1 A resolution.
10669592	1	12	theme	mammalian	112:120	arg1	endopeptidase					93:105	Neutral endopeptidase	85:105	Neutral endopeptidase	85:105	Neutral endopeptidase is a mammalian type II integral membrane zinc-containing endopeptidase, which degrades and inactivates a number of bioactive peptides.
10669592	1	12	theme	mammalian	112:120	arg1	endopeptidase					164:176	a mammalian type II integral membrane zinc-containing endopeptidase	110:176	a mammalian type II integral membrane zinc-containing endopeptidase	110:176	Neutral endopeptidase is a mammalian type II integral membrane zinc-containing endopeptidase, which degrades and inactivates a number of bioactive peptides.
10669592	3	13	theme	nociceptive	483:493	arg1	responses					507:515	nociceptive and pressor responses	483:515	responses	507:515	Due to the physiological importance of neutral endopeptidase in the modulation of nociceptive and pressor responses there is considerable interest in inhibitors of this enzyme as novel analgesics and anti-hypertensive agents.
10669592	6	14	theme	ligand-binding	1054:1067	arg1	understanding					1033:1045	a detailed understanding	1022:1045	a detailed understanding of the ligand-binding and specificity determinants	1022:1096	The inhibitor is bound to one side of this cavity and its binding mode provides a detailed understanding of the ligand-binding and specificity determinants.
10669592	3	15	theme	endopeptidase	448:460	arg1	importance					426:435	the physiological importance	408:435	the physiological importance of neutral endopeptidase in the modulation of nociceptive and pressor responses	408:515	Due to the physiological importance of neutral endopeptidase in the modulation of nociceptive and pressor responses there is considerable interest in inhibitors of this enzyme as novel analgesics and anti-hypertensive agents.
10669592	6	16	dep	ligand-binding	1054:1067	arg1	the					1050:1052	the	1050:1052	the	1050:1052	The inhibitor is bound to one side of this cavity and its binding mode provides a detailed understanding of the ligand-binding and specificity determinants.
10669592	2	17	theme	neutral	277:283	arg1	endopeptidase					285:297	neutral endopeptidase	277:297	neutral endopeptidase	277:297	The range of substrates cleaved by neutral endopeptidase in vitro includes the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor.
10669592	4	18	theme	domain	687:692	arg1	structure					656:664	the crystal structure	644:664	the crystal structure of the extracellular domain (residues 52-749) of human NEP complexed with the generic metalloproteinase inhibitor phosphoramidon at 2.1 A resolution	644:813	Here we describe the crystal structure of the extracellular domain (residues 52-749) of human NEP complexed with the generic metalloproteinase inhibitor phosphoramidon at 2.1 A resolution.
10669592	1	19	theme	Neutral	85:91	arg1	endopeptidase					93:105	Neutral endopeptidase	85:105	Neutral endopeptidase	85:105	Neutral endopeptidase is a mammalian type II integral membrane zinc-containing endopeptidase, which degrades and inactivates a number of bioactive peptides.
10669592	1	19	theme	Neutral	85:91	arg1	endopeptidase					164:176	a mammalian type II integral membrane zinc-containing endopeptidase	110:176	a mammalian type II integral membrane zinc-containing endopeptidase	110:176	Neutral endopeptidase is a mammalian type II integral membrane zinc-containing endopeptidase, which degrades and inactivates a number of bioactive peptides.
10669592	5	20	theme	connected	851:859	arg1	domains					869:875	two multiply connected folding domains	838:875	two multiply connected folding domains which embrace a large central cavity containing the active site	838:939	The structure reveals two multiply connected folding domains which embrace a large central cavity containing the active site.
10669592	6	21	theme	binding	1000:1006	arg1	mode					1008:1011	its binding mode	996:1011	its binding mode	996:1011	The inhibitor is bound to one side of this cavity and its binding mode provides a detailed understanding of the ligand-binding and specificity determinants.
10669592	5	22	theme	central	899:905	arg1	cavity					907:912	a large central cavity	891:912	a large central cavity containing the active site	891:939	The structure reveals two multiply connected folding domains which embrace a large central cavity containing the active site.
10669592	4	23	theme	metalloproteinase	752:768	arg1	phosphoramidon					780:793	the generic metalloproteinase inhibitor phosphoramidon	740:793	the generic metalloproteinase inhibitor phosphoramidon	740:793	Here we describe the crystal structure of the extracellular domain (residues 52-749) of human NEP complexed with the generic metalloproteinase inhibitor phosphoramidon at 2.1 A resolution.
10669592	2	24	theme	natriuretic	381:391	arg1	enkephalins					321:331	the enkephalins	317:331	the enkephalins	317:331	The range of substrates cleaved by neutral endopeptidase in vitro includes the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor.
10669592	2	24	theme	natriuretic	381:391	arg1	factor					393:398	atrial natriuretic factor	374:398	atrial natriuretic factor	374:398	The range of substrates cleaved by neutral endopeptidase in vitro includes the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor.
10669592	0	25	theme	neutral	19:25	arg1	Neprilysin					42:51	Neprilysin	42:51	Neprilysin	42:51	Structure of human neutral endopeptidase (Neprilysin) complexed with phosphoramidon.
10669592	0	25	theme	neutral	19:25	arg1	endopeptidase					27:39	human neutral endopeptidase	13:39	human neutral endopeptidase (Neprilysin)	13:52	Structure of human neutral endopeptidase (Neprilysin) complexed with phosphoramidon.
10669592	0	26	theme	human	13:17	arg1	Neprilysin					42:51	Neprilysin	42:51	Neprilysin	42:51	Structure of human neutral endopeptidase (Neprilysin) complexed with phosphoramidon.
10669592	0	26	theme	human	13:17	arg1	endopeptidase					27:39	human neutral endopeptidase	13:39	human neutral endopeptidase (Neprilysin)	13:52	Structure of human neutral endopeptidase (Neprilysin) complexed with phosphoramidon.
10669592	3	27	theme	novel	580:584	arg1	analgesics					586:595	novel analgesics	580:595	novel analgesics	580:595	Due to the physiological importance of neutral endopeptidase in the modulation of nociceptive and pressor responses there is considerable interest in inhibitors of this enzyme as novel analgesics and anti-hypertensive agents.
10669592	1	28	theme	membrane	139:146	arg1	endopeptidase					93:105	Neutral endopeptidase	85:105	Neutral endopeptidase	85:105	Neutral endopeptidase is a mammalian type II integral membrane zinc-containing endopeptidase, which degrades and inactivates a number of bioactive peptides.
10669592	1	28	theme	membrane	139:146	arg1	endopeptidase					164:176	a mammalian type II integral membrane zinc-containing endopeptidase	110:176	a mammalian type II integral membrane zinc-containing endopeptidase	110:176	Neutral endopeptidase is a mammalian type II integral membrane zinc-containing endopeptidase, which degrades and inactivates a number of bioactive peptides.
10669592	3	29	theme	physiological	412:424	arg1	importance					426:435	the physiological importance	408:435	the physiological importance of neutral endopeptidase in the modulation of nociceptive and pressor responses	408:515	Due to the physiological importance of neutral endopeptidase in the modulation of nociceptive and pressor responses there is considerable interest in inhibitors of this enzyme as novel analgesics and anti-hypertensive agents.
10669592	6	30	theme	cavity	985:990	arg1	side					972:975	one side	968:975	one side of this cavity	968:990	The inhibitor is bound to one side of this cavity and its binding mode provides a detailed understanding of the ligand-binding and specificity determinants.
10669592	6	31	theme	specificity	1073:1083	arg1	determinants					1085:1096	specificity determinants	1073:1096	specificity determinants	1073:1096	The inhibitor is bound to one side of this cavity and its binding mode provides a detailed understanding of the ligand-binding and specificity determinants.
10669592	3	32	theme	neutral	440:446	arg1	endopeptidase					448:460	neutral endopeptidase	440:460	neutral endopeptidase	440:460	Due to the physiological importance of neutral endopeptidase in the modulation of nociceptive and pressor responses there is considerable interest in inhibitors of this enzyme as novel analgesics and anti-hypertensive agents.
10669592	4	33	theme	extracellular	673:685	arg1	NEP					721:723	human NEP	715:723	human NEP	715:723	Here we describe the crystal structure of the extracellular domain (residues 52-749) of human NEP complexed with the generic metalloproteinase inhibitor phosphoramidon at 2.1 A resolution.
10669592	4	33	theme	extracellular	673:685	arg1	residues					695:702	residues 52-749	695:709	residues 52-749	695:709	Here we describe the crystal structure of the extracellular domain (residues 52-749) of human NEP complexed with the generic metalloproteinase inhibitor phosphoramidon at 2.1 A resolution.
10669592	4	33	theme	extracellular	673:685	arg1	domain					687:692	the extracellular domain	669:692	the extracellular domain (residues 52-749) of human NEP complexed with the generic metalloproteinase inhibitor phosphoramidon at 2.1 A resolution	669:813	Here we describe the crystal structure of the extracellular domain (residues 52-749) of human NEP complexed with the generic metalloproteinase inhibitor phosphoramidon at 2.1 A resolution.
10669592	0	34	theme	endopeptidase	27:39	arg1	Structure					0:8	Structure	0:8	Structure of human neutral endopeptidase (Neprilysin)	0:52	Structure of human neutral endopeptidase (Neprilysin) complexed with phosphoramidon.
10669592	5	35	theme	folding	861:867	arg1	domains					869:875	two multiply connected folding domains	838:875	two multiply connected folding domains which embrace a large central cavity containing the active site	838:939	The structure reveals two multiply connected folding domains which embrace a large central cavity containing the active site.
10669592	1	36	theme	bioactive	222:230	arg1	peptides					232:239	bioactive peptides	222:239	bioactive peptides	222:239	Neutral endopeptidase is a mammalian type II integral membrane zinc-containing endopeptidase, which degrades and inactivates a number of bioactive peptides.
10669592	5	37	theme	active	929:934	arg1	site					936:939	the active site	925:939	the active site	925:939	The structure reveals two multiply connected folding domains which embrace a large central cavity containing the active site.
10669592	3	38	theme	anti-hypertensive	601:617	arg1	agents					619:624	anti-hypertensive agents	601:624	anti-hypertensive agents	601:624	Due to the physiological importance of neutral endopeptidase in the modulation of nociceptive and pressor responses there is considerable interest in inhibitors of this enzyme as novel analgesics and anti-hypertensive agents.
10669592	3	39	theme	responses	507:515	arg1	modulation					469:478	the modulation	465:478	the modulation of nociceptive and pressor responses	465:515	Due to the physiological importance of neutral endopeptidase in the modulation of nociceptive and pressor responses there is considerable interest in inhibitors of this enzyme as novel analgesics and anti-hypertensive agents.
10669592	1	40	theme	type	122:125	arg1	endopeptidase					93:105	Neutral endopeptidase	85:105	Neutral endopeptidase	85:105	Neutral endopeptidase is a mammalian type II integral membrane zinc-containing endopeptidase, which degrades and inactivates a number of bioactive peptides.
10669592	1	40	theme	type	122:125	arg1	endopeptidase					164:176	a mammalian type II integral membrane zinc-containing endopeptidase	110:176	a mammalian type II integral membrane zinc-containing endopeptidase	110:176	Neutral endopeptidase is a mammalian type II integral membrane zinc-containing endopeptidase, which degrades and inactivates a number of bioactive peptides.
10669592	4	41	theme	generic	744:750	arg1	phosphoramidon					780:793	the generic metalloproteinase inhibitor phosphoramidon	740:793	the generic metalloproteinase inhibitor phosphoramidon	740:793	Here we describe the crystal structure of the extracellular domain (residues 52-749) of human NEP complexed with the generic metalloproteinase inhibitor phosphoramidon at 2.1 A resolution.
10669592	1	42	theme	peptides	232:239	arg1	number					212:217	a number	210:217	a number of bioactive peptides	210:239	Neutral endopeptidase is a mammalian type II integral membrane zinc-containing endopeptidase, which degrades and inactivates a number of bioactive peptides.
10669592	4	43	dep	residues	695:702	arg1	52-749					704:709	52-749	704:709	52-749	704:709	Here we describe the crystal structure of the extracellular domain (residues 52-749) of human NEP complexed with the generic metalloproteinase inhibitor phosphoramidon at 2.1 A resolution.
10669592	1	44	theme	integral	130:137	arg1	endopeptidase					93:105	Neutral endopeptidase	85:105	Neutral endopeptidase	85:105	Neutral endopeptidase is a mammalian type II integral membrane zinc-containing endopeptidase, which degrades and inactivates a number of bioactive peptides.
10669592	1	44	theme	integral	130:137	arg1	endopeptidase					164:176	a mammalian type II integral membrane zinc-containing endopeptidase	110:176	a mammalian type II integral membrane zinc-containing endopeptidase	110:176	Neutral endopeptidase is a mammalian type II integral membrane zinc-containing endopeptidase, which degrades and inactivates a number of bioactive peptides.
10669592	5	45	theme	large	893:897	arg1	cavity					907:912	a large central cavity	891:912	a large central cavity containing the active site	891:939	The structure reveals two multiply connected folding domains which embrace a large central cavity containing the active site.
10669592	2	46	theme	substrates	255:264	arg1	range					246:250	The range	242:250	The range of substrates cleaved by neutral endopeptidase in vitro	242:306	The range of substrates cleaved by neutral endopeptidase in vitro includes the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor.
10669592	2	47	theme	atrial	374:379	arg1	enkephalins					321:331	the enkephalins	317:331	the enkephalins	317:331	The range of substrates cleaved by neutral endopeptidase in vitro includes the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor.
10669592	2	47	theme	atrial	374:379	arg1	factor					393:398	atrial natriuretic factor	374:398	atrial natriuretic factor	374:398	The range of substrates cleaved by neutral endopeptidase in vitro includes the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor.
10669592	3	48	theme	pressor	499:505	arg1	responses					507:515	nociceptive and pressor responses	483:515	responses	507:515	Due to the physiological importance of neutral endopeptidase in the modulation of nociceptive and pressor responses there is considerable interest in inhibitors of this enzyme as novel analgesics and anti-hypertensive agents.
10669592	4	49	theme	crystal	648:654	arg1	structure					656:664	the crystal structure	644:664	the crystal structure of the extracellular domain (residues 52-749) of human NEP complexed with the generic metalloproteinase inhibitor phosphoramidon at 2.1 A resolution	644:813	Here we describe the crystal structure of the extracellular domain (residues 52-749) of human NEP complexed with the generic metalloproteinase inhibitor phosphoramidon at 2.1 A resolution.
10669592	1	50	theme	zinc-containing	148:162	arg1	endopeptidase					93:105	Neutral endopeptidase	85:105	Neutral endopeptidase	85:105	Neutral endopeptidase is a mammalian type II integral membrane zinc-containing endopeptidase, which degrades and inactivates a number of bioactive peptides.
10669592	1	50	theme	zinc-containing	148:162	arg1	endopeptidase					164:176	a mammalian type II integral membrane zinc-containing endopeptidase	110:176	a mammalian type II integral membrane zinc-containing endopeptidase	110:176	Neutral endopeptidase is a mammalian type II integral membrane zinc-containing endopeptidase, which degrades and inactivates a number of bioactive peptides.
14754895	6	0	theme	reactivity	1333:1342	arg1	change					1344:1349	the observed reactivity change	1320:1349	the observed reactivity change from the peptidyl dipeptidase activity of ACE to the carboxypeptidase activity of ACE2	1320:1436	A few active site residue substitutions in ACE2 relative to ACE appear to eliminate the S(2)' substrate-binding subsite and account for the observed reactivity change from the peptidyl dipeptidase activity of ACE to the carboxypeptidase activity of ACE2.
14754895	6	1	theme	relative	1232:1239	arg1	ACE2					1227:1230	ACE2	1227:1230	ACE2 relative to ACE	1227:1246	A few active site residue substitutions in ACE2 relative to ACE appear to eliminate the S(2)' substrate-binding subsite and account for the observed reactivity change from the peptidyl dipeptidase activity of ACE to the carboxypeptidase activity of ACE2.
14754895	1	2	theme	acids	228:232	arg1	protein					207:213	a type I integral membrane protein	180:213	a type I integral membrane protein of 805 amino acids that contains one HEXXH + E zinc-binding consensus sequence	180:292	The angiotensin-converting enzyme (ACE)-related carboxypeptidase, ACE2, is a type I integral membrane protein of 805 amino acids that contains one HEXXH + E zinc-binding consensus sequence.
14754895	1	2	theme	acids	228:232	arg1	enzyme					132:137	The angiotensin-converting enzyme	105:137	The angiotensin-converting enzyme (ACE)	105:143	The angiotensin-converting enzyme (ACE)-related carboxypeptidase, ACE2, is a type I integral membrane protein of 805 amino acids that contains one HEXXH + E zinc-binding consensus sequence.
14754895	0	3	theme	inhibitor	72:80	arg1	binding					82:88	inhibitor binding	72:88	inhibitor binding	72:88	ACE2 X-ray structures reveal a large hinge-bending motion important for inhibitor binding and catalysis.
14754895	6	4	from	activity	1381:1388	arg1	change					1344:1349	the observed reactivity change	1320:1349	the observed reactivity change from the peptidyl dipeptidase activity of ACE to the carboxypeptidase activity of ACE2	1320:1436	A few active site residue substitutions in ACE2 relative to ACE appear to eliminate the S(2)' substrate-binding subsite and account for the observed reactivity change from the peptidyl dipeptidase activity of ACE to the carboxypeptidase activity of ACE2.
14754895	5	5	dep	catalysis	1147:1155	arg1	specificity					1171:1181	specificity	1171:1181	specificity	1171:1181	The potent inhibitor MLN-4760 ((S,S)-2-[1-carboxy-2-[3-(3,5-dichlorobenzyl)-3H-imidazol4-yl]-ethylamino]-4-methylpentanoic acid) makes key binding interactions within the active site and offers insights regarding the action of residues involved in catalysis and substrate specificity.
14754895	5	6	theme	key	1034:1036	arg1	interactions					1046:1057	key binding interactions	1034:1057	key binding interactions within the active site	1034:1080	The potent inhibitor MLN-4760 ((S,S)-2-[1-carboxy-2-[3-(3,5-dichlorobenzyl)-3H-imidazol4-yl]-ethylamino]-4-methylpentanoic acid) makes key binding interactions within the active site and offers insights regarding the action of residues involved in catalysis and substrate specificity.
14754895	3	7	theme	3.0-A	638:642	arg1	resolution					644:653	3.0-A resolution	638:653	3.0-A resolution	638:653	To gain further insights into this enzyme, the first crystal structures of the native and inhibitor-bound forms of the ACE2 extracellular domains were solved to 2.2- and 3.0-A resolution, respectively.
14754895	4	8	theme	important	851:859	arg1	residues					861:868	important residues	851:868	important residues	851:868	Comparison of these structures revealed a large inhibitor-dependent hinge-bending movement of one catalytic subdomain relative to the other ( approximately 16 degrees ) that brings important residues into position for catalysis.
14754895	6	9	theme	site	1197:1200	arg1	substitutions					1210:1222	A few active site residue substitutions	1184:1222	A few active site residue substitutions in ACE2 relative to ACE	1184:1246	A few active site residue substitutions in ACE2 relative to ACE appear to eliminate the S(2)' substrate-binding subsite and account for the observed reactivity change from the peptidyl dipeptidase activity of ACE to the carboxypeptidase activity of ACE2.
14754895	4	10	theme	inhibitor-dependent	718:736	arg1	movement					752:759	a large inhibitor-dependent hinge-bending movement	710:759	a large inhibitor-dependent hinge-bending movement of one catalytic subdomain relative to the other ( approximately 16 degrees ) that brings important residues into position for catalysis	710:896	Comparison of these structures revealed a large inhibitor-dependent hinge-bending movement of one catalytic subdomain relative to the other ( approximately 16 degrees ) that brings important residues into position for catalysis.
14754895	6	11	theme	carboxypeptidase	1404:1419	arg1	activity					1421:1428	the carboxypeptidase activity	1400:1428	the carboxypeptidase activity of ACE2	1400:1436	A few active site residue substitutions in ACE2 relative to ACE appear to eliminate the S(2)' substrate-binding subsite and account for the observed reactivity change from the peptidyl dipeptidase activity of ACE to the carboxypeptidase activity of ACE2.
14754895	5	12	theme	S	931:931	arg1	inhibitor					910:918	The potent inhibitor MLN-4760	899:927	The potent inhibitor MLN-4760 ((S,S)-2-[1-carboxy-2-[3-(3,5-dichlorobenzyl)-3H-imidazol4-yl]-ethylamino]-4-methylpentanoic acid)	899:1026	The potent inhibitor MLN-4760 ((S,S)-2-[1-carboxy-2-[3-(3,5-dichlorobenzyl)-3H-imidazol4-yl]-ethylamino]-4-methylpentanoic acid) makes key binding interactions within the active site and offers insights regarding the action of residues involved in catalysis and substrate specificity.
14754895	5	12	theme	S	931:931	arg1	acid					1022:1025	(S,S)-2-[1-carboxy-2-[3-(3,5-dichlorobenzyl)-3H-imidazol4-yl]-ethylamino]-4-methylpentanoic acid	930:1025	acid	1022:1025	The potent inhibitor MLN-4760 ((S,S)-2-[1-carboxy-2-[3-(3,5-dichlorobenzyl)-3H-imidazol4-yl]-ethylamino]-4-methylpentanoic acid) makes key binding interactions within the active site and offers insights regarding the action of residues involved in catalysis and substrate specificity.
14754895	4	13	theme	structures	690:699	arg1	Comparison					670:679	Comparison	670:679	Comparison of these structures	670:699	Comparison of these structures revealed a large inhibitor-dependent hinge-bending movement of one catalytic subdomain relative to the other ( approximately 16 degrees ) that brings important residues into position for catalysis.
14754895	4	14	theme	large	712:716	arg1	movement					752:759	a large inhibitor-dependent hinge-bending movement	710:759	a large inhibitor-dependent hinge-bending movement of one catalytic subdomain relative to the other ( approximately 16 degrees ) that brings important residues into position for catalysis	710:896	Comparison of these structures revealed a large inhibitor-dependent hinge-bending movement of one catalytic subdomain relative to the other ( approximately 16 degrees ) that brings important residues into position for catalysis.
14754895	5	15	theme	potent	903:908	arg1	inhibitor					910:918	The potent inhibitor MLN-4760	899:927	The potent inhibitor MLN-4760 ((S,S)-2-[1-carboxy-2-[3-(3,5-dichlorobenzyl)-3H-imidazol4-yl]-ethylamino]-4-methylpentanoic acid)	899:1026	The potent inhibitor MLN-4760 ((S,S)-2-[1-carboxy-2-[3-(3,5-dichlorobenzyl)-3H-imidazol4-yl]-ethylamino]-4-methylpentanoic acid) makes key binding interactions within the active site and offers insights regarding the action of residues involved in catalysis and substrate specificity.
14754895	5	15	theme	potent	903:908	arg1	acid					1022:1025	(S,S)-2-[1-carboxy-2-[3-(3,5-dichlorobenzyl)-3H-imidazol4-yl]-ethylamino]-4-methylpentanoic acid	930:1025	acid	1022:1025	The potent inhibitor MLN-4760 ((S,S)-2-[1-carboxy-2-[3-(3,5-dichlorobenzyl)-3H-imidazol4-yl]-ethylamino]-4-methylpentanoic acid) makes key binding interactions within the active site and offers insights regarding the action of residues involved in catalysis and substrate specificity.
14754895	5	16	theme	active	1070:1075	arg1	site					1077:1080	the active site	1066:1080	the active site	1066:1080	The potent inhibitor MLN-4760 ((S,S)-2-[1-carboxy-2-[3-(3,5-dichlorobenzyl)-3H-imidazol4-yl]-ethylamino]-4-methylpentanoic acid) makes key binding interactions within the active site and offers insights regarding the action of residues involved in catalysis and substrate specificity.
14754895	5	17	dep	acid	1022:1025	arg1	S					933:933	(S,S)-2-[1-carboxy-2-[3-(3,5-dichlorobenzyl)-3H-imidazol4-yl]-ethylamino]-4-methylpentanoic acid	930:1025	S	933:933	The potent inhibitor MLN-4760 ((S,S)-2-[1-carboxy-2-[3-(3,5-dichlorobenzyl)-3H-imidazol4-yl]-ethylamino]-4-methylpentanoic acid) makes key binding interactions within the active site and offers insights regarding the action of residues involved in catalysis and substrate specificity.
14754895	2	18	theme	respiratory	439:449	arg1	SARS					461:464	SARS	461:464	SARS	461:464	ACE2 has been implicated in the regulation of heart function and also as a functional receptor for the coronavirus that causes the severe acute respiratory syndrome (SARS).
14754895	2	18	theme	respiratory	439:449	arg1	syndrome					451:458	the severe acute respiratory syndrome	422:458	the severe acute respiratory syndrome (SARS)	422:465	ACE2 has been implicated in the regulation of heart function and also as a functional receptor for the coronavirus that causes the severe acute respiratory syndrome (SARS).
14754895	1	19	dep	enzyme	132:137	arg1	carboxypeptidase					153:168	-related carboxypeptidase	144:168	-related carboxypeptidase	144:168	The angiotensin-converting enzyme (ACE)-related carboxypeptidase, ACE2, is a type I integral membrane protein of 805 amino acids that contains one HEXXH + E zinc-binding consensus sequence.
14754895	0	20	theme	X-ray	5:9	arg1	structures					11:20	ACE2 X-ray structures	0:20	ACE2 X-ray structures	0:20	ACE2 X-ray structures reveal a large hinge-bending motion important for inhibitor binding and catalysis.
14754895	6	21	theme	observed	1324:1331	arg1	change					1344:1349	the observed reactivity change	1320:1349	the observed reactivity change from the peptidyl dipeptidase activity of ACE to the carboxypeptidase activity of ACE2	1320:1436	A few active site residue substitutions in ACE2 relative to ACE appear to eliminate the S(2)' substrate-binding subsite and account for the observed reactivity change from the peptidyl dipeptidase activity of ACE to the carboxypeptidase activity of ACE2.
14754895	3	22	theme	first	515:519	arg1	structures					529:538	the first crystal structures	511:538	the first crystal structures of the native and inhibitor-bound forms of the ACE2 extracellular domains	511:612	To gain further insights into this enzyme, the first crystal structures of the native and inhibitor-bound forms of the ACE2 extracellular domains were solved to 2.2- and 3.0-A resolution, respectively.
14754895	6	23	theme	peptidyl	1360:1367	arg1	activity					1381:1388	the peptidyl dipeptidase activity	1356:1388	the peptidyl dipeptidase activity of ACE to the carboxypeptidase activity of ACE2	1356:1436	A few active site residue substitutions in ACE2 relative to ACE appear to eliminate the S(2)' substrate-binding subsite and account for the observed reactivity change from the peptidyl dipeptidase activity of ACE to the carboxypeptidase activity of ACE2.
14754895	0	24	theme	ACE2	0:3	arg1	structures					11:20	ACE2 X-ray structures	0:20	ACE2 X-ray structures	0:20	ACE2 X-ray structures reveal a large hinge-bending motion important for inhibitor binding and catalysis.
14754895	3	25	theme	crystal	521:527	arg1	structures					529:538	the first crystal structures	511:538	the first crystal structures of the native and inhibitor-bound forms of the ACE2 extracellular domains	511:612	To gain further insights into this enzyme, the first crystal structures of the native and inhibitor-bound forms of the ACE2 extracellular domains were solved to 2.2- and 3.0-A resolution, respectively.
14754895	2	26	theme	function	347:354	arg1	regulation					327:336	the regulation	323:336	the regulation of heart function	323:354	ACE2 has been implicated in the regulation of heart function and also as a functional receptor for the coronavirus that causes the severe acute respiratory syndrome (SARS).
14754895	6	27	theme	ACE	1393:1395	arg1	activity					1381:1388	the peptidyl dipeptidase activity	1356:1388	the peptidyl dipeptidase activity of ACE to the carboxypeptidase activity of ACE2	1356:1436	A few active site residue substitutions in ACE2 relative to ACE appear to eliminate the S(2)' substrate-binding subsite and account for the observed reactivity change from the peptidyl dipeptidase activity of ACE to the carboxypeptidase activity of ACE2.
14754895	5	28	theme	3,5-dichlorobenzyl	955:972	arg1	inhibitor					910:918	The potent inhibitor MLN-4760	899:927	The potent inhibitor MLN-4760 ((S,S)-2-[1-carboxy-2-[3-(3,5-dichlorobenzyl)-3H-imidazol4-yl]-ethylamino]-4-methylpentanoic acid)	899:1026	The potent inhibitor MLN-4760 ((S,S)-2-[1-carboxy-2-[3-(3,5-dichlorobenzyl)-3H-imidazol4-yl]-ethylamino]-4-methylpentanoic acid) makes key binding interactions within the active site and offers insights regarding the action of residues involved in catalysis and substrate specificity.
14754895	5	28	theme	3,5-dichlorobenzyl	955:972	arg1	acid					1022:1025	(S,S)-2-[1-carboxy-2-[3-(3,5-dichlorobenzyl)-3H-imidazol4-yl]-ethylamino]-4-methylpentanoic acid	930:1025	acid	1022:1025	The potent inhibitor MLN-4760 ((S,S)-2-[1-carboxy-2-[3-(3,5-dichlorobenzyl)-3H-imidazol4-yl]-ethylamino]-4-methylpentanoic acid) makes key binding interactions within the active site and offers insights regarding the action of residues involved in catalysis and substrate specificity.
14754895	3	29	theme	domains	606:612	arg1	forms					574:578	the native and inhibitor-bound forms	543:578	the native and inhibitor-bound forms of the ACE2 extracellular domains	543:612	To gain further insights into this enzyme, the first crystal structures of the native and inhibitor-bound forms of the ACE2 extracellular domains were solved to 2.2- and 3.0-A resolution, respectively.
14754895	1	30	theme	type	182:185	arg1	protein					207:213	a type I integral membrane protein	180:213	a type I integral membrane protein of 805 amino acids that contains one HEXXH + E zinc-binding consensus sequence	180:292	The angiotensin-converting enzyme (ACE)-related carboxypeptidase, ACE2, is a type I integral membrane protein of 805 amino acids that contains one HEXXH + E zinc-binding consensus sequence.
14754895	1	30	theme	type	182:185	arg1	enzyme					132:137	The angiotensin-converting enzyme	105:137	The angiotensin-converting enzyme (ACE)	105:143	The angiotensin-converting enzyme (ACE)-related carboxypeptidase, ACE2, is a type I integral membrane protein of 805 amino acids that contains one HEXXH + E zinc-binding consensus sequence.
14754895	1	31	theme	E	260:260	arg1	sequence					285:292	one HEXXH + E zinc-binding consensus sequence	248:292	sequence	285:292	The angiotensin-converting enzyme (ACE)-related carboxypeptidase, ACE2, is a type I integral membrane protein of 805 amino acids that contains one HEXXH + E zinc-binding consensus sequence.
14754895	6	32	theme	substrate-binding	1278:1294	arg1	subsite					1296:1302	the S(2)' substrate-binding subsite	1268:1302	the S(2)' substrate-binding subsite	1268:1302	A few active site residue substitutions in ACE2 relative to ACE appear to eliminate the S(2)' substrate-binding subsite and account for the observed reactivity change from the peptidyl dipeptidase activity of ACE to the carboxypeptidase activity of ACE2.
14754895	3	33	theme	extracellular	592:604	arg1	domains					606:612	the ACE2 extracellular domains	583:612	the ACE2 extracellular domains	583:612	To gain further insights into this enzyme, the first crystal structures of the native and inhibitor-bound forms of the ACE2 extracellular domains were solved to 2.2- and 3.0-A resolution, respectively.
14754895	1	34	theme	I	187:187	arg1	protein					207:213	a type I integral membrane protein	180:213	a type I integral membrane protein of 805 amino acids that contains one HEXXH + E zinc-binding consensus sequence	180:292	The angiotensin-converting enzyme (ACE)-related carboxypeptidase, ACE2, is a type I integral membrane protein of 805 amino acids that contains one HEXXH + E zinc-binding consensus sequence.
14754895	1	34	theme	I	187:187	arg1	enzyme					132:137	The angiotensin-converting enzyme	105:137	The angiotensin-converting enzyme (ACE)	105:143	The angiotensin-converting enzyme (ACE)-related carboxypeptidase, ACE2, is a type I integral membrane protein of 805 amino acids that contains one HEXXH + E zinc-binding consensus sequence.
14754895	0	35	theme	large	31:35	arg1	motion					51:56	a large hinge-bending motion	29:56	a large hinge-bending motion important for inhibitor binding and catalysis	29:102	ACE2 X-ray structures reveal a large hinge-bending motion important for inhibitor binding and catalysis.
14754895	1	36	theme	zinc-binding	262:273	arg1	sequence					285:292	one HEXXH + E zinc-binding consensus sequence	248:292	sequence	285:292	The angiotensin-converting enzyme (ACE)-related carboxypeptidase, ACE2, is a type I integral membrane protein of 805 amino acids that contains one HEXXH + E zinc-binding consensus sequence.
14754895	6	37	theme	residue	1202:1208	arg1	substitutions					1210:1222	A few active site residue substitutions	1184:1222	A few active site residue substitutions in ACE2 relative to ACE	1184:1246	A few active site residue substitutions in ACE2 relative to ACE appear to eliminate the S(2)' substrate-binding subsite and account for the observed reactivity change from the peptidyl dipeptidase activity of ACE to the carboxypeptidase activity of ACE2.
14754895	1	38	theme	integral	189:196	arg1	protein					207:213	a type I integral membrane protein	180:213	a type I integral membrane protein of 805 amino acids that contains one HEXXH + E zinc-binding consensus sequence	180:292	The angiotensin-converting enzyme (ACE)-related carboxypeptidase, ACE2, is a type I integral membrane protein of 805 amino acids that contains one HEXXH + E zinc-binding consensus sequence.
14754895	1	38	theme	integral	189:196	arg1	enzyme					132:137	The angiotensin-converting enzyme	105:137	The angiotensin-converting enzyme (ACE)	105:143	The angiotensin-converting enzyme (ACE)-related carboxypeptidase, ACE2, is a type I integral membrane protein of 805 amino acids that contains one HEXXH + E zinc-binding consensus sequence.
14754895	5	39	theme	-3H-imidazol4-yl	974:989	arg1	inhibitor					910:918	The potent inhibitor MLN-4760	899:927	The potent inhibitor MLN-4760 ((S,S)-2-[1-carboxy-2-[3-(3,5-dichlorobenzyl)-3H-imidazol4-yl]-ethylamino]-4-methylpentanoic acid)	899:1026	The potent inhibitor MLN-4760 ((S,S)-2-[1-carboxy-2-[3-(3,5-dichlorobenzyl)-3H-imidazol4-yl]-ethylamino]-4-methylpentanoic acid) makes key binding interactions within the active site and offers insights regarding the action of residues involved in catalysis and substrate specificity.
14754895	5	39	theme	-3H-imidazol4-yl	974:989	arg1	acid					1022:1025	(S,S)-2-[1-carboxy-2-[3-(3,5-dichlorobenzyl)-3H-imidazol4-yl]-ethylamino]-4-methylpentanoic acid	930:1025	acid	1022:1025	The potent inhibitor MLN-4760 ((S,S)-2-[1-carboxy-2-[3-(3,5-dichlorobenzyl)-3H-imidazol4-yl]-ethylamino]-4-methylpentanoic acid) makes key binding interactions within the active site and offers insights regarding the action of residues involved in catalysis and substrate specificity.
14754895	2	40	theme	functional	370:379	arg1	receptor					381:388	a functional receptor	368:388	a functional receptor for the coronavirus that causes the severe acute respiratory syndrome (SARS)	368:465	ACE2 has been implicated in the regulation of heart function and also as a functional receptor for the coronavirus that causes the severe acute respiratory syndrome (SARS).
14754895	2	41	theme	acute	433:437	arg1	SARS					461:464	SARS	461:464	SARS	461:464	ACE2 has been implicated in the regulation of heart function and also as a functional receptor for the coronavirus that causes the severe acute respiratory syndrome (SARS).
14754895	2	41	theme	acute	433:437	arg1	syndrome					451:458	the severe acute respiratory syndrome	422:458	the severe acute respiratory syndrome (SARS)	422:465	ACE2 has been implicated in the regulation of heart function and also as a functional receptor for the coronavirus that causes the severe acute respiratory syndrome (SARS).
14754895	1	42	theme	consensus	275:283	arg1	sequence					285:292	one HEXXH + E zinc-binding consensus sequence	248:292	sequence	285:292	The angiotensin-converting enzyme (ACE)-related carboxypeptidase, ACE2, is a type I integral membrane protein of 805 amino acids that contains one HEXXH + E zinc-binding consensus sequence.
14754895	6	43	theme	dipeptidase	1369:1379	arg1	activity					1381:1388	the peptidyl dipeptidase activity	1356:1388	the peptidyl dipeptidase activity of ACE to the carboxypeptidase activity of ACE2	1356:1436	A few active site residue substitutions in ACE2 relative to ACE appear to eliminate the S(2)' substrate-binding subsite and account for the observed reactivity change from the peptidyl dipeptidase activity of ACE to the carboxypeptidase activity of ACE2.
14754895	3	44	theme	native	547:552	arg1	forms					574:578	the native and inhibitor-bound forms	543:578	the native and inhibitor-bound forms of the ACE2 extracellular domains	543:612	To gain further insights into this enzyme, the first crystal structures of the native and inhibitor-bound forms of the ACE2 extracellular domains were solved to 2.2- and 3.0-A resolution, respectively.
14754895	1	45	theme	membrane	198:205	arg1	protein					207:213	a type I integral membrane protein	180:213	a type I integral membrane protein of 805 amino acids that contains one HEXXH + E zinc-binding consensus sequence	180:292	The angiotensin-converting enzyme (ACE)-related carboxypeptidase, ACE2, is a type I integral membrane protein of 805 amino acids that contains one HEXXH + E zinc-binding consensus sequence.
14754895	1	45	theme	membrane	198:205	arg1	enzyme					132:137	The angiotensin-converting enzyme	105:137	The angiotensin-converting enzyme (ACE)	105:143	The angiotensin-converting enzyme (ACE)-related carboxypeptidase, ACE2, is a type I integral membrane protein of 805 amino acids that contains one HEXXH + E zinc-binding consensus sequence.
14754895	2	46	theme	severe	426:431	arg1	SARS					461:464	SARS	461:464	SARS	461:464	ACE2 has been implicated in the regulation of heart function and also as a functional receptor for the coronavirus that causes the severe acute respiratory syndrome (SARS).
14754895	2	46	theme	severe	426:431	arg1	syndrome					451:458	the severe acute respiratory syndrome	422:458	the severe acute respiratory syndrome (SARS)	422:465	ACE2 has been implicated in the regulation of heart function and also as a functional receptor for the coronavirus that causes the severe acute respiratory syndrome (SARS).
14754895	3	47	theme	ACE2	587:590	arg1	domains					606:612	the ACE2 extracellular domains	583:612	the ACE2 extracellular domains	583:612	To gain further insights into this enzyme, the first crystal structures of the native and inhibitor-bound forms of the ACE2 extracellular domains were solved to 2.2- and 3.0-A resolution, respectively.
14754895	5	48	theme	-ethylamino	991:1001	arg1	inhibitor					910:918	The potent inhibitor MLN-4760	899:927	The potent inhibitor MLN-4760 ((S,S)-2-[1-carboxy-2-[3-(3,5-dichlorobenzyl)-3H-imidazol4-yl]-ethylamino]-4-methylpentanoic acid)	899:1026	The potent inhibitor MLN-4760 ((S,S)-2-[1-carboxy-2-[3-(3,5-dichlorobenzyl)-3H-imidazol4-yl]-ethylamino]-4-methylpentanoic acid) makes key binding interactions within the active site and offers insights regarding the action of residues involved in catalysis and substrate specificity.
14754895	5	48	theme	-ethylamino	991:1001	arg1	acid					1022:1025	(S,S)-2-[1-carboxy-2-[3-(3,5-dichlorobenzyl)-3H-imidazol4-yl]-ethylamino]-4-methylpentanoic acid	930:1025	acid	1022:1025	The potent inhibitor MLN-4760 ((S,S)-2-[1-carboxy-2-[3-(3,5-dichlorobenzyl)-3H-imidazol4-yl]-ethylamino]-4-methylpentanoic acid) makes key binding interactions within the active site and offers insights regarding the action of residues involved in catalysis and substrate specificity.
14754895	1	49	theme	angiotensin-converting	109:130	arg1	protein					207:213	a type I integral membrane protein	180:213	a type I integral membrane protein of 805 amino acids that contains one HEXXH + E zinc-binding consensus sequence	180:292	The angiotensin-converting enzyme (ACE)-related carboxypeptidase, ACE2, is a type I integral membrane protein of 805 amino acids that contains one HEXXH + E zinc-binding consensus sequence.
14754895	1	49	theme	angiotensin-converting	109:130	arg1	ACE					140:142	ACE	140:142	ACE	140:142	The angiotensin-converting enzyme (ACE)-related carboxypeptidase, ACE2, is a type I integral membrane protein of 805 amino acids that contains one HEXXH + E zinc-binding consensus sequence.
14754895	1	49	theme	angiotensin-converting	109:130	arg1	enzyme					132:137	The angiotensin-converting enzyme	105:137	The angiotensin-converting enzyme (ACE)	105:143	The angiotensin-converting enzyme (ACE)-related carboxypeptidase, ACE2, is a type I integral membrane protein of 805 amino acids that contains one HEXXH + E zinc-binding consensus sequence.
14754895	1	49	theme	angiotensin-converting	109:130	arg1	ACE2					171:174	ACE2	171:174	ACE2	171:174	The angiotensin-converting enzyme (ACE)-related carboxypeptidase, ACE2, is a type I integral membrane protein of 805 amino acids that contains one HEXXH + E zinc-binding consensus sequence.
14754895	0	50	theme	hinge-bending	37:49	arg1	motion					51:56	a large hinge-bending motion	29:56	a large hinge-bending motion important for inhibitor binding and catalysis	29:102	ACE2 X-ray structures reveal a large hinge-bending motion important for inhibitor binding and catalysis.
14754895	5	51	theme	residues	1126:1133	arg1	action					1116:1121	the action	1112:1121	the action of residues involved in catalysis and substrate specificity	1112:1181	The potent inhibitor MLN-4760 ((S,S)-2-[1-carboxy-2-[3-(3,5-dichlorobenzyl)-3H-imidazol4-yl]-ethylamino]-4-methylpentanoic acid) makes key binding interactions within the active site and offers insights regarding the action of residues involved in catalysis and substrate specificity.
14754895	5	52	theme	-4-methylpentanoic	1003:1020	arg1	inhibitor					910:918	The potent inhibitor MLN-4760	899:927	The potent inhibitor MLN-4760 ((S,S)-2-[1-carboxy-2-[3-(3,5-dichlorobenzyl)-3H-imidazol4-yl]-ethylamino]-4-methylpentanoic acid)	899:1026	The potent inhibitor MLN-4760 ((S,S)-2-[1-carboxy-2-[3-(3,5-dichlorobenzyl)-3H-imidazol4-yl]-ethylamino]-4-methylpentanoic acid) makes key binding interactions within the active site and offers insights regarding the action of residues involved in catalysis and substrate specificity.
14754895	5	52	theme	-4-methylpentanoic	1003:1020	arg1	acid					1022:1025	(S,S)-2-[1-carboxy-2-[3-(3,5-dichlorobenzyl)-3H-imidazol4-yl]-ethylamino]-4-methylpentanoic acid	930:1025	acid	1022:1025	The potent inhibitor MLN-4760 ((S,S)-2-[1-carboxy-2-[3-(3,5-dichlorobenzyl)-3H-imidazol4-yl]-ethylamino]-4-methylpentanoic acid) makes key binding interactions within the active site and offers insights regarding the action of residues involved in catalysis and substrate specificity.
14754895	6	53	theme	active	1190:1195	arg1	substitutions					1210:1222	A few active site residue substitutions	1184:1222	A few active site residue substitutions in ACE2 relative to ACE	1184:1246	A few active site residue substitutions in ACE2 relative to ACE appear to eliminate the S(2)' substrate-binding subsite and account for the observed reactivity change from the peptidyl dipeptidase activity of ACE to the carboxypeptidase activity of ACE2.
14754895	4	54	theme	catalytic	768:776	arg1	subdomain					778:786	one catalytic subdomain	764:786	one catalytic subdomain	764:786	Comparison of these structures revealed a large inhibitor-dependent hinge-bending movement of one catalytic subdomain relative to the other ( approximately 16 degrees ) that brings important residues into position for catalysis.
14754895	6	55	theme	S	1272:1272	arg1	subsite					1296:1302	the S(2)' substrate-binding subsite	1268:1302	the S(2)' substrate-binding subsite	1268:1302	A few active site residue substitutions in ACE2 relative to ACE appear to eliminate the S(2)' substrate-binding subsite and account for the observed reactivity change from the peptidyl dipeptidase activity of ACE to the carboxypeptidase activity of ACE2.
14754895	5	56	theme	-2-[1-carboxy-2-[3-	935:953	arg1	inhibitor					910:918	The potent inhibitor MLN-4760	899:927	The potent inhibitor MLN-4760 ((S,S)-2-[1-carboxy-2-[3-(3,5-dichlorobenzyl)-3H-imidazol4-yl]-ethylamino]-4-methylpentanoic acid)	899:1026	The potent inhibitor MLN-4760 ((S,S)-2-[1-carboxy-2-[3-(3,5-dichlorobenzyl)-3H-imidazol4-yl]-ethylamino]-4-methylpentanoic acid) makes key binding interactions within the active site and offers insights regarding the action of residues involved in catalysis and substrate specificity.
14754895	5	56	theme	-2-[1-carboxy-2-[3-	935:953	arg1	acid					1022:1025	(S,S)-2-[1-carboxy-2-[3-(3,5-dichlorobenzyl)-3H-imidazol4-yl]-ethylamino]-4-methylpentanoic acid	930:1025	acid	1022:1025	The potent inhibitor MLN-4760 ((S,S)-2-[1-carboxy-2-[3-(3,5-dichlorobenzyl)-3H-imidazol4-yl]-ethylamino]-4-methylpentanoic acid) makes key binding interactions within the active site and offers insights regarding the action of residues involved in catalysis and substrate specificity.
14754895	3	57	theme	forms	574:578	arg1	structures					529:538	the first crystal structures	511:538	the first crystal structures of the native and inhibitor-bound forms of the ACE2 extracellular domains	511:612	To gain further insights into this enzyme, the first crystal structures of the native and inhibitor-bound forms of the ACE2 extracellular domains were solved to 2.2- and 3.0-A resolution, respectively.
14754895	4	58	theme	relative	788:795	arg1	movement					752:759	a large inhibitor-dependent hinge-bending movement	710:759	a large inhibitor-dependent hinge-bending movement of one catalytic subdomain relative to the other ( approximately 16 degrees ) that brings important residues into position for catalysis	710:896	Comparison of these structures revealed a large inhibitor-dependent hinge-bending movement of one catalytic subdomain relative to the other ( approximately 16 degrees ) that brings important residues into position for catalysis.
14754895	4	59	theme	hinge-bending	738:750	arg1	movement					752:759	a large inhibitor-dependent hinge-bending movement	710:759	a large inhibitor-dependent hinge-bending movement of one catalytic subdomain relative to the other ( approximately 16 degrees ) that brings important residues into position for catalysis	710:896	Comparison of these structures revealed a large inhibitor-dependent hinge-bending movement of one catalytic subdomain relative to the other ( approximately 16 degrees ) that brings important residues into position for catalysis.
14754895	6	60	theme	few	1186:1188	arg1	substitutions					1210:1222	A few active site residue substitutions	1184:1222	A few active site residue substitutions in ACE2 relative to ACE	1184:1246	A few active site residue substitutions in ACE2 relative to ACE appear to eliminate the S(2)' substrate-binding subsite and account for the observed reactivity change from the peptidyl dipeptidase activity of ACE to the carboxypeptidase activity of ACE2.
14754895	1	61	contain	contains	239:246	arg2	HEXXH					252:256	one HEXXH + E zinc-binding consensus sequence	248:292	HEXXH	252:256	The angiotensin-converting enzyme (ACE)-related carboxypeptidase, ACE2, is a type I integral membrane protein of 805 amino acids that contains one HEXXH + E zinc-binding consensus sequence.
14754895	1	61	contain	contains	239:246	arg1	protein					207:213	a type I integral membrane protein	180:213	a type I integral membrane protein of 805 amino acids that contains one HEXXH + E zinc-binding consensus sequence	180:292	The angiotensin-converting enzyme (ACE)-related carboxypeptidase, ACE2, is a type I integral membrane protein of 805 amino acids that contains one HEXXH + E zinc-binding consensus sequence.
14754895	1	61	contain	contains	239:246	arg2	sequence					285:292	one HEXXH + E zinc-binding consensus sequence	248:292	sequence	285:292	The angiotensin-converting enzyme (ACE)-related carboxypeptidase, ACE2, is a type I integral membrane protein of 805 amino acids that contains one HEXXH + E zinc-binding consensus sequence.
14754895	1	61	contain	contains	239:246	arg1	enzyme					132:137	The angiotensin-converting enzyme	105:137	The angiotensin-converting enzyme (ACE)	105:143	The angiotensin-converting enzyme (ACE)-related carboxypeptidase, ACE2, is a type I integral membrane protein of 805 amino acids that contains one HEXXH + E zinc-binding consensus sequence.
14754895	5	62	theme	binding	1038:1044	arg1	interactions					1046:1057	key binding interactions	1034:1057	key binding interactions within the active site	1034:1080	The potent inhibitor MLN-4760 ((S,S)-2-[1-carboxy-2-[3-(3,5-dichlorobenzyl)-3H-imidazol4-yl]-ethylamino]-4-methylpentanoic acid) makes key binding interactions within the active site and offers insights regarding the action of residues involved in catalysis and substrate specificity.
14754895	3	63	theme	further	476:482	arg1	insights					484:491	further insights	476:491	further insights into this enzyme	476:508	To gain further insights into this enzyme, the first crystal structures of the native and inhibitor-bound forms of the ACE2 extracellular domains were solved to 2.2- and 3.0-A resolution, respectively.
14754895	6	64	from	substitutions	1210:1222	arg1	ACE2					1227:1230	ACE2	1227:1230	ACE2 relative to ACE	1227:1246	A few active site residue substitutions in ACE2 relative to ACE appear to eliminate the S(2)' substrate-binding subsite and account for the observed reactivity change from the peptidyl dipeptidase activity of ACE to the carboxypeptidase activity of ACE2.
14754895	4	65	theme	subdomain	778:786	arg1	movement					752:759	a large inhibitor-dependent hinge-bending movement	710:759	a large inhibitor-dependent hinge-bending movement of one catalytic subdomain relative to the other ( approximately 16 degrees ) that brings important residues into position for catalysis	710:896	Comparison of these structures revealed a large inhibitor-dependent hinge-bending movement of one catalytic subdomain relative to the other ( approximately 16 degrees ) that brings important residues into position for catalysis.
14754895	2	66	theme	heart	341:345	arg1	function					347:354	heart function	341:354	heart function	341:354	ACE2 has been implicated in the regulation of heart function and also as a functional receptor for the coronavirus that causes the severe acute respiratory syndrome (SARS).
14754895	0	67	theme	important	58:66	arg1	motion					51:56	a large hinge-bending motion	29:56	a large hinge-bending motion important for inhibitor binding and catalysis	29:102	ACE2 X-ray structures reveal a large hinge-bending motion important for inhibitor binding and catalysis.
14754895	3	68	theme	inhibitor-bound	558:572	arg1	forms					574:578	the native and inhibitor-bound forms	543:578	the native and inhibitor-bound forms of the ACE2 extracellular domains	543:612	To gain further insights into this enzyme, the first crystal structures of the native and inhibitor-bound forms of the ACE2 extracellular domains were solved to 2.2- and 3.0-A resolution, respectively.
14754895	1	69	theme	-related	144:151	arg1	carboxypeptidase					153:168	-related carboxypeptidase	144:168	-related carboxypeptidase	144:168	The angiotensin-converting enzyme (ACE)-related carboxypeptidase, ACE2, is a type I integral membrane protein of 805 amino acids that contains one HEXXH + E zinc-binding consensus sequence.
14754895	6	70	theme	ACE2	1433:1436	arg1	activity					1421:1428	the carboxypeptidase activity	1400:1428	the carboxypeptidase activity of ACE2	1400:1436	A few active site residue substitutions in ACE2 relative to ACE appear to eliminate the S(2)' substrate-binding subsite and account for the observed reactivity change from the peptidyl dipeptidase activity of ACE to the carboxypeptidase activity of ACE2.
14754895	1	71	theme	amino	222:226	arg1	acids					228:232	805 amino acids	218:232	805 amino acids	218:232	The angiotensin-converting enzyme (ACE)-related carboxypeptidase, ACE2, is a type I integral membrane protein of 805 amino acids that contains one HEXXH + E zinc-binding consensus sequence.
11459848	2	0	from	%	199:199	arg1	bone					241:244	bone	241:244	bone	241:244	Human bone sialoprotein (BSP) comprises 15% of the total noncollagenous proteins in bone and is thought to be involved in bone mineralization and remodeling.
11459848	7	1	theme	complex-type	808:819	arg1	N-glycans					821:829	10 different complex-type N-glycans	795:829	10 different complex-type N-glycans on both proteins	795:846	Carbohydrate analysis revealed 10 different complex-type N-glycans on both proteins and eight different O-glycans on recombinant BSP, four of those were found on bone-derived BSP.
11459848	5	2	theme	average	653:659	arg1	mass					661:664	an average mass	650:664	an average mass of 49 kDa and for recombinant BSP 57 kDa	650:705	Mass spectrometry of bone-derived BSP revealed an average mass of 49 kDa and for recombinant BSP 57 kDa.
11459848	3	3	from	development	375:385	arg1	cancer					360:365	breast cancer	353:365	breast cancer	353:365	Recent data suggest a role for BSP in breast cancer and the development of bone metastases.
11459848	7	4	theme	those	906:910	arg1	those					906:910	those	906:910	those	906:910	Carbohydrate analysis revealed 10 different complex-type N-glycans on both proteins and eight different O-glycans on recombinant BSP, four of those were found on bone-derived BSP.
11459848	7	4	theme	those	906:910	arg1	four					898:901	four	898:901	four	898:901	Carbohydrate analysis revealed 10 different complex-type N-glycans on both proteins and eight different O-glycans on recombinant BSP, four of those were found on bone-derived BSP.
11459848	11	5	theme	recombinant	1301:1311	arg1	BSP					1313:1315	recombinant BSP	1301:1315	recombinant BSP	1301:1315	The affinity for hydroxyapatite was higher for bone-derived BSP than for recombinant BSP.
11459848	8	6	theme	protein	1032:1038	arg1	terminus					1016:1023	the C terminus	1010:1023	the C terminus of the protein free of glycans	1010:1054	We could identify eight threonines modified by O-glycans, leaving the C terminus of the protein free of glycans.
11459848	5	7	theme	Mass	603:606	arg1	spectrometry					608:619	Mass spectrometry	603:619	Mass spectrometry of bone-derived BSP	603:639	Mass spectrometry of bone-derived BSP revealed an average mass of 49 kDa and for recombinant BSP 57 kDa.
11459848	9	8	theme	recombinant	1061:1071	arg1	protein					1073:1079	The recombinant protein	1057:1079	The recombinant protein	1057:1079	The recombinant protein showed similar secondary structures as bone-derived BSP.
11459848	10	9	theme	thread-like	1205:1215	arg1	structure					1217:1225	a thread-like structure	1203:1225	a thread-like structure	1203:1225	BSP was visualized in electron microscopy as a globule linked to a thread-like structure.
11459848	3	10	theme	breast	353:358	arg1	cancer					360:365	breast cancer	353:365	breast cancer	353:365	Recent data suggest a role for BSP in breast cancer and the development of bone metastases.
11459848	4	11	theme	cell	463:466	arg1	line					468:471	a human cell line	455:471	a human cell line	455:471	We have produced full-length recombinant BSP in a human cell line and purified the protein from human bone retaining the native structure with proper folding and post-translational modifications.
11459848	8	12	theme	free	1040:1043	arg1	protein					1032:1038	the protein	1028:1038	the protein free of glycans	1028:1054	We could identify eight threonines modified by O-glycans, leaving the C terminus of the protein free of glycans.
11459848	7	13	from	N-glycans	821:829	arg1	proteins					839:846	both proteins	834:846	both proteins	834:846	Carbohydrate analysis revealed 10 different complex-type N-glycans on both proteins and eight different O-glycans on recombinant BSP, four of those were found on bone-derived BSP.
11459848	7	13	from	N-glycans	821:829	arg1	BSP					893:895	recombinant BSP	881:895	recombinant BSP	881:895	Carbohydrate analysis revealed 10 different complex-type N-glycans on both proteins and eight different O-glycans on recombinant BSP, four of those were found on bone-derived BSP.
11459848	2	14	theme	bone	279:282	arg1	mineralization					284:297	bone mineralization	279:297	bone mineralization	279:297	Human bone sialoprotein (BSP) comprises 15% of the total noncollagenous proteins in bone and is thought to be involved in bone mineralization and remodeling.
11459848	7	15	theme	recombinant	881:891	arg1	BSP					893:895	recombinant BSP	881:895	recombinant BSP	881:895	Carbohydrate analysis revealed 10 different complex-type N-glycans on both proteins and eight different O-glycans on recombinant BSP, four of those were found on bone-derived BSP.
11459848	4	16	theme	post-translational	569:586	arg1	modifications					588:600	post-translational modifications	569:600	post-translational modifications	569:600	We have produced full-length recombinant BSP in a human cell line and purified the protein from human bone retaining the native structure with proper folding and post-translational modifications.
11459848	4	17	theme	human	457:461	arg1	line					468:471	a human cell line	455:471	a human cell line	455:471	We have produced full-length recombinant BSP in a human cell line and purified the protein from human bone retaining the native structure with proper folding and post-translational modifications.
11459848	5	18	theme	bone-derived	624:635	arg1	BSP					637:639	bone-derived BSP	624:639	bone-derived BSP	624:639	Mass spectrometry of bone-derived BSP revealed an average mass of 49 kDa and for recombinant BSP 57 kDa.
11459848	1	19	theme	Functional	85:94	arg1	implications					96:107	Functional implications	85:107	Functional implications for cell attachment and hydroxyapatite binding.	85:155	Functional implications for cell attachment and hydroxyapatite binding.
11459848	12	20	theme	adhesion	1323:1330	arg1	assays					1332:1337	Cell adhesion assays	1318:1337	Cell adhesion assays	1318:1337	Cell adhesion assays showed that the binding of BSP to cells can be reversibly diminished by denaturation.
11459848	0	21	theme	bone-derived	53:64	arg1	sialoprotein					71:82	human recombinant and bone-derived bone sialoprotein	31:82	human recombinant and bone-derived bone sialoprotein	31:82	Structural characterization of human recombinant and bone-derived bone sialoprotein.
11459848	5	22	theme	BSP	637:639	arg1	spectrometry					608:619	Mass spectrometry	603:619	Mass spectrometry of bone-derived BSP	603:639	Mass spectrometry of bone-derived BSP revealed an average mass of 49 kDa and for recombinant BSP 57 kDa.
11459848	8	23	theme	C	1014:1014	arg1	terminus					1016:1023	the C terminus	1010:1023	the C terminus of the protein free of glycans	1010:1054	We could identify eight threonines modified by O-glycans, leaving the C terminus of the protein free of glycans.
11459848	9	24	theme	similar	1088:1094	arg1	structures					1106:1115	similar secondary structures	1088:1115	similar secondary structures	1088:1115	The recombinant protein showed similar secondary structures as bone-derived BSP.
11459848	2	25	theme	bone	163:166	arg1	sialoprotein					168:179	Human bone sialoprotein	157:179	Human bone sialoprotein (BSP)	157:185	Human bone sialoprotein (BSP) comprises 15% of the total noncollagenous proteins in bone and is thought to be involved in bone mineralization and remodeling.
11459848	2	25	theme	bone	163:166	arg1	BSP					182:184	BSP	182:184	BSP	182:184	Human bone sialoprotein (BSP) comprises 15% of the total noncollagenous proteins in bone and is thought to be involved in bone mineralization and remodeling.
11459848	7	26	located	found	917:921	arg1	BSP					939:941	bone-derived BSP	926:941	bone-derived BSP	926:941	Carbohydrate analysis revealed 10 different complex-type N-glycans on both proteins and eight different O-glycans on recombinant BSP, four of those were found on bone-derived BSP.
11459848	7	26	located	found	917:921	arg2	those					906:910	those	906:910	those	906:910	Carbohydrate analysis revealed 10 different complex-type N-glycans on both proteins and eight different O-glycans on recombinant BSP, four of those were found on bone-derived BSP.
11459848	7	26	located	found	917:921	arg2	four					898:901	four	898:901	four	898:901	Carbohydrate analysis revealed 10 different complex-type N-glycans on both proteins and eight different O-glycans on recombinant BSP, four of those were found on bone-derived BSP.
11459848	0	27	link	bone-derived	53:64	arg1	sialoprotein					71:82	human recombinant and bone-derived bone sialoprotein	31:82	human recombinant and bone-derived bone sialoprotein	31:82	Structural characterization of human recombinant and bone-derived bone sialoprotein.
11459848	9	28	theme	secondary	1096:1104	arg1	structures					1106:1115	similar secondary structures	1088:1115	similar secondary structures	1088:1115	The recombinant protein showed similar secondary structures as bone-derived BSP.
11459848	5	29	link	bone-derived	624:635	arg1	BSP					637:639	bone-derived BSP	624:639	bone-derived BSP	624:639	Mass spectrometry of bone-derived BSP revealed an average mass of 49 kDa and for recombinant BSP 57 kDa.
11459848	0	30	theme	Structural	0:9	arg1	characterization					11:26	Structural characterization	0:26	Structural characterization of human recombinant and bone-derived bone sialoprotein.	0:83	Structural characterization of human recombinant and bone-derived bone sialoprotein.
11459848	7	31	link	bone-derived	926:937	arg1	BSP					939:941	bone-derived BSP	926:941	bone-derived BSP	926:941	Carbohydrate analysis revealed 10 different complex-type N-glycans on both proteins and eight different O-glycans on recombinant BSP, four of those were found on bone-derived BSP.
11459848	1	32	theme	cell	113:116	arg1	attachment					118:127	cell attachment	113:127	cell attachment	113:127	Functional implications for cell attachment and hydroxyapatite binding.
11459848	10	33	attach	linked	1193:1198	arg1	structure					1217:1225	a thread-like structure	1203:1225	a thread-like structure	1203:1225	BSP was visualized in electron microscopy as a globule linked to a thread-like structure.
11459848	10	33	attach	linked	1193:1198	arg2	BSP					1138:1140	BSP	1138:1140	BSP	1138:1140	BSP was visualized in electron microscopy as a globule linked to a thread-like structure.
11459848	10	33	attach	linked	1193:1198	arg2	globule					1185:1191	globule	1185:1191	globule	1185:1191	BSP was visualized in electron microscopy as a globule linked to a thread-like structure.
11459848	0	34	theme	human	31:35	arg1	sialoprotein					71:82	human recombinant and bone-derived bone sialoprotein	31:82	human recombinant and bone-derived bone sialoprotein	31:82	Structural characterization of human recombinant and bone-derived bone sialoprotein.
11459848	4	35	theme	native	528:533	arg1	structure					535:543	the native structure	524:543	the native structure with proper folding and post-translational modifications	524:600	We have produced full-length recombinant BSP in a human cell line and purified the protein from human bone retaining the native structure with proper folding and post-translational modifications.
11459848	12	36	theme	BSP	1366:1368	arg1	binding					1355:1361	the binding	1351:1361	the binding of BSP to cells	1351:1377	Cell adhesion assays showed that the binding of BSP to cells can be reversibly diminished by denaturation.
11459848	4	37	from	bone	509:512	arg1	protein					490:496	the protein	486:496	the protein from human bone	486:512	We have produced full-length recombinant BSP in a human cell line and purified the protein from human bone retaining the native structure with proper folding and post-translational modifications.
11459848	7	38	theme	different	858:866	arg1	O-glycans					868:876	eight different O-glycans	852:876	eight different O-glycans on recombinant BSP	852:895	Carbohydrate analysis revealed 10 different complex-type N-glycans on both proteins and eight different O-glycans on recombinant BSP, four of those were found on bone-derived BSP.
11459848	5	39	dep	mass	661:664	arg1	kDa					703:705	57 kDa	700:705	an average mass of 49 kDa and for recombinant BSP 57 kDa	650:705	Mass spectrometry of bone-derived BSP revealed an average mass of 49 kDa and for recombinant BSP 57 kDa.
11459848	4	40	theme	proper	550:555	arg1	folding					557:563	proper folding	550:563	proper folding	550:563	We have produced full-length recombinant BSP in a human cell line and purified the protein from human bone retaining the native structure with proper folding and post-translational modifications.
11459848	4	41	with	structure	535:543	arg1	folding					557:563	proper folding	550:563	proper folding	550:563	We have produced full-length recombinant BSP in a human cell line and purified the protein from human bone retaining the native structure with proper folding and post-translational modifications.
11459848	4	41	with	structure	535:543	arg1	modifications					588:600	post-translational modifications	569:600	post-translational modifications	569:600	We have produced full-length recombinant BSP in a human cell line and purified the protein from human bone retaining the native structure with proper folding and post-translational modifications.
11459848	9	42	theme	bone-derived	1120:1131	arg1	BSP					1133:1135	bone-derived BSP	1120:1135	bone-derived BSP	1120:1135	The recombinant protein showed similar secondary structures as bone-derived BSP.
11459848	3	43	theme	metastases	395:404	arg1	role					337:340	a role	335:340	a role for BSP in breast cancer	335:365	Recent data suggest a role for BSP in breast cancer and the development of bone metastases.
11459848	3	43	theme	metastases	395:404	arg1	development					375:385	the development	371:385	the development of bone metastases	371:404	Recent data suggest a role for BSP in breast cancer and the development of bone metastases.
11459848	4	44	from	BSP	448:450	arg1	line					468:471	a human cell line	455:471	a human cell line	455:471	We have produced full-length recombinant BSP in a human cell line and purified the protein from human bone retaining the native structure with proper folding and post-translational modifications.
11459848	4	45	theme	recombinant	436:446	arg1	BSP					448:450	full-length recombinant BSP	424:450	full-length recombinant BSP in a human cell line	424:471	We have produced full-length recombinant BSP in a human cell line and purified the protein from human bone retaining the native structure with proper folding and post-translational modifications.
11459848	11	46	theme	bone-derived	1275:1286	arg1	BSP					1288:1290	bone-derived BSP	1275:1290	bone-derived BSP	1275:1290	The affinity for hydroxyapatite was higher for bone-derived BSP than for recombinant BSP.
11459848	12	47	theme	Cell	1318:1321	arg1	assays					1332:1337	Cell adhesion assays	1318:1337	Cell adhesion assays	1318:1337	Cell adhesion assays showed that the binding of BSP to cells can be reversibly diminished by denaturation.
11459848	0	48	theme	recombinant	37:47	arg1	sialoprotein					71:82	human recombinant and bone-derived bone sialoprotein	31:82	human recombinant and bone-derived bone sialoprotein	31:82	Structural characterization of human recombinant and bone-derived bone sialoprotein.
11459848	0	49	theme	bone	66:69	arg1	sialoprotein					71:82	human recombinant and bone-derived bone sialoprotein	31:82	human recombinant and bone-derived bone sialoprotein	31:82	Structural characterization of human recombinant and bone-derived bone sialoprotein.
11459848	4	50	theme	human	503:507	arg1	bone					509:512	human bone	503:512	human bone	503:512	We have produced full-length recombinant BSP in a human cell line and purified the protein from human bone retaining the native structure with proper folding and post-translational modifications.
11459848	5	51	theme	kDa	672:674	arg1	mass					661:664	an average mass	650:664	an average mass of 49 kDa and for recombinant BSP 57 kDa	650:705	Mass spectrometry of bone-derived BSP revealed an average mass of 49 kDa and for recombinant BSP 57 kDa.
11459848	1	52	theme	hydroxyapatite	133:146	arg1	binding					148:154	hydroxyapatite binding	133:154	hydroxyapatite binding	133:154	Functional implications for cell attachment and hydroxyapatite binding.
11459848	3	53	theme	bone	390:393	arg1	metastases					395:404	bone metastases	390:404	bone metastases	390:404	Recent data suggest a role for BSP in breast cancer and the development of bone metastases.
11459848	10	54	theme	electron	1160:1167	arg1	microscopy					1169:1178	electron microscopy	1160:1178	electron microscopy	1160:1178	BSP was visualized in electron microscopy as a globule linked to a thread-like structure.
11459848	3	55	theme	Recent	315:320	arg1	data					322:325	Recent data	315:325	Recent data	315:325	Recent data suggest a role for BSP in breast cancer and the development of bone metastases.
11459848	2	56	theme	noncollagenous	214:227	arg1	proteins					229:236	the total noncollagenous proteins	204:236	the total noncollagenous proteins	204:236	Human bone sialoprotein (BSP) comprises 15% of the total noncollagenous proteins in bone and is thought to be involved in bone mineralization and remodeling.
11459848	2	57	theme	proteins	229:236	arg1	proteins					229:236	the total noncollagenous proteins	204:236	the total noncollagenous proteins	204:236	Human bone sialoprotein (BSP) comprises 15% of the total noncollagenous proteins in bone and is thought to be involved in bone mineralization and remodeling.
11459848	2	57	theme	proteins	229:236	arg1	%					199:199	15%	197:199	15% of the total noncollagenous proteins in bone	197:244	Human bone sialoprotein (BSP) comprises 15% of the total noncollagenous proteins in bone and is thought to be involved in bone mineralization and remodeling.
11459848	8	58	theme	glycans	1048:1054	arg1	free					1040:1043	free	1040:1043	free	1040:1043	We could identify eight threonines modified by O-glycans, leaving the C terminus of the protein free of glycans.
11459848	2	59	theme	total	208:212	arg1	proteins					229:236	the total noncollagenous proteins	204:236	the total noncollagenous proteins	204:236	Human bone sialoprotein (BSP) comprises 15% of the total noncollagenous proteins in bone and is thought to be involved in bone mineralization and remodeling.
11459848	7	60	from	O-glycans	868:876	arg1	proteins					839:846	both proteins	834:846	both proteins	834:846	Carbohydrate analysis revealed 10 different complex-type N-glycans on both proteins and eight different O-glycans on recombinant BSP, four of those were found on bone-derived BSP.
11459848	7	60	from	O-glycans	868:876	arg1	BSP					893:895	recombinant BSP	881:895	recombinant BSP	881:895	Carbohydrate analysis revealed 10 different complex-type N-glycans on both proteins and eight different O-glycans on recombinant BSP, four of those were found on bone-derived BSP.
11459848	7	61	theme	bone-derived	926:937	arg1	BSP					939:941	bone-derived BSP	926:941	bone-derived BSP	926:941	Carbohydrate analysis revealed 10 different complex-type N-glycans on both proteins and eight different O-glycans on recombinant BSP, four of those were found on bone-derived BSP.
11459848	5	62	theme	recombinant	684:694	arg1	BSP					696:698	recombinant BSP	684:698	recombinant BSP	684:698	Mass spectrometry of bone-derived BSP revealed an average mass of 49 kDa and for recombinant BSP 57 kDa.
11459848	4	63	theme	full-length	424:434	arg1	BSP					448:450	full-length recombinant BSP	424:450	full-length recombinant BSP in a human cell line	424:471	We have produced full-length recombinant BSP in a human cell line and purified the protein from human bone retaining the native structure with proper folding and post-translational modifications.
11459848	11	64	link	bone-derived	1275:1286	arg1	BSP					1288:1290	bone-derived BSP	1275:1290	bone-derived BSP	1275:1290	The affinity for hydroxyapatite was higher for bone-derived BSP than for recombinant BSP.
11459848	7	65	theme	Carbohydrate	764:775	arg1	analysis					777:784	Carbohydrate analysis	764:784	Carbohydrate analysis	764:784	Carbohydrate analysis revealed 10 different complex-type N-glycans on both proteins and eight different O-glycans on recombinant BSP, four of those were found on bone-derived BSP.
11459848	3	66	from	role	337:340	arg1	cancer					360:365	breast cancer	353:365	breast cancer	353:365	Recent data suggest a role for BSP in breast cancer and the development of bone metastases.
11459848	0	67	theme	sialoprotein	71:82	arg1	characterization					11:26	Structural characterization	0:26	Structural characterization of human recombinant and bone-derived bone sialoprotein.	0:83	Structural characterization of human recombinant and bone-derived bone sialoprotein.
11459848	2	68	theme	Human	157:161	arg1	sialoprotein					168:179	Human bone sialoprotein	157:179	Human bone sialoprotein (BSP)	157:185	Human bone sialoprotein (BSP) comprises 15% of the total noncollagenous proteins in bone and is thought to be involved in bone mineralization and remodeling.
11459848	2	68	theme	Human	157:161	arg1	BSP					182:184	BSP	182:184	BSP	182:184	Human bone sialoprotein (BSP) comprises 15% of the total noncollagenous proteins in bone and is thought to be involved in bone mineralization and remodeling.
11459848	6	69	theme	post-translational	712:729	arg1	modifications					731:743	The post-translational modifications	708:743	The post-translational modifications	708:743	The post-translational modifications contribute 30-40%.
11459848	9	70	link	bone-derived	1120:1131	arg1	BSP					1133:1135	bone-derived BSP	1120:1135	bone-derived BSP	1120:1135	The recombinant protein showed similar secondary structures as bone-derived BSP.
11459848	7	71	theme	different	798:806	arg1	N-glycans					821:829	10 different complex-type N-glycans	795:829	10 different complex-type N-glycans on both proteins	795:846	Carbohydrate analysis revealed 10 different complex-type N-glycans on both proteins and eight different O-glycans on recombinant BSP, four of those were found on bone-derived BSP.
7947762	2	0	from	ring	343:346	arg1	position					377:384	position 7	377:386	position 7 of human RNase Us	377:404	An aldohexopyranosyl residue was found to be linked via a C-C bond to the indole ring of the tryptophan residue at position 7 of human RNase Us.
7947762	3	1	theme	spectrometric	412:424	arg1	analysis					426:433	Mass spectrometric analysis	407:433	Mass spectrometric analysis of peptides containing this residue	407:469	Mass spectrometric analysis of peptides containing this residue showed a molecular mass 162 Da higher than that expected for tryptophan.
7947762	2	2	theme	RNase	397:401	arg1	position					377:384	position 7	377:386	position 7 of human RNase Us	377:404	An aldohexopyranosyl residue was found to be linked via a C-C bond to the indole ring of the tryptophan residue at position 7 of human RNase Us.
7947762	5	3	attach	linked	917:922	arg2	residue					891:897	an aldohexopyranosyl residue	870:897	an aldohexopyranosyl residue	870:897	1H and 13C NMR spectroscopic data confirmed this inference and unequivocally demonstrated the substituent to be an aldohexopyranosyl residue, C-glycosidically linked to the C2 atom of the indole.
7947762	5	3	attach	linked	917:922	arg1	atom					934:937	the C2 atom	927:937	the C2 atom of the indole	927:951	1H and 13C NMR spectroscopic data confirmed this inference and unequivocally demonstrated the substituent to be an aldohexopyranosyl residue, C-glycosidically linked to the C2 atom of the indole.
7947762	5	4	theme	aldohexopyranosyl	873:889	arg1	residue					891:897	an aldohexopyranosyl residue	870:897	an aldohexopyranosyl residue	870:897	1H and 13C NMR spectroscopic data confirmed this inference and unequivocally demonstrated the substituent to be an aldohexopyranosyl residue, C-glycosidically linked to the C2 atom of the indole.
7947762	4	5	theme	direct	671:676	arg1	attachment					678:687	a direct attachment	669:687	a direct attachment of a hexose residue to a C-position of the tryptophan indole moiety	669:755	The fragmentation pattern of the modified amino acid side chain was reminiscent of that of aromatic C-glycosides, suggesting a direct attachment of a hexose residue to a C-position of the tryptophan indole moiety.
7947762	0	6	theme	New	0:2	arg1	type					4:7	New type	0:7	New type of linkage between a carbohydrate and a protein: C-glycosylation of a specific tryptophan residue in human RNase Us.	0:124	New type of linkage between a carbohydrate and a protein: C-glycosylation of a specific tryptophan residue in human RNase Us.
7947762	1	7	theme	modified	217:224	arg1	chain					231:235	the rarely modified side chain	206:235	the rarely modified side chain of a tryptophan residue	206:259	We report a new type of linkage between a carbohydrate and a protein, involving the rarely modified side chain of a tryptophan residue.
7947762	0	8	theme	tryptophan	88:97	arg1	residue					99:105	a specific tryptophan residue	77:105	a specific tryptophan residue	77:105	New type of linkage between a carbohydrate and a protein: C-glycosylation of a specific tryptophan residue in human RNase Us.
7947762	2	9	from	position	377:384	arg1	residue					366:372	the tryptophan residue	351:372	the tryptophan residue at position 7 of human RNase Us	351:404	An aldohexopyranosyl residue was found to be linked via a C-C bond to the indole ring of the tryptophan residue at position 7 of human RNase Us.
7947762	2	9	from	position	377:384	arg1	ring					343:346	the indole ring	332:346	the indole ring of the tryptophan residue at position 7 of human RNase Us	332:404	An aldohexopyranosyl residue was found to be linked via a C-C bond to the indole ring of the tryptophan residue at position 7 of human RNase Us.
7947762	4	10	theme	moiety	750:755	arg1	C-position					714:723	a C-position	712:723	a C-position of the tryptophan indole moiety	712:755	The fragmentation pattern of the modified amino acid side chain was reminiscent of that of aromatic C-glycosides, suggesting a direct attachment of a hexose residue to a C-position of the tryptophan indole moiety.
7947762	6	11	theme	acid	1060:1063	arg1	chain					1070:1074	an amino acid side chain	1051:1074	an amino acid side chain	1051:1074	This mode of attachment differs from the ones known so far, in which carbohydrates are linked to an amino acid side chain by N- or O-glycosidic bonds.
7947762	4	12	theme	acid	592:595	arg1	chain					602:606	the modified amino acid side chain	573:606	the modified amino acid side chain	573:606	The fragmentation pattern of the modified amino acid side chain was reminiscent of that of aromatic C-glycosides, suggesting a direct attachment of a hexose residue to a C-position of the tryptophan indole moiety.
7947762	4	13	theme	modified	577:584	arg1	chain					602:606	the modified amino acid side chain	573:606	the modified amino acid side chain	573:606	The fragmentation pattern of the modified amino acid side chain was reminiscent of that of aromatic C-glycosides, suggesting a direct attachment of a hexose residue to a C-position of the tryptophan indole moiety.
7947762	0	14	theme	specific	79:86	arg1	residue					99:105	a specific tryptophan residue	77:105	a specific tryptophan residue	77:105	New type of linkage between a carbohydrate and a protein: C-glycosylation of a specific tryptophan residue in human RNase Us.
7947762	4	15	theme	indole	743:748	arg1	moiety					750:755	the tryptophan indole moiety	728:755	the tryptophan indole moiety	728:755	The fragmentation pattern of the modified amino acid side chain was reminiscent of that of aromatic C-glycosides, suggesting a direct attachment of a hexose residue to a C-position of the tryptophan indole moiety.
7947762	0	16	gly	C-glycosylation	58:72	arg1	residue					99:105	a specific tryptophan residue	77:105	a specific tryptophan residue	77:105	New type of linkage between a carbohydrate and a protein: C-glycosylation of a specific tryptophan residue in human RNase Us.
7947762	0	16	gly	C-glycosylation	58:72	arg1	RNase					116:120	human RNase Us	110:123	human RNase Us	110:123	New type of linkage between a carbohydrate and a protein: C-glycosylation of a specific tryptophan residue in human RNase Us.
7947762	1	17	theme	new	138:140	arg1	type					142:145	a new type	136:145	a new type of linkage between a carbohydrate and a protein, involving the rarely modified side chain of a tryptophan residue	136:259	We report a new type of linkage between a carbohydrate and a protein, involving the rarely modified side chain of a tryptophan residue.
7947762	3	18	theme	mass	490:493	arg1	Da					499:500	a molecular mass 162 Da	478:500	a molecular mass 162 Da higher than that expected for tryptophan	478:541	Mass spectrometric analysis of peptides containing this residue showed a molecular mass 162 Da higher than that expected for tryptophan.
7947762	2	19	theme	C-C	320:322	arg1	bond					324:327	a C-C bond	318:327	a C-C bond to the indole ring of the tryptophan residue at position 7 of human RNase Us	318:404	An aldohexopyranosyl residue was found to be linked via a C-C bond to the indole ring of the tryptophan residue at position 7 of human RNase Us.
7947762	2	20	theme	residue	366:372	arg1	ring					343:346	the indole ring	332:346	the indole ring of the tryptophan residue at position 7 of human RNase Us	332:404	An aldohexopyranosyl residue was found to be linked via a C-C bond to the indole ring of the tryptophan residue at position 7 of human RNase Us.
7947762	1	21	theme	side	226:229	arg1	chain					231:235	the rarely modified side chain	206:235	the rarely modified side chain of a tryptophan residue	206:259	We report a new type of linkage between a carbohydrate and a protein, involving the rarely modified side chain of a tryptophan residue.
7947762	3	22	theme	162	495:497	arg1	Da					499:500	a molecular mass 162 Da	478:500	a molecular mass 162 Da higher than that expected for tryptophan	478:541	Mass spectrometric analysis of peptides containing this residue showed a molecular mass 162 Da higher than that expected for tryptophan.
7947762	4	23	theme	amino	586:590	arg1	chain					602:606	the modified amino acid side chain	573:606	the modified amino acid side chain	573:606	The fragmentation pattern of the modified amino acid side chain was reminiscent of that of aromatic C-glycosides, suggesting a direct attachment of a hexose residue to a C-position of the tryptophan indole moiety.
7947762	2	24	theme	tryptophan	355:364	arg1	residue					366:372	the tryptophan residue	351:372	the tryptophan residue at position 7 of human RNase Us	351:404	An aldohexopyranosyl residue was found to be linked via a C-C bond to the indole ring of the tryptophan residue at position 7 of human RNase Us.
7947762	4	25	attach	attachment	678:687	arg2	residue					701:707	a hexose residue	692:707	a hexose residue	692:707	The fragmentation pattern of the modified amino acid side chain was reminiscent of that of aromatic C-glycosides, suggesting a direct attachment of a hexose residue to a C-position of the tryptophan indole moiety.
7947762	4	25	attach	attachment	678:687	arg1	C-position					714:723	a C-position	712:723	a C-position of the tryptophan indole moiety	712:755	The fragmentation pattern of the modified amino acid side chain was reminiscent of that of aromatic C-glycosides, suggesting a direct attachment of a hexose residue to a C-position of the tryptophan indole moiety.
7947762	5	26	theme	indole	946:951	arg1	atom					934:937	the C2 atom	927:937	the C2 atom of the indole	927:951	1H and 13C NMR spectroscopic data confirmed this inference and unequivocally demonstrated the substituent to be an aldohexopyranosyl residue, C-glycosidically linked to the C2 atom of the indole.
7947762	1	27	theme	linkage	150:156	arg1	type					142:145	a new type	136:145	a new type of linkage between a carbohydrate and a protein, involving the rarely modified side chain of a tryptophan residue	136:259	We report a new type of linkage between a carbohydrate and a protein, involving the rarely modified side chain of a tryptophan residue.
7947762	0	28	theme	residue	99:105	arg1	C-glycosylation					58:72	C-glycosylation	58:72	New type of linkage between a carbohydrate and a protein: C-glycosylation of a specific tryptophan residue in human RNase Us.	0:124	New type of linkage between a carbohydrate and a protein: C-glycosylation of a specific tryptophan residue in human RNase Us.
7947762	0	29	from	C-glycosylation	58:72	arg1	RNase					116:120	human RNase Us	110:123	human RNase Us	110:123	New type of linkage between a carbohydrate and a protein: C-glycosylation of a specific tryptophan residue in human RNase Us.
7947762	3	30	theme	molecular	480:488	arg1	Da					499:500	a molecular mass 162 Da	478:500	a molecular mass 162 Da higher than that expected for tryptophan	478:541	Mass spectrometric analysis of peptides containing this residue showed a molecular mass 162 Da higher than that expected for tryptophan.
7947762	4	31	theme	chain	602:606	arg1	pattern					562:568	The fragmentation pattern	544:568	The fragmentation pattern of the modified amino acid side chain	544:606	The fragmentation pattern of the modified amino acid side chain was reminiscent of that of aromatic C-glycosides, suggesting a direct attachment of a hexose residue to a C-position of the tryptophan indole moiety.
7947762	4	31	theme	chain	602:606	arg1	reminiscent					612:622	reminiscent	612:622	reminiscent	612:622	The fragmentation pattern of the modified amino acid side chain was reminiscent of that of aromatic C-glycosides, suggesting a direct attachment of a hexose residue to a C-position of the tryptophan indole moiety.
7947762	2	32	theme	human	391:395	arg1	RNase					397:401	human RNase	391:401	human RNase Us	391:404	An aldohexopyranosyl residue was found to be linked via a C-C bond to the indole ring of the tryptophan residue at position 7 of human RNase Us.
7947762	5	33	theme	spectroscopic	773:785	arg1	data					787:790	1H and 13C NMR spectroscopic data	758:790	1H and 13C NMR spectroscopic data	758:790	1H and 13C NMR spectroscopic data confirmed this inference and unequivocally demonstrated the substituent to be an aldohexopyranosyl residue, C-glycosidically linked to the C2 atom of the indole.
7947762	2	34	theme	indole	336:341	arg1	ring					343:346	the indole ring	332:346	the indole ring of the tryptophan residue at position 7 of human RNase Us	332:404	An aldohexopyranosyl residue was found to be linked via a C-C bond to the indole ring of the tryptophan residue at position 7 of human RNase Us.
7947762	1	35	theme	tryptophan	242:251	arg1	residue					253:259	a tryptophan residue	240:259	a tryptophan residue	240:259	We report a new type of linkage between a carbohydrate and a protein, involving the rarely modified side chain of a tryptophan residue.
7947762	0	36	theme	human	110:114	arg1	RNase					116:120	human RNase Us	110:123	human RNase Us	110:123	New type of linkage between a carbohydrate and a protein: C-glycosylation of a specific tryptophan residue in human RNase Us.
7947762	6	37	theme	side	1065:1068	arg1	chain					1070:1074	an amino acid side chain	1051:1074	an amino acid side chain	1051:1074	This mode of attachment differs from the ones known so far, in which carbohydrates are linked to an amino acid side chain by N- or O-glycosidic bonds.
7947762	0	38	theme	linkage	12:18	arg1	type					4:7	New type	0:7	New type of linkage between a carbohydrate and a protein: C-glycosylation of a specific tryptophan residue in human RNase Us.	0:124	New type of linkage between a carbohydrate and a protein: C-glycosylation of a specific tryptophan residue in human RNase Us.
7947762	5	39	theme	1H	758:759	arg1	data					787:790	1H and 13C NMR spectroscopic data	758:790	1H and 13C NMR spectroscopic data	758:790	1H and 13C NMR spectroscopic data confirmed this inference and unequivocally demonstrated the substituent to be an aldohexopyranosyl residue, C-glycosidically linked to the C2 atom of the indole.
7947762	1	40	theme	residue	253:259	arg1	chain					231:235	the rarely modified side chain	206:235	the rarely modified side chain of a tryptophan residue	206:259	We report a new type of linkage between a carbohydrate and a protein, involving the rarely modified side chain of a tryptophan residue.
7947762	4	41	theme	tryptophan	732:741	arg1	moiety					750:755	the tryptophan indole moiety	728:755	the tryptophan indole moiety	728:755	The fragmentation pattern of the modified amino acid side chain was reminiscent of that of aromatic C-glycosides, suggesting a direct attachment of a hexose residue to a C-position of the tryptophan indole moiety.
7947762	4	42	theme	that	627:630	arg1	pattern					562:568	The fragmentation pattern	544:568	The fragmentation pattern of the modified amino acid side chain	544:606	The fragmentation pattern of the modified amino acid side chain was reminiscent of that of aromatic C-glycosides, suggesting a direct attachment of a hexose residue to a C-position of the tryptophan indole moiety.
7947762	4	42	theme	that	627:630	arg1	reminiscent					612:622	reminiscent	612:622	reminiscent	612:622	The fragmentation pattern of the modified amino acid side chain was reminiscent of that of aromatic C-glycosides, suggesting a direct attachment of a hexose residue to a C-position of the tryptophan indole moiety.
7947762	6	43	theme	attachment	967:976	arg1	mode					959:962	This mode	954:962	This mode of attachment	954:976	This mode of attachment differs from the ones known so far, in which carbohydrates are linked to an amino acid side chain by N- or O-glycosidic bonds.
7947762	5	44	theme	NMR	769:771	arg1	data					787:790	1H and 13C NMR spectroscopic data	758:790	1H and 13C NMR spectroscopic data	758:790	1H and 13C NMR spectroscopic data confirmed this inference and unequivocally demonstrated the substituent to be an aldohexopyranosyl residue, C-glycosidically linked to the C2 atom of the indole.
7947762	2	45	dep	RNase	397:401	arg1	Us					403:404	Us	403:404	Us	403:404	An aldohexopyranosyl residue was found to be linked via a C-C bond to the indole ring of the tryptophan residue at position 7 of human RNase Us.
7947762	3	46	theme	higher	502:507	arg1	Da					499:500	a molecular mass 162 Da	478:500	a molecular mass 162 Da higher than that expected for tryptophan	478:541	Mass spectrometric analysis of peptides containing this residue showed a molecular mass 162 Da higher than that expected for tryptophan.
7947762	3	47	theme	Mass	407:410	arg1	analysis					426:433	Mass spectrometric analysis	407:433	Mass spectrometric analysis of peptides containing this residue	407:469	Mass spectrometric analysis of peptides containing this residue showed a molecular mass 162 Da higher than that expected for tryptophan.
7947762	6	48	theme	O-glycosidic	1085:1096	arg1	bonds					1098:1102	O-glycosidic bonds	1085:1102	O-glycosidic bonds	1085:1102	This mode of attachment differs from the ones known so far, in which carbohydrates are linked to an amino acid side chain by N- or O-glycosidic bonds.
7947762	4	49	theme	residue	701:707	arg1	attachment					678:687	a direct attachment	669:687	a direct attachment of a hexose residue to a C-position of the tryptophan indole moiety	669:755	The fragmentation pattern of the modified amino acid side chain was reminiscent of that of aromatic C-glycosides, suggesting a direct attachment of a hexose residue to a C-position of the tryptophan indole moiety.
7947762	4	50	theme	side	597:600	arg1	chain					602:606	the modified amino acid side chain	573:606	the modified amino acid side chain	573:606	The fragmentation pattern of the modified amino acid side chain was reminiscent of that of aromatic C-glycosides, suggesting a direct attachment of a hexose residue to a C-position of the tryptophan indole moiety.
7947762	4	51	theme	aromatic	635:642	arg1	C-glycosides					644:655	aromatic C-glycosides	635:655	aromatic C-glycosides	635:655	The fragmentation pattern of the modified amino acid side chain was reminiscent of that of aromatic C-glycosides, suggesting a direct attachment of a hexose residue to a C-position of the tryptophan indole moiety.
7947762	6	52	theme	amino	1054:1058	arg1	chain					1070:1074	an amino acid side chain	1051:1074	an amino acid side chain	1051:1074	This mode of attachment differs from the ones known so far, in which carbohydrates are linked to an amino acid side chain by N- or O-glycosidic bonds.
7947762	4	53	theme	hexose	694:699	arg1	residue					701:707	a hexose residue	692:707	a hexose residue	692:707	The fragmentation pattern of the modified amino acid side chain was reminiscent of that of aromatic C-glycosides, suggesting a direct attachment of a hexose residue to a C-position of the tryptophan indole moiety.
7947762	2	54	theme	aldohexopyranosyl	265:281	arg1	residue					283:289	An aldohexopyranosyl residue	262:289	An aldohexopyranosyl residue	262:289	An aldohexopyranosyl residue was found to be linked via a C-C bond to the indole ring of the tryptophan residue at position 7 of human RNase Us.
7947762	6	55	attach	linked	1041:1046	arg2	carbohydrates					1023:1035	carbohydrates	1023:1035	carbohydrates	1023:1035	This mode of attachment differs from the ones known so far, in which carbohydrates are linked to an amino acid side chain by N- or O-glycosidic bonds.
7947762	6	55	attach	linked	1041:1046	arg3	ones					995:998	the ones	991:998	the ones	991:998	This mode of attachment differs from the ones known so far, in which carbohydrates are linked to an amino acid side chain by N- or O-glycosidic bonds.
7947762	6	55	attach	linked	1041:1046	arg3	N-					1079:1080	N-	1079:1080	N-	1079:1080	This mode of attachment differs from the ones known so far, in which carbohydrates are linked to an amino acid side chain by N- or O-glycosidic bonds.
7947762	6	55	attach	linked	1041:1046	arg3	bonds					1098:1102	O-glycosidic bonds	1085:1102	O-glycosidic bonds	1085:1102	This mode of attachment differs from the ones known so far, in which carbohydrates are linked to an amino acid side chain by N- or O-glycosidic bonds.
7947762	6	55	attach	linked	1041:1046	arg1	chain					1070:1074	an amino acid side chain	1051:1074	an amino acid side chain	1051:1074	This mode of attachment differs from the ones known so far, in which carbohydrates are linked to an amino acid side chain by N- or O-glycosidic bonds.
7947762	0	56	dep	type	4:7	arg1	C-glycosylation					58:72	C-glycosylation	58:72	New type of linkage between a carbohydrate and a protein: C-glycosylation of a specific tryptophan residue in human RNase Us.	0:124	New type of linkage between a carbohydrate and a protein: C-glycosylation of a specific tryptophan residue in human RNase Us.
7947762	4	57	theme	fragmentation	548:560	arg1	pattern					562:568	The fragmentation pattern	544:568	The fragmentation pattern of the modified amino acid side chain	544:606	The fragmentation pattern of the modified amino acid side chain was reminiscent of that of aromatic C-glycosides, suggesting a direct attachment of a hexose residue to a C-position of the tryptophan indole moiety.
7947762	4	57	theme	fragmentation	548:560	arg1	reminiscent					612:622	reminiscent	612:622	reminiscent	612:622	The fragmentation pattern of the modified amino acid side chain was reminiscent of that of aromatic C-glycosides, suggesting a direct attachment of a hexose residue to a C-position of the tryptophan indole moiety.
7947762	0	58	dep	RNase	116:120	arg1	Us					122:123	Us	122:123	Us	122:123	New type of linkage between a carbohydrate and a protein: C-glycosylation of a specific tryptophan residue in human RNase Us.
7947762	5	59	theme	13C	765:767	arg1	NMR					769:771	13C NMR	765:771	13C NMR	765:771	1H and 13C NMR spectroscopic data confirmed this inference and unequivocally demonstrated the substituent to be an aldohexopyranosyl residue, C-glycosidically linked to the C2 atom of the indole.
7947762	2	60	attach	linked	307:312	arg3	bond					324:327	a C-C bond	318:327	a C-C bond to the indole ring of the tryptophan residue at position 7 of human RNase Us	318:404	An aldohexopyranosyl residue was found to be linked via a C-C bond to the indole ring of the tryptophan residue at position 7 of human RNase Us.
7947762	5	61	theme	C2	931:932	arg1	atom					934:937	the C2 atom	927:937	the C2 atom of the indole	927:951	1H and 13C NMR spectroscopic data confirmed this inference and unequivocally demonstrated the substituent to be an aldohexopyranosyl residue, C-glycosidically linked to the C2 atom of the indole.
7947762	3	62	theme	peptides	438:445	arg1	analysis					426:433	Mass spectrometric analysis	407:433	Mass spectrometric analysis of peptides containing this residue	407:469	Mass spectrometric analysis of peptides containing this residue showed a molecular mass 162 Da higher than that expected for tryptophan.
7947762	3	63	contain	containing	447:456	arg2	residue					463:469	this residue	458:469	this residue	458:469	Mass spectrometric analysis of peptides containing this residue showed a molecular mass 162 Da higher than that expected for tryptophan.
7947762	3	63	contain	containing	447:456	arg1	peptides					438:445	peptides	438:445	peptides containing this residue	438:469	Mass spectrometric analysis of peptides containing this residue showed a molecular mass 162 Da higher than that expected for tryptophan.
15993892	3	0	theme	loop	583:586	arg1	"					587:587	the enzyme "repression loop"	560:587	the enzyme "repression loop"	560:587	The main difference between the two structures is the conformation of the enzyme "repression loop".
15993892	7	1	theme	mammalian	1230:1238	arg1	structures					1244:1253	other mammalian PAP structures	1224:1253	other mammalian PAP structures	1224:1253	In the crystal structure of rHPAP(Pp), the enzyme "repression loop" has an open conformation similar to that observed in other mammalian PAP structures.
15993892	7	2	theme	PAP	1240:1242	arg1	structures					1244:1253	other mammalian PAP structures	1224:1253	other mammalian PAP structures	1224:1253	In the crystal structure of rHPAP(Pp), the enzyme "repression loop" has an open conformation similar to that observed in other mammalian PAP structures.
15993892	2	3	theme	inactive	408:415	arg1	state					418:422	its oxidized (inactive) state	394:422	its oxidized (inactive) state	394:422	In both cases, the enzyme crystallized in its oxidized (inactive) state, in which both Fe atoms in the dinuclear active site are Fe(III).
15993892	1	4	dep	pastoris	254:261	arg1	rHPAP					264:268	rHPAP	264:268	rHPAP(Pp)	264:272	The crystal structure of human purple acid phosphatase recombinantly expressed in Escherichia coli (rHPAP(Ec)) and Pichia pastoris (rHPAP(Pp)) has been determined in two different crystal forms, both at 2.2A resolution.
15993892	1	4	dep	pastoris	254:261	arg1	Pp					270:271	Pp	270:271	Pp	270:271	The crystal structure of human purple acid phosphatase recombinantly expressed in Escherichia coli (rHPAP(Ec)) and Pichia pastoris (rHPAP(Pp)) has been determined in two different crystal forms, both at 2.2A resolution.
15993892	1	5	theme	human	157:161	arg1	phosphatase					175:185	human purple acid phosphatase	157:185	human purple acid phosphatase recombinantly expressed in Escherichia coli (rHPAP(Ec)) and Pichia pastoris (rHPAP(Pp))	157:273	The crystal structure of human purple acid phosphatase recombinantly expressed in Escherichia coli (rHPAP(Ec)) and Pichia pastoris (rHPAP(Pp)) has been determined in two different crystal forms, both at 2.2A resolution.
15993892	2	6	theme	Fe	439:440	arg1	atoms					442:446	both Fe atoms	434:446	both Fe atoms in the dinuclear active site	434:475	In both cases, the enzyme crystallized in its oxidized (inactive) state, in which both Fe atoms in the dinuclear active site are Fe(III).
15993892	2	6	theme	Fe	439:440	arg1	Fe					481:482	Fe	481:482	Fe(III)	481:487	In both cases, the enzyme crystallized in its oxidized (inactive) state, in which both Fe atoms in the dinuclear active site are Fe(III).
15993892	5	7	theme	enzyme-substrate	941:956	arg1	complex					958:964	the enzyme-substrate complex	937:964	the enzyme-substrate complex	937:964	In the crystals obtained from rHPAP(Ec), the carboxylate side-chain of Asp145 of this loop acts as a bidentate ligand that bridges the two metal atoms, in a manner analogous to a possible binding mode for a phosphate ester substrate in the enzyme-substrate complex.
15993892	7	8	theme	repression	1154:1163	arg1	"					1169:1169	the enzyme "repression loop"	1142:1169	the enzyme "repression loop"	1142:1169	In the crystal structure of rHPAP(Pp), the enzyme "repression loop" has an open conformation similar to that observed in other mammalian PAP structures.
15993892	8	9	theme	observed	1373:1380	arg1	mode					1400:1403	the observed alternate binding mode	1369:1403	the observed alternate binding mode	1369:1403	The present structures demonstrate that the repression loop exhibits significant conformational flexibility, and the observed alternate binding mode suggests a possible inhibitory role for this loop.
15993892	7	10	theme	open	1178:1181	arg1	conformation					1183:1194	an open conformation	1175:1194	an open conformation similar to that observed in other mammalian PAP structures	1175:1253	In the crystal structure of rHPAP(Pp), the enzyme "repression loop" has an open conformation similar to that observed in other mammalian PAP structures.
15993892	2	11	from	Fe	481:482	arg1	state					418:422	its oxidized (inactive) state	394:422	its oxidized (inactive) state	394:422	In both cases, the enzyme crystallized in its oxidized (inactive) state, in which both Fe atoms in the dinuclear active site are Fe(III).
15993892	0	12	theme	inhibitory	84:93	arg1	conformation					95:106	an inhibitory conformation	81:106	an inhibitory conformation of the repression loop	81:129	Crystal structures of recombinant human purple Acid phosphatase with and without an inhibitory conformation of the repression loop.
15993892	1	13	theme	different	302:310	arg1	forms					320:324	two different crystal forms	298:324	two different crystal forms	298:324	The crystal structure of human purple acid phosphatase recombinantly expressed in Escherichia coli (rHPAP(Ec)) and Pichia pastoris (rHPAP(Pp)) has been determined in two different crystal forms, both at 2.2A resolution.
15993892	6	14	theme	Phe146	1024:1029	arg1	side-chain					1031:1040	the neighboring Phe146 side-chain	1008:1040	the neighboring Phe146 side-chain	1008:1040	The carboxylate side-chain of Asp145 and the neighboring Phe146 side-chain thus block the active site, thereby inactivating the enzyme.
15993892	6	15	theme	Asp145	997:1002	arg1	side-chain					1031:1040	the neighboring Phe146 side-chain	1008:1040	the neighboring Phe146 side-chain	1008:1040	The carboxylate side-chain of Asp145 and the neighboring Phe146 side-chain thus block the active site, thereby inactivating the enzyme.
15993892	6	15	theme	Asp145	997:1002	arg1	side-chain					983:992	The carboxylate side-chain	967:992	The carboxylate side-chain of Asp145	967:1002	The carboxylate side-chain of Asp145 and the neighboring Phe146 side-chain thus block the active site, thereby inactivating the enzyme.
15993892	5	16	theme	Asp145	772:777	arg1	side-chain					758:767	the carboxylate side-chain	742:767	the carboxylate side-chain of Asp145 of this loop	742:790	In the crystals obtained from rHPAP(Ec), the carboxylate side-chain of Asp145 of this loop acts as a bidentate ligand that bridges the two metal atoms, in a manner analogous to a possible binding mode for a phosphate ester substrate in the enzyme-substrate complex.
15993892	5	16	theme	Asp145	772:777	arg1	ligand					812:817	a bidentate ligand	800:817	a bidentate ligand that bridges the two metal atoms	800:850	In the crystals obtained from rHPAP(Ec), the carboxylate side-chain of Asp145 of this loop acts as a bidentate ligand that bridges the two metal atoms, in a manner analogous to a possible binding mode for a phosphate ester substrate in the enzyme-substrate complex.
15993892	1	17	theme	crystal	312:318	arg1	forms					320:324	two different crystal forms	298:324	two different crystal forms	298:324	The crystal structure of human purple acid phosphatase recombinantly expressed in Escherichia coli (rHPAP(Ec)) and Pichia pastoris (rHPAP(Pp)) has been determined in two different crystal forms, both at 2.2A resolution.
15993892	5	18	theme	bidentate	802:810	arg1	side-chain					758:767	the carboxylate side-chain	742:767	the carboxylate side-chain of Asp145 of this loop	742:790	In the crystals obtained from rHPAP(Ec), the carboxylate side-chain of Asp145 of this loop acts as a bidentate ligand that bridges the two metal atoms, in a manner analogous to a possible binding mode for a phosphate ester substrate in the enzyme-substrate complex.
15993892	5	18	theme	bidentate	802:810	arg1	ligand					812:817	a bidentate ligand	800:817	a bidentate ligand that bridges the two metal atoms	800:850	In the crystals obtained from rHPAP(Ec), the carboxylate side-chain of Asp145 of this loop acts as a bidentate ligand that bridges the two metal atoms, in a manner analogous to a possible binding mode for a phosphate ester substrate in the enzyme-substrate complex.
15993892	7	19	theme	rHPAP	1131:1135	arg1	structure					1118:1126	the crystal structure	1106:1126	the crystal structure of rHPAP(Pp)	1106:1139	In the crystal structure of rHPAP(Pp), the enzyme "repression loop" has an open conformation similar to that observed in other mammalian PAP structures.
15993892	1	20	theme	purple	163:168	arg1	phosphatase					175:185	human purple acid phosphatase	157:185	human purple acid phosphatase recombinantly expressed in Escherichia coli (rHPAP(Ec)) and Pichia pastoris (rHPAP(Pp))	157:273	The crystal structure of human purple acid phosphatase recombinantly expressed in Escherichia coli (rHPAP(Ec)) and Pichia pastoris (rHPAP(Pp)) has been determined in two different crystal forms, both at 2.2A resolution.
15993892	3	21	theme	"	587:587	arg1	conformation					544:555	the conformation	540:555	the conformation of the enzyme "repression loop"	540:587	The main difference between the two structures is the conformation of the enzyme "repression loop".
15993892	3	21	theme	"	587:587	arg1	difference					499:508	The main difference	490:508	The main difference between the two structures	490:535	The main difference between the two structures is the conformation of the enzyme "repression loop".
15993892	1	22	theme	acid	170:173	arg1	phosphatase					175:185	human purple acid phosphatase	157:185	human purple acid phosphatase recombinantly expressed in Escherichia coli (rHPAP(Ec)) and Pichia pastoris (rHPAP(Pp))	157:273	The crystal structure of human purple acid phosphatase recombinantly expressed in Escherichia coli (rHPAP(Ec)) and Pichia pastoris (rHPAP(Pp)) has been determined in two different crystal forms, both at 2.2A resolution.
15993892	5	23	theme	ester	918:922	arg1	substrate					924:932	a phosphate ester substrate	906:932	a phosphate ester substrate in the enzyme-substrate complex	906:964	In the crystals obtained from rHPAP(Ec), the carboxylate side-chain of Asp145 of this loop acts as a bidentate ligand that bridges the two metal atoms, in a manner analogous to a possible binding mode for a phosphate ester substrate in the enzyme-substrate complex.
15993892	6	24	theme	carboxylate	971:981	arg1	side-chain					983:992	The carboxylate side-chain	967:992	The carboxylate side-chain of Asp145	967:1002	The carboxylate side-chain of Asp145 and the neighboring Phe146 side-chain thus block the active site, thereby inactivating the enzyme.
15993892	1	25	theme	phosphatase	175:185	arg1	structure					144:152	The crystal structure	132:152	The crystal structure of human purple acid phosphatase recombinantly expressed in Escherichia coli (rHPAP(Ec)) and Pichia pastoris (rHPAP(Pp))	132:273	The crystal structure of human purple acid phosphatase recombinantly expressed in Escherichia coli (rHPAP(Ec)) and Pichia pastoris (rHPAP(Pp)) has been determined in two different crystal forms, both at 2.2A resolution.
15993892	0	26	theme	Crystal	0:6	arg1	structures					8:17	Crystal structures	0:17	Crystal structures of recombinant human purple Acid phosphatase with and without an inhibitory conformation of the repression loop	0:129	Crystal structures of recombinant human purple Acid phosphatase with and without an inhibitory conformation of the repression loop.
15993892	7	27	theme	similar	1196:1202	arg1	conformation					1183:1194	an open conformation	1175:1194	an open conformation similar to that observed in other mammalian PAP structures	1175:1253	In the crystal structure of rHPAP(Pp), the enzyme "repression loop" has an open conformation similar to that observed in other mammalian PAP structures.
15993892	7	28	contain	has	1171:1173	arg1	"					1169:1169	the enzyme "repression loop"	1142:1169	the enzyme "repression loop"	1142:1169	In the crystal structure of rHPAP(Pp), the enzyme "repression loop" has an open conformation similar to that observed in other mammalian PAP structures.
15993892	7	28	contain	has	1171:1173	arg2	conformation					1183:1194	an open conformation	1175:1194	an open conformation similar to that observed in other mammalian PAP structures	1175:1253	In the crystal structure of rHPAP(Pp), the enzyme "repression loop" has an open conformation similar to that observed in other mammalian PAP structures.
15993892	7	29	theme	other	1224:1228	arg1	structures					1244:1253	other mammalian PAP structures	1224:1253	other mammalian PAP structures	1224:1253	In the crystal structure of rHPAP(Pp), the enzyme "repression loop" has an open conformation similar to that observed in other mammalian PAP structures.
15993892	0	30	theme	recombinant	22:32	arg1	phosphatase					52:62	recombinant human purple Acid phosphatase	22:62	recombinant human purple Acid phosphatase	22:62	Crystal structures of recombinant human purple Acid phosphatase with and without an inhibitory conformation of the repression loop.
15993892	0	31	theme	loop	126:129	arg1	conformation					95:106	an inhibitory conformation	81:106	an inhibitory conformation of the repression loop	81:129	Crystal structures of recombinant human purple Acid phosphatase with and without an inhibitory conformation of the repression loop.
15993892	7	32	theme	loop	1165:1168	arg1	"					1169:1169	the enzyme "repression loop"	1142:1169	the enzyme "repression loop"	1142:1169	In the crystal structure of rHPAP(Pp), the enzyme "repression loop" has an open conformation similar to that observed in other mammalian PAP structures.
15993892	5	33	theme	loop	787:790	arg1	Asp145					772:777	Asp145	772:777	Asp145 of this loop	772:790	In the crystals obtained from rHPAP(Ec), the carboxylate side-chain of Asp145 of this loop acts as a bidentate ligand that bridges the two metal atoms, in a manner analogous to a possible binding mode for a phosphate ester substrate in the enzyme-substrate complex.
15993892	6	34	theme	active	1057:1062	arg1	site					1064:1067	the active site	1053:1067	the active site	1053:1067	The carboxylate side-chain of Asp145 and the neighboring Phe146 side-chain thus block the active site, thereby inactivating the enzyme.
15993892	0	35	theme	repression	115:124	arg1	loop					126:129	the repression loop	111:129	the repression loop	111:129	Crystal structures of recombinant human purple Acid phosphatase with and without an inhibitory conformation of the repression loop.
15993892	4	36	theme	loop	619:622	arg1	cleavage					602:609	Proteolytic cleavage	590:609	Proteolytic cleavage of this loop in vivo or in vitro	590:642	Proteolytic cleavage of this loop in vivo or in vitro results in significant activation of the mammalian PAPs.
15993892	8	37	theme	conformational	1337:1350	arg1	flexibility					1352:1362	significant conformational flexibility	1325:1362	significant conformational flexibility	1325:1362	The present structures demonstrate that the repression loop exhibits significant conformational flexibility, and the observed alternate binding mode suggests a possible inhibitory role for this loop.
15993892	0	38	theme	purple	40:45	arg1	phosphatase					52:62	recombinant human purple Acid phosphatase	22:62	recombinant human purple Acid phosphatase	22:62	Crystal structures of recombinant human purple Acid phosphatase with and without an inhibitory conformation of the repression loop.
15993892	8	39	theme	binding	1392:1398	arg1	mode					1400:1403	the observed alternate binding mode	1369:1403	the observed alternate binding mode	1369:1403	The present structures demonstrate that the repression loop exhibits significant conformational flexibility, and the observed alternate binding mode suggests a possible inhibitory role for this loop.
15993892	5	40	theme	possible	880:887	arg1	mode					897:900	a possible binding mode	878:900	a possible binding mode for a phosphate ester substrate in the enzyme-substrate complex	878:964	In the crystals obtained from rHPAP(Ec), the carboxylate side-chain of Asp145 of this loop acts as a bidentate ligand that bridges the two metal atoms, in a manner analogous to a possible binding mode for a phosphate ester substrate in the enzyme-substrate complex.
15993892	5	41	theme	metal	840:844	arg1	atoms					846:850	the two metal atoms	832:850	the two metal atoms	832:850	In the crystals obtained from rHPAP(Ec), the carboxylate side-chain of Asp145 of this loop acts as a bidentate ligand that bridges the two metal atoms, in a manner analogous to a possible binding mode for a phosphate ester substrate in the enzyme-substrate complex.
15993892	2	42	theme	oxidized	398:405	arg1	state					418:422	its oxidized (inactive) state	394:422	its oxidized (inactive) state	394:422	In both cases, the enzyme crystallized in its oxidized (inactive) state, in which both Fe atoms in the dinuclear active site are Fe(III).
15993892	1	43	dep	forms	320:324	arg1	both					327:330	both	327:330	both	327:330	The crystal structure of human purple acid phosphatase recombinantly expressed in Escherichia coli (rHPAP(Ec)) and Pichia pastoris (rHPAP(Pp)) has been determined in two different crystal forms, both at 2.2A resolution.
15993892	0	44	theme	human	34:38	arg1	phosphatase					52:62	recombinant human purple Acid phosphatase	22:62	recombinant human purple Acid phosphatase	22:62	Crystal structures of recombinant human purple Acid phosphatase with and without an inhibitory conformation of the repression loop.
15993892	1	45	theme	2.2A	335:338	arg1	resolution					340:349	2.2A resolution	335:349	2.2A resolution	335:349	The crystal structure of human purple acid phosphatase recombinantly expressed in Escherichia coli (rHPAP(Ec)) and Pichia pastoris (rHPAP(Pp)) has been determined in two different crystal forms, both at 2.2A resolution.
15993892	7	46	theme	crystal	1110:1116	arg1	structure					1118:1126	the crystal structure	1106:1126	the crystal structure of rHPAP(Pp)	1106:1139	In the crystal structure of rHPAP(Pp), the enzyme "repression loop" has an open conformation similar to that observed in other mammalian PAP structures.
15993892	0	47	theme	phosphatase	52:62	arg1	structures					8:17	Crystal structures	0:17	Crystal structures of recombinant human purple Acid phosphatase with and without an inhibitory conformation of the repression loop	0:129	Crystal structures of recombinant human purple Acid phosphatase with and without an inhibitory conformation of the repression loop.
15993892	7	48	located	observed	1212:1219	arg2	that					1207:1210	that	1207:1210	that	1207:1210	In the crystal structure of rHPAP(Pp), the enzyme "repression loop" has an open conformation similar to that observed in other mammalian PAP structures.
15993892	7	48	located	observed	1212:1219	arg1	structures					1244:1253	other mammalian PAP structures	1224:1253	other mammalian PAP structures	1224:1253	In the crystal structure of rHPAP(Pp), the enzyme "repression loop" has an open conformation similar to that observed in other mammalian PAP structures.
15993892	4	49	theme	PAPs	695:698	arg1	activation					667:676	significant activation	655:676	significant activation of the mammalian PAPs	655:698	Proteolytic cleavage of this loop in vivo or in vitro results in significant activation of the mammalian PAPs.
15993892	5	50	theme	phosphate	908:916	arg1	substrate					924:932	a phosphate ester substrate	906:932	a phosphate ester substrate in the enzyme-substrate complex	906:964	In the crystals obtained from rHPAP(Ec), the carboxylate side-chain of Asp145 of this loop acts as a bidentate ligand that bridges the two metal atoms, in a manner analogous to a possible binding mode for a phosphate ester substrate in the enzyme-substrate complex.
15993892	5	51	theme	carboxylate	746:756	arg1	side-chain					758:767	the carboxylate side-chain	742:767	the carboxylate side-chain of Asp145 of this loop	742:790	In the crystals obtained from rHPAP(Ec), the carboxylate side-chain of Asp145 of this loop acts as a bidentate ligand that bridges the two metal atoms, in a manner analogous to a possible binding mode for a phosphate ester substrate in the enzyme-substrate complex.
15993892	5	51	theme	carboxylate	746:756	arg1	ligand					812:817	a bidentate ligand	800:817	a bidentate ligand that bridges the two metal atoms	800:850	In the crystals obtained from rHPAP(Ec), the carboxylate side-chain of Asp145 of this loop acts as a bidentate ligand that bridges the two metal atoms, in a manner analogous to a possible binding mode for a phosphate ester substrate in the enzyme-substrate complex.
15993892	0	52	theme	Acid	47:50	arg1	phosphatase					52:62	recombinant human purple Acid phosphatase	22:62	recombinant human purple Acid phosphatase	22:62	Crystal structures of recombinant human purple Acid phosphatase with and without an inhibitory conformation of the repression loop.
15993892	2	53	theme	dinuclear	455:463	arg1	site					472:475	the dinuclear active site	451:475	the dinuclear active site	451:475	In both cases, the enzyme crystallized in its oxidized (inactive) state, in which both Fe atoms in the dinuclear active site are Fe(III).
15993892	8	54	theme	alternate	1382:1390	arg1	mode					1400:1403	the observed alternate binding mode	1369:1403	the observed alternate binding mode	1369:1403	The present structures demonstrate that the repression loop exhibits significant conformational flexibility, and the observed alternate binding mode suggests a possible inhibitory role for this loop.
15993892	4	55	theme	mammalian	685:693	arg1	PAPs					695:698	the mammalian PAPs	681:698	the mammalian PAPs	681:698	Proteolytic cleavage of this loop in vivo or in vitro results in significant activation of the mammalian PAPs.
15993892	5	56	theme	binding	889:895	arg1	mode					897:900	a possible binding mode	878:900	a possible binding mode for a phosphate ester substrate in the enzyme-substrate complex	878:964	In the crystals obtained from rHPAP(Ec), the carboxylate side-chain of Asp145 of this loop acts as a bidentate ligand that bridges the two metal atoms, in a manner analogous to a possible binding mode for a phosphate ester substrate in the enzyme-substrate complex.
15993892	4	57	theme	significant	655:665	arg1	activation					667:676	significant activation	655:676	significant activation of the mammalian PAPs	655:698	Proteolytic cleavage of this loop in vivo or in vitro results in significant activation of the mammalian PAPs.
15993892	3	58	theme	enzyme	564:569	arg1	"					587:587	the enzyme "repression loop"	560:587	the enzyme "repression loop"	560:587	The main difference between the two structures is the conformation of the enzyme "repression loop".
15993892	7	59	theme	enzyme	1146:1151	arg1	"					1169:1169	the enzyme "repression loop"	1142:1169	the enzyme "repression loop"	1142:1169	In the crystal structure of rHPAP(Pp), the enzyme "repression loop" has an open conformation similar to that observed in other mammalian PAP structures.
15993892	2	60	theme	active	465:470	arg1	site					472:475	the dinuclear active site	451:475	the dinuclear active site	451:475	In both cases, the enzyme crystallized in its oxidized (inactive) state, in which both Fe atoms in the dinuclear active site are Fe(III).
15993892	5	61	theme	analogous	865:873	arg1	manner					858:863	a manner	856:863	a manner analogous to a possible binding mode for a phosphate ester substrate in the enzyme-substrate complex	856:964	In the crystals obtained from rHPAP(Ec), the carboxylate side-chain of Asp145 of this loop acts as a bidentate ligand that bridges the two metal atoms, in a manner analogous to a possible binding mode for a phosphate ester substrate in the enzyme-substrate complex.
15993892	1	62	dep	coli	226:229	arg1	Ec					238:239	Ec	238:239	Ec	238:239	The crystal structure of human purple acid phosphatase recombinantly expressed in Escherichia coli (rHPAP(Ec)) and Pichia pastoris (rHPAP(Pp)) has been determined in two different crystal forms, both at 2.2A resolution.
15993892	1	62	dep	coli	226:229	arg1	rHPAP					232:236	rHPAP	232:236	rHPAP(Ec)	232:240	The crystal structure of human purple acid phosphatase recombinantly expressed in Escherichia coli (rHPAP(Ec)) and Pichia pastoris (rHPAP(Pp)) has been determined in two different crystal forms, both at 2.2A resolution.
15993892	4	63	theme	Proteolytic	590:600	arg1	cleavage					602:609	Proteolytic cleavage	590:609	Proteolytic cleavage of this loop in vivo or in vitro	590:642	Proteolytic cleavage of this loop in vivo or in vitro results in significant activation of the mammalian PAPs.
15993892	2	64	from	atoms	442:446	arg1	site					472:475	the dinuclear active site	451:475	the dinuclear active site	451:475	In both cases, the enzyme crystallized in its oxidized (inactive) state, in which both Fe atoms in the dinuclear active site are Fe(III).
15993892	8	65	theme	repression	1300:1309	arg1	loop					1311:1314	the repression loop	1296:1314	the repression loop	1296:1314	The present structures demonstrate that the repression loop exhibits significant conformational flexibility, and the observed alternate binding mode suggests a possible inhibitory role for this loop.
15993892	8	66	theme	present	1260:1266	arg1	structures					1268:1277	The present structures	1256:1277	The present structures	1256:1277	The present structures demonstrate that the repression loop exhibits significant conformational flexibility, and the observed alternate binding mode suggests a possible inhibitory role for this loop.
15993892	6	67	theme	neighboring	1012:1022	arg1	side-chain					1031:1040	the neighboring Phe146 side-chain	1008:1040	the neighboring Phe146 side-chain	1008:1040	The carboxylate side-chain of Asp145 and the neighboring Phe146 side-chain thus block the active site, thereby inactivating the enzyme.
15993892	8	68	theme	significant	1325:1335	arg1	flexibility					1352:1362	significant conformational flexibility	1325:1362	significant conformational flexibility	1325:1362	The present structures demonstrate that the repression loop exhibits significant conformational flexibility, and the observed alternate binding mode suggests a possible inhibitory role for this loop.
15993892	1	69	theme	crystal	136:142	arg1	structure					144:152	The crystal structure	132:152	The crystal structure of human purple acid phosphatase recombinantly expressed in Escherichia coli (rHPAP(Ec)) and Pichia pastoris (rHPAP(Pp))	132:273	The crystal structure of human purple acid phosphatase recombinantly expressed in Escherichia coli (rHPAP(Ec)) and Pichia pastoris (rHPAP(Pp)) has been determined in two different crystal forms, both at 2.2A resolution.
15993892	8	70	theme	inhibitory	1425:1434	arg1	role					1436:1439	a possible inhibitory role	1414:1439	a possible inhibitory role for this loop	1414:1453	The present structures demonstrate that the repression loop exhibits significant conformational flexibility, and the observed alternate binding mode suggests a possible inhibitory role for this loop.
15993892	5	71	from	substrate	924:932	arg1	complex					958:964	the enzyme-substrate complex	937:964	the enzyme-substrate complex	937:964	In the crystals obtained from rHPAP(Ec), the carboxylate side-chain of Asp145 of this loop acts as a bidentate ligand that bridges the two metal atoms, in a manner analogous to a possible binding mode for a phosphate ester substrate in the enzyme-substrate complex.
15993892	3	72	theme	repression	572:581	arg1	"					587:587	the enzyme "repression loop"	560:587	the enzyme "repression loop"	560:587	The main difference between the two structures is the conformation of the enzyme "repression loop".
15993892	3	73	theme	main	494:497	arg1	conformation					544:555	the conformation	540:555	the conformation of the enzyme "repression loop"	540:587	The main difference between the two structures is the conformation of the enzyme "repression loop".
15993892	3	73	theme	main	494:497	arg1	difference					499:508	The main difference	490:508	The main difference between the two structures	490:535	The main difference between the two structures is the conformation of the enzyme "repression loop".
15993892	8	74	theme	possible	1416:1423	arg1	role					1436:1439	a possible inhibitory role	1414:1439	a possible inhibitory role for this loop	1414:1453	The present structures demonstrate that the repression loop exhibits significant conformational flexibility, and the observed alternate binding mode suggests a possible inhibitory role for this loop.
33605212	6	0	theme	clinical	486:493	arg1	studies					526:532	clinical, biochemical, and animal model studies	486:532	clinical, biochemical, and animal model studies	486:532	Despite decades of clinical, biochemical, and animal model studies, the molecular mechanism of ABCA4 is unknown.
33605212	1	1	theme	diverse	148:154	arg1	functions					156:164	diverse functions	148:164	diverse functions	148:164	The ATP-binding cassette (ABC) transporter family contains thousands of members with diverse functions.
33605212	6	2	theme	ABCA4	562:566	arg1	mechanism					549:557	the molecular mechanism	535:557	the molecular mechanism of ABCA4	535:566	Despite decades of clinical, biochemical, and animal model studies, the molecular mechanism of ABCA4 is unknown.
33605212	6	2	theme	ABCA4	562:566	arg1	unknown					571:577	unknown	571:577	unknown	571:577	Despite decades of clinical, biochemical, and animal model studies, the molecular mechanism of ABCA4 is unknown.
33605212	7	3	from	structures	600:609	arg1	conformations					633:645	two conformations	629:645	two conformations	629:645	Here, we report the structures of human ABCA4 in two conformations.
33605212	1	4	contain	contains	113:120	arg1	family					106:111	The ATP-binding cassette (ABC) transporter family	63:111	The ATP-binding cassette (ABC) transporter family	63:111	The ATP-binding cassette (ABC) transporter family contains thousands of members with diverse functions.
33605212	1	4	contain	contains	113:120	arg2	thousands					122:130	thousands	122:130	thousands of members with diverse functions	122:164	The ATP-binding cassette (ABC) transporter family contains thousands of members with diverse functions.
33605212	9	5	theme	substrate	821:829	arg1	release					831:837	substrate release	821:837	substrate release	821:837	The presence of ATP induces large conformational changes that could lead to substrate release.
33605212	7	6	theme	human	614:618	arg1	ABCA4					620:624	human ABCA4	614:624	human ABCA4	614:624	Here, we report the structures of human ABCA4 in two conformations.
33605212	8	7	theme	outward-facing	687:700	arg1	conformation					702:713	an outward-facing conformation	684:713	an outward-facing conformation	684:713	In the absence of ATP, ABCA4 adopts an outward-facing conformation, poised to recruit substrate.
33605212	1	8	with	members	135:141	arg1	functions					156:164	diverse functions	148:164	diverse functions	148:164	The ATP-binding cassette (ABC) transporter family contains thousands of members with diverse functions.
33605212	10	9	theme	new	953:955	arg1	experiments					957:967	new experiments	953:967	new experiments	953:967	These structures provide a molecular basis to understand many disease-causing mutations and a rational guide for new experiments to uncover how ABCA4 recruits, flips, and releases retinoids.
33605212	9	10	theme	ATP	761:763	arg1	presence					749:756	The presence	745:756	The presence of ATP	745:763	The presence of ATP induces large conformational changes that could lead to substrate release.
33605212	1	11	theme	ATP-binding	67:77	arg1	ABC					89:91	ABC	89:91	ABC	89:91	The ATP-binding cassette (ABC) transporter family contains thousands of members with diverse functions.
33605212	1	11	theme	ATP-binding	67:77	arg1	cassette					79:86	ATP-binding cassette	67:86	The ATP-binding cassette (ABC) transporter family	63:111	The ATP-binding cassette (ABC) transporter family contains thousands of members with diverse functions.
33605212	5	12	theme	impaired	437:444	arg1	vision					446:451	impaired vision	437:451	impaired vision	437:451	Mutations in ABCA4 cause impaired vision or blindness.
33605212	2	13	dep	outward	228:234	arg1	export					237:242	export	237:242	export	237:242	Movement of the substrate, powered by ATP hydrolysis, can be outward (export) or inward (import).
33605212	0	14	theme	retinal	39:45	arg1	ABCA4					56:60	the eukaryotic retinal importer ABCA4	24:60	the eukaryotic retinal importer ABCA4	24:60	Molecular structures of the eukaryotic retinal importer ABCA4.
33605212	1	15	theme	cassette	79:86	arg1	family					106:111	The ATP-binding cassette (ABC) transporter family	63:111	The ATP-binding cassette (ABC) transporter family	63:111	The ATP-binding cassette (ABC) transporter family contains thousands of members with diverse functions.
33605212	6	16	theme	molecular	539:547	arg1	mechanism					549:557	the molecular mechanism	535:557	the molecular mechanism of ABCA4	535:566	Despite decades of clinical, biochemical, and animal model studies, the molecular mechanism of ABCA4 is unknown.
33605212	6	16	theme	molecular	539:547	arg1	unknown					571:577	unknown	571:577	unknown	571:577	Despite decades of clinical, biochemical, and animal model studies, the molecular mechanism of ABCA4 is unknown.
33605212	6	17	theme	biochemical	496:506	arg1	studies					526:532	clinical, biochemical, and animal model studies	486:532	clinical, biochemical, and animal model studies	486:532	Despite decades of clinical, biochemical, and animal model studies, the molecular mechanism of ABCA4 is unknown.
33605212	10	18	theme	molecular	867:875	arg1	basis					877:881	a molecular basis	865:881	a molecular basis to understand many disease-causing mutations and a rational guide for new experiments to uncover how ABCA4 recruits, flips, and releases retinoids	865:1028	These structures provide a molecular basis to understand many disease-causing mutations and a rational guide for new experiments to uncover how ABCA4 recruits, flips, and releases retinoids.
33605212	0	19	theme	Molecular	0:8	arg1	structures					10:19	Molecular structures	0:19	Molecular structures of the eukaryotic retinal importer ABCA4	0:60	Molecular structures of the eukaryotic retinal importer ABCA4.
33605212	4	20	theme	toxic	375:379	arg1	retinoids					381:389	toxic retinoids	375:389	toxic retinoids	375:389	It also removes toxic retinoids from the disc lumen.
33605212	2	21	theme	ATP	205:207	arg1	hydrolysis					209:218	ATP hydrolysis	205:218	ATP hydrolysis	205:218	Movement of the substrate, powered by ATP hydrolysis, can be outward (export) or inward (import).
33605212	6	22	theme	studies	526:532	arg1	decades					475:481	decades	475:481	decades of clinical, biochemical, and animal model studies	475:532	Despite decades of clinical, biochemical, and animal model studies, the molecular mechanism of ABCA4 is unknown.
33605212	9	23	theme	large	773:777	arg1	changes					794:800	large conformational changes	773:800	large conformational changes that could lead to substrate release	773:837	The presence of ATP induces large conformational changes that could lead to substrate release.
33605212	7	24	theme	ABCA4	620:624	arg1	structures					600:609	the structures	596:609	the structures of human ABCA4 in two conformations	596:645	Here, we report the structures of human ABCA4 in two conformations.
33605212	1	25	theme	transporter	94:104	arg1	family					106:111	The ATP-binding cassette (ABC) transporter family	63:111	The ATP-binding cassette (ABC) transporter family	63:111	The ATP-binding cassette (ABC) transporter family contains thousands of members with diverse functions.
33605212	6	26	theme	model	520:524	arg1	studies					526:532	clinical, biochemical, and animal model studies	486:532	clinical, biochemical, and animal model studies	486:532	Despite decades of clinical, biochemical, and animal model studies, the molecular mechanism of ABCA4 is unknown.
33605212	9	27	theme	conformational	779:792	arg1	changes					794:800	large conformational changes	773:800	large conformational changes that could lead to substrate release	773:837	The presence of ATP induces large conformational changes that could lead to substrate release.
33605212	10	28	theme	many	897:900	arg1	mutations					918:926	many disease-causing mutations	897:926	many disease-causing mutations	897:926	These structures provide a molecular basis to understand many disease-causing mutations and a rational guide for new experiments to uncover how ABCA4 recruits, flips, and releases retinoids.
33605212	0	29	theme	eukaryotic	28:37	arg1	ABCA4					56:60	the eukaryotic retinal importer ABCA4	24:60	the eukaryotic retinal importer ABCA4	24:60	Molecular structures of the eukaryotic retinal importer ABCA4.
33605212	6	30	theme	animal	513:518	arg1	studies					526:532	clinical, biochemical, and animal model studies	486:532	clinical, biochemical, and animal model studies	486:532	Despite decades of clinical, biochemical, and animal model studies, the molecular mechanism of ABCA4 is unknown.
33605212	0	31	theme	ABCA4	56:60	arg1	structures					10:19	Molecular structures	0:19	Molecular structures of the eukaryotic retinal importer ABCA4	0:60	Molecular structures of the eukaryotic retinal importer ABCA4.
33605212	4	32	theme	disc	400:403	arg1	lumen					405:409	the disc lumen	396:409	the disc lumen	396:409	It also removes toxic retinoids from the disc lumen.
33605212	0	33	theme	importer	47:54	arg1	ABCA4					56:60	the eukaryotic retinal importer ABCA4	24:60	the eukaryotic retinal importer ABCA4	24:60	Molecular structures of the eukaryotic retinal importer ABCA4.
33605212	8	34	theme	ATP	666:668	arg1	absence					655:661	the absence	651:661	the absence of ATP	651:668	In the absence of ATP, ABCA4 adopts an outward-facing conformation, poised to recruit substrate.
33605212	5	35	from	Mutations	412:420	arg1	ABCA4					425:429	ABCA4	425:429	ABCA4	425:429	Mutations in ABCA4 cause impaired vision or blindness.
33605212	10	36	theme	rational	934:941	arg1	guide					943:947	a rational guide	932:947	a rational guide for new experiments to uncover how ABCA4 recruits, flips, and releases retinoids	932:1028	These structures provide a molecular basis to understand many disease-causing mutations and a rational guide for new experiments to uncover how ABCA4 recruits, flips, and releases retinoids.
33605212	3	37	theme	eukaryotic	276:285	arg1	importer					287:294	a eukaryotic importer	274:294	a eukaryotic importer transporting retinal to the cytosol to enter the visual cycle	274:356	ABCA4 is a eukaryotic importer transporting retinal to the cytosol to enter the visual cycle.
33605212	3	37	theme	eukaryotic	276:285	arg1	ABCA4					265:269	ABCA4	265:269	ABCA4	265:269	ABCA4 is a eukaryotic importer transporting retinal to the cytosol to enter the visual cycle.
33605212	2	38	theme	substrate	183:191	arg1	Movement					167:174	Movement	167:174	Movement	167:174	Movement of the substrate, powered by ATP hydrolysis, can be outward (export) or inward (import).
33605212	1	39	theme	members	135:141	arg1	thousands					122:130	thousands	122:130	thousands of members with diverse functions	122:164	The ATP-binding cassette (ABC) transporter family contains thousands of members with diverse functions.
33605212	3	40	theme	visual	345:350	arg1	cycle					352:356	the visual cycle	341:356	the visual cycle	341:356	ABCA4 is a eukaryotic importer transporting retinal to the cytosol to enter the visual cycle.
33605212	10	41	theme	disease-causing	902:916	arg1	mutations					918:926	many disease-causing mutations	897:926	many disease-causing mutations	897:926	These structures provide a molecular basis to understand many disease-causing mutations and a rational guide for new experiments to uncover how ABCA4 recruits, flips, and releases retinoids.
17704566	4	0	theme	dual	888:891	arg1	inhibitor					904:912	competitive and potent dual NEP/DPP-IV inhibitor MCB3937	865:920	inhibitor	904:912	Here, the synthesis and crystal structures of the soluble extracellular domain of human NEP (residues 52-749) complexed with the NEP, competitive and potent dual NEP/DPP-IV inhibitor MCB3937 are described.
17704566	4	0	theme	dual	888:891	arg1	synthesis					741:749	synthesis	741:749	synthesis	741:749	Here, the synthesis and crystal structures of the soluble extracellular domain of human NEP (residues 52-749) complexed with the NEP, competitive and potent dual NEP/DPP-IV inhibitor MCB3937 are described.
17704566	3	1	theme	dual	613:616	arg1	concept					639:645	A dual NEP/DPP-IV inhibitor concept	611:645	A dual NEP/DPP-IV inhibitor concept	611:645	A dual NEP/DPP-IV inhibitor concept is proposed, offering an alternative strategy for the treatment of type 2 diabetes.
17704566	2	2	theme	elevated	525:532	arg1	interest					534:541	an elevated interest	522:541	an elevated interest in inhibitors of this enzyme for the treatment of type II diabetes	522:608	The activity of GLP-1 is also rapidly abolished by the serine protease dipeptidyl peptidase IV (DPP-IV), which led to an elevated interest in inhibitors of this enzyme for the treatment of type II diabetes.
17704566	4	3	dep	residues	824:831	arg1	52-749					833:838	52-749	833:838	52-749	833:838	Here, the synthesis and crystal structures of the soluble extracellular domain of human NEP (residues 52-749) complexed with the NEP, competitive and potent dual NEP/DPP-IV inhibitor MCB3937 are described.
17704566	4	4	theme	competitive	865:875	arg1	inhibitor					904:912	competitive and potent dual NEP/DPP-IV inhibitor MCB3937	865:920	inhibitor	904:912	Here, the synthesis and crystal structures of the soluble extracellular domain of human NEP (residues 52-749) complexed with the NEP, competitive and potent dual NEP/DPP-IV inhibitor MCB3937 are described.
17704566	4	4	theme	competitive	865:875	arg1	synthesis					741:749	synthesis	741:749	synthesis	741:749	Here, the synthesis and crystal structures of the soluble extracellular domain of human NEP (residues 52-749) complexed with the NEP, competitive and potent dual NEP/DPP-IV inhibitor MCB3937 are described.
17704566	1	5	theme	incretin	303:310	arg1	peptide					334:340	the incretin hormone glucagon-like peptide 1	299:342	the incretin hormone glucagon-like peptide 1 (GLP-1)	299:350	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion.
17704566	1	5	theme	incretin	303:310	arg1	GLP-1					345:349	GLP-1	345:349	GLP-1	345:349	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion.
17704566	1	6	theme	metabolic	137:145	arg1	inactivation					147:158	the metabolic inactivation	133:158	the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion	133:401	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion.
17704566	2	7	theme	protease	466:473	arg1	peptidase					486:494	the serine protease dipeptidyl peptidase IV	455:497	the serine protease dipeptidyl peptidase IV (DPP-IV)	455:506	The activity of GLP-1 is also rapidly abolished by the serine protease dipeptidyl peptidase IV (DPP-IV), which led to an elevated interest in inhibitors of this enzyme for the treatment of type II diabetes.
17704566	2	7	theme	protease	466:473	arg1	DPP-IV					500:505	DPP-IV	500:505	DPP-IV	500:505	The activity of GLP-1 is also rapidly abolished by the serine protease dipeptidyl peptidase IV (DPP-IV), which led to an elevated interest in inhibitors of this enzyme for the treatment of type II diabetes.
17704566	1	8	theme	hormone	312:318	arg1	peptide					334:340	the incretin hormone glucagon-like peptide 1	299:342	the incretin hormone glucagon-like peptide 1 (GLP-1)	299:350	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion.
17704566	1	8	theme	hormone	312:318	arg1	GLP-1					345:349	GLP-1	345:349	GLP-1	345:349	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion.
17704566	4	9	theme	soluble	781:787	arg1	domain					803:808	the soluble extracellular domain	777:808	the soluble extracellular domain of human NEP (residues 52-749) complexed with the NEP	777:862	Here, the synthesis and crystal structures of the soluble extracellular domain of human NEP (residues 52-749) complexed with the NEP, competitive and potent dual NEP/DPP-IV inhibitor MCB3937 are described.
17704566	4	9	theme	soluble	781:787	arg1	NEP					819:821	human NEP	813:821	human NEP (residues 52-749)	813:839	Here, the synthesis and crystal structures of the soluble extracellular domain of human NEP (residues 52-749) complexed with the NEP, competitive and potent dual NEP/DPP-IV inhibitor MCB3937 are described.
17704566	1	10	theme	insulin	385:391	arg1	secretion					393:401	insulin secretion	385:401	insulin secretion	385:401	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion.
17704566	3	11	theme	diabetes	721:728	arg1	treatment					701:709	the treatment	697:709	the treatment of type 2 diabetes	697:728	A dual NEP/DPP-IV inhibitor concept is proposed, offering an alternative strategy for the treatment of type 2 diabetes.
17704566	2	12	theme	serine	459:464	arg1	peptidase					486:494	the serine protease dipeptidyl peptidase IV	455:497	the serine protease dipeptidyl peptidase IV (DPP-IV)	455:506	The activity of GLP-1 is also rapidly abolished by the serine protease dipeptidyl peptidase IV (DPP-IV), which led to an elevated interest in inhibitors of this enzyme for the treatment of type II diabetes.
17704566	2	12	theme	serine	459:464	arg1	DPP-IV					500:505	DPP-IV	500:505	DPP-IV	500:505	The activity of GLP-1 is also rapidly abolished by the serine protease dipeptidyl peptidase IV (DPP-IV), which led to an elevated interest in inhibitors of this enzyme for the treatment of type II diabetes.
17704566	1	13	theme	glucagon-like	320:332	arg1	peptide					334:340	the incretin hormone glucagon-like peptide 1	299:342	the incretin hormone glucagon-like peptide 1 (GLP-1)	299:350	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion.
17704566	1	13	theme	glucagon-like	320:332	arg1	GLP-1					345:349	GLP-1	345:349	GLP-1	345:349	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion.
17704566	1	14	theme	secretion	393:401	arg1	number					165:170	a number	163:170	a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor	163:285	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion.
17704566	1	14	theme	secretion	393:401	arg1	enkephalins					208:218	the enkephalins	204:218	the enkephalins	204:218	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion.
17704566	1	14	theme	secretion	393:401	arg1	peptide					334:340	the incretin hormone glucagon-like peptide 1	299:342	the incretin hormone glucagon-like peptide 1 (GLP-1)	299:350	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion.
17704566	1	14	theme	secretion	393:401	arg1	bradykinin					246:255	bradykinin	246:255	bradykinin	246:255	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion.
17704566	1	14	theme	secretion	393:401	arg1	which					353:357	which	353:357	which	353:357	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion.
17704566	1	14	theme	secretion	393:401	arg1	P					231:231	substance P	221:231	substance P	221:231	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion.
17704566	1	14	theme	secretion	393:401	arg1	stimulator					371:380	a potent stimulator	362:380	a potent stimulator of insulin secretion	362:401	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion.
17704566	1	14	theme	secretion	393:401	arg1	GLP-1					345:349	GLP-1	345:349	GLP-1	345:349	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion.
17704566	1	14	theme	secretion	393:401	arg1	endothelin					234:243	endothelin	234:243	endothelin	234:243	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion.
17704566	1	14	theme	secretion	393:401	arg1	factor					280:285	atrial natriuretic factor	261:285	atrial natriuretic factor	261:285	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion.
17704566	4	15	theme	potent	881:886	arg1	inhibitor					904:912	competitive and potent dual NEP/DPP-IV inhibitor MCB3937	865:920	inhibitor	904:912	Here, the synthesis and crystal structures of the soluble extracellular domain of human NEP (residues 52-749) complexed with the NEP, competitive and potent dual NEP/DPP-IV inhibitor MCB3937 are described.
17704566	4	15	theme	potent	881:886	arg1	synthesis					741:749	synthesis	741:749	synthesis	741:749	Here, the synthesis and crystal structures of the soluble extracellular domain of human NEP (residues 52-749) complexed with the NEP, competitive and potent dual NEP/DPP-IV inhibitor MCB3937 are described.
17704566	1	16	theme	peptide	334:340	arg1	inactivation					147:158	the metabolic inactivation	133:158	the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion	133:401	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion.
17704566	2	17	theme	enzyme	565:570	arg1	inhibitors					546:555	inhibitors	546:555	inhibitors of this enzyme	546:570	The activity of GLP-1 is also rapidly abolished by the serine protease dipeptidyl peptidase IV (DPP-IV), which led to an elevated interest in inhibitors of this enzyme for the treatment of type II diabetes.
17704566	3	18	theme	NEP/DPP-IV	618:627	arg1	concept					639:645	A dual NEP/DPP-IV inhibitor concept	611:645	A dual NEP/DPP-IV inhibitor concept	611:645	A dual NEP/DPP-IV inhibitor concept is proposed, offering an alternative strategy for the treatment of type 2 diabetes.
17704566	2	19	theme	GLP-1	420:424	arg1	activity					408:415	The activity	404:415	The activity of GLP-1	404:424	The activity of GLP-1 is also rapidly abolished by the serine protease dipeptidyl peptidase IV (DPP-IV), which led to an elevated interest in inhibitors of this enzyme for the treatment of type II diabetes.
17704566	1	20	theme	Neutral	73:79	arg1	enzyme					114:119	the major enzyme	104:119	the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion	104:401	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion.
17704566	1	20	theme	Neutral	73:79	arg1	NEP					96:98	NEP	96:98	NEP	96:98	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion.
17704566	1	20	theme	Neutral	73:79	arg1	endopeptidase					81:93	Neutral endopeptidase	73:93	Neutral endopeptidase (NEP)	73:99	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion.
17704566	3	21	theme	inhibitor	629:637	arg1	concept					639:645	A dual NEP/DPP-IV inhibitor concept	611:645	A dual NEP/DPP-IV inhibitor concept	611:645	A dual NEP/DPP-IV inhibitor concept is proposed, offering an alternative strategy for the treatment of type 2 diabetes.
17704566	4	22	theme	crystal	755:761	arg1	structures					763:772	crystal structures	755:772	crystal structures	755:772	Here, the synthesis and crystal structures of the soluble extracellular domain of human NEP (residues 52-749) complexed with the NEP, competitive and potent dual NEP/DPP-IV inhibitor MCB3937 are described.
17704566	2	23	theme	type	593:596	arg1	diabetes					601:608	type II diabetes	593:608	type II diabetes	593:608	The activity of GLP-1 is also rapidly abolished by the serine protease dipeptidyl peptidase IV (DPP-IV), which led to an elevated interest in inhibitors of this enzyme for the treatment of type II diabetes.
17704566	0	24	theme	Structural	0:9	arg1	studies					11:17	Structural studies	0:17	Structural studies of a bifunctional inhibitor of neprilysin and DPP-IV	0:70	Structural studies of a bifunctional inhibitor of neprilysin and DPP-IV.
17704566	1	25	theme	number	165:170	arg1	inactivation					147:158	the metabolic inactivation	133:158	the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion	133:401	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion.
17704566	4	26	dep	synthesis	741:749	arg1	the					737:739	the	737:739	the	737:739	Here, the synthesis and crystal structures of the soluble extracellular domain of human NEP (residues 52-749) complexed with the NEP, competitive and potent dual NEP/DPP-IV inhibitor MCB3937 are described.
17704566	1	27	theme	atrial	261:266	arg1	factor					280:285	atrial natriuretic factor	261:285	atrial natriuretic factor	261:285	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion.
17704566	4	28	theme	NEP	819:821	arg1	domain					803:808	the soluble extracellular domain	777:808	the soluble extracellular domain of human NEP (residues 52-749) complexed with the NEP	777:862	Here, the synthesis and crystal structures of the soluble extracellular domain of human NEP (residues 52-749) complexed with the NEP, competitive and potent dual NEP/DPP-IV inhibitor MCB3937 are described.
17704566	4	28	theme	NEP	819:821	arg1	NEP					819:821	human NEP	813:821	human NEP (residues 52-749)	813:839	Here, the synthesis and crystal structures of the soluble extracellular domain of human NEP (residues 52-749) complexed with the NEP, competitive and potent dual NEP/DPP-IV inhibitor MCB3937 are described.
17704566	1	29	theme	bioactive	175:183	arg1	enkephalins					208:218	the enkephalins	204:218	the enkephalins	204:218	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion.
17704566	1	29	theme	bioactive	175:183	arg1	bradykinin					246:255	bradykinin	246:255	bradykinin	246:255	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion.
17704566	1	29	theme	bioactive	175:183	arg1	peptides					185:192	bioactive peptides	175:192	bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor	175:285	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion.
17704566	1	29	theme	bioactive	175:183	arg1	P					231:231	substance P	221:231	substance P	221:231	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion.
17704566	1	29	theme	bioactive	175:183	arg1	endothelin					234:243	endothelin	234:243	endothelin	234:243	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion.
17704566	1	29	theme	bioactive	175:183	arg1	factor					280:285	atrial natriuretic factor	261:285	atrial natriuretic factor	261:285	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion.
17704566	0	30	theme	inhibitor	37:45	arg1	studies					11:17	Structural studies	0:17	Structural studies of a bifunctional inhibitor of neprilysin and DPP-IV	0:70	Structural studies of a bifunctional inhibitor of neprilysin and DPP-IV.
17704566	1	31	theme	natriuretic	268:278	arg1	factor					280:285	atrial natriuretic factor	261:285	atrial natriuretic factor	261:285	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion.
17704566	1	32	theme	peptides	185:192	arg1	number					165:170	a number	163:170	a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor	163:285	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion.
17704566	1	32	theme	peptides	185:192	arg1	enkephalins					208:218	the enkephalins	204:218	the enkephalins	204:218	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion.
17704566	1	32	theme	peptides	185:192	arg1	peptide					334:340	the incretin hormone glucagon-like peptide 1	299:342	the incretin hormone glucagon-like peptide 1 (GLP-1)	299:350	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion.
17704566	1	32	theme	peptides	185:192	arg1	bradykinin					246:255	bradykinin	246:255	bradykinin	246:255	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion.
17704566	1	32	theme	peptides	185:192	arg1	which					353:357	which	353:357	which	353:357	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion.
17704566	1	32	theme	peptides	185:192	arg1	P					231:231	substance P	221:231	substance P	221:231	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion.
17704566	1	32	theme	peptides	185:192	arg1	stimulator					371:380	a potent stimulator	362:380	a potent stimulator of insulin secretion	362:401	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion.
17704566	1	32	theme	peptides	185:192	arg1	GLP-1					345:349	GLP-1	345:349	GLP-1	345:349	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion.
17704566	1	32	theme	peptides	185:192	arg1	endothelin					234:243	endothelin	234:243	endothelin	234:243	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion.
17704566	1	32	theme	peptides	185:192	arg1	factor					280:285	atrial natriuretic factor	261:285	atrial natriuretic factor	261:285	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion.
17704566	0	33	theme	bifunctional	24:35	arg1	inhibitor					37:45	a bifunctional inhibitor	22:45	a bifunctional inhibitor of neprilysin and DPP-IV	22:70	Structural studies of a bifunctional inhibitor of neprilysin and DPP-IV.
17704566	2	34	theme	dipeptidyl	475:484	arg1	peptidase					486:494	the serine protease dipeptidyl peptidase IV	455:497	the serine protease dipeptidyl peptidase IV (DPP-IV)	455:506	The activity of GLP-1 is also rapidly abolished by the serine protease dipeptidyl peptidase IV (DPP-IV), which led to an elevated interest in inhibitors of this enzyme for the treatment of type II diabetes.
17704566	2	34	theme	dipeptidyl	475:484	arg1	DPP-IV					500:505	DPP-IV	500:505	DPP-IV	500:505	The activity of GLP-1 is also rapidly abolished by the serine protease dipeptidyl peptidase IV (DPP-IV), which led to an elevated interest in inhibitors of this enzyme for the treatment of type II diabetes.
17704566	0	35	theme	neprilysin	50:59	arg1	inhibitor					37:45	a bifunctional inhibitor	22:45	a bifunctional inhibitor of neprilysin and DPP-IV	22:70	Structural studies of a bifunctional inhibitor of neprilysin and DPP-IV.
17704566	2	36	from	interest	534:541	arg1	inhibitors					546:555	inhibitors	546:555	inhibitors of this enzyme	546:570	The activity of GLP-1 is also rapidly abolished by the serine protease dipeptidyl peptidase IV (DPP-IV), which led to an elevated interest in inhibitors of this enzyme for the treatment of type II diabetes.
17704566	4	37	theme	domain	803:808	arg1	inhibitor					904:912	competitive and potent dual NEP/DPP-IV inhibitor MCB3937	865:920	inhibitor	904:912	Here, the synthesis and crystal structures of the soluble extracellular domain of human NEP (residues 52-749) complexed with the NEP, competitive and potent dual NEP/DPP-IV inhibitor MCB3937 are described.
17704566	4	37	theme	domain	803:808	arg1	synthesis					741:749	synthesis	741:749	synthesis	741:749	Here, the synthesis and crystal structures of the soluble extracellular domain of human NEP (residues 52-749) complexed with the NEP, competitive and potent dual NEP/DPP-IV inhibitor MCB3937 are described.
17704566	4	37	theme	domain	803:808	arg1	structures					763:772	crystal structures	755:772	crystal structures	755:772	Here, the synthesis and crystal structures of the soluble extracellular domain of human NEP (residues 52-749) complexed with the NEP, competitive and potent dual NEP/DPP-IV inhibitor MCB3937 are described.
17704566	4	38	theme	NEP/DPP-IV	893:902	arg1	inhibitor					904:912	competitive and potent dual NEP/DPP-IV inhibitor MCB3937	865:920	inhibitor	904:912	Here, the synthesis and crystal structures of the soluble extracellular domain of human NEP (residues 52-749) complexed with the NEP, competitive and potent dual NEP/DPP-IV inhibitor MCB3937 are described.
17704566	4	38	theme	NEP/DPP-IV	893:902	arg1	synthesis					741:749	synthesis	741:749	synthesis	741:749	Here, the synthesis and crystal structures of the soluble extracellular domain of human NEP (residues 52-749) complexed with the NEP, competitive and potent dual NEP/DPP-IV inhibitor MCB3937 are described.
17704566	3	39	theme	alternative	672:682	arg1	strategy					684:691	an alternative strategy	669:691	an alternative strategy for the treatment of type 2 diabetes	669:728	A dual NEP/DPP-IV inhibitor concept is proposed, offering an alternative strategy for the treatment of type 2 diabetes.
17704566	4	40	theme	extracellular	789:801	arg1	domain					803:808	the soluble extracellular domain	777:808	the soluble extracellular domain of human NEP (residues 52-749) complexed with the NEP	777:862	Here, the synthesis and crystal structures of the soluble extracellular domain of human NEP (residues 52-749) complexed with the NEP, competitive and potent dual NEP/DPP-IV inhibitor MCB3937 are described.
17704566	4	40	theme	extracellular	789:801	arg1	NEP					819:821	human NEP	813:821	human NEP (residues 52-749)	813:839	Here, the synthesis and crystal structures of the soluble extracellular domain of human NEP (residues 52-749) complexed with the NEP, competitive and potent dual NEP/DPP-IV inhibitor MCB3937 are described.
17704566	4	41	theme	human	813:817	arg1	residues					824:831	residues 52-749	824:838	residues 52-749	824:838	Here, the synthesis and crystal structures of the soluble extracellular domain of human NEP (residues 52-749) complexed with the NEP, competitive and potent dual NEP/DPP-IV inhibitor MCB3937 are described.
17704566	4	41	theme	human	813:817	arg1	NEP					819:821	human NEP	813:821	human NEP (residues 52-749)	813:839	Here, the synthesis and crystal structures of the soluble extracellular domain of human NEP (residues 52-749) complexed with the NEP, competitive and potent dual NEP/DPP-IV inhibitor MCB3937 are described.
17704566	2	42	theme	diabetes	601:608	arg1	treatment					580:588	the treatment	576:588	the treatment of type II diabetes	576:608	The activity of GLP-1 is also rapidly abolished by the serine protease dipeptidyl peptidase IV (DPP-IV), which led to an elevated interest in inhibitors of this enzyme for the treatment of type II diabetes.
17704566	1	43	theme	major	108:112	arg1	enzyme					114:119	the major enzyme	104:119	the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion	104:401	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion.
17704566	1	43	theme	major	108:112	arg1	endopeptidase					81:93	Neutral endopeptidase	73:93	Neutral endopeptidase (NEP)	73:99	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion.
17704566	3	44	theme	type	714:717	arg1	diabetes					721:728	type 2 diabetes	714:728	type 2 diabetes	714:728	A dual NEP/DPP-IV inhibitor concept is proposed, offering an alternative strategy for the treatment of type 2 diabetes.
17704566	1	45	theme	potent	364:369	arg1	which					353:357	which	353:357	which	353:357	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion.
17704566	1	45	theme	potent	364:369	arg1	stimulator					371:380	a potent stimulator	362:380	a potent stimulator of insulin secretion	362:401	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion.
17704566	0	46	theme	DPP-IV	65:70	arg1	inhibitor					37:45	a bifunctional inhibitor	22:45	a bifunctional inhibitor of neprilysin and DPP-IV	22:70	Structural studies of a bifunctional inhibitor of neprilysin and DPP-IV.
17704566	1	47	theme	stimulator	371:380	arg1	inactivation					147:158	the metabolic inactivation	133:158	the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion	133:401	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion.
17704566	1	48	theme	substance	221:229	arg1	P					231:231	substance P	221:231	substance P	221:231	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor, as well as the incretin hormone glucagon-like peptide 1 (GLP-1), which is a potent stimulator of insulin secretion.
14747736	2	0	theme	novel	458:462	arg1	analgesics					464:473	novel analgesics	458:473	novel analgesics	458:473	Owing to the physiological importance of NEP in the modulation of nociceptive and pressor responses, there is considerable interest in inhibitors of this enzyme as novel analgesics and antihypertensive agents.
14747736	2	1	theme	NEP	335:337	arg1	importance					321:330	the physiological importance	303:330	the physiological importance of NEP in the modulation of nociceptive and pressor responses	303:392	Owing to the physiological importance of NEP in the modulation of nociceptive and pressor responses, there is considerable interest in inhibitors of this enzyme as novel analgesics and antihypertensive agents.
14747736	3	2	theme	soluble	540:546	arg1	NEP					578:580	human NEP	572:580	human NEP (residues 52-749)	572:598	Here, the crystal structures of the soluble extracellular domain of human NEP (residues 52-749) complexed with various potent and competitive inhibitors are described.
14747736	3	2	theme	soluble	540:546	arg1	domain					562:567	the soluble extracellular domain	536:567	the soluble extracellular domain of human NEP (residues 52-749) complexed with various potent and competitive inhibitors	536:655	Here, the crystal structures of the soluble extracellular domain of human NEP (residues 52-749) complexed with various potent and competitive inhibitors are described.
14747736	4	3	theme	groups	757:762	arg1	specificity					780:790	the subsite specificity	768:790	the subsite specificity of the enzyme	768:804	The structures unambiguously reveal the binding mode of the different zinc-chelating groups and the subsite specificity of the enzyme.
14747736	4	3	theme	groups	757:762	arg1	mode					720:723	the binding mode	708:723	the binding mode of the different zinc-chelating groups	708:762	The structures unambiguously reveal the binding mode of the different zinc-chelating groups and the subsite specificity of the enzyme.
14747736	2	4	from	importance	321:330	arg1	modulation					346:355	the modulation	342:355	the modulation of nociceptive and pressor responses	342:392	Owing to the physiological importance of NEP in the modulation of nociceptive and pressor responses, there is considerable interest in inhibitors of this enzyme as novel analgesics and antihypertensive agents.
14747736	4	5	theme	subsite	772:778	arg1	specificity					780:790	the subsite specificity	768:790	the subsite specificity of the enzyme	768:804	The structures unambiguously reveal the binding mode of the different zinc-chelating groups and the subsite specificity of the enzyme.
14747736	2	6	theme	pressor	376:382	arg1	modulation					346:355	the modulation	342:355	the modulation of nociceptive and pressor responses	342:392	Owing to the physiological importance of NEP in the modulation of nociceptive and pressor responses, there is considerable interest in inhibitors of this enzyme as novel analgesics and antihypertensive agents.
14747736	1	7	theme	Neutral	79:85	arg1	enzyme					120:125	the major enzyme	110:125	the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor	110:291	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor.
14747736	1	7	theme	Neutral	79:85	arg1	NEP					102:104	NEP	102:104	NEP	102:104	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor.
14747736	1	7	theme	Neutral	79:85	arg1	endopeptidase					87:99	Neutral endopeptidase	79:99	Neutral endopeptidase (NEP)	79:105	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor.
14747736	3	8	theme	extracellular	548:560	arg1	NEP					578:580	human NEP	572:580	human NEP (residues 52-749)	572:598	Here, the crystal structures of the soluble extracellular domain of human NEP (residues 52-749) complexed with various potent and competitive inhibitors are described.
14747736	3	8	theme	extracellular	548:560	arg1	domain					562:567	the soluble extracellular domain	536:567	the soluble extracellular domain of human NEP (residues 52-749) complexed with various potent and competitive inhibitors	536:655	Here, the crystal structures of the soluble extracellular domain of human NEP (residues 52-749) complexed with various potent and competitive inhibitors are described.
14747736	2	9	theme	nociceptive	360:370	arg1	modulation					346:355	the modulation	342:355	the modulation of nociceptive and pressor responses	342:392	Owing to the physiological importance of NEP in the modulation of nociceptive and pressor responses, there is considerable interest in inhibitors of this enzyme as novel analgesics and antihypertensive agents.
14747736	0	10	theme	Structural	0:9	arg1	analysis					11:18	Structural analysis	0:18	Structural analysis of neprilysin with various specific and potent inhibitors	0:76	Structural analysis of neprilysin with various specific and potent inhibitors.
14747736	3	11	theme	domain	562:567	arg1	structures					522:531	the crystal structures	510:531	the crystal structures of the soluble extracellular domain of human NEP (residues 52-749) complexed with various potent and competitive inhibitors	510:655	Here, the crystal structures of the soluble extracellular domain of human NEP (residues 52-749) complexed with various potent and competitive inhibitors are described.
14747736	1	12	theme	number	171:176	arg1	inactivation					153:164	the metabolic inactivation	139:164	the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor	139:291	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor.
14747736	0	13	theme	neprilysin	23:32	arg1	analysis					11:18	Structural analysis	0:18	Structural analysis of neprilysin with various specific and potent inhibitors	0:76	Structural analysis of neprilysin with various specific and potent inhibitors.
14747736	4	14	theme	zinc-chelating	742:755	arg1	groups					757:762	the different zinc-chelating groups	728:762	the different zinc-chelating groups	728:762	The structures unambiguously reveal the binding mode of the different zinc-chelating groups and the subsite specificity of the enzyme.
14747736	3	15	dep	residues	583:590	arg1	52-749					592:597	52-749	592:597	52-749	592:597	Here, the crystal structures of the soluble extracellular domain of human NEP (residues 52-749) complexed with various potent and competitive inhibitors are described.
14747736	2	16	theme	considerable	404:415	arg1	interest					417:424	considerable interest	404:424	considerable interest in inhibitors of this enzyme as novel analgesics and antihypertensive agents	404:501	Owing to the physiological importance of NEP in the modulation of nociceptive and pressor responses, there is considerable interest in inhibitors of this enzyme as novel analgesics and antihypertensive agents.
14747736	1	17	theme	atrial	267:272	arg1	factor					286:291	atrial natriuretic factor	267:291	atrial natriuretic factor	267:291	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor.
14747736	3	18	theme	potent	623:628	arg1	inhibitors					646:655	various potent and competitive inhibitors	615:655	various potent and competitive inhibitors	615:655	Here, the crystal structures of the soluble extracellular domain of human NEP (residues 52-749) complexed with various potent and competitive inhibitors are described.
14747736	1	19	theme	metabolic	143:151	arg1	inactivation					153:164	the metabolic inactivation	139:164	the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor	139:291	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor.
14747736	1	20	theme	bioactive	181:189	arg1	enkephalins					214:224	the enkephalins	210:224	the enkephalins	210:224	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor.
14747736	1	20	theme	bioactive	181:189	arg1	bradykinin					252:261	bradykinin	252:261	bradykinin	252:261	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor.
14747736	1	20	theme	bioactive	181:189	arg1	peptides					191:198	bioactive peptides	181:198	bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor	181:291	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor.
14747736	1	20	theme	bioactive	181:189	arg1	P					237:237	substance P	227:237	substance P	227:237	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor.
14747736	1	20	theme	bioactive	181:189	arg1	endothelin					240:249	endothelin	240:249	endothelin	240:249	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor.
14747736	1	20	theme	bioactive	181:189	arg1	factor					286:291	atrial natriuretic factor	267:291	atrial natriuretic factor	267:291	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor.
14747736	0	21	theme	various	39:45	arg1	inhibitors					67:76	various specific and potent inhibitors	39:76	various specific and potent inhibitors	39:76	Structural analysis of neprilysin with various specific and potent inhibitors.
14747736	1	22	theme	natriuretic	274:284	arg1	factor					286:291	atrial natriuretic factor	267:291	atrial natriuretic factor	267:291	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor.
14747736	3	23	theme	NEP	578:580	arg1	NEP					578:580	human NEP	572:580	human NEP (residues 52-749)	572:598	Here, the crystal structures of the soluble extracellular domain of human NEP (residues 52-749) complexed with various potent and competitive inhibitors are described.
14747736	3	23	theme	NEP	578:580	arg1	domain					562:567	the soluble extracellular domain	536:567	the soluble extracellular domain of human NEP (residues 52-749) complexed with various potent and competitive inhibitors	536:655	Here, the crystal structures of the soluble extracellular domain of human NEP (residues 52-749) complexed with various potent and competitive inhibitors are described.
14747736	1	24	theme	peptides	191:198	arg1	number					171:176	a number	169:176	a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor	169:291	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor.
14747736	1	24	theme	peptides	191:198	arg1	enkephalins					214:224	the enkephalins	210:224	the enkephalins	210:224	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor.
14747736	1	24	theme	peptides	191:198	arg1	bradykinin					252:261	bradykinin	252:261	bradykinin	252:261	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor.
14747736	1	24	theme	peptides	191:198	arg1	P					237:237	substance P	227:237	substance P	227:237	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor.
14747736	1	24	theme	peptides	191:198	arg1	endothelin					240:249	endothelin	240:249	endothelin	240:249	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor.
14747736	1	24	theme	peptides	191:198	arg1	factor					286:291	atrial natriuretic factor	267:291	atrial natriuretic factor	267:291	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor.
14747736	2	25	theme	enzyme	448:453	arg1	inhibitors					429:438	inhibitors	429:438	inhibitors of this enzyme as novel analgesics and antihypertensive agents	429:501	Owing to the physiological importance of NEP in the modulation of nociceptive and pressor responses, there is considerable interest in inhibitors of this enzyme as novel analgesics and antihypertensive agents.
14747736	3	26	theme	various	615:621	arg1	inhibitors					646:655	various potent and competitive inhibitors	615:655	various potent and competitive inhibitors	615:655	Here, the crystal structures of the soluble extracellular domain of human NEP (residues 52-749) complexed with various potent and competitive inhibitors are described.
14747736	0	27	theme	specific	47:54	arg1	inhibitors					67:76	various specific and potent inhibitors	39:76	various specific and potent inhibitors	39:76	Structural analysis of neprilysin with various specific and potent inhibitors.
14747736	3	28	theme	human	572:576	arg1	NEP					578:580	human NEP	572:580	human NEP (residues 52-749)	572:598	Here, the crystal structures of the soluble extracellular domain of human NEP (residues 52-749) complexed with various potent and competitive inhibitors are described.
14747736	3	28	theme	human	572:576	arg1	residues					583:590	residues 52-749	583:597	residues 52-749	583:597	Here, the crystal structures of the soluble extracellular domain of human NEP (residues 52-749) complexed with various potent and competitive inhibitors are described.
14747736	0	29	with	analysis	11:18	arg1	inhibitors					67:76	various specific and potent inhibitors	39:76	various specific and potent inhibitors	39:76	Structural analysis of neprilysin with various specific and potent inhibitors.
14747736	2	30	dep	nociceptive	360:370	arg1	responses					384:392	responses	384:392	responses	384:392	Owing to the physiological importance of NEP in the modulation of nociceptive and pressor responses, there is considerable interest in inhibitors of this enzyme as novel analgesics and antihypertensive agents.
14747736	1	31	theme	major	114:118	arg1	enzyme					120:125	the major enzyme	110:125	the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor	110:291	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor.
14747736	1	31	theme	major	114:118	arg1	endopeptidase					87:99	Neutral endopeptidase	79:99	Neutral endopeptidase (NEP)	79:105	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor.
14747736	3	32	theme	crystal	514:520	arg1	structures					522:531	the crystal structures	510:531	the crystal structures of the soluble extracellular domain of human NEP (residues 52-749) complexed with various potent and competitive inhibitors	510:655	Here, the crystal structures of the soluble extracellular domain of human NEP (residues 52-749) complexed with various potent and competitive inhibitors are described.
14747736	3	33	theme	competitive	634:644	arg1	inhibitors					646:655	various potent and competitive inhibitors	615:655	various potent and competitive inhibitors	615:655	Here, the crystal structures of the soluble extracellular domain of human NEP (residues 52-749) complexed with various potent and competitive inhibitors are described.
14747736	4	34	theme	different	732:740	arg1	groups					757:762	the different zinc-chelating groups	728:762	the different zinc-chelating groups	728:762	The structures unambiguously reveal the binding mode of the different zinc-chelating groups and the subsite specificity of the enzyme.
14747736	4	35	theme	binding	712:718	arg1	mode					720:723	the binding mode	708:723	the binding mode of the different zinc-chelating groups	708:762	The structures unambiguously reveal the binding mode of the different zinc-chelating groups and the subsite specificity of the enzyme.
14747736	2	36	theme	physiological	307:319	arg1	importance					321:330	the physiological importance	303:330	the physiological importance of NEP in the modulation of nociceptive and pressor responses	303:392	Owing to the physiological importance of NEP in the modulation of nociceptive and pressor responses, there is considerable interest in inhibitors of this enzyme as novel analgesics and antihypertensive agents.
14747736	2	37	theme	antihypertensive	479:494	arg1	agents					496:501	antihypertensive agents	479:501	antihypertensive agents	479:501	Owing to the physiological importance of NEP in the modulation of nociceptive and pressor responses, there is considerable interest in inhibitors of this enzyme as novel analgesics and antihypertensive agents.
14747736	4	38	theme	enzyme	799:804	arg1	specificity					780:790	the subsite specificity	768:790	the subsite specificity of the enzyme	768:804	The structures unambiguously reveal the binding mode of the different zinc-chelating groups and the subsite specificity of the enzyme.
14747736	4	38	theme	enzyme	799:804	arg1	mode					720:723	the binding mode	708:723	the binding mode of the different zinc-chelating groups	708:762	The structures unambiguously reveal the binding mode of the different zinc-chelating groups and the subsite specificity of the enzyme.
14747736	0	39	theme	potent	60:65	arg1	inhibitors					67:76	various specific and potent inhibitors	39:76	various specific and potent inhibitors	39:76	Structural analysis of neprilysin with various specific and potent inhibitors.
14747736	2	40	from	interest	417:424	arg1	inhibitors					429:438	inhibitors	429:438	inhibitors of this enzyme as novel analgesics and antihypertensive agents	429:501	Owing to the physiological importance of NEP in the modulation of nociceptive and pressor responses, there is considerable interest in inhibitors of this enzyme as novel analgesics and antihypertensive agents.
14747736	1	41	theme	substance	227:235	arg1	P					237:237	substance P	227:237	substance P	227:237	Neutral endopeptidase (NEP) is the major enzyme involved in the metabolic inactivation of a number of bioactive peptides including the enkephalins, substance P, endothelin, bradykinin and atrial natriuretic factor.
32025030	4	0	theme	3.5 Å	667:671	arg1	resolution					639:648	a resolution	637:648	a resolution	637:648	Here we present the structure of full-length human thyroglobulin at a resolution of approximately 3.5 Å, determined by cryo-electron microscopy.
32025030	5	1	theme	hormonogenic	739:750	arg1	pairs					761:765	the hormonogenic tyrosine pairs	735:765	the hormonogenic tyrosine pairs in the structure	735:782	We identified all of the hormonogenic tyrosine pairs in the structure, and verified them using site-directed mutagenesis and in vitro hormone-production assays using human TG expressed in HEK293T cells.
32025030	1	2	from	growth	127:132	arg1	vertebrates1,2					180:193	vertebrates1,2	180:193	vertebrates1,2	180:193	Thyroglobulin (TG) is the protein precursor of thyroid hormones, which are essential for growth, development and the control of metabolism in vertebrates1,2.
32025030	7	3	from	pair	1143:1146	arg1	MBP					1200:1202	MBP	1200:1202	MBP	1200:1202	We transferred the reaction sites from TG to an engineered tyrosine donor-acceptor pair in the unrelated bacterial maltose-binding protein (MBP), which yielded hormone production with an efficiency comparable to that of TG.
32025030	7	3	from	pair	1143:1146	arg1	protein					1191:1197	the unrelated bacterial maltose-binding protein	1151:1197	the unrelated bacterial maltose-binding protein (MBP)	1151:1203	We transferred the reaction sites from TG to an engineered tyrosine donor-acceptor pair in the unrelated bacterial maltose-binding protein (MBP), which yielded hormone production with an efficiency comparable to that of TG.
32025030	6	4	theme	solvent	975:981	arg1	characteristics					1021:1035	the key characteristics	1013:1035	the key characteristics of hormonogenic sites	1013:1057	Our analysis revealed that the proximity, flexibility and solvent exposure of the tyrosines are the key characteristics of hormonogenic sites.
32025030	6	4	theme	solvent	975:981	arg1	flexibility					959:969	flexibility	959:969	flexibility	959:969	Our analysis revealed that the proximity, flexibility and solvent exposure of the tyrosines are the key characteristics of hormonogenic sites.
32025030	6	4	theme	solvent	975:981	arg1	exposure					983:990	solvent exposure	975:990	solvent exposure	975:990	Our analysis revealed that the proximity, flexibility and solvent exposure of the tyrosines are the key characteristics of hormonogenic sites.
32025030	6	4	theme	solvent	975:981	arg1	proximity					948:956	proximity	948:956	proximity	948:956	Our analysis revealed that the proximity, flexibility and solvent exposure of the tyrosines are the key characteristics of hormonogenic sites.
32025030	5	5	from	pairs	761:765	arg1	structure					774:782	the structure	770:782	the structure	770:782	We identified all of the hormonogenic tyrosine pairs in the structure, and verified them using site-directed mutagenesis and in vitro hormone-production assays using human TG expressed in HEK293T cells.
32025030	3	6	theme	structure	511:519	arg1	lack					483:486	the lack	479:486	the lack of a three-dimensional structure of TG	479:525	Tyrosine proximity within TG is thought to enable the coupling reaction but hormonogenic tyrosines have not been clearly identified, and the lack of a three-dimensional structure of TG has prevented mechanistic understanding4.
32025030	7	7	theme	bacterial	1165:1173	arg1	MBP					1200:1202	MBP	1200:1202	MBP	1200:1202	We transferred the reaction sites from TG to an engineered tyrosine donor-acceptor pair in the unrelated bacterial maltose-binding protein (MBP), which yielded hormone production with an efficiency comparable to that of TG.
32025030	7	7	theme	bacterial	1165:1173	arg1	protein					1191:1197	the unrelated bacterial maltose-binding protein	1151:1197	the unrelated bacterial maltose-binding protein (MBP)	1151:1203	We transferred the reaction sites from TG to an engineered tyrosine donor-acceptor pair in the unrelated bacterial maltose-binding protein (MBP), which yielded hormone production with an efficiency comparable to that of TG.
32025030	5	8	theme	human	880:884	arg1	TG					886:887	human TG	880:887	human TG expressed in HEK293T cells	880:914	We identified all of the hormonogenic tyrosine pairs in the structure, and verified them using site-directed mutagenesis and in vitro hormone-production assays using human TG expressed in HEK293T cells.
32025030	5	9	theme	site-directed	809:821	arg1	mutagenesis					823:833	site-directed mutagenesis	809:833	site-directed mutagenesis	809:833	We identified all of the hormonogenic tyrosine pairs in the structure, and verified them using site-directed mutagenesis and in vitro hormone-production assays using human TG expressed in HEK293T cells.
32025030	7	10	theme	maltose-binding	1175:1189	arg1	MBP					1200:1202	MBP	1200:1202	MBP	1200:1202	We transferred the reaction sites from TG to an engineered tyrosine donor-acceptor pair in the unrelated bacterial maltose-binding protein (MBP), which yielded hormone production with an efficiency comparable to that of TG.
32025030	7	10	theme	maltose-binding	1175:1189	arg1	protein					1191:1197	the unrelated bacterial maltose-binding protein	1151:1197	the unrelated bacterial maltose-binding protein (MBP)	1151:1203	We transferred the reaction sites from TG to an engineered tyrosine donor-acceptor pair in the unrelated bacterial maltose-binding protein (MBP), which yielded hormone production with an efficiency comparable to that of TG.
32025030	7	11	theme	reaction	1079:1086	arg1	sites					1088:1092	the reaction sites	1075:1092	the reaction sites from TG	1075:1100	We transferred the reaction sites from TG to an engineered tyrosine donor-acceptor pair in the unrelated bacterial maltose-binding protein (MBP), which yielded hormone production with an efficiency comparable to that of TG.
32025030	3	12	theme	hormonogenic	418:429	arg1	tyrosines					431:439	hormonogenic tyrosines	418:439	hormonogenic tyrosines	418:439	Tyrosine proximity within TG is thought to enable the coupling reaction but hormonogenic tyrosines have not been clearly identified, and the lack of a three-dimensional structure of TG has prevented mechanistic understanding4.
32025030	4	13	theme	thyroglobulin	620:632	arg1	structure					589:597	the structure	585:597	the structure of full-length human thyroglobulin at a resolution of approximately 3.5 Å, determined by cryo-electron microscopy	585:711	Here we present the structure of full-length human thyroglobulin at a resolution of approximately 3.5 Å, determined by cryo-electron microscopy.
32025030	7	14	theme	donor-acceptor	1128:1141	arg1	pair					1143:1146	an engineered tyrosine donor-acceptor pair	1105:1146	an engineered tyrosine donor-acceptor pair in the unrelated bacterial maltose-binding protein (MBP), which yielded hormone production with an efficiency comparable to that of TG	1105:1281	We transferred the reaction sites from TG to an engineered tyrosine donor-acceptor pair in the unrelated bacterial maltose-binding protein (MBP), which yielded hormone production with an efficiency comparable to that of TG.
32025030	2	15	theme	thyroid	236:242	arg1	gland					244:248	the thyroid gland	232:248	the thyroid gland	232:248	Hormone synthesis from TG occurs in the thyroid gland via the iodination and coupling of pairs of tyrosines, and is completed by TG proteolysis3.
32025030	8	16	theme	hormones	1378:1385	arg1	regulation					1356:1365	regulation	1356:1365	regulation	1356:1365	Our study provides a framework to further understand the production and regulation of thyroid hormones.
32025030	8	16	theme	hormones	1378:1385	arg1	production					1341:1350	production	1341:1350	production	1341:1350	Our study provides a framework to further understand the production and regulation of thyroid hormones.
32025030	4	17	theme	human	614:618	arg1	thyroglobulin					620:632	full-length human thyroglobulin	602:632	full-length human thyroglobulin	602:632	Here we present the structure of full-length human thyroglobulin at a resolution of approximately 3.5 Å, determined by cryo-electron microscopy.
32025030	7	18	theme	unrelated	1155:1163	arg1	MBP					1200:1202	MBP	1200:1202	MBP	1200:1202	We transferred the reaction sites from TG to an engineered tyrosine donor-acceptor pair in the unrelated bacterial maltose-binding protein (MBP), which yielded hormone production with an efficiency comparable to that of TG.
32025030	7	18	theme	unrelated	1155:1163	arg1	protein					1191:1197	the unrelated bacterial maltose-binding protein	1151:1197	the unrelated bacterial maltose-binding protein (MBP)	1151:1203	We transferred the reaction sites from TG to an engineered tyrosine donor-acceptor pair in the unrelated bacterial maltose-binding protein (MBP), which yielded hormone production with an efficiency comparable to that of TG.
32025030	8	19	dep	production	1341:1350	arg1	the					1337:1339	the	1337:1339	the	1337:1339	Our study provides a framework to further understand the production and regulation of thyroid hormones.
32025030	1	20	theme	protein	64:70	arg1	precursor					72:80	the protein precursor	60:80	the protein precursor of thyroid hormones, which are essential for growth, development and the control of metabolism in vertebrates1,2	60:193	Thyroglobulin (TG) is the protein precursor of thyroid hormones, which are essential for growth, development and the control of metabolism in vertebrates1,2.
32025030	1	20	theme	protein	64:70	arg1	Thyroglobulin					38:50	Thyroglobulin	38:50	Thyroglobulin (TG)	38:55	Thyroglobulin (TG) is the protein precursor of thyroid hormones, which are essential for growth, development and the control of metabolism in vertebrates1,2.
32025030	7	21	theme	comparable	1258:1267	arg1	efficiency					1247:1256	an efficiency	1244:1256	an efficiency comparable to that of TG	1244:1281	We transferred the reaction sites from TG to an engineered tyrosine donor-acceptor pair in the unrelated bacterial maltose-binding protein (MBP), which yielded hormone production with an efficiency comparable to that of TG.
32025030	6	22	theme	sites	1053:1057	arg1	characteristics					1021:1035	the key characteristics	1013:1035	the key characteristics of hormonogenic sites	1013:1057	Our analysis revealed that the proximity, flexibility and solvent exposure of the tyrosines are the key characteristics of hormonogenic sites.
32025030	6	22	theme	sites	1053:1057	arg1	flexibility					959:969	flexibility	959:969	flexibility	959:969	Our analysis revealed that the proximity, flexibility and solvent exposure of the tyrosines are the key characteristics of hormonogenic sites.
32025030	6	22	theme	sites	1053:1057	arg1	exposure					983:990	solvent exposure	975:990	solvent exposure	975:990	Our analysis revealed that the proximity, flexibility and solvent exposure of the tyrosines are the key characteristics of hormonogenic sites.
32025030	6	22	theme	sites	1053:1057	arg1	proximity					948:956	proximity	948:956	proximity	948:956	Our analysis revealed that the proximity, flexibility and solvent exposure of the tyrosines are the key characteristics of hormonogenic sites.
32025030	3	23	theme	Tyrosine	342:349	arg1	proximity					351:359	Tyrosine proximity	342:359	Tyrosine proximity within TG	342:369	Tyrosine proximity within TG is thought to enable the coupling reaction but hormonogenic tyrosines have not been clearly identified, and the lack of a three-dimensional structure of TG has prevented mechanistic understanding4.
32025030	3	24	theme	TG	524:525	arg1	structure					511:519	a three-dimensional structure	491:519	a three-dimensional structure of TG	491:525	Tyrosine proximity within TG is thought to enable the coupling reaction but hormonogenic tyrosines have not been clearly identified, and the lack of a three-dimensional structure of TG has prevented mechanistic understanding4.
32025030	2	25	theme	TG	325:326	arg1	proteolysis3					328:339	TG proteolysis3	325:339	TG proteolysis3	325:339	Hormone synthesis from TG occurs in the thyroid gland via the iodination and coupling of pairs of tyrosines, and is completed by TG proteolysis3.
32025030	0	26	theme	human	17:21	arg1	thyroglobulin					23:35	human thyroglobulin	17:35	human thyroglobulin	17:35	The structure of human thyroglobulin.
32025030	3	27	theme	three-dimensional	493:509	arg1	structure					511:519	a three-dimensional structure	491:519	a three-dimensional structure of TG	491:525	Tyrosine proximity within TG is thought to enable the coupling reaction but hormonogenic tyrosines have not been clearly identified, and the lack of a three-dimensional structure of TG has prevented mechanistic understanding4.
32025030	2	28	from	TG	219:220	arg1	synthesis					204:212	Hormone synthesis	196:212	Hormone synthesis from TG	196:220	Hormone synthesis from TG occurs in the thyroid gland via the iodination and coupling of pairs of tyrosines, and is completed by TG proteolysis3.
32025030	1	29	theme	thyroid	85:91	arg1	hormones					93:100	thyroid hormones	85:100	thyroid hormones	85:100	Thyroglobulin (TG) is the protein precursor of thyroid hormones, which are essential for growth, development and the control of metabolism in vertebrates1,2.
32025030	1	30	theme	metabolism	166:175	arg1	development					135:145	development	135:145	development	135:145	Thyroglobulin (TG) is the protein precursor of thyroid hormones, which are essential for growth, development and the control of metabolism in vertebrates1,2.
32025030	1	30	theme	metabolism	166:175	arg1	control					155:161	the control	151:161	the control of metabolism in vertebrates1,2	151:193	Thyroglobulin (TG) is the protein precursor of thyroid hormones, which are essential for growth, development and the control of metabolism in vertebrates1,2.
32025030	1	30	theme	metabolism	166:175	arg1	growth					127:132	growth	127:132	growth	127:132	Thyroglobulin (TG) is the protein precursor of thyroid hormones, which are essential for growth, development and the control of metabolism in vertebrates1,2.
32025030	5	31	theme	tyrosine	752:759	arg1	pairs					761:765	the hormonogenic tyrosine pairs	735:765	the hormonogenic tyrosine pairs in the structure	735:782	We identified all of the hormonogenic tyrosine pairs in the structure, and verified them using site-directed mutagenesis and in vitro hormone-production assays using human TG expressed in HEK293T cells.
32025030	2	32	dep	iodination	258:267	arg1	the					254:256	the	254:256	the	254:256	Hormone synthesis from TG occurs in the thyroid gland via the iodination and coupling of pairs of tyrosines, and is completed by TG proteolysis3.
32025030	4	33	theme	full-length	602:612	arg1	thyroglobulin					620:632	full-length human thyroglobulin	602:632	full-length human thyroglobulin	602:632	Here we present the structure of full-length human thyroglobulin at a resolution of approximately 3.5 Å, determined by cryo-electron microscopy.
32025030	3	34	theme	mechanistic	541:551	arg1	understanding4					553:566	mechanistic understanding4	541:566	mechanistic understanding4	541:566	Tyrosine proximity within TG is thought to enable the coupling reaction but hormonogenic tyrosines have not been clearly identified, and the lack of a three-dimensional structure of TG has prevented mechanistic understanding4.
32025030	5	35	theme	hormone-production	848:865	arg1	assays					867:872	in vitro hormone-production assays	839:872	in vitro hormone-production assays using human TG expressed in HEK293T cells	839:914	We identified all of the hormonogenic tyrosine pairs in the structure, and verified them using site-directed mutagenesis and in vitro hormone-production assays using human TG expressed in HEK293T cells.
32025030	3	36	theme	coupling	396:403	arg1	reaction					405:412	the coupling reaction	392:412	the coupling reaction	392:412	Tyrosine proximity within TG is thought to enable the coupling reaction but hormonogenic tyrosines have not been clearly identified, and the lack of a three-dimensional structure of TG has prevented mechanistic understanding4.
32025030	0	37	theme	thyroglobulin	23:35	arg1	structure					4:12	The structure	0:12	The structure of human thyroglobulin	0:35	The structure of human thyroglobulin.
32025030	8	38	theme	thyroid	1370:1376	arg1	hormones					1378:1385	thyroid hormones	1370:1385	thyroid hormones	1370:1385	Our study provides a framework to further understand the production and regulation of thyroid hormones.
32025030	7	39	theme	engineered	1108:1117	arg1	pair					1143:1146	an engineered tyrosine donor-acceptor pair	1105:1146	an engineered tyrosine donor-acceptor pair in the unrelated bacterial maltose-binding protein (MBP), which yielded hormone production with an efficiency comparable to that of TG	1105:1281	We transferred the reaction sites from TG to an engineered tyrosine donor-acceptor pair in the unrelated bacterial maltose-binding protein (MBP), which yielded hormone production with an efficiency comparable to that of TG.
32025030	7	40	from	TG	1099:1100	arg1	sites					1088:1092	the reaction sites	1075:1092	the reaction sites from TG	1075:1100	We transferred the reaction sites from TG to an engineered tyrosine donor-acceptor pair in the unrelated bacterial maltose-binding protein (MBP), which yielded hormone production with an efficiency comparable to that of TG.
32025030	2	41	theme	Hormone	196:202	arg1	synthesis					204:212	Hormone synthesis	196:212	Hormone synthesis from TG	196:220	Hormone synthesis from TG occurs in the thyroid gland via the iodination and coupling of pairs of tyrosines, and is completed by TG proteolysis3.
32025030	1	42	theme	hormones	93:100	arg1	precursor					72:80	the protein precursor	60:80	the protein precursor of thyroid hormones, which are essential for growth, development and the control of metabolism in vertebrates1,2	60:193	Thyroglobulin (TG) is the protein precursor of thyroid hormones, which are essential for growth, development and the control of metabolism in vertebrates1,2.
32025030	1	42	theme	hormones	93:100	arg1	Thyroglobulin					38:50	Thyroglobulin	38:50	Thyroglobulin (TG)	38:55	Thyroglobulin (TG) is the protein precursor of thyroid hormones, which are essential for growth, development and the control of metabolism in vertebrates1,2.
32025030	7	43	theme	tyrosine	1119:1126	arg1	pair					1143:1146	an engineered tyrosine donor-acceptor pair	1105:1146	an engineered tyrosine donor-acceptor pair in the unrelated bacterial maltose-binding protein (MBP), which yielded hormone production with an efficiency comparable to that of TG	1105:1281	We transferred the reaction sites from TG to an engineered tyrosine donor-acceptor pair in the unrelated bacterial maltose-binding protein (MBP), which yielded hormone production with an efficiency comparable to that of TG.
32025030	5	44	dep	in	839:840	arg1	vitro					842:846	vitro	842:846	vitro	842:846	We identified all of the hormonogenic tyrosine pairs in the structure, and verified them using site-directed mutagenesis and in vitro hormone-production assays using human TG expressed in HEK293T cells.
32025030	2	45	theme	tyrosines	294:302	arg1	pairs					285:289	pairs	285:289	pairs of tyrosines	285:302	Hormone synthesis from TG occurs in the thyroid gland via the iodination and coupling of pairs of tyrosines, and is completed by TG proteolysis3.
32025030	6	46	theme	tyrosines	999:1007	arg1	characteristics					1021:1035	the key characteristics	1013:1035	the key characteristics of hormonogenic sites	1013:1057	Our analysis revealed that the proximity, flexibility and solvent exposure of the tyrosines are the key characteristics of hormonogenic sites.
32025030	6	46	theme	tyrosines	999:1007	arg1	flexibility					959:969	flexibility	959:969	flexibility	959:969	Our analysis revealed that the proximity, flexibility and solvent exposure of the tyrosines are the key characteristics of hormonogenic sites.
32025030	6	46	theme	tyrosines	999:1007	arg1	exposure					983:990	solvent exposure	975:990	solvent exposure	975:990	Our analysis revealed that the proximity, flexibility and solvent exposure of the tyrosines are the key characteristics of hormonogenic sites.
32025030	6	46	theme	tyrosines	999:1007	arg1	proximity					948:956	proximity	948:956	proximity	948:956	Our analysis revealed that the proximity, flexibility and solvent exposure of the tyrosines are the key characteristics of hormonogenic sites.
32025030	4	47	theme	cryo-electron	688:700	arg1	microscopy					702:711	cryo-electron microscopy	688:711	cryo-electron microscopy	688:711	Here we present the structure of full-length human thyroglobulin at a resolution of approximately 3.5 Å, determined by cryo-electron microscopy.
32025030	6	48	theme	hormonogenic	1040:1051	arg1	sites					1053:1057	hormonogenic sites	1040:1057	hormonogenic sites	1040:1057	Our analysis revealed that the proximity, flexibility and solvent exposure of the tyrosines are the key characteristics of hormonogenic sites.
32025030	2	49	theme	pairs	285:289	arg1	coupling					273:280	coupling	273:280	coupling	273:280	Hormone synthesis from TG occurs in the thyroid gland via the iodination and coupling of pairs of tyrosines, and is completed by TG proteolysis3.
32025030	2	49	theme	pairs	285:289	arg1	iodination					258:267	iodination	258:267	iodination	258:267	Hormone synthesis from TG occurs in the thyroid gland via the iodination and coupling of pairs of tyrosines, and is completed by TG proteolysis3.
32025030	5	50	theme	HEK293T	902:908	arg1	cells					910:914	HEK293T cells	902:914	HEK293T cells	902:914	We identified all of the hormonogenic tyrosine pairs in the structure, and verified them using site-directed mutagenesis and in vitro hormone-production assays using human TG expressed in HEK293T cells.
32025030	4	51	from	resolution	639:648	arg1	structure					589:597	the structure	585:597	the structure of full-length human thyroglobulin at a resolution of approximately 3.5 Å, determined by cryo-electron microscopy	585:711	Here we present the structure of full-length human thyroglobulin at a resolution of approximately 3.5 Å, determined by cryo-electron microscopy.
32025030	1	52	from	control	155:161	arg1	vertebrates1,2					180:193	vertebrates1,2	180:193	vertebrates1,2	180:193	Thyroglobulin (TG) is the protein precursor of thyroid hormones, which are essential for growth, development and the control of metabolism in vertebrates1,2.
32025030	5	53	theme	in	839:840	arg1	assays					867:872	in vitro hormone-production assays	839:872	in vitro hormone-production assays using human TG expressed in HEK293T cells	839:914	We identified all of the hormonogenic tyrosine pairs in the structure, and verified them using site-directed mutagenesis and in vitro hormone-production assays using human TG expressed in HEK293T cells.
32025030	1	54	from	development	135:145	arg1	vertebrates1,2					180:193	vertebrates1,2	180:193	vertebrates1,2	180:193	Thyroglobulin (TG) is the protein precursor of thyroid hormones, which are essential for growth, development and the control of metabolism in vertebrates1,2.
32025030	7	55	theme	hormone	1220:1226	arg1	production					1228:1237	hormone production	1220:1237	hormone production	1220:1237	We transferred the reaction sites from TG to an engineered tyrosine donor-acceptor pair in the unrelated bacterial maltose-binding protein (MBP), which yielded hormone production with an efficiency comparable to that of TG.
32025030	6	56	theme	key	1017:1019	arg1	characteristics					1021:1035	the key characteristics	1013:1035	the key characteristics of hormonogenic sites	1013:1057	Our analysis revealed that the proximity, flexibility and solvent exposure of the tyrosines are the key characteristics of hormonogenic sites.
32025030	6	56	theme	key	1017:1019	arg1	flexibility					959:969	flexibility	959:969	flexibility	959:969	Our analysis revealed that the proximity, flexibility and solvent exposure of the tyrosines are the key characteristics of hormonogenic sites.
32025030	6	56	theme	key	1017:1019	arg1	exposure					983:990	solvent exposure	975:990	solvent exposure	975:990	Our analysis revealed that the proximity, flexibility and solvent exposure of the tyrosines are the key characteristics of hormonogenic sites.
32025030	6	56	theme	key	1017:1019	arg1	proximity					948:956	proximity	948:956	proximity	948:956	Our analysis revealed that the proximity, flexibility and solvent exposure of the tyrosines are the key characteristics of hormonogenic sites.
1998667	5	0	theme	identical	686:694	arg1	subunits					696:703	The two identical subunits	678:703	The two identical subunits of factor XI	678:716	The two identical subunits of factor XI were connected by a single disulfide bond at Cys321 linking each of the fourth apple domains while each of the Cys residues at position 11 in the first apple domains forms a disulfide bond with another Cys residue.
1998667	5	1	theme	disulfide	745:753	arg1	bond					755:758	a single disulfide bond	736:758	a single disulfide bond at Cys321 linking each of the fourth apple domains	736:809	The two identical subunits of factor XI were connected by a single disulfide bond at Cys321 linking each of the fourth apple domains while each of the Cys residues at position 11 in the first apple domains forms a disulfide bond with another Cys residue.
1998667	2	2	theme	acid	297:300	arg1	analysis					311:318	amino acid sequence analysis	291:318	amino acid sequence analysis of peptide fragments produced by chemical and enzymatic digestion	291:384	Of the 19 disulfide bonds present in each of the subunits of the human protein, 16 were determined by amino acid sequence analysis of peptide fragments produced by chemical and enzymatic digestion.
1998667	3	3	from	present	468:474	arg1	portion					498:504	the amino-terminal portion	479:504	the amino-terminal portion of each subunit of factor XI	479:533	Four apple domains of 90 or 91 amino acids were identified in the tandem repeats present in the amino-terminal portion of each subunit of factor XI.
1998667	2	4	theme	amino	291:295	arg1	analysis					311:318	amino acid sequence analysis	291:318	amino acid sequence analysis of peptide fragments produced by chemical and enzymatic digestion	291:384	Of the 19 disulfide bonds present in each of the subunits of the human protein, 16 were determined by amino acid sequence analysis of peptide fragments produced by chemical and enzymatic digestion.
1998667	0	5	from	Location	0:7	arg1	XI					60:61	human coagulation factor XI	35:61	human coagulation factor XI	35:61	Location of the disulfide bonds in human coagulation factor XI: the presence of tandem apple domains.
1998667	5	6	theme	XI	715:716	arg1	subunits					696:703	The two identical subunits	678:703	The two identical subunits of factor XI	678:716	The two identical subunits of factor XI were connected by a single disulfide bond at Cys321 linking each of the fourth apple domains while each of the Cys residues at position 11 in the first apple domains forms a disulfide bond with another Cys residue.
1998667	5	7	from	Cys321	763:768	arg1	bond					755:758	a single disulfide bond	736:758	a single disulfide bond at Cys321 linking each of the fourth apple domains	736:809	The two identical subunits of factor XI were connected by a single disulfide bond at Cys321 linking each of the fourth apple domains while each of the Cys residues at position 11 in the first apple domains forms a disulfide bond with another Cys residue.
1998667	1	8	theme	plasma	117:122	arg1	XI					109:110	Factor XI	102:110	Factor XI	102:110	Factor XI is a plasma glycoprotein that participates in the blood coagulation cascade.
1998667	1	8	theme	plasma	117:122	arg1	glycoprotein					124:135	a plasma glycoprotein	115:135	a plasma glycoprotein that participates in the blood coagulation cascade	115:186	Factor XI is a plasma glycoprotein that participates in the blood coagulation cascade.
1998667	5	9	theme	Cys	829:831	arg1	residues					833:840	the Cys residues	825:840	the Cys residues at position 11 in the first apple domains	825:882	The two identical subunits of factor XI were connected by a single disulfide bond at Cys321 linking each of the fourth apple domains while each of the Cys residues at position 11 in the first apple domains forms a disulfide bond with another Cys residue.
1998667	0	10	theme	apple	87:91	arg1	domains					93:99	tandem apple domains	80:99	tandem apple domains	80:99	Location of the disulfide bonds in human coagulation factor XI: the presence of tandem apple domains.
1998667	4	11	theme	catalytic	634:642	arg1	region					644:649	the catalytic region	630:649	the catalytic region of other serine proteases	630:675	The disulfide bonds in the carboxyl-terminal portion of the molecule were similar to those in the catalytic region of other serine proteases.
1998667	5	12	theme	first	864:868	arg1	domains					876:882	the first apple domains	860:882	the first apple domains	860:882	The two identical subunits of factor XI were connected by a single disulfide bond at Cys321 linking each of the fourth apple domains while each of the Cys residues at position 11 in the first apple domains forms a disulfide bond with another Cys residue.
1998667	0	13	theme	tandem	80:85	arg1	domains					93:99	tandem apple domains	80:99	tandem apple domains	80:99	Location of the disulfide bonds in human coagulation factor XI: the presence of tandem apple domains.
1998667	3	14	theme	present	468:474	arg1	repeats					460:466	the tandem repeats	449:466	the tandem repeats present in the amino-terminal portion of each subunit of factor XI	449:533	Four apple domains of 90 or 91 amino acids were identified in the tandem repeats present in the amino-terminal portion of each subunit of factor XI.
1998667	2	15	theme	fragments	331:339	arg1	analysis					311:318	amino acid sequence analysis	291:318	amino acid sequence analysis of peptide fragments produced by chemical and enzymatic digestion	291:384	Of the 19 disulfide bonds present in each of the subunits of the human protein, 16 were determined by amino acid sequence analysis of peptide fragments produced by chemical and enzymatic digestion.
1998667	3	16	theme	tandem	453:458	arg1	repeats					460:466	the tandem repeats	449:466	the tandem repeats present in the amino-terminal portion of each subunit of factor XI	449:533	Four apple domains of 90 or 91 amino acids were identified in the tandem repeats present in the amino-terminal portion of each subunit of factor XI.
1998667	4	17	theme	serine	660:665	arg1	proteases					667:675	other serine proteases	654:675	other serine proteases	654:675	The disulfide bonds in the carboxyl-terminal portion of the molecule were similar to those in the catalytic region of other serine proteases.
1998667	2	18	theme	peptide	323:329	arg1	fragments					331:339	peptide fragments	323:339	peptide fragments produced by chemical and enzymatic digestion	323:384	Of the 19 disulfide bonds present in each of the subunits of the human protein, 16 were determined by amino acid sequence analysis of peptide fragments produced by chemical and enzymatic digestion.
1998667	3	19	attach	present	468:474	arg2	repeats					460:466	the tandem repeats	449:466	the tandem repeats present in the amino-terminal portion of each subunit of factor XI	449:533	Four apple domains of 90 or 91 amino acids were identified in the tandem repeats present in the amino-terminal portion of each subunit of factor XI.
1998667	3	19	attach	present	468:474	arg1	portion					498:504	the amino-terminal portion	479:504	the amino-terminal portion of each subunit of factor XI	479:533	Four apple domains of 90 or 91 amino acids were identified in the tandem repeats present in the amino-terminal portion of each subunit of factor XI.
1998667	2	20	theme	protein	260:266	arg1	subunits					238:245	the subunits	234:245	the subunits of the human protein	234:266	Of the 19 disulfide bonds present in each of the subunits of the human protein, 16 were determined by amino acid sequence analysis of peptide fragments produced by chemical and enzymatic digestion.
1998667	2	21	from	present	215:221	arg1	subunits					238:245	the subunits	234:245	the subunits of the human protein	234:266	Of the 19 disulfide bonds present in each of the subunits of the human protein, 16 were determined by amino acid sequence analysis of peptide fragments produced by chemical and enzymatic digestion.
1998667	2	21	from	present	215:221	arg1	each					226:229	each	226:229	each	226:229	Of the 19 disulfide bonds present in each of the subunits of the human protein, 16 were determined by amino acid sequence analysis of peptide fragments produced by chemical and enzymatic digestion.
1998667	3	22	from	portion	498:504	arg1	present					468:474	present	468:474	present	468:474	Four apple domains of 90 or 91 amino acids were identified in the tandem repeats present in the amino-terminal portion of each subunit of factor XI.
1998667	0	23	theme	disulfide	16:24	arg1	bonds					26:30	the disulfide bonds	12:30	the disulfide bonds	12:30	Location of the disulfide bonds in human coagulation factor XI: the presence of tandem apple domains.
1998667	2	24	theme	human	254:258	arg1	protein					260:266	the human protein	250:266	the human protein	250:266	Of the 19 disulfide bonds present in each of the subunits of the human protein, 16 were determined by amino acid sequence analysis of peptide fragments produced by chemical and enzymatic digestion.
1998667	3	25	theme	factor	525:530	arg1	XI					532:533	factor XI	525:533	factor XI	525:533	Four apple domains of 90 or 91 amino acids were identified in the tandem repeats present in the amino-terminal portion of each subunit of factor XI.
1998667	1	26	theme	blood	162:166	arg1	cascade					180:186	the blood coagulation cascade	158:186	the blood coagulation cascade	158:186	Factor XI is a plasma glycoprotein that participates in the blood coagulation cascade.
1998667	4	27	theme	other	654:658	arg1	proteases					667:675	other serine proteases	654:675	other serine proteases	654:675	The disulfide bonds in the carboxyl-terminal portion of the molecule were similar to those in the catalytic region of other serine proteases.
1998667	0	28	theme	domains	93:99	arg1	presence					68:75	the presence	64:75	Location of the disulfide bonds in human coagulation factor XI: the presence of tandem apple domains.	0:100	Location of the disulfide bonds in human coagulation factor XI: the presence of tandem apple domains.
1998667	4	29	theme	proteases	667:675	arg1	region					644:649	the catalytic region	630:649	the catalytic region of other serine proteases	630:675	The disulfide bonds in the carboxyl-terminal portion of the molecule were similar to those in the catalytic region of other serine proteases.
1998667	2	30	from	each	226:229	arg1	present					215:221	present	215:221	present	215:221	Of the 19 disulfide bonds present in each of the subunits of the human protein, 16 were determined by amino acid sequence analysis of peptide fragments produced by chemical and enzymatic digestion.
1998667	1	31	theme	coagulation	168:178	arg1	cascade					180:186	the blood coagulation cascade	158:186	the blood coagulation cascade	158:186	Factor XI is a plasma glycoprotein that participates in the blood coagulation cascade.
1998667	2	32	theme	disulfide	199:207	arg1	bonds					209:213	the 19 disulfide bonds	192:213	the 19 disulfide bonds present in each of the subunits of the human protein	192:266	Of the 19 disulfide bonds present in each of the subunits of the human protein, 16 were determined by amino acid sequence analysis of peptide fragments produced by chemical and enzymatic digestion.
1998667	4	33	theme	molecule	596:603	arg1	portion					581:587	the carboxyl-terminal portion	559:587	the carboxyl-terminal portion of the molecule	559:603	The disulfide bonds in the carboxyl-terminal portion of the molecule were similar to those in the catalytic region of other serine proteases.
1998667	2	34	theme	chemical	353:360	arg1	digestion					376:384	chemical and enzymatic digestion	353:384	chemical and enzymatic digestion	353:384	Of the 19 disulfide bonds present in each of the subunits of the human protein, 16 were determined by amino acid sequence analysis of peptide fragments produced by chemical and enzymatic digestion.
1998667	0	35	theme	bonds	26:30	arg1	Location					0:7	Location	0:7	Location of the disulfide bonds in human coagulation factor XI: the presence of tandem apple domains.	0:100	Location of the disulfide bonds in human coagulation factor XI: the presence of tandem apple domains.
1998667	5	36	theme	factor	708:713	arg1	XI					715:716	factor XI	708:716	factor XI	708:716	The two identical subunits of factor XI were connected by a single disulfide bond at Cys321 linking each of the fourth apple domains while each of the Cys residues at position 11 in the first apple domains forms a disulfide bond with another Cys residue.
1998667	3	37	theme	XI	532:533	arg1	subunit					514:520	each subunit	509:520	each subunit of factor XI	509:533	Four apple domains of 90 or 91 amino acids were identified in the tandem repeats present in the amino-terminal portion of each subunit of factor XI.
1998667	4	38	theme	carboxyl-terminal	563:579	arg1	portion					581:587	the carboxyl-terminal portion	559:587	the carboxyl-terminal portion of the molecule	559:603	The disulfide bonds in the carboxyl-terminal portion of the molecule were similar to those in the catalytic region of other serine proteases.
1998667	0	39	theme	coagulation	41:51	arg1	XI					60:61	human coagulation factor XI	35:61	human coagulation factor XI	35:61	Location of the disulfide bonds in human coagulation factor XI: the presence of tandem apple domains.
1998667	3	40	theme	subunit	514:520	arg1	portion					498:504	the amino-terminal portion	479:504	the amino-terminal portion of each subunit of factor XI	479:533	Four apple domains of 90 or 91 amino acids were identified in the tandem repeats present in the amino-terminal portion of each subunit of factor XI.
1998667	4	41	theme	disulfide	540:548	arg1	similar					610:616	similar	610:616	similar	610:616	The disulfide bonds in the carboxyl-terminal portion of the molecule were similar to those in the catalytic region of other serine proteases.
1998667	4	41	theme	disulfide	540:548	arg1	bonds					550:554	The disulfide bonds	536:554	The disulfide bonds in the carboxyl-terminal portion of the molecule	536:603	The disulfide bonds in the carboxyl-terminal portion of the molecule were similar to those in the catalytic region of other serine proteases.
1998667	3	42	theme	acids	424:428	arg1	acids					424:428	90 or 91 amino acids	409:428	90 or 91 amino acids	409:428	Four apple domains of 90 or 91 amino acids were identified in the tandem repeats present in the amino-terminal portion of each subunit of factor XI.
1998667	3	42	theme	acids	424:428	arg1	domains					398:404	Four apple domains	387:404	Four apple domains of 90 or 91 amino acids	387:428	Four apple domains of 90 or 91 amino acids were identified in the tandem repeats present in the amino-terminal portion of each subunit of factor XI.
1998667	0	43	theme	human	35:39	arg1	XI					60:61	human coagulation factor XI	35:61	human coagulation factor XI	35:61	Location of the disulfide bonds in human coagulation factor XI: the presence of tandem apple domains.
1998667	5	44	theme	Cys	920:922	arg1	residue					924:930	another Cys residue	912:930	another Cys residue	912:930	The two identical subunits of factor XI were connected by a single disulfide bond at Cys321 linking each of the fourth apple domains while each of the Cys residues at position 11 in the first apple domains forms a disulfide bond with another Cys residue.
1998667	5	45	from	position	845:852	arg1	residues					833:840	the Cys residues	825:840	the Cys residues at position 11 in the first apple domains	825:882	The two identical subunits of factor XI were connected by a single disulfide bond at Cys321 linking each of the fourth apple domains while each of the Cys residues at position 11 in the first apple domains forms a disulfide bond with another Cys residue.
1998667	5	45	from	position	845:852	arg1	domains					876:882	the first apple domains	860:882	the first apple domains	860:882	The two identical subunits of factor XI were connected by a single disulfide bond at Cys321 linking each of the fourth apple domains while each of the Cys residues at position 11 in the first apple domains forms a disulfide bond with another Cys residue.
1998667	5	46	theme	disulfide	892:900	arg1	bond					902:905	a disulfide bond	890:905	a disulfide bond with another Cys residue	890:930	The two identical subunits of factor XI were connected by a single disulfide bond at Cys321 linking each of the fourth apple domains while each of the Cys residues at position 11 in the first apple domains forms a disulfide bond with another Cys residue.
1998667	1	47	gly	glycoprotein	124:135	arg1	XI					109:110	Factor XI	102:110	Factor XI	102:110	Factor XI is a plasma glycoprotein that participates in the blood coagulation cascade.
1998667	1	47	gly	glycoprotein	124:135	arg1	glycoprotein					124:135	a plasma glycoprotein	115:135	a plasma glycoprotein that participates in the blood coagulation cascade	115:186	Factor XI is a plasma glycoprotein that participates in the blood coagulation cascade.
1998667	5	48	with	bond	902:905	arg1	residue					924:930	another Cys residue	912:930	another Cys residue	912:930	The two identical subunits of factor XI were connected by a single disulfide bond at Cys321 linking each of the fourth apple domains while each of the Cys residues at position 11 in the first apple domains forms a disulfide bond with another Cys residue.
1998667	1	49	theme	Factor	102:107	arg1	XI					109:110	Factor XI	102:110	Factor XI	102:110	Factor XI is a plasma glycoprotein that participates in the blood coagulation cascade.
1998667	1	49	theme	Factor	102:107	arg1	glycoprotein					124:135	a plasma glycoprotein	115:135	a plasma glycoprotein that participates in the blood coagulation cascade	115:186	Factor XI is a plasma glycoprotein that participates in the blood coagulation cascade.
1998667	3	50	theme	amino-terminal	483:496	arg1	portion					498:504	the amino-terminal portion	479:504	the amino-terminal portion of each subunit of factor XI	479:533	Four apple domains of 90 or 91 amino acids were identified in the tandem repeats present in the amino-terminal portion of each subunit of factor XI.
1998667	5	51	theme	apple	870:874	arg1	domains					876:882	the first apple domains	860:882	the first apple domains	860:882	The two identical subunits of factor XI were connected by a single disulfide bond at Cys321 linking each of the fourth apple domains while each of the Cys residues at position 11 in the first apple domains forms a disulfide bond with another Cys residue.
1998667	5	52	theme	single	738:743	arg1	bond					755:758	a single disulfide bond	736:758	a single disulfide bond at Cys321 linking each of the fourth apple domains	736:809	The two identical subunits of factor XI were connected by a single disulfide bond at Cys321 linking each of the fourth apple domains while each of the Cys residues at position 11 in the first apple domains forms a disulfide bond with another Cys residue.
1998667	3	53	theme	amino	418:422	arg1	acids					424:428	90 or 91 amino acids	409:428	90 or 91 amino acids	409:428	Four apple domains of 90 or 91 amino acids were identified in the tandem repeats present in the amino-terminal portion of each subunit of factor XI.
1998667	4	54	from	bonds	550:554	arg1	portion					581:587	the carboxyl-terminal portion	559:587	the carboxyl-terminal portion of the molecule	559:603	The disulfide bonds in the carboxyl-terminal portion of the molecule were similar to those in the catalytic region of other serine proteases.
1998667	5	55	theme	apple	797:801	arg1	domains					803:809	the fourth apple domains	786:809	the fourth apple domains	786:809	The two identical subunits of factor XI were connected by a single disulfide bond at Cys321 linking each of the fourth apple domains while each of the Cys residues at position 11 in the first apple domains forms a disulfide bond with another Cys residue.
1998667	2	56	theme	present	215:221	arg1	bonds					209:213	the 19 disulfide bonds	192:213	the 19 disulfide bonds present in each of the subunits of the human protein	192:266	Of the 19 disulfide bonds present in each of the subunits of the human protein, 16 were determined by amino acid sequence analysis of peptide fragments produced by chemical and enzymatic digestion.
1998667	2	57	theme	enzymatic	366:374	arg1	digestion					376:384	chemical and enzymatic digestion	353:384	chemical and enzymatic digestion	353:384	Of the 19 disulfide bonds present in each of the subunits of the human protein, 16 were determined by amino acid sequence analysis of peptide fragments produced by chemical and enzymatic digestion.
1998667	5	58	theme	fourth	790:795	arg1	domains					803:809	the fourth apple domains	786:809	the fourth apple domains	786:809	The two identical subunits of factor XI were connected by a single disulfide bond at Cys321 linking each of the fourth apple domains while each of the Cys residues at position 11 in the first apple domains forms a disulfide bond with another Cys residue.
1998667	3	59	theme	apple	392:396	arg1	acids					424:428	90 or 91 amino acids	409:428	90 or 91 amino acids	409:428	Four apple domains of 90 or 91 amino acids were identified in the tandem repeats present in the amino-terminal portion of each subunit of factor XI.
1998667	3	59	theme	apple	392:396	arg1	domains					398:404	Four apple domains	387:404	Four apple domains of 90 or 91 amino acids	387:428	Four apple domains of 90 or 91 amino acids were identified in the tandem repeats present in the amino-terminal portion of each subunit of factor XI.
1998667	0	60	theme	factor	53:58	arg1	XI					60:61	human coagulation factor XI	35:61	human coagulation factor XI	35:61	Location of the disulfide bonds in human coagulation factor XI: the presence of tandem apple domains.
1998667	0	61	dep	Location	0:7	arg1	presence					68:75	the presence	64:75	Location of the disulfide bonds in human coagulation factor XI: the presence of tandem apple domains.	0:100	Location of the disulfide bonds in human coagulation factor XI: the presence of tandem apple domains.
1998667	2	62	theme	sequence	302:309	arg1	analysis					311:318	amino acid sequence analysis	291:318	amino acid sequence analysis of peptide fragments produced by chemical and enzymatic digestion	291:384	Of the 19 disulfide bonds present in each of the subunits of the human protein, 16 were determined by amino acid sequence analysis of peptide fragments produced by chemical and enzymatic digestion.
1998667	2	63	attach	present	215:221	arg1	subunits					238:245	the subunits	234:245	the subunits of the human protein	234:266	Of the 19 disulfide bonds present in each of the subunits of the human protein, 16 were determined by amino acid sequence analysis of peptide fragments produced by chemical and enzymatic digestion.
1998667	2	63	attach	present	215:221	arg2	bonds					209:213	the 19 disulfide bonds	192:213	the 19 disulfide bonds present in each of the subunits of the human protein	192:266	Of the 19 disulfide bonds present in each of the subunits of the human protein, 16 were determined by amino acid sequence analysis of peptide fragments produced by chemical and enzymatic digestion.
1998667	2	63	attach	present	215:221	arg1	each					226:229	each	226:229	each	226:229	Of the 19 disulfide bonds present in each of the subunits of the human protein, 16 were determined by amino acid sequence analysis of peptide fragments produced by chemical and enzymatic digestion.
16859706	0	0	theme	Golgi	86:90	arg1	compartment					92:102	the Golgi compartment	82:102	the Golgi compartment	82:102	Human TPST1 transmembrane domain triggers enzyme dimerisation and localisation to the Golgi compartment.
16859706	8	1	theme	human	1213:1217	arg1	sulfotransferase					1234:1249	the human tyrosylprotein sulfotransferase	1209:1249	the human tyrosylprotein sulfotransferase	1209:1249	Further in vivo FRET studies using the transmembrane domain suggest that the human tyrosylprotein sulfotransferase may be functional as homodimer/oligomer in the trans-Golgi compartment.
16859706	8	1	theme	human	1213:1217	arg1	functional					1258:1267	functional	1258:1267	functional	1258:1267	Further in vivo FRET studies using the transmembrane domain suggest that the human tyrosylprotein sulfotransferase may be functional as homodimer/oligomer in the trans-Golgi compartment.
16859706	5	2	theme	alanine	722:728	arg1	mutation					730:737	alanine mutation	722:737	alanine mutation of these asparagine residues	722:766	By alanine mutation of these asparagine residues, we could determine that the N-linked oligosaccharides do not have an influence on Golgi retention of TPST1.
16859706	3	3	theme	fluorescence	549:560	arg1	techniques					570:579	fluorescence imaging techniques	549:579	fluorescence imaging techniques	549:579	Golgi localisation of the enzyme in COS-7 and HeLa cells was visualised by fluorescence imaging techniques.
16859706	4	4	theme	N-linked	650:657	arg1	residues					668:675	N-linked glycosyl residues	650:675	N-linked glycosyl residues	650:675	PNGase treatment and mutational studies determined that TPST1 bears N-linked glycosyl residues exclusively at position Asn60 and Asn262.
16859706	8	5	theme	in	1144:1145	arg1	studies					1157:1163	Further in vivo FRET studies	1136:1163	Further in vivo FRET studies using the transmembrane domain	1136:1194	Further in vivo FRET studies using the transmembrane domain suggest that the human tyrosylprotein sulfotransferase may be functional as homodimer/oligomer in the trans-Golgi compartment.
16859706	3	6	theme	imaging	562:568	arg1	techniques					570:579	fluorescence imaging techniques	549:579	fluorescence imaging techniques	549:579	Golgi localisation of the enzyme in COS-7 and HeLa cells was visualised by fluorescence imaging techniques.
16859706	5	7	theme	N-linked	797:804	arg1	oligosaccharides					806:821	the N-linked oligosaccharides	793:821	the N-linked oligosaccharides	793:821	By alanine mutation of these asparagine residues, we could determine that the N-linked oligosaccharides do not have an influence on Golgi retention of TPST1.
16859706	5	8	contain	have	830:833	arg2	influence					838:846	an influence	835:846	an influence	835:846	By alanine mutation of these asparagine residues, we could determine that the N-linked oligosaccharides do not have an influence on Golgi retention of TPST1.
16859706	5	8	contain	have	830:833	arg1	oligosaccharides					806:821	the N-linked oligosaccharides	793:821	the N-linked oligosaccharides	793:821	By alanine mutation of these asparagine residues, we could determine that the N-linked oligosaccharides do not have an influence on Golgi retention of TPST1.
16859706	4	9	contain	bears	644:648	arg3	Asn262					711:716	Asn262	711:716	Asn262	711:716	PNGase treatment and mutational studies determined that TPST1 bears N-linked glycosyl residues exclusively at position Asn60 and Asn262.
16859706	4	9	contain	bears	644:648	arg2	residues					668:675	N-linked glycosyl residues	650:675	N-linked glycosyl residues	650:675	PNGase treatment and mutational studies determined that TPST1 bears N-linked glycosyl residues exclusively at position Asn60 and Asn262.
16859706	4	9	contain	bears	644:648	arg3	position					692:699	position Asn60	692:705	position Asn60	692:705	PNGase treatment and mutational studies determined that TPST1 bears N-linked glycosyl residues exclusively at position Asn60 and Asn262.
16859706	4	9	contain	bears	644:648	arg1	TPST1					638:642	TPST1	638:642	TPST1	638:642	PNGase treatment and mutational studies determined that TPST1 bears N-linked glycosyl residues exclusively at position Asn60 and Asn262.
16859706	8	10	theme	tyrosylprotein	1219:1232	arg1	sulfotransferase					1234:1249	the human tyrosylprotein sulfotransferase	1209:1249	the human tyrosylprotein sulfotransferase	1209:1249	Further in vivo FRET studies using the transmembrane domain suggest that the human tyrosylprotein sulfotransferase may be functional as homodimer/oligomer in the trans-Golgi compartment.
16859706	8	10	theme	tyrosylprotein	1219:1232	arg1	functional					1258:1267	functional	1258:1267	functional	1258:1267	Further in vivo FRET studies using the transmembrane domain suggest that the human tyrosylprotein sulfotransferase may be functional as homodimer/oligomer in the trans-Golgi compartment.
16859706	4	11	theme	glycosyl	659:666	arg1	residues					668:675	N-linked glycosyl residues	650:675	N-linked glycosyl residues	650:675	PNGase treatment and mutational studies determined that TPST1 bears N-linked glycosyl residues exclusively at position Asn60 and Asn262.
16859706	6	12	theme	TPST1	957:961	arg1	TPST1					957:961	TPST1	957:961	TPST1	957:961	In concert with N and C-terminal flanking residues, the transmembrane domain of TPST1 was determined to act in targeting and retention of the enzyme to the trans-Golgi compartment.
16859706	6	12	theme	TPST1	957:961	arg1	domain					947:952	the transmembrane domain	929:952	the transmembrane domain of TPST1	929:961	In concert with N and C-terminal flanking residues, the transmembrane domain of TPST1 was determined to act in targeting and retention of the enzyme to the trans-Golgi compartment.
16859706	3	13	theme	HeLa	520:523	arg1	cells					525:529	HeLa cells	520:529	HeLa cells	520:529	Golgi localisation of the enzyme in COS-7 and HeLa cells was visualised by fluorescence imaging techniques.
16859706	2	14	theme	general	303:309	arg1	understanding					311:323	a general understanding	301:323	a general understanding of the cellular role of human tyrosine-directed sulfotransferases	301:389	To achieve a general understanding of the cellular role of human tyrosine-directed sulfotransferases, we investigated targeting, structure and posttranslational modification of TPST1.
16859706	8	15	dep	in	1144:1145	arg1	vivo					1147:1150	vivo	1147:1150	vivo	1147:1150	Further in vivo FRET studies using the transmembrane domain suggest that the human tyrosylprotein sulfotransferase may be functional as homodimer/oligomer in the trans-Golgi compartment.
16859706	6	16	theme	trans-Golgi	1033:1043	arg1	compartment					1045:1055	the trans-Golgi compartment	1029:1055	the trans-Golgi compartment	1029:1055	In concert with N and C-terminal flanking residues, the transmembrane domain of TPST1 was determined to act in targeting and retention of the enzyme to the trans-Golgi compartment.
16859706	8	17	theme	trans-Golgi	1298:1308	arg1	compartment					1310:1320	the trans-Golgi compartment	1294:1320	the trans-Golgi compartment	1294:1320	Further in vivo FRET studies using the transmembrane domain suggest that the human tyrosylprotein sulfotransferase may be functional as homodimer/oligomer in the trans-Golgi compartment.
16859706	2	18	theme	posttranslational	433:449	arg1	modification					451:462	posttranslational modification	433:462	posttranslational modification	433:462	To achieve a general understanding of the cellular role of human tyrosine-directed sulfotransferases, we investigated targeting, structure and posttranslational modification of TPST1.
16859706	0	19	theme	TPST1	6:10	arg1	domain					26:31	Human TPST1 transmembrane domain	0:31	Human TPST1 transmembrane domain	0:31	Human TPST1 transmembrane domain triggers enzyme dimerisation and localisation to the Golgi compartment.
16859706	8	20	theme	Further	1136:1142	arg1	studies					1157:1163	Further in vivo FRET studies	1136:1163	Further in vivo FRET studies using the transmembrane domain	1136:1194	Further in vivo FRET studies using the transmembrane domain suggest that the human tyrosylprotein sulfotransferase may be functional as homodimer/oligomer in the trans-Golgi compartment.
16859706	0	21	theme	Human	0:4	arg1	domain					26:31	Human TPST1 transmembrane domain	0:31	Human TPST1 transmembrane domain	0:31	Human TPST1 transmembrane domain triggers enzyme dimerisation and localisation to the Golgi compartment.
16859706	2	22	theme	role	341:344	arg1	understanding					311:323	a general understanding	301:323	a general understanding of the cellular role of human tyrosine-directed sulfotransferases	301:389	To achieve a general understanding of the cellular role of human tyrosine-directed sulfotransferases, we investigated targeting, structure and posttranslational modification of TPST1.
16859706	2	23	theme	cellular	332:339	arg1	role					341:344	the cellular role	328:344	the cellular role of human tyrosine-directed sulfotransferases	328:389	To achieve a general understanding of the cellular role of human tyrosine-directed sulfotransferases, we investigated targeting, structure and posttranslational modification of TPST1.
16859706	0	24	theme	transmembrane	12:24	arg1	domain					26:31	Human TPST1 transmembrane domain	0:31	Human TPST1 transmembrane domain	0:31	Human TPST1 transmembrane domain triggers enzyme dimerisation and localisation to the Golgi compartment.
16859706	6	25	theme	enzyme	1019:1024	arg1	retention					1002:1010	retention	1002:1010	retention	1002:1010	In concert with N and C-terminal flanking residues, the transmembrane domain of TPST1 was determined to act in targeting and retention of the enzyme to the trans-Golgi compartment.
16859706	6	25	theme	enzyme	1019:1024	arg1	targeting					988:996	targeting	988:996	targeting	988:996	In concert with N and C-terminal flanking residues, the transmembrane domain of TPST1 was determined to act in targeting and retention of the enzyme to the trans-Golgi compartment.
16859706	5	26	link	N-linked	797:804	arg1	oligosaccharides					806:821	the N-linked oligosaccharides	793:821	the N-linked oligosaccharides	793:821	By alanine mutation of these asparagine residues, we could determine that the N-linked oligosaccharides do not have an influence on Golgi retention of TPST1.
16859706	6	27	theme	transmembrane	933:945	arg1	TPST1					957:961	TPST1	957:961	TPST1	957:961	In concert with N and C-terminal flanking residues, the transmembrane domain of TPST1 was determined to act in targeting and retention of the enzyme to the trans-Golgi compartment.
16859706	6	27	theme	transmembrane	933:945	arg1	domain					947:952	the transmembrane domain	929:952	the transmembrane domain of TPST1	929:961	In concert with N and C-terminal flanking residues, the transmembrane domain of TPST1 was determined to act in targeting and retention of the enzyme to the trans-Golgi compartment.
16859706	8	28	from	homodimer/oligomer	1272:1289	arg1	compartment					1310:1320	the trans-Golgi compartment	1294:1320	the trans-Golgi compartment	1294:1320	Further in vivo FRET studies using the transmembrane domain suggest that the human tyrosylprotein sulfotransferase may be functional as homodimer/oligomer in the trans-Golgi compartment.
16859706	1	29	theme	sulfate	223:229	arg1	moiety					231:236	the sulfate moiety	219:236	the sulfate moiety	219:236	TPST1 is a human tyrosylprotein sulfotransferase that uses 3'phosphoadenosine-5'phosphosulfate (PAPS) to transfer the sulfate moiety to proteins predominantly designated for secretion.
16859706	5	30	theme	Golgi	851:855	arg1	retention					857:865	Golgi retention	851:865	Golgi retention of TPST1	851:874	By alanine mutation of these asparagine residues, we could determine that the N-linked oligosaccharides do not have an influence on Golgi retention of TPST1.
16859706	2	31	theme	sulfotransferases	373:389	arg1	role					341:344	the cellular role	328:344	the cellular role of human tyrosine-directed sulfotransferases	328:389	To achieve a general understanding of the cellular role of human tyrosine-directed sulfotransferases, we investigated targeting, structure and posttranslational modification of TPST1.
16859706	7	32	theme	lipid	1117:1121	arg1	environment					1123:1133	a lipid environment	1115:1133	a lipid environment	1115:1133	This domain exhibits a pronounced secondary structure in a lipid environment.
16859706	2	33	theme	TPST1	467:471	arg1	structure					419:427	structure	419:427	structure	419:427	To achieve a general understanding of the cellular role of human tyrosine-directed sulfotransferases, we investigated targeting, structure and posttranslational modification of TPST1.
16859706	2	33	theme	TPST1	467:471	arg1	modification					451:462	posttranslational modification	433:462	posttranslational modification	433:462	To achieve a general understanding of the cellular role of human tyrosine-directed sulfotransferases, we investigated targeting, structure and posttranslational modification of TPST1.
16859706	2	33	theme	TPST1	467:471	arg1	targeting					408:416	targeting	408:416	targeting	408:416	To achieve a general understanding of the cellular role of human tyrosine-directed sulfotransferases, we investigated targeting, structure and posttranslational modification of TPST1.
16859706	3	34	theme	Golgi	474:478	arg1	localisation					480:491	Golgi localisation	474:491	Golgi localisation of the enzyme in COS-7 and HeLa cells	474:529	Golgi localisation of the enzyme in COS-7 and HeLa cells was visualised by fluorescence imaging techniques.
16859706	8	35	theme	FRET	1152:1155	arg1	studies					1157:1163	Further in vivo FRET studies	1136:1163	Further in vivo FRET studies using the transmembrane domain	1136:1194	Further in vivo FRET studies using the transmembrane domain suggest that the human tyrosylprotein sulfotransferase may be functional as homodimer/oligomer in the trans-Golgi compartment.
16859706	4	36	theme	PNGase	582:587	arg1	treatment					589:597	PNGase treatment	582:597	PNGase treatment	582:597	PNGase treatment and mutational studies determined that TPST1 bears N-linked glycosyl residues exclusively at position Asn60 and Asn262.
16859706	5	37	theme	asparagine	748:757	arg1	residues					759:766	these asparagine residues	742:766	these asparagine residues	742:766	By alanine mutation of these asparagine residues, we could determine that the N-linked oligosaccharides do not have an influence on Golgi retention of TPST1.
16859706	0	38	dep	enzyme	42:47	arg1	dimerisation					49:60	dimerisation	49:60	dimerisation	49:60	Human TPST1 transmembrane domain triggers enzyme dimerisation and localisation to the Golgi compartment.
16859706	7	39	theme	pronounced	1081:1090	arg1	structure					1102:1110	a pronounced secondary structure	1079:1110	a pronounced secondary structure	1079:1110	This domain exhibits a pronounced secondary structure in a lipid environment.
16859706	5	40	theme	TPST1	870:874	arg1	retention					857:865	Golgi retention	851:865	Golgi retention of TPST1	851:874	By alanine mutation of these asparagine residues, we could determine that the N-linked oligosaccharides do not have an influence on Golgi retention of TPST1.
16859706	4	41	theme	mutational	603:612	arg1	studies					614:620	mutational studies	603:620	mutational studies	603:620	PNGase treatment and mutational studies determined that TPST1 bears N-linked glycosyl residues exclusively at position Asn60 and Asn262.
16859706	5	42	theme	residues	759:766	arg1	mutation					730:737	alanine mutation	722:737	alanine mutation of these asparagine residues	722:766	By alanine mutation of these asparagine residues, we could determine that the N-linked oligosaccharides do not have an influence on Golgi retention of TPST1.
16859706	6	43	theme	flanking	910:917	arg1	residues					919:926	C-terminal flanking residues	899:926	C-terminal flanking residues	899:926	In concert with N and C-terminal flanking residues, the transmembrane domain of TPST1 was determined to act in targeting and retention of the enzyme to the trans-Golgi compartment.
16859706	1	44	theme	human	116:120	arg1	sulfotransferase					137:152	a human tyrosylprotein sulfotransferase	114:152	a human tyrosylprotein sulfotransferase that uses 3'phosphoadenosine-5'phosphosulfate (PAPS) to transfer the sulfate moiety to proteins predominantly designated for secretion	114:287	TPST1 is a human tyrosylprotein sulfotransferase that uses 3'phosphoadenosine-5'phosphosulfate (PAPS) to transfer the sulfate moiety to proteins predominantly designated for secretion.
16859706	1	44	theme	human	116:120	arg1	TPST1					105:109	TPST1	105:109	TPST1	105:109	TPST1 is a human tyrosylprotein sulfotransferase that uses 3'phosphoadenosine-5'phosphosulfate (PAPS) to transfer the sulfate moiety to proteins predominantly designated for secretion.
16859706	7	45	theme	secondary	1092:1100	arg1	structure					1102:1110	a pronounced secondary structure	1079:1110	a pronounced secondary structure	1079:1110	This domain exhibits a pronounced secondary structure in a lipid environment.
16859706	6	46	theme	C-terminal	899:908	arg1	residues					919:926	C-terminal flanking residues	899:926	C-terminal flanking residues	899:926	In concert with N and C-terminal flanking residues, the transmembrane domain of TPST1 was determined to act in targeting and retention of the enzyme to the trans-Golgi compartment.
16859706	1	47	theme	tyrosylprotein	122:135	arg1	sulfotransferase					137:152	a human tyrosylprotein sulfotransferase	114:152	a human tyrosylprotein sulfotransferase that uses 3'phosphoadenosine-5'phosphosulfate (PAPS) to transfer the sulfate moiety to proteins predominantly designated for secretion	114:287	TPST1 is a human tyrosylprotein sulfotransferase that uses 3'phosphoadenosine-5'phosphosulfate (PAPS) to transfer the sulfate moiety to proteins predominantly designated for secretion.
16859706	1	47	theme	tyrosylprotein	122:135	arg1	TPST1					105:109	TPST1	105:109	TPST1	105:109	TPST1 is a human tyrosylprotein sulfotransferase that uses 3'phosphoadenosine-5'phosphosulfate (PAPS) to transfer the sulfate moiety to proteins predominantly designated for secretion.
16859706	8	48	theme	transmembrane	1175:1187	arg1	domain					1189:1194	the transmembrane domain	1171:1194	the transmembrane domain	1171:1194	Further in vivo FRET studies using the transmembrane domain suggest that the human tyrosylprotein sulfotransferase may be functional as homodimer/oligomer in the trans-Golgi compartment.
16859706	4	49	link	N-linked	650:657	arg1	residues					668:675	N-linked glycosyl residues	650:675	N-linked glycosyl residues	650:675	PNGase treatment and mutational studies determined that TPST1 bears N-linked glycosyl residues exclusively at position Asn60 and Asn262.
16859706	3	50	from	localisation	480:491	arg1	COS-7					510:514	COS-7	510:514	COS-7	510:514	Golgi localisation of the enzyme in COS-7 and HeLa cells was visualised by fluorescence imaging techniques.
16859706	3	50	from	localisation	480:491	arg1	cells					525:529	HeLa cells	520:529	HeLa cells	520:529	Golgi localisation of the enzyme in COS-7 and HeLa cells was visualised by fluorescence imaging techniques.
16859706	2	51	theme	human	349:353	arg1	sulfotransferases					373:389	human tyrosine-directed sulfotransferases	349:389	human tyrosine-directed sulfotransferases	349:389	To achieve a general understanding of the cellular role of human tyrosine-directed sulfotransferases, we investigated targeting, structure and posttranslational modification of TPST1.
16859706	2	52	theme	tyrosine-directed	355:371	arg1	sulfotransferases					373:389	human tyrosine-directed sulfotransferases	349:389	human tyrosine-directed sulfotransferases	349:389	To achieve a general understanding of the cellular role of human tyrosine-directed sulfotransferases, we investigated targeting, structure and posttranslational modification of TPST1.
16859706	3	53	theme	enzyme	500:505	arg1	localisation					480:491	Golgi localisation	474:491	Golgi localisation of the enzyme in COS-7 and HeLa cells	474:529	Golgi localisation of the enzyme in COS-7 and HeLa cells was visualised by fluorescence imaging techniques.
16859706	6	54	with	concert	880:886	arg1	N					893:893	N	893:893	N	893:893	In concert with N and C-terminal flanking residues, the transmembrane domain of TPST1 was determined to act in targeting and retention of the enzyme to the trans-Golgi compartment.
16859706	6	54	with	concert	880:886	arg1	residues					919:926	C-terminal flanking residues	899:926	C-terminal flanking residues	899:926	In concert with N and C-terminal flanking residues, the transmembrane domain of TPST1 was determined to act in targeting and retention of the enzyme to the trans-Golgi compartment.
12154198	1	0	theme	entire	138:143	arg1	region					159:164	the entire extracellular region	134:164	the entire extracellular region of human HER3 (ErbB3), a member of the epidermal growth factor receptor (EGFR) family	134:250	We have determined the 2.6 angstrom crystal structure of the entire extracellular region of human HER3 (ErbB3), a member of the epidermal growth factor receptor (EGFR) family.
12154198	1	1	theme	epidermal	205:213	arg1	EGFR					239:242	EGFR	239:242	EGFR	239:242	We have determined the 2.6 angstrom crystal structure of the entire extracellular region of human HER3 (ErbB3), a member of the epidermal growth factor receptor (EGFR) family.
12154198	1	1	theme	epidermal	205:213	arg1	receptor					229:236	epidermal growth factor receptor	205:236	the epidermal growth factor receptor (EGFR) family	201:250	We have determined the 2.6 angstrom crystal structure of the entire extracellular region of human HER3 (ErbB3), a member of the epidermal growth factor receptor (EGFR) family.
12154198	2	2	theme	type	341:344	arg1	receptor					375:382	the type I insulin-like growth factor receptor	337:382	the type I insulin-like growth factor receptor	337:382	The structure consists of four domains with structural homology to domains found in the type I insulin-like growth factor receptor.
12154198	1	3	theme	extracellular	145:157	arg1	region					159:164	the entire extracellular region	134:164	the entire extracellular region of human HER3 (ErbB3), a member of the epidermal growth factor receptor (EGFR) family	134:250	We have determined the 2.6 angstrom crystal structure of the entire extracellular region of human HER3 (ErbB3), a member of the epidermal growth factor receptor (EGFR) family.
12154198	1	4	theme	growth	215:220	arg1	EGFR					239:242	EGFR	239:242	EGFR	239:242	We have determined the 2.6 angstrom crystal structure of the entire extracellular region of human HER3 (ErbB3), a member of the epidermal growth factor receptor (EGFR) family.
12154198	1	4	theme	growth	215:220	arg1	receptor					229:236	epidermal growth factor receptor	205:236	the epidermal growth factor receptor (EGFR) family	201:250	We have determined the 2.6 angstrom crystal structure of the entire extracellular region of human HER3 (ErbB3), a member of the epidermal growth factor receptor (EGFR) family.
12154198	3	5	theme	ligand	658:663	arg1	binding					665:671	ligand binding	658:671	ligand binding during signaling	658:688	The HER3 structure reveals a contact between domains II and IV that constrains the relative orientations of ligand-binding domains and provides a structural basis for understanding both multiple-affinity forms of EGFRs and conformational changes induced in the receptor by ligand binding during signaling.
12154198	4	6	theme	new	718:720	arg1	approaches					734:743	new therapeutic approaches	718:743	new therapeutic approaches to modulating the behavior of members of the EGFR family	718:800	These results also suggest new therapeutic approaches to modulating the behavior of members of the EGFR family.
12154198	1	7	theme	factor	222:227	arg1	EGFR					239:242	EGFR	239:242	EGFR	239:242	We have determined the 2.6 angstrom crystal structure of the entire extracellular region of human HER3 (ErbB3), a member of the epidermal growth factor receptor (EGFR) family.
12154198	1	7	theme	factor	222:227	arg1	receptor					229:236	epidermal growth factor receptor	205:236	the epidermal growth factor receptor (EGFR) family	201:250	We have determined the 2.6 angstrom crystal structure of the entire extracellular region of human HER3 (ErbB3), a member of the epidermal growth factor receptor (EGFR) family.
12154198	3	8	theme	ligand-binding	493:506	arg1	domains					508:514	ligand-binding domains	493:514	ligand-binding domains	493:514	The HER3 structure reveals a contact between domains II and IV that constrains the relative orientations of ligand-binding domains and provides a structural basis for understanding both multiple-affinity forms of EGFRs and conformational changes induced in the receptor by ligand binding during signaling.
12154198	1	9	theme	receptor	229:236	arg1	family					245:250	the epidermal growth factor receptor (EGFR) family	201:250	the epidermal growth factor receptor (EGFR) family	201:250	We have determined the 2.6 angstrom crystal structure of the entire extracellular region of human HER3 (ErbB3), a member of the epidermal growth factor receptor (EGFR) family.
12154198	3	10	theme	relative	468:475	arg1	orientations					477:488	the relative orientations	464:488	the relative orientations of ligand-binding domains	464:514	The HER3 structure reveals a contact between domains II and IV that constrains the relative orientations of ligand-binding domains and provides a structural basis for understanding both multiple-affinity forms of EGFRs and conformational changes induced in the receptor by ligand binding during signaling.
12154198	1	11	theme	region	159:164	arg1	structure					121:129	the 2.6 angstrom crystal structure	96:129	the 2.6 angstrom crystal structure of the entire extracellular region of human HER3 (ErbB3), a member of the epidermal growth factor receptor (EGFR) family	96:250	We have determined the 2.6 angstrom crystal structure of the entire extracellular region of human HER3 (ErbB3), a member of the epidermal growth factor receptor (EGFR) family.
12154198	3	12	theme	HER3	389:392	arg1	structure					394:402	The HER3 structure	385:402	The HER3 structure	385:402	The HER3 structure reveals a contact between domains II and IV that constrains the relative orientations of ligand-binding domains and provides a structural basis for understanding both multiple-affinity forms of EGFRs and conformational changes induced in the receptor by ligand binding during signaling.
12154198	1	13	theme	human	169:173	arg1	ErbB3					181:185	ErbB3	181:185	ErbB3	181:185	We have determined the 2.6 angstrom crystal structure of the entire extracellular region of human HER3 (ErbB3), a member of the epidermal growth factor receptor (EGFR) family.
12154198	1	13	theme	human	169:173	arg1	HER3					175:178	human HER3	169:178	human HER3 (ErbB3)	169:186	We have determined the 2.6 angstrom crystal structure of the entire extracellular region of human HER3 (ErbB3), a member of the epidermal growth factor receptor (EGFR) family.
12154198	1	13	theme	human	169:173	arg1	member					191:196	a member	189:196	a member of the epidermal growth factor receptor (EGFR) family	189:250	We have determined the 2.6 angstrom crystal structure of the entire extracellular region of human HER3 (ErbB3), a member of the epidermal growth factor receptor (EGFR) family.
12154198	1	14	theme	HER3	175:178	arg1	region					159:164	the entire extracellular region	134:164	the entire extracellular region of human HER3 (ErbB3), a member of the epidermal growth factor receptor (EGFR) family	134:250	We have determined the 2.6 angstrom crystal structure of the entire extracellular region of human HER3 (ErbB3), a member of the epidermal growth factor receptor (EGFR) family.
12154198	0	15	theme	extracellular	17:29	arg1	region					31:36	the extracellular region	13:36	the extracellular region of HER3	13:44	Structure of the extracellular region of HER3 reveals an interdomain tether.
12154198	0	16	dep	interdomain	57:67	arg1	tether					69:74	tether	69:74	tether	69:74	Structure of the extracellular region of HER3 reveals an interdomain tether.
12154198	2	17	theme	factor	368:373	arg1	receptor					375:382	the type I insulin-like growth factor receptor	337:382	the type I insulin-like growth factor receptor	337:382	The structure consists of four domains with structural homology to domains found in the type I insulin-like growth factor receptor.
12154198	3	18	theme	conformational	608:621	arg1	changes					623:629	conformational changes	608:629	conformational changes induced in the receptor by ligand binding during signaling	608:688	The HER3 structure reveals a contact between domains II and IV that constrains the relative orientations of ligand-binding domains and provides a structural basis for understanding both multiple-affinity forms of EGFRs and conformational changes induced in the receptor by ligand binding during signaling.
12154198	2	19	theme	structural	297:306	arg1	homology					308:315	structural homology	297:315	structural homology to domains found in the type I insulin-like growth factor receptor	297:382	The structure consists of four domains with structural homology to domains found in the type I insulin-like growth factor receptor.
12154198	2	20	theme	growth	361:366	arg1	receptor					375:382	the type I insulin-like growth factor receptor	337:382	the type I insulin-like growth factor receptor	337:382	The structure consists of four domains with structural homology to domains found in the type I insulin-like growth factor receptor.
12154198	1	21	theme	family	245:250	arg1	HER3					175:178	human HER3	169:178	human HER3 (ErbB3)	169:186	We have determined the 2.6 angstrom crystal structure of the entire extracellular region of human HER3 (ErbB3), a member of the epidermal growth factor receptor (EGFR) family.
12154198	1	21	theme	family	245:250	arg1	member					191:196	a member	189:196	a member of the epidermal growth factor receptor (EGFR) family	189:250	We have determined the 2.6 angstrom crystal structure of the entire extracellular region of human HER3 (ErbB3), a member of the epidermal growth factor receptor (EGFR) family.
12154198	3	22	theme	changes	623:629	arg1	forms					589:593	both multiple-affinity forms	566:593	both multiple-affinity forms of EGFRs and conformational changes induced in the receptor by ligand binding during signaling	566:688	The HER3 structure reveals a contact between domains II and IV that constrains the relative orientations of ligand-binding domains and provides a structural basis for understanding both multiple-affinity forms of EGFRs and conformational changes induced in the receptor by ligand binding during signaling.
12154198	4	23	theme	EGFR	790:793	arg1	family					795:800	the EGFR family	786:800	the EGFR family	786:800	These results also suggest new therapeutic approaches to modulating the behavior of members of the EGFR family.
12154198	2	24	theme	insulin-like	348:359	arg1	receptor					375:382	the type I insulin-like growth factor receptor	337:382	the type I insulin-like growth factor receptor	337:382	The structure consists of four domains with structural homology to domains found in the type I insulin-like growth factor receptor.
12154198	0	25	theme	region	31:36	arg1	Structure					0:8	Structure	0:8	Structure of the extracellular region of HER3	0:44	Structure of the extracellular region of HER3 reveals an interdomain tether.
12154198	3	26	theme	EGFRs	598:602	arg1	forms					589:593	both multiple-affinity forms	566:593	both multiple-affinity forms of EGFRs and conformational changes induced in the receptor by ligand binding during signaling	566:688	The HER3 structure reveals a contact between domains II and IV that constrains the relative orientations of ligand-binding domains and provides a structural basis for understanding both multiple-affinity forms of EGFRs and conformational changes induced in the receptor by ligand binding during signaling.
12154198	4	27	theme	therapeutic	722:732	arg1	approaches					734:743	new therapeutic approaches	718:743	new therapeutic approaches to modulating the behavior of members of the EGFR family	718:800	These results also suggest new therapeutic approaches to modulating the behavior of members of the EGFR family.
12154198	2	28	with	domains	284:290	arg1	homology					308:315	structural homology	297:315	structural homology to domains found in the type I insulin-like growth factor receptor	297:382	The structure consists of four domains with structural homology to domains found in the type I insulin-like growth factor receptor.
12154198	3	29	theme	structural	531:540	arg1	basis					542:546	a structural basis	529:546	a structural basis for understanding both multiple-affinity forms of EGFRs and conformational changes induced in the receptor by ligand binding during signaling	529:688	The HER3 structure reveals a contact between domains II and IV that constrains the relative orientations of ligand-binding domains and provides a structural basis for understanding both multiple-affinity forms of EGFRs and conformational changes induced in the receptor by ligand binding during signaling.
12154198	1	30	theme	2.6	100:102	arg1	angstrom					104:111	angstrom	104:111	angstrom	104:111	We have determined the 2.6 angstrom crystal structure of the entire extracellular region of human HER3 (ErbB3), a member of the epidermal growth factor receptor (EGFR) family.
12154198	0	31	theme	HER3	41:44	arg1	region					31:36	the extracellular region	13:36	the extracellular region of HER3	13:44	Structure of the extracellular region of HER3 reveals an interdomain tether.
12154198	4	32	theme	family	795:800	arg1	members					775:781	members	775:781	members of the EGFR family	775:800	These results also suggest new therapeutic approaches to modulating the behavior of members of the EGFR family.
12154198	1	33	theme	angstrom	104:111	arg1	structure					121:129	the 2.6 angstrom crystal structure	96:129	the 2.6 angstrom crystal structure of the entire extracellular region of human HER3 (ErbB3), a member of the epidermal growth factor receptor (EGFR) family	96:250	We have determined the 2.6 angstrom crystal structure of the entire extracellular region of human HER3 (ErbB3), a member of the epidermal growth factor receptor (EGFR) family.
12154198	4	34	theme	members	775:781	arg1	behavior					763:770	the behavior	759:770	the behavior of members of the EGFR family	759:800	These results also suggest new therapeutic approaches to modulating the behavior of members of the EGFR family.
12154198	1	35	theme	crystal	113:119	arg1	structure					121:129	the 2.6 angstrom crystal structure	96:129	the 2.6 angstrom crystal structure of the entire extracellular region of human HER3 (ErbB3), a member of the epidermal growth factor receptor (EGFR) family	96:250	We have determined the 2.6 angstrom crystal structure of the entire extracellular region of human HER3 (ErbB3), a member of the epidermal growth factor receptor (EGFR) family.
12154198	3	36	theme	domains	508:514	arg1	orientations					477:488	the relative orientations	464:488	the relative orientations of ligand-binding domains	464:514	The HER3 structure reveals a contact between domains II and IV that constrains the relative orientations of ligand-binding domains and provides a structural basis for understanding both multiple-affinity forms of EGFRs and conformational changes induced in the receptor by ligand binding during signaling.
12154198	2	37	located	found	328:332	arg2	domains					320:326	domains	320:326	domains found in the type I insulin-like growth factor receptor	320:382	The structure consists of four domains with structural homology to domains found in the type I insulin-like growth factor receptor.
12154198	2	37	located	found	328:332	arg1	receptor					375:382	the type I insulin-like growth factor receptor	337:382	the type I insulin-like growth factor receptor	337:382	The structure consists of four domains with structural homology to domains found in the type I insulin-like growth factor receptor.
12154198	3	38	theme	multiple-affinity	571:587	arg1	forms					589:593	both multiple-affinity forms	566:593	both multiple-affinity forms of EGFRs and conformational changes induced in the receptor by ligand binding during signaling	566:688	The HER3 structure reveals a contact between domains II and IV that constrains the relative orientations of ligand-binding domains and provides a structural basis for understanding both multiple-affinity forms of EGFRs and conformational changes induced in the receptor by ligand binding during signaling.
7524900	0	0	theme	basic	69:73	arg1	protein					75:81	human major basic protein	57:81	human major basic protein	57:81	Location and nature of carbohydrate groups in proform of human major basic protein isolated from pregnancy serum.
7524900	0	1	from	nature	13:18	arg1	proform					46:52	proform	46:52	proform of human major basic protein	46:81	Location and nature of carbohydrate groups in proform of human major basic protein isolated from pregnancy serum.
7524900	4	2	theme	peptides	620:627	arg1	profile					584:590	RP-HPLC elution profile	568:590	RP-HPLC elution profile	568:590	From the RP-HPLC elution profile and mass spectra of tryptic peptides it is found that proMBP is extremely heterogeneous with respect to glycosylation.
7524900	4	2	theme	peptides	620:627	arg1	spectra					601:607	mass spectra	596:607	mass spectra	596:607	From the RP-HPLC elution profile and mass spectra of tryptic peptides it is found that proMBP is extremely heterogeneous with respect to glycosylation.
7524900	0	3	theme	major	63:67	arg1	protein					75:81	human major basic protein	57:81	human major basic protein	57:81	Location and nature of carbohydrate groups in proform of human major basic protein isolated from pregnancy serum.
7524900	4	4	theme	tryptic	612:618	arg1	peptides					620:627	tryptic peptides	612:627	tryptic peptides	612:627	From the RP-HPLC elution profile and mass spectra of tryptic peptides it is found that proMBP is extremely heterogeneous with respect to glycosylation.
7524900	0	5	from	Location	0:7	arg1	proform					46:52	proform	46:52	proform of human major basic protein	46:81	Location and nature of carbohydrate groups in proform of human major basic protein isolated from pregnancy serum.
7524900	3	6	theme	N-linked	448:455	arg1	glycan					457:462	N-linked glycan	448:462	N-linked glycan	448:462	N-linked glycan is bound to Asn-86 and O-linked glycosaminoglycan is bound to Ser-62 (both fully substituted).
7524900	0	7	theme	protein	75:81	arg1	proform					46:52	proform	46:52	proform of human major basic protein	46:81	Location and nature of carbohydrate groups in proform of human major basic protein isolated from pregnancy serum.
7524900	0	8	from	proform	46:52	arg1	nature					13:18	nature	13:18	nature	13:18	Location and nature of carbohydrate groups in proform of human major basic protein isolated from pregnancy serum.
7524900	0	8	from	proform	46:52	arg1	Location					0:7	Location	0:7	Location	0:7	Location and nature of carbohydrate groups in proform of human major basic protein isolated from pregnancy serum.
7524900	0	9	theme	pregnancy	97:105	arg1	serum					107:111	pregnancy serum	97:111	pregnancy serum	97:111	Location and nature of carbohydrate groups in proform of human major basic protein isolated from pregnancy serum.
7524900	2	10	dep	substituted	384:394	arg1	fully					378:382	fully	378:382	fully	378:382	It is shown that proMBP contains O-linked glycan bound to Ser-24, Thr-25 (fully substituted), and to Thr-23 and Thr-34 (partially substituted).
7524900	4	11	theme	mass	596:599	arg1	spectra					601:607	mass spectra	596:607	mass spectra	596:607	From the RP-HPLC elution profile and mass spectra of tryptic peptides it is found that proMBP is extremely heterogeneous with respect to glycosylation.
7524900	3	12	dep	bound	517:521	arg1	substituted					545:555	substituted	545:555	substituted	545:555	N-linked glycan is bound to Asn-86 and O-linked glycosaminoglycan is bound to Ser-62 (both fully substituted).
7524900	0	13	from	groups	36:41	arg1	proform					46:52	proform	46:52	proform of human major basic protein	46:81	Location and nature of carbohydrate groups in proform of human major basic protein isolated from pregnancy serum.
7524900	4	14	theme	elution	576:582	arg1	profile					584:590	RP-HPLC elution profile	568:590	RP-HPLC elution profile	568:590	From the RP-HPLC elution profile and mass spectra of tryptic peptides it is found that proMBP is extremely heterogeneous with respect to glycosylation.
7524900	2	15	contain	contains	328:335	arg1	proMBP					321:326	proMBP	321:326	proMBP	321:326	It is shown that proMBP contains O-linked glycan bound to Ser-24, Thr-25 (fully substituted), and to Thr-23 and Thr-34 (partially substituted).
7524900	2	15	contain	contains	328:335	arg2	glycan					346:351	O-linked glycan	337:351	O-linked glycan bound to Ser-24, Thr-25 (fully substituted), and to Thr-23 and Thr-34 (partially substituted)	337:445	It is shown that proMBP contains O-linked glycan bound to Ser-24, Thr-25 (fully substituted), and to Thr-23 and Thr-34 (partially substituted).
7524900	4	16	theme	RP-HPLC	568:574	arg1	profile					584:590	RP-HPLC elution profile	568:590	RP-HPLC elution profile	568:590	From the RP-HPLC elution profile and mass spectra of tryptic peptides it is found that proMBP is extremely heterogeneous with respect to glycosylation.
7524900	2	17	theme	O-linked	337:344	arg1	glycan					346:351	O-linked glycan	337:351	O-linked glycan bound to Ser-24, Thr-25 (fully substituted), and to Thr-23 and Thr-34 (partially substituted)	337:445	It is shown that proMBP contains O-linked glycan bound to Ser-24, Thr-25 (fully substituted), and to Thr-23 and Thr-34 (partially substituted).
7524900	1	18	theme	pregnancy-associated	241:260	arg1	PAPP-A					280:285	PAPP-A	280:285	PAPP-A	280:285	From human pregnancy serum we have isolated the proform of eosinophil major basic protein (proMBP), which forms a complex with pregnancy-associated plasma protein-A (PAPP-A), PAPP-A/proMBP.
7524900	1	18	theme	pregnancy-associated	241:260	arg1	PAPP-A/proMBP					289:301	PAPP-A/proMBP	289:301	PAPP-A/proMBP	289:301	From human pregnancy serum we have isolated the proform of eosinophil major basic protein (proMBP), which forms a complex with pregnancy-associated plasma protein-A (PAPP-A), PAPP-A/proMBP.
7524900	1	18	theme	pregnancy-associated	241:260	arg1	protein-A					269:277	pregnancy-associated plasma protein-A	241:277	pregnancy-associated plasma protein-A (PAPP-A)	241:286	From human pregnancy serum we have isolated the proform of eosinophil major basic protein (proMBP), which forms a complex with pregnancy-associated plasma protein-A (PAPP-A), PAPP-A/proMBP.
7524900	1	19	theme	eosinophil	173:182	arg1	proMBP					205:210	proMBP	205:210	proMBP	205:210	From human pregnancy serum we have isolated the proform of eosinophil major basic protein (proMBP), which forms a complex with pregnancy-associated plasma protein-A (PAPP-A), PAPP-A/proMBP.
7524900	1	19	theme	eosinophil	173:182	arg1	protein					196:202	eosinophil major basic protein	173:202	eosinophil major basic protein (proMBP)	173:211	From human pregnancy serum we have isolated the proform of eosinophil major basic protein (proMBP), which forms a complex with pregnancy-associated plasma protein-A (PAPP-A), PAPP-A/proMBP.
7524900	1	20	theme	plasma	262:267	arg1	PAPP-A					280:285	PAPP-A	280:285	PAPP-A	280:285	From human pregnancy serum we have isolated the proform of eosinophil major basic protein (proMBP), which forms a complex with pregnancy-associated plasma protein-A (PAPP-A), PAPP-A/proMBP.
7524900	1	20	theme	plasma	262:267	arg1	PAPP-A/proMBP					289:301	PAPP-A/proMBP	289:301	PAPP-A/proMBP	289:301	From human pregnancy serum we have isolated the proform of eosinophil major basic protein (proMBP), which forms a complex with pregnancy-associated plasma protein-A (PAPP-A), PAPP-A/proMBP.
7524900	1	20	theme	plasma	262:267	arg1	protein-A					269:277	pregnancy-associated plasma protein-A	241:277	pregnancy-associated plasma protein-A (PAPP-A)	241:286	From human pregnancy serum we have isolated the proform of eosinophil major basic protein (proMBP), which forms a complex with pregnancy-associated plasma protein-A (PAPP-A), PAPP-A/proMBP.
7524900	3	21	theme	O-linked	487:494	arg1	glycosaminoglycan					496:512	O-linked glycosaminoglycan	487:512	O-linked glycosaminoglycan	487:512	N-linked glycan is bound to Asn-86 and O-linked glycosaminoglycan is bound to Ser-62 (both fully substituted).
7524900	1	22	theme	major	184:188	arg1	proMBP					205:210	proMBP	205:210	proMBP	205:210	From human pregnancy serum we have isolated the proform of eosinophil major basic protein (proMBP), which forms a complex with pregnancy-associated plasma protein-A (PAPP-A), PAPP-A/proMBP.
7524900	1	22	theme	major	184:188	arg1	protein					196:202	eosinophil major basic protein	173:202	eosinophil major basic protein (proMBP)	173:211	From human pregnancy serum we have isolated the proform of eosinophil major basic protein (proMBP), which forms a complex with pregnancy-associated plasma protein-A (PAPP-A), PAPP-A/proMBP.
7524900	0	23	theme	groups	36:41	arg1	nature					13:18	nature	13:18	nature	13:18	Location and nature of carbohydrate groups in proform of human major basic protein isolated from pregnancy serum.
7524900	0	23	theme	groups	36:41	arg1	Location					0:7	Location	0:7	Location	0:7	Location and nature of carbohydrate groups in proform of human major basic protein isolated from pregnancy serum.
7524900	3	24	link	N-linked	448:455	arg1	glycan					457:462	N-linked glycan	448:462	N-linked glycan	448:462	N-linked glycan is bound to Asn-86 and O-linked glycosaminoglycan is bound to Ser-62 (both fully substituted).
7524900	2	25	link	O-linked	337:344	arg1	glycan					346:351	O-linked glycan	337:351	O-linked glycan bound to Ser-24, Thr-25 (fully substituted), and to Thr-23 and Thr-34 (partially substituted)	337:445	It is shown that proMBP contains O-linked glycan bound to Ser-24, Thr-25 (fully substituted), and to Thr-23 and Thr-34 (partially substituted).
7524900	1	26	theme	basic	190:194	arg1	proMBP					205:210	proMBP	205:210	proMBP	205:210	From human pregnancy serum we have isolated the proform of eosinophil major basic protein (proMBP), which forms a complex with pregnancy-associated plasma protein-A (PAPP-A), PAPP-A/proMBP.
7524900	1	26	theme	basic	190:194	arg1	protein					196:202	eosinophil major basic protein	173:202	eosinophil major basic protein (proMBP)	173:211	From human pregnancy serum we have isolated the proform of eosinophil major basic protein (proMBP), which forms a complex with pregnancy-associated plasma protein-A (PAPP-A), PAPP-A/proMBP.
7524900	0	27	theme	carbohydrate	23:34	arg1	groups					36:41	carbohydrate groups	23:41	carbohydrate groups in proform of human major basic protein	23:81	Location and nature of carbohydrate groups in proform of human major basic protein isolated from pregnancy serum.
7524900	1	28	theme	protein	196:202	arg1	proform					162:168	the proform	158:168	the proform of eosinophil major basic protein (proMBP), which forms a complex with pregnancy-associated plasma protein-A (PAPP-A), PAPP-A/proMBP	158:301	From human pregnancy serum we have isolated the proform of eosinophil major basic protein (proMBP), which forms a complex with pregnancy-associated plasma protein-A (PAPP-A), PAPP-A/proMBP.
7524900	3	29	dep	substituted	545:555	arg1	fully					539:543	fully	539:543	fully	539:543	N-linked glycan is bound to Asn-86 and O-linked glycosaminoglycan is bound to Ser-62 (both fully substituted).
7524900	3	29	dep	substituted	545:555	arg1	both					534:537	both	534:537	both	534:537	N-linked glycan is bound to Asn-86 and O-linked glycosaminoglycan is bound to Ser-62 (both fully substituted).
7524900	1	30	with	complex	228:234	arg1	PAPP-A					280:285	PAPP-A	280:285	PAPP-A	280:285	From human pregnancy serum we have isolated the proform of eosinophil major basic protein (proMBP), which forms a complex with pregnancy-associated plasma protein-A (PAPP-A), PAPP-A/proMBP.
7524900	1	30	with	complex	228:234	arg1	PAPP-A/proMBP					289:301	PAPP-A/proMBP	289:301	PAPP-A/proMBP	289:301	From human pregnancy serum we have isolated the proform of eosinophil major basic protein (proMBP), which forms a complex with pregnancy-associated plasma protein-A (PAPP-A), PAPP-A/proMBP.
7524900	1	30	with	complex	228:234	arg1	protein-A					269:277	pregnancy-associated plasma protein-A	241:277	pregnancy-associated plasma protein-A (PAPP-A)	241:286	From human pregnancy serum we have isolated the proform of eosinophil major basic protein (proMBP), which forms a complex with pregnancy-associated plasma protein-A (PAPP-A), PAPP-A/proMBP.
7524900	2	31	dep	Thr-25	370:375	arg1	substituted					384:394	substituted	384:394	substituted	384:394	It is shown that proMBP contains O-linked glycan bound to Ser-24, Thr-25 (fully substituted), and to Thr-23 and Thr-34 (partially substituted).
7524900	1	32	theme	human	119:123	arg1	serum					135:139	human pregnancy serum	119:139	human pregnancy serum	119:139	From human pregnancy serum we have isolated the proform of eosinophil major basic protein (proMBP), which forms a complex with pregnancy-associated plasma protein-A (PAPP-A), PAPP-A/proMBP.
7524900	0	33	theme	human	57:61	arg1	protein					75:81	human major basic protein	57:81	human major basic protein	57:81	Location and nature of carbohydrate groups in proform of human major basic protein isolated from pregnancy serum.
7524900	4	34	dep	profile	584:590	arg1	the					564:566	the	564:566	the	564:566	From the RP-HPLC elution profile and mass spectra of tryptic peptides it is found that proMBP is extremely heterogeneous with respect to glycosylation.
7524900	1	35	theme	pregnancy	125:133	arg1	serum					135:139	human pregnancy serum	119:139	human pregnancy serum	119:139	From human pregnancy serum we have isolated the proform of eosinophil major basic protein (proMBP), which forms a complex with pregnancy-associated plasma protein-A (PAPP-A), PAPP-A/proMBP.
7524900	3	36	link	O-linked	487:494	arg1	glycosaminoglycan					496:512	O-linked glycosaminoglycan	487:512	O-linked glycosaminoglycan	487:512	N-linked glycan is bound to Asn-86 and O-linked glycosaminoglycan is bound to Ser-62 (both fully substituted).
8507662	1	0	theme	Chinese	153:159	arg1	cells					176:180	Chinese hamster kidney cells	153:180	Chinese hamster kidney cells	153:180	The amino-acid sequence of purified recombinant pro-major basic protein from Chinese hamster kidney cells was determined to verify the primary structure and glycosylation sites.
8507662	4	1	theme	Sequence	541:548	arg1	analysis					550:557	Sequence analysis	541:557	Sequence analysis	541:557	Sequence analysis and deglycosylation study revealed that Ser-8, Thr-9, Ser-46 and Asn-70 were glycosylated.
8507662	4	2	gly	glycosylated	636:647	arg1	Ser-8					599:603	Ser-8	599:603	Ser-8	599:603	Sequence analysis and deglycosylation study revealed that Ser-8, Thr-9, Ser-46 and Asn-70 were glycosylated.
8507662	4	2	gly	glycosylated	636:647	arg1	Asn-70					624:629	Asn-70	624:629	Asn-70	624:629	Sequence analysis and deglycosylation study revealed that Ser-8, Thr-9, Ser-46 and Asn-70 were glycosylated.
8507662	4	2	gly	glycosylated	636:647	arg1	Ser-46					613:618	Ser-46	613:618	Ser-46	613:618	Sequence analysis and deglycosylation study revealed that Ser-8, Thr-9, Ser-46 and Asn-70 were glycosylated.
8507662	4	2	gly	glycosylated	636:647	arg1	Thr-9					606:610	Thr-9	606:610	Thr-9	606:610	Sequence analysis and deglycosylation study revealed that Ser-8, Thr-9, Ser-46 and Asn-70 were glycosylated.
8507662	1	3	gly	glycosylation	233:245	arg2	sites					247:251	glycosylation sites	233:251	glycosylation sites	233:251	The amino-acid sequence of purified recombinant pro-major basic protein from Chinese hamster kidney cells was determined to verify the primary structure and glycosylation sites.
8507662	3	4	theme	basic	512:516	arg1	sequence					531:538	the pro-major basic protein cDNA sequence	498:538	the pro-major basic protein cDNA sequence	498:538	We could identify all the peptides which were expected from the pro-major basic protein cDNA sequence.
8507662	1	5	theme	hamster	161:167	arg1	cells					176:180	Chinese hamster kidney cells	153:180	Chinese hamster kidney cells	153:180	The amino-acid sequence of purified recombinant pro-major basic protein from Chinese hamster kidney cells was determined to verify the primary structure and glycosylation sites.
8507662	2	6	theme	S-carboxamidemethylated	266:288	arg1	protein					290:296	Reduced and S-carboxamidemethylated protein	254:296	Reduced and S-carboxamidemethylated protein	254:296	Reduced and S-carboxamidemethylated protein was first digested with Achromobacter proteinase I. Each peptide was characterized by amino-acid analysis and amino-acid sequence analysis.
8507662	2	7	theme	sequence	419:426	arg1	analysis					428:435	amino-acid sequence analysis	408:435	amino-acid sequence analysis	408:435	Reduced and S-carboxamidemethylated protein was first digested with Achromobacter proteinase I. Each peptide was characterized by amino-acid analysis and amino-acid sequence analysis.
8507662	0	8	theme	basic	10:14	arg1	protein					16:22	Pro-major basic protein	0:22	Pro-major basic protein	0:22	Pro-major basic protein has three types of sugar chains at the pro-portion.
8507662	0	9	contain	has	24:26	arg1	protein					16:22	Pro-major basic protein	0:22	Pro-major basic protein	0:22	Pro-major basic protein has three types of sugar chains at the pro-portion.
8507662	0	9	contain	has	24:26	arg2	types					34:38	three types	28:38	three types of sugar chains	28:54	Pro-major basic protein has three types of sugar chains at the pro-portion.
8507662	2	10	theme	proteinase	336:345	arg1	I.					347:348	Achromobacter proteinase I.	322:348	Achromobacter proteinase I.	322:348	Reduced and S-carboxamidemethylated protein was first digested with Achromobacter proteinase I. Each peptide was characterized by amino-acid analysis and amino-acid sequence analysis.
8507662	2	11	theme	amino-acid	408:417	arg1	analysis					428:435	amino-acid sequence analysis	408:435	amino-acid sequence analysis	408:435	Reduced and S-carboxamidemethylated protein was first digested with Achromobacter proteinase I. Each peptide was characterized by amino-acid analysis and amino-acid sequence analysis.
8507662	0	12	theme	Pro-major	0:8	arg1	protein					16:22	Pro-major basic protein	0:22	Pro-major basic protein	0:22	Pro-major basic protein has three types of sugar chains at the pro-portion.
8507662	2	13	theme	Achromobacter	322:334	arg1	I.					347:348	Achromobacter proteinase I.	322:348	Achromobacter proteinase I.	322:348	Reduced and S-carboxamidemethylated protein was first digested with Achromobacter proteinase I. Each peptide was characterized by amino-acid analysis and amino-acid sequence analysis.
8507662	1	14	theme	amino-acid	80:89	arg1	sequence					91:98	The amino-acid sequence	76:98	The amino-acid sequence of purified recombinant pro-major basic protein from Chinese hamster kidney cells	76:180	The amino-acid sequence of purified recombinant pro-major basic protein from Chinese hamster kidney cells was determined to verify the primary structure and glycosylation sites.
8507662	3	15	theme	cDNA	526:529	arg1	sequence					531:538	the pro-major basic protein cDNA sequence	498:538	the pro-major basic protein cDNA sequence	498:538	We could identify all the peptides which were expected from the pro-major basic protein cDNA sequence.
8507662	4	16	theme	deglycosylation	563:577	arg1	study					579:583	deglycosylation study	563:583	deglycosylation study	563:583	Sequence analysis and deglycosylation study revealed that Ser-8, Thr-9, Ser-46 and Asn-70 were glycosylated.
8507662	0	17	theme	sugar	43:47	arg1	chains					49:54	sugar chains	43:54	sugar chains	43:54	Pro-major basic protein has three types of sugar chains at the pro-portion.
8507662	5	18	theme	sugar	703:707	arg1	chains					709:714	sugar chains	703:714	sugar chains	703:714	The results indicated that proMBP has three types of sugar chains, O-glycoside, N-glycoside and glycosaminoglycan, in the pro-portion.
8507662	3	19	theme	protein	518:524	arg1	sequence					531:538	the pro-major basic protein cDNA sequence	498:538	the pro-major basic protein cDNA sequence	498:538	We could identify all the peptides which were expected from the pro-major basic protein cDNA sequence.
8507662	2	20	theme	amino-acid	384:393	arg1	analysis					395:402	amino-acid analysis	384:402	amino-acid analysis	384:402	Reduced and S-carboxamidemethylated protein was first digested with Achromobacter proteinase I. Each peptide was characterized by amino-acid analysis and amino-acid sequence analysis.
8507662	5	21	theme	chains	709:714	arg1	N-glycoside					730:740	N-glycoside	730:740	N-glycoside	730:740	The results indicated that proMBP has three types of sugar chains, O-glycoside, N-glycoside and glycosaminoglycan, in the pro-portion.
8507662	5	21	theme	chains	709:714	arg1	O-glycoside					717:727	O-glycoside	717:727	O-glycoside	717:727	The results indicated that proMBP has three types of sugar chains, O-glycoside, N-glycoside and glycosaminoglycan, in the pro-portion.
8507662	5	21	theme	chains	709:714	arg1	types					694:698	three types	688:698	three types of sugar chains	688:714	The results indicated that proMBP has three types of sugar chains, O-glycoside, N-glycoside and glycosaminoglycan, in the pro-portion.
8507662	5	21	theme	chains	709:714	arg1	glycosaminoglycan					746:762	glycosaminoglycan	746:762	glycosaminoglycan	746:762	The results indicated that proMBP has three types of sugar chains, O-glycoside, N-glycoside and glycosaminoglycan, in the pro-portion.
8507662	1	22	theme	purified	103:110	arg1	protein					140:146	purified recombinant pro-major basic protein	103:146	purified recombinant pro-major basic protein from Chinese hamster kidney cells	103:180	The amino-acid sequence of purified recombinant pro-major basic protein from Chinese hamster kidney cells was determined to verify the primary structure and glycosylation sites.
8507662	1	23	theme	recombinant	112:122	arg1	protein					140:146	purified recombinant pro-major basic protein	103:146	purified recombinant pro-major basic protein from Chinese hamster kidney cells	103:180	The amino-acid sequence of purified recombinant pro-major basic protein from Chinese hamster kidney cells was determined to verify the primary structure and glycosylation sites.
8507662	1	24	from	sequence	91:98	arg1	cells					176:180	Chinese hamster kidney cells	153:180	Chinese hamster kidney cells	153:180	The amino-acid sequence of purified recombinant pro-major basic protein from Chinese hamster kidney cells was determined to verify the primary structure and glycosylation sites.
8507662	1	25	theme	primary	211:217	arg1	structure					219:227	the primary structure	207:227	the primary structure	207:227	The amino-acid sequence of purified recombinant pro-major basic protein from Chinese hamster kidney cells was determined to verify the primary structure and glycosylation sites.
8507662	2	26	theme	Reduced	254:260	arg1	protein					290:296	Reduced and S-carboxamidemethylated protein	254:296	Reduced and S-carboxamidemethylated protein	254:296	Reduced and S-carboxamidemethylated protein was first digested with Achromobacter proteinase I. Each peptide was characterized by amino-acid analysis and amino-acid sequence analysis.
8507662	1	27	from	cells	176:180	arg1	protein					140:146	purified recombinant pro-major basic protein	103:146	purified recombinant pro-major basic protein from Chinese hamster kidney cells	103:180	The amino-acid sequence of purified recombinant pro-major basic protein from Chinese hamster kidney cells was determined to verify the primary structure and glycosylation sites.
8507662	1	27	from	cells	176:180	arg1	sequence					91:98	The amino-acid sequence	76:98	The amino-acid sequence of purified recombinant pro-major basic protein from Chinese hamster kidney cells	76:180	The amino-acid sequence of purified recombinant pro-major basic protein from Chinese hamster kidney cells was determined to verify the primary structure and glycosylation sites.
8507662	1	28	theme	pro-major	124:132	arg1	protein					140:146	purified recombinant pro-major basic protein	103:146	purified recombinant pro-major basic protein from Chinese hamster kidney cells	103:180	The amino-acid sequence of purified recombinant pro-major basic protein from Chinese hamster kidney cells was determined to verify the primary structure and glycosylation sites.
8507662	3	29	theme	pro-major	502:510	arg1	sequence					531:538	the pro-major basic protein cDNA sequence	498:538	the pro-major basic protein cDNA sequence	498:538	We could identify all the peptides which were expected from the pro-major basic protein cDNA sequence.
8507662	1	30	theme	basic	134:138	arg1	protein					140:146	purified recombinant pro-major basic protein	103:146	purified recombinant pro-major basic protein from Chinese hamster kidney cells	103:180	The amino-acid sequence of purified recombinant pro-major basic protein from Chinese hamster kidney cells was determined to verify the primary structure and glycosylation sites.
8507662	1	31	theme	kidney	169:174	arg1	cells					176:180	Chinese hamster kidney cells	153:180	Chinese hamster kidney cells	153:180	The amino-acid sequence of purified recombinant pro-major basic protein from Chinese hamster kidney cells was determined to verify the primary structure and glycosylation sites.
8507662	0	32	theme	chains	49:54	arg1	types					34:38	three types	28:38	three types of sugar chains	28:54	Pro-major basic protein has three types of sugar chains at the pro-portion.
8507662	5	33	contain	has	684:686	arg2	glycosaminoglycan					746:762	glycosaminoglycan	746:762	glycosaminoglycan	746:762	The results indicated that proMBP has three types of sugar chains, O-glycoside, N-glycoside and glycosaminoglycan, in the pro-portion.
8507662	5	33	contain	has	684:686	arg2	N-glycoside					730:740	N-glycoside	730:740	N-glycoside	730:740	The results indicated that proMBP has three types of sugar chains, O-glycoside, N-glycoside and glycosaminoglycan, in the pro-portion.
8507662	5	33	contain	has	684:686	arg1	proMBP					677:682	proMBP	677:682	proMBP	677:682	The results indicated that proMBP has three types of sugar chains, O-glycoside, N-glycoside and glycosaminoglycan, in the pro-portion.
8507662	5	33	contain	has	684:686	arg2	O-glycoside					717:727	O-glycoside	717:727	O-glycoside	717:727	The results indicated that proMBP has three types of sugar chains, O-glycoside, N-glycoside and glycosaminoglycan, in the pro-portion.
8507662	5	33	contain	has	684:686	arg2	types					694:698	three types	688:698	three types of sugar chains	688:714	The results indicated that proMBP has three types of sugar chains, O-glycoside, N-glycoside and glycosaminoglycan, in the pro-portion.
8507662	1	34	theme	protein	140:146	arg1	sequence					91:98	The amino-acid sequence	76:98	The amino-acid sequence of purified recombinant pro-major basic protein from Chinese hamster kidney cells	76:180	The amino-acid sequence of purified recombinant pro-major basic protein from Chinese hamster kidney cells was determined to verify the primary structure and glycosylation sites.
8507662	1	35	theme	glycosylation	233:245	arg1	sites					247:251	glycosylation sites	233:251	glycosylation sites	233:251	The amino-acid sequence of purified recombinant pro-major basic protein from Chinese hamster kidney cells was determined to verify the primary structure and glycosylation sites.
25326458	3	0	attach	attached	490:497	arg2	chains					479:484	the CS chains	472:484	the CS chains	472:484	Although many aspects of CSPGs have been studied extensively, little is known of where the CS chains are attached on the core proteins and so far, only a limited number of CSPGs have been identified.
25326458	3	0	attach	attached	490:497	arg3	proteins					511:518	the core proteins	502:518	the core proteins	502:518	Although many aspects of CSPGs have been studied extensively, little is known of where the CS chains are attached on the core proteins and so far, only a limited number of CSPGs have been identified.
25326458	9	1	theme	proteins	1914:1921	arg1	assembly					1882:1889	the assembly	1878:1889	the assembly of chromogranin A core proteins	1878:1921	We hypothesized that the CS side chain may influence the assembly and structural organization of secretory granules and applied surface plasmon resonance spectroscopy to show that CS actually promotes the assembly of chromogranin A core proteins in vitro.
25326458	10	2	contain	has	2146:2148	arg1	A					2144:2144	chromogranin A	2131:2144	chromogranin A	2131:2144	This activity required mild acidic pH and suggests that the CS-side chains may also influence the self-assembly of chromogranin A in vivo giving a possible explanation to previous observations that chromogranin A has an inherent property to assemble in the acidic milieu of secretory granules.
25326458	10	2	contain	has	2146:2148	arg2	property					2162:2169	an inherent property	2150:2169	an inherent property to assemble in the acidic milieu of secretory granules	2150:2224	This activity required mild acidic pH and suggests that the CS-side chains may also influence the self-assembly of chromogranin A in vivo giving a possible explanation to previous observations that chromogranin A has an inherent property to assemble in the acidic milieu of secretory granules.
25326458	10	2	contain	has	2146:2148	arg2	observations					2113:2124	previous observations	2104:2124	previous observations that chromogranin A has an inherent property to assemble in the acidic milieu of secretory granules	2104:2224	This activity required mild acidic pH and suggests that the CS-side chains may also influence the self-assembly of chromogranin A in vivo giving a possible explanation to previous observations that chromogranin A has an inherent property to assemble in the acidic milieu of secretory granules.
25326458	6	3	theme	glycopeptide	1199:1210	arg1	algorithm					1219:1227	a novel glycopeptide search algorithm	1191:1227	a novel glycopeptide search algorithm	1191:1227	CSPGs were enriched from human urine and cerebrospinal fluid samples by strong-anion-exchange chromatography, digested with chondroitinase ABC, a specific CS-lyase used to reduce the CS chain lengths and subsequently analyzed by nLC-MS/MS with a novel glycopeptide search algorithm.
25326458	10	4	theme	previous	2104:2111	arg1	observations					2113:2124	previous observations	2104:2124	previous observations that chromogranin A has an inherent property to assemble in the acidic milieu of secretory granules	2104:2224	This activity required mild acidic pH and suggests that the CS-side chains may also influence the self-assembly of chromogranin A in vivo giving a possible explanation to previous observations that chromogranin A has an inherent property to assemble in the acidic milieu of secretory granules.
25326458	8	5	theme	endocrine	1660:1668	arg1	cells					1670:1674	endocrine cells	1660:1674	endocrine cells	1660:1674	Surprisingly, five of the identified CSPGs are traditionally defined as prohormones (cholecystokinin, chromogranin A, neuropeptide W, secretogranin-1, and secretogranin-3), typically stored and secreted from granules of endocrine cells.
25326458	3	6	theme	limited	539:545	arg1	number					547:552	only a limited number	532:552	only a limited number of CSPGs	532:561	Although many aspects of CSPGs have been studied extensively, little is known of where the CS chains are attached on the core proteins and so far, only a limited number of CSPGs have been identified.
25326458	8	7	dep	prohormones	1512:1522	arg1	A					1555:1555	chromogranin A	1542:1555	chromogranin A	1542:1555	Surprisingly, five of the identified CSPGs are traditionally defined as prohormones (cholecystokinin, chromogranin A, neuropeptide W, secretogranin-1, and secretogranin-3), typically stored and secreted from granules of endocrine cells.
25326458	8	7	dep	prohormones	1512:1522	arg1	secreted					1634:1641	secreted	1634:1641	secreted from granules of endocrine cells	1634:1674	Surprisingly, five of the identified CSPGs are traditionally defined as prohormones (cholecystokinin, chromogranin A, neuropeptide W, secretogranin-1, and secretogranin-3), typically stored and secreted from granules of endocrine cells.
25326458	8	7	dep	prohormones	1512:1522	arg1	secretogranin-3					1595:1609	secretogranin-3	1595:1609	secretogranin-3	1595:1609	Surprisingly, five of the identified CSPGs are traditionally defined as prohormones (cholecystokinin, chromogranin A, neuropeptide W, secretogranin-1, and secretogranin-3), typically stored and secreted from granules of endocrine cells.
25326458	8	7	dep	prohormones	1512:1522	arg1	prohormones					1512:1522	prohormones	1512:1522	prohormones (cholecystokinin, chromogranin A, neuropeptide W, secretogranin-1, and secretogranin-3)	1512:1610	Surprisingly, five of the identified CSPGs are traditionally defined as prohormones (cholecystokinin, chromogranin A, neuropeptide W, secretogranin-1, and secretogranin-3), typically stored and secreted from granules of endocrine cells.
25326458	8	7	dep	prohormones	1512:1522	arg1	cholecystokinin					1525:1539	cholecystokinin	1525:1539	cholecystokinin	1525:1539	Surprisingly, five of the identified CSPGs are traditionally defined as prohormones (cholecystokinin, chromogranin A, neuropeptide W, secretogranin-1, and secretogranin-3), typically stored and secreted from granules of endocrine cells.
25326458	8	7	dep	prohormones	1512:1522	arg1	W					1571:1571	neuropeptide W	1558:1571	neuropeptide W	1558:1571	Surprisingly, five of the identified CSPGs are traditionally defined as prohormones (cholecystokinin, chromogranin A, neuropeptide W, secretogranin-1, and secretogranin-3), typically stored and secreted from granules of endocrine cells.
25326458	8	7	dep	prohormones	1512:1522	arg1	secretogranin-1					1574:1588	secretogranin-1	1574:1588	secretogranin-1	1574:1588	Surprisingly, five of the identified CSPGs are traditionally defined as prohormones (cholecystokinin, chromogranin A, neuropeptide W, secretogranin-1, and secretogranin-3), typically stored and secreted from granules of endocrine cells.
25326458	8	7	dep	prohormones	1512:1522	arg1	stored					1623:1628	stored	1623:1628	stored	1623:1628	Surprisingly, five of the identified CSPGs are traditionally defined as prohormones (cholecystokinin, chromogranin A, neuropeptide W, secretogranin-1, and secretogranin-3), typically stored and secreted from granules of endocrine cells.
25326458	10	8	theme	acidic	1961:1966	arg1	pH					1968:1969	mild acidic pH	1956:1969	mild acidic pH	1956:1969	This activity required mild acidic pH and suggests that the CS-side chains may also influence the self-assembly of chromogranin A in vivo giving a possible explanation to previous observations that chromogranin A has an inherent property to assemble in the acidic milieu of secretory granules.
25326458	5	9	theme	CS	876:877	arg1	regions					887:893	CS linkage regions	876:893	CS linkage regions	876:893	In the present work, we have developed a glycoproteomics approach that characterizes CS linkage regions, attachment sites, and identities of core proteins.
25326458	9	10	theme	CS	1702:1703	arg1	chain					1710:1714	the CS side chain	1698:1714	the CS side chain	1698:1714	We hypothesized that the CS side chain may influence the assembly and structural organization of secretory granules and applied surface plasmon resonance spectroscopy to show that CS actually promotes the assembly of chromogranin A core proteins in vitro.
25326458	7	11	theme	human	1425:1429	arg1	samples					1431:1437	complex human samples	1417:1437	complex human samples	1417:1437	The protocol enabled the identification of 13 novel CSPGs, in addition to 13 previously established CSPGs, demonstrating that this approach can be routinely used to characterize CSPGs in complex human samples.
25326458	10	12	theme	CS-side	1993:1999	arg1	chains					2001:2006	the CS-side chains	1989:2006	the CS-side chains	1989:2006	This activity required mild acidic pH and suggests that the CS-side chains may also influence the self-assembly of chromogranin A in vivo giving a possible explanation to previous observations that chromogranin A has an inherent property to assemble in the acidic milieu of secretory granules.
25326458	2	13	theme	processes	336:344	arg1	regulation					305:314	the regulation	301:314	the regulation of more specialized processes such as neurogenesis and angiogenesis	301:382	CSPGs also contribute to the regulation of more specialized processes such as neurogenesis and angiogenesis.
25326458	1	14	theme	important	201:209	arg1	components					222:231	important structural components	201:231	important structural components of cartilage and other connective tissues	201:273	Vertebrates produce various chondroitin sulfate proteoglycans (CSPGs) that are important structural components of cartilage and other connective tissues.
25326458	1	14	theme	important	201:209	arg1	proteoglycans					170:182	various chondroitin sulfate proteoglycans	142:182	various chondroitin sulfate proteoglycans (CSPGs) that are important structural components of cartilage and other connective tissues	142:273	Vertebrates produce various chondroitin sulfate proteoglycans (CSPGs) that are important structural components of cartilage and other connective tissues.
25326458	6	15	theme	human	972:976	arg1	urine					978:982	human urine	972:982	human urine	972:982	CSPGs were enriched from human urine and cerebrospinal fluid samples by strong-anion-exchange chromatography, digested with chondroitinase ABC, a specific CS-lyase used to reduce the CS chain lengths and subsequently analyzed by nLC-MS/MS with a novel glycopeptide search algorithm.
25326458	5	16	theme	glycoproteomics	832:846	arg1	approach					848:855	a glycoproteomics approach	830:855	a glycoproteomics approach that characterizes CS linkage regions, attachment sites, and identities of core proteins	830:944	In the present work, we have developed a glycoproteomics approach that characterizes CS linkage regions, attachment sites, and identities of core proteins.
25326458	7	17	used	used	1387:1390	arg2	approach					1361:1368	this approach	1356:1368	this approach	1356:1368	The protocol enabled the identification of 13 novel CSPGs, in addition to 13 previously established CSPGs, demonstrating that this approach can be routinely used to characterize CSPGs in complex human samples.
25326458	6	18	gly	glycopeptide	1199:1210	arg2	glycopeptide					1199:1210	a novel glycopeptide search algorithm	1191:1227	a novel glycopeptide search algorithm	1191:1227	CSPGs were enriched from human urine and cerebrospinal fluid samples by strong-anion-exchange chromatography, digested with chondroitinase ABC, a specific CS-lyase used to reduce the CS chain lengths and subsequently analyzed by nLC-MS/MS with a novel glycopeptide search algorithm.
25326458	1	19	theme	cartilage	236:244	arg1	components					222:231	important structural components	201:231	important structural components of cartilage and other connective tissues	201:273	Vertebrates produce various chondroitin sulfate proteoglycans (CSPGs) that are important structural components of cartilage and other connective tissues.
25326458	1	19	theme	cartilage	236:244	arg1	proteoglycans					170:182	various chondroitin sulfate proteoglycans	142:182	various chondroitin sulfate proteoglycans (CSPGs) that are important structural components of cartilage and other connective tissues	142:273	Vertebrates produce various chondroitin sulfate proteoglycans (CSPGs) that are important structural components of cartilage and other connective tissues.
25326458	8	20	theme	identified	1466:1475	arg1	CSPGs					1477:1481	the identified CSPGs	1462:1481	the identified CSPGs	1462:1481	Surprisingly, five of the identified CSPGs are traditionally defined as prohormones (cholecystokinin, chromogranin A, neuropeptide W, secretogranin-1, and secretogranin-3), typically stored and secreted from granules of endocrine cells.
25326458	4	21	theme	structures	722:731	arg1	understanding					680:692	our understanding	676:692	our understanding of the complex proteoglycan structures	676:731	Obtaining global information on glycan structures and attachment sites would contribute to our understanding of the complex proteoglycan structures and may also assist in assigning CSPG specific functions.
25326458	9	22	theme	structural	1747:1756	arg1	organization					1758:1769	structural organization	1747:1769	structural organization	1747:1769	We hypothesized that the CS side chain may influence the assembly and structural organization of secretory granules and applied surface plasmon resonance spectroscopy to show that CS actually promotes the assembly of chromogranin A core proteins in vitro.
25326458	10	23	theme	chromogranin	2048:2059	arg1	A					2061:2061	chromogranin A	2048:2061	chromogranin A	2048:2061	This activity required mild acidic pH and suggests that the CS-side chains may also influence the self-assembly of chromogranin A in vivo giving a possible explanation to previous observations that chromogranin A has an inherent property to assemble in the acidic milieu of secretory granules.
25326458	5	24	theme	core	932:935	arg1	proteins					937:944	core proteins	932:944	core proteins	932:944	In the present work, we have developed a glycoproteomics approach that characterizes CS linkage regions, attachment sites, and identities of core proteins.
25326458	5	25	theme	attachment	896:905	arg1	sites					907:911	attachment sites	896:911	attachment sites	896:911	In the present work, we have developed a glycoproteomics approach that characterizes CS linkage regions, attachment sites, and identities of core proteins.
25326458	5	25	theme	attachment	896:905	arg1	proteins					937:944	core proteins	932:944	core proteins	932:944	In the present work, we have developed a glycoproteomics approach that characterizes CS linkage regions, attachment sites, and identities of core proteins.
25326458	9	26	theme	granules	1784:1791	arg1	assembly					1734:1741	assembly	1734:1741	assembly	1734:1741	We hypothesized that the CS side chain may influence the assembly and structural organization of secretory granules and applied surface plasmon resonance spectroscopy to show that CS actually promotes the assembly of chromogranin A core proteins in vitro.
25326458	9	26	theme	granules	1784:1791	arg1	organization					1758:1769	structural organization	1747:1769	structural organization	1747:1769	We hypothesized that the CS side chain may influence the assembly and structural organization of secretory granules and applied surface plasmon resonance spectroscopy to show that CS actually promotes the assembly of chromogranin A core proteins in vitro.
25326458	10	27	theme	secretory	2207:2215	arg1	granules					2217:2224	secretory granules	2207:2224	secretory granules	2207:2224	This activity required mild acidic pH and suggests that the CS-side chains may also influence the self-assembly of chromogranin A in vivo giving a possible explanation to previous observations that chromogranin A has an inherent property to assemble in the acidic milieu of secretory granules.
25326458	4	28	theme	complex	701:707	arg1	structures					722:731	the complex proteoglycan structures	697:731	the complex proteoglycan structures	697:731	Obtaining global information on glycan structures and attachment sites would contribute to our understanding of the complex proteoglycan structures and may also assist in assigning CSPG specific functions.
25326458	6	29	theme	fluid	1002:1006	arg1	samples					1008:1014	human urine and cerebrospinal fluid samples	972:1014	human urine and cerebrospinal fluid samples	972:1014	CSPGs were enriched from human urine and cerebrospinal fluid samples by strong-anion-exchange chromatography, digested with chondroitinase ABC, a specific CS-lyase used to reduce the CS chain lengths and subsequently analyzed by nLC-MS/MS with a novel glycopeptide search algorithm.
25326458	3	30	theme	many	394:397	arg1	aspects					399:405	many aspects	394:405	many aspects of CSPGs	394:414	Although many aspects of CSPGs have been studied extensively, little is known of where the CS chains are attached on the core proteins and so far, only a limited number of CSPGs have been identified.
25326458	4	31	theme	specific	771:778	arg1	functions					780:788	CSPG specific functions	766:788	CSPG specific functions	766:788	Obtaining global information on glycan structures and attachment sites would contribute to our understanding of the complex proteoglycan structures and may also assist in assigning CSPG specific functions.
25326458	1	32	theme	chondroitin	150:160	arg1	components					222:231	important structural components	201:231	important structural components of cartilage and other connective tissues	201:273	Vertebrates produce various chondroitin sulfate proteoglycans (CSPGs) that are important structural components of cartilage and other connective tissues.
25326458	1	32	theme	chondroitin	150:160	arg1	proteoglycans					170:182	various chondroitin sulfate proteoglycans	142:182	various chondroitin sulfate proteoglycans (CSPGs) that are important structural components of cartilage and other connective tissues	142:273	Vertebrates produce various chondroitin sulfate proteoglycans (CSPGs) that are important structural components of cartilage and other connective tissues.
25326458	1	32	theme	chondroitin	150:160	arg1	CSPGs					185:189	CSPGs	185:189	CSPGs	185:189	Vertebrates produce various chondroitin sulfate proteoglycans (CSPGs) that are important structural components of cartilage and other connective tissues.
25326458	9	33	theme	plasmon	1813:1819	arg1	resonance					1821:1829	surface plasmon resonance	1805:1829	surface plasmon resonance spectroscopy	1805:1842	We hypothesized that the CS side chain may influence the assembly and structural organization of secretory granules and applied surface plasmon resonance spectroscopy to show that CS actually promotes the assembly of chromogranin A core proteins in vitro.
25326458	8	34	theme	chromogranin	1542:1553	arg1	A					1555:1555	chromogranin A	1542:1555	chromogranin A	1542:1555	Surprisingly, five of the identified CSPGs are traditionally defined as prohormones (cholecystokinin, chromogranin A, neuropeptide W, secretogranin-1, and secretogranin-3), typically stored and secreted from granules of endocrine cells.
25326458	8	34	theme	chromogranin	1542:1553	arg1	prohormones					1512:1522	prohormones	1512:1522	prohormones (cholecystokinin, chromogranin A, neuropeptide W, secretogranin-1, and secretogranin-3)	1512:1610	Surprisingly, five of the identified CSPGs are traditionally defined as prohormones (cholecystokinin, chromogranin A, neuropeptide W, secretogranin-1, and secretogranin-3), typically stored and secreted from granules of endocrine cells.
25326458	0	35	theme	proteoglycans	107:119	arg1	class					98:102	a novel class	90:102	a novel class of proteoglycans	90:119	Identification of chondroitin sulfate linkage region glycopeptides reveals prohormones as a novel class of proteoglycans.
25326458	6	36	theme	specific	1093:1100	arg1	ABC					1086:1088	chondroitinase ABC	1071:1088	chondroitinase ABC	1071:1088	CSPGs were enriched from human urine and cerebrospinal fluid samples by strong-anion-exchange chromatography, digested with chondroitinase ABC, a specific CS-lyase used to reduce the CS chain lengths and subsequently analyzed by nLC-MS/MS with a novel glycopeptide search algorithm.
25326458	6	36	theme	specific	1093:1100	arg1	CS-lyase					1102:1109	a specific CS-lyase	1091:1109	a specific CS-lyase used to reduce the CS chain lengths	1091:1145	CSPGs were enriched from human urine and cerebrospinal fluid samples by strong-anion-exchange chromatography, digested with chondroitinase ABC, a specific CS-lyase used to reduce the CS chain lengths and subsequently analyzed by nLC-MS/MS with a novel glycopeptide search algorithm.
25326458	0	37	theme	chondroitin	18:28	arg1	sulfate					30:36	chondroitin sulfate linkage region glycopeptides	18:65	chondroitin sulfate linkage region glycopeptides	18:65	Identification of chondroitin sulfate linkage region glycopeptides reveals prohormones as a novel class of proteoglycans.
25326458	6	38	theme	chondroitinase	1071:1084	arg1	ABC					1086:1088	chondroitinase ABC	1071:1088	chondroitinase ABC	1071:1088	CSPGs were enriched from human urine and cerebrospinal fluid samples by strong-anion-exchange chromatography, digested with chondroitinase ABC, a specific CS-lyase used to reduce the CS chain lengths and subsequently analyzed by nLC-MS/MS with a novel glycopeptide search algorithm.
25326458	6	38	theme	chondroitinase	1071:1084	arg1	CS-lyase					1102:1109	a specific CS-lyase	1091:1109	a specific CS-lyase used to reduce the CS chain lengths	1091:1145	CSPGs were enriched from human urine and cerebrospinal fluid samples by strong-anion-exchange chromatography, digested with chondroitinase ABC, a specific CS-lyase used to reduce the CS chain lengths and subsequently analyzed by nLC-MS/MS with a novel glycopeptide search algorithm.
25326458	0	39	theme	linkage	38:44	arg1	glycopeptides					53:65	linkage region glycopeptides	38:65	chondroitin sulfate linkage region glycopeptides	18:65	Identification of chondroitin sulfate linkage region glycopeptides reveals prohormones as a novel class of proteoglycans.
25326458	8	40	theme	cells	1670:1674	arg1	granules					1648:1655	granules	1648:1655	granules of endocrine cells	1648:1674	Surprisingly, five of the identified CSPGs are traditionally defined as prohormones (cholecystokinin, chromogranin A, neuropeptide W, secretogranin-1, and secretogranin-3), typically stored and secreted from granules of endocrine cells.
25326458	6	41	theme	CS	1130:1131	arg1	lengths					1139:1145	the CS chain lengths	1126:1145	the CS chain lengths	1126:1145	CSPGs were enriched from human urine and cerebrospinal fluid samples by strong-anion-exchange chromatography, digested with chondroitinase ABC, a specific CS-lyase used to reduce the CS chain lengths and subsequently analyzed by nLC-MS/MS with a novel glycopeptide search algorithm.
25326458	9	42	theme	chromogranin	1894:1905	arg1	A					1907:1907	chromogranin A	1894:1907	chromogranin A core proteins	1894:1921	We hypothesized that the CS side chain may influence the assembly and structural organization of secretory granules and applied surface plasmon resonance spectroscopy to show that CS actually promotes the assembly of chromogranin A core proteins in vitro.
25326458	4	43	theme	global	595:600	arg1	information					602:612	global information	595:612	global information on glycan structures and attachment sites	595:654	Obtaining global information on glycan structures and attachment sites would contribute to our understanding of the complex proteoglycan structures and may also assist in assigning CSPG specific functions.
25326458	1	44	theme	connective	256:265	arg1	tissues					267:273	other connective tissues	250:273	other connective tissues	250:273	Vertebrates produce various chondroitin sulfate proteoglycans (CSPGs) that are important structural components of cartilage and other connective tissues.
25326458	7	45	dep	CSPGs	1330:1334	arg1	addition					1292:1299	addition	1292:1299	addition	1292:1299	The protocol enabled the identification of 13 novel CSPGs, in addition to 13 previously established CSPGs, demonstrating that this approach can be routinely used to characterize CSPGs in complex human samples.
25326458	7	46	theme	CSPGs	1282:1286	arg1	identification					1255:1268	the identification	1251:1268	the identification of 13 novel CSPGs	1251:1286	The protocol enabled the identification of 13 novel CSPGs, in addition to 13 previously established CSPGs, demonstrating that this approach can be routinely used to characterize CSPGs in complex human samples.
25326458	9	47	theme	core	1909:1912	arg1	proteins					1914:1921	chromogranin A core proteins	1894:1921	chromogranin A core proteins	1894:1921	We hypothesized that the CS side chain may influence the assembly and structural organization of secretory granules and applied surface plasmon resonance spectroscopy to show that CS actually promotes the assembly of chromogranin A core proteins in vitro.
25326458	4	48	from	information	602:612	arg1	structures					624:633	glycan structures	617:633	glycan structures	617:633	Obtaining global information on glycan structures and attachment sites would contribute to our understanding of the complex proteoglycan structures and may also assist in assigning CSPG specific functions.
25326458	4	48	from	information	602:612	arg1	sites					650:654	attachment sites	639:654	attachment sites	639:654	Obtaining global information on glycan structures and attachment sites would contribute to our understanding of the complex proteoglycan structures and may also assist in assigning CSPG specific functions.
25326458	6	49	theme	novel	1193:1197	arg1	algorithm					1219:1227	a novel glycopeptide search algorithm	1191:1227	a novel glycopeptide search algorithm	1191:1227	CSPGs were enriched from human urine and cerebrospinal fluid samples by strong-anion-exchange chromatography, digested with chondroitinase ABC, a specific CS-lyase used to reduce the CS chain lengths and subsequently analyzed by nLC-MS/MS with a novel glycopeptide search algorithm.
25326458	10	50	theme	inherent	2153:2160	arg1	property					2162:2169	an inherent property	2150:2169	an inherent property to assemble in the acidic milieu of secretory granules	2150:2224	This activity required mild acidic pH and suggests that the CS-side chains may also influence the self-assembly of chromogranin A in vivo giving a possible explanation to previous observations that chromogranin A has an inherent property to assemble in the acidic milieu of secretory granules.
25326458	10	51	theme	mild	1956:1959	arg1	pH					1968:1969	mild acidic pH	1956:1969	mild acidic pH	1956:1969	This activity required mild acidic pH and suggests that the CS-side chains may also influence the self-assembly of chromogranin A in vivo giving a possible explanation to previous observations that chromogranin A has an inherent property to assemble in the acidic milieu of secretory granules.
25326458	3	52	theme	CSPGs	557:561	arg1	number					547:552	only a limited number	532:552	only a limited number of CSPGs	532:561	Although many aspects of CSPGs have been studied extensively, little is known of where the CS chains are attached on the core proteins and so far, only a limited number of CSPGs have been identified.
25326458	5	53	theme	linkage	879:885	arg1	regions					887:893	CS linkage regions	876:893	CS linkage regions	876:893	In the present work, we have developed a glycoproteomics approach that characterizes CS linkage regions, attachment sites, and identities of core proteins.
25326458	6	54	theme	urine	978:982	arg1	samples					1008:1014	human urine and cerebrospinal fluid samples	972:1014	human urine and cerebrospinal fluid samples	972:1014	CSPGs were enriched from human urine and cerebrospinal fluid samples by strong-anion-exchange chromatography, digested with chondroitinase ABC, a specific CS-lyase used to reduce the CS chain lengths and subsequently analyzed by nLC-MS/MS with a novel glycopeptide search algorithm.
25326458	9	55	theme	side	1705:1708	arg1	chain					1710:1714	the CS side chain	1698:1714	the CS side chain	1698:1714	We hypothesized that the CS side chain may influence the assembly and structural organization of secretory granules and applied surface plasmon resonance spectroscopy to show that CS actually promotes the assembly of chromogranin A core proteins in vitro.
25326458	2	56	theme	specialized	324:334	arg1	angiogenesis					371:382	angiogenesis	371:382	angiogenesis	371:382	CSPGs also contribute to the regulation of more specialized processes such as neurogenesis and angiogenesis.
25326458	2	56	theme	specialized	324:334	arg1	processes					336:344	more specialized processes	319:344	more specialized processes such as neurogenesis and angiogenesis	319:382	CSPGs also contribute to the regulation of more specialized processes such as neurogenesis and angiogenesis.
25326458	2	56	theme	specialized	324:334	arg1	neurogenesis					354:365	neurogenesis	354:365	neurogenesis	354:365	CSPGs also contribute to the regulation of more specialized processes such as neurogenesis and angiogenesis.
25326458	1	57	theme	structural	211:220	arg1	components					222:231	important structural components	201:231	important structural components of cartilage and other connective tissues	201:273	Vertebrates produce various chondroitin sulfate proteoglycans (CSPGs) that are important structural components of cartilage and other connective tissues.
25326458	1	57	theme	structural	211:220	arg1	proteoglycans					170:182	various chondroitin sulfate proteoglycans	142:182	various chondroitin sulfate proteoglycans (CSPGs) that are important structural components of cartilage and other connective tissues	142:273	Vertebrates produce various chondroitin sulfate proteoglycans (CSPGs) that are important structural components of cartilage and other connective tissues.
25326458	7	58	theme	complex	1417:1423	arg1	samples					1431:1437	complex human samples	1417:1437	complex human samples	1417:1437	The protocol enabled the identification of 13 novel CSPGs, in addition to 13 previously established CSPGs, demonstrating that this approach can be routinely used to characterize CSPGs in complex human samples.
25326458	8	59	theme	CSPGs	1477:1481	arg1	prohormones					1512:1522	prohormones	1512:1522	prohormones (cholecystokinin, chromogranin A, neuropeptide W, secretogranin-1, and secretogranin-3)	1512:1610	Surprisingly, five of the identified CSPGs are traditionally defined as prohormones (cholecystokinin, chromogranin A, neuropeptide W, secretogranin-1, and secretogranin-3), typically stored and secreted from granules of endocrine cells.
25326458	8	59	theme	CSPGs	1477:1481	arg1	CSPGs					1477:1481	the identified CSPGs	1462:1481	the identified CSPGs	1462:1481	Surprisingly, five of the identified CSPGs are traditionally defined as prohormones (cholecystokinin, chromogranin A, neuropeptide W, secretogranin-1, and secretogranin-3), typically stored and secreted from granules of endocrine cells.
25326458	8	59	theme	CSPGs	1477:1481	arg1	five					1454:1457	five	1454:1457	five	1454:1457	Surprisingly, five of the identified CSPGs are traditionally defined as prohormones (cholecystokinin, chromogranin A, neuropeptide W, secretogranin-1, and secretogranin-3), typically stored and secreted from granules of endocrine cells.
25326458	4	60	theme	attachment	639:648	arg1	sites					650:654	attachment sites	639:654	attachment sites	639:654	Obtaining global information on glycan structures and attachment sites would contribute to our understanding of the complex proteoglycan structures and may also assist in assigning CSPG specific functions.
25326458	6	61	with	nLC-MS/MS	1176:1184	arg1	algorithm					1219:1227	a novel glycopeptide search algorithm	1191:1227	a novel glycopeptide search algorithm	1191:1227	CSPGs were enriched from human urine and cerebrospinal fluid samples by strong-anion-exchange chromatography, digested with chondroitinase ABC, a specific CS-lyase used to reduce the CS chain lengths and subsequently analyzed by nLC-MS/MS with a novel glycopeptide search algorithm.
25326458	10	62	theme	acidic	2190:2195	arg1	milieu					2197:2202	the acidic milieu	2186:2202	the acidic milieu of secretory granules	2186:2224	This activity required mild acidic pH and suggests that the CS-side chains may also influence the self-assembly of chromogranin A in vivo giving a possible explanation to previous observations that chromogranin A has an inherent property to assemble in the acidic milieu of secretory granules.
25326458	4	63	theme	proteoglycan	709:720	arg1	structures					722:731	the complex proteoglycan structures	697:731	the complex proteoglycan structures	697:731	Obtaining global information on glycan structures and attachment sites would contribute to our understanding of the complex proteoglycan structures and may also assist in assigning CSPG specific functions.
25326458	1	64	theme	various	142:148	arg1	components					222:231	important structural components	201:231	important structural components of cartilage and other connective tissues	201:273	Vertebrates produce various chondroitin sulfate proteoglycans (CSPGs) that are important structural components of cartilage and other connective tissues.
25326458	1	64	theme	various	142:148	arg1	proteoglycans					170:182	various chondroitin sulfate proteoglycans	142:182	various chondroitin sulfate proteoglycans (CSPGs) that are important structural components of cartilage and other connective tissues	142:273	Vertebrates produce various chondroitin sulfate proteoglycans (CSPGs) that are important structural components of cartilage and other connective tissues.
25326458	1	64	theme	various	142:148	arg1	CSPGs					185:189	CSPGs	185:189	CSPGs	185:189	Vertebrates produce various chondroitin sulfate proteoglycans (CSPGs) that are important structural components of cartilage and other connective tissues.
25326458	1	65	theme	sulfate	162:168	arg1	components					222:231	important structural components	201:231	important structural components of cartilage and other connective tissues	201:273	Vertebrates produce various chondroitin sulfate proteoglycans (CSPGs) that are important structural components of cartilage and other connective tissues.
25326458	1	65	theme	sulfate	162:168	arg1	proteoglycans					170:182	various chondroitin sulfate proteoglycans	142:182	various chondroitin sulfate proteoglycans (CSPGs) that are important structural components of cartilage and other connective tissues	142:273	Vertebrates produce various chondroitin sulfate proteoglycans (CSPGs) that are important structural components of cartilage and other connective tissues.
25326458	1	65	theme	sulfate	162:168	arg1	CSPGs					185:189	CSPGs	185:189	CSPGs	185:189	Vertebrates produce various chondroitin sulfate proteoglycans (CSPGs) that are important structural components of cartilage and other connective tissues.
25326458	6	66	theme	strong-anion-exchange	1019:1039	arg1	chromatography					1041:1054	strong-anion-exchange chromatography	1019:1054	strong-anion-exchange chromatography	1019:1054	CSPGs were enriched from human urine and cerebrospinal fluid samples by strong-anion-exchange chromatography, digested with chondroitinase ABC, a specific CS-lyase used to reduce the CS chain lengths and subsequently analyzed by nLC-MS/MS with a novel glycopeptide search algorithm.
25326458	9	67	theme	secretory	1774:1782	arg1	granules					1784:1791	secretory granules	1774:1791	secretory granules	1774:1791	We hypothesized that the CS side chain may influence the assembly and structural organization of secretory granules and applied surface plasmon resonance spectroscopy to show that CS actually promotes the assembly of chromogranin A core proteins in vitro.
25326458	6	68	theme	search	1212:1217	arg1	algorithm					1219:1227	a novel glycopeptide search algorithm	1191:1227	a novel glycopeptide search algorithm	1191:1227	CSPGs were enriched from human urine and cerebrospinal fluid samples by strong-anion-exchange chromatography, digested with chondroitinase ABC, a specific CS-lyase used to reduce the CS chain lengths and subsequently analyzed by nLC-MS/MS with a novel glycopeptide search algorithm.
25326458	10	69	theme	granules	2217:2224	arg1	milieu					2197:2202	the acidic milieu	2186:2202	the acidic milieu of secretory granules	2186:2224	This activity required mild acidic pH and suggests that the CS-side chains may also influence the self-assembly of chromogranin A in vivo giving a possible explanation to previous observations that chromogranin A has an inherent property to assemble in the acidic milieu of secretory granules.
25326458	0	70	theme	novel	92:96	arg1	class					98:102	a novel class	90:102	a novel class of proteoglycans	90:119	Identification of chondroitin sulfate linkage region glycopeptides reveals prohormones as a novel class of proteoglycans.
25326458	6	71	theme	cerebrospinal	988:1000	arg1	fluid					1002:1006	cerebrospinal fluid	988:1006	cerebrospinal fluid	988:1006	CSPGs were enriched from human urine and cerebrospinal fluid samples by strong-anion-exchange chromatography, digested with chondroitinase ABC, a specific CS-lyase used to reduce the CS chain lengths and subsequently analyzed by nLC-MS/MS with a novel glycopeptide search algorithm.
25326458	9	72	theme	surface	1805:1811	arg1	resonance					1821:1829	surface plasmon resonance	1805:1829	surface plasmon resonance spectroscopy	1805:1842	We hypothesized that the CS side chain may influence the assembly and structural organization of secretory granules and applied surface plasmon resonance spectroscopy to show that CS actually promotes the assembly of chromogranin A core proteins in vitro.
25326458	4	73	theme	CSPG	766:769	arg1	functions					780:788	CSPG specific functions	766:788	CSPG specific functions	766:788	Obtaining global information on glycan structures and attachment sites would contribute to our understanding of the complex proteoglycan structures and may also assist in assigning CSPG specific functions.
25326458	10	74	theme	A	2061:2061	arg1	self-assembly					2031:2043	the self-assembly	2027:2043	the self-assembly of chromogranin A	2027:2061	This activity required mild acidic pH and suggests that the CS-side chains may also influence the self-assembly of chromogranin A in vivo giving a possible explanation to previous observations that chromogranin A has an inherent property to assemble in the acidic milieu of secretory granules.
25326458	9	75	dep	assembly	1734:1741	arg1	the					1730:1732	the	1730:1732	the	1730:1732	We hypothesized that the CS side chain may influence the assembly and structural organization of secretory granules and applied surface plasmon resonance spectroscopy to show that CS actually promotes the assembly of chromogranin A core proteins in vitro.
25326458	10	76	theme	possible	2080:2087	arg1	explanation					2089:2099	a possible explanation	2078:2099	a possible explanation to previous observations that chromogranin A has an inherent property to assemble in the acidic milieu of secretory granules	2078:2224	This activity required mild acidic pH and suggests that the CS-side chains may also influence the self-assembly of chromogranin A in vivo giving a possible explanation to previous observations that chromogranin A has an inherent property to assemble in the acidic milieu of secretory granules.
25326458	9	77	theme	resonance	1821:1829	arg1	spectroscopy					1831:1842	surface plasmon resonance spectroscopy	1805:1842	surface plasmon resonance spectroscopy	1805:1842	We hypothesized that the CS side chain may influence the assembly and structural organization of secretory granules and applied surface plasmon resonance spectroscopy to show that CS actually promotes the assembly of chromogranin A core proteins in vitro.
25326458	8	78	theme	neuropeptide	1558:1569	arg1	W					1571:1571	neuropeptide W	1558:1571	neuropeptide W	1558:1571	Surprisingly, five of the identified CSPGs are traditionally defined as prohormones (cholecystokinin, chromogranin A, neuropeptide W, secretogranin-1, and secretogranin-3), typically stored and secreted from granules of endocrine cells.
25326458	8	78	theme	neuropeptide	1558:1569	arg1	prohormones					1512:1522	prohormones	1512:1522	prohormones (cholecystokinin, chromogranin A, neuropeptide W, secretogranin-1, and secretogranin-3)	1512:1610	Surprisingly, five of the identified CSPGs are traditionally defined as prohormones (cholecystokinin, chromogranin A, neuropeptide W, secretogranin-1, and secretogranin-3), typically stored and secreted from granules of endocrine cells.
25326458	5	79	theme	proteins	937:944	arg1	sites					907:911	attachment sites	896:911	attachment sites	896:911	In the present work, we have developed a glycoproteomics approach that characterizes CS linkage regions, attachment sites, and identities of core proteins.
25326458	5	79	theme	proteins	937:944	arg1	identities					918:927	identities	918:927	identities of core proteins	918:944	In the present work, we have developed a glycoproteomics approach that characterizes CS linkage regions, attachment sites, and identities of core proteins.
25326458	5	79	theme	proteins	937:944	arg1	proteins					937:944	core proteins	932:944	core proteins	932:944	In the present work, we have developed a glycoproteomics approach that characterizes CS linkage regions, attachment sites, and identities of core proteins.
25326458	5	79	theme	proteins	937:944	arg1	regions					887:893	CS linkage regions	876:893	CS linkage regions	876:893	In the present work, we have developed a glycoproteomics approach that characterizes CS linkage regions, attachment sites, and identities of core proteins.
25326458	0	80	theme	sulfate	30:36	arg1	Identification					0:13	Identification	0:13	Identification of chondroitin sulfate linkage region glycopeptides	0:65	Identification of chondroitin sulfate linkage region glycopeptides reveals prohormones as a novel class of proteoglycans.
25326458	7	81	theme	established	1318:1328	arg1	CSPGs					1330:1334	13 previously established CSPGs	1304:1334	13 previously established CSPGs	1304:1334	The protocol enabled the identification of 13 novel CSPGs, in addition to 13 previously established CSPGs, demonstrating that this approach can be routinely used to characterize CSPGs in complex human samples.
25326458	3	82	theme	CSPGs	410:414	arg1	aspects					399:405	many aspects	394:405	many aspects of CSPGs	394:414	Although many aspects of CSPGs have been studied extensively, little is known of where the CS chains are attached on the core proteins and so far, only a limited number of CSPGs have been identified.
25326458	0	83	theme	region	46:51	arg1	glycopeptides					53:65	linkage region glycopeptides	38:65	chondroitin sulfate linkage region glycopeptides	18:65	Identification of chondroitin sulfate linkage region glycopeptides reveals prohormones as a novel class of proteoglycans.
25326458	7	84	from	CSPGs	1408:1412	arg1	samples					1431:1437	complex human samples	1417:1437	complex human samples	1417:1437	The protocol enabled the identification of 13 novel CSPGs, in addition to 13 previously established CSPGs, demonstrating that this approach can be routinely used to characterize CSPGs in complex human samples.
25326458	3	85	theme	CS	476:477	arg1	chains					479:484	the CS chains	472:484	the CS chains	472:484	Although many aspects of CSPGs have been studied extensively, little is known of where the CS chains are attached on the core proteins and so far, only a limited number of CSPGs have been identified.
25326458	5	86	theme	present	798:804	arg1	work					806:809	the present work	794:809	the present work	794:809	In the present work, we have developed a glycoproteomics approach that characterizes CS linkage regions, attachment sites, and identities of core proteins.
25326458	3	87	theme	core	506:509	arg1	proteins					511:518	the core proteins	502:518	the core proteins	502:518	Although many aspects of CSPGs have been studied extensively, little is known of where the CS chains are attached on the core proteins and so far, only a limited number of CSPGs have been identified.
25326458	0	88	dep	sulfate	30:36	arg1	glycopeptides					53:65	linkage region glycopeptides	38:65	chondroitin sulfate linkage region glycopeptides	18:65	Identification of chondroitin sulfate linkage region glycopeptides reveals prohormones as a novel class of proteoglycans.
25326458	6	89	theme	chain	1133:1137	arg1	lengths					1139:1145	the CS chain lengths	1126:1145	the CS chain lengths	1126:1145	CSPGs were enriched from human urine and cerebrospinal fluid samples by strong-anion-exchange chromatography, digested with chondroitinase ABC, a specific CS-lyase used to reduce the CS chain lengths and subsequently analyzed by nLC-MS/MS with a novel glycopeptide search algorithm.
25326458	1	90	theme	other	250:254	arg1	tissues					267:273	other connective tissues	250:273	other connective tissues	250:273	Vertebrates produce various chondroitin sulfate proteoglycans (CSPGs) that are important structural components of cartilage and other connective tissues.
25326458	0	91	gly	glycopeptides	53:65	arg2	glycopeptides					53:65	linkage region glycopeptides	38:65	chondroitin sulfate linkage region glycopeptides	18:65	Identification of chondroitin sulfate linkage region glycopeptides reveals prohormones as a novel class of proteoglycans.
25326458	10	92	theme	chromogranin	2131:2142	arg1	A					2144:2144	chromogranin A	2131:2144	chromogranin A	2131:2144	This activity required mild acidic pH and suggests that the CS-side chains may also influence the self-assembly of chromogranin A in vivo giving a possible explanation to previous observations that chromogranin A has an inherent property to assemble in the acidic milieu of secretory granules.
25326458	7	93	theme	novel	1276:1280	arg1	CSPGs					1282:1286	13 novel CSPGs	1273:1286	13 novel CSPGs	1273:1286	The protocol enabled the identification of 13 novel CSPGs, in addition to 13 previously established CSPGs, demonstrating that this approach can be routinely used to characterize CSPGs in complex human samples.
25326458	9	94	theme	A	1907:1907	arg1	proteins					1914:1921	chromogranin A core proteins	1894:1921	chromogranin A core proteins	1894:1921	We hypothesized that the CS side chain may influence the assembly and structural organization of secretory granules and applied surface plasmon resonance spectroscopy to show that CS actually promotes the assembly of chromogranin A core proteins in vitro.
25326458	4	95	theme	glycan	617:622	arg1	structures					624:633	glycan structures	617:633	glycan structures	617:633	Obtaining global information on glycan structures and attachment sites would contribute to our understanding of the complex proteoglycan structures and may also assist in assigning CSPG specific functions.
25326458	1	96	theme	tissues	267:273	arg1	components					222:231	important structural components	201:231	important structural components of cartilage and other connective tissues	201:273	Vertebrates produce various chondroitin sulfate proteoglycans (CSPGs) that are important structural components of cartilage and other connective tissues.
25326458	1	96	theme	tissues	267:273	arg1	proteoglycans					170:182	various chondroitin sulfate proteoglycans	142:182	various chondroitin sulfate proteoglycans (CSPGs) that are important structural components of cartilage and other connective tissues	142:273	Vertebrates produce various chondroitin sulfate proteoglycans (CSPGs) that are important structural components of cartilage and other connective tissues.
16293754	0	0	theme	beta	69:72	arg1	receptors					86:94	its alpha, beta, and gammac receptors	58:94	its alpha, beta, and gammac receptors	58:94	Structure of the quaternary complex of interleukin-2 with its alpha, beta, and gammac receptors.
16293754	2	1	theme	IL-2Ralpha	413:422	arg1	binding					402:408	the binding	398:408	the binding of IL-2Ralpha to IL-2	398:430	In the structure of the quaternary ectodomain complex as visualized at a resolution of 2.3 angstroms, the binding of IL-2Ralpha to IL-2 stabilizes a secondary binding site for presentation to IL-2Rbeta.
16293754	5	2	dep	immunodeficiency	841:856	arg1	diseases					858:865	diseases	858:865	X-linked severe combined immunodeficiency diseases (X-SCID)	816:874	The structure of gammac provides a rationale for loss-of-function mutations found in patients with X-linked severe combined immunodeficiency diseases (X-SCID).
16293754	4	3	with	contacts	697:704	arg1	IL-2					711:714	IL-2	711:714	IL-2	711:714	Consistent with its role as a shared receptor for IL-4, IL-7, IL-9, IL-15, and IL-21, gammac forms degenerate contacts with IL-2.
16293754	5	4	with	patients	802:809	arg1	immunodeficiency					841:856	X-linked severe combined immunodeficiency diseases	816:865	X-linked severe combined immunodeficiency diseases (X-SCID)	816:874	The structure of gammac provides a rationale for loss-of-function mutations found in patients with X-linked severe combined immunodeficiency diseases (X-SCID).
16293754	5	4	with	patients	802:809	arg1	X-SCID					868:873	X-SCID	868:873	X-SCID	868:873	The structure of gammac provides a rationale for loss-of-function mutations found in patients with X-linked severe combined immunodeficiency diseases (X-SCID).
16293754	1	5	theme	immunoregulatory	124:139	arg1	cytokine					141:148	an immunoregulatory cytokine	121:148	an immunoregulatory cytokine that acts through a quaternary receptor signaling complex containing alpha (IL-2Ralpha), beta (IL-2Rbeta), and common gamma chain (gc) receptors	121:293	Interleukin-2 (IL-2) is an immunoregulatory cytokine that acts through a quaternary receptor signaling complex containing alpha (IL-2Ralpha), beta (IL-2Rbeta), and common gamma chain (gc) receptors.
16293754	1	5	theme	immunoregulatory	124:139	arg1	Interleukin-2					97:109	Interleukin-2	97:109	Interleukin-2 (IL-2)	97:116	Interleukin-2 (IL-2) is an immunoregulatory cytokine that acts through a quaternary receptor signaling complex containing alpha (IL-2Ralpha), beta (IL-2Rbeta), and common gamma chain (gc) receptors.
16293754	2	6	theme	binding	455:461	arg1	site					463:466	a secondary binding site	443:466	a secondary binding site for presentation to IL-2Rbeta	443:496	In the structure of the quaternary ectodomain complex as visualized at a resolution of 2.3 angstroms, the binding of IL-2Ralpha to IL-2 stabilizes a secondary binding site for presentation to IL-2Rbeta.
16293754	2	7	theme	secondary	445:453	arg1	site					463:466	a secondary binding site	443:466	a secondary binding site for presentation to IL-2Rbeta	443:496	In the structure of the quaternary ectodomain complex as visualized at a resolution of 2.3 angstroms, the binding of IL-2Ralpha to IL-2 stabilizes a secondary binding site for presentation to IL-2Rbeta.
16293754	5	8	located	found	793:797	arg2	mutations					783:791	loss-of-function mutations	766:791	loss-of-function mutations found in patients with X-linked severe combined immunodeficiency diseases (X-SCID)	766:874	The structure of gammac provides a rationale for loss-of-function mutations found in patients with X-linked severe combined immunodeficiency diseases (X-SCID).
16293754	5	8	located	found	793:797	arg1	patients					802:809	patients	802:809	patients with X-linked severe combined immunodeficiency diseases (X-SCID)	802:874	The structure of gammac provides a rationale for loss-of-function mutations found in patients with X-linked severe combined immunodeficiency diseases (X-SCID).
16293754	6	9	theme	IL-2	1015:1018	arg1	therapeutics					1020:1031	improved IL-2 therapeutics	1006:1031	improved IL-2 therapeutics	1006:1031	This complex structure provides a framework for other gammac-dependent cytokine-receptor interactions and for the engineering of improved IL-2 therapeutics.
16293754	2	10	dep	structure	303:311	arg1	visualized					353:362	visualized	353:362	visualized at a resolution of 2.3 angstroms	353:395	In the structure of the quaternary ectodomain complex as visualized at a resolution of 2.3 angstroms, the binding of IL-2Ralpha to IL-2 stabilizes a secondary binding site for presentation to IL-2Rbeta.
16293754	2	11	theme	ectodomain	331:340	arg1	complex					342:348	the quaternary ectodomain complex	316:348	the quaternary ectodomain complex	316:348	In the structure of the quaternary ectodomain complex as visualized at a resolution of 2.3 angstroms, the binding of IL-2Ralpha to IL-2 stabilizes a secondary binding site for presentation to IL-2Rbeta.
16293754	0	12	theme	gammac	79:84	arg1	receptors					86:94	its alpha, beta, and gammac receptors	58:94	its alpha, beta, and gammac receptors	58:94	Structure of the quaternary complex of interleukin-2 with its alpha, beta, and gammac receptors.
16293754	6	13	theme	therapeutics	1020:1031	arg1	engineering					991:1001	the engineering	987:1001	the engineering of improved IL-2 therapeutics	987:1031	This complex structure provides a framework for other gammac-dependent cytokine-receptor interactions and for the engineering of improved IL-2 therapeutics.
16293754	2	14	theme	quaternary	320:329	arg1	complex					342:348	the quaternary ectodomain complex	316:348	the quaternary ectodomain complex	316:348	In the structure of the quaternary ectodomain complex as visualized at a resolution of 2.3 angstroms, the binding of IL-2Ralpha to IL-2 stabilizes a secondary binding site for presentation to IL-2Rbeta.
16293754	6	15	theme	complex	882:888	arg1	structure					890:898	This complex structure	877:898	This complex structure	877:898	This complex structure provides a framework for other gammac-dependent cytokine-receptor interactions and for the engineering of improved IL-2 therapeutics.
16293754	0	16	theme	interleukin-2	39:51	arg1	complex					28:34	the quaternary complex	13:34	the quaternary complex of interleukin-2	13:51	Structure of the quaternary complex of interleukin-2 with its alpha, beta, and gammac receptors.
16293754	5	17	theme	loss-of-function	766:781	arg1	mutations					783:791	loss-of-function mutations	766:791	loss-of-function mutations found in patients with X-linked severe combined immunodeficiency diseases (X-SCID)	766:874	The structure of gammac provides a rationale for loss-of-function mutations found in patients with X-linked severe combined immunodeficiency diseases (X-SCID).
16293754	0	18	theme	quaternary	17:26	arg1	complex					28:34	the quaternary complex	13:34	the quaternary complex of interleukin-2	13:51	Structure of the quaternary complex of interleukin-2 with its alpha, beta, and gammac receptors.
16293754	4	19	theme	shared	617:622	arg1	receptor					624:631	a shared receptor	615:631	a shared receptor for IL-4, IL-7, IL-9, IL-15, and IL-21	615:670	Consistent with its role as a shared receptor for IL-4, IL-7, IL-9, IL-15, and IL-21, gammac forms degenerate contacts with IL-2.
16293754	1	20	theme	quaternary	170:179	arg1	complex					200:206	a quaternary receptor signaling complex	168:206	a quaternary receptor signaling complex containing alpha (IL-2Ralpha), beta (IL-2Rbeta), and common gamma chain (gc) receptors	168:293	Interleukin-2 (IL-2) is an immunoregulatory cytokine that acts through a quaternary receptor signaling complex containing alpha (IL-2Ralpha), beta (IL-2Rbeta), and common gamma chain (gc) receptors.
16293754	5	21	theme	gammac	734:739	arg1	structure					721:729	The structure	717:729	The structure of gammac	717:739	The structure of gammac provides a rationale for loss-of-function mutations found in patients with X-linked severe combined immunodeficiency diseases (X-SCID).
16293754	1	22	theme	receptor	181:188	arg1	complex					200:206	a quaternary receptor signaling complex	168:206	a quaternary receptor signaling complex containing alpha (IL-2Ralpha), beta (IL-2Rbeta), and common gamma chain (gc) receptors	168:293	Interleukin-2 (IL-2) is an immunoregulatory cytokine that acts through a quaternary receptor signaling complex containing alpha (IL-2Ralpha), beta (IL-2Rbeta), and common gamma chain (gc) receptors.
16293754	0	23	theme	complex	28:34	arg1	Structure					0:8	Structure	0:8	Structure of the quaternary complex of interleukin-2 with its alpha, beta, and gammac receptors.	0:95	Structure of the quaternary complex of interleukin-2 with its alpha, beta, and gammac receptors.
16293754	1	24	theme	signaling	190:198	arg1	complex					200:206	a quaternary receptor signaling complex	168:206	a quaternary receptor signaling complex containing alpha (IL-2Ralpha), beta (IL-2Rbeta), and common gamma chain (gc) receptors	168:293	Interleukin-2 (IL-2) is an immunoregulatory cytokine that acts through a quaternary receptor signaling complex containing alpha (IL-2Ralpha), beta (IL-2Rbeta), and common gamma chain (gc) receptors.
16293754	1	25	theme	common	261:266	arg1	gc					281:282	gc	281:282	gc	281:282	Interleukin-2 (IL-2) is an immunoregulatory cytokine that acts through a quaternary receptor signaling complex containing alpha (IL-2Ralpha), beta (IL-2Rbeta), and common gamma chain (gc) receptors.
16293754	1	25	theme	common	261:266	arg1	chain					274:278	common gamma chain	261:278	common gamma chain (gc) receptors	261:293	Interleukin-2 (IL-2) is an immunoregulatory cytokine that acts through a quaternary receptor signaling complex containing alpha (IL-2Ralpha), beta (IL-2Rbeta), and common gamma chain (gc) receptors.
16293754	3	26	theme	IL-2/IL-2Rbeta	563:576	arg1	complex					578:584	the IL-2/IL-2Rbeta complex	559:584	the IL-2/IL-2Rbeta complex	559:584	gammac is then recruited to the composite surface formed by the IL-2/IL-2Rbeta complex.
16293754	1	27	contain	containing	208:217	arg1	complex					200:206	a quaternary receptor signaling complex	168:206	a quaternary receptor signaling complex containing alpha (IL-2Ralpha), beta (IL-2Rbeta), and common gamma chain (gc) receptors	168:293	Interleukin-2 (IL-2) is an immunoregulatory cytokine that acts through a quaternary receptor signaling complex containing alpha (IL-2Ralpha), beta (IL-2Rbeta), and common gamma chain (gc) receptors.
16293754	1	27	contain	containing	208:217	arg2	IL-2Ralpha					226:235	IL-2Ralpha	226:235	IL-2Ralpha	226:235	Interleukin-2 (IL-2) is an immunoregulatory cytokine that acts through a quaternary receptor signaling complex containing alpha (IL-2Ralpha), beta (IL-2Rbeta), and common gamma chain (gc) receptors.
16293754	1	27	contain	containing	208:217	arg2	beta					239:242	beta	239:242	beta (IL-2Rbeta)	239:254	Interleukin-2 (IL-2) is an immunoregulatory cytokine that acts through a quaternary receptor signaling complex containing alpha (IL-2Ralpha), beta (IL-2Rbeta), and common gamma chain (gc) receptors.
16293754	1	27	contain	containing	208:217	arg2	receptors					285:293	common gamma chain (gc) receptors	261:293	common gamma chain (gc) receptors	261:293	Interleukin-2 (IL-2) is an immunoregulatory cytokine that acts through a quaternary receptor signaling complex containing alpha (IL-2Ralpha), beta (IL-2Rbeta), and common gamma chain (gc) receptors.
16293754	1	27	contain	containing	208:217	arg2	IL-2Rbeta					245:253	IL-2Rbeta	245:253	IL-2Rbeta	245:253	Interleukin-2 (IL-2) is an immunoregulatory cytokine that acts through a quaternary receptor signaling complex containing alpha (IL-2Ralpha), beta (IL-2Rbeta), and common gamma chain (gc) receptors.
16293754	1	27	contain	containing	208:217	arg2	alpha					219:223	alpha	219:223	alpha (IL-2Ralpha)	219:236	Interleukin-2 (IL-2) is an immunoregulatory cytokine that acts through a quaternary receptor signaling complex containing alpha (IL-2Ralpha), beta (IL-2Rbeta), and common gamma chain (gc) receptors.
16293754	2	28	theme	angstroms	387:395	arg1	resolution					369:378	a resolution	367:378	a resolution of 2.3 angstroms	367:395	In the structure of the quaternary ectodomain complex as visualized at a resolution of 2.3 angstroms, the binding of IL-2Ralpha to IL-2 stabilizes a secondary binding site for presentation to IL-2Rbeta.
16293754	1	29	theme	gamma	268:272	arg1	gc					281:282	gc	281:282	gc	281:282	Interleukin-2 (IL-2) is an immunoregulatory cytokine that acts through a quaternary receptor signaling complex containing alpha (IL-2Ralpha), beta (IL-2Rbeta), and common gamma chain (gc) receptors.
16293754	1	29	theme	gamma	268:272	arg1	chain					274:278	common gamma chain	261:278	common gamma chain (gc) receptors	261:293	Interleukin-2 (IL-2) is an immunoregulatory cytokine that acts through a quaternary receptor signaling complex containing alpha (IL-2Ralpha), beta (IL-2Rbeta), and common gamma chain (gc) receptors.
16293754	5	30	theme	X-linked	816:823	arg1	immunodeficiency					841:856	X-linked severe combined immunodeficiency diseases	816:865	X-linked severe combined immunodeficiency diseases (X-SCID)	816:874	The structure of gammac provides a rationale for loss-of-function mutations found in patients with X-linked severe combined immunodeficiency diseases (X-SCID).
16293754	5	30	theme	X-linked	816:823	arg1	X-SCID					868:873	X-SCID	868:873	X-SCID	868:873	The structure of gammac provides a rationale for loss-of-function mutations found in patients with X-linked severe combined immunodeficiency diseases (X-SCID).
16293754	1	31	theme	chain	274:278	arg1	receptors					285:293	common gamma chain (gc) receptors	261:293	common gamma chain (gc) receptors	261:293	Interleukin-2 (IL-2) is an immunoregulatory cytokine that acts through a quaternary receptor signaling complex containing alpha (IL-2Ralpha), beta (IL-2Rbeta), and common gamma chain (gc) receptors.
16293754	0	32	with	Structure	0:8	arg1	receptors					86:94	its alpha, beta, and gammac receptors	58:94	its alpha, beta, and gammac receptors	58:94	Structure of the quaternary complex of interleukin-2 with its alpha, beta, and gammac receptors.
16293754	5	33	theme	severe	825:830	arg1	immunodeficiency					841:856	X-linked severe combined immunodeficiency diseases	816:865	X-linked severe combined immunodeficiency diseases (X-SCID)	816:874	The structure of gammac provides a rationale for loss-of-function mutations found in patients with X-linked severe combined immunodeficiency diseases (X-SCID).
16293754	5	33	theme	severe	825:830	arg1	X-SCID					868:873	X-SCID	868:873	X-SCID	868:873	The structure of gammac provides a rationale for loss-of-function mutations found in patients with X-linked severe combined immunodeficiency diseases (X-SCID).
16293754	6	34	theme	cytokine-receptor	948:964	arg1	interactions					966:977	other gammac-dependent cytokine-receptor interactions	925:977	other gammac-dependent cytokine-receptor interactions	925:977	This complex structure provides a framework for other gammac-dependent cytokine-receptor interactions and for the engineering of improved IL-2 therapeutics.
16293754	5	35	link	X-linked	816:823	arg1	immunodeficiency					841:856	X-linked severe combined immunodeficiency diseases	816:865	X-linked severe combined immunodeficiency diseases (X-SCID)	816:874	The structure of gammac provides a rationale for loss-of-function mutations found in patients with X-linked severe combined immunodeficiency diseases (X-SCID).
16293754	5	35	link	X-linked	816:823	arg1	X-SCID					868:873	X-SCID	868:873	X-SCID	868:873	The structure of gammac provides a rationale for loss-of-function mutations found in patients with X-linked severe combined immunodeficiency diseases (X-SCID).
16293754	4	36	with	Consistent	587:596	arg1	role					607:610	its role	603:610	its role as a shared receptor for IL-4, IL-7, IL-9, IL-15, and IL-21	603:670	Consistent with its role as a shared receptor for IL-4, IL-7, IL-9, IL-15, and IL-21, gammac forms degenerate contacts with IL-2.
16293754	5	37	theme	combined	832:839	arg1	immunodeficiency					841:856	X-linked severe combined immunodeficiency diseases	816:865	X-linked severe combined immunodeficiency diseases (X-SCID)	816:874	The structure of gammac provides a rationale for loss-of-function mutations found in patients with X-linked severe combined immunodeficiency diseases (X-SCID).
16293754	5	37	theme	combined	832:839	arg1	X-SCID					868:873	X-SCID	868:873	X-SCID	868:873	The structure of gammac provides a rationale for loss-of-function mutations found in patients with X-linked severe combined immunodeficiency diseases (X-SCID).
16293754	6	38	theme	gammac-dependent	931:946	arg1	interactions					966:977	other gammac-dependent cytokine-receptor interactions	925:977	other gammac-dependent cytokine-receptor interactions	925:977	This complex structure provides a framework for other gammac-dependent cytokine-receptor interactions and for the engineering of improved IL-2 therapeutics.
16293754	0	39	theme	alpha	62:66	arg1	receptors					86:94	its alpha, beta, and gammac receptors	58:94	its alpha, beta, and gammac receptors	58:94	Structure of the quaternary complex of interleukin-2 with its alpha, beta, and gammac receptors.
16293754	2	40	theme	complex	342:348	arg1	structure					303:311	the structure	299:311	the structure of the quaternary ectodomain complex as visualized at a resolution of 2.3 angstroms	299:395	In the structure of the quaternary ectodomain complex as visualized at a resolution of 2.3 angstroms, the binding of IL-2Ralpha to IL-2 stabilizes a secondary binding site for presentation to IL-2Rbeta.
16293754	3	41	theme	composite	531:539	arg1	surface					541:547	the composite surface	527:547	the composite surface formed by the IL-2/IL-2Rbeta complex	527:584	gammac is then recruited to the composite surface formed by the IL-2/IL-2Rbeta complex.
16293754	6	42	theme	improved	1006:1013	arg1	therapeutics					1020:1031	improved IL-2 therapeutics	1006:1031	improved IL-2 therapeutics	1006:1031	This complex structure provides a framework for other gammac-dependent cytokine-receptor interactions and for the engineering of improved IL-2 therapeutics.
16293754	6	43	theme	other	925:929	arg1	interactions					966:977	other gammac-dependent cytokine-receptor interactions	925:977	other gammac-dependent cytokine-receptor interactions	925:977	This complex structure provides a framework for other gammac-dependent cytokine-receptor interactions and for the engineering of improved IL-2 therapeutics.
16293754	4	44	theme	degenerate	686:695	arg1	contacts					697:704	degenerate contacts	686:704	degenerate contacts with IL-2	686:714	Consistent with its role as a shared receptor for IL-4, IL-7, IL-9, IL-15, and IL-21, gammac forms degenerate contacts with IL-2.
12034704	0	0	theme	bound	66:70	arg1	phospholipid					72:83	a bound phospholipid	64:83	a bound phospholipid	64:83	The crystal structure of the endothelial protein C receptor and a bound phospholipid.
12034704	2	1	theme	protein	493:499	arg1	C					501:501	protein C/activated protein C	473:501	protein C/activated protein C binding to the receptor	473:525	Blocking protein C/activated protein C binding to the receptor inhibits not only protein C activation but the ability of the host to respond appropriately to bacterial challenge, exacerbating both the coagulant and inflammatory responses.
12034704	7	2	theme	lipid	1215:1219	arg1	reconstitution					1221:1234	lipid reconstitution	1215:1234	lipid reconstitution	1215:1234	Extraction of the lipid resulted in loss of protein C binding, which could be restored by lipid reconstitution.
12034704	9	3	theme	potential	1394:1402	arg1	functions					1404:1412	additional potential functions	1383:1412	additional potential functions	1383:1412	The EPCR structure is a model for how CD1d binds lipids and further suggests additional potential functions for EPCR in immune regulation, possibly including the anti-phospholipid syndrome.
12034704	2	4	theme	C/activated	481:491	arg1	C					501:501	protein C/activated protein C	473:501	protein C/activated protein C binding to the receptor	473:525	Blocking protein C/activated protein C binding to the receptor inhibits not only protein C activation but the ability of the host to respond appropriately to bacterial challenge, exacerbating both the coagulant and inflammatory responses.
12034704	1	5	theme	natural	338:344	arg1	anticoagulant					346:358	a natural anticoagulant	336:358	a natural anticoagulant	336:358	The endothelial cell protein C receptor (EPCR) shares approximately 20% sequence identity with the major histocompatibility complex class 1/CD1 family of molecules, accelerates the thrombin-thrombomodulin-dependent generation of activated protein C, a natural anticoagulant, binds to activated neutrophils, and can undergo translocation from the plasma membrane to the nucleus.
12034704	1	5	theme	natural	338:344	arg1	C					333:333	activated protein C	315:333	activated protein C	315:333	The endothelial cell protein C receptor (EPCR) shares approximately 20% sequence identity with the major histocompatibility complex class 1/CD1 family of molecules, accelerates the thrombin-thrombomodulin-dependent generation of activated protein C, a natural anticoagulant, binds to activated neutrophils, and can undergo translocation from the plasma membrane to the nucleus.
12034704	2	6	theme	host	589:592	arg1	ability					574:580	the ability	570:580	the ability of the host to respond appropriately to bacterial challenge	570:640	Blocking protein C/activated protein C binding to the receptor inhibits not only protein C activation but the ability of the host to respond appropriately to bacterial challenge, exacerbating both the coagulant and inflammatory responses.
12034704	1	7	theme	plasma	432:437	arg1	membrane					439:446	the plasma membrane	428:446	the plasma membrane	428:446	The endothelial cell protein C receptor (EPCR) shares approximately 20% sequence identity with the major histocompatibility complex class 1/CD1 family of molecules, accelerates the thrombin-thrombomodulin-dependent generation of activated protein C, a natural anticoagulant, binds to activated neutrophils, and can undergo translocation from the plasma membrane to the nucleus.
12034704	1	8	from	membrane	439:446	arg1	translocation					409:421	translocation	409:421	translocation from the plasma membrane to the nucleus	409:461	The endothelial cell protein C receptor (EPCR) shares approximately 20% sequence identity with the major histocompatibility complex class 1/CD1 family of molecules, accelerates the thrombin-thrombomodulin-dependent generation of activated protein C, a natural anticoagulant, binds to activated neutrophils, and can undergo translocation from the plasma membrane to the nucleus.
12034704	3	9	theme	protein	862:868	arg1	C					870:870	protein C	862:870	protein C	862:870	To understand how EPCR accomplishes these multiple tasks, we solved the crystal structure of EPCR alone and in complex with the phospholipid binding domain of protein C.
12034704	3	10	theme	C	870:870	arg1	domain					852:857	the phospholipid binding domain	827:857	the phospholipid binding domain of protein C	827:870	To understand how EPCR accomplishes these multiple tasks, we solved the crystal structure of EPCR alone and in complex with the phospholipid binding domain of protein C.
12034704	3	10	theme	C	870:870	arg1	C					870:870	protein C	862:870	protein C	862:870	To understand how EPCR accomplishes these multiple tasks, we solved the crystal structure of EPCR alone and in complex with the phospholipid binding domain of protein C.
12034704	1	11	theme	molecules	240:248	arg1	family					230:235	the major histocompatibility complex class 1/CD1 family	181:235	the major histocompatibility complex class 1/CD1 family of molecules	181:248	The endothelial cell protein C receptor (EPCR) shares approximately 20% sequence identity with the major histocompatibility complex class 1/CD1 family of molecules, accelerates the thrombin-thrombomodulin-dependent generation of activated protein C, a natural anticoagulant, binds to activated neutrophils, and can undergo translocation from the plasma membrane to the nucleus.
12034704	0	12	theme	phospholipid	72:83	arg1	structure					12:20	The crystal structure	0:20	The crystal structure of the endothelial protein C receptor and a bound phospholipid.	0:84	The crystal structure of the endothelial protein C receptor and a bound phospholipid.
12034704	7	13	theme	lipid	1143:1147	arg1	Extraction					1125:1134	Extraction	1125:1134	Extraction of the lipid	1125:1147	Extraction of the lipid resulted in loss of protein C binding, which could be restored by lipid reconstitution.
12034704	8	14	theme	glycolipid	1285:1294	arg1	antigens					1296:1303	glycolipid antigens	1285:1303	glycolipid antigens	1285:1303	CD1d augments the immune response by presenting glycolipid antigens.
12034704	7	15	theme	C	1177:1177	arg1	binding					1179:1185	protein C binding	1169:1185	protein C binding	1169:1185	Extraction of the lipid resulted in loss of protein C binding, which could be restored by lipid reconstitution.
12034704	2	16	theme	bacterial	622:630	arg1	challenge					632:640	bacterial challenge	622:640	bacterial challenge	622:640	Blocking protein C/activated protein C binding to the receptor inhibits not only protein C activation but the ability of the host to respond appropriately to bacterial challenge, exacerbating both the coagulant and inflammatory responses.
12034704	9	17	dep	syndrome	1486:1493	arg1	including					1454:1462	including	1454:1462	including	1454:1462	The EPCR structure is a model for how CD1d binds lipids and further suggests additional potential functions for EPCR in immune regulation, possibly including the anti-phospholipid syndrome.
12034704	6	18	theme	conserved	1059:1067	arg1	groove					1069:1074	this conserved groove	1054:1074	this conserved groove	1054:1074	The protein C binding site is outside this conserved groove and is distal from the membrane-spanning domain.
12034704	7	19	theme	binding	1179:1185	arg1	loss					1161:1164	loss	1161:1164	loss	1161:1164	Extraction of the lipid resulted in loss of protein C binding, which could be restored by lipid reconstitution.
12034704	9	20	theme	EPCR	1310:1313	arg1	model					1330:1334	a model	1328:1334	a model for how CD1d binds lipids and further suggests additional potential functions for EPCR in immune regulation, possibly including the anti-phospholipid syndrome	1328:1493	The EPCR structure is a model for how CD1d binds lipids and further suggests additional potential functions for EPCR in immune regulation, possibly including the anti-phospholipid syndrome.
12034704	9	20	theme	EPCR	1310:1313	arg1	structure					1315:1323	The EPCR structure	1306:1323	The EPCR structure	1306:1323	The EPCR structure is a model for how CD1d binds lipids and further suggests additional potential functions for EPCR in immune regulation, possibly including the anti-phospholipid syndrome.
12034704	2	21	theme	protein	473:479	arg1	C					501:501	protein C/activated protein C	473:501	protein C/activated protein C binding to the receptor	473:525	Blocking protein C/activated protein C binding to the receptor inhibits not only protein C activation but the ability of the host to respond appropriately to bacterial challenge, exacerbating both the coagulant and inflammatory responses.
12034704	2	22	theme	inflammatory	679:690	arg1	responses					692:700	both the coagulant and inflammatory responses	656:700	responses	692:700	Blocking protein C/activated protein C binding to the receptor inhibits not only protein C activation but the ability of the host to respond appropriately to bacterial challenge, exacerbating both the coagulant and inflammatory responses.
12034704	6	23	theme	protein	1020:1026	arg1	site					1038:1041	The protein C binding site	1016:1041	The protein C binding site	1016:1041	The protein C binding site is outside this conserved groove and is distal from the membrane-spanning domain.
12034704	6	23	theme	protein	1020:1026	arg1	distal					1083:1088	distal	1083:1088	distal	1083:1088	The protein C binding site is outside this conserved groove and is distal from the membrane-spanning domain.
12034704	8	24	theme	immune	1255:1260	arg1	response					1262:1269	the immune response	1251:1269	the immune response	1251:1269	CD1d augments the immune response by presenting glycolipid antigens.
12034704	9	25	theme	immune	1426:1431	arg1	regulation					1433:1442	immune regulation	1426:1442	immune regulation	1426:1442	The EPCR structure is a model for how CD1d binds lipids and further suggests additional potential functions for EPCR in immune regulation, possibly including the anti-phospholipid syndrome.
12034704	0	26	theme	crystal	4:10	arg1	structure					12:20	The crystal structure	0:20	The crystal structure of the endothelial protein C receptor and a bound phospholipid.	0:84	The crystal structure of the endothelial protein C receptor and a bound phospholipid.
12034704	1	27	theme	activated	370:378	arg1	neutrophils					380:390	activated neutrophils	370:390	activated neutrophils	370:390	The endothelial cell protein C receptor (EPCR) shares approximately 20% sequence identity with the major histocompatibility complex class 1/CD1 family of molecules, accelerates the thrombin-thrombomodulin-dependent generation of activated protein C, a natural anticoagulant, binds to activated neutrophils, and can undergo translocation from the plasma membrane to the nucleus.
12034704	3	28	theme	multiple	745:752	arg1	tasks					754:758	these multiple tasks	739:758	these multiple tasks	739:758	To understand how EPCR accomplishes these multiple tasks, we solved the crystal structure of EPCR alone and in complex with the phospholipid binding domain of protein C.
12034704	1	29	theme	%	156:156	arg1	identity					167:174	approximately 20% sequence identity	140:174	approximately 20% sequence identity with the major histocompatibility complex class 1/CD1 family of molecules	140:248	The endothelial cell protein C receptor (EPCR) shares approximately 20% sequence identity with the major histocompatibility complex class 1/CD1 family of molecules, accelerates the thrombin-thrombomodulin-dependent generation of activated protein C, a natural anticoagulant, binds to activated neutrophils, and can undergo translocation from the plasma membrane to the nucleus.
12034704	7	30	theme	protein	1169:1175	arg1	binding					1179:1185	protein C binding	1169:1185	protein C binding	1169:1185	Extraction of the lipid resulted in loss of protein C binding, which could be restored by lipid reconstitution.
12034704	2	31	theme	coagulant	665:673	arg1	responses					692:700	both the coagulant and inflammatory responses	656:700	responses	692:700	Blocking protein C/activated protein C binding to the receptor inhibits not only protein C activation but the ability of the host to respond appropriately to bacterial challenge, exacerbating both the coagulant and inflammatory responses.
12034704	5	32	theme	bound	931:935	arg1	phospholipid					937:948	A tightly bound phospholipid	921:948	A tightly bound phospholipid	921:948	A tightly bound phospholipid resides in the groove typically involved in antigen presentation.
12034704	1	33	theme	sequence	158:165	arg1	identity					167:174	approximately 20% sequence identity	140:174	approximately 20% sequence identity with the major histocompatibility complex class 1/CD1 family of molecules	140:248	The endothelial cell protein C receptor (EPCR) shares approximately 20% sequence identity with the major histocompatibility complex class 1/CD1 family of molecules, accelerates the thrombin-thrombomodulin-dependent generation of activated protein C, a natural anticoagulant, binds to activated neutrophils, and can undergo translocation from the plasma membrane to the nucleus.
12034704	2	34	theme	C	553:553	arg1	activation					555:564	protein C activation	545:564	protein C activation	545:564	Blocking protein C/activated protein C binding to the receptor inhibits not only protein C activation but the ability of the host to respond appropriately to bacterial challenge, exacerbating both the coagulant and inflammatory responses.
12034704	2	35	dep	responses	692:700	arg1	both					656:659	both	656:659	both	656:659	Blocking protein C/activated protein C binding to the receptor inhibits not only protein C activation but the ability of the host to respond appropriately to bacterial challenge, exacerbating both the coagulant and inflammatory responses.
12034704	1	36	theme	thrombin-thrombomodulin-dependent	267:299	arg1	generation					301:310	the thrombin-thrombomodulin-dependent generation	263:310	the thrombin-thrombomodulin-dependent generation of activated protein C, a natural anticoagulant	263:358	The endothelial cell protein C receptor (EPCR) shares approximately 20% sequence identity with the major histocompatibility complex class 1/CD1 family of molecules, accelerates the thrombin-thrombomodulin-dependent generation of activated protein C, a natural anticoagulant, binds to activated neutrophils, and can undergo translocation from the plasma membrane to the nucleus.
12034704	2	37	theme	protein	545:551	arg1	C					553:553	protein C	545:553	protein C activation	545:564	Blocking protein C/activated protein C binding to the receptor inhibits not only protein C activation but the ability of the host to respond appropriately to bacterial challenge, exacerbating both the coagulant and inflammatory responses.
12034704	1	38	theme	endothelial	90:100	arg1	EPCR					127:130	EPCR	127:130	EPCR	127:130	The endothelial cell protein C receptor (EPCR) shares approximately 20% sequence identity with the major histocompatibility complex class 1/CD1 family of molecules, accelerates the thrombin-thrombomodulin-dependent generation of activated protein C, a natural anticoagulant, binds to activated neutrophils, and can undergo translocation from the plasma membrane to the nucleus.
12034704	1	38	theme	endothelial	90:100	arg1	receptor					117:124	The endothelial cell protein C receptor	86:124	The endothelial cell protein C receptor (EPCR)	86:131	The endothelial cell protein C receptor (EPCR) shares approximately 20% sequence identity with the major histocompatibility complex class 1/CD1 family of molecules, accelerates the thrombin-thrombomodulin-dependent generation of activated protein C, a natural anticoagulant, binds to activated neutrophils, and can undergo translocation from the plasma membrane to the nucleus.
12034704	0	39	theme	endothelial	29:39	arg1	receptor					51:58	the endothelial protein C receptor	25:58	the endothelial protein C receptor	25:58	The crystal structure of the endothelial protein C receptor and a bound phospholipid.
12034704	1	40	with	identity	167:174	arg1	family					230:235	the major histocompatibility complex class 1/CD1 family	181:235	the major histocompatibility complex class 1/CD1 family of molecules	181:248	The endothelial cell protein C receptor (EPCR) shares approximately 20% sequence identity with the major histocompatibility complex class 1/CD1 family of molecules, accelerates the thrombin-thrombomodulin-dependent generation of activated protein C, a natural anticoagulant, binds to activated neutrophils, and can undergo translocation from the plasma membrane to the nucleus.
12034704	9	41	from	EPCR	1418:1421	arg1	regulation					1433:1442	immune regulation	1426:1442	immune regulation	1426:1442	The EPCR structure is a model for how CD1d binds lipids and further suggests additional potential functions for EPCR in immune regulation, possibly including the anti-phospholipid syndrome.
12034704	3	42	theme	crystal	775:781	arg1	structure					783:791	the crystal structure	771:791	the crystal structure of EPCR alone and in complex with the phospholipid binding domain of protein C	771:870	To understand how EPCR accomplishes these multiple tasks, we solved the crystal structure of EPCR alone and in complex with the phospholipid binding domain of protein C.
12034704	6	43	from	domain	1117:1122	arg1	distal					1083:1088	distal	1083:1088	distal	1083:1088	The protein C binding site is outside this conserved groove and is distal from the membrane-spanning domain.
12034704	6	43	from	domain	1117:1122	arg1	site					1038:1041	The protein C binding site	1016:1041	The protein C binding site	1016:1041	The protein C binding site is outside this conserved groove and is distal from the membrane-spanning domain.
12034704	1	44	theme	major	185:189	arg1	class					218:222	the major histocompatibility complex class	181:222	the major histocompatibility complex class 1/CD1 family of molecules	181:248	The endothelial cell protein C receptor (EPCR) shares approximately 20% sequence identity with the major histocompatibility complex class 1/CD1 family of molecules, accelerates the thrombin-thrombomodulin-dependent generation of activated protein C, a natural anticoagulant, binds to activated neutrophils, and can undergo translocation from the plasma membrane to the nucleus.
12034704	0	45	theme	C	49:49	arg1	receptor					51:58	the endothelial protein C receptor	25:58	the endothelial protein C receptor	25:58	The crystal structure of the endothelial protein C receptor and a bound phospholipid.
12034704	1	46	theme	activated	315:323	arg1	anticoagulant					346:358	a natural anticoagulant	336:358	a natural anticoagulant	336:358	The endothelial cell protein C receptor (EPCR) shares approximately 20% sequence identity with the major histocompatibility complex class 1/CD1 family of molecules, accelerates the thrombin-thrombomodulin-dependent generation of activated protein C, a natural anticoagulant, binds to activated neutrophils, and can undergo translocation from the plasma membrane to the nucleus.
12034704	1	46	theme	activated	315:323	arg1	C					333:333	activated protein C	315:333	activated protein C	315:333	The endothelial cell protein C receptor (EPCR) shares approximately 20% sequence identity with the major histocompatibility complex class 1/CD1 family of molecules, accelerates the thrombin-thrombomodulin-dependent generation of activated protein C, a natural anticoagulant, binds to activated neutrophils, and can undergo translocation from the plasma membrane to the nucleus.
12034704	2	47	theme	C	501:501	arg1	binding					503:509	protein C/activated protein C binding	473:509	protein C/activated protein C binding to the receptor	473:525	Blocking protein C/activated protein C binding to the receptor inhibits not only protein C activation but the ability of the host to respond appropriately to bacterial challenge, exacerbating both the coagulant and inflammatory responses.
12034704	3	48	with	complex	814:820	arg1	domain					852:857	the phospholipid binding domain	827:857	the phospholipid binding domain of protein C	827:870	To understand how EPCR accomplishes these multiple tasks, we solved the crystal structure of EPCR alone and in complex with the phospholipid binding domain of protein C.
12034704	3	48	with	complex	814:820	arg1	C					870:870	protein C	862:870	protein C	862:870	To understand how EPCR accomplishes these multiple tasks, we solved the crystal structure of EPCR alone and in complex with the phospholipid binding domain of protein C.
12034704	1	49	theme	cell	102:105	arg1	EPCR					127:130	EPCR	127:130	EPCR	127:130	The endothelial cell protein C receptor (EPCR) shares approximately 20% sequence identity with the major histocompatibility complex class 1/CD1 family of molecules, accelerates the thrombin-thrombomodulin-dependent generation of activated protein C, a natural anticoagulant, binds to activated neutrophils, and can undergo translocation from the plasma membrane to the nucleus.
12034704	1	49	theme	cell	102:105	arg1	receptor					117:124	The endothelial cell protein C receptor	86:124	The endothelial cell protein C receptor (EPCR)	86:131	The endothelial cell protein C receptor (EPCR) shares approximately 20% sequence identity with the major histocompatibility complex class 1/CD1 family of molecules, accelerates the thrombin-thrombomodulin-dependent generation of activated protein C, a natural anticoagulant, binds to activated neutrophils, and can undergo translocation from the plasma membrane to the nucleus.
12034704	0	50	theme	protein	41:47	arg1	receptor					51:58	the endothelial protein C receptor	25:58	the endothelial protein C receptor	25:58	The crystal structure of the endothelial protein C receptor and a bound phospholipid.
12034704	1	51	theme	protein	325:331	arg1	anticoagulant					346:358	a natural anticoagulant	336:358	a natural anticoagulant	336:358	The endothelial cell protein C receptor (EPCR) shares approximately 20% sequence identity with the major histocompatibility complex class 1/CD1 family of molecules, accelerates the thrombin-thrombomodulin-dependent generation of activated protein C, a natural anticoagulant, binds to activated neutrophils, and can undergo translocation from the plasma membrane to the nucleus.
12034704	1	51	theme	protein	325:331	arg1	C					333:333	activated protein C	315:333	activated protein C	315:333	The endothelial cell protein C receptor (EPCR) shares approximately 20% sequence identity with the major histocompatibility complex class 1/CD1 family of molecules, accelerates the thrombin-thrombomodulin-dependent generation of activated protein C, a natural anticoagulant, binds to activated neutrophils, and can undergo translocation from the plasma membrane to the nucleus.
12034704	1	52	theme	protein	107:113	arg1	EPCR					127:130	EPCR	127:130	EPCR	127:130	The endothelial cell protein C receptor (EPCR) shares approximately 20% sequence identity with the major histocompatibility complex class 1/CD1 family of molecules, accelerates the thrombin-thrombomodulin-dependent generation of activated protein C, a natural anticoagulant, binds to activated neutrophils, and can undergo translocation from the plasma membrane to the nucleus.
12034704	1	52	theme	protein	107:113	arg1	receptor					117:124	The endothelial cell protein C receptor	86:124	The endothelial cell protein C receptor (EPCR)	86:131	The endothelial cell protein C receptor (EPCR) shares approximately 20% sequence identity with the major histocompatibility complex class 1/CD1 family of molecules, accelerates the thrombin-thrombomodulin-dependent generation of activated protein C, a natural anticoagulant, binds to activated neutrophils, and can undergo translocation from the plasma membrane to the nucleus.
12034704	1	53	theme	C	333:333	arg1	generation					301:310	the thrombin-thrombomodulin-dependent generation	263:310	the thrombin-thrombomodulin-dependent generation of activated protein C, a natural anticoagulant	263:358	The endothelial cell protein C receptor (EPCR) shares approximately 20% sequence identity with the major histocompatibility complex class 1/CD1 family of molecules, accelerates the thrombin-thrombomodulin-dependent generation of activated protein C, a natural anticoagulant, binds to activated neutrophils, and can undergo translocation from the plasma membrane to the nucleus.
12034704	1	54	theme	C	115:115	arg1	EPCR					127:130	EPCR	127:130	EPCR	127:130	The endothelial cell protein C receptor (EPCR) shares approximately 20% sequence identity with the major histocompatibility complex class 1/CD1 family of molecules, accelerates the thrombin-thrombomodulin-dependent generation of activated protein C, a natural anticoagulant, binds to activated neutrophils, and can undergo translocation from the plasma membrane to the nucleus.
12034704	1	54	theme	C	115:115	arg1	receptor					117:124	The endothelial cell protein C receptor	86:124	The endothelial cell protein C receptor (EPCR)	86:131	The endothelial cell protein C receptor (EPCR) shares approximately 20% sequence identity with the major histocompatibility complex class 1/CD1 family of molecules, accelerates the thrombin-thrombomodulin-dependent generation of activated protein C, a natural anticoagulant, binds to activated neutrophils, and can undergo translocation from the plasma membrane to the nucleus.
12034704	1	55	theme	histocompatibility	191:208	arg1	class					218:222	the major histocompatibility complex class	181:222	the major histocompatibility complex class 1/CD1 family of molecules	181:248	The endothelial cell protein C receptor (EPCR) shares approximately 20% sequence identity with the major histocompatibility complex class 1/CD1 family of molecules, accelerates the thrombin-thrombomodulin-dependent generation of activated protein C, a natural anticoagulant, binds to activated neutrophils, and can undergo translocation from the plasma membrane to the nucleus.
12034704	6	56	theme	membrane-spanning	1099:1115	arg1	domain					1117:1122	the membrane-spanning domain	1095:1122	the membrane-spanning domain	1095:1122	The protein C binding site is outside this conserved groove and is distal from the membrane-spanning domain.
12034704	3	57	theme	phospholipid	831:842	arg1	domain					852:857	the phospholipid binding domain	827:857	the phospholipid binding domain of protein C	827:870	To understand how EPCR accomplishes these multiple tasks, we solved the crystal structure of EPCR alone and in complex with the phospholipid binding domain of protein C.
12034704	3	57	theme	phospholipid	831:842	arg1	C					870:870	protein C	862:870	protein C	862:870	To understand how EPCR accomplishes these multiple tasks, we solved the crystal structure of EPCR alone and in complex with the phospholipid binding domain of protein C.
12034704	1	58	theme	complex	210:216	arg1	class					218:222	the major histocompatibility complex class	181:222	the major histocompatibility complex class 1/CD1 family of molecules	181:248	The endothelial cell protein C receptor (EPCR) shares approximately 20% sequence identity with the major histocompatibility complex class 1/CD1 family of molecules, accelerates the thrombin-thrombomodulin-dependent generation of activated protein C, a natural anticoagulant, binds to activated neutrophils, and can undergo translocation from the plasma membrane to the nucleus.
12034704	9	59	theme	anti-phospholipid	1468:1484	arg1	syndrome					1486:1493	the anti-phospholipid syndrome	1464:1493	the anti-phospholipid syndrome	1464:1493	The EPCR structure is a model for how CD1d binds lipids and further suggests additional potential functions for EPCR in immune regulation, possibly including the anti-phospholipid syndrome.
12034704	6	60	theme	binding	1030:1036	arg1	site					1038:1041	The protein C binding site	1016:1041	The protein C binding site	1016:1041	The protein C binding site is outside this conserved groove and is distal from the membrane-spanning domain.
12034704	6	60	theme	binding	1030:1036	arg1	distal					1083:1088	distal	1083:1088	distal	1083:1088	The protein C binding site is outside this conserved groove and is distal from the membrane-spanning domain.
12034704	5	61	theme	antigen	994:1000	arg1	presentation					1002:1013	antigen presentation	994:1013	antigen presentation	994:1013	A tightly bound phospholipid resides in the groove typically involved in antigen presentation.
12034704	3	62	theme	binding	844:850	arg1	domain					852:857	the phospholipid binding domain	827:857	the phospholipid binding domain of protein C	827:870	To understand how EPCR accomplishes these multiple tasks, we solved the crystal structure of EPCR alone and in complex with the phospholipid binding domain of protein C.
12034704	3	62	theme	binding	844:850	arg1	C					870:870	protein C	862:870	protein C	862:870	To understand how EPCR accomplishes these multiple tasks, we solved the crystal structure of EPCR alone and in complex with the phospholipid binding domain of protein C.
12034704	1	63	theme	class	218:222	arg1	family					230:235	the major histocompatibility complex class 1/CD1 family	181:235	the major histocompatibility complex class 1/CD1 family of molecules	181:248	The endothelial cell protein C receptor (EPCR) shares approximately 20% sequence identity with the major histocompatibility complex class 1/CD1 family of molecules, accelerates the thrombin-thrombomodulin-dependent generation of activated protein C, a natural anticoagulant, binds to activated neutrophils, and can undergo translocation from the plasma membrane to the nucleus.
12034704	0	64	theme	receptor	51:58	arg1	structure					12:20	The crystal structure	0:20	The crystal structure of the endothelial protein C receptor and a bound phospholipid.	0:84	The crystal structure of the endothelial protein C receptor and a bound phospholipid.
12034704	3	65	theme	EPCR	796:799	arg1	structure					783:791	the crystal structure	771:791	the crystal structure of EPCR alone and in complex with the phospholipid binding domain of protein C	771:870	To understand how EPCR accomplishes these multiple tasks, we solved the crystal structure of EPCR alone and in complex with the phospholipid binding domain of protein C.
12034704	6	66	theme	C	1028:1028	arg1	site					1038:1041	The protein C binding site	1016:1041	The protein C binding site	1016:1041	The protein C binding site is outside this conserved groove and is distal from the membrane-spanning domain.
12034704	6	66	theme	C	1028:1028	arg1	distal					1083:1088	distal	1083:1088	distal	1083:1088	The protein C binding site is outside this conserved groove and is distal from the membrane-spanning domain.
12034704	9	67	theme	additional	1383:1392	arg1	functions					1404:1412	additional potential functions	1383:1412	additional potential functions	1383:1412	The EPCR structure is a model for how CD1d binds lipids and further suggests additional potential functions for EPCR in immune regulation, possibly including the anti-phospholipid syndrome.
12034704	1	68	theme	1/CD1	224:228	arg1	family					230:235	the major histocompatibility complex class 1/CD1 family	181:235	the major histocompatibility complex class 1/CD1 family of molecules	181:248	The endothelial cell protein C receptor (EPCR) shares approximately 20% sequence identity with the major histocompatibility complex class 1/CD1 family of molecules, accelerates the thrombin-thrombomodulin-dependent generation of activated protein C, a natural anticoagulant, binds to activated neutrophils, and can undergo translocation from the plasma membrane to the nucleus.
10551839	0	0	theme	multiple	76:83	arg1	residues					96:103	multiple tryptophan residues	76:103	multiple tryptophan residues	76:103	The four terminal components of the complement system are C-mannosylated on multiple tryptophan residues.
10551839	2	1	from	C-mannosylated	387:400	arg1	examples					265:272	the two examples	257:272	the two examples found so far	257:285	In the two examples found so far, human RNase 2 and interleukin-12, only the first Trp in the recognition motif WXXW is specifically C-mannosylated.
10551839	2	1	from	C-mannosylated	387:400	arg1	RNase					294:298	human RNase 2	288:300	human RNase 2	288:300	In the two examples found so far, human RNase 2 and interleukin-12, only the first Trp in the recognition motif WXXW is specifically C-mannosylated.
10551839	2	1	from	C-mannosylated	387:400	arg1	interleukin-12					306:319	interleukin-12	306:319	interleukin-12	306:319	In the two examples found so far, human RNase 2 and interleukin-12, only the first Trp in the recognition motif WXXW is specifically C-mannosylated.
10551839	5	2	gly	C-mannosylated	760:773	arg1	six					816:818	six	816:818	six	816:818	These are the first proteins that are C-mannosylated on more than one Trp residue as follows: six in C6, four in C7, C8alpha, and C8beta, and two in C9.
10551839	5	2	gly	C-mannosylated	760:773	arg1	proteins					742:749	the first proteins	732:749	the first proteins that are C-mannosylated on more than one Trp residue as follows	732:813	These are the first proteins that are C-mannosylated on more than one Trp residue as follows: six in C6, four in C7, C8alpha, and C8beta, and two in C9.
10551839	5	2	gly	C-mannosylated	760:773	arg1	two					864:866	two	864:866	two	864:866	These are the first proteins that are C-mannosylated on more than one Trp residue as follows: six in C6, four in C7, C8alpha, and C8beta, and two in C9.
10551839	5	2	gly	C-mannosylated	760:773	arg1	These					722:726	These	722:726	These	722:726	These are the first proteins that are C-mannosylated on more than one Trp residue as follows: six in C6, four in C7, C8alpha, and C8beta, and two in C9.
10551839	5	2	gly	C-mannosylated	760:773	arg1	C-mannosylated					760:773	C-mannosylated	760:773	C-mannosylated	760:773	These are the first proteins that are C-mannosylated on more than one Trp residue as follows: six in C6, four in C7, C8alpha, and C8beta, and two in C9.
10551839	5	2	gly	C-mannosylated	760:773	arg1	four					827:830	four	827:830	four	827:830	These are the first proteins that are C-mannosylated on more than one Trp residue as follows: six in C6, four in C7, C8alpha, and C8beta, and two in C9.
10551839	1	3	theme	glycosylation	150:162	arg1	form					134:137	a unique form	125:137	a unique form of protein glycosylation	125:162	C-Mannosylation is a unique form of protein glycosylation, involving the C-glycosidic attachment of a mannosyl residue to the indole moiety of Trp.
10551839	1	3	theme	glycosylation	150:162	arg1	C-Mannosylation					106:120	C-Mannosylation	106:120	C-Mannosylation	106:120	C-Mannosylation is a unique form of protein glycosylation, involving the C-glycosidic attachment of a mannosyl residue to the indole moiety of Trp.
10551839	11	4	theme	proteins	1506:1513	arg1	number					1490:1495	a large number	1482:1495	a large number of other proteins	1482:1513	Since this module has been found in a large number of other proteins, the results suggest further candidates for C-mannosylation.
10551839	5	5	theme	Trp	792:794	arg1	residue					796:802	more than one Trp residue	778:802	more than one Trp residue	778:802	These are the first proteins that are C-mannosylated on more than one Trp residue as follows: six in C6, four in C7, C8alpha, and C8beta, and two in C9.
10551839	10	6	attach	present	1419:1425	arg1	proteins					1436:1443	these proteins	1430:1443	these proteins	1430:1443	Finally, all modified Trp residues are part of the highly conserved core of the thrombospondin type 1 repeats present in these proteins.
10551839	10	6	attach	present	1419:1425	arg2	repeats					1411:1417	the thrombospondin type 1 repeats	1385:1417	the thrombospondin type 1 repeats present in these proteins	1385:1443	Finally, all modified Trp residues are part of the highly conserved core of the thrombospondin type 1 repeats present in these proteins.
10551839	1	7	theme	Trp	249:251	arg1	moiety					239:244	the indole moiety	228:244	the indole moiety of Trp	228:251	C-Mannosylation is a unique form of protein glycosylation, involving the C-glycosidic attachment of a mannosyl residue to the indole moiety of Trp.
10551839	3	8	theme	complex	601:607	arg1	motifs					621:626	multiple and complex recognition motifs	588:626	multiple and complex recognition motifs	588:626	To establish the generality of protein C-mannosylation, and to learn more about its mechanism, the terminal components of the human complement system (C6, C7, C8,and C9), which contain multiple and complex recognition motifs, were examined.
10551839	7	9	from	C8	1037:1038	arg1	C-mannosylated					1138:1151	C-mannosylated	1138:1151	C-mannosylated	1138:1151	The other important finding is that in C6, C7, C8, and C9 Trp residues without a second Trp (or another aromatic residue) at the +3 position can be C-mannosylated.
10551839	0	10	theme	tryptophan	85:94	arg1	residues					96:103	multiple tryptophan residues	76:103	multiple tryptophan residues	76:103	The four terminal components of the complement system are C-mannosylated on multiple tryptophan residues.
10551839	3	11	theme	terminal	502:509	arg1	components					511:520	the terminal components	498:520	the terminal components	498:520	To establish the generality of protein C-mannosylation, and to learn more about its mechanism, the terminal components of the human complement system (C6, C7, C8,and C9), which contain multiple and complex recognition motifs, were examined.
10551839	6	12	from	residues	898:905	arg1	complex					939:945	the complete membrane attack complex	910:945	the complete membrane attack complex	910:945	Thus, from the 113 Trp residues in the complete membrane attack complex, 50 were found to undergo C-mannosylation.
10551839	0	13	gly	C-mannosylated	58:71	arg1	components					18:27	The four terminal components	0:27	The four terminal components of the complement system	0:52	The four terminal components of the complement system are C-mannosylated on multiple tryptophan residues.
10551839	0	13	gly	C-mannosylated	58:71	arg1	C-mannosylated					58:71	C-mannosylated	58:71	C-mannosylated	58:71	The four terminal components of the complement system are C-mannosylated on multiple tryptophan residues.
10551839	11	14	located	found	1473:1477	arg1	number					1490:1495	a large number	1482:1495	a large number of other proteins	1482:1513	Since this module has been found in a large number of other proteins, the results suggest further candidates for C-mannosylation.
10551839	11	14	located	found	1473:1477	arg2	module					1457:1462	this module	1452:1462	this module	1452:1462	Since this module has been found in a large number of other proteins, the results suggest further candidates for C-mannosylation.
10551839	7	15	theme	Trp	1048:1050	arg1	residues					1052:1059	Trp residues	1048:1059	Trp residues without a second Trp (or another aromatic residue) at the +3 position	1048:1129	The other important finding is that in C6, C7, C8, and C9 Trp residues without a second Trp (or another aromatic residue) at the +3 position can be C-mannosylated.
10551839	7	16	theme	important	1000:1008	arg1	finding					1010:1016	The other important finding	990:1016	The other important finding	990:1016	The other important finding is that in C6, C7, C8, and C9 Trp residues without a second Trp (or another aromatic residue) at the +3 position can be C-mannosylated.
10551839	5	17	theme	first	736:740	arg1	six					816:818	six	816:818	six	816:818	These are the first proteins that are C-mannosylated on more than one Trp residue as follows: six in C6, four in C7, C8alpha, and C8beta, and two in C9.
10551839	5	17	theme	first	736:740	arg1	proteins					742:749	the first proteins	732:749	the first proteins that are C-mannosylated on more than one Trp residue as follows	732:813	These are the first proteins that are C-mannosylated on more than one Trp residue as follows: six in C6, four in C7, C8alpha, and C8beta, and two in C9.
10551839	5	17	theme	first	736:740	arg1	two					864:866	two	864:866	two	864:866	These are the first proteins that are C-mannosylated on more than one Trp residue as follows: six in C6, four in C7, C8alpha, and C8beta, and two in C9.
10551839	5	17	theme	first	736:740	arg1	These					722:726	These	722:726	These	722:726	These are the first proteins that are C-mannosylated on more than one Trp residue as follows: six in C6, four in C7, C8alpha, and C8beta, and two in C9.
10551839	5	17	theme	first	736:740	arg1	C-mannosylated					760:773	C-mannosylated	760:773	C-mannosylated	760:773	These are the first proteins that are C-mannosylated on more than one Trp residue as follows: six in C6, four in C7, C8alpha, and C8beta, and two in C9.
10551839	5	17	theme	first	736:740	arg1	four					827:830	four	827:830	four	827:830	These are the first proteins that are C-mannosylated on more than one Trp residue as follows: six in C6, four in C7, C8alpha, and C8beta, and two in C9.
10551839	10	18	theme	type	1404:1407	arg1	repeats					1411:1417	the thrombospondin type 1 repeats	1385:1417	the thrombospondin type 1 repeats present in these proteins	1385:1443	Finally, all modified Trp residues are part of the highly conserved core of the thrombospondin type 1 repeats present in these proteins.
10551839	2	19	theme	recognition	348:358	arg1	WXXW					366:369	the recognition motif WXXW	344:369	the recognition motif WXXW	344:369	In the two examples found so far, human RNase 2 and interleukin-12, only the first Trp in the recognition motif WXXW is specifically C-mannosylated.
10551839	11	20	theme	other	1500:1504	arg1	proteins					1506:1513	other proteins	1500:1513	other proteins	1500:1513	Since this module has been found in a large number of other proteins, the results suggest further candidates for C-mannosylation.
10551839	6	21	theme	complete	914:921	arg1	complex					939:945	the complete membrane attack complex	910:945	the complete membrane attack complex	910:945	Thus, from the 113 Trp residues in the complete membrane attack complex, 50 were found to undergo C-mannosylation.
10551839	7	22	gly	C-mannosylated	1138:1151	arg1	residues					1052:1059	Trp residues	1048:1059	Trp residues without a second Trp (or another aromatic residue) at the +3 position	1048:1129	The other important finding is that in C6, C7, C8, and C9 Trp residues without a second Trp (or another aromatic residue) at the +3 position can be C-mannosylated.
10551839	7	23	from	C9	1045:1046	arg1	C-mannosylated					1138:1151	C-mannosylated	1138:1151	C-mannosylated	1138:1151	The other important finding is that in C6, C7, C8, and C9 Trp residues without a second Trp (or another aromatic residue) at the +3 position can be C-mannosylated.
10551839	4	24	theme	cytolytic	676:684	arg1	complex					713:719	the membrane attack complex	693:719	the membrane attack complex	693:719	Together with C5b they form the cytolytic agent, the membrane attack complex.
10551839	4	24	theme	cytolytic	676:684	arg1	agent					686:690	the cytolytic agent	672:690	the cytolytic agent	672:690	Together with C5b they form the cytolytic agent, the membrane attack complex.
10551839	3	25	dep	system	546:551	arg1	C9					569:570	C9	569:570	C9	569:570	To establish the generality of protein C-mannosylation, and to learn more about its mechanism, the terminal components of the human complement system (C6, C7, C8,and C9), which contain multiple and complex recognition motifs, were examined.
10551839	3	25	dep	system	546:551	arg1	C7					558:559	C7	558:559	C7	558:559	To establish the generality of protein C-mannosylation, and to learn more about its mechanism, the terminal components of the human complement system (C6, C7, C8,and C9), which contain multiple and complex recognition motifs, were examined.
10551839	3	25	dep	system	546:551	arg1	C6					554:555	C6	554:555	C6	554:555	To establish the generality of protein C-mannosylation, and to learn more about its mechanism, the terminal components of the human complement system (C6, C7, C8,and C9), which contain multiple and complex recognition motifs, were examined.
10551839	3	25	dep	system	546:551	arg1	C8					562:563	C8	562:563	C8	562:563	To establish the generality of protein C-mannosylation, and to learn more about its mechanism, the terminal components of the human complement system (C6, C7, C8,and C9), which contain multiple and complex recognition motifs, were examined.
10551839	8	26	contain	contain	1180:1186	arg1	they					1170:1173	they	1170:1173	they	1170:1173	This shows that they must contain an additional C-mannosylation signal.
10551839	8	26	contain	contain	1180:1186	arg2	signal					1218:1223	an additional C-mannosylation signal	1188:1223	an additional C-mannosylation signal	1188:1223	This shows that they must contain an additional C-mannosylation signal.
10551839	10	27	theme	Trp	1331:1333	arg1	part					1348:1351	part	1348:1351	part of the highly conserved core of the thrombospondin type 1 repeats present in these proteins	1348:1443	Finally, all modified Trp residues are part of the highly conserved core of the thrombospondin type 1 repeats present in these proteins.
10551839	10	27	theme	Trp	1331:1333	arg1	residues					1335:1342	all modified Trp residues	1318:1342	all modified Trp residues	1318:1342	Finally, all modified Trp residues are part of the highly conserved core of the thrombospondin type 1 repeats present in these proteins.
10551839	5	28	from	six	816:818	arg1	C6					823:824	C6	823:824	C6	823:824	These are the first proteins that are C-mannosylated on more than one Trp residue as follows: six in C6, four in C7, C8alpha, and C8beta, and two in C9.
10551839	2	29	theme	human	288:292	arg1	examples					265:272	the two examples	257:272	the two examples found so far	257:285	In the two examples found so far, human RNase 2 and interleukin-12, only the first Trp in the recognition motif WXXW is specifically C-mannosylated.
10551839	2	29	theme	human	288:292	arg1	RNase					294:298	human RNase 2	288:300	human RNase 2	288:300	In the two examples found so far, human RNase 2 and interleukin-12, only the first Trp in the recognition motif WXXW is specifically C-mannosylated.
10551839	1	30	theme	C-glycosidic	179:190	arg1	attachment					192:201	the C-glycosidic attachment	175:201	the C-glycosidic attachment of a mannosyl residue to the indole moiety of Trp	175:251	C-Mannosylation is a unique form of protein glycosylation, involving the C-glycosidic attachment of a mannosyl residue to the indole moiety of Trp.
10551839	7	31	from	C7	1033:1034	arg1	C-mannosylated					1138:1151	C-mannosylated	1138:1151	C-mannosylated	1138:1151	The other important finding is that in C6, C7, C8, and C9 Trp residues without a second Trp (or another aromatic residue) at the +3 position can be C-mannosylated.
10551839	3	32	theme	human	529:533	arg1	system					546:551	the human complement system	525:551	the human complement system (C6, C7, C8,and C9)	525:571	To establish the generality of protein C-mannosylation, and to learn more about its mechanism, the terminal components of the human complement system (C6, C7, C8,and C9), which contain multiple and complex recognition motifs, were examined.
10551839	7	33	from	position	1122:1129	arg1	residues					1052:1059	Trp residues	1048:1059	Trp residues without a second Trp (or another aromatic residue) at the +3 position	1048:1129	The other important finding is that in C6, C7, C8, and C9 Trp residues without a second Trp (or another aromatic residue) at the +3 position can be C-mannosylated.
10551839	3	34	contain	contain	580:586	arg2	motifs					621:626	multiple and complex recognition motifs	588:626	multiple and complex recognition motifs	588:626	To establish the generality of protein C-mannosylation, and to learn more about its mechanism, the terminal components of the human complement system (C6, C7, C8,and C9), which contain multiple and complex recognition motifs, were examined.
10551839	3	34	contain	contain	580:586	arg1	components					511:520	the terminal components	498:520	the terminal components	498:520	To establish the generality of protein C-mannosylation, and to learn more about its mechanism, the terminal components of the human complement system (C6, C7, C8,and C9), which contain multiple and complex recognition motifs, were examined.
10551839	4	35	theme	attack	706:711	arg1	complex					713:719	the membrane attack complex	693:719	the membrane attack complex	693:719	Together with C5b they form the cytolytic agent, the membrane attack complex.
10551839	4	35	theme	attack	706:711	arg1	agent					686:690	the cytolytic agent	672:690	the cytolytic agent	672:690	Together with C5b they form the cytolytic agent, the membrane attack complex.
10551839	10	36	theme	thrombospondin	1389:1402	arg1	type					1404:1407	thrombospondin type 1	1389:1409	the thrombospondin type 1 repeats present in these proteins	1385:1443	Finally, all modified Trp residues are part of the highly conserved core of the thrombospondin type 1 repeats present in these proteins.
10551839	6	37	theme	Trp	894:896	arg1	residues					898:905	the 113 Trp residues	886:905	the 113 Trp residues in the complete membrane attack complex	886:945	Thus, from the 113 Trp residues in the complete membrane attack complex, 50 were found to undergo C-mannosylation.
10551839	10	38	theme	repeats	1411:1417	arg1	core					1377:1380	the highly conserved core	1356:1380	the highly conserved core of the thrombospondin type 1 repeats present in these proteins	1356:1443	Finally, all modified Trp residues are part of the highly conserved core of the thrombospondin type 1 repeats present in these proteins.
10551839	0	39	theme	terminal	9:16	arg1	components					18:27	The four terminal components	0:27	The four terminal components of the complement system	0:52	The four terminal components of the complement system are C-mannosylated on multiple tryptophan residues.
10551839	0	39	theme	terminal	9:16	arg1	C-mannosylated					58:71	C-mannosylated	58:71	C-mannosylated	58:71	The four terminal components of the complement system are C-mannosylated on multiple tryptophan residues.
10551839	9	40	theme	primary	1257:1263	arg1	structure					1277:1285	the primary or tertiary structure	1253:1285	the primary or tertiary structure	1253:1285	Whether this is encoded in the primary or tertiary structure is presently unknown.
10551839	8	41	theme	C-mannosylation	1202:1216	arg1	signal					1218:1223	an additional C-mannosylation signal	1188:1223	an additional C-mannosylation signal	1188:1223	This shows that they must contain an additional C-mannosylation signal.
10551839	7	42	from	C-mannosylated	1138:1151	arg1	C6					1029:1030	C6	1029:1030	C6	1029:1030	The other important finding is that in C6, C7, C8, and C9 Trp residues without a second Trp (or another aromatic residue) at the +3 position can be C-mannosylated.
10551839	7	42	from	C-mannosylated	1138:1151	arg1	C8					1037:1038	C8	1037:1038	C8	1037:1038	The other important finding is that in C6, C7, C8, and C9 Trp residues without a second Trp (or another aromatic residue) at the +3 position can be C-mannosylated.
10551839	7	42	from	C-mannosylated	1138:1151	arg1	C9					1045:1046	C9	1045:1046	C9	1045:1046	The other important finding is that in C6, C7, C8, and C9 Trp residues without a second Trp (or another aromatic residue) at the +3 position can be C-mannosylated.
10551839	7	42	from	C-mannosylated	1138:1151	arg1	C7					1033:1034	C7	1033:1034	C7	1033:1034	The other important finding is that in C6, C7, C8, and C9 Trp residues without a second Trp (or another aromatic residue) at the +3 position can be C-mannosylated.
10551839	3	43	theme	protein	434:440	arg1	C-mannosylation					442:456	protein C-mannosylation	434:456	protein C-mannosylation	434:456	To establish the generality of protein C-mannosylation, and to learn more about its mechanism, the terminal components of the human complement system (C6, C7, C8,and C9), which contain multiple and complex recognition motifs, were examined.
10551839	6	44	theme	membrane	923:930	arg1	complex					939:945	the complete membrane attack complex	910:945	the complete membrane attack complex	910:945	Thus, from the 113 Trp residues in the complete membrane attack complex, 50 were found to undergo C-mannosylation.
10551839	7	45	theme	second	1071:1076	arg1	Trp					1078:1080	a second Trp	1069:1080	a second Trp (or another aromatic residue)	1069:1110	The other important finding is that in C6, C7, C8, and C9 Trp residues without a second Trp (or another aromatic residue) at the +3 position can be C-mannosylated.
10551839	7	45	theme	second	1071:1076	arg1	residue					1103:1109	another aromatic residue	1086:1109	another aromatic residue	1086:1109	The other important finding is that in C6, C7, C8, and C9 Trp residues without a second Trp (or another aromatic residue) at the +3 position can be C-mannosylated.
10551839	8	46	theme	additional	1191:1200	arg1	signal					1218:1223	an additional C-mannosylation signal	1188:1223	an additional C-mannosylation signal	1188:1223	This shows that they must contain an additional C-mannosylation signal.
10551839	5	47	from	two	864:866	arg1	C9					871:872	C9	871:872	C9	871:872	These are the first proteins that are C-mannosylated on more than one Trp residue as follows: six in C6, four in C7, C8alpha, and C8beta, and two in C9.
10551839	1	48	theme	mannosyl	208:215	arg1	residue					217:223	a mannosyl residue	206:223	a mannosyl residue	206:223	C-Mannosylation is a unique form of protein glycosylation, involving the C-glycosidic attachment of a mannosyl residue to the indole moiety of Trp.
10551839	7	49	theme	aromatic	1094:1101	arg1	Trp					1078:1080	a second Trp	1069:1080	a second Trp (or another aromatic residue)	1069:1110	The other important finding is that in C6, C7, C8, and C9 Trp residues without a second Trp (or another aromatic residue) at the +3 position can be C-mannosylated.
10551839	7	49	theme	aromatic	1094:1101	arg1	residue					1103:1109	another aromatic residue	1086:1109	another aromatic residue	1086:1109	The other important finding is that in C6, C7, C8, and C9 Trp residues without a second Trp (or another aromatic residue) at the +3 position can be C-mannosylated.
10551839	10	50	theme	core	1377:1380	arg1	part					1348:1351	part	1348:1351	part of the highly conserved core of the thrombospondin type 1 repeats present in these proteins	1348:1443	Finally, all modified Trp residues are part of the highly conserved core of the thrombospondin type 1 repeats present in these proteins.
10551839	10	50	theme	core	1377:1380	arg1	residues					1335:1342	all modified Trp residues	1318:1342	all modified Trp residues	1318:1342	Finally, all modified Trp residues are part of the highly conserved core of the thrombospondin type 1 repeats present in these proteins.
10551839	1	51	attach	attachment	192:201	arg2	residue					217:223	a mannosyl residue	206:223	a mannosyl residue	206:223	C-Mannosylation is a unique form of protein glycosylation, involving the C-glycosidic attachment of a mannosyl residue to the indole moiety of Trp.
10551839	1	51	attach	attachment	192:201	arg1	moiety					239:244	the indole moiety	228:244	the indole moiety of Trp	228:251	C-Mannosylation is a unique form of protein glycosylation, involving the C-glycosidic attachment of a mannosyl residue to the indole moiety of Trp.
10551839	1	52	theme	residue	217:223	arg1	attachment					192:201	the C-glycosidic attachment	175:201	the C-glycosidic attachment of a mannosyl residue to the indole moiety of Trp	175:251	C-Mannosylation is a unique form of protein glycosylation, involving the C-glycosidic attachment of a mannosyl residue to the indole moiety of Trp.
10551839	0	53	theme	system	47:52	arg1	components					18:27	The four terminal components	0:27	The four terminal components of the complement system	0:52	The four terminal components of the complement system are C-mannosylated on multiple tryptophan residues.
10551839	0	53	theme	system	47:52	arg1	C-mannosylated					58:71	C-mannosylated	58:71	C-mannosylated	58:71	The four terminal components of the complement system are C-mannosylated on multiple tryptophan residues.
10551839	11	54	theme	further	1536:1542	arg1	candidates					1544:1553	further candidates	1536:1553	further candidates for C-mannosylation	1536:1573	Since this module has been found in a large number of other proteins, the results suggest further candidates for C-mannosylation.
10551839	3	55	theme	complement	535:544	arg1	system					546:551	the human complement system	525:551	the human complement system (C6, C7, C8,and C9)	525:571	To establish the generality of protein C-mannosylation, and to learn more about its mechanism, the terminal components of the human complement system (C6, C7, C8,and C9), which contain multiple and complex recognition motifs, were examined.
10551839	2	56	from	Trp	337:339	arg1	WXXW					366:369	the recognition motif WXXW	344:369	the recognition motif WXXW	344:369	In the two examples found so far, human RNase 2 and interleukin-12, only the first Trp in the recognition motif WXXW is specifically C-mannosylated.
10551839	0	57	theme	complement	36:45	arg1	system					47:52	the complement system	32:52	the complement system	32:52	The four terminal components of the complement system are C-mannosylated on multiple tryptophan residues.
10551839	10	58	theme	present	1419:1425	arg1	repeats					1411:1417	the thrombospondin type 1 repeats	1385:1417	the thrombospondin type 1 repeats present in these proteins	1385:1443	Finally, all modified Trp residues are part of the highly conserved core of the thrombospondin type 1 repeats present in these proteins.
10551839	3	59	theme	system	546:551	arg1	components					511:520	the terminal components	498:520	the terminal components	498:520	To establish the generality of protein C-mannosylation, and to learn more about its mechanism, the terminal components of the human complement system (C6, C7, C8,and C9), which contain multiple and complex recognition motifs, were examined.
10551839	10	60	theme	conserved	1367:1375	arg1	core					1377:1380	the highly conserved core	1356:1380	the highly conserved core of the thrombospondin type 1 repeats present in these proteins	1356:1443	Finally, all modified Trp residues are part of the highly conserved core of the thrombospondin type 1 repeats present in these proteins.
10551839	3	61	theme	multiple	588:595	arg1	motifs					621:626	multiple and complex recognition motifs	588:626	multiple and complex recognition motifs	588:626	To establish the generality of protein C-mannosylation, and to learn more about its mechanism, the terminal components of the human complement system (C6, C7, C8,and C9), which contain multiple and complex recognition motifs, were examined.
10551839	5	62	dep	proteins	742:749	arg1	proteins					742:749	the first proteins	732:749	the first proteins that are C-mannosylated on more than one Trp residue as follows	732:813	These are the first proteins that are C-mannosylated on more than one Trp residue as follows: six in C6, four in C7, C8alpha, and C8beta, and two in C9.
10551839	5	62	dep	proteins	742:749	arg1	two					864:866	two	864:866	two	864:866	These are the first proteins that are C-mannosylated on more than one Trp residue as follows: six in C6, four in C7, C8alpha, and C8beta, and two in C9.
10551839	5	62	dep	proteins	742:749	arg1	four					827:830	four	827:830	four	827:830	These are the first proteins that are C-mannosylated on more than one Trp residue as follows: six in C6, four in C7, C8alpha, and C8beta, and two in C9.
10551839	5	62	dep	proteins	742:749	arg1	six					816:818	six	816:818	six	816:818	These are the first proteins that are C-mannosylated on more than one Trp residue as follows: six in C6, four in C7, C8alpha, and C8beta, and two in C9.
10551839	10	63	from	proteins	1436:1443	arg1	present					1419:1425	present	1419:1425	present	1419:1425	Finally, all modified Trp residues are part of the highly conserved core of the thrombospondin type 1 repeats present in these proteins.
10551839	1	64	theme	unique	127:132	arg1	form					134:137	a unique form	125:137	a unique form of protein glycosylation	125:162	C-Mannosylation is a unique form of protein glycosylation, involving the C-glycosidic attachment of a mannosyl residue to the indole moiety of Trp.
10551839	1	64	theme	unique	127:132	arg1	C-Mannosylation					106:120	C-Mannosylation	106:120	C-Mannosylation	106:120	C-Mannosylation is a unique form of protein glycosylation, involving the C-glycosidic attachment of a mannosyl residue to the indole moiety of Trp.
10551839	5	65	from	four	827:830	arg1	C8beta					852:857	C8beta	852:857	C8beta	852:857	These are the first proteins that are C-mannosylated on more than one Trp residue as follows: six in C6, four in C7, C8alpha, and C8beta, and two in C9.
10551839	5	65	from	four	827:830	arg1	C7					835:836	C7	835:836	C7	835:836	These are the first proteins that are C-mannosylated on more than one Trp residue as follows: six in C6, four in C7, C8alpha, and C8beta, and two in C9.
10551839	5	65	from	four	827:830	arg1	C8alpha					839:845	C8alpha	839:845	C8alpha	839:845	These are the first proteins that are C-mannosylated on more than one Trp residue as follows: six in C6, four in C7, C8alpha, and C8beta, and two in C9.
10551839	11	66	theme	large	1484:1488	arg1	number					1490:1495	a large number	1482:1495	a large number of other proteins	1482:1513	Since this module has been found in a large number of other proteins, the results suggest further candidates for C-mannosylation.
10551839	10	67	from	present	1419:1425	arg1	proteins					1436:1443	these proteins	1430:1443	these proteins	1430:1443	Finally, all modified Trp residues are part of the highly conserved core of the thrombospondin type 1 repeats present in these proteins.
10551839	10	68	theme	modified	1322:1329	arg1	part					1348:1351	part	1348:1351	part of the highly conserved core of the thrombospondin type 1 repeats present in these proteins	1348:1443	Finally, all modified Trp residues are part of the highly conserved core of the thrombospondin type 1 repeats present in these proteins.
10551839	10	68	theme	modified	1322:1329	arg1	residues					1335:1342	all modified Trp residues	1318:1342	all modified Trp residues	1318:1342	Finally, all modified Trp residues are part of the highly conserved core of the thrombospondin type 1 repeats present in these proteins.
10551839	6	69	theme	attack	932:937	arg1	complex					939:945	the complete membrane attack complex	910:945	the complete membrane attack complex	910:945	Thus, from the 113 Trp residues in the complete membrane attack complex, 50 were found to undergo C-mannosylation.
10551839	3	70	theme	C-mannosylation	442:456	arg1	generality					420:429	the generality	416:429	the generality of protein C-mannosylation	416:456	To establish the generality of protein C-mannosylation, and to learn more about its mechanism, the terminal components of the human complement system (C6, C7, C8,and C9), which contain multiple and complex recognition motifs, were examined.
10551839	2	71	theme	motif	360:364	arg1	WXXW					366:369	the recognition motif WXXW	344:369	the recognition motif WXXW	344:369	In the two examples found so far, human RNase 2 and interleukin-12, only the first Trp in the recognition motif WXXW is specifically C-mannosylated.
10551839	2	72	gly	C-mannosylated	387:400	arg1	Trp					337:339	only the first Trp	322:339	only the first Trp in the recognition motif WXXW	322:369	In the two examples found so far, human RNase 2 and interleukin-12, only the first Trp in the recognition motif WXXW is specifically C-mannosylated.
10551839	2	72	gly	C-mannosylated	387:400	arg1	C-mannosylated					387:400	C-mannosylated	387:400	C-mannosylated	387:400	In the two examples found so far, human RNase 2 and interleukin-12, only the first Trp in the recognition motif WXXW is specifically C-mannosylated.
10551839	9	73	theme	tertiary	1268:1275	arg1	structure					1277:1285	the primary or tertiary structure	1253:1285	the primary or tertiary structure	1253:1285	Whether this is encoded in the primary or tertiary structure is presently unknown.
10551839	2	74	theme	first	331:335	arg1	Trp					337:339	only the first Trp	322:339	only the first Trp in the recognition motif WXXW	322:369	In the two examples found so far, human RNase 2 and interleukin-12, only the first Trp in the recognition motif WXXW is specifically C-mannosylated.
10551839	2	74	theme	first	331:335	arg1	C-mannosylated					387:400	C-mannosylated	387:400	C-mannosylated	387:400	In the two examples found so far, human RNase 2 and interleukin-12, only the first Trp in the recognition motif WXXW is specifically C-mannosylated.
10551839	2	75	from	examples	265:272	arg1	C-mannosylated					387:400	C-mannosylated	387:400	C-mannosylated	387:400	In the two examples found so far, human RNase 2 and interleukin-12, only the first Trp in the recognition motif WXXW is specifically C-mannosylated.
10551839	2	75	from	examples	265:272	arg1	Trp					337:339	only the first Trp	322:339	only the first Trp in the recognition motif WXXW	322:369	In the two examples found so far, human RNase 2 and interleukin-12, only the first Trp in the recognition motif WXXW is specifically C-mannosylated.
10551839	1	76	theme	indole	232:237	arg1	moiety					239:244	the indole moiety	228:244	the indole moiety of Trp	228:251	C-Mannosylation is a unique form of protein glycosylation, involving the C-glycosidic attachment of a mannosyl residue to the indole moiety of Trp.
10551839	6	77	gly	C-mannosylation	973:987	arg1	50					948:949	50	948:949	50	948:949	Thus, from the 113 Trp residues in the complete membrane attack complex, 50 were found to undergo C-mannosylation.
10551839	3	78	theme	recognition	609:619	arg1	motifs					621:626	multiple and complex recognition motifs	588:626	multiple and complex recognition motifs	588:626	To establish the generality of protein C-mannosylation, and to learn more about its mechanism, the terminal components of the human complement system (C6, C7, C8,and C9), which contain multiple and complex recognition motifs, were examined.
10551839	4	79	theme	membrane	697:704	arg1	complex					713:719	the membrane attack complex	693:719	the membrane attack complex	693:719	Together with C5b they form the cytolytic agent, the membrane attack complex.
10551839	4	79	theme	membrane	697:704	arg1	agent					686:690	the cytolytic agent	672:690	the cytolytic agent	672:690	Together with C5b they form the cytolytic agent, the membrane attack complex.
10551839	1	80	theme	protein	142:148	arg1	glycosylation					150:162	protein glycosylation	142:162	protein glycosylation	142:162	C-Mannosylation is a unique form of protein glycosylation, involving the C-glycosidic attachment of a mannosyl residue to the indole moiety of Trp.
10551839	7	81	from	C6	1029:1030	arg1	C-mannosylated					1138:1151	C-mannosylated	1138:1151	C-mannosylated	1138:1151	The other important finding is that in C6, C7, C8, and C9 Trp residues without a second Trp (or another aromatic residue) at the +3 position can be C-mannosylated.
1281977	11	0	gly	glycosylated	1888:1899	arg1	each					1871:1874	each	1871:1874	each	1871:1874	These studies indicate that human liver aspartylglucosaminidase is composed of two non-identical polypeptides, each of which is glycosylated.
1281977	11	0	gly	glycosylated	1888:1899	arg1	polypeptides					1857:1868	two non-identical polypeptides	1839:1868	two non-identical polypeptides	1839:1868	These studies indicate that human liver aspartylglucosaminidase is composed of two non-identical polypeptides, each of which is glycosylated.
1281977	4	1	gly	glycopeptides	693:705	arg2	glycopeptides					693:705	glycopeptides	693:705	glycopeptides	693:705	The altered metabolism in AGU results from a deficiency of the enzyme aspartylglucosaminidase (1-aspartamido-beta-N-acetylglucosamine amidohydrolase), which hydrolyses the asparagine to N-acetylglucosamine linkages of glycoproteins and glycopeptides.
1281977	7	2	theme	Enzyme	1038:1043	arg1	activity					1045:1052	Enzyme activity	1038:1052	Enzyme activity	1038:1052	Enzyme activity was followed by measuring colorimetrically the N-acetylglucosamine released from aspartylglucosamine at 56 degrees C.
1281977	1	3	theme	family	153:158	arg1	members					131:137	four members	126:137	four members of a Canadian family	126:158	We have recently diagnosed aspartylglucosaminuria (AGU) in four members of a Canadian family.
1281977	6	4	theme	concanavalin	922:933	arg1	A-Sepharose					935:945	concanavalin A-Sepharose	922:945	concanavalin A-Sepharose	922:945	The enzyme has been purified to homogeneity by using heat treatment, (NH4)2SO4 fractionation, and chromatography on concanavalin A-Sepharose, DEAE-Sepharose, sulphopropyl-Sephadex, hydroxyapatite, DEAE-cellulose and Sephadex G-100.
1281977	7	5	theme	degrees	1161:1167	arg1	C					1169:1169	56 degrees C	1158:1169	56 degrees C	1158:1169	Enzyme activity was followed by measuring colorimetrically the N-acetylglucosamine released from aspartylglucosamine at 56 degrees C.
1281977	9	6	from	denaturation	1405:1416	arg1	SDS					1432:1434	SDS	1432:1434	SDS	1432:1434	After denaturation by boiling in SDS the 56 kDa protein was lost with the corresponding appearance of polypeptides alpha,beta and beta 1, lacking enzyme activity, at 24.6, 18.4 and 17.4 kDa respectively.
1281977	6	7	theme	heat	859:862	arg1	treatment					864:872	heat treatment	859:872	heat treatment	859:872	The enzyme has been purified to homogeneity by using heat treatment, (NH4)2SO4 fractionation, and chromatography on concanavalin A-Sepharose, DEAE-Sepharose, sulphopropyl-Sephadex, hydroxyapatite, DEAE-cellulose and Sephadex G-100.
1281977	3	8	theme	glycopeptides	369:381	arg1	accumulation					347:358	A lesser accumulation	338:358	A lesser accumulation of these glycopeptides	338:381	A lesser accumulation of these glycopeptides is seen in the kidney and brain, and they are also excreted in the urine.
1281977	12	9	theme	alpha	1919:1923	arg1	N-termini					1906:1914	The N-termini	1902:1914	The N-termini of alpha,beta and beta 1	1902:1939	The N-termini of alpha,beta and beta 1 were directly accessible for sequencing, and the first 21, 26 and 22 amino acids respectively were identified.
1281977	12	9	theme	alpha	1919:1923	arg1	accessible					1955:1964	accessible	1955:1964	accessible	1955:1964	The N-termini of alpha,beta and beta 1 were directly accessible for sequencing, and the first 21, 26 and 22 amino acids respectively were identified.
1281977	9	10	theme	enzyme	1545:1550	arg1	activity					1552:1559	enzyme activity	1545:1559	enzyme activity	1545:1559	After denaturation by boiling in SDS the 56 kDa protein was lost with the corresponding appearance of polypeptides alpha,beta and beta 1, lacking enzyme activity, at 24.6, 18.4 and 17.4 kDa respectively.
1281977	9	11	theme	kDa	1443:1445	arg1	protein					1447:1453	the 56 kDa protein	1436:1453	the 56 kDa protein	1436:1453	After denaturation by boiling in SDS the 56 kDa protein was lost with the corresponding appearance of polypeptides alpha,beta and beta 1, lacking enzyme activity, at 24.6, 18.4 and 17.4 kDa respectively.
1281977	8	12	theme	molecular	1218:1226	arg1	mass					1228:1231	a 'native' molecular mass	1207:1231	a 'native' molecular mass of 56 kDa in SDS/12.5%-PAGE gels	1207:1264	The purified enzyme protein ran at a 'native' molecular mass of 56 kDa in SDS/12.5%-PAGE gels, and the enzyme activity could be quantitatively recovered at this molecular mass by using gel slices as enzyme source in the assay.
1281977	4	13	theme	altered	461:467	arg1	metabolism					469:478	The altered metabolism	457:478	The altered metabolism in AGU	457:485	The altered metabolism in AGU results from a deficiency of the enzyme aspartylglucosaminidase (1-aspartamido-beta-N-acetylglucosamine amidohydrolase), which hydrolyses the asparagine to N-acetylglucosamine linkages of glycoproteins and glycopeptides.
1281977	8	14	theme	enzyme	1371:1376	arg1	source					1378:1383	enzyme source	1371:1383	enzyme source	1371:1383	The purified enzyme protein ran at a 'native' molecular mass of 56 kDa in SDS/12.5%-PAGE gels, and the enzyme activity could be quantitatively recovered at this molecular mass by using gel slices as enzyme source in the assay.
1281977	12	15	theme	first	1990:1994	arg1	acids					2016:2020	the first 21, 26 and 22 amino acids	1986:2020	the first 21, 26 and 22 amino acids respectively	1986:2033	The N-termini of alpha,beta and beta 1 were directly accessible for sequencing, and the first 21, 26 and 22 amino acids respectively were identified.
1281977	10	16	dep	15.8	1750:1753	arg1	to					1747:1748	to	1747:1748	to	1747:1748	Treatment of heat-denatured enzyme with N-glycosidase F resulted in the following decreases in molecular mass; 24.6 to 23 kDa and 18.4 and 17.4 to 15.8 kDa.
1281977	6	17	from	treatment	864:872	arg1	DEAE-Sepharose					948:961	DEAE-Sepharose	948:961	DEAE-Sepharose	948:961	The enzyme has been purified to homogeneity by using heat treatment, (NH4)2SO4 fractionation, and chromatography on concanavalin A-Sepharose, DEAE-Sepharose, sulphopropyl-Sephadex, hydroxyapatite, DEAE-cellulose and Sephadex G-100.
1281977	6	17	from	treatment	864:872	arg1	DEAE-cellulose					1003:1016	DEAE-cellulose	1003:1016	DEAE-cellulose	1003:1016	The enzyme has been purified to homogeneity by using heat treatment, (NH4)2SO4 fractionation, and chromatography on concanavalin A-Sepharose, DEAE-Sepharose, sulphopropyl-Sephadex, hydroxyapatite, DEAE-cellulose and Sephadex G-100.
1281977	6	17	from	treatment	864:872	arg1	G-100					1031:1035	Sephadex G-100	1022:1035	Sephadex G-100	1022:1035	The enzyme has been purified to homogeneity by using heat treatment, (NH4)2SO4 fractionation, and chromatography on concanavalin A-Sepharose, DEAE-Sepharose, sulphopropyl-Sephadex, hydroxyapatite, DEAE-cellulose and Sephadex G-100.
1281977	6	17	from	treatment	864:872	arg1	sulphopropyl-Sephadex					964:984	sulphopropyl-Sephadex	964:984	sulphopropyl-Sephadex	964:984	The enzyme has been purified to homogeneity by using heat treatment, (NH4)2SO4 fractionation, and chromatography on concanavalin A-Sepharose, DEAE-Sepharose, sulphopropyl-Sephadex, hydroxyapatite, DEAE-cellulose and Sephadex G-100.
1281977	6	17	from	treatment	864:872	arg1	hydroxyapatite					987:1000	hydroxyapatite	987:1000	hydroxyapatite	987:1000	The enzyme has been purified to homogeneity by using heat treatment, (NH4)2SO4 fractionation, and chromatography on concanavalin A-Sepharose, DEAE-Sepharose, sulphopropyl-Sephadex, hydroxyapatite, DEAE-cellulose and Sephadex G-100.
1281977	6	17	from	treatment	864:872	arg1	A-Sepharose					935:945	concanavalin A-Sepharose	922:945	concanavalin A-Sepharose	922:945	The enzyme has been purified to homogeneity by using heat treatment, (NH4)2SO4 fractionation, and chromatography on concanavalin A-Sepharose, DEAE-Sepharose, sulphopropyl-Sephadex, hydroxyapatite, DEAE-cellulose and Sephadex G-100.
1281977	7	18	attach	released	1121:1128	arg1	aspartylglucosamine					1135:1153	aspartylglucosamine	1135:1153	aspartylglucosamine	1135:1153	Enzyme activity was followed by measuring colorimetrically the N-acetylglucosamine released from aspartylglucosamine at 56 degrees C.
1281977	7	18	attach	released	1121:1128	arg2	N-acetylglucosamine					1101:1119	colorimetrically the N-acetylglucosamine	1080:1119	colorimetrically the N-acetylglucosamine released from aspartylglucosamine at 56 degrees C	1080:1169	Enzyme activity was followed by measuring colorimetrically the N-acetylglucosamine released from aspartylglucosamine at 56 degrees C.
1281977	8	19	theme	enzyme	1275:1280	arg1	activity					1282:1289	the enzyme activity	1271:1289	the enzyme activity	1271:1289	The purified enzyme protein ran at a 'native' molecular mass of 56 kDa in SDS/12.5%-PAGE gels, and the enzyme activity could be quantitatively recovered at this molecular mass by using gel slices as enzyme source in the assay.
1281977	0	20	theme	aspartylglucosaminidase	42:64	arg1	structure					17:25	structure	17:25	structure	17:25	Purification and structure of human liver aspartylglucosaminidase.
1281977	0	20	theme	aspartylglucosaminidase	42:64	arg1	Purification					0:11	Purification	0:11	Purification	0:11	Purification and structure of human liver aspartylglucosaminidase.
1281977	4	21	from	metabolism	469:478	arg1	AGU					483:485	AGU	483:485	AGU	483:485	The altered metabolism in AGU results from a deficiency of the enzyme aspartylglucosaminidase (1-aspartamido-beta-N-acetylglucosamine amidohydrolase), which hydrolyses the asparagine to N-acetylglucosamine linkages of glycoproteins and glycopeptides.
1281977	8	22	dep	ran	1200:1202	arg1	mass					1228:1231	a 'native' molecular mass	1207:1231	a 'native' molecular mass of 56 kDa in SDS/12.5%-PAGE gels	1207:1264	The purified enzyme protein ran at a 'native' molecular mass of 56 kDa in SDS/12.5%-PAGE gels, and the enzyme activity could be quantitatively recovered at this molecular mass by using gel slices as enzyme source in the assay.
1281977	4	23	theme	glycopeptides	693:705	arg1	linkages					663:670	N-acetylglucosamine linkages	643:670	N-acetylglucosamine linkages of glycoproteins and glycopeptides	643:705	The altered metabolism in AGU results from a deficiency of the enzyme aspartylglucosaminidase (1-aspartamido-beta-N-acetylglucosamine amidohydrolase), which hydrolyses the asparagine to N-acetylglucosamine linkages of glycoproteins and glycopeptides.
1281977	8	24	theme	native	1210:1215	arg1	mass					1228:1231	a 'native' molecular mass	1207:1231	a 'native' molecular mass of 56 kDa in SDS/12.5%-PAGE gels	1207:1264	The purified enzyme protein ran at a 'native' molecular mass of 56 kDa in SDS/12.5%-PAGE gels, and the enzyme activity could be quantitatively recovered at this molecular mass by using gel slices as enzyme source in the assay.
1281977	4	25	gly	glycoproteins	675:687	arg1	glycoproteins					675:687	glycoproteins	675:687	glycoproteins	675:687	The altered metabolism in AGU results from a deficiency of the enzyme aspartylglucosaminidase (1-aspartamido-beta-N-acetylglucosamine amidohydrolase), which hydrolyses the asparagine to N-acetylglucosamine linkages of glycoproteins and glycopeptides.
1281977	5	26	theme	aspartylglucosaminidase	781:803	arg1	purification					765:776	the purification	761:776	the purification of aspartylglucosaminidase	761:803	We have used human liver as a source of material for the purification of aspartylglucosaminidase.
1281977	2	27	theme	individuals	325:335	arg1	spleen					294:299	spleen	294:299	spleen	294:299	AGU is a lysosomal storage disease in which asparagine-linked glycopeptides accumulate to particularly high concentrations in liver, spleen and thyroid of affected individuals.
1281977	2	27	theme	individuals	325:335	arg1	liver					287:291	liver	287:291	liver	287:291	AGU is a lysosomal storage disease in which asparagine-linked glycopeptides accumulate to particularly high concentrations in liver, spleen and thyroid of affected individuals.
1281977	2	27	theme	individuals	325:335	arg1	thyroid					305:311	thyroid	305:311	thyroid	305:311	AGU is a lysosomal storage disease in which asparagine-linked glycopeptides accumulate to particularly high concentrations in liver, spleen and thyroid of affected individuals.
1281977	8	28	theme	enzyme	1185:1190	arg1	ran					1200:1202	The purified enzyme protein ran	1172:1202	The purified enzyme protein ran	1172:1202	The purified enzyme protein ran at a 'native' molecular mass of 56 kDa in SDS/12.5%-PAGE gels, and the enzyme activity could be quantitatively recovered at this molecular mass by using gel slices as enzyme source in the assay.
1281977	10	29	theme	N-glycosidase	1643:1655	arg1	F					1657:1657	N-glycosidase F	1643:1657	N-glycosidase F	1643:1657	Treatment of heat-denatured enzyme with N-glycosidase F resulted in the following decreases in molecular mass; 24.6 to 23 kDa and 18.4 and 17.4 to 15.8 kDa.
1281977	8	30	theme	kDa	1239:1241	arg1	mass					1228:1231	a 'native' molecular mass	1207:1231	a 'native' molecular mass of 56 kDa in SDS/12.5%-PAGE gels	1207:1264	The purified enzyme protein ran at a 'native' molecular mass of 56 kDa in SDS/12.5%-PAGE gels, and the enzyme activity could be quantitatively recovered at this molecular mass by using gel slices as enzyme source in the assay.
1281977	9	31	theme	24.6	1565:1568	arg1	kDa					1585:1587	24.6, 18.4 and 17.4 kDa	1565:1587	kDa	1585:1587	After denaturation by boiling in SDS the 56 kDa protein was lost with the corresponding appearance of polypeptides alpha,beta and beta 1, lacking enzyme activity, at 24.6, 18.4 and 17.4 kDa respectively.
1281977	2	32	theme	affected	316:323	arg1	individuals					325:335	affected individuals	316:335	affected individuals	316:335	AGU is a lysosomal storage disease in which asparagine-linked glycopeptides accumulate to particularly high concentrations in liver, spleen and thyroid of affected individuals.
1281977	8	33	theme	%	1254:1254	arg1	gels					1261:1264	SDS/12.5%-PAGE gels	1246:1264	SDS/12.5%-PAGE gels	1246:1264	The purified enzyme protein ran at a 'native' molecular mass of 56 kDa in SDS/12.5%-PAGE gels, and the enzyme activity could be quantitatively recovered at this molecular mass by using gel slices as enzyme source in the assay.
1281977	4	34	theme	aspartylglucosaminidase	527:549	arg1	deficiency					502:511	a deficiency	500:511	a deficiency	500:511	The altered metabolism in AGU results from a deficiency of the enzyme aspartylglucosaminidase (1-aspartamido-beta-N-acetylglucosamine amidohydrolase), which hydrolyses the asparagine to N-acetylglucosamine linkages of glycoproteins and glycopeptides.
1281977	9	35	theme	corresponding	1473:1485	arg1	appearance					1487:1496	the corresponding appearance	1469:1496	the corresponding appearance of polypeptides alpha,beta and beta 1	1469:1534	After denaturation by boiling in SDS the 56 kDa protein was lost with the corresponding appearance of polypeptides alpha,beta and beta 1, lacking enzyme activity, at 24.6, 18.4 and 17.4 kDa respectively.
1281977	5	36	used	used	716:719	arg2	We					708:709	We	708:709	We	708:709	We have used human liver as a source of material for the purification of aspartylglucosaminidase.
1281977	3	37	gly	glycopeptides	369:381	arg2	glycopeptides					369:381	these glycopeptides	363:381	these glycopeptides	363:381	A lesser accumulation of these glycopeptides is seen in the kidney and brain, and they are also excreted in the urine.
1281977	2	38	theme	lysosomal	170:178	arg1	disease					188:194	a lysosomal storage disease	168:194	a lysosomal storage disease in which asparagine-linked glycopeptides accumulate to particularly high concentrations in liver, spleen and thyroid of affected individuals	168:335	AGU is a lysosomal storage disease in which asparagine-linked glycopeptides accumulate to particularly high concentrations in liver, spleen and thyroid of affected individuals.
1281977	2	38	theme	lysosomal	170:178	arg1	AGU					161:163	AGU	161:163	AGU	161:163	AGU is a lysosomal storage disease in which asparagine-linked glycopeptides accumulate to particularly high concentrations in liver, spleen and thyroid of affected individuals.
1281977	10	39	dep	mass	1708:1711	arg1	kDa					1755:1757	18.4 and 17.4 to 15.8 kDa	1733:1757	18.4 and 17.4 to 15.8 kDa	1733:1757	Treatment of heat-denatured enzyme with N-glycosidase F resulted in the following decreases in molecular mass; 24.6 to 23 kDa and 18.4 and 17.4 to 15.8 kDa.
1281977	10	39	dep	mass	1708:1711	arg1	kDa					1725:1727	24.6 to 23 kDa	1714:1727	24.6 to 23 kDa	1714:1727	Treatment of heat-denatured enzyme with N-glycosidase F resulted in the following decreases in molecular mass; 24.6 to 23 kDa and 18.4 and 17.4 to 15.8 kDa.
1281977	10	40	theme	following	1675:1683	arg1	decreases					1685:1693	the following decreases	1671:1693	the following decreases in molecular mass; 24.6 to 23 kDa and 18.4 and 17.4 to 15.8 kDa	1671:1757	Treatment of heat-denatured enzyme with N-glycosidase F resulted in the following decreases in molecular mass; 24.6 to 23 kDa and 18.4 and 17.4 to 15.8 kDa.
1281977	0	41	theme	liver	36:40	arg1	aspartylglucosaminidase					42:64	human liver aspartylglucosaminidase	30:64	human liver aspartylglucosaminidase	30:64	Purification and structure of human liver aspartylglucosaminidase.
1281977	4	42	theme	1-aspartamido-beta-N-acetylglucosamine	552:589	arg1	aspartylglucosaminidase					527:549	the enzyme aspartylglucosaminidase	516:549	the enzyme aspartylglucosaminidase (1-aspartamido-beta-N-acetylglucosamine amidohydrolase)	516:605	The altered metabolism in AGU results from a deficiency of the enzyme aspartylglucosaminidase (1-aspartamido-beta-N-acetylglucosamine amidohydrolase), which hydrolyses the asparagine to N-acetylglucosamine linkages of glycoproteins and glycopeptides.
1281977	4	42	theme	1-aspartamido-beta-N-acetylglucosamine	552:589	arg1	amidohydrolase					591:604	1-aspartamido-beta-N-acetylglucosamine amidohydrolase	552:604	1-aspartamido-beta-N-acetylglucosamine amidohydrolase	552:604	The altered metabolism in AGU results from a deficiency of the enzyme aspartylglucosaminidase (1-aspartamido-beta-N-acetylglucosamine amidohydrolase), which hydrolyses the asparagine to N-acetylglucosamine linkages of glycoproteins and glycopeptides.
1281977	8	43	theme	purified	1176:1183	arg1	ran					1200:1202	The purified enzyme protein ran	1172:1202	The purified enzyme protein ran	1172:1202	The purified enzyme protein ran at a 'native' molecular mass of 56 kDa in SDS/12.5%-PAGE gels, and the enzyme activity could be quantitatively recovered at this molecular mass by using gel slices as enzyme source in the assay.
1281977	9	44	theme	17.4	1580:1583	arg1	kDa					1585:1587	24.6, 18.4 and 17.4 kDa	1565:1587	kDa	1585:1587	After denaturation by boiling in SDS the 56 kDa protein was lost with the corresponding appearance of polypeptides alpha,beta and beta 1, lacking enzyme activity, at 24.6, 18.4 and 17.4 kDa respectively.
1281977	2	45	from	concentrations	269:282	arg1	spleen					294:299	spleen	294:299	spleen	294:299	AGU is a lysosomal storage disease in which asparagine-linked glycopeptides accumulate to particularly high concentrations in liver, spleen and thyroid of affected individuals.
1281977	2	45	from	concentrations	269:282	arg1	liver					287:291	liver	287:291	liver	287:291	AGU is a lysosomal storage disease in which asparagine-linked glycopeptides accumulate to particularly high concentrations in liver, spleen and thyroid of affected individuals.
1281977	2	45	from	concentrations	269:282	arg1	thyroid					305:311	thyroid	305:311	thyroid	305:311	AGU is a lysosomal storage disease in which asparagine-linked glycopeptides accumulate to particularly high concentrations in liver, spleen and thyroid of affected individuals.
1281977	0	46	theme	human	30:34	arg1	aspartylglucosaminidase					42:64	human liver aspartylglucosaminidase	30:64	human liver aspartylglucosaminidase	30:64	Purification and structure of human liver aspartylglucosaminidase.
1281977	11	47	theme	human	1788:1792	arg1	aspartylglucosaminidase					1800:1822	human liver aspartylglucosaminidase	1788:1822	human liver aspartylglucosaminidase	1788:1822	These studies indicate that human liver aspartylglucosaminidase is composed of two non-identical polypeptides, each of which is glycosylated.
1281977	5	48	theme	material	748:755	arg1	liver					727:731	human liver	721:731	human liver	721:731	We have used human liver as a source of material for the purification of aspartylglucosaminidase.
1281977	5	48	theme	material	748:755	arg1	source					738:743	a source	736:743	a source of material for the purification of aspartylglucosaminidase	736:803	We have used human liver as a source of material for the purification of aspartylglucosaminidase.
1281977	6	49	theme	2SO4	880:883	arg1	fractionation					885:897	(NH4)2SO4 fractionation	875:897	(NH4)2SO4 fractionation	875:897	The enzyme has been purified to homogeneity by using heat treatment, (NH4)2SO4 fractionation, and chromatography on concanavalin A-Sepharose, DEAE-Sepharose, sulphopropyl-Sephadex, hydroxyapatite, DEAE-cellulose and Sephadex G-100.
1281977	12	50	theme	beta	1925:1928	arg1	N-termini					1906:1914	The N-termini	1902:1914	The N-termini of alpha,beta and beta 1	1902:1939	The N-termini of alpha,beta and beta 1 were directly accessible for sequencing, and the first 21, 26 and 22 amino acids respectively were identified.
1281977	12	50	theme	beta	1925:1928	arg1	accessible					1955:1964	accessible	1955:1964	accessible	1955:1964	The N-termini of alpha,beta and beta 1 were directly accessible for sequencing, and the first 21, 26 and 22 amino acids respectively were identified.
1281977	4	51	theme	glycoproteins	675:687	arg1	linkages					663:670	N-acetylglucosamine linkages	643:670	N-acetylglucosamine linkages of glycoproteins and glycopeptides	643:705	The altered metabolism in AGU results from a deficiency of the enzyme aspartylglucosaminidase (1-aspartamido-beta-N-acetylglucosamine amidohydrolase), which hydrolyses the asparagine to N-acetylglucosamine linkages of glycoproteins and glycopeptides.
1281977	12	52	theme	beta	1934:1937	arg1	N-termini					1906:1914	The N-termini	1902:1914	The N-termini of alpha,beta and beta 1	1902:1939	The N-termini of alpha,beta and beta 1 were directly accessible for sequencing, and the first 21, 26 and 22 amino acids respectively were identified.
1281977	12	52	theme	beta	1934:1937	arg1	accessible					1955:1964	accessible	1955:1964	accessible	1955:1964	The N-termini of alpha,beta and beta 1 were directly accessible for sequencing, and the first 21, 26 and 22 amino acids respectively were identified.
1281977	6	53	from	chromatography	904:917	arg1	DEAE-Sepharose					948:961	DEAE-Sepharose	948:961	DEAE-Sepharose	948:961	The enzyme has been purified to homogeneity by using heat treatment, (NH4)2SO4 fractionation, and chromatography on concanavalin A-Sepharose, DEAE-Sepharose, sulphopropyl-Sephadex, hydroxyapatite, DEAE-cellulose and Sephadex G-100.
1281977	6	53	from	chromatography	904:917	arg1	DEAE-cellulose					1003:1016	DEAE-cellulose	1003:1016	DEAE-cellulose	1003:1016	The enzyme has been purified to homogeneity by using heat treatment, (NH4)2SO4 fractionation, and chromatography on concanavalin A-Sepharose, DEAE-Sepharose, sulphopropyl-Sephadex, hydroxyapatite, DEAE-cellulose and Sephadex G-100.
1281977	6	53	from	chromatography	904:917	arg1	G-100					1031:1035	Sephadex G-100	1022:1035	Sephadex G-100	1022:1035	The enzyme has been purified to homogeneity by using heat treatment, (NH4)2SO4 fractionation, and chromatography on concanavalin A-Sepharose, DEAE-Sepharose, sulphopropyl-Sephadex, hydroxyapatite, DEAE-cellulose and Sephadex G-100.
1281977	6	53	from	chromatography	904:917	arg1	sulphopropyl-Sephadex					964:984	sulphopropyl-Sephadex	964:984	sulphopropyl-Sephadex	964:984	The enzyme has been purified to homogeneity by using heat treatment, (NH4)2SO4 fractionation, and chromatography on concanavalin A-Sepharose, DEAE-Sepharose, sulphopropyl-Sephadex, hydroxyapatite, DEAE-cellulose and Sephadex G-100.
1281977	6	53	from	chromatography	904:917	arg1	hydroxyapatite					987:1000	hydroxyapatite	987:1000	hydroxyapatite	987:1000	The enzyme has been purified to homogeneity by using heat treatment, (NH4)2SO4 fractionation, and chromatography on concanavalin A-Sepharose, DEAE-Sepharose, sulphopropyl-Sephadex, hydroxyapatite, DEAE-cellulose and Sephadex G-100.
1281977	6	53	from	chromatography	904:917	arg1	A-Sepharose					935:945	concanavalin A-Sepharose	922:945	concanavalin A-Sepharose	922:945	The enzyme has been purified to homogeneity by using heat treatment, (NH4)2SO4 fractionation, and chromatography on concanavalin A-Sepharose, DEAE-Sepharose, sulphopropyl-Sephadex, hydroxyapatite, DEAE-cellulose and Sephadex G-100.
1281977	8	54	theme	protein	1192:1198	arg1	ran					1200:1202	The purified enzyme protein ran	1172:1202	The purified enzyme protein ran	1172:1202	The purified enzyme protein ran at a 'native' molecular mass of 56 kDa in SDS/12.5%-PAGE gels, and the enzyme activity could be quantitatively recovered at this molecular mass by using gel slices as enzyme source in the assay.
1281977	6	55	theme	Sephadex	1022:1029	arg1	G-100					1031:1035	Sephadex G-100	1022:1035	Sephadex G-100	1022:1035	The enzyme has been purified to homogeneity by using heat treatment, (NH4)2SO4 fractionation, and chromatography on concanavalin A-Sepharose, DEAE-Sepharose, sulphopropyl-Sephadex, hydroxyapatite, DEAE-cellulose and Sephadex G-100.
1281977	8	56	theme	molecular	1333:1341	arg1	mass					1343:1346	this molecular mass	1328:1346	this molecular mass	1328:1346	The purified enzyme protein ran at a 'native' molecular mass of 56 kDa in SDS/12.5%-PAGE gels, and the enzyme activity could be quantitatively recovered at this molecular mass by using gel slices as enzyme source in the assay.
1281977	2	57	gly	glycopeptides	223:235	arg2	glycopeptides					223:235	asparagine-linked glycopeptides	205:235	asparagine-linked glycopeptides	205:235	AGU is a lysosomal storage disease in which asparagine-linked glycopeptides accumulate to particularly high concentrations in liver, spleen and thyroid of affected individuals.
1281977	4	58	theme	enzyme	520:525	arg1	aspartylglucosaminidase					527:549	the enzyme aspartylglucosaminidase	516:549	the enzyme aspartylglucosaminidase (1-aspartamido-beta-N-acetylglucosamine amidohydrolase)	516:605	The altered metabolism in AGU results from a deficiency of the enzyme aspartylglucosaminidase (1-aspartamido-beta-N-acetylglucosamine amidohydrolase), which hydrolyses the asparagine to N-acetylglucosamine linkages of glycoproteins and glycopeptides.
1281977	4	58	theme	enzyme	520:525	arg1	amidohydrolase					591:604	1-aspartamido-beta-N-acetylglucosamine amidohydrolase	552:604	1-aspartamido-beta-N-acetylglucosamine amidohydrolase	552:604	The altered metabolism in AGU results from a deficiency of the enzyme aspartylglucosaminidase (1-aspartamido-beta-N-acetylglucosamine amidohydrolase), which hydrolyses the asparagine to N-acetylglucosamine linkages of glycoproteins and glycopeptides.
1281977	5	59	theme	human	721:725	arg1	liver					727:731	human liver	721:731	human liver	721:731	We have used human liver as a source of material for the purification of aspartylglucosaminidase.
1281977	5	59	theme	human	721:725	arg1	source					738:743	a source	736:743	a source of material for the purification of aspartylglucosaminidase	736:803	We have used human liver as a source of material for the purification of aspartylglucosaminidase.
1281977	6	60	theme	NH4	876:878	arg1	fractionation					885:897	(NH4)2SO4 fractionation	875:897	(NH4)2SO4 fractionation	875:897	The enzyme has been purified to homogeneity by using heat treatment, (NH4)2SO4 fractionation, and chromatography on concanavalin A-Sepharose, DEAE-Sepharose, sulphopropyl-Sephadex, hydroxyapatite, DEAE-cellulose and Sephadex G-100.
1281977	2	61	theme	asparagine-linked	205:221	arg1	glycopeptides					223:235	asparagine-linked glycopeptides	205:235	asparagine-linked glycopeptides	205:235	AGU is a lysosomal storage disease in which asparagine-linked glycopeptides accumulate to particularly high concentrations in liver, spleen and thyroid of affected individuals.
1281977	8	62	theme	-PAGE	1255:1259	arg1	gels					1261:1264	SDS/12.5%-PAGE gels	1246:1264	SDS/12.5%-PAGE gels	1246:1264	The purified enzyme protein ran at a 'native' molecular mass of 56 kDa in SDS/12.5%-PAGE gels, and the enzyme activity could be quantitatively recovered at this molecular mass by using gel slices as enzyme source in the assay.
1281977	11	63	theme	non-identical	1843:1855	arg1	polypeptides					1857:1868	two non-identical polypeptides	1839:1868	two non-identical polypeptides	1839:1868	These studies indicate that human liver aspartylglucosaminidase is composed of two non-identical polypeptides, each of which is glycosylated.
1281977	12	64	theme	amino	2010:2014	arg1	acids					2016:2020	the first 21, 26 and 22 amino acids	1986:2020	the first 21, 26 and 22 amino acids respectively	1986:2033	The N-termini of alpha,beta and beta 1 were directly accessible for sequencing, and the first 21, 26 and 22 amino acids respectively were identified.
1281977	11	65	theme	liver	1794:1798	arg1	aspartylglucosaminidase					1800:1822	human liver aspartylglucosaminidase	1788:1822	human liver aspartylglucosaminidase	1788:1822	These studies indicate that human liver aspartylglucosaminidase is composed of two non-identical polypeptides, each of which is glycosylated.
1281977	10	66	theme	enzyme	1631:1636	arg1	Treatment					1603:1611	Treatment	1603:1611	Treatment of heat-denatured enzyme with N-glycosidase F	1603:1657	Treatment of heat-denatured enzyme with N-glycosidase F resulted in the following decreases in molecular mass; 24.6 to 23 kDa and 18.4 and 17.4 to 15.8 kDa.
1281977	10	67	theme	molecular	1698:1706	arg1	mass					1708:1711	molecular mass	1698:1711	molecular mass; 24.6 to 23 kDa and 18.4 and 17.4 to 15.8 kDa	1698:1757	Treatment of heat-denatured enzyme with N-glycosidase F resulted in the following decreases in molecular mass; 24.6 to 23 kDa and 18.4 and 17.4 to 15.8 kDa.
1281977	8	68	theme	SDS/12.5	1246:1253	arg1	%					1254:1254	%	1254:1254	%	1254:1254	The purified enzyme protein ran at a 'native' molecular mass of 56 kDa in SDS/12.5%-PAGE gels, and the enzyme activity could be quantitatively recovered at this molecular mass by using gel slices as enzyme source in the assay.
1281977	10	69	dep	23	1722:1723	arg1	to					1719:1720	to	1719:1720	to	1719:1720	Treatment of heat-denatured enzyme with N-glycosidase F resulted in the following decreases in molecular mass; 24.6 to 23 kDa and 18.4 and 17.4 to 15.8 kDa.
1281977	8	70	from	mass	1228:1231	arg1	gels					1261:1264	SDS/12.5%-PAGE gels	1246:1264	SDS/12.5%-PAGE gels	1246:1264	The purified enzyme protein ran at a 'native' molecular mass of 56 kDa in SDS/12.5%-PAGE gels, and the enzyme activity could be quantitatively recovered at this molecular mass by using gel slices as enzyme source in the assay.
1281977	9	71	dep	polypeptides	1501:1512	arg1	beta					1520:1523	beta	1520:1523	beta	1520:1523	After denaturation by boiling in SDS the 56 kDa protein was lost with the corresponding appearance of polypeptides alpha,beta and beta 1, lacking enzyme activity, at 24.6, 18.4 and 17.4 kDa respectively.
1281977	9	71	dep	polypeptides	1501:1512	arg1	alpha					1514:1518	alpha	1514:1518	alpha	1514:1518	After denaturation by boiling in SDS the 56 kDa protein was lost with the corresponding appearance of polypeptides alpha,beta and beta 1, lacking enzyme activity, at 24.6, 18.4 and 17.4 kDa respectively.
1281977	9	71	dep	polypeptides	1501:1512	arg1	beta					1529:1532	beta 1	1529:1534	beta 1	1529:1534	After denaturation by boiling in SDS the 56 kDa protein was lost with the corresponding appearance of polypeptides alpha,beta and beta 1, lacking enzyme activity, at 24.6, 18.4 and 17.4 kDa respectively.
1281977	9	71	dep	polypeptides	1501:1512	arg1	polypeptides					1501:1512	polypeptides alpha,beta and beta 1	1501:1534	polypeptides alpha,beta and beta 1	1501:1534	After denaturation by boiling in SDS the 56 kDa protein was lost with the corresponding appearance of polypeptides alpha,beta and beta 1, lacking enzyme activity, at 24.6, 18.4 and 17.4 kDa respectively.
1281977	1	72	from	aspartylglucosaminuria	94:115	arg1	members					131:137	four members	126:137	four members of a Canadian family	126:158	We have recently diagnosed aspartylglucosaminuria (AGU) in four members of a Canadian family.
1281977	2	73	link	asparagine-linked	205:221	arg1	glycopeptides					223:235	asparagine-linked glycopeptides	205:235	asparagine-linked glycopeptides	205:235	AGU is a lysosomal storage disease in which asparagine-linked glycopeptides accumulate to particularly high concentrations in liver, spleen and thyroid of affected individuals.
1281977	3	74	theme	lesser	340:345	arg1	accumulation					347:358	A lesser accumulation	338:358	A lesser accumulation of these glycopeptides	338:381	A lesser accumulation of these glycopeptides is seen in the kidney and brain, and they are also excreted in the urine.
1281977	2	75	theme	storage	180:186	arg1	disease					188:194	a lysosomal storage disease	168:194	a lysosomal storage disease in which asparagine-linked glycopeptides accumulate to particularly high concentrations in liver, spleen and thyroid of affected individuals	168:335	AGU is a lysosomal storage disease in which asparagine-linked glycopeptides accumulate to particularly high concentrations in liver, spleen and thyroid of affected individuals.
1281977	2	75	theme	storage	180:186	arg1	AGU					161:163	AGU	161:163	AGU	161:163	AGU is a lysosomal storage disease in which asparagine-linked glycopeptides accumulate to particularly high concentrations in liver, spleen and thyroid of affected individuals.
1281977	2	76	theme	high	264:267	arg1	concentrations					269:282	particularly high concentrations	251:282	particularly high concentrations in liver, spleen and thyroid of affected individuals	251:335	AGU is a lysosomal storage disease in which asparagine-linked glycopeptides accumulate to particularly high concentrations in liver, spleen and thyroid of affected individuals.
1281977	10	77	with	Treatment	1603:1611	arg1	F					1657:1657	N-glycosidase F	1643:1657	N-glycosidase F	1643:1657	Treatment of heat-denatured enzyme with N-glycosidase F resulted in the following decreases in molecular mass; 24.6 to 23 kDa and 18.4 and 17.4 to 15.8 kDa.
1281977	8	78	theme	gel	1357:1359	arg1	slices					1361:1366	gel slices	1357:1366	gel slices	1357:1366	The purified enzyme protein ran at a 'native' molecular mass of 56 kDa in SDS/12.5%-PAGE gels, and the enzyme activity could be quantitatively recovered at this molecular mass by using gel slices as enzyme source in the assay.
1281977	9	79	theme	polypeptides	1501:1512	arg1	appearance					1487:1496	the corresponding appearance	1469:1496	the corresponding appearance of polypeptides alpha,beta and beta 1	1469:1534	After denaturation by boiling in SDS the 56 kDa protein was lost with the corresponding appearance of polypeptides alpha,beta and beta 1, lacking enzyme activity, at 24.6, 18.4 and 17.4 kDa respectively.
1281977	4	80	theme	N-acetylglucosamine	643:661	arg1	linkages					663:670	N-acetylglucosamine linkages	643:670	N-acetylglucosamine linkages of glycoproteins and glycopeptides	643:705	The altered metabolism in AGU results from a deficiency of the enzyme aspartylglucosaminidase (1-aspartamido-beta-N-acetylglucosamine amidohydrolase), which hydrolyses the asparagine to N-acetylglucosamine linkages of glycoproteins and glycopeptides.
1281977	6	81	from	fractionation	885:897	arg1	DEAE-Sepharose					948:961	DEAE-Sepharose	948:961	DEAE-Sepharose	948:961	The enzyme has been purified to homogeneity by using heat treatment, (NH4)2SO4 fractionation, and chromatography on concanavalin A-Sepharose, DEAE-Sepharose, sulphopropyl-Sephadex, hydroxyapatite, DEAE-cellulose and Sephadex G-100.
1281977	6	81	from	fractionation	885:897	arg1	DEAE-cellulose					1003:1016	DEAE-cellulose	1003:1016	DEAE-cellulose	1003:1016	The enzyme has been purified to homogeneity by using heat treatment, (NH4)2SO4 fractionation, and chromatography on concanavalin A-Sepharose, DEAE-Sepharose, sulphopropyl-Sephadex, hydroxyapatite, DEAE-cellulose and Sephadex G-100.
1281977	6	81	from	fractionation	885:897	arg1	G-100					1031:1035	Sephadex G-100	1022:1035	Sephadex G-100	1022:1035	The enzyme has been purified to homogeneity by using heat treatment, (NH4)2SO4 fractionation, and chromatography on concanavalin A-Sepharose, DEAE-Sepharose, sulphopropyl-Sephadex, hydroxyapatite, DEAE-cellulose and Sephadex G-100.
1281977	6	81	from	fractionation	885:897	arg1	sulphopropyl-Sephadex					964:984	sulphopropyl-Sephadex	964:984	sulphopropyl-Sephadex	964:984	The enzyme has been purified to homogeneity by using heat treatment, (NH4)2SO4 fractionation, and chromatography on concanavalin A-Sepharose, DEAE-Sepharose, sulphopropyl-Sephadex, hydroxyapatite, DEAE-cellulose and Sephadex G-100.
1281977	6	81	from	fractionation	885:897	arg1	hydroxyapatite					987:1000	hydroxyapatite	987:1000	hydroxyapatite	987:1000	The enzyme has been purified to homogeneity by using heat treatment, (NH4)2SO4 fractionation, and chromatography on concanavalin A-Sepharose, DEAE-Sepharose, sulphopropyl-Sephadex, hydroxyapatite, DEAE-cellulose and Sephadex G-100.
1281977	6	81	from	fractionation	885:897	arg1	A-Sepharose					935:945	concanavalin A-Sepharose	922:945	concanavalin A-Sepharose	922:945	The enzyme has been purified to homogeneity by using heat treatment, (NH4)2SO4 fractionation, and chromatography on concanavalin A-Sepharose, DEAE-Sepharose, sulphopropyl-Sephadex, hydroxyapatite, DEAE-cellulose and Sephadex G-100.
1281977	10	82	from	decreases	1685:1693	arg1	mass					1708:1711	molecular mass	1698:1711	molecular mass; 24.6 to 23 kDa and 18.4 and 17.4 to 15.8 kDa	1698:1757	Treatment of heat-denatured enzyme with N-glycosidase F resulted in the following decreases in molecular mass; 24.6 to 23 kDa and 18.4 and 17.4 to 15.8 kDa.
1281977	1	83	theme	Canadian	144:151	arg1	family					153:158	a Canadian family	142:158	a Canadian family	142:158	We have recently diagnosed aspartylglucosaminuria (AGU) in four members of a Canadian family.
1281977	10	84	theme	heat-denatured	1616:1629	arg1	enzyme					1631:1636	heat-denatured enzyme	1616:1636	heat-denatured enzyme	1616:1636	Treatment of heat-denatured enzyme with N-glycosidase F resulted in the following decreases in molecular mass; 24.6 to 23 kDa and 18.4 and 17.4 to 15.8 kDa.
8846222	5	0	with	enzyme	690:695	arg1	optimum					727:733	an exceptionally high pH optimum	702:733	an exceptionally high pH optimum	702:733	On the basis of the structure of the enzyme-product complex we present a catalytic mechanism for this lysosomal enzyme with an exceptionally high pH optimum.
8846222	4	1	theme	active	565:570	arg1	site					572:575	the funnel-shaped active site	547:575	the funnel-shaped active site	547:575	The catalytically essential residue, the N-terminal threonine of the beta-chain is situated in the deep pocket of the funnel-shaped active site.
8846222	4	2	theme	essential	451:459	arg1	threonine					485:493	the N-terminal threonine	470:493	the N-terminal threonine of the beta-chain	470:511	The catalytically essential residue, the N-terminal threonine of the beta-chain is situated in the deep pocket of the funnel-shaped active site.
8846222	4	2	theme	essential	451:459	arg1	residue					461:467	The catalytically essential residue	433:467	The catalytically essential residue	433:467	The catalytically essential residue, the N-terminal threonine of the beta-chain is situated in the deep pocket of the funnel-shaped active site.
8846222	4	2	theme	essential	451:459	arg1	situated					516:523	situated	516:523	situated	516:523	The catalytically essential residue, the N-terminal threonine of the beta-chain is situated in the deep pocket of the funnel-shaped active site.
8846222	4	3	theme	funnel-shaped	551:563	arg1	site					572:575	the funnel-shaped active site	547:575	the funnel-shaped active site	547:575	The catalytically essential residue, the N-terminal threonine of the beta-chain is situated in the deep pocket of the funnel-shaped active site.
8846222	1	4	theme	high	76:79	arg1	structure					100:108	The high resolution crystal structure	72:108	The high resolution crystal structure of human lysosomal aspartylglucosaminidase (AGA)	72:157	The high resolution crystal structure of human lysosomal aspartylglucosaminidase (AGA) has been determined.
8846222	3	5	theme	final	399:403	arg1	structure					422:430	the final heterotetrameric structure	395:430	the final heterotetrameric structure	395:430	Two alpha- and beta-chains are found to pack together forming the final heterotetrameric structure.
8846222	1	6	theme	resolution	81:90	arg1	structure					100:108	The high resolution crystal structure	72:108	The high resolution crystal structure of human lysosomal aspartylglucosaminidase (AGA)	72:157	The high resolution crystal structure of human lysosomal aspartylglucosaminidase (AGA) has been determined.
8846222	4	7	from	pocket	537:542	arg1	residue					461:467	The catalytically essential residue	433:467	The catalytically essential residue	433:467	The catalytically essential residue, the N-terminal threonine of the beta-chain is situated in the deep pocket of the funnel-shaped active site.
8846222	4	7	from	pocket	537:542	arg1	situated					516:523	situated	516:523	situated	516:523	The catalytically essential residue, the N-terminal threonine of the beta-chain is situated in the deep pocket of the funnel-shaped active site.
8846222	5	8	theme	catalytic	651:659	arg1	mechanism					661:669	a catalytic mechanism	649:669	a catalytic mechanism for this lysosomal enzyme with an exceptionally high pH optimum	649:733	On the basis of the structure of the enzyme-product complex we present a catalytic mechanism for this lysosomal enzyme with an exceptionally high pH optimum.
8846222	1	9	theme	crystal	92:98	arg1	structure					100:108	The high resolution crystal structure	72:108	The high resolution crystal structure of human lysosomal aspartylglucosaminidase (AGA)	72:157	The high resolution crystal structure of human lysosomal aspartylglucosaminidase (AGA) has been determined.
8846222	5	10	dep	structure	598:606	arg1	the					581:583	the	581:583	the	581:583	On the basis of the structure of the enzyme-product complex we present a catalytic mechanism for this lysosomal enzyme with an exceptionally high pH optimum.
8846222	5	10	dep	structure	598:606	arg1	basis					585:589	basis	585:589	basis	585:589	On the basis of the structure of the enzyme-product complex we present a catalytic mechanism for this lysosomal enzyme with an exceptionally high pH optimum.
8846222	2	11	theme	polypeptide	229:239	arg1	precursor					241:249	a single polypeptide precursor	220:249	a single polypeptide precursor	220:249	This lysosomal enzyme is synthesized as a single polypeptide precursor, which is immediately post-translationally cleaved into alpha- and beta-subunits.
8846222	2	11	theme	polypeptide	229:239	arg1	enzyme					195:200	This lysosomal enzyme	180:200	This lysosomal enzyme	180:200	This lysosomal enzyme is synthesized as a single polypeptide precursor, which is immediately post-translationally cleaved into alpha- and beta-subunits.
8846222	4	12	theme	deep	532:535	arg1	pocket					537:542	the deep pocket	528:542	the deep pocket of the funnel-shaped active site	528:575	The catalytically essential residue, the N-terminal threonine of the beta-chain is situated in the deep pocket of the funnel-shaped active site.
8846222	0	13	theme	Three-dimensional	0:16	arg1	structure					18:26	Three-dimensional structure	0:26	Three-dimensional structure of human lysosomal aspartylglucosaminidase	0:69	Three-dimensional structure of human lysosomal aspartylglucosaminidase.
8846222	5	14	theme	lysosomal	680:688	arg1	enzyme					690:695	this lysosomal enzyme	675:695	this lysosomal enzyme with an exceptionally high pH optimum	675:733	On the basis of the structure of the enzyme-product complex we present a catalytic mechanism for this lysosomal enzyme with an exceptionally high pH optimum.
8846222	5	15	theme	enzyme-product	615:628	arg1	complex					630:636	the enzyme-product complex	611:636	the enzyme-product complex	611:636	On the basis of the structure of the enzyme-product complex we present a catalytic mechanism for this lysosomal enzyme with an exceptionally high pH optimum.
8846222	1	16	theme	human	113:117	arg1	AGA					154:156	AGA	154:156	AGA	154:156	The high resolution crystal structure of human lysosomal aspartylglucosaminidase (AGA) has been determined.
8846222	1	16	theme	human	113:117	arg1	aspartylglucosaminidase					129:151	human lysosomal aspartylglucosaminidase	113:151	human lysosomal aspartylglucosaminidase (AGA)	113:157	The high resolution crystal structure of human lysosomal aspartylglucosaminidase (AGA) has been determined.
8846222	3	17	theme	heterotetrameric	405:420	arg1	structure					422:430	the final heterotetrameric structure	395:430	the final heterotetrameric structure	395:430	Two alpha- and beta-chains are found to pack together forming the final heterotetrameric structure.
8846222	6	18	theme	mutations	835:843	arg1	consequences					813:824	the structural consequences	798:824	the structural consequences of human mutations resulting in aspartylglucosaminuria (AGU), a lysosomal storage disease	798:914	The three-dimensional structure also allows the prediction of the structural consequences of human mutations resulting in aspartylglucosaminuria (AGU), a lysosomal storage disease.
8846222	4	19	from	situated	516:523	arg1	pocket					537:542	the deep pocket	528:542	the deep pocket of the funnel-shaped active site	528:575	The catalytically essential residue, the N-terminal threonine of the beta-chain is situated in the deep pocket of the funnel-shaped active site.
8846222	5	20	theme	complex	630:636	arg1	structure					598:606	the structure	594:606	the structure of the enzyme-product complex	594:636	On the basis of the structure of the enzyme-product complex we present a catalytic mechanism for this lysosomal enzyme with an exceptionally high pH optimum.
8846222	1	21	theme	lysosomal	119:127	arg1	AGA					154:156	AGA	154:156	AGA	154:156	The high resolution crystal structure of human lysosomal aspartylglucosaminidase (AGA) has been determined.
8846222	1	21	theme	lysosomal	119:127	arg1	aspartylglucosaminidase					129:151	human lysosomal aspartylglucosaminidase	113:151	human lysosomal aspartylglucosaminidase (AGA)	113:157	The high resolution crystal structure of human lysosomal aspartylglucosaminidase (AGA) has been determined.
8846222	6	22	theme	storage	900:906	arg1	aspartylglucosaminuria					858:879	aspartylglucosaminuria	858:879	aspartylglucosaminuria (AGU)	858:885	The three-dimensional structure also allows the prediction of the structural consequences of human mutations resulting in aspartylglucosaminuria (AGU), a lysosomal storage disease.
8846222	6	22	theme	storage	900:906	arg1	disease					908:914	a lysosomal storage disease	888:914	a lysosomal storage disease	888:914	The three-dimensional structure also allows the prediction of the structural consequences of human mutations resulting in aspartylglucosaminuria (AGU), a lysosomal storage disease.
8846222	4	23	theme	beta-chain	502:511	arg1	threonine					485:493	the N-terminal threonine	470:493	the N-terminal threonine of the beta-chain	470:511	The catalytically essential residue, the N-terminal threonine of the beta-chain is situated in the deep pocket of the funnel-shaped active site.
8846222	4	23	theme	beta-chain	502:511	arg1	residue					461:467	The catalytically essential residue	433:467	The catalytically essential residue	433:467	The catalytically essential residue, the N-terminal threonine of the beta-chain is situated in the deep pocket of the funnel-shaped active site.
8846222	1	24	theme	aspartylglucosaminidase	129:151	arg1	structure					100:108	The high resolution crystal structure	72:108	The high resolution crystal structure of human lysosomal aspartylglucosaminidase (AGA)	72:157	The high resolution crystal structure of human lysosomal aspartylglucosaminidase (AGA) has been determined.
8846222	0	25	theme	aspartylglucosaminidase	47:69	arg1	structure					18:26	Three-dimensional structure	0:26	Three-dimensional structure of human lysosomal aspartylglucosaminidase	0:69	Three-dimensional structure of human lysosomal aspartylglucosaminidase.
8846222	0	26	theme	lysosomal	37:45	arg1	aspartylglucosaminidase					47:69	human lysosomal aspartylglucosaminidase	31:69	human lysosomal aspartylglucosaminidase	31:69	Three-dimensional structure of human lysosomal aspartylglucosaminidase.
8846222	0	27	theme	human	31:35	arg1	aspartylglucosaminidase					47:69	human lysosomal aspartylglucosaminidase	31:69	human lysosomal aspartylglucosaminidase	31:69	Three-dimensional structure of human lysosomal aspartylglucosaminidase.
8846222	4	28	theme	site	572:575	arg1	pocket					537:542	the deep pocket	528:542	the deep pocket of the funnel-shaped active site	528:575	The catalytically essential residue, the N-terminal threonine of the beta-chain is situated in the deep pocket of the funnel-shaped active site.
8846222	5	29	theme	high	719:722	arg1	optimum					727:733	an exceptionally high pH optimum	702:733	an exceptionally high pH optimum	702:733	On the basis of the structure of the enzyme-product complex we present a catalytic mechanism for this lysosomal enzyme with an exceptionally high pH optimum.
8846222	2	30	theme	lysosomal	185:193	arg1	precursor					241:249	a single polypeptide precursor	220:249	a single polypeptide precursor	220:249	This lysosomal enzyme is synthesized as a single polypeptide precursor, which is immediately post-translationally cleaved into alpha- and beta-subunits.
8846222	2	30	theme	lysosomal	185:193	arg1	enzyme					195:200	This lysosomal enzyme	180:200	This lysosomal enzyme	180:200	This lysosomal enzyme is synthesized as a single polypeptide precursor, which is immediately post-translationally cleaved into alpha- and beta-subunits.
8846222	6	31	theme	consequences	813:824	arg1	prediction					784:793	the prediction	780:793	the prediction of the structural consequences of human mutations resulting in aspartylglucosaminuria (AGU), a lysosomal storage disease	780:914	The three-dimensional structure also allows the prediction of the structural consequences of human mutations resulting in aspartylglucosaminuria (AGU), a lysosomal storage disease.
8846222	5	32	theme	pH	724:725	arg1	optimum					727:733	an exceptionally high pH optimum	702:733	an exceptionally high pH optimum	702:733	On the basis of the structure of the enzyme-product complex we present a catalytic mechanism for this lysosomal enzyme with an exceptionally high pH optimum.
8846222	4	33	theme	N-terminal	474:483	arg1	threonine					485:493	the N-terminal threonine	470:493	the N-terminal threonine of the beta-chain	470:511	The catalytically essential residue, the N-terminal threonine of the beta-chain is situated in the deep pocket of the funnel-shaped active site.
8846222	4	33	theme	N-terminal	474:483	arg1	residue					461:467	The catalytically essential residue	433:467	The catalytically essential residue	433:467	The catalytically essential residue, the N-terminal threonine of the beta-chain is situated in the deep pocket of the funnel-shaped active site.
8846222	6	34	theme	lysosomal	890:898	arg1	aspartylglucosaminuria					858:879	aspartylglucosaminuria	858:879	aspartylglucosaminuria (AGU)	858:885	The three-dimensional structure also allows the prediction of the structural consequences of human mutations resulting in aspartylglucosaminuria (AGU), a lysosomal storage disease.
8846222	6	34	theme	lysosomal	890:898	arg1	disease					908:914	a lysosomal storage disease	888:914	a lysosomal storage disease	888:914	The three-dimensional structure also allows the prediction of the structural consequences of human mutations resulting in aspartylglucosaminuria (AGU), a lysosomal storage disease.
8846222	6	35	theme	structural	802:811	arg1	consequences					813:824	the structural consequences	798:824	the structural consequences of human mutations resulting in aspartylglucosaminuria (AGU), a lysosomal storage disease	798:914	The three-dimensional structure also allows the prediction of the structural consequences of human mutations resulting in aspartylglucosaminuria (AGU), a lysosomal storage disease.
8846222	6	36	theme	human	829:833	arg1	mutations					835:843	human mutations	829:843	human mutations resulting in aspartylglucosaminuria (AGU), a lysosomal storage disease	829:914	The three-dimensional structure also allows the prediction of the structural consequences of human mutations resulting in aspartylglucosaminuria (AGU), a lysosomal storage disease.
8846222	2	37	theme	single	222:227	arg1	precursor					241:249	a single polypeptide precursor	220:249	a single polypeptide precursor	220:249	This lysosomal enzyme is synthesized as a single polypeptide precursor, which is immediately post-translationally cleaved into alpha- and beta-subunits.
8846222	2	37	theme	single	222:227	arg1	enzyme					195:200	This lysosomal enzyme	180:200	This lysosomal enzyme	180:200	This lysosomal enzyme is synthesized as a single polypeptide precursor, which is immediately post-translationally cleaved into alpha- and beta-subunits.
8846222	6	38	theme	three-dimensional	740:756	arg1	structure					758:766	The three-dimensional structure	736:766	The three-dimensional structure	736:766	The three-dimensional structure also allows the prediction of the structural consequences of human mutations resulting in aspartylglucosaminuria (AGU), a lysosomal storage disease.
2401370	6	0	theme	predicted	645:653	arg1	site					655:658	the predicted site	641:658	the predicted site where cleavage occurs	641:680	A charge enriched region is present at the predicted site where cleavage occurs.
2401370	4	1	theme	human	445:449	arg1	enzyme					451:456	The human enzyme	441:456	The human enzyme	441:456	The human enzyme is encoded as a 34.6 kDa polypeptide that is post-translationally processed to generate two subunits of approx.
2401370	4	1	theme	human	445:449	arg1	polypeptide					483:493	a 34.6 kDa polypeptide	472:493	a 34.6 kDa polypeptide that is post-translationally processed to generate two subunits of approx	472:567	The human enzyme is encoded as a 34.6 kDa polypeptide that is post-translationally processed to generate two subunits of approx.
2401370	3	2	theme	deduced	312:318	arg1	sequence					331:338	The deduced amino acid sequence	308:338	The deduced amino acid sequence from the human clone	308:359	The deduced amino acid sequence from the human clone showed sequence identity to both the alpha and beta subunits of the rat enzyme.
2401370	4	3	theme	34.6	474:477	arg1	kDa					479:481	kDa	479:481	kDa	479:481	The human enzyme is encoded as a 34.6 kDa polypeptide that is post-translationally processed to generate two subunits of approx.
2401370	2	4	theme	liver	273:277	arg1	sequences					297:305	rat liver asparaginase gene sequences	269:305	rat liver asparaginase gene sequences	269:305	We have isolated a full-length cDNA (HPAsn.6) for human placenta glycosylasparaginase using a 221-bp PCR amplified fragment containing rat liver asparaginase gene sequences.
2401370	7	5	theme	human	797:801	arg1	enzyme					803:808	the human enzyme	793:808	the human enzyme	793:808	Using polyclonal antibodies against the alpha and beta subunits of rat liver asparaginase, we have shown that the human enzyme is similar in structure to the rat enzyme.
2401370	7	5	theme	human	797:801	arg1	similar					813:819	similar	813:819	similar	813:819	Using polyclonal antibodies against the alpha and beta subunits of rat liver asparaginase, we have shown that the human enzyme is similar in structure to the rat enzyme.
2401370	4	6	theme	approx	562:567	arg1	subunits					550:557	two subunits	546:557	two subunits of approx	546:567	The human enzyme is encoded as a 34.6 kDa polypeptide that is post-translationally processed to generate two subunits of approx.
2401370	3	7	theme	human	349:353	arg1	clone					355:359	the human clone	345:359	the human clone	345:359	The deduced amino acid sequence from the human clone showed sequence identity to both the alpha and beta subunits of the rat enzyme.
2401370	3	8	from	clone	355:359	arg1	sequence					331:338	The deduced amino acid sequence	308:338	The deduced amino acid sequence from the human clone	308:359	The deduced amino acid sequence from the human clone showed sequence identity to both the alpha and beta subunits of the rat enzyme.
2401370	2	9	theme	rat	269:271	arg1	liver					273:277	rat liver	269:277	rat liver asparaginase gene sequences	269:305	We have isolated a full-length cDNA (HPAsn.6) for human placenta glycosylasparaginase using a 221-bp PCR amplified fragment containing rat liver asparaginase gene sequences.
2401370	3	10	theme	sequence	368:375	arg1	identity					377:384	sequence identity	368:384	sequence identity	368:384	The deduced amino acid sequence from the human clone showed sequence identity to both the alpha and beta subunits of the rat enzyme.
2401370	1	11	theme	single	74:79	arg1	gene					81:84	A single gene	72:84	A single gene	72:84	A single gene encodes the subunits of this lysosomal amidase.
2401370	1	11	theme	single	74:79	arg1	subunits					98:105	the subunits	94:105	the subunits of this lysosomal amidase	94:131	A single gene encodes the subunits of this lysosomal amidase.
2401370	6	12	attach	present	630:636	arg2	present					630:636	present	630:636	present	630:636	A charge enriched region is present at the predicted site where cleavage occurs.
2401370	6	12	attach	present	630:636	arg2	region					620:625	A charge enriched region	602:625	A charge enriched region	602:625	A charge enriched region is present at the predicted site where cleavage occurs.
2401370	6	12	attach	present	630:636	arg1	site					655:658	the predicted site	641:658	the predicted site where cleavage occurs	641:680	A charge enriched region is present at the predicted site where cleavage occurs.
2401370	7	13	theme	asparaginase	760:771	arg1	subunits					738:745	the alpha and beta subunits	719:745	the alpha and beta subunits of rat liver asparaginase	719:771	Using polyclonal antibodies against the alpha and beta subunits of rat liver asparaginase, we have shown that the human enzyme is similar in structure to the rat enzyme.
2401370	3	14	theme	beta	408:411	arg1	subunits					413:420	both the alpha and beta subunits	389:420	subunits	413:420	The deduced amino acid sequence from the human clone showed sequence identity to both the alpha and beta subunits of the rat enzyme.
2401370	2	15	contain	containing	258:267	arg1	fragment					249:256	a 221-bp PCR amplified fragment	226:256	a 221-bp PCR amplified fragment containing rat liver asparaginase gene sequences	226:305	We have isolated a full-length cDNA (HPAsn.6) for human placenta glycosylasparaginase using a 221-bp PCR amplified fragment containing rat liver asparaginase gene sequences.
2401370	2	15	contain	containing	258:267	arg2	sequences					297:305	rat liver asparaginase gene sequences	269:305	rat liver asparaginase gene sequences	269:305	We have isolated a full-length cDNA (HPAsn.6) for human placenta glycosylasparaginase using a 221-bp PCR amplified fragment containing rat liver asparaginase gene sequences.
2401370	7	16	theme	rat	841:843	arg1	enzyme					845:850	the rat enzyme	837:850	the rat enzyme	837:850	Using polyclonal antibodies against the alpha and beta subunits of rat liver asparaginase, we have shown that the human enzyme is similar in structure to the rat enzyme.
2401370	2	17	theme	gene	292:295	arg1	sequences					297:305	rat liver asparaginase gene sequences	269:305	rat liver asparaginase gene sequences	269:305	We have isolated a full-length cDNA (HPAsn.6) for human placenta glycosylasparaginase using a 221-bp PCR amplified fragment containing rat liver asparaginase gene sequences.
2401370	6	18	theme	enriched	611:618	arg1	present					630:636	present	630:636	present	630:636	A charge enriched region is present at the predicted site where cleavage occurs.
2401370	6	18	theme	enriched	611:618	arg1	region					620:625	A charge enriched region	602:625	A charge enriched region	602:625	A charge enriched region is present at the predicted site where cleavage occurs.
2401370	3	19	theme	enzyme	433:438	arg1	subunits					413:420	both the alpha and beta subunits	389:420	subunits	413:420	The deduced amino acid sequence from the human clone showed sequence identity to both the alpha and beta subunits of the rat enzyme.
2401370	0	20	theme	sequence	12:19	arg1	analysis					21:28	sequence analysis	12:28	sequence analysis	12:28	Cloning and sequence analysis of a cDNA for human glycosylasparaginase.
2401370	2	21	theme	asparaginase	279:290	arg1	sequences					297:305	rat liver asparaginase gene sequences	269:305	rat liver asparaginase gene sequences	269:305	We have isolated a full-length cDNA (HPAsn.6) for human placenta glycosylasparaginase using a 221-bp PCR amplified fragment containing rat liver asparaginase gene sequences.
2401370	6	22	theme	charge	604:609	arg1	present					630:636	present	630:636	present	630:636	A charge enriched region is present at the predicted site where cleavage occurs.
2401370	6	22	theme	charge	604:609	arg1	region					620:625	A charge enriched region	602:625	A charge enriched region	602:625	A charge enriched region is present at the predicted site where cleavage occurs.
2401370	6	23	from	site	655:658	arg1	present					630:636	present	630:636	present	630:636	A charge enriched region is present at the predicted site where cleavage occurs.
2401370	6	23	from	site	655:658	arg1	region					620:625	A charge enriched region	602:625	A charge enriched region	602:625	A charge enriched region is present at the predicted site where cleavage occurs.
2401370	7	24	theme	beta	733:736	arg1	subunits					738:745	the alpha and beta subunits	719:745	the alpha and beta subunits of rat liver asparaginase	719:771	Using polyclonal antibodies against the alpha and beta subunits of rat liver asparaginase, we have shown that the human enzyme is similar in structure to the rat enzyme.
2401370	2	25	theme	full-length	153:163	arg1	cDNA					165:168	a full-length cDNA (HPAsn.6)	151:178	a full-length cDNA (HPAsn.6) for human placenta glycosylasparaginase	151:218	We have isolated a full-length cDNA (HPAsn.6) for human placenta glycosylasparaginase using a 221-bp PCR amplified fragment containing rat liver asparaginase gene sequences.
2401370	7	26	theme	liver	754:758	arg1	asparaginase					760:771	rat liver asparaginase	750:771	rat liver asparaginase	750:771	Using polyclonal antibodies against the alpha and beta subunits of rat liver asparaginase, we have shown that the human enzyme is similar in structure to the rat enzyme.
2401370	3	27	theme	alpha	398:402	arg1	subunits					413:420	both the alpha and beta subunits	389:420	subunits	413:420	The deduced amino acid sequence from the human clone showed sequence identity to both the alpha and beta subunits of the rat enzyme.
2401370	7	28	from	similar	813:819	arg1	structure					824:832	structure	824:832	structure	824:832	Using polyclonal antibodies against the alpha and beta subunits of rat liver asparaginase, we have shown that the human enzyme is similar in structure to the rat enzyme.
2401370	3	29	theme	rat	429:431	arg1	enzyme					433:438	the rat enzyme	425:438	the rat enzyme	425:438	The deduced amino acid sequence from the human clone showed sequence identity to both the alpha and beta subunits of the rat enzyme.
2401370	4	30	theme	kDa	479:481	arg1	enzyme					451:456	The human enzyme	441:456	The human enzyme	441:456	The human enzyme is encoded as a 34.6 kDa polypeptide that is post-translationally processed to generate two subunits of approx.
2401370	4	30	theme	kDa	479:481	arg1	polypeptide					483:493	a 34.6 kDa polypeptide	472:493	a 34.6 kDa polypeptide that is post-translationally processed to generate two subunits of approx	472:567	The human enzyme is encoded as a 34.6 kDa polypeptide that is post-translationally processed to generate two subunits of approx.
2401370	3	31	theme	acid	326:329	arg1	sequence					331:338	The deduced amino acid sequence	308:338	The deduced amino acid sequence from the human clone	308:359	The deduced amino acid sequence from the human clone showed sequence identity to both the alpha and beta subunits of the rat enzyme.
2401370	2	32	theme	placenta	190:197	arg1	glycosylasparaginase					199:218	human placenta glycosylasparaginase	184:218	human placenta glycosylasparaginase	184:218	We have isolated a full-length cDNA (HPAsn.6) for human placenta glycosylasparaginase using a 221-bp PCR amplified fragment containing rat liver asparaginase gene sequences.
2401370	0	33	theme	cDNA	35:38	arg1	Cloning					0:6	Cloning	0:6	Cloning	0:6	Cloning and sequence analysis of a cDNA for human glycosylasparaginase.
2401370	0	33	theme	cDNA	35:38	arg1	analysis					21:28	sequence analysis	12:28	sequence analysis	12:28	Cloning and sequence analysis of a cDNA for human glycosylasparaginase.
2401370	2	34	theme	human	184:188	arg1	glycosylasparaginase					199:218	human placenta glycosylasparaginase	184:218	human placenta glycosylasparaginase	184:218	We have isolated a full-length cDNA (HPAsn.6) for human placenta glycosylasparaginase using a 221-bp PCR amplified fragment containing rat liver asparaginase gene sequences.
2401370	2	35	theme	amplified	239:247	arg1	fragment					249:256	a 221-bp PCR amplified fragment	226:256	a 221-bp PCR amplified fragment containing rat liver asparaginase gene sequences	226:305	We have isolated a full-length cDNA (HPAsn.6) for human placenta glycosylasparaginase using a 221-bp PCR amplified fragment containing rat liver asparaginase gene sequences.
2401370	7	36	from	structure	824:832	arg1	enzyme					803:808	the human enzyme	793:808	the human enzyme	793:808	Using polyclonal antibodies against the alpha and beta subunits of rat liver asparaginase, we have shown that the human enzyme is similar in structure to the rat enzyme.
2401370	7	36	from	structure	824:832	arg1	similar					813:819	similar	813:819	similar	813:819	Using polyclonal antibodies against the alpha and beta subunits of rat liver asparaginase, we have shown that the human enzyme is similar in structure to the rat enzyme.
2401370	2	37	theme	PCR	235:237	arg1	fragment					249:256	a 221-bp PCR amplified fragment	226:256	a 221-bp PCR amplified fragment containing rat liver asparaginase gene sequences	226:305	We have isolated a full-length cDNA (HPAsn.6) for human placenta glycosylasparaginase using a 221-bp PCR amplified fragment containing rat liver asparaginase gene sequences.
2401370	1	38	theme	lysosomal	115:123	arg1	amidase					125:131	this lysosomal amidase	110:131	this lysosomal amidase	110:131	A single gene encodes the subunits of this lysosomal amidase.
2401370	7	39	theme	rat	750:752	arg1	asparaginase					760:771	rat liver asparaginase	750:771	rat liver asparaginase	750:771	Using polyclonal antibodies against the alpha and beta subunits of rat liver asparaginase, we have shown that the human enzyme is similar in structure to the rat enzyme.
2401370	7	40	theme	polyclonal	689:698	arg1	antibodies					700:709	polyclonal antibodies	689:709	polyclonal antibodies against the alpha and beta subunits of rat liver asparaginase	689:771	Using polyclonal antibodies against the alpha and beta subunits of rat liver asparaginase, we have shown that the human enzyme is similar in structure to the rat enzyme.
2401370	3	41	theme	amino	320:324	arg1	sequence					331:338	The deduced amino acid sequence	308:338	The deduced amino acid sequence from the human clone	308:359	The deduced amino acid sequence from the human clone showed sequence identity to both the alpha and beta subunits of the rat enzyme.
2401370	2	42	theme	221-bp	228:233	arg1	fragment					249:256	a 221-bp PCR amplified fragment	226:256	a 221-bp PCR amplified fragment containing rat liver asparaginase gene sequences	226:305	We have isolated a full-length cDNA (HPAsn.6) for human placenta glycosylasparaginase using a 221-bp PCR amplified fragment containing rat liver asparaginase gene sequences.
2401370	1	43	theme	amidase	125:131	arg1	gene					81:84	A single gene	72:84	A single gene	72:84	A single gene encodes the subunits of this lysosomal amidase.
2401370	1	43	theme	amidase	125:131	arg1	subunits					98:105	the subunits	94:105	the subunits of this lysosomal amidase	94:131	A single gene encodes the subunits of this lysosomal amidase.
2401370	0	44	theme	human	44:48	arg1	glycosylasparaginase					50:69	human glycosylasparaginase	44:69	human glycosylasparaginase	44:69	Cloning and sequence analysis of a cDNA for human glycosylasparaginase.
2401370	6	45	located	present	630:636	arg2	present					630:636	present	630:636	present	630:636	A charge enriched region is present at the predicted site where cleavage occurs.
2401370	6	45	located	present	630:636	arg2	region					620:625	A charge enriched region	602:625	A charge enriched region	602:625	A charge enriched region is present at the predicted site where cleavage occurs.
2401370	6	45	located	present	630:636	arg1	site					655:658	the predicted site	641:658	the predicted site where cleavage occurs	641:680	A charge enriched region is present at the predicted site where cleavage occurs.
2401370	5	46	dep	kDa	597:599	arg1	15					587:588	15	587:588	15	587:588	19.5 (alpha) and 15 (beta) kDa.
2401370	5	46	dep	kDa	597:599	arg1	19.5					570:573	19.5	570:573	19.5	570:573	19.5 (alpha) and 15 (beta) kDa.
2401370	5	46	dep	kDa	597:599	arg1	beta					591:594	beta	591:594	beta	591:594	19.5 (alpha) and 15 (beta) kDa.
2401370	5	46	dep	kDa	597:599	arg1	alpha					576:580	alpha	576:580	alpha	576:580	19.5 (alpha) and 15 (beta) kDa.
2401370	7	47	theme	alpha	723:727	arg1	subunits					738:745	the alpha and beta subunits	719:745	the alpha and beta subunits of rat liver asparaginase	719:771	Using polyclonal antibodies against the alpha and beta subunits of rat liver asparaginase, we have shown that the human enzyme is similar in structure to the rat enzyme.
15723809	4	0	from	pocket	794:799	arg1	conformation					806:817	a conformation	804:817	a conformation that closely mimics that of the alkyl chain in the CD1a-sulfatide structure	804:893	Remarkably, the cyclized lysine branch of the peptide moiety lies in the shallow F' pocket in a conformation that closely mimics that of the alkyl chain in the CD1a-sulfatide structure.
15723809	5	1	theme	lipopeptide	1020:1030	arg1	moiety					1006:1011	the peptide moiety	994:1011	the peptide moiety of the lipopeptide	994:1030	Thus, this structural study illustrates how a single chain lipid can be presented by CD1 and that the peptide moiety of the lipopeptide is recognized by the TCR.
15723809	4	2	theme	F	791:791	arg1	pocket					794:799	the shallow F' pocket	779:799	the shallow F' pocket in a conformation that closely mimics that of the alkyl chain in the CD1a-sulfatide structure	779:893	Remarkably, the cyclized lysine branch of the peptide moiety lies in the shallow F' pocket in a conformation that closely mimics that of the alkyl chain in the CD1a-sulfatide structure.
15723809	2	3	theme	T	290:290	arg1	cells					292:296	CD1a-restricted T cells	274:296	CD1a-restricted T cells	274:296	We demonstrate here that CD1a-restricted T cells can discriminate the peptide component of didehydroxymycobactin lipopeptides.
15723809	1	4	theme	dendritic	105:113	arg1	DCs					122:124	DCs	122:124	DCs	122:124	CD1a is expressed on Langerhans cells (LCs) and dendritic cells (DCs), where it mediates T cell recognition of glycolipid and lipopeptide antigens that contain either one or two alkyl chains.
15723809	1	4	theme	dendritic	105:113	arg1	cells					115:119	dendritic cells	105:119	dendritic cells (DCs)	105:125	CD1a is expressed on Langerhans cells (LCs) and dendritic cells (DCs), where it mediates T cell recognition of glycolipid and lipopeptide antigens that contain either one or two alkyl chains.
15723809	4	5	theme	alkyl	851:855	arg1	chain					857:861	the alkyl chain	847:861	the alkyl chain	847:861	Remarkably, the cyclized lysine branch of the peptide moiety lies in the shallow F' pocket in a conformation that closely mimics that of the alkyl chain in the CD1a-sulfatide structure.
15723809	3	6	theme	CD1a	677:680	arg1	surface					666:672	the outer, alpha-helical surface	641:672	surface	666:672	Structure analysis of CD1a cocrystallized with a synthetic mycobactin lipopeptide at 2.8 A resolution further reveals that the single alkyl chain is inserted deep within the A' pocket of the groove, whereas its two peptidic branches protrude along the F' pocket to the outer, alpha-helical surface of CD1a for recognition by the TCR.
15723809	3	7	theme	alpha-helical	652:664	arg1	surface					666:672	the outer, alpha-helical surface	641:672	surface	666:672	Structure analysis of CD1a cocrystallized with a synthetic mycobactin lipopeptide at 2.8 A resolution further reveals that the single alkyl chain is inserted deep within the A' pocket of the groove, whereas its two peptidic branches protrude along the F' pocket to the outer, alpha-helical surface of CD1a for recognition by the TCR.
15723809	2	8	theme	lipopeptides	362:373	arg1	component					327:335	the peptide component	315:335	the peptide component of didehydroxymycobactin lipopeptides	315:373	We demonstrate here that CD1a-restricted T cells can discriminate the peptide component of didehydroxymycobactin lipopeptides.
15723809	4	9	theme	shallow	783:789	arg1	pocket					794:799	the shallow F' pocket	779:799	the shallow F' pocket in a conformation that closely mimics that of the alkyl chain in the CD1a-sulfatide structure	779:893	Remarkably, the cyclized lysine branch of the peptide moiety lies in the shallow F' pocket in a conformation that closely mimics that of the alkyl chain in the CD1a-sulfatide structure.
15723809	3	10	from	resolution	467:476	arg1	lipopeptide					446:456	a synthetic mycobactin lipopeptide	423:456	a synthetic mycobactin lipopeptide at 2.8 A resolution	423:476	Structure analysis of CD1a cocrystallized with a synthetic mycobactin lipopeptide at 2.8 A resolution further reveals that the single alkyl chain is inserted deep within the A' pocket of the groove, whereas its two peptidic branches protrude along the F' pocket to the outer, alpha-helical surface of CD1a for recognition by the TCR.
15723809	1	11	theme	Langerhans	78:87	arg1	cells					89:93	Langerhans cells	78:93	Langerhans cells (LCs)	78:99	CD1a is expressed on Langerhans cells (LCs) and dendritic cells (DCs), where it mediates T cell recognition of glycolipid and lipopeptide antigens that contain either one or two alkyl chains.
15723809	1	11	theme	Langerhans	78:87	arg1	LCs					96:98	LCs	96:98	LCs	96:98	CD1a is expressed on Langerhans cells (LCs) and dendritic cells (DCs), where it mediates T cell recognition of glycolipid and lipopeptide antigens that contain either one or two alkyl chains.
15723809	2	12	theme	didehydroxymycobactin	340:360	arg1	lipopeptides					362:373	didehydroxymycobactin lipopeptides	340:373	didehydroxymycobactin lipopeptides	340:373	We demonstrate here that CD1a-restricted T cells can discriminate the peptide component of didehydroxymycobactin lipopeptides.
15723809	0	13	theme	Molecular	0:8	arg1	mechanism					10:18	Molecular mechanism	0:18	Molecular mechanism of lipopeptide presentation by CD1a	0:54	Molecular mechanism of lipopeptide presentation by CD1a.
15723809	1	14	theme	T	146:146	arg1	recognition					153:163	T cell recognition	146:163	T cell recognition of glycolipid and lipopeptide antigens that contain either one or two alkyl chains	146:246	CD1a is expressed on Langerhans cells (LCs) and dendritic cells (DCs), where it mediates T cell recognition of glycolipid and lipopeptide antigens that contain either one or two alkyl chains.
15723809	0	15	theme	lipopeptide	23:33	arg1	presentation					35:46	lipopeptide presentation	23:46	lipopeptide presentation	23:46	Molecular mechanism of lipopeptide presentation by CD1a.
15723809	1	16	theme	alkyl	235:239	arg1	chains					241:246	either one or two alkyl chains	217:246	either one or two alkyl chains	217:246	CD1a is expressed on Langerhans cells (LCs) and dendritic cells (DCs), where it mediates T cell recognition of glycolipid and lipopeptide antigens that contain either one or two alkyl chains.
15723809	5	17	theme	single	942:947	arg1	lipid					955:959	a single chain lipid	940:959	a single chain lipid	940:959	Thus, this structural study illustrates how a single chain lipid can be presented by CD1 and that the peptide moiety of the lipopeptide is recognized by the TCR.
15723809	1	18	theme	cell	148:151	arg1	recognition					153:163	T cell recognition	146:163	T cell recognition of glycolipid and lipopeptide antigens that contain either one or two alkyl chains	146:246	CD1a is expressed on Langerhans cells (LCs) and dendritic cells (DCs), where it mediates T cell recognition of glycolipid and lipopeptide antigens that contain either one or two alkyl chains.
15723809	3	19	theme	mycobactin	435:444	arg1	lipopeptide					446:456	a synthetic mycobactin lipopeptide	423:456	a synthetic mycobactin lipopeptide at 2.8 A resolution	423:476	Structure analysis of CD1a cocrystallized with a synthetic mycobactin lipopeptide at 2.8 A resolution further reveals that the single alkyl chain is inserted deep within the A' pocket of the groove, whereas its two peptidic branches protrude along the F' pocket to the outer, alpha-helical surface of CD1a for recognition by the TCR.
15723809	0	20	theme	presentation	35:46	arg1	mechanism					10:18	Molecular mechanism	0:18	Molecular mechanism of lipopeptide presentation by CD1a	0:54	Molecular mechanism of lipopeptide presentation by CD1a.
15723809	3	21	theme	CD1a	398:401	arg1	analysis					386:393	Structure analysis	376:393	Structure analysis of CD1a cocrystallized with a synthetic mycobactin lipopeptide at 2.8 A resolution	376:476	Structure analysis of CD1a cocrystallized with a synthetic mycobactin lipopeptide at 2.8 A resolution further reveals that the single alkyl chain is inserted deep within the A' pocket of the groove, whereas its two peptidic branches protrude along the F' pocket to the outer, alpha-helical surface of CD1a for recognition by the TCR.
15723809	3	22	theme	peptidic	591:598	arg1	branches					600:607	two peptidic branches	587:607	its two peptidic branches	583:607	Structure analysis of CD1a cocrystallized with a synthetic mycobactin lipopeptide at 2.8 A resolution further reveals that the single alkyl chain is inserted deep within the A' pocket of the groove, whereas its two peptidic branches protrude along the F' pocket to the outer, alpha-helical surface of CD1a for recognition by the TCR.
15723809	3	23	theme	groove	567:572	arg1	pocket					553:558	the A' pocket	546:558	the A' pocket of the groove	546:572	Structure analysis of CD1a cocrystallized with a synthetic mycobactin lipopeptide at 2.8 A resolution further reveals that the single alkyl chain is inserted deep within the A' pocket of the groove, whereas its two peptidic branches protrude along the F' pocket to the outer, alpha-helical surface of CD1a for recognition by the TCR.
15723809	1	24	theme	glycolipid	168:177	arg1	antigens					195:202	glycolipid and lipopeptide antigens	168:202	antigens	195:202	CD1a is expressed on Langerhans cells (LCs) and dendritic cells (DCs), where it mediates T cell recognition of glycolipid and lipopeptide antigens that contain either one or two alkyl chains.
15723809	3	25	theme	Structure	376:384	arg1	analysis					386:393	Structure analysis	376:393	Structure analysis of CD1a cocrystallized with a synthetic mycobactin lipopeptide at 2.8 A resolution	376:476	Structure analysis of CD1a cocrystallized with a synthetic mycobactin lipopeptide at 2.8 A resolution further reveals that the single alkyl chain is inserted deep within the A' pocket of the groove, whereas its two peptidic branches protrude along the F' pocket to the outer, alpha-helical surface of CD1a for recognition by the TCR.
15723809	4	26	theme	moiety	764:769	arg1	branch					742:747	the cyclized lysine branch	722:747	the cyclized lysine branch of the peptide moiety	722:769	Remarkably, the cyclized lysine branch of the peptide moiety lies in the shallow F' pocket in a conformation that closely mimics that of the alkyl chain in the CD1a-sulfatide structure.
15723809	5	27	theme	peptide	998:1004	arg1	moiety					1006:1011	the peptide moiety	994:1011	the peptide moiety of the lipopeptide	994:1030	Thus, this structural study illustrates how a single chain lipid can be presented by CD1 and that the peptide moiety of the lipopeptide is recognized by the TCR.
15723809	2	28	theme	peptide	319:325	arg1	component					327:335	the peptide component	315:335	the peptide component of didehydroxymycobactin lipopeptides	315:373	We demonstrate here that CD1a-restricted T cells can discriminate the peptide component of didehydroxymycobactin lipopeptides.
15723809	5	29	theme	chain	949:953	arg1	lipid					955:959	a single chain lipid	940:959	a single chain lipid	940:959	Thus, this structural study illustrates how a single chain lipid can be presented by CD1 and that the peptide moiety of the lipopeptide is recognized by the TCR.
15723809	4	30	theme	peptide	756:762	arg1	moiety					764:769	the peptide moiety	752:769	the peptide moiety	752:769	Remarkably, the cyclized lysine branch of the peptide moiety lies in the shallow F' pocket in a conformation that closely mimics that of the alkyl chain in the CD1a-sulfatide structure.
15723809	4	31	theme	lysine	735:740	arg1	branch					742:747	the cyclized lysine branch	722:747	the cyclized lysine branch of the peptide moiety	722:769	Remarkably, the cyclized lysine branch of the peptide moiety lies in the shallow F' pocket in a conformation that closely mimics that of the alkyl chain in the CD1a-sulfatide structure.
15723809	4	32	theme	cyclized	726:733	arg1	branch					742:747	the cyclized lysine branch	722:747	the cyclized lysine branch of the peptide moiety	722:769	Remarkably, the cyclized lysine branch of the peptide moiety lies in the shallow F' pocket in a conformation that closely mimics that of the alkyl chain in the CD1a-sulfatide structure.
15723809	3	33	theme	A	465:465	arg1	resolution					467:476	2.8 A resolution	461:476	2.8 A resolution	461:476	Structure analysis of CD1a cocrystallized with a synthetic mycobactin lipopeptide at 2.8 A resolution further reveals that the single alkyl chain is inserted deep within the A' pocket of the groove, whereas its two peptidic branches protrude along the F' pocket to the outer, alpha-helical surface of CD1a for recognition by the TCR.
15723809	2	34	theme	CD1a-restricted	274:288	arg1	cells					292:296	CD1a-restricted T cells	274:296	CD1a-restricted T cells	274:296	We demonstrate here that CD1a-restricted T cells can discriminate the peptide component of didehydroxymycobactin lipopeptides.
15723809	1	35	theme	lipopeptide	183:193	arg1	antigens					195:202	glycolipid and lipopeptide antigens	168:202	antigens	195:202	CD1a is expressed on Langerhans cells (LCs) and dendritic cells (DCs), where it mediates T cell recognition of glycolipid and lipopeptide antigens that contain either one or two alkyl chains.
15723809	5	36	theme	structural	907:916	arg1	study					918:922	this structural study	902:922	this structural study	902:922	Thus, this structural study illustrates how a single chain lipid can be presented by CD1 and that the peptide moiety of the lipopeptide is recognized by the TCR.
15723809	3	37	theme	single	503:508	arg1	chain					516:520	the single alkyl chain	499:520	the single alkyl chain	499:520	Structure analysis of CD1a cocrystallized with a synthetic mycobactin lipopeptide at 2.8 A resolution further reveals that the single alkyl chain is inserted deep within the A' pocket of the groove, whereas its two peptidic branches protrude along the F' pocket to the outer, alpha-helical surface of CD1a for recognition by the TCR.
15723809	3	38	theme	synthetic	425:433	arg1	lipopeptide					446:456	a synthetic mycobactin lipopeptide	423:456	a synthetic mycobactin lipopeptide at 2.8 A resolution	423:476	Structure analysis of CD1a cocrystallized with a synthetic mycobactin lipopeptide at 2.8 A resolution further reveals that the single alkyl chain is inserted deep within the A' pocket of the groove, whereas its two peptidic branches protrude along the F' pocket to the outer, alpha-helical surface of CD1a for recognition by the TCR.
15723809	1	39	theme	antigens	195:202	arg1	recognition					153:163	T cell recognition	146:163	T cell recognition of glycolipid and lipopeptide antigens that contain either one or two alkyl chains	146:246	CD1a is expressed on Langerhans cells (LCs) and dendritic cells (DCs), where it mediates T cell recognition of glycolipid and lipopeptide antigens that contain either one or two alkyl chains.
15723809	4	40	theme	CD1a-sulfatide	870:883	arg1	structure					885:893	the CD1a-sulfatide structure	866:893	the CD1a-sulfatide structure	866:893	Remarkably, the cyclized lysine branch of the peptide moiety lies in the shallow F' pocket in a conformation that closely mimics that of the alkyl chain in the CD1a-sulfatide structure.
15723809	3	41	theme	outer	645:649	arg1	surface					666:672	the outer, alpha-helical surface	641:672	surface	666:672	Structure analysis of CD1a cocrystallized with a synthetic mycobactin lipopeptide at 2.8 A resolution further reveals that the single alkyl chain is inserted deep within the A' pocket of the groove, whereas its two peptidic branches protrude along the F' pocket to the outer, alpha-helical surface of CD1a for recognition by the TCR.
15723809	1	42	contain	contain	209:215	arg1	antigens					195:202	glycolipid and lipopeptide antigens	168:202	antigens	195:202	CD1a is expressed on Langerhans cells (LCs) and dendritic cells (DCs), where it mediates T cell recognition of glycolipid and lipopeptide antigens that contain either one or two alkyl chains.
15723809	1	42	contain	contain	209:215	arg2	chains					241:246	either one or two alkyl chains	217:246	either one or two alkyl chains	217:246	CD1a is expressed on Langerhans cells (LCs) and dendritic cells (DCs), where it mediates T cell recognition of glycolipid and lipopeptide antigens that contain either one or two alkyl chains.
15723809	3	43	theme	alkyl	510:514	arg1	chain					516:520	the single alkyl chain	499:520	the single alkyl chain	499:520	Structure analysis of CD1a cocrystallized with a synthetic mycobactin lipopeptide at 2.8 A resolution further reveals that the single alkyl chain is inserted deep within the A' pocket of the groove, whereas its two peptidic branches protrude along the F' pocket to the outer, alpha-helical surface of CD1a for recognition by the TCR.
12833155	2	0	theme	sphingosine	403:413	arg1	chain					415:419	the sphingosine chain	399:419	the sphingosine chain completely buried in the A' pocket and the fatty acid chain emerging from the interface of the A' pocket into the more exposed F' pocket	399:556	The lipid adopts an S-shaped conformation, with the sphingosine chain completely buried in the A' pocket and the fatty acid chain emerging from the interface of the A' pocket into the more exposed F' pocket.
12833155	1	1	theme	CD1a	278:281	arg1	structure					259:267	the crystal structure	247:267	the crystal structure of human CD1a in complex with a sulfatide self antigen at a resolution of 2.15 A	247:348	Here we report the crystal structure of human CD1a in complex with a sulfatide self antigen at a resolution of 2.15 A.
12833155	0	2	theme	foreign	134:140	arg1	lipid					142:146	foreign lipid and glycolipid antigens	134:170	lipid	142:146	Crystal structure of CD1a in complex with a sulfatide self antigen at a resolution of 2.15 A. CD1 antigens bind a variety of self and foreign lipid and glycolipid antigens for presentation to CD1-restricted T cell receptors (TCRs).
12833155	1	3	with	complex	286:292	arg1	antigen					316:322	a sulfatide self antigen	299:322	a sulfatide self antigen at a resolution of 2.15 A	299:348	Here we report the crystal structure of human CD1a in complex with a sulfatide self antigen at a resolution of 2.15 A.
12833155	0	4	from	structure	8:16	arg1	complex					29:35	complex	29:35	complex with a sulfatide self antigen	29:65	Crystal structure of CD1a in complex with a sulfatide self antigen at a resolution of 2.15 A. CD1 antigens bind a variety of self and foreign lipid and glycolipid antigens for presentation to CD1-restricted T cell receptors (TCRs).
12833155	0	4	from	structure	8:16	arg1	resolution					72:81	a resolution	70:81	a resolution of 2.15 A. CD1 antigens	70:105	Crystal structure of CD1a in complex with a sulfatide self antigen at a resolution of 2.15 A. CD1 antigens bind a variety of self and foreign lipid and glycolipid antigens for presentation to CD1-restricted T cell receptors (TCRs).
12833155	1	5	theme	A	348:348	arg1	resolution					329:338	a resolution	327:338	a resolution of 2.15 A	327:348	Here we report the crystal structure of human CD1a in complex with a sulfatide self antigen at a resolution of 2.15 A.
12833155	0	6	theme	CD1-restricted	192:205	arg1	TCRs					225:228	TCRs	225:228	TCRs	225:228	Crystal structure of CD1a in complex with a sulfatide self antigen at a resolution of 2.15 A. CD1 antigens bind a variety of self and foreign lipid and glycolipid antigens for presentation to CD1-restricted T cell receptors (TCRs).
12833155	0	6	theme	CD1-restricted	192:205	arg1	receptors					214:222	CD1-restricted T cell receptors	192:222	CD1-restricted T cell receptors (TCRs)	192:229	Crystal structure of CD1a in complex with a sulfatide self antigen at a resolution of 2.15 A. CD1 antigens bind a variety of self and foreign lipid and glycolipid antigens for presentation to CD1-restricted T cell receptors (TCRs).
12833155	1	7	from	structure	259:267	arg1	complex					286:292	complex	286:292	complex with a sulfatide self antigen at a resolution of 2.15 A	286:348	Here we report the crystal structure of human CD1a in complex with a sulfatide self antigen at a resolution of 2.15 A.
12833155	2	8	dep	pocket	449:454	arg1	the					442:444	the	442:444	the	442:444	The lipid adopts an S-shaped conformation, with the sphingosine chain completely buried in the A' pocket and the fatty acid chain emerging from the interface of the A' pocket into the more exposed F' pocket.
12833155	1	9	from	resolution	329:338	arg1	antigen					316:322	a sulfatide self antigen	299:322	a sulfatide self antigen at a resolution of 2.15 A	299:348	Here we report the crystal structure of human CD1a in complex with a sulfatide self antigen at a resolution of 2.15 A.
12833155	0	10	theme	lipid	142:146	arg1	lipid					142:146	foreign lipid and glycolipid antigens	134:170	lipid	142:146	Crystal structure of CD1a in complex with a sulfatide self antigen at a resolution of 2.15 A. CD1 antigens bind a variety of self and foreign lipid and glycolipid antigens for presentation to CD1-restricted T cell receptors (TCRs).
12833155	0	10	theme	lipid	142:146	arg1	variety					114:120	a variety	112:120	a variety of self and foreign lipid and glycolipid antigens for presentation to CD1-restricted T cell receptors (TCRs)	112:229	Crystal structure of CD1a in complex with a sulfatide self antigen at a resolution of 2.15 A. CD1 antigens bind a variety of self and foreign lipid and glycolipid antigens for presentation to CD1-restricted T cell receptors (TCRs).
12833155	0	10	theme	lipid	142:146	arg1	self					125:128	self	125:128	self	125:128	Crystal structure of CD1a in complex with a sulfatide self antigen at a resolution of 2.15 A. CD1 antigens bind a variety of self and foreign lipid and glycolipid antigens for presentation to CD1-restricted T cell receptors (TCRs).
12833155	0	11	theme	cell	209:212	arg1	TCRs					225:228	TCRs	225:228	TCRs	225:228	Crystal structure of CD1a in complex with a sulfatide self antigen at a resolution of 2.15 A. CD1 antigens bind a variety of self and foreign lipid and glycolipid antigens for presentation to CD1-restricted T cell receptors (TCRs).
12833155	0	11	theme	cell	209:212	arg1	receptors					214:222	CD1-restricted T cell receptors	192:222	CD1-restricted T cell receptors (TCRs)	192:229	Crystal structure of CD1a in complex with a sulfatide self antigen at a resolution of 2.15 A. CD1 antigens bind a variety of self and foreign lipid and glycolipid antigens for presentation to CD1-restricted T cell receptors (TCRs).
12833155	4	12	theme	alkyl	760:764	arg1	chains					766:771	select alkyl chains	753:771	select alkyl chains of a particular length	753:794	Because the A' pocket is narrow with a fixed terminus, it can act as a molecular 'ruler' to select alkyl chains of a particular length.
12833155	2	13	theme	pocket	519:524	arg1	interface					499:507	the interface	495:507	the interface of the A' pocket into the more exposed F' pocket	495:556	The lipid adopts an S-shaped conformation, with the sphingosine chain completely buried in the A' pocket and the fatty acid chain emerging from the interface of the A' pocket into the more exposed F' pocket.
12833155	0	14	theme	T	207:207	arg1	TCRs					225:228	TCRs	225:228	TCRs	225:228	Crystal structure of CD1a in complex with a sulfatide self antigen at a resolution of 2.15 A. CD1 antigens bind a variety of self and foreign lipid and glycolipid antigens for presentation to CD1-restricted T cell receptors (TCRs).
12833155	0	14	theme	T	207:207	arg1	receptors					214:222	CD1-restricted T cell receptors	192:222	CD1-restricted T cell receptors (TCRs)	192:229	Crystal structure of CD1a in complex with a sulfatide self antigen at a resolution of 2.15 A. CD1 antigens bind a variety of self and foreign lipid and glycolipid antigens for presentation to CD1-restricted T cell receptors (TCRs).
12833155	2	15	theme	acid	470:473	arg1	chain					475:479	the fatty acid chain	460:479	the fatty acid chain	460:479	The lipid adopts an S-shaped conformation, with the sphingosine chain completely buried in the A' pocket and the fatty acid chain emerging from the interface of the A' pocket into the more exposed F' pocket.
12833155	4	16	theme	fixed	700:704	arg1	terminus					706:713	a fixed terminus	698:713	a fixed terminus	698:713	Because the A' pocket is narrow with a fixed terminus, it can act as a molecular 'ruler' to select alkyl chains of a particular length.
12833155	4	17	theme	select	753:758	arg1	chains					766:771	select alkyl chains	753:771	select alkyl chains of a particular length	753:794	Because the A' pocket is narrow with a fixed terminus, it can act as a molecular 'ruler' to select alkyl chains of a particular length.
12833155	0	18	from	complex	29:35	arg1	structure					8:16	Crystal structure	0:16	Crystal structure of CD1a in complex with a sulfatide self antigen at a resolution of 2.15 A. CD1 antigens	0:105	Crystal structure of CD1a in complex with a sulfatide self antigen at a resolution of 2.15 A. CD1 antigens bind a variety of self and foreign lipid and glycolipid antigens for presentation to CD1-restricted T cell receptors (TCRs).
12833155	0	19	theme	glycolipid	152:161	arg1	antigens					163:170	foreign lipid and glycolipid antigens	134:170	antigens	163:170	Crystal structure of CD1a in complex with a sulfatide self antigen at a resolution of 2.15 A. CD1 antigens bind a variety of self and foreign lipid and glycolipid antigens for presentation to CD1-restricted T cell receptors (TCRs).
12833155	1	20	theme	self	311:314	arg1	antigen					316:322	a sulfatide self antigen	299:322	a sulfatide self antigen at a resolution of 2.15 A	299:348	Here we report the crystal structure of human CD1a in complex with a sulfatide self antigen at a resolution of 2.15 A.
12833155	0	21	theme	Crystal	0:6	arg1	structure					8:16	Crystal structure	0:16	Crystal structure of CD1a in complex with a sulfatide self antigen at a resolution of 2.15 A. CD1 antigens	0:105	Crystal structure of CD1a in complex with a sulfatide self antigen at a resolution of 2.15 A. CD1 antigens bind a variety of self and foreign lipid and glycolipid antigens for presentation to CD1-restricted T cell receptors (TCRs).
12833155	0	22	theme	CD1a	21:24	arg1	structure					8:16	Crystal structure	0:16	Crystal structure of CD1a in complex with a sulfatide self antigen at a resolution of 2.15 A. CD1 antigens	0:105	Crystal structure of CD1a in complex with a sulfatide self antigen at a resolution of 2.15 A. CD1 antigens bind a variety of self and foreign lipid and glycolipid antigens for presentation to CD1-restricted T cell receptors (TCRs).
12833155	0	23	theme	CD1	94:96	arg1	antigens					98:105	2.15 A. CD1 antigens	86:105	2.15 A. CD1 antigens	86:105	Crystal structure of CD1a in complex with a sulfatide self antigen at a resolution of 2.15 A. CD1 antigens bind a variety of self and foreign lipid and glycolipid antigens for presentation to CD1-restricted T cell receptors (TCRs).
12833155	2	24	theme	F	548:548	arg1	pocket					551:556	the more exposed F' pocket	531:556	the more exposed F' pocket	531:556	The lipid adopts an S-shaped conformation, with the sphingosine chain completely buried in the A' pocket and the fatty acid chain emerging from the interface of the A' pocket into the more exposed F' pocket.
12833155	2	25	theme	exposed	540:546	arg1	pocket					551:556	the more exposed F' pocket	531:556	the more exposed F' pocket	531:556	The lipid adopts an S-shaped conformation, with the sphingosine chain completely buried in the A' pocket and the fatty acid chain emerging from the interface of the A' pocket into the more exposed F' pocket.
12833155	4	26	theme	particular	778:787	arg1	length					789:794	a particular length	776:794	a particular length	776:794	Because the A' pocket is narrow with a fixed terminus, it can act as a molecular 'ruler' to select alkyl chains of a particular length.
12833155	0	27	theme	A.	91:92	arg1	antigens					98:105	2.15 A. CD1 antigens	86:105	2.15 A. CD1 antigens	86:105	Crystal structure of CD1a in complex with a sulfatide self antigen at a resolution of 2.15 A. CD1 antigens bind a variety of self and foreign lipid and glycolipid antigens for presentation to CD1-restricted T cell receptors (TCRs).
12833155	4	28	theme	length	789:794	arg1	chains					766:771	select alkyl chains	753:771	select alkyl chains of a particular length	753:794	Because the A' pocket is narrow with a fixed terminus, it can act as a molecular 'ruler' to select alkyl chains of a particular length.
12833155	0	29	theme	antigens	98:105	arg1	resolution					72:81	a resolution	70:81	a resolution of 2.15 A. CD1 antigens	70:105	Crystal structure of CD1a in complex with a sulfatide self antigen at a resolution of 2.15 A. CD1 antigens bind a variety of self and foreign lipid and glycolipid antigens for presentation to CD1-restricted T cell receptors (TCRs).
12833155	1	30	theme	crystal	251:257	arg1	structure					259:267	the crystal structure	247:267	the crystal structure of human CD1a in complex with a sulfatide self antigen at a resolution of 2.15 A	247:348	Here we report the crystal structure of human CD1a in complex with a sulfatide self antigen at a resolution of 2.15 A.
12833155	1	31	theme	sulfatide	301:309	arg1	antigen					316:322	a sulfatide self antigen	299:322	a sulfatide self antigen at a resolution of 2.15 A	299:348	Here we report the crystal structure of human CD1a in complex with a sulfatide self antigen at a resolution of 2.15 A.
12833155	2	32	theme	S-shaped	371:378	arg1	conformation					380:391	an S-shaped conformation	368:391	an S-shaped conformation	368:391	The lipid adopts an S-shaped conformation, with the sphingosine chain completely buried in the A' pocket and the fatty acid chain emerging from the interface of the A' pocket into the more exposed F' pocket.
12833155	1	33	theme	human	272:276	arg1	CD1a					278:281	human CD1a	272:281	human CD1a	272:281	Here we report the crystal structure of human CD1a in complex with a sulfatide self antigen at a resolution of 2.15 A.
12833155	0	34	theme	self	125:128	arg1	lipid					142:146	foreign lipid and glycolipid antigens	134:170	lipid	142:146	Crystal structure of CD1a in complex with a sulfatide self antigen at a resolution of 2.15 A. CD1 antigens bind a variety of self and foreign lipid and glycolipid antigens for presentation to CD1-restricted T cell receptors (TCRs).
12833155	0	34	theme	self	125:128	arg1	variety					114:120	a variety	112:120	a variety of self and foreign lipid and glycolipid antigens for presentation to CD1-restricted T cell receptors (TCRs)	112:229	Crystal structure of CD1a in complex with a sulfatide self antigen at a resolution of 2.15 A. CD1 antigens bind a variety of self and foreign lipid and glycolipid antigens for presentation to CD1-restricted T cell receptors (TCRs).
12833155	0	34	theme	self	125:128	arg1	self					125:128	self	125:128	self	125:128	Crystal structure of CD1a in complex with a sulfatide self antigen at a resolution of 2.15 A. CD1 antigens bind a variety of self and foreign lipid and glycolipid antigens for presentation to CD1-restricted T cell receptors (TCRs).
12833155	1	35	theme	2.15	343:346	arg1	A					348:348	2.15 A	343:348	2.15 A	343:348	Here we report the crystal structure of human CD1a in complex with a sulfatide self antigen at a resolution of 2.15 A.
12833155	2	36	theme	fatty	464:468	arg1	chain					475:479	the fatty acid chain	460:479	the fatty acid chain	460:479	The lipid adopts an S-shaped conformation, with the sphingosine chain completely buried in the A' pocket and the fatty acid chain emerging from the interface of the A' pocket into the more exposed F' pocket.
12833155	0	37	from	resolution	72:81	arg1	CD1a					21:24	CD1a	21:24	CD1a in complex with a sulfatide self antigen at a resolution of 2.15 A. CD1 antigens	21:105	Crystal structure of CD1a in complex with a sulfatide self antigen at a resolution of 2.15 A. CD1 antigens bind a variety of self and foreign lipid and glycolipid antigens for presentation to CD1-restricted T cell receptors (TCRs).
12833155	0	37	from	resolution	72:81	arg1	structure					8:16	Crystal structure	0:16	Crystal structure of CD1a in complex with a sulfatide self antigen at a resolution of 2.15 A. CD1 antigens	0:105	Crystal structure of CD1a in complex with a sulfatide self antigen at a resolution of 2.15 A. CD1 antigens bind a variety of self and foreign lipid and glycolipid antigens for presentation to CD1-restricted T cell receptors (TCRs).
12833155	0	38	theme	self	54:57	arg1	antigen					59:65	a sulfatide self antigen	42:65	a sulfatide self antigen	42:65	Crystal structure of CD1a in complex with a sulfatide self antigen at a resolution of 2.15 A. CD1 antigens bind a variety of self and foreign lipid and glycolipid antigens for presentation to CD1-restricted T cell receptors (TCRs).
12833155	4	39	theme	molecular	732:740	arg1	it					716:717	it	716:717	it	716:717	Because the A' pocket is narrow with a fixed terminus, it can act as a molecular 'ruler' to select alkyl chains of a particular length.
12833155	4	39	theme	molecular	732:740	arg1	ruler					743:747	a molecular 'ruler'	730:748	a molecular 'ruler' to select alkyl chains of a particular length	730:794	Because the A' pocket is narrow with a fixed terminus, it can act as a molecular 'ruler' to select alkyl chains of a particular length.
12833155	4	40	with	narrow	686:691	arg1	terminus					706:713	a fixed terminus	698:713	a fixed terminus	698:713	Because the A' pocket is narrow with a fixed terminus, it can act as a molecular 'ruler' to select alkyl chains of a particular length.
12833155	0	41	theme	sulfatide	44:52	arg1	antigen					59:65	a sulfatide self antigen	42:65	a sulfatide self antigen	42:65	Crystal structure of CD1a in complex with a sulfatide self antigen at a resolution of 2.15 A. CD1 antigens bind a variety of self and foreign lipid and glycolipid antigens for presentation to CD1-restricted T cell receptors (TCRs).
12833155	0	42	from	CD1a	21:24	arg1	complex					29:35	complex	29:35	complex with a sulfatide self antigen	29:65	Crystal structure of CD1a in complex with a sulfatide self antigen at a resolution of 2.15 A. CD1 antigens bind a variety of self and foreign lipid and glycolipid antigens for presentation to CD1-restricted T cell receptors (TCRs).
12833155	0	43	with	complex	29:35	arg1	antigen					59:65	a sulfatide self antigen	42:65	a sulfatide self antigen	42:65	Crystal structure of CD1a in complex with a sulfatide self antigen at a resolution of 2.15 A. CD1 antigens bind a variety of self and foreign lipid and glycolipid antigens for presentation to CD1-restricted T cell receptors (TCRs).
12833155	3	44	theme	TCR	644:646	arg1	recognition					648:658	TCR recognition	644:658	TCR recognition	644:658	The headgroup is anchored in the A'-F' junction and protrudes into the F' pocket for TCR recognition.
25642819	0	0	theme	ligands	69:75	arg1	recognition					27:37	T cell antigen receptor recognition	3:37	T cell antigen receptor recognition of CD1a presenting self lipid ligands	3:75	αβ T cell antigen receptor recognition of CD1a presenting self lipid ligands.
25642819	5	1	theme	TCR-CD1a	730:737	arg1	zone					747:750	the TCR-CD1a contact zone	726:750	the TCR-CD1a contact zone	726:750	Nonpermissive ligands indirectly inhibited TCR binding by disrupting the TCR-CD1a contact zone.
25642819	6	2	theme	αβ	848:849	arg1	cells					853:857	αβ T cells	848:857	αβ T cells	848:857	The exclusive recognition of CD1a by the TCR represents a previously unknown mechanism whereby αβ T cells indirectly sense self antigens that are bound to an antigen-presenting molecule.
25642819	0	3	theme	lipid	63:67	arg1	ligands					69:75	CD1a presenting self lipid ligands	42:75	CD1a presenting self lipid ligands	42:75	αβ T cell antigen receptor recognition of CD1a presenting self lipid ligands.
25642819	6	4	theme	self	876:879	arg1	antigens					881:888	self antigens	876:888	self antigens that are bound to an antigen-presenting molecule	876:937	The exclusive recognition of CD1a by the TCR represents a previously unknown mechanism whereby αβ T cells indirectly sense self antigens that are bound to an antigen-presenting molecule.
25642819	1	5	theme	simultaneous	135:146	arg1	co-recognition					148:161	the simultaneous co-recognition	131:161	the simultaneous co-recognition of antigens and antigen-presenting molecules by the αβ T cell antigen receptor (TCR)	131:246	A central paradigm in αβ T cell-mediated immunity is the simultaneous co-recognition of antigens and antigen-presenting molecules by the αβ T cell antigen receptor (TCR).
25642819	1	5	theme	simultaneous	135:146	arg1	paradigm					88:95	A central paradigm	78:95	A central paradigm in αβ T cell-mediated immunity	78:126	A central paradigm in αβ T cell-mediated immunity is the simultaneous co-recognition of antigens and antigen-presenting molecules by the αβ T cell antigen receptor (TCR).
25642819	6	6	theme	unknown	822:828	arg1	mechanism					830:838	a previously unknown mechanism	809:838	a previously unknown mechanism whereby αβ T cells indirectly sense self antigens that are bound to an antigen-presenting molecule	809:937	The exclusive recognition of CD1a by the TCR represents a previously unknown mechanism whereby αβ T cells indirectly sense self antigens that are bound to an antigen-presenting molecule.
25642819	3	7	theme	prototypical	323:334	arg1	TCR					349:351	a prototypical autoreactive TCR	321:351	a prototypical autoreactive TCR	321:351	We found that a prototypical autoreactive TCR bound CD1a when it was presenting a series of permissive endogenous ligands, while other lipid ligands were nonpermissive to TCR binding.
25642819	6	8	theme	CD1a	782:785	arg1	recognition					767:777	The exclusive recognition	753:777	The exclusive recognition of CD1a by the TCR	753:796	The exclusive recognition of CD1a by the TCR represents a previously unknown mechanism whereby αβ T cells indirectly sense self antigens that are bound to an antigen-presenting molecule.
25642819	3	9	theme	autoreactive	336:347	arg1	TCR					349:351	a prototypical autoreactive TCR	321:351	a prototypical autoreactive TCR	321:351	We found that a prototypical autoreactive TCR bound CD1a when it was presenting a series of permissive endogenous ligands, while other lipid ligands were nonpermissive to TCR binding.
25642819	2	10	theme	antigens	297:304	arg1	repertoire					271:280	a broad repertoire	263:280	a broad repertoire of lipid-based antigens	263:304	CD1a presents a broad repertoire of lipid-based antigens.
25642819	2	10	theme	antigens	297:304	arg1	antigens					297:304	lipid-based antigens	285:304	lipid-based antigens	285:304	CD1a presents a broad repertoire of lipid-based antigens.
25642819	4	11	theme	permissive	637:646	arg1	ligands					648:654	permissive ligands	637:654	permissive ligands	637:654	The structures of two TCR-CD1a-lipid complexes showed that the TCR docked over the A' roof of CD1a in a manner that precluded direct contact with permissive ligands.
25642819	3	12	theme	other	436:440	arg1	ligands					448:454	other lipid ligands	436:454	other lipid ligands	436:454	We found that a prototypical autoreactive TCR bound CD1a when it was presenting a series of permissive endogenous ligands, while other lipid ligands were nonpermissive to TCR binding.
25642819	4	13	theme	direct	617:622	arg1	contact					624:630	direct contact	617:630	direct contact with permissive ligands	617:654	The structures of two TCR-CD1a-lipid complexes showed that the TCR docked over the A' roof of CD1a in a manner that precluded direct contact with permissive ligands.
25642819	3	14	theme	permissive	399:408	arg1	ligands					421:427	permissive endogenous ligands	399:427	permissive endogenous ligands	399:427	We found that a prototypical autoreactive TCR bound CD1a when it was presenting a series of permissive endogenous ligands, while other lipid ligands were nonpermissive to TCR binding.
25642819	6	15	theme	T	851:851	arg1	cells					853:857	αβ T cells	848:857	αβ T cells	848:857	The exclusive recognition of CD1a by the TCR represents a previously unknown mechanism whereby αβ T cells indirectly sense self antigens that are bound to an antigen-presenting molecule.
25642819	6	16	theme	exclusive	757:765	arg1	recognition					767:777	The exclusive recognition	753:777	The exclusive recognition of CD1a by the TCR	753:796	The exclusive recognition of CD1a by the TCR represents a previously unknown mechanism whereby αβ T cells indirectly sense self antigens that are bound to an antigen-presenting molecule.
25642819	3	17	theme	endogenous	410:419	arg1	ligands					421:427	permissive endogenous ligands	399:427	permissive endogenous ligands	399:427	We found that a prototypical autoreactive TCR bound CD1a when it was presenting a series of permissive endogenous ligands, while other lipid ligands were nonpermissive to TCR binding.
25642819	0	18	theme	T	3:3	arg1	recognition					27:37	T cell antigen receptor recognition	3:37	T cell antigen receptor recognition of CD1a presenting self lipid ligands	3:75	αβ T cell antigen receptor recognition of CD1a presenting self lipid ligands.
25642819	4	19	with	contact	624:630	arg1	ligands					648:654	permissive ligands	637:654	permissive ligands	637:654	The structures of two TCR-CD1a-lipid complexes showed that the TCR docked over the A' roof of CD1a in a manner that precluded direct contact with permissive ligands.
25642819	2	20	theme	lipid-based	285:295	arg1	antigens					297:304	lipid-based antigens	285:304	lipid-based antigens	285:304	CD1a presents a broad repertoire of lipid-based antigens.
25642819	1	21	theme	antigens	166:173	arg1	co-recognition					148:161	the simultaneous co-recognition	131:161	the simultaneous co-recognition of antigens and antigen-presenting molecules by the αβ T cell antigen receptor (TCR)	131:246	A central paradigm in αβ T cell-mediated immunity is the simultaneous co-recognition of antigens and antigen-presenting molecules by the αβ T cell antigen receptor (TCR).
25642819	1	21	theme	antigens	166:173	arg1	paradigm					88:95	A central paradigm	78:95	A central paradigm in αβ T cell-mediated immunity	78:126	A central paradigm in αβ T cell-mediated immunity is the simultaneous co-recognition of antigens and antigen-presenting molecules by the αβ T cell antigen receptor (TCR).
25642819	4	22	theme	complexes	528:536	arg1	structures					495:504	The structures	491:504	The structures of two TCR-CD1a-lipid complexes	491:536	The structures of two TCR-CD1a-lipid complexes showed that the TCR docked over the A' roof of CD1a in a manner that precluded direct contact with permissive ligands.
25642819	0	23	theme	antigen	10:16	arg1	recognition					27:37	T cell antigen receptor recognition	3:37	T cell antigen receptor recognition of CD1a presenting self lipid ligands	3:75	αβ T cell antigen receptor recognition of CD1a presenting self lipid ligands.
25642819	4	24	theme	TCR-CD1a-lipid	513:526	arg1	complexes					528:536	two TCR-CD1a-lipid complexes	509:536	two TCR-CD1a-lipid complexes	509:536	The structures of two TCR-CD1a-lipid complexes showed that the TCR docked over the A' roof of CD1a in a manner that precluded direct contact with permissive ligands.
25642819	1	25	theme	central	80:86	arg1	co-recognition					148:161	the simultaneous co-recognition	131:161	the simultaneous co-recognition of antigens and antigen-presenting molecules by the αβ T cell antigen receptor (TCR)	131:246	A central paradigm in αβ T cell-mediated immunity is the simultaneous co-recognition of antigens and antigen-presenting molecules by the αβ T cell antigen receptor (TCR).
25642819	1	25	theme	central	80:86	arg1	paradigm					88:95	A central paradigm	78:95	A central paradigm in αβ T cell-mediated immunity	78:126	A central paradigm in αβ T cell-mediated immunity is the simultaneous co-recognition of antigens and antigen-presenting molecules by the αβ T cell antigen receptor (TCR).
25642819	1	26	theme	antigen-presenting	179:196	arg1	molecules					198:206	antigen-presenting molecules	179:206	antigen-presenting molecules	179:206	A central paradigm in αβ T cell-mediated immunity is the simultaneous co-recognition of antigens and antigen-presenting molecules by the αβ T cell antigen receptor (TCR).
25642819	0	27	theme	cell	5:8	arg1	recognition					27:37	T cell antigen receptor recognition	3:37	T cell antigen receptor recognition of CD1a presenting self lipid ligands	3:75	αβ T cell antigen receptor recognition of CD1a presenting self lipid ligands.
25642819	5	28	theme	Nonpermissive	657:669	arg1	ligands					671:677	Nonpermissive ligands	657:677	Nonpermissive ligands	657:677	Nonpermissive ligands indirectly inhibited TCR binding by disrupting the TCR-CD1a contact zone.
25642819	2	29	theme	broad	265:269	arg1	repertoire					271:280	a broad repertoire	263:280	a broad repertoire of lipid-based antigens	263:304	CD1a presents a broad repertoire of lipid-based antigens.
25642819	2	29	theme	broad	265:269	arg1	antigens					297:304	lipid-based antigens	285:304	lipid-based antigens	285:304	CD1a presents a broad repertoire of lipid-based antigens.
25642819	1	30	theme	molecules	198:206	arg1	co-recognition					148:161	the simultaneous co-recognition	131:161	the simultaneous co-recognition of antigens and antigen-presenting molecules by the αβ T cell antigen receptor (TCR)	131:246	A central paradigm in αβ T cell-mediated immunity is the simultaneous co-recognition of antigens and antigen-presenting molecules by the αβ T cell antigen receptor (TCR).
25642819	1	30	theme	molecules	198:206	arg1	paradigm					88:95	A central paradigm	78:95	A central paradigm in αβ T cell-mediated immunity	78:126	A central paradigm in αβ T cell-mediated immunity is the simultaneous co-recognition of antigens and antigen-presenting molecules by the αβ T cell antigen receptor (TCR).
25642819	6	31	theme	antigen-presenting	911:928	arg1	molecule					930:937	an antigen-presenting molecule	908:937	an antigen-presenting molecule	908:937	The exclusive recognition of CD1a by the TCR represents a previously unknown mechanism whereby αβ T cells indirectly sense self antigens that are bound to an antigen-presenting molecule.
25642819	3	32	theme	ligands	421:427	arg1	series					389:394	a series	387:394	a series of permissive endogenous ligands	387:427	We found that a prototypical autoreactive TCR bound CD1a when it was presenting a series of permissive endogenous ligands, while other lipid ligands were nonpermissive to TCR binding.
25642819	0	33	theme	receptor	18:25	arg1	recognition					27:37	T cell antigen receptor recognition	3:37	T cell antigen receptor recognition of CD1a presenting self lipid ligands	3:75	αβ T cell antigen receptor recognition of CD1a presenting self lipid ligands.
25642819	5	34	theme	contact	739:745	arg1	zone					747:750	the TCR-CD1a contact zone	726:750	the TCR-CD1a contact zone	726:750	Nonpermissive ligands indirectly inhibited TCR binding by disrupting the TCR-CD1a contact zone.
25642819	5	35	theme	TCR	700:702	arg1	binding					704:710	TCR binding	700:710	TCR binding	700:710	Nonpermissive ligands indirectly inhibited TCR binding by disrupting the TCR-CD1a contact zone.
25642819	0	36	theme	CD1a	42:45	arg1	ligands					69:75	CD1a presenting self lipid ligands	42:75	CD1a presenting self lipid ligands	42:75	αβ T cell antigen receptor recognition of CD1a presenting self lipid ligands.
25642819	3	37	theme	lipid	442:446	arg1	ligands					448:454	other lipid ligands	436:454	other lipid ligands	436:454	We found that a prototypical autoreactive TCR bound CD1a when it was presenting a series of permissive endogenous ligands, while other lipid ligands were nonpermissive to TCR binding.
25642819	3	38	theme	TCR	478:480	arg1	binding					482:488	TCR binding	478:488	TCR binding	478:488	We found that a prototypical autoreactive TCR bound CD1a when it was presenting a series of permissive endogenous ligands, while other lipid ligands were nonpermissive to TCR binding.
25642819	1	39	theme	αβ	100:101	arg1	immunity					119:126	αβ T cell-mediated immunity	100:126	αβ T cell-mediated immunity	100:126	A central paradigm in αβ T cell-mediated immunity is the simultaneous co-recognition of antigens and antigen-presenting molecules by the αβ T cell antigen receptor (TCR).
25642819	1	40	theme	T	103:103	arg1	immunity					119:126	αβ T cell-mediated immunity	100:126	αβ T cell-mediated immunity	100:126	A central paradigm in αβ T cell-mediated immunity is the simultaneous co-recognition of antigens and antigen-presenting molecules by the αβ T cell antigen receptor (TCR).
25642819	1	41	from	paradigm	88:95	arg1	immunity					119:126	αβ T cell-mediated immunity	100:126	αβ T cell-mediated immunity	100:126	A central paradigm in αβ T cell-mediated immunity is the simultaneous co-recognition of antigens and antigen-presenting molecules by the αβ T cell antigen receptor (TCR).
25642819	1	42	theme	αβ	215:216	arg1	TCR					243:245	TCR	243:245	TCR	243:245	A central paradigm in αβ T cell-mediated immunity is the simultaneous co-recognition of antigens and antigen-presenting molecules by the αβ T cell antigen receptor (TCR).
25642819	1	42	theme	αβ	215:216	arg1	receptor					233:240	the αβ T cell antigen receptor	211:240	the αβ T cell antigen receptor (TCR)	211:246	A central paradigm in αβ T cell-mediated immunity is the simultaneous co-recognition of antigens and antigen-presenting molecules by the αβ T cell antigen receptor (TCR).
25642819	1	43	theme	cell-mediated	105:117	arg1	immunity					119:126	αβ T cell-mediated immunity	100:126	αβ T cell-mediated immunity	100:126	A central paradigm in αβ T cell-mediated immunity is the simultaneous co-recognition of antigens and antigen-presenting molecules by the αβ T cell antigen receptor (TCR).
25642819	1	44	theme	T	218:218	arg1	TCR					243:245	TCR	243:245	TCR	243:245	A central paradigm in αβ T cell-mediated immunity is the simultaneous co-recognition of antigens and antigen-presenting molecules by the αβ T cell antigen receptor (TCR).
25642819	1	44	theme	T	218:218	arg1	receptor					233:240	the αβ T cell antigen receptor	211:240	the αβ T cell antigen receptor (TCR)	211:246	A central paradigm in αβ T cell-mediated immunity is the simultaneous co-recognition of antigens and antigen-presenting molecules by the αβ T cell antigen receptor (TCR).
25642819	0	45	theme	self	58:61	arg1	ligands					69:75	CD1a presenting self lipid ligands	42:75	CD1a presenting self lipid ligands	42:75	αβ T cell antigen receptor recognition of CD1a presenting self lipid ligands.
25642819	4	46	theme	CD1a	585:588	arg1	roof					577:580	the A' roof	570:580	the A' roof of CD1a	570:588	The structures of two TCR-CD1a-lipid complexes showed that the TCR docked over the A' roof of CD1a in a manner that precluded direct contact with permissive ligands.
25642819	1	47	theme	cell	220:223	arg1	TCR					243:245	TCR	243:245	TCR	243:245	A central paradigm in αβ T cell-mediated immunity is the simultaneous co-recognition of antigens and antigen-presenting molecules by the αβ T cell antigen receptor (TCR).
25642819	1	47	theme	cell	220:223	arg1	receptor					233:240	the αβ T cell antigen receptor	211:240	the αβ T cell antigen receptor (TCR)	211:246	A central paradigm in αβ T cell-mediated immunity is the simultaneous co-recognition of antigens and antigen-presenting molecules by the αβ T cell antigen receptor (TCR).
25642819	0	48	theme	presenting	47:56	arg1	ligands					69:75	CD1a presenting self lipid ligands	42:75	CD1a presenting self lipid ligands	42:75	αβ T cell antigen receptor recognition of CD1a presenting self lipid ligands.
25642819	1	49	theme	antigen	225:231	arg1	TCR					243:245	TCR	243:245	TCR	243:245	A central paradigm in αβ T cell-mediated immunity is the simultaneous co-recognition of antigens and antigen-presenting molecules by the αβ T cell antigen receptor (TCR).
25642819	1	49	theme	antigen	225:231	arg1	receptor					233:240	the αβ T cell antigen receptor	211:240	the αβ T cell antigen receptor (TCR)	211:246	A central paradigm in αβ T cell-mediated immunity is the simultaneous co-recognition of antigens and antigen-presenting molecules by the αβ T cell antigen receptor (TCR).
14529283	10	0	theme	disulfide	2024:2032	arg1	bonds					2034:2038	these two disulfide bonds	2014:2038	these two disulfide bonds	2014:2038	Due to conservation of these cysteine residues, these two disulfide bonds are likely to exist in all NTPDases.
14529283	4	1	theme	ADP	1003:1005	arg1	hydrolysis					969:978	slower hydrolysis	962:978	slower hydrolysis of CDP, ITP, GTP, CTP, ADP, and UTP	962:1014	Consistent with the enzyme expressed in mammalian cells, this recombinant NTPDase6 efficiently hydrolyzes GDP, IDP, and UDP (specific activity of approximately 50000 micromol mg(-1) h(-1)), with slower hydrolysis of CDP, ITP, GTP, CTP, ADP, and UTP and virtually no hydrolysis of ATP.
14529283	2	2	theme	oligomeric	393:402	arg1	NTPDases1-4					377:387	NTPDases1-4	377:387	NTPDases1-4	377:387	NTPDases1-4 are oligomeric integral membrane proteins, whereas NTPDase5 (CD39L4) and NTPDase6 (CD39L2) are soluble monomeric enzymes, making them more amenable to thorough structural and functional analyses than the membrane-bound forms.
14529283	2	2	theme	oligomeric	393:402	arg1	proteins					422:429	oligomeric integral membrane proteins	393:429	oligomeric integral membrane proteins	393:429	NTPDases1-4 are oligomeric integral membrane proteins, whereas NTPDase5 (CD39L4) and NTPDase6 (CD39L2) are soluble monomeric enzymes, making them more amenable to thorough structural and functional analyses than the membrane-bound forms.
14529283	6	3	theme	soluble	1404:1410	arg1	NTPDase6					1412:1419	soluble NTPDase6	1404:1419	soluble NTPDase6	1404:1419	The secondary structure of the refolded enzyme was determined by circular dichroism to be 33% alpha-helix, 18% beta-sheet, and 49% random coil, consistent with the secondary structure predicted from the amino acid sequence of soluble NTPDase6.
14529283	1	4	theme	important	299:307	arg1	clotting					347:354	blood clotting	341:354	blood clotting	341:354	The ectonucleoside triphosphate diphosphohydrolases (NTPDases) control extracellular nucleotide concentrations, thereby modulating many important biological responses, including blood clotting and pain perception.
14529283	1	4	theme	important	299:307	arg1	perception					365:374	pain perception	360:374	pain perception	360:374	The ectonucleoside triphosphate diphosphohydrolases (NTPDases) control extracellular nucleotide concentrations, thereby modulating many important biological responses, including blood clotting and pain perception.
14529283	1	4	theme	important	299:307	arg1	responses					320:328	many important biological responses	294:328	many important biological responses	294:328	The ectonucleoside triphosphate diphosphohydrolases (NTPDases) control extracellular nucleotide concentrations, thereby modulating many important biological responses, including blood clotting and pain perception.
14529283	3	5	theme	human	751:755	arg1	NTPDase6					757:764	human NTPDase6	751:764	human NTPDase6	751:764	Therefore, we report here the bacterial expression, refolding, purification, and biochemical characterization of the soluble portion of human NTPDase6.
14529283	6	6	theme	49	1305:1306	arg1	%					1307:1307	%	1307:1307	%	1307:1307	The secondary structure of the refolded enzyme was determined by circular dichroism to be 33% alpha-helix, 18% beta-sheet, and 49% random coil, consistent with the secondary structure predicted from the amino acid sequence of soluble NTPDase6.
14529283	1	7	theme	ectonucleoside	167:180	arg1	NTPDases					216:223	NTPDases	216:223	NTPDases	216:223	The ectonucleoside triphosphate diphosphohydrolases (NTPDases) control extracellular nucleotide concentrations, thereby modulating many important biological responses, including blood clotting and pain perception.
14529283	1	7	theme	ectonucleoside	167:180	arg1	diphosphohydrolases					195:213	The ectonucleoside triphosphate diphosphohydrolases	163:213	The ectonucleoside triphosphate diphosphohydrolases (NTPDases)	163:224	The ectonucleoside triphosphate diphosphohydrolases (NTPDases) control extracellular nucleotide concentrations, thereby modulating many important biological responses, including blood clotting and pain perception.
14529283	9	8	theme	other	1823:1827	arg1	residues					1843:1850	the other four cysteine residues	1819:1850	the other four cysteine residues	1819:1850	The disulfide pairing of the other four cysteine residues was determined as Cys(249)-Cys(280) and Cys(340)-Cys(354) by HPLC and mass spectral analysis of tryptic peptides.
14529283	6	9	theme	amino	1381:1385	arg1	sequence					1392:1399	the amino acid sequence	1377:1399	the amino acid sequence of soluble NTPDase6	1377:1419	The secondary structure of the refolded enzyme was determined by circular dichroism to be 33% alpha-helix, 18% beta-sheet, and 49% random coil, consistent with the secondary structure predicted from the amino acid sequence of soluble NTPDase6.
14529283	9	10	theme	mass	1922:1925	arg1	analysis					1936:1943	mass spectral analysis	1922:1943	mass spectral analysis	1922:1943	The disulfide pairing of the other four cysteine residues was determined as Cys(249)-Cys(280) and Cys(340)-Cys(354) by HPLC and mass spectral analysis of tryptic peptides.
14529283	0	11	theme	nucleotidase	108:119	arg1	determination					59:71	disulfide bond determination	44:71	disulfide bond determination	44:71	Bacterial expression, characterization, and disulfide bond determination of soluble human NTPDase6 (CD39L2) nucleotidase: implications for structure and function.
14529283	0	11	theme	nucleotidase	108:119	arg1	characterization					22:37	characterization	22:37	characterization	22:37	Bacterial expression, characterization, and disulfide bond determination of soluble human NTPDase6 (CD39L2) nucleotidase: implications for structure and function.
14529283	0	11	theme	nucleotidase	108:119	arg1	expression					10:19	Bacterial expression	0:19	Bacterial expression	0:19	Bacterial expression, characterization, and disulfide bond determination of soluble human NTPDase6 (CD39L2) nucleotidase: implications for structure and function.
14529283	8	12	theme	cysteine	1588:1595	arg1	Mutation					1558:1565	Mutation	1558:1565	Mutation of this nonconserved cysteine	1558:1595	Mutation of this nonconserved cysteine resulted in an enzyme very similar to wild type in its enzymology and secondary structure, indicating that this cysteine exists as a free sulfhydryl and is not essential for structure or function.
14529283	6	13	theme	refolded	1209:1216	arg1	enzyme					1218:1223	the refolded enzyme	1205:1223	the refolded enzyme	1205:1223	The secondary structure of the refolded enzyme was determined by circular dichroism to be 33% alpha-helix, 18% beta-sheet, and 49% random coil, consistent with the secondary structure predicted from the amino acid sequence of soluble NTPDase6.
14529283	4	14	theme	micromol	933:940	arg1	-1					951:952	-1	951:952	-1	951:952	Consistent with the enzyme expressed in mammalian cells, this recombinant NTPDase6 efficiently hydrolyzes GDP, IDP, and UDP (specific activity of approximately 50000 micromol mg(-1) h(-1)), with slower hydrolysis of CDP, ITP, GTP, CTP, ADP, and UTP and virtually no hydrolysis of ATP.
14529283	4	14	theme	micromol	933:940	arg1	h					949:949	approximately 50000 micromol mg(-1) h	913:949	approximately 50000 micromol mg(-1) h(-1)	913:953	Consistent with the enzyme expressed in mammalian cells, this recombinant NTPDase6 efficiently hydrolyzes GDP, IDP, and UDP (specific activity of approximately 50000 micromol mg(-1) h(-1)), with slower hydrolysis of CDP, ITP, GTP, CTP, ADP, and UTP and virtually no hydrolysis of ATP.
14529283	9	15	theme	tryptic	1948:1954	arg1	peptides					1956:1963	tryptic peptides	1948:1963	tryptic peptides	1948:1963	The disulfide pairing of the other four cysteine residues was determined as Cys(249)-Cys(280) and Cys(340)-Cys(354) by HPLC and mass spectral analysis of tryptic peptides.
14529283	4	16	dep	hydrolysis	969:978	arg1	hydrolysis					1033:1042	no hydrolysis	1030:1042	no hydrolysis of ATP	1030:1049	Consistent with the enzyme expressed in mammalian cells, this recombinant NTPDase6 efficiently hydrolyzes GDP, IDP, and UDP (specific activity of approximately 50000 micromol mg(-1) h(-1)), with slower hydrolysis of CDP, ITP, GTP, CTP, ADP, and UTP and virtually no hydrolysis of ATP.
14529283	9	17	theme	disulfide	1798:1806	arg1	-Cys					1878:1881	Cys(249)-Cys	1870:1881	Cys(249)-Cys(280)	1870:1886	The disulfide pairing of the other four cysteine residues was determined as Cys(249)-Cys(280) and Cys(340)-Cys(354) by HPLC and mass spectral analysis of tryptic peptides.
14529283	9	17	theme	disulfide	1798:1806	arg1	-Cys					1900:1903	Cys(340)-Cys	1892:1903	Cys(340)-Cys(354)	1892:1908	The disulfide pairing of the other four cysteine residues was determined as Cys(249)-Cys(280) and Cys(340)-Cys(354) by HPLC and mass spectral analysis of tryptic peptides.
14529283	9	17	theme	disulfide	1798:1806	arg1	pairing					1808:1814	The disulfide pairing	1794:1814	The disulfide pairing of the other four cysteine residues	1794:1850	The disulfide pairing of the other four cysteine residues was determined as Cys(249)-Cys(280) and Cys(340)-Cys(354) by HPLC and mass spectral analysis of tryptic peptides.
14529283	6	18	theme	secondary	1182:1190	arg1	%					1270:1270	33% alpha-helix	1268:1282	33% alpha-helix	1268:1282	The secondary structure of the refolded enzyme was determined by circular dichroism to be 33% alpha-helix, 18% beta-sheet, and 49% random coil, consistent with the secondary structure predicted from the amino acid sequence of soluble NTPDase6.
14529283	6	18	theme	secondary	1182:1190	arg1	structure					1192:1200	The secondary structure	1178:1200	The secondary structure of the refolded enzyme	1178:1223	The secondary structure of the refolded enzyme was determined by circular dichroism to be 33% alpha-helix, 18% beta-sheet, and 49% random coil, consistent with the secondary structure predicted from the amino acid sequence of soluble NTPDase6.
14529283	8	19	theme	similar	1624:1630	arg1	enzyme					1612:1617	an enzyme	1609:1617	an enzyme very similar to wild type in its enzymology and secondary structure	1609:1685	Mutation of this nonconserved cysteine resulted in an enzyme very similar to wild type in its enzymology and secondary structure, indicating that this cysteine exists as a free sulfhydryl and is not essential for structure or function.
14529283	7	20	theme	residues	1448:1455	arg1	Four					1422:1425	Four	1422:1425	Four	1422:1425	Four of the five cysteine residues in the soluble NTPDase6 are highly conserved among all the NTPDases, while the fifth residue is not.
14529283	7	20	theme	residues	1448:1455	arg1	residues					1448:1455	the five cysteine residues	1430:1455	the five cysteine residues in the soluble NTPDase6	1430:1479	Four of the five cysteine residues in the soluble NTPDase6 are highly conserved among all the NTPDases, while the fifth residue is not.
14529283	4	21	theme	slower	962:967	arg1	hydrolysis					969:978	slower hydrolysis	962:978	slower hydrolysis of CDP, ITP, GTP, CTP, ADP, and UTP	962:1014	Consistent with the enzyme expressed in mammalian cells, this recombinant NTPDase6 efficiently hydrolyzes GDP, IDP, and UDP (specific activity of approximately 50000 micromol mg(-1) h(-1)), with slower hydrolysis of CDP, ITP, GTP, CTP, ADP, and UTP and virtually no hydrolysis of ATP.
14529283	3	22	theme	bacterial	645:653	arg1	expression					655:664	the bacterial expression	641:664	the bacterial expression	641:664	Therefore, we report here the bacterial expression, refolding, purification, and biochemical characterization of the soluble portion of human NTPDase6.
14529283	8	23	theme	wild	1635:1638	arg1	type					1640:1643	wild type	1635:1643	wild type in its enzymology and secondary structure	1635:1685	Mutation of this nonconserved cysteine resulted in an enzyme very similar to wild type in its enzymology and secondary structure, indicating that this cysteine exists as a free sulfhydryl and is not essential for structure or function.
14529283	2	24	theme	membrane-bound	593:606	arg1	forms					608:612	the membrane-bound forms	589:612	the membrane-bound forms	589:612	NTPDases1-4 are oligomeric integral membrane proteins, whereas NTPDase5 (CD39L4) and NTPDase6 (CD39L2) are soluble monomeric enzymes, making them more amenable to thorough structural and functional analyses than the membrane-bound forms.
14529283	0	25	theme	soluble	76:82	arg1	nucleotidase					108:119	soluble human NTPDase6 (CD39L2) nucleotidase	76:119	soluble human NTPDase6 (CD39L2) nucleotidase	76:119	Bacterial expression, characterization, and disulfide bond determination of soluble human NTPDase6 (CD39L2) nucleotidase: implications for structure and function.
14529283	9	26	theme	cysteine	1834:1841	arg1	residues					1843:1850	the other four cysteine residues	1819:1850	the other four cysteine residues	1819:1850	The disulfide pairing of the other four cysteine residues was determined as Cys(249)-Cys(280) and Cys(340)-Cys(354) by HPLC and mass spectral analysis of tryptic peptides.
14529283	4	27	theme	mammalian	807:815	arg1	cells					817:821	mammalian cells	807:821	mammalian cells	807:821	Consistent with the enzyme expressed in mammalian cells, this recombinant NTPDase6 efficiently hydrolyzes GDP, IDP, and UDP (specific activity of approximately 50000 micromol mg(-1) h(-1)), with slower hydrolysis of CDP, ITP, GTP, CTP, ADP, and UTP and virtually no hydrolysis of ATP.
14529283	0	28	theme	NTPDase6	90:97	arg1	nucleotidase					108:119	soluble human NTPDase6 (CD39L2) nucleotidase	76:119	soluble human NTPDase6 (CD39L2) nucleotidase	76:119	Bacterial expression, characterization, and disulfide bond determination of soluble human NTPDase6 (CD39L2) nucleotidase: implications for structure and function.
14529283	8	29	theme	free	1730:1733	arg1	sulfhydryl					1735:1744	a free sulfhydryl	1728:1744	a free sulfhydryl	1728:1744	Mutation of this nonconserved cysteine resulted in an enzyme very similar to wild type in its enzymology and secondary structure, indicating that this cysteine exists as a free sulfhydryl and is not essential for structure or function.
14529283	7	30	theme	fifth	1536:1540	arg1	residue					1542:1548	the fifth residue	1532:1548	the fifth residue	1532:1548	Four of the five cysteine residues in the soluble NTPDase6 are highly conserved among all the NTPDases, while the fifth residue is not.
14529283	2	31	theme	thorough	540:547	arg1	analyses					575:582	thorough structural and functional analyses	540:582	thorough structural and functional analyses than the membrane-bound forms	540:612	NTPDases1-4 are oligomeric integral membrane proteins, whereas NTPDase5 (CD39L4) and NTPDase6 (CD39L2) are soluble monomeric enzymes, making them more amenable to thorough structural and functional analyses than the membrane-bound forms.
14529283	2	32	dep	proteins	422:429	arg1	whereas					432:438	whereas	432:438	whereas	432:438	NTPDases1-4 are oligomeric integral membrane proteins, whereas NTPDase5 (CD39L4) and NTPDase6 (CD39L2) are soluble monomeric enzymes, making them more amenable to thorough structural and functional analyses than the membrane-bound forms.
14529283	0	33	theme	CD39L2	100:105	arg1	nucleotidase					108:119	soluble human NTPDase6 (CD39L2) nucleotidase	76:119	soluble human NTPDase6 (CD39L2) nucleotidase	76:119	Bacterial expression, characterization, and disulfide bond determination of soluble human NTPDase6 (CD39L2) nucleotidase: implications for structure and function.
14529283	8	34	theme	secondary	1667:1675	arg1	structure					1677:1685	secondary structure	1667:1685	secondary structure	1667:1685	Mutation of this nonconserved cysteine resulted in an enzyme very similar to wild type in its enzymology and secondary structure, indicating that this cysteine exists as a free sulfhydryl and is not essential for structure or function.
14529283	10	35	theme	cysteine	1995:2002	arg1	residues					2004:2011	these cysteine residues	1989:2011	these cysteine residues	1989:2011	Due to conservation of these cysteine residues, these two disulfide bonds are likely to exist in all NTPDases.
14529283	0	36	theme	Bacterial	0:8	arg1	expression					10:19	Bacterial expression	0:19	Bacterial expression	0:19	Bacterial expression, characterization, and disulfide bond determination of soluble human NTPDase6 (CD39L2) nucleotidase: implications for structure and function.
14529283	1	37	theme	biological	309:318	arg1	clotting					347:354	blood clotting	341:354	blood clotting	341:354	The ectonucleoside triphosphate diphosphohydrolases (NTPDases) control extracellular nucleotide concentrations, thereby modulating many important biological responses, including blood clotting and pain perception.
14529283	1	37	theme	biological	309:318	arg1	perception					365:374	pain perception	360:374	pain perception	360:374	The ectonucleoside triphosphate diphosphohydrolases (NTPDases) control extracellular nucleotide concentrations, thereby modulating many important biological responses, including blood clotting and pain perception.
14529283	1	37	theme	biological	309:318	arg1	responses					320:328	many important biological responses	294:328	many important biological responses	294:328	The ectonucleoside triphosphate diphosphohydrolases (NTPDases) control extracellular nucleotide concentrations, thereby modulating many important biological responses, including blood clotting and pain perception.
14529283	1	38	theme	blood	341:345	arg1	clotting					347:354	blood clotting	341:354	blood clotting	341:354	The ectonucleoside triphosphate diphosphohydrolases (NTPDases) control extracellular nucleotide concentrations, thereby modulating many important biological responses, including blood clotting and pain perception.
14529283	2	39	theme	functional	564:573	arg1	analyses					575:582	thorough structural and functional analyses	540:582	thorough structural and functional analyses than the membrane-bound forms	540:612	NTPDases1-4 are oligomeric integral membrane proteins, whereas NTPDase5 (CD39L4) and NTPDase6 (CD39L2) are soluble monomeric enzymes, making them more amenable to thorough structural and functional analyses than the membrane-bound forms.
14529283	2	40	theme	monomeric	492:500	arg1	NTPDase5					440:447	NTPDase5	440:447	NTPDase5 (CD39L4)	440:456	NTPDases1-4 are oligomeric integral membrane proteins, whereas NTPDase5 (CD39L4) and NTPDase6 (CD39L2) are soluble monomeric enzymes, making them more amenable to thorough structural and functional analyses than the membrane-bound forms.
14529283	2	40	theme	monomeric	492:500	arg1	enzymes					502:508	soluble monomeric enzymes	484:508	soluble monomeric enzymes	484:508	NTPDases1-4 are oligomeric integral membrane proteins, whereas NTPDase5 (CD39L4) and NTPDase6 (CD39L2) are soluble monomeric enzymes, making them more amenable to thorough structural and functional analyses than the membrane-bound forms.
14529283	2	40	theme	monomeric	492:500	arg1	NTPDase6					462:469	NTPDase6	462:469	NTPDase6 (CD39L2)	462:478	NTPDases1-4 are oligomeric integral membrane proteins, whereas NTPDase5 (CD39L4) and NTPDase6 (CD39L2) are soluble monomeric enzymes, making them more amenable to thorough structural and functional analyses than the membrane-bound forms.
14529283	0	41	theme	disulfide	44:52	arg1	determination					59:71	disulfide bond determination	44:71	disulfide bond determination	44:71	Bacterial expression, characterization, and disulfide bond determination of soluble human NTPDase6 (CD39L2) nucleotidase: implications for structure and function.
14529283	4	42	theme	recombinant	829:839	arg1	NTPDase6					841:848	this recombinant NTPDase6	824:848	this recombinant NTPDase6	824:848	Consistent with the enzyme expressed in mammalian cells, this recombinant NTPDase6 efficiently hydrolyzes GDP, IDP, and UDP (specific activity of approximately 50000 micromol mg(-1) h(-1)), with slower hydrolysis of CDP, ITP, GTP, CTP, ADP, and UTP and virtually no hydrolysis of ATP.
14529283	6	43	theme	secondary	1342:1350	arg1	structure					1352:1360	the secondary structure	1338:1360	the secondary structure predicted from the amino acid sequence of soluble NTPDase6	1338:1419	The secondary structure of the refolded enzyme was determined by circular dichroism to be 33% alpha-helix, 18% beta-sheet, and 49% random coil, consistent with the secondary structure predicted from the amino acid sequence of soluble NTPDase6.
14529283	1	44	theme	extracellular	234:246	arg1	concentrations					259:272	extracellular nucleotide concentrations	234:272	extracellular nucleotide concentrations	234:272	The ectonucleoside triphosphate diphosphohydrolases (NTPDases) control extracellular nucleotide concentrations, thereby modulating many important biological responses, including blood clotting and pain perception.
14529283	7	45	from	residues	1448:1455	arg1	NTPDase6					1472:1479	the soluble NTPDase6	1460:1479	the soluble NTPDase6	1460:1479	Four of the five cysteine residues in the soluble NTPDase6 are highly conserved among all the NTPDases, while the fifth residue is not.
14529283	9	46	theme	Cys	1892:1894	arg1	354					1905:1907	354	1905:1907	354	1905:1907	The disulfide pairing of the other four cysteine residues was determined as Cys(249)-Cys(280) and Cys(340)-Cys(354) by HPLC and mass spectral analysis of tryptic peptides.
14529283	9	46	theme	Cys	1892:1894	arg1	-Cys					1900:1903	Cys(340)-Cys	1892:1903	Cys(340)-Cys(354)	1892:1908	The disulfide pairing of the other four cysteine residues was determined as Cys(249)-Cys(280) and Cys(340)-Cys(354) by HPLC and mass spectral analysis of tryptic peptides.
14529283	9	46	theme	Cys	1892:1894	arg1	pairing					1808:1814	The disulfide pairing	1794:1814	The disulfide pairing of the other four cysteine residues	1794:1850	The disulfide pairing of the other four cysteine residues was determined as Cys(249)-Cys(280) and Cys(340)-Cys(354) by HPLC and mass spectral analysis of tryptic peptides.
14529283	11	47	theme	structural	2079:2088	arg1	model					2090:2094	A structural model	2077:2094	A structural model	2077:2094	A structural model for NTPDase6, incorporating these and other findings obtained with other NTPDases, is proposed.
14529283	2	48	theme	integral	404:411	arg1	NTPDases1-4					377:387	NTPDases1-4	377:387	NTPDases1-4	377:387	NTPDases1-4 are oligomeric integral membrane proteins, whereas NTPDase5 (CD39L4) and NTPDase6 (CD39L2) are soluble monomeric enzymes, making them more amenable to thorough structural and functional analyses than the membrane-bound forms.
14529283	2	48	theme	integral	404:411	arg1	proteins					422:429	oligomeric integral membrane proteins	393:429	oligomeric integral membrane proteins	393:429	NTPDases1-4 are oligomeric integral membrane proteins, whereas NTPDase5 (CD39L4) and NTPDase6 (CD39L2) are soluble monomeric enzymes, making them more amenable to thorough structural and functional analyses than the membrane-bound forms.
14529283	4	49	theme	specific	892:899	arg1	activity					901:908	specific activity	892:908	specific activity of approximately 50000 micromol mg(-1) h(-1)	892:953	Consistent with the enzyme expressed in mammalian cells, this recombinant NTPDase6 efficiently hydrolyzes GDP, IDP, and UDP (specific activity of approximately 50000 micromol mg(-1) h(-1)), with slower hydrolysis of CDP, ITP, GTP, CTP, ADP, and UTP and virtually no hydrolysis of ATP.
14529283	4	50	theme	UTP	1012:1014	arg1	hydrolysis					969:978	slower hydrolysis	962:978	slower hydrolysis of CDP, ITP, GTP, CTP, ADP, and UTP	962:1014	Consistent with the enzyme expressed in mammalian cells, this recombinant NTPDase6 efficiently hydrolyzes GDP, IDP, and UDP (specific activity of approximately 50000 micromol mg(-1) h(-1)), with slower hydrolysis of CDP, ITP, GTP, CTP, ADP, and UTP and virtually no hydrolysis of ATP.
14529283	3	51	theme	soluble	732:738	arg1	portion					740:746	the soluble portion	728:746	the soluble portion of human NTPDase6	728:764	Therefore, we report here the bacterial expression, refolding, purification, and biochemical characterization of the soluble portion of human NTPDase6.
14529283	6	52	theme	random	1309:1314	arg1	coil					1316:1319	49% random coil	1305:1319	49% random coil	1305:1319	The secondary structure of the refolded enzyme was determined by circular dichroism to be 33% alpha-helix, 18% beta-sheet, and 49% random coil, consistent with the secondary structure predicted from the amino acid sequence of soluble NTPDase6.
14529283	1	53	theme	many	294:297	arg1	clotting					347:354	blood clotting	341:354	blood clotting	341:354	The ectonucleoside triphosphate diphosphohydrolases (NTPDases) control extracellular nucleotide concentrations, thereby modulating many important biological responses, including blood clotting and pain perception.
14529283	1	53	theme	many	294:297	arg1	perception					365:374	pain perception	360:374	pain perception	360:374	The ectonucleoside triphosphate diphosphohydrolases (NTPDases) control extracellular nucleotide concentrations, thereby modulating many important biological responses, including blood clotting and pain perception.
14529283	1	53	theme	many	294:297	arg1	responses					320:328	many important biological responses	294:328	many important biological responses	294:328	The ectonucleoside triphosphate diphosphohydrolases (NTPDases) control extracellular nucleotide concentrations, thereby modulating many important biological responses, including blood clotting and pain perception.
14529283	2	54	theme	soluble	484:490	arg1	NTPDase5					440:447	NTPDase5	440:447	NTPDase5 (CD39L4)	440:456	NTPDases1-4 are oligomeric integral membrane proteins, whereas NTPDase5 (CD39L4) and NTPDase6 (CD39L2) are soluble monomeric enzymes, making them more amenable to thorough structural and functional analyses than the membrane-bound forms.
14529283	2	54	theme	soluble	484:490	arg1	enzymes					502:508	soluble monomeric enzymes	484:508	soluble monomeric enzymes	484:508	NTPDases1-4 are oligomeric integral membrane proteins, whereas NTPDase5 (CD39L4) and NTPDase6 (CD39L2) are soluble monomeric enzymes, making them more amenable to thorough structural and functional analyses than the membrane-bound forms.
14529283	2	54	theme	soluble	484:490	arg1	NTPDase6					462:469	NTPDase6	462:469	NTPDase6 (CD39L2)	462:478	NTPDases1-4 are oligomeric integral membrane proteins, whereas NTPDase5 (CD39L4) and NTPDase6 (CD39L2) are soluble monomeric enzymes, making them more amenable to thorough structural and functional analyses than the membrane-bound forms.
14529283	3	55	theme	NTPDase6	757:764	arg1	portion					740:746	the soluble portion	728:746	the soluble portion of human NTPDase6	728:764	Therefore, we report here the bacterial expression, refolding, purification, and biochemical characterization of the soluble portion of human NTPDase6.
14529283	6	56	with	consistent	1322:1331	arg1	structure					1352:1360	the secondary structure	1338:1360	the secondary structure predicted from the amino acid sequence of soluble NTPDase6	1338:1419	The secondary structure of the refolded enzyme was determined by circular dichroism to be 33% alpha-helix, 18% beta-sheet, and 49% random coil, consistent with the secondary structure predicted from the amino acid sequence of soluble NTPDase6.
14529283	6	57	theme	acid	1387:1390	arg1	sequence					1392:1399	the amino acid sequence	1377:1399	the amino acid sequence of soluble NTPDase6	1377:1419	The secondary structure of the refolded enzyme was determined by circular dichroism to be 33% alpha-helix, 18% beta-sheet, and 49% random coil, consistent with the secondary structure predicted from the amino acid sequence of soluble NTPDase6.
14529283	1	58	theme	triphosphate	182:193	arg1	NTPDases					216:223	NTPDases	216:223	NTPDases	216:223	The ectonucleoside triphosphate diphosphohydrolases (NTPDases) control extracellular nucleotide concentrations, thereby modulating many important biological responses, including blood clotting and pain perception.
14529283	1	58	theme	triphosphate	182:193	arg1	diphosphohydrolases					195:213	The ectonucleoside triphosphate diphosphohydrolases	163:213	The ectonucleoside triphosphate diphosphohydrolases (NTPDases)	163:224	The ectonucleoside triphosphate diphosphohydrolases (NTPDases) control extracellular nucleotide concentrations, thereby modulating many important biological responses, including blood clotting and pain perception.
14529283	4	59	theme	ATP	1047:1049	arg1	hydrolysis					1033:1042	no hydrolysis	1030:1042	no hydrolysis of ATP	1030:1049	Consistent with the enzyme expressed in mammalian cells, this recombinant NTPDase6 efficiently hydrolyzes GDP, IDP, and UDP (specific activity of approximately 50000 micromol mg(-1) h(-1)), with slower hydrolysis of CDP, ITP, GTP, CTP, ADP, and UTP and virtually no hydrolysis of ATP.
14529283	9	60	theme	spectral	1927:1934	arg1	analysis					1936:1943	mass spectral analysis	1922:1943	mass spectral analysis	1922:1943	The disulfide pairing of the other four cysteine residues was determined as Cys(249)-Cys(280) and Cys(340)-Cys(354) by HPLC and mass spectral analysis of tryptic peptides.
14529283	6	61	theme	enzyme	1218:1223	arg1	%					1270:1270	33% alpha-helix	1268:1282	33% alpha-helix	1268:1282	The secondary structure of the refolded enzyme was determined by circular dichroism to be 33% alpha-helix, 18% beta-sheet, and 49% random coil, consistent with the secondary structure predicted from the amino acid sequence of soluble NTPDase6.
14529283	6	61	theme	enzyme	1218:1223	arg1	structure					1192:1200	The secondary structure	1178:1200	The secondary structure of the refolded enzyme	1178:1223	The secondary structure of the refolded enzyme was determined by circular dichroism to be 33% alpha-helix, 18% beta-sheet, and 49% random coil, consistent with the secondary structure predicted from the amino acid sequence of soluble NTPDase6.
14529283	8	62	theme	nonconserved	1575:1586	arg1	cysteine					1588:1595	this nonconserved cysteine	1570:1595	this nonconserved cysteine	1570:1595	Mutation of this nonconserved cysteine resulted in an enzyme very similar to wild type in its enzymology and secondary structure, indicating that this cysteine exists as a free sulfhydryl and is not essential for structure or function.
14529283	4	63	dep	GDP	873:875	arg1	activity					901:908	specific activity	892:908	specific activity of approximately 50000 micromol mg(-1) h(-1)	892:953	Consistent with the enzyme expressed in mammalian cells, this recombinant NTPDase6 efficiently hydrolyzes GDP, IDP, and UDP (specific activity of approximately 50000 micromol mg(-1) h(-1)), with slower hydrolysis of CDP, ITP, GTP, CTP, ADP, and UTP and virtually no hydrolysis of ATP.
14529283	7	64	theme	soluble	1464:1470	arg1	NTPDase6					1472:1479	the soluble NTPDase6	1460:1479	the soluble NTPDase6	1460:1479	Four of the five cysteine residues in the soluble NTPDase6 are highly conserved among all the NTPDases, while the fifth residue is not.
14529283	4	65	theme	h	949:949	arg1	activity					901:908	specific activity	892:908	specific activity of approximately 50000 micromol mg(-1) h(-1)	892:953	Consistent with the enzyme expressed in mammalian cells, this recombinant NTPDase6 efficiently hydrolyzes GDP, IDP, and UDP (specific activity of approximately 50000 micromol mg(-1) h(-1)), with slower hydrolysis of CDP, ITP, GTP, CTP, ADP, and UTP and virtually no hydrolysis of ATP.
14529283	11	66	theme	other	2163:2167	arg1	NTPDases					2169:2176	other NTPDases	2163:2176	other NTPDases	2163:2176	A structural model for NTPDase6, incorporating these and other findings obtained with other NTPDases, is proposed.
14529283	5	67	theme	mammalian	1161:1169	arg1	cells					1171:1175	mammalian cells	1161:1175	mammalian cells	1161:1175	The K(m) for GDP (130 +/- 30 microM) is similar to that determined for the soluble rat NTPDase6 expressed in mammalian cells.
14529283	9	68	theme	peptides	1956:1963	arg1	HPLC					1913:1916	HPLC	1913:1916	HPLC	1913:1916	The disulfide pairing of the other four cysteine residues was determined as Cys(249)-Cys(280) and Cys(340)-Cys(354) by HPLC and mass spectral analysis of tryptic peptides.
14529283	9	68	theme	peptides	1956:1963	arg1	analysis					1936:1943	mass spectral analysis	1922:1943	mass spectral analysis	1922:1943	The disulfide pairing of the other four cysteine residues was determined as Cys(249)-Cys(280) and Cys(340)-Cys(354) by HPLC and mass spectral analysis of tryptic peptides.
14529283	7	69	theme	cysteine	1439:1446	arg1	residues					1448:1455	the five cysteine residues	1430:1455	the five cysteine residues in the soluble NTPDase6	1430:1479	Four of the five cysteine residues in the soluble NTPDase6 are highly conserved among all the NTPDases, while the fifth residue is not.
14529283	4	70	theme	mg	942:943	arg1	-1					951:952	-1	951:952	-1	951:952	Consistent with the enzyme expressed in mammalian cells, this recombinant NTPDase6 efficiently hydrolyzes GDP, IDP, and UDP (specific activity of approximately 50000 micromol mg(-1) h(-1)), with slower hydrolysis of CDP, ITP, GTP, CTP, ADP, and UTP and virtually no hydrolysis of ATP.
14529283	4	70	theme	mg	942:943	arg1	h					949:949	approximately 50000 micromol mg(-1) h	913:949	approximately 50000 micromol mg(-1) h(-1)	913:953	Consistent with the enzyme expressed in mammalian cells, this recombinant NTPDase6 efficiently hydrolyzes GDP, IDP, and UDP (specific activity of approximately 50000 micromol mg(-1) h(-1)), with slower hydrolysis of CDP, ITP, GTP, CTP, ADP, and UTP and virtually no hydrolysis of ATP.
14529283	8	71	from	type	1640:1643	arg1	enzymology					1652:1661	its enzymology	1648:1661	its enzymology	1648:1661	Mutation of this nonconserved cysteine resulted in an enzyme very similar to wild type in its enzymology and secondary structure, indicating that this cysteine exists as a free sulfhydryl and is not essential for structure or function.
14529283	8	71	from	type	1640:1643	arg1	structure					1677:1685	secondary structure	1667:1685	secondary structure	1667:1685	Mutation of this nonconserved cysteine resulted in an enzyme very similar to wild type in its enzymology and secondary structure, indicating that this cysteine exists as a free sulfhydryl and is not essential for structure or function.
14529283	6	72	theme	alpha-helix	1272:1282	arg1	%					1270:1270	33% alpha-helix	1268:1282	33% alpha-helix	1268:1282	The secondary structure of the refolded enzyme was determined by circular dichroism to be 33% alpha-helix, 18% beta-sheet, and 49% random coil, consistent with the secondary structure predicted from the amino acid sequence of soluble NTPDase6.
14529283	6	72	theme	alpha-helix	1272:1282	arg1	structure					1192:1200	The secondary structure	1178:1200	The secondary structure of the refolded enzyme	1178:1223	The secondary structure of the refolded enzyme was determined by circular dichroism to be 33% alpha-helix, 18% beta-sheet, and 49% random coil, consistent with the secondary structure predicted from the amino acid sequence of soluble NTPDase6.
14529283	5	73	theme	rat	1135:1137	arg1	NTPDase6					1139:1146	the soluble rat NTPDase6	1123:1146	the soluble rat NTPDase6 expressed in mammalian cells	1123:1175	The K(m) for GDP (130 +/- 30 microM) is similar to that determined for the soluble rat NTPDase6 expressed in mammalian cells.
14529283	0	74	theme	human	84:88	arg1	nucleotidase					108:119	soluble human NTPDase6 (CD39L2) nucleotidase	76:119	soluble human NTPDase6 (CD39L2) nucleotidase	76:119	Bacterial expression, characterization, and disulfide bond determination of soluble human NTPDase6 (CD39L2) nucleotidase: implications for structure and function.
14529283	6	75	theme	NTPDase6	1412:1419	arg1	sequence					1392:1399	the amino acid sequence	1377:1399	the amino acid sequence of soluble NTPDase6	1377:1419	The secondary structure of the refolded enzyme was determined by circular dichroism to be 33% alpha-helix, 18% beta-sheet, and 49% random coil, consistent with the secondary structure predicted from the amino acid sequence of soluble NTPDase6.
14529283	2	76	theme	structural	549:558	arg1	analyses					575:582	thorough structural and functional analyses	540:582	thorough structural and functional analyses than the membrane-bound forms	540:612	NTPDases1-4 are oligomeric integral membrane proteins, whereas NTPDase5 (CD39L4) and NTPDase6 (CD39L2) are soluble monomeric enzymes, making them more amenable to thorough structural and functional analyses than the membrane-bound forms.
14529283	9	77	theme	residues	1843:1850	arg1	-Cys					1878:1881	Cys(249)-Cys	1870:1881	Cys(249)-Cys(280)	1870:1886	The disulfide pairing of the other four cysteine residues was determined as Cys(249)-Cys(280) and Cys(340)-Cys(354) by HPLC and mass spectral analysis of tryptic peptides.
14529283	9	77	theme	residues	1843:1850	arg1	-Cys					1900:1903	Cys(340)-Cys	1892:1903	Cys(340)-Cys(354)	1892:1908	The disulfide pairing of the other four cysteine residues was determined as Cys(249)-Cys(280) and Cys(340)-Cys(354) by HPLC and mass spectral analysis of tryptic peptides.
14529283	9	77	theme	residues	1843:1850	arg1	pairing					1808:1814	The disulfide pairing	1794:1814	The disulfide pairing of the other four cysteine residues	1794:1850	The disulfide pairing of the other four cysteine residues was determined as Cys(249)-Cys(280) and Cys(340)-Cys(354) by HPLC and mass spectral analysis of tryptic peptides.
14529283	6	78	theme	circular	1243:1250	arg1	dichroism					1252:1260	circular dichroism	1243:1260	circular dichroism	1243:1260	The secondary structure of the refolded enzyme was determined by circular dichroism to be 33% alpha-helix, 18% beta-sheet, and 49% random coil, consistent with the secondary structure predicted from the amino acid sequence of soluble NTPDase6.
14529283	10	79	theme	residues	2004:2011	arg1	conservation					1973:1984	conservation	1973:1984	conservation of these cysteine residues	1973:2011	Due to conservation of these cysteine residues, these two disulfide bonds are likely to exist in all NTPDases.
14529283	6	80	theme	%	1307:1307	arg1	coil					1316:1319	49% random coil	1305:1319	49% random coil	1305:1319	The secondary structure of the refolded enzyme was determined by circular dichroism to be 33% alpha-helix, 18% beta-sheet, and 49% random coil, consistent with the secondary structure predicted from the amino acid sequence of soluble NTPDase6.
14529283	4	81	theme	GTP	993:995	arg1	hydrolysis					969:978	slower hydrolysis	962:978	slower hydrolysis of CDP, ITP, GTP, CTP, ADP, and UTP	962:1014	Consistent with the enzyme expressed in mammalian cells, this recombinant NTPDase6 efficiently hydrolyzes GDP, IDP, and UDP (specific activity of approximately 50000 micromol mg(-1) h(-1)), with slower hydrolysis of CDP, ITP, GTP, CTP, ADP, and UTP and virtually no hydrolysis of ATP.
14529283	3	82	theme	biochemical	696:706	arg1	characterization					708:723	biochemical characterization	696:723	biochemical characterization	696:723	Therefore, we report here the bacterial expression, refolding, purification, and biochemical characterization of the soluble portion of human NTPDase6.
14529283	9	83	theme	Cys	1870:1872	arg1	-Cys					1878:1881	Cys(249)-Cys	1870:1881	Cys(249)-Cys(280)	1870:1886	The disulfide pairing of the other four cysteine residues was determined as Cys(249)-Cys(280) and Cys(340)-Cys(354) by HPLC and mass spectral analysis of tryptic peptides.
14529283	9	83	theme	Cys	1870:1872	arg1	pairing					1808:1814	The disulfide pairing	1794:1814	The disulfide pairing of the other four cysteine residues	1794:1850	The disulfide pairing of the other four cysteine residues was determined as Cys(249)-Cys(280) and Cys(340)-Cys(354) by HPLC and mass spectral analysis of tryptic peptides.
14529283	9	83	theme	Cys	1870:1872	arg1	280					1883:1885	280	1883:1885	280	1883:1885	The disulfide pairing of the other four cysteine residues was determined as Cys(249)-Cys(280) and Cys(340)-Cys(354) by HPLC and mass spectral analysis of tryptic peptides.
14529283	4	84	theme	CTP	998:1000	arg1	hydrolysis					969:978	slower hydrolysis	962:978	slower hydrolysis of CDP, ITP, GTP, CTP, ADP, and UTP	962:1014	Consistent with the enzyme expressed in mammalian cells, this recombinant NTPDase6 efficiently hydrolyzes GDP, IDP, and UDP (specific activity of approximately 50000 micromol mg(-1) h(-1)), with slower hydrolysis of CDP, ITP, GTP, CTP, ADP, and UTP and virtually no hydrolysis of ATP.
14529283	6	85	theme	beta-sheet	1289:1298	arg1	%					1287:1287	18% beta-sheet	1285:1298	18% beta-sheet	1285:1298	The secondary structure of the refolded enzyme was determined by circular dichroism to be 33% alpha-helix, 18% beta-sheet, and 49% random coil, consistent with the secondary structure predicted from the amino acid sequence of soluble NTPDase6.
14529283	4	86	theme	CDP	983:985	arg1	hydrolysis					969:978	slower hydrolysis	962:978	slower hydrolysis of CDP, ITP, GTP, CTP, ADP, and UTP	962:1014	Consistent with the enzyme expressed in mammalian cells, this recombinant NTPDase6 efficiently hydrolyzes GDP, IDP, and UDP (specific activity of approximately 50000 micromol mg(-1) h(-1)), with slower hydrolysis of CDP, ITP, GTP, CTP, ADP, and UTP and virtually no hydrolysis of ATP.
14529283	0	87	theme	bond	54:57	arg1	determination					59:71	disulfide bond determination	44:71	disulfide bond determination	44:71	Bacterial expression, characterization, and disulfide bond determination of soluble human NTPDase6 (CD39L2) nucleotidase: implications for structure and function.
14529283	4	88	theme	ITP	988:990	arg1	hydrolysis					969:978	slower hydrolysis	962:978	slower hydrolysis of CDP, ITP, GTP, CTP, ADP, and UTP	962:1014	Consistent with the enzyme expressed in mammalian cells, this recombinant NTPDase6 efficiently hydrolyzes GDP, IDP, and UDP (specific activity of approximately 50000 micromol mg(-1) h(-1)), with slower hydrolysis of CDP, ITP, GTP, CTP, ADP, and UTP and virtually no hydrolysis of ATP.
14529283	3	89	theme	portion	740:746	arg1	purification					678:689	purification	678:689	purification	678:689	Therefore, we report here the bacterial expression, refolding, purification, and biochemical characterization of the soluble portion of human NTPDase6.
14529283	3	89	theme	portion	740:746	arg1	characterization					708:723	biochemical characterization	696:723	biochemical characterization	696:723	Therefore, we report here the bacterial expression, refolding, purification, and biochemical characterization of the soluble portion of human NTPDase6.
14529283	3	89	theme	portion	740:746	arg1	refolding					667:675	refolding	667:675	refolding	667:675	Therefore, we report here the bacterial expression, refolding, purification, and biochemical characterization of the soluble portion of human NTPDase6.
14529283	3	89	theme	portion	740:746	arg1	expression					655:664	the bacterial expression	641:664	the bacterial expression	641:664	Therefore, we report here the bacterial expression, refolding, purification, and biochemical characterization of the soluble portion of human NTPDase6.
14529283	1	90	theme	pain	360:363	arg1	perception					365:374	pain perception	360:374	pain perception	360:374	The ectonucleoside triphosphate diphosphohydrolases (NTPDases) control extracellular nucleotide concentrations, thereby modulating many important biological responses, including blood clotting and pain perception.
14529283	11	91	theme	other	2134:2138	arg1	findings					2140:2147	other findings	2134:2147	other findings	2134:2147	A structural model for NTPDase6, incorporating these and other findings obtained with other NTPDases, is proposed.
14529283	1	92	theme	nucleotide	248:257	arg1	concentrations					259:272	extracellular nucleotide concentrations	234:272	extracellular nucleotide concentrations	234:272	The ectonucleoside triphosphate diphosphohydrolases (NTPDases) control extracellular nucleotide concentrations, thereby modulating many important biological responses, including blood clotting and pain perception.
14529283	0	93	dep	expression	10:19	arg1	implications					122:133	implications	122:133	Bacterial expression, characterization, and disulfide bond determination of soluble human NTPDase6 (CD39L2) nucleotidase: implications for structure and function.	0:161	Bacterial expression, characterization, and disulfide bond determination of soluble human NTPDase6 (CD39L2) nucleotidase: implications for structure and function.
14529283	4	94	with	Consistent	767:776	arg1	enzyme					787:792	the enzyme	783:792	the enzyme expressed in mammalian cells	783:821	Consistent with the enzyme expressed in mammalian cells, this recombinant NTPDase6 efficiently hydrolyzes GDP, IDP, and UDP (specific activity of approximately 50000 micromol mg(-1) h(-1)), with slower hydrolysis of CDP, ITP, GTP, CTP, ADP, and UTP and virtually no hydrolysis of ATP.
14529283	2	95	theme	membrane	413:420	arg1	NTPDases1-4					377:387	NTPDases1-4	377:387	NTPDases1-4	377:387	NTPDases1-4 are oligomeric integral membrane proteins, whereas NTPDase5 (CD39L4) and NTPDase6 (CD39L2) are soluble monomeric enzymes, making them more amenable to thorough structural and functional analyses than the membrane-bound forms.
14529283	2	95	theme	membrane	413:420	arg1	proteins					422:429	oligomeric integral membrane proteins	393:429	oligomeric integral membrane proteins	393:429	NTPDases1-4 are oligomeric integral membrane proteins, whereas NTPDase5 (CD39L4) and NTPDase6 (CD39L2) are soluble monomeric enzymes, making them more amenable to thorough structural and functional analyses than the membrane-bound forms.
14529283	5	96	theme	soluble	1127:1133	arg1	NTPDase6					1139:1146	the soluble rat NTPDase6	1123:1146	the soluble rat NTPDase6 expressed in mammalian cells	1123:1175	The K(m) for GDP (130 +/- 30 microM) is similar to that determined for the soluble rat NTPDase6 expressed in mammalian cells.
2590169	2	0	theme	Dermatan	122:129	arg1	proteoglycans					140:152	Dermatan sulphate proteoglycans	122:152	Dermatan sulphate proteoglycans	122:152	Dermatan sulphate proteoglycans were purified from juvenile human articular cartilage, with a yield of about 2 mg/g wet wt.
2590169	7	1	theme	such	1046:1049	arg1	sites					1051:1055	two such sites	1042:1055	two such sites at residues 5 and 10 for DS-PGI	1042:1087	Sequence analysis of the N-terminal 20 amino acid residues reveals the presence of a single site for the potential substitution of dermatan sulphate at residue 4 of DS-PGII and two such sites at residues 5 and 10 for DS-PGI.
2590169	1	2	dep	proteoglycans	98:110	arg1	proteoglycans					98:110	dermatan sulphate proteoglycans I and II	80:119	dermatan sulphate proteoglycans I and II	80:119	The properties of dermatan sulphate proteoglycans I and II.
2590169	1	2	dep	proteoglycans	98:110	arg1	II					118:119	II	118:119	II	118:119	The properties of dermatan sulphate proteoglycans I and II.
2590169	1	2	dep	proteoglycans	98:110	arg1	I					112:112	I	112:112	I	112:112	The properties of dermatan sulphate proteoglycans I and II.
2590169	7	3	theme	single	950:955	arg1	site					957:960	a single site	948:960	a single site for the potential substitution of dermatan sulphate at residue 4 of DS-PGII	948:1036	Sequence analysis of the N-terminal 20 amino acid residues reveals the presence of a single site for the potential substitution of dermatan sulphate at residue 4 of DS-PGII and two such sites at residues 5 and 10 for DS-PGI.
2590169	7	4	theme	Sequence	865:872	arg1	analysis					874:881	Sequence analysis	865:881	Sequence analysis of the N-terminal 20 amino acid residues	865:922	Sequence analysis of the N-terminal 20 amino acid residues reveals the presence of a single site for the potential substitution of dermatan sulphate at residue 4 of DS-PGII and two such sites at residues 5 and 10 for DS-PGI.
2590169	5	5	theme	SDS/polyacrylamide-gel	536:557	arg1	electrophoresis					559:573	SDS/polyacrylamide-gel electrophoresis	536:573	SDS/polyacrylamide-gel electrophoresis	536:573	The two proteoglycans could not be resolved by agarose/polyacrylamide-gel electrophoresis, but could be resolved by SDS/polyacrylamide-gel electrophoresis, which indicated average Mr values of 200,000 and 98,000 for DS-PGI and DS-PGII respectively.
2590169	5	6	theme	200,000	613:619	arg1	values					603:608	average Mr values	592:608	average Mr values of 200,000 and 98,000 for DS-PGI and DS-PGII	592:653	The two proteoglycans could not be resolved by agarose/polyacrylamide-gel electrophoresis, but could be resolved by SDS/polyacrylamide-gel electrophoresis, which indicated average Mr values of 200,000 and 98,000 for DS-PGI and DS-PGII respectively.
2590169	6	7	theme	Mr	716:717	arg1	44,000					752:757	44,000	752:757	44,000	752:757	After digestion with chondroitin ABC lyase the Mr values of the core proteins were 44,000 for DS-PGI and 43,000 and 47,000 for DS-PGII, with the smaller core protein being predominant in DS-PGII.
2590169	6	7	theme	Mr	716:717	arg1	values					719:724	the Mr values	712:724	the Mr values of the core proteins	712:745	After digestion with chondroitin ABC lyase the Mr values of the core proteins were 44,000 for DS-PGI and 43,000 and 47,000 for DS-PGII, with the smaller core protein being predominant in DS-PGII.
2590169	7	8	theme	sulphate	1005:1012	arg1	substitution					980:991	the potential substitution	966:991	the potential substitution of dermatan sulphate at residue 4 of DS-PGII	966:1036	Sequence analysis of the N-terminal 20 amino acid residues reveals the presence of a single site for the potential substitution of dermatan sulphate at residue 4 of DS-PGII and two such sites at residues 5 and 10 for DS-PGI.
2590169	5	9	theme	98,000	625:630	arg1	values					603:608	average Mr values	592:608	average Mr values of 200,000 and 98,000 for DS-PGI and DS-PGII	592:653	The two proteoglycans could not be resolved by agarose/polyacrylamide-gel electrophoresis, but could be resolved by SDS/polyacrylamide-gel electrophoresis, which indicated average Mr values of 200,000 and 98,000 for DS-PGI and DS-PGII respectively.
2590169	4	10	theme	sulphate	274:281	arg1	proteoglycan					283:294	dermatan sulphate proteoglycan I	265:296	dermatan sulphate proteoglycan I (DS-PGI)	265:305	Both dermatan sulphate proteoglycan I (DS-PGI) and dermatan sulphate proteoglycan II (DS-PGII) were identified and the former was present in greater abundance.
2590169	4	10	theme	sulphate	274:281	arg1	DS-PGI					299:304	DS-PGI	299:304	DS-PGI	299:304	Both dermatan sulphate proteoglycan I (DS-PGI) and dermatan sulphate proteoglycan II (DS-PGII) were identified and the former was present in greater abundance.
2590169	1	11	theme	dermatan	80:87	arg1	proteoglycans					98:110	dermatan sulphate proteoglycans I and II	80:119	dermatan sulphate proteoglycans I and II	80:119	The properties of dermatan sulphate proteoglycans I and II.
2590169	1	11	theme	dermatan	80:87	arg1	II					118:119	II	118:119	II	118:119	The properties of dermatan sulphate proteoglycans I and II.
2590169	1	11	theme	dermatan	80:87	arg1	I					112:112	I	112:112	I	112:112	The properties of dermatan sulphate proteoglycans I and II.
2590169	0	12	theme	sulphate	9:16	arg1	proteoglycans					18:30	Dermatan sulphate proteoglycans	0:30	Dermatan sulphate proteoglycans of human articular cartilage	0:59	Dermatan sulphate proteoglycans of human articular cartilage.
2590169	7	13	theme	sites	1051:1055	arg1	presence					936:943	the presence	932:943	the presence of a single site for the potential substitution of dermatan sulphate at residue 4 of DS-PGII and two such sites at residues 5 and 10 for DS-PGI	932:1087	Sequence analysis of the N-terminal 20 amino acid residues reveals the presence of a single site for the potential substitution of dermatan sulphate at residue 4 of DS-PGII and two such sites at residues 5 and 10 for DS-PGI.
2590169	1	14	theme	sulphate	89:96	arg1	proteoglycans					98:110	dermatan sulphate proteoglycans I and II	80:119	dermatan sulphate proteoglycans I and II	80:119	The properties of dermatan sulphate proteoglycans I and II.
2590169	1	14	theme	sulphate	89:96	arg1	II					118:119	II	118:119	II	118:119	The properties of dermatan sulphate proteoglycans I and II.
2590169	1	14	theme	sulphate	89:96	arg1	I					112:112	I	112:112	I	112:112	The properties of dermatan sulphate proteoglycans I and II.
2590169	0	15	theme	Dermatan	0:7	arg1	proteoglycans					18:30	Dermatan sulphate proteoglycans	0:30	Dermatan sulphate proteoglycans of human articular cartilage	0:59	Dermatan sulphate proteoglycans of human articular cartilage.
2590169	5	16	theme	average	592:598	arg1	values					603:608	average Mr values	592:608	average Mr values of 200,000 and 98,000 for DS-PGI and DS-PGII	592:653	The two proteoglycans could not be resolved by agarose/polyacrylamide-gel electrophoresis, but could be resolved by SDS/polyacrylamide-gel electrophoresis, which indicated average Mr values of 200,000 and 98,000 for DS-PGI and DS-PGII respectively.
2590169	1	17	theme	proteoglycans	98:110	arg1	properties					66:75	The properties	62:75	The properties of dermatan sulphate proteoglycans I and II	62:119	The properties of dermatan sulphate proteoglycans I and II.
2590169	6	18	theme	ABC	702:704	arg1	lyase					706:710	chondroitin ABC lyase	690:710	chondroitin ABC lyase	690:710	After digestion with chondroitin ABC lyase the Mr values of the core proteins were 44,000 for DS-PGI and 43,000 and 47,000 for DS-PGII, with the smaller core protein being predominant in DS-PGII.
2590169	6	19	from	DS-PGII	856:862	arg1	predominant					841:851	predominant	841:851	predominant	841:851	After digestion with chondroitin ABC lyase the Mr values of the core proteins were 44,000 for DS-PGI and 43,000 and 47,000 for DS-PGII, with the smaller core protein being predominant in DS-PGII.
2590169	6	19	from	DS-PGII	856:862	arg1	protein					827:833	the smaller core protein	810:833	the smaller core protein	810:833	After digestion with chondroitin ABC lyase the Mr values of the core proteins were 44,000 for DS-PGI and 43,000 and 47,000 for DS-PGII, with the smaller core protein being predominant in DS-PGII.
2590169	7	20	theme	acid	910:913	arg1	residues					915:922	the N-terminal 20 amino acid residues	886:922	the N-terminal 20 amino acid residues	886:922	Sequence analysis of the N-terminal 20 amino acid residues reveals the presence of a single site for the potential substitution of dermatan sulphate at residue 4 of DS-PGII and two such sites at residues 5 and 10 for DS-PGI.
2590169	5	21	theme	Mr	600:601	arg1	values					603:608	average Mr values	592:608	average Mr values of 200,000 and 98,000 for DS-PGI and DS-PGII	592:653	The two proteoglycans could not be resolved by agarose/polyacrylamide-gel electrophoresis, but could be resolved by SDS/polyacrylamide-gel electrophoresis, which indicated average Mr values of 200,000 and 98,000 for DS-PGI and DS-PGII respectively.
2590169	7	22	theme	potential	970:978	arg1	substitution					980:991	the potential substitution	966:991	the potential substitution of dermatan sulphate at residue 4 of DS-PGII	966:1036	Sequence analysis of the N-terminal 20 amino acid residues reveals the presence of a single site for the potential substitution of dermatan sulphate at residue 4 of DS-PGII and two such sites at residues 5 and 10 for DS-PGI.
2590169	6	23	theme	chondroitin	690:700	arg1	lyase					706:710	chondroitin ABC lyase	690:710	chondroitin ABC lyase	690:710	After digestion with chondroitin ABC lyase the Mr values of the core proteins were 44,000 for DS-PGI and 43,000 and 47,000 for DS-PGII, with the smaller core protein being predominant in DS-PGII.
2590169	4	24	located	present	390:396	arg2	present					390:396	present	390:396	present	390:396	Both dermatan sulphate proteoglycan I (DS-PGI) and dermatan sulphate proteoglycan II (DS-PGII) were identified and the former was present in greater abundance.
2590169	4	24	located	present	390:396	arg1	abundance					409:417	greater abundance	401:417	greater abundance	401:417	Both dermatan sulphate proteoglycan I (DS-PGI) and dermatan sulphate proteoglycan II (DS-PGII) were identified and the former was present in greater abundance.
2590169	4	24	located	present	390:396	arg2	former					379:384	former	379:384	former	379:384	Both dermatan sulphate proteoglycan I (DS-PGI) and dermatan sulphate proteoglycan II (DS-PGII) were identified and the former was present in greater abundance.
2590169	6	25	theme	core	733:736	arg1	proteins					738:745	the core proteins	729:745	the core proteins	729:745	After digestion with chondroitin ABC lyase the Mr values of the core proteins were 44,000 for DS-PGI and 43,000 and 47,000 for DS-PGII, with the smaller core protein being predominant in DS-PGII.
2590169	7	26	from	residues	1060:1067	arg1	site					957:960	a single site	948:960	a single site for the potential substitution of dermatan sulphate at residue 4 of DS-PGII	948:1036	Sequence analysis of the N-terminal 20 amino acid residues reveals the presence of a single site for the potential substitution of dermatan sulphate at residue 4 of DS-PGII and two such sites at residues 5 and 10 for DS-PGI.
2590169	7	26	from	residues	1060:1067	arg1	sites					1051:1055	two such sites	1042:1055	two such sites at residues 5 and 10 for DS-PGI	1042:1087	Sequence analysis of the N-terminal 20 amino acid residues reveals the presence of a single site for the potential substitution of dermatan sulphate at residue 4 of DS-PGII and two such sites at residues 5 and 10 for DS-PGI.
2590169	7	26	from	residues	1060:1067	arg1	presence					936:943	the presence	932:943	the presence of a single site for the potential substitution of dermatan sulphate at residue 4 of DS-PGII and two such sites at residues 5 and 10 for DS-PGI	932:1087	Sequence analysis of the N-terminal 20 amino acid residues reveals the presence of a single site for the potential substitution of dermatan sulphate at residue 4 of DS-PGII and two such sites at residues 5 and 10 for DS-PGI.
2590169	7	27	theme	site	957:960	arg1	presence					936:943	the presence	932:943	the presence of a single site for the potential substitution of dermatan sulphate at residue 4 of DS-PGII and two such sites at residues 5 and 10 for DS-PGI	932:1087	Sequence analysis of the N-terminal 20 amino acid residues reveals the presence of a single site for the potential substitution of dermatan sulphate at residue 4 of DS-PGII and two such sites at residues 5 and 10 for DS-PGI.
2590169	6	28	attach	predominant	841:851	arg2	predominant					841:851	predominant	841:851	predominant	841:851	After digestion with chondroitin ABC lyase the Mr values of the core proteins were 44,000 for DS-PGI and 43,000 and 47,000 for DS-PGII, with the smaller core protein being predominant in DS-PGII.
2590169	6	28	attach	predominant	841:851	arg2	protein					827:833	the smaller core protein	810:833	the smaller core protein	810:833	After digestion with chondroitin ABC lyase the Mr values of the core proteins were 44,000 for DS-PGI and 43,000 and 47,000 for DS-PGII, with the smaller core protein being predominant in DS-PGII.
2590169	6	28	attach	predominant	841:851	arg1	DS-PGII					856:862	DS-PGII	856:862	DS-PGII	856:862	After digestion with chondroitin ABC lyase the Mr values of the core proteins were 44,000 for DS-PGI and 43,000 and 47,000 for DS-PGII, with the smaller core protein being predominant in DS-PGII.
2590169	4	29	theme	dermatan	265:272	arg1	proteoglycan					283:294	dermatan sulphate proteoglycan I	265:296	dermatan sulphate proteoglycan I (DS-PGI)	265:305	Both dermatan sulphate proteoglycan I (DS-PGI) and dermatan sulphate proteoglycan II (DS-PGII) were identified and the former was present in greater abundance.
2590169	4	29	theme	dermatan	265:272	arg1	DS-PGI					299:304	DS-PGI	299:304	DS-PGI	299:304	Both dermatan sulphate proteoglycan I (DS-PGI) and dermatan sulphate proteoglycan II (DS-PGII) were identified and the former was present in greater abundance.
2590169	0	30	theme	articular	41:49	arg1	cartilage					51:59	human articular cartilage	35:59	human articular cartilage	35:59	Dermatan sulphate proteoglycans of human articular cartilage.
2590169	5	31	theme	agarose/polyacrylamide-gel	467:492	arg1	electrophoresis					494:508	agarose/polyacrylamide-gel electrophoresis	467:508	agarose/polyacrylamide-gel electrophoresis	467:508	The two proteoglycans could not be resolved by agarose/polyacrylamide-gel electrophoresis, but could be resolved by SDS/polyacrylamide-gel electrophoresis, which indicated average Mr values of 200,000 and 98,000 for DS-PGI and DS-PGII respectively.
2590169	7	32	theme	DS-PGII	1030:1036	arg1	substitution					980:991	the potential substitution	966:991	the potential substitution of dermatan sulphate at residue 4 of DS-PGII	966:1036	Sequence analysis of the N-terminal 20 amino acid residues reveals the presence of a single site for the potential substitution of dermatan sulphate at residue 4 of DS-PGII and two such sites at residues 5 and 10 for DS-PGI.
2590169	2	33	theme	articular	188:196	arg1	cartilage					198:206	juvenile human articular cartilage	173:206	juvenile human articular cartilage	173:206	Dermatan sulphate proteoglycans were purified from juvenile human articular cartilage, with a yield of about 2 mg/g wet wt.
2590169	2	34	theme	mg/g	233:236	arg1	wt					242:243	about 2 mg/g wet wt	225:243	about 2 mg/g wet wt	225:243	Dermatan sulphate proteoglycans were purified from juvenile human articular cartilage, with a yield of about 2 mg/g wet wt.
2590169	0	35	theme	human	35:39	arg1	cartilage					51:59	human articular cartilage	35:59	human articular cartilage	35:59	Dermatan sulphate proteoglycans of human articular cartilage.
2590169	2	36	theme	human	182:186	arg1	cartilage					198:206	juvenile human articular cartilage	173:206	juvenile human articular cartilage	173:206	Dermatan sulphate proteoglycans were purified from juvenile human articular cartilage, with a yield of about 2 mg/g wet wt.
2590169	7	37	theme	dermatan	996:1003	arg1	sulphate					1005:1012	dermatan sulphate	996:1012	dermatan sulphate	996:1012	Sequence analysis of the N-terminal 20 amino acid residues reveals the presence of a single site for the potential substitution of dermatan sulphate at residue 4 of DS-PGII and two such sites at residues 5 and 10 for DS-PGI.
2590169	7	38	from	10	1075:1076	arg1	site					957:960	a single site	948:960	a single site for the potential substitution of dermatan sulphate at residue 4 of DS-PGII	948:1036	Sequence analysis of the N-terminal 20 amino acid residues reveals the presence of a single site for the potential substitution of dermatan sulphate at residue 4 of DS-PGII and two such sites at residues 5 and 10 for DS-PGI.
2590169	7	38	from	10	1075:1076	arg1	sites					1051:1055	two such sites	1042:1055	two such sites at residues 5 and 10 for DS-PGI	1042:1087	Sequence analysis of the N-terminal 20 amino acid residues reveals the presence of a single site for the potential substitution of dermatan sulphate at residue 4 of DS-PGII and two such sites at residues 5 and 10 for DS-PGI.
2590169	7	38	from	10	1075:1076	arg1	presence					936:943	the presence	932:943	the presence of a single site for the potential substitution of dermatan sulphate at residue 4 of DS-PGII and two such sites at residues 5 and 10 for DS-PGI	932:1087	Sequence analysis of the N-terminal 20 amino acid residues reveals the presence of a single site for the potential substitution of dermatan sulphate at residue 4 of DS-PGII and two such sites at residues 5 and 10 for DS-PGI.
2590169	4	39	from	abundance	409:417	arg1	present					390:396	present	390:396	present	390:396	Both dermatan sulphate proteoglycan I (DS-PGI) and dermatan sulphate proteoglycan II (DS-PGII) were identified and the former was present in greater abundance.
2590169	4	39	from	abundance	409:417	arg1	former					379:384	former	379:384	former	379:384	Both dermatan sulphate proteoglycan I (DS-PGI) and dermatan sulphate proteoglycan II (DS-PGII) were identified and the former was present in greater abundance.
2590169	2	40	theme	juvenile	173:180	arg1	cartilage					198:206	juvenile human articular cartilage	173:206	juvenile human articular cartilage	173:206	Dermatan sulphate proteoglycans were purified from juvenile human articular cartilage, with a yield of about 2 mg/g wet wt.
2590169	4	41	theme	sulphate	320:327	arg1	proteoglycan					329:340	dermatan sulphate proteoglycan II	311:343	dermatan sulphate proteoglycan II (DS-PGII)	311:353	Both dermatan sulphate proteoglycan I (DS-PGI) and dermatan sulphate proteoglycan II (DS-PGII) were identified and the former was present in greater abundance.
2590169	4	41	theme	sulphate	320:327	arg1	DS-PGII					346:352	DS-PGII	346:352	DS-PGII	346:352	Both dermatan sulphate proteoglycan I (DS-PGI) and dermatan sulphate proteoglycan II (DS-PGII) were identified and the former was present in greater abundance.
2590169	0	42	theme	cartilage	51:59	arg1	proteoglycans					18:30	Dermatan sulphate proteoglycans	0:30	Dermatan sulphate proteoglycans of human articular cartilage	0:59	Dermatan sulphate proteoglycans of human articular cartilage.
2590169	6	43	with	digestion	675:683	arg1	lyase					706:710	chondroitin ABC lyase	690:710	chondroitin ABC lyase	690:710	After digestion with chondroitin ABC lyase the Mr values of the core proteins were 44,000 for DS-PGI and 43,000 and 47,000 for DS-PGII, with the smaller core protein being predominant in DS-PGII.
2590169	7	44	theme	residues	915:922	arg1	analysis					874:881	Sequence analysis	865:881	Sequence analysis of the N-terminal 20 amino acid residues	865:922	Sequence analysis of the N-terminal 20 amino acid residues reveals the presence of a single site for the potential substitution of dermatan sulphate at residue 4 of DS-PGII and two such sites at residues 5 and 10 for DS-PGI.
2590169	6	45	theme	core	822:825	arg1	predominant					841:851	predominant	841:851	predominant	841:851	After digestion with chondroitin ABC lyase the Mr values of the core proteins were 44,000 for DS-PGI and 43,000 and 47,000 for DS-PGII, with the smaller core protein being predominant in DS-PGII.
2590169	6	45	theme	core	822:825	arg1	protein					827:833	the smaller core protein	810:833	the smaller core protein	810:833	After digestion with chondroitin ABC lyase the Mr values of the core proteins were 44,000 for DS-PGI and 43,000 and 47,000 for DS-PGII, with the smaller core protein being predominant in DS-PGII.
2590169	7	46	theme	amino	904:908	arg1	residues					915:922	the N-terminal 20 amino acid residues	886:922	the N-terminal 20 amino acid residues	886:922	Sequence analysis of the N-terminal 20 amino acid residues reveals the presence of a single site for the potential substitution of dermatan sulphate at residue 4 of DS-PGII and two such sites at residues 5 and 10 for DS-PGI.
2590169	4	47	from	present	390:396	arg1	abundance					409:417	greater abundance	401:417	greater abundance	401:417	Both dermatan sulphate proteoglycan I (DS-PGI) and dermatan sulphate proteoglycan II (DS-PGII) were identified and the former was present in greater abundance.
2590169	6	48	theme	smaller	814:820	arg1	predominant					841:851	predominant	841:851	predominant	841:851	After digestion with chondroitin ABC lyase the Mr values of the core proteins were 44,000 for DS-PGI and 43,000 and 47,000 for DS-PGII, with the smaller core protein being predominant in DS-PGII.
2590169	6	48	theme	smaller	814:820	arg1	protein					827:833	the smaller core protein	810:833	the smaller core protein	810:833	After digestion with chondroitin ABC lyase the Mr values of the core proteins were 44,000 for DS-PGI and 43,000 and 47,000 for DS-PGII, with the smaller core protein being predominant in DS-PGII.
2590169	6	49	theme	proteins	738:745	arg1	44,000					752:757	44,000	752:757	44,000	752:757	After digestion with chondroitin ABC lyase the Mr values of the core proteins were 44,000 for DS-PGI and 43,000 and 47,000 for DS-PGII, with the smaller core protein being predominant in DS-PGII.
2590169	6	49	theme	proteins	738:745	arg1	values					719:724	the Mr values	712:724	the Mr values of the core proteins	712:745	After digestion with chondroitin ABC lyase the Mr values of the core proteins were 44,000 for DS-PGI and 43,000 and 47,000 for DS-PGII, with the smaller core protein being predominant in DS-PGII.
2590169	7	50	from	residue	1017:1023	arg1	substitution					980:991	the potential substitution	966:991	the potential substitution of dermatan sulphate at residue 4 of DS-PGII	966:1036	Sequence analysis of the N-terminal 20 amino acid residues reveals the presence of a single site for the potential substitution of dermatan sulphate at residue 4 of DS-PGII and two such sites at residues 5 and 10 for DS-PGI.
2590169	4	51	theme	greater	401:407	arg1	abundance					409:417	greater abundance	401:417	greater abundance	401:417	Both dermatan sulphate proteoglycan I (DS-PGI) and dermatan sulphate proteoglycan II (DS-PGII) were identified and the former was present in greater abundance.
2590169	2	52	theme	wt	242:243	arg1	yield					216:220	a yield	214:220	a yield of about 2 mg/g wet wt	214:243	Dermatan sulphate proteoglycans were purified from juvenile human articular cartilage, with a yield of about 2 mg/g wet wt.
2590169	4	53	attach	present	390:396	arg1	abundance					409:417	greater abundance	401:417	greater abundance	401:417	Both dermatan sulphate proteoglycan I (DS-PGI) and dermatan sulphate proteoglycan II (DS-PGII) were identified and the former was present in greater abundance.
2590169	4	53	attach	present	390:396	arg2	present					390:396	present	390:396	present	390:396	Both dermatan sulphate proteoglycan I (DS-PGI) and dermatan sulphate proteoglycan II (DS-PGII) were identified and the former was present in greater abundance.
2590169	4	53	attach	present	390:396	arg2	former					379:384	former	379:384	former	379:384	Both dermatan sulphate proteoglycan I (DS-PGI) and dermatan sulphate proteoglycan II (DS-PGII) were identified and the former was present in greater abundance.
2590169	7	54	from	presence	936:943	arg1	residues					1060:1067	residues 5 and 10	1060:1076	residues	1060:1067	Sequence analysis of the N-terminal 20 amino acid residues reveals the presence of a single site for the potential substitution of dermatan sulphate at residue 4 of DS-PGII and two such sites at residues 5 and 10 for DS-PGI.
2590169	7	54	from	presence	936:943	arg1	10					1075:1076	10	1075:1076	10	1075:1076	Sequence analysis of the N-terminal 20 amino acid residues reveals the presence of a single site for the potential substitution of dermatan sulphate at residue 4 of DS-PGII and two such sites at residues 5 and 10 for DS-PGI.
2590169	7	55	theme	N-terminal	890:899	arg1	residues					915:922	the N-terminal 20 amino acid residues	886:922	the N-terminal 20 amino acid residues	886:922	Sequence analysis of the N-terminal 20 amino acid residues reveals the presence of a single site for the potential substitution of dermatan sulphate at residue 4 of DS-PGII and two such sites at residues 5 and 10 for DS-PGI.
2590169	2	56	theme	sulphate	131:138	arg1	proteoglycans					140:152	Dermatan sulphate proteoglycans	122:152	Dermatan sulphate proteoglycans	122:152	Dermatan sulphate proteoglycans were purified from juvenile human articular cartilage, with a yield of about 2 mg/g wet wt.
2590169	2	57	theme	wet	238:240	arg1	wt					242:243	about 2 mg/g wet wt	225:243	about 2 mg/g wet wt	225:243	Dermatan sulphate proteoglycans were purified from juvenile human articular cartilage, with a yield of about 2 mg/g wet wt.
2590169	4	58	theme	dermatan	311:318	arg1	proteoglycan					329:340	dermatan sulphate proteoglycan II	311:343	dermatan sulphate proteoglycan II (DS-PGII)	311:353	Both dermatan sulphate proteoglycan I (DS-PGI) and dermatan sulphate proteoglycan II (DS-PGII) were identified and the former was present in greater abundance.
2590169	4	58	theme	dermatan	311:318	arg1	DS-PGII					346:352	DS-PGII	346:352	DS-PGII	346:352	Both dermatan sulphate proteoglycan I (DS-PGI) and dermatan sulphate proteoglycan II (DS-PGII) were identified and the former was present in greater abundance.
2590169	6	59	from	predominant	841:851	arg1	DS-PGII					856:862	DS-PGII	856:862	DS-PGII	856:862	After digestion with chondroitin ABC lyase the Mr values of the core proteins were 44,000 for DS-PGI and 43,000 and 47,000 for DS-PGII, with the smaller core protein being predominant in DS-PGII.
9245713	0	0	theme	palmitoylated	82:94	arg1	glycoprotein					104:115	a novel palmitoylated surface glycoprotein	74:115	a novel palmitoylated surface glycoprotein of human gastrointestinal epithelium	74:152	Characterization of posttranslational modifications of human A33 antigen, a novel palmitoylated surface glycoprotein of human gastrointestinal epithelium.
9245713	0	0	theme	palmitoylated	82:94	arg1	antigen					65:71	human A33 antigen	55:71	human A33 antigen	55:71	Characterization of posttranslational modifications of human A33 antigen, a novel palmitoylated surface glycoprotein of human gastrointestinal epithelium.
9245713	6	1	theme	A33	1236:1238	arg1	antigen					1240:1246	cell surface A33 antigen	1223:1246	cell surface A33 antigen	1223:1246	The S-palmitoylation may be involved in regulating the internalization process initiated by binding of mAb A33 to cell surface A33 antigen.
9245713	3	2	theme	A33	479:481	arg1	antigen					483:489	the human A33 antigen	469:489	the human A33 antigen	469:489	The cDNA for the human A33 antigen has recently been cloned, and sequence comparison indicated that the A33 antigen is a novel human cell surface molecule of the immunoglobulin superfamily.
9245713	1	3	theme	gastrointestinal	254:269	arg1	epithelium					271:280	normal human gastrointestinal epithelium	241:280	normal human gastrointestinal epithelium	241:280	Monoclonal antibody (mAb) A33 recognizes a differentiation antigen (A33) expressed in normal human gastrointestinal epithelium and in 95% of human colon cancers.
9245713	0	4	theme	novel	76:80	arg1	glycoprotein					104:115	a novel palmitoylated surface glycoprotein	74:115	a novel palmitoylated surface glycoprotein of human gastrointestinal epithelium	74:152	Characterization of posttranslational modifications of human A33 antigen, a novel palmitoylated surface glycoprotein of human gastrointestinal epithelium.
9245713	0	4	theme	novel	76:80	arg1	antigen					65:71	human A33 antigen	55:71	human A33 antigen	55:71	Characterization of posttranslational modifications of human A33 antigen, a novel palmitoylated surface glycoprotein of human gastrointestinal epithelium.
9245713	6	5	theme	surface	1228:1234	arg1	antigen					1240:1246	cell surface A33 antigen	1223:1246	cell surface A33 antigen	1223:1246	The S-palmitoylation may be involved in regulating the internalization process initiated by binding of mAb A33 to cell surface A33 antigen.
9245713	6	6	theme	cell	1223:1226	arg1	antigen					1240:1246	cell surface A33 antigen	1223:1246	cell surface A33 antigen	1223:1246	The S-palmitoylation may be involved in regulating the internalization process initiated by binding of mAb A33 to cell surface A33 antigen.
9245713	4	7	theme	A33	738:740	arg1	antigen					742:748	the A33 antigen	734:748	the A33 antigen	734:748	Because mAb A33 recognizes a conformational epitope, only a partial characterization of the A33 antigen has been carried out to date.
9245713	0	8	theme	surface	96:102	arg1	glycoprotein					104:115	a novel palmitoylated surface glycoprotein	74:115	a novel palmitoylated surface glycoprotein of human gastrointestinal epithelium	74:152	Characterization of posttranslational modifications of human A33 antigen, a novel palmitoylated surface glycoprotein of human gastrointestinal epithelium.
9245713	0	8	theme	surface	96:102	arg1	antigen					65:71	human A33 antigen	55:71	human A33 antigen	55:71	Characterization of posttranslational modifications of human A33 antigen, a novel palmitoylated surface glycoprotein of human gastrointestinal epithelium.
9245713	2	9	theme	mAb	324:326	arg1	A33					328:330	Murine mAb A33	317:330	Murine mAb A33	317:330	Murine mAb A33 shows specific targeting of colon cancer in humans and a humanized A33 antibody is currently being evaluated in the clinic.
9245713	0	10	theme	human	120:124	arg1	epithelium					143:152	human gastrointestinal epithelium	120:152	human gastrointestinal epithelium	120:152	Characterization of posttranslational modifications of human A33 antigen, a novel palmitoylated surface glycoprotein of human gastrointestinal epithelium.
9245713	6	11	theme	A33	1216:1218	arg1	binding					1201:1207	binding	1201:1207	binding of mAb A33 to cell surface A33 antigen	1201:1246	The S-palmitoylation may be involved in regulating the internalization process initiated by binding of mAb A33 to cell surface A33 antigen.
9245713	4	12	theme	partial	706:712	arg1	characterization					714:729	only a partial characterization	699:729	only a partial characterization of the A33 antigen	699:748	Because mAb A33 recognizes a conformational epitope, only a partial characterization of the A33 antigen has been carried out to date.
9245713	6	13	theme	mAb	1212:1214	arg1	A33					1216:1218	mAb A33	1212:1218	mAb A33	1212:1218	The S-palmitoylation may be involved in regulating the internalization process initiated by binding of mAb A33 to cell surface A33 antigen.
9245713	4	14	theme	antigen	742:748	arg1	characterization					714:729	only a partial characterization	699:729	only a partial characterization of the A33 antigen	699:748	Because mAb A33 recognizes a conformational epitope, only a partial characterization of the A33 antigen has been carried out to date.
9245713	5	15	theme	A33	812:814	arg1	N-glycosylated					831:844	N-glycosylated	831:844	N-glycosylated	831:844	In this report we show that the A33 antigen is (I) N-glycosylated, containing approximately 8 K of N-linked carbohydrate and there is no evidence for O-glycosylation, sialylation or glycophosphatidylinositol, and (ii) S-acylated in vitro, incorporating [3H] palmitic acid linked through a hydroxylamine-sensitive thioester bond.
9245713	5	15	theme	A33	812:814	arg1	antigen					816:822	the A33 antigen	808:822	the A33 antigen	808:822	In this report we show that the A33 antigen is (I) N-glycosylated, containing approximately 8 K of N-linked carbohydrate and there is no evidence for O-glycosylation, sialylation or glycophosphatidylinositol, and (ii) S-acylated in vitro, incorporating [3H] palmitic acid linked through a hydroxylamine-sensitive thioester bond.
9245713	5	16	theme	palmitic	1038:1045	arg1	acid					1047:1050	[3H] palmitic acid	1033:1050	[3H] palmitic acid linked through a hydroxylamine-sensitive thioester bond	1033:1106	In this report we show that the A33 antigen is (I) N-glycosylated, containing approximately 8 K of N-linked carbohydrate and there is no evidence for O-glycosylation, sialylation or glycophosphatidylinositol, and (ii) S-acylated in vitro, incorporating [3H] palmitic acid linked through a hydroxylamine-sensitive thioester bond.
9245713	2	17	from	targeting	347:355	arg1	humans					376:381	humans	376:381	humans	376:381	Murine mAb A33 shows specific targeting of colon cancer in humans and a humanized A33 antibody is currently being evaluated in the clinic.
9245713	2	18	theme	Murine	317:322	arg1	A33					328:330	Murine mAb A33	317:330	Murine mAb A33	317:330	Murine mAb A33 shows specific targeting of colon cancer in humans and a humanized A33 antibody is currently being evaluated in the clinic.
9245713	0	19	gly	glycoprotein	104:115	arg1	glycoprotein					104:115	a novel palmitoylated surface glycoprotein	74:115	a novel palmitoylated surface glycoprotein of human gastrointestinal epithelium	74:152	Characterization of posttranslational modifications of human A33 antigen, a novel palmitoylated surface glycoprotein of human gastrointestinal epithelium.
9245713	0	19	gly	glycoprotein	104:115	arg1	antigen					65:71	human A33 antigen	55:71	human A33 antigen	55:71	Characterization of posttranslational modifications of human A33 antigen, a novel palmitoylated surface glycoprotein of human gastrointestinal epithelium.
9245713	1	20	theme	differentiation	198:212	arg1	A33					223:225	A33	223:225	A33	223:225	Monoclonal antibody (mAb) A33 recognizes a differentiation antigen (A33) expressed in normal human gastrointestinal epithelium and in 95% of human colon cancers.
9245713	1	20	theme	differentiation	198:212	arg1	antigen					214:220	a differentiation antigen	196:220	a differentiation antigen (A33) expressed in normal human gastrointestinal epithelium and in 95% of human colon cancers	196:314	Monoclonal antibody (mAb) A33 recognizes a differentiation antigen (A33) expressed in normal human gastrointestinal epithelium and in 95% of human colon cancers.
9245713	0	21	theme	modifications	38:50	arg1	Characterization					0:15	Characterization	0:15	Characterization of posttranslational modifications of human A33 antigen, a novel palmitoylated surface glycoprotein of human gastrointestinal epithelium.	0:153	Characterization of posttranslational modifications of human A33 antigen, a novel palmitoylated surface glycoprotein of human gastrointestinal epithelium.
9245713	0	22	theme	epithelium	143:152	arg1	glycoprotein					104:115	a novel palmitoylated surface glycoprotein	74:115	a novel palmitoylated surface glycoprotein of human gastrointestinal epithelium	74:152	Characterization of posttranslational modifications of human A33 antigen, a novel palmitoylated surface glycoprotein of human gastrointestinal epithelium.
9245713	0	22	theme	epithelium	143:152	arg1	antigen					65:71	human A33 antigen	55:71	human A33 antigen	55:71	Characterization of posttranslational modifications of human A33 antigen, a novel palmitoylated surface glycoprotein of human gastrointestinal epithelium.
9245713	4	23	theme	conformational	675:688	arg1	epitope					690:696	a conformational epitope	673:696	a conformational epitope	673:696	Because mAb A33 recognizes a conformational epitope, only a partial characterization of the A33 antigen has been carried out to date.
9245713	3	24	theme	sequence	521:528	arg1	comparison					530:539	sequence comparison	521:539	sequence comparison	521:539	The cDNA for the human A33 antigen has recently been cloned, and sequence comparison indicated that the A33 antigen is a novel human cell surface molecule of the immunoglobulin superfamily.
9245713	0	25	theme	posttranslational	20:36	arg1	modifications					38:50	posttranslational modifications	20:50	posttranslational modifications of human A33 antigen, a novel palmitoylated surface glycoprotein of human gastrointestinal epithelium	20:152	Characterization of posttranslational modifications of human A33 antigen, a novel palmitoylated surface glycoprotein of human gastrointestinal epithelium.
9245713	0	26	theme	gastrointestinal	126:141	arg1	epithelium					143:152	human gastrointestinal epithelium	120:152	human gastrointestinal epithelium	120:152	Characterization of posttranslational modifications of human A33 antigen, a novel palmitoylated surface glycoprotein of human gastrointestinal epithelium.
9245713	5	27	theme	carbohydrate	888:899	arg1	K					874:874	approximately 8 K	858:874	approximately 8 K of N-linked carbohydrate	858:899	In this report we show that the A33 antigen is (I) N-glycosylated, containing approximately 8 K of N-linked carbohydrate and there is no evidence for O-glycosylation, sialylation or glycophosphatidylinositol, and (ii) S-acylated in vitro, incorporating [3H] palmitic acid linked through a hydroxylamine-sensitive thioester bond.
9245713	2	28	theme	cancer	366:371	arg1	targeting					347:355	specific targeting	338:355	specific targeting of colon cancer in humans	338:381	Murine mAb A33 shows specific targeting of colon cancer in humans and a humanized A33 antibody is currently being evaluated in the clinic.
9245713	0	29	theme	human	55:59	arg1	glycoprotein					104:115	a novel palmitoylated surface glycoprotein	74:115	a novel palmitoylated surface glycoprotein of human gastrointestinal epithelium	74:152	Characterization of posttranslational modifications of human A33 antigen, a novel palmitoylated surface glycoprotein of human gastrointestinal epithelium.
9245713	0	29	theme	human	55:59	arg1	antigen					65:71	human A33 antigen	55:71	human A33 antigen	55:71	Characterization of posttranslational modifications of human A33 antigen, a novel palmitoylated surface glycoprotein of human gastrointestinal epithelium.
9245713	1	30	theme	human	296:300	arg1	cancers					308:314	human colon cancers	296:314	human colon cancers	296:314	Monoclonal antibody (mAb) A33 recognizes a differentiation antigen (A33) expressed in normal human gastrointestinal epithelium and in 95% of human colon cancers.
9245713	2	31	theme	A33	399:401	arg1	antibody					403:410	a humanized A33 antibody	387:410	a humanized A33 antibody	387:410	Murine mAb A33 shows specific targeting of colon cancer in humans and a humanized A33 antibody is currently being evaluated in the clinic.
9245713	1	32	theme	colon	302:306	arg1	cancers					308:314	human colon cancers	296:314	human colon cancers	296:314	Monoclonal antibody (mAb) A33 recognizes a differentiation antigen (A33) expressed in normal human gastrointestinal epithelium and in 95% of human colon cancers.
9245713	3	33	theme	surface	594:600	arg1	antigen					564:570	the A33 antigen	556:570	the A33 antigen	556:570	The cDNA for the human A33 antigen has recently been cloned, and sequence comparison indicated that the A33 antigen is a novel human cell surface molecule of the immunoglobulin superfamily.
9245713	3	33	theme	surface	594:600	arg1	molecule					602:609	a novel human cell surface molecule	575:609	a novel human cell surface molecule of the immunoglobulin superfamily	575:643	The cDNA for the human A33 antigen has recently been cloned, and sequence comparison indicated that the A33 antigen is a novel human cell surface molecule of the immunoglobulin superfamily.
9245713	5	34	dep	S-acylated	998:1007	arg1	ii					994:995	ii	994:995	ii	994:995	In this report we show that the A33 antigen is (I) N-glycosylated, containing approximately 8 K of N-linked carbohydrate and there is no evidence for O-glycosylation, sialylation or glycophosphatidylinositol, and (ii) S-acylated in vitro, incorporating [3H] palmitic acid linked through a hydroxylamine-sensitive thioester bond.
9245713	2	35	theme	humanized	389:397	arg1	antibody					403:410	a humanized A33 antibody	387:410	a humanized A33 antibody	387:410	Murine mAb A33 shows specific targeting of colon cancer in humans and a humanized A33 antibody is currently being evaluated in the clinic.
9245713	0	36	theme	antigen	65:71	arg1	modifications					38:50	posttranslational modifications	20:50	posttranslational modifications of human A33 antigen, a novel palmitoylated surface glycoprotein of human gastrointestinal epithelium	20:152	Characterization of posttranslational modifications of human A33 antigen, a novel palmitoylated surface glycoprotein of human gastrointestinal epithelium.
9245713	1	37	theme	cancers	308:314	arg1	cancers					308:314	human colon cancers	296:314	human colon cancers	296:314	Monoclonal antibody (mAb) A33 recognizes a differentiation antigen (A33) expressed in normal human gastrointestinal epithelium and in 95% of human colon cancers.
9245713	1	37	theme	cancers	308:314	arg1	%					291:291	95%	289:291	95% of human colon cancers	289:314	Monoclonal antibody (mAb) A33 recognizes a differentiation antigen (A33) expressed in normal human gastrointestinal epithelium and in 95% of human colon cancers.
9245713	2	38	theme	specific	338:345	arg1	targeting					347:355	specific targeting	338:355	specific targeting of colon cancer in humans	338:381	Murine mAb A33 shows specific targeting of colon cancer in humans and a humanized A33 antibody is currently being evaluated in the clinic.
9245713	0	39	theme	A33	61:63	arg1	glycoprotein					104:115	a novel palmitoylated surface glycoprotein	74:115	a novel palmitoylated surface glycoprotein of human gastrointestinal epithelium	74:152	Characterization of posttranslational modifications of human A33 antigen, a novel palmitoylated surface glycoprotein of human gastrointestinal epithelium.
9245713	0	39	theme	A33	61:63	arg1	antigen					65:71	human A33 antigen	55:71	human A33 antigen	55:71	Characterization of posttranslational modifications of human A33 antigen, a novel palmitoylated surface glycoprotein of human gastrointestinal epithelium.
9245713	3	40	theme	A33	560:562	arg1	antigen					564:570	the A33 antigen	556:570	the A33 antigen	556:570	The cDNA for the human A33 antigen has recently been cloned, and sequence comparison indicated that the A33 antigen is a novel human cell surface molecule of the immunoglobulin superfamily.
9245713	3	40	theme	A33	560:562	arg1	molecule					602:609	a novel human cell surface molecule	575:609	a novel human cell surface molecule of the immunoglobulin superfamily	575:643	The cDNA for the human A33 antigen has recently been cloned, and sequence comparison indicated that the A33 antigen is a novel human cell surface molecule of the immunoglobulin superfamily.
9245713	5	41	theme	hydroxylamine-sensitive	1069:1091	arg1	bond					1103:1106	a hydroxylamine-sensitive thioester bond	1067:1106	a hydroxylamine-sensitive thioester bond	1067:1106	In this report we show that the A33 antigen is (I) N-glycosylated, containing approximately 8 K of N-linked carbohydrate and there is no evidence for O-glycosylation, sialylation or glycophosphatidylinositol, and (ii) S-acylated in vitro, incorporating [3H] palmitic acid linked through a hydroxylamine-sensitive thioester bond.
9245713	3	42	theme	human	473:477	arg1	antigen					483:489	the human A33 antigen	469:489	the human A33 antigen	469:489	The cDNA for the human A33 antigen has recently been cloned, and sequence comparison indicated that the A33 antigen is a novel human cell surface molecule of the immunoglobulin superfamily.
9245713	6	43	theme	internalization	1164:1178	arg1	process					1180:1186	the internalization process	1160:1186	the internalization process initiated by binding of mAb A33 to cell surface A33 antigen	1160:1246	The S-palmitoylation may be involved in regulating the internalization process initiated by binding of mAb A33 to cell surface A33 antigen.
9245713	5	44	gly	N-glycosylated	831:844	arg1	N-glycosylated					831:844	N-glycosylated	831:844	N-glycosylated	831:844	In this report we show that the A33 antigen is (I) N-glycosylated, containing approximately 8 K of N-linked carbohydrate and there is no evidence for O-glycosylation, sialylation or glycophosphatidylinositol, and (ii) S-acylated in vitro, incorporating [3H] palmitic acid linked through a hydroxylamine-sensitive thioester bond.
9245713	5	44	gly	N-glycosylated	831:844	arg1	antigen					816:822	the A33 antigen	808:822	the A33 antigen	808:822	In this report we show that the A33 antigen is (I) N-glycosylated, containing approximately 8 K of N-linked carbohydrate and there is no evidence for O-glycosylation, sialylation or glycophosphatidylinositol, and (ii) S-acylated in vitro, incorporating [3H] palmitic acid linked through a hydroxylamine-sensitive thioester bond.
9245713	3	45	theme	human	583:587	arg1	antigen					564:570	the A33 antigen	556:570	the A33 antigen	556:570	The cDNA for the human A33 antigen has recently been cloned, and sequence comparison indicated that the A33 antigen is a novel human cell surface molecule of the immunoglobulin superfamily.
9245713	3	45	theme	human	583:587	arg1	molecule					602:609	a novel human cell surface molecule	575:609	a novel human cell surface molecule of the immunoglobulin superfamily	575:643	The cDNA for the human A33 antigen has recently been cloned, and sequence comparison indicated that the A33 antigen is a novel human cell surface molecule of the immunoglobulin superfamily.
9245713	4	46	theme	mAb	654:656	arg1	A33					658:660	mAb A33	654:660	mAb A33	654:660	Because mAb A33 recognizes a conformational epitope, only a partial characterization of the A33 antigen has been carried out to date.
9245713	5	47	theme	N-linked	879:886	arg1	carbohydrate					888:899	N-linked carbohydrate	879:899	N-linked carbohydrate	879:899	In this report we show that the A33 antigen is (I) N-glycosylated, containing approximately 8 K of N-linked carbohydrate and there is no evidence for O-glycosylation, sialylation or glycophosphatidylinositol, and (ii) S-acylated in vitro, incorporating [3H] palmitic acid linked through a hydroxylamine-sensitive thioester bond.
9245713	3	48	theme	immunoglobulin	618:631	arg1	superfamily					633:643	the immunoglobulin superfamily	614:643	the immunoglobulin superfamily	614:643	The cDNA for the human A33 antigen has recently been cloned, and sequence comparison indicated that the A33 antigen is a novel human cell surface molecule of the immunoglobulin superfamily.
9245713	3	49	theme	cell	589:592	arg1	antigen					564:570	the A33 antigen	556:570	the A33 antigen	556:570	The cDNA for the human A33 antigen has recently been cloned, and sequence comparison indicated that the A33 antigen is a novel human cell surface molecule of the immunoglobulin superfamily.
9245713	3	49	theme	cell	589:592	arg1	molecule					602:609	a novel human cell surface molecule	575:609	a novel human cell surface molecule of the immunoglobulin superfamily	575:643	The cDNA for the human A33 antigen has recently been cloned, and sequence comparison indicated that the A33 antigen is a novel human cell surface molecule of the immunoglobulin superfamily.
9245713	1	50	theme	Monoclonal	155:164	arg1	mAb					176:178	mAb	176:178	mAb	176:178	Monoclonal antibody (mAb) A33 recognizes a differentiation antigen (A33) expressed in normal human gastrointestinal epithelium and in 95% of human colon cancers.
9245713	1	50	theme	Monoclonal	155:164	arg1	antibody					166:173	Monoclonal antibody	155:173	Monoclonal antibody (mAb) A33	155:183	Monoclonal antibody (mAb) A33 recognizes a differentiation antigen (A33) expressed in normal human gastrointestinal epithelium and in 95% of human colon cancers.
9245713	5	51	link	N-linked	879:886	arg1	carbohydrate					888:899	N-linked carbohydrate	879:899	N-linked carbohydrate	879:899	In this report we show that the A33 antigen is (I) N-glycosylated, containing approximately 8 K of N-linked carbohydrate and there is no evidence for O-glycosylation, sialylation or glycophosphatidylinositol, and (ii) S-acylated in vitro, incorporating [3H] palmitic acid linked through a hydroxylamine-sensitive thioester bond.
9245713	3	52	theme	superfamily	633:643	arg1	antigen					564:570	the A33 antigen	556:570	the A33 antigen	556:570	The cDNA for the human A33 antigen has recently been cloned, and sequence comparison indicated that the A33 antigen is a novel human cell surface molecule of the immunoglobulin superfamily.
9245713	3	52	theme	superfamily	633:643	arg1	molecule					602:609	a novel human cell surface molecule	575:609	a novel human cell surface molecule of the immunoglobulin superfamily	575:643	The cDNA for the human A33 antigen has recently been cloned, and sequence comparison indicated that the A33 antigen is a novel human cell surface molecule of the immunoglobulin superfamily.
9245713	1	53	theme	antibody	166:173	arg1	A33					181:183	Monoclonal antibody (mAb) A33	155:183	Monoclonal antibody (mAb) A33	155:183	Monoclonal antibody (mAb) A33 recognizes a differentiation antigen (A33) expressed in normal human gastrointestinal epithelium and in 95% of human colon cancers.
9245713	1	54	theme	normal	241:246	arg1	epithelium					271:280	normal human gastrointestinal epithelium	241:280	normal human gastrointestinal epithelium	241:280	Monoclonal antibody (mAb) A33 recognizes a differentiation antigen (A33) expressed in normal human gastrointestinal epithelium and in 95% of human colon cancers.
9245713	5	55	theme	thioester	1093:1101	arg1	bond					1103:1106	a hydroxylamine-sensitive thioester bond	1067:1106	a hydroxylamine-sensitive thioester bond	1067:1106	In this report we show that the A33 antigen is (I) N-glycosylated, containing approximately 8 K of N-linked carbohydrate and there is no evidence for O-glycosylation, sialylation or glycophosphatidylinositol, and (ii) S-acylated in vitro, incorporating [3H] palmitic acid linked through a hydroxylamine-sensitive thioester bond.
9245713	3	56	theme	novel	577:581	arg1	antigen					564:570	the A33 antigen	556:570	the A33 antigen	556:570	The cDNA for the human A33 antigen has recently been cloned, and sequence comparison indicated that the A33 antigen is a novel human cell surface molecule of the immunoglobulin superfamily.
9245713	3	56	theme	novel	577:581	arg1	molecule					602:609	a novel human cell surface molecule	575:609	a novel human cell surface molecule of the immunoglobulin superfamily	575:643	The cDNA for the human A33 antigen has recently been cloned, and sequence comparison indicated that the A33 antigen is a novel human cell surface molecule of the immunoglobulin superfamily.
9245713	2	57	theme	colon	360:364	arg1	cancer					366:371	colon cancer	360:371	colon cancer	360:371	Murine mAb A33 shows specific targeting of colon cancer in humans and a humanized A33 antibody is currently being evaluated in the clinic.
9245713	1	58	theme	human	248:252	arg1	epithelium					271:280	normal human gastrointestinal epithelium	241:280	normal human gastrointestinal epithelium	241:280	Monoclonal antibody (mAb) A33 recognizes a differentiation antigen (A33) expressed in normal human gastrointestinal epithelium and in 95% of human colon cancers.
26280335	5	0	from	side	727:730	arg1	PS1					693:695	PS1	693:695	PS1	693:695	The active site of PS1 is accessible from the convex side of the TM horseshoe, suggesting considerable conformational changes in nicastrin extracellular domain after substrate recruitment.
26280335	5	0	from	side	727:730	arg1	site					685:688	The active site	674:688	The active site of PS1	674:695	The active site of PS1 is accessible from the convex side of the TM horseshoe, suggesting considerable conformational changes in nicastrin extracellular domain after substrate recruitment.
26280335	5	0	from	side	727:730	arg1	accessible					700:709	accessible	700:709	accessible	700:709	The active site of PS1 is accessible from the convex side of the TM horseshoe, suggesting considerable conformational changes in nicastrin extracellular domain after substrate recruitment.
26280335	1	1	theme	most	142:145	arg1	mutations					147:155	most mutations	142:155	most mutations derived from Alzheimer's disease mapping to the catalytic subunit presenilin 1 (PS1)	142:240	Dysfunction of the intramembrane protease γ-secretase is thought to cause Alzheimer's disease, with most mutations derived from Alzheimer's disease mapping to the catalytic subunit presenilin 1 (PS1).
26280335	6	2	theme	protein	873:879	arg1	scaffold					899:906	a scaffold	897:906	a scaffold	897:906	Component protein APH-1 serves as a scaffold, anchoring the lone transmembrane helix from nicastrin and supporting the flexible conformation of PS1.
26280335	6	2	theme	protein	873:879	arg1	APH-1					881:885	Component protein APH-1	863:885	Component protein APH-1	863:885	Component protein APH-1 serves as a scaffold, anchoring the lone transmembrane helix from nicastrin and supporting the flexible conformation of PS1.
26280335	6	3	theme	Component	863:871	arg1	scaffold					899:906	a scaffold	897:906	a scaffold	897:906	Component protein APH-1 serves as a scaffold, anchoring the lone transmembrane helix from nicastrin and supporting the flexible conformation of PS1.
26280335	6	3	theme	Component	863:871	arg1	APH-1					881:885	Component protein APH-1	863:885	Component protein APH-1	863:885	Component protein APH-1 serves as a scaffold, anchoring the lone transmembrane helix from nicastrin and supporting the flexible conformation of PS1.
26280335	5	4	theme	substrate	840:848	arg1	recruitment					850:860	substrate recruitment	840:860	substrate recruitment	840:860	The active site of PS1 is accessible from the convex side of the TM horseshoe, suggesting considerable conformational changes in nicastrin extracellular domain after substrate recruitment.
26280335	4	5	theme	active	626:631	arg1	site					633:636	a plastic active site	616:636	a plastic active site	616:636	TM2 and, to a lesser extent, TM6 exhibit considerable flexibility, yielding a plastic active site and adaptable surrounding elements.
26280335	8	6	theme	mechanistic	1123:1133	arg1	understanding					1135:1147	mechanistic understanding	1123:1147	mechanistic understanding of γ-secretase function	1123:1171	Our structure serves as a molecular basis for mechanistic understanding of γ-secretase function.
26280335	2	7	theme	human	281:285	arg1	γ-secretase					287:297	human γ-secretase	281:297	human γ-secretase	281:297	Here we report an atomic structure of human γ-secretase at 3.4 Å resolution, determined by single-particle cryo-electron microscopy.
26280335	3	8	from	centre	479:484	arg1	located					464:470	located	464:470	located	464:470	Mutations derived from Alzheimer's disease affect residues at two hotspots in PS1, each located at the centre of a distinct four transmembrane segment (TM) bundle.
26280335	3	9	theme	transmembrane	505:517	arg1	TM					528:529	TM	528:529	TM	528:529	Mutations derived from Alzheimer's disease affect residues at two hotspots in PS1, each located at the centre of a distinct four transmembrane segment (TM) bundle.
26280335	3	9	theme	transmembrane	505:517	arg1	segment					519:525	four transmembrane segment	500:525	a distinct four transmembrane segment (TM) bundle	489:537	Mutations derived from Alzheimer's disease affect residues at two hotspots in PS1, each located at the centre of a distinct four transmembrane segment (TM) bundle.
26280335	4	10	theme	surrounding	652:662	arg1	elements					664:671	adaptable surrounding elements	642:671	adaptable surrounding elements	642:671	TM2 and, to a lesser extent, TM6 exhibit considerable flexibility, yielding a plastic active site and adaptable surrounding elements.
26280335	5	11	theme	active	678:683	arg1	PS1					693:695	PS1	693:695	PS1	693:695	The active site of PS1 is accessible from the convex side of the TM horseshoe, suggesting considerable conformational changes in nicastrin extracellular domain after substrate recruitment.
26280335	5	11	theme	active	678:683	arg1	site					685:688	The active site	674:688	The active site of PS1	674:695	The active site of PS1 is accessible from the convex side of the TM horseshoe, suggesting considerable conformational changes in nicastrin extracellular domain after substrate recruitment.
26280335	5	11	theme	active	678:683	arg1	accessible					700:709	accessible	700:709	accessible	700:709	The active site of PS1 is accessible from the convex side of the TM horseshoe, suggesting considerable conformational changes in nicastrin extracellular domain after substrate recruitment.
26280335	4	12	theme	adaptable	642:650	arg1	elements					664:671	adaptable surrounding elements	642:671	adaptable surrounding elements	642:671	TM2 and, to a lesser extent, TM6 exhibit considerable flexibility, yielding a plastic active site and adaptable surrounding elements.
26280335	1	13	theme	intramembrane	61:73	arg1	γ-secretase					84:94	the intramembrane protease γ-secretase	57:94	the intramembrane protease γ-secretase	57:94	Dysfunction of the intramembrane protease γ-secretase is thought to cause Alzheimer's disease, with most mutations derived from Alzheimer's disease mapping to the catalytic subunit presenilin 1 (PS1).
26280335	5	14	theme	nicastrin	803:811	arg1	domain					827:832	nicastrin extracellular domain	803:832	nicastrin extracellular domain	803:832	The active site of PS1 is accessible from the convex side of the TM horseshoe, suggesting considerable conformational changes in nicastrin extracellular domain after substrate recruitment.
26280335	6	15	theme	transmembrane	928:940	arg1	helix					942:946	the lone transmembrane helix	919:946	the lone transmembrane helix from nicastrin	919:961	Component protein APH-1 serves as a scaffold, anchoring the lone transmembrane helix from nicastrin and supporting the flexible conformation of PS1.
26280335	1	16	with	disease	128:134	arg1	mutations					147:155	most mutations	142:155	most mutations derived from Alzheimer's disease mapping to the catalytic subunit presenilin 1 (PS1)	142:240	Dysfunction of the intramembrane protease γ-secretase is thought to cause Alzheimer's disease, with most mutations derived from Alzheimer's disease mapping to the catalytic subunit presenilin 1 (PS1).
26280335	1	17	theme	protease	75:82	arg1	γ-secretase					84:94	the intramembrane protease γ-secretase	57:94	the intramembrane protease γ-secretase	57:94	Dysfunction of the intramembrane protease γ-secretase is thought to cause Alzheimer's disease, with most mutations derived from Alzheimer's disease mapping to the catalytic subunit presenilin 1 (PS1).
26280335	4	18	theme	considerable	581:592	arg1	flexibility					594:604	considerable flexibility	581:604	considerable flexibility	581:604	TM2 and, to a lesser extent, TM6 exhibit considerable flexibility, yielding a plastic active site and adaptable surrounding elements.
26280335	0	19	theme	atomic	3:8	arg1	structure					10:18	An atomic structure	0:18	An atomic structure of human γ-secretase	0:39	An atomic structure of human γ-secretase.
26280335	8	20	theme	molecular	1103:1111	arg1	basis					1113:1117	a molecular basis	1101:1117	a molecular basis for mechanistic understanding of γ-secretase function	1101:1171	Our structure serves as a molecular basis for mechanistic understanding of γ-secretase function.
26280335	8	20	theme	molecular	1103:1111	arg1	structure					1081:1089	Our structure	1077:1089	Our structure	1077:1089	Our structure serves as a molecular basis for mechanistic understanding of γ-secretase function.
26280335	6	21	from	nicastrin	953:961	arg1	helix					942:946	the lone transmembrane helix	919:946	the lone transmembrane helix from nicastrin	919:961	Component protein APH-1 serves as a scaffold, anchoring the lone transmembrane helix from nicastrin and supporting the flexible conformation of PS1.
26280335	2	22	from	resolution	308:317	arg1	structure					268:276	an atomic structure	258:276	an atomic structure	258:276	Here we report an atomic structure of human γ-secretase at 3.4 Å resolution, determined by single-particle cryo-electron microscopy.
26280335	1	23	theme	γ-secretase	84:94	arg1	Dysfunction					42:52	Dysfunction	42:52	Dysfunction of the intramembrane protease γ-secretase	42:94	Dysfunction of the intramembrane protease γ-secretase is thought to cause Alzheimer's disease, with most mutations derived from Alzheimer's disease mapping to the catalytic subunit presenilin 1 (PS1).
26280335	2	24	theme	cryo-electron	350:362	arg1	microscopy					364:373	single-particle cryo-electron microscopy	334:373	single-particle cryo-electron microscopy	334:373	Here we report an atomic structure of human γ-secretase at 3.4 Å resolution, determined by single-particle cryo-electron microscopy.
26280335	8	25	theme	γ-secretase	1152:1162	arg1	function					1164:1171	γ-secretase function	1152:1171	γ-secretase function	1152:1171	Our structure serves as a molecular basis for mechanistic understanding of γ-secretase function.
26280335	6	26	theme	lone	923:926	arg1	helix					942:946	the lone transmembrane helix	919:946	the lone transmembrane helix from nicastrin	919:961	Component protein APH-1 serves as a scaffold, anchoring the lone transmembrane helix from nicastrin and supporting the flexible conformation of PS1.
26280335	2	27	theme	single-particle	334:348	arg1	microscopy					364:373	single-particle cryo-electron microscopy	334:373	single-particle cryo-electron microscopy	334:373	Here we report an atomic structure of human γ-secretase at 3.4 Å resolution, determined by single-particle cryo-electron microscopy.
26280335	5	28	theme	TM	739:740	arg1	horseshoe					742:750	the TM horseshoe	735:750	the TM horseshoe	735:750	The active site of PS1 is accessible from the convex side of the TM horseshoe, suggesting considerable conformational changes in nicastrin extracellular domain after substrate recruitment.
26280335	3	29	theme	segment	519:525	arg1	bundle					532:537	a distinct four transmembrane segment (TM) bundle	489:537	a distinct four transmembrane segment (TM) bundle	489:537	Mutations derived from Alzheimer's disease affect residues at two hotspots in PS1, each located at the centre of a distinct four transmembrane segment (TM) bundle.
26280335	5	30	theme	horseshoe	742:750	arg1	side					727:730	the convex side	716:730	the convex side of the TM horseshoe	716:750	The active site of PS1 is accessible from the convex side of the TM horseshoe, suggesting considerable conformational changes in nicastrin extracellular domain after substrate recruitment.
26280335	2	31	theme	atomic	261:266	arg1	structure					268:276	an atomic structure	258:276	an atomic structure	258:276	Here we report an atomic structure of human γ-secretase at 3.4 Å resolution, determined by single-particle cryo-electron microscopy.
26280335	6	32	theme	PS1	1007:1009	arg1	conformation					991:1002	the flexible conformation	978:1002	the flexible conformation of PS1	978:1009	Component protein APH-1 serves as a scaffold, anchoring the lone transmembrane helix from nicastrin and supporting the flexible conformation of PS1.
26280335	0	33	theme	γ-secretase	29:39	arg1	structure					10:18	An atomic structure	0:18	An atomic structure of human γ-secretase	0:39	An atomic structure of human γ-secretase.
26280335	7	34	theme	Ordered	1012:1018	arg1	phospholipids					1020:1032	Ordered phospholipids	1012:1032	Ordered phospholipids	1012:1032	Ordered phospholipids stabilize the complex inside the membrane.
26280335	5	35	theme	extracellular	813:825	arg1	domain					827:832	nicastrin extracellular domain	803:832	nicastrin extracellular domain	803:832	The active site of PS1 is accessible from the convex side of the TM horseshoe, suggesting considerable conformational changes in nicastrin extracellular domain after substrate recruitment.
26280335	5	36	theme	considerable	764:775	arg1	changes					792:798	considerable conformational changes	764:798	considerable conformational changes in nicastrin extracellular domain after substrate recruitment	764:860	The active site of PS1 is accessible from the convex side of the TM horseshoe, suggesting considerable conformational changes in nicastrin extracellular domain after substrate recruitment.
26280335	0	37	theme	human	23:27	arg1	γ-secretase					29:39	human γ-secretase	23:39	human γ-secretase	23:39	An atomic structure of human γ-secretase.
26280335	5	38	theme	conformational	777:790	arg1	changes					792:798	considerable conformational changes	764:798	considerable conformational changes in nicastrin extracellular domain after substrate recruitment	764:860	The active site of PS1 is accessible from the convex side of the TM horseshoe, suggesting considerable conformational changes in nicastrin extracellular domain after substrate recruitment.
26280335	5	39	theme	convex	720:725	arg1	side					727:730	the convex side	716:730	the convex side of the TM horseshoe	716:750	The active site of PS1 is accessible from the convex side of the TM horseshoe, suggesting considerable conformational changes in nicastrin extracellular domain after substrate recruitment.
26280335	3	40	theme	bundle	532:537	arg1	centre					479:484	the centre	475:484	the centre of a distinct four transmembrane segment (TM) bundle	475:537	Mutations derived from Alzheimer's disease affect residues at two hotspots in PS1, each located at the centre of a distinct four transmembrane segment (TM) bundle.
26280335	2	41	theme	Å	306:306	arg1	resolution					308:317	3.4 Å resolution	302:317	3.4 Å resolution	302:317	Here we report an atomic structure of human γ-secretase at 3.4 Å resolution, determined by single-particle cryo-electron microscopy.
26280335	3	42	from	hotspots	442:449	arg1	PS1					454:456	PS1	454:456	PS1	454:456	Mutations derived from Alzheimer's disease affect residues at two hotspots in PS1, each located at the centre of a distinct four transmembrane segment (TM) bundle.
26280335	3	42	from	hotspots	442:449	arg1	residues					426:433	residues	426:433	residues at two hotspots in PS1, each located at the centre of a distinct four transmembrane segment (TM) bundle	426:537	Mutations derived from Alzheimer's disease affect residues at two hotspots in PS1, each located at the centre of a distinct four transmembrane segment (TM) bundle.
26280335	8	43	theme	function	1164:1171	arg1	understanding					1135:1147	mechanistic understanding	1123:1147	mechanistic understanding of γ-secretase function	1123:1171	Our structure serves as a molecular basis for mechanistic understanding of γ-secretase function.
26280335	1	44	theme	catalytic	205:213	arg1	presenilin					223:232	the catalytic subunit presenilin 1	201:234	the catalytic subunit presenilin 1 (PS1)	201:240	Dysfunction of the intramembrane protease γ-secretase is thought to cause Alzheimer's disease, with most mutations derived from Alzheimer's disease mapping to the catalytic subunit presenilin 1 (PS1).
26280335	1	44	theme	catalytic	205:213	arg1	PS1					237:239	PS1	237:239	PS1	237:239	Dysfunction of the intramembrane protease γ-secretase is thought to cause Alzheimer's disease, with most mutations derived from Alzheimer's disease mapping to the catalytic subunit presenilin 1 (PS1).
26280335	3	45	theme	distinct	491:498	arg1	bundle					532:537	a distinct four transmembrane segment (TM) bundle	489:537	a distinct four transmembrane segment (TM) bundle	489:537	Mutations derived from Alzheimer's disease affect residues at two hotspots in PS1, each located at the centre of a distinct four transmembrane segment (TM) bundle.
26280335	2	46	theme	γ-secretase	287:297	arg1	structure					268:276	an atomic structure	258:276	an atomic structure	258:276	Here we report an atomic structure of human γ-secretase at 3.4 Å resolution, determined by single-particle cryo-electron microscopy.
26280335	1	47	theme	subunit	215:221	arg1	presenilin					223:232	the catalytic subunit presenilin 1	201:234	the catalytic subunit presenilin 1 (PS1)	201:240	Dysfunction of the intramembrane protease γ-secretase is thought to cause Alzheimer's disease, with most mutations derived from Alzheimer's disease mapping to the catalytic subunit presenilin 1 (PS1).
26280335	1	47	theme	subunit	215:221	arg1	PS1					237:239	PS1	237:239	PS1	237:239	Dysfunction of the intramembrane protease γ-secretase is thought to cause Alzheimer's disease, with most mutations derived from Alzheimer's disease mapping to the catalytic subunit presenilin 1 (PS1).
26280335	4	48	theme	plastic	618:624	arg1	site					633:636	a plastic active site	616:636	a plastic active site	616:636	TM2 and, to a lesser extent, TM6 exhibit considerable flexibility, yielding a plastic active site and adaptable surrounding elements.
26280335	4	49	theme	lesser	554:559	arg1	extent					561:566	a lesser extent	552:566	a lesser extent	552:566	TM2 and, to a lesser extent, TM6 exhibit considerable flexibility, yielding a plastic active site and adaptable surrounding elements.
26280335	5	50	theme	PS1	693:695	arg1	PS1					693:695	PS1	693:695	PS1	693:695	The active site of PS1 is accessible from the convex side of the TM horseshoe, suggesting considerable conformational changes in nicastrin extracellular domain after substrate recruitment.
26280335	5	50	theme	PS1	693:695	arg1	site					685:688	The active site	674:688	The active site of PS1	674:695	The active site of PS1 is accessible from the convex side of the TM horseshoe, suggesting considerable conformational changes in nicastrin extracellular domain after substrate recruitment.
26280335	5	50	theme	PS1	693:695	arg1	accessible					700:709	accessible	700:709	accessible	700:709	The active site of PS1 is accessible from the convex side of the TM horseshoe, suggesting considerable conformational changes in nicastrin extracellular domain after substrate recruitment.
26280335	5	51	from	changes	792:798	arg1	domain					827:832	nicastrin extracellular domain	803:832	nicastrin extracellular domain	803:832	The active site of PS1 is accessible from the convex side of the TM horseshoe, suggesting considerable conformational changes in nicastrin extracellular domain after substrate recruitment.
26280335	6	52	theme	flexible	982:989	arg1	conformation					991:1002	the flexible conformation	978:1002	the flexible conformation of PS1	978:1009	Component protein APH-1 serves as a scaffold, anchoring the lone transmembrane helix from nicastrin and supporting the flexible conformation of PS1.
30598546	5	0	theme	substrate	766:774	arg1	binding					776:782	substrate binding	766:782	substrate binding	766:782	PS1 undergoes pronounced conformational rearrangement upon substrate binding.
30598546	3	1	with	β-sheet	483:489	arg1	β-strands					518:526	two substrate-induced β-strands	496:526	two substrate-induced β-strands of PS1	496:533	The transmembrane helix of Notch is surrounded by three transmembrane domains of PS1, and the carboxyl-terminal β-strand of the Notch fragment forms a β-sheet with two substrate-induced β-strands of PS1 on the intracellular side.
30598546	2	2	from	resolution	311:320	arg1	fragment					297:304	a Notch fragment	289:304	a Notch fragment at a resolution of 2.7 Å	289:329	Here we report the cryo-electron microscopy structure of human γ-secretase in complex with a Notch fragment at a resolution of 2.7 Å.
30598546	6	3	contain	have	853:856	arg1	features					791:798	These features	785:798	These features	785:798	These features reveal the structural basis of Notch recognition and have implications for the recruitment of the amyloid precursor protein by γ-secretase.
30598546	6	3	contain	have	853:856	arg2	implications					858:869	implications	858:869	implications for the recruitment of the amyloid precursor protein by γ-secretase	858:937	These features reveal the structural basis of Notch recognition and have implications for the recruitment of the amyloid precursor protein by γ-secretase.
30598546	3	4	theme	transmembrane	336:348	arg1	helix					350:354	The transmembrane helix	332:354	The transmembrane helix of Notch	332:363	The transmembrane helix of Notch is surrounded by three transmembrane domains of PS1, and the carboxyl-terminal β-strand of the Notch fragment forms a β-sheet with two substrate-induced β-strands of PS1 on the intracellular side.
30598546	6	5	theme	protein	916:922	arg1	recruitment					879:889	the recruitment	875:889	the recruitment of the amyloid precursor protein by γ-secretase	875:937	These features reveal the structural basis of Notch recognition and have implications for the recruitment of the amyloid precursor protein by γ-secretase.
30598546	3	6	from	β-sheet	483:489	arg1	side					556:559	the intracellular side	538:559	the intracellular side	538:559	The transmembrane helix of Notch is surrounded by three transmembrane domains of PS1, and the carboxyl-terminal β-strand of the Notch fragment forms a β-sheet with two substrate-induced β-strands of PS1 on the intracellular side.
30598546	3	7	theme	intracellular	542:554	arg1	side					556:559	the intracellular side	538:559	the intracellular side	538:559	The transmembrane helix of Notch is surrounded by three transmembrane domains of PS1, and the carboxyl-terminal β-strand of the Notch fragment forms a β-sheet with two substrate-induced β-strands of PS1 on the intracellular side.
30598546	6	8	theme	precursor	906:914	arg1	protein					916:922	the amyloid precursor protein	894:922	the amyloid precursor protein	894:922	These features reveal the structural basis of Notch recognition and have implications for the recruitment of the amyloid precursor protein by γ-secretase.
30598546	1	9	theme	Aberrant	60:67	arg1	cleavage					69:76	Aberrant cleavage	60:76	Aberrant cleavage of Notch by γ-secretase	60:100	Aberrant cleavage of Notch by γ-secretase leads to several types of cancer, but how γ-secretase recognizes its substrate remains unknown.
30598546	6	10	theme	structural	811:820	arg1	basis					822:826	the structural basis	807:826	the structural basis of Notch recognition	807:847	These features reveal the structural basis of Notch recognition and have implications for the recruitment of the amyloid precursor protein by γ-secretase.
30598546	3	11	theme	PS1	531:533	arg1	β-strands					518:526	two substrate-induced β-strands	496:526	two substrate-induced β-strands of PS1	496:533	The transmembrane helix of Notch is surrounded by three transmembrane domains of PS1, and the carboxyl-terminal β-strand of the Notch fragment forms a β-sheet with two substrate-induced β-strands of PS1 on the intracellular side.
30598546	4	12	theme	helix	700:704	arg1	end					669:671	the carboxyl-terminal end	647:671	the carboxyl-terminal end of the Notch transmembrane helix	647:704	Formation of the hybrid β-sheet is essential for substrate cleavage, which occurs at the carboxyl-terminal end of the Notch transmembrane helix.
30598546	5	13	theme	pronounced	721:730	arg1	rearrangement					747:759	pronounced conformational rearrangement	721:759	pronounced conformational rearrangement	721:759	PS1 undergoes pronounced conformational rearrangement upon substrate binding.
30598546	3	14	theme	fragment	466:473	arg1	β-strand					444:451	the carboxyl-terminal β-strand	422:451	the carboxyl-terminal β-strand of the Notch fragment	422:473	The transmembrane helix of Notch is surrounded by three transmembrane domains of PS1, and the carboxyl-terminal β-strand of the Notch fragment forms a β-sheet with two substrate-induced β-strands of PS1 on the intracellular side.
30598546	3	15	theme	substrate-induced	500:516	arg1	β-strands					518:526	two substrate-induced β-strands	496:526	two substrate-induced β-strands of PS1	496:533	The transmembrane helix of Notch is surrounded by three transmembrane domains of PS1, and the carboxyl-terminal β-strand of the Notch fragment forms a β-sheet with two substrate-induced β-strands of PS1 on the intracellular side.
30598546	5	16	theme	conformational	732:745	arg1	rearrangement					747:759	pronounced conformational rearrangement	721:759	pronounced conformational rearrangement	721:759	PS1 undergoes pronounced conformational rearrangement upon substrate binding.
30598546	2	17	theme	γ-secretase	261:271	arg1	structure					242:250	the cryo-electron microscopy structure	213:250	the cryo-electron microscopy structure of human γ-secretase in complex with a Notch fragment at a resolution of 2.7 Å	213:329	Here we report the cryo-electron microscopy structure of human γ-secretase in complex with a Notch fragment at a resolution of 2.7 Å.
30598546	1	18	theme	Notch	81:85	arg1	cleavage					69:76	Aberrant cleavage	60:76	Aberrant cleavage of Notch by γ-secretase	60:100	Aberrant cleavage of Notch by γ-secretase leads to several types of cancer, but how γ-secretase recognizes its substrate remains unknown.
30598546	6	19	theme	amyloid	898:904	arg1	protein					916:922	the amyloid precursor protein	894:922	the amyloid precursor protein	894:922	These features reveal the structural basis of Notch recognition and have implications for the recruitment of the amyloid precursor protein by γ-secretase.
30598546	0	20	theme	Structural	0:9	arg1	basis					11:15	Structural basis	0:15	Structural basis of Notch recognition by human γ-secretase.	0:58	Structural basis of Notch recognition by human γ-secretase.
30598546	2	21	from	structure	242:250	arg1	complex					276:282	complex	276:282	complex with a Notch fragment at a resolution of 2.7 Å	276:329	Here we report the cryo-electron microscopy structure of human γ-secretase in complex with a Notch fragment at a resolution of 2.7 Å.
30598546	3	22	theme	PS1	413:415	arg1	PS1					413:415	PS1	413:415	PS1	413:415	The transmembrane helix of Notch is surrounded by three transmembrane domains of PS1, and the carboxyl-terminal β-strand of the Notch fragment forms a β-sheet with two substrate-induced β-strands of PS1 on the intracellular side.
30598546	3	22	theme	PS1	413:415	arg1	domains					402:408	three transmembrane domains	382:408	three transmembrane domains of PS1	382:415	The transmembrane helix of Notch is surrounded by three transmembrane domains of PS1, and the carboxyl-terminal β-strand of the Notch fragment forms a β-sheet with two substrate-induced β-strands of PS1 on the intracellular side.
30598546	0	23	theme	Notch	20:24	arg1	recognition					26:36	Notch recognition	20:36	Notch recognition	20:36	Structural basis of Notch recognition by human γ-secretase.
30598546	2	24	theme	Notch	291:295	arg1	fragment					297:304	a Notch fragment	289:304	a Notch fragment at a resolution of 2.7 Å	289:329	Here we report the cryo-electron microscopy structure of human γ-secretase in complex with a Notch fragment at a resolution of 2.7 Å.
30598546	4	25	theme	substrate	611:619	arg1	cleavage					621:628	substrate cleavage	611:628	substrate cleavage	611:628	Formation of the hybrid β-sheet is essential for substrate cleavage, which occurs at the carboxyl-terminal end of the Notch transmembrane helix.
30598546	3	26	theme	Notch	359:363	arg1	helix					350:354	The transmembrane helix	332:354	The transmembrane helix of Notch	332:363	The transmembrane helix of Notch is surrounded by three transmembrane domains of PS1, and the carboxyl-terminal β-strand of the Notch fragment forms a β-sheet with two substrate-induced β-strands of PS1 on the intracellular side.
30598546	3	27	theme	transmembrane	388:400	arg1	PS1					413:415	PS1	413:415	PS1	413:415	The transmembrane helix of Notch is surrounded by three transmembrane domains of PS1, and the carboxyl-terminal β-strand of the Notch fragment forms a β-sheet with two substrate-induced β-strands of PS1 on the intracellular side.
30598546	3	27	theme	transmembrane	388:400	arg1	domains					402:408	three transmembrane domains	382:408	three transmembrane domains of PS1	382:415	The transmembrane helix of Notch is surrounded by three transmembrane domains of PS1, and the carboxyl-terminal β-strand of the Notch fragment forms a β-sheet with two substrate-induced β-strands of PS1 on the intracellular side.
30598546	4	28	theme	Notch	680:684	arg1	helix					700:704	the Notch transmembrane helix	676:704	the Notch transmembrane helix	676:704	Formation of the hybrid β-sheet is essential for substrate cleavage, which occurs at the carboxyl-terminal end of the Notch transmembrane helix.
30598546	2	29	theme	cryo-electron	217:229	arg1	microscopy					231:240	cryo-electron microscopy	217:240	the cryo-electron microscopy structure of human γ-secretase in complex with a Notch fragment at a resolution of 2.7 Å	213:329	Here we report the cryo-electron microscopy structure of human γ-secretase in complex with a Notch fragment at a resolution of 2.7 Å.
30598546	0	30	theme	recognition	26:36	arg1	basis					11:15	Structural basis	0:15	Structural basis of Notch recognition by human γ-secretase.	0:58	Structural basis of Notch recognition by human γ-secretase.
30598546	3	31	theme	carboxyl-terminal	426:442	arg1	β-strand					444:451	the carboxyl-terminal β-strand	422:451	the carboxyl-terminal β-strand of the Notch fragment	422:473	The transmembrane helix of Notch is surrounded by three transmembrane domains of PS1, and the carboxyl-terminal β-strand of the Notch fragment forms a β-sheet with two substrate-induced β-strands of PS1 on the intracellular side.
30598546	2	32	theme	2.7 Å	325:329	arg1	resolution					311:320	a resolution	309:320	a resolution of 2.7 Å	309:329	Here we report the cryo-electron microscopy structure of human γ-secretase in complex with a Notch fragment at a resolution of 2.7 Å.
30598546	0	33	theme	human	41:45	arg1	γ-secretase					47:57	human γ-secretase	41:57	human γ-secretase	41:57	Structural basis of Notch recognition by human γ-secretase.
30598546	1	34	theme	several	111:117	arg1	types					119:123	several types	111:123	several types of cancer	111:133	Aberrant cleavage of Notch by γ-secretase leads to several types of cancer, but how γ-secretase recognizes its substrate remains unknown.
30598546	4	35	theme	transmembrane	686:698	arg1	helix					700:704	the Notch transmembrane helix	676:704	the Notch transmembrane helix	676:704	Formation of the hybrid β-sheet is essential for substrate cleavage, which occurs at the carboxyl-terminal end of the Notch transmembrane helix.
30598546	2	36	theme	human	255:259	arg1	γ-secretase					261:271	human γ-secretase	255:271	human γ-secretase	255:271	Here we report the cryo-electron microscopy structure of human γ-secretase in complex with a Notch fragment at a resolution of 2.7 Å.
30598546	4	37	theme	β-sheet	586:592	arg1	Formation					562:570	Formation	562:570	Formation of the hybrid β-sheet	562:592	Formation of the hybrid β-sheet is essential for substrate cleavage, which occurs at the carboxyl-terminal end of the Notch transmembrane helix.
30598546	6	38	theme	recognition	837:847	arg1	basis					822:826	the structural basis	807:826	the structural basis of Notch recognition	807:847	These features reveal the structural basis of Notch recognition and have implications for the recruitment of the amyloid precursor protein by γ-secretase.
30598546	3	39	theme	Notch	460:464	arg1	fragment					466:473	the Notch fragment	456:473	the Notch fragment	456:473	The transmembrane helix of Notch is surrounded by three transmembrane domains of PS1, and the carboxyl-terminal β-strand of the Notch fragment forms a β-sheet with two substrate-induced β-strands of PS1 on the intracellular side.
30598546	4	40	theme	hybrid	579:584	arg1	β-sheet					586:592	the hybrid β-sheet	575:592	the hybrid β-sheet	575:592	Formation of the hybrid β-sheet is essential for substrate cleavage, which occurs at the carboxyl-terminal end of the Notch transmembrane helix.
30598546	6	41	theme	Notch	831:835	arg1	recognition					837:847	Notch recognition	831:847	Notch recognition	831:847	These features reveal the structural basis of Notch recognition and have implications for the recruitment of the amyloid precursor protein by γ-secretase.
30598546	1	42	theme	cancer	128:133	arg1	types					119:123	several types	111:123	several types of cancer	111:133	Aberrant cleavage of Notch by γ-secretase leads to several types of cancer, but how γ-secretase recognizes its substrate remains unknown.
30598546	2	43	theme	microscopy	231:240	arg1	structure					242:250	the cryo-electron microscopy structure	213:250	the cryo-electron microscopy structure of human γ-secretase in complex with a Notch fragment at a resolution of 2.7 Å	213:329	Here we report the cryo-electron microscopy structure of human γ-secretase in complex with a Notch fragment at a resolution of 2.7 Å.
30598546	4	44	theme	carboxyl-terminal	651:667	arg1	end					669:671	the carboxyl-terminal end	647:671	the carboxyl-terminal end of the Notch transmembrane helix	647:704	Formation of the hybrid β-sheet is essential for substrate cleavage, which occurs at the carboxyl-terminal end of the Notch transmembrane helix.
30598546	2	45	with	complex	276:282	arg1	fragment					297:304	a Notch fragment	289:304	a Notch fragment at a resolution of 2.7 Å	289:329	Here we report the cryo-electron microscopy structure of human γ-secretase in complex with a Notch fragment at a resolution of 2.7 Å.
30630874	4	0	from	strands	499:505	arg1	strand					473:478	a β strand	469:478	a β strand from APP and two β strands from PS1	469:514	A hybrid β sheet, which is formed by a β strand from APP and two β strands from PS1, guides γ-secretase to the scissile peptide bond of APP between its TM and β strand.
30630874	2	1	theme	2.6-angstrom	296:307	arg1	resolution					309:318	2.6-angstrom resolution	296:318	2.6-angstrom resolution	296:318	We report an atomic structure of human γ-secretase in complex with a transmembrane (TM) APP fragment at 2.6-angstrom resolution.
30630874	2	2	theme	TM	276:277	arg1	fragment					284:291	a transmembrane (TM) APP fragment	259:291	a transmembrane (TM) APP fragment at 2.6-angstrom resolution	259:318	We report an atomic structure of human γ-secretase in complex with a transmembrane (TM) APP fragment at 2.6-angstrom resolution.
30630874	4	3	theme	β	591:591	arg1	strand					593:598	its TM and β strand	580:598	its TM and β strand	580:598	A hybrid β sheet, which is formed by a β strand from APP and two β strands from PS1, guides γ-secretase to the scissile peptide bond of APP between its TM and β strand.
30630874	4	4	from	APP	485:487	arg1	strand					473:478	a β strand	469:478	a β strand from APP and two β strands from PS1	469:514	A hybrid β sheet, which is formed by a β strand from APP and two β strands from PS1, guides γ-secretase to the scissile peptide bond of APP between its TM and β strand.
30630874	4	5	theme	scissile	543:550	arg1	bond					560:563	the scissile peptide bond	539:563	the scissile peptide bond of APP between its TM and β strand	539:598	A hybrid β sheet, which is formed by a β strand from APP and two β strands from PS1, guides γ-secretase to the scissile peptide bond of APP between its TM and β strand.
30630874	2	6	from	resolution	309:318	arg1	fragment					284:291	a transmembrane (TM) APP fragment	259:291	a transmembrane (TM) APP fragment at 2.6-angstrom resolution	259:318	We report an atomic structure of human γ-secretase in complex with a transmembrane (TM) APP fragment at 2.6-angstrom resolution.
30630874	2	7	theme	γ-secretase	231:241	arg1	structure					212:220	an atomic structure	202:220	an atomic structure of human γ-secretase in complex with a transmembrane (TM) APP fragment at 2.6-angstrom resolution	202:318	We report an atomic structure of human γ-secretase in complex with a transmembrane (TM) APP fragment at 2.6-angstrom resolution.
30630874	3	8	theme	PS1	388:390	arg1	TMs					381:383	five surrounding TMs	364:383	five surrounding TMs of PS1 (the catalytic subunit of γ-secretase)	364:429	The TM helix of APP closely interacts with five surrounding TMs of PS1 (the catalytic subunit of γ-secretase).
30630874	6	9	theme	binding	816:822	arg1	features					794:801	contrasting features	782:801	contrasting features of substrate binding, which may be applied toward the design of substrate-specific inhibitors	782:895	This structure, together with that of γ-secretase bound to Notch, reveal contrasting features of substrate binding, which may be applied toward the design of substrate-specific inhibitors.
30630874	1	10	theme	amyloid	79:85	arg1	APP					106:108	APP	106:108	APP	106:108	Cleavage of amyloid precursor protein (APP) by the intramembrane protease γ-secretase is linked to Alzheimer's disease (AD).
30630874	1	10	theme	amyloid	79:85	arg1	protein					97:103	amyloid precursor protein	79:103	amyloid precursor protein (APP)	79:109	Cleavage of amyloid precursor protein (APP) by the intramembrane protease γ-secretase is linked to Alzheimer's disease (AD).
30630874	3	11	theme	surrounding	369:379	arg1	TMs					381:383	five surrounding TMs	364:383	five surrounding TMs of PS1 (the catalytic subunit of γ-secretase)	364:429	The TM helix of APP closely interacts with five surrounding TMs of PS1 (the catalytic subunit of γ-secretase).
30630874	3	12	theme	APP	337:339	arg1	helix					328:332	The TM helix	321:332	The TM helix of APP	321:339	The TM helix of APP closely interacts with five surrounding TMs of PS1 (the catalytic subunit of γ-secretase).
30630874	1	13	theme	precursor	87:95	arg1	APP					106:108	APP	106:108	APP	106:108	Cleavage of amyloid precursor protein (APP) by the intramembrane protease γ-secretase is linked to Alzheimer's disease (AD).
30630874	1	13	theme	precursor	87:95	arg1	protein					97:103	amyloid precursor protein	79:103	amyloid precursor protein (APP)	79:109	Cleavage of amyloid precursor protein (APP) by the intramembrane protease γ-secretase is linked to Alzheimer's disease (AD).
30630874	2	14	from	structure	212:220	arg1	complex					246:252	complex	246:252	complex with a transmembrane (TM) APP fragment at 2.6-angstrom resolution	246:318	We report an atomic structure of human γ-secretase in complex with a transmembrane (TM) APP fragment at 2.6-angstrom resolution.
30630874	4	15	theme	peptide	552:558	arg1	bond					560:563	the scissile peptide bond	539:563	the scissile peptide bond of APP between its TM and β strand	539:598	A hybrid β sheet, which is formed by a β strand from APP and two β strands from PS1, guides γ-secretase to the scissile peptide bond of APP between its TM and β strand.
30630874	0	16	theme	amyloid	19:25	arg1	protein					37:43	the amyloid precursor protein	15:43	the amyloid precursor protein	15:43	Recognition of the amyloid precursor protein by human γ-secretase.
30630874	2	17	theme	transmembrane	261:273	arg1	fragment					284:291	a transmembrane (TM) APP fragment	259:291	a transmembrane (TM) APP fragment at 2.6-angstrom resolution	259:318	We report an atomic structure of human γ-secretase in complex with a transmembrane (TM) APP fragment at 2.6-angstrom resolution.
30630874	3	18	theme	catalytic	397:405	arg1	subunit					407:413	the catalytic subunit	393:413	the catalytic subunit of γ-secretase	393:428	The TM helix of APP closely interacts with five surrounding TMs of PS1 (the catalytic subunit of γ-secretase).
30630874	4	19	theme	APP	568:570	arg1	bond					560:563	the scissile peptide bond	539:563	the scissile peptide bond of APP between its TM and β strand	539:598	A hybrid β sheet, which is formed by a β strand from APP and two β strands from PS1, guides γ-secretase to the scissile peptide bond of APP between its TM and β strand.
30630874	0	20	theme	protein	37:43	arg1	Recognition					0:10	Recognition	0:10	Recognition of the amyloid precursor protein by human γ-secretase	0:64	Recognition of the amyloid precursor protein by human γ-secretase.
30630874	4	21	theme	β	471:471	arg1	strand					473:478	a β strand	469:478	a β strand from APP and two β strands from PS1	469:514	A hybrid β sheet, which is formed by a β strand from APP and two β strands from PS1, guides γ-secretase to the scissile peptide bond of APP between its TM and β strand.
30630874	1	22	theme	protein	97:103	arg1	Cleavage					67:74	Cleavage	67:74	Cleavage of amyloid precursor protein (APP) by the intramembrane protease γ-secretase	67:151	Cleavage of amyloid precursor protein (APP) by the intramembrane protease γ-secretase is linked to Alzheimer's disease (AD).
30630874	0	23	theme	precursor	27:35	arg1	protein					37:43	the amyloid precursor protein	15:43	the amyloid precursor protein	15:43	Recognition of the amyloid precursor protein by human γ-secretase.
30630874	6	24	theme	substrate	806:814	arg1	binding					816:822	substrate binding	806:822	substrate binding	806:822	This structure, together with that of γ-secretase bound to Notch, reveal contrasting features of substrate binding, which may be applied toward the design of substrate-specific inhibitors.
30630874	3	25	theme	TM	325:326	arg1	helix					328:332	The TM helix	321:332	The TM helix of APP	321:339	The TM helix of APP closely interacts with five surrounding TMs of PS1 (the catalytic subunit of γ-secretase).
30630874	6	26	dep	together	725:732	arg1	with					734:737	with	734:737	with	734:737	This structure, together with that of γ-secretase bound to Notch, reveal contrasting features of substrate binding, which may be applied toward the design of substrate-specific inhibitors.
30630874	0	27	theme	human	48:52	arg1	γ-secretase					54:64	human γ-secretase	48:64	human γ-secretase	48:64	Recognition of the amyloid precursor protein by human γ-secretase.
30630874	3	28	dep	PS1	388:390	arg1	subunit					407:413	the catalytic subunit	393:413	the catalytic subunit of γ-secretase	393:428	The TM helix of APP closely interacts with five surrounding TMs of PS1 (the catalytic subunit of γ-secretase).
30630874	4	29	theme	TM	584:585	arg1	strand					593:598	its TM and β strand	580:598	its TM and β strand	580:598	A hybrid β sheet, which is formed by a β strand from APP and two β strands from PS1, guides γ-secretase to the scissile peptide bond of APP between its TM and β strand.
30630874	6	30	theme	contrasting	782:792	arg1	features					794:801	contrasting features	782:801	contrasting features of substrate binding, which may be applied toward the design of substrate-specific inhibitors	782:895	This structure, together with that of γ-secretase bound to Notch, reveal contrasting features of substrate binding, which may be applied toward the design of substrate-specific inhibitors.
30630874	2	31	theme	human	225:229	arg1	γ-secretase					231:241	human γ-secretase	225:241	human γ-secretase in complex with a transmembrane (TM) APP fragment at 2.6-angstrom resolution	225:318	We report an atomic structure of human γ-secretase in complex with a transmembrane (TM) APP fragment at 2.6-angstrom resolution.
30630874	6	32	theme	substrate-specific	867:884	arg1	inhibitors					886:895	substrate-specific inhibitors	867:895	substrate-specific inhibitors	867:895	This structure, together with that of γ-secretase bound to Notch, reveal contrasting features of substrate binding, which may be applied toward the design of substrate-specific inhibitors.
30630874	2	33	theme	APP	280:282	arg1	fragment					284:291	a transmembrane (TM) APP fragment	259:291	a transmembrane (TM) APP fragment at 2.6-angstrom resolution	259:318	We report an atomic structure of human γ-secretase in complex with a transmembrane (TM) APP fragment at 2.6-angstrom resolution.
30630874	2	34	from	γ-secretase	231:241	arg1	complex					246:252	complex	246:252	complex with a transmembrane (TM) APP fragment at 2.6-angstrom resolution	246:318	We report an atomic structure of human γ-secretase in complex with a transmembrane (TM) APP fragment at 2.6-angstrom resolution.
30630874	6	35	theme	inhibitors	886:895	arg1	design					857:862	the design	853:862	the design of substrate-specific inhibitors	853:895	This structure, together with that of γ-secretase bound to Notch, reveal contrasting features of substrate binding, which may be applied toward the design of substrate-specific inhibitors.
30630874	5	36	from	interface	617:625	arg1	Residues					601:608	Residues	601:608	Residues at the interface between PS1 and APP	601:645	Residues at the interface between PS1 and APP are heavily targeted by recurring mutations from AD patients.
30630874	3	37	theme	γ-secretase	418:428	arg1	subunit					407:413	the catalytic subunit	393:413	the catalytic subunit of γ-secretase	393:428	The TM helix of APP closely interacts with five surrounding TMs of PS1 (the catalytic subunit of γ-secretase).
30630874	4	38	theme	β	497:497	arg1	strands					499:505	two β strands	493:505	two β strands from PS1	493:514	A hybrid β sheet, which is formed by a β strand from APP and two β strands from PS1, guides γ-secretase to the scissile peptide bond of APP between its TM and β strand.
30630874	4	39	from	PS1	512:514	arg1	strands					499:505	two β strands	493:505	two β strands from PS1	493:514	A hybrid β sheet, which is formed by a β strand from APP and two β strands from PS1, guides γ-secretase to the scissile peptide bond of APP between its TM and β strand.
30630874	4	39	from	PS1	512:514	arg1	APP					485:487	APP	485:487	APP	485:487	A hybrid β sheet, which is formed by a β strand from APP and two β strands from PS1, guides γ-secretase to the scissile peptide bond of APP between its TM and β strand.
30630874	5	40	theme	AD	696:697	arg1	patients					699:706	AD patients	696:706	AD patients	696:706	Residues at the interface between PS1 and APP are heavily targeted by recurring mutations from AD patients.
30630874	1	41	theme	intramembrane	118:130	arg1	γ-secretase					141:151	the intramembrane protease γ-secretase	114:151	the intramembrane protease γ-secretase	114:151	Cleavage of amyloid precursor protein (APP) by the intramembrane protease γ-secretase is linked to Alzheimer's disease (AD).
30630874	2	42	from	complex	246:252	arg1	structure					212:220	an atomic structure	202:220	an atomic structure of human γ-secretase in complex with a transmembrane (TM) APP fragment at 2.6-angstrom resolution	202:318	We report an atomic structure of human γ-secretase in complex with a transmembrane (TM) APP fragment at 2.6-angstrom resolution.
30630874	4	43	theme	hybrid	434:439	arg1	sheet					443:447	A hybrid β sheet	432:447	A hybrid β sheet	432:447	A hybrid β sheet, which is formed by a β strand from APP and two β strands from PS1, guides γ-secretase to the scissile peptide bond of APP between its TM and β strand.
30630874	2	44	theme	atomic	205:210	arg1	structure					212:220	an atomic structure	202:220	an atomic structure of human γ-secretase in complex with a transmembrane (TM) APP fragment at 2.6-angstrom resolution	202:318	We report an atomic structure of human γ-secretase in complex with a transmembrane (TM) APP fragment at 2.6-angstrom resolution.
30630874	1	45	theme	protease	132:139	arg1	γ-secretase					141:151	the intramembrane protease γ-secretase	114:151	the intramembrane protease γ-secretase	114:151	Cleavage of amyloid precursor protein (APP) by the intramembrane protease γ-secretase is linked to Alzheimer's disease (AD).
30630874	2	46	with	complex	246:252	arg1	fragment					284:291	a transmembrane (TM) APP fragment	259:291	a transmembrane (TM) APP fragment at 2.6-angstrom resolution	259:318	We report an atomic structure of human γ-secretase in complex with a transmembrane (TM) APP fragment at 2.6-angstrom resolution.
24305054	8	0	theme	heterodimer	1063:1073	arg1	interface					1075:1083	a novel heterodimer interface	1055:1083	a novel heterodimer interface between subunits	1055:1100	Our data reveal a unique activation mechanism for GABA(B) receptor that involves the formation of a novel heterodimer interface between subunits.
24305054	8	1	theme	novel	1057:1061	arg1	interface					1075:1083	a novel heterodimer interface	1055:1083	a novel heterodimer interface between subunits	1055:1100	Our data reveal a unique activation mechanism for GABA(B) receptor that involves the formation of a novel heterodimer interface between subunits.
24305054	0	2	from	mechanism	11:19	arg1	receptor					59:66	human GABA(B) receptor	45:66	human GABA(B) receptor	45:66	Structural mechanism of ligand activation in human GABA(B) receptor.
24305054	4	3	theme	receptor	527:534	arg1	state					514:518	the resting state	502:518	the resting state of the receptor	502:534	The apo and antagonist-bound structures represent the resting state of the receptor; the agonist-bound complex corresponds to the active state.
24305054	3	4	theme	crystal	301:307	arg1	structures					309:318	the crystal structures	297:318	the crystal structures of a heterodimeric complex between the extracellular domains of GBR1 and GBR2 in the apo, agonist-bound and antagonist-bound forms	297:449	Here we present the crystal structures of a heterodimeric complex between the extracellular domains of GBR1 and GBR2 in the apo, agonist-bound and antagonist-bound forms.
24305054	3	5	from	domains	373:379	arg1	forms					445:449	the apo, agonist-bound and antagonist-bound forms	401:449	the apo, agonist-bound and antagonist-bound forms	401:449	Here we present the crystal structures of a heterodimeric complex between the extracellular domains of GBR1 and GBR2 in the apo, agonist-bound and antagonist-bound forms.
24305054	8	6	theme	unique	975:980	arg1	mechanism					993:1001	a unique activation mechanism	973:1001	a unique activation mechanism for GABA(B) receptor that involves the formation of a novel heterodimer interface between subunits	973:1100	Our data reveal a unique activation mechanism for GABA(B) receptor that involves the formation of a novel heterodimer interface between subunits.
24305054	4	7	theme	agonist-bound	541:553	arg1	complex					555:561	the agonist-bound complex	537:561	the agonist-bound complex	537:561	The apo and antagonist-bound structures represent the resting state of the receptor; the agonist-bound complex corresponds to the active state.
24305054	5	8	theme	agonist-induced	670:684	arg1	activation					695:704	agonist-induced receptor activation	670:704	agonist-induced receptor activation	670:704	Both subunits adopt an open conformation at rest, and only GBR1 closes on agonist-induced receptor activation.
24305054	5	9	theme	open	619:622	arg1	conformation					624:635	an open conformation	616:635	an open conformation at rest	616:643	Both subunits adopt an open conformation at rest, and only GBR1 closes on agonist-induced receptor activation.
24305054	6	10	theme	interdomain	756:766	arg1	crevice					768:774	the interdomain crevice	752:774	the interdomain crevice of GBR1	752:782	The agonists and antagonists are anchored in the interdomain crevice of GBR1 by an overlapping set of residues.
24305054	5	11	theme	receptor	686:693	arg1	activation					695:704	agonist-induced receptor activation	670:704	agonist-induced receptor activation	670:704	Both subunits adopt an open conformation at rest, and only GBR1 closes on agonist-induced receptor activation.
24305054	3	12	theme	antagonist-bound	428:443	arg1	forms					445:449	the apo, agonist-bound and antagonist-bound forms	401:449	the apo, agonist-bound and antagonist-bound forms	401:449	Here we present the crystal structures of a heterodimeric complex between the extracellular domains of GBR1 and GBR2 in the apo, agonist-bound and antagonist-bound forms.
24305054	4	13	theme	active	582:587	arg1	state					589:593	the active state	578:593	the active state	578:593	The apo and antagonist-bound structures represent the resting state of the receptor; the agonist-bound complex corresponds to the active state.
24305054	2	14	theme	obligatory	227:236	arg1	heterodimer					238:248	an obligatory heterodimer	224:248	an obligatory heterodimer of the subunits GBR1 and GBR2	224:278	It functions as an obligatory heterodimer of the subunits GBR1 and GBR2.
24305054	2	14	theme	obligatory	227:236	arg1	It					208:209	It	208:209	It	208:209	It functions as an obligatory heterodimer of the subunits GBR1 and GBR2.
24305054	8	15	theme	activation	982:991	arg1	mechanism					993:1001	a unique activation mechanism	973:1001	a unique activation mechanism for GABA(B) receptor that involves the formation of a novel heterodimer interface between subunits	973:1100	Our data reveal a unique activation mechanism for GABA(B) receptor that involves the formation of a novel heterodimer interface between subunits.
24305054	7	16	theme	inactive	879:886	arg1	state					888:892	the inactive state	875:892	the inactive state	875:892	An antagonist confines GBR1 to the open conformation of the inactive state, whereas an agonist induces its domain closure for activation.
24305054	0	17	theme	Structural	0:9	arg1	mechanism					11:19	Structural mechanism	0:19	Structural mechanism of ligand activation in human GABA(B) receptor	0:66	Structural mechanism of ligand activation in human GABA(B) receptor.
24305054	3	18	theme	GBR2	393:396	arg1	GBR2					393:396	GBR2	393:396	GBR2	393:396	Here we present the crystal structures of a heterodimeric complex between the extracellular domains of GBR1 and GBR2 in the apo, agonist-bound and antagonist-bound forms.
24305054	3	18	theme	GBR2	393:396	arg1	GBR1					384:387	GBR1	384:387	GBR1	384:387	Here we present the crystal structures of a heterodimeric complex between the extracellular domains of GBR1 and GBR2 in the apo, agonist-bound and antagonist-bound forms.
24305054	3	18	theme	GBR2	393:396	arg1	domains					373:379	the extracellular domains	355:379	the extracellular domains of GBR1 and GBR2 in the apo, agonist-bound and antagonist-bound forms	355:449	Here we present the crystal structures of a heterodimeric complex between the extracellular domains of GBR1 and GBR2 in the apo, agonist-bound and antagonist-bound forms.
24305054	3	19	theme	heterodimeric	325:337	arg1	complex					339:345	a heterodimeric complex	323:345	a heterodimeric complex between the extracellular domains of GBR1 and GBR2 in the apo, agonist-bound and antagonist-bound forms	323:449	Here we present the crystal structures of a heterodimeric complex between the extracellular domains of GBR1 and GBR2 in the apo, agonist-bound and antagonist-bound forms.
24305054	0	20	from	activation	31:40	arg1	receptor					59:66	human GABA(B) receptor	45:66	human GABA(B) receptor	45:66	Structural mechanism of ligand activation in human GABA(B) receptor.
24305054	8	21	theme	GABA	1007:1010	arg1	receptor					1015:1022	GABA(B) receptor	1007:1022	GABA(B) receptor that involves the formation of a novel heterodimer interface between subunits	1007:1100	Our data reveal a unique activation mechanism for GABA(B) receptor that involves the formation of a novel heterodimer interface between subunits.
24305054	7	22	theme	state	888:892	arg1	conformation					859:870	the open conformation	850:870	the open conformation of the inactive state	850:892	An antagonist confines GBR1 to the open conformation of the inactive state, whereas an agonist induces its domain closure for activation.
24305054	3	23	theme	complex	339:345	arg1	structures					309:318	the crystal structures	297:318	the crystal structures of a heterodimeric complex between the extracellular domains of GBR1 and GBR2 in the apo, agonist-bound and antagonist-bound forms	297:449	Here we present the crystal structures of a heterodimeric complex between the extracellular domains of GBR1 and GBR2 in the apo, agonist-bound and antagonist-bound forms.
24305054	1	24	theme	Human	69:73	arg1	B					110:110	γ-aminobutyric acid class B	84:110	γ-aminobutyric acid class B	84:110	Human GABA(B) (γ-aminobutyric acid class B) receptor is a G-protein-coupled receptor central to inhibitory neurotransmission in the brain.
24305054	1	24	theme	Human	69:73	arg1	B					80:80	B	80:80	B	80:80	Human GABA(B) (γ-aminobutyric acid class B) receptor is a G-protein-coupled receptor central to inhibitory neurotransmission in the brain.
24305054	1	24	theme	Human	69:73	arg1	GABA					75:78	Human GABA	69:78	Human GABA(B) (γ-aminobutyric acid class B) receptor	69:120	Human GABA(B) (γ-aminobutyric acid class B) receptor is a G-protein-coupled receptor central to inhibitory neurotransmission in the brain.
24305054	1	25	theme	G-protein-coupled	127:143	arg1	receptor					113:120	Human GABA(B) (γ-aminobutyric acid class B) receptor	69:120	Human GABA(B) (γ-aminobutyric acid class B) receptor	69:120	Human GABA(B) (γ-aminobutyric acid class B) receptor is a G-protein-coupled receptor central to inhibitory neurotransmission in the brain.
24305054	1	25	theme	G-protein-coupled	127:143	arg1	receptor					145:152	a G-protein-coupled receptor	125:152	a G-protein-coupled receptor central to inhibitory neurotransmission in the brain	125:205	Human GABA(B) (γ-aminobutyric acid class B) receptor is a G-protein-coupled receptor central to inhibitory neurotransmission in the brain.
24305054	0	26	theme	ligand	24:29	arg1	activation					31:40	ligand activation	24:40	ligand activation in human GABA(B) receptor	24:66	Structural mechanism of ligand activation in human GABA(B) receptor.
24305054	4	27	theme	resting	506:512	arg1	state					514:518	the resting state	502:518	the resting state of the receptor	502:534	The apo and antagonist-bound structures represent the resting state of the receptor; the agonist-bound complex corresponds to the active state.
24305054	8	28	theme	B	1012:1012	arg1	receptor					1015:1022	GABA(B) receptor	1007:1022	GABA(B) receptor that involves the formation of a novel heterodimer interface between subunits	1007:1100	Our data reveal a unique activation mechanism for GABA(B) receptor that involves the formation of a novel heterodimer interface between subunits.
24305054	2	29	theme	subunits	257:264	arg1	heterodimer					238:248	an obligatory heterodimer	224:248	an obligatory heterodimer of the subunits GBR1 and GBR2	224:278	It functions as an obligatory heterodimer of the subunits GBR1 and GBR2.
24305054	2	29	theme	subunits	257:264	arg1	It					208:209	It	208:209	It	208:209	It functions as an obligatory heterodimer of the subunits GBR1 and GBR2.
24305054	3	30	theme	apo	405:407	arg1	forms					445:449	the apo, agonist-bound and antagonist-bound forms	401:449	the apo, agonist-bound and antagonist-bound forms	401:449	Here we present the crystal structures of a heterodimeric complex between the extracellular domains of GBR1 and GBR2 in the apo, agonist-bound and antagonist-bound forms.
24305054	5	31	theme	only	650:653	arg1	GBR1					655:658	only GBR1	650:658	only GBR1	650:658	Both subunits adopt an open conformation at rest, and only GBR1 closes on agonist-induced receptor activation.
24305054	0	32	from	receptor	59:66	arg1	mechanism					11:19	Structural mechanism	0:19	Structural mechanism of ligand activation in human GABA(B) receptor	0:66	Structural mechanism of ligand activation in human GABA(B) receptor.
24305054	1	33	theme	central	154:160	arg1	receptor					113:120	Human GABA(B) (γ-aminobutyric acid class B) receptor	69:120	Human GABA(B) (γ-aminobutyric acid class B) receptor	69:120	Human GABA(B) (γ-aminobutyric acid class B) receptor is a G-protein-coupled receptor central to inhibitory neurotransmission in the brain.
24305054	1	33	theme	central	154:160	arg1	receptor					145:152	a G-protein-coupled receptor	125:152	a G-protein-coupled receptor central to inhibitory neurotransmission in the brain	125:205	Human GABA(B) (γ-aminobutyric acid class B) receptor is a G-protein-coupled receptor central to inhibitory neurotransmission in the brain.
24305054	3	34	theme	extracellular	359:371	arg1	GBR2					393:396	GBR2	393:396	GBR2	393:396	Here we present the crystal structures of a heterodimeric complex between the extracellular domains of GBR1 and GBR2 in the apo, agonist-bound and antagonist-bound forms.
24305054	3	34	theme	extracellular	359:371	arg1	GBR1					384:387	GBR1	384:387	GBR1	384:387	Here we present the crystal structures of a heterodimeric complex between the extracellular domains of GBR1 and GBR2 in the apo, agonist-bound and antagonist-bound forms.
24305054	3	34	theme	extracellular	359:371	arg1	domains					373:379	the extracellular domains	355:379	the extracellular domains of GBR1 and GBR2 in the apo, agonist-bound and antagonist-bound forms	355:449	Here we present the crystal structures of a heterodimeric complex between the extracellular domains of GBR1 and GBR2 in the apo, agonist-bound and antagonist-bound forms.
24305054	6	35	theme	residues	809:816	arg1	residues					809:816	residues	809:816	residues	809:816	The agonists and antagonists are anchored in the interdomain crevice of GBR1 by an overlapping set of residues.
24305054	6	35	theme	residues	809:816	arg1	set					802:804	an overlapping set	787:804	an overlapping set of residues	787:816	The agonists and antagonists are anchored in the interdomain crevice of GBR1 by an overlapping set of residues.
24305054	3	36	theme	GBR1	384:387	arg1	GBR2					393:396	GBR2	393:396	GBR2	393:396	Here we present the crystal structures of a heterodimeric complex between the extracellular domains of GBR1 and GBR2 in the apo, agonist-bound and antagonist-bound forms.
24305054	3	36	theme	GBR1	384:387	arg1	GBR1					384:387	GBR1	384:387	GBR1	384:387	Here we present the crystal structures of a heterodimeric complex between the extracellular domains of GBR1 and GBR2 in the apo, agonist-bound and antagonist-bound forms.
24305054	3	36	theme	GBR1	384:387	arg1	domains					373:379	the extracellular domains	355:379	the extracellular domains of GBR1 and GBR2 in the apo, agonist-bound and antagonist-bound forms	355:449	Here we present the crystal structures of a heterodimeric complex between the extracellular domains of GBR1 and GBR2 in the apo, agonist-bound and antagonist-bound forms.
24305054	0	37	theme	activation	31:40	arg1	mechanism					11:19	Structural mechanism	0:19	Structural mechanism of ligand activation in human GABA(B) receptor	0:66	Structural mechanism of ligand activation in human GABA(B) receptor.
24305054	1	38	theme	inhibitory	165:174	arg1	neurotransmission					176:192	inhibitory neurotransmission	165:192	inhibitory neurotransmission in the brain	165:205	Human GABA(B) (γ-aminobutyric acid class B) receptor is a G-protein-coupled receptor central to inhibitory neurotransmission in the brain.
24305054	0	39	theme	GABA	51:54	arg1	receptor					59:66	human GABA(B) receptor	45:66	human GABA(B) receptor	45:66	Structural mechanism of ligand activation in human GABA(B) receptor.
24305054	4	40	theme	antagonist-bound	464:479	arg1	structures					481:490	antagonist-bound structures	464:490	antagonist-bound structures	464:490	The apo and antagonist-bound structures represent the resting state of the receptor; the agonist-bound complex corresponds to the active state.
24305054	2	41	dep	subunits	257:264	arg1	subunits					257:264	the subunits GBR1 and GBR2	253:278	the subunits GBR1 and GBR2	253:278	It functions as an obligatory heterodimer of the subunits GBR1 and GBR2.
24305054	2	41	dep	subunits	257:264	arg1	GBR2					275:278	GBR2	275:278	GBR2	275:278	It functions as an obligatory heterodimer of the subunits GBR1 and GBR2.
24305054	2	41	dep	subunits	257:264	arg1	GBR1					266:269	GBR1	266:269	GBR1	266:269	It functions as an obligatory heterodimer of the subunits GBR1 and GBR2.
24305054	0	42	theme	human	45:49	arg1	receptor					59:66	human GABA(B) receptor	45:66	human GABA(B) receptor	45:66	Structural mechanism of ligand activation in human GABA(B) receptor.
24305054	6	43	theme	overlapping	790:800	arg1	residues					809:816	residues	809:816	residues	809:816	The agonists and antagonists are anchored in the interdomain crevice of GBR1 by an overlapping set of residues.
24305054	6	43	theme	overlapping	790:800	arg1	set					802:804	an overlapping set	787:804	an overlapping set of residues	787:816	The agonists and antagonists are anchored in the interdomain crevice of GBR1 by an overlapping set of residues.
24305054	7	44	theme	open	854:857	arg1	conformation					859:870	the open conformation	850:870	the open conformation of the inactive state	850:892	An antagonist confines GBR1 to the open conformation of the inactive state, whereas an agonist induces its domain closure for activation.
24305054	1	45	from	neurotransmission	176:192	arg1	brain					201:205	the brain	197:205	the brain	197:205	Human GABA(B) (γ-aminobutyric acid class B) receptor is a G-protein-coupled receptor central to inhibitory neurotransmission in the brain.
24305054	3	46	theme	agonist-bound	410:422	arg1	forms					445:449	the apo, agonist-bound and antagonist-bound forms	401:449	the apo, agonist-bound and antagonist-bound forms	401:449	Here we present the crystal structures of a heterodimeric complex between the extracellular domains of GBR1 and GBR2 in the apo, agonist-bound and antagonist-bound forms.
24305054	1	47	theme	GABA	75:78	arg1	receptor					113:120	Human GABA(B) (γ-aminobutyric acid class B) receptor	69:120	Human GABA(B) (γ-aminobutyric acid class B) receptor	69:120	Human GABA(B) (γ-aminobutyric acid class B) receptor is a G-protein-coupled receptor central to inhibitory neurotransmission in the brain.
24305054	1	47	theme	GABA	75:78	arg1	receptor					145:152	a G-protein-coupled receptor	125:152	a G-protein-coupled receptor central to inhibitory neurotransmission in the brain	125:205	Human GABA(B) (γ-aminobutyric acid class B) receptor is a G-protein-coupled receptor central to inhibitory neurotransmission in the brain.
24305054	5	48	from	rest	640:643	arg1	conformation					624:635	an open conformation	616:635	an open conformation at rest	616:643	Both subunits adopt an open conformation at rest, and only GBR1 closes on agonist-induced receptor activation.
24305054	7	49	theme	domain	926:931	arg1	closure					933:939	its domain closure	922:939	its domain closure	922:939	An antagonist confines GBR1 to the open conformation of the inactive state, whereas an agonist induces its domain closure for activation.
24305054	1	50	theme	γ-aminobutyric	84:97	arg1	GABA					75:78	Human GABA	69:78	Human GABA(B) (γ-aminobutyric acid class B) receptor	69:120	Human GABA(B) (γ-aminobutyric acid class B) receptor is a G-protein-coupled receptor central to inhibitory neurotransmission in the brain.
24305054	1	50	theme	γ-aminobutyric	84:97	arg1	B					110:110	γ-aminobutyric acid class B	84:110	γ-aminobutyric acid class B	84:110	Human GABA(B) (γ-aminobutyric acid class B) receptor is a G-protein-coupled receptor central to inhibitory neurotransmission in the brain.
24305054	0	51	theme	B	56:56	arg1	receptor					59:66	human GABA(B) receptor	45:66	human GABA(B) receptor	45:66	Structural mechanism of ligand activation in human GABA(B) receptor.
24305054	6	52	theme	GBR1	779:782	arg1	crevice					768:774	the interdomain crevice	752:774	the interdomain crevice of GBR1	752:782	The agonists and antagonists are anchored in the interdomain crevice of GBR1 by an overlapping set of residues.
24305054	1	53	theme	acid	99:102	arg1	GABA					75:78	Human GABA	69:78	Human GABA(B) (γ-aminobutyric acid class B) receptor	69:120	Human GABA(B) (γ-aminobutyric acid class B) receptor is a G-protein-coupled receptor central to inhibitory neurotransmission in the brain.
24305054	1	53	theme	acid	99:102	arg1	B					110:110	γ-aminobutyric acid class B	84:110	γ-aminobutyric acid class B	84:110	Human GABA(B) (γ-aminobutyric acid class B) receptor is a G-protein-coupled receptor central to inhibitory neurotransmission in the brain.
24305054	1	54	theme	class	104:108	arg1	GABA					75:78	Human GABA	69:78	Human GABA(B) (γ-aminobutyric acid class B) receptor	69:120	Human GABA(B) (γ-aminobutyric acid class B) receptor is a G-protein-coupled receptor central to inhibitory neurotransmission in the brain.
24305054	1	54	theme	class	104:108	arg1	B					110:110	γ-aminobutyric acid class B	84:110	γ-aminobutyric acid class B	84:110	Human GABA(B) (γ-aminobutyric acid class B) receptor is a G-protein-coupled receptor central to inhibitory neurotransmission in the brain.
24305054	8	55	theme	interface	1075:1083	arg1	formation					1042:1050	the formation	1038:1050	the formation of a novel heterodimer interface between subunits	1038:1100	Our data reveal a unique activation mechanism for GABA(B) receptor that involves the formation of a novel heterodimer interface between subunits.
20356844	4	0	attach	present	750:756	arg1	form					806:809	apo form	802:809	apo form to 3.2 A	802:818	Here we present the crystal structure of the human ntSI, in apo form to 3.2 A and in complex with the inhibitor kotalanol to 2.15 A resolution.
20356844	4	0	attach	present	750:756	arg1	complex					827:833	complex	827:833	complex with the inhibitor kotalanol to 2.15 A resolution	827:883	Here we present the crystal structure of the human ntSI, in apo form to 3.2 A and in complex with the inhibitor kotalanol to 2.15 A resolution.
20356844	4	0	attach	present	750:756	arg2	we					747:748	we	747:748	we	747:748	Here we present the crystal structure of the human ntSI, in apo form to 3.2 A and in complex with the inhibitor kotalanol to 2.15 A resolution.
20356844	3	1	theme	human	553:557	arg1	MGAM					559:562	human MGAM	553:562	human MGAM (ntMGAM)	553:571	The N-terminal catalytic domain of human MGAM (ntMGAM) has a preference for short linear alpha-1,4-oligosaccharides, whereas N-terminal SI (ntSI) has a broader specificity for both alpha-1,4- and alpha-1,6-oligosaccharides.
20356844	3	1	theme	human	553:557	arg1	ntMGAM					565:570	ntMGAM	565:570	ntMGAM	565:570	The N-terminal catalytic domain of human MGAM (ntMGAM) has a preference for short linear alpha-1,4-oligosaccharides, whereas N-terminal SI (ntSI) has a broader specificity for both alpha-1,4- and alpha-1,6-oligosaccharides.
20356844	1	2	theme	alpha-1,4-	265:274	arg1	substrates					315:324	linear alpha-1,4- and branched alpha-1,6-oligosaccharide substrates	258:324	linear alpha-1,4- and branched alpha-1,6-oligosaccharide substrates that typically make up terminal starch digestion products	258:382	Human maltase-glucoamylase (MGAM) and sucrase-isomaltase (SI) are small intestinal enzymes that work concurrently to hydrolyze the mixture of linear alpha-1,4- and branched alpha-1,6-oligosaccharide substrates that typically make up terminal starch digestion products.
20356844	0	3	theme	N-terminal	96:105	arg1	domains					107:113	sucrase-isomaltase N-terminal domains	77:113	sucrase-isomaltase N-terminal domains	77:113	Structural basis for substrate selectivity in human maltase-glucoamylase and sucrase-isomaltase N-terminal domains.
20356844	3	4	theme	MGAM	559:562	arg1	domain					543:548	The N-terminal catalytic domain	518:548	The N-terminal catalytic domain of human MGAM (ntMGAM)	518:571	The N-terminal catalytic domain of human MGAM (ntMGAM) has a preference for short linear alpha-1,4-oligosaccharides, whereas N-terminal SI (ntSI) has a broader specificity for both alpha-1,4- and alpha-1,6-oligosaccharides.
20356844	3	4	theme	MGAM	559:562	arg1	MGAM					559:562	human MGAM	553:562	human MGAM (ntMGAM)	553:571	The N-terminal catalytic domain of human MGAM (ntMGAM) has a preference for short linear alpha-1,4-oligosaccharides, whereas N-terminal SI (ntSI) has a broader specificity for both alpha-1,4- and alpha-1,6-oligosaccharides.
20356844	4	5	theme	apo	802:804	arg1	form					806:809	apo form	802:809	apo form to 3.2 A	802:818	Here we present the crystal structure of the human ntSI, in apo form to 3.2 A and in complex with the inhibitor kotalanol to 2.15 A resolution.
20356844	4	6	theme	ntSI	793:796	arg1	structure					770:778	the crystal structure	758:778	the crystal structure of the human ntSI	758:796	Here we present the crystal structure of the human ntSI, in apo form to 3.2 A and in complex with the inhibitor kotalanol to 2.15 A resolution.
20356844	1	7	theme	branched	280:287	arg1	substrates					315:324	linear alpha-1,4- and branched alpha-1,6-oligosaccharide substrates	258:324	linear alpha-1,4- and branched alpha-1,6-oligosaccharide substrates that typically make up terminal starch digestion products	258:382	Human maltase-glucoamylase (MGAM) and sucrase-isomaltase (SI) are small intestinal enzymes that work concurrently to hydrolyze the mixture of linear alpha-1,4- and branched alpha-1,6-oligosaccharide substrates that typically make up terminal starch digestion products.
20356844	4	8	theme	human	787:791	arg1	ntSI					793:796	the human ntSI	783:796	the human ntSI	783:796	Here we present the crystal structure of the human ntSI, in apo form to 3.2 A and in complex with the inhibitor kotalanol to 2.15 A resolution.
20356844	4	9	dep	resolution	874:883	arg1	to					864:865	to	864:865	to	864:865	Here we present the crystal structure of the human ntSI, in apo form to 3.2 A and in complex with the inhibitor kotalanol to 2.15 A resolution.
20356844	1	10	theme	alpha-1,6-oligosaccharide	289:313	arg1	substrates					315:324	linear alpha-1,4- and branched alpha-1,6-oligosaccharide substrates	258:324	linear alpha-1,4- and branched alpha-1,6-oligosaccharide substrates that typically make up terminal starch digestion products	258:382	Human maltase-glucoamylase (MGAM) and sucrase-isomaltase (SI) are small intestinal enzymes that work concurrently to hydrolyze the mixture of linear alpha-1,4- and branched alpha-1,6-oligosaccharide substrates that typically make up terminal starch digestion products.
20356844	5	11	theme	Structural	886:895	arg1	comparison					897:906	Structural comparison	886:906	Structural comparison with the previously solved structure of ntMGAM	886:953	Structural comparison with the previously solved structure of ntMGAM reveals key active site differences in ntSI, including a narrow hydrophobic +1 subsite, which may account for its additional substrate specificity for alpha-1,6 substrates.
20356844	1	12	theme	small	182:186	arg1	enzymes					199:205	small intestinal enzymes	182:205	small intestinal enzymes that work concurrently to hydrolyze the mixture of linear alpha-1,4- and branched alpha-1,6-oligosaccharide substrates that typically make up terminal starch digestion products	182:382	Human maltase-glucoamylase (MGAM) and sucrase-isomaltase (SI) are small intestinal enzymes that work concurrently to hydrolyze the mixture of linear alpha-1,4- and branched alpha-1,6-oligosaccharide substrates that typically make up terminal starch digestion products.
20356844	1	12	theme	small	182:186	arg1	sucrase-isomaltase					154:171	sucrase-isomaltase	154:171	sucrase-isomaltase (SI)	154:176	Human maltase-glucoamylase (MGAM) and sucrase-isomaltase (SI) are small intestinal enzymes that work concurrently to hydrolyze the mixture of linear alpha-1,4- and branched alpha-1,6-oligosaccharide substrates that typically make up terminal starch digestion products.
20356844	1	12	theme	small	182:186	arg1	maltase-glucoamylase					122:141	Human maltase-glucoamylase	116:141	Human maltase-glucoamylase (MGAM)	116:148	Human maltase-glucoamylase (MGAM) and sucrase-isomaltase (SI) are small intestinal enzymes that work concurrently to hydrolyze the mixture of linear alpha-1,4- and branched alpha-1,6-oligosaccharide substrates that typically make up terminal starch digestion products.
20356844	2	13	theme	substrate	493:501	arg1	specificities					503:515	overlapping substrate specificities	481:515	overlapping substrate specificities	481:515	MGAM and SI are each composed of duplicated catalytic domains, N- and C-terminal, which display overlapping substrate specificities.
20356844	5	14	theme	solved	928:933	arg1	structure					935:943	the previously solved structure	913:943	the previously solved structure of ntMGAM	913:953	Structural comparison with the previously solved structure of ntMGAM reveals key active site differences in ntSI, including a narrow hydrophobic +1 subsite, which may account for its additional substrate specificity for alpha-1,6 substrates.
20356844	4	15	theme	kotalanol	854:862	arg1	resolution					874:883	the inhibitor kotalanol to 2.15 A resolution	840:883	the inhibitor kotalanol to 2.15 A resolution	840:883	Here we present the crystal structure of the human ntSI, in apo form to 3.2 A and in complex with the inhibitor kotalanol to 2.15 A resolution.
20356844	5	16	theme	key	963:965	arg1	differences					979:989	key active site differences	963:989	key active site differences	963:989	Structural comparison with the previously solved structure of ntMGAM reveals key active site differences in ntSI, including a narrow hydrophobic +1 subsite, which may account for its additional substrate specificity for alpha-1,6 substrates.
20356844	5	16	theme	key	963:965	arg1	subsite					1034:1040	a narrow hydrophobic +1 subsite	1010:1040	a narrow hydrophobic +1 subsite	1010:1040	Structural comparison with the previously solved structure of ntMGAM reveals key active site differences in ntSI, including a narrow hydrophobic +1 subsite, which may account for its additional substrate specificity for alpha-1,6 substrates.
20356844	1	17	theme	intestinal	188:197	arg1	enzymes					199:205	small intestinal enzymes	182:205	small intestinal enzymes that work concurrently to hydrolyze the mixture of linear alpha-1,4- and branched alpha-1,6-oligosaccharide substrates that typically make up terminal starch digestion products	182:382	Human maltase-glucoamylase (MGAM) and sucrase-isomaltase (SI) are small intestinal enzymes that work concurrently to hydrolyze the mixture of linear alpha-1,4- and branched alpha-1,6-oligosaccharide substrates that typically make up terminal starch digestion products.
20356844	1	17	theme	intestinal	188:197	arg1	sucrase-isomaltase					154:171	sucrase-isomaltase	154:171	sucrase-isomaltase (SI)	154:176	Human maltase-glucoamylase (MGAM) and sucrase-isomaltase (SI) are small intestinal enzymes that work concurrently to hydrolyze the mixture of linear alpha-1,4- and branched alpha-1,6-oligosaccharide substrates that typically make up terminal starch digestion products.
20356844	1	17	theme	intestinal	188:197	arg1	maltase-glucoamylase					122:141	Human maltase-glucoamylase	116:141	Human maltase-glucoamylase (MGAM)	116:148	Human maltase-glucoamylase (MGAM) and sucrase-isomaltase (SI) are small intestinal enzymes that work concurrently to hydrolyze the mixture of linear alpha-1,4- and branched alpha-1,6-oligosaccharide substrates that typically make up terminal starch digestion products.
20356844	2	18	theme	overlapping	481:491	arg1	specificities					503:515	overlapping substrate specificities	481:515	overlapping substrate specificities	481:515	MGAM and SI are each composed of duplicated catalytic domains, N- and C-terminal, which display overlapping substrate specificities.
20356844	0	19	from	selectivity	31:41	arg1	domains					107:113	sucrase-isomaltase N-terminal domains	77:113	sucrase-isomaltase N-terminal domains	77:113	Structural basis for substrate selectivity in human maltase-glucoamylase and sucrase-isomaltase N-terminal domains.
20356844	0	19	from	selectivity	31:41	arg1	maltase-glucoamylase					52:71	human maltase-glucoamylase	46:71	human maltase-glucoamylase	46:71	Structural basis for substrate selectivity in human maltase-glucoamylase and sucrase-isomaltase N-terminal domains.
20356844	4	20	theme	A	872:872	arg1	resolution					874:883	the inhibitor kotalanol to 2.15 A resolution	840:883	the inhibitor kotalanol to 2.15 A resolution	840:883	Here we present the crystal structure of the human ntSI, in apo form to 3.2 A and in complex with the inhibitor kotalanol to 2.15 A resolution.
20356844	3	21	theme	linear	600:605	arg1	alpha-1,4-oligosaccharides					607:632	short linear alpha-1,4-oligosaccharides	594:632	short linear alpha-1,4-oligosaccharides	594:632	The N-terminal catalytic domain of human MGAM (ntMGAM) has a preference for short linear alpha-1,4-oligosaccharides, whereas N-terminal SI (ntSI) has a broader specificity for both alpha-1,4- and alpha-1,6-oligosaccharides.
20356844	2	22	theme	duplicated	418:427	arg1	N-					448:449	N-	448:449	N-	448:449	MGAM and SI are each composed of duplicated catalytic domains, N- and C-terminal, which display overlapping substrate specificities.
20356844	2	22	theme	duplicated	418:427	arg1	domains					439:445	duplicated catalytic domains	418:445	duplicated catalytic domains	418:445	MGAM and SI are each composed of duplicated catalytic domains, N- and C-terminal, which display overlapping substrate specificities.
20356844	2	22	theme	duplicated	418:427	arg1	C-terminal					455:464	C-terminal	455:464	C-terminal	455:464	MGAM and SI are each composed of duplicated catalytic domains, N- and C-terminal, which display overlapping substrate specificities.
20356844	0	23	theme	Structural	0:9	arg1	basis					11:15	Structural basis	0:15	Structural basis for substrate selectivity in human maltase-glucoamylase and sucrase-isomaltase N-terminal domains.	0:114	Structural basis for substrate selectivity in human maltase-glucoamylase and sucrase-isomaltase N-terminal domains.
20356844	1	24	theme	substrates	315:324	arg1	mixture					247:253	the mixture	243:253	the mixture of linear alpha-1,4- and branched alpha-1,6-oligosaccharide substrates that typically make up terminal starch digestion products	243:382	Human maltase-glucoamylase (MGAM) and sucrase-isomaltase (SI) are small intestinal enzymes that work concurrently to hydrolyze the mixture of linear alpha-1,4- and branched alpha-1,6-oligosaccharide substrates that typically make up terminal starch digestion products.
20356844	1	25	theme	Human	116:120	arg1	enzymes					199:205	small intestinal enzymes	182:205	small intestinal enzymes that work concurrently to hydrolyze the mixture of linear alpha-1,4- and branched alpha-1,6-oligosaccharide substrates that typically make up terminal starch digestion products	182:382	Human maltase-glucoamylase (MGAM) and sucrase-isomaltase (SI) are small intestinal enzymes that work concurrently to hydrolyze the mixture of linear alpha-1,4- and branched alpha-1,6-oligosaccharide substrates that typically make up terminal starch digestion products.
20356844	1	25	theme	Human	116:120	arg1	MGAM					144:147	MGAM	144:147	MGAM	144:147	Human maltase-glucoamylase (MGAM) and sucrase-isomaltase (SI) are small intestinal enzymes that work concurrently to hydrolyze the mixture of linear alpha-1,4- and branched alpha-1,6-oligosaccharide substrates that typically make up terminal starch digestion products.
20356844	1	25	theme	Human	116:120	arg1	sucrase-isomaltase					154:171	sucrase-isomaltase	154:171	sucrase-isomaltase (SI)	154:176	Human maltase-glucoamylase (MGAM) and sucrase-isomaltase (SI) are small intestinal enzymes that work concurrently to hydrolyze the mixture of linear alpha-1,4- and branched alpha-1,6-oligosaccharide substrates that typically make up terminal starch digestion products.
20356844	1	25	theme	Human	116:120	arg1	maltase-glucoamylase					122:141	Human maltase-glucoamylase	116:141	Human maltase-glucoamylase (MGAM)	116:148	Human maltase-glucoamylase (MGAM) and sucrase-isomaltase (SI) are small intestinal enzymes that work concurrently to hydrolyze the mixture of linear alpha-1,4- and branched alpha-1,6-oligosaccharide substrates that typically make up terminal starch digestion products.
20356844	0	26	theme	substrate	21:29	arg1	selectivity					31:41	substrate selectivity	21:41	substrate selectivity in human maltase-glucoamylase and sucrase-isomaltase N-terminal domains	21:113	Structural basis for substrate selectivity in human maltase-glucoamylase and sucrase-isomaltase N-terminal domains.
20356844	5	27	theme	alpha-1,6	1106:1114	arg1	substrates					1116:1125	alpha-1,6 substrates	1106:1125	alpha-1,6 substrates	1106:1125	Structural comparison with the previously solved structure of ntMGAM reveals key active site differences in ntSI, including a narrow hydrophobic +1 subsite, which may account for its additional substrate specificity for alpha-1,6 substrates.
20356844	5	28	theme	site	974:977	arg1	differences					979:989	key active site differences	963:989	key active site differences	963:989	Structural comparison with the previously solved structure of ntMGAM reveals key active site differences in ntSI, including a narrow hydrophobic +1 subsite, which may account for its additional substrate specificity for alpha-1,6 substrates.
20356844	5	28	theme	site	974:977	arg1	subsite					1034:1040	a narrow hydrophobic +1 subsite	1010:1040	a narrow hydrophobic +1 subsite	1010:1040	Structural comparison with the previously solved structure of ntMGAM reveals key active site differences in ntSI, including a narrow hydrophobic +1 subsite, which may account for its additional substrate specificity for alpha-1,6 substrates.
20356844	5	29	theme	active	967:972	arg1	differences					979:989	key active site differences	963:989	key active site differences	963:989	Structural comparison with the previously solved structure of ntMGAM reveals key active site differences in ntSI, including a narrow hydrophobic +1 subsite, which may account for its additional substrate specificity for alpha-1,6 substrates.
20356844	5	29	theme	active	967:972	arg1	subsite					1034:1040	a narrow hydrophobic +1 subsite	1010:1040	a narrow hydrophobic +1 subsite	1010:1040	Structural comparison with the previously solved structure of ntMGAM reveals key active site differences in ntSI, including a narrow hydrophobic +1 subsite, which may account for its additional substrate specificity for alpha-1,6 substrates.
20356844	5	30	theme	substrate	1080:1088	arg1	specificity					1090:1100	its additional substrate specificity	1065:1100	its additional substrate specificity for alpha-1,6 substrates	1065:1125	Structural comparison with the previously solved structure of ntMGAM reveals key active site differences in ntSI, including a narrow hydrophobic +1 subsite, which may account for its additional substrate specificity for alpha-1,6 substrates.
20356844	3	31	theme	short	594:598	arg1	alpha-1,4-oligosaccharides					607:632	short linear alpha-1,4-oligosaccharides	594:632	short linear alpha-1,4-oligosaccharides	594:632	The N-terminal catalytic domain of human MGAM (ntMGAM) has a preference for short linear alpha-1,4-oligosaccharides, whereas N-terminal SI (ntSI) has a broader specificity for both alpha-1,4- and alpha-1,6-oligosaccharides.
20356844	5	32	theme	+1	1031:1032	arg1	subsite					1034:1040	a narrow hydrophobic +1 subsite	1010:1040	a narrow hydrophobic +1 subsite	1010:1040	Structural comparison with the previously solved structure of ntMGAM reveals key active site differences in ntSI, including a narrow hydrophobic +1 subsite, which may account for its additional substrate specificity for alpha-1,6 substrates.
20356844	3	33	theme	N-terminal	643:652	arg1	ntSI					658:661	ntSI	658:661	ntSI	658:661	The N-terminal catalytic domain of human MGAM (ntMGAM) has a preference for short linear alpha-1,4-oligosaccharides, whereas N-terminal SI (ntSI) has a broader specificity for both alpha-1,4- and alpha-1,6-oligosaccharides.
20356844	3	33	theme	N-terminal	643:652	arg1	SI					654:655	N-terminal SI	643:655	N-terminal SI (ntSI)	643:662	The N-terminal catalytic domain of human MGAM (ntMGAM) has a preference for short linear alpha-1,4-oligosaccharides, whereas N-terminal SI (ntSI) has a broader specificity for both alpha-1,4- and alpha-1,6-oligosaccharides.
20356844	3	34	contain	has	573:575	arg1	domain					543:548	The N-terminal catalytic domain	518:548	The N-terminal catalytic domain of human MGAM (ntMGAM)	518:571	The N-terminal catalytic domain of human MGAM (ntMGAM) has a preference for short linear alpha-1,4-oligosaccharides, whereas N-terminal SI (ntSI) has a broader specificity for both alpha-1,4- and alpha-1,6-oligosaccharides.
20356844	3	34	contain	has	573:575	arg1	MGAM					559:562	human MGAM	553:562	human MGAM (ntMGAM)	553:571	The N-terminal catalytic domain of human MGAM (ntMGAM) has a preference for short linear alpha-1,4-oligosaccharides, whereas N-terminal SI (ntSI) has a broader specificity for both alpha-1,4- and alpha-1,6-oligosaccharides.
20356844	3	34	contain	has	573:575	arg2	preference					579:588	a preference	577:588	a preference for short linear alpha-1,4-oligosaccharides	577:632	The N-terminal catalytic domain of human MGAM (ntMGAM) has a preference for short linear alpha-1,4-oligosaccharides, whereas N-terminal SI (ntSI) has a broader specificity for both alpha-1,4- and alpha-1,6-oligosaccharides.
20356844	1	35	theme	terminal	349:356	arg1	products					375:382	terminal starch digestion products	349:382	terminal starch digestion products	349:382	Human maltase-glucoamylase (MGAM) and sucrase-isomaltase (SI) are small intestinal enzymes that work concurrently to hydrolyze the mixture of linear alpha-1,4- and branched alpha-1,6-oligosaccharide substrates that typically make up terminal starch digestion products.
20356844	3	36	theme	broader	670:676	arg1	specificity					678:688	a broader specificity	668:688	a broader specificity for both alpha-1,4- and alpha-1,6-oligosaccharides	668:739	The N-terminal catalytic domain of human MGAM (ntMGAM) has a preference for short linear alpha-1,4-oligosaccharides, whereas N-terminal SI (ntSI) has a broader specificity for both alpha-1,4- and alpha-1,6-oligosaccharides.
20356844	4	37	theme	inhibitor	844:852	arg1	resolution					874:883	the inhibitor kotalanol to 2.15 A resolution	840:883	the inhibitor kotalanol to 2.15 A resolution	840:883	Here we present the crystal structure of the human ntSI, in apo form to 3.2 A and in complex with the inhibitor kotalanol to 2.15 A resolution.
20356844	4	38	theme	crystal	762:768	arg1	structure					770:778	the crystal structure	758:778	the crystal structure of the human ntSI	758:796	Here we present the crystal structure of the human ntSI, in apo form to 3.2 A and in complex with the inhibitor kotalanol to 2.15 A resolution.
20356844	0	39	theme	human	46:50	arg1	maltase-glucoamylase					52:71	human maltase-glucoamylase	46:71	human maltase-glucoamylase	46:71	Structural basis for substrate selectivity in human maltase-glucoamylase and sucrase-isomaltase N-terminal domains.
20356844	1	40	theme	starch	358:363	arg1	products					375:382	terminal starch digestion products	349:382	terminal starch digestion products	349:382	Human maltase-glucoamylase (MGAM) and sucrase-isomaltase (SI) are small intestinal enzymes that work concurrently to hydrolyze the mixture of linear alpha-1,4- and branched alpha-1,6-oligosaccharide substrates that typically make up terminal starch digestion products.
20356844	5	41	with	comparison	897:906	arg1	structure					935:943	the previously solved structure	913:943	the previously solved structure of ntMGAM	913:953	Structural comparison with the previously solved structure of ntMGAM reveals key active site differences in ntSI, including a narrow hydrophobic +1 subsite, which may account for its additional substrate specificity for alpha-1,6 substrates.
20356844	3	42	dep	has	573:575	arg1	whereas					635:641	whereas	635:641	whereas	635:641	The N-terminal catalytic domain of human MGAM (ntMGAM) has a preference for short linear alpha-1,4-oligosaccharides, whereas N-terminal SI (ntSI) has a broader specificity for both alpha-1,4- and alpha-1,6-oligosaccharides.
20356844	1	43	theme	digestion	365:373	arg1	products					375:382	terminal starch digestion products	349:382	terminal starch digestion products	349:382	Human maltase-glucoamylase (MGAM) and sucrase-isomaltase (SI) are small intestinal enzymes that work concurrently to hydrolyze the mixture of linear alpha-1,4- and branched alpha-1,6-oligosaccharide substrates that typically make up terminal starch digestion products.
20356844	3	44	theme	N-terminal	522:531	arg1	domain					543:548	The N-terminal catalytic domain	518:548	The N-terminal catalytic domain of human MGAM (ntMGAM)	518:571	The N-terminal catalytic domain of human MGAM (ntMGAM) has a preference for short linear alpha-1,4-oligosaccharides, whereas N-terminal SI (ntSI) has a broader specificity for both alpha-1,4- and alpha-1,6-oligosaccharides.
20356844	3	44	theme	N-terminal	522:531	arg1	MGAM					559:562	human MGAM	553:562	human MGAM (ntMGAM)	553:571	The N-terminal catalytic domain of human MGAM (ntMGAM) has a preference for short linear alpha-1,4-oligosaccharides, whereas N-terminal SI (ntSI) has a broader specificity for both alpha-1,4- and alpha-1,6-oligosaccharides.
20356844	5	45	from	differences	979:989	arg1	ntSI					994:997	ntSI	994:997	ntSI	994:997	Structural comparison with the previously solved structure of ntMGAM reveals key active site differences in ntSI, including a narrow hydrophobic +1 subsite, which may account for its additional substrate specificity for alpha-1,6 substrates.
20356844	5	46	theme	narrow	1012:1017	arg1	subsite					1034:1040	a narrow hydrophobic +1 subsite	1010:1040	a narrow hydrophobic +1 subsite	1010:1040	Structural comparison with the previously solved structure of ntMGAM reveals key active site differences in ntSI, including a narrow hydrophobic +1 subsite, which may account for its additional substrate specificity for alpha-1,6 substrates.
20356844	3	47	theme	catalytic	533:541	arg1	domain					543:548	The N-terminal catalytic domain	518:548	The N-terminal catalytic domain of human MGAM (ntMGAM)	518:571	The N-terminal catalytic domain of human MGAM (ntMGAM) has a preference for short linear alpha-1,4-oligosaccharides, whereas N-terminal SI (ntSI) has a broader specificity for both alpha-1,4- and alpha-1,6-oligosaccharides.
20356844	3	47	theme	catalytic	533:541	arg1	MGAM					559:562	human MGAM	553:562	human MGAM (ntMGAM)	553:571	The N-terminal catalytic domain of human MGAM (ntMGAM) has a preference for short linear alpha-1,4-oligosaccharides, whereas N-terminal SI (ntSI) has a broader specificity for both alpha-1,4- and alpha-1,6-oligosaccharides.
20356844	5	48	theme	ntMGAM	948:953	arg1	structure					935:943	the previously solved structure	913:943	the previously solved structure of ntMGAM	913:953	Structural comparison with the previously solved structure of ntMGAM reveals key active site differences in ntSI, including a narrow hydrophobic +1 subsite, which may account for its additional substrate specificity for alpha-1,6 substrates.
20356844	0	49	theme	sucrase-isomaltase	77:94	arg1	domains					107:113	sucrase-isomaltase N-terminal domains	77:113	sucrase-isomaltase N-terminal domains	77:113	Structural basis for substrate selectivity in human maltase-glucoamylase and sucrase-isomaltase N-terminal domains.
20356844	5	50	theme	additional	1069:1078	arg1	specificity					1090:1100	its additional substrate specificity	1065:1100	its additional substrate specificity for alpha-1,6 substrates	1065:1125	Structural comparison with the previously solved structure of ntMGAM reveals key active site differences in ntSI, including a narrow hydrophobic +1 subsite, which may account for its additional substrate specificity for alpha-1,6 substrates.
20356844	5	51	theme	hydrophobic	1019:1029	arg1	subsite					1034:1040	a narrow hydrophobic +1 subsite	1010:1040	a narrow hydrophobic +1 subsite	1010:1040	Structural comparison with the previously solved structure of ntMGAM reveals key active site differences in ntSI, including a narrow hydrophobic +1 subsite, which may account for its additional substrate specificity for alpha-1,6 substrates.
20356844	2	52	theme	catalytic	429:437	arg1	N-					448:449	N-	448:449	N-	448:449	MGAM and SI are each composed of duplicated catalytic domains, N- and C-terminal, which display overlapping substrate specificities.
20356844	2	52	theme	catalytic	429:437	arg1	domains					439:445	duplicated catalytic domains	418:445	duplicated catalytic domains	418:445	MGAM and SI are each composed of duplicated catalytic domains, N- and C-terminal, which display overlapping substrate specificities.
20356844	2	52	theme	catalytic	429:437	arg1	C-terminal					455:464	C-terminal	455:464	C-terminal	455:464	MGAM and SI are each composed of duplicated catalytic domains, N- and C-terminal, which display overlapping substrate specificities.
20356844	3	53	contain	has	664:666	arg1	ntSI					658:661	ntSI	658:661	ntSI	658:661	The N-terminal catalytic domain of human MGAM (ntMGAM) has a preference for short linear alpha-1,4-oligosaccharides, whereas N-terminal SI (ntSI) has a broader specificity for both alpha-1,4- and alpha-1,6-oligosaccharides.
20356844	3	53	contain	has	664:666	arg1	SI					654:655	N-terminal SI	643:655	N-terminal SI (ntSI)	643:662	The N-terminal catalytic domain of human MGAM (ntMGAM) has a preference for short linear alpha-1,4-oligosaccharides, whereas N-terminal SI (ntSI) has a broader specificity for both alpha-1,4- and alpha-1,6-oligosaccharides.
20356844	3	53	contain	has	664:666	arg2	specificity					678:688	a broader specificity	668:688	a broader specificity for both alpha-1,4- and alpha-1,6-oligosaccharides	668:739	The N-terminal catalytic domain of human MGAM (ntMGAM) has a preference for short linear alpha-1,4-oligosaccharides, whereas N-terminal SI (ntSI) has a broader specificity for both alpha-1,4- and alpha-1,6-oligosaccharides.
20356844	4	54	with	complex	827:833	arg1	resolution					874:883	the inhibitor kotalanol to 2.15 A resolution	840:883	the inhibitor kotalanol to 2.15 A resolution	840:883	Here we present the crystal structure of the human ntSI, in apo form to 3.2 A and in complex with the inhibitor kotalanol to 2.15 A resolution.
20356844	1	55	theme	linear	258:263	arg1	substrates					315:324	linear alpha-1,4- and branched alpha-1,6-oligosaccharide substrates	258:324	linear alpha-1,4- and branched alpha-1,6-oligosaccharide substrates that typically make up terminal starch digestion products	258:382	Human maltase-glucoamylase (MGAM) and sucrase-isomaltase (SI) are small intestinal enzymes that work concurrently to hydrolyze the mixture of linear alpha-1,4- and branched alpha-1,6-oligosaccharide substrates that typically make up terminal starch digestion products.
30872481	0	0	theme	C5	85:86	arg1	epimerase					88:96	human heparan sulfate d-glucuronyl C5 epimerase	50:96	human heparan sulfate d-glucuronyl C5 epimerase	50:96	Substrate binding mode and catalytic mechanism of human heparan sulfate d-glucuronyl C5 epimerase.
30872481	2	1	theme	internal	435:442	arg1	flexibility					444:454	internal flexibility	435:454	internal flexibility	435:454	Of these, glucuronyl C5-epimerase (Glce) catalyzes C5-epimerization of the HS component, d-glucuronic acid (GlcA), into l-iduronic acid (IdoA), which provides internal flexibility to the polymer and forges protein-binding sites to ensure polymer function.
30872481	7	2	theme	racemase	1514:1521	arg1	intermediate					1475:1486	a neutral enol intermediate	1460:1486	a neutral enol intermediate	1460:1486	The structure-based mechanism involves the two invariant acid/base residues, Glu499 and Tyr578, poised on each side of the target uronic acid residue, thus allowing reversible abstraction and readdition of a proton at the C5 position through a neutral enol intermediate, reminiscent of mandelate racemase.
30872481	7	2	theme	racemase	1514:1521	arg1	reminiscent					1489:1499	reminiscent	1489:1499	reminiscent of mandelate racemase	1489:1521	The structure-based mechanism involves the two invariant acid/base residues, Glu499 and Tyr578, poised on each side of the target uronic acid residue, thus allowing reversible abstraction and readdition of a proton at the C5 position through a neutral enol intermediate, reminiscent of mandelate racemase.
30872481	0	3	theme	d-glucuronyl	72:83	arg1	epimerase					88:96	human heparan sulfate d-glucuronyl C5 epimerase	50:96	human heparan sulfate d-glucuronyl C5 epimerase	50:96	Substrate binding mode and catalytic mechanism of human heparan sulfate d-glucuronyl C5 epimerase.
30872481	7	4	theme	proton	1426:1431	arg1	readdition					1410:1419	readdition	1410:1419	readdition	1410:1419	The structure-based mechanism involves the two invariant acid/base residues, Glu499 and Tyr578, poised on each side of the target uronic acid residue, thus allowing reversible abstraction and readdition of a proton at the C5 position through a neutral enol intermediate, reminiscent of mandelate racemase.
30872481	7	4	theme	proton	1426:1431	arg1	abstraction					1394:1404	reversible abstraction	1383:1404	reversible abstraction	1383:1404	The structure-based mechanism involves the two invariant acid/base residues, Glu499 and Tyr578, poised on each side of the target uronic acid residue, thus allowing reversible abstraction and readdition of a proton at the C5 position through a neutral enol intermediate, reminiscent of mandelate racemase.
30872481	4	5	theme	oligosaccharides	761:776	arg1	infiltration					741:752	Deep infiltration	736:752	Deep infiltration of the oligosaccharides into the active site cleft	736:803	Deep infiltration of the oligosaccharides into the active site cleft imposes a sharp kink within the central GlcNS-GlcA/IdoA-GlcNS trisaccharide motif.
30872481	4	6	theme	GlcNS-GlcA/IdoA-GlcNS	845:865	arg1	motif					881:885	the central GlcNS-GlcA/IdoA-GlcNS trisaccharide motif	833:885	the central GlcNS-GlcA/IdoA-GlcNS trisaccharide motif	833:885	Deep infiltration of the oligosaccharides into the active site cleft imposes a sharp kink within the central GlcNS-GlcA/IdoA-GlcNS trisaccharide motif.
30872481	6	7	theme	boat	1141:1144	arg1	conformations					1146:1158	two closely related boat conformations	1121:1158	two closely related boat conformations	1121:1158	At the epimerization site, the GlcA/IdoA rings are highly constrained in two closely related boat conformations, highlighting ring-puckering signatures during catalysis.
30872481	4	8	theme	active	787:792	arg1	cleft					799:803	the active site cleft	783:803	the active site cleft	783:803	Deep infiltration of the oligosaccharides into the active site cleft imposes a sharp kink within the central GlcNS-GlcA/IdoA-GlcNS trisaccharide motif.
30872481	8	9	dep	heparin	1695:1701	arg1	analogs					1709:1715	analogs	1709:1715	analogs	1709:1715	These structures also shed light on a convergent mechanism of action between HS epimerases and lyases and provide molecular frameworks for the chemoenzymatic synthesis of heparin or HS analogs.
30872481	7	10	theme	reversible	1383:1392	arg1	abstraction					1394:1404	reversible abstraction	1383:1404	reversible abstraction	1383:1404	The structure-based mechanism involves the two invariant acid/base residues, Glu499 and Tyr578, poised on each side of the target uronic acid residue, thus allowing reversible abstraction and readdition of a proton at the C5 position through a neutral enol intermediate, reminiscent of mandelate racemase.
30872481	7	11	theme	acid	1355:1358	arg1	residue					1360:1366	the target uronic acid residue	1337:1366	the target uronic acid residue	1337:1366	The structure-based mechanism involves the two invariant acid/base residues, Glu499 and Tyr578, poised on each side of the target uronic acid residue, thus allowing reversible abstraction and readdition of a proton at the C5 position through a neutral enol intermediate, reminiscent of mandelate racemase.
30872481	0	12	theme	epimerase	88:96	arg1	mode					18:21	mode	18:21	mode	18:21	Substrate binding mode and catalytic mechanism of human heparan sulfate d-glucuronyl C5 epimerase.
30872481	0	12	theme	epimerase	88:96	arg1	mechanism					37:45	catalytic mechanism	27:45	catalytic mechanism of human heparan sulfate d-glucuronyl C5 epimerase	27:96	Substrate binding mode and catalytic mechanism of human heparan sulfate d-glucuronyl C5 epimerase.
30872481	5	13	theme	substrate	1029:1037	arg1	binding					1039:1045	substrate binding	1029:1045	substrate binding	1029:1045	An extensive network of specific interactions illustrates the absolute requirement of N-sulfate groups vicinal to the epimerization site for substrate binding.
30872481	8	14	theme	action	1586:1591	arg1	mechanism					1573:1581	a convergent mechanism	1560:1581	a convergent mechanism of action between HS epimerases and lyases	1560:1624	These structures also shed light on a convergent mechanism of action between HS epimerases and lyases and provide molecular frameworks for the chemoenzymatic synthesis of heparin or HS analogs.
30872481	3	15	theme	n	725:725	arg1	product					727:733	a (IdoA-GlcNS)n product	711:733	a (IdoA-GlcNS)n product	711:733	Here we report crystal structures of human Glce in the unbound state and of an inactive mutant, as assessed by real-time NMR spectroscopy, bound with a (GlcA-GlcNS)n substrate or a (IdoA-GlcNS)n product.
30872481	7	16	theme	target	1341:1346	arg1	residue					1360:1366	the target uronic acid residue	1337:1366	the target uronic acid residue	1337:1366	The structure-based mechanism involves the two invariant acid/base residues, Glu499 and Tyr578, poised on each side of the target uronic acid residue, thus allowing reversible abstraction and readdition of a proton at the C5 position through a neutral enol intermediate, reminiscent of mandelate racemase.
30872481	5	17	theme	extensive	891:899	arg1	network					901:907	An extensive network	888:907	An extensive network of specific interactions	888:932	An extensive network of specific interactions illustrates the absolute requirement of N-sulfate groups vicinal to the epimerization site for substrate binding.
30872481	4	18	theme	trisaccharide	867:879	arg1	motif					881:885	the central GlcNS-GlcA/IdoA-GlcNS trisaccharide motif	833:885	the central GlcNS-GlcA/IdoA-GlcNS trisaccharide motif	833:885	Deep infiltration of the oligosaccharides into the active site cleft imposes a sharp kink within the central GlcNS-GlcA/IdoA-GlcNS trisaccharide motif.
30872481	3	19	theme	real-time	643:651	arg1	spectroscopy					657:668	real-time NMR spectroscopy	643:668	real-time NMR spectroscopy	643:668	Here we report crystal structures of human Glce in the unbound state and of an inactive mutant, as assessed by real-time NMR spectroscopy, bound with a (GlcA-GlcNS)n substrate or a (IdoA-GlcNS)n product.
30872481	4	20	theme	Deep	736:739	arg1	infiltration					741:752	Deep infiltration	736:752	Deep infiltration of the oligosaccharides into the active site cleft	736:803	Deep infiltration of the oligosaccharides into the active site cleft imposes a sharp kink within the central GlcNS-GlcA/IdoA-GlcNS trisaccharide motif.
30872481	3	21	theme	IdoA-GlcNS	714:723	arg1	product					727:733	a (IdoA-GlcNS)n product	711:733	a (IdoA-GlcNS)n product	711:733	Here we report crystal structures of human Glce in the unbound state and of an inactive mutant, as assessed by real-time NMR spectroscopy, bound with a (GlcA-GlcNS)n substrate or a (IdoA-GlcNS)n product.
30872481	2	22	theme	d-glucuronic	365:376	arg1	GlcA					384:387	GlcA	384:387	GlcA	384:387	Of these, glucuronyl C5-epimerase (Glce) catalyzes C5-epimerization of the HS component, d-glucuronic acid (GlcA), into l-iduronic acid (IdoA), which provides internal flexibility to the polymer and forges protein-binding sites to ensure polymer function.
30872481	2	22	theme	d-glucuronic	365:376	arg1	component					354:362	the HS component	347:362	the HS component	347:362	Of these, glucuronyl C5-epimerase (Glce) catalyzes C5-epimerization of the HS component, d-glucuronic acid (GlcA), into l-iduronic acid (IdoA), which provides internal flexibility to the polymer and forges protein-binding sites to ensure polymer function.
30872481	2	22	theme	d-glucuronic	365:376	arg1	acid					378:381	d-glucuronic acid	365:381	d-glucuronic acid (GlcA)	365:388	Of these, glucuronyl C5-epimerase (Glce) catalyzes C5-epimerization of the HS component, d-glucuronic acid (GlcA), into l-iduronic acid (IdoA), which provides internal flexibility to the polymer and forges protein-binding sites to ensure polymer function.
30872481	3	23	theme	NMR	653:655	arg1	spectroscopy					657:668	real-time NMR spectroscopy	643:668	real-time NMR spectroscopy	643:668	Here we report crystal structures of human Glce in the unbound state and of an inactive mutant, as assessed by real-time NMR spectroscopy, bound with a (GlcA-GlcNS)n substrate or a (IdoA-GlcNS)n product.
30872481	7	24	from	position	1443:1450	arg1	readdition					1410:1419	readdition	1410:1419	readdition	1410:1419	The structure-based mechanism involves the two invariant acid/base residues, Glu499 and Tyr578, poised on each side of the target uronic acid residue, thus allowing reversible abstraction and readdition of a proton at the C5 position through a neutral enol intermediate, reminiscent of mandelate racemase.
30872481	7	24	from	position	1443:1450	arg1	abstraction					1394:1404	reversible abstraction	1383:1404	reversible abstraction	1383:1404	The structure-based mechanism involves the two invariant acid/base residues, Glu499 and Tyr578, poised on each side of the target uronic acid residue, thus allowing reversible abstraction and readdition of a proton at the C5 position through a neutral enol intermediate, reminiscent of mandelate racemase.
30872481	7	25	theme	residue	1360:1366	arg1	side					1329:1332	each side	1324:1332	each side of the target uronic acid residue	1324:1366	The structure-based mechanism involves the two invariant acid/base residues, Glu499 and Tyr578, poised on each side of the target uronic acid residue, thus allowing reversible abstraction and readdition of a proton at the C5 position through a neutral enol intermediate, reminiscent of mandelate racemase.
30872481	8	26	theme	chemoenzymatic	1667:1680	arg1	synthesis					1682:1690	the chemoenzymatic synthesis	1663:1690	the chemoenzymatic synthesis of heparin or HS analogs	1663:1715	These structures also shed light on a convergent mechanism of action between HS epimerases and lyases and provide molecular frameworks for the chemoenzymatic synthesis of heparin or HS analogs.
30872481	6	27	theme	related	1133:1139	arg1	conformations					1146:1158	two closely related boat conformations	1121:1158	two closely related boat conformations	1121:1158	At the epimerization site, the GlcA/IdoA rings are highly constrained in two closely related boat conformations, highlighting ring-puckering signatures during catalysis.
30872481	1	28	theme	Golgi-localized	251:265	arg1	enzymes					267:273	Golgi-localized enzymes	251:273	Golgi-localized enzymes	251:273	Heparan sulfate (HS) is a linear, complex polysaccharide that modulates the biological activities of proteins through binding sites made by a series of Golgi-localized enzymes.
30872481	7	29	theme	C5	1440:1441	arg1	position					1443:1450	the C5 position	1436:1450	the C5 position	1436:1450	The structure-based mechanism involves the two invariant acid/base residues, Glu499 and Tyr578, poised on each side of the target uronic acid residue, thus allowing reversible abstraction and readdition of a proton at the C5 position through a neutral enol intermediate, reminiscent of mandelate racemase.
30872481	2	30	theme	glucuronyl	286:295	arg1	Glce					311:314	Glce	311:314	Glce	311:314	Of these, glucuronyl C5-epimerase (Glce) catalyzes C5-epimerization of the HS component, d-glucuronic acid (GlcA), into l-iduronic acid (IdoA), which provides internal flexibility to the polymer and forges protein-binding sites to ensure polymer function.
30872481	2	30	theme	glucuronyl	286:295	arg1	C5-epimerase					297:308	glucuronyl C5-epimerase	286:308	glucuronyl C5-epimerase (Glce)	286:315	Of these, glucuronyl C5-epimerase (Glce) catalyzes C5-epimerization of the HS component, d-glucuronic acid (GlcA), into l-iduronic acid (IdoA), which provides internal flexibility to the polymer and forges protein-binding sites to ensure polymer function.
30872481	7	31	theme	uronic	1348:1353	arg1	residue					1360:1366	the target uronic acid residue	1337:1366	the target uronic acid residue	1337:1366	The structure-based mechanism involves the two invariant acid/base residues, Glu499 and Tyr578, poised on each side of the target uronic acid residue, thus allowing reversible abstraction and readdition of a proton at the C5 position through a neutral enol intermediate, reminiscent of mandelate racemase.
30872481	2	32	theme	component	354:362	arg1	C5-epimerization					327:342	C5-epimerization	327:342	C5-epimerization of the HS component, d-glucuronic acid (GlcA),	327:389	Of these, glucuronyl C5-epimerase (Glce) catalyzes C5-epimerization of the HS component, d-glucuronic acid (GlcA), into l-iduronic acid (IdoA), which provides internal flexibility to the polymer and forges protein-binding sites to ensure polymer function.
30872481	2	33	theme	l-iduronic	396:405	arg1	acid					407:410	l-iduronic acid	396:410	l-iduronic acid (IdoA)	396:417	Of these, glucuronyl C5-epimerase (Glce) catalyzes C5-epimerization of the HS component, d-glucuronic acid (GlcA), into l-iduronic acid (IdoA), which provides internal flexibility to the polymer and forges protein-binding sites to ensure polymer function.
30872481	2	33	theme	l-iduronic	396:405	arg1	IdoA					413:416	IdoA	413:416	IdoA	413:416	Of these, glucuronyl C5-epimerase (Glce) catalyzes C5-epimerization of the HS component, d-glucuronic acid (GlcA), into l-iduronic acid (IdoA), which provides internal flexibility to the polymer and forges protein-binding sites to ensure polymer function.
30872481	1	34	theme	enzymes	267:273	arg1	series					241:246	a series	239:246	a series of Golgi-localized enzymes	239:273	Heparan sulfate (HS) is a linear, complex polysaccharide that modulates the biological activities of proteins through binding sites made by a series of Golgi-localized enzymes.
30872481	7	35	theme	mandelate	1504:1512	arg1	racemase					1514:1521	mandelate racemase	1504:1521	mandelate racemase	1504:1521	The structure-based mechanism involves the two invariant acid/base residues, Glu499 and Tyr578, poised on each side of the target uronic acid residue, thus allowing reversible abstraction and readdition of a proton at the C5 position through a neutral enol intermediate, reminiscent of mandelate racemase.
30872481	1	36	theme	Heparan	99:105	arg1	polysaccharide					141:154	a linear, complex polysaccharide	123:154	a linear, complex polysaccharide that modulates the biological activities of proteins through binding sites made by a series of Golgi-localized enzymes	123:273	Heparan sulfate (HS) is a linear, complex polysaccharide that modulates the biological activities of proteins through binding sites made by a series of Golgi-localized enzymes.
30872481	1	36	theme	Heparan	99:105	arg1	HS					116:117	HS	116:117	HS	116:117	Heparan sulfate (HS) is a linear, complex polysaccharide that modulates the biological activities of proteins through binding sites made by a series of Golgi-localized enzymes.
30872481	1	36	theme	Heparan	99:105	arg1	sulfate					107:113	Heparan sulfate	99:113	Heparan sulfate (HS)	99:118	Heparan sulfate (HS) is a linear, complex polysaccharide that modulates the biological activities of proteins through binding sites made by a series of Golgi-localized enzymes.
30872481	1	37	theme	biological	175:184	arg1	activities					186:195	the biological activities	171:195	the biological activities of proteins	171:207	Heparan sulfate (HS) is a linear, complex polysaccharide that modulates the biological activities of proteins through binding sites made by a series of Golgi-localized enzymes.
30872481	5	38	theme	N-sulfate	974:982	arg1	groups					984:989	N-sulfate groups	974:989	N-sulfate groups vicinal to the epimerization site for substrate binding	974:1045	An extensive network of specific interactions illustrates the absolute requirement of N-sulfate groups vicinal to the epimerization site for substrate binding.
30872481	4	39	theme	sharp	815:819	arg1	kink					821:824	a sharp kink	813:824	a sharp kink within the central GlcNS-GlcA/IdoA-GlcNS trisaccharide motif	813:885	Deep infiltration of the oligosaccharides into the active site cleft imposes a sharp kink within the central GlcNS-GlcA/IdoA-GlcNS trisaccharide motif.
30872481	1	40	dep	linear	125:130	arg1	complex					133:139	complex	133:139	complex	133:139	Heparan sulfate (HS) is a linear, complex polysaccharide that modulates the biological activities of proteins through binding sites made by a series of Golgi-localized enzymes.
30872481	8	41	theme	HS	1706:1707	arg1	synthesis					1682:1690	the chemoenzymatic synthesis	1663:1690	the chemoenzymatic synthesis of heparin or HS analogs	1663:1715	These structures also shed light on a convergent mechanism of action between HS epimerases and lyases and provide molecular frameworks for the chemoenzymatic synthesis of heparin or HS analogs.
30872481	8	42	theme	heparin	1695:1701	arg1	synthesis					1682:1690	the chemoenzymatic synthesis	1663:1690	the chemoenzymatic synthesis of heparin or HS analogs	1663:1715	These structures also shed light on a convergent mechanism of action between HS epimerases and lyases and provide molecular frameworks for the chemoenzymatic synthesis of heparin or HS analogs.
30872481	8	43	theme	molecular	1638:1646	arg1	frameworks					1648:1657	molecular frameworks	1638:1657	molecular frameworks for the chemoenzymatic synthesis of heparin or HS analogs	1638:1715	These structures also shed light on a convergent mechanism of action between HS epimerases and lyases and provide molecular frameworks for the chemoenzymatic synthesis of heparin or HS analogs.
30872481	5	44	theme	epimerization	1006:1018	arg1	site					1020:1023	the epimerization site	1002:1023	the epimerization site for substrate binding	1002:1045	An extensive network of specific interactions illustrates the absolute requirement of N-sulfate groups vicinal to the epimerization site for substrate binding.
30872481	3	45	theme	crystal	547:553	arg1	structures					555:564	crystal structures	547:564	crystal structures of human Glce in the unbound state and of an inactive mutant	547:625	Here we report crystal structures of human Glce in the unbound state and of an inactive mutant, as assessed by real-time NMR spectroscopy, bound with a (GlcA-GlcNS)n substrate or a (IdoA-GlcNS)n product.
30872481	3	46	from	structures	555:564	arg1	state					595:599	the unbound state	583:599	the unbound state	583:599	Here we report crystal structures of human Glce in the unbound state and of an inactive mutant, as assessed by real-time NMR spectroscopy, bound with a (GlcA-GlcNS)n substrate or a (IdoA-GlcNS)n product.
30872481	0	47	theme	catalytic	27:35	arg1	mechanism					37:45	catalytic mechanism	27:45	catalytic mechanism of human heparan sulfate d-glucuronyl C5 epimerase	27:96	Substrate binding mode and catalytic mechanism of human heparan sulfate d-glucuronyl C5 epimerase.
30872481	3	48	theme	n	696:696	arg1	substrate					698:706	a (GlcA-GlcNS)n substrate	682:706	a (GlcA-GlcNS)n substrate	682:706	Here we report crystal structures of human Glce in the unbound state and of an inactive mutant, as assessed by real-time NMR spectroscopy, bound with a (GlcA-GlcNS)n substrate or a (IdoA-GlcNS)n product.
30872481	2	49	theme	protein-binding	482:496	arg1	sites					498:502	protein-binding sites	482:502	protein-binding sites	482:502	Of these, glucuronyl C5-epimerase (Glce) catalyzes C5-epimerization of the HS component, d-glucuronic acid (GlcA), into l-iduronic acid (IdoA), which provides internal flexibility to the polymer and forges protein-binding sites to ensure polymer function.
30872481	7	50	theme	enol	1470:1473	arg1	intermediate					1475:1486	a neutral enol intermediate	1460:1486	a neutral enol intermediate	1460:1486	The structure-based mechanism involves the two invariant acid/base residues, Glu499 and Tyr578, poised on each side of the target uronic acid residue, thus allowing reversible abstraction and readdition of a proton at the C5 position through a neutral enol intermediate, reminiscent of mandelate racemase.
30872481	7	50	theme	enol	1470:1473	arg1	reminiscent					1489:1499	reminiscent	1489:1499	reminiscent of mandelate racemase	1489:1521	The structure-based mechanism involves the two invariant acid/base residues, Glu499 and Tyr578, poised on each side of the target uronic acid residue, thus allowing reversible abstraction and readdition of a proton at the C5 position through a neutral enol intermediate, reminiscent of mandelate racemase.
30872481	5	51	theme	absolute	950:957	arg1	requirement					959:969	the absolute requirement	946:969	the absolute requirement of N-sulfate groups vicinal to the epimerization site for substrate binding	946:1045	An extensive network of specific interactions illustrates the absolute requirement of N-sulfate groups vicinal to the epimerization site for substrate binding.
30872481	1	52	theme	proteins	200:207	arg1	activities					186:195	the biological activities	171:195	the biological activities of proteins	171:207	Heparan sulfate (HS) is a linear, complex polysaccharide that modulates the biological activities of proteins through binding sites made by a series of Golgi-localized enzymes.
30872481	0	53	theme	human	50:54	arg1	sulfate					64:70	human heparan sulfate	50:70	human heparan sulfate d-glucuronyl C5 epimerase	50:96	Substrate binding mode and catalytic mechanism of human heparan sulfate d-glucuronyl C5 epimerase.
30872481	3	54	theme	unbound	587:593	arg1	state					595:599	the unbound state	583:599	the unbound state	583:599	Here we report crystal structures of human Glce in the unbound state and of an inactive mutant, as assessed by real-time NMR spectroscopy, bound with a (GlcA-GlcNS)n substrate or a (IdoA-GlcNS)n product.
30872481	7	55	theme	structure-based	1222:1236	arg1	mechanism					1238:1246	The structure-based mechanism	1218:1246	The structure-based mechanism	1218:1246	The structure-based mechanism involves the two invariant acid/base residues, Glu499 and Tyr578, poised on each side of the target uronic acid residue, thus allowing reversible abstraction and readdition of a proton at the C5 position through a neutral enol intermediate, reminiscent of mandelate racemase.
30872481	3	56	theme	GlcA-GlcNS	685:694	arg1	substrate					698:706	a (GlcA-GlcNS)n substrate	682:706	a (GlcA-GlcNS)n substrate	682:706	Here we report crystal structures of human Glce in the unbound state and of an inactive mutant, as assessed by real-time NMR spectroscopy, bound with a (GlcA-GlcNS)n substrate or a (IdoA-GlcNS)n product.
30872481	4	57	theme	site	794:797	arg1	cleft					799:803	the active site cleft	783:803	the active site cleft	783:803	Deep infiltration of the oligosaccharides into the active site cleft imposes a sharp kink within the central GlcNS-GlcA/IdoA-GlcNS trisaccharide motif.
30872481	3	58	theme	inactive	611:618	arg1	mutant					620:625	an inactive mutant	608:625	an inactive mutant	608:625	Here we report crystal structures of human Glce in the unbound state and of an inactive mutant, as assessed by real-time NMR spectroscopy, bound with a (GlcA-GlcNS)n substrate or a (IdoA-GlcNS)n product.
30872481	5	59	theme	groups	984:989	arg1	requirement					959:969	the absolute requirement	946:969	the absolute requirement of N-sulfate groups vicinal to the epimerization site for substrate binding	946:1045	An extensive network of specific interactions illustrates the absolute requirement of N-sulfate groups vicinal to the epimerization site for substrate binding.
30872481	3	60	theme	mutant	620:625	arg1	structures					555:564	crystal structures	547:564	crystal structures of human Glce in the unbound state and of an inactive mutant	547:625	Here we report crystal structures of human Glce in the unbound state and of an inactive mutant, as assessed by real-time NMR spectroscopy, bound with a (GlcA-GlcNS)n substrate or a (IdoA-GlcNS)n product.
30872481	3	61	theme	Glce	575:578	arg1	structures					555:564	crystal structures	547:564	crystal structures of human Glce in the unbound state and of an inactive mutant	547:625	Here we report crystal structures of human Glce in the unbound state and of an inactive mutant, as assessed by real-time NMR spectroscopy, bound with a (GlcA-GlcNS)n substrate or a (IdoA-GlcNS)n product.
30872481	6	62	theme	ring-puckering	1174:1187	arg1	signatures					1189:1198	ring-puckering signatures	1174:1198	ring-puckering signatures during catalysis	1174:1215	At the epimerization site, the GlcA/IdoA rings are highly constrained in two closely related boat conformations, highlighting ring-puckering signatures during catalysis.
30872481	6	63	theme	epimerization	1055:1067	arg1	site					1069:1072	the epimerization site	1051:1072	the epimerization site	1051:1072	At the epimerization site, the GlcA/IdoA rings are highly constrained in two closely related boat conformations, highlighting ring-puckering signatures during catalysis.
30872481	6	64	theme	GlcA/IdoA	1079:1087	arg1	rings					1089:1093	the GlcA/IdoA rings	1075:1093	the GlcA/IdoA rings	1075:1093	At the epimerization site, the GlcA/IdoA rings are highly constrained in two closely related boat conformations, highlighting ring-puckering signatures during catalysis.
30872481	2	65	theme	polymer	514:520	arg1	function					522:529	polymer function	514:529	polymer function	514:529	Of these, glucuronyl C5-epimerase (Glce) catalyzes C5-epimerization of the HS component, d-glucuronic acid (GlcA), into l-iduronic acid (IdoA), which provides internal flexibility to the polymer and forges protein-binding sites to ensure polymer function.
30872481	5	66	theme	vicinal	991:997	arg1	groups					984:989	N-sulfate groups	974:989	N-sulfate groups vicinal to the epimerization site for substrate binding	974:1045	An extensive network of specific interactions illustrates the absolute requirement of N-sulfate groups vicinal to the epimerization site for substrate binding.
30872481	5	67	theme	specific	912:919	arg1	interactions					921:932	specific interactions	912:932	specific interactions	912:932	An extensive network of specific interactions illustrates the absolute requirement of N-sulfate groups vicinal to the epimerization site for substrate binding.
30872481	1	68	theme	binding	217:223	arg1	sites					225:229	binding sites	217:229	binding sites made by a series of Golgi-localized enzymes	217:273	Heparan sulfate (HS) is a linear, complex polysaccharide that modulates the biological activities of proteins through binding sites made by a series of Golgi-localized enzymes.
30872481	0	69	theme	sulfate	64:70	arg1	epimerase					88:96	human heparan sulfate d-glucuronyl C5 epimerase	50:96	human heparan sulfate d-glucuronyl C5 epimerase	50:96	Substrate binding mode and catalytic mechanism of human heparan sulfate d-glucuronyl C5 epimerase.
30872481	7	70	theme	invariant	1265:1273	arg1	Glu499					1295:1300	Glu499	1295:1300	Glu499	1295:1300	The structure-based mechanism involves the two invariant acid/base residues, Glu499 and Tyr578, poised on each side of the target uronic acid residue, thus allowing reversible abstraction and readdition of a proton at the C5 position through a neutral enol intermediate, reminiscent of mandelate racemase.
30872481	7	70	theme	invariant	1265:1273	arg1	residues					1285:1292	the two invariant acid/base residues	1257:1292	the two invariant acid/base residues	1257:1292	The structure-based mechanism involves the two invariant acid/base residues, Glu499 and Tyr578, poised on each side of the target uronic acid residue, thus allowing reversible abstraction and readdition of a proton at the C5 position through a neutral enol intermediate, reminiscent of mandelate racemase.
30872481	7	70	theme	invariant	1265:1273	arg1	Tyr578					1306:1311	Tyr578	1306:1311	Tyr578	1306:1311	The structure-based mechanism involves the two invariant acid/base residues, Glu499 and Tyr578, poised on each side of the target uronic acid residue, thus allowing reversible abstraction and readdition of a proton at the C5 position through a neutral enol intermediate, reminiscent of mandelate racemase.
30872481	5	71	theme	interactions	921:932	arg1	network					901:907	An extensive network	888:907	An extensive network of specific interactions	888:932	An extensive network of specific interactions illustrates the absolute requirement of N-sulfate groups vicinal to the epimerization site for substrate binding.
30872481	7	72	theme	acid/base	1275:1283	arg1	Glu499					1295:1300	Glu499	1295:1300	Glu499	1295:1300	The structure-based mechanism involves the two invariant acid/base residues, Glu499 and Tyr578, poised on each side of the target uronic acid residue, thus allowing reversible abstraction and readdition of a proton at the C5 position through a neutral enol intermediate, reminiscent of mandelate racemase.
30872481	7	72	theme	acid/base	1275:1283	arg1	residues					1285:1292	the two invariant acid/base residues	1257:1292	the two invariant acid/base residues	1257:1292	The structure-based mechanism involves the two invariant acid/base residues, Glu499 and Tyr578, poised on each side of the target uronic acid residue, thus allowing reversible abstraction and readdition of a proton at the C5 position through a neutral enol intermediate, reminiscent of mandelate racemase.
30872481	7	72	theme	acid/base	1275:1283	arg1	Tyr578					1306:1311	Tyr578	1306:1311	Tyr578	1306:1311	The structure-based mechanism involves the two invariant acid/base residues, Glu499 and Tyr578, poised on each side of the target uronic acid residue, thus allowing reversible abstraction and readdition of a proton at the C5 position through a neutral enol intermediate, reminiscent of mandelate racemase.
30872481	2	73	theme	HS	351:352	arg1	component					354:362	the HS component	347:362	the HS component	347:362	Of these, glucuronyl C5-epimerase (Glce) catalyzes C5-epimerization of the HS component, d-glucuronic acid (GlcA), into l-iduronic acid (IdoA), which provides internal flexibility to the polymer and forges protein-binding sites to ensure polymer function.
30872481	2	73	theme	HS	351:352	arg1	acid					378:381	d-glucuronic acid	365:381	d-glucuronic acid (GlcA)	365:388	Of these, glucuronyl C5-epimerase (Glce) catalyzes C5-epimerization of the HS component, d-glucuronic acid (GlcA), into l-iduronic acid (IdoA), which provides internal flexibility to the polymer and forges protein-binding sites to ensure polymer function.
30872481	8	74	theme	HS	1601:1602	arg1	epimerases					1604:1613	HS epimerases	1601:1613	HS epimerases	1601:1613	These structures also shed light on a convergent mechanism of action between HS epimerases and lyases and provide molecular frameworks for the chemoenzymatic synthesis of heparin or HS analogs.
30872481	8	75	theme	convergent	1562:1571	arg1	mechanism					1573:1581	a convergent mechanism	1560:1581	a convergent mechanism of action between HS epimerases and lyases	1560:1624	These structures also shed light on a convergent mechanism of action between HS epimerases and lyases and provide molecular frameworks for the chemoenzymatic synthesis of heparin or HS analogs.
30872481	0	76	theme	heparan	56:62	arg1	sulfate					64:70	human heparan sulfate	50:70	human heparan sulfate d-glucuronyl C5 epimerase	50:96	Substrate binding mode and catalytic mechanism of human heparan sulfate d-glucuronyl C5 epimerase.
30872481	3	77	theme	human	569:573	arg1	Glce					575:578	human Glce	569:578	human Glce	569:578	Here we report crystal structures of human Glce in the unbound state and of an inactive mutant, as assessed by real-time NMR spectroscopy, bound with a (GlcA-GlcNS)n substrate or a (IdoA-GlcNS)n product.
30872481	7	78	theme	neutral	1462:1468	arg1	intermediate					1475:1486	a neutral enol intermediate	1460:1486	a neutral enol intermediate	1460:1486	The structure-based mechanism involves the two invariant acid/base residues, Glu499 and Tyr578, poised on each side of the target uronic acid residue, thus allowing reversible abstraction and readdition of a proton at the C5 position through a neutral enol intermediate, reminiscent of mandelate racemase.
30872481	7	78	theme	neutral	1462:1468	arg1	reminiscent					1489:1499	reminiscent	1489:1499	reminiscent of mandelate racemase	1489:1521	The structure-based mechanism involves the two invariant acid/base residues, Glu499 and Tyr578, poised on each side of the target uronic acid residue, thus allowing reversible abstraction and readdition of a proton at the C5 position through a neutral enol intermediate, reminiscent of mandelate racemase.
30872481	1	79	theme	linear	125:130	arg1	polysaccharide					141:154	a linear, complex polysaccharide	123:154	a linear, complex polysaccharide that modulates the biological activities of proteins through binding sites made by a series of Golgi-localized enzymes	123:273	Heparan sulfate (HS) is a linear, complex polysaccharide that modulates the biological activities of proteins through binding sites made by a series of Golgi-localized enzymes.
30872481	1	79	theme	linear	125:130	arg1	sulfate					107:113	Heparan sulfate	99:113	Heparan sulfate (HS)	99:118	Heparan sulfate (HS) is a linear, complex polysaccharide that modulates the biological activities of proteins through binding sites made by a series of Golgi-localized enzymes.
30872481	4	80	theme	central	837:843	arg1	motif					881:885	the central GlcNS-GlcA/IdoA-GlcNS trisaccharide motif	833:885	the central GlcNS-GlcA/IdoA-GlcNS trisaccharide motif	833:885	Deep infiltration of the oligosaccharides into the active site cleft imposes a sharp kink within the central GlcNS-GlcA/IdoA-GlcNS trisaccharide motif.
17310251	7	0	from	regulation	954:963	arg1	response					1016:1023	the immune response	1005:1023	the immune response	1005:1023	This allosteric mechanism is crucial for tight regulation of the complement-amplification step in the immune response.
17310251	7	1	from	response	1016:1023	arg1	regulation					954:963	tight regulation	948:963	tight regulation of the complement-amplification step in the immune response	948:1023	This allosteric mechanism is crucial for tight regulation of the complement-amplification step in the immune response.
17310251	0	2	theme	protease	68:75	arg1	activation					42:51	activation	42:51	activation of the central protease of the complement system	42:100	Factor B structure provides insights into activation of the central protease of the complement system.
17310251	6	3	theme	VWA	864:866	arg1	domain					868:873	the VWA domain	860:873	the VWA domain	860:873	Reshuffling of the helices releases the scissile bond for final proteolytic activation and generates a new interface between the VWA domain and the serine protease domain.
17310251	7	4	theme	allosteric	912:921	arg1	mechanism					923:931	This allosteric mechanism	907:931	This allosteric mechanism	907:931	This allosteric mechanism is crucial for tight regulation of the complement-amplification step in the immune response.
17310251	3	5	theme	preceding	437:445	arg1	linker					454:459	the preceding domain linker	433:459	the preceding domain linker	433:459	The canonical activation helix of the Von Willebrand factor A (VWA) domain is displaced by a helix from the preceding domain linker.
17310251	0	6	theme	complement	84:93	arg1	system					95:100	the complement system	80:100	the complement system	80:100	Factor B structure provides insights into activation of the central protease of the complement system.
17310251	4	7	theme	C3b	609:611	arg1	binding					587:593	binding	587:593	binding of the ligand C3b	587:611	The two helices conformationally link the scissile-activation peptide and the metal ion-dependent adhesion site required for binding of the ligand C3b.
17310251	4	8	theme	metal	540:544	arg1	site					569:572	the metal ion-dependent adhesion site	536:572	the metal ion-dependent adhesion site required for binding of the ligand C3b	536:611	The two helices conformationally link the scissile-activation peptide and the metal ion-dependent adhesion site required for binding of the ligand C3b.
17310251	5	9	theme	control	679:685	arg1	domains					687:693	the three N-terminal control domains	658:693	the three N-terminal control domains	658:693	The data suggest that C3b binding displaces the three N-terminal control domains and reshuffles the two central helices.
17310251	6	10	theme	helices	754:760	arg1	Reshuffling					735:745	Reshuffling	735:745	Reshuffling of the helices	735:760	Reshuffling of the helices releases the scissile bond for final proteolytic activation and generates a new interface between the VWA domain and the serine protease domain.
17310251	2	11	theme	2.3-A	240:244	arg1	resolution					246:255	2.3-A resolution	240:255	2.3-A resolution	240:255	Here, we present the crystal structure of human factor B at 2.3-A resolution, which reveals how the five-domain proenzyme is kept securely inactive.
17310251	3	12	from	linker	454:459	arg1	helix					422:426	a helix	420:426	a helix from the preceding domain linker	420:459	The canonical activation helix of the Von Willebrand factor A (VWA) domain is displaced by a helix from the preceding domain linker.
17310251	1	13	theme	complement	143:152	arg1	system					154:159	the complement system	139:159	the complement system of immune defense	139:177	Factor B is the central protease of the complement system of immune defense.
17310251	0	14	theme	system	95:100	arg1	protease					68:75	the central protease	56:75	the central protease of the complement system	56:100	Factor B structure provides insights into activation of the central protease of the complement system.
17310251	6	15	theme	new	838:840	arg1	interface					842:850	a new interface	836:850	a new interface between the VWA domain and the serine protease domain	836:904	Reshuffling of the helices releases the scissile bond for final proteolytic activation and generates a new interface between the VWA domain and the serine protease domain.
17310251	2	16	theme	B	235:235	arg1	structure					209:217	the crystal structure	197:217	the crystal structure of human factor B at 2.3-A resolution, which reveals how the five-domain proenzyme is kept securely inactive	197:326	Here, we present the crystal structure of human factor B at 2.3-A resolution, which reveals how the five-domain proenzyme is kept securely inactive.
17310251	1	17	theme	system	154:159	arg1	protease					127:134	the central protease	115:134	the central protease of the complement system of immune defense	115:177	Factor B is the central protease of the complement system of immune defense.
17310251	1	17	theme	system	154:159	arg1	B					110:110	Factor B	103:110	Factor B	103:110	Factor B is the central protease of the complement system of immune defense.
17310251	3	18	theme	activation	343:352	arg1	helix					354:358	The canonical activation helix	329:358	The canonical activation helix of the Von Willebrand factor A (VWA) domain	329:402	The canonical activation helix of the Von Willebrand factor A (VWA) domain is displaced by a helix from the preceding domain linker.
17310251	5	19	theme	central	718:724	arg1	helices					726:732	the two central helices	710:732	the two central helices	710:732	The data suggest that C3b binding displaces the three N-terminal control domains and reshuffles the two central helices.
17310251	4	20	theme	ligand	602:607	arg1	C3b					609:611	the ligand C3b	598:611	the ligand C3b	598:611	The two helices conformationally link the scissile-activation peptide and the metal ion-dependent adhesion site required for binding of the ligand C3b.
17310251	3	21	theme	factor	382:387	arg1	domain					397:402	the Von Willebrand factor A (VWA) domain	363:402	the Von Willebrand factor A (VWA) domain	363:402	The canonical activation helix of the Von Willebrand factor A (VWA) domain is displaced by a helix from the preceding domain linker.
17310251	0	22	theme	Factor	0:5	arg1	structure					9:17	Factor B structure	0:17	Factor B structure	0:17	Factor B structure provides insights into activation of the central protease of the complement system.
17310251	1	23	theme	immune	164:169	arg1	defense					171:177	immune defense	164:177	immune defense	164:177	Factor B is the central protease of the complement system of immune defense.
17310251	1	24	theme	defense	171:177	arg1	system					154:159	the complement system	139:159	the complement system of immune defense	139:177	Factor B is the central protease of the complement system of immune defense.
17310251	3	25	theme	canonical	333:341	arg1	helix					354:358	The canonical activation helix	329:358	The canonical activation helix of the Von Willebrand factor A (VWA) domain	329:402	The canonical activation helix of the Von Willebrand factor A (VWA) domain is displaced by a helix from the preceding domain linker.
17310251	4	26	theme	scissile-activation	504:522	arg1	peptide					524:530	the scissile-activation peptide	500:530	the scissile-activation peptide	500:530	The two helices conformationally link the scissile-activation peptide and the metal ion-dependent adhesion site required for binding of the ligand C3b.
17310251	1	27	theme	central	119:125	arg1	protease					127:134	the central protease	115:134	the central protease of the complement system of immune defense	115:177	Factor B is the central protease of the complement system of immune defense.
17310251	1	27	theme	central	119:125	arg1	B					110:110	Factor B	103:110	Factor B	103:110	Factor B is the central protease of the complement system of immune defense.
17310251	3	28	theme	Von	367:369	arg1	factor					382:387	Von Willebrand factor	367:387	the Von Willebrand factor A (VWA) domain	363:402	The canonical activation helix of the Von Willebrand factor A (VWA) domain is displaced by a helix from the preceding domain linker.
17310251	2	29	theme	crystal	201:207	arg1	structure					209:217	the crystal structure	197:217	the crystal structure of human factor B at 2.3-A resolution, which reveals how the five-domain proenzyme is kept securely inactive	197:326	Here, we present the crystal structure of human factor B at 2.3-A resolution, which reveals how the five-domain proenzyme is kept securely inactive.
17310251	3	30	theme	A	389:389	arg1	domain					397:402	the Von Willebrand factor A (VWA) domain	363:402	the Von Willebrand factor A (VWA) domain	363:402	The canonical activation helix of the Von Willebrand factor A (VWA) domain is displaced by a helix from the preceding domain linker.
17310251	3	31	theme	Willebrand	371:380	arg1	factor					382:387	Von Willebrand factor	367:387	the Von Willebrand factor A (VWA) domain	363:402	The canonical activation helix of the Von Willebrand factor A (VWA) domain is displaced by a helix from the preceding domain linker.
17310251	3	32	theme	domain	397:402	arg1	helix					354:358	The canonical activation helix	329:358	The canonical activation helix of the Von Willebrand factor A (VWA) domain	329:402	The canonical activation helix of the Von Willebrand factor A (VWA) domain is displaced by a helix from the preceding domain linker.
17310251	5	33	theme	N-terminal	668:677	arg1	domains					687:693	the three N-terminal control domains	658:693	the three N-terminal control domains	658:693	The data suggest that C3b binding displaces the three N-terminal control domains and reshuffles the two central helices.
17310251	6	34	theme	proteolytic	799:809	arg1	activation					811:820	final proteolytic activation	793:820	final proteolytic activation	793:820	Reshuffling of the helices releases the scissile bond for final proteolytic activation and generates a new interface between the VWA domain and the serine protease domain.
17310251	7	35	theme	complement-amplification	972:995	arg1	step					997:1000	the complement-amplification step	968:1000	the complement-amplification step in the immune response	968:1023	This allosteric mechanism is crucial for tight regulation of the complement-amplification step in the immune response.
17310251	1	36	theme	Factor	103:108	arg1	protease					127:134	the central protease	115:134	the central protease of the complement system of immune defense	115:177	Factor B is the central protease of the complement system of immune defense.
17310251	1	36	theme	Factor	103:108	arg1	B					110:110	Factor B	103:110	Factor B	103:110	Factor B is the central protease of the complement system of immune defense.
17310251	6	37	theme	serine	883:888	arg1	domain					899:904	the serine protease domain	879:904	the serine protease domain	879:904	Reshuffling of the helices releases the scissile bond for final proteolytic activation and generates a new interface between the VWA domain and the serine protease domain.
17310251	7	38	theme	immune	1009:1014	arg1	response					1016:1023	the immune response	1005:1023	the immune response	1005:1023	This allosteric mechanism is crucial for tight regulation of the complement-amplification step in the immune response.
17310251	6	39	theme	final	793:797	arg1	activation					811:820	final proteolytic activation	793:820	final proteolytic activation	793:820	Reshuffling of the helices releases the scissile bond for final proteolytic activation and generates a new interface between the VWA domain and the serine protease domain.
17310251	7	40	theme	step	997:1000	arg1	regulation					954:963	tight regulation	948:963	tight regulation of the complement-amplification step in the immune response	948:1023	This allosteric mechanism is crucial for tight regulation of the complement-amplification step in the immune response.
17310251	2	41	theme	factor	228:233	arg1	B					235:235	human factor B	222:235	human factor B	222:235	Here, we present the crystal structure of human factor B at 2.3-A resolution, which reveals how the five-domain proenzyme is kept securely inactive.
17310251	2	42	theme	five-domain	280:290	arg1	proenzyme					292:300	the five-domain proenzyme	276:300	the five-domain proenzyme	276:300	Here, we present the crystal structure of human factor B at 2.3-A resolution, which reveals how the five-domain proenzyme is kept securely inactive.
17310251	2	42	theme	five-domain	280:290	arg1	inactive					319:326	inactive	319:326	inactive	319:326	Here, we present the crystal structure of human factor B at 2.3-A resolution, which reveals how the five-domain proenzyme is kept securely inactive.
17310251	7	43	from	step	997:1000	arg1	response					1016:1023	the immune response	1005:1023	the immune response	1005:1023	This allosteric mechanism is crucial for tight regulation of the complement-amplification step in the immune response.
17310251	4	44	theme	adhesion	560:567	arg1	site					569:572	the metal ion-dependent adhesion site	536:572	the metal ion-dependent adhesion site required for binding of the ligand C3b	536:611	The two helices conformationally link the scissile-activation peptide and the metal ion-dependent adhesion site required for binding of the ligand C3b.
17310251	5	45	theme	C3b	636:638	arg1	binding					640:646	C3b binding	636:646	C3b binding	636:646	The data suggest that C3b binding displaces the three N-terminal control domains and reshuffles the two central helices.
17310251	2	46	theme	human	222:226	arg1	B					235:235	human factor B	222:235	human factor B	222:235	Here, we present the crystal structure of human factor B at 2.3-A resolution, which reveals how the five-domain proenzyme is kept securely inactive.
17310251	2	47	from	resolution	246:255	arg1	structure					209:217	the crystal structure	197:217	the crystal structure of human factor B at 2.3-A resolution, which reveals how the five-domain proenzyme is kept securely inactive	197:326	Here, we present the crystal structure of human factor B at 2.3-A resolution, which reveals how the five-domain proenzyme is kept securely inactive.
17310251	4	48	theme	ion-dependent	546:558	arg1	site					569:572	the metal ion-dependent adhesion site	536:572	the metal ion-dependent adhesion site required for binding of the ligand C3b	536:611	The two helices conformationally link the scissile-activation peptide and the metal ion-dependent adhesion site required for binding of the ligand C3b.
17310251	0	49	theme	central	60:66	arg1	protease					68:75	the central protease	56:75	the central protease of the complement system	56:100	Factor B structure provides insights into activation of the central protease of the complement system.
17310251	6	50	theme	scissile	775:782	arg1	bond					784:787	the scissile bond	771:787	the scissile bond for final proteolytic activation	771:820	Reshuffling of the helices releases the scissile bond for final proteolytic activation and generates a new interface between the VWA domain and the serine protease domain.
17310251	7	51	theme	tight	948:952	arg1	regulation					954:963	tight regulation	948:963	tight regulation of the complement-amplification step in the immune response	948:1023	This allosteric mechanism is crucial for tight regulation of the complement-amplification step in the immune response.
17310251	3	52	theme	domain	447:452	arg1	linker					454:459	the preceding domain linker	433:459	the preceding domain linker	433:459	The canonical activation helix of the Von Willebrand factor A (VWA) domain is displaced by a helix from the preceding domain linker.
17310251	3	53	theme	VWA	392:394	arg1	domain					397:402	the Von Willebrand factor A (VWA) domain	363:402	the Von Willebrand factor A (VWA) domain	363:402	The canonical activation helix of the Von Willebrand factor A (VWA) domain is displaced by a helix from the preceding domain linker.
17310251	0	54	theme	B	7:7	arg1	structure					9:17	Factor B structure	0:17	Factor B structure	0:17	Factor B structure provides insights into activation of the central protease of the complement system.
17310251	6	55	theme	protease	890:897	arg1	domain					899:904	the serine protease domain	879:904	the serine protease domain	879:904	Reshuffling of the helices releases the scissile bond for final proteolytic activation and generates a new interface between the VWA domain and the serine protease domain.
19574954	0	0	theme	factor	76:81	arg1	complex					104:110	the factor B-cobra venom factor complex	72:110	the factor B-cobra venom factor complex	72:110	Insights into complement convertase formation based on the structure of the factor B-cobra venom factor complex.
19574954	7	1	theme	complement	1321:1330	arg1	therapeutics					1332:1343	complement therapeutics	1321:1343	complement therapeutics	1321:1343	These insights into formation of convertases provide a basis for further development of complement therapeutics.
19574954	3	2	attach	present	447:453	arg2	we					444:445	we	444:445	we	444:445	Here, we present the crystal structure at 2.2-A resolution, small-angle X-ray scattering and electron microscopy (EM) data of the pro-convertase formed by human FB and cobra venom factor (CVF), a potent homologue of C3b that generates more stable convertases.
19574954	3	2	attach	present	447:453	arg1	resolution					486:495	2.2-A resolution	480:495	2.2-A resolution	480:495	Here, we present the crystal structure at 2.2-A resolution, small-angle X-ray scattering and electron microscopy (EM) data of the pro-convertase formed by human FB and cobra venom factor (CVF), a potent homologue of C3b that generates more stable convertases.
19574954	1	3	theme	altered	237:243	arg1	cells					250:254	altered host cells	237:254	altered host cells	237:254	Immune protection by the complement system critically depends on assembly of C3 convertases on the surface of pathogens and altered host cells.
19574954	4	4	theme	native	839:844	arg1	C3					846:847	the native C3	835:847	the native C3	835:847	FB is loaded onto CVF through its pro-peptide Ba segment by specific contacts, which explain the specificity for the homologous C3b over the native C3 and inactive products iC3b and C3c.
19574954	2	5	theme	alternative	344:354	arg1	pathway					356:362	the alternative pathway	340:362	the alternative pathway	340:362	These short-lived protease complexes are formed through pro-convertases, which for the alternative pathway consist of the complement component C3b and the pro-enzyme factor B (FB).
19574954	5	6	theme	domain	1025:1030	arg1	domain					1025:1030	the Von Willebrand factor A-type domain	992:1030	the Von Willebrand factor A-type domain	992:1030	The protease segment Bb binds the carboxy terminus of CVF through the metal-ion dependent adhesion site of the Von Willebrand factor A-type domain.
19574954	5	6	theme	domain	1025:1030	arg1	site					984:987	the metal-ion dependent adhesion site	951:987	the metal-ion dependent adhesion site of the Von Willebrand factor A-type domain	951:1030	The protease segment Bb binds the carboxy terminus of CVF through the metal-ion dependent adhesion site of the Von Willebrand factor A-type domain.
19574954	1	7	theme	host	245:248	arg1	cells					250:254	altered host cells	237:254	altered host cells	237:254	Immune protection by the complement system critically depends on assembly of C3 convertases on the surface of pathogens and altered host cells.
19574954	0	8	theme	venom	91:95	arg1	complex					104:110	the factor B-cobra venom factor complex	72:110	the factor B-cobra venom factor complex	72:110	Insights into complement convertase formation based on the structure of the factor B-cobra venom factor complex.
19574954	6	9	theme	crystal	1177:1183	arg1	structure					1185:1193	the crystal structure	1173:1193	the crystal structure of CVFB	1173:1201	A possible dynamic equilibrium between a 'loading' and 'activation' state of the pro-convertase may explain the observed difference between the crystal structure of CVFB and the EM structure of C3bB.
19574954	5	10	theme	CVF	939:941	arg1	terminus					927:934	the carboxy terminus	915:934	the carboxy terminus of CVF	915:941	The protease segment Bb binds the carboxy terminus of CVF through the metal-ion dependent adhesion site of the Von Willebrand factor A-type domain.
19574954	3	11	theme	scattering	516:525	arg1	data					556:559	small-angle X-ray scattering and electron microscopy (EM) data	498:559	small-angle X-ray scattering and electron microscopy (EM) data of the pro-convertase formed by human FB and cobra venom factor (CVF), a potent homologue of C3b that generates more stable convertases	498:695	Here, we present the crystal structure at 2.2-A resolution, small-angle X-ray scattering and electron microscopy (EM) data of the pro-convertase formed by human FB and cobra venom factor (CVF), a potent homologue of C3b that generates more stable convertases.
19574954	3	12	theme	microscopy	540:549	arg1	data					556:559	small-angle X-ray scattering and electron microscopy (EM) data	498:559	small-angle X-ray scattering and electron microscopy (EM) data of the pro-convertase formed by human FB and cobra venom factor (CVF), a potent homologue of C3b that generates more stable convertases	498:695	Here, we present the crystal structure at 2.2-A resolution, small-angle X-ray scattering and electron microscopy (EM) data of the pro-convertase formed by human FB and cobra venom factor (CVF), a potent homologue of C3b that generates more stable convertases.
19574954	1	13	theme	cells	250:254	arg1	surface					212:218	the surface	208:218	the surface of pathogens and altered host cells	208:254	Immune protection by the complement system critically depends on assembly of C3 convertases on the surface of pathogens and altered host cells.
19574954	0	14	theme	B-cobra	83:89	arg1	complex					104:110	the factor B-cobra venom factor complex	72:110	the factor B-cobra venom factor complex	72:110	Insights into complement convertase formation based on the structure of the factor B-cobra venom factor complex.
19574954	5	15	theme	Willebrand	1000:1009	arg1	factor					1011:1016	Von Willebrand factor	996:1016	the Von Willebrand factor A-type domain	992:1030	The protease segment Bb binds the carboxy terminus of CVF through the metal-ion dependent adhesion site of the Von Willebrand factor A-type domain.
19574954	2	16	theme	protease	275:282	arg1	complexes					284:292	These short-lived protease complexes	257:292	These short-lived protease complexes	257:292	These short-lived protease complexes are formed through pro-convertases, which for the alternative pathway consist of the complement component C3b and the pro-enzyme factor B (FB).
19574954	0	17	theme	complex	104:110	arg1	structure					59:67	the structure	55:67	the structure of the factor B-cobra venom factor complex	55:110	Insights into complement convertase formation based on the structure of the factor B-cobra venom factor complex.
19574954	5	18	theme	factor	1011:1016	arg1	domain					1025:1030	the Von Willebrand factor A-type domain	992:1030	the Von Willebrand factor A-type domain	992:1030	The protease segment Bb binds the carboxy terminus of CVF through the metal-ion dependent adhesion site of the Von Willebrand factor A-type domain.
19574954	2	19	theme	pro-enzyme	412:421	arg1	FB					433:434	FB	433:434	FB	433:434	These short-lived protease complexes are formed through pro-convertases, which for the alternative pathway consist of the complement component C3b and the pro-enzyme factor B (FB).
19574954	2	19	theme	pro-enzyme	412:421	arg1	B					430:430	the pro-enzyme factor B	408:430	the pro-enzyme factor B (FB)	408:435	These short-lived protease complexes are formed through pro-convertases, which for the alternative pathway consist of the complement component C3b and the pro-enzyme factor B (FB).
19574954	2	20	theme	short-lived	263:273	arg1	complexes					284:292	These short-lived protease complexes	257:292	These short-lived protease complexes	257:292	These short-lived protease complexes are formed through pro-convertases, which for the alternative pathway consist of the complement component C3b and the pro-enzyme factor B (FB).
19574954	6	21	theme	possible	1035:1042	arg1	equilibrium					1052:1062	A possible dynamic equilibrium	1033:1062	A possible dynamic equilibrium between a 'loading' and 'activation' state of the pro-convertase	1033:1127	A possible dynamic equilibrium between a 'loading' and 'activation' state of the pro-convertase may explain the observed difference between the crystal structure of CVFB and the EM structure of C3bB.
19574954	0	22	theme	factor	97:102	arg1	complex					104:110	the factor B-cobra venom factor complex	72:110	the factor B-cobra venom factor complex	72:110	Insights into complement convertase formation based on the structure of the factor B-cobra venom factor complex.
19574954	5	23	theme	A-type	1018:1023	arg1	domain					1025:1030	the Von Willebrand factor A-type domain	992:1030	the Von Willebrand factor A-type domain	992:1030	The protease segment Bb binds the carboxy terminus of CVF through the metal-ion dependent adhesion site of the Von Willebrand factor A-type domain.
19574954	3	24	theme	X-ray	510:514	arg1	scattering					516:525	small-angle X-ray scattering	498:525	small-angle X-ray scattering	498:525	Here, we present the crystal structure at 2.2-A resolution, small-angle X-ray scattering and electron microscopy (EM) data of the pro-convertase formed by human FB and cobra venom factor (CVF), a potent homologue of C3b that generates more stable convertases.
19574954	5	25	theme	protease	889:896	arg1	Bb					906:907	The protease segment Bb	885:907	The protease segment Bb	885:907	The protease segment Bb binds the carboxy terminus of CVF through the metal-ion dependent adhesion site of the Von Willebrand factor A-type domain.
19574954	2	26	theme	component	390:398	arg1	C3b					400:402	the complement component C3b	375:402	the complement component C3b	375:402	These short-lived protease complexes are formed through pro-convertases, which for the alternative pathway consist of the complement component C3b and the pro-enzyme factor B (FB).
19574954	3	27	theme	C3b	654:656	arg1	homologue					641:649	a potent homologue	632:649	a potent homologue of C3b that generates more stable convertases	632:695	Here, we present the crystal structure at 2.2-A resolution, small-angle X-ray scattering and electron microscopy (EM) data of the pro-convertase formed by human FB and cobra venom factor (CVF), a potent homologue of C3b that generates more stable convertases.
19574954	3	27	theme	C3b	654:656	arg1	factor					618:623	cobra venom factor	606:623	cobra venom factor (CVF)	606:629	Here, we present the crystal structure at 2.2-A resolution, small-angle X-ray scattering and electron microscopy (EM) data of the pro-convertase formed by human FB and cobra venom factor (CVF), a potent homologue of C3b that generates more stable convertases.
19574954	6	28	theme	observed	1145:1152	arg1	difference					1154:1163	the observed difference	1141:1163	the observed difference between the crystal structure of CVFB and the EM structure of C3bB	1141:1230	A possible dynamic equilibrium between a 'loading' and 'activation' state of the pro-convertase may explain the observed difference between the crystal structure of CVFB and the EM structure of C3bB.
19574954	7	29	theme	further	1298:1304	arg1	development					1306:1316	further development	1298:1316	further development of complement therapeutics	1298:1343	These insights into formation of convertases provide a basis for further development of complement therapeutics.
19574954	2	30	theme	complement	379:388	arg1	C3b					400:402	the complement component C3b	375:402	the complement component C3b	375:402	These short-lived protease complexes are formed through pro-convertases, which for the alternative pathway consist of the complement component C3b and the pro-enzyme factor B (FB).
19574954	7	31	theme	therapeutics	1332:1343	arg1	development					1306:1316	further development	1298:1316	further development of complement therapeutics	1298:1343	These insights into formation of convertases provide a basis for further development of complement therapeutics.
19574954	6	32	theme	dynamic	1044:1050	arg1	equilibrium					1052:1062	A possible dynamic equilibrium	1033:1062	A possible dynamic equilibrium between a 'loading' and 'activation' state of the pro-convertase	1033:1127	A possible dynamic equilibrium between a 'loading' and 'activation' state of the pro-convertase may explain the observed difference between the crystal structure of CVFB and the EM structure of C3bB.
19574954	6	33	theme	C3bB	1227:1230	arg1	structure					1185:1193	the crystal structure	1173:1193	the crystal structure of CVFB	1173:1201	A possible dynamic equilibrium between a 'loading' and 'activation' state of the pro-convertase may explain the observed difference between the crystal structure of CVFB and the EM structure of C3bB.
19574954	6	33	theme	C3bB	1227:1230	arg1	structure					1214:1222	the EM structure	1207:1222	the EM structure of C3bB	1207:1230	A possible dynamic equilibrium between a 'loading' and 'activation' state of the pro-convertase may explain the observed difference between the crystal structure of CVFB and the EM structure of C3bB.
19574954	0	34	theme	convertase	25:34	arg1	formation					36:44	complement convertase formation	14:44	complement convertase formation	14:44	Insights into complement convertase formation based on the structure of the factor B-cobra venom factor complex.
19574954	4	35	theme	pro-peptide	732:742	arg1	segment					747:753	its pro-peptide Ba segment	728:753	its pro-peptide Ba segment by specific contacts, which explain the specificity for the homologous C3b over the native C3 and inactive products iC3b and C3c	728:882	FB is loaded onto CVF through its pro-peptide Ba segment by specific contacts, which explain the specificity for the homologous C3b over the native C3 and inactive products iC3b and C3c.
19574954	3	36	theme	electron	531:538	arg1	microscopy					540:549	electron microscopy	531:549	electron microscopy (EM)	531:554	Here, we present the crystal structure at 2.2-A resolution, small-angle X-ray scattering and electron microscopy (EM) data of the pro-convertase formed by human FB and cobra venom factor (CVF), a potent homologue of C3b that generates more stable convertases.
19574954	3	36	theme	electron	531:538	arg1	EM					552:553	EM	552:553	EM	552:553	Here, we present the crystal structure at 2.2-A resolution, small-angle X-ray scattering and electron microscopy (EM) data of the pro-convertase formed by human FB and cobra venom factor (CVF), a potent homologue of C3b that generates more stable convertases.
19574954	2	37	theme	factor	423:428	arg1	FB					433:434	FB	433:434	FB	433:434	These short-lived protease complexes are formed through pro-convertases, which for the alternative pathway consist of the complement component C3b and the pro-enzyme factor B (FB).
19574954	2	37	theme	factor	423:428	arg1	B					430:430	the pro-enzyme factor B	408:430	the pro-enzyme factor B (FB)	408:435	These short-lived protease complexes are formed through pro-convertases, which for the alternative pathway consist of the complement component C3b and the pro-enzyme factor B (FB).
19574954	0	38	theme	complement	14:23	arg1	formation					36:44	complement convertase formation	14:44	complement convertase formation	14:44	Insights into complement convertase formation based on the structure of the factor B-cobra venom factor complex.
19574954	3	39	theme	small-angle	498:508	arg1	scattering					516:525	small-angle X-ray scattering	498:525	small-angle X-ray scattering	498:525	Here, we present the crystal structure at 2.2-A resolution, small-angle X-ray scattering and electron microscopy (EM) data of the pro-convertase formed by human FB and cobra venom factor (CVF), a potent homologue of C3b that generates more stable convertases.
19574954	3	40	theme	cobra	606:610	arg1	homologue					641:649	a potent homologue	632:649	a potent homologue of C3b that generates more stable convertases	632:695	Here, we present the crystal structure at 2.2-A resolution, small-angle X-ray scattering and electron microscopy (EM) data of the pro-convertase formed by human FB and cobra venom factor (CVF), a potent homologue of C3b that generates more stable convertases.
19574954	3	40	theme	cobra	606:610	arg1	CVF					626:628	CVF	626:628	CVF	626:628	Here, we present the crystal structure at 2.2-A resolution, small-angle X-ray scattering and electron microscopy (EM) data of the pro-convertase formed by human FB and cobra venom factor (CVF), a potent homologue of C3b that generates more stable convertases.
19574954	3	40	theme	cobra	606:610	arg1	factor					618:623	cobra venom factor	606:623	cobra venom factor (CVF)	606:629	Here, we present the crystal structure at 2.2-A resolution, small-angle X-ray scattering and electron microscopy (EM) data of the pro-convertase formed by human FB and cobra venom factor (CVF), a potent homologue of C3b that generates more stable convertases.
19574954	3	41	theme	2.2-A	480:484	arg1	resolution					486:495	2.2-A resolution	480:495	2.2-A resolution	480:495	Here, we present the crystal structure at 2.2-A resolution, small-angle X-ray scattering and electron microscopy (EM) data of the pro-convertase formed by human FB and cobra venom factor (CVF), a potent homologue of C3b that generates more stable convertases.
19574954	1	42	theme	convertases	193:203	arg1	assembly					178:185	assembly	178:185	assembly of C3 convertases on the surface of pathogens and altered host cells	178:254	Immune protection by the complement system critically depends on assembly of C3 convertases on the surface of pathogens and altered host cells.
19574954	3	43	theme	stable	678:683	arg1	convertases					685:695	more stable convertases	673:695	more stable convertases	673:695	Here, we present the crystal structure at 2.2-A resolution, small-angle X-ray scattering and electron microscopy (EM) data of the pro-convertase formed by human FB and cobra venom factor (CVF), a potent homologue of C3b that generates more stable convertases.
19574954	4	44	theme	inactive	853:860	arg1	products					862:869	inactive products	853:869	inactive products iC3b and C3c	853:882	FB is loaded onto CVF through its pro-peptide Ba segment by specific contacts, which explain the specificity for the homologous C3b over the native C3 and inactive products iC3b and C3c.
19574954	4	44	theme	inactive	853:860	arg1	C3c					880:882	C3c	880:882	C3c	880:882	FB is loaded onto CVF through its pro-peptide Ba segment by specific contacts, which explain the specificity for the homologous C3b over the native C3 and inactive products iC3b and C3c.
19574954	4	44	theme	inactive	853:860	arg1	iC3b					871:874	iC3b	871:874	iC3b	871:874	FB is loaded onto CVF through its pro-peptide Ba segment by specific contacts, which explain the specificity for the homologous C3b over the native C3 and inactive products iC3b and C3c.
19574954	3	45	theme	venom	612:616	arg1	homologue					641:649	a potent homologue	632:649	a potent homologue of C3b that generates more stable convertases	632:695	Here, we present the crystal structure at 2.2-A resolution, small-angle X-ray scattering and electron microscopy (EM) data of the pro-convertase formed by human FB and cobra venom factor (CVF), a potent homologue of C3b that generates more stable convertases.
19574954	3	45	theme	venom	612:616	arg1	CVF					626:628	CVF	626:628	CVF	626:628	Here, we present the crystal structure at 2.2-A resolution, small-angle X-ray scattering and electron microscopy (EM) data of the pro-convertase formed by human FB and cobra venom factor (CVF), a potent homologue of C3b that generates more stable convertases.
19574954	3	45	theme	venom	612:616	arg1	factor					618:623	cobra venom factor	606:623	cobra venom factor (CVF)	606:629	Here, we present the crystal structure at 2.2-A resolution, small-angle X-ray scattering and electron microscopy (EM) data of the pro-convertase formed by human FB and cobra venom factor (CVF), a potent homologue of C3b that generates more stable convertases.
19574954	4	46	dep	products	862:869	arg1	products					862:869	inactive products	853:869	inactive products iC3b and C3c	853:882	FB is loaded onto CVF through its pro-peptide Ba segment by specific contacts, which explain the specificity for the homologous C3b over the native C3 and inactive products iC3b and C3c.
19574954	4	46	dep	products	862:869	arg1	C3c					880:882	C3c	880:882	C3c	880:882	FB is loaded onto CVF through its pro-peptide Ba segment by specific contacts, which explain the specificity for the homologous C3b over the native C3 and inactive products iC3b and C3c.
19574954	4	46	dep	products	862:869	arg1	iC3b					871:874	iC3b	871:874	iC3b	871:874	FB is loaded onto CVF through its pro-peptide Ba segment by specific contacts, which explain the specificity for the homologous C3b over the native C3 and inactive products iC3b and C3c.
19574954	4	47	theme	Ba	744:745	arg1	segment					747:753	its pro-peptide Ba segment	728:753	its pro-peptide Ba segment by specific contacts, which explain the specificity for the homologous C3b over the native C3 and inactive products iC3b and C3c	728:882	FB is loaded onto CVF through its pro-peptide Ba segment by specific contacts, which explain the specificity for the homologous C3b over the native C3 and inactive products iC3b and C3c.
19574954	6	48	theme	CVFB	1198:1201	arg1	structure					1185:1193	the crystal structure	1173:1193	the crystal structure of CVFB	1173:1201	A possible dynamic equilibrium between a 'loading' and 'activation' state of the pro-convertase may explain the observed difference between the crystal structure of CVFB and the EM structure of C3bB.
19574954	6	48	theme	CVFB	1198:1201	arg1	structure					1214:1222	the EM structure	1207:1222	the EM structure of C3bB	1207:1230	A possible dynamic equilibrium between a 'loading' and 'activation' state of the pro-convertase may explain the observed difference between the crystal structure of CVFB and the EM structure of C3bB.
19574954	6	49	theme	EM	1211:1212	arg1	structure					1214:1222	the EM structure	1207:1222	the EM structure of C3bB	1207:1230	A possible dynamic equilibrium between a 'loading' and 'activation' state of the pro-convertase may explain the observed difference between the crystal structure of CVFB and the EM structure of C3bB.
19574954	5	50	theme	Von	996:998	arg1	factor					1011:1016	Von Willebrand factor	996:1016	the Von Willebrand factor A-type domain	992:1030	The protease segment Bb binds the carboxy terminus of CVF through the metal-ion dependent adhesion site of the Von Willebrand factor A-type domain.
19574954	4	51	theme	specific	758:765	arg1	contacts					767:774	specific contacts	758:774	specific contacts	758:774	FB is loaded onto CVF through its pro-peptide Ba segment by specific contacts, which explain the specificity for the homologous C3b over the native C3 and inactive products iC3b and C3c.
19574954	3	52	theme	crystal	459:465	arg1	structure					467:475	the crystal structure	455:475	the crystal structure	455:475	Here, we present the crystal structure at 2.2-A resolution, small-angle X-ray scattering and electron microscopy (EM) data of the pro-convertase formed by human FB and cobra venom factor (CVF), a potent homologue of C3b that generates more stable convertases.
19574954	4	53	theme	homologous	815:824	arg1	C3b					826:828	the homologous C3b	811:828	the homologous C3b over the native C3	811:847	FB is loaded onto CVF through its pro-peptide Ba segment by specific contacts, which explain the specificity for the homologous C3b over the native C3 and inactive products iC3b and C3c.
19574954	7	54	theme	convertases	1266:1276	arg1	formation					1253:1261	formation	1253:1261	formation of convertases	1253:1276	These insights into formation of convertases provide a basis for further development of complement therapeutics.
19574954	1	55	theme	Immune	113:118	arg1	protection					120:129	Immune protection	113:129	Immune protection by the complement system	113:154	Immune protection by the complement system critically depends on assembly of C3 convertases on the surface of pathogens and altered host cells.
19574954	6	56	theme	activation	1089:1098	arg1	state					1101:1105	'activation' state	1088:1105	'activation' state	1088:1105	A possible dynamic equilibrium between a 'loading' and 'activation' state of the pro-convertase may explain the observed difference between the crystal structure of CVFB and the EM structure of C3bB.
19574954	5	57	theme	segment	898:904	arg1	Bb					906:907	The protease segment Bb	885:907	The protease segment Bb	885:907	The protease segment Bb binds the carboxy terminus of CVF through the metal-ion dependent adhesion site of the Von Willebrand factor A-type domain.
19574954	5	58	theme	dependent	965:973	arg1	domain					1025:1030	the Von Willebrand factor A-type domain	992:1030	the Von Willebrand factor A-type domain	992:1030	The protease segment Bb binds the carboxy terminus of CVF through the metal-ion dependent adhesion site of the Von Willebrand factor A-type domain.
19574954	5	58	theme	dependent	965:973	arg1	site					984:987	the metal-ion dependent adhesion site	951:987	the metal-ion dependent adhesion site of the Von Willebrand factor A-type domain	951:1030	The protease segment Bb binds the carboxy terminus of CVF through the metal-ion dependent adhesion site of the Von Willebrand factor A-type domain.
19574954	3	59	theme	human	593:597	arg1	FB					599:600	human FB	593:600	human FB	593:600	Here, we present the crystal structure at 2.2-A resolution, small-angle X-ray scattering and electron microscopy (EM) data of the pro-convertase formed by human FB and cobra venom factor (CVF), a potent homologue of C3b that generates more stable convertases.
19574954	1	60	from	assembly	178:185	arg1	surface					212:218	the surface	208:218	the surface of pathogens and altered host cells	208:254	Immune protection by the complement system critically depends on assembly of C3 convertases on the surface of pathogens and altered host cells.
19574954	6	61	theme	pro-convertase	1114:1127	arg1	state					1101:1105	'activation' state	1088:1105	'activation' state	1088:1105	A possible dynamic equilibrium between a 'loading' and 'activation' state of the pro-convertase may explain the observed difference between the crystal structure of CVFB and the EM structure of C3bB.
19574954	6	61	theme	pro-convertase	1114:1127	arg1	loading					1075:1081	a 'loading'	1072:1082	a 'loading'	1072:1082	A possible dynamic equilibrium between a 'loading' and 'activation' state of the pro-convertase may explain the observed difference between the crystal structure of CVFB and the EM structure of C3bB.
19574954	5	62	theme	adhesion	975:982	arg1	domain					1025:1030	the Von Willebrand factor A-type domain	992:1030	the Von Willebrand factor A-type domain	992:1030	The protease segment Bb binds the carboxy terminus of CVF through the metal-ion dependent adhesion site of the Von Willebrand factor A-type domain.
19574954	5	62	theme	adhesion	975:982	arg1	site					984:987	the metal-ion dependent adhesion site	951:987	the metal-ion dependent adhesion site of the Von Willebrand factor A-type domain	951:1030	The protease segment Bb binds the carboxy terminus of CVF through the metal-ion dependent adhesion site of the Von Willebrand factor A-type domain.
19574954	3	63	theme	pro-convertase	568:581	arg1	data					556:559	small-angle X-ray scattering and electron microscopy (EM) data	498:559	small-angle X-ray scattering and electron microscopy (EM) data of the pro-convertase formed by human FB and cobra venom factor (CVF), a potent homologue of C3b that generates more stable convertases	498:695	Here, we present the crystal structure at 2.2-A resolution, small-angle X-ray scattering and electron microscopy (EM) data of the pro-convertase formed by human FB and cobra venom factor (CVF), a potent homologue of C3b that generates more stable convertases.
19574954	1	64	theme	C3	190:191	arg1	convertases					193:203	C3 convertases	190:203	C3 convertases	190:203	Immune protection by the complement system critically depends on assembly of C3 convertases on the surface of pathogens and altered host cells.
19574954	1	65	theme	pathogens	223:231	arg1	surface					212:218	the surface	208:218	the surface of pathogens and altered host cells	208:254	Immune protection by the complement system critically depends on assembly of C3 convertases on the surface of pathogens and altered host cells.
19574954	3	66	theme	potent	634:639	arg1	homologue					641:649	a potent homologue	632:649	a potent homologue of C3b that generates more stable convertases	632:695	Here, we present the crystal structure at 2.2-A resolution, small-angle X-ray scattering and electron microscopy (EM) data of the pro-convertase formed by human FB and cobra venom factor (CVF), a potent homologue of C3b that generates more stable convertases.
19574954	3	66	theme	potent	634:639	arg1	factor					618:623	cobra venom factor	606:623	cobra venom factor (CVF)	606:629	Here, we present the crystal structure at 2.2-A resolution, small-angle X-ray scattering and electron microscopy (EM) data of the pro-convertase formed by human FB and cobra venom factor (CVF), a potent homologue of C3b that generates more stable convertases.
19574954	5	67	theme	carboxy	919:925	arg1	terminus					927:934	the carboxy terminus	915:934	the carboxy terminus of CVF	915:941	The protease segment Bb binds the carboxy terminus of CVF through the metal-ion dependent adhesion site of the Von Willebrand factor A-type domain.
19574954	1	68	theme	complement	138:147	arg1	system					149:154	the complement system	134:154	the complement system	134:154	Immune protection by the complement system critically depends on assembly of C3 convertases on the surface of pathogens and altered host cells.
6546754	8	0	theme	catalytic	1246:1254	arg1	region					1256:1261	the catalytic region	1242:1261	the catalytic region of the C3 convertase	1242:1282	It is suggested that these "altered" regions contribute at least in part to the formation of the catalytic region of the C3 convertase.
6546754	6	1	theme	site	858:861	arg1	alignment					834:842	Sequence alignment	825:842	Sequence alignment of the active site of B to the serine proteases	825:890	Sequence alignment of the active site of B to the serine proteases was made using the three-dimensional structures of chymotrypsin and trypsin as molecular models.
6546754	8	2	theme	region	1256:1261	arg1	formation					1229:1237	the formation	1225:1237	the formation of the catalytic region of the C3 convertase	1225:1282	It is suggested that these "altered" regions contribute at least in part to the formation of the catalytic region of the C3 convertase.
6546754	0	3	theme	B	70:70	arg1	zymogen					35:41	the zymogen	31:41	the zymogen of human complement factor B	31:70	Complete primary structure for the zymogen of human complement factor B.
6546754	6	4	theme	active	851:856	arg1	B					866:866	B	866:866	B	866:866	Sequence alignment of the active site of B to the serine proteases was made using the three-dimensional structures of chymotrypsin and trypsin as molecular models.
6546754	6	4	theme	active	851:856	arg1	site					858:861	the active site	847:861	the active site of B to the serine proteases	847:890	Sequence alignment of the active site of B to the serine proteases was made using the three-dimensional structures of chymotrypsin and trypsin as molecular models.
6546754	5	5	theme	Ba	610:611	arg1	fragment					613:620	The Ba fragment	606:620	The Ba fragment	606:620	The Ba fragment was found to contain three regions of internal sequence homology which were unrelated to the "kringle" regions of prothrombin and plasminogen and which suggest an independent evolution for the B genome.
6546754	2	6	theme	COOH-terminal	338:350	arg1	regions					352:358	COOH-terminal regions	338:358	COOH-terminal regions	338:358	The zymogen consists of 739 amino acids, has four asparagine-linked carbohydrate sites, and has independently disulfide-bonded NH2- and COOH-terminal regions.
6546754	5	7	theme	homology	678:685	arg1	regions					649:655	three regions	643:655	three regions of internal sequence homology which were unrelated to the "kringle" regions of prothrombin and plasminogen and which suggest an independent evolution for the B genome	643:822	The Ba fragment was found to contain three regions of internal sequence homology which were unrelated to the "kringle" regions of prothrombin and plasminogen and which suggest an independent evolution for the B genome.
6546754	3	8	theme	classical	479:487	arg1	proteases					496:504	the classical serine proteases	475:504	the classical serine proteases	475:504	The catalytic subunit, Bb, is a unique serine protease containing 259 amino acids that are not integral to any of the classical serine proteases.
6546754	2	9	theme	carbohydrate	270:281	arg1	sites					283:287	four asparagine-linked carbohydrate sites	247:287	four asparagine-linked carbohydrate sites	247:287	The zymogen consists of 739 amino acids, has four asparagine-linked carbohydrate sites, and has independently disulfide-bonded NH2- and COOH-terminal regions.
6546754	4	10	theme	fragment	549:556	arg1	domain					590:595	a cofactor-binding domain	571:595	a cofactor-binding domain for C3b	571:603	It is proposed that this region of the Bb fragment functions as a cofactor-binding domain for C3b.
6546754	4	10	theme	fragment	549:556	arg1	region					532:537	this region	527:537	this region of the Bb fragment	527:556	It is proposed that this region of the Bb fragment functions as a cofactor-binding domain for C3b.
6546754	2	11	theme	asparagine-linked	252:268	arg1	sites					283:287	four asparagine-linked carbohydrate sites	247:287	four asparagine-linked carbohydrate sites	247:287	The zymogen consists of 739 amino acids, has four asparagine-linked carbohydrate sites, and has independently disulfide-bonded NH2- and COOH-terminal regions.
6546754	4	12	theme	Bb	546:547	arg1	fragment					549:556	the Bb fragment	542:556	the Bb fragment	542:556	It is proposed that this region of the Bb fragment functions as a cofactor-binding domain for C3b.
6546754	7	13	theme	predicted	1124:1132	arg1	configuration					1134:1146	predicted configuration	1124:1146	predicted configuration	1124:1146	Three stretches within the hypothetical model for B contrast markedly with all known serine proteases in both amino acid sequences and predicted configuration.
6546754	7	14	theme	B	1039:1039	arg1	contrast					1041:1048	B contrast	1039:1048	B contrast	1039:1048	Three stretches within the hypothetical model for B contrast markedly with all known serine proteases in both amino acid sequences and predicted configuration.
6546754	8	15	theme	convertase	1273:1282	arg1	region					1256:1261	the catalytic region	1242:1261	the catalytic region of the C3 convertase	1242:1282	It is suggested that these "altered" regions contribute at least in part to the formation of the catalytic region of the C3 convertase.
6546754	3	16	theme	serine	400:405	arg1	protease					407:414	a unique serine protease	391:414	a unique serine protease containing 259 amino acids that are not integral to any of the classical serine proteases	391:504	The catalytic subunit, Bb, is a unique serine protease containing 259 amino acids that are not integral to any of the classical serine proteases.
6546754	3	16	theme	serine	400:405	arg1	subunit					375:381	The catalytic subunit	361:381	The catalytic subunit	361:381	The catalytic subunit, Bb, is a unique serine protease containing 259 amino acids that are not integral to any of the classical serine proteases.
6546754	8	17	theme	altered	1177:1183	arg1	regions					1186:1192	these "altered" regions	1170:1192	these "altered" regions	1170:1192	It is suggested that these "altered" regions contribute at least in part to the formation of the catalytic region of the C3 convertase.
6546754	7	18	theme	serine	1074:1079	arg1	proteases					1081:1089	all known serine proteases	1064:1089	all known serine proteases in both amino acid sequences and predicted configuration	1064:1146	Three stretches within the hypothetical model for B contrast markedly with all known serine proteases in both amino acid sequences and predicted configuration.
6546754	6	19	theme	Sequence	825:832	arg1	alignment					834:842	Sequence alignment	825:842	Sequence alignment of the active site of B to the serine proteases	825:890	Sequence alignment of the active site of B to the serine proteases was made using the three-dimensional structures of chymotrypsin and trypsin as molecular models.
6546754	5	20	theme	plasminogen	752:762	arg1	regions					725:731	the "kringle" regions	711:731	the "kringle" regions of prothrombin and plasminogen	711:762	The Ba fragment was found to contain three regions of internal sequence homology which were unrelated to the "kringle" regions of prothrombin and plasminogen and which suggest an independent evolution for the B genome.
6546754	0	21	theme	primary	9:15	arg1	structure					17:25	Complete primary structure	0:25	Complete primary structure for the zymogen of human complement factor B.	0:71	Complete primary structure for the zymogen of human complement factor B.
6546754	5	22	theme	kringle	716:722	arg1	regions					725:731	the "kringle" regions	711:731	the "kringle" regions of prothrombin and plasminogen	711:762	The Ba fragment was found to contain three regions of internal sequence homology which were unrelated to the "kringle" regions of prothrombin and plasminogen and which suggest an independent evolution for the B genome.
6546754	5	23	theme	B	815:815	arg1	genome					817:822	the B genome	811:822	the B genome	811:822	The Ba fragment was found to contain three regions of internal sequence homology which were unrelated to the "kringle" regions of prothrombin and plasminogen and which suggest an independent evolution for the B genome.
6546754	1	24	theme	protein	163:169	arg1	strategies					190:199	both protein and DNA sequencing strategies	158:199	both protein and DNA sequencing strategies	158:199	The entire amino acid sequence of complement factor B has been established combining both protein and DNA sequencing strategies.
6546754	0	25	theme	Complete	0:7	arg1	structure					17:25	Complete primary structure	0:25	Complete primary structure for the zymogen of human complement factor B.	0:71	Complete primary structure for the zymogen of human complement factor B.
6546754	2	26	contain	has	243:245	arg1	zymogen					206:212	The zymogen	202:212	The zymogen	202:212	The zymogen consists of 739 amino acids, has four asparagine-linked carbohydrate sites, and has independently disulfide-bonded NH2- and COOH-terminal regions.
6546754	2	26	contain	has	243:245	arg2	sites					283:287	four asparagine-linked carbohydrate sites	247:287	four asparagine-linked carbohydrate sites	247:287	The zymogen consists of 739 amino acids, has four asparagine-linked carbohydrate sites, and has independently disulfide-bonded NH2- and COOH-terminal regions.
6546754	1	27	theme	entire	77:82	arg1	sequence					95:102	The entire amino acid sequence	73:102	The entire amino acid sequence of complement factor B	73:125	The entire amino acid sequence of complement factor B has been established combining both protein and DNA sequencing strategies.
6546754	7	28	theme	known	1068:1072	arg1	proteases					1081:1089	all known serine proteases	1064:1089	all known serine proteases in both amino acid sequences and predicted configuration	1064:1146	Three stretches within the hypothetical model for B contrast markedly with all known serine proteases in both amino acid sequences and predicted configuration.
6546754	3	29	theme	catalytic	365:373	arg1	Bb					384:385	Bb	384:385	Bb	384:385	The catalytic subunit, Bb, is a unique serine protease containing 259 amino acids that are not integral to any of the classical serine proteases.
6546754	3	29	theme	catalytic	365:373	arg1	subunit					375:381	The catalytic subunit	361:381	The catalytic subunit	361:381	The catalytic subunit, Bb, is a unique serine protease containing 259 amino acids that are not integral to any of the classical serine proteases.
6546754	3	29	theme	catalytic	365:373	arg1	protease					407:414	a unique serine protease	391:414	a unique serine protease containing 259 amino acids that are not integral to any of the classical serine proteases	391:504	The catalytic subunit, Bb, is a unique serine protease containing 259 amino acids that are not integral to any of the classical serine proteases.
6546754	1	30	theme	amino	84:88	arg1	sequence					95:102	The entire amino acid sequence	73:102	The entire amino acid sequence of complement factor B	73:125	The entire amino acid sequence of complement factor B has been established combining both protein and DNA sequencing strategies.
6546754	1	31	theme	DNA	175:177	arg1	sequencing					179:188	DNA sequencing	175:188	DNA sequencing	175:188	The entire amino acid sequence of complement factor B has been established combining both protein and DNA sequencing strategies.
6546754	7	32	theme	acid	1105:1108	arg1	sequences					1110:1118	amino acid sequences	1099:1118	amino acid sequences	1099:1118	Three stretches within the hypothetical model for B contrast markedly with all known serine proteases in both amino acid sequences and predicted configuration.
6546754	7	33	theme	hypothetical	1016:1027	arg1	model					1029:1033	the hypothetical model	1012:1033	the hypothetical model for B contrast	1012:1048	Three stretches within the hypothetical model for B contrast markedly with all known serine proteases in both amino acid sequences and predicted configuration.
6546754	1	34	theme	acid	90:93	arg1	sequence					95:102	The entire amino acid sequence	73:102	The entire amino acid sequence of complement factor B	73:125	The entire amino acid sequence of complement factor B has been established combining both protein and DNA sequencing strategies.
6546754	1	35	theme	sequencing	179:188	arg1	strategies					190:199	both protein and DNA sequencing strategies	158:199	both protein and DNA sequencing strategies	158:199	The entire amino acid sequence of complement factor B has been established combining both protein and DNA sequencing strategies.
6546754	5	36	theme	"	723:723	arg1	regions					725:731	the "kringle" regions	711:731	the "kringle" regions of prothrombin and plasminogen	711:762	The Ba fragment was found to contain three regions of internal sequence homology which were unrelated to the "kringle" regions of prothrombin and plasminogen and which suggest an independent evolution for the B genome.
6546754	2	37	link	asparagine-linked	252:268	arg1	sites					283:287	four asparagine-linked carbohydrate sites	247:287	four asparagine-linked carbohydrate sites	247:287	The zymogen consists of 739 amino acids, has four asparagine-linked carbohydrate sites, and has independently disulfide-bonded NH2- and COOH-terminal regions.
6546754	5	38	theme	internal	660:667	arg1	homology					678:685	internal sequence homology	660:685	internal sequence homology	660:685	The Ba fragment was found to contain three regions of internal sequence homology which were unrelated to the "kringle" regions of prothrombin and plasminogen and which suggest an independent evolution for the B genome.
6546754	5	39	theme	independent	785:795	arg1	evolution					797:805	an independent evolution	782:805	an independent evolution for the B genome	782:822	The Ba fragment was found to contain three regions of internal sequence homology which were unrelated to the "kringle" regions of prothrombin and plasminogen and which suggest an independent evolution for the B genome.
6546754	8	40	theme	"	1184:1184	arg1	regions					1186:1192	these "altered" regions	1170:1192	these "altered" regions	1170:1192	It is suggested that these "altered" regions contribute at least in part to the formation of the catalytic region of the C3 convertase.
6546754	3	41	theme	amino	431:435	arg1	acids					437:441	259 amino acids	427:441	259 amino acids that are not integral to any of the classical serine proteases	427:504	The catalytic subunit, Bb, is a unique serine protease containing 259 amino acids that are not integral to any of the classical serine proteases.
6546754	3	42	theme	unique	393:398	arg1	protease					407:414	a unique serine protease	391:414	a unique serine protease containing 259 amino acids that are not integral to any of the classical serine proteases	391:504	The catalytic subunit, Bb, is a unique serine protease containing 259 amino acids that are not integral to any of the classical serine proteases.
6546754	3	42	theme	unique	393:398	arg1	subunit					375:381	The catalytic subunit	361:381	The catalytic subunit	361:381	The catalytic subunit, Bb, is a unique serine protease containing 259 amino acids that are not integral to any of the classical serine proteases.
6546754	6	43	theme	serine	875:880	arg1	proteases					882:890	the serine proteases	871:890	the serine proteases	871:890	Sequence alignment of the active site of B to the serine proteases was made using the three-dimensional structures of chymotrypsin and trypsin as molecular models.
6546754	5	44	theme	sequence	669:676	arg1	homology					678:685	internal sequence homology	660:685	internal sequence homology	660:685	The Ba fragment was found to contain three regions of internal sequence homology which were unrelated to the "kringle" regions of prothrombin and plasminogen and which suggest an independent evolution for the B genome.
6546754	7	45	theme	amino	1099:1103	arg1	sequences					1110:1118	amino acid sequences	1099:1118	amino acid sequences	1099:1118	Three stretches within the hypothetical model for B contrast markedly with all known serine proteases in both amino acid sequences and predicted configuration.
6546754	6	46	theme	B	866:866	arg1	B					866:866	B	866:866	B	866:866	Sequence alignment of the active site of B to the serine proteases was made using the three-dimensional structures of chymotrypsin and trypsin as molecular models.
6546754	6	46	theme	B	866:866	arg1	site					858:861	the active site	847:861	the active site of B to the serine proteases	847:890	Sequence alignment of the active site of B to the serine proteases was made using the three-dimensional structures of chymotrypsin and trypsin as molecular models.
6546754	0	47	theme	human	46:50	arg1	B					70:70	human complement factor B	46:70	human complement factor B	46:70	Complete primary structure for the zymogen of human complement factor B.
6546754	5	48	contain	contain	635:641	arg1	fragment					613:620	The Ba fragment	606:620	The Ba fragment	606:620	The Ba fragment was found to contain three regions of internal sequence homology which were unrelated to the "kringle" regions of prothrombin and plasminogen and which suggest an independent evolution for the B genome.
6546754	5	48	contain	contain	635:641	arg2	regions					649:655	three regions	643:655	three regions of internal sequence homology which were unrelated to the "kringle" regions of prothrombin and plasminogen and which suggest an independent evolution for the B genome	643:822	The Ba fragment was found to contain three regions of internal sequence homology which were unrelated to the "kringle" regions of prothrombin and plasminogen and which suggest an independent evolution for the B genome.
6546754	6	49	theme	molecular	971:979	arg1	structures					929:938	the three-dimensional structures	907:938	the three-dimensional structures of chymotrypsin and trypsin	907:966	Sequence alignment of the active site of B to the serine proteases was made using the three-dimensional structures of chymotrypsin and trypsin as molecular models.
6546754	6	49	theme	molecular	971:979	arg1	models					981:986	molecular models	971:986	molecular models	971:986	Sequence alignment of the active site of B to the serine proteases was made using the three-dimensional structures of chymotrypsin and trypsin as molecular models.
6546754	5	50	theme	prothrombin	736:746	arg1	regions					725:731	the "kringle" regions	711:731	the "kringle" regions of prothrombin and plasminogen	711:762	The Ba fragment was found to contain three regions of internal sequence homology which were unrelated to the "kringle" regions of prothrombin and plasminogen and which suggest an independent evolution for the B genome.
6546754	7	51	from	proteases	1081:1089	arg1	sequences					1110:1118	amino acid sequences	1099:1118	amino acid sequences	1099:1118	Three stretches within the hypothetical model for B contrast markedly with all known serine proteases in both amino acid sequences and predicted configuration.
6546754	7	51	from	proteases	1081:1089	arg1	configuration					1134:1146	predicted configuration	1124:1146	predicted configuration	1124:1146	Three stretches within the hypothetical model for B contrast markedly with all known serine proteases in both amino acid sequences and predicted configuration.
6546754	2	52	contain	has	294:296	arg2	regions					352:358	COOH-terminal regions	338:358	COOH-terminal regions	338:358	The zymogen consists of 739 amino acids, has four asparagine-linked carbohydrate sites, and has independently disulfide-bonded NH2- and COOH-terminal regions.
6546754	2	52	contain	has	294:296	arg1	zymogen					206:212	The zymogen	202:212	The zymogen	202:212	The zymogen consists of 739 amino acids, has four asparagine-linked carbohydrate sites, and has independently disulfide-bonded NH2- and COOH-terminal regions.
6546754	2	52	contain	has	294:296	arg2	NH2-					329:332	independently disulfide-bonded NH2-	298:332	independently disulfide-bonded NH2-	298:332	The zymogen consists of 739 amino acids, has four asparagine-linked carbohydrate sites, and has independently disulfide-bonded NH2- and COOH-terminal regions.
6546754	6	53	theme	trypsin	960:966	arg1	structures					929:938	the three-dimensional structures	907:938	the three-dimensional structures of chymotrypsin and trypsin	907:966	Sequence alignment of the active site of B to the serine proteases was made using the three-dimensional structures of chymotrypsin and trypsin as molecular models.
6546754	6	53	theme	trypsin	960:966	arg1	models					981:986	molecular models	971:986	molecular models	971:986	Sequence alignment of the active site of B to the serine proteases was made using the three-dimensional structures of chymotrypsin and trypsin as molecular models.
6546754	1	54	theme	complement	107:116	arg1	B					125:125	complement factor B	107:125	complement factor B	107:125	The entire amino acid sequence of complement factor B has been established combining both protein and DNA sequencing strategies.
6546754	6	55	theme	three-dimensional	911:927	arg1	structures					929:938	the three-dimensional structures	907:938	the three-dimensional structures of chymotrypsin and trypsin	907:966	Sequence alignment of the active site of B to the serine proteases was made using the three-dimensional structures of chymotrypsin and trypsin as molecular models.
6546754	6	55	theme	three-dimensional	911:927	arg1	models					981:986	molecular models	971:986	molecular models	971:986	Sequence alignment of the active site of B to the serine proteases was made using the three-dimensional structures of chymotrypsin and trypsin as molecular models.
6546754	8	56	theme	C3	1270:1271	arg1	convertase					1273:1282	the C3 convertase	1266:1282	the C3 convertase	1266:1282	It is suggested that these "altered" regions contribute at least in part to the formation of the catalytic region of the C3 convertase.
6546754	1	57	theme	factor	118:123	arg1	B					125:125	complement factor B	107:125	complement factor B	107:125	The entire amino acid sequence of complement factor B has been established combining both protein and DNA sequencing strategies.
6546754	2	58	theme	disulfide-bonded	312:327	arg1	NH2-					329:332	independently disulfide-bonded NH2-	298:332	independently disulfide-bonded NH2-	298:332	The zymogen consists of 739 amino acids, has four asparagine-linked carbohydrate sites, and has independently disulfide-bonded NH2- and COOH-terminal regions.
6546754	0	59	theme	factor	63:68	arg1	B					70:70	human complement factor B	46:70	human complement factor B	46:70	Complete primary structure for the zymogen of human complement factor B.
6546754	3	60	contain	containing	416:425	arg2	acids					437:441	259 amino acids	427:441	259 amino acids that are not integral to any of the classical serine proteases	427:504	The catalytic subunit, Bb, is a unique serine protease containing 259 amino acids that are not integral to any of the classical serine proteases.
6546754	3	60	contain	containing	416:425	arg1	protease					407:414	a unique serine protease	391:414	a unique serine protease containing 259 amino acids that are not integral to any of the classical serine proteases	391:504	The catalytic subunit, Bb, is a unique serine protease containing 259 amino acids that are not integral to any of the classical serine proteases.
6546754	3	60	contain	containing	416:425	arg1	subunit					375:381	The catalytic subunit	361:381	The catalytic subunit	361:381	The catalytic subunit, Bb, is a unique serine protease containing 259 amino acids that are not integral to any of the classical serine proteases.
6546754	2	61	theme	amino	230:234	arg1	acids					236:240	739 amino acids	226:240	739 amino acids	226:240	The zymogen consists of 739 amino acids, has four asparagine-linked carbohydrate sites, and has independently disulfide-bonded NH2- and COOH-terminal regions.
6546754	1	62	theme	B	125:125	arg1	sequence					95:102	The entire amino acid sequence	73:102	The entire amino acid sequence of complement factor B	73:125	The entire amino acid sequence of complement factor B has been established combining both protein and DNA sequencing strategies.
6546754	4	63	theme	cofactor-binding	573:588	arg1	domain					590:595	a cofactor-binding domain	571:595	a cofactor-binding domain for C3b	571:603	It is proposed that this region of the Bb fragment functions as a cofactor-binding domain for C3b.
6546754	4	63	theme	cofactor-binding	573:588	arg1	region					532:537	this region	527:537	this region of the Bb fragment	527:556	It is proposed that this region of the Bb fragment functions as a cofactor-binding domain for C3b.
6546754	0	64	theme	complement	52:61	arg1	B					70:70	human complement factor B	46:70	human complement factor B	46:70	Complete primary structure for the zymogen of human complement factor B.
6546754	3	65	theme	serine	489:494	arg1	proteases					496:504	the classical serine proteases	475:504	the classical serine proteases	475:504	The catalytic subunit, Bb, is a unique serine protease containing 259 amino acids that are not integral to any of the classical serine proteases.
6546754	6	66	theme	chymotrypsin	943:954	arg1	structures					929:938	the three-dimensional structures	907:938	the three-dimensional structures of chymotrypsin and trypsin	907:966	Sequence alignment of the active site of B to the serine proteases was made using the three-dimensional structures of chymotrypsin and trypsin as molecular models.
6546754	6	66	theme	chymotrypsin	943:954	arg1	models					981:986	molecular models	971:986	molecular models	971:986	Sequence alignment of the active site of B to the serine proteases was made using the three-dimensional structures of chymotrypsin and trypsin as molecular models.
18536718	0	0	theme	complement	67:76	arg1	component					78:86	human complement component 5	61:88	human complement component 5	61:88	Structure of and influence of a tick complement inhibitor on human complement component 5.
18536718	4	1	theme	OmCI	585:588	arg1	Binding					552:558	Binding	552:558	Binding of the tick C5 inhibitor OmCI to C5	552:594	Binding of the tick C5 inhibitor OmCI to C5 resulted in stabilization of the global conformation of C5 but did not block the convertase cleavage site.
18536718	1	2	theme	functional	134:143	arg1	properties					145:154	the structural and functional properties	115:154	the structural and functional properties of human complement component 5 (C5)	115:191	To provide insight into the structural and functional properties of human complement component 5 (C5), we determined its crystal structure at a resolution of 3.1 A.
18536718	1	3	theme	crystal	212:218	arg1	structure					220:228	its crystal structure	208:228	its crystal structure	208:228	To provide insight into the structural and functional properties of human complement component 5 (C5), we determined its crystal structure at a resolution of 3.1 A.
18536718	0	4	theme	human	61:65	arg1	component					78:86	human complement component 5	61:88	human complement component 5	61:88	Structure of and influence of a tick complement inhibitor on human complement component 5.
18536718	4	5	theme	inhibitor	575:583	arg1	OmCI					585:588	the tick C5 inhibitor OmCI	563:588	the tick C5 inhibitor OmCI	563:588	Binding of the tick C5 inhibitor OmCI to C5 resulted in stabilization of the global conformation of C5 but did not block the convertase cleavage site.
18536718	0	6	from	Structure	0:8	arg1	component					78:86	human complement component 5	61:88	human complement component 5	61:88	Structure of and influence of a tick complement inhibitor on human complement component 5.
18536718	3	7	theme	convertase	451:460	arg1	site					471:474	the convertase cleavage site	447:474	the convertase cleavage site in C5	447:480	However, in contrast to C3, the convertase cleavage site in C5 was ordered and the C345C domain flexibly attached to the core of C5.
18536718	4	8	theme	conformation	636:647	arg1	stabilization					608:620	stabilization	608:620	stabilization of the global conformation of C5	608:653	Binding of the tick C5 inhibitor OmCI to C5 resulted in stabilization of the global conformation of C5 but did not block the convertase cleavage site.
18536718	3	9	theme	cleavage	462:469	arg1	site					471:474	the convertase cleavage site	447:474	the convertase cleavage site in C5	447:480	However, in contrast to C3, the convertase cleavage site in C5 was ordered and the C345C domain flexibly attached to the core of C5.
18536718	5	10	theme	selective	792:800	arg1	inhibitors					813:822	new selective complement inhibitors	788:822	new selective complement inhibitors	788:822	The structure of C5 may render possible a structure-based approach for the design of new selective complement inhibitors.
18536718	5	11	theme	possible	734:741	arg1	approach					761:768	possible a structure-based approach	734:768	possible a structure-based approach for the design of new selective complement inhibitors	734:822	The structure of C5 may render possible a structure-based approach for the design of new selective complement inhibitors.
18536718	2	12	theme	domain	323:328	arg1	arrangement					330:340	the domain arrangement	319:340	the domain arrangement at the position corresponding to the C3 thioester	319:390	The core of C5 adopted a structure resembling that of C3, with the domain arrangement at the position corresponding to the C3 thioester being very well conserved.
18536718	4	13	theme	C5	652:653	arg1	conformation					636:647	the global conformation	625:647	the global conformation of C5	625:653	Binding of the tick C5 inhibitor OmCI to C5 resulted in stabilization of the global conformation of C5 but did not block the convertase cleavage site.
18536718	1	14	theme	human	159:163	arg1	C5					189:190	human complement component 5 (C5)	159:191	human complement component 5 (C5)	159:191	To provide insight into the structural and functional properties of human complement component 5 (C5), we determined its crystal structure at a resolution of 3.1 A.
18536718	2	15	theme	C3	379:380	arg1	thioester					382:390	the C3 thioester	375:390	the C3 thioester	375:390	The core of C5 adopted a structure resembling that of C3, with the domain arrangement at the position corresponding to the C3 thioester being very well conserved.
18536718	5	16	theme	complement	802:811	arg1	inhibitors					813:822	new selective complement inhibitors	788:822	new selective complement inhibitors	788:822	The structure of C5 may render possible a structure-based approach for the design of new selective complement inhibitors.
18536718	1	17	theme	complement	165:174	arg1	C5					189:190	human complement component 5 (C5)	159:191	human complement component 5 (C5)	159:191	To provide insight into the structural and functional properties of human complement component 5 (C5), we determined its crystal structure at a resolution of 3.1 A.
18536718	5	18	theme	inhibitors	813:822	arg1	design					778:783	the design	774:783	the design of new selective complement inhibitors	774:822	The structure of C5 may render possible a structure-based approach for the design of new selective complement inhibitors.
18536718	1	19	theme	component	176:184	arg1	C5					189:190	human complement component 5 (C5)	159:191	human complement component 5 (C5)	159:191	To provide insight into the structural and functional properties of human complement component 5 (C5), we determined its crystal structure at a resolution of 3.1 A.
18536718	0	20	theme	influence	17:25	arg1	Structure					0:8	Structure	0:8	Structure of and influence of a tick complement inhibitor on human complement component 5.	0:89	Structure of and influence of a tick complement inhibitor on human complement component 5.
18536718	4	21	theme	global	629:634	arg1	conformation					636:647	the global conformation	625:647	the global conformation of C5	625:653	Binding of the tick C5 inhibitor OmCI to C5 resulted in stabilization of the global conformation of C5 but did not block the convertase cleavage site.
18536718	4	22	theme	C5	572:573	arg1	OmCI					585:588	the tick C5 inhibitor OmCI	563:588	the tick C5 inhibitor OmCI	563:588	Binding of the tick C5 inhibitor OmCI to C5 resulted in stabilization of the global conformation of C5 but did not block the convertase cleavage site.
18536718	1	23	theme	A	253:253	arg1	resolution					235:244	a resolution	233:244	a resolution of 3.1 A	233:253	To provide insight into the structural and functional properties of human complement component 5 (C5), we determined its crystal structure at a resolution of 3.1 A.
18536718	3	24	theme	C5	548:549	arg1	core					540:543	the core	536:543	the core of C5	536:549	However, in contrast to C3, the convertase cleavage site in C5 was ordered and the C345C domain flexibly attached to the core of C5.
18536718	4	25	theme	cleavage	688:695	arg1	site					697:700	the convertase cleavage site	673:700	the convertase cleavage site	673:700	Binding of the tick C5 inhibitor OmCI to C5 resulted in stabilization of the global conformation of C5 but did not block the convertase cleavage site.
18536718	1	26	theme	C5	189:190	arg1	properties					145:154	the structural and functional properties	115:154	the structural and functional properties of human complement component 5 (C5)	115:191	To provide insight into the structural and functional properties of human complement component 5 (C5), we determined its crystal structure at a resolution of 3.1 A.
18536718	3	27	theme	C345C	502:506	arg1	domain					508:513	the C345C domain	498:513	the C345C domain	498:513	However, in contrast to C3, the convertase cleavage site in C5 was ordered and the C345C domain flexibly attached to the core of C5.
18536718	5	28	theme	C5	720:721	arg1	structure					707:715	The structure	703:715	The structure of C5	703:721	The structure of C5 may render possible a structure-based approach for the design of new selective complement inhibitors.
18536718	0	29	theme	complement	37:46	arg1	inhibitor					48:56	a tick complement inhibitor	30:56	a tick complement inhibitor	30:56	Structure of and influence of a tick complement inhibitor on human complement component 5.
18536718	5	30	theme	structure-based	745:759	arg1	approach					761:768	possible a structure-based approach	734:768	possible a structure-based approach for the design of new selective complement inhibitors	734:822	The structure of C5 may render possible a structure-based approach for the design of new selective complement inhibitors.
18536718	0	31	theme	tick	32:35	arg1	inhibitor					48:56	a tick complement inhibitor	30:56	a tick complement inhibitor	30:56	Structure of and influence of a tick complement inhibitor on human complement component 5.
18536718	3	32	from	site	471:474	arg1	C5					479:480	C5	479:480	C5	479:480	However, in contrast to C3, the convertase cleavage site in C5 was ordered and the C345C domain flexibly attached to the core of C5.
18536718	4	33	theme	convertase	677:686	arg1	site					697:700	the convertase cleavage site	673:700	the convertase cleavage site	673:700	Binding of the tick C5 inhibitor OmCI to C5 resulted in stabilization of the global conformation of C5 but did not block the convertase cleavage site.
18536718	5	34	theme	new	788:790	arg1	inhibitors					813:822	new selective complement inhibitors	788:822	new selective complement inhibitors	788:822	The structure of C5 may render possible a structure-based approach for the design of new selective complement inhibitors.
18536718	3	35	attach	attached	524:531	arg2	domain					508:513	the C345C domain	498:513	the C345C domain	498:513	However, in contrast to C3, the convertase cleavage site in C5 was ordered and the C345C domain flexibly attached to the core of C5.
18536718	3	35	attach	attached	524:531	arg1	core					540:543	the core	536:543	the core of C5	536:549	However, in contrast to C3, the convertase cleavage site in C5 was ordered and the C345C domain flexibly attached to the core of C5.
18536718	2	36	theme	C5	268:269	arg1	core					260:263	The core	256:263	The core of C5	256:269	The core of C5 adopted a structure resembling that of C3, with the domain arrangement at the position corresponding to the C3 thioester being very well conserved.
18536718	0	37	from	component	78:86	arg1	Structure					0:8	Structure	0:8	Structure of and influence of a tick complement inhibitor on human complement component 5.	0:89	Structure of and influence of a tick complement inhibitor on human complement component 5.
18536718	1	38	theme	structural	119:128	arg1	properties					145:154	the structural and functional properties	115:154	the structural and functional properties of human complement component 5 (C5)	115:191	To provide insight into the structural and functional properties of human complement component 5 (C5), we determined its crystal structure at a resolution of 3.1 A.
18536718	0	39	theme	inhibitor	48:56	arg1	influence					17:25	and influence	13:25	influence	17:25	Structure of and influence of a tick complement inhibitor on human complement component 5.
18536718	0	40	from	influence	17:25	arg1	component					78:86	human complement component 5	61:88	human complement component 5	61:88	Structure of and influence of a tick complement inhibitor on human complement component 5.
18536718	2	41	from	position	349:356	arg1	arrangement					330:340	the domain arrangement	319:340	the domain arrangement at the position corresponding to the C3 thioester	319:390	The core of C5 adopted a structure resembling that of C3, with the domain arrangement at the position corresponding to the C3 thioester being very well conserved.
18536718	4	42	theme	tick	567:570	arg1	OmCI					585:588	the tick C5 inhibitor OmCI	563:588	the tick C5 inhibitor OmCI	563:588	Binding of the tick C5 inhibitor OmCI to C5 resulted in stabilization of the global conformation of C5 but did not block the convertase cleavage site.
21217642	3	0	with	complex	537:543	arg1	C5					550:551	C5	550:551	C5	550:551	We determined the crystal structures of the C3b homologue cobra venom factor (CVF) in complex with C5, and in complex with C5 and the inhibitor SSL7 at 4.3 Å resolution.
21217642	3	0	with	complex	537:543	arg1	SSL7					571:574	the inhibitor SSL7	557:574	the inhibitor SSL7 at 4.3 Å resolution	557:594	We determined the crystal structures of the C3b homologue cobra venom factor (CVF) in complex with C5, and in complex with C5 and the inhibitor SSL7 at 4.3 Å resolution.
21217642	2	1	contain	contain	313:319	arg1	complex					382:388	complex	382:388	complex with a protease subunit (Bb or C2a)	382:424	These contain a non-catalytic substrate contacting subunit (C3b or C4b) in complex with a protease subunit (Bb or C2a).
21217642	2	1	contain	contain	313:319	arg1	These					307:311	These	307:311	These	307:311	These contain a non-catalytic substrate contacting subunit (C3b or C4b) in complex with a protease subunit (Bb or C2a).
21217642	2	1	contain	contain	313:319	arg2	subunit					358:364	a non-catalytic substrate contacting subunit	321:364	a non-catalytic substrate contacting subunit (C3b or C4b)	321:377	These contain a non-catalytic substrate contacting subunit (C3b or C4b) in complex with a protease subunit (Bb or C2a).
21217642	2	1	contain	contain	313:319	arg2	These					307:311	These	307:311	These	307:311	These contain a non-catalytic substrate contacting subunit (C3b or C4b) in complex with a protease subunit (Bb or C2a).
21217642	4	2	theme	C5	804:805	arg1	cleavage					807:814	C5 cleavage	804:814	C5 cleavage	804:814	The structures reveal a parallel two-point attachment between C5 and CVF, where the presence of SSL7 only slightly affects the C5-CVF interface, explaining the IgA dependence for SSL7-mediated inhibition of C5 cleavage.
21217642	1	3	theme	immune	152:157	arg1	system					159:164	the innate immune system	141:164	the innate immune system	141:164	Complement acts as a danger-sensing system in the innate immune system, and its activation initiates a strong inflammatory response and cleavage of the proteins C3 and C5 by proteolytic enzymes, the convertases.
21217642	0	4	theme	factor	79:84	arg1	complex					86:92	the C5-cobra venom factor complex	60:92	the C5-cobra venom factor complex	60:92	Substrate recognition by complement convertases revealed in the C5-cobra venom factor complex.
21217642	4	5	theme	IgA	757:759	arg1	dependence					761:770	the IgA dependence	753:770	the IgA dependence for SSL7-mediated inhibition of C5 cleavage	753:814	The structures reveal a parallel two-point attachment between C5 and CVF, where the presence of SSL7 only slightly affects the C5-CVF interface, explaining the IgA dependence for SSL7-mediated inhibition of C5 cleavage.
21217642	3	6	from	structures	453:462	arg1	complex					513:519	complex	513:519	complex with C5	513:527	We determined the crystal structures of the C3b homologue cobra venom factor (CVF) in complex with C5, and in complex with C5 and the inhibitor SSL7 at 4.3 Å resolution.
21217642	3	6	from	structures	453:462	arg1	complex					537:543	complex	537:543	complex with C5 and the inhibitor SSL7 at 4.3 Å resolution	537:594	We determined the crystal structures of the C3b homologue cobra venom factor (CVF) in complex with C5, and in complex with C5 and the inhibitor SSL7 at 4.3 Å resolution.
21217642	2	7	theme	substrate	337:345	arg1	subunit					358:364	a non-catalytic substrate contacting subunit	321:364	a non-catalytic substrate contacting subunit (C3b or C4b)	321:377	These contain a non-catalytic substrate contacting subunit (C3b or C4b) in complex with a protease subunit (Bb or C2a).
21217642	1	8	theme	proteins	247:254	arg1	cleavage					231:238	cleavage	231:238	cleavage of the proteins C3 and C5 by proteolytic enzymes, the convertases	231:304	Complement acts as a danger-sensing system in the innate immune system, and its activation initiates a strong inflammatory response and cleavage of the proteins C3 and C5 by proteolytic enzymes, the convertases.
21217642	1	8	theme	proteins	247:254	arg1	system					131:136	a danger-sensing system	114:136	a danger-sensing system in the innate immune system	114:164	Complement acts as a danger-sensing system in the innate immune system, and its activation initiates a strong inflammatory response and cleavage of the proteins C3 and C5 by proteolytic enzymes, the convertases.
21217642	1	8	theme	proteins	247:254	arg1	response					218:225	a strong inflammatory response	196:225	a strong inflammatory response	196:225	Complement acts as a danger-sensing system in the innate immune system, and its activation initiates a strong inflammatory response and cleavage of the proteins C3 and C5 by proteolytic enzymes, the convertases.
21217642	1	8	theme	proteins	247:254	arg1	Complement					95:104	Complement	95:104	Complement	95:104	Complement acts as a danger-sensing system in the innate immune system, and its activation initiates a strong inflammatory response and cleavage of the proteins C3 and C5 by proteolytic enzymes, the convertases.
21217642	3	9	with	complex	513:519	arg1	C5					526:527	C5	526:527	C5	526:527	We determined the crystal structures of the C3b homologue cobra venom factor (CVF) in complex with C5, and in complex with C5 and the inhibitor SSL7 at 4.3 Å resolution.
21217642	4	10	theme	SSL7-mediated	776:788	arg1	inhibition					790:799	SSL7-mediated inhibition	776:799	SSL7-mediated inhibition of C5 cleavage	776:814	The structures reveal a parallel two-point attachment between C5 and CVF, where the presence of SSL7 only slightly affects the C5-CVF interface, explaining the IgA dependence for SSL7-mediated inhibition of C5 cleavage.
21217642	3	11	theme	venom	491:495	arg1	CVF					505:507	CVF	505:507	CVF	505:507	We determined the crystal structures of the C3b homologue cobra venom factor (CVF) in complex with C5, and in complex with C5 and the inhibitor SSL7 at 4.3 Å resolution.
21217642	3	11	theme	venom	491:495	arg1	factor					497:502	homologue cobra venom factor	475:502	the C3b homologue cobra venom factor (CVF)	467:508	We determined the crystal structures of the C3b homologue cobra venom factor (CVF) in complex with C5, and in complex with C5 and the inhibitor SSL7 at 4.3 Å resolution.
21217642	5	12	theme	binding	853:859	arg1	CVF					817:819	CVF	817:819	CVF	817:819	CVF functions as a relatively rigid binding scaffold inducing a conformational change in C5, which positions its cleavage site in proximity to the serine protease Bb.
21217642	5	12	theme	binding	853:859	arg1	scaffold					861:868	a relatively rigid binding scaffold	834:868	a relatively rigid binding scaffold inducing a conformational change in C5, which positions its cleavage site in proximity to the serine protease Bb	834:981	CVF functions as a relatively rigid binding scaffold inducing a conformational change in C5, which positions its cleavage site in proximity to the serine protease Bb.
21217642	2	13	with	complex	382:388	arg1	subunit					406:412	a protease subunit	395:412	a protease subunit (Bb or C2a)	395:424	These contain a non-catalytic substrate contacting subunit (C3b or C4b) in complex with a protease subunit (Bb or C2a).
21217642	2	14	theme	contacting	347:356	arg1	subunit					358:364	a non-catalytic substrate contacting subunit	321:364	a non-catalytic substrate contacting subunit (C3b or C4b)	321:377	These contain a non-catalytic substrate contacting subunit (C3b or C4b) in complex with a protease subunit (Bb or C2a).
21217642	4	15	theme	parallel	621:628	arg1	attachment					640:649	a parallel two-point attachment	619:649	a parallel two-point attachment	619:649	The structures reveal a parallel two-point attachment between C5 and CVF, where the presence of SSL7 only slightly affects the C5-CVF interface, explaining the IgA dependence for SSL7-mediated inhibition of C5 cleavage.
21217642	2	16	dep	subunit	406:412	arg1	C2a					421:423	C2a	421:423	C2a	421:423	These contain a non-catalytic substrate contacting subunit (C3b or C4b) in complex with a protease subunit (Bb or C2a).
21217642	2	16	dep	subunit	406:412	arg1	Bb					415:416	Bb	415:416	Bb	415:416	These contain a non-catalytic substrate contacting subunit (C3b or C4b) in complex with a protease subunit (Bb or C2a).
21217642	3	17	theme	homologue	475:483	arg1	CVF					505:507	CVF	505:507	CVF	505:507	We determined the crystal structures of the C3b homologue cobra venom factor (CVF) in complex with C5, and in complex with C5 and the inhibitor SSL7 at 4.3 Å resolution.
21217642	3	17	theme	homologue	475:483	arg1	factor					497:502	homologue cobra venom factor	475:502	the C3b homologue cobra venom factor (CVF)	467:508	We determined the crystal structures of the C3b homologue cobra venom factor (CVF) in complex with C5, and in complex with C5 and the inhibitor SSL7 at 4.3 Å resolution.
21217642	1	18	from	system	131:136	arg1	system					159:164	the innate immune system	141:164	the innate immune system	141:164	Complement acts as a danger-sensing system in the innate immune system, and its activation initiates a strong inflammatory response and cleavage of the proteins C3 and C5 by proteolytic enzymes, the convertases.
21217642	2	19	dep	subunit	358:364	arg1	C4b					374:376	C4b	374:376	C4b	374:376	These contain a non-catalytic substrate contacting subunit (C3b or C4b) in complex with a protease subunit (Bb or C2a).
21217642	2	19	dep	subunit	358:364	arg1	C3b					367:369	C3b	367:369	C3b	367:369	These contain a non-catalytic substrate contacting subunit (C3b or C4b) in complex with a protease subunit (Bb or C2a).
21217642	5	20	from	change	896:901	arg1	C5					906:907	C5	906:907	C5	906:907	CVF functions as a relatively rigid binding scaffold inducing a conformational change in C5, which positions its cleavage site in proximity to the serine protease Bb.
21217642	0	21	theme	Substrate	0:8	arg1	recognition					10:20	Substrate recognition	0:20	Substrate recognition by complement convertases	0:46	Substrate recognition by complement convertases revealed in the C5-cobra venom factor complex.
21217642	5	22	theme	conformational	881:894	arg1	change					896:901	a conformational change	879:901	a conformational change	879:901	CVF functions as a relatively rigid binding scaffold inducing a conformational change in C5, which positions its cleavage site in proximity to the serine protease Bb.
21217642	5	23	theme	serine	964:969	arg1	Bb					980:981	the serine protease Bb	960:981	the serine protease Bb	960:981	CVF functions as a relatively rigid binding scaffold inducing a conformational change in C5, which positions its cleavage site in proximity to the serine protease Bb.
21217642	0	24	theme	complement	25:34	arg1	convertases					36:46	complement convertases	25:46	complement convertases	25:46	Substrate recognition by complement convertases revealed in the C5-cobra venom factor complex.
21217642	5	25	theme	rigid	847:851	arg1	CVF					817:819	CVF	817:819	CVF	817:819	CVF functions as a relatively rigid binding scaffold inducing a conformational change in C5, which positions its cleavage site in proximity to the serine protease Bb.
21217642	5	25	theme	rigid	847:851	arg1	scaffold					861:868	a relatively rigid binding scaffold	834:868	a relatively rigid binding scaffold inducing a conformational change in C5, which positions its cleavage site in proximity to the serine protease Bb	834:981	CVF functions as a relatively rigid binding scaffold inducing a conformational change in C5, which positions its cleavage site in proximity to the serine protease Bb.
21217642	2	26	theme	protease	397:404	arg1	subunit					406:412	a protease subunit	395:412	a protease subunit (Bb or C2a)	395:424	These contain a non-catalytic substrate contacting subunit (C3b or C4b) in complex with a protease subunit (Bb or C2a).
21217642	1	27	theme	proteolytic	269:279	arg1	enzymes					281:287	proteolytic enzymes	269:287	proteolytic enzymes	269:287	Complement acts as a danger-sensing system in the innate immune system, and its activation initiates a strong inflammatory response and cleavage of the proteins C3 and C5 by proteolytic enzymes, the convertases.
21217642	1	27	theme	proteolytic	269:279	arg1	convertases					294:304	the convertases	290:304	the convertases	290:304	Complement acts as a danger-sensing system in the innate immune system, and its activation initiates a strong inflammatory response and cleavage of the proteins C3 and C5 by proteolytic enzymes, the convertases.
21217642	3	28	dep	C3b	471:473	arg1	CVF					505:507	CVF	505:507	CVF	505:507	We determined the crystal structures of the C3b homologue cobra venom factor (CVF) in complex with C5, and in complex with C5 and the inhibitor SSL7 at 4.3 Å resolution.
21217642	3	28	dep	C3b	471:473	arg1	factor					497:502	homologue cobra venom factor	475:502	the C3b homologue cobra venom factor (CVF)	467:508	We determined the crystal structures of the C3b homologue cobra venom factor (CVF) in complex with C5, and in complex with C5 and the inhibitor SSL7 at 4.3 Å resolution.
21217642	3	29	from	resolution	585:594	arg1	C5					550:551	C5	550:551	C5	550:551	We determined the crystal structures of the C3b homologue cobra venom factor (CVF) in complex with C5, and in complex with C5 and the inhibitor SSL7 at 4.3 Å resolution.
21217642	3	29	from	resolution	585:594	arg1	SSL7					571:574	the inhibitor SSL7	557:574	the inhibitor SSL7 at 4.3 Å resolution	557:594	We determined the crystal structures of the C3b homologue cobra venom factor (CVF) in complex with C5, and in complex with C5 and the inhibitor SSL7 at 4.3 Å resolution.
21217642	3	30	theme	crystal	445:451	arg1	structures					453:462	the crystal structures	441:462	the crystal structures of the C3b homologue cobra venom factor (CVF) in complex with C5, and in complex with C5 and the inhibitor SSL7 at 4.3 Å resolution	441:594	We determined the crystal structures of the C3b homologue cobra venom factor (CVF) in complex with C5, and in complex with C5 and the inhibitor SSL7 at 4.3 Å resolution.
21217642	3	31	theme	inhibitor	561:569	arg1	SSL7					571:574	the inhibitor SSL7	557:574	the inhibitor SSL7 at 4.3 Å resolution	557:594	We determined the crystal structures of the C3b homologue cobra venom factor (CVF) in complex with C5, and in complex with C5 and the inhibitor SSL7 at 4.3 Å resolution.
21217642	1	32	theme	strong	198:203	arg1	system					131:136	a danger-sensing system	114:136	a danger-sensing system in the innate immune system	114:164	Complement acts as a danger-sensing system in the innate immune system, and its activation initiates a strong inflammatory response and cleavage of the proteins C3 and C5 by proteolytic enzymes, the convertases.
21217642	1	32	theme	strong	198:203	arg1	Complement					95:104	Complement	95:104	Complement	95:104	Complement acts as a danger-sensing system in the innate immune system, and its activation initiates a strong inflammatory response and cleavage of the proteins C3 and C5 by proteolytic enzymes, the convertases.
21217642	1	32	theme	strong	198:203	arg1	response					218:225	a strong inflammatory response	196:225	a strong inflammatory response	196:225	Complement acts as a danger-sensing system in the innate immune system, and its activation initiates a strong inflammatory response and cleavage of the proteins C3 and C5 by proteolytic enzymes, the convertases.
21217642	1	32	theme	strong	198:203	arg1	cleavage					231:238	cleavage	231:238	cleavage of the proteins C3 and C5 by proteolytic enzymes, the convertases	231:304	Complement acts as a danger-sensing system in the innate immune system, and its activation initiates a strong inflammatory response and cleavage of the proteins C3 and C5 by proteolytic enzymes, the convertases.
21217642	7	33	theme	Prior	1106:1110	arg1	knowledge					1112:1120	Prior knowledge	1106:1120	Prior knowledge concerning interactions between the endogenous convertases and their substrates	1106:1200	Prior knowledge concerning interactions between the endogenous convertases and their substrates is rationalized by this model.
21217642	5	34	theme	protease	971:978	arg1	Bb					980:981	the serine protease Bb	960:981	the serine protease Bb	960:981	CVF functions as a relatively rigid binding scaffold inducing a conformational change in C5, which positions its cleavage site in proximity to the serine protease Bb.
21217642	1	35	theme	inflammatory	205:216	arg1	system					131:136	a danger-sensing system	114:136	a danger-sensing system in the innate immune system	114:164	Complement acts as a danger-sensing system in the innate immune system, and its activation initiates a strong inflammatory response and cleavage of the proteins C3 and C5 by proteolytic enzymes, the convertases.
21217642	1	35	theme	inflammatory	205:216	arg1	Complement					95:104	Complement	95:104	Complement	95:104	Complement acts as a danger-sensing system in the innate immune system, and its activation initiates a strong inflammatory response and cleavage of the proteins C3 and C5 by proteolytic enzymes, the convertases.
21217642	1	35	theme	inflammatory	205:216	arg1	response					218:225	a strong inflammatory response	196:225	a strong inflammatory response	196:225	Complement acts as a danger-sensing system in the innate immune system, and its activation initiates a strong inflammatory response and cleavage of the proteins C3 and C5 by proteolytic enzymes, the convertases.
21217642	1	35	theme	inflammatory	205:216	arg1	cleavage					231:238	cleavage	231:238	cleavage of the proteins C3 and C5 by proteolytic enzymes, the convertases	231:304	Complement acts as a danger-sensing system in the innate immune system, and its activation initiates a strong inflammatory response and cleavage of the proteins C3 and C5 by proteolytic enzymes, the convertases.
21217642	4	36	theme	C5-CVF	724:729	arg1	interface					731:739	the C5-CVF interface	720:739	the C5-CVF interface	720:739	The structures reveal a parallel two-point attachment between C5 and CVF, where the presence of SSL7 only slightly affects the C5-CVF interface, explaining the IgA dependence for SSL7-mediated inhibition of C5 cleavage.
21217642	6	37	theme	general	986:992	arg1	model					994:998	A general model	984:998	A general model for substrate recognition by the convertases	984:1043	A general model for substrate recognition by the convertases is presented based on the C5-CVF and C3b-Bb-SCIN structures.
21217642	2	38	theme	non-catalytic	323:335	arg1	subunit					358:364	a non-catalytic substrate contacting subunit	321:364	a non-catalytic substrate contacting subunit (C3b or C4b)	321:377	These contain a non-catalytic substrate contacting subunit (C3b or C4b) in complex with a protease subunit (Bb or C2a).
21217642	5	39	theme	cleavage	930:937	arg1	site					939:942	its cleavage site	926:942	its cleavage site	926:942	CVF functions as a relatively rigid binding scaffold inducing a conformational change in C5, which positions its cleavage site in proximity to the serine protease Bb.
21217642	1	40	theme	danger-sensing	116:129	arg1	system					131:136	a danger-sensing system	114:136	a danger-sensing system in the innate immune system	114:164	Complement acts as a danger-sensing system in the innate immune system, and its activation initiates a strong inflammatory response and cleavage of the proteins C3 and C5 by proteolytic enzymes, the convertases.
21217642	1	40	theme	danger-sensing	116:129	arg1	Complement					95:104	Complement	95:104	Complement	95:104	Complement acts as a danger-sensing system in the innate immune system, and its activation initiates a strong inflammatory response and cleavage of the proteins C3 and C5 by proteolytic enzymes, the convertases.
21217642	1	40	theme	danger-sensing	116:129	arg1	response					218:225	a strong inflammatory response	196:225	a strong inflammatory response	196:225	Complement acts as a danger-sensing system in the innate immune system, and its activation initiates a strong inflammatory response and cleavage of the proteins C3 and C5 by proteolytic enzymes, the convertases.
21217642	1	40	theme	danger-sensing	116:129	arg1	cleavage					231:238	cleavage	231:238	cleavage of the proteins C3 and C5 by proteolytic enzymes, the convertases	231:304	Complement acts as a danger-sensing system in the innate immune system, and its activation initiates a strong inflammatory response and cleavage of the proteins C3 and C5 by proteolytic enzymes, the convertases.
21217642	4	41	theme	cleavage	807:814	arg1	inhibition					790:799	SSL7-mediated inhibition	776:799	SSL7-mediated inhibition of C5 cleavage	776:814	The structures reveal a parallel two-point attachment between C5 and CVF, where the presence of SSL7 only slightly affects the C5-CVF interface, explaining the IgA dependence for SSL7-mediated inhibition of C5 cleavage.
21217642	3	42	theme	Å	583:583	arg1	resolution					585:594	4.3 Å resolution	579:594	4.3 Å resolution	579:594	We determined the crystal structures of the C3b homologue cobra venom factor (CVF) in complex with C5, and in complex with C5 and the inhibitor SSL7 at 4.3 Å resolution.
21217642	4	43	theme	two-point	630:638	arg1	attachment					640:649	a parallel two-point attachment	619:649	a parallel two-point attachment	619:649	The structures reveal a parallel two-point attachment between C5 and CVF, where the presence of SSL7 only slightly affects the C5-CVF interface, explaining the IgA dependence for SSL7-mediated inhibition of C5 cleavage.
21217642	3	44	theme	cobra	485:489	arg1	CVF					505:507	CVF	505:507	CVF	505:507	We determined the crystal structures of the C3b homologue cobra venom factor (CVF) in complex with C5, and in complex with C5 and the inhibitor SSL7 at 4.3 Å resolution.
21217642	3	44	theme	cobra	485:489	arg1	factor					497:502	homologue cobra venom factor	475:502	the C3b homologue cobra venom factor (CVF)	467:508	We determined the crystal structures of the C3b homologue cobra venom factor (CVF) in complex with C5, and in complex with C5 and the inhibitor SSL7 at 4.3 Å resolution.
21217642	6	45	theme	C5-CVF	1071:1076	arg1	structures					1094:1103	the C5-CVF and C3b-Bb-SCIN structures	1067:1103	the C5-CVF and C3b-Bb-SCIN structures	1067:1103	A general model for substrate recognition by the convertases is presented based on the C5-CVF and C3b-Bb-SCIN structures.
21217642	3	46	theme	C3b	471:473	arg1	structures					453:462	the crystal structures	441:462	the crystal structures of the C3b homologue cobra venom factor (CVF) in complex with C5, and in complex with C5 and the inhibitor SSL7 at 4.3 Å resolution	441:594	We determined the crystal structures of the C3b homologue cobra venom factor (CVF) in complex with C5, and in complex with C5 and the inhibitor SSL7 at 4.3 Å resolution.
21217642	6	47	theme	substrate	1004:1012	arg1	recognition					1014:1024	substrate recognition	1004:1024	substrate recognition by the convertases	1004:1043	A general model for substrate recognition by the convertases is presented based on the C5-CVF and C3b-Bb-SCIN structures.
21217642	0	48	theme	venom	73:77	arg1	complex					86:92	the C5-cobra venom factor complex	60:92	the C5-cobra venom factor complex	60:92	Substrate recognition by complement convertases revealed in the C5-cobra venom factor complex.
21217642	1	49	dep	proteins	247:254	arg1	proteins					247:254	the proteins C3 and C5	243:264	the proteins C3 and C5	243:264	Complement acts as a danger-sensing system in the innate immune system, and its activation initiates a strong inflammatory response and cleavage of the proteins C3 and C5 by proteolytic enzymes, the convertases.
21217642	1	49	dep	proteins	247:254	arg1	C5					263:264	C5	263:264	C5	263:264	Complement acts as a danger-sensing system in the innate immune system, and its activation initiates a strong inflammatory response and cleavage of the proteins C3 and C5 by proteolytic enzymes, the convertases.
21217642	1	49	dep	proteins	247:254	arg1	C3					256:257	C3	256:257	C3	256:257	Complement acts as a danger-sensing system in the innate immune system, and its activation initiates a strong inflammatory response and cleavage of the proteins C3 and C5 by proteolytic enzymes, the convertases.
21217642	6	50	theme	C3b-Bb-SCIN	1082:1092	arg1	structures					1094:1103	the C5-CVF and C3b-Bb-SCIN structures	1067:1103	the C5-CVF and C3b-Bb-SCIN structures	1067:1103	A general model for substrate recognition by the convertases is presented based on the C5-CVF and C3b-Bb-SCIN structures.
21217642	7	51	theme	endogenous	1158:1167	arg1	convertases					1169:1179	the endogenous convertases	1154:1179	the endogenous convertases	1154:1179	Prior knowledge concerning interactions between the endogenous convertases and their substrates is rationalized by this model.
21217642	0	52	theme	C5-cobra	64:71	arg1	complex					86:92	the C5-cobra venom factor complex	60:92	the C5-cobra venom factor complex	60:92	Substrate recognition by complement convertases revealed in the C5-cobra venom factor complex.
21217642	4	53	theme	SSL7	693:696	arg1	presence					681:688	the presence	677:688	the presence of SSL7	677:696	The structures reveal a parallel two-point attachment between C5 and CVF, where the presence of SSL7 only slightly affects the C5-CVF interface, explaining the IgA dependence for SSL7-mediated inhibition of C5 cleavage.
21217642	1	54	theme	innate	145:150	arg1	system					159:164	the innate immune system	141:164	the innate immune system	141:164	Complement acts as a danger-sensing system in the innate immune system, and its activation initiates a strong inflammatory response and cleavage of the proteins C3 and C5 by proteolytic enzymes, the convertases.
17027507	0	0	theme	substrate	81:89	arg1	binding					91:97	substrate binding	81:97	substrate binding	81:97	Structure of complement component C2A: implications for convertase formation and substrate binding.
17027507	7	1	theme	substrate	1090:1098	arg1	specificity					1100:1110	the high substrate specificity	1081:1110	the high substrate specificity of the convertases	1081:1129	Together with a putative substrate-induced completion of the oxyanion hole, this may contribute to the high substrate specificity of the convertases.
17027507	3	2	theme	activation	507:516	arg1	state					518:522	an intermediate activation state	491:522	an intermediate activation state of helix alpha7 with an open, activated metal-ion-dependent adhesion site	491:596	Both structures reveal a near-active conformation of the catalytic center of the serine protease domains, while the von Willebrand factor A-type domains display an intermediate activation state of helix alpha7 with an open, activated metal-ion-dependent adhesion site.
17027507	0	3	theme	complement	13:22	arg1	C2A					34:36	complement component C2A	13:36	complement component C2A	13:36	Structure of complement component C2A: implications for convertase formation and substrate binding.
17027507	6	4	theme	C3	978:979	arg1	C3					978:979	the substrate C3	964:979	the substrate C3	964:979	Extended loops on the protease domain possibly envelop the protruding anaphylatoxin domain of the substrate C3.
17027507	6	4	theme	C3	978:979	arg1	domain					954:959	the protruding anaphylatoxin domain	925:959	the protruding anaphylatoxin domain of the substrate C3	925:979	Extended loops on the protease domain possibly envelop the protruding anaphylatoxin domain of the substrate C3.
17027507	5	5	theme	C2a	769:771	arg1	C2a					769:771	C2a	769:771	C2a	769:771	Surprisingly, the N-terminal residues of C2a are buried in a crevice near helix alpha7, indicative of a structural switch between C2 and C2a.
17027507	5	5	theme	C2a	769:771	arg1	residues					757:764	the N-terminal residues	742:764	the N-terminal residues of C2a	742:771	Surprisingly, the N-terminal residues of C2a are buried in a crevice near helix alpha7, indicative of a structural switch between C2 and C2a.
17027507	6	6	theme	substrate	968:976	arg1	C3					978:979	the substrate C3	964:979	the substrate C3	964:979	Extended loops on the protease domain possibly envelop the protruding anaphylatoxin domain of the substrate C3.
17027507	3	7	theme	near-active	355:365	arg1	conformation					367:378	a near-active conformation	353:378	a near-active conformation of the catalytic center of the serine protease domains	353:433	Both structures reveal a near-active conformation of the catalytic center of the serine protease domains, while the von Willebrand factor A-type domains display an intermediate activation state of helix alpha7 with an open, activated metal-ion-dependent adhesion site.
17027507	6	8	theme	Extended	870:877	arg1	loops					879:883	Extended loops	870:883	Extended loops on the protease domain	870:906	Extended loops on the protease domain possibly envelop the protruding anaphylatoxin domain of the substrate C3.
17027507	4	9	theme	open	603:606	arg1	site					617:620	The open adhesion site	599:620	The open adhesion site	599:620	The open adhesion site likely serves to enhance the affinity for the ligand C4b, similar to "inside-out" signaling in integrins.
17027507	7	10	theme	high	1085:1088	arg1	specificity					1100:1110	the high substrate specificity	1081:1110	the high substrate specificity of the convertases	1081:1129	Together with a putative substrate-induced completion of the oxyanion hole, this may contribute to the high substrate specificity of the convertases.
17027507	7	11	theme	convertases	1119:1129	arg1	specificity					1100:1110	the high substrate specificity	1081:1110	the high substrate specificity of the convertases	1081:1129	Together with a putative substrate-induced completion of the oxyanion hole, this may contribute to the high substrate specificity of the convertases.
17027507	3	12	theme	open	548:551	arg1	site					593:596	an open, activated metal-ion-dependent adhesion site	545:596	an open, activated metal-ion-dependent adhesion site	545:596	Both structures reveal a near-active conformation of the catalytic center of the serine protease domains, while the von Willebrand factor A-type domains display an intermediate activation state of helix alpha7 with an open, activated metal-ion-dependent adhesion site.
17027507	3	13	dep	open	548:551	arg1	activated					554:562	activated	554:562	activated	554:562	Both structures reveal a near-active conformation of the catalytic center of the serine protease domains, while the von Willebrand factor A-type domains display an intermediate activation state of helix alpha7 with an open, activated metal-ion-dependent adhesion site.
17027507	5	14	theme	indicative	816:825	arg1	alpha7					808:813	helix alpha7	802:813	helix alpha7	802:813	Surprisingly, the N-terminal residues of C2a are buried in a crevice near helix alpha7, indicative of a structural switch between C2 and C2a.
17027507	3	15	theme	alpha7	533:538	arg1	state					518:522	an intermediate activation state	491:522	an intermediate activation state of helix alpha7 with an open, activated metal-ion-dependent adhesion site	491:596	Both structures reveal a near-active conformation of the catalytic center of the serine protease domains, while the von Willebrand factor A-type domains display an intermediate activation state of helix alpha7 with an open, activated metal-ion-dependent adhesion site.
17027507	5	16	theme	switch	843:848	arg1	indicative					816:825	indicative	816:825	indicative	816:825	Surprisingly, the N-terminal residues of C2a are buried in a crevice near helix alpha7, indicative of a structural switch between C2 and C2a.
17027507	3	17	with	alpha7	533:538	arg1	site					593:596	an open, activated metal-ion-dependent adhesion site	545:596	an open, activated metal-ion-dependent adhesion site	545:596	Both structures reveal a near-active conformation of the catalytic center of the serine protease domains, while the von Willebrand factor A-type domains display an intermediate activation state of helix alpha7 with an open, activated metal-ion-dependent adhesion site.
17027507	2	18	theme	C2a	285:287	arg1	structures					259:268	two crystal structures	247:268	two crystal structures of full-length C2a	247:287	We determined two crystal structures of full-length C2a, with and without a pseudo ligand bound.
17027507	1	19	theme	classical	169:177	arg1	pathways					198:205	the classical and lectin-binding pathways	165:205	the classical and lectin-binding pathways of complement activation	165:230	C2a provides the catalytic center to the convertase complexes of the classical and lectin-binding pathways of complement activation.
17027507	3	20	theme	catalytic	387:395	arg1	center					397:402	the catalytic center	383:402	the catalytic center of the serine protease domains	383:433	Both structures reveal a near-active conformation of the catalytic center of the serine protease domains, while the von Willebrand factor A-type domains display an intermediate activation state of helix alpha7 with an open, activated metal-ion-dependent adhesion site.
17027507	3	21	theme	metal-ion-dependent	564:582	arg1	site					593:596	an open, activated metal-ion-dependent adhesion site	545:596	an open, activated metal-ion-dependent adhesion site	545:596	Both structures reveal a near-active conformation of the catalytic center of the serine protease domains, while the von Willebrand factor A-type domains display an intermediate activation state of helix alpha7 with an open, activated metal-ion-dependent adhesion site.
17027507	3	22	theme	domains	427:433	arg1	center					397:402	the catalytic center	383:402	the catalytic center of the serine protease domains	383:433	Both structures reveal a near-active conformation of the catalytic center of the serine protease domains, while the von Willebrand factor A-type domains display an intermediate activation state of helix alpha7 with an open, activated metal-ion-dependent adhesion site.
17027507	3	23	theme	center	397:402	arg1	conformation					367:378	a near-active conformation	353:378	a near-active conformation of the catalytic center of the serine protease domains	353:433	Both structures reveal a near-active conformation of the catalytic center of the serine protease domains, while the von Willebrand factor A-type domains display an intermediate activation state of helix alpha7 with an open, activated metal-ion-dependent adhesion site.
17027507	6	24	theme	protease	892:899	arg1	domain					901:906	the protease domain	888:906	the protease domain	888:906	Extended loops on the protease domain possibly envelop the protruding anaphylatoxin domain of the substrate C3.
17027507	3	25	theme	adhesion	584:591	arg1	site					593:596	an open, activated metal-ion-dependent adhesion site	545:596	an open, activated metal-ion-dependent adhesion site	545:596	Both structures reveal a near-active conformation of the catalytic center of the serine protease domains, while the von Willebrand factor A-type domains display an intermediate activation state of helix alpha7 with an open, activated metal-ion-dependent adhesion site.
17027507	1	26	theme	lectin-binding	183:196	arg1	pathways					198:205	the classical and lectin-binding pathways	165:205	the classical and lectin-binding pathways of complement activation	165:230	C2a provides the catalytic center to the convertase complexes of the classical and lectin-binding pathways of complement activation.
17027507	0	27	theme	component	24:32	arg1	C2A					34:36	complement component C2A	13:36	complement component C2A	13:36	Structure of complement component C2A: implications for convertase formation and substrate binding.
17027507	6	28	theme	anaphylatoxin	940:952	arg1	C3					978:979	the substrate C3	964:979	the substrate C3	964:979	Extended loops on the protease domain possibly envelop the protruding anaphylatoxin domain of the substrate C3.
17027507	6	28	theme	anaphylatoxin	940:952	arg1	domain					954:959	the protruding anaphylatoxin domain	925:959	the protruding anaphylatoxin domain of the substrate C3	925:979	Extended loops on the protease domain possibly envelop the protruding anaphylatoxin domain of the substrate C3.
17027507	7	29	theme	hole	1052:1055	arg1	completion					1025:1034	a putative substrate-induced completion	996:1034	a putative substrate-induced completion of the oxyanion hole	996:1055	Together with a putative substrate-induced completion of the oxyanion hole, this may contribute to the high substrate specificity of the convertases.
17027507	3	30	theme	factor	461:466	arg1	domains					475:481	the von Willebrand factor A-type domains	442:481	the von Willebrand factor A-type domains	442:481	Both structures reveal a near-active conformation of the catalytic center of the serine protease domains, while the von Willebrand factor A-type domains display an intermediate activation state of helix alpha7 with an open, activated metal-ion-dependent adhesion site.
17027507	2	31	theme	pseudo	309:314	arg1	ligand					316:321	a pseudo ligand	307:321	a pseudo ligand bound	307:327	We determined two crystal structures of full-length C2a, with and without a pseudo ligand bound.
17027507	6	32	theme	protruding	929:938	arg1	C3					978:979	the substrate C3	964:979	the substrate C3	964:979	Extended loops on the protease domain possibly envelop the protruding anaphylatoxin domain of the substrate C3.
17027507	6	32	theme	protruding	929:938	arg1	domain					954:959	the protruding anaphylatoxin domain	925:959	the protruding anaphylatoxin domain of the substrate C3	925:979	Extended loops on the protease domain possibly envelop the protruding anaphylatoxin domain of the substrate C3.
17027507	3	33	theme	A-type	468:473	arg1	domains					475:481	the von Willebrand factor A-type domains	442:481	the von Willebrand factor A-type domains	442:481	Both structures reveal a near-active conformation of the catalytic center of the serine protease domains, while the von Willebrand factor A-type domains display an intermediate activation state of helix alpha7 with an open, activated metal-ion-dependent adhesion site.
17027507	3	34	theme	serine	411:416	arg1	domains					427:433	the serine protease domains	407:433	the serine protease domains	407:433	Both structures reveal a near-active conformation of the catalytic center of the serine protease domains, while the von Willebrand factor A-type domains display an intermediate activation state of helix alpha7 with an open, activated metal-ion-dependent adhesion site.
17027507	3	35	theme	intermediate	494:505	arg1	state					518:522	an intermediate activation state	491:522	an intermediate activation state of helix alpha7 with an open, activated metal-ion-dependent adhesion site	491:596	Both structures reveal a near-active conformation of the catalytic center of the serine protease domains, while the von Willebrand factor A-type domains display an intermediate activation state of helix alpha7 with an open, activated metal-ion-dependent adhesion site.
17027507	3	36	theme	von	446:448	arg1	factor					461:466	von Willebrand factor	446:466	the von Willebrand factor A-type domains	442:481	Both structures reveal a near-active conformation of the catalytic center of the serine protease domains, while the von Willebrand factor A-type domains display an intermediate activation state of helix alpha7 with an open, activated metal-ion-dependent adhesion site.
17027507	4	37	theme	ligand	668:673	arg1	C4b					675:677	the ligand C4b	664:677	the ligand C4b	664:677	The open adhesion site likely serves to enhance the affinity for the ligand C4b, similar to "inside-out" signaling in integrins.
17027507	1	38	theme	complement	210:219	arg1	activation					221:230	complement activation	210:230	complement activation	210:230	C2a provides the catalytic center to the convertase complexes of the classical and lectin-binding pathways of complement activation.
17027507	0	39	theme	C2A	34:36	arg1	Structure					0:8	Structure	0:8	Structure of complement component C2A: implications for convertase formation and substrate binding.	0:98	Structure of complement component C2A: implications for convertase formation and substrate binding.
17027507	3	40	theme	protease	418:425	arg1	domains					427:433	the serine protease domains	407:433	the serine protease domains	407:433	Both structures reveal a near-active conformation of the catalytic center of the serine protease domains, while the von Willebrand factor A-type domains display an intermediate activation state of helix alpha7 with an open, activated metal-ion-dependent adhesion site.
17027507	1	41	theme	activation	221:230	arg1	pathways					198:205	the classical and lectin-binding pathways	165:205	the classical and lectin-binding pathways of complement activation	165:230	C2a provides the catalytic center to the convertase complexes of the classical and lectin-binding pathways of complement activation.
17027507	5	42	theme	N-terminal	746:755	arg1	C2a					769:771	C2a	769:771	C2a	769:771	Surprisingly, the N-terminal residues of C2a are buried in a crevice near helix alpha7, indicative of a structural switch between C2 and C2a.
17027507	5	42	theme	N-terminal	746:755	arg1	residues					757:764	the N-terminal residues	742:764	the N-terminal residues of C2a	742:771	Surprisingly, the N-terminal residues of C2a are buried in a crevice near helix alpha7, indicative of a structural switch between C2 and C2a.
17027507	4	43	theme	"	702:702	arg1	signaling					704:712	"inside-out" signaling	691:712	"inside-out" signaling in integrins	691:725	The open adhesion site likely serves to enhance the affinity for the ligand C4b, similar to "inside-out" signaling in integrins.
17027507	7	44	theme	oxyanion	1043:1050	arg1	hole					1052:1055	the oxyanion hole	1039:1055	the oxyanion hole	1039:1055	Together with a putative substrate-induced completion of the oxyanion hole, this may contribute to the high substrate specificity of the convertases.
17027507	1	45	theme	catalytic	117:125	arg1	center					127:132	the catalytic center	113:132	the catalytic center to the convertase complexes of the classical and lectin-binding pathways of complement activation	113:230	C2a provides the catalytic center to the convertase complexes of the classical and lectin-binding pathways of complement activation.
17027507	0	46	dep	Structure	0:8	arg1	implications					39:50	implications	39:50	Structure of complement component C2A: implications for convertase formation and substrate binding.	0:98	Structure of complement component C2A: implications for convertase formation and substrate binding.
17027507	7	47	theme	putative	998:1005	arg1	completion					1025:1034	a putative substrate-induced completion	996:1034	a putative substrate-induced completion of the oxyanion hole	996:1055	Together with a putative substrate-induced completion of the oxyanion hole, this may contribute to the high substrate specificity of the convertases.
17027507	2	48	theme	full-length	273:283	arg1	C2a					285:287	full-length C2a	273:287	full-length C2a	273:287	We determined two crystal structures of full-length C2a, with and without a pseudo ligand bound.
17027507	4	49	from	signaling	704:712	arg1	integrins					717:725	integrins	717:725	integrins	717:725	The open adhesion site likely serves to enhance the affinity for the ligand C4b, similar to "inside-out" signaling in integrins.
17027507	7	50	theme	substrate-induced	1007:1023	arg1	completion					1025:1034	a putative substrate-induced completion	996:1034	a putative substrate-induced completion of the oxyanion hole	996:1055	Together with a putative substrate-induced completion of the oxyanion hole, this may contribute to the high substrate specificity of the convertases.
17027507	5	51	theme	helix	802:806	arg1	alpha7					808:813	helix alpha7	802:813	helix alpha7	802:813	Surprisingly, the N-terminal residues of C2a are buried in a crevice near helix alpha7, indicative of a structural switch between C2 and C2a.
17027507	1	52	theme	convertase	141:150	arg1	complexes					152:160	the convertase complexes	137:160	the convertase complexes of the classical and lectin-binding pathways of complement activation	137:230	C2a provides the catalytic center to the convertase complexes of the classical and lectin-binding pathways of complement activation.
17027507	4	53	theme	adhesion	608:615	arg1	site					617:620	The open adhesion site	599:620	The open adhesion site	599:620	The open adhesion site likely serves to enhance the affinity for the ligand C4b, similar to "inside-out" signaling in integrins.
17027507	6	54	from	loops	879:883	arg1	domain					901:906	the protease domain	888:906	the protease domain	888:906	Extended loops on the protease domain possibly envelop the protruding anaphylatoxin domain of the substrate C3.
17027507	3	55	theme	Willebrand	450:459	arg1	factor					461:466	von Willebrand factor	446:466	the von Willebrand factor A-type domains	442:481	Both structures reveal a near-active conformation of the catalytic center of the serine protease domains, while the von Willebrand factor A-type domains display an intermediate activation state of helix alpha7 with an open, activated metal-ion-dependent adhesion site.
17027507	1	56	theme	pathways	198:205	arg1	complexes					152:160	the convertase complexes	137:160	the convertase complexes of the classical and lectin-binding pathways of complement activation	137:230	C2a provides the catalytic center to the convertase complexes of the classical and lectin-binding pathways of complement activation.
17027507	4	57	theme	similar	680:686	arg1	C4b					675:677	the ligand C4b	664:677	the ligand C4b	664:677	The open adhesion site likely serves to enhance the affinity for the ligand C4b, similar to "inside-out" signaling in integrins.
17027507	5	58	theme	structural	832:841	arg1	switch					843:848	a structural switch	830:848	a structural switch between C2 and C2a	830:867	Surprisingly, the N-terminal residues of C2a are buried in a crevice near helix alpha7, indicative of a structural switch between C2 and C2a.
17027507	0	59	theme	convertase	56:65	arg1	formation					67:75	convertase formation	56:75	convertase formation	56:75	Structure of complement component C2A: implications for convertase formation and substrate binding.
17027507	2	60	theme	crystal	251:257	arg1	structures					259:268	two crystal structures	247:268	two crystal structures of full-length C2a	247:287	We determined two crystal structures of full-length C2a, with and without a pseudo ligand bound.
17027507	3	61	theme	helix	527:531	arg1	alpha7					533:538	helix alpha7	527:538	helix alpha7 with an open, activated metal-ion-dependent adhesion site	527:596	Both structures reveal a near-active conformation of the catalytic center of the serine protease domains, while the von Willebrand factor A-type domains display an intermediate activation state of helix alpha7 with an open, activated metal-ion-dependent adhesion site.
17027507	4	62	theme	inside-out	692:701	arg1	signaling					704:712	"inside-out" signaling	691:712	"inside-out" signaling in integrins	691:725	The open adhesion site likely serves to enhance the affinity for the ligand C4b, similar to "inside-out" signaling in integrins.
1380064	7	0	from	residues	1403:1410	arg1	O-glycosylation					1371:1385	O-glycosylation	1371:1385	O-glycosylation at these serine residues	1371:1410	Upon ESP-MS, EoCP-1 showed an average molecular mass of 8,355 +/- 10 daltons, suggesting O-glycosylation at these serine residues.
1380064	6	1	theme	molecular	1029:1037	arg1	mass					1039:1042	a molecular mass	1027:1042	a molecular mass of 7,862.8 +/- 1.1 daltons, which is 15.8 mass units higher than the calculated value of RANTES, indicating that EoCP-2 is identical to the full-length cytokine, and oxygenation, probably at methionine residue number 64, has taken place	1027:1279	Electrospray mass spectrometry (ESP-MS) of EoCPs revealed for EoCP-2 a molecular mass of 7,862.8 +/- 1.1 daltons, which is 15.8 mass units higher than the calculated value of RANTES, indicating that EoCP-2 is identical to the full-length cytokine, and oxygenation, probably at methionine residue number 64, has taken place.
1380064	8	2	theme	chemotactic	1507:1517	arg1	migration					1519:1527	optimal chemotactic migration	1499:1527	optimal chemotactic migration	1499:1527	Both natural forms of RANTES showed strong Eo-chemotactic activity (ED50 = 2 nM) with optimal chemotactic migration at concentrations near 10 nM, however, there were no significant migratory responses with human neutrophils.
1380064	10	3	theme	lymphocyte-selective	1916:1935	arg1	RANTES					1880:1885	recombinant RANTES	1868:1885	recombinant RANTES	1868:1885	Since RANTES gene expression has been detected in activated T lymphocytes, and recombinant RANTES was shown to be a "memory" T lymphocyte-selective attractant, it is now tempting to speculate about an important role of RANTES in clinical situations such as allergene-induced late-phase skin reactions in atopic subjects or asthma, where in affected tissues both memory T cells and Eos are characteristic.
1380064	10	3	theme	lymphocyte-selective	1916:1935	arg1	attractant					1937:1946	a "memory" T lymphocyte-selective attractant	1903:1946	a "memory" T lymphocyte-selective attractant	1903:1946	Since RANTES gene expression has been detected in activated T lymphocytes, and recombinant RANTES was shown to be a "memory" T lymphocyte-selective attractant, it is now tempting to speculate about an important role of RANTES in clinical situations such as allergene-induced late-phase skin reactions in atopic subjects or asthma, where in affected tissues both memory T cells and Eos are characteristic.
1380064	2	4	theme	chromatography	288:301	arg1	techniques					303:312	different high-performance liquid chromatography techniques	254:312	different high-performance liquid chromatography techniques	254:312	By the use of different high-performance liquid chromatography techniques, two Eo-chemotactic polypeptides (EoCPs), tentatively termed EoCP-1 and EoCP-2, were purified to homogeneity.
1380064	7	5	theme	daltons	1351:1357	arg1	mass					1330:1333	an average molecular mass	1309:1333	an average molecular mass of 8,355 +/- 10 daltons	1309:1357	Upon ESP-MS, EoCP-1 showed an average molecular mass of 8,355 +/- 10 daltons, suggesting O-glycosylation at these serine residues.
1380064	10	6	theme	memory	2151:2156	arg1	cells					2160:2164	memory T cells	2151:2164	memory T cells	2151:2164	Since RANTES gene expression has been detected in activated T lymphocytes, and recombinant RANTES was shown to be a "memory" T lymphocyte-selective attractant, it is now tempting to speculate about an important role of RANTES in clinical situations such as allergene-induced late-phase skin reactions in atopic subjects or asthma, where in affected tissues both memory T cells and Eos are characteristic.
1380064	7	7	theme	average	1312:1318	arg1	mass					1330:1333	an average molecular mass	1309:1333	an average molecular mass of 8,355 +/- 10 daltons	1309:1357	Upon ESP-MS, EoCP-1 showed an average molecular mass of 8,355 +/- 10 daltons, suggesting O-glycosylation at these serine residues.
1380064	9	8	theme	natural	1774:1780	arg1	forms					1782:1786	the natural forms	1770:1786	the natural forms	1770:1786	Chemotactic activity of RANTES for human Eos could be confirmed using recombinant material, which has been found to be as active as the natural forms.
1380064	10	9	theme	RANTES	1795:1800	arg1	expression					1807:1816	RANTES gene expression	1795:1816	RANTES gene expression	1795:1816	Since RANTES gene expression has been detected in activated T lymphocytes, and recombinant RANTES was shown to be a "memory" T lymphocyte-selective attractant, it is now tempting to speculate about an important role of RANTES in clinical situations such as allergene-induced late-phase skin reactions in atopic subjects or asthma, where in affected tissues both memory T cells and Eos are characteristic.
1380064	10	10	from	characteristic	2178:2191	arg1	tissues					2138:2144	affected tissues	2129:2144	affected tissues	2129:2144	Since RANTES gene expression has been detected in activated T lymphocytes, and recombinant RANTES was shown to be a "memory" T lymphocyte-selective attractant, it is now tempting to speculate about an important role of RANTES in clinical situations such as allergene-induced late-phase skin reactions in atopic subjects or asthma, where in affected tissues both memory T cells and Eos are characteristic.
1380064	2	11	theme	high-performance	264:279	arg1	chromatography					288:301	high-performance liquid chromatography	264:301	different high-performance liquid chromatography techniques	254:312	By the use of different high-performance liquid chromatography techniques, two Eo-chemotactic polypeptides (EoCPs), tentatively termed EoCP-1 and EoCP-2, were purified to homogeneity.
1380064	8	12	theme	migratory	1594:1602	arg1	responses					1604:1612	no significant migratory responses	1579:1612	no significant migratory responses	1579:1612	Both natural forms of RANTES showed strong Eo-chemotactic activity (ED50 = 2 nM) with optimal chemotactic migration at concentrations near 10 nM, however, there were no significant migratory responses with human neutrophils.
1380064	1	13	theme	preformed	172:180	arg1	activity					230:237	a preformed proteinaceous human eosinophil (Eo)-chemotactic activity	170:237	a preformed proteinaceous human eosinophil (Eo)-chemotactic activity	170:237	Thrombin stimulation of human platelets results in the release of a preformed proteinaceous human eosinophil (Eo)-chemotactic activity.
1380064	2	14	theme	Eo-chemotactic	319:332	arg1	EoCP-2					386:391	EoCP-2	386:391	EoCP-2	386:391	By the use of different high-performance liquid chromatography techniques, two Eo-chemotactic polypeptides (EoCPs), tentatively termed EoCP-1 and EoCP-2, were purified to homogeneity.
1380064	2	14	theme	Eo-chemotactic	319:332	arg1	EoCP-1					375:380	tentatively termed EoCP-1	356:380	tentatively termed EoCP-1	356:380	By the use of different high-performance liquid chromatography techniques, two Eo-chemotactic polypeptides (EoCPs), tentatively termed EoCP-1 and EoCP-2, were purified to homogeneity.
1380064	2	14	theme	Eo-chemotactic	319:332	arg1	EoCPs					348:352	EoCPs	348:352	EoCPs	348:352	By the use of different high-performance liquid chromatography techniques, two Eo-chemotactic polypeptides (EoCPs), tentatively termed EoCP-1 and EoCP-2, were purified to homogeneity.
1380064	2	14	theme	Eo-chemotactic	319:332	arg1	polypeptides					334:345	two Eo-chemotactic polypeptides	315:345	two Eo-chemotactic polypeptides (EoCPs)	315:353	By the use of different high-performance liquid chromatography techniques, two Eo-chemotactic polypeptides (EoCPs), tentatively termed EoCP-1 and EoCP-2, were purified to homogeneity.
1380064	1	15	theme	human	196:200	arg1	activity					230:237	a preformed proteinaceous human eosinophil (Eo)-chemotactic activity	170:237	a preformed proteinaceous human eosinophil (Eo)-chemotactic activity	170:237	Thrombin stimulation of human platelets results in the release of a preformed proteinaceous human eosinophil (Eo)-chemotactic activity.
1380064	6	16	theme	residue	1246:1252	arg1	number					1254:1259	methionine residue number 64	1235:1262	methionine residue number 64	1235:1262	Electrospray mass spectrometry (ESP-MS) of EoCPs revealed for EoCP-2 a molecular mass of 7,862.8 +/- 1.1 daltons, which is 15.8 mass units higher than the calculated value of RANTES, indicating that EoCP-2 is identical to the full-length cytokine, and oxygenation, probably at methionine residue number 64, has taken place.
1380064	5	17	theme	Eo	838:839	arg1	EoCP-1					853:858	EoCP-1	853:858	EoCP-1	853:858	In the major Eo chemotaxin, EoCP-1, the residues 4 and 5, which in EoCP-2 were found to be serine residues, could not be identified.
1380064	5	17	theme	Eo	838:839	arg1	chemotaxin					841:850	the major Eo chemotaxin	828:850	the major Eo chemotaxin	828:850	In the major Eo chemotaxin, EoCP-1, the residues 4 and 5, which in EoCP-2 were found to be serine residues, could not be identified.
1380064	10	18	theme	RANTES	2008:2013	arg1	role					2000:2003	an important role	1987:2003	an important role of RANTES in clinical situations such as allergene-induced late-phase skin reactions in atopic subjects or asthma, where in affected tissues both memory T cells and Eos are characteristic	1987:2191	Since RANTES gene expression has been detected in activated T lymphocytes, and recombinant RANTES was shown to be a "memory" T lymphocyte-selective attractant, it is now tempting to speculate about an important role of RANTES in clinical situations such as allergene-induced late-phase skin reactions in atopic subjects or asthma, where in affected tissues both memory T cells and Eos are characteristic.
1380064	10	19	theme	T	1849:1849	arg1	lymphocytes					1851:1861	activated T lymphocytes	1839:1861	activated T lymphocytes	1839:1861	Since RANTES gene expression has been detected in activated T lymphocytes, and recombinant RANTES was shown to be a "memory" T lymphocyte-selective attractant, it is now tempting to speculate about an important role of RANTES in clinical situations such as allergene-induced late-phase skin reactions in atopic subjects or asthma, where in affected tissues both memory T cells and Eos are characteristic.
1380064	1	20	theme	human	128:132	arg1	platelets					134:142	human platelets	128:142	human platelets	128:142	Thrombin stimulation of human platelets results in the release of a preformed proteinaceous human eosinophil (Eo)-chemotactic activity.
1380064	4	21	theme	selective	727:735	arg1	attractants					737:747	leukocyte selective attractants	717:747	leukocyte selective attractants	717:747	NH2-terminal amino acid sequence analysis revealed identical sequences for both EoCP-1 and EoCP-2, which are also identical to that of RANTES, a cytokine that structurally belongs to the interleukin 8 superfamily of leukocyte selective attractants, and that is known to be a "memory-type" T lymphocyte-selective attractant.
1380064	10	22	located	detected	1827:1834	arg2	expression					1807:1816	RANTES gene expression	1795:1816	RANTES gene expression	1795:1816	Since RANTES gene expression has been detected in activated T lymphocytes, and recombinant RANTES was shown to be a "memory" T lymphocyte-selective attractant, it is now tempting to speculate about an important role of RANTES in clinical situations such as allergene-induced late-phase skin reactions in atopic subjects or asthma, where in affected tissues both memory T cells and Eos are characteristic.
1380064	10	22	located	detected	1827:1834	arg1	lymphocytes					1851:1861	activated T lymphocytes	1839:1861	activated T lymphocytes	1839:1861	Since RANTES gene expression has been detected in activated T lymphocytes, and recombinant RANTES was shown to be a "memory" T lymphocyte-selective attractant, it is now tempting to speculate about an important role of RANTES in clinical situations such as allergene-induced late-phase skin reactions in atopic subjects or asthma, where in affected tissues both memory T cells and Eos are characteristic.
1380064	6	23	theme	mass	971:974	arg1	ESP-MS					990:995	ESP-MS	990:995	ESP-MS	990:995	Electrospray mass spectrometry (ESP-MS) of EoCPs revealed for EoCP-2 a molecular mass of 7,862.8 +/- 1.1 daltons, which is 15.8 mass units higher than the calculated value of RANTES, indicating that EoCP-2 is identical to the full-length cytokine, and oxygenation, probably at methionine residue number 64, has taken place.
1380064	6	23	theme	mass	971:974	arg1	spectrometry					976:987	Electrospray mass spectrometry	958:987	Electrospray mass spectrometry (ESP-MS) of EoCPs	958:1005	Electrospray mass spectrometry (ESP-MS) of EoCPs revealed for EoCP-2 a molecular mass of 7,862.8 +/- 1.1 daltons, which is 15.8 mass units higher than the calculated value of RANTES, indicating that EoCP-2 is identical to the full-length cytokine, and oxygenation, probably at methionine residue number 64, has taken place.
1380064	6	24	theme	calculated	1113:1122	arg1	value					1124:1128	the calculated value	1109:1128	the calculated value of RANTES	1109:1138	Electrospray mass spectrometry (ESP-MS) of EoCPs revealed for EoCP-2 a molecular mass of 7,862.8 +/- 1.1 daltons, which is 15.8 mass units higher than the calculated value of RANTES, indicating that EoCP-2 is identical to the full-length cytokine, and oxygenation, probably at methionine residue number 64, has taken place.
1380064	10	25	theme	recombinant	1868:1878	arg1	RANTES					1880:1885	recombinant RANTES	1868:1885	recombinant RANTES	1868:1885	Since RANTES gene expression has been detected in activated T lymphocytes, and recombinant RANTES was shown to be a "memory" T lymphocyte-selective attractant, it is now tempting to speculate about an important role of RANTES in clinical situations such as allergene-induced late-phase skin reactions in atopic subjects or asthma, where in affected tissues both memory T cells and Eos are characteristic.
1380064	10	25	theme	recombinant	1868:1878	arg1	attractant					1937:1946	a "memory" T lymphocyte-selective attractant	1903:1946	a "memory" T lymphocyte-selective attractant	1903:1946	Since RANTES gene expression has been detected in activated T lymphocytes, and recombinant RANTES was shown to be a "memory" T lymphocyte-selective attractant, it is now tempting to speculate about an important role of RANTES in clinical situations such as allergene-induced late-phase skin reactions in atopic subjects or asthma, where in affected tissues both memory T cells and Eos are characteristic.
1380064	0	26	theme	potent	63:68	arg1	attractant					70:79	a potent attractant	61:79	a potent attractant for human eosinophils	61:101	Cytokine RANTES released by thrombin-stimulated platelets is a potent attractant for human eosinophils.
1380064	0	26	theme	potent	63:68	arg1	RANTES					9:14	Cytokine RANTES	0:14	Cytokine RANTES released by thrombin-stimulated platelets	0:56	Cytokine RANTES released by thrombin-stimulated platelets is a potent attractant for human eosinophils.
1380064	4	27	theme	NH2-terminal	501:512	arg1	sequence					525:532	NH2-terminal amino acid sequence	501:532	NH2-terminal amino acid sequence analysis	501:541	NH2-terminal amino acid sequence analysis revealed identical sequences for both EoCP-1 and EoCP-2, which are also identical to that of RANTES, a cytokine that structurally belongs to the interleukin 8 superfamily of leukocyte selective attractants, and that is known to be a "memory-type" T lymphocyte-selective attractant.
1380064	10	28	theme	clinical	2018:2025	arg1	situations					2027:2036	clinical situations	2018:2036	clinical situations	2018:2036	Since RANTES gene expression has been detected in activated T lymphocytes, and recombinant RANTES was shown to be a "memory" T lymphocyte-selective attractant, it is now tempting to speculate about an important role of RANTES in clinical situations such as allergene-induced late-phase skin reactions in atopic subjects or asthma, where in affected tissues both memory T cells and Eos are characteristic.
1380064	10	28	theme	clinical	2018:2025	arg1	reactions					2080:2088	allergene-induced late-phase skin reactions	2046:2088	allergene-induced late-phase skin reactions in atopic subjects or asthma	2046:2117	Since RANTES gene expression has been detected in activated T lymphocytes, and recombinant RANTES was shown to be a "memory" T lymphocyte-selective attractant, it is now tempting to speculate about an important role of RANTES in clinical situations such as allergene-induced late-phase skin reactions in atopic subjects or asthma, where in affected tissues both memory T cells and Eos are characteristic.
1380064	9	29	theme	RANTES	1662:1667	arg1	activity					1650:1657	Chemotactic activity	1638:1657	Chemotactic activity of RANTES for human Eos	1638:1681	Chemotactic activity of RANTES for human Eos could be confirmed using recombinant material, which has been found to be as active as the natural forms.
1380064	4	30	theme	acid	520:523	arg1	sequence					525:532	NH2-terminal amino acid sequence	501:532	NH2-terminal amino acid sequence analysis	501:541	NH2-terminal amino acid sequence analysis revealed identical sequences for both EoCP-1 and EoCP-2, which are also identical to that of RANTES, a cytokine that structurally belongs to the interleukin 8 superfamily of leukocyte selective attractants, and that is known to be a "memory-type" T lymphocyte-selective attractant.
1380064	10	31	theme	skin	2075:2078	arg1	reactions					2080:2088	allergene-induced late-phase skin reactions	2046:2088	allergene-induced late-phase skin reactions in atopic subjects or asthma	2046:2117	Since RANTES gene expression has been detected in activated T lymphocytes, and recombinant RANTES was shown to be a "memory" T lymphocyte-selective attractant, it is now tempting to speculate about an important role of RANTES in clinical situations such as allergene-induced late-phase skin reactions in atopic subjects or asthma, where in affected tissues both memory T cells and Eos are characteristic.
1380064	5	32	theme	serine	916:921	arg1	residues					923:930	serine residues	916:930	serine residues	916:930	In the major Eo chemotaxin, EoCP-1, the residues 4 and 5, which in EoCP-2 were found to be serine residues, could not be identified.
1380064	5	32	theme	serine	916:921	arg1	residues					865:872	the residues 4 and 5	861:880	the residues 4 and 5	861:880	In the major Eo chemotaxin, EoCP-1, the residues 4 and 5, which in EoCP-2 were found to be serine residues, could not be identified.
1380064	9	33	theme	human	1673:1677	arg1	Eos					1679:1681	human Eos	1673:1681	human Eos	1673:1681	Chemotactic activity of RANTES for human Eos could be confirmed using recombinant material, which has been found to be as active as the natural forms.
1380064	10	34	theme	allergene-induced	2046:2062	arg1	reactions					2080:2088	allergene-induced late-phase skin reactions	2046:2088	allergene-induced late-phase skin reactions in atopic subjects or asthma	2046:2117	Since RANTES gene expression has been detected in activated T lymphocytes, and recombinant RANTES was shown to be a "memory" T lymphocyte-selective attractant, it is now tempting to speculate about an important role of RANTES in clinical situations such as allergene-induced late-phase skin reactions in atopic subjects or asthma, where in affected tissues both memory T cells and Eos are characteristic.
1380064	3	35	theme	SDS-PAGE	429:436	arg1	analysis					438:445	SDS-PAGE analysis	429:445	SDS-PAGE analysis	429:445	Upon SDS-PAGE analysis, these chemotaxins showed molecular masses near 8 kD.
1380064	0	36	theme	Cytokine	0:7	arg1	RANTES					9:14	Cytokine RANTES	0:14	Cytokine RANTES released by thrombin-stimulated platelets	0:56	Cytokine RANTES released by thrombin-stimulated platelets is a potent attractant for human eosinophils.
1380064	0	36	theme	Cytokine	0:7	arg1	attractant					70:79	a potent attractant	61:79	a potent attractant for human eosinophils	61:101	Cytokine RANTES released by thrombin-stimulated platelets is a potent attractant for human eosinophils.
1380064	6	37	theme	EoCPs	1001:1005	arg1	ESP-MS					990:995	ESP-MS	990:995	ESP-MS	990:995	Electrospray mass spectrometry (ESP-MS) of EoCPs revealed for EoCP-2 a molecular mass of 7,862.8 +/- 1.1 daltons, which is 15.8 mass units higher than the calculated value of RANTES, indicating that EoCP-2 is identical to the full-length cytokine, and oxygenation, probably at methionine residue number 64, has taken place.
1380064	6	37	theme	EoCPs	1001:1005	arg1	spectrometry					976:987	Electrospray mass spectrometry	958:987	Electrospray mass spectrometry (ESP-MS) of EoCPs	958:1005	Electrospray mass spectrometry (ESP-MS) of EoCPs revealed for EoCP-2 a molecular mass of 7,862.8 +/- 1.1 daltons, which is 15.8 mass units higher than the calculated value of RANTES, indicating that EoCP-2 is identical to the full-length cytokine, and oxygenation, probably at methionine residue number 64, has taken place.
1380064	8	38	theme	RANTES	1435:1440	arg1	forms					1426:1430	Both natural forms	1413:1430	Both natural forms of RANTES	1413:1440	Both natural forms of RANTES showed strong Eo-chemotactic activity (ED50 = 2 nM) with optimal chemotactic migration at concentrations near 10 nM, however, there were no significant migratory responses with human neutrophils.
1380064	10	39	from	reactions	2080:2088	arg1	asthma					2112:2117	asthma	2112:2117	asthma	2112:2117	Since RANTES gene expression has been detected in activated T lymphocytes, and recombinant RANTES was shown to be a "memory" T lymphocyte-selective attractant, it is now tempting to speculate about an important role of RANTES in clinical situations such as allergene-induced late-phase skin reactions in atopic subjects or asthma, where in affected tissues both memory T cells and Eos are characteristic.
1380064	10	39	from	reactions	2080:2088	arg1	subjects					2100:2107	atopic subjects	2093:2107	atopic subjects	2093:2107	Since RANTES gene expression has been detected in activated T lymphocytes, and recombinant RANTES was shown to be a "memory" T lymphocyte-selective attractant, it is now tempting to speculate about an important role of RANTES in clinical situations such as allergene-induced late-phase skin reactions in atopic subjects or asthma, where in affected tissues both memory T cells and Eos are characteristic.
1380064	3	40	theme	molecular	473:481	arg1	masses					483:488	molecular masses	473:488	molecular masses near 8 kD	473:498	Upon SDS-PAGE analysis, these chemotaxins showed molecular masses near 8 kD.
1380064	6	41	from	number	1254:1259	arg1	oxygenation					1210:1220	oxygenation	1210:1220	oxygenation	1210:1220	Electrospray mass spectrometry (ESP-MS) of EoCPs revealed for EoCP-2 a molecular mass of 7,862.8 +/- 1.1 daltons, which is 15.8 mass units higher than the calculated value of RANTES, indicating that EoCP-2 is identical to the full-length cytokine, and oxygenation, probably at methionine residue number 64, has taken place.
1380064	9	42	theme	recombinant	1708:1718	arg1	material					1720:1727	recombinant material	1708:1727	recombinant material	1708:1727	Chemotactic activity of RANTES for human Eos could be confirmed using recombinant material, which has been found to be as active as the natural forms.
1380064	8	43	theme	strong	1449:1454	arg1	nM					1490:1491	ED50 = 2 nM	1481:1491	ED50 = 2 nM	1481:1491	Both natural forms of RANTES showed strong Eo-chemotactic activity (ED50 = 2 nM) with optimal chemotactic migration at concentrations near 10 nM, however, there were no significant migratory responses with human neutrophils.
1380064	8	43	theme	strong	1449:1454	arg1	activity					1471:1478	strong Eo-chemotactic activity	1449:1478	strong Eo-chemotactic activity (ED50 = 2 nM)	1449:1492	Both natural forms of RANTES showed strong Eo-chemotactic activity (ED50 = 2 nM) with optimal chemotactic migration at concentrations near 10 nM, however, there were no significant migratory responses with human neutrophils.
1380064	4	44	theme	lymphocyte-selective	792:811	arg1	that					754:757	that	754:757	that	754:757	NH2-terminal amino acid sequence analysis revealed identical sequences for both EoCP-1 and EoCP-2, which are also identical to that of RANTES, a cytokine that structurally belongs to the interleukin 8 superfamily of leukocyte selective attractants, and that is known to be a "memory-type" T lymphocyte-selective attractant.
1380064	4	44	theme	lymphocyte-selective	792:811	arg1	attractant					813:822	a "memory-type" T lymphocyte-selective attractant	774:822	a "memory-type" T lymphocyte-selective attractant	774:822	NH2-terminal amino acid sequence analysis revealed identical sequences for both EoCP-1 and EoCP-2, which are also identical to that of RANTES, a cytokine that structurally belongs to the interleukin 8 superfamily of leukocyte selective attractants, and that is known to be a "memory-type" T lymphocyte-selective attractant.
1380064	0	45	theme	thrombin-stimulated	28:46	arg1	platelets					48:56	thrombin-stimulated platelets	28:56	thrombin-stimulated platelets	28:56	Cytokine RANTES released by thrombin-stimulated platelets is a potent attractant for human eosinophils.
1380064	10	46	theme	T	1914:1914	arg1	RANTES					1880:1885	recombinant RANTES	1868:1885	recombinant RANTES	1868:1885	Since RANTES gene expression has been detected in activated T lymphocytes, and recombinant RANTES was shown to be a "memory" T lymphocyte-selective attractant, it is now tempting to speculate about an important role of RANTES in clinical situations such as allergene-induced late-phase skin reactions in atopic subjects or asthma, where in affected tissues both memory T cells and Eos are characteristic.
1380064	10	46	theme	T	1914:1914	arg1	attractant					1937:1946	a "memory" T lymphocyte-selective attractant	1903:1946	a "memory" T lymphocyte-selective attractant	1903:1946	Since RANTES gene expression has been detected in activated T lymphocytes, and recombinant RANTES was shown to be a "memory" T lymphocyte-selective attractant, it is now tempting to speculate about an important role of RANTES in clinical situations such as allergene-induced late-phase skin reactions in atopic subjects or asthma, where in affected tissues both memory T cells and Eos are characteristic.
1380064	8	47	theme	ED50	1481:1484	arg1	nM					1490:1491	ED50 = 2 nM	1481:1491	ED50 = 2 nM	1481:1491	Both natural forms of RANTES showed strong Eo-chemotactic activity (ED50 = 2 nM) with optimal chemotactic migration at concentrations near 10 nM, however, there were no significant migratory responses with human neutrophils.
1380064	8	47	theme	ED50	1481:1484	arg1	activity					1471:1478	strong Eo-chemotactic activity	1449:1478	strong Eo-chemotactic activity (ED50 = 2 nM)	1449:1492	Both natural forms of RANTES showed strong Eo-chemotactic activity (ED50 = 2 nM) with optimal chemotactic migration at concentrations near 10 nM, however, there were no significant migratory responses with human neutrophils.
1380064	1	48	theme	-chemotactic	217:228	arg1	activity					230:237	a preformed proteinaceous human eosinophil (Eo)-chemotactic activity	170:237	a preformed proteinaceous human eosinophil (Eo)-chemotactic activity	170:237	Thrombin stimulation of human platelets results in the release of a preformed proteinaceous human eosinophil (Eo)-chemotactic activity.
1380064	6	49	theme	mass	1086:1089	arg1	units					1091:1095	15.8 mass units	1081:1095	15.8 mass units	1081:1095	Electrospray mass spectrometry (ESP-MS) of EoCPs revealed for EoCP-2 a molecular mass of 7,862.8 +/- 1.1 daltons, which is 15.8 mass units higher than the calculated value of RANTES, indicating that EoCP-2 is identical to the full-length cytokine, and oxygenation, probably at methionine residue number 64, has taken place.
1380064	4	50	theme	"	788:788	arg1	that					754:757	that	754:757	that	754:757	NH2-terminal amino acid sequence analysis revealed identical sequences for both EoCP-1 and EoCP-2, which are also identical to that of RANTES, a cytokine that structurally belongs to the interleukin 8 superfamily of leukocyte selective attractants, and that is known to be a "memory-type" T lymphocyte-selective attractant.
1380064	4	50	theme	"	788:788	arg1	attractant					813:822	a "memory-type" T lymphocyte-selective attractant	774:822	a "memory-type" T lymphocyte-selective attractant	774:822	NH2-terminal amino acid sequence analysis revealed identical sequences for both EoCP-1 and EoCP-2, which are also identical to that of RANTES, a cytokine that structurally belongs to the interleukin 8 superfamily of leukocyte selective attractants, and that is known to be a "memory-type" T lymphocyte-selective attractant.
1380064	2	51	theme	termed	368:373	arg1	EoCP-1					375:380	tentatively termed EoCP-1	356:380	tentatively termed EoCP-1	356:380	By the use of different high-performance liquid chromatography techniques, two Eo-chemotactic polypeptides (EoCPs), tentatively termed EoCP-1 and EoCP-2, were purified to homogeneity.
1380064	2	51	theme	termed	368:373	arg1	polypeptides					334:345	two Eo-chemotactic polypeptides	315:345	two Eo-chemotactic polypeptides (EoCPs)	315:353	By the use of different high-performance liquid chromatography techniques, two Eo-chemotactic polypeptides (EoCPs), tentatively termed EoCP-1 and EoCP-2, were purified to homogeneity.
1380064	8	52	theme	optimal	1499:1505	arg1	migration					1519:1527	optimal chemotactic migration	1499:1527	optimal chemotactic migration	1499:1527	Both natural forms of RANTES showed strong Eo-chemotactic activity (ED50 = 2 nM) with optimal chemotactic migration at concentrations near 10 nM, however, there were no significant migratory responses with human neutrophils.
1380064	6	53	theme	full-length	1184:1194	arg1	cytokine					1196:1203	the full-length cytokine	1180:1203	the full-length cytokine	1180:1203	Electrospray mass spectrometry (ESP-MS) of EoCPs revealed for EoCP-2 a molecular mass of 7,862.8 +/- 1.1 daltons, which is 15.8 mass units higher than the calculated value of RANTES, indicating that EoCP-2 is identical to the full-length cytokine, and oxygenation, probably at methionine residue number 64, has taken place.
1380064	2	54	theme	techniques	303:312	arg1	use					247:249	the use	243:249	the use of different high-performance liquid chromatography techniques	243:312	By the use of different high-performance liquid chromatography techniques, two Eo-chemotactic polypeptides (EoCPs), tentatively termed EoCP-1 and EoCP-2, were purified to homogeneity.
1380064	10	55	theme	gene	1802:1805	arg1	expression					1807:1816	RANTES gene expression	1795:1816	RANTES gene expression	1795:1816	Since RANTES gene expression has been detected in activated T lymphocytes, and recombinant RANTES was shown to be a "memory" T lymphocyte-selective attractant, it is now tempting to speculate about an important role of RANTES in clinical situations such as allergene-induced late-phase skin reactions in atopic subjects or asthma, where in affected tissues both memory T cells and Eos are characteristic.
1380064	2	56	theme	liquid	281:286	arg1	chromatography					288:301	high-performance liquid chromatography	264:301	different high-performance liquid chromatography techniques	254:312	By the use of different high-performance liquid chromatography techniques, two Eo-chemotactic polypeptides (EoCPs), tentatively termed EoCP-1 and EoCP-2, were purified to homogeneity.
1380064	7	57	theme	molecular	1320:1328	arg1	mass					1330:1333	an average molecular mass	1309:1333	an average molecular mass of 8,355 +/- 10 daltons	1309:1357	Upon ESP-MS, EoCP-1 showed an average molecular mass of 8,355 +/- 10 daltons, suggesting O-glycosylation at these serine residues.
1380064	10	58	from	role	2000:2003	arg1	situations					2027:2036	clinical situations	2018:2036	clinical situations	2018:2036	Since RANTES gene expression has been detected in activated T lymphocytes, and recombinant RANTES was shown to be a "memory" T lymphocyte-selective attractant, it is now tempting to speculate about an important role of RANTES in clinical situations such as allergene-induced late-phase skin reactions in atopic subjects or asthma, where in affected tissues both memory T cells and Eos are characteristic.
1380064	10	58	from	role	2000:2003	arg1	reactions					2080:2088	allergene-induced late-phase skin reactions	2046:2088	allergene-induced late-phase skin reactions in atopic subjects or asthma	2046:2117	Since RANTES gene expression has been detected in activated T lymphocytes, and recombinant RANTES was shown to be a "memory" T lymphocyte-selective attractant, it is now tempting to speculate about an important role of RANTES in clinical situations such as allergene-induced late-phase skin reactions in atopic subjects or asthma, where in affected tissues both memory T cells and Eos are characteristic.
1380064	8	59	theme	significant	1582:1592	arg1	responses					1604:1612	no significant migratory responses	1579:1612	no significant migratory responses	1579:1612	Both natural forms of RANTES showed strong Eo-chemotactic activity (ED50 = 2 nM) with optimal chemotactic migration at concentrations near 10 nM, however, there were no significant migratory responses with human neutrophils.
1380064	1	60	theme	proteinaceous	182:194	arg1	activity					230:237	a preformed proteinaceous human eosinophil (Eo)-chemotactic activity	170:237	a preformed proteinaceous human eosinophil (Eo)-chemotactic activity	170:237	Thrombin stimulation of human platelets results in the release of a preformed proteinaceous human eosinophil (Eo)-chemotactic activity.
1380064	10	61	theme	affected	2129:2136	arg1	tissues					2138:2144	affected tissues	2129:2144	affected tissues	2129:2144	Since RANTES gene expression has been detected in activated T lymphocytes, and recombinant RANTES was shown to be a "memory" T lymphocyte-selective attractant, it is now tempting to speculate about an important role of RANTES in clinical situations such as allergene-induced late-phase skin reactions in atopic subjects or asthma, where in affected tissues both memory T cells and Eos are characteristic.
1380064	10	62	theme	important	1990:1998	arg1	role					2000:2003	an important role	1987:2003	an important role of RANTES in clinical situations such as allergene-induced late-phase skin reactions in atopic subjects or asthma, where in affected tissues both memory T cells and Eos are characteristic	1987:2191	Since RANTES gene expression has been detected in activated T lymphocytes, and recombinant RANTES was shown to be a "memory" T lymphocyte-selective attractant, it is now tempting to speculate about an important role of RANTES in clinical situations such as allergene-induced late-phase skin reactions in atopic subjects or asthma, where in affected tissues both memory T cells and Eos are characteristic.
1380064	1	63	theme	eosinophil	202:211	arg1	activity					230:237	a preformed proteinaceous human eosinophil (Eo)-chemotactic activity	170:237	a preformed proteinaceous human eosinophil (Eo)-chemotactic activity	170:237	Thrombin stimulation of human platelets results in the release of a preformed proteinaceous human eosinophil (Eo)-chemotactic activity.
1380064	6	64	theme	methionine	1235:1244	arg1	number					1254:1259	methionine residue number 64	1235:1262	methionine residue number 64	1235:1262	Electrospray mass spectrometry (ESP-MS) of EoCPs revealed for EoCP-2 a molecular mass of 7,862.8 +/- 1.1 daltons, which is 15.8 mass units higher than the calculated value of RANTES, indicating that EoCP-2 is identical to the full-length cytokine, and oxygenation, probably at methionine residue number 64, has taken place.
1380064	8	65	theme	human	1619:1623	arg1	neutrophils					1625:1635	human neutrophils	1619:1635	human neutrophils	1619:1635	Both natural forms of RANTES showed strong Eo-chemotactic activity (ED50 = 2 nM) with optimal chemotactic migration at concentrations near 10 nM, however, there were no significant migratory responses with human neutrophils.
1380064	5	66	theme	major	832:836	arg1	EoCP-1					853:858	EoCP-1	853:858	EoCP-1	853:858	In the major Eo chemotaxin, EoCP-1, the residues 4 and 5, which in EoCP-2 were found to be serine residues, could not be identified.
1380064	5	66	theme	major	832:836	arg1	chemotaxin					841:850	the major Eo chemotaxin	828:850	the major Eo chemotaxin	828:850	In the major Eo chemotaxin, EoCP-1, the residues 4 and 5, which in EoCP-2 were found to be serine residues, could not be identified.
1380064	10	67	theme	T	2158:2158	arg1	cells					2160:2164	memory T cells	2151:2164	memory T cells	2151:2164	Since RANTES gene expression has been detected in activated T lymphocytes, and recombinant RANTES was shown to be a "memory" T lymphocyte-selective attractant, it is now tempting to speculate about an important role of RANTES in clinical situations such as allergene-induced late-phase skin reactions in atopic subjects or asthma, where in affected tissues both memory T cells and Eos are characteristic.
1380064	4	68	theme	identical	552:560	arg1	sequences					562:570	identical sequences	552:570	identical sequences	552:570	NH2-terminal amino acid sequence analysis revealed identical sequences for both EoCP-1 and EoCP-2, which are also identical to that of RANTES, a cytokine that structurally belongs to the interleukin 8 superfamily of leukocyte selective attractants, and that is known to be a "memory-type" T lymphocyte-selective attractant.
1380064	6	69	theme	RANTES	1133:1138	arg1	value					1124:1128	the calculated value	1109:1128	the calculated value of RANTES	1109:1138	Electrospray mass spectrometry (ESP-MS) of EoCPs revealed for EoCP-2 a molecular mass of 7,862.8 +/- 1.1 daltons, which is 15.8 mass units higher than the calculated value of RANTES, indicating that EoCP-2 is identical to the full-length cytokine, and oxygenation, probably at methionine residue number 64, has taken place.
1380064	10	70	theme	activated	1839:1847	arg1	lymphocytes					1851:1861	activated T lymphocytes	1839:1861	activated T lymphocytes	1839:1861	Since RANTES gene expression has been detected in activated T lymphocytes, and recombinant RANTES was shown to be a "memory" T lymphocyte-selective attractant, it is now tempting to speculate about an important role of RANTES in clinical situations such as allergene-induced late-phase skin reactions in atopic subjects or asthma, where in affected tissues both memory T cells and Eos are characteristic.
1380064	2	71	theme	different	254:262	arg1	techniques					303:312	different high-performance liquid chromatography techniques	254:312	different high-performance liquid chromatography techniques	254:312	By the use of different high-performance liquid chromatography techniques, two Eo-chemotactic polypeptides (EoCPs), tentatively termed EoCP-1 and EoCP-2, were purified to homogeneity.
1380064	1	72	theme	platelets	134:142	arg1	stimulation					113:123	Thrombin stimulation	104:123	Thrombin stimulation of human platelets	104:142	Thrombin stimulation of human platelets results in the release of a preformed proteinaceous human eosinophil (Eo)-chemotactic activity.
1380064	4	73	theme	leukocyte	717:725	arg1	attractants					737:747	leukocyte selective attractants	717:747	leukocyte selective attractants	717:747	NH2-terminal amino acid sequence analysis revealed identical sequences for both EoCP-1 and EoCP-2, which are also identical to that of RANTES, a cytokine that structurally belongs to the interleukin 8 superfamily of leukocyte selective attractants, and that is known to be a "memory-type" T lymphocyte-selective attractant.
1380064	6	74	theme	Electrospray	958:969	arg1	ESP-MS					990:995	ESP-MS	990:995	ESP-MS	990:995	Electrospray mass spectrometry (ESP-MS) of EoCPs revealed for EoCP-2 a molecular mass of 7,862.8 +/- 1.1 daltons, which is 15.8 mass units higher than the calculated value of RANTES, indicating that EoCP-2 is identical to the full-length cytokine, and oxygenation, probably at methionine residue number 64, has taken place.
1380064	6	74	theme	Electrospray	958:969	arg1	spectrometry					976:987	Electrospray mass spectrometry	958:987	Electrospray mass spectrometry (ESP-MS) of EoCPs	958:1005	Electrospray mass spectrometry (ESP-MS) of EoCPs revealed for EoCP-2 a molecular mass of 7,862.8 +/- 1.1 daltons, which is 15.8 mass units higher than the calculated value of RANTES, indicating that EoCP-2 is identical to the full-length cytokine, and oxygenation, probably at methionine residue number 64, has taken place.
1380064	9	75	theme	Chemotactic	1638:1648	arg1	activity					1650:1657	Chemotactic activity	1638:1657	Chemotactic activity of RANTES for human Eos	1638:1681	Chemotactic activity of RANTES for human Eos could be confirmed using recombinant material, which has been found to be as active as the natural forms.
1380064	4	76	theme	amino	514:518	arg1	sequence					525:532	NH2-terminal amino acid sequence	501:532	NH2-terminal amino acid sequence analysis	501:541	NH2-terminal amino acid sequence analysis revealed identical sequences for both EoCP-1 and EoCP-2, which are also identical to that of RANTES, a cytokine that structurally belongs to the interleukin 8 superfamily of leukocyte selective attractants, and that is known to be a "memory-type" T lymphocyte-selective attractant.
1380064	0	77	theme	human	85:89	arg1	eosinophils					91:101	human eosinophils	85:101	human eosinophils	85:101	Cytokine RANTES released by thrombin-stimulated platelets is a potent attractant for human eosinophils.
1380064	4	78	theme	sequence	525:532	arg1	analysis					534:541	NH2-terminal amino acid sequence analysis	501:541	NH2-terminal amino acid sequence analysis	501:541	NH2-terminal amino acid sequence analysis revealed identical sequences for both EoCP-1 and EoCP-2, which are also identical to that of RANTES, a cytokine that structurally belongs to the interleukin 8 superfamily of leukocyte selective attractants, and that is known to be a "memory-type" T lymphocyte-selective attractant.
1380064	4	79	theme	interleukin	688:698	arg1	superfamily					702:712	the interleukin 8 superfamily	684:712	the interleukin 8 superfamily of leukocyte selective attractants	684:747	NH2-terminal amino acid sequence analysis revealed identical sequences for both EoCP-1 and EoCP-2, which are also identical to that of RANTES, a cytokine that structurally belongs to the interleukin 8 superfamily of leukocyte selective attractants, and that is known to be a "memory-type" T lymphocyte-selective attractant.
1380064	8	80	theme	natural	1418:1424	arg1	forms					1426:1430	Both natural forms	1413:1430	Both natural forms of RANTES	1413:1440	Both natural forms of RANTES showed strong Eo-chemotactic activity (ED50 = 2 nM) with optimal chemotactic migration at concentrations near 10 nM, however, there were no significant migratory responses with human neutrophils.
1380064	10	81	theme	late-phase	2064:2073	arg1	reactions					2080:2088	allergene-induced late-phase skin reactions	2046:2088	allergene-induced late-phase skin reactions in atopic subjects or asthma	2046:2117	Since RANTES gene expression has been detected in activated T lymphocytes, and recombinant RANTES was shown to be a "memory" T lymphocyte-selective attractant, it is now tempting to speculate about an important role of RANTES in clinical situations such as allergene-induced late-phase skin reactions in atopic subjects or asthma, where in affected tissues both memory T cells and Eos are characteristic.
1380064	10	82	theme	atopic	2093:2098	arg1	subjects					2100:2107	atopic subjects	2093:2107	atopic subjects	2093:2107	Since RANTES gene expression has been detected in activated T lymphocytes, and recombinant RANTES was shown to be a "memory" T lymphocyte-selective attractant, it is now tempting to speculate about an important role of RANTES in clinical situations such as allergene-induced late-phase skin reactions in atopic subjects or asthma, where in affected tissues both memory T cells and Eos are characteristic.
1380064	4	83	theme	attractants	737:747	arg1	superfamily					702:712	the interleukin 8 superfamily	684:712	the interleukin 8 superfamily of leukocyte selective attractants	684:747	NH2-terminal amino acid sequence analysis revealed identical sequences for both EoCP-1 and EoCP-2, which are also identical to that of RANTES, a cytokine that structurally belongs to the interleukin 8 superfamily of leukocyte selective attractants, and that is known to be a "memory-type" T lymphocyte-selective attractant.
1380064	1	84	theme	Thrombin	104:111	arg1	stimulation					113:123	Thrombin stimulation	104:123	Thrombin stimulation of human platelets	104:142	Thrombin stimulation of human platelets results in the release of a preformed proteinaceous human eosinophil (Eo)-chemotactic activity.
1380064	7	85	gly	O-glycosylation	1371:1385	arg1	residues					1403:1410	these serine residues	1390:1410	these serine residues	1390:1410	Upon ESP-MS, EoCP-1 showed an average molecular mass of 8,355 +/- 10 daltons, suggesting O-glycosylation at these serine residues.
1380064	7	85	gly	O-glycosylation	1371:1385	arg2	residues					1403:1410	these serine residues	1390:1410	these serine residues	1390:1410	Upon ESP-MS, EoCP-1 showed an average molecular mass of 8,355 +/- 10 daltons, suggesting O-glycosylation at these serine residues.
1380064	8	86	theme	Eo-chemotactic	1456:1469	arg1	nM					1490:1491	ED50 = 2 nM	1481:1491	ED50 = 2 nM	1481:1491	Both natural forms of RANTES showed strong Eo-chemotactic activity (ED50 = 2 nM) with optimal chemotactic migration at concentrations near 10 nM, however, there were no significant migratory responses with human neutrophils.
1380064	8	86	theme	Eo-chemotactic	1456:1469	arg1	activity					1471:1478	strong Eo-chemotactic activity	1449:1478	strong Eo-chemotactic activity (ED50 = 2 nM)	1449:1492	Both natural forms of RANTES showed strong Eo-chemotactic activity (ED50 = 2 nM) with optimal chemotactic migration at concentrations near 10 nM, however, there were no significant migratory responses with human neutrophils.
1380064	5	87	dep	residues	865:872	arg1	4					874:874	4	874:874	4	874:874	In the major Eo chemotaxin, EoCP-1, the residues 4 and 5, which in EoCP-2 were found to be serine residues, could not be identified.
1380064	5	87	dep	residues	865:872	arg1	5					880:880	5	880:880	5	880:880	In the major Eo chemotaxin, EoCP-1, the residues 4 and 5, which in EoCP-2 were found to be serine residues, could not be identified.
1380064	1	88	theme	Eo	214:215	arg1	activity					230:237	a preformed proteinaceous human eosinophil (Eo)-chemotactic activity	170:237	a preformed proteinaceous human eosinophil (Eo)-chemotactic activity	170:237	Thrombin stimulation of human platelets results in the release of a preformed proteinaceous human eosinophil (Eo)-chemotactic activity.
1380064	10	89	from	tissues	2138:2144	arg1	characteristic					2178:2191	characteristic	2178:2191	characteristic	2178:2191	Since RANTES gene expression has been detected in activated T lymphocytes, and recombinant RANTES was shown to be a "memory" T lymphocyte-selective attractant, it is now tempting to speculate about an important role of RANTES in clinical situations such as allergene-induced late-phase skin reactions in atopic subjects or asthma, where in affected tissues both memory T cells and Eos are characteristic.
1380064	4	90	theme	T	790:790	arg1	that					754:757	that	754:757	that	754:757	NH2-terminal amino acid sequence analysis revealed identical sequences for both EoCP-1 and EoCP-2, which are also identical to that of RANTES, a cytokine that structurally belongs to the interleukin 8 superfamily of leukocyte selective attractants, and that is known to be a "memory-type" T lymphocyte-selective attractant.
1380064	4	90	theme	T	790:790	arg1	attractant					813:822	a "memory-type" T lymphocyte-selective attractant	774:822	a "memory-type" T lymphocyte-selective attractant	774:822	NH2-terminal amino acid sequence analysis revealed identical sequences for both EoCP-1 and EoCP-2, which are also identical to that of RANTES, a cytokine that structurally belongs to the interleukin 8 superfamily of leukocyte selective attractants, and that is known to be a "memory-type" T lymphocyte-selective attractant.
1380064	6	91	theme	daltons	1063:1069	arg1	mass					1039:1042	a molecular mass	1027:1042	a molecular mass of 7,862.8 +/- 1.1 daltons, which is 15.8 mass units higher than the calculated value of RANTES, indicating that EoCP-2 is identical to the full-length cytokine, and oxygenation, probably at methionine residue number 64, has taken place	1027:1279	Electrospray mass spectrometry (ESP-MS) of EoCPs revealed for EoCP-2 a molecular mass of 7,862.8 +/- 1.1 daltons, which is 15.8 mass units higher than the calculated value of RANTES, indicating that EoCP-2 is identical to the full-length cytokine, and oxygenation, probably at methionine residue number 64, has taken place.
1380064	8	92	theme	=	1486:1486	arg1	nM					1490:1491	ED50 = 2 nM	1481:1491	ED50 = 2 nM	1481:1491	Both natural forms of RANTES showed strong Eo-chemotactic activity (ED50 = 2 nM) with optimal chemotactic migration at concentrations near 10 nM, however, there were no significant migratory responses with human neutrophils.
1380064	8	92	theme	=	1486:1486	arg1	activity					1471:1478	strong Eo-chemotactic activity	1449:1478	strong Eo-chemotactic activity (ED50 = 2 nM)	1449:1492	Both natural forms of RANTES showed strong Eo-chemotactic activity (ED50 = 2 nM) with optimal chemotactic migration at concentrations near 10 nM, however, there were no significant migratory responses with human neutrophils.
1380064	5	93	located	found	904:908	arg1	EoCP-2					892:897	EoCP-2	892:897	EoCP-2	892:897	In the major Eo chemotaxin, EoCP-1, the residues 4 and 5, which in EoCP-2 were found to be serine residues, could not be identified.
1380064	5	93	located	found	904:908	arg2	residues					923:930	serine residues	916:930	serine residues	916:930	In the major Eo chemotaxin, EoCP-1, the residues 4 and 5, which in EoCP-2 were found to be serine residues, could not be identified.
1380064	5	93	located	found	904:908	arg2	residues					865:872	the residues 4 and 5	861:880	the residues 4 and 5	861:880	In the major Eo chemotaxin, EoCP-1, the residues 4 and 5, which in EoCP-2 were found to be serine residues, could not be identified.
1380064	10	94	theme	"	1912:1912	arg1	RANTES					1880:1885	recombinant RANTES	1868:1885	recombinant RANTES	1868:1885	Since RANTES gene expression has been detected in activated T lymphocytes, and recombinant RANTES was shown to be a "memory" T lymphocyte-selective attractant, it is now tempting to speculate about an important role of RANTES in clinical situations such as allergene-induced late-phase skin reactions in atopic subjects or asthma, where in affected tissues both memory T cells and Eos are characteristic.
1380064	10	94	theme	"	1912:1912	arg1	attractant					1937:1946	a "memory" T lymphocyte-selective attractant	1903:1946	a "memory" T lymphocyte-selective attractant	1903:1946	Since RANTES gene expression has been detected in activated T lymphocytes, and recombinant RANTES was shown to be a "memory" T lymphocyte-selective attractant, it is now tempting to speculate about an important role of RANTES in clinical situations such as allergene-induced late-phase skin reactions in atopic subjects or asthma, where in affected tissues both memory T cells and Eos are characteristic.
1380064	1	95	theme	activity	230:237	arg1	release					159:165	the release	155:165	the release of a preformed proteinaceous human eosinophil (Eo)-chemotactic activity	155:237	Thrombin stimulation of human platelets results in the release of a preformed proteinaceous human eosinophil (Eo)-chemotactic activity.
1380064	7	96	theme	serine	1396:1401	arg1	residues					1403:1410	these serine residues	1390:1410	these serine residues	1390:1410	Upon ESP-MS, EoCP-1 showed an average molecular mass of 8,355 +/- 10 daltons, suggesting O-glycosylation at these serine residues.
1380064	4	97	theme	memory-type	777:787	arg1	that					754:757	that	754:757	that	754:757	NH2-terminal amino acid sequence analysis revealed identical sequences for both EoCP-1 and EoCP-2, which are also identical to that of RANTES, a cytokine that structurally belongs to the interleukin 8 superfamily of leukocyte selective attractants, and that is known to be a "memory-type" T lymphocyte-selective attractant.
1380064	4	97	theme	memory-type	777:787	arg1	attractant					813:822	a "memory-type" T lymphocyte-selective attractant	774:822	a "memory-type" T lymphocyte-selective attractant	774:822	NH2-terminal amino acid sequence analysis revealed identical sequences for both EoCP-1 and EoCP-2, which are also identical to that of RANTES, a cytokine that structurally belongs to the interleukin 8 superfamily of leukocyte selective attractants, and that is known to be a "memory-type" T lymphocyte-selective attractant.
22000856	5	0	theme	noninhibitory	735:747	arg1	fragment					758:765	a noninhibitory antibody fragment	733:765	a noninhibitory antibody fragment	733:765	Small-angle X-ray scattering analysis of LRP6(1-4) bound to a noninhibitory antibody fragment or to full-length Dkk1 shows that in both cases the ectodomain adopts a curved conformation that places the first three repeats at a similar height relative to the membrane.
22000856	5	1	theme	antibody	749:756	arg1	fragment					758:765	a noninhibitory antibody fragment	733:765	a noninhibitory antibody fragment	733:765	Small-angle X-ray scattering analysis of LRP6(1-4) bound to a noninhibitory antibody fragment or to full-length Dkk1 shows that in both cases the ectodomain adopts a curved conformation that places the first three repeats at a similar height relative to the membrane.
22000856	1	2	theme	Wnt	214:216	arg1	signaling					218:226	Wnt signaling	214:226	Wnt signaling	214:226	LDL receptor-related proteins 5 and 6 (LRP5/6) are coreceptors for Wnt growth factors, and also bind Dkk proteins, secreted inhibitors of Wnt signaling.
22000856	6	3	theme	Frizzled	1045:1052	arg1	coreceptors					1054:1064	Frizzled coreceptors	1045:1064	Frizzled coreceptors	1045:1064	Thus, Wnts bound to either portion of the LRP6 ectodomain likely bear a similar spatial relationship to Frizzled coreceptors.
22000856	1	4	theme	signaling	218:226	arg1	proteins					181:188	Dkk proteins	177:188	Dkk proteins	177:188	LDL receptor-related proteins 5 and 6 (LRP5/6) are coreceptors for Wnt growth factors, and also bind Dkk proteins, secreted inhibitors of Wnt signaling.
22000856	1	4	theme	signaling	218:226	arg1	inhibitors					200:209	secreted inhibitors	191:209	secreted inhibitors of Wnt signaling	191:226	LDL receptor-related proteins 5 and 6 (LRP5/6) are coreceptors for Wnt growth factors, and also bind Dkk proteins, secreted inhibitors of Wnt signaling.
22000856	3	5	dep	bind	336:339	arg1	whereas					366:372	whereas	366:372	whereas	366:372	The first two repeats, LRP6(1-2), bind to several Wnt variants, whereas LRP6(3-4) binds other Wnts.
22000856	5	6	theme	full-length	773:783	arg1	Dkk1					785:788	full-length Dkk1	773:788	full-length Dkk1	773:788	Small-angle X-ray scattering analysis of LRP6(1-4) bound to a noninhibitory antibody fragment or to full-length Dkk1 shows that in both cases the ectodomain adopts a curved conformation that places the first three repeats at a similar height relative to the membrane.
22000856	4	7	dep	LRP6	474:477	arg1	3-4					479:481	3-4	479:481	3-4	479:481	We present the crystal structure of the Dkk1 C-terminal domain bound to LRP6(3-4), and show that the Dkk1 N-terminal domain binds to LRP6(1-2), demonstrating that a single Dkk1 molecule can bind to both portions of the LRP6 ectodomain and thereby inhibit different Wnts.
22000856	4	8	theme	N-terminal	508:517	arg1	domain					519:524	the Dkk1 N-terminal domain	499:524	the Dkk1 N-terminal domain	499:524	We present the crystal structure of the Dkk1 C-terminal domain bound to LRP6(3-4), and show that the Dkk1 N-terminal domain binds to LRP6(1-2), demonstrating that a single Dkk1 molecule can bind to both portions of the LRP6 ectodomain and thereby inhibit different Wnts.
22000856	2	9	theme	LRP5/6	233:238	arg1	ectodomain					240:249	The LRP5/6 ectodomain	229:249	The LRP5/6 ectodomain	229:249	The LRP5/6 ectodomain contains four β-propeller/EGF-like domain repeats.
22000856	1	10	theme	Wnt	143:145	arg1	factors					154:160	Wnt growth factors	143:160	Wnt growth factors	143:160	LDL receptor-related proteins 5 and 6 (LRP5/6) are coreceptors for Wnt growth factors, and also bind Dkk proteins, secreted inhibitors of Wnt signaling.
22000856	0	11	theme	inhibition	34:43	arg1	basis					11:15	Structural basis	0:15	Structural basis of Wnt signaling inhibition by Dickkopf binding to LRP5/6.	0:74	Structural basis of Wnt signaling inhibition by Dickkopf binding to LRP5/6.
22000856	1	12	theme	growth	147:152	arg1	factors					154:160	Wnt growth factors	143:160	Wnt growth factors	143:160	LDL receptor-related proteins 5 and 6 (LRP5/6) are coreceptors for Wnt growth factors, and also bind Dkk proteins, secreted inhibitors of Wnt signaling.
22000856	0	13	theme	Structural	0:9	arg1	basis					11:15	Structural basis	0:15	Structural basis of Wnt signaling inhibition by Dickkopf binding to LRP5/6.	0:74	Structural basis of Wnt signaling inhibition by Dickkopf binding to LRP5/6.
22000856	6	14	theme	similar	1013:1019	arg1	relationship					1029:1040	a similar spatial relationship	1011:1040	a similar spatial relationship to Frizzled coreceptors	1011:1064	Thus, Wnts bound to either portion of the LRP6 ectodomain likely bear a similar spatial relationship to Frizzled coreceptors.
22000856	1	15	theme	receptor-related	80:95	arg1	coreceptors					127:137	coreceptors	127:137	coreceptors for Wnt growth factors	127:160	LDL receptor-related proteins 5 and 6 (LRP5/6) are coreceptors for Wnt growth factors, and also bind Dkk proteins, secreted inhibitors of Wnt signaling.
22000856	1	15	theme	receptor-related	80:95	arg1	proteins					97:104	LDL receptor-related proteins	76:104	LDL receptor-related proteins 5 and 6 (LRP5/6)	76:121	LDL receptor-related proteins 5 and 6 (LRP5/6) are coreceptors for Wnt growth factors, and also bind Dkk proteins, secreted inhibitors of Wnt signaling.
22000856	0	16	theme	Wnt	20:22	arg1	inhibition					34:43	Wnt signaling inhibition	20:43	Wnt signaling inhibition	20:43	Structural basis of Wnt signaling inhibition by Dickkopf binding to LRP5/6.
22000856	5	17	theme	curved	839:844	arg1	conformation					846:857	a curved conformation	837:857	a curved conformation that places the first three repeats at a similar height relative to the membrane	837:938	Small-angle X-ray scattering analysis of LRP6(1-4) bound to a noninhibitory antibody fragment or to full-length Dkk1 shows that in both cases the ectodomain adopts a curved conformation that places the first three repeats at a similar height relative to the membrane.
22000856	2	18	theme	β-propeller/EGF-like	265:284	arg1	repeats					293:299	four β-propeller/EGF-like domain repeats	260:299	four β-propeller/EGF-like domain repeats	260:299	The LRP5/6 ectodomain contains four β-propeller/EGF-like domain repeats.
22000856	5	19	theme	scattering	691:700	arg1	analysis					702:709	Small-angle X-ray scattering analysis	673:709	Small-angle X-ray scattering analysis of LRP6(1-4) bound to a noninhibitory antibody fragment or to full-length Dkk1	673:788	Small-angle X-ray scattering analysis of LRP6(1-4) bound to a noninhibitory antibody fragment or to full-length Dkk1 shows that in both cases the ectodomain adopts a curved conformation that places the first three repeats at a similar height relative to the membrane.
22000856	2	20	theme	domain	286:291	arg1	repeats					293:299	four β-propeller/EGF-like domain repeats	260:299	four β-propeller/EGF-like domain repeats	260:299	The LRP5/6 ectodomain contains four β-propeller/EGF-like domain repeats.
22000856	4	21	theme	ectodomain	626:635	arg1	portions					605:612	both portions	600:612	both portions of the LRP6 ectodomain	600:635	We present the crystal structure of the Dkk1 C-terminal domain bound to LRP6(3-4), and show that the Dkk1 N-terminal domain binds to LRP6(1-2), demonstrating that a single Dkk1 molecule can bind to both portions of the LRP6 ectodomain and thereby inhibit different Wnts.
22000856	5	22	theme	similar	900:906	arg1	height					908:913	a similar height	898:913	a similar height relative to the membrane	898:938	Small-angle X-ray scattering analysis of LRP6(1-4) bound to a noninhibitory antibody fragment or to full-length Dkk1 shows that in both cases the ectodomain adopts a curved conformation that places the first three repeats at a similar height relative to the membrane.
22000856	5	23	theme	Small-angle	673:683	arg1	scattering					691:700	Small-angle X-ray scattering	673:700	Small-angle X-ray scattering analysis of LRP6(1-4) bound to a noninhibitory antibody fragment or to full-length Dkk1	673:788	Small-angle X-ray scattering analysis of LRP6(1-4) bound to a noninhibitory antibody fragment or to full-length Dkk1 shows that in both cases the ectodomain adopts a curved conformation that places the first three repeats at a similar height relative to the membrane.
22000856	3	24	theme	other	390:394	arg1	Wnts					396:399	other Wnts	390:399	other Wnts	390:399	The first two repeats, LRP6(1-2), bind to several Wnt variants, whereas LRP6(3-4) binds other Wnts.
22000856	3	25	theme	Wnt	352:354	arg1	variants					356:363	several Wnt variants	344:363	several Wnt variants	344:363	The first two repeats, LRP6(1-2), bind to several Wnt variants, whereas LRP6(3-4) binds other Wnts.
22000856	2	26	contain	contains	251:258	arg1	ectodomain					240:249	The LRP5/6 ectodomain	229:249	The LRP5/6 ectodomain	229:249	The LRP5/6 ectodomain contains four β-propeller/EGF-like domain repeats.
22000856	2	26	contain	contains	251:258	arg2	repeats					293:299	four β-propeller/EGF-like domain repeats	260:299	four β-propeller/EGF-like domain repeats	260:299	The LRP5/6 ectodomain contains four β-propeller/EGF-like domain repeats.
22000856	0	27	theme	signaling	24:32	arg1	inhibition					34:43	Wnt signaling inhibition	20:43	Wnt signaling inhibition	20:43	Structural basis of Wnt signaling inhibition by Dickkopf binding to LRP5/6.
22000856	4	28	theme	Dkk1	442:445	arg1	domain					458:463	the Dkk1 C-terminal domain	438:463	the Dkk1 C-terminal domain bound to LRP6(3-4)	438:482	We present the crystal structure of the Dkk1 C-terminal domain bound to LRP6(3-4), and show that the Dkk1 N-terminal domain binds to LRP6(1-2), demonstrating that a single Dkk1 molecule can bind to both portions of the LRP6 ectodomain and thereby inhibit different Wnts.
22000856	5	29	theme	relative	915:922	arg1	height					908:913	a similar height	898:913	a similar height relative to the membrane	898:938	Small-angle X-ray scattering analysis of LRP6(1-4) bound to a noninhibitory antibody fragment or to full-length Dkk1 shows that in both cases the ectodomain adopts a curved conformation that places the first three repeats at a similar height relative to the membrane.
22000856	4	30	theme	Dkk1	503:506	arg1	domain					519:524	the Dkk1 N-terminal domain	499:524	the Dkk1 N-terminal domain	499:524	We present the crystal structure of the Dkk1 C-terminal domain bound to LRP6(3-4), and show that the Dkk1 N-terminal domain binds to LRP6(1-2), demonstrating that a single Dkk1 molecule can bind to both portions of the LRP6 ectodomain and thereby inhibit different Wnts.
22000856	1	31	theme	Dkk	177:179	arg1	proteins					181:188	Dkk proteins	177:188	Dkk proteins	177:188	LDL receptor-related proteins 5 and 6 (LRP5/6) are coreceptors for Wnt growth factors, and also bind Dkk proteins, secreted inhibitors of Wnt signaling.
22000856	1	31	theme	Dkk	177:179	arg1	inhibitors					200:209	secreted inhibitors	191:209	secreted inhibitors of Wnt signaling	191:226	LDL receptor-related proteins 5 and 6 (LRP5/6) are coreceptors for Wnt growth factors, and also bind Dkk proteins, secreted inhibitors of Wnt signaling.
22000856	0	32	theme	Dickkopf	48:55	arg1	binding					57:63	Dickkopf binding	48:63	Dickkopf binding to LRP5/6	48:73	Structural basis of Wnt signaling inhibition by Dickkopf binding to LRP5/6.
22000856	3	33	dep	LRP6	374:377	arg1	3-4					379:381	3-4	379:381	3-4	379:381	The first two repeats, LRP6(1-2), bind to several Wnt variants, whereas LRP6(3-4) binds other Wnts.
22000856	4	34	theme	Dkk1	574:577	arg1	molecule					579:586	a single Dkk1 molecule	565:586	a single Dkk1 molecule	565:586	We present the crystal structure of the Dkk1 C-terminal domain bound to LRP6(3-4), and show that the Dkk1 N-terminal domain binds to LRP6(1-2), demonstrating that a single Dkk1 molecule can bind to both portions of the LRP6 ectodomain and thereby inhibit different Wnts.
22000856	3	35	theme	several	344:350	arg1	variants					356:363	several Wnt variants	344:363	several Wnt variants	344:363	The first two repeats, LRP6(1-2), bind to several Wnt variants, whereas LRP6(3-4) binds other Wnts.
22000856	4	36	theme	domain	458:463	arg1	structure					425:433	the crystal structure	413:433	the crystal structure of the Dkk1 C-terminal domain bound to LRP6(3-4)	413:482	We present the crystal structure of the Dkk1 C-terminal domain bound to LRP6(3-4), and show that the Dkk1 N-terminal domain binds to LRP6(1-2), demonstrating that a single Dkk1 molecule can bind to both portions of the LRP6 ectodomain and thereby inhibit different Wnts.
22000856	5	37	theme	first	875:879	arg1	repeats					887:893	the first three repeats	871:893	the first three repeats	871:893	Small-angle X-ray scattering analysis of LRP6(1-4) bound to a noninhibitory antibody fragment or to full-length Dkk1 shows that in both cases the ectodomain adopts a curved conformation that places the first three repeats at a similar height relative to the membrane.
22000856	4	38	theme	single	567:572	arg1	molecule					579:586	a single Dkk1 molecule	565:586	a single Dkk1 molecule	565:586	We present the crystal structure of the Dkk1 C-terminal domain bound to LRP6(3-4), and show that the Dkk1 N-terminal domain binds to LRP6(1-2), demonstrating that a single Dkk1 molecule can bind to both portions of the LRP6 ectodomain and thereby inhibit different Wnts.
22000856	4	39	theme	C-terminal	447:456	arg1	domain					458:463	the Dkk1 C-terminal domain	438:463	the Dkk1 C-terminal domain bound to LRP6(3-4)	438:482	We present the crystal structure of the Dkk1 C-terminal domain bound to LRP6(3-4), and show that the Dkk1 N-terminal domain binds to LRP6(1-2), demonstrating that a single Dkk1 molecule can bind to both portions of the LRP6 ectodomain and thereby inhibit different Wnts.
22000856	6	40	theme	spatial	1021:1027	arg1	relationship					1029:1040	a similar spatial relationship	1011:1040	a similar spatial relationship to Frizzled coreceptors	1011:1064	Thus, Wnts bound to either portion of the LRP6 ectodomain likely bear a similar spatial relationship to Frizzled coreceptors.
22000856	4	41	dep	bind	592:595	arg1	inhibit					649:655	inhibit	649:655	inhibit different Wnts	649:670	We present the crystal structure of the Dkk1 C-terminal domain bound to LRP6(3-4), and show that the Dkk1 N-terminal domain binds to LRP6(1-2), demonstrating that a single Dkk1 molecule can bind to both portions of the LRP6 ectodomain and thereby inhibit different Wnts.
22000856	3	42	theme	first	306:310	arg1	LRP6					325:328	LRP6	325:328	LRP6	325:328	The first two repeats, LRP6(1-2), bind to several Wnt variants, whereas LRP6(3-4) binds other Wnts.
22000856	3	42	theme	first	306:310	arg1	repeats					316:322	The first two repeats	302:322	The first two repeats	302:322	The first two repeats, LRP6(1-2), bind to several Wnt variants, whereas LRP6(3-4) binds other Wnts.
22000856	5	43	theme	LRP6	714:717	arg1	analysis					702:709	Small-angle X-ray scattering analysis	673:709	Small-angle X-ray scattering analysis of LRP6(1-4) bound to a noninhibitory antibody fragment or to full-length Dkk1	673:788	Small-angle X-ray scattering analysis of LRP6(1-4) bound to a noninhibitory antibody fragment or to full-length Dkk1 shows that in both cases the ectodomain adopts a curved conformation that places the first three repeats at a similar height relative to the membrane.
22000856	4	44	theme	different	657:665	arg1	Wnts					667:670	different Wnts	657:670	different Wnts	657:670	We present the crystal structure of the Dkk1 C-terminal domain bound to LRP6(3-4), and show that the Dkk1 N-terminal domain binds to LRP6(1-2), demonstrating that a single Dkk1 molecule can bind to both portions of the LRP6 ectodomain and thereby inhibit different Wnts.
22000856	1	45	dep	proteins	97:104	arg1	LRP5/6					115:120	LRP5/6	115:120	LRP5/6	115:120	LDL receptor-related proteins 5 and 6 (LRP5/6) are coreceptors for Wnt growth factors, and also bind Dkk proteins, secreted inhibitors of Wnt signaling.
22000856	1	45	dep	proteins	97:104	arg1	6					112:112	6	112:112	6	112:112	LDL receptor-related proteins 5 and 6 (LRP5/6) are coreceptors for Wnt growth factors, and also bind Dkk proteins, secreted inhibitors of Wnt signaling.
22000856	1	45	dep	proteins	97:104	arg1	5					106:106	5	106:106	5	106:106	LDL receptor-related proteins 5 and 6 (LRP5/6) are coreceptors for Wnt growth factors, and also bind Dkk proteins, secreted inhibitors of Wnt signaling.
22000856	6	46	theme	ectodomain	988:997	arg1	portion					968:974	either portion	961:974	either portion of the LRP6 ectodomain	961:997	Thus, Wnts bound to either portion of the LRP6 ectodomain likely bear a similar spatial relationship to Frizzled coreceptors.
22000856	1	47	theme	secreted	191:198	arg1	proteins					181:188	Dkk proteins	177:188	Dkk proteins	177:188	LDL receptor-related proteins 5 and 6 (LRP5/6) are coreceptors for Wnt growth factors, and also bind Dkk proteins, secreted inhibitors of Wnt signaling.
22000856	1	47	theme	secreted	191:198	arg1	inhibitors					200:209	secreted inhibitors	191:209	secreted inhibitors of Wnt signaling	191:226	LDL receptor-related proteins 5 and 6 (LRP5/6) are coreceptors for Wnt growth factors, and also bind Dkk proteins, secreted inhibitors of Wnt signaling.
22000856	4	48	theme	crystal	417:423	arg1	structure					425:433	the crystal structure	413:433	the crystal structure of the Dkk1 C-terminal domain bound to LRP6(3-4)	413:482	We present the crystal structure of the Dkk1 C-terminal domain bound to LRP6(3-4), and show that the Dkk1 N-terminal domain binds to LRP6(1-2), demonstrating that a single Dkk1 molecule can bind to both portions of the LRP6 ectodomain and thereby inhibit different Wnts.
22000856	5	49	theme	X-ray	685:689	arg1	scattering					691:700	Small-angle X-ray scattering	673:700	Small-angle X-ray scattering analysis of LRP6(1-4) bound to a noninhibitory antibody fragment or to full-length Dkk1	673:788	Small-angle X-ray scattering analysis of LRP6(1-4) bound to a noninhibitory antibody fragment or to full-length Dkk1 shows that in both cases the ectodomain adopts a curved conformation that places the first three repeats at a similar height relative to the membrane.
22000856	6	50	contain	bear	1006:1009	arg1	Wnts					947:950	Wnts	947:950	Wnts bound to either portion of the LRP6 ectodomain	947:997	Thus, Wnts bound to either portion of the LRP6 ectodomain likely bear a similar spatial relationship to Frizzled coreceptors.
22000856	6	50	contain	bear	1006:1009	arg2	relationship					1029:1040	a similar spatial relationship	1011:1040	a similar spatial relationship to Frizzled coreceptors	1011:1064	Thus, Wnts bound to either portion of the LRP6 ectodomain likely bear a similar spatial relationship to Frizzled coreceptors.
486087	0	0	theme	subcomponent	76:87	arg1	C1q					89:91	subcomponent C1q	76:91	subcomponent C1q of the first component of human complement	76:134	Complete amino acid sequences of the three collagen-like regions present in subcomponent C1q of the first component of human complement.
486087	7	1	contain	have	764:767	arg2	residues					777:784	alanine residues	769:784	alanine residues	769:784	The B- and C-chains have alanine residues at positions B-9 and C-36 where glycine might be expected.
486087	7	1	contain	have	764:767	arg1	C-chains					755:762	C-chains	755:762	C-chains	755:762	The B- and C-chains have alanine residues at positions B-9 and C-36 where glycine might be expected.
486087	7	1	contain	have	764:767	arg1	B-					748:749	B-	748:749	B-	748:749	The B- and C-chains have alanine residues at positions B-9 and C-36 where glycine might be expected.
486087	2	2	theme	sequence	317:324	arg1	data					326:329	previously published sequence data [Reid (1974)	296:342	previously published sequence data [Reid (1974)	296:342	These results, along with previously published sequence data [Reid (1974) Biochem.J.
486087	5	3	with	presentation	467:478	arg1	other					506:510	other	506:510	other	506:510	173, 863--868] allow the presentation, and comparison with each other, of the complete amino acid sequences of the collagen-like regions found in the A-, B- and C-chains of human subcomponent C1q.
486087	6	4	theme	triplet	708:714	arg1	sequence					727:734	its collagen-like Gly-X-Y repeating triplet amino acid sequence	672:734	its collagen-like Gly-X-Y repeating triplet amino acid sequence broken	672:741	Each chain has the continuity of its collagen-like Gly-X-Y repeating triplet amino acid sequence broken.
486087	2	5	theme	published	307:315	arg1	data					326:329	previously published sequence data [Reid (1974)	296:342	previously published sequence data [Reid (1974)	296:342	These results, along with previously published sequence data [Reid (1974) Biochem.J.
486087	1	6	theme	C-chain	224:230	arg1	residues					165:172	amino acid residues	154:172	amino acid residues	154:172	The sequences of amino acid residues 38--51 of the A-chain, and residues 42--90 of the C-chain, of human subcomponent C1q are given.
486087	1	6	theme	C-chain	224:230	arg1	C-chain					224:230	the C-chain	220:230	the C-chain	220:230	The sequences of amino acid residues 38--51 of the A-chain, and residues 42--90 of the C-chain, of human subcomponent C1q are given.
486087	1	6	theme	C-chain	224:230	arg1	residues					201:208	residues 42--90	201:215	residues 42--90	201:215	The sequences of amino acid residues 38--51 of the A-chain, and residues 42--90 of the C-chain, of human subcomponent C1q are given.
486087	5	7	theme	collagen-like	557:569	arg1	regions					571:577	the collagen-like regions	553:577	the collagen-like regions found in the A-, B- and C-chains of human subcomponent C1q	553:636	173, 863--868] allow the presentation, and comparison with each other, of the complete amino acid sequences of the collagen-like regions found in the A-, B- and C-chains of human subcomponent C1q.
486087	6	8	theme	repeating	698:706	arg1	sequence					727:734	its collagen-like Gly-X-Y repeating triplet amino acid sequence	672:734	its collagen-like Gly-X-Y repeating triplet amino acid sequence broken	672:741	Each chain has the continuity of its collagen-like Gly-X-Y repeating triplet amino acid sequence broken.
486087	5	9	theme	human	615:619	arg1	C1q					634:636	human subcomponent C1q	615:636	human subcomponent C1q	615:636	173, 863--868] allow the presentation, and comparison with each other, of the complete amino acid sequences of the collagen-like regions found in the A-, B- and C-chains of human subcomponent C1q.
486087	5	10	theme	regions	571:577	arg1	sequences					540:548	the complete amino acid sequences	516:548	the complete amino acid sequences of the collagen-like regions found in the A-, B- and C-chains of human subcomponent C1q	516:636	173, 863--868] allow the presentation, and comparison with each other, of the complete amino acid sequences of the collagen-like regions found in the A-, B- and C-chains of human subcomponent C1q.
486087	6	11	theme	Gly-X-Y	690:696	arg1	sequence					727:734	its collagen-like Gly-X-Y repeating triplet amino acid sequence	672:734	its collagen-like Gly-X-Y repeating triplet amino acid sequence broken	672:741	Each chain has the continuity of its collagen-like Gly-X-Y repeating triplet amino acid sequence broken.
486087	5	12	dep	presentation	467:478	arg1	the					463:465	the	463:465	the	463:465	173, 863--868] allow the presentation, and comparison with each other, of the complete amino acid sequences of the collagen-like regions found in the A-, B- and C-chains of human subcomponent C1q.
486087	8	13	contain	has	857:859	arg1	A-chain					849:855	The A-chain	845:855	The A-chain	845:855	The A-chain has a threonine residue at position A-39, which is located between two Gly-X-Y triplets.
486087	8	13	contain	has	857:859	arg2	located					908:914	located	908:914	located	908:914	The A-chain has a threonine residue at position A-39, which is located between two Gly-X-Y triplets.
486087	8	13	contain	has	857:859	arg2	residue					873:879	a threonine residue	861:879	a threonine residue	861:879	The A-chain has a threonine residue at position A-39, which is located between two Gly-X-Y triplets.
486087	0	14	theme	first	100:104	arg1	component					106:114	the first component	96:114	the first component of human complement	96:134	Complete amino acid sequences of the three collagen-like regions present in subcomponent C1q of the first component of human complement.
486087	3	15	dep	141	355:357	arg1	1977					376:379	1977	376:379	1977	376:379	141, 189--203; Reid (1977) Biochem.J.
486087	3	15	dep	141	355:357	arg1	Reid					370:373	Reid	370:373	Reid	370:373	141, 189--203; Reid (1977) Biochem.J.
486087	3	15	dep	141	355:357	arg1	Biochem.J.					382:391	Biochem.J.	382:391	Biochem.J.	382:391	141, 189--203; Reid (1977) Biochem.J.
486087	6	16	theme	collagen-like	676:688	arg1	sequence					727:734	its collagen-like Gly-X-Y repeating triplet amino acid sequence	672:734	its collagen-like Gly-X-Y repeating triplet amino acid sequence broken	672:741	Each chain has the continuity of its collagen-like Gly-X-Y repeating triplet amino acid sequence broken.
486087	1	17	theme	amino	154:158	arg1	residues					165:172	amino acid residues	154:172	amino acid residues	154:172	The sequences of amino acid residues 38--51 of the A-chain, and residues 42--90 of the C-chain, of human subcomponent C1q are given.
486087	1	17	theme	amino	154:158	arg1	C-chain					224:230	the C-chain	220:230	the C-chain	220:230	The sequences of amino acid residues 38--51 of the A-chain, and residues 42--90 of the C-chain, of human subcomponent C1q are given.
486087	5	18	theme	C1q	634:636	arg1	B-					596:597	B-	596:597	B-	596:597	173, 863--868] allow the presentation, and comparison with each other, of the complete amino acid sequences of the collagen-like regions found in the A-, B- and C-chains of human subcomponent C1q.
486087	5	18	theme	C1q	634:636	arg1	A-					592:593	A-	592:593	A-	592:593	173, 863--868] allow the presentation, and comparison with each other, of the complete amino acid sequences of the collagen-like regions found in the A-, B- and C-chains of human subcomponent C1q.
486087	5	18	theme	C1q	634:636	arg1	C-chains					603:610	C-chains	603:610	C-chains	603:610	173, 863--868] allow the presentation, and comparison with each other, of the complete amino acid sequences of the collagen-like regions found in the A-, B- and C-chains of human subcomponent C1q.
486087	5	19	theme	amino	529:533	arg1	sequences					540:548	the complete amino acid sequences	516:548	the complete amino acid sequences of the collagen-like regions found in the A-, B- and C-chains of human subcomponent C1q	516:636	173, 863--868] allow the presentation, and comparison with each other, of the complete amino acid sequences of the collagen-like regions found in the A-, B- and C-chains of human subcomponent C1q.
486087	2	20	dep	data	326:329	arg1	1974					338:341	1974	338:341	1974	338:341	These results, along with previously published sequence data [Reid (1974) Biochem.J.
486087	2	20	dep	data	326:329	arg1	[Reid					331:335	[Reid	331:335	previously published sequence data [Reid (1974)	296:342	These results, along with previously published sequence data [Reid (1974) Biochem.J.
486087	1	21	theme	acid	160:163	arg1	residues					165:172	amino acid residues	154:172	amino acid residues	154:172	The sequences of amino acid residues 38--51 of the A-chain, and residues 42--90 of the C-chain, of human subcomponent C1q are given.
486087	1	21	theme	acid	160:163	arg1	C-chain					224:230	the C-chain	220:230	the C-chain	220:230	The sequences of amino acid residues 38--51 of the A-chain, and residues 42--90 of the C-chain, of human subcomponent C1q are given.
486087	0	22	theme	amino	9:13	arg1	sequences					20:28	Complete amino acid sequences	0:28	Complete amino acid sequences of the three collagen-like regions	0:63	Complete amino acid sequences of the three collagen-like regions present in subcomponent C1q of the first component of human complement.
486087	5	23	theme	acid	535:538	arg1	sequences					540:548	the complete amino acid sequences	516:548	the complete amino acid sequences of the collagen-like regions found in the A-, B- and C-chains of human subcomponent C1q	516:636	173, 863--868] allow the presentation, and comparison with each other, of the complete amino acid sequences of the collagen-like regions found in the A-, B- and C-chains of human subcomponent C1q.
486087	2	24	dep	along	285:289	arg1	with					291:294	with	291:294	with	291:294	These results, along with previously published sequence data [Reid (1974) Biochem.J.
486087	1	25	theme	residues	165:172	arg1	sequences					141:149	The sequences	137:149	The sequences	137:149	The sequences of amino acid residues 38--51 of the A-chain, and residues 42--90 of the C-chain, of human subcomponent C1q are given.
486087	0	26	theme	Complete	0:7	arg1	sequences					20:28	Complete amino acid sequences	0:28	Complete amino acid sequences of the three collagen-like regions	0:63	Complete amino acid sequences of the three collagen-like regions present in subcomponent C1q of the first component of human complement.
486087	1	27	theme	human	236:240	arg1	C1q					255:257	human subcomponent C1q	236:257	human subcomponent C1q	236:257	The sequences of amino acid residues 38--51 of the A-chain, and residues 42--90 of the C-chain, of human subcomponent C1q are given.
486087	5	28	theme	sequences	540:548	arg1	presentation					467:478	presentation	467:478	presentation	467:478	173, 863--868] allow the presentation, and comparison with each other, of the complete amino acid sequences of the collagen-like regions found in the A-, B- and C-chains of human subcomponent C1q.
486087	5	28	theme	sequences	540:548	arg1	comparison					485:494	comparison	485:494	comparison with each other	485:510	173, 863--868] allow the presentation, and comparison with each other, of the complete amino acid sequences of the collagen-like regions found in the A-, B- and C-chains of human subcomponent C1q.
486087	5	29	theme	complete	520:527	arg1	sequences					540:548	the complete amino acid sequences	516:548	the complete amino acid sequences of the collagen-like regions found in the A-, B- and C-chains of human subcomponent C1q	516:636	173, 863--868] allow the presentation, and comparison with each other, of the complete amino acid sequences of the collagen-like regions found in the A-, B- and C-chains of human subcomponent C1q.
486087	1	30	theme	subcomponent	242:253	arg1	C1q					255:257	human subcomponent C1q	236:257	human subcomponent C1q	236:257	The sequences of amino acid residues 38--51 of the A-chain, and residues 42--90 of the C-chain, of human subcomponent C1q are given.
486087	5	31	located	found	579:583	arg2	regions					571:577	the collagen-like regions	553:577	the collagen-like regions found in the A-, B- and C-chains of human subcomponent C1q	553:636	173, 863--868] allow the presentation, and comparison with each other, of the complete amino acid sequences of the collagen-like regions found in the A-, B- and C-chains of human subcomponent C1q.
486087	5	31	located	found	579:583	arg1	B-					596:597	B-	596:597	B-	596:597	173, 863--868] allow the presentation, and comparison with each other, of the complete amino acid sequences of the collagen-like regions found in the A-, B- and C-chains of human subcomponent C1q.
486087	5	31	located	found	579:583	arg1	A-					592:593	A-	592:593	A-	592:593	173, 863--868] allow the presentation, and comparison with each other, of the complete amino acid sequences of the collagen-like regions found in the A-, B- and C-chains of human subcomponent C1q.
486087	5	31	located	found	579:583	arg1	C-chains					603:610	C-chains	603:610	C-chains	603:610	173, 863--868] allow the presentation, and comparison with each other, of the complete amino acid sequences of the collagen-like regions found in the A-, B- and C-chains of human subcomponent C1q.
486087	0	32	theme	acid	15:18	arg1	sequences					20:28	Complete amino acid sequences	0:28	Complete amino acid sequences of the three collagen-like regions	0:63	Complete amino acid sequences of the three collagen-like regions present in subcomponent C1q of the first component of human complement.
486087	1	33	theme	C1q	255:257	arg1	sequences					141:149	The sequences	137:149	The sequences	137:149	The sequences of amino acid residues 38--51 of the A-chain, and residues 42--90 of the C-chain, of human subcomponent C1q are given.
486087	0	34	theme	component	106:114	arg1	C1q					89:91	subcomponent C1q	76:91	subcomponent C1q of the first component of human complement	76:134	Complete amino acid sequences of the three collagen-like regions present in subcomponent C1q of the first component of human complement.
486087	5	35	dep	173	442:444	arg1	863--868					447:454	863--868	447:454	863--868	447:454	173, 863--868] allow the presentation, and comparison with each other, of the complete amino acid sequences of the collagen-like regions found in the A-, B- and C-chains of human subcomponent C1q.
486087	5	36	with	comparison	485:494	arg1	other					506:510	other	506:510	other	506:510	173, 863--868] allow the presentation, and comparison with each other, of the complete amino acid sequences of the collagen-like regions found in the A-, B- and C-chains of human subcomponent C1q.
486087	0	37	theme	complement	125:134	arg1	component					106:114	the first component	96:114	the first component of human complement	96:134	Complete amino acid sequences of the three collagen-like regions present in subcomponent C1q of the first component of human complement.
486087	1	38	dep	residues	165:172	arg1	38--51					174:179	38--51	174:179	38--51	174:179	The sequences of amino acid residues 38--51 of the A-chain, and residues 42--90 of the C-chain, of human subcomponent C1q are given.
486087	1	38	dep	residues	165:172	arg1	A-chain					188:194	the A-chain	184:194	the A-chain	184:194	The sequences of amino acid residues 38--51 of the A-chain, and residues 42--90 of the C-chain, of human subcomponent C1q are given.
486087	1	39	theme	A-chain	188:194	arg1	38--51					174:179	38--51	174:179	38--51	174:179	The sequences of amino acid residues 38--51 of the A-chain, and residues 42--90 of the C-chain, of human subcomponent C1q are given.
486087	1	39	theme	A-chain	188:194	arg1	A-chain					188:194	the A-chain	184:194	the A-chain	184:194	The sequences of amino acid residues 38--51 of the A-chain, and residues 42--90 of the C-chain, of human subcomponent C1q are given.
486087	8	40	theme	threonine	863:871	arg1	located					908:914	located	908:914	located	908:914	The A-chain has a threonine residue at position A-39, which is located between two Gly-X-Y triplets.
486087	8	40	theme	threonine	863:871	arg1	residue					873:879	a threonine residue	861:879	a threonine residue	861:879	The A-chain has a threonine residue at position A-39, which is located between two Gly-X-Y triplets.
486087	0	41	theme	human	119:123	arg1	complement					125:134	human complement	119:134	human complement	119:134	Complete amino acid sequences of the three collagen-like regions present in subcomponent C1q of the first component of human complement.
486087	0	42	theme	collagen-like	43:55	arg1	regions					57:63	the three collagen-like regions	33:63	the three collagen-like regions	33:63	Complete amino acid sequences of the three collagen-like regions present in subcomponent C1q of the first component of human complement.
486087	0	43	attach	present	65:71	arg2	sequences					20:28	Complete amino acid sequences	0:28	Complete amino acid sequences of the three collagen-like regions	0:63	Complete amino acid sequences of the three collagen-like regions present in subcomponent C1q of the first component of human complement.
486087	0	43	attach	present	65:71	arg1	C1q					89:91	subcomponent C1q	76:91	subcomponent C1q of the first component of human complement	76:134	Complete amino acid sequences of the three collagen-like regions present in subcomponent C1q of the first component of human complement.
486087	7	44	dep	B-	748:749	arg1	The					744:746	The	744:746	The	744:746	The B- and C-chains have alanine residues at positions B-9 and C-36 where glycine might be expected.
486087	6	45	theme	sequence	727:734	arg1	continuity					658:667	the continuity	654:667	the continuity of its collagen-like Gly-X-Y repeating triplet amino acid sequence broken	654:741	Each chain has the continuity of its collagen-like Gly-X-Y repeating triplet amino acid sequence broken.
486087	7	46	dep	positions	789:797	arg1	positions					789:797	positions B-9 and C-36	789:810	positions B-9 and C-36 where glycine might be expected	789:842	The B- and C-chains have alanine residues at positions B-9 and C-36 where glycine might be expected.
486087	7	46	dep	positions	789:797	arg1	C-36					807:810	C-36	807:810	C-36	807:810	The B- and C-chains have alanine residues at positions B-9 and C-36 where glycine might be expected.
486087	7	46	dep	positions	789:797	arg1	B-9					799:801	B-9	799:801	B-9	799:801	The B- and C-chains have alanine residues at positions B-9 and C-36 where glycine might be expected.
486087	2	47	dep	results	276:282	arg1	Biochem.J.					344:353	Biochem.J.	344:353	Biochem.J.	344:353	These results, along with previously published sequence data [Reid (1974) Biochem.J.
486087	5	48	theme	subcomponent	621:632	arg1	C1q					634:636	human subcomponent C1q	615:636	human subcomponent C1q	615:636	173, 863--868] allow the presentation, and comparison with each other, of the complete amino acid sequences of the collagen-like regions found in the A-, B- and C-chains of human subcomponent C1q.
486087	6	49	theme	acid	722:725	arg1	sequence					727:734	its collagen-like Gly-X-Y repeating triplet amino acid sequence	672:734	its collagen-like Gly-X-Y repeating triplet amino acid sequence broken	672:741	Each chain has the continuity of its collagen-like Gly-X-Y repeating triplet amino acid sequence broken.
486087	1	50	theme	residues	201:208	arg1	sequences					141:149	The sequences	137:149	The sequences	137:149	The sequences of amino acid residues 38--51 of the A-chain, and residues 42--90 of the C-chain, of human subcomponent C1q are given.
486087	8	51	theme	Gly-X-Y	928:934	arg1	triplets					936:943	two Gly-X-Y triplets	924:943	two Gly-X-Y triplets	924:943	The A-chain has a threonine residue at position A-39, which is located between two Gly-X-Y triplets.
486087	6	52	theme	amino	716:720	arg1	sequence					727:734	its collagen-like Gly-X-Y repeating triplet amino acid sequence	672:734	its collagen-like Gly-X-Y repeating triplet amino acid sequence broken	672:741	Each chain has the continuity of its collagen-like Gly-X-Y repeating triplet amino acid sequence broken.
486087	0	53	theme	regions	57:63	arg1	sequences					20:28	Complete amino acid sequences	0:28	Complete amino acid sequences of the three collagen-like regions	0:63	Complete amino acid sequences of the three collagen-like regions present in subcomponent C1q of the first component of human complement.
486087	6	54	contain	has	650:652	arg1	chain					644:648	Each chain	639:648	Each chain	639:648	Each chain has the continuity of its collagen-like Gly-X-Y repeating triplet amino acid sequence broken.
486087	6	54	contain	has	650:652	arg2	continuity					658:667	the continuity	654:667	the continuity of its collagen-like Gly-X-Y repeating triplet amino acid sequence broken	654:741	Each chain has the continuity of its collagen-like Gly-X-Y repeating triplet amino acid sequence broken.
486087	8	55	from	position	884:891	arg1	located					908:914	located	908:914	located	908:914	The A-chain has a threonine residue at position A-39, which is located between two Gly-X-Y triplets.
486087	8	55	from	position	884:891	arg1	residue					873:879	a threonine residue	861:879	a threonine residue	861:879	The A-chain has a threonine residue at position A-39, which is located between two Gly-X-Y triplets.
486087	7	56	theme	alanine	769:775	arg1	residues					777:784	alanine residues	769:784	alanine residues	769:784	The B- and C-chains have alanine residues at positions B-9 and C-36 where glycine might be expected.
24125761	7	0	dep	N282Q	944:948	arg1	substitutions					969:981	substitutions	969:981	substitutions	969:981	Mutant types of AADAC with the N282Q and the N78Q/N282Q substitutions showed dramatically lower phenacetin hydrolase activity than did the wild-type protein.
24125761	7	1	theme	phenacetin	1009:1018	arg1	activity					1030:1037	dramatically lower phenacetin hydrolase activity	990:1037	dramatically lower phenacetin hydrolase activity	990:1037	Mutant types of AADAC with the N282Q and the N78Q/N282Q substitutions showed dramatically lower phenacetin hydrolase activity than did the wild-type protein.
24125761	11	2	theme	mutant	1403:1408	arg1	types					1410:1414	The mutant types	1399:1414	The mutant types of AADAC containing the N282Q and the N78Q/N282Q substitutions	1399:1477	The mutant types of AADAC containing the N282Q and the N78Q/N282Q substitutions were not detected by immunoblotting analysis after non-reducing SDS-PAGE, suggesting that the glycosylation of AADAC at N282 was important for proper protein folding.
24125761	4	3	theme	Immunoblot	381:390	arg1	analysis					392:399	Immunoblot analysis	381:399	Immunoblot analysis of mutant AADACs that contained an asparagine (N, Asn) to glutamine (Q, Gln) substitution at either residue 78 or 282 (N78Q or N282Q)	381:533	Immunoblot analysis of mutant AADACs that contained an asparagine (N, Asn) to glutamine (Q, Gln) substitution at either residue 78 or 282 (N78Q or N282Q) showed a different migration compared with the wild-type protein.
24125761	4	4	dep	asparagine	436:445	arg1	Asn					451:453	Asn	451:453	Asn	451:453	Immunoblot analysis of mutant AADACs that contained an asparagine (N, Asn) to glutamine (Q, Gln) substitution at either residue 78 or 282 (N78Q or N282Q) showed a different migration compared with the wild-type protein.
24125761	4	4	dep	asparagine	436:445	arg1	N					448:448	N	448:448	N	448:448	Immunoblot analysis of mutant AADACs that contained an asparagine (N, Asn) to glutamine (Q, Gln) substitution at either residue 78 or 282 (N78Q or N282Q) showed a different migration compared with the wild-type protein.
24125761	11	5	theme	non-reducing	1530:1541	arg1	SDS-PAGE					1543:1550	non-reducing SDS-PAGE	1530:1550	non-reducing SDS-PAGE	1530:1550	The mutant types of AADAC containing the N282Q and the N78Q/N282Q substitutions were not detected by immunoblotting analysis after non-reducing SDS-PAGE, suggesting that the glycosylation of AADAC at N282 was important for proper protein folding.
24125761	2	6	theme	glycosylation	258:270	arg1	role					250:253	the role	246:253	the role of glycosylation	246:270	AADAC is a glycoprotein, but the role of glycosylation remains unclear.
24125761	8	7	theme	wild-type	1088:1096	arg1	cells					1121:1125	wild-type AADAC-expressing HuH-7 cells	1088:1125	wild-type AADAC-expressing HuH-7 cells	1088:1125	The treatment of wild-type AADAC-expressing HuH-7 cells with tunicamycin, which produces unglycosylated protein, decreased AADAC enzyme activity.
24125761	1	8	theme	arylacetamide	107:119	arg1	AADAC					134:138	AADAC	134:138	AADAC	134:138	Human arylacetamide deacetylase (AADAC) can hydrolyze clinical drugs such as flutamide, phenacetin, and rifamycins.
24125761	1	8	theme	arylacetamide	107:119	arg1	deacetylase					121:131	Human arylacetamide deacetylase	101:131	Human arylacetamide deacetylase (AADAC)	101:139	Human arylacetamide deacetylase (AADAC) can hydrolyze clinical drugs such as flutamide, phenacetin, and rifamycins.
24125761	5	9	from	residue	660:666	arg1	substitutions					638:650	N to Q substitutions	631:650	N to Q substitutions at both residue 78 and 282 (N78Q/N282Q)	631:690	A mutant AADAC that contained N to Q substitutions at both residue 78 and 282 (N78Q/N282Q) showed a similar migration to AADAC in human liver microsomes (HLM) treated with endoglycosidase H (Endo H), which produces deglycosylated proteins.
24125761	5	10	theme	liver	737:741	arg1	microsomes					743:752	human liver microsomes	731:752	human liver microsomes (HLM) treated with endoglycosidase H (Endo H), which produces deglycosylated proteins	731:838	A mutant AADAC that contained N to Q substitutions at both residue 78 and 282 (N78Q/N282Q) showed a similar migration to AADAC in human liver microsomes (HLM) treated with endoglycosidase H (Endo H), which produces deglycosylated proteins.
24125761	5	10	theme	liver	737:741	arg1	HLM					755:757	HLM	755:757	HLM	755:757	A mutant AADAC that contained N to Q substitutions at both residue 78 and 282 (N78Q/N282Q) showed a similar migration to AADAC in human liver microsomes (HLM) treated with endoglycosidase H (Endo H), which produces deglycosylated proteins.
24125761	8	11	theme	HuH-7	1115:1119	arg1	cells					1121:1125	wild-type AADAC-expressing HuH-7 cells	1088:1125	wild-type AADAC-expressing HuH-7 cells	1088:1125	The treatment of wild-type AADAC-expressing HuH-7 cells with tunicamycin, which produces unglycosylated protein, decreased AADAC enzyme activity.
24125761	3	12	theme	present	296:302	arg1	study					304:308	the present study	292:308	the present study	292:308	In the present study, we investigated the effect of glycosylation on AADAC enzyme activity.
24125761	8	13	theme	enzyme	1200:1205	arg1	activity					1207:1214	AADAC enzyme activity	1194:1214	AADAC enzyme activity	1194:1214	The treatment of wild-type AADAC-expressing HuH-7 cells with tunicamycin, which produces unglycosylated protein, decreased AADAC enzyme activity.
24125761	8	14	gly	unglycosylated	1160:1173	arg1	protein					1175:1181	unglycosylated protein	1160:1181	unglycosylated protein	1160:1181	The treatment of wild-type AADAC-expressing HuH-7 cells with tunicamycin, which produces unglycosylated protein, decreased AADAC enzyme activity.
24125761	4	15	theme	AADACs	411:416	arg1	analysis					392:399	Immunoblot analysis	381:399	Immunoblot analysis of mutant AADACs that contained an asparagine (N, Asn) to glutamine (Q, Gln) substitution at either residue 78 or 282 (N78Q or N282Q)	381:533	Immunoblot analysis of mutant AADACs that contained an asparagine (N, Asn) to glutamine (Q, Gln) substitution at either residue 78 or 282 (N78Q or N282Q) showed a different migration compared with the wild-type protein.
24125761	9	16	with	treatment	1230:1238	arg1	H					1261:1261	Endo H	1256:1261	Endo H	1256:1261	However, the treatment of the HLM with Endo H caused no decrease of AADAC activity.
24125761	11	17	theme	proper	1622:1627	arg1	folding					1637:1643	proper protein folding	1622:1643	proper protein folding	1622:1643	The mutant types of AADAC containing the N282Q and the N78Q/N282Q substitutions were not detected by immunoblotting analysis after non-reducing SDS-PAGE, suggesting that the glycosylation of AADAC at N282 was important for proper protein folding.
24125761	7	18	theme	Mutant	913:918	arg1	types					920:924	Mutant types	913:924	Mutant types of AADAC with the N282Q and the N78Q/N282Q substitutions	913:981	Mutant types of AADAC with the N282Q and the N78Q/N282Q substitutions showed dramatically lower phenacetin hydrolase activity than did the wild-type protein.
24125761	0	19	theme	deacetylase	72:82	arg1	activity					91:98	human arylacetamide deacetylase enzyme activity	52:98	human arylacetamide deacetylase enzyme activity	52:98	N-Glycosylation during translation is essential for human arylacetamide deacetylase enzyme activity.
24125761	7	20	theme	wild-type	1052:1060	arg1	protein					1062:1068	the wild-type protein	1048:1068	the wild-type protein	1048:1068	Mutant types of AADAC with the N282Q and the N78Q/N282Q substitutions showed dramatically lower phenacetin hydrolase activity than did the wild-type protein.
24125761	11	21	contain	containing	1425:1434	arg1	AADAC					1419:1423	AADAC	1419:1423	AADAC containing the N282Q and the N78Q/N282Q substitutions	1419:1477	The mutant types of AADAC containing the N282Q and the N78Q/N282Q substitutions were not detected by immunoblotting analysis after non-reducing SDS-PAGE, suggesting that the glycosylation of AADAC at N282 was important for proper protein folding.
24125761	11	21	contain	containing	1425:1434	arg2	substitutions					1465:1477	the N282Q and the N78Q/N282Q substitutions	1436:1477	the N282Q and the N78Q/N282Q substitutions	1436:1477	The mutant types of AADAC containing the N282Q and the N78Q/N282Q substitutions were not detected by immunoblotting analysis after non-reducing SDS-PAGE, suggesting that the glycosylation of AADAC at N282 was important for proper protein folding.
24125761	11	22	from	N282	1599:1602	arg1	glycosylation					1573:1585	the glycosylation	1569:1585	the glycosylation of AADAC at N282	1569:1602	The mutant types of AADAC containing the N282Q and the N78Q/N282Q substitutions were not detected by immunoblotting analysis after non-reducing SDS-PAGE, suggesting that the glycosylation of AADAC at N282 was important for proper protein folding.
24125761	11	22	from	N282	1599:1602	arg1	important					1608:1616	important	1608:1616	important	1608:1616	The mutant types of AADAC containing the N282Q and the N78Q/N282Q substitutions were not detected by immunoblotting analysis after non-reducing SDS-PAGE, suggesting that the glycosylation of AADAC at N282 was important for proper protein folding.
24125761	12	23	theme	AADAC	1784:1788	arg1	activity					1797:1804	AADAC enzyme activity	1784:1804	AADAC enzyme activity	1784:1804	Overall, this study found that the translational, but not post-translational, N-glycosylation of AADAC plays a crucial role in regulating AADAC enzyme activity.
24125761	5	24	theme	Endo	792:795	arg1	H					789:789	endoglycosidase H	773:789	endoglycosidase H (Endo H)	773:798	A mutant AADAC that contained N to Q substitutions at both residue 78 and 282 (N78Q/N282Q) showed a similar migration to AADAC in human liver microsomes (HLM) treated with endoglycosidase H (Endo H), which produces deglycosylated proteins.
24125761	5	24	theme	Endo	792:795	arg1	H					797:797	Endo H	792:797	Endo H	792:797	A mutant AADAC that contained N to Q substitutions at both residue 78 and 282 (N78Q/N282Q) showed a similar migration to AADAC in human liver microsomes (HLM) treated with endoglycosidase H (Endo H), which produces deglycosylated proteins.
24125761	3	25	theme	glycosylation	341:353	arg1	effect					331:336	the effect	327:336	the effect of glycosylation on AADAC enzyme activity	327:378	In the present study, we investigated the effect of glycosylation on AADAC enzyme activity.
24125761	4	26	dep	282	515:517	arg1	N282Q					528:532	N282Q	528:532	N282Q	528:532	Immunoblot analysis of mutant AADACs that contained an asparagine (N, Asn) to glutamine (Q, Gln) substitution at either residue 78 or 282 (N78Q or N282Q) showed a different migration compared with the wild-type protein.
24125761	4	26	dep	282	515:517	arg1	N78Q					520:523	N78Q	520:523	N78Q	520:523	Immunoblot analysis of mutant AADACs that contained an asparagine (N, Asn) to glutamine (Q, Gln) substitution at either residue 78 or 282 (N78Q or N282Q) showed a different migration compared with the wild-type protein.
24125761	4	27	contain	contained	423:431	arg1	AADACs					411:416	mutant AADACs	404:416	mutant AADACs that contained an asparagine (N, Asn) to glutamine (Q, Gln) substitution at either residue 78 or 282 (N78Q or N282Q)	404:533	Immunoblot analysis of mutant AADACs that contained an asparagine (N, Asn) to glutamine (Q, Gln) substitution at either residue 78 or 282 (N78Q or N282Q) showed a different migration compared with the wild-type protein.
24125761	4	27	contain	contained	423:431	arg2	asparagine					436:445	an asparagine	433:445	an asparagine (N, Asn) to glutamine (Q, Gln) substitution at either residue 78 or 282 (N78Q or N282Q)	433:533	Immunoblot analysis of mutant AADACs that contained an asparagine (N, Asn) to glutamine (Q, Gln) substitution at either residue 78 or 282 (N78Q or N282Q) showed a different migration compared with the wild-type protein.
24125761	5	28	from	migration	709:717	arg1	microsomes					743:752	human liver microsomes	731:752	human liver microsomes (HLM) treated with endoglycosidase H (Endo H), which produces deglycosylated proteins	731:838	A mutant AADAC that contained N to Q substitutions at both residue 78 and 282 (N78Q/N282Q) showed a similar migration to AADAC in human liver microsomes (HLM) treated with endoglycosidase H (Endo H), which produces deglycosylated proteins.
24125761	5	28	from	migration	709:717	arg1	HLM					755:757	HLM	755:757	HLM	755:757	A mutant AADAC that contained N to Q substitutions at both residue 78 and 282 (N78Q/N282Q) showed a similar migration to AADAC in human liver microsomes (HLM) treated with endoglycosidase H (Endo H), which produces deglycosylated proteins.
24125761	12	29	theme	crucial	1757:1763	arg1	role					1765:1768	a crucial role	1755:1768	a crucial role	1755:1768	Overall, this study found that the translational, but not post-translational, N-glycosylation of AADAC plays a crucial role in regulating AADAC enzyme activity.
24125761	5	30	theme	deglycosylated	816:829	arg1	proteins					831:838	deglycosylated proteins	816:838	deglycosylated proteins	816:838	A mutant AADAC that contained N to Q substitutions at both residue 78 and 282 (N78Q/N282Q) showed a similar migration to AADAC in human liver microsomes (HLM) treated with endoglycosidase H (Endo H), which produces deglycosylated proteins.
24125761	3	31	theme	AADAC	358:362	arg1	activity					371:378	AADAC enzyme activity	358:378	AADAC enzyme activity	358:378	In the present study, we investigated the effect of glycosylation on AADAC enzyme activity.
24125761	4	32	from	residue	501:507	arg1	substitution					478:489	glutamine (Q, Gln) substitution	459:489	glutamine (Q, Gln) substitution at either residue 78 or 282 (N78Q or N282Q)	459:533	Immunoblot analysis of mutant AADACs that contained an asparagine (N, Asn) to glutamine (Q, Gln) substitution at either residue 78 or 282 (N78Q or N282Q) showed a different migration compared with the wild-type protein.
24125761	9	33	theme	HLM	1247:1249	arg1	treatment					1230:1238	the treatment	1226:1238	the treatment of the HLM with Endo H	1226:1261	However, the treatment of the HLM with Endo H caused no decrease of AADAC activity.
24125761	3	34	gly	glycosylation	341:353	arg1	AADAC					358:362	AADAC enzyme activity	358:378	AADAC enzyme activity	358:378	In the present study, we investigated the effect of glycosylation on AADAC enzyme activity.
24125761	3	34	gly	glycosylation	341:353	arg1	enzyme					364:369	AADAC enzyme activity	358:378	AADAC enzyme activity	358:378	In the present study, we investigated the effect of glycosylation on AADAC enzyme activity.
24125761	1	35	theme	clinical	155:162	arg1	phenacetin					189:198	phenacetin	189:198	phenacetin	189:198	Human arylacetamide deacetylase (AADAC) can hydrolyze clinical drugs such as flutamide, phenacetin, and rifamycins.
24125761	1	35	theme	clinical	155:162	arg1	drugs					164:168	clinical drugs	155:168	clinical drugs such as flutamide, phenacetin, and rifamycins	155:214	Human arylacetamide deacetylase (AADAC) can hydrolyze clinical drugs such as flutamide, phenacetin, and rifamycins.
24125761	1	35	theme	clinical	155:162	arg1	flutamide					178:186	flutamide	178:186	flutamide	178:186	Human arylacetamide deacetylase (AADAC) can hydrolyze clinical drugs such as flutamide, phenacetin, and rifamycins.
24125761	1	35	theme	clinical	155:162	arg1	rifamycins					205:214	rifamycins	205:214	rifamycins	205:214	Human arylacetamide deacetylase (AADAC) can hydrolyze clinical drugs such as flutamide, phenacetin, and rifamycins.
24125761	12	36	gly	N-glycosylation	1724:1738	arg1	AADAC					1743:1747	AADAC	1743:1747	AADAC	1743:1747	Overall, this study found that the translational, but not post-translational, N-glycosylation of AADAC plays a crucial role in regulating AADAC enzyme activity.
24125761	9	37	theme	Endo	1256:1259	arg1	H					1261:1261	Endo H	1256:1261	Endo H	1256:1261	However, the treatment of the HLM with Endo H caused no decrease of AADAC activity.
24125761	12	38	theme	translational	1681:1693	arg1	N-glycosylation					1724:1738	the translational, but not post-translational, N-glycosylation	1677:1738	the translational, but not post-translational, N-glycosylation of AADAC	1677:1747	Overall, this study found that the translational, but not post-translational, N-glycosylation of AADAC plays a crucial role in regulating AADAC enzyme activity.
24125761	11	39	theme	N78Q/N282Q	1454:1463	arg1	substitutions					1465:1477	the N282Q and the N78Q/N282Q substitutions	1436:1477	the N282Q and the N78Q/N282Q substitutions	1436:1477	The mutant types of AADAC containing the N282Q and the N78Q/N282Q substitutions were not detected by immunoblotting analysis after non-reducing SDS-PAGE, suggesting that the glycosylation of AADAC at N282 was important for proper protein folding.
24125761	5	40	theme	similar	701:707	arg1	migration					709:717	a similar migration	699:717	a similar migration to AADAC in human liver microsomes (HLM) treated with endoglycosidase H (Endo H), which produces deglycosylated proteins	699:838	A mutant AADAC that contained N to Q substitutions at both residue 78 and 282 (N78Q/N282Q) showed a similar migration to AADAC in human liver microsomes (HLM) treated with endoglycosidase H (Endo H), which produces deglycosylated proteins.
24125761	4	41	dep	Q	470:470	arg1	Gln					473:475	Gln	473:475	Gln	473:475	Immunoblot analysis of mutant AADACs that contained an asparagine (N, Asn) to glutamine (Q, Gln) substitution at either residue 78 or 282 (N78Q or N282Q) showed a different migration compared with the wild-type protein.
24125761	9	42	theme	AADAC	1285:1289	arg1	activity					1291:1298	AADAC activity	1285:1298	AADAC activity	1285:1298	However, the treatment of the HLM with Endo H caused no decrease of AADAC activity.
24125761	0	43	theme	arylacetamide	58:70	arg1	activity					91:98	human arylacetamide deacetylase enzyme activity	52:98	human arylacetamide deacetylase enzyme activity	52:98	N-Glycosylation during translation is essential for human arylacetamide deacetylase enzyme activity.
24125761	7	44	theme	lower	1003:1007	arg1	activity					1030:1037	dramatically lower phenacetin hydrolase activity	990:1037	dramatically lower phenacetin hydrolase activity	990:1037	Mutant types of AADAC with the N282Q and the N78Q/N282Q substitutions showed dramatically lower phenacetin hydrolase activity than did the wild-type protein.
24125761	11	45	theme	immunoblotting	1500:1513	arg1	analysis					1515:1522	immunoblotting analysis	1500:1522	immunoblotting analysis	1500:1522	The mutant types of AADAC containing the N282Q and the N78Q/N282Q substitutions were not detected by immunoblotting analysis after non-reducing SDS-PAGE, suggesting that the glycosylation of AADAC at N282 was important for proper protein folding.
24125761	4	46	theme	mutant	404:409	arg1	AADACs					411:416	mutant AADACs	404:416	mutant AADACs that contained an asparagine (N, Asn) to glutamine (Q, Gln) substitution at either residue 78 or 282 (N78Q or N282Q)	404:533	Immunoblot analysis of mutant AADACs that contained an asparagine (N, Asn) to glutamine (Q, Gln) substitution at either residue 78 or 282 (N78Q or N282Q) showed a different migration compared with the wild-type protein.
24125761	0	47	theme	human	52:56	arg1	activity					91:98	human arylacetamide deacetylase enzyme activity	52:98	human arylacetamide deacetylase enzyme activity	52:98	N-Glycosylation during translation is essential for human arylacetamide deacetylase enzyme activity.
24125761	4	48	theme	wild-type	582:590	arg1	protein					592:598	the wild-type protein	578:598	the wild-type protein	578:598	Immunoblot analysis of mutant AADACs that contained an asparagine (N, Asn) to glutamine (Q, Gln) substitution at either residue 78 or 282 (N78Q or N282Q) showed a different migration compared with the wild-type protein.
24125761	5	49	theme	N	631:631	arg1	substitutions					638:650	N to Q substitutions	631:650	N to Q substitutions at both residue 78 and 282 (N78Q/N282Q)	631:690	A mutant AADAC that contained N to Q substitutions at both residue 78 and 282 (N78Q/N282Q) showed a similar migration to AADAC in human liver microsomes (HLM) treated with endoglycosidase H (Endo H), which produces deglycosylated proteins.
24125761	11	50	theme	AADAC	1419:1423	arg1	types					1410:1414	The mutant types	1399:1414	The mutant types of AADAC containing the N282Q and the N78Q/N282Q substitutions	1399:1477	The mutant types of AADAC containing the N282Q and the N78Q/N282Q substitutions were not detected by immunoblotting analysis after non-reducing SDS-PAGE, suggesting that the glycosylation of AADAC at N282 was important for proper protein folding.
24125761	5	51	theme	human	731:735	arg1	microsomes					743:752	human liver microsomes	731:752	human liver microsomes (HLM) treated with endoglycosidase H (Endo H), which produces deglycosylated proteins	731:838	A mutant AADAC that contained N to Q substitutions at both residue 78 and 282 (N78Q/N282Q) showed a similar migration to AADAC in human liver microsomes (HLM) treated with endoglycosidase H (Endo H), which produces deglycosylated proteins.
24125761	5	51	theme	human	731:735	arg1	HLM					755:757	HLM	755:757	HLM	755:757	A mutant AADAC that contained N to Q substitutions at both residue 78 and 282 (N78Q/N282Q) showed a similar migration to AADAC in human liver microsomes (HLM) treated with endoglycosidase H (Endo H), which produces deglycosylated proteins.
24125761	8	52	theme	unglycosylated	1160:1173	arg1	protein					1175:1181	unglycosylated protein	1160:1181	unglycosylated protein	1160:1181	The treatment of wild-type AADAC-expressing HuH-7 cells with tunicamycin, which produces unglycosylated protein, decreased AADAC enzyme activity.
24125761	2	53	gly	glycoprotein	228:239	arg1	glycoprotein					228:239	a glycoprotein	226:239	a glycoprotein	226:239	AADAC is a glycoprotein, but the role of glycosylation remains unclear.
24125761	2	53	gly	glycoprotein	228:239	arg1	AADAC					217:221	AADAC	217:221	AADAC	217:221	AADAC is a glycoprotein, but the role of glycosylation remains unclear.
24125761	7	54	theme	AADAC	929:933	arg1	types					920:924	Mutant types	913:924	Mutant types of AADAC with the N282Q and the N78Q/N282Q substitutions	913:981	Mutant types of AADAC with the N282Q and the N78Q/N282Q substitutions showed dramatically lower phenacetin hydrolase activity than did the wild-type protein.
24125761	8	55	theme	AADAC-expressing	1098:1113	arg1	cells					1121:1125	wild-type AADAC-expressing HuH-7 cells	1088:1125	wild-type AADAC-expressing HuH-7 cells	1088:1125	The treatment of wild-type AADAC-expressing HuH-7 cells with tunicamycin, which produces unglycosylated protein, decreased AADAC enzyme activity.
24125761	5	56	gly	deglycosylated	816:829	arg1	proteins					831:838	deglycosylated proteins	816:838	deglycosylated proteins	816:838	A mutant AADAC that contained N to Q substitutions at both residue 78 and 282 (N78Q/N282Q) showed a similar migration to AADAC in human liver microsomes (HLM) treated with endoglycosidase H (Endo H), which produces deglycosylated proteins.
24125761	5	57	theme	mutant	603:608	arg1	AADAC					610:614	A mutant AADAC	601:614	A mutant AADAC that contained N to Q substitutions at both residue 78 and 282 (N78Q/N282Q)	601:690	A mutant AADAC that contained N to Q substitutions at both residue 78 and 282 (N78Q/N282Q) showed a similar migration to AADAC in human liver microsomes (HLM) treated with endoglycosidase H (Endo H), which produces deglycosylated proteins.
24125761	8	58	theme	cells	1121:1125	arg1	treatment					1075:1083	The treatment	1071:1083	The treatment	1071:1083	The treatment of wild-type AADAC-expressing HuH-7 cells with tunicamycin, which produces unglycosylated protein, decreased AADAC enzyme activity.
24125761	8	59	with	treatment	1075:1083	arg1	tunicamycin					1132:1142	tunicamycin	1132:1142	tunicamycin	1132:1142	The treatment of wild-type AADAC-expressing HuH-7 cells with tunicamycin, which produces unglycosylated protein, decreased AADAC enzyme activity.
24125761	8	60	theme	AADAC	1194:1198	arg1	activity					1207:1214	AADAC enzyme activity	1194:1214	AADAC enzyme activity	1194:1214	The treatment of wild-type AADAC-expressing HuH-7 cells with tunicamycin, which produces unglycosylated protein, decreased AADAC enzyme activity.
24125761	11	61	theme	protein	1629:1635	arg1	folding					1637:1643	proper protein folding	1622:1643	proper protein folding	1622:1643	The mutant types of AADAC containing the N282Q and the N78Q/N282Q substitutions were not detected by immunoblotting analysis after non-reducing SDS-PAGE, suggesting that the glycosylation of AADAC at N282 was important for proper protein folding.
24125761	0	62	theme	enzyme	84:89	arg1	activity					91:98	human arylacetamide deacetylase enzyme activity	52:98	human arylacetamide deacetylase enzyme activity	52:98	N-Glycosylation during translation is essential for human arylacetamide deacetylase enzyme activity.
24125761	5	63	from	282	675:677	arg1	substitutions					638:650	N to Q substitutions	631:650	N to Q substitutions at both residue 78 and 282 (N78Q/N282Q)	631:690	A mutant AADAC that contained N to Q substitutions at both residue 78 and 282 (N78Q/N282Q) showed a similar migration to AADAC in human liver microsomes (HLM) treated with endoglycosidase H (Endo H), which produces deglycosylated proteins.
24125761	5	64	theme	endoglycosidase	773:787	arg1	H					789:789	endoglycosidase H	773:789	endoglycosidase H (Endo H)	773:798	A mutant AADAC that contained N to Q substitutions at both residue 78 and 282 (N78Q/N282Q) showed a similar migration to AADAC in human liver microsomes (HLM) treated with endoglycosidase H (Endo H), which produces deglycosylated proteins.
24125761	5	64	theme	endoglycosidase	773:787	arg1	H					797:797	Endo H	792:797	Endo H	792:797	A mutant AADAC that contained N to Q substitutions at both residue 78 and 282 (N78Q/N282Q) showed a similar migration to AADAC in human liver microsomes (HLM) treated with endoglycosidase H (Endo H), which produces deglycosylated proteins.
24125761	10	65	from	activity	1370:1377	arg1	form					1393:1396	the mature form	1382:1396	the mature form	1382:1396	Thus, the oligosaccharide chain, per se, was not important for AADAC activity in the mature form.
24125761	5	66	dep	substitutions	638:650	arg1	to					633:634	to	633:634	to	633:634	A mutant AADAC that contained N to Q substitutions at both residue 78 and 282 (N78Q/N282Q) showed a similar migration to AADAC in human liver microsomes (HLM) treated with endoglycosidase H (Endo H), which produces deglycosylated proteins.
24125761	11	67	gly	glycosylation	1573:1585	arg1	protein					1629:1635	proper protein folding	1622:1643	proper protein folding	1622:1643	The mutant types of AADAC containing the N282Q and the N78Q/N282Q substitutions were not detected by immunoblotting analysis after non-reducing SDS-PAGE, suggesting that the glycosylation of AADAC at N282 was important for proper protein folding.
24125761	11	67	gly	glycosylation	1573:1585	arg1	N282					1599:1602	N282	1599:1602	N282	1599:1602	The mutant types of AADAC containing the N282Q and the N78Q/N282Q substitutions were not detected by immunoblotting analysis after non-reducing SDS-PAGE, suggesting that the glycosylation of AADAC at N282 was important for proper protein folding.
24125761	11	67	gly	glycosylation	1573:1585	arg1	AADAC					1590:1594	AADAC	1590:1594	AADAC	1590:1594	The mutant types of AADAC containing the N282Q and the N78Q/N282Q substitutions were not detected by immunoblotting analysis after non-reducing SDS-PAGE, suggesting that the glycosylation of AADAC at N282 was important for proper protein folding.
24125761	11	67	gly	glycosylation	1573:1585	arg2	N282					1599:1602	N282	1599:1602	N282	1599:1602	The mutant types of AADAC containing the N282Q and the N78Q/N282Q substitutions were not detected by immunoblotting analysis after non-reducing SDS-PAGE, suggesting that the glycosylation of AADAC at N282 was important for proper protein folding.
24125761	12	68	theme	enzyme	1790:1795	arg1	activity					1797:1804	AADAC enzyme activity	1784:1804	AADAC enzyme activity	1784:1804	Overall, this study found that the translational, but not post-translational, N-glycosylation of AADAC plays a crucial role in regulating AADAC enzyme activity.
24125761	3	69	from	effect	331:336	arg1	activity					371:378	AADAC enzyme activity	358:378	AADAC enzyme activity	358:378	In the present study, we investigated the effect of glycosylation on AADAC enzyme activity.
24125761	10	70	theme	oligosaccharide	1311:1325	arg1	important					1350:1358	important	1350:1358	important	1350:1358	Thus, the oligosaccharide chain, per se, was not important for AADAC activity in the mature form.
24125761	10	70	theme	oligosaccharide	1311:1325	arg1	chain					1327:1331	the oligosaccharide chain	1307:1331	the oligosaccharide chain	1307:1331	Thus, the oligosaccharide chain, per se, was not important for AADAC activity in the mature form.
24125761	10	70	theme	oligosaccharide	1311:1325	arg1	se					1338:1339	per se	1334:1339	per se	1334:1339	Thus, the oligosaccharide chain, per se, was not important for AADAC activity in the mature form.
24125761	4	71	theme	glutamine	459:467	arg1	substitution					478:489	glutamine (Q, Gln) substitution	459:489	glutamine (Q, Gln) substitution at either residue 78 or 282 (N78Q or N282Q)	459:533	Immunoblot analysis of mutant AADACs that contained an asparagine (N, Asn) to glutamine (Q, Gln) substitution at either residue 78 or 282 (N78Q or N282Q) showed a different migration compared with the wild-type protein.
24125761	4	72	from	282	515:517	arg1	substitution					478:489	glutamine (Q, Gln) substitution	459:489	glutamine (Q, Gln) substitution at either residue 78 or 282 (N78Q or N282Q)	459:533	Immunoblot analysis of mutant AADACs that contained an asparagine (N, Asn) to glutamine (Q, Gln) substitution at either residue 78 or 282 (N78Q or N282Q) showed a different migration compared with the wild-type protein.
24125761	1	73	theme	Human	101:105	arg1	AADAC					134:138	AADAC	134:138	AADAC	134:138	Human arylacetamide deacetylase (AADAC) can hydrolyze clinical drugs such as flutamide, phenacetin, and rifamycins.
24125761	1	73	theme	Human	101:105	arg1	deacetylase					121:131	Human arylacetamide deacetylase	101:131	Human arylacetamide deacetylase (AADAC)	101:139	Human arylacetamide deacetylase (AADAC) can hydrolyze clinical drugs such as flutamide, phenacetin, and rifamycins.
24125761	5	74	theme	Q	636:636	arg1	substitutions					638:650	N to Q substitutions	631:650	N to Q substitutions at both residue 78 and 282 (N78Q/N282Q)	631:690	A mutant AADAC that contained N to Q substitutions at both residue 78 and 282 (N78Q/N282Q) showed a similar migration to AADAC in human liver microsomes (HLM) treated with endoglycosidase H (Endo H), which produces deglycosylated proteins.
24125761	7	75	dep	did	1044:1046	arg1	than					1039:1042	than	1039:1042	than	1039:1042	Mutant types of AADAC with the N282Q and the N78Q/N282Q substitutions showed dramatically lower phenacetin hydrolase activity than did the wild-type protein.
24125761	12	76	theme	AADAC	1743:1747	arg1	N-glycosylation					1724:1738	the translational, but not post-translational, N-glycosylation	1677:1738	the translational, but not post-translational, N-glycosylation of AADAC	1677:1747	Overall, this study found that the translational, but not post-translational, N-glycosylation of AADAC plays a crucial role in regulating AADAC enzyme activity.
24125761	7	77	with	AADAC	929:933	arg1	N78Q/N282Q					958:967	N78Q/N282Q	958:967	N78Q/N282Q	958:967	Mutant types of AADAC with the N282Q and the N78Q/N282Q substitutions showed dramatically lower phenacetin hydrolase activity than did the wild-type protein.
24125761	7	77	with	AADAC	929:933	arg1	N282Q					944:948	N282Q	944:948	N282Q	944:948	Mutant types of AADAC with the N282Q and the N78Q/N282Q substitutions showed dramatically lower phenacetin hydrolase activity than did the wild-type protein.
24125761	3	78	theme	enzyme	364:369	arg1	activity					371:378	AADAC enzyme activity	358:378	AADAC enzyme activity	358:378	In the present study, we investigated the effect of glycosylation on AADAC enzyme activity.
24125761	10	79	theme	AADAC	1364:1368	arg1	activity					1370:1377	AADAC activity	1364:1377	AADAC activity in the mature form	1364:1396	Thus, the oligosaccharide chain, per se, was not important for AADAC activity in the mature form.
24125761	5	80	contain	contained	621:629	arg2	substitutions					638:650	N to Q substitutions	631:650	N to Q substitutions at both residue 78 and 282 (N78Q/N282Q)	631:690	A mutant AADAC that contained N to Q substitutions at both residue 78 and 282 (N78Q/N282Q) showed a similar migration to AADAC in human liver microsomes (HLM) treated with endoglycosidase H (Endo H), which produces deglycosylated proteins.
24125761	5	80	contain	contained	621:629	arg1	AADAC					610:614	A mutant AADAC	601:614	A mutant AADAC that contained N to Q substitutions at both residue 78 and 282 (N78Q/N282Q)	601:690	A mutant AADAC that contained N to Q substitutions at both residue 78 and 282 (N78Q/N282Q) showed a similar migration to AADAC in human liver microsomes (HLM) treated with endoglycosidase H (Endo H), which produces deglycosylated proteins.
24125761	6	81	gly	glycosylated	878:889	arg2	N282					907:910	N282	907:910	N282	907:910	This result indicated that AADAC was glycosylated at both N78 and N282.
24125761	6	81	gly	glycosylated	878:889	arg1	AADAC					868:872	AADAC	868:872	AADAC	868:872	This result indicated that AADAC was glycosylated at both N78 and N282.
24125761	6	81	gly	glycosylated	878:889	arg2	N78					899:901	N78	899:901	N78	899:901	This result indicated that AADAC was glycosylated at both N78 and N282.
24125761	7	82	theme	hydrolase	1020:1028	arg1	activity					1030:1037	dramatically lower phenacetin hydrolase activity	990:1037	dramatically lower phenacetin hydrolase activity	990:1037	Mutant types of AADAC with the N282Q and the N78Q/N282Q substitutions showed dramatically lower phenacetin hydrolase activity than did the wild-type protein.
24125761	12	83	theme	post-translational	1704:1721	arg1	N-glycosylation					1724:1738	the translational, but not post-translational, N-glycosylation	1677:1738	the translational, but not post-translational, N-glycosylation of AADAC	1677:1747	Overall, this study found that the translational, but not post-translational, N-glycosylation of AADAC plays a crucial role in regulating AADAC enzyme activity.
24125761	10	84	theme	mature	1386:1391	arg1	form					1393:1396	the mature form	1382:1396	the mature form	1382:1396	Thus, the oligosaccharide chain, per se, was not important for AADAC activity in the mature form.
24125761	11	85	theme	N282Q	1440:1444	arg1	substitutions					1465:1477	the N282Q and the N78Q/N282Q substitutions	1436:1477	the N282Q and the N78Q/N282Q substitutions	1436:1477	The mutant types of AADAC containing the N282Q and the N78Q/N282Q substitutions were not detected by immunoblotting analysis after non-reducing SDS-PAGE, suggesting that the glycosylation of AADAC at N282 was important for proper protein folding.
24125761	11	86	theme	AADAC	1590:1594	arg1	glycosylation					1573:1585	the glycosylation	1569:1585	the glycosylation of AADAC at N282	1569:1602	The mutant types of AADAC containing the N282Q and the N78Q/N282Q substitutions were not detected by immunoblotting analysis after non-reducing SDS-PAGE, suggesting that the glycosylation of AADAC at N282 was important for proper protein folding.
24125761	11	86	theme	AADAC	1590:1594	arg1	important					1608:1616	important	1608:1616	important	1608:1616	The mutant types of AADAC containing the N282Q and the N78Q/N282Q substitutions were not detected by immunoblotting analysis after non-reducing SDS-PAGE, suggesting that the glycosylation of AADAC at N282 was important for proper protein folding.
24125761	4	87	theme	different	544:552	arg1	migration					554:562	a different migration	542:562	a different migration	542:562	Immunoblot analysis of mutant AADACs that contained an asparagine (N, Asn) to glutamine (Q, Gln) substitution at either residue 78 or 282 (N78Q or N282Q) showed a different migration compared with the wild-type protein.
24125761	9	88	theme	activity	1291:1298	arg1	decrease					1273:1280	no decrease	1270:1280	no decrease of AADAC activity	1270:1298	However, the treatment of the HLM with Endo H caused no decrease of AADAC activity.
23776206	0	0	theme	activation	82:91	arg1	pathways					93:100	distinct activation pathways	73:100	distinct activation pathways	73:100	Mechanistic and structural studies on legumain explain its zymogenicity, distinct activation pathways, and regulation.
23776206	1	1	theme	important	156:164	arg1	functions					166:174	important functions	156:174	important functions	156:174	The cysteine protease legumain plays important functions in immunity and cancer at different cellular locations, some of which appeared conflicting with its proteolytic activity and stability.
23776206	0	2	theme	distinct	73:80	arg1	pathways					93:100	distinct activation pathways	73:100	distinct activation pathways	73:100	Mechanistic and structural studies on legumain explain its zymogenicity, distinct activation pathways, and regulation.
23776206	7	3	theme	signal	1163:1168	arg1	transducers					1170:1180	signal transducers	1163:1180	signal transducers	1163:1180	The multibranched and context-dependent activation process of legumain illustrates how proteases can act not only as signal transducers but as decision makers.
23776206	7	3	theme	signal	1163:1168	arg1	proteases					1133:1141	proteases	1133:1141	proteases	1133:1141	The multibranched and context-dependent activation process of legumain illustrates how proteases can act not only as signal transducers but as decision makers.
23776206	4	4	theme	proteolytic	667:677	arg1	activation					679:688	proteolytic activation	667:688	proteolytic activation with the release of an activation peptide	667:730	Completely unexpectedly, the structure points toward a hidden carboxypeptidase activity that develops upon proteolytic activation with the release of an activation peptide.
23776206	2	5	theme	legumain	350:357	arg1	structures					336:345	crystal structures	328:345	crystal structures of legumain in the zymogenic and fully activated form in complex with different substrate analogs	328:443	Here, we report crystal structures of legumain in the zymogenic and fully activated form in complex with different substrate analogs.
23776206	5	6	theme	pH	781:782	arg1	stability					784:792	the enigmatic pH stability	767:792	the enigmatic pH stability of legumain, e.g., lysosomal, nuclear, and extracellular activities	767:860	These activation routes reconcile the enigmatic pH stability of legumain, e.g., lysosomal, nuclear, and extracellular activities with relevance in immunology and cancer.
23776206	6	7	theme	selective	950:958	arg1	protonation					960:970	selective protonation	950:970	selective protonation of the S1 pocket (KM) and the catalytic nucleophile (kcat)	950:1029	Substrate access and turnover is controlled by selective protonation of the S1 pocket (KM) and the catalytic nucleophile (kcat), respectively.
23776206	4	8	theme	carboxypeptidase	622:637	arg1	activity					639:646	a hidden carboxypeptidase activity	613:646	a hidden carboxypeptidase activity that develops upon proteolytic activation with the release of an activation peptide	613:730	Completely unexpectedly, the structure points toward a hidden carboxypeptidase activity that develops upon proteolytic activation with the release of an activation peptide.
23776206	2	9	with	complex	404:410	arg1	analogs					437:443	different substrate analogs	417:443	different substrate analogs	417:443	Here, we report crystal structures of legumain in the zymogenic and fully activated form in complex with different substrate analogs.
23776206	6	10	theme	nucleophile	1012:1022	arg1	protonation					960:970	selective protonation	950:970	selective protonation of the S1 pocket (KM) and the catalytic nucleophile (kcat)	950:1029	Substrate access and turnover is controlled by selective protonation of the S1 pocket (KM) and the catalytic nucleophile (kcat), respectively.
23776206	3	11	theme	endopeptidase	493:505	arg1	activity					507:514	the eponymous asparagine-specific endopeptidase activity	459:514	the eponymous asparagine-specific endopeptidase activity	459:514	We show that the eponymous asparagine-specific endopeptidase activity is electrostatically generated by pH shift.
23776206	5	12	from	relevance	867:875	arg1	cancer					895:900	cancer	895:900	cancer	895:900	These activation routes reconcile the enigmatic pH stability of legumain, e.g., lysosomal, nuclear, and extracellular activities with relevance in immunology and cancer.
23776206	5	12	from	relevance	867:875	arg1	immunology					880:889	immunology	880:889	immunology	880:889	These activation routes reconcile the enigmatic pH stability of legumain, e.g., lysosomal, nuclear, and extracellular activities with relevance in immunology and cancer.
23776206	2	13	from	structures	336:345	arg1	form					396:399	the zymogenic and fully activated form	362:399	the zymogenic and fully activated form in complex with different substrate analogs	362:443	Here, we report crystal structures of legumain in the zymogenic and fully activated form in complex with different substrate analogs.
23776206	4	14	theme	hidden	615:620	arg1	activity					639:646	a hidden carboxypeptidase activity	613:646	a hidden carboxypeptidase activity that develops upon proteolytic activation with the release of an activation peptide	613:730	Completely unexpectedly, the structure points toward a hidden carboxypeptidase activity that develops upon proteolytic activation with the release of an activation peptide.
23776206	2	15	theme	activated	386:394	arg1	form					396:399	the zymogenic and fully activated form	362:399	the zymogenic and fully activated form in complex with different substrate analogs	362:443	Here, we report crystal structures of legumain in the zymogenic and fully activated form in complex with different substrate analogs.
23776206	5	16	theme	extracellular	837:849	arg1	activities					851:860	extracellular activities	837:860	extracellular activities	837:860	These activation routes reconcile the enigmatic pH stability of legumain, e.g., lysosomal, nuclear, and extracellular activities with relevance in immunology and cancer.
23776206	6	17	theme	catalytic	1002:1010	arg1	kcat					1025:1028	kcat	1025:1028	kcat	1025:1028	Substrate access and turnover is controlled by selective protonation of the S1 pocket (KM) and the catalytic nucleophile (kcat), respectively.
23776206	6	17	theme	catalytic	1002:1010	arg1	nucleophile					1012:1022	the catalytic nucleophile	998:1022	the catalytic nucleophile (kcat)	998:1029	Substrate access and turnover is controlled by selective protonation of the S1 pocket (KM) and the catalytic nucleophile (kcat), respectively.
23776206	7	18	theme	activation	1086:1095	arg1	process					1097:1103	The multibranched and context-dependent activation process	1046:1103	The multibranched and context-dependent activation process of legumain	1046:1115	The multibranched and context-dependent activation process of legumain illustrates how proteases can act not only as signal transducers but as decision makers.
23776206	4	19	theme	activation	713:722	arg1	peptide					724:730	an activation peptide	710:730	an activation peptide	710:730	Completely unexpectedly, the structure points toward a hidden carboxypeptidase activity that develops upon proteolytic activation with the release of an activation peptide.
23776206	0	20	theme	Mechanistic	0:10	arg1	studies					27:33	Mechanistic and structural studies	0:33	Mechanistic and structural studies on legumain	0:45	Mechanistic and structural studies on legumain explain its zymogenicity, distinct activation pathways, and regulation.
23776206	1	21	theme	proteolytic	276:286	arg1	activity					288:295	its proteolytic activity	272:295	its proteolytic activity	272:295	The cysteine protease legumain plays important functions in immunity and cancer at different cellular locations, some of which appeared conflicting with its proteolytic activity and stability.
23776206	7	22	theme	legumain	1108:1115	arg1	process					1097:1103	The multibranched and context-dependent activation process	1046:1103	The multibranched and context-dependent activation process of legumain	1046:1115	The multibranched and context-dependent activation process of legumain illustrates how proteases can act not only as signal transducers but as decision makers.
23776206	2	23	theme	different	417:425	arg1	analogs					437:443	different substrate analogs	417:443	different substrate analogs	417:443	Here, we report crystal structures of legumain in the zymogenic and fully activated form in complex with different substrate analogs.
23776206	2	24	theme	substrate	427:435	arg1	analogs					437:443	different substrate analogs	417:443	different substrate analogs	417:443	Here, we report crystal structures of legumain in the zymogenic and fully activated form in complex with different substrate analogs.
23776206	5	25	dep	lysosomal	813:821	arg1	e.g.					807:810	e.g.	807:810	e.g.	807:810	These activation routes reconcile the enigmatic pH stability of legumain, e.g., lysosomal, nuclear, and extracellular activities with relevance in immunology and cancer.
23776206	1	26	theme	different	202:210	arg1	locations					221:229	different cellular locations	202:229	different cellular locations	202:229	The cysteine protease legumain plays important functions in immunity and cancer at different cellular locations, some of which appeared conflicting with its proteolytic activity and stability.
23776206	1	27	theme	cellular	212:219	arg1	locations					221:229	different cellular locations	202:229	different cellular locations	202:229	The cysteine protease legumain plays important functions in immunity and cancer at different cellular locations, some of which appeared conflicting with its proteolytic activity and stability.
23776206	7	28	theme	decision	1189:1196	arg1	proteases					1133:1141	proteases	1133:1141	proteases	1133:1141	The multibranched and context-dependent activation process of legumain illustrates how proteases can act not only as signal transducers but as decision makers.
23776206	7	28	theme	decision	1189:1196	arg1	makers					1198:1203	decision makers	1189:1203	decision makers	1189:1203	The multibranched and context-dependent activation process of legumain illustrates how proteases can act not only as signal transducers but as decision makers.
23776206	5	29	theme	enigmatic	771:779	arg1	stability					784:792	the enigmatic pH stability	767:792	the enigmatic pH stability of legumain, e.g., lysosomal, nuclear, and extracellular activities	767:860	These activation routes reconcile the enigmatic pH stability of legumain, e.g., lysosomal, nuclear, and extracellular activities with relevance in immunology and cancer.
23776206	6	30	theme	Substrate	903:911	arg1	access					913:918	Substrate access	903:918	Substrate access	903:918	Substrate access and turnover is controlled by selective protonation of the S1 pocket (KM) and the catalytic nucleophile (kcat), respectively.
23776206	5	31	theme	legumain	797:804	arg1	stability					784:792	the enigmatic pH stability	767:792	the enigmatic pH stability of legumain, e.g., lysosomal, nuclear, and extracellular activities	767:860	These activation routes reconcile the enigmatic pH stability of legumain, e.g., lysosomal, nuclear, and extracellular activities with relevance in immunology and cancer.
23776206	7	32	theme	context-dependent	1068:1084	arg1	process					1097:1103	The multibranched and context-dependent activation process	1046:1103	The multibranched and context-dependent activation process of legumain	1046:1115	The multibranched and context-dependent activation process of legumain illustrates how proteases can act not only as signal transducers but as decision makers.
23776206	3	33	theme	eponymous	463:471	arg1	activity					507:514	the eponymous asparagine-specific endopeptidase activity	459:514	the eponymous asparagine-specific endopeptidase activity	459:514	We show that the eponymous asparagine-specific endopeptidase activity is electrostatically generated by pH shift.
23776206	6	34	theme	pocket	982:987	arg1	protonation					960:970	selective protonation	950:970	selective protonation of the S1 pocket (KM) and the catalytic nucleophile (kcat)	950:1029	Substrate access and turnover is controlled by selective protonation of the S1 pocket (KM) and the catalytic nucleophile (kcat), respectively.
23776206	3	35	theme	asparagine-specific	473:491	arg1	activity					507:514	the eponymous asparagine-specific endopeptidase activity	459:514	the eponymous asparagine-specific endopeptidase activity	459:514	We show that the eponymous asparagine-specific endopeptidase activity is electrostatically generated by pH shift.
23776206	2	36	from	form	396:399	arg1	complex					404:410	complex	404:410	complex with different substrate analogs	404:443	Here, we report crystal structures of legumain in the zymogenic and fully activated form in complex with different substrate analogs.
23776206	6	37	theme	S1	979:980	arg1	KM					990:991	KM	990:991	KM	990:991	Substrate access and turnover is controlled by selective protonation of the S1 pocket (KM) and the catalytic nucleophile (kcat), respectively.
23776206	6	37	theme	S1	979:980	arg1	pocket					982:987	the S1 pocket	975:987	the S1 pocket (KM)	975:992	Substrate access and turnover is controlled by selective protonation of the S1 pocket (KM) and the catalytic nucleophile (kcat), respectively.
23776206	7	38	theme	multibranched	1050:1062	arg1	process					1097:1103	The multibranched and context-dependent activation process	1046:1103	The multibranched and context-dependent activation process of legumain	1046:1115	The multibranched and context-dependent activation process of legumain illustrates how proteases can act not only as signal transducers but as decision makers.
23776206	4	39	theme	peptide	724:730	arg1	release					699:705	the release	695:705	the release of an activation peptide	695:730	Completely unexpectedly, the structure points toward a hidden carboxypeptidase activity that develops upon proteolytic activation with the release of an activation peptide.
23776206	1	40	theme	cysteine	123:130	arg1	legumain					141:148	The cysteine protease legumain	119:148	The cysteine protease legumain	119:148	The cysteine protease legumain plays important functions in immunity and cancer at different cellular locations, some of which appeared conflicting with its proteolytic activity and stability.
23776206	5	41	theme	activation	739:748	arg1	routes					750:755	These activation routes	733:755	These activation routes	733:755	These activation routes reconcile the enigmatic pH stability of legumain, e.g., lysosomal, nuclear, and extracellular activities with relevance in immunology and cancer.
23776206	4	42	with	activation	679:688	arg1	release					699:705	the release	695:705	the release of an activation peptide	695:730	Completely unexpectedly, the structure points toward a hidden carboxypeptidase activity that develops upon proteolytic activation with the release of an activation peptide.
23776206	1	43	theme	protease	132:139	arg1	legumain					141:148	The cysteine protease legumain	119:148	The cysteine protease legumain	119:148	The cysteine protease legumain plays important functions in immunity and cancer at different cellular locations, some of which appeared conflicting with its proteolytic activity and stability.
23776206	2	44	theme	crystal	328:334	arg1	structures					336:345	crystal structures	328:345	crystal structures of legumain in the zymogenic and fully activated form in complex with different substrate analogs	328:443	Here, we report crystal structures of legumain in the zymogenic and fully activated form in complex with different substrate analogs.
23776206	2	45	theme	zymogenic	366:374	arg1	form					396:399	the zymogenic and fully activated form	362:399	the zymogenic and fully activated form in complex with different substrate analogs	362:443	Here, we report crystal structures of legumain in the zymogenic and fully activated form in complex with different substrate analogs.
23776206	0	46	from	studies	27:33	arg1	legumain					38:45	legumain	38:45	legumain	38:45	Mechanistic and structural studies on legumain explain its zymogenicity, distinct activation pathways, and regulation.
23776206	0	47	theme	structural	16:25	arg1	studies					27:33	Mechanistic and structural studies	0:33	Mechanistic and structural studies on legumain	0:45	Mechanistic and structural studies on legumain explain its zymogenicity, distinct activation pathways, and regulation.
23776206	3	48	theme	pH	550:551	arg1	shift					553:557	pH shift	550:557	pH shift	550:557	We show that the eponymous asparagine-specific endopeptidase activity is electrostatically generated by pH shift.
28514451	1	0	theme	G-protein-coupled	132:148	arg1	family					159:164	the class B G-protein-coupled receptor family	120:164	the class B G-protein-coupled receptor family	120:164	The human glucagon receptor, GCGR, belongs to the class B G-protein-coupled receptor family and plays a key role in glucose homeostasis and the pathophysiology of type 2 diabetes.
28514451	6	1	theme	full-length	1007:1017	arg1	structure					1024:1032	the full-length GCGR structure	1003:1032	the full-length GCGR structure	1003:1032	These insights into the full-length GCGR structure deepen our understanding of the signalling mechanisms of class B G-protein-coupled receptors.
28514451	6	2	theme	signalling	1066:1075	arg1	mechanisms					1077:1086	the signalling mechanisms	1062:1086	the signalling mechanisms of class B G-protein-coupled receptors	1062:1125	These insights into the full-length GCGR structure deepen our understanding of the signalling mechanisms of class B G-protein-coupled receptors.
28514451	1	3	theme	receptor	150:157	arg1	family					159:164	the class B G-protein-coupled receptor family	120:164	the class B G-protein-coupled receptor family	120:164	The human glucagon receptor, GCGR, belongs to the class B G-protein-coupled receptor family and plays a key role in glucose homeostasis and the pathophysiology of type 2 diabetes.
28514451	1	4	theme	type	237:240	arg1	diabetes					244:251	type 2 diabetes	237:251	type 2 diabetes	237:251	The human glucagon receptor, GCGR, belongs to the class B G-protein-coupled receptor family and plays a key role in glucose homeostasis and the pathophysiology of type 2 diabetes.
28514451	6	5	theme	receptors	1117:1125	arg1	mechanisms					1077:1086	the signalling mechanisms	1062:1086	the signalling mechanisms of class B G-protein-coupled receptors	1062:1125	These insights into the full-length GCGR structure deepen our understanding of the signalling mechanisms of class B G-protein-coupled receptors.
28514451	2	6	contain	containing	317:326	arg1	GCGR					312:315	full-length GCGR	300:315	full-length GCGR containing both the extracellular domain and transmembrane domain in an inactive conformation	300:409	Here we report the 3.0 Å crystal structure of full-length GCGR containing both the extracellular domain and transmembrane domain in an inactive conformation.
28514451	2	6	contain	containing	317:326	arg2	domain					351:356	the extracellular domain	333:356	the extracellular domain	333:356	Here we report the 3.0 Å crystal structure of full-length GCGR containing both the extracellular domain and transmembrane domain in an inactive conformation.
28514451	2	6	contain	containing	317:326	arg2	domain					376:381	transmembrane domain	362:381	transmembrane domain	362:381	Here we report the 3.0 Å crystal structure of full-length GCGR containing both the extracellular domain and transmembrane domain in an inactive conformation.
28514451	4	7	theme	compact	735:741	arg1	structure					751:759	a compact β-sheet structure	733:759	a compact β-sheet structure	733:759	The first extracellular loop exhibits a β-hairpin conformation and interacts with the stalk to form a compact β-sheet structure.
28514451	5	8	theme	peptide	935:941	arg1	binding					950:956	peptide ligand binding	935:956	peptide ligand binding	935:956	Hydrogen-deuterium exchange, disulfide crosslinking and molecular dynamics studies suggest that the stalk and the first extracellular loop have critical roles in modulating peptide ligand binding and receptor activation.
28514451	4	9	theme	β-hairpin	673:681	arg1	conformation					683:694	a β-hairpin conformation	671:694	a β-hairpin conformation	671:694	The first extracellular loop exhibits a β-hairpin conformation and interacts with the stalk to form a compact β-sheet structure.
28514451	1	10	theme	diabetes	244:251	arg1	homeostasis					198:208	glucose homeostasis	190:208	glucose homeostasis	190:208	The human glucagon receptor, GCGR, belongs to the class B G-protein-coupled receptor family and plays a key role in glucose homeostasis and the pathophysiology of type 2 diabetes.
28514451	1	10	theme	diabetes	244:251	arg1	pathophysiology					218:232	the pathophysiology	214:232	the pathophysiology of type 2 diabetes	214:251	The human glucagon receptor, GCGR, belongs to the class B G-protein-coupled receptor family and plays a key role in glucose homeostasis and the pathophysiology of type 2 diabetes.
28514451	3	11	theme	β-strand	499:506	arg1	conformation					508:519	a β-strand conformation	497:519	a β-strand conformation	497:519	The two domains are connected by a 12-residue segment termed the stalk, which adopts a β-strand conformation, instead of forming an α-helix as observed in the previously solved structure of the GCGR transmembrane domain.
28514451	4	12	theme	extracellular	643:655	arg1	loop					657:660	The first extracellular loop	633:660	The first extracellular loop	633:660	The first extracellular loop exhibits a β-hairpin conformation and interacts with the stalk to form a compact β-sheet structure.
28514451	6	13	theme	B	1097:1097	arg1	receptors					1117:1125	class B G-protein-coupled receptors	1091:1125	class B G-protein-coupled receptors	1091:1125	These insights into the full-length GCGR structure deepen our understanding of the signalling mechanisms of class B G-protein-coupled receptors.
28514451	1	14	theme	human	78:82	arg1	receptor					93:100	The human glucagon receptor	74:100	The human glucagon receptor	74:100	The human glucagon receptor, GCGR, belongs to the class B G-protein-coupled receptor family and plays a key role in glucose homeostasis and the pathophysiology of type 2 diabetes.
28514451	1	14	theme	human	78:82	arg1	GCGR					103:106	GCGR	103:106	GCGR	103:106	The human glucagon receptor, GCGR, belongs to the class B G-protein-coupled receptor family and plays a key role in glucose homeostasis and the pathophysiology of type 2 diabetes.
28514451	6	15	theme	class	1091:1095	arg1	receptors					1117:1125	class B G-protein-coupled receptors	1091:1125	class B G-protein-coupled receptors	1091:1125	These insights into the full-length GCGR structure deepen our understanding of the signalling mechanisms of class B G-protein-coupled receptors.
28514451	5	16	theme	disulfide	791:799	arg1	crosslinking					801:812	disulfide crosslinking	791:812	disulfide crosslinking	791:812	Hydrogen-deuterium exchange, disulfide crosslinking and molecular dynamics studies suggest that the stalk and the first extracellular loop have critical roles in modulating peptide ligand binding and receptor activation.
28514451	1	17	theme	glucagon	84:91	arg1	receptor					93:100	The human glucagon receptor	74:100	The human glucagon receptor	74:100	The human glucagon receptor, GCGR, belongs to the class B G-protein-coupled receptor family and plays a key role in glucose homeostasis and the pathophysiology of type 2 diabetes.
28514451	1	17	theme	glucagon	84:91	arg1	GCGR					103:106	GCGR	103:106	GCGR	103:106	The human glucagon receptor, GCGR, belongs to the class B G-protein-coupled receptor family and plays a key role in glucose homeostasis and the pathophysiology of type 2 diabetes.
28514451	2	18	theme	transmembrane	362:374	arg1	domain					376:381	transmembrane domain	362:381	transmembrane domain	362:381	Here we report the 3.0 Å crystal structure of full-length GCGR containing both the extracellular domain and transmembrane domain in an inactive conformation.
28514451	5	19	theme	crosslinking	801:812	arg1	studies					837:843	Hydrogen-deuterium exchange, disulfide crosslinking and molecular dynamics studies	762:843	Hydrogen-deuterium exchange, disulfide crosslinking and molecular dynamics studies	762:843	Hydrogen-deuterium exchange, disulfide crosslinking and molecular dynamics studies suggest that the stalk and the first extracellular loop have critical roles in modulating peptide ligand binding and receptor activation.
28514451	2	20	theme	crystal	279:285	arg1	structure					287:295	the 3.0 Å crystal structure	269:295	the 3.0 Å crystal structure of full-length GCGR containing both the extracellular domain and transmembrane domain in an inactive conformation	269:409	Here we report the 3.0 Å crystal structure of full-length GCGR containing both the extracellular domain and transmembrane domain in an inactive conformation.
28514451	4	21	theme	first	637:641	arg1	loop					657:660	The first extracellular loop	633:660	The first extracellular loop	633:660	The first extracellular loop exhibits a β-hairpin conformation and interacts with the stalk to form a compact β-sheet structure.
28514451	0	22	theme	full-length	17:27	arg1	receptor					64:71	the full-length glucagon class B G-protein-coupled receptor	13:71	the full-length glucagon class B G-protein-coupled receptor	13:71	Structure of the full-length glucagon class B G-protein-coupled receptor.
28514451	2	23	theme	3.0 Å	273:277	arg1	structure					287:295	the 3.0 Å crystal structure	269:295	the 3.0 Å crystal structure of full-length GCGR containing both the extracellular domain and transmembrane domain in an inactive conformation	269:409	Here we report the 3.0 Å crystal structure of full-length GCGR containing both the extracellular domain and transmembrane domain in an inactive conformation.
28514451	1	24	theme	key	178:180	arg1	role					182:185	a key role	176:185	a key role	176:185	The human glucagon receptor, GCGR, belongs to the class B G-protein-coupled receptor family and plays a key role in glucose homeostasis and the pathophysiology of type 2 diabetes.
28514451	5	25	theme	ligand	943:948	arg1	binding					950:956	peptide ligand binding	935:956	peptide ligand binding	935:956	Hydrogen-deuterium exchange, disulfide crosslinking and molecular dynamics studies suggest that the stalk and the first extracellular loop have critical roles in modulating peptide ligand binding and receptor activation.
28514451	3	26	theme	transmembrane	611:623	arg1	domain					625:630	the GCGR transmembrane domain	602:630	the GCGR transmembrane domain	602:630	The two domains are connected by a 12-residue segment termed the stalk, which adopts a β-strand conformation, instead of forming an α-helix as observed in the previously solved structure of the GCGR transmembrane domain.
28514451	6	27	theme	G-protein-coupled	1099:1115	arg1	receptors					1117:1125	class B G-protein-coupled receptors	1091:1125	class B G-protein-coupled receptors	1091:1125	These insights into the full-length GCGR structure deepen our understanding of the signalling mechanisms of class B G-protein-coupled receptors.
28514451	3	28	theme	12-residue	447:456	arg1	segment					458:464	a 12-residue segment	445:464	a 12-residue segment termed the stalk, which adopts a β-strand conformation, instead of forming an α-helix as observed in the previously solved structure of the GCGR transmembrane domain	445:630	The two domains are connected by a 12-residue segment termed the stalk, which adopts a β-strand conformation, instead of forming an α-helix as observed in the previously solved structure of the GCGR transmembrane domain.
28514451	0	29	theme	class	38:42	arg1	receptor					64:71	the full-length glucagon class B G-protein-coupled receptor	13:71	the full-length glucagon class B G-protein-coupled receptor	13:71	Structure of the full-length glucagon class B G-protein-coupled receptor.
28514451	3	30	theme	domain	625:630	arg1	structure					589:597	the previously solved structure	567:597	the previously solved structure of the GCGR transmembrane domain	567:630	The two domains are connected by a 12-residue segment termed the stalk, which adopts a β-strand conformation, instead of forming an α-helix as observed in the previously solved structure of the GCGR transmembrane domain.
28514451	6	31	theme	mechanisms	1077:1086	arg1	understanding					1045:1057	our understanding	1041:1057	our understanding of the signalling mechanisms of class B G-protein-coupled receptors	1041:1125	These insights into the full-length GCGR structure deepen our understanding of the signalling mechanisms of class B G-protein-coupled receptors.
28514451	2	32	theme	inactive	389:396	arg1	conformation					398:409	an inactive conformation	386:409	an inactive conformation	386:409	Here we report the 3.0 Å crystal structure of full-length GCGR containing both the extracellular domain and transmembrane domain in an inactive conformation.
28514451	0	33	theme	glucagon	29:36	arg1	receptor					64:71	the full-length glucagon class B G-protein-coupled receptor	13:71	the full-length glucagon class B G-protein-coupled receptor	13:71	Structure of the full-length glucagon class B G-protein-coupled receptor.
28514451	5	34	theme	Hydrogen-deuterium	762:779	arg1	exchange					781:788	Hydrogen-deuterium exchange	762:788	Hydrogen-deuterium exchange	762:788	Hydrogen-deuterium exchange, disulfide crosslinking and molecular dynamics studies suggest that the stalk and the first extracellular loop have critical roles in modulating peptide ligand binding and receptor activation.
28514451	1	35	theme	glucose	190:196	arg1	homeostasis					198:208	glucose homeostasis	190:208	glucose homeostasis	190:208	The human glucagon receptor, GCGR, belongs to the class B G-protein-coupled receptor family and plays a key role in glucose homeostasis and the pathophysiology of type 2 diabetes.
28514451	0	36	theme	G-protein-coupled	46:62	arg1	receptor					64:71	the full-length glucagon class B G-protein-coupled receptor	13:71	the full-length glucagon class B G-protein-coupled receptor	13:71	Structure of the full-length glucagon class B G-protein-coupled receptor.
28514451	5	37	theme	first	876:880	arg1	loop					896:899	the first extracellular loop	872:899	the first extracellular loop	872:899	Hydrogen-deuterium exchange, disulfide crosslinking and molecular dynamics studies suggest that the stalk and the first extracellular loop have critical roles in modulating peptide ligand binding and receptor activation.
28514451	5	38	theme	molecular	818:826	arg1	dynamics					828:835	molecular dynamics	818:835	molecular dynamics	818:835	Hydrogen-deuterium exchange, disulfide crosslinking and molecular dynamics studies suggest that the stalk and the first extracellular loop have critical roles in modulating peptide ligand binding and receptor activation.
28514451	3	39	theme	GCGR	606:609	arg1	domain					625:630	the GCGR transmembrane domain	602:630	the GCGR transmembrane domain	602:630	The two domains are connected by a 12-residue segment termed the stalk, which adopts a β-strand conformation, instead of forming an α-helix as observed in the previously solved structure of the GCGR transmembrane domain.
28514451	5	40	theme	critical	906:913	arg1	roles					915:919	critical roles	906:919	critical roles	906:919	Hydrogen-deuterium exchange, disulfide crosslinking and molecular dynamics studies suggest that the stalk and the first extracellular loop have critical roles in modulating peptide ligand binding and receptor activation.
28514451	0	41	theme	B	44:44	arg1	receptor					64:71	the full-length glucagon class B G-protein-coupled receptor	13:71	the full-length glucagon class B G-protein-coupled receptor	13:71	Structure of the full-length glucagon class B G-protein-coupled receptor.
28514451	2	42	theme	GCGR	312:315	arg1	structure					287:295	the 3.0 Å crystal structure	269:295	the 3.0 Å crystal structure of full-length GCGR containing both the extracellular domain and transmembrane domain in an inactive conformation	269:409	Here we report the 3.0 Å crystal structure of full-length GCGR containing both the extracellular domain and transmembrane domain in an inactive conformation.
28514451	5	43	theme	exchange	781:788	arg1	studies					837:843	Hydrogen-deuterium exchange, disulfide crosslinking and molecular dynamics studies	762:843	Hydrogen-deuterium exchange, disulfide crosslinking and molecular dynamics studies	762:843	Hydrogen-deuterium exchange, disulfide crosslinking and molecular dynamics studies suggest that the stalk and the first extracellular loop have critical roles in modulating peptide ligand binding and receptor activation.
28514451	2	44	theme	full-length	300:310	arg1	GCGR					312:315	full-length GCGR	300:315	full-length GCGR containing both the extracellular domain and transmembrane domain in an inactive conformation	300:409	Here we report the 3.0 Å crystal structure of full-length GCGR containing both the extracellular domain and transmembrane domain in an inactive conformation.
28514451	4	45	theme	β-sheet	743:749	arg1	structure					751:759	a compact β-sheet structure	733:759	a compact β-sheet structure	733:759	The first extracellular loop exhibits a β-hairpin conformation and interacts with the stalk to form a compact β-sheet structure.
28514451	5	46	theme	receptor	962:969	arg1	activation					971:980	receptor activation	962:980	receptor activation	962:980	Hydrogen-deuterium exchange, disulfide crosslinking and molecular dynamics studies suggest that the stalk and the first extracellular loop have critical roles in modulating peptide ligand binding and receptor activation.
28514451	5	47	contain	have	901:904	arg1	loop					896:899	the first extracellular loop	872:899	the first extracellular loop	872:899	Hydrogen-deuterium exchange, disulfide crosslinking and molecular dynamics studies suggest that the stalk and the first extracellular loop have critical roles in modulating peptide ligand binding and receptor activation.
28514451	5	47	contain	have	901:904	arg1	stalk					862:866	the stalk	858:866	the stalk	858:866	Hydrogen-deuterium exchange, disulfide crosslinking and molecular dynamics studies suggest that the stalk and the first extracellular loop have critical roles in modulating peptide ligand binding and receptor activation.
28514451	5	47	contain	have	901:904	arg2	roles					915:919	critical roles	906:919	critical roles	906:919	Hydrogen-deuterium exchange, disulfide crosslinking and molecular dynamics studies suggest that the stalk and the first extracellular loop have critical roles in modulating peptide ligand binding and receptor activation.
28514451	2	48	theme	extracellular	337:349	arg1	domain					351:356	the extracellular domain	333:356	the extracellular domain	333:356	Here we report the 3.0 Å crystal structure of full-length GCGR containing both the extracellular domain and transmembrane domain in an inactive conformation.
28514451	5	49	theme	extracellular	882:894	arg1	loop					896:899	the first extracellular loop	872:899	the first extracellular loop	872:899	Hydrogen-deuterium exchange, disulfide crosslinking and molecular dynamics studies suggest that the stalk and the first extracellular loop have critical roles in modulating peptide ligand binding and receptor activation.
28514451	5	50	theme	dynamics	828:835	arg1	studies					837:843	Hydrogen-deuterium exchange, disulfide crosslinking and molecular dynamics studies	762:843	Hydrogen-deuterium exchange, disulfide crosslinking and molecular dynamics studies	762:843	Hydrogen-deuterium exchange, disulfide crosslinking and molecular dynamics studies suggest that the stalk and the first extracellular loop have critical roles in modulating peptide ligand binding and receptor activation.
28514451	1	51	theme	class	124:128	arg1	family					159:164	the class B G-protein-coupled receptor family	120:164	the class B G-protein-coupled receptor family	120:164	The human glucagon receptor, GCGR, belongs to the class B G-protein-coupled receptor family and plays a key role in glucose homeostasis and the pathophysiology of type 2 diabetes.
28514451	0	52	theme	receptor	64:71	arg1	Structure					0:8	Structure	0:8	Structure of the full-length glucagon class B G-protein-coupled receptor	0:71	Structure of the full-length glucagon class B G-protein-coupled receptor.
28514451	3	53	theme	solved	582:587	arg1	structure					589:597	the previously solved structure	567:597	the previously solved structure of the GCGR transmembrane domain	567:630	The two domains are connected by a 12-residue segment termed the stalk, which adopts a β-strand conformation, instead of forming an α-helix as observed in the previously solved structure of the GCGR transmembrane domain.
28514451	1	54	theme	B	130:130	arg1	family					159:164	the class B G-protein-coupled receptor family	120:164	the class B G-protein-coupled receptor family	120:164	The human glucagon receptor, GCGR, belongs to the class B G-protein-coupled receptor family and plays a key role in glucose homeostasis and the pathophysiology of type 2 diabetes.
28514451	6	55	theme	GCGR	1019:1022	arg1	structure					1024:1032	the full-length GCGR structure	1003:1032	the full-length GCGR structure	1003:1032	These insights into the full-length GCGR structure deepen our understanding of the signalling mechanisms of class B G-protein-coupled receptors.
22908259	5	0	theme	antibody	718:725	arg1	fragment					702:709	the Fab fragment	694:709	the Fab fragment of one antibody, mAb1,	694:732	The crystal structure of the ECD in complex with the Fab fragment of one antibody, mAb1, reveals that this antibody inhibits glucagon receptor by occluding a surface extending across the entire hormone-binding cleft.
22908259	7	1	theme	structure	1162:1170	arg1	context					1129:1135	the context	1125:1135	the context of a high-resolution ECD structure	1125:1170	Biochemical analyses of receptor mutants in the context of a high-resolution ECD structure show that this previously unrecognized inhibitory activity of the ECD involves an interaction with the third extracellular loop of the receptor and suggest that glucagon-mediated structural changes in the ECD accompany receptor activation.
22908259	6	2	theme	receptor	931:938	arg1	activity					940:947	basal receptor activity	925:947	basal receptor activity	925:947	A second antibody, mAb23, blocks glucagon binding and inhibits basal receptor activity, indicating that it is an inverse agonist and that the ECD can negatively regulate receptor activity independent of ligand binding.
22908259	8	3	theme	receptors	1605:1613	arg1	ECDs					1591:1594	the ECDs	1587:1594	the ECDs of these receptors	1587:1613	These studies have implications for the design of drugs to treat class B GPCR-related diseases, including the potential for developing novel allosteric regulators that target the ECDs of these receptors.
22908259	7	4	from	analyses	1093:1100	arg1	context					1129:1135	the context	1125:1135	the context of a high-resolution ECD structure	1125:1170	Biochemical analyses of receptor mutants in the context of a high-resolution ECD structure show that this previously unrecognized inhibitory activity of the ECD involves an interaction with the third extracellular loop of the receptor and suggest that glucagon-mediated structural changes in the ECD accompany receptor activation.
22908259	6	5	theme	second	864:869	arg1	mAb23					881:885	mAb23	881:885	mAb23	881:885	A second antibody, mAb23, blocks glucagon binding and inhibits basal receptor activity, indicating that it is an inverse agonist and that the ECD can negatively regulate receptor activity independent of ligand binding.
22908259	6	5	theme	second	864:869	arg1	antibody					871:878	A second antibody	862:878	A second antibody	862:878	A second antibody, mAb23, blocks glucagon binding and inhibits basal receptor activity, indicating that it is an inverse agonist and that the ECD can negatively regulate receptor activity independent of ligand binding.
22908259	2	6	theme	GPCRs	315:319	arg1	peptide					257:263	peptide, small-molecule, and antibody inhibitors	257:304	peptide	257:263	Although peptide, small-molecule, and antibody inhibitors of these GPCRs have been identified, structure-based descriptions of receptor antagonism are scarce.
22908259	2	6	theme	GPCRs	315:319	arg1	inhibitors					295:304	peptide, small-molecule, and antibody inhibitors	257:304	inhibitors	295:304	Although peptide, small-molecule, and antibody inhibitors of these GPCRs have been identified, structure-based descriptions of receptor antagonism are scarce.
22908259	5	7	from	complex	681:687	arg1	structure					657:665	The crystal structure	645:665	The crystal structure of the ECD in complex with the Fab fragment of one antibody, mAb1,	645:732	The crystal structure of the ECD in complex with the Fab fragment of one antibody, mAb1, reveals that this antibody inhibits glucagon receptor by occluding a surface extending across the entire hormone-binding cleft.
22908259	7	8	theme	high-resolution	1142:1156	arg1	structure					1162:1170	a high-resolution ECD structure	1140:1170	a high-resolution ECD structure	1140:1170	Biochemical analyses of receptor mutants in the context of a high-resolution ECD structure show that this previously unrecognized inhibitory activity of the ECD involves an interaction with the third extracellular loop of the receptor and suggest that glucagon-mediated structural changes in the ECD accompany receptor activation.
22908259	8	9	theme	class	1477:1481	arg1	diseases					1498:1505	class B GPCR-related diseases	1477:1505	class B GPCR-related diseases	1477:1505	These studies have implications for the design of drugs to treat class B GPCR-related diseases, including the potential for developing novel allosteric regulators that target the ECDs of these receptors.
22908259	8	9	theme	class	1477:1481	arg1	potential					1522:1530	the potential	1518:1530	the potential for developing novel allosteric regulators that target the ECDs of these receptors	1518:1613	These studies have implications for the design of drugs to treat class B GPCR-related diseases, including the potential for developing novel allosteric regulators that target the ECDs of these receptors.
22908259	8	10	contain	have	1426:1429	arg1	studies					1418:1424	These studies	1412:1424	These studies	1412:1424	These studies have implications for the design of drugs to treat class B GPCR-related diseases, including the potential for developing novel allosteric regulators that target the ECDs of these receptors.
22908259	8	10	contain	have	1426:1429	arg2	implications					1431:1442	implications	1431:1442	implications for the design of drugs to treat class B GPCR-related diseases, including the potential for developing novel allosteric regulators that target the ECDs of these receptors	1431:1613	These studies have implications for the design of drugs to treat class B GPCR-related diseases, including the potential for developing novel allosteric regulators that target the ECDs of these receptors.
22908259	7	11	theme	ECD	1158:1160	arg1	structure					1162:1170	a high-resolution ECD structure	1140:1170	a high-resolution ECD structure	1140:1170	Biochemical analyses of receptor mutants in the context of a high-resolution ECD structure show that this previously unrecognized inhibitory activity of the ECD involves an interaction with the third extracellular loop of the receptor and suggest that glucagon-mediated structural changes in the ECD accompany receptor activation.
22908259	7	12	from	changes	1362:1368	arg1	ECD					1377:1379	the ECD	1373:1379	the ECD	1373:1379	Biochemical analyses of receptor mutants in the context of a high-resolution ECD structure show that this previously unrecognized inhibitory activity of the ECD involves an interaction with the third extracellular loop of the receptor and suggest that glucagon-mediated structural changes in the ECD accompany receptor activation.
22908259	7	13	theme	unrecognized	1198:1209	arg1	activity					1222:1229	this previously unrecognized inhibitory activity	1182:1229	this previously unrecognized inhibitory activity of the ECD	1182:1240	Biochemical analyses of receptor mutants in the context of a high-resolution ECD structure show that this previously unrecognized inhibitory activity of the ECD involves an interaction with the third extracellular loop of the receptor and suggest that glucagon-mediated structural changes in the ECD accompany receptor activation.
22908259	6	14	theme	receptor	1032:1039	arg1	activity					1041:1048	receptor activity	1032:1048	receptor activity independent of ligand binding	1032:1078	A second antibody, mAb23, blocks glucagon binding and inhibits basal receptor activity, indicating that it is an inverse agonist and that the ECD can negatively regulate receptor activity independent of ligand binding.
22908259	2	15	theme	antibody	286:293	arg1	inhibitors					295:304	peptide, small-molecule, and antibody inhibitors	257:304	inhibitors	295:304	Although peptide, small-molecule, and antibody inhibitors of these GPCRs have been identified, structure-based descriptions of receptor antagonism are scarce.
22908259	5	16	theme	Fab	698:700	arg1	fragment					702:709	the Fab fragment	694:709	the Fab fragment of one antibody, mAb1,	694:732	The crystal structure of the ECD in complex with the Fab fragment of one antibody, mAb1, reveals that this antibody inhibits glucagon receptor by occluding a surface extending across the entire hormone-binding cleft.
22908259	8	17	theme	GPCR-related	1485:1496	arg1	diseases					1498:1505	class B GPCR-related diseases	1477:1505	class B GPCR-related diseases	1477:1505	These studies have implications for the design of drugs to treat class B GPCR-related diseases, including the potential for developing novel allosteric regulators that target the ECDs of these receptors.
22908259	8	17	theme	GPCR-related	1485:1496	arg1	potential					1522:1530	the potential	1518:1530	the potential for developing novel allosteric regulators that target the ECDs of these receptors	1518:1613	These studies have implications for the design of drugs to treat class B GPCR-related diseases, including the potential for developing novel allosteric regulators that target the ECDs of these receptors.
22908259	5	18	with	complex	681:687	arg1	fragment					702:709	the Fab fragment	694:709	the Fab fragment of one antibody, mAb1,	694:732	The crystal structure of the ECD in complex with the Fab fragment of one antibody, mAb1, reveals that this antibody inhibits glucagon receptor by occluding a surface extending across the entire hormone-binding cleft.
22908259	7	19	theme	receptor	1391:1398	arg1	activation					1400:1409	receptor activation	1391:1409	receptor activation	1391:1409	Biochemical analyses of receptor mutants in the context of a high-resolution ECD structure show that this previously unrecognized inhibitory activity of the ECD involves an interaction with the third extracellular loop of the receptor and suggest that glucagon-mediated structural changes in the ECD accompany receptor activation.
22908259	7	20	theme	third	1275:1279	arg1	loop					1295:1298	the third extracellular loop	1271:1298	the third extracellular loop of the receptor	1271:1314	Biochemical analyses of receptor mutants in the context of a high-resolution ECD structure show that this previously unrecognized inhibitory activity of the ECD involves an interaction with the third extracellular loop of the receptor and suggest that glucagon-mediated structural changes in the ECD accompany receptor activation.
22908259	1	21	theme	peptide	140:146	arg1	hormones					148:155	peptide hormones	140:155	peptide hormones	140:155	Members of the class B family of G protein-coupled receptors (GPCRs) bind peptide hormones and have causal roles in many diseases, ranging from diabetes and osteoporosis to anxiety.
22908259	5	22	from	ECD	674:676	arg1	complex					681:687	complex	681:687	complex with the Fab fragment of one antibody, mAb1,	681:732	The crystal structure of the ECD in complex with the Fab fragment of one antibody, mAb1, reveals that this antibody inhibits glucagon receptor by occluding a surface extending across the entire hormone-binding cleft.
22908259	6	23	theme	ligand	1065:1070	arg1	binding					1072:1078	ligand binding	1065:1078	ligand binding	1065:1078	A second antibody, mAb23, blocks glucagon binding and inhibits basal receptor activity, indicating that it is an inverse agonist and that the ECD can negatively regulate receptor activity independent of ligand binding.
22908259	7	24	theme	Biochemical	1081:1091	arg1	analyses					1093:1100	Biochemical analyses	1081:1100	Biochemical analyses of receptor mutants in the context of a high-resolution ECD structure	1081:1170	Biochemical analyses of receptor mutants in the context of a high-resolution ECD structure show that this previously unrecognized inhibitory activity of the ECD involves an interaction with the third extracellular loop of the receptor and suggest that glucagon-mediated structural changes in the ECD accompany receptor activation.
22908259	3	25	theme	extracellular	517:529	arg1	domain					531:536	the receptor's extracellular domain	502:536	the receptor's extracellular domain (ECD)	502:542	Here we report the mechanisms of glucagon receptor inhibition by blocking antibodies targeting the receptor's extracellular domain (ECD).
22908259	3	25	theme	extracellular	517:529	arg1	ECD					539:541	ECD	539:541	ECD	539:541	Here we report the mechanisms of glucagon receptor inhibition by blocking antibodies targeting the receptor's extracellular domain (ECD).
22908259	2	26	theme	structure-based	343:357	arg1	descriptions					359:370	structure-based descriptions	343:370	structure-based descriptions of receptor antagonism	343:393	Although peptide, small-molecule, and antibody inhibitors of these GPCRs have been identified, structure-based descriptions of receptor antagonism are scarce.
22908259	2	26	theme	structure-based	343:357	arg1	scarce					399:404	scarce	399:404	scarce	399:404	Although peptide, small-molecule, and antibody inhibitors of these GPCRs have been identified, structure-based descriptions of receptor antagonism are scarce.
22908259	0	27	theme	Molecular	0:8	arg1	basis					10:14	Molecular basis	0:14	Molecular basis for negative regulation of the glucagon receptor	0:63	Molecular basis for negative regulation of the glucagon receptor.
22908259	6	28	theme	basal	925:929	arg1	activity					940:947	basal receptor activity	925:947	basal receptor activity	925:947	A second antibody, mAb23, blocks glucagon binding and inhibits basal receptor activity, indicating that it is an inverse agonist and that the ECD can negatively regulate receptor activity independent of ligand binding.
22908259	1	29	theme	class	81:85	arg1	family					89:94	the class B family	77:94	the class B family of G protein-coupled receptors (GPCRs)	77:133	Members of the class B family of G protein-coupled receptors (GPCRs) bind peptide hormones and have causal roles in many diseases, ranging from diabetes and osteoporosis to anxiety.
22908259	7	30	with	interaction	1254:1264	arg1	loop					1295:1298	the third extracellular loop	1271:1298	the third extracellular loop of the receptor	1271:1314	Biochemical analyses of receptor mutants in the context of a high-resolution ECD structure show that this previously unrecognized inhibitory activity of the ECD involves an interaction with the third extracellular loop of the receptor and suggest that glucagon-mediated structural changes in the ECD accompany receptor activation.
22908259	4	31	theme	activity	635:642	arg1	regulator					613:621	an intrinsic negative regulator	591:621	an intrinsic negative regulator of receptor activity	591:642	These studies uncovered a role for the ECD as an intrinsic negative regulator of receptor activity.
22908259	0	32	theme	negative	20:27	arg1	regulation					29:38	negative regulation	20:38	negative regulation of the glucagon receptor	20:63	Molecular basis for negative regulation of the glucagon receptor.
22908259	2	33	theme	small-molecule	266:279	arg1	peptide					257:263	peptide, small-molecule, and antibody inhibitors	257:304	peptide	257:263	Although peptide, small-molecule, and antibody inhibitors of these GPCRs have been identified, structure-based descriptions of receptor antagonism are scarce.
22908259	7	34	theme	structural	1351:1360	arg1	changes					1362:1368	glucagon-mediated structural changes	1333:1368	glucagon-mediated structural changes in the ECD	1333:1379	Biochemical analyses of receptor mutants in the context of a high-resolution ECD structure show that this previously unrecognized inhibitory activity of the ECD involves an interaction with the third extracellular loop of the receptor and suggest that glucagon-mediated structural changes in the ECD accompany receptor activation.
22908259	1	35	theme	causal	166:171	arg1	roles					173:177	causal roles	166:177	causal roles in many diseases, ranging from diabetes and osteoporosis to anxiety	166:245	Members of the class B family of G protein-coupled receptors (GPCRs) bind peptide hormones and have causal roles in many diseases, ranging from diabetes and osteoporosis to anxiety.
22908259	5	36	theme	glucagon	770:777	arg1	receptor					779:786	glucagon receptor	770:786	glucagon receptor	770:786	The crystal structure of the ECD in complex with the Fab fragment of one antibody, mAb1, reveals that this antibody inhibits glucagon receptor by occluding a surface extending across the entire hormone-binding cleft.
22908259	5	37	theme	ECD	674:676	arg1	structure					657:665	The crystal structure	645:665	The crystal structure of the ECD in complex with the Fab fragment of one antibody, mAb1,	645:732	The crystal structure of the ECD in complex with the Fab fragment of one antibody, mAb1, reveals that this antibody inhibits glucagon receptor by occluding a surface extending across the entire hormone-binding cleft.
22908259	1	38	contain	have	161:164	arg1	Members					66:72	Members	66:72	Members of the class B family of G protein-coupled receptors (GPCRs)	66:133	Members of the class B family of G protein-coupled receptors (GPCRs) bind peptide hormones and have causal roles in many diseases, ranging from diabetes and osteoporosis to anxiety.
22908259	1	38	contain	have	161:164	arg2	roles					173:177	causal roles	166:177	causal roles in many diseases, ranging from diabetes and osteoporosis to anxiety	166:245	Members of the class B family of G protein-coupled receptors (GPCRs) bind peptide hormones and have causal roles in many diseases, ranging from diabetes and osteoporosis to anxiety.
22908259	1	39	theme	family	89:94	arg1	Members					66:72	Members	66:72	Members of the class B family of G protein-coupled receptors (GPCRs)	66:133	Members of the class B family of G protein-coupled receptors (GPCRs) bind peptide hormones and have causal roles in many diseases, ranging from diabetes and osteoporosis to anxiety.
22908259	3	40	theme	glucagon	440:447	arg1	inhibition					458:467	glucagon receptor inhibition	440:467	glucagon receptor inhibition	440:467	Here we report the mechanisms of glucagon receptor inhibition by blocking antibodies targeting the receptor's extracellular domain (ECD).
22908259	7	41	theme	inhibitory	1211:1220	arg1	activity					1222:1229	this previously unrecognized inhibitory activity	1182:1229	this previously unrecognized inhibitory activity of the ECD	1182:1240	Biochemical analyses of receptor mutants in the context of a high-resolution ECD structure show that this previously unrecognized inhibitory activity of the ECD involves an interaction with the third extracellular loop of the receptor and suggest that glucagon-mediated structural changes in the ECD accompany receptor activation.
22908259	4	42	theme	negative	604:611	arg1	regulator					613:621	an intrinsic negative regulator	591:621	an intrinsic negative regulator of receptor activity	591:642	These studies uncovered a role for the ECD as an intrinsic negative regulator of receptor activity.
22908259	7	43	theme	extracellular	1281:1293	arg1	loop					1295:1298	the third extracellular loop	1271:1298	the third extracellular loop of the receptor	1271:1314	Biochemical analyses of receptor mutants in the context of a high-resolution ECD structure show that this previously unrecognized inhibitory activity of the ECD involves an interaction with the third extracellular loop of the receptor and suggest that glucagon-mediated structural changes in the ECD accompany receptor activation.
22908259	2	44	theme	antagonism	384:393	arg1	descriptions					359:370	structure-based descriptions	343:370	structure-based descriptions of receptor antagonism	343:393	Although peptide, small-molecule, and antibody inhibitors of these GPCRs have been identified, structure-based descriptions of receptor antagonism are scarce.
22908259	2	44	theme	antagonism	384:393	arg1	scarce					399:404	scarce	399:404	scarce	399:404	Although peptide, small-molecule, and antibody inhibitors of these GPCRs have been identified, structure-based descriptions of receptor antagonism are scarce.
22908259	4	45	theme	receptor	626:633	arg1	activity					635:642	receptor activity	626:642	receptor activity	626:642	These studies uncovered a role for the ECD as an intrinsic negative regulator of receptor activity.
22908259	6	46	theme	glucagon	895:902	arg1	binding					904:910	glucagon binding	895:910	glucagon binding	895:910	A second antibody, mAb23, blocks glucagon binding and inhibits basal receptor activity, indicating that it is an inverse agonist and that the ECD can negatively regulate receptor activity independent of ligand binding.
22908259	7	47	theme	receptor	1105:1112	arg1	mutants					1114:1120	receptor mutants	1105:1120	receptor mutants	1105:1120	Biochemical analyses of receptor mutants in the context of a high-resolution ECD structure show that this previously unrecognized inhibitory activity of the ECD involves an interaction with the third extracellular loop of the receptor and suggest that glucagon-mediated structural changes in the ECD accompany receptor activation.
22908259	7	48	theme	mutants	1114:1120	arg1	analyses					1093:1100	Biochemical analyses	1081:1100	Biochemical analyses of receptor mutants in the context of a high-resolution ECD structure	1081:1170	Biochemical analyses of receptor mutants in the context of a high-resolution ECD structure show that this previously unrecognized inhibitory activity of the ECD involves an interaction with the third extracellular loop of the receptor and suggest that glucagon-mediated structural changes in the ECD accompany receptor activation.
22908259	2	49	theme	receptor	375:382	arg1	antagonism					384:393	receptor antagonism	375:393	receptor antagonism	375:393	Although peptide, small-molecule, and antibody inhibitors of these GPCRs have been identified, structure-based descriptions of receptor antagonism are scarce.
22908259	0	50	theme	glucagon	47:54	arg1	receptor					56:63	the glucagon receptor	43:63	the glucagon receptor	43:63	Molecular basis for negative regulation of the glucagon receptor.
22908259	8	51	theme	novel	1547:1551	arg1	regulators					1564:1573	novel allosteric regulators	1547:1573	novel allosteric regulators that target the ECDs of these receptors	1547:1613	These studies have implications for the design of drugs to treat class B GPCR-related diseases, including the potential for developing novel allosteric regulators that target the ECDs of these receptors.
22908259	6	52	theme	inverse	975:981	arg1	it					966:967	it	966:967	it	966:967	A second antibody, mAb23, blocks glucagon binding and inhibits basal receptor activity, indicating that it is an inverse agonist and that the ECD can negatively regulate receptor activity independent of ligand binding.
22908259	6	52	theme	inverse	975:981	arg1	agonist					983:989	an inverse agonist	972:989	an inverse agonist	972:989	A second antibody, mAb23, blocks glucagon binding and inhibits basal receptor activity, indicating that it is an inverse agonist and that the ECD can negatively regulate receptor activity independent of ligand binding.
22908259	6	53	theme	independent	1050:1060	arg1	activity					1041:1048	receptor activity	1032:1048	receptor activity independent of ligand binding	1032:1078	A second antibody, mAb23, blocks glucagon binding and inhibits basal receptor activity, indicating that it is an inverse agonist and that the ECD can negatively regulate receptor activity independent of ligand binding.
22908259	7	54	theme	ECD	1238:1240	arg1	activity					1222:1229	this previously unrecognized inhibitory activity	1182:1229	this previously unrecognized inhibitory activity of the ECD	1182:1240	Biochemical analyses of receptor mutants in the context of a high-resolution ECD structure show that this previously unrecognized inhibitory activity of the ECD involves an interaction with the third extracellular loop of the receptor and suggest that glucagon-mediated structural changes in the ECD accompany receptor activation.
22908259	5	55	theme	crystal	649:655	arg1	structure					657:665	The crystal structure	645:665	The crystal structure of the ECD in complex with the Fab fragment of one antibody, mAb1,	645:732	The crystal structure of the ECD in complex with the Fab fragment of one antibody, mAb1, reveals that this antibody inhibits glucagon receptor by occluding a surface extending across the entire hormone-binding cleft.
22908259	7	56	theme	glucagon-mediated	1333:1349	arg1	changes					1362:1368	glucagon-mediated structural changes	1333:1368	glucagon-mediated structural changes in the ECD	1333:1379	Biochemical analyses of receptor mutants in the context of a high-resolution ECD structure show that this previously unrecognized inhibitory activity of the ECD involves an interaction with the third extracellular loop of the receptor and suggest that glucagon-mediated structural changes in the ECD accompany receptor activation.
22908259	6	57	theme	binding	1072:1078	arg1	independent					1050:1060	independent	1050:1060	independent	1050:1060	A second antibody, mAb23, blocks glucagon binding and inhibits basal receptor activity, indicating that it is an inverse agonist and that the ECD can negatively regulate receptor activity independent of ligand binding.
22908259	1	58	from	roles	173:177	arg1	diseases					187:194	many diseases	182:194	many diseases	182:194	Members of the class B family of G protein-coupled receptors (GPCRs) bind peptide hormones and have causal roles in many diseases, ranging from diabetes and osteoporosis to anxiety.
22908259	1	59	theme	protein-coupled	101:115	arg1	GPCRs					128:132	GPCRs	128:132	GPCRs	128:132	Members of the class B family of G protein-coupled receptors (GPCRs) bind peptide hormones and have causal roles in many diseases, ranging from diabetes and osteoporosis to anxiety.
22908259	1	59	theme	protein-coupled	101:115	arg1	receptors					117:125	G protein-coupled receptors	99:125	G protein-coupled receptors (GPCRs)	99:133	Members of the class B family of G protein-coupled receptors (GPCRs) bind peptide hormones and have causal roles in many diseases, ranging from diabetes and osteoporosis to anxiety.
22908259	1	60	theme	B	87:87	arg1	family					89:94	the class B family	77:94	the class B family of G protein-coupled receptors (GPCRs)	77:133	Members of the class B family of G protein-coupled receptors (GPCRs) bind peptide hormones and have causal roles in many diseases, ranging from diabetes and osteoporosis to anxiety.
22908259	5	61	from	structure	657:665	arg1	complex					681:687	complex	681:687	complex with the Fab fragment of one antibody, mAb1,	681:732	The crystal structure of the ECD in complex with the Fab fragment of one antibody, mAb1, reveals that this antibody inhibits glucagon receptor by occluding a surface extending across the entire hormone-binding cleft.
22908259	8	62	theme	drugs	1462:1466	arg1	design					1452:1457	the design	1448:1457	the design of drugs to treat class B GPCR-related diseases, including the potential for developing novel allosteric regulators that target the ECDs of these receptors	1448:1613	These studies have implications for the design of drugs to treat class B GPCR-related diseases, including the potential for developing novel allosteric regulators that target the ECDs of these receptors.
22908259	1	63	theme	receptors	117:125	arg1	family					89:94	the class B family	77:94	the class B family of G protein-coupled receptors (GPCRs)	77:133	Members of the class B family of G protein-coupled receptors (GPCRs) bind peptide hormones and have causal roles in many diseases, ranging from diabetes and osteoporosis to anxiety.
22908259	3	64	theme	receptor	449:456	arg1	inhibition					458:467	glucagon receptor inhibition	440:467	glucagon receptor inhibition	440:467	Here we report the mechanisms of glucagon receptor inhibition by blocking antibodies targeting the receptor's extracellular domain (ECD).
22908259	8	65	theme	B	1483:1483	arg1	diseases					1498:1505	class B GPCR-related diseases	1477:1505	class B GPCR-related diseases	1477:1505	These studies have implications for the design of drugs to treat class B GPCR-related diseases, including the potential for developing novel allosteric regulators that target the ECDs of these receptors.
22908259	8	65	theme	B	1483:1483	arg1	potential					1522:1530	the potential	1518:1530	the potential for developing novel allosteric regulators that target the ECDs of these receptors	1518:1613	These studies have implications for the design of drugs to treat class B GPCR-related diseases, including the potential for developing novel allosteric regulators that target the ECDs of these receptors.
22908259	1	66	theme	many	182:185	arg1	diseases					187:194	many diseases	182:194	many diseases	182:194	Members of the class B family of G protein-coupled receptors (GPCRs) bind peptide hormones and have causal roles in many diseases, ranging from diabetes and osteoporosis to anxiety.
22908259	4	67	theme	intrinsic	594:602	arg1	regulator					613:621	an intrinsic negative regulator	591:621	an intrinsic negative regulator of receptor activity	591:642	These studies uncovered a role for the ECD as an intrinsic negative regulator of receptor activity.
22908259	5	68	theme	entire	832:837	arg1	cleft					855:859	the entire hormone-binding cleft	828:859	the entire hormone-binding cleft	828:859	The crystal structure of the ECD in complex with the Fab fragment of one antibody, mAb1, reveals that this antibody inhibits glucagon receptor by occluding a surface extending across the entire hormone-binding cleft.
22908259	3	69	theme	inhibition	458:467	arg1	mechanisms					426:435	the mechanisms	422:435	the mechanisms of glucagon receptor inhibition	422:467	Here we report the mechanisms of glucagon receptor inhibition by blocking antibodies targeting the receptor's extracellular domain (ECD).
22908259	8	70	theme	allosteric	1553:1562	arg1	regulators					1564:1573	novel allosteric regulators	1547:1573	novel allosteric regulators that target the ECDs of these receptors	1547:1613	These studies have implications for the design of drugs to treat class B GPCR-related diseases, including the potential for developing novel allosteric regulators that target the ECDs of these receptors.
22908259	0	71	theme	receptor	56:63	arg1	regulation					29:38	negative regulation	20:38	negative regulation of the glucagon receptor	20:63	Molecular basis for negative regulation of the glucagon receptor.
22908259	7	72	theme	receptor	1307:1314	arg1	loop					1295:1298	the third extracellular loop	1271:1298	the third extracellular loop of the receptor	1271:1314	Biochemical analyses of receptor mutants in the context of a high-resolution ECD structure show that this previously unrecognized inhibitory activity of the ECD involves an interaction with the third extracellular loop of the receptor and suggest that glucagon-mediated structural changes in the ECD accompany receptor activation.
22908259	5	73	theme	hormone-binding	839:853	arg1	cleft					855:859	the entire hormone-binding cleft	828:859	the entire hormone-binding cleft	828:859	The crystal structure of the ECD in complex with the Fab fragment of one antibody, mAb1, reveals that this antibody inhibits glucagon receptor by occluding a surface extending across the entire hormone-binding cleft.
19383836	7	0	theme	potential	1330:1338	arg1	risk					1340:1343	potential risk	1330:1343	potential risk	1330:1343	For rapid genetic diagnosis of axillary osmidrosis and potential risk of breast cancer, we developed specific primers for the SmartAmp method that enabled us to clinically genotype the ABCC11 gene within 30 min.
19383836	6	1	theme	dry	1207:1209	arg1	type					1211:1214	the dry type	1203:1214	the dry type of earwax	1203:1224	This SNP variant lacking N-linked glycosylation is recognized as a misfolded protein in the endoplasmic reticulum and readily undergoes ubiquitination and proteasomal degradation, which determines the dry type of earwax as a mendelian trait with a recessive phenotype.
19383836	6	1	theme	dry	1207:1209	arg1	trait					1241:1245	a mendelian trait	1229:1245	a mendelian trait with a recessive phenotype	1229:1272	This SNP variant lacking N-linked glycosylation is recognized as a misfolded protein in the endoplasmic reticulum and readily undergoes ubiquitination and proteasomal degradation, which determines the dry type of earwax as a mendelian trait with a recessive phenotype.
19383836	4	2	theme	ABCC11	587:592	arg1	degradation					634:644	proteasomal degradation	622:644	proteasomal degradation of the variant protein	622:667	We herein provide the evidence that this genetic polymorphism has an effect on the N-linked glycosylation of ABCC11, intracellular sorting, and proteasomal degradation of the variant protein.
19383836	4	2	theme	ABCC11	587:592	arg1	sorting					609:615	intracellular sorting	595:615	intracellular sorting	595:615	We herein provide the evidence that this genetic polymorphism has an effect on the N-linked glycosylation of ABCC11, intracellular sorting, and proteasomal degradation of the variant protein.
19383836	4	2	theme	ABCC11	587:592	arg1	glycosylation					570:582	the N-linked glycosylation	557:582	the N-linked glycosylation of ABCC11	557:592	We herein provide the evidence that this genetic polymorphism has an effect on the N-linked glycosylation of ABCC11, intracellular sorting, and proteasomal degradation of the variant protein.
19383836	5	3	from	cells	889:893	arg1	gland					910:914	the cerumen gland	898:914	the cerumen gland	898:914	Immunohistochemical studies with cerumen gland-containing tissue specimens revealed that the ABCC11 WT protein was localized in intracellular granules and large vacuoles, as well as at the luminal membrane of secretory cells in the cerumen gland, whereas granular or vacuolar localization was not detected for the SNP (Arg180) variant.
19383836	6	4	link	N-linked	1031:1038	arg1	glycosylation					1040:1052	N-linked glycosylation	1031:1052	N-linked glycosylation	1031:1052	This SNP variant lacking N-linked glycosylation is recognized as a misfolded protein in the endoplasmic reticulum and readily undergoes ubiquitination and proteasomal degradation, which determines the dry type of earwax as a mendelian trait with a recessive phenotype.
19383836	5	5	theme	SNP	984:986	arg1	variant					997:1003	the SNP (Arg180) variant	980:1003	the SNP (Arg180) variant	980:1003	Immunohistochemical studies with cerumen gland-containing tissue specimens revealed that the ABCC11 WT protein was localized in intracellular granules and large vacuoles, as well as at the luminal membrane of secretory cells in the cerumen gland, whereas granular or vacuolar localization was not detected for the SNP (Arg180) variant.
19383836	5	6	from	membrane	867:874	arg1	gland					910:914	the cerumen gland	898:914	the cerumen gland	898:914	Immunohistochemical studies with cerumen gland-containing tissue specimens revealed that the ABCC11 WT protein was localized in intracellular granules and large vacuoles, as well as at the luminal membrane of secretory cells in the cerumen gland, whereas granular or vacuolar localization was not detected for the SNP (Arg180) variant.
19383836	5	7	theme	cells	889:893	arg1	membrane					867:874	the luminal membrane	855:874	the luminal membrane of secretory cells in the cerumen gland	855:914	Immunohistochemical studies with cerumen gland-containing tissue specimens revealed that the ABCC11 WT protein was localized in intracellular granules and large vacuoles, as well as at the luminal membrane of secretory cells in the cerumen gland, whereas granular or vacuolar localization was not detected for the SNP (Arg180) variant.
19383836	7	8	theme	specific	1376:1383	arg1	primers					1385:1391	specific primers	1376:1391	specific primers for the SmartAmp method that enabled us to clinically genotype the ABCC11 gene within 30 min	1376:1484	For rapid genetic diagnosis of axillary osmidrosis and potential risk of breast cancer, we developed specific primers for the SmartAmp method that enabled us to clinically genotype the ABCC11 gene within 30 min.
19383836	5	9	theme	granular	925:932	arg1	localization					946:957	granular or vacuolar localization	925:957	granular or vacuolar localization	925:957	Immunohistochemical studies with cerumen gland-containing tissue specimens revealed that the ABCC11 WT protein was localized in intracellular granules and large vacuoles, as well as at the luminal membrane of secretory cells in the cerumen gland, whereas granular or vacuolar localization was not detected for the SNP (Arg180) variant.
19383836	3	10	theme	migratory	431:439	arg1	waves					441:445	global migratory waves	424:445	global migratory waves of the ancestors of humankind	424:475	Wide ethnic differences exist in the frequencies of those alleles, reflecting global migratory waves of the ancestors of humankind.
19383836	5	11	theme	luminal	859:865	arg1	membrane					867:874	the luminal membrane	855:874	the luminal membrane of secretory cells in the cerumen gland	855:914	Immunohistochemical studies with cerumen gland-containing tissue specimens revealed that the ABCC11 WT protein was localized in intracellular granules and large vacuoles, as well as at the luminal membrane of secretory cells in the cerumen gland, whereas granular or vacuolar localization was not detected for the SNP (Arg180) variant.
19383836	4	12	theme	proteasomal	622:632	arg1	degradation					634:644	proteasomal degradation	622:644	proteasomal degradation of the variant protein	622:667	We herein provide the evidence that this genetic polymorphism has an effect on the N-linked glycosylation of ABCC11, intracellular sorting, and proteasomal degradation of the variant protein.
19383836	7	13	theme	axillary	1306:1313	arg1	osmidrosis					1315:1324	axillary osmidrosis	1306:1324	axillary osmidrosis	1306:1324	For rapid genetic diagnosis of axillary osmidrosis and potential risk of breast cancer, we developed specific primers for the SmartAmp method that enabled us to clinically genotype the ABCC11 gene within 30 min.
19383836	4	14	theme	intracellular	595:607	arg1	sorting					609:615	intracellular sorting	595:615	intracellular sorting	595:615	We herein provide the evidence that this genetic polymorphism has an effect on the N-linked glycosylation of ABCC11, intracellular sorting, and proteasomal degradation of the variant protein.
19383836	6	15	from	protein	1083:1089	arg1	reticulum					1110:1118	the endoplasmic reticulum	1094:1118	the endoplasmic reticulum	1094:1118	This SNP variant lacking N-linked glycosylation is recognized as a misfolded protein in the endoplasmic reticulum and readily undergoes ubiquitination and proteasomal degradation, which determines the dry type of earwax as a mendelian trait with a recessive phenotype.
19383836	5	16	theme	secretory	879:887	arg1	cells					889:893	secretory cells	879:893	secretory cells in the cerumen gland	879:914	Immunohistochemical studies with cerumen gland-containing tissue specimens revealed that the ABCC11 WT protein was localized in intracellular granules and large vacuoles, as well as at the luminal membrane of secretory cells in the cerumen gland, whereas granular or vacuolar localization was not detected for the SNP (Arg180) variant.
19383836	5	17	from	gland	910:914	arg1	membrane					867:874	the luminal membrane	855:874	the luminal membrane of secretory cells in the cerumen gland	855:914	Immunohistochemical studies with cerumen gland-containing tissue specimens revealed that the ABCC11 WT protein was localized in intracellular granules and large vacuoles, as well as at the luminal membrane of secretory cells in the cerumen gland, whereas granular or vacuolar localization was not detected for the SNP (Arg180) variant.
19383836	2	18	theme	earwax	297:302	arg1	type					289:292	the wet type	281:292	the wet type of earwax	281:302	The G/G and G/A genotypes correspond to the wet type of earwax, whereas A/A corresponds to the dry type.
19383836	5	19	theme	large	825:829	arg1	vacuoles					831:838	large vacuoles	825:838	large vacuoles	825:838	Immunohistochemical studies with cerumen gland-containing tissue specimens revealed that the ABCC11 WT protein was localized in intracellular granules and large vacuoles, as well as at the luminal membrane of secretory cells in the cerumen gland, whereas granular or vacuolar localization was not detected for the SNP (Arg180) variant.
19383836	5	20	theme	Immunohistochemical	670:688	arg1	studies					690:696	Immunohistochemical studies	670:696	Immunohistochemical studies with cerumen gland-containing tissue specimens	670:743	Immunohistochemical studies with cerumen gland-containing tissue specimens revealed that the ABCC11 WT protein was localized in intracellular granules and large vacuoles, as well as at the luminal membrane of secretory cells in the cerumen gland, whereas granular or vacuolar localization was not detected for the SNP (Arg180) variant.
19383836	7	21	theme	ABCC11	1460:1465	arg1	gene					1467:1470	the ABCC11 gene	1456:1470	the ABCC11 gene	1456:1470	For rapid genetic diagnosis of axillary osmidrosis and potential risk of breast cancer, we developed specific primers for the SmartAmp method that enabled us to clinically genotype the ABCC11 gene within 30 min.
19383836	3	22	theme	global	424:429	arg1	waves					441:445	global migratory waves	424:445	global migratory waves of the ancestors of humankind	424:475	Wide ethnic differences exist in the frequencies of those alleles, reflecting global migratory waves of the ancestors of humankind.
19383836	4	23	from	effect	547:552	arg1	degradation					634:644	proteasomal degradation	622:644	proteasomal degradation of the variant protein	622:667	We herein provide the evidence that this genetic polymorphism has an effect on the N-linked glycosylation of ABCC11, intracellular sorting, and proteasomal degradation of the variant protein.
19383836	4	23	from	effect	547:552	arg1	sorting					609:615	intracellular sorting	595:615	intracellular sorting	595:615	We herein provide the evidence that this genetic polymorphism has an effect on the N-linked glycosylation of ABCC11, intracellular sorting, and proteasomal degradation of the variant protein.
19383836	4	23	from	effect	547:552	arg1	glycosylation					570:582	the N-linked glycosylation	557:582	the N-linked glycosylation of ABCC11	557:592	We herein provide the evidence that this genetic polymorphism has an effect on the N-linked glycosylation of ABCC11, intracellular sorting, and proteasomal degradation of the variant protein.
19383836	5	24	theme	gland-containing	711:726	arg1	specimens					735:743	cerumen gland-containing tissue specimens	703:743	cerumen gland-containing tissue specimens	703:743	Immunohistochemical studies with cerumen gland-containing tissue specimens revealed that the ABCC11 WT protein was localized in intracellular granules and large vacuoles, as well as at the luminal membrane of secretory cells in the cerumen gland, whereas granular or vacuolar localization was not detected for the SNP (Arg180) variant.
19383836	7	25	theme	cancer	1355:1360	arg1	osmidrosis					1315:1324	axillary osmidrosis	1306:1324	axillary osmidrosis	1306:1324	For rapid genetic diagnosis of axillary osmidrosis and potential risk of breast cancer, we developed specific primers for the SmartAmp method that enabled us to clinically genotype the ABCC11 gene within 30 min.
19383836	7	25	theme	cancer	1355:1360	arg1	risk					1340:1343	potential risk	1330:1343	potential risk	1330:1343	For rapid genetic diagnosis of axillary osmidrosis and potential risk of breast cancer, we developed specific primers for the SmartAmp method that enabled us to clinically genotype the ABCC11 gene within 30 min.
19383836	3	26	theme	ancestors	454:462	arg1	waves					441:445	global migratory waves	424:445	global migratory waves of the ancestors of humankind	424:475	Wide ethnic differences exist in the frequencies of those alleles, reflecting global migratory waves of the ancestors of humankind.
19383836	4	27	gly	glycosylation	570:582	arg1	ABCC11					587:592	ABCC11	587:592	ABCC11	587:592	We herein provide the evidence that this genetic polymorphism has an effect on the N-linked glycosylation of ABCC11, intracellular sorting, and proteasomal degradation of the variant protein.
19383836	4	27	gly	glycosylation	570:582	arg1	protein					661:667	the variant protein	649:667	the variant protein	649:667	We herein provide the evidence that this genetic polymorphism has an effect on the N-linked glycosylation of ABCC11, intracellular sorting, and proteasomal degradation of the variant protein.
19383836	2	28	theme	dry	336:338	arg1	type					340:343	the dry type	332:343	the dry type	332:343	The G/G and G/A genotypes correspond to the wet type of earwax, whereas A/A corresponds to the dry type.
19383836	1	29	theme	ABCC11	198:203	arg1	gene					205:208	the ABCC11 gene	194:208	the ABCC11 gene	194:208	One single-nucleotide polymorphism (SNP), 538G>A (Gly180Arg), in the ABCC11 gene determines the type of earwax.
19383836	7	30	theme	SmartAmp	1401:1408	arg1	method					1410:1415	the SmartAmp method	1397:1415	the SmartAmp method	1397:1415	For rapid genetic diagnosis of axillary osmidrosis and potential risk of breast cancer, we developed specific primers for the SmartAmp method that enabled us to clinically genotype the ABCC11 gene within 30 min.
19383836	7	31	theme	osmidrosis	1315:1324	arg1	diagnosis					1293:1301	rapid genetic diagnosis	1279:1301	rapid genetic diagnosis of axillary osmidrosis and potential risk of breast cancer	1279:1360	For rapid genetic diagnosis of axillary osmidrosis and potential risk of breast cancer, we developed specific primers for the SmartAmp method that enabled us to clinically genotype the ABCC11 gene within 30 min.
19383836	2	32	theme	wet	285:287	arg1	type					289:292	the wet type	281:292	the wet type of earwax	281:302	The G/G and G/A genotypes correspond to the wet type of earwax, whereas A/A corresponds to the dry type.
19383836	5	33	theme	tissue	728:733	arg1	specimens					735:743	cerumen gland-containing tissue specimens	703:743	cerumen gland-containing tissue specimens	703:743	Immunohistochemical studies with cerumen gland-containing tissue specimens revealed that the ABCC11 WT protein was localized in intracellular granules and large vacuoles, as well as at the luminal membrane of secretory cells in the cerumen gland, whereas granular or vacuolar localization was not detected for the SNP (Arg180) variant.
19383836	0	34	theme	human	72:76	arg1	gene					101:104	the human ABC transporter ABCC11 gene	68:104	the human ABC transporter ABCC11 gene	68:104	Earwax, osmidrosis, and breast cancer: why does one SNP (538G>A) in the human ABC transporter ABCC11 gene determine earwax type?
19383836	6	35	theme	N-linked	1031:1038	arg1	glycosylation					1040:1052	N-linked glycosylation	1031:1052	N-linked glycosylation	1031:1052	This SNP variant lacking N-linked glycosylation is recognized as a misfolded protein in the endoplasmic reticulum and readily undergoes ubiquitination and proteasomal degradation, which determines the dry type of earwax as a mendelian trait with a recessive phenotype.
19383836	3	36	theme	ethnic	351:356	arg1	differences					358:368	Wide ethnic differences	346:368	Wide ethnic differences	346:368	Wide ethnic differences exist in the frequencies of those alleles, reflecting global migratory waves of the ancestors of humankind.
19383836	6	37	theme	misfolded	1073:1081	arg1	protein					1083:1089	a misfolded protein	1071:1089	a misfolded protein in the endoplasmic reticulum	1071:1118	This SNP variant lacking N-linked glycosylation is recognized as a misfolded protein in the endoplasmic reticulum and readily undergoes ubiquitination and proteasomal degradation, which determines the dry type of earwax as a mendelian trait with a recessive phenotype.
19383836	6	37	theme	misfolded	1073:1081	arg1	degradation					1173:1183	proteasomal degradation	1161:1183	proteasomal degradation	1161:1183	This SNP variant lacking N-linked glycosylation is recognized as a misfolded protein in the endoplasmic reticulum and readily undergoes ubiquitination and proteasomal degradation, which determines the dry type of earwax as a mendelian trait with a recessive phenotype.
19383836	6	37	theme	misfolded	1073:1081	arg1	ubiquitination					1142:1155	ubiquitination	1142:1155	ubiquitination	1142:1155	This SNP variant lacking N-linked glycosylation is recognized as a misfolded protein in the endoplasmic reticulum and readily undergoes ubiquitination and proteasomal degradation, which determines the dry type of earwax as a mendelian trait with a recessive phenotype.
19383836	6	37	theme	misfolded	1073:1081	arg1	variant					1015:1021	This SNP variant	1006:1021	This SNP variant lacking N-linked glycosylation	1006:1052	This SNP variant lacking N-linked glycosylation is recognized as a misfolded protein in the endoplasmic reticulum and readily undergoes ubiquitination and proteasomal degradation, which determines the dry type of earwax as a mendelian trait with a recessive phenotype.
19383836	6	38	theme	mendelian	1231:1239	arg1	type					1211:1214	the dry type	1203:1214	the dry type of earwax	1203:1224	This SNP variant lacking N-linked glycosylation is recognized as a misfolded protein in the endoplasmic reticulum and readily undergoes ubiquitination and proteasomal degradation, which determines the dry type of earwax as a mendelian trait with a recessive phenotype.
19383836	6	38	theme	mendelian	1231:1239	arg1	trait					1241:1245	a mendelian trait	1229:1245	a mendelian trait with a recessive phenotype	1229:1272	This SNP variant lacking N-linked glycosylation is recognized as a misfolded protein in the endoplasmic reticulum and readily undergoes ubiquitination and proteasomal degradation, which determines the dry type of earwax as a mendelian trait with a recessive phenotype.
19383836	0	39	from	SNP	52:54	arg1	gene					101:104	the human ABC transporter ABCC11 gene	68:104	the human ABC transporter ABCC11 gene	68:104	Earwax, osmidrosis, and breast cancer: why does one SNP (538G>A) in the human ABC transporter ABCC11 gene determine earwax type?
19383836	4	40	link	N-linked	561:568	arg1	glycosylation					570:582	the N-linked glycosylation	557:582	the N-linked glycosylation of ABCC11	557:592	We herein provide the evidence that this genetic polymorphism has an effect on the N-linked glycosylation of ABCC11, intracellular sorting, and proteasomal degradation of the variant protein.
19383836	5	41	theme	intracellular	798:810	arg1	granules					812:819	intracellular granules	798:819	intracellular granules	798:819	Immunohistochemical studies with cerumen gland-containing tissue specimens revealed that the ABCC11 WT protein was localized in intracellular granules and large vacuoles, as well as at the luminal membrane of secretory cells in the cerumen gland, whereas granular or vacuolar localization was not detected for the SNP (Arg180) variant.
19383836	0	42	theme	breast	24:29	arg1	cancer					31:36	breast cancer	24:36	breast cancer	24:36	Earwax, osmidrosis, and breast cancer: why does one SNP (538G>A) in the human ABC transporter ABCC11 gene determine earwax type?
19383836	0	43	theme	transporter	82:92	arg1	gene					101:104	the human ABC transporter ABCC11 gene	68:104	the human ABC transporter ABCC11 gene	68:104	Earwax, osmidrosis, and breast cancer: why does one SNP (538G>A) in the human ABC transporter ABCC11 gene determine earwax type?
19383836	4	44	contain	has	540:542	arg1	polymorphism					527:538	this genetic polymorphism	514:538	this genetic polymorphism	514:538	We herein provide the evidence that this genetic polymorphism has an effect on the N-linked glycosylation of ABCC11, intracellular sorting, and proteasomal degradation of the variant protein.
19383836	4	44	contain	has	540:542	arg2	effect					547:552	an effect	544:552	an effect on the N-linked glycosylation of ABCC11, intracellular sorting, and proteasomal degradation of the variant protein	544:667	We herein provide the evidence that this genetic polymorphism has an effect on the N-linked glycosylation of ABCC11, intracellular sorting, and proteasomal degradation of the variant protein.
19383836	7	45	theme	rapid	1279:1283	arg1	diagnosis					1293:1301	rapid genetic diagnosis	1279:1301	rapid genetic diagnosis of axillary osmidrosis and potential risk of breast cancer	1279:1360	For rapid genetic diagnosis of axillary osmidrosis and potential risk of breast cancer, we developed specific primers for the SmartAmp method that enabled us to clinically genotype the ABCC11 gene within 30 min.
19383836	1	46	theme	single-nucleotide	133:149	arg1	SNP					165:167	SNP	165:167	SNP	165:167	One single-nucleotide polymorphism (SNP), 538G>A (Gly180Arg), in the ABCC11 gene determines the type of earwax.
19383836	1	46	theme	single-nucleotide	133:149	arg1	538G>A					171:176	538G>A	171:176	538G>A (Gly180Arg)	171:188	One single-nucleotide polymorphism (SNP), 538G>A (Gly180Arg), in the ABCC11 gene determines the type of earwax.
19383836	1	46	theme	single-nucleotide	133:149	arg1	polymorphism					151:162	One single-nucleotide polymorphism	129:162	One single-nucleotide polymorphism (SNP)	129:168	One single-nucleotide polymorphism (SNP), 538G>A (Gly180Arg), in the ABCC11 gene determines the type of earwax.
19383836	5	47	theme	ABCC11	763:768	arg1	protein					773:779	the ABCC11 WT protein	759:779	the ABCC11 WT protein	759:779	Immunohistochemical studies with cerumen gland-containing tissue specimens revealed that the ABCC11 WT protein was localized in intracellular granules and large vacuoles, as well as at the luminal membrane of secretory cells in the cerumen gland, whereas granular or vacuolar localization was not detected for the SNP (Arg180) variant.
19383836	0	48	theme	ABC	78:80	arg1	gene					101:104	the human ABC transporter ABCC11 gene	68:104	the human ABC transporter ABCC11 gene	68:104	Earwax, osmidrosis, and breast cancer: why does one SNP (538G>A) in the human ABC transporter ABCC11 gene determine earwax type?
19383836	5	49	with	studies	690:696	arg1	specimens					735:743	cerumen gland-containing tissue specimens	703:743	cerumen gland-containing tissue specimens	703:743	Immunohistochemical studies with cerumen gland-containing tissue specimens revealed that the ABCC11 WT protein was localized in intracellular granules and large vacuoles, as well as at the luminal membrane of secretory cells in the cerumen gland, whereas granular or vacuolar localization was not detected for the SNP (Arg180) variant.
19383836	3	50	theme	Wide	346:349	arg1	differences					358:368	Wide ethnic differences	346:368	Wide ethnic differences	346:368	Wide ethnic differences exist in the frequencies of those alleles, reflecting global migratory waves of the ancestors of humankind.
19383836	6	51	theme	earwax	1219:1224	arg1	type					1211:1214	the dry type	1203:1214	the dry type of earwax	1203:1224	This SNP variant lacking N-linked glycosylation is recognized as a misfolded protein in the endoplasmic reticulum and readily undergoes ubiquitination and proteasomal degradation, which determines the dry type of earwax as a mendelian trait with a recessive phenotype.
19383836	6	51	theme	earwax	1219:1224	arg1	trait					1241:1245	a mendelian trait	1229:1245	a mendelian trait with a recessive phenotype	1229:1272	This SNP variant lacking N-linked glycosylation is recognized as a misfolded protein in the endoplasmic reticulum and readily undergoes ubiquitination and proteasomal degradation, which determines the dry type of earwax as a mendelian trait with a recessive phenotype.
19383836	5	52	located	localized	785:793	arg1	granules					812:819	intracellular granules	798:819	intracellular granules	798:819	Immunohistochemical studies with cerumen gland-containing tissue specimens revealed that the ABCC11 WT protein was localized in intracellular granules and large vacuoles, as well as at the luminal membrane of secretory cells in the cerumen gland, whereas granular or vacuolar localization was not detected for the SNP (Arg180) variant.
19383836	5	52	located	localized	785:793	arg2	protein					773:779	the ABCC11 WT protein	759:779	the ABCC11 WT protein	759:779	Immunohistochemical studies with cerumen gland-containing tissue specimens revealed that the ABCC11 WT protein was localized in intracellular granules and large vacuoles, as well as at the luminal membrane of secretory cells in the cerumen gland, whereas granular or vacuolar localization was not detected for the SNP (Arg180) variant.
19383836	3	53	theme	humankind	467:475	arg1	ancestors					454:462	the ancestors	450:462	the ancestors of humankind	450:475	Wide ethnic differences exist in the frequencies of those alleles, reflecting global migratory waves of the ancestors of humankind.
19383836	7	54	theme	breast	1348:1353	arg1	cancer					1355:1360	breast cancer	1348:1360	breast cancer	1348:1360	For rapid genetic diagnosis of axillary osmidrosis and potential risk of breast cancer, we developed specific primers for the SmartAmp method that enabled us to clinically genotype the ABCC11 gene within 30 min.
19383836	2	55	theme	G/A	253:255	arg1	genotypes					257:265	The G/G and G/A genotypes	241:265	The G/G and G/A genotypes	241:265	The G/G and G/A genotypes correspond to the wet type of earwax, whereas A/A corresponds to the dry type.
19383836	5	56	theme	cerumen	703:709	arg1	specimens					735:743	cerumen gland-containing tissue specimens	703:743	cerumen gland-containing tissue specimens	703:743	Immunohistochemical studies with cerumen gland-containing tissue specimens revealed that the ABCC11 WT protein was localized in intracellular granules and large vacuoles, as well as at the luminal membrane of secretory cells in the cerumen gland, whereas granular or vacuolar localization was not detected for the SNP (Arg180) variant.
19383836	1	57	theme	earwax	233:238	arg1	type					225:228	the type	221:228	the type of earwax	221:238	One single-nucleotide polymorphism (SNP), 538G>A (Gly180Arg), in the ABCC11 gene determines the type of earwax.
19383836	0	58	theme	ABCC11	94:99	arg1	gene					101:104	the human ABC transporter ABCC11 gene	68:104	the human ABC transporter ABCC11 gene	68:104	Earwax, osmidrosis, and breast cancer: why does one SNP (538G>A) in the human ABC transporter ABCC11 gene determine earwax type?
19383836	5	59	theme	vacuolar	937:944	arg1	localization					946:957	granular or vacuolar localization	925:957	granular or vacuolar localization	925:957	Immunohistochemical studies with cerumen gland-containing tissue specimens revealed that the ABCC11 WT protein was localized in intracellular granules and large vacuoles, as well as at the luminal membrane of secretory cells in the cerumen gland, whereas granular or vacuolar localization was not detected for the SNP (Arg180) variant.
19383836	6	60	theme	proteasomal	1161:1171	arg1	protein					1083:1089	a misfolded protein	1071:1089	a misfolded protein in the endoplasmic reticulum	1071:1118	This SNP variant lacking N-linked glycosylation is recognized as a misfolded protein in the endoplasmic reticulum and readily undergoes ubiquitination and proteasomal degradation, which determines the dry type of earwax as a mendelian trait with a recessive phenotype.
19383836	6	60	theme	proteasomal	1161:1171	arg1	degradation					1173:1183	proteasomal degradation	1161:1183	proteasomal degradation	1161:1183	This SNP variant lacking N-linked glycosylation is recognized as a misfolded protein in the endoplasmic reticulum and readily undergoes ubiquitination and proteasomal degradation, which determines the dry type of earwax as a mendelian trait with a recessive phenotype.
19383836	6	60	theme	proteasomal	1161:1171	arg1	ubiquitination					1142:1155	ubiquitination	1142:1155	ubiquitination	1142:1155	This SNP variant lacking N-linked glycosylation is recognized as a misfolded protein in the endoplasmic reticulum and readily undergoes ubiquitination and proteasomal degradation, which determines the dry type of earwax as a mendelian trait with a recessive phenotype.
19383836	6	60	theme	proteasomal	1161:1171	arg1	variant					1015:1021	This SNP variant	1006:1021	This SNP variant lacking N-linked glycosylation	1006:1052	This SNP variant lacking N-linked glycosylation is recognized as a misfolded protein in the endoplasmic reticulum and readily undergoes ubiquitination and proteasomal degradation, which determines the dry type of earwax as a mendelian trait with a recessive phenotype.
19383836	1	61	from	polymorphism	151:162	arg1	gene					205:208	the ABCC11 gene	194:208	the ABCC11 gene	194:208	One single-nucleotide polymorphism (SNP), 538G>A (Gly180Arg), in the ABCC11 gene determines the type of earwax.
19383836	6	62	theme	SNP	1011:1013	arg1	protein					1083:1089	a misfolded protein	1071:1089	a misfolded protein in the endoplasmic reticulum	1071:1118	This SNP variant lacking N-linked glycosylation is recognized as a misfolded protein in the endoplasmic reticulum and readily undergoes ubiquitination and proteasomal degradation, which determines the dry type of earwax as a mendelian trait with a recessive phenotype.
19383836	6	62	theme	SNP	1011:1013	arg1	degradation					1173:1183	proteasomal degradation	1161:1183	proteasomal degradation	1161:1183	This SNP variant lacking N-linked glycosylation is recognized as a misfolded protein in the endoplasmic reticulum and readily undergoes ubiquitination and proteasomal degradation, which determines the dry type of earwax as a mendelian trait with a recessive phenotype.
19383836	6	62	theme	SNP	1011:1013	arg1	ubiquitination					1142:1155	ubiquitination	1142:1155	ubiquitination	1142:1155	This SNP variant lacking N-linked glycosylation is recognized as a misfolded protein in the endoplasmic reticulum and readily undergoes ubiquitination and proteasomal degradation, which determines the dry type of earwax as a mendelian trait with a recessive phenotype.
19383836	6	62	theme	SNP	1011:1013	arg1	variant					1015:1021	This SNP variant	1006:1021	This SNP variant lacking N-linked glycosylation	1006:1052	This SNP variant lacking N-linked glycosylation is recognized as a misfolded protein in the endoplasmic reticulum and readily undergoes ubiquitination and proteasomal degradation, which determines the dry type of earwax as a mendelian trait with a recessive phenotype.
19383836	7	63	theme	risk	1340:1343	arg1	diagnosis					1293:1301	rapid genetic diagnosis	1279:1301	rapid genetic diagnosis of axillary osmidrosis and potential risk of breast cancer	1279:1360	For rapid genetic diagnosis of axillary osmidrosis and potential risk of breast cancer, we developed specific primers for the SmartAmp method that enabled us to clinically genotype the ABCC11 gene within 30 min.
19383836	0	64	theme	earwax	116:121	arg1	type					123:126	earwax type	116:126	earwax type	116:126	Earwax, osmidrosis, and breast cancer: why does one SNP (538G>A) in the human ABC transporter ABCC11 gene determine earwax type?
19383836	6	65	theme	endoplasmic	1098:1108	arg1	reticulum					1110:1118	the endoplasmic reticulum	1094:1118	the endoplasmic reticulum	1094:1118	This SNP variant lacking N-linked glycosylation is recognized as a misfolded protein in the endoplasmic reticulum and readily undergoes ubiquitination and proteasomal degradation, which determines the dry type of earwax as a mendelian trait with a recessive phenotype.
19383836	5	66	theme	Arg180	989:994	arg1	variant					997:1003	the SNP (Arg180) variant	980:1003	the SNP (Arg180) variant	980:1003	Immunohistochemical studies with cerumen gland-containing tissue specimens revealed that the ABCC11 WT protein was localized in intracellular granules and large vacuoles, as well as at the luminal membrane of secretory cells in the cerumen gland, whereas granular or vacuolar localization was not detected for the SNP (Arg180) variant.
19383836	7	67	theme	genetic	1285:1291	arg1	diagnosis					1293:1301	rapid genetic diagnosis	1279:1301	rapid genetic diagnosis of axillary osmidrosis and potential risk of breast cancer	1279:1360	For rapid genetic diagnosis of axillary osmidrosis and potential risk of breast cancer, we developed specific primers for the SmartAmp method that enabled us to clinically genotype the ABCC11 gene within 30 min.
19383836	2	68	theme	G/G	245:247	arg1	genotypes					257:265	The G/G and G/A genotypes	241:265	The G/G and G/A genotypes	241:265	The G/G and G/A genotypes correspond to the wet type of earwax, whereas A/A corresponds to the dry type.
19383836	4	69	theme	protein	661:667	arg1	degradation					634:644	proteasomal degradation	622:644	proteasomal degradation of the variant protein	622:667	We herein provide the evidence that this genetic polymorphism has an effect on the N-linked glycosylation of ABCC11, intracellular sorting, and proteasomal degradation of the variant protein.
19383836	4	69	theme	protein	661:667	arg1	sorting					609:615	intracellular sorting	595:615	intracellular sorting	595:615	We herein provide the evidence that this genetic polymorphism has an effect on the N-linked glycosylation of ABCC11, intracellular sorting, and proteasomal degradation of the variant protein.
19383836	4	69	theme	protein	661:667	arg1	glycosylation					570:582	the N-linked glycosylation	557:582	the N-linked glycosylation of ABCC11	557:592	We herein provide the evidence that this genetic polymorphism has an effect on the N-linked glycosylation of ABCC11, intracellular sorting, and proteasomal degradation of the variant protein.
19383836	4	70	theme	variant	653:659	arg1	protein					661:667	the variant protein	649:667	the variant protein	649:667	We herein provide the evidence that this genetic polymorphism has an effect on the N-linked glycosylation of ABCC11, intracellular sorting, and proteasomal degradation of the variant protein.
19383836	6	71	with	trait	1241:1245	arg1	phenotype					1264:1272	a recessive phenotype	1252:1272	a recessive phenotype	1252:1272	This SNP variant lacking N-linked glycosylation is recognized as a misfolded protein in the endoplasmic reticulum and readily undergoes ubiquitination and proteasomal degradation, which determines the dry type of earwax as a mendelian trait with a recessive phenotype.
19383836	5	72	theme	WT	770:771	arg1	protein					773:779	the ABCC11 WT protein	759:779	the ABCC11 WT protein	759:779	Immunohistochemical studies with cerumen gland-containing tissue specimens revealed that the ABCC11 WT protein was localized in intracellular granules and large vacuoles, as well as at the luminal membrane of secretory cells in the cerumen gland, whereas granular or vacuolar localization was not detected for the SNP (Arg180) variant.
19383836	5	73	theme	cerumen	902:908	arg1	gland					910:914	the cerumen gland	898:914	the cerumen gland	898:914	Immunohistochemical studies with cerumen gland-containing tissue specimens revealed that the ABCC11 WT protein was localized in intracellular granules and large vacuoles, as well as at the luminal membrane of secretory cells in the cerumen gland, whereas granular or vacuolar localization was not detected for the SNP (Arg180) variant.
19383836	4	74	theme	genetic	519:525	arg1	polymorphism					527:538	this genetic polymorphism	514:538	this genetic polymorphism	514:538	We herein provide the evidence that this genetic polymorphism has an effect on the N-linked glycosylation of ABCC11, intracellular sorting, and proteasomal degradation of the variant protein.
19383836	3	75	theme	alleles	404:410	arg1	frequencies					383:393	the frequencies	379:393	the frequencies of those alleles	379:410	Wide ethnic differences exist in the frequencies of those alleles, reflecting global migratory waves of the ancestors of humankind.
19383836	4	76	theme	N-linked	561:568	arg1	glycosylation					570:582	the N-linked glycosylation	557:582	the N-linked glycosylation of ABCC11	557:592	We herein provide the evidence that this genetic polymorphism has an effect on the N-linked glycosylation of ABCC11, intracellular sorting, and proteasomal degradation of the variant protein.
19383836	6	77	theme	recessive	1254:1262	arg1	phenotype					1264:1272	a recessive phenotype	1252:1272	a recessive phenotype	1252:1272	This SNP variant lacking N-linked glycosylation is recognized as a misfolded protein in the endoplasmic reticulum and readily undergoes ubiquitination and proteasomal degradation, which determines the dry type of earwax as a mendelian trait with a recessive phenotype.
15066430	2	0	theme	extracellular	586:598	arg1	proteins					600:607	extracellular proteins	586:607	extracellular proteins	586:607	Due to its wide distribution in human tissues, CPM is believed to play important roles in the control of peptide hormone and growth factor activity at the cell surface, and in the membrane-localized degradation of extracellular proteins.
15066430	6	1	theme	substrate	1514:1522	arg1	-Met-enkephalin					1530:1544	the natural substrate Arg(6)-Met-enkephalin	1502:1544	the natural substrate Arg(6)-Met-enkephalin	1502:1544	Modelling of the C-terminal part of the natural substrate Arg(6)-Met-enkephalin into the active site shows that the S1' pocket of CPM is particularly well designed to accommodate P1'-Arg residues, in agreement with the preference of CPM for cleaving C-terminal Arg.
15066430	1	2	theme	"	268:268	arg1	metallo-carboxypeptidases					270:294	"regulatory" metallo-carboxypeptidases	257:294	"regulatory" metallo-carboxypeptidases	257:294	Carboxypeptidase M (CPM), an extracellular glycosylphosphatidyl-inositol(GPI)-anchored membrane glycoprotein belonging to the CPN/E subfamily of "regulatory" metallo-carboxypeptidases, specifically removes C-terminal basic residues from peptides and proteins.
15066430	4	3	attach	attached	1151:1158	arg2	membrane-anchor					1111:1125	the GPI membrane-anchor	1103:1125	the GPI membrane-anchor	1103:1125	The structure analysis reveals that CPM consists of a 295 residue N-terminal catalytic domain similar to that of duck CPD-2 (but only distantly related to CPA/B), an adjacent 86 residue beta-sandwich C-terminal domain characteristic of the CPN/E family but more conically shaped than the equivalent domain in CPD-2, and a unique, partially disordered 25 residue C-terminal extension to which the GPI membrane-anchor is post-translationally attached.
15066430	4	3	attach	attached	1151:1158	arg1	extension					1084:1092	a unique, partially disordered 25 residue C-terminal extension	1031:1092	a unique, partially disordered 25 residue C-terminal extension to which the GPI membrane-anchor is post-translationally attached	1031:1158	The structure analysis reveals that CPM consists of a 295 residue N-terminal catalytic domain similar to that of duck CPD-2 (but only distantly related to CPA/B), an adjacent 86 residue beta-sandwich C-terminal domain characteristic of the CPN/E family but more conically shaped than the equivalent domain in CPD-2, and a unique, partially disordered 25 residue C-terminal extension to which the GPI membrane-anchor is post-translationally attached.
15066430	4	4	theme	equivalent	999:1008	arg1	domain					1010:1015	the equivalent domain	995:1015	the equivalent domain in CPD-2	995:1024	The structure analysis reveals that CPM consists of a 295 residue N-terminal catalytic domain similar to that of duck CPD-2 (but only distantly related to CPA/B), an adjacent 86 residue beta-sandwich C-terminal domain characteristic of the CPN/E family but more conically shaped than the equivalent domain in CPD-2, and a unique, partially disordered 25 residue C-terminal extension to which the GPI membrane-anchor is post-translationally attached.
15066430	4	5	theme	GPI	1107:1109	arg1	membrane-anchor					1111:1125	the GPI membrane-anchor	1103:1125	the GPI membrane-anchor	1103:1125	The structure analysis reveals that CPM consists of a 295 residue N-terminal catalytic domain similar to that of duck CPD-2 (but only distantly related to CPA/B), an adjacent 86 residue beta-sandwich C-terminal domain characteristic of the CPN/E family but more conically shaped than the equivalent domain in CPD-2, and a unique, partially disordered 25 residue C-terminal extension to which the GPI membrane-anchor is post-translationally attached.
15066430	1	6	gly	glycoprotein	208:219	arg1	glycoprotein					208:219	an extracellular glycosylphosphatidyl-inositol(GPI)-anchored membrane glycoprotein	138:219	an extracellular glycosylphosphatidyl-inositol(GPI)-anchored membrane glycoprotein belonging to the CPN/E subfamily of "regulatory" metallo-carboxypeptidases	138:294	Carboxypeptidase M (CPM), an extracellular glycosylphosphatidyl-inositol(GPI)-anchored membrane glycoprotein belonging to the CPN/E subfamily of "regulatory" metallo-carboxypeptidases, specifically removes C-terminal basic residues from peptides and proteins.
15066430	1	6	gly	glycoprotein	208:219	arg1	M					129:129	Carboxypeptidase M	112:129	Carboxypeptidase M (CPM)	112:135	Carboxypeptidase M (CPM), an extracellular glycosylphosphatidyl-inositol(GPI)-anchored membrane glycoprotein belonging to the CPN/E subfamily of "regulatory" metallo-carboxypeptidases, specifically removes C-terminal basic residues from peptides and proteins.
15066430	6	7	theme	part	1494:1497	arg1	Modelling					1466:1474	Modelling	1466:1474	Modelling of the C-terminal part of the natural substrate Arg(6)-Met-enkephalin into the active site	1466:1565	Modelling of the C-terminal part of the natural substrate Arg(6)-Met-enkephalin into the active site shows that the S1' pocket of CPM is particularly well designed to accommodate P1'-Arg residues, in agreement with the preference of CPM for cleaving C-terminal Arg.
15066430	4	8	theme	residue	889:895	arg1	domain					922:927	an adjacent 86 residue beta-sandwich C-terminal domain	874:927	an adjacent 86 residue beta-sandwich C-terminal domain characteristic of the CPN/E family but more conically shaped than the equivalent domain in CPD-2	874:1024	The structure analysis reveals that CPM consists of a 295 residue N-terminal catalytic domain similar to that of duck CPD-2 (but only distantly related to CPA/B), an adjacent 86 residue beta-sandwich C-terminal domain characteristic of the CPN/E family but more conically shaped than the equivalent domain in CPD-2, and a unique, partially disordered 25 residue C-terminal extension to which the GPI membrane-anchor is post-translationally attached.
15066430	4	9	theme	residue	1065:1071	arg1	extension					1084:1092	a unique, partially disordered 25 residue C-terminal extension	1031:1092	a unique, partially disordered 25 residue C-terminal extension to which the GPI membrane-anchor is post-translationally attached	1031:1158	The structure analysis reveals that CPM consists of a 295 residue N-terminal catalytic domain similar to that of duck CPD-2 (but only distantly related to CPA/B), an adjacent 86 residue beta-sandwich C-terminal domain characteristic of the CPN/E family but more conically shaped than the equivalent domain in CPD-2, and a unique, partially disordered 25 residue C-terminal extension to which the GPI membrane-anchor is post-translationally attached.
15066430	1	10	theme	membrane	199:206	arg1	glycoprotein					208:219	an extracellular glycosylphosphatidyl-inositol(GPI)-anchored membrane glycoprotein	138:219	an extracellular glycosylphosphatidyl-inositol(GPI)-anchored membrane glycoprotein belonging to the CPN/E subfamily of "regulatory" metallo-carboxypeptidases	138:294	Carboxypeptidase M (CPM), an extracellular glycosylphosphatidyl-inositol(GPI)-anchored membrane glycoprotein belonging to the CPN/E subfamily of "regulatory" metallo-carboxypeptidases, specifically removes C-terminal basic residues from peptides and proteins.
15066430	1	10	theme	membrane	199:206	arg1	M					129:129	Carboxypeptidase M	112:129	Carboxypeptidase M (CPM)	112:135	Carboxypeptidase M (CPM), an extracellular glycosylphosphatidyl-inositol(GPI)-anchored membrane glycoprotein belonging to the CPN/E subfamily of "regulatory" metallo-carboxypeptidases, specifically removes C-terminal basic residues from peptides and proteins.
15066430	4	11	theme	C-terminal	911:920	arg1	domain					922:927	an adjacent 86 residue beta-sandwich C-terminal domain	874:927	an adjacent 86 residue beta-sandwich C-terminal domain characteristic of the CPN/E family but more conically shaped than the equivalent domain in CPD-2	874:1024	The structure analysis reveals that CPM consists of a 295 residue N-terminal catalytic domain similar to that of duck CPD-2 (but only distantly related to CPA/B), an adjacent 86 residue beta-sandwich C-terminal domain characteristic of the CPN/E family but more conically shaped than the equivalent domain in CPD-2, and a unique, partially disordered 25 residue C-terminal extension to which the GPI membrane-anchor is post-translationally attached.
15066430	6	12	theme	active	1555:1560	arg1	site					1562:1565	the active site	1551:1565	the active site	1551:1565	Modelling of the C-terminal part of the natural substrate Arg(6)-Met-enkephalin into the active site shows that the S1' pocket of CPM is particularly well designed to accommodate P1'-Arg residues, in agreement with the preference of CPM for cleaving C-terminal Arg.
15066430	4	13	theme	adjacent	877:884	arg1	domain					922:927	an adjacent 86 residue beta-sandwich C-terminal domain	874:927	an adjacent 86 residue beta-sandwich C-terminal domain characteristic of the CPN/E family but more conically shaped than the equivalent domain in CPD-2	874:1024	The structure analysis reveals that CPM consists of a 295 residue N-terminal catalytic domain similar to that of duck CPD-2 (but only distantly related to CPA/B), an adjacent 86 residue beta-sandwich C-terminal domain characteristic of the CPN/E family but more conically shaped than the equivalent domain in CPD-2, and a unique, partially disordered 25 residue C-terminal extension to which the GPI membrane-anchor is post-translationally attached.
15066430	3	14	theme	human	631:635	arg1	CPM					646:648	human GPI-free CPM	631:648	human GPI-free CPM	631:648	We have crystallized human GPI-free CPM, and have determined and refined its 3.0A crystal structure.
15066430	4	15	theme	family	957:962	arg1	characteristic					929:942	characteristic	929:942	characteristic	929:942	The structure analysis reveals that CPM consists of a 295 residue N-terminal catalytic domain similar to that of duck CPD-2 (but only distantly related to CPA/B), an adjacent 86 residue beta-sandwich C-terminal domain characteristic of the CPN/E family but more conically shaped than the equivalent domain in CPD-2, and a unique, partially disordered 25 residue C-terminal extension to which the GPI membrane-anchor is post-translationally attached.
15066430	6	16	theme	CPM	1596:1598	arg1	pocket					1586:1591	the S1' pocket	1578:1591	the S1' pocket of CPM	1578:1598	Modelling of the C-terminal part of the natural substrate Arg(6)-Met-enkephalin into the active site shows that the S1' pocket of CPM is particularly well designed to accommodate P1'-Arg residues, in agreement with the preference of CPM for cleaving C-terminal Arg.
15066430	0	17	theme	membrane-bound	49:62	arg1	enzyme					64:69	a membrane-bound enzyme	47:69	a membrane-bound enzyme that regulates peptide hormone activity	47:109	Crystal structure of human carboxypeptidase M, a membrane-bound enzyme that regulates peptide hormone activity.
15066430	0	17	theme	membrane-bound	49:62	arg1	structure					8:16	Crystal structure	0:16	Crystal structure of human carboxypeptidase M	0:44	Crystal structure of human carboxypeptidase M, a membrane-bound enzyme that regulates peptide hormone activity.
15066430	2	18	theme	hormone	485:491	arg1	activity					511:518	peptide hormone and growth factor activity	477:518	peptide hormone and growth factor activity at the cell surface	477:538	Due to its wide distribution in human tissues, CPM is believed to play important roles in the control of peptide hormone and growth factor activity at the cell surface, and in the membrane-localized degradation of extracellular proteins.
15066430	4	19	from	domain	1010:1015	arg1	CPD-2					1020:1024	CPD-2	1020:1024	CPD-2	1020:1024	The structure analysis reveals that CPM consists of a 295 residue N-terminal catalytic domain similar to that of duck CPD-2 (but only distantly related to CPA/B), an adjacent 86 residue beta-sandwich C-terminal domain characteristic of the CPN/E family but more conically shaped than the equivalent domain in CPD-2, and a unique, partially disordered 25 residue C-terminal extension to which the GPI membrane-anchor is post-translationally attached.
15066430	5	20	theme	small	1450:1454	arg1	peptides					1456:1463	small peptides	1450:1463	small peptides	1450:1463	Through this GPI anchor, and presumably via some positively charged side-chains of the C-terminal domain, the CPM molecule may interact with the membrane in such a way that its active centre will face alongside, i.e. well suited to interact with other membrane-bound protein substrates or small peptides.
15066430	6	21	with	agreement	1666:1674	arg1	preference					1685:1694	the preference	1681:1694	the preference of CPM for cleaving C-terminal Arg	1681:1729	Modelling of the C-terminal part of the natural substrate Arg(6)-Met-enkephalin into the active site shows that the S1' pocket of CPM is particularly well designed to accommodate P1'-Arg residues, in agreement with the preference of CPM for cleaving C-terminal Arg.
15066430	4	22	dep	unique	1033:1038	arg1	disordered					1051:1060	disordered	1051:1060	disordered	1051:1060	The structure analysis reveals that CPM consists of a 295 residue N-terminal catalytic domain similar to that of duck CPD-2 (but only distantly related to CPA/B), an adjacent 86 residue beta-sandwich C-terminal domain characteristic of the CPN/E family but more conically shaped than the equivalent domain in CPD-2, and a unique, partially disordered 25 residue C-terminal extension to which the GPI membrane-anchor is post-translationally attached.
15066430	1	23	theme	extracellular	141:153	arg1	glycoprotein					208:219	an extracellular glycosylphosphatidyl-inositol(GPI)-anchored membrane glycoprotein	138:219	an extracellular glycosylphosphatidyl-inositol(GPI)-anchored membrane glycoprotein belonging to the CPN/E subfamily of "regulatory" metallo-carboxypeptidases	138:294	Carboxypeptidase M (CPM), an extracellular glycosylphosphatidyl-inositol(GPI)-anchored membrane glycoprotein belonging to the CPN/E subfamily of "regulatory" metallo-carboxypeptidases, specifically removes C-terminal basic residues from peptides and proteins.
15066430	1	23	theme	extracellular	141:153	arg1	M					129:129	Carboxypeptidase M	112:129	Carboxypeptidase M (CPM)	112:135	Carboxypeptidase M (CPM), an extracellular glycosylphosphatidyl-inositol(GPI)-anchored membrane glycoprotein belonging to the CPN/E subfamily of "regulatory" metallo-carboxypeptidases, specifically removes C-terminal basic residues from peptides and proteins.
15066430	4	24	theme	characteristic	929:942	arg1	domain					922:927	an adjacent 86 residue beta-sandwich C-terminal domain	874:927	an adjacent 86 residue beta-sandwich C-terminal domain characteristic of the CPN/E family but more conically shaped than the equivalent domain in CPD-2	874:1024	The structure analysis reveals that CPM consists of a 295 residue N-terminal catalytic domain similar to that of duck CPD-2 (but only distantly related to CPA/B), an adjacent 86 residue beta-sandwich C-terminal domain characteristic of the CPN/E family but more conically shaped than the equivalent domain in CPD-2, and a unique, partially disordered 25 residue C-terminal extension to which the GPI membrane-anchor is post-translationally attached.
15066430	5	25	theme	domain	1259:1264	arg1	side-chains					1229:1239	some positively charged side-chains	1205:1239	some positively charged side-chains of the C-terminal domain	1205:1264	Through this GPI anchor, and presumably via some positively charged side-chains of the C-terminal domain, the CPM molecule may interact with the membrane in such a way that its active centre will face alongside, i.e. well suited to interact with other membrane-bound protein substrates or small peptides.
15066430	0	26	theme	peptide	86:92	arg1	activity					102:109	peptide hormone activity	86:109	peptide hormone activity	86:109	Crystal structure of human carboxypeptidase M, a membrane-bound enzyme that regulates peptide hormone activity.
15066430	2	27	theme	activity	511:518	arg1	control					466:472	the control	462:472	the control of peptide hormone and growth factor activity at the cell surface	462:538	Due to its wide distribution in human tissues, CPM is believed to play important roles in the control of peptide hormone and growth factor activity at the cell surface, and in the membrane-localized degradation of extracellular proteins.
15066430	5	28	theme	membrane-bound	1413:1426	arg1	substrates					1436:1445	other membrane-bound protein substrates	1407:1445	other membrane-bound protein substrates	1407:1445	Through this GPI anchor, and presumably via some positively charged side-chains of the C-terminal domain, the CPM molecule may interact with the membrane in such a way that its active centre will face alongside, i.e. well suited to interact with other membrane-bound protein substrates or small peptides.
15066430	4	29	theme	residue	769:775	arg1	domain					798:803	a 295 residue N-terminal catalytic domain	763:803	a 295 residue N-terminal catalytic domain similar to that of duck CPD-2 (but only distantly related to CPA/B)	763:871	The structure analysis reveals that CPM consists of a 295 residue N-terminal catalytic domain similar to that of duck CPD-2 (but only distantly related to CPA/B), an adjacent 86 residue beta-sandwich C-terminal domain characteristic of the CPN/E family but more conically shaped than the equivalent domain in CPD-2, and a unique, partially disordered 25 residue C-terminal extension to which the GPI membrane-anchor is post-translationally attached.
15066430	0	30	theme	M	44:44	arg1	structure					8:16	Crystal structure	0:16	Crystal structure of human carboxypeptidase M	0:44	Crystal structure of human carboxypeptidase M, a membrane-bound enzyme that regulates peptide hormone activity.
15066430	0	30	theme	M	44:44	arg1	enzyme					64:69	a membrane-bound enzyme	47:69	a membrane-bound enzyme that regulates peptide hormone activity	47:109	Crystal structure of human carboxypeptidase M, a membrane-bound enzyme that regulates peptide hormone activity.
15066430	2	31	from	control	466:472	arg1	surface					532:538	the cell surface	523:538	the cell surface	523:538	Due to its wide distribution in human tissues, CPM is believed to play important roles in the control of peptide hormone and growth factor activity at the cell surface, and in the membrane-localized degradation of extracellular proteins.
15066430	2	32	theme	growth	497:502	arg1	factor					504:509	growth factor	497:509	growth factor	497:509	Due to its wide distribution in human tissues, CPM is believed to play important roles in the control of peptide hormone and growth factor activity at the cell surface, and in the membrane-localized degradation of extracellular proteins.
15066430	0	33	theme	Crystal	0:6	arg1	structure					8:16	Crystal structure	0:16	Crystal structure of human carboxypeptidase M	0:44	Crystal structure of human carboxypeptidase M, a membrane-bound enzyme that regulates peptide hormone activity.
15066430	0	33	theme	Crystal	0:6	arg1	enzyme					64:69	a membrane-bound enzyme	47:69	a membrane-bound enzyme that regulates peptide hormone activity	47:109	Crystal structure of human carboxypeptidase M, a membrane-bound enzyme that regulates peptide hormone activity.
15066430	1	34	theme	metallo-carboxypeptidases	270:294	arg1	subfamily					244:252	the CPN/E subfamily	234:252	the CPN/E subfamily of "regulatory" metallo-carboxypeptidases	234:294	Carboxypeptidase M (CPM), an extracellular glycosylphosphatidyl-inositol(GPI)-anchored membrane glycoprotein belonging to the CPN/E subfamily of "regulatory" metallo-carboxypeptidases, specifically removes C-terminal basic residues from peptides and proteins.
15066430	4	35	dep	CPD-2	829:833	arg1	related					855:861	related	855:861	related	855:861	The structure analysis reveals that CPM consists of a 295 residue N-terminal catalytic domain similar to that of duck CPD-2 (but only distantly related to CPA/B), an adjacent 86 residue beta-sandwich C-terminal domain characteristic of the CPN/E family but more conically shaped than the equivalent domain in CPD-2, and a unique, partially disordered 25 residue C-terminal extension to which the GPI membrane-anchor is post-translationally attached.
15066430	5	36	theme	GPI	1174:1176	arg1	anchor					1178:1183	this GPI anchor	1169:1183	this GPI anchor	1169:1183	Through this GPI anchor, and presumably via some positively charged side-chains of the C-terminal domain, the CPM molecule may interact with the membrane in such a way that its active centre will face alongside, i.e. well suited to interact with other membrane-bound protein substrates or small peptides.
15066430	4	37	theme	shaped	983:988	arg1	domain					922:927	an adjacent 86 residue beta-sandwich C-terminal domain	874:927	an adjacent 86 residue beta-sandwich C-terminal domain characteristic of the CPN/E family but more conically shaped than the equivalent domain in CPD-2	874:1024	The structure analysis reveals that CPM consists of a 295 residue N-terminal catalytic domain similar to that of duck CPD-2 (but only distantly related to CPA/B), an adjacent 86 residue beta-sandwich C-terminal domain characteristic of the CPN/E family but more conically shaped than the equivalent domain in CPD-2, and a unique, partially disordered 25 residue C-terminal extension to which the GPI membrane-anchor is post-translationally attached.
15066430	0	38	theme	carboxypeptidase	27:42	arg1	M					44:44	human carboxypeptidase M	21:44	human carboxypeptidase M	21:44	Crystal structure of human carboxypeptidase M, a membrane-bound enzyme that regulates peptide hormone activity.
15066430	1	39	theme	C-terminal	318:327	arg1	residues					335:342	C-terminal basic residues	318:342	C-terminal basic residues from peptides and proteins	318:369	Carboxypeptidase M (CPM), an extracellular glycosylphosphatidyl-inositol(GPI)-anchored membrane glycoprotein belonging to the CPN/E subfamily of "regulatory" metallo-carboxypeptidases, specifically removes C-terminal basic residues from peptides and proteins.
15066430	4	40	theme	duck	824:827	arg1	CPD-2					829:833	duck CPD-2	824:833	duck CPD-2 (but only distantly related to CPA/B)	824:871	The structure analysis reveals that CPM consists of a 295 residue N-terminal catalytic domain similar to that of duck CPD-2 (but only distantly related to CPA/B), an adjacent 86 residue beta-sandwich C-terminal domain characteristic of the CPN/E family but more conically shaped than the equivalent domain in CPD-2, and a unique, partially disordered 25 residue C-terminal extension to which the GPI membrane-anchor is post-translationally attached.
15066430	6	41	theme	CPM	1699:1701	arg1	preference					1685:1694	the preference	1681:1694	the preference of CPM for cleaving C-terminal Arg	1681:1729	Modelling of the C-terminal part of the natural substrate Arg(6)-Met-enkephalin into the active site shows that the S1' pocket of CPM is particularly well designed to accommodate P1'-Arg residues, in agreement with the preference of CPM for cleaving C-terminal Arg.
15066430	4	42	theme	catalytic	788:796	arg1	domain					798:803	a 295 residue N-terminal catalytic domain	763:803	a 295 residue N-terminal catalytic domain similar to that of duck CPD-2 (but only distantly related to CPA/B)	763:871	The structure analysis reveals that CPM consists of a 295 residue N-terminal catalytic domain similar to that of duck CPD-2 (but only distantly related to CPA/B), an adjacent 86 residue beta-sandwich C-terminal domain characteristic of the CPN/E family but more conically shaped than the equivalent domain in CPD-2, and a unique, partially disordered 25 residue C-terminal extension to which the GPI membrane-anchor is post-translationally attached.
15066430	4	43	theme	25	1062:1063	arg1	residue					1065:1071	residue	1065:1071	residue	1065:1071	The structure analysis reveals that CPM consists of a 295 residue N-terminal catalytic domain similar to that of duck CPD-2 (but only distantly related to CPA/B), an adjacent 86 residue beta-sandwich C-terminal domain characteristic of the CPN/E family but more conically shaped than the equivalent domain in CPD-2, and a unique, partially disordered 25 residue C-terminal extension to which the GPI membrane-anchor is post-translationally attached.
15066430	4	44	theme	similar	805:811	arg1	domain					798:803	a 295 residue N-terminal catalytic domain	763:803	a 295 residue N-terminal catalytic domain similar to that of duck CPD-2 (but only distantly related to CPA/B)	763:871	The structure analysis reveals that CPM consists of a 295 residue N-terminal catalytic domain similar to that of duck CPD-2 (but only distantly related to CPA/B), an adjacent 86 residue beta-sandwich C-terminal domain characteristic of the CPN/E family but more conically shaped than the equivalent domain in CPD-2, and a unique, partially disordered 25 residue C-terminal extension to which the GPI membrane-anchor is post-translationally attached.
15066430	2	45	theme	wide	383:386	arg1	distribution					388:399	its wide distribution	379:399	its wide distribution in human tissues	379:416	Due to its wide distribution in human tissues, CPM is believed to play important roles in the control of peptide hormone and growth factor activity at the cell surface, and in the membrane-localized degradation of extracellular proteins.
15066430	5	46	theme	charged	1221:1227	arg1	side-chains					1229:1239	some positively charged side-chains	1205:1239	some positively charged side-chains of the C-terminal domain	1205:1264	Through this GPI anchor, and presumably via some positively charged side-chains of the C-terminal domain, the CPM molecule may interact with the membrane in such a way that its active centre will face alongside, i.e. well suited to interact with other membrane-bound protein substrates or small peptides.
15066430	5	47	theme	active	1338:1343	arg1	centre					1345:1350	its active centre	1334:1350	its active centre	1334:1350	Through this GPI anchor, and presumably via some positively charged side-chains of the C-terminal domain, the CPM molecule may interact with the membrane in such a way that its active centre will face alongside, i.e. well suited to interact with other membrane-bound protein substrates or small peptides.
15066430	2	48	theme	proteins	600:607	arg1	degradation					571:581	the membrane-localized degradation	548:581	the membrane-localized degradation of extracellular proteins	548:607	Due to its wide distribution in human tissues, CPM is believed to play important roles in the control of peptide hormone and growth factor activity at the cell surface, and in the membrane-localized degradation of extracellular proteins.
15066430	4	49	theme	unique	1033:1038	arg1	extension					1084:1092	a unique, partially disordered 25 residue C-terminal extension	1031:1092	a unique, partially disordered 25 residue C-terminal extension to which the GPI membrane-anchor is post-translationally attached	1031:1158	The structure analysis reveals that CPM consists of a 295 residue N-terminal catalytic domain similar to that of duck CPD-2 (but only distantly related to CPA/B), an adjacent 86 residue beta-sandwich C-terminal domain characteristic of the CPN/E family but more conically shaped than the equivalent domain in CPD-2, and a unique, partially disordered 25 residue C-terminal extension to which the GPI membrane-anchor is post-translationally attached.
15066430	3	50	theme	3.0A	687:690	arg1	structure					700:708	its 3.0A crystal structure	683:708	its 3.0A crystal structure	683:708	We have crystallized human GPI-free CPM, and have determined and refined its 3.0A crystal structure.
15066430	1	51	theme	regulatory	258:267	arg1	metallo-carboxypeptidases					270:294	"regulatory" metallo-carboxypeptidases	257:294	"regulatory" metallo-carboxypeptidases	257:294	Carboxypeptidase M (CPM), an extracellular glycosylphosphatidyl-inositol(GPI)-anchored membrane glycoprotein belonging to the CPN/E subfamily of "regulatory" metallo-carboxypeptidases, specifically removes C-terminal basic residues from peptides and proteins.
15066430	5	52	theme	other	1407:1411	arg1	substrates					1436:1445	other membrane-bound protein substrates	1407:1445	other membrane-bound protein substrates	1407:1445	Through this GPI anchor, and presumably via some positively charged side-chains of the C-terminal domain, the CPM molecule may interact with the membrane in such a way that its active centre will face alongside, i.e. well suited to interact with other membrane-bound protein substrates or small peptides.
15066430	6	53	theme	natural	1506:1512	arg1	-Met-enkephalin					1530:1544	the natural substrate Arg(6)-Met-enkephalin	1502:1544	the natural substrate Arg(6)-Met-enkephalin	1502:1544	Modelling of the C-terminal part of the natural substrate Arg(6)-Met-enkephalin into the active site shows that the S1' pocket of CPM is particularly well designed to accommodate P1'-Arg residues, in agreement with the preference of CPM for cleaving C-terminal Arg.
15066430	4	54	theme	C-terminal	1073:1082	arg1	extension					1084:1092	a unique, partially disordered 25 residue C-terminal extension	1031:1092	a unique, partially disordered 25 residue C-terminal extension to which the GPI membrane-anchor is post-translationally attached	1031:1158	The structure analysis reveals that CPM consists of a 295 residue N-terminal catalytic domain similar to that of duck CPD-2 (but only distantly related to CPA/B), an adjacent 86 residue beta-sandwich C-terminal domain characteristic of the CPN/E family but more conically shaped than the equivalent domain in CPD-2, and a unique, partially disordered 25 residue C-terminal extension to which the GPI membrane-anchor is post-translationally attached.
15066430	6	55	theme	C-terminal	1483:1492	arg1	part					1494:1497	the C-terminal part	1479:1497	the C-terminal part of the natural substrate Arg(6)-Met-enkephalin	1479:1544	Modelling of the C-terminal part of the natural substrate Arg(6)-Met-enkephalin into the active site shows that the S1' pocket of CPM is particularly well designed to accommodate P1'-Arg residues, in agreement with the preference of CPM for cleaving C-terminal Arg.
15066430	1	56	theme	-anchored	189:197	arg1	glycoprotein					208:219	an extracellular glycosylphosphatidyl-inositol(GPI)-anchored membrane glycoprotein	138:219	an extracellular glycosylphosphatidyl-inositol(GPI)-anchored membrane glycoprotein belonging to the CPN/E subfamily of "regulatory" metallo-carboxypeptidases	138:294	Carboxypeptidase M (CPM), an extracellular glycosylphosphatidyl-inositol(GPI)-anchored membrane glycoprotein belonging to the CPN/E subfamily of "regulatory" metallo-carboxypeptidases, specifically removes C-terminal basic residues from peptides and proteins.
15066430	1	56	theme	-anchored	189:197	arg1	M					129:129	Carboxypeptidase M	112:129	Carboxypeptidase M (CPM)	112:135	Carboxypeptidase M (CPM), an extracellular glycosylphosphatidyl-inositol(GPI)-anchored membrane glycoprotein belonging to the CPN/E subfamily of "regulatory" metallo-carboxypeptidases, specifically removes C-terminal basic residues from peptides and proteins.
15066430	4	57	theme	86	886:887	arg1	residue					889:895	residue	889:895	residue	889:895	The structure analysis reveals that CPM consists of a 295 residue N-terminal catalytic domain similar to that of duck CPD-2 (but only distantly related to CPA/B), an adjacent 86 residue beta-sandwich C-terminal domain characteristic of the CPN/E family but more conically shaped than the equivalent domain in CPD-2, and a unique, partially disordered 25 residue C-terminal extension to which the GPI membrane-anchor is post-translationally attached.
15066430	6	58	theme	P1'-Arg	1645:1651	arg1	residues					1653:1660	P1'-Arg residues	1645:1660	P1'-Arg residues	1645:1660	Modelling of the C-terminal part of the natural substrate Arg(6)-Met-enkephalin into the active site shows that the S1' pocket of CPM is particularly well designed to accommodate P1'-Arg residues, in agreement with the preference of CPM for cleaving C-terminal Arg.
15066430	2	59	theme	cell	527:530	arg1	surface					532:538	the cell surface	523:538	the cell surface	523:538	Due to its wide distribution in human tissues, CPM is believed to play important roles in the control of peptide hormone and growth factor activity at the cell surface, and in the membrane-localized degradation of extracellular proteins.
15066430	1	60	theme	Carboxypeptidase	112:127	arg1	CPM					132:134	CPM	132:134	CPM	132:134	Carboxypeptidase M (CPM), an extracellular glycosylphosphatidyl-inositol(GPI)-anchored membrane glycoprotein belonging to the CPN/E subfamily of "regulatory" metallo-carboxypeptidases, specifically removes C-terminal basic residues from peptides and proteins.
15066430	1	60	theme	Carboxypeptidase	112:127	arg1	glycoprotein					208:219	an extracellular glycosylphosphatidyl-inositol(GPI)-anchored membrane glycoprotein	138:219	an extracellular glycosylphosphatidyl-inositol(GPI)-anchored membrane glycoprotein belonging to the CPN/E subfamily of "regulatory" metallo-carboxypeptidases	138:294	Carboxypeptidase M (CPM), an extracellular glycosylphosphatidyl-inositol(GPI)-anchored membrane glycoprotein belonging to the CPN/E subfamily of "regulatory" metallo-carboxypeptidases, specifically removes C-terminal basic residues from peptides and proteins.
15066430	1	60	theme	Carboxypeptidase	112:127	arg1	M					129:129	Carboxypeptidase M	112:129	Carboxypeptidase M (CPM)	112:135	Carboxypeptidase M (CPM), an extracellular glycosylphosphatidyl-inositol(GPI)-anchored membrane glycoprotein belonging to the CPN/E subfamily of "regulatory" metallo-carboxypeptidases, specifically removes C-terminal basic residues from peptides and proteins.
15066430	2	61	theme	membrane-localized	552:569	arg1	degradation					571:581	the membrane-localized degradation	548:581	the membrane-localized degradation of extracellular proteins	548:607	Due to its wide distribution in human tissues, CPM is believed to play important roles in the control of peptide hormone and growth factor activity at the cell surface, and in the membrane-localized degradation of extracellular proteins.
15066430	6	62	theme	-Met-enkephalin	1530:1544	arg1	part					1494:1497	the C-terminal part	1479:1497	the C-terminal part of the natural substrate Arg(6)-Met-enkephalin	1479:1544	Modelling of the C-terminal part of the natural substrate Arg(6)-Met-enkephalin into the active site shows that the S1' pocket of CPM is particularly well designed to accommodate P1'-Arg residues, in agreement with the preference of CPM for cleaving C-terminal Arg.
15066430	4	63	theme	structure	715:723	arg1	analysis					725:732	The structure analysis	711:732	The structure analysis	711:732	The structure analysis reveals that CPM consists of a 295 residue N-terminal catalytic domain similar to that of duck CPD-2 (but only distantly related to CPA/B), an adjacent 86 residue beta-sandwich C-terminal domain characteristic of the CPN/E family but more conically shaped than the equivalent domain in CPD-2, and a unique, partially disordered 25 residue C-terminal extension to which the GPI membrane-anchor is post-translationally attached.
15066430	5	64	theme	CPM	1271:1273	arg1	molecule					1275:1282	the CPM molecule	1267:1282	the CPM molecule	1267:1282	Through this GPI anchor, and presumably via some positively charged side-chains of the C-terminal domain, the CPM molecule may interact with the membrane in such a way that its active centre will face alongside, i.e. well suited to interact with other membrane-bound protein substrates or small peptides.
15066430	4	65	theme	CPN/E	951:955	arg1	family					957:962	the CPN/E family	947:962	the CPN/E family	947:962	The structure analysis reveals that CPM consists of a 295 residue N-terminal catalytic domain similar to that of duck CPD-2 (but only distantly related to CPA/B), an adjacent 86 residue beta-sandwich C-terminal domain characteristic of the CPN/E family but more conically shaped than the equivalent domain in CPD-2, and a unique, partially disordered 25 residue C-terminal extension to which the GPI membrane-anchor is post-translationally attached.
15066430	6	66	theme	Arg	1524:1526	arg1	-Met-enkephalin					1530:1544	the natural substrate Arg(6)-Met-enkephalin	1502:1544	the natural substrate Arg(6)-Met-enkephalin	1502:1544	Modelling of the C-terminal part of the natural substrate Arg(6)-Met-enkephalin into the active site shows that the S1' pocket of CPM is particularly well designed to accommodate P1'-Arg residues, in agreement with the preference of CPM for cleaving C-terminal Arg.
15066430	2	67	theme	peptide	477:483	arg1	hormone					485:491	peptide hormone	477:491	peptide hormone	477:491	Due to its wide distribution in human tissues, CPM is believed to play important roles in the control of peptide hormone and growth factor activity at the cell surface, and in the membrane-localized degradation of extracellular proteins.
15066430	5	68	theme	C-terminal	1248:1257	arg1	domain					1259:1264	the C-terminal domain	1244:1264	the C-terminal domain	1244:1264	Through this GPI anchor, and presumably via some positively charged side-chains of the C-terminal domain, the CPM molecule may interact with the membrane in such a way that its active centre will face alongside, i.e. well suited to interact with other membrane-bound protein substrates or small peptides.
15066430	0	69	theme	hormone	94:100	arg1	activity					102:109	peptide hormone activity	86:109	peptide hormone activity	86:109	Crystal structure of human carboxypeptidase M, a membrane-bound enzyme that regulates peptide hormone activity.
15066430	2	70	theme	factor	504:509	arg1	activity					511:518	peptide hormone and growth factor activity	477:518	peptide hormone and growth factor activity at the cell surface	477:538	Due to its wide distribution in human tissues, CPM is believed to play important roles in the control of peptide hormone and growth factor activity at the cell surface, and in the membrane-localized degradation of extracellular proteins.
15066430	5	71	theme	protein	1428:1434	arg1	substrates					1436:1445	other membrane-bound protein substrates	1407:1445	other membrane-bound protein substrates	1407:1445	Through this GPI anchor, and presumably via some positively charged side-chains of the C-terminal domain, the CPM molecule may interact with the membrane in such a way that its active centre will face alongside, i.e. well suited to interact with other membrane-bound protein substrates or small peptides.
15066430	4	72	theme	295	765:767	arg1	residue					769:775	residue	769:775	residue	769:775	The structure analysis reveals that CPM consists of a 295 residue N-terminal catalytic domain similar to that of duck CPD-2 (but only distantly related to CPA/B), an adjacent 86 residue beta-sandwich C-terminal domain characteristic of the CPN/E family but more conically shaped than the equivalent domain in CPD-2, and a unique, partially disordered 25 residue C-terminal extension to which the GPI membrane-anchor is post-translationally attached.
15066430	2	73	theme	human	404:408	arg1	tissues					410:416	human tissues	404:416	human tissues	404:416	Due to its wide distribution in human tissues, CPM is believed to play important roles in the control of peptide hormone and growth factor activity at the cell surface, and in the membrane-localized degradation of extracellular proteins.
15066430	2	74	theme	important	443:451	arg1	roles					453:457	important roles	443:457	important roles	443:457	Due to its wide distribution in human tissues, CPM is believed to play important roles in the control of peptide hormone and growth factor activity at the cell surface, and in the membrane-localized degradation of extracellular proteins.
15066430	0	75	theme	human	21:25	arg1	M					44:44	human carboxypeptidase M	21:44	human carboxypeptidase M	21:44	Crystal structure of human carboxypeptidase M, a membrane-bound enzyme that regulates peptide hormone activity.
15066430	1	76	from	proteins	362:369	arg1	residues					335:342	C-terminal basic residues	318:342	C-terminal basic residues from peptides and proteins	318:369	Carboxypeptidase M (CPM), an extracellular glycosylphosphatidyl-inositol(GPI)-anchored membrane glycoprotein belonging to the CPN/E subfamily of "regulatory" metallo-carboxypeptidases, specifically removes C-terminal basic residues from peptides and proteins.
15066430	6	77	theme	C-terminal	1716:1725	arg1	Arg					1727:1729	C-terminal Arg	1716:1729	C-terminal Arg	1716:1729	Modelling of the C-terminal part of the natural substrate Arg(6)-Met-enkephalin into the active site shows that the S1' pocket of CPM is particularly well designed to accommodate P1'-Arg residues, in agreement with the preference of CPM for cleaving C-terminal Arg.
15066430	3	78	theme	GPI-free	637:644	arg1	CPM					646:648	human GPI-free CPM	631:648	human GPI-free CPM	631:648	We have crystallized human GPI-free CPM, and have determined and refined its 3.0A crystal structure.
15066430	1	79	theme	CPN/E	238:242	arg1	subfamily					244:252	the CPN/E subfamily	234:252	the CPN/E subfamily of "regulatory" metallo-carboxypeptidases	234:294	Carboxypeptidase M (CPM), an extracellular glycosylphosphatidyl-inositol(GPI)-anchored membrane glycoprotein belonging to the CPN/E subfamily of "regulatory" metallo-carboxypeptidases, specifically removes C-terminal basic residues from peptides and proteins.
15066430	1	80	from	peptides	349:356	arg1	residues					335:342	C-terminal basic residues	318:342	C-terminal basic residues from peptides and proteins	318:369	Carboxypeptidase M (CPM), an extracellular glycosylphosphatidyl-inositol(GPI)-anchored membrane glycoprotein belonging to the CPN/E subfamily of "regulatory" metallo-carboxypeptidases, specifically removes C-terminal basic residues from peptides and proteins.
15066430	1	81	theme	basic	329:333	arg1	residues					335:342	C-terminal basic residues	318:342	C-terminal basic residues from peptides and proteins	318:369	Carboxypeptidase M (CPM), an extracellular glycosylphosphatidyl-inositol(GPI)-anchored membrane glycoprotein belonging to the CPN/E subfamily of "regulatory" metallo-carboxypeptidases, specifically removes C-terminal basic residues from peptides and proteins.
15066430	2	82	from	distribution	388:399	arg1	tissues					410:416	human tissues	404:416	human tissues	404:416	Due to its wide distribution in human tissues, CPM is believed to play important roles in the control of peptide hormone and growth factor activity at the cell surface, and in the membrane-localized degradation of extracellular proteins.
15066430	4	83	theme	beta-sandwich	897:909	arg1	domain					922:927	an adjacent 86 residue beta-sandwich C-terminal domain	874:927	an adjacent 86 residue beta-sandwich C-terminal domain characteristic of the CPN/E family but more conically shaped than the equivalent domain in CPD-2	874:1024	The structure analysis reveals that CPM consists of a 295 residue N-terminal catalytic domain similar to that of duck CPD-2 (but only distantly related to CPA/B), an adjacent 86 residue beta-sandwich C-terminal domain characteristic of the CPN/E family but more conically shaped than the equivalent domain in CPD-2, and a unique, partially disordered 25 residue C-terminal extension to which the GPI membrane-anchor is post-translationally attached.
15066430	2	84	from	surface	532:538	arg1	activity					511:518	peptide hormone and growth factor activity	477:518	peptide hormone and growth factor activity at the cell surface	477:538	Due to its wide distribution in human tissues, CPM is believed to play important roles in the control of peptide hormone and growth factor activity at the cell surface, and in the membrane-localized degradation of extracellular proteins.
15066430	2	84	from	surface	532:538	arg1	control					466:472	the control	462:472	the control of peptide hormone and growth factor activity at the cell surface	462:538	Due to its wide distribution in human tissues, CPM is believed to play important roles in the control of peptide hormone and growth factor activity at the cell surface, and in the membrane-localized degradation of extracellular proteins.
15066430	4	85	theme	N-terminal	777:786	arg1	domain					798:803	a 295 residue N-terminal catalytic domain	763:803	a 295 residue N-terminal catalytic domain similar to that of duck CPD-2 (but only distantly related to CPA/B)	763:871	The structure analysis reveals that CPM consists of a 295 residue N-terminal catalytic domain similar to that of duck CPD-2 (but only distantly related to CPA/B), an adjacent 86 residue beta-sandwich C-terminal domain characteristic of the CPN/E family but more conically shaped than the equivalent domain in CPD-2, and a unique, partially disordered 25 residue C-terminal extension to which the GPI membrane-anchor is post-translationally attached.
15066430	3	86	theme	crystal	692:698	arg1	structure					700:708	its 3.0A crystal structure	683:708	its 3.0A crystal structure	683:708	We have crystallized human GPI-free CPM, and have determined and refined its 3.0A crystal structure.
26702061	2	0	theme	endothelial	486:496	arg1	junctions					517:525	endothelial cell intercellular junctions	486:525	endothelial cell intercellular junctions	486:525	PECAM-1-mediated homophilic interactions, known to be mediated by its 2 amino-terminal immunoglobulin homology domains, are essential for concentrating PECAM-1 at endothelial cell intercellular junctions, where it functions to facilitate diapedesis, maintain vascular integrity, and transmit survival signals into the cell.
26702061	1	1	theme	monolayers	311:320	arg1	junctions					271:279	the junctions	267:279	the junctions of confluent endothelial cell monolayers	267:320	Platelet endothelial cell adhesion molecule-1 (PECAM-1) is a 130-kDa member of the immunoglobulin gene superfamily (IgSF) that is present on the surface of circulating platelets and leukocytes, and highly expressed at the junctions of confluent endothelial cell monolayers.
26702061	2	2	theme	survival	615:622	arg1	signals					624:630	survival signals	615:630	survival signals into the cell	615:644	PECAM-1-mediated homophilic interactions, known to be mediated by its 2 amino-terminal immunoglobulin homology domains, are essential for concentrating PECAM-1 at endothelial cell intercellular junctions, where it functions to facilitate diapedesis, maintain vascular integrity, and transmit survival signals into the cell.
26702061	6	3	theme	homophilic-binding	1538:1555	arg1	interface					1557:1565	the trans homophilic-binding interface	1528:1565	the trans homophilic-binding interface	1528:1565	Both IgD1 and IgD2 participate importantly in the formation of the trans homophilic-binding interface, with a total buried interface area of >2300 Å(2).
26702061	1	4	theme	gene	147:150	arg1	IgSF					165:168	IgSF	165:168	IgSF	165:168	Platelet endothelial cell adhesion molecule-1 (PECAM-1) is a 130-kDa member of the immunoglobulin gene superfamily (IgSF) that is present on the surface of circulating platelets and leukocytes, and highly expressed at the junctions of confluent endothelial cell monolayers.
26702061	1	4	theme	gene	147:150	arg1	superfamily					152:162	immunoglobulin gene superfamily	132:162	the immunoglobulin gene superfamily (IgSF)	128:169	Platelet endothelial cell adhesion molecule-1 (PECAM-1) is a 130-kDa member of the immunoglobulin gene superfamily (IgSF) that is present on the surface of circulating platelets and leukocytes, and highly expressed at the junctions of confluent endothelial cell monolayers.
26702061	7	5	theme	junctions	1812:1820	arg1	assembly					1769:1776	assembly	1769:1776	assembly of endothelial cell intercellular junctions	1769:1820	These and other unique structural features of PECAM-1 allow for the development of an atomic-level model of the interactions that PECAM-1 forms during assembly of endothelial cell intercellular junctions.
26702061	4	6	theme	disulfide	1246:1254	arg1	bond					1256:1259	the hallmark disulfide bond	1233:1259	the hallmark disulfide bond between the B and F strands	1233:1287	The crystal structure revealed that both IgD1 and IgD2 exhibit a classical IgSF fold, having a β-sandwich topology formed by 2 sheets of antiparallel β strands stabilized by the hallmark disulfide bond between the B and F strands.
26702061	1	7	theme	superfamily	152:162	arg1	member					118:123	a 130-kDa member	108:123	a 130-kDa member of the immunoglobulin gene superfamily (IgSF) that is present on the surface of circulating platelets and leukocytes, and highly expressed at the junctions of confluent endothelial cell monolayers	108:320	Platelet endothelial cell adhesion molecule-1 (PECAM-1) is a 130-kDa member of the immunoglobulin gene superfamily (IgSF) that is present on the surface of circulating platelets and leukocytes, and highly expressed at the junctions of confluent endothelial cell monolayers.
26702061	1	7	theme	superfamily	152:162	arg1	molecule-1					84:93	Platelet endothelial cell adhesion molecule-1	49:93	Platelet endothelial cell adhesion molecule-1 (PECAM-1)	49:103	Platelet endothelial cell adhesion molecule-1 (PECAM-1) is a 130-kDa member of the immunoglobulin gene superfamily (IgSF) that is present on the surface of circulating platelets and leukocytes, and highly expressed at the junctions of confluent endothelial cell monolayers.
26702061	1	8	theme	leukocytes	231:240	arg1	surface					194:200	the surface	190:200	the surface of circulating platelets and leukocytes	190:240	Platelet endothelial cell adhesion molecule-1 (PECAM-1) is a 130-kDa member of the immunoglobulin gene superfamily (IgSF) that is present on the surface of circulating platelets and leukocytes, and highly expressed at the junctions of confluent endothelial cell monolayers.
26702061	4	9	theme	hallmark	1237:1244	arg1	bond					1256:1259	the hallmark disulfide bond	1233:1259	the hallmark disulfide bond between the B and F strands	1233:1287	The crystal structure revealed that both IgD1 and IgD2 exhibit a classical IgSF fold, having a β-sandwich topology formed by 2 sheets of antiparallel β strands stabilized by the hallmark disulfide bond between the B and F strands.
26702061	1	10	theme	endothelial	58:68	arg1	member					118:123	a 130-kDa member	108:123	a 130-kDa member of the immunoglobulin gene superfamily (IgSF) that is present on the surface of circulating platelets and leukocytes, and highly expressed at the junctions of confluent endothelial cell monolayers	108:320	Platelet endothelial cell adhesion molecule-1 (PECAM-1) is a 130-kDa member of the immunoglobulin gene superfamily (IgSF) that is present on the surface of circulating platelets and leukocytes, and highly expressed at the junctions of confluent endothelial cell monolayers.
26702061	1	10	theme	endothelial	58:68	arg1	PECAM-1					96:102	PECAM-1	96:102	PECAM-1	96:102	Platelet endothelial cell adhesion molecule-1 (PECAM-1) is a 130-kDa member of the immunoglobulin gene superfamily (IgSF) that is present on the surface of circulating platelets and leukocytes, and highly expressed at the junctions of confluent endothelial cell monolayers.
26702061	1	10	theme	endothelial	58:68	arg1	molecule-1					84:93	Platelet endothelial cell adhesion molecule-1	49:93	Platelet endothelial cell adhesion molecule-1 (PECAM-1)	49:103	Platelet endothelial cell adhesion molecule-1 (PECAM-1) is a 130-kDa member of the immunoglobulin gene superfamily (IgSF) that is present on the surface of circulating platelets and leukocytes, and highly expressed at the junctions of confluent endothelial cell monolayers.
26702061	3	11	theme	crystal	906:912	arg1	structure					914:922	the crystal structure	902:922	the crystal structure of the PECAM-1 homophilic-binding domain	902:963	Given the importance of PECAM-1-mediated homophilic interactions in mediating each of these cell physiological events, and to reveal the nature and orientation of the PECAM-1-PECAM-1 homophilic-binding interface, we undertook studies aimed at determining the crystal structure of the PECAM-1 homophilic-binding domain, which is composed of amino-terminal immunoglobulin homology domains 1 and 2 (IgD1 and IgD2).
26702061	3	12	theme	interface	849:857	arg1	nature					784:789	nature	784:789	nature	784:789	Given the importance of PECAM-1-mediated homophilic interactions in mediating each of these cell physiological events, and to reveal the nature and orientation of the PECAM-1-PECAM-1 homophilic-binding interface, we undertook studies aimed at determining the crystal structure of the PECAM-1 homophilic-binding domain, which is composed of amino-terminal immunoglobulin homology domains 1 and 2 (IgD1 and IgD2).
26702061	3	12	theme	interface	849:857	arg1	orientation					795:805	orientation	795:805	orientation	795:805	Given the importance of PECAM-1-mediated homophilic interactions in mediating each of these cell physiological events, and to reveal the nature and orientation of the PECAM-1-PECAM-1 homophilic-binding interface, we undertook studies aimed at determining the crystal structure of the PECAM-1 homophilic-binding domain, which is composed of amino-terminal immunoglobulin homology domains 1 and 2 (IgD1 and IgD2).
26702061	7	13	theme	cell	1793:1796	arg1	junctions					1812:1820	endothelial cell intercellular junctions	1781:1820	endothelial cell intercellular junctions	1781:1820	These and other unique structural features of PECAM-1 allow for the development of an atomic-level model of the interactions that PECAM-1 forms during assembly of endothelial cell intercellular junctions.
26702061	3	14	theme	physiological	744:756	arg1	events					758:763	these cell physiological events	733:763	these cell physiological events	733:763	Given the importance of PECAM-1-mediated homophilic interactions in mediating each of these cell physiological events, and to reveal the nature and orientation of the PECAM-1-PECAM-1 homophilic-binding interface, we undertook studies aimed at determining the crystal structure of the PECAM-1 homophilic-binding domain, which is composed of amino-terminal immunoglobulin homology domains 1 and 2 (IgD1 and IgD2).
26702061	6	15	theme	buried	1581:1586	arg1	2					1614:1614	2	1614:1614	2	1614:1614	Both IgD1 and IgD2 participate importantly in the formation of the trans homophilic-binding interface, with a total buried interface area of >2300 Å(2).
26702061	6	15	theme	buried	1581:1586	arg1	area					1598:1601	a total buried interface area	1573:1601	a total buried interface area of >2300 Å(2)	1573:1615	Both IgD1 and IgD2 participate importantly in the formation of the trans homophilic-binding interface, with a total buried interface area of >2300 Å(2).
26702061	5	16	theme	I2	1443:1444	arg1	IgSF					1453:1456	IgSF folds	1453:1462	IgSF folds	1453:1462	Interestingly, despite previous assignment to the C2 class of immunoglobulin-like domains, the structure of IgD1 reveals that it actually belongs to the I2 set of IgSF folds.
26702061	5	16	theme	I2	1443:1444	arg1	set					1446:1448	the I2 set	1439:1448	the I2 set of IgSF folds	1439:1462	Interestingly, despite previous assignment to the C2 class of immunoglobulin-like domains, the structure of IgD1 reveals that it actually belongs to the I2 set of IgSF folds.
26702061	1	17	theme	cell	70:73	arg1	member					118:123	a 130-kDa member	108:123	a 130-kDa member of the immunoglobulin gene superfamily (IgSF) that is present on the surface of circulating platelets and leukocytes, and highly expressed at the junctions of confluent endothelial cell monolayers	108:320	Platelet endothelial cell adhesion molecule-1 (PECAM-1) is a 130-kDa member of the immunoglobulin gene superfamily (IgSF) that is present on the surface of circulating platelets and leukocytes, and highly expressed at the junctions of confluent endothelial cell monolayers.
26702061	1	17	theme	cell	70:73	arg1	PECAM-1					96:102	PECAM-1	96:102	PECAM-1	96:102	Platelet endothelial cell adhesion molecule-1 (PECAM-1) is a 130-kDa member of the immunoglobulin gene superfamily (IgSF) that is present on the surface of circulating platelets and leukocytes, and highly expressed at the junctions of confluent endothelial cell monolayers.
26702061	1	17	theme	cell	70:73	arg1	molecule-1					84:93	Platelet endothelial cell adhesion molecule-1	49:93	Platelet endothelial cell adhesion molecule-1 (PECAM-1)	49:103	Platelet endothelial cell adhesion molecule-1 (PECAM-1) is a 130-kDa member of the immunoglobulin gene superfamily (IgSF) that is present on the surface of circulating platelets and leukocytes, and highly expressed at the junctions of confluent endothelial cell monolayers.
26702061	3	18	theme	homophilic-binding	939:956	arg1	domain					958:963	the PECAM-1 homophilic-binding domain	927:963	the PECAM-1 homophilic-binding domain	927:963	Given the importance of PECAM-1-mediated homophilic interactions in mediating each of these cell physiological events, and to reveal the nature and orientation of the PECAM-1-PECAM-1 homophilic-binding interface, we undertook studies aimed at determining the crystal structure of the PECAM-1 homophilic-binding domain, which is composed of amino-terminal immunoglobulin homology domains 1 and 2 (IgD1 and IgD2).
26702061	3	19	dep	nature	784:789	arg1	the					780:782	the	780:782	the	780:782	Given the importance of PECAM-1-mediated homophilic interactions in mediating each of these cell physiological events, and to reveal the nature and orientation of the PECAM-1-PECAM-1 homophilic-binding interface, we undertook studies aimed at determining the crystal structure of the PECAM-1 homophilic-binding domain, which is composed of amino-terminal immunoglobulin homology domains 1 and 2 (IgD1 and IgD2).
26702061	7	20	theme	other	1628:1632	arg1	features					1652:1659	other unique structural features	1628:1659	other unique structural features of PECAM-1	1628:1670	These and other unique structural features of PECAM-1 allow for the development of an atomic-level model of the interactions that PECAM-1 forms during assembly of endothelial cell intercellular junctions.
26702061	1	21	theme	adhesion	75:82	arg1	member					118:123	a 130-kDa member	108:123	a 130-kDa member of the immunoglobulin gene superfamily (IgSF) that is present on the surface of circulating platelets and leukocytes, and highly expressed at the junctions of confluent endothelial cell monolayers	108:320	Platelet endothelial cell adhesion molecule-1 (PECAM-1) is a 130-kDa member of the immunoglobulin gene superfamily (IgSF) that is present on the surface of circulating platelets and leukocytes, and highly expressed at the junctions of confluent endothelial cell monolayers.
26702061	1	21	theme	adhesion	75:82	arg1	PECAM-1					96:102	PECAM-1	96:102	PECAM-1	96:102	Platelet endothelial cell adhesion molecule-1 (PECAM-1) is a 130-kDa member of the immunoglobulin gene superfamily (IgSF) that is present on the surface of circulating platelets and leukocytes, and highly expressed at the junctions of confluent endothelial cell monolayers.
26702061	1	21	theme	adhesion	75:82	arg1	molecule-1					84:93	Platelet endothelial cell adhesion molecule-1	49:93	Platelet endothelial cell adhesion molecule-1 (PECAM-1)	49:103	Platelet endothelial cell adhesion molecule-1 (PECAM-1) is a 130-kDa member of the immunoglobulin gene superfamily (IgSF) that is present on the surface of circulating platelets and leukocytes, and highly expressed at the junctions of confluent endothelial cell monolayers.
26702061	3	22	theme	domain	958:963	arg1	structure					914:922	the crystal structure	902:922	the crystal structure of the PECAM-1 homophilic-binding domain	902:963	Given the importance of PECAM-1-mediated homophilic interactions in mediating each of these cell physiological events, and to reveal the nature and orientation of the PECAM-1-PECAM-1 homophilic-binding interface, we undertook studies aimed at determining the crystal structure of the PECAM-1 homophilic-binding domain, which is composed of amino-terminal immunoglobulin homology domains 1 and 2 (IgD1 and IgD2).
26702061	7	23	theme	intercellular	1798:1810	arg1	junctions					1812:1820	endothelial cell intercellular junctions	1781:1820	endothelial cell intercellular junctions	1781:1820	These and other unique structural features of PECAM-1 allow for the development of an atomic-level model of the interactions that PECAM-1 forms during assembly of endothelial cell intercellular junctions.
26702061	4	24	theme	classical	1124:1132	arg1	fold					1139:1142	a classical IgSF fold	1122:1142	a classical IgSF fold	1122:1142	The crystal structure revealed that both IgD1 and IgD2 exhibit a classical IgSF fold, having a β-sandwich topology formed by 2 sheets of antiparallel β strands stabilized by the hallmark disulfide bond between the B and F strands.
26702061	5	25	theme	IgSF	1453:1456	arg1	IgSF					1453:1456	IgSF folds	1453:1462	IgSF folds	1453:1462	Interestingly, despite previous assignment to the C2 class of immunoglobulin-like domains, the structure of IgD1 reveals that it actually belongs to the I2 set of IgSF folds.
26702061	5	25	theme	IgSF	1453:1456	arg1	set					1446:1448	the I2 set	1439:1448	the I2 set of IgSF folds	1439:1462	Interestingly, despite previous assignment to the C2 class of immunoglobulin-like domains, the structure of IgD1 reveals that it actually belongs to the I2 set of IgSF folds.
26702061	6	26	theme	Å	1612:1612	arg1	2					1614:1614	2	1614:1614	2	1614:1614	Both IgD1 and IgD2 participate importantly in the formation of the trans homophilic-binding interface, with a total buried interface area of >2300 Å(2).
26702061	6	26	theme	Å	1612:1612	arg1	area					1598:1601	a total buried interface area	1573:1601	a total buried interface area of >2300 Å(2)	1573:1615	Both IgD1 and IgD2 participate importantly in the formation of the trans homophilic-binding interface, with a total buried interface area of >2300 Å(2).
26702061	4	27	theme	β-sandwich	1154:1163	arg1	topology					1165:1172	a β-sandwich topology	1152:1172	a β-sandwich topology formed by 2 sheets of antiparallel β strands stabilized by the hallmark disulfide bond between the B and F strands	1152:1287	The crystal structure revealed that both IgD1 and IgD2 exhibit a classical IgSF fold, having a β-sandwich topology formed by 2 sheets of antiparallel β strands stabilized by the hallmark disulfide bond between the B and F strands.
26702061	3	28	theme	cell	739:742	arg1	events					758:763	these cell physiological events	733:763	these cell physiological events	733:763	Given the importance of PECAM-1-mediated homophilic interactions in mediating each of these cell physiological events, and to reveal the nature and orientation of the PECAM-1-PECAM-1 homophilic-binding interface, we undertook studies aimed at determining the crystal structure of the PECAM-1 homophilic-binding domain, which is composed of amino-terminal immunoglobulin homology domains 1 and 2 (IgD1 and IgD2).
26702061	4	29	theme	strands	1211:1217	arg1	sheets					1186:1191	2 sheets	1184:1191	2 sheets of antiparallel β strands stabilized by the hallmark disulfide bond between the B and F strands	1184:1287	The crystal structure revealed that both IgD1 and IgD2 exhibit a classical IgSF fold, having a β-sandwich topology formed by 2 sheets of antiparallel β strands stabilized by the hallmark disulfide bond between the B and F strands.
26702061	3	30	theme	PECAM-1	931:937	arg1	domain					958:963	the PECAM-1 homophilic-binding domain	927:963	the PECAM-1 homophilic-binding domain	927:963	Given the importance of PECAM-1-mediated homophilic interactions in mediating each of these cell physiological events, and to reveal the nature and orientation of the PECAM-1-PECAM-1 homophilic-binding interface, we undertook studies aimed at determining the crystal structure of the PECAM-1 homophilic-binding domain, which is composed of amino-terminal immunoglobulin homology domains 1 and 2 (IgD1 and IgD2).
26702061	0	31	theme	Structural	0:9	arg1	basis					11:15	Structural basis	0:15	Structural basis for PECAM-1 homophilic binding.	0:47	Structural basis for PECAM-1 homophilic binding.
26702061	7	32	theme	interactions	1730:1741	arg1	model					1717:1721	an atomic-level model	1701:1721	an atomic-level model of the interactions that PECAM-1 forms during assembly of endothelial cell intercellular junctions	1701:1820	These and other unique structural features of PECAM-1 allow for the development of an atomic-level model of the interactions that PECAM-1 forms during assembly of endothelial cell intercellular junctions.
26702061	4	33	theme	B	1273:1273	arg1	strands					1281:1287	the B and F strands	1269:1287	strands	1281:1287	The crystal structure revealed that both IgD1 and IgD2 exhibit a classical IgSF fold, having a β-sandwich topology formed by 2 sheets of antiparallel β strands stabilized by the hallmark disulfide bond between the B and F strands.
26702061	3	34	dep	domains	1026:1032	arg1	1					1034:1034	1	1034:1034	1	1034:1034	Given the importance of PECAM-1-mediated homophilic interactions in mediating each of these cell physiological events, and to reveal the nature and orientation of the PECAM-1-PECAM-1 homophilic-binding interface, we undertook studies aimed at determining the crystal structure of the PECAM-1 homophilic-binding domain, which is composed of amino-terminal immunoglobulin homology domains 1 and 2 (IgD1 and IgD2).
26702061	3	34	dep	domains	1026:1032	arg1	IgD2					1052:1055	IgD2	1052:1055	IgD2	1052:1055	Given the importance of PECAM-1-mediated homophilic interactions in mediating each of these cell physiological events, and to reveal the nature and orientation of the PECAM-1-PECAM-1 homophilic-binding interface, we undertook studies aimed at determining the crystal structure of the PECAM-1 homophilic-binding domain, which is composed of amino-terminal immunoglobulin homology domains 1 and 2 (IgD1 and IgD2).
26702061	3	34	dep	domains	1026:1032	arg1	IgD1					1043:1046	IgD1	1043:1046	IgD1	1043:1046	Given the importance of PECAM-1-mediated homophilic interactions in mediating each of these cell physiological events, and to reveal the nature and orientation of the PECAM-1-PECAM-1 homophilic-binding interface, we undertook studies aimed at determining the crystal structure of the PECAM-1 homophilic-binding domain, which is composed of amino-terminal immunoglobulin homology domains 1 and 2 (IgD1 and IgD2).
26702061	3	34	dep	domains	1026:1032	arg1	domains					1026:1032	amino-terminal immunoglobulin homology domains 1 and 2	987:1040	amino-terminal immunoglobulin homology domains 1 and 2 (IgD1 and IgD2)	987:1056	Given the importance of PECAM-1-mediated homophilic interactions in mediating each of these cell physiological events, and to reveal the nature and orientation of the PECAM-1-PECAM-1 homophilic-binding interface, we undertook studies aimed at determining the crystal structure of the PECAM-1 homophilic-binding domain, which is composed of amino-terminal immunoglobulin homology domains 1 and 2 (IgD1 and IgD2).
26702061	3	34	dep	domains	1026:1032	arg1	2					1040:1040	2	1040:1040	2	1040:1040	Given the importance of PECAM-1-mediated homophilic interactions in mediating each of these cell physiological events, and to reveal the nature and orientation of the PECAM-1-PECAM-1 homophilic-binding interface, we undertook studies aimed at determining the crystal structure of the PECAM-1 homophilic-binding domain, which is composed of amino-terminal immunoglobulin homology domains 1 and 2 (IgD1 and IgD2).
26702061	0	35	theme	PECAM-1	21:27	arg1	binding					40:46	PECAM-1 homophilic binding	21:46	PECAM-1 homophilic binding	21:46	Structural basis for PECAM-1 homophilic binding.
26702061	7	36	theme	structural	1641:1650	arg1	features					1652:1659	other unique structural features	1628:1659	other unique structural features of PECAM-1	1628:1670	These and other unique structural features of PECAM-1 allow for the development of an atomic-level model of the interactions that PECAM-1 forms during assembly of endothelial cell intercellular junctions.
26702061	5	37	theme	previous	1313:1320	arg1	assignment					1322:1331	previous assignment	1313:1331	previous assignment to the C2 class of immunoglobulin-like domains	1313:1378	Interestingly, despite previous assignment to the C2 class of immunoglobulin-like domains, the structure of IgD1 reveals that it actually belongs to the I2 set of IgSF folds.
26702061	2	38	theme	immunoglobulin	410:423	arg1	domains					434:440	2 amino-terminal immunoglobulin homology domains	393:440	its 2 amino-terminal immunoglobulin homology domains	389:440	PECAM-1-mediated homophilic interactions, known to be mediated by its 2 amino-terminal immunoglobulin homology domains, are essential for concentrating PECAM-1 at endothelial cell intercellular junctions, where it functions to facilitate diapedesis, maintain vascular integrity, and transmit survival signals into the cell.
26702061	2	39	theme	homology	425:432	arg1	domains					434:440	2 amino-terminal immunoglobulin homology domains	393:440	its 2 amino-terminal immunoglobulin homology domains	389:440	PECAM-1-mediated homophilic interactions, known to be mediated by its 2 amino-terminal immunoglobulin homology domains, are essential for concentrating PECAM-1 at endothelial cell intercellular junctions, where it functions to facilitate diapedesis, maintain vascular integrity, and transmit survival signals into the cell.
26702061	7	40	theme	endothelial	1781:1791	arg1	junctions					1812:1820	endothelial cell intercellular junctions	1781:1820	endothelial cell intercellular junctions	1781:1820	These and other unique structural features of PECAM-1 allow for the development of an atomic-level model of the interactions that PECAM-1 forms during assembly of endothelial cell intercellular junctions.
26702061	5	41	theme	IgD1	1398:1401	arg1	structure					1385:1393	the structure	1381:1393	the structure of IgD1	1381:1401	Interestingly, despite previous assignment to the C2 class of immunoglobulin-like domains, the structure of IgD1 reveals that it actually belongs to the I2 set of IgSF folds.
26702061	2	42	theme	homophilic	340:349	arg1	interactions					351:362	PECAM-1-mediated homophilic interactions	323:362	PECAM-1-mediated homophilic interactions	323:362	PECAM-1-mediated homophilic interactions, known to be mediated by its 2 amino-terminal immunoglobulin homology domains, are essential for concentrating PECAM-1 at endothelial cell intercellular junctions, where it functions to facilitate diapedesis, maintain vascular integrity, and transmit survival signals into the cell.
26702061	2	43	theme	amino-terminal	395:408	arg1	domains					434:440	2 amino-terminal immunoglobulin homology domains	393:440	its 2 amino-terminal immunoglobulin homology domains	389:440	PECAM-1-mediated homophilic interactions, known to be mediated by its 2 amino-terminal immunoglobulin homology domains, are essential for concentrating PECAM-1 at endothelial cell intercellular junctions, where it functions to facilitate diapedesis, maintain vascular integrity, and transmit survival signals into the cell.
26702061	5	44	theme	C2	1340:1341	arg1	class					1343:1347	the C2 class	1336:1347	the C2 class of immunoglobulin-like domains	1336:1378	Interestingly, despite previous assignment to the C2 class of immunoglobulin-like domains, the structure of IgD1 reveals that it actually belongs to the I2 set of IgSF folds.
26702061	4	45	theme	IgSF	1134:1137	arg1	fold					1139:1142	a classical IgSF fold	1122:1142	a classical IgSF fold	1122:1142	The crystal structure revealed that both IgD1 and IgD2 exhibit a classical IgSF fold, having a β-sandwich topology formed by 2 sheets of antiparallel β strands stabilized by the hallmark disulfide bond between the B and F strands.
26702061	7	46	theme	PECAM-1	1664:1670	arg1	features					1652:1659	other unique structural features	1628:1659	other unique structural features of PECAM-1	1628:1670	These and other unique structural features of PECAM-1 allow for the development of an atomic-level model of the interactions that PECAM-1 forms during assembly of endothelial cell intercellular junctions.
26702061	0	47	theme	homophilic	29:38	arg1	binding					40:46	PECAM-1 homophilic binding	21:46	PECAM-1 homophilic binding	21:46	Structural basis for PECAM-1 homophilic binding.
26702061	4	48	theme	crystal	1063:1069	arg1	structure					1071:1079	The crystal structure	1059:1079	The crystal structure	1059:1079	The crystal structure revealed that both IgD1 and IgD2 exhibit a classical IgSF fold, having a β-sandwich topology formed by 2 sheets of antiparallel β strands stabilized by the hallmark disulfide bond between the B and F strands.
26702061	3	49	theme	immunoglobulin	1002:1015	arg1	IgD2					1052:1055	IgD2	1052:1055	IgD2	1052:1055	Given the importance of PECAM-1-mediated homophilic interactions in mediating each of these cell physiological events, and to reveal the nature and orientation of the PECAM-1-PECAM-1 homophilic-binding interface, we undertook studies aimed at determining the crystal structure of the PECAM-1 homophilic-binding domain, which is composed of amino-terminal immunoglobulin homology domains 1 and 2 (IgD1 and IgD2).
26702061	3	49	theme	immunoglobulin	1002:1015	arg1	IgD1					1043:1046	IgD1	1043:1046	IgD1	1043:1046	Given the importance of PECAM-1-mediated homophilic interactions in mediating each of these cell physiological events, and to reveal the nature and orientation of the PECAM-1-PECAM-1 homophilic-binding interface, we undertook studies aimed at determining the crystal structure of the PECAM-1 homophilic-binding domain, which is composed of amino-terminal immunoglobulin homology domains 1 and 2 (IgD1 and IgD2).
26702061	3	49	theme	immunoglobulin	1002:1015	arg1	domains					1026:1032	amino-terminal immunoglobulin homology domains 1 and 2	987:1040	amino-terminal immunoglobulin homology domains 1 and 2 (IgD1 and IgD2)	987:1056	Given the importance of PECAM-1-mediated homophilic interactions in mediating each of these cell physiological events, and to reveal the nature and orientation of the PECAM-1-PECAM-1 homophilic-binding interface, we undertook studies aimed at determining the crystal structure of the PECAM-1 homophilic-binding domain, which is composed of amino-terminal immunoglobulin homology domains 1 and 2 (IgD1 and IgD2).
26702061	3	50	theme	homology	1017:1024	arg1	IgD2					1052:1055	IgD2	1052:1055	IgD2	1052:1055	Given the importance of PECAM-1-mediated homophilic interactions in mediating each of these cell physiological events, and to reveal the nature and orientation of the PECAM-1-PECAM-1 homophilic-binding interface, we undertook studies aimed at determining the crystal structure of the PECAM-1 homophilic-binding domain, which is composed of amino-terminal immunoglobulin homology domains 1 and 2 (IgD1 and IgD2).
26702061	3	50	theme	homology	1017:1024	arg1	IgD1					1043:1046	IgD1	1043:1046	IgD1	1043:1046	Given the importance of PECAM-1-mediated homophilic interactions in mediating each of these cell physiological events, and to reveal the nature and orientation of the PECAM-1-PECAM-1 homophilic-binding interface, we undertook studies aimed at determining the crystal structure of the PECAM-1 homophilic-binding domain, which is composed of amino-terminal immunoglobulin homology domains 1 and 2 (IgD1 and IgD2).
26702061	3	50	theme	homology	1017:1024	arg1	domains					1026:1032	amino-terminal immunoglobulin homology domains 1 and 2	987:1040	amino-terminal immunoglobulin homology domains 1 and 2 (IgD1 and IgD2)	987:1056	Given the importance of PECAM-1-mediated homophilic interactions in mediating each of these cell physiological events, and to reveal the nature and orientation of the PECAM-1-PECAM-1 homophilic-binding interface, we undertook studies aimed at determining the crystal structure of the PECAM-1 homophilic-binding domain, which is composed of amino-terminal immunoglobulin homology domains 1 and 2 (IgD1 and IgD2).
26702061	2	51	theme	PECAM-1-mediated	323:338	arg1	interactions					351:362	PECAM-1-mediated homophilic interactions	323:362	PECAM-1-mediated homophilic interactions	323:362	PECAM-1-mediated homophilic interactions, known to be mediated by its 2 amino-terminal immunoglobulin homology domains, are essential for concentrating PECAM-1 at endothelial cell intercellular junctions, where it functions to facilitate diapedesis, maintain vascular integrity, and transmit survival signals into the cell.
26702061	5	52	dep	IgSF	1453:1456	arg1	folds					1458:1462	folds	1458:1462	folds	1458:1462	Interestingly, despite previous assignment to the C2 class of immunoglobulin-like domains, the structure of IgD1 reveals that it actually belongs to the I2 set of IgSF folds.
26702061	1	53	theme	confluent	284:292	arg1	monolayers					311:320	confluent endothelial cell monolayers	284:320	confluent endothelial cell monolayers	284:320	Platelet endothelial cell adhesion molecule-1 (PECAM-1) is a 130-kDa member of the immunoglobulin gene superfamily (IgSF) that is present on the surface of circulating platelets and leukocytes, and highly expressed at the junctions of confluent endothelial cell monolayers.
26702061	2	54	theme	vascular	582:589	arg1	integrity					591:599	vascular integrity	582:599	vascular integrity	582:599	PECAM-1-mediated homophilic interactions, known to be mediated by its 2 amino-terminal immunoglobulin homology domains, are essential for concentrating PECAM-1 at endothelial cell intercellular junctions, where it functions to facilitate diapedesis, maintain vascular integrity, and transmit survival signals into the cell.
26702061	3	55	theme	homophilic	688:697	arg1	interactions					699:710	PECAM-1-mediated homophilic interactions	671:710	PECAM-1-mediated homophilic interactions	671:710	Given the importance of PECAM-1-mediated homophilic interactions in mediating each of these cell physiological events, and to reveal the nature and orientation of the PECAM-1-PECAM-1 homophilic-binding interface, we undertook studies aimed at determining the crystal structure of the PECAM-1 homophilic-binding domain, which is composed of amino-terminal immunoglobulin homology domains 1 and 2 (IgD1 and IgD2).
26702061	4	56	theme	β	1209:1209	arg1	strands					1211:1217	antiparallel β strands	1196:1217	antiparallel β strands stabilized by the hallmark disulfide bond between the B and F strands	1196:1287	The crystal structure revealed that both IgD1 and IgD2 exhibit a classical IgSF fold, having a β-sandwich topology formed by 2 sheets of antiparallel β strands stabilized by the hallmark disulfide bond between the B and F strands.
26702061	1	57	theme	130-kDa	110:116	arg1	member					118:123	a 130-kDa member	108:123	a 130-kDa member of the immunoglobulin gene superfamily (IgSF) that is present on the surface of circulating platelets and leukocytes, and highly expressed at the junctions of confluent endothelial cell monolayers	108:320	Platelet endothelial cell adhesion molecule-1 (PECAM-1) is a 130-kDa member of the immunoglobulin gene superfamily (IgSF) that is present on the surface of circulating platelets and leukocytes, and highly expressed at the junctions of confluent endothelial cell monolayers.
26702061	1	57	theme	130-kDa	110:116	arg1	molecule-1					84:93	Platelet endothelial cell adhesion molecule-1	49:93	Platelet endothelial cell adhesion molecule-1 (PECAM-1)	49:103	Platelet endothelial cell adhesion molecule-1 (PECAM-1) is a 130-kDa member of the immunoglobulin gene superfamily (IgSF) that is present on the surface of circulating platelets and leukocytes, and highly expressed at the junctions of confluent endothelial cell monolayers.
26702061	6	58	theme	trans	1532:1536	arg1	interface					1557:1565	the trans homophilic-binding interface	1528:1565	the trans homophilic-binding interface	1528:1565	Both IgD1 and IgD2 participate importantly in the formation of the trans homophilic-binding interface, with a total buried interface area of >2300 Å(2).
26702061	1	59	theme	endothelial	294:304	arg1	monolayers					311:320	confluent endothelial cell monolayers	284:320	confluent endothelial cell monolayers	284:320	Platelet endothelial cell adhesion molecule-1 (PECAM-1) is a 130-kDa member of the immunoglobulin gene superfamily (IgSF) that is present on the surface of circulating platelets and leukocytes, and highly expressed at the junctions of confluent endothelial cell monolayers.
26702061	3	60	theme	interactions	699:710	arg1	importance					657:666	the importance	653:666	the importance of PECAM-1-mediated homophilic interactions in mediating each of these cell physiological events, and to reveal the nature and orientation of the PECAM-1-PECAM-1 homophilic-binding interface	653:857	Given the importance of PECAM-1-mediated homophilic interactions in mediating each of these cell physiological events, and to reveal the nature and orientation of the PECAM-1-PECAM-1 homophilic-binding interface, we undertook studies aimed at determining the crystal structure of the PECAM-1 homophilic-binding domain, which is composed of amino-terminal immunoglobulin homology domains 1 and 2 (IgD1 and IgD2).
26702061	3	61	theme	amino-terminal	987:1000	arg1	IgD2					1052:1055	IgD2	1052:1055	IgD2	1052:1055	Given the importance of PECAM-1-mediated homophilic interactions in mediating each of these cell physiological events, and to reveal the nature and orientation of the PECAM-1-PECAM-1 homophilic-binding interface, we undertook studies aimed at determining the crystal structure of the PECAM-1 homophilic-binding domain, which is composed of amino-terminal immunoglobulin homology domains 1 and 2 (IgD1 and IgD2).
26702061	3	61	theme	amino-terminal	987:1000	arg1	IgD1					1043:1046	IgD1	1043:1046	IgD1	1043:1046	Given the importance of PECAM-1-mediated homophilic interactions in mediating each of these cell physiological events, and to reveal the nature and orientation of the PECAM-1-PECAM-1 homophilic-binding interface, we undertook studies aimed at determining the crystal structure of the PECAM-1 homophilic-binding domain, which is composed of amino-terminal immunoglobulin homology domains 1 and 2 (IgD1 and IgD2).
26702061	3	61	theme	amino-terminal	987:1000	arg1	domains					1026:1032	amino-terminal immunoglobulin homology domains 1 and 2	987:1040	amino-terminal immunoglobulin homology domains 1 and 2 (IgD1 and IgD2)	987:1056	Given the importance of PECAM-1-mediated homophilic interactions in mediating each of these cell physiological events, and to reveal the nature and orientation of the PECAM-1-PECAM-1 homophilic-binding interface, we undertook studies aimed at determining the crystal structure of the PECAM-1 homophilic-binding domain, which is composed of amino-terminal immunoglobulin homology domains 1 and 2 (IgD1 and IgD2).
26702061	7	62	theme	atomic-level	1704:1715	arg1	model					1717:1721	an atomic-level model	1701:1721	an atomic-level model of the interactions that PECAM-1 forms during assembly of endothelial cell intercellular junctions	1701:1820	These and other unique structural features of PECAM-1 allow for the development of an atomic-level model of the interactions that PECAM-1 forms during assembly of endothelial cell intercellular junctions.
26702061	6	63	theme	total	1575:1579	arg1	2					1614:1614	2	1614:1614	2	1614:1614	Both IgD1 and IgD2 participate importantly in the formation of the trans homophilic-binding interface, with a total buried interface area of >2300 Å(2).
26702061	6	63	theme	total	1575:1579	arg1	area					1598:1601	a total buried interface area	1573:1601	a total buried interface area of >2300 Å(2)	1573:1615	Both IgD1 and IgD2 participate importantly in the formation of the trans homophilic-binding interface, with a total buried interface area of >2300 Å(2).
26702061	3	64	theme	PECAM-1-PECAM-1	814:828	arg1	interface					849:857	the PECAM-1-PECAM-1 homophilic-binding interface	810:857	the PECAM-1-PECAM-1 homophilic-binding interface	810:857	Given the importance of PECAM-1-mediated homophilic interactions in mediating each of these cell physiological events, and to reveal the nature and orientation of the PECAM-1-PECAM-1 homophilic-binding interface, we undertook studies aimed at determining the crystal structure of the PECAM-1 homophilic-binding domain, which is composed of amino-terminal immunoglobulin homology domains 1 and 2 (IgD1 and IgD2).
26702061	4	65	theme	antiparallel	1196:1207	arg1	strands					1211:1217	antiparallel β strands	1196:1217	antiparallel β strands stabilized by the hallmark disulfide bond between the B and F strands	1196:1287	The crystal structure revealed that both IgD1 and IgD2 exhibit a classical IgSF fold, having a β-sandwich topology formed by 2 sheets of antiparallel β strands stabilized by the hallmark disulfide bond between the B and F strands.
26702061	4	66	theme	F	1279:1279	arg1	strands					1281:1287	the B and F strands	1269:1287	strands	1281:1287	The crystal structure revealed that both IgD1 and IgD2 exhibit a classical IgSF fold, having a β-sandwich topology formed by 2 sheets of antiparallel β strands stabilized by the hallmark disulfide bond between the B and F strands.
26702061	6	67	theme	interface	1588:1596	arg1	2					1614:1614	2	1614:1614	2	1614:1614	Both IgD1 and IgD2 participate importantly in the formation of the trans homophilic-binding interface, with a total buried interface area of >2300 Å(2).
26702061	6	67	theme	interface	1588:1596	arg1	area					1598:1601	a total buried interface area	1573:1601	a total buried interface area of >2300 Å(2)	1573:1615	Both IgD1 and IgD2 participate importantly in the formation of the trans homophilic-binding interface, with a total buried interface area of >2300 Å(2).
26702061	5	68	theme	immunoglobulin-like	1352:1370	arg1	domains					1372:1378	immunoglobulin-like domains	1352:1378	immunoglobulin-like domains	1352:1378	Interestingly, despite previous assignment to the C2 class of immunoglobulin-like domains, the structure of IgD1 reveals that it actually belongs to the I2 set of IgSF folds.
26702061	7	69	theme	unique	1634:1639	arg1	features					1652:1659	other unique structural features	1628:1659	other unique structural features of PECAM-1	1628:1670	These and other unique structural features of PECAM-1 allow for the development of an atomic-level model of the interactions that PECAM-1 forms during assembly of endothelial cell intercellular junctions.
26702061	3	70	theme	homophilic-binding	830:847	arg1	interface					849:857	the PECAM-1-PECAM-1 homophilic-binding interface	810:857	the PECAM-1-PECAM-1 homophilic-binding interface	810:857	Given the importance of PECAM-1-mediated homophilic interactions in mediating each of these cell physiological events, and to reveal the nature and orientation of the PECAM-1-PECAM-1 homophilic-binding interface, we undertook studies aimed at determining the crystal structure of the PECAM-1 homophilic-binding domain, which is composed of amino-terminal immunoglobulin homology domains 1 and 2 (IgD1 and IgD2).
26702061	2	71	theme	intercellular	503:515	arg1	junctions					517:525	endothelial cell intercellular junctions	486:525	endothelial cell intercellular junctions	486:525	PECAM-1-mediated homophilic interactions, known to be mediated by its 2 amino-terminal immunoglobulin homology domains, are essential for concentrating PECAM-1 at endothelial cell intercellular junctions, where it functions to facilitate diapedesis, maintain vascular integrity, and transmit survival signals into the cell.
26702061	3	72	theme	PECAM-1-mediated	671:686	arg1	interactions					699:710	PECAM-1-mediated homophilic interactions	671:710	PECAM-1-mediated homophilic interactions	671:710	Given the importance of PECAM-1-mediated homophilic interactions in mediating each of these cell physiological events, and to reveal the nature and orientation of the PECAM-1-PECAM-1 homophilic-binding interface, we undertook studies aimed at determining the crystal structure of the PECAM-1 homophilic-binding domain, which is composed of amino-terminal immunoglobulin homology domains 1 and 2 (IgD1 and IgD2).
26702061	5	73	theme	domains	1372:1378	arg1	class					1343:1347	the C2 class	1336:1347	the C2 class of immunoglobulin-like domains	1336:1378	Interestingly, despite previous assignment to the C2 class of immunoglobulin-like domains, the structure of IgD1 reveals that it actually belongs to the I2 set of IgSF folds.
26702061	7	74	theme	model	1717:1721	arg1	development					1686:1696	the development	1682:1696	the development of an atomic-level model of the interactions that PECAM-1 forms during assembly of endothelial cell intercellular junctions	1682:1820	These and other unique structural features of PECAM-1 allow for the development of an atomic-level model of the interactions that PECAM-1 forms during assembly of endothelial cell intercellular junctions.
26702061	1	75	theme	circulating	205:215	arg1	platelets					217:225	circulating platelets	205:225	circulating platelets	205:225	Platelet endothelial cell adhesion molecule-1 (PECAM-1) is a 130-kDa member of the immunoglobulin gene superfamily (IgSF) that is present on the surface of circulating platelets and leukocytes, and highly expressed at the junctions of confluent endothelial cell monolayers.
26702061	2	76	theme	cell	498:501	arg1	junctions					517:525	endothelial cell intercellular junctions	486:525	endothelial cell intercellular junctions	486:525	PECAM-1-mediated homophilic interactions, known to be mediated by its 2 amino-terminal immunoglobulin homology domains, are essential for concentrating PECAM-1 at endothelial cell intercellular junctions, where it functions to facilitate diapedesis, maintain vascular integrity, and transmit survival signals into the cell.
26702061	1	77	theme	cell	306:309	arg1	monolayers					311:320	confluent endothelial cell monolayers	284:320	confluent endothelial cell monolayers	284:320	Platelet endothelial cell adhesion molecule-1 (PECAM-1) is a 130-kDa member of the immunoglobulin gene superfamily (IgSF) that is present on the surface of circulating platelets and leukocytes, and highly expressed at the junctions of confluent endothelial cell monolayers.
26702061	1	78	theme	Platelet	49:56	arg1	member					118:123	a 130-kDa member	108:123	a 130-kDa member of the immunoglobulin gene superfamily (IgSF) that is present on the surface of circulating platelets and leukocytes, and highly expressed at the junctions of confluent endothelial cell monolayers	108:320	Platelet endothelial cell adhesion molecule-1 (PECAM-1) is a 130-kDa member of the immunoglobulin gene superfamily (IgSF) that is present on the surface of circulating platelets and leukocytes, and highly expressed at the junctions of confluent endothelial cell monolayers.
26702061	1	78	theme	Platelet	49:56	arg1	PECAM-1					96:102	PECAM-1	96:102	PECAM-1	96:102	Platelet endothelial cell adhesion molecule-1 (PECAM-1) is a 130-kDa member of the immunoglobulin gene superfamily (IgSF) that is present on the surface of circulating platelets and leukocytes, and highly expressed at the junctions of confluent endothelial cell monolayers.
26702061	1	78	theme	Platelet	49:56	arg1	molecule-1					84:93	Platelet endothelial cell adhesion molecule-1	49:93	Platelet endothelial cell adhesion molecule-1 (PECAM-1)	49:103	Platelet endothelial cell adhesion molecule-1 (PECAM-1) is a 130-kDa member of the immunoglobulin gene superfamily (IgSF) that is present on the surface of circulating platelets and leukocytes, and highly expressed at the junctions of confluent endothelial cell monolayers.
26702061	6	79	theme	interface	1557:1565	arg1	formation					1515:1523	the formation	1511:1523	the formation of the trans homophilic-binding interface	1511:1565	Both IgD1 and IgD2 participate importantly in the formation of the trans homophilic-binding interface, with a total buried interface area of >2300 Å(2).
26702061	1	80	theme	immunoglobulin	132:145	arg1	IgSF					165:168	IgSF	165:168	IgSF	165:168	Platelet endothelial cell adhesion molecule-1 (PECAM-1) is a 130-kDa member of the immunoglobulin gene superfamily (IgSF) that is present on the surface of circulating platelets and leukocytes, and highly expressed at the junctions of confluent endothelial cell monolayers.
26702061	1	80	theme	immunoglobulin	132:145	arg1	superfamily					152:162	immunoglobulin gene superfamily	132:162	the immunoglobulin gene superfamily (IgSF)	128:169	Platelet endothelial cell adhesion molecule-1 (PECAM-1) is a 130-kDa member of the immunoglobulin gene superfamily (IgSF) that is present on the surface of circulating platelets and leukocytes, and highly expressed at the junctions of confluent endothelial cell monolayers.
26702061	1	81	theme	platelets	217:225	arg1	surface					194:200	the surface	190:200	the surface of circulating platelets and leukocytes	190:240	Platelet endothelial cell adhesion molecule-1 (PECAM-1) is a 130-kDa member of the immunoglobulin gene superfamily (IgSF) that is present on the surface of circulating platelets and leukocytes, and highly expressed at the junctions of confluent endothelial cell monolayers.
22267737	7	0	theme	regulatory	940:949	arg1	segment					951:957	the regulatory segment	936:957	the regulatory segment	936:957	In C6, the regulatory segment includes four auxiliary domains that stabilize the closed conformation, inhibiting release of membrane-inserting elements.
22267737	1	1	theme	C6	285:286	arg1	copy					272:275	one copy	268:275	one copy each of C6, C7, and C8	268:298	The complement membrane attack complex (MAC) is formed by the sequential assembly of C5b with four homologous proteins as follows: one copy each of C6, C7, and C8 and 12-14 copies of C9.
22267737	1	1	theme	C6	285:286	arg1	copies					310:315	12-14 copies	304:315	12-14 copies of C9	304:321	The complement membrane attack complex (MAC) is formed by the sequential assembly of C5b with four homologous proteins as follows: one copy each of C6, C7, and C8 and 12-14 copies of C9.
22267737	8	2	theme	partner	1189:1195	arg1	β-sheet					1164:1170	the central β-sheet	1152:1170	the central β-sheet of its clockwise partner, C8α	1152:1200	In C8β, rotation of the regulatory segment is linked to an opening of the central β-sheet of its clockwise partner, C8α.
22267737	3	3	theme	MAC-perforin	406:417	arg1	domain					419:424	a MAC-perforin domain	404:424	a MAC-perforin domain flanked by 4-9 "auxiliary" domains	404:459	C6 through C9 comprise a MAC-perforin domain flanked by 4-9 "auxiliary" domains.
22267737	1	4	dep	follows	259:265	arg1	copy					272:275	one copy	268:275	one copy each of C6, C7, and C8	268:298	The complement membrane attack complex (MAC) is formed by the sequential assembly of C5b with four homologous proteins as follows: one copy each of C6, C7, and C8 and 12-14 copies of C9.
22267737	1	4	dep	follows	259:265	arg1	copies					310:315	12-14 copies	304:315	12-14 copies of C9	304:321	The complement membrane attack complex (MAC) is formed by the sequential assembly of C5b with four homologous proteins as follows: one copy each of C6, C7, and C8 and 12-14 copies of C9.
22267737	1	5	theme	complement	141:150	arg1	complex					168:174	The complement membrane attack complex	137:174	The complement membrane attack complex (MAC)	137:180	The complement membrane attack complex (MAC) is formed by the sequential assembly of C5b with four homologous proteins as follows: one copy each of C6, C7, and C8 and 12-14 copies of C9.
22267737	1	5	theme	complement	141:150	arg1	MAC					177:179	MAC	177:179	MAC	177:179	The complement membrane attack complex (MAC) is formed by the sequential assembly of C5b with four homologous proteins as follows: one copy each of C6, C7, and C8 and 12-14 copies of C9.
22267737	9	6	theme	final	1560:1564	arg1	pore					1566:1569	the final pore	1556:1569	the final pore	1556:1569	Based on these observations, we propose a model for initiation and unidirectional propagation of the MAC in which the auxiliary domains play key roles: in the assembly of the C5b-8 initiation complex; in driving and regulating the opening of the β-sheet of the MAC-performin domain of each new recruit as it adds to the growing pore; and in stabilizing the final pore.
22267737	1	7	theme	C5b	222:224	arg1	assembly					210:217	the sequential assembly	195:217	the sequential assembly of C5b with four homologous proteins as follows: one copy each of C6, C7, and C8 and 12-14 copies of C9	195:321	The complement membrane attack complex (MAC) is formed by the sequential assembly of C5b with four homologous proteins as follows: one copy each of C6, C7, and C8 and 12-14 copies of C9.
22267737	9	8	theme	MAC-performin	1464:1476	arg1	domain					1478:1483	the MAC-performin domain	1460:1483	the MAC-performin domain of each new	1460:1495	Based on these observations, we propose a model for initiation and unidirectional propagation of the MAC in which the auxiliary domains play key roles: in the assembly of the C5b-8 initiation complex; in driving and regulating the opening of the β-sheet of the MAC-performin domain of each new recruit as it adds to the growing pore; and in stabilizing the final pore.
22267737	9	8	theme	MAC-performin	1464:1476	arg1	new					1493:1495	each new	1488:1495	each new	1488:1495	Based on these observations, we propose a model for initiation and unidirectional propagation of the MAC in which the auxiliary domains play key roles: in the assembly of the C5b-8 initiation complex; in driving and regulating the opening of the β-sheet of the MAC-performin domain of each new recruit as it adds to the growing pore; and in stabilizing the final pore.
22267737	2	9	from	pore	352:355	arg1	membranes					370:378	bacterial membranes	360:378	bacterial membranes	360:378	Together these form a lytic pore in bacterial membranes.
22267737	3	10	theme	auxiliary	442:450	arg1	domains					453:459	4-9 "auxiliary" domains	437:459	4-9 "auxiliary" domains	437:459	C6 through C9 comprise a MAC-perforin domain flanked by 4-9 "auxiliary" domains.
22267737	9	11	theme	unidirectional	1270:1283	arg1	propagation					1285:1295	unidirectional propagation	1270:1295	unidirectional propagation	1270:1295	Based on these observations, we propose a model for initiation and unidirectional propagation of the MAC in which the auxiliary domains play key roles: in the assembly of the C5b-8 initiation complex; in driving and regulating the opening of the β-sheet of the MAC-performin domain of each new recruit as it adds to the growing pore; and in stabilizing the final pore.
22267737	4	12	theme	crystal	482:488	arg1	structure					490:498	the crystal structure	478:498	the crystal structure of C6, the first and longest of the pore proteins to be recruited by C5b	478:571	Here, we report the crystal structure of C6, the first and longest of the pore proteins to be recruited by C5b.
22267737	0	13	theme	sequential	83:92	arg1	assembly					94:101	sequential assembly	83:101	sequential assembly of membrane attack complex (MAC)	83:134	Structure of complement C6 suggests a mechanism for initiation and unidirectional, sequential assembly of membrane attack complex (MAC).
22267737	0	13	theme	sequential	83:92	arg1	initiation					52:61	initiation	52:61	initiation	52:61	Structure of complement C6 suggests a mechanism for initiation and unidirectional, sequential assembly of membrane attack complex (MAC).
22267737	1	14	dep	copy	272:275	arg1	each					277:280	each	277:280	each	277:280	The complement membrane attack complex (MAC) is formed by the sequential assembly of C5b with four homologous proteins as follows: one copy each of C6, C7, and C8 and 12-14 copies of C9.
22267737	3	15	theme	"	451:451	arg1	domains					453:459	4-9 "auxiliary" domains	437:459	4-9 "auxiliary" domains	437:459	C6 through C9 comprise a MAC-perforin domain flanked by 4-9 "auxiliary" domains.
22267737	7	16	theme	closed	1010:1015	arg1	conformation					1017:1028	the closed conformation	1006:1028	the closed conformation	1006:1028	In C6, the regulatory segment includes four auxiliary domains that stabilize the closed conformation, inhibiting release of membrane-inserting elements.
22267737	0	17	theme	membrane	106:113	arg1	MAC					131:133	MAC	131:133	MAC	131:133	Structure of complement C6 suggests a mechanism for initiation and unidirectional, sequential assembly of membrane attack complex (MAC).
22267737	0	17	theme	membrane	106:113	arg1	complex					122:128	membrane attack complex	106:128	membrane attack complex (MAC)	106:134	Structure of complement C6 suggests a mechanism for initiation and unidirectional, sequential assembly of membrane attack complex (MAC).
22267737	10	18	theme	pore	1599:1602	arg1	model					1576:1580	Our model	1572:1580	Our model of the assembled pore	1572:1602	Our model of the assembled pore resembles those of the cholesterol-dependent cytolysins but is distinct from that recently proposed for perforin.
22267737	7	19	theme	membrane-inserting	1053:1070	arg1	elements					1072:1079	membrane-inserting elements	1053:1079	membrane-inserting elements	1053:1079	In C6, the regulatory segment includes four auxiliary domains that stabilize the closed conformation, inhibiting release of membrane-inserting elements.
22267737	6	20	contain	contain	811:817	arg1	C8α					798:800	C8α	798:800	C8α	798:800	We further show that C6, C8α, and C8β contain three homologous subdomains ("upper," "lower," and "regulatory") related by rotations about two hinge points.
22267737	6	20	contain	contain	811:817	arg1	C8β					807:809	C8β	807:809	C8β	807:809	We further show that C6, C8α, and C8β contain three homologous subdomains ("upper," "lower," and "regulatory") related by rotations about two hinge points.
22267737	6	20	contain	contain	811:817	arg1	C6					794:795	C6	794:795	C6	794:795	We further show that C6, C8α, and C8β contain three homologous subdomains ("upper," "lower," and "regulatory") related by rotations about two hinge points.
22267737	6	20	contain	contain	811:817	arg2	subdomains					836:845	three homologous subdomains	819:845	three homologous subdomains ("upper," "lower," and "regulatory") related by rotations about two hinge points	819:926	We further show that C6, C8α, and C8β contain three homologous subdomains ("upper," "lower," and "regulatory") related by rotations about two hinge points.
22267737	9	21	theme	growing	1523:1529	arg1	pore					1531:1534	the growing pore	1519:1534	the growing pore	1519:1534	Based on these observations, we propose a model for initiation and unidirectional propagation of the MAC in which the auxiliary domains play key roles: in the assembly of the C5b-8 initiation complex; in driving and regulating the opening of the β-sheet of the MAC-performin domain of each new recruit as it adds to the growing pore; and in stabilizing the final pore.
22267737	1	22	theme	membrane	152:159	arg1	complex					168:174	The complement membrane attack complex	137:174	The complement membrane attack complex (MAC)	137:180	The complement membrane attack complex (MAC) is formed by the sequential assembly of C5b with four homologous proteins as follows: one copy each of C6, C7, and C8 and 12-14 copies of C9.
22267737	1	22	theme	membrane	152:159	arg1	MAC					177:179	MAC	177:179	MAC	177:179	The complement membrane attack complex (MAC) is formed by the sequential assembly of C5b with four homologous proteins as follows: one copy each of C6, C7, and C8 and 12-14 copies of C9.
22267737	5	23	theme	central	658:664	arg1	C6					676:677	C6	676:677	C6	676:677	Comparisons with the structures of the C8αβγ heterodimer and perforin show that the central domain of C6 adopts a "closed" (perforin-like) state that is distinct from the "open" conformations in C8.
22267737	5	23	theme	central	658:664	arg1	domain					666:671	the central domain	654:671	the central domain of C6	654:677	Comparisons with the structures of the C8αβγ heterodimer and perforin show that the central domain of C6 adopts a "closed" (perforin-like) state that is distinct from the "open" conformations in C8.
22267737	1	24	theme	C8	297:298	arg1	copy					272:275	one copy	268:275	one copy each of C6, C7, and C8	268:298	The complement membrane attack complex (MAC) is formed by the sequential assembly of C5b with four homologous proteins as follows: one copy each of C6, C7, and C8 and 12-14 copies of C9.
22267737	1	24	theme	C8	297:298	arg1	copies					310:315	12-14 copies	304:315	12-14 copies of C9	304:321	The complement membrane attack complex (MAC) is formed by the sequential assembly of C5b with four homologous proteins as follows: one copy each of C6, C7, and C8 and 12-14 copies of C9.
22267737	9	25	theme	C5b-8	1378:1382	arg1	complex					1395:1401	the C5b-8 initiation complex	1374:1401	the C5b-8 initiation complex	1374:1401	Based on these observations, we propose a model for initiation and unidirectional propagation of the MAC in which the auxiliary domains play key roles: in the assembly of the C5b-8 initiation complex; in driving and regulating the opening of the β-sheet of the MAC-performin domain of each new recruit as it adds to the growing pore; and in stabilizing the final pore.
22267737	9	26	theme	key	1344:1346	arg1	roles					1348:1352	key roles	1344:1352	key roles:	1344:1353	Based on these observations, we propose a model for initiation and unidirectional propagation of the MAC in which the auxiliary domains play key roles: in the assembly of the C5b-8 initiation complex; in driving and regulating the opening of the β-sheet of the MAC-performin domain of each new recruit as it adds to the growing pore; and in stabilizing the final pore.
22267737	1	27	theme	attack	161:166	arg1	complex					168:174	The complement membrane attack complex	137:174	The complement membrane attack complex (MAC)	137:180	The complement membrane attack complex (MAC) is formed by the sequential assembly of C5b with four homologous proteins as follows: one copy each of C6, C7, and C8 and 12-14 copies of C9.
22267737	1	27	theme	attack	161:166	arg1	MAC					177:179	MAC	177:179	MAC	177:179	The complement membrane attack complex (MAC) is formed by the sequential assembly of C5b with four homologous proteins as follows: one copy each of C6, C7, and C8 and 12-14 copies of C9.
22267737	9	28	theme	new	1493:1495	arg1	domain					1478:1483	the MAC-performin domain	1460:1483	the MAC-performin domain of each new	1460:1495	Based on these observations, we propose a model for initiation and unidirectional propagation of the MAC in which the auxiliary domains play key roles: in the assembly of the C5b-8 initiation complex; in driving and regulating the opening of the β-sheet of the MAC-performin domain of each new recruit as it adds to the growing pore; and in stabilizing the final pore.
22267737	9	28	theme	new	1493:1495	arg1	new					1493:1495	each new	1488:1495	each new	1488:1495	Based on these observations, we propose a model for initiation and unidirectional propagation of the MAC in which the auxiliary domains play key roles: in the assembly of the C5b-8 initiation complex; in driving and regulating the opening of the β-sheet of the MAC-performin domain of each new recruit as it adds to the growing pore; and in stabilizing the final pore.
22267737	5	29	theme	perforin	635:642	arg1	structures					595:604	the structures	591:604	the structures of the C8αβγ heterodimer and perforin	591:642	Comparisons with the structures of the C8αβγ heterodimer and perforin show that the central domain of C6 adopts a "closed" (perforin-like) state that is distinct from the "open" conformations in C8.
22267737	9	30	theme	initiation	1384:1393	arg1	complex					1395:1401	the C5b-8 initiation complex	1374:1401	the C5b-8 initiation complex	1374:1401	Based on these observations, we propose a model for initiation and unidirectional propagation of the MAC in which the auxiliary domains play key roles: in the assembly of the C5b-8 initiation complex; in driving and regulating the opening of the β-sheet of the MAC-performin domain of each new recruit as it adds to the growing pore; and in stabilizing the final pore.
22267737	10	31	theme	cholesterol-dependent	1627:1647	arg1	cytolysins					1649:1658	the cholesterol-dependent cytolysins	1623:1658	the cholesterol-dependent cytolysins	1623:1658	Our model of the assembled pore resembles those of the cholesterol-dependent cytolysins but is distinct from that recently proposed for perforin.
22267737	8	32	theme	segment	1117:1123	arg1	rotation					1090:1097	rotation	1090:1097	rotation of the regulatory segment	1090:1123	In C8β, rotation of the regulatory segment is linked to an opening of the central β-sheet of its clockwise partner, C8α.
22267737	10	33	theme	assembled	1589:1597	arg1	pore					1599:1602	the assembled pore	1585:1602	the assembled pore	1585:1602	Our model of the assembled pore resembles those of the cholesterol-dependent cytolysins but is distinct from that recently proposed for perforin.
22267737	7	34	theme	elements	1072:1079	arg1	release					1042:1048	release	1042:1048	release of membrane-inserting elements	1042:1079	In C6, the regulatory segment includes four auxiliary domains that stabilize the closed conformation, inhibiting release of membrane-inserting elements.
22267737	1	35	theme	homologous	236:245	arg1	proteins					247:254	four homologous proteins	231:254	four homologous proteins as follows: one copy each of C6, C7, and C8 and 12-14 copies of C9	231:321	The complement membrane attack complex (MAC) is formed by the sequential assembly of C5b with four homologous proteins as follows: one copy each of C6, C7, and C8 and 12-14 copies of C9.
22267737	9	36	theme	complex	1395:1401	arg1	assembly					1362:1369	the assembly	1358:1369	the assembly of the C5b-8 initiation complex	1358:1401	Based on these observations, we propose a model for initiation and unidirectional propagation of the MAC in which the auxiliary domains play key roles: in the assembly of the C5b-8 initiation complex; in driving and regulating the opening of the β-sheet of the MAC-performin domain of each new recruit as it adds to the growing pore; and in stabilizing the final pore.
22267737	6	37	dep	upper	849:853	arg1	lower					858:862	lower	858:862	lower	858:862	We further show that C6, C8α, and C8β contain three homologous subdomains ("upper," "lower," and "regulatory") related by rotations about two hinge points.
22267737	4	38	theme	pore	536:539	arg1	proteins					541:548	the pore proteins	532:548	the pore proteins	532:548	Here, we report the crystal structure of C6, the first and longest of the pore proteins to be recruited by C5b.
22267737	0	39	theme	C6	24:25	arg1	Structure					0:8	Structure	0:8	Structure of complement C6	0:25	Structure of complement C6 suggests a mechanism for initiation and unidirectional, sequential assembly of membrane attack complex (MAC).
22267737	0	40	theme	complex	122:128	arg1	assembly					94:101	sequential assembly	83:101	sequential assembly of membrane attack complex (MAC)	83:134	Structure of complement C6 suggests a mechanism for initiation and unidirectional, sequential assembly of membrane attack complex (MAC).
22267737	0	40	theme	complex	122:128	arg1	initiation					52:61	initiation	52:61	initiation	52:61	Structure of complement C6 suggests a mechanism for initiation and unidirectional, sequential assembly of membrane attack complex (MAC).
22267737	9	41	theme	MAC	1304:1306	arg1	initiation					1255:1264	initiation	1255:1264	initiation	1255:1264	Based on these observations, we propose a model for initiation and unidirectional propagation of the MAC in which the auxiliary domains play key roles: in the assembly of the C5b-8 initiation complex; in driving and regulating the opening of the β-sheet of the MAC-performin domain of each new recruit as it adds to the growing pore; and in stabilizing the final pore.
22267737	9	41	theme	MAC	1304:1306	arg1	propagation					1285:1295	unidirectional propagation	1270:1295	unidirectional propagation	1270:1295	Based on these observations, we propose a model for initiation and unidirectional propagation of the MAC in which the auxiliary domains play key roles: in the assembly of the C5b-8 initiation complex; in driving and regulating the opening of the β-sheet of the MAC-performin domain of each new recruit as it adds to the growing pore; and in stabilizing the final pore.
22267737	5	42	with	Comparisons	574:584	arg1	structures					595:604	the structures	591:604	the structures of the C8αβγ heterodimer and perforin	591:642	Comparisons with the structures of the C8αβγ heterodimer and perforin show that the central domain of C6 adopts a "closed" (perforin-like) state that is distinct from the "open" conformations in C8.
22267737	0	43	theme	complement	13:22	arg1	C6					24:25	complement C6	13:25	complement C6	13:25	Structure of complement C6 suggests a mechanism for initiation and unidirectional, sequential assembly of membrane attack complex (MAC).
22267737	0	44	theme	attack	115:120	arg1	MAC					131:133	MAC	131:133	MAC	131:133	Structure of complement C6 suggests a mechanism for initiation and unidirectional, sequential assembly of membrane attack complex (MAC).
22267737	0	44	theme	attack	115:120	arg1	complex					122:128	membrane attack complex	106:128	membrane attack complex (MAC)	106:134	Structure of complement C6 suggests a mechanism for initiation and unidirectional, sequential assembly of membrane attack complex (MAC).
22267737	8	45	theme	clockwise	1179:1187	arg1	partner					1189:1195	its clockwise partner	1175:1195	its clockwise partner	1175:1195	In C8β, rotation of the regulatory segment is linked to an opening of the central β-sheet of its clockwise partner, C8α.
22267737	8	45	theme	clockwise	1179:1187	arg1	C8α					1198:1200	C8α	1198:1200	C8α	1198:1200	In C8β, rotation of the regulatory segment is linked to an opening of the central β-sheet of its clockwise partner, C8α.
22267737	6	46	theme	related	884:890	arg1	subdomains					836:845	three homologous subdomains	819:845	three homologous subdomains ("upper," "lower," and "regulatory") related by rotations about two hinge points	819:926	We further show that C6, C8α, and C8β contain three homologous subdomains ("upper," "lower," and "regulatory") related by rotations about two hinge points.
22267737	5	47	theme	C6	676:677	arg1	C6					676:677	C6	676:677	C6	676:677	Comparisons with the structures of the C8αβγ heterodimer and perforin show that the central domain of C6 adopts a "closed" (perforin-like) state that is distinct from the "open" conformations in C8.
22267737	5	47	theme	C6	676:677	arg1	domain					666:671	the central domain	654:671	the central domain of C6	654:677	Comparisons with the structures of the C8αβγ heterodimer and perforin show that the central domain of C6 adopts a "closed" (perforin-like) state that is distinct from the "open" conformations in C8.
22267737	6	48	theme	upper	849:853	arg1	"					864:864	upper," "lower,"	849:864	upper," "lower,"	849:864	We further show that C6, C8α, and C8β contain three homologous subdomains ("upper," "lower," and "regulatory") related by rotations about two hinge points.
22267737	5	49	theme	closed	689:694	arg1	distinct					727:734	distinct	727:734	distinct	727:734	Comparisons with the structures of the C8αβγ heterodimer and perforin show that the central domain of C6 adopts a "closed" (perforin-like) state that is distinct from the "open" conformations in C8.
22267737	5	49	theme	closed	689:694	arg1	state					713:717	a "closed" (perforin-like) state	686:717	a "closed" (perforin-like) state that is distinct from the "open" conformations in C8	686:770	Comparisons with the structures of the C8αβγ heterodimer and perforin show that the central domain of C6 adopts a "closed" (perforin-like) state that is distinct from the "open" conformations in C8.
22267737	9	50	theme	β-sheet	1449:1455	arg1	opening					1434:1440	the opening	1430:1440	the opening of the β-sheet of the MAC-performin domain of each new recruit as it adds to the growing pore	1430:1534	Based on these observations, we propose a model for initiation and unidirectional propagation of the MAC in which the auxiliary domains play key roles: in the assembly of the C5b-8 initiation complex; in driving and regulating the opening of the β-sheet of the MAC-performin domain of each new recruit as it adds to the growing pore; and in stabilizing the final pore.
22267737	2	51	theme	lytic	346:350	arg1	pore					352:355	a lytic pore	344:355	a lytic pore in bacterial membranes	344:378	Together these form a lytic pore in bacterial membranes.
22267737	5	52	theme	"	695:695	arg1	distinct					727:734	distinct	727:734	distinct	727:734	Comparisons with the structures of the C8αβγ heterodimer and perforin show that the central domain of C6 adopts a "closed" (perforin-like) state that is distinct from the "open" conformations in C8.
22267737	5	52	theme	"	695:695	arg1	state					713:717	a "closed" (perforin-like) state	686:717	a "closed" (perforin-like) state that is distinct from the "open" conformations in C8	686:770	Comparisons with the structures of the C8αβγ heterodimer and perforin show that the central domain of C6 adopts a "closed" (perforin-like) state that is distinct from the "open" conformations in C8.
22267737	9	53	dep	opening	1434:1440	arg1	recruit					1497:1503	recruit	1497:1503	recruit as it adds to the growing pore	1497:1534	Based on these observations, we propose a model for initiation and unidirectional propagation of the MAC in which the auxiliary domains play key roles: in the assembly of the C5b-8 initiation complex; in driving and regulating the opening of the β-sheet of the MAC-performin domain of each new recruit as it adds to the growing pore; and in stabilizing the final pore.
22267737	1	54	theme	C9	320:321	arg1	copy					272:275	one copy	268:275	one copy each of C6, C7, and C8	268:298	The complement membrane attack complex (MAC) is formed by the sequential assembly of C5b with four homologous proteins as follows: one copy each of C6, C7, and C8 and 12-14 copies of C9.
22267737	1	54	theme	C9	320:321	arg1	copies					310:315	12-14 copies	304:315	12-14 copies of C9	304:321	The complement membrane attack complex (MAC) is formed by the sequential assembly of C5b with four homologous proteins as follows: one copy each of C6, C7, and C8 and 12-14 copies of C9.
22267737	9	55	theme	auxiliary	1321:1329	arg1	domains					1331:1337	the auxiliary domains	1317:1337	the auxiliary domains	1317:1337	Based on these observations, we propose a model for initiation and unidirectional propagation of the MAC in which the auxiliary domains play key roles: in the assembly of the C5b-8 initiation complex; in driving and regulating the opening of the β-sheet of the MAC-performin domain of each new recruit as it adds to the growing pore; and in stabilizing the final pore.
22267737	8	56	theme	regulatory	1106:1115	arg1	segment					1117:1123	the regulatory segment	1102:1123	the regulatory segment	1102:1123	In C8β, rotation of the regulatory segment is linked to an opening of the central β-sheet of its clockwise partner, C8α.
22267737	2	57	theme	bacterial	360:368	arg1	membranes					370:378	bacterial membranes	360:378	bacterial membranes	360:378	Together these form a lytic pore in bacterial membranes.
22267737	10	58	from	that	1681:1684	arg1	distinct					1667:1674	distinct	1667:1674	distinct	1667:1674	Our model of the assembled pore resembles those of the cholesterol-dependent cytolysins but is distinct from that recently proposed for perforin.
22267737	1	59	theme	C7	289:290	arg1	copy					272:275	one copy	268:275	one copy each of C6, C7, and C8	268:298	The complement membrane attack complex (MAC) is formed by the sequential assembly of C5b with four homologous proteins as follows: one copy each of C6, C7, and C8 and 12-14 copies of C9.
22267737	1	59	theme	C7	289:290	arg1	copies					310:315	12-14 copies	304:315	12-14 copies of C9	304:321	The complement membrane attack complex (MAC) is formed by the sequential assembly of C5b with four homologous proteins as follows: one copy each of C6, C7, and C8 and 12-14 copies of C9.
22267737	6	60	theme	hinge	915:919	arg1	points					921:926	two hinge points	911:926	two hinge points	911:926	We further show that C6, C8α, and C8β contain three homologous subdomains ("upper," "lower," and "regulatory") related by rotations about two hinge points.
22267737	8	61	theme	central	1156:1162	arg1	β-sheet					1164:1170	the central β-sheet	1152:1170	the central β-sheet of its clockwise partner, C8α	1152:1200	In C8β, rotation of the regulatory segment is linked to an opening of the central β-sheet of its clockwise partner, C8α.
22267737	1	62	with	C5b	222:224	arg1	proteins					247:254	four homologous proteins	231:254	four homologous proteins as follows: one copy each of C6, C7, and C8 and 12-14 copies of C9	231:321	The complement membrane attack complex (MAC) is formed by the sequential assembly of C5b with four homologous proteins as follows: one copy each of C6, C7, and C8 and 12-14 copies of C9.
22267737	5	63	theme	open	746:749	arg1	conformations					752:764	the "open" conformations	741:764	the "open" conformations in C8	741:770	Comparisons with the structures of the C8αβγ heterodimer and perforin show that the central domain of C6 adopts a "closed" (perforin-like) state that is distinct from the "open" conformations in C8.
22267737	6	64	dep	subdomains	836:845	arg1	"					864:864	upper," "lower,"	849:864	upper," "lower,"	849:864	We further show that C6, C8α, and C8β contain three homologous subdomains ("upper," "lower," and "regulatory") related by rotations about two hinge points.
22267737	6	64	dep	subdomains	836:845	arg1	"					881:881	"regulatory"	870:881	"regulatory"	870:881	We further show that C6, C8α, and C8β contain three homologous subdomains ("upper," "lower," and "regulatory") related by rotations about two hinge points.
22267737	5	65	theme	"	750:750	arg1	conformations					752:764	the "open" conformations	741:764	the "open" conformations in C8	741:770	Comparisons with the structures of the C8αβγ heterodimer and perforin show that the central domain of C6 adopts a "closed" (perforin-like) state that is distinct from the "open" conformations in C8.
22267737	5	66	from	conformations	752:764	arg1	C8					769:770	C8	769:770	C8	769:770	Comparisons with the structures of the C8αβγ heterodimer and perforin show that the central domain of C6 adopts a "closed" (perforin-like) state that is distinct from the "open" conformations in C8.
22267737	5	66	from	conformations	752:764	arg1	distinct					727:734	distinct	727:734	distinct	727:734	Comparisons with the structures of the C8αβγ heterodimer and perforin show that the central domain of C6 adopts a "closed" (perforin-like) state that is distinct from the "open" conformations in C8.
22267737	5	66	from	conformations	752:764	arg1	state					713:717	a "closed" (perforin-like) state	686:717	a "closed" (perforin-like) state that is distinct from the "open" conformations in C8	686:770	Comparisons with the structures of the C8αβγ heterodimer and perforin show that the central domain of C6 adopts a "closed" (perforin-like) state that is distinct from the "open" conformations in C8.
22267737	6	67	theme	regulatory	871:880	arg1	"					881:881	"regulatory"	870:881	"regulatory"	870:881	We further show that C6, C8α, and C8β contain three homologous subdomains ("upper," "lower," and "regulatory") related by rotations about two hinge points.
22267737	5	68	theme	C8αβγ	613:617	arg1	heterodimer					619:629	the C8αβγ heterodimer	609:629	the C8αβγ heterodimer	609:629	Comparisons with the structures of the C8αβγ heterodimer and perforin show that the central domain of C6 adopts a "closed" (perforin-like) state that is distinct from the "open" conformations in C8.
22267737	6	69	theme	homologous	825:834	arg1	subdomains					836:845	three homologous subdomains	819:845	three homologous subdomains ("upper," "lower," and "regulatory") related by rotations about two hinge points	819:926	We further show that C6, C8α, and C8β contain three homologous subdomains ("upper," "lower," and "regulatory") related by rotations about two hinge points.
22267737	9	70	theme	domain	1478:1483	arg1	β-sheet					1449:1455	the β-sheet	1445:1455	the β-sheet of the MAC-performin domain of each new	1445:1495	Based on these observations, we propose a model for initiation and unidirectional propagation of the MAC in which the auxiliary domains play key roles: in the assembly of the C5b-8 initiation complex; in driving and regulating the opening of the β-sheet of the MAC-performin domain of each new recruit as it adds to the growing pore; and in stabilizing the final pore.
22267737	8	71	attach	linked	1128:1133	arg1	opening					1141:1147	an opening	1138:1147	an opening of the central β-sheet of its clockwise partner, C8α	1138:1200	In C8β, rotation of the regulatory segment is linked to an opening of the central β-sheet of its clockwise partner, C8α.
22267737	8	71	attach	linked	1128:1133	arg3	C8β					1085:1087	C8β	1085:1087	C8β	1085:1087	In C8β, rotation of the regulatory segment is linked to an opening of the central β-sheet of its clockwise partner, C8α.
22267737	8	71	attach	linked	1128:1133	arg2	rotation					1090:1097	rotation	1090:1097	rotation of the regulatory segment	1090:1123	In C8β, rotation of the regulatory segment is linked to an opening of the central β-sheet of its clockwise partner, C8α.
22267737	5	72	theme	perforin-like	698:710	arg1	distinct					727:734	distinct	727:734	distinct	727:734	Comparisons with the structures of the C8αβγ heterodimer and perforin show that the central domain of C6 adopts a "closed" (perforin-like) state that is distinct from the "open" conformations in C8.
22267737	5	72	theme	perforin-like	698:710	arg1	state					713:717	a "closed" (perforin-like) state	686:717	a "closed" (perforin-like) state that is distinct from the "open" conformations in C8	686:770	Comparisons with the structures of the C8αβγ heterodimer and perforin show that the central domain of C6 adopts a "closed" (perforin-like) state that is distinct from the "open" conformations in C8.
22267737	1	73	theme	sequential	199:208	arg1	assembly					210:217	the sequential assembly	195:217	the sequential assembly of C5b with four homologous proteins as follows: one copy each of C6, C7, and C8 and 12-14 copies of C9	195:321	The complement membrane attack complex (MAC) is formed by the sequential assembly of C5b with four homologous proteins as follows: one copy each of C6, C7, and C8 and 12-14 copies of C9.
22267737	5	74	theme	heterodimer	619:629	arg1	structures					595:604	the structures	591:604	the structures of the C8αβγ heterodimer and perforin	591:642	Comparisons with the structures of the C8αβγ heterodimer and perforin show that the central domain of C6 adopts a "closed" (perforin-like) state that is distinct from the "open" conformations in C8.
22267737	8	75	theme	β-sheet	1164:1170	arg1	opening					1141:1147	an opening	1138:1147	an opening of the central β-sheet of its clockwise partner, C8α	1138:1200	In C8β, rotation of the regulatory segment is linked to an opening of the central β-sheet of its clockwise partner, C8α.
22267737	7	76	theme	auxiliary	973:981	arg1	domains					983:989	four auxiliary domains	968:989	four auxiliary domains that stabilize the closed conformation, inhibiting release of membrane-inserting elements	968:1079	In C6, the regulatory segment includes four auxiliary domains that stabilize the closed conformation, inhibiting release of membrane-inserting elements.
22267737	4	77	theme	C6	503:504	arg1	structure					490:498	the crystal structure	478:498	the crystal structure of C6, the first and longest of the pore proteins to be recruited by C5b	478:571	Here, we report the crystal structure of C6, the first and longest of the pore proteins to be recruited by C5b.
19692335	8	0	theme	metalloproteinase-like	1620:1641	arg1	domain					1643:1648	The metalloproteinase-like domain	1616:1648	The metalloproteinase-like domain	1616:1648	The metalloproteinase-like domain contacts the rest of ADAM22 with discontinuous, hydrophilic, and poorly complemented interactions, suggesting the possibility of modular movement of ADAM22 and other ADAMs.
19692335	0	1	theme	ADAM	167:170	arg1	function					172:179	ADAM function	167:179	ADAM function	167:179	Structural characterization of the ectodomain of a disintegrin and metalloproteinase-22 (ADAM22), a neural adhesion receptor instead of metalloproteinase: insights on ADAM function.
19692335	8	2	theme	hydrophilic	1698:1708	arg1	interactions					1735:1746	discontinuous, hydrophilic, and poorly complemented interactions	1683:1746	discontinuous, hydrophilic, and poorly complemented interactions	1683:1746	The metalloproteinase-like domain contacts the rest of ADAM22 with discontinuous, hydrophilic, and poorly complemented interactions, suggesting the possibility of modular movement of ADAM22 and other ADAMs.
19692335	7	3	from	one	1506:1508	arg1	domain					1540:1545	the metalloproteinase-like domain	1513:1545	the metalloproteinase-like domain	1513:1545	The structure, combined with calorimetric experiments, suggests distinct roles of three putative calcium ions bound to ADAM22, with one in the metalloproteinase-like domain being regulatory and two in the disintegrin domain being structural.
19692335	7	4	theme	calcium	1471:1477	arg1	ions					1479:1482	three putative calcium ions	1456:1482	three putative calcium ions bound to ADAM22	1456:1498	The structure, combined with calorimetric experiments, suggests distinct roles of three putative calcium ions bound to ADAM22, with one in the metalloproteinase-like domain being regulatory and two in the disintegrin domain being structural.
19692335	4	5	theme	synaptic	878:885	arg1	transmission					894:905	synaptic signal transmission	878:905	synaptic signal transmission	878:905	One of such non-proteinase ADAMs, ADAM22, acts as a receptor on the surface of the postsynaptic neuron to regulate synaptic signal transmission.
19692335	9	6	theme	adhesive	1915:1922	arg1	function					1924:1931	their adhesive function	1909:1931	their adhesive function	1909:1931	The ADAM22 structure provides a framework for understanding how different ADAMs exert their adhesive function and shedding activities.
19692335	3	7	theme	protein	734:740	arg1	shedding					753:760	membrane protein ectodomain shedding	725:760	protein-protein interactions instead of membrane protein ectodomain shedding	685:760	Although most members of the ADAM family are active zinc metalloproteinases, 8 of 21 ADAMs lack functional metalloproteinase domains and are implicated in protein-protein interactions instead of membrane protein ectodomain shedding.
19692335	6	8	theme	catalytic	1263:1271	arg1	residues					1273:1280	critical catalytic residues	1254:1280	critical catalytic residues	1254:1280	The loss of metalloproteinase activity is ensured by the absence of critical catalytic residues, the filling of the substrate groove, and the steric hindrance by the cysteine-rich domain.
19692335	1	9	theme	transmembrane	255:267	arg1	glycoproteins					269:281	multidomain transmembrane glycoproteins	243:281	multidomain transmembrane glycoproteins with diverse roles in physiology and diseases	243:327	ADAMs (a disintegrin and metalloproteinases) are a family of multidomain transmembrane glycoproteins with diverse roles in physiology and diseases, with several members being drug targets for cancer and inflammation therapies.
19692335	7	10	theme	calorimetric	1403:1414	arg1	experiments					1416:1426	calorimetric experiments	1403:1426	calorimetric experiments	1403:1426	The structure, combined with calorimetric experiments, suggests distinct roles of three putative calcium ions bound to ADAM22, with one in the metalloproteinase-like domain being regulatory and two in the disintegrin domain being structural.
19692335	5	11	with	clover	1013:1018	arg1	domain					1052:1057	the metalloproteinase-like domain	1025:1057	the metalloproteinase-like domain held in the concave face of a rigid module formed by the disintegrin, cysteine-rich, and epidermal growth factor-like domains	1025:1183	The crystal structure of the full ectodomain of mature human ADAM22 shows that it is a compact four-leaf clover with the metalloproteinase-like domain held in the concave face of a rigid module formed by the disintegrin, cysteine-rich, and epidermal growth factor-like domains.
19692335	1	12	from	roles	296:300	arg1	physiology					305:314	physiology	305:314	physiology	305:314	ADAMs (a disintegrin and metalloproteinases) are a family of multidomain transmembrane glycoproteins with diverse roles in physiology and diseases, with several members being drug targets for cancer and inflammation therapies.
19692335	1	12	from	roles	296:300	arg1	diseases					320:327	diseases	320:327	diseases	320:327	ADAMs (a disintegrin and metalloproteinases) are a family of multidomain transmembrane glycoproteins with diverse roles in physiology and diseases, with several members being drug targets for cancer and inflammation therapies.
19692335	8	13	theme	complemented	1722:1733	arg1	interactions					1735:1746	discontinuous, hydrophilic, and poorly complemented interactions	1683:1746	discontinuous, hydrophilic, and poorly complemented interactions	1683:1746	The metalloproteinase-like domain contacts the rest of ADAM22 with discontinuous, hydrophilic, and poorly complemented interactions, suggesting the possibility of modular movement of ADAM22 and other ADAMs.
19692335	4	14	theme	postsynaptic	846:857	arg1	neuron					859:864	the postsynaptic neuron	842:864	the postsynaptic neuron	842:864	One of such non-proteinase ADAMs, ADAM22, acts as a receptor on the surface of the postsynaptic neuron to regulate synaptic signal transmission.
19692335	1	15	theme	glycoproteins	269:281	arg1	ADAMs					182:186	ADAMs	182:186	ADAMs (a disintegrin and metalloproteinases)	182:225	ADAMs (a disintegrin and metalloproteinases) are a family of multidomain transmembrane glycoproteins with diverse roles in physiology and diseases, with several members being drug targets for cancer and inflammation therapies.
19692335	1	15	theme	glycoproteins	269:281	arg1	family					233:238	a family	231:238	a family of multidomain transmembrane glycoproteins with diverse roles in physiology and diseases	231:327	ADAMs (a disintegrin and metalloproteinases) are a family of multidomain transmembrane glycoproteins with diverse roles in physiology and diseases, with several members being drug targets for cancer and inflammation therapies.
19692335	3	16	theme	family	564:569	arg1	metalloproteinases					587:604	active zinc metalloproteinases	575:604	active zinc metalloproteinases	575:604	Although most members of the ADAM family are active zinc metalloproteinases, 8 of 21 ADAMs lack functional metalloproteinase domains and are implicated in protein-protein interactions instead of membrane protein ectodomain shedding.
19692335	3	16	theme	family	564:569	arg1	members					544:550	most members	539:550	most members of the ADAM family	539:569	Although most members of the ADAM family are active zinc metalloproteinases, 8 of 21 ADAMs lack functional metalloproteinase domains and are implicated in protein-protein interactions instead of membrane protein ectodomain shedding.
19692335	0	17	theme	adhesion	107:114	arg1	receptor					116:123	a neural adhesion receptor	98:123	a neural adhesion receptor	98:123	Structural characterization of the ectodomain of a disintegrin and metalloproteinase-22 (ADAM22), a neural adhesion receptor instead of metalloproteinase: insights on ADAM function.
19692335	0	17	theme	adhesion	107:114	arg1	metalloproteinase-22					67:86	metalloproteinase-22	67:86	metalloproteinase-22 (ADAM22)	67:95	Structural characterization of the ectodomain of a disintegrin and metalloproteinase-22 (ADAM22), a neural adhesion receptor instead of metalloproteinase: insights on ADAM function.
19692335	6	18	theme	groove	1312:1317	arg1	filling					1287:1293	the filling	1283:1293	the filling of the substrate groove	1283:1317	The loss of metalloproteinase activity is ensured by the absence of critical catalytic residues, the filling of the substrate groove, and the steric hindrance by the cysteine-rich domain.
19692335	6	18	theme	groove	1312:1317	arg1	absence					1243:1249	the absence	1239:1249	the absence of critical catalytic residues	1239:1280	The loss of metalloproteinase activity is ensured by the absence of critical catalytic residues, the filling of the substrate groove, and the steric hindrance by the cysteine-rich domain.
19692335	6	18	theme	groove	1312:1317	arg1	hindrance					1335:1343	the steric hindrance	1324:1343	the steric hindrance	1324:1343	The loss of metalloproteinase activity is ensured by the absence of critical catalytic residues, the filling of the substrate groove, and the steric hindrance by the cysteine-rich domain.
19692335	0	19	theme	metalloproteinase	136:152	arg1	metalloproteinase-22					67:86	metalloproteinase-22	67:86	metalloproteinase-22 (ADAM22)	67:95	Structural characterization of the ectodomain of a disintegrin and metalloproteinase-22 (ADAM22), a neural adhesion receptor instead of metalloproteinase: insights on ADAM function.
19692335	0	19	theme	metalloproteinase	136:152	arg1	metalloproteinase					136:152	metalloproteinase	136:152	a disintegrin and metalloproteinase-22 (ADAM22), a neural adhesion receptor instead of metalloproteinase	49:152	Structural characterization of the ectodomain of a disintegrin and metalloproteinase-22 (ADAM22), a neural adhesion receptor instead of metalloproteinase: insights on ADAM function.
19692335	0	19	theme	metalloproteinase	136:152	arg1	ectodomain					35:44	the ectodomain	31:44	the ectodomain of a disintegrin and metalloproteinase-22 (ADAM22), a neural adhesion receptor instead of metalloproteinase	31:152	Structural characterization of the ectodomain of a disintegrin and metalloproteinase-22 (ADAM22), a neural adhesion receptor instead of metalloproteinase: insights on ADAM function.
19692335	0	19	theme	metalloproteinase	136:152	arg1	disintegrin					51:61	a disintegrin	49:61	a disintegrin	49:61	Structural characterization of the ectodomain of a disintegrin and metalloproteinase-22 (ADAM22), a neural adhesion receptor instead of metalloproteinase: insights on ADAM function.
19692335	5	20	theme	metalloproteinase-like	1029:1050	arg1	domain					1052:1057	the metalloproteinase-like domain	1025:1057	the metalloproteinase-like domain held in the concave face of a rigid module formed by the disintegrin, cysteine-rich, and epidermal growth factor-like domains	1025:1183	The crystal structure of the full ectodomain of mature human ADAM22 shows that it is a compact four-leaf clover with the metalloproteinase-like domain held in the concave face of a rigid module formed by the disintegrin, cysteine-rich, and epidermal growth factor-like domains.
19692335	3	21	theme	active	575:580	arg1	members					544:550	most members	539:550	most members of the ADAM family	539:569	Although most members of the ADAM family are active zinc metalloproteinases, 8 of 21 ADAMs lack functional metalloproteinase domains and are implicated in protein-protein interactions instead of membrane protein ectodomain shedding.
19692335	3	21	theme	active	575:580	arg1	metalloproteinases					587:604	active zinc metalloproteinases	575:604	active zinc metalloproteinases	575:604	Although most members of the ADAM family are active zinc metalloproteinases, 8 of 21 ADAMs lack functional metalloproteinase domains and are implicated in protein-protein interactions instead of membrane protein ectodomain shedding.
19692335	8	22	theme	movement	1787:1794	arg1	possibility					1764:1774	the possibility	1760:1774	the possibility of modular movement of ADAM22 and other ADAMs	1760:1820	The metalloproteinase-like domain contacts the rest of ADAM22 with discontinuous, hydrophilic, and poorly complemented interactions, suggesting the possibility of modular movement of ADAM22 and other ADAMs.
19692335	6	23	theme	metalloproteinase	1198:1214	arg1	activity					1216:1223	metalloproteinase activity	1198:1223	metalloproteinase activity	1198:1223	The loss of metalloproteinase activity is ensured by the absence of critical catalytic residues, the filling of the substrate groove, and the steric hindrance by the cysteine-rich domain.
19692335	8	24	theme	ADAM22	1799:1804	arg1	movement					1787:1794	modular movement	1779:1794	modular movement of ADAM22 and other ADAMs	1779:1820	The metalloproteinase-like domain contacts the rest of ADAM22 with discontinuous, hydrophilic, and poorly complemented interactions, suggesting the possibility of modular movement of ADAM22 and other ADAMs.
19692335	7	25	theme	disintegrin	1579:1589	arg1	domain					1591:1596	the disintegrin domain	1575:1596	the disintegrin domain	1575:1596	The structure, combined with calorimetric experiments, suggests distinct roles of three putative calcium ions bound to ADAM22, with one in the metalloproteinase-like domain being regulatory and two in the disintegrin domain being structural.
19692335	8	26	theme	other	1810:1814	arg1	ADAMs					1816:1820	other ADAMs	1810:1820	other ADAMs	1810:1820	The metalloproteinase-like domain contacts the rest of ADAM22 with discontinuous, hydrophilic, and poorly complemented interactions, suggesting the possibility of modular movement of ADAM22 and other ADAMs.
19692335	6	27	theme	cysteine-rich	1352:1364	arg1	domain					1366:1371	the cysteine-rich domain	1348:1371	the cysteine-rich domain	1348:1371	The loss of metalloproteinase activity is ensured by the absence of critical catalytic residues, the filling of the substrate groove, and the steric hindrance by the cysteine-rich domain.
19692335	1	28	theme	several	335:341	arg1	members					343:349	several members	335:349	several members	335:349	ADAMs (a disintegrin and metalloproteinases) are a family of multidomain transmembrane glycoproteins with diverse roles in physiology and diseases, with several members being drug targets for cancer and inflammation therapies.
19692335	4	29	theme	non-proteinase	775:788	arg1	ADAMs					790:794	such non-proteinase ADAMs	770:794	such non-proteinase ADAMs	770:794	One of such non-proteinase ADAMs, ADAM22, acts as a receptor on the surface of the postsynaptic neuron to regulate synaptic signal transmission.
19692335	5	30	theme	ADAM22	969:974	arg1	ADAM22					969:974	mature human ADAM22	956:974	mature human ADAM22	956:974	The crystal structure of the full ectodomain of mature human ADAM22 shows that it is a compact four-leaf clover with the metalloproteinase-like domain held in the concave face of a rigid module formed by the disintegrin, cysteine-rich, and epidermal growth factor-like domains.
19692335	5	30	theme	ADAM22	969:974	arg1	ectodomain					942:951	the full ectodomain	933:951	the full ectodomain of mature human ADAM22	933:974	The crystal structure of the full ectodomain of mature human ADAM22 shows that it is a compact four-leaf clover with the metalloproteinase-like domain held in the concave face of a rigid module formed by the disintegrin, cysteine-rich, and epidermal growth factor-like domains.
19692335	6	31	theme	steric	1328:1333	arg1	hindrance					1335:1343	the steric hindrance	1324:1343	the steric hindrance	1324:1343	The loss of metalloproteinase activity is ensured by the absence of critical catalytic residues, the filling of the substrate groove, and the steric hindrance by the cysteine-rich domain.
19692335	5	32	theme	module	1095:1100	arg1	face					1079:1082	the concave face	1067:1082	the concave face of a rigid module formed by the disintegrin, cysteine-rich, and epidermal growth factor-like domains	1067:1183	The crystal structure of the full ectodomain of mature human ADAM22 shows that it is a compact four-leaf clover with the metalloproteinase-like domain held in the concave face of a rigid module formed by the disintegrin, cysteine-rich, and epidermal growth factor-like domains.
19692335	2	33	theme	extracellular	446:458	arg1	segment					460:466	the ADAM extracellular segment	437:466	the ADAM extracellular segment	437:466	The spatial organization of the ADAM extracellular segment and its influence on the function of ADAMs have been unclear.
19692335	0	34	theme	Structural	0:9	arg1	characterization					11:26	Structural characterization	0:26	Structural characterization of the ectodomain of a disintegrin and metalloproteinase-22 (ADAM22), a neural adhesion receptor instead of metalloproteinase: insights on ADAM function.	0:180	Structural characterization of the ectodomain of a disintegrin and metalloproteinase-22 (ADAM22), a neural adhesion receptor instead of metalloproteinase: insights on ADAM function.
19692335	5	35	theme	growth	1158:1163	arg1	domains					1177:1183	the disintegrin, cysteine-rich, and epidermal growth factor-like domains	1112:1183	the disintegrin, cysteine-rich, and epidermal growth factor-like domains	1112:1183	The crystal structure of the full ectodomain of mature human ADAM22 shows that it is a compact four-leaf clover with the metalloproteinase-like domain held in the concave face of a rigid module formed by the disintegrin, cysteine-rich, and epidermal growth factor-like domains.
19692335	5	36	theme	ectodomain	942:951	arg1	structure					920:928	The crystal structure	908:928	The crystal structure of the full ectodomain of mature human ADAM22	908:974	The crystal structure of the full ectodomain of mature human ADAM22 shows that it is a compact four-leaf clover with the metalloproteinase-like domain held in the concave face of a rigid module formed by the disintegrin, cysteine-rich, and epidermal growth factor-like domains.
19692335	7	37	theme	metalloproteinase-like	1517:1538	arg1	domain					1540:1545	the metalloproteinase-like domain	1513:1545	the metalloproteinase-like domain	1513:1545	The structure, combined with calorimetric experiments, suggests distinct roles of three putative calcium ions bound to ADAM22, with one in the metalloproteinase-like domain being regulatory and two in the disintegrin domain being structural.
19692335	1	38	theme	diverse	288:294	arg1	roles					296:300	diverse roles	288:300	diverse roles in physiology and diseases	288:327	ADAMs (a disintegrin and metalloproteinases) are a family of multidomain transmembrane glycoproteins with diverse roles in physiology and diseases, with several members being drug targets for cancer and inflammation therapies.
19692335	5	39	theme	mature	956:961	arg1	ADAM22					969:974	mature human ADAM22	956:974	mature human ADAM22	956:974	The crystal structure of the full ectodomain of mature human ADAM22 shows that it is a compact four-leaf clover with the metalloproteinase-like domain held in the concave face of a rigid module formed by the disintegrin, cysteine-rich, and epidermal growth factor-like domains.
19692335	3	40	theme	metalloproteinase	637:653	arg1	domains					655:661	functional metalloproteinase domains	626:661	functional metalloproteinase domains	626:661	Although most members of the ADAM family are active zinc metalloproteinases, 8 of 21 ADAMs lack functional metalloproteinase domains and are implicated in protein-protein interactions instead of membrane protein ectodomain shedding.
19692335	0	41	theme	ectodomain	35:44	arg1	characterization					11:26	Structural characterization	0:26	Structural characterization of the ectodomain of a disintegrin and metalloproteinase-22 (ADAM22), a neural adhesion receptor instead of metalloproteinase: insights on ADAM function.	0:180	Structural characterization of the ectodomain of a disintegrin and metalloproteinase-22 (ADAM22), a neural adhesion receptor instead of metalloproteinase: insights on ADAM function.
19692335	5	42	theme	cysteine-rich	1129:1141	arg1	domains					1177:1183	the disintegrin, cysteine-rich, and epidermal growth factor-like domains	1112:1183	the disintegrin, cysteine-rich, and epidermal growth factor-like domains	1112:1183	The crystal structure of the full ectodomain of mature human ADAM22 shows that it is a compact four-leaf clover with the metalloproteinase-like domain held in the concave face of a rigid module formed by the disintegrin, cysteine-rich, and epidermal growth factor-like domains.
19692335	7	43	theme	ions	1479:1482	arg1	roles					1447:1451	distinct roles	1438:1451	distinct roles of three putative calcium ions bound to ADAM22	1438:1498	The structure, combined with calorimetric experiments, suggests distinct roles of three putative calcium ions bound to ADAM22, with one in the metalloproteinase-like domain being regulatory and two in the disintegrin domain being structural.
19692335	5	44	theme	compact	995:1001	arg1	clover					1013:1018	a compact four-leaf clover	993:1018	a compact four-leaf clover with the metalloproteinase-like domain held in the concave face of a rigid module formed by the disintegrin, cysteine-rich, and epidermal growth factor-like domains	993:1183	The crystal structure of the full ectodomain of mature human ADAM22 shows that it is a compact four-leaf clover with the metalloproteinase-like domain held in the concave face of a rigid module formed by the disintegrin, cysteine-rich, and epidermal growth factor-like domains.
19692335	5	44	theme	compact	995:1001	arg1	it					987:988	it	987:988	it	987:988	The crystal structure of the full ectodomain of mature human ADAM22 shows that it is a compact four-leaf clover with the metalloproteinase-like domain held in the concave face of a rigid module formed by the disintegrin, cysteine-rich, and epidermal growth factor-like domains.
19692335	2	45	from	organization	421:432	arg1	function					493:500	the function	489:500	the function of ADAMs	489:509	The spatial organization of the ADAM extracellular segment and its influence on the function of ADAMs have been unclear.
19692335	7	46	theme	putative	1462:1469	arg1	ions					1479:1482	three putative calcium ions	1456:1482	three putative calcium ions bound to ADAM22	1456:1498	The structure, combined with calorimetric experiments, suggests distinct roles of three putative calcium ions bound to ADAM22, with one in the metalloproteinase-like domain being regulatory and two in the disintegrin domain being structural.
19692335	4	47	theme	neuron	859:864	arg1	surface					831:837	the surface	827:837	the surface of the postsynaptic neuron	827:864	One of such non-proteinase ADAMs, ADAM22, acts as a receptor on the surface of the postsynaptic neuron to regulate synaptic signal transmission.
19692335	0	48	from	insights	155:162	arg1	function					172:179	ADAM function	167:179	ADAM function	167:179	Structural characterization of the ectodomain of a disintegrin and metalloproteinase-22 (ADAM22), a neural adhesion receptor instead of metalloproteinase: insights on ADAM function.
19692335	3	49	theme	protein-protein	685:699	arg1	interactions					701:712	protein-protein interactions	685:712	protein-protein interactions instead of membrane protein ectodomain shedding	685:760	Although most members of the ADAM family are active zinc metalloproteinases, 8 of 21 ADAMs lack functional metalloproteinase domains and are implicated in protein-protein interactions instead of membrane protein ectodomain shedding.
19692335	6	50	theme	residues	1273:1280	arg1	filling					1287:1293	the filling	1283:1293	the filling of the substrate groove	1283:1317	The loss of metalloproteinase activity is ensured by the absence of critical catalytic residues, the filling of the substrate groove, and the steric hindrance by the cysteine-rich domain.
19692335	6	50	theme	residues	1273:1280	arg1	absence					1243:1249	the absence	1239:1249	the absence of critical catalytic residues	1239:1280	The loss of metalloproteinase activity is ensured by the absence of critical catalytic residues, the filling of the substrate groove, and the steric hindrance by the cysteine-rich domain.
19692335	6	50	theme	residues	1273:1280	arg1	hindrance					1335:1343	the steric hindrance	1324:1343	the steric hindrance	1324:1343	The loss of metalloproteinase activity is ensured by the absence of critical catalytic residues, the filling of the substrate groove, and the steric hindrance by the cysteine-rich domain.
19692335	3	51	theme	most	539:542	arg1	metalloproteinases					587:604	active zinc metalloproteinases	575:604	active zinc metalloproteinases	575:604	Although most members of the ADAM family are active zinc metalloproteinases, 8 of 21 ADAMs lack functional metalloproteinase domains and are implicated in protein-protein interactions instead of membrane protein ectodomain shedding.
19692335	3	51	theme	most	539:542	arg1	members					544:550	most members	539:550	most members of the ADAM family	539:569	Although most members of the ADAM family are active zinc metalloproteinases, 8 of 21 ADAMs lack functional metalloproteinase domains and are implicated in protein-protein interactions instead of membrane protein ectodomain shedding.
19692335	1	52	theme	multidomain	243:253	arg1	glycoproteins					269:281	multidomain transmembrane glycoproteins	243:281	multidomain transmembrane glycoproteins with diverse roles in physiology and diseases	243:327	ADAMs (a disintegrin and metalloproteinases) are a family of multidomain transmembrane glycoproteins with diverse roles in physiology and diseases, with several members being drug targets for cancer and inflammation therapies.
19692335	8	53	with	contacts	1650:1657	arg1	interactions					1735:1746	discontinuous, hydrophilic, and poorly complemented interactions	1683:1746	discontinuous, hydrophilic, and poorly complemented interactions	1683:1746	The metalloproteinase-like domain contacts the rest of ADAM22 with discontinuous, hydrophilic, and poorly complemented interactions, suggesting the possibility of modular movement of ADAM22 and other ADAMs.
19692335	3	54	theme	ectodomain	742:751	arg1	shedding					753:760	membrane protein ectodomain shedding	725:760	protein-protein interactions instead of membrane protein ectodomain shedding	685:760	Although most members of the ADAM family are active zinc metalloproteinases, 8 of 21 ADAMs lack functional metalloproteinase domains and are implicated in protein-protein interactions instead of membrane protein ectodomain shedding.
19692335	6	55	theme	critical	1254:1261	arg1	residues					1273:1280	critical catalytic residues	1254:1280	critical catalytic residues	1254:1280	The loss of metalloproteinase activity is ensured by the absence of critical catalytic residues, the filling of the substrate groove, and the steric hindrance by the cysteine-rich domain.
19692335	7	56	theme	distinct	1438:1445	arg1	roles					1447:1451	distinct roles	1438:1451	distinct roles of three putative calcium ions bound to ADAM22	1438:1498	The structure, combined with calorimetric experiments, suggests distinct roles of three putative calcium ions bound to ADAM22, with one in the metalloproteinase-like domain being regulatory and two in the disintegrin domain being structural.
19692335	9	57	theme	shedding	1937:1944	arg1	activities					1946:1955	shedding activities	1937:1955	shedding activities	1937:1955	The ADAM22 structure provides a framework for understanding how different ADAMs exert their adhesive function and shedding activities.
19692335	3	58	theme	membrane	725:732	arg1	shedding					753:760	membrane protein ectodomain shedding	725:760	protein-protein interactions instead of membrane protein ectodomain shedding	685:760	Although most members of the ADAM family are active zinc metalloproteinases, 8 of 21 ADAMs lack functional metalloproteinase domains and are implicated in protein-protein interactions instead of membrane protein ectodomain shedding.
19692335	3	59	theme	ADAM	559:562	arg1	family					564:569	the ADAM family	555:569	the ADAM family	555:569	Although most members of the ADAM family are active zinc metalloproteinases, 8 of 21 ADAMs lack functional metalloproteinase domains and are implicated in protein-protein interactions instead of membrane protein ectodomain shedding.
19692335	5	60	theme	disintegrin	1116:1126	arg1	domains					1177:1183	the disintegrin, cysteine-rich, and epidermal growth factor-like domains	1112:1183	the disintegrin, cysteine-rich, and epidermal growth factor-like domains	1112:1183	The crystal structure of the full ectodomain of mature human ADAM22 shows that it is a compact four-leaf clover with the metalloproteinase-like domain held in the concave face of a rigid module formed by the disintegrin, cysteine-rich, and epidermal growth factor-like domains.
19692335	1	61	with	glycoproteins	269:281	arg1	roles					296:300	diverse roles	288:300	diverse roles in physiology and diseases	288:327	ADAMs (a disintegrin and metalloproteinases) are a family of multidomain transmembrane glycoproteins with diverse roles in physiology and diseases, with several members being drug targets for cancer and inflammation therapies.
19692335	5	62	theme	concave	1071:1077	arg1	face					1079:1082	the concave face	1067:1082	the concave face of a rigid module formed by the disintegrin, cysteine-rich, and epidermal growth factor-like domains	1067:1183	The crystal structure of the full ectodomain of mature human ADAM22 shows that it is a compact four-leaf clover with the metalloproteinase-like domain held in the concave face of a rigid module formed by the disintegrin, cysteine-rich, and epidermal growth factor-like domains.
19692335	3	63	theme	zinc	582:585	arg1	members					544:550	most members	539:550	most members of the ADAM family	539:569	Although most members of the ADAM family are active zinc metalloproteinases, 8 of 21 ADAMs lack functional metalloproteinase domains and are implicated in protein-protein interactions instead of membrane protein ectodomain shedding.
19692335	3	63	theme	zinc	582:585	arg1	metalloproteinases					587:604	active zinc metalloproteinases	575:604	active zinc metalloproteinases	575:604	Although most members of the ADAM family are active zinc metalloproteinases, 8 of 21 ADAMs lack functional metalloproteinase domains and are implicated in protein-protein interactions instead of membrane protein ectodomain shedding.
19692335	6	64	theme	substrate	1302:1310	arg1	groove					1312:1317	the substrate groove	1298:1317	the substrate groove	1298:1317	The loss of metalloproteinase activity is ensured by the absence of critical catalytic residues, the filling of the substrate groove, and the steric hindrance by the cysteine-rich domain.
19692335	1	65	gly	glycoproteins	269:281	arg1	glycoproteins					269:281	multidomain transmembrane glycoproteins	243:281	multidomain transmembrane glycoproteins with diverse roles in physiology and diseases	243:327	ADAMs (a disintegrin and metalloproteinases) are a family of multidomain transmembrane glycoproteins with diverse roles in physiology and diseases, with several members being drug targets for cancer and inflammation therapies.
19692335	5	66	theme	crystal	912:918	arg1	structure					920:928	The crystal structure	908:928	The crystal structure of the full ectodomain of mature human ADAM22	908:974	The crystal structure of the full ectodomain of mature human ADAM22 shows that it is a compact four-leaf clover with the metalloproteinase-like domain held in the concave face of a rigid module formed by the disintegrin, cysteine-rich, and epidermal growth factor-like domains.
19692335	4	67	theme	signal	887:892	arg1	transmission					894:905	synaptic signal transmission	878:905	synaptic signal transmission	878:905	One of such non-proteinase ADAMs, ADAM22, acts as a receptor on the surface of the postsynaptic neuron to regulate synaptic signal transmission.
19692335	6	68	theme	activity	1216:1223	arg1	loss					1190:1193	The loss	1186:1193	The loss of metalloproteinase activity	1186:1223	The loss of metalloproteinase activity is ensured by the absence of critical catalytic residues, the filling of the substrate groove, and the steric hindrance by the cysteine-rich domain.
19692335	8	69	theme	modular	1779:1785	arg1	movement					1787:1794	modular movement	1779:1794	modular movement of ADAM22 and other ADAMs	1779:1820	The metalloproteinase-like domain contacts the rest of ADAM22 with discontinuous, hydrophilic, and poorly complemented interactions, suggesting the possibility of modular movement of ADAM22 and other ADAMs.
19692335	0	70	theme	metalloproteinase-22	67:86	arg1	metalloproteinase-22					67:86	metalloproteinase-22	67:86	metalloproteinase-22 (ADAM22)	67:95	Structural characterization of the ectodomain of a disintegrin and metalloproteinase-22 (ADAM22), a neural adhesion receptor instead of metalloproteinase: insights on ADAM function.
19692335	0	70	theme	metalloproteinase-22	67:86	arg1	metalloproteinase					136:152	metalloproteinase	136:152	a disintegrin and metalloproteinase-22 (ADAM22), a neural adhesion receptor instead of metalloproteinase	49:152	Structural characterization of the ectodomain of a disintegrin and metalloproteinase-22 (ADAM22), a neural adhesion receptor instead of metalloproteinase: insights on ADAM function.
19692335	0	70	theme	metalloproteinase-22	67:86	arg1	ectodomain					35:44	the ectodomain	31:44	the ectodomain of a disintegrin and metalloproteinase-22 (ADAM22), a neural adhesion receptor instead of metalloproteinase	31:152	Structural characterization of the ectodomain of a disintegrin and metalloproteinase-22 (ADAM22), a neural adhesion receptor instead of metalloproteinase: insights on ADAM function.
19692335	0	70	theme	metalloproteinase-22	67:86	arg1	disintegrin					51:61	a disintegrin	49:61	a disintegrin	49:61	Structural characterization of the ectodomain of a disintegrin and metalloproteinase-22 (ADAM22), a neural adhesion receptor instead of metalloproteinase: insights on ADAM function.
19692335	8	71	theme	ADAMs	1816:1820	arg1	movement					1787:1794	modular movement	1779:1794	modular movement of ADAM22 and other ADAMs	1779:1820	The metalloproteinase-like domain contacts the rest of ADAM22 with discontinuous, hydrophilic, and poorly complemented interactions, suggesting the possibility of modular movement of ADAM22 and other ADAMs.
19692335	5	72	theme	human	963:967	arg1	ADAM22					969:974	mature human ADAM22	956:974	mature human ADAM22	956:974	The crystal structure of the full ectodomain of mature human ADAM22 shows that it is a compact four-leaf clover with the metalloproteinase-like domain held in the concave face of a rigid module formed by the disintegrin, cysteine-rich, and epidermal growth factor-like domains.
19692335	4	73	theme	such	770:773	arg1	ADAMs					790:794	such non-proteinase ADAMs	770:794	such non-proteinase ADAMs	770:794	One of such non-proteinase ADAMs, ADAM22, acts as a receptor on the surface of the postsynaptic neuron to regulate synaptic signal transmission.
19692335	0	74	theme	neural	100:105	arg1	receptor					116:123	a neural adhesion receptor	98:123	a neural adhesion receptor	98:123	Structural characterization of the ectodomain of a disintegrin and metalloproteinase-22 (ADAM22), a neural adhesion receptor instead of metalloproteinase: insights on ADAM function.
19692335	0	74	theme	neural	100:105	arg1	metalloproteinase-22					67:86	metalloproteinase-22	67:86	metalloproteinase-22 (ADAM22)	67:95	Structural characterization of the ectodomain of a disintegrin and metalloproteinase-22 (ADAM22), a neural adhesion receptor instead of metalloproteinase: insights on ADAM function.
19692335	1	75	theme	drug	357:360	arg1	targets					362:368	drug targets	357:368	drug targets for cancer and inflammation therapies	357:406	ADAMs (a disintegrin and metalloproteinases) are a family of multidomain transmembrane glycoproteins with diverse roles in physiology and diseases, with several members being drug targets for cancer and inflammation therapies.
19692335	2	76	theme	ADAMs	505:509	arg1	function					493:500	the function	489:500	the function of ADAMs	489:509	The spatial organization of the ADAM extracellular segment and its influence on the function of ADAMs have been unclear.
19692335	2	77	from	influence	476:484	arg1	function					493:500	the function	489:500	the function of ADAMs	489:509	The spatial organization of the ADAM extracellular segment and its influence on the function of ADAMs have been unclear.
19692335	4	78	theme	ADAMs	790:794	arg1	One					763:765	One	763:765	One	763:765	One of such non-proteinase ADAMs, ADAM22, acts as a receptor on the surface of the postsynaptic neuron to regulate synaptic signal transmission.
19692335	4	78	theme	ADAMs	790:794	arg1	receptor					815:822	a receptor	813:822	a receptor on the surface of the postsynaptic neuron	813:864	One of such non-proteinase ADAMs, ADAM22, acts as a receptor on the surface of the postsynaptic neuron to regulate synaptic signal transmission.
19692335	4	78	theme	ADAMs	790:794	arg1	ADAM22					797:802	ADAM22	797:802	ADAM22	797:802	One of such non-proteinase ADAMs, ADAM22, acts as a receptor on the surface of the postsynaptic neuron to regulate synaptic signal transmission.
19692335	4	78	theme	ADAMs	790:794	arg1	ADAMs					790:794	such non-proteinase ADAMs	770:794	such non-proteinase ADAMs	770:794	One of such non-proteinase ADAMs, ADAM22, acts as a receptor on the surface of the postsynaptic neuron to regulate synaptic signal transmission.
19692335	5	79	theme	full	937:940	arg1	ADAM22					969:974	mature human ADAM22	956:974	mature human ADAM22	956:974	The crystal structure of the full ectodomain of mature human ADAM22 shows that it is a compact four-leaf clover with the metalloproteinase-like domain held in the concave face of a rigid module formed by the disintegrin, cysteine-rich, and epidermal growth factor-like domains.
19692335	5	79	theme	full	937:940	arg1	ectodomain					942:951	the full ectodomain	933:951	the full ectodomain of mature human ADAM22	933:974	The crystal structure of the full ectodomain of mature human ADAM22 shows that it is a compact four-leaf clover with the metalloproteinase-like domain held in the concave face of a rigid module formed by the disintegrin, cysteine-rich, and epidermal growth factor-like domains.
19692335	5	80	theme	rigid	1089:1093	arg1	module					1095:1100	a rigid module	1087:1100	a rigid module formed by the disintegrin, cysteine-rich, and epidermal growth factor-like domains	1087:1183	The crystal structure of the full ectodomain of mature human ADAM22 shows that it is a compact four-leaf clover with the metalloproteinase-like domain held in the concave face of a rigid module formed by the disintegrin, cysteine-rich, and epidermal growth factor-like domains.
19692335	2	81	theme	ADAM	441:444	arg1	segment					460:466	the ADAM extracellular segment	437:466	the ADAM extracellular segment	437:466	The spatial organization of the ADAM extracellular segment and its influence on the function of ADAMs have been unclear.
19692335	5	82	theme	factor-like	1165:1175	arg1	domains					1177:1183	the disintegrin, cysteine-rich, and epidermal growth factor-like domains	1112:1183	the disintegrin, cysteine-rich, and epidermal growth factor-like domains	1112:1183	The crystal structure of the full ectodomain of mature human ADAM22 shows that it is a compact four-leaf clover with the metalloproteinase-like domain held in the concave face of a rigid module formed by the disintegrin, cysteine-rich, and epidermal growth factor-like domains.
19692335	9	83	theme	ADAM22	1827:1832	arg1	structure					1834:1842	The ADAM22 structure	1823:1842	The ADAM22 structure	1823:1842	The ADAM22 structure provides a framework for understanding how different ADAMs exert their adhesive function and shedding activities.
19692335	3	84	theme	functional	626:635	arg1	domains					655:661	functional metalloproteinase domains	626:661	functional metalloproteinase domains	626:661	Although most members of the ADAM family are active zinc metalloproteinases, 8 of 21 ADAMs lack functional metalloproteinase domains and are implicated in protein-protein interactions instead of membrane protein ectodomain shedding.
19692335	2	85	theme	spatial	413:419	arg1	unclear					521:527	unclear	521:527	unclear	521:527	The spatial organization of the ADAM extracellular segment and its influence on the function of ADAMs have been unclear.
19692335	2	85	theme	spatial	413:419	arg1	organization					421:432	The spatial organization	409:432	The spatial organization of the ADAM extracellular segment	409:466	The spatial organization of the ADAM extracellular segment and its influence on the function of ADAMs have been unclear.
19692335	4	86	from	receptor	815:822	arg1	surface					831:837	the surface	827:837	the surface of the postsynaptic neuron	827:864	One of such non-proteinase ADAMs, ADAM22, acts as a receptor on the surface of the postsynaptic neuron to regulate synaptic signal transmission.
19692335	5	87	theme	four-leaf	1003:1011	arg1	clover					1013:1018	a compact four-leaf clover	993:1018	a compact four-leaf clover with the metalloproteinase-like domain held in the concave face of a rigid module formed by the disintegrin, cysteine-rich, and epidermal growth factor-like domains	993:1183	The crystal structure of the full ectodomain of mature human ADAM22 shows that it is a compact four-leaf clover with the metalloproteinase-like domain held in the concave face of a rigid module formed by the disintegrin, cysteine-rich, and epidermal growth factor-like domains.
19692335	5	87	theme	four-leaf	1003:1011	arg1	it					987:988	it	987:988	it	987:988	The crystal structure of the full ectodomain of mature human ADAM22 shows that it is a compact four-leaf clover with the metalloproteinase-like domain held in the concave face of a rigid module formed by the disintegrin, cysteine-rich, and epidermal growth factor-like domains.
19692335	1	88	dep	ADAMs	182:186	arg1	metalloproteinases					207:224	metalloproteinases	207:224	metalloproteinases	207:224	ADAMs (a disintegrin and metalloproteinases) are a family of multidomain transmembrane glycoproteins with diverse roles in physiology and diseases, with several members being drug targets for cancer and inflammation therapies.
19692335	1	88	dep	ADAMs	182:186	arg1	disintegrin					191:201	a disintegrin	189:201	a disintegrin	189:201	ADAMs (a disintegrin and metalloproteinases) are a family of multidomain transmembrane glycoproteins with diverse roles in physiology and diseases, with several members being drug targets for cancer and inflammation therapies.
19692335	0	89	theme	disintegrin	51:61	arg1	metalloproteinase-22					67:86	metalloproteinase-22	67:86	metalloproteinase-22 (ADAM22)	67:95	Structural characterization of the ectodomain of a disintegrin and metalloproteinase-22 (ADAM22), a neural adhesion receptor instead of metalloproteinase: insights on ADAM function.
19692335	0	89	theme	disintegrin	51:61	arg1	metalloproteinase					136:152	metalloproteinase	136:152	a disintegrin and metalloproteinase-22 (ADAM22), a neural adhesion receptor instead of metalloproteinase	49:152	Structural characterization of the ectodomain of a disintegrin and metalloproteinase-22 (ADAM22), a neural adhesion receptor instead of metalloproteinase: insights on ADAM function.
19692335	0	89	theme	disintegrin	51:61	arg1	ectodomain					35:44	the ectodomain	31:44	the ectodomain of a disintegrin and metalloproteinase-22 (ADAM22), a neural adhesion receptor instead of metalloproteinase	31:152	Structural characterization of the ectodomain of a disintegrin and metalloproteinase-22 (ADAM22), a neural adhesion receptor instead of metalloproteinase: insights on ADAM function.
19692335	0	89	theme	disintegrin	51:61	arg1	disintegrin					51:61	a disintegrin	49:61	a disintegrin	49:61	Structural characterization of the ectodomain of a disintegrin and metalloproteinase-22 (ADAM22), a neural adhesion receptor instead of metalloproteinase: insights on ADAM function.
19692335	7	90	from	two	1568:1570	arg1	domain					1591:1596	the disintegrin domain	1575:1596	the disintegrin domain	1575:1596	The structure, combined with calorimetric experiments, suggests distinct roles of three putative calcium ions bound to ADAM22, with one in the metalloproteinase-like domain being regulatory and two in the disintegrin domain being structural.
19692335	2	91	theme	segment	460:466	arg1	unclear					521:527	unclear	521:527	unclear	521:527	The spatial organization of the ADAM extracellular segment and its influence on the function of ADAMs have been unclear.
19692335	2	91	theme	segment	460:466	arg1	influence					476:484	its influence	472:484	its influence on the function of ADAMs	472:509	The spatial organization of the ADAM extracellular segment and its influence on the function of ADAMs have been unclear.
19692335	2	91	theme	segment	460:466	arg1	organization					421:432	The spatial organization	409:432	The spatial organization of the ADAM extracellular segment	409:466	The spatial organization of the ADAM extracellular segment and its influence on the function of ADAMs have been unclear.
19692335	5	92	theme	epidermal	1148:1156	arg1	growth					1158:1163	epidermal growth	1148:1163	epidermal growth	1148:1163	The crystal structure of the full ectodomain of mature human ADAM22 shows that it is a compact four-leaf clover with the metalloproteinase-like domain held in the concave face of a rigid module formed by the disintegrin, cysteine-rich, and epidermal growth factor-like domains.
19692335	8	93	theme	ADAM22	1671:1676	arg1	rest					1663:1666	the rest	1659:1666	the rest of ADAM22	1659:1676	The metalloproteinase-like domain contacts the rest of ADAM22 with discontinuous, hydrophilic, and poorly complemented interactions, suggesting the possibility of modular movement of ADAM22 and other ADAMs.
19692335	0	94	dep	characterization	11:26	arg1	insights					155:162	insights	155:162	Structural characterization of the ectodomain of a disintegrin and metalloproteinase-22 (ADAM22), a neural adhesion receptor instead of metalloproteinase: insights on ADAM function.	0:180	Structural characterization of the ectodomain of a disintegrin and metalloproteinase-22 (ADAM22), a neural adhesion receptor instead of metalloproteinase: insights on ADAM function.
19692335	9	95	theme	different	1887:1895	arg1	ADAMs					1897:1901	different ADAMs	1887:1901	different ADAMs	1887:1901	The ADAM22 structure provides a framework for understanding how different ADAMs exert their adhesive function and shedding activities.
19692335	1	96	dep	cancer	374:379	arg1	therapies					398:406	therapies	398:406	therapies	398:406	ADAMs (a disintegrin and metalloproteinases) are a family of multidomain transmembrane glycoproteins with diverse roles in physiology and diseases, with several members being drug targets for cancer and inflammation therapies.
19692335	8	97	theme	discontinuous	1683:1695	arg1	interactions					1735:1746	discontinuous, hydrophilic, and poorly complemented interactions	1683:1746	discontinuous, hydrophilic, and poorly complemented interactions	1683:1746	The metalloproteinase-like domain contacts the rest of ADAM22 with discontinuous, hydrophilic, and poorly complemented interactions, suggesting the possibility of modular movement of ADAM22 and other ADAMs.
17662946	0	0	theme	stem	71:74	arg1	factor					81:86	stem cell factor	71:86	stem cell factor	71:86	Structural basis for activation of the receptor tyrosine kinase KIT by stem cell factor.
17662946	7	1	theme	key	844:846	arg1	hallmarks					848:856	key hallmarks	844:856	key hallmarks of KIT structures	844:874	Since key hallmarks of KIT structures, ligand-induced receptor dimerization, and the critical residues in the D4-D4 interface, are conserved in other receptors, the mechanism of KIT stimulation unveiled in this report may apply for other receptor activation.
17662946	1	2	theme	tyrosine	204:211	arg1	activation					220:229	tyrosine kinase activation	204:229	tyrosine kinase activation	204:229	Stem Cell Factor (SCF) initiates its multiple cellular responses by binding to the ectodomain of KIT, resulting in tyrosine kinase activation.
17662946	5	3	theme	KIT	664:666	arg1	activation					668:677	KIT activation	664:677	KIT activation	664:677	Experiments with cultured cells show that KIT activation is compromised by point mutations in amino acids critical for D4-D4 interaction.
17662946	4	4	theme	Receptor	455:462	arg1	dimerization					464:475	Receptor dimerization	455:475	Receptor dimerization	455:475	Receptor dimerization is followed by conformational changes that enable lateral interactions between membrane proximal Ig-like domains D4 and D5 of two KIT molecules.
17662946	1	5	theme	multiple	126:133	arg1	responses					144:152	its multiple cellular responses	122:152	its multiple cellular responses	122:152	Stem Cell Factor (SCF) initiates its multiple cellular responses by binding to the ectodomain of KIT, resulting in tyrosine kinase activation.
17662946	1	6	theme	kinase	213:218	arg1	activation					220:229	tyrosine kinase activation	204:229	tyrosine kinase activation	204:229	Stem Cell Factor (SCF) initiates its multiple cellular responses by binding to the ectodomain of KIT, resulting in tyrosine kinase activation.
17662946	7	7	theme	critical	923:930	arg1	residues					932:939	the critical residues	919:939	the critical residues in the D4-D4 interface	919:962	Since key hallmarks of KIT structures, ligand-induced receptor dimerization, and the critical residues in the D4-D4 interface, are conserved in other receptors, the mechanism of KIT stimulation unveiled in this report may apply for other receptor activation.
17662946	7	7	theme	critical	923:930	arg1	structures					865:874	KIT structures	861:874	KIT structures	861:874	Since key hallmarks of KIT structures, ligand-induced receptor dimerization, and the critical residues in the D4-D4 interface, are conserved in other receptors, the mechanism of KIT stimulation unveiled in this report may apply for other receptor activation.
17662946	2	8	theme	crystal	248:254	arg1	structure					256:264	the crystal structure	244:264	the crystal structure of the entire ectodomain of KIT before and after SCF stimulation	244:329	We describe the crystal structure of the entire ectodomain of KIT before and after SCF stimulation.
17662946	4	9	theme	molecules	611:619	arg1	molecules					611:619	two KIT molecules	603:619	two KIT molecules	603:619	Receptor dimerization is followed by conformational changes that enable lateral interactions between membrane proximal Ig-like domains D4 and D5 of two KIT molecules.
17662946	4	9	theme	molecules	611:619	arg1	domains					582:588	membrane proximal Ig-like domains D4 and D5	556:598	membrane proximal Ig-like domains D4 and D5 of two KIT molecules	556:619	Receptor dimerization is followed by conformational changes that enable lateral interactions between membrane proximal Ig-like domains D4 and D5 of two KIT molecules.
17662946	4	9	theme	molecules	611:619	arg1	D5					597:598	D5	597:598	D5	597:598	Receptor dimerization is followed by conformational changes that enable lateral interactions between membrane proximal Ig-like domains D4 and D5 of two KIT molecules.
17662946	4	9	theme	molecules	611:619	arg1	D4					590:591	D4	590:591	D4	590:591	Receptor dimerization is followed by conformational changes that enable lateral interactions between membrane proximal Ig-like domains D4 and D5 of two KIT molecules.
17662946	4	10	theme	membrane	556:563	arg1	molecules					611:619	two KIT molecules	603:619	two KIT molecules	603:619	Receptor dimerization is followed by conformational changes that enable lateral interactions between membrane proximal Ig-like domains D4 and D5 of two KIT molecules.
17662946	4	10	theme	membrane	556:563	arg1	domains					582:588	membrane proximal Ig-like domains D4 and D5	556:598	membrane proximal Ig-like domains D4 and D5 of two KIT molecules	556:619	Receptor dimerization is followed by conformational changes that enable lateral interactions between membrane proximal Ig-like domains D4 and D5 of two KIT molecules.
17662946	4	10	theme	membrane	556:563	arg1	D5					597:598	D5	597:598	D5	597:598	Receptor dimerization is followed by conformational changes that enable lateral interactions between membrane proximal Ig-like domains D4 and D5 of two KIT molecules.
17662946	4	10	theme	membrane	556:563	arg1	D4					590:591	D4	590:591	D4	590:591	Receptor dimerization is followed by conformational changes that enable lateral interactions between membrane proximal Ig-like domains D4 and D5 of two KIT molecules.
17662946	0	11	theme	cell	76:79	arg1	factor					81:86	stem cell factor	71:86	stem cell factor	71:86	Structural basis for activation of the receptor tyrosine kinase KIT by stem cell factor.
17662946	7	12	from	hallmarks	848:856	arg1	interface					954:962	the D4-D4 interface	944:962	the D4-D4 interface	944:962	Since key hallmarks of KIT structures, ligand-induced receptor dimerization, and the critical residues in the D4-D4 interface, are conserved in other receptors, the mechanism of KIT stimulation unveiled in this report may apply for other receptor activation.
17662946	7	13	from	dimerization	901:912	arg1	interface					954:962	the D4-D4 interface	944:962	the D4-D4 interface	944:962	Since key hallmarks of KIT structures, ligand-induced receptor dimerization, and the critical residues in the D4-D4 interface, are conserved in other receptors, the mechanism of KIT stimulation unveiled in this report may apply for other receptor activation.
17662946	5	14	theme	point	697:701	arg1	mutations					703:711	point mutations	697:711	point mutations in amino acids critical for D4-D4 interaction	697:757	Experiments with cultured cells show that KIT activation is compromised by point mutations in amino acids critical for D4-D4 interaction.
17662946	1	15	theme	cellular	135:142	arg1	responses					144:152	its multiple cellular responses	122:152	its multiple cellular responses	122:152	Stem Cell Factor (SCF) initiates its multiple cellular responses by binding to the ectodomain of KIT, resulting in tyrosine kinase activation.
17662946	0	16	theme	receptor	39:46	arg1	KIT					64:66	the receptor tyrosine kinase KIT	35:66	the receptor tyrosine kinase KIT	35:66	Structural basis for activation of the receptor tyrosine kinase KIT by stem cell factor.
17662946	7	17	theme	KIT	1016:1018	arg1	stimulation					1020:1030	KIT stimulation	1016:1030	KIT stimulation unveiled in this report	1016:1054	Since key hallmarks of KIT structures, ligand-induced receptor dimerization, and the critical residues in the D4-D4 interface, are conserved in other receptors, the mechanism of KIT stimulation unveiled in this report may apply for other receptor activation.
17662946	4	18	theme	KIT	607:609	arg1	molecules					611:619	two KIT molecules	603:619	two KIT molecules	603:619	Receptor dimerization is followed by conformational changes that enable lateral interactions between membrane proximal Ig-like domains D4 and D5 of two KIT molecules.
17662946	5	19	theme	critical	728:735	arg1	acids					722:726	amino acids	716:726	amino acids critical for D4-D4 interaction	716:757	Experiments with cultured cells show that KIT activation is compromised by point mutations in amino acids critical for D4-D4 interaction.
17662946	7	20	theme	stimulation	1020:1030	arg1	mechanism					1003:1011	the mechanism	999:1011	the mechanism of KIT stimulation unveiled in this report	999:1054	Since key hallmarks of KIT structures, ligand-induced receptor dimerization, and the critical residues in the D4-D4 interface, are conserved in other receptors, the mechanism of KIT stimulation unveiled in this report may apply for other receptor activation.
17662946	2	21	theme	entire	273:278	arg1	KIT					294:296	KIT	294:296	KIT	294:296	We describe the crystal structure of the entire ectodomain of KIT before and after SCF stimulation.
17662946	2	21	theme	entire	273:278	arg1	ectodomain					280:289	the entire ectodomain	269:289	the entire ectodomain of KIT	269:296	We describe the crystal structure of the entire ectodomain of KIT before and after SCF stimulation.
17662946	7	22	theme	receptor	892:899	arg1	dimerization					901:912	ligand-induced receptor dimerization	877:912	ligand-induced receptor dimerization	877:912	Since key hallmarks of KIT structures, ligand-induced receptor dimerization, and the critical residues in the D4-D4 interface, are conserved in other receptors, the mechanism of KIT stimulation unveiled in this report may apply for other receptor activation.
17662946	0	23	theme	Structural	0:9	arg1	basis					11:15	Structural basis	0:15	Structural basis for activation of the receptor tyrosine kinase KIT by stem cell factor.	0:87	Structural basis for activation of the receptor tyrosine kinase KIT by stem cell factor.
17662946	5	24	with	Experiments	622:632	arg1	cells					648:652	cultured cells	639:652	cultured cells	639:652	Experiments with cultured cells show that KIT activation is compromised by point mutations in amino acids critical for D4-D4 interaction.
17662946	4	25	theme	conformational	492:505	arg1	changes					507:513	conformational changes	492:513	conformational changes that enable lateral interactions between membrane proximal Ig-like domains D4 and D5 of two KIT molecules	492:619	Receptor dimerization is followed by conformational changes that enable lateral interactions between membrane proximal Ig-like domains D4 and D5 of two KIT molecules.
17662946	7	26	theme	ligand-induced	877:890	arg1	dimerization					901:912	ligand-induced receptor dimerization	877:912	ligand-induced receptor dimerization	877:912	Since key hallmarks of KIT structures, ligand-induced receptor dimerization, and the critical residues in the D4-D4 interface, are conserved in other receptors, the mechanism of KIT stimulation unveiled in this report may apply for other receptor activation.
17662946	4	27	theme	Ig-like	574:580	arg1	molecules					611:619	two KIT molecules	603:619	two KIT molecules	603:619	Receptor dimerization is followed by conformational changes that enable lateral interactions between membrane proximal Ig-like domains D4 and D5 of two KIT molecules.
17662946	4	27	theme	Ig-like	574:580	arg1	domains					582:588	membrane proximal Ig-like domains D4 and D5	556:598	membrane proximal Ig-like domains D4 and D5 of two KIT molecules	556:619	Receptor dimerization is followed by conformational changes that enable lateral interactions between membrane proximal Ig-like domains D4 and D5 of two KIT molecules.
17662946	4	27	theme	Ig-like	574:580	arg1	D5					597:598	D5	597:598	D5	597:598	Receptor dimerization is followed by conformational changes that enable lateral interactions between membrane proximal Ig-like domains D4 and D5 of two KIT molecules.
17662946	4	27	theme	Ig-like	574:580	arg1	D4					590:591	D4	590:591	D4	590:591	Receptor dimerization is followed by conformational changes that enable lateral interactions between membrane proximal Ig-like domains D4 and D5 of two KIT molecules.
17662946	6	28	theme	D5-D5	821:825	arg1	interface					827:835	the D5-D5 interface	817:835	the D5-D5 interface	817:835	Moreover, a variety of oncogenic mutations are mapped to the D5-D5 interface.
17662946	1	29	theme	Stem	89:92	arg1	SCF					107:109	SCF	107:109	SCF	107:109	Stem Cell Factor (SCF) initiates its multiple cellular responses by binding to the ectodomain of KIT, resulting in tyrosine kinase activation.
17662946	1	29	theme	Stem	89:92	arg1	Factor					99:104	Stem Cell Factor	89:104	Stem Cell Factor (SCF)	89:110	Stem Cell Factor (SCF) initiates its multiple cellular responses by binding to the ectodomain of KIT, resulting in tyrosine kinase activation.
17662946	3	30	theme	KIT	431:433	arg1	molecules					435:443	two KIT molecules	427:443	two KIT molecules	427:443	The structures show that KIT dimerization is driven by SCF binding whose sole role is to bring two KIT molecules together.
17662946	5	31	from	mutations	703:711	arg1	acids					722:726	amino acids	716:726	amino acids critical for D4-D4 interaction	716:757	Experiments with cultured cells show that KIT activation is compromised by point mutations in amino acids critical for D4-D4 interaction.
17662946	7	32	theme	other	1070:1074	arg1	activation					1085:1094	other receptor activation	1070:1094	other receptor activation	1070:1094	Since key hallmarks of KIT structures, ligand-induced receptor dimerization, and the critical residues in the D4-D4 interface, are conserved in other receptors, the mechanism of KIT stimulation unveiled in this report may apply for other receptor activation.
17662946	3	33	theme	SCF	387:389	arg1	binding					391:397	SCF binding	387:397	SCF binding whose sole role is to bring two KIT molecules together	387:452	The structures show that KIT dimerization is driven by SCF binding whose sole role is to bring two KIT molecules together.
17662946	4	34	theme	lateral	527:533	arg1	interactions					535:546	lateral interactions	527:546	lateral interactions between membrane proximal Ig-like domains D4 and D5 of two KIT molecules	527:619	Receptor dimerization is followed by conformational changes that enable lateral interactions between membrane proximal Ig-like domains D4 and D5 of two KIT molecules.
17662946	3	35	theme	sole	405:408	arg1	role					410:413	role	410:413	role	410:413	The structures show that KIT dimerization is driven by SCF binding whose sole role is to bring two KIT molecules together.
17662946	0	36	theme	tyrosine	48:55	arg1	KIT					64:66	the receptor tyrosine kinase KIT	35:66	the receptor tyrosine kinase KIT	35:66	Structural basis for activation of the receptor tyrosine kinase KIT by stem cell factor.
17662946	5	37	theme	amino	716:720	arg1	acids					722:726	amino acids	716:726	amino acids critical for D4-D4 interaction	716:757	Experiments with cultured cells show that KIT activation is compromised by point mutations in amino acids critical for D4-D4 interaction.
17662946	1	38	theme	Cell	94:97	arg1	SCF					107:109	SCF	107:109	SCF	107:109	Stem Cell Factor (SCF) initiates its multiple cellular responses by binding to the ectodomain of KIT, resulting in tyrosine kinase activation.
17662946	1	38	theme	Cell	94:97	arg1	Factor					99:104	Stem Cell Factor	89:104	Stem Cell Factor (SCF)	89:110	Stem Cell Factor (SCF) initiates its multiple cellular responses by binding to the ectodomain of KIT, resulting in tyrosine kinase activation.
17662946	3	39	theme	KIT	357:359	arg1	dimerization					361:372	KIT dimerization	357:372	KIT dimerization	357:372	The structures show that KIT dimerization is driven by SCF binding whose sole role is to bring two KIT molecules together.
17662946	5	40	theme	cultured	639:646	arg1	cells					648:652	cultured cells	639:652	cultured cells	639:652	Experiments with cultured cells show that KIT activation is compromised by point mutations in amino acids critical for D4-D4 interaction.
17662946	6	41	theme	mutations	793:801	arg1	mutations					793:801	oncogenic mutations	783:801	oncogenic mutations	783:801	Moreover, a variety of oncogenic mutations are mapped to the D5-D5 interface.
17662946	6	41	theme	mutations	793:801	arg1	variety					772:778	a variety	770:778	a variety of oncogenic mutations	770:801	Moreover, a variety of oncogenic mutations are mapped to the D5-D5 interface.
17662946	2	42	theme	KIT	294:296	arg1	KIT					294:296	KIT	294:296	KIT	294:296	We describe the crystal structure of the entire ectodomain of KIT before and after SCF stimulation.
17662946	2	42	theme	KIT	294:296	arg1	ectodomain					280:289	the entire ectodomain	269:289	the entire ectodomain of KIT	269:296	We describe the crystal structure of the entire ectodomain of KIT before and after SCF stimulation.
17662946	7	43	theme	KIT	861:863	arg1	structures					865:874	KIT structures	861:874	KIT structures	861:874	Since key hallmarks of KIT structures, ligand-induced receptor dimerization, and the critical residues in the D4-D4 interface, are conserved in other receptors, the mechanism of KIT stimulation unveiled in this report may apply for other receptor activation.
17662946	4	44	dep	domains	582:588	arg1	molecules					611:619	two KIT molecules	603:619	two KIT molecules	603:619	Receptor dimerization is followed by conformational changes that enable lateral interactions between membrane proximal Ig-like domains D4 and D5 of two KIT molecules.
17662946	4	44	dep	domains	582:588	arg1	domains					582:588	membrane proximal Ig-like domains D4 and D5	556:598	membrane proximal Ig-like domains D4 and D5 of two KIT molecules	556:619	Receptor dimerization is followed by conformational changes that enable lateral interactions between membrane proximal Ig-like domains D4 and D5 of two KIT molecules.
17662946	4	44	dep	domains	582:588	arg1	D5					597:598	D5	597:598	D5	597:598	Receptor dimerization is followed by conformational changes that enable lateral interactions between membrane proximal Ig-like domains D4 and D5 of two KIT molecules.
17662946	4	44	dep	domains	582:588	arg1	D4					590:591	D4	590:591	D4	590:591	Receptor dimerization is followed by conformational changes that enable lateral interactions between membrane proximal Ig-like domains D4 and D5 of two KIT molecules.
17662946	7	45	theme	receptor	1076:1083	arg1	activation					1085:1094	other receptor activation	1070:1094	other receptor activation	1070:1094	Since key hallmarks of KIT structures, ligand-induced receptor dimerization, and the critical residues in the D4-D4 interface, are conserved in other receptors, the mechanism of KIT stimulation unveiled in this report may apply for other receptor activation.
17662946	7	46	theme	structures	865:874	arg1	residues					932:939	the critical residues	919:939	the critical residues in the D4-D4 interface	919:962	Since key hallmarks of KIT structures, ligand-induced receptor dimerization, and the critical residues in the D4-D4 interface, are conserved in other receptors, the mechanism of KIT stimulation unveiled in this report may apply for other receptor activation.
17662946	7	46	theme	structures	865:874	arg1	dimerization					901:912	ligand-induced receptor dimerization	877:912	ligand-induced receptor dimerization	877:912	Since key hallmarks of KIT structures, ligand-induced receptor dimerization, and the critical residues in the D4-D4 interface, are conserved in other receptors, the mechanism of KIT stimulation unveiled in this report may apply for other receptor activation.
17662946	7	46	theme	structures	865:874	arg1	hallmarks					848:856	key hallmarks	844:856	key hallmarks of KIT structures	844:874	Since key hallmarks of KIT structures, ligand-induced receptor dimerization, and the critical residues in the D4-D4 interface, are conserved in other receptors, the mechanism of KIT stimulation unveiled in this report may apply for other receptor activation.
17662946	7	46	theme	structures	865:874	arg1	structures					865:874	KIT structures	861:874	KIT structures	861:874	Since key hallmarks of KIT structures, ligand-induced receptor dimerization, and the critical residues in the D4-D4 interface, are conserved in other receptors, the mechanism of KIT stimulation unveiled in this report may apply for other receptor activation.
17662946	1	47	theme	KIT	186:188	arg1	KIT					186:188	KIT	186:188	KIT	186:188	Stem Cell Factor (SCF) initiates its multiple cellular responses by binding to the ectodomain of KIT, resulting in tyrosine kinase activation.
17662946	1	47	theme	KIT	186:188	arg1	ectodomain					172:181	the ectodomain	168:181	the ectodomain of KIT	168:188	Stem Cell Factor (SCF) initiates its multiple cellular responses by binding to the ectodomain of KIT, resulting in tyrosine kinase activation.
17662946	7	48	theme	other	982:986	arg1	receptors					988:996	other receptors	982:996	other receptors	982:996	Since key hallmarks of KIT structures, ligand-induced receptor dimerization, and the critical residues in the D4-D4 interface, are conserved in other receptors, the mechanism of KIT stimulation unveiled in this report may apply for other receptor activation.
17662946	6	49	theme	oncogenic	783:791	arg1	mutations					793:801	oncogenic mutations	783:801	oncogenic mutations	783:801	Moreover, a variety of oncogenic mutations are mapped to the D5-D5 interface.
17662946	2	50	theme	ectodomain	280:289	arg1	structure					256:264	the crystal structure	244:264	the crystal structure of the entire ectodomain of KIT before and after SCF stimulation	244:329	We describe the crystal structure of the entire ectodomain of KIT before and after SCF stimulation.
17662946	4	51	theme	proximal	565:572	arg1	molecules					611:619	two KIT molecules	603:619	two KIT molecules	603:619	Receptor dimerization is followed by conformational changes that enable lateral interactions between membrane proximal Ig-like domains D4 and D5 of two KIT molecules.
17662946	4	51	theme	proximal	565:572	arg1	domains					582:588	membrane proximal Ig-like domains D4 and D5	556:598	membrane proximal Ig-like domains D4 and D5 of two KIT molecules	556:619	Receptor dimerization is followed by conformational changes that enable lateral interactions between membrane proximal Ig-like domains D4 and D5 of two KIT molecules.
17662946	4	51	theme	proximal	565:572	arg1	D5					597:598	D5	597:598	D5	597:598	Receptor dimerization is followed by conformational changes that enable lateral interactions between membrane proximal Ig-like domains D4 and D5 of two KIT molecules.
17662946	4	51	theme	proximal	565:572	arg1	D4					590:591	D4	590:591	D4	590:591	Receptor dimerization is followed by conformational changes that enable lateral interactions between membrane proximal Ig-like domains D4 and D5 of two KIT molecules.
17662946	0	52	theme	KIT	64:66	arg1	activation					21:30	activation	21:30	activation of the receptor tyrosine kinase KIT by stem cell factor	21:86	Structural basis for activation of the receptor tyrosine kinase KIT by stem cell factor.
17662946	7	53	theme	D4-D4	948:952	arg1	interface					954:962	the D4-D4 interface	944:962	the D4-D4 interface	944:962	Since key hallmarks of KIT structures, ligand-induced receptor dimerization, and the critical residues in the D4-D4 interface, are conserved in other receptors, the mechanism of KIT stimulation unveiled in this report may apply for other receptor activation.
17662946	7	54	from	residues	932:939	arg1	interface					954:962	the D4-D4 interface	944:962	the D4-D4 interface	944:962	Since key hallmarks of KIT structures, ligand-induced receptor dimerization, and the critical residues in the D4-D4 interface, are conserved in other receptors, the mechanism of KIT stimulation unveiled in this report may apply for other receptor activation.
17662946	0	55	theme	kinase	57:62	arg1	KIT					64:66	the receptor tyrosine kinase KIT	35:66	the receptor tyrosine kinase KIT	35:66	Structural basis for activation of the receptor tyrosine kinase KIT by stem cell factor.
17662946	5	56	theme	D4-D4	741:745	arg1	interaction					747:757	D4-D4 interaction	741:757	D4-D4 interaction	741:757	Experiments with cultured cells show that KIT activation is compromised by point mutations in amino acids critical for D4-D4 interaction.
17662946	2	57	theme	SCF	315:317	arg1	stimulation					319:329	SCF stimulation	315:329	SCF stimulation	315:329	We describe the crystal structure of the entire ectodomain of KIT before and after SCF stimulation.
17889651	0	0	theme	tri-acylated	71:82	arg1	lipopeptide					84:94	a tri-acylated lipopeptide	69:94	a tri-acylated lipopeptide	69:94	Crystal structure of the TLR1-TLR2 heterodimer induced by binding of a tri-acylated lipopeptide.
17889651	4	1	from	pocket	720:725	arg1	TLR2					730:733	TLR2	730:733	TLR2	730:733	The three lipid chains of Pam(3)CSK(4) mediate the heterodimerization of the receptor; the two ester-bound lipid chains are inserted into a pocket in TLR2, while the amide-bound lipid chain is inserted into a hydrophobic channel in TLR1.
17889651	2	2	theme	complex	361:367	arg1	structures					273:282	the crystal structures	261:282	the crystal structures of the human TLR1-TLR2-lipopeptide complex and of the mouse TLR2-lipopeptide complex	261:367	Here we present the crystal structures of the human TLR1-TLR2-lipopeptide complex and of the mouse TLR2-lipopeptide complex.
17889651	2	3	theme	TLR2-lipopeptide	344:359	arg1	complex					361:367	the mouse TLR2-lipopeptide complex	334:367	the mouse TLR2-lipopeptide complex	334:367	Here we present the crystal structures of the human TLR1-TLR2-lipopeptide complex and of the mouse TLR2-lipopeptide complex.
17889651	3	4	theme	TLR1	483:486	arg1	ectodomains					497:507	the TLR1 and TLR2 ectodomains	479:507	ectodomains	497:507	Binding of the tri-acylated lipopeptide, Pam(3)CSK(4), induced the formation of an "m" shaped heterodimer of the TLR1 and TLR2 ectodomains whereas binding of the di-acylated lipopeptide, Pam(2)CSK(4), did not.
17889651	3	5	theme	ectodomains	497:507	arg1	heterodimer					464:474	an "m" shaped heterodimer	450:474	an "m" shaped heterodimer of the TLR1 and TLR2 ectodomains	450:507	Binding of the tri-acylated lipopeptide, Pam(3)CSK(4), induced the formation of an "m" shaped heterodimer of the TLR1 and TLR2 ectodomains whereas binding of the di-acylated lipopeptide, Pam(2)CSK(4), did not.
17889651	0	6	theme	lipopeptide	84:94	arg1	binding					58:64	binding	58:64	binding of a tri-acylated lipopeptide	58:94	Crystal structure of the TLR1-TLR2 heterodimer induced by binding of a tri-acylated lipopeptide.
17889651	6	7	theme	intracellular	1017:1029	arg1	domains					1035:1041	the intracellular TIR domains	1013:1041	the intracellular TIR domains	1013:1041	We propose that formation of the TLR1-TLR2 heterodimer brings the intracellular TIR domains close to each other to promote dimerization and initiate signaling.
17889651	4	8	theme	lipid	590:594	arg1	chains					596:601	The three lipid chains	580:601	The three lipid chains of Pam	580:608	The three lipid chains of Pam(3)CSK(4) mediate the heterodimerization of the receptor; the two ester-bound lipid chains are inserted into a pocket in TLR2, while the amide-bound lipid chain is inserted into a hydrophobic channel in TLR1.
17889651	4	9	theme	hydrophobic	789:799	arg1	channel					801:807	a hydrophobic channel	787:807	a hydrophobic channel in TLR1	787:815	The three lipid chains of Pam(3)CSK(4) mediate the heterodimerization of the receptor; the two ester-bound lipid chains are inserted into a pocket in TLR2, while the amide-bound lipid chain is inserted into a hydrophobic channel in TLR1.
17889651	2	10	theme	crystal	265:271	arg1	structures					273:282	the crystal structures	261:282	the crystal structures of the human TLR1-TLR2-lipopeptide complex and of the mouse TLR2-lipopeptide complex	261:367	Here we present the crystal structures of the human TLR1-TLR2-lipopeptide complex and of the mouse TLR2-lipopeptide complex.
17889651	4	11	theme	lipid	687:691	arg1	chains					693:698	the two ester-bound lipid chains	667:698	the two ester-bound lipid chains	667:698	The three lipid chains of Pam(3)CSK(4) mediate the heterodimerization of the receptor; the two ester-bound lipid chains are inserted into a pocket in TLR2, while the amide-bound lipid chain is inserted into a hydrophobic channel in TLR1.
17889651	3	12	theme	lipopeptide	398:408	arg1	Binding					370:376	Binding	370:376	Binding of the tri-acylated lipopeptide, Pam(3)CSK(4),	370:423	Binding of the tri-acylated lipopeptide, Pam(3)CSK(4), induced the formation of an "m" shaped heterodimer of the TLR1 and TLR2 ectodomains whereas binding of the di-acylated lipopeptide, Pam(2)CSK(4), did not.
17889651	3	13	theme	tri-acylated	385:396	arg1	lipopeptide					398:408	the tri-acylated lipopeptide	381:408	the tri-acylated lipopeptide	381:408	Binding of the tri-acylated lipopeptide, Pam(3)CSK(4), induced the formation of an "m" shaped heterodimer of the TLR1 and TLR2 ectodomains whereas binding of the di-acylated lipopeptide, Pam(2)CSK(4), did not.
17889651	3	13	theme	tri-acylated	385:396	arg1	CSK					417:419	Pam(3)CSK(4)	411:422	Pam(3)CSK(4)	411:422	Binding of the tri-acylated lipopeptide, Pam(3)CSK(4), induced the formation of an "m" shaped heterodimer of the TLR1 and TLR2 ectodomains whereas binding of the di-acylated lipopeptide, Pam(2)CSK(4), did not.
17889651	6	14	theme	heterodimer	994:1004	arg1	formation					967:975	formation	967:975	formation of the TLR1-TLR2 heterodimer	967:1004	We propose that formation of the TLR1-TLR2 heterodimer brings the intracellular TIR domains close to each other to promote dimerization and initiate signaling.
17889651	1	15	with	association	105:115	arg1	TLR1					122:125	TLR1	122:125	TLR1	122:125	TLR2 in association with TLR1 or TLR6 plays an important role in the innate immune response by recognizing microbial lipoproteins and lipopeptides.
17889651	1	15	with	association	105:115	arg1	TLR6					130:133	TLR6	130:133	TLR6	130:133	TLR2 in association with TLR1 or TLR6 plays an important role in the innate immune response by recognizing microbial lipoproteins and lipopeptides.
17889651	2	16	theme	complex	319:325	arg1	structures					273:282	the crystal structures	261:282	the crystal structures of the human TLR1-TLR2-lipopeptide complex and of the mouse TLR2-lipopeptide complex	261:367	Here we present the crystal structures of the human TLR1-TLR2-lipopeptide complex and of the mouse TLR2-lipopeptide complex.
17889651	4	17	dep	mediate	619:625	arg1	3					610:610	3	610:610	3	610:610	The three lipid chains of Pam(3)CSK(4) mediate the heterodimerization of the receptor; the two ester-bound lipid chains are inserted into a pocket in TLR2, while the amide-bound lipid chain is inserted into a hydrophobic channel in TLR1.
17889651	0	18	theme	Crystal	0:6	arg1	structure					8:16	Crystal structure	0:16	Crystal structure of the TLR1-TLR2 heterodimer	0:45	Crystal structure of the TLR1-TLR2 heterodimer induced by binding of a tri-acylated lipopeptide.
17889651	2	19	theme	TLR1-TLR2-lipopeptide	297:317	arg1	complex					319:325	the human TLR1-TLR2-lipopeptide complex	287:325	the human TLR1-TLR2-lipopeptide complex	287:325	Here we present the crystal structures of the human TLR1-TLR2-lipopeptide complex and of the mouse TLR2-lipopeptide complex.
17889651	1	20	theme	innate	166:171	arg1	response					180:187	the innate immune response	162:187	the innate immune response	162:187	TLR2 in association with TLR1 or TLR6 plays an important role in the innate immune response by recognizing microbial lipoproteins and lipopeptides.
17889651	5	21	theme	hydrogen-bonding	831:846	arg1	network					848:854	An extensive hydrogen-bonding network	818:854	An extensive hydrogen-bonding network	818:854	An extensive hydrogen-bonding network, as well as hydrophobic interactions, between TLR1 and TLR2 further stabilize the heterodimer.
17889651	4	22	theme	lipid	758:762	arg1	chain					764:768	the amide-bound lipid chain	742:768	the amide-bound lipid chain	742:768	The three lipid chains of Pam(3)CSK(4) mediate the heterodimerization of the receptor; the two ester-bound lipid chains are inserted into a pocket in TLR2, while the amide-bound lipid chain is inserted into a hydrophobic channel in TLR1.
17889651	3	23	theme	TLR2	492:495	arg1	ectodomains					497:507	the TLR1 and TLR2 ectodomains	479:507	ectodomains	497:507	Binding of the tri-acylated lipopeptide, Pam(3)CSK(4), induced the formation of an "m" shaped heterodimer of the TLR1 and TLR2 ectodomains whereas binding of the di-acylated lipopeptide, Pam(2)CSK(4), did not.
17889651	1	24	theme	immune	173:178	arg1	response					180:187	the innate immune response	162:187	the innate immune response	162:187	TLR2 in association with TLR1 or TLR6 plays an important role in the innate immune response by recognizing microbial lipoproteins and lipopeptides.
17889651	6	25	theme	TLR1-TLR2	984:992	arg1	heterodimer					994:1004	the TLR1-TLR2 heterodimer	980:1004	the TLR1-TLR2 heterodimer	980:1004	We propose that formation of the TLR1-TLR2 heterodimer brings the intracellular TIR domains close to each other to promote dimerization and initiate signaling.
17889651	4	26	theme	amide-bound	746:756	arg1	chain					764:768	the amide-bound lipid chain	742:768	the amide-bound lipid chain	742:768	The three lipid chains of Pam(3)CSK(4) mediate the heterodimerization of the receptor; the two ester-bound lipid chains are inserted into a pocket in TLR2, while the amide-bound lipid chain is inserted into a hydrophobic channel in TLR1.
17889651	6	27	theme	TIR	1031:1033	arg1	domains					1035:1041	the intracellular TIR domains	1013:1041	the intracellular TIR domains	1013:1041	We propose that formation of the TLR1-TLR2 heterodimer brings the intracellular TIR domains close to each other to promote dimerization and initiate signaling.
17889651	1	28	theme	important	144:152	arg1	role					154:157	an important role	141:157	an important role	141:157	TLR2 in association with TLR1 or TLR6 plays an important role in the innate immune response by recognizing microbial lipoproteins and lipopeptides.
17889651	0	29	theme	heterodimer	35:45	arg1	structure					8:16	Crystal structure	0:16	Crystal structure of the TLR1-TLR2 heterodimer	0:45	Crystal structure of the TLR1-TLR2 heterodimer induced by binding of a tri-acylated lipopeptide.
17889651	3	30	theme	di-acylated	532:542	arg1	lipopeptide					544:554	the di-acylated lipopeptide	528:554	the di-acylated lipopeptide	528:554	Binding of the tri-acylated lipopeptide, Pam(3)CSK(4), induced the formation of an "m" shaped heterodimer of the TLR1 and TLR2 ectodomains whereas binding of the di-acylated lipopeptide, Pam(2)CSK(4), did not.
17889651	3	30	theme	di-acylated	532:542	arg1	CSK					563:565	Pam(2)CSK(4)	557:568	Pam(2)CSK(4)	557:568	Binding of the tri-acylated lipopeptide, Pam(3)CSK(4), induced the formation of an "m" shaped heterodimer of the TLR1 and TLR2 ectodomains whereas binding of the di-acylated lipopeptide, Pam(2)CSK(4), did not.
17889651	0	31	theme	TLR1-TLR2	25:33	arg1	heterodimer					35:45	the TLR1-TLR2 heterodimer	21:45	the TLR1-TLR2 heterodimer	21:45	Crystal structure of the TLR1-TLR2 heterodimer induced by binding of a tri-acylated lipopeptide.
17889651	3	32	theme	lipopeptide	544:554	arg1	binding					517:523	binding	517:523	binding of the di-acylated lipopeptide, Pam(2)CSK(4),	517:569	Binding of the tri-acylated lipopeptide, Pam(3)CSK(4), induced the formation of an "m" shaped heterodimer of the TLR1 and TLR2 ectodomains whereas binding of the di-acylated lipopeptide, Pam(2)CSK(4), did not.
17889651	4	33	theme	ester-bound	675:685	arg1	chains					693:698	the two ester-bound lipid chains	667:698	the two ester-bound lipid chains	667:698	The three lipid chains of Pam(3)CSK(4) mediate the heterodimerization of the receptor; the two ester-bound lipid chains are inserted into a pocket in TLR2, while the amide-bound lipid chain is inserted into a hydrophobic channel in TLR1.
17889651	2	34	theme	mouse	338:342	arg1	complex					361:367	the mouse TLR2-lipopeptide complex	334:367	the mouse TLR2-lipopeptide complex	334:367	Here we present the crystal structures of the human TLR1-TLR2-lipopeptide complex and of the mouse TLR2-lipopeptide complex.
17889651	3	35	theme	Pam	411:413	arg1	lipopeptide					398:408	the tri-acylated lipopeptide	381:408	the tri-acylated lipopeptide	381:408	Binding of the tri-acylated lipopeptide, Pam(3)CSK(4), induced the formation of an "m" shaped heterodimer of the TLR1 and TLR2 ectodomains whereas binding of the di-acylated lipopeptide, Pam(2)CSK(4), did not.
17889651	3	35	theme	Pam	411:413	arg1	CSK					417:419	Pam(3)CSK(4)	411:422	Pam(3)CSK(4)	411:422	Binding of the tri-acylated lipopeptide, Pam(3)CSK(4), induced the formation of an "m" shaped heterodimer of the TLR1 and TLR2 ectodomains whereas binding of the di-acylated lipopeptide, Pam(2)CSK(4), did not.
17889651	5	36	theme	hydrophobic	868:878	arg1	interactions					880:891	hydrophobic interactions	868:891	hydrophobic interactions	868:891	An extensive hydrogen-bonding network, as well as hydrophobic interactions, between TLR1 and TLR2 further stabilize the heterodimer.
17889651	3	37	theme	"	455:455	arg1	heterodimer					464:474	an "m" shaped heterodimer	450:474	an "m" shaped heterodimer of the TLR1 and TLR2 ectodomains	450:507	Binding of the tri-acylated lipopeptide, Pam(3)CSK(4), induced the formation of an "m" shaped heterodimer of the TLR1 and TLR2 ectodomains whereas binding of the di-acylated lipopeptide, Pam(2)CSK(4), did not.
17889651	1	38	from	TLR2	97:100	arg1	association					105:115	association	105:115	association with TLR1 or TLR6	105:133	TLR2 in association with TLR1 or TLR6 plays an important role in the innate immune response by recognizing microbial lipoproteins and lipopeptides.
17889651	2	39	theme	human	291:295	arg1	complex					319:325	the human TLR1-TLR2-lipopeptide complex	287:325	the human TLR1-TLR2-lipopeptide complex	287:325	Here we present the crystal structures of the human TLR1-TLR2-lipopeptide complex and of the mouse TLR2-lipopeptide complex.
17889651	1	40	theme	microbial	204:212	arg1	lipoproteins					214:225	microbial lipoproteins	204:225	microbial lipoproteins	204:225	TLR2 in association with TLR1 or TLR6 plays an important role in the innate immune response by recognizing microbial lipoproteins and lipopeptides.
17889651	5	41	theme	extensive	821:829	arg1	network					848:854	An extensive hydrogen-bonding network	818:854	An extensive hydrogen-bonding network	818:854	An extensive hydrogen-bonding network, as well as hydrophobic interactions, between TLR1 and TLR2 further stabilize the heterodimer.
17889651	4	42	theme	Pam	606:608	arg1	chains					596:601	The three lipid chains	580:601	The three lipid chains of Pam	580:608	The three lipid chains of Pam(3)CSK(4) mediate the heterodimerization of the receptor; the two ester-bound lipid chains are inserted into a pocket in TLR2, while the amide-bound lipid chain is inserted into a hydrophobic channel in TLR1.
17889651	4	43	theme	receptor	657:664	arg1	heterodimerization					631:648	the heterodimerization	627:648	the heterodimerization of the receptor	627:664	The three lipid chains of Pam(3)CSK(4) mediate the heterodimerization of the receptor; the two ester-bound lipid chains are inserted into a pocket in TLR2, while the amide-bound lipid chain is inserted into a hydrophobic channel in TLR1.
17889651	3	44	theme	shaped	457:462	arg1	heterodimer					464:474	an "m" shaped heterodimer	450:474	an "m" shaped heterodimer of the TLR1 and TLR2 ectodomains	450:507	Binding of the tri-acylated lipopeptide, Pam(3)CSK(4), induced the formation of an "m" shaped heterodimer of the TLR1 and TLR2 ectodomains whereas binding of the di-acylated lipopeptide, Pam(2)CSK(4), did not.
17889651	3	45	theme	Pam	557:559	arg1	lipopeptide					544:554	the di-acylated lipopeptide	528:554	the di-acylated lipopeptide	528:554	Binding of the tri-acylated lipopeptide, Pam(3)CSK(4), induced the formation of an "m" shaped heterodimer of the TLR1 and TLR2 ectodomains whereas binding of the di-acylated lipopeptide, Pam(2)CSK(4), did not.
17889651	3	45	theme	Pam	557:559	arg1	CSK					563:565	Pam(2)CSK(4)	557:568	Pam(2)CSK(4)	557:568	Binding of the tri-acylated lipopeptide, Pam(3)CSK(4), induced the formation of an "m" shaped heterodimer of the TLR1 and TLR2 ectodomains whereas binding of the di-acylated lipopeptide, Pam(2)CSK(4), did not.
17889651	3	46	theme	heterodimer	464:474	arg1	formation					437:445	the formation	433:445	the formation of an "m" shaped heterodimer of the TLR1 and TLR2 ectodomains	433:507	Binding of the tri-acylated lipopeptide, Pam(3)CSK(4), induced the formation of an "m" shaped heterodimer of the TLR1 and TLR2 ectodomains whereas binding of the di-acylated lipopeptide, Pam(2)CSK(4), did not.
17889651	4	47	from	channel	801:807	arg1	TLR1					812:815	TLR1	812:815	TLR1	812:815	The three lipid chains of Pam(3)CSK(4) mediate the heterodimerization of the receptor; the two ester-bound lipid chains are inserted into a pocket in TLR2, while the amide-bound lipid chain is inserted into a hydrophobic channel in TLR1.
16203964	2	0	theme	several	416:422	arg1	cancers					430:436	several human cancers	416:436	several human cancers	416:436	ErbBs play fundamental roles in cell growth and differentiation events in embryonic and adult tissues, and inappropriate ErbB activity has been implicated in several human cancers.
16203964	3	1	theme	inactive	609:616	arg1	forms					618:622	inactive forms	609:622	inactive forms of ErbB1 and ErbB3	609:641	We report here the 2.4 A crystal structure of the extracellular region of human ErbB4 in the absence of ligand and show that it adopts a tethered conformation similar to inactive forms of ErbB1 and ErbB3.
16203964	6	2	theme	ErbB	1195:1198	arg1	receptor					1200:1207	the same ErbB receptor	1186:1207	the same ErbB receptor	1186:1207	These results indicate an important role for ligand in determining pH-dependent binding and may explain different responses observed when the same ErbB receptor is stimulated by different ligands.
16203964	1	3	theme	kinases	134:140	arg1	family					106:111	The human ErbB family	91:111	The human ErbB family of receptor tyrosine kinases	91:140	The human ErbB family of receptor tyrosine kinases comprises the epidermal growth factor receptor (EGFR/ErbB1/HER1), ErbB2 (HER2/Neu), ErbB3 (HER3), and ErbB4 (HER4).
16203964	5	4	theme	epidermal	977:985	arg1	factor					994:999	epidermal growth factor	977:999	epidermal growth factor	977:999	We also show that the binding of neuregulin-1beta to ErbB4 and ErbB3 and the binding of betacellulin to both ErbB4 and ErbB1 does not decrease at low pH, unlike the binding of epidermal growth factor and transforming growth factor-alpha to ErbB1.
16203964	5	5	theme	growth	1018:1023	arg1	factor-alpha					1025:1036	transforming growth factor-alpha	1005:1036	transforming growth factor-alpha	1005:1036	We also show that the binding of neuregulin-1beta to ErbB4 and ErbB3 and the binding of betacellulin to both ErbB4 and ErbB1 does not decrease at low pH, unlike the binding of epidermal growth factor and transforming growth factor-alpha to ErbB1.
16203964	5	6	theme	factor-alpha	1025:1036	arg1	binding					966:972	the binding	962:972	the binding of epidermal growth factor and transforming growth factor-alpha to ErbB1	962:1045	We also show that the binding of neuregulin-1beta to ErbB4 and ErbB3 and the binding of betacellulin to both ErbB4 and ErbB1 does not decrease at low pH, unlike the binding of epidermal growth factor and transforming growth factor-alpha to ErbB1.
16203964	4	7	theme	autoinhibited	773:785	arg1	conformation					787:798	the autoinhibited conformation	769:798	the autoinhibited conformation	769:798	This structure completes the gallery of unliganded ErbB receptors and demonstrates that all human ligand-binding ErbBs adopt the autoinhibited conformation.
16203964	0	8	theme	ligand	83:88	arg1	absence					72:78	the absence	68:78	the absence of ligand	68:88	The extracellular region of ErbB4 adopts a tethered conformation in the absence of ligand.
16203964	3	9	theme	similar	598:604	arg1	conformation					585:596	a tethered conformation	574:596	a tethered conformation similar to inactive forms of ErbB1 and ErbB3	574:641	We report here the 2.4 A crystal structure of the extracellular region of human ErbB4 in the absence of ligand and show that it adopts a tethered conformation similar to inactive forms of ErbB1 and ErbB3.
16203964	4	10	theme	human	736:740	arg1	ErbBs					757:761	all human ligand-binding ErbBs	732:761	all human ligand-binding ErbBs	732:761	This structure completes the gallery of unliganded ErbB receptors and demonstrates that all human ligand-binding ErbBs adopt the autoinhibited conformation.
16203964	3	11	theme	A	462:462	arg1	structure					472:480	the 2.4 A crystal structure	454:480	the 2.4 A crystal structure of the extracellular region of human ErbB4 in the absence of ligand	454:548	We report here the 2.4 A crystal structure of the extracellular region of human ErbB4 in the absence of ligand and show that it adopts a tethered conformation similar to inactive forms of ErbB1 and ErbB3.
16203964	3	12	theme	ErbB1	627:631	arg1	forms					618:622	inactive forms	609:622	inactive forms of ErbB1 and ErbB3	609:641	We report here the 2.4 A crystal structure of the extracellular region of human ErbB4 in the absence of ligand and show that it adopts a tethered conformation similar to inactive forms of ErbB1 and ErbB3.
16203964	6	13	theme	important	1074:1082	arg1	role					1084:1087	an important role	1071:1087	an important role for ligand in determining pH-dependent binding	1071:1134	These results indicate an important role for ligand in determining pH-dependent binding and may explain different responses observed when the same ErbB receptor is stimulated by different ligands.
16203964	3	14	theme	crystal	464:470	arg1	structure					472:480	the 2.4 A crystal structure	454:480	the 2.4 A crystal structure of the extracellular region of human ErbB4 in the absence of ligand	454:548	We report here the 2.4 A crystal structure of the extracellular region of human ErbB4 in the absence of ligand and show that it adopts a tethered conformation similar to inactive forms of ErbB1 and ErbB3.
16203964	1	15	theme	human	95:99	arg1	family					106:111	The human ErbB family	91:111	The human ErbB family of receptor tyrosine kinases	91:140	The human ErbB family of receptor tyrosine kinases comprises the epidermal growth factor receptor (EGFR/ErbB1/HER1), ErbB2 (HER2/Neu), ErbB3 (HER3), and ErbB4 (HER4).
16203964	2	16	theme	adult	346:350	arg1	tissues					352:358	embryonic and adult tissues	332:358	embryonic and adult tissues	332:358	ErbBs play fundamental roles in cell growth and differentiation events in embryonic and adult tissues, and inappropriate ErbB activity has been implicated in several human cancers.
16203964	2	17	theme	differentiation	306:320	arg1	events					322:327	cell growth and differentiation events	290:327	cell growth and differentiation events in embryonic and adult tissues	290:358	ErbBs play fundamental roles in cell growth and differentiation events in embryonic and adult tissues, and inappropriate ErbB activity has been implicated in several human cancers.
16203964	5	18	theme	factor	994:999	arg1	binding					966:972	the binding	962:972	the binding of epidermal growth factor and transforming growth factor-alpha to ErbB1	962:1045	We also show that the binding of neuregulin-1beta to ErbB4 and ErbB3 and the binding of betacellulin to both ErbB4 and ErbB1 does not decrease at low pH, unlike the binding of epidermal growth factor and transforming growth factor-alpha to ErbB1.
16203964	4	19	theme	ligand-binding	742:755	arg1	ErbBs					757:761	all human ligand-binding ErbBs	732:761	all human ligand-binding ErbBs	732:761	This structure completes the gallery of unliganded ErbB receptors and demonstrates that all human ligand-binding ErbBs adopt the autoinhibited conformation.
16203964	5	20	theme	betacellulin	889:900	arg1	binding					878:884	the binding	874:884	the binding of betacellulin to both ErbB4 and ErbB1	874:924	We also show that the binding of neuregulin-1beta to ErbB4 and ErbB3 and the binding of betacellulin to both ErbB4 and ErbB1 does not decrease at low pH, unlike the binding of epidermal growth factor and transforming growth factor-alpha to ErbB1.
16203964	5	20	theme	betacellulin	889:900	arg1	binding					823:829	the binding	819:829	the binding of neuregulin-1beta to ErbB4 and ErbB3	819:868	We also show that the binding of neuregulin-1beta to ErbB4 and ErbB3 and the binding of betacellulin to both ErbB4 and ErbB1 does not decrease at low pH, unlike the binding of epidermal growth factor and transforming growth factor-alpha to ErbB1.
16203964	3	21	from	absence	532:538	arg1	region					503:508	the extracellular region	485:508	the extracellular region of human ErbB4 in the absence of ligand	485:548	We report here the 2.4 A crystal structure of the extracellular region of human ErbB4 in the absence of ligand and show that it adopts a tethered conformation similar to inactive forms of ErbB1 and ErbB3.
16203964	1	22	theme	epidermal	156:164	arg1	ErbB3					226:230	ErbB3	226:230	ErbB3 (HER3)	226:237	The human ErbB family of receptor tyrosine kinases comprises the epidermal growth factor receptor (EGFR/ErbB1/HER1), ErbB2 (HER2/Neu), ErbB3 (HER3), and ErbB4 (HER4).
16203964	1	22	theme	epidermal	156:164	arg1	EGFR/ErbB1/HER1					190:204	EGFR/ErbB1/HER1	190:204	EGFR/ErbB1/HER1	190:204	The human ErbB family of receptor tyrosine kinases comprises the epidermal growth factor receptor (EGFR/ErbB1/HER1), ErbB2 (HER2/Neu), ErbB3 (HER3), and ErbB4 (HER4).
16203964	1	22	theme	epidermal	156:164	arg1	ErbB2					208:212	ErbB2	208:212	ErbB2 (HER2/Neu)	208:223	The human ErbB family of receptor tyrosine kinases comprises the epidermal growth factor receptor (EGFR/ErbB1/HER1), ErbB2 (HER2/Neu), ErbB3 (HER3), and ErbB4 (HER4).
16203964	1	22	theme	epidermal	156:164	arg1	receptor					180:187	the epidermal growth factor receptor	152:187	the epidermal growth factor receptor (EGFR/ErbB1/HER1)	152:205	The human ErbB family of receptor tyrosine kinases comprises the epidermal growth factor receptor (EGFR/ErbB1/HER1), ErbB2 (HER2/Neu), ErbB3 (HER3), and ErbB4 (HER4).
16203964	1	22	theme	epidermal	156:164	arg1	ErbB4					244:248	ErbB4	244:248	ErbB4 (HER4)	244:255	The human ErbB family of receptor tyrosine kinases comprises the epidermal growth factor receptor (EGFR/ErbB1/HER1), ErbB2 (HER2/Neu), ErbB3 (HER3), and ErbB4 (HER4).
16203964	2	23	theme	ErbB	379:382	arg1	activity					384:391	inappropriate ErbB activity	365:391	inappropriate ErbB activity	365:391	ErbBs play fundamental roles in cell growth and differentiation events in embryonic and adult tissues, and inappropriate ErbB activity has been implicated in several human cancers.
16203964	6	24	theme	different	1152:1160	arg1	responses					1162:1170	different responses	1152:1170	different responses observed when the same ErbB receptor is stimulated by different ligands	1152:1242	These results indicate an important role for ligand in determining pH-dependent binding and may explain different responses observed when the same ErbB receptor is stimulated by different ligands.
16203964	5	25	theme	growth	987:992	arg1	factor					994:999	epidermal growth factor	977:999	epidermal growth factor	977:999	We also show that the binding of neuregulin-1beta to ErbB4 and ErbB3 and the binding of betacellulin to both ErbB4 and ErbB1 does not decrease at low pH, unlike the binding of epidermal growth factor and transforming growth factor-alpha to ErbB1.
16203964	1	26	theme	growth	166:171	arg1	ErbB3					226:230	ErbB3	226:230	ErbB3 (HER3)	226:237	The human ErbB family of receptor tyrosine kinases comprises the epidermal growth factor receptor (EGFR/ErbB1/HER1), ErbB2 (HER2/Neu), ErbB3 (HER3), and ErbB4 (HER4).
16203964	1	26	theme	growth	166:171	arg1	EGFR/ErbB1/HER1					190:204	EGFR/ErbB1/HER1	190:204	EGFR/ErbB1/HER1	190:204	The human ErbB family of receptor tyrosine kinases comprises the epidermal growth factor receptor (EGFR/ErbB1/HER1), ErbB2 (HER2/Neu), ErbB3 (HER3), and ErbB4 (HER4).
16203964	1	26	theme	growth	166:171	arg1	ErbB2					208:212	ErbB2	208:212	ErbB2 (HER2/Neu)	208:223	The human ErbB family of receptor tyrosine kinases comprises the epidermal growth factor receptor (EGFR/ErbB1/HER1), ErbB2 (HER2/Neu), ErbB3 (HER3), and ErbB4 (HER4).
16203964	1	26	theme	growth	166:171	arg1	receptor					180:187	the epidermal growth factor receptor	152:187	the epidermal growth factor receptor (EGFR/ErbB1/HER1)	152:205	The human ErbB family of receptor tyrosine kinases comprises the epidermal growth factor receptor (EGFR/ErbB1/HER1), ErbB2 (HER2/Neu), ErbB3 (HER3), and ErbB4 (HER4).
16203964	1	26	theme	growth	166:171	arg1	ErbB4					244:248	ErbB4	244:248	ErbB4 (HER4)	244:255	The human ErbB family of receptor tyrosine kinases comprises the epidermal growth factor receptor (EGFR/ErbB1/HER1), ErbB2 (HER2/Neu), ErbB3 (HER3), and ErbB4 (HER4).
16203964	2	27	theme	inappropriate	365:377	arg1	activity					384:391	inappropriate ErbB activity	365:391	inappropriate ErbB activity	365:391	ErbBs play fundamental roles in cell growth and differentiation events in embryonic and adult tissues, and inappropriate ErbB activity has been implicated in several human cancers.
16203964	3	28	theme	extracellular	489:501	arg1	region					503:508	the extracellular region	485:508	the extracellular region of human ErbB4 in the absence of ligand	485:548	We report here the 2.4 A crystal structure of the extracellular region of human ErbB4 in the absence of ligand and show that it adopts a tethered conformation similar to inactive forms of ErbB1 and ErbB3.
16203964	3	29	from	region	503:508	arg1	absence					532:538	the absence	528:538	the absence of ligand	528:548	We report here the 2.4 A crystal structure of the extracellular region of human ErbB4 in the absence of ligand and show that it adopts a tethered conformation similar to inactive forms of ErbB1 and ErbB3.
16203964	1	30	theme	factor	173:178	arg1	ErbB3					226:230	ErbB3	226:230	ErbB3 (HER3)	226:237	The human ErbB family of receptor tyrosine kinases comprises the epidermal growth factor receptor (EGFR/ErbB1/HER1), ErbB2 (HER2/Neu), ErbB3 (HER3), and ErbB4 (HER4).
16203964	1	30	theme	factor	173:178	arg1	EGFR/ErbB1/HER1					190:204	EGFR/ErbB1/HER1	190:204	EGFR/ErbB1/HER1	190:204	The human ErbB family of receptor tyrosine kinases comprises the epidermal growth factor receptor (EGFR/ErbB1/HER1), ErbB2 (HER2/Neu), ErbB3 (HER3), and ErbB4 (HER4).
16203964	1	30	theme	factor	173:178	arg1	ErbB2					208:212	ErbB2	208:212	ErbB2 (HER2/Neu)	208:223	The human ErbB family of receptor tyrosine kinases comprises the epidermal growth factor receptor (EGFR/ErbB1/HER1), ErbB2 (HER2/Neu), ErbB3 (HER3), and ErbB4 (HER4).
16203964	1	30	theme	factor	173:178	arg1	receptor					180:187	the epidermal growth factor receptor	152:187	the epidermal growth factor receptor (EGFR/ErbB1/HER1)	152:205	The human ErbB family of receptor tyrosine kinases comprises the epidermal growth factor receptor (EGFR/ErbB1/HER1), ErbB2 (HER2/Neu), ErbB3 (HER3), and ErbB4 (HER4).
16203964	1	30	theme	factor	173:178	arg1	ErbB4					244:248	ErbB4	244:248	ErbB4 (HER4)	244:255	The human ErbB family of receptor tyrosine kinases comprises the epidermal growth factor receptor (EGFR/ErbB1/HER1), ErbB2 (HER2/Neu), ErbB3 (HER3), and ErbB4 (HER4).
16203964	6	31	theme	pH-dependent	1115:1126	arg1	binding					1128:1134	pH-dependent binding	1115:1134	pH-dependent binding	1115:1134	These results indicate an important role for ligand in determining pH-dependent binding and may explain different responses observed when the same ErbB receptor is stimulated by different ligands.
16203964	3	32	theme	ErbB3	637:641	arg1	forms					618:622	inactive forms	609:622	inactive forms of ErbB1 and ErbB3	609:641	We report here the 2.4 A crystal structure of the extracellular region of human ErbB4 in the absence of ligand and show that it adopts a tethered conformation similar to inactive forms of ErbB1 and ErbB3.
16203964	1	33	theme	receptor	116:123	arg1	kinases					134:140	receptor tyrosine kinases	116:140	receptor tyrosine kinases	116:140	The human ErbB family of receptor tyrosine kinases comprises the epidermal growth factor receptor (EGFR/ErbB1/HER1), ErbB2 (HER2/Neu), ErbB3 (HER3), and ErbB4 (HER4).
16203964	3	34	theme	human	513:517	arg1	ErbB4					519:523	human ErbB4	513:523	human ErbB4 in the absence of ligand	513:548	We report here the 2.4 A crystal structure of the extracellular region of human ErbB4 in the absence of ligand and show that it adopts a tethered conformation similar to inactive forms of ErbB1 and ErbB3.
16203964	3	35	from	ErbB4	519:523	arg1	absence					532:538	the absence	528:538	the absence of ligand	528:548	We report here the 2.4 A crystal structure of the extracellular region of human ErbB4 in the absence of ligand and show that it adopts a tethered conformation similar to inactive forms of ErbB1 and ErbB3.
16203964	0	36	theme	ErbB4	28:32	arg1	region					18:23	The extracellular region	0:23	The extracellular region of ErbB4	0:32	The extracellular region of ErbB4 adopts a tethered conformation in the absence of ligand.
16203964	6	37	theme	different	1226:1234	arg1	ligands					1236:1242	different ligands	1226:1242	different ligands	1226:1242	These results indicate an important role for ligand in determining pH-dependent binding and may explain different responses observed when the same ErbB receptor is stimulated by different ligands.
16203964	3	38	theme	ligand	543:548	arg1	absence					532:538	the absence	528:538	the absence of ligand	528:548	We report here the 2.4 A crystal structure of the extracellular region of human ErbB4 in the absence of ligand and show that it adopts a tethered conformation similar to inactive forms of ErbB1 and ErbB3.
16203964	3	39	theme	ErbB4	519:523	arg1	region					503:508	the extracellular region	485:508	the extracellular region of human ErbB4 in the absence of ligand	485:548	We report here the 2.4 A crystal structure of the extracellular region of human ErbB4 in the absence of ligand and show that it adopts a tethered conformation similar to inactive forms of ErbB1 and ErbB3.
16203964	2	40	theme	embryonic	332:340	arg1	tissues					352:358	embryonic and adult tissues	332:358	embryonic and adult tissues	332:358	ErbBs play fundamental roles in cell growth and differentiation events in embryonic and adult tissues, and inappropriate ErbB activity has been implicated in several human cancers.
16203964	0	41	theme	tethered	43:50	arg1	conformation					52:63	a tethered conformation	41:63	a tethered conformation	41:63	The extracellular region of ErbB4 adopts a tethered conformation in the absence of ligand.
16203964	5	42	theme	low	947:949	arg1	pH					951:952	low pH	947:952	low pH	947:952	We also show that the binding of neuregulin-1beta to ErbB4 and ErbB3 and the binding of betacellulin to both ErbB4 and ErbB1 does not decrease at low pH, unlike the binding of epidermal growth factor and transforming growth factor-alpha to ErbB1.
16203964	3	43	theme	region	503:508	arg1	structure					472:480	the 2.4 A crystal structure	454:480	the 2.4 A crystal structure of the extracellular region of human ErbB4 in the absence of ligand	454:548	We report here the 2.4 A crystal structure of the extracellular region of human ErbB4 in the absence of ligand and show that it adopts a tethered conformation similar to inactive forms of ErbB1 and ErbB3.
16203964	2	44	theme	fundamental	269:279	arg1	roles					281:285	fundamental roles	269:285	fundamental roles	269:285	ErbBs play fundamental roles in cell growth and differentiation events in embryonic and adult tissues, and inappropriate ErbB activity has been implicated in several human cancers.
16203964	1	45	theme	tyrosine	125:132	arg1	kinases					134:140	receptor tyrosine kinases	116:140	receptor tyrosine kinases	116:140	The human ErbB family of receptor tyrosine kinases comprises the epidermal growth factor receptor (EGFR/ErbB1/HER1), ErbB2 (HER2/Neu), ErbB3 (HER3), and ErbB4 (HER4).
16203964	1	46	theme	ErbB	101:104	arg1	family					106:111	The human ErbB family	91:111	The human ErbB family of receptor tyrosine kinases	91:140	The human ErbB family of receptor tyrosine kinases comprises the epidermal growth factor receptor (EGFR/ErbB1/HER1), ErbB2 (HER2/Neu), ErbB3 (HER3), and ErbB4 (HER4).
16203964	6	47	theme	same	1190:1193	arg1	receptor					1200:1207	the same ErbB receptor	1186:1207	the same ErbB receptor	1186:1207	These results indicate an important role for ligand in determining pH-dependent binding and may explain different responses observed when the same ErbB receptor is stimulated by different ligands.
16203964	3	48	theme	tethered	576:583	arg1	conformation					585:596	a tethered conformation	574:596	a tethered conformation similar to inactive forms of ErbB1 and ErbB3	574:641	We report here the 2.4 A crystal structure of the extracellular region of human ErbB4 in the absence of ligand and show that it adopts a tethered conformation similar to inactive forms of ErbB1 and ErbB3.
16203964	4	49	theme	ErbB	695:698	arg1	receptors					700:708	unliganded ErbB receptors	684:708	unliganded ErbB receptors	684:708	This structure completes the gallery of unliganded ErbB receptors and demonstrates that all human ligand-binding ErbBs adopt the autoinhibited conformation.
16203964	2	50	from	events	322:327	arg1	tissues					352:358	embryonic and adult tissues	332:358	embryonic and adult tissues	332:358	ErbBs play fundamental roles in cell growth and differentiation events in embryonic and adult tissues, and inappropriate ErbB activity has been implicated in several human cancers.
16203964	5	51	theme	neuregulin-1beta	834:849	arg1	binding					878:884	the binding	874:884	the binding of betacellulin to both ErbB4 and ErbB1	874:924	We also show that the binding of neuregulin-1beta to ErbB4 and ErbB3 and the binding of betacellulin to both ErbB4 and ErbB1 does not decrease at low pH, unlike the binding of epidermal growth factor and transforming growth factor-alpha to ErbB1.
16203964	5	51	theme	neuregulin-1beta	834:849	arg1	binding					823:829	the binding	819:829	the binding of neuregulin-1beta to ErbB4 and ErbB3	819:868	We also show that the binding of neuregulin-1beta to ErbB4 and ErbB3 and the binding of betacellulin to both ErbB4 and ErbB1 does not decrease at low pH, unlike the binding of epidermal growth factor and transforming growth factor-alpha to ErbB1.
16203964	4	52	theme	unliganded	684:693	arg1	receptors					700:708	unliganded ErbB receptors	684:708	unliganded ErbB receptors	684:708	This structure completes the gallery of unliganded ErbB receptors and demonstrates that all human ligand-binding ErbBs adopt the autoinhibited conformation.
16203964	2	53	theme	cell	290:293	arg1	growth					295:300	cell growth	290:300	cell growth	290:300	ErbBs play fundamental roles in cell growth and differentiation events in embryonic and adult tissues, and inappropriate ErbB activity has been implicated in several human cancers.
16203964	2	54	theme	growth	295:300	arg1	events					322:327	cell growth and differentiation events	290:327	cell growth and differentiation events in embryonic and adult tissues	290:358	ErbBs play fundamental roles in cell growth and differentiation events in embryonic and adult tissues, and inappropriate ErbB activity has been implicated in several human cancers.
16203964	2	55	theme	human	424:428	arg1	cancers					430:436	several human cancers	416:436	several human cancers	416:436	ErbBs play fundamental roles in cell growth and differentiation events in embryonic and adult tissues, and inappropriate ErbB activity has been implicated in several human cancers.
16203964	5	56	theme	transforming	1005:1016	arg1	factor-alpha					1025:1036	transforming growth factor-alpha	1005:1036	transforming growth factor-alpha	1005:1036	We also show that the binding of neuregulin-1beta to ErbB4 and ErbB3 and the binding of betacellulin to both ErbB4 and ErbB1 does not decrease at low pH, unlike the binding of epidermal growth factor and transforming growth factor-alpha to ErbB1.
16203964	4	57	theme	receptors	700:708	arg1	gallery					673:679	the gallery	669:679	the gallery of unliganded ErbB receptors	669:708	This structure completes the gallery of unliganded ErbB receptors and demonstrates that all human ligand-binding ErbBs adopt the autoinhibited conformation.
16203964	0	58	theme	extracellular	4:16	arg1	region					18:23	The extracellular region	0:23	The extracellular region of ErbB4	0:32	The extracellular region of ErbB4 adopts a tethered conformation in the absence of ligand.
30004384	1	0	theme	polycystic	112:121	arg1	2-l1					159:162	polycystin 2-l1	148:162	polycystin 2-l1	148:162	We report the near atomic resolution (3.3 Å) of the human polycystic kidney disease 2-like 1 (polycystin 2-l1) ion channel.
30004384	1	0	theme	polycystic	112:121	arg1	disease					130:136	human polycystic kidney disease 2-like 1	106:145	the human polycystic kidney disease 2-like 1 (polycystin 2-l1) ion channel	102:175	We report the near atomic resolution (3.3 Å) of the human polycystic kidney disease 2-like 1 (polycystin 2-l1) ion channel.
30004384	1	1	theme	kidney	123:128	arg1	2-l1					159:162	polycystin 2-l1	148:162	polycystin 2-l1	148:162	We report the near atomic resolution (3.3 Å) of the human polycystic kidney disease 2-like 1 (polycystin 2-l1) ion channel.
30004384	1	1	theme	kidney	123:128	arg1	disease					130:136	human polycystic kidney disease 2-like 1	106:145	the human polycystic kidney disease 2-like 1 (polycystin 2-l1) ion channel	102:175	We report the near atomic resolution (3.3 Å) of the human polycystic kidney disease 2-like 1 (polycystin 2-l1) ion channel.
30004384	2	2	from	channel	261:267	arg1	cilia					280:284	primary cilia	272:284	primary cilia	272:284	Encoded by PKD2L1, polycystin 2-l1 is a calcium and monovalent cation-permeant ion channel in primary cilia and plasma membranes.
30004384	2	2	from	channel	261:267	arg1	membranes					297:305	plasma membranes	290:305	plasma membranes	290:305	Encoded by PKD2L1, polycystin 2-l1 is a calcium and monovalent cation-permeant ion channel in primary cilia and plasma membranes.
30004384	2	3	theme	plasma	290:295	arg1	membranes					297:305	plasma membranes	290:305	plasma membranes	290:305	Encoded by PKD2L1, polycystin 2-l1 is a calcium and monovalent cation-permeant ion channel in primary cilia and plasma membranes.
30004384	3	4	theme	distinct	436:443	arg1	characteristics					458:472	distinct permeability characteristics	436:472	distinct permeability characteristics	436:472	The related primary cilium-specific polycystin-2 protein, encoded by PKD2, shares a high degree of sequence similarity, yet has distinct permeability characteristics.
30004384	1	5	theme	disease	130:136	arg1	channel					169:175	the human polycystic kidney disease 2-like 1 (polycystin 2-l1) ion channel	102:175	the human polycystic kidney disease 2-like 1 (polycystin 2-l1) ion channel	102:175	We report the near atomic resolution (3.3 Å) of the human polycystic kidney disease 2-like 1 (polycystin 2-l1) ion channel.
30004384	3	6	contain	has	432:434	arg2	characteristics					458:472	distinct permeability characteristics	436:472	distinct permeability characteristics	436:472	The related primary cilium-specific polycystin-2 protein, encoded by PKD2, shares a high degree of sequence similarity, yet has distinct permeability characteristics.
30004384	3	6	contain	has	432:434	arg1	protein					357:363	The related primary cilium-specific polycystin-2 protein	308:363	The related primary cilium-specific polycystin-2 protein	308:363	The related primary cilium-specific polycystin-2 protein, encoded by PKD2, shares a high degree of sequence similarity, yet has distinct permeability characteristics.
30004384	3	7	theme	polycystin-2	344:355	arg1	protein					357:363	The related primary cilium-specific polycystin-2 protein	308:363	The related primary cilium-specific polycystin-2 protein	308:363	The related primary cilium-specific polycystin-2 protein, encoded by PKD2, shares a high degree of sequence similarity, yet has distinct permeability characteristics.
30004384	1	8	theme	2-like	138:143	arg1	2-l1					159:162	polycystin 2-l1	148:162	polycystin 2-l1	148:162	We report the near atomic resolution (3.3 Å) of the human polycystic kidney disease 2-like 1 (polycystin 2-l1) ion channel.
30004384	1	8	theme	2-like	138:143	arg1	disease					130:136	human polycystic kidney disease 2-like 1	106:145	the human polycystic kidney disease 2-like 1 (polycystin 2-l1) ion channel	102:175	We report the near atomic resolution (3.3 Å) of the human polycystic kidney disease 2-like 1 (polycystin 2-l1) ion channel.
30004384	3	9	theme	cilium-specific	328:342	arg1	protein					357:363	The related primary cilium-specific polycystin-2 protein	308:363	The related primary cilium-specific polycystin-2 protein	308:363	The related primary cilium-specific polycystin-2 protein, encoded by PKD2, shares a high degree of sequence similarity, yet has distinct permeability characteristics.
30004384	1	10	theme	near	68:71	arg1	resolution					80:89	the near atomic resolution	64:89	the near atomic resolution (3.3 Å) of the human polycystic kidney disease 2-like 1 (polycystin 2-l1) ion channel	64:175	We report the near atomic resolution (3.3 Å) of the human polycystic kidney disease 2-like 1 (polycystin 2-l1) ion channel.
30004384	1	10	theme	near	68:71	arg1	Å					96:96	3.3 Å	92:96	3.3 Å	92:96	We report the near atomic resolution (3.3 Å) of the human polycystic kidney disease 2-like 1 (polycystin 2-l1) ion channel.
30004384	0	11	theme	Cryo-EM	0:6	arg1	structure					8:16	Cryo-EM structure	0:16	Cryo-EM structure of the polycystin 2-l1 ion channel	0:51	Cryo-EM structure of the polycystin 2-l1 ion channel.
30004384	1	12	theme	atomic	73:78	arg1	resolution					80:89	the near atomic resolution	64:89	the near atomic resolution (3.3 Å) of the human polycystic kidney disease 2-like 1 (polycystin 2-l1) ion channel	64:175	We report the near atomic resolution (3.3 Å) of the human polycystic kidney disease 2-like 1 (polycystin 2-l1) ion channel.
30004384	1	12	theme	atomic	73:78	arg1	Å					96:96	3.3 Å	92:96	3.3 Å	92:96	We report the near atomic resolution (3.3 Å) of the human polycystic kidney disease 2-like 1 (polycystin 2-l1) ion channel.
30004384	3	13	theme	related	312:318	arg1	protein					357:363	The related primary cilium-specific polycystin-2 protein	308:363	The related primary cilium-specific polycystin-2 protein	308:363	The related primary cilium-specific polycystin-2 protein, encoded by PKD2, shares a high degree of sequence similarity, yet has distinct permeability characteristics.
30004384	2	14	theme	cation-permeant	241:255	arg1	channel					261:267	a calcium and monovalent cation-permeant ion channel	216:267	channel	261:267	Encoded by PKD2L1, polycystin 2-l1 is a calcium and monovalent cation-permeant ion channel in primary cilia and plasma membranes.
30004384	1	15	theme	polycystin	148:157	arg1	2-l1					159:162	polycystin 2-l1	148:162	polycystin 2-l1	148:162	We report the near atomic resolution (3.3 Å) of the human polycystic kidney disease 2-like 1 (polycystin 2-l1) ion channel.
30004384	1	15	theme	polycystin	148:157	arg1	disease					130:136	human polycystic kidney disease 2-like 1	106:145	the human polycystic kidney disease 2-like 1 (polycystin 2-l1) ion channel	102:175	We report the near atomic resolution (3.3 Å) of the human polycystic kidney disease 2-like 1 (polycystin 2-l1) ion channel.
30004384	2	16	theme	ion	257:259	arg1	channel					261:267	a calcium and monovalent cation-permeant ion channel	216:267	channel	261:267	Encoded by PKD2L1, polycystin 2-l1 is a calcium and monovalent cation-permeant ion channel in primary cilia and plasma membranes.
30004384	4	17	theme	2-l1	559:562	arg1	architecture					532:543	the architecture	528:543	the architecture of polycystin 2-l1	528:562	Here we show that these differences are reflected in the architecture of polycystin 2-l1.
30004384	2	18	theme	monovalent	230:239	arg1	channel					261:267	a calcium and monovalent cation-permeant ion channel	216:267	channel	261:267	Encoded by PKD2L1, polycystin 2-l1 is a calcium and monovalent cation-permeant ion channel in primary cilia and plasma membranes.
30004384	3	19	theme	sequence	407:414	arg1	similarity					416:425	sequence similarity	407:425	sequence similarity	407:425	The related primary cilium-specific polycystin-2 protein, encoded by PKD2, shares a high degree of sequence similarity, yet has distinct permeability characteristics.
30004384	0	20	theme	2-l1	36:39	arg1	channel					45:51	the polycystin 2-l1 ion channel	21:51	the polycystin 2-l1 ion channel	21:51	Cryo-EM structure of the polycystin 2-l1 ion channel.
30004384	3	21	theme	high	392:395	arg1	degree					397:402	a high degree	390:402	a high degree of sequence similarity	390:425	The related primary cilium-specific polycystin-2 protein, encoded by PKD2, shares a high degree of sequence similarity, yet has distinct permeability characteristics.
30004384	0	22	theme	polycystin	25:34	arg1	channel					45:51	the polycystin 2-l1 ion channel	21:51	the polycystin 2-l1 ion channel	21:51	Cryo-EM structure of the polycystin 2-l1 ion channel.
30004384	1	23	theme	ion	165:167	arg1	channel					169:175	the human polycystic kidney disease 2-like 1 (polycystin 2-l1) ion channel	102:175	the human polycystic kidney disease 2-like 1 (polycystin 2-l1) ion channel	102:175	We report the near atomic resolution (3.3 Å) of the human polycystic kidney disease 2-like 1 (polycystin 2-l1) ion channel.
30004384	0	24	theme	channel	45:51	arg1	structure					8:16	Cryo-EM structure	0:16	Cryo-EM structure of the polycystin 2-l1 ion channel	0:51	Cryo-EM structure of the polycystin 2-l1 ion channel.
30004384	0	25	theme	ion	41:43	arg1	channel					45:51	the polycystin 2-l1 ion channel	21:51	the polycystin 2-l1 ion channel	21:51	Cryo-EM structure of the polycystin 2-l1 ion channel.
30004384	3	26	theme	permeability	445:456	arg1	characteristics					458:472	distinct permeability characteristics	436:472	distinct permeability characteristics	436:472	The related primary cilium-specific polycystin-2 protein, encoded by PKD2, shares a high degree of sequence similarity, yet has distinct permeability characteristics.
30004384	2	27	theme	primary	272:278	arg1	cilia					280:284	primary cilia	272:284	primary cilia	272:284	Encoded by PKD2L1, polycystin 2-l1 is a calcium and monovalent cation-permeant ion channel in primary cilia and plasma membranes.
30004384	1	28	theme	channel	169:175	arg1	resolution					80:89	the near atomic resolution	64:89	the near atomic resolution (3.3 Å) of the human polycystic kidney disease 2-like 1 (polycystin 2-l1) ion channel	64:175	We report the near atomic resolution (3.3 Å) of the human polycystic kidney disease 2-like 1 (polycystin 2-l1) ion channel.
30004384	1	28	theme	channel	169:175	arg1	Å					96:96	3.3 Å	92:96	3.3 Å	92:96	We report the near atomic resolution (3.3 Å) of the human polycystic kidney disease 2-like 1 (polycystin 2-l1) ion channel.
30004384	2	29	theme	polycystin	197:206	arg1	calcium					218:224	a calcium and monovalent cation-permeant ion channel	216:267	calcium	218:224	Encoded by PKD2L1, polycystin 2-l1 is a calcium and monovalent cation-permeant ion channel in primary cilia and plasma membranes.
30004384	2	29	theme	polycystin	197:206	arg1	2-l1					208:211	polycystin 2-l1	197:211	polycystin 2-l1	197:211	Encoded by PKD2L1, polycystin 2-l1 is a calcium and monovalent cation-permeant ion channel in primary cilia and plasma membranes.
30004384	3	30	theme	similarity	416:425	arg1	degree					397:402	a high degree	390:402	a high degree of sequence similarity	390:425	The related primary cilium-specific polycystin-2 protein, encoded by PKD2, shares a high degree of sequence similarity, yet has distinct permeability characteristics.
30004384	2	31	from	calcium	218:224	arg1	cilia					280:284	primary cilia	272:284	primary cilia	272:284	Encoded by PKD2L1, polycystin 2-l1 is a calcium and monovalent cation-permeant ion channel in primary cilia and plasma membranes.
30004384	2	31	from	calcium	218:224	arg1	membranes					297:305	plasma membranes	290:305	plasma membranes	290:305	Encoded by PKD2L1, polycystin 2-l1 is a calcium and monovalent cation-permeant ion channel in primary cilia and plasma membranes.
30004384	3	32	theme	primary	320:326	arg1	protein					357:363	The related primary cilium-specific polycystin-2 protein	308:363	The related primary cilium-specific polycystin-2 protein	308:363	The related primary cilium-specific polycystin-2 protein, encoded by PKD2, shares a high degree of sequence similarity, yet has distinct permeability characteristics.
30004384	4	33	theme	polycystin	548:557	arg1	2-l1					559:562	polycystin 2-l1	548:562	polycystin 2-l1	548:562	Here we show that these differences are reflected in the architecture of polycystin 2-l1.
30004384	1	34	theme	human	106:110	arg1	2-l1					159:162	polycystin 2-l1	148:162	polycystin 2-l1	148:162	We report the near atomic resolution (3.3 Å) of the human polycystic kidney disease 2-like 1 (polycystin 2-l1) ion channel.
30004384	1	34	theme	human	106:110	arg1	disease					130:136	human polycystic kidney disease 2-like 1	106:145	the human polycystic kidney disease 2-like 1 (polycystin 2-l1) ion channel	102:175	We report the near atomic resolution (3.3 Å) of the human polycystic kidney disease 2-like 1 (polycystin 2-l1) ion channel.
16874306	5	0	theme	human	615:619	arg1	CD1b					621:624	human CD1b	615:624	human CD1b	615:624	Using isoelectric focusing, native mass spectrometry and resolving the crystal structure at 1.8 A resolution, we found that human CD1b is simultaneously associated with endogenous phosphatidylcholine (PC) and a 41-44 carbon atoms-long spacer molecule.
16874306	7	1	theme	ligands	938:944	arg1	binding					927:933	binding	927:933	binding of ligands with long lipid tails	927:966	We propose that the spacer serves to prevent binding of ligands with long lipid tails, whereas short-chain lipids might still displace the PC, which is exposed at the groove entrance.
16874306	3	2	theme	biosynthesis	307:318	arg1	moment					297:302	the moment	293:302	the moment of biosynthesis in the endoplasmic reticulum and arrival to the endosomes	293:376	This raises the question of how the large hydrophobic CD1 pockets are preserved between the moment of biosynthesis in the endoplasmic reticulum and arrival to the endosomes.
16874306	6	3	theme	groove	865:870	arg1	capacity					872:879	the maximal groove capacity	853:879	the maximal groove capacity	853:879	The two lipids appear to work in concert to stabilize the CD1b groove, their combined size slightly exceeding the maximal groove capacity.
16874306	0	4	theme	CD1b	94:97	arg1	groove					84:89	the lipid-binding groove	66:89	the lipid-binding groove of CD1b	66:97	Endogenous phosphatidylcholine and a long spacer ligand stabilize the lipid-binding groove of CD1b.
16874306	6	5	theme	maximal	857:863	arg1	capacity					872:879	the maximal groove capacity	853:879	the maximal groove capacity	853:879	The two lipids appear to work in concert to stabilize the CD1b groove, their combined size slightly exceeding the maximal groove capacity.
16874306	7	6	theme	groove	1049:1054	arg1	entrance					1056:1063	the groove entrance	1045:1063	the groove entrance	1045:1063	We propose that the spacer serves to prevent binding of ligands with long lipid tails, whereas short-chain lipids might still displace the PC, which is exposed at the groove entrance.
16874306	5	7	theme	A	587:587	arg1	resolution					589:598	1.8 A resolution	583:598	1.8 A resolution	583:598	Using isoelectric focusing, native mass spectrometry and resolving the crystal structure at 1.8 A resolution, we found that human CD1b is simultaneously associated with endogenous phosphatidylcholine (PC) and a 41-44 carbon atoms-long spacer molecule.
16874306	3	8	theme	endoplasmic	327:337	arg1	reticulum					339:347	the endoplasmic reticulum	323:347	the endoplasmic reticulum	323:347	This raises the question of how the large hydrophobic CD1 pockets are preserved between the moment of biosynthesis in the endoplasmic reticulum and arrival to the endosomes.
16874306	8	9	theme	CD1b	1108:1111	arg1	groove					1113:1118	the CD1b groove	1104:1118	the CD1b groove	1104:1118	The data presented herein explain how the CD1b groove is preserved, and provide a rationale for the in vivo antigen-binding properties of CD1b.
16874306	5	10	theme	atoms-long	715:724	arg1	molecule					733:740	a 41-44 carbon atoms-long spacer molecule	700:740	a 41-44 carbon atoms-long spacer molecule	700:740	Using isoelectric focusing, native mass spectrometry and resolving the crystal structure at 1.8 A resolution, we found that human CD1b is simultaneously associated with endogenous phosphatidylcholine (PC) and a 41-44 carbon atoms-long spacer molecule.
16874306	4	11	theme	CD1b	462:465	arg1	form					448:451	a soluble form	438:451	a soluble form of human CD1b	438:465	To address this issue, the natural ligands associated with a soluble form of human CD1b have been investigated.
16874306	3	12	theme	large	241:245	arg1	pockets					263:269	the large hydrophobic CD1 pockets	237:269	the large hydrophobic CD1 pockets	237:269	This raises the question of how the large hydrophobic CD1 pockets are preserved between the moment of biosynthesis in the endoplasmic reticulum and arrival to the endosomes.
16874306	5	13	theme	carbon	708:713	arg1	molecule					733:740	a 41-44 carbon atoms-long spacer molecule	700:740	a 41-44 carbon atoms-long spacer molecule	700:740	Using isoelectric focusing, native mass spectrometry and resolving the crystal structure at 1.8 A resolution, we found that human CD1b is simultaneously associated with endogenous phosphatidylcholine (PC) and a 41-44 carbon atoms-long spacer molecule.
16874306	4	14	theme	human	456:460	arg1	CD1b					462:465	human CD1b	456:465	human CD1b	456:465	To address this issue, the natural ligands associated with a soluble form of human CD1b have been investigated.
16874306	5	15	theme	spacer	726:731	arg1	molecule					733:740	a 41-44 carbon atoms-long spacer molecule	700:740	a 41-44 carbon atoms-long spacer molecule	700:740	Using isoelectric focusing, native mass spectrometry and resolving the crystal structure at 1.8 A resolution, we found that human CD1b is simultaneously associated with endogenous phosphatidylcholine (PC) and a 41-44 carbon atoms-long spacer molecule.
16874306	0	16	theme	Endogenous	0:9	arg1	phosphatidylcholine					11:29	Endogenous phosphatidylcholine	0:29	Endogenous phosphatidylcholine	0:29	Endogenous phosphatidylcholine and a long spacer ligand stabilize the lipid-binding groove of CD1b.
16874306	5	17	theme	crystal	562:568	arg1	structure					570:578	the crystal structure	558:578	the crystal structure at 1.8 A resolution	558:598	Using isoelectric focusing, native mass spectrometry and resolving the crystal structure at 1.8 A resolution, we found that human CD1b is simultaneously associated with endogenous phosphatidylcholine (PC) and a 41-44 carbon atoms-long spacer molecule.
16874306	8	18	dep	in	1166:1167	arg1	vivo					1169:1172	vivo	1169:1172	vivo	1169:1172	The data presented herein explain how the CD1b groove is preserved, and provide a rationale for the in vivo antigen-binding properties of CD1b.
16874306	5	19	dep	focusing	509:516	arg1	isoelectric					497:507	isoelectric	497:507	isoelectric	497:507	Using isoelectric focusing, native mass spectrometry and resolving the crystal structure at 1.8 A resolution, we found that human CD1b is simultaneously associated with endogenous phosphatidylcholine (PC) and a 41-44 carbon atoms-long spacer molecule.
16874306	6	20	theme	combined	820:827	arg1	groove					806:811	the CD1b groove	797:811	the CD1b groove	797:811	The two lipids appear to work in concert to stabilize the CD1b groove, their combined size slightly exceeding the maximal groove capacity.
16874306	6	20	theme	combined	820:827	arg1	size					829:832	their combined size	814:832	their combined size slightly exceeding the maximal groove capacity	814:879	The two lipids appear to work in concert to stabilize the CD1b groove, their combined size slightly exceeding the maximal groove capacity.
16874306	1	21	theme	CD1	100:102	arg1	proteins					104:111	CD1 proteins	100:111	CD1 proteins	100:111	CD1 proteins present lipid antigens to T cells.
16874306	7	22	theme	short-chain	977:987	arg1	lipids					989:994	short-chain lipids	977:994	short-chain lipids	977:994	We propose that the spacer serves to prevent binding of ligands with long lipid tails, whereas short-chain lipids might still displace the PC, which is exposed at the groove entrance.
16874306	8	23	theme	antigen-binding	1174:1188	arg1	properties					1190:1199	the in vivo antigen-binding properties	1162:1199	the in vivo antigen-binding properties of CD1b	1162:1207	The data presented herein explain how the CD1b groove is preserved, and provide a rationale for the in vivo antigen-binding properties of CD1b.
16874306	0	24	theme	spacer	42:47	arg1	ligand					49:54	a long spacer ligand	35:54	a long spacer ligand	35:54	Endogenous phosphatidylcholine and a long spacer ligand stabilize the lipid-binding groove of CD1b.
16874306	3	25	theme	hydrophobic	247:257	arg1	pockets					263:269	the large hydrophobic CD1 pockets	237:269	the large hydrophobic CD1 pockets	237:269	This raises the question of how the large hydrophobic CD1 pockets are preserved between the moment of biosynthesis in the endoplasmic reticulum and arrival to the endosomes.
16874306	3	26	from	reticulum	339:347	arg1	moment					297:302	the moment	293:302	the moment of biosynthesis in the endoplasmic reticulum and arrival to the endosomes	293:376	This raises the question of how the large hydrophobic CD1 pockets are preserved between the moment of biosynthesis in the endoplasmic reticulum and arrival to the endosomes.
16874306	8	27	theme	in	1166:1167	arg1	properties					1190:1199	the in vivo antigen-binding properties	1162:1199	the in vivo antigen-binding properties of CD1b	1162:1207	The data presented herein explain how the CD1b groove is preserved, and provide a rationale for the in vivo antigen-binding properties of CD1b.
16874306	8	28	theme	CD1b	1204:1207	arg1	properties					1190:1199	the in vivo antigen-binding properties	1162:1199	the in vivo antigen-binding properties of CD1b	1162:1207	The data presented herein explain how the CD1b groove is preserved, and provide a rationale for the in vivo antigen-binding properties of CD1b.
16874306	0	29	theme	long	37:40	arg1	ligand					49:54	a long spacer ligand	35:54	a long spacer ligand	35:54	Endogenous phosphatidylcholine and a long spacer ligand stabilize the lipid-binding groove of CD1b.
16874306	3	30	theme	CD1	259:261	arg1	pockets					263:269	the large hydrophobic CD1 pockets	237:269	the large hydrophobic CD1 pockets	237:269	This raises the question of how the large hydrophobic CD1 pockets are preserved between the moment of biosynthesis in the endoplasmic reticulum and arrival to the endosomes.
16874306	4	31	theme	soluble	440:446	arg1	form					448:451	a soluble form	438:451	a soluble form of human CD1b	438:465	To address this issue, the natural ligands associated with a soluble form of human CD1b have been investigated.
16874306	5	32	theme	native	519:524	arg1	focusing					509:516	focusing	509:516	focusing	509:516	Using isoelectric focusing, native mass spectrometry and resolving the crystal structure at 1.8 A resolution, we found that human CD1b is simultaneously associated with endogenous phosphatidylcholine (PC) and a 41-44 carbon atoms-long spacer molecule.
16874306	5	32	theme	native	519:524	arg1	spectrometry					531:542	native mass spectrometry	519:542	native mass spectrometry	519:542	Using isoelectric focusing, native mass spectrometry and resolving the crystal structure at 1.8 A resolution, we found that human CD1b is simultaneously associated with endogenous phosphatidylcholine (PC) and a 41-44 carbon atoms-long spacer molecule.
16874306	3	33	from	arrival	353:359	arg1	moment					297:302	the moment	293:302	the moment of biosynthesis in the endoplasmic reticulum and arrival to the endosomes	293:376	This raises the question of how the large hydrophobic CD1 pockets are preserved between the moment of biosynthesis in the endoplasmic reticulum and arrival to the endosomes.
16874306	5	34	theme	mass	526:529	arg1	focusing					509:516	focusing	509:516	focusing	509:516	Using isoelectric focusing, native mass spectrometry and resolving the crystal structure at 1.8 A resolution, we found that human CD1b is simultaneously associated with endogenous phosphatidylcholine (PC) and a 41-44 carbon atoms-long spacer molecule.
16874306	5	34	theme	mass	526:529	arg1	spectrometry					531:542	native mass spectrometry	519:542	native mass spectrometry	519:542	Using isoelectric focusing, native mass spectrometry and resolving the crystal structure at 1.8 A resolution, we found that human CD1b is simultaneously associated with endogenous phosphatidylcholine (PC) and a 41-44 carbon atoms-long spacer molecule.
16874306	6	35	theme	CD1b	801:804	arg1	groove					806:811	the CD1b groove	797:811	the CD1b groove	797:811	The two lipids appear to work in concert to stabilize the CD1b groove, their combined size slightly exceeding the maximal groove capacity.
16874306	6	35	theme	CD1b	801:804	arg1	size					829:832	their combined size	814:832	their combined size slightly exceeding the maximal groove capacity	814:879	The two lipids appear to work in concert to stabilize the CD1b groove, their combined size slightly exceeding the maximal groove capacity.
16874306	7	36	theme	lipid	956:960	arg1	tails					962:966	long lipid tails	951:966	long lipid tails	951:966	We propose that the spacer serves to prevent binding of ligands with long lipid tails, whereas short-chain lipids might still displace the PC, which is exposed at the groove entrance.
16874306	1	37	theme	lipid	121:125	arg1	antigens					127:134	lipid antigens	121:134	lipid antigens	121:134	CD1 proteins present lipid antigens to T cells.
16874306	7	38	with	binding	927:933	arg1	tails					962:966	long lipid tails	951:966	long lipid tails	951:966	We propose that the spacer serves to prevent binding of ligands with long lipid tails, whereas short-chain lipids might still displace the PC, which is exposed at the groove entrance.
16874306	5	39	theme	endogenous	660:669	arg1	PC					692:693	PC	692:693	PC	692:693	Using isoelectric focusing, native mass spectrometry and resolving the crystal structure at 1.8 A resolution, we found that human CD1b is simultaneously associated with endogenous phosphatidylcholine (PC) and a 41-44 carbon atoms-long spacer molecule.
16874306	5	39	theme	endogenous	660:669	arg1	phosphatidylcholine					671:689	endogenous phosphatidylcholine	660:689	endogenous phosphatidylcholine (PC)	660:694	Using isoelectric focusing, native mass spectrometry and resolving the crystal structure at 1.8 A resolution, we found that human CD1b is simultaneously associated with endogenous phosphatidylcholine (PC) and a 41-44 carbon atoms-long spacer molecule.
16874306	3	40	from	biosynthesis	307:318	arg1	reticulum					339:347	the endoplasmic reticulum	323:347	the endoplasmic reticulum	323:347	This raises the question of how the large hydrophobic CD1 pockets are preserved between the moment of biosynthesis in the endoplasmic reticulum and arrival to the endosomes.
16874306	3	40	from	biosynthesis	307:318	arg1	arrival					353:359	arrival	353:359	arrival to the endosomes	353:376	This raises the question of how the large hydrophobic CD1 pockets are preserved between the moment of biosynthesis in the endoplasmic reticulum and arrival to the endosomes.
16874306	2	41	theme	endosomal	181:189	arg1	compartments					191:202	the endosomal compartments	177:202	the endosomal compartments	177:202	The antigens are acquired in the endosomal compartments.
16874306	0	42	theme	lipid-binding	70:82	arg1	groove					84:89	the lipid-binding groove	66:89	the lipid-binding groove of CD1b	66:97	Endogenous phosphatidylcholine and a long spacer ligand stabilize the lipid-binding groove of CD1b.
16874306	4	43	theme	natural	406:412	arg1	ligands					414:420	the natural ligands	402:420	the natural ligands associated with a soluble form of human CD1b	402:465	To address this issue, the natural ligands associated with a soluble form of human CD1b have been investigated.
16874306	7	44	theme	long	951:954	arg1	tails					962:966	long lipid tails	951:966	long lipid tails	951:966	We propose that the spacer serves to prevent binding of ligands with long lipid tails, whereas short-chain lipids might still displace the PC, which is exposed at the groove entrance.
16874306	1	45	theme	T	139:139	arg1	cells					141:145	T cells	139:145	T cells	139:145	CD1 proteins present lipid antigens to T cells.
16874306	5	46	from	resolution	589:598	arg1	structure					570:578	the crystal structure	558:578	the crystal structure at 1.8 A resolution	558:598	Using isoelectric focusing, native mass spectrometry and resolving the crystal structure at 1.8 A resolution, we found that human CD1b is simultaneously associated with endogenous phosphatidylcholine (PC) and a 41-44 carbon atoms-long spacer molecule.
16874306	3	47	from	moment	297:302	arg1	reticulum					339:347	the endoplasmic reticulum	323:347	the endoplasmic reticulum	323:347	This raises the question of how the large hydrophobic CD1 pockets are preserved between the moment of biosynthesis in the endoplasmic reticulum and arrival to the endosomes.
16874306	3	47	from	moment	297:302	arg1	arrival					353:359	arrival	353:359	arrival to the endosomes	353:376	This raises the question of how the large hydrophobic CD1 pockets are preserved between the moment of biosynthesis in the endoplasmic reticulum and arrival to the endosomes.
32337544	7	0	theme	glycoproteomics	1158:1172	arg1	workflow					1174:1181	a specialized glycoproteomics workflow	1144:1181	a specialized glycoproteomics workflow	1144:1181	To address this question, VAR2CSA-binding proteoglycans were affinity-purified from the human placenta, tumor tissues and cancer cells and analyzed through a specialized glycoproteomics workflow.
32337544	9	1	theme	glycoproteomics	1392:1406	arg1	analysis					1408:1415	glycoproteomics analysis	1392:1415	glycoproteomics analysis	1392:1415	Additionally, this work demonstrates how affinity purification in combination with glycoproteomics analysis can facilitate the characterization of CSPGs with distinct CS epitopes.
32337544	1	2	theme	malaria	239:245	arg1	protein					247:253	the VAR2CSA malaria protein	227:253	the VAR2CSA malaria protein	227:253	Chondroitin sulfate (CS) is the placental receptor for the VAR2CSA malaria protein, expressed at the surface of infected erythrocytes during Plasmodium falciparum infection.
32337544	0	3	theme	sulfate	83:89	arg1	proteoglycans					91:103	the chondroitin sulfate proteoglycans	67:103	the chondroitin sulfate proteoglycans that interact with malarial VAR2CSA in the placenta and in cancer	67:169	An affinity chromatography and glycoproteomics workflow to profile the chondroitin sulfate proteoglycans that interact with malarial VAR2CSA in the placenta and in cancer.
32337544	2	4	from	determinant	453:463	arg1	chains					486:491	a 4-O-sulfated CS chains	468:491	a 4-O-sulfated CS chains	468:491	Infected cells adhere to syncytiotrophoblasts or get trapped within the intervillous space by binding to a determinant in a 4-O-sulfated CS chains.
32337544	9	5	with	CSPGs	1456:1460	arg1	epitopes					1479:1486	distinct CS epitopes	1467:1486	distinct CS epitopes	1467:1486	Additionally, this work demonstrates how affinity purification in combination with glycoproteomics analysis can facilitate the characterization of CSPGs with distinct CS epitopes.
32337544	3	6	theme	exact	507:511	arg1	structure					513:521	the exact structure	503:521	the exact structure of these glycan sequences	503:547	However, the exact structure of these glycan sequences remains unclear.
32337544	10	7	theme	other	1568:1572	arg1	lectins					1585:1591	other CS binding lectins	1568:1591	other CS binding lectins as well	1568:1599	A similar workflow can be applied to investigate the interaction of CSPGs with other CS binding lectins as well.
32337544	7	8	from	tissues	1098:1104	arg1	affinity-purified					1049:1065	affinity-purified	1049:1065	affinity-purified	1049:1065	To address this question, VAR2CSA-binding proteoglycans were affinity-purified from the human placenta, tumor tissues and cancer cells and analyzed through a specialized glycoproteomics workflow.
32337544	8	9	theme	CS	1214:1215	arg1	chains					1217:1222	VAR2CSA-reactive CS chains	1197:1222	VAR2CSA-reactive CS chains	1197:1222	We show that VAR2CSA-reactive CS chains associate with a heterogenous group of proteoglycans, including novel core proteins.
32337544	3	10	theme	sequences	539:547	arg1	structure					513:521	the exact structure	503:521	the exact structure of these glycan sequences	503:547	However, the exact structure of these glycan sequences remains unclear.
32337544	4	11	theme	cancer	655:660	arg1	diagnosis					662:670	cancer diagnosis	655:670	cancer diagnosis	655:670	VAR2CSA-reactive CS is also expressed by tumor cells, making it an attractive target for cancer diagnosis and therapeutics.
32337544	8	12	theme	VAR2CSA-reactive	1197:1212	arg1	chains					1217:1222	VAR2CSA-reactive CS chains	1197:1222	VAR2CSA-reactive CS chains	1197:1222	We show that VAR2CSA-reactive CS chains associate with a heterogenous group of proteoglycans, including novel core proteins.
32337544	6	13	theme	core	921:924	arg1	proteins					926:933	novel core proteins	915:933	novel core proteins	915:933	This information is clinically relevant since presentation of the glycan chains may be mediated by novel core proteins or by a limited subset of established proteoglycans.
32337544	7	14	theme	specialized	1146:1156	arg1	workflow					1174:1181	a specialized glycoproteomics workflow	1144:1181	a specialized glycoproteomics workflow	1144:1181	To address this question, VAR2CSA-binding proteoglycans were affinity-purified from the human placenta, tumor tissues and cancer cells and analyzed through a specialized glycoproteomics workflow.
32337544	10	15	theme	CS	1574:1575	arg1	lectins					1585:1591	other CS binding lectins	1568:1591	other CS binding lectins as well	1568:1599	A similar workflow can be applied to investigate the interaction of CSPGs with other CS binding lectins as well.
32337544	0	16	theme	malarial	124:131	arg1	VAR2CSA					133:139	malarial VAR2CSA	124:139	malarial VAR2CSA in the placenta and in cancer	124:169	An affinity chromatography and glycoproteomics workflow to profile the chondroitin sulfate proteoglycans that interact with malarial VAR2CSA in the placenta and in cancer.
32337544	6	17	theme	novel	915:919	arg1	proteins					926:933	novel core proteins	915:933	novel core proteins	915:933	This information is clinically relevant since presentation of the glycan chains may be mediated by novel core proteins or by a limited subset of established proteoglycans.
32337544	10	18	theme	CSPGs	1557:1561	arg1	interaction					1542:1552	the interaction	1538:1552	the interaction of CSPGs with other CS binding lectins as well	1538:1599	A similar workflow can be applied to investigate the interaction of CSPGs with other CS binding lectins as well.
32337544	1	19	theme	Chondroitin	172:182	arg1	receptor					214:221	the placental receptor	200:221	the placental receptor for the VAR2CSA malaria protein, expressed at the surface of infected erythrocytes during Plasmodium falciparum infection	200:343	Chondroitin sulfate (CS) is the placental receptor for the VAR2CSA malaria protein, expressed at the surface of infected erythrocytes during Plasmodium falciparum infection.
32337544	1	19	theme	Chondroitin	172:182	arg1	CS					193:194	CS	193:194	CS	193:194	Chondroitin sulfate (CS) is the placental receptor for the VAR2CSA malaria protein, expressed at the surface of infected erythrocytes during Plasmodium falciparum infection.
32337544	1	19	theme	Chondroitin	172:182	arg1	sulfate					184:190	Chondroitin sulfate	172:190	Chondroitin sulfate (CS)	172:195	Chondroitin sulfate (CS) is the placental receptor for the VAR2CSA malaria protein, expressed at the surface of infected erythrocytes during Plasmodium falciparum infection.
32337544	5	20	theme	placental	758:766	arg1	tissues					779:785	placental and cancer tissues	758:785	placental and cancer tissues	758:785	The identities of the proteoglycans carrying these modifications in placental and cancer tissues remain poorly characterized.
32337544	8	21	theme	proteoglycans	1263:1275	arg1	proteins					1299:1306	novel core proteins	1288:1306	novel core proteins	1288:1306	We show that VAR2CSA-reactive CS chains associate with a heterogenous group of proteoglycans, including novel core proteins.
32337544	8	21	theme	proteoglycans	1263:1275	arg1	proteoglycans					1263:1275	proteoglycans	1263:1275	proteoglycans	1263:1275	We show that VAR2CSA-reactive CS chains associate with a heterogenous group of proteoglycans, including novel core proteins.
32337544	8	21	theme	proteoglycans	1263:1275	arg1	group					1254:1258	a heterogenous group	1239:1258	a heterogenous group of proteoglycans, including novel core proteins	1239:1306	We show that VAR2CSA-reactive CS chains associate with a heterogenous group of proteoglycans, including novel core proteins.
32337544	3	22	theme	glycan	532:537	arg1	sequences					539:547	these glycan sequences	526:547	these glycan sequences	526:547	However, the exact structure of these glycan sequences remains unclear.
32337544	8	23	theme	novel	1288:1292	arg1	proteins					1299:1306	novel core proteins	1288:1306	novel core proteins	1288:1306	We show that VAR2CSA-reactive CS chains associate with a heterogenous group of proteoglycans, including novel core proteins.
32337544	0	24	theme	affinity	3:10	arg1	chromatography					12:25	An affinity chromatography	0:25	An affinity chromatography	0:25	An affinity chromatography and glycoproteomics workflow to profile the chondroitin sulfate proteoglycans that interact with malarial VAR2CSA in the placenta and in cancer.
32337544	6	25	theme	proteoglycans	973:985	arg1	subset					951:956	a limited subset	941:956	a limited subset of established proteoglycans	941:985	This information is clinically relevant since presentation of the glycan chains may be mediated by novel core proteins or by a limited subset of established proteoglycans.
32337544	7	26	from	cells	1117:1121	arg1	affinity-purified					1049:1065	affinity-purified	1049:1065	affinity-purified	1049:1065	To address this question, VAR2CSA-binding proteoglycans were affinity-purified from the human placenta, tumor tissues and cancer cells and analyzed through a specialized glycoproteomics workflow.
32337544	7	27	theme	tumor	1092:1096	arg1	tissues					1098:1104	tumor tissues	1092:1104	tumor tissues	1092:1104	To address this question, VAR2CSA-binding proteoglycans were affinity-purified from the human placenta, tumor tissues and cancer cells and analyzed through a specialized glycoproteomics workflow.
32337544	5	28	contain	carrying	726:733	arg1	proteoglycans					712:724	the proteoglycans	708:724	the proteoglycans carrying these modifications in placental and cancer tissues	708:785	The identities of the proteoglycans carrying these modifications in placental and cancer tissues remain poorly characterized.
32337544	5	28	contain	carrying	726:733	arg2	modifications					741:753	these modifications	735:753	these modifications	735:753	The identities of the proteoglycans carrying these modifications in placental and cancer tissues remain poorly characterized.
32337544	6	29	theme	limited	943:949	arg1	subset					951:956	a limited subset	941:956	a limited subset of established proteoglycans	941:985	This information is clinically relevant since presentation of the glycan chains may be mediated by novel core proteins or by a limited subset of established proteoglycans.
32337544	10	30	theme	similar	1491:1497	arg1	workflow					1499:1506	A similar workflow	1489:1506	A similar workflow	1489:1506	A similar workflow can be applied to investigate the interaction of CSPGs with other CS binding lectins as well.
32337544	10	31	with	interaction	1542:1552	arg1	lectins					1585:1591	other CS binding lectins	1568:1591	other CS binding lectins as well	1568:1599	A similar workflow can be applied to investigate the interaction of CSPGs with other CS binding lectins as well.
32337544	10	32	theme	binding	1577:1583	arg1	lectins					1585:1591	other CS binding lectins	1568:1591	other CS binding lectins as well	1568:1599	A similar workflow can be applied to investigate the interaction of CSPGs with other CS binding lectins as well.
32337544	8	33	theme	heterogenous	1241:1252	arg1	proteins					1299:1306	novel core proteins	1288:1306	novel core proteins	1288:1306	We show that VAR2CSA-reactive CS chains associate with a heterogenous group of proteoglycans, including novel core proteins.
32337544	8	33	theme	heterogenous	1241:1252	arg1	proteoglycans					1263:1275	proteoglycans	1263:1275	proteoglycans	1263:1275	We show that VAR2CSA-reactive CS chains associate with a heterogenous group of proteoglycans, including novel core proteins.
32337544	8	33	theme	heterogenous	1241:1252	arg1	group					1254:1258	a heterogenous group	1239:1258	a heterogenous group of proteoglycans, including novel core proteins	1239:1306	We show that VAR2CSA-reactive CS chains associate with a heterogenous group of proteoglycans, including novel core proteins.
32337544	7	34	theme	cancer	1110:1115	arg1	cells					1117:1121	cancer cells	1110:1121	cancer cells	1110:1121	To address this question, VAR2CSA-binding proteoglycans were affinity-purified from the human placenta, tumor tissues and cancer cells and analyzed through a specialized glycoproteomics workflow.
32337544	2	35	theme	CS	483:484	arg1	chains					486:491	a 4-O-sulfated CS chains	468:491	a 4-O-sulfated CS chains	468:491	Infected cells adhere to syncytiotrophoblasts or get trapped within the intervillous space by binding to a determinant in a 4-O-sulfated CS chains.
32337544	4	36	theme	VAR2CSA-reactive	566:581	arg1	CS					583:584	VAR2CSA-reactive CS	566:584	VAR2CSA-reactive CS	566:584	VAR2CSA-reactive CS is also expressed by tumor cells, making it an attractive target for cancer diagnosis and therapeutics.
32337544	5	37	theme	proteoglycans	712:724	arg1	identities					694:703	The identities	690:703	The identities of the proteoglycans carrying these modifications in placental and cancer tissues	690:785	The identities of the proteoglycans carrying these modifications in placental and cancer tissues remain poorly characterized.
32337544	2	38	theme	intervillous	418:429	arg1	space					431:435	the intervillous space	414:435	the intervillous space	414:435	Infected cells adhere to syncytiotrophoblasts or get trapped within the intervillous space by binding to a determinant in a 4-O-sulfated CS chains.
32337544	2	39	theme	4-O-sulfated	470:481	arg1	chains					486:491	a 4-O-sulfated CS chains	468:491	a 4-O-sulfated CS chains	468:491	Infected cells adhere to syncytiotrophoblasts or get trapped within the intervillous space by binding to a determinant in a 4-O-sulfated CS chains.
32337544	1	40	theme	infected	284:291	arg1	erythrocytes					293:304	infected erythrocytes	284:304	infected erythrocytes	284:304	Chondroitin sulfate (CS) is the placental receptor for the VAR2CSA malaria protein, expressed at the surface of infected erythrocytes during Plasmodium falciparum infection.
32337544	9	41	from	purification	1359:1370	arg1	combination					1375:1385	combination	1375:1385	combination with glycoproteomics analysis	1375:1415	Additionally, this work demonstrates how affinity purification in combination with glycoproteomics analysis can facilitate the characterization of CSPGs with distinct CS epitopes.
32337544	6	42	theme	chains	889:894	arg1	presentation					862:873	presentation	862:873	presentation of the glycan chains	862:894	This information is clinically relevant since presentation of the glycan chains may be mediated by novel core proteins or by a limited subset of established proteoglycans.
32337544	1	43	theme	placental	204:212	arg1	receptor					214:221	the placental receptor	200:221	the placental receptor for the VAR2CSA malaria protein, expressed at the surface of infected erythrocytes during Plasmodium falciparum infection	200:343	Chondroitin sulfate (CS) is the placental receptor for the VAR2CSA malaria protein, expressed at the surface of infected erythrocytes during Plasmodium falciparum infection.
32337544	1	43	theme	placental	204:212	arg1	sulfate					184:190	Chondroitin sulfate	172:190	Chondroitin sulfate (CS)	172:195	Chondroitin sulfate (CS) is the placental receptor for the VAR2CSA malaria protein, expressed at the surface of infected erythrocytes during Plasmodium falciparum infection.
32337544	1	44	theme	erythrocytes	293:304	arg1	surface					273:279	the surface	269:279	the surface of infected erythrocytes	269:304	Chondroitin sulfate (CS) is the placental receptor for the VAR2CSA malaria protein, expressed at the surface of infected erythrocytes during Plasmodium falciparum infection.
32337544	6	45	theme	glycan	882:887	arg1	chains					889:894	the glycan chains	878:894	the glycan chains	878:894	This information is clinically relevant since presentation of the glycan chains may be mediated by novel core proteins or by a limited subset of established proteoglycans.
32337544	2	46	theme	Infected	346:353	arg1	cells					355:359	Infected cells	346:359	Infected cells	346:359	Infected cells adhere to syncytiotrophoblasts or get trapped within the intervillous space by binding to a determinant in a 4-O-sulfated CS chains.
32337544	9	47	theme	affinity	1350:1357	arg1	purification					1359:1370	affinity purification	1350:1370	affinity purification in combination with glycoproteomics analysis	1350:1415	Additionally, this work demonstrates how affinity purification in combination with glycoproteomics analysis can facilitate the characterization of CSPGs with distinct CS epitopes.
32337544	9	48	theme	CSPGs	1456:1460	arg1	characterization					1436:1451	the characterization	1432:1451	the characterization of CSPGs with distinct CS epitopes	1432:1486	Additionally, this work demonstrates how affinity purification in combination with glycoproteomics analysis can facilitate the characterization of CSPGs with distinct CS epitopes.
32337544	9	49	theme	CS	1476:1477	arg1	epitopes					1479:1486	distinct CS epitopes	1467:1486	distinct CS epitopes	1467:1486	Additionally, this work demonstrates how affinity purification in combination with glycoproteomics analysis can facilitate the characterization of CSPGs with distinct CS epitopes.
32337544	4	50	dep	it	627:628	arg1	target					644:649	an attractive target	630:649	it an attractive target for cancer diagnosis and therapeutics	627:687	VAR2CSA-reactive CS is also expressed by tumor cells, making it an attractive target for cancer diagnosis and therapeutics.
32337544	1	51	theme	Plasmodium	313:322	arg1	falciparum					324:333	Plasmodium falciparum	313:333	Plasmodium falciparum infection	313:343	Chondroitin sulfate (CS) is the placental receptor for the VAR2CSA malaria protein, expressed at the surface of infected erythrocytes during Plasmodium falciparum infection.
32337544	6	52	theme	established	961:971	arg1	proteoglycans					973:985	established proteoglycans	961:985	established proteoglycans	961:985	This information is clinically relevant since presentation of the glycan chains may be mediated by novel core proteins or by a limited subset of established proteoglycans.
32337544	9	53	theme	distinct	1467:1474	arg1	epitopes					1479:1486	distinct CS epitopes	1467:1486	distinct CS epitopes	1467:1486	Additionally, this work demonstrates how affinity purification in combination with glycoproteomics analysis can facilitate the characterization of CSPGs with distinct CS epitopes.
32337544	7	54	theme	human	1076:1080	arg1	placenta					1082:1089	the human placenta	1072:1089	the human placenta	1072:1089	To address this question, VAR2CSA-binding proteoglycans were affinity-purified from the human placenta, tumor tissues and cancer cells and analyzed through a specialized glycoproteomics workflow.
32337544	4	55	theme	tumor	607:611	arg1	cells					613:617	tumor cells	607:617	tumor cells	607:617	VAR2CSA-reactive CS is also expressed by tumor cells, making it an attractive target for cancer diagnosis and therapeutics.
32337544	0	56	theme	chondroitin	71:81	arg1	proteoglycans					91:103	the chondroitin sulfate proteoglycans	67:103	the chondroitin sulfate proteoglycans that interact with malarial VAR2CSA in the placenta and in cancer	67:169	An affinity chromatography and glycoproteomics workflow to profile the chondroitin sulfate proteoglycans that interact with malarial VAR2CSA in the placenta and in cancer.
32337544	4	57	theme	attractive	633:642	arg1	target					644:649	an attractive target	630:649	it an attractive target for cancer diagnosis and therapeutics	627:687	VAR2CSA-reactive CS is also expressed by tumor cells, making it an attractive target for cancer diagnosis and therapeutics.
32337544	7	58	theme	VAR2CSA-binding	1014:1028	arg1	proteoglycans					1030:1042	VAR2CSA-binding proteoglycans	1014:1042	VAR2CSA-binding proteoglycans	1014:1042	To address this question, VAR2CSA-binding proteoglycans were affinity-purified from the human placenta, tumor tissues and cancer cells and analyzed through a specialized glycoproteomics workflow.
32337544	9	59	with	combination	1375:1385	arg1	analysis					1408:1415	glycoproteomics analysis	1392:1415	glycoproteomics analysis	1392:1415	Additionally, this work demonstrates how affinity purification in combination with glycoproteomics analysis can facilitate the characterization of CSPGs with distinct CS epitopes.
32337544	7	60	from	placenta	1082:1089	arg1	affinity-purified					1049:1065	affinity-purified	1049:1065	affinity-purified	1049:1065	To address this question, VAR2CSA-binding proteoglycans were affinity-purified from the human placenta, tumor tissues and cancer cells and analyzed through a specialized glycoproteomics workflow.
32337544	5	61	theme	cancer	772:777	arg1	tissues					779:785	placental and cancer tissues	758:785	placental and cancer tissues	758:785	The identities of the proteoglycans carrying these modifications in placental and cancer tissues remain poorly characterized.
32337544	1	62	theme	falciparum	324:333	arg1	infection					335:343	Plasmodium falciparum infection	313:343	Plasmodium falciparum infection	313:343	Chondroitin sulfate (CS) is the placental receptor for the VAR2CSA malaria protein, expressed at the surface of infected erythrocytes during Plasmodium falciparum infection.
32337544	1	63	theme	VAR2CSA	231:237	arg1	protein					247:253	the VAR2CSA malaria protein	227:253	the VAR2CSA malaria protein	227:253	Chondroitin sulfate (CS) is the placental receptor for the VAR2CSA malaria protein, expressed at the surface of infected erythrocytes during Plasmodium falciparum infection.
32337544	8	64	theme	core	1294:1297	arg1	proteins					1299:1306	novel core proteins	1288:1306	novel core proteins	1288:1306	We show that VAR2CSA-reactive CS chains associate with a heterogenous group of proteoglycans, including novel core proteins.
32337544	0	65	from	VAR2CSA	133:139	arg1	placenta					148:155	the placenta	144:155	the placenta	144:155	An affinity chromatography and glycoproteomics workflow to profile the chondroitin sulfate proteoglycans that interact with malarial VAR2CSA in the placenta and in cancer.
32337544	0	65	from	VAR2CSA	133:139	arg1	cancer					164:169	cancer	164:169	cancer	164:169	An affinity chromatography and glycoproteomics workflow to profile the chondroitin sulfate proteoglycans that interact with malarial VAR2CSA in the placenta and in cancer.
8181059	1	0	theme	interferon	162:171	arg1	interferons					140:150	human interferons alpha and interferon beta	134:176	human interferons alpha and interferon beta (type I IFNs)	134:190	We describe a universal ligand-binding receptor for human interferons alpha and interferon beta (type I IFNs).
8181059	1	0	theme	interferon	162:171	arg1	beta					173:176	interferon beta	162:176	interferon beta	162:176	We describe a universal ligand-binding receptor for human interferons alpha and interferon beta (type I IFNs).
8181059	7	1	theme	cytoplasmic	849:859	arg1	JAK1					872:875	the cytoplasmic Tyr kinase JAK1	845:875	the cytoplasmic Tyr kinase JAK1	845:875	IFN-alpha/beta receptor is physically associated with the cytoplasmic Tyr kinase JAK1, hence, in addition to ligand binding, it is directly involved in signal transduction.
8181059	5	2	theme	kb	627:628	arg1	cDNA					630:633	a 1.5 kb cDNA	621:633	a 1.5 kb cDNA	621:633	We isolated and expressed a 1.5 kb cDNA, coding for the IFN-alpha/beta receptor.
8181059	4	3	theme	disulfide-linked	540:555	arg1	receptor					526:533	The receptor	522:533	The receptor	522:533	The receptor is a disulfide-linked dimer, consisting of 51 kDa subunits.
8181059	4	3	theme	disulfide-linked	540:555	arg1	dimer					557:561	a disulfide-linked dimer	538:561	a disulfide-linked dimer	538:561	The receptor is a disulfide-linked dimer, consisting of 51 kDa subunits.
8181059	5	4	theme	1.5	623:625	arg1	kb					627:628	kb	627:628	kb	627:628	We isolated and expressed a 1.5 kb cDNA, coding for the IFN-alpha/beta receptor.
8181059	7	5	dep	binding	907:913	arg1	addition					888:895	addition	888:895	addition	888:895	IFN-alpha/beta receptor is physically associated with the cytoplasmic Tyr kinase JAK1, hence, in addition to ligand binding, it is directly involved in signal transduction.
8181059	2	6	theme	type	268:271	arg1	IFNs					275:278	type I IFNs	268:278	type I IFNs	268:278	A soluble 40 kDa IFN-alpha/beta receptor (p40) that blocks the activity of type I IFNs was purified from urine and sequenced.
8181059	3	7	with	complexes	494:502	arg1	IFN-alpha					509:517	IFN-alpha 2	509:519	IFN-alpha 2	509:519	Antibodies raised against p40 completely block the activity of several type I IFNs and immuno-precipitate both a cellular 102 kDa IFN-alpha/beta receptor and its cross-linked complexes with IFN-alpha 2.
8181059	1	8	dep	interferons	140:150	arg1	interferons					140:150	human interferons alpha and interferon beta	134:176	human interferons alpha and interferon beta (type I IFNs)	134:190	We describe a universal ligand-binding receptor for human interferons alpha and interferon beta (type I IFNs).
8181059	1	8	dep	interferons	140:150	arg1	alpha					152:156	alpha	152:156	alpha	152:156	We describe a universal ligand-binding receptor for human interferons alpha and interferon beta (type I IFNs).
8181059	1	8	dep	interferons	140:150	arg1	beta					173:176	interferon beta	162:176	interferon beta	162:176	We describe a universal ligand-binding receptor for human interferons alpha and interferon beta (type I IFNs).
8181059	7	9	theme	ligand	900:905	arg1	binding					907:913	ligand binding	900:913	ligand binding	900:913	IFN-alpha/beta receptor is physically associated with the cytoplasmic Tyr kinase JAK1, hence, in addition to ligand binding, it is directly involved in signal transduction.
8181059	3	10	theme	type	390:393	arg1	IFNs					397:400	several type I IFNs	382:400	several type I IFNs	382:400	Antibodies raised against p40 completely block the activity of several type I IFNs and immuno-precipitate both a cellular 102 kDa IFN-alpha/beta receptor and its cross-linked complexes with IFN-alpha 2.
8181059	3	11	theme	IFNs	397:400	arg1	activity					370:377	the activity	366:377	the activity of several type I IFNs	366:400	Antibodies raised against p40 completely block the activity of several type I IFNs and immuno-precipitate both a cellular 102 kDa IFN-alpha/beta receptor and its cross-linked complexes with IFN-alpha 2.
8181059	7	12	theme	IFN-alpha/beta	791:804	arg1	receptor					806:813	IFN-alpha/beta receptor	791:813	IFN-alpha/beta receptor	791:813	IFN-alpha/beta receptor is physically associated with the cytoplasmic Tyr kinase JAK1, hence, in addition to ligand binding, it is directly involved in signal transduction.
8181059	1	13	theme	type	179:182	arg1	IFNs					186:189	type I IFNs	179:189	type I IFNs	179:189	We describe a universal ligand-binding receptor for human interferons alpha and interferon beta (type I IFNs).
8181059	1	13	theme	type	179:182	arg1	interferons					140:150	human interferons alpha and interferon beta	134:176	human interferons alpha and interferon beta (type I IFNs)	134:190	We describe a universal ligand-binding receptor for human interferons alpha and interferon beta (type I IFNs).
8181059	0	14	theme	human	4:8	arg1	receptor					32:39	The human interferon alpha/beta receptor	0:39	The human interferon alpha/beta receptor	0:39	The human interferon alpha/beta receptor: characterization and molecular cloning.
8181059	6	15	theme	transmembrane	728:740	arg1	region					742:747	a leader and a transmembrane region	713:747	region	742:747	Its 331 amino acid sequence includes a leader and a transmembrane region, while its ectodomain corresponds to p40.
8181059	1	16	theme	I	184:184	arg1	IFNs					186:189	type I IFNs	179:189	type I IFNs	179:189	We describe a universal ligand-binding receptor for human interferons alpha and interferon beta (type I IFNs).
8181059	1	16	theme	I	184:184	arg1	interferons					140:150	human interferons alpha and interferon beta	134:176	human interferons alpha and interferon beta (type I IFNs)	134:190	We describe a universal ligand-binding receptor for human interferons alpha and interferon beta (type I IFNs).
8181059	3	17	with	receptor	464:471	arg1	IFN-alpha					509:517	IFN-alpha 2	509:519	IFN-alpha 2	509:519	Antibodies raised against p40 completely block the activity of several type I IFNs and immuno-precipitate both a cellular 102 kDa IFN-alpha/beta receptor and its cross-linked complexes with IFN-alpha 2.
8181059	6	18	theme	a	726:726	arg1	region					742:747	a leader and a transmembrane region	713:747	region	742:747	Its 331 amino acid sequence includes a leader and a transmembrane region, while its ectodomain corresponds to p40.
8181059	2	19	theme	IFNs	275:278	arg1	activity					256:263	the activity	252:263	the activity of type I IFNs	252:278	A soluble 40 kDa IFN-alpha/beta receptor (p40) that blocks the activity of type I IFNs was purified from urine and sequenced.
8181059	3	20	theme	I	395:395	arg1	IFNs					397:400	several type I IFNs	382:400	several type I IFNs	382:400	Antibodies raised against p40 completely block the activity of several type I IFNs and immuno-precipitate both a cellular 102 kDa IFN-alpha/beta receptor and its cross-linked complexes with IFN-alpha 2.
8181059	0	21	theme	alpha/beta	21:30	arg1	receptor					32:39	The human interferon alpha/beta receptor	0:39	The human interferon alpha/beta receptor	0:39	The human interferon alpha/beta receptor: characterization and molecular cloning.
8181059	2	22	theme	I	273:273	arg1	IFNs					275:278	type I IFNs	268:278	type I IFNs	268:278	A soluble 40 kDa IFN-alpha/beta receptor (p40) that blocks the activity of type I IFNs was purified from urine and sequenced.
8181059	0	23	theme	interferon	10:19	arg1	receptor					32:39	The human interferon alpha/beta receptor	0:39	The human interferon alpha/beta receptor	0:39	The human interferon alpha/beta receptor: characterization and molecular cloning.
8181059	5	24	theme	IFN-alpha/beta	651:664	arg1	receptor					666:673	the IFN-alpha/beta receptor	647:673	the IFN-alpha/beta receptor	647:673	We isolated and expressed a 1.5 kb cDNA, coding for the IFN-alpha/beta receptor.
8181059	1	25	theme	ligand-binding	106:119	arg1	receptor					121:128	a universal ligand-binding receptor	94:128	a universal ligand-binding receptor for human interferons alpha and interferon beta (type I IFNs)	94:190	We describe a universal ligand-binding receptor for human interferons alpha and interferon beta (type I IFNs).
8181059	3	26	theme	cellular	432:439	arg1	receptor					464:471	a cellular 102 kDa IFN-alpha/beta receptor	430:471	a cellular 102 kDa IFN-alpha/beta receptor	430:471	Antibodies raised against p40 completely block the activity of several type I IFNs and immuno-precipitate both a cellular 102 kDa IFN-alpha/beta receptor and its cross-linked complexes with IFN-alpha 2.
8181059	3	27	link	cross-linked	481:492	arg1	complexes					494:502	its cross-linked complexes	477:502	its cross-linked complexes with IFN-alpha 2	477:519	Antibodies raised against p40 completely block the activity of several type I IFNs and immuno-precipitate both a cellular 102 kDa IFN-alpha/beta receptor and its cross-linked complexes with IFN-alpha 2.
8181059	3	28	theme	several	382:388	arg1	IFNs					397:400	several type I IFNs	382:400	several type I IFNs	382:400	Antibodies raised against p40 completely block the activity of several type I IFNs and immuno-precipitate both a cellular 102 kDa IFN-alpha/beta receptor and its cross-linked complexes with IFN-alpha 2.
8181059	2	29	theme	IFN-alpha/beta	210:223	arg1	p40					235:237	p40	235:237	p40	235:237	A soluble 40 kDa IFN-alpha/beta receptor (p40) that blocks the activity of type I IFNs was purified from urine and sequenced.
8181059	2	29	theme	IFN-alpha/beta	210:223	arg1	receptor					225:232	A soluble 40 kDa IFN-alpha/beta receptor	193:232	A soluble 40 kDa IFN-alpha/beta receptor (p40) that blocks the activity of type I IFNs	193:278	A soluble 40 kDa IFN-alpha/beta receptor (p40) that blocks the activity of type I IFNs was purified from urine and sequenced.
8181059	2	30	theme	kDa	206:208	arg1	p40					235:237	p40	235:237	p40	235:237	A soluble 40 kDa IFN-alpha/beta receptor (p40) that blocks the activity of type I IFNs was purified from urine and sequenced.
8181059	2	30	theme	kDa	206:208	arg1	receptor					225:232	A soluble 40 kDa IFN-alpha/beta receptor	193:232	A soluble 40 kDa IFN-alpha/beta receptor (p40) that blocks the activity of type I IFNs	193:278	A soluble 40 kDa IFN-alpha/beta receptor (p40) that blocks the activity of type I IFNs was purified from urine and sequenced.
8181059	3	31	theme	IFN-alpha/beta	449:462	arg1	receptor					464:471	a cellular 102 kDa IFN-alpha/beta receptor	430:471	a cellular 102 kDa IFN-alpha/beta receptor	430:471	Antibodies raised against p40 completely block the activity of several type I IFNs and immuno-precipitate both a cellular 102 kDa IFN-alpha/beta receptor and its cross-linked complexes with IFN-alpha 2.
8181059	2	32	theme	soluble	195:201	arg1	p40					235:237	p40	235:237	p40	235:237	A soluble 40 kDa IFN-alpha/beta receptor (p40) that blocks the activity of type I IFNs was purified from urine and sequenced.
8181059	2	32	theme	soluble	195:201	arg1	receptor					225:232	A soluble 40 kDa IFN-alpha/beta receptor	193:232	A soluble 40 kDa IFN-alpha/beta receptor (p40) that blocks the activity of type I IFNs	193:278	A soluble 40 kDa IFN-alpha/beta receptor (p40) that blocks the activity of type I IFNs was purified from urine and sequenced.
8181059	2	33	theme	40	203:204	arg1	kDa					206:208	kDa	206:208	kDa	206:208	A soluble 40 kDa IFN-alpha/beta receptor (p40) that blocks the activity of type I IFNs was purified from urine and sequenced.
8181059	0	34	dep	characterization	42:57	arg1	receptor					32:39	The human interferon alpha/beta receptor	0:39	The human interferon alpha/beta receptor	0:39	The human interferon alpha/beta receptor: characterization and molecular cloning.
8181059	1	35	theme	human	134:138	arg1	interferons					140:150	human interferons alpha and interferon beta	134:176	human interferons alpha and interferon beta (type I IFNs)	134:190	We describe a universal ligand-binding receptor for human interferons alpha and interferon beta (type I IFNs).
8181059	1	35	theme	human	134:138	arg1	beta					173:176	interferon beta	162:176	interferon beta	162:176	We describe a universal ligand-binding receptor for human interferons alpha and interferon beta (type I IFNs).
8181059	1	35	theme	human	134:138	arg1	alpha					152:156	alpha	152:156	alpha	152:156	We describe a universal ligand-binding receptor for human interferons alpha and interferon beta (type I IFNs).
8181059	1	35	theme	human	134:138	arg1	IFNs					186:189	type I IFNs	179:189	type I IFNs	179:189	We describe a universal ligand-binding receptor for human interferons alpha and interferon beta (type I IFNs).
8181059	1	36	theme	universal	96:104	arg1	receptor					121:128	a universal ligand-binding receptor	94:128	a universal ligand-binding receptor for human interferons alpha and interferon beta (type I IFNs)	94:190	We describe a universal ligand-binding receptor for human interferons alpha and interferon beta (type I IFNs).
8181059	7	37	theme	signal	943:948	arg1	transduction					950:961	signal transduction	943:961	signal transduction	943:961	IFN-alpha/beta receptor is physically associated with the cytoplasmic Tyr kinase JAK1, hence, in addition to ligand binding, it is directly involved in signal transduction.
8181059	6	38	theme	acid	690:693	arg1	sequence					695:702	Its 331 amino acid sequence	676:702	Its 331 amino acid sequence	676:702	Its 331 amino acid sequence includes a leader and a transmembrane region, while its ectodomain corresponds to p40.
8181059	3	39	theme	kDa	445:447	arg1	receptor					464:471	a cellular 102 kDa IFN-alpha/beta receptor	430:471	a cellular 102 kDa IFN-alpha/beta receptor	430:471	Antibodies raised against p40 completely block the activity of several type I IFNs and immuno-precipitate both a cellular 102 kDa IFN-alpha/beta receptor and its cross-linked complexes with IFN-alpha 2.
8181059	7	40	theme	Tyr	861:863	arg1	JAK1					872:875	the cytoplasmic Tyr kinase JAK1	845:875	the cytoplasmic Tyr kinase JAK1	845:875	IFN-alpha/beta receptor is physically associated with the cytoplasmic Tyr kinase JAK1, hence, in addition to ligand binding, it is directly involved in signal transduction.
8181059	3	41	theme	102	441:443	arg1	kDa					445:447	kDa	445:447	kDa	445:447	Antibodies raised against p40 completely block the activity of several type I IFNs and immuno-precipitate both a cellular 102 kDa IFN-alpha/beta receptor and its cross-linked complexes with IFN-alpha 2.
8181059	4	42	link	disulfide-linked	540:555	arg1	receptor					526:533	The receptor	522:533	The receptor	522:533	The receptor is a disulfide-linked dimer, consisting of 51 kDa subunits.
8181059	4	42	link	disulfide-linked	540:555	arg1	dimer					557:561	a disulfide-linked dimer	538:561	a disulfide-linked dimer	538:561	The receptor is a disulfide-linked dimer, consisting of 51 kDa subunits.
8181059	6	43	theme	amino	684:688	arg1	sequence					695:702	Its 331 amino acid sequence	676:702	Its 331 amino acid sequence	676:702	Its 331 amino acid sequence includes a leader and a transmembrane region, while its ectodomain corresponds to p40.
8181059	3	44	theme	cross-linked	481:492	arg1	complexes					494:502	its cross-linked complexes	477:502	its cross-linked complexes with IFN-alpha 2	477:519	Antibodies raised against p40 completely block the activity of several type I IFNs and immuno-precipitate both a cellular 102 kDa IFN-alpha/beta receptor and its cross-linked complexes with IFN-alpha 2.
8181059	7	45	theme	kinase	865:870	arg1	JAK1					872:875	the cytoplasmic Tyr kinase JAK1	845:875	the cytoplasmic Tyr kinase JAK1	845:875	IFN-alpha/beta receptor is physically associated with the cytoplasmic Tyr kinase JAK1, hence, in addition to ligand binding, it is directly involved in signal transduction.
8181059	0	46	theme	molecular	63:71	arg1	cloning					73:79	molecular cloning	63:79	molecular cloning	63:79	The human interferon alpha/beta receptor: characterization and molecular cloning.
8181059	4	47	theme	kDa	581:583	arg1	subunits					585:592	51 kDa subunits	578:592	51 kDa subunits	578:592	The receptor is a disulfide-linked dimer, consisting of 51 kDa subunits.
23744091	3	0	theme	Fc	656:657	arg1	variant					659:665	a novel Fc variant	648:665	a novel Fc variant with selectively enhanced FcγRIIb binding over both FcγRIIa(R131) and FcγRIIa(H131)	648:749	In this study, we applied comprehensive mutagenesis and structure-guided design based on the crystal structure of the Fc/FcγRIIb complex to identify a novel Fc variant with selectively enhanced FcγRIIb binding over both FcγRIIa(R131) and FcγRIIa(H131).
23744091	4	1	theme	stronger	794:801	arg1	affinity					811:818	more than 200-fold stronger binding affinity	775:818	more than 200-fold stronger binding affinity to FcγRIIb than wild-type IgG1	775:849	This novel variant has more than 200-fold stronger binding affinity to FcγRIIb than wild-type IgG1, while binding affinity to FcγRIIa(R131) and FcγRIIa(H131) is comparable with or lower than wild-type IgG1.
23744091	1	2	theme	inhibitory	125:134	arg1	approach					204:211	an attractive approach	190:211	an attractive approach for improving the efficacy of antibody therapeutics	190:263	Engaging inhibitory FcγRIIb by Fc region has been recently reported to be an attractive approach for improving the efficacy of antibody therapeutics.
23744091	1	2	theme	inhibitory	125:134	arg1	FcγRIIb					136:142	Engaging inhibitory FcγRIIb	116:142	Engaging inhibitory FcγRIIb by Fc region	116:155	Engaging inhibitory FcγRIIb by Fc region has been recently reported to be an attractive approach for improving the efficacy of antibody therapeutics.
23744091	5	3	theme	C	1021:1021	arg1	domain					1027:1032	the C(H)2 domain	1017:1032	the C(H)2 domain	1017:1032	This selectivity was achieved by conformational change of the C(H)2 domain by mutating Pro to Asp at position 238.
23744091	2	4	theme	enhanced	324:331	arg1	affinity					341:348	enhanced binding affinity	324:348	enhanced binding affinity	324:348	However, the previously reported S267E/L328F variant with enhanced binding affinity to FcγRIIb, also enhances binding affinity to FcγRIIa(R131) allotype to a similar degree because FcγRIIb and FcγRIIa(R131) are structurally similar.
23744091	6	5	theme	platelet	1144:1151	arg1	aggregation					1153:1163	platelet aggregation	1144:1163	platelet aggregation	1144:1163	Fc variant with increased binding to both FcγRIIb and FcγRIIa induced platelet aggregation and activation in an immune complex form in vitro while our novel variant did not.
23744091	5	6	theme	H	1023:1023	arg1	domain					1027:1032	the C(H)2 domain	1017:1032	the C(H)2 domain	1017:1032	This selectivity was achieved by conformational change of the C(H)2 domain by mutating Pro to Asp at position 238.
23744091	7	7	theme	IgG1	1285:1288	arg1	antibody					1290:1297	agonistic anti-CD137 IgG1 antibody	1264:1297	agonistic anti-CD137 IgG1 antibody	1264:1297	When applied to agonistic anti-CD137 IgG1 antibody, our variant greatly enhanced the agonistic activity.
23744091	8	8	theme	antibody	1483:1490	arg1	therapeutics					1492:1503	antibody therapeutics	1483:1503	antibody therapeutics	1483:1503	Thus, the selective enhancement of FcγRIIb binding achieved by our Fc variant provides a novel tool for improving the efficacy of antibody therapeutics.
23744091	4	9	theme	binding	803:809	arg1	affinity					811:818	more than 200-fold stronger binding affinity	775:818	more than 200-fold stronger binding affinity to FcγRIIb than wild-type IgG1	775:849	This novel variant has more than 200-fold stronger binding affinity to FcγRIIb than wild-type IgG1, while binding affinity to FcγRIIa(R131) and FcγRIIa(H131) is comparable with or lower than wild-type IgG1.
23744091	2	10	theme	binding	333:339	arg1	affinity					341:348	enhanced binding affinity	324:348	enhanced binding affinity	324:348	However, the previously reported S267E/L328F variant with enhanced binding affinity to FcγRIIb, also enhances binding affinity to FcγRIIa(R131) allotype to a similar degree because FcγRIIb and FcγRIIa(R131) are structurally similar.
23744091	3	11	theme	enhanced	684:691	arg1	binding					701:707	selectively enhanced FcγRIIb binding	672:707	selectively enhanced FcγRIIb binding over both FcγRIIa(R131) and FcγRIIa(H131)	672:749	In this study, we applied comprehensive mutagenesis and structure-guided design based on the crystal structure of the Fc/FcγRIIb complex to identify a novel Fc variant with selectively enhanced FcγRIIb binding over both FcγRIIa(R131) and FcγRIIa(H131).
23744091	7	12	theme	agonistic	1264:1272	arg1	antibody					1290:1297	agonistic anti-CD137 IgG1 antibody	1264:1297	agonistic anti-CD137 IgG1 antibody	1264:1297	When applied to agonistic anti-CD137 IgG1 antibody, our variant greatly enhanced the agonistic activity.
23744091	8	13	theme	FcγRIIb	1388:1394	arg1	binding					1396:1402	FcγRIIb binding	1388:1402	FcγRIIb binding	1388:1402	Thus, the selective enhancement of FcγRIIb binding achieved by our Fc variant provides a novel tool for improving the efficacy of antibody therapeutics.
23744091	7	14	theme	anti-CD137	1274:1283	arg1	antibody					1290:1297	agonistic anti-CD137 IgG1 antibody	1264:1297	agonistic anti-CD137 IgG1 antibody	1264:1297	When applied to agonistic anti-CD137 IgG1 antibody, our variant greatly enhanced the agonistic activity.
23744091	1	15	theme	Fc	147:148	arg1	region					150:155	Fc region	147:155	Fc region	147:155	Engaging inhibitory FcγRIIb by Fc region has been recently reported to be an attractive approach for improving the efficacy of antibody therapeutics.
23744091	0	16	theme	antibody	11:18	arg1	variant					23:29	antibody Fc variant	11:29	antibody Fc variant with selectively enhanced FcγRIIb binding over both FcγRIIa(R131) and FcγRIIa(H131)	11:113	Engineered antibody Fc variant with selectively enhanced FcγRIIb binding over both FcγRIIa(R131) and FcγRIIa(H131).
23744091	6	17	theme	novel	1225:1229	arg1	variant					1231:1237	our novel variant	1221:1237	our novel variant	1221:1237	Fc variant with increased binding to both FcγRIIb and FcγRIIa induced platelet aggregation and activation in an immune complex form in vitro while our novel variant did not.
23744091	5	18	theme	conformational	992:1005	arg1	change					1007:1012	conformational change	992:1012	conformational change of the C(H)2 domain	992:1032	This selectivity was achieved by conformational change of the C(H)2 domain by mutating Pro to Asp at position 238.
23744091	6	19	theme	immune	1186:1191	arg1	form					1201:1204	an immune complex form	1183:1204	an immune complex form	1183:1204	Fc variant with increased binding to both FcγRIIb and FcγRIIa induced platelet aggregation and activation in an immune complex form in vitro while our novel variant did not.
23744091	2	20	theme	R131	404:407	arg1	allotype					410:417	FcγRIIa(R131) allotype	396:417	FcγRIIa(R131) allotype	396:417	However, the previously reported S267E/L328F variant with enhanced binding affinity to FcγRIIb, also enhances binding affinity to FcγRIIa(R131) allotype to a similar degree because FcγRIIb and FcγRIIa(R131) are structurally similar.
23744091	1	21	theme	antibody	243:250	arg1	therapeutics					252:263	antibody therapeutics	243:263	antibody therapeutics	243:263	Engaging inhibitory FcγRIIb by Fc region has been recently reported to be an attractive approach for improving the efficacy of antibody therapeutics.
23744091	6	22	theme	Fc	1074:1075	arg1	variant					1077:1083	Fc variant	1074:1083	Fc variant with increased binding to both FcγRIIb and FcγRIIa	1074:1134	Fc variant with increased binding to both FcγRIIb and FcγRIIa induced platelet aggregation and activation in an immune complex form in vitro while our novel variant did not.
23744091	2	23	theme	FcγRIIa	396:402	arg1	allotype					410:417	FcγRIIa(R131) allotype	396:417	FcγRIIa(R131) allotype	396:417	However, the previously reported S267E/L328F variant with enhanced binding affinity to FcγRIIb, also enhances binding affinity to FcγRIIa(R131) allotype to a similar degree because FcγRIIb and FcγRIIa(R131) are structurally similar.
23744091	0	24	theme	Fc	20:21	arg1	variant					23:29	antibody Fc variant	11:29	antibody Fc variant with selectively enhanced FcγRIIb binding over both FcγRIIa(R131) and FcγRIIa(H131)	11:113	Engineered antibody Fc variant with selectively enhanced FcγRIIb binding over both FcγRIIa(R131) and FcγRIIa(H131).
23744091	1	25	theme	therapeutics	252:263	arg1	efficacy					231:238	the efficacy	227:238	the efficacy of antibody therapeutics	227:263	Engaging inhibitory FcγRIIb by Fc region has been recently reported to be an attractive approach for improving the efficacy of antibody therapeutics.
23744091	6	26	theme	complex	1193:1199	arg1	form					1201:1204	an immune complex form	1183:1204	an immune complex form	1183:1204	Fc variant with increased binding to both FcγRIIb and FcγRIIa induced platelet aggregation and activation in an immune complex form in vitro while our novel variant did not.
23744091	4	27	theme	binding	858:864	arg1	affinity					866:873	binding affinity	858:873	binding affinity to FcγRIIa(R131) and FcγRIIa(H131)	858:908	This novel variant has more than 200-fold stronger binding affinity to FcγRIIb than wild-type IgG1, while binding affinity to FcγRIIa(R131) and FcγRIIa(H131) is comparable with or lower than wild-type IgG1.
23744091	6	28	theme	increased	1090:1098	arg1	binding					1100:1106	increased binding	1090:1106	increased binding to both FcγRIIb and FcγRIIa	1090:1134	Fc variant with increased binding to both FcγRIIb and FcγRIIa induced platelet aggregation and activation in an immune complex form in vitro while our novel variant did not.
23744091	2	29	theme	similar	424:430	arg1	degree					432:437	a similar degree	422:437	a similar degree	422:437	However, the previously reported S267E/L328F variant with enhanced binding affinity to FcγRIIb, also enhances binding affinity to FcγRIIa(R131) allotype to a similar degree because FcγRIIb and FcγRIIa(R131) are structurally similar.
23744091	0	30	with	variant	23:29	arg1	binding					65:71	selectively enhanced FcγRIIb binding	36:71	selectively enhanced FcγRIIb binding over both FcγRIIa(R131) and FcγRIIa(H131)	36:113	Engineered antibody Fc variant with selectively enhanced FcγRIIb binding over both FcγRIIa(R131) and FcγRIIa(H131).
23744091	2	31	theme	binding	376:382	arg1	affinity					384:391	binding affinity	376:391	binding affinity to FcγRIIa(R131) allotype to a similar degree	376:437	However, the previously reported S267E/L328F variant with enhanced binding affinity to FcγRIIb, also enhances binding affinity to FcγRIIa(R131) allotype to a similar degree because FcγRIIb and FcγRIIa(R131) are structurally similar.
23744091	0	32	theme	FcγRIIb	57:63	arg1	binding					65:71	selectively enhanced FcγRIIb binding	36:71	selectively enhanced FcγRIIb binding over both FcγRIIa(R131) and FcγRIIa(H131)	36:113	Engineered antibody Fc variant with selectively enhanced FcγRIIb binding over both FcγRIIa(R131) and FcγRIIa(H131).
23744091	6	33	from	aggregation	1153:1163	arg1	form					1201:1204	an immune complex form	1183:1204	an immune complex form	1183:1204	Fc variant with increased binding to both FcγRIIb and FcγRIIa induced platelet aggregation and activation in an immune complex form in vitro while our novel variant did not.
23744091	2	34	dep	FcγRIIb	447:453	arg1	similar					490:496	similar	490:496	similar	490:496	However, the previously reported S267E/L328F variant with enhanced binding affinity to FcγRIIb, also enhances binding affinity to FcγRIIa(R131) allotype to a similar degree because FcγRIIb and FcγRIIa(R131) are structurally similar.
23744091	3	35	theme	crystal	592:598	arg1	structure					600:608	the crystal structure	588:608	the crystal structure of the Fc/FcγRIIb complex to identify a novel Fc variant with selectively enhanced FcγRIIb binding over both FcγRIIa(R131) and FcγRIIa(H131)	588:749	In this study, we applied comprehensive mutagenesis and structure-guided design based on the crystal structure of the Fc/FcγRIIb complex to identify a novel Fc variant with selectively enhanced FcγRIIb binding over both FcγRIIa(R131) and FcγRIIa(H131).
23744091	4	36	theme	novel	757:761	arg1	variant					763:769	This novel variant	752:769	This novel variant	752:769	This novel variant has more than 200-fold stronger binding affinity to FcγRIIb than wild-type IgG1, while binding affinity to FcγRIIa(R131) and FcγRIIa(H131) is comparable with or lower than wild-type IgG1.
23744091	0	37	theme	enhanced	48:55	arg1	binding					65:71	selectively enhanced FcγRIIb binding	36:71	selectively enhanced FcγRIIb binding over both FcγRIIa(R131) and FcγRIIa(H131)	36:113	Engineered antibody Fc variant with selectively enhanced FcγRIIb binding over both FcγRIIa(R131) and FcγRIIa(H131).
23744091	5	38	theme	domain	1027:1032	arg1	change					1007:1012	conformational change	992:1012	conformational change of the C(H)2 domain	992:1032	This selectivity was achieved by conformational change of the C(H)2 domain by mutating Pro to Asp at position 238.
23744091	7	39	theme	agonistic	1333:1341	arg1	activity					1343:1350	the agonistic activity	1329:1350	the agonistic activity	1329:1350	When applied to agonistic anti-CD137 IgG1 antibody, our variant greatly enhanced the agonistic activity.
23744091	3	40	theme	complex	628:634	arg1	structure					600:608	the crystal structure	588:608	the crystal structure of the Fc/FcγRIIb complex to identify a novel Fc variant with selectively enhanced FcγRIIb binding over both FcγRIIa(R131) and FcγRIIa(H131)	588:749	In this study, we applied comprehensive mutagenesis and structure-guided design based on the crystal structure of the Fc/FcγRIIb complex to identify a novel Fc variant with selectively enhanced FcγRIIb binding over both FcγRIIa(R131) and FcγRIIa(H131).
23744091	3	41	theme	comprehensive	525:537	arg1	mutagenesis					539:549	comprehensive mutagenesis	525:549	comprehensive mutagenesis	525:549	In this study, we applied comprehensive mutagenesis and structure-guided design based on the crystal structure of the Fc/FcγRIIb complex to identify a novel Fc variant with selectively enhanced FcγRIIb binding over both FcγRIIa(R131) and FcγRIIa(H131).
23744091	3	42	with	variant	659:665	arg1	binding					701:707	selectively enhanced FcγRIIb binding	672:707	selectively enhanced FcγRIIb binding over both FcγRIIa(R131) and FcγRIIa(H131)	672:749	In this study, we applied comprehensive mutagenesis and structure-guided design based on the crystal structure of the Fc/FcγRIIb complex to identify a novel Fc variant with selectively enhanced FcγRIIb binding over both FcγRIIa(R131) and FcγRIIa(H131).
23744091	6	43	from	activation	1169:1178	arg1	form					1201:1204	an immune complex form	1183:1204	an immune complex form	1183:1204	Fc variant with increased binding to both FcγRIIb and FcγRIIa induced platelet aggregation and activation in an immune complex form in vitro while our novel variant did not.
23744091	4	44	theme	wild-type	836:844	arg1	IgG1					846:849	wild-type IgG1	836:849	wild-type IgG1	836:849	This novel variant has more than 200-fold stronger binding affinity to FcγRIIb than wild-type IgG1, while binding affinity to FcγRIIa(R131) and FcγRIIa(H131) is comparable with or lower than wild-type IgG1.
23744091	2	45	theme	S267E/L328F	299:309	arg1	variant					311:317	the previously reported S267E/L328F variant	275:317	the previously reported S267E/L328F variant	275:317	However, the previously reported S267E/L328F variant with enhanced binding affinity to FcγRIIb, also enhances binding affinity to FcγRIIa(R131) allotype to a similar degree because FcγRIIb and FcγRIIa(R131) are structurally similar.
23744091	8	46	theme	therapeutics	1492:1503	arg1	efficacy					1471:1478	the efficacy	1467:1478	the efficacy of antibody therapeutics	1467:1503	Thus, the selective enhancement of FcγRIIb binding achieved by our Fc variant provides a novel tool for improving the efficacy of antibody therapeutics.
23744091	6	47	with	variant	1077:1083	arg1	binding					1100:1106	increased binding	1090:1106	increased binding to both FcγRIIb and FcγRIIa	1090:1134	Fc variant with increased binding to both FcγRIIb and FcγRIIa induced platelet aggregation and activation in an immune complex form in vitro while our novel variant did not.
23744091	8	48	theme	selective	1363:1371	arg1	enhancement					1373:1383	the selective enhancement	1359:1383	the selective enhancement of FcγRIIb binding achieved by our Fc variant	1359:1429	Thus, the selective enhancement of FcγRIIb binding achieved by our Fc variant provides a novel tool for improving the efficacy of antibody therapeutics.
23744091	2	49	theme	reported	290:297	arg1	variant					311:317	the previously reported S267E/L328F variant	275:317	the previously reported S267E/L328F variant	275:317	However, the previously reported S267E/L328F variant with enhanced binding affinity to FcγRIIb, also enhances binding affinity to FcγRIIa(R131) allotype to a similar degree because FcγRIIb and FcγRIIa(R131) are structurally similar.
23744091	3	50	theme	FcγRIIb	693:699	arg1	binding					701:707	selectively enhanced FcγRIIb binding	672:707	selectively enhanced FcγRIIb binding over both FcγRIIa(R131) and FcγRIIa(H131)	672:749	In this study, we applied comprehensive mutagenesis and structure-guided design based on the crystal structure of the Fc/FcγRIIb complex to identify a novel Fc variant with selectively enhanced FcγRIIb binding over both FcγRIIa(R131) and FcγRIIa(H131).
23744091	8	51	theme	novel	1442:1446	arg1	tool					1448:1451	a novel tool	1440:1451	a novel tool for improving the efficacy of antibody therapeutics	1440:1503	Thus, the selective enhancement of FcγRIIb binding achieved by our Fc variant provides a novel tool for improving the efficacy of antibody therapeutics.
23744091	3	52	theme	Fc/FcγRIIb	617:626	arg1	complex					628:634	the Fc/FcγRIIb complex	613:634	the Fc/FcγRIIb complex	613:634	In this study, we applied comprehensive mutagenesis and structure-guided design based on the crystal structure of the Fc/FcγRIIb complex to identify a novel Fc variant with selectively enhanced FcγRIIb binding over both FcγRIIa(R131) and FcγRIIa(H131).
23744091	3	53	theme	structure-guided	555:570	arg1	design					572:577	structure-guided design	555:577	structure-guided design	555:577	In this study, we applied comprehensive mutagenesis and structure-guided design based on the crystal structure of the Fc/FcγRIIb complex to identify a novel Fc variant with selectively enhanced FcγRIIb binding over both FcγRIIa(R131) and FcγRIIa(H131).
23744091	8	54	theme	binding	1396:1402	arg1	enhancement					1373:1383	the selective enhancement	1359:1383	the selective enhancement of FcγRIIb binding achieved by our Fc variant	1359:1429	Thus, the selective enhancement of FcγRIIb binding achieved by our Fc variant provides a novel tool for improving the efficacy of antibody therapeutics.
23744091	2	55	with	variant	311:317	arg1	affinity					341:348	enhanced binding affinity	324:348	enhanced binding affinity	324:348	However, the previously reported S267E/L328F variant with enhanced binding affinity to FcγRIIb, also enhances binding affinity to FcγRIIa(R131) allotype to a similar degree because FcγRIIb and FcγRIIa(R131) are structurally similar.
23744091	4	56	contain	has	771:773	arg2	affinity					811:818	more than 200-fold stronger binding affinity	775:818	more than 200-fold stronger binding affinity to FcγRIIb than wild-type IgG1	775:849	This novel variant has more than 200-fold stronger binding affinity to FcγRIIb than wild-type IgG1, while binding affinity to FcγRIIa(R131) and FcγRIIa(H131) is comparable with or lower than wild-type IgG1.
23744091	4	56	contain	has	771:773	arg1	variant					763:769	This novel variant	752:769	This novel variant	752:769	This novel variant has more than 200-fold stronger binding affinity to FcγRIIb than wild-type IgG1, while binding affinity to FcγRIIa(R131) and FcγRIIa(H131) is comparable with or lower than wild-type IgG1.
23744091	1	57	theme	attractive	193:202	arg1	approach					204:211	an attractive approach	190:211	an attractive approach for improving the efficacy of antibody therapeutics	190:263	Engaging inhibitory FcγRIIb by Fc region has been recently reported to be an attractive approach for improving the efficacy of antibody therapeutics.
23744091	1	57	theme	attractive	193:202	arg1	FcγRIIb					136:142	Engaging inhibitory FcγRIIb	116:142	Engaging inhibitory FcγRIIb by Fc region	116:155	Engaging inhibitory FcγRIIb by Fc region has been recently reported to be an attractive approach for improving the efficacy of antibody therapeutics.
23744091	3	58	theme	novel	650:654	arg1	variant					659:665	a novel Fc variant	648:665	a novel Fc variant with selectively enhanced FcγRIIb binding over both FcγRIIa(R131) and FcγRIIa(H131)	648:749	In this study, we applied comprehensive mutagenesis and structure-guided design based on the crystal structure of the Fc/FcγRIIb complex to identify a novel Fc variant with selectively enhanced FcγRIIb binding over both FcγRIIa(R131) and FcγRIIa(H131).
23744091	1	59	theme	Engaging	116:123	arg1	approach					204:211	an attractive approach	190:211	an attractive approach for improving the efficacy of antibody therapeutics	190:263	Engaging inhibitory FcγRIIb by Fc region has been recently reported to be an attractive approach for improving the efficacy of antibody therapeutics.
23744091	1	59	theme	Engaging	116:123	arg1	FcγRIIb					136:142	Engaging inhibitory FcγRIIb	116:142	Engaging inhibitory FcγRIIb by Fc region	116:155	Engaging inhibitory FcγRIIb by Fc region has been recently reported to be an attractive approach for improving the efficacy of antibody therapeutics.
23744091	4	60	theme	wild-type	943:951	arg1	IgG1					953:956	wild-type IgG1	943:956	wild-type IgG1	943:956	This novel variant has more than 200-fold stronger binding affinity to FcγRIIb than wild-type IgG1, while binding affinity to FcγRIIa(R131) and FcγRIIa(H131) is comparable with or lower than wild-type IgG1.
23744091	8	61	theme	Fc	1420:1421	arg1	variant					1423:1429	our Fc variant	1416:1429	our Fc variant	1416:1429	Thus, the selective enhancement of FcγRIIb binding achieved by our Fc variant provides a novel tool for improving the efficacy of antibody therapeutics.
23934049	8	0	theme	diseases	1578:1585	arg1	treatment					1541:1549	the treatment	1537:1549	the treatment of cancer and inflammatory diseases	1537:1585	On the whole, our data form the basis for rapid design and implementation of unique, FR-targeted, folate-based drugs for the treatment of cancer and inflammatory diseases.
23934049	6	1	theme	stages	1140:1145	arg1	representative					1118:1131	representative	1118:1131	representative	1118:1131	From comparison of the structures, we delineate discrete structural conformations representative of key stages in the endocytic trafficking of FRs and propose models for pH-dependent conformational changes.
23934049	3	2	theme	affinity	481:488	arg1	receptors					490:498	high affinity receptors	476:498	high affinity receptors that transport folate via endocytosis	476:536	More recently, human folate receptors (FRs), high affinity receptors that transport folate via endocytosis, have been proposed as targets for the specific delivery of new classes of antifolates or folate conjugates to tumors or sites of inflammation.
23934049	3	2	theme	affinity	481:488	arg1	receptors					459:467	human folate receptors	446:467	human folate receptors (FRs)	446:473	More recently, human folate receptors (FRs), high affinity receptors that transport folate via endocytosis, have been proposed as targets for the specific delivery of new classes of antifolates or folate conjugates to tumors or sites of inflammation.
23934049	2	3	from	uptake	315:320	arg1	use					353:355	clinical use	344:355	clinical use	344:355	Cellular uptake of the antifolates in clinical use occurs primarily via widely expressed facilitative membrane transporters.
23934049	2	4	theme	antifolates	329:339	arg1	uptake					315:320	Cellular uptake	306:320	Cellular uptake of the antifolates in clinical use	306:355	Cellular uptake of the antifolates in clinical use occurs primarily via widely expressed facilitative membrane transporters.
23934049	1	5	theme	several	235:241	arg1	decades					243:249	several decades	235:249	several decades	235:249	Antifolates, folate analogs that inhibit vitamin B9 (folic acid)-using cellular enzymes, have been used over several decades for the treatment of cancer and inflammatory diseases.
23934049	6	6	theme	structural	1093:1102	arg1	conformations					1104:1116	discrete structural conformations	1084:1116	discrete structural conformations representative of key stages in the endocytic trafficking of FRs	1084:1181	From comparison of the structures, we delineate discrete structural conformations representative of key stages in the endocytic trafficking of FRs and propose models for pH-dependent conformational changes.
23934049	4	7	theme	biophysical	770:780	arg1	models					812:817	particularly structural models	788:817	particularly structural models of the receptors	788:834	The development of specific, FR-targeted antifolates would be accelerated if additional biophysical data, particularly structural models of the receptors, were available.
23934049	4	7	theme	biophysical	770:780	arg1	data					782:785	additional biophysical data	759:785	additional biophysical data	759:785	The development of specific, FR-targeted antifolates would be accelerated if additional biophysical data, particularly structural models of the receptors, were available.
23934049	5	8	theme	distinct	874:881	arg1	models					900:905	six distinct crystallographic models	870:905	six distinct crystallographic models that provide insight into biological trafficking of FRs and distinct binding modes of folate and antifolates to these receptors	870:1033	Here we describe six distinct crystallographic models that provide insight into biological trafficking of FRs and distinct binding modes of folate and antifolates to these receptors.
23934049	5	9	theme	FRs	959:961	arg1	trafficking					944:954	biological trafficking	933:954	biological trafficking of FRs and distinct binding modes of folate and antifolates to these receptors	933:1033	Here we describe six distinct crystallographic models that provide insight into biological trafficking of FRs and distinct binding modes of folate and antifolates to these receptors.
23934049	8	10	dep	unique	1493:1498	arg1	folate-based					1514:1525	folate-based	1514:1525	folate-based	1514:1525	On the whole, our data form the basis for rapid design and implementation of unique, FR-targeted, folate-based drugs for the treatment of cancer and inflammatory diseases.
23934049	8	10	dep	unique	1493:1498	arg1	FR-targeted					1501:1511	FR-targeted	1501:1511	FR-targeted	1501:1511	On the whole, our data form the basis for rapid design and implementation of unique, FR-targeted, folate-based drugs for the treatment of cancer and inflammatory diseases.
23934049	5	11	theme	biological	933:942	arg1	trafficking					944:954	biological trafficking	933:954	biological trafficking of FRs and distinct binding modes of folate and antifolates to these receptors	933:1033	Here we describe six distinct crystallographic models that provide insight into biological trafficking of FRs and distinct binding modes of folate and antifolates to these receptors.
23934049	5	12	theme	distinct	967:974	arg1	modes					984:988	distinct binding modes	967:988	distinct binding modes	967:988	Here we describe six distinct crystallographic models that provide insight into biological trafficking of FRs and distinct binding modes of folate and antifolates to these receptors.
23934049	5	13	theme	crystallographic	883:898	arg1	models					900:905	six distinct crystallographic models	870:905	six distinct crystallographic models that provide insight into biological trafficking of FRs and distinct binding modes of folate and antifolates to these receptors	870:1033	Here we describe six distinct crystallographic models that provide insight into biological trafficking of FRs and distinct binding modes of folate and antifolates to these receptors.
23934049	2	14	theme	Cellular	306:313	arg1	uptake					315:320	Cellular uptake	306:320	Cellular uptake of the antifolates in clinical use	306:355	Cellular uptake of the antifolates in clinical use occurs primarily via widely expressed facilitative membrane transporters.
23934049	7	15	theme	molecular	1273:1281	arg1	details					1283:1289	the molecular details	1269:1289	the molecular details of human FR in complex with three clinically prevalent antifolates, pemetrexed (also Alimta), aminopterin, and methotrexate	1269:1413	Additionally, we describe the molecular details of human FR in complex with three clinically prevalent antifolates, pemetrexed (also Alimta), aminopterin, and methotrexate.
23934049	2	16	theme	membrane	408:415	arg1	transporters					417:428	widely expressed facilitative membrane transporters	378:428	widely expressed facilitative membrane transporters	378:428	Cellular uptake of the antifolates in clinical use occurs primarily via widely expressed facilitative membrane transporters.
23934049	4	17	theme	additional	759:768	arg1	models					812:817	particularly structural models	788:817	particularly structural models of the receptors	788:834	The development of specific, FR-targeted antifolates would be accelerated if additional biophysical data, particularly structural models of the receptors, were available.
23934049	4	17	theme	additional	759:768	arg1	data					782:785	additional biophysical data	759:785	additional biophysical data	759:785	The development of specific, FR-targeted antifolates would be accelerated if additional biophysical data, particularly structural models of the receptors, were available.
23934049	7	18	theme	prevalent	1336:1344	arg1	antifolates					1346:1356	three clinically prevalent antifolates	1319:1356	three clinically prevalent antifolates	1319:1356	Additionally, we describe the molecular details of human FR in complex with three clinically prevalent antifolates, pemetrexed (also Alimta), aminopterin, and methotrexate.
23934049	7	18	theme	prevalent	1336:1344	arg1	methotrexate					1402:1413	methotrexate	1402:1413	methotrexate	1402:1413	Additionally, we describe the molecular details of human FR in complex with three clinically prevalent antifolates, pemetrexed (also Alimta), aminopterin, and methotrexate.
23934049	7	18	theme	prevalent	1336:1344	arg1	aminopterin					1385:1395	aminopterin	1385:1395	aminopterin	1385:1395	Additionally, we describe the molecular details of human FR in complex with three clinically prevalent antifolates, pemetrexed (also Alimta), aminopterin, and methotrexate.
23934049	7	18	theme	prevalent	1336:1344	arg1	pemetrexed					1359:1368	pemetrexed	1359:1368	pemetrexed (also Alimta)	1359:1382	Additionally, we describe the molecular details of human FR in complex with three clinically prevalent antifolates, pemetrexed (also Alimta), aminopterin, and methotrexate.
23934049	6	19	theme	conformational	1219:1232	arg1	changes					1234:1240	pH-dependent conformational changes	1206:1240	pH-dependent conformational changes	1206:1240	From comparison of the structures, we delineate discrete structural conformations representative of key stages in the endocytic trafficking of FRs and propose models for pH-dependent conformational changes.
23934049	0	20	theme	antifolate	102:111	arg1	recognition					113:123	antifolate recognition	102:123	antifolate recognition	102:123	Structures of human folate receptors reveal biological trafficking states and diversity in folate and antifolate recognition.
23934049	4	21	theme	receptors	826:834	arg1	models					812:817	particularly structural models	788:817	particularly structural models of the receptors	788:834	The development of specific, FR-targeted antifolates would be accelerated if additional biophysical data, particularly structural models of the receptors, were available.
23934049	4	21	theme	receptors	826:834	arg1	data					782:785	additional biophysical data	759:785	additional biophysical data	759:785	The development of specific, FR-targeted antifolates would be accelerated if additional biophysical data, particularly structural models of the receptors, were available.
23934049	5	22	theme	modes	984:988	arg1	trafficking					944:954	biological trafficking	933:954	biological trafficking of FRs and distinct binding modes of folate and antifolates to these receptors	933:1033	Here we describe six distinct crystallographic models that provide insight into biological trafficking of FRs and distinct binding modes of folate and antifolates to these receptors.
23934049	1	23	theme	cellular	197:204	arg1	enzymes					206:212	vitamin B9 (folic acid)-using cellular enzymes	167:212	vitamin B9 (folic acid)-using cellular enzymes	167:212	Antifolates, folate analogs that inhibit vitamin B9 (folic acid)-using cellular enzymes, have been used over several decades for the treatment of cancer and inflammatory diseases.
23934049	5	24	theme	folate	993:998	arg1	FRs					959:961	FRs	959:961	FRs	959:961	Here we describe six distinct crystallographic models that provide insight into biological trafficking of FRs and distinct binding modes of folate and antifolates to these receptors.
23934049	5	24	theme	folate	993:998	arg1	modes					984:988	distinct binding modes	967:988	distinct binding modes	967:988	Here we describe six distinct crystallographic models that provide insight into biological trafficking of FRs and distinct binding modes of folate and antifolates to these receptors.
23934049	3	25	theme	transport	505:513	arg1	folate					515:520	transport folate	505:520	transport folate via endocytosis	505:536	More recently, human folate receptors (FRs), high affinity receptors that transport folate via endocytosis, have been proposed as targets for the specific delivery of new classes of antifolates or folate conjugates to tumors or sites of inflammation.
23934049	4	26	dep	specific	701:708	arg1	FR-targeted					711:721	FR-targeted	711:721	FR-targeted	711:721	The development of specific, FR-targeted antifolates would be accelerated if additional biophysical data, particularly structural models of the receptors, were available.
23934049	6	27	theme	discrete	1084:1091	arg1	conformations					1104:1116	discrete structural conformations	1084:1116	discrete structural conformations representative of key stages in the endocytic trafficking of FRs	1084:1181	From comparison of the structures, we delineate discrete structural conformations representative of key stages in the endocytic trafficking of FRs and propose models for pH-dependent conformational changes.
23934049	1	28	theme	folic	179:183	arg1	acid					185:188	folic acid	179:188	folic acid	179:188	Antifolates, folate analogs that inhibit vitamin B9 (folic acid)-using cellular enzymes, have been used over several decades for the treatment of cancer and inflammatory diseases.
23934049	7	29	dep	pemetrexed	1359:1368	arg1	Alimta					1376:1381	Alimta	1376:1381	also Alimta	1371:1381	Additionally, we describe the molecular details of human FR in complex with three clinically prevalent antifolates, pemetrexed (also Alimta), aminopterin, and methotrexate.
23934049	7	30	from	FR	1300:1301	arg1	complex					1306:1312	complex	1306:1312	complex with three clinically prevalent antifolates, pemetrexed (also Alimta), aminopterin, and methotrexate	1306:1413	Additionally, we describe the molecular details of human FR in complex with three clinically prevalent antifolates, pemetrexed (also Alimta), aminopterin, and methotrexate.
23934049	3	31	theme	folate	628:633	arg1	conjugates					635:644	folate conjugates	628:644	folate conjugates	628:644	More recently, human folate receptors (FRs), high affinity receptors that transport folate via endocytosis, have been proposed as targets for the specific delivery of new classes of antifolates or folate conjugates to tumors or sites of inflammation.
23934049	0	32	theme	folate	20:25	arg1	receptors					27:35	human folate receptors	14:35	human folate receptors	14:35	Structures of human folate receptors reveal biological trafficking states and diversity in folate and antifolate recognition.
23934049	6	33	theme	pH-dependent	1206:1217	arg1	changes					1234:1240	pH-dependent conformational changes	1206:1240	pH-dependent conformational changes	1206:1240	From comparison of the structures, we delineate discrete structural conformations representative of key stages in the endocytic trafficking of FRs and propose models for pH-dependent conformational changes.
23934049	7	34	with	complex	1306:1312	arg1	antifolates					1346:1356	three clinically prevalent antifolates	1319:1356	three clinically prevalent antifolates	1319:1356	Additionally, we describe the molecular details of human FR in complex with three clinically prevalent antifolates, pemetrexed (also Alimta), aminopterin, and methotrexate.
23934049	7	34	with	complex	1306:1312	arg1	methotrexate					1402:1413	methotrexate	1402:1413	methotrexate	1402:1413	Additionally, we describe the molecular details of human FR in complex with three clinically prevalent antifolates, pemetrexed (also Alimta), aminopterin, and methotrexate.
23934049	7	34	with	complex	1306:1312	arg1	aminopterin					1385:1395	aminopterin	1385:1395	aminopterin	1385:1395	Additionally, we describe the molecular details of human FR in complex with three clinically prevalent antifolates, pemetrexed (also Alimta), aminopterin, and methotrexate.
23934049	7	34	with	complex	1306:1312	arg1	pemetrexed					1359:1368	pemetrexed	1359:1368	pemetrexed (also Alimta)	1359:1382	Additionally, we describe the molecular details of human FR in complex with three clinically prevalent antifolates, pemetrexed (also Alimta), aminopterin, and methotrexate.
23934049	7	35	from	details	1283:1289	arg1	complex					1306:1312	complex	1306:1312	complex with three clinically prevalent antifolates, pemetrexed (also Alimta), aminopterin, and methotrexate	1306:1413	Additionally, we describe the molecular details of human FR in complex with three clinically prevalent antifolates, pemetrexed (also Alimta), aminopterin, and methotrexate.
23934049	6	36	theme	endocytic	1154:1162	arg1	trafficking					1164:1174	the endocytic trafficking	1150:1174	the endocytic trafficking of FRs	1150:1181	From comparison of the structures, we delineate discrete structural conformations representative of key stages in the endocytic trafficking of FRs and propose models for pH-dependent conformational changes.
23934049	0	37	theme	human	14:18	arg1	receptors					27:35	human folate receptors	14:35	human folate receptors	14:35	Structures of human folate receptors reveal biological trafficking states and diversity in folate and antifolate recognition.
23934049	8	38	theme	cancer	1554:1559	arg1	treatment					1541:1549	the treatment	1537:1549	the treatment of cancer and inflammatory diseases	1537:1585	On the whole, our data form the basis for rapid design and implementation of unique, FR-targeted, folate-based drugs for the treatment of cancer and inflammatory diseases.
23934049	5	39	theme	binding	976:982	arg1	modes					984:988	distinct binding modes	967:988	distinct binding modes	967:988	Here we describe six distinct crystallographic models that provide insight into biological trafficking of FRs and distinct binding modes of folate and antifolates to these receptors.
23934049	4	40	theme	antifolates	723:733	arg1	development					686:696	The development	682:696	The development of specific, FR-targeted antifolates	682:733	The development of specific, FR-targeted antifolates would be accelerated if additional biophysical data, particularly structural models of the receptors, were available.
23934049	1	41	theme	-using	190:195	arg1	enzymes					206:212	vitamin B9 (folic acid)-using cellular enzymes	167:212	vitamin B9 (folic acid)-using cellular enzymes	167:212	Antifolates, folate analogs that inhibit vitamin B9 (folic acid)-using cellular enzymes, have been used over several decades for the treatment of cancer and inflammatory diseases.
23934049	1	42	theme	cancer	272:277	arg1	treatment					259:267	the treatment	255:267	the treatment of cancer and inflammatory diseases	255:303	Antifolates, folate analogs that inhibit vitamin B9 (folic acid)-using cellular enzymes, have been used over several decades for the treatment of cancer and inflammatory diseases.
23934049	0	43	from	diversity	78:86	arg1	folate					91:96	folate	91:96	folate	91:96	Structures of human folate receptors reveal biological trafficking states and diversity in folate and antifolate recognition.
23934049	0	43	from	diversity	78:86	arg1	recognition					113:123	antifolate recognition	102:123	antifolate recognition	102:123	Structures of human folate receptors reveal biological trafficking states and diversity in folate and antifolate recognition.
23934049	6	44	theme	structures	1059:1068	arg1	comparison					1041:1050	comparison	1041:1050	comparison of the structures	1041:1068	From comparison of the structures, we delineate discrete structural conformations representative of key stages in the endocytic trafficking of FRs and propose models for pH-dependent conformational changes.
23934049	2	45	theme	facilitative	395:406	arg1	transporters					417:428	widely expressed facilitative membrane transporters	378:428	widely expressed facilitative membrane transporters	378:428	Cellular uptake of the antifolates in clinical use occurs primarily via widely expressed facilitative membrane transporters.
23934049	0	46	theme	receptors	27:35	arg1	Structures					0:9	Structures	0:9	Structures of human folate receptors	0:35	Structures of human folate receptors reveal biological trafficking states and diversity in folate and antifolate recognition.
23934049	8	47	theme	inflammatory	1565:1576	arg1	diseases					1578:1585	inflammatory diseases	1565:1585	inflammatory diseases	1565:1585	On the whole, our data form the basis for rapid design and implementation of unique, FR-targeted, folate-based drugs for the treatment of cancer and inflammatory diseases.
23934049	3	48	theme	specific	577:584	arg1	delivery					586:593	the specific delivery	573:593	the specific delivery of new classes of antifolates or folate conjugates to tumors or sites of inflammation	573:679	More recently, human folate receptors (FRs), high affinity receptors that transport folate via endocytosis, have been proposed as targets for the specific delivery of new classes of antifolates or folate conjugates to tumors or sites of inflammation.
23934049	7	49	theme	human	1294:1298	arg1	FR					1300:1301	human FR	1294:1301	human FR in complex with three clinically prevalent antifolates, pemetrexed (also Alimta), aminopterin, and methotrexate	1294:1413	Additionally, we describe the molecular details of human FR in complex with three clinically prevalent antifolates, pemetrexed (also Alimta), aminopterin, and methotrexate.
23934049	2	50	theme	expressed	385:393	arg1	transporters					417:428	widely expressed facilitative membrane transporters	378:428	widely expressed facilitative membrane transporters	378:428	Cellular uptake of the antifolates in clinical use occurs primarily via widely expressed facilitative membrane transporters.
23934049	0	51	theme	trafficking	55:65	arg1	states					67:72	biological trafficking states	44:72	biological trafficking states	44:72	Structures of human folate receptors reveal biological trafficking states and diversity in folate and antifolate recognition.
23934049	1	52	theme	inflammatory	283:294	arg1	diseases					296:303	inflammatory diseases	283:303	inflammatory diseases	283:303	Antifolates, folate analogs that inhibit vitamin B9 (folic acid)-using cellular enzymes, have been used over several decades for the treatment of cancer and inflammatory diseases.
23934049	0	53	from	states	67:72	arg1	folate					91:96	folate	91:96	folate	91:96	Structures of human folate receptors reveal biological trafficking states and diversity in folate and antifolate recognition.
23934049	0	53	from	states	67:72	arg1	recognition					113:123	antifolate recognition	102:123	antifolate recognition	102:123	Structures of human folate receptors reveal biological trafficking states and diversity in folate and antifolate recognition.
23934049	7	54	from	complex	1306:1312	arg1	details					1283:1289	the molecular details	1269:1289	the molecular details of human FR in complex with three clinically prevalent antifolates, pemetrexed (also Alimta), aminopterin, and methotrexate	1269:1413	Additionally, we describe the molecular details of human FR in complex with three clinically prevalent antifolates, pemetrexed (also Alimta), aminopterin, and methotrexate.
23934049	6	55	theme	key	1136:1138	arg1	stages					1140:1145	key stages	1136:1145	key stages in the endocytic trafficking of FRs	1136:1181	From comparison of the structures, we delineate discrete structural conformations representative of key stages in the endocytic trafficking of FRs and propose models for pH-dependent conformational changes.
23934049	7	56	theme	FR	1300:1301	arg1	details					1283:1289	the molecular details	1269:1289	the molecular details of human FR in complex with three clinically prevalent antifolates, pemetrexed (also Alimta), aminopterin, and methotrexate	1269:1413	Additionally, we describe the molecular details of human FR in complex with three clinically prevalent antifolates, pemetrexed (also Alimta), aminopterin, and methotrexate.
23934049	0	57	theme	biological	44:53	arg1	states					67:72	biological trafficking states	44:72	biological trafficking states	44:72	Structures of human folate receptors reveal biological trafficking states and diversity in folate and antifolate recognition.
23934049	1	58	theme	diseases	296:303	arg1	treatment					259:267	the treatment	255:267	the treatment of cancer and inflammatory diseases	255:303	Antifolates, folate analogs that inhibit vitamin B9 (folic acid)-using cellular enzymes, have been used over several decades for the treatment of cancer and inflammatory diseases.
23934049	8	59	theme	unique	1493:1498	arg1	drugs					1527:1531	unique, FR-targeted, folate-based drugs	1493:1531	unique, FR-targeted, folate-based drugs for the treatment of cancer and inflammatory diseases	1493:1585	On the whole, our data form the basis for rapid design and implementation of unique, FR-targeted, folate-based drugs for the treatment of cancer and inflammatory diseases.
23934049	1	60	used	used	225:228	arg2	analogs					146:152	folate analogs	139:152	folate analogs that inhibit vitamin B9 (folic acid)-using cellular enzymes	139:212	Antifolates, folate analogs that inhibit vitamin B9 (folic acid)-using cellular enzymes, have been used over several decades for the treatment of cancer and inflammatory diseases.
23934049	1	60	used	used	225:228	arg2	Antifolates					126:136	Antifolates	126:136	Antifolates	126:136	Antifolates, folate analogs that inhibit vitamin B9 (folic acid)-using cellular enzymes, have been used over several decades for the treatment of cancer and inflammatory diseases.
23934049	6	61	from	stages	1140:1145	arg1	trafficking					1164:1174	the endocytic trafficking	1150:1174	the endocytic trafficking of FRs	1150:1181	From comparison of the structures, we delineate discrete structural conformations representative of key stages in the endocytic trafficking of FRs and propose models for pH-dependent conformational changes.
23934049	3	62	theme	high	476:479	arg1	receptors					490:498	high affinity receptors	476:498	high affinity receptors that transport folate via endocytosis	476:536	More recently, human folate receptors (FRs), high affinity receptors that transport folate via endocytosis, have been proposed as targets for the specific delivery of new classes of antifolates or folate conjugates to tumors or sites of inflammation.
23934049	3	62	theme	high	476:479	arg1	receptors					459:467	human folate receptors	446:467	human folate receptors (FRs)	446:473	More recently, human folate receptors (FRs), high affinity receptors that transport folate via endocytosis, have been proposed as targets for the specific delivery of new classes of antifolates or folate conjugates to tumors or sites of inflammation.
23934049	5	63	theme	antifolates	1004:1014	arg1	FRs					959:961	FRs	959:961	FRs	959:961	Here we describe six distinct crystallographic models that provide insight into biological trafficking of FRs and distinct binding modes of folate and antifolates to these receptors.
23934049	5	63	theme	antifolates	1004:1014	arg1	modes					984:988	distinct binding modes	967:988	distinct binding modes	967:988	Here we describe six distinct crystallographic models that provide insight into biological trafficking of FRs and distinct binding modes of folate and antifolates to these receptors.
23934049	8	64	theme	rapid	1458:1462	arg1	design					1464:1469	rapid design	1458:1469	rapid design	1458:1469	On the whole, our data form the basis for rapid design and implementation of unique, FR-targeted, folate-based drugs for the treatment of cancer and inflammatory diseases.
23934049	3	65	theme	new	598:600	arg1	classes					602:608	new classes	598:608	new classes of antifolates or folate conjugates	598:644	More recently, human folate receptors (FRs), high affinity receptors that transport folate via endocytosis, have been proposed as targets for the specific delivery of new classes of antifolates or folate conjugates to tumors or sites of inflammation.
23934049	4	66	theme	structural	801:810	arg1	models					812:817	particularly structural models	788:817	particularly structural models of the receptors	788:834	The development of specific, FR-targeted antifolates would be accelerated if additional biophysical data, particularly structural models of the receptors, were available.
23934049	4	66	theme	structural	801:810	arg1	data					782:785	additional biophysical data	759:785	additional biophysical data	759:785	The development of specific, FR-targeted antifolates would be accelerated if additional biophysical data, particularly structural models of the receptors, were available.
23934049	3	67	theme	antifolates	613:623	arg1	classes					602:608	new classes	598:608	new classes of antifolates or folate conjugates	598:644	More recently, human folate receptors (FRs), high affinity receptors that transport folate via endocytosis, have been proposed as targets for the specific delivery of new classes of antifolates or folate conjugates to tumors or sites of inflammation.
23934049	6	68	theme	FRs	1179:1181	arg1	trafficking					1164:1174	the endocytic trafficking	1150:1174	the endocytic trafficking of FRs	1150:1181	From comparison of the structures, we delineate discrete structural conformations representative of key stages in the endocytic trafficking of FRs and propose models for pH-dependent conformational changes.
23934049	3	69	theme	conjugates	635:644	arg1	classes					602:608	new classes	598:608	new classes of antifolates or folate conjugates	598:644	More recently, human folate receptors (FRs), high affinity receptors that transport folate via endocytosis, have been proposed as targets for the specific delivery of new classes of antifolates or folate conjugates to tumors or sites of inflammation.
23934049	3	70	theme	classes	602:608	arg1	delivery					586:593	the specific delivery	573:593	the specific delivery of new classes of antifolates or folate conjugates to tumors or sites of inflammation	573:679	More recently, human folate receptors (FRs), high affinity receptors that transport folate via endocytosis, have been proposed as targets for the specific delivery of new classes of antifolates or folate conjugates to tumors or sites of inflammation.
23934049	1	71	theme	folate	139:144	arg1	Antifolates					126:136	Antifolates	126:136	Antifolates	126:136	Antifolates, folate analogs that inhibit vitamin B9 (folic acid)-using cellular enzymes, have been used over several decades for the treatment of cancer and inflammatory diseases.
23934049	1	71	theme	folate	139:144	arg1	analogs					146:152	folate analogs	139:152	folate analogs that inhibit vitamin B9 (folic acid)-using cellular enzymes	139:212	Antifolates, folate analogs that inhibit vitamin B9 (folic acid)-using cellular enzymes, have been used over several decades for the treatment of cancer and inflammatory diseases.
23934049	4	72	theme	specific	701:708	arg1	antifolates					723:733	specific, FR-targeted antifolates	701:733	specific, FR-targeted antifolates	701:733	The development of specific, FR-targeted antifolates would be accelerated if additional biophysical data, particularly structural models of the receptors, were available.
23934049	3	73	theme	folate	452:457	arg1	receptors					490:498	high affinity receptors	476:498	high affinity receptors that transport folate via endocytosis	476:536	More recently, human folate receptors (FRs), high affinity receptors that transport folate via endocytosis, have been proposed as targets for the specific delivery of new classes of antifolates or folate conjugates to tumors or sites of inflammation.
23934049	3	73	theme	folate	452:457	arg1	FRs					470:472	FRs	470:472	FRs	470:472	More recently, human folate receptors (FRs), high affinity receptors that transport folate via endocytosis, have been proposed as targets for the specific delivery of new classes of antifolates or folate conjugates to tumors or sites of inflammation.
23934049	3	73	theme	folate	452:457	arg1	receptors					459:467	human folate receptors	446:467	human folate receptors (FRs)	446:473	More recently, human folate receptors (FRs), high affinity receptors that transport folate via endocytosis, have been proposed as targets for the specific delivery of new classes of antifolates or folate conjugates to tumors or sites of inflammation.
23934049	3	73	theme	folate	452:457	arg1	targets					561:567	targets	561:567	targets for the specific delivery of new classes of antifolates or folate conjugates to tumors or sites of inflammation	561:679	More recently, human folate receptors (FRs), high affinity receptors that transport folate via endocytosis, have been proposed as targets for the specific delivery of new classes of antifolates or folate conjugates to tumors or sites of inflammation.
23934049	3	74	theme	human	446:450	arg1	receptors					490:498	high affinity receptors	476:498	high affinity receptors that transport folate via endocytosis	476:536	More recently, human folate receptors (FRs), high affinity receptors that transport folate via endocytosis, have been proposed as targets for the specific delivery of new classes of antifolates or folate conjugates to tumors or sites of inflammation.
23934049	3	74	theme	human	446:450	arg1	FRs					470:472	FRs	470:472	FRs	470:472	More recently, human folate receptors (FRs), high affinity receptors that transport folate via endocytosis, have been proposed as targets for the specific delivery of new classes of antifolates or folate conjugates to tumors or sites of inflammation.
23934049	3	74	theme	human	446:450	arg1	receptors					459:467	human folate receptors	446:467	human folate receptors (FRs)	446:473	More recently, human folate receptors (FRs), high affinity receptors that transport folate via endocytosis, have been proposed as targets for the specific delivery of new classes of antifolates or folate conjugates to tumors or sites of inflammation.
23934049	3	74	theme	human	446:450	arg1	targets					561:567	targets	561:567	targets for the specific delivery of new classes of antifolates or folate conjugates to tumors or sites of inflammation	561:679	More recently, human folate receptors (FRs), high affinity receptors that transport folate via endocytosis, have been proposed as targets for the specific delivery of new classes of antifolates or folate conjugates to tumors or sites of inflammation.
23934049	8	75	theme	drugs	1527:1531	arg1	design					1464:1469	rapid design	1458:1469	rapid design	1458:1469	On the whole, our data form the basis for rapid design and implementation of unique, FR-targeted, folate-based drugs for the treatment of cancer and inflammatory diseases.
23934049	8	75	theme	drugs	1527:1531	arg1	implementation					1475:1488	implementation	1475:1488	implementation	1475:1488	On the whole, our data form the basis for rapid design and implementation of unique, FR-targeted, folate-based drugs for the treatment of cancer and inflammatory diseases.
23934049	6	76	theme	representative	1118:1131	arg1	conformations					1104:1116	discrete structural conformations	1084:1116	discrete structural conformations representative of key stages in the endocytic trafficking of FRs	1084:1181	From comparison of the structures, we delineate discrete structural conformations representative of key stages in the endocytic trafficking of FRs and propose models for pH-dependent conformational changes.
23934049	3	77	theme	inflammation	668:679	arg1	inflammation					668:679	inflammation	668:679	inflammation	668:679	More recently, human folate receptors (FRs), high affinity receptors that transport folate via endocytosis, have been proposed as targets for the specific delivery of new classes of antifolates or folate conjugates to tumors or sites of inflammation.
23934049	3	77	theme	inflammation	668:679	arg1	sites					659:663	sites	659:663	sites of inflammation	659:679	More recently, human folate receptors (FRs), high affinity receptors that transport folate via endocytosis, have been proposed as targets for the specific delivery of new classes of antifolates or folate conjugates to tumors or sites of inflammation.
23934049	3	77	theme	inflammation	668:679	arg1	tumors					649:654	tumors	649:654	tumors	649:654	More recently, human folate receptors (FRs), high affinity receptors that transport folate via endocytosis, have been proposed as targets for the specific delivery of new classes of antifolates or folate conjugates to tumors or sites of inflammation.
23934049	1	78	dep	-using	190:195	arg1	acid					185:188	folic acid	179:188	folic acid	179:188	Antifolates, folate analogs that inhibit vitamin B9 (folic acid)-using cellular enzymes, have been used over several decades for the treatment of cancer and inflammatory diseases.
23934049	2	79	theme	clinical	344:351	arg1	use					353:355	clinical use	344:355	clinical use	344:355	Cellular uptake of the antifolates in clinical use occurs primarily via widely expressed facilitative membrane transporters.
1150658	2	0	theme	acid	103:106	arg1	sequences					108:116	The amino acid sequences	93:116	The amino acid sequences of both the alpha and beta subunits of human chorionic gonadotropin	93:184	The amino acid sequences of both the alpha and beta subunits of human chorionic gonadotropin have been determined.
1150658	12	1	from	helpful	2320:2326	arg1	determination					2335:2347	the determination	2331:2347	the determination of the beta sequence	2331:2368	The proteolytic enzyme, thrombin, which appears to cleave a limited number of arginyl bonds, proved helpful in the determination of the beta sequence.
1150658	2	2	theme	amino	97:101	arg1	sequences					108:116	The amino acid sequences	93:116	The amino acid sequences of both the alpha and beta subunits of human chorionic gonadotropin	93:184	The amino acid sequences of both the alpha and beta subunits of human chorionic gonadotropin have been determined.
1150658	12	3	theme	limited	2280:2286	arg1	number					2288:2293	a limited number	2278:2293	a limited number of arginyl bonds	2278:2310	The proteolytic enzyme, thrombin, which appears to cleave a limited number of arginyl bonds, proved helpful in the determination of the beta sequence.
1150658	3	4	dep	Thr	521:523	arg1	Val					710:712	Val	710:712	Val	710:712	The amino acid sequence of the alpha subunit is: Ala - Asp - Val - Gln - Asp - Cys - Pro - Glu - Cys-10 - Thr - Leu - Gln - Asp - Pro - Phe - Ser - Gln-20 - Pro - Gly - Ala - Pro - Ile - Leu - Gln - Cys - Met - Gly-30 - Cys - Cys - Phe - Ser - Arg - Ala - Tyr - Pro - Thr - Pro-40 - Leu - Arg - Ser - Lys - Lys - Thr - Met - Leu - Val - Gln-50 - Lys - Asn - Val - Thr - Ser - Glu - Ser - Thr - Cys - Cys-60 - Val - Ala - Lys - Ser - Thr - Asn - Arg - Val - Thr - Val-70 - Met - Gly - Gly - Phe - Lys - Val - Glu - Asn - His - Thr-80 - Ala - Cys - His - Cys - Ser - Thr - Cys - Tyr - Tyr - His-90 - Lys - Ser.
1150658	3	4	dep	Thr	521:523	arg1	Asn					722:724	Asn	722:724	Thr - Met - Leu - Val - Gln-50 - Lys - Asn - Val - Thr - Ser - Glu - Ser - Thr - Cys - Cys-60 - Val - Ala - Lys - Ser - Thr - Asn - Arg - Val - Thr - Val-70 - Met - Gly - Gly - Phe - Lys - Val - Glu - Asn	521:724	The amino acid sequence of the alpha subunit is: Ala - Asp - Val - Gln - Asp - Cys - Pro - Glu - Cys-10 - Thr - Leu - Gln - Asp - Pro - Phe - Ser - Gln-20 - Pro - Gly - Ala - Pro - Ile - Leu - Gln - Cys - Met - Gly-30 - Cys - Cys - Phe - Ser - Arg - Ala - Tyr - Pro - Thr - Pro-40 - Leu - Arg - Ser - Lys - Lys - Thr - Met - Leu - Val - Gln-50 - Lys - Asn - Val - Thr - Ser - Glu - Ser - Thr - Cys - Cys-60 - Val - Ala - Lys - Ser - Thr - Asn - Arg - Val - Thr - Val-70 - Met - Gly - Gly - Phe - Lys - Val - Glu - Asn - His - Thr-80 - Ala - Cys - His - Cys - Ser - Thr - Cys - Tyr - Tyr - His-90 - Lys - Ser.
1150658	3	4	dep	Thr	521:523	arg1	Lys					704:706	Lys	704:706	Lys	704:706	The amino acid sequence of the alpha subunit is: Ala - Asp - Val - Gln - Asp - Cys - Pro - Glu - Cys-10 - Thr - Leu - Gln - Asp - Pro - Phe - Ser - Gln-20 - Pro - Gly - Ala - Pro - Ile - Leu - Gln - Cys - Met - Gly-30 - Cys - Cys - Phe - Ser - Arg - Ala - Tyr - Pro - Thr - Pro-40 - Leu - Arg - Ser - Lys - Lys - Thr - Met - Leu - Val - Gln-50 - Lys - Asn - Val - Thr - Ser - Glu - Ser - Thr - Cys - Cys-60 - Val - Ala - Lys - Ser - Thr - Asn - Arg - Val - Thr - Val-70 - Met - Gly - Gly - Phe - Lys - Val - Glu - Asn - His - Thr-80 - Ala - Cys - His - Cys - Ser - Thr - Cys - Tyr - Tyr - His-90 - Lys - Ser.
1150658	3	4	dep	Thr	521:523	arg1	Phe					698:700	Phe	698:700	Phe	698:700	The amino acid sequence of the alpha subunit is: Ala - Asp - Val - Gln - Asp - Cys - Pro - Glu - Cys-10 - Thr - Leu - Gln - Asp - Pro - Phe - Ser - Gln-20 - Pro - Gly - Ala - Pro - Ile - Leu - Gln - Cys - Met - Gly-30 - Cys - Cys - Phe - Ser - Arg - Ala - Tyr - Pro - Thr - Pro-40 - Leu - Arg - Ser - Lys - Lys - Thr - Met - Leu - Val - Gln-50 - Lys - Asn - Val - Thr - Ser - Glu - Ser - Thr - Cys - Cys-60 - Val - Ala - Lys - Ser - Thr - Asn - Arg - Val - Thr - Val-70 - Met - Gly - Gly - Phe - Lys - Val - Glu - Asn - His - Thr-80 - Ala - Cys - His - Cys - Ser - Thr - Cys - Tyr - Tyr - His-90 - Lys - Ser.
1150658	3	4	dep	Thr	521:523	arg1	Glu					716:718	Glu	716:718	Glu	716:718	The amino acid sequence of the alpha subunit is: Ala - Asp - Val - Gln - Asp - Cys - Pro - Glu - Cys-10 - Thr - Leu - Gln - Asp - Pro - Phe - Ser - Gln-20 - Pro - Gly - Ala - Pro - Ile - Leu - Gln - Cys - Met - Gly-30 - Cys - Cys - Phe - Ser - Arg - Ala - Tyr - Pro - Thr - Pro-40 - Leu - Arg - Ser - Lys - Lys - Thr - Met - Leu - Val - Gln-50 - Lys - Asn - Val - Thr - Ser - Glu - Ser - Thr - Cys - Cys-60 - Val - Ala - Lys - Ser - Thr - Asn - Arg - Val - Thr - Val-70 - Met - Gly - Gly - Phe - Lys - Val - Glu - Asn - His - Thr-80 - Ala - Cys - His - Cys - Ser - Thr - Cys - Tyr - Tyr - His-90 - Lys - Ser.
1150658	3	5	dep	Ala	257:259	arg1	Lys					806:808	Lys	806:808	Lys	806:808	The amino acid sequence of the alpha subunit is: Ala - Asp - Val - Gln - Asp - Cys - Pro - Glu - Cys-10 - Thr - Leu - Gln - Asp - Pro - Phe - Ser - Gln-20 - Pro - Gly - Ala - Pro - Ile - Leu - Gln - Cys - Met - Gly-30 - Cys - Cys - Phe - Ser - Arg - Ala - Tyr - Pro - Thr - Pro-40 - Leu - Arg - Ser - Lys - Lys - Thr - Met - Leu - Val - Gln-50 - Lys - Asn - Val - Thr - Ser - Glu - Ser - Thr - Cys - Cys-60 - Val - Ala - Lys - Ser - Thr - Asn - Arg - Val - Thr - Val-70 - Met - Gly - Gly - Phe - Lys - Val - Glu - Asn - His - Thr-80 - Ala - Cys - His - Cys - Ser - Thr - Cys - Tyr - Tyr - His-90 - Lys - Ser.
1150658	3	5	dep	Ala	257:259	arg1	Tyr					464:466	Tyr	464:466	Tyr	464:466	The amino acid sequence of the alpha subunit is: Ala - Asp - Val - Gln - Asp - Cys - Pro - Glu - Cys-10 - Thr - Leu - Gln - Asp - Pro - Phe - Ser - Gln-20 - Pro - Gly - Ala - Pro - Ile - Leu - Gln - Cys - Met - Gly-30 - Cys - Cys - Phe - Ser - Arg - Ala - Tyr - Pro - Thr - Pro-40 - Leu - Arg - Ser - Lys - Lys - Thr - Met - Leu - Val - Gln-50 - Lys - Asn - Val - Thr - Ser - Glu - Ser - Thr - Cys - Cys-60 - Val - Ala - Lys - Ser - Thr - Asn - Arg - Val - Thr - Val-70 - Met - Gly - Gly - Phe - Lys - Val - Glu - Asn - His - Thr-80 - Ala - Cys - His - Cys - Ser - Thr - Cys - Tyr - Tyr - His-90 - Lys - Ser.
1150658	3	5	dep	Ala	257:259	arg1	Pro					383:385	Pro	383:385	Pro	383:385	The amino acid sequence of the alpha subunit is: Ala - Asp - Val - Gln - Asp - Cys - Pro - Glu - Cys-10 - Thr - Leu - Gln - Asp - Pro - Phe - Ser - Gln-20 - Pro - Gly - Ala - Pro - Ile - Leu - Gln - Cys - Met - Gly-30 - Cys - Cys - Phe - Ser - Arg - Ala - Tyr - Pro - Thr - Pro-40 - Leu - Arg - Ser - Lys - Lys - Thr - Met - Leu - Val - Gln-50 - Lys - Asn - Val - Thr - Ser - Glu - Ser - Thr - Cys - Cys-60 - Val - Ala - Lys - Ser - Thr - Asn - Arg - Val - Thr - Val-70 - Met - Gly - Gly - Phe - Lys - Val - Glu - Asn - His - Thr-80 - Ala - Cys - His - Cys - Ser - Thr - Cys - Tyr - Tyr - His-90 - Lys - Ser.
1150658	3	5	dep	Ala	257:259	arg1	Ser					446:448	Ser	446:448	Ser	446:448	The amino acid sequence of the alpha subunit is: Ala - Asp - Val - Gln - Asp - Cys - Pro - Glu - Cys-10 - Thr - Leu - Gln - Asp - Pro - Phe - Ser - Gln-20 - Pro - Gly - Ala - Pro - Ile - Leu - Gln - Cys - Met - Gly-30 - Cys - Cys - Phe - Ser - Arg - Ala - Tyr - Pro - Thr - Pro-40 - Leu - Arg - Ser - Lys - Lys - Thr - Met - Leu - Val - Gln-50 - Lys - Asn - Val - Thr - Ser - Glu - Ser - Thr - Cys - Cys-60 - Val - Ala - Lys - Ser - Thr - Asn - Arg - Val - Thr - Val-70 - Met - Gly - Gly - Phe - Lys - Val - Glu - Asn - His - Thr-80 - Ala - Cys - His - Cys - Ser - Thr - Cys - Tyr - Tyr - His-90 - Lys - Ser.
1150658	3	5	dep	Ala	257:259	arg1	Ser					812:814	Ser	812:814	Ala - Asp - Val - Gln - Asp - Cys - Pro - Glu - Cys-10 - Thr - Leu - Gln - Asp - Pro - Phe - Ser - Gln-20 - Pro - Gly - Ala - Pro - Ile - Leu - Gln - Cys - Met - Gly-30 - Cys - Cys - Phe - Ser - Arg - Ala - Tyr - Pro - Thr - Pro-40 - Leu - Arg - Ser - Lys - Lys - Thr - Met - Leu - Val - Gln-50 - Lys - Asn - Val - Thr - Ser - Glu - Ser - Thr - Cys - Cys-60 - Val - Ala - Lys - Ser - Thr - Asn - Arg - Val - Thr - Val-70 - Met - Gly - Gly - Phe - Lys - Val - Glu - Asn - His - Thr-80 - Ala - Cys - His - Cys - Ser - Thr - Cys - Tyr - Tyr - His-90 - Lys - Ser	257:814	The amino acid sequence of the alpha subunit is: Ala - Asp - Val - Gln - Asp - Cys - Pro - Glu - Cys-10 - Thr - Leu - Gln - Asp - Pro - Phe - Ser - Gln-20 - Pro - Gly - Ala - Pro - Ile - Leu - Gln - Cys - Met - Gly-30 - Cys - Cys - Phe - Ser - Arg - Ala - Tyr - Pro - Thr - Pro-40 - Leu - Arg - Ser - Lys - Lys - Thr - Met - Leu - Val - Gln-50 - Lys - Asn - Val - Thr - Ser - Glu - Ser - Thr - Cys - Cys-60 - Val - Ala - Lys - Ser - Thr - Asn - Arg - Val - Thr - Val-70 - Met - Gly - Gly - Phe - Lys - Val - Glu - Asn - His - Thr-80 - Ala - Cys - His - Cys - Ser - Thr - Cys - Tyr - Tyr - His-90 - Lys - Ser.
1150658	3	5	dep	Ala	257:259	arg1	Arg					452:454	Arg	452:454	Arg	452:454	The amino acid sequence of the alpha subunit is: Ala - Asp - Val - Gln - Asp - Cys - Pro - Glu - Cys-10 - Thr - Leu - Gln - Asp - Pro - Phe - Ser - Gln-20 - Pro - Gly - Ala - Pro - Ile - Leu - Gln - Cys - Met - Gly-30 - Cys - Cys - Phe - Ser - Arg - Ala - Tyr - Pro - Thr - Pro-40 - Leu - Arg - Ser - Lys - Lys - Thr - Met - Leu - Val - Gln-50 - Lys - Asn - Val - Thr - Ser - Glu - Ser - Thr - Cys - Cys-60 - Val - Ala - Lys - Ser - Thr - Asn - Arg - Val - Thr - Val-70 - Met - Gly - Gly - Phe - Lys - Val - Glu - Asn - His - Thr-80 - Ala - Cys - His - Cys - Ser - Thr - Cys - Tyr - Tyr - His-90 - Lys - Ser.
1150658	3	5	dep	Ala	257:259	arg1	Ala					377:379	Ala	377:379	Ala	377:379	The amino acid sequence of the alpha subunit is: Ala - Asp - Val - Gln - Asp - Cys - Pro - Glu - Cys-10 - Thr - Leu - Gln - Asp - Pro - Phe - Ser - Gln-20 - Pro - Gly - Ala - Pro - Ile - Leu - Gln - Cys - Met - Gly-30 - Cys - Cys - Phe - Ser - Arg - Ala - Tyr - Pro - Thr - Pro-40 - Leu - Arg - Ser - Lys - Lys - Thr - Met - Leu - Val - Gln-50 - Lys - Asn - Val - Thr - Ser - Glu - Ser - Thr - Cys - Cys-60 - Val - Ala - Lys - Ser - Thr - Asn - Arg - Val - Thr - Val-70 - Met - Gly - Gly - Phe - Lys - Val - Glu - Asn - His - Thr-80 - Ala - Cys - His - Cys - Ser - Thr - Cys - Tyr - Tyr - His-90 - Lys - Ser.
1150658	3	5	dep	Ala	257:259	arg1	His-90					797:802	His-90	797:802	His-90	797:802	The amino acid sequence of the alpha subunit is: Ala - Asp - Val - Gln - Asp - Cys - Pro - Glu - Cys-10 - Thr - Leu - Gln - Asp - Pro - Phe - Ser - Gln-20 - Pro - Gly - Ala - Pro - Ile - Leu - Gln - Cys - Met - Gly-30 - Cys - Cys - Phe - Ser - Arg - Ala - Tyr - Pro - Thr - Pro-40 - Leu - Arg - Ser - Lys - Lys - Thr - Met - Leu - Val - Gln-50 - Lys - Asn - Val - Thr - Ser - Glu - Ser - Thr - Cys - Cys-60 - Val - Ala - Lys - Ser - Thr - Asn - Arg - Val - Thr - Val-70 - Met - Gly - Gly - Phe - Lys - Val - Glu - Asn - His - Thr-80 - Ala - Cys - His - Cys - Ser - Thr - Cys - Tyr - Tyr - His-90 - Lys - Ser.
1150658	3	5	dep	Ala	257:259	arg1	Phe					440:442	Phe	440:442	Phe	440:442	The amino acid sequence of the alpha subunit is: Ala - Asp - Val - Gln - Asp - Cys - Pro - Glu - Cys-10 - Thr - Leu - Gln - Asp - Pro - Phe - Ser - Gln-20 - Pro - Gly - Ala - Pro - Ile - Leu - Gln - Cys - Met - Gly-30 - Cys - Cys - Phe - Ser - Arg - Ala - Tyr - Pro - Thr - Pro-40 - Leu - Arg - Ser - Lys - Lys - Thr - Met - Leu - Val - Gln-50 - Lys - Asn - Val - Thr - Ser - Glu - Ser - Thr - Cys - Cys-60 - Val - Ala - Lys - Ser - Thr - Asn - Arg - Val - Thr - Val-70 - Met - Gly - Gly - Phe - Lys - Val - Glu - Asn - His - Thr-80 - Ala - Cys - His - Cys - Ser - Thr - Cys - Tyr - Tyr - His-90 - Lys - Ser.
1150658	2	6	theme	alpha	130:134	arg1	subunits					145:152	both the alpha and beta subunits	121:152	subunits	145:152	The amino acid sequences of both the alpha and beta subunits of human chorionic gonadotropin have been determined.
1150658	12	7	theme	beta	2356:2359	arg1	sequence					2361:2368	the beta sequence	2352:2368	the beta sequence	2352:2368	The proteolytic enzyme, thrombin, which appears to cleave a limited number of arginyl bonds, proved helpful in the determination of the beta sequence.
1150658	6	8	theme	luteinizing	1063:1073	arg1	hormone					1075:1081	human luteinizing hormone	1057:1081	human luteinizing hormone	1057:1081	This sequence is almost identical with that of human luteinizing hormone (Sairam, M. R., Papkoff, H., and Li, C. H. (1972) Biochem.
1150658	1	9	theme	alpha	61:65	arg1	subunit					67:73	alpha subunit	61:73	alpha subunit	61:73	The alpha subunit and beta subunit.
1150658	6	10	with	identical	1034:1042	arg1	that					1049:1052	that	1049:1052	that	1049:1052	This sequence is almost identical with that of human luteinizing hormone (Sairam, M. R., Papkoff, H., and Li, C. H. (1972) Biochem.
1150658	11	11	located	found	2170:2174	arg1	residues					2179:2186	residues 13, 30, 121, 127, 132, and 138	2179:2217	residues 13, 30, 121, 127, 132, and 138	2179:2217	Oligosaccharide side chains are found at residues 13, 30, 121, 127, 132, and 138.
1150658	11	11	located	found	2170:2174	arg2	chains					2159:2164	Oligosaccharide side chains	2138:2164	Oligosaccharide side chains	2138:2164	Oligosaccharide side chains are found at residues 13, 30, 121, 127, 132, and 138.
1150658	6	12	theme	human	1057:1061	arg1	hormone					1075:1081	human luteinizing hormone	1057:1081	human luteinizing hormone	1057:1081	This sequence is almost identical with that of human luteinizing hormone (Sairam, M. R., Papkoff, H., and Li, C. H. (1972) Biochem.
1150658	5	13	theme	initial	957:963	arg1	residues					986:993	the initial 2 and 3 NH2-terminal residues	953:993	the initial 2 and 3 NH2-terminal residues	953:993	In the preparations studied approximately 10 and 30% of the chains lack the initial 2 and 3 NH2-terminal residues, respectively.
1150658	0	14	theme	amino	4:8	arg1	sequence					15:22	The amino acid sequence	0:22	The amino acid sequence of human chorionic gonadotropin	0:54	The amino acid sequence of human chorionic gonadotropin.
1150658	3	15	theme	amino	212:216	arg1	Ala					257:259	Ala	257:259	Ala	257:259	The amino acid sequence of the alpha subunit is: Ala - Asp - Val - Gln - Asp - Cys - Pro - Glu - Cys-10 - Thr - Leu - Gln - Asp - Pro - Phe - Ser - Gln-20 - Pro - Gly - Ala - Pro - Ile - Leu - Gln - Cys - Met - Gly-30 - Cys - Cys - Phe - Ser - Arg - Ala - Tyr - Pro - Thr - Pro-40 - Leu - Arg - Ser - Lys - Lys - Thr - Met - Leu - Val - Gln-50 - Lys - Asn - Val - Thr - Ser - Glu - Ser - Thr - Cys - Cys-60 - Val - Ala - Lys - Ser - Thr - Asn - Arg - Val - Thr - Val-70 - Met - Gly - Gly - Phe - Lys - Val - Glu - Asn - His - Thr-80 - Ala - Cys - His - Cys - Ser - Thr - Cys - Tyr - Tyr - His-90 - Lys - Ser.
1150658	3	15	theme	amino	212:216	arg1	sequence					223:230	The amino acid sequence	208:230	The amino acid sequence of the alpha subunit	208:251	The amino acid sequence of the alpha subunit is: Ala - Asp - Val - Gln - Asp - Cys - Pro - Glu - Cys-10 - Thr - Leu - Gln - Asp - Pro - Phe - Ser - Gln-20 - Pro - Gly - Ala - Pro - Ile - Leu - Gln - Cys - Met - Gly-30 - Cys - Cys - Phe - Ser - Arg - Ala - Tyr - Pro - Thr - Pro-40 - Leu - Arg - Ser - Lys - Lys - Thr - Met - Leu - Val - Gln-50 - Lys - Asn - Val - Thr - Ser - Glu - Ser - Thr - Cys - Cys-60 - Val - Ala - Lys - Ser - Thr - Asn - Arg - Val - Thr - Val-70 - Met - Gly - Gly - Phe - Lys - Val - Glu - Asn - His - Thr-80 - Ala - Cys - His - Cys - Ser - Thr - Cys - Tyr - Tyr - His-90 - Lys - Ser.
1150658	12	16	theme	sequence	2361:2368	arg1	determination					2335:2347	the determination	2331:2347	the determination of the beta sequence	2331:2368	The proteolytic enzyme, thrombin, which appears to cleave a limited number of arginyl bonds, proved helpful in the determination of the beta sequence.
1150658	12	17	theme	bonds	2306:2310	arg1	number					2288:2293	a limited number	2278:2293	a limited number of arginyl bonds	2278:2310	The proteolytic enzyme, thrombin, which appears to cleave a limited number of arginyl bonds, proved helpful in the determination of the beta sequence.
1150658	3	18	theme	acid	218:221	arg1	Ala					257:259	Ala	257:259	Ala	257:259	The amino acid sequence of the alpha subunit is: Ala - Asp - Val - Gln - Asp - Cys - Pro - Glu - Cys-10 - Thr - Leu - Gln - Asp - Pro - Phe - Ser - Gln-20 - Pro - Gly - Ala - Pro - Ile - Leu - Gln - Cys - Met - Gly-30 - Cys - Cys - Phe - Ser - Arg - Ala - Tyr - Pro - Thr - Pro-40 - Leu - Arg - Ser - Lys - Lys - Thr - Met - Leu - Val - Gln-50 - Lys - Asn - Val - Thr - Ser - Glu - Ser - Thr - Cys - Cys-60 - Val - Ala - Lys - Ser - Thr - Asn - Arg - Val - Thr - Val-70 - Met - Gly - Gly - Phe - Lys - Val - Glu - Asn - His - Thr-80 - Ala - Cys - His - Cys - Ser - Thr - Cys - Tyr - Tyr - His-90 - Lys - Ser.
1150658	3	18	theme	acid	218:221	arg1	sequence					223:230	The amino acid sequence	208:230	The amino acid sequence of the alpha subunit	208:251	The amino acid sequence of the alpha subunit is: Ala - Asp - Val - Gln - Asp - Cys - Pro - Glu - Cys-10 - Thr - Leu - Gln - Asp - Pro - Phe - Ser - Gln-20 - Pro - Gly - Ala - Pro - Ile - Leu - Gln - Cys - Met - Gly-30 - Cys - Cys - Phe - Ser - Arg - Ala - Tyr - Pro - Thr - Pro-40 - Leu - Arg - Ser - Lys - Lys - Thr - Met - Leu - Val - Gln-50 - Lys - Asn - Val - Thr - Ser - Glu - Ser - Thr - Cys - Cys-60 - Val - Ala - Lys - Ser - Thr - Asn - Arg - Val - Thr - Val-70 - Met - Gly - Gly - Phe - Lys - Val - Glu - Asn - His - Thr-80 - Ala - Cys - His - Cys - Ser - Thr - Cys - Tyr - Tyr - His-90 - Lys - Ser.
1150658	1	19	theme	beta	79:82	arg1	subunit					84:90	beta subunit	79:90	beta subunit	79:90	The alpha subunit and beta subunit.
1150658	6	20	dep	R.	1095:1096	arg1	H					1123:1123	H	1123:1123	H	1123:1123	This sequence is almost identical with that of human luteinizing hormone (Sairam, M. R., Papkoff, H., and Li, C. H. (1972) Biochem.
1150658	6	20	dep	R.	1095:1096	arg1	Biochem					1133:1139	Biochem	1133:1139	Sairam, M. R., Papkoff, H., and Li, C. H. (1972) Biochem	1084:1139	This sequence is almost identical with that of human luteinizing hormone (Sairam, M. R., Papkoff, H., and Li, C. H. (1972) Biochem.
1150658	3	21	theme	subunit	245:251	arg1	Ala					257:259	Ala	257:259	Ala	257:259	The amino acid sequence of the alpha subunit is: Ala - Asp - Val - Gln - Asp - Cys - Pro - Glu - Cys-10 - Thr - Leu - Gln - Asp - Pro - Phe - Ser - Gln-20 - Pro - Gly - Ala - Pro - Ile - Leu - Gln - Cys - Met - Gly-30 - Cys - Cys - Phe - Ser - Arg - Ala - Tyr - Pro - Thr - Pro-40 - Leu - Arg - Ser - Lys - Lys - Thr - Met - Leu - Val - Gln-50 - Lys - Asn - Val - Thr - Ser - Glu - Ser - Thr - Cys - Cys-60 - Val - Ala - Lys - Ser - Thr - Asn - Arg - Val - Thr - Val-70 - Met - Gly - Gly - Phe - Lys - Val - Glu - Asn - His - Thr-80 - Ala - Cys - His - Cys - Ser - Thr - Cys - Tyr - Tyr - His-90 - Lys - Ser.
1150658	3	21	theme	subunit	245:251	arg1	sequence					223:230	The amino acid sequence	208:230	The amino acid sequence of the alpha subunit	208:251	The amino acid sequence of the alpha subunit is: Ala - Asp - Val - Gln - Asp - Cys - Pro - Glu - Cys-10 - Thr - Leu - Gln - Asp - Pro - Phe - Ser - Gln-20 - Pro - Gly - Ala - Pro - Ile - Leu - Gln - Cys - Met - Gly-30 - Cys - Cys - Phe - Ser - Arg - Ala - Tyr - Pro - Thr - Pro-40 - Leu - Arg - Ser - Lys - Lys - Thr - Met - Leu - Val - Gln-50 - Lys - Asn - Val - Thr - Ser - Glu - Ser - Thr - Cys - Cys-60 - Val - Ala - Lys - Ser - Thr - Asn - Arg - Val - Thr - Val-70 - Met - Gly - Gly - Phe - Lys - Val - Glu - Asn - His - Thr-80 - Ala - Cys - His - Cys - Ser - Thr - Cys - Tyr - Tyr - His-90 - Lys - Ser.
1150658	0	22	theme	acid	10:13	arg1	sequence					15:22	The amino acid sequence	0:22	The amino acid sequence of human chorionic gonadotropin	0:54	The amino acid sequence of human chorionic gonadotropin.
1150658	4	23	attach	attached	849:856	arg3	78					877:878	78	877:878	78	877:878	Oligosaccharide side chains are attached at residues 52 and 78.
1150658	4	23	attach	attached	849:856	arg2	chains					838:843	Oligosaccharide side chains	817:843	Oligosaccharide side chains	817:843	Oligosaccharide side chains are attached at residues 52 and 78.
1150658	4	23	attach	attached	849:856	arg3	residues					861:868	residues 52 and 78	861:878	residues	861:868	Oligosaccharide side chains are attached at residues 52 and 78.
1150658	4	24	theme	side	833:836	arg1	chains					838:843	Oligosaccharide side chains	817:843	Oligosaccharide side chains	817:843	Oligosaccharide side chains are attached at residues 52 and 78.
1150658	0	25	theme	human	27:31	arg1	gonadotropin					43:54	human chorionic gonadotropin	27:54	human chorionic gonadotropin	27:54	The amino acid sequence of human chorionic gonadotropin.
1150658	2	26	theme	subunits	145:152	arg1	sequences					108:116	The amino acid sequences	93:116	The amino acid sequences of both the alpha and beta subunits of human chorionic gonadotropin	93:184	The amino acid sequences of both the alpha and beta subunits of human chorionic gonadotropin have been determined.
1150658	12	27	theme	arginyl	2298:2304	arg1	bonds					2306:2310	arginyl bonds	2298:2310	arginyl bonds	2298:2310	The proteolytic enzyme, thrombin, which appears to cleave a limited number of arginyl bonds, proved helpful in the determination of the beta sequence.
1150658	11	28	theme	Oligosaccharide	2138:2152	arg1	chains					2159:2164	Oligosaccharide side chains	2138:2164	Oligosaccharide side chains	2138:2164	Oligosaccharide side chains are found at residues 13, 30, 121, 127, 132, and 138.
1150658	6	29	dep	identical	1034:1042	arg1	1972					1127:1130	1972	1127:1130	1972	1127:1130	This sequence is almost identical with that of human luteinizing hormone (Sairam, M. R., Papkoff, H., and Li, C. H. (1972) Biochem.
1150658	6	29	dep	identical	1034:1042	arg1	R.					1095:1096	R.	1095:1096	R.	1095:1096	This sequence is almost identical with that of human luteinizing hormone (Sairam, M. R., Papkoff, H., and Li, C. H. (1972) Biochem.
1150658	6	29	dep	identical	1034:1042	arg1	C.					1120:1121	C.	1120:1121	C.	1120:1121	This sequence is almost identical with that of human luteinizing hormone (Sairam, M. R., Papkoff, H., and Li, C. H. (1972) Biochem.
1150658	6	29	dep	identical	1034:1042	arg1	H.					1108:1109	H.	1108:1109	H.	1108:1109	This sequence is almost identical with that of human luteinizing hormone (Sairam, M. R., Papkoff, H., and Li, C. H. (1972) Biochem.
1150658	6	29	dep	identical	1034:1042	arg1	M.					1092:1093	M.	1092:1093	M.	1092:1093	This sequence is almost identical with that of human luteinizing hormone (Sairam, M. R., Papkoff, H., and Li, C. H. (1972) Biochem.
1150658	3	30	theme	alpha	239:243	arg1	subunit					245:251	the alpha subunit	235:251	the alpha subunit	235:251	The amino acid sequence of the alpha subunit is: Ala - Asp - Val - Gln - Asp - Cys - Pro - Glu - Cys-10 - Thr - Leu - Gln - Asp - Pro - Phe - Ser - Gln-20 - Pro - Gly - Ala - Pro - Ile - Leu - Gln - Cys - Met - Gly-30 - Cys - Cys - Phe - Ser - Arg - Ala - Tyr - Pro - Thr - Pro-40 - Leu - Arg - Ser - Lys - Lys - Thr - Met - Leu - Val - Gln-50 - Lys - Asn - Val - Thr - Ser - Glu - Ser - Thr - Cys - Cys-60 - Val - Ala - Lys - Ser - Thr - Asn - Arg - Val - Thr - Val-70 - Met - Gly - Gly - Phe - Lys - Val - Glu - Asn - His - Thr-80 - Ala - Cys - His - Cys - Ser - Thr - Cys - Tyr - Tyr - His-90 - Lys - Ser.
1150658	2	31	theme	beta	140:143	arg1	subunits					145:152	both the alpha and beta subunits	121:152	subunits	145:152	The amino acid sequences of both the alpha and beta subunits of human chorionic gonadotropin have been determined.
1150658	10	32	dep	48	1164:1165	arg1	530-537					1168:1174	530-537	1168:1174	530-537	1168:1174	48, 530-537).
1150658	11	33	theme	side	2154:2157	arg1	chains					2159:2164	Oligosaccharide side chains	2138:2164	Oligosaccharide side chains	2138:2164	Oligosaccharide side chains are found at residues 13, 30, 121, 127, 132, and 138.
1150658	0	34	theme	gonadotropin	43:54	arg1	sequence					15:22	The amino acid sequence	0:22	The amino acid sequence of human chorionic gonadotropin	0:54	The amino acid sequence of human chorionic gonadotropin.
1150658	0	35	theme	chorionic	33:41	arg1	gonadotropin					43:54	human chorionic gonadotropin	27:54	human chorionic gonadotropin	27:54	The amino acid sequence of human chorionic gonadotropin.
1150658	3	36	dep	Lys	509:511	arg1	Thr-80					734:739	Thr-80	734:739	Thr-80	734:739	The amino acid sequence of the alpha subunit is: Ala - Asp - Val - Gln - Asp - Cys - Pro - Glu - Cys-10 - Thr - Leu - Gln - Asp - Pro - Phe - Ser - Gln-20 - Pro - Gly - Ala - Pro - Ile - Leu - Gln - Cys - Met - Gly-30 - Cys - Cys - Phe - Ser - Arg - Ala - Tyr - Pro - Thr - Pro-40 - Leu - Arg - Ser - Lys - Lys - Thr - Met - Leu - Val - Gln-50 - Lys - Asn - Val - Thr - Ser - Glu - Ser - Thr - Cys - Cys-60 - Val - Ala - Lys - Ser - Thr - Asn - Arg - Val - Thr - Val-70 - Met - Gly - Gly - Phe - Lys - Val - Glu - Asn - His - Thr-80 - Ala - Cys - His - Cys - Ser - Thr - Cys - Tyr - Tyr - His-90 - Lys - Ser.
1150658	3	36	dep	Lys	509:511	arg1	Lys					515:517	Lys	515:517	Lys	515:517	The amino acid sequence of the alpha subunit is: Ala - Asp - Val - Gln - Asp - Cys - Pro - Glu - Cys-10 - Thr - Leu - Gln - Asp - Pro - Phe - Ser - Gln-20 - Pro - Gly - Ala - Pro - Ile - Leu - Gln - Cys - Met - Gly-30 - Cys - Cys - Phe - Ser - Arg - Ala - Tyr - Pro - Thr - Pro-40 - Leu - Arg - Ser - Lys - Lys - Thr - Met - Leu - Val - Gln-50 - Lys - Asn - Val - Thr - Ser - Glu - Ser - Thr - Cys - Cys-60 - Val - Ala - Lys - Ser - Thr - Asn - Arg - Val - Thr - Val-70 - Met - Gly - Gly - Phe - Lys - Val - Glu - Asn - His - Thr-80 - Ala - Cys - His - Cys - Ser - Thr - Cys - Tyr - Tyr - His-90 - Lys - Ser.
1150658	3	36	dep	Lys	509:511	arg1	His					728:730	His	728:730	His	728:730	The amino acid sequence of the alpha subunit is: Ala - Asp - Val - Gln - Asp - Cys - Pro - Glu - Cys-10 - Thr - Leu - Gln - Asp - Pro - Phe - Ser - Gln-20 - Pro - Gly - Ala - Pro - Ile - Leu - Gln - Cys - Met - Gly-30 - Cys - Cys - Phe - Ser - Arg - Ala - Tyr - Pro - Thr - Pro-40 - Leu - Arg - Ser - Lys - Lys - Thr - Met - Leu - Val - Gln-50 - Lys - Asn - Val - Thr - Ser - Glu - Ser - Thr - Cys - Cys-60 - Val - Ala - Lys - Ser - Thr - Asn - Arg - Val - Thr - Val-70 - Met - Gly - Gly - Phe - Lys - Val - Glu - Asn - His - Thr-80 - Ala - Cys - His - Cys - Ser - Thr - Cys - Tyr - Tyr - His-90 - Lys - Ser.
1150658	3	36	dep	Lys	509:511	arg1	Thr					521:523	Thr	521:523	Thr	521:523	The amino acid sequence of the alpha subunit is: Ala - Asp - Val - Gln - Asp - Cys - Pro - Glu - Cys-10 - Thr - Leu - Gln - Asp - Pro - Phe - Ser - Gln-20 - Pro - Gly - Ala - Pro - Ile - Leu - Gln - Cys - Met - Gly-30 - Cys - Cys - Phe - Ser - Arg - Ala - Tyr - Pro - Thr - Pro-40 - Leu - Arg - Ser - Lys - Lys - Thr - Met - Leu - Val - Gln-50 - Lys - Asn - Val - Thr - Ser - Glu - Ser - Thr - Cys - Cys-60 - Val - Ala - Lys - Ser - Thr - Asn - Arg - Val - Thr - Val-70 - Met - Gly - Gly - Phe - Lys - Val - Glu - Asn - His - Thr-80 - Ala - Cys - His - Cys - Ser - Thr - Cys - Tyr - Tyr - His-90 - Lys - Ser.
1150658	3	36	dep	Lys	509:511	arg1	Ala					743:745	Ala	743:745	Ala	743:745	The amino acid sequence of the alpha subunit is: Ala - Asp - Val - Gln - Asp - Cys - Pro - Glu - Cys-10 - Thr - Leu - Gln - Asp - Pro - Phe - Ser - Gln-20 - Pro - Gly - Ala - Pro - Ile - Leu - Gln - Cys - Met - Gly-30 - Cys - Cys - Phe - Ser - Arg - Ala - Tyr - Pro - Thr - Pro-40 - Leu - Arg - Ser - Lys - Lys - Thr - Met - Leu - Val - Gln-50 - Lys - Asn - Val - Thr - Ser - Glu - Ser - Thr - Cys - Cys-60 - Val - Ala - Lys - Ser - Thr - Asn - Arg - Val - Thr - Val-70 - Met - Gly - Gly - Phe - Lys - Val - Glu - Asn - His - Thr-80 - Ala - Cys - His - Cys - Ser - Thr - Cys - Tyr - Tyr - His-90 - Lys - Ser.
1150658	1	37	dep	subunit	67:73	arg1	The					57:59	The	57:59	The	57:59	The alpha subunit and beta subunit.
1150658	2	38	theme	gonadotropin	173:184	arg1	subunits					145:152	both the alpha and beta subunits	121:152	subunits	145:152	The amino acid sequences of both the alpha and beta subunits of human chorionic gonadotropin have been determined.
1150658	2	39	theme	chorionic	163:171	arg1	gonadotropin					173:184	human chorionic gonadotropin	157:184	human chorionic gonadotropin	157:184	The amino acid sequences of both the alpha and beta subunits of human chorionic gonadotropin have been determined.
1150658	12	40	from	determination	2335:2347	arg1	helpful					2320:2326	helpful	2320:2326	helpful	2320:2326	The proteolytic enzyme, thrombin, which appears to cleave a limited number of arginyl bonds, proved helpful in the determination of the beta sequence.
1150658	2	41	theme	human	157:161	arg1	gonadotropin					173:184	human chorionic gonadotropin	157:184	human chorionic gonadotropin	157:184	The amino acid sequences of both the alpha and beta subunits of human chorionic gonadotropin have been determined.
1150658	3	42	dep	Asn	560:562	arg1	Ser					635:637	Ser	635:637	Ser	635:637	The amino acid sequence of the alpha subunit is: Ala - Asp - Val - Gln - Asp - Cys - Pro - Glu - Cys-10 - Thr - Leu - Gln - Asp - Pro - Phe - Ser - Gln-20 - Pro - Gly - Ala - Pro - Ile - Leu - Gln - Cys - Met - Gly-30 - Cys - Cys - Phe - Ser - Arg - Ala - Tyr - Pro - Thr - Pro-40 - Leu - Arg - Ser - Lys - Lys - Thr - Met - Leu - Val - Gln-50 - Lys - Asn - Val - Thr - Ser - Glu - Ser - Thr - Cys - Cys-60 - Val - Ala - Lys - Ser - Thr - Asn - Arg - Val - Thr - Val-70 - Met - Gly - Gly - Phe - Lys - Val - Glu - Asn - His - Thr-80 - Ala - Cys - His - Cys - Ser - Thr - Cys - Tyr - Tyr - His-90 - Lys - Ser.
1150658	3	42	dep	Asn	560:562	arg1	Thr					665:667	Thr	665:667	Thr	665:667	The amino acid sequence of the alpha subunit is: Ala - Asp - Val - Gln - Asp - Cys - Pro - Glu - Cys-10 - Thr - Leu - Gln - Asp - Pro - Phe - Ser - Gln-20 - Pro - Gly - Ala - Pro - Ile - Leu - Gln - Cys - Met - Gly-30 - Cys - Cys - Phe - Ser - Arg - Ala - Tyr - Pro - Thr - Pro-40 - Leu - Arg - Ser - Lys - Lys - Thr - Met - Leu - Val - Gln-50 - Lys - Asn - Val - Thr - Ser - Glu - Ser - Thr - Cys - Cys-60 - Val - Ala - Lys - Ser - Thr - Asn - Arg - Val - Thr - Val-70 - Met - Gly - Gly - Phe - Lys - Val - Glu - Asn - His - Thr-80 - Ala - Cys - His - Cys - Ser - Thr - Cys - Tyr - Tyr - His-90 - Lys - Ser.
1150658	3	42	dep	Asn	560:562	arg1	Met					680:682	Met	680:682	Asn - Val - Thr - Ser - Glu - Ser - Thr - Cys - Cys-60 - Val - Ala - Lys - Ser - Thr - Asn - Arg - Val - Thr - Val-70 - Met	560:682	The amino acid sequence of the alpha subunit is: Ala - Asp - Val - Gln - Asp - Cys - Pro - Glu - Cys-10 - Thr - Leu - Gln - Asp - Pro - Phe - Ser - Gln-20 - Pro - Gly - Ala - Pro - Ile - Leu - Gln - Cys - Met - Gly-30 - Cys - Cys - Phe - Ser - Arg - Ala - Tyr - Pro - Thr - Pro-40 - Leu - Arg - Ser - Lys - Lys - Thr - Met - Leu - Val - Gln-50 - Lys - Asn - Val - Thr - Ser - Glu - Ser - Thr - Cys - Cys-60 - Val - Ala - Lys - Ser - Thr - Asn - Arg - Val - Thr - Val-70 - Met - Gly - Gly - Phe - Lys - Val - Glu - Asn - His - Thr-80 - Ala - Cys - His - Cys - Ser - Thr - Cys - Tyr - Tyr - His-90 - Lys - Ser.
1150658	3	42	dep	Asn	560:562	arg1	Val-70					671:676	Val-70	671:676	Val-70	671:676	The amino acid sequence of the alpha subunit is: Ala - Asp - Val - Gln - Asp - Cys - Pro - Glu - Cys-10 - Thr - Leu - Gln - Asp - Pro - Phe - Ser - Gln-20 - Pro - Gly - Ala - Pro - Ile - Leu - Gln - Cys - Met - Gly-30 - Cys - Cys - Phe - Ser - Arg - Ala - Tyr - Pro - Thr - Pro-40 - Leu - Arg - Ser - Lys - Lys - Thr - Met - Leu - Val - Gln-50 - Lys - Asn - Val - Thr - Ser - Glu - Ser - Thr - Cys - Cys-60 - Val - Ala - Lys - Ser - Thr - Asn - Arg - Val - Thr - Val-70 - Met - Gly - Gly - Phe - Lys - Val - Glu - Asn - His - Thr-80 - Ala - Cys - His - Cys - Ser - Thr - Cys - Tyr - Tyr - His-90 - Lys - Ser.
1150658	3	42	dep	Asn	560:562	arg1	Thr					641:643	Thr	641:643	Thr	641:643	The amino acid sequence of the alpha subunit is: Ala - Asp - Val - Gln - Asp - Cys - Pro - Glu - Cys-10 - Thr - Leu - Gln - Asp - Pro - Phe - Ser - Gln-20 - Pro - Gly - Ala - Pro - Ile - Leu - Gln - Cys - Met - Gly-30 - Cys - Cys - Phe - Ser - Arg - Ala - Tyr - Pro - Thr - Pro-40 - Leu - Arg - Ser - Lys - Lys - Thr - Met - Leu - Val - Gln-50 - Lys - Asn - Val - Thr - Ser - Glu - Ser - Thr - Cys - Cys-60 - Val - Ala - Lys - Ser - Thr - Asn - Arg - Val - Thr - Val-70 - Met - Gly - Gly - Phe - Lys - Val - Glu - Asn - His - Thr-80 - Ala - Cys - His - Cys - Ser - Thr - Cys - Tyr - Tyr - His-90 - Lys - Ser.
1150658	12	43	theme	proteolytic	2224:2234	arg1	enzyme					2236:2241	The proteolytic enzyme	2220:2241	The proteolytic enzyme	2220:2241	The proteolytic enzyme, thrombin, which appears to cleave a limited number of arginyl bonds, proved helpful in the determination of the beta sequence.
1150658	12	43	theme	proteolytic	2224:2234	arg1	thrombin					2244:2251	thrombin	2244:2251	thrombin	2244:2251	The proteolytic enzyme, thrombin, which appears to cleave a limited number of arginyl bonds, proved helpful in the determination of the beta sequence.
1150658	4	44	theme	Oligosaccharide	817:831	arg1	chains					838:843	Oligosaccharide side chains	817:843	Oligosaccharide side chains	817:843	Oligosaccharide side chains are attached at residues 52 and 78.
1150658	5	45	theme	chains	941:946	arg1	%					932:932	approximately 10 and 30%	909:932	approximately 10 and 30% of the chains	909:946	In the preparations studied approximately 10 and 30% of the chains lack the initial 2 and 3 NH2-terminal residues, respectively.
1150658	5	45	theme	chains	941:946	arg1	chains					941:946	the chains	937:946	the chains	937:946	In the preparations studied approximately 10 and 30% of the chains lack the initial 2 and 3 NH2-terminal residues, respectively.
1150658	5	46	theme	NH2-terminal	973:984	arg1	residues					986:993	the initial 2 and 3 NH2-terminal residues	953:993	the initial 2 and 3 NH2-terminal residues	953:993	In the preparations studied approximately 10 and 30% of the chains lack the initial 2 and 3 NH2-terminal residues, respectively.
12297050	0	0	theme	receptor	70:77	arg1	domains					93:99	receptor extracellular domains	70:99	receptor extracellular domains	70:99	Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains.
12297050	1	1	theme	tyrosine	314:321	arg1	kinase					323:328	the receptor tyrosine kinase	301:328	the receptor tyrosine kinase	301:328	Epidermal growth factor (EGF) regulates cell proliferation and differentiation by binding to the EGF receptor (EGFR) extracellular region, comprising domains I-IV, with the resultant dimerization of the receptor tyrosine kinase.
12297050	1	2	theme	cell	142:145	arg1	proliferation					147:159	cell proliferation	142:159	cell proliferation	142:159	Epidermal growth factor (EGF) regulates cell proliferation and differentiation by binding to the EGF receptor (EGFR) extracellular region, comprising domains I-IV, with the resultant dimerization of the receptor tyrosine kinase.
12297050	1	3	theme	kinase	323:328	arg1	dimerization					285:296	the resultant dimerization	271:296	the resultant dimerization of the receptor tyrosine kinase	271:328	Epidermal growth factor (EGF) regulates cell proliferation and differentiation by binding to the EGF receptor (EGFR) extracellular region, comprising domains I-IV, with the resultant dimerization of the receptor tyrosine kinase.
12297050	0	4	theme	domains	93:99	arg1	complex					25:31	the complex	21:31	the complex of human epidermal growth factor and receptor extracellular domains	21:99	Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains.
12297050	4	5	theme	protruding	658:667	arg1	domain					694:699	each domain II	689:702	each domain II	689:702	The 1:1 EGF*EGFR complex dimerizes through a direct receptor*receptor interaction, in which a protruding beta-hairpin arm of each domain II holds the body of the other.
12297050	4	5	theme	protruding	658:667	arg1	arm					682:684	a protruding beta-hairpin arm	656:684	a protruding beta-hairpin arm of each domain II	656:702	The 1:1 EGF*EGFR complex dimerizes through a direct receptor*receptor interaction, in which a protruding beta-hairpin arm of each domain II holds the body of the other.
12297050	0	6	theme	extracellular	79:91	arg1	domains					93:99	receptor extracellular domains	70:99	receptor extracellular domains	70:99	Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains.
12297050	5	7	theme	unique	737:742	arg1	"					775:775	The unique "receptor-mediated dimerization"	733:775	The unique "receptor-mediated dimerization"	733:775	The unique "receptor-mediated dimerization" was verified by EGFR mutagenesis.
12297050	4	8	theme	receptor	616:623	arg1	interaction					634:644	a direct receptor*receptor interaction	607:644	a direct receptor*receptor interaction	607:644	The 1:1 EGF*EGFR complex dimerizes through a direct receptor*receptor interaction, in which a protruding beta-hairpin arm of each domain II holds the body of the other.
12297050	4	9	theme	other	726:730	arg1	body					714:717	the body	710:717	the body of the other	710:730	The 1:1 EGF*EGFR complex dimerizes through a direct receptor*receptor interaction, in which a protruding beta-hairpin arm of each domain II holds the body of the other.
12297050	4	10	theme	EGFR	576:579	arg1	complex					581:587	The 1:1 EGF*EGFR complex	564:587	The 1:1 EGF*EGFR complex	564:587	The 1:1 EGF*EGFR complex dimerizes through a direct receptor*receptor interaction, in which a protruding beta-hairpin arm of each domain II holds the body of the other.
12297050	4	11	theme	EGF	572:574	arg1	complex					581:587	The 1:1 EGF*EGFR complex	564:587	The 1:1 EGF*EGFR complex	564:587	The 1:1 EGF*EGFR complex dimerizes through a direct receptor*receptor interaction, in which a protruding beta-hairpin arm of each domain II holds the body of the other.
12297050	2	12	theme	EGFR	406:409	arg1	region					425:430	the EGFR extracellular region	402:430	the EGFR extracellular region	402:430	In this study, the crystal structure of a 2:2 complex of human EGF and the EGFR extracellular region has been determined at 3.3 A resolution.
12297050	4	13	theme	beta-hairpin	669:680	arg1	domain					694:699	each domain II	689:702	each domain II	689:702	The 1:1 EGF*EGFR complex dimerizes through a direct receptor*receptor interaction, in which a protruding beta-hairpin arm of each domain II holds the body of the other.
12297050	4	13	theme	beta-hairpin	669:680	arg1	arm					682:684	a protruding beta-hairpin arm	656:684	a protruding beta-hairpin arm of each domain II	656:702	The 1:1 EGF*EGFR complex dimerizes through a direct receptor*receptor interaction, in which a protruding beta-hairpin arm of each domain II holds the body of the other.
12297050	4	14	theme	1:1	568:570	arg1	complex					581:587	The 1:1 EGF*EGFR complex	564:587	The 1:1 EGF*EGFR complex	564:587	The 1:1 EGF*EGFR complex dimerizes through a direct receptor*receptor interaction, in which a protruding beta-hairpin arm of each domain II holds the body of the other.
12297050	3	15	theme	C	510:510	arg1	shape					512:516	a C shape	508:516	a C shape	508:516	EGFR domains I-III are arranged in a C shape, and EGF is docked between domains I and III.
12297050	2	16	theme	crystal	350:356	arg1	structure					358:366	the crystal structure	346:366	the crystal structure of a 2:2 complex of human EGF and the EGFR extracellular region	346:430	In this study, the crystal structure of a 2:2 complex of human EGF and the EGFR extracellular region has been determined at 3.3 A resolution.
12297050	0	17	theme	Crystal	0:6	arg1	structure					8:16	Crystal structure	0:16	Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains.	0:100	Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains.
12297050	4	18	theme	*	575:575	arg1	complex					581:587	The 1:1 EGF*EGFR complex	564:587	The 1:1 EGF*EGFR complex	564:587	The 1:1 EGF*EGFR complex dimerizes through a direct receptor*receptor interaction, in which a protruding beta-hairpin arm of each domain II holds the body of the other.
12297050	2	19	theme	EGF	394:396	arg1	region					425:430	the EGFR extracellular region	402:430	the EGFR extracellular region	402:430	In this study, the crystal structure of a 2:2 complex of human EGF and the EGFR extracellular region has been determined at 3.3 A resolution.
12297050	2	19	theme	EGF	394:396	arg1	complex					377:383	a 2:2 complex	371:383	a 2:2 complex of human EGF	371:396	In this study, the crystal structure of a 2:2 complex of human EGF and the EGFR extracellular region has been determined at 3.3 A resolution.
12297050	2	20	theme	human	388:392	arg1	EGF					394:396	human EGF	388:396	human EGF	388:396	In this study, the crystal structure of a 2:2 complex of human EGF and the EGFR extracellular region has been determined at 3.3 A resolution.
12297050	1	21	theme	Epidermal	102:110	arg1	EGF					127:129	EGF	127:129	EGF	127:129	Epidermal growth factor (EGF) regulates cell proliferation and differentiation by binding to the EGF receptor (EGFR) extracellular region, comprising domains I-IV, with the resultant dimerization of the receptor tyrosine kinase.
12297050	1	21	theme	Epidermal	102:110	arg1	factor					119:124	Epidermal growth factor	102:124	Epidermal growth factor (EGF)	102:130	Epidermal growth factor (EGF) regulates cell proliferation and differentiation by binding to the EGF receptor (EGFR) extracellular region, comprising domains I-IV, with the resultant dimerization of the receptor tyrosine kinase.
12297050	2	22	theme	extracellular	411:423	arg1	region					425:430	the EGFR extracellular region	402:430	the EGFR extracellular region	402:430	In this study, the crystal structure of a 2:2 complex of human EGF and the EGFR extracellular region has been determined at 3.3 A resolution.
12297050	2	23	theme	complex	377:383	arg1	structure					358:366	the crystal structure	346:366	the crystal structure of a 2:2 complex of human EGF and the EGFR extracellular region	346:430	In this study, the crystal structure of a 2:2 complex of human EGF and the EGFR extracellular region has been determined at 3.3 A resolution.
12297050	2	24	theme	2:2	373:375	arg1	complex					377:383	a 2:2 complex	371:383	a 2:2 complex of human EGF	371:396	In this study, the crystal structure of a 2:2 complex of human EGF and the EGFR extracellular region has been determined at 3.3 A resolution.
12297050	5	25	theme	dimerization	763:774	arg1	"					775:775	The unique "receptor-mediated dimerization"	733:775	The unique "receptor-mediated dimerization"	733:775	The unique "receptor-mediated dimerization" was verified by EGFR mutagenesis.
12297050	1	26	theme	EGF	199:201	arg1	EGFR					213:216	EGFR	213:216	EGFR	213:216	Epidermal growth factor (EGF) regulates cell proliferation and differentiation by binding to the EGF receptor (EGFR) extracellular region, comprising domains I-IV, with the resultant dimerization of the receptor tyrosine kinase.
12297050	1	26	theme	EGF	199:201	arg1	receptor					203:210	EGF receptor	199:210	the EGF receptor (EGFR) extracellular region	195:238	Epidermal growth factor (EGF) regulates cell proliferation and differentiation by binding to the EGF receptor (EGFR) extracellular region, comprising domains I-IV, with the resultant dimerization of the receptor tyrosine kinase.
12297050	0	27	theme	complex	25:31	arg1	structure					8:16	Crystal structure	0:16	Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains.	0:100	Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains.
12297050	1	28	theme	resultant	275:283	arg1	dimerization					285:296	the resultant dimerization	271:296	the resultant dimerization of the receptor tyrosine kinase	271:328	Epidermal growth factor (EGF) regulates cell proliferation and differentiation by binding to the EGF receptor (EGFR) extracellular region, comprising domains I-IV, with the resultant dimerization of the receptor tyrosine kinase.
12297050	2	29	theme	region	425:430	arg1	structure					358:366	the crystal structure	346:366	the crystal structure of a 2:2 complex of human EGF and the EGFR extracellular region	346:430	In this study, the crystal structure of a 2:2 complex of human EGF and the EGFR extracellular region has been determined at 3.3 A resolution.
12297050	1	30	theme	receptor	203:210	arg1	region					233:238	the EGF receptor (EGFR) extracellular region	195:238	the EGF receptor (EGFR) extracellular region	195:238	Epidermal growth factor (EGF) regulates cell proliferation and differentiation by binding to the EGF receptor (EGFR) extracellular region, comprising domains I-IV, with the resultant dimerization of the receptor tyrosine kinase.
12297050	0	31	theme	epidermal	42:50	arg1	factor					59:64	human epidermal growth factor	36:64	human epidermal growth factor	36:64	Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains.
12297050	5	32	theme	receptor-mediated	745:761	arg1	"					775:775	The unique "receptor-mediated dimerization"	733:775	The unique "receptor-mediated dimerization"	733:775	The unique "receptor-mediated dimerization" was verified by EGFR mutagenesis.
12297050	1	33	theme	growth	112:117	arg1	EGF					127:129	EGF	127:129	EGF	127:129	Epidermal growth factor (EGF) regulates cell proliferation and differentiation by binding to the EGF receptor (EGFR) extracellular region, comprising domains I-IV, with the resultant dimerization of the receptor tyrosine kinase.
12297050	1	33	theme	growth	112:117	arg1	factor					119:124	Epidermal growth factor	102:124	Epidermal growth factor (EGF)	102:130	Epidermal growth factor (EGF) regulates cell proliferation and differentiation by binding to the EGF receptor (EGFR) extracellular region, comprising domains I-IV, with the resultant dimerization of the receptor tyrosine kinase.
12297050	0	34	theme	human	36:40	arg1	factor					59:64	human epidermal growth factor	36:64	human epidermal growth factor	36:64	Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains.
12297050	4	35	theme	direct	609:614	arg1	interaction					634:644	a direct receptor*receptor interaction	607:644	a direct receptor*receptor interaction	607:644	The 1:1 EGF*EGFR complex dimerizes through a direct receptor*receptor interaction, in which a protruding beta-hairpin arm of each domain II holds the body of the other.
12297050	1	36	dep	domains	252:258	arg1	I-IV					260:263	I-IV	260:263	domains I-IV	252:263	Epidermal growth factor (EGF) regulates cell proliferation and differentiation by binding to the EGF receptor (EGFR) extracellular region, comprising domains I-IV, with the resultant dimerization of the receptor tyrosine kinase.
12297050	4	37	theme	each	689:692	arg1	domain					694:699	each domain II	689:702	each domain II	689:702	The 1:1 EGF*EGFR complex dimerizes through a direct receptor*receptor interaction, in which a protruding beta-hairpin arm of each domain II holds the body of the other.
12297050	4	38	theme	receptor	625:632	arg1	interaction					634:644	a direct receptor*receptor interaction	607:644	a direct receptor*receptor interaction	607:644	The 1:1 EGF*EGFR complex dimerizes through a direct receptor*receptor interaction, in which a protruding beta-hairpin arm of each domain II holds the body of the other.
12297050	5	39	theme	EGFR	793:796	arg1	mutagenesis					798:808	EGFR mutagenesis	793:808	EGFR mutagenesis	793:808	The unique "receptor-mediated dimerization" was verified by EGFR mutagenesis.
12297050	4	40	theme	*	624:624	arg1	interaction					634:644	a direct receptor*receptor interaction	607:644	a direct receptor*receptor interaction	607:644	The 1:1 EGF*EGFR complex dimerizes through a direct receptor*receptor interaction, in which a protruding beta-hairpin arm of each domain II holds the body of the other.
12297050	0	41	theme	factor	59:64	arg1	complex					25:31	the complex	21:31	the complex of human epidermal growth factor and receptor extracellular domains	21:99	Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains.
12297050	0	42	theme	growth	52:57	arg1	factor					59:64	human epidermal growth factor	36:64	human epidermal growth factor	36:64	Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains.
12297050	1	43	theme	receptor	305:312	arg1	kinase					323:328	the receptor tyrosine kinase	301:328	the receptor tyrosine kinase	301:328	Epidermal growth factor (EGF) regulates cell proliferation and differentiation by binding to the EGF receptor (EGFR) extracellular region, comprising domains I-IV, with the resultant dimerization of the receptor tyrosine kinase.
12297050	4	44	theme	domain	694:699	arg1	domain					694:699	each domain II	689:702	each domain II	689:702	The 1:1 EGF*EGFR complex dimerizes through a direct receptor*receptor interaction, in which a protruding beta-hairpin arm of each domain II holds the body of the other.
12297050	4	44	theme	domain	694:699	arg1	arm					682:684	a protruding beta-hairpin arm	656:684	a protruding beta-hairpin arm of each domain II	656:702	The 1:1 EGF*EGFR complex dimerizes through a direct receptor*receptor interaction, in which a protruding beta-hairpin arm of each domain II holds the body of the other.
12297050	3	45	theme	EGFR	473:476	arg1	domains					478:484	EGFR domains I-III	473:490	EGFR domains I-III	473:490	EGFR domains I-III are arranged in a C shape, and EGF is docked between domains I and III.
12297050	1	46	theme	extracellular	219:231	arg1	region					233:238	the EGF receptor (EGFR) extracellular region	195:238	the EGF receptor (EGFR) extracellular region	195:238	Epidermal growth factor (EGF) regulates cell proliferation and differentiation by binding to the EGF receptor (EGFR) extracellular region, comprising domains I-IV, with the resultant dimerization of the receptor tyrosine kinase.
12297049	6	0	theme	surface	828:834	arg1	area					836:839	buried surface area	821:839	buried surface area	821:839	Based on sequence conservation, buried surface area, and mutagenesis experiments, the back-to-back dimer is favored to be biologically relevant.
12297049	2	1	theme	chain	313:317	arg1	contacts					319:326	many main chain contacts	303:326	many main chain contacts with L1	303:334	TGFalpha interacts with both L1 and L2 domains of EGFR, making many main chain contacts with L1 and interacting with L2 via key conserved residues.
12297049	0	2	theme	domain	80:85	arg1	structure					8:16	Crystal structure	0:16	Crystal structure of a truncated epidermal growth factor receptor extracellular domain	0:85	Crystal structure of a truncated epidermal growth factor receptor extracellular domain bound to transforming growth factor alpha.
12297049	6	3	theme	buried	821:826	arg1	area					836:839	buried surface area	821:839	buried surface area	821:839	Based on sequence conservation, buried surface area, and mutagenesis experiments, the back-to-back dimer is favored to be biologically relevant.
12297049	2	4	theme	main	308:311	arg1	contacts					319:326	many main chain contacts	303:326	many main chain contacts with L1	303:334	TGFalpha interacts with both L1 and L2 domains of EGFR, making many main chain contacts with L1 and interacting with L2 via key conserved residues.
12297049	0	5	theme	transforming	96:107	arg1	factor					116:121	transforming growth factor	96:121	transforming growth factor alpha	96:127	Crystal structure of a truncated epidermal growth factor receptor extracellular domain bound to transforming growth factor alpha.
12297049	2	6	theme	L1	269:270	arg1	EGFR					290:293	EGFR	290:293	EGFR	290:293	TGFalpha interacts with both L1 and L2 domains of EGFR, making many main chain contacts with L1 and interacting with L2 via key conserved residues.
12297049	2	6	theme	L1	269:270	arg1	domains					279:285	both L1 and L2 domains	264:285	both L1 and L2 domains of EGFR	264:293	TGFalpha interacts with both L1 and L2 domains of EGFR, making many main chain contacts with L1 and interacting with L2 via key conserved residues.
12297049	5	7	from	unit	620:623	arg1	types					586:590	two types	582:590	two types of dimers in the asymmetric unit: a head-to-head dimer involving contacts between the L1 and L2 domains and a back-to-back dimer dominated by interactions between the CR1 domains of each receptor	582:786	There are two types of dimers in the asymmetric unit: a head-to-head dimer involving contacts between the L1 and L2 domains and a back-to-back dimer dominated by interactions between the CR1 domains of each receptor.
12297049	6	8	theme	back-to-back	875:886	arg1	relevant					924:931	relevant	924:931	relevant	924:931	Based on sequence conservation, buried surface area, and mutagenesis experiments, the back-to-back dimer is favored to be biologically relevant.
12297049	6	8	theme	back-to-back	875:886	arg1	dimer					888:892	the back-to-back dimer	871:892	the back-to-back dimer	871:892	Based on sequence conservation, buried surface area, and mutagenesis experiments, the back-to-back dimer is favored to be biologically relevant.
12297049	4	9	theme	receptor	553:560	arg1	molecule					562:569	only one receptor molecule	544:569	only one receptor molecule	544:569	In the 2:2 TGFalpha:sEGFR501 complex, each ligand interacts with only one receptor molecule.
12297049	0	10	theme	factor	116:121	arg1	alpha					123:127	transforming growth factor alpha	96:127	transforming growth factor alpha	96:127	Crystal structure of a truncated epidermal growth factor receptor extracellular domain bound to transforming growth factor alpha.
12297049	6	11	theme	sequence	798:805	arg1	conservation					807:818	sequence conservation	798:818	sequence conservation	798:818	Based on sequence conservation, buried surface area, and mutagenesis experiments, the back-to-back dimer is favored to be biologically relevant.
12297049	3	12	theme	family	418:423	arg1	members					425:431	EGFR family members	413:431	EGFR family members	413:431	The results indicate how EGFR family members can bind a family of highly variable ligands.
12297049	3	13	theme	ligands	470:476	arg1	family					444:449	a family	442:449	a family of highly variable ligands	442:476	The results indicate how EGFR family members can bind a family of highly variable ligands.
12297049	5	14	theme	receptor	779:786	arg1	domains					763:769	the CR1 domains	755:769	the CR1 domains of each receptor	755:786	There are two types of dimers in the asymmetric unit: a head-to-head dimer involving contacts between the L1 and L2 domains and a back-to-back dimer dominated by interactions between the CR1 domains of each receptor.
12297049	5	14	theme	receptor	779:786	arg1	receptor					779:786	each receptor	774:786	each receptor	774:786	There are two types of dimers in the asymmetric unit: a head-to-head dimer involving contacts between the L1 and L2 domains and a back-to-back dimer dominated by interactions between the CR1 domains of each receptor.
12297049	0	15	theme	growth	109:114	arg1	factor					116:121	transforming growth factor	96:121	transforming growth factor alpha	96:127	Crystal structure of a truncated epidermal growth factor receptor extracellular domain bound to transforming growth factor alpha.
12297049	5	16	dep	types	586:590	arg1	dimer					641:645	a head-to-head dimer	626:645	two types of dimers in the asymmetric unit: a head-to-head dimer involving contacts between the L1 and L2 domains and a back-to-back dimer dominated by interactions between the CR1 domains of each receptor	582:786	There are two types of dimers in the asymmetric unit: a head-to-head dimer involving contacts between the L1 and L2 domains and a back-to-back dimer dominated by interactions between the CR1 domains of each receptor.
12297049	3	17	theme	variable	461:468	arg1	ligands					470:476	highly variable ligands	454:476	highly variable ligands	454:476	The results indicate how EGFR family members can bind a family of highly variable ligands.
12297049	1	18	theme	A	170:170	arg1	resolution					172:181	2.5 A resolution	166:181	2.5 A resolution	166:181	We report the crystal structure, at 2.5 A resolution, of a truncated human EGFR ectodomain bound to TGFalpha.
12297049	0	19	theme	Crystal	0:6	arg1	structure					8:16	Crystal structure	0:16	Crystal structure of a truncated epidermal growth factor receptor extracellular domain	0:85	Crystal structure of a truncated epidermal growth factor receptor extracellular domain bound to transforming growth factor alpha.
12297049	4	20	theme	TGFalpha	490:497	arg1	complex					508:514	the 2:2 TGFalpha:sEGFR501 complex	482:514	the 2:2 TGFalpha:sEGFR501 complex	482:514	In the 2:2 TGFalpha:sEGFR501 complex, each ligand interacts with only one receptor molecule.
12297049	4	21	theme	2:2	486:488	arg1	complex					508:514	the 2:2 TGFalpha:sEGFR501 complex	482:514	the 2:2 TGFalpha:sEGFR501 complex	482:514	In the 2:2 TGFalpha:sEGFR501 complex, each ligand interacts with only one receptor molecule.
12297049	2	22	theme	L2	276:277	arg1	EGFR					290:293	EGFR	290:293	EGFR	290:293	TGFalpha interacts with both L1 and L2 domains of EGFR, making many main chain contacts with L1 and interacting with L2 via key conserved residues.
12297049	2	22	theme	L2	276:277	arg1	domains					279:285	both L1 and L2 domains	264:285	both L1 and L2 domains of EGFR	264:293	TGFalpha interacts with both L1 and L2 domains of EGFR, making many main chain contacts with L1 and interacting with L2 via key conserved residues.
12297049	2	23	theme	conserved	368:376	arg1	residues					378:385	key conserved residues	364:385	key conserved residues	364:385	TGFalpha interacts with both L1 and L2 domains of EGFR, making many main chain contacts with L1 and interacting with L2 via key conserved residues.
12297049	3	24	theme	EGFR	413:416	arg1	members					425:431	EGFR family members	413:431	EGFR family members	413:431	The results indicate how EGFR family members can bind a family of highly variable ligands.
12297049	4	25	theme	sEGFR501	499:506	arg1	complex					508:514	the 2:2 TGFalpha:sEGFR501 complex	482:514	the 2:2 TGFalpha:sEGFR501 complex	482:514	In the 2:2 TGFalpha:sEGFR501 complex, each ligand interacts with only one receptor molecule.
12297049	5	26	theme	back-to-back	702:713	arg1	dimer					715:719	a back-to-back dimer	700:719	a back-to-back dimer dominated by interactions between the CR1 domains of each receptor	700:786	There are two types of dimers in the asymmetric unit: a head-to-head dimer involving contacts between the L1 and L2 domains and a back-to-back dimer dominated by interactions between the CR1 domains of each receptor.
12297049	2	27	theme	key	364:366	arg1	residues					378:385	key conserved residues	364:385	key conserved residues	364:385	TGFalpha interacts with both L1 and L2 domains of EGFR, making many main chain contacts with L1 and interacting with L2 via key conserved residues.
12297049	0	28	theme	epidermal	33:41	arg1	receptor					57:64	a truncated epidermal growth factor receptor	21:64	a truncated epidermal growth factor receptor extracellular domain	21:85	Crystal structure of a truncated epidermal growth factor receptor extracellular domain bound to transforming growth factor alpha.
12297049	5	29	theme	head-to-head	628:639	arg1	dimer					641:645	a head-to-head dimer	626:645	two types of dimers in the asymmetric unit: a head-to-head dimer involving contacts between the L1 and L2 domains and a back-to-back dimer dominated by interactions between the CR1 domains of each receptor	582:786	There are two types of dimers in the asymmetric unit: a head-to-head dimer involving contacts between the L1 and L2 domains and a back-to-back dimer dominated by interactions between the CR1 domains of each receptor.
12297049	5	30	theme	CR1	759:761	arg1	domains					763:769	the CR1 domains	755:769	the CR1 domains of each receptor	755:786	There are two types of dimers in the asymmetric unit: a head-to-head dimer involving contacts between the L1 and L2 domains and a back-to-back dimer dominated by interactions between the CR1 domains of each receptor.
12297049	5	30	theme	CR1	759:761	arg1	receptor					779:786	each receptor	774:786	each receptor	774:786	There are two types of dimers in the asymmetric unit: a head-to-head dimer involving contacts between the L1 and L2 domains and a back-to-back dimer dominated by interactions between the CR1 domains of each receptor.
12297049	0	31	theme	truncated	23:31	arg1	receptor					57:64	a truncated epidermal growth factor receptor	21:64	a truncated epidermal growth factor receptor extracellular domain	21:85	Crystal structure of a truncated epidermal growth factor receptor extracellular domain bound to transforming growth factor alpha.
12297049	5	32	from	types	586:590	arg1	unit					620:623	the asymmetric unit	605:623	the asymmetric unit	605:623	There are two types of dimers in the asymmetric unit: a head-to-head dimer involving contacts between the L1 and L2 domains and a back-to-back dimer dominated by interactions between the CR1 domains of each receptor.
12297049	5	33	theme	L2	685:686	arg1	domains					688:694	the L1 and L2 domains	674:694	the L1 and L2 domains	674:694	There are two types of dimers in the asymmetric unit: a head-to-head dimer involving contacts between the L1 and L2 domains and a back-to-back dimer dominated by interactions between the CR1 domains of each receptor.
12297049	5	34	from	dimers	595:600	arg1	unit					620:623	the asymmetric unit	605:623	the asymmetric unit	605:623	There are two types of dimers in the asymmetric unit: a head-to-head dimer involving contacts between the L1 and L2 domains and a back-to-back dimer dominated by interactions between the CR1 domains of each receptor.
12297049	1	35	theme	truncated	189:197	arg1	ectodomain					210:219	a truncated human EGFR ectodomain	187:219	a truncated human EGFR ectodomain bound to TGFalpha	187:237	We report the crystal structure, at 2.5 A resolution, of a truncated human EGFR ectodomain bound to TGFalpha.
12297049	0	36	theme	factor	50:55	arg1	receptor					57:64	a truncated epidermal growth factor receptor	21:64	a truncated epidermal growth factor receptor extracellular domain	21:85	Crystal structure of a truncated epidermal growth factor receptor extracellular domain bound to transforming growth factor alpha.
12297049	6	37	theme	mutagenesis	846:856	arg1	experiments					858:868	mutagenesis experiments	846:868	mutagenesis experiments	846:868	Based on sequence conservation, buried surface area, and mutagenesis experiments, the back-to-back dimer is favored to be biologically relevant.
12297049	5	38	theme	dimers	595:600	arg1	types					586:590	two types	582:590	two types of dimers in the asymmetric unit: a head-to-head dimer involving contacts between the L1 and L2 domains and a back-to-back dimer dominated by interactions between the CR1 domains of each receptor	582:786	There are two types of dimers in the asymmetric unit: a head-to-head dimer involving contacts between the L1 and L2 domains and a back-to-back dimer dominated by interactions between the CR1 domains of each receptor.
12297049	5	39	theme	L1	678:679	arg1	domains					688:694	the L1 and L2 domains	674:694	the L1 and L2 domains	674:694	There are two types of dimers in the asymmetric unit: a head-to-head dimer involving contacts between the L1 and L2 domains and a back-to-back dimer dominated by interactions between the CR1 domains of each receptor.
12297049	2	40	theme	many	303:306	arg1	contacts					319:326	many main chain contacts	303:326	many main chain contacts with L1	303:334	TGFalpha interacts with both L1 and L2 domains of EGFR, making many main chain contacts with L1 and interacting with L2 via key conserved residues.
12297049	0	41	theme	growth	43:48	arg1	receptor					57:64	a truncated epidermal growth factor receptor	21:64	a truncated epidermal growth factor receptor extracellular domain	21:85	Crystal structure of a truncated epidermal growth factor receptor extracellular domain bound to transforming growth factor alpha.
12297049	5	42	dep	L1	678:679	arg1	the					674:676	the	674:676	the	674:676	There are two types of dimers in the asymmetric unit: a head-to-head dimer involving contacts between the L1 and L2 domains and a back-to-back dimer dominated by interactions between the CR1 domains of each receptor.
12297049	1	43	theme	human	199:203	arg1	ectodomain					210:219	a truncated human EGFR ectodomain	187:219	a truncated human EGFR ectodomain bound to TGFalpha	187:237	We report the crystal structure, at 2.5 A resolution, of a truncated human EGFR ectodomain bound to TGFalpha.
12297049	5	44	theme	asymmetric	609:618	arg1	unit					620:623	the asymmetric unit	605:623	the asymmetric unit	605:623	There are two types of dimers in the asymmetric unit: a head-to-head dimer involving contacts between the L1 and L2 domains and a back-to-back dimer dominated by interactions between the CR1 domains of each receptor.
12297049	2	45	theme	EGFR	290:293	arg1	EGFR					290:293	EGFR	290:293	EGFR	290:293	TGFalpha interacts with both L1 and L2 domains of EGFR, making many main chain contacts with L1 and interacting with L2 via key conserved residues.
12297049	2	45	theme	EGFR	290:293	arg1	domains					279:285	both L1 and L2 domains	264:285	both L1 and L2 domains of EGFR	264:293	TGFalpha interacts with both L1 and L2 domains of EGFR, making many main chain contacts with L1 and interacting with L2 via key conserved residues.
12297049	1	46	theme	EGFR	205:208	arg1	ectodomain					210:219	a truncated human EGFR ectodomain	187:219	a truncated human EGFR ectodomain bound to TGFalpha	187:237	We report the crystal structure, at 2.5 A resolution, of a truncated human EGFR ectodomain bound to TGFalpha.
12297049	0	47	theme	extracellular	66:78	arg1	domain					80:85	a truncated epidermal growth factor receptor extracellular domain	21:85	a truncated epidermal growth factor receptor extracellular domain	21:85	Crystal structure of a truncated epidermal growth factor receptor extracellular domain bound to transforming growth factor alpha.
12297049	2	48	with	contacts	319:326	arg1	L1					333:334	L1	333:334	L1	333:334	TGFalpha interacts with both L1 and L2 domains of EGFR, making many main chain contacts with L1 and interacting with L2 via key conserved residues.
12297049	1	49	from	resolution	172:181	arg1	structure					152:160	the crystal structure	140:160	the crystal structure	140:160	We report the crystal structure, at 2.5 A resolution, of a truncated human EGFR ectodomain bound to TGFalpha.
12297049	1	50	theme	ectodomain	210:219	arg1	structure					152:160	the crystal structure	140:160	the crystal structure	140:160	We report the crystal structure, at 2.5 A resolution, of a truncated human EGFR ectodomain bound to TGFalpha.
12297049	0	51	theme	receptor	57:64	arg1	domain					80:85	a truncated epidermal growth factor receptor extracellular domain	21:85	a truncated epidermal growth factor receptor extracellular domain	21:85	Crystal structure of a truncated epidermal growth factor receptor extracellular domain bound to transforming growth factor alpha.
12297049	1	52	theme	crystal	144:150	arg1	structure					152:160	the crystal structure	140:160	the crystal structure	140:160	We report the crystal structure, at 2.5 A resolution, of a truncated human EGFR ectodomain bound to TGFalpha.
11546839	5	0	theme	striking	722:729	arg1	resemblance					731:741	a striking resemblance	720:741	a striking resemblance to the Galpha/Gbeta interface in G proteins	720:785	The main inter-subunit interface lies within the head, between a seven-bladed beta-propeller from alphaV and an A domain from beta3, and bears a striking resemblance to the Galpha/Gbeta interface in G proteins.
11546839	5	1	from	interface	763:771	arg1	proteins					778:785	G proteins	776:785	G proteins	776:785	The main inter-subunit interface lies within the head, between a seven-bladed beta-propeller from alphaV and an A domain from beta3, and bears a striking resemblance to the Galpha/Gbeta interface in G proteins.
11546839	1	2	theme	cell-matrix	174:184	arg1	adhesion					186:193	divalent cation-dependent cell-cell and cell-matrix adhesion	134:193	divalent cation-dependent cell-cell and cell-matrix adhesion	134:193	Integrins are alphabeta heterodimeric receptors that mediate divalent cation-dependent cell-cell and cell-matrix adhesion through tightly regulated interactions with ligands.
11546839	4	3	from	crystal	428:434	arg1	bent					461:464	bent	461:464	bent	461:464	In the crystal, alphaVbeta3 is severely bent at a defined region in its tails, reflecting an unusual flexibility that may be linked to integrin regulation.
11546839	6	4	theme	betaA	950:954	arg1	domains					956:962	the propeller and betaA domains	932:962	domains	956:962	A metal ion-dependent adhesion site (MIDAS) in the betaA domain is positioned to participate in a ligand-binding interface formed of loops from the propeller and betaA domains.
11546839	5	5	theme	Galpha/Gbeta	750:761	arg1	interface					763:771	the Galpha/Gbeta interface	746:771	the Galpha/Gbeta interface in G proteins	746:785	The main inter-subunit interface lies within the head, between a seven-bladed beta-propeller from alphaV and an A domain from beta3, and bears a striking resemblance to the Galpha/Gbeta interface in G proteins.
11546839	5	6	contain	bears	714:718	arg2	resemblance					731:741	a striking resemblance	720:741	a striking resemblance to the Galpha/Gbeta interface in G proteins	720:785	The main inter-subunit interface lies within the head, between a seven-bladed beta-propeller from alphaV and an A domain from beta3, and bears a striking resemblance to the Galpha/Gbeta interface in G proteins.
11546839	5	6	contain	bears	714:718	arg1	interface					600:608	The main inter-subunit interface	577:608	The main inter-subunit interface	577:608	The main inter-subunit interface lies within the head, between a seven-bladed beta-propeller from alphaV and an A domain from beta3, and bears a striking resemblance to the Galpha/Gbeta interface in G proteins.
11546839	2	7	theme	alphaVbeta3	326:336	arg1	portion					306:312	the extracellular portion	288:312	the extracellular portion of integrin alphaVbeta3	288:336	We have solved the crystal structure of the extracellular portion of integrin alphaVbeta3 at 3.1 A resolution.
11546839	6	8	theme	propeller	936:944	arg1	domains					956:962	the propeller and betaA domains	932:962	domains	956:962	A metal ion-dependent adhesion site (MIDAS) in the betaA domain is positioned to participate in a ligand-binding interface formed of loops from the propeller and betaA domains.
11546839	3	9	theme	ovoid	391:395	arg1	"					402:402	an ovoid "head"	388:402	an ovoid "head"	388:402	Its 12 domains assemble into an ovoid "head" and two "tails."
11546839	4	10	from	region	479:484	arg1	bent					461:464	bent	461:464	bent	461:464	In the crystal, alphaVbeta3 is severely bent at a defined region in its tails, reflecting an unusual flexibility that may be linked to integrin regulation.
11546839	4	10	from	region	479:484	arg1	tails					493:497	its tails	489:497	its tails	489:497	In the crystal, alphaVbeta3 is severely bent at a defined region in its tails, reflecting an unusual flexibility that may be linked to integrin regulation.
11546839	5	11	theme	main	581:584	arg1	interface					600:608	The main inter-subunit interface	577:608	The main inter-subunit interface	577:608	The main inter-subunit interface lies within the head, between a seven-bladed beta-propeller from alphaV and an A domain from beta3, and bears a striking resemblance to the Galpha/Gbeta interface in G proteins.
11546839	2	12	theme	integrin	317:324	arg1	alphaVbeta3					326:336	integrin alphaVbeta3	317:336	integrin alphaVbeta3	317:336	We have solved the crystal structure of the extracellular portion of integrin alphaVbeta3 at 3.1 A resolution.
11546839	4	13	theme	integrin	556:563	arg1	regulation					565:574	integrin regulation	556:574	integrin regulation	556:574	In the crystal, alphaVbeta3 is severely bent at a defined region in its tails, reflecting an unusual flexibility that may be linked to integrin regulation.
11546839	6	14	theme	betaA	839:843	arg1	domain					845:850	the betaA domain	835:850	the betaA domain	835:850	A metal ion-dependent adhesion site (MIDAS) in the betaA domain is positioned to participate in a ligand-binding interface formed of loops from the propeller and betaA domains.
11546839	5	15	theme	inter-subunit	586:598	arg1	interface					600:608	The main inter-subunit interface	577:608	The main inter-subunit interface	577:608	The main inter-subunit interface lies within the head, between a seven-bladed beta-propeller from alphaV and an A domain from beta3, and bears a striking resemblance to the Galpha/Gbeta interface in G proteins.
11546839	4	16	theme	defined	471:477	arg1	region					479:484	a defined region	469:484	a defined region in its tails	469:497	In the crystal, alphaVbeta3 is severely bent at a defined region in its tails, reflecting an unusual flexibility that may be linked to integrin regulation.
11546839	2	17	theme	portion	306:312	arg1	structure					275:283	the crystal structure	263:283	the crystal structure of the extracellular portion of integrin alphaVbeta3	263:336	We have solved the crystal structure of the extracellular portion of integrin alphaVbeta3 at 3.1 A resolution.
11546839	7	18	theme	regulatory	1028:1037	arg1	function					1039:1046	a potential regulatory function	1016:1046	a potential regulatory function	1016:1046	MIDAS lies adjacent to a calcium-binding site with a potential regulatory function.
11546839	2	19	theme	A	345:345	arg1	resolution					347:356	3.1 A resolution	341:356	3.1 A resolution	341:356	We have solved the crystal structure of the extracellular portion of integrin alphaVbeta3 at 3.1 A resolution.
11546839	7	20	theme	calcium-binding	990:1004	arg1	site					1006:1009	a calcium-binding site	988:1009	a calcium-binding site with a potential regulatory function	988:1046	MIDAS lies adjacent to a calcium-binding site with a potential regulatory function.
11546839	1	21	theme	regulated	211:219	arg1	interactions					221:232	tightly regulated interactions	203:232	tightly regulated interactions with ligands	203:245	Integrins are alphabeta heterodimeric receptors that mediate divalent cation-dependent cell-cell and cell-matrix adhesion through tightly regulated interactions with ligands.
11546839	0	22	theme	Crystal	0:6	arg1	structure					8:16	Crystal structure	0:16	Crystal structure of the extracellular segment of integrin alpha	0:63	Crystal structure of the extracellular segment of integrin alpha Vbeta3.
11546839	4	23	from	bent	461:464	arg1	crystal					428:434	the crystal	424:434	the crystal	424:434	In the crystal, alphaVbeta3 is severely bent at a defined region in its tails, reflecting an unusual flexibility that may be linked to integrin regulation.
11546839	1	24	theme	alphabeta	87:95	arg1	Integrins					73:81	Integrins	73:81	Integrins	73:81	Integrins are alphabeta heterodimeric receptors that mediate divalent cation-dependent cell-cell and cell-matrix adhesion through tightly regulated interactions with ligands.
11546839	1	24	theme	alphabeta	87:95	arg1	receptors					111:119	alphabeta heterodimeric receptors	87:119	alphabeta heterodimeric receptors that mediate divalent cation-dependent cell-cell and cell-matrix adhesion through tightly regulated interactions with ligands	87:245	Integrins are alphabeta heterodimeric receptors that mediate divalent cation-dependent cell-cell and cell-matrix adhesion through tightly regulated interactions with ligands.
11546839	5	25	theme	G	776:776	arg1	proteins					778:785	G proteins	776:785	G proteins	776:785	The main inter-subunit interface lies within the head, between a seven-bladed beta-propeller from alphaV and an A domain from beta3, and bears a striking resemblance to the Galpha/Gbeta interface in G proteins.
11546839	1	26	theme	heterodimeric	97:109	arg1	Integrins					73:81	Integrins	73:81	Integrins	73:81	Integrins are alphabeta heterodimeric receptors that mediate divalent cation-dependent cell-cell and cell-matrix adhesion through tightly regulated interactions with ligands.
11546839	1	26	theme	heterodimeric	97:109	arg1	receptors					111:119	alphabeta heterodimeric receptors	87:119	alphabeta heterodimeric receptors that mediate divalent cation-dependent cell-cell and cell-matrix adhesion through tightly regulated interactions with ligands	87:245	Integrins are alphabeta heterodimeric receptors that mediate divalent cation-dependent cell-cell and cell-matrix adhesion through tightly regulated interactions with ligands.
11546839	7	27	with	site	1006:1009	arg1	function					1039:1046	a potential regulatory function	1016:1046	a potential regulatory function	1016:1046	MIDAS lies adjacent to a calcium-binding site with a potential regulatory function.
11546839	3	28	theme	head	398:401	arg1	"					402:402	an ovoid "head"	388:402	an ovoid "head"	388:402	Its 12 domains assemble into an ovoid "head" and two "tails."
11546839	7	29	theme	potential	1018:1026	arg1	function					1039:1046	a potential regulatory function	1016:1046	a potential regulatory function	1016:1046	MIDAS lies adjacent to a calcium-binding site with a potential regulatory function.
11546839	6	30	from	site	819:822	arg1	domain					845:850	the betaA domain	835:850	the betaA domain	835:850	A metal ion-dependent adhesion site (MIDAS) in the betaA domain is positioned to participate in a ligand-binding interface formed of loops from the propeller and betaA domains.
11546839	0	31	theme	segment	39:45	arg1	structure					8:16	Crystal structure	0:16	Crystal structure of the extracellular segment of integrin alpha	0:63	Crystal structure of the extracellular segment of integrin alpha Vbeta3.
11546839	5	32	theme	A	689:689	arg1	domain					691:696	an A domain	686:696	an A domain from beta3	686:707	The main inter-subunit interface lies within the head, between a seven-bladed beta-propeller from alphaV and an A domain from beta3, and bears a striking resemblance to the Galpha/Gbeta interface in G proteins.
11546839	2	33	theme	crystal	267:273	arg1	structure					275:283	the crystal structure	263:283	the crystal structure of the extracellular portion of integrin alphaVbeta3	263:336	We have solved the crystal structure of the extracellular portion of integrin alphaVbeta3 at 3.1 A resolution.
11546839	0	34	theme	extracellular	25:37	arg1	segment					39:45	the extracellular segment	21:45	the extracellular segment of integrin alpha	21:63	Crystal structure of the extracellular segment of integrin alpha Vbeta3.
11546839	0	35	theme	integrin	50:57	arg1	alpha					59:63	integrin alpha	50:63	integrin alpha	50:63	Crystal structure of the extracellular segment of integrin alpha Vbeta3.
11546839	6	36	theme	ligand-binding	886:899	arg1	interface					901:909	a ligand-binding interface	884:909	a ligand-binding interface formed of loops from the propeller and betaA domains	884:962	A metal ion-dependent adhesion site (MIDAS) in the betaA domain is positioned to participate in a ligand-binding interface formed of loops from the propeller and betaA domains.
11546839	3	37	dep	assemble	374:381	arg1	"					419:419	"	419:419	"	419:419	Its 12 domains assemble into an ovoid "head" and two "tails."
11546839	5	38	from	beta3	703:707	arg1	beta-propeller					655:668	a seven-bladed beta-propeller	640:668	a seven-bladed beta-propeller from alphaV	640:680	The main inter-subunit interface lies within the head, between a seven-bladed beta-propeller from alphaV and an A domain from beta3, and bears a striking resemblance to the Galpha/Gbeta interface in G proteins.
11546839	5	38	from	beta3	703:707	arg1	domain					691:696	an A domain	686:696	an A domain from beta3	686:707	The main inter-subunit interface lies within the head, between a seven-bladed beta-propeller from alphaV and an A domain from beta3, and bears a striking resemblance to the Galpha/Gbeta interface in G proteins.
11546839	4	39	theme	unusual	514:520	arg1	flexibility					522:532	an unusual flexibility	511:532	an unusual flexibility that may be linked to integrin regulation	511:574	In the crystal, alphaVbeta3 is severely bent at a defined region in its tails, reflecting an unusual flexibility that may be linked to integrin regulation.
11546839	1	40	with	interactions	221:232	arg1	ligands					239:245	ligands	239:245	ligands	239:245	Integrins are alphabeta heterodimeric receptors that mediate divalent cation-dependent cell-cell and cell-matrix adhesion through tightly regulated interactions with ligands.
11546839	6	41	theme	adhesion	810:817	arg1	MIDAS					825:829	MIDAS	825:829	MIDAS	825:829	A metal ion-dependent adhesion site (MIDAS) in the betaA domain is positioned to participate in a ligand-binding interface formed of loops from the propeller and betaA domains.
11546839	6	41	theme	adhesion	810:817	arg1	site					819:822	A metal ion-dependent adhesion site	788:822	A metal ion-dependent adhesion site (MIDAS) in the betaA domain	788:850	A metal ion-dependent adhesion site (MIDAS) in the betaA domain is positioned to participate in a ligand-binding interface formed of loops from the propeller and betaA domains.
11546839	6	42	theme	ion-dependent	796:808	arg1	MIDAS					825:829	MIDAS	825:829	MIDAS	825:829	A metal ion-dependent adhesion site (MIDAS) in the betaA domain is positioned to participate in a ligand-binding interface formed of loops from the propeller and betaA domains.
11546839	6	42	theme	ion-dependent	796:808	arg1	site					819:822	A metal ion-dependent adhesion site	788:822	A metal ion-dependent adhesion site (MIDAS) in the betaA domain	788:850	A metal ion-dependent adhesion site (MIDAS) in the betaA domain is positioned to participate in a ligand-binding interface formed of loops from the propeller and betaA domains.
11546839	5	43	theme	seven-bladed	642:653	arg1	beta-propeller					655:668	a seven-bladed beta-propeller	640:668	a seven-bladed beta-propeller from alphaV	640:680	The main inter-subunit interface lies within the head, between a seven-bladed beta-propeller from alphaV and an A domain from beta3, and bears a striking resemblance to the Galpha/Gbeta interface in G proteins.
11546839	4	44	attach	linked	546:551	arg1	regulation					565:574	integrin regulation	556:574	integrin regulation	556:574	In the crystal, alphaVbeta3 is severely bent at a defined region in its tails, reflecting an unusual flexibility that may be linked to integrin regulation.
11546839	4	44	attach	linked	546:551	arg2	flexibility					522:532	an unusual flexibility	511:532	an unusual flexibility that may be linked to integrin regulation	511:574	In the crystal, alphaVbeta3 is severely bent at a defined region in its tails, reflecting an unusual flexibility that may be linked to integrin regulation.
11546839	2	45	theme	extracellular	292:304	arg1	portion					306:312	the extracellular portion	288:312	the extracellular portion of integrin alphaVbeta3	288:336	We have solved the crystal structure of the extracellular portion of integrin alphaVbeta3 at 3.1 A resolution.
11546839	1	46	theme	divalent	134:141	arg1	adhesion					186:193	divalent cation-dependent cell-cell and cell-matrix adhesion	134:193	divalent cation-dependent cell-cell and cell-matrix adhesion	134:193	Integrins are alphabeta heterodimeric receptors that mediate divalent cation-dependent cell-cell and cell-matrix adhesion through tightly regulated interactions with ligands.
11546839	0	47	dep	Vbeta3	65:70	arg1	structure					8:16	Crystal structure	0:16	Crystal structure of the extracellular segment of integrin alpha	0:63	Crystal structure of the extracellular segment of integrin alpha Vbeta3.
11546839	6	48	theme	metal	790:794	arg1	MIDAS					825:829	MIDAS	825:829	MIDAS	825:829	A metal ion-dependent adhesion site (MIDAS) in the betaA domain is positioned to participate in a ligand-binding interface formed of loops from the propeller and betaA domains.
11546839	6	48	theme	metal	790:794	arg1	site					819:822	A metal ion-dependent adhesion site	788:822	A metal ion-dependent adhesion site (MIDAS) in the betaA domain	788:850	A metal ion-dependent adhesion site (MIDAS) in the betaA domain is positioned to participate in a ligand-binding interface formed of loops from the propeller and betaA domains.
11546839	1	49	theme	cation-dependent	143:158	arg1	adhesion					186:193	divalent cation-dependent cell-cell and cell-matrix adhesion	134:193	divalent cation-dependent cell-cell and cell-matrix adhesion	134:193	Integrins are alphabeta heterodimeric receptors that mediate divalent cation-dependent cell-cell and cell-matrix adhesion through tightly regulated interactions with ligands.
11546839	5	50	from	alphaV	675:680	arg1	beta-propeller					655:668	a seven-bladed beta-propeller	640:668	a seven-bladed beta-propeller from alphaV	640:680	The main inter-subunit interface lies within the head, between a seven-bladed beta-propeller from alphaV and an A domain from beta3, and bears a striking resemblance to the Galpha/Gbeta interface in G proteins.
11546839	5	50	from	alphaV	675:680	arg1	domain					691:696	an A domain	686:696	an A domain from beta3	686:707	The main inter-subunit interface lies within the head, between a seven-bladed beta-propeller from alphaV and an A domain from beta3, and bears a striking resemblance to the Galpha/Gbeta interface in G proteins.
11546839	1	51	theme	cell-cell	160:168	arg1	adhesion					186:193	divalent cation-dependent cell-cell and cell-matrix adhesion	134:193	divalent cation-dependent cell-cell and cell-matrix adhesion	134:193	Integrins are alphabeta heterodimeric receptors that mediate divalent cation-dependent cell-cell and cell-matrix adhesion through tightly regulated interactions with ligands.
11546839	0	52	theme	alpha	59:63	arg1	segment					39:45	the extracellular segment	21:45	the extracellular segment of integrin alpha	21:63	Crystal structure of the extracellular segment of integrin alpha Vbeta3.
19704023	0	0	theme	transmembrane	85:97	arg1	fragment					99:106	an alpha/beta transmembrane fragment	71:106	an alpha/beta transmembrane fragment	71:106	Crystal structure of the complete integrin alphaVbeta3 ectodomain plus an alpha/beta transmembrane fragment.
19704023	5	1	theme	inactive	705:712	arg1	alphaVbeta3					726:736	inactive full-length alphaVbeta3	705:736	inactive full-length alphaVbeta3	705:736	Fluorescent lifetime imaging microscopy of inactive full-length alphaVbeta3 on live cells yields a donor-membrane acceptor distance, which is consistent with the bent conformation and does not change in the activated integrin.
19704023	6	2	theme	conformational	1153:1166	arg1	changes					1168:1174	conformational changes	1153:1174	conformational changes other than the postulated switch to a genu-linear state	1153:1230	These data are the first direct demonstration of conformational coupling of the integrin leg and head domains, identify the IE2-thigh interface as a critical steric barrier in integrin activation, and suggest that inside-out activation in intact cells may involve conformational changes other than the postulated switch to a genu-linear state.
19704023	0	3	theme	alpha/beta	74:83	arg1	fragment					99:106	an alpha/beta transmembrane fragment	71:106	an alpha/beta transmembrane fragment	71:106	Crystal structure of the complete integrin alphaVbeta3 ectodomain plus an alpha/beta transmembrane fragment.
19704023	6	4	theme	leg	978:980	arg1	coupling					953:960	conformational coupling	938:960	conformational coupling of the integrin leg and head domains	938:997	These data are the first direct demonstration of conformational coupling of the integrin leg and head domains, identify the IE2-thigh interface as a critical steric barrier in integrin activation, and suggest that inside-out activation in intact cells may involve conformational changes other than the postulated switch to a genu-linear state.
19704023	5	5	theme	full-length	714:724	arg1	alphaVbeta3					726:736	inactive full-length alphaVbeta3	705:736	inactive full-length alphaVbeta3	705:736	Fluorescent lifetime imaging microscopy of inactive full-length alphaVbeta3 on live cells yields a donor-membrane acceptor distance, which is consistent with the bent conformation and does not change in the activated integrin.
19704023	6	6	theme	first	908:912	arg1	demonstration					921:933	the first direct demonstration	904:933	the first direct demonstration of conformational coupling of the integrin leg and head domains	904:997	These data are the first direct demonstration of conformational coupling of the integrin leg and head domains, identify the IE2-thigh interface as a critical steric barrier in integrin activation, and suggest that inside-out activation in intact cells may involve conformational changes other than the postulated switch to a genu-linear state.
19704023	6	6	theme	first	908:912	arg1	data					895:898	These data	889:898	These data	889:898	These data are the first direct demonstration of conformational coupling of the integrin leg and head domains, identify the IE2-thigh interface as a critical steric barrier in integrin activation, and suggest that inside-out activation in intact cells may involve conformational changes other than the postulated switch to a genu-linear state.
19704023	1	7	theme	beta3	284:288	arg1	subunits					290:297	the alphaV and beta3 subunits	269:297	subunits	290:297	We determined the crystal structure of 1TM-alphaVbeta3, which represents the complete unconstrained ectodomain plus short C-terminal transmembrane stretches of the alphaV and beta3 subunits.
19704023	6	8	theme	integrin	969:976	arg1	leg					978:980	the integrin leg and head domains	965:997	leg	978:980	These data are the first direct demonstration of conformational coupling of the integrin leg and head domains, identify the IE2-thigh interface as a critical steric barrier in integrin activation, and suggest that inside-out activation in intact cells may involve conformational changes other than the postulated switch to a genu-linear state.
19704023	5	9	theme	alphaVbeta3	726:736	arg1	microscopy					691:700	Fluorescent lifetime imaging microscopy	662:700	Fluorescent lifetime imaging microscopy of inactive full-length alphaVbeta3 on live cells	662:750	Fluorescent lifetime imaging microscopy of inactive full-length alphaVbeta3 on live cells yields a donor-membrane acceptor distance, which is consistent with the bent conformation and does not change in the activated integrin.
19704023	2	10	from	solution	351:358	arg1	compact					324:330	compact	324:330	compact	324:330	1TM-alphaVbeta3 is more compact and less active in solution when compared with DeltaTM-alphaVbeta3, which lacks the short C-terminal stretches.
19704023	1	11	theme	subunits	290:297	arg1	ectodomain					209:218	complete unconstrained ectodomain	186:218	complete unconstrained ectodomain	186:218	We determined the crystal structure of 1TM-alphaVbeta3, which represents the complete unconstrained ectodomain plus short C-terminal transmembrane stretches of the alphaV and beta3 subunits.
19704023	1	11	theme	subunits	290:297	arg1	subunits					290:297	the alphaV and beta3 subunits	269:297	subunits	290:297	We determined the crystal structure of 1TM-alphaVbeta3, which represents the complete unconstrained ectodomain plus short C-terminal transmembrane stretches of the alphaV and beta3 subunits.
19704023	0	12	theme	fragment	99:106	arg1	structure					8:16	Crystal structure	0:16	Crystal structure of the complete integrin alphaVbeta3 ectodomain plus an alpha/beta transmembrane fragment	0:106	Crystal structure of the complete integrin alphaVbeta3 ectodomain plus an alpha/beta transmembrane fragment.
19704023	6	13	theme	critical	1038:1045	arg1	barrier					1054:1060	a critical steric barrier	1036:1060	a critical steric barrier in integrin activation	1036:1083	These data are the first direct demonstration of conformational coupling of the integrin leg and head domains, identify the IE2-thigh interface as a critical steric barrier in integrin activation, and suggest that inside-out activation in intact cells may involve conformational changes other than the postulated switch to a genu-linear state.
19704023	6	13	theme	critical	1038:1045	arg1	interface					1023:1031	the IE2-thigh interface	1009:1031	the IE2-thigh interface	1009:1031	These data are the first direct demonstration of conformational coupling of the integrin leg and head domains, identify the IE2-thigh interface as a critical steric barrier in integrin activation, and suggest that inside-out activation in intact cells may involve conformational changes other than the postulated switch to a genu-linear state.
19704023	5	14	theme	lifetime	674:681	arg1	microscopy					691:700	Fluorescent lifetime imaging microscopy	662:700	Fluorescent lifetime imaging microscopy of inactive full-length alphaVbeta3 on live cells	662:750	Fluorescent lifetime imaging microscopy of inactive full-length alphaVbeta3 on live cells yields a donor-membrane acceptor distance, which is consistent with the bent conformation and does not change in the activated integrin.
19704023	5	15	theme	Fluorescent	662:672	arg1	microscopy					691:700	Fluorescent lifetime imaging microscopy	662:700	Fluorescent lifetime imaging microscopy of inactive full-length alphaVbeta3 on live cells	662:750	Fluorescent lifetime imaging microscopy of inactive full-length alphaVbeta3 on live cells yields a donor-membrane acceptor distance, which is consistent with the bent conformation and does not change in the activated integrin.
19704023	3	16	theme	thigh	556:560	arg1	domains					562:568	the thigh domains	552:568	the thigh domains	552:568	The structure reveals a bent conformation and defines the alpha-beta interface between IE2 (EGF-like 2) and the thigh domains.
19704023	2	17	theme	short	416:420	arg1	stretches					433:441	the short C-terminal stretches	412:441	the short C-terminal stretches	412:441	1TM-alphaVbeta3 is more compact and less active in solution when compared with DeltaTM-alphaVbeta3, which lacks the short C-terminal stretches.
19704023	6	18	theme	inside-out	1103:1112	arg1	activation					1114:1123	inside-out activation	1103:1123	inside-out activation in intact cells	1103:1139	These data are the first direct demonstration of conformational coupling of the integrin leg and head domains, identify the IE2-thigh interface as a critical steric barrier in integrin activation, and suggest that inside-out activation in intact cells may involve conformational changes other than the postulated switch to a genu-linear state.
19704023	6	19	theme	coupling	953:960	arg1	demonstration					921:933	the first direct demonstration	904:933	the first direct demonstration of conformational coupling of the integrin leg and head domains	904:997	These data are the first direct demonstration of conformational coupling of the integrin leg and head domains, identify the IE2-thigh interface as a critical steric barrier in integrin activation, and suggest that inside-out activation in intact cells may involve conformational changes other than the postulated switch to a genu-linear state.
19704023	6	19	theme	coupling	953:960	arg1	data					895:898	These data	889:898	These data	889:898	These data are the first direct demonstration of conformational coupling of the integrin leg and head domains, identify the IE2-thigh interface as a critical steric barrier in integrin activation, and suggest that inside-out activation in intact cells may involve conformational changes other than the postulated switch to a genu-linear state.
19704023	5	20	theme	imaging	683:689	arg1	microscopy					691:700	Fluorescent lifetime imaging microscopy	662:700	Fluorescent lifetime imaging microscopy of inactive full-length alphaVbeta3 on live cells	662:750	Fluorescent lifetime imaging microscopy of inactive full-length alphaVbeta3 on live cells yields a donor-membrane acceptor distance, which is consistent with the bent conformation and does not change in the activated integrin.
19704023	5	21	theme	activated	869:877	arg1	integrin					879:886	the activated integrin	865:886	the activated integrin	865:886	Fluorescent lifetime imaging microscopy of inactive full-length alphaVbeta3 on live cells yields a donor-membrane acceptor distance, which is consistent with the bent conformation and does not change in the activated integrin.
19704023	1	22	theme	complete	186:193	arg1	ectodomain					209:218	complete unconstrained ectodomain	186:218	complete unconstrained ectodomain	186:218	We determined the crystal structure of 1TM-alphaVbeta3, which represents the complete unconstrained ectodomain plus short C-terminal transmembrane stretches of the alphaV and beta3 subunits.
19704023	1	22	theme	complete	186:193	arg1	subunits					290:297	the alphaV and beta3 subunits	269:297	subunits	290:297	We determined the crystal structure of 1TM-alphaVbeta3, which represents the complete unconstrained ectodomain plus short C-terminal transmembrane stretches of the alphaV and beta3 subunits.
19704023	6	23	theme	conformational	938:951	arg1	coupling					953:960	conformational coupling	938:960	conformational coupling of the integrin leg and head domains	938:997	These data are the first direct demonstration of conformational coupling of the integrin leg and head domains, identify the IE2-thigh interface as a critical steric barrier in integrin activation, and suggest that inside-out activation in intact cells may involve conformational changes other than the postulated switch to a genu-linear state.
19704023	6	24	theme	intact	1128:1133	arg1	cells					1135:1139	intact cells	1128:1139	intact cells	1128:1139	These data are the first direct demonstration of conformational coupling of the integrin leg and head domains, identify the IE2-thigh interface as a critical steric barrier in integrin activation, and suggest that inside-out activation in intact cells may involve conformational changes other than the postulated switch to a genu-linear state.
19704023	1	25	theme	unconstrained	195:207	arg1	ectodomain					209:218	complete unconstrained ectodomain	186:218	complete unconstrained ectodomain	186:218	We determined the crystal structure of 1TM-alphaVbeta3, which represents the complete unconstrained ectodomain plus short C-terminal transmembrane stretches of the alphaV and beta3 subunits.
19704023	1	25	theme	unconstrained	195:207	arg1	subunits					290:297	the alphaV and beta3 subunits	269:297	subunits	290:297	We determined the crystal structure of 1TM-alphaVbeta3, which represents the complete unconstrained ectodomain plus short C-terminal transmembrane stretches of the alphaV and beta3 subunits.
19704023	0	26	theme	Crystal	0:6	arg1	structure					8:16	Crystal structure	0:16	Crystal structure of the complete integrin alphaVbeta3 ectodomain plus an alpha/beta transmembrane fragment	0:106	Crystal structure of the complete integrin alphaVbeta3 ectodomain plus an alpha/beta transmembrane fragment.
19704023	5	27	from	microscopy	691:700	arg1	cells					746:750	live cells	741:750	live cells	741:750	Fluorescent lifetime imaging microscopy of inactive full-length alphaVbeta3 on live cells yields a donor-membrane acceptor distance, which is consistent with the bent conformation and does not change in the activated integrin.
19704023	6	28	from	barrier	1054:1060	arg1	activation					1074:1083	integrin activation	1065:1083	integrin activation	1065:1083	These data are the first direct demonstration of conformational coupling of the integrin leg and head domains, identify the IE2-thigh interface as a critical steric barrier in integrin activation, and suggest that inside-out activation in intact cells may involve conformational changes other than the postulated switch to a genu-linear state.
19704023	6	29	from	activation	1114:1123	arg1	cells					1135:1139	intact cells	1128:1139	intact cells	1128:1139	These data are the first direct demonstration of conformational coupling of the integrin leg and head domains, identify the IE2-thigh interface as a critical steric barrier in integrin activation, and suggest that inside-out activation in intact cells may involve conformational changes other than the postulated switch to a genu-linear state.
19704023	6	30	theme	genu-linear	1214:1224	arg1	state					1226:1230	a genu-linear state	1212:1230	a genu-linear state	1212:1230	These data are the first direct demonstration of conformational coupling of the integrin leg and head domains, identify the IE2-thigh interface as a critical steric barrier in integrin activation, and suggest that inside-out activation in intact cells may involve conformational changes other than the postulated switch to a genu-linear state.
19704023	3	31	theme	bent	468:471	arg1	conformation					473:484	a bent conformation	466:484	a bent conformation	466:484	The structure reveals a bent conformation and defines the alpha-beta interface between IE2 (EGF-like 2) and the thigh domains.
19704023	5	32	theme	donor-membrane	761:774	arg1	consistent					804:813	consistent	804:813	consistent	804:813	Fluorescent lifetime imaging microscopy of inactive full-length alphaVbeta3 on live cells yields a donor-membrane acceptor distance, which is consistent with the bent conformation and does not change in the activated integrin.
19704023	5	32	theme	donor-membrane	761:774	arg1	distance					785:792	a donor-membrane acceptor distance	759:792	a donor-membrane acceptor distance	759:792	Fluorescent lifetime imaging microscopy of inactive full-length alphaVbeta3 on live cells yields a donor-membrane acceptor distance, which is consistent with the bent conformation and does not change in the activated integrin.
19704023	3	33	theme	alpha-beta	502:511	arg1	interface					513:521	the alpha-beta interface	498:521	the alpha-beta interface between IE2 (EGF-like 2) and the thigh domains	498:568	The structure reveals a bent conformation and defines the alpha-beta interface between IE2 (EGF-like 2) and the thigh domains.
19704023	4	34	theme	site-directed	599:611	arg1	mutagenesis					613:623	site-directed mutagenesis	599:623	site-directed mutagenesis	599:623	Modifying this interface by site-directed mutagenesis leads to robust integrin activation.
19704023	5	35	theme	acceptor	776:783	arg1	consistent					804:813	consistent	804:813	consistent	804:813	Fluorescent lifetime imaging microscopy of inactive full-length alphaVbeta3 on live cells yields a donor-membrane acceptor distance, which is consistent with the bent conformation and does not change in the activated integrin.
19704023	5	35	theme	acceptor	776:783	arg1	distance					785:792	a donor-membrane acceptor distance	759:792	a donor-membrane acceptor distance	759:792	Fluorescent lifetime imaging microscopy of inactive full-length alphaVbeta3 on live cells yields a donor-membrane acceptor distance, which is consistent with the bent conformation and does not change in the activated integrin.
19704023	1	36	theme	short	225:229	arg1	stretches					256:264	short C-terminal transmembrane stretches	225:264	short C-terminal transmembrane stretches	225:264	We determined the crystal structure of 1TM-alphaVbeta3, which represents the complete unconstrained ectodomain plus short C-terminal transmembrane stretches of the alphaV and beta3 subunits.
19704023	0	37	theme	integrin	34:41	arg1	ectodomain					55:64	the complete integrin alphaVbeta3 ectodomain	21:64	the complete integrin alphaVbeta3 ectodomain	21:64	Crystal structure of the complete integrin alphaVbeta3 ectodomain plus an alpha/beta transmembrane fragment.
19704023	6	38	theme	IE2-thigh	1013:1021	arg1	barrier					1054:1060	a critical steric barrier	1036:1060	a critical steric barrier in integrin activation	1036:1083	These data are the first direct demonstration of conformational coupling of the integrin leg and head domains, identify the IE2-thigh interface as a critical steric barrier in integrin activation, and suggest that inside-out activation in intact cells may involve conformational changes other than the postulated switch to a genu-linear state.
19704023	6	38	theme	IE2-thigh	1013:1021	arg1	interface					1023:1031	the IE2-thigh interface	1009:1031	the IE2-thigh interface	1009:1031	These data are the first direct demonstration of conformational coupling of the integrin leg and head domains, identify the IE2-thigh interface as a critical steric barrier in integrin activation, and suggest that inside-out activation in intact cells may involve conformational changes other than the postulated switch to a genu-linear state.
19704023	6	39	theme	postulated	1191:1200	arg1	switch					1202:1207	the postulated switch	1187:1207	the postulated switch to a genu-linear state	1187:1230	These data are the first direct demonstration of conformational coupling of the integrin leg and head domains, identify the IE2-thigh interface as a critical steric barrier in integrin activation, and suggest that inside-out activation in intact cells may involve conformational changes other than the postulated switch to a genu-linear state.
19704023	5	40	with	consistent	804:813	arg1	conformation					829:840	the bent conformation	820:840	the bent conformation	820:840	Fluorescent lifetime imaging microscopy of inactive full-length alphaVbeta3 on live cells yields a donor-membrane acceptor distance, which is consistent with the bent conformation and does not change in the activated integrin.
19704023	1	41	theme	C-terminal	231:240	arg1	stretches					256:264	short C-terminal transmembrane stretches	225:264	short C-terminal transmembrane stretches	225:264	We determined the crystal structure of 1TM-alphaVbeta3, which represents the complete unconstrained ectodomain plus short C-terminal transmembrane stretches of the alphaV and beta3 subunits.
19704023	0	42	theme	complete	25:32	arg1	ectodomain					55:64	the complete integrin alphaVbeta3 ectodomain	21:64	the complete integrin alphaVbeta3 ectodomain	21:64	Crystal structure of the complete integrin alphaVbeta3 ectodomain plus an alpha/beta transmembrane fragment.
19704023	6	43	theme	direct	914:919	arg1	demonstration					921:933	the first direct demonstration	904:933	the first direct demonstration of conformational coupling of the integrin leg and head domains	904:997	These data are the first direct demonstration of conformational coupling of the integrin leg and head domains, identify the IE2-thigh interface as a critical steric barrier in integrin activation, and suggest that inside-out activation in intact cells may involve conformational changes other than the postulated switch to a genu-linear state.
19704023	6	43	theme	direct	914:919	arg1	data					895:898	These data	889:898	These data	889:898	These data are the first direct demonstration of conformational coupling of the integrin leg and head domains, identify the IE2-thigh interface as a critical steric barrier in integrin activation, and suggest that inside-out activation in intact cells may involve conformational changes other than the postulated switch to a genu-linear state.
19704023	1	44	dep	ectodomain	209:218	arg1	the					182:184	the	182:184	the	182:184	We determined the crystal structure of 1TM-alphaVbeta3, which represents the complete unconstrained ectodomain plus short C-terminal transmembrane stretches of the alphaV and beta3 subunits.
19704023	1	45	theme	transmembrane	242:254	arg1	stretches					256:264	short C-terminal transmembrane stretches	225:264	short C-terminal transmembrane stretches	225:264	We determined the crystal structure of 1TM-alphaVbeta3, which represents the complete unconstrained ectodomain plus short C-terminal transmembrane stretches of the alphaV and beta3 subunits.
19704023	0	46	theme	ectodomain	55:64	arg1	structure					8:16	Crystal structure	0:16	Crystal structure of the complete integrin alphaVbeta3 ectodomain plus an alpha/beta transmembrane fragment	0:106	Crystal structure of the complete integrin alphaVbeta3 ectodomain plus an alpha/beta transmembrane fragment.
19704023	5	47	theme	live	741:744	arg1	cells					746:750	live cells	741:750	live cells	741:750	Fluorescent lifetime imaging microscopy of inactive full-length alphaVbeta3 on live cells yields a donor-membrane acceptor distance, which is consistent with the bent conformation and does not change in the activated integrin.
19704023	5	48	theme	bent	824:827	arg1	conformation					829:840	the bent conformation	820:840	the bent conformation	820:840	Fluorescent lifetime imaging microscopy of inactive full-length alphaVbeta3 on live cells yields a donor-membrane acceptor distance, which is consistent with the bent conformation and does not change in the activated integrin.
19704023	6	49	theme	other	1176:1180	arg1	changes					1168:1174	conformational changes	1153:1174	conformational changes other than the postulated switch to a genu-linear state	1153:1230	These data are the first direct demonstration of conformational coupling of the integrin leg and head domains, identify the IE2-thigh interface as a critical steric barrier in integrin activation, and suggest that inside-out activation in intact cells may involve conformational changes other than the postulated switch to a genu-linear state.
19704023	0	50	theme	alphaVbeta3	43:53	arg1	ectodomain					55:64	the complete integrin alphaVbeta3 ectodomain	21:64	the complete integrin alphaVbeta3 ectodomain	21:64	Crystal structure of the complete integrin alphaVbeta3 ectodomain plus an alpha/beta transmembrane fragment.
19704023	1	51	theme	crystal	127:133	arg1	structure					135:143	the crystal structure	123:143	the crystal structure	123:143	We determined the crystal structure of 1TM-alphaVbeta3, which represents the complete unconstrained ectodomain plus short C-terminal transmembrane stretches of the alphaV and beta3 subunits.
19704023	6	52	theme	domains	991:997	arg1	coupling					953:960	conformational coupling	938:960	conformational coupling of the integrin leg and head domains	938:997	These data are the first direct demonstration of conformational coupling of the integrin leg and head domains, identify the IE2-thigh interface as a critical steric barrier in integrin activation, and suggest that inside-out activation in intact cells may involve conformational changes other than the postulated switch to a genu-linear state.
19704023	6	53	theme	steric	1047:1052	arg1	barrier					1054:1060	a critical steric barrier	1036:1060	a critical steric barrier in integrin activation	1036:1083	These data are the first direct demonstration of conformational coupling of the integrin leg and head domains, identify the IE2-thigh interface as a critical steric barrier in integrin activation, and suggest that inside-out activation in intact cells may involve conformational changes other than the postulated switch to a genu-linear state.
19704023	6	53	theme	steric	1047:1052	arg1	interface					1023:1031	the IE2-thigh interface	1009:1031	the IE2-thigh interface	1009:1031	These data are the first direct demonstration of conformational coupling of the integrin leg and head domains, identify the IE2-thigh interface as a critical steric barrier in integrin activation, and suggest that inside-out activation in intact cells may involve conformational changes other than the postulated switch to a genu-linear state.
19704023	2	54	from	compact	324:330	arg1	solution					351:358	solution	351:358	solution	351:358	1TM-alphaVbeta3 is more compact and less active in solution when compared with DeltaTM-alphaVbeta3, which lacks the short C-terminal stretches.
19704023	4	55	theme	integrin	641:648	arg1	activation					650:659	robust integrin activation	634:659	robust integrin activation	634:659	Modifying this interface by site-directed mutagenesis leads to robust integrin activation.
19704023	1	56	theme	1TM-alphaVbeta3	148:162	arg1	structure					135:143	the crystal structure	123:143	the crystal structure	123:143	We determined the crystal structure of 1TM-alphaVbeta3, which represents the complete unconstrained ectodomain plus short C-terminal transmembrane stretches of the alphaV and beta3 subunits.
19704023	2	57	theme	C-terminal	422:431	arg1	stretches					433:441	the short C-terminal stretches	412:441	the short C-terminal stretches	412:441	1TM-alphaVbeta3 is more compact and less active in solution when compared with DeltaTM-alphaVbeta3, which lacks the short C-terminal stretches.
19704023	4	58	theme	robust	634:639	arg1	activation					650:659	robust integrin activation	634:659	robust integrin activation	634:659	Modifying this interface by site-directed mutagenesis leads to robust integrin activation.
19704023	6	59	theme	head	986:989	arg1	domains					991:997	the integrin leg and head domains	965:997	domains	991:997	These data are the first direct demonstration of conformational coupling of the integrin leg and head domains, identify the IE2-thigh interface as a critical steric barrier in integrin activation, and suggest that inside-out activation in intact cells may involve conformational changes other than the postulated switch to a genu-linear state.
19704023	6	60	theme	integrin	1065:1072	arg1	activation					1074:1083	integrin activation	1065:1083	integrin activation	1065:1083	These data are the first direct demonstration of conformational coupling of the integrin leg and head domains, identify the IE2-thigh interface as a critical steric barrier in integrin activation, and suggest that inside-out activation in intact cells may involve conformational changes other than the postulated switch to a genu-linear state.
19704023	1	61	theme	alphaV	273:278	arg1	subunits					290:297	the alphaV and beta3 subunits	269:297	subunits	290:297	We determined the crystal structure of 1TM-alphaVbeta3, which represents the complete unconstrained ectodomain plus short C-terminal transmembrane stretches of the alphaV and beta3 subunits.
19111664	7	0	theme	open	1039:1042	arg1	conformation					1059:1070	the open, high-affinity conformation	1035:1070	conformation	1059:1070	By contrast, an additional lateral force applied to the beta subunit to mimic attachment to moving actin filaments stabilizes the open, high-affinity conformation.
19111664	4	1	theme	beta	582:585	arg1	-PSI					589:592	the beta(3)-PSI	578:592	the beta(3)-PSI	578:592	The beta(3) knee passes between the beta(3)-PSI and alpha(IIb)-knob to bury the lower beta leg in a cleft, from which it is released for extension.
19111664	2	2	theme	ligand	445:450	arg1	binding					452:458	ligand binding	445:458	ligand binding	445:458	Ca and Mg ions in the recognition site, including the synergistic metal ion binding site (SyMBS), are loaded prior to ligand binding.
19111664	1	3	theme	cytoskeleton	274:285	arg1	attachment					287:296	cytoskeleton attachment	274:296	cytoskeleton attachment	274:296	The complete ectodomain of integrin alpha(IIb)beta(3) reveals a bent, closed, low-affinity conformation, the beta knee, and a mechanism for linking cytoskeleton attachment to high affinity for ligand.
19111664	5	4	from	molecules	713:721	arg1	EM					739:740	EM	739:740	EM	739:740	Different integrin molecules in crystals and EM reveal breathing that appears on pathway to extension.
19111664	5	4	from	molecules	713:721	arg1	crystals					726:733	crystals	726:733	crystals	726:733	Different integrin molecules in crystals and EM reveal breathing that appears on pathway to extension.
19111664	1	5	theme	integrin	153:160	arg1	3					177:177	3	177:177	3	177:177	The complete ectodomain of integrin alpha(IIb)beta(3) reveals a bent, closed, low-affinity conformation, the beta knee, and a mechanism for linking cytoskeleton attachment to high affinity for ligand.
19111664	1	5	theme	integrin	153:160	arg1	beta					172:175	integrin alpha(IIb)beta	153:175	integrin alpha(IIb)beta(3)	153:178	The complete ectodomain of integrin alpha(IIb)beta(3) reveals a bent, closed, low-affinity conformation, the beta knee, and a mechanism for linking cytoskeleton attachment to high affinity for ligand.
19111664	0	6	from	Structure	0:8	arg1	state					69:73	a physiologic resting state	47:73	a physiologic resting state	47:73	Structure of a complete integrin ectodomain in a physiologic resting state and activation and deactivation by applied forces.
19111664	7	7	theme	lateral	936:942	arg1	force					944:948	an additional lateral force	922:948	an additional lateral force applied to the beta subunit to mimic attachment to moving actin filaments	922:1022	By contrast, an additional lateral force applied to the beta subunit to mimic attachment to moving actin filaments stabilizes the open, high-affinity conformation.
19111664	4	8	from	leg	637:639	arg1	cleft					646:650	a cleft	644:650	a cleft	644:650	The beta(3) knee passes between the beta(3)-PSI and alpha(IIb)-knob to bury the lower beta leg in a cleft, from which it is released for extension.
19111664	8	9	theme	high-affinity	1187:1199	arg1	state					1201:1205	their high-affinity state	1181:1205	their high-affinity state	1181:1205	This mechanism propagates allostery over long distances and couples cytoskeleton attachment of integrins to their high-affinity state.
19111664	6	10	theme	Tensile	797:803	arg1	force					805:809	Tensile force	797:809	Tensile force applied to the extended ligand-receptor complex	797:857	Tensile force applied to the extended ligand-receptor complex stabilizes the closed, low-affinity conformation.
19111664	7	11	theme	actin	1008:1012	arg1	filaments					1014:1022	moving actin filaments	1001:1022	moving actin filaments	1001:1022	By contrast, an additional lateral force applied to the beta subunit to mimic attachment to moving actin filaments stabilizes the open, high-affinity conformation.
19111664	1	12	theme	high	301:304	arg1	affinity					306:313	high affinity	301:313	high affinity for ligand	301:324	The complete ectodomain of integrin alpha(IIb)beta(3) reveals a bent, closed, low-affinity conformation, the beta knee, and a mechanism for linking cytoskeleton attachment to high affinity for ligand.
19111664	6	13	theme	closed	874:879	arg1	conformation					895:906	the closed, low-affinity conformation	870:906	the closed, low-affinity conformation	870:906	Tensile force applied to the extended ligand-receptor complex stabilizes the closed, low-affinity conformation.
19111664	1	14	theme	alpha	162:166	arg1	3					177:177	3	177:177	3	177:177	The complete ectodomain of integrin alpha(IIb)beta(3) reveals a bent, closed, low-affinity conformation, the beta knee, and a mechanism for linking cytoskeleton attachment to high affinity for ligand.
19111664	1	14	theme	alpha	162:166	arg1	beta					172:175	integrin alpha(IIb)beta	153:175	integrin alpha(IIb)beta(3)	153:178	The complete ectodomain of integrin alpha(IIb)beta(3) reveals a bent, closed, low-affinity conformation, the beta knee, and a mechanism for linking cytoskeleton attachment to high affinity for ligand.
19111664	0	15	from	ectodomain	33:42	arg1	state					69:73	a physiologic resting state	47:73	a physiologic resting state	47:73	Structure of a complete integrin ectodomain in a physiologic resting state and activation and deactivation by applied forces.
19111664	2	16	theme	ion	399:401	arg1	SyMBS					417:421	SyMBS	417:421	SyMBS	417:421	Ca and Mg ions in the recognition site, including the synergistic metal ion binding site (SyMBS), are loaded prior to ligand binding.
19111664	2	16	theme	ion	399:401	arg1	site					411:414	the synergistic metal ion binding site	377:414	the synergistic metal ion binding site (SyMBS)	377:422	Ca and Mg ions in the recognition site, including the synergistic metal ion binding site (SyMBS), are loaded prior to ligand binding.
19111664	6	17	dep	closed	874:879	arg1	low-affinity					882:893	low-affinity	882:893	low-affinity	882:893	Tensile force applied to the extended ligand-receptor complex stabilizes the closed, low-affinity conformation.
19111664	2	18	theme	Ca	327:328	arg1	ions					337:340	Ca and Mg ions	327:340	Ca and Mg ions	327:340	Ca and Mg ions in the recognition site, including the synergistic metal ion binding site (SyMBS), are loaded prior to ligand binding.
19111664	2	18	theme	Ca	327:328	arg1	site					411:414	the synergistic metal ion binding site	377:414	the synergistic metal ion binding site (SyMBS)	377:422	Ca and Mg ions in the recognition site, including the synergistic metal ion binding site (SyMBS), are loaded prior to ligand binding.
19111664	2	19	theme	binding	403:409	arg1	SyMBS					417:421	SyMBS	417:421	SyMBS	417:421	Ca and Mg ions in the recognition site, including the synergistic metal ion binding site (SyMBS), are loaded prior to ligand binding.
19111664	2	19	theme	binding	403:409	arg1	site					411:414	the synergistic metal ion binding site	377:414	the synergistic metal ion binding site (SyMBS)	377:422	Ca and Mg ions in the recognition site, including the synergistic metal ion binding site (SyMBS), are loaded prior to ligand binding.
19111664	7	20	dep	subunit	970:976	arg1	mimic					981:985	mimic	981:985	to mimic attachment to moving actin filaments	978:1022	By contrast, an additional lateral force applied to the beta subunit to mimic attachment to moving actin filaments stabilizes the open, high-affinity conformation.
19111664	7	21	theme	high-affinity	1045:1057	arg1	conformation					1059:1070	the open, high-affinity conformation	1035:1070	conformation	1059:1070	By contrast, an additional lateral force applied to the beta subunit to mimic attachment to moving actin filaments stabilizes the open, high-affinity conformation.
19111664	4	22	theme	alpha	598:602	arg1	-knob					608:612	alpha(IIb)-knob	598:612	alpha(IIb)-knob	598:612	The beta(3) knee passes between the beta(3)-PSI and alpha(IIb)-knob to bury the lower beta leg in a cleft, from which it is released for extension.
19111664	1	23	theme	IIb	168:170	arg1	3					177:177	3	177:177	3	177:177	The complete ectodomain of integrin alpha(IIb)beta(3) reveals a bent, closed, low-affinity conformation, the beta knee, and a mechanism for linking cytoskeleton attachment to high affinity for ligand.
19111664	1	23	theme	IIb	168:170	arg1	beta					172:175	integrin alpha(IIb)beta	153:175	integrin alpha(IIb)beta(3)	153:178	The complete ectodomain of integrin alpha(IIb)beta(3) reveals a bent, closed, low-affinity conformation, the beta knee, and a mechanism for linking cytoskeleton attachment to high affinity for ligand.
19111664	7	24	theme	moving	1001:1006	arg1	filaments					1014:1022	moving actin filaments	1001:1022	moving actin filaments	1001:1022	By contrast, an additional lateral force applied to the beta subunit to mimic attachment to moving actin filaments stabilizes the open, high-affinity conformation.
19111664	8	25	theme	integrins	1168:1176	arg1	attachment					1154:1163	cytoskeleton attachment	1141:1163	cytoskeleton attachment of integrins	1141:1176	This mechanism propagates allostery over long distances and couples cytoskeleton attachment of integrins to their high-affinity state.
19111664	0	26	theme	complete	15:22	arg1	ectodomain					33:42	a complete integrin ectodomain	13:42	a complete integrin ectodomain in a physiologic resting state	13:73	Structure of a complete integrin ectodomain in a physiologic resting state and activation and deactivation by applied forces.
19111664	7	27	theme	additional	925:934	arg1	force					944:948	an additional lateral force	922:948	an additional lateral force applied to the beta subunit to mimic attachment to moving actin filaments	922:1022	By contrast, an additional lateral force applied to the beta subunit to mimic attachment to moving actin filaments stabilizes the open, high-affinity conformation.
19111664	1	28	theme	beta	172:175	arg1	ectodomain					139:148	The complete ectodomain	126:148	The complete ectodomain of integrin alpha(IIb)beta(3)	126:178	The complete ectodomain of integrin alpha(IIb)beta(3) reveals a bent, closed, low-affinity conformation, the beta knee, and a mechanism for linking cytoskeleton attachment to high affinity for ligand.
19111664	1	28	theme	beta	172:175	arg1	beta					172:175	integrin alpha(IIb)beta	153:175	integrin alpha(IIb)beta(3)	153:178	The complete ectodomain of integrin alpha(IIb)beta(3) reveals a bent, closed, low-affinity conformation, the beta knee, and a mechanism for linking cytoskeleton attachment to high affinity for ligand.
19111664	2	29	theme	recognition	349:359	arg1	site					361:364	the recognition site	345:364	the recognition site	345:364	Ca and Mg ions in the recognition site, including the synergistic metal ion binding site (SyMBS), are loaded prior to ligand binding.
19111664	1	30	theme	beta	235:238	arg1	knee					240:243	the beta knee	231:243	the beta knee	231:243	The complete ectodomain of integrin alpha(IIb)beta(3) reveals a bent, closed, low-affinity conformation, the beta knee, and a mechanism for linking cytoskeleton attachment to high affinity for ligand.
19111664	0	31	theme	applied	110:116	arg1	forces					118:123	applied forces	110:123	applied forces	110:123	Structure of a complete integrin ectodomain in a physiologic resting state and activation and deactivation by applied forces.
19111664	1	32	dep	bent	190:193	arg1	low-affinity					204:215	low-affinity	204:215	low-affinity	204:215	The complete ectodomain of integrin alpha(IIb)beta(3) reveals a bent, closed, low-affinity conformation, the beta knee, and a mechanism for linking cytoskeleton attachment to high affinity for ligand.
19111664	1	32	dep	bent	190:193	arg1	closed					196:201	closed	196:201	closed	196:201	The complete ectodomain of integrin alpha(IIb)beta(3) reveals a bent, closed, low-affinity conformation, the beta knee, and a mechanism for linking cytoskeleton attachment to high affinity for ligand.
19111664	5	33	theme	Different	694:702	arg1	molecules					713:721	Different integrin molecules	694:721	Different integrin molecules in crystals and EM	694:740	Different integrin molecules in crystals and EM reveal breathing that appears on pathway to extension.
19111664	0	34	theme	ectodomain	33:42	arg1	Structure					0:8	Structure	0:8	Structure of a complete integrin ectodomain in a physiologic resting state	0:73	Structure of a complete integrin ectodomain in a physiologic resting state and activation and deactivation by applied forces.
19111664	0	34	theme	ectodomain	33:42	arg1	deactivation					94:105	deactivation	94:105	deactivation	94:105	Structure of a complete integrin ectodomain in a physiologic resting state and activation and deactivation by applied forces.
19111664	0	34	theme	ectodomain	33:42	arg1	activation					79:88	activation	79:88	activation	79:88	Structure of a complete integrin ectodomain in a physiologic resting state and activation and deactivation by applied forces.
19111664	0	35	from	state	69:73	arg1	Structure					0:8	Structure	0:8	Structure of a complete integrin ectodomain in a physiologic resting state	0:73	Structure of a complete integrin ectodomain in a physiologic resting state and activation and deactivation by applied forces.
19111664	0	35	from	state	69:73	arg1	deactivation					94:105	deactivation	94:105	deactivation	94:105	Structure of a complete integrin ectodomain in a physiologic resting state and activation and deactivation by applied forces.
19111664	0	35	from	state	69:73	arg1	activation					79:88	activation	79:88	activation	79:88	Structure of a complete integrin ectodomain in a physiologic resting state and activation and deactivation by applied forces.
19111664	3	36	theme	ion	503:505	arg1	Electrophilicity					461:476	Electrophilicity	461:476	Electrophilicity of the ligand-binding Mg ion	461:505	Electrophilicity of the ligand-binding Mg ion is increased in the open conformation.
19111664	4	37	theme	beta	550:553	arg1	knee					558:561	The beta(3) knee	546:561	The beta(3) knee	546:561	The beta(3) knee passes between the beta(3)-PSI and alpha(IIb)-knob to bury the lower beta leg in a cleft, from which it is released for extension.
19111664	0	38	theme	integrin	24:31	arg1	ectodomain					33:42	a complete integrin ectodomain	13:42	a complete integrin ectodomain in a physiologic resting state	13:73	Structure of a complete integrin ectodomain in a physiologic resting state and activation and deactivation by applied forces.
19111664	2	39	theme	metal	393:397	arg1	SyMBS					417:421	SyMBS	417:421	SyMBS	417:421	Ca and Mg ions in the recognition site, including the synergistic metal ion binding site (SyMBS), are loaded prior to ligand binding.
19111664	2	39	theme	metal	393:397	arg1	site					411:414	the synergistic metal ion binding site	377:414	the synergistic metal ion binding site (SyMBS)	377:422	Ca and Mg ions in the recognition site, including the synergistic metal ion binding site (SyMBS), are loaded prior to ligand binding.
19111664	6	40	theme	extended	826:833	arg1	complex					851:857	the extended ligand-receptor complex	822:857	the extended ligand-receptor complex	822:857	Tensile force applied to the extended ligand-receptor complex stabilizes the closed, low-affinity conformation.
19111664	2	41	theme	Mg	334:335	arg1	ions					337:340	Ca and Mg ions	327:340	Ca and Mg ions	327:340	Ca and Mg ions in the recognition site, including the synergistic metal ion binding site (SyMBS), are loaded prior to ligand binding.
19111664	2	41	theme	Mg	334:335	arg1	site					411:414	the synergistic metal ion binding site	377:414	the synergistic metal ion binding site (SyMBS)	377:422	Ca and Mg ions in the recognition site, including the synergistic metal ion binding site (SyMBS), are loaded prior to ligand binding.
19111664	2	42	theme	synergistic	381:391	arg1	SyMBS					417:421	SyMBS	417:421	SyMBS	417:421	Ca and Mg ions in the recognition site, including the synergistic metal ion binding site (SyMBS), are loaded prior to ligand binding.
19111664	2	42	theme	synergistic	381:391	arg1	site					411:414	the synergistic metal ion binding site	377:414	the synergistic metal ion binding site (SyMBS)	377:422	Ca and Mg ions in the recognition site, including the synergistic metal ion binding site (SyMBS), are loaded prior to ligand binding.
19111664	3	43	theme	ligand-binding	485:498	arg1	ion					503:505	the ligand-binding Mg ion	481:505	the ligand-binding Mg ion	481:505	Electrophilicity of the ligand-binding Mg ion is increased in the open conformation.
19111664	7	44	theme	beta	965:968	arg1	subunit					970:976	the beta subunit	961:976	the beta subunit to mimic attachment to moving actin filaments	961:1022	By contrast, an additional lateral force applied to the beta subunit to mimic attachment to moving actin filaments stabilizes the open, high-affinity conformation.
19111664	3	45	theme	Mg	500:501	arg1	ion					503:505	the ligand-binding Mg ion	481:505	the ligand-binding Mg ion	481:505	Electrophilicity of the ligand-binding Mg ion is increased in the open conformation.
19111664	4	46	attach	released	670:677	arg1	cleft					646:650	a cleft	644:650	a cleft	644:650	The beta(3) knee passes between the beta(3)-PSI and alpha(IIb)-knob to bury the lower beta leg in a cleft, from which it is released for extension.
19111664	4	46	attach	released	670:677	arg2	it					664:665	it	664:665	it	664:665	The beta(3) knee passes between the beta(3)-PSI and alpha(IIb)-knob to bury the lower beta leg in a cleft, from which it is released for extension.
19111664	0	47	from	deactivation	94:105	arg1	state					69:73	a physiologic resting state	47:73	a physiologic resting state	47:73	Structure of a complete integrin ectodomain in a physiologic resting state and activation and deactivation by applied forces.
19111664	4	48	theme	lower	626:630	arg1	leg					637:639	the lower beta leg	622:639	the lower beta leg in a cleft, from which it is released for extension	622:691	The beta(3) knee passes between the beta(3)-PSI and alpha(IIb)-knob to bury the lower beta leg in a cleft, from which it is released for extension.
19111664	8	49	theme	long	1114:1117	arg1	distances					1119:1127	long distances	1114:1127	long distances	1114:1127	This mechanism propagates allostery over long distances and couples cytoskeleton attachment of integrins to their high-affinity state.
19111664	3	50	theme	open	527:530	arg1	conformation					532:543	the open conformation	523:543	the open conformation	523:543	Electrophilicity of the ligand-binding Mg ion is increased in the open conformation.
19111664	2	51	from	ions	337:340	arg1	site					361:364	the recognition site	345:364	the recognition site	345:364	Ca and Mg ions in the recognition site, including the synergistic metal ion binding site (SyMBS), are loaded prior to ligand binding.
19111664	8	52	theme	cytoskeleton	1141:1152	arg1	attachment					1154:1163	cytoskeleton attachment	1141:1163	cytoskeleton attachment of integrins	1141:1176	This mechanism propagates allostery over long distances and couples cytoskeleton attachment of integrins to their high-affinity state.
19111664	6	53	theme	ligand-receptor	835:849	arg1	complex					851:857	the extended ligand-receptor complex	822:857	the extended ligand-receptor complex	822:857	Tensile force applied to the extended ligand-receptor complex stabilizes the closed, low-affinity conformation.
19111664	0	54	theme	resting	61:67	arg1	state					69:73	a physiologic resting state	47:73	a physiologic resting state	47:73	Structure of a complete integrin ectodomain in a physiologic resting state and activation and deactivation by applied forces.
19111664	0	55	from	activation	79:88	arg1	state					69:73	a physiologic resting state	47:73	a physiologic resting state	47:73	Structure of a complete integrin ectodomain in a physiologic resting state and activation and deactivation by applied forces.
19111664	1	56	theme	complete	130:137	arg1	ectodomain					139:148	The complete ectodomain	126:148	The complete ectodomain of integrin alpha(IIb)beta(3)	126:178	The complete ectodomain of integrin alpha(IIb)beta(3) reveals a bent, closed, low-affinity conformation, the beta knee, and a mechanism for linking cytoskeleton attachment to high affinity for ligand.
19111664	1	56	theme	complete	130:137	arg1	beta					172:175	integrin alpha(IIb)beta	153:175	integrin alpha(IIb)beta(3)	153:178	The complete ectodomain of integrin alpha(IIb)beta(3) reveals a bent, closed, low-affinity conformation, the beta knee, and a mechanism for linking cytoskeleton attachment to high affinity for ligand.
19111664	1	57	theme	bent	190:193	arg1	conformation					217:228	a bent, closed, low-affinity conformation	188:228	a bent, closed, low-affinity conformation	188:228	The complete ectodomain of integrin alpha(IIb)beta(3) reveals a bent, closed, low-affinity conformation, the beta knee, and a mechanism for linking cytoskeleton attachment to high affinity for ligand.
19111664	0	58	theme	physiologic	49:59	arg1	state					69:73	a physiologic resting state	47:73	a physiologic resting state	47:73	Structure of a complete integrin ectodomain in a physiologic resting state and activation and deactivation by applied forces.
19111664	4	59	theme	beta	632:635	arg1	leg					637:639	the lower beta leg	622:639	the lower beta leg in a cleft, from which it is released for extension	622:691	The beta(3) knee passes between the beta(3)-PSI and alpha(IIb)-knob to bury the lower beta leg in a cleft, from which it is released for extension.
19111664	5	60	theme	integrin	704:711	arg1	molecules					713:721	Different integrin molecules	694:721	Different integrin molecules in crystals and EM	694:740	Different integrin molecules in crystals and EM reveal breathing that appears on pathway to extension.
27626375	2	0	theme	therapeutic	329:339	arg1	agents					341:346	therapeutic agents	329:346	therapeutic agents	329:346	Despite their central function in human physiology and although they are potential targets of therapeutic agents, there are no structures of human P2X receptors.
27626375	1	1	theme	immune	219:224	arg1	systems					226:232	the cardiovascular, neuronal and immune systems	186:232	the cardiovascular, neuronal and immune systems	186:232	P2X receptors are trimeric, non-selective cation channels activated by ATP that have important roles in the cardiovascular, neuronal and immune systems.
27626375	5	2	theme	intracellular	807:819	arg1	motif					821:825	an intracellular motif	804:825	an intracellular motif we term the 'cytoplasmic cap', which stabilizes the open state of the ion channel pore and creates lateral, phospholipid-lined cytoplasmic fenestrations for water and ion egress	804:1003	The open state structure harbours an intracellular motif we term the 'cytoplasmic cap', which stabilizes the open state of the ion channel pore and creates lateral, phospholipid-lined cytoplasmic fenestrations for water and ion egress.
27626375	7	3	theme	conformational	1187:1200	arg1	rearrangements					1202:1215	the conformational rearrangements	1183:1215	the conformational rearrangements that underlie P2X receptor gating and provide a foundation for the development of new pharmacological agents	1183:1324	These structures illuminate the conformational rearrangements that underlie P2X receptor gating and provide a foundation for the development of new pharmacological agents.
27626375	5	4	theme	pore	909:912	arg1	state					884:888	the open state	875:888	the open state of the ion channel pore	875:912	The open state structure harbours an intracellular motif we term the 'cytoplasmic cap', which stabilizes the open state of the ion channel pore and creates lateral, phospholipid-lined cytoplasmic fenestrations for water and ion egress.
27626375	4	5	theme	agonist-bound/open-pore	670:692	arg1	states					762:767	apo/resting, agonist-bound/open-pore, agonist-bound/closed-pore/desensitized and antagonist-bound/closed states	657:767	apo/resting, agonist-bound/open-pore, agonist-bound/closed-pore/desensitized and antagonist-bound/closed states	657:767	Here we report X-ray crystal structures of the human P2X3 receptor in apo/resting, agonist-bound/open-pore, agonist-bound/closed-pore/desensitized and antagonist-bound/closed states.
27626375	6	6	dep	antagonists	1022:1032	arg1	antagonists					1022:1032	The competitive antagonists	1006:1032	The competitive antagonists TNP-ATP and A-317491	1006:1053	The competitive antagonists TNP-ATP and A-317491 stabilize the apo/resting state and reveal the interactions responsible for competitive inhibition.
27626375	6	6	dep	antagonists	1022:1032	arg1	A-317491					1046:1053	A-317491	1046:1053	A-317491	1046:1053	The competitive antagonists TNP-ATP and A-317491 stabilize the apo/resting state and reveal the interactions responsible for competitive inhibition.
27626375	6	6	dep	antagonists	1022:1032	arg1	TNP-ATP					1034:1040	TNP-ATP	1034:1040	TNP-ATP	1034:1040	The competitive antagonists TNP-ATP and A-317491 stabilize the apo/resting state and reveal the interactions responsible for competitive inhibition.
27626375	1	7	dep	trimeric	100:107	arg1	non-selective					110:122	non-selective	110:122	non-selective	110:122	P2X receptors are trimeric, non-selective cation channels activated by ATP that have important roles in the cardiovascular, neuronal and immune systems.
27626375	2	8	theme	human	269:273	arg1	physiology					275:284	human physiology	269:284	human physiology	269:284	Despite their central function in human physiology and although they are potential targets of therapeutic agents, there are no structures of human P2X receptors.
27626375	6	9	theme	competitive	1010:1020	arg1	antagonists					1022:1032	The competitive antagonists	1006:1032	The competitive antagonists TNP-ATP and A-317491	1006:1053	The competitive antagonists TNP-ATP and A-317491 stabilize the apo/resting state and reveal the interactions responsible for competitive inhibition.
27626375	6	9	theme	competitive	1010:1020	arg1	A-317491					1046:1053	A-317491	1046:1053	A-317491	1046:1053	The competitive antagonists TNP-ATP and A-317491 stabilize the apo/resting state and reveal the interactions responsible for competitive inhibition.
27626375	6	9	theme	competitive	1010:1020	arg1	TNP-ATP					1034:1040	TNP-ATP	1034:1040	TNP-ATP	1034:1040	The competitive antagonists TNP-ATP and A-317491 stabilize the apo/resting state and reveal the interactions responsible for competitive inhibition.
27626375	0	10	theme	antagonist	63:72	arg1	action					74:79	antagonist action	63:79	antagonist action	63:79	X-ray structures define human P2X(3) receptor gating cycle and antagonist action.
27626375	4	11	theme	crystal	608:614	arg1	structures					616:625	X-ray crystal structures	602:625	X-ray crystal structures of the human P2X3 receptor in apo/resting, agonist-bound/open-pore, agonist-bound/closed-pore/desensitized and antagonist-bound/closed states	602:767	Here we report X-ray crystal structures of the human P2X3 receptor in apo/resting, agonist-bound/open-pore, agonist-bound/closed-pore/desensitized and antagonist-bound/closed states.
27626375	3	12	theme	pore-forming	517:528	arg1	domains					544:550	the pore-forming transmembrane domains	513:550	the pore-forming transmembrane domains of these receptors	513:569	The mechanisms of receptor desensitization and ion permeation, principles of antagonism, and complete structures of the pore-forming transmembrane domains of these receptors remain unclear.
27626375	3	12	theme	pore-forming	517:528	arg1	receptors					561:569	these receptors	555:569	these receptors	555:569	The mechanisms of receptor desensitization and ion permeation, principles of antagonism, and complete structures of the pore-forming transmembrane domains of these receptors remain unclear.
27626375	2	13	from	targets	318:324	arg1	physiology					275:284	human physiology	269:284	human physiology	269:284	Despite their central function in human physiology and although they are potential targets of therapeutic agents, there are no structures of human P2X receptors.
27626375	3	14	theme	antagonism	474:483	arg1	mechanisms					401:410	The mechanisms	397:410	The mechanisms of receptor desensitization and ion permeation	397:457	The mechanisms of receptor desensitization and ion permeation, principles of antagonism, and complete structures of the pore-forming transmembrane domains of these receptors remain unclear.
27626375	3	14	theme	antagonism	474:483	arg1	principles					460:469	principles	460:469	principles of antagonism	460:483	The mechanisms of receptor desensitization and ion permeation, principles of antagonism, and complete structures of the pore-forming transmembrane domains of these receptors remain unclear.
27626375	3	14	theme	antagonism	474:483	arg1	structures					499:508	complete structures	490:508	complete structures of the pore-forming transmembrane domains of these receptors	490:569	The mechanisms of receptor desensitization and ion permeation, principles of antagonism, and complete structures of the pore-forming transmembrane domains of these receptors remain unclear.
27626375	4	15	theme	antagonist-bound/closed	738:760	arg1	states					762:767	apo/resting, agonist-bound/open-pore, agonist-bound/closed-pore/desensitized and antagonist-bound/closed states	657:767	apo/resting, agonist-bound/open-pore, agonist-bound/closed-pore/desensitized and antagonist-bound/closed states	657:767	Here we report X-ray crystal structures of the human P2X3 receptor in apo/resting, agonist-bound/open-pore, agonist-bound/closed-pore/desensitized and antagonist-bound/closed states.
27626375	5	16	theme	open	774:777	arg1	structure					785:793	The open state structure	770:793	The open state structure	770:793	The open state structure harbours an intracellular motif we term the 'cytoplasmic cap', which stabilizes the open state of the ion channel pore and creates lateral, phospholipid-lined cytoplasmic fenestrations for water and ion egress.
27626375	3	17	theme	ion	444:446	arg1	permeation					448:457	ion permeation	444:457	ion permeation	444:457	The mechanisms of receptor desensitization and ion permeation, principles of antagonism, and complete structures of the pore-forming transmembrane domains of these receptors remain unclear.
27626375	2	18	theme	central	249:255	arg1	function					257:264	their central function	243:264	their central function in human physiology	243:284	Despite their central function in human physiology and although they are potential targets of therapeutic agents, there are no structures of human P2X receptors.
27626375	4	19	theme	P2X3	640:643	arg1	receptor					645:652	the human P2X3 receptor	630:652	the human P2X3 receptor	630:652	Here we report X-ray crystal structures of the human P2X3 receptor in apo/resting, agonist-bound/open-pore, agonist-bound/closed-pore/desensitized and antagonist-bound/closed states.
27626375	5	20	theme	state	779:783	arg1	structure					785:793	The open state structure	770:793	The open state structure	770:793	The open state structure harbours an intracellular motif we term the 'cytoplasmic cap', which stabilizes the open state of the ion channel pore and creates lateral, phospholipid-lined cytoplasmic fenestrations for water and ion egress.
27626375	5	21	theme	cytoplasmic	840:850	arg1	cap					852:854	the 'cytoplasmic cap'	835:855	the 'cytoplasmic cap'	835:855	The open state structure harbours an intracellular motif we term the 'cytoplasmic cap', which stabilizes the open state of the ion channel pore and creates lateral, phospholipid-lined cytoplasmic fenestrations for water and ion egress.
27626375	6	22	theme	competitive	1131:1141	arg1	inhibition					1143:1152	competitive inhibition	1131:1152	competitive inhibition	1131:1152	The competitive antagonists TNP-ATP and A-317491 stabilize the apo/resting state and reveal the interactions responsible for competitive inhibition.
27626375	4	23	theme	human	634:638	arg1	receptor					645:652	the human P2X3 receptor	630:652	the human P2X3 receptor	630:652	Here we report X-ray crystal structures of the human P2X3 receptor in apo/resting, agonist-bound/open-pore, agonist-bound/closed-pore/desensitized and antagonist-bound/closed states.
27626375	3	24	theme	complete	490:497	arg1	structures					499:508	complete structures	490:508	complete structures of the pore-forming transmembrane domains of these receptors	490:569	The mechanisms of receptor desensitization and ion permeation, principles of antagonism, and complete structures of the pore-forming transmembrane domains of these receptors remain unclear.
27626375	5	25	dep	motif	821:825	arg1	term					830:833	term	830:833	term the 'cytoplasmic cap', which stabilizes the open state of the ion channel pore and creates lateral, phospholipid-lined cytoplasmic fenestrations for water and ion egress	830:1003	The open state structure harbours an intracellular motif we term the 'cytoplasmic cap', which stabilizes the open state of the ion channel pore and creates lateral, phospholipid-lined cytoplasmic fenestrations for water and ion egress.
27626375	5	26	theme	cytoplasmic	954:964	arg1	fenestrations					966:978	lateral, phospholipid-lined cytoplasmic fenestrations	926:978	lateral, phospholipid-lined cytoplasmic fenestrations for water and ion egress	926:1003	The open state structure harbours an intracellular motif we term the 'cytoplasmic cap', which stabilizes the open state of the ion channel pore and creates lateral, phospholipid-lined cytoplasmic fenestrations for water and ion egress.
27626375	0	27	theme	X-ray	0:4	arg1	structures					6:15	X-ray structures	0:15	X-ray structures	0:15	X-ray structures define human P2X(3) receptor gating cycle and antagonist action.
27626375	3	28	theme	domains	544:550	arg1	mechanisms					401:410	The mechanisms	397:410	The mechanisms of receptor desensitization and ion permeation	397:457	The mechanisms of receptor desensitization and ion permeation, principles of antagonism, and complete structures of the pore-forming transmembrane domains of these receptors remain unclear.
27626375	3	28	theme	domains	544:550	arg1	principles					460:469	principles	460:469	principles of antagonism	460:483	The mechanisms of receptor desensitization and ion permeation, principles of antagonism, and complete structures of the pore-forming transmembrane domains of these receptors remain unclear.
27626375	3	28	theme	domains	544:550	arg1	structures					499:508	complete structures	490:508	complete structures of the pore-forming transmembrane domains of these receptors	490:569	The mechanisms of receptor desensitization and ion permeation, principles of antagonism, and complete structures of the pore-forming transmembrane domains of these receptors remain unclear.
27626375	5	29	theme	open	879:882	arg1	state					884:888	the open state	875:888	the open state of the ion channel pore	875:912	The open state structure harbours an intracellular motif we term the 'cytoplasmic cap', which stabilizes the open state of the ion channel pore and creates lateral, phospholipid-lined cytoplasmic fenestrations for water and ion egress.
27626375	4	30	theme	receptor	645:652	arg1	structures					616:625	X-ray crystal structures	602:625	X-ray crystal structures of the human P2X3 receptor in apo/resting, agonist-bound/open-pore, agonist-bound/closed-pore/desensitized and antagonist-bound/closed states	602:767	Here we report X-ray crystal structures of the human P2X3 receptor in apo/resting, agonist-bound/open-pore, agonist-bound/closed-pore/desensitized and antagonist-bound/closed states.
27626375	0	31	theme	human	24:28	arg1	receptor					37:44	human P2X(3) receptor	24:44	human P2X(3) receptor gating cycle and antagonist action	24:79	X-ray structures define human P2X(3) receptor gating cycle and antagonist action.
27626375	6	32	theme	responsible	1115:1125	arg1	interactions					1102:1113	the interactions	1098:1113	the interactions responsible for competitive inhibition	1098:1152	The competitive antagonists TNP-ATP and A-317491 stabilize the apo/resting state and reveal the interactions responsible for competitive inhibition.
27626375	3	33	theme	transmembrane	530:542	arg1	domains					544:550	the pore-forming transmembrane domains	513:550	the pore-forming transmembrane domains of these receptors	513:569	The mechanisms of receptor desensitization and ion permeation, principles of antagonism, and complete structures of the pore-forming transmembrane domains of these receptors remain unclear.
27626375	3	33	theme	transmembrane	530:542	arg1	receptors					561:569	these receptors	555:569	these receptors	555:569	The mechanisms of receptor desensitization and ion permeation, principles of antagonism, and complete structures of the pore-forming transmembrane domains of these receptors remain unclear.
27626375	2	34	theme	receptors	386:394	arg1	structures					362:371	no structures	359:371	no structures of human P2X receptors	359:394	Despite their central function in human physiology and although they are potential targets of therapeutic agents, there are no structures of human P2X receptors.
27626375	5	35	theme	lateral	926:932	arg1	fenestrations					966:978	lateral, phospholipid-lined cytoplasmic fenestrations	926:978	lateral, phospholipid-lined cytoplasmic fenestrations for water and ion egress	926:1003	The open state structure harbours an intracellular motif we term the 'cytoplasmic cap', which stabilizes the open state of the ion channel pore and creates lateral, phospholipid-lined cytoplasmic fenestrations for water and ion egress.
27626375	1	36	contain	have	162:165	arg2	roles					177:181	important roles	167:181	important roles	167:181	P2X receptors are trimeric, non-selective cation channels activated by ATP that have important roles in the cardiovascular, neuronal and immune systems.
27626375	1	36	contain	have	162:165	arg1	channels					131:138	trimeric, non-selective cation channels	100:138	trimeric, non-selective cation channels activated by ATP that have important roles in the cardiovascular, neuronal and immune systems	100:232	P2X receptors are trimeric, non-selective cation channels activated by ATP that have important roles in the cardiovascular, neuronal and immune systems.
27626375	1	36	contain	have	162:165	arg1	receptors					86:94	P2X receptors	82:94	P2X receptors	82:94	P2X receptors are trimeric, non-selective cation channels activated by ATP that have important roles in the cardiovascular, neuronal and immune systems.
27626375	1	37	theme	P2X	82:84	arg1	receptors					86:94	P2X receptors	82:94	P2X receptors	82:94	P2X receptors are trimeric, non-selective cation channels activated by ATP that have important roles in the cardiovascular, neuronal and immune systems.
27626375	1	37	theme	P2X	82:84	arg1	channels					131:138	trimeric, non-selective cation channels	100:138	trimeric, non-selective cation channels activated by ATP that have important roles in the cardiovascular, neuronal and immune systems	100:232	P2X receptors are trimeric, non-selective cation channels activated by ATP that have important roles in the cardiovascular, neuronal and immune systems.
27626375	4	38	from	structures	616:625	arg1	states					762:767	apo/resting, agonist-bound/open-pore, agonist-bound/closed-pore/desensitized and antagonist-bound/closed states	657:767	apo/resting, agonist-bound/open-pore, agonist-bound/closed-pore/desensitized and antagonist-bound/closed states	657:767	Here we report X-ray crystal structures of the human P2X3 receptor in apo/resting, agonist-bound/open-pore, agonist-bound/closed-pore/desensitized and antagonist-bound/closed states.
27626375	2	39	theme	P2X	382:384	arg1	receptors					386:394	human P2X receptors	376:394	human P2X receptors	376:394	Despite their central function in human physiology and although they are potential targets of therapeutic agents, there are no structures of human P2X receptors.
27626375	4	40	theme	agonist-bound/closed-pore/desensitized	695:732	arg1	states					762:767	apo/resting, agonist-bound/open-pore, agonist-bound/closed-pore/desensitized and antagonist-bound/closed states	657:767	apo/resting, agonist-bound/open-pore, agonist-bound/closed-pore/desensitized and antagonist-bound/closed states	657:767	Here we report X-ray crystal structures of the human P2X3 receptor in apo/resting, agonist-bound/open-pore, agonist-bound/closed-pore/desensitized and antagonist-bound/closed states.
27626375	3	41	theme	receptor	415:422	arg1	desensitization					424:438	receptor desensitization	415:438	receptor desensitization	415:438	The mechanisms of receptor desensitization and ion permeation, principles of antagonism, and complete structures of the pore-forming transmembrane domains of these receptors remain unclear.
27626375	2	42	theme	human	376:380	arg1	receptors					386:394	human P2X receptors	376:394	human P2X receptors	376:394	Despite their central function in human physiology and although they are potential targets of therapeutic agents, there are no structures of human P2X receptors.
27626375	0	43	theme	P2X	30:32	arg1	receptor					37:44	human P2X(3) receptor	24:44	human P2X(3) receptor gating cycle and antagonist action	24:79	X-ray structures define human P2X(3) receptor gating cycle and antagonist action.
27626375	7	44	theme	P2X	1231:1233	arg1	gating					1244:1249	P2X receptor gating	1231:1249	P2X receptor gating	1231:1249	These structures illuminate the conformational rearrangements that underlie P2X receptor gating and provide a foundation for the development of new pharmacological agents.
27626375	4	45	theme	X-ray	602:606	arg1	structures					616:625	X-ray crystal structures	602:625	X-ray crystal structures of the human P2X3 receptor in apo/resting, agonist-bound/open-pore, agonist-bound/closed-pore/desensitized and antagonist-bound/closed states	602:767	Here we report X-ray crystal structures of the human P2X3 receptor in apo/resting, agonist-bound/open-pore, agonist-bound/closed-pore/desensitized and antagonist-bound/closed states.
27626375	3	46	theme	desensitization	424:438	arg1	mechanisms					401:410	The mechanisms	397:410	The mechanisms of receptor desensitization and ion permeation	397:457	The mechanisms of receptor desensitization and ion permeation, principles of antagonism, and complete structures of the pore-forming transmembrane domains of these receptors remain unclear.
27626375	3	46	theme	desensitization	424:438	arg1	principles					460:469	principles	460:469	principles of antagonism	460:483	The mechanisms of receptor desensitization and ion permeation, principles of antagonism, and complete structures of the pore-forming transmembrane domains of these receptors remain unclear.
27626375	3	46	theme	desensitization	424:438	arg1	structures					499:508	complete structures	490:508	complete structures of the pore-forming transmembrane domains of these receptors	490:569	The mechanisms of receptor desensitization and ion permeation, principles of antagonism, and complete structures of the pore-forming transmembrane domains of these receptors remain unclear.
27626375	6	47	theme	apo/resting	1069:1079	arg1	state					1081:1085	the apo/resting state	1065:1085	the apo/resting state	1065:1085	The competitive antagonists TNP-ATP and A-317491 stabilize the apo/resting state and reveal the interactions responsible for competitive inhibition.
27626375	3	48	theme	receptors	561:569	arg1	domains					544:550	the pore-forming transmembrane domains	513:550	the pore-forming transmembrane domains of these receptors	513:569	The mechanisms of receptor desensitization and ion permeation, principles of antagonism, and complete structures of the pore-forming transmembrane domains of these receptors remain unclear.
27626375	3	48	theme	receptors	561:569	arg1	receptors					561:569	these receptors	555:569	these receptors	555:569	The mechanisms of receptor desensitization and ion permeation, principles of antagonism, and complete structures of the pore-forming transmembrane domains of these receptors remain unclear.
27626375	2	49	theme	potential	308:316	arg1	they					299:302	they	299:302	they	299:302	Despite their central function in human physiology and although they are potential targets of therapeutic agents, there are no structures of human P2X receptors.
27626375	2	49	theme	potential	308:316	arg1	targets					318:324	potential targets	308:324	potential targets of therapeutic agents	308:346	Despite their central function in human physiology and although they are potential targets of therapeutic agents, there are no structures of human P2X receptors.
27626375	7	50	theme	receptor	1235:1242	arg1	gating					1244:1249	P2X receptor gating	1231:1249	P2X receptor gating	1231:1249	These structures illuminate the conformational rearrangements that underlie P2X receptor gating and provide a foundation for the development of new pharmacological agents.
27626375	4	51	theme	apo/resting	657:667	arg1	states					762:767	apo/resting, agonist-bound/open-pore, agonist-bound/closed-pore/desensitized and antagonist-bound/closed states	657:767	apo/resting, agonist-bound/open-pore, agonist-bound/closed-pore/desensitized and antagonist-bound/closed states	657:767	Here we report X-ray crystal structures of the human P2X3 receptor in apo/resting, agonist-bound/open-pore, agonist-bound/closed-pore/desensitized and antagonist-bound/closed states.
27626375	1	52	theme	trimeric	100:107	arg1	receptors					86:94	P2X receptors	82:94	P2X receptors	82:94	P2X receptors are trimeric, non-selective cation channels activated by ATP that have important roles in the cardiovascular, neuronal and immune systems.
27626375	1	52	theme	trimeric	100:107	arg1	channels					131:138	trimeric, non-selective cation channels	100:138	trimeric, non-selective cation channels activated by ATP that have important roles in the cardiovascular, neuronal and immune systems	100:232	P2X receptors are trimeric, non-selective cation channels activated by ATP that have important roles in the cardiovascular, neuronal and immune systems.
27626375	1	53	theme	cardiovascular	190:203	arg1	systems					226:232	the cardiovascular, neuronal and immune systems	186:232	the cardiovascular, neuronal and immune systems	186:232	P2X receptors are trimeric, non-selective cation channels activated by ATP that have important roles in the cardiovascular, neuronal and immune systems.
27626375	5	54	dep	lateral	926:932	arg1	phospholipid-lined					935:952	phospholipid-lined	935:952	phospholipid-lined	935:952	The open state structure harbours an intracellular motif we term the 'cytoplasmic cap', which stabilizes the open state of the ion channel pore and creates lateral, phospholipid-lined cytoplasmic fenestrations for water and ion egress.
27626375	1	55	theme	cation	124:129	arg1	receptors					86:94	P2X receptors	82:94	P2X receptors	82:94	P2X receptors are trimeric, non-selective cation channels activated by ATP that have important roles in the cardiovascular, neuronal and immune systems.
27626375	1	55	theme	cation	124:129	arg1	channels					131:138	trimeric, non-selective cation channels	100:138	trimeric, non-selective cation channels activated by ATP that have important roles in the cardiovascular, neuronal and immune systems	100:232	P2X receptors are trimeric, non-selective cation channels activated by ATP that have important roles in the cardiovascular, neuronal and immune systems.
27626375	3	56	theme	permeation	448:457	arg1	mechanisms					401:410	The mechanisms	397:410	The mechanisms of receptor desensitization and ion permeation	397:457	The mechanisms of receptor desensitization and ion permeation, principles of antagonism, and complete structures of the pore-forming transmembrane domains of these receptors remain unclear.
27626375	3	56	theme	permeation	448:457	arg1	principles					460:469	principles	460:469	principles of antagonism	460:483	The mechanisms of receptor desensitization and ion permeation, principles of antagonism, and complete structures of the pore-forming transmembrane domains of these receptors remain unclear.
27626375	3	56	theme	permeation	448:457	arg1	structures					499:508	complete structures	490:508	complete structures of the pore-forming transmembrane domains of these receptors	490:569	The mechanisms of receptor desensitization and ion permeation, principles of antagonism, and complete structures of the pore-forming transmembrane domains of these receptors remain unclear.
27626375	7	57	theme	new	1299:1301	arg1	agents					1319:1324	new pharmacological agents	1299:1324	new pharmacological agents	1299:1324	These structures illuminate the conformational rearrangements that underlie P2X receptor gating and provide a foundation for the development of new pharmacological agents.
27626375	5	58	theme	channel	901:907	arg1	pore					909:912	the ion channel pore	893:912	the ion channel pore	893:912	The open state structure harbours an intracellular motif we term the 'cytoplasmic cap', which stabilizes the open state of the ion channel pore and creates lateral, phospholipid-lined cytoplasmic fenestrations for water and ion egress.
27626375	1	59	theme	important	167:175	arg1	roles					177:181	important roles	167:181	important roles	167:181	P2X receptors are trimeric, non-selective cation channels activated by ATP that have important roles in the cardiovascular, neuronal and immune systems.
27626375	5	60	theme	ion	897:899	arg1	pore					909:912	the ion channel pore	893:912	the ion channel pore	893:912	The open state structure harbours an intracellular motif we term the 'cytoplasmic cap', which stabilizes the open state of the ion channel pore and creates lateral, phospholipid-lined cytoplasmic fenestrations for water and ion egress.
27626375	2	61	from	function	257:264	arg1	physiology					275:284	human physiology	269:284	human physiology	269:284	Despite their central function in human physiology and although they are potential targets of therapeutic agents, there are no structures of human P2X receptors.
27626375	1	62	theme	neuronal	206:213	arg1	systems					226:232	the cardiovascular, neuronal and immune systems	186:232	the cardiovascular, neuronal and immune systems	186:232	P2X receptors are trimeric, non-selective cation channels activated by ATP that have important roles in the cardiovascular, neuronal and immune systems.
27626375	7	63	theme	pharmacological	1303:1317	arg1	agents					1319:1324	new pharmacological agents	1299:1324	new pharmacological agents	1299:1324	These structures illuminate the conformational rearrangements that underlie P2X receptor gating and provide a foundation for the development of new pharmacological agents.
27626375	5	64	theme	ion	994:996	arg1	egress					998:1003	ion egress	994:1003	ion egress	994:1003	The open state structure harbours an intracellular motif we term the 'cytoplasmic cap', which stabilizes the open state of the ion channel pore and creates lateral, phospholipid-lined cytoplasmic fenestrations for water and ion egress.
27626375	2	65	theme	agents	341:346	arg1	function					257:264	their central function	243:264	their central function in human physiology	243:284	Despite their central function in human physiology and although they are potential targets of therapeutic agents, there are no structures of human P2X receptors.
27626375	2	65	theme	agents	341:346	arg1	they					299:302	they	299:302	they	299:302	Despite their central function in human physiology and although they are potential targets of therapeutic agents, there are no structures of human P2X receptors.
27626375	2	65	theme	agents	341:346	arg1	targets					318:324	potential targets	308:324	potential targets of therapeutic agents	308:346	Despite their central function in human physiology and although they are potential targets of therapeutic agents, there are no structures of human P2X receptors.
27626375	7	66	theme	agents	1319:1324	arg1	development					1284:1294	the development	1280:1294	the development of new pharmacological agents	1280:1324	These structures illuminate the conformational rearrangements that underlie P2X receptor gating and provide a foundation for the development of new pharmacological agents.
29224781	2	0	theme	protein	504:510	arg1	cleavage					466:473	the non-amyloidogenic α-secretase cleavage	432:473	the non-amyloidogenic α-secretase cleavage of the Alzheimer's precursor protein (APP)	432:516	Among ADAM family members, ADAM10 stands out as particularly important because it is both responsible for regulated proteolysis of Notch receptors and catalyzes the non-amyloidogenic α-secretase cleavage of the Alzheimer's precursor protein (APP).
29224781	5	1	theme	antibody	903:910	arg1	domain					933:938	a modulatory antibody to the cysteine-rich domain	890:938	a modulatory antibody to the cysteine-rich domain	890:938	Binding of a modulatory antibody to the cysteine-rich domain liberates the catalytic domain from autoinhibition, enhancing enzymatic activity toward a peptide substrate.
29224781	1	2	theme	protein	243:249	arg1	processes					260:268	protein turnover processes	243:268	protein turnover processes	243:268	Cleavage of membrane-anchored proteins by ADAM (a disintegrin and metalloproteinase) endopeptidases plays a key role in a wide variety of biological signal transduction and protein turnover processes.
29224781	2	3	theme	precursor	494:502	arg1	APP					513:515	APP	513:515	APP	513:515	Among ADAM family members, ADAM10 stands out as particularly important because it is both responsible for regulated proteolysis of Notch receptors and catalyzes the non-amyloidogenic α-secretase cleavage of the Alzheimer's precursor protein (APP).
29224781	2	3	theme	precursor	494:502	arg1	protein					504:510	the Alzheimer's precursor protein	478:510	the Alzheimer's precursor protein (APP)	478:516	Among ADAM family members, ADAM10 stands out as particularly important because it is both responsible for regulated proteolysis of Notch receptors and catalyzes the non-amyloidogenic α-secretase cleavage of the Alzheimer's precursor protein (APP).
29224781	3	4	theme	enzyme	670:675	arg1	site					684:687	the enzyme active site	666:687	the enzyme active site	666:687	We present here the X-ray crystal structure of the ADAM10 ectodomain, which, together with biochemical and cellular studies, reveals how access to the enzyme active site is regulated.
29224781	5	5	theme	to the	912:917	arg1	domain					933:938	a modulatory antibody to the cysteine-rich domain	890:938	a modulatory antibody to the cysteine-rich domain	890:938	Binding of a modulatory antibody to the cysteine-rich domain liberates the catalytic domain from autoinhibition, enhancing enzymatic activity toward a peptide substrate.
29224781	1	6	theme	turnover	251:258	arg1	processes					260:268	protein turnover processes	243:268	protein turnover processes	243:268	Cleavage of membrane-anchored proteins by ADAM (a disintegrin and metalloproteinase) endopeptidases plays a key role in a wide variety of biological signal transduction and protein turnover processes.
29224781	3	7	theme	active	677:682	arg1	site					684:687	the enzyme active site	666:687	the enzyme active site	666:687	We present here the X-ray crystal structure of the ADAM10 ectodomain, which, together with biochemical and cellular studies, reveals how access to the enzyme active site is regulated.
29224781	3	8	theme	X-ray	539:543	arg1	structure					553:561	the X-ray crystal structure	535:561	the X-ray crystal structure	535:561	We present here the X-ray crystal structure of the ADAM10 ectodomain, which, together with biochemical and cellular studies, reveals how access to the enzyme active site is regulated.
29224781	4	9	theme	unanticipated	724:736	arg1	architecture					738:749	an unanticipated architecture	721:749	an unanticipated architecture in which the C-terminal cysteine-rich domain partially occludes the enzyme active site, preventing unfettered substrate access	721:876	The enzyme adopts an unanticipated architecture in which the C-terminal cysteine-rich domain partially occludes the enzyme active site, preventing unfettered substrate access.
29224781	1	10	theme	processes	260:268	arg1	transduction					226:237	biological signal transduction	208:237	biological signal transduction	208:237	Cleavage of membrane-anchored proteins by ADAM (a disintegrin and metalloproteinase) endopeptidases plays a key role in a wide variety of biological signal transduction and protein turnover processes.
29224781	1	10	theme	processes	260:268	arg1	processes					260:268	protein turnover processes	243:268	protein turnover processes	243:268	Cleavage of membrane-anchored proteins by ADAM (a disintegrin and metalloproteinase) endopeptidases plays a key role in a wide variety of biological signal transduction and protein turnover processes.
29224781	1	10	theme	processes	260:268	arg1	variety					197:203	a wide variety	190:203	a wide variety of biological signal transduction and protein turnover processes	190:268	Cleavage of membrane-anchored proteins by ADAM (a disintegrin and metalloproteinase) endopeptidases plays a key role in a wide variety of biological signal transduction and protein turnover processes.
29224781	5	11	theme	catalytic	954:962	arg1	domain					964:969	the catalytic domain	950:969	the catalytic domain from autoinhibition	950:989	Binding of a modulatory antibody to the cysteine-rich domain liberates the catalytic domain from autoinhibition, enhancing enzymatic activity toward a peptide substrate.
29224781	3	12	theme	crystal	545:551	arg1	structure					553:561	the X-ray crystal structure	535:561	the X-ray crystal structure	535:561	We present here the X-ray crystal structure of the ADAM10 ectodomain, which, together with biochemical and cellular studies, reveals how access to the enzyme active site is regulated.
29224781	2	13	theme	family	282:287	arg1	members					289:295	ADAM family members	277:295	ADAM family members	277:295	Among ADAM family members, ADAM10 stands out as particularly important because it is both responsible for regulated proteolysis of Notch receptors and catalyzes the non-amyloidogenic α-secretase cleavage of the Alzheimer's precursor protein (APP).
29224781	2	14	theme	ADAM	277:280	arg1	members					289:295	ADAM family members	277:295	ADAM family members	277:295	Among ADAM family members, ADAM10 stands out as particularly important because it is both responsible for regulated proteolysis of Notch receptors and catalyzes the non-amyloidogenic α-secretase cleavage of the Alzheimer's precursor protein (APP).
29224781	6	15	theme	ADAM	1110:1113	arg1	activity					1115:1122	ADAM activity	1110:1122	ADAM activity	1110:1122	Together, these studies reveal a mechanism for regulation of ADAM activity and offer a roadmap for its modulation.
29224781	2	16	theme	α-secretase	454:464	arg1	cleavage					466:473	the non-amyloidogenic α-secretase cleavage	432:473	the non-amyloidogenic α-secretase cleavage of the Alzheimer's precursor protein (APP)	432:516	Among ADAM family members, ADAM10 stands out as particularly important because it is both responsible for regulated proteolysis of Notch receptors and catalyzes the non-amyloidogenic α-secretase cleavage of the Alzheimer's precursor protein (APP).
29224781	6	17	theme	activity	1115:1122	arg1	regulation					1096:1105	regulation	1096:1105	regulation of ADAM activity	1096:1122	Together, these studies reveal a mechanism for regulation of ADAM activity and offer a roadmap for its modulation.
29224781	1	18	theme	key	178:180	arg1	role					182:185	a key role	176:185	a key role	176:185	Cleavage of membrane-anchored proteins by ADAM (a disintegrin and metalloproteinase) endopeptidases plays a key role in a wide variety of biological signal transduction and protein turnover processes.
29224781	4	19	theme	substrate	861:869	arg1	access					871:876	unfettered substrate access	850:876	unfettered substrate access	850:876	The enzyme adopts an unanticipated architecture in which the C-terminal cysteine-rich domain partially occludes the enzyme active site, preventing unfettered substrate access.
29224781	1	20	theme	membrane-anchored	82:98	arg1	proteins					100:107	membrane-anchored proteins	82:107	membrane-anchored proteins	82:107	Cleavage of membrane-anchored proteins by ADAM (a disintegrin and metalloproteinase) endopeptidases plays a key role in a wide variety of biological signal transduction and protein turnover processes.
29224781	2	21	theme	regulated	377:385	arg1	proteolysis					387:397	regulated proteolysis	377:397	regulated proteolysis of Notch receptors	377:416	Among ADAM family members, ADAM10 stands out as particularly important because it is both responsible for regulated proteolysis of Notch receptors and catalyzes the non-amyloidogenic α-secretase cleavage of the Alzheimer's precursor protein (APP).
29224781	0	22	theme	Structural	0:9	arg1	Basis					11:15	Structural Basis	0:15	Structural Basis for Regulated Proteolysis by the α-Secretase ADAM10	0:67	Structural Basis for Regulated Proteolysis by the α-Secretase ADAM10.
29224781	4	23	theme	unfettered	850:859	arg1	access					871:876	unfettered substrate access	850:876	unfettered substrate access	850:876	The enzyme adopts an unanticipated architecture in which the C-terminal cysteine-rich domain partially occludes the enzyme active site, preventing unfettered substrate access.
29224781	1	24	theme	proteins	100:107	arg1	Cleavage					70:77	Cleavage	70:77	Cleavage of membrane-anchored proteins by ADAM (a disintegrin and metalloproteinase) endopeptidases	70:168	Cleavage of membrane-anchored proteins by ADAM (a disintegrin and metalloproteinase) endopeptidases plays a key role in a wide variety of biological signal transduction and protein turnover processes.
29224781	0	25	theme	Regulated	21:29	arg1	Proteolysis					31:41	Regulated Proteolysis	21:41	Regulated Proteolysis by the α-Secretase ADAM10	21:67	Structural Basis for Regulated Proteolysis by the α-Secretase ADAM10.
29224781	2	26	dep	responsible	361:371	arg1	both					356:359	both	356:359	both	356:359	Among ADAM family members, ADAM10 stands out as particularly important because it is both responsible for regulated proteolysis of Notch receptors and catalyzes the non-amyloidogenic α-secretase cleavage of the Alzheimer's precursor protein (APP).
29224781	1	27	theme	ADAM	112:115	arg1	endopeptidases					155:168	ADAM (a disintegrin and metalloproteinase) endopeptidases	112:168	ADAM (a disintegrin and metalloproteinase) endopeptidases	112:168	Cleavage of membrane-anchored proteins by ADAM (a disintegrin and metalloproteinase) endopeptidases plays a key role in a wide variety of biological signal transduction and protein turnover processes.
29224781	1	28	theme	wide	192:195	arg1	transduction					226:237	biological signal transduction	208:237	biological signal transduction	208:237	Cleavage of membrane-anchored proteins by ADAM (a disintegrin and metalloproteinase) endopeptidases plays a key role in a wide variety of biological signal transduction and protein turnover processes.
29224781	1	28	theme	wide	192:195	arg1	processes					260:268	protein turnover processes	243:268	protein turnover processes	243:268	Cleavage of membrane-anchored proteins by ADAM (a disintegrin and metalloproteinase) endopeptidases plays a key role in a wide variety of biological signal transduction and protein turnover processes.
29224781	1	28	theme	wide	192:195	arg1	variety					197:203	a wide variety	190:203	a wide variety of biological signal transduction and protein turnover processes	190:268	Cleavage of membrane-anchored proteins by ADAM (a disintegrin and metalloproteinase) endopeptidases plays a key role in a wide variety of biological signal transduction and protein turnover processes.
29224781	4	29	theme	enzyme	819:824	arg1	site					833:836	the enzyme active site	815:836	the enzyme active site	815:836	The enzyme adopts an unanticipated architecture in which the C-terminal cysteine-rich domain partially occludes the enzyme active site, preventing unfettered substrate access.
29224781	2	30	theme	receptors	408:416	arg1	proteolysis					387:397	regulated proteolysis	377:397	regulated proteolysis of Notch receptors	377:416	Among ADAM family members, ADAM10 stands out as particularly important because it is both responsible for regulated proteolysis of Notch receptors and catalyzes the non-amyloidogenic α-secretase cleavage of the Alzheimer's precursor protein (APP).
29224781	3	31	theme	cellular	626:633	arg1	studies					635:641	biochemical and cellular studies	610:641	biochemical and cellular studies	610:641	We present here the X-ray crystal structure of the ADAM10 ectodomain, which, together with biochemical and cellular studies, reveals how access to the enzyme active site is regulated.
29224781	2	32	theme	non-amyloidogenic	436:452	arg1	cleavage					466:473	the non-amyloidogenic α-secretase cleavage	432:473	the non-amyloidogenic α-secretase cleavage of the Alzheimer's precursor protein (APP)	432:516	Among ADAM family members, ADAM10 stands out as particularly important because it is both responsible for regulated proteolysis of Notch receptors and catalyzes the non-amyloidogenic α-secretase cleavage of the Alzheimer's precursor protein (APP).
29224781	2	33	theme	Notch	402:406	arg1	receptors					408:416	Notch receptors	402:416	Notch receptors	402:416	Among ADAM family members, ADAM10 stands out as particularly important because it is both responsible for regulated proteolysis of Notch receptors and catalyzes the non-amyloidogenic α-secretase cleavage of the Alzheimer's precursor protein (APP).
29224781	0	34	theme	α-Secretase	50:60	arg1	ADAM10					62:67	the α-Secretase ADAM10	46:67	the α-Secretase ADAM10	46:67	Structural Basis for Regulated Proteolysis by the α-Secretase ADAM10.
29224781	3	35	theme	ectodomain	577:586	arg1	structure					553:561	the X-ray crystal structure	535:561	the X-ray crystal structure	535:561	We present here the X-ray crystal structure of the ADAM10 ectodomain, which, together with biochemical and cellular studies, reveals how access to the enzyme active site is regulated.
29224781	5	36	theme	cysteine-rich	919:931	arg1	domain					933:938	a modulatory antibody to the cysteine-rich domain	890:938	a modulatory antibody to the cysteine-rich domain	890:938	Binding of a modulatory antibody to the cysteine-rich domain liberates the catalytic domain from autoinhibition, enhancing enzymatic activity toward a peptide substrate.
29224781	4	37	theme	active	826:831	arg1	site					833:836	the enzyme active site	815:836	the enzyme active site	815:836	The enzyme adopts an unanticipated architecture in which the C-terminal cysteine-rich domain partially occludes the enzyme active site, preventing unfettered substrate access.
29224781	5	38	theme	domain	933:938	arg1	Binding					879:885	Binding	879:885	Binding of a modulatory antibody to the cysteine-rich domain	879:938	Binding of a modulatory antibody to the cysteine-rich domain liberates the catalytic domain from autoinhibition, enhancing enzymatic activity toward a peptide substrate.
29224781	3	39	theme	biochemical	610:620	arg1	studies					635:641	biochemical and cellular studies	610:641	biochemical and cellular studies	610:641	We present here the X-ray crystal structure of the ADAM10 ectodomain, which, together with biochemical and cellular studies, reveals how access to the enzyme active site is regulated.
29224781	5	40	from	autoinhibition	976:989	arg1	domain					964:969	the catalytic domain	950:969	the catalytic domain from autoinhibition	950:989	Binding of a modulatory antibody to the cysteine-rich domain liberates the catalytic domain from autoinhibition, enhancing enzymatic activity toward a peptide substrate.
29224781	1	41	theme	biological	208:217	arg1	transduction					226:237	biological signal transduction	208:237	biological signal transduction	208:237	Cleavage of membrane-anchored proteins by ADAM (a disintegrin and metalloproteinase) endopeptidases plays a key role in a wide variety of biological signal transduction and protein turnover processes.
29224781	4	42	theme	C-terminal	764:773	arg1	domain					789:794	the C-terminal cysteine-rich domain	760:794	the C-terminal cysteine-rich domain	760:794	The enzyme adopts an unanticipated architecture in which the C-terminal cysteine-rich domain partially occludes the enzyme active site, preventing unfettered substrate access.
29224781	4	43	theme	cysteine-rich	775:787	arg1	domain					789:794	the C-terminal cysteine-rich domain	760:794	the C-terminal cysteine-rich domain	760:794	The enzyme adopts an unanticipated architecture in which the C-terminal cysteine-rich domain partially occludes the enzyme active site, preventing unfettered substrate access.
29224781	5	44	theme	modulatory	892:901	arg1	domain					933:938	a modulatory antibody to the cysteine-rich domain	890:938	a modulatory antibody to the cysteine-rich domain	890:938	Binding of a modulatory antibody to the cysteine-rich domain liberates the catalytic domain from autoinhibition, enhancing enzymatic activity toward a peptide substrate.
29224781	1	45	theme	signal	219:224	arg1	transduction					226:237	biological signal transduction	208:237	biological signal transduction	208:237	Cleavage of membrane-anchored proteins by ADAM (a disintegrin and metalloproteinase) endopeptidases plays a key role in a wide variety of biological signal transduction and protein turnover processes.
29224781	5	46	theme	enzymatic	1002:1010	arg1	activity					1012:1019	enzymatic activity	1002:1019	enzymatic activity toward a peptide substrate	1002:1046	Binding of a modulatory antibody to the cysteine-rich domain liberates the catalytic domain from autoinhibition, enhancing enzymatic activity toward a peptide substrate.
29224781	5	47	theme	peptide	1030:1036	arg1	substrate					1038:1046	a peptide substrate	1028:1046	a peptide substrate	1028:1046	Binding of a modulatory antibody to the cysteine-rich domain liberates the catalytic domain from autoinhibition, enhancing enzymatic activity toward a peptide substrate.
29224781	1	48	theme	transduction	226:237	arg1	transduction					226:237	biological signal transduction	208:237	biological signal transduction	208:237	Cleavage of membrane-anchored proteins by ADAM (a disintegrin and metalloproteinase) endopeptidases plays a key role in a wide variety of biological signal transduction and protein turnover processes.
29224781	1	48	theme	transduction	226:237	arg1	processes					260:268	protein turnover processes	243:268	protein turnover processes	243:268	Cleavage of membrane-anchored proteins by ADAM (a disintegrin and metalloproteinase) endopeptidases plays a key role in a wide variety of biological signal transduction and protein turnover processes.
29224781	1	48	theme	transduction	226:237	arg1	variety					197:203	a wide variety	190:203	a wide variety of biological signal transduction and protein turnover processes	190:268	Cleavage of membrane-anchored proteins by ADAM (a disintegrin and metalloproteinase) endopeptidases plays a key role in a wide variety of biological signal transduction and protein turnover processes.
29224781	1	49	dep	ADAM	112:115	arg1	disintegrin					120:130	a disintegrin	118:130	a disintegrin	118:130	Cleavage of membrane-anchored proteins by ADAM (a disintegrin and metalloproteinase) endopeptidases plays a key role in a wide variety of biological signal transduction and protein turnover processes.
29224781	1	49	dep	ADAM	112:115	arg1	metalloproteinase					136:152	metalloproteinase	136:152	metalloproteinase	136:152	Cleavage of membrane-anchored proteins by ADAM (a disintegrin and metalloproteinase) endopeptidases plays a key role in a wide variety of biological signal transduction and protein turnover processes.
24047895	10	0	from	GGTs	1609:1612	arg1	absent					1585:1590	absent	1585:1590	absent	1585:1590	These are absent in the bacterial GGTs.
24047895	8	1	theme	several	1293:1299	arg1	counterparts					1311:1322	several bacterial counterparts	1293:1322	several bacterial counterparts	1293:1322	Compared with several bacterial counterparts, the lid loop in the crystal structure of hGGT1 adopts an open conformation that allows greater access to the active site.
24047895	8	2	from	loop	1333:1336	arg1	structure					1353:1361	the crystal structure	1341:1361	the crystal structure of hGGT1	1341:1370	Compared with several bacterial counterparts, the lid loop in the crystal structure of hGGT1 adopts an open conformation that allows greater access to the active site.
24047895	1	3	theme	glutathione	272:282	arg1	bond					264:267	the γ-glutamyl bond	249:267	the γ-glutamyl bond of glutathione and other γ-glutamyl compounds	249:313	The enzyme γ-glutamyltranspeptidase 1 (GGT1) is a conserved member of the N-terminal nucleophile hydrolase family that cleaves the γ-glutamyl bond of glutathione and other γ-glutamyl compounds.
24047895	7	4	theme	hGGT1	1037:1041	arg1	architecture					1021:1032	the active site architecture	1005:1032	the active site architecture of hGGT1	1005:1041	Comparisons of the active site architecture of hGGT1 with those of its bacterial orthologs highlight key differences in the residues responsible for substrate binding, including a bimodal switch in the orientation of the catalytic nucleophile (Thr-381) that is unique to the human enzyme.
24047895	1	5	theme	conserved	172:180	arg1	member					182:187	a conserved member	170:187	a conserved member of the N-terminal nucleophile hydrolase family that cleaves the γ-glutamyl bond of glutathione and other γ-glutamyl compounds	170:313	The enzyme γ-glutamyltranspeptidase 1 (GGT1) is a conserved member of the N-terminal nucleophile hydrolase family that cleaves the γ-glutamyl bond of glutathione and other γ-glutamyl compounds.
24047895	1	5	theme	conserved	172:180	arg1	γ-glutamyltranspeptidase					133:156	The enzyme γ-glutamyltranspeptidase 1	122:158	The enzyme γ-glutamyltranspeptidase 1 (GGT1)	122:165	The enzyme γ-glutamyltranspeptidase 1 (GGT1) is a conserved member of the N-terminal nucleophile hydrolase family that cleaves the γ-glutamyl bond of glutathione and other γ-glutamyl compounds.
24047895	7	6	theme	architecture	1021:1032	arg1	Comparisons					990:1000	Comparisons	990:1000	Comparisons of the active site architecture of hGGT1 with those of its bacterial orthologs	990:1079	Comparisons of the active site architecture of hGGT1 with those of its bacterial orthologs highlight key differences in the residues responsible for substrate binding, including a bimodal switch in the orientation of the catalytic nucleophile (Thr-381) that is unique to the human enzyme.
24047895	3	7	theme	disease	564:570	arg1	potentiator					526:536	a potentiator	524:536	a potentiator of asthma, cardiovascular disease, and cancer	524:582	Expression of GGT1 has been implicated as a potentiator of asthma, cardiovascular disease, and cancer.
24047895	3	7	theme	disease	564:570	arg1	Expression					482:491	Expression	482:491	Expression of GGT1	482:499	Expression of GGT1 has been implicated as a potentiator of asthma, cardiovascular disease, and cancer.
24047895	4	8	theme	inhibitors	618:627	arg1	design					598:603	The rational design	585:603	The rational design of effective inhibitors of human GGT1 (hGGT1)	585:649	The rational design of effective inhibitors of human GGT1 (hGGT1) has been delayed by the lack of a reliable structural model.
24047895	7	9	theme	active	1009:1014	arg1	architecture					1021:1032	the active site architecture	1005:1032	the active site architecture of hGGT1	1005:1041	Comparisons of the active site architecture of hGGT1 with those of its bacterial orthologs highlight key differences in the residues responsible for substrate binding, including a bimodal switch in the orientation of the catalytic nucleophile (Thr-381) that is unique to the human enzyme.
24047895	5	10	theme	due	796:798	arg1	use					792:794	limited use	784:794	limited use due to differences in the catalytic behavior of bacterial and mammalian GGTs	784:871	The available crystal structures of several bacterial GGTs have been of limited use due to differences in the catalytic behavior of bacterial and mammalian GGTs.
24047895	4	11	theme	human	632:636	arg1	hGGT1					644:648	hGGT1	644:648	hGGT1	644:648	The rational design of effective inhibitors of human GGT1 (hGGT1) has been delayed by the lack of a reliable structural model.
24047895	4	11	theme	human	632:636	arg1	GGT1					638:641	human GGT1	632:641	human GGT1 (hGGT1)	632:649	The rational design of effective inhibitors of human GGT1 (hGGT1) has been delayed by the lack of a reliable structural model.
24047895	11	12	theme	GGT1-dependent	1751:1764	arg1	diseases					1766:1773	GGT1-dependent diseases	1751:1773	GGT1-dependent diseases	1751:1773	These differences between bacterial and mammalian GGTs and the new structural data will accelerate the development of new therapies for GGT1-dependent diseases.
24047895	2	13	contain	has	377:379	arg1	GGT1					328:331	GGT1	328:331	GGT1	328:331	In animals, GGT1 is expressed on the surface of the cell and has critical roles in maintaining cysteine levels in the body and regulating intracellular redox status.
24047895	2	13	contain	has	377:379	arg2	roles					390:394	critical roles	381:394	critical roles	381:394	In animals, GGT1 is expressed on the surface of the cell and has critical roles in maintaining cysteine levels in the body and regulating intracellular redox status.
24047895	1	14	theme	hydrolase	219:227	arg1	family					229:234	the N-terminal nucleophile hydrolase family	192:234	the N-terminal nucleophile hydrolase family	192:234	The enzyme γ-glutamyltranspeptidase 1 (GGT1) is a conserved member of the N-terminal nucleophile hydrolase family that cleaves the γ-glutamyl bond of glutathione and other γ-glutamyl compounds.
24047895	6	15	theme	resolution	893:902	arg1	structure					921:929	the high resolution (1.67 Å) crystal structure	884:929	the high resolution (1.67 Å) crystal structure of glutamate-bound hGGT1	884:954	We report the high resolution (1.67 Å) crystal structure of glutamate-bound hGGT1, the first of any eukaryotic GGT.
24047895	6	15	theme	resolution	893:902	arg1	first					961:965	first	961:965	first	961:965	We report the high resolution (1.67 Å) crystal structure of glutamate-bound hGGT1, the first of any eukaryotic GGT.
24047895	11	16	theme	therapies	1737:1745	arg1	development					1718:1728	the development	1714:1728	the development of new therapies for GGT1-dependent diseases	1714:1773	These differences between bacterial and mammalian GGTs and the new structural data will accelerate the development of new therapies for GGT1-dependent diseases.
24047895	1	17	theme	enzyme	126:131	arg1	γ-glutamyltranspeptidase					133:156	The enzyme γ-glutamyltranspeptidase 1	122:158	The enzyme γ-glutamyltranspeptidase 1 (GGT1)	122:165	The enzyme γ-glutamyltranspeptidase 1 (GGT1) is a conserved member of the N-terminal nucleophile hydrolase family that cleaves the γ-glutamyl bond of glutathione and other γ-glutamyl compounds.
24047895	1	17	theme	enzyme	126:131	arg1	GGT1					161:164	GGT1	161:164	GGT1	161:164	The enzyme γ-glutamyltranspeptidase 1 (GGT1) is a conserved member of the N-terminal nucleophile hydrolase family that cleaves the γ-glutamyl bond of glutathione and other γ-glutamyl compounds.
24047895	1	17	theme	enzyme	126:131	arg1	member					182:187	a conserved member	170:187	a conserved member of the N-terminal nucleophile hydrolase family that cleaves the γ-glutamyl bond of glutathione and other γ-glutamyl compounds	170:313	The enzyme γ-glutamyltranspeptidase 1 (GGT1) is a conserved member of the N-terminal nucleophile hydrolase family that cleaves the γ-glutamyl bond of glutathione and other γ-glutamyl compounds.
24047895	8	18	theme	open	1382:1385	arg1	conformation					1387:1398	an open conformation	1379:1398	an open conformation that allows greater access to the active site	1379:1444	Compared with several bacterial counterparts, the lid loop in the crystal structure of hGGT1 adopts an open conformation that allows greater access to the active site.
24047895	7	19	theme	human	1265:1269	arg1	enzyme					1271:1276	the human enzyme	1261:1276	the human enzyme	1261:1276	Comparisons of the active site architecture of hGGT1 with those of its bacterial orthologs highlight key differences in the residues responsible for substrate binding, including a bimodal switch in the orientation of the catalytic nucleophile (Thr-381) that is unique to the human enzyme.
24047895	10	20	theme	bacterial	1599:1607	arg1	GGTs					1609:1612	the bacterial GGTs	1595:1612	the bacterial GGTs	1595:1612	These are absent in the bacterial GGTs.
24047895	5	21	theme	available	716:724	arg1	structures					734:743	The available crystal structures	712:743	The available crystal structures of several bacterial GGTs	712:769	The available crystal structures of several bacterial GGTs have been of limited use due to differences in the catalytic behavior of bacterial and mammalian GGTs.
24047895	5	22	theme	bacterial	844:852	arg1	GGTs					868:871	bacterial and mammalian GGTs	844:871	bacterial and mammalian GGTs	844:871	The available crystal structures of several bacterial GGTs have been of limited use due to differences in the catalytic behavior of bacterial and mammalian GGTs.
24047895	2	23	from	levels	420:425	arg1	body					434:437	the body	430:437	the body	430:437	In animals, GGT1 is expressed on the surface of the cell and has critical roles in maintaining cysteine levels in the body and regulating intracellular redox status.
24047895	5	24	theme	mammalian	858:866	arg1	GGTs					868:871	bacterial and mammalian GGTs	844:871	bacterial and mammalian GGTs	844:871	The available crystal structures of several bacterial GGTs have been of limited use due to differences in the catalytic behavior of bacterial and mammalian GGTs.
24047895	6	25	theme	glutamate-bound	934:948	arg1	hGGT1					950:954	glutamate-bound hGGT1	934:954	glutamate-bound hGGT1	934:954	We report the high resolution (1.67 Å) crystal structure of glutamate-bound hGGT1, the first of any eukaryotic GGT.
24047895	4	26	theme	model	705:709	arg1	lack					675:678	the lack	671:678	the lack of a reliable structural model	671:709	The rational design of effective inhibitors of human GGT1 (hGGT1) has been delayed by the lack of a reliable structural model.
24047895	11	27	theme	structural	1682:1691	arg1	data					1693:1696	the new structural data	1674:1696	the new structural data	1674:1696	These differences between bacterial and mammalian GGTs and the new structural data will accelerate the development of new therapies for GGT1-dependent diseases.
24047895	0	28	theme	glutamate-bound	92:106	arg1	enzyme					114:119	the glutamate-bound human enzyme	88:119	the glutamate-bound human enzyme	88:119	Novel insights into eukaryotic γ-glutamyltranspeptidase 1 from the crystal structure of the glutamate-bound human enzyme.
24047895	8	29	theme	active	1434:1439	arg1	site					1441:1444	the active site	1430:1444	the active site	1430:1444	Compared with several bacterial counterparts, the lid loop in the crystal structure of hGGT1 adopts an open conformation that allows greater access to the active site.
24047895	2	30	theme	critical	381:388	arg1	roles					390:394	critical roles	381:394	critical roles	381:394	In animals, GGT1 is expressed on the surface of the cell and has critical roles in maintaining cysteine levels in the body and regulating intracellular redox status.
24047895	0	31	theme	enzyme	114:119	arg1	structure					75:83	the crystal structure	63:83	the crystal structure of the glutamate-bound human enzyme	63:119	Novel insights into eukaryotic γ-glutamyltranspeptidase 1 from the crystal structure of the glutamate-bound human enzyme.
24047895	4	32	theme	structural	694:703	arg1	model					705:709	a reliable structural model	683:709	a reliable structural model	683:709	The rational design of effective inhibitors of human GGT1 (hGGT1) has been delayed by the lack of a reliable structural model.
24047895	0	33	theme	Novel	0:4	arg1	insights					6:13	Novel insights	0:13	Novel insights into eukaryotic γ-glutamyltranspeptidase 1 from the crystal structure of the glutamate-bound human enzyme	0:119	Novel insights into eukaryotic γ-glutamyltranspeptidase 1 from the crystal structure of the glutamate-bound human enzyme.
24047895	9	34	theme	bound	1489:1493	arg1	chlorides					1495:1503	tightly bound chlorides	1481:1503	tightly bound chlorides	1481:1503	The hGGT1 structure also revealed tightly bound chlorides near the catalytic residue that may contribute to catalytic activity.
24047895	2	35	theme	cysteine	411:418	arg1	levels					420:425	cysteine levels	411:425	cysteine levels in the body	411:437	In animals, GGT1 is expressed on the surface of the cell and has critical roles in maintaining cysteine levels in the body and regulating intracellular redox status.
24047895	5	36	theme	limited	784:790	arg1	use					792:794	limited use	784:794	limited use due to differences in the catalytic behavior of bacterial and mammalian GGTs	784:871	The available crystal structures of several bacterial GGTs have been of limited use due to differences in the catalytic behavior of bacterial and mammalian GGTs.
24047895	1	37	theme	γ-glutamyl	294:303	arg1	compounds					305:313	other γ-glutamyl compounds	288:313	other γ-glutamyl compounds	288:313	The enzyme γ-glutamyltranspeptidase 1 (GGT1) is a conserved member of the N-terminal nucleophile hydrolase family that cleaves the γ-glutamyl bond of glutathione and other γ-glutamyl compounds.
24047895	6	38	theme	GGT	985:987	arg1	structure					921:929	the high resolution (1.67 Å) crystal structure	884:929	the high resolution (1.67 Å) crystal structure of glutamate-bound hGGT1	884:954	We report the high resolution (1.67 Å) crystal structure of glutamate-bound hGGT1, the first of any eukaryotic GGT.
24047895	6	38	theme	GGT	985:987	arg1	first					961:965	first	961:965	first	961:965	We report the high resolution (1.67 Å) crystal structure of glutamate-bound hGGT1, the first of any eukaryotic GGT.
24047895	2	39	theme	redox	468:472	arg1	status					474:479	intracellular redox status	454:479	intracellular redox status	454:479	In animals, GGT1 is expressed on the surface of the cell and has critical roles in maintaining cysteine levels in the body and regulating intracellular redox status.
24047895	0	40	theme	crystal	67:73	arg1	structure					75:83	the crystal structure	63:83	the crystal structure of the glutamate-bound human enzyme	63:119	Novel insights into eukaryotic γ-glutamyltranspeptidase 1 from the crystal structure of the glutamate-bound human enzyme.
24047895	7	41	theme	key	1091:1093	arg1	differences					1095:1105	key differences	1091:1105	key differences in the residues responsible for substrate binding, including a bimodal switch in the orientation of the catalytic nucleophile (Thr-381) that is unique to the human enzyme	1091:1276	Comparisons of the active site architecture of hGGT1 with those of its bacterial orthologs highlight key differences in the residues responsible for substrate binding, including a bimodal switch in the orientation of the catalytic nucleophile (Thr-381) that is unique to the human enzyme.
24047895	5	42	theme	several	748:754	arg1	GGTs					766:769	several bacterial GGTs	748:769	several bacterial GGTs	748:769	The available crystal structures of several bacterial GGTs have been of limited use due to differences in the catalytic behavior of bacterial and mammalian GGTs.
24047895	9	43	theme	catalytic	1514:1522	arg1	residue					1524:1530	the catalytic residue	1510:1530	the catalytic residue that may contribute to catalytic activity	1510:1572	The hGGT1 structure also revealed tightly bound chlorides near the catalytic residue that may contribute to catalytic activity.
24047895	7	44	theme	bimodal	1170:1176	arg1	switch					1178:1183	a bimodal switch	1168:1183	a bimodal switch in the orientation of the catalytic nucleophile (Thr-381) that is unique to the human enzyme	1168:1276	Comparisons of the active site architecture of hGGT1 with those of its bacterial orthologs highlight key differences in the residues responsible for substrate binding, including a bimodal switch in the orientation of the catalytic nucleophile (Thr-381) that is unique to the human enzyme.
24047895	5	45	theme	GGTs	766:769	arg1	structures					734:743	The available crystal structures	712:743	The available crystal structures of several bacterial GGTs	712:769	The available crystal structures of several bacterial GGTs have been of limited use due to differences in the catalytic behavior of bacterial and mammalian GGTs.
24047895	7	46	theme	nucleophile	1221:1231	arg1	orientation					1192:1202	the orientation	1188:1202	the orientation of the catalytic nucleophile (Thr-381) that is unique to the human enzyme	1188:1276	Comparisons of the active site architecture of hGGT1 with those of its bacterial orthologs highlight key differences in the residues responsible for substrate binding, including a bimodal switch in the orientation of the catalytic nucleophile (Thr-381) that is unique to the human enzyme.
24047895	11	47	theme	mammalian	1655:1663	arg1	GGTs					1665:1668	bacterial and mammalian GGTs	1641:1668	bacterial and mammalian GGTs	1641:1668	These differences between bacterial and mammalian GGTs and the new structural data will accelerate the development of new therapies for GGT1-dependent diseases.
24047895	1	48	theme	family	229:234	arg1	member					182:187	a conserved member	170:187	a conserved member of the N-terminal nucleophile hydrolase family that cleaves the γ-glutamyl bond of glutathione and other γ-glutamyl compounds	170:313	The enzyme γ-glutamyltranspeptidase 1 (GGT1) is a conserved member of the N-terminal nucleophile hydrolase family that cleaves the γ-glutamyl bond of glutathione and other γ-glutamyl compounds.
24047895	1	48	theme	family	229:234	arg1	γ-glutamyltranspeptidase					133:156	The enzyme γ-glutamyltranspeptidase 1	122:158	The enzyme γ-glutamyltranspeptidase 1 (GGT1)	122:165	The enzyme γ-glutamyltranspeptidase 1 (GGT1) is a conserved member of the N-terminal nucleophile hydrolase family that cleaves the γ-glutamyl bond of glutathione and other γ-glutamyl compounds.
24047895	11	49	theme	bacterial	1641:1649	arg1	GGTs					1665:1668	bacterial and mammalian GGTs	1641:1668	bacterial and mammalian GGTs	1641:1668	These differences between bacterial and mammalian GGTs and the new structural data will accelerate the development of new therapies for GGT1-dependent diseases.
24047895	5	50	theme	bacterial	756:764	arg1	GGTs					766:769	several bacterial GGTs	748:769	several bacterial GGTs	748:769	The available crystal structures of several bacterial GGTs have been of limited use due to differences in the catalytic behavior of bacterial and mammalian GGTs.
24047895	9	51	theme	catalytic	1555:1563	arg1	activity					1565:1572	catalytic activity	1555:1572	catalytic activity	1555:1572	The hGGT1 structure also revealed tightly bound chlorides near the catalytic residue that may contribute to catalytic activity.
24047895	3	52	theme	GGT1	496:499	arg1	Expression					482:491	Expression	482:491	Expression of GGT1	482:499	Expression of GGT1 has been implicated as a potentiator of asthma, cardiovascular disease, and cancer.
24047895	3	52	theme	GGT1	496:499	arg1	potentiator					526:536	a potentiator	524:536	a potentiator of asthma, cardiovascular disease, and cancer	524:582	Expression of GGT1 has been implicated as a potentiator of asthma, cardiovascular disease, and cancer.
24047895	1	53	theme	γ-glutamyl	253:262	arg1	bond					264:267	the γ-glutamyl bond	249:267	the γ-glutamyl bond of glutathione and other γ-glutamyl compounds	249:313	The enzyme γ-glutamyltranspeptidase 1 (GGT1) is a conserved member of the N-terminal nucleophile hydrolase family that cleaves the γ-glutamyl bond of glutathione and other γ-glutamyl compounds.
24047895	8	54	theme	greater	1412:1418	arg1	access					1420:1425	greater access	1412:1425	greater access to the active site	1412:1444	Compared with several bacterial counterparts, the lid loop in the crystal structure of hGGT1 adopts an open conformation that allows greater access to the active site.
24047895	7	55	from	switch	1178:1183	arg1	orientation					1192:1202	the orientation	1188:1202	the orientation of the catalytic nucleophile (Thr-381) that is unique to the human enzyme	1188:1276	Comparisons of the active site architecture of hGGT1 with those of its bacterial orthologs highlight key differences in the residues responsible for substrate binding, including a bimodal switch in the orientation of the catalytic nucleophile (Thr-381) that is unique to the human enzyme.
24047895	4	56	theme	GGT1	638:641	arg1	inhibitors					618:627	effective inhibitors	608:627	effective inhibitors of human GGT1 (hGGT1)	608:649	The rational design of effective inhibitors of human GGT1 (hGGT1) has been delayed by the lack of a reliable structural model.
24047895	7	57	theme	site	1016:1019	arg1	architecture					1021:1032	the active site architecture	1005:1032	the active site architecture of hGGT1	1005:1041	Comparisons of the active site architecture of hGGT1 with those of its bacterial orthologs highlight key differences in the residues responsible for substrate binding, including a bimodal switch in the orientation of the catalytic nucleophile (Thr-381) that is unique to the human enzyme.
24047895	3	58	theme	cardiovascular	549:562	arg1	disease					564:570	cardiovascular disease	549:570	cardiovascular disease	549:570	Expression of GGT1 has been implicated as a potentiator of asthma, cardiovascular disease, and cancer.
24047895	5	59	theme	catalytic	822:830	arg1	behavior					832:839	the catalytic behavior	818:839	the catalytic behavior of bacterial and mammalian GGTs	818:871	The available crystal structures of several bacterial GGTs have been of limited use due to differences in the catalytic behavior of bacterial and mammalian GGTs.
24047895	6	60	theme	crystal	913:919	arg1	structure					921:929	the high resolution (1.67 Å) crystal structure	884:929	the high resolution (1.67 Å) crystal structure of glutamate-bound hGGT1	884:954	We report the high resolution (1.67 Å) crystal structure of glutamate-bound hGGT1, the first of any eukaryotic GGT.
24047895	6	60	theme	crystal	913:919	arg1	first					961:965	first	961:965	first	961:965	We report the high resolution (1.67 Å) crystal structure of glutamate-bound hGGT1, the first of any eukaryotic GGT.
24047895	11	61	theme	new	1733:1735	arg1	therapies					1737:1745	new therapies	1733:1745	new therapies for GGT1-dependent diseases	1733:1773	These differences between bacterial and mammalian GGTs and the new structural data will accelerate the development of new therapies for GGT1-dependent diseases.
24047895	3	62	theme	asthma	541:546	arg1	potentiator					526:536	a potentiator	524:536	a potentiator of asthma, cardiovascular disease, and cancer	524:582	Expression of GGT1 has been implicated as a potentiator of asthma, cardiovascular disease, and cancer.
24047895	3	62	theme	asthma	541:546	arg1	Expression					482:491	Expression	482:491	Expression of GGT1	482:499	Expression of GGT1 has been implicated as a potentiator of asthma, cardiovascular disease, and cancer.
24047895	8	63	theme	hGGT1	1366:1370	arg1	structure					1353:1361	the crystal structure	1341:1361	the crystal structure of hGGT1	1341:1370	Compared with several bacterial counterparts, the lid loop in the crystal structure of hGGT1 adopts an open conformation that allows greater access to the active site.
24047895	4	64	theme	effective	608:616	arg1	inhibitors					618:627	effective inhibitors	608:627	effective inhibitors of human GGT1 (hGGT1)	608:649	The rational design of effective inhibitors of human GGT1 (hGGT1) has been delayed by the lack of a reliable structural model.
24047895	3	65	theme	cancer	577:582	arg1	potentiator					526:536	a potentiator	524:536	a potentiator of asthma, cardiovascular disease, and cancer	524:582	Expression of GGT1 has been implicated as a potentiator of asthma, cardiovascular disease, and cancer.
24047895	3	65	theme	cancer	577:582	arg1	Expression					482:491	Expression	482:491	Expression of GGT1	482:499	Expression of GGT1 has been implicated as a potentiator of asthma, cardiovascular disease, and cancer.
24047895	1	66	theme	nucleophile	207:217	arg1	family					229:234	the N-terminal nucleophile hydrolase family	192:234	the N-terminal nucleophile hydrolase family	192:234	The enzyme γ-glutamyltranspeptidase 1 (GGT1) is a conserved member of the N-terminal nucleophile hydrolase family that cleaves the γ-glutamyl bond of glutathione and other γ-glutamyl compounds.
24047895	0	67	from	structure	75:83	arg1	γ-glutamyltranspeptidase					31:54	eukaryotic γ-glutamyltranspeptidase 1	20:56	eukaryotic γ-glutamyltranspeptidase 1 from the crystal structure of the glutamate-bound human enzyme	20:119	Novel insights into eukaryotic γ-glutamyltranspeptidase 1 from the crystal structure of the glutamate-bound human enzyme.
24047895	7	68	theme	substrate	1139:1147	arg1	binding					1149:1155	substrate binding	1139:1155	substrate binding	1139:1155	Comparisons of the active site architecture of hGGT1 with those of its bacterial orthologs highlight key differences in the residues responsible for substrate binding, including a bimodal switch in the orientation of the catalytic nucleophile (Thr-381) that is unique to the human enzyme.
24047895	5	69	from	differences	803:813	arg1	behavior					832:839	the catalytic behavior	818:839	the catalytic behavior of bacterial and mammalian GGTs	818:871	The available crystal structures of several bacterial GGTs have been of limited use due to differences in the catalytic behavior of bacterial and mammalian GGTs.
24047895	5	70	theme	GGTs	868:871	arg1	behavior					832:839	the catalytic behavior	818:839	the catalytic behavior of bacterial and mammalian GGTs	818:871	The available crystal structures of several bacterial GGTs have been of limited use due to differences in the catalytic behavior of bacterial and mammalian GGTs.
24047895	6	71	theme	high	888:891	arg1	resolution					893:902	high resolution	888:902	the high resolution (1.67 Å) crystal structure of glutamate-bound hGGT1	884:954	We report the high resolution (1.67 Å) crystal structure of glutamate-bound hGGT1, the first of any eukaryotic GGT.
24047895	6	71	theme	high	888:891	arg1	Å					910:910	1.67 Å	905:910	1.67 Å	905:910	We report the high resolution (1.67 Å) crystal structure of glutamate-bound hGGT1, the first of any eukaryotic GGT.
24047895	11	72	theme	new	1678:1680	arg1	data					1693:1696	the new structural data	1674:1696	the new structural data	1674:1696	These differences between bacterial and mammalian GGTs and the new structural data will accelerate the development of new therapies for GGT1-dependent diseases.
24047895	5	73	theme	crystal	726:732	arg1	structures					734:743	The available crystal structures	712:743	The available crystal structures of several bacterial GGTs	712:769	The available crystal structures of several bacterial GGTs have been of limited use due to differences in the catalytic behavior of bacterial and mammalian GGTs.
24047895	6	74	theme	hGGT1	950:954	arg1	structure					921:929	the high resolution (1.67 Å) crystal structure	884:929	the high resolution (1.67 Å) crystal structure of glutamate-bound hGGT1	884:954	We report the high resolution (1.67 Å) crystal structure of glutamate-bound hGGT1, the first of any eukaryotic GGT.
24047895	6	74	theme	hGGT1	950:954	arg1	first					961:965	first	961:965	first	961:965	We report the high resolution (1.67 Å) crystal structure of glutamate-bound hGGT1, the first of any eukaryotic GGT.
24047895	0	75	theme	human	108:112	arg1	enzyme					114:119	the glutamate-bound human enzyme	88:119	the glutamate-bound human enzyme	88:119	Novel insights into eukaryotic γ-glutamyltranspeptidase 1 from the crystal structure of the glutamate-bound human enzyme.
24047895	9	76	theme	hGGT1	1451:1455	arg1	structure					1457:1465	The hGGT1 structure	1447:1465	The hGGT1 structure	1447:1465	The hGGT1 structure also revealed tightly bound chlorides near the catalytic residue that may contribute to catalytic activity.
24047895	7	77	from	differences	1095:1105	arg1	switch					1178:1183	a bimodal switch	1168:1183	a bimodal switch in the orientation of the catalytic nucleophile (Thr-381) that is unique to the human enzyme	1168:1276	Comparisons of the active site architecture of hGGT1 with those of its bacterial orthologs highlight key differences in the residues responsible for substrate binding, including a bimodal switch in the orientation of the catalytic nucleophile (Thr-381) that is unique to the human enzyme.
24047895	7	77	from	differences	1095:1105	arg1	residues					1114:1121	the residues	1110:1121	the residues	1110:1121	Comparisons of the active site architecture of hGGT1 with those of its bacterial orthologs highlight key differences in the residues responsible for substrate binding, including a bimodal switch in the orientation of the catalytic nucleophile (Thr-381) that is unique to the human enzyme.
24047895	7	78	theme	responsible	1123:1133	arg1	switch					1178:1183	a bimodal switch	1168:1183	a bimodal switch in the orientation of the catalytic nucleophile (Thr-381) that is unique to the human enzyme	1168:1276	Comparisons of the active site architecture of hGGT1 with those of its bacterial orthologs highlight key differences in the residues responsible for substrate binding, including a bimodal switch in the orientation of the catalytic nucleophile (Thr-381) that is unique to the human enzyme.
24047895	7	78	theme	responsible	1123:1133	arg1	residues					1114:1121	the residues	1110:1121	the residues	1110:1121	Comparisons of the active site architecture of hGGT1 with those of its bacterial orthologs highlight key differences in the residues responsible for substrate binding, including a bimodal switch in the orientation of the catalytic nucleophile (Thr-381) that is unique to the human enzyme.
24047895	1	79	theme	N-terminal	196:205	arg1	family					229:234	the N-terminal nucleophile hydrolase family	192:234	the N-terminal nucleophile hydrolase family	192:234	The enzyme γ-glutamyltranspeptidase 1 (GGT1) is a conserved member of the N-terminal nucleophile hydrolase family that cleaves the γ-glutamyl bond of glutathione and other γ-glutamyl compounds.
24047895	4	80	theme	reliable	685:692	arg1	model					705:709	a reliable structural model	683:709	a reliable structural model	683:709	The rational design of effective inhibitors of human GGT1 (hGGT1) has been delayed by the lack of a reliable structural model.
24047895	2	81	theme	cell	368:371	arg1	surface					353:359	the surface	349:359	the surface of the cell	349:371	In animals, GGT1 is expressed on the surface of the cell and has critical roles in maintaining cysteine levels in the body and regulating intracellular redox status.
24047895	0	82	theme	eukaryotic	20:29	arg1	γ-glutamyltranspeptidase					31:54	eukaryotic γ-glutamyltranspeptidase 1	20:56	eukaryotic γ-glutamyltranspeptidase 1 from the crystal structure of the glutamate-bound human enzyme	20:119	Novel insights into eukaryotic γ-glutamyltranspeptidase 1 from the crystal structure of the glutamate-bound human enzyme.
24047895	1	83	theme	other	288:292	arg1	compounds					305:313	other γ-glutamyl compounds	288:313	other γ-glutamyl compounds	288:313	The enzyme γ-glutamyltranspeptidase 1 (GGT1) is a conserved member of the N-terminal nucleophile hydrolase family that cleaves the γ-glutamyl bond of glutathione and other γ-glutamyl compounds.
24047895	7	84	with	Comparisons	990:1000	arg1	those					1048:1052	those	1048:1052	those	1048:1052	Comparisons of the active site architecture of hGGT1 with those of its bacterial orthologs highlight key differences in the residues responsible for substrate binding, including a bimodal switch in the orientation of the catalytic nucleophile (Thr-381) that is unique to the human enzyme.
24047895	8	85	theme	bacterial	1301:1309	arg1	counterparts					1311:1322	several bacterial counterparts	1293:1322	several bacterial counterparts	1293:1322	Compared with several bacterial counterparts, the lid loop in the crystal structure of hGGT1 adopts an open conformation that allows greater access to the active site.
24047895	1	86	theme	compounds	305:313	arg1	bond					264:267	the γ-glutamyl bond	249:267	the γ-glutamyl bond of glutathione and other γ-glutamyl compounds	249:313	The enzyme γ-glutamyltranspeptidase 1 (GGT1) is a conserved member of the N-terminal nucleophile hydrolase family that cleaves the γ-glutamyl bond of glutathione and other γ-glutamyl compounds.
24047895	6	87	theme	eukaryotic	974:983	arg1	GGT					985:987	any eukaryotic GGT	970:987	any eukaryotic GGT	970:987	We report the high resolution (1.67 Å) crystal structure of glutamate-bound hGGT1, the first of any eukaryotic GGT.
24047895	2	88	theme	intracellular	454:466	arg1	status					474:479	intracellular redox status	454:479	intracellular redox status	454:479	In animals, GGT1 is expressed on the surface of the cell and has critical roles in maintaining cysteine levels in the body and regulating intracellular redox status.
24047895	7	89	theme	bacterial	1061:1069	arg1	orthologs					1071:1079	its bacterial orthologs	1057:1079	its bacterial orthologs	1057:1079	Comparisons of the active site architecture of hGGT1 with those of its bacterial orthologs highlight key differences in the residues responsible for substrate binding, including a bimodal switch in the orientation of the catalytic nucleophile (Thr-381) that is unique to the human enzyme.
24047895	7	90	theme	catalytic	1211:1219	arg1	unique					1251:1256	unique	1251:1256	unique	1251:1256	Comparisons of the active site architecture of hGGT1 with those of its bacterial orthologs highlight key differences in the residues responsible for substrate binding, including a bimodal switch in the orientation of the catalytic nucleophile (Thr-381) that is unique to the human enzyme.
24047895	7	90	theme	catalytic	1211:1219	arg1	Thr-381					1234:1240	Thr-381	1234:1240	Thr-381	1234:1240	Comparisons of the active site architecture of hGGT1 with those of its bacterial orthologs highlight key differences in the residues responsible for substrate binding, including a bimodal switch in the orientation of the catalytic nucleophile (Thr-381) that is unique to the human enzyme.
24047895	7	90	theme	catalytic	1211:1219	arg1	nucleophile					1221:1231	the catalytic nucleophile	1207:1231	the catalytic nucleophile (Thr-381) that is unique to the human enzyme	1207:1276	Comparisons of the active site architecture of hGGT1 with those of its bacterial orthologs highlight key differences in the residues responsible for substrate binding, including a bimodal switch in the orientation of the catalytic nucleophile (Thr-381) that is unique to the human enzyme.
24047895	8	91	theme	lid	1329:1331	arg1	loop					1333:1336	the lid loop	1325:1336	the lid loop in the crystal structure of hGGT1	1325:1370	Compared with several bacterial counterparts, the lid loop in the crystal structure of hGGT1 adopts an open conformation that allows greater access to the active site.
24047895	4	92	theme	rational	589:596	arg1	design					598:603	The rational design	585:603	The rational design of effective inhibitors of human GGT1 (hGGT1)	585:649	The rational design of effective inhibitors of human GGT1 (hGGT1) has been delayed by the lack of a reliable structural model.
24047895	10	93	from	absent	1585:1590	arg1	GGTs					1609:1612	the bacterial GGTs	1595:1612	the bacterial GGTs	1595:1612	These are absent in the bacterial GGTs.
24047895	8	94	theme	crystal	1345:1351	arg1	structure					1353:1361	the crystal structure	1341:1361	the crystal structure of hGGT1	1341:1370	Compared with several bacterial counterparts, the lid loop in the crystal structure of hGGT1 adopts an open conformation that allows greater access to the active site.
26013825	9	0	from	development	1853:1863	arg1	invaluable					1835:1844	invaluable	1835:1844	invaluable	1835:1844	These data provide new insights into the mechanism of hGGT1-catalyzed reactions and will be invaluable in the development of new classes of hGGT1 inhibitors for therapeutic use.
26013825	9	1	theme	inhibitors	1889:1898	arg1	classes					1872:1878	new classes	1868:1878	new classes of hGGT1 inhibitors for therapeutic use	1868:1918	These data provide new insights into the mechanism of hGGT1-catalyzed reactions and will be invaluable in the development of new classes of hGGT1 inhibitors for therapeutic use.
26013825	0	2	theme	ACTIVE	173:178	arg1	SITE					180:183	THE ACTIVE SITE	169:183	THE ACTIVE SITE	169:183	Human γ-Glutamyl Transpeptidase 1: STRUCTURES OF THE FREE ENZYME, INHIBITOR-BOUND TETRAHEDRAL TRANSITION STATES, AND GLUTAMATE-BOUND ENZYME REVEAL NOVEL MOVEMENT WITHIN THE ACTIVE SITE DURING CATALYSIS.
26013825	1	3	theme	cell	243:246	arg1	hydrolase					280:288	a cell surface, N-terminal nucleophile hydrolase	241:288	hydrolase	280:288	γ-Glutamyl transpeptidase 1 (GGT1) is a cell surface, N-terminal nucleophile hydrolase that cleaves glutathione and other γ-glutamyl compounds.
26013825	1	3	theme	cell	243:246	arg1	transpeptidase					214:227	γ-Glutamyl transpeptidase 1	203:229	γ-Glutamyl transpeptidase 1 (GGT1)	203:236	γ-Glutamyl transpeptidase 1 (GGT1) is a cell surface, N-terminal nucleophile hydrolase that cleaves glutathione and other γ-glutamyl compounds.
26013825	9	4	theme	therapeutic	1904:1914	arg1	use					1916:1918	therapeutic use	1904:1918	therapeutic use	1904:1918	These data provide new insights into the mechanism of hGGT1-catalyzed reactions and will be invaluable in the development of new classes of hGGT1 inhibitors for therapeutic use.
26013825	3	5	theme	inhibitor-bound	679:693	arg1	states					718:723	inhibitor-bound tetrahedral transition states	679:723	inhibitor-bound tetrahedral transition states	679:723	In this study, we report four new crystal structures of human GGT1 (hGGT1) that show conformational changes within the active site as the enzyme progresses from the free enzyme to inhibitor-bound tetrahedral transition states and finally to the glutamate-bound structure prior to the release of this final product of the reaction.
26013825	8	6	theme	active	1718:1723	arg1	site					1725:1728	the active site	1714:1728	the active site	1714:1728	The glutamate-bound structure shows the conformation of the enzyme prior to release of the final product and reveals novel information regarding the displacement of the main chain atoms that form the oxyanion hole and movement of the lid loop region when the active site is occupied.
26013825	7	7	theme	catalytic	1440:1448	arg1	Thr-381					1450:1456	the catalytic Thr-381	1436:1456	the catalytic Thr-381	1436:1456	These structures are the first structures for any eukaryotic GGT that include a molecule in the active site covalently bound to the catalytic Thr-381.
26013825	6	8	theme	potent	1259:1264	arg1	diesters					1241:1248	neutral phosphonate diesters	1221:1248	neutral phosphonate diesters	1221:1248	The structure of GGsTop-bound hGGT1 reveals its interactions with the enzyme and why neutral phosphonate diesters are more potent inhibitors than monoanionic phosphonates.
26013825	6	8	theme	potent	1259:1264	arg1	inhibitors					1266:1275	more potent inhibitors	1254:1275	more potent inhibitors than monoanionic phosphonates	1254:1305	The structure of GGsTop-bound hGGT1 reveals its interactions with the enzyme and why neutral phosphonate diesters are more potent inhibitors than monoanionic phosphonates.
26013825	8	9	used	occupied	1733:1740	arg2	site					1725:1728	the active site	1714:1728	the active site	1714:1728	The glutamate-bound structure shows the conformation of the enzyme prior to release of the final product and reveals novel information regarding the displacement of the main chain atoms that form the oxyanion hole and movement of the lid loop region when the active site is occupied.
26013825	4	10	theme	active	890:895	arg1	site					897:900	the active site	886:900	the active site	886:900	The structure of the apoenzyme shows flexibility within the active site.
26013825	2	11	from	essential	366:374	arg1	homeostasis					388:398	cysteine homeostasis	379:398	cysteine homeostasis	379:398	GGT1 expression is essential in cysteine homeostasis, and its induction has been implicated in the pathology of asthma, reperfusion injury, and cancer.
26013825	6	12	theme	GGsTop-bound	1153:1164	arg1	hGGT1					1166:1170	GGsTop-bound hGGT1	1153:1170	GGsTop-bound hGGT1	1153:1170	The structure of GGsTop-bound hGGT1 reveals its interactions with the enzyme and why neutral phosphonate diesters are more potent inhibitors than monoanionic phosphonates.
26013825	3	13	theme	transition	707:716	arg1	states					718:723	inhibitor-bound tetrahedral transition states	679:723	inhibitor-bound tetrahedral transition states	679:723	In this study, we report four new crystal structures of human GGT1 (hGGT1) that show conformational changes within the active site as the enzyme progresses from the free enzyme to inhibitor-bound tetrahedral transition states and finally to the glutamate-bound structure prior to the release of this final product of the reaction.
26013825	3	14	theme	crystal	533:539	arg1	structures					541:550	four new crystal structures	524:550	four new crystal structures of human GGT1 (hGGT1) that show conformational changes within the active site as the enzyme progresses from the free enzyme to inhibitor-bound tetrahedral transition states and finally to the glutamate-bound structure prior to the release of this final product of the reaction	524:827	In this study, we report four new crystal structures of human GGT1 (hGGT1) that show conformational changes within the active site as the enzyme progresses from the free enzyme to inhibitor-bound tetrahedral transition states and finally to the glutamate-bound structure prior to the release of this final product of the reaction.
26013825	1	15	theme	γ-Glutamyl	203:212	arg1	hydrolase					280:288	a cell surface, N-terminal nucleophile hydrolase	241:288	hydrolase	280:288	γ-Glutamyl transpeptidase 1 (GGT1) is a cell surface, N-terminal nucleophile hydrolase that cleaves glutathione and other γ-glutamyl compounds.
26013825	1	15	theme	γ-Glutamyl	203:212	arg1	transpeptidase					214:227	γ-Glutamyl transpeptidase 1	203:229	γ-Glutamyl transpeptidase 1 (GGT1)	203:236	γ-Glutamyl transpeptidase 1 (GGT1) is a cell surface, N-terminal nucleophile hydrolase that cleaves glutathione and other γ-glutamyl compounds.
26013825	1	15	theme	γ-Glutamyl	203:212	arg1	GGT1					232:235	GGT1	232:235	GGT1	232:235	γ-Glutamyl transpeptidase 1 (GGT1) is a cell surface, N-terminal nucleophile hydrolase that cleaves glutathione and other γ-glutamyl compounds.
26013825	8	16	theme	glutamate-bound	1463:1477	arg1	structure					1479:1487	The glutamate-bound structure	1459:1487	The glutamate-bound structure	1459:1487	The glutamate-bound structure shows the conformation of the enzyme prior to release of the final product and reveals novel information regarding the displacement of the main chain atoms that form the oxyanion hole and movement of the lid loop region when the active site is occupied.
26013825	7	17	theme	active	1404:1409	arg1	site					1411:1414	the active site	1400:1414	the active site covalently bound to the catalytic Thr-381	1400:1456	These structures are the first structures for any eukaryotic GGT that include a molecule in the active site covalently bound to the catalytic Thr-381.
26013825	3	18	theme	glutamate-bound	744:758	arg1	structure					760:768	the glutamate-bound structure	740:768	the glutamate-bound structure prior to the release of this final product of the reaction	740:827	In this study, we report four new crystal structures of human GGT1 (hGGT1) that show conformational changes within the active site as the enzyme progresses from the free enzyme to inhibitor-bound tetrahedral transition states and finally to the glutamate-bound structure prior to the release of this final product of the reaction.
26013825	0	19	theme	ENZYME	133:138	arg1	STRUCTURES					35:44	STRUCTURES	35:44	STRUCTURES OF THE FREE ENZYME, INHIBITOR-BOUND TETRAHEDRAL TRANSITION STATES, AND GLUTAMATE-BOUND ENZYME	35:138	Human γ-Glutamyl Transpeptidase 1: STRUCTURES OF THE FREE ENZYME, INHIBITOR-BOUND TETRAHEDRAL TRANSITION STATES, AND GLUTAMATE-BOUND ENZYME REVEAL NOVEL MOVEMENT WITHIN THE ACTIVE SITE DURING CATALYSIS.
26013825	0	20	theme	NOVEL	147:151	arg1	MOVEMENT					153:160	NOVEL MOVEMENT	147:160	NOVEL MOVEMENT	147:160	Human γ-Glutamyl Transpeptidase 1: STRUCTURES OF THE FREE ENZYME, INHIBITOR-BOUND TETRAHEDRAL TRANSITION STATES, AND GLUTAMATE-BOUND ENZYME REVEAL NOVEL MOVEMENT WITHIN THE ACTIVE SITE DURING CATALYSIS.
26013825	3	21	theme	GGT1	561:564	arg1	structures					541:550	four new crystal structures	524:550	four new crystal structures of human GGT1 (hGGT1) that show conformational changes within the active site as the enzyme progresses from the free enzyme to inhibitor-bound tetrahedral transition states and finally to the glutamate-bound structure prior to the release of this final product of the reaction	524:827	In this study, we report four new crystal structures of human GGT1 (hGGT1) that show conformational changes within the active site as the enzyme progresses from the free enzyme to inhibitor-bound tetrahedral transition states and finally to the glutamate-bound structure prior to the release of this final product of the reaction.
26013825	3	22	theme	reaction	820:827	arg1	product					805:811	this final product	794:811	this final product of the reaction	794:827	In this study, we report four new crystal structures of human GGT1 (hGGT1) that show conformational changes within the active site as the enzyme progresses from the free enzyme to inhibitor-bound tetrahedral transition states and finally to the glutamate-bound structure prior to the release of this final product of the reaction.
26013825	6	23	theme	neutral	1221:1227	arg1	diesters					1241:1248	neutral phosphonate diesters	1221:1248	neutral phosphonate diesters	1221:1248	The structure of GGsTop-bound hGGT1 reveals its interactions with the enzyme and why neutral phosphonate diesters are more potent inhibitors than monoanionic phosphonates.
26013825	6	23	theme	neutral	1221:1227	arg1	inhibitors					1266:1275	more potent inhibitors	1254:1275	more potent inhibitors than monoanionic phosphonates	1254:1305	The structure of GGsTop-bound hGGT1 reveals its interactions with the enzyme and why neutral phosphonate diesters are more potent inhibitors than monoanionic phosphonates.
26013825	3	24	theme	conformational	584:597	arg1	changes					599:605	conformational changes	584:605	conformational changes within the active site	584:628	In this study, we report four new crystal structures of human GGT1 (hGGT1) that show conformational changes within the active site as the enzyme progresses from the free enzyme to inhibitor-bound tetrahedral transition states and finally to the glutamate-bound structure prior to the release of this final product of the reaction.
26013825	3	24	theme	conformational	584:597	arg1	progresses					644:653	the enzyme progresses	633:653	the enzyme progresses from the free enzyme to inhibitor-bound tetrahedral transition states and finally to the glutamate-bound structure prior to the release of this final product of the reaction	633:827	In this study, we report four new crystal structures of human GGT1 (hGGT1) that show conformational changes within the active site as the enzyme progresses from the free enzyme to inhibitor-bound tetrahedral transition states and finally to the glutamate-bound structure prior to the release of this final product of the reaction.
26013825	2	25	theme	cancer	491:496	arg1	pathology					446:454	the pathology	442:454	the pathology of asthma, reperfusion injury, and cancer	442:496	GGT1 expression is essential in cysteine homeostasis, and its induction has been implicated in the pathology of asthma, reperfusion injury, and cancer.
26013825	3	26	theme	prior	770:774	arg1	structure					760:768	the glutamate-bound structure	740:768	the glutamate-bound structure prior to the release of this final product of the reaction	740:827	In this study, we report four new crystal structures of human GGT1 (hGGT1) that show conformational changes within the active site as the enzyme progresses from the free enzyme to inhibitor-bound tetrahedral transition states and finally to the glutamate-bound structure prior to the release of this final product of the reaction.
26013825	0	27	theme	FREE	53:56	arg1	ENZYME					58:63	THE FREE ENZYME	49:63	THE FREE ENZYME	49:63	Human γ-Glutamyl Transpeptidase 1: STRUCTURES OF THE FREE ENZYME, INHIBITOR-BOUND TETRAHEDRAL TRANSITION STATES, AND GLUTAMATE-BOUND ENZYME REVEAL NOVEL MOVEMENT WITHIN THE ACTIVE SITE DURING CATALYSIS.
26013825	1	28	theme	γ-glutamyl	325:334	arg1	compounds					336:344	other γ-glutamyl compounds	319:344	other γ-glutamyl compounds	319:344	γ-Glutamyl transpeptidase 1 (GGT1) is a cell surface, N-terminal nucleophile hydrolase that cleaves glutathione and other γ-glutamyl compounds.
26013825	8	29	theme	prior	1526:1530	arg1	enzyme					1519:1524	the enzyme	1515:1524	the enzyme prior to release of the final product	1515:1562	The glutamate-bound structure shows the conformation of the enzyme prior to release of the final product and reveals novel information regarding the displacement of the main chain atoms that form the oxyanion hole and movement of the lid loop region when the active site is occupied.
26013825	3	30	theme	final	799:803	arg1	product					805:811	this final product	794:811	this final product of the reaction	794:827	In this study, we report four new crystal structures of human GGT1 (hGGT1) that show conformational changes within the active site as the enzyme progresses from the free enzyme to inhibitor-bound tetrahedral transition states and finally to the glutamate-bound structure prior to the release of this final product of the reaction.
26013825	0	31	theme	TETRAHEDRAL	82:92	arg1	STATES					105:110	INHIBITOR-BOUND TETRAHEDRAL TRANSITION STATES	66:110	INHIBITOR-BOUND TETRAHEDRAL TRANSITION STATES	66:110	Human γ-Glutamyl Transpeptidase 1: STRUCTURES OF THE FREE ENZYME, INHIBITOR-BOUND TETRAHEDRAL TRANSITION STATES, AND GLUTAMATE-BOUND ENZYME REVEAL NOVEL MOVEMENT WITHIN THE ACTIVE SITE DURING CATALYSIS.
26013825	0	32	theme	STATES	105:110	arg1	STRUCTURES					35:44	STRUCTURES	35:44	STRUCTURES OF THE FREE ENZYME, INHIBITOR-BOUND TETRAHEDRAL TRANSITION STATES, AND GLUTAMATE-BOUND ENZYME	35:138	Human γ-Glutamyl Transpeptidase 1: STRUCTURES OF THE FREE ENZYME, INHIBITOR-BOUND TETRAHEDRAL TRANSITION STATES, AND GLUTAMATE-BOUND ENZYME REVEAL NOVEL MOVEMENT WITHIN THE ACTIVE SITE DURING CATALYSIS.
26013825	5	33	theme	tetrahedral	1093:1103	arg1	state					1129:1133	the enzyme's tetrahedral intermediate/transition state	1080:1133	the enzyme's tetrahedral intermediate/transition state	1080:1133	The serine-borate-bound hGGT1 crystal structure demonstrates that serine-borate occupies the active site of the enzyme, resulting in an enzyme-inhibitor complex that replicates the enzyme's tetrahedral intermediate/transition state.
26013825	9	34	theme	reactions	1813:1821	arg1	mechanism					1784:1792	the mechanism	1780:1792	the mechanism of hGGT1-catalyzed reactions	1780:1821	These data provide new insights into the mechanism of hGGT1-catalyzed reactions and will be invaluable in the development of new classes of hGGT1 inhibitors for therapeutic use.
26013825	8	35	theme	product	1556:1562	arg1	release					1535:1541	release	1535:1541	release of the final product	1535:1562	The glutamate-bound structure shows the conformation of the enzyme prior to release of the final product and reveals novel information regarding the displacement of the main chain atoms that form the oxyanion hole and movement of the lid loop region when the active site is occupied.
26013825	0	36	theme	Human	0:4	arg1	Transpeptidase					17:30	Human γ-Glutamyl Transpeptidase 1	0:32	Human γ-Glutamyl Transpeptidase 1: STRUCTURES OF THE FREE ENZYME, INHIBITOR-BOUND TETRAHEDRAL TRANSITION STATES, AND GLUTAMATE-BOUND ENZYME REVEAL NOVEL MOVEMENT WITHIN THE ACTIVE SITE DURING CATALYSIS.	0:201	Human γ-Glutamyl Transpeptidase 1: STRUCTURES OF THE FREE ENZYME, INHIBITOR-BOUND TETRAHEDRAL TRANSITION STATES, AND GLUTAMATE-BOUND ENZYME REVEAL NOVEL MOVEMENT WITHIN THE ACTIVE SITE DURING CATALYSIS.
26013825	1	37	theme	N-terminal	257:266	arg1	hydrolase					280:288	a cell surface, N-terminal nucleophile hydrolase	241:288	hydrolase	280:288	γ-Glutamyl transpeptidase 1 (GGT1) is a cell surface, N-terminal nucleophile hydrolase that cleaves glutathione and other γ-glutamyl compounds.
26013825	1	37	theme	N-terminal	257:266	arg1	transpeptidase					214:227	γ-Glutamyl transpeptidase 1	203:229	γ-Glutamyl transpeptidase 1 (GGT1)	203:236	γ-Glutamyl transpeptidase 1 (GGT1) is a cell surface, N-terminal nucleophile hydrolase that cleaves glutathione and other γ-glutamyl compounds.
26013825	5	38	theme	serine-borate-bound	907:925	arg1	structure					941:949	The serine-borate-bound hGGT1 crystal structure	903:949	The serine-borate-bound hGGT1 crystal structure	903:949	The serine-borate-bound hGGT1 crystal structure demonstrates that serine-borate occupies the active site of the enzyme, resulting in an enzyme-inhibitor complex that replicates the enzyme's tetrahedral intermediate/transition state.
26013825	5	39	theme	crystal	933:939	arg1	structure					941:949	The serine-borate-bound hGGT1 crystal structure	903:949	The serine-borate-bound hGGT1 crystal structure	903:949	The serine-borate-bound hGGT1 crystal structure demonstrates that serine-borate occupies the active site of the enzyme, resulting in an enzyme-inhibitor complex that replicates the enzyme's tetrahedral intermediate/transition state.
26013825	2	40	theme	reperfusion	467:477	arg1	injury					479:484	reperfusion injury	467:484	reperfusion injury	467:484	GGT1 expression is essential in cysteine homeostasis, and its induction has been implicated in the pathology of asthma, reperfusion injury, and cancer.
26013825	3	41	theme	active	618:623	arg1	site					625:628	the active site	614:628	the active site	614:628	In this study, we report four new crystal structures of human GGT1 (hGGT1) that show conformational changes within the active site as the enzyme progresses from the free enzyme to inhibitor-bound tetrahedral transition states and finally to the glutamate-bound structure prior to the release of this final product of the reaction.
26013825	2	42	from	homeostasis	388:398	arg1	essential					366:374	essential	366:374	essential	366:374	GGT1 expression is essential in cysteine homeostasis, and its induction has been implicated in the pathology of asthma, reperfusion injury, and cancer.
26013825	2	43	theme	asthma	459:464	arg1	pathology					446:454	the pathology	442:454	the pathology of asthma, reperfusion injury, and cancer	442:496	GGT1 expression is essential in cysteine homeostasis, and its induction has been implicated in the pathology of asthma, reperfusion injury, and cancer.
26013825	2	44	theme	GGT1	347:350	arg1	expression					352:361	GGT1 expression	347:361	GGT1 expression	347:361	GGT1 expression is essential in cysteine homeostasis, and its induction has been implicated in the pathology of asthma, reperfusion injury, and cancer.
26013825	3	45	theme	enzyme	637:642	arg1	progresses					644:653	the enzyme progresses	633:653	the enzyme progresses from the free enzyme to inhibitor-bound tetrahedral transition states and finally to the glutamate-bound structure prior to the release of this final product of the reaction	633:827	In this study, we report four new crystal structures of human GGT1 (hGGT1) that show conformational changes within the active site as the enzyme progresses from the free enzyme to inhibitor-bound tetrahedral transition states and finally to the glutamate-bound structure prior to the release of this final product of the reaction.
26013825	3	45	theme	enzyme	637:642	arg1	changes					599:605	conformational changes	584:605	conformational changes within the active site	584:628	In this study, we report four new crystal structures of human GGT1 (hGGT1) that show conformational changes within the active site as the enzyme progresses from the free enzyme to inhibitor-bound tetrahedral transition states and finally to the glutamate-bound structure prior to the release of this final product of the reaction.
26013825	0	46	dep	Transpeptidase	17:30	arg1	REVEAL					140:145	REVEAL	140:145	REVEAL NOVEL MOVEMENT WITHIN THE ACTIVE SITE DURING CATALYSIS	140:200	Human γ-Glutamyl Transpeptidase 1: STRUCTURES OF THE FREE ENZYME, INHIBITOR-BOUND TETRAHEDRAL TRANSITION STATES, AND GLUTAMATE-BOUND ENZYME REVEAL NOVEL MOVEMENT WITHIN THE ACTIVE SITE DURING CATALYSIS.
26013825	9	47	theme	classes	1872:1878	arg1	development					1853:1863	the development	1849:1863	the development of new classes of hGGT1 inhibitors for therapeutic use	1849:1918	These data provide new insights into the mechanism of hGGT1-catalyzed reactions and will be invaluable in the development of new classes of hGGT1 inhibitors for therapeutic use.
26013825	8	48	theme	main	1628:1631	arg1	atoms					1639:1643	the main chain atoms	1624:1643	the main chain atoms that form the oxyanion hole and movement of the lid loop region when the active site is occupied	1624:1740	The glutamate-bound structure shows the conformation of the enzyme prior to release of the final product and reveals novel information regarding the displacement of the main chain atoms that form the oxyanion hole and movement of the lid loop region when the active site is occupied.
26013825	9	49	theme	hGGT1	1883:1887	arg1	inhibitors					1889:1898	hGGT1 inhibitors	1883:1898	hGGT1 inhibitors for therapeutic use	1883:1918	These data provide new insights into the mechanism of hGGT1-catalyzed reactions and will be invaluable in the development of new classes of hGGT1 inhibitors for therapeutic use.
26013825	8	50	theme	atoms	1639:1643	arg1	displacement					1608:1619	the displacement	1604:1619	the displacement of the main chain atoms that form the oxyanion hole and movement of the lid loop region when the active site is occupied	1604:1740	The glutamate-bound structure shows the conformation of the enzyme prior to release of the final product and reveals novel information regarding the displacement of the main chain atoms that form the oxyanion hole and movement of the lid loop region when the active site is occupied.
26013825	3	51	theme	free	664:667	arg1	enzyme					669:674	the free enzyme	660:674	the free enzyme to inhibitor-bound tetrahedral transition states and finally to the glutamate-bound structure prior to the release of this final product of the reaction	660:827	In this study, we report four new crystal structures of human GGT1 (hGGT1) that show conformational changes within the active site as the enzyme progresses from the free enzyme to inhibitor-bound tetrahedral transition states and finally to the glutamate-bound structure prior to the release of this final product of the reaction.
26013825	8	52	theme	lid	1693:1695	arg1	region					1702:1707	the lid loop region	1689:1707	the lid loop region	1689:1707	The glutamate-bound structure shows the conformation of the enzyme prior to release of the final product and reveals novel information regarding the displacement of the main chain atoms that form the oxyanion hole and movement of the lid loop region when the active site is occupied.
26013825	9	53	from	invaluable	1835:1844	arg1	development					1853:1863	the development	1849:1863	the development of new classes of hGGT1 inhibitors for therapeutic use	1849:1918	These data provide new insights into the mechanism of hGGT1-catalyzed reactions and will be invaluable in the development of new classes of hGGT1 inhibitors for therapeutic use.
26013825	8	54	theme	region	1702:1707	arg1	movement					1677:1684	movement	1677:1684	movement	1677:1684	The glutamate-bound structure shows the conformation of the enzyme prior to release of the final product and reveals novel information regarding the displacement of the main chain atoms that form the oxyanion hole and movement of the lid loop region when the active site is occupied.
26013825	8	54	theme	region	1702:1707	arg1	hole					1668:1671	the oxyanion hole	1655:1671	the oxyanion hole	1655:1671	The glutamate-bound structure shows the conformation of the enzyme prior to release of the final product and reveals novel information regarding the displacement of the main chain atoms that form the oxyanion hole and movement of the lid loop region when the active site is occupied.
26013825	1	55	theme	surface	248:254	arg1	hydrolase					280:288	a cell surface, N-terminal nucleophile hydrolase	241:288	hydrolase	280:288	γ-Glutamyl transpeptidase 1 (GGT1) is a cell surface, N-terminal nucleophile hydrolase that cleaves glutathione and other γ-glutamyl compounds.
26013825	1	55	theme	surface	248:254	arg1	transpeptidase					214:227	γ-Glutamyl transpeptidase 1	203:229	γ-Glutamyl transpeptidase 1 (GGT1)	203:236	γ-Glutamyl transpeptidase 1 (GGT1) is a cell surface, N-terminal nucleophile hydrolase that cleaves glutathione and other γ-glutamyl compounds.
26013825	8	56	theme	oxyanion	1659:1666	arg1	hole					1668:1671	the oxyanion hole	1655:1671	the oxyanion hole	1655:1671	The glutamate-bound structure shows the conformation of the enzyme prior to release of the final product and reveals novel information regarding the displacement of the main chain atoms that form the oxyanion hole and movement of the lid loop region when the active site is occupied.
26013825	3	57	theme	tetrahedral	695:705	arg1	states					718:723	inhibitor-bound tetrahedral transition states	679:723	inhibitor-bound tetrahedral transition states	679:723	In this study, we report four new crystal structures of human GGT1 (hGGT1) that show conformational changes within the active site as the enzyme progresses from the free enzyme to inhibitor-bound tetrahedral transition states and finally to the glutamate-bound structure prior to the release of this final product of the reaction.
26013825	6	58	theme	monoanionic	1282:1292	arg1	phosphonates					1294:1305	monoanionic phosphonates	1282:1305	monoanionic phosphonates	1282:1305	The structure of GGsTop-bound hGGT1 reveals its interactions with the enzyme and why neutral phosphonate diesters are more potent inhibitors than monoanionic phosphonates.
26013825	3	59	from	enzyme	669:674	arg1	progresses					644:653	the enzyme progresses	633:653	the enzyme progresses from the free enzyme to inhibitor-bound tetrahedral transition states and finally to the glutamate-bound structure prior to the release of this final product of the reaction	633:827	In this study, we report four new crystal structures of human GGT1 (hGGT1) that show conformational changes within the active site as the enzyme progresses from the free enzyme to inhibitor-bound tetrahedral transition states and finally to the glutamate-bound structure prior to the release of this final product of the reaction.
26013825	3	59	from	enzyme	669:674	arg1	changes					599:605	conformational changes	584:605	conformational changes within the active site	584:628	In this study, we report four new crystal structures of human GGT1 (hGGT1) that show conformational changes within the active site as the enzyme progresses from the free enzyme to inhibitor-bound tetrahedral transition states and finally to the glutamate-bound structure prior to the release of this final product of the reaction.
26013825	6	60	with	interactions	1184:1195	arg1	enzyme					1206:1211	the enzyme	1202:1211	the enzyme	1202:1211	The structure of GGsTop-bound hGGT1 reveals its interactions with the enzyme and why neutral phosphonate diesters are more potent inhibitors than monoanionic phosphonates.
26013825	6	61	theme	hGGT1	1166:1170	arg1	structure					1140:1148	The structure	1136:1148	The structure of GGsTop-bound hGGT1	1136:1170	The structure of GGsTop-bound hGGT1 reveals its interactions with the enzyme and why neutral phosphonate diesters are more potent inhibitors than monoanionic phosphonates.
26013825	0	62	theme	GLUTAMATE-BOUND	117:131	arg1	ENZYME					133:138	GLUTAMATE-BOUND ENZYME	117:138	GLUTAMATE-BOUND ENZYME	117:138	Human γ-Glutamyl Transpeptidase 1: STRUCTURES OF THE FREE ENZYME, INHIBITOR-BOUND TETRAHEDRAL TRANSITION STATES, AND GLUTAMATE-BOUND ENZYME REVEAL NOVEL MOVEMENT WITHIN THE ACTIVE SITE DURING CATALYSIS.
26013825	3	63	theme	new	529:531	arg1	structures					541:550	four new crystal structures	524:550	four new crystal structures of human GGT1 (hGGT1) that show conformational changes within the active site as the enzyme progresses from the free enzyme to inhibitor-bound tetrahedral transition states and finally to the glutamate-bound structure prior to the release of this final product of the reaction	524:827	In this study, we report four new crystal structures of human GGT1 (hGGT1) that show conformational changes within the active site as the enzyme progresses from the free enzyme to inhibitor-bound tetrahedral transition states and finally to the glutamate-bound structure prior to the release of this final product of the reaction.
26013825	3	64	theme	human	555:559	arg1	hGGT1					567:571	hGGT1	567:571	hGGT1	567:571	In this study, we report four new crystal structures of human GGT1 (hGGT1) that show conformational changes within the active site as the enzyme progresses from the free enzyme to inhibitor-bound tetrahedral transition states and finally to the glutamate-bound structure prior to the release of this final product of the reaction.
26013825	3	64	theme	human	555:559	arg1	GGT1					561:564	human GGT1	555:564	human GGT1 (hGGT1)	555:572	In this study, we report four new crystal structures of human GGT1 (hGGT1) that show conformational changes within the active site as the enzyme progresses from the free enzyme to inhibitor-bound tetrahedral transition states and finally to the glutamate-bound structure prior to the release of this final product of the reaction.
26013825	4	65	theme	apoenzyme	851:859	arg1	structure					834:842	The structure	830:842	The structure of the apoenzyme	830:859	The structure of the apoenzyme shows flexibility within the active site.
26013825	6	66	theme	phosphonate	1229:1239	arg1	diesters					1241:1248	neutral phosphonate diesters	1221:1248	neutral phosphonate diesters	1221:1248	The structure of GGsTop-bound hGGT1 reveals its interactions with the enzyme and why neutral phosphonate diesters are more potent inhibitors than monoanionic phosphonates.
26013825	6	66	theme	phosphonate	1229:1239	arg1	inhibitors					1266:1275	more potent inhibitors	1254:1275	more potent inhibitors than monoanionic phosphonates	1254:1305	The structure of GGsTop-bound hGGT1 reveals its interactions with the enzyme and why neutral phosphonate diesters are more potent inhibitors than monoanionic phosphonates.
26013825	8	67	theme	enzyme	1519:1524	arg1	conformation					1499:1510	the conformation	1495:1510	the conformation of the enzyme prior to release of the final product	1495:1562	The glutamate-bound structure shows the conformation of the enzyme prior to release of the final product and reveals novel information regarding the displacement of the main chain atoms that form the oxyanion hole and movement of the lid loop region when the active site is occupied.
26013825	0	68	theme	ENZYME	58:63	arg1	STRUCTURES					35:44	STRUCTURES	35:44	STRUCTURES OF THE FREE ENZYME, INHIBITOR-BOUND TETRAHEDRAL TRANSITION STATES, AND GLUTAMATE-BOUND ENZYME	35:138	Human γ-Glutamyl Transpeptidase 1: STRUCTURES OF THE FREE ENZYME, INHIBITOR-BOUND TETRAHEDRAL TRANSITION STATES, AND GLUTAMATE-BOUND ENZYME REVEAL NOVEL MOVEMENT WITHIN THE ACTIVE SITE DURING CATALYSIS.
26013825	5	69	theme	enzyme-inhibitor	1039:1054	arg1	complex					1056:1062	an enzyme-inhibitor complex	1036:1062	an enzyme-inhibitor complex that replicates the enzyme's tetrahedral intermediate/transition state	1036:1133	The serine-borate-bound hGGT1 crystal structure demonstrates that serine-borate occupies the active site of the enzyme, resulting in an enzyme-inhibitor complex that replicates the enzyme's tetrahedral intermediate/transition state.
26013825	9	70	theme	new	1762:1764	arg1	insights					1766:1773	new insights	1762:1773	new insights into the mechanism of hGGT1-catalyzed reactions	1762:1821	These data provide new insights into the mechanism of hGGT1-catalyzed reactions and will be invaluable in the development of new classes of hGGT1 inhibitors for therapeutic use.
26013825	0	71	theme	INHIBITOR-BOUND	66:80	arg1	STATES					105:110	INHIBITOR-BOUND TETRAHEDRAL TRANSITION STATES	66:110	INHIBITOR-BOUND TETRAHEDRAL TRANSITION STATES	66:110	Human γ-Glutamyl Transpeptidase 1: STRUCTURES OF THE FREE ENZYME, INHIBITOR-BOUND TETRAHEDRAL TRANSITION STATES, AND GLUTAMATE-BOUND ENZYME REVEAL NOVEL MOVEMENT WITHIN THE ACTIVE SITE DURING CATALYSIS.
26013825	2	72	theme	injury	479:484	arg1	pathology					446:454	the pathology	442:454	the pathology of asthma, reperfusion injury, and cancer	442:496	GGT1 expression is essential in cysteine homeostasis, and its induction has been implicated in the pathology of asthma, reperfusion injury, and cancer.
26013825	3	73	theme	product	805:811	arg1	release					783:789	the release	779:789	the release of this final product of the reaction	779:827	In this study, we report four new crystal structures of human GGT1 (hGGT1) that show conformational changes within the active site as the enzyme progresses from the free enzyme to inhibitor-bound tetrahedral transition states and finally to the glutamate-bound structure prior to the release of this final product of the reaction.
26013825	0	74	theme	TRANSITION	94:103	arg1	STATES					105:110	INHIBITOR-BOUND TETRAHEDRAL TRANSITION STATES	66:110	INHIBITOR-BOUND TETRAHEDRAL TRANSITION STATES	66:110	Human γ-Glutamyl Transpeptidase 1: STRUCTURES OF THE FREE ENZYME, INHIBITOR-BOUND TETRAHEDRAL TRANSITION STATES, AND GLUTAMATE-BOUND ENZYME REVEAL NOVEL MOVEMENT WITHIN THE ACTIVE SITE DURING CATALYSIS.
26013825	8	75	theme	final	1550:1554	arg1	product					1556:1562	the final product	1546:1562	the final product	1546:1562	The glutamate-bound structure shows the conformation of the enzyme prior to release of the final product and reveals novel information regarding the displacement of the main chain atoms that form the oxyanion hole and movement of the lid loop region when the active site is occupied.
26013825	7	76	theme	eukaryotic	1358:1367	arg1	GGT					1369:1371	any eukaryotic GGT	1354:1371	any eukaryotic GGT	1354:1371	These structures are the first structures for any eukaryotic GGT that include a molecule in the active site covalently bound to the catalytic Thr-381.
26013825	9	77	theme	hGGT1-catalyzed	1797:1811	arg1	reactions					1813:1821	hGGT1-catalyzed reactions	1797:1821	hGGT1-catalyzed reactions	1797:1821	These data provide new insights into the mechanism of hGGT1-catalyzed reactions and will be invaluable in the development of new classes of hGGT1 inhibitors for therapeutic use.
26013825	0	78	theme	γ-Glutamyl	6:15	arg1	Transpeptidase					17:30	Human γ-Glutamyl Transpeptidase 1	0:32	Human γ-Glutamyl Transpeptidase 1: STRUCTURES OF THE FREE ENZYME, INHIBITOR-BOUND TETRAHEDRAL TRANSITION STATES, AND GLUTAMATE-BOUND ENZYME REVEAL NOVEL MOVEMENT WITHIN THE ACTIVE SITE DURING CATALYSIS.	0:201	Human γ-Glutamyl Transpeptidase 1: STRUCTURES OF THE FREE ENZYME, INHIBITOR-BOUND TETRAHEDRAL TRANSITION STATES, AND GLUTAMATE-BOUND ENZYME REVEAL NOVEL MOVEMENT WITHIN THE ACTIVE SITE DURING CATALYSIS.
26013825	5	79	theme	intermediate/transition	1105:1127	arg1	state					1129:1133	the enzyme's tetrahedral intermediate/transition state	1080:1133	the enzyme's tetrahedral intermediate/transition state	1080:1133	The serine-borate-bound hGGT1 crystal structure demonstrates that serine-borate occupies the active site of the enzyme, resulting in an enzyme-inhibitor complex that replicates the enzyme's tetrahedral intermediate/transition state.
26013825	7	80	from	molecule	1388:1395	arg1	site					1411:1414	the active site	1400:1414	the active site covalently bound to the catalytic Thr-381	1400:1456	These structures are the first structures for any eukaryotic GGT that include a molecule in the active site covalently bound to the catalytic Thr-381.
26013825	8	81	theme	novel	1576:1580	arg1	information					1582:1592	novel information	1576:1592	novel information regarding the displacement of the main chain atoms that form the oxyanion hole and movement of the lid loop region when the active site is occupied	1576:1740	The glutamate-bound structure shows the conformation of the enzyme prior to release of the final product and reveals novel information regarding the displacement of the main chain atoms that form the oxyanion hole and movement of the lid loop region when the active site is occupied.
26013825	2	82	theme	cysteine	379:386	arg1	homeostasis					388:398	cysteine homeostasis	379:398	cysteine homeostasis	379:398	GGT1 expression is essential in cysteine homeostasis, and its induction has been implicated in the pathology of asthma, reperfusion injury, and cancer.
26013825	1	83	theme	nucleophile	268:278	arg1	hydrolase					280:288	a cell surface, N-terminal nucleophile hydrolase	241:288	hydrolase	280:288	γ-Glutamyl transpeptidase 1 (GGT1) is a cell surface, N-terminal nucleophile hydrolase that cleaves glutathione and other γ-glutamyl compounds.
26013825	1	83	theme	nucleophile	268:278	arg1	transpeptidase					214:227	γ-Glutamyl transpeptidase 1	203:229	γ-Glutamyl transpeptidase 1 (GGT1)	203:236	γ-Glutamyl transpeptidase 1 (GGT1) is a cell surface, N-terminal nucleophile hydrolase that cleaves glutathione and other γ-glutamyl compounds.
26013825	5	84	theme	hGGT1	927:931	arg1	structure					941:949	The serine-borate-bound hGGT1 crystal structure	903:949	The serine-borate-bound hGGT1 crystal structure	903:949	The serine-borate-bound hGGT1 crystal structure demonstrates that serine-borate occupies the active site of the enzyme, resulting in an enzyme-inhibitor complex that replicates the enzyme's tetrahedral intermediate/transition state.
26013825	7	85	theme	first	1333:1337	arg1	structures					1339:1348	the first structures	1329:1348	the first structures for any eukaryotic GGT that include a molecule in the active site covalently bound to the catalytic Thr-381	1329:1456	These structures are the first structures for any eukaryotic GGT that include a molecule in the active site covalently bound to the catalytic Thr-381.
26013825	7	85	theme	first	1333:1337	arg1	structures					1314:1323	These structures	1308:1323	These structures	1308:1323	These structures are the first structures for any eukaryotic GGT that include a molecule in the active site covalently bound to the catalytic Thr-381.
26013825	5	86	theme	enzyme	1015:1020	arg1	site					1003:1006	the active site	992:1006	the active site of the enzyme	992:1020	The serine-borate-bound hGGT1 crystal structure demonstrates that serine-borate occupies the active site of the enzyme, resulting in an enzyme-inhibitor complex that replicates the enzyme's tetrahedral intermediate/transition state.
26013825	5	86	theme	enzyme	1015:1020	arg1	enzyme					1015:1020	the enzyme	1011:1020	the enzyme	1011:1020	The serine-borate-bound hGGT1 crystal structure demonstrates that serine-borate occupies the active site of the enzyme, resulting in an enzyme-inhibitor complex that replicates the enzyme's tetrahedral intermediate/transition state.
26013825	1	87	theme	other	319:323	arg1	compounds					336:344	other γ-glutamyl compounds	319:344	other γ-glutamyl compounds	319:344	γ-Glutamyl transpeptidase 1 (GGT1) is a cell surface, N-terminal nucleophile hydrolase that cleaves glutathione and other γ-glutamyl compounds.
26013825	9	88	theme	new	1868:1870	arg1	classes					1872:1878	new classes	1868:1878	new classes of hGGT1 inhibitors for therapeutic use	1868:1918	These data provide new insights into the mechanism of hGGT1-catalyzed reactions and will be invaluable in the development of new classes of hGGT1 inhibitors for therapeutic use.
26013825	8	89	theme	chain	1633:1637	arg1	atoms					1639:1643	the main chain atoms	1624:1643	the main chain atoms that form the oxyanion hole and movement of the lid loop region when the active site is occupied	1624:1740	The glutamate-bound structure shows the conformation of the enzyme prior to release of the final product and reveals novel information regarding the displacement of the main chain atoms that form the oxyanion hole and movement of the lid loop region when the active site is occupied.
26013825	5	90	theme	active	996:1001	arg1	site					1003:1006	the active site	992:1006	the active site of the enzyme	992:1020	The serine-borate-bound hGGT1 crystal structure demonstrates that serine-borate occupies the active site of the enzyme, resulting in an enzyme-inhibitor complex that replicates the enzyme's tetrahedral intermediate/transition state.
26013825	5	90	theme	active	996:1001	arg1	enzyme					1015:1020	the enzyme	1011:1020	the enzyme	1011:1020	The serine-borate-bound hGGT1 crystal structure demonstrates that serine-borate occupies the active site of the enzyme, resulting in an enzyme-inhibitor complex that replicates the enzyme's tetrahedral intermediate/transition state.
26013825	8	91	theme	loop	1697:1700	arg1	region					1702:1707	the lid loop region	1689:1707	the lid loop region	1689:1707	The glutamate-bound structure shows the conformation of the enzyme prior to release of the final product and reveals novel information regarding the displacement of the main chain atoms that form the oxyanion hole and movement of the lid loop region when the active site is occupied.
19678840	4	0	theme	a	873:873	arg1	L-glutamate					876:886	(a) L-glutamate	872:886	(a) L-glutamate (a product of hydrolysis)	872:912	In the present study, we report high-resolution crystal structures of the human GCPIII ectodomain in a 'pseudo-unliganded' state and in a complex with: (a) L-glutamate (a product of hydrolysis); (b) a phosphapeptide transition state mimetic, namely (2S,3'S)-{[(3'-amino-3'-carboxy-propyl)-hydroxyphosphinoyl]methyl}-pentanedioic acid; and (c) quisqualic acid, a glutamate biostere.
19678840	5	1	theme	active	1335:1340	arg1	site					1342:1345	the bimetallic active site	1320:1345	the bimetallic active site	1320:1345	Our data reveal the overall fold and quaternary arrangement of the GCPIII molecule, define the architecture of the GCPIII substrate-binding cavity, and offer an experimental evidence for the presence of Zn(2+) ions in the bimetallic active site.
19678840	5	2	theme	fold	1130:1133	arg1	arrangement					1150:1160	the overall fold and quaternary arrangement	1118:1160	the overall fold and quaternary arrangement of the GCPIII molecule	1118:1183	Our data reveal the overall fold and quaternary arrangement of the GCPIII molecule, define the architecture of the GCPIII substrate-binding cavity, and offer an experimental evidence for the presence of Zn(2+) ions in the bimetallic active site.
19678840	4	3	theme	-hydroxyphosphinoyl	1008:1026	arg1	}					1034:1034	namely (2S,3'S)-{[(3'-amino-3'-carboxy-propyl)-hydroxyphosphinoyl]methyl}	962:1034	namely (2S,3'S)-{[(3'-amino-3'-carboxy-propyl)-hydroxyphosphinoyl]methyl}	962:1034	In the present study, we report high-resolution crystal structures of the human GCPIII ectodomain in a 'pseudo-unliganded' state and in a complex with: (a) L-glutamate (a product of hydrolysis); (b) a phosphapeptide transition state mimetic, namely (2S,3'S)-{[(3'-amino-3'-carboxy-propyl)-hydroxyphosphinoyl]methyl}-pentanedioic acid; and (c) quisqualic acid, a glutamate biostere.
19678840	4	3	theme	-hydroxyphosphinoyl	1008:1026	arg1	3'-amino-3'-carboxy-propyl					981:1006	3'-amino-3'-carboxy-propyl	981:1006	3'-amino-3'-carboxy-propyl	981:1006	In the present study, we report high-resolution crystal structures of the human GCPIII ectodomain in a 'pseudo-unliganded' state and in a complex with: (a) L-glutamate (a product of hydrolysis); (b) a phosphapeptide transition state mimetic, namely (2S,3'S)-{[(3'-amino-3'-carboxy-propyl)-hydroxyphosphinoyl]methyl}-pentanedioic acid; and (c) quisqualic acid, a glutamate biostere.
19678840	5	4	theme	quaternary	1139:1148	arg1	arrangement					1150:1160	the overall fold and quaternary arrangement	1118:1160	the overall fold and quaternary arrangement of the GCPIII molecule	1118:1183	Our data reveal the overall fold and quaternary arrangement of the GCPIII molecule, define the architecture of the GCPIII substrate-binding cavity, and offer an experimental evidence for the presence of Zn(2+) ions in the bimetallic active site.
19678840	6	5	dep	enzyme	1420:1425	arg1	the					1416:1418	the	1416:1418	the	1416:1418	Furthermore, the structures allow us to detail interactions between the enzyme and its ligands and to characterize the functional flexibility of GCPIII, which is essential for substrate recognition.
19678840	7	6	from	differences	1631:1641	arg1	occupancy					1730:1738	the occupancy	1726:1738	the occupancy of the co-catalytic zinc sites	1726:1769	A comparison of these GCPIII structures with the equivalent GCPII complexes reveals differences in the organization of specificity pockets, in surface charge distribution, and in the occupancy of the co-catalytic zinc sites.
19678840	7	6	from	differences	1631:1641	arg1	organization					1650:1661	the organization	1646:1661	the organization of specificity pockets	1646:1684	A comparison of these GCPIII structures with the equivalent GCPII complexes reveals differences in the organization of specificity pockets, in surface charge distribution, and in the occupancy of the co-catalytic zinc sites.
19678840	7	6	from	differences	1631:1641	arg1	distribution					1705:1716	surface charge distribution	1690:1716	surface charge distribution	1690:1716	A comparison of these GCPIII structures with the equivalent GCPII complexes reveals differences in the organization of specificity pockets, in surface charge distribution, and in the occupancy of the co-catalytic zinc sites.
19678840	5	7	theme	ions	1312:1315	arg1	presence					1293:1300	the presence	1289:1300	the presence of Zn(2+) ions in the bimetallic active site	1289:1345	Our data reveal the overall fold and quaternary arrangement of the GCPIII molecule, define the architecture of the GCPIII substrate-binding cavity, and offer an experimental evidence for the presence of Zn(2+) ions in the bimetallic active site.
19678840	7	8	theme	surface	1690:1696	arg1	distribution					1705:1716	surface charge distribution	1690:1716	surface charge distribution	1690:1716	A comparison of these GCPIII structures with the equivalent GCPII complexes reveals differences in the organization of specificity pockets, in surface charge distribution, and in the occupancy of the co-catalytic zinc sites.
19678840	3	9	theme	structural	593:602	arg1	properties					622:631	the structural and physiological properties	589:631	the structural and physiological properties of GCPIII	589:641	Given the potential functional and pharmacological overlap between GCPIII and GCPII, studies addressing the structural and physiological properties of GCPIII are crucial for obtaining a deeper understanding of the GCPII/GCPIII system.
19678840	7	10	gly	occupancy	1730:1738	arg2	sites					1765:1769	the co-catalytic zinc sites	1743:1769	the co-catalytic zinc sites	1743:1769	A comparison of these GCPIII structures with the equivalent GCPII complexes reveals differences in the organization of specificity pockets, in surface charge distribution, and in the occupancy of the co-catalytic zinc sites.
19678840	1	11	theme	receptor/glutamate	202:219	arg1	superfamily					263:273	the transferrin receptor/glutamate carboxypeptidase II (GCPII; EC 3.4.17.21) superfamily	186:273	the transferrin receptor/glutamate carboxypeptidase II (GCPII; EC 3.4.17.21) superfamily	186:273	Glutamate carboxypeptidase III (GCPIII) is a metalloenzyme that belongs to the transferrin receptor/glutamate carboxypeptidase II (GCPII; EC 3.4.17.21) superfamily.
19678840	1	12	theme	II	238:239	arg1	superfamily					263:273	the transferrin receptor/glutamate carboxypeptidase II (GCPII; EC 3.4.17.21) superfamily	186:273	the transferrin receptor/glutamate carboxypeptidase II (GCPII; EC 3.4.17.21) superfamily	186:273	Glutamate carboxypeptidase III (GCPIII) is a metalloenzyme that belongs to the transferrin receptor/glutamate carboxypeptidase II (GCPII; EC 3.4.17.21) superfamily.
19678840	1	13	dep	GCPII	242:246	arg1	EC					249:250	EC 3.4.17.21	249:260	GCPII; EC 3.4.17.21	242:260	Glutamate carboxypeptidase III (GCPIII) is a metalloenzyme that belongs to the transferrin receptor/glutamate carboxypeptidase II (GCPII; EC 3.4.17.21) superfamily.
19678840	4	14	dep	mimetic	953:959	arg1	-pentanedioic					1035:1047	-pentanedioic	1035:1047	-pentanedioic	1035:1047	In the present study, we report high-resolution crystal structures of the human GCPIII ectodomain in a 'pseudo-unliganded' state and in a complex with: (a) L-glutamate (a product of hydrolysis); (b) a phosphapeptide transition state mimetic, namely (2S,3'S)-{[(3'-amino-3'-carboxy-propyl)-hydroxyphosphinoyl]methyl}-pentanedioic acid; and (c) quisqualic acid, a glutamate biostere.
19678840	3	15	theme	physiological	608:620	arg1	properties					622:631	the structural and physiological properties	589:631	the structural and physiological properties of GCPIII	589:641	Given the potential functional and pharmacological overlap between GCPIII and GCPII, studies addressing the structural and physiological properties of GCPIII are crucial for obtaining a deeper understanding of the GCPII/GCPIII system.
19678840	6	16	theme	GCPIII	1493:1498	arg1	flexibility					1478:1488	the functional flexibility	1463:1488	the functional flexibility of GCPIII	1463:1498	Furthermore, the structures allow us to detail interactions between the enzyme and its ligands and to characterize the functional flexibility of GCPIII, which is essential for substrate recognition.
19678840	5	17	theme	GCPIII	1217:1222	arg1	cavity					1242:1247	the GCPIII substrate-binding cavity	1213:1247	the GCPIII substrate-binding cavity	1213:1247	Our data reveal the overall fold and quaternary arrangement of the GCPIII molecule, define the architecture of the GCPIII substrate-binding cavity, and offer an experimental evidence for the presence of Zn(2+) ions in the bimetallic active site.
19678840	8	18	theme	comparative	1955:1965	arg1	studies					1980:1986	future comparative GCPII/GCPIII studies	1948:1986	future comparative GCPII/GCPIII studies	1948:1986	The data presented here provide information that should prove to be essential for the structurally-aided design of GCPIII-specific inhibitors and might comprise guidelines for future comparative GCPII/GCPIII studies.
19678840	4	19	theme	present	727:733	arg1	study					735:739	the present study	723:739	the present study	723:739	In the present study, we report high-resolution crystal structures of the human GCPIII ectodomain in a 'pseudo-unliganded' state and in a complex with: (a) L-glutamate (a product of hydrolysis); (b) a phosphapeptide transition state mimetic, namely (2S,3'S)-{[(3'-amino-3'-carboxy-propyl)-hydroxyphosphinoyl]methyl}-pentanedioic acid; and (c) quisqualic acid, a glutamate biostere.
19678840	0	20	theme	carboxypeptidases	81:97	arg1	homology					59:66	the evolutionary and pharmacologic homology	24:66	the evolutionary and pharmacologic homology of glutamate carboxypeptidases II and III	24:108	Structural insight into the evolutionary and pharmacologic homology of glutamate carboxypeptidases II and III.
19678840	4	21	with	complex	858:864	arg1	biostere					1092:1099	a glutamate biostere	1080:1099	a glutamate biostere	1080:1099	In the present study, we report high-resolution crystal structures of the human GCPIII ectodomain in a 'pseudo-unliganded' state and in a complex with: (a) L-glutamate (a product of hydrolysis); (b) a phosphapeptide transition state mimetic, namely (2S,3'S)-{[(3'-amino-3'-carboxy-propyl)-hydroxyphosphinoyl]methyl}-pentanedioic acid; and (c) quisqualic acid, a glutamate biostere.
19678840	4	21	with	complex	858:864	arg1	acid					1049:1052	a phosphapeptide transition state mimetic, namely (2S,3'S)-{[(3'-amino-3'-carboxy-propyl)-hydroxyphosphinoyl]methyl}-pentanedioic acid	919:1052	(b) a phosphapeptide transition state mimetic, namely (2S,3'S)-{[(3'-amino-3'-carboxy-propyl)-hydroxyphosphinoyl]methyl}-pentanedioic acid	915:1052	In the present study, we report high-resolution crystal structures of the human GCPIII ectodomain in a 'pseudo-unliganded' state and in a complex with: (a) L-glutamate (a product of hydrolysis); (b) a phosphapeptide transition state mimetic, namely (2S,3'S)-{[(3'-amino-3'-carboxy-propyl)-hydroxyphosphinoyl]methyl}-pentanedioic acid; and (c) quisqualic acid, a glutamate biostere.
19678840	4	21	with	complex	858:864	arg1	acid					1074:1077	(c) quisqualic acid	1059:1077	(c) quisqualic acid	1059:1077	In the present study, we report high-resolution crystal structures of the human GCPIII ectodomain in a 'pseudo-unliganded' state and in a complex with: (a) L-glutamate (a product of hydrolysis); (b) a phosphapeptide transition state mimetic, namely (2S,3'S)-{[(3'-amino-3'-carboxy-propyl)-hydroxyphosphinoyl]methyl}-pentanedioic acid; and (c) quisqualic acid, a glutamate biostere.
19678840	4	21	with	complex	858:864	arg1	L-glutamate					876:886	(a) L-glutamate	872:886	(a) L-glutamate (a product of hydrolysis)	872:912	In the present study, we report high-resolution crystal structures of the human GCPIII ectodomain in a 'pseudo-unliganded' state and in a complex with: (a) L-glutamate (a product of hydrolysis); (b) a phosphapeptide transition state mimetic, namely (2S,3'S)-{[(3'-amino-3'-carboxy-propyl)-hydroxyphosphinoyl]methyl}-pentanedioic acid; and (c) quisqualic acid, a glutamate biostere.
19678840	4	22	theme	human	794:798	arg1	ectodomain					807:816	the human GCPIII ectodomain	790:816	the human GCPIII ectodomain	790:816	In the present study, we report high-resolution crystal structures of the human GCPIII ectodomain in a 'pseudo-unliganded' state and in a complex with: (a) L-glutamate (a product of hydrolysis); (b) a phosphapeptide transition state mimetic, namely (2S,3'S)-{[(3'-amino-3'-carboxy-propyl)-hydroxyphosphinoyl]methyl}-pentanedioic acid; and (c) quisqualic acid, a glutamate biostere.
19678840	7	23	theme	equivalent	1596:1605	arg1	complexes					1613:1621	the equivalent GCPII complexes	1592:1621	the equivalent GCPII complexes	1592:1621	A comparison of these GCPIII structures with the equivalent GCPII complexes reveals differences in the organization of specificity pockets, in surface charge distribution, and in the occupancy of the co-catalytic zinc sites.
19678840	4	24	theme	phosphapeptide	921:934	arg1	state					947:951	phosphapeptide transition state	921:951	phosphapeptide transition state	921:951	In the present study, we report high-resolution crystal structures of the human GCPIII ectodomain in a 'pseudo-unliganded' state and in a complex with: (a) L-glutamate (a product of hydrolysis); (b) a phosphapeptide transition state mimetic, namely (2S,3'S)-{[(3'-amino-3'-carboxy-propyl)-hydroxyphosphinoyl]methyl}-pentanedioic acid; and (c) quisqualic acid, a glutamate biostere.
19678840	4	25	theme	ectodomain	807:816	arg1	structures					776:785	high-resolution crystal structures	752:785	high-resolution crystal structures of the human GCPIII ectodomain in a 'pseudo-unliganded' state and in a complex with: (a) L-glutamate (a product of hydrolysis); (b) a phosphapeptide transition state mimetic, namely (2S,3'S)-{[(3'-amino-3'-carboxy-propyl)-hydroxyphosphinoyl]methyl}-pentanedioic acid; and (c) quisqualic acid, a glutamate biostere	752:1099	In the present study, we report high-resolution crystal structures of the human GCPIII ectodomain in a 'pseudo-unliganded' state and in a complex with: (a) L-glutamate (a product of hydrolysis); (b) a phosphapeptide transition state mimetic, namely (2S,3'S)-{[(3'-amino-3'-carboxy-propyl)-hydroxyphosphinoyl]methyl}-pentanedioic acid; and (c) quisqualic acid, a glutamate biostere.
19678840	5	26	attach	presence	1293:1300	arg2	ions					1312:1315	Zn(2+) ions	1305:1315	Zn(2+) ions	1305:1315	Our data reveal the overall fold and quaternary arrangement of the GCPIII molecule, define the architecture of the GCPIII substrate-binding cavity, and offer an experimental evidence for the presence of Zn(2+) ions in the bimetallic active site.
19678840	5	26	attach	presence	1293:1300	arg1	site					1342:1345	the bimetallic active site	1320:1345	the bimetallic active site	1320:1345	Our data reveal the overall fold and quaternary arrangement of the GCPIII molecule, define the architecture of the GCPIII substrate-binding cavity, and offer an experimental evidence for the presence of Zn(2+) ions in the bimetallic active site.
19678840	4	27	dep	acid	1049:1052	arg1	b					916:916	b	916:916	b	916:916	In the present study, we report high-resolution crystal structures of the human GCPIII ectodomain in a 'pseudo-unliganded' state and in a complex with: (a) L-glutamate (a product of hydrolysis); (b) a phosphapeptide transition state mimetic, namely (2S,3'S)-{[(3'-amino-3'-carboxy-propyl)-hydroxyphosphinoyl]methyl}-pentanedioic acid; and (c) quisqualic acid, a glutamate biostere.
19678840	3	28	dep	functional	505:514	arg1	overlap					536:542	overlap	536:542	overlap between GCPIII and GCPII	536:567	Given the potential functional and pharmacological overlap between GCPIII and GCPII, studies addressing the structural and physiological properties of GCPIII are crucial for obtaining a deeper understanding of the GCPII/GCPIII system.
19678840	3	28	dep	functional	505:514	arg1	the					491:493	the	491:493	the	491:493	Given the potential functional and pharmacological overlap between GCPIII and GCPII, studies addressing the structural and physiological properties of GCPIII are crucial for obtaining a deeper understanding of the GCPII/GCPIII system.
19678840	4	29	theme	crystal	768:774	arg1	structures					776:785	high-resolution crystal structures	752:785	high-resolution crystal structures of the human GCPIII ectodomain in a 'pseudo-unliganded' state and in a complex with: (a) L-glutamate (a product of hydrolysis); (b) a phosphapeptide transition state mimetic, namely (2S,3'S)-{[(3'-amino-3'-carboxy-propyl)-hydroxyphosphinoyl]methyl}-pentanedioic acid; and (c) quisqualic acid, a glutamate biostere	752:1099	In the present study, we report high-resolution crystal structures of the human GCPIII ectodomain in a 'pseudo-unliganded' state and in a complex with: (a) L-glutamate (a product of hydrolysis); (b) a phosphapeptide transition state mimetic, namely (2S,3'S)-{[(3'-amino-3'-carboxy-propyl)-hydroxyphosphinoyl]methyl}-pentanedioic acid; and (c) quisqualic acid, a glutamate biostere.
19678840	0	30	theme	Structural	0:9	arg1	insight					11:17	Structural insight	0:17	Structural insight into the evolutionary and pharmacologic homology of glutamate carboxypeptidases II and III	0:108	Structural insight into the evolutionary and pharmacologic homology of glutamate carboxypeptidases II and III.
19678840	0	31	dep	carboxypeptidases	81:97	arg1	carboxypeptidases					81:97	glutamate carboxypeptidases II and III	71:108	glutamate carboxypeptidases II and III	71:108	Structural insight into the evolutionary and pharmacologic homology of glutamate carboxypeptidases II and III.
19678840	0	31	dep	carboxypeptidases	81:97	arg1	III					106:108	III	106:108	III	106:108	Structural insight into the evolutionary and pharmacologic homology of glutamate carboxypeptidases II and III.
19678840	0	31	dep	carboxypeptidases	81:97	arg1	II					99:100	II	99:100	II	99:100	Structural insight into the evolutionary and pharmacologic homology of glutamate carboxypeptidases II and III.
19678840	7	32	theme	GCPIII	1569:1574	arg1	structures					1576:1585	these GCPIII structures	1563:1585	these GCPIII structures	1563:1585	A comparison of these GCPIII structures with the equivalent GCPII complexes reveals differences in the organization of specificity pockets, in surface charge distribution, and in the occupancy of the co-catalytic zinc sites.
19678840	5	33	theme	cavity	1242:1247	arg1	architecture					1197:1208	the architecture	1193:1208	the architecture of the GCPIII substrate-binding cavity	1193:1247	Our data reveal the overall fold and quaternary arrangement of the GCPIII molecule, define the architecture of the GCPIII substrate-binding cavity, and offer an experimental evidence for the presence of Zn(2+) ions in the bimetallic active site.
19678840	4	34	dep	acid	1074:1077	arg1	c					1060:1060	c	1060:1060	c	1060:1060	In the present study, we report high-resolution crystal structures of the human GCPIII ectodomain in a 'pseudo-unliganded' state and in a complex with: (a) L-glutamate (a product of hydrolysis); (b) a phosphapeptide transition state mimetic, namely (2S,3'S)-{[(3'-amino-3'-carboxy-propyl)-hydroxyphosphinoyl]methyl}-pentanedioic acid; and (c) quisqualic acid, a glutamate biostere.
19678840	1	35	theme	Glutamate	111:119	arg1	GCPIII					143:148	Glutamate carboxypeptidase III (GCPIII)	111:149	Glutamate carboxypeptidase III (GCPIII)	111:149	Glutamate carboxypeptidase III (GCPIII) is a metalloenzyme that belongs to the transferrin receptor/glutamate carboxypeptidase II (GCPII; EC 3.4.17.21) superfamily.
19678840	1	35	theme	Glutamate	111:119	arg1	metalloenzyme					156:168	a metalloenzyme	154:168	a metalloenzyme that belongs to the transferrin receptor/glutamate carboxypeptidase II (GCPII; EC 3.4.17.21) superfamily	154:273	Glutamate carboxypeptidase III (GCPIII) is a metalloenzyme that belongs to the transferrin receptor/glutamate carboxypeptidase II (GCPII; EC 3.4.17.21) superfamily.
19678840	0	36	theme	evolutionary	28:39	arg1	homology					59:66	the evolutionary and pharmacologic homology	24:66	the evolutionary and pharmacologic homology of glutamate carboxypeptidases II and III	24:108	Structural insight into the evolutionary and pharmacologic homology of glutamate carboxypeptidases II and III.
19678840	7	37	theme	zinc	1760:1763	arg1	sites					1765:1769	the co-catalytic zinc sites	1743:1769	the co-catalytic zinc sites	1743:1769	A comparison of these GCPIII structures with the equivalent GCPII complexes reveals differences in the organization of specificity pockets, in surface charge distribution, and in the occupancy of the co-catalytic zinc sites.
19678840	2	38	theme	prostate	468:475	arg1	cancer					477:482	prostate cancer	468:482	prostate cancer	468:482	GCPIII has been studied mainly because of its evolutionary relationship to GCPII, an enzyme involved in a variety of neuropathologies and malignancies, such as glutamatergic neurotoxicity and prostate cancer.
19678840	0	39	theme	pharmacologic	45:57	arg1	homology					59:66	the evolutionary and pharmacologic homology	24:66	the evolutionary and pharmacologic homology of glutamate carboxypeptidases II and III	24:108	Structural insight into the evolutionary and pharmacologic homology of glutamate carboxypeptidases II and III.
19678840	3	40	theme	system	712:717	arg1	understanding					678:690	a deeper understanding	669:690	a deeper understanding of the GCPII/GCPIII system	669:717	Given the potential functional and pharmacological overlap between GCPIII and GCPII, studies addressing the structural and physiological properties of GCPIII are crucial for obtaining a deeper understanding of the GCPII/GCPIII system.
19678840	6	41	theme	detail	1388:1393	arg1	interactions					1395:1406	detail interactions	1388:1406	detail interactions between the enzyme and its ligands	1388:1441	Furthermore, the structures allow us to detail interactions between the enzyme and its ligands and to characterize the functional flexibility of GCPIII, which is essential for substrate recognition.
19678840	4	42	theme	pseudo-unliganded	824:840	arg1	state					843:847	a 'pseudo-unliganded' state	821:847	a 'pseudo-unliganded' state	821:847	In the present study, we report high-resolution crystal structures of the human GCPIII ectodomain in a 'pseudo-unliganded' state and in a complex with: (a) L-glutamate (a product of hydrolysis); (b) a phosphapeptide transition state mimetic, namely (2S,3'S)-{[(3'-amino-3'-carboxy-propyl)-hydroxyphosphinoyl]methyl}-pentanedioic acid; and (c) quisqualic acid, a glutamate biostere.
19678840	5	43	theme	overall	1122:1128	arg1	arrangement					1150:1160	the overall fold and quaternary arrangement	1118:1160	the overall fold and quaternary arrangement of the GCPIII molecule	1118:1183	Our data reveal the overall fold and quaternary arrangement of the GCPIII molecule, define the architecture of the GCPIII substrate-binding cavity, and offer an experimental evidence for the presence of Zn(2+) ions in the bimetallic active site.
19678840	7	44	theme	charge	1698:1703	arg1	distribution					1705:1716	surface charge distribution	1690:1716	surface charge distribution	1690:1716	A comparison of these GCPIII structures with the equivalent GCPII complexes reveals differences in the organization of specificity pockets, in surface charge distribution, and in the occupancy of the co-catalytic zinc sites.
19678840	4	45	theme	quisqualic	1063:1072	arg1	biostere					1092:1099	a glutamate biostere	1080:1099	a glutamate biostere	1080:1099	In the present study, we report high-resolution crystal structures of the human GCPIII ectodomain in a 'pseudo-unliganded' state and in a complex with: (a) L-glutamate (a product of hydrolysis); (b) a phosphapeptide transition state mimetic, namely (2S,3'S)-{[(3'-amino-3'-carboxy-propyl)-hydroxyphosphinoyl]methyl}-pentanedioic acid; and (c) quisqualic acid, a glutamate biostere.
19678840	4	45	theme	quisqualic	1063:1072	arg1	acid					1074:1077	(c) quisqualic acid	1059:1077	(c) quisqualic acid	1059:1077	In the present study, we report high-resolution crystal structures of the human GCPIII ectodomain in a 'pseudo-unliganded' state and in a complex with: (a) L-glutamate (a product of hydrolysis); (b) a phosphapeptide transition state mimetic, namely (2S,3'S)-{[(3'-amino-3'-carboxy-propyl)-hydroxyphosphinoyl]methyl}-pentanedioic acid; and (c) quisqualic acid, a glutamate biostere.
19678840	8	46	theme	GCPIII-specific	1887:1901	arg1	inhibitors					1903:1912	GCPIII-specific inhibitors	1887:1912	GCPIII-specific inhibitors	1887:1912	The data presented here provide information that should prove to be essential for the structurally-aided design of GCPIII-specific inhibitors and might comprise guidelines for future comparative GCPII/GCPIII studies.
19678840	7	47	theme	pockets	1678:1684	arg1	organization					1650:1661	the organization	1646:1661	the organization of specificity pockets	1646:1684	A comparison of these GCPIII structures with the equivalent GCPII complexes reveals differences in the organization of specificity pockets, in surface charge distribution, and in the occupancy of the co-catalytic zinc sites.
19678840	5	48	theme	bimetallic	1324:1333	arg1	site					1342:1345	the bimetallic active site	1320:1345	the bimetallic active site	1320:1345	Our data reveal the overall fold and quaternary arrangement of the GCPIII molecule, define the architecture of the GCPIII substrate-binding cavity, and offer an experimental evidence for the presence of Zn(2+) ions in the bimetallic active site.
19678840	1	49	theme	transferrin	190:200	arg1	superfamily					263:273	the transferrin receptor/glutamate carboxypeptidase II (GCPII; EC 3.4.17.21) superfamily	186:273	the transferrin receptor/glutamate carboxypeptidase II (GCPII; EC 3.4.17.21) superfamily	186:273	Glutamate carboxypeptidase III (GCPIII) is a metalloenzyme that belongs to the transferrin receptor/glutamate carboxypeptidase II (GCPII; EC 3.4.17.21) superfamily.
19678840	4	50	theme	hydrolysis	902:911	arg1	product					891:897	a product	889:897	a product of hydrolysis	889:911	In the present study, we report high-resolution crystal structures of the human GCPIII ectodomain in a 'pseudo-unliganded' state and in a complex with: (a) L-glutamate (a product of hydrolysis); (b) a phosphapeptide transition state mimetic, namely (2S,3'S)-{[(3'-amino-3'-carboxy-propyl)-hydroxyphosphinoyl]methyl}-pentanedioic acid; and (c) quisqualic acid, a glutamate biostere.
19678840	1	51	theme	carboxypeptidase	221:236	arg1	superfamily					263:273	the transferrin receptor/glutamate carboxypeptidase II (GCPII; EC 3.4.17.21) superfamily	186:273	the transferrin receptor/glutamate carboxypeptidase II (GCPII; EC 3.4.17.21) superfamily	186:273	Glutamate carboxypeptidase III (GCPIII) is a metalloenzyme that belongs to the transferrin receptor/glutamate carboxypeptidase II (GCPII; EC 3.4.17.21) superfamily.
19678840	1	52	theme	carboxypeptidase	121:136	arg1	GCPIII					143:148	Glutamate carboxypeptidase III (GCPIII)	111:149	Glutamate carboxypeptidase III (GCPIII)	111:149	Glutamate carboxypeptidase III (GCPIII) is a metalloenzyme that belongs to the transferrin receptor/glutamate carboxypeptidase II (GCPII; EC 3.4.17.21) superfamily.
19678840	1	52	theme	carboxypeptidase	121:136	arg1	metalloenzyme					156:168	a metalloenzyme	154:168	a metalloenzyme that belongs to the transferrin receptor/glutamate carboxypeptidase II (GCPII; EC 3.4.17.21) superfamily	154:273	Glutamate carboxypeptidase III (GCPIII) is a metalloenzyme that belongs to the transferrin receptor/glutamate carboxypeptidase II (GCPII; EC 3.4.17.21) superfamily.
19678840	1	53	dep	superfamily	263:273	arg1	GCPII					242:246	GCPII	242:246	GCPII; EC 3.4.17.21	242:260	Glutamate carboxypeptidase III (GCPIII) is a metalloenzyme that belongs to the transferrin receptor/glutamate carboxypeptidase II (GCPII; EC 3.4.17.21) superfamily.
19678840	8	54	theme	structurally-aided	1858:1875	arg1	design					1877:1882	the structurally-aided design	1854:1882	the structurally-aided design of GCPIII-specific inhibitors	1854:1912	The data presented here provide information that should prove to be essential for the structurally-aided design of GCPIII-specific inhibitors and might comprise guidelines for future comparative GCPII/GCPIII studies.
19678840	7	55	theme	specificity	1666:1676	arg1	pockets					1678:1684	specificity pockets	1666:1684	specificity pockets	1666:1684	A comparison of these GCPIII structures with the equivalent GCPII complexes reveals differences in the organization of specificity pockets, in surface charge distribution, and in the occupancy of the co-catalytic zinc sites.
19678840	4	56	theme	glutamate	1082:1090	arg1	biostere					1092:1099	a glutamate biostere	1080:1099	a glutamate biostere	1080:1099	In the present study, we report high-resolution crystal structures of the human GCPIII ectodomain in a 'pseudo-unliganded' state and in a complex with: (a) L-glutamate (a product of hydrolysis); (b) a phosphapeptide transition state mimetic, namely (2S,3'S)-{[(3'-amino-3'-carboxy-propyl)-hydroxyphosphinoyl]methyl}-pentanedioic acid; and (c) quisqualic acid, a glutamate biostere.
19678840	4	56	theme	glutamate	1082:1090	arg1	acid					1074:1077	(c) quisqualic acid	1059:1077	(c) quisqualic acid	1059:1077	In the present study, we report high-resolution crystal structures of the human GCPIII ectodomain in a 'pseudo-unliganded' state and in a complex with: (a) L-glutamate (a product of hydrolysis); (b) a phosphapeptide transition state mimetic, namely (2S,3'S)-{[(3'-amino-3'-carboxy-propyl)-hydroxyphosphinoyl]methyl}-pentanedioic acid; and (c) quisqualic acid, a glutamate biostere.
19678840	0	57	theme	glutamate	71:79	arg1	carboxypeptidases					81:97	glutamate carboxypeptidases II and III	71:108	glutamate carboxypeptidases II and III	71:108	Structural insight into the evolutionary and pharmacologic homology of glutamate carboxypeptidases II and III.
19678840	0	57	theme	glutamate	71:79	arg1	III					106:108	III	106:108	III	106:108	Structural insight into the evolutionary and pharmacologic homology of glutamate carboxypeptidases II and III.
19678840	0	57	theme	glutamate	71:79	arg1	II					99:100	II	99:100	II	99:100	Structural insight into the evolutionary and pharmacologic homology of glutamate carboxypeptidases II and III.
19678840	3	58	theme	GCPIII	636:641	arg1	properties					622:631	the structural and physiological properties	589:631	the structural and physiological properties of GCPIII	589:641	Given the potential functional and pharmacological overlap between GCPIII and GCPII, studies addressing the structural and physiological properties of GCPIII are crucial for obtaining a deeper understanding of the GCPII/GCPIII system.
19678840	6	59	theme	functional	1467:1476	arg1	flexibility					1478:1488	the functional flexibility	1463:1488	the functional flexibility of GCPIII	1463:1498	Furthermore, the structures allow us to detail interactions between the enzyme and its ligands and to characterize the functional flexibility of GCPIII, which is essential for substrate recognition.
19678840	4	60	theme	transition	936:945	arg1	state					947:951	phosphapeptide transition state	921:951	phosphapeptide transition state	921:951	In the present study, we report high-resolution crystal structures of the human GCPIII ectodomain in a 'pseudo-unliganded' state and in a complex with: (a) L-glutamate (a product of hydrolysis); (b) a phosphapeptide transition state mimetic, namely (2S,3'S)-{[(3'-amino-3'-carboxy-propyl)-hydroxyphosphinoyl]methyl}-pentanedioic acid; and (c) quisqualic acid, a glutamate biostere.
19678840	5	61	theme	molecule	1176:1183	arg1	arrangement					1150:1160	the overall fold and quaternary arrangement	1118:1160	the overall fold and quaternary arrangement of the GCPIII molecule	1118:1183	Our data reveal the overall fold and quaternary arrangement of the GCPIII molecule, define the architecture of the GCPIII substrate-binding cavity, and offer an experimental evidence for the presence of Zn(2+) ions in the bimetallic active site.
19678840	8	62	theme	inhibitors	1903:1912	arg1	design					1877:1882	the structurally-aided design	1854:1882	the structurally-aided design of GCPIII-specific inhibitors	1854:1912	The data presented here provide information that should prove to be essential for the structurally-aided design of GCPIII-specific inhibitors and might comprise guidelines for future comparative GCPII/GCPIII studies.
19678840	4	63	theme	mimetic	953:959	arg1	acid					1049:1052	a phosphapeptide transition state mimetic, namely (2S,3'S)-{[(3'-amino-3'-carboxy-propyl)-hydroxyphosphinoyl]methyl}-pentanedioic acid	919:1052	(b) a phosphapeptide transition state mimetic, namely (2S,3'S)-{[(3'-amino-3'-carboxy-propyl)-hydroxyphosphinoyl]methyl}-pentanedioic acid	915:1052	In the present study, we report high-resolution crystal structures of the human GCPIII ectodomain in a 'pseudo-unliganded' state and in a complex with: (a) L-glutamate (a product of hydrolysis); (b) a phosphapeptide transition state mimetic, namely (2S,3'S)-{[(3'-amino-3'-carboxy-propyl)-hydroxyphosphinoyl]methyl}-pentanedioic acid; and (c) quisqualic acid, a glutamate biostere.
19678840	7	64	theme	GCPII	1607:1611	arg1	complexes					1613:1621	the equivalent GCPII complexes	1592:1621	the equivalent GCPII complexes	1592:1621	A comparison of these GCPIII structures with the equivalent GCPII complexes reveals differences in the organization of specificity pockets, in surface charge distribution, and in the occupancy of the co-catalytic zinc sites.
19678840	5	65	from	presence	1293:1300	arg1	site					1342:1345	the bimetallic active site	1320:1345	the bimetallic active site	1320:1345	Our data reveal the overall fold and quaternary arrangement of the GCPIII molecule, define the architecture of the GCPIII substrate-binding cavity, and offer an experimental evidence for the presence of Zn(2+) ions in the bimetallic active site.
19678840	4	66	theme	GCPIII	800:805	arg1	ectodomain					807:816	the human GCPIII ectodomain	790:816	the human GCPIII ectodomain	790:816	In the present study, we report high-resolution crystal structures of the human GCPIII ectodomain in a 'pseudo-unliganded' state and in a complex with: (a) L-glutamate (a product of hydrolysis); (b) a phosphapeptide transition state mimetic, namely (2S,3'S)-{[(3'-amino-3'-carboxy-propyl)-hydroxyphosphinoyl]methyl}-pentanedioic acid; and (c) quisqualic acid, a glutamate biostere.
19678840	5	67	theme	experimental	1263:1274	arg1	evidence					1276:1283	an experimental evidence	1260:1283	an experimental evidence for the presence of Zn(2+) ions in the bimetallic active site	1260:1345	Our data reveal the overall fold and quaternary arrangement of the GCPIII molecule, define the architecture of the GCPIII substrate-binding cavity, and offer an experimental evidence for the presence of Zn(2+) ions in the bimetallic active site.
19678840	8	68	theme	future	1948:1953	arg1	studies					1980:1986	future comparative GCPII/GCPIII studies	1948:1986	future comparative GCPII/GCPIII studies	1948:1986	The data presented here provide information that should prove to be essential for the structurally-aided design of GCPIII-specific inhibitors and might comprise guidelines for future comparative GCPII/GCPIII studies.
19678840	4	69	from	structures	776:785	arg1	state					843:847	a 'pseudo-unliganded' state	821:847	a 'pseudo-unliganded' state	821:847	In the present study, we report high-resolution crystal structures of the human GCPIII ectodomain in a 'pseudo-unliganded' state and in a complex with: (a) L-glutamate (a product of hydrolysis); (b) a phosphapeptide transition state mimetic, namely (2S,3'S)-{[(3'-amino-3'-carboxy-propyl)-hydroxyphosphinoyl]methyl}-pentanedioic acid; and (c) quisqualic acid, a glutamate biostere.
19678840	4	69	from	structures	776:785	arg1	complex					858:864	a complex	856:864	a complex with: (a) L-glutamate (a product of hydrolysis); (b) a phosphapeptide transition state mimetic, namely (2S,3'S)-{[(3'-amino-3'-carboxy-propyl)-hydroxyphosphinoyl]methyl}-pentanedioic acid; and (c) quisqualic acid, a glutamate biostere	856:1099	In the present study, we report high-resolution crystal structures of the human GCPIII ectodomain in a 'pseudo-unliganded' state and in a complex with: (a) L-glutamate (a product of hydrolysis); (b) a phosphapeptide transition state mimetic, namely (2S,3'S)-{[(3'-amino-3'-carboxy-propyl)-hydroxyphosphinoyl]methyl}-pentanedioic acid; and (c) quisqualic acid, a glutamate biostere.
19678840	2	70	theme	glutamatergic	436:448	arg1	neurotoxicity					450:462	glutamatergic neurotoxicity	436:462	glutamatergic neurotoxicity	436:462	GCPIII has been studied mainly because of its evolutionary relationship to GCPII, an enzyme involved in a variety of neuropathologies and malignancies, such as glutamatergic neurotoxicity and prostate cancer.
19678840	4	71	theme	high-resolution	752:766	arg1	structures					776:785	high-resolution crystal structures	752:785	high-resolution crystal structures of the human GCPIII ectodomain in a 'pseudo-unliganded' state and in a complex with: (a) L-glutamate (a product of hydrolysis); (b) a phosphapeptide transition state mimetic, namely (2S,3'S)-{[(3'-amino-3'-carboxy-propyl)-hydroxyphosphinoyl]methyl}-pentanedioic acid; and (c) quisqualic acid, a glutamate biostere	752:1099	In the present study, we report high-resolution crystal structures of the human GCPIII ectodomain in a 'pseudo-unliganded' state and in a complex with: (a) L-glutamate (a product of hydrolysis); (b) a phosphapeptide transition state mimetic, namely (2S,3'S)-{[(3'-amino-3'-carboxy-propyl)-hydroxyphosphinoyl]methyl}-pentanedioic acid; and (c) quisqualic acid, a glutamate biostere.
19678840	5	72	theme	substrate-binding	1224:1240	arg1	cavity					1242:1247	the GCPIII substrate-binding cavity	1213:1247	the GCPIII substrate-binding cavity	1213:1247	Our data reveal the overall fold and quaternary arrangement of the GCPIII molecule, define the architecture of the GCPIII substrate-binding cavity, and offer an experimental evidence for the presence of Zn(2+) ions in the bimetallic active site.
19678840	8	73	theme	GCPII/GCPIII	1967:1978	arg1	studies					1980:1986	future comparative GCPII/GCPIII studies	1948:1986	future comparative GCPII/GCPIII studies	1948:1986	The data presented here provide information that should prove to be essential for the structurally-aided design of GCPIII-specific inhibitors and might comprise guidelines for future comparative GCPII/GCPIII studies.
19678840	7	74	with	comparison	1549:1558	arg1	complexes					1613:1621	the equivalent GCPII complexes	1592:1621	the equivalent GCPII complexes	1592:1621	A comparison of these GCPIII structures with the equivalent GCPII complexes reveals differences in the organization of specificity pockets, in surface charge distribution, and in the occupancy of the co-catalytic zinc sites.
19678840	7	75	theme	structures	1576:1585	arg1	comparison					1549:1558	A comparison	1547:1558	A comparison of these GCPIII structures with the equivalent GCPII complexes	1547:1621	A comparison of these GCPIII structures with the equivalent GCPII complexes reveals differences in the organization of specificity pockets, in surface charge distribution, and in the occupancy of the co-catalytic zinc sites.
19678840	3	76	theme	deeper	671:676	arg1	understanding					678:690	a deeper understanding	669:690	a deeper understanding of the GCPII/GCPIII system	669:717	Given the potential functional and pharmacological overlap between GCPIII and GCPII, studies addressing the structural and physiological properties of GCPIII are crucial for obtaining a deeper understanding of the GCPII/GCPIII system.
19678840	2	77	theme	malignancies	414:425	arg1	variety					382:388	a variety	380:388	a variety of neuropathologies and malignancies, such as glutamatergic neurotoxicity and prostate cancer	380:482	GCPIII has been studied mainly because of its evolutionary relationship to GCPII, an enzyme involved in a variety of neuropathologies and malignancies, such as glutamatergic neurotoxicity and prostate cancer.
19678840	2	77	theme	malignancies	414:425	arg1	cancer					477:482	prostate cancer	468:482	prostate cancer	468:482	GCPIII has been studied mainly because of its evolutionary relationship to GCPII, an enzyme involved in a variety of neuropathologies and malignancies, such as glutamatergic neurotoxicity and prostate cancer.
19678840	2	77	theme	malignancies	414:425	arg1	neurotoxicity					450:462	glutamatergic neurotoxicity	436:462	glutamatergic neurotoxicity	436:462	GCPIII has been studied mainly because of its evolutionary relationship to GCPII, an enzyme involved in a variety of neuropathologies and malignancies, such as glutamatergic neurotoxicity and prostate cancer.
19678840	2	77	theme	malignancies	414:425	arg1	malignancies					414:425	malignancies	414:425	malignancies	414:425	GCPIII has been studied mainly because of its evolutionary relationship to GCPII, an enzyme involved in a variety of neuropathologies and malignancies, such as glutamatergic neurotoxicity and prostate cancer.
19678840	2	77	theme	malignancies	414:425	arg1	neuropathologies					393:408	neuropathologies	393:408	neuropathologies	393:408	GCPIII has been studied mainly because of its evolutionary relationship to GCPII, an enzyme involved in a variety of neuropathologies and malignancies, such as glutamatergic neurotoxicity and prostate cancer.
19678840	4	78	dep	L-glutamate	876:886	arg1	product					891:897	a product	889:897	a product of hydrolysis	889:911	In the present study, we report high-resolution crystal structures of the human GCPIII ectodomain in a 'pseudo-unliganded' state and in a complex with: (a) L-glutamate (a product of hydrolysis); (b) a phosphapeptide transition state mimetic, namely (2S,3'S)-{[(3'-amino-3'-carboxy-propyl)-hydroxyphosphinoyl]methyl}-pentanedioic acid; and (c) quisqualic acid, a glutamate biostere.
19678840	5	79	theme	Zn	1305:1306	arg1	ions					1312:1315	Zn(2+) ions	1305:1315	Zn(2+) ions	1305:1315	Our data reveal the overall fold and quaternary arrangement of the GCPIII molecule, define the architecture of the GCPIII substrate-binding cavity, and offer an experimental evidence for the presence of Zn(2+) ions in the bimetallic active site.
19678840	2	80	theme	neuropathologies	393:408	arg1	variety					382:388	a variety	380:388	a variety of neuropathologies and malignancies, such as glutamatergic neurotoxicity and prostate cancer	380:482	GCPIII has been studied mainly because of its evolutionary relationship to GCPII, an enzyme involved in a variety of neuropathologies and malignancies, such as glutamatergic neurotoxicity and prostate cancer.
19678840	2	80	theme	neuropathologies	393:408	arg1	cancer					477:482	prostate cancer	468:482	prostate cancer	468:482	GCPIII has been studied mainly because of its evolutionary relationship to GCPII, an enzyme involved in a variety of neuropathologies and malignancies, such as glutamatergic neurotoxicity and prostate cancer.
19678840	2	80	theme	neuropathologies	393:408	arg1	neurotoxicity					450:462	glutamatergic neurotoxicity	436:462	glutamatergic neurotoxicity	436:462	GCPIII has been studied mainly because of its evolutionary relationship to GCPII, an enzyme involved in a variety of neuropathologies and malignancies, such as glutamatergic neurotoxicity and prostate cancer.
19678840	2	80	theme	neuropathologies	393:408	arg1	malignancies					414:425	malignancies	414:425	malignancies	414:425	GCPIII has been studied mainly because of its evolutionary relationship to GCPII, an enzyme involved in a variety of neuropathologies and malignancies, such as glutamatergic neurotoxicity and prostate cancer.
19678840	2	80	theme	neuropathologies	393:408	arg1	neuropathologies					393:408	neuropathologies	393:408	neuropathologies	393:408	GCPIII has been studied mainly because of its evolutionary relationship to GCPII, an enzyme involved in a variety of neuropathologies and malignancies, such as glutamatergic neurotoxicity and prostate cancer.
19678840	7	81	theme	sites	1765:1769	arg1	occupancy					1730:1738	the occupancy	1726:1738	the occupancy of the co-catalytic zinc sites	1726:1769	A comparison of these GCPIII structures with the equivalent GCPII complexes reveals differences in the organization of specificity pockets, in surface charge distribution, and in the occupancy of the co-catalytic zinc sites.
19678840	3	82	theme	GCPII/GCPIII	699:710	arg1	system					712:717	the GCPII/GCPIII system	695:717	the GCPII/GCPIII system	695:717	Given the potential functional and pharmacological overlap between GCPIII and GCPII, studies addressing the structural and physiological properties of GCPIII are crucial for obtaining a deeper understanding of the GCPII/GCPIII system.
19678840	6	83	theme	substrate	1524:1532	arg1	recognition					1534:1544	substrate recognition	1524:1544	substrate recognition	1524:1544	Furthermore, the structures allow us to detail interactions between the enzyme and its ligands and to characterize the functional flexibility of GCPIII, which is essential for substrate recognition.
19678840	7	84	theme	co-catalytic	1747:1758	arg1	sites					1765:1769	the co-catalytic zinc sites	1743:1769	the co-catalytic zinc sites	1743:1769	A comparison of these GCPIII structures with the equivalent GCPII complexes reveals differences in the organization of specificity pockets, in surface charge distribution, and in the occupancy of the co-catalytic zinc sites.
19678840	4	85	theme	methyl	1028:1033	arg1	}					1034:1034	namely (2S,3'S)-{[(3'-amino-3'-carboxy-propyl)-hydroxyphosphinoyl]methyl}	962:1034	namely (2S,3'S)-{[(3'-amino-3'-carboxy-propyl)-hydroxyphosphinoyl]methyl}	962:1034	In the present study, we report high-resolution crystal structures of the human GCPIII ectodomain in a 'pseudo-unliganded' state and in a complex with: (a) L-glutamate (a product of hydrolysis); (b) a phosphapeptide transition state mimetic, namely (2S,3'S)-{[(3'-amino-3'-carboxy-propyl)-hydroxyphosphinoyl]methyl}-pentanedioic acid; and (c) quisqualic acid, a glutamate biostere.
19678840	4	85	theme	methyl	1028:1033	arg1	3'-amino-3'-carboxy-propyl					981:1006	3'-amino-3'-carboxy-propyl	981:1006	3'-amino-3'-carboxy-propyl	981:1006	In the present study, we report high-resolution crystal structures of the human GCPIII ectodomain in a 'pseudo-unliganded' state and in a complex with: (a) L-glutamate (a product of hydrolysis); (b) a phosphapeptide transition state mimetic, namely (2S,3'S)-{[(3'-amino-3'-carboxy-propyl)-hydroxyphosphinoyl]methyl}-pentanedioic acid; and (c) quisqualic acid, a glutamate biostere.
19678840	2	86	theme	evolutionary	322:333	arg1	relationship					335:346	its evolutionary relationship	318:346	its evolutionary relationship to GCPII, an enzyme involved in a variety of neuropathologies and malignancies, such as glutamatergic neurotoxicity and prostate cancer	318:482	GCPIII has been studied mainly because of its evolutionary relationship to GCPII, an enzyme involved in a variety of neuropathologies and malignancies, such as glutamatergic neurotoxicity and prostate cancer.
19678840	5	87	theme	GCPIII	1169:1174	arg1	molecule					1176:1183	the GCPIII molecule	1165:1183	the GCPIII molecule	1165:1183	Our data reveal the overall fold and quaternary arrangement of the GCPIII molecule, define the architecture of the GCPIII substrate-binding cavity, and offer an experimental evidence for the presence of Zn(2+) ions in the bimetallic active site.
22988105	2	0	theme	tumor	511:515	arg1	progression					517:527	tumor progression	511:527	tumor progression	511:527	Human meprin β is a 145-kDa disulfide-linked homodimeric multidomain type-I membrane metallopeptidase that sheds membrane-bound cytokines and growth factors, thereby contributing to inflammatory diseases, angiogenesis, and tumor progression.
22988105	2	1	theme	type-I	357:362	arg1	β					301:301	Human meprin β	288:301	Human meprin β	288:301	Human meprin β is a 145-kDa disulfide-linked homodimeric multidomain type-I membrane metallopeptidase that sheds membrane-bound cytokines and growth factors, thereby contributing to inflammatory diseases, angiogenesis, and tumor progression.
22988105	2	1	theme	type-I	357:362	arg1	metallopeptidase					373:388	a 145-kDa disulfide-linked homodimeric multidomain type-I membrane metallopeptidase	306:388	a 145-kDa disulfide-linked homodimeric multidomain type-I membrane metallopeptidase that sheds membrane-bound cytokines and growth factors, thereby contributing to inflammatory diseases, angiogenesis, and tumor progression	306:527	Human meprin β is a 145-kDa disulfide-linked homodimeric multidomain type-I membrane metallopeptidase that sheds membrane-bound cytokines and growth factors, thereby contributing to inflammatory diseases, angiogenesis, and tumor progression.
22988105	0	2	theme	metalloproteinase	61:77	arg1	function					34:41	the sheddase function	21:41	the sheddase function of human meprin β metalloproteinase at the plasma membrane	21:100	Structural basis for the sheddase function of human meprin β metalloproteinase at the plasma membrane.
22988105	6	3	link	structure-derived	1052:1068	arg1	mechanism					1078:1086	A plausible structure-derived working mechanism	1040:1086	A plausible structure-derived working mechanism	1040:1086	A plausible structure-derived working mechanism suggests that substrates such as APP are shed close to the plasma membrane surface following an "N-like" chain trace.
22988105	2	4	theme	multidomain	345:355	arg1	β					301:301	Human meprin β	288:301	Human meprin β	288:301	Human meprin β is a 145-kDa disulfide-linked homodimeric multidomain type-I membrane metallopeptidase that sheds membrane-bound cytokines and growth factors, thereby contributing to inflammatory diseases, angiogenesis, and tumor progression.
22988105	2	4	theme	multidomain	345:355	arg1	metallopeptidase					373:388	a 145-kDa disulfide-linked homodimeric multidomain type-I membrane metallopeptidase	306:388	a 145-kDa disulfide-linked homodimeric multidomain type-I membrane metallopeptidase that sheds membrane-bound cytokines and growth factors, thereby contributing to inflammatory diseases, angiogenesis, and tumor progression	306:527	Human meprin β is a 145-kDa disulfide-linked homodimeric multidomain type-I membrane metallopeptidase that sheds membrane-bound cytokines and growth factors, thereby contributing to inflammatory diseases, angiogenesis, and tumor progression.
22988105	1	5	theme	signaling	245:253	arg1	proteins					255:262	signaling proteins	245:262	signaling proteins	245:262	Ectodomain shedding at the cell surface is a major mechanism to regulate the extracellular and circulatory concentration or the activities of signaling proteins at the plasma membrane.
22988105	0	6	theme	plasma	86:91	arg1	membrane					93:100	the plasma membrane	82:100	the plasma membrane	82:100	Structural basis for the sheddase function of human meprin β metalloproteinase at the plasma membrane.
22988105	2	7	link	disulfide-linked	316:331	arg1	β					301:301	Human meprin β	288:301	Human meprin β	288:301	Human meprin β is a 145-kDa disulfide-linked homodimeric multidomain type-I membrane metallopeptidase that sheds membrane-bound cytokines and growth factors, thereby contributing to inflammatory diseases, angiogenesis, and tumor progression.
22988105	2	7	link	disulfide-linked	316:331	arg1	metallopeptidase					373:388	a 145-kDa disulfide-linked homodimeric multidomain type-I membrane metallopeptidase	306:388	a 145-kDa disulfide-linked homodimeric multidomain type-I membrane metallopeptidase that sheds membrane-bound cytokines and growth factors, thereby contributing to inflammatory diseases, angiogenesis, and tumor progression	306:527	Human meprin β is a 145-kDa disulfide-linked homodimeric multidomain type-I membrane metallopeptidase that sheds membrane-bound cytokines and growth factors, thereby contributing to inflammatory diseases, angiogenesis, and tumor progression.
22988105	6	8	theme	chain	1193:1197	arg1	trace					1199:1203	an "N-like" chain trace	1181:1203	an "N-like" chain trace	1181:1203	A plausible structure-derived working mechanism suggests that substrates such as APP are shed close to the plasma membrane surface following an "N-like" chain trace.
22988105	3	9	theme	precursor	562:570	arg1	APP					581:583	APP	581:583	APP	581:583	In addition, it cleaves amyloid precursor protein (APP) at the β-secretase site, giving rise to amyloidogenic peptides.
22988105	3	9	theme	precursor	562:570	arg1	protein					572:578	amyloid precursor protein	554:578	amyloid precursor protein (APP)	554:584	In addition, it cleaves amyloid precursor protein (APP) at the β-secretase site, giving rise to amyloidogenic peptides.
22988105	5	10	theme	sugar-rich	968:977	arg1	channel					979:985	a sugar-rich channel	966:985	a sugar-rich channel	966:985	The meprin β dimer displays a compact shape, whose catalytic domain undergoes major rearrangement upon activation, and reveals an exosite and a sugar-rich channel, both of which possibly engage in substrate binding.
22988105	1	11	theme	proteins	255:262	arg1	concentration					210:222	the extracellular and circulatory concentration	176:222	concentration	210:222	Ectodomain shedding at the cell surface is a major mechanism to regulate the extracellular and circulatory concentration or the activities of signaling proteins at the plasma membrane.
22988105	1	11	theme	proteins	255:262	arg1	activities					231:240	the activities	227:240	the activities of signaling proteins	227:262	Ectodomain shedding at the cell surface is a major mechanism to regulate the extracellular and circulatory concentration or the activities of signaling proteins at the plasma membrane.
22988105	6	12	theme	membrane	1154:1161	arg1	surface					1163:1169	the plasma membrane surface	1143:1169	the plasma membrane surface	1143:1169	A plausible structure-derived working mechanism suggests that substrates such as APP are shed close to the plasma membrane surface following an "N-like" chain trace.
22988105	4	13	theme	major	698:702	arg1	first					746:750	first	746:750	first	746:750	We have solved the X-ray crystal structure of a major fragment of the meprin β ectoprotein, the first of a multidomain oligomeric transmembrane sheddase, and of its zymogen.
22988105	4	13	theme	major	698:702	arg1	fragment					704:711	a major fragment	696:711	a major fragment of the meprin β ectoprotein	696:739	We have solved the X-ray crystal structure of a major fragment of the meprin β ectoprotein, the first of a multidomain oligomeric transmembrane sheddase, and of its zymogen.
22988105	2	14	theme	homodimeric	333:343	arg1	β					301:301	Human meprin β	288:301	Human meprin β	288:301	Human meprin β is a 145-kDa disulfide-linked homodimeric multidomain type-I membrane metallopeptidase that sheds membrane-bound cytokines and growth factors, thereby contributing to inflammatory diseases, angiogenesis, and tumor progression.
22988105	2	14	theme	homodimeric	333:343	arg1	metallopeptidase					373:388	a 145-kDa disulfide-linked homodimeric multidomain type-I membrane metallopeptidase	306:388	a 145-kDa disulfide-linked homodimeric multidomain type-I membrane metallopeptidase that sheds membrane-bound cytokines and growth factors, thereby contributing to inflammatory diseases, angiogenesis, and tumor progression	306:527	Human meprin β is a 145-kDa disulfide-linked homodimeric multidomain type-I membrane metallopeptidase that sheds membrane-bound cytokines and growth factors, thereby contributing to inflammatory diseases, angiogenesis, and tumor progression.
22988105	1	15	from	surface	135:141	arg1	shedding					114:121	Ectodomain shedding	103:121	Ectodomain shedding at the cell surface	103:141	Ectodomain shedding at the cell surface is a major mechanism to regulate the extracellular and circulatory concentration or the activities of signaling proteins at the plasma membrane.
22988105	1	15	from	surface	135:141	arg1	mechanism					154:162	a major mechanism	146:162	a major mechanism to regulate the extracellular and circulatory concentration or the activities of signaling proteins at the plasma membrane	146:285	Ectodomain shedding at the cell surface is a major mechanism to regulate the extracellular and circulatory concentration or the activities of signaling proteins at the plasma membrane.
22988105	4	16	theme	multidomain	757:767	arg1	sheddase					794:801	a multidomain oligomeric transmembrane sheddase	755:801	a multidomain oligomeric transmembrane sheddase	755:801	We have solved the X-ray crystal structure of a major fragment of the meprin β ectoprotein, the first of a multidomain oligomeric transmembrane sheddase, and of its zymogen.
22988105	4	17	theme	oligomeric	769:778	arg1	sheddase					794:801	a multidomain oligomeric transmembrane sheddase	755:801	a multidomain oligomeric transmembrane sheddase	755:801	We have solved the X-ray crystal structure of a major fragment of the meprin β ectoprotein, the first of a multidomain oligomeric transmembrane sheddase, and of its zymogen.
22988105	1	18	theme	major	148:152	arg1	mechanism					154:162	a major mechanism	146:162	a major mechanism to regulate the extracellular and circulatory concentration or the activities of signaling proteins at the plasma membrane	146:285	Ectodomain shedding at the cell surface is a major mechanism to regulate the extracellular and circulatory concentration or the activities of signaling proteins at the plasma membrane.
22988105	1	18	theme	major	148:152	arg1	shedding					114:121	Ectodomain shedding	103:121	Ectodomain shedding at the cell surface	103:141	Ectodomain shedding at the cell surface is a major mechanism to regulate the extracellular and circulatory concentration or the activities of signaling proteins at the plasma membrane.
22988105	5	19	theme	catalytic	875:883	arg1	domain					885:890	domain	885:890	domain	885:890	The meprin β dimer displays a compact shape, whose catalytic domain undergoes major rearrangement upon activation, and reveals an exosite and a sugar-rich channel, both of which possibly engage in substrate binding.
22988105	3	20	theme	amyloid	554:560	arg1	APP					581:583	APP	581:583	APP	581:583	In addition, it cleaves amyloid precursor protein (APP) at the β-secretase site, giving rise to amyloidogenic peptides.
22988105	3	20	theme	amyloid	554:560	arg1	protein					572:578	amyloid precursor protein	554:578	amyloid precursor protein (APP)	554:584	In addition, it cleaves amyloid precursor protein (APP) at the β-secretase site, giving rise to amyloidogenic peptides.
22988105	6	21	theme	working	1070:1076	arg1	mechanism					1078:1086	A plausible structure-derived working mechanism	1040:1086	A plausible structure-derived working mechanism	1040:1086	A plausible structure-derived working mechanism suggests that substrates such as APP are shed close to the plasma membrane surface following an "N-like" chain trace.
22988105	2	22	theme	membrane-bound	401:414	arg1	cytokines					416:424	membrane-bound cytokines	401:424	membrane-bound cytokines	401:424	Human meprin β is a 145-kDa disulfide-linked homodimeric multidomain type-I membrane metallopeptidase that sheds membrane-bound cytokines and growth factors, thereby contributing to inflammatory diseases, angiogenesis, and tumor progression.
22988105	2	23	theme	inflammatory	470:481	arg1	diseases					483:490	inflammatory diseases	470:490	inflammatory diseases	470:490	Human meprin β is a 145-kDa disulfide-linked homodimeric multidomain type-I membrane metallopeptidase that sheds membrane-bound cytokines and growth factors, thereby contributing to inflammatory diseases, angiogenesis, and tumor progression.
22988105	6	24	theme	structure-derived	1052:1068	arg1	mechanism					1078:1086	A plausible structure-derived working mechanism	1040:1086	A plausible structure-derived working mechanism	1040:1086	A plausible structure-derived working mechanism suggests that substrates such as APP are shed close to the plasma membrane surface following an "N-like" chain trace.
22988105	4	25	theme	ectoprotein	729:739	arg1	first					746:750	first	746:750	first	746:750	We have solved the X-ray crystal structure of a major fragment of the meprin β ectoprotein, the first of a multidomain oligomeric transmembrane sheddase, and of its zymogen.
22988105	4	25	theme	ectoprotein	729:739	arg1	fragment					704:711	a major fragment	696:711	a major fragment of the meprin β ectoprotein	696:739	We have solved the X-ray crystal structure of a major fragment of the meprin β ectoprotein, the first of a multidomain oligomeric transmembrane sheddase, and of its zymogen.
22988105	4	26	theme	crystal	675:681	arg1	structure					683:691	the X-ray crystal structure	665:691	the X-ray crystal structure of a major fragment of the meprin β ectoprotein, the first of a multidomain oligomeric transmembrane sheddase, and of its zymogen	665:821	We have solved the X-ray crystal structure of a major fragment of the meprin β ectoprotein, the first of a multidomain oligomeric transmembrane sheddase, and of its zymogen.
22988105	0	27	theme	Structural	0:9	arg1	basis					11:15	Structural basis	0:15	Structural basis for the sheddase function of human meprin β metalloproteinase at the plasma membrane.	0:101	Structural basis for the sheddase function of human meprin β metalloproteinase at the plasma membrane.
22988105	4	28	theme	β	727:727	arg1	ectoprotein					729:739	the meprin β ectoprotein	716:739	the meprin β ectoprotein	716:739	We have solved the X-ray crystal structure of a major fragment of the meprin β ectoprotein, the first of a multidomain oligomeric transmembrane sheddase, and of its zymogen.
22988105	4	29	theme	X-ray	669:673	arg1	structure					683:691	the X-ray crystal structure	665:691	the X-ray crystal structure of a major fragment of the meprin β ectoprotein, the first of a multidomain oligomeric transmembrane sheddase, and of its zymogen	665:821	We have solved the X-ray crystal structure of a major fragment of the meprin β ectoprotein, the first of a multidomain oligomeric transmembrane sheddase, and of its zymogen.
22988105	1	30	theme	plasma	271:276	arg1	membrane					278:285	the plasma membrane	267:285	the plasma membrane	267:285	Ectodomain shedding at the cell surface is a major mechanism to regulate the extracellular and circulatory concentration or the activities of signaling proteins at the plasma membrane.
22988105	6	31	theme	"	1191:1191	arg1	chain					1193:1197	an "N-like" chain	1181:1197	an "N-like" chain trace	1181:1203	A plausible structure-derived working mechanism suggests that substrates such as APP are shed close to the plasma membrane surface following an "N-like" chain trace.
22988105	2	32	theme	meprin	294:299	arg1	β					301:301	Human meprin β	288:301	Human meprin β	288:301	Human meprin β is a 145-kDa disulfide-linked homodimeric multidomain type-I membrane metallopeptidase that sheds membrane-bound cytokines and growth factors, thereby contributing to inflammatory diseases, angiogenesis, and tumor progression.
22988105	2	32	theme	meprin	294:299	arg1	metallopeptidase					373:388	a 145-kDa disulfide-linked homodimeric multidomain type-I membrane metallopeptidase	306:388	a 145-kDa disulfide-linked homodimeric multidomain type-I membrane metallopeptidase that sheds membrane-bound cytokines and growth factors, thereby contributing to inflammatory diseases, angiogenesis, and tumor progression	306:527	Human meprin β is a 145-kDa disulfide-linked homodimeric multidomain type-I membrane metallopeptidase that sheds membrane-bound cytokines and growth factors, thereby contributing to inflammatory diseases, angiogenesis, and tumor progression.
22988105	6	33	theme	plasma	1147:1152	arg1	surface					1163:1169	the plasma membrane surface	1143:1169	the plasma membrane surface	1143:1169	A plausible structure-derived working mechanism suggests that substrates such as APP are shed close to the plasma membrane surface following an "N-like" chain trace.
22988105	2	34	theme	Human	288:292	arg1	β					301:301	Human meprin β	288:301	Human meprin β	288:301	Human meprin β is a 145-kDa disulfide-linked homodimeric multidomain type-I membrane metallopeptidase that sheds membrane-bound cytokines and growth factors, thereby contributing to inflammatory diseases, angiogenesis, and tumor progression.
22988105	2	34	theme	Human	288:292	arg1	metallopeptidase					373:388	a 145-kDa disulfide-linked homodimeric multidomain type-I membrane metallopeptidase	306:388	a 145-kDa disulfide-linked homodimeric multidomain type-I membrane metallopeptidase that sheds membrane-bound cytokines and growth factors, thereby contributing to inflammatory diseases, angiogenesis, and tumor progression	306:527	Human meprin β is a 145-kDa disulfide-linked homodimeric multidomain type-I membrane metallopeptidase that sheds membrane-bound cytokines and growth factors, thereby contributing to inflammatory diseases, angiogenesis, and tumor progression.
22988105	1	35	theme	extracellular	180:192	arg1	concentration					210:222	the extracellular and circulatory concentration	176:222	concentration	210:222	Ectodomain shedding at the cell surface is a major mechanism to regulate the extracellular and circulatory concentration or the activities of signaling proteins at the plasma membrane.
22988105	4	36	theme	fragment	704:711	arg1	structure					683:691	the X-ray crystal structure	665:691	the X-ray crystal structure of a major fragment of the meprin β ectoprotein, the first of a multidomain oligomeric transmembrane sheddase, and of its zymogen	665:821	We have solved the X-ray crystal structure of a major fragment of the meprin β ectoprotein, the first of a multidomain oligomeric transmembrane sheddase, and of its zymogen.
22988105	5	37	theme	meprin	828:833	arg1	dimer					837:841	The meprin β dimer	824:841	The meprin β dimer	824:841	The meprin β dimer displays a compact shape, whose catalytic domain undergoes major rearrangement upon activation, and reveals an exosite and a sugar-rich channel, both of which possibly engage in substrate binding.
22988105	5	38	theme	compact	854:860	arg1	shape					862:866	a compact shape	852:866	a compact shape	852:866	The meprin β dimer displays a compact shape, whose catalytic domain undergoes major rearrangement upon activation, and reveals an exosite and a sugar-rich channel, both of which possibly engage in substrate binding.
22988105	2	39	theme	growth	430:435	arg1	factors					437:443	growth factors	430:443	growth factors	430:443	Human meprin β is a 145-kDa disulfide-linked homodimeric multidomain type-I membrane metallopeptidase that sheds membrane-bound cytokines and growth factors, thereby contributing to inflammatory diseases, angiogenesis, and tumor progression.
22988105	0	40	theme	sheddase	25:32	arg1	function					34:41	the sheddase function	21:41	the sheddase function of human meprin β metalloproteinase at the plasma membrane	21:100	Structural basis for the sheddase function of human meprin β metalloproteinase at the plasma membrane.
22988105	1	41	theme	circulatory	198:208	arg1	concentration					210:222	the extracellular and circulatory concentration	176:222	concentration	210:222	Ectodomain shedding at the cell surface is a major mechanism to regulate the extracellular and circulatory concentration or the activities of signaling proteins at the plasma membrane.
22988105	0	42	theme	human	46:50	arg1	metalloproteinase					61:77	human meprin β metalloproteinase	46:77	human meprin β metalloproteinase	46:77	Structural basis for the sheddase function of human meprin β metalloproteinase at the plasma membrane.
22988105	4	43	theme	zymogen	815:821	arg1	structure					683:691	the X-ray crystal structure	665:691	the X-ray crystal structure of a major fragment of the meprin β ectoprotein, the first of a multidomain oligomeric transmembrane sheddase, and of its zymogen	665:821	We have solved the X-ray crystal structure of a major fragment of the meprin β ectoprotein, the first of a multidomain oligomeric transmembrane sheddase, and of its zymogen.
22988105	6	44	theme	N-like	1185:1190	arg1	chain					1193:1197	an "N-like" chain	1181:1197	an "N-like" chain trace	1181:1203	A plausible structure-derived working mechanism suggests that substrates such as APP are shed close to the plasma membrane surface following an "N-like" chain trace.
22988105	1	45	theme	Ectodomain	103:112	arg1	shedding					114:121	Ectodomain shedding	103:121	Ectodomain shedding at the cell surface	103:141	Ectodomain shedding at the cell surface is a major mechanism to regulate the extracellular and circulatory concentration or the activities of signaling proteins at the plasma membrane.
22988105	1	45	theme	Ectodomain	103:112	arg1	mechanism					154:162	a major mechanism	146:162	a major mechanism to regulate the extracellular and circulatory concentration or the activities of signaling proteins at the plasma membrane	146:285	Ectodomain shedding at the cell surface is a major mechanism to regulate the extracellular and circulatory concentration or the activities of signaling proteins at the plasma membrane.
22988105	3	46	theme	β-secretase	593:603	arg1	site					605:608	the β-secretase site	589:608	the β-secretase site	589:608	In addition, it cleaves amyloid precursor protein (APP) at the β-secretase site, giving rise to amyloidogenic peptides.
22988105	2	47	theme	disulfide-linked	316:331	arg1	β					301:301	Human meprin β	288:301	Human meprin β	288:301	Human meprin β is a 145-kDa disulfide-linked homodimeric multidomain type-I membrane metallopeptidase that sheds membrane-bound cytokines and growth factors, thereby contributing to inflammatory diseases, angiogenesis, and tumor progression.
22988105	2	47	theme	disulfide-linked	316:331	arg1	metallopeptidase					373:388	a 145-kDa disulfide-linked homodimeric multidomain type-I membrane metallopeptidase	306:388	a 145-kDa disulfide-linked homodimeric multidomain type-I membrane metallopeptidase that sheds membrane-bound cytokines and growth factors, thereby contributing to inflammatory diseases, angiogenesis, and tumor progression	306:527	Human meprin β is a 145-kDa disulfide-linked homodimeric multidomain type-I membrane metallopeptidase that sheds membrane-bound cytokines and growth factors, thereby contributing to inflammatory diseases, angiogenesis, and tumor progression.
22988105	0	48	from	membrane	93:100	arg1	function					34:41	the sheddase function	21:41	the sheddase function of human meprin β metalloproteinase at the plasma membrane	21:100	Structural basis for the sheddase function of human meprin β metalloproteinase at the plasma membrane.
22988105	4	49	theme	transmembrane	780:792	arg1	sheddase					794:801	a multidomain oligomeric transmembrane sheddase	755:801	a multidomain oligomeric transmembrane sheddase	755:801	We have solved the X-ray crystal structure of a major fragment of the meprin β ectoprotein, the first of a multidomain oligomeric transmembrane sheddase, and of its zymogen.
22988105	2	50	theme	145-kDa	308:314	arg1	β					301:301	Human meprin β	288:301	Human meprin β	288:301	Human meprin β is a 145-kDa disulfide-linked homodimeric multidomain type-I membrane metallopeptidase that sheds membrane-bound cytokines and growth factors, thereby contributing to inflammatory diseases, angiogenesis, and tumor progression.
22988105	2	50	theme	145-kDa	308:314	arg1	metallopeptidase					373:388	a 145-kDa disulfide-linked homodimeric multidomain type-I membrane metallopeptidase	306:388	a 145-kDa disulfide-linked homodimeric multidomain type-I membrane metallopeptidase that sheds membrane-bound cytokines and growth factors, thereby contributing to inflammatory diseases, angiogenesis, and tumor progression	306:527	Human meprin β is a 145-kDa disulfide-linked homodimeric multidomain type-I membrane metallopeptidase that sheds membrane-bound cytokines and growth factors, thereby contributing to inflammatory diseases, angiogenesis, and tumor progression.
22988105	5	51	theme	major	902:906	arg1	rearrangement					908:920	major rearrangement	902:920	major rearrangement	902:920	The meprin β dimer displays a compact shape, whose catalytic domain undergoes major rearrangement upon activation, and reveals an exosite and a sugar-rich channel, both of which possibly engage in substrate binding.
22988105	5	52	theme	substrate	1021:1029	arg1	binding					1031:1037	substrate binding	1021:1037	substrate binding	1021:1037	The meprin β dimer displays a compact shape, whose catalytic domain undergoes major rearrangement upon activation, and reveals an exosite and a sugar-rich channel, both of which possibly engage in substrate binding.
22988105	3	53	theme	amyloidogenic	626:638	arg1	peptides					640:647	amyloidogenic peptides	626:647	amyloidogenic peptides	626:647	In addition, it cleaves amyloid precursor protein (APP) at the β-secretase site, giving rise to amyloidogenic peptides.
22988105	4	54	theme	meprin	720:725	arg1	ectoprotein					729:739	the meprin β ectoprotein	716:739	the meprin β ectoprotein	716:739	We have solved the X-ray crystal structure of a major fragment of the meprin β ectoprotein, the first of a multidomain oligomeric transmembrane sheddase, and of its zymogen.
22988105	0	55	theme	β	59:59	arg1	metalloproteinase					61:77	human meprin β metalloproteinase	46:77	human meprin β metalloproteinase	46:77	Structural basis for the sheddase function of human meprin β metalloproteinase at the plasma membrane.
22988105	5	56	theme	β	835:835	arg1	dimer					837:841	The meprin β dimer	824:841	The meprin β dimer	824:841	The meprin β dimer displays a compact shape, whose catalytic domain undergoes major rearrangement upon activation, and reveals an exosite and a sugar-rich channel, both of which possibly engage in substrate binding.
22988105	1	57	theme	cell	130:133	arg1	surface					135:141	the cell surface	126:141	the cell surface	126:141	Ectodomain shedding at the cell surface is a major mechanism to regulate the extracellular and circulatory concentration or the activities of signaling proteins at the plasma membrane.
22988105	6	58	theme	plausible	1042:1050	arg1	mechanism					1078:1086	A plausible structure-derived working mechanism	1040:1086	A plausible structure-derived working mechanism	1040:1086	A plausible structure-derived working mechanism suggests that substrates such as APP are shed close to the plasma membrane surface following an "N-like" chain trace.
22988105	0	59	theme	meprin	52:57	arg1	metalloproteinase					61:77	human meprin β metalloproteinase	46:77	human meprin β metalloproteinase	46:77	Structural basis for the sheddase function of human meprin β metalloproteinase at the plasma membrane.
22988105	4	60	theme	sheddase	794:801	arg1	fragment					704:711	a major fragment	696:711	a major fragment of the meprin β ectoprotein	696:739	We have solved the X-ray crystal structure of a major fragment of the meprin β ectoprotein, the first of a multidomain oligomeric transmembrane sheddase, and of its zymogen.
22988105	4	60	theme	sheddase	794:801	arg1	first					746:750	first	746:750	first	746:750	We have solved the X-ray crystal structure of a major fragment of the meprin β ectoprotein, the first of a multidomain oligomeric transmembrane sheddase, and of its zymogen.
22988105	2	61	theme	membrane	364:371	arg1	β					301:301	Human meprin β	288:301	Human meprin β	288:301	Human meprin β is a 145-kDa disulfide-linked homodimeric multidomain type-I membrane metallopeptidase that sheds membrane-bound cytokines and growth factors, thereby contributing to inflammatory diseases, angiogenesis, and tumor progression.
22988105	2	61	theme	membrane	364:371	arg1	metallopeptidase					373:388	a 145-kDa disulfide-linked homodimeric multidomain type-I membrane metallopeptidase	306:388	a 145-kDa disulfide-linked homodimeric multidomain type-I membrane metallopeptidase that sheds membrane-bound cytokines and growth factors, thereby contributing to inflammatory diseases, angiogenesis, and tumor progression	306:527	Human meprin β is a 145-kDa disulfide-linked homodimeric multidomain type-I membrane metallopeptidase that sheds membrane-bound cytokines and growth factors, thereby contributing to inflammatory diseases, angiogenesis, and tumor progression.
26117840	2	0	from	force	444:448	arg1	mode					484:487	a so-called catch-bond binding mode	453:487	a so-called catch-bond binding mode	453:487	Efficient leukocyte recruitment under vascular flow conditions depends on an increased lifetime of E-selectin/ligand complexes under tensile force in a so-called catch-bond binding mode.
26117840	3	1	theme	representative	517:530	arg1	fragment					532:539	a representative fragment	515:539	a representative fragment of the extracellular E-selectin region with sLe(x)	515:590	Co-crystal structures of a representative fragment of the extracellular E-selectin region with sLe(x) and a glycomimetic antagonist thereof reveal an extended E-selectin conformation, which is identified as a high-affinity binding state of E-selectin by molecular dynamics simulations.
26117840	4	2	from	conditions	920:929	arg1	solution					934:941	solution	934:941	solution	934:941	Small-angle X-ray scattering experiments demonstrate a direct link between ligand binding and E-selectin conformational transition under static conditions in solution.
26117840	3	3	theme	high-affinity	699:711	arg1	state					721:725	a high-affinity binding state	697:725	a high-affinity binding state of E-selectin	697:739	Co-crystal structures of a representative fragment of the extracellular E-selectin region with sLe(x) and a glycomimetic antagonist thereof reveal an extended E-selectin conformation, which is identified as a high-affinity binding state of E-selectin by molecular dynamics simulations.
26117840	3	3	theme	high-affinity	699:711	arg1	conformation					660:671	an extended E-selectin conformation	637:671	an extended E-selectin conformation	637:671	Co-crystal structures of a representative fragment of the extracellular E-selectin region with sLe(x) and a glycomimetic antagonist thereof reveal an extended E-selectin conformation, which is identified as a high-affinity binding state of E-selectin by molecular dynamics simulations.
26117840	2	4	theme	flow	350:353	arg1	conditions					355:364	vascular flow conditions	341:364	vascular flow conditions	341:364	Efficient leukocyte recruitment under vascular flow conditions depends on an increased lifetime of E-selectin/ligand complexes under tensile force in a so-called catch-bond binding mode.
26117840	7	5	theme	pan-selectin	1362:1373	arg1	antagonists					1375:1385	the pan-selectin antagonists	1358:1385	the pan-selectin antagonists GMI-1070 (Rivipansel)	1358:1407	This is of special interest, since their therapeutic potential was recently demonstrated with the pan-selectin antagonists GMI-1070 (Rivipansel).
26117840	3	6	theme	binding	713:719	arg1	state					721:725	a high-affinity binding state	697:725	a high-affinity binding state of E-selectin	697:739	Co-crystal structures of a representative fragment of the extracellular E-selectin region with sLe(x) and a glycomimetic antagonist thereof reveal an extended E-selectin conformation, which is identified as a high-affinity binding state of E-selectin by molecular dynamics simulations.
26117840	3	6	theme	binding	713:719	arg1	conformation					660:671	an extended E-selectin conformation	637:671	an extended E-selectin conformation	637:671	Co-crystal structures of a representative fragment of the extracellular E-selectin region with sLe(x) and a glycomimetic antagonist thereof reveal an extended E-selectin conformation, which is identified as a high-affinity binding state of E-selectin by molecular dynamics simulations.
26117840	5	7	theme	recruitment	1129:1139	arg1	binding					1024:1030	ligand binding	1017:1030	ligand binding to conformational stretching	1017:1059	This permits tracing a series of concerted structural changes connecting ligand binding to conformational stretching as the structural basis of E-selectin catch-bond-mediated leukocyte recruitment.
26117840	5	7	theme	recruitment	1129:1139	arg1	basis					1079:1083	the structural basis	1064:1083	the structural basis of E-selectin catch-bond-mediated leukocyte recruitment	1064:1139	This permits tracing a series of concerted structural changes connecting ligand binding to conformational stretching as the structural basis of E-selectin catch-bond-mediated leukocyte recruitment.
26117840	3	8	theme	region	573:578	arg1	fragment					532:539	a representative fragment	515:539	a representative fragment of the extracellular E-selectin region with sLe(x)	515:590	Co-crystal structures of a representative fragment of the extracellular E-selectin region with sLe(x) and a glycomimetic antagonist thereof reveal an extended E-selectin conformation, which is identified as a high-affinity binding state of E-selectin by molecular dynamics simulations.
26117840	4	9	theme	Small-angle	776:786	arg1	scattering					794:803	Small-angle X-ray scattering	776:803	Small-angle X-ray scattering experiments	776:815	Small-angle X-ray scattering experiments demonstrate a direct link between ligand binding and E-selectin conformational transition under static conditions in solution.
26117840	5	10	theme	conformational	1035:1048	arg1	stretching					1050:1059	conformational stretching	1035:1059	conformational stretching	1035:1059	This permits tracing a series of concerted structural changes connecting ligand binding to conformational stretching as the structural basis of E-selectin catch-bond-mediated leukocyte recruitment.
26117840	2	11	theme	Efficient	303:311	arg1	recruitment					323:333	Efficient leukocyte recruitment	303:333	Efficient leukocyte recruitment under vascular flow conditions	303:364	Efficient leukocyte recruitment under vascular flow conditions depends on an increased lifetime of E-selectin/ligand complexes under tensile force in a so-called catch-bond binding mode.
26117840	3	12	theme	molecular	744:752	arg1	simulations					763:773	molecular dynamics simulations	744:773	molecular dynamics simulations	744:773	Co-crystal structures of a representative fragment of the extracellular E-selectin region with sLe(x) and a glycomimetic antagonist thereof reveal an extended E-selectin conformation, which is identified as a high-affinity binding state of E-selectin by molecular dynamics simulations.
26117840	4	13	theme	direct	831:836	arg1	link					838:841	a direct link	829:841	a direct link between ligand binding and E-selectin conformational transition	829:905	Small-angle X-ray scattering experiments demonstrate a direct link between ligand binding and E-selectin conformational transition under static conditions in solution.
26117840	4	14	theme	scattering	794:803	arg1	experiments					805:815	Small-angle X-ray scattering experiments	776:815	Small-angle X-ray scattering experiments	776:815	Small-angle X-ray scattering experiments demonstrate a direct link between ligand binding and E-selectin conformational transition under static conditions in solution.
26117840	5	15	theme	changes	998:1004	arg1	series					967:972	a series	965:972	a series of concerted structural changes connecting ligand binding to conformational stretching as the structural basis of E-selectin catch-bond-mediated leukocyte recruitment	965:1139	This permits tracing a series of concerted structural changes connecting ligand binding to conformational stretching as the structural basis of E-selectin catch-bond-mediated leukocyte recruitment.
26117840	2	16	theme	vascular	341:348	arg1	conditions					355:364	vascular flow conditions	341:364	vascular flow conditions	341:364	Efficient leukocyte recruitment under vascular flow conditions depends on an increased lifetime of E-selectin/ligand complexes under tensile force in a so-called catch-bond binding mode.
26117840	3	17	theme	extracellular	548:560	arg1	region					573:578	the extracellular E-selectin region	544:578	the extracellular E-selectin region with sLe(x)	544:590	Co-crystal structures of a representative fragment of the extracellular E-selectin region with sLe(x) and a glycomimetic antagonist thereof reveal an extended E-selectin conformation, which is identified as a high-affinity binding state of E-selectin by molecular dynamics simulations.
26117840	2	18	theme	increased	380:388	arg1	lifetime					390:397	an increased lifetime	377:397	an increased lifetime of E-selectin/ligand complexes under tensile force in a so-called catch-bond binding mode	377:487	Efficient leukocyte recruitment under vascular flow conditions depends on an increased lifetime of E-selectin/ligand complexes under tensile force in a so-called catch-bond binding mode.
26117840	6	19	theme	site	1185:1188	arg1	view					1165:1168	The detailed molecular view	1142:1168	The detailed molecular view of the binding site	1142:1188	The detailed molecular view of the binding site paves the way for the design of a new generation of selectin antagonists.
26117840	0	20	theme	high-affinity	46:58	arg1	conformation					60:71	an extended high-affinity conformation	34:71	an extended high-affinity conformation	34:71	E-selectin ligand complexes adopt an extended high-affinity conformation.
26117840	3	21	theme	E-selectin	730:739	arg1	state					721:725	a high-affinity binding state	697:725	a high-affinity binding state of E-selectin	697:739	Co-crystal structures of a representative fragment of the extracellular E-selectin region with sLe(x) and a glycomimetic antagonist thereof reveal an extended E-selectin conformation, which is identified as a high-affinity binding state of E-selectin by molecular dynamics simulations.
26117840	3	21	theme	E-selectin	730:739	arg1	conformation					660:671	an extended E-selectin conformation	637:671	an extended E-selectin conformation	637:671	Co-crystal structures of a representative fragment of the extracellular E-selectin region with sLe(x) and a glycomimetic antagonist thereof reveal an extended E-selectin conformation, which is identified as a high-affinity binding state of E-selectin by molecular dynamics simulations.
26117840	2	22	theme	so-called	455:463	arg1	mode					484:487	a so-called catch-bond binding mode	453:487	a so-called catch-bond binding mode	453:487	Efficient leukocyte recruitment under vascular flow conditions depends on an increased lifetime of E-selectin/ligand complexes under tensile force in a so-called catch-bond binding mode.
26117840	1	23	theme	early	190:194	arg1	response					209:216	the early inflammatory response	186:216	the early inflammatory response	186:216	E-selectin is a cell-adhesion molecule of the vascular endothelium that promotes essential leukocyte rolling in the early inflammatory response by binding to glycoproteins containing the tetrasaccharide sialyl Lewis(x) (sLe(x)).
26117840	0	24	theme	ligand	11:16	arg1	complexes					18:26	E-selectin ligand complexes	0:26	E-selectin ligand complexes	0:26	E-selectin ligand complexes adopt an extended high-affinity conformation.
26117840	6	25	theme	selectin	1242:1249	arg1	antagonists					1251:1261	selectin antagonists	1242:1261	selectin antagonists	1242:1261	The detailed molecular view of the binding site paves the way for the design of a new generation of selectin antagonists.
26117840	1	26	gly	glycoproteins	232:244	arg1	glycoproteins					232:244	glycoproteins	232:244	glycoproteins containing the tetrasaccharide sialyl Lewis(x) (sLe(x))	232:300	E-selectin is a cell-adhesion molecule of the vascular endothelium that promotes essential leukocyte rolling in the early inflammatory response by binding to glycoproteins containing the tetrasaccharide sialyl Lewis(x) (sLe(x)).
26117840	1	27	theme	cell-adhesion	90:102	arg1	molecule					104:111	a cell-adhesion molecule	88:111	a cell-adhesion molecule of the vascular endothelium that promotes essential leukocyte rolling in the early inflammatory response by binding to glycoproteins containing the tetrasaccharide sialyl Lewis(x) (sLe(x))	88:300	E-selectin is a cell-adhesion molecule of the vascular endothelium that promotes essential leukocyte rolling in the early inflammatory response by binding to glycoproteins containing the tetrasaccharide sialyl Lewis(x) (sLe(x)).
26117840	1	27	theme	cell-adhesion	90:102	arg1	E-selectin					74:83	E-selectin	74:83	E-selectin	74:83	E-selectin is a cell-adhesion molecule of the vascular endothelium that promotes essential leukocyte rolling in the early inflammatory response by binding to glycoproteins containing the tetrasaccharide sialyl Lewis(x) (sLe(x)).
26117840	3	28	theme	dynamics	754:761	arg1	simulations					763:773	molecular dynamics simulations	744:773	molecular dynamics simulations	744:773	Co-crystal structures of a representative fragment of the extracellular E-selectin region with sLe(x) and a glycomimetic antagonist thereof reveal an extended E-selectin conformation, which is identified as a high-affinity binding state of E-selectin by molecular dynamics simulations.
26117840	1	29	theme	inflammatory	196:207	arg1	response					209:216	the early inflammatory response	186:216	the early inflammatory response	186:216	E-selectin is a cell-adhesion molecule of the vascular endothelium that promotes essential leukocyte rolling in the early inflammatory response by binding to glycoproteins containing the tetrasaccharide sialyl Lewis(x) (sLe(x)).
26117840	0	30	theme	E-selectin	0:9	arg1	complexes					18:26	E-selectin ligand complexes	0:26	E-selectin ligand complexes	0:26	E-selectin ligand complexes adopt an extended high-affinity conformation.
26117840	4	31	theme	static	913:918	arg1	conditions					920:929	static conditions	913:929	static conditions in solution	913:941	Small-angle X-ray scattering experiments demonstrate a direct link between ligand binding and E-selectin conformational transition under static conditions in solution.
26117840	5	32	theme	ligand	1017:1022	arg1	binding					1024:1030	ligand binding	1017:1030	ligand binding to conformational stretching	1017:1059	This permits tracing a series of concerted structural changes connecting ligand binding to conformational stretching as the structural basis of E-selectin catch-bond-mediated leukocyte recruitment.
26117840	5	32	theme	ligand	1017:1022	arg1	basis					1079:1083	the structural basis	1064:1083	the structural basis of E-selectin catch-bond-mediated leukocyte recruitment	1064:1139	This permits tracing a series of concerted structural changes connecting ligand binding to conformational stretching as the structural basis of E-selectin catch-bond-mediated leukocyte recruitment.
26117840	4	33	theme	E-selectin	870:879	arg1	transition					896:905	E-selectin conformational transition	870:905	E-selectin conformational transition	870:905	Small-angle X-ray scattering experiments demonstrate a direct link between ligand binding and E-selectin conformational transition under static conditions in solution.
26117840	4	34	theme	X-ray	788:792	arg1	scattering					794:803	Small-angle X-ray scattering	776:803	Small-angle X-ray scattering experiments	776:815	Small-angle X-ray scattering experiments demonstrate a direct link between ligand binding and E-selectin conformational transition under static conditions in solution.
26117840	5	35	theme	catch-bond-mediated	1099:1117	arg1	recruitment					1129:1139	E-selectin catch-bond-mediated leukocyte recruitment	1088:1139	E-selectin catch-bond-mediated leukocyte recruitment	1088:1139	This permits tracing a series of concerted structural changes connecting ligand binding to conformational stretching as the structural basis of E-selectin catch-bond-mediated leukocyte recruitment.
26117840	2	36	theme	tensile	436:442	arg1	force					444:448	tensile force	436:448	tensile force in a so-called catch-bond binding mode	436:487	Efficient leukocyte recruitment under vascular flow conditions depends on an increased lifetime of E-selectin/ligand complexes under tensile force in a so-called catch-bond binding mode.
26117840	7	37	dep	antagonists	1375:1385	arg1	Rivipansel					1397:1406	Rivipansel	1397:1406	Rivipansel	1397:1406	This is of special interest, since their therapeutic potential was recently demonstrated with the pan-selectin antagonists GMI-1070 (Rivipansel).
26117840	7	37	dep	antagonists	1375:1385	arg1	GMI-1070					1387:1394	GMI-1070	1387:1394	the pan-selectin antagonists GMI-1070 (Rivipansel)	1358:1407	This is of special interest, since their therapeutic potential was recently demonstrated with the pan-selectin antagonists GMI-1070 (Rivipansel).
26117840	3	38	theme	fragment	532:539	arg1	antagonist					611:620	a glycomimetic antagonist	596:620	a glycomimetic antagonist	596:620	Co-crystal structures of a representative fragment of the extracellular E-selectin region with sLe(x) and a glycomimetic antagonist thereof reveal an extended E-selectin conformation, which is identified as a high-affinity binding state of E-selectin by molecular dynamics simulations.
26117840	3	38	theme	fragment	532:539	arg1	structures					501:510	Co-crystal structures	490:510	Co-crystal structures of a representative fragment of the extracellular E-selectin region with sLe(x)	490:590	Co-crystal structures of a representative fragment of the extracellular E-selectin region with sLe(x) and a glycomimetic antagonist thereof reveal an extended E-selectin conformation, which is identified as a high-affinity binding state of E-selectin by molecular dynamics simulations.
26117840	6	39	theme	molecular	1155:1163	arg1	view					1165:1168	The detailed molecular view	1142:1168	The detailed molecular view of the binding site	1142:1188	The detailed molecular view of the binding site paves the way for the design of a new generation of selectin antagonists.
26117840	0	40	theme	extended	37:44	arg1	conformation					60:71	an extended high-affinity conformation	34:71	an extended high-affinity conformation	34:71	E-selectin ligand complexes adopt an extended high-affinity conformation.
26117840	5	41	theme	concerted	977:985	arg1	changes					998:1004	concerted structural changes	977:1004	concerted structural changes connecting ligand binding to conformational stretching as the structural basis of E-selectin catch-bond-mediated leukocyte recruitment	977:1139	This permits tracing a series of concerted structural changes connecting ligand binding to conformational stretching as the structural basis of E-selectin catch-bond-mediated leukocyte recruitment.
26117840	6	42	theme	detailed	1146:1153	arg1	view					1165:1168	The detailed molecular view	1142:1168	The detailed molecular view of the binding site	1142:1188	The detailed molecular view of the binding site paves the way for the design of a new generation of selectin antagonists.
26117840	3	43	theme	glycomimetic	598:609	arg1	antagonist					611:620	a glycomimetic antagonist	596:620	a glycomimetic antagonist	596:620	Co-crystal structures of a representative fragment of the extracellular E-selectin region with sLe(x) and a glycomimetic antagonist thereof reveal an extended E-selectin conformation, which is identified as a high-affinity binding state of E-selectin by molecular dynamics simulations.
26117840	2	44	theme	complexes	420:428	arg1	lifetime					390:397	an increased lifetime	377:397	an increased lifetime of E-selectin/ligand complexes under tensile force in a so-called catch-bond binding mode	377:487	Efficient leukocyte recruitment under vascular flow conditions depends on an increased lifetime of E-selectin/ligand complexes under tensile force in a so-called catch-bond binding mode.
26117840	3	45	theme	E-selectin	649:658	arg1	state					721:725	a high-affinity binding state	697:725	a high-affinity binding state of E-selectin	697:739	Co-crystal structures of a representative fragment of the extracellular E-selectin region with sLe(x) and a glycomimetic antagonist thereof reveal an extended E-selectin conformation, which is identified as a high-affinity binding state of E-selectin by molecular dynamics simulations.
26117840	3	45	theme	E-selectin	649:658	arg1	conformation					660:671	an extended E-selectin conformation	637:671	an extended E-selectin conformation	637:671	Co-crystal structures of a representative fragment of the extracellular E-selectin region with sLe(x) and a glycomimetic antagonist thereof reveal an extended E-selectin conformation, which is identified as a high-affinity binding state of E-selectin by molecular dynamics simulations.
26117840	5	46	theme	leukocyte	1119:1127	arg1	recruitment					1129:1139	E-selectin catch-bond-mediated leukocyte recruitment	1088:1139	E-selectin catch-bond-mediated leukocyte recruitment	1088:1139	This permits tracing a series of concerted structural changes connecting ligand binding to conformational stretching as the structural basis of E-selectin catch-bond-mediated leukocyte recruitment.
26117840	2	47	theme	E-selectin/ligand	402:418	arg1	complexes					420:428	E-selectin/ligand complexes	402:428	E-selectin/ligand complexes under tensile force in a so-called catch-bond binding mode	402:487	Efficient leukocyte recruitment under vascular flow conditions depends on an increased lifetime of E-selectin/ligand complexes under tensile force in a so-called catch-bond binding mode.
26117840	2	48	theme	binding	476:482	arg1	mode					484:487	a so-called catch-bond binding mode	453:487	a so-called catch-bond binding mode	453:487	Efficient leukocyte recruitment under vascular flow conditions depends on an increased lifetime of E-selectin/ligand complexes under tensile force in a so-called catch-bond binding mode.
26117840	4	49	theme	conformational	881:894	arg1	transition					896:905	E-selectin conformational transition	870:905	E-selectin conformational transition	870:905	Small-angle X-ray scattering experiments demonstrate a direct link between ligand binding and E-selectin conformational transition under static conditions in solution.
26117840	1	50	theme	vascular	120:127	arg1	endothelium					129:139	the vascular endothelium	116:139	the vascular endothelium	116:139	E-selectin is a cell-adhesion molecule of the vascular endothelium that promotes essential leukocyte rolling in the early inflammatory response by binding to glycoproteins containing the tetrasaccharide sialyl Lewis(x) (sLe(x)).
26117840	2	51	theme	catch-bond	465:474	arg1	mode					484:487	a so-called catch-bond binding mode	453:487	a so-called catch-bond binding mode	453:487	Efficient leukocyte recruitment under vascular flow conditions depends on an increased lifetime of E-selectin/ligand complexes under tensile force in a so-called catch-bond binding mode.
26117840	7	52	theme	special	1275:1281	arg1	interest					1283:1290	special interest	1275:1290	special interest	1275:1290	This is of special interest, since their therapeutic potential was recently demonstrated with the pan-selectin antagonists GMI-1070 (Rivipansel).
26117840	1	53	contain	containing	246:255	arg2	x					290:290	x	290:290	x	290:290	E-selectin is a cell-adhesion molecule of the vascular endothelium that promotes essential leukocyte rolling in the early inflammatory response by binding to glycoproteins containing the tetrasaccharide sialyl Lewis(x) (sLe(x)).
26117840	1	53	contain	containing	246:255	arg2	Lewis					284:288	the tetrasaccharide sialyl Lewis	257:288	the tetrasaccharide sialyl Lewis(x) (sLe(x))	257:300	E-selectin is a cell-adhesion molecule of the vascular endothelium that promotes essential leukocyte rolling in the early inflammatory response by binding to glycoproteins containing the tetrasaccharide sialyl Lewis(x) (sLe(x)).
26117840	1	53	contain	containing	246:255	arg1	glycoproteins					232:244	glycoproteins	232:244	glycoproteins containing the tetrasaccharide sialyl Lewis(x) (sLe(x))	232:300	E-selectin is a cell-adhesion molecule of the vascular endothelium that promotes essential leukocyte rolling in the early inflammatory response by binding to glycoproteins containing the tetrasaccharide sialyl Lewis(x) (sLe(x)).
26117840	1	54	theme	endothelium	129:139	arg1	molecule					104:111	a cell-adhesion molecule	88:111	a cell-adhesion molecule of the vascular endothelium that promotes essential leukocyte rolling in the early inflammatory response by binding to glycoproteins containing the tetrasaccharide sialyl Lewis(x) (sLe(x))	88:300	E-selectin is a cell-adhesion molecule of the vascular endothelium that promotes essential leukocyte rolling in the early inflammatory response by binding to glycoproteins containing the tetrasaccharide sialyl Lewis(x) (sLe(x)).
26117840	1	54	theme	endothelium	129:139	arg1	E-selectin					74:83	E-selectin	74:83	E-selectin	74:83	E-selectin is a cell-adhesion molecule of the vascular endothelium that promotes essential leukocyte rolling in the early inflammatory response by binding to glycoproteins containing the tetrasaccharide sialyl Lewis(x) (sLe(x)).
26117840	5	55	theme	structural	1068:1077	arg1	binding					1024:1030	ligand binding	1017:1030	ligand binding to conformational stretching	1017:1059	This permits tracing a series of concerted structural changes connecting ligand binding to conformational stretching as the structural basis of E-selectin catch-bond-mediated leukocyte recruitment.
26117840	5	55	theme	structural	1068:1077	arg1	basis					1079:1083	the structural basis	1064:1083	the structural basis of E-selectin catch-bond-mediated leukocyte recruitment	1064:1139	This permits tracing a series of concerted structural changes connecting ligand binding to conformational stretching as the structural basis of E-selectin catch-bond-mediated leukocyte recruitment.
26117840	3	56	theme	Co-crystal	490:499	arg1	structures					501:510	Co-crystal structures	490:510	Co-crystal structures of a representative fragment of the extracellular E-selectin region with sLe(x)	490:590	Co-crystal structures of a representative fragment of the extracellular E-selectin region with sLe(x) and a glycomimetic antagonist thereof reveal an extended E-selectin conformation, which is identified as a high-affinity binding state of E-selectin by molecular dynamics simulations.
26117840	6	57	theme	generation	1228:1237	arg1	design					1212:1217	the design	1208:1217	the design of a new generation of selectin antagonists	1208:1261	The detailed molecular view of the binding site paves the way for the design of a new generation of selectin antagonists.
26117840	3	58	theme	E-selectin	562:571	arg1	region					573:578	the extracellular E-selectin region	544:578	the extracellular E-selectin region with sLe(x)	544:590	Co-crystal structures of a representative fragment of the extracellular E-selectin region with sLe(x) and a glycomimetic antagonist thereof reveal an extended E-selectin conformation, which is identified as a high-affinity binding state of E-selectin by molecular dynamics simulations.
26117840	1	59	dep	Lewis	284:288	arg1	x					298:298	x	298:298	x	298:298	E-selectin is a cell-adhesion molecule of the vascular endothelium that promotes essential leukocyte rolling in the early inflammatory response by binding to glycoproteins containing the tetrasaccharide sialyl Lewis(x) (sLe(x)).
26117840	1	59	dep	Lewis	284:288	arg1	sLe					294:296	sLe	294:296	sLe(x)	294:299	E-selectin is a cell-adhesion molecule of the vascular endothelium that promotes essential leukocyte rolling in the early inflammatory response by binding to glycoproteins containing the tetrasaccharide sialyl Lewis(x) (sLe(x)).
26117840	3	60	theme	extended	640:647	arg1	state					721:725	a high-affinity binding state	697:725	a high-affinity binding state of E-selectin	697:739	Co-crystal structures of a representative fragment of the extracellular E-selectin region with sLe(x) and a glycomimetic antagonist thereof reveal an extended E-selectin conformation, which is identified as a high-affinity binding state of E-selectin by molecular dynamics simulations.
26117840	3	60	theme	extended	640:647	arg1	conformation					660:671	an extended E-selectin conformation	637:671	an extended E-selectin conformation	637:671	Co-crystal structures of a representative fragment of the extracellular E-selectin region with sLe(x) and a glycomimetic antagonist thereof reveal an extended E-selectin conformation, which is identified as a high-affinity binding state of E-selectin by molecular dynamics simulations.
26117840	2	61	theme	leukocyte	313:321	arg1	recruitment					323:333	Efficient leukocyte recruitment	303:333	Efficient leukocyte recruitment under vascular flow conditions	303:364	Efficient leukocyte recruitment under vascular flow conditions depends on an increased lifetime of E-selectin/ligand complexes under tensile force in a so-called catch-bond binding mode.
26117840	5	62	theme	structural	987:996	arg1	changes					998:1004	concerted structural changes	977:1004	concerted structural changes connecting ligand binding to conformational stretching as the structural basis of E-selectin catch-bond-mediated leukocyte recruitment	977:1139	This permits tracing a series of concerted structural changes connecting ligand binding to conformational stretching as the structural basis of E-selectin catch-bond-mediated leukocyte recruitment.
26117840	7	63	theme	therapeutic	1305:1315	arg1	potential					1317:1325	their therapeutic potential	1299:1325	their therapeutic potential	1299:1325	This is of special interest, since their therapeutic potential was recently demonstrated with the pan-selectin antagonists GMI-1070 (Rivipansel).
26117840	4	64	theme	ligand	851:856	arg1	binding					858:864	ligand binding	851:864	ligand binding	851:864	Small-angle X-ray scattering experiments demonstrate a direct link between ligand binding and E-selectin conformational transition under static conditions in solution.
26117840	6	65	theme	antagonists	1251:1261	arg1	generation					1228:1237	a new generation	1222:1237	a new generation of selectin antagonists	1222:1261	The detailed molecular view of the binding site paves the way for the design of a new generation of selectin antagonists.
26117840	1	66	theme	essential	155:163	arg1	rolling					175:181	essential leukocyte rolling	155:181	essential leukocyte rolling	155:181	E-selectin is a cell-adhesion molecule of the vascular endothelium that promotes essential leukocyte rolling in the early inflammatory response by binding to glycoproteins containing the tetrasaccharide sialyl Lewis(x) (sLe(x)).
26117840	6	67	theme	binding	1177:1183	arg1	site					1185:1188	the binding site	1173:1188	the binding site	1173:1188	The detailed molecular view of the binding site paves the way for the design of a new generation of selectin antagonists.
26117840	1	68	theme	tetrasaccharide	261:275	arg1	x					290:290	x	290:290	x	290:290	E-selectin is a cell-adhesion molecule of the vascular endothelium that promotes essential leukocyte rolling in the early inflammatory response by binding to glycoproteins containing the tetrasaccharide sialyl Lewis(x) (sLe(x)).
26117840	1	68	theme	tetrasaccharide	261:275	arg1	Lewis					284:288	the tetrasaccharide sialyl Lewis	257:288	the tetrasaccharide sialyl Lewis(x) (sLe(x))	257:300	E-selectin is a cell-adhesion molecule of the vascular endothelium that promotes essential leukocyte rolling in the early inflammatory response by binding to glycoproteins containing the tetrasaccharide sialyl Lewis(x) (sLe(x)).
26117840	3	69	with	region	573:578	arg1	x					589:589	x	589:589	x	589:589	Co-crystal structures of a representative fragment of the extracellular E-selectin region with sLe(x) and a glycomimetic antagonist thereof reveal an extended E-selectin conformation, which is identified as a high-affinity binding state of E-selectin by molecular dynamics simulations.
26117840	3	69	with	region	573:578	arg1	sLe					585:587	sLe	585:587	sLe(x)	585:590	Co-crystal structures of a representative fragment of the extracellular E-selectin region with sLe(x) and a glycomimetic antagonist thereof reveal an extended E-selectin conformation, which is identified as a high-affinity binding state of E-selectin by molecular dynamics simulations.
26117840	6	70	theme	new	1224:1226	arg1	generation					1228:1237	a new generation	1222:1237	a new generation of selectin antagonists	1222:1261	The detailed molecular view of the binding site paves the way for the design of a new generation of selectin antagonists.
26117840	5	71	theme	E-selectin	1088:1097	arg1	recruitment					1129:1139	E-selectin catch-bond-mediated leukocyte recruitment	1088:1139	E-selectin catch-bond-mediated leukocyte recruitment	1088:1139	This permits tracing a series of concerted structural changes connecting ligand binding to conformational stretching as the structural basis of E-selectin catch-bond-mediated leukocyte recruitment.
26117840	1	72	theme	leukocyte	165:173	arg1	rolling					175:181	essential leukocyte rolling	155:181	essential leukocyte rolling	155:181	E-selectin is a cell-adhesion molecule of the vascular endothelium that promotes essential leukocyte rolling in the early inflammatory response by binding to glycoproteins containing the tetrasaccharide sialyl Lewis(x) (sLe(x)).
26117840	1	73	theme	sialyl	277:282	arg1	x					290:290	x	290:290	x	290:290	E-selectin is a cell-adhesion molecule of the vascular endothelium that promotes essential leukocyte rolling in the early inflammatory response by binding to glycoproteins containing the tetrasaccharide sialyl Lewis(x) (sLe(x)).
26117840	1	73	theme	sialyl	277:282	arg1	Lewis					284:288	the tetrasaccharide sialyl Lewis	257:288	the tetrasaccharide sialyl Lewis(x) (sLe(x))	257:300	E-selectin is a cell-adhesion molecule of the vascular endothelium that promotes essential leukocyte rolling in the early inflammatory response by binding to glycoproteins containing the tetrasaccharide sialyl Lewis(x) (sLe(x)).
19017259	2	0	theme	human	365:369	arg1	plasma					371:376	human plasma	365:376	human plasma	365:376	Most TFPI in human plasma is associated with lipoproteins; however, the most functionally active form is thought to be the free, full-length form (f-pTFPI).
19017259	9	1	theme	sialyl	1591:1596	arg1	chains					1617:1622	sialyl complex-type sugar chains	1591:1622	sialyl complex-type sugar chains	1591:1622	(Sialyl) Galbeta1-3GalNAc was linked to Thr(175), partially to Thr(14) and Ser(174); sialyl complex-type sugar chains to Asn(117) and Asn(167), whereas Asn(228) was not glycosylated.
19017259	6	2	from	plasma	1060:1065	arg1	homogeneity					1037:1047	homogeneity	1037:1047	homogeneity from blood plasma	1037:1065	RESULTS AND CONCLUSION f-pTFPI was purified to homogeneity from blood plasma using a combination of anion-exchange, heparin affinity, immunoaffinity, and reversed-phase chromatographies, resulting in a yield of 76%.
19017259	4	3	theme	CHO	839:841	arg1	cells					844:848	Chinese hamster ovary (CHO) cells	816:848	Chinese hamster ovary (CHO) cells	816:848	Sugar chain structures in rTFPI expressed in Chinese hamster ovary (CHO) cells have been reported previously, but those of plasma TFPI have not been.
19017259	2	4	from	TFPI	357:360	arg1	plasma					371:376	human plasma	365:376	human plasma	365:376	Most TFPI in human plasma is associated with lipoproteins; however, the most functionally active form is thought to be the free, full-length form (f-pTFPI).
19017259	3	5	theme	frequent	696:703	arg1	differences					705:715	the frequent differences	692:715	the frequent differences in sugar chain structures among recombinant proteins	692:768	Cell culture derived TFPI and recombinant TFPI (rTFPI) exhibit variations in their respective anticoagulant activity, which may be caused by post-translational modifications, such as the frequent differences in sugar chain structures among recombinant proteins.
19017259	1	6	theme	Tissue	195:200	arg1	TFPI					228:231	TFPI	228:231	TFPI	228:231	BACKGROUND Tissue factor pathway inhibitor (TFPI) is a physiological protease inhibitor that inhibits the initial reactions of the extrinsic blood coagulation pathway.
19017259	1	6	theme	Tissue	195:200	arg1	inhibitor					262:270	a physiological protease inhibitor	237:270	a physiological protease inhibitor that inhibits the initial reactions of the extrinsic blood coagulation pathway	237:349	BACKGROUND Tissue factor pathway inhibitor (TFPI) is a physiological protease inhibitor that inhibits the initial reactions of the extrinsic blood coagulation pathway.
19017259	1	6	theme	Tissue	195:200	arg1	inhibitor					217:225	BACKGROUND Tissue factor pathway inhibitor	184:225	BACKGROUND Tissue factor pathway inhibitor (TFPI)	184:232	BACKGROUND Tissue factor pathway inhibitor (TFPI) is a physiological protease inhibitor that inhibits the initial reactions of the extrinsic blood coagulation pathway.
19017259	9	7	dep	Thr	1569:1571	arg1	chains					1617:1622	sialyl complex-type sugar chains	1591:1622	sialyl complex-type sugar chains	1591:1622	(Sialyl) Galbeta1-3GalNAc was linked to Thr(175), partially to Thr(14) and Ser(174); sialyl complex-type sugar chains to Asn(117) and Asn(167), whereas Asn(228) was not glycosylated.
19017259	3	8	from	differences	705:715	arg1	structures					732:741	sugar chain structures	720:741	sugar chain structures among recombinant proteins	720:768	Cell culture derived TFPI and recombinant TFPI (rTFPI) exhibit variations in their respective anticoagulant activity, which may be caused by post-translational modifications, such as the frequent differences in sugar chain structures among recombinant proteins.
19017259	1	9	theme	pathway	209:215	arg1	TFPI					228:231	TFPI	228:231	TFPI	228:231	BACKGROUND Tissue factor pathway inhibitor (TFPI) is a physiological protease inhibitor that inhibits the initial reactions of the extrinsic blood coagulation pathway.
19017259	1	9	theme	pathway	209:215	arg1	inhibitor					262:270	a physiological protease inhibitor	237:270	a physiological protease inhibitor that inhibits the initial reactions of the extrinsic blood coagulation pathway	237:349	BACKGROUND Tissue factor pathway inhibitor (TFPI) is a physiological protease inhibitor that inhibits the initial reactions of the extrinsic blood coagulation pathway.
19017259	1	9	theme	pathway	209:215	arg1	inhibitor					217:225	BACKGROUND Tissue factor pathway inhibitor	184:225	BACKGROUND Tissue factor pathway inhibitor (TFPI)	184:232	BACKGROUND Tissue factor pathway inhibitor (TFPI) is a physiological protease inhibitor that inhibits the initial reactions of the extrinsic blood coagulation pathway.
19017259	11	10	theme	CHO	1974:1976	arg1	cells					1978:1982	CHO cells	1974:1982	CHO cells	1974:1982	The protease inhibitory activities of f-pTFPI towards activated factor (F) X and tissue factor-activated FVII complex were identical to those of full-length rTFPI expressed in CHO cells.
19017259	3	11	theme	chain	726:730	arg1	structures					732:741	sugar chain structures	720:741	sugar chain structures among recombinant proteins	720:768	Cell culture derived TFPI and recombinant TFPI (rTFPI) exhibit variations in their respective anticoagulant activity, which may be caused by post-translational modifications, such as the frequent differences in sugar chain structures among recombinant proteins.
19017259	8	12	theme	pyridylamino	1439:1450	arg1	chains					1458:1463	the pyridylamino sugar chains	1435:1463	the pyridylamino sugar chains	1435:1463	The sugar chain structures were analyzed by two-dimensional sugar mapping combined with exoglycosidase digestion of the pyridylamino sugar chains and the following results were obtained.
19017259	10	13	theme	Neuraminidase-resistant	1689:1711	arg1	chains					1726:1731	Neuraminidase-resistant acidic sugar chains	1689:1731	Neuraminidase-resistant acidic sugar chains including sulfated sugar chains	1689:1763	Neuraminidase-resistant acidic sugar chains including sulfated sugar chains were not observed significantly.
19017259	8	14	theme	chains	1458:1463	arg1	digestion					1422:1430	exoglycosidase digestion	1407:1430	exoglycosidase digestion of the pyridylamino sugar chains	1407:1463	The sugar chain structures were analyzed by two-dimensional sugar mapping combined with exoglycosidase digestion of the pyridylamino sugar chains and the following results were obtained.
19017259	6	15	theme	%	1203:1203	arg1	yield					1192:1196	a yield	1190:1196	a yield of 76%	1190:1203	RESULTS AND CONCLUSION f-pTFPI was purified to homogeneity from blood plasma using a combination of anion-exchange, heparin affinity, immunoaffinity, and reversed-phase chromatographies, resulting in a yield of 76%.
19017259	11	16	theme	F	1870:1870	arg1	X					1873:1873	activated factor (F) X and tissue factor-activated FVII complex	1852:1914	X	1873:1873	The protease inhibitory activities of f-pTFPI towards activated factor (F) X and tissue factor-activated FVII complex were identical to those of full-length rTFPI expressed in CHO cells.
19017259	10	17	theme	sulfated	1743:1750	arg1	chains					1758:1763	sulfated sugar chains	1743:1763	sulfated sugar chains	1743:1763	Neuraminidase-resistant acidic sugar chains including sulfated sugar chains were not observed significantly.
19017259	11	18	theme	FVII	1903:1906	arg1	complex					1908:1914	activated factor (F) X and tissue factor-activated FVII complex	1852:1914	complex	1908:1914	The protease inhibitory activities of f-pTFPI towards activated factor (F) X and tissue factor-activated FVII complex were identical to those of full-length rTFPI expressed in CHO cells.
19017259	9	19	theme	Sialyl	1507:1512	arg1	Galbeta1-3GalNAc					1515:1530	(Sialyl) Galbeta1-3GalNAc	1506:1530	(Sialyl) Galbeta1-3GalNAc	1506:1530	(Sialyl) Galbeta1-3GalNAc was linked to Thr(175), partially to Thr(14) and Ser(174); sialyl complex-type sugar chains to Asn(117) and Asn(167), whereas Asn(228) was not glycosylated.
19017259	10	20	theme	sugar	1720:1724	arg1	chains					1726:1731	Neuraminidase-resistant acidic sugar chains	1689:1731	Neuraminidase-resistant acidic sugar chains including sulfated sugar chains	1689:1763	Neuraminidase-resistant acidic sugar chains including sulfated sugar chains were not observed significantly.
19017259	8	21	theme	sugar	1323:1327	arg1	structures					1335:1344	The sugar chain structures	1319:1344	The sugar chain structures	1319:1344	The sugar chain structures were analyzed by two-dimensional sugar mapping combined with exoglycosidase digestion of the pyridylamino sugar chains and the following results were obtained.
19017259	0	22	theme	free	115:118	arg1	form					133:136	free, full-length form	115:136	free, full-length form	115:136	Biochemical characterization of plasma-derived tissue factor pathway inhibitor: post-translational modification of free, full-length form with particular reference to the sugar chain.
19017259	4	23	theme	chain	777:781	arg1	structures					783:792	Sugar chain structures	771:792	Sugar chain structures in rTFPI expressed in Chinese hamster ovary (CHO) cells	771:848	Sugar chain structures in rTFPI expressed in Chinese hamster ovary (CHO) cells have been reported previously, but those of plasma TFPI have not been.
19017259	0	24	dep	free	115:118	arg1	full-length					121:131	full-length	121:131	full-length	121:131	Biochemical characterization of plasma-derived tissue factor pathway inhibitor: post-translational modification of free, full-length form with particular reference to the sugar chain.
19017259	6	25	theme	blood	1054:1058	arg1	plasma					1060:1065	blood plasma	1054:1065	blood plasma	1054:1065	RESULTS AND CONCLUSION f-pTFPI was purified to homogeneity from blood plasma using a combination of anion-exchange, heparin affinity, immunoaffinity, and reversed-phase chromatographies, resulting in a yield of 76%.
19017259	11	26	theme	protease	1802:1809	arg1	activities					1822:1831	The protease inhibitory activities	1798:1831	The protease inhibitory activities of f-pTFPI towards activated factor (F) X and tissue factor-activated FVII complex	1798:1914	The protease inhibitory activities of f-pTFPI towards activated factor (F) X and tissue factor-activated FVII complex were identical to those of full-length rTFPI expressed in CHO cells.
19017259	11	26	theme	protease	1802:1809	arg1	identical					1921:1929	identical	1921:1929	identical	1921:1929	The protease inhibitory activities of f-pTFPI towards activated factor (F) X and tissue factor-activated FVII complex were identical to those of full-length rTFPI expressed in CHO cells.
19017259	0	27	theme	Biochemical	0:10	arg1	characterization					12:27	Biochemical characterization	0:27	Biochemical characterization of plasma-derived tissue factor pathway inhibitor: post-translational modification of free, full-length form with particular reference to the sugar chain.	0:182	Biochemical characterization of plasma-derived tissue factor pathway inhibitor: post-translational modification of free, full-length form with particular reference to the sugar chain.
19017259	1	28	theme	initial	290:296	arg1	reactions					298:306	the initial reactions	286:306	the initial reactions of the extrinsic blood coagulation pathway	286:349	BACKGROUND Tissue factor pathway inhibitor (TFPI) is a physiological protease inhibitor that inhibits the initial reactions of the extrinsic blood coagulation pathway.
19017259	9	29	theme	sugar	1611:1615	arg1	chains					1617:1622	sialyl complex-type sugar chains	1591:1622	sialyl complex-type sugar chains	1591:1622	(Sialyl) Galbeta1-3GalNAc was linked to Thr(175), partially to Thr(14) and Ser(174); sialyl complex-type sugar chains to Asn(117) and Asn(167), whereas Asn(228) was not glycosylated.
19017259	7	30	theme	peptide	1302:1308	arg1	mapping					1310:1316	peptide mapping	1302:1316	peptide mapping	1302:1316	f-pTFPI showed a partially phosphorylated glycoprotein comprising a total of 276 amino acids by peptide mapping.
19017259	8	31	theme	two-dimensional	1363:1377	arg1	mapping					1385:1391	two-dimensional sugar mapping	1363:1391	two-dimensional sugar mapping combined with exoglycosidase digestion of the pyridylamino sugar chains	1363:1463	The sugar chain structures were analyzed by two-dimensional sugar mapping combined with exoglycosidase digestion of the pyridylamino sugar chains and the following results were obtained.
19017259	11	32	theme	activated	1852:1860	arg1	X					1873:1873	activated factor (F) X and tissue factor-activated FVII complex	1852:1914	X	1873:1873	The protease inhibitory activities of f-pTFPI towards activated factor (F) X and tissue factor-activated FVII complex were identical to those of full-length rTFPI expressed in CHO cells.
19017259	7	33	theme	acids	1293:1297	arg1	total					1274:1278	a total	1272:1278	a total of 276 amino acids by peptide mapping	1272:1316	f-pTFPI showed a partially phosphorylated glycoprotein comprising a total of 276 amino acids by peptide mapping.
19017259	2	34	theme	free	475:478	arg1	form					493:496	the free, full-length form	471:496	the free, full-length form (f-pTFPI)	471:506	Most TFPI in human plasma is associated with lipoproteins; however, the most functionally active form is thought to be the free, full-length form (f-pTFPI).
19017259	2	34	theme	free	475:478	arg1	form					449:452	the most functionally active form	420:452	the most functionally active form	420:452	Most TFPI in human plasma is associated with lipoproteins; however, the most functionally active form is thought to be the free, full-length form (f-pTFPI).
19017259	2	34	theme	free	475:478	arg1	f-pTFPI					499:505	f-pTFPI	499:505	f-pTFPI	499:505	Most TFPI in human plasma is associated with lipoproteins; however, the most functionally active form is thought to be the free, full-length form (f-pTFPI).
19017259	4	35	theme	Chinese	816:822	arg1	cells					844:848	Chinese hamster ovary (CHO) cells	816:848	Chinese hamster ovary (CHO) cells	816:848	Sugar chain structures in rTFPI expressed in Chinese hamster ovary (CHO) cells have been reported previously, but those of plasma TFPI have not been.
19017259	11	36	theme	f-pTFPI	1836:1842	arg1	activities					1822:1831	The protease inhibitory activities	1798:1831	The protease inhibitory activities of f-pTFPI towards activated factor (F) X and tissue factor-activated FVII complex	1798:1914	The protease inhibitory activities of f-pTFPI towards activated factor (F) X and tissue factor-activated FVII complex were identical to those of full-length rTFPI expressed in CHO cells.
19017259	11	36	theme	f-pTFPI	1836:1842	arg1	identical					1921:1929	identical	1921:1929	identical	1921:1929	The protease inhibitory activities of f-pTFPI towards activated factor (F) X and tissue factor-activated FVII complex were identical to those of full-length rTFPI expressed in CHO cells.
19017259	0	37	theme	tissue	47:52	arg1	inhibitor					69:77	plasma-derived tissue factor pathway inhibitor	32:77	plasma-derived tissue factor pathway inhibitor	32:77	Biochemical characterization of plasma-derived tissue factor pathway inhibitor: post-translational modification of free, full-length form with particular reference to the sugar chain.
19017259	1	38	theme	extrinsic	315:323	arg1	pathway					343:349	the extrinsic blood coagulation pathway	311:349	the extrinsic blood coagulation pathway	311:349	BACKGROUND Tissue factor pathway inhibitor (TFPI) is a physiological protease inhibitor that inhibits the initial reactions of the extrinsic blood coagulation pathway.
19017259	10	39	theme	sugar	1752:1756	arg1	chains					1758:1763	sulfated sugar chains	1743:1763	sulfated sugar chains	1743:1763	Neuraminidase-resistant acidic sugar chains including sulfated sugar chains were not observed significantly.
19017259	4	40	theme	ovary	832:836	arg1	cells					844:848	Chinese hamster ovary (CHO) cells	816:848	Chinese hamster ovary (CHO) cells	816:848	Sugar chain structures in rTFPI expressed in Chinese hamster ovary (CHO) cells have been reported previously, but those of plasma TFPI have not been.
19017259	0	41	theme	pathway	61:67	arg1	inhibitor					69:77	plasma-derived tissue factor pathway inhibitor	32:77	plasma-derived tissue factor pathway inhibitor	32:77	Biochemical characterization of plasma-derived tissue factor pathway inhibitor: post-translational modification of free, full-length form with particular reference to the sugar chain.
19017259	1	42	theme	coagulation	331:341	arg1	pathway					343:349	the extrinsic blood coagulation pathway	311:349	the extrinsic blood coagulation pathway	311:349	BACKGROUND Tissue factor pathway inhibitor (TFPI) is a physiological protease inhibitor that inhibits the initial reactions of the extrinsic blood coagulation pathway.
19017259	6	43	theme	heparin	1106:1112	arg1	affinity					1114:1121	heparin affinity	1106:1121	heparin affinity	1106:1121	RESULTS AND CONCLUSION f-pTFPI was purified to homogeneity from blood plasma using a combination of anion-exchange, heparin affinity, immunoaffinity, and reversed-phase chromatographies, resulting in a yield of 76%.
19017259	3	44	theme	respective	592:601	arg1	activity					617:624	their respective anticoagulant activity	586:624	their respective anticoagulant activity	586:624	Cell culture derived TFPI and recombinant TFPI (rTFPI) exhibit variations in their respective anticoagulant activity, which may be caused by post-translational modifications, such as the frequent differences in sugar chain structures among recombinant proteins.
19017259	9	45	attach	linked	1536:1541	arg1	14					1573:1574	14	1573:1574	14	1573:1574	(Sialyl) Galbeta1-3GalNAc was linked to Thr(175), partially to Thr(14) and Ser(174); sialyl complex-type sugar chains to Asn(117) and Asn(167), whereas Asn(228) was not glycosylated.
19017259	9	45	attach	linked	1536:1541	arg2	Galbeta1-3GalNAc					1515:1530	(Sialyl) Galbeta1-3GalNAc	1506:1530	(Sialyl) Galbeta1-3GalNAc	1506:1530	(Sialyl) Galbeta1-3GalNAc was linked to Thr(175), partially to Thr(14) and Ser(174); sialyl complex-type sugar chains to Asn(117) and Asn(167), whereas Asn(228) was not glycosylated.
19017259	9	45	attach	linked	1536:1541	arg1	Ser					1581:1583	Ser(174);	1581:1589	Ser(174);	1581:1589	(Sialyl) Galbeta1-3GalNAc was linked to Thr(175), partially to Thr(14) and Ser(174); sialyl complex-type sugar chains to Asn(117) and Asn(167), whereas Asn(228) was not glycosylated.
19017259	9	45	attach	linked	1536:1541	arg1	Thr					1546:1548	Thr	1546:1548	Thr(175)	1546:1553	(Sialyl) Galbeta1-3GalNAc was linked to Thr(175), partially to Thr(14) and Ser(174); sialyl complex-type sugar chains to Asn(117) and Asn(167), whereas Asn(228) was not glycosylated.
19017259	9	45	attach	linked	1536:1541	arg1	Thr					1569:1571	Thr	1569:1571	Thr(14)	1569:1575	(Sialyl) Galbeta1-3GalNAc was linked to Thr(175), partially to Thr(14) and Ser(174); sialyl complex-type sugar chains to Asn(117) and Asn(167), whereas Asn(228) was not glycosylated.
19017259	9	45	attach	linked	1536:1541	arg1	175					1550:1552	175	1550:1552	175	1550:1552	(Sialyl) Galbeta1-3GalNAc was linked to Thr(175), partially to Thr(14) and Ser(174); sialyl complex-type sugar chains to Asn(117) and Asn(167), whereas Asn(228) was not glycosylated.
19017259	9	45	attach	linked	1536:1541	arg1	Asn					1640:1642	Asn(167)	1640:1647	Asn(167)	1640:1647	(Sialyl) Galbeta1-3GalNAc was linked to Thr(175), partially to Thr(14) and Ser(174); sialyl complex-type sugar chains to Asn(117) and Asn(167), whereas Asn(228) was not glycosylated.
19017259	9	45	attach	linked	1536:1541	arg1	Asn					1627:1629	Asn(117)	1627:1634	Asn(117)	1627:1634	(Sialyl) Galbeta1-3GalNAc was linked to Thr(175), partially to Thr(14) and Ser(174); sialyl complex-type sugar chains to Asn(117) and Asn(167), whereas Asn(228) was not glycosylated.
19017259	2	46	theme	Most	352:355	arg1	TFPI					357:360	Most TFPI	352:360	Most TFPI in human plasma	352:376	Most TFPI in human plasma is associated with lipoproteins; however, the most functionally active form is thought to be the free, full-length form (f-pTFPI).
19017259	7	47	gly	glycoprotein	1248:1259	arg1	glycoprotein					1248:1259	a partially phosphorylated glycoprotein	1221:1259	a partially phosphorylated glycoprotein comprising a total of 276 amino acids by peptide mapping	1221:1316	f-pTFPI showed a partially phosphorylated glycoprotein comprising a total of 276 amino acids by peptide mapping.
19017259	5	48	theme	sugar	966:970	arg1	structures					978:987	the sugar chain structures	962:987	the sugar chain structures	962:987	OBJECTIVES To purify f-pTFPI and analyze the sugar chain structures.
19017259	6	49	theme	anion-exchange	1090:1103	arg1	combination					1075:1085	a combination	1073:1085	a combination of anion-exchange	1073:1103	RESULTS AND CONCLUSION f-pTFPI was purified to homogeneity from blood plasma using a combination of anion-exchange, heparin affinity, immunoaffinity, and reversed-phase chromatographies, resulting in a yield of 76%.
19017259	6	49	theme	anion-exchange	1090:1103	arg1	chromatographies					1159:1174	reversed-phase chromatographies	1144:1174	reversed-phase chromatographies	1144:1174	RESULTS AND CONCLUSION f-pTFPI was purified to homogeneity from blood plasma using a combination of anion-exchange, heparin affinity, immunoaffinity, and reversed-phase chromatographies, resulting in a yield of 76%.
19017259	6	49	theme	anion-exchange	1090:1103	arg1	immunoaffinity					1124:1137	immunoaffinity	1124:1137	immunoaffinity	1124:1137	RESULTS AND CONCLUSION f-pTFPI was purified to homogeneity from blood plasma using a combination of anion-exchange, heparin affinity, immunoaffinity, and reversed-phase chromatographies, resulting in a yield of 76%.
19017259	6	49	theme	anion-exchange	1090:1103	arg1	affinity					1114:1121	heparin affinity	1106:1121	heparin affinity	1106:1121	RESULTS AND CONCLUSION f-pTFPI was purified to homogeneity from blood plasma using a combination of anion-exchange, heparin affinity, immunoaffinity, and reversed-phase chromatographies, resulting in a yield of 76%.
19017259	3	50	dep	exhibit	564:570	arg1	caused					640:645	caused	640:645	may be caused by post-translational modifications, such as the frequent differences in sugar chain structures among recombinant proteins	633:768	Cell culture derived TFPI and recombinant TFPI (rTFPI) exhibit variations in their respective anticoagulant activity, which may be caused by post-translational modifications, such as the frequent differences in sugar chain structures among recombinant proteins.
19017259	1	51	theme	physiological	239:251	arg1	inhibitor					217:225	BACKGROUND Tissue factor pathway inhibitor	184:225	BACKGROUND Tissue factor pathway inhibitor (TFPI)	184:232	BACKGROUND Tissue factor pathway inhibitor (TFPI) is a physiological protease inhibitor that inhibits the initial reactions of the extrinsic blood coagulation pathway.
19017259	1	51	theme	physiological	239:251	arg1	inhibitor					262:270	a physiological protease inhibitor	237:270	a physiological protease inhibitor that inhibits the initial reactions of the extrinsic blood coagulation pathway	237:349	BACKGROUND Tissue factor pathway inhibitor (TFPI) is a physiological protease inhibitor that inhibits the initial reactions of the extrinsic blood coagulation pathway.
19017259	7	52	theme	phosphorylated	1233:1246	arg1	glycoprotein					1248:1259	a partially phosphorylated glycoprotein	1221:1259	a partially phosphorylated glycoprotein comprising a total of 276 amino acids by peptide mapping	1221:1316	f-pTFPI showed a partially phosphorylated glycoprotein comprising a total of 276 amino acids by peptide mapping.
19017259	0	53	link	plasma-derived	32:45	arg1	inhibitor					69:77	plasma-derived tissue factor pathway inhibitor	32:77	plasma-derived tissue factor pathway inhibitor	32:77	Biochemical characterization of plasma-derived tissue factor pathway inhibitor: post-translational modification of free, full-length form with particular reference to the sugar chain.
19017259	0	54	with	modification	99:110	arg1	reference					154:162	particular reference	143:162	particular reference to the sugar chain	143:181	Biochemical characterization of plasma-derived tissue factor pathway inhibitor: post-translational modification of free, full-length form with particular reference to the sugar chain.
19017259	9	55	theme	complex-type	1598:1609	arg1	chains					1617:1622	sialyl complex-type sugar chains	1591:1622	sialyl complex-type sugar chains	1591:1622	(Sialyl) Galbeta1-3GalNAc was linked to Thr(175), partially to Thr(14) and Ser(174); sialyl complex-type sugar chains to Asn(117) and Asn(167), whereas Asn(228) was not glycosylated.
19017259	3	56	theme	sugar	720:724	arg1	structures					732:741	sugar chain structures	720:741	sugar chain structures among recombinant proteins	720:768	Cell culture derived TFPI and recombinant TFPI (rTFPI) exhibit variations in their respective anticoagulant activity, which may be caused by post-translational modifications, such as the frequent differences in sugar chain structures among recombinant proteins.
19017259	1	57	theme	BACKGROUND	184:193	arg1	TFPI					228:231	TFPI	228:231	TFPI	228:231	BACKGROUND Tissue factor pathway inhibitor (TFPI) is a physiological protease inhibitor that inhibits the initial reactions of the extrinsic blood coagulation pathway.
19017259	1	57	theme	BACKGROUND	184:193	arg1	inhibitor					262:270	a physiological protease inhibitor	237:270	a physiological protease inhibitor that inhibits the initial reactions of the extrinsic blood coagulation pathway	237:349	BACKGROUND Tissue factor pathway inhibitor (TFPI) is a physiological protease inhibitor that inhibits the initial reactions of the extrinsic blood coagulation pathway.
19017259	1	57	theme	BACKGROUND	184:193	arg1	inhibitor					217:225	BACKGROUND Tissue factor pathway inhibitor	184:225	BACKGROUND Tissue factor pathway inhibitor (TFPI)	184:232	BACKGROUND Tissue factor pathway inhibitor (TFPI) is a physiological protease inhibitor that inhibits the initial reactions of the extrinsic blood coagulation pathway.
19017259	11	58	theme	tissue	1879:1884	arg1	complex					1908:1914	activated factor (F) X and tissue factor-activated FVII complex	1852:1914	complex	1908:1914	The protease inhibitory activities of f-pTFPI towards activated factor (F) X and tissue factor-activated FVII complex were identical to those of full-length rTFPI expressed in CHO cells.
19017259	6	59	theme	reversed-phase	1144:1157	arg1	chromatographies					1159:1174	reversed-phase chromatographies	1144:1174	reversed-phase chromatographies	1144:1174	RESULTS AND CONCLUSION f-pTFPI was purified to homogeneity from blood plasma using a combination of anion-exchange, heparin affinity, immunoaffinity, and reversed-phase chromatographies, resulting in a yield of 76%.
19017259	11	60	theme	full-length	1943:1953	arg1	rTFPI					1955:1959	full-length rTFPI	1943:1959	full-length rTFPI expressed in CHO cells	1943:1982	The protease inhibitory activities of f-pTFPI towards activated factor (F) X and tissue factor-activated FVII complex were identical to those of full-length rTFPI expressed in CHO cells.
19017259	1	61	theme	factor	202:207	arg1	TFPI					228:231	TFPI	228:231	TFPI	228:231	BACKGROUND Tissue factor pathway inhibitor (TFPI) is a physiological protease inhibitor that inhibits the initial reactions of the extrinsic blood coagulation pathway.
19017259	1	61	theme	factor	202:207	arg1	inhibitor					262:270	a physiological protease inhibitor	237:270	a physiological protease inhibitor that inhibits the initial reactions of the extrinsic blood coagulation pathway	237:349	BACKGROUND Tissue factor pathway inhibitor (TFPI) is a physiological protease inhibitor that inhibits the initial reactions of the extrinsic blood coagulation pathway.
19017259	1	61	theme	factor	202:207	arg1	inhibitor					217:225	BACKGROUND Tissue factor pathway inhibitor	184:225	BACKGROUND Tissue factor pathway inhibitor (TFPI)	184:232	BACKGROUND Tissue factor pathway inhibitor (TFPI) is a physiological protease inhibitor that inhibits the initial reactions of the extrinsic blood coagulation pathway.
19017259	3	62	theme	recombinant	749:759	arg1	proteins					761:768	recombinant proteins	749:768	recombinant proteins	749:768	Cell culture derived TFPI and recombinant TFPI (rTFPI) exhibit variations in their respective anticoagulant activity, which may be caused by post-translational modifications, such as the frequent differences in sugar chain structures among recombinant proteins.
19017259	0	63	theme	particular	143:152	arg1	reference					154:162	particular reference	143:162	particular reference to the sugar chain	143:181	Biochemical characterization of plasma-derived tissue factor pathway inhibitor: post-translational modification of free, full-length form with particular reference to the sugar chain.
19017259	3	64	theme	recombinant	539:549	arg1	TFPI					551:554	recombinant TFPI	539:554	recombinant TFPI (rTFPI)	539:562	Cell culture derived TFPI and recombinant TFPI (rTFPI) exhibit variations in their respective anticoagulant activity, which may be caused by post-translational modifications, such as the frequent differences in sugar chain structures among recombinant proteins.
19017259	3	64	theme	recombinant	539:549	arg1	rTFPI					557:561	rTFPI	557:561	rTFPI	557:561	Cell culture derived TFPI and recombinant TFPI (rTFPI) exhibit variations in their respective anticoagulant activity, which may be caused by post-translational modifications, such as the frequent differences in sugar chain structures among recombinant proteins.
19017259	4	65	theme	plasma	894:899	arg1	TFPI					901:904	plasma TFPI	894:904	plasma TFPI	894:904	Sugar chain structures in rTFPI expressed in Chinese hamster ovary (CHO) cells have been reported previously, but those of plasma TFPI have not been.
19017259	8	66	theme	sugar	1452:1456	arg1	chains					1458:1463	the pyridylamino sugar chains	1435:1463	the pyridylamino sugar chains	1435:1463	The sugar chain structures were analyzed by two-dimensional sugar mapping combined with exoglycosidase digestion of the pyridylamino sugar chains and the following results were obtained.
19017259	10	67	theme	acidic	1713:1718	arg1	chains					1726:1731	Neuraminidase-resistant acidic sugar chains	1689:1731	Neuraminidase-resistant acidic sugar chains including sulfated sugar chains	1689:1763	Neuraminidase-resistant acidic sugar chains including sulfated sugar chains were not observed significantly.
19017259	11	68	theme	factor-activated	1886:1901	arg1	complex					1908:1914	activated factor (F) X and tissue factor-activated FVII complex	1852:1914	complex	1908:1914	The protease inhibitory activities of f-pTFPI towards activated factor (F) X and tissue factor-activated FVII complex were identical to those of full-length rTFPI expressed in CHO cells.
19017259	0	69	theme	sugar	171:175	arg1	chain					177:181	the sugar chain	167:181	the sugar chain	167:181	Biochemical characterization of plasma-derived tissue factor pathway inhibitor: post-translational modification of free, full-length form with particular reference to the sugar chain.
19017259	8	70	theme	following	1473:1481	arg1	results					1483:1489	the following results	1469:1489	the following results	1469:1489	The sugar chain structures were analyzed by two-dimensional sugar mapping combined with exoglycosidase digestion of the pyridylamino sugar chains and the following results were obtained.
19017259	3	71	theme	anticoagulant	603:615	arg1	activity					617:624	their respective anticoagulant activity	586:624	their respective anticoagulant activity	586:624	Cell culture derived TFPI and recombinant TFPI (rTFPI) exhibit variations in their respective anticoagulant activity, which may be caused by post-translational modifications, such as the frequent differences in sugar chain structures among recombinant proteins.
19017259	6	72	theme	CONCLUSION	1002:1011	arg1	f-pTFPI					1013:1019	RESULTS AND CONCLUSION f-pTFPI	990:1019	RESULTS AND CONCLUSION f-pTFPI	990:1019	RESULTS AND CONCLUSION f-pTFPI was purified to homogeneity from blood plasma using a combination of anion-exchange, heparin affinity, immunoaffinity, and reversed-phase chromatographies, resulting in a yield of 76%.
19017259	0	73	theme	post-translational	80:97	arg1	modification					99:110	post-translational modification	80:110	Biochemical characterization of plasma-derived tissue factor pathway inhibitor: post-translational modification of free, full-length form with particular reference to the sugar chain.	0:182	Biochemical characterization of plasma-derived tissue factor pathway inhibitor: post-translational modification of free, full-length form with particular reference to the sugar chain.
19017259	6	74	theme	RESULTS	990:996	arg1	f-pTFPI					1013:1019	RESULTS AND CONCLUSION f-pTFPI	990:1019	RESULTS AND CONCLUSION f-pTFPI	990:1019	RESULTS AND CONCLUSION f-pTFPI was purified to homogeneity from blood plasma using a combination of anion-exchange, heparin affinity, immunoaffinity, and reversed-phase chromatographies, resulting in a yield of 76%.
19017259	4	75	from	structures	783:792	arg1	rTFPI					797:801	rTFPI	797:801	rTFPI expressed in Chinese hamster ovary (CHO) cells	797:848	Sugar chain structures in rTFPI expressed in Chinese hamster ovary (CHO) cells have been reported previously, but those of plasma TFPI have not been.
19017259	2	76	dep	free	475:478	arg1	full-length					481:491	full-length	481:491	full-length	481:491	Most TFPI in human plasma is associated with lipoproteins; however, the most functionally active form is thought to be the free, full-length form (f-pTFPI).
19017259	9	77	gly	glycosylated	1675:1686	arg1	Asn					1658:1660	Asn	1658:1660	Asn(228)	1658:1665	(Sialyl) Galbeta1-3GalNAc was linked to Thr(175), partially to Thr(14) and Ser(174); sialyl complex-type sugar chains to Asn(117) and Asn(167), whereas Asn(228) was not glycosylated.
19017259	9	77	gly	glycosylated	1675:1686	arg1	228					1662:1664	228	1662:1664	228	1662:1664	(Sialyl) Galbeta1-3GalNAc was linked to Thr(175), partially to Thr(14) and Ser(174); sialyl complex-type sugar chains to Asn(117) and Asn(167), whereas Asn(228) was not glycosylated.
19017259	0	78	theme	form	133:136	arg1	modification					99:110	post-translational modification	80:110	Biochemical characterization of plasma-derived tissue factor pathway inhibitor: post-translational modification of free, full-length form with particular reference to the sugar chain.	0:182	Biochemical characterization of plasma-derived tissue factor pathway inhibitor: post-translational modification of free, full-length form with particular reference to the sugar chain.
19017259	8	79	theme	chain	1329:1333	arg1	structures					1335:1344	The sugar chain structures	1319:1344	The sugar chain structures	1319:1344	The sugar chain structures were analyzed by two-dimensional sugar mapping combined with exoglycosidase digestion of the pyridylamino sugar chains and the following results were obtained.
19017259	9	80	dep	linked	1536:1541	arg1	whereas					1650:1656	whereas	1650:1656	whereas	1650:1656	(Sialyl) Galbeta1-3GalNAc was linked to Thr(175), partially to Thr(14) and Ser(174); sialyl complex-type sugar chains to Asn(117) and Asn(167), whereas Asn(228) was not glycosylated.
19017259	11	81	theme	inhibitory	1811:1820	arg1	activities					1822:1831	The protease inhibitory activities	1798:1831	The protease inhibitory activities of f-pTFPI towards activated factor (F) X and tissue factor-activated FVII complex	1798:1914	The protease inhibitory activities of f-pTFPI towards activated factor (F) X and tissue factor-activated FVII complex were identical to those of full-length rTFPI expressed in CHO cells.
19017259	11	81	theme	inhibitory	1811:1820	arg1	identical					1921:1929	identical	1921:1929	identical	1921:1929	The protease inhibitory activities of f-pTFPI towards activated factor (F) X and tissue factor-activated FVII complex were identical to those of full-length rTFPI expressed in CHO cells.
19017259	0	82	theme	plasma-derived	32:45	arg1	inhibitor					69:77	plasma-derived tissue factor pathway inhibitor	32:77	plasma-derived tissue factor pathway inhibitor	32:77	Biochemical characterization of plasma-derived tissue factor pathway inhibitor: post-translational modification of free, full-length form with particular reference to the sugar chain.
19017259	0	83	dep	characterization	12:27	arg1	modification					99:110	post-translational modification	80:110	Biochemical characterization of plasma-derived tissue factor pathway inhibitor: post-translational modification of free, full-length form with particular reference to the sugar chain.	0:182	Biochemical characterization of plasma-derived tissue factor pathway inhibitor: post-translational modification of free, full-length form with particular reference to the sugar chain.
19017259	7	84	theme	amino	1287:1291	arg1	acids					1293:1297	276 amino acids	1283:1297	276 amino acids	1283:1297	f-pTFPI showed a partially phosphorylated glycoprotein comprising a total of 276 amino acids by peptide mapping.
19017259	2	85	theme	active	442:447	arg1	form					493:496	the free, full-length form	471:496	the free, full-length form (f-pTFPI)	471:506	Most TFPI in human plasma is associated with lipoproteins; however, the most functionally active form is thought to be the free, full-length form (f-pTFPI).
19017259	2	85	theme	active	442:447	arg1	form					449:452	the most functionally active form	420:452	the most functionally active form	420:452	Most TFPI in human plasma is associated with lipoproteins; however, the most functionally active form is thought to be the free, full-length form (f-pTFPI).
19017259	3	86	from	variations	572:581	arg1	activity					617:624	their respective anticoagulant activity	586:624	their respective anticoagulant activity	586:624	Cell culture derived TFPI and recombinant TFPI (rTFPI) exhibit variations in their respective anticoagulant activity, which may be caused by post-translational modifications, such as the frequent differences in sugar chain structures among recombinant proteins.
19017259	11	87	theme	factor	1862:1867	arg1	X					1873:1873	activated factor (F) X and tissue factor-activated FVII complex	1852:1914	X	1873:1873	The protease inhibitory activities of f-pTFPI towards activated factor (F) X and tissue factor-activated FVII complex were identical to those of full-length rTFPI expressed in CHO cells.
19017259	0	88	theme	factor	54:59	arg1	inhibitor					69:77	plasma-derived tissue factor pathway inhibitor	32:77	plasma-derived tissue factor pathway inhibitor	32:77	Biochemical characterization of plasma-derived tissue factor pathway inhibitor: post-translational modification of free, full-length form with particular reference to the sugar chain.
19017259	8	89	theme	sugar	1379:1383	arg1	mapping					1385:1391	two-dimensional sugar mapping	1363:1391	two-dimensional sugar mapping combined with exoglycosidase digestion of the pyridylamino sugar chains	1363:1463	The sugar chain structures were analyzed by two-dimensional sugar mapping combined with exoglycosidase digestion of the pyridylamino sugar chains and the following results were obtained.
19017259	0	90	theme	inhibitor	69:77	arg1	characterization					12:27	Biochemical characterization	0:27	Biochemical characterization of plasma-derived tissue factor pathway inhibitor: post-translational modification of free, full-length form with particular reference to the sugar chain.	0:182	Biochemical characterization of plasma-derived tissue factor pathway inhibitor: post-translational modification of free, full-length form with particular reference to the sugar chain.
19017259	1	91	theme	blood	325:329	arg1	pathway					343:349	the extrinsic blood coagulation pathway	311:349	the extrinsic blood coagulation pathway	311:349	BACKGROUND Tissue factor pathway inhibitor (TFPI) is a physiological protease inhibitor that inhibits the initial reactions of the extrinsic blood coagulation pathway.
19017259	3	92	theme	post-translational	650:667	arg1	differences					705:715	the frequent differences	692:715	the frequent differences in sugar chain structures among recombinant proteins	692:768	Cell culture derived TFPI and recombinant TFPI (rTFPI) exhibit variations in their respective anticoagulant activity, which may be caused by post-translational modifications, such as the frequent differences in sugar chain structures among recombinant proteins.
19017259	3	92	theme	post-translational	650:667	arg1	modifications					669:681	post-translational modifications	650:681	post-translational modifications	650:681	Cell culture derived TFPI and recombinant TFPI (rTFPI) exhibit variations in their respective anticoagulant activity, which may be caused by post-translational modifications, such as the frequent differences in sugar chain structures among recombinant proteins.
19017259	4	93	theme	hamster	824:830	arg1	cells					844:848	Chinese hamster ovary (CHO) cells	816:848	Chinese hamster ovary (CHO) cells	816:848	Sugar chain structures in rTFPI expressed in Chinese hamster ovary (CHO) cells have been reported previously, but those of plasma TFPI have not been.
19017259	1	94	theme	pathway	343:349	arg1	reactions					298:306	the initial reactions	286:306	the initial reactions of the extrinsic blood coagulation pathway	286:349	BACKGROUND Tissue factor pathway inhibitor (TFPI) is a physiological protease inhibitor that inhibits the initial reactions of the extrinsic blood coagulation pathway.
19017259	4	95	theme	Sugar	771:775	arg1	structures					783:792	Sugar chain structures	771:792	Sugar chain structures in rTFPI expressed in Chinese hamster ovary (CHO) cells	771:848	Sugar chain structures in rTFPI expressed in Chinese hamster ovary (CHO) cells have been reported previously, but those of plasma TFPI have not been.
19017259	8	96	theme	exoglycosidase	1407:1420	arg1	digestion					1422:1430	exoglycosidase digestion	1407:1430	exoglycosidase digestion of the pyridylamino sugar chains	1407:1463	The sugar chain structures were analyzed by two-dimensional sugar mapping combined with exoglycosidase digestion of the pyridylamino sugar chains and the following results were obtained.
19017259	5	97	theme	chain	972:976	arg1	structures					978:987	the sugar chain structures	962:987	the sugar chain structures	962:987	OBJECTIVES To purify f-pTFPI and analyze the sugar chain structures.
19017259	3	98	theme	Cell	509:512	arg1	culture					514:520	Cell culture	509:520	Cell culture derived TFPI	509:533	Cell culture derived TFPI and recombinant TFPI (rTFPI) exhibit variations in their respective anticoagulant activity, which may be caused by post-translational modifications, such as the frequent differences in sugar chain structures among recombinant proteins.
19017259	1	99	theme	protease	253:260	arg1	inhibitor					217:225	BACKGROUND Tissue factor pathway inhibitor	184:225	BACKGROUND Tissue factor pathway inhibitor (TFPI)	184:232	BACKGROUND Tissue factor pathway inhibitor (TFPI) is a physiological protease inhibitor that inhibits the initial reactions of the extrinsic blood coagulation pathway.
19017259	1	99	theme	protease	253:260	arg1	inhibitor					262:270	a physiological protease inhibitor	237:270	a physiological protease inhibitor that inhibits the initial reactions of the extrinsic blood coagulation pathway	237:349	BACKGROUND Tissue factor pathway inhibitor (TFPI) is a physiological protease inhibitor that inhibits the initial reactions of the extrinsic blood coagulation pathway.
21980294	0	0	theme	receptor	68:75	arg1	nectin-1					77:84	the human receptor nectin-1	58:84	the human receptor nectin-1	58:84	Structure of herpes simplex virus glycoprotein D bound to the human receptor nectin-1.
21980294	6	1	theme	C-terminal	903:912	arg1	residues					914:921	C-terminal residues	903:921	C-terminal residues in the unliganded gD	903:942	Phenylalanine 129, at the tip of the loop connecting β-strands F and G of nectin-1, protrudes into a groove on gD, which is otherwise occupied by C-terminal residues in the unliganded gD and by N-terminal residues in the gD/HVEM complex.
21980294	1	2	theme	glycoprotein	125:136	arg1	gD					141:142	gD	141:142	gD	141:142	Binding of herpes simplex virus (HSV) glycoprotein D (gD) to a cell surface receptor is required to trigger membrane fusion during entry into host cells.
21980294	1	2	theme	glycoprotein	125:136	arg1	D					138:138	herpes simplex virus (HSV) glycoprotein D	98:138	herpes simplex virus (HSV) glycoprotein D (gD)	98:143	Binding of herpes simplex virus (HSV) glycoprotein D (gD) to a cell surface receptor is required to trigger membrane fusion during entry into host cells.
21980294	1	3	theme	membrane	195:202	arg1	fusion					204:209	membrane fusion	195:209	membrane fusion	195:209	Binding of herpes simplex virus (HSV) glycoprotein D (gD) to a cell surface receptor is required to trigger membrane fusion during entry into host cells.
21980294	0	4	theme	human	62:66	arg1	nectin-1					77:84	the human receptor nectin-1	58:84	the human receptor nectin-1	58:84	Structure of herpes simplex virus glycoprotein D bound to the human receptor nectin-1.
21980294	6	5	theme	loop	794:797	arg1	tip					783:785	the tip	779:785	the tip of the loop connecting β-strands F and G of nectin-1	779:838	Phenylalanine 129, at the tip of the loop connecting β-strands F and G of nectin-1, protrudes into a groove on gD, which is otherwise occupied by C-terminal residues in the unliganded gD and by N-terminal residues in the gD/HVEM complex.
21980294	2	6	from	molecule	269:276	arg1	neurons					307:313	neurons	307:313	neurons	307:313	Nectin-1 is a cell adhesion molecule and the main HSV receptor in neurons and epithelial cells.
21980294	2	6	from	molecule	269:276	arg1	cells					330:334	epithelial cells	319:334	epithelial cells	319:334	Nectin-1 is a cell adhesion molecule and the main HSV receptor in neurons and epithelial cells.
21980294	1	7	theme	D	138:138	arg1	Binding					87:93	Binding	87:93	Binding of herpes simplex virus (HSV) glycoprotein D (gD) to a cell surface receptor	87:170	Binding of herpes simplex virus (HSV) glycoprotein D (gD) to a cell surface receptor is required to trigger membrane fusion during entry into host cells.
21980294	6	8	dep	β-strands	810:818	arg1	G					826:826	G	826:826	G	826:826	Phenylalanine 129, at the tip of the loop connecting β-strands F and G of nectin-1, protrudes into a groove on gD, which is otherwise occupied by C-terminal residues in the unliganded gD and by N-terminal residues in the gD/HVEM complex.
21980294	6	8	dep	β-strands	810:818	arg1	F					820:820	F	820:820	F	820:820	Phenylalanine 129, at the tip of the loop connecting β-strands F and G of nectin-1, protrudes into a groove on gD, which is otherwise occupied by C-terminal residues in the unliganded gD and by N-terminal residues in the gD/HVEM complex.
21980294	6	8	dep	β-strands	810:818	arg1	β-strands					810:818	β-strands F and G	810:826	β-strands F and G of nectin-1	810:838	Phenylalanine 129, at the tip of the loop connecting β-strands F and G of nectin-1, protrudes into a groove on gD, which is otherwise occupied by C-terminal residues in the unliganded gD and by N-terminal residues in the gD/HVEM complex.
21980294	5	9	theme	Ig-like	641:647	arg1	molecules					663:671	Ig-like cell adhesion molecules	641:671	Ig-like cell adhesion molecules	641:671	A surface on the first Ig-domain of nectin-1, which mediates homophilic interactions of Ig-like cell adhesion molecules, buries an area composed by residues from both the gD N- and C-terminal extensions.
21980294	5	10	theme	first	570:574	arg1	nectin-1					589:596	nectin-1	589:596	nectin-1	589:596	A surface on the first Ig-domain of nectin-1, which mediates homophilic interactions of Ig-like cell adhesion molecules, buries an area composed by residues from both the gD N- and C-terminal extensions.
21980294	5	10	theme	first	570:574	arg1	Ig-domain					576:584	the first Ig-domain	566:584	the first Ig-domain of nectin-1	566:596	A surface on the first Ig-domain of nectin-1, which mediates homophilic interactions of Ig-like cell adhesion molecules, buries an area composed by residues from both the gD N- and C-terminal extensions.
21980294	2	11	theme	HSV	291:293	arg1	receptor					295:302	the main HSV receptor	282:302	the main HSV receptor in neurons and epithelial cells	282:334	Nectin-1 is a cell adhesion molecule and the main HSV receptor in neurons and epithelial cells.
21980294	9	12	theme	region	1375:1380	arg1	displacement					1341:1352	receptor-mediated displacement	1323:1352	receptor-mediated displacement of the gD C-terminal region	1323:1380	Furthermore, the structure of the complex supports a model in which gD-receptor binding triggers HSV entry through receptor-mediated displacement of the gD C-terminal region.
21980294	5	13	theme	cell	649:652	arg1	molecules					663:671	Ig-like cell adhesion molecules	641:671	Ig-like cell adhesion molecules	641:671	A surface on the first Ig-domain of nectin-1, which mediates homophilic interactions of Ig-like cell adhesion molecules, buries an area composed by residues from both the gD N- and C-terminal extensions.
21980294	6	14	from	groove	858:863	arg1	gD					868:869	gD	868:869	gD	868:869	Phenylalanine 129, at the tip of the loop connecting β-strands F and G of nectin-1, protrudes into a groove on gD, which is otherwise occupied by C-terminal residues in the unliganded gD and by N-terminal residues in the gD/HVEM complex.
21980294	4	15	theme	HVEM	538:541	arg1	receptor					543:550	the HVEM receptor	534:550	the HVEM receptor	534:550	The structure reveals that the nectin-1 binding site on gD differs from the binding site of the HVEM receptor.
21980294	8	16	theme	homophilic	1183:1192	arg1	interactions					1194:1205	the normal nectin-1 homophilic interactions	1163:1205	the normal nectin-1 homophilic interactions	1163:1205	Together these data are consistent with previous studies showing that gD disrupts the normal nectin-1 homophilic interactions.
21980294	3	17	theme	gD	364:365	arg1	structure					351:359	the structure	347:359	the structure of gD bound to nectin-1 determined by x-ray crystallography to 4.0 Å resolution	347:439	We report the structure of gD bound to nectin-1 determined by x-ray crystallography to 4.0 Å resolution.
21980294	5	18	theme	adhesion	654:661	arg1	molecules					663:671	Ig-like cell adhesion molecules	641:671	Ig-like cell adhesion molecules	641:671	A surface on the first Ig-domain of nectin-1, which mediates homophilic interactions of Ig-like cell adhesion molecules, buries an area composed by residues from both the gD N- and C-terminal extensions.
21980294	8	19	with	consistent	1105:1114	arg1	studies					1130:1136	previous studies	1121:1136	previous studies showing that gD disrupts the normal nectin-1 homophilic interactions	1121:1205	Together these data are consistent with previous studies showing that gD disrupts the normal nectin-1 homophilic interactions.
21980294	4	20	theme	binding	518:524	arg1	site					526:529	the binding site	514:529	the binding site of the HVEM receptor	514:550	The structure reveals that the nectin-1 binding site on gD differs from the binding site of the HVEM receptor.
21980294	4	20	theme	binding	518:524	arg1	receptor					543:550	the HVEM receptor	534:550	the HVEM receptor	534:550	The structure reveals that the nectin-1 binding site on gD differs from the binding site of the HVEM receptor.
21980294	2	21	theme	epithelial	319:328	arg1	cells					330:334	epithelial cells	319:334	epithelial cells	319:334	Nectin-1 is a cell adhesion molecule and the main HSV receptor in neurons and epithelial cells.
21980294	6	22	theme	nectin-1	831:838	arg1	G					826:826	G	826:826	G	826:826	Phenylalanine 129, at the tip of the loop connecting β-strands F and G of nectin-1, protrudes into a groove on gD, which is otherwise occupied by C-terminal residues in the unliganded gD and by N-terminal residues in the gD/HVEM complex.
21980294	6	22	theme	nectin-1	831:838	arg1	F					820:820	F	820:820	F	820:820	Phenylalanine 129, at the tip of the loop connecting β-strands F and G of nectin-1, protrudes into a groove on gD, which is otherwise occupied by C-terminal residues in the unliganded gD and by N-terminal residues in the gD/HVEM complex.
21980294	6	22	theme	nectin-1	831:838	arg1	β-strands					810:818	β-strands F and G	810:826	β-strands F and G of nectin-1	810:838	Phenylalanine 129, at the tip of the loop connecting β-strands F and G of nectin-1, protrudes into a groove on gD, which is otherwise occupied by C-terminal residues in the unliganded gD and by N-terminal residues in the gD/HVEM complex.
21980294	7	23	theme	HSV	1070:1072	arg1	entry					1074:1078	HSV entry	1070:1078	HSV entry	1070:1078	Notably, mutation of Phe129 to alanine prevents nectin-1 binding to gD and HSV entry.
21980294	2	24	theme	cell	255:258	arg1	molecule					269:276	a cell adhesion molecule	253:276	a cell adhesion molecule	253:276	Nectin-1 is a cell adhesion molecule and the main HSV receptor in neurons and epithelial cells.
21980294	2	24	theme	cell	255:258	arg1	Nectin-1					241:248	Nectin-1	241:248	Nectin-1	241:248	Nectin-1 is a cell adhesion molecule and the main HSV receptor in neurons and epithelial cells.
21980294	9	25	theme	HSV	1305:1307	arg1	entry					1309:1313	HSV entry	1305:1313	HSV entry	1305:1313	Furthermore, the structure of the complex supports a model in which gD-receptor binding triggers HSV entry through receptor-mediated displacement of the gD C-terminal region.
21980294	4	26	from	site	490:493	arg1	gD					498:499	gD	498:499	gD	498:499	The structure reveals that the nectin-1 binding site on gD differs from the binding site of the HVEM receptor.
21980294	4	27	theme	binding	482:488	arg1	site					490:493	the nectin-1 binding site	469:493	the nectin-1 binding site on gD	469:499	The structure reveals that the nectin-1 binding site on gD differs from the binding site of the HVEM receptor.
21980294	6	28	from	residues	914:921	arg1	gD					941:942	the unliganded gD	926:942	the unliganded gD	926:942	Phenylalanine 129, at the tip of the loop connecting β-strands F and G of nectin-1, protrudes into a groove on gD, which is otherwise occupied by C-terminal residues in the unliganded gD and by N-terminal residues in the gD/HVEM complex.
21980294	0	29	theme	simplex	20:26	arg1	virus					28:32	herpes simplex virus	13:32	herpes simplex virus glycoprotein D	13:47	Structure of herpes simplex virus glycoprotein D bound to the human receptor nectin-1.
21980294	1	30	theme	host	229:232	arg1	cells					234:238	host cells	229:238	host cells	229:238	Binding of herpes simplex virus (HSV) glycoprotein D (gD) to a cell surface receptor is required to trigger membrane fusion during entry into host cells.
21980294	9	31	theme	receptor-mediated	1323:1339	arg1	displacement					1341:1352	receptor-mediated displacement	1323:1352	receptor-mediated displacement of the gD C-terminal region	1323:1380	Furthermore, the structure of the complex supports a model in which gD-receptor binding triggers HSV entry through receptor-mediated displacement of the gD C-terminal region.
21980294	2	32	from	receptor	295:302	arg1	neurons					307:313	neurons	307:313	neurons	307:313	Nectin-1 is a cell adhesion molecule and the main HSV receptor in neurons and epithelial cells.
21980294	2	32	from	receptor	295:302	arg1	cells					330:334	epithelial cells	319:334	epithelial cells	319:334	Nectin-1 is a cell adhesion molecule and the main HSV receptor in neurons and epithelial cells.
21980294	8	33	theme	normal	1167:1172	arg1	interactions					1194:1205	the normal nectin-1 homophilic interactions	1163:1205	the normal nectin-1 homophilic interactions	1163:1205	Together these data are consistent with previous studies showing that gD disrupts the normal nectin-1 homophilic interactions.
21980294	6	34	used	occupied	891:898	arg2	gD					868:869	gD	868:869	gD	868:869	Phenylalanine 129, at the tip of the loop connecting β-strands F and G of nectin-1, protrudes into a groove on gD, which is otherwise occupied by C-terminal residues in the unliganded gD and by N-terminal residues in the gD/HVEM complex.
21980294	4	35	theme	receptor	543:550	arg1	site					526:529	the binding site	514:529	the binding site of the HVEM receptor	514:550	The structure reveals that the nectin-1 binding site on gD differs from the binding site of the HVEM receptor.
21980294	4	35	theme	receptor	543:550	arg1	receptor					543:550	the HVEM receptor	534:550	the HVEM receptor	534:550	The structure reveals that the nectin-1 binding site on gD differs from the binding site of the HVEM receptor.
21980294	0	36	theme	herpes	13:18	arg1	virus					28:32	herpes simplex virus	13:32	herpes simplex virus glycoprotein D	13:47	Structure of herpes simplex virus glycoprotein D bound to the human receptor nectin-1.
21980294	9	37	theme	C-terminal	1364:1373	arg1	region					1375:1380	the gD C-terminal region	1357:1380	the gD C-terminal region	1357:1380	Furthermore, the structure of the complex supports a model in which gD-receptor binding triggers HSV entry through receptor-mediated displacement of the gD C-terminal region.
21980294	2	38	theme	main	286:289	arg1	receptor					295:302	the main HSV receptor	282:302	the main HSV receptor in neurons and epithelial cells	282:334	Nectin-1 is a cell adhesion molecule and the main HSV receptor in neurons and epithelial cells.
21980294	9	39	theme	gD-receptor	1276:1286	arg1	binding					1288:1294	gD-receptor binding	1276:1294	gD-receptor binding	1276:1294	Furthermore, the structure of the complex supports a model in which gD-receptor binding triggers HSV entry through receptor-mediated displacement of the gD C-terminal region.
21980294	1	40	theme	cell	150:153	arg1	receptor					163:170	a cell surface receptor	148:170	a cell surface receptor	148:170	Binding of herpes simplex virus (HSV) glycoprotein D (gD) to a cell surface receptor is required to trigger membrane fusion during entry into host cells.
21980294	0	41	theme	glycoprotein	34:45	arg1	D					47:47	herpes simplex virus glycoprotein D	13:47	herpes simplex virus glycoprotein D	13:47	Structure of herpes simplex virus glycoprotein D bound to the human receptor nectin-1.
21980294	6	42	theme	gD/HVEM	978:984	arg1	complex					986:992	the gD/HVEM complex	974:992	the gD/HVEM complex	974:992	Phenylalanine 129, at the tip of the loop connecting β-strands F and G of nectin-1, protrudes into a groove on gD, which is otherwise occupied by C-terminal residues in the unliganded gD and by N-terminal residues in the gD/HVEM complex.
21980294	5	43	theme	homophilic	614:623	arg1	interactions					625:636	homophilic interactions	614:636	homophilic interactions of Ig-like cell adhesion molecules	614:671	A surface on the first Ig-domain of nectin-1, which mediates homophilic interactions of Ig-like cell adhesion molecules, buries an area composed by residues from both the gD N- and C-terminal extensions.
21980294	5	44	theme	C-terminal	734:743	arg1	extensions					745:754	C-terminal extensions	734:754	C-terminal extensions	734:754	A surface on the first Ig-domain of nectin-1, which mediates homophilic interactions of Ig-like cell adhesion molecules, buries an area composed by residues from both the gD N- and C-terminal extensions.
21980294	1	45	theme	surface	155:161	arg1	receptor					163:170	a cell surface receptor	148:170	a cell surface receptor	148:170	Binding of herpes simplex virus (HSV) glycoprotein D (gD) to a cell surface receptor is required to trigger membrane fusion during entry into host cells.
21980294	0	46	theme	virus	28:32	arg1	D					47:47	herpes simplex virus glycoprotein D	13:47	herpes simplex virus glycoprotein D	13:47	Structure of herpes simplex virus glycoprotein D bound to the human receptor nectin-1.
21980294	7	47	theme	Phe129	1016:1021	arg1	mutation					1004:1011	mutation	1004:1011	mutation of Phe129 to alanine	1004:1032	Notably, mutation of Phe129 to alanine prevents nectin-1 binding to gD and HSV entry.
21980294	8	48	theme	previous	1121:1128	arg1	studies					1130:1136	previous studies	1121:1136	previous studies showing that gD disrupts the normal nectin-1 homophilic interactions	1121:1205	Together these data are consistent with previous studies showing that gD disrupts the normal nectin-1 homophilic interactions.
21980294	6	49	from	tip	783:785	arg1	Phenylalanine					757:769	Phenylalanine 129	757:773	Phenylalanine 129	757:773	Phenylalanine 129, at the tip of the loop connecting β-strands F and G of nectin-1, protrudes into a groove on gD, which is otherwise occupied by C-terminal residues in the unliganded gD and by N-terminal residues in the gD/HVEM complex.
21980294	3	50	theme	Å	428:428	arg1	resolution					430:439	4.0 Å resolution	424:439	4.0 Å resolution	424:439	We report the structure of gD bound to nectin-1 determined by x-ray crystallography to 4.0 Å resolution.
21980294	4	51	theme	nectin-1	473:480	arg1	site					490:493	the nectin-1 binding site	469:493	the nectin-1 binding site on gD	469:499	The structure reveals that the nectin-1 binding site on gD differs from the binding site of the HVEM receptor.
21980294	5	52	from	extensions	745:754	arg1	residues					701:708	residues	701:708	residues from both the gD N- and C-terminal extensions	701:754	A surface on the first Ig-domain of nectin-1, which mediates homophilic interactions of Ig-like cell adhesion molecules, buries an area composed by residues from both the gD N- and C-terminal extensions.
21980294	1	53	theme	herpes	98:103	arg1	virus					113:117	herpes simplex virus	98:117	herpes simplex virus (HSV) glycoprotein D (gD)	98:143	Binding of herpes simplex virus (HSV) glycoprotein D (gD) to a cell surface receptor is required to trigger membrane fusion during entry into host cells.
21980294	1	53	theme	herpes	98:103	arg1	HSV					120:122	HSV	120:122	HSV	120:122	Binding of herpes simplex virus (HSV) glycoprotein D (gD) to a cell surface receptor is required to trigger membrane fusion during entry into host cells.
21980294	0	54	theme	D	47:47	arg1	Structure					0:8	Structure	0:8	Structure of herpes simplex virus glycoprotein D	0:47	Structure of herpes simplex virus glycoprotein D bound to the human receptor nectin-1.
21980294	5	55	from	surface	555:561	arg1	nectin-1					589:596	nectin-1	589:596	nectin-1	589:596	A surface on the first Ig-domain of nectin-1, which mediates homophilic interactions of Ig-like cell adhesion molecules, buries an area composed by residues from both the gD N- and C-terminal extensions.
21980294	5	55	from	surface	555:561	arg1	Ig-domain					576:584	the first Ig-domain	566:584	the first Ig-domain of nectin-1	566:596	A surface on the first Ig-domain of nectin-1, which mediates homophilic interactions of Ig-like cell adhesion molecules, buries an area composed by residues from both the gD N- and C-terminal extensions.
21980294	7	56	theme	nectin-1	1043:1050	arg1	binding					1052:1058	nectin-1 binding	1043:1058	nectin-1 binding to gD and HSV entry	1043:1078	Notably, mutation of Phe129 to alanine prevents nectin-1 binding to gD and HSV entry.
21980294	5	57	from	N-	727:728	arg1	residues					701:708	residues	701:708	residues from both the gD N- and C-terminal extensions	701:754	A surface on the first Ig-domain of nectin-1, which mediates homophilic interactions of Ig-like cell adhesion molecules, buries an area composed by residues from both the gD N- and C-terminal extensions.
21980294	1	58	theme	simplex	105:111	arg1	virus					113:117	herpes simplex virus	98:117	herpes simplex virus (HSV) glycoprotein D (gD)	98:143	Binding of herpes simplex virus (HSV) glycoprotein D (gD) to a cell surface receptor is required to trigger membrane fusion during entry into host cells.
21980294	1	58	theme	simplex	105:111	arg1	HSV					120:122	HSV	120:122	HSV	120:122	Binding of herpes simplex virus (HSV) glycoprotein D (gD) to a cell surface receptor is required to trigger membrane fusion during entry into host cells.
21980294	5	59	theme	nectin-1	589:596	arg1	nectin-1					589:596	nectin-1	589:596	nectin-1	589:596	A surface on the first Ig-domain of nectin-1, which mediates homophilic interactions of Ig-like cell adhesion molecules, buries an area composed by residues from both the gD N- and C-terminal extensions.
21980294	5	59	theme	nectin-1	589:596	arg1	Ig-domain					576:584	the first Ig-domain	566:584	the first Ig-domain of nectin-1	566:596	A surface on the first Ig-domain of nectin-1, which mediates homophilic interactions of Ig-like cell adhesion molecules, buries an area composed by residues from both the gD N- and C-terminal extensions.
21980294	1	60	theme	virus	113:117	arg1	gD					141:142	gD	141:142	gD	141:142	Binding of herpes simplex virus (HSV) glycoprotein D (gD) to a cell surface receptor is required to trigger membrane fusion during entry into host cells.
21980294	1	60	theme	virus	113:117	arg1	D					138:138	herpes simplex virus (HSV) glycoprotein D	98:138	herpes simplex virus (HSV) glycoprotein D (gD)	98:143	Binding of herpes simplex virus (HSV) glycoprotein D (gD) to a cell surface receptor is required to trigger membrane fusion during entry into host cells.
21980294	1	61	gly	glycoprotein	125:136	arg1	glycoprotein					125:136	herpes simplex virus (HSV) glycoprotein D	98:138	herpes simplex virus (HSV) glycoprotein D (gD)	98:143	Binding of herpes simplex virus (HSV) glycoprotein D (gD) to a cell surface receptor is required to trigger membrane fusion during entry into host cells.
21980294	9	62	theme	complex	1242:1248	arg1	structure					1225:1233	the structure	1221:1233	the structure of the complex	1221:1248	Furthermore, the structure of the complex supports a model in which gD-receptor binding triggers HSV entry through receptor-mediated displacement of the gD C-terminal region.
21980294	0	63	gly	glycoprotein	34:45	arg1	glycoprotein					34:45	herpes simplex virus glycoprotein D	13:47	herpes simplex virus glycoprotein D	13:47	Structure of herpes simplex virus glycoprotein D bound to the human receptor nectin-1.
21980294	2	64	theme	adhesion	260:267	arg1	molecule					269:276	a cell adhesion molecule	253:276	a cell adhesion molecule	253:276	Nectin-1 is a cell adhesion molecule and the main HSV receptor in neurons and epithelial cells.
21980294	2	64	theme	adhesion	260:267	arg1	Nectin-1					241:248	Nectin-1	241:248	Nectin-1	241:248	Nectin-1 is a cell adhesion molecule and the main HSV receptor in neurons and epithelial cells.
21980294	8	65	theme	nectin-1	1174:1181	arg1	interactions					1194:1205	the normal nectin-1 homophilic interactions	1163:1205	the normal nectin-1 homophilic interactions	1163:1205	Together these data are consistent with previous studies showing that gD disrupts the normal nectin-1 homophilic interactions.
21980294	3	66	theme	x-ray	399:403	arg1	crystallography					405:419	x-ray crystallography	399:419	x-ray crystallography to 4.0 Å resolution	399:439	We report the structure of gD bound to nectin-1 determined by x-ray crystallography to 4.0 Å resolution.
21980294	5	67	theme	molecules	663:671	arg1	interactions					625:636	homophilic interactions	614:636	homophilic interactions of Ig-like cell adhesion molecules	614:671	A surface on the first Ig-domain of nectin-1, which mediates homophilic interactions of Ig-like cell adhesion molecules, buries an area composed by residues from both the gD N- and C-terminal extensions.
21980294	9	68	theme	gD	1361:1362	arg1	region					1375:1380	the gD C-terminal region	1357:1380	the gD C-terminal region	1357:1380	Furthermore, the structure of the complex supports a model in which gD-receptor binding triggers HSV entry through receptor-mediated displacement of the gD C-terminal region.
21980294	6	69	theme	unliganded	930:939	arg1	gD					941:942	the unliganded gD	926:942	the unliganded gD	926:942	Phenylalanine 129, at the tip of the loop connecting β-strands F and G of nectin-1, protrudes into a groove on gD, which is otherwise occupied by C-terminal residues in the unliganded gD and by N-terminal residues in the gD/HVEM complex.
21980294	5	70	theme	gD	724:725	arg1	N-					727:728	the gD N-	720:728	the gD N-	720:728	A surface on the first Ig-domain of nectin-1, which mediates homophilic interactions of Ig-like cell adhesion molecules, buries an area composed by residues from both the gD N- and C-terminal extensions.
21980294	6	71	from	residues	962:969	arg1	complex					986:992	the gD/HVEM complex	974:992	the gD/HVEM complex	974:992	Phenylalanine 129, at the tip of the loop connecting β-strands F and G of nectin-1, protrudes into a groove on gD, which is otherwise occupied by C-terminal residues in the unliganded gD and by N-terminal residues in the gD/HVEM complex.
21980294	6	72	theme	N-terminal	951:960	arg1	residues					962:969	N-terminal residues	951:969	N-terminal residues in the gD/HVEM complex	951:992	Phenylalanine 129, at the tip of the loop connecting β-strands F and G of nectin-1, protrudes into a groove on gD, which is otherwise occupied by C-terminal residues in the unliganded gD and by N-terminal residues in the gD/HVEM complex.
20837704	2	0	theme	rod-like	468:475	arg1	domain					477:482	the extended, rod-like domain IV	454:485	domain	477:482	A crystal structure of the extracellular domain of EGFR dimerized by epidermal growth factor (EGF) reveals the extended, rod-like domain IV and a small, hydrophobic domain IV interface compatible with flexibility.
20837704	4	1	from	association	802:812	arg1	turns					841:845	the first two α-helical turns	817:845	the first two α-helical turns	817:845	Disulfide cross-linking of the transmembrane domain shows that EGF stimulates only moderate association in the first two α-helical turns, in contrast to association throughout the membrane over five α-helical turns in glycophorin A and integrin.
20837704	2	2	theme	crystal	349:355	arg1	structure					357:365	A crystal structure	347:365	A crystal structure of the extracellular domain of EGFR dimerized by epidermal growth factor (EGF)	347:444	A crystal structure of the extracellular domain of EGFR dimerized by epidermal growth factor (EGF) reveals the extended, rod-like domain IV and a small, hydrophobic domain IV interface compatible with flexibility.
20837704	2	3	with	compatible	532:541	arg1	flexibility					548:558	flexibility	548:558	flexibility	548:558	A crystal structure of the extracellular domain of EGFR dimerized by epidermal growth factor (EGF) reveals the extended, rod-like domain IV and a small, hydrophobic domain IV interface compatible with flexibility.
20837704	3	4	dep	extracellular	657:669	arg1	domains					689:695	domains	689:695	domains	689:695	The crystal structure and disulfide cross-linking suggest that the 7-residue linker between the extracellular and transmembrane domains is flexible.
20837704	0	5	theme	epidermal	90:98	arg1	receptor					114:121	the epidermal growth factor receptor	86:121	the epidermal growth factor receptor	86:121	Structural evidence for loose linkage between ligand binding and kinase activation in the epidermal growth factor receptor.
20837704	6	6	theme	kinase	1197:1202	arg1	activation					1204:1213	tyrosine kinase activation	1188:1213	tyrosine kinase activation	1188:1213	These results suggest that linkage between ligand-induced dimerization and tyrosine kinase activation is much looser than was previously envisioned.
20837704	1	7	theme	single-pass	260:270	arg1	domains					286:292	single-pass transmembrane domains	260:292	single-pass transmembrane domains such as the epidermal growth factor receptor (EGFR)	260:344	The mechanisms by which signals are transmitted across the plasma membrane to regulate signaling are largely unknown for receptors with single-pass transmembrane domains such as the epidermal growth factor receptor (EGFR).
20837704	1	7	theme	single-pass	260:270	arg1	receptor					330:337	the epidermal growth factor receptor	302:337	the epidermal growth factor receptor (EGFR)	302:344	The mechanisms by which signals are transmitted across the plasma membrane to regulate signaling are largely unknown for receptors with single-pass transmembrane domains such as the epidermal growth factor receptor (EGFR).
20837704	2	8	theme	small	493:497	arg1	domain					512:517	a small, hydrophobic domain	491:517	a small, hydrophobic domain IV interface compatible with flexibility	491:558	A crystal structure of the extracellular domain of EGFR dimerized by epidermal growth factor (EGF) reveals the extended, rod-like domain IV and a small, hydrophobic domain IV interface compatible with flexibility.
20837704	0	9	from	binding	53:59	arg1	receptor					114:121	the epidermal growth factor receptor	86:121	the epidermal growth factor receptor	86:121	Structural evidence for loose linkage between ligand binding and kinase activation in the epidermal growth factor receptor.
20837704	1	10	theme	transmembrane	272:284	arg1	domains					286:292	single-pass transmembrane domains	260:292	single-pass transmembrane domains such as the epidermal growth factor receptor (EGFR)	260:344	The mechanisms by which signals are transmitted across the plasma membrane to regulate signaling are largely unknown for receptors with single-pass transmembrane domains such as the epidermal growth factor receptor (EGFR).
20837704	1	10	theme	transmembrane	272:284	arg1	receptor					330:337	the epidermal growth factor receptor	302:337	the epidermal growth factor receptor (EGFR)	302:344	The mechanisms by which signals are transmitted across the plasma membrane to regulate signaling are largely unknown for receptors with single-pass transmembrane domains such as the epidermal growth factor receptor (EGFR).
20837704	0	11	theme	factor	107:112	arg1	receptor					114:121	the epidermal growth factor receptor	86:121	the epidermal growth factor receptor	86:121	Structural evidence for loose linkage between ligand binding and kinase activation in the epidermal growth factor receptor.
20837704	4	12	theme	moderate	793:800	arg1	association					802:812	only moderate association	788:812	only moderate association in the first two α-helical turns	788:845	Disulfide cross-linking of the transmembrane domain shows that EGF stimulates only moderate association in the first two α-helical turns, in contrast to association throughout the membrane over five α-helical turns in glycophorin A and integrin.
20837704	0	13	theme	growth	100:105	arg1	receptor					114:121	the epidermal growth factor receptor	86:121	the epidermal growth factor receptor	86:121	Structural evidence for loose linkage between ligand binding and kinase activation in the epidermal growth factor receptor.
20837704	2	14	theme	domain	388:393	arg1	structure					357:365	A crystal structure	347:365	A crystal structure of the extracellular domain of EGFR dimerized by epidermal growth factor (EGF)	347:444	A crystal structure of the extracellular domain of EGFR dimerized by epidermal growth factor (EGF) reveals the extended, rod-like domain IV and a small, hydrophobic domain IV interface compatible with flexibility.
20837704	4	15	dep	association	863:873	arg1	contrast					851:858	contrast	851:858	contrast	851:858	Disulfide cross-linking of the transmembrane domain shows that EGF stimulates only moderate association in the first two α-helical turns, in contrast to association throughout the membrane over five α-helical turns in glycophorin A and integrin.
20837704	4	16	theme	domain	755:760	arg1	cross-linking					720:732	Disulfide cross-linking	710:732	Disulfide cross-linking of the transmembrane domain	710:760	Disulfide cross-linking of the transmembrane domain shows that EGF stimulates only moderate association in the first two α-helical turns, in contrast to association throughout the membrane over five α-helical turns in glycophorin A and integrin.
20837704	2	17	theme	extracellular	374:386	arg1	domain					388:393	the extracellular domain	370:393	the extracellular domain of EGFR dimerized by epidermal growth factor (EGF)	370:444	A crystal structure of the extracellular domain of EGFR dimerized by epidermal growth factor (EGF) reveals the extended, rod-like domain IV and a small, hydrophobic domain IV interface compatible with flexibility.
20837704	2	17	theme	extracellular	374:386	arg1	EGFR					398:401	EGFR	398:401	EGFR dimerized by epidermal growth factor (EGF)	398:444	A crystal structure of the extracellular domain of EGFR dimerized by epidermal growth factor (EGF) reveals the extended, rod-like domain IV and a small, hydrophobic domain IV interface compatible with flexibility.
20837704	0	18	theme	Structural	0:9	arg1	evidence					11:18	Structural evidence	0:18	Structural evidence for loose linkage between ligand binding and kinase activation in the epidermal growth factor receptor.	0:122	Structural evidence for loose linkage between ligand binding and kinase activation in the epidermal growth factor receptor.
20837704	4	19	theme	transmembrane	741:753	arg1	domain					755:760	the transmembrane domain	737:760	the transmembrane domain	737:760	Disulfide cross-linking of the transmembrane domain shows that EGF stimulates only moderate association in the first two α-helical turns, in contrast to association throughout the membrane over five α-helical turns in glycophorin A and integrin.
20837704	1	20	theme	plasma	183:188	arg1	membrane					190:197	the plasma membrane	179:197	the plasma membrane	179:197	The mechanisms by which signals are transmitted across the plasma membrane to regulate signaling are largely unknown for receptors with single-pass transmembrane domains such as the epidermal growth factor receptor (EGFR).
20837704	0	21	theme	loose	24:28	arg1	linkage					30:36	loose linkage	24:36	loose linkage between ligand binding and kinase activation in the epidermal growth factor receptor	24:121	Structural evidence for loose linkage between ligand binding and kinase activation in the epidermal growth factor receptor.
20837704	4	22	theme	first	821:825	arg1	turns					841:845	the first two α-helical turns	817:845	the first two α-helical turns	817:845	Disulfide cross-linking of the transmembrane domain shows that EGF stimulates only moderate association in the first two α-helical turns, in contrast to association throughout the membrane over five α-helical turns in glycophorin A and integrin.
20837704	5	23	theme	specific	1038:1045	arg1	interfaces					1061:1070	no specific transmembrane interfaces	1035:1070	no specific transmembrane interfaces	1035:1070	Furthermore, systematic mutagenesis to leucine and phenylalanine suggests that no specific transmembrane interfaces are required for EGFR kinase activation.
20837704	2	24	theme	epidermal	416:424	arg1	EGF					441:443	EGF	441:443	EGF	441:443	A crystal structure of the extracellular domain of EGFR dimerized by epidermal growth factor (EGF) reveals the extended, rod-like domain IV and a small, hydrophobic domain IV interface compatible with flexibility.
20837704	2	24	theme	epidermal	416:424	arg1	factor					433:438	epidermal growth factor	416:438	epidermal growth factor (EGF)	416:444	A crystal structure of the extracellular domain of EGFR dimerized by epidermal growth factor (EGF) reveals the extended, rod-like domain IV and a small, hydrophobic domain IV interface compatible with flexibility.
20837704	2	25	theme	growth	426:431	arg1	EGF					441:443	EGF	441:443	EGF	441:443	A crystal structure of the extracellular domain of EGFR dimerized by epidermal growth factor (EGF) reveals the extended, rod-like domain IV and a small, hydrophobic domain IV interface compatible with flexibility.
20837704	2	25	theme	growth	426:431	arg1	factor					433:438	epidermal growth factor	416:438	epidermal growth factor (EGF)	416:444	A crystal structure of the extracellular domain of EGFR dimerized by epidermal growth factor (EGF) reveals the extended, rod-like domain IV and a small, hydrophobic domain IV interface compatible with flexibility.
20837704	4	26	theme	glycophorin	928:938	arg1	A					940:940	glycophorin A	928:940	glycophorin A	928:940	Disulfide cross-linking of the transmembrane domain shows that EGF stimulates only moderate association in the first two α-helical turns, in contrast to association throughout the membrane over five α-helical turns in glycophorin A and integrin.
20837704	5	27	theme	systematic	969:978	arg1	mutagenesis					980:990	systematic mutagenesis	969:990	systematic mutagenesis to leucine and phenylalanine	969:1019	Furthermore, systematic mutagenesis to leucine and phenylalanine suggests that no specific transmembrane interfaces are required for EGFR kinase activation.
20837704	2	28	theme	extended	458:465	arg1	domain					477:482	the extended, rod-like domain IV	454:485	domain	477:482	A crystal structure of the extracellular domain of EGFR dimerized by epidermal growth factor (EGF) reveals the extended, rod-like domain IV and a small, hydrophobic domain IV interface compatible with flexibility.
20837704	0	29	from	activation	72:81	arg1	receptor					114:121	the epidermal growth factor receptor	86:121	the epidermal growth factor receptor	86:121	Structural evidence for loose linkage between ligand binding and kinase activation in the epidermal growth factor receptor.
20837704	4	30	theme	α-helical	831:839	arg1	turns					841:845	the first two α-helical turns	817:845	the first two α-helical turns	817:845	Disulfide cross-linking of the transmembrane domain shows that EGF stimulates only moderate association in the first two α-helical turns, in contrast to association throughout the membrane over five α-helical turns in glycophorin A and integrin.
20837704	1	31	theme	epidermal	306:314	arg1	EGFR					340:343	EGFR	340:343	EGFR	340:343	The mechanisms by which signals are transmitted across the plasma membrane to regulate signaling are largely unknown for receptors with single-pass transmembrane domains such as the epidermal growth factor receptor (EGFR).
20837704	1	31	theme	epidermal	306:314	arg1	receptor					330:337	the epidermal growth factor receptor	302:337	the epidermal growth factor receptor (EGFR)	302:344	The mechanisms by which signals are transmitted across the plasma membrane to regulate signaling are largely unknown for receptors with single-pass transmembrane domains such as the epidermal growth factor receptor (EGFR).
20837704	2	32	dep	small	493:497	arg1	hydrophobic					500:510	hydrophobic	500:510	hydrophobic	500:510	A crystal structure of the extracellular domain of EGFR dimerized by epidermal growth factor (EGF) reveals the extended, rod-like domain IV and a small, hydrophobic domain IV interface compatible with flexibility.
20837704	2	33	dep	EGFR	398:401	arg1	dimerized					403:411	dimerized	403:411	dimerized	403:411	A crystal structure of the extracellular domain of EGFR dimerized by epidermal growth factor (EGF) reveals the extended, rod-like domain IV and a small, hydrophobic domain IV interface compatible with flexibility.
20837704	2	34	theme	EGFR	398:401	arg1	domain					388:393	the extracellular domain	370:393	the extracellular domain of EGFR dimerized by epidermal growth factor (EGF)	370:444	A crystal structure of the extracellular domain of EGFR dimerized by epidermal growth factor (EGF) reveals the extended, rod-like domain IV and a small, hydrophobic domain IV interface compatible with flexibility.
20837704	2	34	theme	EGFR	398:401	arg1	EGFR					398:401	EGFR	398:401	EGFR dimerized by epidermal growth factor (EGF)	398:444	A crystal structure of the extracellular domain of EGFR dimerized by epidermal growth factor (EGF) reveals the extended, rod-like domain IV and a small, hydrophobic domain IV interface compatible with flexibility.
20837704	1	35	theme	growth	316:321	arg1	EGFR					340:343	EGFR	340:343	EGFR	340:343	The mechanisms by which signals are transmitted across the plasma membrane to regulate signaling are largely unknown for receptors with single-pass transmembrane domains such as the epidermal growth factor receptor (EGFR).
20837704	1	35	theme	growth	316:321	arg1	receptor					330:337	the epidermal growth factor receptor	302:337	the epidermal growth factor receptor (EGFR)	302:344	The mechanisms by which signals are transmitted across the plasma membrane to regulate signaling are largely unknown for receptors with single-pass transmembrane domains such as the epidermal growth factor receptor (EGFR).
20837704	4	36	theme	α-helical	909:917	arg1	turns					919:923	five α-helical turns	904:923	five α-helical turns in glycophorin A and integrin	904:953	Disulfide cross-linking of the transmembrane domain shows that EGF stimulates only moderate association in the first two α-helical turns, in contrast to association throughout the membrane over five α-helical turns in glycophorin A and integrin.
20837704	3	37	theme	7-residue	628:636	arg1	linker					638:643	the 7-residue linker	624:643	the 7-residue linker between the extracellular and transmembrane domains	624:695	The crystal structure and disulfide cross-linking suggest that the 7-residue linker between the extracellular and transmembrane domains is flexible.
20837704	3	37	theme	7-residue	628:636	arg1	flexible					700:707	flexible	700:707	flexible	700:707	The crystal structure and disulfide cross-linking suggest that the 7-residue linker between the extracellular and transmembrane domains is flexible.
20837704	6	38	theme	tyrosine	1188:1195	arg1	kinase					1197:1202	tyrosine kinase	1188:1202	tyrosine kinase activation	1188:1213	These results suggest that linkage between ligand-induced dimerization and tyrosine kinase activation is much looser than was previously envisioned.
20837704	0	39	theme	ligand	46:51	arg1	binding					53:59	ligand binding	46:59	ligand binding	46:59	Structural evidence for loose linkage between ligand binding and kinase activation in the epidermal growth factor receptor.
20837704	1	40	theme	factor	323:328	arg1	EGFR					340:343	EGFR	340:343	EGFR	340:343	The mechanisms by which signals are transmitted across the plasma membrane to regulate signaling are largely unknown for receptors with single-pass transmembrane domains such as the epidermal growth factor receptor (EGFR).
20837704	1	40	theme	factor	323:328	arg1	receptor					330:337	the epidermal growth factor receptor	302:337	the epidermal growth factor receptor (EGFR)	302:344	The mechanisms by which signals are transmitted across the plasma membrane to regulate signaling are largely unknown for receptors with single-pass transmembrane domains such as the epidermal growth factor receptor (EGFR).
20837704	3	41	theme	crystal	565:571	arg1	structure					573:581	The crystal structure	561:581	The crystal structure	561:581	The crystal structure and disulfide cross-linking suggest that the 7-residue linker between the extracellular and transmembrane domains is flexible.
20837704	1	42	with	receptors	245:253	arg1	domains					286:292	single-pass transmembrane domains	260:292	single-pass transmembrane domains such as the epidermal growth factor receptor (EGFR)	260:344	The mechanisms by which signals are transmitted across the plasma membrane to regulate signaling are largely unknown for receptors with single-pass transmembrane domains such as the epidermal growth factor receptor (EGFR).
20837704	1	42	with	receptors	245:253	arg1	receptor					330:337	the epidermal growth factor receptor	302:337	the epidermal growth factor receptor (EGFR)	302:344	The mechanisms by which signals are transmitted across the plasma membrane to regulate signaling are largely unknown for receptors with single-pass transmembrane domains such as the epidermal growth factor receptor (EGFR).
20837704	4	43	theme	Disulfide	710:718	arg1	cross-linking					720:732	Disulfide cross-linking	710:732	Disulfide cross-linking of the transmembrane domain	710:760	Disulfide cross-linking of the transmembrane domain shows that EGF stimulates only moderate association in the first two α-helical turns, in contrast to association throughout the membrane over five α-helical turns in glycophorin A and integrin.
20837704	4	44	from	turns	919:923	arg1	A					940:940	glycophorin A	928:940	glycophorin A	928:940	Disulfide cross-linking of the transmembrane domain shows that EGF stimulates only moderate association in the first two α-helical turns, in contrast to association throughout the membrane over five α-helical turns in glycophorin A and integrin.
20837704	4	44	from	turns	919:923	arg1	integrin					946:953	integrin	946:953	integrin	946:953	Disulfide cross-linking of the transmembrane domain shows that EGF stimulates only moderate association in the first two α-helical turns, in contrast to association throughout the membrane over five α-helical turns in glycophorin A and integrin.
20837704	5	45	theme	transmembrane	1047:1059	arg1	interfaces					1061:1070	no specific transmembrane interfaces	1035:1070	no specific transmembrane interfaces	1035:1070	Furthermore, systematic mutagenesis to leucine and phenylalanine suggests that no specific transmembrane interfaces are required for EGFR kinase activation.
20837704	2	46	theme	compatible	532:541	arg1	domain					512:517	a small, hydrophobic domain	491:517	a small, hydrophobic domain IV interface compatible with flexibility	491:558	A crystal structure of the extracellular domain of EGFR dimerized by epidermal growth factor (EGF) reveals the extended, rod-like domain IV and a small, hydrophobic domain IV interface compatible with flexibility.
20837704	5	47	theme	EGFR	1089:1092	arg1	activation					1101:1110	EGFR kinase activation	1089:1110	EGFR kinase activation	1089:1110	Furthermore, systematic mutagenesis to leucine and phenylalanine suggests that no specific transmembrane interfaces are required for EGFR kinase activation.
20837704	6	48	theme	ligand-induced	1156:1169	arg1	dimerization					1171:1182	ligand-induced dimerization	1156:1182	ligand-induced dimerization	1156:1182	These results suggest that linkage between ligand-induced dimerization and tyrosine kinase activation is much looser than was previously envisioned.
20837704	0	49	theme	kinase	65:70	arg1	activation					72:81	kinase activation	65:81	kinase activation	65:81	Structural evidence for loose linkage between ligand binding and kinase activation in the epidermal growth factor receptor.
20837704	5	50	theme	kinase	1094:1099	arg1	activation					1101:1110	EGFR kinase activation	1089:1110	EGFR kinase activation	1089:1110	Furthermore, systematic mutagenesis to leucine and phenylalanine suggests that no specific transmembrane interfaces are required for EGFR kinase activation.
20837704	3	51	theme	disulfide	587:595	arg1	cross-linking					597:609	disulfide cross-linking	587:609	disulfide cross-linking	587:609	The crystal structure and disulfide cross-linking suggest that the 7-residue linker between the extracellular and transmembrane domains is flexible.
3756141	0	0	theme	chromosomal	57:67	arg1	localization					69:80	chromosomal localization	57:80	chromosomal localization	57:80	Human C1 inhibitor: primary structure, cDNA cloning, and chromosomal localization.
3756141	5	1	theme	sequence	720:727	arg1	Glx-Pro-Thr-Thr					729:743	the tetrapeptide sequence Glx-Pro-Thr-Thr	703:743	the tetrapeptide sequence Glx-Pro-Thr-Thr	703:743	Most of the carbohydrate prosthetic groups (probably 17) are located at the amino-terminal end (residues 1-120) of the protein and are particularly concentrated in a region where the tetrapeptide sequence Glx-Pro-Thr-Thr, and variants thereof, is repeated 7 times.
3756141	4	2	gly	glycosylated	510:521	arg1	residues					483:490	Another nine threonine residues	460:490	Another nine threonine residues	460:490	Another nine threonine residues are probably also glycosylated.
3756141	2	3	theme	molecular	302:310	arg1	mass					312:315	the apparent molecular mass	289:315	the apparent molecular mass of the circulating protein (104,000 Da)	289:355	The single-chain polypeptide moiety of the intact inhibitor is 478 residues (52,869 Da), accounting for only 51% of the apparent molecular mass of the circulating protein (104,000 Da).
3756141	5	4	located	located	585:591	arg2	Most					524:527	Most	524:527	Most	524:527	Most of the carbohydrate prosthetic groups (probably 17) are located at the amino-terminal end (residues 1-120) of the protein and are particularly concentrated in a region where the tetrapeptide sequence Glx-Pro-Thr-Thr, and variants thereof, is repeated 7 times.
3756141	5	4	located	located	585:591	arg1	residues					620:627	residues 1-120	620:633	residues 1-120	620:633	Most of the carbohydrate prosthetic groups (probably 17) are located at the amino-terminal end (residues 1-120) of the protein and are particularly concentrated in a region where the tetrapeptide sequence Glx-Pro-Thr-Thr, and variants thereof, is repeated 7 times.
3756141	5	4	located	located	585:591	arg1	end					615:617	the amino-terminal end	596:617	the amino-terminal end (residues 1-120) of the protein	596:649	Most of the carbohydrate prosthetic groups (probably 17) are located at the amino-terminal end (residues 1-120) of the protein and are particularly concentrated in a region where the tetrapeptide sequence Glx-Pro-Thr-Thr, and variants thereof, is repeated 7 times.
3756141	5	4	located	located	585:591	arg2	groups					560:565	the carbohydrate prosthetic groups	532:565	the carbohydrate prosthetic groups (probably 17)	532:579	Most of the carbohydrate prosthetic groups (probably 17) are located at the amino-terminal end (residues 1-120) of the protein and are particularly concentrated in a region where the tetrapeptide sequence Glx-Pro-Thr-Thr, and variants thereof, is repeated 7 times.
3756141	14	5	theme	sequence	1694:1701	arg1	variants					1703:1710	sequence variants	1694:1710	sequence variants	1694:1710	A HgiAI DNA polymorphism, identified following the observation of sequence variants, will be useful as a linkage marker in studies of mutant C1 inhibitor genes.
3756141	11	6	theme	nonconserved	1320:1331	arg1	regions					1333:1339	conserved and nonconserved regions	1306:1339	conserved and nonconserved regions	1306:1339	The sequence was compared with those of nine other serpins, and conserved and nonconserved regions correlated with elements in the tertiary structure of alpha 1-antitrypsin.
3756141	12	7	theme	C1	1420:1421	arg1	gene					1433:1436	The C1 inhibitor gene	1416:1436	The C1 inhibitor gene	1416:1436	The C1 inhibitor gene maps to chromosome 11, p11.2-q13.
3756141	8	8	theme	amino	943:947	arg1	acid					949:952	the amino acid and cDNA sequences	939:971	acid	949:952	Comparison of the amino acid and cDNA sequences indicates that secretion is mediated by a 22-residue signal peptide and that further proteolytic processing does not occur.
3756141	2	9	theme	apparent	293:300	arg1	mass					312:315	the apparent molecular mass	289:315	the apparent molecular mass of the circulating protein (104,000 Da)	289:355	The single-chain polypeptide moiety of the intact inhibitor is 478 residues (52,869 Da), accounting for only 51% of the apparent molecular mass of the circulating protein (104,000 Da).
3756141	6	10	located	detected	806:813	arg1	inhibitor					821:829	C1 inhibitor	818:829	C1 inhibitor	818:829	No phosphate was detected in C1 inhibitor.
3756141	6	10	located	detected	806:813	arg2	phosphate					792:800	No phosphate	789:800	No phosphate	789:800	No phosphate was detected in C1 inhibitor.
3756141	9	11	theme	family	1175:1180	arg1	inhibitor					1100:1108	C1 inhibitor	1097:1108	C1 inhibitor	1097:1108	C1 inhibitor is a member of the large serine protease inhibitor (serpin) gene family.
3756141	9	11	theme	family	1175:1180	arg1	member					1115:1120	a member	1113:1120	a member of the large serine protease inhibitor (serpin) gene family	1113:1180	C1 inhibitor is a member of the large serine protease inhibitor (serpin) gene family.
3756141	4	12	theme	threonine	473:481	arg1	residues					483:490	Another nine threonine residues	460:490	Another nine threonine residues	460:490	Another nine threonine residues are probably also glycosylated.
3756141	9	13	theme	serine	1135:1140	arg1	family					1175:1180	the large serine protease inhibitor (serpin) gene family	1125:1180	the large serine protease inhibitor (serpin) gene family	1125:1180	C1 inhibitor is a member of the large serine protease inhibitor (serpin) gene family.
3756141	8	14	theme	signal	1026:1031	arg1	peptide					1033:1039	a 22-residue signal peptide	1013:1039	a 22-residue signal peptide	1013:1039	Comparison of the amino acid and cDNA sequences indicates that secretion is mediated by a 22-residue signal peptide and that further proteolytic processing does not occur.
3756141	14	15	from	marker	1741:1746	arg1	studies					1751:1757	studies	1751:1757	studies of mutant C1 inhibitor genes	1751:1786	A HgiAI DNA polymorphism, identified following the observation of sequence variants, will be useful as a linkage marker in studies of mutant C1 inhibitor genes.
3756141	8	16	theme	sequences	963:971	arg1	Comparison					925:934	Comparison	925:934	Comparison of the amino acid and cDNA sequences	925:971	Comparison of the amino acid and cDNA sequences indicates that secretion is mediated by a 22-residue signal peptide and that further proteolytic processing does not occur.
3756141	13	17	contain	have	1560:1563	arg2	deletions					1573:1581	obvious deletions	1565:1581	obvious deletions	1565:1581	C1 inhibitor genes of patients from four hereditary angioneurotic edema kindreds do not have obvious deletions or rearrangements in the C1 inhibitor locus.
3756141	13	17	contain	have	1560:1563	arg1	genes					1485:1489	C1 inhibitor genes	1472:1489	C1 inhibitor genes of patients from four hereditary angioneurotic edema kindreds	1472:1551	C1 inhibitor genes of patients from four hereditary angioneurotic edema kindreds do not have obvious deletions or rearrangements in the C1 inhibitor locus.
3756141	13	17	contain	have	1560:1563	arg2	rearrangements					1586:1599	rearrangements	1586:1599	rearrangements	1586:1599	C1 inhibitor genes of patients from four hereditary angioneurotic edema kindreds do not have obvious deletions or rearrangements in the C1 inhibitor locus.
3756141	8	18	theme	cDNA	958:961	arg1	sequences					963:971	the amino acid and cDNA sequences	939:971	sequences	963:971	Comparison of the amino acid and cDNA sequences indicates that secretion is mediated by a 22-residue signal peptide and that further proteolytic processing does not occur.
3756141	8	19	theme	22-residue	1015:1024	arg1	peptide					1033:1039	a 22-residue signal peptide	1013:1039	a 22-residue signal peptide	1013:1039	Comparison of the amino acid and cDNA sequences indicates that secretion is mediated by a 22-residue signal peptide and that further proteolytic processing does not occur.
3756141	7	20	theme	disulfide	836:844	arg1	bridges					846:852	Two disulfide bridges	832:852	Two disulfide bridges	832:852	Two disulfide bridges connect cysteine-101 to cysteine-406 and cysteine-108 to cysteine-183.
3756141	1	21	theme	DNA	157:159	arg1	sequencing					161:170	DNA sequencing	157:170	DNA sequencing	157:170	The primary structure of human C1 inhibitor was determined by peptide and DNA sequencing.
3756141	14	22	theme	mutant	1762:1767	arg1	genes					1782:1786	mutant C1 inhibitor genes	1762:1786	mutant C1 inhibitor genes	1762:1786	A HgiAI DNA polymorphism, identified following the observation of sequence variants, will be useful as a linkage marker in studies of mutant C1 inhibitor genes.
3756141	9	23	theme	serpin	1162:1167	arg1	family					1175:1180	the large serine protease inhibitor (serpin) gene family	1125:1180	the large serine protease inhibitor (serpin) gene family	1125:1180	C1 inhibitor is a member of the large serine protease inhibitor (serpin) gene family.
3756141	5	24	theme	carbohydrate	536:547	arg1	groups					560:565	the carbohydrate prosthetic groups	532:565	the carbohydrate prosthetic groups (probably 17)	532:579	Most of the carbohydrate prosthetic groups (probably 17) are located at the amino-terminal end (residues 1-120) of the protein and are particularly concentrated in a region where the tetrapeptide sequence Glx-Pro-Thr-Thr, and variants thereof, is repeated 7 times.
3756141	11	25	theme	other	1287:1291	arg1	serpins					1293:1299	nine other serpins	1282:1299	nine other serpins	1282:1299	The sequence was compared with those of nine other serpins, and conserved and nonconserved regions correlated with elements in the tertiary structure of alpha 1-antitrypsin.
3756141	11	26	theme	tertiary	1373:1380	arg1	structure					1382:1390	the tertiary structure	1369:1390	the tertiary structure of alpha 1-antitrypsin	1369:1413	The sequence was compared with those of nine other serpins, and conserved and nonconserved regions correlated with elements in the tertiary structure of alpha 1-antitrypsin.
3756141	2	27	theme	protein	336:342	arg1	mass					312:315	the apparent molecular mass	289:315	the apparent molecular mass of the circulating protein (104,000 Da)	289:355	The single-chain polypeptide moiety of the intact inhibitor is 478 residues (52,869 Da), accounting for only 51% of the apparent molecular mass of the circulating protein (104,000 Da).
3756141	0	28	theme	C1	6:7	arg1	inhibitor					9:17	Human C1 inhibitor	0:17	Human C1 inhibitor	0:17	Human C1 inhibitor: primary structure, cDNA cloning, and chromosomal localization.
3756141	5	29	theme	prosthetic	549:558	arg1	groups					560:565	the carbohydrate prosthetic groups	532:565	the carbohydrate prosthetic groups (probably 17)	532:579	Most of the carbohydrate prosthetic groups (probably 17) are located at the amino-terminal end (residues 1-120) of the protein and are particularly concentrated in a region where the tetrapeptide sequence Glx-Pro-Thr-Thr, and variants thereof, is repeated 7 times.
3756141	13	30	theme	hereditary	1513:1522	arg1	kindreds					1544:1551	four hereditary angioneurotic edema kindreds	1508:1551	four hereditary angioneurotic edema kindreds	1508:1551	C1 inhibitor genes of patients from four hereditary angioneurotic edema kindreds do not have obvious deletions or rearrangements in the C1 inhibitor locus.
3756141	2	31	theme	circulating	324:334	arg1	protein					336:342	the circulating protein	320:342	the circulating protein (104,000 Da)	320:355	The single-chain polypeptide moiety of the intact inhibitor is 478 residues (52,869 Da), accounting for only 51% of the apparent molecular mass of the circulating protein (104,000 Da).
3756141	2	31	theme	circulating	324:334	arg1	Da					353:354	104,000 Da	345:354	104,000 Da	345:354	The single-chain polypeptide moiety of the intact inhibitor is 478 residues (52,869 Da), accounting for only 51% of the apparent molecular mass of the circulating protein (104,000 Da).
3756141	0	32	theme	Human	0:4	arg1	inhibitor					9:17	Human C1 inhibitor	0:17	Human C1 inhibitor	0:17	Human C1 inhibitor: primary structure, cDNA cloning, and chromosomal localization.
3756141	5	33	theme	amino-terminal	600:613	arg1	residues					620:627	residues 1-120	620:633	residues 1-120	620:633	Most of the carbohydrate prosthetic groups (probably 17) are located at the amino-terminal end (residues 1-120) of the protein and are particularly concentrated in a region where the tetrapeptide sequence Glx-Pro-Thr-Thr, and variants thereof, is repeated 7 times.
3756141	5	33	theme	amino-terminal	600:613	arg1	end					615:617	the amino-terminal end	596:617	the amino-terminal end (residues 1-120) of the protein	596:649	Most of the carbohydrate prosthetic groups (probably 17) are located at the amino-terminal end (residues 1-120) of the protein and are particularly concentrated in a region where the tetrapeptide sequence Glx-Pro-Thr-Thr, and variants thereof, is repeated 7 times.
3756141	13	34	theme	angioneurotic	1524:1536	arg1	kindreds					1544:1551	four hereditary angioneurotic edema kindreds	1508:1551	four hereditary angioneurotic edema kindreds	1508:1551	C1 inhibitor genes of patients from four hereditary angioneurotic edema kindreds do not have obvious deletions or rearrangements in the C1 inhibitor locus.
3756141	14	35	theme	genes	1782:1786	arg1	studies					1751:1757	studies	1751:1757	studies of mutant C1 inhibitor genes	1751:1786	A HgiAI DNA polymorphism, identified following the observation of sequence variants, will be useful as a linkage marker in studies of mutant C1 inhibitor genes.
3756141	8	36	theme	acid	949:952	arg1	Comparison					925:934	Comparison	925:934	Comparison of the amino acid and cDNA sequences	925:971	Comparison of the amino acid and cDNA sequences indicates that secretion is mediated by a 22-residue signal peptide and that further proteolytic processing does not occur.
3756141	13	37	theme	inhibitor	1611:1619	arg1	locus					1621:1625	the C1 inhibitor locus	1604:1625	the C1 inhibitor locus	1604:1625	C1 inhibitor genes of patients from four hereditary angioneurotic edema kindreds do not have obvious deletions or rearrangements in the C1 inhibitor locus.
3756141	9	38	theme	large	1129:1133	arg1	family					1175:1180	the large serine protease inhibitor (serpin) gene family	1125:1180	the large serine protease inhibitor (serpin) gene family	1125:1180	C1 inhibitor is a member of the large serine protease inhibitor (serpin) gene family.
3756141	14	39	theme	inhibitor	1772:1780	arg1	genes					1782:1786	mutant C1 inhibitor genes	1762:1786	mutant C1 inhibitor genes	1762:1786	A HgiAI DNA polymorphism, identified following the observation of sequence variants, will be useful as a linkage marker in studies of mutant C1 inhibitor genes.
3756141	13	40	theme	C1	1608:1609	arg1	locus					1621:1625	the C1 inhibitor locus	1604:1625	the C1 inhibitor locus	1604:1625	C1 inhibitor genes of patients from four hereditary angioneurotic edema kindreds do not have obvious deletions or rearrangements in the C1 inhibitor locus.
3756141	6	41	theme	C1	818:819	arg1	inhibitor					821:829	C1 inhibitor	818:829	C1 inhibitor	818:829	No phosphate was detected in C1 inhibitor.
3756141	1	42	theme	primary	87:93	arg1	structure					95:103	The primary structure	83:103	The primary structure of human C1 inhibitor	83:125	The primary structure of human C1 inhibitor was determined by peptide and DNA sequencing.
3756141	11	43	theme	1-antitrypsin	1401:1413	arg1	structure					1382:1390	the tertiary structure	1369:1390	the tertiary structure of alpha 1-antitrypsin	1369:1413	The sequence was compared with those of nine other serpins, and conserved and nonconserved regions correlated with elements in the tertiary structure of alpha 1-antitrypsin.
3756141	3	44	theme	galactosamine-based	406:424	arg1	oligosaccharides					426:441	five galactosamine-based oligosaccharides	401:441	five galactosamine-based oligosaccharides	401:441	The positions of six glucosamine-based and five galactosamine-based oligosaccharides were determined.
3756141	14	45	theme	HgiAI	1630:1634	arg1	useful					1721:1726	useful	1721:1726	useful	1721:1726	A HgiAI DNA polymorphism, identified following the observation of sequence variants, will be useful as a linkage marker in studies of mutant C1 inhibitor genes.
3756141	14	45	theme	HgiAI	1630:1634	arg1	polymorphism					1640:1651	A HgiAI DNA polymorphism	1628:1651	A HgiAI DNA polymorphism	1628:1651	A HgiAI DNA polymorphism, identified following the observation of sequence variants, will be useful as a linkage marker in studies of mutant C1 inhibitor genes.
3756141	11	46	theme	alpha	1395:1399	arg1	1-antitrypsin					1401:1413	alpha 1-antitrypsin	1395:1413	alpha 1-antitrypsin	1395:1413	The sequence was compared with those of nine other serpins, and conserved and nonconserved regions correlated with elements in the tertiary structure of alpha 1-antitrypsin.
3756141	8	47	theme	proteolytic	1058:1068	arg1	processing					1070:1079	further proteolytic processing	1050:1079	further proteolytic processing	1050:1079	Comparison of the amino acid and cDNA sequences indicates that secretion is mediated by a 22-residue signal peptide and that further proteolytic processing does not occur.
3756141	11	48	from	elements	1357:1364	arg1	structure					1382:1390	the tertiary structure	1369:1390	the tertiary structure of alpha 1-antitrypsin	1369:1413	The sequence was compared with those of nine other serpins, and conserved and nonconserved regions correlated with elements in the tertiary structure of alpha 1-antitrypsin.
3756141	2	49	theme	intact	216:221	arg1	inhibitor					223:231	the intact inhibitor	212:231	the intact inhibitor	212:231	The single-chain polypeptide moiety of the intact inhibitor is 478 residues (52,869 Da), accounting for only 51% of the apparent molecular mass of the circulating protein (104,000 Da).
3756141	13	50	theme	obvious	1565:1571	arg1	deletions					1573:1581	obvious deletions	1565:1581	obvious deletions	1565:1581	C1 inhibitor genes of patients from four hereditary angioneurotic edema kindreds do not have obvious deletions or rearrangements in the C1 inhibitor locus.
3756141	3	51	theme	glucosamine-based	379:395	arg1	positions					362:370	The positions	358:370	The positions of six glucosamine-based and five galactosamine-based oligosaccharides	358:441	The positions of six glucosamine-based and five galactosamine-based oligosaccharides were determined.
3756141	0	52	theme	primary	20:26	arg1	structure					28:36	primary structure	20:36	primary structure	20:36	Human C1 inhibitor: primary structure, cDNA cloning, and chromosomal localization.
3756141	14	53	theme	linkage	1733:1739	arg1	marker					1741:1746	a linkage marker	1731:1746	a linkage marker in studies of mutant C1 inhibitor genes	1731:1786	A HgiAI DNA polymorphism, identified following the observation of sequence variants, will be useful as a linkage marker in studies of mutant C1 inhibitor genes.
3756141	8	54	theme	further	1050:1056	arg1	processing					1070:1079	further proteolytic processing	1050:1079	further proteolytic processing	1050:1079	Comparison of the amino acid and cDNA sequences indicates that secretion is mediated by a 22-residue signal peptide and that further proteolytic processing does not occur.
3756141	13	55	theme	patients	1494:1501	arg1	genes					1485:1489	C1 inhibitor genes	1472:1489	C1 inhibitor genes of patients from four hereditary angioneurotic edema kindreds	1472:1551	C1 inhibitor genes of patients from four hereditary angioneurotic edema kindreds do not have obvious deletions or rearrangements in the C1 inhibitor locus.
3756141	0	56	theme	cDNA	39:42	arg1	cloning					44:50	cDNA cloning	39:50	cDNA cloning	39:50	Human C1 inhibitor: primary structure, cDNA cloning, and chromosomal localization.
3756141	9	57	theme	protease	1142:1149	arg1	family					1175:1180	the large serine protease inhibitor (serpin) gene family	1125:1180	the large serine protease inhibitor (serpin) gene family	1125:1180	C1 inhibitor is a member of the large serine protease inhibitor (serpin) gene family.
3756141	13	58	from	genes	1485:1489	arg1	kindreds					1544:1551	four hereditary angioneurotic edema kindreds	1508:1551	four hereditary angioneurotic edema kindreds	1508:1551	C1 inhibitor genes of patients from four hereditary angioneurotic edema kindreds do not have obvious deletions or rearrangements in the C1 inhibitor locus.
3756141	0	59	dep	structure	28:36	arg1	inhibitor					9:17	Human C1 inhibitor	0:17	Human C1 inhibitor	0:17	Human C1 inhibitor: primary structure, cDNA cloning, and chromosomal localization.
3756141	9	60	theme	C1	1097:1098	arg1	inhibitor					1100:1108	C1 inhibitor	1097:1108	C1 inhibitor	1097:1108	C1 inhibitor is a member of the large serine protease inhibitor (serpin) gene family.
3756141	9	60	theme	C1	1097:1098	arg1	member					1115:1120	a member	1113:1120	a member of the large serine protease inhibitor (serpin) gene family	1113:1180	C1 inhibitor is a member of the large serine protease inhibitor (serpin) gene family.
3756141	14	61	theme	C1	1769:1770	arg1	genes					1782:1786	mutant C1 inhibitor genes	1762:1786	mutant C1 inhibitor genes	1762:1786	A HgiAI DNA polymorphism, identified following the observation of sequence variants, will be useful as a linkage marker in studies of mutant C1 inhibitor genes.
3756141	5	62	from	end	615:617	arg1	located					585:591	located	585:591	located	585:591	Most of the carbohydrate prosthetic groups (probably 17) are located at the amino-terminal end (residues 1-120) of the protein and are particularly concentrated in a region where the tetrapeptide sequence Glx-Pro-Thr-Thr, and variants thereof, is repeated 7 times.
3756141	2	63	theme	polypeptide	190:200	arg1	moiety					202:207	The single-chain polypeptide moiety	173:207	The single-chain polypeptide moiety of the intact inhibitor	173:231	The single-chain polypeptide moiety of the intact inhibitor is 478 residues (52,869 Da), accounting for only 51% of the apparent molecular mass of the circulating protein (104,000 Da).
3756141	2	63	theme	polypeptide	190:200	arg1	residues					240:247	478 residues	236:247	478 residues (52,869 Da)	236:259	The single-chain polypeptide moiety of the intact inhibitor is 478 residues (52,869 Da), accounting for only 51% of the apparent molecular mass of the circulating protein (104,000 Da).
3756141	12	64	theme	inhibitor	1423:1431	arg1	gene					1433:1436	The C1 inhibitor gene	1416:1436	The C1 inhibitor gene	1416:1436	The C1 inhibitor gene maps to chromosome 11, p11.2-q13.
3756141	9	65	theme	gene	1170:1173	arg1	family					1175:1180	the large serine protease inhibitor (serpin) gene family	1125:1180	the large serine protease inhibitor (serpin) gene family	1125:1180	C1 inhibitor is a member of the large serine protease inhibitor (serpin) gene family.
3756141	2	66	theme	single-chain	177:188	arg1	moiety					202:207	The single-chain polypeptide moiety	173:207	The single-chain polypeptide moiety of the intact inhibitor	173:231	The single-chain polypeptide moiety of the intact inhibitor is 478 residues (52,869 Da), accounting for only 51% of the apparent molecular mass of the circulating protein (104,000 Da).
3756141	2	66	theme	single-chain	177:188	arg1	residues					240:247	478 residues	236:247	478 residues (52,869 Da)	236:259	The single-chain polypeptide moiety of the intact inhibitor is 478 residues (52,869 Da), accounting for only 51% of the apparent molecular mass of the circulating protein (104,000 Da).
3756141	14	67	theme	DNA	1636:1638	arg1	useful					1721:1726	useful	1721:1726	useful	1721:1726	A HgiAI DNA polymorphism, identified following the observation of sequence variants, will be useful as a linkage marker in studies of mutant C1 inhibitor genes.
3756141	14	67	theme	DNA	1636:1638	arg1	polymorphism					1640:1651	A HgiAI DNA polymorphism	1628:1651	A HgiAI DNA polymorphism	1628:1651	A HgiAI DNA polymorphism, identified following the observation of sequence variants, will be useful as a linkage marker in studies of mutant C1 inhibitor genes.
3756141	1	68	theme	human	108:112	arg1	inhibitor					117:125	human C1 inhibitor	108:125	human C1 inhibitor	108:125	The primary structure of human C1 inhibitor was determined by peptide and DNA sequencing.
3756141	13	69	theme	edema	1538:1542	arg1	kindreds					1544:1551	four hereditary angioneurotic edema kindreds	1508:1551	four hereditary angioneurotic edema kindreds	1508:1551	C1 inhibitor genes of patients from four hereditary angioneurotic edema kindreds do not have obvious deletions or rearrangements in the C1 inhibitor locus.
3756141	5	70	theme	protein	643:649	arg1	residues					620:627	residues 1-120	620:633	residues 1-120	620:633	Most of the carbohydrate prosthetic groups (probably 17) are located at the amino-terminal end (residues 1-120) of the protein and are particularly concentrated in a region where the tetrapeptide sequence Glx-Pro-Thr-Thr, and variants thereof, is repeated 7 times.
3756141	5	70	theme	protein	643:649	arg1	end					615:617	the amino-terminal end	596:617	the amino-terminal end (residues 1-120) of the protein	596:649	Most of the carbohydrate prosthetic groups (probably 17) are located at the amino-terminal end (residues 1-120) of the protein and are particularly concentrated in a region where the tetrapeptide sequence Glx-Pro-Thr-Thr, and variants thereof, is repeated 7 times.
3756141	13	71	theme	C1	1472:1473	arg1	genes					1485:1489	C1 inhibitor genes	1472:1489	C1 inhibitor genes of patients from four hereditary angioneurotic edema kindreds	1472:1551	C1 inhibitor genes of patients from four hereditary angioneurotic edema kindreds do not have obvious deletions or rearrangements in the C1 inhibitor locus.
3756141	11	72	theme	conserved	1306:1314	arg1	regions					1333:1339	conserved and nonconserved regions	1306:1339	conserved and nonconserved regions	1306:1339	The sequence was compared with those of nine other serpins, and conserved and nonconserved regions correlated with elements in the tertiary structure of alpha 1-antitrypsin.
3756141	1	73	theme	C1	114:115	arg1	inhibitor					117:125	human C1 inhibitor	108:125	human C1 inhibitor	108:125	The primary structure of human C1 inhibitor was determined by peptide and DNA sequencing.
3756141	9	74	theme	inhibitor	1151:1159	arg1	family					1175:1180	the large serine protease inhibitor (serpin) gene family	1125:1180	the large serine protease inhibitor (serpin) gene family	1125:1180	C1 inhibitor is a member of the large serine protease inhibitor (serpin) gene family.
3756141	3	75	theme	oligosaccharides	426:441	arg1	positions					362:370	The positions	358:370	The positions of six glucosamine-based and five galactosamine-based oligosaccharides	358:441	The positions of six glucosamine-based and five galactosamine-based oligosaccharides were determined.
3756141	13	76	theme	inhibitor	1475:1483	arg1	genes					1485:1489	C1 inhibitor genes	1472:1489	C1 inhibitor genes of patients from four hereditary angioneurotic edema kindreds	1472:1551	C1 inhibitor genes of patients from four hereditary angioneurotic edema kindreds do not have obvious deletions or rearrangements in the C1 inhibitor locus.
3756141	7	77	dep	cysteine-406	878:889	arg1	to					908:909	to	908:909	to	908:909	Two disulfide bridges connect cysteine-101 to cysteine-406 and cysteine-108 to cysteine-183.
3756141	7	77	dep	cysteine-406	878:889	arg1	cysteine-183					911:922	cysteine-183	911:922	cysteine-183	911:922	Two disulfide bridges connect cysteine-101 to cysteine-406 and cysteine-108 to cysteine-183.
3756141	1	78	theme	inhibitor	117:125	arg1	structure					95:103	The primary structure	83:103	The primary structure of human C1 inhibitor	83:125	The primary structure of human C1 inhibitor was determined by peptide and DNA sequencing.
3756141	13	79	from	kindreds	1544:1551	arg1	patients					1494:1501	patients	1494:1501	patients from four hereditary angioneurotic edema kindreds	1494:1551	C1 inhibitor genes of patients from four hereditary angioneurotic edema kindreds do not have obvious deletions or rearrangements in the C1 inhibitor locus.
3756141	13	79	from	kindreds	1544:1551	arg1	genes					1485:1489	C1 inhibitor genes	1472:1489	C1 inhibitor genes of patients from four hereditary angioneurotic edema kindreds	1472:1551	C1 inhibitor genes of patients from four hereditary angioneurotic edema kindreds do not have obvious deletions or rearrangements in the C1 inhibitor locus.
3756141	5	80	theme	tetrapeptide	707:718	arg1	Glx-Pro-Thr-Thr					729:743	the tetrapeptide sequence Glx-Pro-Thr-Thr	703:743	the tetrapeptide sequence Glx-Pro-Thr-Thr	703:743	Most of the carbohydrate prosthetic groups (probably 17) are located at the amino-terminal end (residues 1-120) of the protein and are particularly concentrated in a region where the tetrapeptide sequence Glx-Pro-Thr-Thr, and variants thereof, is repeated 7 times.
3756141	2	81	theme	inhibitor	223:231	arg1	moiety					202:207	The single-chain polypeptide moiety	173:207	The single-chain polypeptide moiety of the intact inhibitor	173:231	The single-chain polypeptide moiety of the intact inhibitor is 478 residues (52,869 Da), accounting for only 51% of the apparent molecular mass of the circulating protein (104,000 Da).
3756141	2	81	theme	inhibitor	223:231	arg1	residues					240:247	478 residues	236:247	478 residues (52,869 Da)	236:259	The single-chain polypeptide moiety of the intact inhibitor is 478 residues (52,869 Da), accounting for only 51% of the apparent molecular mass of the circulating protein (104,000 Da).
3756141	2	82	theme	mass	312:315	arg1	mass					312:315	the apparent molecular mass	289:315	the apparent molecular mass of the circulating protein (104,000 Da)	289:355	The single-chain polypeptide moiety of the intact inhibitor is 478 residues (52,869 Da), accounting for only 51% of the apparent molecular mass of the circulating protein (104,000 Da).
3756141	2	82	theme	mass	312:315	arg1	%					284:284	only 51%	277:284	only 51% of the apparent molecular mass of the circulating protein (104,000 Da)	277:355	The single-chain polypeptide moiety of the intact inhibitor is 478 residues (52,869 Da), accounting for only 51% of the apparent molecular mass of the circulating protein (104,000 Da).
3756141	5	83	dep	groups	560:565	arg1	17					577:578	17	577:578	17	577:578	Most of the carbohydrate prosthetic groups (probably 17) are located at the amino-terminal end (residues 1-120) of the protein and are particularly concentrated in a region where the tetrapeptide sequence Glx-Pro-Thr-Thr, and variants thereof, is repeated 7 times.
3756141	14	84	theme	variants	1703:1710	arg1	observation					1679:1689	the observation	1675:1689	the observation of sequence variants	1675:1710	A HgiAI DNA polymorphism, identified following the observation of sequence variants, will be useful as a linkage marker in studies of mutant C1 inhibitor genes.
12421832	13	0	theme	PAPP-A	1724:1729	arg1	bonds					1711:1715	disulfide bonds	1701:1715	disulfide bonds of the PAPP-A	1701:1729	The large number of disulfide bonds of the PAPP-A.
12421832	7	1	attach	derived	1091:1097	arg2	peptides					1082:1089	peptides	1082:1089	peptides derived from purified protein	1082:1119	pro-MBP complex, biochemical analyses of peptides derived from purified protein were performed.
12421832	7	1	attach	derived	1091:1097	arg1	protein					1113:1119	purified protein	1104:1119	purified protein	1104:1119	pro-MBP complex, biochemical analyses of peptides derived from purified protein were performed.
12421832	13	2	theme	bonds	1711:1715	arg1	number					1691:1696	The large number	1681:1696	The large number of disulfide bonds of the PAPP-A	1681:1729	The large number of disulfide bonds of the PAPP-A.
12421832	2	3	theme	plasma	170:175	arg1	metalloproteinase					223:239	a metzincin superfamily metalloproteinase	199:239	a metzincin superfamily metalloproteinase responsible for cleavage of insulin-like growth factor-binding protein-4	199:312	Pregnancy-associated plasma protein-A (PAPP-A) is a metzincin superfamily metalloproteinase responsible for cleavage of insulin-like growth factor-binding protein-4, thus causing release of bound insulin-like growth factor.
12421832	2	3	theme	plasma	170:175	arg1	PAPP-A					188:193	PAPP-A	188:193	PAPP-A	188:193	Pregnancy-associated plasma protein-A (PAPP-A) is a metzincin superfamily metalloproteinase responsible for cleavage of insulin-like growth factor-binding protein-4, thus causing release of bound insulin-like growth factor.
12421832	2	3	theme	plasma	170:175	arg1	protein-A					177:185	Pregnancy-associated plasma protein-A	149:185	Pregnancy-associated plasma protein-A (PAPP-A)	149:194	Pregnancy-associated plasma protein-A (PAPP-A) is a metzincin superfamily metalloproteinase responsible for cleavage of insulin-like growth factor-binding protein-4, thus causing release of bound insulin-like growth factor.
12421832	7	4	theme	peptides	1082:1089	arg1	analyses					1070:1077	pro-MBP complex, biochemical analyses	1041:1077	pro-MBP complex, biochemical analyses of peptides derived from purified protein	1041:1119	pro-MBP complex, biochemical analyses of peptides derived from purified protein were performed.
12421832	12	5	used	occupied	1671:1678	arg2	11					1664:1665	11	1664:1665	11	1664:1665	We also show that of 13 potential sites for N-linked carbohydrate substitution of the PAPP-A subunit, 11 are occupied.
12421832	14	6	theme	pattern	1826:1832	arg1	knowledge					1799:1807	knowledge	1799:1807	knowledge of the disulfide pattern of PAPP-A	1799:1842	pro-MBP complex imposes many restraints on polypeptide folding, and knowledge of the disulfide pattern of PAPP-A will facilitate structural studies based on recombinant expression of individual, putative PAPP-A domains.
12421832	12	7	theme	subunit	1655:1661	arg1	substitution					1628:1639	N-linked carbohydrate substitution	1606:1639	N-linked carbohydrate substitution of the PAPP-A subunit	1606:1661	We also show that of 13 potential sites for N-linked carbohydrate substitution of the PAPP-A subunit, 11 are occupied.
12421832	2	8	theme	growth	358:363	arg1	factor					365:370	bound insulin-like growth factor	339:370	bound insulin-like growth factor	339:370	Pregnancy-associated plasma protein-A (PAPP-A) is a metzincin superfamily metalloproteinase responsible for cleavage of insulin-like growth factor-binding protein-4, thus causing release of bound insulin-like growth factor.
12421832	5	9	theme	other	861:865	arg1	proteins					867:874	other proteins	861:874	other proteins	861:874	Three lin-notch (LNR or LIN-12) modules and five complement control protein modules (also known as SCR modules) have been identified in PAPP-A by sequence similarity with other proteins, but no data are available that allow unambiguous prediction of disulfide bonds of these modules.
12421832	8	10	theme	cysteine	1179:1186	arg1	residues					1188:1195	82 cysteine residues	1176:1195	82 cysteine residues	1176:1195	The PAPP-A subunit contains a total of 82 cysteine residues, of which 81 have been accounted for.
12421832	5	11	dep	modules	766:772	arg1	known					780:784	known	780:784	known as SCR modules	780:799	Three lin-notch (LNR or LIN-12) modules and five complement control protein modules (also known as SCR modules) have been identified in PAPP-A by sequence similarity with other proteins, but no data are available that allow unambiguous prediction of disulfide bonds of these modules.
12421832	13	12	theme	large	1685:1689	arg1	number					1691:1696	The large number	1681:1696	The large number of disulfide bonds of the PAPP-A	1681:1729	The large number of disulfide bonds of the PAPP-A.
12421832	2	13	theme	bound	339:343	arg1	factor					365:370	bound insulin-like growth factor	339:370	bound insulin-like growth factor	339:370	Pregnancy-associated plasma protein-A (PAPP-A) is a metzincin superfamily metalloproteinase responsible for cleavage of insulin-like growth factor-binding protein-4, thus causing release of bound insulin-like growth factor.
12421832	14	14	theme	polypeptide	1774:1784	arg1	folding					1786:1792	polypeptide folding	1774:1792	polypeptide folding	1774:1792	pro-MBP complex imposes many restraints on polypeptide folding, and knowledge of the disulfide pattern of PAPP-A will facilitate structural studies based on recombinant expression of individual, putative PAPP-A domains.
12421832	4	15	theme	global	651:656	arg1	similarity					658:667	global similarity	651:667	global similarity with other proteins	651:687	Except for PAPP-A2, PAPP-A does not share global similarity with other proteins.
12421832	16	16	theme	pro-MBP	2080:2086	arg1	complex					2088:2094	pro-MBP complex	2080:2094	pro-MBP complex	2080:2094	pro-MBP complex, as well as the inhibitory mechanism of pro-MBP.
12421832	7	17	theme	pro-MBP	1041:1047	arg1	analyses					1070:1077	pro-MBP complex, biochemical analyses	1041:1077	pro-MBP complex, biochemical analyses of peptides derived from purified protein	1041:1119	pro-MBP complex, biochemical analyses of peptides derived from purified protein were performed.
12421832	12	18	link	N-linked	1606:1613	arg1	substitution					1628:1639	N-linked carbohydrate substitution	1606:1639	N-linked carbohydrate substitution of the PAPP-A subunit	1606:1661	We also show that of 13 potential sites for N-linked carbohydrate substitution of the PAPP-A subunit, 11 are occupied.
12421832	3	19	theme	PAPP-A	601:606	arg1	inhibitor					588:596	a proteinase inhibitor	575:596	a proteinase inhibitor of PAPP-A	575:606	PAPP-A is secreted as a dimer of 400 kDa but circulates in pregnancy as a disulfide-bound 500-kDa 2:2 complex with the proform of eosinophil major basic protein (pro-MBP), recently shown to function as a proteinase inhibitor of PAPP-A.
12421832	1	20	theme	carbohydrate	124:135	arg1	attachment					137:146	carbohydrate attachment	124:146	carbohydrate attachment	124:146	Disulfide structure and carbohydrate attachment.
12421832	3	21	with	complex	475:481	arg1	proform					492:498	the proform	488:498	the proform of eosinophil major basic protein (pro-MBP), recently shown to function as a proteinase inhibitor of PAPP-A	488:606	PAPP-A is secreted as a dimer of 400 kDa but circulates in pregnancy as a disulfide-bound 500-kDa 2:2 complex with the proform of eosinophil major basic protein (pro-MBP), recently shown to function as a proteinase inhibitor of PAPP-A.
12421832	2	22	theme	protein-4	304:312	arg1	cleavage					257:264	cleavage	257:264	cleavage of insulin-like growth factor-binding protein-4	257:312	Pregnancy-associated plasma protein-A (PAPP-A) is a metzincin superfamily metalloproteinase responsible for cleavage of insulin-like growth factor-binding protein-4, thus causing release of bound insulin-like growth factor.
12421832	12	23	theme	PAPP-A	1648:1653	arg1	subunit					1655:1661	the PAPP-A subunit	1644:1661	the PAPP-A subunit	1644:1661	We also show that of 13 potential sites for N-linked carbohydrate substitution of the PAPP-A subunit, 11 are occupied.
12421832	5	24	theme	protein	758:764	arg1	modules					766:772	five complement control protein modules	734:772	five complement control protein modules (also known as SCR modules)	734:800	Three lin-notch (LNR or LIN-12) modules and five complement control protein modules (also known as SCR modules) have been identified in PAPP-A by sequence similarity with other proteins, but no data are available that allow unambiguous prediction of disulfide bonds of these modules.
12421832	2	25	theme	growth	282:287	arg1	protein-4					304:312	insulin-like growth factor-binding protein-4	269:312	insulin-like growth factor-binding protein-4	269:312	Pregnancy-associated plasma protein-A (PAPP-A) is a metzincin superfamily metalloproteinase responsible for cleavage of insulin-like growth factor-binding protein-4, thus causing release of bound insulin-like growth factor.
12421832	8	26	theme	PAPP-A	1141:1146	arg1	subunit					1148:1154	The PAPP-A subunit	1137:1154	The PAPP-A subunit	1137:1154	The PAPP-A subunit contains a total of 82 cysteine residues, of which 81 have been accounted for.
12421832	0	27	theme	major	79:83	arg1	protein					91:97	eosinophil major basic protein	68:97	eosinophil major basic protein	68:97	Complex of pregnancy-associated plasma protein-A and the proform of eosinophil major basic protein.
12421832	14	28	theme	pro-MBP	1731:1737	arg1	complex					1739:1745	pro-MBP complex	1731:1745	pro-MBP complex	1731:1745	pro-MBP complex imposes many restraints on polypeptide folding, and knowledge of the disulfide pattern of PAPP-A will facilitate structural studies based on recombinant expression of individual, putative PAPP-A domains.
12421832	12	29	theme	carbohydrate	1615:1626	arg1	substitution					1628:1639	N-linked carbohydrate substitution	1606:1639	N-linked carbohydrate substitution of the PAPP-A subunit	1606:1661	We also show that of 13 potential sites for N-linked carbohydrate substitution of the PAPP-A subunit, 11 are occupied.
12421832	15	30	theme	rational	1978:1985	arg1	design					2000:2005	rational experimental design	1978:2005	rational experimental design of functional studies aimed at understanding the formation of the PAPP-A	1978:2078	Furthermore, it will allow rational experimental design of functional studies aimed at understanding the formation of the PAPP-A.
12421832	5	31	dep	lin-notch	696:704	arg1	LIN-12					714:719	LIN-12	714:719	LIN-12	714:719	Three lin-notch (LNR or LIN-12) modules and five complement control protein modules (also known as SCR modules) have been identified in PAPP-A by sequence similarity with other proteins, but no data are available that allow unambiguous prediction of disulfide bonds of these modules.
12421832	5	31	dep	lin-notch	696:704	arg1	LNR					707:709	LNR	707:709	LNR	707:709	Three lin-notch (LNR or LIN-12) modules and five complement control protein modules (also known as SCR modules) have been identified in PAPP-A by sequence similarity with other proteins, but no data are available that allow unambiguous prediction of disulfide bonds of these modules.
12421832	10	32	theme	disulfide	1379:1387	arg1	bond					1389:1392	a single disulfide bond	1370:1392	a single disulfide bond	1370:1392	Within the 2:2 complex, PAPP-A is dimerized by a single disulfide bond; pro-MBP is dimerized by two disulfides, and each PAPP-A subunit is connected to a pro-MBP subunit by two disulfide bonds.
12421832	0	33	theme	protein	91:97	arg1	Complex					0:6	Complex	0:6	Complex of pregnancy-associated plasma protein-A	0:47	Complex of pregnancy-associated plasma protein-A and the proform of eosinophil major basic protein.
12421832	0	33	theme	protein	91:97	arg1	proform					57:63	the proform	53:63	the proform of eosinophil major basic protein	53:97	Complex of pregnancy-associated plasma protein-A and the proform of eosinophil major basic protein.
12421832	5	34	theme	bonds	950:954	arg1	prediction					926:935	unambiguous prediction	914:935	unambiguous prediction of disulfide bonds of these modules	914:971	Three lin-notch (LNR or LIN-12) modules and five complement control protein modules (also known as SCR modules) have been identified in PAPP-A by sequence similarity with other proteins, but no data are available that allow unambiguous prediction of disulfide bonds of these modules.
12421832	3	35	theme	2:2	471:473	arg1	complex					475:481	a disulfide-bound 500-kDa 2:2 complex	445:481	a disulfide-bound 500-kDa 2:2 complex with the proform of eosinophil major basic protein (pro-MBP), recently shown to function as a proteinase inhibitor of PAPP-A	445:606	PAPP-A is secreted as a dimer of 400 kDa but circulates in pregnancy as a disulfide-bound 500-kDa 2:2 complex with the proform of eosinophil major basic protein (pro-MBP), recently shown to function as a proteinase inhibitor of PAPP-A.
12421832	5	36	theme	complement	739:748	arg1	modules					766:772	five complement control protein modules	734:772	five complement control protein modules (also known as SCR modules)	734:800	Three lin-notch (LNR or LIN-12) modules and five complement control protein modules (also known as SCR modules) have been identified in PAPP-A by sequence similarity with other proteins, but no data are available that allow unambiguous prediction of disulfide bonds of these modules.
12421832	14	37	theme	putative	1926:1933	arg1	domains					1942:1948	individual, putative PAPP-A domains	1914:1948	domains	1942:1948	pro-MBP complex imposes many restraints on polypeptide folding, and knowledge of the disulfide pattern of PAPP-A will facilitate structural studies based on recombinant expression of individual, putative PAPP-A domains.
12421832	12	38	theme	potential	1586:1594	arg1	sites					1596:1600	13 potential sites	1583:1600	13 potential sites for N-linked carbohydrate substitution of the PAPP-A subunit	1583:1661	We also show that of 13 potential sites for N-linked carbohydrate substitution of the PAPP-A subunit, 11 are occupied.
12421832	0	39	theme	eosinophil	68:77	arg1	protein					91:97	eosinophil major basic protein	68:97	eosinophil major basic protein	68:97	Complex of pregnancy-associated plasma protein-A and the proform of eosinophil major basic protein.
12421832	3	40	theme	disulfide-bound	447:461	arg1	complex					475:481	a disulfide-bound 500-kDa 2:2 complex	445:481	a disulfide-bound 500-kDa 2:2 complex with the proform of eosinophil major basic protein (pro-MBP), recently shown to function as a proteinase inhibitor of PAPP-A	445:606	PAPP-A is secreted as a dimer of 400 kDa but circulates in pregnancy as a disulfide-bound 500-kDa 2:2 complex with the proform of eosinophil major basic protein (pro-MBP), recently shown to function as a proteinase inhibitor of PAPP-A.
12421832	5	41	theme	unambiguous	914:924	arg1	prediction					926:935	unambiguous prediction	914:935	unambiguous prediction of disulfide bonds of these modules	914:971	Three lin-notch (LNR or LIN-12) modules and five complement control protein modules (also known as SCR modules) have been identified in PAPP-A by sequence similarity with other proteins, but no data are available that allow unambiguous prediction of disulfide bonds of these modules.
12421832	14	42	theme	domains	1942:1948	arg1	expression					1900:1909	recombinant expression	1888:1909	recombinant expression of individual, putative PAPP-A domains	1888:1948	pro-MBP complex imposes many restraints on polypeptide folding, and knowledge of the disulfide pattern of PAPP-A will facilitate structural studies based on recombinant expression of individual, putative PAPP-A domains.
12421832	0	43	theme	pregnancy-associated	11:30	arg1	protein-A					39:47	pregnancy-associated plasma protein-A	11:47	pregnancy-associated plasma protein-A	11:47	Complex of pregnancy-associated plasma protein-A and the proform of eosinophil major basic protein.
12421832	0	44	theme	protein-A	39:47	arg1	Complex					0:6	Complex	0:6	Complex of pregnancy-associated plasma protein-A	0:47	Complex of pregnancy-associated plasma protein-A and the proform of eosinophil major basic protein.
12421832	0	44	theme	protein-A	39:47	arg1	proform					57:63	the proform	53:63	the proform of eosinophil major basic protein	53:97	Complex of pregnancy-associated plasma protein-A and the proform of eosinophil major basic protein.
12421832	16	45	theme	pro-MBP	2136:2142	arg1	complex					2088:2094	pro-MBP complex	2080:2094	pro-MBP complex	2080:2094	pro-MBP complex, as well as the inhibitory mechanism of pro-MBP.
12421832	16	45	theme	pro-MBP	2136:2142	arg1	mechanism					2123:2131	the inhibitory mechanism	2108:2131	the inhibitory mechanism of pro-MBP	2108:2142	pro-MBP complex, as well as the inhibitory mechanism of pro-MBP.
12421832	6	46	theme	residues	1018:1025	arg1	connectivities					991:1004	the connectivities	987:1004	the connectivities of cysteine residues of the PAPP-A	987:1039	To establish the connectivities of cysteine residues of the PAPP-A.
12421832	4	47	with	similarity	658:667	arg1	proteins					680:687	other proteins	674:687	other proteins	674:687	Except for PAPP-A2, PAPP-A does not share global similarity with other proteins.
12421832	11	48	theme	other	1521:1525	arg1	disulfides					1527:1536	All other disulfides	1517:1536	All other disulfides	1517:1536	All other disulfides are intrachain bridges.
12421832	11	48	theme	other	1521:1525	arg1	bridges					1553:1559	intrachain bridges	1542:1559	intrachain bridges	1542:1559	All other disulfides are intrachain bridges.
12421832	3	49	theme	basic	520:524	arg1	pro-MBP					535:541	pro-MBP	535:541	pro-MBP	535:541	PAPP-A is secreted as a dimer of 400 kDa but circulates in pregnancy as a disulfide-bound 500-kDa 2:2 complex with the proform of eosinophil major basic protein (pro-MBP), recently shown to function as a proteinase inhibitor of PAPP-A.
12421832	3	49	theme	basic	520:524	arg1	protein					526:532	eosinophil major basic protein	503:532	eosinophil major basic protein (pro-MBP)	503:542	PAPP-A is secreted as a dimer of 400 kDa but circulates in pregnancy as a disulfide-bound 500-kDa 2:2 complex with the proform of eosinophil major basic protein (pro-MBP), recently shown to function as a proteinase inhibitor of PAPP-A.
12421832	5	50	theme	SCR	789:791	arg1	modules					793:799	SCR modules	789:799	SCR modules	789:799	Three lin-notch (LNR or LIN-12) modules and five complement control protein modules (also known as SCR modules) have been identified in PAPP-A by sequence similarity with other proteins, but no data are available that allow unambiguous prediction of disulfide bonds of these modules.
12421832	10	51	theme	PAPP-A	1444:1449	arg1	subunit					1451:1457	each PAPP-A subunit	1439:1457	each PAPP-A subunit	1439:1457	Within the 2:2 complex, PAPP-A is dimerized by a single disulfide bond; pro-MBP is dimerized by two disulfides, and each PAPP-A subunit is connected to a pro-MBP subunit by two disulfide bonds.
12421832	3	52	theme	eosinophil	503:512	arg1	pro-MBP					535:541	pro-MBP	535:541	pro-MBP	535:541	PAPP-A is secreted as a dimer of 400 kDa but circulates in pregnancy as a disulfide-bound 500-kDa 2:2 complex with the proform of eosinophil major basic protein (pro-MBP), recently shown to function as a proteinase inhibitor of PAPP-A.
12421832	3	52	theme	eosinophil	503:512	arg1	protein					526:532	eosinophil major basic protein	503:532	eosinophil major basic protein (pro-MBP)	503:542	PAPP-A is secreted as a dimer of 400 kDa but circulates in pregnancy as a disulfide-bound 500-kDa 2:2 complex with the proform of eosinophil major basic protein (pro-MBP), recently shown to function as a proteinase inhibitor of PAPP-A.
12421832	10	53	theme	pro-MBP	1477:1483	arg1	subunit					1485:1491	a pro-MBP subunit	1475:1491	a pro-MBP subunit	1475:1491	Within the 2:2 complex, PAPP-A is dimerized by a single disulfide bond; pro-MBP is dimerized by two disulfides, and each PAPP-A subunit is connected to a pro-MBP subunit by two disulfide bonds.
12421832	2	54	theme	metzincin	201:209	arg1	protein-A					177:185	Pregnancy-associated plasma protein-A	149:185	Pregnancy-associated plasma protein-A (PAPP-A)	149:194	Pregnancy-associated plasma protein-A (PAPP-A) is a metzincin superfamily metalloproteinase responsible for cleavage of insulin-like growth factor-binding protein-4, thus causing release of bound insulin-like growth factor.
12421832	2	54	theme	metzincin	201:209	arg1	metalloproteinase					223:239	a metzincin superfamily metalloproteinase	199:239	a metzincin superfamily metalloproteinase responsible for cleavage of insulin-like growth factor-binding protein-4	199:312	Pregnancy-associated plasma protein-A (PAPP-A) is a metzincin superfamily metalloproteinase responsible for cleavage of insulin-like growth factor-binding protein-4, thus causing release of bound insulin-like growth factor.
12421832	14	55	theme	PAPP-A	1837:1842	arg1	pattern					1826:1832	the disulfide pattern	1812:1832	the disulfide pattern of PAPP-A	1812:1842	pro-MBP complex imposes many restraints on polypeptide folding, and knowledge of the disulfide pattern of PAPP-A will facilitate structural studies based on recombinant expression of individual, putative PAPP-A domains.
12421832	7	56	dep	complex	1049:1055	arg1	biochemical					1058:1068	biochemical	1058:1068	biochemical	1058:1068	pro-MBP complex, biochemical analyses of peptides derived from purified protein were performed.
12421832	7	57	theme	purified	1104:1111	arg1	protein					1113:1119	purified protein	1104:1119	purified protein	1104:1119	pro-MBP complex, biochemical analyses of peptides derived from purified protein were performed.
12421832	10	58	theme	disulfide	1500:1508	arg1	bonds					1510:1514	two disulfide bonds	1496:1514	two disulfide bonds	1496:1514	Within the 2:2 complex, PAPP-A is dimerized by a single disulfide bond; pro-MBP is dimerized by two disulfides, and each PAPP-A subunit is connected to a pro-MBP subunit by two disulfide bonds.
12421832	14	59	theme	individual	1914:1923	arg1	domains					1942:1948	individual, putative PAPP-A domains	1914:1948	domains	1942:1948	pro-MBP complex imposes many restraints on polypeptide folding, and knowledge of the disulfide pattern of PAPP-A will facilitate structural studies based on recombinant expression of individual, putative PAPP-A domains.
12421832	8	60	contain	contains	1156:1163	arg1	subunit					1148:1154	The PAPP-A subunit	1137:1154	The PAPP-A subunit	1137:1154	The PAPP-A subunit contains a total of 82 cysteine residues, of which 81 have been accounted for.
12421832	8	60	contain	contains	1156:1163	arg2	total					1167:1171	a total	1165:1171	a total of 82 cysteine residues, of which 81 have been accounted for	1165:1232	The PAPP-A subunit contains a total of 82 cysteine residues, of which 81 have been accounted for.
12421832	3	61	theme	proteinase	577:586	arg1	inhibitor					588:596	a proteinase inhibitor	575:596	a proteinase inhibitor of PAPP-A	575:606	PAPP-A is secreted as a dimer of 400 kDa but circulates in pregnancy as a disulfide-bound 500-kDa 2:2 complex with the proform of eosinophil major basic protein (pro-MBP), recently shown to function as a proteinase inhibitor of PAPP-A.
12421832	13	62	theme	disulfide	1701:1709	arg1	bonds					1711:1715	disulfide bonds	1701:1715	disulfide bonds of the PAPP-A	1701:1729	The large number of disulfide bonds of the PAPP-A.
12421832	10	63	theme	2:2	1334:1336	arg1	complex					1338:1344	the 2:2 complex	1330:1344	the 2:2 complex	1330:1344	Within the 2:2 complex, PAPP-A is dimerized by a single disulfide bond; pro-MBP is dimerized by two disulfides, and each PAPP-A subunit is connected to a pro-MBP subunit by two disulfide bonds.
12421832	5	64	theme	sequence	836:843	arg1	similarity					845:854	sequence similarity	836:854	sequence similarity with other proteins	836:874	Three lin-notch (LNR or LIN-12) modules and five complement control protein modules (also known as SCR modules) have been identified in PAPP-A by sequence similarity with other proteins, but no data are available that allow unambiguous prediction of disulfide bonds of these modules.
12421832	2	65	theme	Pregnancy-associated	149:168	arg1	metalloproteinase					223:239	a metzincin superfamily metalloproteinase	199:239	a metzincin superfamily metalloproteinase responsible for cleavage of insulin-like growth factor-binding protein-4	199:312	Pregnancy-associated plasma protein-A (PAPP-A) is a metzincin superfamily metalloproteinase responsible for cleavage of insulin-like growth factor-binding protein-4, thus causing release of bound insulin-like growth factor.
12421832	2	65	theme	Pregnancy-associated	149:168	arg1	PAPP-A					188:193	PAPP-A	188:193	PAPP-A	188:193	Pregnancy-associated plasma protein-A (PAPP-A) is a metzincin superfamily metalloproteinase responsible for cleavage of insulin-like growth factor-binding protein-4, thus causing release of bound insulin-like growth factor.
12421832	2	65	theme	Pregnancy-associated	149:168	arg1	protein-A					177:185	Pregnancy-associated plasma protein-A	149:185	Pregnancy-associated plasma protein-A (PAPP-A)	149:194	Pregnancy-associated plasma protein-A (PAPP-A) is a metzincin superfamily metalloproteinase responsible for cleavage of insulin-like growth factor-binding protein-4, thus causing release of bound insulin-like growth factor.
12421832	2	66	theme	factor	365:370	arg1	release					328:334	release	328:334	release of bound insulin-like growth factor	328:370	Pregnancy-associated plasma protein-A (PAPP-A) is a metzincin superfamily metalloproteinase responsible for cleavage of insulin-like growth factor-binding protein-4, thus causing release of bound insulin-like growth factor.
12421832	14	67	theme	disulfide	1816:1824	arg1	pattern					1826:1832	the disulfide pattern	1812:1832	the disulfide pattern of PAPP-A	1812:1842	pro-MBP complex imposes many restraints on polypeptide folding, and knowledge of the disulfide pattern of PAPP-A will facilitate structural studies based on recombinant expression of individual, putative PAPP-A domains.
12421832	5	68	dep	known	780:784	arg1	also					775:778	also	775:778	also	775:778	Three lin-notch (LNR or LIN-12) modules and five complement control protein modules (also known as SCR modules) have been identified in PAPP-A by sequence similarity with other proteins, but no data are available that allow unambiguous prediction of disulfide bonds of these modules.
12421832	4	69	theme	other	674:678	arg1	proteins					680:687	other proteins	674:687	other proteins	674:687	Except for PAPP-A2, PAPP-A does not share global similarity with other proteins.
12421832	7	70	theme	complex	1049:1055	arg1	analyses					1070:1077	pro-MBP complex, biochemical analyses	1041:1077	pro-MBP complex, biochemical analyses of peptides derived from purified protein	1041:1119	pro-MBP complex, biochemical analyses of peptides derived from purified protein were performed.
12421832	2	71	theme	insulin-like	345:356	arg1	factor					365:370	bound insulin-like growth factor	339:370	bound insulin-like growth factor	339:370	Pregnancy-associated plasma protein-A (PAPP-A) is a metzincin superfamily metalloproteinase responsible for cleavage of insulin-like growth factor-binding protein-4, thus causing release of bound insulin-like growth factor.
12421832	15	72	theme	PAPP-A	2073:2078	arg1	formation					2056:2064	the formation	2052:2064	the formation of the PAPP-A	2052:2078	Furthermore, it will allow rational experimental design of functional studies aimed at understanding the formation of the PAPP-A.
12421832	2	73	theme	insulin-like	269:280	arg1	protein-4					304:312	insulin-like growth factor-binding protein-4	269:312	insulin-like growth factor-binding protein-4	269:312	Pregnancy-associated plasma protein-A (PAPP-A) is a metzincin superfamily metalloproteinase responsible for cleavage of insulin-like growth factor-binding protein-4, thus causing release of bound insulin-like growth factor.
12421832	8	74	theme	residues	1188:1195	arg1	total					1167:1171	a total	1165:1171	a total of 82 cysteine residues, of which 81 have been accounted for	1165:1232	The PAPP-A subunit contains a total of 82 cysteine residues, of which 81 have been accounted for.
12421832	5	75	theme	lin-notch	696:704	arg1	modules					722:728	Three lin-notch (LNR or LIN-12) modules	690:728	Three lin-notch (LNR or LIN-12) modules	690:728	Three lin-notch (LNR or LIN-12) modules and five complement control protein modules (also known as SCR modules) have been identified in PAPP-A by sequence similarity with other proteins, but no data are available that allow unambiguous prediction of disulfide bonds of these modules.
12421832	14	76	theme	structural	1860:1869	arg1	studies					1871:1877	structural studies	1860:1877	structural studies based on recombinant expression of individual, putative PAPP-A domains	1860:1948	pro-MBP complex imposes many restraints on polypeptide folding, and knowledge of the disulfide pattern of PAPP-A will facilitate structural studies based on recombinant expression of individual, putative PAPP-A domains.
12421832	6	77	theme	cysteine	1009:1016	arg1	residues					1018:1025	cysteine residues	1009:1025	cysteine residues of the PAPP-A	1009:1039	To establish the connectivities of cysteine residues of the PAPP-A.
12421832	6	77	theme	cysteine	1009:1016	arg1	PAPP-A					1034:1039	the PAPP-A	1030:1039	the PAPP-A	1030:1039	To establish the connectivities of cysteine residues of the PAPP-A.
12421832	15	78	theme	experimental	1987:1998	arg1	design					2000:2005	rational experimental design	1978:2005	rational experimental design of functional studies aimed at understanding the formation of the PAPP-A	1978:2078	Furthermore, it will allow rational experimental design of functional studies aimed at understanding the formation of the PAPP-A.
12421832	5	79	theme	control	750:756	arg1	modules					766:772	five complement control protein modules	734:772	five complement control protein modules (also known as SCR modules)	734:800	Three lin-notch (LNR or LIN-12) modules and five complement control protein modules (also known as SCR modules) have been identified in PAPP-A by sequence similarity with other proteins, but no data are available that allow unambiguous prediction of disulfide bonds of these modules.
12421832	9	80	theme	pro-MBP	1239:1245	arg1	subunit					1247:1253	The pro-MBP subunit	1235:1253	The pro-MBP subunit	1235:1253	The pro-MBP subunit contains 12 cysteine residues, of which 10 have been accounted for.
12421832	2	81	theme	factor-binding	289:302	arg1	protein-4					304:312	insulin-like growth factor-binding protein-4	269:312	insulin-like growth factor-binding protein-4	269:312	Pregnancy-associated plasma protein-A (PAPP-A) is a metzincin superfamily metalloproteinase responsible for cleavage of insulin-like growth factor-binding protein-4, thus causing release of bound insulin-like growth factor.
12421832	14	82	theme	many	1755:1758	arg1	restraints					1760:1769	many restraints	1755:1769	many restraints	1755:1769	pro-MBP complex imposes many restraints on polypeptide folding, and knowledge of the disulfide pattern of PAPP-A will facilitate structural studies based on recombinant expression of individual, putative PAPP-A domains.
12421832	0	83	theme	basic	85:89	arg1	protein					91:97	eosinophil major basic protein	68:97	eosinophil major basic protein	68:97	Complex of pregnancy-associated plasma protein-A and the proform of eosinophil major basic protein.
12421832	9	84	theme	cysteine	1267:1274	arg1	residues					1276:1283	12 cysteine residues	1264:1283	12 cysteine residues	1264:1283	The pro-MBP subunit contains 12 cysteine residues, of which 10 have been accounted for.
12421832	5	85	theme	disulfide	940:948	arg1	bonds					950:954	disulfide bonds	940:954	disulfide bonds of these modules	940:971	Three lin-notch (LNR or LIN-12) modules and five complement control protein modules (also known as SCR modules) have been identified in PAPP-A by sequence similarity with other proteins, but no data are available that allow unambiguous prediction of disulfide bonds of these modules.
12421832	12	86	theme	N-linked	1606:1613	arg1	substitution					1628:1639	N-linked carbohydrate substitution	1606:1639	N-linked carbohydrate substitution of the PAPP-A subunit	1606:1661	We also show that of 13 potential sites for N-linked carbohydrate substitution of the PAPP-A subunit, 11 are occupied.
12421832	10	87	theme	single	1372:1377	arg1	bond					1389:1392	a single disulfide bond	1370:1392	a single disulfide bond	1370:1392	Within the 2:2 complex, PAPP-A is dimerized by a single disulfide bond; pro-MBP is dimerized by two disulfides, and each PAPP-A subunit is connected to a pro-MBP subunit by two disulfide bonds.
12421832	14	88	theme	PAPP-A	1935:1940	arg1	domains					1942:1948	individual, putative PAPP-A domains	1914:1948	domains	1942:1948	pro-MBP complex imposes many restraints on polypeptide folding, and knowledge of the disulfide pattern of PAPP-A will facilitate structural studies based on recombinant expression of individual, putative PAPP-A domains.
12421832	9	89	contain	contains	1255:1262	arg1	subunit					1247:1253	The pro-MBP subunit	1235:1253	The pro-MBP subunit	1235:1253	The pro-MBP subunit contains 12 cysteine residues, of which 10 have been accounted for.
12421832	9	89	contain	contains	1255:1262	arg2	residues					1276:1283	12 cysteine residues	1264:1283	12 cysteine residues	1264:1283	The pro-MBP subunit contains 12 cysteine residues, of which 10 have been accounted for.
12421832	3	90	theme	500-kDa	463:469	arg1	complex					475:481	a disulfide-bound 500-kDa 2:2 complex	445:481	a disulfide-bound 500-kDa 2:2 complex with the proform of eosinophil major basic protein (pro-MBP), recently shown to function as a proteinase inhibitor of PAPP-A	445:606	PAPP-A is secreted as a dimer of 400 kDa but circulates in pregnancy as a disulfide-bound 500-kDa 2:2 complex with the proform of eosinophil major basic protein (pro-MBP), recently shown to function as a proteinase inhibitor of PAPP-A.
12421832	0	91	theme	plasma	32:37	arg1	protein-A					39:47	pregnancy-associated plasma protein-A	11:47	pregnancy-associated plasma protein-A	11:47	Complex of pregnancy-associated plasma protein-A and the proform of eosinophil major basic protein.
12421832	1	92	theme	Disulfide	100:108	arg1	structure					110:118	Disulfide structure	100:118	Disulfide structure	100:118	Disulfide structure and carbohydrate attachment.
12421832	6	93	theme	PAPP-A	1034:1039	arg1	residues					1018:1025	cysteine residues	1009:1025	cysteine residues of the PAPP-A	1009:1039	To establish the connectivities of cysteine residues of the PAPP-A.
12421832	6	93	theme	PAPP-A	1034:1039	arg1	PAPP-A					1034:1039	the PAPP-A	1030:1039	the PAPP-A	1030:1039	To establish the connectivities of cysteine residues of the PAPP-A.
12421832	3	94	theme	kDa	410:412	arg1	dimer					397:401	a dimer	395:401	a dimer of 400 kDa	395:412	PAPP-A is secreted as a dimer of 400 kDa but circulates in pregnancy as a disulfide-bound 500-kDa 2:2 complex with the proform of eosinophil major basic protein (pro-MBP), recently shown to function as a proteinase inhibitor of PAPP-A.
12421832	3	94	theme	kDa	410:412	arg1	PAPP-A					373:378	PAPP-A	373:378	PAPP-A	373:378	PAPP-A is secreted as a dimer of 400 kDa but circulates in pregnancy as a disulfide-bound 500-kDa 2:2 complex with the proform of eosinophil major basic protein (pro-MBP), recently shown to function as a proteinase inhibitor of PAPP-A.
12421832	14	95	theme	recombinant	1888:1898	arg1	expression					1900:1909	recombinant expression	1888:1909	recombinant expression of individual, putative PAPP-A domains	1888:1948	pro-MBP complex imposes many restraints on polypeptide folding, and knowledge of the disulfide pattern of PAPP-A will facilitate structural studies based on recombinant expression of individual, putative PAPP-A domains.
12421832	16	96	theme	inhibitory	2112:2121	arg1	mechanism					2123:2131	the inhibitory mechanism	2108:2131	the inhibitory mechanism of pro-MBP	2108:2142	pro-MBP complex, as well as the inhibitory mechanism of pro-MBP.
12421832	2	97	theme	responsible	241:251	arg1	protein-A					177:185	Pregnancy-associated plasma protein-A	149:185	Pregnancy-associated plasma protein-A (PAPP-A)	149:194	Pregnancy-associated plasma protein-A (PAPP-A) is a metzincin superfamily metalloproteinase responsible for cleavage of insulin-like growth factor-binding protein-4, thus causing release of bound insulin-like growth factor.
12421832	2	97	theme	responsible	241:251	arg1	metalloproteinase					223:239	a metzincin superfamily metalloproteinase	199:239	a metzincin superfamily metalloproteinase responsible for cleavage of insulin-like growth factor-binding protein-4	199:312	Pregnancy-associated plasma protein-A (PAPP-A) is a metzincin superfamily metalloproteinase responsible for cleavage of insulin-like growth factor-binding protein-4, thus causing release of bound insulin-like growth factor.
12421832	3	98	theme	protein	526:532	arg1	proform					492:498	the proform	488:498	the proform of eosinophil major basic protein (pro-MBP), recently shown to function as a proteinase inhibitor of PAPP-A	488:606	PAPP-A is secreted as a dimer of 400 kDa but circulates in pregnancy as a disulfide-bound 500-kDa 2:2 complex with the proform of eosinophil major basic protein (pro-MBP), recently shown to function as a proteinase inhibitor of PAPP-A.
12421832	15	99	theme	functional	2010:2019	arg1	studies					2021:2027	functional studies	2010:2027	functional studies aimed at understanding the formation of the PAPP-A	2010:2078	Furthermore, it will allow rational experimental design of functional studies aimed at understanding the formation of the PAPP-A.
12421832	5	100	theme	modules	965:971	arg1	bonds					950:954	disulfide bonds	940:954	disulfide bonds of these modules	940:971	Three lin-notch (LNR or LIN-12) modules and five complement control protein modules (also known as SCR modules) have been identified in PAPP-A by sequence similarity with other proteins, but no data are available that allow unambiguous prediction of disulfide bonds of these modules.
12421832	5	101	with	similarity	845:854	arg1	proteins					867:874	other proteins	861:874	other proteins	861:874	Three lin-notch (LNR or LIN-12) modules and five complement control protein modules (also known as SCR modules) have been identified in PAPP-A by sequence similarity with other proteins, but no data are available that allow unambiguous prediction of disulfide bonds of these modules.
12421832	2	102	theme	superfamily	211:221	arg1	protein-A					177:185	Pregnancy-associated plasma protein-A	149:185	Pregnancy-associated plasma protein-A (PAPP-A)	149:194	Pregnancy-associated plasma protein-A (PAPP-A) is a metzincin superfamily metalloproteinase responsible for cleavage of insulin-like growth factor-binding protein-4, thus causing release of bound insulin-like growth factor.
12421832	2	102	theme	superfamily	211:221	arg1	metalloproteinase					223:239	a metzincin superfamily metalloproteinase	199:239	a metzincin superfamily metalloproteinase responsible for cleavage of insulin-like growth factor-binding protein-4	199:312	Pregnancy-associated plasma protein-A (PAPP-A) is a metzincin superfamily metalloproteinase responsible for cleavage of insulin-like growth factor-binding protein-4, thus causing release of bound insulin-like growth factor.
12421832	11	103	theme	intrachain	1542:1551	arg1	disulfides					1527:1536	All other disulfides	1517:1536	All other disulfides	1517:1536	All other disulfides are intrachain bridges.
12421832	11	103	theme	intrachain	1542:1551	arg1	bridges					1553:1559	intrachain bridges	1542:1559	intrachain bridges	1542:1559	All other disulfides are intrachain bridges.
12421832	3	104	theme	major	514:518	arg1	pro-MBP					535:541	pro-MBP	535:541	pro-MBP	535:541	PAPP-A is secreted as a dimer of 400 kDa but circulates in pregnancy as a disulfide-bound 500-kDa 2:2 complex with the proform of eosinophil major basic protein (pro-MBP), recently shown to function as a proteinase inhibitor of PAPP-A.
12421832	3	104	theme	major	514:518	arg1	protein					526:532	eosinophil major basic protein	503:532	eosinophil major basic protein (pro-MBP)	503:542	PAPP-A is secreted as a dimer of 400 kDa but circulates in pregnancy as a disulfide-bound 500-kDa 2:2 complex with the proform of eosinophil major basic protein (pro-MBP), recently shown to function as a proteinase inhibitor of PAPP-A.
12421832	15	105	theme	studies	2021:2027	arg1	design					2000:2005	rational experimental design	1978:2005	rational experimental design of functional studies aimed at understanding the formation of the PAPP-A	1978:2078	Furthermore, it will allow rational experimental design of functional studies aimed at understanding the formation of the PAPP-A.
3839598	7	0	theme	kidney	1144:1149	arg1	tissue					1151:1156	human kidney tissue	1138:1156	human kidney tissue	1138:1156	Messenger RNA species homologous to HepG2 glucose transporter messenger RNA were detected in K562 leukemic cells, HT29 colon adenocarcinoma cells, and human kidney tissue.
3839598	7	1	theme	HT29	1101:1104	arg1	cells					1127:1131	HT29 colon adenocarcinoma cells	1101:1131	HT29 colon adenocarcinoma cells	1101:1131	Messenger RNA species homologous to HepG2 glucose transporter messenger RNA were detected in K562 leukemic cells, HT29 colon adenocarcinoma cells, and human kidney tissue.
3839598	5	2	theme	amide	717:721	arg1	chains					728:733	abundant hydroxyl and amide side chains	695:733	chains	728:733	Several of these may form amphipathic alpha helices and contain abundant hydroxyl and amide side chains that could participate in glucose binding or line a transmembrane pore through which the sugar moves.
3839598	5	3	theme	amphipathic	657:667	arg1	helices					675:681	amphipathic alpha helices	657:681	amphipathic alpha helices	657:681	Several of these may form amphipathic alpha helices and contain abundant hydroxyl and amide side chains that could participate in glucose binding or line a transmembrane pore through which the sugar moves.
3839598	1	4	from	cells	138:142	arg1	protein					104:110	the glucose transport protein	82:110	the glucose transport protein from human HepG2 hepatoma cells	82:142	The amino acid sequence of the glucose transport protein from human HepG2 hepatoma cells was deduced from analysis of a complementary DNA clone.
3839598	1	4	from	cells	138:142	arg1	sequence					70:77	The amino acid sequence	55:77	The amino acid sequence of the glucose transport protein from human HepG2 hepatoma cells	55:142	The amino acid sequence of the glucose transport protein from human HepG2 hepatoma cells was deduced from analysis of a complementary DNA clone.
3839598	6	5	theme	cytoplasmic	969:979	arg1	face					981:984	the cytoplasmic face	965:984	the cytoplasmic face	965:984	The amino terminus, carboxyl terminus, and a highly hydrophilic domain in the center of the protein are all predicted to lie on the cytoplasmic face.
3839598	5	6	theme	alpha	669:673	arg1	helices					675:681	amphipathic alpha helices	657:681	amphipathic alpha helices	657:681	Several of these may form amphipathic alpha helices and contain abundant hydroxyl and amide side chains that could participate in glucose binding or line a transmembrane pore through which the sugar moves.
3839598	3	7	theme	cleavable	500:508	arg1	sequence					532:539	a cleavable amino-terminal signal sequence	498:539	a cleavable amino-terminal signal sequence	498:539	The protein lacks a cleavable amino-terminal signal sequence.
3839598	2	8	theme	fast	277:280	arg1	bombardment					287:297	fast atom bombardment mapping	277:305	fast atom bombardment mapping	277:305	Structural analysis of the purified human erythrocyte glucose transporter by fast atom bombardment mapping and gas phase Edman degradation confirmed the identity of the clone and demonstrated that the HepG2 and erythrocyte transporters are highly homologous and may be identical.
3839598	1	9	theme	glucose	86:92	arg1	protein					104:110	the glucose transport protein	82:110	the glucose transport protein from human HepG2 hepatoma cells	82:142	The amino acid sequence of the glucose transport protein from human HepG2 hepatoma cells was deduced from analysis of a complementary DNA clone.
3839598	6	10	theme	hydrophilic	889:899	arg1	domain					901:906	a highly hydrophilic domain	880:906	a highly hydrophilic domain in the center of the protein	880:935	The amino terminus, carboxyl terminus, and a highly hydrophilic domain in the center of the protein are all predicted to lie on the cytoplasmic face.
3839598	2	11	theme	gas	311:313	arg1	degradation					327:337	gas phase Edman degradation	311:337	gas phase Edman degradation	311:337	Structural analysis of the purified human erythrocyte glucose transporter by fast atom bombardment mapping and gas phase Edman degradation confirmed the identity of the clone and demonstrated that the HepG2 and erythrocyte transporters are highly homologous and may be identical.
3839598	7	12	theme	K562	1080:1083	arg1	cells					1094:1098	K562 leukemic cells	1080:1098	K562 leukemic cells	1080:1098	Messenger RNA species homologous to HepG2 glucose transporter messenger RNA were detected in K562 leukemic cells, HT29 colon adenocarcinoma cells, and human kidney tissue.
3839598	2	13	theme	HepG2	401:405	arg1	identical					469:477	identical	469:477	identical	469:477	Structural analysis of the purified human erythrocyte glucose transporter by fast atom bombardment mapping and gas phase Edman degradation confirmed the identity of the clone and demonstrated that the HepG2 and erythrocyte transporters are highly homologous and may be identical.
3839598	2	13	theme	HepG2	401:405	arg1	transporters					423:434	the HepG2 and erythrocyte transporters	397:434	transporters	423:434	Structural analysis of the purified human erythrocyte glucose transporter by fast atom bombardment mapping and gas phase Edman degradation confirmed the identity of the clone and demonstrated that the HepG2 and erythrocyte transporters are highly homologous and may be identical.
3839598	2	13	theme	HepG2	401:405	arg1	homologous					447:456	homologous	447:456	homologous	447:456	Structural analysis of the purified human erythrocyte glucose transporter by fast atom bombardment mapping and gas phase Edman degradation confirmed the identity of the clone and demonstrated that the HepG2 and erythrocyte transporters are highly homologous and may be identical.
3839598	1	14	theme	amino	59:63	arg1	sequence					70:77	The amino acid sequence	55:77	The amino acid sequence of the glucose transport protein from human HepG2 hepatoma cells	55:142	The amino acid sequence of the glucose transport protein from human HepG2 hepatoma cells was deduced from analysis of a complementary DNA clone.
3839598	7	15	theme	adenocarcinoma	1112:1125	arg1	cells					1127:1131	HT29 colon adenocarcinoma cells	1101:1131	HT29 colon adenocarcinoma cells	1101:1131	Messenger RNA species homologous to HepG2 glucose transporter messenger RNA were detected in K562 leukemic cells, HT29 colon adenocarcinoma cells, and human kidney tissue.
3839598	7	16	theme	leukemic	1085:1092	arg1	cells					1094:1098	K562 leukemic cells	1080:1098	K562 leukemic cells	1080:1098	Messenger RNA species homologous to HepG2 glucose transporter messenger RNA were detected in K562 leukemic cells, HT29 colon adenocarcinoma cells, and human kidney tissue.
3839598	1	17	theme	acid	65:68	arg1	sequence					70:77	The amino acid sequence	55:77	The amino acid sequence of the glucose transport protein from human HepG2 hepatoma cells	55:142	The amino acid sequence of the glucose transport protein from human HepG2 hepatoma cells was deduced from analysis of a complementary DNA clone.
3839598	3	18	theme	amino-terminal	510:523	arg1	sequence					532:539	a cleavable amino-terminal signal sequence	498:539	a cleavable amino-terminal signal sequence	498:539	The protein lacks a cleavable amino-terminal signal sequence.
3839598	5	19	theme	these	642:646	arg1	Several					631:637	Several	631:637	Several	631:637	Several of these may form amphipathic alpha helices and contain abundant hydroxyl and amide side chains that could participate in glucose binding or line a transmembrane pore through which the sugar moves.
3839598	3	20	theme	signal	525:530	arg1	sequence					532:539	a cleavable amino-terminal signal sequence	498:539	a cleavable amino-terminal signal sequence	498:539	The protein lacks a cleavable amino-terminal signal sequence.
3839598	2	21	theme	clone	369:373	arg1	identity					353:360	the identity	349:360	the identity of the clone	349:373	Structural analysis of the purified human erythrocyte glucose transporter by fast atom bombardment mapping and gas phase Edman degradation confirmed the identity of the clone and demonstrated that the HepG2 and erythrocyte transporters are highly homologous and may be identical.
3839598	7	22	theme	transporter	1037:1047	arg1	RNA					1059:1061	HepG2 glucose transporter messenger RNA	1023:1061	HepG2 glucose transporter messenger RNA	1023:1061	Messenger RNA species homologous to HepG2 glucose transporter messenger RNA were detected in K562 leukemic cells, HT29 colon adenocarcinoma cells, and human kidney tissue.
3839598	2	23	theme	mapping	299:305	arg1	bombardment					287:297	fast atom bombardment mapping	277:305	fast atom bombardment mapping	277:305	Structural analysis of the purified human erythrocyte glucose transporter by fast atom bombardment mapping and gas phase Edman degradation confirmed the identity of the clone and demonstrated that the HepG2 and erythrocyte transporters are highly homologous and may be identical.
3839598	7	24	theme	colon	1106:1110	arg1	cells					1127:1131	HT29 colon adenocarcinoma cells	1101:1131	HT29 colon adenocarcinoma cells	1101:1131	Messenger RNA species homologous to HepG2 glucose transporter messenger RNA were detected in K562 leukemic cells, HT29 colon adenocarcinoma cells, and human kidney tissue.
3839598	7	25	theme	human	1138:1142	arg1	tissue					1151:1156	human kidney tissue	1138:1156	human kidney tissue	1138:1156	Messenger RNA species homologous to HepG2 glucose transporter messenger RNA were detected in K562 leukemic cells, HT29 colon adenocarcinoma cells, and human kidney tissue.
3839598	4	26	theme	primary	558:564	arg1	structure					566:574	the primary structure	554:574	the primary structure	554:574	Analysis of the primary structure suggests the presence of 12 membrane-spanning domains.
3839598	2	27	theme	erythrocyte	411:421	arg1	identical					469:477	identical	469:477	identical	469:477	Structural analysis of the purified human erythrocyte glucose transporter by fast atom bombardment mapping and gas phase Edman degradation confirmed the identity of the clone and demonstrated that the HepG2 and erythrocyte transporters are highly homologous and may be identical.
3839598	2	27	theme	erythrocyte	411:421	arg1	transporters					423:434	the HepG2 and erythrocyte transporters	397:434	transporters	423:434	Structural analysis of the purified human erythrocyte glucose transporter by fast atom bombardment mapping and gas phase Edman degradation confirmed the identity of the clone and demonstrated that the HepG2 and erythrocyte transporters are highly homologous and may be identical.
3839598	2	27	theme	erythrocyte	411:421	arg1	homologous					447:456	homologous	447:456	homologous	447:456	Structural analysis of the purified human erythrocyte glucose transporter by fast atom bombardment mapping and gas phase Edman degradation confirmed the identity of the clone and demonstrated that the HepG2 and erythrocyte transporters are highly homologous and may be identical.
3839598	4	28	theme	structure	566:574	arg1	Analysis					542:549	Analysis	542:549	Analysis of the primary structure	542:574	Analysis of the primary structure suggests the presence of 12 membrane-spanning domains.
3839598	2	29	theme	transporter	262:272	arg1	analysis					211:218	Structural analysis	200:218	Structural analysis of the purified human erythrocyte glucose transporter by fast atom bombardment mapping and gas phase Edman degradation	200:337	Structural analysis of the purified human erythrocyte glucose transporter by fast atom bombardment mapping and gas phase Edman degradation confirmed the identity of the clone and demonstrated that the HepG2 and erythrocyte transporters are highly homologous and may be identical.
3839598	2	30	theme	atom	282:285	arg1	bombardment					287:297	fast atom bombardment mapping	277:305	fast atom bombardment mapping	277:305	Structural analysis of the purified human erythrocyte glucose transporter by fast atom bombardment mapping and gas phase Edman degradation confirmed the identity of the clone and demonstrated that the HepG2 and erythrocyte transporters are highly homologous and may be identical.
3839598	1	31	theme	complementary	175:187	arg1	clone					193:197	a complementary DNA clone	173:197	a complementary DNA clone	173:197	The amino acid sequence of the glucose transport protein from human HepG2 hepatoma cells was deduced from analysis of a complementary DNA clone.
3839598	0	32	theme	human	28:32	arg1	transporter					42:52	a human glucose transporter	26:52	a human glucose transporter	26:52	Sequence and structure of a human glucose transporter.
3839598	2	33	theme	Edman	321:325	arg1	degradation					327:337	gas phase Edman degradation	311:337	gas phase Edman degradation	311:337	Structural analysis of the purified human erythrocyte glucose transporter by fast atom bombardment mapping and gas phase Edman degradation confirmed the identity of the clone and demonstrated that the HepG2 and erythrocyte transporters are highly homologous and may be identical.
3839598	5	34	theme	side	723:726	arg1	chains					728:733	abundant hydroxyl and amide side chains	695:733	chains	728:733	Several of these may form amphipathic alpha helices and contain abundant hydroxyl and amide side chains that could participate in glucose binding or line a transmembrane pore through which the sugar moves.
3839598	1	35	theme	DNA	189:191	arg1	clone					193:197	a complementary DNA clone	173:197	a complementary DNA clone	173:197	The amino acid sequence of the glucose transport protein from human HepG2 hepatoma cells was deduced from analysis of a complementary DNA clone.
3839598	5	36	theme	transmembrane	787:799	arg1	pore					801:804	a transmembrane pore	785:804	a transmembrane pore through which the sugar moves	785:834	Several of these may form amphipathic alpha helices and contain abundant hydroxyl and amide side chains that could participate in glucose binding or line a transmembrane pore through which the sugar moves.
3839598	7	37	theme	messenger	1049:1057	arg1	RNA					1059:1061	HepG2 glucose transporter messenger RNA	1023:1061	HepG2 glucose transporter messenger RNA	1023:1061	Messenger RNA species homologous to HepG2 glucose transporter messenger RNA were detected in K562 leukemic cells, HT29 colon adenocarcinoma cells, and human kidney tissue.
3839598	6	38	theme	carboxyl	857:864	arg1	terminus					866:873	carboxyl terminus	857:873	carboxyl terminus	857:873	The amino terminus, carboxyl terminus, and a highly hydrophilic domain in the center of the protein are all predicted to lie on the cytoplasmic face.
3839598	7	39	theme	RNA	997:999	arg1	species					1001:1007	Messenger RNA species	987:1007	Messenger RNA species homologous to HepG2 glucose transporter messenger RNA	987:1061	Messenger RNA species homologous to HepG2 glucose transporter messenger RNA were detected in K562 leukemic cells, HT29 colon adenocarcinoma cells, and human kidney tissue.
3839598	1	40	theme	clone	193:197	arg1	analysis					161:168	analysis	161:168	analysis of a complementary DNA clone	161:197	The amino acid sequence of the glucose transport protein from human HepG2 hepatoma cells was deduced from analysis of a complementary DNA clone.
3839598	0	41	theme	transporter	42:52	arg1	structure					13:21	structure	13:21	structure	13:21	Sequence and structure of a human glucose transporter.
3839598	0	41	theme	transporter	42:52	arg1	Sequence					0:7	Sequence	0:7	Sequence	0:7	Sequence and structure of a human glucose transporter.
3839598	6	42	theme	protein	929:935	arg1	center					915:920	the center	911:920	the center of the protein	911:935	The amino terminus, carboxyl terminus, and a highly hydrophilic domain in the center of the protein are all predicted to lie on the cytoplasmic face.
3839598	7	43	theme	HepG2	1023:1027	arg1	RNA					1059:1061	HepG2 glucose transporter messenger RNA	1023:1061	HepG2 glucose transporter messenger RNA	1023:1061	Messenger RNA species homologous to HepG2 glucose transporter messenger RNA were detected in K562 leukemic cells, HT29 colon adenocarcinoma cells, and human kidney tissue.
3839598	6	44	from	domain	901:906	arg1	center					915:920	the center	911:920	the center of the protein	911:935	The amino terminus, carboxyl terminus, and a highly hydrophilic domain in the center of the protein are all predicted to lie on the cytoplasmic face.
3839598	2	45	theme	Structural	200:209	arg1	analysis					211:218	Structural analysis	200:218	Structural analysis of the purified human erythrocyte glucose transporter by fast atom bombardment mapping and gas phase Edman degradation	200:337	Structural analysis of the purified human erythrocyte glucose transporter by fast atom bombardment mapping and gas phase Edman degradation confirmed the identity of the clone and demonstrated that the HepG2 and erythrocyte transporters are highly homologous and may be identical.
3839598	7	46	theme	homologous	1009:1018	arg1	species					1001:1007	Messenger RNA species	987:1007	Messenger RNA species homologous to HepG2 glucose transporter messenger RNA	987:1061	Messenger RNA species homologous to HepG2 glucose transporter messenger RNA were detected in K562 leukemic cells, HT29 colon adenocarcinoma cells, and human kidney tissue.
3839598	1	47	theme	transport	94:102	arg1	protein					104:110	the glucose transport protein	82:110	the glucose transport protein from human HepG2 hepatoma cells	82:142	The amino acid sequence of the glucose transport protein from human HepG2 hepatoma cells was deduced from analysis of a complementary DNA clone.
3839598	0	48	theme	glucose	34:40	arg1	transporter					42:52	a human glucose transporter	26:52	a human glucose transporter	26:52	Sequence and structure of a human glucose transporter.
3839598	5	49	contain	contain	687:693	arg2	chains					728:733	abundant hydroxyl and amide side chains	695:733	chains	728:733	Several of these may form amphipathic alpha helices and contain abundant hydroxyl and amide side chains that could participate in glucose binding or line a transmembrane pore through which the sugar moves.
3839598	5	49	contain	contain	687:693	arg1	Several					631:637	Several	631:637	Several	631:637	Several of these may form amphipathic alpha helices and contain abundant hydroxyl and amide side chains that could participate in glucose binding or line a transmembrane pore through which the sugar moves.
3839598	5	49	contain	contain	687:693	arg2	hydroxyl					704:711	abundant hydroxyl and amide side chains	695:733	hydroxyl	704:711	Several of these may form amphipathic alpha helices and contain abundant hydroxyl and amide side chains that could participate in glucose binding or line a transmembrane pore through which the sugar moves.
3839598	7	50	theme	glucose	1029:1035	arg1	RNA					1059:1061	HepG2 glucose transporter messenger RNA	1023:1061	HepG2 glucose transporter messenger RNA	1023:1061	Messenger RNA species homologous to HepG2 glucose transporter messenger RNA were detected in K562 leukemic cells, HT29 colon adenocarcinoma cells, and human kidney tissue.
3839598	1	51	theme	protein	104:110	arg1	sequence					70:77	The amino acid sequence	55:77	The amino acid sequence of the glucose transport protein from human HepG2 hepatoma cells	55:142	The amino acid sequence of the glucose transport protein from human HepG2 hepatoma cells was deduced from analysis of a complementary DNA clone.
3839598	5	52	theme	abundant	695:702	arg1	hydroxyl					704:711	abundant hydroxyl and amide side chains	695:733	hydroxyl	704:711	Several of these may form amphipathic alpha helices and contain abundant hydroxyl and amide side chains that could participate in glucose binding or line a transmembrane pore through which the sugar moves.
3839598	6	53	theme	amino	841:845	arg1	terminus					847:854	The amino terminus	837:854	The amino terminus	837:854	The amino terminus, carboxyl terminus, and a highly hydrophilic domain in the center of the protein are all predicted to lie on the cytoplasmic face.
3839598	2	54	theme	erythrocyte	242:252	arg1	transporter					262:272	the purified human erythrocyte glucose transporter	223:272	the purified human erythrocyte glucose transporter	223:272	Structural analysis of the purified human erythrocyte glucose transporter by fast atom bombardment mapping and gas phase Edman degradation confirmed the identity of the clone and demonstrated that the HepG2 and erythrocyte transporters are highly homologous and may be identical.
3839598	7	55	theme	Messenger	987:995	arg1	species					1001:1007	Messenger RNA species	987:1007	Messenger RNA species homologous to HepG2 glucose transporter messenger RNA	987:1061	Messenger RNA species homologous to HepG2 glucose transporter messenger RNA were detected in K562 leukemic cells, HT29 colon adenocarcinoma cells, and human kidney tissue.
3839598	2	56	theme	phase	315:319	arg1	degradation					327:337	gas phase Edman degradation	311:337	gas phase Edman degradation	311:337	Structural analysis of the purified human erythrocyte glucose transporter by fast atom bombardment mapping and gas phase Edman degradation confirmed the identity of the clone and demonstrated that the HepG2 and erythrocyte transporters are highly homologous and may be identical.
3839598	4	57	theme	membrane-spanning	604:620	arg1	domains					622:628	12 membrane-spanning domains	601:628	12 membrane-spanning domains	601:628	Analysis of the primary structure suggests the presence of 12 membrane-spanning domains.
3839598	2	58	theme	glucose	254:260	arg1	transporter					262:272	the purified human erythrocyte glucose transporter	223:272	the purified human erythrocyte glucose transporter	223:272	Structural analysis of the purified human erythrocyte glucose transporter by fast atom bombardment mapping and gas phase Edman degradation confirmed the identity of the clone and demonstrated that the HepG2 and erythrocyte transporters are highly homologous and may be identical.
3839598	2	59	theme	human	236:240	arg1	transporter					262:272	the purified human erythrocyte glucose transporter	223:272	the purified human erythrocyte glucose transporter	223:272	Structural analysis of the purified human erythrocyte glucose transporter by fast atom bombardment mapping and gas phase Edman degradation confirmed the identity of the clone and demonstrated that the HepG2 and erythrocyte transporters are highly homologous and may be identical.
3839598	1	60	theme	human	117:121	arg1	cells					138:142	human HepG2 hepatoma cells	117:142	human HepG2 hepatoma cells	117:142	The amino acid sequence of the glucose transport protein from human HepG2 hepatoma cells was deduced from analysis of a complementary DNA clone.
3839598	1	61	from	sequence	70:77	arg1	cells					138:142	human HepG2 hepatoma cells	117:142	human HepG2 hepatoma cells	117:142	The amino acid sequence of the glucose transport protein from human HepG2 hepatoma cells was deduced from analysis of a complementary DNA clone.
3839598	5	62	theme	glucose	761:767	arg1	binding					769:775	glucose binding	761:775	glucose binding	761:775	Several of these may form amphipathic alpha helices and contain abundant hydroxyl and amide side chains that could participate in glucose binding or line a transmembrane pore through which the sugar moves.
3839598	2	63	theme	purified	227:234	arg1	transporter					262:272	the purified human erythrocyte glucose transporter	223:272	the purified human erythrocyte glucose transporter	223:272	Structural analysis of the purified human erythrocyte glucose transporter by fast atom bombardment mapping and gas phase Edman degradation confirmed the identity of the clone and demonstrated that the HepG2 and erythrocyte transporters are highly homologous and may be identical.
3839598	1	64	theme	HepG2	123:127	arg1	cells					138:142	human HepG2 hepatoma cells	117:142	human HepG2 hepatoma cells	117:142	The amino acid sequence of the glucose transport protein from human HepG2 hepatoma cells was deduced from analysis of a complementary DNA clone.
3839598	7	65	located	detected	1068:1075	arg2	species					1001:1007	Messenger RNA species	987:1007	Messenger RNA species homologous to HepG2 glucose transporter messenger RNA	987:1061	Messenger RNA species homologous to HepG2 glucose transporter messenger RNA were detected in K562 leukemic cells, HT29 colon adenocarcinoma cells, and human kidney tissue.
3839598	7	65	located	detected	1068:1075	arg1	tissue					1151:1156	human kidney tissue	1138:1156	human kidney tissue	1138:1156	Messenger RNA species homologous to HepG2 glucose transporter messenger RNA were detected in K562 leukemic cells, HT29 colon adenocarcinoma cells, and human kidney tissue.
3839598	7	65	located	detected	1068:1075	arg1	cells					1127:1131	HT29 colon adenocarcinoma cells	1101:1131	HT29 colon adenocarcinoma cells	1101:1131	Messenger RNA species homologous to HepG2 glucose transporter messenger RNA were detected in K562 leukemic cells, HT29 colon adenocarcinoma cells, and human kidney tissue.
3839598	7	65	located	detected	1068:1075	arg1	cells					1094:1098	K562 leukemic cells	1080:1098	K562 leukemic cells	1080:1098	Messenger RNA species homologous to HepG2 glucose transporter messenger RNA were detected in K562 leukemic cells, HT29 colon adenocarcinoma cells, and human kidney tissue.
3839598	6	66	from	terminus	847:854	arg1	center					915:920	the center	911:920	the center of the protein	911:935	The amino terminus, carboxyl terminus, and a highly hydrophilic domain in the center of the protein are all predicted to lie on the cytoplasmic face.
3839598	6	67	from	terminus	866:873	arg1	center					915:920	the center	911:920	the center of the protein	911:935	The amino terminus, carboxyl terminus, and a highly hydrophilic domain in the center of the protein are all predicted to lie on the cytoplasmic face.
3839598	1	68	theme	hepatoma	129:136	arg1	cells					138:142	human HepG2 hepatoma cells	117:142	human HepG2 hepatoma cells	117:142	The amino acid sequence of the glucose transport protein from human HepG2 hepatoma cells was deduced from analysis of a complementary DNA clone.
3839598	4	69	theme	domains	622:628	arg1	presence					589:596	the presence	585:596	the presence of 12 membrane-spanning domains	585:628	Analysis of the primary structure suggests the presence of 12 membrane-spanning domains.
21677192	1	0	theme	cell	354:357	arg1	biosynthesis					364:375	cell wall biosynthesis	354:375	cell wall biosynthesis	354:375	Tunicamycin (TM) inhibits eukaryotic asparagine-linked glycosylation, protein palmitoylation, ganglioside production, proteoglycan synthesis, 3-hydroxy-3-methylglutaryl coenzyme-A reductase activity, and cell wall biosynthesis in bacteria.
21677192	1	1	from	activity	340:347	arg1	bacteria					380:387	bacteria	380:387	bacteria	380:387	Tunicamycin (TM) inhibits eukaryotic asparagine-linked glycosylation, protein palmitoylation, ganglioside production, proteoglycan synthesis, 3-hydroxy-3-methylglutaryl coenzyme-A reductase activity, and cell wall biosynthesis in bacteria.
21677192	0	2	contain	containing	65:74	arg1	mediator					109:116	a key mediator	103:116	a key mediator in the response to tunicamycin	103:147	A haploid genetic screen identifies the major facilitator domain containing 2A (MFSD2A) transporter as a key mediator in the response to tunicamycin.
21677192	0	2	contain	containing	65:74	arg1	domain					58:63	the major facilitator domain	36:63	the major facilitator domain containing 2A (MFSD2A) transporter	36:98	A haploid genetic screen identifies the major facilitator domain containing 2A (MFSD2A) transporter as a key mediator in the response to tunicamycin.
21677192	0	2	contain	containing	65:74	arg2	transporter					88:98	2A (MFSD2A) transporter	76:98	2A (MFSD2A) transporter	76:98	A haploid genetic screen identifies the major facilitator domain containing 2A (MFSD2A) transporter as a key mediator in the response to tunicamycin.
21677192	4	3	theme	facilitator	700:710	arg1	MFSD2A					734:739	MFSD2A	734:739	MFSD2A	734:739	Here, we identify in an unbiased genetic screen a transporter of the major facilitator superfamily, major facilitator domain containing 2A (MFSD2A), as a critical mediator of TM toxicity.
21677192	4	3	theme	facilitator	700:710	arg1	2A					730:731	major facilitator domain containing 2A	694:731	major facilitator domain containing 2A (MFSD2A)	694:740	Here, we identify in an unbiased genetic screen a transporter of the major facilitator superfamily, major facilitator domain containing 2A (MFSD2A), as a critical mediator of TM toxicity.
21677192	4	3	theme	facilitator	700:710	arg1	superfamily					681:691	the major facilitator superfamily	659:691	the major facilitator superfamily	659:691	Here, we identify in an unbiased genetic screen a transporter of the major facilitator superfamily, major facilitator domain containing 2A (MFSD2A), as a critical mediator of TM toxicity.
21677192	0	4	theme	2A	76:77	arg1	transporter					88:98	2A (MFSD2A) transporter	76:98	2A (MFSD2A) transporter	76:98	A haploid genetic screen identifies the major facilitator domain containing 2A (MFSD2A) transporter as a key mediator in the response to tunicamycin.
21677192	1	5	theme	wall	359:362	arg1	biosynthesis					364:375	cell wall biosynthesis	354:375	cell wall biosynthesis	354:375	Tunicamycin (TM) inhibits eukaryotic asparagine-linked glycosylation, protein palmitoylation, ganglioside production, proteoglycan synthesis, 3-hydroxy-3-methylglutaryl coenzyme-A reductase activity, and cell wall biosynthesis in bacteria.
21677192	1	6	link	asparagine-linked	187:203	arg1	glycosylation					205:217	eukaryotic asparagine-linked glycosylation	176:217	eukaryotic asparagine-linked glycosylation	176:217	Tunicamycin (TM) inhibits eukaryotic asparagine-linked glycosylation, protein palmitoylation, ganglioside production, proteoglycan synthesis, 3-hydroxy-3-methylglutaryl coenzyme-A reductase activity, and cell wall biosynthesis in bacteria.
21677192	4	7	theme	major	694:698	arg1	MFSD2A					734:739	MFSD2A	734:739	MFSD2A	734:739	Here, we identify in an unbiased genetic screen a transporter of the major facilitator superfamily, major facilitator domain containing 2A (MFSD2A), as a critical mediator of TM toxicity.
21677192	4	7	theme	major	694:698	arg1	2A					730:731	major facilitator domain containing 2A	694:731	major facilitator domain containing 2A (MFSD2A)	694:740	Here, we identify in an unbiased genetic screen a transporter of the major facilitator superfamily, major facilitator domain containing 2A (MFSD2A), as a critical mediator of TM toxicity.
21677192	4	7	theme	major	694:698	arg1	superfamily					681:691	the major facilitator superfamily	659:691	the major facilitator superfamily	659:691	Here, we identify in an unbiased genetic screen a transporter of the major facilitator superfamily, major facilitator domain containing 2A (MFSD2A), as a critical mediator of TM toxicity.
21677192	1	8	theme	ganglioside	244:254	arg1	production					256:265	ganglioside production	244:265	ganglioside production	244:265	Tunicamycin (TM) inhibits eukaryotic asparagine-linked glycosylation, protein palmitoylation, ganglioside production, proteoglycan synthesis, 3-hydroxy-3-methylglutaryl coenzyme-A reductase activity, and cell wall biosynthesis in bacteria.
21677192	7	9	theme	C	1083:1083	arg1	terminus					1085:1092	the C terminus	1079:1092	the C terminus	1079:1092	Furthermore, MFSD2A mutant analysis reveals an important function of the C terminus for correct intracellular localization and protein stability, and it identifies transmembrane helical amino acid residues essential for mediating TM sensitivity.
21677192	6	10	theme	cellular	923:930	arg1	uptake					935:940	increased cellular TM uptake	913:940	increased cellular TM uptake concomitant with an enhanced endoplasmic reticulum stress response	913:1007	Hypersensitivity is associated with increased cellular TM uptake concomitant with an enhanced endoplasmic reticulum stress response.
21677192	1	11	gly	glycosylation	205:217	arg1	bacteria					380:387	bacteria	380:387	bacteria	380:387	Tunicamycin (TM) inhibits eukaryotic asparagine-linked glycosylation, protein palmitoylation, ganglioside production, proteoglycan synthesis, 3-hydroxy-3-methylglutaryl coenzyme-A reductase activity, and cell wall biosynthesis in bacteria.
21677192	4	12	theme	critical	748:755	arg1	transporter					644:654	a transporter	642:654	a transporter of the major facilitator superfamily, major facilitator domain containing 2A (MFSD2A),	642:741	Here, we identify in an unbiased genetic screen a transporter of the major facilitator superfamily, major facilitator domain containing 2A (MFSD2A), as a critical mediator of TM toxicity.
21677192	4	12	theme	critical	748:755	arg1	mediator					757:764	a critical mediator	746:764	a critical mediator of TM toxicity	746:779	Here, we identify in an unbiased genetic screen a transporter of the major facilitator superfamily, major facilitator domain containing 2A (MFSD2A), as a critical mediator of TM toxicity.
21677192	0	13	theme	MFSD2A	80:85	arg1	transporter					88:98	2A (MFSD2A) transporter	76:98	2A (MFSD2A) transporter	76:98	A haploid genetic screen identifies the major facilitator domain containing 2A (MFSD2A) transporter as a key mediator in the response to tunicamycin.
21677192	6	14	theme	increased	913:921	arg1	uptake					935:940	increased cellular TM uptake	913:940	increased cellular TM uptake concomitant with an enhanced endoplasmic reticulum stress response	913:1007	Hypersensitivity is associated with increased cellular TM uptake concomitant with an enhanced endoplasmic reticulum stress response.
21677192	8	15	theme	TM	1333:1334	arg1	transporter					1336:1346	a putative TM transporter	1322:1346	a putative TM transporter at the plasma membrane	1322:1369	Overall, our data uncover a critical role for MFSD2A by acting as a putative TM transporter at the plasma membrane.
21677192	7	16	theme	TM	1240:1241	arg1	sensitivity					1243:1253	TM sensitivity	1240:1253	TM sensitivity	1240:1253	Furthermore, MFSD2A mutant analysis reveals an important function of the C terminus for correct intracellular localization and protein stability, and it identifies transmembrane helical amino acid residues essential for mediating TM sensitivity.
21677192	8	17	theme	putative	1324:1331	arg1	transporter					1336:1346	a putative TM transporter	1322:1346	a putative TM transporter at the plasma membrane	1322:1369	Overall, our data uncover a critical role for MFSD2A by acting as a putative TM transporter at the plasma membrane.
21677192	7	18	theme	protein	1137:1143	arg1	stability					1145:1153	protein stability	1137:1153	protein stability	1137:1153	Furthermore, MFSD2A mutant analysis reveals an important function of the C terminus for correct intracellular localization and protein stability, and it identifies transmembrane helical amino acid residues essential for mediating TM sensitivity.
21677192	4	19	theme	genetic	627:633	arg1	screen					635:640	an unbiased genetic screen	615:640	an unbiased genetic screen	615:640	Here, we identify in an unbiased genetic screen a transporter of the major facilitator superfamily, major facilitator domain containing 2A (MFSD2A), as a critical mediator of TM toxicity.
21677192	4	20	theme	facilitator	669:679	arg1	superfamily					681:691	the major facilitator superfamily	659:691	the major facilitator superfamily	659:691	Here, we identify in an unbiased genetic screen a transporter of the major facilitator superfamily, major facilitator domain containing 2A (MFSD2A), as a critical mediator of TM toxicity.
21677192	4	20	theme	facilitator	669:679	arg1	2A					730:731	major facilitator domain containing 2A	694:731	major facilitator domain containing 2A (MFSD2A)	694:740	Here, we identify in an unbiased genetic screen a transporter of the major facilitator superfamily, major facilitator domain containing 2A (MFSD2A), as a critical mediator of TM toxicity.
21677192	8	21	theme	critical	1284:1291	arg1	role					1293:1296	a critical role	1282:1296	a critical role for MFSD2A	1282:1307	Overall, our data uncover a critical role for MFSD2A by acting as a putative TM transporter at the plasma membrane.
21677192	2	22	theme	protein	481:487	arg1	response					489:496	the unfolded protein response	468:496	the unfolded protein response	468:496	Treatment of cells with TM elicits endoplasmic reticulum stress and activates the unfolded protein response.
21677192	8	23	from	membrane	1362:1369	arg1	transporter					1336:1346	a putative TM transporter	1322:1346	a putative TM transporter at the plasma membrane	1322:1369	Overall, our data uncover a critical role for MFSD2A by acting as a putative TM transporter at the plasma membrane.
21677192	0	24	theme	haploid	2:8	arg1	screen					18:23	A haploid genetic screen	0:23	A haploid genetic screen	0:23	A haploid genetic screen identifies the major facilitator domain containing 2A (MFSD2A) transporter as a key mediator in the response to tunicamycin.
21677192	6	25	theme	reticulum	983:991	arg1	response					1000:1007	an enhanced endoplasmic reticulum stress response	959:1007	an enhanced endoplasmic reticulum stress response	959:1007	Hypersensitivity is associated with increased cellular TM uptake concomitant with an enhanced endoplasmic reticulum stress response.
21677192	1	26	from	palmitoylation	228:241	arg1	bacteria					380:387	bacteria	380:387	bacteria	380:387	Tunicamycin (TM) inhibits eukaryotic asparagine-linked glycosylation, protein palmitoylation, ganglioside production, proteoglycan synthesis, 3-hydroxy-3-methylglutaryl coenzyme-A reductase activity, and cell wall biosynthesis in bacteria.
21677192	2	27	theme	cells	403:407	arg1	Treatment					390:398	Treatment	390:398	Treatment of cells with TM	390:415	Treatment of cells with TM elicits endoplasmic reticulum stress and activates the unfolded protein response.
21677192	6	28	theme	TM	932:933	arg1	uptake					935:940	increased cellular TM uptake	913:940	increased cellular TM uptake concomitant with an enhanced endoplasmic reticulum stress response	913:1007	Hypersensitivity is associated with increased cellular TM uptake concomitant with an enhanced endoplasmic reticulum stress response.
21677192	1	29	theme	proteoglycan	268:279	arg1	synthesis					281:289	proteoglycan synthesis	268:289	proteoglycan synthesis	268:289	Tunicamycin (TM) inhibits eukaryotic asparagine-linked glycosylation, protein palmitoylation, ganglioside production, proteoglycan synthesis, 3-hydroxy-3-methylglutaryl coenzyme-A reductase activity, and cell wall biosynthesis in bacteria.
21677192	1	30	from	synthesis	281:289	arg1	bacteria					380:387	bacteria	380:387	bacteria	380:387	Tunicamycin (TM) inhibits eukaryotic asparagine-linked glycosylation, protein palmitoylation, ganglioside production, proteoglycan synthesis, 3-hydroxy-3-methylglutaryl coenzyme-A reductase activity, and cell wall biosynthesis in bacteria.
21677192	7	31	theme	correct	1098:1104	arg1	localization					1120:1131	correct intracellular localization	1098:1131	correct intracellular localization	1098:1131	Furthermore, MFSD2A mutant analysis reveals an important function of the C terminus for correct intracellular localization and protein stability, and it identifies transmembrane helical amino acid residues essential for mediating TM sensitivity.
21677192	4	32	theme	major	663:667	arg1	superfamily					681:691	the major facilitator superfamily	659:691	the major facilitator superfamily	659:691	Here, we identify in an unbiased genetic screen a transporter of the major facilitator superfamily, major facilitator domain containing 2A (MFSD2A), as a critical mediator of TM toxicity.
21677192	4	32	theme	major	663:667	arg1	2A					730:731	major facilitator domain containing 2A	694:731	major facilitator domain containing 2A (MFSD2A)	694:740	Here, we identify in an unbiased genetic screen a transporter of the major facilitator superfamily, major facilitator domain containing 2A (MFSD2A), as a critical mediator of TM toxicity.
21677192	5	33	theme	MFSD2A-overexpressing	829:849	arg1	cells					851:855	MFSD2A-overexpressing cells	829:855	MFSD2A-overexpressing cells	829:855	Cells without MFSD2A are TM-resistant, whereas MFSD2A-overexpressing cells are hypersensitive.
21677192	0	34	theme	key	105:107	arg1	mediator					109:116	a key mediator	103:116	a key mediator in the response to tunicamycin	103:147	A haploid genetic screen identifies the major facilitator domain containing 2A (MFSD2A) transporter as a key mediator in the response to tunicamycin.
21677192	0	34	theme	key	105:107	arg1	domain					58:63	the major facilitator domain	36:63	the major facilitator domain containing 2A (MFSD2A) transporter	36:98	A haploid genetic screen identifies the major facilitator domain containing 2A (MFSD2A) transporter as a key mediator in the response to tunicamycin.
21677192	0	35	theme	genetic	10:16	arg1	screen					18:23	A haploid genetic screen	0:23	A haploid genetic screen	0:23	A haploid genetic screen identifies the major facilitator domain containing 2A (MFSD2A) transporter as a key mediator in the response to tunicamycin.
21677192	6	36	theme	stress	993:998	arg1	response					1000:1007	an enhanced endoplasmic reticulum stress response	959:1007	an enhanced endoplasmic reticulum stress response	959:1007	Hypersensitivity is associated with increased cellular TM uptake concomitant with an enhanced endoplasmic reticulum stress response.
21677192	7	37	theme	intracellular	1106:1118	arg1	localization					1120:1131	correct intracellular localization	1098:1131	correct intracellular localization	1098:1131	Furthermore, MFSD2A mutant analysis reveals an important function of the C terminus for correct intracellular localization and protein stability, and it identifies transmembrane helical amino acid residues essential for mediating TM sensitivity.
21677192	8	38	theme	plasma	1355:1360	arg1	membrane					1362:1369	the plasma membrane	1351:1369	the plasma membrane	1351:1369	Overall, our data uncover a critical role for MFSD2A by acting as a putative TM transporter at the plasma membrane.
21677192	2	39	theme	reticulum	437:445	arg1	stress					447:452	endoplasmic reticulum stress	425:452	endoplasmic reticulum stress	425:452	Treatment of cells with TM elicits endoplasmic reticulum stress and activates the unfolded protein response.
21677192	7	40	theme	amino	1196:1200	arg1	residues					1207:1214	transmembrane helical amino acid residues	1174:1214	transmembrane helical amino acid residues essential for mediating TM sensitivity	1174:1253	Furthermore, MFSD2A mutant analysis reveals an important function of the C terminus for correct intracellular localization and protein stability, and it identifies transmembrane helical amino acid residues essential for mediating TM sensitivity.
21677192	1	41	theme	3-hydroxy-3-methylglutaryl	292:317	arg1	reductase					330:338	3-hydroxy-3-methylglutaryl coenzyme-A reductase	292:338	3-hydroxy-3-methylglutaryl coenzyme-A reductase activity	292:347	Tunicamycin (TM) inhibits eukaryotic asparagine-linked glycosylation, protein palmitoylation, ganglioside production, proteoglycan synthesis, 3-hydroxy-3-methylglutaryl coenzyme-A reductase activity, and cell wall biosynthesis in bacteria.
21677192	7	42	theme	terminus	1085:1092	arg1	function					1067:1074	an important function	1054:1074	an important function of the C terminus for correct intracellular localization and protein stability	1054:1153	Furthermore, MFSD2A mutant analysis reveals an important function of the C terminus for correct intracellular localization and protein stability, and it identifies transmembrane helical amino acid residues essential for mediating TM sensitivity.
21677192	2	43	theme	endoplasmic	425:435	arg1	stress					447:452	endoplasmic reticulum stress	425:452	endoplasmic reticulum stress	425:452	Treatment of cells with TM elicits endoplasmic reticulum stress and activates the unfolded protein response.
21677192	1	44	theme	eukaryotic	176:185	arg1	glycosylation					205:217	eukaryotic asparagine-linked glycosylation	176:217	eukaryotic asparagine-linked glycosylation	176:217	Tunicamycin (TM) inhibits eukaryotic asparagine-linked glycosylation, protein palmitoylation, ganglioside production, proteoglycan synthesis, 3-hydroxy-3-methylglutaryl coenzyme-A reductase activity, and cell wall biosynthesis in bacteria.
21677192	1	45	from	biosynthesis	364:375	arg1	bacteria					380:387	bacteria	380:387	bacteria	380:387	Tunicamycin (TM) inhibits eukaryotic asparagine-linked glycosylation, protein palmitoylation, ganglioside production, proteoglycan synthesis, 3-hydroxy-3-methylglutaryl coenzyme-A reductase activity, and cell wall biosynthesis in bacteria.
21677192	1	46	theme	coenzyme-A	319:328	arg1	reductase					330:338	3-hydroxy-3-methylglutaryl coenzyme-A reductase	292:338	3-hydroxy-3-methylglutaryl coenzyme-A reductase activity	292:347	Tunicamycin (TM) inhibits eukaryotic asparagine-linked glycosylation, protein palmitoylation, ganglioside production, proteoglycan synthesis, 3-hydroxy-3-methylglutaryl coenzyme-A reductase activity, and cell wall biosynthesis in bacteria.
21677192	7	47	theme	acid	1202:1205	arg1	residues					1207:1214	transmembrane helical amino acid residues	1174:1214	transmembrane helical amino acid residues essential for mediating TM sensitivity	1174:1253	Furthermore, MFSD2A mutant analysis reveals an important function of the C terminus for correct intracellular localization and protein stability, and it identifies transmembrane helical amino acid residues essential for mediating TM sensitivity.
21677192	7	48	theme	helical	1188:1194	arg1	residues					1207:1214	transmembrane helical amino acid residues	1174:1214	transmembrane helical amino acid residues essential for mediating TM sensitivity	1174:1253	Furthermore, MFSD2A mutant analysis reveals an important function of the C terminus for correct intracellular localization and protein stability, and it identifies transmembrane helical amino acid residues essential for mediating TM sensitivity.
21677192	4	49	theme	unbiased	618:625	arg1	screen					635:640	an unbiased genetic screen	615:640	an unbiased genetic screen	615:640	Here, we identify in an unbiased genetic screen a transporter of the major facilitator superfamily, major facilitator domain containing 2A (MFSD2A), as a critical mediator of TM toxicity.
21677192	1	50	theme	asparagine-linked	187:203	arg1	glycosylation					205:217	eukaryotic asparagine-linked glycosylation	176:217	eukaryotic asparagine-linked glycosylation	176:217	Tunicamycin (TM) inhibits eukaryotic asparagine-linked glycosylation, protein palmitoylation, ganglioside production, proteoglycan synthesis, 3-hydroxy-3-methylglutaryl coenzyme-A reductase activity, and cell wall biosynthesis in bacteria.
21677192	0	51	theme	facilitator	46:56	arg1	mediator					109:116	a key mediator	103:116	a key mediator in the response to tunicamycin	103:147	A haploid genetic screen identifies the major facilitator domain containing 2A (MFSD2A) transporter as a key mediator in the response to tunicamycin.
21677192	0	51	theme	facilitator	46:56	arg1	domain					58:63	the major facilitator domain	36:63	the major facilitator domain containing 2A (MFSD2A) transporter	36:98	A haploid genetic screen identifies the major facilitator domain containing 2A (MFSD2A) transporter as a key mediator in the response to tunicamycin.
21677192	1	52	theme	reductase	330:338	arg1	activity					340:347	3-hydroxy-3-methylglutaryl coenzyme-A reductase activity	292:347	3-hydroxy-3-methylglutaryl coenzyme-A reductase activity	292:347	Tunicamycin (TM) inhibits eukaryotic asparagine-linked glycosylation, protein palmitoylation, ganglioside production, proteoglycan synthesis, 3-hydroxy-3-methylglutaryl coenzyme-A reductase activity, and cell wall biosynthesis in bacteria.
21677192	7	53	theme	important	1057:1065	arg1	function					1067:1074	an important function	1054:1074	an important function of the C terminus for correct intracellular localization and protein stability	1054:1153	Furthermore, MFSD2A mutant analysis reveals an important function of the C terminus for correct intracellular localization and protein stability, and it identifies transmembrane helical amino acid residues essential for mediating TM sensitivity.
21677192	4	54	theme	containing	719:728	arg1	MFSD2A					734:739	MFSD2A	734:739	MFSD2A	734:739	Here, we identify in an unbiased genetic screen a transporter of the major facilitator superfamily, major facilitator domain containing 2A (MFSD2A), as a critical mediator of TM toxicity.
21677192	4	54	theme	containing	719:728	arg1	2A					730:731	major facilitator domain containing 2A	694:731	major facilitator domain containing 2A (MFSD2A)	694:740	Here, we identify in an unbiased genetic screen a transporter of the major facilitator superfamily, major facilitator domain containing 2A (MFSD2A), as a critical mediator of TM toxicity.
21677192	4	54	theme	containing	719:728	arg1	superfamily					681:691	the major facilitator superfamily	659:691	the major facilitator superfamily	659:691	Here, we identify in an unbiased genetic screen a transporter of the major facilitator superfamily, major facilitator domain containing 2A (MFSD2A), as a critical mediator of TM toxicity.
21677192	0	55	theme	major	40:44	arg1	mediator					109:116	a key mediator	103:116	a key mediator in the response to tunicamycin	103:147	A haploid genetic screen identifies the major facilitator domain containing 2A (MFSD2A) transporter as a key mediator in the response to tunicamycin.
21677192	0	55	theme	major	40:44	arg1	domain					58:63	the major facilitator domain	36:63	the major facilitator domain containing 2A (MFSD2A) transporter	36:98	A haploid genetic screen identifies the major facilitator domain containing 2A (MFSD2A) transporter as a key mediator in the response to tunicamycin.
21677192	5	56	dep	TM-resistant	807:818	arg1	whereas					821:827	whereas	821:827	whereas	821:827	Cells without MFSD2A are TM-resistant, whereas MFSD2A-overexpressing cells are hypersensitive.
21677192	1	57	from	production	256:265	arg1	bacteria					380:387	bacteria	380:387	bacteria	380:387	Tunicamycin (TM) inhibits eukaryotic asparagine-linked glycosylation, protein palmitoylation, ganglioside production, proteoglycan synthesis, 3-hydroxy-3-methylglutaryl coenzyme-A reductase activity, and cell wall biosynthesis in bacteria.
21677192	3	58	theme	laboratory	523:532	arg1	settings					534:541	laboratory settings	523:541	laboratory settings	523:541	Although widely used in laboratory settings for many years, it is unknown how TM enters cells.
21677192	6	59	theme	endoplasmic	971:981	arg1	reticulum					983:991	endoplasmic reticulum	971:991	an enhanced endoplasmic reticulum stress response	959:1007	Hypersensitivity is associated with increased cellular TM uptake concomitant with an enhanced endoplasmic reticulum stress response.
21677192	1	60	from	glycosylation	205:217	arg1	bacteria					380:387	bacteria	380:387	bacteria	380:387	Tunicamycin (TM) inhibits eukaryotic asparagine-linked glycosylation, protein palmitoylation, ganglioside production, proteoglycan synthesis, 3-hydroxy-3-methylglutaryl coenzyme-A reductase activity, and cell wall biosynthesis in bacteria.
21677192	4	61	theme	toxicity	772:779	arg1	transporter					644:654	a transporter	642:654	a transporter of the major facilitator superfamily, major facilitator domain containing 2A (MFSD2A),	642:741	Here, we identify in an unbiased genetic screen a transporter of the major facilitator superfamily, major facilitator domain containing 2A (MFSD2A), as a critical mediator of TM toxicity.
21677192	4	61	theme	toxicity	772:779	arg1	mediator					757:764	a critical mediator	746:764	a critical mediator of TM toxicity	746:779	Here, we identify in an unbiased genetic screen a transporter of the major facilitator superfamily, major facilitator domain containing 2A (MFSD2A), as a critical mediator of TM toxicity.
21677192	6	62	with	concomitant	942:952	arg1	response					1000:1007	an enhanced endoplasmic reticulum stress response	959:1007	an enhanced endoplasmic reticulum stress response	959:1007	Hypersensitivity is associated with increased cellular TM uptake concomitant with an enhanced endoplasmic reticulum stress response.
21677192	2	63	with	Treatment	390:398	arg1	TM					414:415	TM	414:415	TM	414:415	Treatment of cells with TM elicits endoplasmic reticulum stress and activates the unfolded protein response.
21677192	4	64	theme	TM	769:770	arg1	toxicity					772:779	TM toxicity	769:779	TM toxicity	769:779	Here, we identify in an unbiased genetic screen a transporter of the major facilitator superfamily, major facilitator domain containing 2A (MFSD2A), as a critical mediator of TM toxicity.
21677192	7	65	theme	MFSD2A	1023:1028	arg1	analysis					1037:1044	MFSD2A mutant analysis	1023:1044	MFSD2A mutant analysis	1023:1044	Furthermore, MFSD2A mutant analysis reveals an important function of the C terminus for correct intracellular localization and protein stability, and it identifies transmembrane helical amino acid residues essential for mediating TM sensitivity.
21677192	4	66	theme	superfamily	681:691	arg1	transporter					644:654	a transporter	642:654	a transporter of the major facilitator superfamily, major facilitator domain containing 2A (MFSD2A),	642:741	Here, we identify in an unbiased genetic screen a transporter of the major facilitator superfamily, major facilitator domain containing 2A (MFSD2A), as a critical mediator of TM toxicity.
21677192	4	66	theme	superfamily	681:691	arg1	mediator					757:764	a critical mediator	746:764	a critical mediator of TM toxicity	746:779	Here, we identify in an unbiased genetic screen a transporter of the major facilitator superfamily, major facilitator domain containing 2A (MFSD2A), as a critical mediator of TM toxicity.
21677192	0	67	from	mediator	109:116	arg1	response					125:132	the response	121:132	the response to tunicamycin	121:147	A haploid genetic screen identifies the major facilitator domain containing 2A (MFSD2A) transporter as a key mediator in the response to tunicamycin.
21677192	7	68	theme	mutant	1030:1035	arg1	analysis					1037:1044	MFSD2A mutant analysis	1023:1044	MFSD2A mutant analysis	1023:1044	Furthermore, MFSD2A mutant analysis reveals an important function of the C terminus for correct intracellular localization and protein stability, and it identifies transmembrane helical amino acid residues essential for mediating TM sensitivity.
21677192	3	69	theme	many	547:550	arg1	years					552:556	many years	547:556	many years	547:556	Although widely used in laboratory settings for many years, it is unknown how TM enters cells.
21677192	1	70	theme	protein	220:226	arg1	palmitoylation					228:241	protein palmitoylation	220:241	protein palmitoylation	220:241	Tunicamycin (TM) inhibits eukaryotic asparagine-linked glycosylation, protein palmitoylation, ganglioside production, proteoglycan synthesis, 3-hydroxy-3-methylglutaryl coenzyme-A reductase activity, and cell wall biosynthesis in bacteria.
21677192	7	71	theme	transmembrane	1174:1186	arg1	residues					1207:1214	transmembrane helical amino acid residues	1174:1214	transmembrane helical amino acid residues essential for mediating TM sensitivity	1174:1253	Furthermore, MFSD2A mutant analysis reveals an important function of the C terminus for correct intracellular localization and protein stability, and it identifies transmembrane helical amino acid residues essential for mediating TM sensitivity.
21677192	6	72	theme	concomitant	942:952	arg1	uptake					935:940	increased cellular TM uptake	913:940	increased cellular TM uptake concomitant with an enhanced endoplasmic reticulum stress response	913:1007	Hypersensitivity is associated with increased cellular TM uptake concomitant with an enhanced endoplasmic reticulum stress response.
21677192	7	73	theme	essential	1216:1224	arg1	residues					1207:1214	transmembrane helical amino acid residues	1174:1214	transmembrane helical amino acid residues essential for mediating TM sensitivity	1174:1253	Furthermore, MFSD2A mutant analysis reveals an important function of the C terminus for correct intracellular localization and protein stability, and it identifies transmembrane helical amino acid residues essential for mediating TM sensitivity.
21677192	2	74	theme	unfolded	472:479	arg1	response					489:496	the unfolded protein response	468:496	the unfolded protein response	468:496	Treatment of cells with TM elicits endoplasmic reticulum stress and activates the unfolded protein response.
21677192	6	75	theme	enhanced	962:969	arg1	response					1000:1007	an enhanced endoplasmic reticulum stress response	959:1007	an enhanced endoplasmic reticulum stress response	959:1007	Hypersensitivity is associated with increased cellular TM uptake concomitant with an enhanced endoplasmic reticulum stress response.
21677192	4	76	theme	domain	712:717	arg1	MFSD2A					734:739	MFSD2A	734:739	MFSD2A	734:739	Here, we identify in an unbiased genetic screen a transporter of the major facilitator superfamily, major facilitator domain containing 2A (MFSD2A), as a critical mediator of TM toxicity.
21677192	4	76	theme	domain	712:717	arg1	2A					730:731	major facilitator domain containing 2A	694:731	major facilitator domain containing 2A (MFSD2A)	694:740	Here, we identify in an unbiased genetic screen a transporter of the major facilitator superfamily, major facilitator domain containing 2A (MFSD2A), as a critical mediator of TM toxicity.
21677192	4	76	theme	domain	712:717	arg1	superfamily					681:691	the major facilitator superfamily	659:691	the major facilitator superfamily	659:691	Here, we identify in an unbiased genetic screen a transporter of the major facilitator superfamily, major facilitator domain containing 2A (MFSD2A), as a critical mediator of TM toxicity.
7505568	1	0	gly	glycoprotein	102:113	arg1	MAG					116:118	MAG	116:118	MAG	116:118	Myelin-associated glycoprotein (MAG) is a neural cell adhesion molecule expressing the L2/HNK-1 carbohydrate epitope.
7505568	1	0	gly	glycoprotein	102:113	arg1	glycoprotein					102:113	Myelin-associated glycoprotein	84:113	Myelin-associated glycoprotein (MAG)	84:119	Myelin-associated glycoprotein (MAG) is a neural cell adhesion molecule expressing the L2/HNK-1 carbohydrate epitope.
7505568	1	0	gly	glycoprotein	102:113	arg1	molecule					147:154	a neural cell adhesion molecule	124:154	a neural cell adhesion molecule expressing the L2/HNK-1 carbohydrate epitope	124:199	Myelin-associated glycoprotein (MAG) is a neural cell adhesion molecule expressing the L2/HNK-1 carbohydrate epitope.
7505568	6	1	contain	bear	593:596	arg2	epitope					611:617	the L2/HNK-1 epitope	598:617	the L2/HNK-1 epitope	598:617	Furthermore, preliminary data indicate that all MAG glycosylated sequons might bear the L2/HNK-1 epitope.
7505568	6	1	contain	bear	593:596	arg1	sequons					579:585	all MAG glycosylated sequons	558:585	all MAG glycosylated sequons	558:585	Furthermore, preliminary data indicate that all MAG glycosylated sequons might bear the L2/HNK-1 epitope.
7505568	3	2	gly	glycopeptides	294:306	arg2	glycopeptides					294:306	human MAG glycopeptides	284:306	human MAG glycopeptides	284:306	In this study, human MAG glycopeptides were isolated and sequenced.
7505568	1	3	theme	L2/HNK-1	171:178	arg1	epitope					193:199	the L2/HNK-1 carbohydrate epitope	167:199	the L2/HNK-1 carbohydrate epitope	167:199	Myelin-associated glycoprotein (MAG) is a neural cell adhesion molecule expressing the L2/HNK-1 carbohydrate epitope.
7505568	4	4	gly	glycosylated	365:376	arg1	7					358:358	7	358:358	7	358:358	Of the 9 MAG sequons 7 were glycosylated and 1 was partially glycosylated at Asn106.
7505568	5	5	gly	glycosylated	500:511	arg1	Asn332					422:427	Asn332	422:427	Asn332 which was not recovered in the glycopeptide fractions	422:481	Asn332 which was not recovered in the glycopeptide fractions was probably not glycosylated.
7505568	0	6	gly	glycoprotein	70:81	arg1	glycoprotein					70:81	human myelin-associated glycoprotein	46:81	human myelin-associated glycoprotein	46:81	Identification of the glycosylated sequons of human myelin-associated glycoprotein.
7505568	6	7	theme	preliminary	527:537	arg1	data					539:542	preliminary data	527:542	preliminary data	527:542	Furthermore, preliminary data indicate that all MAG glycosylated sequons might bear the L2/HNK-1 epitope.
7505568	5	8	gly	glycopeptide	460:471	arg2	glycopeptide					460:471	glycopeptide	460:471	glycopeptide	460:471	Asn332 which was not recovered in the glycopeptide fractions was probably not glycosylated.
7505568	1	9	theme	Myelin-associated	84:100	arg1	MAG					116:118	MAG	116:118	MAG	116:118	Myelin-associated glycoprotein (MAG) is a neural cell adhesion molecule expressing the L2/HNK-1 carbohydrate epitope.
7505568	1	9	theme	Myelin-associated	84:100	arg1	glycoprotein					102:113	Myelin-associated glycoprotein	84:113	Myelin-associated glycoprotein (MAG)	84:119	Myelin-associated glycoprotein (MAG) is a neural cell adhesion molecule expressing the L2/HNK-1 carbohydrate epitope.
7505568	1	9	theme	Myelin-associated	84:100	arg1	molecule					147:154	a neural cell adhesion molecule	124:154	a neural cell adhesion molecule expressing the L2/HNK-1 carbohydrate epitope	124:199	Myelin-associated glycoprotein (MAG) is a neural cell adhesion molecule expressing the L2/HNK-1 carbohydrate epitope.
7505568	1	10	theme	carbohydrate	180:191	arg1	epitope					193:199	the L2/HNK-1 carbohydrate epitope	167:199	the L2/HNK-1 carbohydrate epitope	167:199	Myelin-associated glycoprotein (MAG) is a neural cell adhesion molecule expressing the L2/HNK-1 carbohydrate epitope.
7505568	6	11	theme	glycosylated	566:577	arg1	sequons					579:585	all MAG glycosylated sequons	558:585	all MAG glycosylated sequons	558:585	Furthermore, preliminary data indicate that all MAG glycosylated sequons might bear the L2/HNK-1 epitope.
7505568	6	12	gly	glycosylated	566:577	arg1	sequons					579:585	all MAG glycosylated sequons	558:585	all MAG glycosylated sequons	558:585	Furthermore, preliminary data indicate that all MAG glycosylated sequons might bear the L2/HNK-1 epitope.
7505568	0	13	theme	glycosylated	22:33	arg1	sequons					35:41	the glycosylated sequons	18:41	the glycosylated sequons of human myelin-associated glycoprotein	18:81	Identification of the glycosylated sequons of human myelin-associated glycoprotein.
7505568	3	14	theme	human	284:288	arg1	glycopeptides					294:306	human MAG glycopeptides	284:306	human MAG glycopeptides	284:306	In this study, human MAG glycopeptides were isolated and sequenced.
7505568	0	15	gly	glycosylated	22:33	arg1	sequons					35:41	the glycosylated sequons	18:41	the glycosylated sequons of human myelin-associated glycoprotein	18:81	Identification of the glycosylated sequons of human myelin-associated glycoprotein.
7505568	5	16	theme	glycopeptide	460:471	arg1	fractions					473:481	the glycopeptide fractions	456:481	the glycopeptide fractions	456:481	Asn332 which was not recovered in the glycopeptide fractions was probably not glycosylated.
7505568	3	17	theme	MAG	290:292	arg1	glycopeptides					294:306	human MAG glycopeptides	284:306	human MAG glycopeptides	284:306	In this study, human MAG glycopeptides were isolated and sequenced.
7505568	0	18	theme	sequons	35:41	arg1	Identification					0:13	Identification	0:13	Identification of the glycosylated sequons of human myelin-associated glycoprotein.	0:82	Identification of the glycosylated sequons of human myelin-associated glycoprotein.
7505568	6	19	theme	L2/HNK-1	602:609	arg1	epitope					611:617	the L2/HNK-1 epitope	598:617	the L2/HNK-1 epitope	598:617	Furthermore, preliminary data indicate that all MAG glycosylated sequons might bear the L2/HNK-1 epitope.
7505568	4	20	theme	MAG	346:348	arg1	sequons					350:356	the 9 MAG sequons	340:356	the 9 MAG sequons	340:356	Of the 9 MAG sequons 7 were glycosylated and 1 was partially glycosylated at Asn106.
7505568	0	21	theme	myelin-associated	52:68	arg1	glycoprotein					70:81	human myelin-associated glycoprotein	46:81	human myelin-associated glycoprotein	46:81	Identification of the glycosylated sequons of human myelin-associated glycoprotein.
7505568	2	22	theme	%	243:243	arg1	carbohydrate					245:256	30% carbohydrate	241:256	30% carbohydrate	241:256	MAG is heavily glycosylated containing 30% carbohydrate by weight.
7505568	0	23	theme	human	46:50	arg1	glycoprotein					70:81	human myelin-associated glycoprotein	46:81	human myelin-associated glycoprotein	46:81	Identification of the glycosylated sequons of human myelin-associated glycoprotein.
7505568	2	24	theme	30	241:242	arg1	%					243:243	%	243:243	%	243:243	MAG is heavily glycosylated containing 30% carbohydrate by weight.
7505568	1	25	theme	neural	126:131	arg1	glycoprotein					102:113	Myelin-associated glycoprotein	84:113	Myelin-associated glycoprotein (MAG)	84:119	Myelin-associated glycoprotein (MAG) is a neural cell adhesion molecule expressing the L2/HNK-1 carbohydrate epitope.
7505568	1	25	theme	neural	126:131	arg1	molecule					147:154	a neural cell adhesion molecule	124:154	a neural cell adhesion molecule expressing the L2/HNK-1 carbohydrate epitope	124:199	Myelin-associated glycoprotein (MAG) is a neural cell adhesion molecule expressing the L2/HNK-1 carbohydrate epitope.
7505568	2	26	gly	glycosylated	217:228	arg1	MAG					202:204	MAG	202:204	MAG	202:204	MAG is heavily glycosylated containing 30% carbohydrate by weight.
7505568	1	27	theme	cell	133:136	arg1	glycoprotein					102:113	Myelin-associated glycoprotein	84:113	Myelin-associated glycoprotein (MAG)	84:119	Myelin-associated glycoprotein (MAG) is a neural cell adhesion molecule expressing the L2/HNK-1 carbohydrate epitope.
7505568	1	27	theme	cell	133:136	arg1	molecule					147:154	a neural cell adhesion molecule	124:154	a neural cell adhesion molecule expressing the L2/HNK-1 carbohydrate epitope	124:199	Myelin-associated glycoprotein (MAG) is a neural cell adhesion molecule expressing the L2/HNK-1 carbohydrate epitope.
7505568	1	28	theme	adhesion	138:145	arg1	glycoprotein					102:113	Myelin-associated glycoprotein	84:113	Myelin-associated glycoprotein (MAG)	84:119	Myelin-associated glycoprotein (MAG) is a neural cell adhesion molecule expressing the L2/HNK-1 carbohydrate epitope.
7505568	1	28	theme	adhesion	138:145	arg1	molecule					147:154	a neural cell adhesion molecule	124:154	a neural cell adhesion molecule expressing the L2/HNK-1 carbohydrate epitope	124:199	Myelin-associated glycoprotein (MAG) is a neural cell adhesion molecule expressing the L2/HNK-1 carbohydrate epitope.
7505568	4	29	gly	glycosylated	398:409	arg2	Asn106					414:419	Asn106	414:419	Asn106	414:419	Of the 9 MAG sequons 7 were glycosylated and 1 was partially glycosylated at Asn106.
7505568	4	29	gly	glycosylated	398:409	arg1	1					382:382	1	382:382	1	382:382	Of the 9 MAG sequons 7 were glycosylated and 1 was partially glycosylated at Asn106.
7505568	0	30	theme	glycoprotein	70:81	arg1	sequons					35:41	the glycosylated sequons	18:41	the glycosylated sequons of human myelin-associated glycoprotein	18:81	Identification of the glycosylated sequons of human myelin-associated glycoprotein.
7505568	6	31	dep	glycosylated	566:577	arg1	MAG					562:564	MAG	562:564	MAG	562:564	Furthermore, preliminary data indicate that all MAG glycosylated sequons might bear the L2/HNK-1 epitope.
19368529	11	0	theme	BChE-based	2362:2371	arg1	bioscavengers					2383:2395	BChE-based catalytic bioscavengers	2362:2395	BChE-based catalytic bioscavengers	2362:2395	This study provides the structural basis to design new oximes capable of reactivating phosphoramidyl-hBChE conjugates after intoxication, notably when hBChE is used as pretreatment, or to design BChE-based catalytic bioscavengers.
19368529	6	1	theme	N-propyl	1396:1403	arg1	analogues					1405:1413	N-propyl analogues	1396:1413	N-propyl analogues	1396:1413	The refined structures of aged hBChE conjugates show that aging proceeds through O-dealkylation of the P(R) enantiomer of N,N-diethyl and N-propyl analogues, with subsequent formation of a salt bridge preventing reactivation, similarly to a previous observation made on tabun-ChE conjugates.
19368529	5	2	theme	crystal	1162:1168	arg1	structures					1170:1179	the crystal structures	1158:1179	the crystal structures	1158:1179	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	9	3	theme	N-monoalkyl	1866:1876	arg1	length					1884:1889	the N-monoalkyl chain length	1862:1889	the N-monoalkyl chain length	1862:1889	The correlation between the inhibitory potency and the N-monoalkyl chain length is related to increasingly optimized interactions with the acyl-binding pocket as shown by the X-ray structures.
19368529	5	4	theme	resistance	645:654	arg1	analogues					1247:1255	N-dialkyl tabun analogues	1231:1255	N-dialkyl tabun analogues	1231:1255	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	4	theme	resistance	645:654	arg1	basis					630:634	the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE	626:1188	the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N	626:1229	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	2	5	theme	OP	276:277	arg1	intoxication					279:290	OP intoxication	276:290	OP intoxication	276:290	This bioscavenger is currently in Clinical Phase I for pretreatment of OP intoxication.
19368529	5	6	theme	phosphoramidyl-BChE	659:677	arg1	conjugates					679:688	phosphoramidyl-BChE conjugates	659:688	phosphoramidyl-BChE conjugates	659:688	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	7	7	theme	amino	1600:1604	arg1	group					1606:1610	its amino group	1596:1610	its amino group	1596:1610	Interestingly, the N-methyl analogue projects its amino group towards the choline-binding pocket, so that aging proceeds through deamination.
19368529	10	8	theme	substituent	2135:2145	arg1	effects					2114:2120	steric and electronic effects	2092:2120	steric and electronic effects of the amino substituent of phosphoramidate	2092:2164	These kinetics and X-ray data lead to a structure-activity relationship that highlights steric and electronic effects of the amino substituent of phosphoramidate.
19368529	6	9	theme	conjugates	1295:1304	arg1	structures					1270:1279	The refined structures	1258:1279	The refined structures of aged hBChE conjugates	1258:1304	The refined structures of aged hBChE conjugates show that aging proceeds through O-dealkylation of the P(R) enantiomer of N,N-diethyl and N-propyl analogues, with subsequent formation of a salt bridge preventing reactivation, similarly to a previous observation made on tabun-ChE conjugates.
19368529	5	10	theme	pyridinio	1056:1064	arg1	}					1141:1141	HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate}	907:1141	}	1141:1141	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	10	theme	pyridinio	1056:1064	arg1	reactivation					733:744	reactivation	733:744	reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide]	733:904	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	6	11	theme	salt	1447:1450	arg1	bridge					1452:1457	a salt bridge	1445:1457	a salt bridge preventing reactivation	1445:1481	The refined structures of aged hBChE conjugates show that aging proceeds through O-dealkylation of the P(R) enantiomer of N,N-diethyl and N-propyl analogues, with subsequent formation of a salt bridge preventing reactivation, similarly to a previous observation made on tabun-ChE conjugates.
19368529	5	12	theme	4-hydroxyiminomethylpyridinium	863:892	arg1	dibromide					895:903	TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide	835:903	TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide	835:903	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	12	theme	4-hydroxyiminomethylpyridinium	863:892	arg1	}					832:832	obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}	747:832	obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}	747:832	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	13	theme	{	757:757	arg1	dibromide					895:903	TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide	835:903	TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide	835:903	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	13	theme	{	757:757	arg1	}					832:832	obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}	747:832	obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}	747:832	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	14	theme	methoxy	1067:1073	arg1	}					1141:1141	HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate}	907:1141	}	1141:1141	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	14	theme	methoxy	1067:1073	arg1	reactivation					733:744	reactivation	733:744	reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide]	733:904	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	2	15	theme	Clinical	239:246	arg1	I					254:254	Clinical Phase I	239:254	Clinical Phase I for pretreatment of OP intoxication	239:290	This bioscavenger is currently in Clinical Phase I for pretreatment of OP intoxication.
19368529	5	16	theme	TMB-4	835:839	arg1	dibromide					895:903	TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide	835:903	TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide	835:903	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	16	theme	TMB-4	835:839	arg1	}					832:832	obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}	747:832	obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}	747:832	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	7	17	theme	N-methyl	1569:1576	arg1	analogue					1578:1585	the N-methyl analogue	1565:1585	the N-methyl analogue	1565:1585	Interestingly, the N-methyl analogue projects its amino group towards the choline-binding pocket, so that aging proceeds through deamination.
19368529	5	18	theme	inhibition	721:730	arg1	structures					1170:1179	the crystal structures	1158:1179	the crystal structures	1158:1179	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	18	theme	inhibition	721:730	arg1	kinetics					709:716	the kinetics	705:716	the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging,	705:1152	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	19	theme	1-[[[4-	1033:1039	arg1	}					1141:1141	HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate}	907:1141	}	1141:1141	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	19	theme	1-[[[4-	1033:1039	arg1	reactivation					733:744	reactivation	733:744	reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide]	733:904	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	6	20	theme	tabun-ChE	1528:1536	arg1	conjugates					1538:1547	tabun-ChE conjugates	1528:1547	tabun-ChE conjugates	1528:1547	The refined structures of aged hBChE conjugates show that aging proceeds through O-dealkylation of the P(R) enantiomer of N,N-diethyl and N-propyl analogues, with subsequent formation of a salt bridge preventing reactivation, similarly to a previous observation made on tabun-ChE conjugates.
19368529	5	21	theme	pyridinio	937:945	arg1	}					1141:1141	HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate}	907:1141	}	1141:1141	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	21	theme	pyridinio	937:945	arg1	reactivation					733:744	reactivation	733:744	reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide]	733:904	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	10	22	theme	phosphoramidate	2150:2164	arg1	substituent					2135:2145	the amino substituent	2125:2145	the amino substituent of phosphoramidate	2125:2164	These kinetics and X-ray data lead to a structure-activity relationship that highlights steric and electronic effects of the amino substituent of phosphoramidate.
19368529	5	23	theme	tabun	1241:1245	arg1	basis					630:634	the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE	626:1188	the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N	626:1229	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	23	theme	tabun	1241:1245	arg1	analogues					1247:1255	N-dialkyl tabun analogues	1231:1255	N-dialkyl tabun analogues	1231:1255	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	24	theme	aminocarbonyl	1041:1053	arg1	}					1141:1141	HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate}	907:1141	}	1141:1141	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	24	theme	aminocarbonyl	1041:1053	arg1	reactivation					733:744	reactivation	733:744	reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide]	733:904	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	25	theme	methoxy	947:953	arg1	}					1141:1141	HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate}	907:1141	}	1141:1141	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	25	theme	methoxy	947:953	arg1	reactivation					733:744	reactivation	733:744	reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide]	733:904	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	11	26	theme	new	2218:2220	arg1	oximes					2222:2227	new oximes	2218:2227	new oximes capable of reactivating phosphoramidyl-hBChE conjugates after intoxication	2218:2302	This study provides the structural basis to design new oximes capable of reactivating phosphoramidyl-hBChE conjugates after intoxication, notably when hBChE is used as pretreatment, or to design BChE-based catalytic bioscavengers.
19368529	0	27	theme	butyrylcholinesterase	63:83	arg1	reactivation					41:52	reactivation	41:52	reactivation	41:52	Structure-activity analysis of aging and reactivation of human butyrylcholinesterase inhibited by analogues of tabun.
19368529	0	27	theme	butyrylcholinesterase	63:83	arg1	aging					31:35	aging	31:35	aging	31:35	Structure-activity analysis of aging and reactivation of human butyrylcholinesterase inhibited by analogues of tabun.
19368529	5	28	theme	hydroxyimino	1088:1099	arg1	}					1141:1141	HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate}	907:1141	}	1141:1141	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	28	theme	hydroxyimino	1088:1099	arg1	reactivation					733:744	reactivation	733:744	reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide]	733:904	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	8	29	theme	pocket	1759:1764	arg1	preference					1724:1733	a preference	1722:1733	a preference of hBChE's acyl-binding pocket for larger than 2-atoms linear substituents	1722:1808	This orientation results from a preference of hBChE's acyl-binding pocket for larger than 2-atoms linear substituents.
19368529	5	30	theme	1-[[[4-	914:920	arg1	}					1141:1141	HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate}	907:1141	}	1141:1141	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	30	theme	1-[[[4-	914:920	arg1	reactivation					733:744	reactivation	733:744	reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide]	733:904	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	31	dep	reactivation	733:744	arg1	dibromide					895:903	TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide	835:903	TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide	835:903	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	31	dep	reactivation	733:744	arg1	}					832:832	obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}	747:832	obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}	747:832	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	32	theme	methyl	1101:1106	arg1	}					1141:1141	HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate}	907:1141	}	1141:1141	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	32	theme	methyl	1101:1106	arg1	reactivation					733:744	reactivation	733:744	reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide]	733:904	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	8	33	theme	larger	1770:1775	arg1	substituents					1797:1808	larger than 2-atoms linear substituents	1770:1808	larger than 2-atoms linear substituents	1770:1808	This orientation results from a preference of hBChE's acyl-binding pocket for larger than 2-atoms linear substituents.
19368529	5	34	theme	aminocarbonyl	922:934	arg1	}					1141:1141	HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate}	907:1141	}	1141:1141	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	34	theme	aminocarbonyl	922:934	arg1	reactivation					733:744	reactivation	733:744	reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide]	733:904	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	1	35	theme	hBChE	118:122	arg1	butyrylcholinesterase					137:157	butyrylcholinesterase	137:157	butyrylcholinesterase	137:157	hBChE [human BChE (butyrylcholinesterase)] naturally scavenges OPs (organophosphates).
19368529	1	35	theme	hBChE	118:122	arg1	BChE					131:134	hBChE [human BChE	118:134	hBChE [human BChE (butyrylcholinesterase)]	118:159	hBChE [human BChE (butyrylcholinesterase)] naturally scavenges OPs (organophosphates).
19368529	5	36	theme	methyl	1076:1081	arg1	}					1141:1141	HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate}	907:1141	}	1141:1141	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	36	theme	methyl	1076:1081	arg1	reactivation					733:744	reactivation	733:744	reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide]	733:904	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	37	theme	hydroxyimino	973:984	arg1	}					1141:1141	HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate}	907:1141	}	1141:1141	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	37	theme	hydroxyimino	973:984	arg1	reactivation					733:744	reactivation	733:744	reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide]	733:904	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	3	38	theme	time-dependent	355:368	arg1	process					370:376	a spontaneous time-dependent process	341:376	a spontaneous time-dependent process called 'aging' during which the conjugate is dealkylated	341:433	Phosphylated ChEs (cholinesterases) can undergo a spontaneous time-dependent process called 'aging' during which the conjugate is dealkylated, leading to creation of an enzyme that cannot be reactivated.
19368529	5	39	theme	-2-[	1083:1086	arg1	}					1141:1141	HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate}	907:1141	}	1141:1141	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	39	theme	-2-[	1083:1086	arg1	reactivation					733:744	reactivation	733:744	reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide]	733:904	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	6	40	theme	enantiomer	1366:1375	arg1	O-dealkylation					1339:1352	O-dealkylation	1339:1352	O-dealkylation of the P(R) enantiomer of N,N-diethyl and N-propyl analogues	1339:1413	The refined structures of aged hBChE conjugates show that aging proceeds through O-dealkylation of the P(R) enantiomer of N,N-diethyl and N-propyl analogues, with subsequent formation of a salt bridge preventing reactivation, similarly to a previous observation made on tabun-ChE conjugates.
19368529	5	41	theme	methyl	986:991	arg1	}					1141:1141	HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate}	907:1141	}	1141:1141	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	41	theme	methyl	986:991	arg1	reactivation					733:744	reactivation	733:744	reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide]	733:904	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	42	theme	bis[4-	782:787	arg1	dibromide					895:903	TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide	835:903	TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide	835:903	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	42	theme	bis[4-	782:787	arg1	}					832:832	obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}	747:832	obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}	747:832	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	0	43	theme	Structure-activity	0:17	arg1	analysis					19:26	Structure-activity analysis	0:26	Structure-activity analysis of aging and reactivation of human butyrylcholinesterase	0:83	Structure-activity analysis of aging and reactivation of human butyrylcholinesterase inhibited by analogues of tabun.
19368529	5	44	theme	methyl	955:960	arg1	}					1141:1141	HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate}	907:1141	}	1141:1141	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	44	theme	methyl	955:960	arg1	reactivation					733:744	reactivation	733:744	reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide]	733:904	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	3	45	theme	enzyme	462:467	arg1	creation					447:454	creation	447:454	creation of an enzyme that cannot be reactivated	447:494	Phosphylated ChEs (cholinesterases) can undergo a spontaneous time-dependent process called 'aging' during which the conjugate is dealkylated, leading to creation of an enzyme that cannot be reactivated.
19368529	5	46	theme	[1,3-trimethylene-bis	841:861	arg1	dibromide					895:903	TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide	835:903	TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide	835:903	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	46	theme	[1,3-trimethylene-bis	841:861	arg1	}					832:832	obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}	747:832	obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}	747:832	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	47	theme	-2,4-bis-[	962:971	arg1	}					1141:1141	HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate}	907:1141	}	1141:1141	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	47	theme	-2,4-bis-[	962:971	arg1	reactivation					733:744	reactivation	733:744	reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide]	733:904	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	11	48	theme	structural	2191:2200	arg1	basis					2202:2206	the structural basis	2187:2206	the structural basis to design new oximes capable of reactivating phosphoramidyl-hBChE conjugates after intoxication, notably when hBChE is used as pretreatment, or to design BChE-based catalytic bioscavengers	2187:2395	This study provides the structural basis to design new oximes capable of reactivating phosphoramidyl-hBChE conjugates after intoxication, notably when hBChE is used as pretreatment, or to design BChE-based catalytic bioscavengers.
19368529	9	49	with	interactions	1928:1939	arg1	pocket					1963:1968	the acyl-binding pocket	1946:1968	the acyl-binding pocket	1946:1968	The correlation between the inhibitory potency and the N-monoalkyl chain length is related to increasingly optimized interactions with the acyl-binding pocket as shown by the X-ray structures.
19368529	5	50	theme	pyridinium	1108:1117	arg1	}					1141:1141	HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate}	907:1141	}	1141:1141	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	50	theme	pyridinium	1108:1117	arg1	reactivation					733:744	reactivation	733:744	reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide]	733:904	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	51	theme	dichloride	822:831	arg1	dibromide					895:903	TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide	835:903	TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide	835:903	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	51	theme	dichloride	822:831	arg1	}					832:832	obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}	747:832	obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}	747:832	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	52	theme	monohydrate	1130:1140	arg1	}					1141:1141	HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate}	907:1141	}	1141:1141	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	52	theme	monohydrate	1130:1140	arg1	reactivation					733:744	reactivation	733:744	reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide]	733:904	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	53	theme	{	1032:1032	arg1	}					1141:1141	HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate}	907:1141	}	1141:1141	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	53	theme	{	1032:1032	arg1	reactivation					733:744	reactivation	733:744	reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide]	733:904	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	10	54	theme	structure-activity	2044:2061	arg1	relationship					2063:2074	a structure-activity relationship	2042:2074	a structure-activity relationship that highlights steric and electronic effects of the amino substituent of phosphoramidate	2042:2164	These kinetics and X-ray data lead to a structure-activity relationship that highlights steric and electronic effects of the amino substituent of phosphoramidate.
19368529	6	55	theme	previous	1499:1506	arg1	observation					1508:1518	a previous observation	1497:1518	a previous observation made on tabun-ChE conjugates	1497:1547	The refined structures of aged hBChE conjugates show that aging proceeds through O-dealkylation of the P(R) enantiomer of N,N-diethyl and N-propyl analogues, with subsequent formation of a salt bridge preventing reactivation, similarly to a previous observation made on tabun-ChE conjugates.
19368529	5	56	theme	hBChE	1184:1188	arg1	structures					1170:1179	the crystal structures	1158:1179	the crystal structures	1158:1179	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	56	theme	hBChE	1184:1188	arg1	kinetics					709:716	the kinetics	705:716	the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging,	705:1152	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	57	theme	pyridinium	994:1003	arg1	}					1141:1141	HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate}	907:1141	}	1141:1141	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	57	theme	pyridinium	994:1003	arg1	reactivation					733:744	reactivation	733:744	reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide]	733:904	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	6	58	theme	N	1380:1380	arg1	enantiomer					1366:1375	the P(R) enantiomer	1357:1375	the P(R) enantiomer of N,N-diethyl and N-propyl analogues	1357:1413	The refined structures of aged hBChE conjugates show that aging proceeds through O-dealkylation of the P(R) enantiomer of N,N-diethyl and N-propyl analogues, with subsequent formation of a salt bridge preventing reactivation, similarly to a previous observation made on tabun-ChE conjugates.
19368529	5	59	theme	pyridinium	811:820	arg1	dibromide					895:903	TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide	835:903	TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide	835:903	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	59	theme	pyridinium	811:820	arg1	}					832:832	obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}	747:832	obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}	747:832	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	10	60	theme	steric	2092:2097	arg1	effects					2114:2120	steric and electronic effects	2092:2120	steric and electronic effects of the amino substituent of phosphoramidate	2092:2164	These kinetics and X-ray data lead to a structure-activity relationship that highlights steric and electronic effects of the amino substituent of phosphoramidate.
19368529	5	61	theme	conjugates	679:688	arg1	resistance					645:654	oxime resistance	639:654	oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE	639:1188	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	6	62	theme	analogues	1405:1413	arg1	enantiomer					1366:1375	the P(R) enantiomer	1357:1375	the P(R) enantiomer of N,N-diethyl and N-propyl analogues	1357:1413	The refined structures of aged hBChE conjugates show that aging proceeds through O-dealkylation of the P(R) enantiomer of N,N-diethyl and N-propyl analogues, with subsequent formation of a salt bridge preventing reactivation, similarly to a previous observation made on tabun-ChE conjugates.
19368529	4	63	theme	oxime-mediated	581:594	arg1	reactivation					596:607	oxime-mediated reactivation	581:607	oxime-mediated reactivation	581:607	hBChE inhibited by phosphoramidates such as tabun displays a peculiar resistance to oxime-mediated reactivation.
19368529	9	64	theme	chain	1878:1882	arg1	length					1884:1889	the N-monoalkyl chain length	1862:1889	the N-monoalkyl chain length	1862:1889	The correlation between the inhibitory potency and the N-monoalkyl chain length is related to increasingly optimized interactions with the acyl-binding pocket as shown by the X-ray structures.
19368529	5	65	theme	oxime	639:643	arg1	resistance					645:654	oxime resistance	639:654	oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE	639:1188	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	2	66	theme	intoxication	279:290	arg1	pretreatment					260:271	pretreatment	260:271	pretreatment of OP intoxication	260:290	This bioscavenger is currently in Clinical Phase I for pretreatment of OP intoxication.
19368529	10	67	theme	electronic	2103:2112	arg1	effects					2114:2120	steric and electronic effects	2092:2120	steric and electronic effects of the amino substituent of phosphoramidate	2092:2164	These kinetics and X-ray data lead to a structure-activity relationship that highlights steric and electronic effects of the amino substituent of phosphoramidate.
19368529	5	68	theme	HLö	907:909	arg1	}					1141:1141	HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate}	907:1141	}	1141:1141	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	68	theme	HLö	907:909	arg1	reactivation					733:744	reactivation	733:744	reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide]	733:904	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	0	69	theme	human	57:61	arg1	butyrylcholinesterase					63:83	human butyrylcholinesterase	57:83	human butyrylcholinesterase	57:83	Structure-activity analysis of aging and reactivation of human butyrylcholinesterase inhibited by analogues of tabun.
19368529	6	70	theme	bridge	1452:1457	arg1	formation					1432:1440	subsequent formation	1421:1440	subsequent formation of a salt bridge preventing reactivation	1421:1481	The refined structures of aged hBChE conjugates show that aging proceeds through O-dealkylation of the P(R) enantiomer of N,N-diethyl and N-propyl analogues, with subsequent formation of a salt bridge preventing reactivation, similarly to a previous observation made on tabun-ChE conjugates.
19368529	3	71	theme	Phosphylated	293:304	arg1	cholinesterases					312:326	cholinesterases	312:326	cholinesterases	312:326	Phosphylated ChEs (cholinesterases) can undergo a spontaneous time-dependent process called 'aging' during which the conjugate is dealkylated, leading to creation of an enzyme that cannot be reactivated.
19368529	3	71	theme	Phosphylated	293:304	arg1	ChEs					306:309	Phosphylated ChEs	293:309	Phosphylated ChEs (cholinesterases)	293:327	Phosphylated ChEs (cholinesterases) can undergo a spontaneous time-dependent process called 'aging' during which the conjugate is dealkylated, leading to creation of an enzyme that cannot be reactivated.
19368529	9	72	theme	optimized	1918:1926	arg1	interactions					1928:1939	increasingly optimized interactions	1905:1939	increasingly optimized interactions with the acyl-binding pocket	1905:1968	The correlation between the inhibitory potency and the N-monoalkyl chain length is related to increasingly optimized interactions with the acyl-binding pocket as shown by the X-ray structures.
19368529	6	73	theme	hBChE	1289:1293	arg1	conjugates					1295:1304	aged hBChE conjugates	1284:1304	aged hBChE conjugates	1284:1304	The refined structures of aged hBChE conjugates show that aging proceeds through O-dealkylation of the P(R) enantiomer of N,N-diethyl and N-propyl analogues, with subsequent formation of a salt bridge preventing reactivation, similarly to a previous observation made on tabun-ChE conjugates.
19368529	2	74	theme	Phase	248:252	arg1	I					254:254	Clinical Phase I	239:254	Clinical Phase I for pretreatment of OP intoxication	239:290	This bioscavenger is currently in Clinical Phase I for pretreatment of OP intoxication.
19368529	5	75	theme	1,1'-	758:762	arg1	dibromide					895:903	TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide	835:903	TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide	835:903	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	75	theme	1,1'-	758:762	arg1	}					832:832	obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}	747:832	obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}	747:832	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	1	76	theme	[human	124:129	arg1	butyrylcholinesterase					137:157	butyrylcholinesterase	137:157	butyrylcholinesterase	137:157	hBChE [human BChE (butyrylcholinesterase)] naturally scavenges OPs (organophosphates).
19368529	1	76	theme	[human	124:129	arg1	BChE					131:134	hBChE [human BChE	118:134	hBChE [human BChE (butyrylcholinesterase)]	118:159	hBChE [human BChE (butyrylcholinesterase)] naturally scavenges OPs (organophosphates).
19368529	9	77	theme	acyl-binding	1950:1961	arg1	pocket					1963:1968	the acyl-binding pocket	1946:1968	the acyl-binding pocket	1946:1968	The correlation between the inhibitory potency and the N-monoalkyl chain length is related to increasingly optimized interactions with the acyl-binding pocket as shown by the X-ray structures.
19368529	5	78	theme	N-dialkyl	1231:1239	arg1	basis					630:634	the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE	626:1188	the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N	626:1229	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	78	theme	N-dialkyl	1231:1239	arg1	analogues					1247:1255	N-dialkyl tabun analogues	1231:1255	N-dialkyl tabun analogues	1231:1255	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	6	79	theme	refined	1262:1268	arg1	structures					1270:1279	The refined structures	1258:1279	The refined structures of aged hBChE conjugates	1258:1304	The refined structures of aged hBChE conjugates show that aging proceeds through O-dealkylation of the P(R) enantiomer of N,N-diethyl and N-propyl analogues, with subsequent formation of a salt bridge preventing reactivation, similarly to a previous observation made on tabun-ChE conjugates.
19368529	0	80	theme	reactivation	41:52	arg1	analysis					19:26	Structure-activity analysis	0:26	Structure-activity analysis of aging and reactivation of human butyrylcholinesterase	0:83	Structure-activity analysis of aging and reactivation of human butyrylcholinesterase inhibited by analogues of tabun.
19368529	6	81	theme	P	1361:1361	arg1	enantiomer					1366:1375	the P(R) enantiomer	1357:1375	the P(R) enantiomer of N,N-diethyl and N-propyl analogues	1357:1413	The refined structures of aged hBChE conjugates show that aging proceeds through O-dealkylation of the P(R) enantiomer of N,N-diethyl and N-propyl analogues, with subsequent formation of a salt bridge preventing reactivation, similarly to a previous observation made on tabun-ChE conjugates.
19368529	5	82	theme	{	913:913	arg1	}					1141:1141	HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate}	907:1141	}	1141:1141	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	82	theme	{	913:913	arg1	reactivation					733:744	reactivation	733:744	reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide]	733:904	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	3	83	theme	spontaneous	343:353	arg1	process					370:376	a spontaneous time-dependent process	341:376	a spontaneous time-dependent process called 'aging' during which the conjugate is dealkylated	341:433	Phosphylated ChEs (cholinesterases) can undergo a spontaneous time-dependent process called 'aging' during which the conjugate is dealkylated, leading to creation of an enzyme that cannot be reactivated.
19368529	5	84	theme	hydroxyimino	789:800	arg1	dibromide					895:903	TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide	835:903	TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide	835:903	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	84	theme	hydroxyimino	789:800	arg1	}					832:832	obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}	747:832	obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}	747:832	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	8	85	theme	acyl-binding	1746:1757	arg1	pocket					1759:1764	hBChE's acyl-binding pocket	1738:1764	hBChE's acyl-binding pocket	1738:1764	This orientation results from a preference of hBChE's acyl-binding pocket for larger than 2-atoms linear substituents.
19368529	9	86	theme	X-ray	1986:1990	arg1	structures					1992:2001	the X-ray structures	1982:2001	the X-ray structures	1982:2001	The correlation between the inhibitory potency and the N-monoalkyl chain length is related to increasingly optimized interactions with the acyl-binding pocket as shown by the X-ray structures.
19368529	10	87	theme	X-ray	2023:2027	arg1	data					2029:2032	These kinetics and X-ray data	2004:2032	These kinetics and X-ray data	2004:2032	These kinetics and X-ray data lead to a structure-activity relationship that highlights steric and electronic effects of the amino substituent of phosphoramidate.
19368529	0	88	theme	tabun	111:115	arg1	analogues					98:106	analogues	98:106	analogues of tabun	98:115	Structure-activity analysis of aging and reactivation of human butyrylcholinesterase inhibited by analogues of tabun.
19368529	11	89	theme	phosphoramidyl-hBChE	2253:2272	arg1	conjugates					2274:2283	phosphoramidyl-hBChE conjugates	2253:2283	phosphoramidyl-hBChE conjugates	2253:2283	This study provides the structural basis to design new oximes capable of reactivating phosphoramidyl-hBChE conjugates after intoxication, notably when hBChE is used as pretreatment, or to design BChE-based catalytic bioscavengers.
19368529	11	90	used	used	2327:2330	arg2	hBChE					2318:2322	hBChE	2318:2322	hBChE	2318:2322	This study provides the structural basis to design new oximes capable of reactivating phosphoramidyl-hBChE conjugates after intoxication, notably when hBChE is used as pretreatment, or to design BChE-based catalytic bioscavengers.
19368529	11	90	used	used	2327:2330	arg2	pretreatment					2335:2346	pretreatment	2335:2346	pretreatment	2335:2346	This study provides the structural basis to design new oximes capable of reactivating phosphoramidyl-hBChE conjugates after intoxication, notably when hBChE is used as pretreatment, or to design BChE-based catalytic bioscavengers.
19368529	11	91	theme	catalytic	2373:2381	arg1	bioscavengers					2383:2395	BChE-based catalytic bioscavengers	2362:2395	BChE-based catalytic bioscavengers	2362:2395	This study provides the structural basis to design new oximes capable of reactivating phosphoramidyl-hBChE conjugates after intoxication, notably when hBChE is used as pretreatment, or to design BChE-based catalytic bioscavengers.
19368529	10	92	theme	amino	2129:2133	arg1	substituent					2135:2145	the amino substituent	2125:2145	the amino substituent of phosphoramidate	2125:2164	These kinetics and X-ray data lead to a structure-activity relationship that highlights steric and electronic effects of the amino substituent of phosphoramidate.
19368529	10	93	theme	kinetics	2010:2017	arg1	data					2029:2032	These kinetics and X-ray data	2004:2032	These kinetics and X-ray data	2004:2032	These kinetics and X-ray data lead to a structure-activity relationship that highlights steric and electronic effects of the amino substituent of phosphoramidate.
19368529	5	94	theme	oxybis-methylene	764:779	arg1	dibromide					895:903	TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide	835:903	TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide	835:903	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	94	theme	oxybis-methylene	764:779	arg1	}					832:832	obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}	747:832	obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}	747:832	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	11	95	theme	capable	2229:2235	arg1	oximes					2222:2227	new oximes	2218:2227	new oximes capable of reactivating phosphoramidyl-hBChE conjugates after intoxication	2218:2302	This study provides the structural basis to design new oximes capable of reactivating phosphoramidyl-hBChE conjugates after intoxication, notably when hBChE is used as pretreatment, or to design BChE-based catalytic bioscavengers.
19368529	6	96	theme	N-diethyl	1382:1390	arg1	enantiomer					1366:1375	the P(R) enantiomer	1357:1375	the P(R) enantiomer of N,N-diethyl and N-propyl analogues	1357:1413	The refined structures of aged hBChE conjugates show that aging proceeds through O-dealkylation of the P(R) enantiomer of N,N-diethyl and N-propyl analogues, with subsequent formation of a salt bridge preventing reactivation, similarly to a previous observation made on tabun-ChE conjugates.
19368529	8	97	theme	linear	1790:1795	arg1	substituents					1797:1808	larger than 2-atoms linear substituents	1770:1808	larger than 2-atoms linear substituents	1770:1808	This orientation results from a preference of hBChE's acyl-binding pocket for larger than 2-atoms linear substituents.
19368529	5	98	theme	obidoxime	747:755	arg1	dibromide					895:903	TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide	835:903	TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide	835:903	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	98	theme	obidoxime	747:755	arg1	}					832:832	obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}	747:832	obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}	747:832	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	4	99	theme	peculiar	558:565	arg1	resistance					567:576	a peculiar resistance	556:576	a peculiar resistance to oxime-mediated reactivation	556:607	hBChE inhibited by phosphoramidates such as tabun displays a peculiar resistance to oxime-mediated reactivation.
19368529	11	100	dep	basis	2202:2206	arg1	design					2355:2360	design	2355:2360	to design BChE-based catalytic bioscavengers	2352:2395	This study provides the structural basis to design new oximes capable of reactivating phosphoramidyl-hBChE conjugates after intoxication, notably when hBChE is used as pretreatment, or to design BChE-based catalytic bioscavengers.
19368529	11	100	dep	basis	2202:2206	arg1	design					2211:2216	design	2211:2216	design	2211:2216	This study provides the structural basis to design new oximes capable of reactivating phosphoramidyl-hBChE conjugates after intoxication, notably when hBChE is used as pretreatment, or to design BChE-based catalytic bioscavengers.
19368529	0	101	theme	aging	31:35	arg1	analysis					19:26	Structure-activity analysis	0:26	Structure-activity analysis of aging and reactivation of human butyrylcholinesterase	0:83	Structure-activity analysis of aging and reactivation of human butyrylcholinesterase inhibited by analogues of tabun.
19368529	7	102	theme	choline-binding	1624:1638	arg1	pocket					1640:1645	the choline-binding pocket	1620:1645	the choline-binding pocket	1620:1645	Interestingly, the N-methyl analogue projects its amino group towards the choline-binding pocket, so that aging proceeds through deamination.
19368529	5	103	theme	methyl	803:808	arg1	dibromide					895:903	TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide	835:903	TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide	835:903	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	103	theme	methyl	803:808	arg1	}					832:832	obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}	747:832	obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}	747:832	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	6	104	theme	R	1363:1363	arg1	enantiomer					1366:1375	the P(R) enantiomer	1357:1375	the P(R) enantiomer of N,N-diethyl and N-propyl analogues	1357:1413	The refined structures of aged hBChE conjugates show that aging proceeds through O-dealkylation of the P(R) enantiomer of N,N-diethyl and N-propyl analogues, with subsequent formation of a salt bridge preventing reactivation, similarly to a previous observation made on tabun-ChE conjugates.
19368529	5	105	theme	dichloride	1119:1128	arg1	}					1141:1141	HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate}	907:1141	}	1141:1141	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	105	theme	dichloride	1119:1128	arg1	reactivation					733:744	reactivation	733:744	reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide]	733:904	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	6	106	theme	aged	1284:1287	arg1	conjugates					1295:1304	aged hBChE conjugates	1284:1304	aged hBChE conjugates	1284:1304	The refined structures of aged hBChE conjugates show that aging proceeds through O-dealkylation of the P(R) enantiomer of N,N-diethyl and N-propyl analogues, with subsequent formation of a salt bridge preventing reactivation, similarly to a previous observation made on tabun-ChE conjugates.
19368529	6	107	theme	subsequent	1421:1430	arg1	formation					1432:1440	subsequent formation	1421:1440	subsequent formation of a salt bridge preventing reactivation	1421:1481	The refined structures of aged hBChE conjugates show that aging proceeds through O-dealkylation of the P(R) enantiomer of N,N-diethyl and N-propyl analogues, with subsequent formation of a salt bridge preventing reactivation, similarly to a previous observation made on tabun-ChE conjugates.
19368529	5	108	theme	dimethanesulfonate	1005:1022	arg1	}					1141:1141	HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate}	907:1141	}	1141:1141	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	5	108	theme	dimethanesulfonate	1005:1022	arg1	reactivation					733:744	reactivation	733:744	reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide]	733:904	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
19368529	9	109	theme	inhibitory	1839:1848	arg1	potency					1850:1856	the inhibitory potency	1835:1856	the inhibitory potency	1835:1856	The correlation between the inhibitory potency and the N-monoalkyl chain length is related to increasingly optimized interactions with the acyl-binding pocket as shown by the X-ray structures.
19368529	5	110	theme	different	1203:1211	arg1	N-monoalkyl					1213:1223	different N-monoalkyl	1203:1223	different N-monoalkyl	1203:1223	We investigated the basis of oxime resistance of phosphoramidyl-BChE conjugates by determining the kinetics of inhibition, reactivation (obidoxime {1,1'-(oxybis-methylene) bis[4-(hydroxyimino) methyl] pyridinium dichloride}, TMB-4 [1,3-trimethylene-bis(4-hydroxyiminomethylpyridinium) dibromide], HLö 7 {1-[[[4-(aminocarbonyl) pyridinio]methoxy]methyl]-2,4-bis-[(hydroxyimino)methyl] pyridinium dimethanesulfonate)}, HI-6 {1-[[[4-(aminocarbonyl) pyridinio] methoxy] methyl]-2-[(hydroxyimino)methyl]pyridinium dichloride monohydrate} and aging, and the crystal structures of hBChE inhibited by different N-monoalkyl and N,N-dialkyl tabun analogues.
12869558	3	0	theme	crystal	336:342	arg1	structures					344:353	Several crystal structures	328:353	Several crystal structures of the former	328:367	Several crystal structures of the former have shown that the active site is located at the bottom of a deep and narrow gorge, raising the question of how substrate and products enter and leave.
12869558	5	1	theme	human	764:768	arg1	complexes					775:783	several recombinant truncated human BChE complexes	734:783	several recombinant truncated human BChE complexes	734:783	Here we report the crystal structures of several recombinant truncated human BChE complexes and conjugates and provide a description for mechanistically relevant non-productive substrate and product binding.
12869558	5	2	theme	BChE	770:773	arg1	complexes					775:783	several recombinant truncated human BChE complexes	734:783	several recombinant truncated human BChE complexes	734:783	Here we report the crystal structures of several recombinant truncated human BChE complexes and conjugates and provide a description for mechanistically relevant non-productive substrate and product binding.
12869558	5	3	theme	crystal	712:718	arg1	structures					720:729	the crystal structures	708:729	the crystal structures of several recombinant truncated human BChE complexes and conjugates	708:798	Here we report the crystal structures of several recombinant truncated human BChE complexes and conjugates and provide a description for mechanistically relevant non-productive substrate and product binding.
12869558	3	4	from	bottom	419:424	arg1	site					396:399	the active site	385:399	the active site	385:399	Several crystal structures of the former have shown that the active site is located at the bottom of a deep and narrow gorge, raising the question of how substrate and products enter and leave.
12869558	3	4	from	bottom	419:424	arg1	located					404:410	located	404:410	located	404:410	Several crystal structures of the former have shown that the active site is located at the bottom of a deep and narrow gorge, raising the question of how substrate and products enter and leave.
12869558	6	5	theme	enzyme	999:1004	arg1	model					985:989	a previously published theoretical model	950:989	a previously published theoretical model of this enzyme	950:1004	As expected, the structure of BChE is similar to a previously published theoretical model of this enzyme and to the structure of Torpedo acetylcholinesterase.
12869558	3	6	theme	former	362:367	arg1	structures					344:353	Several crystal structures	328:353	Several crystal structures of the former	328:367	Several crystal structures of the former have shown that the active site is located at the bottom of a deep and narrow gorge, raising the question of how substrate and products enter and leave.
12869558	0	7	with	complexes	60:68	arg1	substrate					75:83	substrate	75:83	substrate	75:83	Crystal structure of human butyrylcholinesterase and of its complexes with substrate and products.
12869558	0	7	with	complexes	60:68	arg1	products					89:96	products	89:96	products	89:96	Crystal structure of human butyrylcholinesterase and of its complexes with substrate and products.
12869558	3	8	theme	deep	431:434	arg1	gorge					447:451	a deep and narrow gorge	429:451	a deep and narrow gorge	429:451	Several crystal structures of the former have shown that the active site is located at the bottom of a deep and narrow gorge, raising the question of how substrate and products enter and leave.
12869558	5	9	theme	several	734:740	arg1	complexes					775:783	several recombinant truncated human BChE complexes	734:783	several recombinant truncated human BChE complexes	734:783	Here we report the crystal structures of several recombinant truncated human BChE complexes and conjugates and provide a description for mechanistically relevant non-productive substrate and product binding.
12869558	7	10	theme	acyl	1163:1166	arg1	bigger					1205:1210	bigger	1205:1210	bigger	1205:1210	The main difference between the experimentally determined BChE structure and its model is found at the acyl binding pocket that is significantly bigger than expected.
12869558	7	10	theme	acyl	1163:1166	arg1	pocket					1176:1181	the acyl binding pocket	1159:1181	the acyl binding pocket that is significantly bigger than expected	1159:1224	The main difference between the experimentally determined BChE structure and its model is found at the acyl binding pocket that is significantly bigger than expected.
12869558	5	11	theme	product	884:890	arg1	binding					892:898	mechanistically relevant non-productive substrate and product binding	830:898	mechanistically relevant non-productive substrate and product binding	830:898	Here we report the crystal structures of several recombinant truncated human BChE complexes and conjugates and provide a description for mechanistically relevant non-productive substrate and product binding.
12869558	7	12	theme	determined	1107:1116	arg1	structure					1123:1131	the experimentally determined BChE structure	1088:1131	the experimentally determined BChE structure	1088:1131	The main difference between the experimentally determined BChE structure and its model is found at the acyl binding pocket that is significantly bigger than expected.
12869558	7	13	theme	main	1064:1067	arg1	difference					1069:1078	The main difference	1060:1078	The main difference between the experimentally determined BChE structure and its model	1060:1145	The main difference between the experimentally determined BChE structure and its model is found at the acyl binding pocket that is significantly bigger than expected.
12869558	8	14	theme	catalytic	1265:1273	arg1	198					1279:1281	198	1279:1281	198	1279:1281	An electron density peak close to the catalytic Ser(198) has been modeled as bound butyrate.
12869558	8	14	theme	catalytic	1265:1273	arg1	Ser					1275:1277	the catalytic Ser	1261:1277	the catalytic Ser(198)	1261:1282	An electron density peak close to the catalytic Ser(198) has been modeled as bound butyrate.
12869558	0	15	theme	Crystal	0:6	arg1	structure					8:16	Crystal structure	0:16	Crystal structure of human butyrylcholinesterase and of its complexes with substrate and products	0:96	Crystal structure of human butyrylcholinesterase and of its complexes with substrate and products.
12869558	7	16	theme	BChE	1118:1121	arg1	structure					1123:1131	the experimentally determined BChE structure	1088:1131	the experimentally determined BChE structure	1088:1131	The main difference between the experimentally determined BChE structure and its model is found at the acyl binding pocket that is significantly bigger than expected.
12869558	4	17	theme	organophosphorus	647:662	arg1	pesticides					664:673	organophosphorus pesticides	647:673	organophosphorus pesticides	647:673	Human butyrylcholinesterase (BChE) has attracted attention because it can hydrolyze toxic esters such as cocaine or scavenge organophosphorus pesticides and nerve agents.
12869558	0	18	theme	human	21:25	arg1	butyrylcholinesterase					27:47	human butyrylcholinesterase	21:47	human butyrylcholinesterase	21:47	Crystal structure of human butyrylcholinesterase and of its complexes with substrate and products.
12869558	2	19	theme	function	318:325	arg1	butyrylcholinesterase					285:305	butyrylcholinesterase	285:305	butyrylcholinesterase of unknown function	285:325	They are divided into two groups: acetylcholinesterase, involved in the hydrolysis of the neurotransmitter acetylcholine, and butyrylcholinesterase of unknown function.
12869558	2	19	theme	function	318:325	arg1	acetylcholinesterase					193:212	acetylcholinesterase	193:212	acetylcholinesterase	193:212	They are divided into two groups: acetylcholinesterase, involved in the hydrolysis of the neurotransmitter acetylcholine, and butyrylcholinesterase of unknown function.
12869558	2	19	theme	function	318:325	arg1	groups					185:190	two groups	181:190	two groups: acetylcholinesterase, involved in the hydrolysis of the neurotransmitter acetylcholine, and butyrylcholinesterase of unknown function	181:325	They are divided into two groups: acetylcholinesterase, involved in the hydrolysis of the neurotransmitter acetylcholine, and butyrylcholinesterase of unknown function.
12869558	3	20	theme	active	389:394	arg1	site					396:399	the active site	385:399	the active site	385:399	Several crystal structures of the former have shown that the active site is located at the bottom of a deep and narrow gorge, raising the question of how substrate and products enter and leave.
12869558	3	20	theme	active	389:394	arg1	located					404:410	located	404:410	located	404:410	Several crystal structures of the former have shown that the active site is located at the bottom of a deep and narrow gorge, raising the question of how substrate and products enter and leave.
12869558	6	21	theme	theoretical	973:983	arg1	model					985:989	a previously published theoretical model	950:989	a previously published theoretical model of this enzyme	950:1004	As expected, the structure of BChE is similar to a previously published theoretical model of this enzyme and to the structure of Torpedo acetylcholinesterase.
12869558	2	22	theme	unknown	310:316	arg1	function					318:325	unknown function	310:325	unknown function	310:325	They are divided into two groups: acetylcholinesterase, involved in the hydrolysis of the neurotransmitter acetylcholine, and butyrylcholinesterase of unknown function.
12869558	6	23	theme	BChE	931:934	arg1	similar					939:945	similar	939:945	similar	939:945	As expected, the structure of BChE is similar to a previously published theoretical model of this enzyme and to the structure of Torpedo acetylcholinesterase.
12869558	6	23	theme	BChE	931:934	arg1	structure					918:926	the structure	914:926	the structure of BChE	914:934	As expected, the structure of BChE is similar to a previously published theoretical model of this enzyme and to the structure of Torpedo acetylcholinesterase.
12869558	5	24	theme	relevant	846:853	arg1	binding					892:898	mechanistically relevant non-productive substrate and product binding	830:898	mechanistically relevant non-productive substrate and product binding	830:898	Here we report the crystal structures of several recombinant truncated human BChE complexes and conjugates and provide a description for mechanistically relevant non-productive substrate and product binding.
12869558	5	25	theme	complexes	775:783	arg1	structures					720:729	the crystal structures	708:729	the crystal structures of several recombinant truncated human BChE complexes and conjugates	708:798	Here we report the crystal structures of several recombinant truncated human BChE complexes and conjugates and provide a description for mechanistically relevant non-productive substrate and product binding.
12869558	6	26	theme	published	963:971	arg1	model					985:989	a previously published theoretical model	950:989	a previously published theoretical model of this enzyme	950:1004	As expected, the structure of BChE is similar to a previously published theoretical model of this enzyme and to the structure of Torpedo acetylcholinesterase.
12869558	3	27	theme	narrow	440:445	arg1	gorge					447:451	a deep and narrow gorge	429:451	a deep and narrow gorge	429:451	Several crystal structures of the former have shown that the active site is located at the bottom of a deep and narrow gorge, raising the question of how substrate and products enter and leave.
12869558	0	28	theme	butyrylcholinesterase	27:47	arg1	structure					8:16	Crystal structure	0:16	Crystal structure of human butyrylcholinesterase and of its complexes with substrate and products	0:96	Crystal structure of human butyrylcholinesterase and of its complexes with substrate and products.
12869558	7	29	theme	binding	1168:1174	arg1	bigger					1205:1210	bigger	1205:1210	bigger	1205:1210	The main difference between the experimentally determined BChE structure and its model is found at the acyl binding pocket that is significantly bigger than expected.
12869558	7	29	theme	binding	1168:1174	arg1	pocket					1176:1181	the acyl binding pocket	1159:1181	the acyl binding pocket that is significantly bigger than expected	1159:1224	The main difference between the experimentally determined BChE structure and its model is found at the acyl binding pocket that is significantly bigger than expected.
12869558	3	30	theme	gorge	447:451	arg1	bottom					419:424	the bottom	415:424	the bottom of a deep and narrow gorge	415:451	Several crystal structures of the former have shown that the active site is located at the bottom of a deep and narrow gorge, raising the question of how substrate and products enter and leave.
12869558	5	31	theme	conjugates	789:798	arg1	structures					720:729	the crystal structures	708:729	the crystal structures of several recombinant truncated human BChE complexes and conjugates	708:798	Here we report the crystal structures of several recombinant truncated human BChE complexes and conjugates and provide a description for mechanistically relevant non-productive substrate and product binding.
12869558	6	32	theme	acetylcholinesterase	1038:1057	arg1	structure					1017:1025	the structure	1013:1025	the structure of Torpedo acetylcholinesterase	1013:1057	As expected, the structure of BChE is similar to a previously published theoretical model of this enzyme and to the structure of Torpedo acetylcholinesterase.
12869558	3	33	located	located	404:410	arg2	site					396:399	the active site	385:399	the active site	385:399	Several crystal structures of the former have shown that the active site is located at the bottom of a deep and narrow gorge, raising the question of how substrate and products enter and leave.
12869558	3	33	located	located	404:410	arg2	located					404:410	located	404:410	located	404:410	Several crystal structures of the former have shown that the active site is located at the bottom of a deep and narrow gorge, raising the question of how substrate and products enter and leave.
12869558	3	33	located	located	404:410	arg1	bottom					419:424	the bottom	415:424	the bottom of a deep and narrow gorge	415:451	Several crystal structures of the former have shown that the active site is located at the bottom of a deep and narrow gorge, raising the question of how substrate and products enter and leave.
12869558	8	34	theme	density	1239:1245	arg1	butyrate					1310:1317	bound butyrate	1304:1317	bound butyrate	1304:1317	An electron density peak close to the catalytic Ser(198) has been modeled as bound butyrate.
12869558	8	34	theme	density	1239:1245	arg1	peak					1247:1250	An electron density peak	1227:1250	An electron density peak close to the catalytic Ser(198)	1227:1282	An electron density peak close to the catalytic Ser(198) has been modeled as bound butyrate.
12869558	4	35	theme	Human	522:526	arg1	BChE					551:554	BChE	551:554	BChE	551:554	Human butyrylcholinesterase (BChE) has attracted attention because it can hydrolyze toxic esters such as cocaine or scavenge organophosphorus pesticides and nerve agents.
12869558	4	35	theme	Human	522:526	arg1	butyrylcholinesterase					528:548	Human butyrylcholinesterase	522:548	Human butyrylcholinesterase (BChE)	522:555	Human butyrylcholinesterase (BChE) has attracted attention because it can hydrolyze toxic esters such as cocaine or scavenge organophosphorus pesticides and nerve agents.
12869558	3	36	theme	Several	328:334	arg1	structures					344:353	Several crystal structures	328:353	Several crystal structures of the former	328:367	Several crystal structures of the former have shown that the active site is located at the bottom of a deep and narrow gorge, raising the question of how substrate and products enter and leave.
12869558	8	37	theme	electron	1230:1237	arg1	butyrate					1310:1317	bound butyrate	1304:1317	bound butyrate	1304:1317	An electron density peak close to the catalytic Ser(198) has been modeled as bound butyrate.
12869558	8	37	theme	electron	1230:1237	arg1	peak					1247:1250	An electron density peak	1227:1250	An electron density peak close to the catalytic Ser(198)	1227:1282	An electron density peak close to the catalytic Ser(198) has been modeled as bound butyrate.
12869558	2	38	theme	acetylcholine	266:278	arg1	hydrolysis					231:240	the hydrolysis	227:240	the hydrolysis of the neurotransmitter acetylcholine	227:278	They are divided into two groups: acetylcholinesterase, involved in the hydrolysis of the neurotransmitter acetylcholine, and butyrylcholinesterase of unknown function.
12869558	5	39	theme	truncated	754:762	arg1	complexes					775:783	several recombinant truncated human BChE complexes	734:783	several recombinant truncated human BChE complexes	734:783	Here we report the crystal structures of several recombinant truncated human BChE complexes and conjugates and provide a description for mechanistically relevant non-productive substrate and product binding.
12869558	6	40	theme	Torpedo	1030:1036	arg1	acetylcholinesterase					1038:1057	Torpedo acetylcholinesterase	1030:1057	Torpedo acetylcholinesterase	1030:1057	As expected, the structure of BChE is similar to a previously published theoretical model of this enzyme and to the structure of Torpedo acetylcholinesterase.
12869558	2	41	theme	neurotransmitter	249:264	arg1	acetylcholine					266:278	the neurotransmitter acetylcholine	245:278	the neurotransmitter acetylcholine	245:278	They are divided into two groups: acetylcholinesterase, involved in the hydrolysis of the neurotransmitter acetylcholine, and butyrylcholinesterase of unknown function.
12869558	1	42	theme	efficient	134:142	arg1	enzymes					144:150	the most efficient enzymes	125:150	the most efficient enzymes known	125:156	Cholinesterases are among the most efficient enzymes known.
12869558	2	43	dep	groups	185:190	arg1	butyrylcholinesterase					285:305	butyrylcholinesterase	285:305	butyrylcholinesterase of unknown function	285:325	They are divided into two groups: acetylcholinesterase, involved in the hydrolysis of the neurotransmitter acetylcholine, and butyrylcholinesterase of unknown function.
12869558	2	43	dep	groups	185:190	arg1	acetylcholinesterase					193:212	acetylcholinesterase	193:212	acetylcholinesterase	193:212	They are divided into two groups: acetylcholinesterase, involved in the hydrolysis of the neurotransmitter acetylcholine, and butyrylcholinesterase of unknown function.
12869558	2	43	dep	groups	185:190	arg1	groups					185:190	two groups	181:190	two groups: acetylcholinesterase, involved in the hydrolysis of the neurotransmitter acetylcholine, and butyrylcholinesterase of unknown function	181:325	They are divided into two groups: acetylcholinesterase, involved in the hydrolysis of the neurotransmitter acetylcholine, and butyrylcholinesterase of unknown function.
12869558	5	44	theme	recombinant	742:752	arg1	complexes					775:783	several recombinant truncated human BChE complexes	734:783	several recombinant truncated human BChE complexes	734:783	Here we report the crystal structures of several recombinant truncated human BChE complexes and conjugates and provide a description for mechanistically relevant non-productive substrate and product binding.
12869558	5	45	theme	substrate	870:878	arg1	binding					892:898	mechanistically relevant non-productive substrate and product binding	830:898	mechanistically relevant non-productive substrate and product binding	830:898	Here we report the crystal structures of several recombinant truncated human BChE complexes and conjugates and provide a description for mechanistically relevant non-productive substrate and product binding.
12869558	4	46	theme	nerve	679:683	arg1	agents					685:690	nerve agents	679:690	nerve agents	679:690	Human butyrylcholinesterase (BChE) has attracted attention because it can hydrolyze toxic esters such as cocaine or scavenge organophosphorus pesticides and nerve agents.
12869558	4	47	theme	toxic	606:610	arg1	esters					612:617	toxic esters	606:617	toxic esters such as cocaine	606:633	Human butyrylcholinesterase (BChE) has attracted attention because it can hydrolyze toxic esters such as cocaine or scavenge organophosphorus pesticides and nerve agents.
12869558	4	47	theme	toxic	606:610	arg1	cocaine					627:633	cocaine	627:633	cocaine	627:633	Human butyrylcholinesterase (BChE) has attracted attention because it can hydrolyze toxic esters such as cocaine or scavenge organophosphorus pesticides and nerve agents.
12869558	0	48	theme	complexes	60:68	arg1	structure					8:16	Crystal structure	0:16	Crystal structure of human butyrylcholinesterase and of its complexes with substrate and products	0:96	Crystal structure of human butyrylcholinesterase and of its complexes with substrate and products.
12869558	5	49	dep	relevant	846:853	arg1	non-productive					855:868	non-productive	855:868	non-productive	855:868	Here we report the crystal structures of several recombinant truncated human BChE complexes and conjugates and provide a description for mechanistically relevant non-productive substrate and product binding.
12869558	8	50	theme	bound	1304:1308	arg1	butyrate					1310:1317	bound butyrate	1304:1317	bound butyrate	1304:1317	An electron density peak close to the catalytic Ser(198) has been modeled as bound butyrate.
12869558	8	50	theme	bound	1304:1308	arg1	peak					1247:1250	An electron density peak	1227:1250	An electron density peak close to the catalytic Ser(198)	1227:1282	An electron density peak close to the catalytic Ser(198) has been modeled as bound butyrate.
12869558	7	51	located	found	1150:1154	arg1	bigger					1205:1210	bigger	1205:1210	bigger	1205:1210	The main difference between the experimentally determined BChE structure and its model is found at the acyl binding pocket that is significantly bigger than expected.
12869558	7	51	located	found	1150:1154	arg2	difference					1069:1078	The main difference	1060:1078	The main difference between the experimentally determined BChE structure and its model	1060:1145	The main difference between the experimentally determined BChE structure and its model is found at the acyl binding pocket that is significantly bigger than expected.
12869558	7	51	located	found	1150:1154	arg1	pocket					1176:1181	the acyl binding pocket	1159:1181	the acyl binding pocket that is significantly bigger than expected	1159:1224	The main difference between the experimentally determined BChE structure and its model is found at the acyl binding pocket that is significantly bigger than expected.
17768338	7	0	theme	first	1188:1192	arg1	time					1194:1197	the first time	1184:1197	the first time	1184:1197	Towards these ends, full-length monomeric recombinant BChE has been crystallized for the first time.
17768338	5	1	theme	recombinant	628:638	arg1	BChE					640:643	Full-length recombinant BChE	616:643	Full-length recombinant BChE produced in Chinese hamster ovary (CHO) cells or human embryonic kidney cells	616:721	Full-length recombinant BChE produced in Chinese hamster ovary (CHO) cells or human embryonic kidney cells has been shown to associate as monomers, with a shorter circulatory residence time than the naturally occurring tetrameric serum protein.
17768338	1	2	theme	endogenous	160:169	arg1	butyrylcholinesterase					98:118	Human butyrylcholinesterase	92:118	Human butyrylcholinesterase (BChE)	92:125	Human butyrylcholinesterase (BChE) has been shown to function as an endogenous scavenger of diverse poisons.
17768338	1	2	theme	endogenous	160:169	arg1	scavenger					171:179	an endogenous scavenger	157:179	an endogenous scavenger of diverse poisons	157:198	Human butyrylcholinesterase (BChE) has been shown to function as an endogenous scavenger of diverse poisons.
17768338	6	3	theme	mass	965:968	arg1	production					970:979	the mass production	961:979	the mass production of therapeutic recombinant BChE	961:1011	Based on the preceding observation as well as the need to develop novel methodologies to facilitate the mass production of therapeutic recombinant BChE, studies have been initiated to determine the structural basis of tetramer formation.
17768338	6	4	theme	preceding	874:882	arg1	observation					884:894	the preceding observation	870:894	the preceding observation	870:894	Based on the preceding observation as well as the need to develop novel methodologies to facilitate the mass production of therapeutic recombinant BChE, studies have been initiated to determine the structural basis of tetramer formation.
17768338	3	5	theme	documented	317:326	arg1	effects					340:346	The well documented therapeutic effects	308:346	The well documented therapeutic effects of BChE on cocaine toxicity and organophosphorus agent poisoning	308:411	The well documented therapeutic effects of BChE on cocaine toxicity and organophosphorus agent poisoning has increased the need for effective methods of producing recombinant therapeutic BChE.
17768338	4	6	contain	have	550:553	arg2	time					584:587	a long circulatory residence time	555:587	a long circulatory residence time	555:587	In order to be therapeutically useful, BChE must have a long circulatory residence time or associate as tetramers.
17768338	4	6	contain	have	550:553	arg1	BChE					540:543	BChE	540:543	BChE	540:543	In order to be therapeutically useful, BChE must have a long circulatory residence time or associate as tetramers.
17768338	4	7	theme	circulatory	562:572	arg1	time					584:587	a long circulatory residence time	555:587	a long circulatory residence time	555:587	In order to be therapeutically useful, BChE must have a long circulatory residence time or associate as tetramers.
17768338	3	8	theme	therapeutic	328:338	arg1	effects					340:346	The well documented therapeutic effects	308:346	The well documented therapeutic effects of BChE on cocaine toxicity and organophosphorus agent poisoning	308:411	The well documented therapeutic effects of BChE on cocaine toxicity and organophosphorus agent poisoning has increased the need for effective methods of producing recombinant therapeutic BChE.
17768338	3	9	from	effects	340:346	arg1	toxicity					367:374	cocaine toxicity	359:374	cocaine toxicity	359:374	The well documented therapeutic effects of BChE on cocaine toxicity and organophosphorus agent poisoning has increased the need for effective methods of producing recombinant therapeutic BChE.
17768338	3	9	from	effects	340:346	arg1	poisoning					403:411	organophosphorus agent poisoning	380:411	organophosphorus agent poisoning	380:411	The well documented therapeutic effects of BChE on cocaine toxicity and organophosphorus agent poisoning has increased the need for effective methods of producing recombinant therapeutic BChE.
17768338	8	10	theme	unit-cell	1264:1272	arg1	parameters					1274:1283	unit-cell parameters	1264:1283	unit-cell parameters a = b = 156, c = 146 A	1264:1306	A 2.8 A X-ray structure was solved in space group P42(1)2, with unit-cell parameters a = b = 156, c = 146 A.
17768338	3	11	theme	therapeutic	483:493	arg1	BChE					495:498	recombinant therapeutic BChE	471:498	recombinant therapeutic BChE	471:498	The well documented therapeutic effects of BChE on cocaine toxicity and organophosphorus agent poisoning has increased the need for effective methods of producing recombinant therapeutic BChE.
17768338	4	12	theme	long	557:560	arg1	time					584:587	a long circulatory residence time	555:587	a long circulatory residence time	555:587	In order to be therapeutically useful, BChE must have a long circulatory residence time or associate as tetramers.
17768338	5	13	theme	kidney	710:715	arg1	cells					717:721	human embryonic kidney cells	694:721	human embryonic kidney cells	694:721	Full-length recombinant BChE produced in Chinese hamster ovary (CHO) cells or human embryonic kidney cells has been shown to associate as monomers, with a shorter circulatory residence time than the naturally occurring tetrameric serum protein.
17768338	6	14	theme	structural	1059:1068	arg1	basis					1070:1074	the structural basis	1055:1074	the structural basis of tetramer formation	1055:1096	Based on the preceding observation as well as the need to develop novel methodologies to facilitate the mass production of therapeutic recombinant BChE, studies have been initiated to determine the structural basis of tetramer formation.
17768338	1	15	theme	Human	92:96	arg1	BChE					121:124	BChE	121:124	BChE	121:124	Human butyrylcholinesterase (BChE) has been shown to function as an endogenous scavenger of diverse poisons.
17768338	1	15	theme	Human	92:96	arg1	butyrylcholinesterase					98:118	Human butyrylcholinesterase	92:118	Human butyrylcholinesterase (BChE)	92:125	Human butyrylcholinesterase (BChE) has been shown to function as an endogenous scavenger of diverse poisons.
17768338	1	15	theme	Human	92:96	arg1	scavenger					171:179	an endogenous scavenger	157:179	an endogenous scavenger of diverse poisons	157:198	Human butyrylcholinesterase (BChE) has been shown to function as an endogenous scavenger of diverse poisons.
17768338	3	16	theme	agent	397:401	arg1	poisoning					403:411	organophosphorus agent poisoning	380:411	organophosphorus agent poisoning	380:411	The well documented therapeutic effects of BChE on cocaine toxicity and organophosphorus agent poisoning has increased the need for effective methods of producing recombinant therapeutic BChE.
17768338	8	17	theme	A	1206:1206	arg1	structure					1214:1222	A 2.8 A X-ray structure	1200:1222	A 2.8 A X-ray structure	1200:1222	A 2.8 A X-ray structure was solved in space group P42(1)2, with unit-cell parameters a = b = 156, c = 146 A.
17768338	0	18	theme	full-length	39:49	arg1	butyrylcholinesterase					69:89	full-length recombinant human butyrylcholinesterase	39:89	full-length recombinant human butyrylcholinesterase	39:89	Crystallization and X-ray structure of full-length recombinant human butyrylcholinesterase.
17768338	6	19	theme	therapeutic	984:994	arg1	BChE					1008:1011	therapeutic recombinant BChE	984:1011	therapeutic recombinant BChE	984:1011	Based on the preceding observation as well as the need to develop novel methodologies to facilitate the mass production of therapeutic recombinant BChE, studies have been initiated to determine the structural basis of tetramer formation.
17768338	1	20	theme	diverse	184:190	arg1	poisons					192:198	diverse poisons	184:198	diverse poisons	184:198	Human butyrylcholinesterase (BChE) has been shown to function as an endogenous scavenger of diverse poisons.
17768338	3	21	theme	BChE	351:354	arg1	effects					340:346	The well documented therapeutic effects	308:346	The well documented therapeutic effects of BChE on cocaine toxicity and organophosphorus agent poisoning	308:411	The well documented therapeutic effects of BChE on cocaine toxicity and organophosphorus agent poisoning has increased the need for effective methods of producing recombinant therapeutic BChE.
17768338	8	22	dep	146	1302:1304	arg1	A					1306:1306	A	1306:1306	A	1306:1306	A 2.8 A X-ray structure was solved in space group P42(1)2, with unit-cell parameters a = b = 156, c = 146 A.
17768338	2	23	theme	l	301:301	arg1	concentration					279:291	a concentration	277:291	a concentration of 5 mg l(-1)	277:305	BChE is a 340 kDa tetrameric glycoprotein that is present in human serum at a concentration of 5 mg l(-1).
17768338	1	24	theme	poisons	192:198	arg1	butyrylcholinesterase					98:118	Human butyrylcholinesterase	92:118	Human butyrylcholinesterase (BChE)	92:125	Human butyrylcholinesterase (BChE) has been shown to function as an endogenous scavenger of diverse poisons.
17768338	1	24	theme	poisons	192:198	arg1	scavenger					171:179	an endogenous scavenger	157:179	an endogenous scavenger of diverse poisons	157:198	Human butyrylcholinesterase (BChE) has been shown to function as an endogenous scavenger of diverse poisons.
17768338	7	25	theme	full-length	1119:1129	arg1	BChE					1153:1156	full-length monomeric recombinant BChE	1119:1156	full-length monomeric recombinant BChE	1119:1156	Towards these ends, full-length monomeric recombinant BChE has been crystallized for the first time.
17768338	5	26	theme	Full-length	616:626	arg1	BChE					640:643	Full-length recombinant BChE	616:643	Full-length recombinant BChE produced in Chinese hamster ovary (CHO) cells or human embryonic kidney cells	616:721	Full-length recombinant BChE produced in Chinese hamster ovary (CHO) cells or human embryonic kidney cells has been shown to associate as monomers, with a shorter circulatory residence time than the naturally occurring tetrameric serum protein.
17768338	2	27	theme	mg	298:299	arg1	-1					303:304	-1	303:304	-1	303:304	BChE is a 340 kDa tetrameric glycoprotein that is present in human serum at a concentration of 5 mg l(-1).
17768338	2	27	theme	mg	298:299	arg1	l					301:301	5 mg l	296:301	5 mg l(-1)	296:305	BChE is a 340 kDa tetrameric glycoprotein that is present in human serum at a concentration of 5 mg l(-1).
17768338	2	28	from	present	251:257	arg1	serum					268:272	human serum	262:272	human serum	262:272	BChE is a 340 kDa tetrameric glycoprotein that is present in human serum at a concentration of 5 mg l(-1).
17768338	5	29	theme	serum	846:850	arg1	protein					852:858	the naturally occurring tetrameric serum protein	811:858	the naturally occurring tetrameric serum protein	811:858	Full-length recombinant BChE produced in Chinese hamster ovary (CHO) cells or human embryonic kidney cells has been shown to associate as monomers, with a shorter circulatory residence time than the naturally occurring tetrameric serum protein.
17768338	5	30	theme	shorter	771:777	arg1	time					801:804	a shorter circulatory residence time	769:804	a shorter circulatory residence time than the naturally occurring tetrameric serum protein	769:858	Full-length recombinant BChE produced in Chinese hamster ovary (CHO) cells or human embryonic kidney cells has been shown to associate as monomers, with a shorter circulatory residence time than the naturally occurring tetrameric serum protein.
17768338	6	31	theme	novel	927:931	arg1	methodologies					933:945	novel methodologies	927:945	novel methodologies	927:945	Based on the preceding observation as well as the need to develop novel methodologies to facilitate the mass production of therapeutic recombinant BChE, studies have been initiated to determine the structural basis of tetramer formation.
17768338	5	32	theme	CHO	680:682	arg1	cells					685:689	Chinese hamster ovary (CHO) cells	657:689	Chinese hamster ovary (CHO) cells	657:689	Full-length recombinant BChE produced in Chinese hamster ovary (CHO) cells or human embryonic kidney cells has been shown to associate as monomers, with a shorter circulatory residence time than the naturally occurring tetrameric serum protein.
17768338	5	33	theme	residence	791:799	arg1	time					801:804	a shorter circulatory residence time	769:804	a shorter circulatory residence time than the naturally occurring tetrameric serum protein	769:858	Full-length recombinant BChE produced in Chinese hamster ovary (CHO) cells or human embryonic kidney cells has been shown to associate as monomers, with a shorter circulatory residence time than the naturally occurring tetrameric serum protein.
17768338	0	34	theme	X-ray	20:24	arg1	structure					26:34	X-ray structure	20:34	X-ray structure	20:34	Crystallization and X-ray structure of full-length recombinant human butyrylcholinesterase.
17768338	8	35	theme	=	1287:1287	arg1	156					1293:1295	a = b = 156	1285:1295	a = b = 156	1285:1295	A 2.8 A X-ray structure was solved in space group P42(1)2, with unit-cell parameters a = b = 156, c = 146 A.
17768338	8	36	theme	=	1291:1291	arg1	156					1293:1295	a = b = 156	1285:1295	a = b = 156	1285:1295	A 2.8 A X-ray structure was solved in space group P42(1)2, with unit-cell parameters a = b = 156, c = 146 A.
17768338	3	37	theme	effective	440:448	arg1	methods					450:456	effective methods	440:456	effective methods of producing recombinant therapeutic BChE	440:498	The well documented therapeutic effects of BChE on cocaine toxicity and organophosphorus agent poisoning has increased the need for effective methods of producing recombinant therapeutic BChE.
17768338	2	38	gly	glycoprotein	230:241	arg1	glycoprotein					230:241	a 340 kDa tetrameric glycoprotein	209:241	a 340 kDa tetrameric glycoprotein that is present in human serum at a concentration of 5 mg l(-1)	209:305	BChE is a 340 kDa tetrameric glycoprotein that is present in human serum at a concentration of 5 mg l(-1).
17768338	2	38	gly	glycoprotein	230:241	arg1	present					251:257	present	251:257	present	251:257	BChE is a 340 kDa tetrameric glycoprotein that is present in human serum at a concentration of 5 mg l(-1).
17768338	2	38	gly	glycoprotein	230:241	arg1	BChE					201:204	BChE	201:204	BChE	201:204	BChE is a 340 kDa tetrameric glycoprotein that is present in human serum at a concentration of 5 mg l(-1).
17768338	8	39	dep	parameters	1274:1283	arg1	156					1293:1295	a = b = 156	1285:1295	a = b = 156	1285:1295	A 2.8 A X-ray structure was solved in space group P42(1)2, with unit-cell parameters a = b = 156, c = 146 A.
17768338	8	40	theme	X-ray	1208:1212	arg1	structure					1214:1222	A 2.8 A X-ray structure	1200:1222	A 2.8 A X-ray structure	1200:1222	A 2.8 A X-ray structure was solved in space group P42(1)2, with unit-cell parameters a = b = 156, c = 146 A.
17768338	8	41	theme	space	1238:1242	arg1	group					1244:1248	space group P42(1)2	1238:1256	space group P42(1)2	1238:1256	A 2.8 A X-ray structure was solved in space group P42(1)2, with unit-cell parameters a = b = 156, c = 146 A.
17768338	3	42	theme	organophosphorus	380:395	arg1	poisoning					403:411	organophosphorus agent poisoning	380:411	organophosphorus agent poisoning	380:411	The well documented therapeutic effects of BChE on cocaine toxicity and organophosphorus agent poisoning has increased the need for effective methods of producing recombinant therapeutic BChE.
17768338	5	43	theme	tetrameric	835:844	arg1	protein					852:858	the naturally occurring tetrameric serum protein	811:858	the naturally occurring tetrameric serum protein	811:858	Full-length recombinant BChE produced in Chinese hamster ovary (CHO) cells or human embryonic kidney cells has been shown to associate as monomers, with a shorter circulatory residence time than the naturally occurring tetrameric serum protein.
17768338	5	44	theme	embryonic	700:708	arg1	kidney					710:715	human embryonic kidney	694:715	human embryonic kidney cells	694:721	Full-length recombinant BChE produced in Chinese hamster ovary (CHO) cells or human embryonic kidney cells has been shown to associate as monomers, with a shorter circulatory residence time than the naturally occurring tetrameric serum protein.
17768338	7	45	theme	monomeric	1131:1139	arg1	BChE					1153:1156	full-length monomeric recombinant BChE	1119:1156	full-length monomeric recombinant BChE	1119:1156	Towards these ends, full-length monomeric recombinant BChE has been crystallized for the first time.
17768338	6	46	theme	BChE	1008:1011	arg1	production					970:979	the mass production	961:979	the mass production of therapeutic recombinant BChE	961:1011	Based on the preceding observation as well as the need to develop novel methodologies to facilitate the mass production of therapeutic recombinant BChE, studies have been initiated to determine the structural basis of tetramer formation.
17768338	3	47	theme	cocaine	359:365	arg1	toxicity					367:374	cocaine toxicity	359:374	cocaine toxicity	359:374	The well documented therapeutic effects of BChE on cocaine toxicity and organophosphorus agent poisoning has increased the need for effective methods of producing recombinant therapeutic BChE.
17768338	5	48	theme	human	694:698	arg1	kidney					710:715	human embryonic kidney	694:715	human embryonic kidney cells	694:721	Full-length recombinant BChE produced in Chinese hamster ovary (CHO) cells or human embryonic kidney cells has been shown to associate as monomers, with a shorter circulatory residence time than the naturally occurring tetrameric serum protein.
17768338	5	49	theme	Chinese	657:663	arg1	cells					685:689	Chinese hamster ovary (CHO) cells	657:689	Chinese hamster ovary (CHO) cells	657:689	Full-length recombinant BChE produced in Chinese hamster ovary (CHO) cells or human embryonic kidney cells has been shown to associate as monomers, with a shorter circulatory residence time than the naturally occurring tetrameric serum protein.
17768338	0	50	theme	butyrylcholinesterase	69:89	arg1	Crystallization					0:14	Crystallization	0:14	Crystallization	0:14	Crystallization and X-ray structure of full-length recombinant human butyrylcholinesterase.
17768338	0	50	theme	butyrylcholinesterase	69:89	arg1	structure					26:34	X-ray structure	20:34	X-ray structure	20:34	Crystallization and X-ray structure of full-length recombinant human butyrylcholinesterase.
17768338	2	51	theme	tetrameric	219:228	arg1	glycoprotein					230:241	a 340 kDa tetrameric glycoprotein	209:241	a 340 kDa tetrameric glycoprotein that is present in human serum at a concentration of 5 mg l(-1)	209:305	BChE is a 340 kDa tetrameric glycoprotein that is present in human serum at a concentration of 5 mg l(-1).
17768338	2	51	theme	tetrameric	219:228	arg1	present					251:257	present	251:257	present	251:257	BChE is a 340 kDa tetrameric glycoprotein that is present in human serum at a concentration of 5 mg l(-1).
17768338	2	51	theme	tetrameric	219:228	arg1	BChE					201:204	BChE	201:204	BChE	201:204	BChE is a 340 kDa tetrameric glycoprotein that is present in human serum at a concentration of 5 mg l(-1).
17768338	8	52	theme	b	1289:1289	arg1	156					1293:1295	a = b = 156	1285:1295	a = b = 156	1285:1295	A 2.8 A X-ray structure was solved in space group P42(1)2, with unit-cell parameters a = b = 156, c = 146 A.
17768338	0	53	theme	recombinant	51:61	arg1	butyrylcholinesterase					69:89	full-length recombinant human butyrylcholinesterase	39:89	full-length recombinant human butyrylcholinesterase	39:89	Crystallization and X-ray structure of full-length recombinant human butyrylcholinesterase.
17768338	5	54	theme	hamster	665:671	arg1	cells					685:689	Chinese hamster ovary (CHO) cells	657:689	Chinese hamster ovary (CHO) cells	657:689	Full-length recombinant BChE produced in Chinese hamster ovary (CHO) cells or human embryonic kidney cells has been shown to associate as monomers, with a shorter circulatory residence time than the naturally occurring tetrameric serum protein.
17768338	2	55	theme	340	211:213	arg1	kDa					215:217	kDa	215:217	kDa	215:217	BChE is a 340 kDa tetrameric glycoprotein that is present in human serum at a concentration of 5 mg l(-1).
17768338	2	56	theme	kDa	215:217	arg1	glycoprotein					230:241	a 340 kDa tetrameric glycoprotein	209:241	a 340 kDa tetrameric glycoprotein that is present in human serum at a concentration of 5 mg l(-1)	209:305	BChE is a 340 kDa tetrameric glycoprotein that is present in human serum at a concentration of 5 mg l(-1).
17768338	2	56	theme	kDa	215:217	arg1	present					251:257	present	251:257	present	251:257	BChE is a 340 kDa tetrameric glycoprotein that is present in human serum at a concentration of 5 mg l(-1).
17768338	2	56	theme	kDa	215:217	arg1	BChE					201:204	BChE	201:204	BChE	201:204	BChE is a 340 kDa tetrameric glycoprotein that is present in human serum at a concentration of 5 mg l(-1).
17768338	3	57	theme	recombinant	471:481	arg1	BChE					495:498	recombinant therapeutic BChE	471:498	recombinant therapeutic BChE	471:498	The well documented therapeutic effects of BChE on cocaine toxicity and organophosphorus agent poisoning has increased the need for effective methods of producing recombinant therapeutic BChE.
17768338	5	58	theme	ovary	673:677	arg1	cells					685:689	Chinese hamster ovary (CHO) cells	657:689	Chinese hamster ovary (CHO) cells	657:689	Full-length recombinant BChE produced in Chinese hamster ovary (CHO) cells or human embryonic kidney cells has been shown to associate as monomers, with a shorter circulatory residence time than the naturally occurring tetrameric serum protein.
17768338	8	59	dep	156	1293:1295	arg1	=					1300:1300	=	1300:1300	=	1300:1300	A 2.8 A X-ray structure was solved in space group P42(1)2, with unit-cell parameters a = b = 156, c = 146 A.
17768338	2	60	theme	human	262:266	arg1	serum					268:272	human serum	262:272	human serum	262:272	BChE is a 340 kDa tetrameric glycoprotein that is present in human serum at a concentration of 5 mg l(-1).
17768338	6	61	theme	formation	1088:1096	arg1	basis					1070:1074	the structural basis	1055:1074	the structural basis of tetramer formation	1055:1096	Based on the preceding observation as well as the need to develop novel methodologies to facilitate the mass production of therapeutic recombinant BChE, studies have been initiated to determine the structural basis of tetramer formation.
17768338	2	62	from	serum	268:272	arg1	glycoprotein					230:241	a 340 kDa tetrameric glycoprotein	209:241	a 340 kDa tetrameric glycoprotein that is present in human serum at a concentration of 5 mg l(-1)	209:305	BChE is a 340 kDa tetrameric glycoprotein that is present in human serum at a concentration of 5 mg l(-1).
17768338	2	62	from	serum	268:272	arg1	present					251:257	present	251:257	present	251:257	BChE is a 340 kDa tetrameric glycoprotein that is present in human serum at a concentration of 5 mg l(-1).
17768338	2	62	from	serum	268:272	arg1	BChE					201:204	BChE	201:204	BChE	201:204	BChE is a 340 kDa tetrameric glycoprotein that is present in human serum at a concentration of 5 mg l(-1).
17768338	6	63	theme	recombinant	996:1006	arg1	BChE					1008:1011	therapeutic recombinant BChE	984:1011	therapeutic recombinant BChE	984:1011	Based on the preceding observation as well as the need to develop novel methodologies to facilitate the mass production of therapeutic recombinant BChE, studies have been initiated to determine the structural basis of tetramer formation.
17768338	5	64	theme	circulatory	779:789	arg1	time					801:804	a shorter circulatory residence time	769:804	a shorter circulatory residence time than the naturally occurring tetrameric serum protein	769:858	Full-length recombinant BChE produced in Chinese hamster ovary (CHO) cells or human embryonic kidney cells has been shown to associate as monomers, with a shorter circulatory residence time than the naturally occurring tetrameric serum protein.
17768338	6	65	theme	tetramer	1079:1086	arg1	formation					1088:1096	tetramer formation	1079:1096	tetramer formation	1079:1096	Based on the preceding observation as well as the need to develop novel methodologies to facilitate the mass production of therapeutic recombinant BChE, studies have been initiated to determine the structural basis of tetramer formation.
17768338	2	66	from	concentration	279:291	arg1	glycoprotein					230:241	a 340 kDa tetrameric glycoprotein	209:241	a 340 kDa tetrameric glycoprotein that is present in human serum at a concentration of 5 mg l(-1)	209:305	BChE is a 340 kDa tetrameric glycoprotein that is present in human serum at a concentration of 5 mg l(-1).
17768338	2	66	from	concentration	279:291	arg1	present					251:257	present	251:257	present	251:257	BChE is a 340 kDa tetrameric glycoprotein that is present in human serum at a concentration of 5 mg l(-1).
17768338	2	66	from	concentration	279:291	arg1	BChE					201:204	BChE	201:204	BChE	201:204	BChE is a 340 kDa tetrameric glycoprotein that is present in human serum at a concentration of 5 mg l(-1).
17768338	4	67	theme	residence	574:582	arg1	time					584:587	a long circulatory residence time	555:587	a long circulatory residence time	555:587	In order to be therapeutically useful, BChE must have a long circulatory residence time or associate as tetramers.
17768338	5	68	theme	occurring	825:833	arg1	protein					852:858	the naturally occurring tetrameric serum protein	811:858	the naturally occurring tetrameric serum protein	811:858	Full-length recombinant BChE produced in Chinese hamster ovary (CHO) cells or human embryonic kidney cells has been shown to associate as monomers, with a shorter circulatory residence time than the naturally occurring tetrameric serum protein.
17768338	0	69	theme	human	63:67	arg1	butyrylcholinesterase					69:89	full-length recombinant human butyrylcholinesterase	39:89	full-length recombinant human butyrylcholinesterase	39:89	Crystallization and X-ray structure of full-length recombinant human butyrylcholinesterase.
17768338	2	70	attach	present	251:257	arg1	serum					268:272	human serum	262:272	human serum	262:272	BChE is a 340 kDa tetrameric glycoprotein that is present in human serum at a concentration of 5 mg l(-1).
17768338	2	70	attach	present	251:257	arg1	concentration					279:291	a concentration	277:291	a concentration of 5 mg l(-1)	277:305	BChE is a 340 kDa tetrameric glycoprotein that is present in human serum at a concentration of 5 mg l(-1).
17768338	2	70	attach	present	251:257	arg2	BChE					201:204	BChE	201:204	BChE	201:204	BChE is a 340 kDa tetrameric glycoprotein that is present in human serum at a concentration of 5 mg l(-1).
17768338	2	70	attach	present	251:257	arg2	present					251:257	present	251:257	present	251:257	BChE is a 340 kDa tetrameric glycoprotein that is present in human serum at a concentration of 5 mg l(-1).
17768338	2	70	attach	present	251:257	arg2	glycoprotein					230:241	a 340 kDa tetrameric glycoprotein	209:241	a 340 kDa tetrameric glycoprotein that is present in human serum at a concentration of 5 mg l(-1)	209:305	BChE is a 340 kDa tetrameric glycoprotein that is present in human serum at a concentration of 5 mg l(-1).
17768338	7	71	theme	recombinant	1141:1151	arg1	BChE					1153:1156	full-length monomeric recombinant BChE	1119:1156	full-length monomeric recombinant BChE	1119:1156	Towards these ends, full-length monomeric recombinant BChE has been crystallized for the first time.
17768338	2	72	located	present	251:257	arg1	serum					268:272	human serum	262:272	human serum	262:272	BChE is a 340 kDa tetrameric glycoprotein that is present in human serum at a concentration of 5 mg l(-1).
17768338	2	72	located	present	251:257	arg1	concentration					279:291	a concentration	277:291	a concentration of 5 mg l(-1)	277:305	BChE is a 340 kDa tetrameric glycoprotein that is present in human serum at a concentration of 5 mg l(-1).
17768338	2	72	located	present	251:257	arg2	BChE					201:204	BChE	201:204	BChE	201:204	BChE is a 340 kDa tetrameric glycoprotein that is present in human serum at a concentration of 5 mg l(-1).
17768338	2	72	located	present	251:257	arg2	present					251:257	present	251:257	present	251:257	BChE is a 340 kDa tetrameric glycoprotein that is present in human serum at a concentration of 5 mg l(-1).
17768338	2	72	located	present	251:257	arg2	glycoprotein					230:241	a 340 kDa tetrameric glycoprotein	209:241	a 340 kDa tetrameric glycoprotein that is present in human serum at a concentration of 5 mg l(-1)	209:305	BChE is a 340 kDa tetrameric glycoprotein that is present in human serum at a concentration of 5 mg l(-1).
23679855	4	0	theme	key	920:922	arg1	interactions					924:935	key interactions	920:935	key interactions	920:935	Huprine W in hAChE and tacrine in hBChE reside in strikingly similar positions highlighting the conservation of key interactions, namely, π-π/cation-π interactions with Trp86 (Trp82), and hydrogen bonding with the main chain carbonyl of the catalytic histidine residue.
23679855	5	1	theme	hydrophobic	1465:1475	arg1	pocket					1477:1482	a hydrophobic pocket	1463:1482	a hydrophobic pocket interacting strongly with Trp439	1463:1515	Huprine W forms additional interactions with hAChE, which explains its superior affinity: the isoquinoline moiety is associated with a group of aromatic residues (Tyr337, Phe338 and Phe295 not present in hBChE) in addition to Trp86; the hydroxyl group is hydrogen bonded to both the catalytic serine residue and residues in the oxyanion hole; and the chlorine substituent is nested in a hydrophobic pocket interacting strongly with Trp439.
23679855	5	2	theme	catalytic	1361:1369	arg1	residue					1378:1384	the catalytic serine residue	1357:1384	the catalytic serine residue	1357:1384	Huprine W forms additional interactions with hAChE, which explains its superior affinity: the isoquinoline moiety is associated with a group of aromatic residues (Tyr337, Phe338 and Phe295 not present in hBChE) in addition to Trp86; the hydroxyl group is hydrogen bonded to both the catalytic serine residue and residues in the oxyanion hole; and the chlorine substituent is nested in a hydrophobic pocket interacting strongly with Trp439.
23679855	5	3	theme	Huprine	1078:1084	arg1	W					1086:1086	Huprine W	1078:1086	Huprine W	1078:1086	Huprine W forms additional interactions with hAChE, which explains its superior affinity: the isoquinoline moiety is associated with a group of aromatic residues (Tyr337, Phe338 and Phe295 not present in hBChE) in addition to Trp86; the hydroxyl group is hydrogen bonded to both the catalytic serine residue and residues in the oxyanion hole; and the chlorine substituent is nested in a hydrophobic pocket interacting strongly with Trp439.
23679855	6	4	from	pocket	1530:1535	arg1	hBChE					1540:1544	hBChE	1540:1544	hBChE	1540:1544	There is no pocket in hBChE that is able to accommodate the chlorine substituent.
23679855	5	5	theme	isoquinoline	1172:1183	arg1	moiety					1185:1190	the isoquinoline moiety	1168:1190	the isoquinoline moiety	1168:1190	Huprine W forms additional interactions with hAChE, which explains its superior affinity: the isoquinoline moiety is associated with a group of aromatic residues (Tyr337, Phe338 and Phe295 not present in hBChE) in addition to Trp86; the hydroxyl group is hydrogen bonded to both the catalytic serine residue and residues in the oxyanion hole; and the chlorine substituent is nested in a hydrophobic pocket interacting strongly with Trp439.
23679855	1	6	theme	multitarget-directed	247:266	arg1	MTDLs					240:244	MTDLs	240:244	MTDLs (multitarget-directed ligands)	240:275	The multifunctional nature of Alzheimer's disease calls for MTDLs (multitarget-directed ligands) to act on different components of the pathology, like the cholinergic dysfunction and amyloid aggregation.
23679855	1	6	theme	multitarget-directed	247:266	arg1	ligands					268:274	multitarget-directed ligands	247:274	multitarget-directed ligands	247:274	The multifunctional nature of Alzheimer's disease calls for MTDLs (multitarget-directed ligands) to act on different components of the pathology, like the cholinergic dysfunction and amyloid aggregation.
23679855	1	7	theme	cholinergic	335:345	arg1	dysfunction					347:357	the cholinergic dysfunction	331:357	the cholinergic dysfunction	331:357	The multifunctional nature of Alzheimer's disease calls for MTDLs (multitarget-directed ligands) to act on different components of the pathology, like the cholinergic dysfunction and amyloid aggregation.
23679855	2	8	dep	tacrine	455:461	arg1	e.g.					450:453	e.g.	450:453	e.g.	450:453	Such MTDLs are usually on the basis of cholinesterase inhibitors (e.g. tacrine or huprine) coupled with another active molecule aimed at a different target.
23679855	5	9	theme	hydroxyl	1315:1322	arg1	group					1324:1328	the hydroxyl group	1311:1328	the hydroxyl group	1311:1328	Huprine W forms additional interactions with hAChE, which explains its superior affinity: the isoquinoline moiety is associated with a group of aromatic residues (Tyr337, Phe338 and Phe295 not present in hBChE) in addition to Trp86; the hydroxyl group is hydrogen bonded to both the catalytic serine residue and residues in the oxyanion hole; and the chlorine substituent is nested in a hydrophobic pocket interacting strongly with Trp439.
23679855	5	9	theme	hydroxyl	1315:1322	arg1	bonded					1342:1347	bonded	1342:1347	bonded	1342:1347	Huprine W forms additional interactions with hAChE, which explains its superior affinity: the isoquinoline moiety is associated with a group of aromatic residues (Tyr337, Phe338 and Phe295 not present in hBChE) in addition to Trp86; the hydroxyl group is hydrogen bonded to both the catalytic serine residue and residues in the oxyanion hole; and the chlorine substituent is nested in a hydrophobic pocket interacting strongly with Trp439.
23679855	3	10	from	structures	600:609	arg1	complex					786:792	complex	786:792	complex with tacrine	786:805	To aid in the design of these MTDLs, we report the crystal structures of hAChE (human acetylcholinesterase) in complex with FAS-2 (fasciculin 2) and a hydroxylated derivative of huprine (huprine W), and of hBChE (human butyrylcholinesterase) in complex with tacrine.
23679855	3	10	from	structures	600:609	arg1	complex					652:658	complex	652:658	complex with FAS-2 (fasciculin 2) and a hydroxylated derivative of huprine (huprine W)	652:737	To aid in the design of these MTDLs, we report the crystal structures of hAChE (human acetylcholinesterase) in complex with FAS-2 (fasciculin 2) and a hydroxylated derivative of huprine (huprine W), and of hBChE (human butyrylcholinesterase) in complex with tacrine.
23679855	4	11	theme	residue	1069:1075	arg1	carbonyl					1033:1040	the main chain carbonyl	1018:1040	the main chain carbonyl of the catalytic histidine residue	1018:1075	Huprine W in hAChE and tacrine in hBChE reside in strikingly similar positions highlighting the conservation of key interactions, namely, π-π/cation-π interactions with Trp86 (Trp82), and hydrogen bonding with the main chain carbonyl of the catalytic histidine residue.
23679855	3	12	theme	hBChE	747:751	arg1	structures					600:609	the crystal structures	588:609	the crystal structures of hAChE (human acetylcholinesterase) in complex with FAS-2 (fasciculin 2) and a hydroxylated derivative of huprine (huprine W), and of hBChE (human butyrylcholinesterase) in complex with tacrine	588:805	To aid in the design of these MTDLs, we report the crystal structures of hAChE (human acetylcholinesterase) in complex with FAS-2 (fasciculin 2) and a hydroxylated derivative of huprine (huprine W), and of hBChE (human butyrylcholinesterase) in complex with tacrine.
23679855	3	13	from	hAChE	614:618	arg1	complex					652:658	complex	652:658	complex with FAS-2 (fasciculin 2) and a hydroxylated derivative of huprine (huprine W)	652:737	To aid in the design of these MTDLs, we report the crystal structures of hAChE (human acetylcholinesterase) in complex with FAS-2 (fasciculin 2) and a hydroxylated derivative of huprine (huprine W), and of hBChE (human butyrylcholinesterase) in complex with tacrine.
23679855	4	14	theme	Huprine	808:814	arg1	W					816:816	Huprine W	808:816	Huprine W in hAChE and tacrine in hBChE	808:846	Huprine W in hAChE and tacrine in hBChE reside in strikingly similar positions highlighting the conservation of key interactions, namely, π-π/cation-π interactions with Trp86 (Trp82), and hydrogen bonding with the main chain carbonyl of the catalytic histidine residue.
23679855	4	15	with	interactions	959:970	arg1	carbonyl					1033:1040	the main chain carbonyl	1018:1040	the main chain carbonyl of the catalytic histidine residue	1018:1075	Huprine W in hAChE and tacrine in hBChE reside in strikingly similar positions highlighting the conservation of key interactions, namely, π-π/cation-π interactions with Trp86 (Trp82), and hydrogen bonding with the main chain carbonyl of the catalytic histidine residue.
23679855	4	15	with	interactions	959:970	arg1	Trp82					984:988	Trp82	984:988	Trp82	984:988	Huprine W in hAChE and tacrine in hBChE reside in strikingly similar positions highlighting the conservation of key interactions, namely, π-π/cation-π interactions with Trp86 (Trp82), and hydrogen bonding with the main chain carbonyl of the catalytic histidine residue.
23679855	4	15	with	interactions	959:970	arg1	Trp86					977:981	Trp86	977:981	Trp86 (Trp82)	977:989	Huprine W in hAChE and tacrine in hBChE reside in strikingly similar positions highlighting the conservation of key interactions, namely, π-π/cation-π interactions with Trp86 (Trp82), and hydrogen bonding with the main chain carbonyl of the catalytic histidine residue.
23679855	4	16	theme	interactions	924:935	arg1	conservation					904:915	the conservation	900:915	the conservation of key interactions, namely, π-π/cation-π interactions with Trp86 (Trp82), and hydrogen bonding with the main chain carbonyl of the catalytic histidine residue	900:1075	Huprine W in hAChE and tacrine in hBChE reside in strikingly similar positions highlighting the conservation of key interactions, namely, π-π/cation-π interactions with Trp86 (Trp82), and hydrogen bonding with the main chain carbonyl of the catalytic histidine residue.
23679855	0	17	theme	specificity	95:105	arg1	elements					83:90	elements	83:90	Crystal structures of human cholinesterases in complex with huprine W and tacrine: elements of specificity for anti-Alzheimer's drugs targeting acetyl- and butyryl-cholinesterase.	0:178	Crystal structures of human cholinesterases in complex with huprine W and tacrine: elements of specificity for anti-Alzheimer's drugs targeting acetyl- and butyryl-cholinesterase.
23679855	1	18	theme	amyloid	363:369	arg1	aggregation					371:381	amyloid aggregation	363:381	amyloid aggregation	363:381	The multifunctional nature of Alzheimer's disease calls for MTDLs (multitarget-directed ligands) to act on different components of the pathology, like the cholinergic dysfunction and amyloid aggregation.
23679855	5	19	from	present	1271:1277	arg1	hBChE					1282:1286	hBChE	1282:1286	hBChE	1282:1286	Huprine W forms additional interactions with hAChE, which explains its superior affinity: the isoquinoline moiety is associated with a group of aromatic residues (Tyr337, Phe338 and Phe295 not present in hBChE) in addition to Trp86; the hydroxyl group is hydrogen bonded to both the catalytic serine residue and residues in the oxyanion hole; and the chlorine substituent is nested in a hydrophobic pocket interacting strongly with Trp439.
23679855	5	20	attach	present	1271:1277	arg2	Phe338					1249:1254	Phe338	1249:1254	Phe338	1249:1254	Huprine W forms additional interactions with hAChE, which explains its superior affinity: the isoquinoline moiety is associated with a group of aromatic residues (Tyr337, Phe338 and Phe295 not present in hBChE) in addition to Trp86; the hydroxyl group is hydrogen bonded to both the catalytic serine residue and residues in the oxyanion hole; and the chlorine substituent is nested in a hydrophobic pocket interacting strongly with Trp439.
23679855	5	20	attach	present	1271:1277	arg1	hBChE					1282:1286	hBChE	1282:1286	hBChE	1282:1286	Huprine W forms additional interactions with hAChE, which explains its superior affinity: the isoquinoline moiety is associated with a group of aromatic residues (Tyr337, Phe338 and Phe295 not present in hBChE) in addition to Trp86; the hydroxyl group is hydrogen bonded to both the catalytic serine residue and residues in the oxyanion hole; and the chlorine substituent is nested in a hydrophobic pocket interacting strongly with Trp439.
23679855	3	21	with	complex	786:792	arg1	tacrine					799:805	tacrine	799:805	tacrine	799:805	To aid in the design of these MTDLs, we report the crystal structures of hAChE (human acetylcholinesterase) in complex with FAS-2 (fasciculin 2) and a hydroxylated derivative of huprine (huprine W), and of hBChE (human butyrylcholinesterase) in complex with tacrine.
23679855	3	22	theme	human	754:758	arg1	hBChE					747:751	hBChE	747:751	hBChE (human butyrylcholinesterase) in complex with tacrine	747:805	To aid in the design of these MTDLs, we report the crystal structures of hAChE (human acetylcholinesterase) in complex with FAS-2 (fasciculin 2) and a hydroxylated derivative of huprine (huprine W), and of hBChE (human butyrylcholinesterase) in complex with tacrine.
23679855	3	22	theme	human	754:758	arg1	butyrylcholinesterase					760:780	human butyrylcholinesterase	754:780	human butyrylcholinesterase	754:780	To aid in the design of these MTDLs, we report the crystal structures of hAChE (human acetylcholinesterase) in complex with FAS-2 (fasciculin 2) and a hydroxylated derivative of huprine (huprine W), and of hBChE (human butyrylcholinesterase) in complex with tacrine.
23679855	5	23	with	interactions	1105:1116	arg1	hAChE					1123:1127	hAChE	1123:1127	hAChE	1123:1127	Huprine W forms additional interactions with hAChE, which explains its superior affinity: the isoquinoline moiety is associated with a group of aromatic residues (Tyr337, Phe338 and Phe295 not present in hBChE) in addition to Trp86; the hydroxyl group is hydrogen bonded to both the catalytic serine residue and residues in the oxyanion hole; and the chlorine substituent is nested in a hydrophobic pocket interacting strongly with Trp439.
23679855	0	24	theme	Crystal	0:6	arg1	structures					8:17	Crystal structures	0:17	Crystal structures of human cholinesterases in complex with huprine W and tacrine: elements of specificity for anti-Alzheimer's drugs targeting acetyl- and butyryl-cholinesterase.	0:178	Crystal structures of human cholinesterases in complex with huprine W and tacrine: elements of specificity for anti-Alzheimer's drugs targeting acetyl- and butyryl-cholinesterase.
23679855	4	25	theme	histidine	1059:1067	arg1	residue					1069:1075	the catalytic histidine residue	1045:1075	the catalytic histidine residue	1045:1075	Huprine W in hAChE and tacrine in hBChE reside in strikingly similar positions highlighting the conservation of key interactions, namely, π-π/cation-π interactions with Trp86 (Trp82), and hydrogen bonding with the main chain carbonyl of the catalytic histidine residue.
23679855	3	26	theme	huprine	719:725	arg1	FAS-2					665:669	FAS-2	665:669	FAS-2 (fasciculin 2)	665:684	To aid in the design of these MTDLs, we report the crystal structures of hAChE (human acetylcholinesterase) in complex with FAS-2 (fasciculin 2) and a hydroxylated derivative of huprine (huprine W), and of hBChE (human butyrylcholinesterase) in complex with tacrine.
23679855	3	26	theme	huprine	719:725	arg1	derivative					705:714	a hydroxylated derivative	690:714	a hydroxylated derivative of huprine (huprine W)	690:737	To aid in the design of these MTDLs, we report the crystal structures of hAChE (human acetylcholinesterase) in complex with FAS-2 (fasciculin 2) and a hydroxylated derivative of huprine (huprine W), and of hBChE (human butyrylcholinesterase) in complex with tacrine.
23679855	3	26	theme	huprine	719:725	arg1	fasciculin					672:681	fasciculin 2	672:683	fasciculin 2	672:683	To aid in the design of these MTDLs, we report the crystal structures of hAChE (human acetylcholinesterase) in complex with FAS-2 (fasciculin 2) and a hydroxylated derivative of huprine (huprine W), and of hBChE (human butyrylcholinesterase) in complex with tacrine.
23679855	3	26	theme	huprine	719:725	arg1	W					736:736	huprine W	728:736	huprine W	728:736	To aid in the design of these MTDLs, we report the crystal structures of hAChE (human acetylcholinesterase) in complex with FAS-2 (fasciculin 2) and a hydroxylated derivative of huprine (huprine W), and of hBChE (human butyrylcholinesterase) in complex with tacrine.
23679855	4	27	theme	interactions	959:970	arg1	conservation					904:915	the conservation	900:915	the conservation of key interactions, namely, π-π/cation-π interactions with Trp86 (Trp82), and hydrogen bonding with the main chain carbonyl of the catalytic histidine residue	900:1075	Huprine W in hAChE and tacrine in hBChE reside in strikingly similar positions highlighting the conservation of key interactions, namely, π-π/cation-π interactions with Trp86 (Trp82), and hydrogen bonding with the main chain carbonyl of the catalytic histidine residue.
23679855	4	28	theme	catalytic	1049:1057	arg1	residue					1069:1075	the catalytic histidine residue	1045:1075	the catalytic histidine residue	1045:1075	Huprine W in hAChE and tacrine in hBChE reside in strikingly similar positions highlighting the conservation of key interactions, namely, π-π/cation-π interactions with Trp86 (Trp82), and hydrogen bonding with the main chain carbonyl of the catalytic histidine residue.
23679855	1	29	theme	multifunctional	184:198	arg1	nature					200:205	The multifunctional nature	180:205	The multifunctional nature of Alzheimer's disease calls for MTDLs (multitarget-directed ligands)	180:275	The multifunctional nature of Alzheimer's disease calls for MTDLs (multitarget-directed ligands) to act on different components of the pathology, like the cholinergic dysfunction and amyloid aggregation.
23679855	0	30	from	structures	8:17	arg1	complex					47:53	complex	47:53	complex with huprine W and tacrine	47:80	Crystal structures of human cholinesterases in complex with huprine W and tacrine: elements of specificity for anti-Alzheimer's drugs targeting acetyl- and butyryl-cholinesterase.
23679855	4	31	theme	π-π/cation-π	946:957	arg1	interactions					959:970	π-π/cation-π interactions	946:970	π-π/cation-π interactions with Trp86 (Trp82)	946:989	Huprine W in hAChE and tacrine in hBChE reside in strikingly similar positions highlighting the conservation of key interactions, namely, π-π/cation-π interactions with Trp86 (Trp82), and hydrogen bonding with the main chain carbonyl of the catalytic histidine residue.
23679855	4	32	theme	main	1022:1025	arg1	carbonyl					1033:1040	the main chain carbonyl	1018:1040	the main chain carbonyl of the catalytic histidine residue	1018:1075	Huprine W in hAChE and tacrine in hBChE reside in strikingly similar positions highlighting the conservation of key interactions, namely, π-π/cation-π interactions with Trp86 (Trp82), and hydrogen bonding with the main chain carbonyl of the catalytic histidine residue.
23679855	2	33	theme	Such	384:387	arg1	MTDLs					389:393	Such MTDLs	384:393	Such MTDLs	384:393	Such MTDLs are usually on the basis of cholinesterase inhibitors (e.g. tacrine or huprine) coupled with another active molecule aimed at a different target.
23679855	0	34	theme	human	22:26	arg1	cholinesterases					28:42	human cholinesterases	22:42	human cholinesterases	22:42	Crystal structures of human cholinesterases in complex with huprine W and tacrine: elements of specificity for anti-Alzheimer's drugs targeting acetyl- and butyryl-cholinesterase.
23679855	5	35	theme	additional	1094:1103	arg1	interactions					1105:1116	additional interactions	1094:1116	additional interactions with hAChE, which explains its superior affinity	1094:1165	Huprine W forms additional interactions with hAChE, which explains its superior affinity: the isoquinoline moiety is associated with a group of aromatic residues (Tyr337, Phe338 and Phe295 not present in hBChE) in addition to Trp86; the hydroxyl group is hydrogen bonded to both the catalytic serine residue and residues in the oxyanion hole; and the chlorine substituent is nested in a hydrophobic pocket interacting strongly with Trp439.
23679855	3	36	from	hBChE	747:751	arg1	complex					786:792	complex	786:792	complex with tacrine	786:805	To aid in the design of these MTDLs, we report the crystal structures of hAChE (human acetylcholinesterase) in complex with FAS-2 (fasciculin 2) and a hydroxylated derivative of huprine (huprine W), and of hBChE (human butyrylcholinesterase) in complex with tacrine.
23679855	4	37	with	interactions	924:935	arg1	carbonyl					1033:1040	the main chain carbonyl	1018:1040	the main chain carbonyl of the catalytic histidine residue	1018:1075	Huprine W in hAChE and tacrine in hBChE reside in strikingly similar positions highlighting the conservation of key interactions, namely, π-π/cation-π interactions with Trp86 (Trp82), and hydrogen bonding with the main chain carbonyl of the catalytic histidine residue.
23679855	4	37	with	interactions	924:935	arg1	Trp82					984:988	Trp82	984:988	Trp82	984:988	Huprine W in hAChE and tacrine in hBChE reside in strikingly similar positions highlighting the conservation of key interactions, namely, π-π/cation-π interactions with Trp86 (Trp82), and hydrogen bonding with the main chain carbonyl of the catalytic histidine residue.
23679855	4	37	with	interactions	924:935	arg1	Trp86					977:981	Trp86	977:981	Trp86 (Trp82)	977:989	Huprine W in hAChE and tacrine in hBChE reside in strikingly similar positions highlighting the conservation of key interactions, namely, π-π/cation-π interactions with Trp86 (Trp82), and hydrogen bonding with the main chain carbonyl of the catalytic histidine residue.
23679855	3	38	from	complex	786:792	arg1	structures					600:609	the crystal structures	588:609	the crystal structures of hAChE (human acetylcholinesterase) in complex with FAS-2 (fasciculin 2) and a hydroxylated derivative of huprine (huprine W), and of hBChE (human butyrylcholinesterase) in complex with tacrine	588:805	To aid in the design of these MTDLs, we report the crystal structures of hAChE (human acetylcholinesterase) in complex with FAS-2 (fasciculin 2) and a hydroxylated derivative of huprine (huprine W), and of hBChE (human butyrylcholinesterase) in complex with tacrine.
23679855	5	39	theme	aromatic	1222:1229	arg1	residues					1231:1238	aromatic residues	1222:1238	aromatic residues (Tyr337, Phe338 and Phe295 not present in hBChE) in addition to Trp86	1222:1308	Huprine W forms additional interactions with hAChE, which explains its superior affinity: the isoquinoline moiety is associated with a group of aromatic residues (Tyr337, Phe338 and Phe295 not present in hBChE) in addition to Trp86; the hydroxyl group is hydrogen bonded to both the catalytic serine residue and residues in the oxyanion hole; and the chlorine substituent is nested in a hydrophobic pocket interacting strongly with Trp439.
23679855	2	40	theme	cholinesterase	423:436	arg1	inhibitors					438:447	cholinesterase inhibitors	423:447	cholinesterase inhibitors (e.g. tacrine or huprine) coupled with another active molecule aimed at a different target	423:538	Such MTDLs are usually on the basis of cholinesterase inhibitors (e.g. tacrine or huprine) coupled with another active molecule aimed at a different target.
23679855	1	41	theme	different	287:295	arg1	components					297:306	different components	287:306	different components of the pathology	287:323	The multifunctional nature of Alzheimer's disease calls for MTDLs (multitarget-directed ligands) to act on different components of the pathology, like the cholinergic dysfunction and amyloid aggregation.
23679855	5	42	dep	Tyr337	1241:1246	arg1	Phe295					1260:1265	Phe295	1260:1265	Phe295	1260:1265	Huprine W forms additional interactions with hAChE, which explains its superior affinity: the isoquinoline moiety is associated with a group of aromatic residues (Tyr337, Phe338 and Phe295 not present in hBChE) in addition to Trp86; the hydroxyl group is hydrogen bonded to both the catalytic serine residue and residues in the oxyanion hole; and the chlorine substituent is nested in a hydrophobic pocket interacting strongly with Trp439.
23679855	5	42	dep	Tyr337	1241:1246	arg1	Phe338					1249:1254	Phe338	1249:1254	Phe338	1249:1254	Huprine W forms additional interactions with hAChE, which explains its superior affinity: the isoquinoline moiety is associated with a group of aromatic residues (Tyr337, Phe338 and Phe295 not present in hBChE) in addition to Trp86; the hydroxyl group is hydrogen bonded to both the catalytic serine residue and residues in the oxyanion hole; and the chlorine substituent is nested in a hydrophobic pocket interacting strongly with Trp439.
23679855	3	43	theme	hAChE	614:618	arg1	structures					600:609	the crystal structures	588:609	the crystal structures of hAChE (human acetylcholinesterase) in complex with FAS-2 (fasciculin 2) and a hydroxylated derivative of huprine (huprine W), and of hBChE (human butyrylcholinesterase) in complex with tacrine	588:805	To aid in the design of these MTDLs, we report the crystal structures of hAChE (human acetylcholinesterase) in complex with FAS-2 (fasciculin 2) and a hydroxylated derivative of huprine (huprine W), and of hBChE (human butyrylcholinesterase) in complex with tacrine.
23679855	5	44	theme	residues	1231:1238	arg1	residues					1231:1238	aromatic residues	1222:1238	aromatic residues (Tyr337, Phe338 and Phe295 not present in hBChE) in addition to Trp86	1222:1308	Huprine W forms additional interactions with hAChE, which explains its superior affinity: the isoquinoline moiety is associated with a group of aromatic residues (Tyr337, Phe338 and Phe295 not present in hBChE) in addition to Trp86; the hydroxyl group is hydrogen bonded to both the catalytic serine residue and residues in the oxyanion hole; and the chlorine substituent is nested in a hydrophobic pocket interacting strongly with Trp439.
23679855	5	44	theme	residues	1231:1238	arg1	group					1213:1217	a group	1211:1217	a group of aromatic residues (Tyr337, Phe338 and Phe295 not present in hBChE) in addition to Trp86	1211:1308	Huprine W forms additional interactions with hAChE, which explains its superior affinity: the isoquinoline moiety is associated with a group of aromatic residues (Tyr337, Phe338 and Phe295 not present in hBChE) in addition to Trp86; the hydroxyl group is hydrogen bonded to both the catalytic serine residue and residues in the oxyanion hole; and the chlorine substituent is nested in a hydrophobic pocket interacting strongly with Trp439.
23679855	3	45	from	complex	652:658	arg1	structures					600:609	the crystal structures	588:609	the crystal structures of hAChE (human acetylcholinesterase) in complex with FAS-2 (fasciculin 2) and a hydroxylated derivative of huprine (huprine W), and of hBChE (human butyrylcholinesterase) in complex with tacrine	588:805	To aid in the design of these MTDLs, we report the crystal structures of hAChE (human acetylcholinesterase) in complex with FAS-2 (fasciculin 2) and a hydroxylated derivative of huprine (huprine W), and of hBChE (human butyrylcholinesterase) in complex with tacrine.
23679855	3	46	theme	hydroxylated	692:703	arg1	derivative					705:714	a hydroxylated derivative	690:714	a hydroxylated derivative of huprine (huprine W)	690:737	To aid in the design of these MTDLs, we report the crystal structures of hAChE (human acetylcholinesterase) in complex with FAS-2 (fasciculin 2) and a hydroxylated derivative of huprine (huprine W), and of hBChE (human butyrylcholinesterase) in complex with tacrine.
23679855	3	46	theme	hydroxylated	692:703	arg1	W					736:736	huprine W	728:736	huprine W	728:736	To aid in the design of these MTDLs, we report the crystal structures of hAChE (human acetylcholinesterase) in complex with FAS-2 (fasciculin 2) and a hydroxylated derivative of huprine (huprine W), and of hBChE (human butyrylcholinesterase) in complex with tacrine.
23679855	4	47	with	bonding	1005:1011	arg1	carbonyl					1033:1040	the main chain carbonyl	1018:1040	the main chain carbonyl of the catalytic histidine residue	1018:1075	Huprine W in hAChE and tacrine in hBChE reside in strikingly similar positions highlighting the conservation of key interactions, namely, π-π/cation-π interactions with Trp86 (Trp82), and hydrogen bonding with the main chain carbonyl of the catalytic histidine residue.
23679855	4	47	with	bonding	1005:1011	arg1	Trp82					984:988	Trp82	984:988	Trp82	984:988	Huprine W in hAChE and tacrine in hBChE reside in strikingly similar positions highlighting the conservation of key interactions, namely, π-π/cation-π interactions with Trp86 (Trp82), and hydrogen bonding with the main chain carbonyl of the catalytic histidine residue.
23679855	4	47	with	bonding	1005:1011	arg1	Trp86					977:981	Trp86	977:981	Trp86 (Trp82)	977:989	Huprine W in hAChE and tacrine in hBChE reside in strikingly similar positions highlighting the conservation of key interactions, namely, π-π/cation-π interactions with Trp86 (Trp82), and hydrogen bonding with the main chain carbonyl of the catalytic histidine residue.
23679855	3	48	theme	MTDLs	571:575	arg1	design					555:560	the design	551:560	the design of these MTDLs	551:575	To aid in the design of these MTDLs, we report the crystal structures of hAChE (human acetylcholinesterase) in complex with FAS-2 (fasciculin 2) and a hydroxylated derivative of huprine (huprine W), and of hBChE (human butyrylcholinesterase) in complex with tacrine.
23679855	4	49	theme	chain	1027:1031	arg1	carbonyl					1033:1040	the main chain carbonyl	1018:1040	the main chain carbonyl of the catalytic histidine residue	1018:1075	Huprine W in hAChE and tacrine in hBChE reside in strikingly similar positions highlighting the conservation of key interactions, namely, π-π/cation-π interactions with Trp86 (Trp82), and hydrogen bonding with the main chain carbonyl of the catalytic histidine residue.
23679855	5	50	from	hBChE	1282:1286	arg1	present					1271:1277	present	1271:1277	present	1271:1277	Huprine W forms additional interactions with hAChE, which explains its superior affinity: the isoquinoline moiety is associated with a group of aromatic residues (Tyr337, Phe338 and Phe295 not present in hBChE) in addition to Trp86; the hydroxyl group is hydrogen bonded to both the catalytic serine residue and residues in the oxyanion hole; and the chlorine substituent is nested in a hydrophobic pocket interacting strongly with Trp439.
23679855	0	51	theme	cholinesterases	28:42	arg1	structures					8:17	Crystal structures	0:17	Crystal structures of human cholinesterases in complex with huprine W and tacrine: elements of specificity for anti-Alzheimer's drugs targeting acetyl- and butyryl-cholinesterase.	0:178	Crystal structures of human cholinesterases in complex with huprine W and tacrine: elements of specificity for anti-Alzheimer's drugs targeting acetyl- and butyryl-cholinesterase.
23679855	3	52	theme	huprine	728:734	arg1	derivative					705:714	a hydroxylated derivative	690:714	a hydroxylated derivative of huprine (huprine W)	690:737	To aid in the design of these MTDLs, we report the crystal structures of hAChE (human acetylcholinesterase) in complex with FAS-2 (fasciculin 2) and a hydroxylated derivative of huprine (huprine W), and of hBChE (human butyrylcholinesterase) in complex with tacrine.
23679855	3	52	theme	huprine	728:734	arg1	W					736:736	huprine W	728:736	huprine W	728:736	To aid in the design of these MTDLs, we report the crystal structures of hAChE (human acetylcholinesterase) in complex with FAS-2 (fasciculin 2) and a hydroxylated derivative of huprine (huprine W), and of hBChE (human butyrylcholinesterase) in complex with tacrine.
23679855	2	53	theme	different	523:531	arg1	target					533:538	a different target	521:538	a different target	521:538	Such MTDLs are usually on the basis of cholinesterase inhibitors (e.g. tacrine or huprine) coupled with another active molecule aimed at a different target.
23679855	2	54	theme	inhibitors	438:447	arg1	basis					414:418	the basis	410:418	the basis of cholinesterase inhibitors (e.g. tacrine or huprine) coupled with another active molecule aimed at a different target	410:538	Such MTDLs are usually on the basis of cholinesterase inhibitors (e.g. tacrine or huprine) coupled with another active molecule aimed at a different target.
23679855	5	55	theme	chlorine	1429:1436	arg1	substituent					1438:1448	the chlorine substituent	1425:1448	the chlorine substituent	1425:1448	Huprine W forms additional interactions with hAChE, which explains its superior affinity: the isoquinoline moiety is associated with a group of aromatic residues (Tyr337, Phe338 and Phe295 not present in hBChE) in addition to Trp86; the hydroxyl group is hydrogen bonded to both the catalytic serine residue and residues in the oxyanion hole; and the chlorine substituent is nested in a hydrophobic pocket interacting strongly with Trp439.
23679855	1	56	theme	disease	222:228	arg1	calls					230:234	Alzheimer's disease calls	210:234	Alzheimer's disease calls for MTDLs (multitarget-directed ligands)	210:275	The multifunctional nature of Alzheimer's disease calls for MTDLs (multitarget-directed ligands) to act on different components of the pathology, like the cholinergic dysfunction and amyloid aggregation.
23679855	4	57	theme	similar	869:875	arg1	positions					877:885	strikingly similar positions	858:885	strikingly similar positions highlighting the conservation of key interactions, namely, π-π/cation-π interactions with Trp86 (Trp82), and hydrogen bonding with the main chain carbonyl of the catalytic histidine residue	858:1075	Huprine W in hAChE and tacrine in hBChE reside in strikingly similar positions highlighting the conservation of key interactions, namely, π-π/cation-π interactions with Trp86 (Trp82), and hydrogen bonding with the main chain carbonyl of the catalytic histidine residue.
23679855	6	58	theme	chlorine	1578:1585	arg1	substituent					1587:1597	the chlorine substituent	1574:1597	the chlorine substituent	1574:1597	There is no pocket in hBChE that is able to accommodate the chlorine substituent.
23679855	1	59	theme	pathology	315:323	arg1	components					297:306	different components	287:306	different components of the pathology	287:323	The multifunctional nature of Alzheimer's disease calls for MTDLs (multitarget-directed ligands) to act on different components of the pathology, like the cholinergic dysfunction and amyloid aggregation.
23679855	5	60	theme	serine	1371:1376	arg1	residue					1378:1384	the catalytic serine residue	1357:1384	the catalytic serine residue	1357:1384	Huprine W forms additional interactions with hAChE, which explains its superior affinity: the isoquinoline moiety is associated with a group of aromatic residues (Tyr337, Phe338 and Phe295 not present in hBChE) in addition to Trp86; the hydroxyl group is hydrogen bonded to both the catalytic serine residue and residues in the oxyanion hole; and the chlorine substituent is nested in a hydrophobic pocket interacting strongly with Trp439.
23679855	4	61	theme	hydrogen	996:1003	arg1	bonding					1005:1011	hydrogen bonding	996:1011	hydrogen bonding with the main chain carbonyl of the catalytic histidine residue	996:1075	Huprine W in hAChE and tacrine in hBChE reside in strikingly similar positions highlighting the conservation of key interactions, namely, π-π/cation-π interactions with Trp86 (Trp82), and hydrogen bonding with the main chain carbonyl of the catalytic histidine residue.
23679855	5	62	from	residue	1378:1384	arg1	hole					1415:1418	the oxyanion hole	1402:1418	the oxyanion hole	1402:1418	Huprine W forms additional interactions with hAChE, which explains its superior affinity: the isoquinoline moiety is associated with a group of aromatic residues (Tyr337, Phe338 and Phe295 not present in hBChE) in addition to Trp86; the hydroxyl group is hydrogen bonded to both the catalytic serine residue and residues in the oxyanion hole; and the chlorine substituent is nested in a hydrophobic pocket interacting strongly with Trp439.
23679855	1	63	theme	calls	230:234	arg1	nature					200:205	The multifunctional nature	180:205	The multifunctional nature of Alzheimer's disease calls for MTDLs (multitarget-directed ligands)	180:275	The multifunctional nature of Alzheimer's disease calls for MTDLs (multitarget-directed ligands) to act on different components of the pathology, like the cholinergic dysfunction and amyloid aggregation.
23679855	5	64	theme	oxyanion	1406:1413	arg1	hole					1415:1418	the oxyanion hole	1402:1418	the oxyanion hole	1402:1418	Huprine W forms additional interactions with hAChE, which explains its superior affinity: the isoquinoline moiety is associated with a group of aromatic residues (Tyr337, Phe338 and Phe295 not present in hBChE) in addition to Trp86; the hydroxyl group is hydrogen bonded to both the catalytic serine residue and residues in the oxyanion hole; and the chlorine substituent is nested in a hydrophobic pocket interacting strongly with Trp439.
23679855	3	65	theme	human	621:625	arg1	hAChE					614:618	hAChE	614:618	hAChE (human acetylcholinesterase) in complex with FAS-2 (fasciculin 2) and a hydroxylated derivative of huprine (huprine W)	614:737	To aid in the design of these MTDLs, we report the crystal structures of hAChE (human acetylcholinesterase) in complex with FAS-2 (fasciculin 2) and a hydroxylated derivative of huprine (huprine W), and of hBChE (human butyrylcholinesterase) in complex with tacrine.
23679855	3	65	theme	human	621:625	arg1	acetylcholinesterase					627:646	human acetylcholinesterase	621:646	human acetylcholinesterase	621:646	To aid in the design of these MTDLs, we report the crystal structures of hAChE (human acetylcholinesterase) in complex with FAS-2 (fasciculin 2) and a hydroxylated derivative of huprine (huprine W), and of hBChE (human butyrylcholinesterase) in complex with tacrine.
23679855	3	66	theme	crystal	592:598	arg1	structures					600:609	the crystal structures	588:609	the crystal structures of hAChE (human acetylcholinesterase) in complex with FAS-2 (fasciculin 2) and a hydroxylated derivative of huprine (huprine W), and of hBChE (human butyrylcholinesterase) in complex with tacrine	588:805	To aid in the design of these MTDLs, we report the crystal structures of hAChE (human acetylcholinesterase) in complex with FAS-2 (fasciculin 2) and a hydroxylated derivative of huprine (huprine W), and of hBChE (human butyrylcholinesterase) in complex with tacrine.
23679855	5	67	dep	residues	1231:1238	arg1	Tyr337					1241:1246	Tyr337	1241:1246	Tyr337	1241:1246	Huprine W forms additional interactions with hAChE, which explains its superior affinity: the isoquinoline moiety is associated with a group of aromatic residues (Tyr337, Phe338 and Phe295 not present in hBChE) in addition to Trp86; the hydroxyl group is hydrogen bonded to both the catalytic serine residue and residues in the oxyanion hole; and the chlorine substituent is nested in a hydrophobic pocket interacting strongly with Trp439.
23679855	5	68	theme	superior	1149:1156	arg1	affinity					1158:1165	its superior affinity	1145:1165	its superior affinity	1145:1165	Huprine W forms additional interactions with hAChE, which explains its superior affinity: the isoquinoline moiety is associated with a group of aromatic residues (Tyr337, Phe338 and Phe295 not present in hBChE) in addition to Trp86; the hydroxyl group is hydrogen bonded to both the catalytic serine residue and residues in the oxyanion hole; and the chlorine substituent is nested in a hydrophobic pocket interacting strongly with Trp439.
23679855	2	69	theme	active	496:501	arg1	molecule					503:510	another active molecule	488:510	another active molecule aimed at a different target	488:538	Such MTDLs are usually on the basis of cholinesterase inhibitors (e.g. tacrine or huprine) coupled with another active molecule aimed at a different target.
23679855	0	70	dep	structures	8:17	arg1	elements					83:90	elements	83:90	Crystal structures of human cholinesterases in complex with huprine W and tacrine: elements of specificity for anti-Alzheimer's drugs targeting acetyl- and butyryl-cholinesterase.	0:178	Crystal structures of human cholinesterases in complex with huprine W and tacrine: elements of specificity for anti-Alzheimer's drugs targeting acetyl- and butyryl-cholinesterase.
23679855	0	71	with	complex	47:53	arg1	tacrine					74:80	tacrine	74:80	tacrine	74:80	Crystal structures of human cholinesterases in complex with huprine W and tacrine: elements of specificity for anti-Alzheimer's drugs targeting acetyl- and butyryl-cholinesterase.
23679855	0	71	with	complex	47:53	arg1	W					68:68	huprine W	60:68	huprine W	60:68	Crystal structures of human cholinesterases in complex with huprine W and tacrine: elements of specificity for anti-Alzheimer's drugs targeting acetyl- and butyryl-cholinesterase.
23679855	4	72	theme	bonding	1005:1011	arg1	conservation					904:915	the conservation	900:915	the conservation of key interactions, namely, π-π/cation-π interactions with Trp86 (Trp82), and hydrogen bonding with the main chain carbonyl of the catalytic histidine residue	900:1075	Huprine W in hAChE and tacrine in hBChE reside in strikingly similar positions highlighting the conservation of key interactions, namely, π-π/cation-π interactions with Trp86 (Trp82), and hydrogen bonding with the main chain carbonyl of the catalytic histidine residue.
23679855	5	73	from	residues	1390:1397	arg1	hole					1415:1418	the oxyanion hole	1402:1418	the oxyanion hole	1402:1418	Huprine W forms additional interactions with hAChE, which explains its superior affinity: the isoquinoline moiety is associated with a group of aromatic residues (Tyr337, Phe338 and Phe295 not present in hBChE) in addition to Trp86; the hydroxyl group is hydrogen bonded to both the catalytic serine residue and residues in the oxyanion hole; and the chlorine substituent is nested in a hydrophobic pocket interacting strongly with Trp439.
23679855	0	74	theme	huprine	60:66	arg1	W					68:68	huprine W	60:68	huprine W	60:68	Crystal structures of human cholinesterases in complex with huprine W and tacrine: elements of specificity for anti-Alzheimer's drugs targeting acetyl- and butyryl-cholinesterase.
23679855	4	75	from	W	816:816	arg1	hBChE					842:846	hBChE	842:846	hBChE	842:846	Huprine W in hAChE and tacrine in hBChE reside in strikingly similar positions highlighting the conservation of key interactions, namely, π-π/cation-π interactions with Trp86 (Trp82), and hydrogen bonding with the main chain carbonyl of the catalytic histidine residue.
23679855	4	75	from	W	816:816	arg1	tacrine					831:837	tacrine	831:837	tacrine	831:837	Huprine W in hAChE and tacrine in hBChE reside in strikingly similar positions highlighting the conservation of key interactions, namely, π-π/cation-π interactions with Trp86 (Trp82), and hydrogen bonding with the main chain carbonyl of the catalytic histidine residue.
23679855	4	75	from	W	816:816	arg1	hAChE					821:825	hAChE	821:825	hAChE	821:825	Huprine W in hAChE and tacrine in hBChE reside in strikingly similar positions highlighting the conservation of key interactions, namely, π-π/cation-π interactions with Trp86 (Trp82), and hydrogen bonding with the main chain carbonyl of the catalytic histidine residue.
23679855	3	76	with	complex	652:658	arg1	derivative					705:714	a hydroxylated derivative	690:714	a hydroxylated derivative of huprine (huprine W)	690:737	To aid in the design of these MTDLs, we report the crystal structures of hAChE (human acetylcholinesterase) in complex with FAS-2 (fasciculin 2) and a hydroxylated derivative of huprine (huprine W), and of hBChE (human butyrylcholinesterase) in complex with tacrine.
23679855	3	76	with	complex	652:658	arg1	FAS-2					665:669	FAS-2	665:669	FAS-2 (fasciculin 2)	665:684	To aid in the design of these MTDLs, we report the crystal structures of hAChE (human acetylcholinesterase) in complex with FAS-2 (fasciculin 2) and a hydroxylated derivative of huprine (huprine W), and of hBChE (human butyrylcholinesterase) in complex with tacrine.
23679855	3	76	with	complex	652:658	arg1	fasciculin					672:681	fasciculin 2	672:683	fasciculin 2	672:683	To aid in the design of these MTDLs, we report the crystal structures of hAChE (human acetylcholinesterase) in complex with FAS-2 (fasciculin 2) and a hydroxylated derivative of huprine (huprine W), and of hBChE (human butyrylcholinesterase) in complex with tacrine.
23679855	3	76	with	complex	652:658	arg1	W					736:736	huprine W	728:736	huprine W	728:736	To aid in the design of these MTDLs, we report the crystal structures of hAChE (human acetylcholinesterase) in complex with FAS-2 (fasciculin 2) and a hydroxylated derivative of huprine (huprine W), and of hBChE (human butyrylcholinesterase) in complex with tacrine.
16043704	7	0	theme	distinct	1062:1069	arg1	receptors					1092:1100	distinct pathogen recognition receptors	1062:1100	distinct pathogen recognition receptors	1062:1100	The TLR3-ECD structure indicates how LRR loops can establish distinct pathogen recognition receptors.
16043704	6	1	from	insertions	953:962	arg1	glycans					992:998	11 N-linked glycans	980:998	11 N-linked glycans	980:998	The extensive beta-sheet on the molecule's concave surface forms a platform for several modifications, including insertions in the LRRs and 11 N-linked glycans.
16043704	6	1	from	insertions	953:962	arg1	LRRs					971:974	the LRRs	967:974	the LRRs	967:974	The extensive beta-sheet on the molecule's concave surface forms a platform for several modifications, including insertions in the LRRs and 11 N-linked glycans.
16043704	2	2	theme	Toll-like	148:156	arg1	TLRs					169:172	TLRs	169:172	TLRs	169:172	Toll-like receptors (TLRs) act as sentinels of the innate immune system, sensing a variety of ligands from lipopolysaccharide to flagellin to dsRNA through their ligand-binding domain that is composed of leucine-rich repeats (LRRs).
16043704	2	2	theme	Toll-like	148:156	arg1	receptors					158:166	Toll-like receptors	148:166	Toll-like receptors (TLRs)	148:173	Toll-like receptors (TLRs) act as sentinels of the innate immune system, sensing a variety of ligands from lipopolysaccharide to flagellin to dsRNA through their ligand-binding domain that is composed of leucine-rich repeats (LRRs).
16043704	2	2	theme	Toll-like	148:156	arg1	sentinels					182:190	sentinels	182:190	sentinels of the innate immune system	182:218	Toll-like receptors (TLRs) act as sentinels of the innate immune system, sensing a variety of ligands from lipopolysaccharide to flagellin to dsRNA through their ligand-binding domain that is composed of leucine-rich repeats (LRRs).
16043704	6	3	theme	several	920:926	arg1	modifications					928:940	several modifications	920:940	several modifications	920:940	The extensive beta-sheet on the molecule's concave surface forms a platform for several modifications, including insertions in the LRRs and 11 N-linked glycans.
16043704	6	3	theme	several	920:926	arg1	insertions					953:962	insertions	953:962	insertions in the LRRs and 11 N-linked glycans	953:998	The extensive beta-sheet on the molecule's concave surface forms a platform for several modifications, including insertions in the LRRs and 11 N-linked glycans.
16043704	4	4	theme	molecular	653:661	arg1	structure					663:671	the molecular structure	649:671	the molecular structure to 2.4-A resolution	649:691	In this study, we have expressed and crystallized the ectodomain (ECD) of human TLR3, which recognizes dsRNA, a molecular signature of viruses, and have determined the molecular structure to 2.4-A resolution.
16043704	7	5	theme	LRR	1038:1040	arg1	loops					1042:1046	LRR loops	1038:1046	LRR loops	1038:1046	The TLR3-ECD structure indicates how LRR loops can establish distinct pathogen recognition receptors.
16043704	6	6	theme	N-linked	983:990	arg1	glycans					992:998	11 N-linked glycans	980:998	11 N-linked glycans	980:998	The extensive beta-sheet on the molecule's concave surface forms a platform for several modifications, including insertions in the LRRs and 11 N-linked glycans.
16043704	2	7	theme	ligands	242:248	arg1	ligands					242:248	ligands	242:248	ligands from lipopolysaccharide	242:272	Toll-like receptors (TLRs) act as sentinels of the innate immune system, sensing a variety of ligands from lipopolysaccharide to flagellin to dsRNA through their ligand-binding domain that is composed of leucine-rich repeats (LRRs).
16043704	2	7	theme	ligands	242:248	arg1	variety					231:237	a variety	229:237	a variety of ligands from lipopolysaccharide to flagellin to dsRNA	229:294	Toll-like receptors (TLRs) act as sentinels of the innate immune system, sensing a variety of ligands from lipopolysaccharide to flagellin to dsRNA through their ligand-binding domain that is composed of leucine-rich repeats (LRRs).
16043704	3	8	theme	signaling	408:416	arg1	cascade					418:424	a signaling cascade	406:424	a signaling cascade that leads to the up-regulation of inflammation mediators	406:482	Ligand binding initiates a signaling cascade that leads to the up-regulation of inflammation mediators.
16043704	3	9	theme	Ligand	381:386	arg1	binding					388:394	Ligand binding	381:394	Ligand binding	381:394	Ligand binding initiates a signaling cascade that leads to the up-regulation of inflammation mediators.
16043704	1	10	theme	Innate	75:80	arg1	line					104:107	the first line	94:107	the first line of defense against invading pathogens	94:145	Innate immunity is the first line of defense against invading pathogens.
16043704	1	10	theme	Innate	75:80	arg1	immunity					82:89	Innate immunity	75:89	Innate immunity	75:89	Innate immunity is the first line of defense against invading pathogens.
16043704	4	11	theme	molecular	597:605	arg1	signature					607:615	a molecular signature	595:615	a molecular signature of viruses	595:626	In this study, we have expressed and crystallized the ectodomain (ECD) of human TLR3, which recognizes dsRNA, a molecular signature of viruses, and have determined the molecular structure to 2.4-A resolution.
16043704	4	11	theme	molecular	597:605	arg1	dsRNA					588:592	dsRNA	588:592	dsRNA	588:592	In this study, we have expressed and crystallized the ectodomain (ECD) of human TLR3, which recognizes dsRNA, a molecular signature of viruses, and have determined the molecular structure to 2.4-A resolution.
16043704	0	12	theme	molecular	4:12	arg1	structure					14:22	The molecular structure	0:22	The molecular structure of the Toll-like receptor	0:48	The molecular structure of the Toll-like receptor 3 ligand-binding domain.
16043704	6	13	link	N-linked	983:990	arg1	glycans					992:998	11 N-linked glycans	980:998	11 N-linked glycans	980:998	The extensive beta-sheet on the molecule's concave surface forms a platform for several modifications, including insertions in the LRRs and 11 N-linked glycans.
16043704	4	14	theme	viruses	620:626	arg1	signature					607:615	a molecular signature	595:615	a molecular signature of viruses	595:626	In this study, we have expressed and crystallized the ectodomain (ECD) of human TLR3, which recognizes dsRNA, a molecular signature of viruses, and have determined the molecular structure to 2.4-A resolution.
16043704	4	14	theme	viruses	620:626	arg1	dsRNA					588:592	dsRNA	588:592	dsRNA	588:592	In this study, we have expressed and crystallized the ectodomain (ECD) of human TLR3, which recognizes dsRNA, a molecular signature of viruses, and have determined the molecular structure to 2.4-A resolution.
16043704	4	15	theme	2.4-A	676:680	arg1	resolution					682:691	2.4-A resolution	676:691	2.4-A resolution	676:691	In this study, we have expressed and crystallized the ectodomain (ECD) of human TLR3, which recognizes dsRNA, a molecular signature of viruses, and have determined the molecular structure to 2.4-A resolution.
16043704	2	16	theme	leucine-rich	352:363	arg1	LRRs					374:377	LRRs	374:377	LRRs	374:377	Toll-like receptors (TLRs) act as sentinels of the innate immune system, sensing a variety of ligands from lipopolysaccharide to flagellin to dsRNA through their ligand-binding domain that is composed of leucine-rich repeats (LRRs).
16043704	2	16	theme	leucine-rich	352:363	arg1	repeats					365:371	leucine-rich repeats	352:371	leucine-rich repeats (LRRs)	352:378	Toll-like receptors (TLRs) act as sentinels of the innate immune system, sensing a variety of ligands from lipopolysaccharide to flagellin to dsRNA through their ligand-binding domain that is composed of leucine-rich repeats (LRRs).
16043704	5	17	theme	repeating	765:773	arg1	LRRs					775:778	23 repeating LRRs	762:778	23 repeating LRRs that are capped at each end by specialized non-LRR domains	762:837	The overall horseshoe-shaped structure of the TLR3-ECD is formed by 23 repeating LRRs that are capped at each end by specialized non-LRR domains.
16043704	7	18	theme	TLR3-ECD	1005:1012	arg1	structure					1014:1022	The TLR3-ECD structure	1001:1022	The TLR3-ECD structure	1001:1022	The TLR3-ECD structure indicates how LRR loops can establish distinct pathogen recognition receptors.
16043704	0	19	dep	domain	67:72	arg1	structure					14:22	The molecular structure	0:22	The molecular structure of the Toll-like receptor	0:48	The molecular structure of the Toll-like receptor 3 ligand-binding domain.
16043704	1	20	theme	first	98:102	arg1	line					104:107	the first line	94:107	the first line of defense against invading pathogens	94:145	Innate immunity is the first line of defense against invading pathogens.
16043704	1	20	theme	first	98:102	arg1	immunity					82:89	Innate immunity	75:89	Innate immunity	75:89	Innate immunity is the first line of defense against invading pathogens.
16043704	2	21	from	variety	231:237	arg1	lipopolysaccharide					255:272	lipopolysaccharide	255:272	lipopolysaccharide	255:272	Toll-like receptors (TLRs) act as sentinels of the innate immune system, sensing a variety of ligands from lipopolysaccharide to flagellin to dsRNA through their ligand-binding domain that is composed of leucine-rich repeats (LRRs).
16043704	5	22	theme	non-LRR	823:829	arg1	domains					831:837	specialized non-LRR domains	811:837	specialized non-LRR domains	811:837	The overall horseshoe-shaped structure of the TLR3-ECD is formed by 23 repeating LRRs that are capped at each end by specialized non-LRR domains.
16043704	0	23	theme	Toll-like	31:39	arg1	receptor					41:48	the Toll-like receptor	27:48	the Toll-like receptor	27:48	The molecular structure of the Toll-like receptor 3 ligand-binding domain.
16043704	3	24	theme	mediators	474:482	arg1	up-regulation					444:456	the up-regulation	440:456	the up-regulation of inflammation mediators	440:482	Ligand binding initiates a signaling cascade that leads to the up-regulation of inflammation mediators.
16043704	2	25	theme	system	213:218	arg1	receptors					158:166	Toll-like receptors	148:166	Toll-like receptors (TLRs)	148:173	Toll-like receptors (TLRs) act as sentinels of the innate immune system, sensing a variety of ligands from lipopolysaccharide to flagellin to dsRNA through their ligand-binding domain that is composed of leucine-rich repeats (LRRs).
16043704	2	25	theme	system	213:218	arg1	sentinels					182:190	sentinels	182:190	sentinels of the innate immune system	182:218	Toll-like receptors (TLRs) act as sentinels of the innate immune system, sensing a variety of ligands from lipopolysaccharide to flagellin to dsRNA through their ligand-binding domain that is composed of leucine-rich repeats (LRRs).
16043704	5	26	theme	specialized	811:821	arg1	domains					831:837	specialized non-LRR domains	811:837	specialized non-LRR domains	811:837	The overall horseshoe-shaped structure of the TLR3-ECD is formed by 23 repeating LRRs that are capped at each end by specialized non-LRR domains.
16043704	7	27	theme	recognition	1080:1090	arg1	receptors					1092:1100	distinct pathogen recognition receptors	1062:1100	distinct pathogen recognition receptors	1062:1100	The TLR3-ECD structure indicates how LRR loops can establish distinct pathogen recognition receptors.
16043704	5	28	theme	TLR3-ECD	740:747	arg1	structure					723:731	The overall horseshoe-shaped structure	694:731	The overall horseshoe-shaped structure of the TLR3-ECD	694:747	The overall horseshoe-shaped structure of the TLR3-ECD is formed by 23 repeating LRRs that are capped at each end by specialized non-LRR domains.
16043704	2	29	theme	immune	206:211	arg1	system					213:218	the innate immune system	195:218	the innate immune system	195:218	Toll-like receptors (TLRs) act as sentinels of the innate immune system, sensing a variety of ligands from lipopolysaccharide to flagellin to dsRNA through their ligand-binding domain that is composed of leucine-rich repeats (LRRs).
16043704	7	30	theme	pathogen	1071:1078	arg1	receptors					1092:1100	distinct pathogen recognition receptors	1062:1100	distinct pathogen recognition receptors	1062:1100	The TLR3-ECD structure indicates how LRR loops can establish distinct pathogen recognition receptors.
16043704	6	31	theme	concave	883:889	arg1	surface					891:897	the molecule's concave surface	868:897	the molecule's concave surface	868:897	The extensive beta-sheet on the molecule's concave surface forms a platform for several modifications, including insertions in the LRRs and 11 N-linked glycans.
16043704	5	32	theme	horseshoe-shaped	706:721	arg1	structure					723:731	The overall horseshoe-shaped structure	694:731	The overall horseshoe-shaped structure of the TLR3-ECD	694:747	The overall horseshoe-shaped structure of the TLR3-ECD is formed by 23 repeating LRRs that are capped at each end by specialized non-LRR domains.
16043704	2	33	theme	innate	199:204	arg1	system					213:218	the innate immune system	195:218	the innate immune system	195:218	Toll-like receptors (TLRs) act as sentinels of the innate immune system, sensing a variety of ligands from lipopolysaccharide to flagellin to dsRNA through their ligand-binding domain that is composed of leucine-rich repeats (LRRs).
16043704	3	34	theme	inflammation	461:472	arg1	mediators					474:482	inflammation mediators	461:482	inflammation mediators	461:482	Ligand binding initiates a signaling cascade that leads to the up-regulation of inflammation mediators.
16043704	0	35	theme	receptor	41:48	arg1	structure					14:22	The molecular structure	0:22	The molecular structure of the Toll-like receptor	0:48	The molecular structure of the Toll-like receptor 3 ligand-binding domain.
16043704	2	36	theme	ligand-binding	310:323	arg1	domain					325:330	their ligand-binding domain	304:330	their ligand-binding domain that is composed of leucine-rich repeats (LRRs)	304:378	Toll-like receptors (TLRs) act as sentinels of the innate immune system, sensing a variety of ligands from lipopolysaccharide to flagellin to dsRNA through their ligand-binding domain that is composed of leucine-rich repeats (LRRs).
16043704	1	37	theme	defense	112:118	arg1	line					104:107	the first line	94:107	the first line of defense against invading pathogens	94:145	Innate immunity is the first line of defense against invading pathogens.
16043704	1	37	theme	defense	112:118	arg1	immunity					82:89	Innate immunity	75:89	Innate immunity	75:89	Innate immunity is the first line of defense against invading pathogens.
16043704	4	38	theme	TLR3	565:568	arg1	TLR3					565:568	human TLR3	559:568	human TLR3	559:568	In this study, we have expressed and crystallized the ectodomain (ECD) of human TLR3, which recognizes dsRNA, a molecular signature of viruses, and have determined the molecular structure to 2.4-A resolution.
16043704	4	38	theme	TLR3	565:568	arg1	ECD					551:553	ECD	551:553	ECD	551:553	In this study, we have expressed and crystallized the ectodomain (ECD) of human TLR3, which recognizes dsRNA, a molecular signature of viruses, and have determined the molecular structure to 2.4-A resolution.
16043704	4	38	theme	TLR3	565:568	arg1	ectodomain					539:548	the ectodomain	535:548	the ectodomain (ECD) of human TLR3, which recognizes dsRNA, a molecular signature of viruses	535:626	In this study, we have expressed and crystallized the ectodomain (ECD) of human TLR3, which recognizes dsRNA, a molecular signature of viruses, and have determined the molecular structure to 2.4-A resolution.
16043704	2	39	from	lipopolysaccharide	255:272	arg1	ligands					242:248	ligands	242:248	ligands from lipopolysaccharide	242:272	Toll-like receptors (TLRs) act as sentinels of the innate immune system, sensing a variety of ligands from lipopolysaccharide to flagellin to dsRNA through their ligand-binding domain that is composed of leucine-rich repeats (LRRs).
16043704	2	39	from	lipopolysaccharide	255:272	arg1	variety					231:237	a variety	229:237	a variety of ligands from lipopolysaccharide to flagellin to dsRNA	229:294	Toll-like receptors (TLRs) act as sentinels of the innate immune system, sensing a variety of ligands from lipopolysaccharide to flagellin to dsRNA through their ligand-binding domain that is composed of leucine-rich repeats (LRRs).
16043704	4	40	theme	human	559:563	arg1	TLR3					565:568	human TLR3	559:568	human TLR3	559:568	In this study, we have expressed and crystallized the ectodomain (ECD) of human TLR3, which recognizes dsRNA, a molecular signature of viruses, and have determined the molecular structure to 2.4-A resolution.
16043704	5	41	theme	overall	698:704	arg1	structure					723:731	The overall horseshoe-shaped structure	694:731	The overall horseshoe-shaped structure of the TLR3-ECD	694:747	The overall horseshoe-shaped structure of the TLR3-ECD is formed by 23 repeating LRRs that are capped at each end by specialized non-LRR domains.
16043704	1	42	theme	invading	128:135	arg1	pathogens					137:145	invading pathogens	128:145	invading pathogens	128:145	Innate immunity is the first line of defense against invading pathogens.
16043704	0	43	theme	ligand-binding	52:65	arg1	domain					67:72	3 ligand-binding domain	50:72	3 ligand-binding domain	50:72	The molecular structure of the Toll-like receptor 3 ligand-binding domain.
19764817	9	0	theme	diamine	1221:1227	arg1	oxidases					1229:1236	all diamine oxidases	1217:1236	all diamine oxidases	1217:1236	The inhibitor binding suggests that an aspartic acid residue, conserved in all diamine oxidases but absent from other amine oxidases, is responsible for the diamine specificity by interacting with the second amino group of preferred diamine substrates.
19764817	5	1	theme	active	495:500	arg1	one					509:511	one	509:511	one	509:511	Two active sites, one in each subunit, are characterized by the presence of a copper ion and a topaquinone residue formed by the post-translational modification of a tyrosine.
19764817	5	1	theme	active	495:500	arg1	sites					502:506	Two active sites	491:506	Two active sites	491:506	Two active sites, one in each subunit, are characterized by the presence of a copper ion and a topaquinone residue formed by the post-translational modification of a tyrosine.
19764817	2	2	theme	AOC1	152:155	arg1	gene					157:160	the AOC1 gene	148:160	the AOC1 gene	148:160	The product of the AOC1 gene is a so-called diamine oxidase (hDAO), named for its substrate preference for diamines, particularly histamine.
19764817	9	3	theme	second	1343:1348	arg1	substrates					1383:1392	preferred diamine substrates	1365:1392	preferred diamine substrates	1365:1392	The inhibitor binding suggests that an aspartic acid residue, conserved in all diamine oxidases but absent from other amine oxidases, is responsible for the diamine specificity by interacting with the second amino group of preferred diamine substrates.
19764817	9	3	theme	second	1343:1348	arg1	group					1356:1360	the second amino group	1339:1360	the second amino group of preferred diamine substrates	1339:1392	The inhibitor binding suggests that an aspartic acid residue, conserved in all diamine oxidases but absent from other amine oxidases, is responsible for the diamine specificity by interacting with the second amino group of preferred diamine substrates.
19764817	4	4	theme	oxidase	477:483	arg1	fold					485:488	the archetypal amine oxidase fold	456:488	the archetypal amine oxidase fold	456:488	The homodimeric structure has the archetypal amine oxidase fold.
19764817	9	5	from	oxidases	1266:1273	arg1	absent					1242:1247	absent	1242:1247	absent	1242:1247	The inhibitor binding suggests that an aspartic acid residue, conserved in all diamine oxidases but absent from other amine oxidases, is responsible for the diamine specificity by interacting with the second amino group of preferred diamine substrates.
19764817	6	6	theme	semicarbazide	753:765	arg1	oxidase					783:789	semicarbazide sensitive amine oxidase	753:789	semicarbazide sensitive amine oxidase	753:789	Although hDAO shares 37.9% sequence identity with another human copper amine oxidase, semicarbazide sensitive amine oxidase or vascular adhesion protein-1, its substrate binding pocket and entry channel are distinctly different in accord with the different substrate specificities.
19764817	6	6	theme	semicarbazide	753:765	arg1	oxidase					744:750	another human copper amine oxidase	717:750	another human copper amine oxidase	717:750	Although hDAO shares 37.9% sequence identity with another human copper amine oxidase, semicarbazide sensitive amine oxidase or vascular adhesion protein-1, its substrate binding pocket and entry channel are distinctly different in accord with the different substrate specificities.
19764817	6	7	theme	vascular	794:801	arg1	oxidase					744:750	another human copper amine oxidase	717:750	another human copper amine oxidase	717:750	Although hDAO shares 37.9% sequence identity with another human copper amine oxidase, semicarbazide sensitive amine oxidase or vascular adhesion protein-1, its substrate binding pocket and entry channel are distinctly different in accord with the different substrate specificities.
19764817	6	7	theme	vascular	794:801	arg1	protein-1					812:820	vascular adhesion protein-1	794:820	vascular adhesion protein-1	794:820	Although hDAO shares 37.9% sequence identity with another human copper amine oxidase, semicarbazide sensitive amine oxidase or vascular adhesion protein-1, its substrate binding pocket and entry channel are distinctly different in accord with the different substrate specificities.
19764817	9	8	theme	amino	1350:1354	arg1	substrates					1383:1392	preferred diamine substrates	1365:1392	preferred diamine substrates	1365:1392	The inhibitor binding suggests that an aspartic acid residue, conserved in all diamine oxidases but absent from other amine oxidases, is responsible for the diamine specificity by interacting with the second amino group of preferred diamine substrates.
19764817	9	8	theme	amino	1350:1354	arg1	group					1356:1360	the second amino group	1339:1360	the second amino group of preferred diamine substrates	1339:1392	The inhibitor binding suggests that an aspartic acid residue, conserved in all diamine oxidases but absent from other amine oxidases, is responsible for the diamine specificity by interacting with the second amino group of preferred diamine substrates.
19764817	4	9	theme	amine	471:475	arg1	fold					485:488	the archetypal amine oxidase fold	456:488	the archetypal amine oxidase fold	456:488	The homodimeric structure has the archetypal amine oxidase fold.
19764817	5	10	theme	topaquinone	586:596	arg1	residue					598:604	a topaquinone residue	584:604	a topaquinone residue	584:604	Two active sites, one in each subunit, are characterized by the presence of a copper ion and a topaquinone residue formed by the post-translational modification of a tyrosine.
19764817	9	11	dep	residue	1195:1201	arg1	conserved					1204:1212	conserved	1204:1212	conserved in all diamine oxidases	1204:1236	The inhibitor binding suggests that an aspartic acid residue, conserved in all diamine oxidases but absent from other amine oxidases, is responsible for the diamine specificity by interacting with the second amino group of preferred diamine substrates.
19764817	9	11	dep	residue	1195:1201	arg1	absent					1242:1247	absent	1242:1247	absent	1242:1247	The inhibitor binding suggests that an aspartic acid residue, conserved in all diamine oxidases but absent from other amine oxidases, is responsible for the diamine specificity by interacting with the second amino group of preferred diamine substrates.
19764817	4	12	theme	homodimeric	430:440	arg1	structure					442:450	The homodimeric structure	426:450	The homodimeric structure	426:450	The homodimeric structure has the archetypal amine oxidase fold.
19764817	5	13	theme	residue	598:604	arg1	presence					555:562	the presence	551:562	the presence of a copper ion and a topaquinone residue formed by the post-translational modification of a tyrosine	551:664	Two active sites, one in each subunit, are characterized by the presence of a copper ion and a topaquinone residue formed by the post-translational modification of a tyrosine.
19764817	3	14	theme	insect	312:317	arg1	cells					319:323	insect cells	312:323	insect cells	312:323	hDAO has been cloned and expressed in insect cells and the structure of the native enzyme determined by X-ray crystallography to a resolution of 1.8 A.
19764817	6	15	theme	binding	837:843	arg1	pocket					845:850	its substrate binding pocket	823:850	its substrate binding pocket	823:850	Although hDAO shares 37.9% sequence identity with another human copper amine oxidase, semicarbazide sensitive amine oxidase or vascular adhesion protein-1, its substrate binding pocket and entry channel are distinctly different in accord with the different substrate specificities.
19764817	6	16	theme	amine	738:742	arg1	oxidase					783:789	semicarbazide sensitive amine oxidase	753:789	semicarbazide sensitive amine oxidase	753:789	Although hDAO shares 37.9% sequence identity with another human copper amine oxidase, semicarbazide sensitive amine oxidase or vascular adhesion protein-1, its substrate binding pocket and entry channel are distinctly different in accord with the different substrate specificities.
19764817	6	16	theme	amine	738:742	arg1	oxidase					744:750	another human copper amine oxidase	717:750	another human copper amine oxidase	717:750	Although hDAO shares 37.9% sequence identity with another human copper amine oxidase, semicarbazide sensitive amine oxidase or vascular adhesion protein-1, its substrate binding pocket and entry channel are distinctly different in accord with the different substrate specificities.
19764817	6	16	theme	amine	738:742	arg1	protein-1					812:820	vascular adhesion protein-1	794:820	vascular adhesion protein-1	794:820	Although hDAO shares 37.9% sequence identity with another human copper amine oxidase, semicarbazide sensitive amine oxidase or vascular adhesion protein-1, its substrate binding pocket and entry channel are distinctly different in accord with the different substrate specificities.
19764817	9	17	theme	preferred	1365:1373	arg1	substrates					1383:1392	preferred diamine substrates	1365:1392	preferred diamine substrates	1365:1392	The inhibitor binding suggests that an aspartic acid residue, conserved in all diamine oxidases but absent from other amine oxidases, is responsible for the diamine specificity by interacting with the second amino group of preferred diamine substrates.
19764817	6	18	theme	substrate	827:835	arg1	pocket					845:850	its substrate binding pocket	823:850	its substrate binding pocket	823:850	Although hDAO shares 37.9% sequence identity with another human copper amine oxidase, semicarbazide sensitive amine oxidase or vascular adhesion protein-1, its substrate binding pocket and entry channel are distinctly different in accord with the different substrate specificities.
19764817	9	19	theme	inhibitor	1146:1154	arg1	binding					1156:1162	The inhibitor binding	1142:1162	The inhibitor binding	1142:1162	The inhibitor binding suggests that an aspartic acid residue, conserved in all diamine oxidases but absent from other amine oxidases, is responsible for the diamine specificity by interacting with the second amino group of preferred diamine substrates.
19764817	6	20	theme	copper	731:736	arg1	oxidase					783:789	semicarbazide sensitive amine oxidase	753:789	semicarbazide sensitive amine oxidase	753:789	Although hDAO shares 37.9% sequence identity with another human copper amine oxidase, semicarbazide sensitive amine oxidase or vascular adhesion protein-1, its substrate binding pocket and entry channel are distinctly different in accord with the different substrate specificities.
19764817	6	20	theme	copper	731:736	arg1	oxidase					744:750	another human copper amine oxidase	717:750	another human copper amine oxidase	717:750	Although hDAO shares 37.9% sequence identity with another human copper amine oxidase, semicarbazide sensitive amine oxidase or vascular adhesion protein-1, its substrate binding pocket and entry channel are distinctly different in accord with the different substrate specificities.
19764817	6	20	theme	copper	731:736	arg1	protein-1					812:820	vascular adhesion protein-1	794:820	vascular adhesion protein-1	794:820	Although hDAO shares 37.9% sequence identity with another human copper amine oxidase, semicarbazide sensitive amine oxidase or vascular adhesion protein-1, its substrate binding pocket and entry channel are distinctly different in accord with the different substrate specificities.
19764817	1	21	theme	functioning	69:79	arg1	oxidases					123:130	copper-containing amine oxidases	99:130	copper-containing amine oxidases	99:130	Humans have three functioning genes that encode copper-containing amine oxidases.
19764817	1	21	theme	functioning	69:79	arg1	genes					81:85	three functioning genes	63:85	three functioning genes that encode copper-containing amine oxidases	63:130	Humans have three functioning genes that encode copper-containing amine oxidases.
19764817	9	22	theme	aspartic	1181:1188	arg1	responsible					1279:1289	responsible	1279:1289	responsible	1279:1289	The inhibitor binding suggests that an aspartic acid residue, conserved in all diamine oxidases but absent from other amine oxidases, is responsible for the diamine specificity by interacting with the second amino group of preferred diamine substrates.
19764817	9	22	theme	aspartic	1181:1188	arg1	residue					1195:1201	an aspartic acid residue	1178:1201	an aspartic acid residue	1178:1201	The inhibitor binding suggests that an aspartic acid residue, conserved in all diamine oxidases but absent from other amine oxidases, is responsible for the diamine specificity by interacting with the second amino group of preferred diamine substrates.
19764817	9	23	theme	diamine	1375:1381	arg1	substrates					1383:1392	preferred diamine substrates	1365:1392	preferred diamine substrates	1365:1392	The inhibitor binding suggests that an aspartic acid residue, conserved in all diamine oxidases but absent from other amine oxidases, is responsible for the diamine specificity by interacting with the second amino group of preferred diamine substrates.
19764817	8	24	theme	active-site	1121:1131	arg1	channel					1133:1139	the active-site channel	1117:1139	the active-site channel	1117:1139	They bind noncovalently in the active-site channel.
19764817	9	25	theme	amine	1260:1264	arg1	oxidases					1266:1273	other amine oxidases	1254:1273	other amine oxidases	1254:1273	The inhibitor binding suggests that an aspartic acid residue, conserved in all diamine oxidases but absent from other amine oxidases, is responsible for the diamine specificity by interacting with the second amino group of preferred diamine substrates.
19764817	5	26	theme	copper	569:574	arg1	ion					576:578	a copper ion	567:578	a copper ion	567:578	Two active sites, one in each subunit, are characterized by the presence of a copper ion and a topaquinone residue formed by the post-translational modification of a tyrosine.
19764817	6	27	theme	human	725:729	arg1	oxidase					783:789	semicarbazide sensitive amine oxidase	753:789	semicarbazide sensitive amine oxidase	753:789	Although hDAO shares 37.9% sequence identity with another human copper amine oxidase, semicarbazide sensitive amine oxidase or vascular adhesion protein-1, its substrate binding pocket and entry channel are distinctly different in accord with the different substrate specificities.
19764817	6	27	theme	human	725:729	arg1	oxidase					744:750	another human copper amine oxidase	717:750	another human copper amine oxidase	717:750	Although hDAO shares 37.9% sequence identity with another human copper amine oxidase, semicarbazide sensitive amine oxidase or vascular adhesion protein-1, its substrate binding pocket and entry channel are distinctly different in accord with the different substrate specificities.
19764817	6	27	theme	human	725:729	arg1	protein-1					812:820	vascular adhesion protein-1	794:820	vascular adhesion protein-1	794:820	Although hDAO shares 37.9% sequence identity with another human copper amine oxidase, semicarbazide sensitive amine oxidase or vascular adhesion protein-1, its substrate binding pocket and entry channel are distinctly different in accord with the different substrate specificities.
19764817	9	28	theme	substrates	1383:1392	arg1	substrates					1383:1392	preferred diamine substrates	1365:1392	preferred diamine substrates	1365:1392	The inhibitor binding suggests that an aspartic acid residue, conserved in all diamine oxidases but absent from other amine oxidases, is responsible for the diamine specificity by interacting with the second amino group of preferred diamine substrates.
19764817	9	28	theme	substrates	1383:1392	arg1	group					1356:1360	the second amino group	1339:1360	the second amino group of preferred diamine substrates	1339:1392	The inhibitor binding suggests that an aspartic acid residue, conserved in all diamine oxidases but absent from other amine oxidases, is responsible for the diamine specificity by interacting with the second amino group of preferred diamine substrates.
19764817	3	29	theme	native	350:355	arg1	enzyme					357:362	the native enzyme	346:362	the native enzyme	346:362	hDAO has been cloned and expressed in insect cells and the structure of the native enzyme determined by X-ray crystallography to a resolution of 1.8 A.
19764817	6	30	theme	substrate	924:932	arg1	specificities					934:946	the different substrate specificities	910:946	the different substrate specificities	910:946	Although hDAO shares 37.9% sequence identity with another human copper amine oxidase, semicarbazide sensitive amine oxidase or vascular adhesion protein-1, its substrate binding pocket and entry channel are distinctly different in accord with the different substrate specificities.
19764817	5	31	theme	ion	576:578	arg1	presence					555:562	the presence	551:562	the presence of a copper ion and a topaquinone residue formed by the post-translational modification of a tyrosine	551:664	Two active sites, one in each subunit, are characterized by the presence of a copper ion and a topaquinone residue formed by the post-translational modification of a tyrosine.
19764817	6	32	theme	different	914:922	arg1	specificities					934:946	the different substrate specificities	910:946	the different substrate specificities	910:946	Although hDAO shares 37.9% sequence identity with another human copper amine oxidase, semicarbazide sensitive amine oxidase or vascular adhesion protein-1, its substrate binding pocket and entry channel are distinctly different in accord with the different substrate specificities.
19764817	3	33	theme	A	423:423	arg1	resolution					405:414	a resolution	403:414	a resolution of 1.8 A	403:423	hDAO has been cloned and expressed in insect cells and the structure of the native enzyme determined by X-ray crystallography to a resolution of 1.8 A.
19764817	1	34	contain	have	58:61	arg1	Humans					51:56	Humans	51:56	Humans	51:56	Humans have three functioning genes that encode copper-containing amine oxidases.
19764817	1	34	contain	have	58:61	arg2	genes					81:85	three functioning genes	63:85	three functioning genes that encode copper-containing amine oxidases	63:130	Humans have three functioning genes that encode copper-containing amine oxidases.
19764817	1	34	contain	have	58:61	arg2	oxidases					123:130	copper-containing amine oxidases	99:130	copper-containing amine oxidases	99:130	Humans have three functioning genes that encode copper-containing amine oxidases.
19764817	2	35	theme	so-called	167:175	arg1	oxidase					185:191	a so-called diamine oxidase	165:191	a so-called diamine oxidase (hDAO)	165:198	The product of the AOC1 gene is a so-called diamine oxidase (hDAO), named for its substrate preference for diamines, particularly histamine.
19764817	2	35	theme	so-called	167:175	arg1	histamine					263:271	histamine	263:271	histamine	263:271	The product of the AOC1 gene is a so-called diamine oxidase (hDAO), named for its substrate preference for diamines, particularly histamine.
19764817	2	35	theme	so-called	167:175	arg1	product					137:143	The product	133:143	The product of the AOC1 gene	133:160	The product of the AOC1 gene is a so-called diamine oxidase (hDAO), named for its substrate preference for diamines, particularly histamine.
19764817	2	35	theme	so-called	167:175	arg1	hDAO					194:197	hDAO	194:197	hDAO	194:197	The product of the AOC1 gene is a so-called diamine oxidase (hDAO), named for its substrate preference for diamines, particularly histamine.
19764817	1	36	theme	copper-containing	99:115	arg1	oxidases					123:130	copper-containing amine oxidases	99:130	copper-containing amine oxidases	99:130	Humans have three functioning genes that encode copper-containing amine oxidases.
19764817	1	36	theme	copper-containing	99:115	arg1	genes					81:85	three functioning genes	63:85	three functioning genes that encode copper-containing amine oxidases	63:130	Humans have three functioning genes that encode copper-containing amine oxidases.
19764817	0	37	theme	diamine	34:40	arg1	oxidase					42:48	human diamine oxidase	28:48	human diamine oxidase	28:48	Structure and inhibition of human diamine oxidase.
19764817	5	38	theme	tyrosine	657:664	arg1	modification					639:650	the post-translational modification	616:650	the post-translational modification of a tyrosine	616:664	Two active sites, one in each subunit, are characterized by the presence of a copper ion and a topaquinone residue formed by the post-translational modification of a tyrosine.
19764817	0	39	theme	human	28:32	arg1	oxidase					42:48	human diamine oxidase	28:48	human diamine oxidase	28:48	Structure and inhibition of human diamine oxidase.
19764817	3	40	theme	X-ray	378:382	arg1	crystallography					384:398	X-ray crystallography	378:398	X-ray crystallography	378:398	hDAO has been cloned and expressed in insect cells and the structure of the native enzyme determined by X-ray crystallography to a resolution of 1.8 A.
19764817	6	41	theme	adhesion	803:810	arg1	oxidase					744:750	another human copper amine oxidase	717:750	another human copper amine oxidase	717:750	Although hDAO shares 37.9% sequence identity with another human copper amine oxidase, semicarbazide sensitive amine oxidase or vascular adhesion protein-1, its substrate binding pocket and entry channel are distinctly different in accord with the different substrate specificities.
19764817	6	41	theme	adhesion	803:810	arg1	protein-1					812:820	vascular adhesion protein-1	794:820	vascular adhesion protein-1	794:820	Although hDAO shares 37.9% sequence identity with another human copper amine oxidase, semicarbazide sensitive amine oxidase or vascular adhesion protein-1, its substrate binding pocket and entry channel are distinctly different in accord with the different substrate specificities.
19764817	7	42	theme	hDAO	994:997	arg1	complexes					981:989	two inhibitor complexes	967:989	two inhibitor complexes of hDAO	967:997	The structures of two inhibitor complexes of hDAO, berenil and pentamidine, have been refined to resolutions of 2.1 and 2.2 A, respectively.
19764817	7	43	theme	inhibitor	971:979	arg1	complexes					981:989	two inhibitor complexes	967:989	two inhibitor complexes of hDAO	967:997	The structures of two inhibitor complexes of hDAO, berenil and pentamidine, have been refined to resolutions of 2.1 and 2.2 A, respectively.
19764817	3	44	theme	enzyme	357:362	arg1	structure					333:341	the structure	329:341	the structure of the native enzyme	329:362	hDAO has been cloned and expressed in insect cells and the structure of the native enzyme determined by X-ray crystallography to a resolution of 1.8 A.
19764817	2	45	theme	gene	157:160	arg1	oxidase					185:191	a so-called diamine oxidase	165:191	a so-called diamine oxidase (hDAO)	165:198	The product of the AOC1 gene is a so-called diamine oxidase (hDAO), named for its substrate preference for diamines, particularly histamine.
19764817	2	45	theme	gene	157:160	arg1	product					137:143	The product	133:143	The product of the AOC1 gene	133:160	The product of the AOC1 gene is a so-called diamine oxidase (hDAO), named for its substrate preference for diamines, particularly histamine.
19764817	6	46	theme	sequence	694:701	arg1	identity					703:710	37.9% sequence identity	688:710	37.9% sequence identity	688:710	Although hDAO shares 37.9% sequence identity with another human copper amine oxidase, semicarbazide sensitive amine oxidase or vascular adhesion protein-1, its substrate binding pocket and entry channel are distinctly different in accord with the different substrate specificities.
19764817	1	47	theme	amine	117:121	arg1	oxidases					123:130	copper-containing amine oxidases	99:130	copper-containing amine oxidases	99:130	Humans have three functioning genes that encode copper-containing amine oxidases.
19764817	1	47	theme	amine	117:121	arg1	genes					81:85	three functioning genes	63:85	three functioning genes that encode copper-containing amine oxidases	63:130	Humans have three functioning genes that encode copper-containing amine oxidases.
19764817	0	48	theme	oxidase	42:48	arg1	inhibition					14:23	inhibition	14:23	inhibition	14:23	Structure and inhibition of human diamine oxidase.
19764817	0	48	theme	oxidase	42:48	arg1	Structure					0:8	Structure	0:8	Structure	0:8	Structure and inhibition of human diamine oxidase.
19764817	9	49	theme	diamine	1299:1305	arg1	specificity					1307:1317	the diamine specificity	1295:1317	the diamine specificity	1295:1317	The inhibitor binding suggests that an aspartic acid residue, conserved in all diamine oxidases but absent from other amine oxidases, is responsible for the diamine specificity by interacting with the second amino group of preferred diamine substrates.
19764817	6	50	theme	entry	856:860	arg1	channel					862:868	entry channel	856:868	entry channel	856:868	Although hDAO shares 37.9% sequence identity with another human copper amine oxidase, semicarbazide sensitive amine oxidase or vascular adhesion protein-1, its substrate binding pocket and entry channel are distinctly different in accord with the different substrate specificities.
19764817	9	51	theme	acid	1190:1193	arg1	responsible					1279:1289	responsible	1279:1289	responsible	1279:1289	The inhibitor binding suggests that an aspartic acid residue, conserved in all diamine oxidases but absent from other amine oxidases, is responsible for the diamine specificity by interacting with the second amino group of preferred diamine substrates.
19764817	9	51	theme	acid	1190:1193	arg1	residue					1195:1201	an aspartic acid residue	1178:1201	an aspartic acid residue	1178:1201	The inhibitor binding suggests that an aspartic acid residue, conserved in all diamine oxidases but absent from other amine oxidases, is responsible for the diamine specificity by interacting with the second amino group of preferred diamine substrates.
19764817	6	52	theme	%	692:692	arg1	identity					703:710	37.9% sequence identity	688:710	37.9% sequence identity	688:710	Although hDAO shares 37.9% sequence identity with another human copper amine oxidase, semicarbazide sensitive amine oxidase or vascular adhesion protein-1, its substrate binding pocket and entry channel are distinctly different in accord with the different substrate specificities.
19764817	4	53	contain	has	452:454	arg1	structure					442:450	The homodimeric structure	426:450	The homodimeric structure	426:450	The homodimeric structure has the archetypal amine oxidase fold.
19764817	4	53	contain	has	452:454	arg2	fold					485:488	the archetypal amine oxidase fold	456:488	the archetypal amine oxidase fold	456:488	The homodimeric structure has the archetypal amine oxidase fold.
19764817	9	54	theme	other	1254:1258	arg1	oxidases					1266:1273	other amine oxidases	1254:1273	other amine oxidases	1254:1273	The inhibitor binding suggests that an aspartic acid residue, conserved in all diamine oxidases but absent from other amine oxidases, is responsible for the diamine specificity by interacting with the second amino group of preferred diamine substrates.
19764817	6	55	theme	37.9	688:691	arg1	%					692:692	%	692:692	%	692:692	Although hDAO shares 37.9% sequence identity with another human copper amine oxidase, semicarbazide sensitive amine oxidase or vascular adhesion protein-1, its substrate binding pocket and entry channel are distinctly different in accord with the different substrate specificities.
19764817	5	56	theme	post-translational	620:637	arg1	modification					639:650	the post-translational modification	616:650	the post-translational modification of a tyrosine	616:664	Two active sites, one in each subunit, are characterized by the presence of a copper ion and a topaquinone residue formed by the post-translational modification of a tyrosine.
19764817	6	57	theme	amine	777:781	arg1	oxidase					783:789	semicarbazide sensitive amine oxidase	753:789	semicarbazide sensitive amine oxidase	753:789	Although hDAO shares 37.9% sequence identity with another human copper amine oxidase, semicarbazide sensitive amine oxidase or vascular adhesion protein-1, its substrate binding pocket and entry channel are distinctly different in accord with the different substrate specificities.
19764817	6	57	theme	amine	777:781	arg1	oxidase					744:750	another human copper amine oxidase	717:750	another human copper amine oxidase	717:750	Although hDAO shares 37.9% sequence identity with another human copper amine oxidase, semicarbazide sensitive amine oxidase or vascular adhesion protein-1, its substrate binding pocket and entry channel are distinctly different in accord with the different substrate specificities.
19764817	7	58	theme	complexes	981:989	arg1	pentamidine					1012:1022	pentamidine	1012:1022	pentamidine	1012:1022	The structures of two inhibitor complexes of hDAO, berenil and pentamidine, have been refined to resolutions of 2.1 and 2.2 A, respectively.
19764817	7	58	theme	complexes	981:989	arg1	structures					953:962	The structures	949:962	The structures of two inhibitor complexes of hDAO	949:997	The structures of two inhibitor complexes of hDAO, berenil and pentamidine, have been refined to resolutions of 2.1 and 2.2 A, respectively.
19764817	7	58	theme	complexes	981:989	arg1	berenil					1000:1006	berenil	1000:1006	berenil	1000:1006	The structures of two inhibitor complexes of hDAO, berenil and pentamidine, have been refined to resolutions of 2.1 and 2.2 A, respectively.
19764817	2	59	theme	diamine	177:183	arg1	oxidase					185:191	a so-called diamine oxidase	165:191	a so-called diamine oxidase (hDAO)	165:198	The product of the AOC1 gene is a so-called diamine oxidase (hDAO), named for its substrate preference for diamines, particularly histamine.
19764817	2	59	theme	diamine	177:183	arg1	histamine					263:271	histamine	263:271	histamine	263:271	The product of the AOC1 gene is a so-called diamine oxidase (hDAO), named for its substrate preference for diamines, particularly histamine.
19764817	2	59	theme	diamine	177:183	arg1	product					137:143	The product	133:143	The product of the AOC1 gene	133:160	The product of the AOC1 gene is a so-called diamine oxidase (hDAO), named for its substrate preference for diamines, particularly histamine.
19764817	2	59	theme	diamine	177:183	arg1	hDAO					194:197	hDAO	194:197	hDAO	194:197	The product of the AOC1 gene is a so-called diamine oxidase (hDAO), named for its substrate preference for diamines, particularly histamine.
19764817	2	60	theme	substrate	215:223	arg1	preference					225:234	its substrate preference	211:234	its substrate preference for diamines	211:247	The product of the AOC1 gene is a so-called diamine oxidase (hDAO), named for its substrate preference for diamines, particularly histamine.
19764817	5	61	from	one	509:511	arg1	subunit					521:527	each subunit	516:527	each subunit	516:527	Two active sites, one in each subunit, are characterized by the presence of a copper ion and a topaquinone residue formed by the post-translational modification of a tyrosine.
19764817	6	62	theme	sensitive	767:775	arg1	oxidase					783:789	semicarbazide sensitive amine oxidase	753:789	semicarbazide sensitive amine oxidase	753:789	Although hDAO shares 37.9% sequence identity with another human copper amine oxidase, semicarbazide sensitive amine oxidase or vascular adhesion protein-1, its substrate binding pocket and entry channel are distinctly different in accord with the different substrate specificities.
19764817	6	62	theme	sensitive	767:775	arg1	oxidase					744:750	another human copper amine oxidase	717:750	another human copper amine oxidase	717:750	Although hDAO shares 37.9% sequence identity with another human copper amine oxidase, semicarbazide sensitive amine oxidase or vascular adhesion protein-1, its substrate binding pocket and entry channel are distinctly different in accord with the different substrate specificities.
19764817	7	63	theme	A	1073:1073	arg1	resolutions					1046:1056	resolutions	1046:1056	resolutions of 2.1 and 2.2 A	1046:1073	The structures of two inhibitor complexes of hDAO, berenil and pentamidine, have been refined to resolutions of 2.1 and 2.2 A, respectively.
19764817	4	64	theme	archetypal	460:469	arg1	fold					485:488	the archetypal amine oxidase fold	456:488	the archetypal amine oxidase fold	456:488	The homodimeric structure has the archetypal amine oxidase fold.
11531339	0	0	theme	Ri	64:65	arg1	analysis					4:11	The analysis	0:11	The analysis of the human high affinity IgE receptor Fc epsilon Ri	0:65	The analysis of the human high affinity IgE receptor Fc epsilon Ri alpha from multiple crystal forms.
11531339	7	1	theme	new	1049:1051	arg1	directions					1053:1062	new directions	1049:1062	new directions for the design of molecules to inhibit the interaction of Fc epsilon RI alpha with its natural ligand and thus to prevent a primary step in the allergic response	1049:1224	The results of this study point to new directions for the design of molecules to inhibit the interaction of Fc epsilon RI alpha with its natural ligand and thus to prevent a primary step in the allergic response.
11531339	3	2	contain	has	474:476	arg1	receptor					465:472	the receptor	461:472	the receptor	461:472	However, the receptor has local conformational variability in the C' strand of D2 and in the BC loop of D1.
11531339	3	2	contain	has	474:476	arg2	variability					499:509	local conformational variability	478:509	local conformational variability	478:509	However, the receptor has local conformational variability in the C' strand of D2 and in the BC loop of D1.
11531339	0	3	theme	epsilon	56:62	arg1	Ri					64:65	the human high affinity IgE receptor Fc epsilon Ri	16:65	the human high affinity IgE receptor Fc epsilon Ri	16:65	The analysis of the human high affinity IgE receptor Fc epsilon Ri alpha from multiple crystal forms.
11531339	6	4	from	contacts	841:848	arg1	forms					867:871	the different forms	853:871	the different forms	853:871	An analysis of crystal contacts in the different forms indicates regions where the molecule interacts with other proteins, and reveals a potential new binding site distal to the IgE binding site.
11531339	1	5	from	structure	121:129	arg1	forms					218:222	six different crystal forms	196:222	six different crystal forms	196:222	We have solved the structure of the human high affinity IgE receptor, Fc epsilon RI alpha, in six different crystal forms, showing the structure in 15 different chemical environments.
11531339	6	6	theme	other	925:929	arg1	proteins					931:938	other proteins	925:938	other proteins	925:938	An analysis of crystal contacts in the different forms indicates regions where the molecule interacts with other proteins, and reveals a potential new binding site distal to the IgE binding site.
11531339	3	7	theme	D1	556:557	arg1	loop					548:551	the BC loop	541:551	the BC loop of D1	541:557	However, the receptor has local conformational variability in the C' strand of D2 and in the BC loop of D1.
11531339	1	8	from	structure	237:245	arg1	environments					272:283	15 different chemical environments	250:283	15 different chemical environments	250:283	We have solved the structure of the human high affinity IgE receptor, Fc epsilon RI alpha, in six different crystal forms, showing the structure in 15 different chemical environments.
11531339	7	9	dep	design	1072:1077	arg1	inhibit					1095:1101	inhibit	1095:1101	to inhibit the interaction of Fc epsilon RI alpha with its natural ligand	1092:1164	The results of this study point to new directions for the design of molecules to inhibit the interaction of Fc epsilon RI alpha with its natural ligand and thus to prevent a primary step in the allergic response.
11531339	7	9	dep	design	1072:1077	arg1	prevent					1178:1184	prevent	1178:1184	thus to prevent a primary step in the allergic response	1170:1224	The results of this study point to new directions for the design of molecules to inhibit the interaction of Fc epsilon RI alpha with its natural ligand and thus to prevent a primary step in the allergic response.
11531339	7	10	theme	primary	1188:1194	arg1	step					1196:1199	a primary step	1186:1199	a primary step in the allergic response	1186:1224	The results of this study point to new directions for the design of molecules to inhibit the interaction of Fc epsilon RI alpha with its natural ligand and thus to prevent a primary step in the allergic response.
11531339	1	11	theme	different	200:208	arg1	forms					218:222	six different crystal forms	196:222	six different crystal forms	196:222	We have solved the structure of the human high affinity IgE receptor, Fc epsilon RI alpha, in six different crystal forms, showing the structure in 15 different chemical environments.
11531339	4	12	from	ligand	690:695	arg1	position					655:662	the position	651:662	the position of a proline from the IgE ligand	651:695	In every crystal form, a residue inserts between tryptophan residues 87 and 110, mimicking the position of a proline from the IgE ligand.
11531339	4	12	from	ligand	690:695	arg1	proline					669:675	a proline	667:675	a proline from the IgE ligand	667:695	In every crystal form, a residue inserts between tryptophan residues 87 and 110, mimicking the position of a proline from the IgE ligand.
11531339	6	13	theme	binding	1000:1006	arg1	site					1008:1011	the IgE binding site	992:1011	the IgE binding site	992:1011	An analysis of crystal contacts in the different forms indicates regions where the molecule interacts with other proteins, and reveals a potential new binding site distal to the IgE binding site.
11531339	4	14	theme	tryptophan	609:618	arg1	residues					620:627	tryptophan residues 87 and 110	609:638	residues	620:627	In every crystal form, a residue inserts between tryptophan residues 87 and 110, mimicking the position of a proline from the IgE ligand.
11531339	1	15	theme	crystal	210:216	arg1	forms					218:222	six different crystal forms	196:222	six different crystal forms	196:222	We have solved the structure of the human high affinity IgE receptor, Fc epsilon RI alpha, in six different crystal forms, showing the structure in 15 different chemical environments.
11531339	0	16	theme	crystal	87:93	arg1	forms					95:99	multiple crystal forms	78:99	multiple crystal forms	78:99	The analysis of the human high affinity IgE receptor Fc epsilon Ri alpha from multiple crystal forms.
11531339	6	17	theme	new	965:967	arg1	site					977:980	a potential new binding site	953:980	a potential new binding site distal to the IgE binding site	953:1011	An analysis of crystal contacts in the different forms indicates regions where the molecule interacts with other proteins, and reveals a potential new binding site distal to the IgE binding site.
11531339	6	18	from	analysis	821:828	arg1	forms					867:871	the different forms	853:871	the different forms	853:871	An analysis of crystal contacts in the different forms indicates regions where the molecule interacts with other proteins, and reveals a potential new binding site distal to the IgE binding site.
11531339	5	19	theme	structure	807:815	arg1	surfaces					791:798	the front and back surfaces	772:798	surfaces	791:798	The different crystal forms reveal a distribution of carbohydrates lining the front and back surfaces of the structure.
11531339	5	20	theme	different	702:710	arg1	forms					720:724	The different crystal forms	698:724	The different crystal forms	698:724	The different crystal forms reveal a distribution of carbohydrates lining the front and back surfaces of the structure.
11531339	7	21	theme	RI	1133:1134	arg1	alpha					1136:1140	Fc epsilon RI alpha	1122:1140	Fc epsilon RI alpha	1122:1140	The results of this study point to new directions for the design of molecules to inhibit the interaction of Fc epsilon RI alpha with its natural ligand and thus to prevent a primary step in the allergic response.
11531339	0	22	theme	multiple	78:85	arg1	forms					95:99	multiple crystal forms	78:99	multiple crystal forms	78:99	The analysis of the human high affinity IgE receptor Fc epsilon Ri alpha from multiple crystal forms.
11531339	6	23	theme	crystal	833:839	arg1	contacts					841:848	crystal contacts	833:848	crystal contacts in the different forms	833:871	An analysis of crystal contacts in the different forms indicates regions where the molecule interacts with other proteins, and reveals a potential new binding site distal to the IgE binding site.
11531339	5	24	dep	carbohydrates	751:763	arg1	lining					765:770	lining	765:770	lining	765:770	The different crystal forms reveal a distribution of carbohydrates lining the front and back surfaces of the structure.
11531339	1	25	theme	human	138:142	arg1	alpha					186:190	Fc epsilon RI alpha	172:190	Fc epsilon RI alpha	172:190	We have solved the structure of the human high affinity IgE receptor, Fc epsilon RI alpha, in six different crystal forms, showing the structure in 15 different chemical environments.
11531339	1	25	theme	human	138:142	arg1	receptor					162:169	the human high affinity IgE receptor	134:169	the human high affinity IgE receptor	134:169	We have solved the structure of the human high affinity IgE receptor, Fc epsilon RI alpha, in six different crystal forms, showing the structure in 15 different chemical environments.
11531339	7	26	theme	study	1034:1038	arg1	results					1018:1024	The results	1014:1024	The results of this study	1014:1038	The results of this study point to new directions for the design of molecules to inhibit the interaction of Fc epsilon RI alpha with its natural ligand and thus to prevent a primary step in the allergic response.
11531339	6	27	from	forms	867:871	arg1	analysis					821:828	An analysis	818:828	An analysis of crystal contacts in the different forms	818:871	An analysis of crystal contacts in the different forms indicates regions where the molecule interacts with other proteins, and reveals a potential new binding site distal to the IgE binding site.
11531339	5	28	theme	front	776:780	arg1	surfaces					791:798	the front and back surfaces	772:798	surfaces	791:798	The different crystal forms reveal a distribution of carbohydrates lining the front and back surfaces of the structure.
11531339	1	29	theme	high	144:147	arg1	alpha					186:190	Fc epsilon RI alpha	172:190	Fc epsilon RI alpha	172:190	We have solved the structure of the human high affinity IgE receptor, Fc epsilon RI alpha, in six different crystal forms, showing the structure in 15 different chemical environments.
11531339	1	29	theme	high	144:147	arg1	receptor					162:169	the human high affinity IgE receptor	134:169	the human high affinity IgE receptor	134:169	We have solved the structure of the human high affinity IgE receptor, Fc epsilon RI alpha, in six different crystal forms, showing the structure in 15 different chemical environments.
11531339	6	30	theme	different	857:865	arg1	forms					867:871	the different forms	853:871	the different forms	853:871	An analysis of crystal contacts in the different forms indicates regions where the molecule interacts with other proteins, and reveals a potential new binding site distal to the IgE binding site.
11531339	4	31	theme	IgE	686:688	arg1	ligand					690:695	the IgE ligand	682:695	the IgE ligand	682:695	In every crystal form, a residue inserts between tryptophan residues 87 and 110, mimicking the position of a proline from the IgE ligand.
11531339	6	32	theme	distal	982:987	arg1	site					977:980	a potential new binding site	953:980	a potential new binding site distal to the IgE binding site	953:1011	An analysis of crystal contacts in the different forms indicates regions where the molecule interacts with other proteins, and reveals a potential new binding site distal to the IgE binding site.
11531339	1	33	theme	affinity	149:156	arg1	alpha					186:190	Fc epsilon RI alpha	172:190	Fc epsilon RI alpha	172:190	We have solved the structure of the human high affinity IgE receptor, Fc epsilon RI alpha, in six different crystal forms, showing the structure in 15 different chemical environments.
11531339	1	33	theme	affinity	149:156	arg1	receptor					162:169	the human high affinity IgE receptor	134:169	the human high affinity IgE receptor	134:169	We have solved the structure of the human high affinity IgE receptor, Fc epsilon RI alpha, in six different crystal forms, showing the structure in 15 different chemical environments.
11531339	1	34	theme	IgE	158:160	arg1	alpha					186:190	Fc epsilon RI alpha	172:190	Fc epsilon RI alpha	172:190	We have solved the structure of the human high affinity IgE receptor, Fc epsilon RI alpha, in six different crystal forms, showing the structure in 15 different chemical environments.
11531339	1	34	theme	IgE	158:160	arg1	receptor					162:169	the human high affinity IgE receptor	134:169	the human high affinity IgE receptor	134:169	We have solved the structure of the human high affinity IgE receptor, Fc epsilon RI alpha, in six different crystal forms, showing the structure in 15 different chemical environments.
11531339	2	35	theme	molecule	358:365	arg1	shape					345:349	the overall shape	333:349	the overall shape of the molecule	333:365	This database of structures shows no change in the overall shape of the molecule, as the angle between domains 1 and 2 (D1 and D2) varies little across the ensemble.
11531339	6	36	theme	IgE	996:998	arg1	site					1008:1011	the IgE binding site	992:1011	the IgE binding site	992:1011	An analysis of crystal contacts in the different forms indicates regions where the molecule interacts with other proteins, and reveals a potential new binding site distal to the IgE binding site.
11531339	3	37	theme	D2	531:532	arg1	strand					521:526	the C' strand	514:526	the C' strand of D2	514:532	However, the receptor has local conformational variability in the C' strand of D2 and in the BC loop of D1.
11531339	6	38	theme	binding	969:975	arg1	site					977:980	a potential new binding site	953:980	a potential new binding site distal to the IgE binding site	953:1011	An analysis of crystal contacts in the different forms indicates regions where the molecule interacts with other proteins, and reveals a potential new binding site distal to the IgE binding site.
11531339	1	39	theme	receptor	162:169	arg1	structure					121:129	the structure	117:129	the structure of the human high affinity IgE receptor, Fc epsilon RI alpha, in six different crystal forms	117:222	We have solved the structure of the human high affinity IgE receptor, Fc epsilon RI alpha, in six different crystal forms, showing the structure in 15 different chemical environments.
11531339	0	40	theme	high	26:29	arg1	receptor					44:51	the human high affinity IgE receptor	16:51	the human high affinity IgE receptor Fc epsilon Ri	16:65	The analysis of the human high affinity IgE receptor Fc epsilon Ri alpha from multiple crystal forms.
11531339	6	41	theme	potential	955:963	arg1	site					977:980	a potential new binding site	953:980	a potential new binding site distal to the IgE binding site	953:1011	An analysis of crystal contacts in the different forms indicates regions where the molecule interacts with other proteins, and reveals a potential new binding site distal to the IgE binding site.
11531339	7	42	with	interaction	1107:1117	arg1	ligand					1159:1164	its natural ligand	1147:1164	its natural ligand	1147:1164	The results of this study point to new directions for the design of molecules to inhibit the interaction of Fc epsilon RI alpha with its natural ligand and thus to prevent a primary step in the allergic response.
11531339	3	43	theme	local	478:482	arg1	variability					499:509	local conformational variability	478:509	local conformational variability	478:509	However, the receptor has local conformational variability in the C' strand of D2 and in the BC loop of D1.
11531339	5	44	theme	crystal	712:718	arg1	forms					720:724	The different crystal forms	698:724	The different crystal forms	698:724	The different crystal forms reveal a distribution of carbohydrates lining the front and back surfaces of the structure.
11531339	0	45	theme	human	20:24	arg1	receptor					44:51	the human high affinity IgE receptor	16:51	the human high affinity IgE receptor Fc epsilon Ri	16:65	The analysis of the human high affinity IgE receptor Fc epsilon Ri alpha from multiple crystal forms.
11531339	3	46	theme	conformational	484:497	arg1	variability					499:509	local conformational variability	478:509	local conformational variability	478:509	However, the receptor has local conformational variability in the C' strand of D2 and in the BC loop of D1.
11531339	2	47	from	change	323:328	arg1	shape					345:349	the overall shape	333:349	the overall shape of the molecule	333:365	This database of structures shows no change in the overall shape of the molecule, as the angle between domains 1 and 2 (D1 and D2) varies little across the ensemble.
11531339	1	48	theme	Fc	172:173	arg1	RI					183:184	Fc epsilon RI	172:184	Fc epsilon RI alpha	172:190	We have solved the structure of the human high affinity IgE receptor, Fc epsilon RI alpha, in six different crystal forms, showing the structure in 15 different chemical environments.
11531339	0	49	theme	IgE	40:42	arg1	receptor					44:51	the human high affinity IgE receptor	16:51	the human high affinity IgE receptor Fc epsilon Ri	16:65	The analysis of the human high affinity IgE receptor Fc epsilon Ri alpha from multiple crystal forms.
11531339	4	50	theme	proline	669:675	arg1	position					655:662	the position	651:662	the position of a proline from the IgE ligand	651:695	In every crystal form, a residue inserts between tryptophan residues 87 and 110, mimicking the position of a proline from the IgE ligand.
11531339	4	51	theme	crystal	569:575	arg1	form					577:580	every crystal form	563:580	every crystal form	563:580	In every crystal form, a residue inserts between tryptophan residues 87 and 110, mimicking the position of a proline from the IgE ligand.
11531339	0	52	theme	affinity	31:38	arg1	receptor					44:51	the human high affinity IgE receptor	16:51	the human high affinity IgE receptor Fc epsilon Ri	16:65	The analysis of the human high affinity IgE receptor Fc epsilon Ri alpha from multiple crystal forms.
11531339	7	53	theme	epsilon	1125:1131	arg1	RI					1133:1134	Fc epsilon RI	1122:1134	Fc epsilon RI alpha	1122:1140	The results of this study point to new directions for the design of molecules to inhibit the interaction of Fc epsilon RI alpha with its natural ligand and thus to prevent a primary step in the allergic response.
11531339	3	54	theme	BC	545:546	arg1	loop					548:551	the BC loop	541:551	the BC loop of D1	541:557	However, the receptor has local conformational variability in the C' strand of D2 and in the BC loop of D1.
11531339	7	55	theme	molecules	1082:1090	arg1	design					1072:1077	the design	1068:1077	the design of molecules to inhibit the interaction of Fc epsilon RI alpha with its natural ligand and thus to prevent a primary step in the allergic response	1068:1224	The results of this study point to new directions for the design of molecules to inhibit the interaction of Fc epsilon RI alpha with its natural ligand and thus to prevent a primary step in the allergic response.
11531339	5	56	theme	carbohydrates	751:763	arg1	distribution					735:746	a distribution	733:746	a distribution of carbohydrates lining the front and back surfaces of the structure	733:815	The different crystal forms reveal a distribution of carbohydrates lining the front and back surfaces of the structure.
11531339	1	57	theme	different	253:261	arg1	environments					272:283	15 different chemical environments	250:283	15 different chemical environments	250:283	We have solved the structure of the human high affinity IgE receptor, Fc epsilon RI alpha, in six different crystal forms, showing the structure in 15 different chemical environments.
11531339	7	58	theme	natural	1151:1157	arg1	ligand					1159:1164	its natural ligand	1147:1164	its natural ligand	1147:1164	The results of this study point to new directions for the design of molecules to inhibit the interaction of Fc epsilon RI alpha with its natural ligand and thus to prevent a primary step in the allergic response.
11531339	4	59	from	position	655:662	arg1	ligand					690:695	the IgE ligand	682:695	the IgE ligand	682:695	In every crystal form, a residue inserts between tryptophan residues 87 and 110, mimicking the position of a proline from the IgE ligand.
11531339	7	60	from	step	1196:1199	arg1	response					1217:1224	the allergic response	1204:1224	the allergic response	1204:1224	The results of this study point to new directions for the design of molecules to inhibit the interaction of Fc epsilon RI alpha with its natural ligand and thus to prevent a primary step in the allergic response.
11531339	1	61	theme	epsilon	175:181	arg1	RI					183:184	Fc epsilon RI	172:184	Fc epsilon RI alpha	172:190	We have solved the structure of the human high affinity IgE receptor, Fc epsilon RI alpha, in six different crystal forms, showing the structure in 15 different chemical environments.
11531339	7	62	theme	allergic	1208:1215	arg1	response					1217:1224	the allergic response	1204:1224	the allergic response	1204:1224	The results of this study point to new directions for the design of molecules to inhibit the interaction of Fc epsilon RI alpha with its natural ligand and thus to prevent a primary step in the allergic response.
11531339	3	63	theme	C'	518:519	arg1	strand					521:526	the C' strand	514:526	the C' strand of D2	514:532	However, the receptor has local conformational variability in the C' strand of D2 and in the BC loop of D1.
11531339	7	64	theme	Fc	1122:1123	arg1	RI					1133:1134	Fc epsilon RI	1122:1134	Fc epsilon RI alpha	1122:1140	The results of this study point to new directions for the design of molecules to inhibit the interaction of Fc epsilon RI alpha with its natural ligand and thus to prevent a primary step in the allergic response.
11531339	1	65	theme	RI	183:184	arg1	alpha					186:190	Fc epsilon RI alpha	172:190	Fc epsilon RI alpha	172:190	We have solved the structure of the human high affinity IgE receptor, Fc epsilon RI alpha, in six different crystal forms, showing the structure in 15 different chemical environments.
11531339	1	65	theme	RI	183:184	arg1	receptor					162:169	the human high affinity IgE receptor	134:169	the human high affinity IgE receptor	134:169	We have solved the structure of the human high affinity IgE receptor, Fc epsilon RI alpha, in six different crystal forms, showing the structure in 15 different chemical environments.
11531339	0	66	theme	Fc	53:54	arg1	Ri					64:65	the human high affinity IgE receptor Fc epsilon Ri	16:65	the human high affinity IgE receptor Fc epsilon Ri	16:65	The analysis of the human high affinity IgE receptor Fc epsilon Ri alpha from multiple crystal forms.
11531339	2	67	theme	overall	337:343	arg1	shape					345:349	the overall shape	333:349	the overall shape of the molecule	333:365	This database of structures shows no change in the overall shape of the molecule, as the angle between domains 1 and 2 (D1 and D2) varies little across the ensemble.
11531339	7	68	theme	alpha	1136:1140	arg1	interaction					1107:1117	the interaction	1103:1117	the interaction of Fc epsilon RI alpha with its natural ligand	1103:1164	The results of this study point to new directions for the design of molecules to inhibit the interaction of Fc epsilon RI alpha with its natural ligand and thus to prevent a primary step in the allergic response.
11531339	0	69	theme	receptor	44:51	arg1	Ri					64:65	the human high affinity IgE receptor Fc epsilon Ri	16:65	the human high affinity IgE receptor Fc epsilon Ri	16:65	The analysis of the human high affinity IgE receptor Fc epsilon Ri alpha from multiple crystal forms.
11531339	1	70	theme	chemical	263:270	arg1	environments					272:283	15 different chemical environments	250:283	15 different chemical environments	250:283	We have solved the structure of the human high affinity IgE receptor, Fc epsilon RI alpha, in six different crystal forms, showing the structure in 15 different chemical environments.
11531339	6	71	theme	contacts	841:848	arg1	analysis					821:828	An analysis	818:828	An analysis of crystal contacts in the different forms	818:871	An analysis of crystal contacts in the different forms indicates regions where the molecule interacts with other proteins, and reveals a potential new binding site distal to the IgE binding site.
11531339	2	72	theme	structures	303:312	arg1	database					291:298	This database	286:298	This database of structures	286:312	This database of structures shows no change in the overall shape of the molecule, as the angle between domains 1 and 2 (D1 and D2) varies little across the ensemble.
11531339	0	73	from	forms	95:99	arg1	alpha					67:71	alpha	67:71	alpha	67:71	The analysis of the human high affinity IgE receptor Fc epsilon Ri alpha from multiple crystal forms.
15667209	10	0	theme	water	1483:1487	arg1	molecule					1489:1496	one water molecule	1479:1496	one water molecule interacting with Glu197 and the catalytic triad histidine (His438)	1479:1563	The nonaged hBChE structure shows one water molecule interacting with Glu197 and the catalytic triad histidine (His438).
15667209	11	1	theme	water	1586:1590	arg1	molecule					1592:1599	this water molecule	1581:1599	this water molecule	1581:1599	Interestingly, this water molecule is ideally positioned to promote aging by two mechanisms: breaking either a C-O bond or a P-O bond.
15667209	8	2	from	shift	1173:1177	arg1	position					1186:1193	the position	1182:1193	the position of the catalytic triad histidine	1182:1226	No appreciable shift in the position of the catalytic triad histidine was observed between the aged and nonaged conjugates of hBChE.
15667209	1	3	theme	Organophosphorus	150:165	arg1	OP					176:177	OP	176:177	OP	176:177	Organophosphorus poisons (OP) bind covalently to the active-site serine of cholinesterases.
15667209	1	3	theme	Organophosphorus	150:165	arg1	poisons					167:173	Organophosphorus poisons	150:173	Organophosphorus poisons (OP)	150:178	Organophosphorus poisons (OP) bind covalently to the active-site serine of cholinesterases.
15667209	11	4	theme	C-O	1677:1679	arg1	bond					1681:1684	a C-O bond	1675:1684	a C-O bond	1675:1684	Interestingly, this water molecule is ideally positioned to promote aging by two mechanisms: breaking either a C-O bond or a P-O bond.
15667209	4	5	theme	active-site	557:567	arg1	Ser198					577:582	Ser198	577:582	Ser198	577:582	In human butyrylcholinesterase (hBChE), aging involves the residues His438 and Glu197 that are proximal to the active-site serine (Ser198).
15667209	4	5	theme	active-site	557:567	arg1	serine					569:574	the active-site serine	553:574	the active-site serine (Ser198)	553:583	In human butyrylcholinesterase (hBChE), aging involves the residues His438 and Glu197 that are proximal to the active-site serine (Ser198).
15667209	0	6	theme	crystal	86:92	arg1	structure					94:102	the crystal structure	82:102	the crystal structure	82:102	Role of water in aging of human butyrylcholinesterase inhibited by echothiophate: the crystal structure suggests two alternative mechanisms of aging.
15667209	0	7	from	Role	0:3	arg1	aging					17:21	aging	17:21	aging of human butyrylcholinesterase	17:52	Role of water in aging of human butyrylcholinesterase inhibited by echothiophate: the crystal structure suggests two alternative mechanisms of aging.
15667209	12	8	theme	certain	1716:1722	arg1	stereoisomers					1724:1736	certain stereoisomers	1716:1736	certain stereoisomers	1716:1736	Pesticides and certain stereoisomers of nerve agents are expected to undergo aging by breaking the P-O bond.
15667209	9	9	theme	crystal	1349:1355	arg1	structures					1357:1366	the aged and nonaged crystal structures	1328:1366	the aged and nonaged crystal structures of Torpedo californica acetylcholinesterase inhibited by the nerve agent VX	1328:1442	This absence of shift contrasts with the aged and nonaged crystal structures of Torpedo californica acetylcholinesterase inhibited by the nerve agent VX.
15667209	7	10	theme	A	1130:1130	arg1	resolution					1132:1141	2.1, 2.25, and 2.2 A resolution	1111:1141	2.1, 2.25, and 2.2 A resolution	1111:1141	In this work, the crystal structures of hBChE inhibited by the ophthalmic reagents echothiophate (nonaged and aged) and diisopropylfluorophosphate (aged) were solved and refined to 2.1, 2.25, and 2.2 A resolution, respectively.
15667209	6	11	theme	acetylcholinesterase	758:777	arg1	Aging					722:726	Aging	722:726	Aging of soman- and sarin-inhibited acetylcholinesterase	722:777	Aging of soman- and sarin-inhibited acetylcholinesterase occurs by C-O bond cleavage, whereas that of tabun- and isomalathion-inhibited acetylcholinesterase occurs by P-N and P-S bond cleavage, respectively.
15667209	8	12	theme	nonaged	1262:1268	arg1	conjugates					1270:1279	the aged and nonaged conjugates	1249:1279	the aged and nonaged conjugates of hBChE	1249:1288	No appreciable shift in the position of the catalytic triad histidine was observed between the aged and nonaged conjugates of hBChE.
15667209	11	13	theme	P-O	1691:1693	arg1	bond					1695:1698	a P-O bond	1689:1698	a P-O bond	1689:1698	Interestingly, this water molecule is ideally positioned to promote aging by two mechanisms: breaking either a C-O bond or a P-O bond.
15667209	7	14	dep	reagents	1004:1011	arg1	diisopropylfluorophosphate					1050:1075	diisopropylfluorophosphate	1050:1075	diisopropylfluorophosphate (aged)	1050:1082	In this work, the crystal structures of hBChE inhibited by the ophthalmic reagents echothiophate (nonaged and aged) and diisopropylfluorophosphate (aged) were solved and refined to 2.1, 2.25, and 2.2 A resolution, respectively.
15667209	7	14	dep	reagents	1004:1011	arg1	reagents					1004:1011	the ophthalmic reagents echothiophate (nonaged and aged) and diisopropylfluorophosphate (aged)	989:1082	the ophthalmic reagents echothiophate (nonaged and aged) and diisopropylfluorophosphate (aged)	989:1082	In this work, the crystal structures of hBChE inhibited by the ophthalmic reagents echothiophate (nonaged and aged) and diisopropylfluorophosphate (aged) were solved and refined to 2.1, 2.25, and 2.2 A resolution, respectively.
15667209	7	14	dep	reagents	1004:1011	arg1	echothiophate					1013:1025	echothiophate	1013:1025	echothiophate (nonaged and aged)	1013:1044	In this work, the crystal structures of hBChE inhibited by the ophthalmic reagents echothiophate (nonaged and aged) and diisopropylfluorophosphate (aged) were solved and refined to 2.1, 2.25, and 2.2 A resolution, respectively.
15667209	3	15	dep	reaction	388:395	arg1	termed					398:403	termed	398:403	termed aging	398:409	However, the covalently bound OP can undergo a suicide reaction (termed aging) yielding nonreactivatable enzyme.
15667209	6	16	theme	sarin-inhibited	742:756	arg1	acetylcholinesterase					758:777	soman- and sarin-inhibited acetylcholinesterase	731:777	soman- and sarin-inhibited acetylcholinesterase	731:777	Aging of soman- and sarin-inhibited acetylcholinesterase occurs by C-O bond cleavage, whereas that of tabun- and isomalathion-inhibited acetylcholinesterase occurs by P-N and P-S bond cleavage, respectively.
15667209	10	17	theme	nonaged	1449:1455	arg1	structure					1463:1471	The nonaged hBChE structure	1445:1471	The nonaged hBChE structure	1445:1471	The nonaged hBChE structure shows one water molecule interacting with Glu197 and the catalytic triad histidine (His438).
15667209	3	18	theme	nonreactivatable	421:436	arg1	enzyme					438:443	nonreactivatable enzyme	421:443	nonreactivatable enzyme	421:443	However, the covalently bound OP can undergo a suicide reaction (termed aging) yielding nonreactivatable enzyme.
15667209	5	19	dep	gases	642:646	arg1	soman					648:652	soman	648:652	soman	648:652	The mechanism of aging is known in detail for the nerve gases soman, sarin, and tabun as well as the pesticide metabolite isomalathion.
15667209	5	19	dep	gases	642:646	arg1	gases					642:646	the nerve gases soman, sarin, and tabun	632:670	the nerve gases soman, sarin, and tabun as well as the pesticide metabolite isomalathion	632:719	The mechanism of aging is known in detail for the nerve gases soman, sarin, and tabun as well as the pesticide metabolite isomalathion.
15667209	5	19	dep	gases	642:646	arg1	sarin					655:659	sarin	655:659	sarin	655:659	The mechanism of aging is known in detail for the nerve gases soman, sarin, and tabun as well as the pesticide metabolite isomalathion.
15667209	5	19	dep	gases	642:646	arg1	tabun					666:670	tabun	666:670	tabun	666:670	The mechanism of aging is known in detail for the nerve gases soman, sarin, and tabun as well as the pesticide metabolite isomalathion.
15667209	6	20	theme	isomalathion-inhibited	835:856	arg1	acetylcholinesterase					858:877	tabun- and isomalathion-inhibited acetylcholinesterase	824:877	tabun- and isomalathion-inhibited acetylcholinesterase	824:877	Aging of soman- and sarin-inhibited acetylcholinesterase occurs by C-O bond cleavage, whereas that of tabun- and isomalathion-inhibited acetylcholinesterase occurs by P-N and P-S bond cleavage, respectively.
15667209	5	21	theme	aging	603:607	arg1	mechanism					590:598	The mechanism	586:598	The mechanism of aging	586:607	The mechanism of aging is known in detail for the nerve gases soman, sarin, and tabun as well as the pesticide metabolite isomalathion.
15667209	8	22	theme	hBChE	1284:1288	arg1	conjugates					1270:1279	the aged and nonaged conjugates	1249:1279	the aged and nonaged conjugates of hBChE	1249:1288	No appreciable shift in the position of the catalytic triad histidine was observed between the aged and nonaged conjugates of hBChE.
15667209	7	23	dep	diisopropylfluorophosphate	1050:1075	arg1	aged					1078:1081	aged	1078:1081	aged	1078:1081	In this work, the crystal structures of hBChE inhibited by the ophthalmic reagents echothiophate (nonaged and aged) and diisopropylfluorophosphate (aged) were solved and refined to 2.1, 2.25, and 2.2 A resolution, respectively.
15667209	9	24	theme	Torpedo	1371:1377	arg1	acetylcholinesterase					1391:1410	Torpedo californica acetylcholinesterase	1371:1410	Torpedo californica acetylcholinesterase inhibited by the nerve agent VX	1371:1442	This absence of shift contrasts with the aged and nonaged crystal structures of Torpedo californica acetylcholinesterase inhibited by the nerve agent VX.
15667209	6	25	theme	soman-	731:736	arg1	acetylcholinesterase					758:777	soman- and sarin-inhibited acetylcholinesterase	731:777	soman- and sarin-inhibited acetylcholinesterase	731:777	Aging of soman- and sarin-inhibited acetylcholinesterase occurs by C-O bond cleavage, whereas that of tabun- and isomalathion-inhibited acetylcholinesterase occurs by P-N and P-S bond cleavage, respectively.
15667209	9	26	theme	californica	1379:1389	arg1	acetylcholinesterase					1391:1410	Torpedo californica acetylcholinesterase	1371:1410	Torpedo californica acetylcholinesterase inhibited by the nerve agent VX	1371:1442	This absence of shift contrasts with the aged and nonaged crystal structures of Torpedo californica acetylcholinesterase inhibited by the nerve agent VX.
15667209	3	27	theme	suicide	380:386	arg1	reaction					388:395	a suicide reaction	378:395	a suicide reaction (termed aging)	378:410	However, the covalently bound OP can undergo a suicide reaction (termed aging) yielding nonreactivatable enzyme.
15667209	9	28	theme	acetylcholinesterase	1391:1410	arg1	structures					1357:1366	the aged and nonaged crystal structures	1328:1366	the aged and nonaged crystal structures of Torpedo californica acetylcholinesterase inhibited by the nerve agent VX	1328:1442	This absence of shift contrasts with the aged and nonaged crystal structures of Torpedo californica acetylcholinesterase inhibited by the nerve agent VX.
15667209	10	29	theme	triad	1540:1544	arg1	histidine					1546:1554	the catalytic triad histidine	1526:1554	the catalytic triad histidine (His438)	1526:1563	The nonaged hBChE structure shows one water molecule interacting with Glu197 and the catalytic triad histidine (His438).
15667209	10	29	theme	triad	1540:1544	arg1	His438					1557:1562	His438	1557:1562	His438	1557:1562	The nonaged hBChE structure shows one water molecule interacting with Glu197 and the catalytic triad histidine (His438).
15667209	0	30	theme	alternative	117:127	arg1	mechanisms					129:138	two alternative mechanisms	113:138	two alternative mechanisms of aging	113:147	Role of water in aging of human butyrylcholinesterase inhibited by echothiophate: the crystal structure suggests two alternative mechanisms of aging.
15667209	0	31	theme	water	8:12	arg1	Role					0:3	Role	0:3	Role of water in aging of human butyrylcholinesterase	0:52	Role of water in aging of human butyrylcholinesterase inhibited by echothiophate: the crystal structure suggests two alternative mechanisms of aging.
15667209	9	32	theme	nonaged	1341:1347	arg1	structures					1357:1366	the aged and nonaged crystal structures	1328:1366	the aged and nonaged crystal structures of Torpedo californica acetylcholinesterase inhibited by the nerve agent VX	1328:1442	This absence of shift contrasts with the aged and nonaged crystal structures of Torpedo californica acetylcholinesterase inhibited by the nerve agent VX.
15667209	6	33	theme	tabun-	824:829	arg1	acetylcholinesterase					858:877	tabun- and isomalathion-inhibited acetylcholinesterase	824:877	tabun- and isomalathion-inhibited acetylcholinesterase	824:877	Aging of soman- and sarin-inhibited acetylcholinesterase occurs by C-O bond cleavage, whereas that of tabun- and isomalathion-inhibited acetylcholinesterase occurs by P-N and P-S bond cleavage, respectively.
15667209	2	34	theme	powerful	295:302	arg1	nucleophiles					304:315	powerful nucleophiles	295:315	powerful nucleophiles such as oximes	295:330	The inhibited enzyme can usually be reactivated with powerful nucleophiles such as oximes.
15667209	2	34	theme	powerful	295:302	arg1	oximes					325:330	oximes	325:330	oximes	325:330	The inhibited enzyme can usually be reactivated with powerful nucleophiles such as oximes.
15667209	12	35	theme	P-O	1800:1802	arg1	bond					1804:1807	the P-O bond	1796:1807	the P-O bond	1796:1807	Pesticides and certain stereoisomers of nerve agents are expected to undergo aging by breaking the P-O bond.
15667209	6	36	dep	occurs	779:784	arg1	whereas					808:814	whereas	808:814	whereas	808:814	Aging of soman- and sarin-inhibited acetylcholinesterase occurs by C-O bond cleavage, whereas that of tabun- and isomalathion-inhibited acetylcholinesterase occurs by P-N and P-S bond cleavage, respectively.
15667209	8	37	theme	triad	1212:1216	arg1	histidine					1218:1226	the catalytic triad histidine	1198:1226	the catalytic triad histidine	1198:1226	No appreciable shift in the position of the catalytic triad histidine was observed between the aged and nonaged conjugates of hBChE.
15667209	4	38	dep	residues	505:512	arg1	Glu197					525:530	Glu197	525:530	Glu197	525:530	In human butyrylcholinesterase (hBChE), aging involves the residues His438 and Glu197 that are proximal to the active-site serine (Ser198).
15667209	4	38	dep	residues	505:512	arg1	His438					514:519	His438	514:519	His438	514:519	In human butyrylcholinesterase (hBChE), aging involves the residues His438 and Glu197 that are proximal to the active-site serine (Ser198).
15667209	4	38	dep	residues	505:512	arg1	residues					505:512	the residues His438 and Glu197	501:530	the residues His438 and Glu197 that are proximal to the active-site serine (Ser198)	501:583	In human butyrylcholinesterase (hBChE), aging involves the residues His438 and Glu197 that are proximal to the active-site serine (Ser198).
15667209	9	39	theme	shift	1307:1311	arg1	absence					1296:1302	This absence	1291:1302	This absence of shift	1291:1311	This absence of shift contrasts with the aged and nonaged crystal structures of Torpedo californica acetylcholinesterase inhibited by the nerve agent VX.
15667209	9	40	theme	nerve	1429:1433	arg1	VX					1441:1442	the nerve agent VX	1425:1442	the nerve agent VX	1425:1442	This absence of shift contrasts with the aged and nonaged crystal structures of Torpedo californica acetylcholinesterase inhibited by the nerve agent VX.
15667209	12	41	theme	agents	1747:1752	arg1	Pesticides					1701:1710	Pesticides	1701:1710	Pesticides	1701:1710	Pesticides and certain stereoisomers of nerve agents are expected to undergo aging by breaking the P-O bond.
15667209	12	41	theme	agents	1747:1752	arg1	stereoisomers					1724:1736	certain stereoisomers	1716:1736	certain stereoisomers	1716:1736	Pesticides and certain stereoisomers of nerve agents are expected to undergo aging by breaking the P-O bond.
15667209	11	42	dep	mechanisms	1647:1656	arg1	breaking					1659:1666	breaking	1659:1666	breaking	1659:1666	Interestingly, this water molecule is ideally positioned to promote aging by two mechanisms: breaking either a C-O bond or a P-O bond.
15667209	1	43	theme	active-site	203:213	arg1	serine					215:220	the active-site serine	199:220	the active-site serine of cholinesterases	199:239	Organophosphorus poisons (OP) bind covalently to the active-site serine of cholinesterases.
15667209	0	44	theme	butyrylcholinesterase	32:52	arg1	aging					17:21	aging	17:21	aging of human butyrylcholinesterase	17:52	Role of water in aging of human butyrylcholinesterase inhibited by echothiophate: the crystal structure suggests two alternative mechanisms of aging.
15667209	3	45	theme	bound	357:361	arg1	OP					363:364	the covalently bound OP	342:364	the covalently bound OP	342:364	However, the covalently bound OP can undergo a suicide reaction (termed aging) yielding nonreactivatable enzyme.
15667209	5	46	theme	nerve	636:640	arg1	soman					648:652	soman	648:652	soman	648:652	The mechanism of aging is known in detail for the nerve gases soman, sarin, and tabun as well as the pesticide metabolite isomalathion.
15667209	5	46	theme	nerve	636:640	arg1	gases					642:646	the nerve gases soman, sarin, and tabun	632:670	the nerve gases soman, sarin, and tabun as well as the pesticide metabolite isomalathion	632:719	The mechanism of aging is known in detail for the nerve gases soman, sarin, and tabun as well as the pesticide metabolite isomalathion.
15667209	5	46	theme	nerve	636:640	arg1	sarin					655:659	sarin	655:659	sarin	655:659	The mechanism of aging is known in detail for the nerve gases soman, sarin, and tabun as well as the pesticide metabolite isomalathion.
15667209	5	46	theme	nerve	636:640	arg1	tabun					666:670	tabun	666:670	tabun	666:670	The mechanism of aging is known in detail for the nerve gases soman, sarin, and tabun as well as the pesticide metabolite isomalathion.
15667209	4	47	theme	human	449:453	arg1	hBChE					478:482	hBChE	478:482	hBChE	478:482	In human butyrylcholinesterase (hBChE), aging involves the residues His438 and Glu197 that are proximal to the active-site serine (Ser198).
15667209	4	47	theme	human	449:453	arg1	butyrylcholinesterase					455:475	human butyrylcholinesterase	449:475	human butyrylcholinesterase (hBChE)	449:483	In human butyrylcholinesterase (hBChE), aging involves the residues His438 and Glu197 that are proximal to the active-site serine (Ser198).
15667209	9	48	theme	agent	1435:1439	arg1	VX					1441:1442	the nerve agent VX	1425:1442	the nerve agent VX	1425:1442	This absence of shift contrasts with the aged and nonaged crystal structures of Torpedo californica acetylcholinesterase inhibited by the nerve agent VX.
15667209	0	49	theme	human	26:30	arg1	butyrylcholinesterase					32:52	human butyrylcholinesterase	26:52	human butyrylcholinesterase	26:52	Role of water in aging of human butyrylcholinesterase inhibited by echothiophate: the crystal structure suggests two alternative mechanisms of aging.
15667209	0	50	theme	aging	143:147	arg1	mechanisms					129:138	two alternative mechanisms	113:138	two alternative mechanisms of aging	113:147	Role of water in aging of human butyrylcholinesterase inhibited by echothiophate: the crystal structure suggests two alternative mechanisms of aging.
15667209	8	51	theme	histidine	1218:1226	arg1	position					1186:1193	the position	1182:1193	the position of the catalytic triad histidine	1182:1226	No appreciable shift in the position of the catalytic triad histidine was observed between the aged and nonaged conjugates of hBChE.
15667209	6	52	theme	bond	901:904	arg1	cleavage					906:913	P-S bond cleavage	897:913	P-S bond cleavage	897:913	Aging of soman- and sarin-inhibited acetylcholinesterase occurs by C-O bond cleavage, whereas that of tabun- and isomalathion-inhibited acetylcholinesterase occurs by P-N and P-S bond cleavage, respectively.
15667209	10	53	theme	hBChE	1457:1461	arg1	structure					1463:1471	The nonaged hBChE structure	1445:1471	The nonaged hBChE structure	1445:1471	The nonaged hBChE structure shows one water molecule interacting with Glu197 and the catalytic triad histidine (His438).
15667209	7	54	theme	hBChE	970:974	arg1	structures					956:965	the crystal structures	944:965	the crystal structures of hBChE inhibited by the ophthalmic reagents echothiophate (nonaged and aged) and diisopropylfluorophosphate (aged)	944:1082	In this work, the crystal structures of hBChE inhibited by the ophthalmic reagents echothiophate (nonaged and aged) and diisopropylfluorophosphate (aged) were solved and refined to 2.1, 2.25, and 2.2 A resolution, respectively.
15667209	8	55	theme	catalytic	1202:1210	arg1	histidine					1218:1226	the catalytic triad histidine	1198:1226	the catalytic triad histidine	1198:1226	No appreciable shift in the position of the catalytic triad histidine was observed between the aged and nonaged conjugates of hBChE.
15667209	7	56	theme	ophthalmic	993:1002	arg1	reagents					1004:1011	the ophthalmic reagents echothiophate (nonaged and aged) and diisopropylfluorophosphate (aged)	989:1082	the ophthalmic reagents echothiophate (nonaged and aged) and diisopropylfluorophosphate (aged)	989:1082	In this work, the crystal structures of hBChE inhibited by the ophthalmic reagents echothiophate (nonaged and aged) and diisopropylfluorophosphate (aged) were solved and refined to 2.1, 2.25, and 2.2 A resolution, respectively.
15667209	7	56	theme	ophthalmic	993:1002	arg1	diisopropylfluorophosphate					1050:1075	diisopropylfluorophosphate	1050:1075	diisopropylfluorophosphate (aged)	1050:1082	In this work, the crystal structures of hBChE inhibited by the ophthalmic reagents echothiophate (nonaged and aged) and diisopropylfluorophosphate (aged) were solved and refined to 2.1, 2.25, and 2.2 A resolution, respectively.
15667209	7	56	theme	ophthalmic	993:1002	arg1	echothiophate					1013:1025	echothiophate	1013:1025	echothiophate (nonaged and aged)	1013:1044	In this work, the crystal structures of hBChE inhibited by the ophthalmic reagents echothiophate (nonaged and aged) and diisopropylfluorophosphate (aged) were solved and refined to 2.1, 2.25, and 2.2 A resolution, respectively.
15667209	6	57	theme	bond	793:796	arg1	cleavage					798:805	C-O bond cleavage	789:805	C-O bond cleavage	789:805	Aging of soman- and sarin-inhibited acetylcholinesterase occurs by C-O bond cleavage, whereas that of tabun- and isomalathion-inhibited acetylcholinesterase occurs by P-N and P-S bond cleavage, respectively.
15667209	12	58	theme	nerve	1741:1745	arg1	agents					1747:1752	nerve agents	1741:1752	nerve agents	1741:1752	Pesticides and certain stereoisomers of nerve agents are expected to undergo aging by breaking the P-O bond.
15667209	7	59	theme	crystal	948:954	arg1	structures					956:965	the crystal structures	944:965	the crystal structures of hBChE inhibited by the ophthalmic reagents echothiophate (nonaged and aged) and diisopropylfluorophosphate (aged)	944:1082	In this work, the crystal structures of hBChE inhibited by the ophthalmic reagents echothiophate (nonaged and aged) and diisopropylfluorophosphate (aged) were solved and refined to 2.1, 2.25, and 2.2 A resolution, respectively.
15667209	8	60	theme	appreciable	1161:1171	arg1	shift					1173:1177	No appreciable shift	1158:1177	No appreciable shift in the position of the catalytic triad histidine	1158:1226	No appreciable shift in the position of the catalytic triad histidine was observed between the aged and nonaged conjugates of hBChE.
15667209	7	61	dep	echothiophate	1013:1025	arg1	nonaged					1028:1034	nonaged	1028:1034	nonaged	1028:1034	In this work, the crystal structures of hBChE inhibited by the ophthalmic reagents echothiophate (nonaged and aged) and diisopropylfluorophosphate (aged) were solved and refined to 2.1, 2.25, and 2.2 A resolution, respectively.
15667209	7	61	dep	echothiophate	1013:1025	arg1	aged					1040:1043	aged	1040:1043	aged	1040:1043	In this work, the crystal structures of hBChE inhibited by the ophthalmic reagents echothiophate (nonaged and aged) and diisopropylfluorophosphate (aged) were solved and refined to 2.1, 2.25, and 2.2 A resolution, respectively.
15667209	5	62	theme	pesticide	687:695	arg1	isomalathion					708:719	the pesticide metabolite isomalathion	683:719	the nerve gases soman, sarin, and tabun as well as the pesticide metabolite isomalathion	632:719	The mechanism of aging is known in detail for the nerve gases soman, sarin, and tabun as well as the pesticide metabolite isomalathion.
15667209	6	63	theme	C-O	789:791	arg1	cleavage					798:805	C-O bond cleavage	789:805	C-O bond cleavage	789:805	Aging of soman- and sarin-inhibited acetylcholinesterase occurs by C-O bond cleavage, whereas that of tabun- and isomalathion-inhibited acetylcholinesterase occurs by P-N and P-S bond cleavage, respectively.
15667209	2	64	theme	inhibited	246:254	arg1	enzyme					256:261	The inhibited enzyme	242:261	The inhibited enzyme	242:261	The inhibited enzyme can usually be reactivated with powerful nucleophiles such as oximes.
15667209	8	65	theme	aged	1253:1256	arg1	conjugates					1270:1279	the aged and nonaged conjugates	1249:1279	the aged and nonaged conjugates of hBChE	1249:1288	No appreciable shift in the position of the catalytic triad histidine was observed between the aged and nonaged conjugates of hBChE.
15667209	1	66	theme	cholinesterases	225:239	arg1	serine					215:220	the active-site serine	199:220	the active-site serine of cholinesterases	199:239	Organophosphorus poisons (OP) bind covalently to the active-site serine of cholinesterases.
15667209	5	67	theme	metabolite	697:706	arg1	isomalathion					708:719	the pesticide metabolite isomalathion	683:719	the nerve gases soman, sarin, and tabun as well as the pesticide metabolite isomalathion	632:719	The mechanism of aging is known in detail for the nerve gases soman, sarin, and tabun as well as the pesticide metabolite isomalathion.
15667209	6	68	theme	P-S	897:899	arg1	cleavage					906:913	P-S bond cleavage	897:913	P-S bond cleavage	897:913	Aging of soman- and sarin-inhibited acetylcholinesterase occurs by C-O bond cleavage, whereas that of tabun- and isomalathion-inhibited acetylcholinesterase occurs by P-N and P-S bond cleavage, respectively.
15667209	10	69	theme	catalytic	1530:1538	arg1	triad					1540:1544	the catalytic triad	1526:1544	the catalytic triad histidine (His438)	1526:1563	The nonaged hBChE structure shows one water molecule interacting with Glu197 and the catalytic triad histidine (His438).
15667209	9	70	theme	aged	1332:1335	arg1	structures					1357:1366	the aged and nonaged crystal structures	1328:1366	the aged and nonaged crystal structures of Torpedo californica acetylcholinesterase inhibited by the nerve agent VX	1328:1442	This absence of shift contrasts with the aged and nonaged crystal structures of Torpedo californica acetylcholinesterase inhibited by the nerve agent VX.
17355286	3	0	from	h	661:661	arg1	range					681:685	the micromolar range	666:685	the micromolar range	666:685	Our results show that when a free sensitive sulfhydryl group is present in the enzyme, as in Torpedo californica acetylcholinesterase, inhibition is irreversible and follows pseudo-first-order kinetics that are completed within 1 h in the micromolar range.
17355286	3	1	theme	sulfhydryl	475:484	arg1	group					486:490	a free sensitive sulfhydryl group	458:490	a free sensitive sulfhydryl group	458:490	Our results show that when a free sensitive sulfhydryl group is present in the enzyme, as in Torpedo californica acetylcholinesterase, inhibition is irreversible and follows pseudo-first-order kinetics that are completed within 1 h in the micromolar range.
17355286	3	1	theme	sulfhydryl	475:484	arg1	present					495:501	present	495:501	present	495:501	Our results show that when a free sensitive sulfhydryl group is present in the enzyme, as in Torpedo californica acetylcholinesterase, inhibition is irreversible and follows pseudo-first-order kinetics that are completed within 1 h in the micromolar range.
17355286	1	2	theme	biological	223:232	arg1	components					234:243	biological components	223:243	biological components of biosensors to survey polluted areas	223:282	The poorly known mechanism of inhibition of cholinesterases by inorganic mercury (HgCl2) has been studied with a view to using these enzymes as biomarkers or as biological components of biosensors to survey polluted areas.
17355286	8	3	theme	various	1332:1338	arg1	cholinesterases					1340:1354	the various cholinesterases	1328:1354	the various cholinesterases that we have studied	1328:1375	Our results indicate that among the various cholinesterases that we have studied, only Torpedo californica acetylcholinesterase is suitable for mercury detection using biosensors, and that a careful study of cholinesterase inhibition in a species is a prerequisite before using it as a biomarker to survey mercury in the environment.
17355286	8	4	from	biomarker	1582:1590	arg1	environment					1617:1627	the environment	1613:1627	the environment	1613:1627	Our results indicate that among the various cholinesterases that we have studied, only Torpedo californica acetylcholinesterase is suitable for mercury detection using biosensors, and that a careful study of cholinesterase inhibition in a species is a prerequisite before using it as a biomarker to survey mercury in the environment.
17355286	4	5	theme	melanogaster	759:770	arg1	acetylcholinesterase					772:791	Drosophila melanogaster acetylcholinesterase	748:791	Drosophila melanogaster acetylcholinesterase	748:791	When the free sulfhydryl group is not sensitive to mercury (Drosophila melanogaster acetylcholinesterase and human butyrylcholinesterase) or is otherwise absent (Electrophorus electricus acetylcholinesterase), then inhibition occurs in the millimolar range.
17355286	3	6	from	enzyme	510:515	arg1	group					486:490	a free sensitive sulfhydryl group	458:490	a free sensitive sulfhydryl group	458:490	Our results show that when a free sensitive sulfhydryl group is present in the enzyme, as in Torpedo californica acetylcholinesterase, inhibition is irreversible and follows pseudo-first-order kinetics that are completed within 1 h in the micromolar range.
17355286	3	6	from	enzyme	510:515	arg1	present					495:501	present	495:501	present	495:501	Our results show that when a free sensitive sulfhydryl group is present in the enzyme, as in Torpedo californica acetylcholinesterase, inhibition is irreversible and follows pseudo-first-order kinetics that are completed within 1 h in the micromolar range.
17355286	3	7	theme	pseudo-first-order	605:622	arg1	kinetics					624:631	pseudo-first-order kinetics	605:631	pseudo-first-order kinetics that are completed within 1 h in the micromolar range	605:685	Our results show that when a free sensitive sulfhydryl group is present in the enzyme, as in Torpedo californica acetylcholinesterase, inhibition is irreversible and follows pseudo-first-order kinetics that are completed within 1 h in the micromolar range.
17355286	5	8	theme	binding	972:978	arg1	model					980:984	a slow binding model	965:984	a slow binding model	965:984	Inhibition follows a slow binding model, with successive binding of two mercury ions to the enzyme surface.
17355286	4	9	dep	absent	842:847	arg1	acetylcholinesterase					875:894	Electrophorus electricus acetylcholinesterase	850:894	Electrophorus electricus acetylcholinesterase	850:894	When the free sulfhydryl group is not sensitive to mercury (Drosophila melanogaster acetylcholinesterase and human butyrylcholinesterase) or is otherwise absent (Electrophorus electricus acetylcholinesterase), then inhibition occurs in the millimolar range.
17355286	4	9	dep	absent	842:847	arg1	group					713:717	the free sulfhydryl group	693:717	the free sulfhydryl group	693:717	When the free sulfhydryl group is not sensitive to mercury (Drosophila melanogaster acetylcholinesterase and human butyrylcholinesterase) or is otherwise absent (Electrophorus electricus acetylcholinesterase), then inhibition occurs in the millimolar range.
17355286	4	9	dep	absent	842:847	arg1	sensitive					726:734	sensitive	726:734	sensitive	726:734	When the free sulfhydryl group is not sensitive to mercury (Drosophila melanogaster acetylcholinesterase and human butyrylcholinesterase) or is otherwise absent (Electrophorus electricus acetylcholinesterase), then inhibition occurs in the millimolar range.
17355286	4	9	dep	absent	842:847	arg1	absent					842:847	absent	842:847	absent	842:847	When the free sulfhydryl group is not sensitive to mercury (Drosophila melanogaster acetylcholinesterase and human butyrylcholinesterase) or is otherwise absent (Electrophorus electricus acetylcholinesterase), then inhibition occurs in the millimolar range.
17355286	7	10	theme	Mercury-induced	1214:1228	arg1	process					1287:1293	a rather complex process	1270:1293	a rather complex process	1270:1293	Mercury-induced inactivation of cholinesterases is thus a rather complex process.
17355286	7	10	theme	Mercury-induced	1214:1228	arg1	inactivation					1230:1241	Mercury-induced inactivation	1214:1241	Mercury-induced inactivation of cholinesterases	1214:1260	Mercury-induced inactivation of cholinesterases is thus a rather complex process.
17355286	4	11	dep	mercury	739:745	arg1	acetylcholinesterase					772:791	Drosophila melanogaster acetylcholinesterase	748:791	Drosophila melanogaster acetylcholinesterase	748:791	When the free sulfhydryl group is not sensitive to mercury (Drosophila melanogaster acetylcholinesterase and human butyrylcholinesterase) or is otherwise absent (Electrophorus electricus acetylcholinesterase), then inhibition occurs in the millimolar range.
17355286	4	11	dep	mercury	739:745	arg1	butyrylcholinesterase					803:823	human butyrylcholinesterase	797:823	human butyrylcholinesterase	797:823	When the free sulfhydryl group is not sensitive to mercury (Drosophila melanogaster acetylcholinesterase and human butyrylcholinesterase) or is otherwise absent (Electrophorus electricus acetylcholinesterase), then inhibition occurs in the millimolar range.
17355286	3	12	from	irreversible	580:591	arg1	acetylcholinesterase					544:563	Torpedo californica acetylcholinesterase	524:563	Torpedo californica acetylcholinesterase	524:563	Our results show that when a free sensitive sulfhydryl group is present in the enzyme, as in Torpedo californica acetylcholinesterase, inhibition is irreversible and follows pseudo-first-order kinetics that are completed within 1 h in the micromolar range.
17355286	1	13	theme	biosensors	248:257	arg1	components					234:243	biological components	223:243	biological components of biosensors to survey polluted areas	223:282	The poorly known mechanism of inhibition of cholinesterases by inorganic mercury (HgCl2) has been studied with a view to using these enzymes as biomarkers or as biological components of biosensors to survey polluted areas.
17355286	2	14	theme	cholinesterases	316:330	arg1	cholinesterases					316:330	cholinesterases	316:330	cholinesterases	316:330	The inhibition of a variety of cholinesterases by HgCl2 was investigated by kinetic studies, X-ray crystallography, and dynamic light scattering.
17355286	2	14	theme	cholinesterases	316:330	arg1	variety					305:311	a variety	303:311	a variety of cholinesterases	303:330	The inhibition of a variety of cholinesterases by HgCl2 was investigated by kinetic studies, X-ray crystallography, and dynamic light scattering.
17355286	3	15	from	present	495:501	arg1	enzyme					510:515	the enzyme	506:515	the enzyme	506:515	Our results show that when a free sensitive sulfhydryl group is present in the enzyme, as in Torpedo californica acetylcholinesterase, inhibition is irreversible and follows pseudo-first-order kinetics that are completed within 1 h in the micromolar range.
17355286	1	16	theme	known	73:77	arg1	mechanism					79:87	The poorly known mechanism	62:87	The poorly known mechanism of inhibition of cholinesterases by inorganic mercury (HgCl2)	62:149	The poorly known mechanism of inhibition of cholinesterases by inorganic mercury (HgCl2) has been studied with a view to using these enzymes as biomarkers or as biological components of biosensors to survey polluted areas.
17355286	6	17	theme	mercury	1065:1071	arg1	ions					1073:1076	mercury ions	1065:1076	mercury ions	1065:1076	Binding of mercury ions has several consequences: reversible inhibition, enzyme denaturation, and protein aggregation, protecting the enzyme from denaturation.
17355286	6	18	theme	several	1082:1088	arg1	aggregation					1160:1170	protein aggregation	1152:1170	protein aggregation	1152:1170	Binding of mercury ions has several consequences: reversible inhibition, enzyme denaturation, and protein aggregation, protecting the enzyme from denaturation.
17355286	6	18	theme	several	1082:1088	arg1	consequences					1090:1101	several consequences	1082:1101	several consequences: reversible inhibition, enzyme denaturation, and protein aggregation	1082:1170	Binding of mercury ions has several consequences: reversible inhibition, enzyme denaturation, and protein aggregation, protecting the enzyme from denaturation.
17355286	6	18	theme	several	1082:1088	arg1	inhibition					1115:1124	reversible inhibition	1104:1124	reversible inhibition	1104:1124	Binding of mercury ions has several consequences: reversible inhibition, enzyme denaturation, and protein aggregation, protecting the enzyme from denaturation.
17355286	6	18	theme	several	1082:1088	arg1	denaturation					1134:1145	enzyme denaturation	1127:1145	enzyme denaturation	1127:1145	Binding of mercury ions has several consequences: reversible inhibition, enzyme denaturation, and protein aggregation, protecting the enzyme from denaturation.
17355286	6	19	theme	ions	1073:1076	arg1	Binding					1054:1060	Binding	1054:1060	Binding of mercury ions	1054:1076	Binding of mercury ions has several consequences: reversible inhibition, enzyme denaturation, and protein aggregation, protecting the enzyme from denaturation.
17355286	4	20	dep	Electrophorus	850:862	arg1	electricus					864:873	electricus	864:873	electricus	864:873	When the free sulfhydryl group is not sensitive to mercury (Drosophila melanogaster acetylcholinesterase and human butyrylcholinesterase) or is otherwise absent (Electrophorus electricus acetylcholinesterase), then inhibition occurs in the millimolar range.
17355286	4	21	theme	Electrophorus	850:862	arg1	acetylcholinesterase					875:894	Electrophorus electricus acetylcholinesterase	850:894	Electrophorus electricus acetylcholinesterase	850:894	When the free sulfhydryl group is not sensitive to mercury (Drosophila melanogaster acetylcholinesterase and human butyrylcholinesterase) or is otherwise absent (Electrophorus electricus acetylcholinesterase), then inhibition occurs in the millimolar range.
17355286	4	21	theme	Electrophorus	850:862	arg1	group					713:717	the free sulfhydryl group	693:717	the free sulfhydryl group	693:717	When the free sulfhydryl group is not sensitive to mercury (Drosophila melanogaster acetylcholinesterase and human butyrylcholinesterase) or is otherwise absent (Electrophorus electricus acetylcholinesterase), then inhibition occurs in the millimolar range.
17355286	4	21	theme	Electrophorus	850:862	arg1	sensitive					726:734	sensitive	726:734	sensitive	726:734	When the free sulfhydryl group is not sensitive to mercury (Drosophila melanogaster acetylcholinesterase and human butyrylcholinesterase) or is otherwise absent (Electrophorus electricus acetylcholinesterase), then inhibition occurs in the millimolar range.
17355286	4	21	theme	Electrophorus	850:862	arg1	absent					842:847	absent	842:847	absent	842:847	When the free sulfhydryl group is not sensitive to mercury (Drosophila melanogaster acetylcholinesterase and human butyrylcholinesterase) or is otherwise absent (Electrophorus electricus acetylcholinesterase), then inhibition occurs in the millimolar range.
17355286	8	22	from	study	1495:1499	arg1	species					1535:1541	a species	1533:1541	a species	1533:1541	Our results indicate that among the various cholinesterases that we have studied, only Torpedo californica acetylcholinesterase is suitable for mercury detection using biosensors, and that a careful study of cholinesterase inhibition in a species is a prerequisite before using it as a biomarker to survey mercury in the environment.
17355286	3	23	theme	Torpedo	524:530	arg1	acetylcholinesterase					544:563	Torpedo californica acetylcholinesterase	524:563	Torpedo californica acetylcholinesterase	524:563	Our results show that when a free sensitive sulfhydryl group is present in the enzyme, as in Torpedo californica acetylcholinesterase, inhibition is irreversible and follows pseudo-first-order kinetics that are completed within 1 h in the micromolar range.
17355286	2	24	theme	kinetic	361:367	arg1	studies					369:375	kinetic studies	361:375	kinetic studies	361:375	The inhibition of a variety of cholinesterases by HgCl2 was investigated by kinetic studies, X-ray crystallography, and dynamic light scattering.
17355286	1	25	theme	inhibition	92:101	arg1	mechanism					79:87	The poorly known mechanism	62:87	The poorly known mechanism of inhibition of cholinesterases by inorganic mercury (HgCl2)	62:149	The poorly known mechanism of inhibition of cholinesterases by inorganic mercury (HgCl2) has been studied with a view to using these enzymes as biomarkers or as biological components of biosensors to survey polluted areas.
17355286	3	26	from	acetylcholinesterase	544:563	arg1	irreversible					580:591	irreversible	580:591	irreversible	580:591	Our results show that when a free sensitive sulfhydryl group is present in the enzyme, as in Torpedo californica acetylcholinesterase, inhibition is irreversible and follows pseudo-first-order kinetics that are completed within 1 h in the micromolar range.
17355286	2	27	theme	light	413:417	arg1	scattering					419:428	dynamic light scattering	405:428	dynamic light scattering	405:428	The inhibition of a variety of cholinesterases by HgCl2 was investigated by kinetic studies, X-ray crystallography, and dynamic light scattering.
17355286	1	28	theme	survey	262:267	arg1	areas					278:282	survey polluted areas	262:282	survey polluted areas	262:282	The poorly known mechanism of inhibition of cholinesterases by inorganic mercury (HgCl2) has been studied with a view to using these enzymes as biomarkers or as biological components of biosensors to survey polluted areas.
17355286	4	29	theme	millimolar	928:937	arg1	range					939:943	the millimolar range	924:943	the millimolar range	924:943	When the free sulfhydryl group is not sensitive to mercury (Drosophila melanogaster acetylcholinesterase and human butyrylcholinesterase) or is otherwise absent (Electrophorus electricus acetylcholinesterase), then inhibition occurs in the millimolar range.
17355286	6	30	dep	consequences	1090:1101	arg1	aggregation					1160:1170	protein aggregation	1152:1170	protein aggregation	1152:1170	Binding of mercury ions has several consequences: reversible inhibition, enzyme denaturation, and protein aggregation, protecting the enzyme from denaturation.
17355286	6	30	dep	consequences	1090:1101	arg1	consequences					1090:1101	several consequences	1082:1101	several consequences: reversible inhibition, enzyme denaturation, and protein aggregation	1082:1170	Binding of mercury ions has several consequences: reversible inhibition, enzyme denaturation, and protein aggregation, protecting the enzyme from denaturation.
17355286	6	30	dep	consequences	1090:1101	arg1	inhibition					1115:1124	reversible inhibition	1104:1124	reversible inhibition	1104:1124	Binding of mercury ions has several consequences: reversible inhibition, enzyme denaturation, and protein aggregation, protecting the enzyme from denaturation.
17355286	6	30	dep	consequences	1090:1101	arg1	denaturation					1134:1145	enzyme denaturation	1127:1145	enzyme denaturation	1127:1145	Binding of mercury ions has several consequences: reversible inhibition, enzyme denaturation, and protein aggregation, protecting the enzyme from denaturation.
17355286	2	31	theme	dynamic	405:411	arg1	scattering					419:428	dynamic light scattering	405:428	dynamic light scattering	405:428	The inhibition of a variety of cholinesterases by HgCl2 was investigated by kinetic studies, X-ray crystallography, and dynamic light scattering.
17355286	1	32	theme	polluted	269:276	arg1	areas					278:282	survey polluted areas	262:282	survey polluted areas	262:282	The poorly known mechanism of inhibition of cholinesterases by inorganic mercury (HgCl2) has been studied with a view to using these enzymes as biomarkers or as biological components of biosensors to survey polluted areas.
17355286	4	33	theme	Drosophila	748:757	arg1	acetylcholinesterase					772:791	Drosophila melanogaster acetylcholinesterase	748:791	Drosophila melanogaster acetylcholinesterase	748:791	When the free sulfhydryl group is not sensitive to mercury (Drosophila melanogaster acetylcholinesterase and human butyrylcholinesterase) or is otherwise absent (Electrophorus electricus acetylcholinesterase), then inhibition occurs in the millimolar range.
17355286	1	34	theme	cholinesterases	106:120	arg1	inhibition					92:101	inhibition	92:101	inhibition of cholinesterases by inorganic mercury (HgCl2)	92:149	The poorly known mechanism of inhibition of cholinesterases by inorganic mercury (HgCl2) has been studied with a view to using these enzymes as biomarkers or as biological components of biosensors to survey polluted areas.
17355286	6	35	theme	protein	1152:1158	arg1	aggregation					1160:1170	protein aggregation	1152:1170	protein aggregation	1152:1170	Binding of mercury ions has several consequences: reversible inhibition, enzyme denaturation, and protein aggregation, protecting the enzyme from denaturation.
17355286	6	35	theme	protein	1152:1158	arg1	consequences					1090:1101	several consequences	1082:1101	several consequences: reversible inhibition, enzyme denaturation, and protein aggregation	1082:1170	Binding of mercury ions has several consequences: reversible inhibition, enzyme denaturation, and protein aggregation, protecting the enzyme from denaturation.
17355286	0	36	theme	inorganic	43:51	arg1	mercury					53:59	inorganic mercury	43:59	inorganic mercury	43:59	Mechanisms of cholinesterase inhibition by inorganic mercury.
17355286	3	37	theme	sensitive	465:473	arg1	group					486:490	a free sensitive sulfhydryl group	458:490	a free sensitive sulfhydryl group	458:490	Our results show that when a free sensitive sulfhydryl group is present in the enzyme, as in Torpedo californica acetylcholinesterase, inhibition is irreversible and follows pseudo-first-order kinetics that are completed within 1 h in the micromolar range.
17355286	3	37	theme	sensitive	465:473	arg1	present					495:501	present	495:501	present	495:501	Our results show that when a free sensitive sulfhydryl group is present in the enzyme, as in Torpedo californica acetylcholinesterase, inhibition is irreversible and follows pseudo-first-order kinetics that are completed within 1 h in the micromolar range.
17355286	6	38	theme	enzyme	1127:1132	arg1	consequences					1090:1101	several consequences	1082:1101	several consequences: reversible inhibition, enzyme denaturation, and protein aggregation	1082:1170	Binding of mercury ions has several consequences: reversible inhibition, enzyme denaturation, and protein aggregation, protecting the enzyme from denaturation.
17355286	6	38	theme	enzyme	1127:1132	arg1	denaturation					1134:1145	enzyme denaturation	1127:1145	enzyme denaturation	1127:1145	Binding of mercury ions has several consequences: reversible inhibition, enzyme denaturation, and protein aggregation, protecting the enzyme from denaturation.
17355286	5	39	theme	mercury	1018:1024	arg1	ions					1026:1029	two mercury ions	1014:1029	two mercury ions	1014:1029	Inhibition follows a slow binding model, with successive binding of two mercury ions to the enzyme surface.
17355286	6	40	contain	has	1078:1080	arg2	denaturation					1134:1145	enzyme denaturation	1127:1145	enzyme denaturation	1127:1145	Binding of mercury ions has several consequences: reversible inhibition, enzyme denaturation, and protein aggregation, protecting the enzyme from denaturation.
17355286	6	40	contain	has	1078:1080	arg1	Binding					1054:1060	Binding	1054:1060	Binding of mercury ions	1054:1076	Binding of mercury ions has several consequences: reversible inhibition, enzyme denaturation, and protein aggregation, protecting the enzyme from denaturation.
17355286	6	40	contain	has	1078:1080	arg2	aggregation					1160:1170	protein aggregation	1152:1170	protein aggregation	1152:1170	Binding of mercury ions has several consequences: reversible inhibition, enzyme denaturation, and protein aggregation, protecting the enzyme from denaturation.
17355286	6	40	contain	has	1078:1080	arg2	inhibition					1115:1124	reversible inhibition	1104:1124	reversible inhibition	1104:1124	Binding of mercury ions has several consequences: reversible inhibition, enzyme denaturation, and protein aggregation, protecting the enzyme from denaturation.
17355286	6	40	contain	has	1078:1080	arg2	consequences					1090:1101	several consequences	1082:1101	several consequences: reversible inhibition, enzyme denaturation, and protein aggregation	1082:1170	Binding of mercury ions has several consequences: reversible inhibition, enzyme denaturation, and protein aggregation, protecting the enzyme from denaturation.
17355286	0	41	theme	inhibition	29:38	arg1	Mechanisms					0:9	Mechanisms	0:9	Mechanisms of cholinesterase inhibition by inorganic mercury.	0:60	Mechanisms of cholinesterase inhibition by inorganic mercury.
17355286	3	42	located	present	495:501	arg1	enzyme					510:515	the enzyme	506:515	the enzyme	506:515	Our results show that when a free sensitive sulfhydryl group is present in the enzyme, as in Torpedo californica acetylcholinesterase, inhibition is irreversible and follows pseudo-first-order kinetics that are completed within 1 h in the micromolar range.
17355286	3	42	located	present	495:501	arg2	present					495:501	present	495:501	present	495:501	Our results show that when a free sensitive sulfhydryl group is present in the enzyme, as in Torpedo californica acetylcholinesterase, inhibition is irreversible and follows pseudo-first-order kinetics that are completed within 1 h in the micromolar range.
17355286	3	42	located	present	495:501	arg2	group					486:490	a free sensitive sulfhydryl group	458:490	a free sensitive sulfhydryl group	458:490	Our results show that when a free sensitive sulfhydryl group is present in the enzyme, as in Torpedo californica acetylcholinesterase, inhibition is irreversible and follows pseudo-first-order kinetics that are completed within 1 h in the micromolar range.
17355286	2	43	theme	X-ray	378:382	arg1	crystallography					384:398	X-ray crystallography	378:398	X-ray crystallography	378:398	The inhibition of a variety of cholinesterases by HgCl2 was investigated by kinetic studies, X-ray crystallography, and dynamic light scattering.
17355286	8	44	theme	cholinesterase	1504:1517	arg1	inhibition					1519:1528	cholinesterase inhibition	1504:1528	cholinesterase inhibition	1504:1528	Our results indicate that among the various cholinesterases that we have studied, only Torpedo californica acetylcholinesterase is suitable for mercury detection using biosensors, and that a careful study of cholinesterase inhibition in a species is a prerequisite before using it as a biomarker to survey mercury in the environment.
17355286	8	45	theme	survey	1595:1600	arg1	mercury					1602:1608	survey mercury	1595:1608	survey mercury	1595:1608	Our results indicate that among the various cholinesterases that we have studied, only Torpedo californica acetylcholinesterase is suitable for mercury detection using biosensors, and that a careful study of cholinesterase inhibition in a species is a prerequisite before using it as a biomarker to survey mercury in the environment.
17355286	8	46	theme	californica	1391:1401	arg1	acetylcholinesterase					1403:1422	only Torpedo californica acetylcholinesterase	1378:1422	only Torpedo californica acetylcholinesterase	1378:1422	Our results indicate that among the various cholinesterases that we have studied, only Torpedo californica acetylcholinesterase is suitable for mercury detection using biosensors, and that a careful study of cholinesterase inhibition in a species is a prerequisite before using it as a biomarker to survey mercury in the environment.
17355286	8	47	theme	careful	1487:1493	arg1	study					1495:1499	a careful study	1485:1499	a careful study of cholinesterase inhibition in a species	1485:1541	Our results indicate that among the various cholinesterases that we have studied, only Torpedo californica acetylcholinesterase is suitable for mercury detection using biosensors, and that a careful study of cholinesterase inhibition in a species is a prerequisite before using it as a biomarker to survey mercury in the environment.
17355286	8	47	theme	careful	1487:1493	arg1	prerequisite					1548:1559	a prerequisite	1546:1559	a prerequisite before using it as a biomarker to survey mercury in the environment	1546:1627	Our results indicate that among the various cholinesterases that we have studied, only Torpedo californica acetylcholinesterase is suitable for mercury detection using biosensors, and that a careful study of cholinesterase inhibition in a species is a prerequisite before using it as a biomarker to survey mercury in the environment.
17355286	6	48	theme	reversible	1104:1113	arg1	consequences					1090:1101	several consequences	1082:1101	several consequences: reversible inhibition, enzyme denaturation, and protein aggregation	1082:1170	Binding of mercury ions has several consequences: reversible inhibition, enzyme denaturation, and protein aggregation, protecting the enzyme from denaturation.
17355286	6	48	theme	reversible	1104:1113	arg1	inhibition					1115:1124	reversible inhibition	1104:1124	reversible inhibition	1104:1124	Binding of mercury ions has several consequences: reversible inhibition, enzyme denaturation, and protein aggregation, protecting the enzyme from denaturation.
17355286	3	49	theme	free	460:463	arg1	group					486:490	a free sensitive sulfhydryl group	458:490	a free sensitive sulfhydryl group	458:490	Our results show that when a free sensitive sulfhydryl group is present in the enzyme, as in Torpedo californica acetylcholinesterase, inhibition is irreversible and follows pseudo-first-order kinetics that are completed within 1 h in the micromolar range.
17355286	3	49	theme	free	460:463	arg1	present					495:501	present	495:501	present	495:501	Our results show that when a free sensitive sulfhydryl group is present in the enzyme, as in Torpedo californica acetylcholinesterase, inhibition is irreversible and follows pseudo-first-order kinetics that are completed within 1 h in the micromolar range.
17355286	3	50	theme	micromolar	670:679	arg1	range					681:685	the micromolar range	666:685	the micromolar range	666:685	Our results show that when a free sensitive sulfhydryl group is present in the enzyme, as in Torpedo californica acetylcholinesterase, inhibition is irreversible and follows pseudo-first-order kinetics that are completed within 1 h in the micromolar range.
17355286	5	51	theme	enzyme	1038:1043	arg1	surface					1045:1051	the enzyme surface	1034:1051	the enzyme surface	1034:1051	Inhibition follows a slow binding model, with successive binding of two mercury ions to the enzyme surface.
17355286	8	52	theme	mercury	1440:1446	arg1	detection					1448:1456	mercury detection	1440:1456	mercury detection using biosensors	1440:1473	Our results indicate that among the various cholinesterases that we have studied, only Torpedo californica acetylcholinesterase is suitable for mercury detection using biosensors, and that a careful study of cholinesterase inhibition in a species is a prerequisite before using it as a biomarker to survey mercury in the environment.
17355286	1	53	theme	inorganic	125:133	arg1	mercury					135:141	inorganic mercury	125:141	inorganic mercury (HgCl2)	125:149	The poorly known mechanism of inhibition of cholinesterases by inorganic mercury (HgCl2) has been studied with a view to using these enzymes as biomarkers or as biological components of biosensors to survey polluted areas.
17355286	1	53	theme	inorganic	125:133	arg1	HgCl2					144:148	HgCl2	144:148	HgCl2	144:148	The poorly known mechanism of inhibition of cholinesterases by inorganic mercury (HgCl2) has been studied with a view to using these enzymes as biomarkers or as biological components of biosensors to survey polluted areas.
17355286	7	54	theme	complex	1279:1285	arg1	inactivation					1230:1241	Mercury-induced inactivation	1214:1241	Mercury-induced inactivation of cholinesterases	1214:1260	Mercury-induced inactivation of cholinesterases is thus a rather complex process.
17355286	7	54	theme	complex	1279:1285	arg1	process					1287:1293	a rather complex process	1270:1293	a rather complex process	1270:1293	Mercury-induced inactivation of cholinesterases is thus a rather complex process.
17355286	5	55	theme	successive	992:1001	arg1	binding					1003:1009	successive binding	992:1009	successive binding of two mercury ions to the enzyme surface	992:1051	Inhibition follows a slow binding model, with successive binding of two mercury ions to the enzyme surface.
17355286	5	56	theme	ions	1026:1029	arg1	binding					1003:1009	successive binding	992:1009	successive binding of two mercury ions to the enzyme surface	992:1051	Inhibition follows a slow binding model, with successive binding of two mercury ions to the enzyme surface.
17355286	2	57	theme	variety	305:311	arg1	inhibition					289:298	The inhibition	285:298	The inhibition of a variety of cholinesterases by HgCl2	285:339	The inhibition of a variety of cholinesterases by HgCl2 was investigated by kinetic studies, X-ray crystallography, and dynamic light scattering.
17355286	3	58	attach	present	495:501	arg1	enzyme					510:515	the enzyme	506:515	the enzyme	506:515	Our results show that when a free sensitive sulfhydryl group is present in the enzyme, as in Torpedo californica acetylcholinesterase, inhibition is irreversible and follows pseudo-first-order kinetics that are completed within 1 h in the micromolar range.
17355286	3	58	attach	present	495:501	arg2	present					495:501	present	495:501	present	495:501	Our results show that when a free sensitive sulfhydryl group is present in the enzyme, as in Torpedo californica acetylcholinesterase, inhibition is irreversible and follows pseudo-first-order kinetics that are completed within 1 h in the micromolar range.
17355286	3	58	attach	present	495:501	arg2	group					486:490	a free sensitive sulfhydryl group	458:490	a free sensitive sulfhydryl group	458:490	Our results show that when a free sensitive sulfhydryl group is present in the enzyme, as in Torpedo californica acetylcholinesterase, inhibition is irreversible and follows pseudo-first-order kinetics that are completed within 1 h in the micromolar range.
17355286	4	59	theme	free	697:700	arg1	acetylcholinesterase					875:894	Electrophorus electricus acetylcholinesterase	850:894	Electrophorus electricus acetylcholinesterase	850:894	When the free sulfhydryl group is not sensitive to mercury (Drosophila melanogaster acetylcholinesterase and human butyrylcholinesterase) or is otherwise absent (Electrophorus electricus acetylcholinesterase), then inhibition occurs in the millimolar range.
17355286	4	59	theme	free	697:700	arg1	group					713:717	the free sulfhydryl group	693:717	the free sulfhydryl group	693:717	When the free sulfhydryl group is not sensitive to mercury (Drosophila melanogaster acetylcholinesterase and human butyrylcholinesterase) or is otherwise absent (Electrophorus electricus acetylcholinesterase), then inhibition occurs in the millimolar range.
17355286	4	59	theme	free	697:700	arg1	sensitive					726:734	sensitive	726:734	sensitive	726:734	When the free sulfhydryl group is not sensitive to mercury (Drosophila melanogaster acetylcholinesterase and human butyrylcholinesterase) or is otherwise absent (Electrophorus electricus acetylcholinesterase), then inhibition occurs in the millimolar range.
17355286	4	59	theme	free	697:700	arg1	absent					842:847	absent	842:847	absent	842:847	When the free sulfhydryl group is not sensitive to mercury (Drosophila melanogaster acetylcholinesterase and human butyrylcholinesterase) or is otherwise absent (Electrophorus electricus acetylcholinesterase), then inhibition occurs in the millimolar range.
17355286	8	60	theme	Torpedo	1383:1389	arg1	acetylcholinesterase					1403:1422	only Torpedo californica acetylcholinesterase	1378:1422	only Torpedo californica acetylcholinesterase	1378:1422	Our results indicate that among the various cholinesterases that we have studied, only Torpedo californica acetylcholinesterase is suitable for mercury detection using biosensors, and that a careful study of cholinesterase inhibition in a species is a prerequisite before using it as a biomarker to survey mercury in the environment.
17355286	4	61	theme	sulfhydryl	702:711	arg1	acetylcholinesterase					875:894	Electrophorus electricus acetylcholinesterase	850:894	Electrophorus electricus acetylcholinesterase	850:894	When the free sulfhydryl group is not sensitive to mercury (Drosophila melanogaster acetylcholinesterase and human butyrylcholinesterase) or is otherwise absent (Electrophorus electricus acetylcholinesterase), then inhibition occurs in the millimolar range.
17355286	4	61	theme	sulfhydryl	702:711	arg1	group					713:717	the free sulfhydryl group	693:717	the free sulfhydryl group	693:717	When the free sulfhydryl group is not sensitive to mercury (Drosophila melanogaster acetylcholinesterase and human butyrylcholinesterase) or is otherwise absent (Electrophorus electricus acetylcholinesterase), then inhibition occurs in the millimolar range.
17355286	4	61	theme	sulfhydryl	702:711	arg1	sensitive					726:734	sensitive	726:734	sensitive	726:734	When the free sulfhydryl group is not sensitive to mercury (Drosophila melanogaster acetylcholinesterase and human butyrylcholinesterase) or is otherwise absent (Electrophorus electricus acetylcholinesterase), then inhibition occurs in the millimolar range.
17355286	4	61	theme	sulfhydryl	702:711	arg1	absent					842:847	absent	842:847	absent	842:847	When the free sulfhydryl group is not sensitive to mercury (Drosophila melanogaster acetylcholinesterase and human butyrylcholinesterase) or is otherwise absent (Electrophorus electricus acetylcholinesterase), then inhibition occurs in the millimolar range.
17355286	7	62	theme	cholinesterases	1246:1260	arg1	process					1287:1293	a rather complex process	1270:1293	a rather complex process	1270:1293	Mercury-induced inactivation of cholinesterases is thus a rather complex process.
17355286	7	62	theme	cholinesterases	1246:1260	arg1	inactivation					1230:1241	Mercury-induced inactivation	1214:1241	Mercury-induced inactivation of cholinesterases	1214:1260	Mercury-induced inactivation of cholinesterases is thus a rather complex process.
17355286	8	63	theme	inhibition	1519:1528	arg1	study					1495:1499	a careful study	1485:1499	a careful study of cholinesterase inhibition in a species	1485:1541	Our results indicate that among the various cholinesterases that we have studied, only Torpedo californica acetylcholinesterase is suitable for mercury detection using biosensors, and that a careful study of cholinesterase inhibition in a species is a prerequisite before using it as a biomarker to survey mercury in the environment.
17355286	8	63	theme	inhibition	1519:1528	arg1	prerequisite					1548:1559	a prerequisite	1546:1559	a prerequisite before using it as a biomarker to survey mercury in the environment	1546:1627	Our results indicate that among the various cholinesterases that we have studied, only Torpedo californica acetylcholinesterase is suitable for mercury detection using biosensors, and that a careful study of cholinesterase inhibition in a species is a prerequisite before using it as a biomarker to survey mercury in the environment.
17355286	4	64	theme	human	797:801	arg1	butyrylcholinesterase					803:823	human butyrylcholinesterase	797:823	human butyrylcholinesterase	797:823	When the free sulfhydryl group is not sensitive to mercury (Drosophila melanogaster acetylcholinesterase and human butyrylcholinesterase) or is otherwise absent (Electrophorus electricus acetylcholinesterase), then inhibition occurs in the millimolar range.
17355286	5	65	theme	slow	967:970	arg1	model					980:984	a slow binding model	965:984	a slow binding model	965:984	Inhibition follows a slow binding model, with successive binding of two mercury ions to the enzyme surface.
17355286	0	66	theme	cholinesterase	14:27	arg1	inhibition					29:38	cholinesterase inhibition	14:38	cholinesterase inhibition	14:38	Mechanisms of cholinesterase inhibition by inorganic mercury.
17355286	3	67	theme	californica	532:542	arg1	acetylcholinesterase					544:563	Torpedo californica acetylcholinesterase	524:563	Torpedo californica acetylcholinesterase	524:563	Our results show that when a free sensitive sulfhydryl group is present in the enzyme, as in Torpedo californica acetylcholinesterase, inhibition is irreversible and follows pseudo-first-order kinetics that are completed within 1 h in the micromolar range.
18975951	7	0	theme	aged	1119:1122	arg1	tabun-hBChE					1124:1134	non-aged and aged tabun-hBChE	1106:1134	non-aged and aged tabun-hBChE	1106:1134	Structures for non-aged and aged tabun-hBChE were refined to 2.3 and 2.1 A, respectively.
18975951	9	1	theme	charged	1364:1370	arg1	oxygen					1372:1377	the negatively charged oxygen	1349:1377	the negatively charged oxygen	1349:1377	After dealkylation, the negatively charged oxygen forms a strong salt bridge with protonated His438N epsilon2 that prevents reactivation.
18975951	1	2	theme	toxic	156:160	arg1	heroin					180:185	heroin	180:185	heroin	180:185	Human butyrylcholinesterase (hBChE) hydrolyzes or scavenges a wide range of toxic esters, including heroin, cocaine, carbamate pesticides, organophosphorus pesticides, and nerve agents.
18975951	1	2	theme	toxic	156:160	arg1	pesticides					236:245	organophosphorus pesticides	219:245	organophosphorus pesticides	219:245	Human butyrylcholinesterase (hBChE) hydrolyzes or scavenges a wide range of toxic esters, including heroin, cocaine, carbamate pesticides, organophosphorus pesticides, and nerve agents.
18975951	1	2	theme	toxic	156:160	arg1	cocaine					188:194	cocaine	188:194	cocaine	188:194	Human butyrylcholinesterase (hBChE) hydrolyzes or scavenges a wide range of toxic esters, including heroin, cocaine, carbamate pesticides, organophosphorus pesticides, and nerve agents.
18975951	1	2	theme	toxic	156:160	arg1	esters					162:167	toxic esters	156:167	toxic esters	156:167	Human butyrylcholinesterase (hBChE) hydrolyzes or scavenges a wide range of toxic esters, including heroin, cocaine, carbamate pesticides, organophosphorus pesticides, and nerve agents.
18975951	1	2	theme	toxic	156:160	arg1	pesticides					207:216	carbamate pesticides	197:216	carbamate pesticides	197:216	Human butyrylcholinesterase (hBChE) hydrolyzes or scavenges a wide range of toxic esters, including heroin, cocaine, carbamate pesticides, organophosphorus pesticides, and nerve agents.
18975951	1	2	theme	toxic	156:160	arg1	agents					258:263	nerve agents	252:263	nerve agents	252:263	Human butyrylcholinesterase (hBChE) hydrolyzes or scavenges a wide range of toxic esters, including heroin, cocaine, carbamate pesticides, organophosphorus pesticides, and nerve agents.
18975951	10	3	theme	hBChE	1523:1527	arg1	analysis					1486:1493	Mass spectrometric analysis	1467:1493	Mass spectrometric analysis of the aged tabun-inhibited hBChE	1467:1527	Mass spectrometric analysis of the aged tabun-inhibited hBChE showed that both the dimethylamine and ethoxy side chains were missing from the phosphorus.
18975951	13	4	theme	reported	1829:1836	arg1	data					1841:1844	The reported 3D data	1825:1844	The reported 3D data	1825:1844	The reported 3D data will help in the design of new oximes capable of reactivating tabun-ChE conjugates.
18975951	8	5	theme	aging	1249:1253	arg1	reaction					1255:1262	the aging reaction	1245:1262	the aging reaction	1245:1262	The refined structures of aged ChE conjugates clearly show that the aging reaction proceeds through O-dealkylation of the P(R) enantiomer of tabun.
18975951	1	6	theme	esters	162:167	arg1	heroin					180:185	heroin	180:185	heroin	180:185	Human butyrylcholinesterase (hBChE) hydrolyzes or scavenges a wide range of toxic esters, including heroin, cocaine, carbamate pesticides, organophosphorus pesticides, and nerve agents.
18975951	1	6	theme	esters	162:167	arg1	range					147:151	a wide range	140:151	a wide range of toxic esters, including heroin, cocaine, carbamate pesticides, organophosphorus pesticides, and nerve agents	140:263	Human butyrylcholinesterase (hBChE) hydrolyzes or scavenges a wide range of toxic esters, including heroin, cocaine, carbamate pesticides, organophosphorus pesticides, and nerve agents.
18975951	1	6	theme	esters	162:167	arg1	pesticides					236:245	organophosphorus pesticides	219:245	organophosphorus pesticides	219:245	Human butyrylcholinesterase (hBChE) hydrolyzes or scavenges a wide range of toxic esters, including heroin, cocaine, carbamate pesticides, organophosphorus pesticides, and nerve agents.
18975951	1	6	theme	esters	162:167	arg1	cocaine					188:194	cocaine	188:194	cocaine	188:194	Human butyrylcholinesterase (hBChE) hydrolyzes or scavenges a wide range of toxic esters, including heroin, cocaine, carbamate pesticides, organophosphorus pesticides, and nerve agents.
18975951	1	6	theme	esters	162:167	arg1	pesticides					207:216	carbamate pesticides	197:216	carbamate pesticides	197:216	Human butyrylcholinesterase (hBChE) hydrolyzes or scavenges a wide range of toxic esters, including heroin, cocaine, carbamate pesticides, organophosphorus pesticides, and nerve agents.
18975951	1	6	theme	esters	162:167	arg1	agents					258:263	nerve agents	252:263	nerve agents	252:263	Human butyrylcholinesterase (hBChE) hydrolyzes or scavenges a wide range of toxic esters, including heroin, cocaine, carbamate pesticides, organophosphorus pesticides, and nerve agents.
18975951	13	7	theme	capable	1884:1890	arg1	oximes					1877:1882	new oximes	1873:1882	new oximes capable of reactivating tabun-ChE conjugates	1873:1927	The reported 3D data will help in the design of new oximes capable of reactivating tabun-ChE conjugates.
18975951	1	8	theme	nerve	252:256	arg1	agents					258:263	nerve agents	252:263	nerve agents	252:263	Human butyrylcholinesterase (hBChE) hydrolyzes or scavenges a wide range of toxic esters, including heroin, cocaine, carbamate pesticides, organophosphorus pesticides, and nerve agents.
18975951	10	9	theme	side	1575:1578	arg1	chains					1580:1585	the dimethylamine and ethoxy side chains	1546:1585	chains	1580:1585	Mass spectrometric analysis of the aged tabun-inhibited hBChE showed that both the dimethylamine and ethoxy side chains were missing from the phosphorus.
18975951	6	10	theme	crystal	924:930	arg1	structures					932:941	the crystal structures	920:941	the crystal structures of the non-aged and aged forms of hBChE inhibited by tabun, and by updating the refinement of non-aged and aged tabun-inhibited mouse AChE (mAChE)	920:1088	We investigated the structural basis of oxime resistance for phosphoramidated ChE conjugates by determining the crystal structures of the non-aged and aged forms of hBChE inhibited by tabun, and by updating the refinement of non-aged and aged tabun-inhibited mouse AChE (mAChE).
18975951	7	11	theme	non-aged	1106:1113	arg1	tabun-hBChE					1124:1134	non-aged and aged tabun-hBChE	1106:1134	non-aged and aged tabun-hBChE	1106:1134	Structures for non-aged and aged tabun-hBChE were refined to 2.3 and 2.1 A, respectively.
18975951	3	12	theme	OP-ChE	527:532	arg1	conjugate					534:542	the OP-ChE conjugate	523:542	the OP-ChE conjugate	523:542	Phosphylated cholinesterase (ChE) can undergo a spontaneous, time-dependent process called "aging", during which the OP-ChE conjugate is dealkylated.
18975951	9	13	theme	salt	1394:1397	arg1	bridge					1399:1404	a strong salt bridge	1385:1404	a strong salt bridge with protonated His438N epsilon2 that prevents reactivation	1385:1464	After dealkylation, the negatively charged oxygen forms a strong salt bridge with protonated His438N epsilon2 that prevents reactivation.
18975951	5	14	theme	tabun-ChE	715:723	arg1	conjugates					725:734	tabun-ChE conjugates	715:734	tabun-ChE conjugates	715:734	The inhibition of ChEs by tabun and the subsequent aging reaction are of particular interest, because tabun-ChE conjugates display an extraordinary resistance toward most current oxime reactivators.
18975951	10	15	from	phosphorus	1609:1618	arg1	missing					1592:1598	missing	1592:1598	missing	1592:1598	Mass spectrometric analysis of the aged tabun-inhibited hBChE showed that both the dimethylamine and ethoxy side chains were missing from the phosphorus.
18975951	10	15	from	phosphorus	1609:1618	arg1	dimethylamine					1550:1562	the dimethylamine and ethoxy side chains	1546:1585	dimethylamine	1550:1562	Mass spectrometric analysis of the aged tabun-inhibited hBChE showed that both the dimethylamine and ethoxy side chains were missing from the phosphorus.
18975951	8	16	theme	enantiomer	1308:1317	arg1	O-dealkylation					1281:1294	O-dealkylation	1281:1294	O-dealkylation of the P(R) enantiomer of tabun	1281:1326	The refined structures of aged ChE conjugates clearly show that the aging reaction proceeds through O-dealkylation of the P(R) enantiomer of tabun.
18975951	3	17	theme	aging	502:506	arg1	"					507:507	aging"	502:507	aging"	502:507	Phosphylated cholinesterase (ChE) can undergo a spontaneous, time-dependent process called "aging", during which the OP-ChE conjugate is dealkylated.
18975951	4	18	theme	irreversible	574:585	arg1	inhibition					587:596	irreversible inhibition	574:596	irreversible inhibition of the enzyme	574:610	This leads to irreversible inhibition of the enzyme.
18975951	11	19	theme	crystallography	1663:1677	arg1	results					1679:1685	the crystallography results	1659:1685	the crystallography results	1659:1685	Loss of the ethoxy is consistent with the crystallography results.
18975951	13	20	theme	oximes	1877:1882	arg1	design					1863:1868	the design	1859:1868	the design of new oximes capable of reactivating tabun-ChE conjugates	1859:1927	The reported 3D data will help in the design of new oximes capable of reactivating tabun-ChE conjugates.
18975951	1	21	theme	Human	80:84	arg1	hBChE					109:113	hBChE	109:113	hBChE	109:113	Human butyrylcholinesterase (hBChE) hydrolyzes or scavenges a wide range of toxic esters, including heroin, cocaine, carbamate pesticides, organophosphorus pesticides, and nerve agents.
18975951	1	21	theme	Human	80:84	arg1	butyrylcholinesterase					86:106	Human butyrylcholinesterase	80:106	Human butyrylcholinesterase (hBChE)	80:114	Human butyrylcholinesterase (hBChE) hydrolyzes or scavenges a wide range of toxic esters, including heroin, cocaine, carbamate pesticides, organophosphorus pesticides, and nerve agents.
18975951	9	22	theme	His438N	1422:1428	arg1	epsilon2					1430:1437	protonated His438N epsilon2	1411:1437	protonated His438N epsilon2	1411:1437	After dealkylation, the negatively charged oxygen forms a strong salt bridge with protonated His438N epsilon2 that prevents reactivation.
18975951	2	23	theme	catalytic	392:400	arg1	serine					402:407	the catalytic serine	388:407	the catalytic serine	388:407	Organophosphates (OPs) exert their acute toxicity through inhibition of acetylcholinesterase (AChE) by phosphorylation of the catalytic serine.
18975951	5	24	theme	most	779:782	arg1	reactivators					798:809	most current oxime reactivators	779:809	most current oxime reactivators	779:809	The inhibition of ChEs by tabun and the subsequent aging reaction are of particular interest, because tabun-ChE conjugates display an extraordinary resistance toward most current oxime reactivators.
18975951	10	25	theme	Mass	1467:1470	arg1	analysis					1486:1493	Mass spectrometric analysis	1467:1493	Mass spectrometric analysis of the aged tabun-inhibited hBChE	1467:1527	Mass spectrometric analysis of the aged tabun-inhibited hBChE showed that both the dimethylamine and ethoxy side chains were missing from the phosphorus.
18975951	8	26	theme	tabun	1322:1326	arg1	enantiomer					1308:1317	the P(R) enantiomer	1299:1317	the P(R) enantiomer of tabun	1299:1326	The refined structures of aged ChE conjugates clearly show that the aging reaction proceeds through O-dealkylation of the P(R) enantiomer of tabun.
18975951	8	27	theme	conjugates	1216:1225	arg1	structures					1193:1202	The refined structures	1181:1202	The refined structures of aged ChE conjugates	1181:1225	The refined structures of aged ChE conjugates clearly show that the aging reaction proceeds through O-dealkylation of the P(R) enantiomer of tabun.
18975951	10	28	theme	ethoxy	1568:1573	arg1	chains					1580:1585	the dimethylamine and ethoxy side chains	1546:1585	chains	1580:1585	Mass spectrometric analysis of the aged tabun-inhibited hBChE showed that both the dimethylamine and ethoxy side chains were missing from the phosphorus.
18975951	10	29	theme	tabun-inhibited	1507:1521	arg1	hBChE					1523:1527	the aged tabun-inhibited hBChE	1498:1527	the aged tabun-inhibited hBChE	1498:1527	Mass spectrometric analysis of the aged tabun-inhibited hBChE showed that both the dimethylamine and ethoxy side chains were missing from the phosphorus.
18975951	6	30	theme	AChE	1077:1080	arg1	refinement					1023:1032	the refinement	1019:1032	the refinement of non-aged and aged tabun-inhibited mouse AChE (mAChE)	1019:1088	We investigated the structural basis of oxime resistance for phosphoramidated ChE conjugates by determining the crystal structures of the non-aged and aged forms of hBChE inhibited by tabun, and by updating the refinement of non-aged and aged tabun-inhibited mouse AChE (mAChE).
18975951	6	30	theme	AChE	1077:1080	arg1	updating					1010:1017	updating	1010:1017	updating	1010:1017	We investigated the structural basis of oxime resistance for phosphoramidated ChE conjugates by determining the crystal structures of the non-aged and aged forms of hBChE inhibited by tabun, and by updating the refinement of non-aged and aged tabun-inhibited mouse AChE (mAChE).
18975951	5	31	theme	ChEs	631:634	arg1	reaction					670:677	the subsequent aging reaction	649:677	the subsequent aging reaction	649:677	The inhibition of ChEs by tabun and the subsequent aging reaction are of particular interest, because tabun-ChE conjugates display an extraordinary resistance toward most current oxime reactivators.
18975951	5	31	theme	ChEs	631:634	arg1	inhibition					617:626	The inhibition	613:626	The inhibition of ChEs by tabun	613:643	The inhibition of ChEs by tabun and the subsequent aging reaction are of particular interest, because tabun-ChE conjugates display an extraordinary resistance toward most current oxime reactivators.
18975951	2	32	theme	acute	301:305	arg1	toxicity					307:314	their acute toxicity	295:314	their acute toxicity	295:314	Organophosphates (OPs) exert their acute toxicity through inhibition of acetylcholinesterase (AChE) by phosphorylation of the catalytic serine.
18975951	13	33	theme	3D	1838:1839	arg1	data					1841:1844	The reported 3D data	1825:1844	The reported 3D data	1825:1844	The reported 3D data will help in the design of new oximes capable of reactivating tabun-ChE conjugates.
18975951	6	34	theme	mouse	1071:1075	arg1	AChE					1077:1080	tabun-inhibited mouse AChE	1055:1080	non-aged and aged tabun-inhibited mouse AChE (mAChE)	1037:1088	We investigated the structural basis of oxime resistance for phosphoramidated ChE conjugates by determining the crystal structures of the non-aged and aged forms of hBChE inhibited by tabun, and by updating the refinement of non-aged and aged tabun-inhibited mouse AChE (mAChE).
18975951	6	34	theme	mouse	1071:1075	arg1	mAChE					1083:1087	mAChE	1083:1087	mAChE	1083:1087	We investigated the structural basis of oxime resistance for phosphoramidated ChE conjugates by determining the crystal structures of the non-aged and aged forms of hBChE inhibited by tabun, and by updating the refinement of non-aged and aged tabun-inhibited mouse AChE (mAChE).
18975951	8	35	theme	refined	1185:1191	arg1	structures					1193:1202	The refined structures	1181:1202	The refined structures of aged ChE conjugates	1181:1225	The refined structures of aged ChE conjugates clearly show that the aging reaction proceeds through O-dealkylation of the P(R) enantiomer of tabun.
18975951	3	36	theme	spontaneous	458:468	arg1	process					486:492	a spontaneous, time-dependent process	456:492	a spontaneous, time-dependent process	456:492	Phosphylated cholinesterase (ChE) can undergo a spontaneous, time-dependent process called "aging", during which the OP-ChE conjugate is dealkylated.
18975951	0	37	theme	cholinesterases	9:23	arg1	Aging					0:4	Aging	0:4	Aging of cholinesterases phosphylated by tabun	0:45	Aging of cholinesterases phosphylated by tabun proceeds through O-dealkylation.
18975951	6	38	theme	hBChE	977:981	arg1	forms					968:972	the non-aged and aged forms	946:972	the non-aged and aged forms of hBChE inhibited by tabun, and by updating the refinement of non-aged and aged tabun-inhibited mouse AChE (mAChE)	946:1088	We investigated the structural basis of oxime resistance for phosphoramidated ChE conjugates by determining the crystal structures of the non-aged and aged forms of hBChE inhibited by tabun, and by updating the refinement of non-aged and aged tabun-inhibited mouse AChE (mAChE).
18975951	5	39	theme	particular	686:695	arg1	interest					697:704	particular interest	686:704	particular interest	686:704	The inhibition of ChEs by tabun and the subsequent aging reaction are of particular interest, because tabun-ChE conjugates display an extraordinary resistance toward most current oxime reactivators.
18975951	6	40	theme	ChE	890:892	arg1	conjugates					894:903	phosphoramidated ChE conjugates	873:903	phosphoramidated ChE conjugates	873:903	We investigated the structural basis of oxime resistance for phosphoramidated ChE conjugates by determining the crystal structures of the non-aged and aged forms of hBChE inhibited by tabun, and by updating the refinement of non-aged and aged tabun-inhibited mouse AChE (mAChE).
18975951	12	41	theme	acid-catalyzed	1733:1746	arg1	deamidation					1748:1758	acid-catalyzed deamidation	1733:1758	acid-catalyzed deamidation during the preparation of the aged adduct for mass spectrometry	1733:1822	Loss of the dimethylamine is consistent with acid-catalyzed deamidation during the preparation of the aged adduct for mass spectrometry.
18975951	6	42	theme	aged	1050:1053	arg1	AChE					1077:1080	tabun-inhibited mouse AChE	1055:1080	non-aged and aged tabun-inhibited mouse AChE (mAChE)	1037:1088	We investigated the structural basis of oxime resistance for phosphoramidated ChE conjugates by determining the crystal structures of the non-aged and aged forms of hBChE inhibited by tabun, and by updating the refinement of non-aged and aged tabun-inhibited mouse AChE (mAChE).
18975951	6	42	theme	aged	1050:1053	arg1	mAChE					1083:1087	mAChE	1083:1087	mAChE	1083:1087	We investigated the structural basis of oxime resistance for phosphoramidated ChE conjugates by determining the crystal structures of the non-aged and aged forms of hBChE inhibited by tabun, and by updating the refinement of non-aged and aged tabun-inhibited mouse AChE (mAChE).
18975951	3	43	theme	Phosphylated	410:421	arg1	ChE					439:441	ChE	439:441	ChE	439:441	Phosphylated cholinesterase (ChE) can undergo a spontaneous, time-dependent process called "aging", during which the OP-ChE conjugate is dealkylated.
18975951	3	43	theme	Phosphylated	410:421	arg1	cholinesterase					423:436	Phosphylated cholinesterase	410:436	Phosphylated cholinesterase (ChE)	410:442	Phosphylated cholinesterase (ChE) can undergo a spontaneous, time-dependent process called "aging", during which the OP-ChE conjugate is dealkylated.
18975951	10	44	theme	spectrometric	1472:1484	arg1	analysis					1486:1493	Mass spectrometric analysis	1467:1493	Mass spectrometric analysis of the aged tabun-inhibited hBChE	1467:1527	Mass spectrometric analysis of the aged tabun-inhibited hBChE showed that both the dimethylamine and ethoxy side chains were missing from the phosphorus.
18975951	6	45	theme	phosphoramidated	873:888	arg1	conjugates					894:903	phosphoramidated ChE conjugates	873:903	phosphoramidated ChE conjugates	873:903	We investigated the structural basis of oxime resistance for phosphoramidated ChE conjugates by determining the crystal structures of the non-aged and aged forms of hBChE inhibited by tabun, and by updating the refinement of non-aged and aged tabun-inhibited mouse AChE (mAChE).
18975951	1	46	theme	carbamate	197:205	arg1	pesticides					207:216	carbamate pesticides	197:216	carbamate pesticides	197:216	Human butyrylcholinesterase (hBChE) hydrolyzes or scavenges a wide range of toxic esters, including heroin, cocaine, carbamate pesticides, organophosphorus pesticides, and nerve agents.
18975951	5	47	theme	current	784:790	arg1	reactivators					798:809	most current oxime reactivators	779:809	most current oxime reactivators	779:809	The inhibition of ChEs by tabun and the subsequent aging reaction are of particular interest, because tabun-ChE conjugates display an extraordinary resistance toward most current oxime reactivators.
18975951	6	48	theme	forms	968:972	arg1	structures					932:941	the crystal structures	920:941	the crystal structures of the non-aged and aged forms of hBChE inhibited by tabun, and by updating the refinement of non-aged and aged tabun-inhibited mouse AChE (mAChE)	920:1088	We investigated the structural basis of oxime resistance for phosphoramidated ChE conjugates by determining the crystal structures of the non-aged and aged forms of hBChE inhibited by tabun, and by updating the refinement of non-aged and aged tabun-inhibited mouse AChE (mAChE).
18975951	9	49	theme	strong	1387:1392	arg1	bridge					1399:1404	a strong salt bridge	1385:1404	a strong salt bridge with protonated His438N epsilon2 that prevents reactivation	1385:1464	After dealkylation, the negatively charged oxygen forms a strong salt bridge with protonated His438N epsilon2 that prevents reactivation.
18975951	2	50	theme	serine	402:407	arg1	phosphorylation					369:383	phosphorylation	369:383	phosphorylation of the catalytic serine	369:407	Organophosphates (OPs) exert their acute toxicity through inhibition of acetylcholinesterase (AChE) by phosphorylation of the catalytic serine.
18975951	5	51	theme	oxime	792:796	arg1	reactivators					798:809	most current oxime reactivators	779:809	most current oxime reactivators	779:809	The inhibition of ChEs by tabun and the subsequent aging reaction are of particular interest, because tabun-ChE conjugates display an extraordinary resistance toward most current oxime reactivators.
18975951	6	52	theme	aged	963:966	arg1	forms					968:972	the non-aged and aged forms	946:972	the non-aged and aged forms of hBChE inhibited by tabun, and by updating the refinement of non-aged and aged tabun-inhibited mouse AChE (mAChE)	946:1088	We investigated the structural basis of oxime resistance for phosphoramidated ChE conjugates by determining the crystal structures of the non-aged and aged forms of hBChE inhibited by tabun, and by updating the refinement of non-aged and aged tabun-inhibited mouse AChE (mAChE).
18975951	5	53	theme	subsequent	653:662	arg1	reaction					670:677	the subsequent aging reaction	649:677	the subsequent aging reaction	649:677	The inhibition of ChEs by tabun and the subsequent aging reaction are of particular interest, because tabun-ChE conjugates display an extraordinary resistance toward most current oxime reactivators.
18975951	6	54	theme	resistance	858:867	arg1	basis					843:847	the structural basis	828:847	the structural basis of oxime resistance for phosphoramidated ChE conjugates	828:903	We investigated the structural basis of oxime resistance for phosphoramidated ChE conjugates by determining the crystal structures of the non-aged and aged forms of hBChE inhibited by tabun, and by updating the refinement of non-aged and aged tabun-inhibited mouse AChE (mAChE).
18975951	9	55	with	bridge	1399:1404	arg1	epsilon2					1430:1437	protonated His438N epsilon2	1411:1437	protonated His438N epsilon2	1411:1437	After dealkylation, the negatively charged oxygen forms a strong salt bridge with protonated His438N epsilon2 that prevents reactivation.
18975951	2	56	theme	acetylcholinesterase	338:357	arg1	inhibition					324:333	inhibition	324:333	inhibition of acetylcholinesterase (AChE) by phosphorylation of the catalytic serine	324:407	Organophosphates (OPs) exert their acute toxicity through inhibition of acetylcholinesterase (AChE) by phosphorylation of the catalytic serine.
18975951	8	57	theme	aged	1207:1210	arg1	conjugates					1216:1225	aged ChE conjugates	1207:1225	aged ChE conjugates	1207:1225	The refined structures of aged ChE conjugates clearly show that the aging reaction proceeds through O-dealkylation of the P(R) enantiomer of tabun.
18975951	5	58	theme	aging	664:668	arg1	reaction					670:677	the subsequent aging reaction	649:677	the subsequent aging reaction	649:677	The inhibition of ChEs by tabun and the subsequent aging reaction are of particular interest, because tabun-ChE conjugates display an extraordinary resistance toward most current oxime reactivators.
18975951	6	59	theme	oxime	852:856	arg1	resistance					858:867	oxime resistance	852:867	oxime resistance	852:867	We investigated the structural basis of oxime resistance for phosphoramidated ChE conjugates by determining the crystal structures of the non-aged and aged forms of hBChE inhibited by tabun, and by updating the refinement of non-aged and aged tabun-inhibited mouse AChE (mAChE).
18975951	11	60	with	consistent	1643:1652	arg1	results					1679:1685	the crystallography results	1659:1685	the crystallography results	1659:1685	Loss of the ethoxy is consistent with the crystallography results.
18975951	6	61	theme	non-aged	950:957	arg1	forms					968:972	the non-aged and aged forms	946:972	the non-aged and aged forms of hBChE inhibited by tabun, and by updating the refinement of non-aged and aged tabun-inhibited mouse AChE (mAChE)	946:1088	We investigated the structural basis of oxime resistance for phosphoramidated ChE conjugates by determining the crystal structures of the non-aged and aged forms of hBChE inhibited by tabun, and by updating the refinement of non-aged and aged tabun-inhibited mouse AChE (mAChE).
18975951	10	62	theme	aged	1502:1505	arg1	hBChE					1523:1527	the aged tabun-inhibited hBChE	1498:1527	the aged tabun-inhibited hBChE	1498:1527	Mass spectrometric analysis of the aged tabun-inhibited hBChE showed that both the dimethylamine and ethoxy side chains were missing from the phosphorus.
18975951	12	63	theme	dimethylamine	1700:1712	arg1	Loss					1688:1691	Loss	1688:1691	Loss of the dimethylamine	1688:1712	Loss of the dimethylamine is consistent with acid-catalyzed deamidation during the preparation of the aged adduct for mass spectrometry.
18975951	13	64	theme	tabun-ChE	1908:1916	arg1	conjugates					1918:1927	tabun-ChE conjugates	1908:1927	tabun-ChE conjugates	1908:1927	The reported 3D data will help in the design of new oximes capable of reactivating tabun-ChE conjugates.
18975951	12	65	with	consistent	1717:1726	arg1	deamidation					1748:1758	acid-catalyzed deamidation	1733:1758	acid-catalyzed deamidation during the preparation of the aged adduct for mass spectrometry	1733:1822	Loss of the dimethylamine is consistent with acid-catalyzed deamidation during the preparation of the aged adduct for mass spectrometry.
18975951	12	66	theme	adduct	1795:1800	arg1	preparation					1771:1781	the preparation	1767:1781	the preparation of the aged adduct for mass spectrometry	1767:1822	Loss of the dimethylamine is consistent with acid-catalyzed deamidation during the preparation of the aged adduct for mass spectrometry.
18975951	1	67	theme	wide	142:145	arg1	heroin					180:185	heroin	180:185	heroin	180:185	Human butyrylcholinesterase (hBChE) hydrolyzes or scavenges a wide range of toxic esters, including heroin, cocaine, carbamate pesticides, organophosphorus pesticides, and nerve agents.
18975951	1	67	theme	wide	142:145	arg1	range					147:151	a wide range	140:151	a wide range of toxic esters, including heroin, cocaine, carbamate pesticides, organophosphorus pesticides, and nerve agents	140:263	Human butyrylcholinesterase (hBChE) hydrolyzes or scavenges a wide range of toxic esters, including heroin, cocaine, carbamate pesticides, organophosphorus pesticides, and nerve agents.
18975951	1	67	theme	wide	142:145	arg1	pesticides					236:245	organophosphorus pesticides	219:245	organophosphorus pesticides	219:245	Human butyrylcholinesterase (hBChE) hydrolyzes or scavenges a wide range of toxic esters, including heroin, cocaine, carbamate pesticides, organophosphorus pesticides, and nerve agents.
18975951	1	67	theme	wide	142:145	arg1	cocaine					188:194	cocaine	188:194	cocaine	188:194	Human butyrylcholinesterase (hBChE) hydrolyzes or scavenges a wide range of toxic esters, including heroin, cocaine, carbamate pesticides, organophosphorus pesticides, and nerve agents.
18975951	1	67	theme	wide	142:145	arg1	pesticides					207:216	carbamate pesticides	197:216	carbamate pesticides	197:216	Human butyrylcholinesterase (hBChE) hydrolyzes or scavenges a wide range of toxic esters, including heroin, cocaine, carbamate pesticides, organophosphorus pesticides, and nerve agents.
18975951	1	67	theme	wide	142:145	arg1	agents					258:263	nerve agents	252:263	nerve agents	252:263	Human butyrylcholinesterase (hBChE) hydrolyzes or scavenges a wide range of toxic esters, including heroin, cocaine, carbamate pesticides, organophosphorus pesticides, and nerve agents.
18975951	8	68	theme	ChE	1212:1214	arg1	conjugates					1216:1225	aged ChE conjugates	1207:1225	aged ChE conjugates	1207:1225	The refined structures of aged ChE conjugates clearly show that the aging reaction proceeds through O-dealkylation of the P(R) enantiomer of tabun.
18975951	1	69	theme	organophosphorus	219:234	arg1	pesticides					236:245	organophosphorus pesticides	219:245	organophosphorus pesticides	219:245	Human butyrylcholinesterase (hBChE) hydrolyzes or scavenges a wide range of toxic esters, including heroin, cocaine, carbamate pesticides, organophosphorus pesticides, and nerve agents.
18975951	12	70	theme	aged	1790:1793	arg1	adduct					1795:1800	the aged adduct	1786:1800	the aged adduct	1786:1800	Loss of the dimethylamine is consistent with acid-catalyzed deamidation during the preparation of the aged adduct for mass spectrometry.
18975951	6	71	theme	non-aged	1037:1044	arg1	AChE					1077:1080	tabun-inhibited mouse AChE	1055:1080	non-aged and aged tabun-inhibited mouse AChE (mAChE)	1037:1088	We investigated the structural basis of oxime resistance for phosphoramidated ChE conjugates by determining the crystal structures of the non-aged and aged forms of hBChE inhibited by tabun, and by updating the refinement of non-aged and aged tabun-inhibited mouse AChE (mAChE).
18975951	6	71	theme	non-aged	1037:1044	arg1	mAChE					1083:1087	mAChE	1083:1087	mAChE	1083:1087	We investigated the structural basis of oxime resistance for phosphoramidated ChE conjugates by determining the crystal structures of the non-aged and aged forms of hBChE inhibited by tabun, and by updating the refinement of non-aged and aged tabun-inhibited mouse AChE (mAChE).
18975951	3	72	dep	spontaneous	458:468	arg1	time-dependent					471:484	time-dependent	471:484	time-dependent	471:484	Phosphylated cholinesterase (ChE) can undergo a spontaneous, time-dependent process called "aging", during which the OP-ChE conjugate is dealkylated.
18975951	6	73	theme	tabun-inhibited	1055:1069	arg1	AChE					1077:1080	tabun-inhibited mouse AChE	1055:1080	non-aged and aged tabun-inhibited mouse AChE (mAChE)	1037:1088	We investigated the structural basis of oxime resistance for phosphoramidated ChE conjugates by determining the crystal structures of the non-aged and aged forms of hBChE inhibited by tabun, and by updating the refinement of non-aged and aged tabun-inhibited mouse AChE (mAChE).
18975951	6	73	theme	tabun-inhibited	1055:1069	arg1	mAChE					1083:1087	mAChE	1083:1087	mAChE	1083:1087	We investigated the structural basis of oxime resistance for phosphoramidated ChE conjugates by determining the crystal structures of the non-aged and aged forms of hBChE inhibited by tabun, and by updating the refinement of non-aged and aged tabun-inhibited mouse AChE (mAChE).
18975951	9	74	theme	protonated	1411:1420	arg1	epsilon2					1430:1437	protonated His438N epsilon2	1411:1437	protonated His438N epsilon2	1411:1437	After dealkylation, the negatively charged oxygen forms a strong salt bridge with protonated His438N epsilon2 that prevents reactivation.
18975951	6	75	theme	structural	832:841	arg1	basis					843:847	the structural basis	828:847	the structural basis of oxime resistance for phosphoramidated ChE conjugates	828:903	We investigated the structural basis of oxime resistance for phosphoramidated ChE conjugates by determining the crystal structures of the non-aged and aged forms of hBChE inhibited by tabun, and by updating the refinement of non-aged and aged tabun-inhibited mouse AChE (mAChE).
18975951	5	76	theme	extraordinary	747:759	arg1	resistance					761:770	an extraordinary resistance	744:770	an extraordinary resistance toward most current oxime reactivators	744:809	The inhibition of ChEs by tabun and the subsequent aging reaction are of particular interest, because tabun-ChE conjugates display an extraordinary resistance toward most current oxime reactivators.
18975951	11	77	theme	ethoxy	1633:1638	arg1	Loss					1621:1624	Loss	1621:1624	Loss of the ethoxy	1621:1638	Loss of the ethoxy is consistent with the crystallography results.
18975951	12	78	theme	mass	1806:1809	arg1	spectrometry					1811:1822	mass spectrometry	1806:1822	mass spectrometry	1806:1822	Loss of the dimethylamine is consistent with acid-catalyzed deamidation during the preparation of the aged adduct for mass spectrometry.
18975951	8	79	theme	P	1303:1303	arg1	enantiomer					1308:1317	the P(R) enantiomer	1299:1317	the P(R) enantiomer of tabun	1299:1326	The refined structures of aged ChE conjugates clearly show that the aging reaction proceeds through O-dealkylation of the P(R) enantiomer of tabun.
18975951	13	80	theme	new	1873:1875	arg1	oximes					1877:1882	new oximes	1873:1882	new oximes capable of reactivating tabun-ChE conjugates	1873:1927	The reported 3D data will help in the design of new oximes capable of reactivating tabun-ChE conjugates.
18975951	4	81	theme	enzyme	605:610	arg1	inhibition					587:596	irreversible inhibition	574:596	irreversible inhibition of the enzyme	574:610	This leads to irreversible inhibition of the enzyme.